[med-svn] [plip] 04/14: Imported Upstream version 1.3.0a+dfsg

Alex Mestiashvili malex-guest at moszumanska.debian.org
Thu Mar 24 16:43:52 UTC 2016


This is an automated email from the git hooks/post-receive script.

malex-guest pushed a commit to branch master
in repository plip.

commit 4279f15daa85d08a22a84cc4db8601557d6d993d
Author: Alexandre Mestiashvili <alex at biotec.tu-dresden.de>
Date:   Wed Mar 23 14:41:24 2016 +0100

    Imported Upstream version 1.3.0a+dfsg
---
 .gitignore                             |     1 +
 CHANGES.txt                            |    54 +-
 DOCUMENTATION.md                       |   224 +-
 README.md                              |     8 +-
 plip/__init__.py                       |    18 +-
 plip/modules/__init__.py               |    18 +-
 plip/modules/config.py                 |    44 +-
 plip/modules/detection.py              |   240 +-
 plip/modules/mp.py                     |    69 +
 plip/modules/preparation.py            |  1015 +-
 plip/modules/report.py                 |   210 +-
 plip/modules/supplemental.py           |   455 +-
 plip/modules/visualize.py              |   371 +-
 plip/plipcmd                           |   308 +-
 plip/test/pdb/1acj.pdb                 |  4774 ----
 plip/test/pdb/1aku.pdb                 |  1765 --
 plip/test/pdb/1ay8.pdb                 |  6838 ------
 plip/test/pdb/1bju.pdb                 |  2217 --
 plip/test/pdb/1bma.pdb                 |  2569 ---
 plip/test/pdb/1eve.pdb                 |  5376 -----
 plip/test/pdb/1h2t.pdb                 |  7978 -------
 plip/test/pdb/1hii.pdb                 |  2163 --
 plip/test/pdb/1hvi.pdb                 |  2409 --
 plip/test/pdb/1hwu.pdb                 |  5032 -----
 plip/test/pdb/1n7g.pdb                 | 12315 -----------
 plip/test/pdb/1osn.pdb                 | 11018 ----------
 plip/test/pdb/1p5e.pdb                 |  9844 ---------
 plip/test/pdb/1vsn.pdb                 |  2355 --
 plip/test/pdb/1xdn.pdb                 |  5703 -----
 plip/test/pdb/2efj.pdb                 |  3525 ---
 plip/test/pdb/2iuz.pdb                 |  8056 -------
 plip/test/pdb/2reg.pdb                 |  5374 -----
 plip/test/pdb/2w0s.pdb                 |  3928 ----
 plip/test/pdb/2zoz.pdb                 |  3856 ----
 plip/test/pdb/3o1h.pdb                 |  5090 -----
 plip/test/pdb/3og7.pdb                 |  8757 --------
 plip/test/pdb/3pxf.pdb                 |  3215 ---
 plip/test/pdb/3r0t.pdb                 |  6723 ------
 plip/test/pdb/3shy.pdb                 |  2872 ---
 plip/test/pdb/3tah.pdb                 |  5381 -----
 plip/test/pdb/3thy.pdb                 | 30958 --------------------------
 plip/test/pdb/4agl.pdb                 |  4509 ----
 plip/test/pdb/4alw.pdb                 |  3305 ---
 plip/test/pdb/4kya.pdb                 | 36156 -------------------------------
 plip/test/pdb/4pjt.pdb                 | 22489 -------------------
 plip/test/pdb/4qnb.pdb                 |  4070 ----
 plip/test/pdb/4rao.pdb                 | 14899 -------------
 plip/test/pdb/4rdl.pdb                 | 11637 ----------
 plip/test/test_basic_functions.py      |    60 +
 plip/test/test_literature_validated.py |   208 +-
 plip/test/test_metal_coordination.py   |   145 +
 plip/test/test_special_cases.py        |    13 +-
 setup.py                               |     6 +-
 53 files changed, 2576 insertions(+), 268047 deletions(-)

diff --git a/.gitignore b/.gitignore
index eccfef0..2516804 100644
--- a/.gitignore
+++ b/.gitignore
@@ -47,3 +47,4 @@ target/
 .idea/*
 # Other
 *~
+.nfs*
diff --git a/CHANGES.txt b/CHANGES.txt
index 146411e..a044023 100644
--- a/CHANGES.txt
+++ b/CHANGES.txt
@@ -1,6 +1,58 @@
 Changelog
 ---------
 
+### 1.3.0
+* __Batch processing__
+* Improvements to verbose mode and textual output
+
+### 1.2.3
+* __Better support for files from MD and docking software__
+* __Fixes issues with large and complex structures__
+* Speed optimizations
+
+
+### 1.2.2
+* __Option to consider alternate atom locations (e.g. for ligands with several conformations__
+* Automatic fixing of missing ligand names
+* Improved handling of broken PDB files and non-standard filenames
+* Improved error handling
+
+### 1.2.1
+* __Mapping of canonical atom order to PDB atom order for each ligand__
+* __Introduction of debug mode (--debug)__
+* More robust visualization
+* Handling of negative residue numbers for more cases
+* Composite members in alphabetical order
+* Fixes errors in aromatic ring detection
+* Code improvements
+
+### 1.2.0
+* __Support for DNA and RNA as ligands__
+* __Detection of metal complexes with proteins/ligands, including prediction of geometry__
+* __Extended result files with detailed information on binding site residues and unpaired atoms__
+*__Support for zipped and gzipped files__
+* Rich verbose mode in command line with information on detected functional groups and interactions
+* Automatic fixing of common errors in custom PDB files
+* Refined binding site selection
+* Better overall performance
+* Initial test suite for metal coordination
+* Classification of ligands
+* Improves detection of aromatic rings and interactions involving aromatic rings
+* Single nucleotides and ions not excluded anymore as ligands
+* Generation of canonical smiles for complete (composite) ligands
+* Generation of txt files is now optional
+* Basic support for PDBQT files
+* Correct handling of negative chain positions of ligands
+* Improved check for valid PDB IDs
+* Fixes several bugs
+
+
+
+### 1.1.1
+* __Detailed information on binding site residues in XML files__
+* Improved extraction of binding site residues
+* Information whether halogen bonds are made with side- or main chain of protein
+
 #### 1.1.0
 * __Folder structure and setup.py for automatic installation using pip__
 * __H-Bond Donor Prioritization (see documentation for details)__
@@ -35,4 +87,4 @@ Changelog
 * Fixed bug leading to duplicate interactions with quartamine groups
 
 #### 1.0.0
-* __Initial Release__
\ No newline at end of file
+* __Initial Release__
diff --git a/DOCUMENTATION.md b/DOCUMENTATION.md
index c659c42..7099037 100644
--- a/DOCUMENTATION.md
+++ b/DOCUMENTATION.md
@@ -1,20 +1,22 @@
-==================
-PLIProfiler v1.1.0
-==================
+===========
+PLIP v1.2.2
+===========
 
 The Protein-Ligand Interaction Profiler (PLIP) is a tool to analyze and visualize protein-ligand interactions in PDB files.
 
 
 Features
 ========
-* Detection of eight different types of noncovalent interactions
-* Automatic detection of relevant ligands in a PDB file
+* Detection of eight different types of noncovalent interactions, including metal complexes
+* Works for complexes of protein with small molecules, ions, polymers, or DNA/RNA (and all combinations)
+* Automatic detection and grouping of relevant ligands in a PDB file
+* Rich additional information on binding, e.g. unpaired functional groups
 * Direct download of PDB structures from wwPDB server if valid PDB ID is given
 * Processing of custom PDB files containing protein-ligand complexes (e.g. from docking)
 * No need for special preparation of a PDB file, works out of the box
-* Atom-level interaction reports in rST and XML formats for easy parsing
-* Generation of PyMOL session files (.pse) for each pairing, enabling easy preparation of images for publications and talks
-* Rendering of preview image for each ligand and its interactions with the protein
+* Atom-level interaction reports in TXT and XML formats for easy parsing
+* Generation of PyMOL session files (.pse), enabling easy preparation of images for publications and talks
+* Rendering of 3D interaction diagram for each ligand and its interactions with the protein
 
 Quickstart
 ==========
@@ -23,6 +25,12 @@ To analyze a protein-ligand complex from a Protein Data Bank entry -- e.g. 1vsn
     `plipcmd -i 1vsn`.
 To analyze a PDB file from your workstation, run
     `plipcmd -f path_to_pdbfile.pdb`.
+The output format(s) can be chosen freely, ranging from ...
+* XML report files (`-x`, highest level of detail)
+* Text report files (`-t`, medium level of detail)
+* PyMOL session files (`-y`)
+* Ray-traced images (`-p`)
+* Verbose output on command line (`-v`)
 
 Threshold settings
 ==================
@@ -53,7 +61,7 @@ Exit codes
 ----------
 1 : Unspecified Error
 2 : Empty PDB file as input
-3 : Invalid PDB ID
+3 : Invalid PDB ID (wrong format)
 4 : PDB file can't be read by OpenBabel (due to invalid input files)
 5 : PDB ID is valid, but wwPDB offers no file in PDB format for download.
 
@@ -62,73 +70,193 @@ Legend for PyMOL visualization
 All colors given as RGB values.
 <Description> - <RGB> - <PyMOL color> - <Representation>
 
-Structural Elements
-"""""""""""""""""""
+__Structural Elements__
+
+
 Protein - [43, 131, 186] - myblue (custom) - sticks
+
 Ligand - [253, 174, 97] - myorange (custom) - sticks
+
 Water - [191, 191, 255] - lightblue - nb_spheres
+
 Charge Center - [255, 255, 0] - yellow - spheres
+
 Aromatic Ring Center - [230, 230, 230] -  grey90 - spheres
 
-Interactions
-""""""""""""
+Ions - [255, 255, 128] - hotpink - spheres
+
+
+__Interactions__
+
+
 Hydrophobic Interaction - [128, 128, 128] - grey50 - dashed Line
+
 Hydrogen Bond - [0, 0, 255] - blue - solid Line
+
 Water Bridges - [191, 191, 255] - lightblue - solid Line
+
 pi-Stacking (parallel) - [0, 255, 0] - green - dashed Line
+
 pi-Stacking (perpendicular) - [140, 179, 102] - smudge - dashed Line
+
 pi-Cation Interaction - [255, 128, 0] - orange - dashed Line
+
 Halogen Bond - [64, 255, 191] - greencyan - solid Line
+
 Salt Bridge - [255, 255, 0] - yellow - dashed Line
 
-Output Files
-------------
-All output files contain information on non-covalent interactions between the protein and all relevant ligands in the PDB structure.
+Metal Complexation - [140, 64, 153] - violetpurple - dashed Line
+
+
+XML Report Documentation
+------------------------
+
+
+**report**
+
+Contains all binding site information
+
+
+**plipversion**
+
+Version of PLIP used for generating the output file
+
+**bindingsite**
+
+Information for one bindingsite. Has a unique ID and attribute `has_interactions`
+
+
+**identifiers**
+
+Ligand/bindingsite identifiers
+
+
+**longname**
+
+Long name of ligand, contains all het ids of ligands in one composite cluster
+
+
+**ligtype**
+
+Classification of ligand, can be SMALLMOLECULE/POLYMER/DNA/RNA/ION or combinations of the first four with ION
+
+
+**hetid**
+
+PDB hetero ID of the ligand
+
+
+**chain**
+
+Chain assigned to the ligand in the PDB file
+
+
+**position**
+Position in chain of the ligand in the PDB file
+
+**composite**
+
+Can be True or False depending on whether the ligand consists of several separate subunits or not
+
+
+**members**
+
+Lists the members of a composite ligand cluster
+
+
+**smiles**
+
+The SMILES string of the complete (composite) ligand
+
+
+**lig_properties**
+
+Additional information on the ligand, i.e. number of functional atoms
+
+
+**num_heavy_atoms**
+
+Number of heavy atoms in the ligand
+
+
+**num_hbd**
+
+Number of hydrogen bond donors in the ligand
+
+
+**num_unpaired_hbd**
+
+Number of unpaired hydrogen bond donors in the ligand (not involved as acceptor/donor in hydrogen bonds, salt bridges,
+water bridges, metal complexes)
+
+
+**num_hba**
+
+Number of hydrogen bond acceptors in the ligand
+
+
+**num_unpaired_hba**
+
+Number of unpaired hydrogen bond acceptors in the ligand (not involved as acceptor/donor in hydrogen bonds, salt bridges,
+water bridges, metal complexes)
+
+
+**num_hal**
+
+Number of halogen bond donors in the ligand
+
+
+**num_unpaired_hal**
+
+Number of unpaired halogen bond donors in the ligand
+
+
+**num_aromatic_rings**
+
+Number of aromatic rings in the ligand
+
+
+**interacting chains**
+
+Lists the chains the ligand interacts with
+
+
+**bs_residues**
+
+Listing of binding site residues the ligand is near to or interacts with. Contains the type of amino acid, information
+on contact, a unique id and the minimal distance to the ligand in Angstrom
+
+
+**interactions**
+
+Detailed information on all interactions (general attributes documented below)
+
+
+**resnr**
 
-XML/RST Result Files
-""""""""""""""""""""
+Residue number of interacting amino acid
 
-<pdbid>
-Unique identifier for the corresponding entry of the protein structure in Protein Data Bank.
 
-<hetid>
-Unique identifier for ligand molecule in Protein Data Bank (PDB).
+**restype**
 
-<chain>
-One protein can consist of multiple separate amino acids chains which are named alphabetically
+Residue type of interacting amino acid
 
-<position>
-Position of ligand in PDB numbering. Combination of pdbid, hetid, chain and position gives a unique identifier for
-each protein-ligand complex. Same numbering as <resnr>
 
-<interactions>
-Contains interaction for protein-ligand complex, organized by interaction type, e.g. hydrophobic interactions
+**reschain**
 
-<resnr>
-Position of amino acid in protein chain according to PDB numbering
+Residue chain of interacting amino acid
 
-<restype>
-Amino acid type in three-letter code
 
-<dist*>
-Distance of interacting atoms
+**dist**
 
-<*idx>
-Atom ID in original PDB structure
+Distance of interacting atoms or groups in Angstrom
 
-<lig_idx_list>
-Atom IDs if several ligand atoms are relevant for a single interaction (e.g. when forming a charge center)
 
-<*angle>
-Angle between interacting groups
+**ligcoo**
 
-<protispos>, <protisdon>, <protischarged>
-Determines if the protein is positively charged, provides a donor or a charge.
-Important for interactions with directionality.
+Coordinates of interacting ligand atom or interaction center in ligand
 
-<sidechain>
-Is true if a hydrogen bond is formed with the sidechain of the protein and false if it is formed with the backbone.
 
-<ligcoo>, <protcoo>
-Coordinates of protein and ligand interacting atoms or interaction centers (e.g. charge centers)
+**protcoo**
 
+Coordinates of interacting protein atom or interaction center in ligand
diff --git a/README.md b/README.md
index 3b16e82..fb8cb63 100644
--- a/README.md
+++ b/README.md
@@ -3,6 +3,10 @@ PLIP
 
 Protein-Ligand Interaction Profiler (PLIP) - Analyze non-covalent protein-ligand interactions in 3D structures
 
+Versions
+--------
+The latest commits may contain newer, but untested features. The last version marked as release is always stable.
+
 Installation
 ------------
 
@@ -19,7 +23,9 @@ To install PLIP, simply run the following command using a terminal
 Code Contributions
 ------------------
 Sebastian Salentin sebastian.salentin (at) biotec.tu-dresden.de
+
 Joachim Haupt joachim.haupt (at) biotec.tu-dresden.de
+
 Melissa F. Adasme Mora melissa.adasme (at) biotec.tu-dresden.de (Testing and Validation)
 
 PLIP Web Server
@@ -34,4 +40,4 @@ Citation Information
 --------------------
 If you are using PLIP in your work, please cite
 > Salentin,S. et al. PLIP: fully automated protein-ligand interaction profiler.
-> Nucl. Acids Res. first published online April 14, 2015 doi:10.1093/nar/gkv315
+> Nucl. Acids Res. (1 July 2015) 43 (W1): W443-W447. doi: 10.1093/nar/gkv315
diff --git a/plip/__init__.py b/plip/__init__.py
index e1cefcd..1ab663b 100644
--- a/plip/__init__.py
+++ b/plip/__init__.py
@@ -1 +1,17 @@
-__author__ = 'sebastians'
+"""
+Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
+__init__.py - Needed for python modules.
+Copyright 2014-2015 Sebastian Salentin
+
+Licensed under the Apache License, Version 2.0 (the "License");
+you may not use this file except in compliance with the License.
+You may obtain a copy of the License at
+
+    http://www.apache.org/licenses/LICENSE-2.0
+
+Unless required by applicable law or agreed to in writing, software
+distributed under the License is distributed on an "AS IS" BASIS,
+WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
+See the License for the specific language governing permissions and
+limitations under the License.
+"""
\ No newline at end of file
diff --git a/plip/modules/__init__.py b/plip/modules/__init__.py
index e1cefcd..1ab663b 100644
--- a/plip/modules/__init__.py
+++ b/plip/modules/__init__.py
@@ -1 +1,17 @@
-__author__ = 'sebastians'
+"""
+Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
+__init__.py - Needed for python modules.
+Copyright 2014-2015 Sebastian Salentin
+
+Licensed under the Apache License, Version 2.0 (the "License");
+you may not use this file except in compliance with the License.
+You may obtain a copy of the License at
+
+    http://www.apache.org/licenses/LICENSE-2.0
+
+Unless required by applicable law or agreed to in writing, software
+distributed under the License is distributed on an "AS IS" BASIS,
+WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
+See the License for the specific language governing permissions and
+limitations under the License.
+"""
\ No newline at end of file
diff --git a/plip/modules/config.py b/plip/modules/config.py
index 0e70af2..66a23ec 100644
--- a/plip/modules/config.py
+++ b/plip/modules/config.py
@@ -16,12 +16,24 @@ See the License for the specific language governing permissions and
 limitations under the License.
 """
 
+VERBOSE = False  # Set verbose mode
+DEBUG = False  # Set debug mode
+MAXTHREADS = 1  # Maximum number of main threads for binding site visualization
+XML = False
+TXT = False
+PICS = False
+PYMOL = False
+OUTPATH = './'
+BASEPATH = './'
+BREAKCOMPOSITE = False  # Break up composite ligands with covalent bonds
+ALTLOC = False  # Consider alternate locations
+
 # Configuration file for Protein-Ligand Interaction Profiler (PLIP)
 # Set thresholds for detection of interactions
 
 # Thresholds for detection (global variables)
-BS_DIST = 8.5  # Determines maximum distance to include binding site residues
-AROMATIC_PLANARITY = 7.5  # Determines allowed deviation from planarity in aromatic rings
+BS_DIST = 7.5  # Determines maximum distance to include binding site residues
+AROMATIC_PLANARITY = 5.0  # Determines allowed deviation from planarity in aromatic rings
 
 # Some distance thresholds were extended (max. 1.0A) if too restrictive too account for low-quality structures
 HYDROPH_DIST_MAX = 4.0  # Distance cutoff for detection of hydrophobic contacts
@@ -41,20 +53,27 @@ WATER_BRIDGE_MAXDIST = 4.0  # Max. distance between water oxygen and polar atom
 WATER_BRIDGE_OMEGA_MIN = 75  # Min. angle between acceptor, water oxygen and donor hydrogen (Jiang et al., 2005) - 5
 WATER_BRIDGE_OMEGA_MAX = 140  # Max. angle between acceptor, water oxygen and donor hydrogen (Jiang et al., 2005)
 WATER_BRIDGE_THETA_MIN = 100  # Min. angle between water oxygen, donor hydrogen and donor atom (Jiang et al., 2005)
+METAL_DIST_MAX = 3.0  # Max. distance between metal ion and interacting atom (Harding, 2001)
+
+#############
+# Whitelist #
+#############
+
+# Metal cations which can be complexed
+
+METAL_IONS = ['CA', 'CO', 'MG', 'MN', 'FE', 'CU', 'ZN', 'FE2', 'FE3', 'FE4', 'LI', 'NA', 'K', 'RB', 'SR', 'CS', 'BA',
+              'CR', 'NI', 'FE1', 'NI', 'RU', 'RU1', 'RH', 'RH1', 'PD', 'AG', 'CD', 'LA', 'W', 'W1', 'OS', 'IR', 'PT',
+              'PT1', 'AU', 'HG', 'CE', 'PR', 'SM', 'EU', 'GD', 'TB', 'YB', 'LU', 'AL', 'GA', 'IN', 'SB', 'TL', 'PB']
+
 
 ##############
 # Blacklists #
 ##############
 
-# DNA or RNA bases
-dna = ['A', 'C', 'T', 'G', 'U', 'DA', 'DC', 'DT', 'DG', 'DU']
-
-# Ions
-ions = ['LI', 'BE', 'NA', 'MG', 'K', 'CA', 'RB', 'SR', 'CS', 'BA', 'V', 'CR', 'MN', 'CO', 'NI', 'FE', 'FE1', 'CL',
-        'IOD', 'BR', 'FE2', 'FE3', 'FE4', 'CO', 'NI', 'CU', 'ZN', 'Y', 'ZR1', 'ZR2', 'ZR3', 'MO', 'RU', 'RU1', 'RH',
-        'RH1', 'PD', 'AG', 'CD', 'LA', 'HFA', 'HFB', 'HFC', 'HFD', 'HFE', 'TA1', 'TA2', 'TA3', 'TA4', 'TA5', 'TA6', 'W',
-        'W1', 'RE', 'OS', 'IR', 'PT', 'PT1', 'AU', 'HG', 'CE', 'PR', 'SM', 'EU', 'GD', 'TB', 'HO', 'ER', 'YB', 'LU',
-        'PA', 'U', 'AL', 'GA', 'GE', 'IN', 'SN1', 'SB', 'TL', 'PB']
+# Other Ions/Atoms (not yet supported)
+anions = ['CL', 'IOD', 'BR']
+other = ['MO', 'RE', 'HO']
+UNSUPPORTED = anions + other
 
 # BioLiP list of suspicious ligands from http://zhanglab.ccmb.med.umich.edu/BioLiP/ligand_list (2014-07-10)
 biolip_list = ['ACE', 'HEX', 'TMA', 'SOH', 'P25', 'CCN', 'PR', 'PTN', 'NO3', 'TCN', 'BU1', 'BCN', 'CB3', 'HCS', 'NBN',
@@ -88,6 +107,3 @@ biolip_list = ['ACE', 'HEX', 'TMA', 'SOH', 'P25', 'CCN', 'PR', 'PTN', 'NO3', 'TC
                'L2C', '4AG', 'B3H', '1EM', 'DDR', 'I42', 'CNS', 'PC7', 'HGP', 'PC8', 'HGX', 'LIO', 'PLD', 'PC2', 'PCF',
                'MC3', 'P1O', 'PLC', 'PC6', 'HSH', 'BXC', 'HSG', 'DPG', '2DP', 'POV', 'PCW', 'GVT', 'CE9', 'CXE', 'C10',
                'CE1', 'SPJ', 'SPZ', 'SPK', 'SPW', 'HT3', 'HTH', '2OP', '3NI', 'BO3', 'DET', 'D1D', 'SWE', 'SOG']
-
-
-
diff --git a/plip/modules/detection.py b/plip/modules/detection.py
index b2d751a..21cf11f 100644
--- a/plip/modules/detection.py
+++ b/plip/modules/detection.py
@@ -1,7 +1,7 @@
 """
 Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
 detection.py - Detect non-covalent interactions.
-Copyright 2014 Sebastian Salentin
+Copyright 2014-2015 Sebastian Salentin
 
 Licensed under the Apache License, Version 2.0 (the "License");
 you may not use this file except in compliance with the License.
@@ -18,6 +18,7 @@ limitations under the License.
 
 # Python standard library
 import itertools
+from collections import defaultdict
 
 # Own modules
 from supplemental import *
@@ -32,13 +33,15 @@ def hydrophobic_interactions(atom_set_a, atom_set_b):
     """Detection of hydrophobic pliprofiler between atom_set_a (binding site) and atom_set_b (ligand).
     Definition: All pairs of qualified carbon atoms within a distance of HYDROPH_DIST_MAX
     """
-    data = namedtuple('hydroph_interaction', 'bsatom ligatom distance restype resnr reschain')
+    data = namedtuple('hydroph_interaction', 'bsatom bsatom_orig_idx ligatom ligatom_orig_idx '
+                                             'distance restype resnr reschain')
     pairings = []
-    for a, b in itertools.product(atom_set_a.atoms, atom_set_b.atoms):
-        e = euclidean3d(a.coords, b.coords)
+    for a, b in itertools.product(atom_set_a, atom_set_b):
+        e = euclidean3d(a.atom.coords, b.atom.coords)
         if e < config.HYDROPH_DIST_MAX:
-            contact = data(bsatom=a, ligatom=b, distance=e, restype=whichrestype(a),
-                           resnr=whichresnumber(a), reschain=whichchain(a))
+            contact = data(bsatom=a.atom, bsatom_orig_idx=a.orig_idx, ligatom=b.atom, ligatom_orig_idx=b.orig_idx,
+                           distance=e, restype=whichrestype(a.atom), resnr=whichresnumber(a.atom),
+                           reschain=whichchain(a.atom))
             pairings.append(contact)
     return pairings
 
@@ -49,7 +52,8 @@ def hbonds(acceptors, donor_pairs, protisdon, typ):
     donor hydrogens and acceptor showing a distance within HBOND DIST MIN and HBOND DIST MAX
     and donor angles above HBOND_DON_ANGLE_MIN
     """
-    data = namedtuple('hbond', 'a d h distance_ah distance_ad angle type protisdon resnr restype reschain sidechain atype dtype')
+    data = namedtuple('hbond', 'a a_orig_idx d d_orig_idx h distance_ah distance_ad angle type protisdon resnr '
+                               'restype reschain sidechain atype dtype')
     pairings = []
     for acc, don in itertools.product(acceptors, donor_pairs):
         if typ == 'strong':  # Regular (strong) hydrogen bonds
@@ -64,9 +68,10 @@ def hbonds(acceptors, donor_pairs, protisdon, typ):
                     protatom = don.d.OBAtom if protisdon else acc.a.OBAtom
                     is_sidechain_hbond = protatom.GetResidue().GetAtomProperty(protatom, 8)  # Check if sidechain atom
                     resnr = whichresnumber(don.d)if protisdon else whichresnumber(acc.a)
-                    contact = data(a=acc.a, d=don.d, h=don.h, distance_ah=dist_ah, distance_ad=dist_ad, angle=v,
-                                   type=typ, protisdon=protisdon, resnr=resnr, restype=restype, reschain=reschain,
-                                   sidechain=is_sidechain_hbond, atype=acc.a.type, dtype=don.d.type)
+                    contact = data(a=acc.a, a_orig_idx=acc.a_orig_idx, d=don.d, d_orig_idx=don.d_orig_idx, h=don.h,
+                                   distance_ah=dist_ah, distance_ad=dist_ad, angle=v, type=typ, protisdon=protisdon,
+                                   resnr=resnr, restype=restype, reschain=reschain, sidechain=is_sidechain_hbond,
+                                   atype=acc.a.type, dtype=don.d.type)
                     pairings.append(contact)
     return pairings
 
@@ -79,7 +84,7 @@ def pistacking(rings_bs, rings_lig):
         # DISTANCE AND RING ANGLE CALCULATION
         d = euclidean3d(r.center, l.center)
         b = vecangle(r.normal, l.normal)
-        a = min(b, 180-b if not 180-b < 0 else b)  # Smallest of two angles, depending on direction of normal
+        a = min(b, 180 - b if not 180 - b < 0 else b)  # Smallest of two angles, depending on direction of normal
 
         # RING CENTER OFFSET CALCULATION (project each ring center into the other ring)
         proj1 = projection(l.normal, l.center, r.center)
@@ -95,11 +100,10 @@ def pistacking(rings_bs, rings_lig):
                 contact = data(proteinring=r, ligandring=l, distance=d, angle=a, offset=offset,
                                type='P', resnr=resnr, restype=restype, reschain=reschain)
                 pairings.append(contact)
-            if 90-config.PISTACK_ANG_DEV < a < 90+config.PISTACK_ANG_DEV and offset < config.PISTACK_OFFSET_MAX:
+            if 90 - config.PISTACK_ANG_DEV < a < 90 + config.PISTACK_ANG_DEV and offset < config.PISTACK_OFFSET_MAX:
                 contact = data(proteinring=r, ligandring=l, distance=d, angle=a, offset=offset,
                                type='T', resnr=resnr, restype=restype, reschain=reschain)
                 pairings.append(contact)
-
     return pairings
 
 
@@ -127,7 +131,7 @@ def pication(rings, pos_charged, protcharged):
                                                 vector(n_atoms_coords[2], n_atoms_coords[0]))
                         b = vecangle(ring.normal, amine_normal)
                         # Smallest of two angles, depending on direction of normal
-                        a = min(b, 180-b if not 180-b < 0 else b)
+                        a = min(b, 180 - b if not 180 - b < 0 else b)
                         if not a > 30.0:
                             resnr, restype = whichresnumber(ring.atoms[0]), whichrestype(ring.atoms[0])
                             reschain = whichchain(ring.atoms[0])
@@ -161,7 +165,8 @@ def saltbridge(poscenter, negcenter, protispos):
 
 def halogen(acceptor, donor):
     """Detect all halogen bonds of the type Y-O...X-C"""
-    data = namedtuple('halogenbond', 'acc don distance don_angle acc_angle restype resnr reschain donortype acctype')
+    data = namedtuple('halogenbond', 'acc acc_orig_idx don don_orig_idx distance don_angle acc_angle restype '
+                                     'resnr reschain donortype acctype sidechain')
     pairings = []
     for acc, don in itertools.product(acceptor, donor):
         dist = euclidean3d(acc.o.coords, don.x.coords)
@@ -169,62 +174,219 @@ def halogen(acceptor, donor):
             vec1, vec2 = vector(acc.o.coords, acc.y.coords), vector(acc.o.coords, don.x.coords)
             vec3, vec4 = vector(don.x.coords, acc.o.coords), vector(don.x.coords, don.c.coords)
             acc_angle, don_angle = vecangle(vec1, vec2), vecangle(vec3, vec4)
-            if config.HALOGEN_ACC_ANGLE-config.HALOGEN_ANGLE_DEV < acc_angle < config.HALOGEN_ACC_ANGLE+config.HALOGEN_ANGLE_DEV:
-                if config.HALOGEN_DON_ANGLE-config.HALOGEN_ANGLE_DEV < don_angle < config.HALOGEN_DON_ANGLE+config.HALOGEN_ANGLE_DEV:
-                    contact = data(acc=acc, don=don, distance=dist, don_angle=don_angle, acc_angle=acc_angle,
+            is_sidechain_hal = acc.o.OBAtom.GetResidue().GetAtomProperty(acc.o.OBAtom, 8)  # Check if sidechain atom
+            if config.HALOGEN_ACC_ANGLE - config.HALOGEN_ANGLE_DEV < acc_angle \
+                    < config.HALOGEN_ACC_ANGLE + config.HALOGEN_ANGLE_DEV:
+                if config.HALOGEN_DON_ANGLE - config.HALOGEN_ANGLE_DEV < don_angle \
+                        < config.HALOGEN_DON_ANGLE + config.HALOGEN_ANGLE_DEV:
+                    contact = data(acc=acc, acc_orig_idx=acc.o_orig_idx, don=don, don_orig_idx=don.x_orig_idx,
+                                   distance=dist, don_angle=don_angle, acc_angle=acc_angle,
                                    restype=whichrestype(acc.o), resnr=whichresnumber(acc.o),
-                                   reschain=whichchain(acc.o), donortype=don.x.OBAtom.GetType(), acctype=acc.o.type)
+                                   reschain=whichchain(acc.o), donortype=don.x.OBAtom.GetType(), acctype=acc.o.type,
+                                   sidechain=is_sidechain_hal)
                     pairings.append(contact)
     return pairings
 
 
 def water_bridges(bs_hba, lig_hba, bs_hbd, lig_hbd, water):
     """Find water-bridged hydrogen bonds between ligand and protein. For now only considers bridged of first degree."""
-    data = namedtuple('waterbridge', 'a atype d dtype h water distance_aw distance_dw d_angle w_angle type resnr restype reschain protisdon')
+    data = namedtuple('waterbridge', 'a a_orig_idx atype d d_orig_idx dtype h water water_orig_idx distance_aw '
+                                     'distance_dw d_angle w_angle type resnr restype reschain protisdon')
     pairings = []
     # First find all acceptor-water pairs with distance within d
     # and all donor-water pairs with distance within d and angle greater theta
     lig_aw, prot_aw, lig_dw, prot_hw = [], [], [], []
     for w in water:
         for acc1 in lig_hba:
-            dist = euclidean3d(acc1.a.coords, w.coords)
+            dist = euclidean3d(acc1.a.coords, w.oxy.coords)
             if config.WATER_BRIDGE_MINDIST <= dist <= config.WATER_BRIDGE_MAXDIST:
                 lig_aw.append((acc1, w, dist))
         for acc2 in bs_hba:
-            dist = euclidean3d(acc2.a.coords, w.coords)
+            dist = euclidean3d(acc2.a.coords, w.oxy.coords)
             if config.WATER_BRIDGE_MINDIST <= dist <= config.WATER_BRIDGE_MAXDIST:
                 prot_aw.append((acc2, w, dist))
         for don1 in lig_hbd:
-            dist = euclidean3d(don1.d.coords, w.coords)
-            d_angle = vecangle(vector(don1.h.coords, don1.d.coords), vector(don1.h.coords, w.coords))
-            if config.WATER_BRIDGE_MINDIST <= dist <= config.WATER_BRIDGE_MAXDIST and d_angle > config.WATER_BRIDGE_THETA_MIN:
+            dist = euclidean3d(don1.d.coords, w.oxy.coords)
+            d_angle = vecangle(vector(don1.h.coords, don1.d.coords), vector(don1.h.coords, w.oxy.coords))
+            if config.WATER_BRIDGE_MINDIST <= dist <= config.WATER_BRIDGE_MAXDIST \
+                    and d_angle > config.WATER_BRIDGE_THETA_MIN:
                 lig_dw.append((don1, w, dist, d_angle))
         for don2 in bs_hbd:
-            dist = euclidean3d(don2.d.coords, w.coords)
-            d_angle = vecangle(vector(don2.h.coords, don2.d.coords), vector(don2.h.coords, w.coords))
-            if config.WATER_BRIDGE_MINDIST <= dist <= config.WATER_BRIDGE_MAXDIST and d_angle > config.WATER_BRIDGE_THETA_MIN:
+            dist = euclidean3d(don2.d.coords, w.oxy.coords)
+            d_angle = vecangle(vector(don2.h.coords, don2.d.coords), vector(don2.h.coords, w.oxy.coords))
+            if config.WATER_BRIDGE_MINDIST <= dist <= config.WATER_BRIDGE_MAXDIST \
+                    and d_angle > config.WATER_BRIDGE_THETA_MIN:
                 prot_hw.append((don2, w, dist, d_angle))
 
     for l, p in itertools.product(lig_aw, prot_hw):
         acc, wl, distance_aw = l
         don, wd, distance_dw, d_angle = p
-        if wl == wd:  # Same water molecule and angle within omega
-            w_angle = vecangle(vector(acc.a.coords, wl.coords), vector(wl.coords, don.h.coords))
+        if wl.oxy == wd.oxy:  # Same water molecule and angle within omega
+            w_angle = vecangle(vector(acc.a.coords, wl.oxy.coords), vector(wl.oxy.coords, don.h.coords))
             if config.WATER_BRIDGE_OMEGA_MIN < w_angle < config.WATER_BRIDGE_OMEGA_MAX:
-                contact = data(a=acc.a, atype=acc.a.type, d=don.d, dtype=don.d.type, h=don.h, water=wl,
-                               distance_aw=distance_aw, distance_dw=distance_dw,
-                               d_angle=d_angle, w_angle=w_angle, type='first_deg', resnr=whichresnumber(don.d),
-                               restype=whichrestype(don.d), reschain=whichchain(don.d), protisdon=True)
+                contact = data(a=acc.a, a_orig_idx=acc.a_orig_idx, atype=acc.a.type, d=don.d, d_orig_idx=don.d_orig_idx,
+                               dtype=don.d.type, h=don.h, water=wl.oxy, water_orig_idx=wl.oxy_orig_idx,
+                               distance_aw=distance_aw, distance_dw=distance_dw, d_angle=d_angle, w_angle=w_angle,
+                               type='first_deg', resnr=whichresnumber(don.d), restype=whichrestype(don.d),
+                               reschain=whichchain(don.d), protisdon=True)
                 pairings.append(contact)
     for p, l in itertools.product(prot_aw, lig_dw):
         acc, wl, distance_aw = p
         don, wd, distance_dw, d_angle = l
-        if wl == wd:  # Same water molecule and angle within omega
-            w_angle = vecangle(vector(acc.a.coords, wl.coords), vector(wl.coords, don.h.coords))
+        if wl.oxy == wd.oxy:  # Same water molecule and angle within omega
+            w_angle = vecangle(vector(acc.a.coords, wl.oxy.coords), vector(wl.oxy.coords, don.h.coords))
             if config.WATER_BRIDGE_OMEGA_MIN < w_angle < config.WATER_BRIDGE_OMEGA_MAX:
-                contact = data(a=acc.a, atype=acc.a.type, d=don.d, dtype=don.d.type, h=don.h, water=wl,
-                               distance_aw=distance_aw, distance_dw=distance_dw, d_angle=d_angle, w_angle=w_angle,
-                               type='first_deg', resnr=whichresnumber(acc.a),
+                contact = data(a=acc.a, a_orig_idx=acc.a_orig_idx, atype=acc.a.type, d=don.d, d_orig_idx=don.d_orig_idx,
+                               dtype=don.d.type, h=don.h, water=wl.oxy, water_orig_idx=wl.oxy_orig_idx,
+                               distance_aw=distance_aw, distance_dw=distance_dw,
+                               d_angle=d_angle, w_angle=w_angle, type='first_deg', resnr=whichresnumber(acc.a),
                                restype=whichrestype(acc.a), reschain=whichchain(acc.a), protisdon=False)
                 pairings.append(contact)
     return pairings
+
+
+def metal_complexation(metals, metal_binding_lig, metal_binding_bs):
+    """Find all metal complexes between metals and appropriate groups in both protein and ligand, as well as water"""
+    data = namedtuple('metal_complex', 'metal metal_orig_idx metal_type target target_orig_idx target_type '
+                                       'coordination_num distance resnr restype '
+                                       'reschain location rms, geometry num_partners complexnum')
+    pairings_dict = {}
+    pairings = []
+    # #@todo Refactor
+    metal_to_id = {}
+    for metal, target in itertools.product(metals, metal_binding_lig + metal_binding_bs):
+        distance = euclidean3d(metal.m.coords, target.atom.coords)
+        if distance < config.METAL_DIST_MAX:
+            if metal.m not in pairings_dict:
+                pairings_dict[metal.m] = [(target, distance), ]
+                metal_to_id[metal.m] = metal.m_orig_idx
+            else:
+                pairings_dict[metal.m].append((target, distance))
+    for cnum, metal in enumerate(pairings_dict):
+        rms = 0.0
+        excluded = []
+        # cnum +1 being the complex number
+        contact_pairs = pairings_dict[metal]
+        num_targets = len(contact_pairs)
+        vectors_dict = defaultdict(list)
+        for contact_pair in contact_pairs:
+            target, distance = contact_pair
+            vectors_dict[target.atom.idx].append(vector(metal.coords, target.atom.coords))
+
+        # Listing of coordination numbers and their geometries
+        configs = {2: ['linear', ],
+                   3: ['trigonal.planar', 'trigonal.pyramidal'],
+                   4: ['tetrahedral', 'square.planar'],
+                   5: ['trigonal.bipyramidal', 'square.pyramidal'],
+                   6: ['octahedral', ]}
+
+        # Angle signatures for each geometry (as seen from each target atom)
+        ideal_angles = {'linear': [[180.0]] * 2,
+                        'trigonal.planar': [[120.0, 120.0]] * 3,
+                        'trigonal.pyramidal': [[109.5, 109.5]] * 3,
+                        'tetrahedral': [[109.5, 109.5, 109.5, 109.5]] * 4,
+                        'square.planar': [[90.0, 90.0, 90.0, 90.0]] * 4,
+                        'trigonal.bipyramidal': [[120.0, 120.0, 90.0, 90.0]] * 3 + [[90.0, 90.0, 90.0, 180.0]] * 2,
+                        'square.pyramidal': [[90.0, 90.0, 90.0, 180.0]] * 4 + [[90.0, 90.0, 90.0, 90.0]],
+                        'octahedral': [[90.0, 90.0, 90.0, 90.0, 180.0]] * 6}
+        angles_dict = {}
+
+        for target in vectors_dict:
+            cur_vector = vectors_dict[target]
+            other_vectors = []
+            for t in vectors_dict:
+                if not t == target:
+                    [other_vectors.append(x) for x in vectors_dict[t]]
+            angles = [vecangle(pair[0], pair[1]) for pair in itertools.product(cur_vector, other_vectors)]
+            angles_dict[target] = angles
+
+        all_total = []  # Record fit information for each geometry tested
+        gdata = namedtuple('gdata', 'geometry rms coordination excluded diff_targets')  # Geometry Data
+        # Can't specify geometry with only one target
+        if num_targets == 1:
+            final_geom = 'NA'
+            final_coo = 1
+            excluded = []
+            rms = 0.0
+        else:
+            for coo in sorted(configs, reverse=True):  # Start with highest coordination number
+                geometries = configs[coo]
+                for geometry in geometries:
+                    signature = ideal_angles[geometry]  # Set of ideal angles for geometry, from each perspective
+                    geometry_total = 0
+                    geometry_scores = []  # All scores for one geometry (from all subsignatures)
+                    used_up_targets = []  # Use each target just once for a subsignature
+                    not_used = []
+                    coo_diff = num_targets - coo  # How many more observed targets are there?
+
+                    # Find best match for each subsignature
+                    for subsignature in signature:  # Ideal angles from one perspective
+                        best_target = None  # There's one best-matching target for each subsignature
+                        best_target_score = 999
+
+                        for k, target in enumerate(angles_dict):
+                            if target not in used_up_targets:
+                                observed_angles = angles_dict[target]  # Observed angles from perspective of one target
+                                single_target_scores = []
+                                used_up_observed_angles = []
+                                for i, ideal_angle in enumerate(subsignature):
+                                    # For each angle in the signature, find the best-matching observed angle
+                                    best_match = None
+                                    best_match_diff = 999
+                                    for j, observed_angle in enumerate(observed_angles):
+                                        if j not in used_up_observed_angles:
+                                            diff = abs(ideal_angle - observed_angle)
+                                            if diff < best_match_diff:
+                                                best_match_diff = diff
+                                                best_match = j
+                                    if best_match is not None:
+                                        used_up_observed_angles.append(best_match)
+                                        single_target_scores.append(best_match_diff)
+                                # Calculate RMS for target angles
+                                target_total = sum([x ** 2 for x in single_target_scores]) ** 0.5  # Tot. score targ/sig
+                                if target_total < best_target_score:
+                                    best_target_score = target_total
+                                    best_target = target
+
+                        used_up_targets.append(best_target)
+                        geometry_scores.append(best_target_score)
+                        # Total score is mean of RMS values
+                        geometry_total = np.mean(geometry_scores)
+                    # Record the targets not used for excluding them when deciding for a final geometry
+                    [not_used.append(target) for target in angles_dict if target not in used_up_targets]
+                    all_total.append(gdata(geometry=geometry, rms=geometry_total, coordination=coo,
+                                           excluded=not_used, diff_targets=coo_diff))
+
+        # Make a decision here. Starting with the geometry with lowest difference in ideal and observed partners ...
+        # Check if the difference between the RMS to the next best solution is not larger than 0.5
+        if not num_targets == 1:  # Can't decide for any geoemtry in that case
+            all_total = sorted(all_total, key=lambda x: abs(x.diff_targets))
+            for i, total in enumerate(all_total):
+                next_total = all_total[i + 1]
+                this_rms, next_rms = total.rms, next_total.rms
+                diff_to_next = next_rms - this_rms
+                if diff_to_next > 0.5:
+                    final_geom, final_coo, rms, excluded = total.geometry, total.coordination, total.rms, total.excluded
+                    break
+                elif next_total.rms < 3.5:
+                    final_geom, final_coo, = next_total.geometry, next_total.coordination
+                    rms, excluded = next_total.rms, next_total.excluded
+                    break
+                elif i == len(all_total) - 1:
+                    final_geom, final_coo, rms, excluded = "NA", "NA", 0.0, []
+
+        # Record all contact pairing, excluding those with targets superfluous for chosen geometry
+        only_water = set([x[0].location for x in contact_pairs]) == {'water'}
+        if not only_water:  # No complex if just with water as targets
+            message("Metal ion %s complexed with %s geometry (coo. number %r/ %i observed).\n"
+                    % (metal.type, final_geom, final_coo, num_targets), indent=True)
+            for contact_pair in contact_pairs:
+                target, distance = contact_pair
+                if target.atom.idx not in excluded:
+                    contact = data(metal=metal, metal_orig_idx=metal_to_id[metal], metal_type=metal.type,
+                                   target=target, target_orig_idx=target.atom_orig_idx, target_type=target.type,
+                                   coordination_num=final_coo, distance=distance, resnr=target.resnr,
+                                   restype=target.restype, reschain=target.reschain, location=target.location,
+                                   rms=rms, geometry=final_geom, num_partners=num_targets, complexnum=cnum + 1)
+                    pairings.append(contact)
+    return pairings
diff --git a/plip/modules/mp.py b/plip/modules/mp.py
new file mode 100644
index 0000000..ae5a951
--- /dev/null
+++ b/plip/modules/mp.py
@@ -0,0 +1,69 @@
+"""
+Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
+mp.py - Functions for parallel processing
+Copyright 2014-2015 Sebastian Salentin, Joachim Haupt
+
+Licensed under the Apache License, Version 2.0 (the "License");
+you may not use this file except in compliance with the License.
+You may obtain a copy of the License at
+
+    http://www.apache.org/licenses/LICENSE-2.0
+
+Unless required by applicable law or agreed to in writing, software
+distributed under the License is distributed on an "AS IS" BASIS,
+WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
+See the License for the specific language governing permissions and
+limitations under the License.
+"""
+
+# Python Standard Library
+from __future__ import division
+import multiprocessing
+import itertools
+from numpy import asarray
+from functools import partial
+
+
+class SubProcessError(Exception):
+    def __init__(self, e, exitcode=1):
+        self.exitcode = exitcode
+        super(SubProcessError, self).__init__(e)
+    pass
+
+
+def universal_worker(input_pair):
+    """This is a wrapper function expecting a tiplet of function, single
+       argument, dict of keyword arguments. The provided function is called
+       with the appropriate arguments.""" 
+    function, arg, kwargs = input_pair
+    return function(arg, **kwargs)
+
+
+def pool_args(function, sequence, kwargs):
+    """Return a single iterator of n elements of lists of length 3, given a sequence of len n."""
+    return itertools.izip(itertools.repeat(function), sequence, itertools.repeat(kwargs))
+
+
+def parallel_fn(f):
+    """Simple wrapper function, returning a parallel version of the given function f.
+       The function f must have one argument and may have an arbitray number of
+       keyword arguments. """
+       
+    def simple_parallel(func, sequence, **args):
+        """ f takes an element of sequence as input and the keyword args in **args"""
+        multiprocessing.freeze_support()
+        if 'processes' in args:
+            processes = args.get('processes')
+            del args['processes']
+        else:
+            processes = multiprocessing.cpu_count()
+        
+        pool = multiprocessing.Pool(processes=processes)  # depends on available cores
+        result = pool.map(universal_worker, pool_args(func, sequence, args))
+        cleaned = [x for x in result if x is not None]  # getting results
+        cleaned = asarray(cleaned)
+        pool.close()
+        pool.join()
+        return cleaned
+    return partial(simple_parallel, f)
+
diff --git a/plip/modules/preparation.py b/plip/modules/preparation.py
index 51a678a..3ad4f3a 100644
--- a/plip/modules/preparation.py
+++ b/plip/modules/preparation.py
@@ -1,7 +1,7 @@
 """
 Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
 preparation.py - Prepare PDB input files for processing.
-Copyright 2014 Sebastian Salentin
+Copyright 2014-2015 Sebastian Salentin
 
 Licensed under the Apache License, Version 2.0 (the "License");
 you may not use this file except in compliance with the License.
@@ -25,92 +25,397 @@ from detection import *
 from supplemental import *
 import config
 
+
 ################
 # MAIN CLASSES #
 ################
 
+class PDBParser:
+    def __init__(self, pdbpath):
+        self.pdbpath = pdbpath
+        self.num_fixed_lines = 0
+        self.covlinkage = namedtuple("covlinkage", "id1 chain1 pos1 conf1 id2 chain2 pos2 conf2")
+        self.proteinmap, self.modres, self.covalent, self.altconformations, self.corrected_pdb = self.parse_pdb()
+
+    def parse_pdb(self):
+        """Extracts additional information from PDB files.
+        I. When reading in a PDB file, OpenBabel numbers ATOMS and HETATOMS continously.
+        In PDB files, TER records are also counted, leading to a different numbering system.
+        This functions reads in a PDB file and provides a mapping as a dictionary.
+        II. Additionally, it returns a list of modified residues.
+        III. Furthermore, covalent linkages between ligands and protein residues/other ligands are identified
+        IV. Alternative conformations
+        """
+        fil = read(self.pdbpath).readlines()
+        # #@todo Also consider SSBOND entries here
+        corrected_lines = []
+        i, j = 0, 0  # idx and PDB numbering
+        d = {}
+        modres = set()
+        covalent = []
+        alt = []
+        previous_ter = False
+
+        #New code : Do fixing first and then do mapping on fixed lines
+        #@TODO Test code
+        lastnum = 0 # Atom numbering (has to be consecutive)
+        for line in fil:
+            corrected_line, newnum = self.fix_pdbline(line, lastnum)
+            if corrected_line is not None:
+                corrected_lines.append(corrected_line)
+                lastnum = newnum
+        corrected_pdb = ''.join(corrected_lines)
+
+
+        for line in corrected_lines:
+            if line.startswith(("ATOM", "HETATM")):
+                # Retrieve alternate conformations
+                atomid, location = int(line[6:11]), line[16]
+                location = 'A' if location == ' ' else location
+                if location != 'A':
+                    alt.append(atomid)
+
+                if not previous_ter:
+                    i += 1
+                    j += 1
+                else:
+                    i += 1
+                    j += 2
+                d[i] = j
+                previous_ter = False
+            # Numbering Changes at TER records
+            if line.startswith("TER"):
+                previous_ter = True
+            # Get modified residues
+            if line.startswith("MODRES"):
+                modres.add(line[12:15].strip())
+            # Get covalent linkages between ligands
+            if line.startswith("LINK"):
+                covalent.append(self.get_linkage(line))
+        return d, modres, covalent, alt, corrected_pdb
+
+    def fix_pdbline(self, pdbline, lastnum):
+        """Fix a PDB line if information is missing."""
+        fixed = False
+        newnum = 0
+        pdbline = pdbline.strip('\n')
+        # Some MD / Docking tools produce empty lines, leading to segfaults
+        if len(pdbline.strip()) == 0:
+            self.num_fixed_lines += 1
+            return None, lastnum
+        if len(pdbline) > 100: # Should be 80 long
+            self.num_fixed_lines += 1
+            return None, lastnum
+        # TER Entries also have continuing numbering, consider them as well
+        if pdbline.startswith('TER'):
+            newnum = lastnum + 1
+        if pdbline.startswith('ATOM'):
+            newnum = lastnum + 1
+            currentnum = int(pdbline[6:11])
+            if lastnum + 1 != currentnum:
+                pdbline = pdbline[:6] + (5 - len(str(newnum))) * ' ' + str(newnum) + ' ' + pdbline[12:]
+                fixed = True
+            # No chain assigned
+            if pdbline[21] == ' ':
+                pdbline = pdbline[:21] + 'A' + pdbline[22:]
+                fixed = True
+            if pdbline.endswith('H'):
+                self.num_fixed_lines += 1
+                return None, lastnum
+        if pdbline.startswith('HETATM'):
+            newnum = lastnum + 1
+            currentnum = int(pdbline[6:11])
+            if lastnum + 1 != currentnum:
+                pdbline = pdbline[:6] + (5 - len(str(newnum))) * ' ' + str(newnum) + ' ' + pdbline[12:]
+                fixed = True
+            # No chain assigned
+            if pdbline[21] == ' ':
+                pdbline = pdbline[:21] + 'Z' + pdbline[22:]
+                fixed = True
+            # No residue number assigned
+            if pdbline[23:26] == '   ':
+                pdbline = pdbline[:23] + '999' + pdbline[26:]
+                fixed = True
+            # Non-standard Ligand Names
+            ligname = pdbline[17:20]
+            if re.match("[^a-zA-Z0-9_]", ligname.strip()):
+                pdbline = pdbline[:17] + 'LIG ' + pdbline[21:]
+                fixed = True
+            if len(ligname.strip()) == 0:
+                pdbline = pdbline[:17] + 'LIG ' + pdbline[21:]
+                fixed = True
+            if pdbline.endswith('H'):
+                self.num_fixed_lines += 1
+                return None, lastnum
+        self.num_fixed_lines += 1 if fixed else 0
+        return pdbline + '\n', max(newnum, lastnum)
+
+    def get_linkage(self, line):
+        """Get the linkage information from a LINK entry PDB line."""
+        conf1, id1, chain1, pos1 = line[16].strip(), line[17:20].strip(), line[21].strip(), int(line[22:26])
+        conf2, id2, chain2, pos2 = line[46].strip(), line[47:50].strip(), line[51].strip(), int(line[52:56])
+        return self.covlinkage(id1=id1, chain1=chain1, pos1=pos1, conf1=conf1,
+                               id2=id2, chain2=chain2, pos2=pos2, conf2=conf2)
+
+
+class LigandFinder:
+    def __init__(self, proteincomplex, altconf, modres, covalent, mapper):
+        self.lignames_all = None
+        self.lignames_kept = None
+        self.water = None
+        self.proteincomplex = proteincomplex
+        self.altconformations = altconf
+        self.modresidues = modres
+        self.covalent = covalent
+        self.mapper = mapper
+        self.ligands = self.getligs()
+        self.excluded = sorted(list(self.lignames_all.difference(set(self.lignames_kept))))
+
+    def getligs(self):
+        """Get all ligands from a PDB file and prepare them for analysis.
+        Returns all non-empty ligands.
+        """
+        ligands = []
+
+        # Filter for ligands using lists
+        ligand_residues, self.lignames_all, self.water = self.filter_for_ligands()
+
+        all_res_dict = {(a.GetName(), a.GetChain(), a.GetNum()): a for a in ligand_residues}
+        self.lignames_kept = list(set([a.GetName() for a in ligand_residues]))
 
-class Mol():
+        if not config.BREAKCOMPOSITE:
+            #  Update register of covalent links with those between DNA/RNA subunits
+            self.covalent += nucleotide_linkage(all_res_dict)
+            #  Find fragment linked by covalent bonds
+            res_kmers = self.identify_kmers(all_res_dict)
+        else:
+            res_kmers = [[a, ] for a in ligand_residues]
+        for kmer in res_kmers:  # iterate over all ligands and extract molecules + information
+            ligands.append(self.extract_ligand(kmer))
+        return [lig for lig in ligands if len(lig.mol.atoms) != 0]
+
+    def extract_ligand(self, kmer):
+        """Extract the ligand by copying atoms and bonds and assign all information necessary for later steps."""
+        data = namedtuple('ligand', 'mol hetid chain position water members longname type atomorder can_to_pdb')
+        members = [(res.GetName(), res.GetChain(), int32_to_negative(res.GetNum())) for res in kmer]
+        members = sorted(members, key=lambda x: (x[1], x[2]))
+        rname, rchain, rnum = members[0]
+        debuglog("Finalizing extraction for ligand %s:%s:%s" % (rname, rchain, rnum))
+        names = [x[0] for x in members]
+        longname = '-'.join([x[0] for x in members])
+
+        # Classify a ligand by its HETID(s)
+        ligtype = classify_by_name(names)
+
+        hetatoms = set()
+        for obresidue in kmer:
+            hetatoms_res = set([(obatom.GetIdx(), obatom) for obatom in pybel.ob.OBResidueAtomIter(obresidue)
+                                if not obatom.IsHydrogen()])
+
+            if not config.ALTLOC:
+                # Remove alternative conformations (standard -> True)
+                hetatoms_res = set([atm for atm in hetatoms_res
+                                    if not self.mapper.mapid(atm[0], mtype='protein',
+                                                             to='internal') in self.altconformations])
+            hetatoms.update(hetatoms_res)
+
+        hetatoms = dict(hetatoms)  # make it a dict with idx as key and OBAtom as value
+        lig = pybel.ob.OBMol()  # new ligand mol
+        neighbours = dict()
+        for obatom in hetatoms.values():  # iterate over atom objects
+            idx = obatom.GetIdx()
+            lig.AddAtom(obatom)
+            # ids of all neighbours of obatom
+            neighbours[idx] = set([neighbour_atom.GetIdx() for neighbour_atom
+                                   in pybel.ob.OBAtomAtomIter(obatom)]) & set(hetatoms.keys())
+
+        ##############################################################
+        # map the old atom idx of OBMol to the new idx of the ligand #
+        ##############################################################
+
+        newidx = dict(zip(hetatoms.keys(), [obatom.GetIdx() for obatom in pybel.ob.OBMolAtomIter(lig)]))
+        mapold = dict(zip(newidx.values(), newidx))
+        # copy the bonds
+        for obatom in hetatoms:
+            for neighbour_atom in neighbours[obatom]:
+                bond = hetatoms[obatom].GetBond(hetatoms[neighbour_atom])
+                lig.AddBond(newidx[obatom], newidx[neighbour_atom], bond.GetBondOrder())
+        lig = pybel.Molecule(lig)
+
+        # For kmers, the representative ids are chosen (first residue of kmer)
+        lig.data.update({'Name': rname, 'Chain': rchain, 'ResNr': rnum})
+
+        # Check if a negative residue number is represented as a 32 bit integer
+        if rnum > 10 ** 5:
+            rnum = int32_to_negative(rnum)
+
+        lig.title = ':'.join((rname, rchain, str(rnum)))
+        self.mapper.ligandmaps[lig.title] = mapold
+
+        atomorder = canonicalize(lig)
+
+        can_to_pdb = {}
+        if atomorder is not None:
+            can_to_pdb = {atomorder[key-1]: mapold[key] for key in mapold}
+
+        ligand = data(mol=lig, hetid=rname, chain=rchain, position=rnum, water=self.water,
+                      members=members, longname=longname, type=ligtype, atomorder=atomorder,
+                      can_to_pdb=can_to_pdb)
+        return ligand
+
+    def filter_for_ligands(self):
+        """Given an OpenBabel Molecule, get all ligands, their names, and water"""
+
+        candidates1 = [o for o in pybel.ob.OBResidueIter(self.proteincomplex.OBMol) if not (o.GetResidueProperty(9)
+                                                                                         or o.GetResidueProperty(0))]
+        all_lignames = set([a.GetName() for a in candidates1])
+
+        water = [o for o in pybel.ob.OBResidueIter(self.proteincomplex.OBMol) if o.GetResidueProperty(9)]
+        # Filter out non-ligands
+        candidates2 = [a for a in candidates1 if is_lig(a.GetName()) and a.GetName() not in self.modresidues]
+        debuglog("%i ligand(s) after first filtering step." % len(candidates2))
+
+        ############################################
+        # Filtering by counting and artifacts list #
+        ############################################
+        artifacts = []
+        unique_ligs = set(a.GetName() for a in candidates2)
+        for ulig in unique_ligs:
+            # Discard if appearing 15 times or more and is possible artifact
+            if ulig in config.biolip_list and [a.GetName() for a in candidates2].count(ulig) >= 15:
+                artifacts.append(ulig)
+
+        selected_ligands = [a for a in candidates2 if a.GetName() not in artifacts]
+
+        return selected_ligands, all_lignames, water
+
+    def identify_kmers(self, residues):
+        """Using the covalent linkage information, find out which fragments/subunits form a ligand."""
+
+        # Remove all those not considered by ligands and pairings including alternate conformations
+        ligdoubles = [[(link.id1, link.chain1, link.pos1),
+                       (link.id2, link.chain2, link.pos2)] for link in
+                      [c for c in self.covalent if c.id1 in self.lignames_kept and c.id2 in self.lignames_kept and
+                       c.conf1 in ['A', ''] and c.conf2 in ['A', '']
+                      and (c.id1, c.chain1, c.pos1) in residues and (c.id2, c.chain2, c.pos2) in residues]]
+        kmers = cluster_doubles(ligdoubles)
+        if not kmers:  # No ligand kmers, just normal independent ligands
+            return [[residues[res]] for res in residues]
 
-    def __init__(self, altconf):
+        else:
+            # res_kmers contains clusters of covalently bound ligand residues (kmer ligands)
+            res_kmers = [[residues[res] for res in kmer] for kmer in kmers]
+
+            # In this case, add other ligands which are not part of a kmer
+            in_kmer = []
+            for res_kmer in res_kmers:
+                for res in res_kmer:
+                    in_kmer.append((res.GetName(), res.GetChain(), res.GetNum()))
+            for res in residues:
+                if res not in in_kmer:
+                    newres = [residues[res], ]
+                    res_kmers.append(newres)
+            return res_kmers
+
+
+class Mapper:
+    """Provides functions for mapping atom IDs in the correct way"""
+    def __init__(self):
+        self.proteinmap = None  # Map internal atom IDs of protein residues to original PDB Atom IDs
+        self.ligandmaps = {}  # Map IDs of new ligand molecules to internal IDs (or PDB IDs?)
+
+    def mapid(self, idx, mtype, bsid=None, to='original'):  # Mapping to original IDs is standard for ligands
+        # #@todo Check for correct type of idx
+        # #@todo Include more safety checks
+        if mtype == 'protein':
+            return self.proteinmap[idx]
+        elif mtype == 'ligand':
+            if to == 'internal':
+                return self.ligandmaps[bsid][idx]
+            elif to == 'original':
+                return self.proteinmap[self.ligandmaps[bsid][idx]]
+
+    # #@todo Include chains, resnr and positions here!
+
+
+class Mol:
+    def __init__(self, altconf, mapper, mtype, bsid):
+        self.mtype = mtype
+        self.bsid = bsid
         self.rings = None
         self.hydroph_atoms = None
         self.charged = None
         self.hbond_don_atom_pairs = None
         self.hbond_acc_atoms = None
         self.altconf = altconf
+        self.Mapper = mapper
 
     def hydrophobic_atoms(self, all_atoms):
         """Select all carbon atoms which have only carbons and/or hydrogens as direct neighbors."""
-        data = namedtuple('hydrophobic', 'atoms')
+        atom_set = []
+        data = namedtuple('hydrophobic', 'atom orig_idx')
         atm = [a for a in all_atoms if a.atomicnum == 6 and set([natom.GetAtomicNum() for natom
-                                                                in pybel.ob.OBAtomAtomIter(a.OBAtom)]).issubset({1, 6})]
-        atm = [a for a in atm if a.idx not in self.altconf]
-        return data(atoms=atm)
+                                                                 in pybel.ob.OBAtomAtomIter(a.OBAtom)]).issubset(
+            {1, 6})]
+        for atom in atm:
+            orig_idx = self.Mapper.mapid(atom.idx, mtype=self.mtype, bsid=self.bsid)
+            if atom.idx not in self.altconf:
+                atom_set.append(data(atom=atom, orig_idx=orig_idx))
+        return atom_set
 
     def find_hba(self, all_atoms):
         """Find all possible hydrogen bond acceptors"""
-        data = namedtuple('hbondacceptor', 'a type')
+        data = namedtuple('hbondacceptor', 'a a_orig_idx type')
         a_set = []
         for atom in itertools.ifilter(lambda at: at.OBAtom.IsHbondAcceptor(), all_atoms):
             if atom.atomicnum not in [9, 17, 35, 53] and atom.idx not in self.altconf:  # Exclude halogen atoms
-                a_set.append(data(a=atom, type='regular'))
+                a_orig_idx = self.Mapper.mapid(atom.idx, mtype=self.mtype, bsid=self.bsid)
+                a_set.append(data(a=atom, a_orig_idx=a_orig_idx, type='regular'))
         return a_set
 
     def find_hbd(self, all_atoms, hydroph_atoms):
         """Find all possible strong and weak hydrogen bonds donors (all hydrophobic C-H pairings)"""
         donor_pairs = []
-        data = namedtuple('hbonddonor', 'd h type')
+        data = namedtuple('hbonddonor', 'd d_orig_idx h type')
         for donor in [a for a in all_atoms if a.OBAtom.IsHbondDonor() and a.idx not in self.altconf]:
             in_ring = False
             if not in_ring:
                 for adj_atom in [a for a in pybel.ob.OBAtomAtomIter(donor.OBAtom) if a.IsHbondDonorH()]:
-                    donor_pairs.append(data(d=donor, h=pybel.Atom(adj_atom), type='regular'))
-        for carbon in hydroph_atoms.atoms:
-            for adj_atom in [a for a in pybel.ob.OBAtomAtomIter(carbon.OBAtom) if a.GetAtomicNum() == 1]:
-                donor_pairs.append(data(d=carbon, h=pybel.Atom(adj_atom), type='weak'))
+                    d_orig_idx = self.Mapper.mapid(donor.idx, mtype=self.mtype, bsid=self.bsid)
+                    donor_pairs.append(data(d=donor, d_orig_idx=d_orig_idx, h=pybel.Atom(adj_atom), type='regular'))
+        for carbon in hydroph_atoms:
+            for adj_atom in [a for a in pybel.ob.OBAtomAtomIter(carbon.atom.OBAtom) if a.GetAtomicNum() == 1]:
+                d_orig_idx = self.Mapper.mapid(carbon.atom.idx, mtype=self.mtype, bsid=self.bsid)
+                donor_pairs.append(data(d=carbon, d_orig_idx=d_orig_idx, h=pybel.Atom(adj_atom), type='weak'))
         return donor_pairs
 
+
     def find_rings(self, mol, all_atoms):
-        """Find rings and return only aromatic."""
-        data = namedtuple('aromatic_ring', 'atoms normal obj center type')
-        rings, arings = [], []
+        """Find rings and return only aromatic.
+        Rings have to be sufficiently planar OR be detected by OpenBabel as aromatic."""
+        data = namedtuple('aromatic_ring', 'atoms atoms_orig_idx normal obj center type')
+        rings = []
+        aromatic_amino = ['TYR', 'TRP', 'HIS', 'PHE']
+        ring_candidates = mol.OBMol.GetSSSR()
+        debuglog("Number of aromatic ring candidates: %i" % len(ring_candidates))
         # Check here first for ligand rings not being detected as aromatic by Babel and check for planarity
-        if len(mol.title) > 0:  # it's the ligand
-            for ring in [r for r in mol.OBMol.GetSSSR()]:
-                r_atoms = [a for a in all_atoms if ring.IsMember(a.OBAtom)]
-                normals = []
-                aromatic = True
-                for a in r_atoms:
-                    adj = pybel.ob.OBAtomAtomIter(a.OBAtom)
-                    # Check for neighboring atoms in the ring
-                    n_coords = [pybel.Atom(neigh).coords for neigh in adj if ring.IsMember(neigh)]
-                    vec1, vec2 = vector(a.coords, n_coords[0]), vector(a.coords, n_coords[1])
-                    normals.append(np.cross(vec1, vec2))
-                # Given all normals of ring atoms and their neighbors, the angle between any has to be 7.5 deg or less
-                for n1, n2 in itertools.product(normals, repeat=2):
-                    if config.AROMATIC_PLANARITY < vecangle(n1, n2) < 180.0-config.AROMATIC_PLANARITY:
-                            aromatic = False
-                            break
-                # Ring is aromatic either by OpenBabel's criteria or if sufficiently planar
-                if aromatic or ring.IsAromatic():
-                    arings.append(ring)
-        else:
-            arings = [r for r in mol.OBMol.GetSSSR() if r.IsAromatic()]
-
-        # Store all rings which are detected as aromatic by Babel or are sufficiently planar
-        for r in arings:
-            r_atoms = [a for a in all_atoms if r.IsMember(a.OBAtom)]
-            # Only consider rings with a minimum size of 5 atoms and restrict selection to avoid problems in
-            # covalently bound ligands
-            if 4 < len(r_atoms) <= 6 and whichrestype(r_atoms[0]) in ['LIG', 'PHE', 'TYR', 'TRP', 'HIS']:
-                typ = r.GetType() if not r.GetType() == '' else 'unknown'
-                ring_atms = [r_atoms[a].coords for a in [0, 2, 4]]  # Probe atoms for normals, assuming planarity
-                ringv1 = vector(ring_atms[0], ring_atms[1])
-                ringv2 = vector(ring_atms[2], ring_atms[0])
-                rings.append(data(atoms=r_atoms,
+        for ring in ring_candidates:
+            r_atoms = [a for a in all_atoms if ring.IsMember(a.OBAtom)]
+            if 4 < len(r_atoms) <= 6:
+                res = list(set([whichrestype(a) for a in r_atoms]))
+                if ring.IsAromatic() or res[0] in aromatic_amino or ring_is_planar(ring, r_atoms):
+                    # Causes segfault with OpenBabel 2.3.2, so deactivated
+                    #typ = ring.GetType() if not ring.GetType() == '' else 'unknown'
+                    # Alternative typing
+                    typ = '%s-membered' % len(r_atoms)
+                    ring_atms = [r_atoms[a].coords for a in [0, 2, 4]]  # Probe atoms for normals, assuming planarity
+                    ringv1 = vector(ring_atms[0], ring_atms[1])
+                    ringv2 = vector(ring_atms[2], ring_atms[0])
+                    atoms_orig_idx = [self.Mapper.mapid(r_atom.idx, mtype=self.mtype, bsid=self.bsid) for r_atom in r_atoms]
+                    rings.append(data(atoms=r_atoms,
+                                  atoms_orig_idx=atoms_orig_idx,
                                   normal=normalize_vector(np.cross(ringv1, ringv2)),
-                                  obj=r,
+                                  obj=ring,
                                   center=centroid([ra.coords for ra in r_atoms]),
                                   type=typ))
         return rings
@@ -127,9 +432,6 @@ class Mol():
     def get_weak_hbd(self):
         return [don_pair for don_pair in self.hbond_don_atom_pairs if don_pair.type == 'weak']
 
-    def get_rings(self):
-        return self.rings
-
     def get_pos_charged(self):
         return [charge for charge in self.charged if charge.type == 'positive']
 
@@ -137,19 +439,19 @@ class Mol():
         return [charge for charge in self.charged if charge.type == 'negative']
 
 
-class PLInteraction():
+class PLInteraction:
     """Class to store a ligand, a protein and their interactions."""
+
     def __init__(self, lig_obj, bs_obj, protcomplex):
         """Detect all interactions when initializing"""
         self.ligand = lig_obj
-        self.name = lig_obj.name
         self.lig_members = lig_obj.members
         self.pdbid = protcomplex.pymol_name
         self.bindingsite = bs_obj
-        self.idx_to_pdb = protcomplex.idx_to_pdb_mapping
-        self.lig_to_pdb = lig_obj.pymol_data.maptopdb
+        self.Mapper = protcomplex.Mapper
         self.output_path = protcomplex.output_path
         self.altconf = protcomplex.altconf
+        # #@todo Refactor code to combine different directionality
 
         self.saltbridge_lneg = saltbridge(self.bindingsite.get_pos_charged(), self.ligand.get_neg_charged(), True)
         self.saltbridge_pneg = saltbridge(self.ligand.get_pos_charged(), self.bindingsite.get_neg_charged(), False)
@@ -164,10 +466,10 @@ class PLInteraction():
         self.hbonds_pdon = self.refine_hbonds_pdon(self.all_hbonds_pdon, self.saltbridge_lneg,
                                                    self.saltbridge_pneg)
 
-        self.pistacking = pistacking(self.bindingsite.get_rings(), self.ligand.get_rings())
+        self.pistacking = pistacking(self.bindingsite.rings, self.ligand.rings)
 
-        self.all_pi_cation_laro = pication(self.ligand.get_rings(), self.bindingsite.get_pos_charged(), True)
-        self.pication_paro = pication(self.bindingsite.get_rings(), self.ligand.get_pos_charged(), False)
+        self.all_pi_cation_laro = pication(self.ligand.rings, self.bindingsite.get_pos_charged(), True)
+        self.pication_paro = pication(self.bindingsite.rings, self.ligand.get_pos_charged(), False)
 
         self.pication_laro = self.refine_pi_cation_laro(self.all_pi_cation_laro, self.pistacking)
 
@@ -180,20 +482,91 @@ class PLInteraction():
                                            self.ligand.water)
 
         self.water_bridges = self.refine_water_bridges(self.water_bridges, self.hbonds_ldon, self.hbonds_pdon)
-        self.no_interactions = all(len(i) == 0 for i in [self.saltbridge_lneg, self.saltbridge_pneg, self.hbonds_ldon,
-                                                         self.hbonds_pdon, self.pistacking, self.pication_paro,
-                                                         self.pication_paro, self.hydrophobic_contacts,
-                                                         self.halogen_bonds, self.water_bridges])
 
-        self.interacting_chains = sorted(list(set([i.reschain for i in self.saltbridge_lneg + self.saltbridge_pneg +
-                                                   self.hbonds_pdon + self.hbonds_ldon + self.pistacking +
-                                                   self.pication_laro + self.pication_paro + self.hydrophobic_contacts +
-                                                   self.halogen_bonds + self.water_bridges])))
+        self.metal_complexes = metal_complexation(self.ligand.metals, self.ligand.metal_binding,
+                                                  self.bindingsite.metal_binding)
+
+        self.all_itypes = self.saltbridge_lneg + self.saltbridge_pneg + self.hbonds_pdon
+        self.all_itypes = self.all_itypes + self.hbonds_ldon + self.pistacking + self.pication_laro + self.pication_paro
+        self.all_itypes = self.all_itypes + self.hydrophobic_contacts + self.halogen_bonds + self.water_bridges
+        self.all_itypes = self.all_itypes + self.metal_complexes
+
+        self.no_interactions = all(len(i) == 0 for i in self.all_itypes)
+        self.unpaired_hba, self.unpaired_hbd, self.unpaired_hal = self.find_unpaired_ligand()
+        self.unpaired_hba_orig_idx = [self.Mapper.mapid(atom.idx, mtype='ligand', bsid=self.ligand.bsid)
+                                      for atom in self.unpaired_hba]
+        self.unpaired_hbd_orig_idx = [self.Mapper.mapid(atom.idx, mtype='ligand', bsid=self.ligand.bsid)
+                                      for atom in self.unpaired_hbd]
+        self.unpaired_hal_orig_idx = [self.Mapper.mapid(atom.idx, mtype='ligand', bsid=self.ligand.bsid)
+                                      for atom in self.unpaired_hal]
+        self.num_unpaired_hba, self.num_unpaired_hbd = len(self.unpaired_hba), len(self.unpaired_hbd)
+        self.num_unpaired_hal = len(self.unpaired_hal)
+
+        # Exclude empty chains (coming from ligand as a target, from metal complexes)
+        self.interacting_chains = sorted(list(set([i.reschain for i in self.all_itypes
+                                                   if i.reschain not in [' ', None]])))
+
+        # Get all interacting residues, excluding ligand and water molecules
+        self.interacting_res = list(set([''.join([str(i.resnr), str(i.reschain)]) for i in self.all_itypes
+                                         if i.restype not in ['LIG', 'HOH']]))
+        if len(self.interacting_res) != 0:
+            message('Ligand interacts with %i binding site residue(s) in chain(s) %s.\n'
+                    % (len(self.interacting_res), '/'.join(self.interacting_chains)), indent=True)
+            interactions_list = []
+            num_saltbridges = len(self.saltbridge_lneg + self.saltbridge_pneg)
+            num_hbonds = len(self.hbonds_ldon + self.hbonds_pdon)
+            num_pication = len(self.pication_laro + self.pication_paro)
+            num_pistack = len(self.pistacking)
+            num_halogen = len(self.halogen_bonds)
+            num_waterbridges = len(self.water_bridges)
+            if num_saltbridges != 0:
+                interactions_list.append('%i salt bridge(s)' % num_saltbridges)
+            if num_hbonds != 0:
+                interactions_list.append('%i hydrogen bond(s)' % num_hbonds)
+            if num_pication != 0:
+                interactions_list.append('%i pi-cation interaction(s)' % num_pication)
+            if num_pistack != 0:
+                interactions_list.append('%i pi-stacking(s)' % num_pistack)
+            if num_halogen != 0:
+                interactions_list.append('%i halogen bond(s)' % num_halogen)
+            if num_waterbridges != 0:
+                interactions_list.append('%i water bridge(s)' % num_waterbridges)
+            if not len(interactions_list) == 0:
+                message('Complex uses %s.\n' % ', '.join(interactions_list), indent=True)
+        else:
+            message('No interactions for this ligand.\n', indent=True)
+
+    def find_unpaired_ligand(self):
+        """Identify unpaired functional in groups in ligands, involving H-Bond donors, acceptors, halogen bond donors.
+        """
+        unpaired_hba, unpaired_hbd, unpaired_hal = [], [], []
+        # Unpaired hydrogen bond acceptors/donors in ligand (not used for hydrogen bonds/water, salt bridges/mcomplex)
+        involved_atoms = [hbond.a.idx for hbond in self.hbonds_pdon] + [hbond.d.idx for hbond in self.hbonds_ldon]
+        [[involved_atoms.append(atom.idx) for atom in sb.negative.atoms] for sb in self.saltbridge_lneg]
+        [[involved_atoms.append(atom.idx) for atom in sb.positive.atoms] for sb in self.saltbridge_pneg]
+        [involved_atoms.append(wb.a.idx) for wb in self.water_bridges if wb.protisdon]
+        [involved_atoms.append(wb.d.idx) for wb in self.water_bridges if not wb.protisdon]
+        [involved_atoms.append(mcomplex.target.atom.idx) for mcomplex in self.metal_complexes
+         if mcomplex.location == 'ligand']
+        for atom in [hba.a for hba in self.ligand.get_hba()]:
+            if atom.idx not in involved_atoms:
+                unpaired_hba.append(atom)
+        for atom in [hbd.d for hbd in self.ligand.get_hbd()]:
+            if atom.idx not in involved_atoms:
+                unpaired_hbd.append(atom)
+
+        # unpaired halogen bond donors in ligand (not used for the previous + halogen bonds)
+        [involved_atoms.append(atom.don.x.idx) for atom in self.halogen_bonds]
+        for atom in [haldon.x for haldon in self.ligand.halogenbond_don]:
+            if atom.idx not in involved_atoms:
+                unpaired_hal.append(atom)
+
+        return unpaired_hba, unpaired_hbd, unpaired_hal
 
     def refine_hydrophobic(self, all_h, pistacks):
         """Apply several rules to reduce the number of hydrophobic interactions."""
         sel = {}
-        #  1. Rings interacting via stacking can't have additional hydrophobic pliprofiler between each other.
+        #  1. Rings interacting via stacking can't have additional hydrophobic contacts between each other.
         for pistack, h in itertools.product(pistacks, all_h):
             h1, h2 = h.bsatom.idx, h.ligatom.idx
             brs, lrs = [p1.idx for p1 in pistack.proteinring.atoms], [p2.idx for p2 in pistack.ligandring.atoms]
@@ -252,7 +625,9 @@ class PLInteraction():
                         min_dist = h.distance
                         min_h = h
                 hydroph_final.append(min_h)
-
+        before, reduced = len(all_h), len(hydroph_final)
+        if not before == 0 and not before == reduced:
+            message('Reduced number of hydrophobic contacts from %i to %i.\n' % (before, reduced), indent=True)
         return hydroph_final
 
     def refine_hbonds_ldon(self, all_hbonds, salt_lneg, salt_pneg):
@@ -325,26 +700,27 @@ class PLInteraction():
     def refine_water_bridges(self, wbridges, hbonds_ldon, hbonds_pdon):
         """A donor atom already forming a hydrogen bond is not allowed to form a water bridge. Each water molecule
         can only be donor for two water bridges, selecting the constellation with the omega angle closest to 110 deg."""
-        donor_atoms_hbonds = [hb.d.idx for hb in hbonds_ldon+hbonds_pdon]
+        donor_atoms_hbonds = [hb.d.idx for hb in hbonds_ldon + hbonds_pdon]
         wb_dict = {}
         wb_dict2 = {}
+        omega = 110.0
 
         # Just one hydrogen bond per donor atom
         for wbridge in [wb for wb in wbridges if wb.d.idx not in donor_atoms_hbonds]:
             if (wbridge.water.idx, wbridge.a.idx) not in wb_dict:
                 wb_dict[(wbridge.water.idx, wbridge.a.idx)] = wbridge
             else:
-                if abs(110.0-wb_dict[(wbridge.water.idx, wbridge.a.idx)].w_angle) < abs(110.0-wbridge.w_angle):
+                if abs(omega - wb_dict[(wbridge.water.idx, wbridge.a.idx)].w_angle) < abs(omega - wbridge.w_angle):
                     wb_dict[(wbridge.water.idx, wbridge.a.idx)] = wbridge
         for wb_tuple in wb_dict:
             water, acceptor = wb_tuple
             if water not in wb_dict2:
-                wb_dict2[water] = [(abs(110.0-wb_dict[wb_tuple].w_angle), wb_dict[wb_tuple]), ]
+                wb_dict2[water] = [(abs(omega - wb_dict[wb_tuple].w_angle), wb_dict[wb_tuple]), ]
             elif len(wb_dict2[water]) == 1:
-                wb_dict2[water].append((abs(110.0-wb_dict[wb_tuple].w_angle), wb_dict[wb_tuple]))
+                wb_dict2[water].append((abs(omega - wb_dict[wb_tuple].w_angle), wb_dict[wb_tuple]))
                 wb_dict2[water] = sorted(wb_dict2[water])
             else:
-                if wb_dict2[water][1][0] < abs(110.0-wb_dict[wb_tuple].w_angle):
+                if wb_dict2[water][1][0] < abs(omega - wb_dict[wb_tuple].w_angle):
                     wb_dict2[water] = [wb_dict2[water][0], (wb_dict[wb_tuple].w_angle, wb_dict[wb_tuple])]
 
         filtered_wb = []
@@ -354,43 +730,51 @@ class PLInteraction():
 
 
 class BindingSite(Mol):
-    def __init__(self, atoms, protcomplex, cclass, altconf):
+    def __init__(self, atoms, protcomplex, cclass, altconf, min_dist, mapper):
         """Find all relevant parts which could take part in interactions"""
-        Mol.__init__(self, altconf)
+        Mol.__init__(self, altconf, mapper, mtype='protein', bsid=None)
         self.complex = cclass
         self.full_mol = protcomplex
         self.all_atoms = atoms
+        self.min_dist = min_dist  # Minimum distance of bs res to ligand
+        self.bs_res = list(set([''.join([str(whichresnumber(a)), whichchain(a)]) for a in self.all_atoms]))  # e.g. 47A
         self.rings = self.find_rings(self.full_mol, self.all_atoms)
         self.hydroph_atoms = self.hydrophobic_atoms(self.all_atoms)
         self.hbond_acc_atoms = self.find_hba(self.all_atoms)
         self.hbond_don_atom_pairs = self.find_hbd(self.all_atoms, self.hydroph_atoms)
         self.charged = self.find_charged(self.full_mol)
         self.halogenbond_acc = self.find_hal(self.all_atoms)
+        self.metal_binding = self.find_metal_binding(self.full_mol)
 
     def find_hal(self, atoms):
         """Look for halogen bond acceptors (Y-{O|P|N|S}, with Y=C,P,S)"""
-        data = namedtuple('hal_acceptor', 'o y')
+        data = namedtuple('hal_acceptor', 'o o_orig_idx y y_orig_idx')
         a_set = []
         # All oxygens, nitrogen, sulfurs with neighboring carbon, phosphor, nitrogen or sulfur
         for a in [at for at in atoms if at.atomicnum in [8, 7, 16]]:
             n_atoms = [na for na in pybel.ob.OBAtomAtomIter(a.OBAtom) if na.GetAtomicNum() in [6, 7, 15, 16]]
             if len(n_atoms) == 1:  # Proximal atom
-                a_set.append(data(o=a, y=pybel.Atom(n_atoms[0])))
+                o_orig_idx = self.Mapper.mapid(a.idx, mtype=self.mtype, bsid=self.bsid)
+                y_orig_idx = self.Mapper.mapid(n_atoms[0].GetIdx(), mtype=self.mtype, bsid=self.bsid)
+                a_set.append(data(o=a, o_orig_idx=o_orig_idx, y=pybel.Atom(n_atoms[0]), y_orig_idx=y_orig_idx))
         return a_set
 
     def find_charged(self, mol):
         """Looks for positive charges in arginine, histidine or lysine, for negative in aspartic and glutamic acid."""
-        data = namedtuple('pcharge', 'atoms type center restype resnr reschain')
+        data = namedtuple('pcharge', 'atoms atoms_orig_idx type center restype resnr reschain')
         a_set = []
         for res in pybel.ob.OBResidueIter(mol.OBMol):
             a_contributing = []
+            a_contributing_orig_idx = []
             if res.GetName() in ('ARG', 'HIS', 'LYS'):  # Arginine, Histidine or Lysine have charged sidechains
                 for a in pybel.ob.OBResidueAtomIter(res):
                     if a.GetType().startswith('N') and res.GetAtomProperty(a, 8) \
-                            and not self.complex.idx_to_pdb_mapping[a.GetIdx()] in self.altconf:
+                            and not self.Mapper.mapid(a.GetIdx(), mtype='protein') in self.altconf:
                         a_contributing.append(pybel.Atom(a))
+                        a_contributing_orig_idx.append(self.Mapper.mapid(a.GetIdx(), mtype='protein'))
                 if not len(a_contributing) == 0:
                     a_set.append(data(atoms=a_contributing,
+                                      atoms_orig_idx=a_contributing_orig_idx,
                                       type='positive',
                                       center=centroid([ac.coords for ac in a_contributing]),
                                       restype=res.GetName(),
@@ -399,10 +783,12 @@ class BindingSite(Mol):
             if res.GetName() in ('GLU', 'ASP'):  # Aspartic or Glutamic Acid
                 for a in pybel.ob.OBResidueAtomIter(res):
                     if a.GetType().startswith('O') and res.GetAtomProperty(a, 8) \
-                            and not self.complex.idx_to_pdb_mapping[a.GetIdx()] in self.altconf:
+                            and not self.Mapper.mapid(a.GetIdx(), mtype='protein') in self.altconf:
                         a_contributing.append(pybel.Atom(a))
+                        a_contributing_orig_idx.append(self.Mapper.mapid(a.GetIdx(), mtype='protein'))
                 if not len(a_contributing) == 0:
                     a_set.append(data(atoms=a_contributing,
+                                      atoms_orig_idx=a_contributing_orig_idx,
                                       type='negative',
                                       center=centroid([ac.coords for ac in a_contributing]),
                                       restype=res.GetName(),
@@ -410,36 +796,96 @@ class BindingSite(Mol):
                                       reschain=res.GetChain()))
         return a_set
 
+    def find_metal_binding(self, mol):
+        """Looks for atoms that could possibly be involved in chelating a metal ion.
+        This can be any main chain oxygen atom or oxygen, nitrogen and sulfur from specific amino acids"""
+        data = namedtuple('metal_binding', 'atom atom_orig_idx type restype resnr reschain location')
+        a_set = []
+        for res in pybel.ob.OBResidueIter(mol.OBMol):
+            restype, reschain, resnr = res.GetName().upper(), res.GetChain(), res.GetNum()
+            if restype in ['ASP', 'GLU', 'SER', 'THR', 'TYR']:  # Look for oxygens here
+                for a in pybel.ob.OBResidueAtomIter(res):
+                    if a.GetType().startswith('O') and res.GetAtomProperty(a, 8) \
+                            and not self.Mapper.mapid(a.GetIdx(), mtype='protein') in self.altconf:
+                        atom_orig_idx = self.Mapper.mapid(a.GetIdx(), mtype=self.mtype, bsid=self.bsid)
+                        a_set.append(data(atom=pybel.Atom(a), atom_orig_idx=atom_orig_idx, type='O', restype=restype,
+                                          resnr=resnr, reschain=reschain,
+                                          location='protein.sidechain'))
+            if restype == 'HIS':  # Look for nitrogen here
+                for a in pybel.ob.OBResidueAtomIter(res):
+                    if a.GetType().startswith('N') and res.GetAtomProperty(a, 8) \
+                            and not self.Mapper.mapid(a.GetIdx(), mtype='protein') in self.altconf:
+                        atom_orig_idx = self.Mapper.mapid(a.GetIdx(), mtype=self.mtype, bsid=self.bsid)
+                        a_set.append(data(atom=pybel.Atom(a), atom_orig_idx=atom_orig_idx, type='N', restype=restype,
+                                          resnr=resnr, reschain=reschain,
+                                          location='protein.sidechain'))
+            if restype == 'CYS':  # Look for sulfur here
+                for a in pybel.ob.OBResidueAtomIter(res):
+                    if a.GetType().startswith('S') and res.GetAtomProperty(a, 8) \
+                            and not self.Mapper.mapid(a.GetIdx(), mtype='protein') in self.altconf:
+                        atom_orig_idx = self.Mapper.mapid(a.GetIdx(), mtype=self.mtype, bsid=self.bsid)
+                        a_set.append(data(atom=pybel.Atom(a), atom_orig_idx=atom_orig_idx, type='S', restype=restype,
+                                          resnr=resnr, reschain=reschain,
+                                          location='protein.sidechain'))
+            for a in pybel.ob.OBResidueAtomIter(res):  # All main chain oxygens
+                if a.GetType().startswith('O') and res.GetAtomProperty(a, 2) \
+                        and not self.Mapper.mapid(a.GetIdx(), mtype='protein') in self.altconf and restype != 'HOH':
+                    atom_orig_idx = self.Mapper.mapid(a.GetIdx(), mtype=self.mtype, bsid=self.bsid)
+                    a_set.append(data(atom=pybel.Atom(a), atom_orig_idx=atom_orig_idx, type='O', restype=res.GetName(),
+                                      resnr=res.GetNum(), reschain=res.GetChain(),
+                                      location='protein.mainchain'))
+        return a_set
+
 
 class Ligand(Mol):
-    def __init__(self, lig, cclass, mapping, water, altconf, members):
-        Mol.__init__(self, altconf)
+    def __init__(self, cclass, ligand):
+        altconf = cclass.altconf
+        self.hetid, self.chain, self.position = ligand.hetid, ligand.chain, ligand.position
+        self.bsid = ':'.join([self.hetid, self.chain, str(self.position)])
+        Mol.__init__(self, altconf, cclass.Mapper, mtype='ligand', bsid=self.bsid)
+        self.members = ligand.members
+        self.longname = ligand.longname
+        self.type = ligand.type
         self.complex = cclass
-        self.molecule = lig
-        self.name = lig.title
-        self.all_atoms = lig.atoms
+        self.molecule = ligand.mol  # Pybel Molecule
+        self.smiles = self.molecule.write(format='can')  # SMILES String
+        self.can_to_pdb = ligand.can_to_pdb
+        if not len(self.smiles) == 0:
+            self.smiles = self.smiles.split()[0]
+        else:
+            message('[Warning] Could not write SMILES for this ligand.\n', indent=True)
+            self.smiles = ''
+        self.heavy_atoms = self.molecule.OBMol.NumHvyAtoms()  # Heavy atoms count
+        self.all_atoms = self.molecule.atoms
         self.atmdict = {l.idx: l for l in self.all_atoms}
         self.rings = self.find_rings(self.molecule, self.all_atoms)
         self.hydroph_atoms = self.hydrophobic_atoms(self.all_atoms)
         self.hbond_acc_atoms = self.find_hba(self.all_atoms)
+        self.num_rings = len(self.rings)
+        if self.num_rings != 0:
+            message('Contains %i aromatic ring(s).\n' % self.num_rings, indent=True)
+        descvalues = self.molecule.calcdesc()
+        self.molweight, self.logp = float(descvalues['MW']), float(descvalues['logP'])
+        self.num_rot_bonds = int(self.molecule.OBMol.NumRotors())
+        self.atomorder = ligand.atomorder
 
         ##########################################################
         # Special Case for hydrogen bond acceptor identification #
         ##########################################################
 
-        self.inverse_mapping = {v: k for k, v in mapping.items()}
-        self.pdb_to_idx_mapping = {v: k for k, v in cclass.idx_to_pdb_mapping.items()}
+        self.inverse_mapping = {v: k for k, v in self.Mapper.ligandmaps[self.bsid].items()}
+        self.pdb_to_idx_mapping = {v: k for k, v in self.Mapper.proteinmap.items()}
         self.hbond_don_atom_pairs = self.find_hbd(self.all_atoms, self.hydroph_atoms)
 
         ######
         donor_pairs = []
-        data = namedtuple('hbonddonor', 'd h type')
+        data = namedtuple('hbonddonor', 'd d_orig_idx h type')
         for donor in self.all_atoms:
-            pdbidx = cclass.idx_to_pdb_mapping[mapping[donor.idx]]  # Work with protonated atoms for HBD search
+            pdbidx = self.Mapper.mapid(donor.idx, mtype='ligand', bsid=self.bsid, to='original')
             d = cclass.atoms[self.pdb_to_idx_mapping[pdbidx]]
             if d.OBAtom.IsHbondDonor():
                 for adj_atom in [a for a in pybel.ob.OBAtomAtomIter(d.OBAtom) if a.IsHbondDonorH()]:
-                    donor_pairs.append(data(d=donor, h=pybel.Atom(adj_atom), type='regular'))
+                    donor_pairs.append(data(d=donor, d_orig_idx=pdbidx, h=pybel.Atom(adj_atom), type='regular'))
         self.hbond_don_atom_pairs = donor_pairs
         #######
 
@@ -447,8 +893,8 @@ class Ligand(Mol):
         self.centroid = centroid([a.coords for a in self.all_atoms])
         self.max_dist_to_center = max((euclidean3d(self.centroid, a.coords) for a in self.all_atoms))
         self.water = []
-        self.members = members
-        for hoh in water:
+        data = namedtuple('water', 'oxy oxy_orig_idx')
+        for hoh in ligand.water:
             oxy = None
             for at in pybel.ob.OBResidueAtomIter(hoh):
                 if at.GetAtomicNum() == 8 and at.GetIdx() not in self.altconf:
@@ -456,77 +902,208 @@ class Ligand(Mol):
             # There are some cases where there is no oxygen in a water residue, ignore those
             if not set([at.GetAtomicNum() for at in pybel.ob.OBResidueAtomIter(hoh)]) == {1} and oxy is not None:
                 if euclidean3d(self.centroid, oxy.coords) < self.max_dist_to_center + config.BS_DIST:
-                    self.water.append(oxy)
-        s = lig.title.split('-')
-        data = namedtuple('pymol_data', 'hetid chain resid maptopdb bs_id')
-        self.pymol_data = data(hetid=s[0], chain=s[1], resid=s[2], maptopdb=mapping, bs_id=s)
+                    oxy_orig_idx = self.Mapper.mapid(oxy.idx, mtype='protein')
+                    self.water.append(data(oxy=oxy, oxy_orig_idx=oxy_orig_idx))
         self.halogenbond_don = self.find_hal(self.all_atoms)
+        self.metal_binding = self.find_metal_binding(self.all_atoms, self.water)
+        self.metals = []
+        data = namedtuple('metal', 'm m_orig_idx')
+        for a in [a for a in self.all_atoms if a.type.upper() in config.METAL_IONS]:
+            self.metals.append(data(m=a, m_orig_idx=self.Mapper.mapid(a.idx, mtype=self.mtype, bsid=self.bsid)))
+        self.num_hba, self.num_hbd = len(self.hbond_acc_atoms), len(self.hbond_don_atom_pairs)
+        self.num_hal = len(self.halogenbond_don)
+
+    def get_canonical_num(self, atomnum):
+        """Converts internal atom ID into canonical atom ID. Agrees with Canonical SMILES in XML."""
+        return self.atomorder[atomnum-1]
+
+
+    def is_functional_group(self, atom, group):
+        """Given a pybel atom, look up if it belongs to a function group"""
+        n_atoms = [a_neighbor.GetAtomicNum() for a_neighbor in pybel.ob.OBAtomAtomIter(atom.OBAtom)]
+
+        if group in ['quartamine', 'tertamine'] and atom.atomicnum == 7:  # Nitrogen
+            # It's a nitrogen, so could be a protonated amine or quaternary ammonium
+            if '1' not in n_atoms and len(n_atoms) == 4:
+                return True if group == 'quartamine' else False  # It's a quat. ammonium (N with 4 residues != H)
+            elif atom.OBAtom.GetHyb() == 3 and len(n_atoms) >= 3:
+                return True if group == 'tertamine' else False  # It's sp3-hybridized, so could pick up an hydrogen
+            else:
+                return False
+
+        if group in ['sulfonium', 'sulfonicacid', 'sulfate'] and atom.atomicnum == 16:  # Sulfur
+            if '1' not in n_atoms and len(n_atoms) == 3:  # It's a sulfonium (S with 3 residues != H)
+                return True if group == 'sulfonium' else False
+            elif n_atoms.count(8) == 3:  # It's a sulfonate or sulfonic acid
+                return True if group == 'sulfonicacid' else False
+            elif n_atoms.count(8) == 4:  # It's a sulfate
+                return True if group == 'sulfate' else False
+
+        if group == 'phosphate' and atom.atomicnum == 15:  # Phosphor
+            if set(n_atoms) == {8}:  # It's a phosphate
+                return True
+
+        if group in ['carboxylate', 'guanidine'] and atom.atomicnum == 6:  # It's a carbon atom
+            if n_atoms.count(8) == 2 and n_atoms.count(6) == 1:  # It's a carboxylate group
+                return True if group == 'carboxylate' else False
+            elif n_atoms.count(7) == 3 and len(n_atoms) == 3:  # It's a guanidine group
+                nitro_partners = []
+                for nitro in pybel.ob.OBAtomAtomIter(atom.OBAtom):
+                    nitro_partners.append(len([b_neighbor for b_neighbor in pybel.ob.OBAtomAtomIter(nitro)]))
+                if min(nitro_partners) == 1:  # One nitrogen is only connected to the carbon, can pick up a H
+                    return True if group == 'guanidine' else False
+
+        if group == 'halocarbon' and atom.atomicnum in [9, 17, 35, 53]:  # Halogen atoms
+            n_atoms = [na for na in pybel.ob.OBAtomAtomIter(atom.OBAtom) if na.GetAtomicNum() == 6]
+            if len(n_atoms) == 1:  # Halocarbon
+                return True
+        else:
+            return False
 
     def find_hal(self, atoms):
         """Look for halogen bond donors (X-C, with X=F, Cl, Br, I)"""
-        data = namedtuple('hal_donor', 'x c')
+        data = namedtuple('hal_donor', 'x x_orig_idx c c_orig_idx')
         a_set = []
-        for a in [at for at in atoms if at.atomicnum in [9, 17, 35, 53]]:  # All halogens bound to carbon
-            n_atoms = [na for na in pybel.ob.OBAtomAtomIter(a.OBAtom) if na.GetAtomicNum() == 6]
-            if len(n_atoms) == 1:  # Proximal halogen
-                a_set.append(data(x=a, c=pybel.Atom(n_atoms[0])))
+        for a in atoms:
+            if self.is_functional_group(a, 'halocarbon'):
+                n_atoms = [na for na in pybel.ob.OBAtomAtomIter(a.OBAtom) if na.GetAtomicNum() == 6]
+                x_orig_idx = self.Mapper.mapid(a.idx, mtype=self.mtype, bsid=self.bsid)
+                c_orig_idx = [self.Mapper.mapid(na.GetIdx(), mtype=self.mtype, bsid=self.bsid) for na in n_atoms]
+                a_set.append(data(x=a, x_orig_idx=x_orig_idx, c=pybel.Atom(n_atoms[0]), c_orig_idx=c_orig_idx))
+        if len(a_set) != 0:
+            message('Ligand contains %i halogen atom(s).\n' % len(a_set), indent=True)
         return a_set
 
     def find_charged(self, all_atoms):
         """Identify all positively charged groups in a ligand. This search is not exhaustive, as the cases can be quite
         diverse. The typical cases seem to be protonated amines, quaternary ammoinium and sulfonium
-        as mentioned in 'Cation-pi pliprofiler in ligand recognition and catalysis' (Zacharias et al., 2002)).
+        as mentioned in 'Cation-pi interactions in ligand recognition and catalysis' (Zacharias et al., 2002)).
         Identify negatively charged groups in the ligand.
         """
-        data = namedtuple('lcharge', 'atoms type center fgroup')
+        data = namedtuple('lcharge', 'atoms atoms_orig_idx type center fgroup')
         a_set = []
         for a in all_atoms:
-            if a.atomicnum == 7:  # It's a nitrogen, so could be a protonated amine or quaternary ammonium
-                n_atoms = [a_neighbor.GetAtomicNum() for a_neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
-                if '1' not in n_atoms and len(n_atoms) == 4:  # It's a quaternary ammonium (N with 4 residues != H)
-                    a_set.append(data(atoms=[a, ], type='positive', center=list(a.coords), fgroup='quartamine'))
-                elif a.OBAtom.GetHyb() == 3 and len(n_atoms) >= 3:  # It's sp3-hybridized, so could pick up an hydrogen
-                    a_set.append(data(atoms=[a, ], type='positive', center=list(a.coords), fgroup='tertamine'))
-            if a.atomicnum == 16:  # It's a sulfur
-                n_atoms = [a_neighbor.GetAtomicNum() for a_neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
-                if '1' not in n_atoms and len(n_atoms) == 3:  # It's a sulfonium (S with 3 residues != H)
-                    a_set.append(data(atoms=[a, ], type='positive', center=list(a.coords), fgroup='sulfonium'))
+            a_orig_idx = self.Mapper.mapid(a.idx, mtype=self.mtype, bsid=self.bsid)
+            if self.is_functional_group(a, 'quartamine'):
+                a_set.append(data(atoms=[a, ], atoms_orig_idx=[a_orig_idx, ], type='positive',
+                                  center=list(a.coords), fgroup='quartamine'))
+            elif self.is_functional_group(a, 'tertamine'):
+                a_set.append(data(atoms=[a, ], atoms_orig_idx=[a_orig_idx, ], type='positive', center=list(a.coords),
+                                  fgroup='tertamine'))
+            if self.is_functional_group(a, 'sulfonium'):
+                a_set.append(data(atoms=[a, ], atoms_orig_idx=[a_orig_idx, ], type='positive', center=list(a.coords),
+                                  fgroup='sulfonium'))
+            if self.is_functional_group(a, 'phosphate'):
+                a_contributing = [a, ]
+                a_contributing_orig_idx = [a_orig_idx, ]
+                [a_contributing.append(pybel.Atom(neighbor)) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
+                [a_contributing_orig_idx.append(self.Mapper.mapid(neighbor.idx, mtype=self.mtype, bsid=self.bsid))
+                 for neighbor in a_contributing]
+                a_set.append(data(atoms=a_contributing, atoms_orig_idx=a_contributing_orig_idx, type='negative',
+                                  center=a.coords, fgroup='phosphate'))
+            if self.is_functional_group(a, 'sulfonicacid'):
+                a_contributing = [a, ]
+                a_contributing_orig_idx = [a_orig_idx, ]
+                [a_contributing.append(pybel.Atom(neighbor)) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom) if
+                 neighbor.GetAtomicNum() == 8]
+                [a_contributing_orig_idx.append(self.Mapper.mapid(neighbor.idx, mtype=self.mtype, bsid=self.bsid))
+                 for neighbor in a_contributing]
+                a_set.append(data(atoms=a_contributing, atoms_orig_idx=a_contributing_orig_idx, type='negative',
+                                  center=a.coords, fgroup='sulfonicacid'))
+            elif self.is_functional_group(a, 'sulfate'):
+                a_contributing = [a, ]
+                a_contributing_orig_idx = [a_orig_idx, ]
+                [a_contributing_orig_idx.append(self.Mapper.mapid(neighbor.idx, mtype=self.mtype, bsid=self.bsid))
+                 for neighbor in a_contributing]
+                [a_contributing.append(pybel.Atom(neighbor)) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
+                a_set.append(data(atoms=a_contributing, atoms_orig_idx=a_contributing_orig_idx, type='negative',
+                                  center=a.coords, fgroup='sulfate'))
+            if self.is_functional_group(a, 'carboxylate'):
+                a_contributing = [pybel.Atom(neighbor) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)
+                                  if neighbor.GetAtomicNum() == 8]
+                a_contributing_orig_idx = [self.Mapper.mapid(neighbor.idx, mtype=self.mtype, bsid=self.bsid)
+                                           for neighbor in a_contributing]
+                a_set.append(data(atoms=a_contributing, atoms_orig_idx=a_contributing_orig_idx, type='negative',
+                                  center=centroid([a.coords for a in a_contributing]), fgroup='carboxylate'))
+            elif self.is_functional_group(a, 'guanidine'):
+                a_contributing = [pybel.Atom(neighbor) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)
+                                  if neighbor.GetAtomicNum() == 7]
+                a_contributing_orig_idx = [self.Mapper.mapid(neighbor.idx, mtype=self.mtype, bsid=self.bsid)
+                                           for neighbor in a_contributing]
+                a_set.append(data(atoms=a_contributing, atoms_orig_idx=a_contributing_orig_idx, type='positive',
+                                  center=a.coords, fgroup='guanidine'))
+        return a_set
+
+    def find_metal_binding(self, lig_atoms, water_oxygens):
+        """Looks for atoms that could possibly be involved in binding a metal ion.
+        This can be any water oxygen, as well as oxygen from carboxylate, phophoryl, phenolate, alcohol;
+        nitrogen from imidazole; sulfur from thiolate.
+        """
+        a_set = []
+        data = namedtuple('metal_binding', 'atom atom_orig_idx type fgroup restype resnr reschain location')
+        for oxygen in water_oxygens:
+            a_set.append(data(atom=oxygen.oxy, atom_orig_idx=oxygen.oxy_orig_idx, type='O', fgroup='water',
+                              restype=whichrestype(oxygen.oxy), resnr=whichresnumber(oxygen.oxy),
+                              reschain=whichchain(oxygen.oxy), location='water'))
+        # #@todo Refactor code
+        for a in lig_atoms:
+            a_orig_idx = self.Mapper.mapid(a.idx, mtype='ligand', bsid=self.bsid)
+            n_atoms = pybel.ob.OBAtomAtomIter(a.OBAtom)  # Neighboring atoms
+            # All atomic numbers of neighboring atoms
+            n_atoms_atomicnum = [n.GetAtomicNum() for n in pybel.ob.OBAtomAtomIter(a.OBAtom)]
+            if a.atomicnum == 8:  # Oxygen
+                if n_atoms_atomicnum.count('1') == 1 and len(n_atoms_atomicnum) == 2:  # Oxygen in alcohol (R-[O]-H)
+                    a_set.append(data(atom=a, atom_orig_idx=a_orig_idx, type='O', fgroup='alcohol',
+                                      restype=self.hetid, resnr=self.position, reschain=self.chain,
+                                      location='ligand'))
+                if True in [n.IsAromatic() for n in n_atoms] and not a.OBAtom.IsAromatic():  # Phenolate oxygen
+                    a_set.append(data(atom=a, atom_orig_idx=a_orig_idx, type='O', fgroup='phenolate',
+                                      restype=self.hetid, resnr=self.position, reschain=self.chain,
+                                      location='ligand'))
+            if a.atomicnum == 6:  # It's a carbon atom
+                if n_atoms_atomicnum.count(8) == 2 and n_atoms_atomicnum.count(6) == 1:  # It's a carboxylate group
+                    for neighbor in [n for n in n_atoms if n.GetAtomicNum() == 8]:
+                        neighbor_orig_idx = self.Mapper.mapid(neighbor.GetIdx(), mtype='ligand', bsid=self.bsid)
+                        a_set.append(data(atom=pybel.Atom(neighbor), atom_orig_idx=neighbor_orig_idx, type='O',
+                                          fgroup='carboxylate',
+                                          restype=self.hetid,
+                                          resnr=self.position, reschain=self.chain,
+                                          location='ligand'))
             if a.atomicnum == 15:  # It's a phosphor atom
-                n_atoms = [a_neighbor.GetAtomicNum() for a_neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
-                if set(n_atoms) == {8}:  # It's a phosphate
-                    a_contributing = [a, ]
-                    [a_contributing.append(pybel.Atom(neighbor)) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
-                    a_set.append(data(atoms=a_contributing, type='negative', center=a.coords, fgroup='phosphate'))
+                if n_atoms_atomicnum.count(8) >= 3:  # It's a phosphoryl
+                    for neighbor in [n for n in n_atoms if n.GetAtomicNum() == 8]:
+                        neighbor_orig_idx = self.Mapper.mapid(neighbor.GetIdx(), mtype='ligand', bsid=self.bsid)
+                        a_set.append(data(atom=pybel.Atom(neighbor), atom_orig_idx=neighbor_orig_idx, type='O',
+                                          fgroup='phosphoryl',
+                                          restype=self.hetid,
+                                          resnr=self.position, reschain=self.chain,
+                                          location='ligand'))
+                if n_atoms_atomicnum.count(8) == 2:  # It's another phosphor-containing group #@todo (correct name?)
+                    for neighbor in [n for n in n_atoms if n.GetAtomicNum() == 8]:
+                        neighbor_orig_idx = self.Mapper.mapid(neighbor.GetIdx(), mtype='ligand', bsid=self.bsid)
+                        a_set.append(data(atom=pybel.Atom(neighbor), atom_orig_idx=neighbor_orig_idx, type='O',
+                                          fgroup='phosphor.other', restype=self.hetid,
+                                          resnr=self.position,
+                                          reschain=self.chain, location='ligand'))
+            if a.atomicnum == 7:  # It's a nitrogen atom
+                if n_atoms_atomicnum.count(6) == 2:  # It's imidazole/pyrrole or similar
+                    a_set.append(data(atom=a, atom_orig_idx=a_orig_idx, type='N', fgroup='imidazole/pyrrole',
+                                      restype=self.hetid, resnr=self.position, reschain=self.chain,
+                                      location='ligand'))
             if a.atomicnum == 16:  # It's a sulfur atom
-                n_atoms = [a_neighbor.GetAtomicNum() for a_neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
-                if n_atoms.count(8) == 3:  # It's a sulfonate or sulfonic acid
-                    a_contributing = [a, ]
-                    [a_contributing.append(pybel.Atom(neighbor)) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom) if
-                     neighbor.GetAtomicNum() == 8]
-                    a_set.append(data(atoms=a_contributing, type='negative', center=a.coords, fgroup='sulfonicacid'))
-                elif n_atoms.count(8) == 4:  # It's a sulfate
-                    a_contributing = [a, ]
-                    [a_contributing.append(pybel.Atom(neighbor)) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
-                    a_set.append(data(atoms=a_contributing, type='negative', center=a.coords, fgroup='sulfate'))
-            if a.atomicnum == 6:  # It's a carbon atom
-                n_atoms = [a_neighbor.GetAtomicNum() for a_neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)]
-                if n_atoms.count(8) == 2 and n_atoms.count(6) == 1:  # It's a carboxylate group
-                    a_contributing = [pybel.Atom(neighbor) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)
-                                      if neighbor.GetAtomicNum() == 8]
-                    a_set.append(data(atoms=a_contributing, type='negative',
-                                      center=centroid([a.coords for a in a_contributing]), fgroup='carboxylate'))
-                if n_atoms.count(7) == 3 and len(n_atoms) == 3:  # It's a guanidine group
-                    nitro_partners = []
-                    for nitro in pybel.ob.OBAtomAtomIter(a.OBAtom):
-                        nitro_partners.append(len([b_neighbor for b_neighbor in pybel.ob.OBAtomAtomIter(nitro)]))
-                    if min(nitro_partners) == 1:  # One nitrogen is only connected to the carbon, can pick up a H
-                        a_contributing = [pybel.Atom(neighbor) for neighbor in pybel.ob.OBAtomAtomIter(a.OBAtom)
-                                          if neighbor.GetAtomicNum() == 7]
-                        a_set.append(data(atoms=a_contributing, type='positive', center=a.coords, fgroup='guanidine'))
+                if True in [n.IsAromatic() for n in n_atoms] and not a.OBAtom.IsAromatic():  # Thiolate
+                    a_set.append(data(atom=a, atom_orig_idx=a_orig_idx, type='S', fgroup='thiolate',
+                                      restype=self.hetid, resnr=self.position, reschain=self.chain,
+                                      location='ligand'))
+                if set(n_atoms_atomicnum) == {26}:  # Sulfur in Iron sulfur cluster
+                    a_set.append(data(atom=a, atom_orig_idx=a_orig_idx, type='S', fgroup='iron-sulfur.cluster',
+                                      restype=self.hetid, resnr=self.position, reschain=self.chain,
+                                      location='ligand'))
+
         return a_set
 
 
-class PDBComplex():
+class PDBComplex:
     """Contains a collection of objects associated with a PDB complex, i.e. one or several ligands and their binding
     sites as well as information about the pliprofiler between them. Provides functions to load and prepare input files
     such as PDB files.
@@ -535,59 +1112,139 @@ class PDBComplex():
     def __init__(self):
         self.interaction_sets = {}  # Dictionary with site identifiers as keys and object as value
         self.protcomplex = None
+        self.filetype = None
         self.atoms = {}  # Dictionary of Pybel atoms, accessible by their idx
         self.sourcefiles = {}
+        self.information = {}
+        self.corrected_pdb = ''
         self.output_path = '/tmp'
         self.pymol_name = None
-        self.idx_to_pdb_mapping = {}
         self.modres = set()
+        self.resis = []
         self.altconf = []  # Atom idx of atoms with alternate conformations
         self.covalent = []  # Covalent linkages between ligands and protein residues/other ligands
         self.excluded = []  # Excluded ligands
+        self.Mapper = Mapper()
+        self.ligands = []
 
     def load_pdb(self, pdbpath):
         """Loads a pdb file with protein AND ligand(s), separates and prepares them."""
+        self.sourcefiles['pdbcomplex.original'] = pdbpath
         self.sourcefiles['pdbcomplex'] = pdbpath
-        self.protcomplex = read_pdb(pdbpath, safe=False)  # Don't do safe reading
-        # Counting is different from PDB if TER records present
-        self.idx_to_pdb_mapping, self.modres, self.covalent = parse_pdb(open(tilde_expansion(pdbpath)).readlines())
-        # #@todo Include this in the parse_pdb function, return named tuple?
-        self.altconf = get_altconf_atoms(open(tilde_expansion(pdbpath)).readlines())
-        try:
-            self.pymol_name = self.protcomplex.data['HEADER'][56:60].lower()  # Get name from HEADER data
-        except KeyError:  # Extract the PDBID from the filename
-            self.pymol_name = extract_pdbid(pdbpath.split('/')[-1])
+        self.information['pdbfixes'] = False
+        pdbparser = PDBParser(pdbpath)  # Parse PDB file to find errors and get additonal data
+        # #@todo Refactor and rename here
+        self.Mapper.proteinmap = pdbparser.proteinmap
+        self.modres = pdbparser.modres
+        self.covalent = pdbparser.covalent
+        self.altconf = pdbparser.altconformations
+        self.corrected_pdb = pdbparser.corrected_pdb
+
+        if pdbparser.num_fixed_lines > 0:
+            message('%i lines automatically fixed in PDB input file.\n' % pdbparser.num_fixed_lines)
+            # Save modified PDB file
+            basename = os.path.basename(pdbpath).split('.')[0]
+            pdbpath_fixed = tmpfile(prefix='plipfixed.' + basename + '_', direc=self.output_path)
+            create_folder_if_not_exists(self.output_path)
+            self.sourcefiles['pdbcomplex'] = pdbpath_fixed
+            self.corrected_pdb = re.sub(r'[^\x00-\x7F]+', ' ', self.corrected_pdb)  # Strip non-unicode chars
+            with open(pdbpath_fixed, 'w') as f:
+                f.write(self.corrected_pdb)
+            self.information['pdbfixes'] = True
+
+        self.sourcefiles['filename'] = os.path.basename(self.sourcefiles['pdbcomplex'])
+        self.protcomplex, self.filetype = read_pdb(self.sourcefiles['pdbcomplex'])
+        message('PDB structure successfully read.\n')
+
+        # Determine (temporary) PyMOL Name from Filename
+        self.pymol_name = pdbpath.split('/')[-1].split('.')[0] + '-Protein'
+        # Replace characters causing problems in PyMOL
+        self.pymol_name = self.pymol_name.replace(' ', '').replace('(', '').replace(')', '').replace('-','_')
+        # But if possible, name it after PDBID in Header
+        if 'HEADER' in self.protcomplex.data:  # If the PDB file has a proper header
+            potential_name = self.protcomplex.data['HEADER'][56:60].lower()
+            if extract_pdbid(potential_name) != 'UnknownProtein':
+                self.pymol_name = potential_name
+        debuglog("Pymol Name set as: '%s'" % self.pymol_name)
+
         self.protcomplex.OBMol.AddPolarHydrogens()
         for atm in self.protcomplex:
             self.atoms[atm.idx] = atm
-        ligands, excluded = getligs(self.protcomplex, self.altconf, self.idx_to_pdb_mapping, self.modres, self.covalent)
-        self.excluded = excluded
-        resis = [obres for obres in pybel.ob.OBResidueIter(self.protcomplex.OBMol) if obres.GetResidueProperty(0)]
-        for ligand in ligands:
-            lig_obj = Ligand(ligand.mol, self, ligand.mapping, ligand.water, self.altconf, ligand.members)
-            cutoff = lig_obj.max_dist_to_center + config.BS_DIST
-            bs_res = self.extract_bs(cutoff, lig_obj.centroid, resis)
-            # Get a list of all atoms belonging to the binding site, search by idx
-            bs_atoms = [self.atoms[idx] for idx in [i for i in self.atoms.keys()
-                                                    if self.atoms[i].OBAtom.GetResidue().GetIdx() in bs_res]
-                        if idx in self.idx_to_pdb_mapping and self.idx_to_pdb_mapping[idx] not in self.altconf]
-            bs_obj = BindingSite(bs_atoms, self.protcomplex, self, self.altconf)
-            pli_obj = PLInteraction(lig_obj, bs_obj, self)
-            self.interaction_sets[ligand.mol.title] = pli_obj
+
+        # Extract and prepare ligands
+        ligandfinder = LigandFinder(self.protcomplex, self.altconf, self.modres, self.covalent, self.Mapper)
+        self.ligands = ligandfinder.ligands
+        self.excluded = ligandfinder.excluded
+
+        if len(self.excluded) != 0:
+            message("Excluded molecules as ligands: %s\n" % ','.join([lig for lig in self.excluded]))
+
+        self.resis = [obres for obres in pybel.ob.OBResidueIter(self.protcomplex.OBMol) if obres.GetResidueProperty(0)]
+
+        num_ligs = len(self.ligands)
+        if num_ligs == 1:
+            message("Analyzing one ligand...\n")
+        elif num_ligs > 1:
+            message("Analyzing %i ligands...\n" % num_ligs)
+        else:
+            message("Structure contains no ligands.\n\n")
+
+    def characterize_complex(self, ligand):
+        """Handles all basic functions for characterizing the interactions for one ligand"""
+
+        single_sites = []
+        for member in ligand.members:
+            single_sites.append(':'.join([str(x) for x in member]))
+        site = ' + '.join(single_sites)
+        site = site if not len(site) > 20 else site[:20] + '...'
+        longname = ligand.longname if not len(ligand.longname) > 20 else ligand.longname[:20] + '...'
+        ligtype = 'Unspecified type' if ligand.type == 'UNSPECIFIED' else ligand.type
+        ligtext = "\n%s [%s] -- %s" % (longname, ligtype, site)
+        any_in_biolip = len(set([x[0] for x in ligand.members]).intersection(config.biolip_list)) != 0
+        message(ligtext)
+        message('\n' + '-' * len(ligtext) + '\n')
+
+        if ligtype not in ['POLYMER', 'DNA', 'ION', 'DNA+ION', 'RNA+ION', 'SMALLMOLECULE+ION'] and any_in_biolip:
+            message('  -> may be biologically irrelevant <-\n')
+
+        lig_obj = Ligand(self, ligand)
+        cutoff = lig_obj.max_dist_to_center + config.BS_DIST
+        bs_res = self.extract_bs(cutoff, lig_obj.centroid, self.resis)
+        # Get a list of all atoms belonging to the binding site, search by idx
+        bs_atoms = [self.atoms[idx] for idx in [i for i in self.atoms.keys()
+                                                if self.atoms[i].OBAtom.GetResidue().GetIdx() in bs_res]
+                    if idx in self.Mapper.proteinmap and self.Mapper.mapid(idx, mtype='protein') not in self.altconf]
+        bs_atoms_refined = []
+
+        # Create hash with BSRES -> (MINDIST_TO_LIG, AA_TYPE)
+        # and refine binding site atom selection with exact threshold
+        min_dist = {}
+        for r in bs_atoms:
+            bs_res_id = ''.join([str(whichresnumber(r)), whichchain(r)])
+            for l in ligand.mol.atoms:
+                distance = euclidean3d(r.coords, l.coords)
+                if bs_res_id not in min_dist:
+                    min_dist[bs_res_id] = (distance, whichrestype(r))
+                elif min_dist[bs_res_id][0] > distance:
+                    min_dist[bs_res_id] = (distance, whichrestype(r))
+                if distance <= config.BS_DIST and r not in bs_atoms_refined:
+                    bs_atoms_refined.append(r)
+        num_bs_atoms = len(bs_atoms_refined)
+        message('Binding site atoms in vicinity (%.1f A max. dist: %i).\n' % (config.BS_DIST, num_bs_atoms),
+                indent=True)
+
+        bs_obj = BindingSite(bs_atoms_refined, self.protcomplex, self, self.altconf, min_dist, self.Mapper)
+        pli_obj = PLInteraction(lig_obj, bs_obj, self)
+        self.interaction_sets[ligand.mol.title] = pli_obj
 
     def extract_bs(self, cutoff, ligcentroid, resis):
         """Return list of ids from residues belonging to the binding site"""
         return [obres.GetIdx() for obres in resis if self.res_belongs_to_bs(obres, cutoff, ligcentroid)]
 
     def res_belongs_to_bs(self, res, cutoff, ligcentroid):
-        """Do an all-vs-all comparison of ligand and residue atoms until a distance of less than bs_dist cutoff
-        is reached
-        """
-        for coo in ((atm.x(), atm.y(), atm.z()) for atm in pybel.ob.OBResidueAtomIter(res)):
-                if (abs(coo[0]-ligcentroid[0]) or abs(coo[1]-ligcentroid[1]) or abs(coo[2]-ligcentroid[2])) < cutoff:
-                    if euclidean3d(coo, ligcentroid) < cutoff:
-                        return True
-        return False
+        """Check for each residue if its centroid is within a certain distance to the ligand centroid."""
+        rescentroid = centroid([(atm.x(), atm.y(), atm.z()) for atm in pybel.ob.OBResidueAtomIter(res)])
+        return True if euclidean3d(rescentroid, ligcentroid) < cutoff else False
 
     def get_atom(self, idx):
         return self.atoms[idx]
diff --git a/plip/modules/report.py b/plip/modules/report.py
index cfa384a..a5fd480 100644
--- a/plip/modules/report.py
+++ b/plip/modules/report.py
@@ -1,7 +1,7 @@
 """
 Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
 report.py - Write PLIP results to output files.
-Copyright 2014 Sebastian Salentin
+Copyright 2014-2015 Sebastian Salentin
 
 Licensed under the Apache License, Version 2.0 (the "License");
 you may not use this file except in compliance with the License.
@@ -25,23 +25,27 @@ from operator import itemgetter
 import lxml.etree as et
 
 
-class TextOutput():
+class TextOutput:
     """Gather report data and generate reports for one binding site in different formats"""
-    def __init__(self, pli_class):
+    def __init__(self, plcomplex):
 
         ################
         # GENERAL DATA #
         ################
 
-        self.output_path = pli_class.output_path
-        self.name = pli_class.name
-        self.pdbid = pli_class.pdbid.upper()
-        self.lig_members = pli_class.lig_members
-        self.interacting_chains = pli_class.interacting_chains
-        mapping = pli_class.idx_to_pdb
-        lig_to_pdb = {key: mapping[pli_class.lig_to_pdb[key]] for key in pli_class.lig_to_pdb}  # Atom mapping ligand
-        self.header = ['#PREDICTION OF NONCOVALENT INTERACTIONS FOR %s:%s' % (self.pdbid, self.name),
-                       '#Created on %s' % time.strftime("%Y/%m/%d")]
+        self.complex = plcomplex
+        self.ligand = self.complex.ligand
+        self.bindingsite = self.complex.bindingsite
+        self.output_path = self.complex.output_path
+        self.bsid = ':'.join([self.ligand.hetid, self.ligand.chain, str(self.ligand.position)])
+        self.longname = self.ligand.longname
+        self.ligtype = self.ligand.type
+        self.bs_res = self.bindingsite.bs_res
+        self.min_dist = self.bindingsite.min_dist
+        self.bs_res_interacting = self.complex.interacting_res
+        self.pdbid = self.complex.pdbid.upper()
+        self.lig_members = self.complex.lig_members
+        self.interacting_chains = self.complex.interacting_chains
 
         ############################
         # HYDROPHOBIC INTERACTIONS #
@@ -50,10 +54,10 @@ class TextOutput():
         self.hydrophobic_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'DIST', 'LIGCARBONIDX', 'PROTCARBONIDX', 'LIGCOO',
                                      'PROTCOO')
         self.hydrophobic_info = []
-        for hydroph in pli_class.hydrophobic_contacts:
+        for hydroph in self.complex.hydrophobic_contacts:
             self.hydrophobic_info.append((hydroph.resnr, hydroph.restype, hydroph.reschain, '%.2f' % hydroph.distance,
-                                          lig_to_pdb[hydroph.ligatom.idx], mapping[hydroph.bsatom.idx]
-                                          , hydroph.ligatom.coords, hydroph.bsatom.coords))
+                                          hydroph.ligatom_orig_idx, hydroph.bsatom_orig_idx, hydroph.ligatom.coords,
+                                          hydroph.bsatom.coords))
 
         ##################
         # HYDROGEN BONDS #
@@ -62,36 +66,29 @@ class TextOutput():
         self.hbond_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'SIDECHAIN', 'DIST_H-A', 'DIST_D-A', 'DON_ANGLE',
                                'PROTISDON', 'DONORIDX', 'DONORTYPE', 'ACCEPTORIDX', 'ACCEPTORTYPE', 'LIGCOO', 'PROTCOO')
         self.hbond_info = []
-        for hbond in pli_class.hbonds_pdon+pli_class.hbonds_ldon:
-            if hbond.protisdon:
-                donidx, accidx = mapping[hbond.d.idx], lig_to_pdb[hbond.a.idx]
-                self.hbond_info.append((hbond.resnr, hbond.restype, hbond.reschain, hbond.sidechain,
-                                        '%.2f' % hbond.distance_ah, '%.2f' % hbond.distance_ad, '%.2f' % hbond.angle,
-                                        hbond.protisdon, donidx, hbond.dtype, accidx, hbond.atype, hbond.a.coords,
-                                        hbond.d.coords))
-            else:
-                donidx, accidx = lig_to_pdb[hbond.d.idx], mapping[hbond.a.idx]
-                self.hbond_info.append((hbond.resnr, hbond.restype, hbond.reschain, hbond.sidechain,
-                                        '%.2f' % hbond.distance_ah, '%.2f' % hbond.distance_ad, '%.2f' % hbond.angle,
-                                        hbond.protisdon, donidx, hbond.dtype, accidx, hbond.atype, hbond.d.coords,
-                                        hbond.a.coords))
+        for hbond in self.complex.hbonds_pdon + self.complex.hbonds_ldon:
+            ligatom, protatom = (hbond.a, hbond.d) if hbond.protisdon else (hbond.d, hbond.a)
+            self.hbond_info.append((hbond.resnr, hbond.restype, hbond.reschain, hbond.sidechain,
+                                    '%.2f' % hbond.distance_ah, '%.2f' % hbond.distance_ad, '%.2f' % hbond.angle,
+                                    hbond.protisdon, hbond.d_orig_idx, hbond.dtype, hbond.a_orig_idx, hbond.atype,
+                                    ligatom.coords, protatom.coords))
 
         #################
         # WATER-BRIDGES #
         #################
 
         self.waterbridge_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'DIST_A-W', 'DIST_D-W', 'DON_ANGLE', 'WATER_ANGLE',
-                                     'PROTISDON', 'DONOR_IDX', 'DONORTYPE', 'ACCEPTOR_IDX', 'ACCEPTORTYPE', 'WATER_IDX')
+                                     'PROTISDON', 'DONOR_IDX', 'DONORTYPE', 'ACCEPTOR_IDX', 'ACCEPTORTYPE', 'WATER_IDX',
+                                     'LIGCOO', 'PROTCOO', 'WATERCOO')
+        # The coordinate format is an exception here, since the interaction is not only between ligand and protein
         self.waterbridge_info = []
-        for wbridge in pli_class.water_bridges:
-            if wbridge.protisdon:
-                donidx, accidx = mapping[wbridge.d.idx], lig_to_pdb[wbridge.a.idx]
-            else:
-                donidx, accidx = lig_to_pdb[wbridge.d.idx], mapping[wbridge.a.idx]
+        for wbridge in self.complex.water_bridges:
+            lig, prot = (wbridge.a, wbridge.d) if wbridge.protisdon else (wbridge.d, wbridge.a)
             self.waterbridge_info.append((wbridge.resnr, wbridge.restype, wbridge.reschain,
                                           '%.2f' % wbridge.distance_aw, '%.2f' % wbridge.distance_dw,
                                           '%.2f' % wbridge.d_angle, '%.2f' % wbridge.w_angle, wbridge.protisdon,
-                                          donidx, wbridge.dtype, accidx, wbridge.atype, mapping[wbridge.water.idx]))
+                                          wbridge.d_orig_idx, wbridge.dtype, wbridge.a_orig_idx, wbridge.atype,
+                                          wbridge.water_orig_idx, lig.coords, prot.coords, wbridge.water.coords))
 
         ################
         # SALT BRIDGES #
@@ -100,14 +97,14 @@ class TextOutput():
         self.saltbridge_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'DIST', 'PROTISPOS', 'LIG_GROUP', 'LIG_IDX_LIST',
                                     'LIGCOO', 'PROTCOO')
         self.saltbridge_info = []
-        for sb in pli_class.saltbridge_lneg+pli_class.saltbridge_pneg:
+        for sb in self.complex.saltbridge_lneg + self.complex.saltbridge_pneg:
             if sb.protispos:
-                group, ids = sb.negative.fgroup, [str(lig_to_pdb[x.idx]) for x in sb.negative.atoms]
+                group, ids = sb.negative.fgroup, [str(x) for x in sb.negative.atoms_orig_idx]
                 self.saltbridge_info.append((sb.resnr, sb.restype, sb.reschain, '%.2f' % sb.distance, sb.protispos,
                                              group.capitalize(), ",".join(ids),
                                              tuple(sb.negative.center), tuple(sb.positive.center)))
             else:
-                group, ids = sb.positive.fgroup, [str(lig_to_pdb[x.idx]) for x in sb.positive.atoms]
+                group, ids = sb.positive.fgroup, [str(x) for x in sb.positive.atoms_orig_idx]
                 self.saltbridge_info.append((sb.resnr, sb.restype, sb.reschain, '%.2f' % sb.distance, sb.protispos,
                                              group.capitalize(), ",".join(ids),
                                              tuple(sb.positive.center), tuple(sb.negative.center)))
@@ -119,11 +116,11 @@ class TextOutput():
         self.pistacking_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'CENTDIST', 'ANGLE', 'OFFSET', 'TYPE',
                                     'LIG_IDX_LIST', 'LIGCOO', 'PROTCOO')
         self.pistacking_info = []
-        for stack in pli_class.pistacking:
-            ids = [str(lig_to_pdb[x.idx]) for x in stack.ligandring.atoms]
+        for stack in self.complex.pistacking:
+            ids = [str(x) for x in stack.ligandring.atoms_orig_idx]
             self.pistacking_info.append((stack.resnr, stack.restype, stack.reschain, '%.2f' % stack.distance,
-                                         '%.2f' % stack.angle, '%.2f' % stack.offset, stack.type, ",".join(ids)
-                                         , tuple(stack.ligandring.center), tuple(stack.proteinring.center)))
+                                         '%.2f' % stack.angle, '%.2f' % stack.offset, stack.type, ",".join(ids),
+                                         tuple(stack.ligandring.center), tuple(stack.proteinring.center)))
 
         ##########################
         # PI-CATION INTERACTIONS #
@@ -132,15 +129,15 @@ class TextOutput():
         self.pication_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'DIST', 'OFFSET', 'PROTCHARGED', 'LIG_GROUP',
                                   'LIG_IDX_LIST', 'LIGCOO', 'PROTCOO')
         self.pication_info = []
-        for picat in pli_class.pication_laro+pli_class.pication_paro:
+        for picat in self.complex.pication_laro + self.complex.pication_paro:
             if picat.protcharged:
-                ids = [str(lig_to_pdb[x.idx]) for x in picat.ring.atoms]
+                ids = [str(x) for x in picat.ring.atoms_orig_idx]
                 group = 'Aromatic'
                 self.pication_info.append((picat.resnr, picat.restype, picat.reschain, '%.2f' % picat.distance,
                                            '%.2f' % picat.offset, picat.protcharged, group, ",".join(ids),
                                            tuple(picat.ring.center), tuple(picat.charge.center)))
             else:
-                ids = [str(lig_to_pdb[x.idx]) for x in picat.charge.atoms]
+                ids = [str(x) for x in picat.charge.atoms_orig_idx]
                 group = picat.charge.fgroup
                 self.pication_info.append((picat.resnr, picat.restype, picat.reschain, '%.2f' % picat.distance,
                                            '%.2f' % picat.offset, picat.protcharged, group, ",".join(ids),
@@ -150,16 +147,31 @@ class TextOutput():
         # HALOGEN BONDS #
         #################
 
-        self.halogen_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'DIST', 'DON_ANGLE', 'ACC_ANGLE', 'DON_IDX',
-                                 'DONORTYPE', 'ACC_IDX', 'ACCEPTORTYPE', 'LIGCOO', 'PROTCOO')
+        self.halogen_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'SIDECHAIN', 'DIST', 'DON_ANGLE', 'ACC_ANGLE',
+                                 'DON_IDX', 'DONORTYPE', 'ACC_IDX', 'ACCEPTORTYPE', 'LIGCOO', 'PROTCOO')
         self.halogen_info = []
-        for halogen in pli_class.halogen_bonds:
-            self.halogen_info.append((halogen.resnr, halogen.restype, halogen.reschain, '%.2f' % halogen.distance,
-                                      '%.2f' % halogen.don_angle, '%.2f' % halogen.acc_angle,
-                                      lig_to_pdb[halogen.don.x.idx], halogen.donortype,
-                                      mapping[halogen.acc.o.idx], halogen.acctype,
+        for halogen in self.complex.halogen_bonds:
+            self.halogen_info.append((halogen.resnr, halogen.restype, halogen.reschain, halogen.sidechain,
+                                      '%.2f' % halogen.distance, '%.2f' % halogen.don_angle, '%.2f' % halogen.acc_angle,
+                                      halogen.don_orig_idx, halogen.donortype,
+                                      halogen.acc_orig_idx, halogen.acctype,
                                       halogen.acc.o.coords, halogen.don.x.coords))
 
+        ###################
+        # METAL COMPLEXES #
+        ###################
+
+        self.metal_features = ('RESNR', 'RESTYPE', 'RESCHAIN', 'METAL_IDX', 'METAL_TYPE', 'TARGET_IDX', 'TARGET_TYPE',
+                               'COORDINATION', 'DIST', 'LOCATION', 'RMS', 'GEOMETRY', 'COMPLEXNUM', 'METALCOO',
+                               'TARGETCOO')
+        self.metal_info = []
+        # Coordinate format here is non-standard since the interaction partner can be either ligand or protein
+        for m in self.complex.metal_complexes:
+            self.metal_info.append((m.resnr, m.restype, m.reschain, m.metal_orig_idx, m.metal_type,
+                                    m.target_orig_idx, m.target_type, m.coordination_num, '%.2f' % m.distance,
+                                    m.location, '%.2f' % m.rms, m.geometry, str(m.complexnum), m.metal.coords,
+                                    m.target.atom.coords))
+
     def write_section(self, name, features, info, f):
         """Provides formatting for one section (e.g. hydrogen bonds)"""
         if not len(info) == 0:
@@ -178,13 +190,13 @@ class TextOutput():
                     cell_dict[j] = []
                 cell_dict[j].append(val)
         for item in cell_dict:
-            cell_dict[item] = max([len(x) for x in cell_dict[item]])+1  # Contains adapted width for each column
+            cell_dict[item] = max([len(x) for x in cell_dict[item]]) + 1  # Contains adapted width for each column
 
         # Format top line
         num_cols = len(array[0])
         form = '+'
         for col in range(num_cols):
-            form += (cell_dict[col]+1)*'-'
+            form += (cell_dict[col] + 1) * '-'
             form += '+'
         form += '\n'
 
@@ -204,18 +216,20 @@ class TextOutput():
             else:
                 sign = '-'
             for col in range(num_cols):
-                form += (cell_dict[col]+1)*sign
+                form += (cell_dict[col] + 1) * sign
                 form += '+'
             form += '\n'
         return form
 
-    def generate_rst(self):
+    def generate_txt(self):
         """Generates an flat text report for a single binding site"""
+
         txt = []
-        txt.append('%s' % self.name)
-        for i, member in enumerate(sorted(self.lig_members)[1:]):
-            txt.append('  + %s' % "-".join(str(element) for element in member))
-        txt.append("-"*len(self.name))
+        titletext = '%s (%s) - %s' % (self.bsid, self.longname, self.ligtype)
+        txt.append(titletext)
+        for i, member in enumerate(self.lig_members[1:]):
+            txt.append('  + %s' % ":".join(str(element) for element in member))
+        txt.append("-" * len(titletext))
         txt.append("Interacting chain(s): %s\n" % ','.join([chain for chain in self.interacting_chains]))
         for section in [['Hydrophobic Interactions', self.hydrophobic_features, self.hydrophobic_info],
                         ['Hydrogen Bonds', self.hbond_features, self.hbond_info],
@@ -223,7 +237,8 @@ class TextOutput():
                         ['Salt Bridges', self.saltbridge_features, self.saltbridge_info],
                         ['pi-Stacking', self.pistacking_features, self.pistacking_info],
                         ['pi-Cation Interactions', self.pication_features, self.pication_info],
-                        ['Halogen Bonds', self.halogen_features, self.halogen_info]]:
+                        ['Halogen Bonds', self.halogen_features, self.halogen_info],
+                        ['Metal Complexes', self.metal_features, self.metal_info]]:
             iname, features, interaction_information = section
             # Sort results first by res number, then by distance and finally ligand coordinates to get a unique order
             interaction_information = sorted(interaction_information, key=itemgetter(0, 2, -2))
@@ -243,27 +258,65 @@ class TextOutput():
                     table.append(values)
                 txt.append(self.rst_table(table))
         txt.append('\n')
-
         return txt
 
     def generate_xml(self):
         """Generates an XML-formatted report for a single binding site"""
         report = et.Element('bindingsite')
         identifiers = et.SubElement(report, 'identifiers')
+        longname = et.SubElement(identifiers, 'longname')
+        ligtype = et.SubElement(identifiers, 'ligtype')
         hetid = et.SubElement(identifiers, 'hetid')
         chain = et.SubElement(identifiers, 'chain')
         position = et.SubElement(identifiers, 'position')
         composite = et.SubElement(identifiers, 'composite')
         members = et.SubElement(identifiers, 'members')
+        smiles = et.SubElement(identifiers, 'smiles')
+
+        # Ligand properties. Number of (unpaired) functional atoms and rings.
+        lig_properties = et.SubElement(report, 'lig_properties')
+        num_heavy_atoms = et.SubElement(lig_properties, 'num_heavy_atoms')
+        num_hbd = et.SubElement(lig_properties, 'num_hbd')
+        num_hbd.text = str(self.ligand.num_hbd)
+        num_unpaired_hbd = et.SubElement(lig_properties, 'num_unpaired_hbd')
+        num_unpaired_hbd.text = str(self.complex.num_unpaired_hbd)
+        num_hba = et.SubElement(lig_properties, 'num_hba')
+        num_hba.text = str(self.ligand.num_hba)
+        num_unpaired_hba = et.SubElement(lig_properties, 'num_unpaired_hba')
+        num_unpaired_hba.text = str(self.complex.num_unpaired_hba)
+        num_hal = et.SubElement(lig_properties, 'num_hal')
+        num_hal.text = str(self.ligand.num_hal)
+        num_unpaired_hal = et.SubElement(lig_properties, 'num_unpaired_hal')
+        num_unpaired_hal.text = str(self.complex.num_unpaired_hal)
+        num_aromatic_rings = et.SubElement(lig_properties, 'num_aromatic_rings')
+        num_aromatic_rings.text = str(self.ligand.num_rings)
+        num_rot_bonds = et.SubElement(lig_properties, 'num_rotatable_bonds')
+        num_rot_bonds.text = str(self.ligand.num_rot_bonds)
+        molweight = et.SubElement(lig_properties, 'molweight')
+        molweight.text = str(self.ligand.molweight)
+        logp = et.SubElement(lig_properties, 'logp')
+        logp.text = str(self.ligand.logp)
+
         ichains = et.SubElement(report, 'interacting_chains')
+        bsresidues = et.SubElement(report, 'bs_residues')
         for i, ichain in enumerate(self.interacting_chains):
-            c = et.SubElement(ichains, 'interacting_chain', id=str(i+1))
+            c = et.SubElement(ichains, 'interacting_chain', id=str(i + 1))
             c.text = ichain
-        hetid.text, chain.text, position.text = self.name.split('-')
+        for i, bsres in enumerate(self.bs_res):
+            contact = 'True' if bsres in self.bs_res_interacting else 'False'
+            distance = '%.1f' % self.min_dist[bsres][0]
+            aatype = self.min_dist[bsres][1]
+            c = et.SubElement(bsresidues, 'bs_residue', id=str(i + 1), contact=contact, min_dist=distance, aa=aatype)
+            c.text = bsres
+        hetid.text, chain.text, position.text = self.ligand.hetid, self.ligand.chain, str(self.ligand.position)
         composite.text = 'True' if len(self.lig_members) > 1 else 'False'
-        for i, member in enumerate(sorted(self.lig_members)):
-            bsid = "-".join(str(element) for element in member)
-            m = et.SubElement(members, 'member', id=str(i+1))
+        longname.text = self.longname
+        ligtype.text = self.ligtype
+        smiles.text = self.ligand.smiles
+        num_heavy_atoms.text = str(self.ligand.heavy_atoms)  # Number of heavy atoms in ligand
+        for i, member in enumerate(self.lig_members):
+            bsid = ":".join(str(element) for element in member)
+            m = et.SubElement(members, 'member', id=str(i + 1))
             m.text = bsid
         interactions = et.SubElement(report, 'interactions')
 
@@ -273,15 +326,18 @@ class TextOutput():
             # Sort results first by res number, then by distance and finally ligand coordinates to get a unique order
             interaction_information = sorted(interaction_information, key=itemgetter(0, 2, -2))
             for j, single_contact in enumerate(interaction_information):
-                new_contact = et.SubElement(interaction, element_name[:-1], id=str(j+1))
+                if not element_name == 'metal_complexes':
+                    new_contact = et.SubElement(interaction, element_name[:-1], id=str(j + 1))
+                else:  # Metal Complex[es]
+                    new_contact = et.SubElement(interaction, element_name[:-2], id=str(j + 1))
                 for i, feature in enumerate(single_contact):
                     # Just assign the value unless it's an atom list, use subelements in this case
                     if features[i] == 'LIG_IDX_LIST':
                         feat = et.SubElement(new_contact, features[i].lower())
                         for k, atm_idx in enumerate(feature.split(',')):
-                            idx = et.SubElement(feat, 'idx', id=str(k+1))
+                            idx = et.SubElement(feat, 'idx', id=str(k + 1))
                             idx.text = str(atm_idx)
-                    elif features[i] in ['LIGCOO', 'PROTCOO']:
+                    elif features[i].endswith('COO'):
                         feat = et.SubElement(new_contact, features[i].lower())
                         xc, yc, zc = feature
                         xcoo = et.SubElement(feat, 'x')
@@ -303,4 +359,16 @@ class TextOutput():
         interactions.append(format_interactions('pi_stacks', self.pistacking_features, self.pistacking_info))
         interactions.append(format_interactions('pi_cation_interactions', self.pication_features, self.pication_info))
         interactions.append(format_interactions('halogen_bonds', self.halogen_features, self.halogen_info))
-        return report
\ No newline at end of file
+        interactions.append(format_interactions('metal_complexes', self.metal_features, self.metal_info))
+
+        # Mappings
+        mappings = et.SubElement(report, 'mappings')
+        smiles_to_pdb = et.SubElement(mappings, 'smiles_to_pdb')  # SMILES numbering to PDB file numbering (atoms)
+        bsid = ':'.join([self.ligand.hetid, self.ligand.chain, str(self.ligand.position)])
+        if self.ligand.atomorder is not None:
+            smiles_to_pdb_map = [(key, self.ligand.Mapper.mapid(self.ligand.can_to_pdb[key], mtype='protein', bsid=bsid)) for key in self.ligand.can_to_pdb]
+            smiles_to_pdb.text = ','.join([str(mapping[0])+':'+str(mapping[1]) for mapping in smiles_to_pdb_map])
+        else:
+            smiles_to_pdb.text = ''
+
+        return report
diff --git a/plip/modules/supplemental.py b/plip/modules/supplemental.py
index 0022d1c..859f42d 100644
--- a/plip/modules/supplemental.py
+++ b/plip/modules/supplemental.py
@@ -1,7 +1,7 @@
 """
 Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
 supplemental.py - Supplemental functions for PLIP analysis.
-Copyright 2014 Sebastian Salentin
+Copyright 2014-2015 Sebastian Salentin, Joachim Haupt
 
 Licensed under the Apache License, Version 2.0 (the "License");
 you may not use this file except in compliance with the License.
@@ -26,11 +26,12 @@ import config
 import re
 from collections import namedtuple
 import os
-from multiprocessing import Process
 if os.name != 'nt':  # Resource module not available for Windows
     import resource
 import subprocess
-import math  # Reimport for Windows
+import codecs
+import gzip
+import zipfile
 
 # External libraries
 import pybel
@@ -39,64 +40,21 @@ from openbabel import *
 import numpy as np
 from pymol import cmd
 from pymol import finish_launching
+import itertools
+
+# Settings
+np.seterr(all='ignore')  # No runtime warnings
+
+
+def tmpfile(prefix, direc):
+    """Returns the path to a newly created temporary file."""
+    return tempfile.mktemp(prefix=prefix, suffix='.pdb', dir=direc)
 
 
 def is_lig(hetid):
     """Checks if a PDB compound can be excluded as a small molecule ligand"""
     h = hetid.upper()
-    return not (h == 'HOH' or h in config.dna + config.ions)
-
-
-def parse_pdb(fil):
-    """Extracts additional information from PDB files.
-    I. When reading in a PDB file, OpenBabel numbers ATOMS and HETATOMS continously.
-    In PDB files, TER records are also counted, leading to a different numbering system.
-    This functions reads in a PDB file and provides a mapping as a dictionary.
-    II. Additionally, it returns a list of modified residues.
-    III. Furthermore, covalent linkages between ligands and protein residues/other ligands are identified
-    """
-    # #@todo Also consider SSBOND entries here
-    i, j = 0, 0  # idx and PDB numbering
-    d = {}
-    modres = set()
-    covlinkage = namedtuple("covlinkage", "id1 chain1 pos1 conf1 id2 chain2 pos2 conf2")
-    covalent = []
-    previous_ter = False
-    for line in fil:
-        if line.startswith(("ATOM", "HETATM")):
-            if not previous_ter:
-                i += 1
-                j += 1
-            else:
-                i += 1
-                j += 2
-            d[i] = j
-            previous_ter = False
-        # Numbering Changes at TER records
-        if line.startswith("TER"):
-            previous_ter = True
-        # Get modified residues
-        if line.startswith("MODRES"):
-            modres.add(line[12:15].strip())
-        # Get covalent linkages between ligands
-        if line.startswith("LINK"):
-            conf1, id1, chain1, pos1 = line[16].strip(), line[17:20].strip(), line[21].strip(), int(line[22:26])
-            conf2, id2, chain2, pos2 = line[46].strip(), line[47:50].strip(), line[51].strip(), int(line[52:56])
-            covalent.append(covlinkage(id1=id1, chain1=chain1, pos1=pos1, conf1=conf1,
-                                       id2=id2, chain2=chain2, pos2=pos2, conf2=conf2))
-    return d, modres, covalent
-
-
-def get_altconf_atoms(f):
-    """Return a list of PDB atom ids belonging to atoms with alternate conformations."""
-    alt = []
-    for line in f:
-        if line.startswith(("ATOM", "HETATM")):
-            atomid, location = int(line[6:11]), line[16]
-            location = 'A' if location == ' ' else location
-            if location != 'A':
-                alt.append(atomid)
-    return alt
+    return not (h == 'HOH' or h in config.UNSUPPORTED)
 
 
 def extract_pdbid(string):
@@ -111,35 +69,20 @@ def extract_pdbid(string):
 
 def whichrestype(atom):
     """Returns the residue name of an Pybel or OpenBabel atom."""
-    if isinstance(atom, Atom):
-        try:
-            return atom.OBAtom.GetResidue().GetName()
-        except AttributeError:
-            return None
-    elif isinstance(atom, OBAtom):
-        return atom.GetResidue().GetName() if atom.GetResidue is not None else None
-    else:
-        return None
+    atom = atom if not isinstance(atom, Atom) else atom.OBAtom  # Convert to OpenBabel Atom
+    return atom.GetResidue().GetName() if atom.GetResidue() is not None else None
 
 
 def whichresnumber(atom):
     """Returns the residue number of an Pybel or OpenBabel atom (numbering as in original PDB file)."""
-    if isinstance(atom, Atom):
-        return atom.OBAtom.GetResidue().GetNum()
-    elif isinstance(atom, OBAtom):
-        return atom.GetResidue().GetNum()
-    else:
-        return None
+    atom = atom if not isinstance(atom, Atom) else atom.OBAtom  # Convert to OpenBabel Atom
+    return atom.GetResidue().GetNum() if atom.GetResidue() is not None else None
 
 
 def whichchain(atom):
     """Returns the residue number of an PyBel or OpenBabel atom."""
-    if isinstance(atom, Atom):
-        return atom.OBAtom.GetResidue().GetChain()
-    elif isinstance(atom, OBAtom):
-        return atom.GetResidue().GetChain()
-    else:
-        return None
+    atom = atom if not isinstance(atom, Atom) else atom.OBAtom  # Convert to OpenBabel Atom
+    return atom.GetResidue().GetChain() if atom.GetResidue() is not None else None
 
 #########################
 # Mathematical operations
@@ -151,7 +94,7 @@ def euclidean3d(v1, v2):
     if not len(v1) == 3 and len(v2) == 3:
         print("Vectors are not in 3D space. Returning None.")
         return None
-    return math.sqrt((v1[0] - v2[0]) ** 2 + (v1[1] - v2[1]) ** 2 + (v1[2] - v2[2]) ** 2)
+    return np.sqrt((v1[0] - v2[0]) ** 2 + (v1[1] - v2[1]) ** 2 + (v1[2] - v2[2]) ** 2)
 
 
 def vector(p1, p2):
@@ -160,7 +103,7 @@ def vector(p1, p2):
     :param p2: coordinates of point p2
     :returns : numpy array with vector coordinates
     """
-    return None if len(p1) != len(p2) else np.array([p2[i]-p1[i] for i in xrange(len(p1))])
+    return None if len(p1) != len(p2) else np.array([p2[i] - p1[i] for i in xrange(len(p1))])
 
 
 def vecangle(v1, v2, deg=True):
@@ -173,8 +116,8 @@ def vecangle(v1, v2, deg=True):
         return 0.0
     dm = np.dot(v1, v2)
     cm = np.linalg.norm(v1) * np.linalg.norm(v2)
-    angle = np.arccos(round(dm/cm, 10))  # Round here to prevent floating point errors
-    return math.degrees(angle) if deg else angle
+    angle = np.arccos(round(dm / cm, 10))  # Round here to prevent floating point errors
+    return np.degrees([angle, ])[0] if deg else angle
 
 
 def normalize_vector(v):
@@ -210,7 +153,7 @@ def projection(pnormal1, ppoint, tpoint):
     sn = -np.dot(pnormal, vector(ppoint, tpoint))
     sd = np.dot(pnormal, pnormal)
     sb = sn / sd
-    return [c1 + c2 for c1, c2 in zip(tpoint, [sb*pn for pn in pnormal])]
+    return [c1 + c2 for c1, c2 in zip(tpoint, [sb * pn for pn in pnormal])]
 
 
 def cluster_doubles(double_list):
@@ -329,164 +272,206 @@ def set_custom_colorset():
     cmd.set_color('mylightgreen', '[229, 245, 224]')
 
 
-#############################################
-# Following code adapted from Joachim Haupt #
-#############################################
-
-
-def getligs(mol, altconf, idx_to_pdb, modres, covalent):
-    """Get all ligands from a PDB file. Adapted from Joachim's structTools"""
-    #############################
-    # Read in file and get name #
-    #############################
-
-    data = namedtuple('ligand', 'mol mapping water members')
-    ligands = []
-    # #@todo Consider ions and attribute them to ligand molecules
-
-    #########################
-    # Filtering using lists #
-    #########################
-
-    all_res1 = [o for o in pybel.ob.OBResidueIter(mol.OBMol)
-               if not (o.GetResidueProperty(9) or o.GetResidueProperty(0))]
-    all_lignames = set([a.GetName() for a in all_res1])
-
-    water = [o for o in pybel.ob.OBResidueIter(mol.OBMol) if o.GetResidueProperty(9)]
-    all_res2 = [a for a in all_res1 if is_lig(a.GetName()) and a.GetName() not in modres]  # Filter out non-ligands
-
-    ############################################
-    # Filtering by counting and artifacts list #
-    ############################################
-    artifacts = []
-    unique_ligs = set(a.GetName() for a in all_res2)
-    for ulig in unique_ligs:
-        # Discard if appearing 15 times or more and is possible artifact
-        if ulig in config.biolip_list and [a.GetName() for a in all_res2].count(ulig) >= 15:
-            artifacts.append(ulig)
-    all_res3 = [a for a in all_res2 if a.GetName() not in artifacts]
-    all_res_dict = {(a.GetName(), a.GetChain(), a.GetNum()): a for a in all_res3}
-
-    #########################
-    # Identify kmer ligands #
-    #########################
-
-    lignames = list(set([a.GetName() for a in all_res3]))
-    # Remove all those not considered by ligands and pairings including alternate conformations
-
-    ligdoubles = [[(link.id1, link.chain1, link.pos1),
-                   (link.id2, link.chain2, link.pos2)] for link in
-                  [c for c in covalent if c.id1 in lignames and c.id2 in lignames and
-                   c.conf1 in ['A', ''] and c.conf2 in ['A', '']
-                  and (c.id1, c.chain1, c.pos1) in all_res_dict and (c.id2, c.chain2, c.pos2) in all_res_dict]]
-    kmers = cluster_doubles(ligdoubles)
-    if not kmers:  # No ligand kmers, just normal independent ligands
-        res_kmers = [[all_res_dict[res]] for res in all_res_dict]
+def nucleotide_linkage(residues):
+    """Support for DNA/RNA ligands by finding missing covalent linkages to stitch DNA/RNA together."""
+
+    nuc_covalent = []
+    #######################################
+    # Basic support for RNA/DNA as ligand #
+    #######################################
+    nucleotides = ['A', 'C', 'T', 'G', 'U', 'DA', 'DC', 'DT', 'DG', 'DU']
+    dna_rna = {}  # Dictionary of DNA/RNA residues by chain
+    covlinkage = namedtuple("covlinkage", "id1 chain1 pos1 conf1 id2 chain2 pos2 conf2")
+    # Create missing covlinkage entries for DNA/RNA
+    for ligand in residues:
+        resname, chain, pos = ligand
+        if resname in nucleotides:
+            if chain not in dna_rna:
+                dna_rna[chain] = [(resname, pos), ]
+            else:
+                dna_rna[chain].append((resname, pos))
+    for chain in dna_rna:
+        nuc_list = dna_rna[chain]
+        for i, nucleotide in enumerate(nuc_list):
+            if not i == len(nuc_list) - 1:
+                name, pos = nucleotide
+                nextnucleotide = nuc_list[i + 1]
+                nextname, nextpos = nextnucleotide
+                newlink = covlinkage(id1=name, chain1=chain, pos1=pos, conf1='',
+                                     id2=nextname, chain2=chain, pos2=nextpos, conf2='')
+                nuc_covalent.append(newlink)
+
+    return nuc_covalent
+
+def ring_is_planar(ring, r_atoms):
+    """Given a set of ring atoms, check if the ring is sufficiently planar
+    to be considered aromatic"""
+    normals = []
+    for a in r_atoms:
+        adj = pybel.ob.OBAtomAtomIter(a.OBAtom)
+        # Check for neighboring atoms in the ring
+        n_coords = [pybel.Atom(neigh).coords for neigh in adj if ring.IsMember(neigh)]
+        vec1, vec2 = vector(a.coords, n_coords[0]), vector(a.coords, n_coords[1])
+        normals.append(np.cross(vec1, vec2))
+    # Given all normals of ring atoms and their neighbors, the angle between any has to be 5.0 deg or less
+    for n1, n2 in itertools.product(normals, repeat=2):
+        arom_angle = vecangle(n1, n2)
+        if all([arom_angle > config.AROMATIC_PLANARITY, arom_angle < 180.0 - config.AROMATIC_PLANARITY]):
+            return False
+    return True
+
+
+def classify_by_name(names):
+    """Classify a (composite) ligand by the HETID(s)"""
+    if len(names) > 3:  # Polymer
+        if len({'U', 'A', 'C', 'G'}.intersection(set(names))) != 0:
+            ligtype = 'RNA'
+        elif len({'DT', 'DA', 'DC', 'DG'}.intersection(set(names))) != 0:
+            ligtype = 'DNA'
+        else:
+            ligtype = "POLYMER"
+    else:
+        ligtype = 'SMALLMOLECULE'
+
+    for name in names:
+        if name in config.METAL_IONS:
+            if len(names) == 1:
+                ligtype = 'ION'
+            else:
+                if "ION" not in ligtype:
+                    ligtype += '+ION'
+    return ligtype
+
+
+def get_isomorphisms(reference, lig):
+    """Get all isomorphisms of the ligand."""
+    query = pybel.ob.CompileMoleculeQuery(reference.OBMol)
+    mappr = pybel.ob.OBIsomorphismMapper.GetInstance(query)
+    if all:
+        isomorphs = pybel.ob.vvpairUIntUInt()
+        mappr.MapAll(lig.OBMol, isomorphs)
+    else:
+        isomorphs = pybel.ob.vpairUIntUInt()
+        mappr.MapFirst(lig.OBMol, isomorphs)
+        isomorphs = [isomorphs]
+    debuglog("Number of isomorphisms: %i" % len(isomorphs))
+    # #@todo Check which isomorphism to take
+    return isomorphs
+
+
+def canonicalize(lig):
+    """Get the canonical atom order for the ligand."""
+    atomorder = None
+    # Get canonical atom order
+
+    lig = pybel.ob.OBMol(lig.OBMol)
+    for bond in pybel.ob.OBMolBondIter(lig):
+        if bond.GetBondOrder() != 1:
+            bond.SetBondOrder(1)
+    lig.DeleteData(pybel.ob.StereoData)
+    lig = pybel.Molecule(lig)
+    testcan = lig.write(format='can')
+    try:
+        pybel.readstring('can', testcan)
+        reference = pybel.readstring('can', testcan)
+    except IOError:
+        testcan, reference = '', ''
+    if testcan != '':
+        reference.removeh()
+        isomorphs = get_isomorphisms(reference, lig)  # isomorphs now holds all isomorphisms within the molecule
+        if not len(isomorphs) == 0:
+            smi_dict = {}
+            smi_to_can = isomorphs[0]
+            for x in smi_to_can:
+                smi_dict[int(x[1]) + 1] = int(x[0]) + 1
+            atomorder = [smi_dict[x + 1] for x in range(len(lig.atoms))]
+        else:
+            atomorder = None
+    return atomorder
+
+
+def int32_to_negative(int32):
+    """Checks if a suspicious number (e.g. ligand position) is in fact a negative number represented as a
+    32 bit integer and returns the actual number.
+    """
+    dct = {}
+    if int32 == 4294967295:  # Special case in some structures (note, this is just a workaround)
+        return -1
+    for i in range(-1000, -1):
+        dct[np.uint32(i)] = i
+    if int32 in dct:
+        return dct[int32]
     else:
-        # res_kmers contains clusters of covalently bound ligand residues (kmer ligands)
-        res_kmers = [[all_res_dict[res] for res in kmer] for kmer in kmers]
-
-        # In this case, add other ligands which are not part of a kmer
-        in_kmer = []
-        for res_kmer in res_kmers:
-            for res in res_kmer:
-                in_kmer.append((res.GetName(), res.GetChain(), res.GetNum()))
-        for res in all_res_dict:
-            if res not in in_kmer:
-                newres = [all_res_dict[res], ]
-                res_kmers.append(newres)
-
-    ###################
-    # Extract ligands #
-    ###################
-
-    for kmer in res_kmers:  # iterate over all ligands
-        members = [(res.GetName(), res.GetChain(), res.GetNum()) for res in kmer]
-        rname, rchain, rnum = sorted(members)[0]  # representative name, chain, and number
-        hetatoms = set()
-        for obresidue in kmer:
-            hetatoms_res = set([(obatom.GetIdx(), obatom) for obatom in pybel.ob.OBResidueAtomIter(obresidue)
-                        if not obatom.IsHydrogen()])
-
-            hetatoms_res = set([atm for atm in hetatoms_res if not idx_to_pdb[atm[0]] in altconf])  # Remove alt. conformations
-            hetatoms.update(hetatoms_res)
-        if len(hetatoms) == 0:
-            continue
-        hetatoms = dict(hetatoms)  # make it a dict with idx as key and OBAtom as value
-        lig = pybel.ob.OBMol()  # new ligand mol
-        neighbours = dict()
-        for obatom in hetatoms.values():  # iterate over atom objects
-            idx = obatom.GetIdx()
-            lig.AddAtom(obatom)
-            # ids of all neighbours of obatom
-            neighbours[idx] = set([neighbour_atom.GetIdx() for neighbour_atom
-                                   in pybel.ob.OBAtomAtomIter(obatom)]) & set(hetatoms.keys())
-
-        ##############################################################
-        # map the old atom idx of OBMol to the new idx of the ligand #
-        ##############################################################
-
-        newidx = dict(zip(hetatoms.keys(), [obatom.GetIdx() for obatom in pybel.ob.OBMolAtomIter(lig)]))
-        mapold = dict(zip(newidx.values(), newidx))
-        # copy the bonds
-        for obatom in hetatoms:
-            for neighbour_atom in neighbours[obatom]:
-                bond = hetatoms[obatom].GetBond(hetatoms[neighbour_atom])
-                lig.AddBond(newidx[obatom], newidx[neighbour_atom], bond.GetBondOrder())
-        lig = pybel.Molecule(lig)
-        # For kmers, the representative ids are chosen (first residue of kmer)
-        lig.data.update({'Name': rname,
-                         'Chain': rchain,
-                         'ResNr': rnum})
-        lig.title = '-'.join((rname, rchain, str(rnum)))
-        ligands.append(data(mol=lig, mapping=mapold, water=water, members=members))
-    excluded = sorted(list(all_lignames.difference(set(lignames))))
-    return ligands, excluded
-
-
-def read_pdb(pdbfname, safe=False):
-    """Reads a given PDB file and returns a Pybel Molecule. If requested, do it
-    safely to except Open Babel crashes. All bonds are read in as single bonds
-    if requested, saving a lot of time at OpenBabel import."""
-    global exitcode
+        return int32
+
+
+def read_pdb(pdbfname):
+    """Reads a given PDB file and returns a Pybel Molecule."""
     pybel.ob.obErrorLog.StopLogging()  # Suppress all OpenBabel warnings
     if os.name != 'nt':  # Resource module not available for Windows
-        resource.setrlimit(resource.RLIMIT_STACK, (2**28, -1))  # set stack size to 256MB
-    sys.setrecursionlimit(10**5)  # increase Python recoursion limit
-    success = True
-    if safe:  # read the file safely, since it can happen, that babel crashes on large files
-        if os.path.exists(pdbfname):
-            def f(fname):
-                readmol('pdb', fname)
-            p = Process(target=f, args=(pdbfname,))  # make the file reading a separate process
-            p.start()
-            p.join()
-            exitcode = p.exitcode
-            success = exitcode == 0
-            del p
-        else:
-            print("  Error: PDB file not found!")
-            success = False
-            exitcode = 1
-    if success:
-        mol = readmol('pdb', pdbfname)  # only read the file iff it was successful before
-    elif exitcode == 4:
-        sys.stderr.write('Error: Input file could not be read by OpenBabel.')
-        sys.exit(4)
+        maxsize = resource.getrlimit(resource.RLIMIT_STACK)[-1]
+        resource.setrlimit(resource.RLIMIT_STACK, (min(2 ** 28, maxsize), maxsize))
+    sys.setrecursionlimit(10 ** 5)  # increase Python recoursion limit
+    return readmol(pdbfname)
+
+
+def read(fil):
+    """Returns a file handler and detects gzipped files."""
+    if os.path.splitext(fil)[-1] == '.gz':
+        return gzip.open(fil, 'rb')
+    elif os.path.splitext(fil)[-1] == '.zip':
+        zf = zipfile.ZipFile(fil, 'r')
+        return zf.open(zf.infolist()[0].filename)
     else:
-        mol = pybel.Molecule(pybel.ob.OBMol())
-        print("  Error: Failed to read '%s' with OpenBabel (exit code %d)!" % (pdbfname, exitcode))
-    return mol
+        try:
+            codecs.open(fil, 'r', 'utf-8').read()
+            return codecs.open(fil, 'r', 'utf-8')
+        except UnicodeDecodeError:
+            return open(fil, 'r')
 
 
-def readmol(fformat='mol', path=None):
-    """Reads the given molecule file and returns the corresponding Pybel molecule.
+def readmol(path):
+    """Reads the given molecule file and returns the corresponding Pybel molecule as well as the input file type.
     In contrast to the standard Pybel implementation, the file is closed properly."""
+    supported_formats = ['pdb', 'pdbqt', 'mmcif']
     obc = pybel.ob.OBConversion()
-    obc.SetInFormat(fformat)
-    mol = pybel.ob.OBMol()
-    with open(path) as f:
-        obc.ReadString(mol, str(f.read()))
-        if mol.Empty():
-            sys.exit(4)
-    return pybel.Molecule(mol)
\ No newline at end of file
+
+    with read(path) as f:
+        filestr = str(f.read())
+
+    for sformat in supported_formats:
+        obc.SetInFormat(sformat)
+        mol = pybel.ob.OBMol()
+        obc.ReadString(mol, filestr)
+        if not mol.Empty():
+            if sformat == 'pdbqt':
+                message('[EXPERIMENTAL] Input is PDBQT file. Some features (especially visualization) might not '
+                        'work as expected. Please consider using PDB format instead.\n')
+            if sformat == 'mmcif':
+                message('[EXPERIMENTAL] Input is mmCIF file. Most features do currently not work with this format.\n')
+            return pybel.Molecule(mol), sformat
+    sysexit(4, 'No valid file format provided.')
+
+
+def sysexit(code, msg):
+    """Exit using an custom error message and error code."""
+    sys.stderr.write(msg)
+    sys.exit(code)
+
+
+def message(msg, indent=False):
+    """Writes messages in verbose mode"""
+    if config.VERBOSE:
+        if indent:
+            msg = '  ' + msg
+        sys.stdout.write(msg)
+
+
+def debuglog(msg):
+    """Writes debug messages"""
+    if config.DEBUG:
+        msg = '    %% DEBUG: ' + msg
+        if len(msg) > 100:
+            msg = msg[:100] + ' ...'
+        msg += '\n'
+        sys.stdout.write(msg)
diff --git a/plip/modules/visualize.py b/plip/modules/visualize.py
index 355d211..423a833 100644
--- a/plip/modules/visualize.py
+++ b/plip/modules/visualize.py
@@ -1,7 +1,7 @@
 """
 Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
 visualize.py - Visualization of PLIP results using PyMOL.
-Copyright 2014 Sebastian Salentin
+Copyright 2014-2015 Sebastian Salentin
 
 Licensed under the Apache License, Version 2.0 (the "License");
 you may not use this file except in compliance with the License.
@@ -20,6 +20,110 @@ limitations under the License.
 # Own modules
 from supplemental import *
 from time import sleep
+from collections import namedtuple
+
+hbonds_info = namedtuple('hbonds_info', 'ldon_id lig_don_id prot_acc_id pdon_id prot_don_id lig_acc_id')
+hydrophobic_info = namedtuple('hydrophobic_info', 'bs_ids lig_ids pairs_ids')
+halogen_info = namedtuple('halogen_info', 'don_id acc_id')
+pistack_info = namedtuple('pistack_info', 'proteinring_atoms, proteinring_center ligandring_atoms '
+                                          'ligandring_center type')
+pication_info = namedtuple('pication_info', 'ring_center charge_center ring_atoms charge_atoms, protcharged')
+sbridge_info = namedtuple('sbridge_info', 'positive_atoms negative_atoms positive_center negative_center protispos')
+wbridge_info = namedtuple('wbridge_info', 'don_id acc_id water_id protisdon')
+metal_info = namedtuple('metal_info', 'metal_id, target_id location')
+
+
+def select_by_ids(selname, idlist, selection_exists=False, chunksize=20):
+    """Selection with a large number of ids concatenated into a selection
+    list can cause buffer overflow in PyMOL. This function takes a selection
+    name and and list of IDs (list of integers) as input and makes a careful
+    step-by-step selection (packages of 20 by default)"""
+    idlist = list(set(idlist))  # Remove duplicates
+    if not selection_exists:
+        cmd.select(selname, 'None')  # Empty selection first
+    idchunks = [idlist[i:i+chunksize] for i in xrange(0, len(idlist), chunksize)]
+    for idchunk in idchunks:
+        cmd.select(selname, '%s or (id %s)' % (selname, '+'.join(map(str, idchunk))))
+
+class PyMOLComplex:
+    """Contains all information on a complex relevant for visualization. Can be pickled"""
+    def __init__(self, mol, site):
+        pcomp = mol
+        pli = mol.interaction_sets[site]
+        ligand = pli.ligand
+
+        # General Information
+        self.lig_members = sorted(pli.ligand.members)
+        self.sourcefile = pcomp.sourcefiles['pdbcomplex']
+        self.corrected_pdb = pcomp.corrected_pdb
+        self.pdbid = mol.pymol_name
+        self.hetid = ligand.hetid
+        self.chain = ligand.chain if not ligand.chain == "0" else ""  # #@todo Fix this
+        self.position = str(ligand.position)
+        self.outpath = mol.output_path
+        self.metal_ids = [x.m_orig_idx for x in pli.ligand.metals]
+        self.unpaired_hba_idx = pli.unpaired_hba_orig_idx
+        self.unpaired_hbd_idx = pli.unpaired_hbd_orig_idx
+        self.unpaired_hal_idx = pli.unpaired_hal_orig_idx
+
+        # Information on Interactions
+
+        # Hydrophobic Contacts
+        # Contains IDs of contributing binding site, ligand atoms and the pairings
+        hydroph_pairs_id = [(h.bsatom_orig_idx, h.ligatom_orig_idx) for h in pli.hydrophobic_contacts]
+        self.hydrophobic_contacts = hydrophobic_info(bs_ids=[hp[0] for hp in hydroph_pairs_id],
+                                                     lig_ids=[hp[1] for hp in hydroph_pairs_id],
+                                                     pairs_ids=hydroph_pairs_id)
+
+        # Hydrogen Bonds
+        # #@todo Don't use indices, simplify this code here
+        hbonds_ldon, hbonds_pdon = pli.hbonds_ldon, pli.hbonds_pdon
+        hbonds_ldon_id = [(hb.a_orig_idx, hb.d_orig_idx) for hb in hbonds_ldon]
+        hbonds_pdon_id = [(hb.a_orig_idx, hb.d_orig_idx) for hb in hbonds_pdon]
+        self.hbonds = hbonds_info(ldon_id=[(hb.a_orig_idx, hb.d_orig_idx) for hb in hbonds_ldon],
+                                  lig_don_id=[hb[1] for hb in hbonds_ldon_id],
+                                  prot_acc_id=[hb[0] for hb in hbonds_ldon_id],
+                                  pdon_id=[(hb.a_orig_idx, hb.d_orig_idx) for hb in hbonds_pdon],
+                                  prot_don_id=[hb[1] for hb in hbonds_pdon_id],
+                                  lig_acc_id=[hb[0] for hb in hbonds_pdon_id])
+
+        # Halogen Bonds
+        self.halogen_bonds = [halogen_info(don_id=h.don_orig_idx, acc_id=h.acc_orig_idx)
+                              for h in pli.halogen_bonds]
+
+        # Pistacking
+        self.pistacking = [pistack_info(proteinring_atoms=pistack.proteinring.atoms_orig_idx,
+                                        proteinring_center=pistack.proteinring.center,
+                                        ligandring_atoms=pistack.ligandring.atoms_orig_idx,
+                                        ligandring_center=pistack.ligandring.center,
+                                        type=pistack.type) for pistack in pli.pistacking]
+
+        # Pi-cation interactions
+        self.pication = [pication_info(ring_center=picat.ring.center,
+                                       charge_center=picat.charge.center,
+                                       ring_atoms=picat.ring.atoms_orig_idx,
+                                       charge_atoms=picat.charge.atoms_orig_idx,
+                                       protcharged=picat.protcharged)
+                         for picat in pli.pication_paro+pli.pication_laro]
+
+        # Salt Bridges
+        self.saltbridges = [sbridge_info(positive_atoms=sbridge.positive.atoms_orig_idx,
+                                         negative_atoms=sbridge.negative.atoms_orig_idx,
+                                         positive_center=sbridge.positive.center,
+                                         negative_center=sbridge.negative.center,
+                                         protispos=sbridge.protispos)
+                            for sbridge in pli.saltbridge_lneg+pli.saltbridge_pneg]
+
+        # Water Bridgese('wbridge_info', 'don_id acc_id water_id protisdon')
+        self.waterbridges = [wbridge_info(don_id=wbridge.d_orig_idx,
+                                          acc_id=wbridge.a_orig_idx,
+                                          water_id=wbridge.water_orig_idx,
+                                          protisdon=wbridge.protisdon) for wbridge in pli.water_bridges]
+
+        # Metal Complexes
+        self.metal_complexes = [metal_info(metal_id=metalc.metal_orig_idx,
+                                           target_id=metalc.target_orig_idx,
+                                           location=metalc.location) for metalc in pli.metal_complexes]
 
 
 def set_fancy_ray():
@@ -78,54 +182,58 @@ def png_workaround(filepath, width=1200, height=800):
         getheight = 'h=`convert ' + newfile + ' -ping -format "%h" info:`;'  # Get the hight of the new image
         newres = 'if [ "$w" -gt "$h" ]; then newr="${w%.*}x$w"; else newr="${h%.*}x$h"; fi;'  # Set quadratic ratio
         quadratic = 'convert ' + newfile + ' -gravity center -extent "$newr" ' + newfile  # Fill with whitespace
-        os.system(getwidth+getheight+newres+quadratic)
+        os.system(getwidth + getheight + newres + quadratic)
     else:
         sys.stderr.write('Imagemagick not available. Images will not be resized or cropped.')
 
 
-def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=False, fancy=False):
+def visualize_in_pymol(plcomplex):
     """Visualizes the protein-ligand pliprofiler at one site in PyMOL."""
 
     #####################
     # Set everything up #
     #####################
 
-    pcomp = protcomplex_class
-    pdbid = pcomp.pymol_name
-    pli = pcomp.interaction_sets[pli_site]  # Select the interaction class corresponding to the selection
-    ligdata = pli.ligand.pymol_data
-    lig_members = sorted(pli.ligand.members)
-    mapping = pcomp.idx_to_pdb_mapping  # Mapping internal -> external for protein atoms
-    lig_to_pdb = {key: mapping[ligdata.maptopdb[key]] for key in ligdata.maptopdb}  # Atom mapping for ligand
-    save_to = protcomplex_class.output_path
-    chain = ligdata.chain if not ligdata.chain == "0" else ""
-    ligname = ligdata.hetid
+    pdbid = plcomplex.pdbid
+    lig_members = plcomplex.lig_members
+    chain = plcomplex.chain
+    ligname = plcomplex.hetid
+    metal_ids = plcomplex.metal_ids
+    metal_ids_str = '+'.join([str(i) for i in metal_ids])
 
     ########################
     # Basic visualizations #
     ########################
 
-    opts = '-p' if show else '-pcq'
-    start_pymol(run=True, options=opts, quiet=True)
+    start_pymol(run=True, options='-pcq', quiet=not config.DEBUG)
     standard_settings()
     cmd.set('dash_gap', 0)  # Show not dashes, but lines for the pliprofiler
     cmd.set('ray_shadow', 0)  # Turn on ray shadows for clearer ray-traced images
     cmd.set('cartoon_color', 'mylightblue')
-    cmd.load(pcomp.sourcefiles['pdbcomplex'])
+    cmd.load(plcomplex.sourcefile)
     current_name = cmd.get_object_list(selection='(all)')[0]
+    debuglog('Setting current_name to "%s" and pdbid to "%s"' % (current_name, pdbid))
     cmd.set_name(current_name, pdbid)
     cmd.hide('everything', 'all')
-    cmd.select(ligname, 'resn %s and chain %s and resi %s' % (ligdata.hetid, chain, ligdata.resid))
+    cmd.select(ligname, 'resn %s and chain %s and resi %s*' % (ligname, chain, plcomplex.position))
+
+    # Visualize and color metal ions if there are any
+    if not len(metal_ids) == 0:
+        select_by_ids(ligname, metal_ids, selection_exists=True)
+        cmd.show('spheres', 'id %s and %s' % (metal_ids_str, pdbid))
 
     # Additionally, select all members of composite ligands
     for member in lig_members:
         resid, chain, resnr = member[0], member[1], str(member[2])
         cmd.select(ligname, '%s or (resn %s and chain %s and resi %s)' % (ligname, resid, chain, resnr))
-    # #@todo Does not work if no bonds are available (e.g.
     cmd.show('sticks', ligname)
     cmd.color('myblue')
     cmd.color('myorange', ligname)
     cmd.util.cnc('all')
+    if not len(metal_ids) == 0:
+        cmd.color('hotpink', 'id %s' % metal_ids_str)
+        cmd.hide('sticks', 'id %s' % metal_ids_str)
+        cmd.set('sphere_scale', 0.3, ligname)
     cmd.deselect()
 
     ###########################
@@ -134,20 +242,21 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
 
     for group in ['Hydrophobic-P', 'Hydrophobic-L', 'HBondDonor-P', 'HBondDonor-L', 'HBondAccept-P', 'HBondAccept-L',
                   'HalogenAccept', 'HalogenDonor', 'Water', 'MetalIons', 'StackRings-P', 'PosCharge-P', 'PosCharge-L',
-                  'NegCharge-P', 'NegCharge-L', 'PiCatRing-P', 'StackRings-L', 'PiCatRing-L']:
+                  'NegCharge-P', 'NegCharge-L', 'PiCatRing-P', 'StackRings-L', 'PiCatRing-L', 'Metal-M', 'Metal-P',
+                  'Metal-W', 'Metal-L', 'Unpaired-HBA', 'Unpaired-HBD', 'Unpaired-HAL', 'Unpaired-RINGS']:
         cmd.select(group, 'None')
 
+    # #@todo Up here, define all names necessary for analysis
+
     ######################################
     # Visualize hydrophobic interactions #
     ######################################
 
-    hydroph = pli.hydrophobic_contacts
-    hydroph_pairs_id = [(mapping[h[0].idx], lig_to_pdb[h[1].idx]) for h in hydroph]
-    hydroph_bs_id, hydroph_lig_id = [hp[0] for hp in hydroph_pairs_id], [hp[1] for hp in hydroph_pairs_id]
-    if not len(hydroph_bs_id) == 0:
-        for h in [['Hydrophobic-P', hydroph_bs_id], ['Hydrophobic-L', hydroph_lig_id]]:
-            cmd.select(h[0], 'id %s' % '+'.join(map(str, h[1])))
-        for i in hydroph_pairs_id:
+    if not len(plcomplex.hydrophobic_contacts.bs_ids) == 0:
+        for h in [['Hydrophobic-P', plcomplex.hydrophobic_contacts.bs_ids],
+                  ['Hydrophobic-L', plcomplex.hydrophobic_contacts.lig_ids]]:
+            select_by_ids(h[0], h[1])
+        for i in plcomplex.hydrophobic_contacts.pairs_ids:
             cmd.select('tmp_bs', 'id %i' % i[0])
             cmd.select('tmp_lig', 'id %i' % i[1])
             cmd.distance('Hydrophobic', 'tmp_bs', 'tmp_lig')
@@ -161,20 +270,15 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     # Visualize H-Bonds #
     #####################
 
-    hbonds_ldon, hbonds_pdon = pli.hbonds_ldon, pli.hbonds_pdon
-    hbonds_ldon_id = [(mapping[hb.a.idx], lig_to_pdb[hb.d.idx]) for hb in hbonds_ldon]
-    hbonds_lig_don_id, hbonds_prot_acc_id = [hb[1] for hb in hbonds_ldon_id], [hb[0] for hb in hbonds_ldon_id]
-    hbonds_pdon_id = [(lig_to_pdb[hb.a.idx], mapping[hb.d.idx]) for hb in hbonds_pdon]
-    hbonds_prot_don_id, hbonds_lig_acc_id = [hb[1] for hb in hbonds_pdon_id], [hb[0] for hb in hbonds_pdon_id]
-    for group in [['HBondDonor-L', hbonds_lig_don_id], ['HBondDonor-P', hbonds_prot_don_id],
-                  ['HBondAccept-L', hbonds_lig_acc_id], ['HBondAccept-P', hbonds_prot_acc_id]]:
+    for group in [['HBondDonor-L', plcomplex.hbonds.lig_don_id], ['HBondDonor-P', plcomplex.hbonds.prot_don_id],
+                  ['HBondAccept-L', plcomplex.hbonds.lig_acc_id], ['HBondAccept-P', plcomplex.hbonds.prot_acc_id]]:
         if not len(group[1]) == 0:
-            cmd.select(group[0], 'id %s' % '+'.join(map(str, group[1])))
-    for i in hbonds_ldon_id:
+            select_by_ids(group[0], group[1])
+    for i in plcomplex.hbonds.ldon_id:
         cmd.select('tmp_bs', 'id %i' % i[0])
         cmd.select('tmp_lig', 'id %i' % i[1])
         cmd.distance('HBonds', 'tmp_bs', 'tmp_lig')
-    for i in hbonds_pdon_id:
+    for i in plcomplex.hbonds.pdon_id:
         cmd.select('tmp_bs', 'id %i' % i[1])
         cmd.select('tmp_lig', 'id %i' % i[0])
         cmd.distance('HBonds', 'tmp_bs', 'tmp_lig')
@@ -185,19 +289,18 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     # Visualize Halogen Bonds #
     ###########################
 
-    halogen = pli.halogen_bonds
+    halogen = plcomplex.halogen_bonds
     all_don_x, all_acc_o = [], []
     for h in halogen:
-        don_x, don_c = lig_to_pdb[h.don.x.idx], lig_to_pdb[h.don.c.idx]
-        acc_y, acc_o = mapping[h.acc.y.idx], mapping[h.acc.o.idx]
-        all_don_x.append(don_x)
-        all_acc_o.append(acc_o)
-        for group in [['tmp_bs', acc_o], ['tmp_lig', don_x]]:
+        all_don_x.append(h.don_id)
+        all_acc_o.append(h.acc_id)
+        for group in [['tmp_bs', h.acc_id], ['tmp_lig', h.don_id]]:
             cmd.select(group[0], 'id %i' % group[1])
         cmd.distance('HalogenBonds', 'tmp_bs', 'tmp_lig')
     if not len(all_acc_o) == 0:
-        cmd.select('HalogenAccept', 'id %s' % '+'.join(map(str, all_acc_o)))
-        cmd.select('HalogenDonor', 'id %s' % '+'.join(map(str, all_don_x)))
+        select_by_ids('HalogenAccept', all_acc_o)
+        select_by_ids('HalogenDonor', all_don_x)
+        #cmd.select('HalogenDonor', 'id %s' % '+'.join(map(str, all_don_x)))
     if object_exists('HalogenBonds'):
         cmd.set('dash_color', 'greencyan', 'HalogenBonds')
 
@@ -205,19 +308,19 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     # Visualize Pi-Stacking #
     #########################
 
-    stacks = pli.pistacking
+    stacks = plcomplex.pistacking
     for i, stack in enumerate(stacks):
-        pires_ids = '+'.join(map(str, [mapping[atm.idx] for atm in stack.proteinring.atoms]))
-        pilig_ids = '+'.join(map(str, [lig_to_pdb[atm.idx] for atm in stack.ligandring.atoms]))
+        pires_ids = '+'.join(map(str, stack.proteinring_atoms))
+        pilig_ids = '+'.join(map(str, stack.ligandring_atoms))
         cmd.select('StackRings-P', 'StackRings-P or id %s' % pires_ids)
         cmd.select('StackRings-L', 'StackRings-L or id %s' % pilig_ids)
         cmd.select('StackRings-P', 'byres StackRings-P')
         cmd.show('sticks', 'StackRings-P')
 
-        cmd.pseudoatom('ps-pistack-1-%i' % i, pos=stack.proteinring.center)
-        cmd.pseudoatom('ps-pistack-2-%i' % i, pos=stack.ligandring.center)
-        cmd.pseudoatom('Centroids-P', pos=stack.proteinring.center)
-        cmd.pseudoatom('Centroids-L', pos=stack.ligandring.center)
+        cmd.pseudoatom('ps-pistack-1-%i' % i, pos=stack.proteinring_center)
+        cmd.pseudoatom('ps-pistack-2-%i' % i, pos=stack.ligandring_center)
+        cmd.pseudoatom('Centroids-P', pos=stack.proteinring_center)
+        cmd.pseudoatom('Centroids-L', pos=stack.ligandring_center)
 
         if stack.type == 'P':
             cmd.distance('PiStackingP', 'ps-pistack-1-%i' % i, 'ps-pistack-2-%i' % i)
@@ -236,22 +339,23 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     # Visualize Cation-pi interactions #
     ####################################
 
-    for i, p in enumerate(pli.pication_paro+pli.pication_laro):
-        cmd.pseudoatom('ps-picat-1-%i' % i, pos=p.ring.center)
-        cmd.pseudoatom('ps-picat-2-%i' % i, pos=p.charge.center)
+    for i, p in enumerate(plcomplex.pication):
+        cmd.pseudoatom('ps-picat-1-%i' % i, pos=p.ring_center)
+        cmd.pseudoatom('ps-picat-2-%i' % i, pos=p.charge_center)
         if p.protcharged:
-            cmd.pseudoatom('Chargecenter-P', pos=p.charge.center)
-            cmd.pseudoatom('Centroids-L', pos=p.ring.center)
-            pilig_ids = '+'.join(map(str, [lig_to_pdb[atm.idx] for atm in p.ring.atoms]))
+            cmd.pseudoatom('Chargecenter-P', pos=p.charge_center)
+            cmd.pseudoatom('Centroids-L', pos=p.ring_center)
+            pilig_ids = '+'.join(map(str, p.ring_atoms))
             cmd.select('PiCatRing-L', 'PiCatRing-L or id %s' % pilig_ids)
-            for a in p.charge.atoms:
-                cmd.select('PosCharge-P', 'PosCharge-P or id %i' % mapping[a.idx])
+            for a in p.charge_atoms:
+                cmd.select('PosCharge-P', 'PosCharge-P or id %i' % a)
         else:
-            cmd.pseudoatom('Chargecenter-L', pos=p.charge.center)
-            cmd.pseudoatom('Centroids-P', pos=p.ring.center)
-            pires_ids = '+'.join(map(str, [mapping[atm.idx] for atm in p.ring.atoms]))
+            cmd.pseudoatom('Chargecenter-L', pos=p.charge_center)
+            cmd.pseudoatom('Centroids-P', pos=p.ring_center)
+            pires_ids = '+'.join(map(str, p.ring_atoms))
             cmd.select('PiCatRing-P', 'PiCatRing-P or id %s' % pires_ids)
-            cmd.select('PosCharge-L', 'PosCharge-L or id %i' % lig_to_pdb[p.charge.atoms[0].idx])
+            for a in p.charge_atoms:
+                cmd.select('PosCharge-L', 'PosCharge-L or id %i' % a)
         cmd.distance('PiCation', 'ps-picat-1-%i' % i, 'ps-picat-2-%i' % i)
     if object_exists('PiCation'):
         cmd.set('dash_color', 'orange', 'PiCation')
@@ -262,30 +366,27 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     # Visualize salt bridges #
     ##########################
 
-    saltbridge_lneg = pli.saltbridge_lneg
-    saltbridge_pneg = pli.saltbridge_pneg
-
-    for i, saltb in enumerate(saltbridge_lneg):
-        for patom in saltb.positive.atoms:
-            cmd.select('PosCharge-P', 'PosCharge-P or id %i' % mapping[patom.idx])
-        for latom in saltb.negative.atoms:
-            cmd.select('NegCharge-L', 'NegCharge-L or id %i' % lig_to_pdb[latom.idx])
-        for sbgroup in [['ps-sbl-1-%i' % i, 'Chargecenter-P', saltb.positive.center],
-                        ['ps-sbl-2-%i' % i, 'Chargecenter-L', saltb.negative.center]]:
-            cmd.pseudoatom(sbgroup[0], pos=sbgroup[2])
-            cmd.pseudoatom(sbgroup[1], pos=sbgroup[2])
-        cmd.distance('Saltbridges', 'ps-sbl-1-%i' % i, 'ps-sbl-2-%i' % i)
-
-    for i, saltb in enumerate(saltbridge_pneg):
-        for patom in saltb.negative.atoms:
-            cmd.select('NegCharge-P', 'NegCharge-P or id %i' % mapping[patom.idx])
-        for latom in saltb.positive.atoms:
-            cmd.select('PosCharge-L', 'PosCharge-L or id %i' % lig_to_pdb[latom.idx])
-        for sbgroup in [['ps-sbp-1-%i' % i, 'Chargecenter-P', saltb.negative.center],
-                        ['ps-sbp-2-%i' % i, 'Chargecenter-L', saltb.positive.center]]:
-            cmd.pseudoatom(sbgroup[0], pos=sbgroup[2])
-            cmd.pseudoatom(sbgroup[1], pos=sbgroup[2])
-        cmd.distance('Saltbridges', 'ps-sbp-1-%i' % i, 'ps-sbp-2-%i' % i)
+    for i, saltb in enumerate(plcomplex.saltbridges):
+        if saltb.protispos:
+            for patom in saltb.positive_atoms:
+                cmd.select('PosCharge-P', 'PosCharge-P or id %i' % patom)
+            for latom in saltb.negative_atoms:
+                cmd.select('NegCharge-L', 'NegCharge-L or id %i' % latom)
+            for sbgroup in [['ps-sbl-1-%i' % i, 'Chargecenter-P', saltb.positive_center],
+                            ['ps-sbl-2-%i' % i, 'Chargecenter-L', saltb.negative_center]]:
+                cmd.pseudoatom(sbgroup[0], pos=sbgroup[2])
+                cmd.pseudoatom(sbgroup[1], pos=sbgroup[2])
+            cmd.distance('Saltbridges', 'ps-sbl-1-%i' % i, 'ps-sbl-2-%i' % i)
+        else:
+            for patom in saltb.negative_atoms:
+                cmd.select('NegCharge-P', 'NegCharge-P or id %i' % patom)
+            for latom in saltb.positive_atoms:
+                cmd.select('PosCharge-L', 'PosCharge-L or id %i' % latom)
+            for sbgroup in [['ps-sbp-1-%i' % i, 'Chargecenter-P', saltb.negative_center],
+                            ['ps-sbp-2-%i' % i, 'Chargecenter-L', saltb.positive_center]]:
+                cmd.pseudoatom(sbgroup[0], pos=sbgroup[2])
+                cmd.pseudoatom(sbgroup[1], pos=sbgroup[2])
+            cmd.distance('Saltbridges', 'ps-sbp-1-%i' % i, 'ps-sbp-2-%i' % i)
 
     if object_exists('Saltbridges'):
         cmd.set('dash_color', 'yellow', 'Saltbridges')
@@ -295,22 +396,17 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     # Water-bridged H-Bonds (first degree) #
     ########################################
 
-    for bridge in pli.water_bridges:
+    for bridge in plcomplex.waterbridges:
         if bridge.protisdon:
-            a_idx = lig_to_pdb[bridge.a.idx]
-            d_idx = mapping[bridge.d.idx]
-            cmd.select('HBondDonor-P', 'HBondDonor-P or id %i' % d_idx)
-            cmd.select('HBondAccept-L', 'HBondAccept-L or id %i' % a_idx)
+            cmd.select('HBondDonor-P', 'HBondDonor-P or id %i' % bridge.don_id)
+            cmd.select('HBondAccept-L', 'HBondAccept-L or id %i' % bridge.acc_id)
         else:
-            a_idx = mapping[bridge.a.idx]
-            d_idx = lig_to_pdb[bridge.d.idx]
-            cmd.select('HBondDonor-L', 'HBondDonor-L or id %i' % d_idx)
-            cmd.select('HBondAccept-P', 'HBondAccept-P or id %i' % a_idx)
-        w_idx = mapping[bridge.water.idx]
-        cmd.select('Water', 'Water or id %i' % w_idx)
-        cmd.select('tmp_don', 'id %i' % d_idx)
-        cmd.select('tmp_water', 'id %i' % w_idx)
-        cmd.select('tmp_acc', 'id %i' % a_idx)
+            cmd.select('HBondDonor-L', 'HBondDonor-L or id %i' % bridge.don_id)
+            cmd.select('HBondAccept-P', 'HBondAccept-P or id %i' % bridge.acc_id)
+        cmd.select('Water', 'Water or id %i' % bridge.water_id)
+        cmd.select('tmp_don', 'id %i' % bridge.don_id)
+        cmd.select('tmp_water', 'id %i' % bridge.water_id)
+        cmd.select('tmp_acc', 'id %i' % bridge.acc_id)
         cmd.distance('WaterBridges', 'tmp_acc', 'tmp_water')
         cmd.distance('WaterBridges', 'tmp_don', 'tmp_water')
     if object_exists('WaterBridges'):
@@ -319,13 +415,38 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     cmd.color('lightblue', 'Water')
     cmd.show('spheres', 'Water')
 
+    ###################
+    # Metal Complexes #
+    ###################
+
+    if not len(plcomplex.metal_complexes) == 0:
+        select_by_ids('Metal-M', metal_ids)
+        for metal_complex in plcomplex.metal_complexes:
+            cmd.select('tmp_m', 'id %i' % metal_complex.metal_id)
+            cmd.select('tmp_t', 'id %i' % metal_complex.target_id)
+            if metal_complex.location == 'water':
+                cmd.select('Metal-W', 'Metal-W or id %s' % metal_complex.target_id)
+            if metal_complex.location.startswith('protein'):
+                cmd.select('Metal-P', 'Metal-P or id %s' % metal_complex.target_id)
+            if metal_complex.location == 'ligand':
+                cmd.select('Metal-L', 'Metal-L or id %s' % metal_complex.target_id)
+            cmd.distance('MetalComplexes', 'tmp_m', 'tmp_t')
+            cmd.delete('tmp_m or tmp_t')
+    if object_exists('MetalComplexes'):
+        cmd.set('dash_color', 'violetpurple', 'MetalComplexes')
+        cmd.set('dash_gap', 0.5, 'MetalComplexes')
+        # Show water molecules for metal complexes
+        cmd.show('spheres', 'Metal-W')
+        cmd.color('lightblue', 'Metal-W')
+
     ######################
     # Visualize the rest #
     ######################
 
     # Show sticks for all residues interacing with the ligand
     cmd.select('AllBSRes', 'byres (Hydrophobic-P or HBondDonor-P or HBondAccept-P or PosCharge-P or NegCharge-P or '
-                           'StackRings-P or PiCatRing-P or HalogenAcc)')
+                           'StackRings-P or PiCatRing-P or HalogenAcc or Metal-P)')
+    # #@todo Check, should be HalogenAccept here?
     cmd.show('sticks', 'AllBSRes')
     # Show spheres for the ring centroids
     cmd.hide('everything', 'centroids*')
@@ -348,16 +469,37 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     cmd.show('sticks', '%sCartoon' % pdbid)
     cmd.set('stick_transparency', 1, '%sCartoon' % pdbid)
     # Set view. Zoom on the ligand (and its pliprofiler)
+
+    cmd.center(ligname)
+    cmd.orient(ligname)
+    cmd.turn('x', 110)  # If the ligand is aligned with the longest axis, aromatic rings are hidden
     if 'AllBSRes' in cmd.get_names("selections"):
-        cmd.zoom('%s or AllBSRes' % ligname)
+        cmd.zoom('%s or AllBSRes' % ligname, 3)
     else:
         if object_exists(ligname):
             cmd.zoom(ligname, 3)
-    cmd.set('sphere_scale', 0.2, 'resn HOH')  # Needs to be done here because of the copy made
-    cmd.set('sphere_transparency', 0.4, '!resn HOH')
+
+    # Resize water molecules. Sometimes they are not heteroatoms HOH, but part of the protein
+    cmd.set('sphere_scale', 0.2, 'resn HOH or Water')  # Needs to be done here because of the copy made
+    cmd.set('sphere_transparency', 0.4, '!(resn HOH or Water)')
+
     cmd.origin(ligname)
     if 'Centroids*' in cmd.get_names("selections"):
         cmd.color('grey80', 'Centroids*')
+    cmd.hide('spheres', '%sCartoon' % pdbid)
+    cmd.hide('cartoon', '%sCartoon and resn DA+DG+DC+DU+DT+A+G+C+U+T' % pdbid)  # Hide DNA/RNA Cartoon
+    if ligname == 'SF4':  # Special case for iron-sulfur clusters, can't be visualized with sticks
+        cmd.show('spheres', '%s' % ligname)
+
+    ##################################
+    # Selections for unpaired groups #
+    ##################################
+    if not len(plcomplex.unpaired_hba_idx) == 0:
+        select_by_ids('Unpaired-HBA', plcomplex.unpaired_hba_idx, selection_exists=True)
+    if not len(plcomplex.unpaired_hbd_idx) == 0:
+        select_by_ids('Unpaired-HBD', plcomplex.unpaired_hbd_idx, selection_exists=True)
+    if not len(plcomplex.unpaired_hal_idx) == 0:
+        select_by_ids('Unpaired-HAL', plcomplex.unpaired_hal_idx, selection_exists=True)
 
     ##############################
     # Organization of selections #
@@ -375,13 +517,14 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     # Group non-empty selections
     cmd.group('Structures', '%s %s %sCartoon' % (pdbid, ligname, pdbid))
     cmd.group('Interactions', 'Hydrophobic HBonds HalogenBonds WaterBridges PiCation PiStackingP PiStackingT '
-                              'Saltbridges')
+                              'Saltbridges MetalComplexes')
     cmd.group('Atoms', '')
     cmd.group('Atoms.Protein', 'Hydrophobic-P HBondAccept-P HBondDonor-P HalogenAccept Centroids-P PiCatRing-P '
-                               'StackRings-P PosCharge-P NegCharge-P AllBSRes Chargecenter-P')
+                               'StackRings-P PosCharge-P NegCharge-P AllBSRes Chargecenter-P  Metal-P')
     cmd.group('Atoms.Ligand', 'Hydrophobic-L HBondAccept-L HBondDonor-L HalogenDonor Centroids-L NegCharge-L '
-                              'PosCharge-L NegCharge-L ChargeCenter-L StackRings-L PiCatRing-L')
-    cmd.group('Atoms.Other', 'Water')
+                              'PosCharge-L NegCharge-L ChargeCenter-L StackRings-L PiCatRing-L Metal-L Metal-M '
+                              'Unpaired-HBA Unpaired-HBD Unpaired-HAL Unpaired-RINGS')
+    cmd.group('Atoms.Other', 'Water Metal-W')
     cmd.order('*', 'y')
 
     ###############################################
@@ -398,11 +541,11 @@ def visualize_in_pymol(protcomplex_class, pli_site, show=False, pics=False, pse=
     cmd.disable('%sCartoon' % pdbid)
     cmd.hide('everything', 'hydrogens')
 
-    filename = '%s-%s' % (pdbid.upper(), "-".join(ligdata.bs_id).upper())
-    if pse:
-        cmd.save("".join([save_to, "%s.pse" % filename]))
+    filename = '%s_%s' % (pdbid.upper(), "_".join([ligname, plcomplex.chain, plcomplex.position]))
+    if config.PYMOL:
+        cmd.save("/".join([config.OUTPATH, "%s.pse" % filename]))
 
     # Create output pictures (experimental)
     set_fancy_ray()
-    if pics:
-        png_workaround("".join([save_to, filename]))
+    if config.PICS:
+        png_workaround("/".join([config.OUTPATH, filename]))
diff --git a/plip/plipcmd b/plip/plipcmd
index 3a678ce..9aa84de 100755
--- a/plip/plipcmd
+++ b/plip/plipcmd
@@ -1,8 +1,8 @@
 #! /usr/bin/env python
 """
 Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
-plip-cmd.py - Main script for PLIP command line execution.
-Copyright 2014 Sebastian Salentin
+plipcmd - Main script for PLIP command line execution.
+Copyright 2014-2015 Sebastian Salentin
 
 Licensed under the Apache License, Version 2.0 (the "License");
 you may not use this file except in compliance with the License.
@@ -21,10 +21,18 @@ limitations under the License.
 from __future__ import print_function
 
 # Own modules
-from plip.modules.preparation import *
-from plip.modules.visualize import visualize_in_pymol
-from plip.modules.report import TextOutput
-from plip.modules import config
+try:
+    from plip.modules.preparation import *
+    from plip.modules.visualize import visualize_in_pymol, PyMOLComplex
+    from plip.modules.report import TextOutput
+    from plip.modules import config
+    from plip.modules.mp import parallel_fn
+except ImportError:
+    from modules.preparation import *
+    from modules.visualize import visualize_in_pymol, PyMOLComplex
+    from modules.report import TextOutput
+    from modules import config
+    from modules.mp import parallel_fn
 
 # Python standard library
 import sys
@@ -37,12 +45,12 @@ import multiprocessing
 # External libraries
 import lxml.etree as et
 
-__version__ = '1.1.0'
+__version__ = '1.3.0'
 descript = "Protein-Ligand Interaction Profiler (PLIP) v%s " \
            "is a command-line based tool to analyze interactions in a protein-ligand complex. " \
            "If you are using PLIP in your work, please cite: " \
            "Salentin,S. et al. PLIP: fully automated protein-ligand interaction profiler. " \
-           "Nucl. Acids Res. first published online April 14, 2015 doi:10.1093/nar/gkv315" % __version__
+           "Nucl. Acids Res. (1 July 2015) 43 (W1): W443-W447. doi: 10.1093/nar/gkv315" % __version__
 
 
 def threshold_limiter(aparser, arg):
@@ -52,12 +60,6 @@ def threshold_limiter(aparser, arg):
     return arg
 
 
-def sysexit(code, msg):
-    """Exit using an custom error message and error code."""
-    sys.stderr.write(msg)
-    sys.exit(code)
-
-
 def check_pdb_status(pdbid):
     """Returns the status and up-to-date entry in the PDB for a given PDB ID"""
     url = 'http://www.rcsb.org/pdb/rest/idStatus?structureId=%s' % pdbid
@@ -73,37 +75,41 @@ def check_pdb_status(pdbid):
     return [status, current_pdbid.lower()]
 
 
-def fetch_pdb(pdbid, verbose_mode):
+def fetch_pdb(pdbid):
     """Get the newest entry from the RCSB server for the given PDB ID. Exits with '1' if PDB ID is invalid."""
     pdbid = pdbid.lower()
-    if verbose_mode:
-        sys.stdout.write('Checking status of PDB ID %s ... ' % pdbid)
+    message('\nChecking status of PDB ID %s ... ' % pdbid)
     state, current_entry = check_pdb_status(pdbid)  # Get state and current PDB ID
 
-    if verbose_mode:
-        if state == 'OBSOLETE':
-            sys.stdout.write('entry is obsolete, getting %s instead.\n' % current_entry)
-        elif state == 'CURRENT':
-            sys.stdout.write('entry is up to date.\n')
-    if state == 'UNKNOWN':
-        sysexit(3, 'Invalid PDB ID')
-    if verbose_mode:
-        sys.stdout.write('Downloading file from PDB ... ')
+    if state == 'OBSOLETE':
+        message('entry is obsolete, getting %s instead.\n' % current_entry)
+    elif state == 'CURRENT':
+        message('entry is up to date.\n')
+    elif state == 'UNKNOWN':
+        sysexit(3, 'Invalid PDB ID (Entry does not exist on PDB server)')
+    message('Downloading file from PDB ... ')
     pdburl = 'http://www.rcsb.org/pdb/files/%s.pdb' % current_entry  # Get URL for current entry
-    pdbfile = None
-    try:
-        pdbfile = urllib2.urlopen(pdburl).read()
-    except urllib2.HTTPError:
-        sysexit(5, "Error: No file in PDB format available from wwPDB for the given PDB ID.")
+    pdbfile = urllib2.urlopen(pdburl).read()
+    # If no PDB file is available, a text is now shown with "We're sorry, but ..."
+    # Could previously be distinguished by an HTTP error
+    if 'sorry' in pdbfile:
+        sysexit(5, "Error: No file in PDB format available from wwPDB for the given PDB ID.\n")
     return [pdbfile, current_entry]
 
 
-def process_pdb(pdbfile, outpath, xml=False, verbose_mode=False, pics=False, pymol=False, maxthreads=None):
+def process_pdb(pdbfile, outpath):
     """Analysis of a single PDB file. Can generate textual reports XML, PyMOL session files and images as output."""
+    startmessage = '\nStarting analysis of %s\n' % pdbfile.split('/')[-1]
+    message(startmessage)
+    message('='*len(startmessage)+'\n')
     mol = PDBComplex()
     mol.output_path = outpath
     mol.load_pdb(pdbfile)
+    # #@todo Offers possibility for filter function from command line (by ligand chain, position, hetid)
+    for ligand in mol.ligands:
+        mol.characterize_complex(ligand)
     excluded = mol.excluded
+    create_folder_if_not_exists(outpath)
 
     # Begin constructing the XML tree
     report = et.Element('report')
@@ -111,135 +117,133 @@ def process_pdb(pdbfile, outpath, xml=False, verbose_mode=False, pics=False, pym
     plipversion.text = __version__
     pdbid = et.SubElement(report, 'pdbid')
     pdbid.text = mol.pymol_name.upper()
+    filetype = et.SubElement(report, 'filetype')
+    filetype.text = mol.filetype.upper()
+    pdbfile = et.SubElement(report, 'pdbfile')
+    pdbfile.text = mol.sourcefiles['pdbcomplex']
+    pdbfixes = et.SubElement(report, 'pdbfixes')
+    pdbfixes.text = str(mol.information['pdbfixes'])
+    filename = et.SubElement(report, 'filename')
+    filename.text = str(mol.sourcefiles['filename'])
     exligs = et.SubElement(report, 'excluded_ligands')
     for i, exlig in enumerate(excluded):
-        e = et.SubElement(exligs, 'excluded_ligand', id=str(i+1))
+        e = et.SubElement(exligs, 'excluded_ligand', id=str(i + 1))
         e.text = exlig
 
     # Write header of rST file
     textlines = ['Prediction of noncovalent interactions for PDB structure %s' % mol.pymol_name.upper(), ]
-    textlines.append("="*len(textlines[0]))
+    textlines.append("=" * len(textlines[0]))
     textlines.append('Created on %s using PLIP v%s\n' % (time.strftime("%Y/%m/%d"), __version__))
     if len(excluded) != 0:
         textlines.append('Excluded molecules as ligands: %s\n' % ','.join([lig for lig in excluded]))
 
-    if verbose_mode:
-        if len(excluded) == 0:
-            sys.stdout.write("No molecules excluded as ligands.\n")
-        else:
-            sys.stdout.write("Excluded molecules as ligands: %s\n" % ','.join([lig for lig in excluded]))
-        num_ligs = len([site for site in mol.interaction_sets if not mol.interaction_sets[site].no_interactions])
-        if num_ligs == 1:
-            sys.stdout.write("Analyzing %s with one ligand:\n" % mol.pymol_name)
-        elif num_ligs > 1:
-            sys.stdout.write("Analyzing %s with %i ligands:\n" % (mol.pymol_name, num_ligs))
-        else:
-            sys.stdout.write("%s contains no ligands.\n" % mol.pymol_name)
+    config.MAXTHREADS = min(config.MAXTHREADS, len(mol.interaction_sets))
+
+    ######################################
+    # PyMOL Visualization (parallelized) #
+    ######################################
 
-    ######################################################################################################
-    # Generate XML- and rST-formatted reports for each binding site and initialize visualization threads #
-    ######################################################################################################
+    if config.PYMOL or config.PICS:
+        complexes = [PyMOLComplex(mol, site) for site in sorted(mol.interaction_sets)
+                     if not len(mol.interaction_sets[site].interacting_res) == 0]
+        if config.MAXTHREADS > 1:
+            message('\nGenerating visualizations in parallel on %i cores ...' % config.MAXTHREADS)
+            parfn = parallel_fn(visualize_in_pymol)
+            parfn(complexes, processes=config.MAXTHREADS)
+        else:
+            [visualize_in_pymol(plcomplex) for plcomplex in complexes]
 
-    threads = []
-    running_threads = []
+    ##################################################################
+    # Generate XML- and rST-formatted reports for each binding site. #
+    ##################################################################
 
     for i, site in enumerate(sorted(mol.interaction_sets)):
         s = mol.interaction_sets[site]
         bindingsite = TextOutput(s).generate_xml()
-        bindingsite.set('id', str(i+1))
+        bindingsite.set('id', str(i + 1))
         bindingsite.set('has_interactions', 'False')
-        report.insert(i+1, bindingsite)
-        for itype in TextOutput(s).generate_rst():
+        report.insert(i + 1, bindingsite)
+        for itype in TextOutput(s).generate_txt():
             textlines.append(itype)
         if not s.no_interactions:
             bindingsite.set('has_interactions', 'True')
-            if verbose_mode:
-                sys.stdout.write("  @ %s\n" % site)
-
-            if pymol or pics:
-                if os.name != 'nt':
-                    if maxthreads != 0:
-                        # Initialize thread for PyMOL visualization and add to list of threads to be processed
-                        p = multiprocessing.Process(target=visualize_in_pymol, args=(mol, site, False, pics, pymol))
-                        threads.append(p)
-                    else:
-                        visualize_in_pymol(mol, site, False, pics, pymol)
-                else:
-                    visualize_in_pymol(mol, site, False, pics, pymol)
         else:
             textlines.append('No interactions detected.')
         sys.stdout = sys.__stdout__  # Change back to original stdout, gets changed when PyMOL has been used before
 
-    ##############################################
-    # Use multithreading for PyMOL visualization #
-    ##############################################
-
-    if maxthreads is None:  # Use as many threads as there are processor cores (should be a safe value)
-        maxthreads = multiprocessing.cpu_count()
-    else:
-        maxthreads = max(2, maxthreads)
-    while len(threads) != 0:
-        # Add threads as long as there are free threads available
-        for i, tr in enumerate(threads):
-            if len(running_threads) <= maxthreads-2:  # One can be still added, one used for the main process
-                tr.start()
-                running_threads.append(tr)
-                threads.pop(i)
-        # Check if running threads have finished and delete them
-        for j, tr in enumerate(running_threads):
-            if not tr.is_alive():
-                running_threads.pop(j)
-
-    ###########################################
-    # Write final rST and XML to output files #
-    ###########################################
-
     tree = et.ElementTree(report)
-    create_folder_if_not_exists(tilde_expansion(outpath))
-    if xml:
-        tree.write('%s/report.xml' % tilde_expansion(outpath), pretty_print=True, xml_declaration=True)
+    if config.XML:  # Generate report in xml format
+        tree.write('%s/report.xml' % outpath, pretty_print=True, xml_declaration=True)
 
-    with open('%s/report.rst.txt' % tilde_expansion(outpath), 'w') as f:
-        [f.write(textline+'\n') for textline in textlines]
+    if config.TXT:  # Generate report in txt (rst) format
+        with open('%s/report.txt' % outpath, 'w') as f:
+            [f.write(textline + '\n') for textline in textlines]
 
-
-def main(args):
+def download_structure(inputpdbid):
+    """Given a PDB ID, downloads the corresponding PDB structure.
+    Checks for validity of ID and handles error while downloading.
+    Returns the path of the downloaded file."""
+    try:
+        if len(inputpdbid) != 4 or extract_pdbid(inputpdbid.lower()) == 'UnknownProtein':
+            sysexit(3, 'Error: Invalid PDB ID (Wrong format)')
+        pdbfile, pdbid = fetch_pdb(inputpdbid.lower())
+        pdbpath = tilde_expansion('%s/%s.pdb' % (config.BASEPATH.rstrip('/'), pdbid))
+        create_folder_if_not_exists(config.BASEPATH)
+        with open(pdbpath, 'w') as g:
+            g.write(pdbfile)
+        message('file downloaded as %s\n\n' % pdbpath)
+        return pdbpath, pdbid
+
+    except ValueError:  # Invalid PDB ID, cannot fetch from RCBS server
+        sysexit(3, 'Error: Invalid PDB ID (Entry does not exist)')
+
+def remove_duplicates(slist):
+    """Checks input lists for duplicates and returns
+    a list with unique entries"""
+    unique = list(set(slist))
+    difference = len(slist) - len(unique)
+    if difference == 1:
+        message("Removed one duplicate entry from input list.\n")
+    if difference > 1:
+        message("Removed %i duplicate entries from input list.\n" % difference)
+    return unique
+
+
+def main(inputstructs, inputpdbids):
     """Main function. Calls functions for processing, report generation and visualization."""
-    pdbid, outp = None, None
-    outp = "".join([args.outpath, '/']) if not args.outpath.endswith('/') else args.outpath
-
-    if args.verbose:
-        # Print title and version
-        title = "* Protein-Ligand Interaction Profiler v%s *" % __version__
-        sys.stdout.write('\n'+'*'*len(title)+'\n')
-        sys.stdout.write(title)
-        sys.stdout.write('\n'+'*'*len(title)+'\n\n')
-
-    if args.input is not None:  # Process PDB file
-        if os.path.getsize(args.input) == 0:
-            sysexit(2, 'Error: Empty PDB file')  # Exit if input file is empty
-        process_pdb(args.input, outp, xml=args.xml, verbose_mode=args.verbose, pics=args.pics, pymol=args.pymol,
-                    maxthreads=int(args.maxthreads))
-    else:  # Try to fetch the current PDB structure directly from the RCBS server
-        try:
-            pdbfile, pdbid = fetch_pdb(args.pdbid.lower(), verbose_mode=args.verbose)
-            pdbpath = '%s/%s.pdb' % (args.outpath.rstrip('/'), pdbid)
-            create_folder_if_not_exists(args.outpath)
-
-            if args.verbose:
-                sys.stdout.write('file downloaded as %s\n\n' % pdbpath)
-
-            with open(tilde_expansion(pdbpath), 'w') as g:
-                g.write(pdbfile)
-            process_pdb(tilde_expansion(pdbpath), tilde_expansion(outp), xml=args.xml, verbose_mode=args.verbose,
-                        pics=args.pics, pymol=args.pymol, maxthreads=int(args.maxthreads))
-        except ValueError:  # Invalid PDB ID, cannot fetch from RCBS server
-            sysexit(3, 'Error: Invalid PDB ID')
-    if pdbid is not None and outp is not None:
-        if outp in ['.', './']:
-            outp = 'the working directory.'
-        if args.verbose:
-            sys.stdout.write('\nNearly finished with analysis of %s. Find the result files in %s\n\n' % (pdbid, outp))
+    pdbid, pdbpath = None, None
+    # #@todo For multiprocessing, implement better stacktracing for errors
+
+    # Print title and version
+    title = "* Protein-Ligand Interaction Profiler v%s *" % __version__
+    message('\n' + '*' * len(title) + '\n')
+    message(title)
+    message('\n' + '*' * len(title) + '\n\n')
+
+    if inputstructs is not None:  # Process PDB file(s)
+        num_structures = len(inputstructs)
+        inputstructs = remove_duplicates(inputstructs)
+        for inputstruct in inputstructs:
+            if os.path.getsize(inputstruct) == 0:
+                sysexit(2, 'Error: Empty PDB file')  # Exit if input file is empty
+            if num_structures > 1:
+                basename = inputstruct.split('.')[0].split('/')[-1]
+                config.OUTPATH = '/'.join([config.BASEPATH, basename])
+            process_pdb(inputstruct, config.OUTPATH)
+    else:  # Try to fetch the current PDB structure(s) directly from the RCBS server
+        num_pdbids = len(inputpdbids)
+        inputpdbids =remove_duplicates(inputpdbids)
+        for inputpdbid in inputpdbids:
+            pdbpath, pdbid = download_structure(inputpdbid)
+            if num_pdbids > 1:
+                config.OUTPATH = '/'.join([config.BASEPATH, pdbid[1:3].upper(), pdbid.upper()])
+            process_pdb(pdbpath, config.OUTPATH)
+
+    if (pdbid is not None or inputstructs is not None) and config.BASEPATH is not None:
+        if config.BASEPATH in ['.', './']:
+            message('\nFinished analysis. Find the result files in the working directory.\n\n')
+        else:
+            message('\nFinished analysis. Find the result files in %s\n\n' % config.BASEPATH)
 
 if __name__ == '__main__':
 
@@ -249,18 +253,31 @@ if __name__ == '__main__':
 
     parser = ArgumentParser(prog="PLIP", description=descript)
     pdbstructure = parser.add_mutually_exclusive_group(required=True)  # Needs either PDB ID or file
-    pdbstructure.add_argument("-f", "--file", dest="input")
-    pdbstructure.add_argument("-i", "--input", dest="pdbid")
+    pdbstructure.add_argument("-f", "--file", dest="input", nargs="+")
+    pdbstructure.add_argument("-i", "--input", dest="pdbid", nargs="+")
     parser.add_argument("-o", "--out", dest="outpath", default="./")
     parser.add_argument("-v", "--verbose", dest="verbose", default=False, help="Set verbose mode", action="store_true")
     parser.add_argument("-p", "--pics", dest="pics", default=False, help="Additional pictures", action="store_true")
-    parser.add_argument("-x", "--xml", dest="xml", default=False, help="Additional XML output for reports",
+    parser.add_argument("-x", "--xml", dest="xml", default=False, help="Generate report file in XML format",
+                        action="store_true")
+    parser.add_argument("-t", "--txt", dest="txt", default=False, help="Generate report file in TXT (RST) format",
                         action="store_true")
     parser.add_argument("-y", "--pymol", dest="pymol", default=False, help="Additional PyMOL session files",
                         action="store_true")
-    parser.add_argument("--maxthreads", dest="maxthreads", default=1,
-                        help="Set maximum number of main threads (number of binding sites processed simultaneously)",
+    parser.add_argument("--maxthreads", dest="maxthreads", default=multiprocessing.cpu_count(),
+                        help="Set maximum number of main threads (number of binding sites processed simultaneously)."
+                             "If not set, PLIP uses all available CPUs if possible.",
                         type=int)
+    parser.add_argument("--breakcomposite", dest="breakcomposite", default=False,
+                        help="Don't combine ligand fragments into with covalent bonds but treat them as single ligands"
+                             "fot the analysis.",
+                        action="store_true")
+    parser.add_argument("--altlocation", dest="altlocation", default=False,
+                        help="Also consider alternate locations for atoms (e.g. alternate conformations).",
+                        action="store_true")
+    parser.add_argument("--debug", dest="debug", default=False,
+                        help="Turn on DEBUG mode with extended log.",
+                        action="store_true")
     # Optional threshold arguments, not shown in help
     thr = namedtuple('threshold', 'name type')
     thresholds = [thr(name='aromatic_planarity', type='angle'),
@@ -278,6 +295,16 @@ if __name__ == '__main__':
                             help=argparse.SUPPRESS)
 
     arguments = parser.parse_args()
+    config.VERBOSE = True if (arguments.verbose or arguments.debug) else False
+    config.DEBUG = True if arguments.debug else False
+    config.MAXTHREADS = arguments.maxthreads
+    config.XML, config.TXT, config.PICS, config.PYMOL = arguments.xml, arguments.txt, arguments.pics, arguments.pymol
+    config.OUTPATH = arguments.outpath
+    config.OUTPATH = tilde_expansion("".join([config.OUTPATH, '/'])
+                                     if not config.OUTPATH.endswith('/') else config.OUTPATH)
+    config.BASEPATH = config.OUTPATH  # Used for batch processing
+    config.BREAKCOMPOSITE = arguments.breakcomposite
+    config.ALTLOC = arguments.altlocation
     # Assign values to global thresholds
     for t in thresholds:
         tvalue = getattr(arguments, t.name)
@@ -287,7 +314,7 @@ if __name__ == '__main__':
             if t.type == 'distance':
                 if tvalue > 10:  # Check value for angle thresholds
                     parser.error("Threshold for distances must not be larger than 10 Angstrom.")
-                elif tvalue > config.BS_DIST+1:  # Dynamically adapt the search space for binding site residues
+                elif tvalue > config.BS_DIST + 1:  # Dynamically adapt the search space for binding site residues
                     config.BS_DIST = tvalue + 1
             setattr(config, t.name.upper(), tvalue)
     # Check additional conditions for interdependent thresholds
@@ -299,4 +326,5 @@ if __name__ == '__main__':
         parser.error("The water bridge minimum distance has to be smaller than the water bridge maximum distance.")
     if not config.WATER_BRIDGE_OMEGA_MIN < config.WATER_BRIDGE_OMEGA_MAX:
         parser.error("The water bridge omega minimum angle has to be smaller than the water bridge omega maximum angle")
-    main(arguments)  # Start main script
+    expanded_path = tilde_expansion(arguments.input) if arguments.input is not None else None
+    main(expanded_path, arguments.pdbid)  # Start main script
diff --git a/plip/test/pdb/1acj.pdb b/plip/test/pdb/1acj.pdb
deleted file mode 100644
index ad226a1..0000000
--- a/plip/test/pdb/1acj.pdb
+++ /dev/null
@@ -1,4774 +0,0 @@
-HEADER    HYDROLASE(CARBOXYLIC ESTERASE)          18-AUG-93   1ACJ              
-TITLE     QUATERNARY LIGAND BINDING TO AROMATIC RESIDUES IN THE                 
-TITLE    2 ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE                            
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 EC: 3.1.1.7;                                                         
-COMPND   5 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;                            
-SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
-SOURCE   4 ORGANISM_TAXID: 7787                                                 
-KEYWDS    HYDROLASE(CARBOXYLIC ESTERASE)                                        
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    J.L.SUSSMAN,M.HAREL,I.SILMAN                                          
-REVDAT   3   24-FEB-09 1ACJ    1       VERSN                                    
-REVDAT   2   01-APR-03 1ACJ    1       JRNL                                     
-REVDAT   1   31-AUG-94 1ACJ    0                                                
-JRNL        AUTH   M.HAREL,I.SCHALK,L.EHRET-SABATIER,F.BOUET,                   
-JRNL        AUTH 2 M.GOELDNER,C.HIRTH,P.H.AXELSEN,I.SILMAN,J.L.SUSSMAN          
-JRNL        TITL   QUATERNARY LIGAND BINDING TO AROMATIC RESIDUES IN            
-JRNL        TITL 2 THE ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE.               
-JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  90  9031 1993              
-JRNL        REFN                   ISSN 0027-8424                               
-JRNL        PMID   8415649                                                      
-JRNL        DOI    10.1073/PNAS.90.19.9031                                      
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   J.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN,               
-REMARK   1  AUTH 2 L.TOKER,I.SILMAN                                             
-REMARK   1  TITL   ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM                
-REMARK   1  TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC                            
-REMARK   1  TITL 3 ACETYLCHOLINE-BINDING PROTEIN                                
-REMARK   1  REF    SCIENCE                       V. 253   872 1991              
-REMARK   1  REFN                   ISSN 0036-8075                               
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : X-PLOR                                               
-REMARK   3   AUTHORS     : BRUNGER                                              
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
-REMARK   3   NUMBER OF REFLECTIONS             : 23213                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
-REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
-REMARK   3   R VALUE            (WORKING SET) : 0.195                           
-REMARK   3   FREE R VALUE                     : NULL                            
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
-REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
-REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
-REMARK   3   BIN FREE R VALUE                    : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 4095                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 15                                      
-REMARK   3   SOLVENT ATOMS            : 82                                      
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
-REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.025                           
-REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
-REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: THE STRUCTURE WAS REFINED STARTING        
-REMARK   3  FROM NATIVE COORDINATES USING X-PLOR. 82 WATER MOLECULES ARE        
-REMARK   3  INCLUDED.                                                           
-REMARK   4                                                                      
-REMARK   4 1ACJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : NULL                               
-REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
-REMARK 200  PH                             : NULL                               
-REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
-REMARK 200  RADIATION SOURCE               : NULL                               
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
-REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : NULL                               
-REMARK 200  DETECTOR MANUFACTURER          : NULL                               
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
-REMARK 200  DATA SCALING SOFTWARE          : NULL                               
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
-REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
-REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
-REMARK 200 SOFTWARE USED: X-PLOR                                                
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 70.97                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.24                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -Y,X-Y,Z+1/3                                            
-REMARK 290       3555   -X+Y,-X,Z+2/3                                           
-REMARK 290       4555   Y,X,-Z                                                  
-REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
-REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.03333            
-REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       92.06667            
-REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       92.06667            
-REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       46.03333            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     ASP A     1                                                      
-REMARK 465     ASP A     2                                                      
-REMARK 465     HIS A     3                                                      
-REMARK 465     HIS A   486                                                      
-REMARK 465     SER A   487                                                      
-REMARK 465     GLN A   488                                                      
-REMARK 465     GLU A   489                                                      
-REMARK 465     GLU A   536                                                      
-REMARK 465     THR A   537                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     ARG A  19    NE   CZ   NH1  NH2                                  
-REMARK 470     HIS A  26    CG   ND1  CD2  CE1  NE2                             
-REMARK 470     ASN A  42    CG   OD1  ND2                                       
-REMARK 470     ARG A  46    CZ   NH1  NH2                                       
-REMARK 470     GLN A  74    OE1  NE2                                            
-REMARK 470     ARG A  88    NH1  NH2                                            
-REMARK 470     GLU A  89    CD   OE1  OE2                                       
-REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
-REMARK 470     GLN A 162    CD   OE1  NE2                                       
-REMARK 470     GLU A 163    OE1  OE2                                            
-REMARK 470     ASN A 253    OD1  ND2                                            
-REMARK 470     ASN A 257    CG   OD1  ND2                                       
-REMARK 470     GLU A 260    CG   CD   OE1  OE2                                  
-REMARK 470     GLU A 261    CD   OE1  OE2                                       
-REMARK 470     GLU A 268    CD   OE1  OE2                                       
-REMARK 470     LYS A 270    CD   CE   NZ                                        
-REMARK 470     PHE A 284    CD1  CD2  CE1  CE2  CZ                              
-REMARK 470     SER A 286    OG                                                  
-REMARK 470     GLU A 299    CD   OE1  OE2                                       
-REMARK 470     ASN A 310    CG   OD1  ND2                                       
-REMARK 470     LYS A 325    NZ                                                  
-REMARK 470     GLU A 344    CD   OE1  OE2                                       
-REMARK 470     GLU A 350    CD   OE1  OE2                                       
-REMARK 470     MET A 353    SD   CE                                             
-REMARK 470     ASP A 365    CG   OD1  OD2                                       
-REMARK 470     ASN A 382    CG   OD1  ND2                                       
-REMARK 470     LYS A 413    CE   NZ                                             
-REMARK 470     GLU A 434    CD   OE1  OE2                                       
-REMARK 470     GLU A 455    CG   CD   OE1  OE2                                  
-REMARK 470     GLU A 461    CD   OE1  OE2                                       
-REMARK 470     LYS A 478    CE   NZ                                             
-REMARK 470     GLU A 484    CD   OE1  OE2                                       
-REMARK 470     LYS A 498    CG   CD   CE   NZ                                   
-REMARK 470     GLU A 499    CD   OE1  OE2                                       
-REMARK 470     GLU A 508    CD   OE1  OE2                                       
-REMARK 470     LYS A 511    CD   CE   NZ                                        
-REMARK 470     ARG A 515    CZ   NH1  NH2                                       
-REMARK 470     GLN A 526    CD   OE1  NE2                                       
-REMARK 470     ASN A 533    CG   OD1  ND2                                       
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
-REMARK 500    TRP A  54   CE2   TRP A  54   CD2     0.076                       
-REMARK 500    HIS A 159   CG    HIS A 159   CD2     0.060                       
-REMARK 500    TRP A 179   CE2   TRP A 179   CD2     0.079                       
-REMARK 500    HIS A 181   CG    HIS A 181   CD2     0.066                       
-REMARK 500    HIS A 209   CG    HIS A 209   CD2     0.064                       
-REMARK 500    TRP A 233   CE2   TRP A 233   CD2     0.077                       
-REMARK 500    HIS A 264   CG    HIS A 264   CD2     0.068                       
-REMARK 500    TRP A 279   CE2   TRP A 279   CD2     0.079                       
-REMARK 500    HIS A 362   CG    HIS A 362   CD2     0.057                       
-REMARK 500    HIS A 398   CG    HIS A 398   CD2     0.066                       
-REMARK 500    HIS A 406   CG    HIS A 406   CD2     0.060                       
-REMARK 500    HIS A 425   CG    HIS A 425   CD2     0.060                       
-REMARK 500    TRP A 432   CE2   TRP A 432   CD2     0.074                       
-REMARK 500    TRP A 435   CE2   TRP A 435   CD2     0.075                       
-REMARK 500    HIS A 440   CG    HIS A 440   CD2     0.064                       
-REMARK 500    HIS A 471   CG    HIS A 471   CD2     0.061                       
-REMARK 500    TRP A 473   CE2   TRP A 473   CD2     0.072                       
-REMARK 500    HIS A 513   CG    HIS A 513   CD2     0.063                       
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    ARG A  47   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
-REMARK 500    ARG A  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES          
-REMARK 500    ARG A 216   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
-REMARK 500    ARG A 267   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
-REMARK 500    SER A 343   N   -  CA  -  CB  ANGL. DEV. =  -9.5 DEGREES          
-REMARK 500    PHE A 414   CB  -  CG  -  CD2 ANGL. DEV. =  -6.3 DEGREES          
-REMARK 500    PHE A 414   CB  -  CG  -  CD1 ANGL. DEV. =   8.0 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    GLU A   5      -54.44     82.74                                   
-REMARK 500    LEU A  23     -117.52     58.24                                   
-REMARK 500    SER A  25     -148.71   -130.90                                   
-REMARK 500    PHE A  45      -13.00     77.90                                   
-REMARK 500    ALA A  60       54.33   -114.64                                   
-REMARK 500    CYS A  94       10.02   -140.13                                   
-REMARK 500    PHE A 120       -7.55     71.73                                   
-REMARK 500    HIS A 159      -71.17    -18.74                                   
-REMARK 500    ASN A 167       18.23     45.27                                   
-REMARK 500    ASN A 183       -2.07   -150.41                                   
-REMARK 500    THR A 193       51.16   -142.72                                   
-REMARK 500    SER A 200     -122.35     61.05                                   
-REMARK 500    ARG A 220      -67.37    -99.61                                   
-REMARK 500    GLU A 299      -76.18   -107.66                                   
-REMARK 500    ASP A 326       78.45   -116.39                                   
-REMARK 500    SER A 329      -63.42    -24.13                                   
-REMARK 500    SER A 345       69.41     30.02                                   
-REMARK 500    VAL A 360       65.15   -118.47                                   
-REMARK 500    ASP A 380       30.81   -162.16                                   
-REMARK 500    ASP A 381      -55.24    -23.32                                   
-REMARK 500    VAL A 400      -54.20   -133.32                                   
-REMARK 500    ASN A 416       40.81   -109.87                                   
-REMARK 500    LYS A 498      -73.98    -69.78                                   
-REMARK 500    GLN A 500       73.98    -63.70                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
-REMARK 500                                                                      
-REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
-REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
-REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
-REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
-REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        RMS     TYPE                                    
-REMARK 500    TYR A 442         0.06    SIDE_CHAIN                              
-REMARK 500    TYR A 458         0.07    SIDE_CHAIN                              
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
-REMARK 500                                                                      
-REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
-REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
-REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
-REMARK 500                                                                      
-REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
-REMARK 500     HIS A 159        21.9      L          L   OUTSIDE RANGE          
-REMARK 500     CYS A 402        24.7      L          L   OUTSIDE RANGE          
-REMARK 500     TYR A 442        22.8      L          L   OUTSIDE RANGE          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A 649        DISTANCE =  7.43 ANGSTROMS                       
-REMARK 525    HOH A 650        DISTANCE =  6.42 ANGSTROMS                       
-REMARK 525    HOH A 654        DISTANCE =  5.16 ANGSTROMS                       
-REMARK 525    HOH A 664        DISTANCE =  6.40 ANGSTROMS                       
-REMARK 525    HOH A 668        DISTANCE =  5.22 ANGSTROMS                       
-REMARK 600                                                                      
-REMARK 600 HETEROGEN                                                            
-REMARK 600 RESIDUE THA 999 IS BOUND NON-COVALENTLY IN THE ACTIVE SITE.          
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: THA                                                 
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: NULL                                               
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THA A 999                 
-DBREF  1ACJ A    1   535  UNP    P04058   ACES_TORCA      22    556             
-SEQRES   1 A  537  ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY          
-SEQRES   2 A  537  LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS          
-SEQRES   3 A  537  ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO          
-SEQRES   4 A  537  VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS          
-SEQRES   5 A  537  PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN          
-SEQRES   6 A  537  ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE          
-SEQRES   7 A  537  SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER          
-SEQRES   8 A  537  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO          
-SEQRES   9 A  537  ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY          
-SEQRES  10 A  537  GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR          
-SEQRES  11 A  537  ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU          
-SEQRES  12 A  537  VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU          
-SEQRES  13 A  537  ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY          
-SEQRES  14 A  537  LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP          
-SEQRES  15 A  537  ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR          
-SEQRES  16 A  537  ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET          
-SEQRES  17 A  537  HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG          
-SEQRES  18 A  537  ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA          
-SEQRES  19 A  537  SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU          
-SEQRES  20 A  537  LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU          
-SEQRES  21 A  537  GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU          
-SEQRES  22 A  537  LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER          
-SEQRES  23 A  537  ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU          
-SEQRES  24 A  537  PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY          
-SEQRES  25 A  537  ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS          
-SEQRES  26 A  537  ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY          
-SEQRES  27 A  537  PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP          
-SEQRES  28 A  537  PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN          
-SEQRES  29 A  537  ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP          
-SEQRES  30 A  537  TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY          
-SEQRES  31 A  537  LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO          
-SEQRES  32 A  537  LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN          
-SEQRES  33 A  537  GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN          
-SEQRES  34 A  537  LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR          
-SEQRES  35 A  537  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU          
-SEQRES  36 A  537  LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG          
-SEQRES  37 A  537  ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN          
-SEQRES  38 A  537  PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU          
-SEQRES  39 A  537  PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR          
-SEQRES  40 A  537  GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET          
-SEQRES  41 A  537  CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN          
-SEQRES  42 A  537  ALA THR GLU THR                                              
-HET    THA  A 999      15                                                       
-HETNAM     THA TACRINE                                                          
-FORMUL   2  THA    C13 H14 N2                                                   
-FORMUL   3  HOH   *82(H2 O)                                                     
-HELIX    1  H1 SER A   79  ASN A   85  1                                   7    
-HELIX    2  H2 GLY A  132  GLU A  139  1                                   8    
-HELIX    3  H3 VAL A  168  ASN A  183  1                                  16    
-HELIX    4  H4 SER A  200  LEU A  211  1                                  12    
-HELIX    5  H5 VAL A  238  LEU A  252  1                                  15    
-HELIX    6  H6 ASP A  259  GLU A  268  1                                  10    
-HELIX    7  H7 PRO A  271  GLU A  278  1                                   8    
-HELIX    8  H8 LEU A  305  SER A  311  1                                   7    
-HELIX    9  H9 SER A  329  GLY A  335  1                                   7    
-HELIX   10 H10 ARG A  349  VAL A  360  1                                  12    
-HELIX   11 H11 ASP A  365  THR A  376  1                                  12    
-HELIX   12 H12 GLY A  384  TYR A  411  1                                  28    
-HELIX   13 H13 GLU A  443  PHE A  448  1                                   6    
-HELIX   14 H14 ALA A  460  THR A  479  1                                  20    
-HELIX   15 H15 VAL A  518  ALA A  534  1                                  17    
-SHEET    1  S112 LEU A   6  THR A  10  0                                        
-SHEET    2  S112 GLY A  13  MET A  16 -1                                        
-SHEET    3  S112 THR A  18  PRO A  21 -1                                        
-SHEET    4  S112 HIS A  26  PRO A  34 -1                                        
-SHEET    5  S112 VAL A  57  ALA A  60 -1                                        
-SHEET    6  S112 TYR A  96  PRO A 102 -1                                        
-SHEET    7  S112 VAL A 142  SER A 147 -1                                        
-SHEET    8  S112 THR A 109  TYR A 116  1                                        
-SHEET    9  S112 THR A 193  GLU A 199  1                                        
-SHEET   10  S112 ARG A 220  SER A 226  1                                        
-SHEET   11  S112 GLN A 318  TYR A 334  1                                        
-SHEET   12  S112 GLY A 417  PHE A 423  1                                        
-SHEET    1  S2 2 PHE A 502  LEU A 505  0                                        
-SHEET    2  S2 2 MET A 510  GLN A 514 -1                                        
-SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.04  
-SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.03  
-SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.07  
-CISPEP   1 SER A  103    PRO A  104          0        -4.12                     
-SITE     1 THA  4 SER A 200  HIS A 440  GLU A 327  THA A 999                    
-SITE     1 AC1  7 TRP A  84  GLY A 118  GLU A 199  PHE A 330                    
-SITE     2 AC1  7 TRP A 432  HIS A 440  GLY A 441                               
-CRYST1  113.700  113.700  138.100  90.00  90.00 120.00 P 31 2 1      6          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.008795  0.005078  0.000000        0.00000                         
-SCALE2      0.000000  0.010156  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.007241        0.00000                         
-ATOM      1  N   SER A   4     -12.503  89.084  35.130  1.00 66.28           N  
-ATOM      2  CA  SER A   4     -12.189  87.877  35.866  1.00 63.52           C  
-ATOM      3  C   SER A   4     -11.066  88.196  36.842  1.00 59.52           C  
-ATOM      4  O   SER A   4     -11.260  89.101  37.633  1.00 57.70           O  
-ATOM      5  CB  SER A   4     -12.025  86.720  34.856  1.00 67.07           C  
-ATOM      6  OG  SER A   4     -13.195  86.792  34.018  1.00 70.02           O  
-ATOM      7  N   GLU A   5      -9.920  87.515  36.768  1.00 54.99           N  
-ATOM      8  CA  GLU A   5      -8.763  87.673  37.662  1.00 47.42           C  
-ATOM      9  C   GLU A   5      -9.082  86.841  38.872  1.00 43.05           C  
-ATOM     10  O   GLU A   5      -8.332  85.956  39.236  1.00 44.40           O  
-ATOM     11  CB  GLU A   5      -8.315  89.106  38.012  1.00 47.14           C  
-ATOM     12  CG  GLU A   5      -7.047  89.190  38.917  1.00 51.13           C  
-ATOM     13  CD  GLU A   5      -5.714  88.670  38.353  1.00 52.76           C  
-ATOM     14  OE1 GLU A   5      -5.502  88.765  37.150  1.00 54.93           O  
-ATOM     15  OE2 GLU A   5      -4.880  88.179  39.122  1.00 56.48           O  
-ATOM     16  N   LEU A   6     -10.253  87.138  39.444  1.00 36.79           N  
-ATOM     17  CA  LEU A   6     -10.748  86.426  40.612  1.00 32.75           C  
-ATOM     18  C   LEU A   6     -11.840  85.431  40.295  1.00 33.35           C  
-ATOM     19  O   LEU A   6     -12.296  84.700  41.162  1.00 35.53           O  
-ATOM     20  CB  LEU A   6     -11.321  87.429  41.633  1.00 28.61           C  
-ATOM     21  CG  LEU A   6     -10.276  87.885  42.667  1.00 29.95           C  
-ATOM     22  CD1 LEU A   6      -9.060  88.579  42.040  1.00 28.52           C  
-ATOM     23  CD2 LEU A   6     -10.937  88.762  43.732  1.00 28.46           C  
-ATOM     24  N   LEU A   7     -12.302  85.444  39.053  1.00 33.35           N  
-ATOM     25  CA  LEU A   7     -13.363  84.515  38.679  1.00 33.07           C  
-ATOM     26  C   LEU A   7     -12.689  83.488  37.822  1.00 32.11           C  
-ATOM     27  O   LEU A   7     -12.018  83.906  36.874  1.00 36.48           O  
-ATOM     28  CB  LEU A   7     -14.409  85.233  37.811  1.00 33.65           C  
-ATOM     29  CG  LEU A   7     -15.741  84.489  37.662  1.00 33.73           C  
-ATOM     30  CD1 LEU A   7     -15.669  83.103  37.017  1.00 34.68           C  
-ATOM     31  CD2 LEU A   7     -16.471  84.394  38.993  1.00 34.90           C  
-ATOM     32  N   VAL A   8     -12.856  82.204  38.136  1.00 24.81           N  
-ATOM     33  CA  VAL A   8     -12.232  81.181  37.334  1.00 21.36           C  
-ATOM     34  C   VAL A   8     -13.261  80.103  37.069  1.00 25.40           C  
-ATOM     35  O   VAL A   8     -14.082  79.793  37.921  1.00 27.94           O  
-ATOM     36  CB  VAL A   8     -11.015  80.653  38.107  1.00 15.33           C  
-ATOM     37  CG1 VAL A   8     -10.339  79.451  37.430  1.00 17.12           C  
-ATOM     38  CG2 VAL A   8      -9.983  81.780  38.306  1.00 14.32           C  
-ATOM     39  N   ASN A   9     -13.228  79.552  35.849  1.00 29.47           N  
-ATOM     40  CA  ASN A   9     -14.133  78.459  35.493  1.00 33.22           C  
-ATOM     41  C   ASN A   9     -13.227  77.276  35.611  1.00 34.13           C  
-ATOM     42  O   ASN A   9     -12.125  77.308  35.074  1.00 35.41           O  
-ATOM     43  CB  ASN A   9     -14.555  78.386  34.013  1.00 38.11           C  
-ATOM     44  CG  ASN A   9     -15.552  79.424  33.597  1.00 42.62           C  
-ATOM     45  OD1 ASN A   9     -16.720  79.332  33.924  1.00 48.35           O  
-ATOM     46  ND2 ASN A   9     -15.081  80.421  32.850  1.00 41.34           N  
-ATOM     47  N   THR A  10     -13.656  76.260  36.320  1.00 33.20           N  
-ATOM     48  CA  THR A  10     -12.829  75.086  36.438  1.00 30.23           C  
-ATOM     49  C   THR A  10     -13.712  74.031  35.844  1.00 31.69           C  
-ATOM     50  O   THR A  10     -14.915  74.252  35.715  1.00 35.98           O  
-ATOM     51  CB  THR A  10     -12.478  74.820  37.913  1.00 27.41           C  
-ATOM     52  OG1 THR A  10     -13.619  74.419  38.674  1.00 24.65           O  
-ATOM     53  CG2 THR A  10     -11.894  76.058  38.615  1.00 27.48           C  
-ATOM     54  N   LYS A  11     -13.156  72.866  35.542  1.00 27.84           N  
-ATOM     55  CA  LYS A  11     -14.023  71.850  34.980  1.00 24.67           C  
-ATOM     56  C   LYS A  11     -15.154  71.440  35.929  1.00 24.68           C  
-ATOM     57  O   LYS A  11     -16.072  70.775  35.486  1.00 27.54           O  
-ATOM     58  CB  LYS A  11     -13.208  70.653  34.493  1.00 17.20           C  
-ATOM     59  CG  LYS A  11     -12.087  71.099  33.547  1.00 14.65           C  
-ATOM     60  CD  LYS A  11     -11.250  69.939  33.014  1.00 16.35           C  
-ATOM     61  CE  LYS A  11      -9.911  70.312  32.358  1.00 19.73           C  
-ATOM     62  NZ  LYS A  11      -9.107  69.103  32.179  1.00 22.74           N  
-ATOM     63  N   SER A  12     -15.078  71.792  37.231  1.00 27.83           N  
-ATOM     64  CA  SER A  12     -16.163  71.425  38.154  1.00 28.06           C  
-ATOM     65  C   SER A  12     -17.186  72.558  38.349  1.00 29.85           C  
-ATOM     66  O   SER A  12     -18.303  72.296  38.787  1.00 26.76           O  
-ATOM     67  CB  SER A  12     -15.645  71.067  39.569  1.00 28.31           C  
-ATOM     68  OG  SER A  12     -14.456  70.262  39.614  1.00 28.89           O  
-ATOM     69  N   GLY A  13     -16.789  73.809  38.067  1.00 27.92           N  
-ATOM     70  CA  GLY A  13     -17.743  74.889  38.268  1.00 30.42           C  
-ATOM     71  C   GLY A  13     -16.970  76.173  38.361  1.00 32.86           C  
-ATOM     72  O   GLY A  13     -15.750  76.147  38.199  1.00 31.43           O  
-ATOM     73  N   LYS A  14     -17.661  77.300  38.603  1.00 34.06           N  
-ATOM     74  CA  LYS A  14     -16.946  78.577  38.695  1.00 35.67           C  
-ATOM     75  C   LYS A  14     -16.546  78.847  40.127  1.00 34.96           C  
-ATOM     76  O   LYS A  14     -17.215  78.370  41.034  1.00 34.65           O  
-ATOM     77  CB  LYS A  14     -17.839  79.721  38.192  1.00 38.99           C  
-ATOM     78  CG  LYS A  14     -17.873  79.759  36.661  1.00 47.77           C  
-ATOM     79  CD  LYS A  14     -18.766  80.858  36.070  1.00 55.48           C  
-ATOM     80  CE  LYS A  14     -20.267  80.650  36.336  1.00 64.81           C  
-ATOM     81  NZ  LYS A  14     -20.749  79.427  35.705  1.00 71.00           N  
-ATOM     82  N   VAL A  15     -15.479  79.629  40.328  1.00 34.04           N  
-ATOM     83  CA  VAL A  15     -15.026  79.952  41.667  1.00 32.93           C  
-ATOM     84  C   VAL A  15     -14.591  81.417  41.683  1.00 34.62           C  
-ATOM     85  O   VAL A  15     -13.953  81.902  40.751  1.00 29.89           O  
-ATOM     86  CB  VAL A  15     -13.875  79.002  42.098  1.00 29.03           C  
-ATOM     87  CG1 VAL A  15     -14.269  77.516  42.075  1.00 29.98           C  
-ATOM     88  CG2 VAL A  15     -12.622  79.141  41.229  1.00 31.49           C  
-ATOM     89  N   MET A  16     -14.981  82.082  42.777  1.00 37.70           N  
-ATOM     90  CA  MET A  16     -14.696  83.486  43.083  1.00 39.31           C  
-ATOM     91  C   MET A  16     -13.672  83.472  44.208  1.00 37.45           C  
-ATOM     92  O   MET A  16     -13.922  82.839  45.227  1.00 37.64           O  
-ATOM     93  CB  MET A  16     -15.964  84.164  43.671  1.00 43.76           C  
-ATOM     94  CG  MET A  16     -16.786  84.967  42.656  1.00 51.80           C  
-ATOM     95  SD  MET A  16     -15.852  86.472  42.182  1.00 59.52           S  
-ATOM     96  CE  MET A  16     -16.117  87.473  43.685  1.00 62.28           C  
-ATOM     97  N   GLY A  17     -12.555  84.166  44.044  1.00 35.12           N  
-ATOM     98  CA  GLY A  17     -11.542  84.181  45.098  1.00 31.94           C  
-ATOM     99  C   GLY A  17     -11.538  85.515  45.789  1.00 29.25           C  
-ATOM    100  O   GLY A  17     -12.538  86.225  45.821  1.00 29.77           O  
-ATOM    101  N   THR A  18     -10.387  85.877  46.335  1.00 29.14           N  
-ATOM    102  CA  THR A  18     -10.240  87.143  47.021  1.00 32.39           C  
-ATOM    103  C   THR A  18      -8.877  87.671  46.695  1.00 29.82           C  
-ATOM    104  O   THR A  18      -7.952  86.944  46.354  1.00 29.28           O  
-ATOM    105  CB  THR A  18     -10.270  86.929  48.552  1.00 38.14           C  
-ATOM    106  OG1 THR A  18     -11.384  86.119  48.917  1.00 42.11           O  
-ATOM    107  CG2 THR A  18     -10.355  88.216  49.399  1.00 41.82           C  
-ATOM    108  N   ARG A  19      -8.772  88.981  46.807  1.00 28.01           N  
-ATOM    109  CA  ARG A  19      -7.503  89.605  46.570  1.00 29.07           C  
-ATOM    110  C   ARG A  19      -6.948  89.704  47.989  1.00 30.93           C  
-ATOM    111  O   ARG A  19      -7.634  90.258  48.842  1.00 35.56           O  
-ATOM    112  CB  ARG A  19      -7.758  90.976  45.920  1.00 28.93           C  
-ATOM    113  CG  ARG A  19      -6.503  91.613  45.339  1.00 32.23           C  
-ATOM    114  CD  ARG A  19      -6.762  93.028  44.816  1.00 35.26           C  
-ATOM    115  N   VAL A  20      -5.760  89.164  48.263  1.00 30.18           N  
-ATOM    116  CA  VAL A  20      -5.210  89.235  49.617  1.00 26.81           C  
-ATOM    117  C   VAL A  20      -3.984  90.126  49.576  1.00 28.42           C  
-ATOM    118  O   VAL A  20      -3.243  90.053  48.604  1.00 28.65           O  
-ATOM    119  CB  VAL A  20      -4.849  87.825  50.132  1.00 25.26           C  
-ATOM    120  CG1 VAL A  20      -6.086  86.908  50.086  1.00 20.35           C  
-ATOM    121  CG2 VAL A  20      -3.672  87.168  49.377  1.00 25.28           C  
-ATOM    122  N   PRO A  21      -3.764  90.961  50.603  1.00 29.36           N  
-ATOM    123  CA  PRO A  21      -2.543  91.749  50.665  1.00 28.64           C  
-ATOM    124  C   PRO A  21      -1.347  90.886  50.931  1.00 28.38           C  
-ATOM    125  O   PRO A  21      -1.405  89.986  51.758  1.00 29.32           O  
-ATOM    126  CB  PRO A  21      -2.741  92.681  51.869  1.00 30.26           C  
-ATOM    127  CG  PRO A  21      -4.219  92.582  52.263  1.00 31.39           C  
-ATOM    128  CD  PRO A  21      -4.740  91.285  51.635  1.00 31.49           C  
-ATOM    129  N   VAL A  22      -0.249  91.183  50.261  1.00 29.82           N  
-ATOM    130  CA  VAL A  22       0.960  90.419  50.471  1.00 31.13           C  
-ATOM    131  C   VAL A  22       2.012  91.460  50.498  1.00 34.00           C  
-ATOM    132  O   VAL A  22       2.306  92.090  49.498  1.00 36.68           O  
-ATOM    133  CB  VAL A  22       1.232  89.459  49.316  1.00 28.17           C  
-ATOM    134  CG1 VAL A  22       2.433  88.577  49.605  1.00 27.98           C  
-ATOM    135  CG2 VAL A  22       0.011  88.599  49.042  1.00 33.00           C  
-ATOM    136  N   LEU A  23       2.605  91.635  51.659  1.00 35.38           N  
-ATOM    137  CA  LEU A  23       3.623  92.660  51.758  1.00 37.84           C  
-ATOM    138  C   LEU A  23       3.003  93.998  51.372  1.00 43.58           C  
-ATOM    139  O   LEU A  23       2.056  94.464  51.991  1.00 47.15           O  
-ATOM    140  CB  LEU A  23       4.926  92.342  51.009  1.00 34.91           C  
-ATOM    141  CG  LEU A  23       5.762  91.224  51.648  1.00 37.14           C  
-ATOM    142  CD1 LEU A  23       5.306  89.823  51.252  1.00 37.74           C  
-ATOM    143  CD2 LEU A  23       7.228  91.372  51.229  1.00 43.47           C  
-ATOM    144  N   SER A  24       3.546  94.547  50.304  1.00 45.59           N  
-ATOM    145  CA  SER A  24       3.151  95.833  49.783  1.00 47.78           C  
-ATOM    146  C   SER A  24       2.170  95.764  48.633  1.00 46.42           C  
-ATOM    147  O   SER A  24       1.802  96.789  48.070  1.00 49.47           O  
-ATOM    148  CB  SER A  24       4.454  96.470  49.252  1.00 53.04           C  
-ATOM    149  OG  SER A  24       5.276  95.514  48.535  1.00 56.67           O  
-ATOM    150  N   SER A  25       1.764  94.551  48.285  1.00 43.60           N  
-ATOM    151  CA  SER A  25       0.900  94.351  47.149  1.00 41.55           C  
-ATOM    152  C   SER A  25      -0.283  93.474  47.480  1.00 39.27           C  
-ATOM    153  O   SER A  25      -0.777  93.456  48.602  1.00 42.44           O  
-ATOM    154  CB  SER A  25       1.780  93.725  46.060  1.00 43.12           C  
-ATOM    155  OG  SER A  25       3.058  94.368  46.008  1.00 49.23           O  
-ATOM    156  N   HIS A  26      -0.731  92.728  46.465  1.00 35.32           N  
-ATOM    157  CA  HIS A  26      -1.858  91.841  46.579  1.00 32.06           C  
-ATOM    158  C   HIS A  26      -1.588  90.547  45.794  1.00 29.59           C  
-ATOM    159  O   HIS A  26      -0.578  90.415  45.113  1.00 31.42           O  
-ATOM    160  CB  HIS A  26      -3.032  92.623  45.990  1.00 31.02           C  
-ATOM    161  N   ILE A  27      -2.509  89.600  45.908  1.00 21.50           N  
-ATOM    162  CA  ILE A  27      -2.427  88.321  45.230  1.00 20.27           C  
-ATOM    163  C   ILE A  27      -3.851  87.860  45.203  1.00 21.51           C  
-ATOM    164  O   ILE A  27      -4.717  88.495  45.793  1.00 19.80           O  
-ATOM    165  CB  ILE A  27      -1.505  87.378  46.027  1.00 19.81           C  
-ATOM    166  CG1 ILE A  27      -0.111  87.355  45.413  1.00 25.98           C  
-ATOM    167  CG2 ILE A  27      -2.007  85.970  46.354  1.00 21.89           C  
-ATOM    168  CD1 ILE A  27       0.663  86.040  45.648  1.00 33.64           C  
-ATOM    169  N   SER A  28      -4.094  86.767  44.510  1.00 21.19           N  
-ATOM    170  CA  SER A  28      -5.439  86.251  44.469  1.00 25.17           C  
-ATOM    171  C   SER A  28      -5.369  85.028  45.334  1.00 25.66           C  
-ATOM    172  O   SER A  28      -4.345  84.353  45.388  1.00 30.04           O  
-ATOM    173  CB  SER A  28      -5.835  85.861  43.030  1.00 29.04           C  
-ATOM    174  OG  SER A  28      -5.758  86.989  42.156  1.00 36.88           O  
-ATOM    175  N   ALA A  29      -6.460  84.718  46.010  1.00 23.77           N  
-ATOM    176  CA  ALA A  29      -6.460  83.548  46.848  1.00 21.82           C  
-ATOM    177  C   ALA A  29      -7.798  82.928  46.654  1.00 22.70           C  
-ATOM    178  O   ALA A  29      -8.797  83.637  46.615  1.00 21.72           O  
-ATOM    179  CB  ALA A  29      -6.325  83.972  48.315  1.00 24.17           C  
-ATOM    180  N   PHE A  30      -7.788  81.613  46.502  1.00 22.31           N  
-ATOM    181  CA  PHE A  30      -9.018  80.867  46.330  1.00 23.55           C  
-ATOM    182  C   PHE A  30      -8.917  79.880  47.469  1.00 24.51           C  
-ATOM    183  O   PHE A  30      -8.094  78.969  47.399  1.00 27.63           O  
-ATOM    184  CB  PHE A  30      -9.061  80.119  44.960  1.00 25.71           C  
-ATOM    185  CG  PHE A  30      -9.027  81.019  43.728  1.00 21.98           C  
-ATOM    186  CD1 PHE A  30      -7.797  81.505  43.221  1.00 18.64           C  
-ATOM    187  CD2 PHE A  30     -10.233  81.399  43.094  1.00 19.09           C  
-ATOM    188  CE1 PHE A  30      -7.779  82.375  42.119  1.00 16.13           C  
-ATOM    189  CE2 PHE A  30     -10.221  82.265  41.995  1.00 12.59           C  
-ATOM    190  CZ  PHE A  30      -8.995  82.757  41.517  1.00 19.18           C  
-ATOM    191  N   LEU A  31      -9.699  80.075  48.528  1.00 22.04           N  
-ATOM    192  CA  LEU A  31      -9.615  79.160  49.663  1.00 18.95           C  
-ATOM    193  C   LEU A  31     -10.854  78.281  49.734  1.00 20.31           C  
-ATOM    194  O   LEU A  31     -11.951  78.708  49.409  1.00 22.57           O  
-ATOM    195  CB  LEU A  31      -9.615  79.944  50.992  1.00 15.90           C  
-ATOM    196  CG  LEU A  31      -8.438  80.872  51.338  1.00 10.17           C  
-ATOM    197  CD1 LEU A  31      -7.296  80.912  50.334  1.00  9.79           C  
-ATOM    198  CD2 LEU A  31      -8.958  82.277  51.614  1.00  7.92           C  
-ATOM    199  N   GLY A  32     -10.675  77.043  50.189  1.00 19.63           N  
-ATOM    200  CA  GLY A  32     -11.825  76.159  50.338  1.00 17.79           C  
-ATOM    201  C   GLY A  32     -12.485  75.571  49.094  1.00 17.48           C  
-ATOM    202  O   GLY A  32     -13.682  75.307  49.118  1.00 19.31           O  
-ATOM    203  N   ILE A  33     -11.741  75.327  47.998  1.00 16.16           N  
-ATOM    204  CA  ILE A  33     -12.403  74.743  46.822  1.00 12.47           C  
-ATOM    205  C   ILE A  33     -12.593  73.236  47.093  1.00 11.92           C  
-ATOM    206  O   ILE A  33     -11.624  72.549  47.397  1.00 15.94           O  
-ATOM    207  CB  ILE A  33     -11.539  74.952  45.567  1.00  9.82           C  
-ATOM    208  CG1 ILE A  33     -11.207  76.435  45.302  1.00  9.70           C  
-ATOM    209  CG2 ILE A  33     -12.199  74.334  44.332  1.00 11.40           C  
-ATOM    210  CD1 ILE A  33     -10.035  76.570  44.319  1.00 10.55           C  
-ATOM    211  N   PRO A  34     -13.822  72.711  47.015  1.00  9.19           N  
-ATOM    212  CA  PRO A  34     -14.031  71.303  47.350  1.00 12.31           C  
-ATOM    213  C   PRO A  34     -13.398  70.436  46.293  1.00 13.30           C  
-ATOM    214  O   PRO A  34     -13.393  70.816  45.138  1.00 18.57           O  
-ATOM    215  CB  PRO A  34     -15.562  71.124  47.334  1.00  8.07           C  
-ATOM    216  CG  PRO A  34     -16.099  72.321  46.537  1.00  5.81           C  
-ATOM    217  CD  PRO A  34     -15.028  73.419  46.629  1.00  7.70           C  
-ATOM    218  N   PHE A  35     -12.895  69.263  46.671  1.00 14.36           N  
-ATOM    219  CA  PHE A  35     -12.300  68.406  45.655  1.00  9.91           C  
-ATOM    220  C   PHE A  35     -12.831  66.998  45.693  1.00 12.79           C  
-ATOM    221  O   PHE A  35     -12.381  66.173  44.914  1.00 15.80           O  
-ATOM    222  CB  PHE A  35     -10.776  68.408  45.715  1.00 11.07           C  
-ATOM    223  CG  PHE A  35     -10.152  67.808  46.961  1.00 17.39           C  
-ATOM    224  CD1 PHE A  35     -10.133  66.414  47.151  1.00 16.80           C  
-ATOM    225  CD2 PHE A  35      -9.518  68.631  47.914  1.00 19.76           C  
-ATOM    226  CE1 PHE A  35      -9.469  65.840  48.245  1.00 18.35           C  
-ATOM    227  CE2 PHE A  35      -8.852  68.058  49.009  1.00 19.78           C  
-ATOM    228  CZ  PHE A  35      -8.822  66.664  49.171  1.00 20.22           C  
-ATOM    229  N   ALA A  36     -13.774  66.688  46.592  1.00 10.85           N  
-ATOM    230  CA  ALA A  36     -14.325  65.340  46.667  1.00  8.56           C  
-ATOM    231  C   ALA A  36     -15.632  65.480  47.393  1.00 12.49           C  
-ATOM    232  O   ALA A  36     -15.897  66.525  47.967  1.00 18.58           O  
-ATOM    233  CB  ALA A  36     -13.386  64.415  47.425  1.00  6.98           C  
-ATOM    234  N   GLU A  37     -16.480  64.461  47.356  1.00 17.66           N  
-ATOM    235  CA  GLU A  37     -17.760  64.582  48.069  1.00 21.71           C  
-ATOM    236  C   GLU A  37     -17.514  64.410  49.571  1.00 22.94           C  
-ATOM    237  O   GLU A  37     -16.832  63.452  49.918  1.00 26.27           O  
-ATOM    238  CB  GLU A  37     -18.750  63.467  47.648  1.00 23.74           C  
-ATOM    239  CG  GLU A  37     -19.328  63.616  46.228  1.00 27.33           C  
-ATOM    240  CD  GLU A  37     -20.406  64.704  46.157  1.00 31.25           C  
-ATOM    241  OE1 GLU A  37     -21.535  64.424  46.561  1.00 34.04           O  
-ATOM    242  OE2 GLU A  37     -20.126  65.817  45.704  1.00 30.36           O  
-ATOM    243  N   PRO A  38     -18.101  65.289  50.436  1.00 23.11           N  
-ATOM    244  CA  PRO A  38     -17.897  65.221  51.887  1.00 17.99           C  
-ATOM    245  C   PRO A  38     -18.053  63.833  52.455  1.00 17.78           C  
-ATOM    246  O   PRO A  38     -19.148  63.295  52.367  1.00 23.08           O  
-ATOM    247  CB  PRO A  38     -18.999  66.109  52.467  1.00 15.25           C  
-ATOM    248  CG  PRO A  38     -19.381  67.077  51.348  1.00 21.82           C  
-ATOM    249  CD  PRO A  38     -19.040  66.343  50.042  1.00 25.22           C  
-ATOM    250  N   PRO A  39     -16.988  63.271  53.040  1.00 14.62           N  
-ATOM    251  CA  PRO A  39     -17.013  61.878  53.449  1.00 14.68           C  
-ATOM    252  C   PRO A  39     -17.702  61.743  54.784  1.00 18.19           C  
-ATOM    253  O   PRO A  39     -17.113  61.328  55.779  1.00 26.50           O  
-ATOM    254  CB  PRO A  39     -15.525  61.549  53.563  1.00 12.52           C  
-ATOM    255  CG  PRO A  39     -14.860  62.880  53.931  1.00 13.31           C  
-ATOM    256  CD  PRO A  39     -15.722  63.950  53.278  1.00 10.24           C  
-ATOM    257  N   VAL A  40     -18.959  62.123  54.810  1.00 17.25           N  
-ATOM    258  CA  VAL A  40     -19.699  62.057  56.038  1.00 17.22           C  
-ATOM    259  C   VAL A  40     -20.662  60.892  55.947  1.00 20.33           C  
-ATOM    260  O   VAL A  40     -20.742  60.152  54.976  1.00 25.80           O  
-ATOM    261  CB  VAL A  40     -20.370  63.440  56.216  1.00 15.36           C  
-ATOM    262  CG1 VAL A  40     -19.347  64.601  56.138  1.00  6.48           C  
-ATOM    263  CG2 VAL A  40     -21.509  63.677  55.208  1.00 18.85           C  
-ATOM    264  N   GLY A  41     -21.420  60.721  57.009  1.00 24.29           N  
-ATOM    265  CA  GLY A  41     -22.414  59.661  57.013  1.00 25.93           C  
-ATOM    266  C   GLY A  41     -21.868  58.298  56.733  1.00 26.15           C  
-ATOM    267  O   GLY A  41     -20.822  57.901  57.228  1.00 30.02           O  
-ATOM    268  N   ASN A  42     -22.623  57.602  55.878  1.00 28.14           N  
-ATOM    269  CA  ASN A  42     -22.273  56.252  55.477  1.00 31.52           C  
-ATOM    270  C   ASN A  42     -20.982  56.182  54.642  1.00 32.76           C  
-ATOM    271  O   ASN A  42     -20.514  55.113  54.276  1.00 31.62           O  
-ATOM    272  CB  ASN A  42     -23.492  55.583  54.843  1.00 29.49           C  
-ATOM    273  N   MET A  43     -20.390  57.351  54.357  1.00 33.93           N  
-ATOM    274  CA  MET A  43     -19.153  57.405  53.590  1.00 34.65           C  
-ATOM    275  C   MET A  43     -17.935  57.446  54.473  1.00 33.26           C  
-ATOM    276  O   MET A  43     -16.805  57.433  53.997  1.00 34.27           O  
-ATOM    277  CB  MET A  43     -19.165  58.630  52.682  1.00 37.67           C  
-ATOM    278  CG  MET A  43     -20.371  58.550  51.737  1.00 40.13           C  
-ATOM    279  SD  MET A  43     -19.833  59.076  50.095  1.00 47.63           S  
-ATOM    280  CE  MET A  43     -19.690  60.877  50.378  1.00 44.23           C  
-ATOM    281  N   ARG A  44     -18.166  57.528  55.783  1.00 30.06           N  
-ATOM    282  CA  ARG A  44     -17.026  57.556  56.677  1.00 26.22           C  
-ATOM    283  C   ARG A  44     -16.200  56.290  56.450  1.00 23.34           C  
-ATOM    284  O   ARG A  44     -16.777  55.227  56.309  1.00 17.04           O  
-ATOM    285  CB  ARG A  44     -17.503  57.608  58.154  1.00 26.73           C  
-ATOM    286  CG  ARG A  44     -16.350  57.879  59.143  1.00 24.95           C  
-ATOM    287  CD  ARG A  44     -16.741  57.776  60.605  1.00 19.41           C  
-ATOM    288  NE  ARG A  44     -17.507  58.934  61.005  1.00 20.92           N  
-ATOM    289  CZ  ARG A  44     -18.057  58.982  62.228  1.00 25.75           C  
-ATOM    290  NH1 ARG A  44     -17.995  57.949  63.063  1.00 20.03           N  
-ATOM    291  NH2 ARG A  44     -18.688  60.079  62.620  1.00 28.74           N  
-ATOM    292  N   PHE A  45     -14.874  56.430  56.432  1.00 22.58           N  
-ATOM    293  CA  PHE A  45     -13.973  55.303  56.241  1.00 24.60           C  
-ATOM    294  C   PHE A  45     -13.869  54.856  54.801  1.00 26.95           C  
-ATOM    295  O   PHE A  45     -12.971  54.090  54.462  1.00 32.12           O  
-ATOM    296  CB  PHE A  45     -14.279  54.062  57.117  1.00 24.86           C  
-ATOM    297  CG  PHE A  45     -14.422  54.432  58.584  1.00 31.63           C  
-ATOM    298  CD1 PHE A  45     -13.381  55.119  59.260  1.00 29.49           C  
-ATOM    299  CD2 PHE A  45     -15.605  54.120  59.289  1.00 29.74           C  
-ATOM    300  CE1 PHE A  45     -13.531  55.500  60.597  1.00 26.98           C  
-ATOM    301  CE2 PHE A  45     -15.744  54.500  60.630  1.00 28.30           C  
-ATOM    302  CZ  PHE A  45     -14.716  55.196  61.278  1.00 26.58           C  
-ATOM    303  N   ARG A  46     -14.770  55.330  53.947  1.00 26.89           N  
-ATOM    304  CA  ARG A  46     -14.704  54.881  52.560  1.00 25.38           C  
-ATOM    305  C   ARG A  46     -13.835  55.815  51.756  1.00 22.97           C  
-ATOM    306  O   ARG A  46     -13.538  56.937  52.136  1.00 19.69           O  
-ATOM    307  CB  ARG A  46     -16.095  54.907  51.956  1.00 30.17           C  
-ATOM    308  CG  ARG A  46     -16.952  53.785  52.545  1.00 36.60           C  
-ATOM    309  CD  ARG A  46     -18.289  53.639  51.817  1.00 45.15           C  
-ATOM    310  NE  ARG A  46     -18.359  52.390  51.078  1.00 50.41           N  
-ATOM    311  N   ARG A  47     -13.446  55.274  50.622  1.00 17.96           N  
-ATOM    312  CA  ARG A  47     -12.572  56.029  49.722  1.00 13.93           C  
-ATOM    313  C   ARG A  47     -13.318  57.269  49.231  1.00 10.14           C  
-ATOM    314  O   ARG A  47     -14.526  57.161  49.107  1.00 14.08           O  
-ATOM    315  CB  ARG A  47     -12.068  55.222  48.516  1.00 16.88           C  
-ATOM    316  CG  ARG A  47     -12.371  53.729  48.484  1.00 22.12           C  
-ATOM    317  CD  ARG A  47     -11.133  52.923  47.979  1.00 23.05           C  
-ATOM    318  NE  ARG A  47     -11.447  51.504  47.852  0.06 15.19           N  
-ATOM    319  CZ  ARG A  47     -10.463  50.635  47.534  0.06 12.62           C  
-ATOM    320  NH1 ARG A  47      -9.186  50.983  47.289  0.06 11.23           N  
-ATOM    321  NH2 ARG A  47     -10.897  49.352  47.483  0.06 10.41           N  
-ATOM    322  N   PRO A  48     -12.618  58.367  48.935  1.00  6.34           N  
-ATOM    323  CA  PRO A  48     -13.323  59.597  48.534  1.00 11.93           C  
-ATOM    324  C   PRO A  48     -13.937  59.577  47.126  1.00 16.79           C  
-ATOM    325  O   PRO A  48     -13.374  59.012  46.195  1.00 17.10           O  
-ATOM    326  CB  PRO A  48     -12.224  60.664  48.594  1.00  8.51           C  
-ATOM    327  CG  PRO A  48     -10.920  59.881  48.407  1.00  8.25           C  
-ATOM    328  CD  PRO A  48     -11.171  58.513  49.037  1.00  5.71           C  
-ATOM    329  N   GLU A  49     -15.109  60.234  46.973  1.00 20.27           N  
-ATOM    330  CA  GLU A  49     -15.726  60.303  45.642  1.00 20.95           C  
-ATOM    331  C   GLU A  49     -15.296  61.616  45.036  1.00 20.57           C  
-ATOM    332  O   GLU A  49     -15.185  62.573  45.792  1.00 21.43           O  
-ATOM    333  CB  GLU A  49     -17.264  60.383  45.663  1.00 27.74           C  
-ATOM    334  CG  GLU A  49     -17.958  59.115  46.176  1.00 37.97           C  
-ATOM    335  CD  GLU A  49     -19.473  59.230  46.012  1.00 42.75           C  
-ATOM    336  OE1 GLU A  49     -20.030  60.296  46.295  1.00 47.09           O  
-ATOM    337  OE2 GLU A  49     -20.092  58.250  45.598  1.00 49.76           O  
-ATOM    338  N   PRO A  50     -15.143  61.696  43.692  1.00 19.49           N  
-ATOM    339  CA  PRO A  50     -14.871  62.976  43.054  1.00 17.83           C  
-ATOM    340  C   PRO A  50     -16.095  63.827  43.265  1.00 22.18           C  
-ATOM    341  O   PRO A  50     -17.208  63.309  43.296  1.00 26.65           O  
-ATOM    342  CB  PRO A  50     -14.564  62.647  41.609  1.00 18.41           C  
-ATOM    343  CG  PRO A  50     -14.684  61.118  41.449  1.00 22.20           C  
-ATOM    344  CD  PRO A  50     -15.207  60.570  42.775  1.00 20.22           C  
-ATOM    345  N   LYS A  51     -15.878  65.129  43.433  1.00 24.77           N  
-ATOM    346  CA  LYS A  51     -17.011  65.994  43.725  1.00 29.54           C  
-ATOM    347  C   LYS A  51     -17.920  66.304  42.558  1.00 33.14           C  
-ATOM    348  O   LYS A  51     -17.460  66.654  41.482  1.00 36.22           O  
-ATOM    349  CB  LYS A  51     -16.494  67.315  44.305  1.00 30.84           C  
-ATOM    350  CG  LYS A  51     -17.438  67.930  45.350  1.00 29.10           C  
-ATOM    351  CD  LYS A  51     -17.954  69.297  44.917  1.00 32.33           C  
-ATOM    352  CE  LYS A  51     -18.780  70.023  45.989  1.00 37.69           C  
-ATOM    353  NZ  LYS A  51     -19.987  69.282  46.342  1.00 44.09           N  
-ATOM    354  N   LYS A  52     -19.237  66.214  42.814  1.00 33.86           N  
-ATOM    355  CA  LYS A  52     -20.193  66.535  41.757  1.00 34.64           C  
-ATOM    356  C   LYS A  52     -20.045  68.015  41.406  1.00 34.51           C  
-ATOM    357  O   LYS A  52     -19.902  68.825  42.311  1.00 32.61           O  
-ATOM    358  CB  LYS A  52     -21.631  66.295  42.230  1.00 38.77           C  
-ATOM    359  CG  LYS A  52     -21.923  64.811  42.475  1.00 43.55           C  
-ATOM    360  CD  LYS A  52     -23.163  64.610  43.356  1.00 47.58           C  
-ATOM    361  CE  LYS A  52     -23.393  63.127  43.700  1.00 52.94           C  
-ATOM    362  NZ  LYS A  52     -24.124  62.998  44.953  1.00 56.70           N  
-ATOM    363  N   PRO A  53     -20.056  68.371  40.105  1.00 35.14           N  
-ATOM    364  CA  PRO A  53     -19.880  69.766  39.752  1.00 35.65           C  
-ATOM    365  C   PRO A  53     -20.983  70.593  40.350  1.00 36.92           C  
-ATOM    366  O   PRO A  53     -22.042  70.101  40.731  1.00 37.97           O  
-ATOM    367  CB  PRO A  53     -19.919  69.766  38.220  1.00 34.28           C  
-ATOM    368  CG  PRO A  53     -19.604  68.327  37.802  1.00 32.67           C  
-ATOM    369  CD  PRO A  53     -20.125  67.473  38.956  1.00 33.93           C  
-ATOM    370  N   TRP A  54     -20.715  71.881  40.395  1.00 37.83           N  
-ATOM    371  CA  TRP A  54     -21.704  72.773  40.948  1.00 37.84           C  
-ATOM    372  C   TRP A  54     -22.015  73.853  39.924  1.00 41.97           C  
-ATOM    373  O   TRP A  54     -21.310  74.126  38.951  1.00 41.63           O  
-ATOM    374  CB  TRP A  54     -21.223  73.316  42.315  1.00 30.12           C  
-ATOM    375  CG  TRP A  54     -19.918  74.055  42.160  1.00 17.64           C  
-ATOM    376  CD1 TRP A  54     -19.780  75.404  41.755  1.00 17.68           C  
-ATOM    377  CD2 TRP A  54     -18.631  73.527  42.308  1.00 15.11           C  
-ATOM    378  NE1 TRP A  54     -18.473  75.731  41.635  1.00 18.46           N  
-ATOM    379  CE2 TRP A  54     -17.707  74.634  41.955  1.00 16.29           C  
-ATOM    380  CE3 TRP A  54     -18.123  72.274  42.655  1.00  9.58           C  
-ATOM    381  CZ2 TRP A  54     -16.324  74.409  41.983  1.00 12.62           C  
-ATOM    382  CZ3 TRP A  54     -16.732  72.090  42.666  1.00  8.82           C  
-ATOM    383  CH2 TRP A  54     -15.847  73.138  42.342  1.00 11.55           C  
-ATOM    384  N   SER A  55     -23.157  74.468  40.195  1.00 46.06           N  
-ATOM    385  CA  SER A  55     -23.649  75.549  39.372  1.00 48.87           C  
-ATOM    386  C   SER A  55     -23.364  76.787  40.199  1.00 47.85           C  
-ATOM    387  O   SER A  55     -23.043  76.715  41.382  1.00 46.18           O  
-ATOM    388  CB  SER A  55     -25.153  75.354  39.109  1.00 51.18           C  
-ATOM    389  OG  SER A  55     -25.787  74.843  40.292  1.00 58.54           O  
-ATOM    390  N   GLY A  56     -23.508  77.943  39.575  1.00 46.29           N  
-ATOM    391  CA  GLY A  56     -23.243  79.120  40.376  1.00 46.52           C  
-ATOM    392  C   GLY A  56     -21.763  79.303  40.447  1.00 43.81           C  
-ATOM    393  O   GLY A  56     -21.016  78.780  39.623  1.00 46.74           O  
-ATOM    394  N   VAL A  57     -21.377  80.089  41.434  1.00 39.39           N  
-ATOM    395  CA  VAL A  57     -19.994  80.367  41.663  1.00 35.44           C  
-ATOM    396  C   VAL A  57     -19.775  79.847  43.070  1.00 38.08           C  
-ATOM    397  O   VAL A  57     -20.596  80.025  43.964  1.00 37.40           O  
-ATOM    398  CB  VAL A  57     -19.733  81.891  41.571  1.00 29.31           C  
-ATOM    399  CG1 VAL A  57     -18.822  82.249  40.414  1.00 29.88           C  
-ATOM    400  CG2 VAL A  57     -21.016  82.725  41.454  1.00 35.24           C  
-ATOM    401  N   TRP A  58     -18.641  79.180  43.258  1.00 38.80           N  
-ATOM    402  CA  TRP A  58     -18.314  78.692  44.572  1.00 34.49           C  
-ATOM    403  C   TRP A  58     -17.604  79.887  45.168  1.00 35.37           C  
-ATOM    404  O   TRP A  58     -16.763  80.508  44.513  1.00 36.57           O  
-ATOM    405  CB  TRP A  58     -17.320  77.542  44.483  1.00 32.34           C  
-ATOM    406  CG  TRP A  58     -17.216  76.872  45.822  1.00 33.36           C  
-ATOM    407  CD1 TRP A  58     -16.307  77.208  46.851  1.00 30.36           C  
-ATOM    408  CD2 TRP A  58     -18.023  75.828  46.280  1.00 30.42           C  
-ATOM    409  NE1 TRP A  58     -16.530  76.417  47.920  1.00 30.04           N  
-ATOM    410  CE2 TRP A  58     -17.560  75.553  47.647  1.00 28.90           C  
-ATOM    411  CE3 TRP A  58     -19.060  75.079  45.722  1.00 32.78           C  
-ATOM    412  CZ2 TRP A  58     -18.195  74.553  48.389  1.00 30.89           C  
-ATOM    413  CZ3 TRP A  58     -19.668  74.071  46.487  1.00 34.22           C  
-ATOM    414  CH2 TRP A  58     -19.244  73.819  47.804  1.00 35.78           C  
-ATOM    415  N   ASN A  59     -17.961  80.227  46.395  1.00 34.61           N  
-ATOM    416  CA  ASN A  59     -17.306  81.370  47.007  1.00 32.65           C  
-ATOM    417  C   ASN A  59     -16.065  80.811  47.645  1.00 30.32           C  
-ATOM    418  O   ASN A  59     -16.183  79.977  48.525  1.00 33.22           O  
-ATOM    419  CB  ASN A  59     -18.226  81.979  48.075  1.00 37.84           C  
-ATOM    420  CG  ASN A  59     -17.671  83.293  48.596  1.00 42.52           C  
-ATOM    421  OD1 ASN A  59     -17.007  83.365  49.615  1.00 47.22           O  
-ATOM    422  ND2 ASN A  59     -17.927  84.356  47.842  1.00 44.27           N  
-ATOM    423  N   ALA A  60     -14.896  81.244  47.205  1.00 24.99           N  
-ATOM    424  CA  ALA A  60     -13.669  80.730  47.765  1.00 23.98           C  
-ATOM    425  C   ALA A  60     -12.939  81.819  48.482  1.00 27.18           C  
-ATOM    426  O   ALA A  60     -11.769  82.062  48.199  1.00 27.44           O  
-ATOM    427  CB  ALA A  60     -12.767  80.191  46.652  1.00 26.41           C  
-ATOM    428  N   SER A  61     -13.642  82.467  49.421  1.00 31.48           N  
-ATOM    429  CA  SER A  61     -13.040  83.578  50.173  1.00 32.86           C  
-ATOM    430  C   SER A  61     -12.625  83.304  51.622  1.00 34.53           C  
-ATOM    431  O   SER A  61     -12.053  84.157  52.298  1.00 36.50           O  
-ATOM    432  CB  SER A  61     -14.065  84.730  50.228  1.00 31.96           C  
-ATOM    433  OG  SER A  61     -14.657  84.951  48.941  1.00 38.85           O  
-ATOM    434  N   THR A  62     -12.931  82.118  52.137  1.00 33.87           N  
-ATOM    435  CA  THR A  62     -12.587  81.857  53.529  1.00 30.62           C  
-ATOM    436  C   THR A  62     -11.978  80.477  53.615  1.00 28.79           C  
-ATOM    437  O   THR A  62     -12.095  79.707  52.675  1.00 32.61           O  
-ATOM    438  CB  THR A  62     -13.883  82.017  54.348  1.00 31.32           C  
-ATOM    439  OG1 THR A  62     -14.976  81.404  53.663  1.00 29.68           O  
-ATOM    440  CG2 THR A  62     -14.286  83.490  54.576  1.00 31.03           C  
-ATOM    441  N   TYR A  63     -11.300  80.174  54.729  1.00 25.93           N  
-ATOM    442  CA  TYR A  63     -10.717  78.836  54.813  1.00 19.78           C  
-ATOM    443  C   TYR A  63     -11.796  77.818  55.072  1.00 18.69           C  
-ATOM    444  O   TYR A  63     -12.836  78.140  55.619  1.00 18.46           O  
-ATOM    445  CB  TYR A  63      -9.722  78.710  55.951  1.00 15.15           C  
-ATOM    446  CG  TYR A  63      -8.453  79.424  55.622  1.00 15.43           C  
-ATOM    447  CD1 TYR A  63      -7.489  78.794  54.827  1.00 15.81           C  
-ATOM    448  CD2 TYR A  63      -8.225  80.720  56.109  1.00 17.62           C  
-ATOM    449  CE1 TYR A  63      -6.285  79.443  54.537  1.00 19.43           C  
-ATOM    450  CE2 TYR A  63      -7.024  81.375  55.809  1.00 20.65           C  
-ATOM    451  CZ  TYR A  63      -6.048  80.737  55.025  1.00 19.70           C  
-ATOM    452  OH  TYR A  63      -4.857  81.380  54.735  1.00 24.19           O  
-ATOM    453  N   PRO A  64     -11.522  76.573  54.693  1.00 19.06           N  
-ATOM    454  CA  PRO A  64     -12.468  75.517  55.001  1.00 20.68           C  
-ATOM    455  C   PRO A  64     -12.327  75.036  56.444  1.00 18.38           C  
-ATOM    456  O   PRO A  64     -11.485  75.450  57.224  1.00 17.54           O  
-ATOM    457  CB  PRO A  64     -12.081  74.422  53.982  1.00 22.54           C  
-ATOM    458  CG  PRO A  64     -10.591  74.661  53.665  1.00 21.58           C  
-ATOM    459  CD  PRO A  64     -10.386  76.162  53.866  1.00 19.54           C  
-ATOM    460  N   ASN A  65     -13.221  74.112  56.766  1.00 20.56           N  
-ATOM    461  CA  ASN A  65     -13.196  73.527  58.091  1.00 23.26           C  
-ATOM    462  C   ASN A  65     -11.989  72.626  58.109  1.00 22.74           C  
-ATOM    463  O   ASN A  65     -11.470  72.232  57.067  1.00 23.75           O  
-ATOM    464  CB  ASN A  65     -14.439  72.651  58.366  1.00 27.73           C  
-ATOM    465  CG  ASN A  65     -15.731  73.455  58.323  1.00 36.61           C  
-ATOM    466  OD1 ASN A  65     -15.859  74.583  58.789  1.00 37.06           O  
-ATOM    467  ND2 ASN A  65     -16.725  72.834  57.702  1.00 40.45           N  
-ATOM    468  N   ASN A  66     -11.573  72.259  59.314  1.00 21.64           N  
-ATOM    469  CA  ASN A  66     -10.423  71.387  59.440  1.00 16.44           C  
-ATOM    470  C   ASN A  66     -10.979  70.013  59.711  1.00 16.55           C  
-ATOM    471  O   ASN A  66     -12.110  69.833  60.146  1.00 14.30           O  
-ATOM    472  CB  ASN A  66      -9.482  71.882  60.547  1.00 16.96           C  
-ATOM    473  CG  ASN A  66      -8.813  73.191  60.115  1.00 18.49           C  
-ATOM    474  OD1 ASN A  66      -8.817  73.579  58.965  1.00 26.03           O  
-ATOM    475  ND2 ASN A  66      -8.183  73.894  61.037  1.00 16.89           N  
-ATOM    476  N   CYS A  67     -10.185  68.993  59.417  1.00 17.25           N  
-ATOM    477  CA  CYS A  67     -10.706  67.656  59.682  1.00 18.57           C  
-ATOM    478  C   CYS A  67     -10.667  67.450  61.184  1.00 19.81           C  
-ATOM    479  O   CYS A  67      -9.984  68.203  61.875  1.00 20.61           O  
-ATOM    480  CB  CYS A  67      -9.863  66.601  58.960  1.00 17.42           C  
-ATOM    481  SG  CYS A  67      -9.905  66.802  57.151  1.00 18.98           S  
-ATOM    482  N   GLN A  68     -11.393  66.439  61.675  1.00 17.55           N  
-ATOM    483  CA  GLN A  68     -11.407  66.168  63.091  1.00 17.18           C  
-ATOM    484  C   GLN A  68     -10.043  65.664  63.483  1.00 19.88           C  
-ATOM    485  O   GLN A  68      -9.417  64.953  62.712  1.00 21.99           O  
-ATOM    486  CB  GLN A  68     -12.416  65.039  63.353  1.00 15.22           C  
-ATOM    487  CG  GLN A  68     -13.847  65.325  62.915  1.00 18.79           C  
-ATOM    488  CD  GLN A  68     -14.639  66.144  63.915  1.00 21.79           C  
-ATOM    489  OE1 GLN A  68     -15.813  65.936  64.118  1.00 25.17           O  
-ATOM    490  NE2 GLN A  68     -14.006  67.092  64.571  1.00 21.53           N  
-ATOM    491  N   GLN A  69      -9.585  66.025  64.673  1.00 20.12           N  
-ATOM    492  CA  GLN A  69      -8.279  65.555  65.080  1.00 18.14           C  
-ATOM    493  C   GLN A  69      -8.147  65.827  66.551  1.00 17.20           C  
-ATOM    494  O   GLN A  69      -9.001  66.466  67.156  1.00 19.15           O  
-ATOM    495  CB  GLN A  69      -7.197  66.296  64.294  1.00 13.21           C  
-ATOM    496  CG  GLN A  69      -7.408  67.813  64.392  1.00 13.01           C  
-ATOM    497  CD  GLN A  69      -6.498  68.483  63.423  1.00 16.68           C  
-ATOM    498  OE1 GLN A  69      -5.318  68.723  63.680  1.00 11.84           O  
-ATOM    499  NE2 GLN A  69      -7.090  68.699  62.256  1.00 13.06           N  
-ATOM    500  N   TYR A  70      -7.044  65.343  67.113  1.00 14.49           N  
-ATOM    501  CA  TYR A  70      -6.790  65.538  68.513  1.00 12.98           C  
-ATOM    502  C   TYR A  70      -6.205  66.938  68.694  1.00 15.14           C  
-ATOM    503  O   TYR A  70      -5.191  67.281  68.101  1.00 14.54           O  
-ATOM    504  CB  TYR A  70      -5.840  64.438  68.969  1.00 12.17           C  
-ATOM    505  CG  TYR A  70      -5.233  64.737  70.316  1.00 23.88           C  
-ATOM    506  CD1 TYR A  70      -5.991  64.599  71.488  1.00 25.60           C  
-ATOM    507  CD2 TYR A  70      -3.895  65.176  70.399  1.00 30.10           C  
-ATOM    508  CE1 TYR A  70      -5.410  64.871  72.737  1.00 33.68           C  
-ATOM    509  CE2 TYR A  70      -3.309  65.448  71.647  1.00 34.94           C  
-ATOM    510  CZ  TYR A  70      -4.068  65.298  72.822  1.00 37.28           C  
-ATOM    511  OH  TYR A  70      -3.512  65.590  74.064  1.00 42.92           O  
-ATOM    512  N   VAL A  71      -6.861  67.738  69.544  1.00 15.09           N  
-ATOM    513  CA  VAL A  71      -6.376  69.079  69.781  1.00 17.72           C  
-ATOM    514  C   VAL A  71      -5.276  68.956  70.821  1.00 20.76           C  
-ATOM    515  O   VAL A  71      -5.424  68.232  71.802  1.00 23.36           O  
-ATOM    516  CB  VAL A  71      -7.523  69.971  70.266  1.00 13.32           C  
-ATOM    517  CG1 VAL A  71      -7.165  71.450  70.135  1.00 14.34           C  
-ATOM    518  CG2 VAL A  71      -8.824  69.702  69.504  1.00 20.84           C  
-ATOM    519  N   ASP A  72      -4.183  69.698  70.626  1.00 20.45           N  
-ATOM    520  CA  ASP A  72      -3.127  69.544  71.594  1.00 21.84           C  
-ATOM    521  C   ASP A  72      -3.302  70.556  72.658  1.00 26.30           C  
-ATOM    522  O   ASP A  72      -3.206  71.743  72.396  1.00 30.97           O  
-ATOM    523  CB  ASP A  72      -1.754  69.806  70.955  1.00 20.11           C  
-ATOM    524  CG  ASP A  72      -0.569  69.712  71.938  1.00 16.69           C  
-ATOM    525  OD1 ASP A  72      -0.730  69.182  73.035  1.00 14.30           O  
-ATOM    526  OD2 ASP A  72       0.509  70.179  71.599  1.00 15.91           O  
-ATOM    527  N   GLU A  73      -3.506  70.103  73.893  1.00 26.74           N  
-ATOM    528  CA  GLU A  73      -3.640  71.101  74.945  1.00 27.99           C  
-ATOM    529  C   GLU A  73      -2.727  70.780  76.094  1.00 27.05           C  
-ATOM    530  O   GLU A  73      -3.059  70.917  77.258  1.00 29.33           O  
-ATOM    531  CB  GLU A  73      -5.101  71.421  75.302  1.00 27.16           C  
-ATOM    532  CG  GLU A  73      -5.977  70.214  75.663  1.00 24.07           C  
-ATOM    533  CD  GLU A  73      -7.451  70.568  75.563  1.00 25.62           C  
-ATOM    534  OE1 GLU A  73      -7.784  71.736  75.339  1.00 26.72           O  
-ATOM    535  OE2 GLU A  73      -8.264  69.660  75.686  1.00 28.37           O  
-ATOM    536  N   GLN A  74      -1.517  70.335  75.725  1.00 24.18           N  
-ATOM    537  CA  GLN A  74      -0.546  70.019  76.766  1.00 19.75           C  
-ATOM    538  C   GLN A  74       0.044  71.294  77.338  1.00 19.07           C  
-ATOM    539  O   GLN A  74       0.621  71.275  78.414  1.00 27.55           O  
-ATOM    540  CB  GLN A  74       0.568  69.058  76.295  1.00 17.91           C  
-ATOM    541  CG  GLN A  74       1.124  68.127  77.404  1.00 15.27           C  
-ATOM    542  CD  GLN A  74       1.981  68.819  78.458  1.00 19.09           C  
-ATOM    543  N   PHE A  75      -0.054  72.391  76.599  1.00 16.81           N  
-ATOM    544  CA  PHE A  75       0.473  73.652  77.110  1.00 14.63           C  
-ATOM    545  C   PHE A  75      -0.519  74.701  76.670  1.00 15.75           C  
-ATOM    546  O   PHE A  75      -0.237  75.476  75.759  1.00 12.66           O  
-ATOM    547  CB  PHE A  75       1.868  73.986  76.534  1.00 15.63           C  
-ATOM    548  CG  PHE A  75       2.928  72.957  76.865  1.00 18.37           C  
-ATOM    549  CD1 PHE A  75       3.598  72.994  78.100  1.00 20.71           C  
-ATOM    550  CD2 PHE A  75       3.258  71.951  75.946  1.00 18.70           C  
-ATOM    551  CE1 PHE A  75       4.584  72.045  78.399  1.00 19.08           C  
-ATOM    552  CE2 PHE A  75       4.235  70.996  76.251  1.00 18.19           C  
-ATOM    553  CZ  PHE A  75       4.903  71.041  77.477  1.00 17.69           C  
-ATOM    554  N   PRO A  76      -1.744  74.678  77.265  1.00 16.59           N  
-ATOM    555  CA  PRO A  76      -2.817  75.523  76.755  1.00 14.83           C  
-ATOM    556  C   PRO A  76      -2.395  76.960  76.723  1.00 13.89           C  
-ATOM    557  O   PRO A  76      -1.759  77.441  77.645  1.00 13.58           O  
-ATOM    558  CB  PRO A  76      -3.987  75.306  77.719  1.00  8.91           C  
-ATOM    559  CG  PRO A  76      -3.700  73.971  78.406  1.00 14.56           C  
-ATOM    560  CD  PRO A  76      -2.166  73.842  78.392  1.00 16.53           C  
-ATOM    561  N   GLY A  77      -2.741  77.619  75.619  1.00 15.94           N  
-ATOM    562  CA  GLY A  77      -2.389  79.024  75.478  1.00 19.13           C  
-ATOM    563  C   GLY A  77      -0.983  79.255  74.957  1.00 20.30           C  
-ATOM    564  O   GLY A  77      -0.685  80.291  74.364  1.00 21.30           O  
-ATOM    565  N   PHE A  78      -0.109  78.252  75.139  1.00 15.84           N  
-ATOM    566  CA  PHE A  78       1.246  78.450  74.670  1.00 12.27           C  
-ATOM    567  C   PHE A  78       1.308  78.493  73.158  1.00 14.11           C  
-ATOM    568  O   PHE A  78       0.957  77.528  72.493  1.00 13.80           O  
-ATOM    569  CB  PHE A  78       2.119  77.307  75.170  1.00  5.30           C  
-ATOM    570  CG  PHE A  78       3.577  77.446  74.816  1.00  2.00           C  
-ATOM    571  CD1 PHE A  78       4.231  78.684  74.890  1.00  2.00           C  
-ATOM    572  CD2 PHE A  78       4.300  76.310  74.427  1.00  4.23           C  
-ATOM    573  CE1 PHE A  78       5.597  78.780  74.589  1.00  4.27           C  
-ATOM    574  CE2 PHE A  78       5.664  76.406  74.135  1.00  2.00           C  
-ATOM    575  CZ  PHE A  78       6.313  77.638  74.221  1.00  3.02           C  
-ATOM    576  N   SER A  79       1.815  79.598  72.611  1.00 14.75           N  
-ATOM    577  CA  SER A  79       1.897  79.700  71.151  1.00 15.44           C  
-ATOM    578  C   SER A  79       2.697  78.584  70.502  1.00 14.29           C  
-ATOM    579  O   SER A  79       2.311  78.023  69.490  1.00 16.49           O  
-ATOM    580  CB  SER A  79       2.481  81.045  70.710  1.00 15.68           C  
-ATOM    581  OG  SER A  79       3.691  81.268  71.437  1.00 27.82           O  
-ATOM    582  N   GLY A  80       3.810  78.235  71.123  1.00 11.96           N  
-ATOM    583  CA  GLY A  80       4.616  77.182  70.527  1.00 13.22           C  
-ATOM    584  C   GLY A  80       3.864  75.898  70.204  1.00 11.30           C  
-ATOM    585  O   GLY A  80       4.277  75.133  69.351  1.00 10.75           O  
-ATOM    586  N   SER A  81       2.763  75.636  70.908  1.00 13.86           N  
-ATOM    587  CA  SER A  81       2.028  74.419  70.622  1.00 18.66           C  
-ATOM    588  C   SER A  81       0.785  74.773  69.848  1.00 19.99           C  
-ATOM    589  O   SER A  81       0.384  74.134  68.881  1.00 22.67           O  
-ATOM    590  CB  SER A  81       1.723  73.612  71.906  1.00 18.45           C  
-ATOM    591  OG  SER A  81       0.831  74.263  72.818  1.00 22.06           O  
-ATOM    592  N   GLU A  82       0.180  75.859  70.287  1.00 22.40           N  
-ATOM    593  CA  GLU A  82      -1.040  76.335  69.685  1.00 25.67           C  
-ATOM    594  C   GLU A  82      -0.906  76.617  68.200  1.00 23.30           C  
-ATOM    595  O   GLU A  82      -1.831  76.370  67.440  1.00 27.14           O  
-ATOM    596  CB  GLU A  82      -1.532  77.605  70.422  1.00 32.47           C  
-ATOM    597  CG  GLU A  82      -1.881  77.416  71.915  1.00 36.84           C  
-ATOM    598  CD  GLU A  82      -3.270  76.830  72.117  1.00 43.72           C  
-ATOM    599  OE1 GLU A  82      -3.543  75.763  71.555  1.00 46.39           O  
-ATOM    600  OE2 GLU A  82      -4.068  77.443  72.835  1.00 46.73           O  
-ATOM    601  N   MET A  83       0.248  77.120  67.780  1.00 18.06           N  
-ATOM    602  CA  MET A  83       0.401  77.412  66.360  1.00 17.25           C  
-ATOM    603  C   MET A  83       0.068  76.234  65.434  1.00 17.90           C  
-ATOM    604  O   MET A  83      -0.217  76.428  64.259  1.00 21.67           O  
-ATOM    605  CB  MET A  83       1.822  77.934  66.058  1.00 15.60           C  
-ATOM    606  CG  MET A  83       2.927  76.975  66.505  1.00 19.41           C  
-ATOM    607  SD  MET A  83       4.383  77.143  65.446  1.00 28.06           S  
-ATOM    608  CE  MET A  83       5.245  78.487  66.290  1.00 35.21           C  
-ATOM    609  N   TRP A  84       0.122  75.015  65.987  1.00 13.03           N  
-ATOM    610  CA  TRP A  84      -0.154  73.823  65.211  1.00 10.68           C  
-ATOM    611  C   TRP A  84      -1.550  73.249  65.396  1.00 11.34           C  
-ATOM    612  O   TRP A  84      -1.813  72.168  64.877  1.00 14.46           O  
-ATOM    613  CB  TRP A  84       0.789  72.670  65.625  1.00 11.48           C  
-ATOM    614  CG  TRP A  84       2.245  73.044  65.576  1.00 11.73           C  
-ATOM    615  CD1 TRP A  84       3.028  73.442  66.672  1.00 10.38           C  
-ATOM    616  CD2 TRP A  84       3.062  73.098  64.437  1.00 12.68           C  
-ATOM    617  NE1 TRP A  84       4.277  73.747  66.266  1.00  9.30           N  
-ATOM    618  CE2 TRP A  84       4.378  73.566  64.911  1.00 12.27           C  
-ATOM    619  CE3 TRP A  84       2.858  72.867  63.071  1.00 14.19           C  
-ATOM    620  CZ2 TRP A  84       5.406  73.766  63.977  1.00 13.17           C  
-ATOM    621  CZ3 TRP A  84       3.909  73.089  62.167  1.00 12.49           C  
-ATOM    622  CH2 TRP A  84       5.167  73.528  62.615  1.00 12.78           C  
-ATOM    623  N   ASN A  85      -2.439  73.908  66.131  1.00 11.34           N  
-ATOM    624  CA  ASN A  85      -3.767  73.296  66.338  1.00 14.49           C  
-ATOM    625  C   ASN A  85      -4.784  73.834  65.359  1.00 15.95           C  
-ATOM    626  O   ASN A  85      -4.643  74.972  64.916  1.00 19.96           O  
-ATOM    627  CB  ASN A  85      -4.309  73.642  67.730  1.00 19.34           C  
-ATOM    628  CG  ASN A  85      -3.765  72.718  68.778  1.00 22.60           C  
-ATOM    629  OD1 ASN A  85      -2.968  71.846  68.502  1.00 26.16           O  
-ATOM    630  ND2 ASN A  85      -4.202  72.907  70.003  1.00 26.67           N  
-ATOM    631  N   PRO A  86      -5.850  73.044  65.055  1.00 10.84           N  
-ATOM    632  CA  PRO A  86      -6.830  73.496  64.089  1.00 12.43           C  
-ATOM    633  C   PRO A  86      -7.317  74.875  64.470  1.00 14.14           C  
-ATOM    634  O   PRO A  86      -7.778  75.053  65.585  1.00 23.78           O  
-ATOM    635  CB  PRO A  86      -7.953  72.437  64.107  1.00  8.30           C  
-ATOM    636  CG  PRO A  86      -7.633  71.487  65.260  1.00  7.62           C  
-ATOM    637  CD  PRO A  86      -6.166  71.751  65.639  1.00 12.16           C  
-ATOM    638  N   ASN A  87      -7.184  75.827  63.546  1.00 13.45           N  
-ATOM    639  CA  ASN A  87      -7.612  77.184  63.822  1.00 11.93           C  
-ATOM    640  C   ASN A  87      -8.935  77.473  63.171  1.00 14.55           C  
-ATOM    641  O   ASN A  87      -9.237  78.627  62.907  1.00 18.89           O  
-ATOM    642  CB  ASN A  87      -6.571  78.188  63.300  1.00 14.24           C  
-ATOM    643  CG  ASN A  87      -6.456  78.117  61.801  1.00 16.61           C  
-ATOM    644  OD1 ASN A  87      -6.933  77.187  61.179  1.00 21.68           O  
-ATOM    645  ND2 ASN A  87      -5.786  79.091  61.213  1.00 23.10           N  
-ATOM    646  N   ARG A  88      -9.727  76.438  62.877  1.00 17.04           N  
-ATOM    647  CA  ARG A  88     -11.026  76.615  62.228  1.00 16.41           C  
-ATOM    648  C   ARG A  88     -11.900  75.523  62.793  1.00 15.60           C  
-ATOM    649  O   ARG A  88     -11.425  74.616  63.461  1.00 19.57           O  
-ATOM    650  CB  ARG A  88     -10.897  76.429  60.692  1.00 18.43           C  
-ATOM    651  CG  ARG A  88     -10.398  77.678  59.953  1.00 18.59           C  
-ATOM    652  CD  ARG A  88     -11.553  78.663  59.658  1.00 25.23           C  
-ATOM    653  NE  ARG A  88     -11.109  79.955  59.127  1.00 30.01           N  
-ATOM    654  CZ  ARG A  88     -10.173  80.693  59.756  1.00 28.05           C  
-ATOM    655  N   GLU A  89     -13.204  75.606  62.516  1.00 14.40           N  
-ATOM    656  CA  GLU A  89     -14.088  74.573  63.058  1.00 14.71           C  
-ATOM    657  C   GLU A  89     -13.716  73.272  62.445  1.00 12.51           C  
-ATOM    658  O   GLU A  89     -13.467  73.181  61.256  1.00 15.65           O  
-ATOM    659  CB  GLU A  89     -15.585  74.844  62.744  1.00 19.87           C  
-ATOM    660  CG  GLU A  89     -16.649  73.877  63.346  1.00 26.55           C  
-ATOM    661  N   MET A  90     -13.654  72.264  63.280  1.00 12.40           N  
-ATOM    662  CA  MET A  90     -13.329  70.979  62.735  1.00 12.40           C  
-ATOM    663  C   MET A  90     -14.657  70.444  62.245  1.00 13.29           C  
-ATOM    664  O   MET A  90     -15.685  70.875  62.764  1.00 11.14           O  
-ATOM    665  CB  MET A  90     -12.753  70.062  63.817  1.00 13.61           C  
-ATOM    666  CG  MET A  90     -11.597  70.693  64.597  1.00 13.67           C  
-ATOM    667  SD  MET A  90     -10.606  69.351  65.317  1.00 19.43           S  
-ATOM    668  CE  MET A  90     -11.676  68.792  66.655  1.00 20.51           C  
-ATOM    669  N   SER A  91     -14.617  69.531  61.273  1.00 13.06           N  
-ATOM    670  CA  SER A  91     -15.811  68.921  60.732  1.00 14.99           C  
-ATOM    671  C   SER A  91     -15.326  67.704  59.970  1.00 15.19           C  
-ATOM    672  O   SER A  91     -14.161  67.604  59.592  1.00 14.69           O  
-ATOM    673  CB  SER A  91     -16.520  69.899  59.763  1.00 18.90           C  
-ATOM    674  OG  SER A  91     -17.801  69.436  59.296  1.00 25.45           O  
-ATOM    675  N   GLU A  92     -16.250  66.746  59.745  1.00 13.93           N  
-ATOM    676  CA  GLU A  92     -15.851  65.579  58.959  1.00 13.90           C  
-ATOM    677  C   GLU A  92     -15.772  66.009  57.501  1.00 18.57           C  
-ATOM    678  O   GLU A  92     -15.003  65.503  56.698  1.00 20.05           O  
-ATOM    679  CB  GLU A  92     -16.781  64.389  59.120  1.00 10.43           C  
-ATOM    680  CG  GLU A  92     -16.496  63.628  60.415  1.00 12.39           C  
-ATOM    681  CD  GLU A  92     -17.146  62.256  60.346  1.00 13.13           C  
-ATOM    682  OE1 GLU A  92     -18.335  62.159  60.636  1.00 10.48           O  
-ATOM    683  OE2 GLU A  92     -16.460  61.294  59.986  1.00 16.23           O  
-ATOM    684  N   ASP A  93     -16.625  66.984  57.189  1.00 17.71           N  
-ATOM    685  CA  ASP A  93     -16.665  67.591  55.878  1.00 17.64           C  
-ATOM    686  C   ASP A  93     -15.462  68.539  55.844  1.00 19.89           C  
-ATOM    687  O   ASP A  93     -15.565  69.715  56.197  1.00 20.41           O  
-ATOM    688  CB  ASP A  93     -17.978  68.384  55.757  1.00 17.65           C  
-ATOM    689  CG  ASP A  93     -18.136  69.104  54.433  1.00 23.35           C  
-ATOM    690  OD1 ASP A  93     -17.123  69.476  53.846  1.00 22.00           O  
-ATOM    691  OD2 ASP A  93     -19.273  69.294  53.993  1.00 26.90           O  
-ATOM    692  N   CYS A  94     -14.311  68.010  55.427  1.00 18.50           N  
-ATOM    693  CA  CYS A  94     -13.140  68.872  55.416  1.00 18.58           C  
-ATOM    694  C   CYS A  94     -12.241  68.687  54.217  1.00 20.84           C  
-ATOM    695  O   CYS A  94     -11.129  69.207  54.206  1.00 24.77           O  
-ATOM    696  CB  CYS A  94     -12.313  68.570  56.663  1.00 15.68           C  
-ATOM    697  SG  CYS A  94     -11.885  66.805  56.660  1.00  8.01           S  
-ATOM    698  N   LEU A  95     -12.699  67.928  53.211  1.00 17.60           N  
-ATOM    699  CA  LEU A  95     -11.859  67.746  52.024  1.00 15.22           C  
-ATOM    700  C   LEU A  95     -12.026  68.932  51.043  1.00 13.32           C  
-ATOM    701  O   LEU A  95     -12.969  68.980  50.253  1.00 14.93           O  
-ATOM    702  CB  LEU A  95     -12.223  66.423  51.337  1.00 11.27           C  
-ATOM    703  CG  LEU A  95     -11.924  65.184  52.183  1.00  9.22           C  
-ATOM    704  CD1 LEU A  95     -12.398  63.918  51.459  1.00 12.24           C  
-ATOM    705  CD2 LEU A  95     -10.420  65.086  52.473  1.00  9.44           C  
-ATOM    706  N   TYR A  96     -11.101  69.895  51.130  1.00  9.45           N  
-ATOM    707  CA  TYR A  96     -11.074  71.093  50.284  1.00 10.39           C  
-ATOM    708  C   TYR A  96      -9.627  71.405  50.015  1.00  9.24           C  
-ATOM    709  O   TYR A  96      -8.755  70.757  50.572  1.00 11.56           O  
-ATOM    710  CB  TYR A  96     -11.648  72.315  51.011  1.00  6.27           C  
-ATOM    711  CG  TYR A  96     -13.088  72.116  51.361  1.00 12.78           C  
-ATOM    712  CD1 TYR A  96     -13.465  71.437  52.529  1.00 17.73           C  
-ATOM    713  CD2 TYR A  96     -14.069  72.620  50.511  1.00 17.02           C  
-ATOM    714  CE1 TYR A  96     -14.825  71.256  52.837  1.00 24.42           C  
-ATOM    715  CE2 TYR A  96     -15.421  72.460  50.809  1.00 23.71           C  
-ATOM    716  CZ  TYR A  96     -15.807  71.768  51.968  1.00 25.91           C  
-ATOM    717  OH  TYR A  96     -17.150  71.591  52.241  1.00 30.42           O  
-ATOM    718  N   LEU A  97      -9.366  72.384  49.156  1.00  7.65           N  
-ATOM    719  CA  LEU A  97      -7.987  72.753  48.892  1.00  7.91           C  
-ATOM    720  C   LEU A  97      -7.950  74.249  48.762  1.00  9.01           C  
-ATOM    721  O   LEU A  97      -8.992  74.870  48.596  1.00 10.81           O  
-ATOM    722  CB  LEU A  97      -7.373  71.963  47.728  1.00  9.23           C  
-ATOM    723  CG  LEU A  97      -8.126  71.943  46.392  1.00  6.13           C  
-ATOM    724  CD1 LEU A  97      -8.029  73.281  45.657  1.00  8.91           C  
-ATOM    725  CD2 LEU A  97      -7.571  70.818  45.512  1.00  3.47           C  
-ATOM    726  N   ASN A  98      -6.752  74.834  48.859  1.00 11.33           N  
-ATOM    727  CA  ASN A  98      -6.601  76.300  48.768  1.00 13.70           C  
-ATOM    728  C   ASN A  98      -5.518  76.564  47.749  1.00 16.15           C  
-ATOM    729  O   ASN A  98      -4.615  75.746  47.647  1.00 20.18           O  
-ATOM    730  CB  ASN A  98      -6.149  76.913  50.122  1.00 17.58           C  
-ATOM    731  CG  ASN A  98      -6.964  76.389  51.307  1.00 18.01           C  
-ATOM    732  OD1 ASN A  98      -8.144  76.679  51.485  1.00 12.42           O  
-ATOM    733  ND2 ASN A  98      -6.307  75.544  52.103  1.00 16.23           N  
-ATOM    734  N   ILE A  99      -5.592  77.688  47.031  1.00 18.79           N  
-ATOM    735  CA  ILE A  99      -4.629  78.040  45.997  1.00 15.69           C  
-ATOM    736  C   ILE A  99      -4.294  79.528  46.085  1.00 12.75           C  
-ATOM    737  O   ILE A  99      -5.196  80.364  46.115  1.00 12.25           O  
-ATOM    738  CB  ILE A  99      -5.339  77.820  44.625  1.00 21.08           C  
-ATOM    739  CG1 ILE A  99      -6.118  76.476  44.526  1.00 22.08           C  
-ATOM    740  CG2 ILE A  99      -4.408  78.076  43.422  1.00 20.15           C  
-ATOM    741  CD1 ILE A  99      -6.870  76.280  43.201  1.00 26.01           C  
-ATOM    742  N   TRP A 100      -3.013  79.861  46.120  1.00 10.55           N  
-ATOM    743  CA  TRP A 100      -2.637  81.271  46.144  1.00 17.45           C  
-ATOM    744  C   TRP A 100      -2.096  81.427  44.763  1.00 23.25           C  
-ATOM    745  O   TRP A 100      -1.264  80.608  44.366  1.00 28.28           O  
-ATOM    746  CB  TRP A 100      -1.524  81.610  47.157  1.00 18.88           C  
-ATOM    747  CG  TRP A 100      -2.133  81.683  48.538  1.00 18.39           C  
-ATOM    748  CD1 TRP A 100      -2.729  82.828  49.114  1.00 18.87           C  
-ATOM    749  CD2 TRP A 100      -2.332  80.619  49.423  1.00 16.27           C  
-ATOM    750  NE1 TRP A 100      -3.304  82.509  50.294  1.00 20.89           N  
-ATOM    751  CE2 TRP A 100      -3.111  81.179  50.541  1.00 14.55           C  
-ATOM    752  CE3 TRP A 100      -2.010  79.260  49.404  1.00 17.00           C  
-ATOM    753  CZ2 TRP A 100      -3.551  80.332  51.550  1.00 15.08           C  
-ATOM    754  CZ3 TRP A 100      -2.458  78.443  50.445  1.00 16.68           C  
-ATOM    755  CH2 TRP A 100      -3.225  78.966  51.500  1.00 20.05           C  
-ATOM    756  N   VAL A 101      -2.574  82.443  44.034  1.00 25.62           N  
-ATOM    757  CA  VAL A 101      -2.140  82.667  42.646  1.00 23.97           C  
-ATOM    758  C   VAL A 101      -1.583  84.090  42.563  1.00 24.09           C  
-ATOM    759  O   VAL A 101      -2.116  84.979  43.228  1.00 26.95           O  
-ATOM    760  CB  VAL A 101      -3.342  82.445  41.686  1.00 21.20           C  
-ATOM    761  CG1 VAL A 101      -2.914  82.450  40.222  1.00 22.08           C  
-ATOM    762  CG2 VAL A 101      -4.116  81.135  41.970  1.00 21.41           C  
-ATOM    763  N   PRO A 102      -0.491  84.299  41.786  1.00 21.15           N  
-ATOM    764  CA  PRO A 102      -0.021  85.659  41.549  1.00 21.79           C  
-ATOM    765  C   PRO A 102      -1.007  86.572  40.836  1.00 27.45           C  
-ATOM    766  O   PRO A 102      -2.032  86.168  40.293  1.00 29.87           O  
-ATOM    767  CB  PRO A 102       1.267  85.476  40.748  1.00 18.71           C  
-ATOM    768  CG  PRO A 102       1.739  84.039  41.042  1.00 19.23           C  
-ATOM    769  CD  PRO A 102       0.455  83.261  41.369  1.00 21.10           C  
-ATOM    770  N   SER A 103      -0.639  87.853  40.861  1.00 31.89           N  
-ATOM    771  CA  SER A 103      -1.418  88.895  40.214  1.00 36.65           C  
-ATOM    772  C   SER A 103      -0.335  89.673  39.495  1.00 40.27           C  
-ATOM    773  O   SER A 103       0.624  90.067  40.149  1.00 45.43           O  
-ATOM    774  CB  SER A 103      -2.139  89.825  41.201  1.00 33.60           C  
-ATOM    775  OG  SER A 103      -2.995  90.716  40.485  1.00 36.95           O  
-ATOM    776  N   PRO A 104      -0.464  89.891  38.178  1.00 39.36           N  
-ATOM    777  CA  PRO A 104      -1.536  89.364  37.338  1.00 34.51           C  
-ATOM    778  C   PRO A 104      -1.392  87.856  37.227  1.00 29.79           C  
-ATOM    779  O   PRO A 104      -0.305  87.316  37.385  1.00 27.40           O  
-ATOM    780  CB  PRO A 104      -1.295  90.051  35.988  1.00 39.40           C  
-ATOM    781  CG  PRO A 104       0.176  90.518  35.995  1.00 40.72           C  
-ATOM    782  CD  PRO A 104       0.561  90.646  37.471  1.00 40.10           C  
-ATOM    783  N   ARG A 105      -2.532  87.204  36.976  1.00 25.21           N  
-ATOM    784  CA  ARG A 105      -2.520  85.753  36.840  1.00 25.56           C  
-ATOM    785  C   ARG A 105      -1.487  85.352  35.791  1.00 28.23           C  
-ATOM    786  O   ARG A 105      -1.502  85.940  34.720  1.00 31.77           O  
-ATOM    787  CB  ARG A 105      -3.902  85.296  36.371  1.00 23.36           C  
-ATOM    788  CG  ARG A 105      -4.102  83.777  36.413  1.00 25.28           C  
-ATOM    789  CD  ARG A 105      -5.452  83.331  35.826  1.00 33.93           C  
-ATOM    790  NE  ARG A 105      -6.571  84.129  36.333  1.00 38.86           N  
-ATOM    791  CZ  ARG A 105      -7.844  83.856  35.996  1.00 40.85           C  
-ATOM    792  NH1 ARG A 105      -8.146  82.852  35.176  1.00 45.02           N  
-ATOM    793  NH2 ARG A 105      -8.831  84.600  36.485  1.00 41.71           N  
-ATOM    794  N   PRO A 106      -0.605  84.386  36.088  1.00 30.08           N  
-ATOM    795  CA  PRO A 106       0.352  83.921  35.084  1.00 30.73           C  
-ATOM    796  C   PRO A 106      -0.389  83.037  34.076  1.00 32.25           C  
-ATOM    797  O   PRO A 106      -1.511  82.591  34.312  1.00 32.38           O  
-ATOM    798  CB  PRO A 106       1.400  83.140  35.902  1.00 30.25           C  
-ATOM    799  CG  PRO A 106       0.702  82.765  37.223  1.00 31.36           C  
-ATOM    800  CD  PRO A 106      -0.475  83.744  37.389  1.00 29.44           C  
-ATOM    801  N   LYS A 107       0.301  82.769  32.946  1.00 30.72           N  
-ATOM    802  CA  LYS A 107      -0.264  81.958  31.873  1.00 27.34           C  
-ATOM    803  C   LYS A 107      -0.089  80.476  32.151  1.00 26.12           C  
-ATOM    804  O   LYS A 107      -1.005  79.674  32.119  1.00 25.20           O  
-ATOM    805  CB  LYS A 107       0.287  82.423  30.530  1.00 28.41           C  
-ATOM    806  N   SER A 108       1.144  80.134  32.430  1.00 25.79           N  
-ATOM    807  CA  SER A 108       1.465  78.762  32.780  1.00 29.14           C  
-ATOM    808  C   SER A 108       2.701  78.929  33.610  1.00 30.57           C  
-ATOM    809  O   SER A 108       3.641  79.517  33.095  1.00 30.49           O  
-ATOM    810  CB  SER A 108       1.841  77.916  31.571  1.00 28.68           C  
-ATOM    811  OG  SER A 108       0.699  77.249  31.060  1.00 37.53           O  
-ATOM    812  N   THR A 109       2.696  78.444  34.861  1.00 29.70           N  
-ATOM    813  CA  THR A 109       3.864  78.570  35.721  1.00 25.60           C  
-ATOM    814  C   THR A 109       3.887  77.365  36.631  1.00 25.96           C  
-ATOM    815  O   THR A 109       2.918  76.606  36.626  1.00 28.79           O  
-ATOM    816  CB  THR A 109       3.839  79.919  36.435  1.00 22.51           C  
-ATOM    817  OG1 THR A 109       5.133  80.163  36.970  1.00 30.15           O  
-ATOM    818  CG2 THR A 109       2.746  80.107  37.496  1.00 20.47           C  
-ATOM    819  N   THR A 110       4.999  77.202  37.372  1.00 20.30           N  
-ATOM    820  CA  THR A 110       5.191  76.072  38.277  1.00 16.91           C  
-ATOM    821  C   THR A 110       4.161  76.062  39.382  1.00 16.26           C  
-ATOM    822  O   THR A 110       3.648  77.099  39.804  1.00 16.76           O  
-ATOM    823  CB  THR A 110       6.597  76.167  38.862  1.00 17.56           C  
-ATOM    824  OG1 THR A 110       7.482  76.435  37.782  1.00 19.32           O  
-ATOM    825  CG2 THR A 110       7.093  74.903  39.562  1.00 17.74           C  
-ATOM    826  N   VAL A 111       3.905  74.847  39.850  1.00 12.04           N  
-ATOM    827  CA  VAL A 111       2.933  74.650  40.884  1.00 12.71           C  
-ATOM    828  C   VAL A 111       3.619  73.910  42.015  1.00 13.45           C  
-ATOM    829  O   VAL A 111       4.440  73.036  41.749  1.00  8.98           O  
-ATOM    830  CB  VAL A 111       1.822  73.790  40.267  1.00 10.48           C  
-ATOM    831  CG1 VAL A 111       0.650  73.518  41.209  1.00 17.35           C  
-ATOM    832  CG2 VAL A 111       1.294  74.387  38.961  1.00 10.89           C  
-ATOM    833  N   MET A 112       3.268  74.270  43.272  1.00 13.92           N  
-ATOM    834  CA  MET A 112       3.810  73.625  44.465  1.00  8.38           C  
-ATOM    835  C   MET A 112       2.588  73.253  45.273  1.00 10.42           C  
-ATOM    836  O   MET A 112       1.780  74.125  45.580  1.00 12.73           O  
-ATOM    837  CB  MET A 112       4.730  74.574  45.226  1.00  2.88           C  
-ATOM    838  CG  MET A 112       5.907  75.036  44.352  1.00  2.00           C  
-ATOM    839  SD  MET A 112       7.230  75.786  45.353  1.00  8.80           S  
-ATOM    840  CE  MET A 112       7.892  74.272  46.113  1.00  5.32           C  
-ATOM    841  N   VAL A 113       2.431  71.954  45.563  1.00  9.72           N  
-ATOM    842  CA  VAL A 113       1.284  71.466  46.333  1.00  9.94           C  
-ATOM    843  C   VAL A 113       1.840  71.047  47.683  1.00 12.79           C  
-ATOM    844  O   VAL A 113       2.714  70.192  47.747  1.00 17.85           O  
-ATOM    845  CB  VAL A 113       0.700  70.192  45.662  1.00  8.48           C  
-ATOM    846  CG1 VAL A 113      -0.476  69.582  46.422  1.00  5.76           C  
-ATOM    847  CG2 VAL A 113       0.339  70.337  44.185  1.00  5.88           C  
-ATOM    848  N   TRP A 114       1.310  71.613  48.756  1.00 13.62           N  
-ATOM    849  CA  TRP A 114       1.767  71.319  50.113  1.00 13.84           C  
-ATOM    850  C   TRP A 114       0.871  70.289  50.789  1.00 13.20           C  
-ATOM    851  O   TRP A 114      -0.340  70.506  50.888  1.00 16.95           O  
-ATOM    852  CB  TRP A 114       1.693  72.653  50.908  1.00 15.62           C  
-ATOM    853  CG  TRP A 114       2.009  72.493  52.386  1.00 16.04           C  
-ATOM    854  CD1 TRP A 114       1.093  72.608  53.465  1.00 16.62           C  
-ATOM    855  CD2 TRP A 114       3.257  72.186  52.940  1.00 12.64           C  
-ATOM    856  NE1 TRP A 114       1.724  72.376  54.643  1.00 14.39           N  
-ATOM    857  CE2 TRP A 114       3.044  72.106  54.395  1.00 10.99           C  
-ATOM    858  CE3 TRP A 114       4.520  71.943  52.408  1.00 12.85           C  
-ATOM    859  CZ2 TRP A 114       4.130  71.810  55.211  1.00 10.13           C  
-ATOM    860  CZ3 TRP A 114       5.589  71.640  53.260  1.00  9.96           C  
-ATOM    861  CH2 TRP A 114       5.392  71.573  54.643  1.00  9.36           C  
-ATOM    862  N   ILE A 115       1.487  69.200  51.262  1.00 12.94           N  
-ATOM    863  CA  ILE A 115       0.812  68.126  51.991  1.00 11.91           C  
-ATOM    864  C   ILE A 115       1.353  68.264  53.426  1.00 17.84           C  
-ATOM    865  O   ILE A 115       2.548  68.034  53.654  1.00 21.48           O  
-ATOM    866  CB  ILE A 115       1.185  66.764  51.380  1.00  8.50           C  
-ATOM    867  CG1 ILE A 115       1.022  66.806  49.833  1.00  6.95           C  
-ATOM    868  CG2 ILE A 115       0.438  65.597  52.059  1.00  2.50           C  
-ATOM    869  CD1 ILE A 115       1.134  65.447  49.121  1.00  5.12           C  
-ATOM    870  N   TYR A 116       0.453  68.652  54.372  1.00 16.62           N  
-ATOM    871  CA  TYR A 116       0.810  68.865  55.784  1.00 11.94           C  
-ATOM    872  C   TYR A 116       1.152  67.614  56.581  1.00 14.71           C  
-ATOM    873  O   TYR A 116       0.761  66.489  56.293  1.00 16.59           O  
-ATOM    874  CB  TYR A 116      -0.278  69.648  56.545  1.00  9.80           C  
-ATOM    875  CG  TYR A 116      -1.647  69.008  56.579  1.00  8.10           C  
-ATOM    876  CD1 TYR A 116      -1.881  67.740  57.158  1.00  9.71           C  
-ATOM    877  CD2 TYR A 116      -2.725  69.704  56.022  1.00  7.13           C  
-ATOM    878  CE1 TYR A 116      -3.169  67.182  57.164  1.00  6.62           C  
-ATOM    879  CE2 TYR A 116      -4.006  69.153  56.019  1.00  3.94           C  
-ATOM    880  CZ  TYR A 116      -4.225  67.898  56.586  1.00  4.37           C  
-ATOM    881  OH  TYR A 116      -5.500  67.391  56.594  1.00 10.79           O  
-ATOM    882  N   GLY A 117       1.886  67.862  57.656  1.00 16.91           N  
-ATOM    883  CA  GLY A 117       2.315  66.812  58.550  1.00 14.98           C  
-ATOM    884  C   GLY A 117       1.378  66.772  59.725  1.00 16.30           C  
-ATOM    885  O   GLY A 117       0.361  67.469  59.779  1.00 13.80           O  
-ATOM    886  N   GLY A 118       1.802  65.935  60.691  1.00 17.02           N  
-ATOM    887  CA  GLY A 118       1.026  65.735  61.919  1.00 11.44           C  
-ATOM    888  C   GLY A 118       0.969  64.274  62.377  1.00  8.72           C  
-ATOM    889  O   GLY A 118      -0.008  63.845  62.978  1.00  5.62           O  
-ATOM    890  N   GLY A 119       2.020  63.492  62.055  1.00  2.00           N  
-ATOM    891  CA  GLY A 119       1.985  62.085  62.487  1.00  5.94           C  
-ATOM    892  C   GLY A 119       0.749  61.270  62.079  1.00  8.79           C  
-ATOM    893  O   GLY A 119       0.359  60.285  62.688  1.00 13.50           O  
-ATOM    894  N   PHE A 120       0.105  61.718  61.013  1.00 11.22           N  
-ATOM    895  CA  PHE A 120      -1.093  61.067  60.490  1.00 12.14           C  
-ATOM    896  C   PHE A 120      -2.344  61.235  61.335  1.00 15.23           C  
-ATOM    897  O   PHE A 120      -3.405  60.852  60.864  1.00 15.16           O  
-ATOM    898  CB  PHE A 120      -0.898  59.592  60.086  1.00 11.92           C  
-ATOM    899  CG  PHE A 120      -0.021  59.437  58.865  1.00 11.41           C  
-ATOM    900  CD1 PHE A 120      -0.517  59.828  57.608  1.00 11.70           C  
-ATOM    901  CD2 PHE A 120       1.272  58.896  58.957  1.00 12.73           C  
-ATOM    902  CE1 PHE A 120       0.257  59.674  56.456  1.00 11.52           C  
-ATOM    903  CE2 PHE A 120       2.049  58.734  57.798  1.00 14.44           C  
-ATOM    904  CZ  PHE A 120       1.542  59.125  56.554  1.00 14.34           C  
-ATOM    905  N   TYR A 121      -2.252  61.817  62.554  1.00 19.62           N  
-ATOM    906  CA  TYR A 121      -3.430  62.023  63.438  1.00 13.61           C  
-ATOM    907  C   TYR A 121      -3.834  63.487  63.533  1.00 12.90           C  
-ATOM    908  O   TYR A 121      -4.836  63.806  64.170  1.00 15.56           O  
-ATOM    909  CB  TYR A 121      -3.222  61.517  64.891  1.00 11.91           C  
-ATOM    910  CG  TYR A 121      -2.162  62.299  65.637  1.00 11.99           C  
-ATOM    911  CD1 TYR A 121      -0.821  61.913  65.545  1.00 12.64           C  
-ATOM    912  CD2 TYR A 121      -2.498  63.446  66.378  1.00  8.96           C  
-ATOM    913  CE1 TYR A 121       0.169  62.668  66.173  1.00 16.39           C  
-ATOM    914  CE2 TYR A 121      -1.511  64.207  67.010  1.00 10.84           C  
-ATOM    915  CZ  TYR A 121      -0.169  63.811  66.912  1.00 16.22           C  
-ATOM    916  OH  TYR A 121       0.852  64.505  67.542  1.00 20.04           O  
-ATOM    917  N   SER A 122      -3.043  64.388  62.951  1.00 12.66           N  
-ATOM    918  CA  SER A 122      -3.433  65.783  63.028  1.00 13.78           C  
-ATOM    919  C   SER A 122      -2.996  66.469  61.746  1.00 15.52           C  
-ATOM    920  O   SER A 122      -2.343  65.840  60.917  1.00 19.00           O  
-ATOM    921  CB  SER A 122      -2.833  66.390  64.309  1.00 15.76           C  
-ATOM    922  OG  SER A 122      -1.385  66.399  64.278  1.00 15.94           O  
-ATOM    923  N   GLY A 123      -3.381  67.749  61.621  1.00 14.94           N  
-ATOM    924  CA  GLY A 123      -2.982  68.541  60.481  1.00 12.91           C  
-ATOM    925  C   GLY A 123      -4.081  69.464  59.985  1.00 14.38           C  
-ATOM    926  O   GLY A 123      -5.277  69.204  60.076  1.00 17.47           O  
-ATOM    927  N   SER A 124      -3.667  70.609  59.463  1.00 12.13           N  
-ATOM    928  CA  SER A 124      -4.608  71.546  58.902  1.00 15.36           C  
-ATOM    929  C   SER A 124      -3.839  72.263  57.826  1.00 19.62           C  
-ATOM    930  O   SER A 124      -2.623  72.360  57.868  1.00 21.18           O  
-ATOM    931  CB  SER A 124      -5.124  72.554  59.919  1.00 16.61           C  
-ATOM    932  OG  SER A 124      -5.954  71.920  60.876  1.00 22.82           O  
-ATOM    933  N   SER A 125      -4.571  72.752  56.839  1.00 20.53           N  
-ATOM    934  CA  SER A 125      -3.953  73.469  55.739  1.00 19.71           C  
-ATOM    935  C   SER A 125      -4.045  74.981  55.940  1.00 19.53           C  
-ATOM    936  O   SER A 125      -3.391  75.776  55.296  1.00 23.23           O  
-ATOM    937  CB  SER A 125      -4.691  73.059  54.458  1.00 16.00           C  
-ATOM    938  OG  SER A 125      -6.096  73.286  54.626  1.00 20.88           O  
-ATOM    939  N   THR A 126      -4.918  75.336  56.865  1.00 17.15           N  
-ATOM    940  CA  THR A 126      -5.267  76.683  57.258  1.00 16.37           C  
-ATOM    941  C   THR A 126      -4.343  77.317  58.289  1.00 15.76           C  
-ATOM    942  O   THR A 126      -4.533  78.441  58.740  1.00 19.46           O  
-ATOM    943  CB  THR A 126      -6.684  76.536  57.859  1.00 18.02           C  
-ATOM    944  OG1 THR A 126      -6.568  75.606  58.952  1.00 21.85           O  
-ATOM    945  CG2 THR A 126      -7.685  75.878  56.882  1.00 14.37           C  
-ATOM    946  N   LEU A 127      -3.337  76.562  58.719  1.00 13.50           N  
-ATOM    947  CA  LEU A 127      -2.451  77.133  59.722  1.00 11.70           C  
-ATOM    948  C   LEU A 127      -1.705  78.306  59.147  1.00 12.34           C  
-ATOM    949  O   LEU A 127      -1.409  78.366  57.975  1.00 17.17           O  
-ATOM    950  CB  LEU A 127      -1.422  76.104  60.212  1.00  9.96           C  
-ATOM    951  CG  LEU A 127      -2.002  74.756  60.677  1.00  7.51           C  
-ATOM    952  CD1 LEU A 127      -0.870  73.911  61.282  1.00  9.80           C  
-ATOM    953  CD2 LEU A 127      -3.143  74.925  61.696  1.00  6.16           C  
-ATOM    954  N   ASP A 128      -1.321  79.238  59.977  1.00 13.92           N  
-ATOM    955  CA  ASP A 128      -0.609  80.406  59.501  1.00 16.51           C  
-ATOM    956  C   ASP A 128       0.772  80.081  59.013  1.00 15.68           C  
-ATOM    957  O   ASP A 128       1.313  80.837  58.228  1.00 18.82           O  
-ATOM    958  CB  ASP A 128      -0.487  81.527  60.544  1.00 23.30           C  
-ATOM    959  CG  ASP A 128      -1.804  82.083  61.084  1.00 28.62           C  
-ATOM    960  OD1 ASP A 128      -2.870  81.733  60.572  1.00 36.47           O  
-ATOM    961  OD2 ASP A 128      -1.751  82.873  62.029  1.00 35.21           O  
-ATOM    962  N   VAL A 129       1.374  78.973  59.458  1.00 16.76           N  
-ATOM    963  CA  VAL A 129       2.721  78.716  58.919  1.00 17.51           C  
-ATOM    964  C   VAL A 129       2.614  78.002  57.572  1.00 20.95           C  
-ATOM    965  O   VAL A 129       3.617  77.561  57.037  1.00 24.78           O  
-ATOM    966  CB  VAL A 129       3.617  77.937  59.912  1.00  9.97           C  
-ATOM    967  CG1 VAL A 129       4.157  78.846  61.020  1.00 15.67           C  
-ATOM    968  CG2 VAL A 129       2.894  76.746  60.546  1.00  7.52           C  
-ATOM    969  N   TYR A 130       1.381  77.844  57.063  1.00 17.72           N  
-ATOM    970  CA  TYR A 130       1.176  77.188  55.783  1.00 15.58           C  
-ATOM    971  C   TYR A 130       0.429  78.157  54.867  1.00 22.21           C  
-ATOM    972  O   TYR A 130      -0.228  77.797  53.894  1.00 24.39           O  
-ATOM    973  CB  TYR A 130       0.299  75.934  55.952  1.00 11.62           C  
-ATOM    974  CG  TYR A 130       0.825  74.823  56.857  1.00  9.44           C  
-ATOM    975  CD1 TYR A 130       2.180  74.673  57.197  1.00  5.49           C  
-ATOM    976  CD2 TYR A 130      -0.092  73.884  57.363  1.00  8.88           C  
-ATOM    977  CE1 TYR A 130       2.591  73.611  58.022  1.00  6.11           C  
-ATOM    978  CE2 TYR A 130       0.320  72.812  58.171  1.00  5.33           C  
-ATOM    979  CZ  TYR A 130       1.671  72.666  58.500  1.00  7.17           C  
-ATOM    980  OH  TYR A 130       2.143  71.595  59.244  1.00  4.45           O  
-ATOM    981  N   ASN A 131       0.493  79.452  55.222  1.00 24.81           N  
-ATOM    982  CA  ASN A 131      -0.197  80.445  54.400  1.00 23.92           C  
-ATOM    983  C   ASN A 131       0.734  80.708  53.237  1.00 23.49           C  
-ATOM    984  O   ASN A 131       1.803  81.283  53.393  1.00 25.76           O  
-ATOM    985  CB  ASN A 131      -0.482  81.708  55.217  1.00 24.47           C  
-ATOM    986  CG  ASN A 131      -1.187  82.722  54.362  1.00 22.55           C  
-ATOM    987  OD1 ASN A 131      -0.626  83.207  53.402  1.00 22.56           O  
-ATOM    988  ND2 ASN A 131      -2.427  83.044  54.691  1.00 27.84           N  
-ATOM    989  N   GLY A 132       0.325  80.257  52.049  1.00 25.22           N  
-ATOM    990  CA  GLY A 132       1.201  80.415  50.887  1.00 24.01           C  
-ATOM    991  C   GLY A 132       1.292  81.780  50.223  1.00 24.53           C  
-ATOM    992  O   GLY A 132       1.938  81.880  49.181  1.00 22.81           O  
-ATOM    993  N   LYS A 133       0.691  82.840  50.796  1.00 23.16           N  
-ATOM    994  CA  LYS A 133       0.787  84.142  50.126  1.00 20.32           C  
-ATOM    995  C   LYS A 133       2.206  84.627  49.859  1.00 20.65           C  
-ATOM    996  O   LYS A 133       2.522  85.208  48.831  1.00 21.83           O  
-ATOM    997  CB  LYS A 133       0.023  85.259  50.877  1.00 16.95           C  
-ATOM    998  CG  LYS A 133       0.713  85.863  52.142  1.00 22.40           C  
-ATOM    999  CD  LYS A 133      -0.033  87.022  52.852  1.00 20.59           C  
-ATOM   1000  CE  LYS A 133      -1.463  86.654  53.243  1.00 30.03           C  
-ATOM   1001  NZ  LYS A 133      -2.093  87.733  53.974  1.00 36.80           N  
-ATOM   1002  N   TYR A 134       3.082  84.366  50.816  1.00 21.50           N  
-ATOM   1003  CA  TYR A 134       4.442  84.873  50.659  1.00 22.90           C  
-ATOM   1004  C   TYR A 134       5.211  84.124  49.615  1.00 22.76           C  
-ATOM   1005  O   TYR A 134       5.920  84.695  48.808  1.00 22.22           O  
-ATOM   1006  CB  TYR A 134       5.214  84.878  52.002  1.00 25.06           C  
-ATOM   1007  CG  TYR A 134       4.405  85.495  53.122  1.00 25.21           C  
-ATOM   1008  CD1 TYR A 134       4.387  86.883  53.331  1.00 26.12           C  
-ATOM   1009  CD2 TYR A 134       3.620  84.668  53.938  1.00 27.87           C  
-ATOM   1010  CE1 TYR A 134       3.581  87.440  54.333  1.00 29.44           C  
-ATOM   1011  CE2 TYR A 134       2.807  85.215  54.935  1.00 30.74           C  
-ATOM   1012  CZ  TYR A 134       2.783  86.605  55.135  1.00 32.62           C  
-ATOM   1013  OH  TYR A 134       1.969  87.160  56.108  1.00 36.70           O  
-ATOM   1014  N   LEU A 135       5.041  82.804  49.612  1.00 25.17           N  
-ATOM   1015  CA  LEU A 135       5.786  82.023  48.620  1.00 22.13           C  
-ATOM   1016  C   LEU A 135       5.305  82.336  47.200  1.00 23.51           C  
-ATOM   1017  O   LEU A 135       6.081  82.613  46.287  1.00 23.54           O  
-ATOM   1018  CB  LEU A 135       5.709  80.520  48.958  1.00 13.03           C  
-ATOM   1019  CG  LEU A 135       6.761  79.635  48.278  1.00  9.29           C  
-ATOM   1020  CD1 LEU A 135       8.181  80.179  48.469  1.00  6.96           C  
-ATOM   1021  CD2 LEU A 135       6.710  78.203  48.836  1.00  2.00           C  
-ATOM   1022  N   ALA A 136       3.969  82.313  47.054  1.00 22.76           N  
-ATOM   1023  CA  ALA A 136       3.352  82.583  45.765  1.00 22.99           C  
-ATOM   1024  C   ALA A 136       3.797  83.909  45.190  1.00 26.43           C  
-ATOM   1025  O   ALA A 136       4.072  84.061  44.008  1.00 31.51           O  
-ATOM   1026  CB  ALA A 136       1.822  82.620  45.886  1.00 24.06           C  
-ATOM   1027  N   TYR A 137       3.864  84.891  46.075  1.00 25.08           N  
-ATOM   1028  CA  TYR A 137       4.259  86.228  45.667  1.00 21.07           C  
-ATOM   1029  C   TYR A 137       5.752  86.352  45.390  1.00 19.78           C  
-ATOM   1030  O   TYR A 137       6.186  86.678  44.302  1.00 22.62           O  
-ATOM   1031  CB  TYR A 137       3.776  87.176  46.780  1.00 21.86           C  
-ATOM   1032  CG  TYR A 137       4.207  88.596  46.587  1.00 25.22           C  
-ATOM   1033  CD1 TYR A 137       5.469  89.006  47.056  1.00 26.11           C  
-ATOM   1034  CD2 TYR A 137       3.390  89.502  45.897  1.00 27.33           C  
-ATOM   1035  CE1 TYR A 137       5.934  90.303  46.813  1.00 26.02           C  
-ATOM   1036  CE2 TYR A 137       3.861  90.803  45.650  1.00 29.82           C  
-ATOM   1037  CZ  TYR A 137       5.131  91.205  46.099  1.00 27.30           C  
-ATOM   1038  OH  TYR A 137       5.590  92.473  45.816  1.00 30.83           O  
-ATOM   1039  N   THR A 138       6.561  86.075  46.389  1.00 20.97           N  
-ATOM   1040  CA  THR A 138       7.994  86.219  46.226  1.00 20.55           C  
-ATOM   1041  C   THR A 138       8.594  85.388  45.105  1.00 19.98           C  
-ATOM   1042  O   THR A 138       9.536  85.824  44.465  1.00 22.83           O  
-ATOM   1043  CB  THR A 138       8.658  85.913  47.603  1.00 23.61           C  
-ATOM   1044  OG1 THR A 138       8.013  86.675  48.628  1.00 26.10           O  
-ATOM   1045  CG2 THR A 138      10.153  86.255  47.751  1.00 24.64           C  
-ATOM   1046  N   GLU A 139       8.076  84.177  44.875  1.00 20.94           N  
-ATOM   1047  CA  GLU A 139       8.660  83.342  43.822  1.00 20.56           C  
-ATOM   1048  C   GLU A 139       7.784  83.199  42.580  1.00 24.47           C  
-ATOM   1049  O   GLU A 139       8.175  82.603  41.583  1.00 25.05           O  
-ATOM   1050  CB  GLU A 139       9.037  81.968  44.390  1.00 14.12           C  
-ATOM   1051  CG  GLU A 139      10.209  82.052  45.386  1.00 17.03           C  
-ATOM   1052  CD  GLU A 139      11.524  82.428  44.705  1.00 24.78           C  
-ATOM   1053  OE1 GLU A 139      11.720  82.081  43.540  1.00 26.19           O  
-ATOM   1054  OE2 GLU A 139      12.362  83.065  45.341  1.00 27.39           O  
-ATOM   1055  N   GLU A 140       6.575  83.751  42.655  1.00 25.50           N  
-ATOM   1056  CA  GLU A 140       5.678  83.684  41.516  1.00 25.77           C  
-ATOM   1057  C   GLU A 140       5.417  82.271  41.083  1.00 23.21           C  
-ATOM   1058  O   GLU A 140       5.790  81.845  40.001  1.00 24.20           O  
-ATOM   1059  CB  GLU A 140       6.182  84.550  40.358  1.00 31.13           C  
-ATOM   1060  CG  GLU A 140       6.341  86.013  40.826  1.00 42.92           C  
-ATOM   1061  CD  GLU A 140       7.014  86.896  39.795  1.00 46.01           C  
-ATOM   1062  OE1 GLU A 140       8.247  86.987  39.816  1.00 48.31           O  
-ATOM   1063  OE2 GLU A 140       6.300  87.494  38.988  1.00 48.93           O  
-ATOM   1064  N   VAL A 141       4.758  81.551  41.978  1.00 19.10           N  
-ATOM   1065  CA  VAL A 141       4.408  80.193  41.681  1.00 16.20           C  
-ATOM   1066  C   VAL A 141       2.971  80.098  42.117  1.00 17.91           C  
-ATOM   1067  O   VAL A 141       2.477  80.967  42.828  1.00 19.30           O  
-ATOM   1068  CB  VAL A 141       5.310  79.223  42.464  1.00 13.59           C  
-ATOM   1069  CG1 VAL A 141       6.789  79.545  42.267  1.00 14.93           C  
-ATOM   1070  CG2 VAL A 141       5.016  79.148  43.974  1.00 15.84           C  
-ATOM   1071  N   VAL A 142       2.297  79.049  41.667  1.00 19.99           N  
-ATOM   1072  CA  VAL A 142       0.929  78.836  42.099  1.00 21.84           C  
-ATOM   1073  C   VAL A 142       1.158  77.865  43.278  1.00 25.41           C  
-ATOM   1074  O   VAL A 142       1.933  76.905  43.156  1.00 28.57           O  
-ATOM   1075  CB  VAL A 142       0.102  78.239  40.935  1.00 16.98           C  
-ATOM   1076  CG1 VAL A 142      -1.294  77.780  41.354  1.00 13.15           C  
-ATOM   1077  CG2 VAL A 142      -0.015  79.247  39.779  1.00 14.31           C  
-ATOM   1078  N   LEU A 143       0.506  78.116  44.421  1.00 20.39           N  
-ATOM   1079  CA  LEU A 143       0.739  77.203  45.521  1.00 16.77           C  
-ATOM   1080  C   LEU A 143      -0.568  76.675  45.998  1.00 14.76           C  
-ATOM   1081  O   LEU A 143      -1.495  77.470  46.130  1.00 16.15           O  
-ATOM   1082  CB  LEU A 143       1.421  77.980  46.647  1.00 18.86           C  
-ATOM   1083  CG  LEU A 143       2.033  77.054  47.721  1.00 21.71           C  
-ATOM   1084  CD1 LEU A 143       3.315  77.673  48.226  1.00 23.56           C  
-ATOM   1085  CD2 LEU A 143       1.098  76.749  48.911  1.00 25.64           C  
-ATOM   1086  N   VAL A 144      -0.655  75.366  46.252  1.00 10.75           N  
-ATOM   1087  CA  VAL A 144      -1.919  74.860  46.755  1.00 14.28           C  
-ATOM   1088  C   VAL A 144      -1.633  74.090  48.043  1.00 17.51           C  
-ATOM   1089  O   VAL A 144      -0.498  73.691  48.307  1.00 17.97           O  
-ATOM   1090  CB  VAL A 144      -2.686  74.015  45.688  1.00 13.80           C  
-ATOM   1091  CG1 VAL A 144      -2.732  74.691  44.318  1.00 12.20           C  
-ATOM   1092  CG2 VAL A 144      -2.147  72.612  45.491  1.00 12.87           C  
-ATOM   1093  N   SER A 145      -2.688  73.863  48.838  1.00 18.01           N  
-ATOM   1094  CA  SER A 145      -2.565  73.094  50.077  1.00 16.75           C  
-ATOM   1095  C   SER A 145      -3.721  72.102  50.093  1.00 18.35           C  
-ATOM   1096  O   SER A 145      -4.841  72.534  49.830  1.00 21.33           O  
-ATOM   1097  CB  SER A 145      -2.752  73.997  51.294  1.00 14.17           C  
-ATOM   1098  OG  SER A 145      -1.903  75.113  51.205  1.00 15.89           O  
-ATOM   1099  N   LEU A 146      -3.436  70.823  50.382  1.00 16.79           N  
-ATOM   1100  CA  LEU A 146      -4.478  69.793  50.431  1.00 18.68           C  
-ATOM   1101  C   LEU A 146      -5.026  69.673  51.849  1.00 20.48           C  
-ATOM   1102  O   LEU A 146      -4.548  70.291  52.790  1.00 21.78           O  
-ATOM   1103  CB  LEU A 146      -3.892  68.376  50.129  1.00 16.79           C  
-ATOM   1104  CG  LEU A 146      -2.875  68.317  48.994  1.00 14.27           C  
-ATOM   1105  CD1 LEU A 146      -2.457  66.882  48.684  1.00 13.59           C  
-ATOM   1106  CD2 LEU A 146      -3.470  68.973  47.764  1.00 19.32           C  
-ATOM   1107  N   SER A 147      -6.012  68.801  51.976  1.00 19.32           N  
-ATOM   1108  CA  SER A 147      -6.625  68.454  53.232  1.00 18.72           C  
-ATOM   1109  C   SER A 147      -6.769  66.967  53.082  1.00 19.40           C  
-ATOM   1110  O   SER A 147      -6.957  66.501  51.965  1.00 22.27           O  
-ATOM   1111  CB  SER A 147      -8.036  69.035  53.378  1.00 20.89           C  
-ATOM   1112  OG  SER A 147      -7.956  70.444  53.544  1.00 37.06           O  
-ATOM   1113  N   TYR A 148      -6.666  66.195  54.149  1.00 17.63           N  
-ATOM   1114  CA  TYR A 148      -6.852  64.775  54.008  1.00 13.26           C  
-ATOM   1115  C   TYR A 148      -7.206  64.252  55.354  1.00 11.54           C  
-ATOM   1116  O   TYR A 148      -6.831  64.780  56.380  1.00 13.23           O  
-ATOM   1117  CB  TYR A 148      -5.637  64.082  53.421  1.00 14.40           C  
-ATOM   1118  CG  TYR A 148      -4.381  64.141  54.265  1.00  9.41           C  
-ATOM   1119  CD1 TYR A 148      -3.487  65.221  54.133  1.00 10.32           C  
-ATOM   1120  CD2 TYR A 148      -4.081  63.096  55.175  1.00 10.52           C  
-ATOM   1121  CE1 TYR A 148      -2.315  65.264  54.877  1.00 12.35           C  
-ATOM   1122  CE2 TYR A 148      -2.915  63.128  55.942  1.00  7.28           C  
-ATOM   1123  CZ  TYR A 148      -2.053  64.227  55.784  1.00  8.13           C  
-ATOM   1124  OH  TYR A 148      -0.947  64.277  56.571  1.00 10.17           O  
-ATOM   1125  N   ARG A 149      -7.992  63.207  55.347  1.00  8.06           N  
-ATOM   1126  CA  ARG A 149      -8.396  62.667  56.614  1.00  7.55           C  
-ATOM   1127  C   ARG A 149      -7.230  62.040  57.315  1.00 10.66           C  
-ATOM   1128  O   ARG A 149      -6.502  61.285  56.693  1.00 15.64           O  
-ATOM   1129  CB  ARG A 149      -9.464  61.634  56.327  1.00  2.81           C  
-ATOM   1130  CG  ARG A 149     -10.742  62.352  55.885  1.00  4.63           C  
-ATOM   1131  CD  ARG A 149     -11.813  61.344  55.529  1.00  7.73           C  
-ATOM   1132  NE  ARG A 149     -11.515  60.858  54.207  1.00  6.60           N  
-ATOM   1133  CZ  ARG A 149     -12.149  59.825  53.671  1.00  8.52           C  
-ATOM   1134  NH1 ARG A 149     -12.956  59.041  54.382  1.00  5.14           N  
-ATOM   1135  NH2 ARG A 149     -11.952  59.587  52.384  1.00 12.44           N  
-ATOM   1136  N   VAL A 150      -7.116  62.352  58.605  1.00 10.93           N  
-ATOM   1137  CA  VAL A 150      -6.094  61.871  59.496  1.00  9.40           C  
-ATOM   1138  C   VAL A 150      -6.789  60.995  60.528  1.00 11.21           C  
-ATOM   1139  O   VAL A 150      -8.006  60.908  60.612  1.00 10.42           O  
-ATOM   1140  CB  VAL A 150      -5.471  63.106  60.162  1.00  5.14           C  
-ATOM   1141  CG1 VAL A 150      -4.638  63.903  59.153  1.00  8.30           C  
-ATOM   1142  CG2 VAL A 150      -6.524  64.009  60.828  1.00  2.00           C  
-ATOM   1143  N   GLY A 151      -6.004  60.306  61.333  1.00  8.74           N  
-ATOM   1144  CA  GLY A 151      -6.612  59.499  62.367  1.00 13.27           C  
-ATOM   1145  C   GLY A 151      -7.414  58.318  61.874  1.00 13.43           C  
-ATOM   1146  O   GLY A 151      -7.234  57.777  60.799  1.00 18.94           O  
-ATOM   1147  N   ALA A 152      -8.338  57.913  62.734  1.00 15.81           N  
-ATOM   1148  CA  ALA A 152      -9.201  56.786  62.448  1.00 15.08           C  
-ATOM   1149  C   ALA A 152      -9.902  56.996  61.142  1.00 16.48           C  
-ATOM   1150  O   ALA A 152      -9.926  56.157  60.255  1.00 19.77           O  
-ATOM   1151  CB  ALA A 152     -10.277  56.644  63.557  1.00 16.38           C  
-ATOM   1152  N   PHE A 153     -10.456  58.201  61.068  1.00 16.47           N  
-ATOM   1153  CA  PHE A 153     -11.234  58.661  59.929  1.00 17.52           C  
-ATOM   1154  C   PHE A 153     -10.564  58.546  58.590  1.00 19.10           C  
-ATOM   1155  O   PHE A 153     -11.256  58.502  57.578  1.00 22.12           O  
-ATOM   1156  CB  PHE A 153     -11.598  60.141  60.079  1.00 17.58           C  
-ATOM   1157  CG  PHE A 153     -12.250  60.434  61.396  1.00 18.29           C  
-ATOM   1158  CD1 PHE A 153     -13.592  60.077  61.604  1.00 17.81           C  
-ATOM   1159  CD2 PHE A 153     -11.517  61.048  62.428  1.00 19.79           C  
-ATOM   1160  CE1 PHE A 153     -14.192  60.328  62.843  1.00 19.64           C  
-ATOM   1161  CE2 PHE A 153     -12.119  61.298  63.664  1.00 14.71           C  
-ATOM   1162  CZ  PHE A 153     -13.454  60.935  63.873  1.00 16.31           C  
-ATOM   1163  N   GLY A 154      -9.223  58.559  58.589  1.00 17.08           N  
-ATOM   1164  CA  GLY A 154      -8.510  58.461  57.335  1.00 13.20           C  
-ATOM   1165  C   GLY A 154      -7.645  57.226  57.227  1.00 16.76           C  
-ATOM   1166  O   GLY A 154      -7.200  56.899  56.126  1.00 21.42           O  
-ATOM   1167  N   PHE A 155      -7.410  56.495  58.332  1.00 10.13           N  
-ATOM   1168  CA  PHE A 155      -6.518  55.357  58.190  1.00  4.35           C  
-ATOM   1169  C   PHE A 155      -6.946  54.070  58.856  1.00  6.32           C  
-ATOM   1170  O   PHE A 155      -6.132  53.154  59.010  1.00  5.80           O  
-ATOM   1171  CB  PHE A 155      -5.110  55.781  58.600  1.00  2.53           C  
-ATOM   1172  CG  PHE A 155      -4.545  56.853  57.682  1.00  7.11           C  
-ATOM   1173  CD1 PHE A 155      -4.762  58.218  57.957  1.00  7.24           C  
-ATOM   1174  CD2 PHE A 155      -3.771  56.499  56.553  1.00  8.43           C  
-ATOM   1175  CE1 PHE A 155      -4.200  59.206  57.133  1.00  6.69           C  
-ATOM   1176  CE2 PHE A 155      -3.213  57.491  55.732  1.00  5.43           C  
-ATOM   1177  CZ  PHE A 155      -3.423  58.846  56.027  1.00  3.73           C  
-ATOM   1178  N   LEU A 156      -8.224  53.988  59.250  1.00  5.30           N  
-ATOM   1179  CA  LEU A 156      -8.702  52.738  59.857  1.00  8.53           C  
-ATOM   1180  C   LEU A 156      -8.566  51.683  58.777  1.00  8.36           C  
-ATOM   1181  O   LEU A 156      -8.850  51.994  57.634  1.00 10.64           O  
-ATOM   1182  CB  LEU A 156     -10.174  52.893  60.269  1.00 11.58           C  
-ATOM   1183  CG  LEU A 156     -10.789  51.648  60.921  1.00  9.96           C  
-ATOM   1184  CD1 LEU A 156     -10.048  51.273  62.201  1.00 13.48           C  
-ATOM   1185  CD2 LEU A 156     -12.269  51.889  61.218  1.00 11.63           C  
-ATOM   1186  N   ALA A 157      -8.180  50.451  59.089  1.00  8.96           N  
-ATOM   1187  CA  ALA A 157      -8.007  49.543  57.969  1.00  8.75           C  
-ATOM   1188  C   ALA A 157      -8.408  48.094  58.168  1.00 12.30           C  
-ATOM   1189  O   ALA A 157      -7.582  47.229  58.464  1.00  8.91           O  
-ATOM   1190  CB  ALA A 157      -6.513  49.552  57.612  1.00  8.11           C  
-ATOM   1191  N   LEU A 158      -9.694  47.818  57.925  1.00 15.41           N  
-ATOM   1192  CA  LEU A 158     -10.188  46.440  58.014  1.00 18.08           C  
-ATOM   1193  C   LEU A 158     -10.000  45.902  56.602  1.00 18.96           C  
-ATOM   1194  O   LEU A 158     -10.913  45.777  55.804  1.00 19.40           O  
-ATOM   1195  CB  LEU A 158     -11.651  46.445  58.445  1.00 16.34           C  
-ATOM   1196  CG  LEU A 158     -11.791  46.932  59.889  1.00 16.07           C  
-ATOM   1197  CD1 LEU A 158     -13.179  47.487  60.148  1.00 16.62           C  
-ATOM   1198  CD2 LEU A 158     -11.417  45.835  60.895  1.00 16.50           C  
-ATOM   1199  N   HIS A 159      -8.738  45.603  56.329  1.00 22.98           N  
-ATOM   1200  CA  HIS A 159      -8.257  45.148  55.040  1.00 30.84           C  
-ATOM   1201  C   HIS A 159      -9.211  44.578  54.011  1.00 34.01           C  
-ATOM   1202  O   HIS A 159      -9.410  45.223  52.986  1.00 40.62           O  
-ATOM   1203  CB  HIS A 159      -6.949  44.348  55.106  1.00 38.70           C  
-ATOM   1204  CG  HIS A 159      -6.384  44.161  53.698  1.00 45.22           C  
-ATOM   1205  ND1 HIS A 159      -6.542  45.038  52.670  1.00 47.49           N  
-ATOM   1206  CD2 HIS A 159      -5.646  43.062  53.201  1.00 48.81           C  
-ATOM   1207  CE1 HIS A 159      -5.920  44.506  51.599  1.00 48.99           C  
-ATOM   1208  NE2 HIS A 159      -5.375  43.317  51.906  1.00 48.28           N  
-ATOM   1209  N   GLY A 160      -9.753  43.384  54.212  1.00 32.34           N  
-ATOM   1210  CA  GLY A 160     -10.620  42.905  53.139  1.00 30.82           C  
-ATOM   1211  C   GLY A 160     -11.985  43.554  53.111  1.00 33.28           C  
-ATOM   1212  O   GLY A 160     -12.973  42.851  52.919  1.00 37.69           O  
-ATOM   1213  N   SER A 161     -12.084  44.860  53.310  1.00 32.25           N  
-ATOM   1214  CA  SER A 161     -13.387  45.468  53.317  1.00 33.51           C  
-ATOM   1215  C   SER A 161     -13.352  46.684  52.425  1.00 34.90           C  
-ATOM   1216  O   SER A 161     -12.417  47.471  52.363  1.00 39.21           O  
-ATOM   1217  CB  SER A 161     -13.697  45.914  54.752  1.00 31.18           C  
-ATOM   1218  OG  SER A 161     -15.002  46.512  54.807  1.00 36.26           O  
-ATOM   1219  N   GLN A 162     -14.531  46.811  51.795  1.00 35.80           N  
-ATOM   1220  CA  GLN A 162     -14.720  47.953  50.900  1.00 36.93           C  
-ATOM   1221  C   GLN A 162     -15.178  49.161  51.716  1.00 34.72           C  
-ATOM   1222  O   GLN A 162     -15.019  50.319  51.367  1.00 36.56           O  
-ATOM   1223  CB  GLN A 162     -15.836  47.628  49.860  1.00 39.31           C  
-ATOM   1224  CG  GLN A 162     -15.532  46.469  48.834  1.00 41.84           C  
-ATOM   1225  N   GLU A 163     -15.808  48.818  52.853  1.00 31.51           N  
-ATOM   1226  CA  GLU A 163     -16.312  49.886  53.716  1.00 26.96           C  
-ATOM   1227  C   GLU A 163     -15.213  50.641  54.439  1.00 23.35           C  
-ATOM   1228  O   GLU A 163     -15.340  51.820  54.704  1.00 26.46           O  
-ATOM   1229  CB  GLU A 163     -17.382  49.341  54.675  1.00 29.38           C  
-ATOM   1230  CG  GLU A 163     -18.573  48.666  53.964  1.00 23.59           C  
-ATOM   1231  CD  GLU A 163     -19.228  49.607  52.977  1.00 23.58           C  
-ATOM   1232  N   ALA A 164     -14.150  49.927  54.793  1.00 16.59           N  
-ATOM   1233  CA  ALA A 164     -13.012  50.549  55.458  1.00 15.06           C  
-ATOM   1234  C   ALA A 164     -11.768  49.786  54.980  1.00 16.71           C  
-ATOM   1235  O   ALA A 164     -11.191  48.965  55.698  1.00 20.04           O  
-ATOM   1236  CB  ALA A 164     -13.102  50.473  56.993  1.00  9.11           C  
-ATOM   1237  N   PRO A 165     -11.363  50.053  53.733  1.00 14.97           N  
-ATOM   1238  CA  PRO A 165     -10.059  49.592  53.279  1.00 13.44           C  
-ATOM   1239  C   PRO A 165      -9.125  50.605  53.898  1.00 16.94           C  
-ATOM   1240  O   PRO A 165      -9.521  51.684  54.341  1.00 23.84           O  
-ATOM   1241  CB  PRO A 165     -10.132  49.788  51.767  1.00 14.41           C  
-ATOM   1242  CG  PRO A 165     -11.148  50.929  51.544  1.00 13.25           C  
-ATOM   1243  CD  PRO A 165     -12.055  50.921  52.779  1.00 11.35           C  
-ATOM   1244  N   GLY A 166      -7.847  50.290  53.930  1.00 14.46           N  
-ATOM   1245  CA  GLY A 166      -7.054  51.348  54.567  1.00 15.06           C  
-ATOM   1246  C   GLY A 166      -6.750  52.485  53.617  1.00 10.60           C  
-ATOM   1247  O   GLY A 166      -7.401  52.732  52.616  1.00 14.05           O  
-ATOM   1248  N   ASN A 167      -5.690  53.192  53.974  1.00  6.94           N  
-ATOM   1249  CA  ASN A 167      -5.128  54.278  53.193  1.00  3.98           C  
-ATOM   1250  C   ASN A 167      -6.064  55.306  52.602  1.00  5.66           C  
-ATOM   1251  O   ASN A 167      -5.674  56.072  51.728  1.00  7.40           O  
-ATOM   1252  CB  ASN A 167      -4.268  53.663  52.087  1.00  2.00           C  
-ATOM   1253  CG  ASN A 167      -3.276  52.695  52.707  1.00  8.15           C  
-ATOM   1254  OD1 ASN A 167      -2.762  52.947  53.782  1.00 16.28           O  
-ATOM   1255  ND2 ASN A 167      -3.023  51.567  52.071  1.00  7.46           N  
-ATOM   1256  N   VAL A 168      -7.279  55.390  53.110  1.00  6.08           N  
-ATOM   1257  CA  VAL A 168      -8.209  56.344  52.551  1.00  8.29           C  
-ATOM   1258  C   VAL A 168      -7.717  57.784  52.574  1.00 10.31           C  
-ATOM   1259  O   VAL A 168      -7.963  58.584  51.681  1.00 17.23           O  
-ATOM   1260  CB  VAL A 168      -9.541  56.083  53.259  1.00  9.91           C  
-ATOM   1261  CG1 VAL A 168     -10.541  57.207  53.160  1.00  7.10           C  
-ATOM   1262  CG2 VAL A 168     -10.166  54.775  52.740  1.00 11.93           C  
-ATOM   1263  N   GLY A 169      -6.979  58.137  53.601  1.00 14.57           N  
-ATOM   1264  CA  GLY A 169      -6.485  59.514  53.652  1.00 13.64           C  
-ATOM   1265  C   GLY A 169      -5.486  59.788  52.558  1.00 11.80           C  
-ATOM   1266  O   GLY A 169      -5.331  60.897  52.058  1.00 12.92           O  
-ATOM   1267  N   LEU A 170      -4.818  58.707  52.181  1.00  8.00           N  
-ATOM   1268  CA  LEU A 170      -3.813  58.722  51.151  1.00  8.15           C  
-ATOM   1269  C   LEU A 170      -4.537  58.945  49.820  1.00 10.89           C  
-ATOM   1270  O   LEU A 170      -4.164  59.742  48.956  1.00 10.83           O  
-ATOM   1271  CB  LEU A 170      -3.015  57.415  51.312  1.00  5.68           C  
-ATOM   1272  CG  LEU A 170      -1.491  57.557  51.374  1.00  3.76           C  
-ATOM   1273  CD1 LEU A 170      -0.946  58.687  52.256  1.00  4.84           C  
-ATOM   1274  CD2 LEU A 170      -0.888  56.218  51.803  1.00  3.40           C  
-ATOM   1275  N   LEU A 171      -5.679  58.255  49.700  1.00 12.59           N  
-ATOM   1276  CA  LEU A 171      -6.450  58.469  48.466  1.00 13.94           C  
-ATOM   1277  C   LEU A 171      -6.950  59.916  48.384  1.00 16.31           C  
-ATOM   1278  O   LEU A 171      -6.981  60.529  47.327  1.00 22.51           O  
-ATOM   1279  CB  LEU A 171      -7.633  57.509  48.325  1.00  6.31           C  
-ATOM   1280  CG  LEU A 171      -7.182  56.046  48.320  1.00  4.35           C  
-ATOM   1281  CD1 LEU A 171      -8.382  55.107  48.295  1.00 10.78           C  
-ATOM   1282  CD2 LEU A 171      -6.277  55.739  47.141  1.00  7.49           C  
-ATOM   1283  N   ASP A 172      -7.333  60.493  49.524  1.00 15.07           N  
-ATOM   1284  CA  ASP A 172      -7.785  61.875  49.442  1.00 14.35           C  
-ATOM   1285  C   ASP A 172      -6.727  62.773  48.866  1.00 15.63           C  
-ATOM   1286  O   ASP A 172      -7.038  63.722  48.161  1.00 18.63           O  
-ATOM   1287  CB  ASP A 172      -8.118  62.497  50.799  1.00 18.99           C  
-ATOM   1288  CG  ASP A 172      -9.113  61.733  51.635  1.00 24.06           C  
-ATOM   1289  OD1 ASP A 172      -9.846  60.915  51.094  1.00 26.06           O  
-ATOM   1290  OD2 ASP A 172      -9.144  61.963  52.839  1.00 30.47           O  
-ATOM   1291  N   GLN A 173      -5.463  62.456  49.191  1.00 15.38           N  
-ATOM   1292  CA  GLN A 173      -4.376  63.289  48.687  1.00 13.29           C  
-ATOM   1293  C   GLN A 173      -4.322  63.187  47.198  1.00 13.91           C  
-ATOM   1294  O   GLN A 173      -4.220  64.154  46.457  1.00 14.44           O  
-ATOM   1295  CB  GLN A 173      -3.008  62.871  49.249  1.00 10.88           C  
-ATOM   1296  CG  GLN A 173      -2.957  62.897  50.779  1.00 12.69           C  
-ATOM   1297  CD  GLN A 173      -1.554  62.665  51.307  1.00 12.03           C  
-ATOM   1298  OE1 GLN A 173      -0.559  62.832  50.633  1.00  8.80           O  
-ATOM   1299  NE2 GLN A 173      -1.480  62.303  52.567  1.00 17.30           N  
-ATOM   1300  N   ARG A 174      -4.424  61.930  46.775  1.00 14.81           N  
-ATOM   1301  CA  ARG A 174      -4.386  61.661  45.346  1.00 13.15           C  
-ATOM   1302  C   ARG A 174      -5.470  62.412  44.626  1.00 11.65           C  
-ATOM   1303  O   ARG A 174      -5.216  63.072  43.635  1.00 14.76           O  
-ATOM   1304  CB  ARG A 174      -4.520  60.167  45.099  1.00 10.52           C  
-ATOM   1305  CG  ARG A 174      -4.373  59.751  43.646  1.00  7.57           C  
-ATOM   1306  CD  ARG A 174      -4.632  58.244  43.505  1.00 15.22           C  
-ATOM   1307  NE  ARG A 174      -3.503  57.506  44.014  1.00 12.35           N  
-ATOM   1308  CZ  ARG A 174      -3.431  56.166  44.057  1.00 16.56           C  
-ATOM   1309  NH1 ARG A 174      -4.500  55.388  43.885  1.00 13.82           N  
-ATOM   1310  NH2 ARG A 174      -2.258  55.603  44.296  1.00 15.94           N  
-ATOM   1311  N   MET A 175      -6.692  62.313  45.140  1.00  9.23           N  
-ATOM   1312  CA  MET A 175      -7.790  63.018  44.507  1.00  9.52           C  
-ATOM   1313  C   MET A 175      -7.516  64.506  44.372  1.00 11.08           C  
-ATOM   1314  O   MET A 175      -7.845  65.149  43.384  1.00 14.83           O  
-ATOM   1315  CB  MET A 175      -9.079  62.809  45.275  1.00 12.36           C  
-ATOM   1316  CG  MET A 175     -10.280  63.432  44.559  1.00 17.99           C  
-ATOM   1317  SD  MET A 175     -11.671  62.302  44.755  1.00 26.77           S  
-ATOM   1318  CE  MET A 175     -11.147  61.180  43.418  1.00 23.60           C  
-ATOM   1319  N   ALA A 176      -6.883  65.076  45.383  1.00 13.80           N  
-ATOM   1320  CA  ALA A 176      -6.607  66.488  45.224  1.00 12.57           C  
-ATOM   1321  C   ALA A 176      -5.559  66.667  44.156  1.00 11.01           C  
-ATOM   1322  O   ALA A 176      -5.618  67.616  43.404  1.00 14.19           O  
-ATOM   1323  CB  ALA A 176      -6.152  67.113  46.519  1.00 15.81           C  
-ATOM   1324  N   LEU A 177      -4.603  65.740  44.080  1.00 12.40           N  
-ATOM   1325  CA  LEU A 177      -3.565  65.816  43.039  1.00 15.13           C  
-ATOM   1326  C   LEU A 177      -4.202  65.733  41.646  1.00 17.24           C  
-ATOM   1327  O   LEU A 177      -3.788  66.347  40.668  1.00 19.47           O  
-ATOM   1328  CB  LEU A 177      -2.537  64.662  43.180  1.00 13.77           C  
-ATOM   1329  CG  LEU A 177      -1.163  64.996  43.810  1.00  9.51           C  
-ATOM   1330  CD1 LEU A 177      -1.056  66.379  44.458  1.00  2.74           C  
-ATOM   1331  CD2 LEU A 177      -0.756  63.887  44.783  1.00  8.15           C  
-ATOM   1332  N   GLN A 178      -5.261  64.929  41.573  1.00 17.82           N  
-ATOM   1333  CA  GLN A 178      -5.959  64.804  40.312  1.00 14.51           C  
-ATOM   1334  C   GLN A 178      -6.584  66.124  39.954  1.00 13.43           C  
-ATOM   1335  O   GLN A 178      -6.358  66.654  38.885  1.00 21.47           O  
-ATOM   1336  CB  GLN A 178      -7.046  63.733  40.379  1.00 10.61           C  
-ATOM   1337  CG  GLN A 178      -7.709  63.438  39.027  1.00 18.80           C  
-ATOM   1338  CD  GLN A 178      -6.842  62.486  38.228  1.00 21.16           C  
-ATOM   1339  OE1 GLN A 178      -6.622  61.349  38.610  1.00 25.52           O  
-ATOM   1340  NE2 GLN A 178      -6.331  62.966  37.106  1.00 22.73           N  
-ATOM   1341  N   TRP A 179      -7.383  66.675  40.850  1.00 10.74           N  
-ATOM   1342  CA  TRP A 179      -8.034  67.945  40.549  1.00 10.13           C  
-ATOM   1343  C   TRP A 179      -7.021  68.996  40.155  1.00 12.00           C  
-ATOM   1344  O   TRP A 179      -7.252  69.795  39.264  1.00 19.76           O  
-ATOM   1345  CB  TRP A 179      -8.838  68.399  41.776  1.00 10.49           C  
-ATOM   1346  CG  TRP A 179      -9.853  69.491  41.510  1.00  6.08           C  
-ATOM   1347  CD1 TRP A 179     -11.250  69.295  41.381  1.00  9.25           C  
-ATOM   1348  CD2 TRP A 179      -9.633  70.880  41.419  1.00  4.45           C  
-ATOM   1349  NE1 TRP A 179     -11.899  70.487  41.223  1.00  8.77           N  
-ATOM   1350  CE2 TRP A 179     -10.977  71.493  41.236  1.00  2.68           C  
-ATOM   1351  CE3 TRP A 179      -8.500  71.697  41.465  1.00  2.00           C  
-ATOM   1352  CZ2 TRP A 179     -11.100  72.872  41.112  1.00  2.18           C  
-ATOM   1353  CZ3 TRP A 179      -8.663  73.088  41.336  1.00  2.57           C  
-ATOM   1354  CH2 TRP A 179      -9.937  73.663  41.165  1.00  2.00           C  
-ATOM   1355  N   VAL A 180      -5.873  69.006  40.810  1.00 11.87           N  
-ATOM   1356  CA  VAL A 180      -4.876  70.004  40.443  1.00 11.64           C  
-ATOM   1357  C   VAL A 180      -4.423  69.780  39.005  1.00 14.32           C  
-ATOM   1358  O   VAL A 180      -4.296  70.711  38.218  1.00 14.72           O  
-ATOM   1359  CB  VAL A 180      -3.729  69.940  41.459  1.00  5.95           C  
-ATOM   1360  CG1 VAL A 180      -2.492  70.774  41.089  1.00  7.08           C  
-ATOM   1361  CG2 VAL A 180      -4.286  70.381  42.817  1.00  9.69           C  
-ATOM   1362  N   HIS A 181      -4.209  68.510  38.675  1.00 15.12           N  
-ATOM   1363  CA  HIS A 181      -3.773  68.124  37.336  1.00 17.44           C  
-ATOM   1364  C   HIS A 181      -4.755  68.548  36.260  1.00 17.59           C  
-ATOM   1365  O   HIS A 181      -4.426  69.055  35.200  1.00 21.94           O  
-ATOM   1366  CB  HIS A 181      -3.624  66.595  37.336  1.00 19.59           C  
-ATOM   1367  CG  HIS A 181      -3.014  66.035  36.074  1.00 25.78           C  
-ATOM   1368  ND1 HIS A 181      -3.709  65.319  35.169  1.00 24.30           N  
-ATOM   1369  CD2 HIS A 181      -1.650  66.070  35.680  1.00 30.09           C  
-ATOM   1370  CE1 HIS A 181      -2.819  64.901  34.257  1.00 31.34           C  
-ATOM   1371  NE2 HIS A 181      -1.573  65.342  34.544  1.00 35.14           N  
-ATOM   1372  N   ASP A 182      -6.016  68.345  36.586  1.00 16.68           N  
-ATOM   1373  CA  ASP A 182      -7.076  68.676  35.656  1.00 17.41           C  
-ATOM   1374  C   ASP A 182      -7.573  70.110  35.729  1.00 19.32           C  
-ATOM   1375  O   ASP A 182      -8.522  70.425  35.029  1.00 25.05           O  
-ATOM   1376  CB  ASP A 182      -8.311  67.791  35.923  1.00 16.95           C  
-ATOM   1377  CG  ASP A 182      -8.047  66.296  35.756  1.00 24.00           C  
-ATOM   1378  OD1 ASP A 182      -7.010  65.927  35.196  1.00 26.34           O  
-ATOM   1379  OD2 ASP A 182      -8.894  65.503  36.173  1.00 23.74           O  
-ATOM   1380  N   ASN A 183      -7.035  70.994  36.574  1.00 14.46           N  
-ATOM   1381  CA  ASN A 183      -7.651  72.321  36.518  1.00  9.77           C  
-ATOM   1382  C   ASN A 183      -6.696  73.420  36.867  1.00 14.26           C  
-ATOM   1383  O   ASN A 183      -7.050  74.589  36.787  1.00 14.61           O  
-ATOM   1384  CB  ASN A 183      -8.816  72.502  37.490  1.00  7.86           C  
-ATOM   1385  CG  ASN A 183      -9.939  71.512  37.343  1.00 13.76           C  
-ATOM   1386  OD1 ASN A 183     -11.011  71.777  36.814  1.00 20.88           O  
-ATOM   1387  ND2 ASN A 183      -9.696  70.337  37.881  1.00 19.16           N  
-ATOM   1388  N   ILE A 184      -5.451  73.094  37.220  1.00 15.04           N  
-ATOM   1389  CA  ILE A 184      -4.580  74.188  37.591  1.00 15.27           C  
-ATOM   1390  C   ILE A 184      -4.324  75.187  36.459  1.00 20.74           C  
-ATOM   1391  O   ILE A 184      -4.015  76.361  36.670  1.00 24.30           O  
-ATOM   1392  CB  ILE A 184      -3.371  73.644  38.359  1.00 12.84           C  
-ATOM   1393  CG1 ILE A 184      -2.721  74.747  39.222  1.00 14.79           C  
-ATOM   1394  CG2 ILE A 184      -2.389  72.882  37.477  1.00 10.86           C  
-ATOM   1395  CD1 ILE A 184      -3.634  75.214  40.373  1.00 14.42           C  
-ATOM   1396  N   GLN A 185      -4.498  74.683  35.222  1.00 21.09           N  
-ATOM   1397  CA  GLN A 185      -4.327  75.498  34.020  1.00 18.39           C  
-ATOM   1398  C   GLN A 185      -5.223  76.718  34.082  1.00 18.63           C  
-ATOM   1399  O   GLN A 185      -4.812  77.806  33.720  1.00 20.92           O  
-ATOM   1400  CB  GLN A 185      -4.637  74.678  32.746  1.00 15.12           C  
-ATOM   1401  CG  GLN A 185      -5.989  73.945  32.830  1.00 19.60           C  
-ATOM   1402  CD  GLN A 185      -6.305  73.169  31.586  1.00 19.46           C  
-ATOM   1403  OE1 GLN A 185      -6.282  71.952  31.557  1.00 24.41           O  
-ATOM   1404  NE2 GLN A 185      -6.625  73.910  30.555  1.00 19.15           N  
-ATOM   1405  N   PHE A 186      -6.446  76.544  34.602  1.00 13.62           N  
-ATOM   1406  CA  PHE A 186      -7.335  77.705  34.653  1.00 15.96           C  
-ATOM   1407  C   PHE A 186      -6.889  78.759  35.633  1.00 16.69           C  
-ATOM   1408  O   PHE A 186      -7.435  79.855  35.684  1.00 18.51           O  
-ATOM   1409  CB  PHE A 186      -8.799  77.332  34.931  1.00 18.39           C  
-ATOM   1410  CG  PHE A 186      -9.188  76.212  34.006  1.00 23.70           C  
-ATOM   1411  CD1 PHE A 186      -9.287  76.437  32.624  1.00 23.43           C  
-ATOM   1412  CD2 PHE A 186      -9.383  74.923  34.514  1.00 26.04           C  
-ATOM   1413  CE1 PHE A 186      -9.560  75.372  31.761  1.00 22.42           C  
-ATOM   1414  CE2 PHE A 186      -9.654  73.861  33.652  1.00 23.14           C  
-ATOM   1415  CZ  PHE A 186      -9.738  74.083  32.274  1.00 23.73           C  
-ATOM   1416  N   PHE A 187      -5.879  78.411  36.429  1.00 15.55           N  
-ATOM   1417  CA  PHE A 187      -5.357  79.346  37.407  1.00 14.10           C  
-ATOM   1418  C   PHE A 187      -3.978  79.810  36.991  1.00 13.32           C  
-ATOM   1419  O   PHE A 187      -3.339  80.559  37.714  1.00 19.48           O  
-ATOM   1420  CB  PHE A 187      -5.288  78.723  38.811  1.00  9.50           C  
-ATOM   1421  CG  PHE A 187      -6.641  78.300  39.334  1.00  4.66           C  
-ATOM   1422  CD1 PHE A 187      -7.440  79.189  40.061  1.00  6.69           C  
-ATOM   1423  CD2 PHE A 187      -7.114  76.999  39.104  1.00  6.80           C  
-ATOM   1424  CE1 PHE A 187      -8.689  78.783  40.557  1.00  6.63           C  
-ATOM   1425  CE2 PHE A 187      -8.361  76.586  39.595  1.00  5.03           C  
-ATOM   1426  CZ  PHE A 187      -9.154  77.480  40.325  1.00  3.61           C  
-ATOM   1427  N   GLY A 188      -3.499  79.342  35.845  1.00  8.19           N  
-ATOM   1428  CA  GLY A 188      -2.186  79.785  35.402  1.00  4.82           C  
-ATOM   1429  C   GLY A 188      -1.104  78.791  35.711  1.00  8.15           C  
-ATOM   1430  O   GLY A 188       0.080  79.026  35.509  1.00  9.97           O  
-ATOM   1431  N   GLY A 189      -1.481  77.614  36.203  1.00  8.79           N  
-ATOM   1432  CA  GLY A 189      -0.411  76.673  36.528  1.00 13.76           C  
-ATOM   1433  C   GLY A 189      -0.188  75.661  35.446  1.00 16.62           C  
-ATOM   1434  O   GLY A 189      -1.086  75.289  34.711  1.00 22.62           O  
-ATOM   1435  N   ASP A 190       1.039  75.177  35.352  1.00 15.07           N  
-ATOM   1436  CA  ASP A 190       1.391  74.193  34.349  1.00 13.98           C  
-ATOM   1437  C   ASP A 190       1.259  72.804  34.955  1.00 12.79           C  
-ATOM   1438  O   ASP A 190       2.108  72.434  35.749  1.00 11.02           O  
-ATOM   1439  CB  ASP A 190       2.866  74.426  33.998  1.00 15.65           C  
-ATOM   1440  CG  ASP A 190       3.469  73.435  33.006  1.00 23.99           C  
-ATOM   1441  OD1 ASP A 190       2.841  72.443  32.626  1.00 21.26           O  
-ATOM   1442  OD2 ASP A 190       4.602  73.669  32.608  1.00 34.62           O  
-ATOM   1443  N   PRO A 191       0.259  71.998  34.566  1.00 12.68           N  
-ATOM   1444  CA  PRO A 191       0.122  70.660  35.150  1.00 16.22           C  
-ATOM   1445  C   PRO A 191       1.292  69.707  34.980  1.00 19.00           C  
-ATOM   1446  O   PRO A 191       1.365  68.673  35.628  1.00 22.85           O  
-ATOM   1447  CB  PRO A 191      -1.149  70.073  34.529  1.00 15.20           C  
-ATOM   1448  CG  PRO A 191      -1.519  71.005  33.364  1.00 13.76           C  
-ATOM   1449  CD  PRO A 191      -0.786  72.335  33.612  1.00 11.62           C  
-ATOM   1450  N   LYS A 192       2.204  70.064  34.084  1.00 21.61           N  
-ATOM   1451  CA  LYS A 192       3.363  69.217  33.860  1.00 28.35           C  
-ATOM   1452  C   LYS A 192       4.542  69.661  34.684  1.00 27.64           C  
-ATOM   1453  O   LYS A 192       5.659  69.192  34.486  1.00 23.51           O  
-ATOM   1454  CB  LYS A 192       3.752  69.154  32.373  1.00 35.92           C  
-ATOM   1455  CG  LYS A 192       2.560  68.817  31.450  1.00 47.01           C  
-ATOM   1456  CD  LYS A 192       1.747  67.549  31.847  1.00 52.79           C  
-ATOM   1457  CE  LYS A 192       0.462  67.361  31.003  1.00 57.95           C  
-ATOM   1458  NZ  LYS A 192      -0.422  66.361  31.583  1.00 62.00           N  
-ATOM   1459  N   THR A 193       4.303  70.605  35.598  1.00 29.06           N  
-ATOM   1460  CA  THR A 193       5.398  71.065  36.445  1.00 31.46           C  
-ATOM   1461  C   THR A 193       4.927  71.348  37.860  1.00 28.81           C  
-ATOM   1462  O   THR A 193       5.159  72.434  38.382  1.00 30.32           O  
-ATOM   1463  CB  THR A 193       6.157  72.253  35.831  1.00 31.79           C  
-ATOM   1464  OG1 THR A 193       6.252  72.054  34.417  1.00 35.69           O  
-ATOM   1465  CG2 THR A 193       7.596  72.396  36.364  1.00 33.07           C  
-ATOM   1466  N   VAL A 194       4.224  70.353  38.450  1.00 27.55           N  
-ATOM   1467  CA  VAL A 194       3.775  70.498  39.821  1.00 23.61           C  
-ATOM   1468  C   VAL A 194       4.735  69.675  40.659  1.00 23.20           C  
-ATOM   1469  O   VAL A 194       5.070  68.553  40.286  1.00 21.51           O  
-ATOM   1470  CB  VAL A 194       2.301  70.058  40.037  1.00 18.62           C  
-ATOM   1471  CG1 VAL A 194       1.364  70.532  38.913  1.00 23.81           C  
-ATOM   1472  CG2 VAL A 194       2.127  68.549  40.147  1.00 18.56           C  
-ATOM   1473  N   THR A 195       5.167  70.242  41.773  1.00 24.74           N  
-ATOM   1474  CA  THR A 195       6.053  69.596  42.723  1.00 24.42           C  
-ATOM   1475  C   THR A 195       5.240  69.404  44.033  1.00 21.50           C  
-ATOM   1476  O   THR A 195       4.592  70.330  44.517  1.00 23.06           O  
-ATOM   1477  CB  THR A 195       7.246  70.554  42.929  1.00 25.90           C  
-ATOM   1478  OG1 THR A 195       7.944  70.758  41.698  1.00 26.70           O  
-ATOM   1479  CG2 THR A 195       8.274  70.117  43.978  1.00 23.91           C  
-ATOM   1480  N   ILE A 196       5.234  68.191  44.586  1.00 17.85           N  
-ATOM   1481  CA  ILE A 196       4.520  68.008  45.837  1.00 13.44           C  
-ATOM   1482  C   ILE A 196       5.592  68.167  46.934  1.00 17.35           C  
-ATOM   1483  O   ILE A 196       6.678  67.597  46.804  1.00 19.81           O  
-ATOM   1484  CB  ILE A 196       3.856  66.618  45.882  1.00  4.26           C  
-ATOM   1485  CG1 ILE A 196       4.785  65.463  45.468  1.00  2.00           C  
-ATOM   1486  CG2 ILE A 196       2.594  66.612  45.039  1.00  3.52           C  
-ATOM   1487  CD1 ILE A 196       4.190  64.075  45.727  1.00  2.00           C  
-ATOM   1488  N   PHE A 197       5.316  68.960  47.982  1.00 16.41           N  
-ATOM   1489  CA  PHE A 197       6.277  69.120  49.077  1.00 15.70           C  
-ATOM   1490  C   PHE A 197       5.505  68.817  50.347  1.00 16.69           C  
-ATOM   1491  O   PHE A 197       4.294  68.990  50.354  1.00 20.30           O  
-ATOM   1492  CB  PHE A 197       7.093  70.444  49.051  1.00 14.78           C  
-ATOM   1493  CG  PHE A 197       6.459  71.814  49.265  1.00 11.75           C  
-ATOM   1494  CD1 PHE A 197       5.179  72.144  48.782  1.00  8.99           C  
-ATOM   1495  CD2 PHE A 197       7.204  72.808  49.944  1.00  6.26           C  
-ATOM   1496  CE1 PHE A 197       4.653  73.437  48.985  1.00  9.05           C  
-ATOM   1497  CE2 PHE A 197       6.683  74.095  50.142  1.00  5.01           C  
-ATOM   1498  CZ  PHE A 197       5.400  74.412  49.668  1.00  4.37           C  
-ATOM   1499  N   GLY A 198       6.169  68.335  51.407  1.00 17.51           N  
-ATOM   1500  CA  GLY A 198       5.440  68.026  52.652  1.00 14.35           C  
-ATOM   1501  C   GLY A 198       6.441  67.752  53.757  1.00 12.67           C  
-ATOM   1502  O   GLY A 198       7.595  67.431  53.481  1.00  7.51           O  
-ATOM   1503  N   GLU A 199       6.002  67.858  55.024  1.00 13.87           N  
-ATOM   1504  CA  GLU A 199       6.901  67.638  56.174  1.00 11.81           C  
-ATOM   1505  C   GLU A 199       6.361  66.609  57.156  1.00 12.20           C  
-ATOM   1506  O   GLU A 199       5.153  66.503  57.326  1.00 13.40           O  
-ATOM   1507  CB  GLU A 199       7.090  68.986  56.878  1.00 11.00           C  
-ATOM   1508  CG  GLU A 199       8.063  69.009  58.069  1.00 16.00           C  
-ATOM   1509  CD  GLU A 199       7.362  68.769  59.401  1.00 15.20           C  
-ATOM   1510  OE1 GLU A 199       6.154  68.632  59.412  1.00 17.52           O  
-ATOM   1511  OE2 GLU A 199       8.012  68.711  60.431  1.00 11.72           O  
-ATOM   1512  N   SER A 200       7.242  65.857  57.833  1.00 11.87           N  
-ATOM   1513  CA  SER A 200       6.778  64.855  58.793  1.00 12.54           C  
-ATOM   1514  C   SER A 200       5.938  63.860  58.001  1.00 12.69           C  
-ATOM   1515  O   SER A 200       6.403  63.292  57.025  1.00 15.40           O  
-ATOM   1516  CB  SER A 200       6.151  65.519  60.050  1.00 13.30           C  
-ATOM   1517  OG  SER A 200       5.634  64.653  61.093  1.00 21.59           O  
-ATOM   1518  N   ALA A 201       4.675  63.680  58.393  1.00 11.48           N  
-ATOM   1519  CA  ALA A 201       3.821  62.741  57.676  1.00 10.52           C  
-ATOM   1520  C   ALA A 201       3.596  63.203  56.250  1.00 13.66           C  
-ATOM   1521  O   ALA A 201       3.349  62.402  55.369  1.00 17.28           O  
-ATOM   1522  CB  ALA A 201       2.477  62.545  58.374  1.00 10.33           C  
-ATOM   1523  N   GLY A 202       3.704  64.518  56.030  1.00 12.24           N  
-ATOM   1524  CA  GLY A 202       3.539  65.025  54.675  1.00 12.84           C  
-ATOM   1525  C   GLY A 202       4.710  64.547  53.834  1.00 14.34           C  
-ATOM   1526  O   GLY A 202       4.568  64.000  52.754  1.00 18.23           O  
-ATOM   1527  N   GLY A 203       5.918  64.706  54.373  1.00  9.95           N  
-ATOM   1528  CA  GLY A 203       7.081  64.248  53.628  1.00  6.16           C  
-ATOM   1529  C   GLY A 203       7.043  62.740  53.414  1.00  3.97           C  
-ATOM   1530  O   GLY A 203       7.506  62.188  52.429  1.00  7.91           O  
-ATOM   1531  N   ALA A 204       6.469  62.029  54.374  1.00  4.18           N  
-ATOM   1532  CA  ALA A 204       6.396  60.587  54.173  1.00  5.94           C  
-ATOM   1533  C   ALA A 204       5.338  60.269  53.101  1.00  6.82           C  
-ATOM   1534  O   ALA A 204       5.487  59.338  52.319  1.00 10.15           O  
-ATOM   1535  CB  ALA A 204       6.106  59.837  55.485  1.00  4.71           C  
-ATOM   1536  N   SER A 205       4.261  61.055  53.073  1.00  5.33           N  
-ATOM   1537  CA  SER A 205       3.218  60.858  52.077  1.00  5.86           C  
-ATOM   1538  C   SER A 205       3.780  61.076  50.653  1.00  8.20           C  
-ATOM   1539  O   SER A 205       3.547  60.320  49.715  1.00  8.05           O  
-ATOM   1540  CB  SER A 205       2.075  61.857  52.346  1.00  7.72           C  
-ATOM   1541  OG  SER A 205       1.365  61.451  53.513  1.00  5.90           O  
-ATOM   1542  N   VAL A 206       4.566  62.146  50.515  1.00  6.12           N  
-ATOM   1543  CA  VAL A 206       5.196  62.469  49.256  1.00  2.00           C  
-ATOM   1544  C   VAL A 206       5.972  61.252  48.764  1.00  3.78           C  
-ATOM   1545  O   VAL A 206       5.787  60.752  47.665  1.00 11.42           O  
-ATOM   1546  CB  VAL A 206       6.055  63.713  49.507  1.00  2.00           C  
-ATOM   1547  CG1 VAL A 206       7.097  63.956  48.444  1.00  2.00           C  
-ATOM   1548  CG2 VAL A 206       5.182  64.976  49.697  1.00  2.00           C  
-ATOM   1549  N   GLY A 207       6.842  60.733  49.604  1.00  4.92           N  
-ATOM   1550  CA  GLY A 207       7.560  59.553  49.153  1.00  5.92           C  
-ATOM   1551  C   GLY A 207       6.625  58.386  48.855  1.00  8.28           C  
-ATOM   1552  O   GLY A 207       6.941  57.511  48.058  1.00 10.84           O  
-ATOM   1553  N   MET A 208       5.454  58.370  49.497  1.00  7.20           N  
-ATOM   1554  CA  MET A 208       4.528  57.283  49.206  1.00 13.02           C  
-ATOM   1555  C   MET A 208       3.913  57.475  47.828  1.00 14.81           C  
-ATOM   1556  O   MET A 208       3.509  56.511  47.199  1.00 18.28           O  
-ATOM   1557  CB  MET A 208       3.466  57.097  50.302  1.00 12.68           C  
-ATOM   1558  CG  MET A 208       4.136  56.577  51.591  1.00 17.91           C  
-ATOM   1559  SD  MET A 208       3.052  56.711  53.030  1.00 20.21           S  
-ATOM   1560  CE  MET A 208       3.906  55.526  54.098  1.00 20.24           C  
-ATOM   1561  N   HIS A 209       3.848  58.718  47.340  1.00 14.66           N  
-ATOM   1562  CA  HIS A 209       3.291  58.947  45.996  1.00 11.19           C  
-ATOM   1563  C   HIS A 209       4.358  58.572  44.978  1.00 11.42           C  
-ATOM   1564  O   HIS A 209       4.084  58.017  43.928  1.00 14.54           O  
-ATOM   1565  CB  HIS A 209       2.747  60.365  45.814  1.00  5.09           C  
-ATOM   1566  CG  HIS A 209       1.485  60.551  46.643  1.00 10.19           C  
-ATOM   1567  ND1 HIS A 209       1.229  61.615  47.439  1.00  6.95           N  
-ATOM   1568  CD2 HIS A 209       0.350  59.703  46.712  1.00 11.14           C  
-ATOM   1569  CE1 HIS A 209      -0.001  61.438  47.940  1.00  5.74           C  
-ATOM   1570  NE2 HIS A 209      -0.557  60.293  47.518  1.00  9.38           N  
-ATOM   1571  N   ILE A 210       5.610  58.860  45.305  1.00  6.53           N  
-ATOM   1572  CA  ILE A 210       6.673  58.440  44.411  1.00  3.94           C  
-ATOM   1573  C   ILE A 210       6.668  56.913  44.266  1.00  5.37           C  
-ATOM   1574  O   ILE A 210       7.180  56.400  43.284  1.00  6.16           O  
-ATOM   1575  CB  ILE A 210       8.032  58.884  45.019  1.00  2.00           C  
-ATOM   1576  CG1 ILE A 210       8.188  60.403  44.963  1.00  2.00           C  
-ATOM   1577  CG2 ILE A 210       9.267  58.176  44.438  1.00  2.00           C  
-ATOM   1578  CD1 ILE A 210       9.641  60.860  45.130  1.00  2.00           C  
-ATOM   1579  N   LEU A 211       6.136  56.196  45.270  1.00  9.23           N  
-ATOM   1580  CA  LEU A 211       6.130  54.723  45.227  1.00 11.06           C  
-ATOM   1581  C   LEU A 211       4.860  54.134  44.636  1.00 10.95           C  
-ATOM   1582  O   LEU A 211       4.847  53.175  43.886  1.00 11.23           O  
-ATOM   1583  CB  LEU A 211       6.248  54.128  46.660  1.00 12.80           C  
-ATOM   1584  CG  LEU A 211       7.587  54.369  47.402  1.00 13.52           C  
-ATOM   1585  CD1 LEU A 211       7.445  54.183  48.916  1.00 17.51           C  
-ATOM   1586  CD2 LEU A 211       8.665  53.413  46.916  1.00 12.10           C  
-ATOM   1587  N   SER A 212       3.736  54.704  45.013  1.00 14.70           N  
-ATOM   1588  CA  SER A 212       2.476  54.173  44.523  1.00 14.50           C  
-ATOM   1589  C   SER A 212       2.337  54.386  43.025  1.00 21.75           C  
-ATOM   1590  O   SER A 212       2.259  55.534  42.568  1.00 21.93           O  
-ATOM   1591  CB  SER A 212       1.355  54.934  45.211  1.00 15.12           C  
-ATOM   1592  OG  SER A 212       0.118  54.303  44.978  1.00 13.22           O  
-ATOM   1593  N   PRO A 213       2.192  53.264  42.271  1.00 23.23           N  
-ATOM   1594  CA  PRO A 213       1.945  53.349  40.829  1.00 21.02           C  
-ATOM   1595  C   PRO A 213       0.849  54.321  40.459  1.00 19.13           C  
-ATOM   1596  O   PRO A 213       1.017  55.184  39.612  1.00 27.56           O  
-ATOM   1597  CB  PRO A 213       1.602  51.919  40.393  1.00 20.29           C  
-ATOM   1598  CG  PRO A 213       2.090  51.014  41.535  1.00 28.00           C  
-ATOM   1599  CD  PRO A 213       2.252  51.897  42.783  1.00 25.05           C  
-ATOM   1600  N   GLY A 214      -0.279  54.169  41.142  1.00 14.82           N  
-ATOM   1601  CA  GLY A 214      -1.396  55.057  40.855  1.00 11.73           C  
-ATOM   1602  C   GLY A 214      -1.131  56.562  40.981  1.00 16.73           C  
-ATOM   1603  O   GLY A 214      -1.838  57.366  40.392  1.00 18.79           O  
-ATOM   1604  N   SER A 215      -0.120  56.979  41.746  1.00 17.16           N  
-ATOM   1605  CA  SER A 215       0.068  58.425  41.839  1.00 16.69           C  
-ATOM   1606  C   SER A 215       1.252  58.958  41.067  1.00 16.13           C  
-ATOM   1607  O   SER A 215       1.328  60.161  40.835  1.00 15.15           O  
-ATOM   1608  CB  SER A 215       0.333  58.824  43.298  1.00 18.02           C  
-ATOM   1609  OG  SER A 215      -0.780  58.428  44.069  1.00 16.10           O  
-ATOM   1610  N   ARG A 216       2.166  58.067  40.662  1.00 11.76           N  
-ATOM   1611  CA  ARG A 216       3.365  58.553  39.993  1.00  7.47           C  
-ATOM   1612  C   ARG A 216       3.154  59.544  38.901  1.00 12.43           C  
-ATOM   1613  O   ARG A 216       4.003  60.381  38.658  1.00 13.54           O  
-ATOM   1614  CB  ARG A 216       4.172  57.414  39.365  1.00  3.07           C  
-ATOM   1615  CG  ARG A 216       4.511  56.315  40.358  1.00  4.23           C  
-ATOM   1616  CD  ARG A 216       5.389  55.216  39.790  1.00  3.04           C  
-ATOM   1617  NE  ARG A 216       5.359  54.129  40.725  1.00  5.69           N  
-ATOM   1618  CZ  ARG A 216       5.964  52.959  40.550  1.00 11.34           C  
-ATOM   1619  NH1 ARG A 216       6.790  52.725  39.536  1.00 14.95           N  
-ATOM   1620  NH2 ARG A 216       5.701  52.009  41.433  1.00 13.59           N  
-ATOM   1621  N   ASP A 217       2.000  59.449  38.236  1.00 15.00           N  
-ATOM   1622  CA  ASP A 217       1.829  60.353  37.105  1.00 19.24           C  
-ATOM   1623  C   ASP A 217       1.248  61.740  37.367  1.00 18.74           C  
-ATOM   1624  O   ASP A 217       1.229  62.518  36.421  1.00 21.91           O  
-ATOM   1625  CB  ASP A 217       0.959  59.675  36.016  1.00 23.06           C  
-ATOM   1626  CG  ASP A 217       1.414  58.278  35.549  1.00 25.62           C  
-ATOM   1627  OD1 ASP A 217       2.548  57.880  35.829  1.00 22.78           O  
-ATOM   1628  OD2 ASP A 217       0.623  57.592  34.893  1.00 22.82           O  
-ATOM   1629  N   LEU A 218       0.777  62.060  38.588  1.00 16.28           N  
-ATOM   1630  CA  LEU A 218       0.167  63.379  38.791  1.00  7.33           C  
-ATOM   1631  C   LEU A 218       1.103  64.435  39.320  1.00  6.79           C  
-ATOM   1632  O   LEU A 218       0.637  65.480  39.781  1.00  8.66           O  
-ATOM   1633  CB  LEU A 218      -1.065  63.315  39.710  1.00  4.41           C  
-ATOM   1634  CG  LEU A 218      -2.056  62.222  39.286  1.00  5.15           C  
-ATOM   1635  CD1 LEU A 218      -1.925  61.003  40.179  1.00 12.78           C  
-ATOM   1636  CD2 LEU A 218      -3.501  62.692  39.304  1.00  9.62           C  
-ATOM   1637  N   PHE A 219       2.408  64.162  39.300  1.00  2.00           N  
-ATOM   1638  CA  PHE A 219       3.315  65.184  39.796  1.00  3.78           C  
-ATOM   1639  C   PHE A 219       4.652  64.960  39.090  1.00  6.87           C  
-ATOM   1640  O   PHE A 219       4.892  63.889  38.535  1.00  2.00           O  
-ATOM   1641  CB  PHE A 219       3.368  65.195  41.347  1.00  3.53           C  
-ATOM   1642  CG  PHE A 219       3.986  63.928  41.898  1.00  2.00           C  
-ATOM   1643  CD1 PHE A 219       3.212  62.771  42.060  1.00  2.00           C  
-ATOM   1644  CD2 PHE A 219       5.364  63.892  42.168  1.00  2.00           C  
-ATOM   1645  CE1 PHE A 219       3.828  61.581  42.454  1.00  2.00           C  
-ATOM   1646  CE2 PHE A 219       5.977  62.707  42.564  1.00  2.00           C  
-ATOM   1647  CZ  PHE A 219       5.206  61.550  42.701  1.00  2.00           C  
-ATOM   1648  N   ARG A 220       5.515  65.991  39.120  1.00  6.39           N  
-ATOM   1649  CA  ARG A 220       6.808  65.884  38.440  1.00  9.97           C  
-ATOM   1650  C   ARG A 220       7.912  65.556  39.397  1.00 14.43           C  
-ATOM   1651  O   ARG A 220       8.466  64.473  39.360  1.00 18.16           O  
-ATOM   1652  CB  ARG A 220       7.108  67.173  37.640  1.00 12.04           C  
-ATOM   1653  CG  ARG A 220       8.271  67.027  36.635  1.00 15.91           C  
-ATOM   1654  CD  ARG A 220       8.000  67.797  35.337  1.00 19.43           C  
-ATOM   1655  NE  ARG A 220       9.148  67.726  34.445  1.00 22.80           N  
-ATOM   1656  CZ  ARG A 220       9.270  68.564  33.400  1.00 22.42           C  
-ATOM   1657  NH1 ARG A 220       8.375  69.516  33.153  1.00 20.61           N  
-ATOM   1658  NH2 ARG A 220      10.321  68.455  32.605  1.00 25.46           N  
-ATOM   1659  N   ARG A 221       8.195  66.527  40.276  1.00 17.89           N  
-ATOM   1660  CA  ARG A 221       9.258  66.383  41.266  1.00 17.22           C  
-ATOM   1661  C   ARG A 221       8.644  66.313  42.658  1.00 17.46           C  
-ATOM   1662  O   ARG A 221       7.445  66.512  42.819  1.00 17.58           O  
-ATOM   1663  CB  ARG A 221      10.161  67.625  41.216  1.00 19.05           C  
-ATOM   1664  CG  ARG A 221      10.647  68.028  39.816  1.00 16.37           C  
-ATOM   1665  CD  ARG A 221      11.060  69.518  39.785  1.00 28.68           C  
-ATOM   1666  NE  ARG A 221      10.931  70.103  38.460  1.00 33.55           N  
-ATOM   1667  CZ  ARG A 221      11.679  69.665  37.455  1.00 35.29           C  
-ATOM   1668  NH1 ARG A 221      12.631  68.772  37.692  1.00 34.37           N  
-ATOM   1669  NH2 ARG A 221      11.456  70.112  36.218  1.00 36.84           N  
-ATOM   1670  N   ALA A 222       9.486  66.088  43.675  1.00 15.70           N  
-ATOM   1671  CA  ALA A 222       8.963  66.034  45.036  1.00 13.29           C  
-ATOM   1672  C   ALA A 222      10.009  66.556  46.017  1.00 13.23           C  
-ATOM   1673  O   ALA A 222      11.200  66.445  45.737  1.00 14.05           O  
-ATOM   1674  CB  ALA A 222       8.669  64.583  45.397  1.00  9.62           C  
-ATOM   1675  N   ILE A 223       9.543  67.114  47.149  1.00 13.40           N  
-ATOM   1676  CA  ILE A 223      10.397  67.622  48.233  1.00 11.20           C  
-ATOM   1677  C   ILE A 223       9.900  66.909  49.494  1.00 11.06           C  
-ATOM   1678  O   ILE A 223       8.696  66.894  49.755  1.00  9.43           O  
-ATOM   1679  CB  ILE A 223      10.267  69.139  48.446  1.00  7.01           C  
-ATOM   1680  CG1 ILE A 223      10.630  69.951  47.196  1.00  8.53           C  
-ATOM   1681  CG2 ILE A 223      11.073  69.602  49.656  1.00  6.83           C  
-ATOM   1682  CD1 ILE A 223      10.706  71.477  47.400  1.00  2.00           C  
-ATOM   1683  N   LEU A 224      10.832  66.364  50.282  1.00 10.82           N  
-ATOM   1684  CA  LEU A 224      10.454  65.636  51.504  1.00 10.14           C  
-ATOM   1685  C   LEU A 224      11.186  66.286  52.662  1.00  7.47           C  
-ATOM   1686  O   LEU A 224      12.407  66.353  52.657  1.00  8.76           O  
-ATOM   1687  CB  LEU A 224      10.856  64.138  51.432  1.00  9.75           C  
-ATOM   1688  CG  LEU A 224      10.162  63.329  50.311  1.00  4.79           C  
-ATOM   1689  CD1 LEU A 224      10.817  63.512  48.939  1.00  5.18           C  
-ATOM   1690  CD2 LEU A 224      10.126  61.833  50.641  1.00  2.00           C  
-ATOM   1691  N   GLN A 225      10.441  66.772  53.661  1.00  6.25           N  
-ATOM   1692  CA  GLN A 225      11.071  67.435  54.809  1.00  5.17           C  
-ATOM   1693  C   GLN A 225      10.840  66.600  56.068  1.00  5.65           C  
-ATOM   1694  O   GLN A 225       9.703  66.387  56.488  1.00  4.29           O  
-ATOM   1695  CB  GLN A 225      10.491  68.867  54.981  1.00  6.19           C  
-ATOM   1696  CG  GLN A 225      10.039  69.499  53.638  1.00  9.69           C  
-ATOM   1697  CD  GLN A 225       9.983  71.001  53.631  1.00  7.42           C  
-ATOM   1698  OE1 GLN A 225       8.963  71.660  53.579  1.00 11.52           O  
-ATOM   1699  NE2 GLN A 225      11.165  71.555  53.655  1.00 14.31           N  
-ATOM   1700  N   SER A 226      11.935  66.119  56.667  1.00  7.22           N  
-ATOM   1701  CA  SER A 226      11.870  65.309  57.882  1.00  7.97           C  
-ATOM   1702  C   SER A 226      10.855  64.187  57.790  1.00  9.27           C  
-ATOM   1703  O   SER A 226      10.069  63.996  58.704  1.00 14.08           O  
-ATOM   1704  CB  SER A 226      11.509  66.207  59.087  1.00  9.13           C  
-ATOM   1705  OG  SER A 226      12.345  67.380  59.155  1.00 17.16           O  
-ATOM   1706  N   GLY A 227      10.841  63.453  56.686  1.00  9.93           N  
-ATOM   1707  CA  GLY A 227       9.866  62.365  56.553  1.00 10.00           C  
-ATOM   1708  C   GLY A 227      10.398  61.422  55.485  1.00  9.65           C  
-ATOM   1709  O   GLY A 227      11.241  61.798  54.678  1.00  9.92           O  
-ATOM   1710  N   SER A 228       9.934  60.186  55.475  1.00  4.61           N  
-ATOM   1711  CA  SER A 228      10.456  59.283  54.477  1.00  4.86           C  
-ATOM   1712  C   SER A 228       9.499  58.143  54.546  1.00  8.96           C  
-ATOM   1713  O   SER A 228       9.098  57.836  55.653  1.00 14.21           O  
-ATOM   1714  CB  SER A 228      11.860  58.847  54.901  1.00  2.40           C  
-ATOM   1715  OG  SER A 228      12.576  58.342  53.834  1.00 10.54           O  
-ATOM   1716  N   PRO A 229       9.076  57.527  53.426  1.00 11.99           N  
-ATOM   1717  CA  PRO A 229       7.931  56.615  53.484  1.00  9.60           C  
-ATOM   1718  C   PRO A 229       8.277  55.397  54.298  1.00  7.79           C  
-ATOM   1719  O   PRO A 229       7.446  54.725  54.874  1.00 10.90           O  
-ATOM   1720  CB  PRO A 229       7.694  56.249  52.014  1.00 10.02           C  
-ATOM   1721  CG  PRO A 229       9.027  56.508  51.286  1.00 11.62           C  
-ATOM   1722  CD  PRO A 229       9.709  57.613  52.107  1.00 11.57           C  
-ATOM   1723  N   ASN A 230       9.573  55.114  54.322  1.00  7.25           N  
-ATOM   1724  CA  ASN A 230      10.101  53.963  55.035  1.00  6.94           C  
-ATOM   1725  C   ASN A 230      10.359  54.238  56.512  1.00  9.37           C  
-ATOM   1726  O   ASN A 230      10.986  53.433  57.193  1.00 15.47           O  
-ATOM   1727  CB  ASN A 230      11.407  53.456  54.369  1.00  2.00           C  
-ATOM   1728  CG  ASN A 230      12.516  54.501  54.448  1.00  6.77           C  
-ATOM   1729  OD1 ASN A 230      12.303  55.690  54.241  1.00  2.00           O  
-ATOM   1730  ND2 ASN A 230      13.720  54.047  54.770  1.00 11.81           N  
-ATOM   1731  N   CYS A 231       9.937  55.401  57.009  1.00  7.38           N  
-ATOM   1732  CA  CYS A 231      10.172  55.654  58.423  1.00  5.55           C  
-ATOM   1733  C   CYS A 231       9.274  54.707  59.206  1.00  7.90           C  
-ATOM   1734  O   CYS A 231       8.155  54.482  58.758  1.00  6.82           O  
-ATOM   1735  CB  CYS A 231       9.735  57.072  58.763  1.00  2.72           C  
-ATOM   1736  SG  CYS A 231      10.980  58.262  58.302  1.00 16.21           S  
-ATOM   1737  N   PRO A 232       9.742  54.211  60.387  1.00  6.94           N  
-ATOM   1738  CA  PRO A 232       9.078  53.113  61.078  1.00  6.07           C  
-ATOM   1739  C   PRO A 232       7.696  53.428  61.555  1.00 10.04           C  
-ATOM   1740  O   PRO A 232       6.866  52.567  61.792  1.00 14.91           O  
-ATOM   1741  CB  PRO A 232       9.964  52.840  62.296  1.00  3.63           C  
-ATOM   1742  CG  PRO A 232      10.918  54.028  62.451  1.00  2.00           C  
-ATOM   1743  CD  PRO A 232      10.904  54.738  61.101  1.00  6.31           C  
-ATOM   1744  N   TRP A 233       7.475  54.719  61.733  1.00 10.65           N  
-ATOM   1745  CA  TRP A 233       6.176  55.128  62.214  1.00 10.28           C  
-ATOM   1746  C   TRP A 233       5.197  55.439  61.106  1.00 12.09           C  
-ATOM   1747  O   TRP A 233       4.084  55.868  61.389  1.00 15.11           O  
-ATOM   1748  CB  TRP A 233       6.341  56.372  63.088  1.00  7.96           C  
-ATOM   1749  CG  TRP A 233       7.222  57.386  62.399  1.00  7.00           C  
-ATOM   1750  CD1 TRP A 233       8.621  57.518  62.583  1.00  9.69           C  
-ATOM   1751  CD2 TRP A 233       6.822  58.383  61.495  1.00  5.75           C  
-ATOM   1752  NE1 TRP A 233       9.099  58.558  61.845  1.00  9.36           N  
-ATOM   1753  CE2 TRP A 233       8.057  59.138  61.158  1.00  6.32           C  
-ATOM   1754  CE3 TRP A 233       5.602  58.746  60.911  1.00  4.33           C  
-ATOM   1755  CZ2 TRP A 233       7.987  60.215  60.272  1.00  2.00           C  
-ATOM   1756  CZ3 TRP A 233       5.565  59.831  60.018  1.00  4.01           C  
-ATOM   1757  CH2 TRP A 233       6.738  60.552  59.709  1.00  5.70           C  
-ATOM   1758  N   ALA A 234       5.603  55.263  59.837  1.00 10.40           N  
-ATOM   1759  CA  ALA A 234       4.664  55.613  58.762  1.00 10.23           C  
-ATOM   1760  C   ALA A 234       3.829  54.471  58.193  1.00  9.20           C  
-ATOM   1761  O   ALA A 234       2.994  54.737  57.345  1.00  8.66           O  
-ATOM   1762  CB  ALA A 234       5.389  56.299  57.601  1.00  9.92           C  
-ATOM   1763  N   SER A 235       4.009  53.214  58.584  1.00  9.85           N  
-ATOM   1764  CA  SER A 235       3.125  52.240  57.963  1.00  8.55           C  
-ATOM   1765  C   SER A 235       2.925  51.041  58.838  1.00 11.23           C  
-ATOM   1766  O   SER A 235       3.702  50.831  59.755  1.00 14.24           O  
-ATOM   1767  CB  SER A 235       3.689  51.813  56.616  1.00  9.56           C  
-ATOM   1768  OG  SER A 235       5.031  51.343  56.756  1.00 11.78           O  
-ATOM   1769  N   VAL A 236       1.875  50.263  58.594  1.00 12.67           N  
-ATOM   1770  CA  VAL A 236       1.665  49.054  59.377  1.00 12.89           C  
-ATOM   1771  C   VAL A 236       1.203  47.980  58.410  1.00 14.64           C  
-ATOM   1772  O   VAL A 236       0.770  48.250  57.299  1.00 18.52           O  
-ATOM   1773  CB  VAL A 236       0.694  49.230  60.562  1.00 13.36           C  
-ATOM   1774  CG1 VAL A 236       1.252  50.234  61.568  1.00  9.32           C  
-ATOM   1775  CG2 VAL A 236      -0.759  49.575  60.164  1.00 12.44           C  
-ATOM   1776  N   SER A 237       1.280  46.733  58.829  1.00 11.99           N  
-ATOM   1777  CA  SER A 237       0.841  45.682  57.934  1.00 14.87           C  
-ATOM   1778  C   SER A 237      -0.664  45.589  58.008  1.00 16.44           C  
-ATOM   1779  O   SER A 237      -1.283  46.134  58.916  1.00 17.84           O  
-ATOM   1780  CB  SER A 237       1.473  44.359  58.355  1.00 20.46           C  
-ATOM   1781  OG  SER A 237       1.233  44.181  59.749  1.00 31.59           O  
-ATOM   1782  N   VAL A 238      -1.261  44.849  57.074  1.00 16.30           N  
-ATOM   1783  CA  VAL A 238      -2.705  44.760  57.161  1.00 17.07           C  
-ATOM   1784  C   VAL A 238      -3.148  44.105  58.431  1.00 17.30           C  
-ATOM   1785  O   VAL A 238      -4.183  44.417  59.005  1.00 20.67           O  
-ATOM   1786  CB  VAL A 238      -3.267  44.082  55.922  1.00 13.86           C  
-ATOM   1787  CG1 VAL A 238      -3.019  44.988  54.718  1.00 21.79           C  
-ATOM   1788  CG2 VAL A 238      -2.649  42.709  55.657  1.00 20.71           C  
-ATOM   1789  N   ALA A 239      -2.299  43.184  58.874  1.00 16.88           N  
-ATOM   1790  CA  ALA A 239      -2.651  42.491  60.097  1.00 19.71           C  
-ATOM   1791  C   ALA A 239      -2.739  43.451  61.258  1.00 22.34           C  
-ATOM   1792  O   ALA A 239      -3.704  43.480  62.010  1.00 24.99           O  
-ATOM   1793  CB  ALA A 239      -1.629  41.400  60.402  1.00 20.58           C  
-ATOM   1794  N   GLU A 240      -1.687  44.271  61.369  1.00 21.45           N  
-ATOM   1795  CA  GLU A 240      -1.680  45.231  62.462  1.00 20.50           C  
-ATOM   1796  C   GLU A 240      -2.828  46.188  62.386  1.00 19.54           C  
-ATOM   1797  O   GLU A 240      -3.458  46.502  63.378  1.00 22.06           O  
-ATOM   1798  CB  GLU A 240      -0.360  46.019  62.554  1.00 23.57           C  
-ATOM   1799  CG  GLU A 240       0.418  45.679  63.843  1.00 30.30           C  
-ATOM   1800  CD  GLU A 240      -0.134  46.401  65.072  1.00 27.07           C  
-ATOM   1801  OE1 GLU A 240      -1.308  46.735  65.099  1.00 26.76           O  
-ATOM   1802  OE2 GLU A 240       0.622  46.643  65.998  1.00 28.68           O  
-ATOM   1803  N   GLY A 241      -3.095  46.672  61.187  1.00 19.60           N  
-ATOM   1804  CA  GLY A 241      -4.201  47.607  61.081  1.00 17.71           C  
-ATOM   1805  C   GLY A 241      -5.484  46.963  61.526  1.00 16.81           C  
-ATOM   1806  O   GLY A 241      -6.326  47.575  62.165  1.00 17.07           O  
-ATOM   1807  N   ARG A 242      -5.615  45.674  61.211  1.00 18.59           N  
-ATOM   1808  CA  ARG A 242      -6.839  45.009  61.630  1.00 21.59           C  
-ATOM   1809  C   ARG A 242      -6.910  44.993  63.144  1.00 22.77           C  
-ATOM   1810  O   ARG A 242      -7.902  45.334  63.782  1.00 24.72           O  
-ATOM   1811  CB  ARG A 242      -6.885  43.591  61.054  1.00 20.14           C  
-ATOM   1812  CG  ARG A 242      -8.240  42.915  61.291  1.00 27.41           C  
-ATOM   1813  CD  ARG A 242      -8.448  41.677  60.402  1.00 32.04           C  
-ATOM   1814  NE  ARG A 242      -8.830  42.067  59.050  1.00 38.93           N  
-ATOM   1815  CZ  ARG A 242     -10.099  42.372  58.735  1.00 42.03           C  
-ATOM   1816  NH1 ARG A 242     -11.063  42.318  59.650  1.00 41.27           N  
-ATOM   1817  NH2 ARG A 242     -10.400  42.719  57.484  1.00 48.90           N  
-ATOM   1818  N   ARG A 243      -5.778  44.583  63.707  1.00 21.15           N  
-ATOM   1819  CA  ARG A 243      -5.649  44.508  65.137  1.00 19.68           C  
-ATOM   1820  C   ARG A 243      -6.085  45.804  65.811  1.00 20.18           C  
-ATOM   1821  O   ARG A 243      -6.945  45.824  66.687  1.00 22.86           O  
-ATOM   1822  CB  ARG A 243      -4.203  44.175  65.490  1.00 25.56           C  
-ATOM   1823  CG  ARG A 243      -4.106  43.158  66.634  1.00 39.24           C  
-ATOM   1824  CD  ARG A 243      -2.964  43.359  67.672  1.00 50.63           C  
-ATOM   1825  NE  ARG A 243      -2.293  44.668  67.651  1.00 52.71           N  
-ATOM   1826  CZ  ARG A 243      -2.663  45.754  68.373  1.00 54.11           C  
-ATOM   1827  NH1 ARG A 243      -3.759  45.769  69.142  1.00 53.49           N  
-ATOM   1828  NH2 ARG A 243      -1.899  46.844  68.331  1.00 52.99           N  
-ATOM   1829  N   ARG A 244      -5.476  46.905  65.381  1.00 14.29           N  
-ATOM   1830  CA  ARG A 244      -5.837  48.182  65.980  1.00 13.22           C  
-ATOM   1831  C   ARG A 244      -7.269  48.582  65.667  1.00 18.25           C  
-ATOM   1832  O   ARG A 244      -7.947  49.238  66.450  1.00 22.33           O  
-ATOM   1833  CB  ARG A 244      -4.915  49.321  65.515  1.00  8.69           C  
-ATOM   1834  CG  ARG A 244      -3.440  48.987  65.728  1.00  3.14           C  
-ATOM   1835  CD  ARG A 244      -2.461  50.102  65.352  1.00  2.00           C  
-ATOM   1836  NE  ARG A 244      -1.132  49.595  65.636  1.00  2.00           N  
-ATOM   1837  CZ  ARG A 244      -0.019  50.311  65.467  1.00  4.07           C  
-ATOM   1838  NH1 ARG A 244      -0.037  51.595  65.109  1.00  3.12           N  
-ATOM   1839  NH2 ARG A 244       1.148  49.721  65.664  1.00  3.18           N  
-ATOM   1840  N   ALA A 245      -7.734  48.170  64.494  1.00 19.86           N  
-ATOM   1841  CA  ALA A 245      -9.075  48.541  64.107  1.00 18.78           C  
-ATOM   1842  C   ALA A 245     -10.095  47.949  65.022  1.00 20.84           C  
-ATOM   1843  O   ALA A 245     -11.067  48.583  65.403  1.00 21.84           O  
-ATOM   1844  CB  ALA A 245      -9.343  48.070  62.679  1.00 21.74           C  
-ATOM   1845  N   VAL A 246      -9.839  46.699  65.386  1.00 22.44           N  
-ATOM   1846  CA  VAL A 246     -10.754  45.975  66.263  1.00 25.15           C  
-ATOM   1847  C   VAL A 246     -10.609  46.438  67.693  1.00 25.86           C  
-ATOM   1848  O   VAL A 246     -11.558  46.574  68.455  1.00 26.45           O  
-ATOM   1849  CB  VAL A 246     -10.494  44.470  66.075  1.00 23.34           C  
-ATOM   1850  CG1 VAL A 246     -10.293  43.644  67.350  1.00 23.96           C  
-ATOM   1851  CG2 VAL A 246     -11.575  43.874  65.168  1.00 29.50           C  
-ATOM   1852  N   GLU A 247      -9.357  46.691  68.063  1.00 28.05           N  
-ATOM   1853  CA  GLU A 247      -9.075  47.151  69.409  1.00 23.29           C  
-ATOM   1854  C   GLU A 247      -9.797  48.444  69.684  1.00 19.74           C  
-ATOM   1855  O   GLU A 247     -10.273  48.697  70.782  1.00 22.40           O  
-ATOM   1856  CB  GLU A 247      -7.564  47.278  69.601  1.00 28.40           C  
-ATOM   1857  CG  GLU A 247      -7.144  47.345  71.067  1.00 40.09           C  
-ATOM   1858  CD  GLU A 247      -7.638  46.115  71.815  1.00 46.37           C  
-ATOM   1859  OE1 GLU A 247      -7.740  45.049  71.196  1.00 45.76           O  
-ATOM   1860  OE2 GLU A 247      -7.933  46.237  73.007  1.00 52.56           O  
-ATOM   1861  N   LEU A 248      -9.884  49.267  68.644  1.00 17.77           N  
-ATOM   1862  CA  LEU A 248     -10.612  50.516  68.796  1.00 16.07           C  
-ATOM   1863  C   LEU A 248     -12.057  50.175  69.038  1.00 16.10           C  
-ATOM   1864  O   LEU A 248     -12.733  50.697  69.906  1.00 18.19           O  
-ATOM   1865  CB  LEU A 248     -10.540  51.368  67.524  1.00 13.23           C  
-ATOM   1866  CG  LEU A 248     -11.058  52.795  67.764  1.00 12.13           C  
-ATOM   1867  CD1 LEU A 248     -10.051  53.618  68.579  1.00 21.34           C  
-ATOM   1868  CD2 LEU A 248     -11.360  53.513  66.456  1.00 10.06           C  
-ATOM   1869  N   GLY A 249     -12.517  49.220  68.249  1.00 17.29           N  
-ATOM   1870  CA  GLY A 249     -13.888  48.784  68.363  1.00 18.58           C  
-ATOM   1871  C   GLY A 249     -14.254  48.364  69.750  1.00 21.46           C  
-ATOM   1872  O   GLY A 249     -15.311  48.718  70.259  1.00 19.70           O  
-ATOM   1873  N   ARG A 250     -13.353  47.612  70.389  1.00 24.60           N  
-ATOM   1874  CA  ARG A 250     -13.712  47.195  71.734  1.00 29.78           C  
-ATOM   1875  C   ARG A 250     -13.672  48.348  72.707  1.00 28.84           C  
-ATOM   1876  O   ARG A 250     -14.412  48.351  73.672  1.00 32.85           O  
-ATOM   1877  CB  ARG A 250     -13.000  45.921  72.197  1.00 31.65           C  
-ATOM   1878  CG  ARG A 250     -11.564  46.095  72.694  1.00 38.32           C  
-ATOM   1879  CD  ARG A 250     -10.716  44.826  72.510  1.00 42.10           C  
-ATOM   1880  NE  ARG A 250     -11.511  43.603  72.529  1.00 47.16           N  
-ATOM   1881  CZ  ARG A 250     -11.060  42.488  71.919  1.00 52.25           C  
-ATOM   1882  NH1 ARG A 250      -9.846  42.455  71.360  1.00 51.05           N  
-ATOM   1883  NH2 ARG A 250     -11.833  41.398  71.868  1.00 54.19           N  
-ATOM   1884  N   ASN A 251     -12.838  49.354  72.455  1.00 27.17           N  
-ATOM   1885  CA  ASN A 251     -12.850  50.482  73.400  1.00 27.75           C  
-ATOM   1886  C   ASN A 251     -14.185  51.219  73.329  1.00 24.12           C  
-ATOM   1887  O   ASN A 251     -14.548  51.915  74.259  1.00 23.52           O  
-ATOM   1888  CB  ASN A 251     -11.711  51.511  73.204  1.00 32.09           C  
-ATOM   1889  CG  ASN A 251     -10.356  51.085  73.755  1.00 34.22           C  
-ATOM   1890  OD1 ASN A 251      -9.710  51.814  74.491  1.00 37.29           O  
-ATOM   1891  ND2 ASN A 251      -9.902  49.886  73.399  1.00 34.04           N  
-ATOM   1892  N   LEU A 252     -14.909  51.094  72.209  1.00 24.55           N  
-ATOM   1893  CA  LEU A 252     -16.217  51.752  72.133  1.00 25.74           C  
-ATOM   1894  C   LEU A 252     -17.323  50.719  72.346  1.00 26.48           C  
-ATOM   1895  O   LEU A 252     -18.519  50.958  72.198  1.00 23.35           O  
-ATOM   1896  CB  LEU A 252     -16.488  52.490  70.818  1.00 25.90           C  
-ATOM   1897  CG  LEU A 252     -15.578  53.685  70.503  1.00 28.99           C  
-ATOM   1898  CD1 LEU A 252     -15.508  54.707  71.638  1.00 28.34           C  
-ATOM   1899  CD2 LEU A 252     -14.181  53.256  70.045  1.00 33.43           C  
-ATOM   1900  N   ASN A 253     -16.888  49.519  72.719  1.00 30.95           N  
-ATOM   1901  CA  ASN A 253     -17.778  48.392  72.987  1.00 36.81           C  
-ATOM   1902  C   ASN A 253     -18.655  48.030  71.804  1.00 34.30           C  
-ATOM   1903  O   ASN A 253     -19.840  47.745  71.914  1.00 31.53           O  
-ATOM   1904  CB  ASN A 253     -18.562  48.511  74.327  1.00 41.04           C  
-ATOM   1905  CG  ASN A 253     -19.823  49.371  74.216  1.00 46.22           C  
-ATOM   1906  N   CYS A 254     -18.026  48.082  70.650  1.00 35.23           N  
-ATOM   1907  CA  CYS A 254     -18.746  47.740  69.444  1.00 36.37           C  
-ATOM   1908  C   CYS A 254     -18.806  46.251  69.356  1.00 40.41           C  
-ATOM   1909  O   CYS A 254     -17.977  45.558  69.928  1.00 42.26           O  
-ATOM   1910  CB  CYS A 254     -17.968  48.234  68.238  1.00 29.99           C  
-ATOM   1911  SG  CYS A 254     -18.232  49.996  68.077  1.00 22.76           S  
-ATOM   1912  N   ASN A 255     -19.809  45.776  68.607  1.00 40.92           N  
-ATOM   1913  CA  ASN A 255     -19.980  44.344  68.396  1.00 40.55           C  
-ATOM   1914  C   ASN A 255     -18.837  43.974  67.487  1.00 39.35           C  
-ATOM   1915  O   ASN A 255     -18.743  44.576  66.427  1.00 38.20           O  
-ATOM   1916  CB  ASN A 255     -21.341  44.116  67.707  1.00 42.22           C  
-ATOM   1917  CG  ASN A 255     -21.585  42.672  67.309  1.00 42.69           C  
-ATOM   1918  OD1 ASN A 255     -20.725  41.998  66.773  1.00 44.86           O  
-ATOM   1919  ND2 ASN A 255     -22.792  42.190  67.567  1.00 44.25           N  
-ATOM   1920  N   LEU A 256     -17.980  43.038  67.899  1.00 39.51           N  
-ATOM   1921  CA  LEU A 256     -16.841  42.692  67.051  1.00 42.33           C  
-ATOM   1922  C   LEU A 256     -16.977  41.364  66.324  1.00 44.21           C  
-ATOM   1923  O   LEU A 256     -15.986  40.706  66.026  1.00 47.32           O  
-ATOM   1924  CB  LEU A 256     -15.527  42.636  67.853  1.00 43.59           C  
-ATOM   1925  CG  LEU A 256     -15.167  43.899  68.662  1.00 47.10           C  
-ATOM   1926  CD1 LEU A 256     -15.667  43.837  70.112  1.00 50.25           C  
-ATOM   1927  CD2 LEU A 256     -13.648  44.085  68.684  1.00 49.35           C  
-ATOM   1928  N   ASN A 257     -18.209  40.954  66.040  1.00 44.93           N  
-ATOM   1929  CA  ASN A 257     -18.446  39.689  65.349  1.00 45.58           C  
-ATOM   1930  C   ASN A 257     -18.190  39.770  63.848  1.00 45.23           C  
-ATOM   1931  O   ASN A 257     -18.074  38.772  63.153  1.00 44.48           O  
-ATOM   1932  CB  ASN A 257     -19.885  39.220  65.621  1.00 47.18           C  
-ATOM   1933  N   SER A 258     -18.108  40.983  63.317  1.00 47.53           N  
-ATOM   1934  CA  SER A 258     -17.875  41.086  61.879  1.00 46.62           C  
-ATOM   1935  C   SER A 258     -17.447  42.492  61.525  1.00 45.93           C  
-ATOM   1936  O   SER A 258     -17.716  43.454  62.239  1.00 45.45           O  
-ATOM   1937  CB  SER A 258     -19.177  40.743  61.130  1.00 48.28           C  
-ATOM   1938  OG  SER A 258     -20.272  41.439  61.741  1.00 49.10           O  
-ATOM   1939  N   ASP A 259     -16.807  42.611  60.356  1.00 43.15           N  
-ATOM   1940  CA  ASP A 259     -16.392  43.960  59.967  1.00 39.16           C  
-ATOM   1941  C   ASP A 259     -17.603  44.839  59.743  1.00 36.02           C  
-ATOM   1942  O   ASP A 259     -17.582  46.030  59.962  1.00 34.56           O  
-ATOM   1943  CB  ASP A 259     -15.510  44.013  58.702  1.00 37.85           C  
-ATOM   1944  CG  ASP A 259     -14.228  43.207  58.821  1.00 39.63           C  
-ATOM   1945  OD1 ASP A 259     -13.947  42.697  59.903  1.00 42.63           O  
-ATOM   1946  OD2 ASP A 259     -13.511  43.092  57.827  1.00 40.96           O  
-ATOM   1947  N   GLU A 260     -18.687  44.211  59.313  1.00 34.31           N  
-ATOM   1948  CA  GLU A 260     -19.893  44.978  59.060  1.00 34.44           C  
-ATOM   1949  C   GLU A 260     -20.438  45.628  60.310  1.00 34.84           C  
-ATOM   1950  O   GLU A 260     -20.857  46.782  60.338  1.00 32.90           O  
-ATOM   1951  CB  GLU A 260     -20.997  44.034  58.553  1.00 35.01           C  
-ATOM   1952  N   GLU A 261     -20.432  44.797  61.367  1.00 34.19           N  
-ATOM   1953  CA  GLU A 261     -20.950  45.244  62.649  1.00 32.00           C  
-ATOM   1954  C   GLU A 261     -20.023  46.281  63.250  1.00 31.67           C  
-ATOM   1955  O   GLU A 261     -20.417  47.345  63.730  1.00 31.79           O  
-ATOM   1956  CB  GLU A 261     -21.191  44.038  63.594  1.00 35.52           C  
-ATOM   1957  CG  GLU A 261     -22.578  43.336  63.399  1.00 32.88           C  
-ATOM   1958  N   LEU A 262     -18.747  45.931  63.201  1.00 27.26           N  
-ATOM   1959  CA  LEU A 262     -17.738  46.803  63.731  1.00 23.27           C  
-ATOM   1960  C   LEU A 262     -17.801  48.161  63.070  1.00 25.58           C  
-ATOM   1961  O   LEU A 262     -17.867  49.203  63.706  1.00 29.63           O  
-ATOM   1962  CB  LEU A 262     -16.390  46.126  63.490  1.00 23.67           C  
-ATOM   1963  CG  LEU A 262     -15.172  46.989  63.827  1.00 24.34           C  
-ATOM   1964  CD1 LEU A 262     -15.243  47.536  65.250  1.00 31.17           C  
-ATOM   1965  CD2 LEU A 262     -13.881  46.193  63.629  1.00 25.63           C  
-ATOM   1966  N   ILE A 263     -17.818  48.130  61.749  1.00 25.88           N  
-ATOM   1967  CA  ILE A 263     -17.847  49.358  60.975  1.00 28.49           C  
-ATOM   1968  C   ILE A 263     -19.124  50.128  61.189  1.00 31.31           C  
-ATOM   1969  O   ILE A 263     -19.069  51.329  61.404  1.00 33.92           O  
-ATOM   1970  CB  ILE A 263     -17.535  49.065  59.487  1.00 24.74           C  
-ATOM   1971  CG1 ILE A 263     -16.059  48.644  59.363  1.00 22.96           C  
-ATOM   1972  CG2 ILE A 263     -17.839  50.236  58.544  1.00 19.49           C  
-ATOM   1973  CD1 ILE A 263     -15.716  48.015  58.015  1.00 19.48           C  
-ATOM   1974  N   HIS A 264     -20.278  49.455  61.149  1.00 33.61           N  
-ATOM   1975  CA  HIS A 264     -21.518  50.205  61.354  1.00 38.39           C  
-ATOM   1976  C   HIS A 264     -21.444  50.922  62.677  1.00 37.97           C  
-ATOM   1977  O   HIS A 264     -21.759  52.098  62.833  1.00 40.86           O  
-ATOM   1978  CB  HIS A 264     -22.772  49.289  61.292  1.00 48.98           C  
-ATOM   1979  CG  HIS A 264     -23.998  49.912  61.975  1.00 61.06           C  
-ATOM   1980  ND1 HIS A 264     -24.607  51.064  61.597  1.00 64.46           N  
-ATOM   1981  CD2 HIS A 264     -24.674  49.438  63.133  1.00 65.12           C  
-ATOM   1982  CE1 HIS A 264     -25.606  51.285  62.475  1.00 66.51           C  
-ATOM   1983  NE2 HIS A 264     -25.661  50.319  63.410  1.00 67.54           N  
-ATOM   1984  N   CYS A 265     -20.976  50.147  63.640  1.00 32.83           N  
-ATOM   1985  CA  CYS A 265     -20.856  50.683  64.969  1.00 29.03           C  
-ATOM   1986  C   CYS A 265     -20.017  51.947  64.991  1.00 27.28           C  
-ATOM   1987  O   CYS A 265     -20.428  53.001  65.464  1.00 30.45           O  
-ATOM   1988  CB  CYS A 265     -20.271  49.584  65.840  1.00 29.44           C  
-ATOM   1989  SG  CYS A 265     -20.203  50.034  67.584  1.00 30.11           S  
-ATOM   1990  N   LEU A 266     -18.829  51.837  64.402  1.00 22.45           N  
-ATOM   1991  CA  LEU A 266     -17.952  52.988  64.390  1.00 20.17           C  
-ATOM   1992  C   LEU A 266     -18.529  54.142  63.596  1.00 21.08           C  
-ATOM   1993  O   LEU A 266     -18.179  55.288  63.818  1.00 22.26           O  
-ATOM   1994  CB  LEU A 266     -16.566  52.593  63.860  1.00 13.80           C  
-ATOM   1995  CG  LEU A 266     -15.856  51.541  64.743  1.00  9.35           C  
-ATOM   1996  CD1 LEU A 266     -14.740  50.835  63.993  1.00  6.60           C  
-ATOM   1997  CD2 LEU A 266     -15.281  52.153  66.026  1.00 11.99           C  
-ATOM   1998  N   ARG A 267     -19.415  53.842  62.651  1.00 25.36           N  
-ATOM   1999  CA  ARG A 267     -19.995  54.917  61.850  1.00 28.09           C  
-ATOM   2000  C   ARG A 267     -21.064  55.661  62.610  1.00 29.00           C  
-ATOM   2001  O   ARG A 267     -21.477  56.728  62.177  1.00 30.66           O  
-ATOM   2002  CB  ARG A 267     -20.549  54.436  60.474  1.00 29.47           C  
-ATOM   2003  CG  ARG A 267     -19.486  53.801  59.531  1.00 29.74           C  
-ATOM   2004  CD  ARG A 267     -19.493  54.271  58.048  1.00 31.57           C  
-ATOM   2005  NE  ARG A 267     -20.047  53.252  57.148  1.00 29.99           N  
-ATOM   2006  CZ  ARG A 267     -19.349  52.606  56.184  1.00 29.62           C  
-ATOM   2007  NH1 ARG A 267     -18.071  52.858  55.912  1.00 21.41           N  
-ATOM   2008  NH2 ARG A 267     -19.958  51.667  55.468  1.00 32.91           N  
-ATOM   2009  N   GLU A 268     -21.536  55.071  63.718  1.00 30.51           N  
-ATOM   2010  CA  GLU A 268     -22.578  55.737  64.515  1.00 31.71           C  
-ATOM   2011  C   GLU A 268     -21.981  56.554  65.625  1.00 32.42           C  
-ATOM   2012  O   GLU A 268     -22.645  57.400  66.212  1.00 36.23           O  
-ATOM   2013  CB  GLU A 268     -23.553  54.751  65.201  1.00 32.99           C  
-ATOM   2014  CG  GLU A 268     -24.478  53.994  64.216  1.00 40.92           C  
-ATOM   2015  N   LYS A 269     -20.727  56.248  65.966  1.00 30.23           N  
-ATOM   2016  CA  LYS A 269     -20.136  57.002  67.048  1.00 28.67           C  
-ATOM   2017  C   LYS A 269     -19.852  58.419  66.608  1.00 27.17           C  
-ATOM   2018  O   LYS A 269     -19.518  58.714  65.474  1.00 28.28           O  
-ATOM   2019  CB  LYS A 269     -18.853  56.308  67.490  1.00 31.35           C  
-ATOM   2020  CG  LYS A 269     -19.103  54.880  67.994  1.00 35.61           C  
-ATOM   2021  CD  LYS A 269     -19.619  54.834  69.447  1.00 42.51           C  
-ATOM   2022  CE  LYS A 269     -19.981  53.407  69.892  1.00 46.28           C  
-ATOM   2023  NZ  LYS A 269     -21.133  52.934  69.153  1.00 51.59           N  
-ATOM   2024  N   LYS A 270     -19.979  59.330  67.561  1.00 25.86           N  
-ATOM   2025  CA  LYS A 270     -19.709  60.724  67.236  1.00 25.82           C  
-ATOM   2026  C   LYS A 270     -18.202  60.845  67.060  1.00 25.56           C  
-ATOM   2027  O   LYS A 270     -17.471  60.112  67.724  1.00 28.89           O  
-ATOM   2028  CB  LYS A 270     -20.179  61.623  68.394  1.00 29.72           C  
-ATOM   2029  CG  LYS A 270     -21.486  61.133  69.055  1.00 34.57           C  
-ATOM   2030  N   PRO A 271     -17.728  61.788  66.223  1.00 21.99           N  
-ATOM   2031  CA  PRO A 271     -16.312  61.825  65.882  1.00 19.77           C  
-ATOM   2032  C   PRO A 271     -15.406  61.873  67.097  1.00 19.51           C  
-ATOM   2033  O   PRO A 271     -14.427  61.145  67.208  1.00 18.77           O  
-ATOM   2034  CB  PRO A 271     -16.150  63.032  64.951  1.00 17.86           C  
-ATOM   2035  CG  PRO A 271     -17.502  63.772  64.960  1.00 19.70           C  
-ATOM   2036  CD  PRO A 271     -18.527  62.824  65.588  1.00 21.39           C  
-ATOM   2037  N   GLN A 272     -15.781  62.747  68.045  1.00 20.44           N  
-ATOM   2038  CA  GLN A 272     -14.959  62.861  69.255  1.00 20.29           C  
-ATOM   2039  C   GLN A 272     -14.813  61.567  70.024  1.00 16.35           C  
-ATOM   2040  O   GLN A 272     -13.796  61.346  70.659  1.00 14.98           O  
-ATOM   2041  CB  GLN A 272     -15.424  63.988  70.206  1.00 25.23           C  
-ATOM   2042  CG  GLN A 272     -14.716  65.336  69.967  1.00 35.78           C  
-ATOM   2043  CD  GLN A 272     -13.264  65.246  70.428  1.00 40.78           C  
-ATOM   2044  OE1 GLN A 272     -12.922  64.449  71.287  1.00 41.42           O  
-ATOM   2045  NE2 GLN A 272     -12.403  66.076  69.832  1.00 43.62           N  
-ATOM   2046  N   GLU A 273     -15.814  60.683  69.974  1.00 15.06           N  
-ATOM   2047  CA  GLU A 273     -15.616  59.448  70.732  1.00 16.59           C  
-ATOM   2048  C   GLU A 273     -14.449  58.688  70.170  1.00 17.35           C  
-ATOM   2049  O   GLU A 273     -13.670  58.105  70.916  1.00 18.34           O  
-ATOM   2050  CB  GLU A 273     -16.839  58.526  70.737  1.00 19.35           C  
-ATOM   2051  CG  GLU A 273     -17.982  59.089  71.591  1.00 26.28           C  
-ATOM   2052  CD  GLU A 273     -19.280  58.340  71.341  1.00 32.07           C  
-ATOM   2053  OE1 GLU A 273     -19.991  58.685  70.392  1.00 31.44           O  
-ATOM   2054  OE2 GLU A 273     -19.578  57.420  72.102  1.00 35.54           O  
-ATOM   2055  N   LEU A 274     -14.342  58.737  68.832  1.00 17.24           N  
-ATOM   2056  CA  LEU A 274     -13.243  58.017  68.201  1.00 16.07           C  
-ATOM   2057  C   LEU A 274     -11.927  58.632  68.622  1.00 12.97           C  
-ATOM   2058  O   LEU A 274     -10.984  57.957  69.004  1.00 16.28           O  
-ATOM   2059  CB  LEU A 274     -13.388  57.989  66.664  1.00 19.09           C  
-ATOM   2060  CG  LEU A 274     -14.568  57.105  66.157  1.00 21.29           C  
-ATOM   2061  CD1 LEU A 274     -15.439  57.817  65.127  1.00 18.90           C  
-ATOM   2062  CD2 LEU A 274     -14.099  55.763  65.575  1.00 19.75           C  
-ATOM   2063  N   ILE A 275     -11.874  59.954  68.582  1.00  9.96           N  
-ATOM   2064  CA  ILE A 275     -10.621  60.576  68.970  1.00  9.89           C  
-ATOM   2065  C   ILE A 275     -10.229  60.260  70.403  1.00 13.55           C  
-ATOM   2066  O   ILE A 275      -9.072  59.954  70.664  1.00 17.07           O  
-ATOM   2067  CB  ILE A 275     -10.652  62.094  68.769  1.00 11.57           C  
-ATOM   2068  CG1 ILE A 275     -11.319  62.423  67.420  1.00  2.17           C  
-ATOM   2069  CG2 ILE A 275      -9.236  62.708  68.908  1.00  9.05           C  
-ATOM   2070  CD1 ILE A 275     -11.178  63.888  67.037  1.00  6.35           C  
-ATOM   2071  N   ASP A 276     -11.214  60.323  71.312  1.00 13.66           N  
-ATOM   2072  CA  ASP A 276     -10.967  60.055  72.736  1.00  9.99           C  
-ATOM   2073  C   ASP A 276     -10.209  58.755  72.987  1.00  9.78           C  
-ATOM   2074  O   ASP A 276      -9.256  58.728  73.749  1.00 15.86           O  
-ATOM   2075  CB  ASP A 276     -12.268  60.066  73.579  1.00  6.67           C  
-ATOM   2076  CG  ASP A 276     -12.935  61.437  73.832  1.00 13.34           C  
-ATOM   2077  OD1 ASP A 276     -12.247  62.466  73.816  1.00 11.05           O  
-ATOM   2078  OD2 ASP A 276     -14.149  61.465  74.080  1.00 12.50           O  
-ATOM   2079  N   VAL A 277     -10.607  57.654  72.345  1.00 10.57           N  
-ATOM   2080  CA  VAL A 277      -9.861  56.422  72.639  1.00 11.18           C  
-ATOM   2081  C   VAL A 277      -8.818  56.096  71.598  1.00  9.73           C  
-ATOM   2082  O   VAL A 277      -8.168  55.065  71.658  1.00  6.66           O  
-ATOM   2083  CB  VAL A 277     -10.844  55.258  72.819  1.00 12.00           C  
-ATOM   2084  CG1 VAL A 277     -11.716  55.499  74.059  1.00 14.32           C  
-ATOM   2085  CG2 VAL A 277     -11.750  55.051  71.604  1.00 14.63           C  
-ATOM   2086  N   GLU A 278      -8.644  56.991  70.636  1.00 13.19           N  
-ATOM   2087  CA  GLU A 278      -7.692  56.760  69.568  1.00 15.23           C  
-ATOM   2088  C   GLU A 278      -6.290  56.328  70.024  1.00 17.91           C  
-ATOM   2089  O   GLU A 278      -5.709  55.380  69.506  1.00 17.63           O  
-ATOM   2090  CB  GLU A 278      -7.666  58.018  68.686  1.00 14.05           C  
-ATOM   2091  CG  GLU A 278      -6.897  57.868  67.363  1.00 22.36           C  
-ATOM   2092  CD  GLU A 278      -6.148  59.113  66.886  1.00 24.06           C  
-ATOM   2093  OE1 GLU A 278      -6.613  60.233  67.110  1.00 17.72           O  
-ATOM   2094  OE2 GLU A 278      -5.080  58.936  66.290  1.00 29.64           O  
-ATOM   2095  N   TRP A 279      -5.748  56.995  71.039  1.00 19.53           N  
-ATOM   2096  CA  TRP A 279      -4.375  56.663  71.456  1.00 23.58           C  
-ATOM   2097  C   TRP A 279      -4.326  55.378  72.305  1.00 21.75           C  
-ATOM   2098  O   TRP A 279      -3.270  54.887  72.685  1.00 20.15           O  
-ATOM   2099  CB  TRP A 279      -3.626  57.911  72.073  1.00 27.83           C  
-ATOM   2100  CG  TRP A 279      -3.609  59.185  71.180  1.00 45.87           C  
-ATOM   2101  CD1 TRP A 279      -4.600  59.611  70.245  1.00 51.14           C  
-ATOM   2102  CD2 TRP A 279      -2.638  60.215  71.124  1.00 51.75           C  
-ATOM   2103  NE1 TRP A 279      -4.320  60.787  69.652  1.00 49.73           N  
-ATOM   2104  CE2 TRP A 279      -3.129  61.217  70.139  1.00 49.88           C  
-ATOM   2105  CE3 TRP A 279      -1.396  60.443  71.739  1.00 58.48           C  
-ATOM   2106  CZ2 TRP A 279      -2.355  62.344  69.845  1.00 52.53           C  
-ATOM   2107  CZ3 TRP A 279      -0.651  61.593  71.411  1.00 56.28           C  
-ATOM   2108  CH2 TRP A 279      -1.121  62.532  70.477  1.00 54.43           C  
-ATOM   2109  N   ASN A 280      -5.489  54.797  72.608  1.00 20.31           N  
-ATOM   2110  CA  ASN A 280      -5.433  53.582  73.429  1.00 20.08           C  
-ATOM   2111  C   ASN A 280      -5.039  52.341  72.694  1.00 22.62           C  
-ATOM   2112  O   ASN A 280      -4.460  51.425  73.248  1.00 26.63           O  
-ATOM   2113  CB  ASN A 280      -6.789  53.199  74.043  1.00 20.19           C  
-ATOM   2114  CG  ASN A 280      -7.137  54.098  75.195  1.00 24.84           C  
-ATOM   2115  OD1 ASN A 280      -6.304  54.823  75.717  1.00 25.20           O  
-ATOM   2116  ND2 ASN A 280      -8.397  54.069  75.590  1.00 28.34           N  
-ATOM   2117  N   VAL A 281      -5.380  52.275  71.420  1.00 25.56           N  
-ATOM   2118  CA  VAL A 281      -5.062  51.042  70.707  1.00 24.42           C  
-ATOM   2119  C   VAL A 281      -3.599  50.711  70.393  1.00 22.95           C  
-ATOM   2120  O   VAL A 281      -3.372  49.647  69.821  1.00 24.23           O  
-ATOM   2121  CB  VAL A 281      -5.906  51.000  69.425  1.00 25.83           C  
-ATOM   2122  CG1 VAL A 281      -7.411  51.111  69.722  1.00 27.99           C  
-ATOM   2123  CG2 VAL A 281      -5.501  52.081  68.401  1.00 30.18           C  
-ATOM   2124  N   LEU A 282      -2.624  51.588  70.698  1.00 20.87           N  
-ATOM   2125  CA  LEU A 282      -1.259  51.173  70.351  1.00 23.00           C  
-ATOM   2126  C   LEU A 282      -0.893  49.880  71.054  1.00 27.86           C  
-ATOM   2127  O   LEU A 282      -1.344  49.607  72.150  1.00 32.56           O  
-ATOM   2128  CB  LEU A 282      -0.159  52.178  70.739  1.00 21.55           C  
-ATOM   2129  CG  LEU A 282      -0.144  53.460  69.926  1.00 18.06           C  
-ATOM   2130  CD1 LEU A 282       0.864  54.445  70.504  1.00 16.80           C  
-ATOM   2131  CD2 LEU A 282       0.197  53.174  68.463  1.00 26.92           C  
-ATOM   2132  N   PRO A 283      -0.024  49.098  70.427  1.00 30.70           N  
-ATOM   2133  CA  PRO A 283       0.402  47.861  71.049  1.00 32.14           C  
-ATOM   2134  C   PRO A 283       1.517  48.007  72.090  1.00 33.95           C  
-ATOM   2135  O   PRO A 283       1.919  47.011  72.680  1.00 36.67           O  
-ATOM   2136  CB  PRO A 283       0.991  47.076  69.875  1.00 30.98           C  
-ATOM   2137  CG  PRO A 283       1.456  48.150  68.884  1.00 33.78           C  
-ATOM   2138  CD  PRO A 283       0.527  49.340  69.104  1.00 32.00           C  
-ATOM   2139  N   PHE A 284       2.073  49.210  72.301  1.00 33.22           N  
-ATOM   2140  CA  PHE A 284       3.173  49.257  73.275  1.00 33.70           C  
-ATOM   2141  C   PHE A 284       3.401  50.664  73.784  1.00 31.26           C  
-ATOM   2142  O   PHE A 284       2.904  51.640  73.250  1.00 35.29           O  
-ATOM   2143  CB  PHE A 284       4.480  48.725  72.623  1.00 37.60           C  
-ATOM   2144  CG  PHE A 284       4.800  49.364  71.288  1.00 35.44           C  
-ATOM   2145  N   ASP A 285       4.190  50.780  74.844  1.00 27.46           N  
-ATOM   2146  CA  ASP A 285       4.458  52.113  75.370  1.00 27.08           C  
-ATOM   2147  C   ASP A 285       5.465  52.645  74.399  1.00 24.63           C  
-ATOM   2148  O   ASP A 285       6.459  51.963  74.202  1.00 23.44           O  
-ATOM   2149  CB  ASP A 285       5.088  52.010  76.783  1.00 32.77           C  
-ATOM   2150  CG  ASP A 285       4.963  53.250  77.680  1.00 36.82           C  
-ATOM   2151  OD1 ASP A 285       4.601  54.334  77.200  1.00 41.07           O  
-ATOM   2152  OD2 ASP A 285       5.201  53.110  78.885  1.00 39.75           O  
-ATOM   2153  N   SER A 286       5.244  53.807  73.796  1.00 22.20           N  
-ATOM   2154  CA  SER A 286       6.287  54.187  72.865  1.00 20.31           C  
-ATOM   2155  C   SER A 286       6.190  55.639  72.579  1.00 20.85           C  
-ATOM   2156  O   SER A 286       5.215  56.291  72.907  1.00 25.15           O  
-ATOM   2157  CB  SER A 286       6.124  53.397  71.571  1.00 22.04           C  
-ATOM   2158  N   ILE A 287       7.231  56.149  71.957  1.00 20.58           N  
-ATOM   2159  CA  ILE A 287       7.316  57.542  71.600  1.00 18.81           C  
-ATOM   2160  C   ILE A 287       7.566  57.539  70.101  1.00 23.59           C  
-ATOM   2161  O   ILE A 287       8.253  56.669  69.584  1.00 23.54           O  
-ATOM   2162  CB  ILE A 287       8.386  58.168  72.526  1.00 19.40           C  
-ATOM   2163  CG1 ILE A 287       7.674  58.758  73.738  1.00 26.33           C  
-ATOM   2164  CG2 ILE A 287       9.381  59.180  71.969  1.00 12.50           C  
-ATOM   2165  CD1 ILE A 287       6.783  59.964  73.388  1.00 37.57           C  
-ATOM   2166  N   PHE A 288       6.980  58.527  69.409  1.00 22.61           N  
-ATOM   2167  CA  PHE A 288       7.142  58.613  67.965  1.00 18.77           C  
-ATOM   2168  C   PHE A 288       6.488  57.438  67.263  1.00 17.49           C  
-ATOM   2169  O   PHE A 288       7.068  56.848  66.366  1.00 18.77           O  
-ATOM   2170  CB  PHE A 288       8.626  58.732  67.524  1.00 18.74           C  
-ATOM   2171  CG  PHE A 288       8.842  59.709  66.391  1.00 20.03           C  
-ATOM   2172  CD1 PHE A 288       7.959  59.770  65.297  1.00 18.55           C  
-ATOM   2173  CD2 PHE A 288       9.937  60.591  66.439  1.00 20.66           C  
-ATOM   2174  CE1 PHE A 288       8.162  60.724  64.286  1.00 21.85           C  
-ATOM   2175  CE2 PHE A 288      10.152  61.527  65.417  1.00 18.68           C  
-ATOM   2176  CZ  PHE A 288       9.258  61.601  64.342  1.00 18.73           C  
-ATOM   2177  N   ARG A 289       5.281  57.080  67.706  1.00 13.71           N  
-ATOM   2178  CA  ARG A 289       4.589  55.990  67.040  1.00 10.97           C  
-ATOM   2179  C   ARG A 289       3.133  56.446  67.008  1.00 13.17           C  
-ATOM   2180  O   ARG A 289       2.672  57.044  67.976  1.00 15.46           O  
-ATOM   2181  CB  ARG A 289       4.870  54.676  67.752  1.00  7.32           C  
-ATOM   2182  CG  ARG A 289       5.166  53.550  66.761  1.00 10.17           C  
-ATOM   2183  CD  ARG A 289       6.592  52.986  66.804  1.00  8.16           C  
-ATOM   2184  NE  ARG A 289       7.610  53.993  66.528  1.00  6.44           N  
-ATOM   2185  CZ  ARG A 289       8.888  53.619  66.311  1.00  7.30           C  
-ATOM   2186  NH1 ARG A 289       9.265  52.332  66.314  1.00  9.32           N  
-ATOM   2187  NH2 ARG A 289       9.799  54.549  66.100  1.00  2.00           N  
-ATOM   2188  N   PHE A 290       2.423  56.202  65.890  1.00 13.80           N  
-ATOM   2189  CA  PHE A 290       1.030  56.669  65.753  1.00  7.02           C  
-ATOM   2190  C   PHE A 290       0.166  55.475  65.563  1.00  7.77           C  
-ATOM   2191  O   PHE A 290       0.620  54.426  65.140  1.00  8.78           O  
-ATOM   2192  CB  PHE A 290       0.930  57.706  64.649  1.00  5.39           C  
-ATOM   2193  CG  PHE A 290       2.049  58.697  64.835  1.00  6.71           C  
-ATOM   2194  CD1 PHE A 290       2.069  59.518  65.980  1.00  9.75           C  
-ATOM   2195  CD2 PHE A 290       3.094  58.785  63.908  1.00  5.00           C  
-ATOM   2196  CE1 PHE A 290       3.123  60.416  66.204  1.00 12.99           C  
-ATOM   2197  CE2 PHE A 290       4.152  59.683  64.134  1.00 15.40           C  
-ATOM   2198  CZ  PHE A 290       4.175  60.502  65.278  1.00 13.61           C  
-ATOM   2199  N   SER A 291      -1.106  55.638  65.857  1.00  8.32           N  
-ATOM   2200  CA  SER A 291      -1.972  54.462  65.823  1.00 16.13           C  
-ATOM   2201  C   SER A 291      -2.512  54.045  64.482  1.00 17.73           C  
-ATOM   2202  O   SER A 291      -2.336  52.912  64.051  1.00 20.12           O  
-ATOM   2203  CB  SER A 291      -3.099  54.609  66.872  1.00 19.54           C  
-ATOM   2204  OG  SER A 291      -3.357  56.010  67.071  1.00 33.63           O  
-ATOM   2205  N   PHE A 292      -3.239  54.985  63.879  1.00 17.03           N  
-ATOM   2206  CA  PHE A 292      -3.854  54.779  62.570  1.00 16.67           C  
-ATOM   2207  C   PHE A 292      -2.927  55.452  61.567  1.00 16.80           C  
-ATOM   2208  O   PHE A 292      -2.770  56.670  61.518  1.00 15.50           O  
-ATOM   2209  CB  PHE A 292      -5.270  55.372  62.539  1.00 17.52           C  
-ATOM   2210  CG  PHE A 292      -6.134  54.657  63.543  1.00 17.08           C  
-ATOM   2211  CD1 PHE A 292      -6.500  53.322  63.309  1.00 15.40           C  
-ATOM   2212  CD2 PHE A 292      -6.550  55.293  64.726  1.00 18.33           C  
-ATOM   2213  CE1 PHE A 292      -7.267  52.620  64.249  1.00 18.53           C  
-ATOM   2214  CE2 PHE A 292      -7.321  54.589  65.666  1.00 17.40           C  
-ATOM   2215  CZ  PHE A 292      -7.677  53.255  65.429  1.00 14.64           C  
-ATOM   2216  N   VAL A 293      -2.289  54.601  60.776  1.00 12.34           N  
-ATOM   2217  CA  VAL A 293      -1.336  55.080  59.827  1.00  8.67           C  
-ATOM   2218  C   VAL A 293      -1.555  54.254  58.525  1.00 12.18           C  
-ATOM   2219  O   VAL A 293      -2.342  53.305  58.560  1.00 16.80           O  
-ATOM   2220  CB  VAL A 293      -0.041  54.883  60.652  1.00  4.33           C  
-ATOM   2221  CG1 VAL A 293       0.600  53.521  60.414  1.00  2.00           C  
-ATOM   2222  CG2 VAL A 293       0.897  56.091  60.681  1.00  2.00           C  
-ATOM   2223  N   PRO A 294      -0.904  54.629  57.388  1.00  9.30           N  
-ATOM   2224  CA  PRO A 294      -0.938  53.815  56.186  1.00  8.79           C  
-ATOM   2225  C   PRO A 294      -0.599  52.352  56.371  1.00 10.50           C  
-ATOM   2226  O   PRO A 294       0.323  51.972  57.076  1.00  9.56           O  
-ATOM   2227  CB  PRO A 294       0.094  54.478  55.268  1.00  6.80           C  
-ATOM   2228  CG  PRO A 294       0.162  55.948  55.710  1.00  6.81           C  
-ATOM   2229  CD  PRO A 294      -0.242  55.919  57.186  1.00  9.07           C  
-ATOM   2230  N   VAL A 295      -1.359  51.520  55.684  1.00 11.41           N  
-ATOM   2231  CA  VAL A 295      -1.144  50.105  55.753  1.00 11.66           C  
-ATOM   2232  C   VAL A 295      -0.563  49.626  54.426  1.00 11.36           C  
-ATOM   2233  O   VAL A 295      -0.921  50.100  53.345  1.00 15.72           O  
-ATOM   2234  CB  VAL A 295      -2.500  49.475  56.064  1.00 11.25           C  
-ATOM   2235  CG1 VAL A 295      -3.536  49.665  54.957  1.00 11.82           C  
-ATOM   2236  CG2 VAL A 295      -2.383  48.012  56.439  1.00 13.92           C  
-ATOM   2237  N   ILE A 296       0.332  48.650  54.494  1.00  7.67           N  
-ATOM   2238  CA  ILE A 296       0.909  48.108  53.269  1.00  9.07           C  
-ATOM   2239  C   ILE A 296      -0.113  47.067  52.819  1.00 13.22           C  
-ATOM   2240  O   ILE A 296      -0.081  45.901  53.170  1.00 16.51           O  
-ATOM   2241  CB  ILE A 296       2.320  47.588  53.556  1.00  3.19           C  
-ATOM   2242  CG1 ILE A 296       3.177  48.649  54.284  1.00  7.61           C  
-ATOM   2243  CG2 ILE A 296       3.046  47.123  52.298  1.00  9.21           C  
-ATOM   2244  CD1 ILE A 296       3.414  49.937  53.482  1.00  2.00           C  
-ATOM   2245  N   ASP A 297      -1.079  47.551  52.048  1.00 17.57           N  
-ATOM   2246  CA  ASP A 297      -2.187  46.710  51.598  1.00 18.19           C  
-ATOM   2247  C   ASP A 297      -2.087  45.968  50.305  1.00 18.63           C  
-ATOM   2248  O   ASP A 297      -3.040  45.291  49.965  1.00 20.40           O  
-ATOM   2249  CB  ASP A 297      -3.443  47.587  51.441  1.00 21.53           C  
-ATOM   2250  CG  ASP A 297      -3.249  48.707  50.408  1.00 25.52           C  
-ATOM   2251  OD1 ASP A 297      -2.118  48.919  49.965  1.00 25.27           O  
-ATOM   2252  OD2 ASP A 297      -4.229  49.360  50.045  1.00 30.02           O  
-ATOM   2253  N   GLY A 298      -1.035  46.149  49.527  1.00 19.76           N  
-ATOM   2254  CA  GLY A 298      -1.012  45.399  48.265  1.00 20.13           C  
-ATOM   2255  C   GLY A 298      -1.680  46.119  47.101  1.00 21.29           C  
-ATOM   2256  O   GLY A 298      -1.650  45.683  45.964  1.00 21.74           O  
-ATOM   2257  N   GLU A 299      -2.354  47.242  47.391  1.00 24.12           N  
-ATOM   2258  CA  GLU A 299      -2.987  48.004  46.305  1.00 25.75           C  
-ATOM   2259  C   GLU A 299      -2.149  49.253  46.134  1.00 24.40           C  
-ATOM   2260  O   GLU A 299      -1.330  49.372  45.239  1.00 26.48           O  
-ATOM   2261  CB  GLU A 299      -4.484  48.325  46.503  1.00 25.83           C  
-ATOM   2262  CG  GLU A 299      -5.398  47.079  46.580  1.00 32.58           C  
-ATOM   2263  N   PHE A 300      -2.350  50.184  47.083  1.00 18.19           N  
-ATOM   2264  CA  PHE A 300      -1.590  51.437  47.050  1.00 12.45           C  
-ATOM   2265  C   PHE A 300      -0.093  51.132  46.920  1.00 11.34           C  
-ATOM   2266  O   PHE A 300       0.658  51.681  46.131  1.00 13.48           O  
-ATOM   2267  CB  PHE A 300      -1.975  52.258  48.291  1.00  7.90           C  
-ATOM   2268  CG  PHE A 300      -1.758  53.743  48.144  1.00  2.53           C  
-ATOM   2269  CD1 PHE A 300      -0.450  54.264  48.217  1.00  2.00           C  
-ATOM   2270  CD2 PHE A 300      -2.854  54.617  47.978  1.00  2.00           C  
-ATOM   2271  CE1 PHE A 300      -0.238  55.646  48.138  1.00  2.00           C  
-ATOM   2272  CE2 PHE A 300      -2.636  56.001  47.897  1.00  2.42           C  
-ATOM   2273  CZ  PHE A 300      -1.329  56.516  47.975  1.00  2.00           C  
-ATOM   2274  N   PHE A 301       0.338  50.182  47.740  1.00 13.91           N  
-ATOM   2275  CA  PHE A 301       1.728  49.748  47.685  1.00 16.40           C  
-ATOM   2276  C   PHE A 301       1.552  48.355  47.154  1.00 17.78           C  
-ATOM   2277  O   PHE A 301       0.813  47.606  47.779  1.00 18.74           O  
-ATOM   2278  CB  PHE A 301       2.442  49.680  49.055  1.00 12.10           C  
-ATOM   2279  CG  PHE A 301       2.334  50.999  49.759  1.00  8.05           C  
-ATOM   2280  CD1 PHE A 301       3.190  52.053  49.410  1.00  8.60           C  
-ATOM   2281  CD2 PHE A 301       1.335  51.199  50.731  1.00  7.13           C  
-ATOM   2282  CE1 PHE A 301       3.033  53.309  50.021  1.00 11.99           C  
-ATOM   2283  CE2 PHE A 301       1.180  52.448  51.337  1.00  7.18           C  
-ATOM   2284  CZ  PHE A 301       2.027  53.509  50.983  1.00  6.39           C  
-ATOM   2285  N   PRO A 302       2.178  48.011  46.027  1.00 22.94           N  
-ATOM   2286  CA  PRO A 302       2.077  46.642  45.548  1.00 24.21           C  
-ATOM   2287  C   PRO A 302       2.809  45.660  46.448  1.00 26.54           C  
-ATOM   2288  O   PRO A 302       2.337  44.569  46.749  1.00 30.30           O  
-ATOM   2289  CB  PRO A 302       2.681  46.708  44.135  1.00 22.95           C  
-ATOM   2290  CG  PRO A 302       3.442  48.048  44.018  1.00 21.28           C  
-ATOM   2291  CD  PRO A 302       2.862  48.938  45.116  1.00 25.04           C  
-ATOM   2292  N   THR A 303       4.011  46.070  46.872  1.00 24.95           N  
-ATOM   2293  CA  THR A 303       4.819  45.204  47.717  1.00 23.35           C  
-ATOM   2294  C   THR A 303       5.359  46.023  48.858  1.00 21.75           C  
-ATOM   2295  O   THR A 303       5.061  47.188  49.080  1.00 22.57           O  
-ATOM   2296  CB  THR A 303       5.960  44.619  46.857  1.00 24.02           C  
-ATOM   2297  OG1 THR A 303       5.373  44.118  45.672  1.00 35.66           O  
-ATOM   2298  CG2 THR A 303       6.781  43.426  47.395  1.00 32.95           C  
-ATOM   2299  N   SER A 304       6.179  45.353  49.634  1.00 19.64           N  
-ATOM   2300  CA  SER A 304       6.777  46.036  50.737  1.00 22.00           C  
-ATOM   2301  C   SER A 304       7.647  47.171  50.223  1.00 20.40           C  
-ATOM   2302  O   SER A 304       8.325  47.026  49.214  1.00 21.63           O  
-ATOM   2303  CB  SER A 304       7.617  45.022  51.523  1.00 25.76           C  
-ATOM   2304  OG  SER A 304       8.746  44.583  50.764  1.00 28.88           O  
-ATOM   2305  N   LEU A 305       7.668  48.268  50.974  1.00 17.53           N  
-ATOM   2306  CA  LEU A 305       8.469  49.379  50.532  1.00 16.57           C  
-ATOM   2307  C   LEU A 305       9.931  49.020  50.352  1.00 19.69           C  
-ATOM   2308  O   LEU A 305      10.656  49.623  49.579  1.00 24.75           O  
-ATOM   2309  CB  LEU A 305       8.384  50.527  51.537  1.00 12.69           C  
-ATOM   2310  CG  LEU A 305       6.978  50.885  52.035  1.00 13.00           C  
-ATOM   2311  CD1 LEU A 305       7.040  52.244  52.743  1.00 15.70           C  
-ATOM   2312  CD2 LEU A 305       5.920  50.939  50.919  1.00 16.88           C  
-ATOM   2313  N   GLU A 306      10.385  48.013  51.088  1.00 21.26           N  
-ATOM   2314  CA  GLU A 306      11.788  47.694  50.939  1.00 23.53           C  
-ATOM   2315  C   GLU A 306      12.068  47.065  49.589  1.00 26.40           C  
-ATOM   2316  O   GLU A 306      13.099  47.362  48.988  1.00 26.99           O  
-ATOM   2317  CB  GLU A 306      12.304  46.861  52.115  1.00 27.54           C  
-ATOM   2318  CG  GLU A 306      13.848  46.784  52.138  1.00 36.12           C  
-ATOM   2319  CD  GLU A 306      14.553  48.135  52.349  1.00 42.13           C  
-ATOM   2320  OE1 GLU A 306      13.897  49.103  52.749  1.00 48.53           O  
-ATOM   2321  OE2 GLU A 306      15.763  48.207  52.113  1.00 41.09           O  
-ATOM   2322  N   SER A 307      11.155  46.186  49.122  1.00 24.56           N  
-ATOM   2323  CA  SER A 307      11.386  45.608  47.794  1.00 23.34           C  
-ATOM   2324  C   SER A 307      11.332  46.696  46.751  1.00 22.27           C  
-ATOM   2325  O   SER A 307      12.171  46.808  45.879  1.00 25.50           O  
-ATOM   2326  CB  SER A 307      10.291  44.624  47.401  1.00 25.32           C  
-ATOM   2327  OG  SER A 307      10.486  43.433  48.131  1.00 35.53           O  
-ATOM   2328  N   MET A 308      10.309  47.540  46.867  1.00 18.81           N  
-ATOM   2329  CA  MET A 308      10.191  48.616  45.913  1.00 14.66           C  
-ATOM   2330  C   MET A 308      11.475  49.436  45.845  1.00 16.78           C  
-ATOM   2331  O   MET A 308      12.003  49.676  44.766  1.00 18.54           O  
-ATOM   2332  CB  MET A 308       8.931  49.437  46.194  1.00 10.18           C  
-ATOM   2333  CG  MET A 308       7.683  48.546  46.106  1.00  9.23           C  
-ATOM   2334  SD  MET A 308       6.168  49.530  46.289  1.00 18.45           S  
-ATOM   2335  CE  MET A 308       6.091  50.363  44.685  1.00 12.01           C  
-ATOM   2336  N   LEU A 309      11.991  49.825  47.011  1.00 16.99           N  
-ATOM   2337  CA  LEU A 309      13.222  50.592  46.993  1.00 17.95           C  
-ATOM   2338  C   LEU A 309      14.345  49.795  46.357  1.00 17.65           C  
-ATOM   2339  O   LEU A 309      15.151  50.301  45.592  1.00 16.10           O  
-ATOM   2340  CB  LEU A 309      13.666  51.032  48.407  1.00 17.08           C  
-ATOM   2341  CG  LEU A 309      12.687  52.013  49.072  1.00 19.36           C  
-ATOM   2342  CD1 LEU A 309      12.952  52.089  50.571  1.00 21.60           C  
-ATOM   2343  CD2 LEU A 309      12.728  53.417  48.462  1.00 21.39           C  
-ATOM   2344  N   ASN A 310      14.386  48.511  46.680  1.00 21.00           N  
-ATOM   2345  CA  ASN A 310      15.469  47.696  46.131  1.00 24.25           C  
-ATOM   2346  C   ASN A 310      15.341  47.420  44.651  1.00 23.67           C  
-ATOM   2347  O   ASN A 310      16.341  47.175  43.994  1.00 28.49           O  
-ATOM   2348  CB  ASN A 310      15.643  46.361  46.879  1.00 22.68           C  
-ATOM   2349  N   SER A 311      14.126  47.470  44.120  1.00 22.33           N  
-ATOM   2350  CA  SER A 311      13.956  47.185  42.700  1.00 20.64           C  
-ATOM   2351  C   SER A 311      13.793  48.386  41.819  1.00 19.56           C  
-ATOM   2352  O   SER A 311      13.630  48.256  40.625  1.00 23.99           O  
-ATOM   2353  CB  SER A 311      12.680  46.370  42.501  1.00 17.52           C  
-ATOM   2354  OG  SER A 311      12.759  45.201  43.314  1.00 28.32           O  
-ATOM   2355  N   GLY A 312      13.792  49.586  42.366  1.00 22.66           N  
-ATOM   2356  CA  GLY A 312      13.590  50.708  41.450  1.00 16.05           C  
-ATOM   2357  C   GLY A 312      12.176  50.853  41.018  1.00 15.93           C  
-ATOM   2358  O   GLY A 312      11.823  51.512  40.050  1.00 16.26           O  
-ATOM   2359  N   ASN A 313      11.317  50.212  41.788  1.00 13.55           N  
-ATOM   2360  CA  ASN A 313       9.934  50.273  41.428  1.00 12.79           C  
-ATOM   2361  C   ASN A 313       9.345  51.562  41.939  1.00 14.18           C  
-ATOM   2362  O   ASN A 313       8.511  51.543  42.827  1.00 17.05           O  
-ATOM   2363  CB  ASN A 313       9.246  49.058  42.036  1.00  9.57           C  
-ATOM   2364  CG  ASN A 313       7.795  48.867  41.661  1.00  9.15           C  
-ATOM   2365  OD1 ASN A 313       7.154  47.935  42.126  1.00 17.83           O  
-ATOM   2366  ND2 ASN A 313       7.261  49.725  40.809  1.00  7.64           N  
-ATOM   2367  N   PHE A 314       9.769  52.687  41.365  1.00 12.17           N  
-ATOM   2368  CA  PHE A 314       9.246  53.960  41.811  1.00 11.47           C  
-ATOM   2369  C   PHE A 314       9.491  55.002  40.742  1.00  9.09           C  
-ATOM   2370  O   PHE A 314      10.292  54.813  39.841  1.00 11.88           O  
-ATOM   2371  CB  PHE A 314       9.927  54.378  43.142  1.00  8.27           C  
-ATOM   2372  CG  PHE A 314      11.439  54.212  43.190  1.00  5.34           C  
-ATOM   2373  CD1 PHE A 314      12.275  55.125  42.522  1.00  5.50           C  
-ATOM   2374  CD2 PHE A 314      12.032  53.161  43.921  1.00  6.88           C  
-ATOM   2375  CE1 PHE A 314      13.670  55.013  42.589  1.00  5.64           C  
-ATOM   2376  CE2 PHE A 314      13.434  53.046  43.990  1.00  6.23           C  
-ATOM   2377  CZ  PHE A 314      14.252  53.974  43.326  1.00  8.11           C  
-ATOM   2378  N   LYS A 315       8.780  56.117  40.865  1.00  6.19           N  
-ATOM   2379  CA  LYS A 315       8.949  57.212  39.930  1.00  5.55           C  
-ATOM   2380  C   LYS A 315      10.401  57.689  39.991  1.00  8.59           C  
-ATOM   2381  O   LYS A 315      10.940  57.798  41.078  1.00 11.14           O  
-ATOM   2382  CB  LYS A 315       8.034  58.359  40.375  1.00  2.00           C  
-ATOM   2383  CG  LYS A 315       7.791  59.418  39.309  1.00  2.00           C  
-ATOM   2384  CD  LYS A 315       6.984  60.602  39.844  1.00  5.62           C  
-ATOM   2385  CE  LYS A 315       7.012  61.841  38.941  1.00  2.23           C  
-ATOM   2386  NZ  LYS A 315       6.314  61.584  37.702  1.00  7.21           N  
-ATOM   2387  N   LYS A 316      11.009  57.995  38.832  1.00 11.74           N  
-ATOM   2388  CA  LYS A 316      12.404  58.456  38.780  1.00 11.54           C  
-ATOM   2389  C   LYS A 316      12.451  59.858  38.240  1.00 13.56           C  
-ATOM   2390  O   LYS A 316      12.348  60.074  37.049  1.00 20.69           O  
-ATOM   2391  CB  LYS A 316      13.171  57.521  37.864  1.00  8.26           C  
-ATOM   2392  CG  LYS A 316      13.127  56.119  38.485  1.00 16.81           C  
-ATOM   2393  CD  LYS A 316      13.289  54.969  37.505  1.00 20.85           C  
-ATOM   2394  CE  LYS A 316      12.902  53.663  38.201  1.00 26.47           C  
-ATOM   2395  NZ  LYS A 316      13.286  52.521  37.401  1.00 38.01           N  
-ATOM   2396  N   THR A 317      12.594  60.814  39.134  1.00 14.01           N  
-ATOM   2397  CA  THR A 317      12.652  62.244  38.864  1.00  9.79           C  
-ATOM   2398  C   THR A 317      13.686  62.692  39.841  1.00 10.09           C  
-ATOM   2399  O   THR A 317      14.387  61.834  40.377  1.00 14.11           O  
-ATOM   2400  CB  THR A 317      11.268  62.826  39.158  1.00  8.40           C  
-ATOM   2401  OG1 THR A 317      11.163  64.217  38.919  1.00  3.20           O  
-ATOM   2402  CG2 THR A 317      10.726  62.508  40.561  1.00 13.38           C  
-ATOM   2403  N   GLN A 318      13.803  63.988  40.092  1.00  6.37           N  
-ATOM   2404  CA  GLN A 318      14.777  64.420  41.073  1.00 12.87           C  
-ATOM   2405  C   GLN A 318      13.988  64.827  42.278  1.00 14.14           C  
-ATOM   2406  O   GLN A 318      12.856  65.269  42.127  1.00 16.56           O  
-ATOM   2407  CB  GLN A 318      15.678  65.574  40.599  1.00 15.58           C  
-ATOM   2408  CG  GLN A 318      14.988  66.667  39.762  1.00 19.31           C  
-ATOM   2409  CD  GLN A 318      14.540  66.130  38.419  1.00 22.16           C  
-ATOM   2410  OE1 GLN A 318      13.369  66.144  38.104  1.00 23.76           O  
-ATOM   2411  NE2 GLN A 318      15.466  65.585  37.653  1.00 23.65           N  
-ATOM   2412  N   ILE A 319      14.601  64.668  43.460  1.00 14.51           N  
-ATOM   2413  CA  ILE A 319      13.962  65.028  44.715  1.00 13.89           C  
-ATOM   2414  C   ILE A 319      14.935  65.892  45.481  1.00 13.76           C  
-ATOM   2415  O   ILE A 319      16.143  65.848  45.224  1.00 15.41           O  
-ATOM   2416  CB  ILE A 319      13.606  63.764  45.533  1.00  8.68           C  
-ATOM   2417  CG1 ILE A 319      14.810  62.833  45.701  1.00  9.47           C  
-ATOM   2418  CG2 ILE A 319      12.439  63.029  44.879  1.00  8.02           C  
-ATOM   2419  CD1 ILE A 319      14.535  61.645  46.616  1.00 10.02           C  
-ATOM   2420  N   LEU A 320      14.374  66.653  46.433  1.00 12.95           N  
-ATOM   2421  CA  LEU A 320      15.133  67.534  47.325  1.00 13.55           C  
-ATOM   2422  C   LEU A 320      14.604  67.179  48.708  1.00 16.92           C  
-ATOM   2423  O   LEU A 320      13.402  67.300  48.938  1.00 17.93           O  
-ATOM   2424  CB  LEU A 320      14.885  68.995  46.946  1.00 10.04           C  
-ATOM   2425  CG  LEU A 320      15.616  70.015  47.806  1.00  2.89           C  
-ATOM   2426  CD1 LEU A 320      15.902  71.283  46.999  1.00  2.00           C  
-ATOM   2427  CD2 LEU A 320      14.777  70.365  49.034  1.00  2.00           C  
-ATOM   2428  N   LEU A 321      15.471  66.724  49.628  1.00 19.13           N  
-ATOM   2429  CA  LEU A 321      14.983  66.334  50.959  1.00 20.76           C  
-ATOM   2430  C   LEU A 321      15.948  66.716  52.073  1.00 21.85           C  
-ATOM   2431  O   LEU A 321      17.080  67.123  51.823  1.00 21.77           O  
-ATOM   2432  CB  LEU A 321      14.567  64.848  50.994  1.00 13.85           C  
-ATOM   2433  CG  LEU A 321      15.662  63.771  50.878  1.00 10.01           C  
-ATOM   2434  CD1 LEU A 321      14.969  62.419  50.669  1.00 14.33           C  
-ATOM   2435  CD2 LEU A 321      16.697  64.033  49.786  1.00 12.34           C  
-ATOM   2436  N   GLY A 322      15.474  66.606  53.323  1.00 20.68           N  
-ATOM   2437  CA  GLY A 322      16.364  66.975  54.413  1.00 21.02           C  
-ATOM   2438  C   GLY A 322      15.837  66.670  55.788  1.00 20.39           C  
-ATOM   2439  O   GLY A 322      14.748  66.148  56.012  1.00 17.65           O  
-ATOM   2440  N   VAL A 323      16.676  67.039  56.737  1.00 19.21           N  
-ATOM   2441  CA  VAL A 323      16.454  66.802  58.135  1.00 16.39           C  
-ATOM   2442  C   VAL A 323      16.833  68.060  58.918  1.00 18.43           C  
-ATOM   2443  O   VAL A 323      17.569  68.917  58.453  1.00 21.23           O  
-ATOM   2444  CB  VAL A 323      17.385  65.595  58.390  1.00 13.97           C  
-ATOM   2445  CG1 VAL A 323      18.247  65.660  59.636  1.00 22.44           C  
-ATOM   2446  CG2 VAL A 323      16.668  64.246  58.256  1.00 12.08           C  
-ATOM   2447  N   ASN A 324      16.312  68.130  60.140  1.00 19.64           N  
-ATOM   2448  CA  ASN A 324      16.576  69.232  61.065  1.00 20.25           C  
-ATOM   2449  C   ASN A 324      17.483  68.638  62.123  1.00 18.45           C  
-ATOM   2450  O   ASN A 324      17.417  67.451  62.429  1.00 17.84           O  
-ATOM   2451  CB  ASN A 324      15.325  69.717  61.812  1.00 22.56           C  
-ATOM   2452  CG  ASN A 324      14.487  70.641  60.991  1.00 27.51           C  
-ATOM   2453  OD1 ASN A 324      14.739  70.895  59.826  1.00 37.47           O  
-ATOM   2454  ND2 ASN A 324      13.440  71.163  61.614  1.00 29.83           N  
-ATOM   2455  N   LYS A 325      18.277  69.490  62.736  1.00 16.85           N  
-ATOM   2456  CA  LYS A 325      19.209  69.004  63.749  1.00 18.86           C  
-ATOM   2457  C   LYS A 325      18.633  68.269  64.972  1.00 19.76           C  
-ATOM   2458  O   LYS A 325      19.155  67.238  65.376  1.00 22.32           O  
-ATOM   2459  CB  LYS A 325      20.041  70.206  64.203  1.00 19.84           C  
-ATOM   2460  CG  LYS A 325      21.235  69.913  65.106  1.00 18.37           C  
-ATOM   2461  CD  LYS A 325      21.879  71.216  65.602  1.00 23.69           C  
-ATOM   2462  CE  LYS A 325      22.953  70.945  66.686  1.00 31.93           C  
-ATOM   2463  N   ASP A 326      17.564  68.800  65.589  1.00 19.00           N  
-ATOM   2464  CA  ASP A 326      16.997  68.168  66.786  1.00 15.13           C  
-ATOM   2465  C   ASP A 326      15.582  67.685  66.541  1.00 15.41           C  
-ATOM   2466  O   ASP A 326      14.554  68.246  66.915  1.00 17.38           O  
-ATOM   2467  CB  ASP A 326      17.045  69.147  67.964  1.00 14.86           C  
-ATOM   2468  CG  ASP A 326      18.481  69.585  68.202  1.00 15.21           C  
-ATOM   2469  OD1 ASP A 326      19.246  68.787  68.744  1.00 12.30           O  
-ATOM   2470  OD2 ASP A 326      18.837  70.705  67.836  1.00 17.21           O  
-ATOM   2471  N   GLU A 327      15.548  66.544  65.869  1.00 15.52           N  
-ATOM   2472  CA  GLU A 327      14.229  66.004  65.564  1.00 13.42           C  
-ATOM   2473  C   GLU A 327      13.532  65.379  66.751  1.00 10.57           C  
-ATOM   2474  O   GLU A 327      12.316  65.300  66.771  1.00  9.81           O  
-ATOM   2475  CB  GLU A 327      14.333  64.889  64.496  1.00 17.15           C  
-ATOM   2476  CG  GLU A 327      14.964  65.334  63.166  1.00 18.52           C  
-ATOM   2477  CD  GLU A 327      13.970  66.056  62.282  1.00 19.62           C  
-ATOM   2478  OE1 GLU A 327      12.931  66.484  62.781  1.00 21.93           O  
-ATOM   2479  OE2 GLU A 327      14.237  66.179  61.090  1.00 16.45           O  
-ATOM   2480  N   GLY A 328      14.326  64.899  67.718  1.00 11.45           N  
-ATOM   2481  CA  GLY A 328      13.742  64.223  68.891  1.00  9.29           C  
-ATOM   2482  C   GLY A 328      13.019  65.075  69.925  1.00  5.98           C  
-ATOM   2483  O   GLY A 328      11.947  64.733  70.402  1.00  5.07           O  
-ATOM   2484  N   SER A 329      13.605  66.213  70.250  1.00  4.05           N  
-ATOM   2485  CA  SER A 329      13.070  67.137  71.237  1.00  6.39           C  
-ATOM   2486  C   SER A 329      11.602  67.111  71.523  1.00  9.36           C  
-ATOM   2487  O   SER A 329      11.178  66.831  72.631  1.00 15.58           O  
-ATOM   2488  CB  SER A 329      13.402  68.587  70.876  1.00  4.71           C  
-ATOM   2489  OG  SER A 329      14.743  68.550  70.442  1.00 15.15           O  
-ATOM   2490  N   PHE A 330      10.831  67.435  70.503  1.00 10.03           N  
-ATOM   2491  CA  PHE A 330       9.388  67.504  70.670  1.00  9.24           C  
-ATOM   2492  C   PHE A 330       8.801  66.222  71.233  1.00 11.37           C  
-ATOM   2493  O   PHE A 330       7.995  66.250  72.151  1.00 14.67           O  
-ATOM   2494  CB  PHE A 330       8.797  67.941  69.310  1.00  9.90           C  
-ATOM   2495  CG  PHE A 330       7.361  67.570  69.090  1.00  5.23           C  
-ATOM   2496  CD1 PHE A 330       6.355  68.074  69.932  1.00  7.49           C  
-ATOM   2497  CD2 PHE A 330       7.029  66.699  68.050  1.00  2.00           C  
-ATOM   2498  CE1 PHE A 330       5.016  67.694  69.746  1.00  5.45           C  
-ATOM   2499  CE2 PHE A 330       5.702  66.309  67.869  1.00  6.92           C  
-ATOM   2500  CZ  PHE A 330       4.692  66.803  68.719  1.00  7.06           C  
-ATOM   2501  N   PHE A 331       9.253  65.093  70.703  1.00 10.22           N  
-ATOM   2502  CA  PHE A 331       8.704  63.827  71.186  1.00  9.49           C  
-ATOM   2503  C   PHE A 331       9.104  63.550  72.605  1.00 10.53           C  
-ATOM   2504  O   PHE A 331       8.302  63.082  73.401  1.00 18.03           O  
-ATOM   2505  CB  PHE A 331       9.108  62.653  70.283  1.00  5.51           C  
-ATOM   2506  CG  PHE A 331       8.718  62.957  68.870  1.00  7.87           C  
-ATOM   2507  CD1 PHE A 331       9.586  63.696  68.044  1.00  9.94           C  
-ATOM   2508  CD2 PHE A 331       7.436  62.607  68.414  1.00  7.15           C  
-ATOM   2509  CE1 PHE A 331       9.155  64.126  66.787  1.00  9.44           C  
-ATOM   2510  CE2 PHE A 331       7.007  63.035  67.154  1.00  9.46           C  
-ATOM   2511  CZ  PHE A 331       7.863  63.800  66.344  1.00 11.59           C  
-ATOM   2512  N   LEU A 332      10.375  63.847  72.918  1.00  9.05           N  
-ATOM   2513  CA  LEU A 332      10.840  63.607  74.285  1.00  7.07           C  
-ATOM   2514  C   LEU A 332      10.027  64.468  75.245  1.00  7.31           C  
-ATOM   2515  O   LEU A 332       9.320  63.979  76.117  1.00  5.40           O  
-ATOM   2516  CB  LEU A 332      12.349  63.825  74.423  1.00  2.00           C  
-ATOM   2517  CG  LEU A 332      13.172  62.733  73.743  1.00  2.00           C  
-ATOM   2518  CD1 LEU A 332      14.622  63.164  73.595  1.00  2.00           C  
-ATOM   2519  CD2 LEU A 332      13.094  61.403  74.488  1.00  2.00           C  
-ATOM   2520  N   LEU A 333      10.102  65.774  75.008  1.00  4.82           N  
-ATOM   2521  CA  LEU A 333       9.359  66.732  75.799  1.00  4.67           C  
-ATOM   2522  C   LEU A 333       7.899  66.344  76.002  1.00  6.42           C  
-ATOM   2523  O   LEU A 333       7.330  66.523  77.071  1.00 13.53           O  
-ATOM   2524  CB  LEU A 333       9.460  68.073  75.079  1.00  6.73           C  
-ATOM   2525  CG  LEU A 333       8.757  69.310  75.682  1.00  8.90           C  
-ATOM   2526  CD1 LEU A 333       7.382  69.539  75.101  1.00  9.01           C  
-ATOM   2527  CD2 LEU A 333       8.713  69.365  77.212  1.00 12.87           C  
-ATOM   2528  N   TYR A 334       7.280  65.785  74.975  1.00  6.07           N  
-ATOM   2529  CA  TYR A 334       5.871  65.437  75.152  1.00  6.57           C  
-ATOM   2530  C   TYR A 334       5.629  64.108  75.786  1.00  6.32           C  
-ATOM   2531  O   TYR A 334       4.517  63.901  76.249  1.00  8.62           O  
-ATOM   2532  CB  TYR A 334       5.054  65.477  73.835  1.00  5.74           C  
-ATOM   2533  CG  TYR A 334       4.521  66.852  73.512  1.00  2.00           C  
-ATOM   2534  CD1 TYR A 334       5.409  67.907  73.254  1.00  2.00           C  
-ATOM   2535  CD2 TYR A 334       3.137  67.079  73.460  1.00  2.00           C  
-ATOM   2536  CE1 TYR A 334       4.912  69.181  72.946  1.00  5.08           C  
-ATOM   2537  CE2 TYR A 334       2.633  68.349  73.155  1.00  2.00           C  
-ATOM   2538  CZ  TYR A 334       3.521  69.399  72.890  1.00  4.53           C  
-ATOM   2539  OH  TYR A 334       3.049  70.651  72.554  1.00 11.53           O  
-ATOM   2540  N   GLY A 335       6.595  63.194  75.819  1.00  6.87           N  
-ATOM   2541  CA  GLY A 335       6.176  61.960  76.480  1.00  7.35           C  
-ATOM   2542  C   GLY A 335       7.252  61.095  77.070  1.00  9.23           C  
-ATOM   2543  O   GLY A 335       7.053  59.912  77.296  1.00  7.96           O  
-ATOM   2544  N   ALA A 336       8.413  61.661  77.332  1.00 10.09           N  
-ATOM   2545  CA  ALA A 336       9.487  60.899  77.920  1.00 11.90           C  
-ATOM   2546  C   ALA A 336       9.673  61.485  79.315  1.00 15.96           C  
-ATOM   2547  O   ALA A 336       9.580  62.702  79.500  1.00 18.28           O  
-ATOM   2548  CB  ALA A 336      10.768  61.057  77.107  1.00 15.83           C  
-ATOM   2549  N   PRO A 337       9.904  60.610  80.308  1.00 15.53           N  
-ATOM   2550  CA  PRO A 337       9.985  61.082  81.683  1.00 14.25           C  
-ATOM   2551  C   PRO A 337      11.283  61.808  82.017  1.00 15.93           C  
-ATOM   2552  O   PRO A 337      12.366  61.243  81.891  1.00 15.63           O  
-ATOM   2553  CB  PRO A 337       9.910  59.789  82.500  1.00 16.93           C  
-ATOM   2554  CG  PRO A 337      10.331  58.651  81.553  1.00 17.25           C  
-ATOM   2555  CD  PRO A 337       9.995  59.158  80.154  1.00 17.55           C  
-ATOM   2556  N   GLY A 338      11.154  63.059  82.479  1.00 14.88           N  
-ATOM   2557  CA  GLY A 338      12.336  63.815  82.855  1.00 14.54           C  
-ATOM   2558  C   GLY A 338      12.454  65.113  82.127  1.00 17.81           C  
-ATOM   2559  O   GLY A 338      13.127  66.053  82.554  1.00 22.81           O  
-ATOM   2560  N   PHE A 339      11.757  65.184  80.999  1.00 19.32           N  
-ATOM   2561  CA  PHE A 339      11.838  66.393  80.199  1.00 13.96           C  
-ATOM   2562  C   PHE A 339      10.696  67.272  80.539  1.00 13.96           C  
-ATOM   2563  O   PHE A 339       9.606  66.770  80.776  1.00 22.31           O  
-ATOM   2564  CB  PHE A 339      11.708  66.044  78.717  1.00 10.64           C  
-ATOM   2565  CG  PHE A 339      12.837  65.169  78.270  1.00  3.88           C  
-ATOM   2566  CD1 PHE A 339      12.760  63.776  78.437  1.00  2.63           C  
-ATOM   2567  CD2 PHE A 339      13.967  65.743  77.680  1.00  2.00           C  
-ATOM   2568  CE1 PHE A 339      13.811  62.968  78.001  1.00  2.88           C  
-ATOM   2569  CE2 PHE A 339      15.001  64.936  77.218  1.00  2.00           C  
-ATOM   2570  CZ  PHE A 339      14.928  63.553  77.384  1.00  2.00           C  
-ATOM   2571  N   SER A 340      10.907  68.570  80.551  1.00  5.93           N  
-ATOM   2572  CA  SER A 340       9.788  69.412  80.861  1.00  8.24           C  
-ATOM   2573  C   SER A 340      10.176  70.702  80.211  1.00  9.54           C  
-ATOM   2574  O   SER A 340      11.351  71.018  80.104  1.00 12.25           O  
-ATOM   2575  CB  SER A 340       9.520  69.474  82.370  1.00 13.24           C  
-ATOM   2576  OG  SER A 340      10.769  69.483  83.055  1.00 20.34           O  
-ATOM   2577  N   LYS A 341       9.165  71.447  79.776  1.00  8.55           N  
-ATOM   2578  CA  LYS A 341       9.393  72.688  79.084  1.00  6.09           C  
-ATOM   2579  C   LYS A 341      10.149  73.771  79.809  1.00 10.80           C  
-ATOM   2580  O   LYS A 341      10.918  74.490  79.193  1.00 16.03           O  
-ATOM   2581  CB  LYS A 341       8.028  73.295  78.730  1.00  8.30           C  
-ATOM   2582  CG  LYS A 341       8.154  74.489  77.781  1.00 12.38           C  
-ATOM   2583  CD  LYS A 341       6.811  75.078  77.352  1.00 17.57           C  
-ATOM   2584  CE  LYS A 341       6.425  76.349  78.108  1.00 20.78           C  
-ATOM   2585  NZ  LYS A 341       5.582  75.995  79.230  1.00 27.83           N  
-ATOM   2586  N   ASP A 342       9.896  73.931  81.115  1.00 11.84           N  
-ATOM   2587  CA  ASP A 342      10.561  75.064  81.769  1.00 10.44           C  
-ATOM   2588  C   ASP A 342      11.803  74.749  82.550  1.00 11.23           C  
-ATOM   2589  O   ASP A 342      12.316  75.581  83.279  1.00 11.16           O  
-ATOM   2590  CB  ASP A 342       9.553  75.748  82.683  1.00 13.39           C  
-ATOM   2591  CG  ASP A 342       8.298  76.132  81.915  1.00 18.79           C  
-ATOM   2592  OD1 ASP A 342       8.437  76.553  80.772  1.00 19.02           O  
-ATOM   2593  OD2 ASP A 342       7.189  76.011  82.446  1.00 26.74           O  
-ATOM   2594  N   SER A 343      12.270  73.537  82.398  1.00 12.35           N  
-ATOM   2595  CA  SER A 343      13.432  73.038  83.083  1.00 13.10           C  
-ATOM   2596  C   SER A 343      14.442  72.800  81.979  1.00 14.58           C  
-ATOM   2597  O   SER A 343      14.082  72.847  80.821  1.00 22.87           O  
-ATOM   2598  CB  SER A 343      12.901  71.703  83.628  1.00  9.72           C  
-ATOM   2599  OG  SER A 343      13.862  70.896  84.288  1.00 24.12           O  
-ATOM   2600  N   GLU A 344      15.701  72.514  82.304  1.00 12.45           N  
-ATOM   2601  CA  GLU A 344      16.664  72.234  81.208  1.00 12.60           C  
-ATOM   2602  C   GLU A 344      16.839  70.723  81.029  1.00 14.76           C  
-ATOM   2603  O   GLU A 344      17.855  70.186  80.595  1.00 12.18           O  
-ATOM   2604  CB  GLU A 344      18.042  72.927  81.380  1.00 16.85           C  
-ATOM   2605  CG  GLU A 344      18.786  72.592  82.679  1.00 22.04           C  
-ATOM   2606  N   SER A 345      15.812  70.055  81.504  1.00 14.52           N  
-ATOM   2607  CA  SER A 345      15.761  68.621  81.409  1.00 17.55           C  
-ATOM   2608  C   SER A 345      17.032  67.777  81.415  1.00 20.59           C  
-ATOM   2609  O   SER A 345      17.349  67.167  80.404  1.00 21.82           O  
-ATOM   2610  CB  SER A 345      14.978  68.355  80.137  1.00 16.43           C  
-ATOM   2611  OG  SER A 345      13.731  69.049  80.314  1.00 18.13           O  
-ATOM   2612  N   LYS A 346      17.716  67.723  82.579  1.00 21.86           N  
-ATOM   2613  CA  LYS A 346      18.910  66.879  82.705  1.00 23.77           C  
-ATOM   2614  C   LYS A 346      18.369  65.497  83.043  1.00 25.00           C  
-ATOM   2615  O   LYS A 346      17.660  65.332  84.033  1.00 29.16           O  
-ATOM   2616  CB  LYS A 346      19.810  67.439  83.801  1.00 24.40           C  
-ATOM   2617  CG  LYS A 346      20.523  68.699  83.294  1.00 33.23           C  
-ATOM   2618  CD  LYS A 346      21.118  69.581  84.404  1.00 39.97           C  
-ATOM   2619  CE  LYS A 346      22.034  70.688  83.836  1.00 45.95           C  
-ATOM   2620  NZ  LYS A 346      21.742  71.993  84.410  1.00 51.42           N  
-ATOM   2621  N   ILE A 347      18.678  64.494  82.229  1.00 25.23           N  
-ATOM   2622  CA  ILE A 347      18.097  63.181  82.513  1.00 24.86           C  
-ATOM   2623  C   ILE A 347      19.087  62.314  83.248  1.00 24.84           C  
-ATOM   2624  O   ILE A 347      20.276  62.293  82.982  1.00 25.36           O  
-ATOM   2625  CB  ILE A 347      17.521  62.564  81.206  1.00 20.35           C  
-ATOM   2626  CG1 ILE A 347      16.094  63.087  80.926  1.00 19.69           C  
-ATOM   2627  CG2 ILE A 347      17.475  61.029  81.185  1.00 18.16           C  
-ATOM   2628  CD1 ILE A 347      15.975  64.597  80.697  1.00 12.30           C  
-ATOM   2629  N   SER A 348      18.517  61.576  84.190  1.00 22.60           N  
-ATOM   2630  CA  SER A 348      19.280  60.669  85.023  1.00 22.96           C  
-ATOM   2631  C   SER A 348      19.473  59.374  84.291  1.00 25.12           C  
-ATOM   2632  O   SER A 348      18.705  59.101  83.376  1.00 29.86           O  
-ATOM   2633  CB  SER A 348      18.412  60.381  86.270  1.00 22.94           C  
-ATOM   2634  OG  SER A 348      17.043  60.109  85.921  1.00 21.81           O  
-ATOM   2635  N   ARG A 349      20.421  58.520  84.727  1.00 26.78           N  
-ATOM   2636  CA  ARG A 349      20.509  57.267  83.982  1.00 26.44           C  
-ATOM   2637  C   ARG A 349      19.252  56.469  84.092  1.00 23.30           C  
-ATOM   2638  O   ARG A 349      18.958  55.655  83.241  1.00 23.92           O  
-ATOM   2639  CB  ARG A 349      21.692  56.337  84.303  1.00 28.34           C  
-ATOM   2640  CG  ARG A 349      23.027  56.810  83.672  1.00 39.36           C  
-ATOM   2641  CD  ARG A 349      23.038  57.123  82.138  1.00 42.13           C  
-ATOM   2642  NE  ARG A 349      23.855  56.244  81.299  1.00 42.13           N  
-ATOM   2643  CZ  ARG A 349      23.557  54.954  81.069  1.00 43.18           C  
-ATOM   2644  NH1 ARG A 349      22.555  54.338  81.691  1.00 44.85           N  
-ATOM   2645  NH2 ARG A 349      24.288  54.268  80.201  1.00 43.64           N  
-ATOM   2646  N   GLU A 350      18.488  56.699  85.144  1.00 26.90           N  
-ATOM   2647  CA  GLU A 350      17.263  55.911  85.222  1.00 31.45           C  
-ATOM   2648  C   GLU A 350      16.301  56.334  84.127  1.00 30.75           C  
-ATOM   2649  O   GLU A 350      15.825  55.539  83.332  1.00 33.01           O  
-ATOM   2650  CB  GLU A 350      16.599  55.970  86.622  1.00 35.70           C  
-ATOM   2651  CG  GLU A 350      15.595  54.810  86.857  1.00 42.44           C  
-ATOM   2652  N   ASP A 351      16.039  57.637  84.077  1.00 29.40           N  
-ATOM   2653  CA  ASP A 351      15.114  58.079  83.044  1.00 28.05           C  
-ATOM   2654  C   ASP A 351      15.675  57.927  81.642  1.00 27.22           C  
-ATOM   2655  O   ASP A 351      14.950  57.870  80.655  1.00 30.60           O  
-ATOM   2656  CB  ASP A 351      14.650  59.510  83.302  1.00 28.99           C  
-ATOM   2657  CG  ASP A 351      13.711  59.620  84.492  1.00 28.45           C  
-ATOM   2658  OD1 ASP A 351      12.964  58.665  84.744  1.00 26.02           O  
-ATOM   2659  OD2 ASP A 351      13.732  60.665  85.149  1.00 27.93           O  
-ATOM   2660  N   PHE A 352      17.001  57.870  81.560  1.00 24.01           N  
-ATOM   2661  CA  PHE A 352      17.655  57.687  80.279  1.00 19.62           C  
-ATOM   2662  C   PHE A 352      17.260  56.333  79.769  1.00 19.15           C  
-ATOM   2663  O   PHE A 352      16.744  56.171  78.675  1.00 25.45           O  
-ATOM   2664  CB  PHE A 352      19.180  57.737  80.436  1.00 18.20           C  
-ATOM   2665  CG  PHE A 352      19.923  57.384  79.172  1.00 18.83           C  
-ATOM   2666  CD1 PHE A 352      20.242  58.377  78.231  1.00 21.32           C  
-ATOM   2667  CD2 PHE A 352      20.326  56.058  78.941  1.00 15.96           C  
-ATOM   2668  CE1 PHE A 352      20.986  58.048  77.086  1.00 21.96           C  
-ATOM   2669  CE2 PHE A 352      21.057  55.728  77.794  1.00 14.30           C  
-ATOM   2670  CZ  PHE A 352      21.399  56.724  76.869  1.00 18.25           C  
-ATOM   2671  N   MET A 353      17.487  55.335  80.612  1.00 17.09           N  
-ATOM   2672  CA  MET A 353      17.134  53.996  80.193  1.00 18.52           C  
-ATOM   2673  C   MET A 353      15.644  53.840  79.978  1.00 20.49           C  
-ATOM   2674  O   MET A 353      15.198  53.013  79.189  1.00 19.81           O  
-ATOM   2675  CB  MET A 353      17.754  52.953  81.110  1.00 19.65           C  
-ATOM   2676  CG  MET A 353      19.295  53.119  81.050  1.00 18.12           C  
-ATOM   2677  N   SER A 354      14.859  54.645  80.703  1.00 22.71           N  
-ATOM   2678  CA  SER A 354      13.424  54.538  80.475  1.00 25.84           C  
-ATOM   2679  C   SER A 354      13.094  55.109  79.090  1.00 25.87           C  
-ATOM   2680  O   SER A 354      12.221  54.666  78.352  1.00 28.42           O  
-ATOM   2681  CB  SER A 354      12.633  55.339  81.526  1.00 27.61           C  
-ATOM   2682  OG  SER A 354      13.050  55.077  82.868  1.00 35.58           O  
-ATOM   2683  N   GLY A 355      13.847  56.145  78.754  1.00 23.04           N  
-ATOM   2684  CA  GLY A 355      13.632  56.789  77.491  1.00 20.76           C  
-ATOM   2685  C   GLY A 355      13.913  55.887  76.330  1.00 20.74           C  
-ATOM   2686  O   GLY A 355      13.065  55.716  75.465  1.00 20.96           O  
-ATOM   2687  N   VAL A 356      15.118  55.281  76.330  1.00 16.58           N  
-ATOM   2688  CA  VAL A 356      15.436  54.406  75.221  1.00 12.80           C  
-ATOM   2689  C   VAL A 356      14.445  53.285  75.072  1.00 12.89           C  
-ATOM   2690  O   VAL A 356      14.189  52.860  73.962  1.00 20.26           O  
-ATOM   2691  CB  VAL A 356      16.919  53.999  75.178  1.00 15.13           C  
-ATOM   2692  CG1 VAL A 356      17.576  53.882  76.541  1.00 11.98           C  
-ATOM   2693  CG2 VAL A 356      17.220  52.742  74.320  1.00 16.47           C  
-ATOM   2694  N   LYS A 357      13.868  52.798  76.158  1.00 17.12           N  
-ATOM   2695  CA  LYS A 357      12.876  51.743  75.975  1.00 18.30           C  
-ATOM   2696  C   LYS A 357      11.719  52.291  75.167  1.00 16.64           C  
-ATOM   2697  O   LYS A 357      11.169  51.615  74.316  1.00 20.77           O  
-ATOM   2698  CB  LYS A 357      12.315  51.214  77.311  1.00 23.65           C  
-ATOM   2699  CG  LYS A 357      13.340  50.427  78.147  1.00 34.69           C  
-ATOM   2700  CD  LYS A 357      12.893  49.065  78.757  1.00 48.38           C  
-ATOM   2701  CE  LYS A 357      11.495  48.500  78.390  1.00 53.77           C  
-ATOM   2702  NZ  LYS A 357      11.366  48.161  76.970  1.00 58.39           N  
-ATOM   2703  N   LEU A 358      11.354  53.539  75.448  1.00 16.56           N  
-ATOM   2704  CA  LEU A 358      10.239  54.119  74.705  1.00 16.67           C  
-ATOM   2705  C   LEU A 358      10.595  54.389  73.255  1.00 19.85           C  
-ATOM   2706  O   LEU A 358       9.729  54.354  72.389  1.00 26.58           O  
-ATOM   2707  CB  LEU A 358       9.796  55.471  75.298  1.00  7.56           C  
-ATOM   2708  CG  LEU A 358       9.274  55.385  76.723  1.00  2.00           C  
-ATOM   2709  CD1 LEU A 358       9.116  56.780  77.314  1.00  2.00           C  
-ATOM   2710  CD2 LEU A 358       7.937  54.652  76.758  1.00  2.00           C  
-ATOM   2711  N   SER A 359      11.862  54.715  73.003  1.00 17.69           N  
-ATOM   2712  CA  SER A 359      12.256  54.998  71.638  1.00 15.36           C  
-ATOM   2713  C   SER A 359      12.405  53.770  70.792  1.00 16.54           C  
-ATOM   2714  O   SER A 359      12.192  53.833  69.594  1.00 22.90           O  
-ATOM   2715  CB  SER A 359      13.594  55.739  71.579  1.00 13.60           C  
-ATOM   2716  OG  SER A 359      13.573  56.801  72.535  1.00 20.22           O  
-ATOM   2717  N   VAL A 360      12.759  52.645  71.391  1.00 11.65           N  
-ATOM   2718  CA  VAL A 360      12.944  51.481  70.561  1.00  9.46           C  
-ATOM   2719  C   VAL A 360      11.964  50.393  70.960  1.00 12.11           C  
-ATOM   2720  O   VAL A 360      12.368  49.333  71.408  1.00 16.36           O  
-ATOM   2721  CB  VAL A 360      14.434  51.063  70.661  1.00  9.14           C  
-ATOM   2722  CG1 VAL A 360      14.841  50.178  69.466  1.00 10.89           C  
-ATOM   2723  CG2 VAL A 360      15.367  52.292  70.691  1.00 10.29           C  
-ATOM   2724  N   PRO A 361      10.655  50.620  70.779  1.00 15.18           N  
-ATOM   2725  CA  PRO A 361       9.654  49.694  71.335  1.00 15.98           C  
-ATOM   2726  C   PRO A 361       9.757  48.242  70.921  1.00 19.48           C  
-ATOM   2727  O   PRO A 361       9.177  47.348  71.504  1.00 23.85           O  
-ATOM   2728  CB  PRO A 361       8.306  50.273  70.880  1.00 11.55           C  
-ATOM   2729  CG  PRO A 361       8.642  51.317  69.810  1.00 12.75           C  
-ATOM   2730  CD  PRO A 361      10.084  51.755  70.062  1.00 14.40           C  
-ATOM   2731  N   HIS A 362      10.477  48.020  69.845  1.00 25.44           N  
-ATOM   2732  CA  HIS A 362      10.623  46.670  69.321  1.00 29.48           C  
-ATOM   2733  C   HIS A 362      11.939  46.025  69.693  1.00 30.30           C  
-ATOM   2734  O   HIS A 362      12.196  44.881  69.334  1.00 34.95           O  
-ATOM   2735  CB  HIS A 362      10.507  46.696  67.769  1.00 35.06           C  
-ATOM   2736  CG  HIS A 362      11.270  47.870  67.165  1.00 36.68           C  
-ATOM   2737  ND1 HIS A 362      10.727  49.092  66.938  1.00 35.63           N  
-ATOM   2738  CD2 HIS A 362      12.633  47.919  66.802  1.00 35.92           C  
-ATOM   2739  CE1 HIS A 362      11.710  49.868  66.466  1.00 36.94           C  
-ATOM   2740  NE2 HIS A 362      12.865  49.175  66.382  1.00 39.26           N  
-ATOM   2741  N   ALA A 363      12.812  46.774  70.361  1.00 25.05           N  
-ATOM   2742  CA  ALA A 363      14.062  46.133  70.675  1.00 24.30           C  
-ATOM   2743  C   ALA A 363      13.848  45.186  71.823  1.00 26.94           C  
-ATOM   2744  O   ALA A 363      12.951  45.319  72.646  1.00 27.66           O  
-ATOM   2745  CB  ALA A 363      15.134  47.133  71.121  1.00 24.12           C  
-ATOM   2746  N   ASN A 364      14.749  44.213  71.849  1.00 25.62           N  
-ATOM   2747  CA  ASN A 364      14.758  43.232  72.908  1.00 22.62           C  
-ATOM   2748  C   ASN A 364      15.867  43.752  73.798  1.00 24.40           C  
-ATOM   2749  O   ASN A 364      16.571  44.705  73.484  1.00 24.24           O  
-ATOM   2750  CB  ASN A 364      15.012  41.792  72.399  1.00 23.27           C  
-ATOM   2751  CG  ASN A 364      16.304  41.675  71.630  1.00 23.08           C  
-ATOM   2752  OD1 ASN A 364      17.141  42.556  71.718  1.00 28.93           O  
-ATOM   2753  ND2 ASN A 364      16.476  40.606  70.870  1.00 23.88           N  
-ATOM   2754  N   ASP A 365      16.056  43.061  74.917  1.00 27.48           N  
-ATOM   2755  CA  ASP A 365      17.081  43.472  75.882  1.00 25.27           C  
-ATOM   2756  C   ASP A 365      18.430  43.730  75.275  1.00 25.82           C  
-ATOM   2757  O   ASP A 365      19.141  44.680  75.568  1.00 28.02           O  
-ATOM   2758  CB  ASP A 365      17.372  42.372  76.914  1.00 26.63           C  
-ATOM   2759  N   LEU A 366      18.782  42.827  74.380  1.00 23.27           N  
-ATOM   2760  CA  LEU A 366      20.075  42.962  73.762  1.00 21.37           C  
-ATOM   2761  C   LEU A 366      20.147  44.191  72.883  1.00 21.66           C  
-ATOM   2762  O   LEU A 366      21.144  44.898  72.806  1.00 22.93           O  
-ATOM   2763  CB  LEU A 366      20.344  41.690  72.966  1.00 22.53           C  
-ATOM   2764  CG  LEU A 366      21.729  41.107  73.176  1.00 21.41           C  
-ATOM   2765  CD1 LEU A 366      21.853  39.905  72.247  1.00 26.47           C  
-ATOM   2766  CD2 LEU A 366      22.850  42.138  72.963  1.00 22.36           C  
-ATOM   2767  N   GLY A 367      19.025  44.444  72.229  1.00 18.78           N  
-ATOM   2768  CA  GLY A 367      18.936  45.581  71.345  1.00 20.09           C  
-ATOM   2769  C   GLY A 367      19.094  46.861  72.104  1.00 19.16           C  
-ATOM   2770  O   GLY A 367      19.884  47.713  71.725  1.00 17.49           O  
-ATOM   2771  N   LEU A 368      18.342  46.960  73.218  1.00 19.69           N  
-ATOM   2772  CA  LEU A 368      18.410  48.152  74.058  1.00 18.37           C  
-ATOM   2773  C   LEU A 368      19.844  48.330  74.525  1.00 18.27           C  
-ATOM   2774  O   LEU A 368      20.426  49.409  74.485  1.00 15.58           O  
-ATOM   2775  CB  LEU A 368      17.438  48.068  75.248  1.00 21.93           C  
-ATOM   2776  CG  LEU A 368      15.933  48.026  74.877  1.00 25.14           C  
-ATOM   2777  CD1 LEU A 368      15.070  47.567  76.053  1.00 22.66           C  
-ATOM   2778  CD2 LEU A 368      15.401  49.388  74.386  1.00 26.92           C  
-ATOM   2779  N   ASP A 369      20.428  47.189  74.923  1.00 18.38           N  
-ATOM   2780  CA  ASP A 369      21.827  47.226  75.362  1.00 19.79           C  
-ATOM   2781  C   ASP A 369      22.745  47.793  74.289  1.00 19.98           C  
-ATOM   2782  O   ASP A 369      23.653  48.575  74.568  1.00 20.06           O  
-ATOM   2783  CB  ASP A 369      22.362  45.826  75.703  1.00 20.42           C  
-ATOM   2784  CG  ASP A 369      22.133  45.388  77.141  1.00 25.81           C  
-ATOM   2785  OD1 ASP A 369      21.345  46.014  77.858  1.00 28.18           O  
-ATOM   2786  OD2 ASP A 369      22.771  44.415  77.545  1.00 28.77           O  
-ATOM   2787  N   ALA A 370      22.475  47.355  73.042  1.00 19.57           N  
-ATOM   2788  CA  ALA A 370      23.252  47.794  71.903  1.00 12.88           C  
-ATOM   2789  C   ALA A 370      23.109  49.283  71.682  1.00 13.98           C  
-ATOM   2790  O   ALA A 370      24.088  49.947  71.360  1.00 17.14           O  
-ATOM   2791  CB  ALA A 370      22.849  47.031  70.655  1.00 10.17           C  
-ATOM   2792  N   VAL A 371      21.890  49.808  71.859  1.00 13.39           N  
-ATOM   2793  CA  VAL A 371      21.688  51.248  71.663  1.00 13.99           C  
-ATOM   2794  C   VAL A 371      22.480  52.053  72.704  1.00 14.95           C  
-ATOM   2795  O   VAL A 371      23.202  52.998  72.393  1.00 18.40           O  
-ATOM   2796  CB  VAL A 371      20.179  51.599  71.742  1.00 13.56           C  
-ATOM   2797  CG1 VAL A 371      19.924  53.103  71.535  1.00  9.32           C  
-ATOM   2798  CG2 VAL A 371      19.330  50.764  70.762  1.00  6.60           C  
-ATOM   2799  N   THR A 372      22.316  51.663  73.967  1.00 14.34           N  
-ATOM   2800  CA  THR A 372      23.003  52.331  75.058  1.00 13.68           C  
-ATOM   2801  C   THR A 372      24.507  52.355  74.841  1.00 12.35           C  
-ATOM   2802  O   THR A 372      25.194  53.339  75.056  1.00  9.76           O  
-ATOM   2803  CB  THR A 372      22.682  51.541  76.319  1.00 18.11           C  
-ATOM   2804  OG1 THR A 372      21.272  51.359  76.415  1.00 21.72           O  
-ATOM   2805  CG2 THR A 372      23.187  52.181  77.614  1.00 26.75           C  
-ATOM   2806  N   LEU A 373      25.014  51.219  74.372  1.00 12.03           N  
-ATOM   2807  CA  LEU A 373      26.438  51.164  74.118  1.00 12.19           C  
-ATOM   2808  C   LEU A 373      26.899  52.318  73.242  1.00 15.50           C  
-ATOM   2809  O   LEU A 373      27.837  53.027  73.567  1.00 15.29           O  
-ATOM   2810  CB  LEU A 373      26.804  49.835  73.429  1.00  9.08           C  
-ATOM   2811  CG  LEU A 373      28.225  49.330  73.745  1.00 11.38           C  
-ATOM   2812  CD1 LEU A 373      28.554  48.051  72.978  1.00 14.39           C  
-ATOM   2813  CD2 LEU A 373      29.337  50.350  73.488  1.00 17.82           C  
-ATOM   2814  N   GLN A 374      26.163  52.495  72.132  1.00 20.44           N  
-ATOM   2815  CA  GLN A 374      26.528  53.529  71.166  1.00 21.57           C  
-ATOM   2816  C   GLN A 374      26.289  54.941  71.597  1.00 22.18           C  
-ATOM   2817  O   GLN A 374      27.070  55.833  71.300  1.00 23.00           O  
-ATOM   2818  CB  GLN A 374      25.739  53.401  69.848  1.00 24.24           C  
-ATOM   2819  CG  GLN A 374      25.628  51.987  69.285  1.00 33.24           C  
-ATOM   2820  CD  GLN A 374      26.957  51.458  68.790  1.00 39.05           C  
-ATOM   2821  OE1 GLN A 374      27.753  52.173  68.192  1.00 42.09           O  
-ATOM   2822  NE2 GLN A 374      27.159  50.156  69.011  1.00 39.02           N  
-ATOM   2823  N   TYR A 375      25.159  55.138  72.272  1.00 20.75           N  
-ATOM   2824  CA  TYR A 375      24.832  56.505  72.658  1.00 22.88           C  
-ATOM   2825  C   TYR A 375      25.365  56.972  74.005  1.00 25.42           C  
-ATOM   2826  O   TYR A 375      25.221  58.143  74.345  1.00 26.36           O  
-ATOM   2827  CB  TYR A 375      23.308  56.706  72.501  1.00 22.55           C  
-ATOM   2828  CG  TYR A 375      22.939  56.796  71.029  1.00 24.01           C  
-ATOM   2829  CD1 TYR A 375      22.995  58.053  70.382  1.00 21.13           C  
-ATOM   2830  CD2 TYR A 375      22.608  55.639  70.277  1.00 20.10           C  
-ATOM   2831  CE1 TYR A 375      22.734  58.162  69.013  1.00 16.38           C  
-ATOM   2832  CE2 TYR A 375      22.344  55.752  68.898  1.00 13.81           C  
-ATOM   2833  CZ  TYR A 375      22.400  57.021  68.275  1.00 17.25           C  
-ATOM   2834  OH  TYR A 375      22.110  57.194  66.939  1.00 18.33           O  
-ATOM   2835  N   THR A 376      25.972  56.094  74.795  1.00 27.14           N  
-ATOM   2836  CA  THR A 376      26.466  56.558  76.079  1.00 26.81           C  
-ATOM   2837  C   THR A 376      27.950  56.896  76.026  1.00 30.00           C  
-ATOM   2838  O   THR A 376      28.788  56.256  75.401  1.00 32.19           O  
-ATOM   2839  CB  THR A 376      26.248  55.429  77.102  1.00 24.27           C  
-ATOM   2840  OG1 THR A 376      24.848  55.183  77.221  1.00 26.14           O  
-ATOM   2841  CG2 THR A 376      26.772  55.689  78.525  1.00 26.13           C  
-ATOM   2842  N   ASP A 377      28.267  57.974  76.756  1.00 32.90           N  
-ATOM   2843  CA  ASP A 377      29.663  58.373  76.884  1.00 33.12           C  
-ATOM   2844  C   ASP A 377      30.088  57.620  78.138  1.00 33.75           C  
-ATOM   2845  O   ASP A 377      29.853  58.093  79.246  1.00 35.52           O  
-ATOM   2846  CB  ASP A 377      29.821  59.888  77.099  1.00 29.45           C  
-ATOM   2847  CG  ASP A 377      31.259  60.278  77.411  1.00 32.39           C  
-ATOM   2848  OD1 ASP A 377      32.052  59.407  77.779  1.00 31.09           O  
-ATOM   2849  OD2 ASP A 377      31.587  61.456  77.284  1.00 36.13           O  
-ATOM   2850  N   TRP A 378      30.724  56.467  77.964  1.00 33.67           N  
-ATOM   2851  CA  TRP A 378      31.115  55.677  79.118  1.00 32.74           C  
-ATOM   2852  C   TRP A 378      32.033  56.368  80.072  1.00 35.40           C  
-ATOM   2853  O   TRP A 378      32.005  56.047  81.250  1.00 38.33           O  
-ATOM   2854  CB  TRP A 378      31.630  54.292  78.729  1.00 34.03           C  
-ATOM   2855  CG  TRP A 378      30.471  53.588  78.076  1.00 34.63           C  
-ATOM   2856  CD1 TRP A 378      30.183  53.518  76.694  1.00 35.42           C  
-ATOM   2857  CD2 TRP A 378      29.417  52.973  78.756  1.00 33.28           C  
-ATOM   2858  NE1 TRP A 378      29.000  52.899  76.494  1.00 35.74           N  
-ATOM   2859  CE2 TRP A 378      28.471  52.533  77.709  1.00 34.52           C  
-ATOM   2860  CE3 TRP A 378      29.112  52.790  80.102  1.00 32.54           C  
-ATOM   2861  CZ2 TRP A 378      27.263  51.928  78.090  1.00 33.96           C  
-ATOM   2862  CZ3 TRP A 378      27.891  52.181  80.439  1.00 37.50           C  
-ATOM   2863  CH2 TRP A 378      26.978  51.757  79.451  1.00 33.89           C  
-ATOM   2864  N   MET A 379      32.825  57.343  79.609  1.00 35.43           N  
-ATOM   2865  CA  MET A 379      33.697  58.015  80.583  1.00 38.11           C  
-ATOM   2866  C   MET A 379      33.006  59.171  81.323  1.00 37.63           C  
-ATOM   2867  O   MET A 379      33.621  60.030  81.937  1.00 37.01           O  
-ATOM   2868  CB  MET A 379      34.997  58.503  79.946  1.00 39.47           C  
-ATOM   2869  CG  MET A 379      36.089  58.677  81.013  1.00 48.58           C  
-ATOM   2870  SD  MET A 379      37.630  59.176  80.217  1.00 60.48           S  
-ATOM   2871  CE  MET A 379      38.186  57.574  79.529  1.00 60.32           C  
-ATOM   2872  N   ASP A 380      31.684  59.210  81.242  1.00 37.26           N  
-ATOM   2873  CA  ASP A 380      30.950  60.276  81.901  1.00 35.20           C  
-ATOM   2874  C   ASP A 380      29.496  59.852  82.031  1.00 36.78           C  
-ATOM   2875  O   ASP A 380      28.558  60.633  82.001  1.00 36.31           O  
-ATOM   2876  CB  ASP A 380      31.085  61.573  81.080  1.00 37.41           C  
-ATOM   2877  CG  ASP A 380      30.946  62.833  81.916  1.00 42.24           C  
-ATOM   2878  OD1 ASP A 380      30.115  62.841  82.818  1.00 44.95           O  
-ATOM   2879  OD2 ASP A 380      31.680  63.796  81.681  1.00 46.59           O  
-ATOM   2880  N   ASP A 381      29.362  58.537  82.159  1.00 39.63           N  
-ATOM   2881  CA  ASP A 381      28.137  57.774  82.303  1.00 41.26           C  
-ATOM   2882  C   ASP A 381      26.898  58.498  82.853  1.00 40.30           C  
-ATOM   2883  O   ASP A 381      25.862  58.482  82.204  1.00 41.14           O  
-ATOM   2884  CB  ASP A 381      28.520  56.477  83.058  1.00 44.63           C  
-ATOM   2885  CG  ASP A 381      27.429  55.697  83.761  1.00 53.35           C  
-ATOM   2886  OD1 ASP A 381      26.283  55.738  83.316  1.00 56.74           O  
-ATOM   2887  OD2 ASP A 381      27.743  55.043  84.760  1.00 59.44           O  
-ATOM   2888  N   ASN A 382      27.006  59.118  84.031  1.00 42.03           N  
-ATOM   2889  CA  ASN A 382      25.865  59.779  84.670  1.00 41.65           C  
-ATOM   2890  C   ASN A 382      25.642  61.248  84.350  1.00 42.00           C  
-ATOM   2891  O   ASN A 382      24.947  61.916  85.107  1.00 45.11           O  
-ATOM   2892  CB  ASN A 382      26.124  59.744  86.202  1.00 39.34           C  
-ATOM   2893  N   ASN A 383      26.225  61.785  83.267  1.00 41.46           N  
-ATOM   2894  CA  ASN A 383      26.010  63.225  83.006  1.00 35.71           C  
-ATOM   2895  C   ASN A 383      24.620  63.545  82.472  1.00 33.59           C  
-ATOM   2896  O   ASN A 383      24.279  63.254  81.336  1.00 38.41           O  
-ATOM   2897  CB  ASN A 383      27.083  63.795  82.076  1.00 31.38           C  
-ATOM   2898  CG  ASN A 383      26.928  65.278  81.831  1.00 32.86           C  
-ATOM   2899  OD1 ASN A 383      25.842  65.826  81.848  1.00 35.62           O  
-ATOM   2900  ND2 ASN A 383      28.040  65.962  81.597  1.00 33.67           N  
-ATOM   2901  N   GLY A 384      23.850  64.252  83.289  1.00 30.80           N  
-ATOM   2902  CA  GLY A 384      22.496  64.597  82.893  1.00 27.25           C  
-ATOM   2903  C   GLY A 384      22.328  65.341  81.593  1.00 22.82           C  
-ATOM   2904  O   GLY A 384      21.356  65.150  80.884  1.00 24.91           O  
-ATOM   2905  N   ILE A 385      23.257  66.223  81.275  1.00 19.50           N  
-ATOM   2906  CA  ILE A 385      23.151  66.941  80.018  1.00 21.44           C  
-ATOM   2907  C   ILE A 385      23.415  65.938  78.883  1.00 21.19           C  
-ATOM   2908  O   ILE A 385      22.682  65.776  77.911  1.00 22.17           O  
-ATOM   2909  CB  ILE A 385      24.161  68.106  80.037  1.00 22.64           C  
-ATOM   2910  CG1 ILE A 385      23.678  69.272  80.907  1.00 25.55           C  
-ATOM   2911  CG2 ILE A 385      24.550  68.612  78.650  1.00 26.15           C  
-ATOM   2912  CD1 ILE A 385      22.582  70.084  80.198  1.00 31.32           C  
-ATOM   2913  N   LYS A 386      24.507  65.208  79.051  1.00 19.41           N  
-ATOM   2914  CA  LYS A 386      24.846  64.229  78.030  1.00 16.41           C  
-ATOM   2915  C   LYS A 386      23.746  63.214  77.802  1.00 15.50           C  
-ATOM   2916  O   LYS A 386      23.520  62.748  76.696  1.00 19.02           O  
-ATOM   2917  CB  LYS A 386      26.163  63.511  78.355  1.00 15.67           C  
-ATOM   2918  CG  LYS A 386      27.363  64.470  78.269  1.00 13.97           C  
-ATOM   2919  CD  LYS A 386      28.705  63.748  78.404  1.00 22.76           C  
-ATOM   2920  CE  LYS A 386      29.899  64.709  78.258  1.00 29.85           C  
-ATOM   2921  NZ  LYS A 386      31.167  63.988  78.174  1.00 32.24           N  
-ATOM   2922  N   ASN A 387      23.045  62.872  78.863  1.00 14.39           N  
-ATOM   2923  CA  ASN A 387      21.969  61.905  78.713  1.00 15.86           C  
-ATOM   2924  C   ASN A 387      20.782  62.521  78.022  1.00 15.13           C  
-ATOM   2925  O   ASN A 387      20.085  61.866  77.261  1.00 17.02           O  
-ATOM   2926  CB  ASN A 387      21.521  61.340  80.070  1.00 21.64           C  
-ATOM   2927  CG  ASN A 387      22.530  60.443  80.766  1.00 28.33           C  
-ATOM   2928  OD1 ASN A 387      22.410  60.183  81.952  1.00 35.96           O  
-ATOM   2929  ND2 ASN A 387      23.541  59.943  80.033  1.00 29.77           N  
-ATOM   2930  N   ARG A 388      20.558  63.808  78.281  1.00 11.15           N  
-ATOM   2931  CA  ARG A 388      19.430  64.467  77.645  1.00 11.50           C  
-ATOM   2932  C   ARG A 388      19.648  64.479  76.139  1.00 13.43           C  
-ATOM   2933  O   ARG A 388      18.815  64.110  75.308  1.00 10.98           O  
-ATOM   2934  CB  ARG A 388      19.340  65.916  78.167  1.00  9.27           C  
-ATOM   2935  CG  ARG A 388      18.216  66.780  77.556  1.00  7.23           C  
-ATOM   2936  CD  ARG A 388      18.418  68.277  77.829  1.00 10.14           C  
-ATOM   2937  NE  ARG A 388      19.677  68.697  77.262  1.00  9.96           N  
-ATOM   2938  CZ  ARG A 388      20.276  69.841  77.586  1.00 14.29           C  
-ATOM   2939  NH1 ARG A 388      19.710  70.708  78.412  1.00 19.41           N  
-ATOM   2940  NH2 ARG A 388      21.468  70.114  77.068  1.00 21.28           N  
-ATOM   2941  N   ASP A 389      20.858  64.938  75.812  1.00 10.11           N  
-ATOM   2942  CA  ASP A 389      21.227  65.033  74.418  1.00  6.98           C  
-ATOM   2943  C   ASP A 389      21.295  63.682  73.756  1.00  6.78           C  
-ATOM   2944  O   ASP A 389      20.832  63.526  72.638  1.00 11.27           O  
-ATOM   2945  CB  ASP A 389      22.537  65.804  74.258  1.00 11.29           C  
-ATOM   2946  CG  ASP A 389      22.402  67.288  74.636  1.00 17.29           C  
-ATOM   2947  OD1 ASP A 389      21.275  67.756  74.811  1.00 17.15           O  
-ATOM   2948  OD2 ASP A 389      23.423  67.979  74.735  1.00 17.35           O  
-ATOM   2949  N   GLY A 390      21.829  62.673  74.429  1.00  3.73           N  
-ATOM   2950  CA  GLY A 390      21.891  61.375  73.763  1.00  6.75           C  
-ATOM   2951  C   GLY A 390      20.517  60.854  73.369  1.00 11.44           C  
-ATOM   2952  O   GLY A 390      20.280  60.300  72.303  1.00 18.60           O  
-ATOM   2953  N   LEU A 391      19.560  61.102  74.239  1.00 12.73           N  
-ATOM   2954  CA  LEU A 391      18.210  60.633  73.972  1.00 13.42           C  
-ATOM   2955  C   LEU A 391      17.604  61.378  72.800  1.00 12.34           C  
-ATOM   2956  O   LEU A 391      16.874  60.877  71.957  1.00 11.07           O  
-ATOM   2957  CB  LEU A 391      17.431  60.825  75.281  1.00 17.09           C  
-ATOM   2958  CG  LEU A 391      16.427  59.725  75.627  1.00 15.61           C  
-ATOM   2959  CD1 LEU A 391      17.014  58.315  75.658  1.00 20.05           C  
-ATOM   2960  CD2 LEU A 391      15.854  60.061  76.993  1.00 18.22           C  
-ATOM   2961  N   ASP A 392      17.964  62.645  72.739  1.00 13.63           N  
-ATOM   2962  CA  ASP A 392      17.482  63.480  71.651  1.00 16.96           C  
-ATOM   2963  C   ASP A 392      18.015  62.979  70.298  1.00 21.00           C  
-ATOM   2964  O   ASP A 392      17.426  63.204  69.238  1.00 25.56           O  
-ATOM   2965  CB  ASP A 392      17.897  64.926  71.935  1.00 22.14           C  
-ATOM   2966  CG  ASP A 392      17.358  65.901  70.910  1.00 25.90           C  
-ATOM   2967  OD1 ASP A 392      17.973  66.037  69.857  1.00 33.47           O  
-ATOM   2968  OD2 ASP A 392      16.335  66.521  71.162  1.00 26.93           O  
-ATOM   2969  N   ASP A 393      19.156  62.283  70.341  1.00 19.36           N  
-ATOM   2970  CA  ASP A 393      19.713  61.750  69.109  1.00 14.77           C  
-ATOM   2971  C   ASP A 393      19.246  60.355  68.865  1.00 16.13           C  
-ATOM   2972  O   ASP A 393      19.321  59.871  67.745  1.00 15.95           O  
-ATOM   2973  CB  ASP A 393      21.224  61.641  69.157  1.00 16.70           C  
-ATOM   2974  CG  ASP A 393      21.909  62.970  69.052  1.00 20.90           C  
-ATOM   2975  OD1 ASP A 393      21.285  63.912  68.572  1.00 28.23           O  
-ATOM   2976  OD2 ASP A 393      23.076  63.058  69.438  1.00 28.40           O  
-ATOM   2977  N   ILE A 394      18.806  59.670  69.917  1.00 16.81           N  
-ATOM   2978  CA  ILE A 394      18.326  58.320  69.686  1.00 14.79           C  
-ATOM   2979  C   ILE A 394      17.034  58.468  68.911  1.00 14.40           C  
-ATOM   2980  O   ILE A 394      16.827  57.899  67.848  1.00 15.07           O  
-ATOM   2981  CB  ILE A 394      18.197  57.526  71.020  1.00  9.94           C  
-ATOM   2982  CG1 ILE A 394      19.600  57.171  71.545  1.00  9.43           C  
-ATOM   2983  CG2 ILE A 394      17.360  56.246  70.892  1.00  3.78           C  
-ATOM   2984  CD1 ILE A 394      19.620  56.444  72.895  1.00 11.88           C  
-ATOM   2985  N   VAL A 395      16.159  59.314  69.440  1.00 17.14           N  
-ATOM   2986  CA  VAL A 395      14.882  59.476  68.762  1.00 16.27           C  
-ATOM   2987  C   VAL A 395      15.066  59.986  67.326  1.00 18.15           C  
-ATOM   2988  O   VAL A 395      14.518  59.477  66.360  1.00 17.08           O  
-ATOM   2989  CB  VAL A 395      13.981  60.346  69.672  1.00 13.18           C  
-ATOM   2990  CG1 VAL A 395      12.546  60.519  69.153  1.00 12.93           C  
-ATOM   2991  CG2 VAL A 395      13.926  59.757  71.097  1.00  6.53           C  
-ATOM   2992  N   GLY A 396      15.891  61.009  67.180  1.00 21.58           N  
-ATOM   2993  CA  GLY A 396      16.084  61.550  65.844  1.00 18.28           C  
-ATOM   2994  C   GLY A 396      16.695  60.588  64.847  1.00 16.40           C  
-ATOM   2995  O   GLY A 396      16.185  60.406  63.751  1.00 23.24           O  
-ATOM   2996  N   ASP A 397      17.805  59.961  65.219  1.00 12.43           N  
-ATOM   2997  CA  ASP A 397      18.447  59.048  64.289  1.00  3.45           C  
-ATOM   2998  C   ASP A 397      17.594  57.853  63.993  1.00  5.71           C  
-ATOM   2999  O   ASP A 397      17.481  57.433  62.852  1.00 11.98           O  
-ATOM   3000  CB  ASP A 397      19.799  58.569  64.821  1.00  2.73           C  
-ATOM   3001  CG  ASP A 397      20.775  59.713  65.035  1.00  7.64           C  
-ATOM   3002  OD1 ASP A 397      20.479  60.845  64.650  1.00  6.63           O  
-ATOM   3003  OD2 ASP A 397      21.844  59.477  65.595  1.00 10.63           O  
-ATOM   3004  N   HIS A 398      16.974  57.304  65.016  1.00  5.99           N  
-ATOM   3005  CA  HIS A 398      16.160  56.141  64.764  1.00  8.08           C  
-ATOM   3006  C   HIS A 398      14.946  56.444  63.901  1.00 12.21           C  
-ATOM   3007  O   HIS A 398      14.656  55.722  62.959  1.00 17.17           O  
-ATOM   3008  CB  HIS A 398      15.656  55.541  66.098  1.00  5.36           C  
-ATOM   3009  CG  HIS A 398      14.660  54.405  65.892  1.00  3.31           C  
-ATOM   3010  ND1 HIS A 398      14.967  53.237  65.314  1.00  2.00           N  
-ATOM   3011  CD2 HIS A 398      13.281  54.365  66.230  1.00  5.16           C  
-ATOM   3012  CE1 HIS A 398      13.840  52.506  65.297  1.00  2.44           C  
-ATOM   3013  NE2 HIS A 398      12.802  53.160  65.843  1.00  2.00           N  
-ATOM   3014  N   ASN A 399      14.251  57.533  64.234  1.00 11.60           N  
-ATOM   3015  CA  ASN A 399      13.000  57.822  63.527  1.00 11.44           C  
-ATOM   3016  C   ASN A 399      12.992  58.748  62.330  1.00 10.94           C  
-ATOM   3017  O   ASN A 399      11.989  58.763  61.629  1.00 11.39           O  
-ATOM   3018  CB  ASN A 399      11.987  58.485  64.480  1.00 13.59           C  
-ATOM   3019  CG  ASN A 399      11.643  57.649  65.659  1.00 12.03           C  
-ATOM   3020  OD1 ASN A 399      10.740  56.841  65.605  1.00  7.86           O  
-ATOM   3021  ND2 ASN A 399      12.376  57.852  66.740  1.00 16.18           N  
-ATOM   3022  N   VAL A 400      14.027  59.553  62.106  1.00  8.13           N  
-ATOM   3023  CA  VAL A 400      13.945  60.448  60.962  1.00  6.64           C  
-ATOM   3024  C   VAL A 400      15.215  60.433  60.133  1.00 11.94           C  
-ATOM   3025  O   VAL A 400      15.197  60.192  58.936  1.00 19.91           O  
-ATOM   3026  CB  VAL A 400      13.629  61.870  61.447  1.00  2.00           C  
-ATOM   3027  CG1 VAL A 400      13.447  62.823  60.272  1.00  9.10           C  
-ATOM   3028  CG2 VAL A 400      12.362  61.916  62.321  1.00  2.00           C  
-ATOM   3029  N   ILE A 401      16.354  60.678  60.767  1.00 12.04           N  
-ATOM   3030  CA  ILE A 401      17.569  60.715  59.961  1.00 10.10           C  
-ATOM   3031  C   ILE A 401      17.938  59.398  59.349  1.00 11.78           C  
-ATOM   3032  O   ILE A 401      18.093  59.291  58.145  1.00 18.25           O  
-ATOM   3033  CB  ILE A 401      18.755  61.335  60.721  1.00  8.29           C  
-ATOM   3034  CG1 ILE A 401      18.295  62.654  61.372  1.00  3.74           C  
-ATOM   3035  CG2 ILE A 401      19.984  61.535  59.814  1.00  8.02           C  
-ATOM   3036  CD1 ILE A 401      19.433  63.514  61.913  1.00  2.00           C  
-ATOM   3037  N   CYS A 402      18.088  58.365  60.152  1.00 13.62           N  
-ATOM   3038  CA  CYS A 402      18.495  57.121  59.506  1.00 14.50           C  
-ATOM   3039  C   CYS A 402      17.572  56.533  58.450  1.00 13.22           C  
-ATOM   3040  O   CYS A 402      18.124  56.120  57.438  1.00 19.78           O  
-ATOM   3041  CB  CYS A 402      19.014  56.084  60.477  1.00 11.32           C  
-ATOM   3042  SG  CYS A 402      20.385  56.807  61.425  1.00 15.97           S  
-ATOM   3043  N   PRO A 403      16.235  56.464  58.600  1.00  8.93           N  
-ATOM   3044  CA  PRO A 403      15.429  55.964  57.494  1.00 10.79           C  
-ATOM   3045  C   PRO A 403      15.525  56.854  56.245  1.00 12.36           C  
-ATOM   3046  O   PRO A 403      15.529  56.351  55.119  1.00 14.53           O  
-ATOM   3047  CB  PRO A 403      14.006  55.757  58.043  1.00  6.70           C  
-ATOM   3048  CG  PRO A 403      14.020  56.382  59.436  1.00 11.20           C  
-ATOM   3049  CD  PRO A 403      15.491  56.629  59.826  1.00 10.36           C  
-ATOM   3050  N   LEU A 404      15.628  58.175  56.465  1.00 11.19           N  
-ATOM   3051  CA  LEU A 404      15.735  59.087  55.320  1.00  9.91           C  
-ATOM   3052  C   LEU A 404      17.004  58.797  54.535  1.00 13.85           C  
-ATOM   3053  O   LEU A 404      17.003  58.677  53.314  1.00 16.68           O  
-ATOM   3054  CB  LEU A 404      15.669  60.553  55.770  1.00  5.07           C  
-ATOM   3055  CG  LEU A 404      15.739  61.585  54.627  1.00  2.50           C  
-ATOM   3056  CD1 LEU A 404      14.649  62.656  54.746  1.00  2.00           C  
-ATOM   3057  CD2 LEU A 404      17.120  62.247  54.544  1.00  6.97           C  
-ATOM   3058  N   MET A 405      18.117  58.637  55.263  1.00 12.00           N  
-ATOM   3059  CA  MET A 405      19.348  58.326  54.539  1.00 10.39           C  
-ATOM   3060  C   MET A 405      19.229  57.001  53.802  1.00 10.10           C  
-ATOM   3061  O   MET A 405      19.838  56.745  52.774  1.00 12.42           O  
-ATOM   3062  CB  MET A 405      20.552  58.236  55.476  1.00  6.38           C  
-ATOM   3063  CG  MET A 405      20.791  59.550  56.205  1.00  8.23           C  
-ATOM   3064  SD  MET A 405      21.080  60.867  55.011  1.00  9.64           S  
-ATOM   3065  CE  MET A 405      22.706  60.365  54.398  1.00  6.69           C  
-ATOM   3066  N   HIS A 406      18.421  56.121  54.352  1.00  8.78           N  
-ATOM   3067  CA  HIS A 406      18.273  54.847  53.674  1.00 14.38           C  
-ATOM   3068  C   HIS A 406      17.589  55.083  52.331  1.00 17.53           C  
-ATOM   3069  O   HIS A 406      18.028  54.641  51.274  1.00 22.81           O  
-ATOM   3070  CB  HIS A 406      17.449  53.885  54.554  1.00 14.21           C  
-ATOM   3071  CG  HIS A 406      17.406  52.506  53.951  1.00 11.97           C  
-ATOM   3072  ND1 HIS A 406      18.492  51.722  53.819  1.00  8.45           N  
-ATOM   3073  CD2 HIS A 406      16.284  51.813  53.440  1.00 10.64           C  
-ATOM   3074  CE1 HIS A 406      18.058  50.585  53.250  1.00 10.91           C  
-ATOM   3075  NE2 HIS A 406      16.734  50.620  53.012  1.00  7.82           N  
-ATOM   3076  N   PHE A 407      16.493  55.848  52.405  1.00 17.65           N  
-ATOM   3077  CA  PHE A 407      15.696  56.164  51.206  1.00 14.69           C  
-ATOM   3078  C   PHE A 407      16.547  56.830  50.161  1.00 14.22           C  
-ATOM   3079  O   PHE A 407      16.575  56.427  49.013  1.00 17.34           O  
-ATOM   3080  CB  PHE A 407      14.542  57.078  51.605  1.00 12.33           C  
-ATOM   3081  CG  PHE A 407      13.625  57.489  50.499  1.00  3.35           C  
-ATOM   3082  CD1 PHE A 407      12.684  56.579  50.008  1.00  5.65           C  
-ATOM   3083  CD2 PHE A 407      13.668  58.801  50.002  1.00  6.05           C  
-ATOM   3084  CE1 PHE A 407      11.771  56.991  49.026  1.00  8.33           C  
-ATOM   3085  CE2 PHE A 407      12.757  59.209  49.016  1.00  9.10           C  
-ATOM   3086  CZ  PHE A 407      11.805  58.305  48.524  1.00  4.46           C  
-ATOM   3087  N   VAL A 408      17.279  57.849  50.591  1.00 12.31           N  
-ATOM   3088  CA  VAL A 408      18.151  58.552  49.671  1.00  9.26           C  
-ATOM   3089  C   VAL A 408      19.090  57.619  48.972  1.00 11.77           C  
-ATOM   3090  O   VAL A 408      19.218  57.638  47.761  1.00 17.89           O  
-ATOM   3091  CB  VAL A 408      18.942  59.613  50.439  1.00  5.68           C  
-ATOM   3092  CG1 VAL A 408      20.075  60.236  49.642  1.00  4.05           C  
-ATOM   3093  CG2 VAL A 408      17.982  60.718  50.857  1.00 15.34           C  
-ATOM   3094  N   ASN A 409      19.735  56.759  49.738  1.00 11.92           N  
-ATOM   3095  CA  ASN A 409      20.667  55.896  49.049  1.00 11.95           C  
-ATOM   3096  C   ASN A 409      20.016  54.975  48.085  1.00 13.78           C  
-ATOM   3097  O   ASN A 409      20.558  54.718  47.022  1.00 17.57           O  
-ATOM   3098  CB  ASN A 409      21.513  55.093  50.010  1.00 17.99           C  
-ATOM   3099  CG  ASN A 409      22.596  56.014  50.523  1.00 27.06           C  
-ATOM   3100  OD1 ASN A 409      23.575  56.287  49.842  1.00 31.47           O  
-ATOM   3101  ND2 ASN A 409      22.413  56.505  51.746  1.00 30.06           N  
-ATOM   3102  N   LYS A 410      18.847  54.458  48.435  1.00 14.56           N  
-ATOM   3103  CA  LYS A 410      18.255  53.555  47.450  1.00 17.00           C  
-ATOM   3104  C   LYS A 410      17.628  54.304  46.266  1.00 17.50           C  
-ATOM   3105  O   LYS A 410      17.487  53.799  45.165  1.00 19.56           O  
-ATOM   3106  CB  LYS A 410      17.248  52.611  48.122  1.00 20.71           C  
-ATOM   3107  CG  LYS A 410      17.908  51.718  49.185  1.00 20.55           C  
-ATOM   3108  CD  LYS A 410      17.452  50.251  49.115  1.00 26.51           C  
-ATOM   3109  CE  LYS A 410      18.611  49.238  49.018  1.00 29.06           C  
-ATOM   3110  NZ  LYS A 410      18.277  48.013  49.749  1.00 39.74           N  
-ATOM   3111  N   TYR A 411      17.242  55.543  46.489  1.00 16.18           N  
-ATOM   3112  CA  TYR A 411      16.627  56.259  45.386  1.00 18.03           C  
-ATOM   3113  C   TYR A 411      17.659  56.751  44.412  1.00 22.49           C  
-ATOM   3114  O   TYR A 411      17.502  56.663  43.201  1.00 22.41           O  
-ATOM   3115  CB  TYR A 411      15.854  57.471  45.904  1.00 11.23           C  
-ATOM   3116  CG  TYR A 411      14.999  58.125  44.836  1.00  5.60           C  
-ATOM   3117  CD1 TYR A 411      13.747  57.578  44.508  1.00  2.08           C  
-ATOM   3118  CD2 TYR A 411      15.428  59.307  44.207  1.00  4.34           C  
-ATOM   3119  CE1 TYR A 411      12.913  58.220  43.586  1.00  4.24           C  
-ATOM   3120  CE2 TYR A 411      14.598  59.950  43.287  1.00  2.00           C  
-ATOM   3121  CZ  TYR A 411      13.344  59.409  42.977  1.00  8.61           C  
-ATOM   3122  OH  TYR A 411      12.557  60.074  42.057  1.00 16.66           O  
-ATOM   3123  N   THR A 412      18.740  57.293  44.956  1.00 24.51           N  
-ATOM   3124  CA  THR A 412      19.797  57.830  44.105  1.00 25.23           C  
-ATOM   3125  C   THR A 412      20.306  56.858  43.091  1.00 22.66           C  
-ATOM   3126  O   THR A 412      20.812  57.270  42.056  1.00 23.24           O  
-ATOM   3127  CB  THR A 412      20.895  58.461  44.978  1.00 24.60           C  
-ATOM   3128  OG1 THR A 412      20.281  59.445  45.809  1.00 26.37           O  
-ATOM   3129  CG2 THR A 412      21.998  59.210  44.205  1.00 26.60           C  
-ATOM   3130  N   LYS A 413      20.163  55.564  43.354  1.00 23.19           N  
-ATOM   3131  CA  LYS A 413      20.682  54.713  42.345  1.00 25.73           C  
-ATOM   3132  C   LYS A 413      19.917  54.864  41.029  1.00 26.73           C  
-ATOM   3133  O   LYS A 413      20.461  54.651  40.014  1.00 28.60           O  
-ATOM   3134  CB  LYS A 413      20.665  53.230  42.754  1.00 24.16           C  
-ATOM   3135  CG  LYS A 413      21.693  52.927  43.883  1.00 27.52           C  
-ATOM   3136  CD  LYS A 413      21.330  51.727  44.779  1.00 36.17           C  
-ATOM   3137  N   PHE A 414      18.623  55.180  41.183  1.00 28.42           N  
-ATOM   3138  CA  PHE A 414      17.814  55.245  39.972  1.00 29.89           C  
-ATOM   3139  C   PHE A 414      17.061  56.556  39.706  1.00 28.33           C  
-ATOM   3140  O   PHE A 414      16.297  56.674  38.736  1.00 31.27           O  
-ATOM   3141  CB  PHE A 414      16.740  54.146  40.065  1.00 32.75           C  
-ATOM   3142  CG  PHE A 414      17.272  52.746  40.301  1.00 37.50           C  
-ATOM   3143  CD1 PHE A 414      18.572  52.276  40.169  1.00 44.88           C  
-ATOM   3144  CD2 PHE A 414      16.344  51.858  40.722  1.00 43.49           C  
-ATOM   3145  CE1 PHE A 414      18.984  51.007  40.512  1.00 50.06           C  
-ATOM   3146  CE2 PHE A 414      16.694  50.529  41.049  1.00 45.95           C  
-ATOM   3147  CZ  PHE A 414      18.030  50.125  40.954  1.00 46.66           C  
-ATOM   3148  N   GLY A 415      17.218  57.553  40.575  1.00 26.12           N  
-ATOM   3149  CA  GLY A 415      16.485  58.772  40.358  1.00 25.57           C  
-ATOM   3150  C   GLY A 415      17.222  59.643  39.391  1.00 25.05           C  
-ATOM   3151  O   GLY A 415      18.299  59.318  38.929  1.00 23.29           O  
-ATOM   3152  N   ASN A 416      16.658  60.812  39.103  1.00 28.85           N  
-ATOM   3153  CA  ASN A 416      17.307  61.714  38.161  1.00 34.03           C  
-ATOM   3154  C   ASN A 416      17.867  62.946  38.848  1.00 33.90           C  
-ATOM   3155  O   ASN A 416      17.753  64.054  38.351  1.00 35.24           O  
-ATOM   3156  CB  ASN A 416      16.331  62.053  36.999  1.00 39.49           C  
-ATOM   3157  CG  ASN A 416      16.946  62.694  35.738  1.00 42.24           C  
-ATOM   3158  OD1 ASN A 416      16.387  63.603  35.139  1.00 46.71           O  
-ATOM   3159  ND2 ASN A 416      18.100  62.178  35.308  1.00 38.36           N  
-ATOM   3160  N   GLY A 417      18.467  62.755  40.028  1.00 37.53           N  
-ATOM   3161  CA  GLY A 417      19.061  63.874  40.788  1.00 35.91           C  
-ATOM   3162  C   GLY A 417      18.572  63.903  42.225  1.00 30.56           C  
-ATOM   3163  O   GLY A 417      17.407  63.631  42.488  1.00 29.49           O  
-ATOM   3164  N   THR A 418      19.465  64.226  43.162  1.00 27.58           N  
-ATOM   3165  CA  THR A 418      19.038  64.247  44.557  1.00 27.31           C  
-ATOM   3166  C   THR A 418      19.764  65.383  45.256  1.00 25.21           C  
-ATOM   3167  O   THR A 418      20.978  65.478  45.111  1.00 26.31           O  
-ATOM   3168  CB  THR A 418      19.424  62.879  45.187  1.00 23.65           C  
-ATOM   3169  OG1 THR A 418      18.789  61.811  44.470  1.00 29.40           O  
-ATOM   3170  CG2 THR A 418      19.017  62.701  46.648  1.00 21.43           C  
-ATOM   3171  N   TYR A 419      19.030  66.227  45.997  1.00 22.29           N  
-ATOM   3172  CA  TYR A 419      19.643  67.346  46.738  1.00 25.88           C  
-ATOM   3173  C   TYR A 419      19.254  67.124  48.199  1.00 25.80           C  
-ATOM   3174  O   TYR A 419      18.079  66.883  48.465  1.00 27.82           O  
-ATOM   3175  CB  TYR A 419      19.164  68.702  46.184  1.00 30.13           C  
-ATOM   3176  CG  TYR A 419      19.512  68.841  44.711  1.00 29.73           C  
-ATOM   3177  CD1 TYR A 419      18.600  68.368  43.751  1.00 31.80           C  
-ATOM   3178  CD2 TYR A 419      20.734  69.407  44.287  1.00 26.44           C  
-ATOM   3179  CE1 TYR A 419      18.899  68.453  42.387  1.00 32.84           C  
-ATOM   3180  CE2 TYR A 419      21.036  69.489  42.917  1.00 27.55           C  
-ATOM   3181  CZ  TYR A 419      20.114  69.013  41.961  1.00 31.05           C  
-ATOM   3182  OH  TYR A 419      20.364  69.090  40.602  1.00 31.88           O  
-ATOM   3183  N   LEU A 420      20.228  67.176  49.121  1.00 19.41           N  
-ATOM   3184  CA  LEU A 420      20.014  66.915  50.540  1.00 17.98           C  
-ATOM   3185  C   LEU A 420      20.492  68.074  51.392  1.00 19.04           C  
-ATOM   3186  O   LEU A 420      21.580  68.595  51.158  1.00 16.48           O  
-ATOM   3187  CB  LEU A 420      20.834  65.657  50.884  1.00 13.19           C  
-ATOM   3188  CG  LEU A 420      20.683  65.139  52.324  1.00 13.97           C  
-ATOM   3189  CD1 LEU A 420      19.221  64.883  52.694  1.00 13.11           C  
-ATOM   3190  CD2 LEU A 420      21.501  63.860  52.553  1.00  9.68           C  
-ATOM   3191  N   TYR A 421      19.674  68.470  52.388  1.00 20.00           N  
-ATOM   3192  CA  TYR A 421      20.041  69.576  53.300  1.00 21.21           C  
-ATOM   3193  C   TYR A 421      19.942  69.123  54.759  1.00 22.16           C  
-ATOM   3194  O   TYR A 421      19.268  68.147  55.083  1.00 27.68           O  
-ATOM   3195  CB  TYR A 421      19.160  70.825  53.113  1.00 18.16           C  
-ATOM   3196  CG  TYR A 421      17.717  70.594  53.501  1.00 20.61           C  
-ATOM   3197  CD1 TYR A 421      16.780  70.057  52.595  1.00 18.30           C  
-ATOM   3198  CD2 TYR A 421      17.312  70.898  54.806  1.00 17.41           C  
-ATOM   3199  CE1 TYR A 421      15.451  69.838  53.002  1.00 18.02           C  
-ATOM   3200  CE2 TYR A 421      15.996  70.665  55.207  1.00 18.17           C  
-ATOM   3201  CZ  TYR A 421      15.057  70.145  54.313  1.00 17.49           C  
-ATOM   3202  OH  TYR A 421      13.749  69.954  54.734  1.00 23.43           O  
-ATOM   3203  N   PHE A 422      20.608  69.887  55.631  1.00 19.35           N  
-ATOM   3204  CA  PHE A 422      20.637  69.652  57.073  1.00 16.89           C  
-ATOM   3205  C   PHE A 422      20.322  71.005  57.627  1.00 15.31           C  
-ATOM   3206  O   PHE A 422      21.156  71.895  57.543  1.00 17.01           O  
-ATOM   3207  CB  PHE A 422      22.054  69.215  57.459  1.00 17.68           C  
-ATOM   3208  CG  PHE A 422      22.178  68.850  58.909  1.00 18.34           C  
-ATOM   3209  CD1 PHE A 422      21.524  67.705  59.394  1.00 17.93           C  
-ATOM   3210  CD2 PHE A 422      22.957  69.638  59.779  1.00 20.27           C  
-ATOM   3211  CE1 PHE A 422      21.650  67.347  60.742  1.00 16.41           C  
-ATOM   3212  CE2 PHE A 422      23.087  69.277  61.123  1.00 16.33           C  
-ATOM   3213  CZ  PHE A 422      22.431  68.132  61.601  1.00 17.51           C  
-ATOM   3214  N   PHE A 423      19.102  71.191  58.111  1.00 14.66           N  
-ATOM   3215  CA  PHE A 423      18.694  72.484  58.631  1.00 16.94           C  
-ATOM   3216  C   PHE A 423      19.040  72.523  60.103  1.00 20.96           C  
-ATOM   3217  O   PHE A 423      18.555  71.738  60.923  1.00 26.49           O  
-ATOM   3218  CB  PHE A 423      17.200  72.684  58.390  1.00 12.96           C  
-ATOM   3219  CG  PHE A 423      16.724  74.040  58.834  1.00 12.99           C  
-ATOM   3220  CD1 PHE A 423      16.886  75.165  58.004  1.00 14.02           C  
-ATOM   3221  CD2 PHE A 423      16.100  74.192  60.080  1.00 17.13           C  
-ATOM   3222  CE1 PHE A 423      16.416  76.428  58.401  1.00 11.33           C  
-ATOM   3223  CE2 PHE A 423      15.623  75.456  60.481  1.00 20.89           C  
-ATOM   3224  CZ  PHE A 423      15.778  76.573  59.637  1.00 15.84           C  
-ATOM   3225  N   ASN A 424      19.894  73.481  60.441  1.00 18.24           N  
-ATOM   3226  CA  ASN A 424      20.337  73.577  61.812  1.00 14.83           C  
-ATOM   3227  C   ASN A 424      20.403  74.990  62.302  1.00 12.86           C  
-ATOM   3228  O   ASN A 424      21.415  75.403  62.828  1.00 16.41           O  
-ATOM   3229  CB  ASN A 424      21.694  72.892  61.978  1.00  9.86           C  
-ATOM   3230  CG  ASN A 424      22.744  73.517  61.102  1.00 14.25           C  
-ATOM   3231  OD1 ASN A 424      22.489  74.376  60.268  1.00 19.01           O  
-ATOM   3232  ND2 ASN A 424      23.976  73.051  61.272  1.00 17.43           N  
-ATOM   3233  N   HIS A 425      19.324  75.737  62.152  1.00 14.01           N  
-ATOM   3234  CA  HIS A 425      19.291  77.111  62.619  1.00 14.70           C  
-ATOM   3235  C   HIS A 425      18.127  77.227  63.581  1.00 20.28           C  
-ATOM   3236  O   HIS A 425      17.025  76.743  63.342  1.00 22.87           O  
-ATOM   3237  CB  HIS A 425      19.069  78.038  61.424  1.00 13.69           C  
-ATOM   3238  CG  HIS A 425      18.758  79.457  61.849  1.00 16.20           C  
-ATOM   3239  ND1 HIS A 425      19.673  80.364  62.264  1.00 14.43           N  
-ATOM   3240  CD2 HIS A 425      17.483  80.067  61.888  1.00 16.15           C  
-ATOM   3241  CE1 HIS A 425      18.988  81.491  62.540  1.00 13.89           C  
-ATOM   3242  NE2 HIS A 425      17.667  81.335  62.316  1.00 13.71           N  
-ATOM   3243  N   ARG A 426      18.386  77.897  64.696  1.00 24.28           N  
-ATOM   3244  CA  ARG A 426      17.337  78.083  65.683  1.00 27.35           C  
-ATOM   3245  C   ARG A 426      16.832  79.506  65.509  1.00 27.39           C  
-ATOM   3246  O   ARG A 426      17.588  80.471  65.630  1.00 26.12           O  
-ATOM   3247  CB  ARG A 426      17.902  77.842  67.106  1.00 30.12           C  
-ATOM   3248  CG  ARG A 426      16.810  77.838  68.200  1.00 36.19           C  
-ATOM   3249  CD  ARG A 426      17.260  77.301  69.568  1.00 36.30           C  
-ATOM   3250  NE  ARG A 426      16.233  77.525  70.574  1.00 39.87           N  
-ATOM   3251  CZ  ARG A 426      16.103  78.735  71.150  1.00 44.86           C  
-ATOM   3252  NH1 ARG A 426      16.896  79.766  70.825  1.00 45.41           N  
-ATOM   3253  NH2 ARG A 426      15.158  78.908  72.068  1.00 46.68           N  
-ATOM   3254  N   ALA A 427      15.526  79.628  65.219  1.00 25.42           N  
-ATOM   3255  CA  ALA A 427      15.003  80.979  65.054  1.00 24.06           C  
-ATOM   3256  C   ALA A 427      15.285  81.755  66.302  1.00 24.95           C  
-ATOM   3257  O   ALA A 427      15.147  81.236  67.399  1.00 23.58           O  
-ATOM   3258  CB  ALA A 427      13.487  81.020  64.833  1.00 21.86           C  
-ATOM   3259  N   SER A 428      15.636  83.023  66.100  1.00 27.92           N  
-ATOM   3260  CA  SER A 428      15.952  83.883  67.235  1.00 27.44           C  
-ATOM   3261  C   SER A 428      14.768  84.113  68.163  1.00 27.61           C  
-ATOM   3262  O   SER A 428      14.926  84.401  69.339  1.00 33.83           O  
-ATOM   3263  CB  SER A 428      16.575  85.213  66.778  1.00 25.08           C  
-ATOM   3264  OG  SER A 428      15.802  85.842  65.750  1.00 27.48           O  
-ATOM   3265  N   ASN A 429      13.572  83.993  67.608  1.00 25.58           N  
-ATOM   3266  CA  ASN A 429      12.360  84.182  68.382  1.00 26.14           C  
-ATOM   3267  C   ASN A 429      11.719  82.855  68.810  1.00 29.45           C  
-ATOM   3268  O   ASN A 429      10.538  82.806  69.149  1.00 31.59           O  
-ATOM   3269  CB  ASN A 429      11.360  85.021  67.566  1.00 27.84           C  
-ATOM   3270  CG  ASN A 429      11.162  84.534  66.142  1.00 30.89           C  
-ATOM   3271  OD1 ASN A 429      11.689  83.507  65.720  1.00 28.88           O  
-ATOM   3272  ND2 ASN A 429      10.414  85.321  65.380  1.00 31.96           N  
-ATOM   3273  N   LEU A 430      12.494  81.755  68.801  1.00 27.22           N  
-ATOM   3274  CA  LEU A 430      11.872  80.491  69.183  1.00 24.25           C  
-ATOM   3275  C   LEU A 430      11.330  80.608  70.604  1.00 25.62           C  
-ATOM   3276  O   LEU A 430      12.050  81.102  71.463  1.00 28.75           O  
-ATOM   3277  CB  LEU A 430      12.928  79.358  69.116  1.00 22.89           C  
-ATOM   3278  CG  LEU A 430      12.497  78.024  68.491  1.00 21.01           C  
-ATOM   3279  CD1 LEU A 430      11.098  77.558  68.878  1.00 25.25           C  
-ATOM   3280  CD2 LEU A 430      12.610  78.064  66.978  1.00 32.12           C  
-ATOM   3281  N   VAL A 431      10.083  80.155  70.846  1.00 24.53           N  
-ATOM   3282  CA  VAL A 431       9.550  80.220  72.222  1.00 23.47           C  
-ATOM   3283  C   VAL A 431       9.752  78.924  73.018  1.00 20.42           C  
-ATOM   3284  O   VAL A 431       9.338  78.790  74.157  1.00 22.54           O  
-ATOM   3285  CB  VAL A 431       8.045  80.571  72.220  1.00 20.23           C  
-ATOM   3286  CG1 VAL A 431       7.851  81.943  71.578  1.00 24.35           C  
-ATOM   3287  CG2 VAL A 431       7.178  79.519  71.508  1.00 17.82           C  
-ATOM   3288  N   TRP A 432      10.322  77.925  72.377  1.00 16.34           N  
-ATOM   3289  CA  TRP A 432      10.549  76.664  73.056  1.00 14.40           C  
-ATOM   3290  C   TRP A 432      11.928  76.825  73.709  1.00 13.99           C  
-ATOM   3291  O   TRP A 432      12.698  77.677  73.290  1.00 13.34           O  
-ATOM   3292  CB  TRP A 432      10.491  75.491  72.050  1.00 11.71           C  
-ATOM   3293  CG  TRP A 432       9.087  75.215  71.549  1.00 13.78           C  
-ATOM   3294  CD1 TRP A 432       8.494  75.696  70.352  1.00 14.89           C  
-ATOM   3295  CD2 TRP A 432       8.113  74.417  72.184  1.00 15.44           C  
-ATOM   3296  NE1 TRP A 432       7.217  75.230  70.222  1.00 13.83           N  
-ATOM   3297  CE2 TRP A 432       6.919  74.434  71.305  1.00 16.22           C  
-ATOM   3298  CE3 TRP A 432       8.058  73.711  73.388  1.00 16.05           C  
-ATOM   3299  CZ2 TRP A 432       5.771  73.727  71.707  1.00 14.52           C  
-ATOM   3300  CZ3 TRP A 432       6.884  73.027  73.752  1.00 15.01           C  
-ATOM   3301  CH2 TRP A 432       5.757  73.028  72.921  1.00 12.98           C  
-ATOM   3302  N   PRO A 433      12.245  76.018  74.743  1.00 12.67           N  
-ATOM   3303  CA  PRO A 433      13.523  76.153  75.404  1.00  9.19           C  
-ATOM   3304  C   PRO A 433      14.678  75.802  74.534  1.00 12.11           C  
-ATOM   3305  O   PRO A 433      14.623  74.982  73.635  1.00 21.23           O  
-ATOM   3306  CB  PRO A 433      13.459  75.154  76.556  1.00  8.32           C  
-ATOM   3307  CG  PRO A 433      12.309  74.202  76.229  1.00  4.90           C  
-ATOM   3308  CD  PRO A 433      11.370  75.011  75.342  1.00  9.63           C  
-ATOM   3309  N   GLU A 434      15.797  76.398  74.910  1.00 15.38           N  
-ATOM   3310  CA  GLU A 434      17.052  76.209  74.207  1.00 14.21           C  
-ATOM   3311  C   GLU A 434      17.471  74.746  74.132  1.00 13.83           C  
-ATOM   3312  O   GLU A 434      18.152  74.354  73.203  1.00 17.17           O  
-ATOM   3313  CB  GLU A 434      18.131  77.082  74.901  1.00 12.25           C  
-ATOM   3314  CG  GLU A 434      19.471  77.250  74.154  1.00 20.68           C  
-ATOM   3315  N   TRP A 435      17.062  73.930  75.109  1.00 13.60           N  
-ATOM   3316  CA  TRP A 435      17.525  72.544  75.044  1.00 13.74           C  
-ATOM   3317  C   TRP A 435      16.939  71.785  73.877  1.00 16.40           C  
-ATOM   3318  O   TRP A 435      17.517  70.819  73.400  1.00 23.41           O  
-ATOM   3319  CB  TRP A 435      17.391  71.777  76.402  1.00 13.33           C  
-ATOM   3320  CG  TRP A 435      15.962  71.442  76.812  1.00  7.61           C  
-ATOM   3321  CD1 TRP A 435      15.117  72.204  77.650  1.00  5.44           C  
-ATOM   3322  CD2 TRP A 435      15.215  70.325  76.407  1.00  5.75           C  
-ATOM   3323  NE1 TRP A 435      13.895  71.623  77.769  1.00  2.00           N  
-ATOM   3324  CE2 TRP A 435      13.876  70.476  77.028  1.00  4.00           C  
-ATOM   3325  CE3 TRP A 435      15.492  69.206  75.613  1.00  5.40           C  
-ATOM   3326  CZ2 TRP A 435      12.889  69.511  76.783  1.00  5.82           C  
-ATOM   3327  CZ3 TRP A 435      14.484  68.250  75.403  1.00  9.91           C  
-ATOM   3328  CH2 TRP A 435      13.197  68.405  75.967  1.00  8.73           C  
-ATOM   3329  N   MET A 436      15.758  72.216  73.436  1.00 16.03           N  
-ATOM   3330  CA  MET A 436      15.126  71.534  72.318  1.00 17.89           C  
-ATOM   3331  C   MET A 436      15.859  71.830  70.984  1.00 20.10           C  
-ATOM   3332  O   MET A 436      15.715  71.137  69.985  1.00 20.80           O  
-ATOM   3333  CB  MET A 436      13.632  71.873  72.286  1.00 14.73           C  
-ATOM   3334  CG  MET A 436      12.913  71.395  73.543  1.00 10.31           C  
-ATOM   3335  SD  MET A 436      11.190  71.974  73.524  1.00 13.56           S  
-ATOM   3336  CE  MET A 436      10.487  70.820  72.309  1.00 13.12           C  
-ATOM   3337  N   GLY A 437      16.660  72.895  70.964  1.00 20.64           N  
-ATOM   3338  CA  GLY A 437      17.403  73.168  69.739  1.00 18.75           C  
-ATOM   3339  C   GLY A 437      16.552  73.492  68.521  1.00 17.03           C  
-ATOM   3340  O   GLY A 437      15.594  74.256  68.593  1.00 18.08           O  
-ATOM   3341  N   VAL A 438      16.977  72.905  67.382  1.00 12.62           N  
-ATOM   3342  CA  VAL A 438      16.330  73.055  66.081  1.00  9.94           C  
-ATOM   3343  C   VAL A 438      15.270  71.965  66.028  1.00  6.84           C  
-ATOM   3344  O   VAL A 438      15.538  70.830  65.653  1.00  2.00           O  
-ATOM   3345  CB  VAL A 438      17.385  72.902  64.976  1.00  6.49           C  
-ATOM   3346  CG1 VAL A 438      16.813  73.247  63.604  1.00 12.47           C  
-ATOM   3347  CG2 VAL A 438      18.622  73.766  65.262  1.00  4.15           C  
-ATOM   3348  N   ILE A 439      14.062  72.371  66.379  1.00  8.21           N  
-ATOM   3349  CA  ILE A 439      12.963  71.434  66.493  1.00  9.83           C  
-ATOM   3350  C   ILE A 439      12.315  70.981  65.199  1.00 12.68           C  
-ATOM   3351  O   ILE A 439      12.240  71.645  64.166  1.00 17.50           O  
-ATOM   3352  CB  ILE A 439      11.928  72.134  67.412  1.00  8.73           C  
-ATOM   3353  CG1 ILE A 439      12.536  72.553  68.764  1.00  5.52           C  
-ATOM   3354  CG2 ILE A 439      10.641  71.337  67.687  1.00  9.39           C  
-ATOM   3355  CD1 ILE A 439      11.738  73.672  69.435  1.00  2.00           C  
-ATOM   3356  N   HIS A 440      11.787  69.767  65.315  1.00 10.68           N  
-ATOM   3357  CA  HIS A 440      11.053  69.108  64.252  1.00  9.48           C  
-ATOM   3358  C   HIS A 440       9.911  70.051  63.934  1.00  9.31           C  
-ATOM   3359  O   HIS A 440       9.208  70.462  64.829  1.00  8.12           O  
-ATOM   3360  CB  HIS A 440      10.550  67.777  64.839  1.00  8.57           C  
-ATOM   3361  CG  HIS A 440       9.657  66.946  63.948  1.00  7.99           C  
-ATOM   3362  ND1 HIS A 440      10.086  66.014  63.073  1.00  6.63           N  
-ATOM   3363  CD2 HIS A 440       8.240  66.895  63.984  1.00  9.96           C  
-ATOM   3364  CE1 HIS A 440       8.975  65.395  62.600  1.00 12.43           C  
-ATOM   3365  NE2 HIS A 440       7.845  65.912  63.137  1.00 10.39           N  
-ATOM   3366  N   GLY A 441       9.782  70.443  62.665  1.00 12.04           N  
-ATOM   3367  CA  GLY A 441       8.713  71.358  62.293  1.00  8.35           C  
-ATOM   3368  C   GLY A 441       9.180  72.772  62.174  1.00  8.92           C  
-ATOM   3369  O   GLY A 441       8.565  73.583  61.507  1.00  9.77           O  
-ATOM   3370  N   TYR A 442      10.356  73.065  62.706  1.00  8.66           N  
-ATOM   3371  CA  TYR A 442      10.755  74.475  62.684  1.00 11.82           C  
-ATOM   3372  C   TYR A 442      11.364  75.119  61.445  1.00 13.54           C  
-ATOM   3373  O   TYR A 442      11.672  76.305  61.457  1.00 20.09           O  
-ATOM   3374  CB  TYR A 442      11.369  74.815  64.079  1.00 11.19           C  
-ATOM   3375  CG  TYR A 442      10.204  74.997  65.047  1.00  7.21           C  
-ATOM   3376  CD1 TYR A 442       9.504  73.889  65.567  1.00  5.33           C  
-ATOM   3377  CD2 TYR A 442       9.715  76.291  65.292  1.00  2.00           C  
-ATOM   3378  CE1 TYR A 442       8.320  74.070  66.286  1.00  2.00           C  
-ATOM   3379  CE2 TYR A 442       8.531  76.476  66.001  1.00  2.00           C  
-ATOM   3380  CZ  TYR A 442       7.836  75.369  66.490  1.00  4.13           C  
-ATOM   3381  OH  TYR A 442       6.660  75.593  67.164  1.00 13.11           O  
-ATOM   3382  N   GLU A 443      11.519  74.358  60.342  1.00 15.74           N  
-ATOM   3383  CA  GLU A 443      12.072  74.942  59.086  1.00  7.98           C  
-ATOM   3384  C   GLU A 443      10.944  75.473  58.230  1.00  5.61           C  
-ATOM   3385  O   GLU A 443      11.091  76.316  57.364  1.00  7.19           O  
-ATOM   3386  CB  GLU A 443      12.889  73.972  58.219  1.00  9.60           C  
-ATOM   3387  CG  GLU A 443      12.093  72.991  57.312  1.00  7.55           C  
-ATOM   3388  CD  GLU A 443      11.196  72.053  58.088  1.00  6.46           C  
-ATOM   3389  OE1 GLU A 443      11.514  71.797  59.235  1.00  8.12           O  
-ATOM   3390  OE2 GLU A 443      10.196  71.582  57.551  1.00  6.22           O  
-ATOM   3391  N   ILE A 444       9.757  74.944  58.494  1.00  3.67           N  
-ATOM   3392  CA  ILE A 444       8.602  75.371  57.745  1.00  2.76           C  
-ATOM   3393  C   ILE A 444       8.391  76.890  57.829  1.00  6.05           C  
-ATOM   3394  O   ILE A 444       7.849  77.504  56.938  1.00  9.34           O  
-ATOM   3395  CB  ILE A 444       7.359  74.564  58.209  1.00  2.00           C  
-ATOM   3396  CG1 ILE A 444       7.604  73.028  58.241  1.00  5.67           C  
-ATOM   3397  CG2 ILE A 444       6.150  74.919  57.348  1.00  3.61           C  
-ATOM   3398  CD1 ILE A 444       6.379  72.173  58.631  1.00  2.00           C  
-ATOM   3399  N   GLU A 445       8.840  77.540  58.906  1.00 16.65           N  
-ATOM   3400  CA  GLU A 445       8.601  78.992  58.980  1.00 17.10           C  
-ATOM   3401  C   GLU A 445       9.356  79.694  57.924  1.00 14.25           C  
-ATOM   3402  O   GLU A 445       8.937  80.729  57.438  1.00  8.96           O  
-ATOM   3403  CB  GLU A 445       9.088  79.671  60.292  1.00 24.89           C  
-ATOM   3404  CG  GLU A 445       8.687  78.932  61.563  1.00 25.68           C  
-ATOM   3405  CD  GLU A 445       9.181  79.521  62.848  1.00 31.64           C  
-ATOM   3406  OE1 GLU A 445      10.321  79.998  62.881  1.00 28.92           O  
-ATOM   3407  OE2 GLU A 445       8.421  79.476  63.819  1.00 35.91           O  
-ATOM   3408  N   PHE A 446      10.512  79.084  57.639  1.00 14.43           N  
-ATOM   3409  CA  PHE A 446      11.436  79.601  56.650  1.00 17.47           C  
-ATOM   3410  C   PHE A 446      10.935  79.364  55.231  1.00 17.92           C  
-ATOM   3411  O   PHE A 446      10.854  80.285  54.429  1.00 17.24           O  
-ATOM   3412  CB  PHE A 446      12.841  79.006  56.892  1.00 14.25           C  
-ATOM   3413  CG  PHE A 446      13.479  79.696  58.073  1.00 18.46           C  
-ATOM   3414  CD1 PHE A 446      13.109  79.356  59.382  1.00 21.45           C  
-ATOM   3415  CD2 PHE A 446      14.397  80.744  57.865  1.00 17.73           C  
-ATOM   3416  CE1 PHE A 446      13.632  80.089  60.462  1.00 25.35           C  
-ATOM   3417  CE2 PHE A 446      14.922  81.463  58.941  1.00 16.63           C  
-ATOM   3418  CZ  PHE A 446      14.533  81.146  60.246  1.00 17.92           C  
-ATOM   3419  N   VAL A 447      10.587  78.103  54.953  1.00 15.23           N  
-ATOM   3420  CA  VAL A 447      10.097  77.751  53.637  1.00 11.34           C  
-ATOM   3421  C   VAL A 447       8.867  78.578  53.236  1.00 13.43           C  
-ATOM   3422  O   VAL A 447       8.675  78.844  52.058  1.00 18.88           O  
-ATOM   3423  CB  VAL A 447       9.843  76.228  53.599  1.00  9.38           C  
-ATOM   3424  CG1 VAL A 447       9.027  75.750  52.392  1.00  4.32           C  
-ATOM   3425  CG2 VAL A 447      11.168  75.435  53.691  1.00  3.90           C  
-ATOM   3426  N   PHE A 448       8.042  78.981  54.207  1.00  4.53           N  
-ATOM   3427  CA  PHE A 448       6.869  79.755  53.840  1.00  3.52           C  
-ATOM   3428  C   PHE A 448       7.071  81.254  53.952  1.00  7.21           C  
-ATOM   3429  O   PHE A 448       6.141  82.041  53.829  1.00 10.21           O  
-ATOM   3430  CB  PHE A 448       5.622  79.283  54.591  1.00  3.13           C  
-ATOM   3431  CG  PHE A 448       4.956  78.088  53.952  1.00  3.83           C  
-ATOM   3432  CD1 PHE A 448       5.567  76.827  53.991  1.00  2.43           C  
-ATOM   3433  CD2 PHE A 448       3.705  78.237  53.307  1.00  6.22           C  
-ATOM   3434  CE1 PHE A 448       4.929  75.722  53.393  1.00  9.88           C  
-ATOM   3435  CE2 PHE A 448       3.070  77.138  52.709  1.00  5.13           C  
-ATOM   3436  CZ  PHE A 448       3.685  75.876  52.751  1.00  8.76           C  
-ATOM   3437  N   GLY A 449       8.302  81.669  54.212  1.00 12.35           N  
-ATOM   3438  CA  GLY A 449       8.601  83.113  54.262  1.00 19.06           C  
-ATOM   3439  C   GLY A 449       8.035  83.979  55.378  1.00 22.16           C  
-ATOM   3440  O   GLY A 449       7.885  85.192  55.224  1.00 23.38           O  
-ATOM   3441  N   LEU A 450       7.735  83.363  56.538  1.00 23.86           N  
-ATOM   3442  CA  LEU A 450       7.219  84.190  57.634  1.00 20.32           C  
-ATOM   3443  C   LEU A 450       8.256  85.211  58.121  1.00 17.70           C  
-ATOM   3444  O   LEU A 450       7.883  86.310  58.488  1.00 16.68           O  
-ATOM   3445  CB  LEU A 450       6.676  83.381  58.824  1.00 18.87           C  
-ATOM   3446  CG  LEU A 450       5.459  82.475  58.544  1.00 19.02           C  
-ATOM   3447  CD1 LEU A 450       4.479  82.480  59.723  1.00 23.46           C  
-ATOM   3448  CD2 LEU A 450       4.688  82.824  57.271  1.00 23.14           C  
-ATOM   3449  N   PRO A 451       9.564  84.906  58.111  1.00 16.06           N  
-ATOM   3450  CA  PRO A 451      10.523  85.973  58.367  1.00 20.20           C  
-ATOM   3451  C   PRO A 451      10.389  87.265  57.568  1.00 25.32           C  
-ATOM   3452  O   PRO A 451      10.988  88.278  57.919  1.00 30.73           O  
-ATOM   3453  CB  PRO A 451      11.898  85.312  58.167  1.00 16.42           C  
-ATOM   3454  CG  PRO A 451      11.663  83.804  58.374  1.00 13.92           C  
-ATOM   3455  CD  PRO A 451      10.182  83.586  58.012  1.00 15.33           C  
-ATOM   3456  N   LEU A 452       9.636  87.218  56.456  1.00 30.14           N  
-ATOM   3457  CA  LEU A 452       9.477  88.436  55.666  1.00 31.12           C  
-ATOM   3458  C   LEU A 452       8.561  89.402  56.374  1.00 32.76           C  
-ATOM   3459  O   LEU A 452       8.601  90.608  56.162  1.00 34.65           O  
-ATOM   3460  CB  LEU A 452       8.945  88.149  54.262  1.00 28.34           C  
-ATOM   3461  CG  LEU A 452       9.855  87.242  53.419  1.00 25.04           C  
-ATOM   3462  CD1 LEU A 452       9.640  87.572  51.947  1.00 29.84           C  
-ATOM   3463  CD2 LEU A 452      11.347  87.363  53.738  1.00 21.13           C  
-ATOM   3464  N   VAL A 453       7.715  88.831  57.230  1.00 33.50           N  
-ATOM   3465  CA  VAL A 453       6.785  89.616  58.003  1.00 35.18           C  
-ATOM   3466  C   VAL A 453       7.585  90.214  59.143  1.00 37.58           C  
-ATOM   3467  O   VAL A 453       7.915  89.555  60.116  1.00 41.33           O  
-ATOM   3468  CB  VAL A 453       5.670  88.683  58.497  1.00 33.52           C  
-ATOM   3469  CG1 VAL A 453       4.555  89.448  59.213  1.00 36.53           C  
-ATOM   3470  CG2 VAL A 453       5.056  87.869  57.338  1.00 35.81           C  
-ATOM   3471  N   LYS A 454       7.877  91.503  59.035  1.00 42.92           N  
-ATOM   3472  CA  LYS A 454       8.669  92.165  60.076  1.00 47.90           C  
-ATOM   3473  C   LYS A 454       8.020  92.125  61.467  1.00 47.66           C  
-ATOM   3474  O   LYS A 454       8.691  92.052  62.489  1.00 47.79           O  
-ATOM   3475  CB  LYS A 454       9.056  93.591  59.627  1.00 51.97           C  
-ATOM   3476  CG  LYS A 454       9.627  93.678  58.174  1.00 61.84           C  
-ATOM   3477  CD  LYS A 454      11.067  93.135  57.962  1.00 65.28           C  
-ATOM   3478  CE  LYS A 454      11.212  91.600  57.792  1.00 69.26           C  
-ATOM   3479  NZ  LYS A 454      12.612  91.209  57.883  1.00 74.01           N  
-ATOM   3480  N   GLU A 455       6.675  92.124  61.481  1.00 45.37           N  
-ATOM   3481  CA  GLU A 455       5.960  92.071  62.763  1.00 38.25           C  
-ATOM   3482  C   GLU A 455       6.248  90.803  63.540  1.00 35.88           C  
-ATOM   3483  O   GLU A 455       5.957  90.725  64.719  1.00 37.11           O  
-ATOM   3484  CB  GLU A 455       4.420  92.127  62.657  1.00 37.95           C  
-ATOM   3485  N   LEU A 456       6.810  89.791  62.886  1.00 31.87           N  
-ATOM   3486  CA  LEU A 456       7.071  88.568  63.621  1.00 30.70           C  
-ATOM   3487  C   LEU A 456       8.401  88.558  64.368  1.00 32.17           C  
-ATOM   3488  O   LEU A 456       8.719  87.593  65.061  1.00 30.98           O  
-ATOM   3489  CB  LEU A 456       6.879  87.370  62.708  1.00 30.84           C  
-ATOM   3490  CG  LEU A 456       5.485  87.371  62.068  1.00 31.62           C  
-ATOM   3491  CD1 LEU A 456       5.310  86.161  61.149  1.00 36.79           C  
-ATOM   3492  CD2 LEU A 456       4.328  87.460  63.076  1.00 27.13           C  
-ATOM   3493  N   ASN A 457       9.185  89.624  64.218  1.00 31.39           N  
-ATOM   3494  CA  ASN A 457      10.453  89.752  64.958  1.00 35.14           C  
-ATOM   3495  C   ASN A 457      11.590  88.804  64.619  1.00 32.17           C  
-ATOM   3496  O   ASN A 457      12.171  88.197  65.517  1.00 32.00           O  
-ATOM   3497  CB  ASN A 457      10.273  89.624  66.508  1.00 43.52           C  
-ATOM   3498  CG  ASN A 457       9.348  90.650  67.137  1.00 49.23           C  
-ATOM   3499  OD1 ASN A 457       9.710  91.802  67.325  1.00 54.33           O  
-ATOM   3500  ND2 ASN A 457       8.133  90.219  67.469  1.00 51.90           N  
-ATOM   3501  N   TYR A 458      11.913  88.633  63.338  1.00 28.42           N  
-ATOM   3502  CA  TYR A 458      13.045  87.738  63.059  1.00 25.04           C  
-ATOM   3503  C   TYR A 458      14.182  88.661  62.723  1.00 24.07           C  
-ATOM   3504  O   TYR A 458      13.974  89.827  62.420  1.00 25.65           O  
-ATOM   3505  CB  TYR A 458      12.794  86.785  61.881  1.00 20.00           C  
-ATOM   3506  CG  TYR A 458      11.774  85.705  62.144  1.00 15.51           C  
-ATOM   3507  CD1 TYR A 458      10.402  85.989  61.988  1.00 15.40           C  
-ATOM   3508  CD2 TYR A 458      12.175  84.390  62.453  1.00 12.32           C  
-ATOM   3509  CE1 TYR A 458       9.447  84.962  62.057  1.00 11.67           C  
-ATOM   3510  CE2 TYR A 458      11.221  83.364  62.531  1.00 12.05           C  
-ATOM   3511  CZ  TYR A 458       9.861  83.644  62.307  1.00 12.36           C  
-ATOM   3512  OH  TYR A 458       8.926  82.623  62.289  1.00 16.52           O  
-ATOM   3513  N   THR A 459      15.397  88.146  62.764  1.00 25.51           N  
-ATOM   3514  CA  THR A 459      16.491  89.042  62.421  1.00 30.49           C  
-ATOM   3515  C   THR A 459      16.556  89.189  60.907  1.00 34.22           C  
-ATOM   3516  O   THR A 459      16.074  88.354  60.138  1.00 38.20           O  
-ATOM   3517  CB  THR A 459      17.828  88.505  62.978  1.00 31.63           C  
-ATOM   3518  OG1 THR A 459      18.006  87.127  62.639  1.00 32.54           O  
-ATOM   3519  CG2 THR A 459      17.895  88.568  64.503  1.00 37.27           C  
-ATOM   3520  N   ALA A 460      17.256  90.250  60.485  1.00 35.28           N  
-ATOM   3521  CA  ALA A 460      17.392  90.463  59.049  1.00 31.19           C  
-ATOM   3522  C   ALA A 460      18.147  89.318  58.423  1.00 31.00           C  
-ATOM   3523  O   ALA A 460      17.868  88.901  57.311  1.00 36.66           O  
-ATOM   3524  CB  ALA A 460      18.138  91.756  58.740  1.00 31.44           C  
-ATOM   3525  N   GLU A 461      19.120  88.794  59.182  1.00 26.39           N  
-ATOM   3526  CA  GLU A 461      19.890  87.674  58.654  1.00 23.78           C  
-ATOM   3527  C   GLU A 461      18.974  86.461  58.393  1.00 23.06           C  
-ATOM   3528  O   GLU A 461      19.246  85.601  57.572  1.00 26.98           O  
-ATOM   3529  CB  GLU A 461      21.064  87.271  59.585  1.00 25.76           C  
-ATOM   3530  CG  GLU A 461      21.864  88.405  60.275  1.00 31.33           C  
-ATOM   3531  N   GLU A 462      17.866  86.374  59.133  1.00 22.80           N  
-ATOM   3532  CA  GLU A 462      16.933  85.262  58.938  1.00 22.36           C  
-ATOM   3533  C   GLU A 462      16.067  85.557  57.749  1.00 23.82           C  
-ATOM   3534  O   GLU A 462      15.620  84.657  57.053  1.00 26.24           O  
-ATOM   3535  CB  GLU A 462      16.067  85.018  60.182  1.00 19.23           C  
-ATOM   3536  CG  GLU A 462      16.911  84.411  61.317  1.00 16.08           C  
-ATOM   3537  CD  GLU A 462      16.242  84.428  62.681  1.00 16.57           C  
-ATOM   3538  OE1 GLU A 462      15.343  85.249  62.900  1.00 10.48           O  
-ATOM   3539  OE2 GLU A 462      16.636  83.613  63.518  1.00  6.73           O  
-ATOM   3540  N   GLU A 463      15.804  86.853  57.519  1.00 26.21           N  
-ATOM   3541  CA  GLU A 463      15.000  87.209  56.343  1.00 27.74           C  
-ATOM   3542  C   GLU A 463      15.748  86.741  55.097  1.00 24.31           C  
-ATOM   3543  O   GLU A 463      15.214  86.181  54.152  1.00 23.26           O  
-ATOM   3544  CB  GLU A 463      14.741  88.720  56.214  1.00 33.13           C  
-ATOM   3545  CG  GLU A 463      13.667  88.991  55.142  1.00 43.02           C  
-ATOM   3546  CD  GLU A 463      13.678  90.403  54.567  1.00 49.44           C  
-ATOM   3547  OE1 GLU A 463      14.724  90.820  54.065  1.00 55.82           O  
-ATOM   3548  OE2 GLU A 463      12.639  91.071  54.602  1.00 52.07           O  
-ATOM   3549  N   ALA A 464      17.053  86.988  55.147  1.00 21.45           N  
-ATOM   3550  CA  ALA A 464      17.904  86.571  54.059  1.00 17.40           C  
-ATOM   3551  C   ALA A 464      17.806  85.072  53.872  1.00 16.84           C  
-ATOM   3552  O   ALA A 464      17.625  84.578  52.772  1.00 23.96           O  
-ATOM   3553  CB  ALA A 464      19.359  86.947  54.361  1.00 18.00           C  
-ATOM   3554  N   LEU A 465      17.917  84.353  54.990  1.00 14.92           N  
-ATOM   3555  CA  LEU A 465      17.840  82.901  54.957  1.00 11.99           C  
-ATOM   3556  C   LEU A 465      16.538  82.392  54.346  1.00 13.91           C  
-ATOM   3557  O   LEU A 465      16.581  81.508  53.502  1.00 14.21           O  
-ATOM   3558  CB  LEU A 465      18.063  82.291  56.357  1.00 10.67           C  
-ATOM   3559  CG  LEU A 465      18.192  80.753  56.381  1.00 11.62           C  
-ATOM   3560  CD1 LEU A 465      19.344  80.255  55.509  1.00 19.35           C  
-ATOM   3561  CD2 LEU A 465      18.403  80.203  57.788  1.00 11.16           C  
-ATOM   3562  N   SER A 466      15.367  82.933  54.737  1.00 12.62           N  
-ATOM   3563  CA  SER A 466      14.166  82.366  54.110  1.00 17.34           C  
-ATOM   3564  C   SER A 466      14.102  82.694  52.637  1.00 22.63           C  
-ATOM   3565  O   SER A 466      13.545  81.933  51.858  1.00 26.36           O  
-ATOM   3566  CB  SER A 466      12.832  82.685  54.780  1.00 14.63           C  
-ATOM   3567  OG  SER A 466      12.762  84.077  55.007  1.00 25.19           O  
-ATOM   3568  N   ARG A 467      14.675  83.836  52.233  1.00 22.38           N  
-ATOM   3569  CA  ARG A 467      14.612  84.090  50.803  1.00 20.89           C  
-ATOM   3570  C   ARG A 467      15.467  83.065  50.051  1.00 20.90           C  
-ATOM   3571  O   ARG A 467      15.126  82.650  48.949  1.00 22.37           O  
-ATOM   3572  CB  ARG A 467      15.008  85.515  50.486  1.00 20.62           C  
-ATOM   3573  CG  ARG A 467      14.021  86.543  51.059  1.00 24.03           C  
-ATOM   3574  CD  ARG A 467      14.477  87.965  50.698  1.00 29.71           C  
-ATOM   3575  NE  ARG A 467      13.686  88.998  51.343  1.00 34.93           N  
-ATOM   3576  CZ  ARG A 467      12.560  89.506  50.812  1.00 36.36           C  
-ATOM   3577  NH1 ARG A 467      12.048  89.034  49.678  1.00 36.65           N  
-ATOM   3578  NH2 ARG A 467      11.944  90.507  51.441  1.00 40.08           N  
-ATOM   3579  N   ARG A 468      16.576  82.636  50.669  1.00 17.65           N  
-ATOM   3580  CA  ARG A 468      17.387  81.648  49.973  1.00 19.11           C  
-ATOM   3581  C   ARG A 468      16.678  80.334  49.900  1.00 20.33           C  
-ATOM   3582  O   ARG A 468      16.709  79.626  48.903  1.00 22.41           O  
-ATOM   3583  CB  ARG A 468      18.738  81.360  50.640  1.00 18.67           C  
-ATOM   3584  CG  ARG A 468      19.467  82.632  51.088  1.00 28.44           C  
-ATOM   3585  CD  ARG A 468      21.002  82.519  51.106  1.00 34.04           C  
-ATOM   3586  NE  ARG A 468      21.519  81.658  52.167  1.00 40.98           N  
-ATOM   3587  CZ  ARG A 468      21.745  80.345  51.975  1.00 44.67           C  
-ATOM   3588  NH1 ARG A 468      21.341  79.745  50.866  1.00 46.16           N  
-ATOM   3589  NH2 ARG A 468      22.383  79.621  52.895  1.00 46.32           N  
-ATOM   3590  N   ILE A 469      16.030  80.025  51.022  1.00 20.68           N  
-ATOM   3591  CA  ILE A 469      15.311  78.769  51.105  1.00 19.33           C  
-ATOM   3592  C   ILE A 469      14.193  78.758  50.084  1.00 19.36           C  
-ATOM   3593  O   ILE A 469      14.060  77.842  49.284  1.00 23.77           O  
-ATOM   3594  CB  ILE A 469      14.783  78.529  52.537  1.00 17.87           C  
-ATOM   3595  CG1 ILE A 469      15.877  78.713  53.626  1.00 17.95           C  
-ATOM   3596  CG2 ILE A 469      14.077  77.177  52.658  1.00 17.95           C  
-ATOM   3597  CD1 ILE A 469      16.398  77.436  54.273  1.00 10.76           C  
-ATOM   3598  N   MET A 470      13.390  79.821  50.110  1.00 16.41           N  
-ATOM   3599  CA  MET A 470      12.270  79.928  49.189  1.00 16.31           C  
-ATOM   3600  C   MET A 470      12.703  79.892  47.736  1.00 16.06           C  
-ATOM   3601  O   MET A 470      11.992  79.431  46.852  1.00 13.24           O  
-ATOM   3602  CB  MET A 470      11.493  81.220  49.444  1.00 14.61           C  
-ATOM   3603  CG  MET A 470      10.687  81.174  50.737  1.00 15.84           C  
-ATOM   3604  SD  MET A 470       9.476  82.526  50.688  1.00 15.15           S  
-ATOM   3605  CE  MET A 470      10.636  83.920  50.863  1.00 15.78           C  
-ATOM   3606  N   HIS A 471      13.896  80.417  47.493  1.00 17.20           N  
-ATOM   3607  CA  HIS A 471      14.352  80.401  46.118  1.00 21.69           C  
-ATOM   3608  C   HIS A 471      14.757  78.995  45.748  1.00 20.45           C  
-ATOM   3609  O   HIS A 471      14.348  78.472  44.731  1.00 20.20           O  
-ATOM   3610  CB  HIS A 471      15.475  81.429  45.913  1.00 29.47           C  
-ATOM   3611  CG  HIS A 471      15.657  81.781  44.446  1.00 33.27           C  
-ATOM   3612  ND1 HIS A 471      14.668  82.211  43.634  1.00 33.46           N  
-ATOM   3613  CD2 HIS A 471      16.854  81.743  43.693  1.00 34.65           C  
-ATOM   3614  CE1 HIS A 471      15.227  82.430  42.433  1.00 37.54           C  
-ATOM   3615  NE2 HIS A 471      16.548  82.159  42.446  1.00 37.05           N  
-ATOM   3616  N   TYR A 472      15.524  78.353  46.625  1.00 21.14           N  
-ATOM   3617  CA  TYR A 472      15.949  76.982  46.342  1.00 19.71           C  
-ATOM   3618  C   TYR A 472      14.750  76.076  46.083  1.00 20.98           C  
-ATOM   3619  O   TYR A 472      14.714  75.220  45.206  1.00 22.37           O  
-ATOM   3620  CB  TYR A 472      16.667  76.379  47.569  1.00 20.34           C  
-ATOM   3621  CG  TYR A 472      18.070  76.843  47.860  1.00 23.95           C  
-ATOM   3622  CD1 TYR A 472      18.992  77.017  46.826  1.00 24.90           C  
-ATOM   3623  CD2 TYR A 472      18.484  77.038  49.186  1.00 26.94           C  
-ATOM   3624  CE1 TYR A 472      20.319  77.345  47.103  1.00 26.10           C  
-ATOM   3625  CE2 TYR A 472      19.814  77.368  49.468  1.00 30.01           C  
-ATOM   3626  CZ  TYR A 472      20.740  77.515  48.424  1.00 30.84           C  
-ATOM   3627  OH  TYR A 472      22.066  77.823  48.690  1.00 36.97           O  
-ATOM   3628  N   TRP A 473      13.744  76.283  46.923  1.00 18.72           N  
-ATOM   3629  CA  TRP A 473      12.550  75.483  46.804  1.00 20.30           C  
-ATOM   3630  C   TRP A 473      11.855  75.781  45.475  1.00 20.82           C  
-ATOM   3631  O   TRP A 473      11.469  74.865  44.757  1.00 22.52           O  
-ATOM   3632  CB  TRP A 473      11.611  75.704  48.027  1.00 17.97           C  
-ATOM   3633  CG  TRP A 473      11.772  74.677  49.157  1.00 18.66           C  
-ATOM   3634  CD1 TRP A 473      10.715  73.896  49.684  1.00 15.00           C  
-ATOM   3635  CD2 TRP A 473      12.930  74.304  49.885  1.00 16.88           C  
-ATOM   3636  NE1 TRP A 473      11.154  73.078  50.675  1.00 14.33           N  
-ATOM   3637  CE2 TRP A 473      12.501  73.272  50.857  1.00 13.46           C  
-ATOM   3638  CE3 TRP A 473      14.272  74.684  49.864  1.00 18.34           C  
-ATOM   3639  CZ2 TRP A 473      13.458  72.703  51.715  1.00 10.94           C  
-ATOM   3640  CZ3 TRP A 473      15.204  74.093  50.741  1.00 15.94           C  
-ATOM   3641  CH2 TRP A 473      14.797  73.118  51.659  1.00 13.44           C  
-ATOM   3642  N   ALA A 474      11.725  77.080  45.143  1.00 18.06           N  
-ATOM   3643  CA  ALA A 474      11.038  77.443  43.897  1.00 12.46           C  
-ATOM   3644  C   ALA A 474      11.815  76.997  42.682  1.00 10.86           C  
-ATOM   3645  O   ALA A 474      11.290  76.292  41.835  1.00 13.28           O  
-ATOM   3646  CB  ALA A 474      10.740  78.933  43.835  1.00 11.11           C  
-ATOM   3647  N   THR A 475      13.074  77.399  42.593  1.00  7.89           N  
-ATOM   3648  CA  THR A 475      13.950  77.014  41.495  1.00  9.64           C  
-ATOM   3649  C   THR A 475      14.029  75.501  41.324  1.00 12.78           C  
-ATOM   3650  O   THR A 475      14.080  74.974  40.219  1.00 12.13           O  
-ATOM   3651  CB  THR A 475      15.327  77.597  41.792  1.00  7.84           C  
-ATOM   3652  OG1 THR A 475      15.073  78.985  41.895  1.00 11.47           O  
-ATOM   3653  CG2 THR A 475      16.398  77.356  40.722  1.00  6.36           C  
-ATOM   3654  N   PHE A 476      14.034  74.766  42.439  1.00 16.53           N  
-ATOM   3655  CA  PHE A 476      14.063  73.322  42.254  1.00 16.97           C  
-ATOM   3656  C   PHE A 476      12.729  72.858  41.634  1.00 19.25           C  
-ATOM   3657  O   PHE A 476      12.684  71.957  40.806  1.00 20.45           O  
-ATOM   3658  CB  PHE A 476      14.322  72.604  43.592  1.00 14.69           C  
-ATOM   3659  CG  PHE A 476      14.130  71.110  43.470  1.00  8.02           C  
-ATOM   3660  CD1 PHE A 476      15.191  70.290  43.041  1.00  8.40           C  
-ATOM   3661  CD2 PHE A 476      12.871  70.541  43.736  1.00  2.00           C  
-ATOM   3662  CE1 PHE A 476      14.993  68.913  42.870  1.00  8.04           C  
-ATOM   3663  CE2 PHE A 476      12.666  69.171  43.563  1.00  2.00           C  
-ATOM   3664  CZ  PHE A 476      13.726  68.359  43.132  1.00  8.31           C  
-ATOM   3665  N   ALA A 477      11.641  73.498  42.056  1.00 19.29           N  
-ATOM   3666  CA  ALA A 477      10.344  73.088  41.528  1.00 23.33           C  
-ATOM   3667  C   ALA A 477      10.208  73.333  40.055  1.00 25.47           C  
-ATOM   3668  O   ALA A 477       9.512  72.608  39.359  1.00 31.09           O  
-ATOM   3669  CB  ALA A 477       9.185  73.787  42.257  1.00 21.87           C  
-ATOM   3670  N   LYS A 478      10.871  74.396  39.589  1.00 25.09           N  
-ATOM   3671  CA  LYS A 478      10.770  74.689  38.160  1.00 23.32           C  
-ATOM   3672  C   LYS A 478      11.755  73.867  37.357  1.00 20.81           C  
-ATOM   3673  O   LYS A 478      11.423  73.053  36.521  1.00 26.35           O  
-ATOM   3674  CB  LYS A 478      11.013  76.172  37.858  1.00 24.55           C  
-ATOM   3675  CG  LYS A 478      10.290  77.145  38.788  1.00 27.31           C  
-ATOM   3676  CD  LYS A 478      10.070  78.487  38.068  1.00 36.59           C  
-ATOM   3677  N   THR A 479      13.002  74.130  37.645  1.00 15.01           N  
-ATOM   3678  CA  THR A 479      14.102  73.509  36.995  1.00 13.07           C  
-ATOM   3679  C   THR A 479      14.392  72.091  37.362  1.00 16.43           C  
-ATOM   3680  O   THR A 479      14.615  71.263  36.499  1.00 22.36           O  
-ATOM   3681  CB  THR A 479      15.332  74.313  37.420  1.00 13.16           C  
-ATOM   3682  OG1 THR A 479      15.090  75.645  37.005  1.00 20.56           O  
-ATOM   3683  CG2 THR A 479      16.670  73.866  36.836  1.00 19.93           C  
-ATOM   3684  N   GLY A 480      14.472  71.805  38.653  1.00 20.24           N  
-ATOM   3685  CA  GLY A 480      14.836  70.440  39.044  1.00 16.81           C  
-ATOM   3686  C   GLY A 480      16.209  70.443  39.664  1.00 15.43           C  
-ATOM   3687  O   GLY A 480      16.827  69.429  39.964  1.00 16.07           O  
-ATOM   3688  N   ASN A 481      16.709  71.653  39.846  1.00 13.23           N  
-ATOM   3689  CA  ASN A 481      18.005  71.873  40.445  1.00 15.96           C  
-ATOM   3690  C   ASN A 481      17.730  73.119  41.247  1.00 18.94           C  
-ATOM   3691  O   ASN A 481      17.024  73.960  40.705  1.00 22.56           O  
-ATOM   3692  CB  ASN A 481      19.029  72.126  39.349  1.00 17.90           C  
-ATOM   3693  CG  ASN A 481      20.375  72.417  39.921  1.00 19.48           C  
-ATOM   3694  OD1 ASN A 481      20.513  73.084  40.924  1.00 25.74           O  
-ATOM   3695  ND2 ASN A 481      21.399  71.899  39.278  1.00 23.51           N  
-ATOM   3696  N   PRO A 482      18.168  73.197  42.528  1.00 19.54           N  
-ATOM   3697  CA  PRO A 482      17.886  74.366  43.366  1.00 19.34           C  
-ATOM   3698  C   PRO A 482      18.739  75.583  43.049  1.00 21.48           C  
-ATOM   3699  O   PRO A 482      18.451  76.700  43.465  1.00 21.62           O  
-ATOM   3700  CB  PRO A 482      18.230  73.874  44.785  1.00 18.08           C  
-ATOM   3701  CG  PRO A 482      19.205  72.705  44.604  1.00 16.26           C  
-ATOM   3702  CD  PRO A 482      18.867  72.121  43.238  1.00 17.03           C  
-ATOM   3703  N   ASN A 483      19.846  75.327  42.358  1.00 23.18           N  
-ATOM   3704  CA  ASN A 483      20.779  76.374  41.991  1.00 25.35           C  
-ATOM   3705  C   ASN A 483      20.437  77.083  40.708  1.00 29.38           C  
-ATOM   3706  O   ASN A 483      20.162  76.487  39.676  1.00 31.96           O  
-ATOM   3707  CB  ASN A 483      22.151  75.763  41.699  1.00 22.37           C  
-ATOM   3708  CG  ASN A 483      22.794  75.294  42.960  1.00 25.40           C  
-ATOM   3709  OD1 ASN A 483      22.995  74.115  43.211  1.00 18.89           O  
-ATOM   3710  ND2 ASN A 483      23.130  76.288  43.791  1.00 27.50           N  
-ATOM   3711  N   GLU A 484      20.466  78.424  40.773  1.00 34.07           N  
-ATOM   3712  CA  GLU A 484      20.242  79.176  39.540  1.00 37.82           C  
-ATOM   3713  C   GLU A 484      21.578  78.951  38.851  1.00 44.50           C  
-ATOM   3714  O   GLU A 484      22.560  78.711  39.559  1.00 43.46           O  
-ATOM   3715  CB  GLU A 484      20.014  80.696  39.740  1.00 36.04           C  
-ATOM   3716  CG  GLU A 484      18.511  81.037  39.875  1.00 34.11           C  
-ATOM   3717  N   PRO A 485      21.583  79.025  37.500  1.00 50.47           N  
-ATOM   3718  CA  PRO A 485      22.850  79.019  36.758  1.00 51.91           C  
-ATOM   3719  C   PRO A 485      23.766  80.205  37.072  1.00 52.65           C  
-ATOM   3720  O   PRO A 485      24.981  80.013  37.035  1.00 52.72           O  
-ATOM   3721  CB  PRO A 485      22.418  78.986  35.283  1.00 52.01           C  
-ATOM   3722  CG  PRO A 485      20.927  78.579  35.263  1.00 50.28           C  
-ATOM   3723  CD  PRO A 485      20.381  78.905  36.656  1.00 49.49           C  
-ATOM   3724  N   SER A 490      26.591  79.111  46.480  1.00 46.63           N  
-ATOM   3725  CA  SER A 490      27.530  78.335  45.692  1.00 45.59           C  
-ATOM   3726  C   SER A 490      26.698  77.159  45.269  1.00 42.64           C  
-ATOM   3727  O   SER A 490      25.538  77.111  45.674  1.00 42.60           O  
-ATOM   3728  CB  SER A 490      28.772  78.073  46.562  1.00 47.19           C  
-ATOM   3729  OG  SER A 490      29.102  79.384  47.073  1.00 50.73           O  
-ATOM   3730  N   LYS A 491      27.241  76.276  44.447  1.00 38.77           N  
-ATOM   3731  CA  LYS A 491      26.402  75.181  44.041  1.00 36.63           C  
-ATOM   3732  C   LYS A 491      26.177  74.297  45.234  1.00 33.13           C  
-ATOM   3733  O   LYS A 491      27.062  74.134  46.060  1.00 35.13           O  
-ATOM   3734  CB  LYS A 491      27.005  74.422  42.846  1.00 40.99           C  
-ATOM   3735  CG  LYS A 491      27.213  75.311  41.594  1.00 48.99           C  
-ATOM   3736  CD  LYS A 491      25.893  75.808  40.953  1.00 57.24           C  
-ATOM   3737  CE  LYS A 491      26.055  76.967  39.944  1.00 61.63           C  
-ATOM   3738  NZ  LYS A 491      26.300  78.221  40.640  1.00 62.54           N  
-ATOM   3739  N   TRP A 492      24.951  73.815  45.309  1.00 26.12           N  
-ATOM   3740  CA  TRP A 492      24.500  72.929  46.334  1.00 19.00           C  
-ATOM   3741  C   TRP A 492      24.755  71.623  45.588  1.00 18.58           C  
-ATOM   3742  O   TRP A 492      24.022  71.332  44.657  1.00 20.29           O  
-ATOM   3743  CB  TRP A 492      22.994  73.252  46.571  1.00 11.79           C  
-ATOM   3744  CG  TRP A 492      22.225  72.250  47.431  1.00 10.05           C  
-ATOM   3745  CD1 TRP A 492      22.584  70.919  47.775  1.00  7.17           C  
-ATOM   3746  CD2 TRP A 492      20.962  72.476  48.003  1.00  6.08           C  
-ATOM   3747  NE1 TRP A 492      21.616  70.329  48.509  1.00  9.72           N  
-ATOM   3748  CE2 TRP A 492      20.594  71.219  48.686  1.00  6.70           C  
-ATOM   3749  CE3 TRP A 492      20.074  73.558  48.020  1.00  9.07           C  
-ATOM   3750  CZ2 TRP A 492      19.363  71.130  49.348  1.00  5.91           C  
-ATOM   3751  CZ3 TRP A 492      18.846  73.430  48.700  1.00  6.97           C  
-ATOM   3752  CH2 TRP A 492      18.498  72.235  49.355  1.00  4.77           C  
-ATOM   3753  N   PRO A 493      25.819  70.870  45.921  1.00 17.27           N  
-ATOM   3754  CA  PRO A 493      26.128  69.659  45.145  1.00 19.88           C  
-ATOM   3755  C   PRO A 493      25.022  68.629  45.075  1.00 20.16           C  
-ATOM   3756  O   PRO A 493      24.136  68.597  45.921  1.00 26.93           O  
-ATOM   3757  CB  PRO A 493      27.271  68.983  45.936  1.00 19.03           C  
-ATOM   3758  CG  PRO A 493      27.844  70.063  46.857  1.00 22.50           C  
-ATOM   3759  CD  PRO A 493      26.749  71.135  47.013  1.00 18.43           C  
-ATOM   3760  N   LEU A 494      25.130  67.751  44.078  1.00 18.42           N  
-ATOM   3761  CA  LEU A 494      24.140  66.682  43.997  1.00 19.26           C  
-ATOM   3762  C   LEU A 494      24.604  65.687  45.037  1.00 21.65           C  
-ATOM   3763  O   LEU A 494      25.778  65.617  45.407  1.00 26.28           O  
-ATOM   3764  CB  LEU A 494      24.198  65.863  42.675  1.00 18.39           C  
-ATOM   3765  CG  LEU A 494      23.502  66.431  41.420  1.00 14.50           C  
-ATOM   3766  CD1 LEU A 494      24.072  65.720  40.181  1.00 14.53           C  
-ATOM   3767  CD2 LEU A 494      21.976  66.245  41.464  1.00  4.23           C  
-ATOM   3768  N   PHE A 495      23.658  64.893  45.485  1.00 20.58           N  
-ATOM   3769  CA  PHE A 495      24.010  63.884  46.449  1.00 24.09           C  
-ATOM   3770  C   PHE A 495      24.387  62.725  45.561  1.00 25.16           C  
-ATOM   3771  O   PHE A 495      23.678  62.448  44.600  1.00 27.40           O  
-ATOM   3772  CB  PHE A 495      22.790  63.533  47.346  1.00 24.00           C  
-ATOM   3773  CG  PHE A 495      23.040  62.305  48.198  1.00 19.91           C  
-ATOM   3774  CD1 PHE A 495      22.816  61.023  47.681  1.00 19.53           C  
-ATOM   3775  CD2 PHE A 495      23.561  62.437  49.487  1.00 19.87           C  
-ATOM   3776  CE1 PHE A 495      23.152  59.888  48.429  1.00 23.95           C  
-ATOM   3777  CE2 PHE A 495      23.875  61.305  50.240  1.00 20.88           C  
-ATOM   3778  CZ  PHE A 495      23.690  60.024  49.713  1.00 20.47           C  
-ATOM   3779  N   THR A 496      25.487  62.048  45.868  1.00 26.97           N  
-ATOM   3780  CA  THR A 496      25.872  60.907  45.060  1.00 28.29           C  
-ATOM   3781  C   THR A 496      26.175  59.786  46.027  1.00 30.14           C  
-ATOM   3782  O   THR A 496      26.657  60.005  47.130  1.00 31.89           O  
-ATOM   3783  CB  THR A 496      27.053  61.284  44.158  1.00 30.33           C  
-ATOM   3784  OG1 THR A 496      28.256  61.472  44.897  1.00 36.96           O  
-ATOM   3785  CG2 THR A 496      26.828  62.591  43.379  1.00 34.12           C  
-ATOM   3786  N   THR A 497      25.927  58.562  45.611  1.00 31.97           N  
-ATOM   3787  CA  THR A 497      26.216  57.468  46.527  1.00 33.76           C  
-ATOM   3788  C   THR A 497      27.712  57.368  46.853  1.00 37.80           C  
-ATOM   3789  O   THR A 497      28.118  56.851  47.886  1.00 40.57           O  
-ATOM   3790  CB  THR A 497      25.634  56.185  45.937  1.00 32.55           C  
-ATOM   3791  OG1 THR A 497      26.015  56.130  44.560  1.00 37.23           O  
-ATOM   3792  CG2 THR A 497      24.099  56.140  45.988  1.00 34.37           C  
-ATOM   3793  N   LYS A 498      28.511  57.888  45.908  1.00 40.37           N  
-ATOM   3794  CA  LYS A 498      29.960  57.887  46.057  1.00 42.80           C  
-ATOM   3795  C   LYS A 498      30.373  58.851  47.147  1.00 42.93           C  
-ATOM   3796  O   LYS A 498      30.764  58.517  48.254  1.00 43.73           O  
-ATOM   3797  CB  LYS A 498      30.722  58.284  44.762  1.00 42.58           C  
-ATOM   3798  N   GLU A 499      30.274  60.117  46.782  1.00 43.38           N  
-ATOM   3799  CA  GLU A 499      30.643  61.219  47.656  1.00 44.02           C  
-ATOM   3800  C   GLU A 499      29.337  61.877  48.026  1.00 42.03           C  
-ATOM   3801  O   GLU A 499      28.832  62.794  47.380  1.00 45.50           O  
-ATOM   3802  CB  GLU A 499      31.619  62.139  46.899  1.00 45.86           C  
-ATOM   3803  CG  GLU A 499      31.172  62.342  45.437  1.00 45.32           C  
-ATOM   3804  N   GLN A 500      28.787  61.317  49.089  1.00 36.62           N  
-ATOM   3805  CA  GLN A 500      27.509  61.713  49.653  1.00 33.88           C  
-ATOM   3806  C   GLN A 500      27.470  63.138  50.196  1.00 31.50           C  
-ATOM   3807  O   GLN A 500      27.473  63.311  51.409  1.00 37.01           O  
-ATOM   3808  CB  GLN A 500      27.230  60.692  50.764  1.00 35.36           C  
-ATOM   3809  CG  GLN A 500      27.456  59.250  50.291  1.00 34.03           C  
-ATOM   3810  CD  GLN A 500      26.779  58.232  51.164  1.00 36.65           C  
-ATOM   3811  OE1 GLN A 500      26.191  58.493  52.215  1.00 38.59           O  
-ATOM   3812  NE2 GLN A 500      26.894  57.016  50.684  1.00 39.33           N  
-ATOM   3813  N   LYS A 501      27.434  64.140  49.321  1.00 26.18           N  
-ATOM   3814  CA  LYS A 501      27.421  65.517  49.789  1.00 21.65           C  
-ATOM   3815  C   LYS A 501      26.041  66.019  50.134  1.00 21.55           C  
-ATOM   3816  O   LYS A 501      25.049  65.554  49.594  1.00 21.60           O  
-ATOM   3817  CB  LYS A 501      27.978  66.424  48.693  1.00 22.57           C  
-ATOM   3818  CG  LYS A 501      29.489  66.261  48.541  1.00 27.22           C  
-ATOM   3819  CD  LYS A 501      29.927  66.053  47.091  1.00 34.72           C  
-ATOM   3820  CE  LYS A 501      31.419  66.344  46.895  1.00 37.58           C  
-ATOM   3821  NZ  LYS A 501      31.651  67.784  46.932  1.00 41.05           N  
-ATOM   3822  N   PHE A 502      26.030  67.015  51.026  1.00 19.88           N  
-ATOM   3823  CA  PHE A 502      24.828  67.687  51.502  1.00 20.61           C  
-ATOM   3824  C   PHE A 502      25.297  69.030  51.998  1.00 21.35           C  
-ATOM   3825  O   PHE A 502      26.501  69.257  52.126  1.00 20.82           O  
-ATOM   3826  CB  PHE A 502      24.091  66.939  52.623  1.00 20.67           C  
-ATOM   3827  CG  PHE A 502      24.852  66.899  53.936  1.00 19.91           C  
-ATOM   3828  CD1 PHE A 502      24.654  67.907  54.902  1.00 19.70           C  
-ATOM   3829  CD2 PHE A 502      25.717  65.828  54.225  1.00 18.02           C  
-ATOM   3830  CE1 PHE A 502      25.280  67.827  56.149  1.00 16.32           C  
-ATOM   3831  CE2 PHE A 502      26.338  65.743  55.477  1.00 16.24           C  
-ATOM   3832  CZ  PHE A 502      26.110  66.737  56.438  1.00 16.77           C  
-ATOM   3833  N   ILE A 503      24.340  69.909  52.303  1.00 19.70           N  
-ATOM   3834  CA  ILE A 503      24.756  71.214  52.769  1.00 21.62           C  
-ATOM   3835  C   ILE A 503      24.054  71.584  54.048  1.00 23.19           C  
-ATOM   3836  O   ILE A 503      23.018  71.033  54.414  1.00 26.92           O  
-ATOM   3837  CB  ILE A 503      24.485  72.259  51.670  1.00 20.67           C  
-ATOM   3838  CG1 ILE A 503      23.007  72.413  51.293  1.00 18.01           C  
-ATOM   3839  CG2 ILE A 503      25.304  71.926  50.425  1.00 24.07           C  
-ATOM   3840  CD1 ILE A 503      22.765  73.733  50.558  1.00 17.69           C  
-ATOM   3841  N   ASP A 504      24.667  72.543  54.740  1.00 23.58           N  
-ATOM   3842  CA  ASP A 504      24.075  73.039  55.972  1.00 24.35           C  
-ATOM   3843  C   ASP A 504      23.161  74.165  55.530  1.00 23.37           C  
-ATOM   3844  O   ASP A 504      23.494  74.928  54.633  1.00 26.80           O  
-ATOM   3845  CB  ASP A 504      25.142  73.603  56.917  1.00 28.56           C  
-ATOM   3846  CG  ASP A 504      25.866  72.563  57.755  1.00 31.28           C  
-ATOM   3847  OD1 ASP A 504      25.449  71.404  57.795  1.00 30.48           O  
-ATOM   3848  OD2 ASP A 504      26.854  72.935  58.387  1.00 36.62           O  
-ATOM   3849  N   LEU A 505      22.027  74.291  56.181  1.00 21.29           N  
-ATOM   3850  CA  LEU A 505      21.099  75.326  55.795  1.00 19.77           C  
-ATOM   3851  C   LEU A 505      20.890  76.199  57.017  1.00 22.78           C  
-ATOM   3852  O   LEU A 505      20.004  75.992  57.834  1.00 27.15           O  
-ATOM   3853  CB  LEU A 505      19.843  74.574  55.338  1.00 16.00           C  
-ATOM   3854  CG  LEU A 505      19.007  75.260  54.277  1.00 14.53           C  
-ATOM   3855  CD1 LEU A 505      19.803  75.551  52.994  1.00 11.95           C  
-ATOM   3856  CD2 LEU A 505      17.796  74.358  53.969  1.00 13.12           C  
-ATOM   3857  N   ASN A 506      21.768  77.168  57.181  1.00 22.31           N  
-ATOM   3858  CA  ASN A 506      21.673  78.071  58.314  1.00 23.56           C  
-ATOM   3859  C   ASN A 506      22.193  79.378  57.791  1.00 26.60           C  
-ATOM   3860  O   ASN A 506      22.670  79.422  56.675  1.00 31.76           O  
-ATOM   3861  CB  ASN A 506      22.439  77.572  59.537  1.00 21.45           C  
-ATOM   3862  CG  ASN A 506      23.910  77.470  59.239  1.00 21.54           C  
-ATOM   3863  OD1 ASN A 506      24.511  78.471  58.895  1.00 15.80           O  
-ATOM   3864  ND2 ASN A 506      24.483  76.272  59.376  1.00 18.47           N  
-ATOM   3865  N   THR A 507      22.104  80.426  58.594  1.00 26.94           N  
-ATOM   3866  CA  THR A 507      22.532  81.752  58.159  1.00 28.80           C  
-ATOM   3867  C   THR A 507      24.014  82.032  57.809  1.00 31.21           C  
-ATOM   3868  O   THR A 507      24.354  83.131  57.382  1.00 32.73           O  
-ATOM   3869  CB  THR A 507      22.051  82.754  59.214  1.00 29.17           C  
-ATOM   3870  OG1 THR A 507      22.596  82.406  60.489  1.00 30.67           O  
-ATOM   3871  CG2 THR A 507      20.523  82.841  59.393  1.00 27.48           C  
-ATOM   3872  N   GLU A 508      24.918  81.088  58.022  1.00 33.28           N  
-ATOM   3873  CA  GLU A 508      26.312  81.365  57.690  1.00 37.80           C  
-ATOM   3874  C   GLU A 508      26.534  81.120  56.192  1.00 43.12           C  
-ATOM   3875  O   GLU A 508      25.679  80.610  55.477  1.00 46.45           O  
-ATOM   3876  CB  GLU A 508      27.222  80.495  58.560  1.00 36.74           C  
-ATOM   3877  CG  GLU A 508      27.087  80.878  60.030  1.00 37.93           C  
-ATOM   3878  N   PRO A 509      27.753  81.462  55.723  1.00 45.16           N  
-ATOM   3879  CA  PRO A 509      28.326  80.814  54.543  1.00 45.89           C  
-ATOM   3880  C   PRO A 509      28.195  79.279  54.480  1.00 46.40           C  
-ATOM   3881  O   PRO A 509      28.728  78.532  55.291  1.00 47.25           O  
-ATOM   3882  CB  PRO A 509      29.783  81.285  54.586  1.00 47.53           C  
-ATOM   3883  CG  PRO A 509      29.772  82.639  55.328  1.00 49.06           C  
-ATOM   3884  CD  PRO A 509      28.515  82.611  56.209  1.00 47.98           C  
-ATOM   3885  N   MET A 510      27.466  78.864  53.443  1.00 45.34           N  
-ATOM   3886  CA  MET A 510      27.173  77.470  53.140  1.00 43.84           C  
-ATOM   3887  C   MET A 510      28.368  76.540  53.244  1.00 42.69           C  
-ATOM   3888  O   MET A 510      29.455  76.849  52.775  1.00 45.05           O  
-ATOM   3889  CB  MET A 510      26.687  77.420  51.678  1.00 44.66           C  
-ATOM   3890  CG  MET A 510      25.631  76.352  51.383  1.00 48.03           C  
-ATOM   3891  SD  MET A 510      25.524  76.214  49.574  1.00 48.04           S  
-ATOM   3892  CE  MET A 510      26.976  75.147  49.315  1.00 46.50           C  
-ATOM   3893  N   LYS A 511      28.127  75.365  53.813  1.00 38.25           N  
-ATOM   3894  CA  LYS A 511      29.199  74.402  53.925  1.00 37.85           C  
-ATOM   3895  C   LYS A 511      28.612  73.139  53.386  1.00 36.58           C  
-ATOM   3896  O   LYS A 511      27.443  72.831  53.590  1.00 41.64           O  
-ATOM   3897  CB  LYS A 511      29.680  74.208  55.364  1.00 39.61           C  
-ATOM   3898  CG  LYS A 511      30.365  75.483  55.888  1.00 45.90           C  
-ATOM   3899  N   VAL A 512      29.451  72.433  52.668  1.00 33.40           N  
-ATOM   3900  CA  VAL A 512      29.092  71.186  52.072  1.00 31.10           C  
-ATOM   3901  C   VAL A 512      29.763  70.204  52.995  1.00 31.86           C  
-ATOM   3902  O   VAL A 512      30.877  70.441  53.458  1.00 35.08           O  
-ATOM   3903  CB  VAL A 512      29.715  71.171  50.663  1.00 29.54           C  
-ATOM   3904  CG1 VAL A 512      29.595  69.803  49.976  1.00 24.94           C  
-ATOM   3905  CG2 VAL A 512      29.173  72.324  49.782  1.00 24.63           C  
-ATOM   3906  N   HIS A 513      29.103  69.099  53.252  1.00 30.57           N  
-ATOM   3907  CA  HIS A 513      29.684  68.110  54.137  1.00 28.81           C  
-ATOM   3908  C   HIS A 513      29.496  66.808  53.442  1.00 25.76           C  
-ATOM   3909  O   HIS A 513      29.010  66.767  52.325  1.00 25.49           O  
-ATOM   3910  CB  HIS A 513      28.911  68.108  55.460  1.00 30.36           C  
-ATOM   3911  CG  HIS A 513      29.010  69.433  56.177  1.00 30.18           C  
-ATOM   3912  ND1 HIS A 513      29.984  69.762  57.046  1.00 27.05           N  
-ATOM   3913  CD2 HIS A 513      28.120  70.531  56.077  1.00 30.29           C  
-ATOM   3914  CE1 HIS A 513      29.710  71.006  57.465  1.00 29.04           C  
-ATOM   3915  NE2 HIS A 513      28.595  71.488  56.893  1.00 27.19           N  
-ATOM   3916  N   GLN A 514      29.878  65.729  54.107  1.00 26.12           N  
-ATOM   3917  CA  GLN A 514      29.700  64.446  53.466  1.00 28.73           C  
-ATOM   3918  C   GLN A 514      29.154  63.479  54.488  1.00 26.20           C  
-ATOM   3919  O   GLN A 514      29.258  63.668  55.688  1.00 28.26           O  
-ATOM   3920  CB  GLN A 514      31.047  63.886  52.982  1.00 34.39           C  
-ATOM   3921  CG  GLN A 514      31.757  64.771  51.948  1.00 43.27           C  
-ATOM   3922  CD  GLN A 514      32.749  63.918  51.176  1.00 50.37           C  
-ATOM   3923  OE1 GLN A 514      32.742  63.829  49.961  1.00 54.52           O  
-ATOM   3924  NE2 GLN A 514      33.595  63.232  51.934  1.00 54.93           N  
-ATOM   3925  N   ARG A 515      28.572  62.430  53.950  1.00 22.03           N  
-ATOM   3926  CA  ARG A 515      28.017  61.340  54.718  1.00 25.43           C  
-ATOM   3927  C   ARG A 515      27.241  61.698  55.989  1.00 26.46           C  
-ATOM   3928  O   ARG A 515      27.659  61.338  57.085  1.00 28.69           O  
-ATOM   3929  CB  ARG A 515      29.141  60.360  55.035  1.00 22.70           C  
-ATOM   3930  CG  ARG A 515      30.029  60.068  53.829  1.00 28.79           C  
-ATOM   3931  CD  ARG A 515      30.769  58.730  53.914  1.00 32.56           C  
-ATOM   3932  NE  ARG A 515      31.746  58.638  52.841  1.00 36.56           N  
-ATOM   3933  N   LEU A 516      26.088  62.384  55.818  1.00 26.31           N  
-ATOM   3934  CA  LEU A 516      25.240  62.770  56.973  1.00 23.29           C  
-ATOM   3935  C   LEU A 516      25.011  61.575  57.903  1.00 23.73           C  
-ATOM   3936  O   LEU A 516      24.396  60.585  57.519  1.00 27.68           O  
-ATOM   3937  CB  LEU A 516      23.860  63.311  56.494  1.00 18.50           C  
-ATOM   3938  CG  LEU A 516      22.863  63.749  57.589  1.00 14.83           C  
-ATOM   3939  CD1 LEU A 516      23.390  64.914  58.426  1.00 12.67           C  
-ATOM   3940  CD2 LEU A 516      21.511  64.142  56.982  1.00 13.11           C  
-ATOM   3941  N   ARG A 517      25.558  61.711  59.122  1.00 20.27           N  
-ATOM   3942  CA  ARG A 517      25.469  60.716  60.191  1.00 17.84           C  
-ATOM   3943  C   ARG A 517      25.761  59.285  59.806  1.00 15.26           C  
-ATOM   3944  O   ARG A 517      24.978  58.420  60.175  1.00 16.45           O  
-ATOM   3945  CB  ARG A 517      24.117  60.794  60.935  1.00 19.67           C  
-ATOM   3946  CG  ARG A 517      23.890  62.214  61.487  1.00 30.15           C  
-ATOM   3947  CD  ARG A 517      22.794  62.298  62.550  1.00 36.82           C  
-ATOM   3948  NE  ARG A 517      23.183  61.635  63.783  1.00 41.57           N  
-ATOM   3949  CZ  ARG A 517      23.891  62.251  64.733  1.00 43.20           C  
-ATOM   3950  NH1 ARG A 517      24.358  63.482  64.526  1.00 47.32           N  
-ATOM   3951  NH2 ARG A 517      24.121  61.624  65.890  1.00 42.62           N  
-ATOM   3952  N   VAL A 518      26.889  59.019  59.127  1.00 13.18           N  
-ATOM   3953  CA  VAL A 518      27.135  57.612  58.778  1.00 17.36           C  
-ATOM   3954  C   VAL A 518      27.213  56.664  59.963  1.00 18.52           C  
-ATOM   3955  O   VAL A 518      26.413  55.754  60.096  1.00 14.69           O  
-ATOM   3956  CB  VAL A 518      28.401  57.398  57.912  1.00 18.87           C  
-ATOM   3957  CG1 VAL A 518      27.970  57.120  56.474  1.00 28.46           C  
-ATOM   3958  CG2 VAL A 518      29.428  58.554  57.996  1.00 21.55           C  
-ATOM   3959  N   GLN A 519      28.214  56.902  60.832  1.00 22.65           N  
-ATOM   3960  CA  GLN A 519      28.449  56.063  62.017  1.00 24.45           C  
-ATOM   3961  C   GLN A 519      27.175  55.603  62.702  1.00 22.52           C  
-ATOM   3962  O   GLN A 519      26.929  54.421  62.883  1.00 24.00           O  
-ATOM   3963  CB  GLN A 519      29.347  56.800  63.032  1.00 32.94           C  
-ATOM   3964  CG  GLN A 519      30.815  57.005  62.565  1.00 45.37           C  
-ATOM   3965  CD  GLN A 519      31.899  56.076  63.138  1.00 53.76           C  
-ATOM   3966  OE1 GLN A 519      32.995  56.074  62.600  1.00 55.27           O  
-ATOM   3967  NE2 GLN A 519      31.604  55.292  64.188  1.00 57.01           N  
-ATOM   3968  N   MET A 520      26.362  56.589  63.069  1.00 18.13           N  
-ATOM   3969  CA  MET A 520      25.139  56.218  63.731  1.00 17.36           C  
-ATOM   3970  C   MET A 520      24.192  55.493  62.790  1.00 17.54           C  
-ATOM   3971  O   MET A 520      23.574  54.475  63.097  1.00 20.36           O  
-ATOM   3972  CB  MET A 520      24.492  57.463  64.356  1.00 21.26           C  
-ATOM   3973  CG  MET A 520      25.296  58.011  65.558  1.00 29.41           C  
-ATOM   3974  SD  MET A 520      25.354  56.747  66.907  1.00 39.85           S  
-ATOM   3975  CE  MET A 520      27.122  56.322  67.005  1.00 34.92           C  
-ATOM   3976  N   CYS A 521      24.081  56.023  61.579  1.00 17.21           N  
-ATOM   3977  CA  CYS A 521      23.154  55.371  60.677  1.00 14.00           C  
-ATOM   3978  C   CYS A 521      23.529  53.950  60.292  1.00 16.98           C  
-ATOM   3979  O   CYS A 521      22.612  53.181  60.031  1.00 17.51           O  
-ATOM   3980  CB  CYS A 521      22.786  56.281  59.529  1.00  8.52           C  
-ATOM   3981  SG  CYS A 521      21.751  57.655  60.125  1.00 16.59           S  
-ATOM   3982  N   VAL A 522      24.819  53.545  60.268  1.00 17.40           N  
-ATOM   3983  CA  VAL A 522      25.074  52.145  59.913  1.00 18.14           C  
-ATOM   3984  C   VAL A 522      24.569  51.258  61.053  1.00 19.65           C  
-ATOM   3985  O   VAL A 522      24.107  50.131  60.864  1.00 20.84           O  
-ATOM   3986  CB  VAL A 522      26.535  51.858  59.422  1.00 18.71           C  
-ATOM   3987  CG1 VAL A 522      27.443  53.092  59.300  1.00 18.10           C  
-ATOM   3988  CG2 VAL A 522      27.275  50.710  60.133  1.00 19.79           C  
-ATOM   3989  N   PHE A 523      24.641  51.823  62.273  1.00 17.39           N  
-ATOM   3990  CA  PHE A 523      24.176  51.083  63.433  1.00  9.03           C  
-ATOM   3991  C   PHE A 523      22.695  50.785  63.259  1.00  8.45           C  
-ATOM   3992  O   PHE A 523      22.258  49.643  63.346  1.00  3.41           O  
-ATOM   3993  CB  PHE A 523      24.518  51.825  64.769  1.00  7.45           C  
-ATOM   3994  CG  PHE A 523      23.720  51.305  65.945  1.00  5.37           C  
-ATOM   3995  CD1 PHE A 523      24.035  50.067  66.541  1.00  6.23           C  
-ATOM   3996  CD2 PHE A 523      22.576  52.001  66.370  1.00  3.83           C  
-ATOM   3997  CE1 PHE A 523      23.190  49.508  67.508  1.00  2.00           C  
-ATOM   3998  CE2 PHE A 523      21.724  51.438  67.331  1.00  7.44           C  
-ATOM   3999  CZ  PHE A 523      22.026  50.187  67.892  1.00  6.72           C  
-ATOM   4000  N   TRP A 524      21.937  51.834  62.952  1.00  7.86           N  
-ATOM   4001  CA  TRP A 524      20.500  51.585  62.835  1.00 11.10           C  
-ATOM   4002  C   TRP A 524      20.040  50.879  61.586  1.00 15.89           C  
-ATOM   4003  O   TRP A 524      19.126  50.063  61.596  1.00 17.80           O  
-ATOM   4004  CB  TRP A 524      19.715  52.895  62.845  1.00 12.61           C  
-ATOM   4005  CG  TRP A 524      19.798  53.607  64.177  1.00 15.47           C  
-ATOM   4006  CD1 TRP A 524      20.569  54.758  64.435  1.00 15.71           C  
-ATOM   4007  CD2 TRP A 524      19.075  53.306  65.356  1.00 18.98           C  
-ATOM   4008  NE1 TRP A 524      20.342  55.184  65.697  1.00 20.24           N  
-ATOM   4009  CE2 TRP A 524      19.442  54.362  66.316  1.00 19.98           C  
-ATOM   4010  CE3 TRP A 524      18.150  52.319  65.742  1.00 19.46           C  
-ATOM   4011  CZ2 TRP A 524      18.834  54.384  67.573  1.00 19.02           C  
-ATOM   4012  CZ3 TRP A 524      17.566  52.368  67.018  1.00 17.22           C  
-ATOM   4013  CH2 TRP A 524      17.898  53.396  67.915  1.00 18.94           C  
-ATOM   4014  N   ASN A 525      20.692  51.232  60.494  1.00 17.10           N  
-ATOM   4015  CA  ASN A 525      20.282  50.645  59.219  1.00 16.79           C  
-ATOM   4016  C   ASN A 525      20.845  49.277  58.944  1.00 14.42           C  
-ATOM   4017  O   ASN A 525      20.261  48.520  58.189  1.00 16.93           O  
-ATOM   4018  CB  ASN A 525      20.606  51.587  58.051  1.00 17.20           C  
-ATOM   4019  CG  ASN A 525      19.745  52.837  58.125  1.00 18.04           C  
-ATOM   4020  OD1 ASN A 525      18.776  52.946  58.867  1.00 21.34           O  
-ATOM   4021  ND2 ASN A 525      20.136  53.832  57.342  1.00 14.58           N  
-ATOM   4022  N   GLN A 526      21.976  48.930  59.546  1.00 12.51           N  
-ATOM   4023  CA  GLN A 526      22.513  47.607  59.243  1.00 14.28           C  
-ATOM   4024  C   GLN A 526      22.716  46.736  60.470  1.00 16.98           C  
-ATOM   4025  O   GLN A 526      22.320  45.578  60.494  1.00 19.08           O  
-ATOM   4026  CB  GLN A 526      23.829  47.745  58.438  1.00 13.48           C  
-ATOM   4027  CG  GLN A 526      23.650  48.678  57.207  1.00 17.90           C  
-ATOM   4028  N   PHE A 527      23.318  47.297  61.527  1.00 16.07           N  
-ATOM   4029  CA  PHE A 527      23.563  46.421  62.686  1.00 16.54           C  
-ATOM   4030  C   PHE A 527      22.332  46.007  63.488  1.00 16.59           C  
-ATOM   4031  O   PHE A 527      22.007  44.828  63.604  1.00 13.61           O  
-ATOM   4032  CB  PHE A 527      24.655  47.012  63.596  1.00 14.68           C  
-ATOM   4033  CG  PHE A 527      25.076  46.046  64.677  1.00 10.73           C  
-ATOM   4034  CD1 PHE A 527      25.852  44.917  64.363  1.00 11.88           C  
-ATOM   4035  CD2 PHE A 527      24.671  46.263  66.008  1.00 12.72           C  
-ATOM   4036  CE1 PHE A 527      26.214  44.004  65.365  1.00 13.01           C  
-ATOM   4037  CE2 PHE A 527      25.025  45.356  67.012  1.00  8.78           C  
-ATOM   4038  CZ  PHE A 527      25.794  44.223  66.689  1.00 12.29           C  
-ATOM   4039  N   LEU A 528      21.662  47.022  64.063  1.00 16.71           N  
-ATOM   4040  CA  LEU A 528      20.475  46.833  64.892  1.00 14.70           C  
-ATOM   4041  C   LEU A 528      19.553  45.799  64.305  1.00 18.13           C  
-ATOM   4042  O   LEU A 528      19.262  44.812  64.965  1.00 20.42           O  
-ATOM   4043  CB  LEU A 528      19.785  48.171  65.282  1.00 15.48           C  
-ATOM   4044  CG  LEU A 528      18.899  48.182  66.562  1.00 17.15           C  
-ATOM   4045  CD1 LEU A 528      17.433  47.902  66.268  1.00 17.51           C  
-ATOM   4046  CD2 LEU A 528      19.384  47.234  67.680  1.00 22.24           C  
-ATOM   4047  N   PRO A 529      19.117  45.982  63.041  1.00 21.47           N  
-ATOM   4048  CA  PRO A 529      18.174  45.038  62.469  1.00 19.45           C  
-ATOM   4049  C   PRO A 529      18.692  43.611  62.490  1.00 19.92           C  
-ATOM   4050  O   PRO A 529      17.931  42.702  62.791  1.00 22.84           O  
-ATOM   4051  CB  PRO A 529      17.891  45.584  61.059  1.00 20.48           C  
-ATOM   4052  CG  PRO A 529      18.428  47.033  61.030  1.00 22.90           C  
-ATOM   4053  CD  PRO A 529      19.505  47.054  62.112  1.00 24.83           C  
-ATOM   4054  N   LYS A 530      19.993  43.418  62.184  1.00 20.19           N  
-ATOM   4055  CA  LYS A 530      20.520  42.043  62.197  1.00 21.49           C  
-ATOM   4056  C   LYS A 530      20.456  41.436  63.567  1.00 22.31           C  
-ATOM   4057  O   LYS A 530      20.130  40.275  63.761  1.00 21.11           O  
-ATOM   4058  CB  LYS A 530      22.023  41.919  61.863  1.00 24.91           C  
-ATOM   4059  CG  LYS A 530      22.412  42.144  60.399  1.00 33.70           C  
-ATOM   4060  CD  LYS A 530      23.846  41.645  60.116  1.00 35.91           C  
-ATOM   4061  CE  LYS A 530      23.982  40.107  60.198  1.00 38.83           C  
-ATOM   4062  NZ  LYS A 530      25.241  39.667  59.617  1.00 41.88           N  
-ATOM   4063  N   LEU A 531      20.847  42.280  64.517  1.00 22.30           N  
-ATOM   4064  CA  LEU A 531      20.876  41.865  65.898  1.00 18.46           C  
-ATOM   4065  C   LEU A 531      19.522  41.358  66.294  1.00 17.79           C  
-ATOM   4066  O   LEU A 531      19.353  40.208  66.678  1.00 16.65           O  
-ATOM   4067  CB  LEU A 531      21.411  43.010  66.772  1.00 17.72           C  
-ATOM   4068  CG  LEU A 531      21.552  42.671  68.270  1.00 15.86           C  
-ATOM   4069  CD1 LEU A 531      22.744  43.392  68.889  1.00 16.38           C  
-ATOM   4070  CD2 LEU A 531      20.288  43.038  69.055  1.00 16.82           C  
-ATOM   4071  N   LEU A 532      18.546  42.244  66.105  1.00 15.97           N  
-ATOM   4072  CA  LEU A 532      17.185  41.887  66.469  1.00 20.58           C  
-ATOM   4073  C   LEU A 532      16.678  40.657  65.760  1.00 24.00           C  
-ATOM   4074  O   LEU A 532      15.829  39.963  66.296  1.00 29.22           O  
-ATOM   4075  CB  LEU A 532      16.181  43.042  66.267  1.00 15.90           C  
-ATOM   4076  CG  LEU A 532      16.396  44.267  67.183  1.00 18.48           C  
-ATOM   4077  CD1 LEU A 532      15.331  45.338  66.923  1.00 16.50           C  
-ATOM   4078  CD2 LEU A 532      16.394  43.907  68.686  1.00 17.77           C  
-ATOM   4079  N   ASN A 533      17.185  40.405  64.549  1.00 27.83           N  
-ATOM   4080  CA  ASN A 533      16.745  39.236  63.789  1.00 28.48           C  
-ATOM   4081  C   ASN A 533      17.405  37.945  64.224  1.00 30.57           C  
-ATOM   4082  O   ASN A 533      16.837  36.864  64.159  1.00 29.70           O  
-ATOM   4083  CB  ASN A 533      17.090  39.419  62.312  1.00 26.73           C  
-ATOM   4084  N   ALA A 534      18.662  38.069  64.651  1.00 32.89           N  
-ATOM   4085  CA  ALA A 534      19.349  36.857  65.054  1.00 36.26           C  
-ATOM   4086  C   ALA A 534      18.814  36.337  66.354  1.00 42.30           C  
-ATOM   4087  O   ALA A 534      18.765  35.133  66.595  1.00 44.56           O  
-ATOM   4088  CB  ALA A 534      20.852  37.072  65.222  1.00 32.57           C  
-ATOM   4089  N   THR A 535      18.484  37.298  67.215  1.00 47.29           N  
-ATOM   4090  CA  THR A 535      17.953  36.960  68.511  1.00 51.46           C  
-ATOM   4091  C   THR A 535      16.502  36.487  68.376  1.00 53.10           C  
-ATOM   4092  O   THR A 535      15.627  37.055  69.040  1.00 57.37           O  
-ATOM   4093  CB  THR A 535      18.060  38.196  69.422  1.00 53.08           C  
-ATOM   4094  OG1 THR A 535      19.279  38.910  69.244  1.00 52.38           O  
-ATOM   4095  CG2 THR A 535      18.026  37.829  70.916  1.00 59.93           C  
-TER    4096      THR A 535                                                      
-HETATM 4097  C1  THA A 999       6.362  71.261  69.025  1.00 22.38           C  
-HETATM 4098  C2  THA A 999       6.697  70.955  67.712  1.00 25.41           C  
-HETATM 4099  C3  THA A 999       5.719  70.518  66.819  1.00 24.66           C  
-HETATM 4100  C4  THA A 999       4.351  70.381  67.260  1.00 21.70           C  
-HETATM 4101  C5  THA A 999       4.056  70.702  68.603  1.00 20.76           C  
-HETATM 4102  C6  THA A 999       5.053  71.136  69.468  1.00 18.93           C  
-HETATM 4103  N7  THA A 999       6.068  70.236  65.585  1.00 21.62           N  
-HETATM 4104  C8  THA A 999       5.207  69.821  64.683  1.00 20.49           C  
-HETATM 4105  C9  THA A 999       3.833  69.634  64.995  1.00 19.83           C  
-HETATM 4106  C10 THA A 999       3.396  69.933  66.309  1.00 17.75           C  
-HETATM 4107  C11 THA A 999       5.776  69.459  63.289  1.00 18.30           C  
-HETATM 4108  C12 THA A 999       4.736  69.363  62.145  1.00 20.27           C  
-HETATM 4109  C13 THA A 999       3.515  68.540  62.597  1.00 19.36           C  
-HETATM 4110  C14 THA A 999       2.860  69.177  63.848  1.00 21.42           C  
-HETATM 4111  N15 THA A 999       2.092  69.798  66.625  1.00 20.69           N  
-HETATM 4112  O   HOH A 601      21.436  52.967  54.670  1.00 16.26           O  
-HETATM 4113  O   HOH A 602      -9.713  62.939  60.080  1.00  9.25           O  
-HETATM 4114  O   HOH A 603      24.198  67.851  85.549  1.00 70.20           O  
-HETATM 4115  O   HOH A 604       3.897  69.768  58.109  1.00  2.00           O  
-HETATM 4116  O   HOH A 605      -1.728  70.694  53.271  1.00  6.67           O  
-HETATM 4117  O   HOH A 606     -14.301  59.527  57.034  1.00  6.46           O  
-HETATM 4118  O   HOH A 607      -2.078  69.350  67.406  1.00 12.08           O  
-HETATM 4119  O   HOH A 608      -6.865  62.657  65.578  1.00 12.95           O  
-HETATM 4120  O   HOH A 609       0.027  70.297  60.632  1.00  6.46           O  
-HETATM 4121  O   HOH A 610      -3.893  52.228  41.330  1.00 39.68           O  
-HETATM 4122  O   HOH A 611       7.233  80.005  68.092  1.00 36.26           O  
-HETATM 4123  O   HOH A 612      24.646  60.791  40.027  1.00 18.08           O  
-HETATM 4124  O   HOH A 613      21.313  59.198  38.314  1.00 36.84           O  
-HETATM 4125  O   HOH A 614      -0.421  64.062  59.320  1.00 12.50           O  
-HETATM 4126  O   HOH A 615       0.001  83.914  58.002  1.00 43.23           O  
-HETATM 4127  O   HOH A 616      -0.460  66.877  69.033  1.00 36.24           O  
-HETATM 4128  O   HOH A 617       2.101  41.668  61.980  1.00 40.25           O  
-HETATM 4129  O   HOH A 618      10.934  56.303  68.662  1.00 12.08           O  
-HETATM 4130  O   HOH A 619       2.682  81.870  62.939  1.00 32.61           O  
-HETATM 4131  O   HOH A 620       3.300  53.939  63.596  1.00 18.53           O  
-HETATM 4132  O   HOH A 621      10.421  48.537  38.102  1.00 64.57           O  
-HETATM 4133  O   HOH A 622      18.266  72.459  85.879  1.00 58.97           O  
-HETATM 4134  O   HOH A 623      -1.187  96.318  44.308  1.00 54.71           O  
-HETATM 4135  O   HOH A 624      10.416  69.328  59.826  1.00  5.83           O  
-HETATM 4136  O   HOH A 625     -12.114  68.571  37.502  1.00 32.99           O  
-HETATM 4137  O   HOH A 626      -6.304  61.451  71.954  1.00 42.24           O  
-HETATM 4138  O   HOH A 627      -6.447  50.296  61.416  1.00 10.24           O  
-HETATM 4139  O   HOH A 628       2.152  63.062  72.710  1.00 61.59           O  
-HETATM 4140  O   HOH A 629      31.963  66.709  56.534  1.00 16.65           O  
-HETATM 4141  O   HOH A 630       9.379  58.011  85.633  1.00 44.47           O  
-HETATM 4142  O   HOH A 631      -7.920  58.968  44.298  1.00 42.11           O  
-HETATM 4143  O   HOH A 632       9.288  57.159  35.791  1.00 36.44           O  
-HETATM 4144  O   HOH A 633      -3.902  51.644  60.543  1.00  9.44           O  
-HETATM 4145  O   HOH A 634      -0.179  69.329  64.529  1.00 24.06           O  
-HETATM 4146  O   HOH A 635      12.302  66.886  33.785  1.00 33.25           O  
-HETATM 4147  O   HOH A 636      -0.829  58.797  69.112  1.00 22.60           O  
-HETATM 4148  O   HOH A 637       5.229  58.019  35.824  1.00 20.86           O  
-HETATM 4149  O   HOH A 638       6.341  81.499  64.810  1.00 23.90           O  
-HETATM 4150  O   HOH A 639     -12.258  64.448  59.540  1.00 42.34           O  
-HETATM 4151  O   HOH A 640       7.609  52.533  56.827  1.00 30.17           O  
-HETATM 4152  O   HOH A 641      24.358  57.909  56.015  1.00 36.95           O  
-HETATM 4153  O   HOH A 642       5.862  63.777  80.088  1.00 61.65           O  
-HETATM 4154  O   HOH A 643       0.529  71.248  68.951  1.00 20.34           O  
-HETATM 4155  O   HOH A 644      11.370  63.907  35.699  1.00 19.83           O  
-HETATM 4156  O   HOH A 645       2.328  91.164  54.939  1.00 13.04           O  
-HETATM 4157  O   HOH A 646     -15.401  67.703  52.231  1.00 24.77           O  
-HETATM 4158  O   HOH A 647      -2.176  79.106  62.623  1.00 32.03           O  
-HETATM 4159  O   HOH A 648      25.329  55.453  53.425  1.00 40.01           O  
-HETATM 4160  O   HOH A 649      25.021  64.798  35.997  1.00 30.72           O  
-HETATM 4161  O   HOH A 650      13.669  47.295  59.660  1.00 45.32           O  
-HETATM 4162  O   HOH A 651     -13.244  50.312  44.199  1.00 54.67           O  
-HETATM 4163  O   HOH A 652       3.242  83.352  32.284  1.00 34.21           O  
-HETATM 4164  O   HOH A 653      -5.381  58.887  37.832  1.00 40.03           O  
-HETATM 4165  O   HOH A 654      12.644  49.806  33.065  1.00 51.32           O  
-HETATM 4166  O   HOH A 655       7.810  76.268  61.395  1.00 50.53           O  
-HETATM 4167  O   HOH A 656      -0.969  59.532  33.421  1.00 25.89           O  
-HETATM 4168  O   HOH A 657     -14.849  67.281  39.525  1.00 42.11           O  
-HETATM 4169  O   HOH A 658     -18.694  86.088  50.675  1.00 47.80           O  
-HETATM 4170  O   HOH A 659     -15.520  83.163  31.580  1.00 47.06           O  
-HETATM 4171  O   HOH A 660      21.328  50.999  53.078  1.00 17.17           O  
-HETATM 4172  O   HOH A 661      18.419  92.769  62.731  1.00 36.34           O  
-HETATM 4173  O   HOH A 662      29.951  58.597  85.155  1.00 72.74           O  
-HETATM 4174  O   HOH A 663      20.915  62.497  36.857  1.00 27.46           O  
-HETATM 4175  O   HOH A 664      23.889  59.314  35.821  1.00 40.76           O  
-HETATM 4176  O   HOH A 665      -0.387  90.815  55.611  1.00 41.40           O  
-HETATM 4177  O   HOH A 666       4.850  58.304  76.420  1.00 53.69           O  
-HETATM 4178  O   HOH A 667      19.660  62.741  32.748  1.00 83.14           O  
-HETATM 4179  O   HOH A 668     -19.347  84.392  54.165  1.00 37.79           O  
-HETATM 4180  O   HOH A 669      11.705  50.605  81.909  1.00 43.68           O  
-HETATM 4181  O   HOH A 670      13.043  77.224  85.640  1.00 50.32           O  
-HETATM 4182  O   HOH A 671      32.987  69.879  57.554  1.00 28.33           O  
-HETATM 4183  O   HOH A 672      22.971  53.558  52.370  1.00 84.49           O  
-HETATM 4184  O   HOH A 673      15.230  62.617  89.723  1.00 55.09           O  
-HETATM 4185  O   HOH A 674       8.378  94.303  47.727  1.00 56.64           O  
-HETATM 4186  O   HOH A 675     -21.202  67.831  58.722  1.00 68.40           O  
-HETATM 4187  O   HOH A 676     -11.439  84.351  57.579  1.00 46.30           O  
-HETATM 4188  O   HOH A 677      16.299  59.930  32.317  1.00 40.67           O  
-HETATM 4189  O   HOH A 678       3.879  46.681  60.148  1.00 67.54           O  
-HETATM 4190  O   HOH A 679      17.253  64.097  87.165  1.00 52.19           O  
-HETATM 4191  O   HOH A 680      19.551  31.826  68.006  1.00 39.50           O  
-HETATM 4192  O   HOH A 681      23.095  67.354  48.330  1.00 12.96           O  
-HETATM 4193  O   HOH A 682     -13.326  47.816  47.354  1.00 46.29           O  
-CONECT  481  697                                                                
-CONECT  697  481                                                                
-CONECT 1911 1989                                                                
-CONECT 1989 1911                                                                
-CONECT 3042 3981                                                                
-CONECT 3981 3042                                                                
-CONECT 4097 4098 4102                                                           
-CONECT 4098 4097 4099                                                           
-CONECT 4099 4098 4100 4103                                                      
-CONECT 4100 4099 4101 4106                                                      
-CONECT 4101 4100 4102                                                           
-CONECT 4102 4097 4101                                                           
-CONECT 4103 4099 4104                                                           
-CONECT 4104 4103 4105 4107                                                      
-CONECT 4105 4104 4106 4110                                                      
-CONECT 4106 4100 4105 4111                                                      
-CONECT 4107 4104 4108                                                           
-CONECT 4108 4107 4109                                                           
-CONECT 4109 4108 4110                                                           
-CONECT 4110 4105 4109                                                           
-CONECT 4111 4106                                                                
-MASTER      442    2    1   15   14    0    3    6 4192    1   21   42          
-END                                                                             
diff --git a/plip/test/pdb/1aku.pdb b/plip/test/pdb/1aku.pdb
deleted file mode 100644
index 3bf66d3..0000000
--- a/plip/test/pdb/1aku.pdb
+++ /dev/null
@@ -1,1765 +0,0 @@
-HEADER    ELECTRON TRANSPORT                      27-MAY-97   1AKU              
-TITLE     D95A HYDROQUINONE FLAVODOXIN MUTANT FROM D. VULGARIS                  
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: FLAVODOXIN;                                                
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 ENGINEERED: YES;                                                     
-COMPND   5 MUTATION: YES;                                                       
-COMPND   6 OTHER_DETAILS: HYDROQUINONE                                          
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS SUBSP.                   
-SOURCE   3 VULGARIS STR. HILDENBOROUGH;                                         
-SOURCE   4 ORGANISM_TAXID: 882;                                                 
-SOURCE   5 STRAIN: HILDENBOROUGH;                                               
-SOURCE   6 CELLULAR_LOCATION: CYTOPLASM;                                        
-SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   9 EXPRESSION_SYSTEM_STRAIN: TG2                                        
-KEYWDS    ELECTRON TRANSPORT, ELECTRON TRANSFER, FLAVOPROTEIN, FMN,             
-KEYWDS   2 FLAVODOXIN, MUTANT                                                   
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    A.MCCARTHY,M.WALSH,T.HIGGINS                                          
-REVDAT   3   24-FEB-09 1AKU    1       VERSN                                    
-REVDAT   2   23-DEC-02 1AKU    1       JRNL                                     
-REVDAT   1   02-DEC-98 1AKU    0                                                
-JRNL        AUTH   A.A.MCCARTHY,M.A.WALSH,C.S.VERMA,D.P.O'CONNELL,              
-JRNL        AUTH 2 M.REINHOLD,G.N.YALLOWAY,D.D'ARCY,T.M.HIGGINS,                
-JRNL        AUTH 3 G.VOORDOUW,S.G.MAYHEW                                        
-JRNL        TITL   CRYSTALLOGRAPHIC INVESTIGATION OF THE ROLE OF                
-JRNL        TITL 2 ASPARTATE 95 IN THE MODULATION OF THE REDOX                  
-JRNL        TITL 3 POTENTIALS OF DESULFOVIBRIO VULGARIS FLAVODOXIN.             
-JRNL        REF    BIOCHEMISTRY                  V.  41 10950 2002              
-JRNL        REFN                   ISSN 0006-2960                               
-JRNL        PMID   12206666                                                     
-JRNL        DOI    10.1021/BI020225H                                            
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   A.MCCARTHY                                                   
-REMARK   1  TITL   X-RAY CRYSTALLOGRAPHIC STUDIES ON THE FLAVIN                 
-REMARK   1  TITL 2 BINDING SITE OF FLAVODOXIN FROM DESULFOVIBRIO                
-REMARK   1  TITL 3 VULGARIS                                                     
-REMARK   1  REF    THESIS, NATIONAL UNIVERSITY                1997              
-REMARK   1  REF  2 OF IRELAND                                                   
-REMARK   1  PUBL   DUBLIN : NATIONAL UNIVERSITY OF IRELAND (THESIS)             
-REMARK   1  REFN                                                                
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PROLSQ                                               
-REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
-REMARK   3   NUMBER OF REFLECTIONS             : 16098                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
-REMARK   3   R VALUE            (WORKING SET) : 0.212                           
-REMARK   3   FREE R VALUE                     : 0.270                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 805                             
-REMARK   3                                                                      
-REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
-REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.2150                 
-REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.2120                 
-REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.270                  
-REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
-REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 805                    
-REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 16098                  
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 1101                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 41                                      
-REMARK   3   SOLVENT ATOMS            : 155                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 21.70                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.60                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.15                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 12.00                           
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
-REMARK   3    BOND LENGTH                     (A) : 0.015 ; 0.020               
-REMARK   3    ANGLE DISTANCE                  (A) : 0.047 ; 0.050               
-REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.045 ; 0.040               
-REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
-REMARK   3                                                                      
-REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
-REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.170 ; 0.150               
-REMARK   3                                                                      
-REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
-REMARK   3    SINGLE TORSION                  (A) : 0.180 ; 0.300               
-REMARK   3    MULTIPLE TORSION                (A) : 0.260 ; 0.300               
-REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
-REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
-REMARK   3                                                                      
-REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
-REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
-REMARK   3    PLANAR                    (DEGREES) : 2.340 ; 3.000               
-REMARK   3    STAGGERED                 (DEGREES) : 19.460; 15.000              
-REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
-REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
-REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
-REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1AKU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : AUG-95                             
-REMARK 200  TEMPERATURE           (KELVIN) : 120                                
-REMARK 200  PH                             : 7.0                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
-REMARK 200  BEAMLINE                       : X11                                
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.937                              
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
-REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16098                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
-REMARK 200  DATA REDUNDANCY                : 4.400                              
-REMARK 200  R MERGE                    (I) : 0.42000                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7800                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: AMORE                                                 
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 60-70% AMMONIUM SULFATE, 100MM TRIS      
-REMARK 280  -HCL, PH=7.0.                                                       
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,-Y,Z+1/2                                             
-REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
-REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
-REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
-REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
-REMARK 290       7555   Y,X,-Z                                                  
-REMARK 290       8555   -Y,-X,-Z+1/2                                            
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.13000            
-REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       26.30000            
-REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       26.30000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      105.19500            
-REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       26.30000            
-REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       26.30000            
-REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       35.06500            
-REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       26.30000            
-REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       26.30000            
-REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      105.19500            
-REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       26.30000            
-REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       26.30000            
-REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       35.06500            
-REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       70.13000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   OE1  GLU A    32     O    HOH A   259              2.01            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
-REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
-REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
-REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
-REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
-REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
-REMARK 500                                                                      
-REMARK 500 DISTANCE CUTOFF:                                                     
-REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
-REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
-REMARK 500   O    HOH A   249     O    HOH A   261     4455     1.87            
-REMARK 500   O    HOH A   220     O    HOH A   261     4455     2.16            
-REMARK 500   O    HOH A   253     O    HOH A   257     6565     2.19            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    ARG A  24   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
-REMARK 500    ASP A  28   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
-REMARK 500    TYR A  31   CB  -  CG  -  CD2 ANGL. DEV. =  -4.9 DEGREES          
-REMARK 500    TYR A  31   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES          
-REMARK 500    GLU A  32   OE1 -  CD  -  OE2 ANGL. DEV. =  10.2 DEGREES          
-REMARK 500    GLY A  61   CA  -  C   -  O   ANGL. DEV. =  11.3 DEGREES          
-REMARK 500    ASP A  62   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
-REMARK 500    ASP A  63   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
-REMARK 500    ASP A  63   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
-REMARK 500    ASP A  63   CA  -  C   -  O   ANGL. DEV. =  14.3 DEGREES          
-REMARK 500    ASP A  63   O   -  C   -  N   ANGL. DEV. =  -9.8 DEGREES          
-REMARK 500    GLU A  66   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES          
-REMARK 500    ASP A  70   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
-REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
-REMARK 500    TYR A  98   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES          
-REMARK 500    ASP A 106   CB  -  CG  -  OD1 ANGL. DEV. =  -7.4 DEGREES          
-REMARK 500    ASP A 106   CB  -  CG  -  OD2 ANGL. DEV. =   8.8 DEGREES          
-REMARK 500    LYS A 113   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
-REMARK 500    GLN A 121   CA  -  CB  -  CG  ANGL. DEV. =  17.9 DEGREES          
-REMARK 500    ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.4 DEGREES          
-REMARK 500    ASP A 129   CB  -  CG  -  OD1 ANGL. DEV. =   9.7 DEGREES          
-REMARK 500    ASP A 129   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
-REMARK 500    ARG A 134   CG  -  CD  -  NE  ANGL. DEV. = -13.3 DEGREES          
-REMARK 500    ARG A 134   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
-REMARK 500    ARG A 134   NH1 -  CZ  -  NH2 ANGL. DEV. =   9.4 DEGREES          
-REMARK 500    ARG A 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    SER A  64       90.70   -169.32                                   
-REMARK 500    TYR A 100       79.32   -108.88                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A 228        DISTANCE =  8.12 ANGSTROMS                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: FMN                                                 
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: FMN CO-FACTOR.                                     
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 149                 
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 150                 
-DBREF  1AKU A    2   148  UNP    P00323   FLAV_DESVH       2    148             
-SEQADV 1AKU ALA A   95  UNP  P00323    ASP    95 ENGINEERED                     
-SEQRES   1 A  147  PRO LYS ALA LEU ILE VAL TYR GLY SER THR THR GLY ASN          
-SEQRES   2 A  147  THR GLU TYR THR ALA GLU THR ILE ALA ARG GLU LEU ALA          
-SEQRES   3 A  147  ASP ALA GLY TYR GLU VAL ASP SER ARG ASP ALA ALA SER          
-SEQRES   4 A  147  VAL GLU ALA GLY GLY LEU PHE GLU GLY PHE ASP LEU VAL          
-SEQRES   5 A  147  LEU LEU GLY CYS SER THR TRP GLY ASP ASP SER ILE GLU          
-SEQRES   6 A  147  LEU GLN ASP ASP PHE ILE PRO LEU PHE ASP SER LEU GLU          
-SEQRES   7 A  147  GLU THR GLY ALA GLN GLY ARG LYS VAL ALA CYS PHE GLY          
-SEQRES   8 A  147  CYS GLY ALA SER SER TYR GLU TYR PHE CYS GLY ALA VAL          
-SEQRES   9 A  147  ASP ALA ILE GLU GLU LYS LEU LYS ASN LEU GLY ALA GLU          
-SEQRES  10 A  147  ILE VAL GLN ASP GLY LEU ARG ILE ASP GLY ASP PRO ARG          
-SEQRES  11 A  147  ALA ALA ARG ASP ASP ILE VAL GLY TRP ALA HIS ASP VAL          
-SEQRES  12 A  147  ARG GLY ALA ILE                                              
-HET    SO4  A   1       5                                                       
-HET    SO4  A 149       5                                                       
-HET    FMN  A 150      31                                                       
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
-HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
-FORMUL   2  SO4    2(O4 S 2-)                                                   
-FORMUL   4  FMN    C17 H21 N4 O9 P                                              
-FORMUL   5  HOH   *155(H2 O)                                                    
-HELIX    1   1 ASN A   14  ASP A   28  1                                  15    
-HELIX    2   2 ALA A   38  SER A   40  5                                   3    
-HELIX    3   3 ASP A   69  GLU A   80  1                                  12    
-HELIX    4   4 GLY A  103  ASN A  114  1                                  12    
-HELIX    5   5 PRO A  130  ALA A  132  5                                   3    
-HELIX    6   6 ARG A  134  GLY A  146  1                                  13    
-SHEET    1   A 5 GLU A  32  ASP A  37  0                                        
-SHEET    2   A 5 LYS A   3  GLY A   9  1  N  ALA A   4   O  GLU A  32           
-SHEET    3   A 5 LEU A  52  CYS A  57  1  N  LEU A  52   O  LEU A   5           
-SHEET    4   A 5 VAL A  88  GLY A  94  1  N  ALA A  89   O  VAL A  53           
-SHEET    5   A 5 LEU A 124  ASP A 127  1  N  LEU A 124   O  GLY A  92           
-SITE     1 FMN  1 FMN A 150                                                     
-SITE     1 AC1  3 GLU A  48  GLY A  49  ARG A  86                               
-SITE     1 AC2  3 TYR A  17  ARG A 131  HOH A 214                               
-SITE     1 AC3 24 SER A  10  THR A  11  THR A  12  GLY A  13                    
-SITE     2 AC3 24 ASN A  14  THR A  15  ASP A  28  SER A  58                    
-SITE     3 AC3 24 THR A  59  TRP A  60  GLY A  61  CYS A  93                    
-SITE     4 AC3 24 GLY A  94  ALA A  95  TYR A  98  TYR A 100                    
-SITE     5 AC3 24 PHE A 101  CYS A 102  HOH A 171  HOH A 173                    
-SITE     6 AC3 24 HOH A 185  HOH A 195  HOH A 225  HOH A 244                    
-CRYST1   52.600   52.600  140.260  90.00  90.00  90.00 P 43 21 2     8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.019011  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.019011  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.007130        0.00000                         
-ATOM      1  N   PRO A   2       2.201  26.003  -7.393  1.00 17.99           N  
-ATOM      2  CA  PRO A   2       3.317  26.075  -6.387  1.00 20.18           C  
-ATOM      3  C   PRO A   2       2.936  25.266  -5.164  1.00 17.44           C  
-ATOM      4  O   PRO A   2       1.746  24.988  -4.959  1.00 19.16           O  
-ATOM      5  CB  PRO A   2       3.639  27.555  -6.048  1.00 19.52           C  
-ATOM      6  CG  PRO A   2       2.890  28.318  -7.128  1.00 17.16           C  
-ATOM      7  CD  PRO A   2       1.735  27.429  -7.543  1.00 16.46           C  
-ATOM      8  N   LYS A   3       3.909  24.829  -4.361  1.00 22.63           N  
-ATOM      9  CA  LYS A   3       3.693  24.043  -3.147  1.00 20.00           C  
-ATOM     10  C   LYS A   3       4.112  24.888  -1.922  1.00 15.28           C  
-ATOM     11  O   LYS A   3       5.285  25.243  -1.804  1.00 16.34           O  
-ATOM     12  CB  LYS A   3       4.543  22.765  -3.055  1.00 23.35           C  
-ATOM     13  CG  LYS A   3       4.520  22.028  -4.370  1.00 34.29           C  
-ATOM     14  CD  LYS A   3       5.327  20.743  -4.329  1.00 48.37           C  
-ATOM     15  CE  LYS A   3       4.998  19.927  -5.583  1.00 55.02           C  
-ATOM     16  NZ  LYS A   3       6.077  18.988  -5.998  1.00 67.66           N  
-ATOM     17  N   ALA A   4       3.112  25.133  -1.094  1.00 18.10           N  
-ATOM     18  CA  ALA A   4       3.365  25.925   0.111  1.00 17.74           C  
-ATOM     19  C   ALA A   4       3.185  25.068   1.373  1.00 17.39           C  
-ATOM     20  O   ALA A   4       2.408  24.122   1.467  1.00 17.07           O  
-ATOM     21  CB  ALA A   4       2.407  27.119   0.204  1.00 12.34           C  
-ATOM     22  N   LEU A   5       3.987  25.381   2.401  1.00 15.37           N  
-ATOM     23  CA  LEU A   5       3.899  24.735   3.695  1.00 16.24           C  
-ATOM     24  C   LEU A   5       3.500  25.874   4.666  1.00 12.18           C  
-ATOM     25  O   LEU A   5       4.096  26.919   4.541  1.00 13.08           O  
-ATOM     26  CB  LEU A   5       5.267  24.297   4.169  1.00 17.07           C  
-ATOM     27  CG  LEU A   5       5.510  23.144   5.114  1.00 20.87           C  
-ATOM     28  CD1 LEU A   5       6.709  23.554   5.979  1.00 19.02           C  
-ATOM     29  CD2 LEU A   5       4.378  22.576   5.905  1.00 13.53           C  
-ATOM     30  N   ILE A   6       2.527  25.707   5.572  1.00 17.20           N  
-ATOM     31  CA  ILE A   6       2.093  26.667   6.576  1.00  9.35           C  
-ATOM     32  C   ILE A   6       2.346  25.978   7.942  1.00 10.33           C  
-ATOM     33  O   ILE A   6       1.851  24.872   8.125  1.00 12.16           O  
-ATOM     34  CB  ILE A   6       0.616  27.112   6.473  1.00 11.23           C  
-ATOM     35  CG1 ILE A   6       0.398  27.848   5.100  1.00  9.01           C  
-ATOM     36  CG2 ILE A   6       0.152  28.149   7.504  1.00 10.22           C  
-ATOM     37  CD1 ILE A   6      -1.086  28.094   4.826  1.00  8.83           C  
-ATOM     38  N   VAL A   7       3.167  26.541   8.836  1.00 14.72           N  
-ATOM     39  CA  VAL A   7       3.371  25.874  10.160  1.00 17.23           C  
-ATOM     40  C   VAL A   7       2.916  26.931  11.184  1.00 14.58           C  
-ATOM     41  O   VAL A   7       3.374  28.088  11.057  1.00 14.55           O  
-ATOM     42  CB  VAL A   7       4.785  25.419  10.482  1.00 20.04           C  
-ATOM     43  CG1 VAL A   7       4.853  24.954  11.941  1.00 19.25           C  
-ATOM     44  CG2 VAL A   7       5.299  24.267   9.599  1.00 18.69           C  
-ATOM     45  N   TYR A   8       1.962  26.601  12.077  1.00 15.58           N  
-ATOM     46  CA  TYR A   8       1.505  27.626  13.021  1.00 13.53           C  
-ATOM     47  C   TYR A   8       1.659  27.187  14.497  1.00 12.40           C  
-ATOM     48  O   TYR A   8       1.599  25.998  14.768  1.00 11.72           O  
-ATOM     49  CB  TYR A   8       0.037  28.109  12.734  1.00 14.19           C  
-ATOM     50  CG  TYR A   8      -0.899  26.921  12.746  1.00 17.84           C  
-ATOM     51  CD1 TYR A   8      -1.038  26.140  11.587  1.00 15.69           C  
-ATOM     52  CD2 TYR A   8      -1.552  26.551  13.940  1.00 13.52           C  
-ATOM     53  CE1 TYR A   8      -1.838  25.018  11.615  1.00 17.19           C  
-ATOM     54  CE2 TYR A   8      -2.329  25.401  13.974  1.00 15.16           C  
-ATOM     55  CZ  TYR A   8      -2.480  24.666  12.809  1.00 18.94           C  
-ATOM     56  OH  TYR A   8      -3.257  23.526  12.831  1.00 15.69           O  
-ATOM     57  N   GLY A   9       1.912  28.098  15.426  1.00 16.90           N  
-ATOM     58  CA  GLY A   9       2.011  27.921  16.872  1.00 15.19           C  
-ATOM     59  C   GLY A   9       0.780  28.739  17.373  1.00 11.98           C  
-ATOM     60  O   GLY A   9       0.754  29.978  17.241  1.00 12.11           O  
-ATOM     61  N   SER A  10      -0.218  28.088  17.971  1.00 12.52           N  
-ATOM     62  CA  SER A  10      -1.421  28.760  18.451  1.00 11.03           C  
-ATOM     63  C   SER A  10      -1.911  28.240  19.812  1.00 13.05           C  
-ATOM     64  O   SER A  10      -2.069  27.008  19.907  1.00 12.25           O  
-ATOM     65  CB  SER A  10      -2.546  28.545  17.413  1.00  8.91           C  
-ATOM     66  OG  SER A  10      -3.573  29.488  17.816  1.00 12.44           O  
-ATOM     67  N   THR A  11      -2.100  29.092  20.819  1.00 10.69           N  
-ATOM     68  CA  THR A  11      -2.516  28.615  22.175  1.00 13.49           C  
-ATOM     69  C   THR A  11      -4.035  28.687  22.294  1.00 15.49           C  
-ATOM     70  O   THR A  11      -4.661  27.704  22.709  1.00 14.52           O  
-ATOM     71  CB  THR A  11      -1.796  29.400  23.313  1.00 11.23           C  
-ATOM     72  OG1 THR A  11      -0.422  28.970  23.475  1.00 15.57           O  
-ATOM     73  CG2 THR A  11      -2.449  29.286  24.696  1.00 10.76           C  
-ATOM     74  N   THR A  12      -4.673  29.790  21.975  1.00 12.10           N  
-ATOM     75  CA  THR A  12      -6.107  30.003  22.035  1.00 14.58           C  
-ATOM     76  C   THR A  12      -6.804  29.834  20.677  1.00 18.17           C  
-ATOM     77  O   THR A  12      -8.027  30.065  20.669  1.00 14.81           O  
-ATOM     78  CB  THR A  12      -6.471  31.350  22.693  1.00 18.71           C  
-ATOM     79  OG1 THR A  12      -6.348  32.575  21.968  1.00 19.95           O  
-ATOM     80  CG2 THR A  12      -5.549  31.527  23.937  1.00 15.82           C  
-ATOM     81  N   GLY A  13      -6.059  29.496  19.623  1.00 15.79           N  
-ATOM     82  CA  GLY A  13      -6.595  29.288  18.285  1.00 16.70           C  
-ATOM     83  C   GLY A  13      -6.731  30.461  17.333  1.00 12.92           C  
-ATOM     84  O   GLY A  13      -7.347  30.362  16.278  1.00 16.25           O  
-ATOM     85  N   ASN A  14      -6.255  31.645  17.643  1.00  9.46           N  
-ATOM     86  CA  ASN A  14      -6.375  32.824  16.786  1.00 10.76           C  
-ATOM     87  C   ASN A  14      -5.373  32.666  15.627  1.00 15.27           C  
-ATOM     88  O   ASN A  14      -5.775  32.834  14.469  1.00 13.58           O  
-ATOM     89  CB  ASN A  14      -6.142  34.105  17.586  1.00  6.76           C  
-ATOM     90  CG  ASN A  14      -7.333  34.505  18.448  1.00 12.83           C  
-ATOM     91  OD1 ASN A  14      -8.481  34.077  18.273  1.00 14.95           O  
-ATOM     92  ND2 ASN A  14      -7.017  35.377  19.392  1.00 12.54           N  
-ATOM     93  N   THR A  15      -4.097  32.303  15.899  1.00 11.60           N  
-ATOM     94  CA  THR A  15      -3.118  32.107  14.855  1.00 12.36           C  
-ATOM     95  C   THR A  15      -3.499  30.857  14.056  1.00 16.94           C  
-ATOM     96  O   THR A  15      -3.234  30.774  12.856  1.00 16.04           O  
-ATOM     97  CB  THR A  15      -1.679  31.989  15.377  1.00 12.61           C  
-ATOM     98  OG1 THR A  15      -1.432  33.192  16.173  1.00 13.75           O  
-ATOM     99  CG2 THR A  15      -0.702  31.965  14.213  1.00  9.76           C  
-ATOM    100  N   GLU A  16      -4.156  29.882  14.676  1.00 10.45           N  
-ATOM    101  CA  GLU A  16      -4.578  28.727  13.891  1.00 11.69           C  
-ATOM    102  C   GLU A  16      -5.705  29.144  12.958  1.00 17.64           C  
-ATOM    103  O   GLU A  16      -5.715  28.677  11.812  1.00 15.38           O  
-ATOM    104  CB  GLU A  16      -5.042  27.644  14.840  1.00 13.44           C  
-ATOM    105  CG  GLU A  16      -5.678  26.512  14.009  1.00 14.94           C  
-ATOM    106  CD  GLU A  16      -6.129  25.393  14.940  1.00 21.72           C  
-ATOM    107  OE1 GLU A  16      -6.765  25.590  16.002  1.00 25.49           O  
-ATOM    108  OE2 GLU A  16      -5.840  24.255  14.542  1.00 24.71           O  
-ATOM    109  N   TYR A  17      -6.638  30.002  13.391  1.00 15.26           N  
-ATOM    110  CA  TYR A  17      -7.725  30.490  12.561  1.00 13.35           C  
-ATOM    111  C   TYR A  17      -7.053  31.320  11.452  1.00 16.52           C  
-ATOM    112  O   TYR A  17      -7.530  31.214  10.316  1.00 15.61           O  
-ATOM    113  CB  TYR A  17      -8.759  31.315  13.328  1.00  9.95           C  
-ATOM    114  CG  TYR A  17      -9.647  32.157  12.443  1.00 12.47           C  
-ATOM    115  CD1 TYR A  17      -9.264  33.402  11.959  1.00 12.59           C  
-ATOM    116  CD2 TYR A  17     -10.921  31.663  12.115  1.00 16.89           C  
-ATOM    117  CE1 TYR A  17     -10.096  34.146  11.109  1.00 13.54           C  
-ATOM    118  CE2 TYR A  17     -11.764  32.393  11.287  1.00 16.53           C  
-ATOM    119  CZ  TYR A  17     -11.341  33.616  10.792  1.00 18.78           C  
-ATOM    120  OH  TYR A  17     -12.217  34.335   9.988  1.00 23.85           O  
-ATOM    121  N   THR A  18      -6.033  32.119  11.657  1.00 16.52           N  
-ATOM    122  CA  THR A  18      -5.348  32.900  10.608  1.00 18.36           C  
-ATOM    123  C   THR A  18      -4.697  31.961   9.589  1.00 19.13           C  
-ATOM    124  O   THR A  18      -4.772  32.125   8.344  1.00 18.29           O  
-ATOM    125  CB  THR A  18      -4.281  33.806  11.241  1.00 16.65           C  
-ATOM    126  OG1 THR A  18      -5.006  34.616  12.216  1.00 14.28           O  
-ATOM    127  CG2 THR A  18      -3.611  34.773  10.279  1.00  9.00           C  
-ATOM    128  N   ALA A  19      -4.057  30.902  10.024  1.00 13.77           N  
-ATOM    129  CA  ALA A  19      -3.414  29.906   9.182  1.00 12.86           C  
-ATOM    130  C   ALA A  19      -4.454  29.246   8.285  1.00 14.93           C  
-ATOM    131  O   ALA A  19      -4.197  29.054   7.087  1.00 15.31           O  
-ATOM    132  CB  ALA A  19      -2.725  28.798  10.001  1.00 16.42           C  
-ATOM    133  N   GLU A  20      -5.619  28.882   8.803  1.00 14.68           N  
-ATOM    134  CA  GLU A  20      -6.673  28.255   7.992  1.00 16.24           C  
-ATOM    135  C   GLU A  20      -7.250  29.200   6.954  1.00 14.60           C  
-ATOM    136  O   GLU A  20      -7.663  28.774   5.869  1.00 16.44           O  
-ATOM    137  CB  GLU A  20      -7.844  27.808   8.851  1.00 20.51           C  
-ATOM    138  CG  GLU A  20      -7.447  26.686   9.820  1.00 23.16           C  
-ATOM    139  CD  GLU A  20      -8.473  26.532  10.945  1.00 31.50           C  
-ATOM    140  OE1 GLU A  20      -9.246  27.496  11.208  1.00 25.26           O  
-ATOM    141  OE2 GLU A  20      -8.464  25.422  11.556  1.00 28.73           O  
-ATOM    142  N   THR A  21      -7.347  30.482   7.237  1.00 13.35           N  
-ATOM    143  CA  THR A  21      -7.866  31.506   6.304  1.00 13.51           C  
-ATOM    144  C   THR A  21      -6.867  31.661   5.143  1.00 14.76           C  
-ATOM    145  O   THR A  21      -7.260  31.745   3.949  1.00 13.36           O  
-ATOM    146  CB  THR A  21      -8.098  32.838   7.058  1.00 16.95           C  
-ATOM    147  OG1 THR A  21      -9.164  32.659   7.987  1.00 12.29           O  
-ATOM    148  CG2 THR A  21      -8.454  33.999   6.134  1.00 16.82           C  
-ATOM    149  N   ILE A  22      -5.575  31.761   5.475  1.00  9.75           N  
-ATOM    150  CA  ILE A  22      -4.453  31.842   4.540  1.00 11.94           C  
-ATOM    151  C   ILE A  22      -4.420  30.532   3.730  1.00 12.87           C  
-ATOM    152  O   ILE A  22      -4.282  30.587   2.489  1.00 14.71           O  
-ATOM    153  CB  ILE A  22      -3.096  32.104   5.223  1.00  8.93           C  
-ATOM    154  CG1 ILE A  22      -3.009  33.518   5.844  1.00  8.35           C  
-ATOM    155  CG2 ILE A  22      -1.969  31.942   4.196  1.00 13.09           C  
-ATOM    156  CD1 ILE A  22      -1.759  33.541   6.764  1.00 10.01           C  
-ATOM    157  N   ALA A  23      -4.588  29.313   4.293  1.00 12.31           N  
-ATOM    158  CA  ALA A  23      -4.589  28.066   3.551  1.00 12.85           C  
-ATOM    159  C   ALA A  23      -5.700  28.027   2.472  1.00 17.41           C  
-ATOM    160  O   ALA A  23      -5.471  27.562   1.338  1.00 17.40           O  
-ATOM    161  CB  ALA A  23      -4.709  26.817   4.418  1.00  9.24           C  
-ATOM    162  N   ARG A  24      -6.894  28.466   2.793  1.00 13.94           N  
-ATOM    163  CA  ARG A  24      -8.017  28.506   1.844  1.00 15.64           C  
-ATOM    164  C   ARG A  24      -7.793  29.493   0.682  1.00 16.17           C  
-ATOM    165  O   ARG A  24      -8.140  29.145  -0.457  1.00 15.04           O  
-ATOM    166  CB  ARG A  24      -9.294  28.806   2.632  1.00 13.03           C  
-ATOM    167  CG  ARG A  24     -10.559  28.934   1.771  1.00 14.69           C  
-ATOM    168  CD  ARG A  24     -10.818  27.557   1.152  1.00 19.17           C  
-ATOM    169  NE  ARG A  24     -12.010  27.666   0.269  1.00 30.00           N  
-ATOM    170  CZ  ARG A  24     -13.256  27.480   0.732  1.00 37.44           C  
-ATOM    171  NH1 ARG A  24     -13.562  27.202   2.012  1.00 28.41           N  
-ATOM    172  NH2 ARG A  24     -14.265  27.578  -0.140  1.00 34.34           N  
-ATOM    173  N   GLU A  25      -7.267  30.693   0.935  1.00 15.12           N  
-ATOM    174  CA  GLU A  25      -6.957  31.687  -0.081  1.00 17.82           C  
-ATOM    175  C   GLU A  25      -5.980  31.096  -1.110  1.00 20.59           C  
-ATOM    176  O   GLU A  25      -6.160  31.120  -2.345  1.00 17.50           O  
-ATOM    177  CB  GLU A  25      -6.345  32.962   0.544  1.00 14.67           C  
-ATOM    178  CG  GLU A  25      -7.411  33.801   1.261  1.00 31.97           C  
-ATOM    179  CD  GLU A  25      -8.603  34.134   0.348  1.00 40.34           C  
-ATOM    180  OE1 GLU A  25      -8.402  34.852  -0.654  1.00 40.08           O  
-ATOM    181  OE2 GLU A  25      -9.757  33.695   0.598  1.00 31.32           O  
-ATOM    182  N   LEU A  26      -4.897  30.457  -0.647  1.00 18.00           N  
-ATOM    183  CA  LEU A  26      -3.875  29.797  -1.442  1.00 19.24           C  
-ATOM    184  C   LEU A  26      -4.442  28.605  -2.213  1.00 20.77           C  
-ATOM    185  O   LEU A  26      -4.060  28.504  -3.406  1.00 17.21           O  
-ATOM    186  CB  LEU A  26      -2.678  29.326  -0.588  1.00 15.99           C  
-ATOM    187  CG  LEU A  26      -1.482  30.262  -0.466  1.00 18.33           C  
-ATOM    188  CD1 LEU A  26      -1.761  31.731  -0.604  1.00 13.22           C  
-ATOM    189  CD2 LEU A  26      -0.659  29.984   0.800  1.00 18.93           C  
-ATOM    190  N   ALA A  27      -5.283  27.770  -1.619  1.00 18.17           N  
-ATOM    191  CA  ALA A  27      -5.889  26.618  -2.282  1.00 14.11           C  
-ATOM    192  C   ALA A  27      -6.902  27.033  -3.357  1.00 17.59           C  
-ATOM    193  O   ALA A  27      -7.021  26.405  -4.438  1.00 16.28           O  
-ATOM    194  CB  ALA A  27      -6.553  25.760  -1.227  1.00 12.35           C  
-ATOM    195  N   ASP A  28      -7.621  28.133  -3.116  1.00 18.60           N  
-ATOM    196  CA  ASP A  28      -8.616  28.686  -4.036  1.00 17.48           C  
-ATOM    197  C   ASP A  28      -7.934  29.214  -5.307  1.00 19.09           C  
-ATOM    198  O   ASP A  28      -8.562  29.299  -6.393  1.00 15.92           O  
-ATOM    199  CB  ASP A  28      -9.408  29.852  -3.435  1.00 13.13           C  
-ATOM    200  CG  ASP A  28     -10.489  29.364  -2.503  1.00 20.17           C  
-ATOM    201  OD1 ASP A  28     -10.861  28.162  -2.432  1.00 18.19           O  
-ATOM    202  OD2 ASP A  28     -10.960  30.271  -1.785  1.00 18.72           O  
-ATOM    203  N   ALA A  29      -6.672  29.612  -5.170  1.00 13.37           N  
-ATOM    204  CA  ALA A  29      -5.950  30.100  -6.341  1.00 17.10           C  
-ATOM    205  C   ALA A  29      -5.215  28.981  -7.098  1.00 17.12           C  
-ATOM    206  O   ALA A  29      -4.522  29.302  -8.088  1.00 19.58           O  
-ATOM    207  CB  ALA A  29      -4.974  31.216  -5.963  1.00 17.66           C  
-ATOM    208  N   GLY A  30      -5.313  27.711  -6.679  1.00 13.63           N  
-ATOM    209  CA  GLY A  30      -4.651  26.583  -7.296  1.00 12.99           C  
-ATOM    210  C   GLY A  30      -3.343  26.147  -6.636  1.00 18.66           C  
-ATOM    211  O   GLY A  30      -2.705  25.186  -7.138  1.00 16.21           O  
-ATOM    212  N   TYR A  31      -2.852  26.788  -5.535  1.00 13.95           N  
-ATOM    213  CA  TYR A  31      -1.623  26.258  -4.949  1.00 15.44           C  
-ATOM    214  C   TYR A  31      -1.923  24.902  -4.262  1.00 15.75           C  
-ATOM    215  O   TYR A  31      -3.034  24.501  -3.900  1.00 16.03           O  
-ATOM    216  CB  TYR A  31      -1.140  27.074  -3.747  1.00 13.84           C  
-ATOM    217  CG  TYR A  31      -0.310  28.268  -4.096  1.00 18.02           C  
-ATOM    218  CD1 TYR A  31      -0.610  29.175  -5.105  1.00 15.31           C  
-ATOM    219  CD2 TYR A  31       0.845  28.460  -3.332  1.00 19.74           C  
-ATOM    220  CE1 TYR A  31       0.195  30.257  -5.350  1.00 13.81           C  
-ATOM    221  CE2 TYR A  31       1.669  29.533  -3.591  1.00 22.10           C  
-ATOM    222  CZ  TYR A  31       1.338  30.432  -4.584  1.00 20.58           C  
-ATOM    223  OH  TYR A  31       2.214  31.475  -4.765  1.00 21.31           O  
-ATOM    224  N   GLU A  32      -0.866  24.142  -4.097  1.00 15.38           N  
-ATOM    225  CA  GLU A  32      -0.842  22.868  -3.358  1.00 16.55           C  
-ATOM    226  C   GLU A  32      -0.424  23.356  -1.935  1.00 17.75           C  
-ATOM    227  O   GLU A  32       0.533  24.145  -1.749  1.00 16.09           O  
-ATOM    228  CB  GLU A  32       0.162  21.974  -4.026  1.00 24.79           C  
-ATOM    229  CG  GLU A  32      -0.073  20.580  -3.456  1.00 44.47           C  
-ATOM    230  CD  GLU A  32       1.077  19.684  -3.931  1.00 53.03           C  
-ATOM    231  OE1 GLU A  32       1.374  19.888  -5.139  1.00 43.90           O  
-ATOM    232  OE2 GLU A  32       1.543  18.925  -3.040  1.00 56.05           O  
-ATOM    233  N   VAL A  33      -1.227  23.083  -0.932  1.00 18.98           N  
-ATOM    234  CA  VAL A  33      -1.069  23.549   0.458  1.00 20.18           C  
-ATOM    235  C   VAL A  33      -1.022  22.461   1.541  1.00 23.43           C  
-ATOM    236  O   VAL A  33      -1.917  21.636   1.775  1.00 22.84           O  
-ATOM    237  CB  VAL A  33      -2.265  24.483   0.811  1.00 20.59           C  
-ATOM    238  CG1 VAL A  33      -2.132  25.104   2.229  1.00 20.63           C  
-ATOM    239  CG2 VAL A  33      -2.401  25.628  -0.203  1.00 19.39           C  
-ATOM    240  N   ASP A  34       0.077  22.470   2.297  1.00 21.83           N  
-ATOM    241  CA  ASP A  34       0.346  21.561   3.434  1.00 20.47           C  
-ATOM    242  C   ASP A  34       0.342  22.425   4.732  1.00 20.29           C  
-ATOM    243  O   ASP A  34       1.289  23.207   4.937  1.00 17.65           O  
-ATOM    244  CB  ASP A  34       1.697  20.926   3.069  1.00 20.51           C  
-ATOM    245  CG  ASP A  34       2.079  19.725   3.890  1.00 33.18           C  
-ATOM    246  OD1 ASP A  34       1.692  19.649   5.094  1.00 29.64           O  
-ATOM    247  OD2 ASP A  34       2.785  18.839   3.352  1.00 33.32           O  
-ATOM    248  N   SER A  35      -0.694  22.310   5.583  1.00 15.04           N  
-ATOM    249  CA  SER A  35      -0.817  23.142   6.805  1.00 20.09           C  
-ATOM    250  C   SER A  35      -0.580  22.291   8.042  1.00 23.49           C  
-ATOM    251  O   SER A  35      -1.232  21.265   8.251  1.00 25.37           O  
-ATOM    252  CB  SER A  35      -2.153  23.892   6.665  1.00 20.07           C  
-ATOM    253  OG  SER A  35      -2.306  24.884   7.679  1.00 38.07           O  
-ATOM    254  N   ARG A  36       0.408  22.594   8.891  1.00 17.84           N  
-ATOM    255  CA  ARG A  36       0.786  21.810  10.056  1.00 21.82           C  
-ATOM    256  C   ARG A  36       0.921  22.599  11.367  1.00 16.31           C  
-ATOM    257  O   ARG A  36       1.405  23.713  11.372  1.00 17.04           O  
-ATOM    258  CB  ARG A  36       2.183  21.122   9.848  1.00 18.83           C  
-ATOM    259  CG  ARG A  36       2.229  20.230   8.594  1.00 17.28           C  
-ATOM    260  CD  ARG A  36       3.541  19.447   8.476  1.00 22.69           C  
-ATOM    261  NE  ARG A  36       3.805  19.023   7.095  1.00 27.07           N  
-ATOM    262  CZ  ARG A  36       4.947  18.660   6.525  1.00 26.45           C  
-ATOM    263  NH1 ARG A  36       6.048  18.636   7.268  1.00 24.27           N  
-ATOM    264  NH2 ARG A  36       5.031  18.345   5.231  1.00 22.36           N  
-ATOM    265  N   ASP A  37       0.396  22.014  12.432  1.00 19.89           N  
-ATOM    266  CA  ASP A  37       0.512  22.638  13.762  1.00 15.41           C  
-ATOM    267  C   ASP A  37       1.982  22.489  14.165  1.00 13.96           C  
-ATOM    268  O   ASP A  37       2.544  21.371  14.063  1.00 14.99           O  
-ATOM    269  CB  ASP A  37      -0.443  21.887  14.723  1.00 19.84           C  
-ATOM    270  CG  ASP A  37      -0.594  22.541  16.094  1.00 22.44           C  
-ATOM    271  OD1 ASP A  37       0.409  23.023  16.676  1.00 18.85           O  
-ATOM    272  OD2 ASP A  37      -1.733  22.686  16.610  1.00 21.31           O  
-ATOM    273  N   ALA A  38       2.673  23.517  14.679  1.00 13.11           N  
-ATOM    274  CA  ALA A  38       4.075  23.428  15.088  1.00 17.09           C  
-ATOM    275  C   ALA A  38       4.323  22.315  16.115  1.00 21.37           C  
-ATOM    276  O   ALA A  38       5.451  21.826  16.310  1.00 20.37           O  
-ATOM    277  CB  ALA A  38       4.522  24.739  15.740  1.00 14.89           C  
-ATOM    278  N   ALA A  39       3.288  21.905  16.838  1.00 20.66           N  
-ATOM    279  CA  ALA A  39       3.334  20.860  17.860  1.00 22.28           C  
-ATOM    280  C   ALA A  39       3.599  19.491  17.270  1.00 23.93           C  
-ATOM    281  O   ALA A  39       4.193  18.646  17.939  1.00 25.87           O  
-ATOM    282  CB  ALA A  39       2.005  20.787  18.628  1.00 19.91           C  
-ATOM    283  N   SER A  40       3.233  19.233  16.041  1.00 27.70           N  
-ATOM    284  CA  SER A  40       3.409  17.988  15.323  1.00 34.57           C  
-ATOM    285  C   SER A  40       4.604  17.889  14.368  1.00 37.29           C  
-ATOM    286  O   SER A  40       4.776  16.873  13.669  1.00 36.97           O  
-ATOM    287  CB  SER A  40       2.189  17.874  14.343  1.00 40.59           C  
-ATOM    288  OG  SER A  40       2.249  18.806  13.250  1.00 31.56           O  
-ATOM    289  N   VAL A  41       5.396  18.941  14.287  1.00 35.13           N  
-ATOM    290  CA  VAL A  41       6.490  19.094  13.338  1.00 32.06           C  
-ATOM    291  C   VAL A  41       7.879  18.803  13.843  1.00 35.77           C  
-ATOM    292  O   VAL A  41       8.197  19.001  15.024  1.00 29.31           O  
-ATOM    293  CB  VAL A  41       6.213  20.575  12.872  1.00 28.90           C  
-ATOM    294  CG1 VAL A  41       7.292  21.600  13.135  1.00 25.25           C  
-ATOM    295  CG2 VAL A  41       5.625  20.630  11.493  1.00 25.65           C  
-ATOM    296  N   GLU A  42       8.728  18.297  12.933  1.00 35.73           N  
-ATOM    297  CA  GLU A  42      10.139  18.030  13.211  1.00 37.92           C  
-ATOM    298  C   GLU A  42      10.903  19.050  12.345  1.00 36.58           C  
-ATOM    299  O   GLU A  42      10.612  19.185  11.147  1.00 37.84           O  
-ATOM    300  CB  GLU A  42      10.627  16.629  12.942  1.00 53.16           C  
-ATOM    301  CG  GLU A  42      10.097  15.576  13.886  1.00 72.84           C  
-ATOM    302  CD  GLU A  42      10.430  15.599  15.358  1.00 81.89           C  
-ATOM    303  OE1 GLU A  42      10.532  16.570  16.146  1.00 78.85           O  
-ATOM    304  OE2 GLU A  42      10.601  14.433  15.820  1.00 90.07           O  
-ATOM    305  N   ALA A  43      11.836  19.780  12.955  1.00 33.19           N  
-ATOM    306  CA  ALA A  43      12.554  20.797  12.204  1.00 32.24           C  
-ATOM    307  C   ALA A  43      13.415  20.202  11.095  1.00 32.04           C  
-ATOM    308  O   ALA A  43      13.455  20.827  10.034  1.00 31.44           O  
-ATOM    309  CB  ALA A  43      13.393  21.719  13.085  1.00 18.78           C  
-ATOM    310  N   GLY A  44      14.077  19.080  11.304  1.00 30.86           N  
-ATOM    311  CA  GLY A  44      14.974  18.439  10.361  1.00 32.46           C  
-ATOM    312  C   GLY A  44      14.526  18.381   8.926  1.00 28.09           C  
-ATOM    313  O   GLY A  44      13.653  17.572   8.595  1.00 31.87           O  
-ATOM    314  N   GLY A  45      15.095  19.228   8.075  1.00 31.03           N  
-ATOM    315  CA  GLY A  45      14.757  19.350   6.650  1.00 29.84           C  
-ATOM    316  C   GLY A  45      13.271  19.674   6.429  1.00 26.17           C  
-ATOM    317  O   GLY A  45      12.699  19.422   5.346  1.00 25.38           O  
-ATOM    318  N   LEU A  46      12.575  20.279   7.379  1.00 20.48           N  
-ATOM    319  CA  LEU A  46      11.147  20.560   7.220  1.00 21.21           C  
-ATOM    320  C   LEU A  46      10.694  21.315   5.967  1.00 21.53           C  
-ATOM    321  O   LEU A  46       9.584  21.018   5.457  1.00 20.34           O  
-ATOM    322  CB  LEU A  46      10.719  21.296   8.503  1.00 18.13           C  
-ATOM    323  CG  LEU A  46       9.253  21.661   8.706  1.00 18.59           C  
-ATOM    324  CD1 LEU A  46       8.347  20.453   8.745  1.00 18.56           C  
-ATOM    325  CD2 LEU A  46       9.206  22.512   9.967  1.00 22.50           C  
-ATOM    326  N   PHE A  47      11.464  22.307   5.504  1.00 17.30           N  
-ATOM    327  CA  PHE A  47      11.092  23.127   4.379  1.00 20.87           C  
-ATOM    328  C   PHE A  47      11.467  22.532   3.026  1.00 22.09           C  
-ATOM    329  O   PHE A  47      11.211  23.161   2.002  1.00 23.16           O  
-ATOM    330  CB  PHE A  47      11.743  24.518   4.489  1.00 18.94           C  
-ATOM    331  CG  PHE A  47      11.508  25.276   5.771  1.00 14.91           C  
-ATOM    332  CD1 PHE A  47      10.511  24.918   6.664  1.00 14.35           C  
-ATOM    333  CD2 PHE A  47      12.275  26.405   6.034  1.00 17.38           C  
-ATOM    334  CE1 PHE A  47      10.312  25.643   7.820  1.00 20.19           C  
-ATOM    335  CE2 PHE A  47      12.054  27.147   7.180  1.00 22.76           C  
-ATOM    336  CZ  PHE A  47      11.068  26.774   8.103  1.00 13.24           C  
-ATOM    337  N   GLU A  48      12.098  21.370   3.074  1.00 22.15           N  
-ATOM    338  CA  GLU A  48      12.539  20.722   1.839  1.00 26.56           C  
-ATOM    339  C   GLU A  48      11.322  20.351   0.988  1.00 25.47           C  
-ATOM    340  O   GLU A  48      10.286  19.843   1.406  1.00 22.04           O  
-ATOM    341  CB  GLU A  48      13.539  19.581   2.059  1.00 23.91           C  
-ATOM    342  CG  GLU A  48      14.929  20.153   2.317  1.00 35.14           C  
-ATOM    343  CD  GLU A  48      15.990  19.313   3.015  1.00 42.27           C  
-ATOM    344  OE1 GLU A  48      15.716  18.097   3.203  1.00 39.14           O  
-ATOM    345  OE2 GLU A  48      17.066  19.901   3.376  1.00 42.12           O  
-ATOM    346  N   GLY A  49      11.495  20.716  -0.285  1.00 25.45           N  
-ATOM    347  CA  GLY A  49      10.513  20.501  -1.335  1.00 23.62           C  
-ATOM    348  C   GLY A  49       9.437  21.568  -1.384  1.00 24.99           C  
-ATOM    349  O   GLY A  49       8.511  21.292  -2.153  1.00 24.44           O  
-ATOM    350  N   PHE A  50       9.501  22.689  -0.655  1.00 25.43           N  
-ATOM    351  CA  PHE A  50       8.453  23.702  -0.688  1.00 21.48           C  
-ATOM    352  C   PHE A  50       8.862  24.958  -1.437  1.00 19.39           C  
-ATOM    353  O   PHE A  50       9.998  25.434  -1.258  1.00 16.71           O  
-ATOM    354  CB  PHE A  50       7.987  24.064   0.752  1.00 14.07           C  
-ATOM    355  CG  PHE A  50       7.178  22.946   1.322  1.00 14.11           C  
-ATOM    356  CD1 PHE A  50       5.841  22.764   0.952  1.00 12.30           C  
-ATOM    357  CD2 PHE A  50       7.768  22.068   2.227  1.00 17.88           C  
-ATOM    358  CE1 PHE A  50       5.162  21.674   1.481  1.00 16.02           C  
-ATOM    359  CE2 PHE A  50       7.068  21.002   2.768  1.00 16.62           C  
-ATOM    360  CZ  PHE A  50       5.745  20.794   2.389  1.00 14.57           C  
-ATOM    361  N   ASP A  51       7.936  25.527  -2.245  1.00 15.85           N  
-ATOM    362  CA  ASP A  51       8.250  26.748  -2.975  1.00 14.31           C  
-ATOM    363  C   ASP A  51       8.098  27.983  -2.084  1.00 14.20           C  
-ATOM    364  O   ASP A  51       8.738  29.025  -2.258  1.00 14.68           O  
-ATOM    365  CB  ASP A  51       7.340  26.938  -4.232  1.00 16.19           C  
-ATOM    366  CG  ASP A  51       7.509  25.751  -5.175  1.00 23.17           C  
-ATOM    367  OD1 ASP A  51       8.637  25.470  -5.695  1.00 22.25           O  
-ATOM    368  OD2 ASP A  51       6.521  25.017  -5.395  1.00 18.40           O  
-ATOM    369  N   LEU A  52       7.168  27.829  -1.138  1.00 14.83           N  
-ATOM    370  CA  LEU A  52       6.883  28.904  -0.211  1.00 15.68           C  
-ATOM    371  C   LEU A  52       6.598  28.253   1.169  1.00 14.61           C  
-ATOM    372  O   LEU A  52       5.938  27.225   1.268  1.00 16.58           O  
-ATOM    373  CB  LEU A  52       5.573  29.572  -0.613  1.00 15.18           C  
-ATOM    374  CG  LEU A  52       5.180  31.006  -0.384  1.00 20.01           C  
-ATOM    375  CD1 LEU A  52       3.709  31.109  -0.014  1.00 18.94           C  
-ATOM    376  CD2 LEU A  52       6.056  31.892   0.456  1.00 12.50           C  
-ATOM    377  N   VAL A  53       7.107  28.905   2.206  1.00 17.35           N  
-ATOM    378  CA  VAL A  53       6.907  28.446   3.601  1.00 15.40           C  
-ATOM    379  C   VAL A  53       6.394  29.655   4.387  1.00 15.62           C  
-ATOM    380  O   VAL A  53       7.004  30.761   4.366  1.00 13.34           O  
-ATOM    381  CB  VAL A  53       8.183  27.826   4.214  1.00 23.32           C  
-ATOM    382  CG1 VAL A  53       7.932  27.528   5.695  1.00 13.20           C  
-ATOM    383  CG2 VAL A  53       8.683  26.546   3.521  1.00 15.35           C  
-ATOM    384  N   LEU A  54       5.215  29.518   5.046  1.00 14.79           N  
-ATOM    385  CA  LEU A  54       4.563  30.564   5.840  1.00 13.31           C  
-ATOM    386  C   LEU A  54       4.544  30.086   7.304  1.00 13.16           C  
-ATOM    387  O   LEU A  54       4.076  28.995   7.665  1.00 14.81           O  
-ATOM    388  CB  LEU A  54       3.156  30.837   5.312  1.00 11.37           C  
-ATOM    389  CG  LEU A  54       3.092  31.333   3.846  1.00  9.35           C  
-ATOM    390  CD1 LEU A  54       1.583  31.558   3.544  1.00 11.84           C  
-ATOM    391  CD2 LEU A  54       3.866  32.593   3.594  1.00  8.10           C  
-ATOM    392  N   LEU A  55       5.124  30.909   8.169  1.00 13.84           N  
-ATOM    393  CA  LEU A  55       5.269  30.591   9.612  1.00 12.59           C  
-ATOM    394  C   LEU A  55       4.423  31.531  10.432  1.00  9.02           C  
-ATOM    395  O   LEU A  55       4.571  32.775  10.349  1.00 12.02           O  
-ATOM    396  CB  LEU A  55       6.777  30.740   9.924  1.00 13.75           C  
-ATOM    397  CG  LEU A  55       7.717  29.567   9.934  1.00 21.66           C  
-ATOM    398  CD1 LEU A  55       7.364  28.301   9.170  1.00 15.65           C  
-ATOM    399  CD2 LEU A  55       9.170  29.960   9.647  1.00 24.30           C  
-ATOM    400  N   GLY A  56       3.550  30.895  11.229  1.00 13.06           N  
-ATOM    401  CA  GLY A  56       2.626  31.648  12.071  1.00  9.14           C  
-ATOM    402  C   GLY A  56       2.910  31.459  13.571  1.00 11.51           C  
-ATOM    403  O   GLY A  56       3.126  30.318  13.950  1.00 11.18           O  
-ATOM    404  N   CYS A  57       2.922  32.527  14.339  1.00 12.33           N  
-ATOM    405  CA  CYS A  57       3.219  32.456  15.790  1.00 13.79           C  
-ATOM    406  C   CYS A  57       2.704  33.644  16.574  1.00  8.84           C  
-ATOM    407  O   CYS A  57       2.904  34.844  16.274  1.00 12.01           O  
-ATOM    408  CB  CYS A  57       4.779  32.309  15.926  1.00 11.36           C  
-ATOM    409  SG  CYS A  57       5.223  31.892  17.667  1.00 13.50           S  
-ATOM    410  N   SER A  58       1.972  33.354  17.687  1.00 14.10           N  
-ATOM    411  CA  SER A  58       1.464  34.393  18.632  1.00 13.40           C  
-ATOM    412  C   SER A  58       2.571  34.775  19.642  1.00 11.75           C  
-ATOM    413  O   SER A  58       3.548  34.039  19.843  1.00 11.33           O  
-ATOM    414  CB  SER A  58       0.153  34.010  19.361  1.00  7.32           C  
-ATOM    415  OG  SER A  58       0.305  32.720  19.999  1.00 12.04           O  
-ATOM    416  N   THR A  59       2.493  35.955  20.268  1.00  9.84           N  
-ATOM    417  CA  THR A  59       3.436  36.551  21.192  1.00 12.32           C  
-ATOM    418  C   THR A  59       2.849  36.495  22.639  1.00 17.25           C  
-ATOM    419  O   THR A  59       1.651  36.653  22.922  1.00  8.12           O  
-ATOM    420  CB  THR A  59       3.687  38.028  20.837  1.00 11.89           C  
-ATOM    421  OG1 THR A  59       4.130  37.977  19.454  1.00 16.76           O  
-ATOM    422  CG2 THR A  59       4.803  38.634  21.686  1.00 11.72           C  
-ATOM    423  N   TRP A  60       3.725  36.117  23.558  1.00 14.15           N  
-ATOM    424  CA  TRP A  60       3.482  35.864  24.979  1.00 16.76           C  
-ATOM    425  C   TRP A  60       4.508  36.583  25.853  1.00 17.90           C  
-ATOM    426  O   TRP A  60       5.415  37.257  25.329  1.00 13.29           O  
-ATOM    427  CB  TRP A  60       3.462  34.296  25.204  1.00  7.81           C  
-ATOM    428  CG  TRP A  60       2.269  33.701  24.512  1.00 11.61           C  
-ATOM    429  CD1 TRP A  60       2.290  33.200  23.216  1.00 11.27           C  
-ATOM    430  CD2 TRP A  60       0.899  33.675  24.926  1.00 14.30           C  
-ATOM    431  NE1 TRP A  60       1.030  32.866  22.821  1.00 12.24           N  
-ATOM    432  CE2 TRP A  60       0.144  33.133  23.868  1.00 13.78           C  
-ATOM    433  CE3 TRP A  60       0.244  34.070  26.113  1.00  9.37           C  
-ATOM    434  CZ2 TRP A  60      -1.223  32.932  23.934  1.00 11.49           C  
-ATOM    435  CZ3 TRP A  60      -1.129  33.863  26.189  1.00  9.00           C  
-ATOM    436  CH2 TRP A  60      -1.869  33.315  25.101  1.00 14.29           C  
-ATOM    437  N   GLY A  61       4.388  36.455  27.193  1.00 14.79           N  
-ATOM    438  CA  GLY A  61       5.384  37.158  28.006  1.00 14.60           C  
-ATOM    439  C   GLY A  61       4.779  38.509  28.371  1.00 20.72           C  
-ATOM    440  O   GLY A  61       3.828  39.132  27.912  1.00 19.15           O  
-ATOM    441  N   ASP A  62       5.454  39.045  29.391  1.00 25.06           N  
-ATOM    442  CA  ASP A  62       5.038  40.362  29.884  1.00 23.96           C  
-ATOM    443  C   ASP A  62       6.085  41.370  29.466  1.00 28.48           C  
-ATOM    444  O   ASP A  62       7.069  41.675  30.168  1.00 26.17           O  
-ATOM    445  CB  ASP A  62       4.879  40.261  31.381  1.00 35.60           C  
-ATOM    446  CG  ASP A  62       4.371  41.563  31.988  1.00 42.07           C  
-ATOM    447  OD1 ASP A  62       3.816  42.426  31.262  1.00 46.07           O  
-ATOM    448  OD2 ASP A  62       4.585  41.605  33.223  1.00 42.46           O  
-ATOM    449  N   ASP A  63       5.915  41.872  28.243  1.00 36.06           N  
-ATOM    450  CA  ASP A  63       6.854  42.842  27.632  1.00 42.24           C  
-ATOM    451  C   ASP A  63       8.315  42.390  27.876  1.00 43.27           C  
-ATOM    452  O   ASP A  63       9.305  42.910  28.408  1.00 40.47           O  
-ATOM    453  CB  ASP A  63       6.503  44.261  28.037  1.00 52.78           C  
-ATOM    454  CG  ASP A  63       5.166  44.956  27.956  1.00 58.52           C  
-ATOM    455  OD1 ASP A  63       4.213  44.648  27.193  1.00 57.34           O  
-ATOM    456  OD2 ASP A  63       5.036  45.958  28.748  1.00 62.32           O  
-ATOM    457  N   SER A  64       8.555  41.161  27.424  1.00 40.36           N  
-ATOM    458  CA  SER A  64       9.701  40.284  27.394  1.00 33.69           C  
-ATOM    459  C   SER A  64       9.148  39.188  26.440  1.00 33.26           C  
-ATOM    460  O   SER A  64       8.459  38.291  26.928  1.00 33.77           O  
-ATOM    461  CB  SER A  64      10.089  39.765  28.740  1.00 18.25           C  
-ATOM    462  OG  SER A  64      11.321  39.104  28.662  1.00 23.38           O  
-ATOM    463  N   ILE A  65       9.425  39.436  25.162  1.00 31.28           N  
-ATOM    464  CA  ILE A  65       8.887  38.546  24.136  1.00 30.91           C  
-ATOM    465  C   ILE A  65       9.182  37.082  24.437  1.00 26.51           C  
-ATOM    466  O   ILE A  65      10.287  36.646  24.712  1.00 26.14           O  
-ATOM    467  CB  ILE A  65       9.362  38.890  22.709  1.00 23.55           C  
-ATOM    468  CG1 ILE A  65       8.837  40.255  22.239  1.00 20.55           C  
-ATOM    469  CG2 ILE A  65       8.982  37.855  21.648  1.00 25.67           C  
-ATOM    470  CD1 ILE A  65       9.792  40.769  21.179  1.00 16.61           C  
-ATOM    471  N   GLU A  66       8.137  36.290  24.387  1.00 22.86           N  
-ATOM    472  CA  GLU A  66       8.204  34.830  24.568  1.00 22.81           C  
-ATOM    473  C   GLU A  66       7.415  34.278  23.334  1.00 20.55           C  
-ATOM    474  O   GLU A  66       6.339  34.806  23.021  1.00 19.69           O  
-ATOM    475  CB  GLU A  66       7.606  34.343  25.882  1.00 26.32           C  
-ATOM    476  CG  GLU A  66       8.359  33.921  27.113  1.00 48.80           C  
-ATOM    477  CD  GLU A  66       7.938  34.494  28.458  1.00 49.68           C  
-ATOM    478  OE1 GLU A  66       6.969  33.956  29.038  1.00 45.93           O  
-ATOM    479  OE2 GLU A  66       8.544  35.465  29.011  1.00 51.18           O  
-ATOM    480  N   LEU A  67       7.882  33.267  22.621  1.00 20.75           N  
-ATOM    481  CA  LEU A  67       7.142  32.676  21.500  1.00 18.92           C  
-ATOM    482  C   LEU A  67       6.078  31.696  21.988  1.00 18.54           C  
-ATOM    483  O   LEU A  67       6.221  31.155  23.100  1.00 16.14           O  
-ATOM    484  CB  LEU A  67       8.147  31.940  20.601  1.00 17.09           C  
-ATOM    485  CG  LEU A  67       8.814  32.719  19.468  1.00 21.10           C  
-ATOM    486  CD1 LEU A  67       9.295  34.123  19.829  1.00 17.74           C  
-ATOM    487  CD2 LEU A  67       9.896  31.813  18.865  1.00 20.43           C  
-ATOM    488  N   GLN A  68       5.001  31.476  21.238  1.00 16.75           N  
-ATOM    489  CA  GLN A  68       3.957  30.513  21.567  1.00 16.66           C  
-ATOM    490  C   GLN A  68       4.668  29.169  21.841  1.00 15.62           C  
-ATOM    491  O   GLN A  68       5.621  28.779  21.154  1.00 13.40           O  
-ATOM    492  CB  GLN A  68       2.896  30.430  20.485  1.00 13.61           C  
-ATOM    493  CG  GLN A  68       1.679  29.590  20.685  1.00  9.15           C  
-ATOM    494  CD  GLN A  68       1.776  28.096  20.646  1.00  9.24           C  
-ATOM    495  OE1 GLN A  68       1.033  27.304  21.321  1.00 13.20           O  
-ATOM    496  NE2 GLN A  68       2.658  27.611  19.808  1.00 10.14           N  
-ATOM    497  N   ASP A  69       4.226  28.500  22.919  1.00 13.63           N  
-ATOM    498  CA  ASP A  69       4.802  27.268  23.444  1.00 13.80           C  
-ATOM    499  C   ASP A  69       5.214  26.169  22.493  1.00 15.87           C  
-ATOM    500  O   ASP A  69       6.350  25.624  22.542  1.00 14.61           O  
-ATOM    501  CB  ASP A  69       3.876  26.719  24.569  1.00 10.81           C  
-ATOM    502  CG  ASP A  69       4.515  25.597  25.331  1.00 15.81           C  
-ATOM    503  OD1 ASP A  69       5.534  25.801  26.007  1.00 20.85           O  
-ATOM    504  OD2 ASP A  69       4.056  24.460  25.187  1.00 19.51           O  
-ATOM    505  N   ASP A  70       4.323  25.786  21.596  1.00 15.64           N  
-ATOM    506  CA  ASP A  70       4.545  24.762  20.595  1.00 13.07           C  
-ATOM    507  C   ASP A  70       5.532  25.233  19.540  1.00 13.90           C  
-ATOM    508  O   ASP A  70       6.164  24.323  18.982  1.00 19.31           O  
-ATOM    509  CB  ASP A  70       3.207  24.462  19.934  1.00 14.93           C  
-ATOM    510  CG  ASP A  70       2.148  23.933  20.858  1.00 16.36           C  
-ATOM    511  OD1 ASP A  70       2.453  22.978  21.604  1.00 20.35           O  
-ATOM    512  OD2 ASP A  70       0.964  24.310  20.874  1.00 17.12           O  
-ATOM    513  N   PHE A  71       5.663  26.530  19.270  1.00 13.62           N  
-ATOM    514  CA  PHE A  71       6.597  26.991  18.254  1.00 11.23           C  
-ATOM    515  C   PHE A  71       8.037  27.049  18.708  1.00 17.56           C  
-ATOM    516  O   PHE A  71       9.024  27.007  17.942  1.00 14.15           O  
-ATOM    517  CB  PHE A  71       6.126  28.407  17.875  1.00 10.88           C  
-ATOM    518  CG  PHE A  71       6.561  28.698  16.460  1.00 15.05           C  
-ATOM    519  CD1 PHE A  71       7.803  29.240  16.206  1.00 18.27           C  
-ATOM    520  CD2 PHE A  71       5.705  28.368  15.406  1.00 13.16           C  
-ATOM    521  CE1 PHE A  71       8.256  29.492  14.910  1.00 17.01           C  
-ATOM    522  CE2 PHE A  71       6.145  28.629  14.116  1.00 17.57           C  
-ATOM    523  CZ  PHE A  71       7.402  29.186  13.866  1.00 13.24           C  
-ATOM    524  N   ILE A  72       8.279  27.153  20.038  1.00 18.59           N  
-ATOM    525  CA  ILE A  72       9.639  27.260  20.580  1.00 16.77           C  
-ATOM    526  C   ILE A  72      10.637  26.265  20.054  1.00 18.35           C  
-ATOM    527  O   ILE A  72      11.720  26.654  19.552  1.00 19.43           O  
-ATOM    528  CB  ILE A  72       9.647  27.366  22.125  1.00 19.65           C  
-ATOM    529  CG1 ILE A  72       8.989  28.668  22.552  1.00 15.33           C  
-ATOM    530  CG2 ILE A  72      11.057  27.324  22.737  1.00 18.74           C  
-ATOM    531  CD1 ILE A  72       8.658  28.632  24.063  1.00 14.68           C  
-ATOM    532  N   PRO A  73      10.401  24.960  20.109  1.00 20.08           N  
-ATOM    533  CA  PRO A  73      11.283  23.915  19.590  1.00 21.89           C  
-ATOM    534  C   PRO A  73      11.678  24.121  18.118  1.00 22.99           C  
-ATOM    535  O   PRO A  73      12.873  23.993  17.762  1.00 16.25           O  
-ATOM    536  CB  PRO A  73      10.618  22.546  19.843  1.00 17.90           C  
-ATOM    537  CG  PRO A  73       9.546  22.939  20.836  1.00 18.32           C  
-ATOM    538  CD  PRO A  73       9.184  24.400  20.684  1.00 20.11           C  
-ATOM    539  N   LEU A  74      10.703  24.461  17.263  1.00 21.37           N  
-ATOM    540  CA  LEU A  74      11.002  24.732  15.841  1.00 18.93           C  
-ATOM    541  C   LEU A  74      11.892  25.946  15.701  1.00 20.45           C  
-ATOM    542  O   LEU A  74      12.907  25.902  14.987  1.00 19.08           O  
-ATOM    543  CB  LEU A  74       9.697  24.902  15.054  1.00 19.25           C  
-ATOM    544  CG  LEU A  74       9.909  25.243  13.547  1.00 17.71           C  
-ATOM    545  CD1 LEU A  74      10.712  24.155  12.861  1.00 19.27           C  
-ATOM    546  CD2 LEU A  74       8.485  25.447  13.056  1.00 14.79           C  
-ATOM    547  N   PHE A  75      11.567  27.064  16.405  1.00 16.33           N  
-ATOM    548  CA  PHE A  75      12.391  28.260  16.346  1.00 12.95           C  
-ATOM    549  C   PHE A  75      13.815  27.891  16.769  1.00 20.84           C  
-ATOM    550  O   PHE A  75      14.819  28.325  16.186  1.00 19.22           O  
-ATOM    551  CB  PHE A  75      11.893  29.398  17.272  1.00 15.68           C  
-ATOM    552  CG  PHE A  75      12.679  30.688  17.281  1.00 20.79           C  
-ATOM    553  CD1 PHE A  75      12.463  31.709  16.356  1.00 20.21           C  
-ATOM    554  CD2 PHE A  75      13.673  30.925  18.246  1.00 26.22           C  
-ATOM    555  CE1 PHE A  75      13.146  32.898  16.374  1.00 18.96           C  
-ATOM    556  CE2 PHE A  75      14.377  32.120  18.292  1.00 20.51           C  
-ATOM    557  CZ  PHE A  75      14.120  33.120  17.355  1.00 25.49           C  
-ATOM    558  N   ASP A  76      13.947  27.078  17.841  1.00 19.54           N  
-ATOM    559  CA  ASP A  76      15.269  26.684  18.322  1.00 26.12           C  
-ATOM    560  C   ASP A  76      16.108  25.878  17.326  1.00 26.43           C  
-ATOM    561  O   ASP A  76      17.343  25.939  17.385  1.00 28.29           O  
-ATOM    562  CB  ASP A  76      15.163  25.912  19.654  1.00 26.26           C  
-ATOM    563  CG  ASP A  76      14.921  26.796  20.877  1.00 32.04           C  
-ATOM    564  OD1 ASP A  76      15.147  28.045  20.817  1.00 26.24           O  
-ATOM    565  OD2 ASP A  76      14.494  26.152  21.895  1.00 36.64           O  
-ATOM    566  N   SER A  77      15.436  25.109  16.475  1.00 24.12           N  
-ATOM    567  CA  SER A  77      16.167  24.324  15.471  1.00 23.21           C  
-ATOM    568  C   SER A  77      15.930  24.838  14.066  1.00 19.95           C  
-ATOM    569  O   SER A  77      16.011  24.056  13.124  1.00 21.31           O  
-ATOM    570  CB  SER A  77      15.646  22.880  15.603  1.00 22.11           C  
-ATOM    571  OG  SER A  77      15.957  22.553  16.965  1.00 33.85           O  
-ATOM    572  N   LEU A  78      15.640  26.113  13.846  1.00 18.28           N  
-ATOM    573  CA  LEU A  78      15.372  26.667  12.538  1.00 17.12           C  
-ATOM    574  C   LEU A  78      16.522  26.526  11.558  1.00 22.71           C  
-ATOM    575  O   LEU A  78      16.340  26.523  10.337  1.00 19.39           O  
-ATOM    576  CB  LEU A  78      15.023  28.141  12.626  1.00 18.01           C  
-ATOM    577  CG  LEU A  78      13.585  28.602  12.491  1.00 19.73           C  
-ATOM    578  CD1 LEU A  78      13.668  30.098  12.211  1.00 20.94           C  
-ATOM    579  CD2 LEU A  78      12.773  27.784  11.531  1.00  9.46           C  
-ATOM    580  N   GLU A  79      17.743  26.422  12.068  1.00 23.23           N  
-ATOM    581  CA  GLU A  79      18.969  26.242  11.321  1.00 26.93           C  
-ATOM    582  C   GLU A  79      18.992  24.856  10.658  1.00 25.31           C  
-ATOM    583  O   GLU A  79      19.836  24.662   9.750  1.00 28.09           O  
-ATOM    584  CB  GLU A  79      20.263  26.491  12.123  1.00 26.12           C  
-ATOM    585  CG  GLU A  79      20.593  25.548  13.244  1.00 42.49           C  
-ATOM    586  CD  GLU A  79      19.744  25.494  14.505  1.00 43.90           C  
-ATOM    587  OE1 GLU A  79      18.976  26.460  14.791  1.00 38.35           O  
-ATOM    588  OE2 GLU A  79      19.866  24.465  15.241  1.00 43.54           O  
-ATOM    589  N   GLU A  80      18.111  23.923  11.005  1.00 21.29           N  
-ATOM    590  CA  GLU A  80      18.070  22.609  10.393  1.00 24.10           C  
-ATOM    591  C   GLU A  80      16.932  22.448   9.354  1.00 23.32           C  
-ATOM    592  O   GLU A  80      16.804  21.378   8.737  1.00 20.67           O  
-ATOM    593  CB  GLU A  80      17.820  21.500  11.410  1.00 26.63           C  
-ATOM    594  CG  GLU A  80      18.700  21.201  12.612  1.00 49.64           C  
-ATOM    595  CD  GLU A  80      17.957  20.152  13.457  1.00 62.32           C  
-ATOM    596  OE1 GLU A  80      17.906  18.965  13.026  1.00 72.13           O  
-ATOM    597  OE2 GLU A  80      17.384  20.480  14.522  1.00 69.37           O  
-ATOM    598  N   THR A  81      16.079  23.456   9.166  1.00 22.22           N  
-ATOM    599  CA  THR A  81      14.921  23.341   8.291  1.00 18.26           C  
-ATOM    600  C   THR A  81      15.171  23.450   6.788  1.00 21.61           C  
-ATOM    601  O   THR A  81      14.302  23.050   5.995  1.00 22.09           O  
-ATOM    602  CB  THR A  81      13.884  24.411   8.728  1.00 15.95           C  
-ATOM    603  OG1 THR A  81      14.549  25.685   8.559  1.00 15.10           O  
-ATOM    604  CG2 THR A  81      13.307  24.256  10.127  1.00 14.47           C  
-ATOM    605  N   GLY A  82      16.315  24.011   6.420  1.00 22.06           N  
-ATOM    606  CA  GLY A  82      16.610  24.227   4.999  1.00 23.39           C  
-ATOM    607  C   GLY A  82      15.988  25.567   4.575  1.00 20.03           C  
-ATOM    608  O   GLY A  82      15.306  25.647   3.535  1.00 22.28           O  
-ATOM    609  N   ALA A  83      16.200  26.628   5.325  1.00 17.37           N  
-ATOM    610  CA  ALA A  83      15.656  27.954   5.060  1.00 16.27           C  
-ATOM    611  C   ALA A  83      16.538  28.751   4.126  1.00 14.45           C  
-ATOM    612  O   ALA A  83      16.145  29.758   3.572  1.00 19.04           O  
-ATOM    613  CB  ALA A  83      15.614  28.798   6.363  1.00 21.87           C  
-ATOM    614  N   GLN A  84      17.802  28.383   3.969  1.00 16.26           N  
-ATOM    615  CA  GLN A  84      18.697  29.116   3.096  1.00 18.84           C  
-ATOM    616  C   GLN A  84      18.123  29.182   1.683  1.00 19.91           C  
-ATOM    617  O   GLN A  84      17.809  28.131   1.106  1.00 19.89           O  
-ATOM    618  CB  GLN A  84      20.039  28.375   3.117  1.00 24.79           C  
-ATOM    619  CG  GLN A  84      21.205  28.903   2.342  1.00 39.36           C  
-ATOM    620  CD  GLN A  84      21.833  30.238   2.639  1.00 52.59           C  
-ATOM    621  OE1 GLN A  84      21.619  31.233   1.895  1.00 61.51           O  
-ATOM    622  NE2 GLN A  84      22.653  30.326   3.699  1.00 56.20           N  
-ATOM    623  N   GLY A  85      17.933  30.363   1.107  1.00 22.13           N  
-ATOM    624  CA  GLY A  85      17.398  30.508  -0.253  1.00 24.35           C  
-ATOM    625  C   GLY A  85      15.918  30.238  -0.407  1.00 22.39           C  
-ATOM    626  O   GLY A  85      15.396  30.301  -1.517  1.00 24.39           O  
-ATOM    627  N   ARG A  86      15.226  29.928   0.674  1.00 22.32           N  
-ATOM    628  CA  ARG A  86      13.805  29.618   0.697  1.00 19.56           C  
-ATOM    629  C   ARG A  86      12.967  30.880   0.789  1.00 20.88           C  
-ATOM    630  O   ARG A  86      13.335  31.804   1.551  1.00 19.30           O  
-ATOM    631  CB  ARG A  86      13.471  28.729   1.891  1.00 18.63           C  
-ATOM    632  CG  ARG A  86      12.067  28.211   1.972  1.00 19.52           C  
-ATOM    633  CD  ARG A  86      11.904  26.885   1.258  1.00 24.30           C  
-ATOM    634  NE  ARG A  86      13.037  25.988   1.451  1.00 25.86           N  
-ATOM    635  CZ  ARG A  86      13.306  24.914   0.730  1.00 26.55           C  
-ATOM    636  NH1 ARG A  86      12.594  24.500  -0.303  1.00 18.08           N  
-ATOM    637  NH2 ARG A  86      14.346  24.131   0.993  1.00 28.13           N  
-ATOM    638  N   LYS A  87      11.885  30.859  -0.031  1.00 15.85           N  
-ATOM    639  CA  LYS A  87      10.962  31.995  -0.013  1.00 16.26           C  
-ATOM    640  C   LYS A  87      10.000  31.719   1.174  1.00 14.68           C  
-ATOM    641  O   LYS A  87       9.385  30.638   1.230  1.00 12.11           O  
-ATOM    642  CB  LYS A  87      10.088  32.128  -1.285  1.00 21.25           C  
-ATOM    643  CG  LYS A  87      10.991  32.580  -2.442  1.00 22.93           C  
-ATOM    644  CD  LYS A  87      10.255  32.546  -3.772  1.00 31.37           C  
-ATOM    645  CE  LYS A  87      11.252  32.076  -4.820  1.00 44.79           C  
-ATOM    646  NZ  LYS A  87      11.490  33.105  -5.870  1.00 59.03           N  
-ATOM    647  N   VAL A  88      10.020  32.721   2.059  1.00 16.58           N  
-ATOM    648  CA  VAL A  88       9.258  32.696   3.304  1.00 16.63           C  
-ATOM    649  C   VAL A  88       8.554  34.000   3.627  1.00 14.35           C  
-ATOM    650  O   VAL A  88       8.870  35.120   3.184  1.00 18.98           O  
-ATOM    651  CB  VAL A  88      10.226  32.347   4.508  1.00 14.67           C  
-ATOM    652  CG1 VAL A  88      11.181  31.171   4.301  1.00 13.89           C  
-ATOM    653  CG2 VAL A  88      11.097  33.539   4.869  1.00 14.77           C  
-ATOM    654  N   ALA A  89       7.518  33.952   4.487  1.00 14.31           N  
-ATOM    655  CA  ALA A  89       6.799  35.140   4.965  1.00 15.43           C  
-ATOM    656  C   ALA A  89       6.225  34.714   6.355  1.00 14.09           C  
-ATOM    657  O   ALA A  89       5.953  33.526   6.575  1.00 11.69           O  
-ATOM    658  CB  ALA A  89       5.739  35.738   4.060  1.00 14.79           C  
-ATOM    659  N   CYS A  90       6.075  35.689   7.260  1.00 15.80           N  
-ATOM    660  CA  CYS A  90       5.558  35.341   8.609  1.00 16.72           C  
-ATOM    661  C   CYS A  90       4.279  36.057   8.943  1.00 13.58           C  
-ATOM    662  O   CYS A  90       3.955  37.104   8.391  1.00 14.26           O  
-ATOM    663  CB  CYS A  90       6.637  35.728   9.642  1.00 12.88           C  
-ATOM    664  SG  CYS A  90       8.260  34.970   9.380  1.00 16.61           S  
-ATOM    665  N   PHE A  91       3.554  35.516   9.939  1.00 13.60           N  
-ATOM    666  CA  PHE A  91       2.280  36.073  10.384  1.00 14.60           C  
-ATOM    667  C   PHE A  91       2.060  35.737  11.873  1.00 14.87           C  
-ATOM    668  O   PHE A  91       2.735  34.841  12.401  1.00 15.38           O  
-ATOM    669  CB  PHE A  91       1.052  35.486   9.611  1.00 12.44           C  
-ATOM    670  CG  PHE A  91       0.750  33.986   9.590  1.00 10.63           C  
-ATOM    671  CD1 PHE A  91       1.434  33.099   8.787  1.00 12.27           C  
-ATOM    672  CD2 PHE A  91      -0.285  33.454  10.370  1.00  7.87           C  
-ATOM    673  CE1 PHE A  91       1.175  31.728   8.770  1.00 13.48           C  
-ATOM    674  CE2 PHE A  91      -0.555  32.103  10.378  1.00  9.70           C  
-ATOM    675  CZ  PHE A  91       0.171  31.215   9.563  1.00 13.68           C  
-ATOM    676  N   GLY A  92       1.095  36.375  12.494  1.00 19.04           N  
-ATOM    677  CA  GLY A  92       0.794  36.037  13.895  1.00 18.92           C  
-ATOM    678  C   GLY A  92      -0.219  37.029  14.438  1.00 14.88           C  
-ATOM    679  O   GLY A  92      -0.527  38.061  13.857  1.00 11.95           O  
-ATOM    680  N   CYS A  93      -0.701  36.662  15.633  1.00 15.04           N  
-ATOM    681  CA  CYS A  93      -1.673  37.465  16.385  1.00 16.32           C  
-ATOM    682  C   CYS A  93      -1.004  38.015  17.657  1.00 13.05           C  
-ATOM    683  O   CYS A  93      -0.080  37.390  18.189  1.00 13.02           O  
-ATOM    684  CB  CYS A  93      -2.905  36.627  16.734  1.00 20.71           C  
-ATOM    685  SG  CYS A  93      -3.862  36.155  15.270  1.00 16.45           S  
-ATOM    686  N   GLY A  94      -1.457  39.207  18.045  1.00 14.40           N  
-ATOM    687  CA  GLY A  94      -0.926  39.921  19.201  1.00 13.94           C  
-ATOM    688  C   GLY A  94      -1.920  40.990  19.644  1.00 15.92           C  
-ATOM    689  O   GLY A  94      -3.142  40.931  19.394  1.00 14.79           O  
-ATOM    690  N   ALA A  95      -1.371  41.965  20.370  1.00 16.25           N  
-ATOM    691  CA  ALA A  95      -2.182  43.069  20.925  1.00 21.77           C  
-ATOM    692  C   ALA A  95      -1.427  44.368  20.706  1.00 19.89           C  
-ATOM    693  O   ALA A  95      -0.326  44.600  21.201  1.00 22.31           O  
-ATOM    694  CB  ALA A  95      -2.461  42.859  22.412  1.00 23.94           C  
-ATOM    695  N   SER A  96      -1.997  45.224  19.847  1.00 20.88           N  
-ATOM    696  CA  SER A  96      -1.402  46.479  19.449  1.00 26.84           C  
-ATOM    697  C   SER A  96      -1.071  47.440  20.573  1.00 30.95           C  
-ATOM    698  O   SER A  96      -0.190  48.297  20.425  1.00 31.01           O  
-ATOM    699  CB  SER A  96      -2.155  47.182  18.309  1.00 32.87           C  
-ATOM    700  OG  SER A  96      -3.182  48.033  18.765  1.00 53.85           O  
-ATOM    701  N   SER A  97      -1.695  47.309  21.725  1.00 35.72           N  
-ATOM    702  CA  SER A  97      -1.571  48.014  22.970  1.00 35.42           C  
-ATOM    703  C   SER A  97      -0.228  47.683  23.649  1.00 35.51           C  
-ATOM    704  O   SER A  97       0.340  48.532  24.351  1.00 39.10           O  
-ATOM    705  CB  SER A  97      -2.722  47.598  23.933  1.00 33.65           C  
-ATOM    706  OG  SER A  97      -3.779  46.801  23.374  1.00 47.07           O  
-ATOM    707  N   TYR A  98       0.326  46.475  23.470  1.00 32.66           N  
-ATOM    708  CA  TYR A  98       1.561  46.040  24.112  1.00 29.62           C  
-ATOM    709  C   TYR A  98       2.866  46.621  23.620  1.00 29.71           C  
-ATOM    710  O   TYR A  98       2.896  47.183  22.545  1.00 30.16           O  
-ATOM    711  CB  TYR A  98       1.674  44.500  24.110  1.00 27.59           C  
-ATOM    712  CG  TYR A  98       0.510  43.929  24.888  1.00 26.85           C  
-ATOM    713  CD1 TYR A  98      -0.553  44.672  25.396  1.00 30.98           C  
-ATOM    714  CD2 TYR A  98       0.491  42.581  25.111  1.00 26.45           C  
-ATOM    715  CE1 TYR A  98      -1.594  44.104  26.074  1.00 35.34           C  
-ATOM    716  CE2 TYR A  98      -0.525  41.953  25.786  1.00 27.67           C  
-ATOM    717  CZ  TYR A  98      -1.564  42.723  26.268  1.00 36.04           C  
-ATOM    718  OH  TYR A  98      -2.604  42.085  26.924  1.00 37.41           O  
-ATOM    719  N   GLU A  99       3.926  46.536  24.409  1.00 31.01           N  
-ATOM    720  CA  GLU A  99       5.249  47.062  24.028  1.00 33.11           C  
-ATOM    721  C   GLU A  99       5.741  46.370  22.753  1.00 28.67           C  
-ATOM    722  O   GLU A  99       6.087  47.126  21.822  1.00 31.78           O  
-ATOM    723  CB  GLU A  99       6.222  46.948  25.191  1.00 35.10           C  
-ATOM    724  CG  GLU A  99       7.569  47.616  25.222  1.00 43.99           C  
-ATOM    725  CD  GLU A  99       7.625  49.091  24.878  1.00 59.58           C  
-ATOM    726  OE1 GLU A  99       6.790  49.917  25.341  1.00 67.79           O  
-ATOM    727  OE2 GLU A  99       8.544  49.474  24.089  1.00 65.71           O  
-ATOM    728  N   TYR A 100       5.757  45.034  22.711  1.00 25.77           N  
-ATOM    729  CA  TYR A 100       6.197  44.304  21.509  1.00 18.65           C  
-ATOM    730  C   TYR A 100       4.978  43.650  20.851  1.00 15.33           C  
-ATOM    731  O   TYR A 100       4.723  42.451  20.985  1.00 20.29           O  
-ATOM    732  CB  TYR A 100       7.258  43.259  21.887  1.00 18.96           C  
-ATOM    733  CG  TYR A 100       8.390  43.880  22.705  1.00 25.27           C  
-ATOM    734  CD1 TYR A 100       9.231  44.843  22.159  1.00 24.39           C  
-ATOM    735  CD2 TYR A 100       8.586  43.537  24.034  1.00 27.71           C  
-ATOM    736  CE1 TYR A 100      10.245  45.457  22.872  1.00 27.54           C  
-ATOM    737  CE2 TYR A 100       9.574  44.152  24.780  1.00 31.85           C  
-ATOM    738  CZ  TYR A 100      10.394  45.118  24.212  1.00 33.44           C  
-ATOM    739  OH  TYR A 100      11.387  45.700  24.999  1.00 30.99           O  
-ATOM    740  N   PHE A 101       4.226  44.451  20.118  1.00 16.17           N  
-ATOM    741  CA  PHE A 101       3.050  44.005  19.368  1.00 20.34           C  
-ATOM    742  C   PHE A 101       3.529  43.003  18.296  1.00 19.90           C  
-ATOM    743  O   PHE A 101       4.347  43.328  17.411  1.00 20.29           O  
-ATOM    744  CB  PHE A 101       2.351  45.140  18.642  1.00 20.88           C  
-ATOM    745  CG  PHE A 101       1.253  44.776  17.667  1.00 22.66           C  
-ATOM    746  CD1 PHE A 101       0.316  43.799  17.963  1.00 19.70           C  
-ATOM    747  CD2 PHE A 101       1.164  45.415  16.437  1.00 19.32           C  
-ATOM    748  CE1 PHE A 101      -0.709  43.465  17.120  1.00 15.28           C  
-ATOM    749  CE2 PHE A 101       0.128  45.115  15.584  1.00 19.26           C  
-ATOM    750  CZ  PHE A 101      -0.794  44.137  15.915  1.00 16.11           C  
-ATOM    751  N   CYS A 102       3.053  41.769  18.391  1.00 15.23           N  
-ATOM    752  CA  CYS A 102       3.488  40.702  17.489  1.00 11.68           C  
-ATOM    753  C   CYS A 102       4.992  40.616  17.501  1.00 13.82           C  
-ATOM    754  O   CYS A 102       5.588  40.294  16.459  1.00 16.64           O  
-ATOM    755  CB  CYS A 102       2.901  40.708  16.071  1.00  7.56           C  
-ATOM    756  SG  CYS A 102       1.128  40.464  16.063  1.00 13.16           S  
-ATOM    757  N   GLY A 103       5.700  40.793  18.629  1.00 11.79           N  
-ATOM    758  CA  GLY A 103       7.151  40.704  18.686  1.00  6.67           C  
-ATOM    759  C   GLY A 103       7.576  39.313  18.280  1.00  9.86           C  
-ATOM    760  O   GLY A 103       8.774  39.173  17.857  1.00 11.36           O  
-ATOM    761  N   ALA A 104       6.768  38.243  18.373  1.00 12.20           N  
-ATOM    762  CA  ALA A 104       7.236  36.937  17.917  1.00 12.95           C  
-ATOM    763  C   ALA A 104       7.399  36.953  16.359  1.00 17.78           C  
-ATOM    764  O   ALA A 104       8.342  36.244  15.939  1.00 16.46           O  
-ATOM    765  CB  ALA A 104       6.375  35.748  18.264  1.00 14.41           C  
-ATOM    766  N   VAL A 105       6.576  37.663  15.588  1.00 16.36           N  
-ATOM    767  CA  VAL A 105       6.732  37.746  14.131  1.00 13.12           C  
-ATOM    768  C   VAL A 105       8.062  38.408  13.823  1.00 14.71           C  
-ATOM    769  O   VAL A 105       8.754  37.909  12.944  1.00 16.81           O  
-ATOM    770  CB  VAL A 105       5.576  38.499  13.441  1.00 18.79           C  
-ATOM    771  CG1 VAL A 105       5.851  38.620  11.949  1.00 13.75           C  
-ATOM    772  CG2 VAL A 105       4.280  37.793  13.816  1.00 12.66           C  
-ATOM    773  N   ASP A 106       8.510  39.499  14.470  1.00 14.27           N  
-ATOM    774  CA  ASP A 106       9.792  40.124  14.229  1.00 13.35           C  
-ATOM    775  C   ASP A 106      10.988  39.235  14.515  1.00 17.52           C  
-ATOM    776  O   ASP A 106      12.012  39.244  13.832  1.00 17.20           O  
-ATOM    777  CB  ASP A 106      10.113  41.322  15.129  1.00 19.52           C  
-ATOM    778  CG  ASP A 106       9.013  42.344  15.166  1.00 27.85           C  
-ATOM    779  OD1 ASP A 106       8.297  42.254  14.168  1.00 40.03           O  
-ATOM    780  OD2 ASP A 106       8.772  43.149  16.073  1.00 32.26           O  
-ATOM    781  N   ALA A 107      10.918  38.480  15.635  1.00 18.21           N  
-ATOM    782  CA  ALA A 107      11.972  37.588  16.045  1.00 16.59           C  
-ATOM    783  C   ALA A 107      12.189  36.449  15.050  1.00 14.48           C  
-ATOM    784  O   ALA A 107      13.335  36.093  14.741  1.00 12.72           O  
-ATOM    785  CB  ALA A 107      11.631  36.972  17.420  1.00 13.85           C  
-ATOM    786  N   ILE A 108      11.072  35.885  14.599  1.00 13.28           N  
-ATOM    787  CA  ILE A 108      11.140  34.770  13.607  1.00 14.93           C  
-ATOM    788  C   ILE A 108      11.689  35.317  12.279  1.00 15.59           C  
-ATOM    789  O   ILE A 108      12.576  34.691  11.677  1.00 15.15           O  
-ATOM    790  CB  ILE A 108       9.787  34.054  13.434  1.00 14.66           C  
-ATOM    791  CG1 ILE A 108       9.342  33.351  14.764  1.00 12.65           C  
-ATOM    792  CG2 ILE A 108       9.812  32.992  12.310  1.00 12.56           C  
-ATOM    793  CD1 ILE A 108       7.842  33.218  14.847  1.00 13.94           C  
-ATOM    794  N   GLU A 109      11.234  36.471  11.777  1.00 17.35           N  
-ATOM    795  CA  GLU A 109      11.724  37.108  10.555  1.00 16.84           C  
-ATOM    796  C   GLU A 109      13.224  37.376  10.649  1.00 18.22           C  
-ATOM    797  O   GLU A 109      13.993  37.053   9.743  1.00 18.08           O  
-ATOM    798  CB  GLU A 109      11.060  38.480  10.287  1.00 15.53           C  
-ATOM    799  CG  GLU A 109       9.595  38.273   9.913  1.00 17.86           C  
-ATOM    800  CD  GLU A 109       9.005  39.486   9.231  1.00 25.82           C  
-ATOM    801  OE1 GLU A 109       9.720  40.482   9.315  1.00 27.68           O  
-ATOM    802  OE2 GLU A 109       7.884  39.377   8.695  1.00 26.36           O  
-ATOM    803  N   GLU A 110      13.686  37.960  11.764  1.00 21.22           N  
-ATOM    804  CA  GLU A 110      15.111  38.233  11.962  1.00 21.17           C  
-ATOM    805  C   GLU A 110      15.970  36.992  11.916  1.00 17.48           C  
-ATOM    806  O   GLU A 110      17.077  37.061  11.337  1.00 21.35           O  
-ATOM    807  CB  GLU A 110      15.360  39.082  13.210  1.00 20.67           C  
-ATOM    808  CG  GLU A 110      16.833  39.378  13.472  1.00 32.15           C  
-ATOM    809  CD  GLU A 110      17.175  40.849  13.560  1.00 42.74           C  
-ATOM    810  OE1 GLU A 110      16.256  41.656  13.847  1.00 48.15           O  
-ATOM    811  OE2 GLU A 110      18.330  41.293  13.334  1.00 46.94           O  
-ATOM    812  N   LYS A 111      15.592  35.846  12.488  1.00 17.56           N  
-ATOM    813  CA  LYS A 111      16.358  34.629  12.452  1.00 16.63           C  
-ATOM    814  C   LYS A 111      16.339  34.090  11.002  1.00 18.09           C  
-ATOM    815  O   LYS A 111      17.371  33.642  10.498  1.00 18.20           O  
-ATOM    816  CB  LYS A 111      15.814  33.537  13.387  1.00 14.56           C  
-ATOM    817  CG  LYS A 111      16.787  32.378  13.465  1.00 15.85           C  
-ATOM    818  CD  LYS A 111      16.340  31.417  14.558  1.00 21.54           C  
-ATOM    819  CE  LYS A 111      17.620  30.866  15.192  1.00 30.18           C  
-ATOM    820  NZ  LYS A 111      17.369  29.777  16.195  1.00 26.12           N  
-ATOM    821  N   LEU A 112      15.165  34.103  10.354  1.00 15.74           N  
-ATOM    822  CA  LEU A 112      15.102  33.601   8.952  1.00 17.01           C  
-ATOM    823  C   LEU A 112      16.058  34.383   8.053  1.00 17.73           C  
-ATOM    824  O   LEU A 112      16.755  33.752   7.245  1.00 19.71           O  
-ATOM    825  CB  LEU A 112      13.652  33.688   8.440  1.00 11.95           C  
-ATOM    826  CG  LEU A 112      12.696  32.638   8.998  1.00 11.14           C  
-ATOM    827  CD1 LEU A 112      11.254  33.007   8.626  1.00 16.12           C  
-ATOM    828  CD2 LEU A 112      13.044  31.219   8.574  1.00 12.23           C  
-ATOM    829  N   LYS A 113      16.099  35.712   8.173  1.00 20.50           N  
-ATOM    830  CA  LYS A 113      16.948  36.635   7.448  1.00 23.12           C  
-ATOM    831  C   LYS A 113      18.418  36.229   7.667  1.00 27.63           C  
-ATOM    832  O   LYS A 113      19.199  36.112   6.711  1.00 24.54           O  
-ATOM    833  CB  LYS A 113      16.840  38.090   7.870  1.00 29.33           C  
-ATOM    834  CG  LYS A 113      16.121  39.217   7.203  1.00 46.21           C  
-ATOM    835  CD  LYS A 113      14.648  39.380   7.528  1.00 63.51           C  
-ATOM    836  CE  LYS A 113      14.032  40.722   7.875  1.00 65.50           C  
-ATOM    837  NZ  LYS A 113      13.860  40.988   9.348  1.00 64.25           N  
-ATOM    838  N   ASN A 114      18.798  36.020   8.937  1.00 26.50           N  
-ATOM    839  CA  ASN A 114      20.142  35.605   9.338  1.00 24.05           C  
-ATOM    840  C   ASN A 114      20.432  34.224   8.741  1.00 26.73           C  
-ATOM    841  O   ASN A 114      21.588  33.903   8.479  1.00 26.84           O  
-ATOM    842  CB  ASN A 114      20.299  35.447  10.849  1.00 22.43           C  
-ATOM    843  CG  ASN A 114      20.151  36.611  11.812  1.00 27.53           C  
-ATOM    844  OD1 ASN A 114      19.916  36.350  13.022  1.00 27.38           O  
-ATOM    845  ND2 ASN A 114      20.277  37.826  11.292  1.00 19.49           N  
-ATOM    846  N   LEU A 115      19.452  33.345   8.509  1.00 22.64           N  
-ATOM    847  CA  LEU A 115      19.677  32.020   7.965  1.00 21.73           C  
-ATOM    848  C   LEU A 115      19.706  31.911   6.442  1.00 18.55           C  
-ATOM    849  O   LEU A 115      19.751  30.783   5.905  1.00 18.93           O  
-ATOM    850  CB  LEU A 115      18.585  31.086   8.543  1.00 20.47           C  
-ATOM    851  CG  LEU A 115      18.796  30.706  10.009  1.00 19.34           C  
-ATOM    852  CD1 LEU A 115      17.637  29.876  10.564  1.00 18.47           C  
-ATOM    853  CD2 LEU A 115      20.072  29.881  10.160  1.00 16.95           C  
-ATOM    854  N   GLY A 116      19.628  33.047   5.786  1.00 18.41           N  
-ATOM    855  CA  GLY A 116      19.633  33.142   4.319  1.00 20.96           C  
-ATOM    856  C   GLY A 116      18.291  32.947   3.619  1.00 23.12           C  
-ATOM    857  O   GLY A 116      18.268  32.671   2.385  1.00 19.80           O  
-ATOM    858  N   ALA A 117      17.144  33.033   4.304  1.00 20.20           N  
-ATOM    859  CA  ALA A 117      15.837  32.857   3.676  1.00 17.01           C  
-ATOM    860  C   ALA A 117      15.521  34.116   2.868  1.00 19.90           C  
-ATOM    861  O   ALA A 117      16.153  35.184   3.063  1.00 17.90           O  
-ATOM    862  CB  ALA A 117      14.703  32.612   4.685  1.00 14.98           C  
-ATOM    863  N   GLU A 118      14.538  34.026   1.956  1.00 16.23           N  
-ATOM    864  CA  GLU A 118      14.173  35.226   1.210  1.00 19.02           C  
-ATOM    865  C   GLU A 118      12.811  35.682   1.757  1.00 16.71           C  
-ATOM    866  O   GLU A 118      11.883  34.919   1.432  1.00 18.58           O  
-ATOM    867  CB  GLU A 118      14.047  34.958  -0.310  1.00 25.33           C  
-ATOM    868  CG  GLU A 118      13.654  36.202  -1.115  1.00 29.63           C  
-ATOM    869  CD  GLU A 118      13.305  35.913  -2.569  1.00 38.17           C  
-ATOM    870  OE1 GLU A 118      13.713  34.873  -3.142  1.00 36.11           O  
-ATOM    871  OE2 GLU A 118      12.594  36.745  -3.185  1.00 34.79           O  
-ATOM    872  N   ILE A 119      12.747  36.789   2.493  1.00 18.90           N  
-ATOM    873  CA  ILE A 119      11.462  37.262   3.063  1.00 19.52           C  
-ATOM    874  C   ILE A 119      10.740  37.908   1.880  1.00 18.52           C  
-ATOM    875  O   ILE A 119      11.230  38.961   1.483  1.00 20.04           O  
-ATOM    876  CB  ILE A 119      11.659  38.274   4.212  1.00 20.88           C  
-ATOM    877  CG1 ILE A 119      12.570  37.768   5.332  1.00 26.93           C  
-ATOM    878  CG2 ILE A 119      10.410  38.807   4.874  1.00 14.51           C  
-ATOM    879  CD1 ILE A 119      12.506  36.381   5.860  1.00 26.64           C  
-ATOM    880  N   VAL A 120       9.674  37.324   1.385  1.00 19.91           N  
-ATOM    881  CA  VAL A 120       8.928  37.791   0.213  1.00 21.42           C  
-ATOM    882  C   VAL A 120       7.961  38.911   0.514  1.00 24.75           C  
-ATOM    883  O   VAL A 120       7.639  39.717  -0.356  1.00 23.54           O  
-ATOM    884  CB  VAL A 120       8.160  36.698  -0.561  1.00 21.61           C  
-ATOM    885  CG1 VAL A 120       9.147  35.600  -1.021  1.00 22.49           C  
-ATOM    886  CG2 VAL A 120       7.022  36.003   0.147  1.00 13.84           C  
-ATOM    887  N   GLN A 121       7.533  38.953   1.774  1.00 23.67           N  
-ATOM    888  CA  GLN A 121       6.577  39.986   2.221  1.00 23.30           C  
-ATOM    889  C   GLN A 121       6.828  40.267   3.713  1.00 14.93           C  
-ATOM    890  O   GLN A 121       7.226  39.376   4.451  1.00 18.08           O  
-ATOM    891  CB  GLN A 121       5.198  39.349   2.041  1.00 24.37           C  
-ATOM    892  CG  GLN A 121       3.878  39.947   1.779  1.00 39.80           C  
-ATOM    893  CD  GLN A 121       3.817  41.033   0.723  1.00 50.16           C  
-ATOM    894  OE1 GLN A 121       4.378  40.926  -0.375  1.00 52.18           O  
-ATOM    895  NE2 GLN A 121       3.128  42.142   1.041  1.00 48.89           N  
-ATOM    896  N   ASP A 122       6.562  41.506   4.101  1.00 17.06           N  
-ATOM    897  CA  ASP A 122       6.694  41.832   5.543  1.00 23.53           C  
-ATOM    898  C   ASP A 122       5.552  41.091   6.285  1.00 22.60           C  
-ATOM    899  O   ASP A 122       4.435  40.938   5.724  1.00 20.84           O  
-ATOM    900  CB  ASP A 122       6.589  43.324   5.776  1.00 27.33           C  
-ATOM    901  CG  ASP A 122       7.745  44.169   5.228  1.00 37.27           C  
-ATOM    902  OD1 ASP A 122       8.905  43.698   5.054  1.00 49.08           O  
-ATOM    903  OD2 ASP A 122       7.442  45.368   4.991  1.00 37.00           O  
-ATOM    904  N   GLY A 123       5.821  40.620   7.499  1.00 23.18           N  
-ATOM    905  CA  GLY A 123       4.893  39.883   8.306  1.00 17.34           C  
-ATOM    906  C   GLY A 123       3.523  40.492   8.512  1.00 14.91           C  
-ATOM    907  O   GLY A 123       3.355  41.708   8.663  1.00 19.80           O  
-ATOM    908  N   LEU A 124       2.496  39.644   8.538  1.00 14.87           N  
-ATOM    909  CA  LEU A 124       1.122  40.014   8.803  1.00 11.79           C  
-ATOM    910  C   LEU A 124       1.021  39.972  10.372  1.00 16.46           C  
-ATOM    911  O   LEU A 124       1.313  38.962  11.031  1.00 14.14           O  
-ATOM    912  CB  LEU A 124       0.180  38.958   8.320  1.00 12.48           C  
-ATOM    913  CG  LEU A 124      -1.307  39.211   8.585  1.00 11.67           C  
-ATOM    914  CD1 LEU A 124      -1.765  40.540   8.007  1.00 16.22           C  
-ATOM    915  CD2 LEU A 124      -2.007  38.030   7.932  1.00 13.25           C  
-ATOM    916  N   ARG A 125       0.682  41.103  10.933  1.00 14.33           N  
-ATOM    917  CA  ARG A 125       0.542  41.252  12.395  1.00 15.84           C  
-ATOM    918  C   ARG A 125      -0.903  41.620  12.733  1.00 17.06           C  
-ATOM    919  O   ARG A 125      -1.368  42.776  12.485  1.00 19.72           O  
-ATOM    920  CB  ARG A 125       1.459  42.389  12.852  1.00 13.87           C  
-ATOM    921  CG  ARG A 125       2.923  42.101  12.684  1.00 13.95           C  
-ATOM    922  CD  ARG A 125       3.724  43.391  13.040  1.00 38.59           C  
-ATOM    923  NE  ARG A 125       4.926  43.189  12.207  1.00 61.23           N  
-ATOM    924  CZ  ARG A 125       6.080  42.707  12.645  1.00 67.61           C  
-ATOM    925  NH1 ARG A 125       6.056  42.473  13.967  1.00 70.19           N  
-ATOM    926  NH2 ARG A 125       7.130  42.483  11.844  1.00 59.90           N  
-ATOM    927  N   ILE A 126      -1.669  40.678  13.271  1.00 19.06           N  
-ATOM    928  CA  ILE A 126      -3.100  40.873  13.607  1.00 17.29           C  
-ATOM    929  C   ILE A 126      -3.345  41.381  15.038  1.00 17.45           C  
-ATOM    930  O   ILE A 126      -2.790  40.799  15.997  1.00 13.94           O  
-ATOM    931  CB  ILE A 126      -3.875  39.551  13.397  1.00 15.86           C  
-ATOM    932  CG1 ILE A 126      -3.712  39.011  11.957  1.00 18.20           C  
-ATOM    933  CG2 ILE A 126      -5.374  39.621  13.769  1.00 16.46           C  
-ATOM    934  CD1 ILE A 126      -4.292  39.979  10.947  1.00 24.20           C  
-ATOM    935  N   ASP A 127      -4.148  42.429  15.132  1.00 15.23           N  
-ATOM    936  CA  ASP A 127      -4.501  42.995  16.426  1.00 14.83           C  
-ATOM    937  C   ASP A 127      -5.818  42.394  16.895  1.00 14.91           C  
-ATOM    938  O   ASP A 127      -6.730  42.398  16.069  1.00 19.70           O  
-ATOM    939  CB  ASP A 127      -4.647  44.521  16.325  1.00 18.60           C  
-ATOM    940  CG  ASP A 127      -4.775  45.155  17.704  1.00 25.74           C  
-ATOM    941  OD1 ASP A 127      -4.480  44.537  18.757  1.00 26.59           O  
-ATOM    942  OD2 ASP A 127      -5.180  46.329  17.757  1.00 27.86           O  
-ATOM    943  N   GLY A 128      -5.936  41.867  18.128  1.00 15.53           N  
-ATOM    944  CA  GLY A 128      -7.208  41.338  18.501  1.00 16.04           C  
-ATOM    945  C   GLY A 128      -7.645  40.078  17.794  1.00 16.09           C  
-ATOM    946  O   GLY A 128      -6.910  39.177  17.394  1.00 18.59           O  
-ATOM    947  N   ASP A 129      -8.979  39.955  17.691  1.00 17.95           N  
-ATOM    948  CA  ASP A 129      -9.625  38.783  17.096  1.00 18.94           C  
-ATOM    949  C   ASP A 129      -9.380  38.819  15.591  1.00 18.66           C  
-ATOM    950  O   ASP A 129      -9.790  39.814  15.008  1.00 18.48           O  
-ATOM    951  CB  ASP A 129     -11.156  38.815  17.323  1.00 14.41           C  
-ATOM    952  CG  ASP A 129     -11.833  37.501  17.039  1.00 16.84           C  
-ATOM    953  OD1 ASP A 129     -11.401  36.540  16.350  1.00 16.07           O  
-ATOM    954  OD2 ASP A 129     -12.986  37.423  17.588  1.00 21.31           O  
-ATOM    955  N   PRO A 130      -8.805  37.774  15.042  1.00 20.42           N  
-ATOM    956  CA  PRO A 130      -8.520  37.673  13.623  1.00 16.21           C  
-ATOM    957  C   PRO A 130      -9.788  37.533  12.823  1.00 18.12           C  
-ATOM    958  O   PRO A 130      -9.824  37.879  11.625  1.00 19.56           O  
-ATOM    959  CB  PRO A 130      -7.677  36.377  13.480  1.00 16.08           C  
-ATOM    960  CG  PRO A 130      -8.026  35.546  14.704  1.00 16.04           C  
-ATOM    961  CD  PRO A 130      -8.373  36.587  15.785  1.00 16.99           C  
-ATOM    962  N   ARG A 131     -10.893  37.053  13.420  1.00 14.94           N  
-ATOM    963  CA  ARG A 131     -12.142  36.904  12.662  1.00 12.42           C  
-ATOM    964  C   ARG A 131     -12.687  38.211  12.169  1.00 14.55           C  
-ATOM    965  O   ARG A 131     -13.556  38.373  11.311  1.00 20.84           O  
-ATOM    966  CB  ARG A 131     -13.176  36.177  13.532  1.00 11.10           C  
-ATOM    967  CG  ARG A 131     -12.780  34.753  13.822  1.00  9.98           C  
-ATOM    968  CD  ARG A 131     -13.488  34.131  15.010  1.00 13.04           C  
-ATOM    969  NE  ARG A 131     -12.725  32.936  15.417  1.00 18.23           N  
-ATOM    970  CZ  ARG A 131     -11.585  32.818  16.126  1.00 14.86           C  
-ATOM    971  NH1 ARG A 131     -10.969  33.875  16.608  1.00 16.57           N  
-ATOM    972  NH2 ARG A 131     -10.993  31.649  16.350  1.00 14.55           N  
-ATOM    973  N   ALA A 132     -12.254  39.326  12.731  1.00 15.70           N  
-ATOM    974  CA  ALA A 132     -12.596  40.696  12.481  1.00 19.98           C  
-ATOM    975  C   ALA A 132     -11.537  41.360  11.592  1.00 21.68           C  
-ATOM    976  O   ALA A 132     -11.702  42.569  11.331  1.00 23.53           O  
-ATOM    977  CB  ALA A 132     -12.686  41.539  13.774  1.00 18.00           C  
-ATOM    978  N   ALA A 133     -10.542  40.563  11.188  1.00 20.72           N  
-ATOM    979  CA  ALA A 133      -9.470  41.158  10.349  1.00 22.09           C  
-ATOM    980  C   ALA A 133      -9.324  40.326   9.079  1.00 20.97           C  
-ATOM    981  O   ALA A 133      -8.293  40.344   8.428  1.00 18.25           O  
-ATOM    982  CB  ALA A 133      -8.162  41.243  11.150  1.00 19.76           C  
-ATOM    983  N   ARG A 134     -10.385  39.579   8.746  1.00 22.36           N  
-ATOM    984  CA  ARG A 134     -10.453  38.676   7.609  1.00 23.91           C  
-ATOM    985  C   ARG A 134     -10.010  39.231   6.262  1.00 27.26           C  
-ATOM    986  O   ARG A 134      -9.257  38.596   5.493  1.00 23.61           O  
-ATOM    987  CB  ARG A 134     -11.905  38.204   7.559  1.00 26.11           C  
-ATOM    988  CG  ARG A 134     -11.984  36.731   7.458  1.00 21.73           C  
-ATOM    989  CD  ARG A 134     -13.284  36.200   6.819  1.00 24.98           C  
-ATOM    990  NE  ARG A 134     -12.989  34.787   6.876  1.00 42.57           N  
-ATOM    991  CZ  ARG A 134     -12.543  33.930   5.989  1.00 46.04           C  
-ATOM    992  NH1 ARG A 134     -12.350  34.352   4.750  1.00 45.09           N  
-ATOM    993  NH2 ARG A 134     -12.320  32.714   6.507  1.00 47.85           N  
-ATOM    994  N   ASP A 135     -10.449  40.467   5.943  1.00 26.84           N  
-ATOM    995  CA  ASP A 135     -10.074  41.150   4.711  1.00 25.75           C  
-ATOM    996  C   ASP A 135      -8.574  41.443   4.675  1.00 24.26           C  
-ATOM    997  O   ASP A 135      -8.029  41.322   3.572  1.00 26.05           O  
-ATOM    998  CB  ASP A 135     -10.882  42.418   4.456  1.00 31.52           C  
-ATOM    999  CG  ASP A 135     -12.360  42.171   4.193  1.00 28.73           C  
-ATOM   1000  OD1 ASP A 135     -12.750  41.147   3.597  1.00 34.11           O  
-ATOM   1001  OD2 ASP A 135     -13.154  43.028   4.639  1.00 40.77           O  
-ATOM   1002  N   ASP A 136      -7.854  41.773   5.731  1.00 20.42           N  
-ATOM   1003  CA  ASP A 136      -6.421  42.001   5.745  1.00 21.21           C  
-ATOM   1004  C   ASP A 136      -5.649  40.694   5.562  1.00 21.16           C  
-ATOM   1005  O   ASP A 136      -4.567  40.615   4.964  1.00 25.28           O  
-ATOM   1006  CB  ASP A 136      -5.952  42.589   7.086  1.00 27.24           C  
-ATOM   1007  CG  ASP A 136      -6.513  43.950   7.451  1.00 34.91           C  
-ATOM   1008  OD1 ASP A 136      -6.949  44.710   6.558  1.00 34.97           O  
-ATOM   1009  OD2 ASP A 136      -6.509  44.316   8.656  1.00 34.29           O  
-ATOM   1010  N   ILE A 137      -6.176  39.616   6.165  1.00 19.15           N  
-ATOM   1011  CA  ILE A 137      -5.528  38.301   6.063  1.00 18.06           C  
-ATOM   1012  C   ILE A 137      -5.580  37.892   4.583  1.00 17.43           C  
-ATOM   1013  O   ILE A 137      -4.584  37.526   3.984  1.00 15.40           O  
-ATOM   1014  CB  ILE A 137      -6.264  37.272   6.938  1.00 15.49           C  
-ATOM   1015  CG1 ILE A 137      -6.274  37.670   8.428  1.00 21.21           C  
-ATOM   1016  CG2 ILE A 137      -5.615  35.919   6.718  1.00 15.05           C  
-ATOM   1017  CD1 ILE A 137      -7.029  36.750   9.386  1.00 16.70           C  
-ATOM   1018  N   VAL A 138      -6.775  37.950   3.991  1.00 19.65           N  
-ATOM   1019  CA  VAL A 138      -7.026  37.625   2.585  1.00 18.00           C  
-ATOM   1020  C   VAL A 138      -6.162  38.443   1.650  1.00 16.38           C  
-ATOM   1021  O   VAL A 138      -5.532  37.969   0.695  1.00 18.57           O  
-ATOM   1022  CB  VAL A 138      -8.529  37.857   2.317  1.00 22.16           C  
-ATOM   1023  CG1 VAL A 138      -8.825  38.024   0.823  1.00 21.77           C  
-ATOM   1024  CG2 VAL A 138      -9.312  36.676   2.882  1.00 17.89           C  
-ATOM   1025  N   GLY A 139      -6.064  39.753   1.904  1.00 13.92           N  
-ATOM   1026  CA  GLY A 139      -5.278  40.717   1.161  1.00 12.72           C  
-ATOM   1027  C   GLY A 139      -3.789  40.408   1.298  1.00 19.19           C  
-ATOM   1028  O   GLY A 139      -3.050  40.466   0.296  1.00 16.06           O  
-ATOM   1029  N   TRP A 140      -3.297  40.049   2.498  1.00 14.47           N  
-ATOM   1030  CA  TRP A 140      -1.881  39.706   2.673  1.00 14.92           C  
-ATOM   1031  C   TRP A 140      -1.526  38.423   1.931  1.00 15.71           C  
-ATOM   1032  O   TRP A 140      -0.429  38.308   1.341  1.00 20.26           O  
-ATOM   1033  CB  TRP A 140      -1.660  39.493   4.186  1.00 15.81           C  
-ATOM   1034  CG  TRP A 140      -0.233  39.157   4.551  1.00  7.90           C  
-ATOM   1035  CD1 TRP A 140       0.730  40.076   4.732  1.00  7.50           C  
-ATOM   1036  CD2 TRP A 140       0.360  37.876   4.765  1.00 11.32           C  
-ATOM   1037  NE1 TRP A 140       1.922  39.458   5.032  1.00 13.38           N  
-ATOM   1038  CE2 TRP A 140       1.720  38.092   5.101  1.00 12.90           C  
-ATOM   1039  CE3 TRP A 140      -0.115  36.552   4.742  1.00 15.93           C  
-ATOM   1040  CZ2 TRP A 140       2.627  37.084   5.436  1.00  8.65           C  
-ATOM   1041  CZ3 TRP A 140       0.792  35.529   5.025  1.00 13.46           C  
-ATOM   1042  CH2 TRP A 140       2.133  35.807   5.361  1.00 12.73           C  
-ATOM   1043  N   ALA A 141      -2.399  37.414   1.882  1.00 15.74           N  
-ATOM   1044  CA  ALA A 141      -2.149  36.140   1.210  1.00 15.46           C  
-ATOM   1045  C   ALA A 141      -2.085  36.343  -0.311  1.00 20.91           C  
-ATOM   1046  O   ALA A 141      -1.295  35.738  -1.020  1.00 16.67           O  
-ATOM   1047  CB  ALA A 141      -3.175  35.102   1.628  1.00 14.60           C  
-ATOM   1048  N   HIS A 142      -2.903  37.267  -0.833  1.00 23.29           N  
-ATOM   1049  CA  HIS A 142      -2.920  37.630  -2.256  1.00 25.42           C  
-ATOM   1050  C   HIS A 142      -1.570  38.246  -2.594  1.00 19.26           C  
-ATOM   1051  O   HIS A 142      -0.936  37.884  -3.592  1.00 22.61           O  
-ATOM   1052  CB  HIS A 142      -4.037  38.607  -2.642  1.00 24.24           C  
-ATOM   1053  CG  HIS A 142      -4.055  39.073  -4.071  1.00 34.89           C  
-ATOM   1054  ND1 HIS A 142      -3.681  40.346  -4.477  1.00 35.98           N  
-ATOM   1055  CD2 HIS A 142      -4.441  38.448  -5.217  1.00 42.64           C  
-ATOM   1056  CE1 HIS A 142      -3.842  40.480  -5.777  1.00 37.24           C  
-ATOM   1057  NE2 HIS A 142      -4.293  39.335  -6.259  1.00 45.36           N  
-ATOM   1058  N   ASP A 143      -1.089  39.180  -1.798  1.00 17.79           N  
-ATOM   1059  CA  ASP A 143       0.199  39.826  -2.016  1.00 19.16           C  
-ATOM   1060  C   ASP A 143       1.373  38.862  -1.932  1.00 22.37           C  
-ATOM   1061  O   ASP A 143       2.374  39.054  -2.674  1.00 24.04           O  
-ATOM   1062  CB  ASP A 143       0.368  40.924  -0.971  1.00 18.57           C  
-ATOM   1063  CG  ASP A 143      -0.532  42.127  -1.133  1.00 28.00           C  
-ATOM   1064  OD1 ASP A 143      -1.299  42.262  -2.122  1.00 32.74           O  
-ATOM   1065  OD2 ASP A 143      -0.451  42.964  -0.204  1.00 31.00           O  
-ATOM   1066  N   VAL A 144       1.352  37.852  -1.034  1.00 17.94           N  
-ATOM   1067  CA  VAL A 144       2.497  36.922  -0.975  1.00 17.82           C  
-ATOM   1068  C   VAL A 144       2.609  36.150  -2.293  1.00 16.08           C  
-ATOM   1069  O   VAL A 144       3.721  35.915  -2.748  1.00 18.80           O  
-ATOM   1070  CB  VAL A 144       2.344  35.955   0.235  1.00 15.55           C  
-ATOM   1071  CG1 VAL A 144       3.228  34.755   0.197  1.00 16.39           C  
-ATOM   1072  CG2 VAL A 144       2.608  36.758   1.514  1.00 19.93           C  
-ATOM   1073  N   ARG A 145       1.478  35.741  -2.885  1.00 17.70           N  
-ATOM   1074  CA  ARG A 145       1.342  34.991  -4.133  1.00 18.30           C  
-ATOM   1075  C   ARG A 145       1.965  35.768  -5.304  1.00 18.39           C  
-ATOM   1076  O   ARG A 145       2.695  35.289  -6.157  1.00 18.93           O  
-ATOM   1077  CB  ARG A 145      -0.135  34.709  -4.452  1.00 18.74           C  
-ATOM   1078  CG  ARG A 145      -0.659  33.502  -3.720  1.00 13.62           C  
-ATOM   1079  CD  ARG A 145      -1.971  32.964  -4.273  1.00 15.65           C  
-ATOM   1080  NE  ARG A 145      -3.123  33.785  -4.077  1.00 17.06           N  
-ATOM   1081  CZ  ARG A 145      -3.721  34.586  -4.924  1.00 29.00           C  
-ATOM   1082  NH1 ARG A 145      -3.216  34.714  -6.173  1.00 35.89           N  
-ATOM   1083  NH2 ARG A 145      -4.827  35.209  -4.503  1.00 32.04           N  
-ATOM   1084  N   GLY A 146       1.694  37.065  -5.313  1.00 19.95           N  
-ATOM   1085  CA  GLY A 146       2.213  37.980  -6.297  1.00 26.12           C  
-ATOM   1086  C   GLY A 146       3.681  38.237  -5.964  1.00 30.88           C  
-ATOM   1087  O   GLY A 146       4.379  38.681  -6.884  1.00 34.98           O  
-ATOM   1088  N   ALA A 147       4.194  37.992  -4.761  1.00 29.46           N  
-ATOM   1089  CA  ALA A 147       5.580  38.262  -4.419  1.00 31.03           C  
-ATOM   1090  C   ALA A 147       6.531  37.107  -4.653  1.00 33.11           C  
-ATOM   1091  O   ALA A 147       7.775  37.266  -4.587  1.00 30.96           O  
-ATOM   1092  CB  ALA A 147       5.668  38.683  -2.951  1.00 22.52           C  
-ATOM   1093  N   ILE A 148       5.982  35.905  -4.903  1.00 34.47           N  
-ATOM   1094  CA  ILE A 148       6.875  34.773  -5.123  1.00 38.69           C  
-ATOM   1095  C   ILE A 148       7.278  34.713  -6.599  1.00 48.24           C  
-ATOM   1096  O   ILE A 148       7.875  33.671  -6.973  1.00 56.21           O  
-ATOM   1097  CB  ILE A 148       6.419  33.427  -4.556  1.00 34.61           C  
-ATOM   1098  CG1 ILE A 148       5.201  32.809  -5.268  1.00 35.29           C  
-ATOM   1099  CG2 ILE A 148       6.134  33.510  -3.056  1.00 28.02           C  
-ATOM   1100  CD1 ILE A 148       5.093  31.314  -4.944  1.00 32.89           C  
-ATOM   1101  OXT ILE A 148       7.089  35.629  -7.445  1.00 51.57           O  
-TER    1102      ILE A 148                                                      
-HETATM 1103  S   SO4 A   1      14.843  21.501  -1.857  1.00 41.13           S  
-HETATM 1104  O1  SO4 A   1      14.125  21.916  -0.625  1.00 53.96           O  
-HETATM 1105  O2  SO4 A   1      15.611  22.635  -2.442  1.00 53.97           O  
-HETATM 1106  O3  SO4 A   1      15.655  20.279  -1.543  1.00 55.74           O  
-HETATM 1107  O4  SO4 A   1      13.790  21.107  -2.878  1.00 57.87           O  
-HETATM 1108  S   SO4 A 149     -13.673  29.571  14.301  1.00 69.15           S  
-HETATM 1109  O1  SO4 A 149     -14.332  29.528  15.665  1.00 70.83           O  
-HETATM 1110  O2  SO4 A 149     -13.478  31.031  13.925  1.00 70.06           O  
-HETATM 1111  O3  SO4 A 149     -12.367  28.804  14.363  1.00 67.82           O  
-HETATM 1112  O4  SO4 A 149     -14.500  28.996  13.173  1.00 71.07           O  
-HETATM 1113  N1  FMN A 150       0.574  40.235  22.229  1.00 12.36           N  
-HETATM 1114  C2  FMN A 150       1.607  41.032  21.792  1.00 11.89           C  
-HETATM 1115  O2  FMN A 150       1.465  41.647  20.603  1.00 17.40           O  
-HETATM 1116  N3  FMN A 150       2.721  41.267  22.554  1.00 18.84           N  
-HETATM 1117  C4  FMN A 150       2.889  40.622  23.808  1.00 17.97           C  
-HETATM 1118  O4  FMN A 150       4.049  40.808  24.551  1.00 18.76           O  
-HETATM 1119  C4A FMN A 150       1.844  39.770  24.269  1.00 19.47           C  
-HETATM 1120  N5  FMN A 150       2.003  39.112  25.490  1.00 16.85           N  
-HETATM 1121  C5A FMN A 150       0.882  38.458  26.071  1.00 18.25           C  
-HETATM 1122  C6  FMN A 150       0.945  37.963  27.412  1.00 16.39           C  
-HETATM 1123  C7  FMN A 150      -0.180  37.336  27.988  1.00 19.84           C  
-HETATM 1124  C7M FMN A 150      -0.222  36.801  29.340  1.00 15.19           C  
-HETATM 1125  C8  FMN A 150      -1.337  37.199  27.207  1.00 18.24           C  
-HETATM 1126  C8M FMN A 150      -2.529  36.582  27.701  1.00 14.11           C  
-HETATM 1127  C9  FMN A 150      -1.388  37.693  25.862  1.00 15.61           C  
-HETATM 1128  C9A FMN A 150      -0.278  38.342  25.269  1.00 18.29           C  
-HETATM 1129  N10 FMN A 150      -0.362  38.788  23.914  1.00 18.06           N  
-HETATM 1130  C10 FMN A 150       0.694  39.590  23.467  1.00 12.51           C  
-HETATM 1131  C1' FMN A 150      -1.507  38.669  23.091  1.00 12.62           C  
-HETATM 1132  C2' FMN A 150      -1.629  37.283  22.453  1.00  9.97           C  
-HETATM 1133  O2' FMN A 150      -0.539  37.006  21.577  1.00 15.37           O  
-HETATM 1134  C3' FMN A 150      -2.893  37.307  21.572  1.00 11.36           C  
-HETATM 1135  O3' FMN A 150      -3.989  37.158  22.494  1.00 13.62           O  
-HETATM 1136  C4' FMN A 150      -2.954  36.301  20.474  1.00 11.25           C  
-HETATM 1137  O4' FMN A 150      -4.243  36.514  19.780  1.00 16.71           O  
-HETATM 1138  C5' FMN A 150      -2.895  34.945  20.908  1.00  9.35           C  
-HETATM 1139  O5' FMN A 150      -2.950  34.111  19.788  1.00 12.14           O  
-HETATM 1140  P   FMN A 150      -3.082  32.468  19.750  1.00 11.76           P  
-HETATM 1141  O1P FMN A 150      -2.037  31.661  20.758  1.00 12.93           O  
-HETATM 1142  O2P FMN A 150      -2.791  31.884  18.195  1.00 14.25           O  
-HETATM 1143  O3P FMN A 150      -4.638  32.055  20.139  1.00 11.71           O  
-HETATM 1144  O   HOH A 151       2.604  37.271  17.252  1.00 10.01           O  
-HETATM 1145  O   HOH A 152       7.428  38.078   6.739  1.00 11.50           O  
-HETATM 1146  O   HOH A 153      -2.626  25.019  17.880  1.00 28.64           O  
-HETATM 1147  O   HOH A 154      -4.057  31.825  -9.388  1.00 20.19           O  
-HETATM 1148  O   HOH A 155       9.906  31.811  26.468  1.00 36.90           O  
-HETATM 1149  O   HOH A 156      -9.562  31.341  18.547  1.00 31.31           O  
-HETATM 1150  O   HOH A 157      -0.174  24.629  -8.009  1.00 15.31           O  
-HETATM 1151  O   HOH A 158      15.601  36.301  16.426  1.00 16.32           O  
-HETATM 1152  O   HOH A 159      -8.960  28.078  15.798  1.00 22.73           O  
-HETATM 1153  O   HOH A 160      -8.428  26.066   5.349  1.00 22.39           O  
-HETATM 1154  O   HOH A 161      -0.290  26.279  24.507  1.00 17.91           O  
-HETATM 1155  O   HOH A 162      -4.907  22.604  -2.931  1.00 25.25           O  
-HETATM 1156  O   HOH A 163       6.462  28.150  27.139  1.00 18.70           O  
-HETATM 1157  O   HOH A 164      -5.371  43.715  12.902  1.00 19.82           O  
-HETATM 1158  O   HOH A 165     -10.077  25.600  -2.076  1.00 23.56           O  
-HETATM 1159  O   HOH A 166       3.225  23.228  -7.640  1.00 24.37           O  
-HETATM 1160  O   HOH A 167       2.044  29.673  24.522  1.00 11.11           O  
-HETATM 1161  O   HOH A 168      -1.141  19.177  12.274  1.00 21.98           O  
-HETATM 1162  O   HOH A 169      10.093  41.741   2.617  1.00 39.23           O  
-HETATM 1163  O   HOH A 170     -10.258  32.847  -2.237  1.00 26.15           O  
-HETATM 1164  O   HOH A 171      -4.748  38.958  19.003  1.00 15.52           O  
-HETATM 1165  O   HOH A 172      -8.104  45.950  16.978  1.00 32.44           O  
-HETATM 1166  O   HOH A 173       3.116  41.858  27.252  1.00 21.06           O  
-HETATM 1167  O   HOH A 174      -7.880  24.815   2.729  1.00 25.60           O  
-HETATM 1168  O   HOH A 175       3.413  17.138  10.881  1.00 38.47           O  
-HETATM 1169  O   HOH A 176       9.223  39.917  -3.082  1.00 46.63           O  
-HETATM 1170  O   HOH A 177       7.503  37.834  30.845  1.00 23.89           O  
-HETATM 1171  O   HOH A 178      -9.903  32.219   2.933  1.00 24.34           O  
-HETATM 1172  O   HOH A 179      17.794  26.628   7.822  1.00 26.45           O  
-HETATM 1173  O   HOH A 180      19.689  25.923   5.089  1.00 33.18           O  
-HETATM 1174  O   HOH A 181       0.332  43.653   9.179  1.00 26.85           O  
-HETATM 1175  O   HOH A 182     -15.095  37.069   9.968  1.00 25.35           O  
-HETATM 1176  O   HOH A 183      -5.034  26.264  18.347  1.00 19.47           O  
-HETATM 1177  O   HOH A 184       0.065  25.267  18.376  1.00 15.17           O  
-HETATM 1178  O   HOH A 185       4.939  43.423  24.722  1.00 21.09           O  
-HETATM 1179  O   HOH A 186      -4.754  24.838   8.821  1.00 37.67           O  
-HETATM 1180  O   HOH A 187     -12.110  42.192   7.538  1.00 25.50           O  
-HETATM 1181  O   HOH A 188       3.684  25.918  -9.905  1.00 16.31           O  
-HETATM 1182  O   HOH A 189       2.175  32.830  -7.173  1.00 26.37           O  
-HETATM 1183  O   HOH A 190      -5.748  24.051   2.242  1.00 19.96           O  
-HETATM 1184  O   HOH A 191      -4.187  21.647  15.597  1.00 35.34           O  
-HETATM 1185  O   HOH A 192      11.854  28.764  -2.180  1.00 20.87           O  
-HETATM 1186  O   HOH A 193      19.135  23.943   6.878  1.00 28.98           O  
-HETATM 1187  O   HOH A 194      11.414  41.874  11.608  1.00 31.65           O  
-HETATM 1188  O   HOH A 195      -5.570  35.207  24.035  1.00 33.39           O  
-HETATM 1189  O   HOH A 196       6.668  34.016  31.573  1.00 20.62           O  
-HETATM 1190  O   HOH A 197      10.332  32.425  23.560  1.00 25.82           O  
-HETATM 1191  O   HOH A 198      -2.901  24.620  21.387  1.00 37.02           O  
-HETATM 1192  O   HOH A 199     -11.724  39.748   0.979  1.00 40.17           O  
-HETATM 1193  O   HOH A 200      -1.853  21.685  19.282  1.00 28.58           O  
-HETATM 1194  O   HOH A 201     -15.169  37.634  16.290  1.00 33.82           O  
-HETATM 1195  O   HOH A 202       8.036  22.676  17.023  1.00 36.57           O  
-HETATM 1196  O   HOH A 203      -4.318  34.619  -1.936  1.00 28.46           O  
-HETATM 1197  O   HOH A 204      -5.590  22.358  -0.067  1.00 26.16           O  
-HETATM 1198  O   HOH A 205       1.825  46.323  11.114  1.00 42.33           O  
-HETATM 1199  O   HOH A 206       4.103  18.347  21.240  1.00 43.87           O  
-HETATM 1200  O   HOH A 207      -3.041  43.884   1.848  1.00 43.55           O  
-HETATM 1201  O   HOH A 208      -8.821  42.177  14.343  1.00 26.52           O  
-HETATM 1202  O   HOH A 209      -3.843  20.893   4.678  1.00 51.40           O  
-HETATM 1203  O   HOH A 210       8.851  26.131  26.621  1.00 34.93           O  
-HETATM 1204  O   HOH A 211      13.278  31.298  22.506  1.00 34.49           O  
-HETATM 1205  O   HOH A 212      18.531  36.652   4.089  1.00 35.46           O  
-HETATM 1206  O   HOH A 213      -6.455  25.977  20.596  1.00 30.77           O  
-HETATM 1207  O   HOH A 214     -10.315  27.647  13.976  1.00 29.51           O  
-HETATM 1208  O   HOH A 215       6.179  23.301  -7.491  1.00 25.69           O  
-HETATM 1209  O   HOH A 216      18.278  25.268   1.535  1.00 27.53           O  
-HETATM 1210  O   HOH A 217       8.236  42.911   8.797  1.00 36.22           O  
-HETATM 1211  O   HOH A 218      -6.965  24.027  -4.791  1.00 18.13           O  
-HETATM 1212  O   HOH A 219      -0.283  21.263  21.630  1.00 38.49           O  
-HETATM 1213  O   HOH A 220      -3.795  32.685  28.060  1.00 21.25           O  
-HETATM 1214  O   HOH A 221       2.374  21.552  -0.472  1.00 25.32           O  
-HETATM 1215  O   HOH A 222     -11.400  28.719   9.563  1.00 30.69           O  
-HETATM 1216  O   HOH A 223      -5.593  34.150  26.758  1.00 17.70           O  
-HETATM 1217  O   HOH A 224     -13.592  40.233   9.201  1.00 23.47           O  
-HETATM 1218  O   HOH A 225       6.176  40.159  25.455  1.00 24.96           O  
-HETATM 1219  O   HOH A 226      10.831  17.265   8.925  1.00 33.82           O  
-HETATM 1220  O   HOH A 227     -11.121  30.451   7.752  1.00 34.18           O  
-HETATM 1221  O   HOH A 228      -3.102  35.492  31.635  1.00 28.51           O  
-HETATM 1222  O   HOH A 229      15.714  44.417  14.899  1.00 48.82           O  
-HETATM 1223  O   HOH A 230      14.968  32.280  -3.033  1.00 38.82           O  
-HETATM 1224  O   HOH A 231       9.912  18.396   3.623  1.00 35.18           O  
-HETATM 1225  O   HOH A 232     -12.879  44.775   1.727  1.00 48.14           O  
-HETATM 1226  O   HOH A 233      -2.896  47.827  27.319  1.00 34.47           O  
-HETATM 1227  O   HOH A 234       1.964  15.686   4.464  1.00 62.24           O  
-HETATM 1228  O   HOH A 235       3.102  41.112  -4.187  1.00 28.16           O  
-HETATM 1229  O   HOH A 236       6.586  17.230  10.306  1.00 38.14           O  
-HETATM 1230  O   HOH A 237      12.505  24.940  -3.743  1.00 43.27           O  
-HETATM 1231  O   HOH A 238      -4.653  43.326  10.299  1.00 24.97           O  
-HETATM 1232  O   HOH A 239       4.840  21.364  21.901  1.00 31.62           O  
-HETATM 1233  O   HOH A 240      10.937  46.328  27.984  1.00 51.22           O  
-HETATM 1234  O   HOH A 241      -6.395  23.983   6.586  1.00 36.32           O  
-HETATM 1235  O   HOH A 242       0.164  19.025  -0.157  1.00 43.99           O  
-HETATM 1236  O   HOH A 243       2.888  18.627  -8.700  1.00 43.64           O  
-HETATM 1237  O   HOH A 244      20.179  40.050  13.748  1.00 16.19           O  
-HETATM 1238  O   HOH A 245      -3.722  43.522  29.631  1.00 53.05           O  
-HETATM 1239  O   HOH A 246      -9.677  24.672   0.665  1.00 30.51           O  
-HETATM 1240  O   HOH A 247       5.123  21.835  26.103  1.00 40.22           O  
-HETATM 1241  O   HOH A 248     -13.764  44.502  11.355  1.00 48.34           O  
-HETATM 1242  O   HOH A 249      -5.101  29.026  27.743  1.00 39.66           O  
-HETATM 1243  O   HOH A 250      -3.164  43.093   4.504  1.00 30.97           O  
-HETATM 1244  O   HOH A 251       8.344  24.656  24.352  1.00 31.39           O  
-HETATM 1245  O   HOH A 252      -4.175  26.258  26.742  1.00 23.25           O  
-HETATM 1246  O   HOH A 253      20.118  34.367  14.094  1.00 23.35           O  
-HETATM 1247  O   HOH A 254     -13.382  27.407  -2.968  1.00 28.08           O  
-HETATM 1248  O   HOH A 255      -2.882  20.083  -2.148  1.00 32.66           O  
-HETATM 1249  O   HOH A 256       1.173  43.389   6.512  1.00 42.61           O  
-HETATM 1250  O   HOH A 257      -5.341  46.370  21.809  1.00 34.47           O  
-HETATM 1251  O   HOH A 258       3.397  17.785   1.046  1.00 29.38           O  
-HETATM 1252  O   HOH A 259       1.643  21.098  -6.716  1.00 30.37           O  
-HETATM 1253  O   HOH A 260     -14.059  37.068   3.421  1.00 33.35           O  
-HETATM 1254  O   HOH A 261      -4.245  22.230  -6.952  1.00 31.36           O  
-HETATM 1255  O   HOH A 262       8.757  40.259  32.188  1.00 33.12           O  
-HETATM 1256  O   HOH A 263      -8.070  21.871  -0.920  1.00 48.03           O  
-HETATM 1257  O   HOH A 264      -5.920  23.784  11.367  1.00 33.41           O  
-HETATM 1258  O   HOH A 265       2.209  23.046  24.177  1.00 44.33           O  
-HETATM 1259  O   HOH A 266       1.460  48.935  17.460  1.00 45.76           O  
-HETATM 1260  O   HOH A 267       6.557  21.649  19.871  1.00 31.69           O  
-HETATM 1261  O   HOH A 268      -2.845  21.144  22.971  1.00 43.45           O  
-HETATM 1262  O   HOH A 269      -0.785  39.128  -6.192  1.00 37.59           O  
-HETATM 1263  O   HOH A 270     -10.413  28.229  18.332  1.00 27.50           O  
-HETATM 1264  O   HOH A 271       3.032  23.120 -10.551  1.00 40.15           O  
-HETATM 1265  O   HOH A 272      12.135  20.471  16.706  1.00 37.92           O  
-HETATM 1266  O   HOH A 273      10.339  36.282  -5.062  1.00 36.17           O  
-HETATM 1267  O   HOH A 274     -11.499  31.071   4.672  1.00 39.81           O  
-HETATM 1268  O   HOH A 275     -10.522  36.780  -2.339  1.00 38.67           O  
-HETATM 1269  O   HOH A 276      14.857  39.154   2.471  1.00 35.96           O  
-HETATM 1270  O   HOH A 277       2.419  47.110  27.534  1.00 51.20           O  
-HETATM 1271  O   HOH A 278       1.320  41.278  29.822  1.00 49.19           O  
-HETATM 1272  O   HOH A 279     -11.957  26.535   4.895  1.00 40.89           O  
-HETATM 1273  O   HOH A 280      -5.154  48.978  20.866  1.00 42.04           O  
-HETATM 1274  O   HOH A 281       4.452  35.447  -7.965  1.00 42.86           O  
-HETATM 1275  O   HOH A 282     -12.985  30.947  -0.293  1.00 35.31           O  
-HETATM 1276  O   HOH A 283      17.326  29.481  19.620  1.00 36.22           O  
-HETATM 1277  O   HOH A 284      17.670  34.535  16.077  1.00 27.51           O  
-HETATM 1278  O   HOH A 285     -17.088  27.276   2.082  1.00 37.88           O  
-HETATM 1279  O   HOH A 286      -4.367  43.261  -1.362  1.00 44.23           O  
-HETATM 1280  O   HOH A 287      -7.646  44.265  12.937  1.00 45.19           O  
-HETATM 1281  O   HOH A 288      12.007  39.264  -2.152  1.00 42.79           O  
-HETATM 1282  O   HOH A 289      11.254  48.090  24.681  1.00 37.59           O  
-HETATM 1283  O   HOH A 290      13.359  43.105  14.904  1.00 75.59           O  
-HETATM 1284  O   HOH A 291      17.690  32.760  20.712  1.00 39.32           O  
-HETATM 1285  O   HOH A 292      -0.469  18.461  16.126  1.00 49.34           O  
-HETATM 1286  O   HOH A 293       0.549  42.760   2.238  1.00 31.82           O  
-HETATM 1287  O   HOH A 294      15.472  18.344  15.806  1.00 47.09           O  
-HETATM 1288  O   HOH A 295      -1.200  37.695  -8.216  1.00 45.29           O  
-HETATM 1289  O   HOH A 296      -6.904  38.983  -8.209  1.00 48.06           O  
-HETATM 1290  O   HOH A 297      -6.288  46.331  14.117  1.00 38.63           O  
-HETATM 1291  O   HOH A 298      -2.485  44.219   9.183  1.00 38.39           O  
-HETATM 1292  O   HOH A 299      10.402  22.790  -5.240  1.00 52.71           O  
-HETATM 1293  O   HOH A 300      -0.562  40.740  28.446  1.00 45.87           O  
-HETATM 1294  O   HOH A 301     -15.510  44.771   2.782  1.00 43.38           O  
-HETATM 1295  O   HOH A 302      19.536  28.133  16.273  1.00 49.65           O  
-HETATM 1296  O   HOH A 303       5.393  43.208   9.828  1.00 40.07           O  
-HETATM 1297  O   HOH A 304       9.315  44.036  18.605  1.00 51.47           O  
-HETATM 1298  O   HOH A 305       7.981  18.092   0.433  1.00 49.66           O  
-CONECT 1103 1104 1105 1106 1107                                                 
-CONECT 1104 1103                                                                
-CONECT 1105 1103                                                                
-CONECT 1106 1103                                                                
-CONECT 1107 1103                                                                
-CONECT 1108 1109 1110 1111 1112                                                 
-CONECT 1109 1108                                                                
-CONECT 1110 1108                                                                
-CONECT 1111 1108                                                                
-CONECT 1112 1108                                                                
-CONECT 1113 1114 1130                                                           
-CONECT 1114 1113 1115 1116                                                      
-CONECT 1115 1114                                                                
-CONECT 1116 1114 1117                                                           
-CONECT 1117 1116 1118 1119                                                      
-CONECT 1118 1117                                                                
-CONECT 1119 1117 1120 1130                                                      
-CONECT 1120 1119 1121                                                           
-CONECT 1121 1120 1122 1128                                                      
-CONECT 1122 1121 1123                                                           
-CONECT 1123 1122 1124 1125                                                      
-CONECT 1124 1123                                                                
-CONECT 1125 1123 1126 1127                                                      
-CONECT 1126 1125                                                                
-CONECT 1127 1125 1128                                                           
-CONECT 1128 1121 1127 1129                                                      
-CONECT 1129 1128 1130 1131                                                      
-CONECT 1130 1113 1119 1129                                                      
-CONECT 1131 1129 1132                                                           
-CONECT 1132 1131 1133 1134                                                      
-CONECT 1133 1132                                                                
-CONECT 1134 1132 1135 1136                                                      
-CONECT 1135 1134                                                                
-CONECT 1136 1134 1137 1138                                                      
-CONECT 1137 1136                                                                
-CONECT 1138 1136 1139                                                           
-CONECT 1139 1138 1140                                                           
-CONECT 1140 1139 1141 1142 1143                                                 
-CONECT 1141 1140                                                                
-CONECT 1142 1140                                                                
-CONECT 1143 1140                                                                
-MASTER      340    0    3    6    5    0    9    6 1297    1   41   12          
-END                                                                             
diff --git a/plip/test/pdb/1ay8.pdb b/plip/test/pdb/1ay8.pdb
deleted file mode 100644
index 87fe3a4..0000000
--- a/plip/test/pdb/1ay8.pdb
+++ /dev/null
@@ -1,6838 +0,0 @@
-HEADER    TRANSFERASE                             14-NOV-97   1AY8              
-TITLE     AROMATIC AMINO ACID AMINOTRANSFERASE COMPLEX WITH 3-PHENYLPROPIONATE  
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: AROMATIC AMINO ACID AMINOTRANSFERASE;                      
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 SYNONYM: AROAT;                                                      
-COMPND   5 EC: 2.6.1.57;                                                        
-COMPND   6 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;                       
-SOURCE   3 ORGANISM_TAXID: 266;                                                 
-SOURCE   4 STRAIN: IFO12442;                                                    
-SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   7 EXPRESSION_SYSTEM_STRAIN: TY103;                                     
-SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PUC118                                    
-KEYWDS    TRANSFERASE, AMINOTRANSFERASE                                         
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    A.OKAMOTO,K.HIROTSU,H.KAGAMIYAMA                                      
-REVDAT   4   13-JUL-11 1AY8    1       VERSN                                    
-REVDAT   3   24-FEB-09 1AY8    1       VERSN                                    
-REVDAT   2   18-NOV-98 1AY8    3       ATOM   REMARK HETATM KEYWDS              
-REVDAT   2 2                   3       HEADER MODRES                            
-REVDAT   1   14-OCT-98 1AY8    0                                                
-JRNL        AUTH   A.OKAMOTO,Y.NAKAI,H.HAYASHI,K.HIROTSU,H.KAGAMIYAMA           
-JRNL        TITL   CRYSTAL STRUCTURES OF PARACOCCUS DENITRIFICANS AROMATIC      
-JRNL        TITL 2 AMINO ACID AMINOTRANSFERASE: A SUBSTRATE RECOGNITION SITE    
-JRNL        TITL 3 CONSTRUCTED BY REARRANGEMENT OF HYDROGEN BOND NETWORK.       
-JRNL        REF    J.MOL.BIOL.                   V. 280   443 1998              
-JRNL        REFN                   ISSN 0022-2836                               
-JRNL        PMID   9665848                                                      
-JRNL        DOI    10.1006/JMBI.1998.1869                                       
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   S.OUE,A.OKAMOTO,Y.NAKAI,M.NAKAHIRA,T.SHIBATANI,H.HAYASHI,    
-REMARK   1  AUTH 2 H.KAGAMIYAMA                                                 
-REMARK   1  TITL   PARACOCCUS DENITRIFICANS AROMATIC AMINO ACID                 
-REMARK   1  TITL 2 AMINOTRANSFERASE: A MODEL ENZYME FOR THE STUDY OF DUAL       
-REMARK   1  TITL 3 SUBSTRATE RECOGNITION MECHANISM                              
-REMARK   1  REF    J.BIOCHEM.(TOKYO)             V. 121   161 1997              
-REMARK   1  REFN                   ISSN 0021-924X                               
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : X-PLOR 3.1                                           
-REMARK   3   AUTHORS     : BRUNGER                                              
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.6                           
-REMARK   3   NUMBER OF REFLECTIONS             : 33456                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.181                           
-REMARK   3   FREE R VALUE                     : 0.239                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
-REMARK   3   FREE R VALUE TEST SET COUNT      : 3335                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.60                        
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4681                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
-REMARK   3   BIN FREE R VALUE                    : 0.2750                       
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 526                          
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 5941                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 41                                      
-REMARK   3   SOLVENT ATOMS            : 328                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 18.80                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.20                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.27                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.006                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.17                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.900 ; 1.500                
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.580 ; 2.000                
-REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.470 ; 2.000                
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.320 ; 2.500                
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
-REMARK   3  PARAMETER FILE  2  : PARAM11.WAT                                    
-REMARK   3  PARAMETER FILE  3  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
-REMARK   3  TOPOLOGY FILE  2   : TOPH11.WAT                                     
-REMARK   3  TOPOLOGY FILE  3   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1AY8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-96                          
-REMARK 200  TEMPERATURE           (KELVIN) : 293                                
-REMARK 200  PH                             : 5.6                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : N                                  
-REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
-REMARK 200  MONOCHROMATOR                  : NI FILTER                          
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
-REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS (RIGAKU)                   
-REMARK 200  DATA SCALING SOFTWARE          : PROCESS (RIGAKU)                   
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35751                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 123.000                            
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
-REMARK 200  DATA REDUNDANCY                : 3.400                              
-REMARK 200  R MERGE                    (I) : 0.06080                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.14000                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.200                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
-REMARK 200 STARTING MODEL: 1ART                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 48.80                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 18.0%      
-REMARK 280  PEG 4000, 0.2 M SODIUM MALEATE, PH 5.6; THEN SOAKED IN 20.0% PEG    
-REMARK 280  4000, 0.2 M SODIUM CITRATE, 0.1 M 3-PHENYLPROPIONATE, PH 5.6        
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       62.11500            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       27.63500            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.90500            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       27.63500            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       62.11500            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.90500            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 8450 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 28660 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     ARG B    25                                                      
-REMARK 465     ALA B    26                                                      
-REMARK 465     ASP B    27                                                      
-REMARK 465     PRO B    28                                                      
-REMARK 465     ARG B    29                                                      
-REMARK 465     GLN B    30                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    LEU A   6       -9.39    -58.08                                   
-REMARK 500    LYS A  16      -24.66    110.89                                   
-REMARK 500    ASP A  42     -168.80    -79.93                                   
-REMARK 500    ALA A  71     -142.06   -113.25                                   
-REMARK 500    TYR A 160      -60.27   -150.32                                   
-REMARK 500    CYS A 192       63.51     39.10                                   
-REMARK 500    ARG A 266       66.90     66.23                                   
-REMARK 500    TYR A 295       22.11   -164.41                                   
-REMARK 500    SER A 296      -87.35     64.23                                   
-REMARK 500    ALA B  71     -138.12   -118.74                                   
-REMARK 500    TYR B 160      -58.41   -144.19                                   
-REMARK 500    ARG B 266       75.23     64.17                                   
-REMARK 500    TYR B 295       14.34   -159.85                                   
-REMARK 500    SER B 296     -118.06     71.61                                   
-REMARK 500    SER B 361      134.56   -170.04                                   
-REMARK 500    LEU B 363      -73.21    -76.20                                   
-REMARK 500    GLU B 376      -39.18   -134.51                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH B 519        DISTANCE =  9.05 ANGSTROMS                       
-REMARK 525    HOH B 527        DISTANCE =  6.23 ANGSTROMS                       
-REMARK 525    HOH B 543        DISTANCE =  7.66 ANGSTROMS                       
-REMARK 525    HOH B 545        DISTANCE =  5.07 ANGSTROMS                       
-REMARK 525    HOH B 547        DISTANCE =  8.48 ANGSTROMS                       
-REMARK 525    HOH B 552        DISTANCE =  5.06 ANGSTROMS                       
-REMARK 525    HOH B 568        DISTANCE =  5.62 ANGSTROMS                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 413                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 413                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HCI B 414                 
-DBREF  1AY8 A    5   409  UNP    P95468   TYRB_PARDE       1    394             
-DBREF  1AY8 B    5   409  UNP    P95468   TYRB_PARDE       1    394             
-SEQRES   1 A  394  MET LEU GLY ASN LEU LYS PRO GLN ALA PRO ASP LYS ILE          
-SEQRES   2 A  394  LEU ALA LEU MET GLY GLU PHE ARG ALA ASP PRO ARG GLN          
-SEQRES   3 A  394  GLY LYS ILE ASP LEU GLY VAL GLY VAL TYR LYS ASP ALA          
-SEQRES   4 A  394  THR GLY HIS THR PRO ILE MET ARG ALA VAL HIS ALA ALA          
-SEQRES   5 A  394  GLU GLN ARG MET LEU GLU THR GLU THR THR LYS THR TYR          
-SEQRES   6 A  394  ALA GLY LEU SER GLY GLU PRO GLU PHE GLN LYS ALA MET          
-SEQRES   7 A  394  GLY GLU LEU ILE LEU GLY ASP GLY LEU LYS SER GLU THR          
-SEQRES   8 A  394  THR ALA THR LEU ALA THR VAL GLY GLY THR GLY ALA LEU          
-SEQRES   9 A  394  ARG GLN ALA LEU GLU LEU ALA ARG MET ALA ASN PRO ASP          
-SEQRES  10 A  394  LEU ARG VAL PHE VAL SER ASP PRO THR TRP PRO ASN HIS          
-SEQRES  11 A  394  VAL SER ILE MET ASN PHE MET GLY LEU PRO VAL GLN THR          
-SEQRES  12 A  394  TYR ARG TYR PHE ASP ALA GLU THR ARG GLY VAL ASP PHE          
-SEQRES  13 A  394  GLU GLY MET LYS ALA ASP LEU ALA ALA ALA LYS LYS GLY          
-SEQRES  14 A  394  ASP MET VAL LEU LEU HIS GLY CYS CYS HIS ASN PRO THR          
-SEQRES  15 A  394  GLY ALA ASN LEU THR LEU ASP GLN TRP ALA GLU ILE ALA          
-SEQRES  16 A  394  SER ILE LEU GLU LYS THR GLY ALA LEU PRO LEU ILE ASP          
-SEQRES  17 A  394  LEU ALA TYR GLN GLY PHE GLY ASP GLY LEU GLU GLU ASP          
-SEQRES  18 A  394  ALA ALA GLY THR ARG LEU ILE ALA SER ARG ILE PRO GLU          
-SEQRES  19 A  394  VAL LEU ILE ALA ALA SER CYS SER LYS ASN PHE GLY ILE          
-SEQRES  20 A  394  TYR ARG GLU ARG THR GLY CYS LEU LEU ALA LEU CYS ALA          
-SEQRES  21 A  394  ASP ALA ALA THR ARG GLU LEU ALA GLN GLY ALA MET ALA          
-SEQRES  22 A  394  PHE LEU ASN ARG GLN THR TYR SER PHE PRO PRO PHE HIS          
-SEQRES  23 A  394  GLY ALA LYS ILE VAL SER THR VAL LEU THR THR PRO GLU          
-SEQRES  24 A  394  LEU ARG ALA ASP TRP MET ALA GLU LEU GLU ALA VAL ARG          
-SEQRES  25 A  394  SER GLY MET LEU ARG LEU ARG GLU GLN LEU ALA GLY GLU          
-SEQRES  26 A  394  LEU ARG ASP LEU SER GLY SER ASP ARG PHE GLY PHE VAL          
-SEQRES  27 A  394  ALA GLU HIS ARG GLY MET PHE SER ARG LEU GLY ALA THR          
-SEQRES  28 A  394  PRO GLU GLN VAL LYS ARG ILE LYS GLU GLU PHE GLY ILE          
-SEQRES  29 A  394  TYR MET VAL GLY ASP SER ARG ILE ASN ILE ALA GLY LEU          
-SEQRES  30 A  394  ASN ASP ASN THR ILE PRO ILE LEU ALA ARG ALA ILE ILE          
-SEQRES  31 A  394  GLU VAL GLY VAL                                              
-SEQRES   1 B  394  MET LEU GLY ASN LEU LYS PRO GLN ALA PRO ASP LYS ILE          
-SEQRES   2 B  394  LEU ALA LEU MET GLY GLU PHE ARG ALA ASP PRO ARG GLN          
-SEQRES   3 B  394  GLY LYS ILE ASP LEU GLY VAL GLY VAL TYR LYS ASP ALA          
-SEQRES   4 B  394  THR GLY HIS THR PRO ILE MET ARG ALA VAL HIS ALA ALA          
-SEQRES   5 B  394  GLU GLN ARG MET LEU GLU THR GLU THR THR LYS THR TYR          
-SEQRES   6 B  394  ALA GLY LEU SER GLY GLU PRO GLU PHE GLN LYS ALA MET          
-SEQRES   7 B  394  GLY GLU LEU ILE LEU GLY ASP GLY LEU LYS SER GLU THR          
-SEQRES   8 B  394  THR ALA THR LEU ALA THR VAL GLY GLY THR GLY ALA LEU          
-SEQRES   9 B  394  ARG GLN ALA LEU GLU LEU ALA ARG MET ALA ASN PRO ASP          
-SEQRES  10 B  394  LEU ARG VAL PHE VAL SER ASP PRO THR TRP PRO ASN HIS          
-SEQRES  11 B  394  VAL SER ILE MET ASN PHE MET GLY LEU PRO VAL GLN THR          
-SEQRES  12 B  394  TYR ARG TYR PHE ASP ALA GLU THR ARG GLY VAL ASP PHE          
-SEQRES  13 B  394  GLU GLY MET LYS ALA ASP LEU ALA ALA ALA LYS LYS GLY          
-SEQRES  14 B  394  ASP MET VAL LEU LEU HIS GLY CYS CYS HIS ASN PRO THR          
-SEQRES  15 B  394  GLY ALA ASN LEU THR LEU ASP GLN TRP ALA GLU ILE ALA          
-SEQRES  16 B  394  SER ILE LEU GLU LYS THR GLY ALA LEU PRO LEU ILE ASP          
-SEQRES  17 B  394  LEU ALA TYR GLN GLY PHE GLY ASP GLY LEU GLU GLU ASP          
-SEQRES  18 B  394  ALA ALA GLY THR ARG LEU ILE ALA SER ARG ILE PRO GLU          
-SEQRES  19 B  394  VAL LEU ILE ALA ALA SER CYS SER LYS ASN PHE GLY ILE          
-SEQRES  20 B  394  TYR ARG GLU ARG THR GLY CYS LEU LEU ALA LEU CYS ALA          
-SEQRES  21 B  394  ASP ALA ALA THR ARG GLU LEU ALA GLN GLY ALA MET ALA          
-SEQRES  22 B  394  PHE LEU ASN ARG GLN THR TYR SER PHE PRO PRO PHE HIS          
-SEQRES  23 B  394  GLY ALA LYS ILE VAL SER THR VAL LEU THR THR PRO GLU          
-SEQRES  24 B  394  LEU ARG ALA ASP TRP MET ALA GLU LEU GLU ALA VAL ARG          
-SEQRES  25 B  394  SER GLY MET LEU ARG LEU ARG GLU GLN LEU ALA GLY GLU          
-SEQRES  26 B  394  LEU ARG ASP LEU SER GLY SER ASP ARG PHE GLY PHE VAL          
-SEQRES  27 B  394  ALA GLU HIS ARG GLY MET PHE SER ARG LEU GLY ALA THR          
-SEQRES  28 B  394  PRO GLU GLN VAL LYS ARG ILE LYS GLU GLU PHE GLY ILE          
-SEQRES  29 B  394  TYR MET VAL GLY ASP SER ARG ILE ASN ILE ALA GLY LEU          
-SEQRES  30 B  394  ASN ASP ASN THR ILE PRO ILE LEU ALA ARG ALA ILE ILE          
-SEQRES  31 B  394  GLU VAL GLY VAL                                              
-HET    PLP  A 413      15                                                       
-HET    PLP  B 413      15                                                       
-HET    HCI  B 414      11                                                       
-HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
-HETNAM     HCI HYDROCINNAMIC ACID                                               
-HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
-HETSYN     HCI 3PP; 3-PHENYLPROPIONIC ACID                                      
-FORMUL   3  PLP    2(C8 H10 N O6 P)                                             
-FORMUL   5  HCI    C9 H10 O2                                                    
-FORMUL   6  HOH   *328(H2 O)                                                    
-HELIX    1  1A ILE A   17  ALA A   26  1                                  10    
-HELIX    2  2A ARG A   51  THR A   63  1                                  13    
-HELIX    3  3A PRO A   77  LEU A   88  1                                  12    
-HELIX    4  5A GLY A  107  ALA A  122  1                                  16    
-HELIX    5  6A PRO A  141  MET A  150  1                                  10    
-HELIX    6  7A PHE A  170  LEU A  177  1                                   8    
-HELIX    7  8A LEU A  202  THR A  215  1                                  14    
-HELIX    8  9A LEU A  233  ARG A  246  1                                  14    
-HELIX    9 11A ALA A  277  TYR A  295  1                                  19    
-HELIX   10 12A HIS A  301  THR A  311  1                                  11    
-HELIX   11 13A PRO A  313  SER A  345  1                                  33    
-HELIX   12 14A PHE A  352  GLU A  355  1                                   4    
-HELIX   13 15A PRO A  367  PHE A  377  1                                  11    
-HELIX   14 16A ILE A  397  GLU A  406  1                                  10    
-HELIX   15  1B ILE B   17  GLU B   23  1                                   7    
-HELIX   16  2B ARG B   51  THR B   63  1                                  13    
-HELIX   17  3B PRO B   77  LEU B   88  1                                  12    
-HELIX   18  5B GLY B  107  ALA B  122  1                                  16    
-HELIX   19  6B PRO B  141  MET B  150  1                                  10    
-HELIX   20  7B PHE B  170  ALA B  178  1                                   9    
-HELIX   21  8B LEU B  202  THR B  215  1                                  14    
-HELIX   22  9B LEU B  233  ARG B  246  1                                  14    
-HELIX   23 11B ALA B  277  THR B  294  1                                  18    
-HELIX   24 12B HIS B  301  THR B  311  1                                  11    
-HELIX   25 13B PRO B  313  SER B  345  1                                  33    
-HELIX   26 14B PHE B  352  GLU B  355  1                                   4    
-HELIX   27 15B PRO B  367  PHE B  377  1                                  11    
-HELIX   28 16B THR B  396  GLU B  406  1                                  11    
-SHEET    1  AA 2 ILE A  33  ASP A  34  0                                        
-SHEET    2  AA 2 ILE A 379  TYR A 380  1  N  TYR A 380   O  ILE A  33           
-SHEET    1  AB 7 THR A 100  VAL A 106  0                                        
-SHEET    2  AB 7 THR A 267  LEU A 273 -1  O  ALA A 272   N  ALA A 101           
-SHEET    3  AB 7 VAL A 250  SER A 255 -1  N  VAL A 250   O  LEU A 273           
-SHEET    4  AB 7 LEU A 218  LEU A 223  1  O  PRO A 219   N  LEU A 251           
-SHEET    5  AB 7 MET A 185  HIS A 189  1  N  VAL A 186   O  LEU A 218           
-SHEET    6  AB 7 VAL A 133  ASP A 137  1  N  PHE A 134   O  MET A 185           
-SHEET    7  AB 7 VAL A 155  ARG A 159  1  N  GLN A 156   O  VAL A 133           
-SHEET    1  AC 2 PHE A 161  ASP A 162  0                                        
-SHEET    2  AC 2 GLY A 167  VAL A 168 -1  O  GLY A 167   N  ASP A 162           
-SHEET    1  AD 2 PHE A 360  ARG A 362  0                                        
-SHEET    2  AD 2 ARG A 386  ASN A 388 -1  O  ILE A 387   N  SER A 361           
-SHEET    1  BA 2 ILE B  33  ASP B  34  0                                        
-SHEET    2  BA 2 ILE B 379  TYR B 380  1  N  TYR B 380   O  ILE B  33           
-SHEET    1  BB 7 THR B 100  THR B 105  0                                        
-SHEET    2  BB 7 GLY B 268  LEU B 273 -1  O  ALA B 272   N  ALA B 101           
-SHEET    3  BB 7 VAL B 250  SER B 255 -1  N  VAL B 250   O  LEU B 273           
-SHEET    4  BB 7 LEU B 218  LEU B 223  1  O  PRO B 219   N  LEU B 251           
-SHEET    5  BB 7 MET B 185  HIS B 189  1  N  VAL B 186   O  LEU B 218           
-SHEET    6  BB 7 VAL B 133  ASP B 137  1  N  PHE B 134   O  MET B 185           
-SHEET    7  BB 7 VAL B 155  ARG B 159  1  N  GLN B 156   O  VAL B 133           
-SHEET    1  BC 2 PHE B 161  ASP B 162  0                                        
-SHEET    2  BC 2 GLY B 167  VAL B 168 -1  O  GLY B 167   N  ASP B 162           
-SHEET    1  BD 2 PHE B 360  ARG B 362  0                                        
-SHEET    2  BD 2 ARG B 386  ASN B 388 -1  O  ILE B 387   N  SER B 361           
-LINK         C4A PLP A 413                 NZ  LYS A 258     1555   1555  1.35  
-LINK         C4A PLP B 413                 NZ  LYS B 258     1555   1555  1.37  
-CISPEP   1 ASP A  137    PRO A  138          0         0.11                     
-CISPEP   2 ASN A  194    PRO A  195          0         0.73                     
-CISPEP   3 ASP B  137    PRO B  138          0         0.32                     
-CISPEP   4 ASN B  194    PRO B  195          0         0.37                     
-SITE     1 AC1 12 GLY A 107  GLY A 108  THR A 109  TRP A 140                    
-SITE     2 AC1 12 ASN A 194  ASP A 222  TYR A 225  SER A 255                    
-SITE     3 AC1 12 SER A 257  LYS A 258  ARG A 266  TYR B  70                    
-SITE     1 AC2 12 TYR A  70  GLY B 108  THR B 109  TRP B 140                    
-SITE     2 AC2 12 ASN B 194  ASP B 222  ALA B 224  TYR B 225                    
-SITE     3 AC2 12 SER B 255  SER B 257  LYS B 258  ARG B 266                    
-SITE     1 AC3 10 TYR A  70  SER A 296  ILE B  17  VAL B  37                    
-SITE     2 AC3 10 GLY B  38  TRP B 140  ASN B 142  ASN B 194                    
-SITE     3 AC3 10 LYS B 258  ARG B 386                                          
-CRYST1  124.230  121.810   55.270  90.00  90.00  90.00 P 21 21 21    8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.008050  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.008210  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.018093        0.00000                         
-MTRIX1   1 -0.955296  0.130119 -0.265478      188.09711    1                    
-MTRIX2   1  0.124434 -0.637584 -0.760265       42.86650    1                    
-MTRIX3   1 -0.268189 -0.759312  0.592891       51.88500    1                    
-ATOM      1  N   MET A   5     116.166  20.679  21.702  1.00 32.70           N  
-ATOM      2  CA  MET A   5     114.714  20.487  21.963  1.00 33.25           C  
-ATOM      3  C   MET A   5     114.015  19.800  20.798  1.00 32.39           C  
-ATOM      4  O   MET A   5     113.289  18.830  20.990  1.00 32.32           O  
-ATOM      5  CB  MET A   5     114.039  21.826  22.249  1.00 35.21           C  
-ATOM      6  CG  MET A   5     112.600  21.704  22.717  1.00 37.74           C  
-ATOM      7  SD  MET A   5     111.847  23.308  23.034  1.00 41.68           S  
-ATOM      8  CE  MET A   5     111.123  23.658  21.461  1.00 40.75           C  
-ATOM      9  N   LEU A   6     114.282  20.269  19.584  1.00 31.92           N  
-ATOM     10  CA  LEU A   6     113.656  19.712  18.385  1.00 31.72           C  
-ATOM     11  C   LEU A   6     113.885  18.215  18.152  1.00 32.01           C  
-ATOM     12  O   LEU A   6     113.254  17.618  17.285  1.00 32.06           O  
-ATOM     13  CB  LEU A   6     114.063  20.521  17.146  1.00 29.65           C  
-ATOM     14  CG  LEU A   6     113.824  22.033  17.242  1.00 28.73           C  
-ATOM     15  CD1 LEU A   6     114.088  22.698  15.900  1.00 28.59           C  
-ATOM     16  CD2 LEU A   6     112.406  22.313  17.704  1.00 27.45           C  
-ATOM     17  N   GLY A   7     114.772  17.610  18.934  1.00 32.75           N  
-ATOM     18  CA  GLY A   7     115.043  16.190  18.782  1.00 32.62           C  
-ATOM     19  C   GLY A   7     113.931  15.330  19.349  1.00 32.60           C  
-ATOM     20  O   GLY A   7     113.810  14.163  18.997  1.00 32.00           O  
-ATOM     21  N   ASN A   8     113.118  15.921  20.220  1.00 33.85           N  
-ATOM     22  CA  ASN A   8     111.996  15.231  20.861  1.00 35.46           C  
-ATOM     23  C   ASN A   8     110.795  15.141  19.925  1.00 35.83           C  
-ATOM     24  O   ASN A   8     109.794  14.497  20.231  1.00 35.85           O  
-ATOM     25  CB  ASN A   8     111.573  15.983  22.125  1.00 37.10           C  
-ATOM     26  CG  ASN A   8     112.739  16.286  23.052  1.00 39.12           C  
-ATOM     27  OD1 ASN A   8     113.781  15.619  23.012  1.00 39.47           O  
-ATOM     28  ND2 ASN A   8     112.575  17.310  23.883  1.00 39.64           N  
-ATOM     29  N   LEU A   9     110.899  15.826  18.795  1.00 36.44           N  
-ATOM     30  CA  LEU A   9     109.856  15.871  17.785  1.00 36.65           C  
-ATOM     31  C   LEU A   9     109.523  14.468  17.258  1.00 37.10           C  
-ATOM     32  O   LEU A   9     110.415  13.722  16.848  1.00 36.27           O  
-ATOM     33  CB  LEU A   9     110.344  16.760  16.634  1.00 35.90           C  
-ATOM     34  CG  LEU A   9     109.513  17.905  16.051  1.00 36.05           C  
-ATOM     35  CD1 LEU A   9     108.814  18.707  17.135  1.00 34.93           C  
-ATOM     36  CD2 LEU A   9     110.434  18.796  15.227  1.00 34.27           C  
-ATOM     37  N   LYS A  10     108.245  14.097  17.302  1.00 38.02           N  
-ATOM     38  CA  LYS A  10     107.826  12.796  16.785  1.00 38.86           C  
-ATOM     39  C   LYS A  10     107.783  12.910  15.264  1.00 38.30           C  
-ATOM     40  O   LYS A  10     107.380  13.942  14.724  1.00 38.00           O  
-ATOM     41  CB  LYS A  10     106.445  12.396  17.324  1.00 40.26           C  
-ATOM     42  CG  LYS A  10     106.389  12.140  18.831  1.00 42.61           C  
-ATOM     43  CD  LYS A  10     107.274  10.967  19.249  1.00 44.29           C  
-ATOM     44  CE  LYS A  10     108.343  11.403  20.250  1.00 45.09           C  
-ATOM     45  NZ  LYS A  10     109.213  10.278  20.705  1.00 45.92           N  
-ATOM     46  N   PRO A  11     108.254  11.877  14.552  1.00 38.53           N  
-ATOM     47  CA  PRO A  11     108.245  11.913  13.086  1.00 39.02           C  
-ATOM     48  C   PRO A  11     106.839  11.954  12.499  1.00 39.52           C  
-ATOM     49  O   PRO A  11     105.954  11.210  12.927  1.00 40.03           O  
-ATOM     50  CB  PRO A  11     109.001  10.637  12.702  1.00 38.43           C  
-ATOM     51  CG  PRO A  11     108.755   9.734  13.853  1.00 38.69           C  
-ATOM     52  CD  PRO A  11     108.885  10.640  15.043  1.00 38.21           C  
-ATOM     53  N   GLN A  12     106.633  12.860  11.550  1.00 40.07           N  
-ATOM     54  CA  GLN A  12     105.343  13.012  10.894  1.00 40.47           C  
-ATOM     55  C   GLN A  12     105.393  12.351   9.528  1.00 42.40           C  
-ATOM     56  O   GLN A  12     106.362  12.508   8.785  1.00 42.46           O  
-ATOM     57  CB  GLN A  12     104.989  14.492  10.752  1.00 38.88           C  
-ATOM     58  CG  GLN A  12     104.888  15.239  12.073  1.00 36.77           C  
-ATOM     59  CD  GLN A  12     103.813  14.679  12.980  1.00 35.68           C  
-ATOM     60  OE1 GLN A  12     102.773  14.220  12.516  1.00 36.52           O  
-ATOM     61  NE2 GLN A  12     104.054  14.722  14.280  1.00 35.16           N  
-ATOM     62  N   ALA A  13     104.347  11.599   9.208  1.00 45.00           N  
-ATOM     63  CA  ALA A  13     104.254  10.896   7.938  1.00 47.94           C  
-ATOM     64  C   ALA A  13     104.082  11.849   6.765  1.00 50.41           C  
-ATOM     65  O   ALA A  13     103.461  12.905   6.897  1.00 51.04           O  
-ATOM     66  CB  ALA A  13     103.102   9.905   7.979  1.00 47.57           C  
-ATOM     67  N   PRO A  14     104.693  11.520   5.618  1.00 53.10           N  
-ATOM     68  CA  PRO A  14     104.625  12.318   4.389  1.00 55.98           C  
-ATOM     69  C   PRO A  14     103.192  12.369   3.846  1.00 58.97           C  
-ATOM     70  O   PRO A  14     102.315  11.667   4.340  1.00 59.49           O  
-ATOM     71  CB  PRO A  14     105.542  11.545   3.442  1.00 55.53           C  
-ATOM     72  CG  PRO A  14     106.556  10.947   4.373  1.00 54.64           C  
-ATOM     73  CD  PRO A  14     105.684  10.438   5.482  1.00 53.65           C  
-ATOM     74  N   ASP A  15     102.963  13.189   2.819  1.00 62.38           N  
-ATOM     75  CA  ASP A  15     101.634  13.329   2.208  1.00 65.68           C  
-ATOM     76  C   ASP A  15     101.049  12.004   1.734  1.00 67.01           C  
-ATOM     77  O   ASP A  15      99.920  11.658   2.074  1.00 67.26           O  
-ATOM     78  CB  ASP A  15     101.687  14.276   1.007  1.00 66.94           C  
-ATOM     79  CG  ASP A  15     101.921  15.712   1.407  1.00 68.77           C  
-ATOM     80  OD1 ASP A  15     103.057  16.034   1.819  1.00 69.96           O  
-ATOM     81  OD2 ASP A  15     100.968  16.516   1.305  1.00 69.29           O  
-ATOM     82  N   LYS A  16     101.818  11.339   0.874  1.00 68.51           N  
-ATOM     83  CA  LYS A  16     101.512  10.051   0.247  1.00 70.54           C  
-ATOM     84  C   LYS A  16     101.260  10.244  -1.241  1.00 71.52           C  
-ATOM     85  O   LYS A  16     101.524   9.349  -2.045  1.00 71.89           O  
-ATOM     86  CB  LYS A  16     100.356   9.301   0.930  1.00 70.97           C  
-ATOM     87  CG  LYS A  16     100.417   7.778   0.784  1.00 71.73           C  
-ATOM     88  CD  LYS A  16     101.854   7.249   0.867  1.00 72.36           C  
-ATOM     89  CE  LYS A  16     102.599   7.742   2.107  1.00 72.58           C  
-ATOM     90  NZ  LYS A  16     104.076   7.741   1.908  1.00 72.95           N  
-ATOM     91  N   ILE A  17     100.854  11.457  -1.610  1.00 72.39           N  
-ATOM     92  CA  ILE A  17     100.609  11.808  -3.006  1.00 73.00           C  
-ATOM     93  C   ILE A  17     101.930  11.657  -3.770  1.00 73.38           C  
-ATOM     94  O   ILE A  17     101.943  11.472  -4.987  1.00 73.60           O  
-ATOM     95  CB  ILE A  17     100.117  13.274  -3.127  1.00 73.11           C  
-ATOM     96  CG1 ILE A  17      98.826  13.463  -2.324  1.00 73.52           C  
-ATOM     97  CG2 ILE A  17      99.892  13.648  -4.587  1.00 73.34           C  
-ATOM     98  CD1 ILE A  17      98.310  14.891  -2.302  1.00 73.95           C  
-ATOM     99  N   LEU A  18     103.035  11.697  -3.030  1.00 73.77           N  
-ATOM    100  CA  LEU A  18     104.369  11.578  -3.605  1.00 73.95           C  
-ATOM    101  C   LEU A  18     104.889  10.147  -3.678  1.00 73.69           C  
-ATOM    102  O   LEU A  18     105.685   9.825  -4.555  1.00 73.92           O  
-ATOM    103  CB  LEU A  18     105.370  12.482  -2.861  1.00 74.62           C  
-ATOM    104  CG  LEU A  18     105.815  12.301  -1.398  1.00 75.17           C  
-ATOM    105  CD1 LEU A  18     104.624  12.226  -0.465  1.00 75.06           C  
-ATOM    106  CD2 LEU A  18     106.700  11.073  -1.237  1.00 75.63           C  
-ATOM    107  N   ALA A  19     104.456   9.293  -2.756  1.00 73.16           N  
-ATOM    108  CA  ALA A  19     104.900   7.903  -2.755  1.00 72.76           C  
-ATOM    109  C   ALA A  19     104.351   7.238  -4.010  1.00 72.60           C  
-ATOM    110  O   ALA A  19     105.038   6.460  -4.677  1.00 72.77           O  
-ATOM    111  CB  ALA A  19     104.404   7.192  -1.517  1.00 73.07           C  
-ATOM    112  N   LEU A  20     103.108   7.578  -4.333  1.00 71.93           N  
-ATOM    113  CA  LEU A  20     102.436   7.051  -5.513  1.00 71.15           C  
-ATOM    114  C   LEU A  20     103.155   7.617  -6.738  1.00 70.08           C  
-ATOM    115  O   LEU A  20     103.352   6.923  -7.739  1.00 70.46           O  
-ATOM    116  CB  LEU A  20     100.969   7.498  -5.527  1.00 72.02           C  
-ATOM    117  CG  LEU A  20     100.255   7.752  -4.191  1.00 72.48           C  
-ATOM    118  CD1 LEU A  20      98.838   8.246  -4.446  1.00 72.91           C  
-ATOM    119  CD2 LEU A  20     100.244   6.501  -3.324  1.00 72.88           C  
-ATOM    120  N   MET A  21     103.562   8.878  -6.631  1.00 68.28           N  
-ATOM    121  CA  MET A  21     104.270   9.576  -7.698  1.00 66.76           C  
-ATOM    122  C   MET A  21     105.636   8.967  -7.994  1.00 65.26           C  
-ATOM    123  O   MET A  21     105.980   8.740  -9.154  1.00 64.92           O  
-ATOM    124  CB  MET A  21     104.432  11.052  -7.338  1.00 67.73           C  
-ATOM    125  CG  MET A  21     103.389  11.965  -7.955  1.00 69.14           C  
-ATOM    126  SD  MET A  21     103.884  12.581  -9.584  1.00 71.37           S  
-ATOM    127  CE  MET A  21     103.486  11.167 -10.648  1.00 70.51           C  
-ATOM    128  N   GLY A  22     106.403   8.697  -6.941  1.00 63.75           N  
-ATOM    129  CA  GLY A  22     107.726   8.121  -7.099  1.00 61.72           C  
-ATOM    130  C   GLY A  22     107.673   6.758  -7.754  1.00 60.00           C  
-ATOM    131  O   GLY A  22     108.536   6.411  -8.567  1.00 60.00           O  
-ATOM    132  N   GLU A  23     106.652   5.985  -7.395  1.00 58.18           N  
-ATOM    133  CA  GLU A  23     106.455   4.652  -7.945  1.00 56.14           C  
-ATOM    134  C   GLU A  23     106.114   4.744  -9.426  1.00 54.07           C  
-ATOM    135  O   GLU A  23     106.710   4.052 -10.253  1.00 54.22           O  
-ATOM    136  CB  GLU A  23     105.333   3.935  -7.195  1.00 57.16           C  
-ATOM    137  CG  GLU A  23     105.025   2.551  -7.733  1.00 58.82           C  
-ATOM    138  CD  GLU A  23     103.923   1.852  -6.963  1.00 59.49           C  
-ATOM    139  OE1 GLU A  23     102.924   2.511  -6.599  1.00 60.00           O  
-ATOM    140  OE2 GLU A  23     104.061   0.636  -6.725  1.00 60.08           O  
-ATOM    141  N   PHE A  24     105.172   5.622  -9.753  1.00 51.49           N  
-ATOM    142  CA  PHE A  24     104.749   5.819 -11.132  1.00 49.20           C  
-ATOM    143  C   PHE A  24     105.924   6.229 -12.018  1.00 49.07           C  
-ATOM    144  O   PHE A  24     106.110   5.679 -13.102  1.00 49.00           O  
-ATOM    145  CB  PHE A  24     103.639   6.872 -11.206  1.00 46.91           C  
-ATOM    146  CG  PHE A  24     103.154   7.147 -12.601  1.00 44.53           C  
-ATOM    147  CD1 PHE A  24     102.345   6.232 -13.263  1.00 43.30           C  
-ATOM    148  CD2 PHE A  24     103.524   8.313 -13.261  1.00 43.27           C  
-ATOM    149  CE1 PHE A  24     101.913   6.471 -14.560  1.00 42.52           C  
-ATOM    150  CE2 PHE A  24     103.098   8.560 -14.559  1.00 42.33           C  
-ATOM    151  CZ  PHE A  24     102.292   7.638 -15.211  1.00 42.30           C  
-ATOM    152  N   ARG A  25     106.715   7.189 -11.548  1.00 48.86           N  
-ATOM    153  CA  ARG A  25     107.871   7.674 -12.298  1.00 48.67           C  
-ATOM    154  C   ARG A  25     108.930   6.592 -12.495  1.00 47.72           C  
-ATOM    155  O   ARG A  25     109.599   6.542 -13.527  1.00 47.62           O  
-ATOM    156  CB  ARG A  25     108.499   8.873 -11.587  1.00 50.06           C  
-ATOM    157  CG  ARG A  25     107.593  10.081 -11.474  1.00 52.24           C  
-ATOM    158  CD  ARG A  25     108.317  11.237 -10.804  1.00 54.70           C  
-ATOM    159  NE  ARG A  25     108.824  10.884  -9.477  1.00 56.66           N  
-ATOM    160  CZ  ARG A  25     108.652  11.625  -8.385  1.00 57.51           C  
-ATOM    161  NH1 ARG A  25     107.972  12.765  -8.444  1.00 58.08           N  
-ATOM    162  NH2 ARG A  25     109.153  11.219  -7.225  1.00 57.85           N  
-ATOM    163  N   ALA A  26     109.091   5.742 -11.490  1.00 46.55           N  
-ATOM    164  CA  ALA A  26     110.069   4.665 -11.549  1.00 45.67           C  
-ATOM    165  C   ALA A  26     109.710   3.575 -12.565  1.00 44.90           C  
-ATOM    166  O   ALA A  26     110.587   2.827 -13.013  1.00 45.54           O  
-ATOM    167  CB  ALA A  26     110.248   4.054 -10.163  1.00 46.41           C  
-ATOM    168  N   ASP A  27     108.428   3.477 -12.918  1.00 42.82           N  
-ATOM    169  CA  ASP A  27     107.957   2.473 -13.866  1.00 40.62           C  
-ATOM    170  C   ASP A  27     108.490   2.737 -15.276  1.00 39.59           C  
-ATOM    171  O   ASP A  27     108.165   3.746 -15.893  1.00 39.80           O  
-ATOM    172  CB  ASP A  27     106.425   2.446 -13.883  1.00 40.61           C  
-ATOM    173  CG  ASP A  27     105.860   1.185 -14.516  1.00 40.63           C  
-ATOM    174  OD1 ASP A  27     106.501   0.601 -15.413  1.00 40.89           O  
-ATOM    175  OD2 ASP A  27     104.760   0.768 -14.114  1.00 41.18           O  
-ATOM    176  N   PRO A  28     109.288   1.805 -15.819  1.00 38.65           N  
-ATOM    177  CA  PRO A  28     109.865   1.939 -17.159  1.00 38.05           C  
-ATOM    178  C   PRO A  28     108.923   1.587 -18.315  1.00 37.91           C  
-ATOM    179  O   PRO A  28     109.361   1.476 -19.464  1.00 37.78           O  
-ATOM    180  CB  PRO A  28     111.049   0.979 -17.101  1.00 37.79           C  
-ATOM    181  CG  PRO A  28     110.517  -0.122 -16.248  1.00 37.26           C  
-ATOM    182  CD  PRO A  28     109.850   0.628 -15.126  1.00 37.97           C  
-ATOM    183  N   ARG A  29     107.646   1.380 -18.014  1.00 37.99           N  
-ATOM    184  CA  ARG A  29     106.675   1.035 -19.051  1.00 37.80           C  
-ATOM    185  C   ARG A  29     106.220   2.258 -19.834  1.00 37.98           C  
-ATOM    186  O   ARG A  29     105.813   3.266 -19.259  1.00 37.36           O  
-ATOM    187  CB  ARG A  29     105.473   0.296 -18.457  1.00 37.50           C  
-ATOM    188  CG  ARG A  29     105.757  -1.163 -18.134  1.00 36.30           C  
-ATOM    189  CD  ARG A  29     104.536  -1.871 -17.586  1.00 35.04           C  
-ATOM    190  NE  ARG A  29     104.178  -1.392 -16.256  1.00 34.41           N  
-ATOM    191  CZ  ARG A  29     103.402  -2.057 -15.408  1.00 33.64           C  
-ATOM    192  NH1 ARG A  29     102.889  -3.228 -15.753  1.00 33.29           N  
-ATOM    193  NH2 ARG A  29     103.130  -1.547 -14.217  1.00 34.04           N  
-ATOM    194  N   GLN A  30     106.275   2.145 -21.155  1.00 38.69           N  
-ATOM    195  CA  GLN A  30     105.893   3.229 -22.048  1.00 40.14           C  
-ATOM    196  C   GLN A  30     104.403   3.539 -21.976  1.00 39.32           C  
-ATOM    197  O   GLN A  30     104.000   4.692 -22.094  1.00 39.98           O  
-ATOM    198  CB  GLN A  30     106.272   2.886 -23.493  1.00 42.82           C  
-ATOM    199  CG  GLN A  30     107.777   2.794 -23.765  1.00 47.86           C  
-ATOM    200  CD  GLN A  30     108.484   1.737 -22.919  1.00 50.50           C  
-ATOM    201  OE1 GLN A  30     107.956   0.638 -22.694  1.00 51.65           O  
-ATOM    202  NE2 GLN A  30     109.674   2.071 -22.433  1.00 51.15           N  
-ATOM    203  N   GLY A  31     103.587   2.509 -21.774  1.00 37.55           N  
-ATOM    204  CA  GLY A  31     102.152   2.715 -21.712  1.00 35.30           C  
-ATOM    205  C   GLY A  31     101.554   2.947 -20.337  1.00 33.62           C  
-ATOM    206  O   GLY A  31     100.357   2.732 -20.150  1.00 34.52           O  
-ATOM    207  N   LYS A  32     102.355   3.376 -19.370  1.00 31.31           N  
-ATOM    208  CA  LYS A  32     101.828   3.608 -18.033  1.00 29.60           C  
-ATOM    209  C   LYS A  32     100.863   4.794 -18.013  1.00 29.31           C  
-ATOM    210  O   LYS A  32     101.081   5.799 -18.691  1.00 29.13           O  
-ATOM    211  CB  LYS A  32     102.956   3.809 -17.021  1.00 28.83           C  
-ATOM    212  CG  LYS A  32     103.923   4.929 -17.357  1.00 28.95           C  
-ATOM    213  CD  LYS A  32     104.925   5.130 -16.234  1.00 28.58           C  
-ATOM    214  CE  LYS A  32     105.980   6.154 -16.606  1.00 28.20           C  
-ATOM    215  NZ  LYS A  32     106.828   6.484 -15.430  1.00 28.55           N  
-ATOM    216  N   ILE A  33      99.795   4.659 -17.231  1.00 28.76           N  
-ATOM    217  CA  ILE A  33      98.766   5.693 -17.100  1.00 27.22           C  
-ATOM    218  C   ILE A  33      98.621   6.093 -15.627  1.00 26.71           C  
-ATOM    219  O   ILE A  33      98.755   5.254 -14.733  1.00 26.85           O  
-ATOM    220  CB  ILE A  33      97.405   5.171 -17.645  1.00 26.35           C  
-ATOM    221  CG1 ILE A  33      97.545   4.807 -19.122  1.00 25.39           C  
-ATOM    222  CG2 ILE A  33      96.321   6.214 -17.488  1.00 24.83           C  
-ATOM    223  CD1 ILE A  33      96.407   3.986 -19.656  1.00 26.38           C  
-ATOM    224  N   ASP A  34      98.375   7.375 -15.373  1.00 25.97           N  
-ATOM    225  CA  ASP A  34      98.217   7.864 -14.009  1.00 25.35           C  
-ATOM    226  C   ASP A  34      96.809   8.414 -13.768  1.00 25.57           C  
-ATOM    227  O   ASP A  34      96.475   9.513 -14.207  1.00 26.66           O  
-ATOM    228  CB  ASP A  34      99.261   8.942 -13.713  1.00 25.56           C  
-ATOM    229  CG  ASP A  34      99.228   9.422 -12.267  1.00 27.10           C  
-ATOM    230  OD1 ASP A  34      98.782   8.668 -11.373  1.00 27.24           O  
-ATOM    231  OD2 ASP A  34      99.668  10.561 -12.018  1.00 28.86           O  
-ATOM    232  N   LEU A  35      95.980   7.636 -13.080  1.00 23.90           N  
-ATOM    233  CA  LEU A  35      94.616   8.048 -12.762  1.00 22.50           C  
-ATOM    234  C   LEU A  35      94.522   8.451 -11.296  1.00 22.02           C  
-ATOM    235  O   LEU A  35      93.430   8.566 -10.742  1.00 21.45           O  
-ATOM    236  CB  LEU A  35      93.635   6.913 -13.057  1.00 21.72           C  
-ATOM    237  CG  LEU A  35      92.935   6.905 -14.415  1.00 21.07           C  
-ATOM    238  CD1 LEU A  35      93.781   7.558 -15.484  1.00 21.55           C  
-ATOM    239  CD2 LEU A  35      92.598   5.483 -14.783  1.00 20.74           C  
-ATOM    240  N   GLY A  36      95.676   8.654 -10.672  1.00 21.55           N  
-ATOM    241  CA  GLY A  36      95.708   9.044  -9.278  1.00 21.01           C  
-ATOM    242  C   GLY A  36      95.826  10.542  -9.080  1.00 21.02           C  
-ATOM    243  O   GLY A  36      95.769  11.018  -7.949  1.00 22.10           O  
-ATOM    244  N   VAL A  37      96.019  11.288 -10.163  1.00 21.27           N  
-ATOM    245  CA  VAL A  37      96.144  12.745 -10.075  1.00 21.91           C  
-ATOM    246  C   VAL A  37      94.903  13.375  -9.447  1.00 22.01           C  
-ATOM    247  O   VAL A  37      93.778  12.955  -9.724  1.00 23.36           O  
-ATOM    248  CB  VAL A  37      96.390  13.388 -11.462  1.00 22.29           C  
-ATOM    249  CG1 VAL A  37      97.768  13.030 -11.949  1.00 23.09           C  
-ATOM    250  CG2 VAL A  37      95.347  12.920 -12.472  1.00 21.13           C  
-ATOM    251  N   GLY A  38      95.110  14.397  -8.621  1.00 21.16           N  
-ATOM    252  CA  GLY A  38      93.998  15.056  -7.957  1.00 20.19           C  
-ATOM    253  C   GLY A  38      93.659  16.444  -8.467  1.00 19.42           C  
-ATOM    254  O   GLY A  38      93.059  17.240  -7.751  1.00 19.19           O  
-ATOM    255  N   VAL A  39      94.055  16.749  -9.693  1.00 18.60           N  
-ATOM    256  CA  VAL A  39      93.770  18.049 -10.282  1.00 18.70           C  
-ATOM    257  C   VAL A  39      93.289  17.812 -11.699  1.00 19.14           C  
-ATOM    258  O   VAL A  39      93.457  16.720 -12.241  1.00 19.19           O  
-ATOM    259  CB  VAL A  39      95.025  18.952 -10.344  1.00 19.23           C  
-ATOM    260  CG1 VAL A  39      95.557  19.230  -8.943  1.00 19.84           C  
-ATOM    261  CG2 VAL A  39      96.101  18.307 -11.218  1.00 19.12           C  
-ATOM    262  N   TYR A  40      92.691  18.830 -12.299  1.00 19.80           N  
-ATOM    263  CA  TYR A  40      92.207  18.709 -13.661  1.00 20.83           C  
-ATOM    264  C   TYR A  40      93.366  18.783 -14.649  1.00 22.45           C  
-ATOM    265  O   TYR A  40      94.300  19.562 -14.468  1.00 22.96           O  
-ATOM    266  CB  TYR A  40      91.196  19.814 -13.972  1.00 19.19           C  
-ATOM    267  CG  TYR A  40      90.808  19.868 -15.427  1.00 18.91           C  
-ATOM    268  CD1 TYR A  40      89.856  18.994 -15.943  1.00 19.11           C  
-ATOM    269  CD2 TYR A  40      91.431  20.756 -16.302  1.00 19.18           C  
-ATOM    270  CE1 TYR A  40      89.535  18.996 -17.293  1.00 20.17           C  
-ATOM    271  CE2 TYR A  40      91.118  20.767 -17.656  1.00 20.65           C  
-ATOM    272  CZ  TYR A  40      90.172  19.881 -18.147  1.00 20.74           C  
-ATOM    273  OH  TYR A  40      89.881  19.868 -19.497  1.00 21.75           O  
-ATOM    274  N   LYS A  41      93.286  17.974 -15.698  1.00 23.87           N  
-ATOM    275  CA  LYS A  41      94.295  17.951 -16.748  1.00 25.86           C  
-ATOM    276  C   LYS A  41      93.533  17.875 -18.054  1.00 26.77           C  
-ATOM    277  O   LYS A  41      92.573  17.120 -18.155  1.00 28.13           O  
-ATOM    278  CB  LYS A  41      95.187  16.716 -16.620  1.00 26.45           C  
-ATOM    279  CG  LYS A  41      96.066  16.704 -15.395  1.00 27.08           C  
-ATOM    280  CD  LYS A  41      97.074  15.587 -15.472  1.00 28.07           C  
-ATOM    281  CE  LYS A  41      98.095  15.725 -14.362  1.00 30.53           C  
-ATOM    282  NZ  LYS A  41      98.813  17.031 -14.421  1.00 31.16           N  
-ATOM    283  N   ASP A  42      93.923  18.672 -19.041  1.00 28.03           N  
-ATOM    284  CA  ASP A  42      93.241  18.642 -20.326  1.00 28.76           C  
-ATOM    285  C   ASP A  42      93.711  17.469 -21.180  1.00 29.80           C  
-ATOM    286  O   ASP A  42      94.465  16.610 -20.710  1.00 29.12           O  
-ATOM    287  CB  ASP A  42      93.392  19.979 -21.076  1.00 28.95           C  
-ATOM    288  CG  ASP A  42      94.840  20.342 -21.389  1.00 29.28           C  
-ATOM    289  OD1 ASP A  42      95.730  19.462 -21.381  1.00 29.44           O  
-ATOM    290  OD2 ASP A  42      95.085  21.534 -21.660  1.00 29.00           O  
-ATOM    291  N   ALA A  43      93.325  17.482 -22.452  1.00 31.12           N  
-ATOM    292  CA  ALA A  43      93.677  16.424 -23.392  1.00 32.91           C  
-ATOM    293  C   ALA A  43      95.179  16.179 -23.531  1.00 33.97           C  
-ATOM    294  O   ALA A  43      95.610  15.040 -23.720  1.00 34.63           O  
-ATOM    295  CB  ALA A  43      93.069  16.722 -24.751  1.00 33.24           C  
-ATOM    296  N   THR A  44      95.967  17.245 -23.424  1.00 34.58           N  
-ATOM    297  CA  THR A  44      97.419  17.147 -23.554  1.00 34.61           C  
-ATOM    298  C   THR A  44      98.137  16.825 -22.242  1.00 33.88           C  
-ATOM    299  O   THR A  44      99.368  16.859 -22.176  1.00 34.72           O  
-ATOM    300  CB  THR A  44      98.001  18.447 -24.154  1.00 35.69           C  
-ATOM    301  OG1 THR A  44      97.866  19.528 -23.219  1.00 36.32           O  
-ATOM    302  CG2 THR A  44      97.251  18.810 -25.430  1.00 36.74           C  
-ATOM    303  N   GLY A  45      97.366  16.529 -21.199  1.00 32.71           N  
-ATOM    304  CA  GLY A  45      97.945  16.208 -19.908  1.00 31.61           C  
-ATOM    305  C   GLY A  45      98.501  17.416 -19.176  1.00 31.26           C  
-ATOM    306  O   GLY A  45      99.462  17.301 -18.420  1.00 31.74           O  
-ATOM    307  N   HIS A  46      97.891  18.576 -19.388  1.00 30.83           N  
-ATOM    308  CA  HIS A  46      98.330  19.810 -18.744  1.00 29.99           C  
-ATOM    309  C   HIS A  46      97.204  20.416 -17.920  1.00 28.40           C  
-ATOM    310  O   HIS A  46      96.034  20.165 -18.193  1.00 27.98           O  
-ATOM    311  CB  HIS A  46      98.757  20.835 -19.796  1.00 32.14           C  
-ATOM    312  CG  HIS A  46      99.926  20.406 -20.624  1.00 34.94           C  
-ATOM    313  ND1 HIS A  46      99.987  20.616 -21.985  1.00 35.62           N  
-ATOM    314  CD2 HIS A  46     101.077  19.776 -20.290  1.00 36.53           C  
-ATOM    315  CE1 HIS A  46     101.124  20.132 -22.454  1.00 37.20           C  
-ATOM    316  NE2 HIS A  46     101.802  19.615 -21.445  1.00 37.49           N  
-ATOM    317  N   THR A  47      97.569  21.215 -16.921  1.00 26.78           N  
-ATOM    318  CA  THR A  47      96.610  21.916 -16.067  1.00 25.72           C  
-ATOM    319  C   THR A  47      96.764  23.397 -16.433  1.00 24.56           C  
-ATOM    320  O   THR A  47      97.544  24.131 -15.828  1.00 24.93           O  
-ATOM    321  CB  THR A  47      96.933  21.689 -14.590  1.00 25.39           C  
-ATOM    322  OG1 THR A  47      96.993  20.279 -14.345  1.00 25.71           O  
-ATOM    323  CG2 THR A  47      95.870  22.319 -13.702  1.00 24.75           C  
-ATOM    324  N   PRO A  48      96.013  23.850 -17.442  1.00 23.66           N  
-ATOM    325  CA  PRO A  48      96.080  25.238 -17.899  1.00 22.38           C  
-ATOM    326  C   PRO A  48      95.593  26.302 -16.931  1.00 21.54           C  
-ATOM    327  O   PRO A  48      95.053  26.009 -15.868  1.00 21.10           O  
-ATOM    328  CB  PRO A  48      95.217  25.207 -19.161  1.00 22.64           C  
-ATOM    329  CG  PRO A  48      94.140  24.231 -18.789  1.00 23.42           C  
-ATOM    330  CD  PRO A  48      94.926  23.119 -18.126  1.00 22.94           C  
-ATOM    331  N   ILE A  49      95.851  27.549 -17.300  1.00 21.02           N  
-ATOM    332  CA  ILE A  49      95.407  28.702 -16.536  1.00 20.24           C  
-ATOM    333  C   ILE A  49      94.214  29.164 -17.356  1.00 19.86           C  
-ATOM    334  O   ILE A  49      94.321  29.333 -18.571  1.00 19.50           O  
-ATOM    335  CB  ILE A  49      96.475  29.827 -16.497  1.00 19.42           C  
-ATOM    336  CG1 ILE A  49      97.745  29.325 -15.800  1.00 18.99           C  
-ATOM    337  CG2 ILE A  49      95.921  31.054 -15.784  1.00 17.84           C  
-ATOM    338  CD1 ILE A  49      98.861  30.360 -15.680  1.00 18.11           C  
-ATOM    339  N   MET A  50      93.062  29.283 -16.718  1.00 20.07           N  
-ATOM    340  CA  MET A  50      91.861  29.710 -17.412  1.00 20.79           C  
-ATOM    341  C   MET A  50      92.042  31.087 -18.045  1.00 21.62           C  
-ATOM    342  O   MET A  50      92.663  31.976 -17.456  1.00 22.86           O  
-ATOM    343  CB  MET A  50      90.679  29.679 -16.447  1.00 19.84           C  
-ATOM    344  CG  MET A  50      90.397  28.271 -15.956  1.00 20.83           C  
-ATOM    345  SD  MET A  50      89.001  28.124 -14.852  1.00 21.71           S  
-ATOM    346  CE  MET A  50      87.657  27.943 -16.041  1.00 21.11           C  
-ATOM    347  N   ARG A  51      91.505  31.251 -19.252  1.00 22.45           N  
-ATOM    348  CA  ARG A  51      91.610  32.503 -20.006  1.00 22.96           C  
-ATOM    349  C   ARG A  51      91.236  33.746 -19.209  1.00 22.27           C  
-ATOM    350  O   ARG A  51      91.975  34.740 -19.200  1.00 22.36           O  
-ATOM    351  CB  ARG A  51      90.743  32.449 -21.269  1.00 24.37           C  
-ATOM    352  CG  ARG A  51      91.096  31.339 -22.236  1.00 26.60           C  
-ATOM    353  CD  ARG A  51      90.271  31.448 -23.505  1.00 29.75           C  
-ATOM    354  NE  ARG A  51      88.834  31.371 -23.245  1.00 33.24           N  
-ATOM    355  CZ  ARG A  51      88.114  30.254 -23.322  1.00 34.50           C  
-ATOM    356  NH1 ARG A  51      88.693  29.106 -23.657  1.00 36.53           N  
-ATOM    357  NH2 ARG A  51      86.811  30.283 -23.066  1.00 34.38           N  
-ATOM    358  N   ALA A  52      90.085  33.692 -18.551  1.00 21.68           N  
-ATOM    359  CA  ALA A  52      89.598  34.817 -17.762  1.00 20.60           C  
-ATOM    360  C   ALA A  52      90.545  35.137 -16.615  1.00 19.63           C  
-ATOM    361  O   ALA A  52      90.716  36.302 -16.261  1.00 20.07           O  
-ATOM    362  CB  ALA A  52      88.198  34.533 -17.243  1.00 20.08           C  
-ATOM    363  N   VAL A  53      91.183  34.109 -16.062  1.00 18.90           N  
-ATOM    364  CA  VAL A  53      92.126  34.297 -14.963  1.00 19.49           C  
-ATOM    365  C   VAL A  53      93.379  35.021 -15.456  1.00 19.71           C  
-ATOM    366  O   VAL A  53      93.882  35.928 -14.792  1.00 19.39           O  
-ATOM    367  CB  VAL A  53      92.508  32.949 -14.304  1.00 19.67           C  
-ATOM    368  CG1 VAL A  53      93.652  33.138 -13.319  1.00 18.49           C  
-ATOM    369  CG2 VAL A  53      91.298  32.371 -13.585  1.00 20.00           C  
-ATOM    370  N   HIS A  54      93.870  34.636 -16.629  1.00 20.24           N  
-ATOM    371  CA  HIS A  54      95.043  35.289 -17.187  1.00 21.27           C  
-ATOM    372  C   HIS A  54      94.701  36.730 -17.537  1.00 21.33           C  
-ATOM    373  O   HIS A  54      95.565  37.605 -17.512  1.00 21.76           O  
-ATOM    374  CB  HIS A  54      95.536  34.568 -18.436  1.00 22.66           C  
-ATOM    375  CG  HIS A  54      96.834  35.101 -18.962  1.00 24.97           C  
-ATOM    376  ND1 HIS A  54      96.907  36.172 -19.829  1.00 26.20           N  
-ATOM    377  CD2 HIS A  54      98.112  34.719 -18.732  1.00 24.58           C  
-ATOM    378  CE1 HIS A  54      98.174  36.425 -20.108  1.00 26.03           C  
-ATOM    379  NE2 HIS A  54      98.925  35.558 -19.453  1.00 25.94           N  
-ATOM    380  N   ALA A  55      93.442  36.961 -17.895  1.00 21.87           N  
-ATOM    381  CA  ALA A  55      92.972  38.296 -18.249  1.00 21.07           C  
-ATOM    382  C   ALA A  55      92.931  39.160 -16.995  1.00 20.70           C  
-ATOM    383  O   ALA A  55      93.343  40.325 -17.016  1.00 20.56           O  
-ATOM    384  CB  ALA A  55      91.586  38.218 -18.890  1.00 20.51           C  
-ATOM    385  N   ALA A  56      92.458  38.579 -15.896  1.00 19.98           N  
-ATOM    386  CA  ALA A  56      92.376  39.300 -14.632  1.00 20.58           C  
-ATOM    387  C   ALA A  56      93.765  39.695 -14.129  1.00 20.62           C  
-ATOM    388  O   ALA A  56      93.953  40.797 -13.623  1.00 21.48           O  
-ATOM    389  CB  ALA A  56      91.650  38.468 -13.591  1.00 19.79           C  
-ATOM    390  N   GLU A  57      94.740  38.808 -14.283  1.00 21.14           N  
-ATOM    391  CA  GLU A  57      96.098  39.104 -13.842  1.00 21.33           C  
-ATOM    392  C   GLU A  57      96.750  40.227 -14.639  1.00 22.03           C  
-ATOM    393  O   GLU A  57      97.513  41.016 -14.080  1.00 22.95           O  
-ATOM    394  CB  GLU A  57      96.963  37.847 -13.842  1.00 20.25           C  
-ATOM    395  CG  GLU A  57      96.758  36.996 -12.598  1.00 19.74           C  
-ATOM    396  CD  GLU A  57      97.634  35.758 -12.570  1.00 19.43           C  
-ATOM    397  OE1 GLU A  57      97.811  35.125 -13.628  1.00 19.69           O  
-ATOM    398  OE2 GLU A  57      98.132  35.399 -11.485  1.00 18.11           O  
-ATOM    399  N   GLN A  58      96.462  40.296 -15.937  1.00 23.32           N  
-ATOM    400  CA  GLN A  58      96.997  41.367 -16.782  1.00 24.84           C  
-ATOM    401  C   GLN A  58      96.389  42.670 -16.282  1.00 24.69           C  
-ATOM    402  O   GLN A  58      97.077  43.673 -16.106  1.00 24.58           O  
-ATOM    403  CB  GLN A  58      96.589  41.177 -18.246  1.00 26.96           C  
-ATOM    404  CG  GLN A  58      97.153  39.941 -18.928  1.00 31.13           C  
-ATOM    405  CD  GLN A  58      96.656  39.772 -20.359  1.00 33.63           C  
-ATOM    406  OE1 GLN A  58      96.281  38.670 -20.772  1.00 35.92           O  
-ATOM    407  NE2 GLN A  58      96.659  40.857 -21.124  1.00 34.59           N  
-ATOM    408  N   ARG A  59      95.091  42.617 -16.013  1.00 25.29           N  
-ATOM    409  CA  ARG A  59      94.326  43.760 -15.539  1.00 26.44           C  
-ATOM    410  C   ARG A  59      94.820  44.277 -14.186  1.00 25.70           C  
-ATOM    411  O   ARG A  59      94.933  45.487 -13.974  1.00 24.57           O  
-ATOM    412  CB  ARG A  59      92.851  43.366 -15.456  1.00 28.29           C  
-ATOM    413  CG  ARG A  59      91.875  44.516 -15.556  1.00 33.00           C  
-ATOM    414  CD  ARG A  59      90.488  44.004 -15.931  1.00 36.64           C  
-ATOM    415  NE  ARG A  59      90.530  43.238 -17.177  1.00 39.62           N  
-ATOM    416  CZ  ARG A  59      89.645  43.347 -18.163  1.00 40.85           C  
-ATOM    417  NH1 ARG A  59      88.618  44.183 -18.062  1.00 40.88           N  
-ATOM    418  NH2 ARG A  59      89.786  42.605 -19.253  1.00 41.40           N  
-ATOM    419  N   MET A  60      95.100  43.355 -13.271  1.00 25.76           N  
-ATOM    420  CA  MET A  60      95.580  43.710 -11.939  1.00 25.98           C  
-ATOM    421  C   MET A  60      96.956  44.364 -12.010  1.00 26.45           C  
-ATOM    422  O   MET A  60      97.222  45.345 -11.311  1.00 26.11           O  
-ATOM    423  CB  MET A  60      95.645  42.467 -11.052  1.00 25.27           C  
-ATOM    424  CG  MET A  60      94.294  41.850 -10.730  1.00 24.82           C  
-ATOM    425  SD  MET A  60      94.424  40.171 -10.034  1.00 24.93           S  
-ATOM    426  CE  MET A  60      95.411  40.478  -8.544  1.00 23.29           C  
-ATOM    427  N   LEU A  61      97.806  43.838 -12.888  1.00 28.03           N  
-ATOM    428  CA  LEU A  61      99.167  44.340 -13.075  1.00 30.14           C  
-ATOM    429  C   LEU A  61      99.205  45.785 -13.569  1.00 31.27           C  
-ATOM    430  O   LEU A  61     100.194  46.496 -13.363  1.00 31.43           O  
-ATOM    431  CB  LEU A  61      99.925  43.438 -14.056  1.00 30.56           C  
-ATOM    432  CG  LEU A  61     101.409  43.732 -14.301  1.00 31.27           C  
-ATOM    433  CD1 LEU A  61     102.188  43.673 -12.995  1.00 31.70           C  
-ATOM    434  CD2 LEU A  61     101.966  42.730 -15.294  1.00 31.76           C  
-ATOM    435  N   GLU A  62      98.126  46.216 -14.213  1.00 32.29           N  
-ATOM    436  CA  GLU A  62      98.044  47.570 -14.737  1.00 33.12           C  
-ATOM    437  C   GLU A  62      97.267  48.544 -13.864  1.00 32.69           C  
-ATOM    438  O   GLU A  62      97.467  49.753 -13.957  1.00 33.38           O  
-ATOM    439  CB  GLU A  62      97.424  47.557 -16.131  1.00 34.70           C  
-ATOM    440  CG  GLU A  62      98.220  46.786 -17.154  1.00 38.33           C  
-ATOM    441  CD  GLU A  62      97.622  46.898 -18.535  1.00 41.43           C  
-ATOM    442  OE1 GLU A  62      96.660  46.155 -18.830  1.00 42.42           O  
-ATOM    443  OE2 GLU A  62      98.105  47.739 -19.324  1.00 44.18           O  
-ATOM    444  N   THR A  63      96.392  48.032 -13.011  1.00 32.06           N  
-ATOM    445  CA  THR A  63      95.583  48.908 -12.177  1.00 32.26           C  
-ATOM    446  C   THR A  63      96.027  49.031 -10.724  1.00 32.48           C  
-ATOM    447  O   THR A  63      95.788  50.053 -10.078  1.00 33.32           O  
-ATOM    448  CB  THR A  63      94.111  48.472 -12.220  1.00 31.97           C  
-ATOM    449  OG1 THR A  63      94.006  47.121 -11.756  1.00 33.21           O  
-ATOM    450  CG2 THR A  63      93.576  48.553 -13.647  1.00 31.37           C  
-ATOM    451  N   GLU A  64      96.651  47.989 -10.196  1.00 32.06           N  
-ATOM    452  CA  GLU A  64      97.087  48.024  -8.811  1.00 31.96           C  
-ATOM    453  C   GLU A  64      98.265  48.985  -8.633  1.00 30.39           C  
-ATOM    454  O   GLU A  64      99.237  48.949  -9.394  1.00 29.84           O  
-ATOM    455  CB  GLU A  64      97.428  46.614  -8.338  1.00 34.01           C  
-ATOM    456  CG  GLU A  64      96.648  46.169  -7.103  1.00 38.21           C  
-ATOM    457  CD  GLU A  64      95.128  46.090  -7.295  1.00 40.37           C  
-ATOM    458  OE1 GLU A  64      94.665  45.714  -8.399  1.00 41.86           O  
-ATOM    459  OE2 GLU A  64      94.395  46.384  -6.319  1.00 39.82           O  
-ATOM    460  N   THR A  66      98.154  49.859  -7.637  1.00 28.31           N  
-ATOM    461  CA  THR A  66      99.177  50.858  -7.352  1.00 26.72           C  
-ATOM    462  C   THR A  66      99.884  50.625  -6.021  1.00 25.04           C  
-ATOM    463  O   THR A  66     100.916  51.240  -5.742  1.00 24.58           O  
-ATOM    464  CB  THR A  66      98.561  52.266  -7.310  1.00 26.53           C  
-ATOM    465  OG1 THR A  66      97.533  52.303  -6.312  1.00 27.68           O  
-ATOM    466  CG2 THR A  66      97.960  52.631  -8.661  1.00 27.39           C  
-ATOM    467  N   THR A  67      99.330  49.741  -5.202  1.00 22.89           N  
-ATOM    468  CA  THR A  67      99.909  49.461  -3.902  1.00 20.70           C  
-ATOM    469  C   THR A  67      99.641  48.029  -3.466  1.00 20.08           C  
-ATOM    470  O   THR A  67      98.792  47.335  -4.034  1.00 20.51           O  
-ATOM    471  CB  THR A  67      99.352  50.424  -2.832  1.00 20.16           C  
-ATOM    472  OG1 THR A  67      99.953  50.133  -1.566  1.00 20.12           O  
-ATOM    473  CG2 THR A  67      97.848  50.274  -2.700  1.00 20.26           C  
-ATOM    474  N   LYS A  68     100.409  47.583  -2.480  1.00 19.00           N  
-ATOM    475  CA  LYS A  68     100.275  46.248  -1.921  1.00 17.36           C  
-ATOM    476  C   LYS A  68     100.252  46.345  -0.408  1.00 17.13           C  
-ATOM    477  O   LYS A  68     100.623  45.399   0.283  1.00 17.92           O  
-ATOM    478  CB  LYS A  68     101.413  45.330  -2.377  1.00 15.78           C  
-ATOM    479  CG  LYS A  68     101.319  44.891  -3.828  1.00 14.56           C  
-ATOM    480  CD  LYS A  68     102.499  44.012  -4.203  1.00 14.99           C  
-ATOM    481  CE  LYS A  68     102.458  43.605  -5.666  1.00 14.89           C  
-ATOM    482  NZ  LYS A  68     101.320  42.693  -5.969  1.00 14.15           N  
-ATOM    483  N   THR A  69      99.813  47.492   0.104  1.00 17.85           N  
-ATOM    484  CA  THR A  69      99.725  47.705   1.548  1.00 19.53           C  
-ATOM    485  C   THR A  69      98.731  46.710   2.126  1.00 19.20           C  
-ATOM    486  O   THR A  69      97.990  46.065   1.389  1.00 19.28           O  
-ATOM    487  CB  THR A  69      99.151  49.098   1.909  1.00 20.48           C  
-ATOM    488  OG1 THR A  69      99.272  49.994   0.801  1.00 22.71           O  
-ATOM    489  CG2 THR A  69      99.879  49.668   3.103  1.00 19.63           C  
-ATOM    490  N   TYR A  70      98.698  46.618   3.448  1.00 19.08           N  
-ATOM    491  CA  TYR A  70      97.762  45.734   4.118  1.00 19.83           C  
-ATOM    492  C   TYR A  70      96.338  46.096   3.674  1.00 20.56           C  
-ATOM    493  O   TYR A  70      96.002  47.276   3.518  1.00 20.32           O  
-ATOM    494  CB  TYR A  70      97.902  45.880   5.630  1.00 19.61           C  
-ATOM    495  CG  TYR A  70      99.218  45.379   6.167  1.00 19.94           C  
-ATOM    496  CD1 TYR A  70      99.599  44.047   5.997  1.00 20.23           C  
-ATOM    497  CD2 TYR A  70     100.073  46.226   6.872  1.00 20.34           C  
-ATOM    498  CE1 TYR A  70     100.797  43.567   6.523  1.00 20.95           C  
-ATOM    499  CE2 TYR A  70     101.278  45.759   7.405  1.00 20.60           C  
-ATOM    500  CZ  TYR A  70     101.631  44.428   7.228  1.00 21.41           C  
-ATOM    501  OH  TYR A  70     102.790  43.945   7.780  1.00 21.55           O  
-ATOM    502  N   ALA A  71      95.526  45.075   3.432  1.00 20.65           N  
-ATOM    503  CA  ALA A  71      94.156  45.264   2.986  1.00 20.14           C  
-ATOM    504  C   ALA A  71      93.177  44.797   4.063  1.00 20.56           C  
-ATOM    505  O   ALA A  71      93.444  44.956   5.249  1.00 22.43           O  
-ATOM    506  CB  ALA A  71      93.931  44.517   1.672  1.00 19.43           C  
-ATOM    507  N   GLY A  72      92.072  44.178   3.652  1.00 20.76           N  
-ATOM    508  CA  GLY A  72      91.071  43.726   4.599  1.00 19.19           C  
-ATOM    509  C   GLY A  72      91.443  42.488   5.375  1.00 19.16           C  
-ATOM    510  O   GLY A  72      91.782  41.463   4.789  1.00 19.52           O  
-ATOM    511  N   LEU A  73      91.316  42.571   6.692  1.00 18.64           N  
-ATOM    512  CA  LEU A  73      91.629  41.473   7.591  1.00 20.11           C  
-ATOM    513  C   LEU A  73      90.846  40.194   7.271  1.00 21.30           C  
-ATOM    514  O   LEU A  73      91.402  39.093   7.256  1.00 20.86           O  
-ATOM    515  CB  LEU A  73      91.329  41.900   9.024  1.00 20.91           C  
-ATOM    516  CG  LEU A  73      91.811  40.990  10.147  1.00 22.82           C  
-ATOM    517  CD1 LEU A  73      93.258  41.341  10.500  1.00 24.32           C  
-ATOM    518  CD2 LEU A  73      90.921  41.181  11.354  1.00 23.39           C  
-ATOM    519  N   SER A  74      89.547  40.336   7.039  1.00 21.90           N  
-ATOM    520  CA  SER A  74      88.710  39.181   6.739  1.00 22.74           C  
-ATOM    521  C   SER A  74      88.415  39.044   5.252  1.00 22.10           C  
-ATOM    522  O   SER A  74      87.566  38.244   4.845  1.00 21.17           O  
-ATOM    523  CB  SER A  74      87.419  39.237   7.559  1.00 22.98           C  
-ATOM    524  OG  SER A  74      86.883  40.547   7.589  1.00 27.46           O  
-ATOM    525  N   GLY A  75      89.175  39.783   4.449  1.00 22.59           N  
-ATOM    526  CA  GLY A  75      89.002  39.761   3.011  1.00 22.22           C  
-ATOM    527  C   GLY A  75      88.481  41.089   2.502  1.00 22.73           C  
-ATOM    528  O   GLY A  75      88.179  41.995   3.286  1.00 22.75           O  
-ATOM    529  N   GLU A  76      88.416  41.216   1.184  1.00 23.37           N  
-ATOM    530  CA  GLU A  76      87.921  42.423   0.544  1.00 24.34           C  
-ATOM    531  C   GLU A  76      86.433  42.272   0.294  1.00 24.14           C  
-ATOM    532  O   GLU A  76      85.973  41.211  -0.135  1.00 23.68           O  
-ATOM    533  CB  GLU A  76      88.647  42.656  -0.785  1.00 25.98           C  
-ATOM    534  CG  GLU A  76      89.742  43.716  -0.731  1.00 27.80           C  
-ATOM    535  CD  GLU A  76      90.609  43.602   0.502  1.00 28.43           C  
-ATOM    536  OE1 GLU A  76      91.455  42.690   0.554  1.00 30.22           O  
-ATOM    537  OE2 GLU A  76      90.440  44.423   1.422  1.00 28.74           O  
-ATOM    538  N   PRO A  77      85.664  43.340   0.536  1.00 24.33           N  
-ATOM    539  CA  PRO A  77      84.212  43.344   0.341  1.00 24.55           C  
-ATOM    540  C   PRO A  77      83.788  42.796  -1.025  1.00 24.59           C  
-ATOM    541  O   PRO A  77      82.879  41.973  -1.107  1.00 24.97           O  
-ATOM    542  CB  PRO A  77      83.863  44.822   0.493  1.00 25.30           C  
-ATOM    543  CG  PRO A  77      84.851  45.275   1.538  1.00 25.29           C  
-ATOM    544  CD  PRO A  77      86.131  44.639   1.053  1.00 24.14           C  
-ATOM    545  N   GLU A  78      84.466  43.225  -2.085  1.00 24.23           N  
-ATOM    546  CA  GLU A  78      84.151  42.770  -3.435  1.00 24.10           C  
-ATOM    547  C   GLU A  78      84.209  41.252  -3.528  1.00 23.52           C  
-ATOM    548  O   GLU A  78      83.380  40.632  -4.195  1.00 23.62           O  
-ATOM    549  CB  GLU A  78      85.114  43.390  -4.453  1.00 26.47           C  
-ATOM    550  CG  GLU A  78      84.861  42.975  -5.901  1.00 31.02           C  
-ATOM    551  CD  GLU A  78      85.765  43.692  -6.902  1.00 34.25           C  
-ATOM    552  OE1 GLU A  78      86.929  43.268  -7.097  1.00 36.13           O  
-ATOM    553  OE2 GLU A  78      85.303  44.680  -7.512  1.00 35.82           O  
-ATOM    554  N   PHE A  79      85.187  40.658  -2.852  1.00 22.50           N  
-ATOM    555  CA  PHE A  79      85.358  39.210  -2.864  1.00 20.30           C  
-ATOM    556  C   PHE A  79      84.288  38.526  -2.026  1.00 20.77           C  
-ATOM    557  O   PHE A  79      83.653  37.572  -2.483  1.00 20.67           O  
-ATOM    558  CB  PHE A  79      86.750  38.837  -2.350  1.00 17.57           C  
-ATOM    559  CG  PHE A  79      87.021  37.362  -2.335  1.00 13.51           C  
-ATOM    560  CD1 PHE A  79      87.182  36.660  -3.518  1.00 12.22           C  
-ATOM    561  CD2 PHE A  79      87.137  36.680  -1.129  1.00 13.74           C  
-ATOM    562  CE1 PHE A  79      87.461  35.290  -3.509  1.00 13.24           C  
-ATOM    563  CE2 PHE A  79      87.415  35.311  -1.105  1.00 14.45           C  
-ATOM    564  CZ  PHE A  79      87.578  34.615  -2.300  1.00 12.72           C  
-ATOM    565  N   GLN A  80      84.089  39.018  -0.806  1.00 20.88           N  
-ATOM    566  CA  GLN A  80      83.100  38.455   0.114  1.00 21.75           C  
-ATOM    567  C   GLN A  80      81.701  38.444  -0.491  1.00 22.17           C  
-ATOM    568  O   GLN A  80      80.974  37.453  -0.373  1.00 22.22           O  
-ATOM    569  CB  GLN A  80      83.069  39.249   1.421  1.00 21.70           C  
-ATOM    570  CG  GLN A  80      84.360  39.233   2.214  1.00 22.16           C  
-ATOM    571  CD  GLN A  80      84.309  40.185   3.391  1.00 23.23           C  
-ATOM    572  OE1 GLN A  80      84.202  41.398   3.216  1.00 23.71           O  
-ATOM    573  NE2 GLN A  80      84.366  39.641   4.597  1.00 24.96           N  
-ATOM    574  N   LYS A  81      81.322  39.552  -1.121  1.00 22.26           N  
-ATOM    575  CA  LYS A  81      80.010  39.671  -1.734  1.00 22.98           C  
-ATOM    576  C   LYS A  81      79.889  38.806  -2.978  1.00 22.82           C  
-ATOM    577  O   LYS A  81      78.914  38.066  -3.129  1.00 22.98           O  
-ATOM    578  CB  LYS A  81      79.703  41.134  -2.066  1.00 25.02           C  
-ATOM    579  CG  LYS A  81      78.350  41.360  -2.736  1.00 29.69           C  
-ATOM    580  CD  LYS A  81      77.196  40.709  -1.957  1.00 33.57           C  
-ATOM    581  CE  LYS A  81      76.226  41.735  -1.374  1.00 36.03           C  
-ATOM    582  NZ  LYS A  81      76.771  42.430  -0.164  1.00 39.08           N  
-ATOM    583  N   ALA A  82      80.887  38.876  -3.853  1.00 22.09           N  
-ATOM    584  CA  ALA A  82      80.874  38.091  -5.081  1.00 21.40           C  
-ATOM    585  C   ALA A  82      80.818  36.592  -4.780  1.00 21.25           C  
-ATOM    586  O   ALA A  82      80.071  35.850  -5.417  1.00 22.20           O  
-ATOM    587  CB  ALA A  82      82.083  38.423  -5.939  1.00 21.75           C  
-ATOM    588  N   MET A  83      81.580  36.150  -3.787  1.00 19.84           N  
-ATOM    589  CA  MET A  83      81.584  34.741  -3.420  1.00 18.87           C  
-ATOM    590  C   MET A  83      80.244  34.328  -2.831  1.00 18.61           C  
-ATOM    591  O   MET A  83      79.725  33.261  -3.156  1.00 19.30           O  
-ATOM    592  CB  MET A  83      82.721  34.437  -2.440  1.00 18.77           C  
-ATOM    593  CG  MET A  83      84.064  34.217  -3.117  1.00 17.22           C  
-ATOM    594  SD  MET A  83      84.114  32.665  -4.033  1.00 17.10           S  
-ATOM    595  CE  MET A  83      83.831  33.195  -5.621  1.00 16.74           C  
-ATOM    596  N   GLY A  84      79.675  35.186  -1.990  1.00 17.90           N  
-ATOM    597  CA  GLY A  84      78.391  34.894  -1.379  1.00 17.75           C  
-ATOM    598  C   GLY A  84      77.288  34.764  -2.413  1.00 18.11           C  
-ATOM    599  O   GLY A  84      76.430  33.891  -2.306  1.00 17.27           O  
-ATOM    600  N   GLU A  85      77.314  35.628  -3.420  1.00 18.06           N  
-ATOM    601  CA  GLU A  85      76.317  35.595  -4.477  1.00 19.88           C  
-ATOM    602  C   GLU A  85      76.499  34.381  -5.384  1.00 18.94           C  
-ATOM    603  O   GLU A  85      75.524  33.793  -5.850  1.00 18.85           O  
-ATOM    604  CB  GLU A  85      76.364  36.888  -5.299  1.00 22.03           C  
-ATOM    605  CG  GLU A  85      75.891  38.121  -4.525  1.00 27.17           C  
-ATOM    606  CD  GLU A  85      76.138  39.446  -5.255  1.00 30.22           C  
-ATOM    607  OE1 GLU A  85      76.796  39.454  -6.324  1.00 32.51           O  
-ATOM    608  OE2 GLU A  85      75.678  40.491  -4.744  1.00 31.62           O  
-ATOM    609  N   LEU A  86      77.748  33.998  -5.621  1.00 18.52           N  
-ATOM    610  CA  LEU A  86      78.053  32.853  -6.475  1.00 18.44           C  
-ATOM    611  C   LEU A  86      77.525  31.555  -5.853  1.00 18.76           C  
-ATOM    612  O   LEU A  86      76.948  30.704  -6.537  1.00 19.18           O  
-ATOM    613  CB  LEU A  86      79.569  32.783  -6.697  1.00 18.39           C  
-ATOM    614  CG  LEU A  86      80.249  31.923  -7.772  1.00 18.88           C  
-ATOM    615  CD1 LEU A  86      80.858  30.684  -7.157  1.00 19.25           C  
-ATOM    616  CD2 LEU A  86      79.308  31.592  -8.910  1.00 17.72           C  
-ATOM    617  N   ILE A  87      77.686  31.436  -4.540  1.00 18.10           N  
-ATOM    618  CA  ILE A  87      77.254  30.258  -3.804  1.00 17.00           C  
-ATOM    619  C   ILE A  87      75.762  30.246  -3.452  1.00 18.52           C  
-ATOM    620  O   ILE A  87      75.066  29.273  -3.733  1.00 18.10           O  
-ATOM    621  CB  ILE A  87      78.097  30.102  -2.515  1.00 15.20           C  
-ATOM    622  CG1 ILE A  87      79.555  29.819  -2.886  1.00 14.42           C  
-ATOM    623  CG2 ILE A  87      77.536  29.007  -1.618  1.00 14.78           C  
-ATOM    624  CD1 ILE A  87      80.519  30.015  -1.754  1.00 12.26           C  
-ATOM    625  N   LEU A  88      75.272  31.335  -2.864  1.00 19.74           N  
-ATOM    626  CA  LEU A  88      73.881  31.418  -2.429  1.00 21.53           C  
-ATOM    627  C   LEU A  88      72.905  32.122  -3.363  1.00 23.22           C  
-ATOM    628  O   LEU A  88      71.717  32.208  -3.059  1.00 23.37           O  
-ATOM    629  CB  LEU A  88      73.816  32.053  -1.035  1.00 20.92           C  
-ATOM    630  CG  LEU A  88      74.566  31.290   0.064  1.00 20.21           C  
-ATOM    631  CD1 LEU A  88      74.636  32.104   1.341  1.00 19.80           C  
-ATOM    632  CD2 LEU A  88      73.889  29.952   0.313  1.00 20.56           C  
-ATOM    633  N   GLY A  89      73.403  32.641  -4.480  1.00 25.42           N  
-ATOM    634  CA  GLY A  89      72.544  33.325  -5.433  1.00 28.29           C  
-ATOM    635  C   GLY A  89      71.718  34.443  -4.823  1.00 30.50           C  
-ATOM    636  O   GLY A  89      72.219  35.221  -4.009  1.00 30.57           O  
-ATOM    637  N   ASP A  90      70.441  34.503  -5.202  1.00 32.22           N  
-ATOM    638  CA  ASP A  90      69.522  35.521  -4.695  1.00 33.83           C  
-ATOM    639  C   ASP A  90      69.135  35.315  -3.236  1.00 33.77           C  
-ATOM    640  O   ASP A  90      68.594  36.221  -2.604  1.00 33.64           O  
-ATOM    641  CB  ASP A  90      68.252  35.573  -5.549  1.00 35.99           C  
-ATOM    642  CG  ASP A  90      68.505  36.123  -6.939  1.00 38.70           C  
-ATOM    643  OD1 ASP A  90      68.896  37.307  -7.055  1.00 39.99           O  
-ATOM    644  OD2 ASP A  90      68.307  35.371  -7.920  1.00 41.00           O  
-ATOM    645  N   GLY A  91      69.414  34.131  -2.700  1.00 34.20           N  
-ATOM    646  CA  GLY A  91      69.076  33.847  -1.316  1.00 34.94           C  
-ATOM    647  C   GLY A  91      70.046  34.417  -0.294  1.00 35.84           C  
-ATOM    648  O   GLY A  91      69.879  34.209   0.911  1.00 36.85           O  
-ATOM    649  N   LEU A  95      71.063  35.132  -0.759  1.00 35.98           N  
-ATOM    650  CA  LEU A  95      72.053  35.714   0.136  1.00 36.03           C  
-ATOM    651  C   LEU A  95      71.469  36.802   1.031  1.00 36.06           C  
-ATOM    652  O   LEU A  95      70.999  37.828   0.547  1.00 36.93           O  
-ATOM    653  CB  LEU A  95      73.230  36.276  -0.666  1.00 36.49           C  
-ATOM    654  CG  LEU A  95      74.267  37.108   0.101  1.00 36.69           C  
-ATOM    655  CD1 LEU A  95      74.920  36.275   1.200  1.00 36.00           C  
-ATOM    656  CD2 LEU A  95      75.306  37.647  -0.869  1.00 36.61           C  
-ATOM    657  N   LYS A  96      71.517  36.569   2.337  1.00 35.85           N  
-ATOM    658  CA  LYS A  96      71.021  37.516   3.325  1.00 36.00           C  
-ATOM    659  C   LYS A  96      72.206  38.197   3.992  1.00 35.27           C  
-ATOM    660  O   LYS A  96      72.639  37.788   5.066  1.00 35.39           O  
-ATOM    661  CB  LYS A  96      70.206  36.801   4.402  1.00 37.48           C  
-ATOM    662  CG  LYS A  96      68.778  36.435   4.034  1.00 39.84           C  
-ATOM    663  CD  LYS A  96      68.057  35.917   5.277  1.00 41.69           C  
-ATOM    664  CE  LYS A  96      68.153  36.937   6.419  1.00 42.67           C  
-ATOM    665  NZ  LYS A  96      67.780  36.366   7.744  1.00 43.99           N  
-ATOM    666  N   SER A  97      72.702  39.263   3.382  1.00 34.58           N  
-ATOM    667  CA  SER A  97      73.843  39.992   3.918  1.00 35.17           C  
-ATOM    668  C   SER A  97      73.745  40.343   5.407  1.00 35.07           C  
-ATOM    669  O   SER A  97      74.760  40.381   6.106  1.00 35.15           O  
-ATOM    670  CB  SER A  97      74.079  41.251   3.088  1.00 35.73           C  
-ATOM    671  OG  SER A  97      74.205  40.913   1.718  1.00 36.81           O  
-ATOM    672  N   GLU A  98      72.526  40.571   5.890  1.00 34.87           N  
-ATOM    673  CA  GLU A  98      72.293  40.922   7.291  1.00 33.75           C  
-ATOM    674  C   GLU A  98      72.705  39.825   8.261  1.00 31.90           C  
-ATOM    675  O   GLU A  98      73.136  40.111   9.375  1.00 31.89           O  
-ATOM    676  CB  GLU A  98      70.808  41.243   7.539  1.00 35.83           C  
-ATOM    677  CG  GLU A  98      70.493  41.522   9.020  1.00 39.24           C  
-ATOM    678  CD  GLU A  98      69.017  41.397   9.383  1.00 41.33           C  
-ATOM    679  OE1 GLU A  98      68.456  40.279   9.294  1.00 42.07           O  
-ATOM    680  OE2 GLU A  98      68.425  42.417   9.799  1.00 42.89           O  
-ATOM    681  N   THR A  99      72.537  38.573   7.850  1.00 30.03           N  
-ATOM    682  CA  THR A  99      72.853  37.447   8.717  1.00 28.22           C  
-ATOM    683  C   THR A  99      74.016  36.562   8.260  1.00 27.08           C  
-ATOM    684  O   THR A  99      74.285  35.524   8.867  1.00 26.94           O  
-ATOM    685  CB  THR A  99      71.586  36.581   8.958  1.00 28.15           C  
-ATOM    686  OG1 THR A  99      70.911  36.343   7.714  1.00 27.20           O  
-ATOM    687  CG2 THR A  99      70.632  37.285   9.910  1.00 27.29           C  
-ATOM    688  N   THR A 100      74.736  36.995   7.235  1.00 25.46           N  
-ATOM    689  CA  THR A 100      75.854  36.216   6.732  1.00 25.24           C  
-ATOM    690  C   THR A 100      77.208  36.862   7.012  1.00 23.87           C  
-ATOM    691  O   THR A 100      77.444  38.014   6.638  1.00 23.43           O  
-ATOM    692  CB  THR A 100      75.730  35.991   5.207  1.00 26.50           C  
-ATOM    693  OG1 THR A 100      74.432  35.458   4.907  1.00 27.90           O  
-ATOM    694  CG2 THR A 100      76.807  35.017   4.716  1.00 25.98           C  
-ATOM    695  N   ALA A 101      78.080  36.124   7.696  1.00 22.34           N  
-ATOM    696  CA  ALA A 101      79.436  36.586   7.998  1.00 20.08           C  
-ATOM    697  C   ALA A 101      80.342  35.894   6.991  1.00 19.15           C  
-ATOM    698  O   ALA A 101      80.136  34.723   6.675  1.00 18.65           O  
-ATOM    699  CB  ALA A 101      79.829  36.198   9.415  1.00 19.52           C  
-ATOM    700  N   THR A 102      81.350  36.599   6.495  1.00 19.26           N  
-ATOM    701  CA  THR A 102      82.261  36.019   5.508  1.00 19.31           C  
-ATOM    702  C   THR A 102      83.733  36.228   5.885  1.00 18.47           C  
-ATOM    703  O   THR A 102      84.097  37.250   6.473  1.00 19.22           O  
-ATOM    704  CB  THR A 102      81.976  36.610   4.111  1.00 19.39           C  
-ATOM    705  OG1 THR A 102      80.560  36.625   3.897  1.00 20.45           O  
-ATOM    706  CG2 THR A 102      82.627  35.779   3.015  1.00 19.38           C  
-ATOM    707  N   LEU A 103      84.571  35.255   5.547  1.00 17.07           N  
-ATOM    708  CA  LEU A 103      85.995  35.317   5.852  1.00 15.69           C  
-ATOM    709  C   LEU A 103      86.837  34.727   4.720  1.00 15.08           C  
-ATOM    710  O   LEU A 103      86.656  33.560   4.358  1.00 13.59           O  
-ATOM    711  CB  LEU A 103      86.274  34.525   7.127  1.00 15.12           C  
-ATOM    712  CG  LEU A 103      87.696  34.544   7.687  1.00 15.29           C  
-ATOM    713  CD1 LEU A 103      87.935  35.844   8.449  1.00 13.08           C  
-ATOM    714  CD2 LEU A 103      87.881  33.347   8.615  1.00 15.55           C  
-ATOM    715  N   ALA A 104      87.725  35.534   4.140  1.00 14.83           N  
-ATOM    716  CA  ALA A 104      88.609  35.049   3.074  1.00 14.52           C  
-ATOM    717  C   ALA A 104      89.614  34.144   3.772  1.00 14.13           C  
-ATOM    718  O   ALA A 104      90.102  34.465   4.863  1.00 14.41           O  
-ATOM    719  CB  ALA A 104      89.323  36.196   2.381  1.00 13.83           C  
-ATOM    720  N   THR A 105      89.904  33.004   3.162  1.00 13.60           N  
-ATOM    721  CA  THR A 105      90.813  32.046   3.768  1.00 12.45           C  
-ATOM    722  C   THR A 105      91.901  31.558   2.814  1.00 12.30           C  
-ATOM    723  O   THR A 105      91.870  31.834   1.607  1.00 11.73           O  
-ATOM    724  CB  THR A 105      90.010  30.825   4.261  1.00 11.95           C  
-ATOM    725  OG1 THR A 105      89.266  30.277   3.164  1.00 11.39           O  
-ATOM    726  CG2 THR A 105      89.042  31.228   5.358  1.00 10.72           C  
-ATOM    727  N   VAL A 106      92.859  30.819   3.366  1.00 11.90           N  
-ATOM    728  CA  VAL A 106      93.951  30.249   2.581  1.00 11.10           C  
-ATOM    729  C   VAL A 106      93.417  28.936   1.987  1.00 10.09           C  
-ATOM    730  O   VAL A 106      93.579  27.859   2.559  1.00 10.48           O  
-ATOM    731  CB  VAL A 106      95.204  30.000   3.474  1.00 10.50           C  
-ATOM    732  CG1 VAL A 106      96.366  29.461   2.640  1.00 10.49           C  
-ATOM    733  CG2 VAL A 106      95.605  31.287   4.175  1.00  6.82           C  
-ATOM    734  N   GLY A 107      92.697  29.058   0.878  1.00 10.17           N  
-ATOM    735  CA  GLY A 107      92.117  27.896   0.230  1.00 10.91           C  
-ATOM    736  C   GLY A 107      90.947  27.314   1.014  1.00 11.65           C  
-ATOM    737  O   GLY A 107      90.609  27.787   2.101  1.00 11.85           O  
-ATOM    738  N   GLY A 108      90.296  26.309   0.439  1.00 12.28           N  
-ATOM    739  CA  GLY A 108      89.185  25.657   1.106  1.00 11.69           C  
-ATOM    740  C   GLY A 108      89.616  24.987   2.398  1.00 12.18           C  
-ATOM    741  O   GLY A 108      88.854  24.965   3.366  1.00 13.62           O  
-ATOM    742  N   THR A 109      90.839  24.456   2.426  1.00 11.36           N  
-ATOM    743  CA  THR A 109      91.366  23.802   3.621  1.00 10.16           C  
-ATOM    744  C   THR A 109      91.431  24.795   4.775  1.00 10.05           C  
-ATOM    745  O   THR A 109      91.131  24.443   5.919  1.00 10.54           O  
-ATOM    746  CB  THR A 109      92.763  23.213   3.375  1.00  9.82           C  
-ATOM    747  OG1 THR A 109      92.718  22.363   2.223  1.00 10.74           O  
-ATOM    748  CG2 THR A 109      93.225  22.400   4.583  1.00  9.46           C  
-ATOM    749  N   GLY A 110      91.817  26.034   4.466  1.00 10.30           N  
-ATOM    750  CA  GLY A 110      91.888  27.070   5.482  1.00 10.17           C  
-ATOM    751  C   GLY A 110      90.492  27.381   5.986  1.00 10.78           C  
-ATOM    752  O   GLY A 110      90.281  27.586   7.179  1.00 11.14           O  
-ATOM    753  N   ALA A 111      89.527  27.397   5.072  1.00 10.91           N  
-ATOM    754  CA  ALA A 111      88.138  27.657   5.437  1.00 12.17           C  
-ATOM    755  C   ALA A 111      87.648  26.552   6.368  1.00 12.30           C  
-ATOM    756  O   ALA A 111      87.016  26.832   7.383  1.00 13.06           O  
-ATOM    757  CB  ALA A 111      87.264  27.728   4.192  1.00 10.54           C  
-ATOM    758  N   LEU A 112      87.980  25.305   6.037  1.00 13.00           N  
-ATOM    759  CA  LEU A 112      87.590  24.150   6.843  1.00 13.28           C  
-ATOM    760  C   LEU A 112      88.185  24.231   8.244  1.00 13.60           C  
-ATOM    761  O   LEU A 112      87.477  24.086   9.242  1.00 14.13           O  
-ATOM    762  CB  LEU A 112      88.037  22.853   6.167  1.00 14.70           C  
-ATOM    763  CG  LEU A 112      87.301  22.420   4.893  1.00 16.31           C  
-ATOM    764  CD1 LEU A 112      88.014  21.234   4.258  1.00 17.31           C  
-ATOM    765  CD2 LEU A 112      85.867  22.038   5.232  1.00 17.07           C  
-ATOM    766  N   ARG A 113      89.488  24.485   8.314  1.00 13.96           N  
-ATOM    767  CA  ARG A 113      90.190  24.592   9.588  1.00 13.64           C  
-ATOM    768  C   ARG A 113      89.575  25.689  10.455  1.00 13.68           C  
-ATOM    769  O   ARG A 113      89.370  25.499  11.657  1.00 13.50           O  
-ATOM    770  CB  ARG A 113      91.679  24.870   9.345  1.00 13.47           C  
-ATOM    771  CG  ARG A 113      92.476  25.186  10.598  1.00 13.71           C  
-ATOM    772  CD  ARG A 113      92.519  24.007  11.546  1.00 15.44           C  
-ATOM    773  NE  ARG A 113      93.137  24.379  12.814  1.00 18.73           N  
-ATOM    774  CZ  ARG A 113      94.427  24.213  13.104  1.00 20.88           C  
-ATOM    775  NH1 ARG A 113      95.252  23.671  12.214  1.00 20.89           N  
-ATOM    776  NH2 ARG A 113      94.899  24.613  14.282  1.00 21.42           N  
-ATOM    777  N   GLN A 114      89.292  26.840   9.847  1.00 14.03           N  
-ATOM    778  CA  GLN A 114      88.694  27.955  10.574  1.00 14.40           C  
-ATOM    779  C   GLN A 114      87.271  27.618  11.039  1.00 13.97           C  
-ATOM    780  O   GLN A 114      86.913  27.901  12.182  1.00 14.39           O  
-ATOM    781  CB  GLN A 114      88.700  29.232   9.723  1.00 15.60           C  
-ATOM    782  CG  GLN A 114      90.090  29.693   9.256  1.00 17.91           C  
-ATOM    783  CD  GLN A 114      91.002  30.177  10.383  1.00 18.68           C  
-ATOM    784  OE1 GLN A 114      91.508  31.297  10.339  1.00 21.22           O  
-ATOM    785  NE2 GLN A 114      91.252  29.323  11.368  1.00 18.17           N  
-ATOM    786  N   ALA A 115      86.484  26.975  10.177  1.00 13.12           N  
-ATOM    787  CA  ALA A 115      85.104  26.593  10.522  1.00 13.58           C  
-ATOM    788  C   ALA A 115      85.116  25.752  11.797  1.00 13.88           C  
-ATOM    789  O   ALA A 115      84.332  25.988  12.723  1.00 13.46           O  
-ATOM    790  CB  ALA A 115      84.471  25.812   9.384  1.00 11.16           C  
-ATOM    791  N   LEU A 116      86.056  24.807  11.845  1.00 14.89           N  
-ATOM    792  CA  LEU A 116      86.255  23.912  12.982  1.00 14.54           C  
-ATOM    793  C   LEU A 116      86.672  24.675  14.246  1.00 15.03           C  
-ATOM    794  O   LEU A 116      86.215  24.359  15.345  1.00 14.58           O  
-ATOM    795  CB  LEU A 116      87.314  22.861  12.627  1.00 13.60           C  
-ATOM    796  CG  LEU A 116      86.903  21.464  12.138  1.00 13.93           C  
-ATOM    797  CD1 LEU A 116      85.511  21.466  11.553  1.00 14.77           C  
-ATOM    798  CD2 LEU A 116      87.915  20.943  11.125  1.00 12.19           C  
-ATOM    799  N   GLU A 117      87.551  25.668  14.093  1.00 16.81           N  
-ATOM    800  CA  GLU A 117      88.013  26.476  15.232  1.00 17.45           C  
-ATOM    801  C   GLU A 117      86.858  27.317  15.769  1.00 17.13           C  
-ATOM    802  O   GLU A 117      86.703  27.490  16.984  1.00 16.05           O  
-ATOM    803  CB  GLU A 117      89.165  27.414  14.827  1.00 18.35           C  
-ATOM    804  CG  GLU A 117      90.480  26.738  14.443  1.00 20.94           C  
-ATOM    805  CD  GLU A 117      91.280  26.224  15.634  1.00 22.81           C  
-ATOM    806  OE1 GLU A 117      90.886  26.471  16.793  1.00 24.55           O  
-ATOM    807  OE2 GLU A 117      92.318  25.563  15.412  1.00 23.37           O  
-ATOM    808  N   LEU A 118      86.058  27.847  14.851  1.00 17.20           N  
-ATOM    809  CA  LEU A 118      84.914  28.676  15.209  1.00 18.13           C  
-ATOM    810  C   LEU A 118      83.885  27.857  15.994  1.00 17.99           C  
-ATOM    811  O   LEU A 118      83.466  28.246  17.085  1.00 17.70           O  
-ATOM    812  CB  LEU A 118      84.275  29.265  13.943  1.00 17.69           C  
-ATOM    813  CG  LEU A 118      83.157  30.293  14.151  1.00 17.36           C  
-ATOM    814  CD1 LEU A 118      83.714  31.541  14.831  1.00 15.30           C  
-ATOM    815  CD2 LEU A 118      82.527  30.640  12.809  1.00 16.28           C  
-ATOM    816  N   ALA A 119      83.504  26.711  15.446  1.00 18.48           N  
-ATOM    817  CA  ALA A 119      82.532  25.845  16.099  1.00 19.90           C  
-ATOM    818  C   ALA A 119      82.996  25.413  17.494  1.00 21.37           C  
-ATOM    819  O   ALA A 119      82.225  25.466  18.456  1.00 20.67           O  
-ATOM    820  CB  ALA A 119      82.258  24.633  15.237  1.00 17.94           C  
-ATOM    821  N   ARG A 120      84.253  24.991  17.602  1.00 23.06           N  
-ATOM    822  CA  ARG A 120      84.808  24.557  18.879  1.00 25.08           C  
-ATOM    823  C   ARG A 120      84.826  25.734  19.854  1.00 25.90           C  
-ATOM    824  O   ARG A 120      84.705  25.563  21.066  1.00 25.88           O  
-ATOM    825  CB  ARG A 120      86.231  24.027  18.686  1.00 27.02           C  
-ATOM    826  CG  ARG A 120      86.869  23.523  19.965  1.00 30.28           C  
-ATOM    827  CD  ARG A 120      88.326  23.930  20.046  1.00 33.49           C  
-ATOM    828  NE  ARG A 120      89.234  22.851  19.673  1.00 35.94           N  
-ATOM    829  CZ  ARG A 120      90.434  23.035  19.130  1.00 36.31           C  
-ATOM    830  NH1 ARG A 120      90.866  24.262  18.854  1.00 35.77           N  
-ATOM    831  NH2 ARG A 120      91.190  21.985  18.836  1.00 36.06           N  
-ATOM    832  N   MET A 121      84.967  26.934  19.304  1.00 26.95           N  
-ATOM    833  CA  MET A 121      85.003  28.151  20.098  1.00 27.64           C  
-ATOM    834  C   MET A 121      83.630  28.392  20.743  1.00 27.66           C  
-ATOM    835  O   MET A 121      83.541  28.846  21.885  1.00 28.70           O  
-ATOM    836  CB  MET A 121      85.407  29.323  19.197  1.00 27.99           C  
-ATOM    837  CG  MET A 121      85.953  30.537  19.916  1.00 30.63           C  
-ATOM    838  SD  MET A 121      86.849  31.654  18.799  1.00 31.12           S  
-ATOM    839  CE  MET A 121      88.473  30.943  18.866  1.00 32.36           C  
-ATOM    840  N   ALA A 122      82.569  28.046  20.016  1.00 26.76           N  
-ATOM    841  CA  ALA A 122      81.198  28.219  20.489  1.00 25.83           C  
-ATOM    842  C   ALA A 122      80.678  26.998  21.243  1.00 26.34           C  
-ATOM    843  O   ALA A 122      79.764  27.116  22.063  1.00 26.05           O  
-ATOM    844  CB  ALA A 122      80.282  28.531  19.319  1.00 24.48           C  
-ATOM    845  N   ASN A 123      81.247  25.829  20.954  1.00 26.08           N  
-ATOM    846  CA  ASN A 123      80.835  24.586  21.598  1.00 26.80           C  
-ATOM    847  C   ASN A 123      82.036  23.688  21.827  1.00 27.59           C  
-ATOM    848  O   ASN A 123      82.431  22.926  20.944  1.00 28.24           O  
-ATOM    849  CB  ASN A 123      79.799  23.847  20.742  1.00 26.73           C  
-ATOM    850  CG  ASN A 123      79.325  22.546  21.382  1.00 26.59           C  
-ATOM    851  OD1 ASN A 123      79.483  22.331  22.586  1.00 26.18           O  
-ATOM    852  ND2 ASN A 123      78.743  21.673  20.576  1.00 27.30           N  
-ATOM    853  N   PRO A 124      82.611  23.733  23.037  1.00 28.79           N  
-ATOM    854  CA  PRO A 124      83.778  22.921  23.392  1.00 29.51           C  
-ATOM    855  C   PRO A 124      83.555  21.415  23.285  1.00 30.10           C  
-ATOM    856  O   PRO A 124      84.466  20.679  22.919  1.00 30.39           O  
-ATOM    857  CB  PRO A 124      84.052  23.341  24.836  1.00 29.38           C  
-ATOM    858  CG  PRO A 124      83.580  24.774  24.860  1.00 28.98           C  
-ATOM    859  CD  PRO A 124      82.265  24.652  24.135  1.00 28.69           C  
-ATOM    860  N   ASP A 125      82.343  20.958  23.580  1.00 31.20           N  
-ATOM    861  CA  ASP A 125      82.043  19.528  23.525  1.00 32.31           C  
-ATOM    862  C   ASP A 125      81.585  19.074  22.145  1.00 31.69           C  
-ATOM    863  O   ASP A 125      80.865  18.083  22.005  1.00 32.19           O  
-ATOM    864  CB  ASP A 125      81.007  19.171  24.589  1.00 34.13           C  
-ATOM    865  CG  ASP A 125      81.451  19.574  25.982  1.00 36.93           C  
-ATOM    866  OD1 ASP A 125      82.544  19.140  26.415  1.00 37.72           O  
-ATOM    867  OD2 ASP A 125      80.718  20.342  26.641  1.00 39.20           O  
-ATOM    868  N   LEU A 126      82.035  19.796  21.129  1.00 30.69           N  
-ATOM    869  CA  LEU A 126      81.696  19.520  19.742  1.00 29.43           C  
-ATOM    870  C   LEU A 126      82.137  18.137  19.261  1.00 28.41           C  
-ATOM    871  O   LEU A 126      83.246  17.689  19.559  1.00 28.65           O  
-ATOM    872  CB  LEU A 126      82.365  20.575  18.856  1.00 29.50           C  
-ATOM    873  CG  LEU A 126      82.070  20.573  17.358  1.00 29.78           C  
-ATOM    874  CD1 LEU A 126      81.009  21.615  17.057  1.00 29.72           C  
-ATOM    875  CD2 LEU A 126      83.334  20.885  16.583  1.00 30.22           C  
-ATOM    876  N   ARG A 129      81.255  17.468  18.525  1.00 27.08           N  
-ATOM    877  CA  ARG A 129      81.552  16.169  17.920  1.00 25.62           C  
-ATOM    878  C   ARG A 129      81.319  16.404  16.434  1.00 23.71           C  
-ATOM    879  O   ARG A 129      80.416  17.157  16.071  1.00 22.67           O  
-ATOM    880  CB  ARG A 129      80.583  15.083  18.378  1.00 27.56           C  
-ATOM    881  CG  ARG A 129      80.848  14.486  19.734  1.00 29.97           C  
-ATOM    882  CD  ARG A 129      80.092  13.169  19.856  1.00 33.16           C  
-ATOM    883  NE  ARG A 129      78.673  13.291  19.507  1.00 36.15           N  
-ATOM    884  CZ  ARG A 129      77.860  12.256  19.298  1.00 37.47           C  
-ATOM    885  NH1 ARG A 129      78.317  11.013  19.395  1.00 38.33           N  
-ATOM    886  NH2 ARG A 129      76.576  12.458  19.024  1.00 37.30           N  
-ATOM    887  N   VAL A 133      82.112  15.769  15.577  1.00 21.54           N  
-ATOM    888  CA  VAL A 133      81.948  15.945  14.139  1.00 19.09           C  
-ATOM    889  C   VAL A 133      81.630  14.626  13.460  1.00 18.14           C  
-ATOM    890  O   VAL A 133      82.261  13.617  13.739  1.00 18.46           O  
-ATOM    891  CB  VAL A 133      83.219  16.532  13.477  1.00 18.63           C  
-ATOM    892  CG1 VAL A 133      82.934  16.902  12.023  1.00 16.87           C  
-ATOM    893  CG2 VAL A 133      83.721  17.742  14.252  1.00 18.22           C  
-ATOM    894  N   PHE A 134      80.624  14.639  12.595  1.00 17.24           N  
-ATOM    895  CA  PHE A 134      80.214  13.463  11.839  1.00 16.05           C  
-ATOM    896  C   PHE A 134      80.727  13.666  10.411  1.00 15.58           C  
-ATOM    897  O   PHE A 134      80.497  14.724   9.817  1.00 15.30           O  
-ATOM    898  CB  PHE A 134      78.682  13.346  11.811  1.00 15.09           C  
-ATOM    899  CG  PHE A 134      78.082  12.795  13.074  1.00 14.95           C  
-ATOM    900  CD1 PHE A 134      78.006  13.570  14.227  1.00 14.55           C  
-ATOM    901  CD2 PHE A 134      77.587  11.490  13.109  1.00 14.90           C  
-ATOM    902  CE1 PHE A 134      77.450  13.054  15.395  1.00 13.27           C  
-ATOM    903  CE2 PHE A 134      77.028  10.966  14.274  1.00 12.26           C  
-ATOM    904  CZ  PHE A 134      76.961  11.747  15.416  1.00 13.28           C  
-ATOM    905  N   VAL A 135      81.434  12.677   9.873  1.00 15.55           N  
-ATOM    906  CA  VAL A 135      81.964  12.749   8.506  1.00 16.16           C  
-ATOM    907  C   VAL A 135      81.482  11.524   7.741  1.00 15.95           C  
-ATOM    908  O   VAL A 135      81.151  10.503   8.344  1.00 15.99           O  
-ATOM    909  CB  VAL A 135      83.522  12.797   8.466  1.00 15.76           C  
-ATOM    910  CG1 VAL A 135      84.034  13.966   9.279  1.00 15.07           C  
-ATOM    911  CG2 VAL A 135      84.117  11.494   8.975  1.00 16.14           C  
-ATOM    912  N   SER A 136      81.399  11.635   6.423  1.00 16.38           N  
-ATOM    913  CA  SER A 136      80.931  10.520   5.625  1.00 17.51           C  
-ATOM    914  C   SER A 136      81.934   9.391   5.532  1.00 19.69           C  
-ATOM    915  O   SER A 136      83.128   9.569   5.796  1.00 19.93           O  
-ATOM    916  CB  SER A 136      80.505  10.974   4.220  1.00 17.01           C  
-ATOM    917  OG  SER A 136      81.551  11.571   3.469  1.00 17.80           O  
-ATOM    918  N   ASP A 137      81.418   8.219   5.193  1.00 21.58           N  
-ATOM    919  CA  ASP A 137      82.214   7.022   5.026  1.00 23.82           C  
-ATOM    920  C   ASP A 137      82.090   6.644   3.551  1.00 24.00           C  
-ATOM    921  O   ASP A 137      81.057   6.134   3.125  1.00 24.96           O  
-ATOM    922  CB  ASP A 137      81.641   5.910   5.910  1.00 26.10           C  
-ATOM    923  CG  ASP A 137      82.393   4.599   5.778  1.00 29.40           C  
-ATOM    924  OD1 ASP A 137      83.642   4.619   5.687  1.00 30.90           O  
-ATOM    925  OD2 ASP A 137      81.727   3.540   5.778  1.00 31.66           O  
-ATOM    926  N   PRO A 138      83.111   6.954   2.736  1.00 24.38           N  
-ATOM    927  CA  PRO A 138      84.362   7.625   3.096  1.00 23.69           C  
-ATOM    928  C   PRO A 138      84.295   9.135   2.856  1.00 23.51           C  
-ATOM    929  O   PRO A 138      83.270   9.668   2.407  1.00 22.82           O  
-ATOM    930  CB  PRO A 138      85.353   6.981   2.142  1.00 23.80           C  
-ATOM    931  CG  PRO A 138      84.547   6.916   0.879  1.00 23.72           C  
-ATOM    932  CD  PRO A 138      83.185   6.432   1.357  1.00 24.04           C  
-ATOM    933  N   THR A 139      85.412   9.807   3.104  1.00 23.08           N  
-ATOM    934  CA  THR A 139      85.499  11.244   2.908  1.00 23.78           C  
-ATOM    935  C   THR A 139      86.929  11.595   2.537  1.00 24.97           C  
-ATOM    936  O   THR A 139      87.813  10.736   2.547  1.00 25.34           O  
-ATOM    937  CB  THR A 139      85.105  12.019   4.196  1.00 23.13           C  
-ATOM    938  OG1 THR A 139      84.889  13.403   3.884  1.00 22.07           O  
-ATOM    939  CG2 THR A 139      86.202  11.919   5.254  1.00 22.00           C  
-ATOM    940  N   TRP A 140      87.132  12.858   2.172  1.00 25.55           N  
-ATOM    941  CA  TRP A 140      88.446  13.392   1.823  1.00 24.97           C  
-ATOM    942  C   TRP A 140      89.306  13.158   3.072  1.00 25.09           C  
-ATOM    943  O   TRP A 140      89.045  13.734   4.133  1.00 25.07           O  
-ATOM    944  CB  TRP A 140      88.291  14.886   1.539  1.00 24.09           C  
-ATOM    945  CG  TRP A 140      89.478  15.572   0.979  1.00 23.62           C  
-ATOM    946  CD1 TRP A 140      90.234  15.171  -0.082  1.00 23.68           C  
-ATOM    947  CD2 TRP A 140      90.012  16.829   1.400  1.00 23.48           C  
-ATOM    948  NE1 TRP A 140      91.200  16.109  -0.354  1.00 23.24           N  
-ATOM    949  CE2 TRP A 140      91.087  17.138   0.543  1.00 23.62           C  
-ATOM    950  CE3 TRP A 140      89.679  17.732   2.421  1.00 23.17           C  
-ATOM    951  CZ2 TRP A 140      91.837  18.311   0.669  1.00 23.78           C  
-ATOM    952  CZ3 TRP A 140      90.423  18.898   2.547  1.00 23.29           C  
-ATOM    953  CH2 TRP A 140      91.492  19.176   1.674  1.00 23.25           C  
-ATOM    954  N   PRO A 141      90.339  12.309   2.964  1.00 25.61           N  
-ATOM    955  CA  PRO A 141      91.243  11.978   4.075  1.00 25.64           C  
-ATOM    956  C   PRO A 141      91.732  13.148   4.928  1.00 25.27           C  
-ATOM    957  O   PRO A 141      91.879  13.021   6.146  1.00 25.48           O  
-ATOM    958  CB  PRO A 141      92.391  11.233   3.380  1.00 25.42           C  
-ATOM    959  CG  PRO A 141      92.319  11.704   1.955  1.00 26.44           C  
-ATOM    960  CD  PRO A 141      90.839  11.736   1.704  1.00 25.82           C  
-ATOM    961  N   ASN A 142      91.932  14.297   4.300  1.00 25.34           N  
-ATOM    962  CA  ASN A 142      92.398  15.486   5.004  1.00 25.75           C  
-ATOM    963  C   ASN A 142      91.445  15.962   6.097  1.00 25.34           C  
-ATOM    964  O   ASN A 142      91.883  16.569   7.077  1.00 24.94           O  
-ATOM    965  CB  ASN A 142      92.668  16.608   4.010  1.00 27.18           C  
-ATOM    966  CG  ASN A 142      93.641  16.191   2.930  1.00 30.41           C  
-ATOM    967  OD1 ASN A 142      93.345  15.307   2.116  1.00 31.61           O  
-ATOM    968  ND2 ASN A 142      94.823  16.788   2.937  1.00 31.26           N  
-ATOM    969  N   HIS A 143      90.150  15.683   5.931  1.00 24.64           N  
-ATOM    970  CA  HIS A 143      89.136  16.069   6.922  1.00 23.88           C  
-ATOM    971  C   HIS A 143      89.454  15.452   8.280  1.00 22.85           C  
-ATOM    972  O   HIS A 143      89.507  16.137   9.301  1.00 22.43           O  
-ATOM    973  CB  HIS A 143      87.748  15.579   6.498  1.00 23.68           C  
-ATOM    974  CG  HIS A 143      87.104  16.414   5.440  1.00 23.12           C  
-ATOM    975  ND1 HIS A 143      86.266  15.884   4.484  1.00 22.79           N  
-ATOM    976  CD2 HIS A 143      87.149  17.746   5.207  1.00 23.47           C  
-ATOM    977  CE1 HIS A 143      85.816  16.856   3.710  1.00 23.13           C  
-ATOM    978  NE2 HIS A 143      86.338  17.994   4.128  1.00 22.09           N  
-ATOM    979  N   VAL A 144      89.657  14.142   8.270  1.00 22.62           N  
-ATOM    980  CA  VAL A 144      89.956  13.396   9.477  1.00 22.92           C  
-ATOM    981  C   VAL A 144      91.314  13.790  10.043  1.00 22.08           C  
-ATOM    982  O   VAL A 144      91.468  13.893  11.254  1.00 23.46           O  
-ATOM    983  CB  VAL A 144      89.906  11.878   9.208  1.00 23.34           C  
-ATOM    984  CG1 VAL A 144      90.125  11.099  10.491  1.00 23.73           C  
-ATOM    985  CG2 VAL A 144      88.569  11.508   8.584  1.00 22.72           C  
-ATOM    986  N   SER A 145      92.284  14.039   9.173  1.00 21.62           N  
-ATOM    987  CA  SER A 145      93.623  14.427   9.612  1.00 22.58           C  
-ATOM    988  C   SER A 145      93.603  15.714  10.432  1.00 21.83           C  
-ATOM    989  O   SER A 145      94.197  15.782  11.514  1.00 21.90           O  
-ATOM    990  CB  SER A 145      94.541  14.606   8.405  1.00 24.15           C  
-ATOM    991  OG  SER A 145      94.498  13.453   7.577  1.00 30.16           O  
-ATOM    992  N   ILE A 146      92.920  16.734   9.917  1.00 20.75           N  
-ATOM    993  CA  ILE A 146      92.824  18.015  10.602  1.00 19.13           C  
-ATOM    994  C   ILE A 146      92.124  17.811  11.935  1.00 18.85           C  
-ATOM    995  O   ILE A 146      92.622  18.235  12.981  1.00 18.98           O  
-ATOM    996  CB  ILE A 146      92.049  19.042   9.749  1.00 19.29           C  
-ATOM    997  CG1 ILE A 146      92.839  19.359   8.479  1.00 20.04           C  
-ATOM    998  CG2 ILE A 146      91.788  20.315  10.546  1.00 19.25           C  
-ATOM    999  CD1 ILE A 146      92.167  20.353   7.562  1.00 20.84           C  
-ATOM   1000  N   MET A 147      91.001  17.099  11.896  1.00 17.99           N  
-ATOM   1001  CA  MET A 147      90.216  16.823  13.096  1.00 17.89           C  
-ATOM   1002  C   MET A 147      91.002  16.053  14.158  1.00 17.41           C  
-ATOM   1003  O   MET A 147      90.906  16.358  15.345  1.00 16.54           O  
-ATOM   1004  CB  MET A 147      88.924  16.096  12.721  1.00 17.61           C  
-ATOM   1005  CG  MET A 147      87.902  17.011  12.054  1.00 18.48           C  
-ATOM   1006  SD  MET A 147      86.494  16.155  11.328  1.00 19.45           S  
-ATOM   1007  CE  MET A 147      86.444  16.898   9.715  1.00 20.14           C  
-ATOM   1008  N   ASN A 148      91.795  15.078  13.726  1.00 17.65           N  
-ATOM   1009  CA  ASN A 148      92.616  14.289  14.642  1.00 17.92           C  
-ATOM   1010  C   ASN A 148      93.661  15.198  15.263  1.00 18.12           C  
-ATOM   1011  O   ASN A 148      93.907  15.153  16.463  1.00 19.51           O  
-ATOM   1012  CB  ASN A 148      93.305  13.137  13.906  1.00 17.94           C  
-ATOM   1013  CG  ASN A 148      92.392  11.955  13.694  1.00 17.35           C  
-ATOM   1014  OD1 ASN A 148      91.310  11.885  14.270  1.00 18.29           O  
-ATOM   1015  ND2 ASN A 148      92.823  11.013  12.871  1.00 16.70           N  
-ATOM   1016  N   PHE A 149      94.231  16.068  14.442  1.00 18.54           N  
-ATOM   1017  CA  PHE A 149      95.236  17.005  14.904  1.00 19.19           C  
-ATOM   1018  C   PHE A 149      94.654  17.947  15.956  1.00 19.13           C  
-ATOM   1019  O   PHE A 149      95.332  18.297  16.917  1.00 19.10           O  
-ATOM   1020  CB  PHE A 149      95.792  17.798  13.715  1.00 20.45           C  
-ATOM   1021  CG  PHE A 149      96.675  18.955  14.108  1.00 20.99           C  
-ATOM   1022  CD1 PHE A 149      97.963  18.736  14.583  1.00 21.28           C  
-ATOM   1023  CD2 PHE A 149      96.210  20.263  14.005  1.00 19.99           C  
-ATOM   1024  CE1 PHE A 149      98.773  19.803  14.953  1.00 21.35           C  
-ATOM   1025  CE2 PHE A 149      97.007  21.329  14.371  1.00 20.64           C  
-ATOM   1026  CZ  PHE A 149      98.292  21.102  14.846  1.00 21.11           C  
-ATOM   1027  N   MET A 150      93.403  18.362  15.763  1.00 18.76           N  
-ATOM   1028  CA  MET A 150      92.740  19.268  16.698  1.00 18.17           C  
-ATOM   1029  C   MET A 150      92.261  18.568  17.967  1.00 18.57           C  
-ATOM   1030  O   MET A 150      91.938  19.222  18.955  1.00 18.60           O  
-ATOM   1031  CB  MET A 150      91.555  19.966  16.025  1.00 18.65           C  
-ATOM   1032  CG  MET A 150      91.929  20.976  14.945  1.00 19.08           C  
-ATOM   1033  SD  MET A 150      90.494  21.827  14.212  1.00 19.85           S  
-ATOM   1034  CE  MET A 150      89.967  22.874  15.568  1.00 17.01           C  
-ATOM   1035  N   GLY A 151      92.212  17.239  17.939  1.00 18.63           N  
-ATOM   1036  CA  GLY A 151      91.756  16.483  19.096  1.00 18.74           C  
-ATOM   1037  C   GLY A 151      90.239  16.372  19.178  1.00 19.01           C  
-ATOM   1038  O   GLY A 151      89.682  15.975  20.207  1.00 18.86           O  
-ATOM   1039  N   LEU A 152      89.572  16.683  18.073  1.00 19.14           N  
-ATOM   1040  CA  LEU A 152      88.120  16.634  18.008  1.00 19.48           C  
-ATOM   1041  C   LEU A 152      87.584  15.214  17.888  1.00 19.74           C  
-ATOM   1042  O   LEU A 152      88.190  14.366  17.229  1.00 19.76           O  
-ATOM   1043  CB  LEU A 152      87.611  17.455  16.818  1.00 18.82           C  
-ATOM   1044  CG  LEU A 152      87.756  18.974  16.832  1.00 18.04           C  
-ATOM   1045  CD1 LEU A 152      87.274  19.522  15.510  1.00 18.70           C  
-ATOM   1046  CD2 LEU A 152      86.957  19.571  17.969  1.00 18.77           C  
-ATOM   1047  N   PRO A 154      86.468  14.923  18.577  1.00 19.60           N  
-ATOM   1048  CA  PRO A 154      85.845  13.598  18.531  1.00 19.69           C  
-ATOM   1049  C   PRO A 154      85.241  13.464  17.132  1.00 20.21           C  
-ATOM   1050  O   PRO A 154      84.516  14.359  16.692  1.00 19.79           O  
-ATOM   1051  CB  PRO A 154      84.736  13.707  19.581  1.00 19.02           C  
-ATOM   1052  CG  PRO A 154      85.249  14.750  20.528  1.00 19.79           C  
-ATOM   1053  CD  PRO A 154      85.817  15.772  19.590  1.00 18.68           C  
-ATOM   1054  N   VAL A 155      85.567  12.384  16.424  1.00 21.21           N  
-ATOM   1055  CA  VAL A 155      85.048  12.168  15.072  1.00 21.58           C  
-ATOM   1056  C   VAL A 155      84.154  10.936  14.997  1.00 23.12           C  
-ATOM   1057  O   VAL A 155      84.508   9.858  15.481  1.00 23.37           O  
-ATOM   1058  CB  VAL A 155      86.183  12.060  14.027  1.00 20.43           C  
-ATOM   1059  CG1 VAL A 155      85.619  11.738  12.652  1.00 19.38           C  
-ATOM   1060  CG2 VAL A 155      86.954  13.365  13.970  1.00 20.53           C  
-ATOM   1061  N   GLN A 156      83.011  11.108  14.347  1.00 24.35           N  
-ATOM   1062  CA  GLN A 156      82.023  10.061  14.192  1.00 25.48           C  
-ATOM   1063  C   GLN A 156      81.773   9.876  12.701  1.00 24.18           C  
-ATOM   1064  O   GLN A 156      81.814  10.834  11.934  1.00 24.65           O  
-ATOM   1065  CB  GLN A 156      80.729  10.491  14.882  1.00 28.70           C  
-ATOM   1066  CG  GLN A 156      79.811   9.355  15.269  1.00 33.57           C  
-ATOM   1067  CD  GLN A 156      80.119   8.802  16.643  1.00 35.95           C  
-ATOM   1068  OE1 GLN A 156      81.277   8.588  16.996  1.00 38.56           O  
-ATOM   1069  NE2 GLN A 156      79.078   8.556  17.424  1.00 37.42           N  
-ATOM   1070  N   THR A 157      81.475   8.650  12.300  1.00 22.96           N  
-ATOM   1071  CA  THR A 157      81.222   8.339  10.903  1.00 21.67           C  
-ATOM   1072  C   THR A 157      79.752   7.990  10.620  1.00 20.83           C  
-ATOM   1073  O   THR A 157      79.037   7.484  11.497  1.00 21.66           O  
-ATOM   1074  CB  THR A 157      82.144   7.172  10.466  1.00 22.22           C  
-ATOM   1075  OG1 THR A 157      83.500   7.639  10.369  1.00 23.52           O  
-ATOM   1076  CG2 THR A 157      81.719   6.602   9.146  1.00 22.78           C  
-ATOM   1077  N   TYR A 158      79.287   8.345   9.425  1.00 18.47           N  
-ATOM   1078  CA  TYR A 158      77.935   8.024   8.989  1.00 16.89           C  
-ATOM   1079  C   TYR A 158      78.080   7.331   7.647  1.00 17.14           C  
-ATOM   1080  O   TYR A 158      78.915   7.729   6.825  1.00 17.38           O  
-ATOM   1081  CB  TYR A 158      77.028   9.268   8.901  1.00 15.56           C  
-ATOM   1082  CG  TYR A 158      77.407  10.355   7.904  1.00 14.01           C  
-ATOM   1083  CD1 TYR A 158      77.098  10.232   6.550  1.00 13.21           C  
-ATOM   1084  CD2 TYR A 158      78.002  11.544   8.331  1.00 14.01           C  
-ATOM   1085  CE1 TYR A 158      77.367  11.263   5.648  1.00 11.79           C  
-ATOM   1086  CE2 TYR A 158      78.277  12.584   7.434  1.00 13.14           C  
-ATOM   1087  CZ  TYR A 158      77.955  12.436   6.095  1.00 12.93           C  
-ATOM   1088  OH  TYR A 158      78.223  13.460   5.201  1.00 11.88           O  
-ATOM   1089  N   ARG A 159      77.333   6.246   7.461  1.00 17.39           N  
-ATOM   1090  CA  ARG A 159      77.387   5.474   6.220  1.00 17.02           C  
-ATOM   1091  C   ARG A 159      77.075   6.363   5.030  1.00 16.59           C  
-ATOM   1092  O   ARG A 159      76.284   7.303   5.140  1.00 16.43           O  
-ATOM   1093  CB  ARG A 159      76.435   4.279   6.283  1.00 16.38           C  
-ATOM   1094  CG  ARG A 159      76.987   3.110   7.082  1.00 16.90           C  
-ATOM   1095  CD  ARG A 159      75.907   2.098   7.436  1.00 18.07           C  
-ATOM   1096  NE  ARG A 159      74.980   2.613   8.445  1.00 19.23           N  
-ATOM   1097  CZ  ARG A 159      73.835   2.027   8.788  1.00 20.04           C  
-ATOM   1098  NH1 ARG A 159      73.445   0.912   8.181  1.00 19.52           N  
-ATOM   1099  NH2 ARG A 159      73.064   2.569   9.723  1.00 19.66           N  
-ATOM   1100  N   TYR A 160      77.721   6.084   3.904  1.00 16.29           N  
-ATOM   1101  CA  TYR A 160      77.519   6.889   2.714  1.00 16.43           C  
-ATOM   1102  C   TYR A 160      77.701   6.127   1.400  1.00 17.74           C  
-ATOM   1103  O   TYR A 160      76.774   6.034   0.599  1.00 18.76           O  
-ATOM   1104  CB  TYR A 160      78.442   8.115   2.756  1.00 14.10           C  
-ATOM   1105  CG  TYR A 160      78.170   9.104   1.654  1.00 12.30           C  
-ATOM   1106  CD1 TYR A 160      77.205  10.098   1.809  1.00 10.36           C  
-ATOM   1107  CD2 TYR A 160      78.834   9.008   0.431  1.00 11.55           C  
-ATOM   1108  CE1 TYR A 160      76.903  10.969   0.767  1.00 10.68           C  
-ATOM   1109  CE2 TYR A 160      78.540   9.867  -0.614  1.00 10.65           C  
-ATOM   1110  CZ  TYR A 160      77.574  10.843  -0.440  1.00 10.73           C  
-ATOM   1111  OH  TYR A 160      77.282  11.682  -1.483  1.00 12.21           O  
-ATOM   1112  N   PHE A 161      78.885   5.579   1.168  1.00 19.44           N  
-ATOM   1113  CA  PHE A 161      79.134   4.873  -0.079  1.00 20.44           C  
-ATOM   1114  C   PHE A 161      78.699   3.433   0.006  1.00 22.18           C  
-ATOM   1115  O   PHE A 161      79.083   2.717   0.931  1.00 23.08           O  
-ATOM   1116  CB  PHE A 161      80.618   4.923  -0.440  1.00 20.00           C  
-ATOM   1117  CG  PHE A 161      80.924   4.473  -1.848  1.00 19.97           C  
-ATOM   1118  CD1 PHE A 161      80.440   5.182  -2.942  1.00 20.46           C  
-ATOM   1119  CD2 PHE A 161      81.745   3.378  -2.079  1.00 20.32           C  
-ATOM   1120  CE1 PHE A 161      80.776   4.811  -4.248  1.00 20.20           C  
-ATOM   1121  CE2 PHE A 161      82.085   3.002  -3.378  1.00 20.17           C  
-ATOM   1122  CZ  PHE A 161      81.599   3.723  -4.462  1.00 20.34           C  
-ATOM   1123  N   ASP A 162      77.892   3.011  -0.957  1.00 23.71           N  
-ATOM   1124  CA  ASP A 162      77.440   1.634  -1.005  1.00 24.65           C  
-ATOM   1125  C   ASP A 162      78.384   0.928  -1.962  1.00 24.15           C  
-ATOM   1126  O   ASP A 162      78.275   1.079  -3.176  1.00 23.04           O  
-ATOM   1127  CB  ASP A 162      76.001   1.542  -1.514  1.00 27.36           C  
-ATOM   1128  CG  ASP A 162      75.405   0.160  -1.318  1.00 29.21           C  
-ATOM   1129  OD1 ASP A 162      75.902  -0.809  -1.937  1.00 30.67           O  
-ATOM   1130  OD2 ASP A 162      74.446   0.041  -0.526  1.00 31.51           O  
-ATOM   1131  N   ALA A 163      79.312   0.168  -1.397  1.00 24.80           N  
-ATOM   1132  CA  ALA A 163      80.318  -0.574  -2.151  1.00 25.18           C  
-ATOM   1133  C   ALA A 163      79.802  -1.441  -3.296  1.00 25.73           C  
-ATOM   1134  O   ALA A 163      80.496  -1.623  -4.292  1.00 25.69           O  
-ATOM   1135  CB  ALA A 163      81.136  -1.422  -1.199  1.00 26.03           C  
-ATOM   1136  N   GLU A 164      78.594  -1.978  -3.153  1.00 26.66           N  
-ATOM   1137  CA  GLU A 164      78.020  -2.839  -4.179  1.00 27.08           C  
-ATOM   1138  C   GLU A 164      77.402  -2.100  -5.360  1.00 26.61           C  
-ATOM   1139  O   GLU A 164      77.602  -2.477  -6.517  1.00 26.30           O  
-ATOM   1140  CB  GLU A 164      76.986  -3.781  -3.565  1.00 30.08           C  
-ATOM   1141  CG  GLU A 164      76.288  -4.671  -4.588  1.00 35.27           C  
-ATOM   1142  CD  GLU A 164      75.468  -5.780  -3.955  1.00 38.33           C  
-ATOM   1143  OE1 GLU A 164      74.622  -5.490  -3.076  1.00 39.43           O  
-ATOM   1144  OE2 GLU A 164      75.672  -6.949  -4.350  1.00 40.51           O  
-ATOM   1145  N   THR A 165      76.624  -1.070  -5.070  1.00 25.67           N  
-ATOM   1146  CA  THR A 165      75.974  -0.313  -6.128  1.00 25.79           C  
-ATOM   1147  C   THR A 165      76.789   0.907  -6.544  1.00 25.08           C  
-ATOM   1148  O   THR A 165      76.519   1.521  -7.581  1.00 26.65           O  
-ATOM   1149  CB  THR A 165      74.573   0.149  -5.682  1.00 26.28           C  
-ATOM   1150  OG1 THR A 165      74.691   0.962  -4.507  1.00 27.82           O  
-ATOM   1151  CG2 THR A 165      73.691  -1.054  -5.368  1.00 27.56           C  
-ATOM   1152  N   ARG A 166      77.803   1.229  -5.746  1.00 23.29           N  
-ATOM   1153  CA  ARG A 166      78.648   2.393  -5.974  1.00 21.45           C  
-ATOM   1154  C   ARG A 166      77.784   3.648  -5.920  1.00 20.38           C  
-ATOM   1155  O   ARG A 166      78.124   4.676  -6.507  1.00 20.13           O  
-ATOM   1156  CB  ARG A 166      79.382   2.313  -7.315  1.00 21.76           C  
-ATOM   1157  CG  ARG A 166      80.598   1.399  -7.348  1.00 22.59           C  
-ATOM   1158  CD  ARG A 166      80.222  -0.068  -7.461  1.00 22.84           C  
-ATOM   1159  NE  ARG A 166      81.338  -0.851  -7.986  1.00 23.97           N  
-ATOM   1160  CZ  ARG A 166      81.437  -2.174  -7.916  1.00 24.16           C  
-ATOM   1161  NH1 ARG A 166      80.491  -2.888  -7.322  1.00 24.57           N  
-ATOM   1162  NH2 ARG A 166      82.496  -2.785  -8.431  1.00 24.50           N  
-ATOM   1163  N   GLY A 167      76.664   3.549  -5.211  1.00 19.44           N  
-ATOM   1164  CA  GLY A 167      75.753   4.669  -5.076  1.00 18.37           C  
-ATOM   1165  C   GLY A 167      75.701   5.078  -3.622  1.00 18.65           C  
-ATOM   1166  O   GLY A 167      76.538   4.641  -2.833  1.00 19.09           O  
-ATOM   1167  N   VAL A 168      74.719   5.896  -3.257  1.00 18.65           N  
-ATOM   1168  CA  VAL A 168      74.585   6.355  -1.879  1.00 18.04           C  
-ATOM   1169  C   VAL A 168      73.701   5.440  -1.034  1.00 18.94           C  
-ATOM   1170  O   VAL A 168      72.565   5.123  -1.412  1.00 19.82           O  
-ATOM   1171  CB  VAL A 168      74.005   7.801  -1.813  1.00 17.76           C  
-ATOM   1172  CG1 VAL A 168      73.778   8.222  -0.364  1.00 17.71           C  
-ATOM   1173  CG2 VAL A 168      74.945   8.787  -2.495  1.00 16.93           C  
-ATOM   1174  N   ASP A 169      74.228   4.997   0.101  1.00 18.56           N  
-ATOM   1175  CA  ASP A 169      73.457   4.171   1.017  1.00 18.55           C  
-ATOM   1176  C   ASP A 169      72.644   5.160   1.863  1.00 18.40           C  
-ATOM   1177  O   ASP A 169      72.954   5.404   3.030  1.00 18.18           O  
-ATOM   1178  CB  ASP A 169      74.401   3.346   1.895  1.00 18.65           C  
-ATOM   1179  CG  ASP A 169      73.667   2.476   2.895  1.00 18.54           C  
-ATOM   1180  OD1 ASP A 169      72.437   2.293   2.761  1.00 20.86           O  
-ATOM   1181  OD2 ASP A 169      74.321   1.980   3.833  1.00 19.00           O  
-ATOM   1182  N   PHE A 170      71.603   5.735   1.269  1.00 19.73           N  
-ATOM   1183  CA  PHE A 170      70.793   6.729   1.974  1.00 20.32           C  
-ATOM   1184  C   PHE A 170      70.132   6.276   3.269  1.00 20.82           C  
-ATOM   1185  O   PHE A 170      70.136   7.019   4.250  1.00 21.78           O  
-ATOM   1186  CB  PHE A 170      69.752   7.361   1.051  1.00 20.41           C  
-ATOM   1187  CG  PHE A 170      69.269   8.705   1.527  1.00 21.00           C  
-ATOM   1188  CD1 PHE A 170      70.181   9.697   1.882  1.00 20.69           C  
-ATOM   1189  CD2 PHE A 170      67.911   8.983   1.620  1.00 20.86           C  
-ATOM   1190  CE1 PHE A 170      69.743  10.940   2.320  1.00 21.35           C  
-ATOM   1191  CE2 PHE A 170      67.465  10.228   2.058  1.00 20.23           C  
-ATOM   1192  CZ  PHE A 170      68.380  11.205   2.407  1.00 20.54           C  
-ATOM   1193  N   GLU A 171      69.561   5.076   3.282  1.00 20.92           N  
-ATOM   1194  CA  GLU A 171      68.914   4.571   4.489  1.00 21.33           C  
-ATOM   1195  C   GLU A 171      69.922   4.522   5.626  1.00 20.66           C  
-ATOM   1196  O   GLU A 171      69.611   4.915   6.750  1.00 20.66           O  
-ATOM   1197  CB  GLU A 171      68.316   3.181   4.257  1.00 24.06           C  
-ATOM   1198  CG  GLU A 171      67.173   3.148   3.244  1.00 28.17           C  
-ATOM   1199  CD  GLU A 171      66.034   4.081   3.619  1.00 31.49           C  
-ATOM   1200  OE1 GLU A 171      65.529   3.974   4.761  1.00 33.62           O  
-ATOM   1201  OE2 GLU A 171      65.656   4.933   2.780  1.00 33.53           O  
-ATOM   1202  N   GLY A 172      71.139   4.075   5.316  1.00 19.53           N  
-ATOM   1203  CA  GLY A 172      72.186   3.996   6.321  1.00 18.00           C  
-ATOM   1204  C   GLY A 172      72.605   5.373   6.792  1.00 16.91           C  
-ATOM   1205  O   GLY A 172      72.748   5.621   7.991  1.00 17.12           O  
-ATOM   1206  N   MET A 173      72.785   6.280   5.839  1.00 16.81           N  
-ATOM   1207  CA  MET A 173      73.175   7.652   6.141  1.00 16.85           C  
-ATOM   1208  C   MET A 173      72.167   8.273   7.109  1.00 17.39           C  
-ATOM   1209  O   MET A 173      72.544   8.878   8.113  1.00 17.73           O  
-ATOM   1210  CB  MET A 173      73.245   8.464   4.841  1.00 15.62           C  
-ATOM   1211  CG  MET A 173      73.608   9.930   5.012  1.00 13.68           C  
-ATOM   1212  SD  MET A 173      73.752  10.756   3.420  1.00 15.48           S  
-ATOM   1213  CE  MET A 173      74.036  12.412   3.937  1.00 12.92           C  
-ATOM   1214  N   LYS A 174      70.884   8.089   6.813  1.00 19.12           N  
-ATOM   1215  CA  LYS A 174      69.809   8.624   7.644  1.00 20.37           C  
-ATOM   1216  C   LYS A 174      69.812   8.012   9.041  1.00 19.90           C  
-ATOM   1217  O   LYS A 174      69.727   8.727  10.044  1.00 20.65           O  
-ATOM   1218  CB  LYS A 174      68.450   8.402   6.972  1.00 21.71           C  
-ATOM   1219  CG  LYS A 174      68.234   9.242   5.723  1.00 24.46           C  
-ATOM   1220  CD  LYS A 174      66.762   9.311   5.337  1.00 27.35           C  
-ATOM   1221  CE  LYS A 174      66.270   8.102   4.531  1.00 28.64           C  
-ATOM   1222  NZ  LYS A 174      66.417   6.798   5.223  1.00 31.04           N  
-ATOM   1223  N   ALA A 175      69.930   6.692   9.107  1.00 19.65           N  
-ATOM   1224  CA  ALA A 175      69.955   5.992  10.383  1.00 19.92           C  
-ATOM   1225  C   ALA A 175      71.101   6.475  11.277  1.00 21.33           C  
-ATOM   1226  O   ALA A 175      70.907   6.681  12.478  1.00 22.81           O  
-ATOM   1227  CB  ALA A 175      70.058   4.497  10.157  1.00 19.01           C  
-ATOM   1228  N   ASP A 176      72.282   6.678  10.690  1.00 21.51           N  
-ATOM   1229  CA  ASP A 176      73.452   7.127  11.450  1.00 21.18           C  
-ATOM   1230  C   ASP A 176      73.383   8.588  11.889  1.00 21.28           C  
-ATOM   1231  O   ASP A 176      73.747   8.932  13.019  1.00 21.31           O  
-ATOM   1232  CB  ASP A 176      74.737   6.886  10.652  1.00 21.22           C  
-ATOM   1233  CG  ASP A 176      75.100   5.413  10.539  1.00 20.61           C  
-ATOM   1234  OD1 ASP A 176      74.542   4.580  11.287  1.00 21.78           O  
-ATOM   1235  OD2 ASP A 176      75.962   5.088   9.704  1.00 19.91           O  
-ATOM   1236  N   LEU A 177      72.920   9.452  10.992  1.00 21.60           N  
-ATOM   1237  CA  LEU A 177      72.809  10.867  11.300  1.00 21.24           C  
-ATOM   1238  C   LEU A 177      71.776  11.125  12.373  1.00 22.48           C  
-ATOM   1239  O   LEU A 177      71.858  12.126  13.083  1.00 22.49           O  
-ATOM   1240  CB  LEU A 177      72.475  11.665  10.047  1.00 20.18           C  
-ATOM   1241  CG  LEU A 177      73.656  11.838   9.100  1.00 20.07           C  
-ATOM   1242  CD1 LEU A 177      73.229  12.547   7.833  1.00 20.23           C  
-ATOM   1243  CD2 LEU A 177      74.737  12.622   9.814  1.00 20.65           C  
-ATOM   1244  N   ALA A 178      70.814  10.215  12.507  1.00 24.35           N  
-ATOM   1245  CA  ALA A 178      69.761  10.358  13.513  1.00 25.82           C  
-ATOM   1246  C   ALA A 178      70.328  10.390  14.937  1.00 25.92           C  
-ATOM   1247  O   ALA A 178      69.698  10.920  15.857  1.00 26.38           O  
-ATOM   1248  CB  ALA A 178      68.737   9.236  13.371  1.00 26.18           C  
-ATOM   1249  N   ALA A 179      71.531   9.848  15.102  1.00 25.45           N  
-ATOM   1250  CA  ALA A 179      72.187   9.811  16.398  1.00 25.55           C  
-ATOM   1251  C   ALA A 179      72.883  11.121  16.767  1.00 26.21           C  
-ATOM   1252  O   ALA A 179      73.447  11.241  17.853  1.00 26.96           O  
-ATOM   1253  CB  ALA A 179      73.172   8.672  16.432  1.00 25.45           C  
-ATOM   1254  N   ALA A 180      72.886  12.087  15.857  1.00 27.16           N  
-ATOM   1255  CA  ALA A 180      73.524  13.373  16.131  1.00 28.60           C  
-ATOM   1256  C   ALA A 180      72.719  14.134  17.175  1.00 29.75           C  
-ATOM   1257  O   ALA A 180      71.491  14.061  17.195  1.00 30.43           O  
-ATOM   1258  CB  ALA A 180      73.641  14.199  14.851  1.00 27.86           C  
-ATOM   1259  N   LYS A 181      73.417  14.829  18.065  1.00 30.92           N  
-ATOM   1260  CA  LYS A 181      72.763  15.612  19.104  1.00 32.14           C  
-ATOM   1261  C   LYS A 181      72.905  17.095  18.756  1.00 32.13           C  
-ATOM   1262  O   LYS A 181      73.673  17.467  17.861  1.00 31.77           O  
-ATOM   1263  CB  LYS A 181      73.409  15.345  20.472  1.00 33.87           C  
-ATOM   1264  CG  LYS A 181      73.668  13.876  20.791  1.00 36.30           C  
-ATOM   1265  CD  LYS A 181      72.385  13.051  20.775  1.00 39.13           C  
-ATOM   1266  CE  LYS A 181      72.684  11.556  20.869  1.00 40.20           C  
-ATOM   1267  NZ  LYS A 181      71.471  10.718  20.627  1.00 41.60           N  
-ATOM   1268  N   LYS A 182      72.166  17.936  19.467  1.00 32.54           N  
-ATOM   1269  CA  LYS A 182      72.219  19.377  19.265  1.00 32.44           C  
-ATOM   1270  C   LYS A 182      73.624  19.830  19.628  1.00 32.03           C  
-ATOM   1271  O   LYS A 182      74.156  19.429  20.666  1.00 32.50           O  
-ATOM   1272  CB  LYS A 182      71.193  20.065  20.169  1.00 34.20           C  
-ATOM   1273  CG  LYS A 182      71.198  21.583  20.112  1.00 36.72           C  
-ATOM   1274  CD  LYS A 182      70.006  22.146  20.871  1.00 38.88           C  
-ATOM   1275  CE  LYS A 182      69.984  23.671  20.855  1.00 40.19           C  
-ATOM   1276  NZ  LYS A 182      71.079  24.262  21.678  1.00 42.26           N  
-ATOM   1277  N   GLY A 183      74.242  20.626  18.761  1.00 30.83           N  
-ATOM   1278  CA  GLY A 183      75.589  21.093  19.036  1.00 29.54           C  
-ATOM   1279  C   GLY A 183      76.663  20.336  18.270  1.00 28.88           C  
-ATOM   1280  O   GLY A 183      77.809  20.788  18.188  1.00 29.39           O  
-ATOM   1281  N   ASP A 184      76.318  19.162  17.753  1.00 26.68           N  
-ATOM   1282  CA  ASP A 184      77.263  18.379  16.972  1.00 24.09           C  
-ATOM   1283  C   ASP A 184      77.329  18.996  15.586  1.00 22.50           C  
-ATOM   1284  O   ASP A 184      76.438  19.744  15.186  1.00 21.94           O  
-ATOM   1285  CB  ASP A 184      76.813  16.917  16.868  1.00 24.35           C  
-ATOM   1286  CG  ASP A 184      77.011  16.145  18.159  1.00 24.81           C  
-ATOM   1287  OD1 ASP A 184      77.751  16.627  19.045  1.00 25.64           O  
-ATOM   1288  OD2 ASP A 184      76.440  15.042  18.282  1.00 24.16           O  
-ATOM   1289  N   MET A 185      78.369  18.653  14.844  1.00 20.76           N  
-ATOM   1290  CA  MET A 185      78.564  19.177  13.509  1.00 19.28           C  
-ATOM   1291  C   MET A 185      78.532  18.031  12.512  1.00 18.31           C  
-ATOM   1292  O   MET A 185      79.115  16.975  12.755  1.00 19.19           O  
-ATOM   1293  CB  MET A 185      79.907  19.899  13.455  1.00 21.55           C  
-ATOM   1294  CG  MET A 185      80.308  20.448  12.102  1.00 23.77           C  
-ATOM   1295  SD  MET A 185      81.763  21.511  12.283  1.00 28.50           S  
-ATOM   1296  CE  MET A 185      80.966  23.058  12.568  1.00 25.15           C  
-ATOM   1297  N   VAL A 186      77.819  18.222  11.411  1.00 15.95           N  
-ATOM   1298  CA  VAL A 186      77.725  17.205  10.375  1.00 14.43           C  
-ATOM   1299  C   VAL A 186      78.348  17.788   9.108  1.00 14.65           C  
-ATOM   1300  O   VAL A 186      77.878  18.802   8.586  1.00 13.60           O  
-ATOM   1301  CB  VAL A 186      76.257  16.799  10.108  1.00 14.37           C  
-ATOM   1302  CG1 VAL A 186      76.182  15.771   8.981  1.00 13.63           C  
-ATOM   1303  CG2 VAL A 186      75.627  16.239  11.374  1.00 12.98           C  
-ATOM   1304  N   LEU A 187      79.413  17.151   8.626  1.00 14.60           N  
-ATOM   1305  CA  LEU A 187      80.111  17.625   7.436  1.00 15.66           C  
-ATOM   1306  C   LEU A 187      79.532  16.983   6.187  1.00 15.01           C  
-ATOM   1307  O   LEU A 187      79.559  15.758   6.051  1.00 15.28           O  
-ATOM   1308  CB  LEU A 187      81.613  17.314   7.543  1.00 16.47           C  
-ATOM   1309  CG  LEU A 187      82.621  18.132   6.723  1.00 17.27           C  
-ATOM   1310  CD1 LEU A 187      84.014  17.673   7.088  1.00 18.61           C  
-ATOM   1311  CD2 LEU A 187      82.414  17.992   5.225  1.00 17.22           C  
-ATOM   1312  N   LEU A 188      79.054  17.819   5.267  1.00 15.57           N  
-ATOM   1313  CA  LEU A 188      78.463  17.368   4.008  1.00 15.58           C  
-ATOM   1314  C   LEU A 188      79.193  17.958   2.811  1.00 15.67           C  
-ATOM   1315  O   LEU A 188      79.538  19.136   2.808  1.00 15.48           O  
-ATOM   1316  CB  LEU A 188      77.001  17.821   3.875  1.00 15.42           C  
-ATOM   1317  CG  LEU A 188      75.806  17.362   4.710  1.00 16.15           C  
-ATOM   1318  CD1 LEU A 188      75.913  15.886   5.034  1.00 17.39           C  
-ATOM   1319  CD2 LEU A 188      75.689  18.203   5.959  1.00 17.51           C  
-ATOM   1320  N   HIS A 189      79.399  17.152   1.778  1.00 16.20           N  
-ATOM   1321  CA  HIS A 189      80.028  17.652   0.565  1.00 16.70           C  
-ATOM   1322  C   HIS A 189      78.862  18.263  -0.214  1.00 17.26           C  
-ATOM   1323  O   HIS A 189      77.849  17.597  -0.441  1.00 17.63           O  
-ATOM   1324  CB  HIS A 189      80.641  16.515  -0.256  1.00 17.85           C  
-ATOM   1325  CG  HIS A 189      81.781  15.815   0.419  1.00 18.73           C  
-ATOM   1326  ND1 HIS A 189      82.999  15.614  -0.197  1.00 18.42           N  
-ATOM   1327  CD2 HIS A 189      81.880  15.239   1.641  1.00 18.78           C  
-ATOM   1328  CE1 HIS A 189      83.795  14.943   0.612  1.00 18.57           C  
-ATOM   1329  NE2 HIS A 189      83.141  14.702   1.734  1.00 18.98           N  
-ATOM   1330  N   GLY A 190      78.986  19.532  -0.582  1.00 16.71           N  
-ATOM   1331  CA  GLY A 190      77.929  20.192  -1.321  1.00 15.89           C  
-ATOM   1332  C   GLY A 190      77.617  19.513  -2.638  1.00 15.41           C  
-ATOM   1333  O   GLY A 190      76.456  19.474  -3.056  1.00 15.41           O  
-ATOM   1334  N   CYS A 191      78.653  19.009  -3.305  1.00 14.48           N  
-ATOM   1335  CA  CYS A 191      78.502  18.321  -4.583  1.00 14.12           C  
-ATOM   1336  C   CYS A 191      79.797  17.597  -4.931  1.00 14.86           C  
-ATOM   1337  O   CYS A 191      80.787  17.724  -4.214  1.00 14.12           O  
-ATOM   1338  CB  CYS A 191      78.164  19.320  -5.692  1.00 14.45           C  
-ATOM   1339  SG  CYS A 191      79.446  20.555  -6.018  1.00 16.64           S  
-ATOM   1340  N   CYS A 192      79.774  16.826  -6.020  1.00 15.76           N  
-ATOM   1341  CA  CYS A 192      80.940  16.084  -6.509  1.00 15.77           C  
-ATOM   1342  C   CYS A 192      81.752  15.492  -5.369  1.00 15.40           C  
-ATOM   1343  O   CYS A 192      82.918  15.860  -5.158  1.00 15.26           O  
-ATOM   1344  CB  CYS A 192      81.824  17.003  -7.353  1.00 16.47           C  
-ATOM   1345  SG  CYS A 192      80.934  17.834  -8.684  1.00 16.53           S  
-ATOM   1346  N   HIS A 193      81.121  14.581  -4.634  1.00 13.77           N  
-ATOM   1347  CA  HIS A 193      81.736  13.936  -3.488  1.00 13.50           C  
-ATOM   1348  C   HIS A 193      83.109  13.351  -3.827  1.00 13.86           C  
-ATOM   1349  O   HIS A 193      83.263  12.589  -4.781  1.00 14.14           O  
-ATOM   1350  CB  HIS A 193      80.797  12.860  -2.925  1.00 12.31           C  
-ATOM   1351  CG  HIS A 193      81.234  12.298  -1.606  1.00 12.63           C  
-ATOM   1352  ND1 HIS A 193      81.993  11.154  -1.502  1.00 13.53           N  
-ATOM   1353  CD2 HIS A 193      81.030  12.726  -0.337  1.00 13.15           C  
-ATOM   1354  CE1 HIS A 193      82.243  10.902  -0.229  1.00 12.96           C  
-ATOM   1355  NE2 HIS A 193      81.670  11.841   0.499  1.00 13.55           N  
-ATOM   1356  N   ASN A 194      84.111  13.794  -3.076  1.00 14.86           N  
-ATOM   1357  CA  ASN A 194      85.497  13.342  -3.214  1.00 14.76           C  
-ATOM   1358  C   ASN A 194      85.664  12.407  -2.017  1.00 14.53           C  
-ATOM   1359  O   ASN A 194      85.487  12.835  -0.869  1.00 15.42           O  
-ATOM   1360  CB  ASN A 194      86.430  14.559  -3.093  1.00 15.82           C  
-ATOM   1361  CG  ASN A 194      87.913  14.202  -3.193  1.00 16.75           C  
-ATOM   1362  OD1 ASN A 194      88.285  13.028  -3.252  1.00 16.37           O  
-ATOM   1363  ND2 ASN A 194      88.764  15.228  -3.215  1.00 15.26           N  
-ATOM   1364  N   PRO A 195      86.102  11.156  -2.240  1.00 13.90           N  
-ATOM   1365  CA  PRO A 195      86.492  10.454  -3.467  1.00 14.03           C  
-ATOM   1366  C   PRO A 195      85.464   9.666  -4.291  1.00 14.85           C  
-ATOM   1367  O   PRO A 195      85.738   9.336  -5.444  1.00 14.40           O  
-ATOM   1368  CB  PRO A 195      87.531   9.478  -2.935  1.00 14.41           C  
-ATOM   1369  CG  PRO A 195      86.889   9.016  -1.670  1.00 12.78           C  
-ATOM   1370  CD  PRO A 195      86.384  10.316  -1.059  1.00 13.28           C  
-ATOM   1371  N   THR A 196      84.301   9.359  -3.724  1.00 14.51           N  
-ATOM   1372  CA  THR A 196      83.331   8.516  -4.422  1.00 14.00           C  
-ATOM   1373  C   THR A 196      82.722   8.951  -5.743  1.00 14.38           C  
-ATOM   1374  O   THR A 196      82.634   8.150  -6.677  1.00 14.62           O  
-ATOM   1375  CB  THR A 196      82.196   8.069  -3.488  1.00 13.84           C  
-ATOM   1376  OG1 THR A 196      81.336   9.179  -3.203  1.00 15.24           O  
-ATOM   1377  CG2 THR A 196      82.771   7.544  -2.187  1.00 13.41           C  
-ATOM   1378  N   GLY A 197      82.265  10.194  -5.814  1.00 15.14           N  
-ATOM   1379  CA  GLY A 197      81.621  10.671  -7.024  1.00 14.90           C  
-ATOM   1380  C   GLY A 197      80.123  10.403  -6.960  1.00 15.46           C  
-ATOM   1381  O   GLY A 197      79.387  10.740  -7.892  1.00 15.39           O  
-ATOM   1382  N   ALA A 198      79.681   9.762  -5.876  1.00 15.62           N  
-ATOM   1383  CA  ALA A 198      78.270   9.439  -5.655  1.00 15.41           C  
-ATOM   1384  C   ALA A 198      77.641  10.609  -4.913  1.00 16.28           C  
-ATOM   1385  O   ALA A 198      78.107  10.991  -3.838  1.00 15.06           O  
-ATOM   1386  CB  ALA A 198      78.136   8.167  -4.833  1.00 14.96           C  
-ATOM   1387  N   ASN A 199      76.556  11.145  -5.463  1.00 16.92           N  
-ATOM   1388  CA  ASN A 199      75.912  12.305  -4.860  1.00 18.01           C  
-ATOM   1389  C   ASN A 199      74.444  12.168  -4.485  1.00 17.98           C  
-ATOM   1390  O   ASN A 199      73.725  11.294  -4.991  1.00 17.10           O  
-ATOM   1391  CB  ASN A 199      76.099  13.521  -5.767  1.00 17.98           C  
-ATOM   1392  CG  ASN A 199      77.561  13.856  -5.983  1.00 17.87           C  
-ATOM   1393  OD1 ASN A 199      78.249  14.299  -5.063  1.00 18.88           O  
-ATOM   1394  ND2 ASN A 199      78.043  13.655  -7.202  1.00 17.13           N  
-ATOM   1395  N   LEU A 200      74.022  13.049  -3.579  1.00 17.38           N  
-ATOM   1396  CA  LEU A 200      72.652  13.100  -3.086  1.00 16.51           C  
-ATOM   1397  C   LEU A 200      71.795  13.861  -4.081  1.00 15.91           C  
-ATOM   1398  O   LEU A 200      72.278  14.784  -4.744  1.00 16.51           O  
-ATOM   1399  CB  LEU A 200      72.597  13.839  -1.743  1.00 16.57           C  
-ATOM   1400  CG  LEU A 200      73.437  13.330  -0.566  1.00 16.32           C  
-ATOM   1401  CD1 LEU A 200      73.243  14.248   0.631  1.00 16.41           C  
-ATOM   1402  CD2 LEU A 200      73.049  11.908  -0.209  1.00 16.36           C  
-ATOM   1403  N   THR A 201      70.539  13.450  -4.215  1.00 14.96           N  
-ATOM   1404  CA  THR A 201      69.608  14.131  -5.105  1.00 13.28           C  
-ATOM   1405  C   THR A 201      69.000  15.270  -4.283  1.00 12.58           C  
-ATOM   1406  O   THR A 201      69.079  15.267  -3.051  1.00 12.90           O  
-ATOM   1407  CB  THR A 201      68.477  13.197  -5.541  1.00 12.45           C  
-ATOM   1408  OG1 THR A 201      67.782  12.726  -4.383  1.00 12.54           O  
-ATOM   1409  CG2 THR A 201      69.020  12.013  -6.314  1.00 12.64           C  
-ATOM   1410  N   LEU A 202      68.357  16.222  -4.946  1.00 12.31           N  
-ATOM   1411  CA  LEU A 202      67.750  17.333  -4.229  1.00 12.51           C  
-ATOM   1412  C   LEU A 202      66.709  16.832  -3.208  1.00 13.11           C  
-ATOM   1413  O   LEU A 202      66.602  17.381  -2.106  1.00 12.31           O  
-ATOM   1414  CB  LEU A 202      67.152  18.333  -5.220  1.00 11.92           C  
-ATOM   1415  CG  LEU A 202      66.840  19.744  -4.713  1.00 13.18           C  
-ATOM   1416  CD1 LEU A 202      68.005  20.314  -3.904  1.00 12.31           C  
-ATOM   1417  CD2 LEU A 202      66.516  20.637  -5.899  1.00 12.42           C  
-ATOM   1418  N   ASP A 203      65.983  15.764  -3.550  1.00 13.27           N  
-ATOM   1419  CA  ASP A 203      64.994  15.188  -2.634  1.00 13.54           C  
-ATOM   1420  C   ASP A 203      65.661  14.609  -1.385  1.00 13.33           C  
-ATOM   1421  O   ASP A 203      65.168  14.790  -0.271  1.00 13.72           O  
-ATOM   1422  CB  ASP A 203      64.150  14.110  -3.333  1.00 13.95           C  
-ATOM   1423  CG  ASP A 203      62.961  14.696  -4.088  1.00 14.61           C  
-ATOM   1424  OD1 ASP A 203      62.092  15.314  -3.435  1.00 14.50           O  
-ATOM   1425  OD2 ASP A 203      62.897  14.550  -5.329  1.00 14.22           O  
-ATOM   1426  N   GLN A 204      66.785  13.917  -1.571  1.00 13.57           N  
-ATOM   1427  CA  GLN A 204      67.520  13.337  -0.446  1.00 12.68           C  
-ATOM   1428  C   GLN A 204      68.057  14.465   0.428  1.00 12.48           C  
-ATOM   1429  O   GLN A 204      68.068  14.360   1.651  1.00 12.60           O  
-ATOM   1430  CB  GLN A 204      68.647  12.433  -0.949  1.00 13.05           C  
-ATOM   1431  CG  GLN A 204      68.133  11.183  -1.639  1.00 12.51           C  
-ATOM   1432  CD  GLN A 204      69.231  10.341  -2.235  1.00 13.97           C  
-ATOM   1433  OE1 GLN A 204      70.235  10.859  -2.726  1.00 16.08           O  
-ATOM   1434  NE2 GLN A 204      69.045   9.029  -2.210  1.00 13.86           N  
-ATOM   1435  N   TRP A 205      68.481  15.553  -0.208  1.00 12.85           N  
-ATOM   1436  CA  TRP A 205      68.958  16.727   0.515  1.00 13.95           C  
-ATOM   1437  C   TRP A 205      67.842  17.227   1.428  1.00 13.66           C  
-ATOM   1438  O   TRP A 205      68.073  17.518   2.602  1.00 13.96           O  
-ATOM   1439  CB  TRP A 205      69.333  17.836  -0.460  1.00 14.42           C  
-ATOM   1440  CG  TRP A 205      70.731  17.779  -0.920  1.00 15.86           C  
-ATOM   1441  CD1 TRP A 205      71.165  17.503  -2.177  1.00 15.90           C  
-ATOM   1442  CD2 TRP A 205      71.898  18.039  -0.132  1.00 17.88           C  
-ATOM   1443  NE1 TRP A 205      72.530  17.580  -2.229  1.00 17.67           N  
-ATOM   1444  CE2 TRP A 205      73.010  17.903  -0.991  1.00 18.33           C  
-ATOM   1445  CE3 TRP A 205      72.113  18.373   1.212  1.00 19.40           C  
-ATOM   1446  CZ2 TRP A 205      74.328  18.091  -0.547  1.00 19.32           C  
-ATOM   1447  CZ3 TRP A 205      73.425  18.562   1.655  1.00 20.83           C  
-ATOM   1448  CH2 TRP A 205      74.515  18.419   0.773  1.00 20.66           C  
-ATOM   1449  N   ALA A 206      66.628  17.298   0.882  1.00 14.17           N  
-ATOM   1450  CA  ALA A 206      65.453  17.745   1.625  1.00 15.00           C  
-ATOM   1451  C   ALA A 206      65.227  16.899   2.881  1.00 15.10           C  
-ATOM   1452  O   ALA A 206      64.901  17.429   3.940  1.00 15.82           O  
-ATOM   1453  CB  ALA A 206      64.223  17.717   0.727  1.00 15.39           C  
-ATOM   1454  N   GLU A 207      65.408  15.588   2.767  1.00 15.85           N  
-ATOM   1455  CA  GLU A 207      65.251  14.710   3.922  1.00 18.02           C  
-ATOM   1456  C   GLU A 207      66.365  14.953   4.931  1.00 18.53           C  
-ATOM   1457  O   GLU A 207      66.123  14.927   6.138  1.00 20.28           O  
-ATOM   1458  CB  GLU A 207      65.243  13.248   3.512  1.00 19.24           C  
-ATOM   1459  CG  GLU A 207      63.961  12.796   2.866  1.00 23.32           C  
-ATOM   1460  CD  GLU A 207      63.935  11.303   2.618  1.00 25.90           C  
-ATOM   1461  OE1 GLU A 207      63.946  10.523   3.600  1.00 26.09           O  
-ATOM   1462  OE2 GLU A 207      63.901  10.910   1.424  1.00 27.34           O  
-ATOM   1463  N   ILE A 208      67.583  15.184   4.445  1.00 18.90           N  
-ATOM   1464  CA  ILE A 208      68.721  15.457   5.323  1.00 18.40           C  
-ATOM   1465  C   ILE A 208      68.428  16.727   6.121  1.00 18.23           C  
-ATOM   1466  O   ILE A 208      68.710  16.792   7.321  1.00 18.09           O  
-ATOM   1467  CB  ILE A 208      70.051  15.611   4.516  1.00 18.48           C  
-ATOM   1468  CG1 ILE A 208      70.456  14.264   3.921  1.00 18.26           C  
-ATOM   1469  CG2 ILE A 208      71.169  16.150   5.392  1.00 16.92           C  
-ATOM   1470  CD1 ILE A 208      70.553  13.152   4.945  1.00 17.99           C  
-ATOM   1471  N   ALA A 209      67.817  17.711   5.464  1.00 18.14           N  
-ATOM   1472  CA  ALA A 209      67.465  18.964   6.129  1.00 18.92           C  
-ATOM   1473  C   ALA A 209      66.527  18.682   7.293  1.00 19.60           C  
-ATOM   1474  O   ALA A 209      66.721  19.219   8.383  1.00 21.27           O  
-ATOM   1475  CB  ALA A 209      66.820  19.937   5.150  1.00 18.88           C  
-ATOM   1476  N   SER A 210      65.537  17.815   7.076  1.00 19.81           N  
-ATOM   1477  CA  SER A 210      64.583  17.452   8.125  1.00 20.61           C  
-ATOM   1478  C   SER A 210      65.272  16.840   9.339  1.00 20.10           C  
-ATOM   1479  O   SER A 210      64.959  17.191  10.479  1.00 20.26           O  
-ATOM   1480  CB  SER A 210      63.551  16.468   7.588  1.00 21.56           C  
-ATOM   1481  OG  SER A 210      62.852  17.028   6.493  1.00 26.98           O  
-ATOM   1482  N   ILE A 211      66.197  15.915   9.093  1.00 20.62           N  
-ATOM   1483  CA  ILE A 211      66.943  15.258  10.169  1.00 20.53           C  
-ATOM   1484  C   ILE A 211      67.795  16.284  10.924  1.00 20.98           C  
-ATOM   1485  O   ILE A 211      67.909  16.227  12.147  1.00 20.32           O  
-ATOM   1486  CB  ILE A 211      67.845  14.108   9.620  1.00 20.49           C  
-ATOM   1487  CG1 ILE A 211      66.973  13.010   9.004  1.00 19.78           C  
-ATOM   1488  CG2 ILE A 211      68.705  13.515  10.734  1.00 19.49           C  
-ATOM   1489  CD1 ILE A 211      67.754  11.939   8.269  1.00 20.52           C  
-ATOM   1490  N   LEU A 212      68.354  17.247  10.199  1.00 22.23           N  
-ATOM   1491  CA  LEU A 212      69.173  18.276  10.823  1.00 24.48           C  
-ATOM   1492  C   LEU A 212      68.321  19.203  11.696  1.00 25.97           C  
-ATOM   1493  O   LEU A 212      68.736  19.582  12.793  1.00 26.74           O  
-ATOM   1494  CB  LEU A 212      69.957  19.065   9.764  1.00 25.12           C  
-ATOM   1495  CG  LEU A 212      71.080  18.309   9.033  1.00 25.93           C  
-ATOM   1496  CD1 LEU A 212      71.704  19.193   7.956  1.00 25.76           C  
-ATOM   1497  CD2 LEU A 212      72.148  17.854  10.024  1.00 25.97           C  
-ATOM   1498  N   GLU A 213      67.127  19.554  11.227  1.00 26.96           N  
-ATOM   1499  CA  GLU A 213      66.240  20.408  12.015  1.00 28.59           C  
-ATOM   1500  C   GLU A 213      65.901  19.657  13.303  1.00 28.43           C  
-ATOM   1501  O   GLU A 213      66.007  20.199  14.406  1.00 29.04           O  
-ATOM   1502  CB  GLU A 213      64.934  20.692  11.269  1.00 30.71           C  
-ATOM   1503  CG  GLU A 213      65.089  21.350   9.917  1.00 35.26           C  
-ATOM   1504  CD  GLU A 213      63.756  21.551   9.218  1.00 38.25           C  
-ATOM   1505  OE1 GLU A 213      62.873  22.201   9.818  1.00 40.63           O  
-ATOM   1506  OE2 GLU A 213      63.589  21.062   8.075  1.00 39.30           O  
-ATOM   1507  N   LYS A 214      65.498  18.401  13.138  1.00 27.11           N  
-ATOM   1508  CA  LYS A 214      65.127  17.538  14.246  1.00 26.47           C  
-ATOM   1509  C   LYS A 214      66.220  17.406  15.299  1.00 25.28           C  
-ATOM   1510  O   LYS A 214      65.966  17.601  16.482  1.00 25.17           O  
-ATOM   1511  CB  LYS A 214      64.767  16.152  13.714  1.00 28.31           C  
-ATOM   1512  CG  LYS A 214      64.463  15.135  14.793  1.00 31.94           C  
-ATOM   1513  CD  LYS A 214      64.636  13.710  14.272  1.00 35.89           C  
-ATOM   1514  CE  LYS A 214      66.031  13.499  13.672  1.00 37.19           C  
-ATOM   1515  NZ  LYS A 214      66.383  12.063  13.477  1.00 38.21           N  
-ATOM   1516  N   THR A 215      67.428  17.058  14.866  1.00 24.31           N  
-ATOM   1517  CA  THR A 215      68.555  16.872  15.780  1.00 23.01           C  
-ATOM   1518  C   THR A 215      69.176  18.162  16.321  1.00 22.13           C  
-ATOM   1519  O   THR A 215      69.696  18.184  17.438  1.00 21.42           O  
-ATOM   1520  CB  THR A 215      69.674  16.031  15.124  1.00 23.17           C  
-ATOM   1521  OG1 THR A 215      70.185  16.719  13.976  1.00 22.68           O  
-ATOM   1522  CG2 THR A 215      69.144  14.669  14.699  1.00 22.45           C  
-ATOM   1523  N   GLY A 216      69.126  19.229  15.533  1.00 21.14           N  
-ATOM   1524  CA  GLY A 216      69.714  20.482  15.964  1.00 21.48           C  
-ATOM   1525  C   GLY A 216      71.220  20.498  15.728  1.00 21.87           C  
-ATOM   1526  O   GLY A 216      71.959  21.256  16.368  1.00 22.58           O  
-ATOM   1527  N   ALA A 217      71.678  19.633  14.828  1.00 21.60           N  
-ATOM   1528  CA  ALA A 217      73.087  19.539  14.495  1.00 20.38           C  
-ATOM   1529  C   ALA A 217      73.424  20.647  13.510  1.00 20.73           C  
-ATOM   1530  O   ALA A 217      72.605  21.018  12.670  1.00 20.28           O  
-ATOM   1531  CB  ALA A 217      73.401  18.183  13.895  1.00 19.37           C  
-ATOM   1532  N   LEU A 218      74.637  21.176  13.631  1.00 20.99           N  
-ATOM   1533  CA  LEU A 218      75.118  22.252  12.775  1.00 20.06           C  
-ATOM   1534  C   LEU A 218      75.769  21.679  11.518  1.00 19.26           C  
-ATOM   1535  O   LEU A 218      76.685  20.865  11.606  1.00 19.71           O  
-ATOM   1536  CB  LEU A 218      76.132  23.097  13.547  1.00 20.08           C  
-ATOM   1537  CG  LEU A 218      76.759  24.303  12.843  1.00 22.04           C  
-ATOM   1538  CD1 LEU A 218      75.690  25.321  12.503  1.00 21.72           C  
-ATOM   1539  CD2 LEU A 218      77.815  24.931  13.745  1.00 21.75           C  
-ATOM   1540  N   PRO A 219      75.255  22.039  10.332  1.00 18.69           N  
-ATOM   1541  CA  PRO A 219      75.850  21.521   9.096  1.00 18.02           C  
-ATOM   1542  C   PRO A 219      77.030  22.355   8.572  1.00 17.30           C  
-ATOM   1543  O   PRO A 219      77.009  23.587   8.621  1.00 17.18           O  
-ATOM   1544  CB  PRO A 219      74.670  21.541   8.125  1.00 17.84           C  
-ATOM   1545  CG  PRO A 219      73.905  22.747   8.561  1.00 17.69           C  
-ATOM   1546  CD  PRO A 219      73.934  22.648  10.070  1.00 18.65           C  
-ATOM   1547  N   LEU A 220      78.076  21.666   8.127  1.00 16.65           N  
-ATOM   1548  CA  LEU A 220      79.256  22.304   7.554  1.00 15.05           C  
-ATOM   1549  C   LEU A 220      79.368  21.765   6.135  1.00 15.12           C  
-ATOM   1550  O   LEU A 220      79.643  20.582   5.937  1.00 15.75           O  
-ATOM   1551  CB  LEU A 220      80.525  21.955   8.344  1.00 14.32           C  
-ATOM   1552  CG  LEU A 220      81.870  22.355   7.709  1.00 13.74           C  
-ATOM   1553  CD1 LEU A 220      81.905  23.840   7.419  1.00 13.38           C  
-ATOM   1554  CD2 LEU A 220      83.035  21.972   8.609  1.00 13.43           C  
-ATOM   1555  N   ILE A 221      79.092  22.607   5.148  1.00 15.18           N  
-ATOM   1556  CA  ILE A 221      79.178  22.174   3.764  1.00 16.05           C  
-ATOM   1557  C   ILE A 221      80.528  22.492   3.129  1.00 15.87           C  
-ATOM   1558  O   ILE A 221      80.980  23.643   3.117  1.00 15.63           O  
-ATOM   1559  CB  ILE A 221      78.043  22.767   2.878  1.00 16.03           C  
-ATOM   1560  CG1 ILE A 221      76.677  22.260   3.338  1.00 17.54           C  
-ATOM   1561  CG2 ILE A 221      78.241  22.362   1.428  1.00 15.45           C  
-ATOM   1562  CD1 ILE A 221      75.936  23.223   4.207  1.00 20.23           C  
-ATOM   1563  N   ASP A 222      81.172  21.446   2.628  1.00 15.81           N  
-ATOM   1564  CA  ASP A 222      82.449  21.560   1.951  1.00 15.44           C  
-ATOM   1565  C   ASP A 222      82.113  21.720   0.470  1.00 15.34           C  
-ATOM   1566  O   ASP A 222      81.832  20.734  -0.216  1.00 15.79           O  
-ATOM   1567  CB  ASP A 222      83.275  20.292   2.173  1.00 15.35           C  
-ATOM   1568  CG  ASP A 222      84.680  20.395   1.602  1.00 16.61           C  
-ATOM   1569  OD1 ASP A 222      84.915  21.174   0.658  1.00 16.90           O  
-ATOM   1570  OD2 ASP A 222      85.565  19.682   2.101  1.00 17.71           O  
-ATOM   1571  N   LEU A 223      82.129  22.961  -0.009  1.00 15.78           N  
-ATOM   1572  CA  LEU A 223      81.818  23.267  -1.403  1.00 16.10           C  
-ATOM   1573  C   LEU A 223      83.091  23.586  -2.202  1.00 16.74           C  
-ATOM   1574  O   LEU A 223      83.451  24.751  -2.415  1.00 16.75           O  
-ATOM   1575  CB  LEU A 223      80.823  24.432  -1.471  1.00 16.30           C  
-ATOM   1576  CG  LEU A 223      80.137  24.694  -2.817  1.00 17.32           C  
-ATOM   1577  CD1 LEU A 223      79.297  23.486  -3.230  1.00 16.74           C  
-ATOM   1578  CD2 LEU A 223      79.271  25.938  -2.725  1.00 15.91           C  
-ATOM   1579  N   ALA A 224      83.761  22.533  -2.658  1.00 16.63           N  
-ATOM   1580  CA  ALA A 224      84.998  22.661  -3.410  1.00 16.32           C  
-ATOM   1581  C   ALA A 224      84.887  22.482  -4.922  1.00 15.80           C  
-ATOM   1582  O   ALA A 224      85.793  22.888  -5.656  1.00 16.00           O  
-ATOM   1583  CB  ALA A 224      86.037  21.685  -2.848  1.00 16.67           C  
-ATOM   1584  N   TYR A 225      83.785  21.904  -5.397  1.00 15.07           N  
-ATOM   1585  CA  TYR A 225      83.631  21.659  -6.831  1.00 14.14           C  
-ATOM   1586  C   TYR A 225      82.437  22.284  -7.535  1.00 14.06           C  
-ATOM   1587  O   TYR A 225      81.931  21.716  -8.505  1.00 15.10           O  
-ATOM   1588  CB  TYR A 225      83.645  20.156  -7.108  1.00 13.04           C  
-ATOM   1589  CG  TYR A 225      84.968  19.498  -6.803  1.00 14.02           C  
-ATOM   1590  CD1 TYR A 225      86.031  19.567  -7.709  1.00 13.48           C  
-ATOM   1591  CD2 TYR A 225      85.167  18.808  -5.605  1.00 13.40           C  
-ATOM   1592  CE1 TYR A 225      87.256  18.966  -7.426  1.00 13.43           C  
-ATOM   1593  CE2 TYR A 225      86.390  18.203  -5.316  1.00 12.84           C  
-ATOM   1594  CZ  TYR A 225      87.423  18.288  -6.228  1.00 12.99           C  
-ATOM   1595  OH  TYR A 225      88.613  17.677  -5.943  1.00 14.75           O  
-ATOM   1596  N   GLN A 226      82.018  23.471  -7.111  1.00 13.95           N  
-ATOM   1597  CA  GLN A 226      80.877  24.119  -7.749  1.00 14.45           C  
-ATOM   1598  C   GLN A 226      81.162  24.410  -9.216  1.00 14.34           C  
-ATOM   1599  O   GLN A 226      81.972  25.271  -9.533  1.00 15.82           O  
-ATOM   1600  CB  GLN A 226      80.500  25.421  -7.033  1.00 14.31           C  
-ATOM   1601  CG  GLN A 226      79.224  26.057  -7.579  1.00 14.54           C  
-ATOM   1602  CD  GLN A 226      78.851  27.349  -6.884  1.00 15.21           C  
-ATOM   1603  OE1 GLN A 226      79.556  27.810  -5.993  1.00 16.02           O  
-ATOM   1604  NE2 GLN A 226      77.734  27.940  -7.289  1.00 15.38           N  
-ATOM   1605  N   GLY A 227      80.505  23.675 -10.103  1.00 15.45           N  
-ATOM   1606  CA  GLY A 227      80.691  23.876 -11.529  1.00 15.62           C  
-ATOM   1607  C   GLY A 227      81.159  22.647 -12.288  1.00 16.72           C  
-ATOM   1608  O   GLY A 227      81.091  22.622 -13.519  1.00 17.04           O  
-ATOM   1609  N   PHE A 228      81.628  21.631 -11.565  1.00 16.89           N  
-ATOM   1610  CA  PHE A 228      82.112  20.393 -12.183  1.00 17.79           C  
-ATOM   1611  C   PHE A 228      81.064  19.284 -12.220  1.00 17.94           C  
-ATOM   1612  O   PHE A 228      81.282  18.244 -12.838  1.00 18.85           O  
-ATOM   1613  CB  PHE A 228      83.353  19.873 -11.450  1.00 18.83           C  
-ATOM   1614  CG  PHE A 228      84.584  20.698 -11.667  1.00 19.11           C  
-ATOM   1615  CD1 PHE A 228      84.801  21.852 -10.933  1.00 20.44           C  
-ATOM   1616  CD2 PHE A 228      85.540  20.307 -12.595  1.00 21.39           C  
-ATOM   1617  CE1 PHE A 228      85.958  22.608 -11.118  1.00 22.07           C  
-ATOM   1618  CE2 PHE A 228      86.706  21.054 -12.792  1.00 21.79           C  
-ATOM   1619  CZ  PHE A 228      86.913  22.207 -12.051  1.00 21.44           C  
-ATOM   1620  N   GLY A 229      79.958  19.480 -11.511  1.00 18.28           N  
-ATOM   1621  CA  GLY A 229      78.907  18.480 -11.489  1.00 19.68           C  
-ATOM   1622  C   GLY A 229      77.919  18.630 -12.629  1.00 20.45           C  
-ATOM   1623  O   GLY A 229      78.130  18.124 -13.730  1.00 20.53           O  
-ATOM   1624  N   ASP A 230      76.821  19.321 -12.356  1.00 21.78           N  
-ATOM   1625  CA  ASP A 230      75.790  19.548 -13.353  1.00 23.36           C  
-ATOM   1626  C   ASP A 230      75.751  20.994 -13.829  1.00 23.66           C  
-ATOM   1627  O   ASP A 230      75.085  21.311 -14.810  1.00 25.39           O  
-ATOM   1628  CB  ASP A 230      74.430  19.131 -12.800  1.00 23.86           C  
-ATOM   1629  CG  ASP A 230      74.338  17.641 -12.563  1.00 24.33           C  
-ATOM   1630  OD1 ASP A 230      74.380  16.886 -13.556  1.00 24.36           O  
-ATOM   1631  OD2 ASP A 230      74.245  17.228 -11.387  1.00 24.56           O  
-ATOM   1632  N   GLY A 231      76.473  21.866 -13.136  1.00 23.55           N  
-ATOM   1633  CA  GLY A 231      76.507  23.269 -13.505  1.00 22.74           C  
-ATOM   1634  C   GLY A 231      76.664  24.104 -12.254  1.00 22.53           C  
-ATOM   1635  O   GLY A 231      76.479  23.586 -11.151  1.00 22.72           O  
-ATOM   1636  N   LEU A 233      76.988  25.385 -12.411  1.00 22.00           N  
-ATOM   1637  CA  LEU A 233      77.170  26.278 -11.266  1.00 22.12           C  
-ATOM   1638  C   LEU A 233      75.961  26.364 -10.334  1.00 21.44           C  
-ATOM   1639  O   LEU A 233      76.094  26.177  -9.125  1.00 20.86           O  
-ATOM   1640  CB  LEU A 233      77.586  27.685 -11.726  1.00 22.36           C  
-ATOM   1641  CG  LEU A 233      79.060  27.865 -12.100  1.00 22.17           C  
-ATOM   1642  CD1 LEU A 233      79.293  29.219 -12.747  1.00 22.16           C  
-ATOM   1643  CD2 LEU A 233      79.917  27.717 -10.856  1.00 22.48           C  
-ATOM   1644  N   GLU A 234      74.791  26.649 -10.895  1.00 21.55           N  
-ATOM   1645  CA  GLU A 234      73.571  26.756 -10.100  1.00 21.75           C  
-ATOM   1646  C   GLU A 234      73.129  25.387  -9.595  1.00 20.78           C  
-ATOM   1647  O   GLU A 234      72.827  25.214  -8.418  1.00 20.15           O  
-ATOM   1648  CB  GLU A 234      72.453  27.394 -10.926  1.00 23.53           C  
-ATOM   1649  CG  GLU A 234      72.709  28.839 -11.319  1.00 27.13           C  
-ATOM   1650  CD  GLU A 234      72.684  29.788 -10.128  1.00 30.63           C  
-ATOM   1651  OE1 GLU A 234      71.586  30.276  -9.778  1.00 32.55           O  
-ATOM   1652  OE2 GLU A 234      73.759  30.058  -9.545  1.00 32.25           O  
-ATOM   1653  N   GLU A 235      73.163  24.404 -10.485  1.00 20.50           N  
-ATOM   1654  CA  GLU A 235      72.759  23.044 -10.154  1.00 21.40           C  
-ATOM   1655  C   GLU A 235      73.557  22.471  -8.983  1.00 21.59           C  
-ATOM   1656  O   GLU A 235      72.992  21.823  -8.092  1.00 22.07           O  
-ATOM   1657  CB  GLU A 235      72.908  22.128 -11.370  1.00 22.27           C  
-ATOM   1658  CG  GLU A 235      71.917  22.386 -12.495  1.00 24.69           C  
-ATOM   1659  CD  GLU A 235      72.310  23.531 -13.425  1.00 26.88           C  
-ATOM   1660  OE1 GLU A 235      73.312  24.234 -13.166  1.00 26.53           O  
-ATOM   1661  OE2 GLU A 235      71.609  23.725 -14.443  1.00 28.93           O  
-ATOM   1662  N   ASP A 236      74.866  22.730  -8.980  1.00 20.55           N  
-ATOM   1663  CA  ASP A 236      75.753  22.233  -7.936  1.00 18.61           C  
-ATOM   1664  C   ASP A 236      75.550  22.885  -6.579  1.00 17.75           C  
-ATOM   1665  O   ASP A 236      75.908  22.308  -5.552  1.00 17.28           O  
-ATOM   1666  CB  ASP A 236      77.215  22.351  -8.376  1.00 18.93           C  
-ATOM   1667  CG  ASP A 236      77.535  21.447  -9.554  1.00 20.14           C  
-ATOM   1668  OD1 ASP A 236      76.711  20.560  -9.848  1.00 22.22           O  
-ATOM   1669  OD2 ASP A 236      78.589  21.619 -10.198  1.00 18.59           O  
-ATOM   1670  N   ALA A 237      74.973  24.082  -6.574  1.00 16.76           N  
-ATOM   1671  CA  ALA A 237      74.727  24.793  -5.326  1.00 16.18           C  
-ATOM   1672  C   ALA A 237      73.308  24.561  -4.800  1.00 15.41           C  
-ATOM   1673  O   ALA A 237      72.974  25.006  -3.700  1.00 15.78           O  
-ATOM   1674  CB  ALA A 237      74.995  26.282  -5.505  1.00 15.34           C  
-ATOM   1675  N   ALA A 238      72.496  23.826  -5.555  1.00 14.59           N  
-ATOM   1676  CA  ALA A 238      71.110  23.549  -5.162  1.00 15.05           C  
-ATOM   1677  C   ALA A 238      70.977  22.952  -3.765  1.00 15.34           C  
-ATOM   1678  O   ALA A 238      70.216  23.455  -2.937  1.00 15.93           O  
-ATOM   1679  CB  ALA A 238      70.433  22.646  -6.192  1.00 14.57           C  
-ATOM   1680  N   GLY A 239      71.745  21.906  -3.486  1.00 15.39           N  
-ATOM   1681  CA  GLY A 239      71.676  21.271  -2.183  1.00 15.63           C  
-ATOM   1682  C   GLY A 239      72.047  22.231  -1.075  1.00 15.90           C  
-ATOM   1683  O   GLY A 239      71.406  22.268  -0.024  1.00 16.13           O  
-ATOM   1684  N   THR A 240      73.076  23.027  -1.324  1.00 16.06           N  
-ATOM   1685  CA  THR A 240      73.546  23.992  -0.352  1.00 16.52           C  
-ATOM   1686  C   THR A 240      72.480  25.053  -0.084  1.00 17.41           C  
-ATOM   1687  O   THR A 240      72.220  25.404   1.071  1.00 17.84           O  
-ATOM   1688  CB  THR A 240      74.848  24.657  -0.844  1.00 17.08           C  
-ATOM   1689  OG1 THR A 240      75.843  23.646  -1.060  1.00 16.83           O  
-ATOM   1690  CG2 THR A 240      75.361  25.656   0.176  1.00 14.95           C  
-ATOM   1691  N   ARG A 241      71.831  25.526  -1.146  1.00 17.86           N  
-ATOM   1692  CA  ARG A 241      70.797  26.551  -1.019  1.00 17.50           C  
-ATOM   1693  C   ARG A 241      69.565  26.066  -0.269  1.00 17.43           C  
-ATOM   1694  O   ARG A 241      68.925  26.851   0.431  1.00 17.47           O  
-ATOM   1695  CB  ARG A 241      70.433  27.113  -2.389  1.00 17.27           C  
-ATOM   1696  CG  ARG A 241      71.582  27.890  -3.000  1.00 18.17           C  
-ATOM   1697  CD  ARG A 241      71.356  28.240  -4.454  1.00 18.62           C  
-ATOM   1698  NE  ARG A 241      72.546  28.882  -5.008  1.00 20.45           N  
-ATOM   1699  CZ  ARG A 241      72.684  29.282  -6.269  1.00 21.01           C  
-ATOM   1700  NH1 ARG A 241      71.698  29.114  -7.141  1.00 20.44           N  
-ATOM   1701  NH2 ARG A 241      73.822  29.840  -6.661  1.00 20.09           N  
-ATOM   1702  N   LEU A 242      69.250  24.777  -0.397  1.00 17.46           N  
-ATOM   1703  CA  LEU A 242      68.110  24.188   0.304  1.00 17.27           C  
-ATOM   1704  C   LEU A 242      68.429  24.185   1.795  1.00 17.83           C  
-ATOM   1705  O   LEU A 242      67.622  24.615   2.615  1.00 18.19           O  
-ATOM   1706  CB  LEU A 242      67.840  22.762  -0.197  1.00 17.07           C  
-ATOM   1707  CG  LEU A 242      66.640  21.981   0.363  1.00 16.55           C  
-ATOM   1708  CD1 LEU A 242      66.181  20.948  -0.644  1.00 15.96           C  
-ATOM   1709  CD2 LEU A 242      66.981  21.314   1.687  1.00 15.82           C  
-ATOM   1710  N   ILE A 243      69.617  23.699   2.140  1.00 18.58           N  
-ATOM   1711  CA  ILE A 243      70.059  23.662   3.531  1.00 19.12           C  
-ATOM   1712  C   ILE A 243      70.047  25.077   4.112  1.00 20.51           C  
-ATOM   1713  O   ILE A 243      69.573  25.304   5.227  1.00 21.57           O  
-ATOM   1714  CB  ILE A 243      71.504  23.101   3.644  1.00 18.83           C  
-ATOM   1715  CG1 ILE A 243      71.547  21.636   3.198  1.00 19.41           C  
-ATOM   1716  CG2 ILE A 243      72.035  23.257   5.069  1.00 17.60           C  
-ATOM   1717  CD1 ILE A 243      70.695  20.704   4.043  1.00 19.73           C  
-ATOM   1718  N   ALA A 244      70.557  26.027   3.336  1.00 21.07           N  
-ATOM   1719  CA  ALA A 244      70.642  27.418   3.760  1.00 21.77           C  
-ATOM   1720  C   ALA A 244      69.297  28.051   4.086  1.00 22.76           C  
-ATOM   1721  O   ALA A 244      69.191  28.828   5.032  1.00 23.51           O  
-ATOM   1722  CB  ALA A 244      71.365  28.233   2.707  1.00 21.11           C  
-ATOM   1723  N   SER A 245      68.268  27.719   3.314  1.00 23.61           N  
-ATOM   1724  CA  SER A 245      66.950  28.295   3.542  1.00 25.12           C  
-ATOM   1725  C   SER A 245      66.113  27.644   4.639  1.00 25.61           C  
-ATOM   1726  O   SER A 245      65.276  28.312   5.252  1.00 26.07           O  
-ATOM   1727  CB  SER A 245      66.158  28.360   2.236  1.00 26.11           C  
-ATOM   1728  OG  SER A 245      66.203  27.129   1.541  1.00 27.86           O  
-ATOM   1729  N   ARG A 246      66.346  26.363   4.909  1.00 25.46           N  
-ATOM   1730  CA  ARG A 246      65.578  25.660   5.937  1.00 24.61           C  
-ATOM   1731  C   ARG A 246      66.267  25.559   7.300  1.00 24.96           C  
-ATOM   1732  O   ARG A 246      65.602  25.352   8.320  1.00 25.60           O  
-ATOM   1733  CB  ARG A 246      65.183  24.268   5.439  1.00 24.63           C  
-ATOM   1734  CG  ARG A 246      64.518  24.284   4.069  1.00 24.55           C  
-ATOM   1735  CD  ARG A 246      63.932  22.933   3.708  1.00 25.68           C  
-ATOM   1736  NE  ARG A 246      63.476  22.889   2.318  1.00 26.05           N  
-ATOM   1737  CZ  ARG A 246      62.873  21.843   1.755  1.00 26.16           C  
-ATOM   1738  NH1 ARG A 246      62.636  20.744   2.458  1.00 25.85           N  
-ATOM   1739  NH2 ARG A 246      62.502  21.898   0.483  1.00 26.80           N  
-ATOM   1740  N   ILE A 247      67.589  25.702   7.320  1.00 24.20           N  
-ATOM   1741  CA  ILE A 247      68.360  25.619   8.559  1.00 23.66           C  
-ATOM   1742  C   ILE A 247      68.875  27.010   8.956  1.00 24.20           C  
-ATOM   1743  O   ILE A 247      69.493  27.707   8.149  1.00 24.66           O  
-ATOM   1744  CB  ILE A 247      69.550  24.647   8.390  1.00 23.62           C  
-ATOM   1745  CG1 ILE A 247      69.057  23.300   7.845  1.00 23.94           C  
-ATOM   1746  CG2 ILE A 247      70.273  24.443   9.718  1.00 23.27           C  
-ATOM   1747  CD1 ILE A 247      68.169  22.528   8.794  1.00 23.19           C  
-ATOM   1748  N   PRO A 248      68.645  27.420  10.215  1.00 24.57           N  
-ATOM   1749  CA  PRO A 248      69.082  28.733  10.710  1.00 24.96           C  
-ATOM   1750  C   PRO A 248      70.596  28.990  10.678  1.00 24.93           C  
-ATOM   1751  O   PRO A 248      71.037  29.992  10.114  1.00 25.09           O  
-ATOM   1752  CB  PRO A 248      68.514  28.770  12.133  1.00 25.02           C  
-ATOM   1753  CG  PRO A 248      68.483  27.325  12.529  1.00 25.39           C  
-ATOM   1754  CD  PRO A 248      67.970  26.655  11.279  1.00 24.28           C  
-ATOM   1755  N   GLU A 249      71.380  28.118  11.309  1.00 24.01           N  
-ATOM   1756  CA  GLU A 249      72.837  28.268  11.331  1.00 23.78           C  
-ATOM   1757  C   GLU A 249      73.468  27.270  10.376  1.00 21.69           C  
-ATOM   1758  O   GLU A 249      73.223  26.067  10.485  1.00 21.40           O  
-ATOM   1759  CB  GLU A 249      73.406  28.022  12.731  1.00 25.48           C  
-ATOM   1760  CG  GLU A 249      73.205  29.145  13.733  1.00 29.32           C  
-ATOM   1761  CD  GLU A 249      73.863  28.851  15.083  1.00 31.99           C  
-ATOM   1762  OE1 GLU A 249      74.427  27.746  15.259  1.00 34.06           O  
-ATOM   1763  OE2 GLU A 249      73.820  29.725  15.972  1.00 32.42           O  
-ATOM   1764  N   VAL A 250      74.301  27.763   9.468  1.00 20.45           N  
-ATOM   1765  CA  VAL A 250      74.970  26.912   8.486  1.00 19.25           C  
-ATOM   1766  C   VAL A 250      76.385  27.423   8.230  1.00 18.75           C  
-ATOM   1767  O   VAL A 250      76.607  28.631   8.134  1.00 17.77           O  
-ATOM   1768  CB  VAL A 250      74.188  26.884   7.132  1.00 18.55           C  
-ATOM   1769  CG1 VAL A 250      74.938  26.081   6.094  1.00 17.83           C  
-ATOM   1770  CG2 VAL A 250      72.790  26.298   7.324  1.00 18.79           C  
-ATOM   1771  N   LEU A 251      77.341  26.503   8.141  1.00 18.72           N  
-ATOM   1772  CA  LEU A 251      78.732  26.864   7.869  1.00 18.54           C  
-ATOM   1773  C   LEU A 251      79.117  26.322   6.495  1.00 17.44           C  
-ATOM   1774  O   LEU A 251      78.858  25.159   6.197  1.00 16.75           O  
-ATOM   1775  CB  LEU A 251      79.646  26.293   8.954  1.00 19.42           C  
-ATOM   1776  CG  LEU A 251      80.141  27.224  10.071  1.00 20.86           C  
-ATOM   1777  CD1 LEU A 251      79.104  28.269  10.451  1.00 21.65           C  
-ATOM   1778  CD2 LEU A 251      80.538  26.391  11.278  1.00 20.85           C  
-ATOM   1779  N   ILE A 252      79.675  27.177   5.640  1.00 16.90           N  
-ATOM   1780  CA  ILE A 252      80.080  26.769   4.293  1.00 16.32           C  
-ATOM   1781  C   ILE A 252      81.542  27.122   4.005  1.00 16.54           C  
-ATOM   1782  O   ILE A 252      81.929  28.289   4.074  1.00 17.36           O  
-ATOM   1783  CB  ILE A 252      79.202  27.446   3.214  1.00 16.46           C  
-ATOM   1784  CG1 ILE A 252      77.732  27.058   3.405  1.00 16.66           C  
-ATOM   1785  CG2 ILE A 252      79.682  27.053   1.809  1.00 15.63           C  
-ATOM   1786  CD1 ILE A 252      76.780  27.844   2.544  1.00 15.14           C  
-ATOM   1787  N   ALA A 253      82.345  26.114   3.680  1.00 15.43           N  
-ATOM   1788  CA  ALA A 253      83.759  26.316   3.363  1.00 13.89           C  
-ATOM   1789  C   ALA A 253      83.933  26.082   1.868  1.00 13.35           C  
-ATOM   1790  O   ALA A 253      83.934  24.940   1.406  1.00 12.65           O  
-ATOM   1791  CB  ALA A 253      84.619  25.339   4.149  1.00 13.89           C  
-ATOM   1792  N   ALA A 254      84.054  27.162   1.111  1.00 12.81           N  
-ATOM   1793  CA  ALA A 254      84.197  27.064  -0.335  1.00 13.48           C  
-ATOM   1794  C   ALA A 254      85.633  27.174  -0.819  1.00 14.00           C  
-ATOM   1795  O   ALA A 254      86.480  27.799  -0.175  1.00 12.79           O  
-ATOM   1796  CB  ALA A 254      83.345  28.125  -1.015  1.00 13.44           C  
-ATOM   1797  N   SER A 255      85.888  26.589  -1.982  1.00 14.61           N  
-ATOM   1798  CA  SER A 255      87.205  26.629  -2.582  1.00 15.86           C  
-ATOM   1799  C   SER A 255      87.130  27.211  -3.997  1.00 15.92           C  
-ATOM   1800  O   SER A 255      86.130  27.034  -4.696  1.00 16.11           O  
-ATOM   1801  CB  SER A 255      87.805  25.219  -2.632  1.00 16.76           C  
-ATOM   1802  OG  SER A 255      89.121  25.237  -3.173  1.00 15.89           O  
-ATOM   1803  N   CYS A 256      88.166  27.949  -4.386  1.00 15.41           N  
-ATOM   1804  CA  CYS A 256      88.246  28.521  -5.723  1.00 14.17           C  
-ATOM   1805  C   CYS A 256      89.373  27.834  -6.491  1.00 12.87           C  
-ATOM   1806  O   CYS A 256      89.568  28.088  -7.681  1.00 11.30           O  
-ATOM   1807  CB  CYS A 256      88.532  30.017  -5.658  1.00 15.28           C  
-ATOM   1808  SG  CYS A 256      87.269  30.991  -4.840  1.00 16.13           S  
-ATOM   1809  N   SER A 257      90.105  26.961  -5.803  1.00 13.18           N  
-ATOM   1810  CA  SER A 257      91.233  26.240  -6.393  1.00 13.03           C  
-ATOM   1811  C   SER A 257      90.927  25.542  -7.708  1.00 13.90           C  
-ATOM   1812  O   SER A 257      91.589  25.807  -8.721  1.00 14.51           O  
-ATOM   1813  CB  SER A 257      91.793  25.208  -5.411  1.00 11.36           C  
-ATOM   1814  OG  SER A 257      92.265  25.825  -4.231  1.00 10.92           O  
-ATOM   1815  N   LYS A 258      89.925  24.663  -7.696  1.00 14.13           N  
-ATOM   1816  CA  LYS A 258      89.567  23.898  -8.885  1.00 14.81           C  
-ATOM   1817  C   LYS A 258      88.703  24.595  -9.925  1.00 15.43           C  
-ATOM   1818  O   LYS A 258      89.070  24.615 -11.097  1.00 14.83           O  
-ATOM   1819  CB  LYS A 258      88.927  22.564  -8.502  1.00 15.51           C  
-ATOM   1820  CG  LYS A 258      89.825  21.653  -7.676  1.00 16.44           C  
-ATOM   1821  CD  LYS A 258      89.396  21.659  -6.224  1.00 17.06           C  
-ATOM   1822  CE  LYS A 258      90.224  20.705  -5.378  1.00 17.31           C  
-ATOM   1823  NZ  LYS A 258      89.549  20.445  -4.110  1.00 17.40           N  
-ATOM   1824  N   ASN A 259      87.568  25.167  -9.509  1.00 16.26           N  
-ATOM   1825  CA  ASN A 259      86.668  25.828 -10.453  1.00 16.53           C  
-ATOM   1826  C   ASN A 259      87.204  27.111 -11.065  1.00 16.96           C  
-ATOM   1827  O   ASN A 259      86.642  27.613 -12.038  1.00 18.28           O  
-ATOM   1828  CB  ASN A 259      85.245  26.002  -9.896  1.00 16.84           C  
-ATOM   1829  CG  ASN A 259      85.162  26.991  -8.752  1.00 18.26           C  
-ATOM   1830  OD1 ASN A 259      86.175  27.394  -8.174  1.00 18.77           O  
-ATOM   1831  ND2 ASN A 259      83.942  27.366  -8.398  1.00 17.14           N  
-ATOM   1832  N   PHE A 260      88.279  27.647 -10.493  1.00 15.89           N  
-ATOM   1833  CA  PHE A 260      88.923  28.828 -11.054  1.00 15.47           C  
-ATOM   1834  C   PHE A 260      90.316  28.440 -11.557  1.00 14.91           C  
-ATOM   1835  O   PHE A 260      90.965  29.214 -12.252  1.00 15.66           O  
-ATOM   1836  CB  PHE A 260      89.008  29.974 -10.038  1.00 16.62           C  
-ATOM   1837  CG  PHE A 260      87.750  30.801  -9.943  1.00 16.65           C  
-ATOM   1838  CD1 PHE A 260      87.534  31.863 -10.814  1.00 17.28           C  
-ATOM   1839  CD2 PHE A 260      86.780  30.516  -8.987  1.00 16.63           C  
-ATOM   1840  CE1 PHE A 260      86.366  32.629 -10.732  1.00 17.50           C  
-ATOM   1841  CE2 PHE A 260      85.610  31.275  -8.900  1.00 16.59           C  
-ATOM   1842  CZ  PHE A 260      85.405  32.331  -9.774  1.00 16.51           C  
-ATOM   1843  N   GLY A 261      90.765  27.232 -11.216  1.00 13.64           N  
-ATOM   1844  CA  GLY A 261      92.071  26.760 -11.650  1.00 13.43           C  
-ATOM   1845  C   GLY A 261      93.256  27.521 -11.075  1.00 13.30           C  
-ATOM   1846  O   GLY A 261      94.286  27.675 -11.731  1.00 12.12           O  
-ATOM   1847  N   ILE A 262      93.110  27.993  -9.842  1.00 13.71           N  
-ATOM   1848  CA  ILE A 262      94.158  28.749  -9.164  1.00 13.96           C  
-ATOM   1849  C   ILE A 262      94.581  28.027  -7.881  1.00 13.92           C  
-ATOM   1850  O   ILE A 262      94.705  28.637  -6.820  1.00 14.50           O  
-ATOM   1851  CB  ILE A 262      93.685  30.195  -8.823  1.00 14.73           C  
-ATOM   1852  CG1 ILE A 262      92.396  30.164  -7.993  1.00 14.85           C  
-ATOM   1853  CG2 ILE A 262      93.468  31.004 -10.099  1.00 14.88           C  
-ATOM   1854  CD1 ILE A 262      91.935  31.531  -7.526  1.00 14.10           C  
-ATOM   1855  N   TYR A 263      94.856  26.732  -8.009  1.00 13.47           N  
-ATOM   1856  CA  TYR A 263      95.246  25.882  -6.888  1.00 13.30           C  
-ATOM   1857  C   TYR A 263      96.314  26.468  -5.970  1.00 13.64           C  
-ATOM   1858  O   TYR A 263      96.101  26.575  -4.766  1.00 14.27           O  
-ATOM   1859  CB  TYR A 263      95.739  24.522  -7.389  1.00 13.59           C  
-ATOM   1860  CG  TYR A 263      94.844  23.822  -8.391  1.00 14.17           C  
-ATOM   1861  CD1 TYR A 263      94.883  24.158  -9.742  1.00 14.44           C  
-ATOM   1862  CD2 TYR A 263      93.996  22.788  -7.995  1.00 13.85           C  
-ATOM   1863  CE1 TYR A 263      94.104  23.482 -10.676  1.00 14.60           C  
-ATOM   1864  CE2 TYR A 263      93.218  22.105  -8.917  1.00 13.77           C  
-ATOM   1865  CZ  TYR A 263      93.277  22.454 -10.254  1.00 15.18           C  
-ATOM   1866  OH  TYR A 263      92.530  21.757 -11.173  1.00 15.84           O  
-ATOM   1867  N   ARG A 264      97.455  26.843  -6.541  1.00 13.13           N  
-ATOM   1868  CA  ARG A 264      98.572  27.379  -5.767  1.00 13.94           C  
-ATOM   1869  C   ARG A 264      98.392  28.782  -5.184  1.00 14.43           C  
-ATOM   1870  O   ARG A 264      99.185  29.209  -4.341  1.00 14.63           O  
-ATOM   1871  CB  ARG A 264      99.857  27.336  -6.595  1.00 14.42           C  
-ATOM   1872  CG  ARG A 264      99.824  28.235  -7.822  1.00 15.18           C  
-ATOM   1873  CD  ARG A 264     101.113  28.159  -8.613  1.00 16.72           C  
-ATOM   1874  NE  ARG A 264     101.433  26.794  -9.017  1.00 18.49           N  
-ATOM   1875  CZ  ARG A 264     102.493  26.457  -9.745  1.00 18.92           C  
-ATOM   1876  NH1 ARG A 264     103.328  27.391 -10.179  1.00 19.48           N  
-ATOM   1877  NH2 ARG A 264     102.707  25.186 -10.056  1.00 18.00           N  
-ATOM   1878  N   GLU A 265      97.380  29.514  -5.634  1.00 14.41           N  
-ATOM   1879  CA  GLU A 265      97.159  30.860  -5.114  1.00 14.62           C  
-ATOM   1880  C   GLU A 265      96.553  30.842  -3.706  1.00 14.64           C  
-ATOM   1881  O   GLU A 265      96.732  31.784  -2.934  1.00 14.77           O  
-ATOM   1882  CB  GLU A 265      96.304  31.674  -6.085  1.00 14.97           C  
-ATOM   1883  CG  GLU A 265      96.905  31.796  -7.496  1.00 15.75           C  
-ATOM   1884  CD  GLU A 265      98.199  32.625  -7.561  1.00 17.96           C  
-ATOM   1885  OE1 GLU A 265      98.591  33.245  -6.549  1.00 19.12           O  
-ATOM   1886  OE2 GLU A 265      98.826  32.668  -8.642  1.00 17.25           O  
-ATOM   1887  N   ARG A 266      95.873  29.748  -3.372  1.00 15.19           N  
-ATOM   1888  CA  ARG A 266      95.254  29.545  -2.059  1.00 15.45           C  
-ATOM   1889  C   ARG A 266      94.101  30.508  -1.768  1.00 16.68           C  
-ATOM   1890  O   ARG A 266      94.161  31.323  -0.840  1.00 16.23           O  
-ATOM   1891  CB  ARG A 266      96.309  29.611  -0.945  1.00 14.26           C  
-ATOM   1892  CG  ARG A 266      97.614  28.847  -1.249  1.00 14.09           C  
-ATOM   1893  CD  ARG A 266      97.374  27.410  -1.697  1.00 12.19           C  
-ATOM   1894  NE  ARG A 266      96.738  26.620  -0.649  1.00 12.66           N  
-ATOM   1895  CZ  ARG A 266      95.659  25.862  -0.824  1.00 12.99           C  
-ATOM   1896  NH1 ARG A 266      95.076  25.781  -2.016  1.00 11.02           N  
-ATOM   1897  NH2 ARG A 266      95.169  25.177   0.201  1.00 11.54           N  
-ATOM   1898  N   THR A 267      93.020  30.352  -2.527  1.00 17.12           N  
-ATOM   1899  CA  THR A 267      91.837  31.197  -2.396  1.00 17.28           C  
-ATOM   1900  C   THR A 267      90.608  30.405  -1.934  1.00 16.85           C  
-ATOM   1901  O   THR A 267      90.086  29.548  -2.659  1.00 14.90           O  
-ATOM   1902  CB  THR A 267      91.542  31.897  -3.737  1.00 17.12           C  
-ATOM   1903  OG1 THR A 267      92.743  32.523  -4.214  1.00 16.91           O  
-ATOM   1904  CG2 THR A 267      90.451  32.944  -3.576  1.00 15.66           C  
-ATOM   1905  N   GLY A 268      90.172  30.693  -0.713  1.00 17.09           N  
-ATOM   1906  CA  GLY A 268      89.016  30.023  -0.148  1.00 18.47           C  
-ATOM   1907  C   GLY A 268      88.098  31.009   0.540  1.00 17.95           C  
-ATOM   1908  O   GLY A 268      88.459  32.172   0.708  1.00 17.60           O  
-ATOM   1909  N   CYS A 269      86.959  30.526   1.027  1.00 19.47           N  
-ATOM   1910  CA  CYS A 269      85.977  31.392   1.676  1.00 20.50           C  
-ATOM   1911  C   CYS A 269      85.117  30.677   2.731  1.00 18.37           C  
-ATOM   1912  O   CYS A 269      84.590  29.600   2.471  1.00 18.09           O  
-ATOM   1913  CB  CYS A 269      85.075  31.972   0.585  1.00 22.56           C  
-ATOM   1914  SG  CYS A 269      83.836  33.115   1.152  1.00 31.69           S  
-ATOM   1915  N   LEU A 270      85.004  31.259   3.924  1.00 16.83           N  
-ATOM   1916  CA  LEU A 270      84.181  30.677   4.985  1.00 16.75           C  
-ATOM   1917  C   LEU A 270      82.949  31.551   5.182  1.00 16.82           C  
-ATOM   1918  O   LEU A 270      83.071  32.729   5.525  1.00 16.60           O  
-ATOM   1919  CB  LEU A 270      84.932  30.601   6.319  1.00 15.93           C  
-ATOM   1920  CG  LEU A 270      84.555  29.525   7.365  1.00 16.35           C  
-ATOM   1921  CD1 LEU A 270      84.596  30.113   8.769  1.00 14.90           C  
-ATOM   1922  CD2 LEU A 270      83.198  28.896   7.104  1.00 15.69           C  
-ATOM   1923  N   LEU A 271      81.773  30.967   4.972  1.00 16.77           N  
-ATOM   1924  CA  LEU A 271      80.501  31.667   5.136  1.00 16.70           C  
-ATOM   1925  C   LEU A 271      79.782  31.163   6.377  1.00 16.54           C  
-ATOM   1926  O   LEU A 271      79.611  29.954   6.559  1.00 16.54           O  
-ATOM   1927  CB  LEU A 271      79.608  31.453   3.909  1.00 16.76           C  
-ATOM   1928  CG  LEU A 271      80.061  32.103   2.601  1.00 16.90           C  
-ATOM   1929  CD1 LEU A 271      79.199  31.643   1.457  1.00 18.08           C  
-ATOM   1930  CD2 LEU A 271      79.990  33.601   2.729  1.00 17.91           C  
-ATOM   1931  N   ALA A 272      79.404  32.088   7.250  1.00 17.19           N  
-ATOM   1932  CA  ALA A 272      78.679  31.750   8.470  1.00 18.26           C  
-ATOM   1933  C   ALA A 272      77.256  32.321   8.396  1.00 18.82           C  
-ATOM   1934  O   ALA A 272      77.059  33.540   8.460  1.00 18.83           O  
-ATOM   1935  CB  ALA A 272      79.410  32.300   9.696  1.00 17.88           C  
-ATOM   1936  N   LEU A 273      76.284  31.444   8.172  1.00 19.32           N  
-ATOM   1937  CA  LEU A 273      74.876  31.836   8.094  1.00 20.33           C  
-ATOM   1938  C   LEU A 273      74.321  31.785   9.513  1.00 21.04           C  
-ATOM   1939  O   LEU A 273      74.272  30.717  10.133  1.00 21.29           O  
-ATOM   1940  CB  LEU A 273      74.104  30.879   7.184  1.00 20.63           C  
-ATOM   1941  CG  LEU A 273      74.196  31.080   5.669  1.00 21.51           C  
-ATOM   1942  CD1 LEU A 273      75.638  31.234   5.195  1.00 22.89           C  
-ATOM   1943  CD2 LEU A 273      73.537  29.901   4.988  1.00 21.68           C  
-ATOM   1944  N   CYS A 274      73.911  32.938  10.026  1.00 21.81           N  
-ATOM   1945  CA  CYS A 274      73.407  33.034  11.388  1.00 23.36           C  
-ATOM   1946  C   CYS A 274      71.914  33.337  11.482  1.00 24.19           C  
-ATOM   1947  O   CYS A 274      71.325  33.890  10.561  1.00 23.54           O  
-ATOM   1948  CB  CYS A 274      74.196  34.104  12.139  1.00 23.82           C  
-ATOM   1949  SG  CYS A 274      75.981  33.984  11.900  1.00 24.52           S  
-ATOM   1950  N   ALA A 275      71.323  33.003  12.627  1.00 25.67           N  
-ATOM   1951  CA  ALA A 275      69.898  33.222  12.876  1.00 28.40           C  
-ATOM   1952  C   ALA A 275      69.482  34.688  12.994  1.00 29.96           C  
-ATOM   1953  O   ALA A 275      68.319  35.021  12.760  1.00 30.38           O  
-ATOM   1954  CB  ALA A 275      69.462  32.461  14.112  1.00 27.74           C  
-ATOM   1955  N   ASP A 276      70.414  35.553  13.387  1.00 31.12           N  
-ATOM   1956  CA  ASP A 276      70.123  36.976  13.532  1.00 32.48           C  
-ATOM   1957  C   ASP A 276      71.376  37.840  13.429  1.00 32.66           C  
-ATOM   1958  O   ASP A 276      72.487  37.368  13.681  1.00 33.14           O  
-ATOM   1959  CB  ASP A 276      69.390  37.250  14.850  1.00 33.78           C  
-ATOM   1960  CG  ASP A 276      70.079  36.629  16.045  1.00 35.83           C  
-ATOM   1961  OD1 ASP A 276      71.053  37.225  16.541  1.00 38.07           O  
-ATOM   1962  OD2 ASP A 276      69.642  35.550  16.500  1.00 38.13           O  
-ATOM   1963  N   ALA A 277      71.178  39.111  13.084  1.00 32.59           N  
-ATOM   1964  CA  ALA A 277      72.267  40.073  12.921  1.00 32.24           C  
-ATOM   1965  C   ALA A 277      73.196  40.192  14.123  1.00 32.02           C  
-ATOM   1966  O   ALA A 277      74.406  40.341  13.961  1.00 32.14           O  
-ATOM   1967  CB  ALA A 277      71.710  41.439  12.551  1.00 32.50           C  
-ATOM   1968  N   ALA A 278      72.638  40.136  15.329  1.00 31.76           N  
-ATOM   1969  CA  ALA A 278      73.454  40.234  16.535  1.00 31.71           C  
-ATOM   1970  C   ALA A 278      74.469  39.095  16.529  1.00 31.88           C  
-ATOM   1971  O   ALA A 278      75.658  39.314  16.767  1.00 32.21           O  
-ATOM   1972  CB  ALA A 278      72.587  40.163  17.774  1.00 30.93           C  
-ATOM   1973  N   THR A 279      73.996  37.893  16.208  1.00 31.77           N  
-ATOM   1974  CA  THR A 279      74.851  36.717  16.148  1.00 31.48           C  
-ATOM   1975  C   THR A 279      75.853  36.873  15.006  1.00 31.19           C  
-ATOM   1976  O   THR A 279      77.002  36.447  15.119  1.00 31.10           O  
-ATOM   1977  CB  THR A 279      74.033  35.417  15.913  1.00 31.82           C  
-ATOM   1978  OG1 THR A 279      72.923  35.370  16.817  1.00 31.61           O  
-ATOM   1979  CG2 THR A 279      74.905  34.190  16.145  1.00 30.99           C  
-ATOM   1980  N   ARG A 280      75.420  37.493  13.914  1.00 30.63           N  
-ATOM   1981  CA  ARG A 280      76.290  37.693  12.764  1.00 32.01           C  
-ATOM   1982  C   ARG A 280      77.513  38.530  13.142  1.00 32.78           C  
-ATOM   1983  O   ARG A 280      78.637  38.186  12.775  1.00 32.59           O  
-ATOM   1984  CB  ARG A 280      75.534  38.369  11.621  1.00 32.79           C  
-ATOM   1985  CG  ARG A 280      76.230  38.269  10.277  1.00 34.05           C  
-ATOM   1986  CD  ARG A 280      76.252  39.601   9.553  1.00 36.26           C  
-ATOM   1987  NE  ARG A 280      77.205  40.514  10.170  1.00 38.27           N  
-ATOM   1988  CZ  ARG A 280      78.330  40.926   9.592  1.00 39.94           C  
-ATOM   1989  NH1 ARG A 280      78.647  40.523   8.365  1.00 39.26           N  
-ATOM   1990  NH2 ARG A 280      79.137  41.755  10.245  1.00 40.75           N  
-ATOM   1991  N   GLU A 281      77.298  39.610  13.891  1.00 33.38           N  
-ATOM   1992  CA  GLU A 281      78.398  40.473  14.312  1.00 34.01           C  
-ATOM   1993  C   GLU A 281      79.343  39.687  15.204  1.00 32.72           C  
-ATOM   1994  O   GLU A 281      80.563  39.857  15.140  1.00 32.40           O  
-ATOM   1995  CB  GLU A 281      77.883  41.697  15.078  1.00 37.31           C  
-ATOM   1996  CG  GLU A 281      76.754  42.458  14.387  1.00 42.97           C  
-ATOM   1997  CD  GLU A 281      77.014  42.726  12.918  1.00 46.09           C  
-ATOM   1998  OE1 GLU A 281      78.070  43.308  12.566  1.00 46.96           O  
-ATOM   1999  OE2 GLU A 281      76.138  42.352  12.095  1.00 47.71           O  
-ATOM   2000  N   LEU A 282      78.765  38.814  16.023  1.00 30.73           N  
-ATOM   2001  CA  LEU A 282      79.524  37.965  16.932  1.00 29.94           C  
-ATOM   2002  C   LEU A 282      80.408  36.991  16.146  1.00 28.98           C  
-ATOM   2003  O   LEU A 282      81.586  36.797  16.466  1.00 29.41           O  
-ATOM   2004  CB  LEU A 282      78.556  37.180  17.820  1.00 30.61           C  
-ATOM   2005  CG  LEU A 282      78.631  37.363  19.335  1.00 30.83           C  
-ATOM   2006  CD1 LEU A 282      78.711  38.831  19.706  1.00 30.53           C  
-ATOM   2007  CD2 LEU A 282      77.414  36.707  19.975  1.00 31.06           C  
-ATOM   2008  N   ALA A 283      79.830  36.397  15.106  1.00 27.31           N  
-ATOM   2009  CA  ALA A 283      80.532  35.439  14.265  1.00 26.00           C  
-ATOM   2010  C   ALA A 283      81.606  36.119  13.426  1.00 24.77           C  
-ATOM   2011  O   ALA A 283      82.737  35.646  13.358  1.00 24.42           O  
-ATOM   2012  CB  ALA A 283      79.540  34.701  13.367  1.00 25.46           C  
-ATOM   2013  N   GLN A 284      81.255  37.240  12.808  1.00 23.47           N  
-ATOM   2014  CA  GLN A 284      82.192  37.975  11.974  1.00 23.44           C  
-ATOM   2015  C   GLN A 284      83.418  38.416  12.779  1.00 22.96           C  
-ATOM   2016  O   GLN A 284      84.555  38.326  12.300  1.00 23.30           O  
-ATOM   2017  CB  GLN A 284      81.496  39.185  11.337  1.00 23.21           C  
-ATOM   2018  CG  GLN A 284      82.371  39.998  10.383  1.00 22.79           C  
-ATOM   2019  CD  GLN A 284      82.805  39.222   9.157  1.00 21.99           C  
-ATOM   2020  OE1 GLN A 284      82.069  39.127   8.182  1.00 22.87           O  
-ATOM   2021  NE2 GLN A 284      84.015  38.682   9.191  1.00 21.78           N  
-ATOM   2022  N   GLY A 285      83.183  38.869  14.006  1.00 21.75           N  
-ATOM   2023  CA  GLY A 285      84.273  39.305  14.852  1.00 20.26           C  
-ATOM   2024  C   GLY A 285      85.191  38.159  15.221  1.00 20.04           C  
-ATOM   2025  O   GLY A 285      86.412  38.298  15.171  1.00 20.54           O  
-ATOM   2026  N   ALA A 286      84.608  37.017  15.574  1.00 19.23           N  
-ATOM   2027  CA  ALA A 286      85.387  35.840  15.957  1.00 18.85           C  
-ATOM   2028  C   ALA A 286      86.175  35.259  14.783  1.00 18.04           C  
-ATOM   2029  O   ALA A 286      87.255  34.702  14.972  1.00 17.97           O  
-ATOM   2030  CB  ALA A 286      84.484  34.778  16.572  1.00 18.25           C  
-ATOM   2031  N   MET A 287      85.627  35.384  13.580  1.00 17.98           N  
-ATOM   2032  CA  MET A 287      86.285  34.895  12.375  1.00 18.67           C  
-ATOM   2033  C   MET A 287      87.497  35.771  12.073  1.00 19.67           C  
-ATOM   2034  O   MET A 287      88.571  35.263  11.736  1.00 20.78           O  
-ATOM   2035  CB  MET A 287      85.319  34.912  11.191  1.00 19.50           C  
-ATOM   2036  CG  MET A 287      84.279  33.791  11.208  1.00 22.25           C  
-ATOM   2037  SD  MET A 287      82.834  34.148  10.160  1.00 24.79           S  
-ATOM   2038  CE  MET A 287      83.245  33.338   8.659  1.00 23.84           C  
-ATOM   2039  N   ALA A 288      87.326  37.086  12.206  1.00 18.98           N  
-ATOM   2040  CA  ALA A 288      88.408  38.039  11.963  1.00 18.43           C  
-ATOM   2041  C   ALA A 288      89.531  37.787  12.968  1.00 18.82           C  
-ATOM   2042  O   ALA A 288      90.711  37.792  12.623  1.00 19.81           O  
-ATOM   2043  CB  ALA A 288      87.889  39.458  12.087  1.00 17.52           C  
-ATOM   2044  N   PHE A 289      89.145  37.540  14.211  1.00 18.42           N  
-ATOM   2045  CA  PHE A 289      90.078  37.249  15.289  1.00 18.19           C  
-ATOM   2046  C   PHE A 289      90.885  35.983  14.945  1.00 18.58           C  
-ATOM   2047  O   PHE A 289      92.099  35.922  15.178  1.00 18.87           O  
-ATOM   2048  CB  PHE A 289      89.273  37.053  16.582  1.00 17.77           C  
-ATOM   2049  CG  PHE A 289      90.079  36.564  17.747  1.00 18.41           C  
-ATOM   2050  CD1 PHE A 289      90.823  37.452  18.519  1.00 18.44           C  
-ATOM   2051  CD2 PHE A 289      90.084  35.212  18.082  1.00 17.41           C  
-ATOM   2052  CE1 PHE A 289      91.560  36.999  19.605  1.00 18.03           C  
-ATOM   2053  CE2 PHE A 289      90.818  34.751  19.163  1.00 17.78           C  
-ATOM   2054  CZ  PHE A 289      91.557  35.643  19.927  1.00 17.42           C  
-ATOM   2055  N   LEU A 290      90.205  34.990  14.378  1.00 18.35           N  
-ATOM   2056  CA  LEU A 290      90.825  33.725  13.990  1.00 18.28           C  
-ATOM   2057  C   LEU A 290      91.899  33.930  12.924  1.00 18.88           C  
-ATOM   2058  O   LEU A 290      92.947  33.284  12.964  1.00 19.41           O  
-ATOM   2059  CB  LEU A 290      89.757  32.746  13.492  1.00 17.41           C  
-ATOM   2060  CG  LEU A 290      89.550  31.420  14.235  1.00 17.77           C  
-ATOM   2061  CD1 LEU A 290      89.933  31.521  15.698  1.00 16.03           C  
-ATOM   2062  CD2 LEU A 290      88.102  30.980  14.080  1.00 15.52           C  
-ATOM   2063  N   ASN A 291      91.639  34.806  11.960  1.00 18.67           N  
-ATOM   2064  CA  ASN A 291      92.636  35.077  10.932  1.00 18.76           C  
-ATOM   2065  C   ASN A 291      93.834  35.770  11.573  1.00 19.31           C  
-ATOM   2066  O   ASN A 291      94.977  35.366  11.354  1.00 19.08           O  
-ATOM   2067  CB  ASN A 291      92.059  35.934   9.802  1.00 17.80           C  
-ATOM   2068  CG  ASN A 291      91.655  35.106   8.592  1.00 17.72           C  
-ATOM   2069  OD1 ASN A 291      91.612  33.871   8.649  1.00 17.53           O  
-ATOM   2070  ND2 ASN A 291      91.377  35.780   7.483  1.00 17.24           N  
-ATOM   2071  N   ARG A 292      93.562  36.748  12.437  1.00 20.41           N  
-ATOM   2072  CA  ARG A 292      94.617  37.496  13.131  1.00 21.99           C  
-ATOM   2073  C   ARG A 292      95.609  36.615  13.891  1.00 20.92           C  
-ATOM   2074  O   ARG A 292      96.823  36.772  13.745  1.00 20.14           O  
-ATOM   2075  CB  ARG A 292      94.030  38.498  14.133  1.00 23.65           C  
-ATOM   2076  CG  ARG A 292      93.030  39.474  13.572  1.00 28.61           C  
-ATOM   2077  CD  ARG A 292      93.037  40.798  14.338  1.00 32.01           C  
-ATOM   2078  NE  ARG A 292      93.214  40.638  15.782  1.00 35.02           N  
-ATOM   2079  CZ  ARG A 292      92.244  40.762  16.684  1.00 35.94           C  
-ATOM   2080  NH1 ARG A 292      90.999  41.040  16.311  1.00 35.87           N  
-ATOM   2081  NH2 ARG A 292      92.535  40.654  17.972  1.00 37.17           N  
-ATOM   2082  N   GLN A 293      95.082  35.698  14.699  1.00 20.41           N  
-ATOM   2083  CA  GLN A 293      95.906  34.815  15.517  1.00 20.13           C  
-ATOM   2084  C   GLN A 293      96.591  33.689  14.750  1.00 19.65           C  
-ATOM   2085  O   GLN A 293      97.390  32.942  15.317  1.00 20.62           O  
-ATOM   2086  CB  GLN A 293      95.083  34.228  16.672  1.00 20.31           C  
-ATOM   2087  CG  GLN A 293      94.265  35.244  17.471  1.00 21.11           C  
-ATOM   2088  CD  GLN A 293      95.064  36.474  17.889  1.00 22.32           C  
-ATOM   2089  OE1 GLN A 293      96.232  36.379  18.267  1.00 22.86           O  
-ATOM   2090  NE2 GLN A 293      94.430  37.636  17.818  1.00 21.60           N  
-ATOM   2091  N   THR A 294      96.285  33.566  13.465  1.00 18.86           N  
-ATOM   2092  CA  THR A 294      96.887  32.519  12.655  1.00 18.12           C  
-ATOM   2093  C   THR A 294      97.917  33.064  11.667  1.00 17.60           C  
-ATOM   2094  O   THR A 294      98.985  32.476  11.490  1.00 16.60           O  
-ATOM   2095  CB  THR A 294      95.794  31.716  11.917  1.00 17.84           C  
-ATOM   2096  OG1 THR A 294      94.827  31.269  12.874  1.00 19.05           O  
-ATOM   2097  CG2 THR A 294      96.389  30.495  11.223  1.00 16.69           C  
-ATOM   2098  N   TYR A 295      97.604  34.197  11.044  1.00 17.21           N  
-ATOM   2099  CA  TYR A 295      98.500  34.810  10.068  1.00 17.51           C  
-ATOM   2100  C   TYR A 295      98.155  36.262   9.750  1.00 17.72           C  
-ATOM   2101  O   TYR A 295      98.553  36.776   8.708  1.00 18.47           O  
-ATOM   2102  CB  TYR A 295      98.517  33.987   8.771  1.00 18.04           C  
-ATOM   2103  CG  TYR A 295      97.142  33.567   8.271  1.00 19.04           C  
-ATOM   2104  CD1 TYR A 295      96.185  34.515   7.892  1.00 19.28           C  
-ATOM   2105  CD2 TYR A 295      96.788  32.220   8.211  1.00 18.82           C  
-ATOM   2106  CE1 TYR A 295      94.912  34.128   7.468  1.00 18.69           C  
-ATOM   2107  CE2 TYR A 295      95.521  31.824   7.794  1.00 18.87           C  
-ATOM   2108  CZ  TYR A 295      94.589  32.781   7.425  1.00 19.18           C  
-ATOM   2109  OH  TYR A 295      93.332  32.382   7.023  1.00 19.98           O  
-ATOM   2110  N   SER A 296      97.442  36.926  10.655  1.00 17.30           N  
-ATOM   2111  CA  SER A 296      97.036  38.314  10.457  1.00 17.97           C  
-ATOM   2112  C   SER A 296      96.081  38.501   9.279  1.00 18.43           C  
-ATOM   2113  O   SER A 296      94.865  38.463   9.454  1.00 21.24           O  
-ATOM   2114  CB  SER A 296      98.252  39.235  10.287  1.00 18.40           C  
-ATOM   2115  OG  SER A 296      98.975  39.393  11.501  1.00 20.66           O  
-ATOM   2116  N   PHE A 297      96.628  38.688   8.083  1.00 17.85           N  
-ATOM   2117  CA  PHE A 297      95.820  38.918   6.886  1.00 16.29           C  
-ATOM   2118  C   PHE A 297      95.888  37.726   5.949  1.00 16.23           C  
-ATOM   2119  O   PHE A 297      96.884  37.004   5.919  1.00 15.54           O  
-ATOM   2120  CB  PHE A 297      96.322  40.154   6.121  1.00 15.65           C  
-ATOM   2121  CG  PHE A 297      96.260  41.437   6.900  1.00 15.16           C  
-ATOM   2122  CD1 PHE A 297      97.305  41.807   7.739  1.00 15.26           C  
-ATOM   2123  CD2 PHE A 297      95.160  42.274   6.794  1.00 14.59           C  
-ATOM   2124  CE1 PHE A 297      97.257  42.993   8.460  1.00 14.89           C  
-ATOM   2125  CE2 PHE A 297      95.101  43.460   7.508  1.00 15.68           C  
-ATOM   2126  CZ  PHE A 297      96.155  43.823   8.346  1.00 15.73           C  
-ATOM   2127  N   PRO A 298      94.806  37.495   5.183  1.00 16.46           N  
-ATOM   2128  CA  PRO A 298      94.748  36.388   4.222  1.00 16.35           C  
-ATOM   2129  C   PRO A 298      95.362  36.826   2.881  1.00 15.97           C  
-ATOM   2130  O   PRO A 298      95.491  38.020   2.606  1.00 15.35           O  
-ATOM   2131  CB  PRO A 298      93.237  36.133   4.114  1.00 16.58           C  
-ATOM   2132  CG  PRO A 298      92.667  37.521   4.226  1.00 16.54           C  
-ATOM   2133  CD  PRO A 298      93.485  38.117   5.360  1.00 17.12           C  
-ATOM   2134  N   PRO A 299      95.773  35.864   2.040  1.00 16.44           N  
-ATOM   2135  CA  PRO A 299      96.381  36.164   0.738  1.00 17.24           C  
-ATOM   2136  C   PRO A 299      95.438  37.010  -0.116  1.00 16.87           C  
-ATOM   2137  O   PRO A 299      94.231  36.786  -0.124  1.00 18.68           O  
-ATOM   2138  CB  PRO A 299      96.582  34.775   0.127  1.00 18.08           C  
-ATOM   2139  CG  PRO A 299      96.749  33.891   1.329  1.00 18.36           C  
-ATOM   2140  CD  PRO A 299      95.677  34.410   2.252  1.00 16.45           C  
-ATOM   2141  N   PHE A 300      96.002  37.943  -0.870  1.00 15.89           N  
-ATOM   2142  CA  PHE A 300      95.219  38.848  -1.699  1.00 14.55           C  
-ATOM   2143  C   PHE A 300      95.129  38.482  -3.176  1.00 14.08           C  
-ATOM   2144  O   PHE A 300      94.060  38.592  -3.773  1.00 14.52           O  
-ATOM   2145  CB  PHE A 300      95.780  40.277  -1.535  1.00 14.17           C  
-ATOM   2146  CG  PHE A 300      95.195  41.303  -2.485  1.00 13.53           C  
-ATOM   2147  CD1 PHE A 300      95.779  41.537  -3.729  1.00 14.64           C  
-ATOM   2148  CD2 PHE A 300      94.084  42.054  -2.125  1.00 14.24           C  
-ATOM   2149  CE1 PHE A 300      95.263  42.505  -4.597  1.00 13.46           C  
-ATOM   2150  CE2 PHE A 300      93.565  43.022  -2.986  1.00 13.28           C  
-ATOM   2151  CZ  PHE A 300      94.156  43.247  -4.223  1.00 12.03           C  
-ATOM   2152  N   HIS A 301      96.231  38.021  -3.758  1.00 12.33           N  
-ATOM   2153  CA  HIS A 301      96.260  37.732  -5.187  1.00 11.84           C  
-ATOM   2154  C   HIS A 301      95.126  36.904  -5.785  1.00 12.61           C  
-ATOM   2155  O   HIS A 301      94.476  37.347  -6.735  1.00 13.49           O  
-ATOM   2156  CB  HIS A 301      97.609  37.147  -5.614  1.00  9.67           C  
-ATOM   2157  CG  HIS A 301      97.864  37.253  -7.083  1.00  7.88           C  
-ATOM   2158  ND1 HIS A 301      98.150  38.453  -7.700  1.00  9.65           N  
-ATOM   2159  CD2 HIS A 301      97.835  36.326  -8.068  1.00  8.60           C  
-ATOM   2160  CE1 HIS A 301      98.284  38.262  -9.000  1.00  8.30           C  
-ATOM   2161  NE2 HIS A 301      98.095  36.981  -9.249  1.00  8.22           N  
-ATOM   2162  N   GLY A 302      94.925  35.695  -5.273  1.00 12.90           N  
-ATOM   2163  CA  GLY A 302      93.888  34.827  -5.800  1.00 12.79           C  
-ATOM   2164  C   GLY A 302      92.506  35.414  -5.640  1.00 13.64           C  
-ATOM   2165  O   GLY A 302      91.705  35.386  -6.574  1.00 14.38           O  
-ATOM   2166  N   ALA A 303      92.233  35.959  -4.459  1.00 14.09           N  
-ATOM   2167  CA  ALA A 303      90.943  36.566  -4.154  1.00 14.71           C  
-ATOM   2168  C   ALA A 303      90.631  37.702  -5.127  1.00 15.46           C  
-ATOM   2169  O   ALA A 303      89.511  37.813  -5.631  1.00 16.53           O  
-ATOM   2170  CB  ALA A 303      90.929  37.068  -2.721  1.00 14.03           C  
-ATOM   2171  N   LYS A 304      91.633  38.519  -5.423  1.00 15.53           N  
-ATOM   2172  CA  LYS A 304      91.453  39.625  -6.348  1.00 15.42           C  
-ATOM   2173  C   LYS A 304      91.213  39.115  -7.771  1.00 15.18           C  
-ATOM   2174  O   LYS A 304      90.535  39.768  -8.557  1.00 14.48           O  
-ATOM   2175  CB  LYS A 304      92.664  40.561  -6.304  1.00 17.37           C  
-ATOM   2176  CG  LYS A 304      92.515  41.838  -7.130  1.00 18.15           C  
-ATOM   2177  CD  LYS A 304      91.352  42.675  -6.645  1.00 19.62           C  
-ATOM   2178  CE  LYS A 304      91.284  43.993  -7.381  1.00 20.71           C  
-ATOM   2179  NZ  LYS A 304      90.107  44.778  -6.921  1.00 22.93           N  
-ATOM   2180  N   ILE A 305      91.789  37.965  -8.114  1.00 14.60           N  
-ATOM   2181  CA  ILE A 305      91.583  37.399  -9.446  1.00 14.86           C  
-ATOM   2182  C   ILE A 305      90.112  37.016  -9.556  1.00 15.36           C  
-ATOM   2183  O   ILE A 305      89.441  37.345 -10.534  1.00 15.56           O  
-ATOM   2184  CB  ILE A 305      92.434  36.110  -9.680  1.00 14.96           C  
-ATOM   2185  CG1 ILE A 305      93.911  36.461  -9.890  1.00 14.25           C  
-ATOM   2186  CG2 ILE A 305      91.906  35.332 -10.890  1.00 14.73           C  
-ATOM   2187  CD1 ILE A 305      94.794  35.250 -10.048  1.00 11.30           C  
-ATOM   2188  N   VAL A 306      89.618  36.341  -8.521  1.00 14.98           N  
-ATOM   2189  CA  VAL A 306      88.240  35.876  -8.461  1.00 14.76           C  
-ATOM   2190  C   VAL A 306      87.217  37.010  -8.530  1.00 15.06           C  
-ATOM   2191  O   VAL A 306      86.364  37.017  -9.414  1.00 14.31           O  
-ATOM   2192  CB  VAL A 306      88.011  35.031  -7.195  1.00 14.45           C  
-ATOM   2193  CG1 VAL A 306      86.540  34.676  -7.048  1.00 14.51           C  
-ATOM   2194  CG2 VAL A 306      88.858  33.768  -7.262  1.00 12.24           C  
-ATOM   2195  N   SER A 307      87.320  37.977  -7.624  1.00 16.10           N  
-ATOM   2196  CA  SER A 307      86.389  39.096  -7.617  1.00 17.13           C  
-ATOM   2197  C   SER A 307      86.401  39.854  -8.949  1.00 18.55           C  
-ATOM   2198  O   SER A 307      85.359  40.317  -9.410  1.00 19.75           O  
-ATOM   2199  CB  SER A 307      86.686  40.035  -6.453  1.00 17.24           C  
-ATOM   2200  OG  SER A 307      87.986  40.585  -6.549  1.00 19.26           O  
-ATOM   2201  N   THR A 308      87.572  39.952  -9.574  1.00 18.68           N  
-ATOM   2202  CA  THR A 308      87.721  40.623 -10.861  1.00 19.50           C  
-ATOM   2203  C   THR A 308      86.956  39.872 -11.960  1.00 20.83           C  
-ATOM   2204  O   THR A 308      86.268  40.480 -12.781  1.00 21.71           O  
-ATOM   2205  CB  THR A 308      89.220  40.730 -11.248  1.00 19.86           C  
-ATOM   2206  OG1 THR A 308      89.903  41.540 -10.284  1.00 19.63           O  
-ATOM   2207  CG2 THR A 308      89.399  41.342 -12.632  1.00 19.04           C  
-ATOM   2208  N   VAL A 309      87.087  38.548 -11.975  1.00 20.98           N  
-ATOM   2209  CA  VAL A 309      86.408  37.714 -12.960  1.00 20.31           C  
-ATOM   2210  C   VAL A 309      84.895  37.798 -12.752  1.00 20.98           C  
-ATOM   2211  O   VAL A 309      84.122  37.935 -13.702  1.00 20.92           O  
-ATOM   2212  CB  VAL A 309      86.860  36.235 -12.831  1.00 19.67           C  
-ATOM   2213  CG1 VAL A 309      85.967  35.321 -13.663  1.00 19.15           C  
-ATOM   2214  CG2 VAL A 309      88.305  36.095 -13.272  1.00 18.94           C  
-ATOM   2215  N   LEU A 310      84.485  37.742 -11.495  1.00 20.82           N  
-ATOM   2216  CA  LEU A 310      83.079  37.790 -11.146  1.00 20.96           C  
-ATOM   2217  C   LEU A 310      82.403  39.137 -11.353  1.00 21.62           C  
-ATOM   2218  O   LEU A 310      81.215  39.177 -11.649  1.00 22.77           O  
-ATOM   2219  CB  LEU A 310      82.891  37.320  -9.701  1.00 19.81           C  
-ATOM   2220  CG  LEU A 310      82.402  35.885  -9.468  1.00 18.65           C  
-ATOM   2221  CD1 LEU A 310      82.845  34.959 -10.573  1.00 17.71           C  
-ATOM   2222  CD2 LEU A 310      82.887  35.405  -8.116  1.00 17.95           C  
-ATOM   2223  N   THR A 311      83.139  40.233 -11.189  1.00 22.28           N  
-ATOM   2224  CA  THR A 311      82.559  41.566 -11.340  1.00 22.67           C  
-ATOM   2225  C   THR A 311      82.632  42.135 -12.752  1.00 23.55           C  
-ATOM   2226  O   THR A 311      81.865  43.034 -13.104  1.00 24.42           O  
-ATOM   2227  CB  THR A 311      83.181  42.569 -10.352  1.00 21.62           C  
-ATOM   2228  OG1 THR A 311      84.595  42.635 -10.558  1.00 22.84           O  
-ATOM   2229  CG2 THR A 311      82.907  42.141  -8.926  1.00 21.62           C  
-ATOM   2230  N   THR A 312      83.564  41.632 -13.551  1.00 24.54           N  
-ATOM   2231  CA  THR A 312      83.726  42.082 -14.929  1.00 25.07           C  
-ATOM   2232  C   THR A 312      82.936  41.159 -15.855  1.00 25.64           C  
-ATOM   2233  O   THR A 312      83.410  40.084 -16.224  1.00 26.17           O  
-ATOM   2234  CB  THR A 312      85.212  42.084 -15.335  1.00 25.01           C  
-ATOM   2235  OG1 THR A 312      85.934  42.965 -14.468  1.00 26.50           O  
-ATOM   2236  CG2 THR A 312      85.382  42.550 -16.772  1.00 24.81           C  
-ATOM   2237  N   PRO A 313      81.753  41.608 -16.308  1.00 26.18           N  
-ATOM   2238  CA  PRO A 313      80.840  40.883 -17.196  1.00 26.45           C  
-ATOM   2239  C   PRO A 313      81.530  40.096 -18.299  1.00 27.52           C  
-ATOM   2240  O   PRO A 313      81.272  38.908 -18.476  1.00 28.30           O  
-ATOM   2241  CB  PRO A 313      79.983  41.999 -17.773  1.00 26.51           C  
-ATOM   2242  CG  PRO A 313      79.879  42.934 -16.635  1.00 26.92           C  
-ATOM   2243  CD  PRO A 313      81.295  42.998 -16.131  1.00 25.88           C  
-ATOM   2244  N   GLU A 314      82.427  40.756 -19.021  1.00 28.66           N  
-ATOM   2245  CA  GLU A 314      83.149  40.113 -20.111  1.00 29.90           C  
-ATOM   2246  C   GLU A 314      83.912  38.891 -19.613  1.00 29.45           C  
-ATOM   2247  O   GLU A 314      83.875  37.830 -20.230  1.00 29.40           O  
-ATOM   2248  CB  GLU A 314      84.133  41.092 -20.760  1.00 32.66           C  
-ATOM   2249  CG  GLU A 314      83.549  42.450 -21.142  1.00 37.21           C  
-ATOM   2250  CD  GLU A 314      83.600  43.460 -20.005  1.00 39.79           C  
-ATOM   2251  OE1 GLU A 314      84.712  43.928 -19.677  1.00 41.12           O  
-ATOM   2252  OE2 GLU A 314      82.529  43.794 -19.444  1.00 41.60           O  
-ATOM   2253  N   LEU A 315      84.586  39.042 -18.479  1.00 29.24           N  
-ATOM   2254  CA  LEU A 315      85.373  37.955 -17.909  1.00 29.07           C  
-ATOM   2255  C   LEU A 315      84.494  36.846 -17.330  1.00 28.84           C  
-ATOM   2256  O   LEU A 315      84.694  35.667 -17.638  1.00 28.89           O  
-ATOM   2257  CB  LEU A 315      86.346  38.499 -16.855  1.00 28.77           C  
-ATOM   2258  CG  LEU A 315      87.693  39.052 -17.347  1.00 28.09           C  
-ATOM   2259  CD1 LEU A 315      87.546  39.808 -18.651  1.00 28.42           C  
-ATOM   2260  CD2 LEU A 315      88.305  39.941 -16.275  1.00 27.82           C  
-ATOM   2261  N   ARG A 316      83.517  37.228 -16.513  1.00 28.07           N  
-ATOM   2262  CA  ARG A 316      82.596  36.273 -15.901  1.00 28.12           C  
-ATOM   2263  C   ARG A 316      82.005  35.375 -16.985  1.00 27.13           C  
-ATOM   2264  O   ARG A 316      81.885  34.160 -16.810  1.00 26.57           O  
-ATOM   2265  CB  ARG A 316      81.470  37.021 -15.181  1.00 29.33           C  
-ATOM   2266  CG  ARG A 316      80.514  36.136 -14.397  1.00 31.77           C  
-ATOM   2267  CD  ARG A 316      79.324  36.941 -13.890  1.00 33.64           C  
-ATOM   2268  NE  ARG A 316      79.060  36.717 -12.468  1.00 36.70           N  
-ATOM   2269  CZ  ARG A 316      78.533  35.604 -11.961  1.00 37.26           C  
-ATOM   2270  NH1 ARG A 316      78.207  34.592 -12.754  1.00 38.63           N  
-ATOM   2271  NH2 ARG A 316      78.318  35.509 -10.656  1.00 37.50           N  
-ATOM   2272  N   ALA A 317      81.683  35.986 -18.120  1.00 26.16           N  
-ATOM   2273  CA  ALA A 317      81.109  35.274 -19.247  1.00 25.75           C  
-ATOM   2274  C   ALA A 317      82.073  34.234 -19.790  1.00 25.51           C  
-ATOM   2275  O   ALA A 317      81.721  33.059 -19.910  1.00 25.43           O  
-ATOM   2276  CB  ALA A 317      80.723  36.252 -20.343  1.00 25.32           C  
-ATOM   2277  N   ASP A 318      83.300  34.656 -20.082  1.00 25.76           N  
-ATOM   2278  CA  ASP A 318      84.302  33.744 -20.626  1.00 25.21           C  
-ATOM   2279  C   ASP A 318      84.667  32.633 -19.649  1.00 24.39           C  
-ATOM   2280  O   ASP A 318      84.963  31.509 -20.065  1.00 24.41           O  
-ATOM   2281  CB  ASP A 318      85.555  34.498 -21.068  1.00 26.29           C  
-ATOM   2282  CG  ASP A 318      86.546  33.598 -21.792  1.00 29.12           C  
-ATOM   2283  OD1 ASP A 318      86.287  33.226 -22.958  1.00 30.05           O  
-ATOM   2284  OD2 ASP A 318      87.581  33.244 -21.191  1.00 31.22           O  
-ATOM   2285  N   TRP A 319      84.639  32.942 -18.354  1.00 23.07           N  
-ATOM   2286  CA  TRP A 319      84.951  31.958 -17.326  1.00 22.04           C  
-ATOM   2287  C   TRP A 319      83.885  30.855 -17.285  1.00 22.00           C  
-ATOM   2288  O   TRP A 319      84.209  29.666 -17.309  1.00 21.46           O  
-ATOM   2289  CB  TRP A 319      85.090  32.625 -15.951  1.00 21.40           C  
-ATOM   2290  CG  TRP A 319      85.142  31.632 -14.813  1.00 20.67           C  
-ATOM   2291  CD1 TRP A 319      86.090  30.668 -14.601  1.00 20.12           C  
-ATOM   2292  CD2 TRP A 319      84.169  31.470 -13.777  1.00 19.43           C  
-ATOM   2293  NE1 TRP A 319      85.760  29.912 -13.504  1.00 19.53           N  
-ATOM   2294  CE2 TRP A 319      84.586  30.384 -12.975  1.00 19.51           C  
-ATOM   2295  CE3 TRP A 319      82.983  32.135 -13.446  1.00 19.68           C  
-ATOM   2296  CZ2 TRP A 319      83.859  29.947 -11.868  1.00 19.80           C  
-ATOM   2297  CZ3 TRP A 319      82.256  31.699 -12.341  1.00 19.52           C  
-ATOM   2298  CH2 TRP A 319      82.701  30.616 -11.565  1.00 19.90           C  
-ATOM   2299  N   MET A 320      82.618  31.252 -17.242  1.00 22.03           N  
-ATOM   2300  CA  MET A 320      81.523  30.288 -17.209  1.00 22.52           C  
-ATOM   2301  C   MET A 320      81.557  29.405 -18.452  1.00 21.06           C  
-ATOM   2302  O   MET A 320      81.257  28.216 -18.390  1.00 20.86           O  
-ATOM   2303  CB  MET A 320      80.172  31.004 -17.099  1.00 24.42           C  
-ATOM   2304  CG  MET A 320      80.011  31.839 -15.838  1.00 27.18           C  
-ATOM   2305  SD  MET A 320      78.412  32.679 -15.732  1.00 30.59           S  
-ATOM   2306  CE  MET A 320      77.731  31.921 -14.291  1.00 30.56           C  
-ATOM   2307  N   ALA A 321      81.955  29.987 -19.575  1.00 20.09           N  
-ATOM   2308  CA  ALA A 321      82.040  29.248 -20.825  1.00 19.96           C  
-ATOM   2309  C   ALA A 321      83.150  28.201 -20.780  1.00 20.34           C  
-ATOM   2310  O   ALA A 321      82.992  27.091 -21.298  1.00 20.12           O  
-ATOM   2311  CB  ALA A 321      82.269  30.200 -21.984  1.00 19.46           C  
-ATOM   2312  N   GLU A 322      84.286  28.558 -20.195  1.00 20.19           N  
-ATOM   2313  CA  GLU A 322      85.390  27.617 -20.114  1.00 20.08           C  
-ATOM   2314  C   GLU A 322      85.092  26.510 -19.102  1.00 19.56           C  
-ATOM   2315  O   GLU A 322      85.413  25.344 -19.339  1.00 18.80           O  
-ATOM   2316  CB  GLU A 322      86.698  28.335 -19.774  1.00 20.27           C  
-ATOM   2317  CG  GLU A 322      87.924  27.471 -20.022  1.00 22.12           C  
-ATOM   2318  CD  GLU A 322      89.237  28.205 -19.840  1.00 22.22           C  
-ATOM   2319  OE1 GLU A 322      89.229  29.433 -19.650  1.00 24.35           O  
-ATOM   2320  OE2 GLU A 322      90.290  27.545 -19.894  1.00 23.75           O  
-ATOM   2321  N   LEU A 323      84.459  26.866 -17.988  1.00 19.66           N  
-ATOM   2322  CA  LEU A 323      84.119  25.878 -16.971  1.00 19.97           C  
-ATOM   2323  C   LEU A 323      83.115  24.889 -17.572  1.00 21.46           C  
-ATOM   2324  O   LEU A 323      83.270  23.672 -17.419  1.00 21.29           O  
-ATOM   2325  CB  LEU A 323      83.517  26.548 -15.734  1.00 19.03           C  
-ATOM   2326  CG  LEU A 323      84.037  26.155 -14.345  1.00 18.91           C  
-ATOM   2327  CD1 LEU A 323      83.011  26.569 -13.313  1.00 18.18           C  
-ATOM   2328  CD2 LEU A 323      84.309  24.665 -14.231  1.00 19.11           C  
-ATOM   2329  N   GLU A 324      82.115  25.411 -18.287  1.00 22.26           N  
-ATOM   2330  CA  GLU A 324      81.105  24.574 -18.927  1.00 23.42           C  
-ATOM   2331  C   GLU A 324      81.710  23.571 -19.901  1.00 22.91           C  
-ATOM   2332  O   GLU A 324      81.277  22.422 -19.962  1.00 22.35           O  
-ATOM   2333  CB  GLU A 324      80.068  25.420 -19.659  1.00 26.06           C  
-ATOM   2334  CG  GLU A 324      78.666  25.317 -19.070  1.00 30.52           C  
-ATOM   2335  CD  GLU A 324      78.274  23.889 -18.711  1.00 32.92           C  
-ATOM   2336  OE1 GLU A 324      77.776  23.152 -19.596  1.00 34.59           O  
-ATOM   2337  OE2 GLU A 324      78.469  23.503 -17.535  1.00 33.88           O  
-ATOM   2338  N   ALA A 325      82.694  24.024 -20.673  1.00 22.47           N  
-ATOM   2339  CA  ALA A 325      83.389  23.179 -21.638  1.00 22.16           C  
-ATOM   2340  C   ALA A 325      84.087  22.043 -20.894  1.00 22.65           C  
-ATOM   2341  O   ALA A 325      84.097  20.892 -21.349  1.00 22.81           O  
-ATOM   2342  CB  ALA A 325      84.414  24.000 -22.415  1.00 21.50           C  
-ATOM   2343  N   VAL A 326      84.673  22.383 -19.749  1.00 22.71           N  
-ATOM   2344  CA  VAL A 326      85.372  21.417 -18.906  1.00 22.93           C  
-ATOM   2345  C   VAL A 326      84.406  20.364 -18.356  1.00 22.86           C  
-ATOM   2346  O   VAL A 326      84.641  19.163 -18.499  1.00 23.06           O  
-ATOM   2347  CB  VAL A 326      86.117  22.135 -17.742  1.00 22.64           C  
-ATOM   2348  CG1 VAL A 326      86.591  21.131 -16.697  1.00 22.44           C  
-ATOM   2349  CG2 VAL A 326      87.303  22.916 -18.293  1.00 20.59           C  
-ATOM   2350  N   ARG A 327      83.304  20.823 -17.770  1.00 23.35           N  
-ATOM   2351  CA  ARG A 327      82.291  19.942 -17.199  1.00 23.78           C  
-ATOM   2352  C   ARG A 327      81.748  18.991 -18.271  1.00 24.27           C  
-ATOM   2353  O   ARG A 327      81.712  17.772 -18.071  1.00 24.35           O  
-ATOM   2354  CB  ARG A 327      81.155  20.777 -16.601  1.00 24.44           C  
-ATOM   2355  CG  ARG A 327      80.191  19.989 -15.724  1.00 26.62           C  
-ATOM   2356  CD  ARG A 327      78.905  20.774 -15.436  1.00 27.46           C  
-ATOM   2357  NE  ARG A 327      78.066  20.910 -16.626  1.00 27.20           N  
-ATOM   2358  CZ  ARG A 327      77.406  19.911 -17.208  1.00 27.27           C  
-ATOM   2359  NH1 ARG A 327      77.420  18.691 -16.682  1.00 26.20           N  
-ATOM   2360  NH2 ARG A 327      76.690  20.146 -18.299  1.00 26.96           N  
-ATOM   2361  N   SER A 328      81.359  19.548 -19.415  1.00 24.13           N  
-ATOM   2362  CA  SER A 328      80.832  18.766 -20.533  1.00 24.88           C  
-ATOM   2363  C   SER A 328      81.849  17.750 -21.034  1.00 24.58           C  
-ATOM   2364  O   SER A 328      81.495  16.620 -21.377  1.00 24.73           O  
-ATOM   2365  CB  SER A 328      80.444  19.688 -21.687  1.00 25.77           C  
-ATOM   2366  OG  SER A 328      79.453  20.609 -21.278  1.00 30.37           O  
-ATOM   2367  N   GLY A 329      83.111  18.168 -21.098  1.00 24.46           N  
-ATOM   2368  CA  GLY A 329      84.166  17.280 -21.553  1.00 23.79           C  
-ATOM   2369  C   GLY A 329      84.314  16.068 -20.653  1.00 23.18           C  
-ATOM   2370  O   GLY A 329      84.427  14.945 -21.137  1.00 23.50           O  
-ATOM   2371  N   MET A 330      84.295  16.286 -19.341  1.00 23.17           N  
-ATOM   2372  CA  MET A 330      84.426  15.182 -18.398  1.00 22.95           C  
-ATOM   2373  C   MET A 330      83.204  14.277 -18.455  1.00 23.27           C  
-ATOM   2374  O   MET A 330      83.329  13.053 -18.404  1.00 23.22           O  
-ATOM   2375  CB  MET A 330      84.632  15.692 -16.975  1.00 22.53           C  
-ATOM   2376  CG  MET A 330      85.936  16.434 -16.770  1.00 23.52           C  
-ATOM   2377  SD  MET A 330      86.377  16.521 -15.032  1.00 24.38           S  
-ATOM   2378  CE  MET A 330      84.839  17.136 -14.319  1.00 26.11           C  
-ATOM   2379  N   LEU A 331      82.031  14.882 -18.606  1.00 23.93           N  
-ATOM   2380  CA  LEU A 331      80.779  14.137 -18.687  1.00 24.80           C  
-ATOM   2381  C   LEU A 331      80.774  13.203 -19.899  1.00 24.73           C  
-ATOM   2382  O   LEU A 331      80.236  12.100 -19.837  1.00 24.58           O  
-ATOM   2383  CB  LEU A 331      79.596  15.105 -18.751  1.00 26.18           C  
-ATOM   2384  CG  LEU A 331      78.206  14.500 -18.568  1.00 27.57           C  
-ATOM   2385  CD1 LEU A 331      78.130  13.767 -17.235  1.00 28.22           C  
-ATOM   2386  CD2 LEU A 331      77.159  15.599 -18.631  1.00 28.33           C  
-ATOM   2387  N   ARG A 332      81.383  13.637 -20.997  1.00 25.45           N  
-ATOM   2388  CA  ARG A 332      81.457  12.807 -22.194  1.00 26.81           C  
-ATOM   2389  C   ARG A 332      82.450  11.660 -21.986  1.00 26.18           C  
-ATOM   2390  O   ARG A 332      82.255  10.553 -22.496  1.00 26.49           O  
-ATOM   2391  CB  ARG A 332      81.825  13.651 -23.414  1.00 28.85           C  
-ATOM   2392  CG  ARG A 332      80.684  14.550 -23.856  1.00 34.38           C  
-ATOM   2393  CD  ARG A 332      81.098  15.528 -24.941  1.00 38.72           C  
-ATOM   2394  NE  ARG A 332      79.970  16.363 -25.352  1.00 42.90           N  
-ATOM   2395  CZ  ARG A 332      79.994  17.205 -26.382  1.00 45.57           C  
-ATOM   2396  NH1 ARG A 332      81.094  17.333 -27.112  1.00 46.57           N  
-ATOM   2397  NH2 ARG A 332      78.915  17.923 -26.682  1.00 46.60           N  
-ATOM   2398  N   LEU A 333      83.504  11.920 -21.222  1.00 24.77           N  
-ATOM   2399  CA  LEU A 333      84.486  10.888 -20.920  1.00 23.79           C  
-ATOM   2400  C   LEU A 333      83.781   9.795 -20.125  1.00 22.95           C  
-ATOM   2401  O   LEU A 333      84.006   8.607 -20.357  1.00 23.17           O  
-ATOM   2402  CB  LEU A 333      85.639  11.479 -20.111  1.00 23.78           C  
-ATOM   2403  CG  LEU A 333      86.937  11.840 -20.842  1.00 24.70           C  
-ATOM   2404  CD1 LEU A 333      86.686  12.221 -22.287  1.00 25.10           C  
-ATOM   2405  CD2 LEU A 333      87.642  12.956 -20.088  1.00 24.25           C  
-ATOM   2406  N   ARG A 334      82.911  10.202 -19.202  1.00 22.78           N  
-ATOM   2407  CA  ARG A 334      82.148   9.260 -18.382  1.00 23.10           C  
-ATOM   2408  C   ARG A 334      81.251   8.390 -19.253  1.00 24.55           C  
-ATOM   2409  O   ARG A 334      81.224   7.167 -19.106  1.00 24.02           O  
-ATOM   2410  CB  ARG A 334      81.289   9.998 -17.357  1.00 21.02           C  
-ATOM   2411  CG  ARG A 334      82.058  10.516 -16.159  1.00 20.00           C  
-ATOM   2412  CD  ARG A 334      81.123  11.142 -15.133  1.00 19.09           C  
-ATOM   2413  NE  ARG A 334      81.834  11.571 -13.934  1.00 17.66           N  
-ATOM   2414  CZ  ARG A 334      82.355  10.745 -13.032  1.00 17.60           C  
-ATOM   2415  NH1 ARG A 334      82.245   9.433 -13.175  1.00 16.77           N  
-ATOM   2416  NH2 ARG A 334      82.986  11.234 -11.975  1.00 18.79           N  
-ATOM   2417  N   GLU A 335      80.519   9.032 -20.159  1.00 26.73           N  
-ATOM   2418  CA  GLU A 335      79.619   8.329 -21.069  1.00 28.76           C  
-ATOM   2419  C   GLU A 335      80.374   7.301 -21.912  1.00 27.92           C  
-ATOM   2420  O   GLU A 335      79.927   6.164 -22.059  1.00 28.42           O  
-ATOM   2421  CB  GLU A 335      78.903   9.328 -21.978  1.00 31.30           C  
-ATOM   2422  CG  GLU A 335      77.992  10.298 -21.234  1.00 37.19           C  
-ATOM   2423  CD  GLU A 335      77.454  11.408 -22.128  1.00 41.05           C  
-ATOM   2424  OE1 GLU A 335      77.087  11.119 -23.291  1.00 43.82           O  
-ATOM   2425  OE2 GLU A 335      77.405  12.574 -21.671  1.00 43.39           O  
-ATOM   2426  N   GLN A 336      81.527   7.696 -22.443  1.00 27.13           N  
-ATOM   2427  CA  GLN A 336      82.339   6.802 -23.264  1.00 26.68           C  
-ATOM   2428  C   GLN A 336      82.805   5.581 -22.490  1.00 25.14           C  
-ATOM   2429  O   GLN A 336      82.624   4.450 -22.943  1.00 24.90           O  
-ATOM   2430  CB  GLN A 336      83.549   7.534 -23.832  1.00 27.72           C  
-ATOM   2431  CG  GLN A 336      83.224   8.431 -24.997  1.00 31.95           C  
-ATOM   2432  CD  GLN A 336      84.453   9.111 -25.555  1.00 34.56           C  
-ATOM   2433  OE1 GLN A 336      85.381   8.451 -26.029  1.00 36.96           O  
-ATOM   2434  NE2 GLN A 336      84.478  10.436 -25.485  1.00 36.07           N  
-ATOM   2435  N   LEU A 337      83.414   5.814 -21.331  1.00 23.66           N  
-ATOM   2436  CA  LEU A 337      83.900   4.727 -20.492  1.00 22.91           C  
-ATOM   2437  C   LEU A 337      82.764   3.770 -20.148  1.00 23.25           C  
-ATOM   2438  O   LEU A 337      82.918   2.552 -20.269  1.00 23.64           O  
-ATOM   2439  CB  LEU A 337      84.533   5.269 -19.208  1.00 21.26           C  
-ATOM   2440  CG  LEU A 337      84.991   4.213 -18.199  1.00 19.55           C  
-ATOM   2441  CD1 LEU A 337      86.030   3.285 -18.816  1.00 18.28           C  
-ATOM   2442  CD2 LEU A 337      85.552   4.910 -16.971  1.00 20.26           C  
-ATOM   2443  N   ALA A 338      81.620   4.319 -19.745  1.00 21.80           N  
-ATOM   2444  CA  ALA A 338      80.469   3.499 -19.394  1.00 21.54           C  
-ATOM   2445  C   ALA A 338      80.023   2.643 -20.585  1.00 21.16           C  
-ATOM   2446  O   ALA A 338      79.703   1.465 -20.425  1.00 20.76           O  
-ATOM   2447  CB  ALA A 338      79.323   4.378 -18.903  1.00 21.84           C  
-ATOM   2448  N   GLY A 339      80.030   3.233 -21.778  1.00 21.59           N  
-ATOM   2449  CA  GLY A 339      79.634   2.503 -22.972  1.00 21.80           C  
-ATOM   2450  C   GLY A 339      80.609   1.386 -23.268  1.00 23.19           C  
-ATOM   2451  O   GLY A 339      80.213   0.250 -23.530  1.00 23.78           O  
-ATOM   2452  N   GLU A 340      81.897   1.706 -23.193  1.00 24.24           N  
-ATOM   2453  CA  GLU A 340      82.965   0.741 -23.438  1.00 24.75           C  
-ATOM   2454  C   GLU A 340      82.805  -0.431 -22.470  1.00 24.48           C  
-ATOM   2455  O   GLU A 340      82.861  -1.593 -22.866  1.00 24.34           O  
-ATOM   2456  CB  GLU A 340      84.325   1.420 -23.231  1.00 25.92           C  
-ATOM   2457  CG  GLU A 340      85.547   0.573 -23.578  1.00 28.03           C  
-ATOM   2458  CD  GLU A 340      85.867   0.525 -25.067  1.00 29.61           C  
-ATOM   2459  OE1 GLU A 340      85.178   1.198 -25.867  1.00 30.35           O  
-ATOM   2460  OE2 GLU A 340      86.826  -0.188 -25.433  1.00 30.18           O  
-ATOM   2461  N   LEU A 341      82.581  -0.113 -21.202  1.00 24.73           N  
-ATOM   2462  CA  LEU A 341      82.395  -1.127 -20.176  1.00 25.86           C  
-ATOM   2463  C   LEU A 341      81.126  -1.940 -20.410  1.00 27.69           C  
-ATOM   2464  O   LEU A 341      81.067  -3.110 -20.053  1.00 27.74           O  
-ATOM   2465  CB  LEU A 341      82.355  -0.482 -18.790  1.00 23.57           C  
-ATOM   2466  CG  LEU A 341      83.713  -0.132 -18.193  1.00 22.53           C  
-ATOM   2467  CD1 LEU A 341      83.556   0.656 -16.905  1.00 21.90           C  
-ATOM   2468  CD2 LEU A 341      84.458  -1.407 -17.937  1.00 22.43           C  
-ATOM   2469  N   ARG A 342      80.115  -1.312 -21.001  1.00 30.12           N  
-ATOM   2470  CA  ARG A 342      78.852  -1.977 -21.290  1.00 32.49           C  
-ATOM   2471  C   ARG A 342      79.083  -3.007 -22.391  1.00 32.69           C  
-ATOM   2472  O   ARG A 342      78.654  -4.157 -22.281  1.00 32.21           O  
-ATOM   2473  CB  ARG A 342      77.818  -0.947 -21.741  1.00 35.81           C  
-ATOM   2474  CG  ARG A 342      76.408  -1.479 -21.933  1.00 40.75           C  
-ATOM   2475  CD  ARG A 342      75.488  -0.364 -22.427  1.00 45.66           C  
-ATOM   2476  NE  ARG A 342      75.530   0.804 -21.545  1.00 49.71           N  
-ATOM   2477  CZ  ARG A 342      75.156   2.035 -21.892  1.00 51.21           C  
-ATOM   2478  NH1 ARG A 342      74.702   2.286 -23.116  1.00 52.13           N  
-ATOM   2479  NH2 ARG A 342      75.241   3.020 -21.006  1.00 51.57           N  
-ATOM   2480  N   ASP A 343      79.794  -2.590 -23.436  1.00 32.73           N  
-ATOM   2481  CA  ASP A 343      80.106  -3.459 -24.563  1.00 32.90           C  
-ATOM   2482  C   ASP A 343      80.963  -4.650 -24.145  1.00 33.01           C  
-ATOM   2483  O   ASP A 343      80.735  -5.769 -24.599  1.00 33.20           O  
-ATOM   2484  CB  ASP A 343      80.812  -2.670 -25.669  1.00 33.94           C  
-ATOM   2485  CG  ASP A 343      79.879  -1.717 -26.408  1.00 35.24           C  
-ATOM   2486  OD1 ASP A 343      78.675  -1.646 -26.068  1.00 36.89           O  
-ATOM   2487  OD2 ASP A 343      80.352  -1.037 -27.342  1.00 35.78           O  
-ATOM   2488  N   LEU A 344      81.940  -4.404 -23.280  1.00 32.94           N  
-ATOM   2489  CA  LEU A 344      82.837  -5.449 -22.795  1.00 33.52           C  
-ATOM   2490  C   LEU A 344      82.215  -6.376 -21.753  1.00 33.92           C  
-ATOM   2491  O   LEU A 344      82.416  -7.588 -21.800  1.00 34.28           O  
-ATOM   2492  CB  LEU A 344      84.113  -4.830 -22.215  1.00 33.73           C  
-ATOM   2493  CG  LEU A 344      85.294  -4.505 -23.137  1.00 34.50           C  
-ATOM   2494  CD1 LEU A 344      86.098  -5.761 -23.443  1.00 35.03           C  
-ATOM   2495  CD2 LEU A 344      84.812  -3.844 -24.413  1.00 35.19           C  
-ATOM   2496  N   SER A 345      81.470  -5.809 -20.811  1.00 33.88           N  
-ATOM   2497  CA  SER A 345      80.856  -6.592 -19.747  1.00 34.21           C  
-ATOM   2498  C   SER A 345      79.626  -7.360 -20.197  1.00 35.22           C  
-ATOM   2499  O   SER A 345      79.293  -8.404 -19.628  1.00 35.86           O  
-ATOM   2500  CB  SER A 345      80.471  -5.684 -18.580  1.00 33.55           C  
-ATOM   2501  OG  SER A 345      79.449  -4.785 -18.969  1.00 33.93           O  
-ATOM   2502  N   GLY A 346      78.942  -6.836 -21.206  1.00 35.60           N  
-ATOM   2503  CA  GLY A 346      77.737  -7.487 -21.675  1.00 35.98           C  
-ATOM   2504  C   GLY A 346      76.640  -7.238 -20.655  1.00 36.55           C  
-ATOM   2505  O   GLY A 346      75.640  -7.956 -20.604  1.00 37.07           O  
-ATOM   2506  N   SER A 347      76.840  -6.217 -19.830  1.00 36.51           N  
-ATOM   2507  CA  SER A 347      75.875  -5.857 -18.812  1.00 36.86           C  
-ATOM   2508  C   SER A 347      75.944  -4.356 -18.585  1.00 37.05           C  
-ATOM   2509  O   SER A 347      76.745  -3.658 -19.204  1.00 36.88           O  
-ATOM   2510  CB  SER A 347      76.160  -6.612 -17.508  1.00 37.49           C  
-ATOM   2511  OG  SER A 347      77.344  -6.155 -16.870  1.00 38.25           O  
-ATOM   2512  N   ASP A 348      75.074  -3.854 -17.722  1.00 37.77           N  
-ATOM   2513  CA  ASP A 348      75.055  -2.435 -17.418  1.00 38.27           C  
-ATOM   2514  C   ASP A 348      75.452  -2.198 -15.962  1.00 36.85           C  
-ATOM   2515  O   ASP A 348      75.081  -1.190 -15.357  1.00 37.12           O  
-ATOM   2516  CB  ASP A 348      73.682  -1.833 -17.753  1.00 41.08           C  
-ATOM   2517  CG  ASP A 348      73.466  -1.669 -19.263  1.00 43.22           C  
-ATOM   2518  OD1 ASP A 348      73.404  -2.689 -19.987  1.00 44.73           O  
-ATOM   2519  OD2 ASP A 348      73.368  -0.513 -19.730  1.00 44.94           O  
-ATOM   2520  N   ARG A 349      76.268  -3.111 -15.436  1.00 35.19           N  
-ATOM   2521  CA  ARG A 349      76.757  -3.049 -14.059  1.00 33.52           C  
-ATOM   2522  C   ARG A 349      77.540  -1.784 -13.750  1.00 30.99           C  
-ATOM   2523  O   ARG A 349      77.403  -1.213 -12.674  1.00 31.13           O  
-ATOM   2524  CB  ARG A 349      77.676  -4.229 -13.761  1.00 35.26           C  
-ATOM   2525  CG  ARG A 349      76.995  -5.561 -13.632  1.00 37.23           C  
-ATOM   2526  CD  ARG A 349      77.955  -6.561 -13.027  1.00 38.07           C  
-ATOM   2527  NE  ARG A 349      79.141  -6.751 -13.857  1.00 38.35           N  
-ATOM   2528  CZ  ARG A 349      80.389  -6.585 -13.427  1.00 39.50           C  
-ATOM   2529  NH1 ARG A 349      80.628  -6.198 -12.177  1.00 39.08           N  
-ATOM   2530  NH2 ARG A 349      81.402  -6.789 -14.256  1.00 39.89           N  
-ATOM   2531  N   PHE A 350      78.401  -1.389 -14.678  1.00 28.10           N  
-ATOM   2532  CA  PHE A 350      79.236  -0.207 -14.517  1.00 25.34           C  
-ATOM   2533  C   PHE A 350      78.545   1.099 -14.884  1.00 24.08           C  
-ATOM   2534  O   PHE A 350      79.185   2.148 -14.961  1.00 24.20           O  
-ATOM   2535  CB  PHE A 350      80.518  -0.377 -15.328  1.00 24.87           C  
-ATOM   2536  CG  PHE A 350      81.342  -1.556 -14.901  1.00 25.02           C  
-ATOM   2537  CD1 PHE A 350      82.211  -1.457 -13.814  1.00 24.74           C  
-ATOM   2538  CD2 PHE A 350      81.228  -2.777 -15.559  1.00 24.46           C  
-ATOM   2539  CE1 PHE A 350      82.949  -2.559 -13.386  1.00 24.14           C  
-ATOM   2540  CE2 PHE A 350      81.964  -3.884 -15.138  1.00 24.37           C  
-ATOM   2541  CZ  PHE A 350      82.825  -3.772 -14.049  1.00 23.93           C  
-ATOM   2542  N   GLY A 351      77.229   1.047 -15.050  1.00 23.01           N  
-ATOM   2543  CA  GLY A 351      76.478   2.235 -15.407  1.00 21.04           C  
-ATOM   2544  C   GLY A 351      76.665   3.390 -14.445  1.00 20.18           C  
-ATOM   2545  O   GLY A 351      76.495   4.547 -14.828  1.00 20.82           O  
-ATOM   2546  N   PHE A 352      77.031   3.086 -13.204  1.00 19.42           N  
-ATOM   2547  CA  PHE A 352      77.241   4.112 -12.192  1.00 19.02           C  
-ATOM   2548  C   PHE A 352      78.285   5.140 -12.610  1.00 19.99           C  
-ATOM   2549  O   PHE A 352      78.235   6.294 -12.172  1.00 19.99           O  
-ATOM   2550  CB  PHE A 352      77.617   3.484 -10.842  1.00 18.64           C  
-ATOM   2551  CG  PHE A 352      78.900   2.705 -10.861  1.00 18.89           C  
-ATOM   2552  CD1 PHE A 352      80.124   3.348 -10.691  1.00 18.69           C  
-ATOM   2553  CD2 PHE A 352      78.886   1.327 -11.042  1.00 18.45           C  
-ATOM   2554  CE1 PHE A 352      81.315   2.630 -10.704  1.00 19.63           C  
-ATOM   2555  CE2 PHE A 352      80.070   0.596 -11.058  1.00 19.20           C  
-ATOM   2556  CZ  PHE A 352      81.290   1.250 -10.888  1.00 19.79           C  
-ATOM   2557  N   VAL A 353      79.223   4.729 -13.460  1.00 20.45           N  
-ATOM   2558  CA  VAL A 353      80.269   5.636 -13.931  1.00 21.97           C  
-ATOM   2559  C   VAL A 353      79.656   6.861 -14.615  1.00 21.74           C  
-ATOM   2560  O   VAL A 353      80.145   7.979 -14.451  1.00 21.59           O  
-ATOM   2561  CB  VAL A 353      81.244   4.941 -14.927  1.00 22.03           C  
-ATOM   2562  CG1 VAL A 353      82.344   5.910 -15.340  1.00 23.08           C  
-ATOM   2563  CG2 VAL A 353      81.852   3.697 -14.299  1.00 22.30           C  
-ATOM   2564  N   ALA A 354      78.572   6.643 -15.357  1.00 21.69           N  
-ATOM   2565  CA  ALA A 354      77.893   7.720 -16.070  1.00 21.79           C  
-ATOM   2566  C   ALA A 354      76.933   8.487 -15.167  1.00 22.46           C  
-ATOM   2567  O   ALA A 354      76.441   9.554 -15.534  1.00 22.39           O  
-ATOM   2568  CB  ALA A 354      77.157   7.168 -17.277  1.00 21.65           C  
-ATOM   2569  N   GLU A 355      76.661   7.935 -13.991  1.00 23.19           N  
-ATOM   2570  CA  GLU A 355      75.762   8.577 -13.045  1.00 23.97           C  
-ATOM   2571  C   GLU A 355      76.533   9.444 -12.058  1.00 23.23           C  
-ATOM   2572  O   GLU A 355      76.003  10.438 -11.554  1.00 22.77           O  
-ATOM   2573  CB  GLU A 355      74.935   7.532 -12.297  1.00 26.58           C  
-ATOM   2574  CG  GLU A 355      74.069   6.684 -13.211  1.00 31.24           C  
-ATOM   2575  CD  GLU A 355      73.188   5.719 -12.448  1.00 34.53           C  
-ATOM   2576  OE1 GLU A 355      73.728   4.879 -11.695  1.00 36.78           O  
-ATOM   2577  OE2 GLU A 355      71.952   5.802 -12.599  1.00 36.87           O  
-ATOM   2578  N   HIS A 356      77.774   9.056 -11.773  1.00 21.27           N  
-ATOM   2579  CA  HIS A 356      78.624   9.805 -10.853  1.00 19.33           C  
-ATOM   2580  C   HIS A 356      78.897  11.196 -11.402  1.00 18.63           C  
-ATOM   2581  O   HIS A 356      78.881  11.405 -12.615  1.00 18.61           O  
-ATOM   2582  CB  HIS A 356      79.955   9.083 -10.645  1.00 18.55           C  
-ATOM   2583  CG  HIS A 356      79.876   7.922  -9.707  1.00 17.74           C  
-ATOM   2584  ND1 HIS A 356      80.992   7.239  -9.274  1.00 16.93           N  
-ATOM   2585  CD2 HIS A 356      78.819   7.340  -9.093  1.00 17.88           C  
-ATOM   2586  CE1 HIS A 356      80.628   6.290  -8.435  1.00 17.27           C  
-ATOM   2587  NE2 HIS A 356      79.313   6.328  -8.308  1.00 17.55           N  
-ATOM   2588  N   ARG A 357      79.136  12.146 -10.506  1.00 18.18           N  
-ATOM   2589  CA  ARG A 357      79.430  13.515 -10.907  1.00 18.00           C  
-ATOM   2590  C   ARG A 357      80.691  14.002 -10.202  1.00 18.00           C  
-ATOM   2591  O   ARG A 357      80.916  13.697  -9.024  1.00 17.10           O  
-ATOM   2592  CB  ARG A 357      78.250  14.444 -10.598  1.00 17.71           C  
-ATOM   2593  CG  ARG A 357      77.026  14.218 -11.480  1.00 18.52           C  
-ATOM   2594  CD  ARG A 357      77.359  14.435 -12.945  1.00 20.33           C  
-ATOM   2595  NE  ARG A 357      76.193  14.306 -13.818  1.00 21.53           N  
-ATOM   2596  CZ  ARG A 357      75.809  13.177 -14.406  1.00 21.94           C  
-ATOM   2597  NH1 ARG A 357      76.477  12.049 -14.214  1.00 22.10           N  
-ATOM   2598  NH2 ARG A 357      74.742  13.173 -15.186  1.00 22.93           N  
-ATOM   2599  N   GLY A 358      81.497  14.765 -10.931  1.00 17.99           N  
-ATOM   2600  CA  GLY A 358      82.739  15.295 -10.398  1.00 18.60           C  
-ATOM   2601  C   GLY A 358      83.875  14.702 -11.207  1.00 19.38           C  
-ATOM   2602  O   GLY A 358      83.627  13.978 -12.175  1.00 19.81           O  
-ATOM   2603  N   MET A 359      85.116  15.018 -10.864  1.00 19.50           N  
-ATOM   2604  CA  MET A 359      86.219  14.447 -11.623  1.00 20.38           C  
-ATOM   2605  C   MET A 359      86.718  13.136 -11.034  1.00 18.89           C  
-ATOM   2606  O   MET A 359      87.571  12.481 -11.618  1.00 19.85           O  
-ATOM   2607  CB  MET A 359      87.368  15.450 -11.834  1.00 21.16           C  
-ATOM   2608  CG  MET A 359      88.089  15.935 -10.596  1.00 21.64           C  
-ATOM   2609  SD  MET A 359      89.567  16.894 -11.076  1.00 23.14           S  
-ATOM   2610  CE  MET A 359      88.847  18.481 -11.439  1.00 20.81           C  
-ATOM   2611  N   PHE A 360      86.139  12.723  -9.915  1.00 17.77           N  
-ATOM   2612  CA  PHE A 360      86.542  11.485  -9.268  1.00 17.60           C  
-ATOM   2613  C   PHE A 360      85.454  10.430  -9.276  1.00 17.98           C  
-ATOM   2614  O   PHE A 360      84.264  10.734  -9.397  1.00 18.48           O  
-ATOM   2615  CB  PHE A 360      86.954  11.745  -7.818  1.00 17.24           C  
-ATOM   2616  CG  PHE A 360      88.127  12.668  -7.678  1.00 18.61           C  
-ATOM   2617  CD1 PHE A 360      89.349  12.355  -8.267  1.00 18.09           C  
-ATOM   2618  CD2 PHE A 360      88.011  13.859  -6.970  1.00 18.13           C  
-ATOM   2619  CE1 PHE A 360      90.432  13.211  -8.154  1.00 18.35           C  
-ATOM   2620  CE2 PHE A 360      89.088  14.719  -6.851  1.00 18.64           C  
-ATOM   2621  CZ  PHE A 360      90.302  14.396  -7.445  1.00 19.24           C  
-ATOM   2622  N   SER A 361      85.881   9.185  -9.131  1.00 18.18           N  
-ATOM   2623  CA  SER A 361      84.975   8.056  -9.066  1.00 18.46           C  
-ATOM   2624  C   SER A 361      85.673   6.905  -8.382  1.00 18.43           C  
-ATOM   2625  O   SER A 361      86.878   6.709  -8.550  1.00 17.93           O  
-ATOM   2626  CB  SER A 361      84.535   7.619 -10.463  1.00 18.85           C  
-ATOM   2627  OG  SER A 361      83.201   8.017 -10.730  1.00 19.66           O  
-ATOM   2628  N   ARG A 362      84.938   6.218  -7.523  1.00 18.85           N  
-ATOM   2629  CA  ARG A 362      85.460   5.040  -6.855  1.00 19.02           C  
-ATOM   2630  C   ARG A 362      84.884   3.887  -7.659  1.00 19.29           C  
-ATOM   2631  O   ARG A 362      83.662   3.788  -7.815  1.00 19.40           O  
-ATOM   2632  CB  ARG A 362      84.971   4.943  -5.416  1.00 19.36           C  
-ATOM   2633  CG  ARG A 362      86.022   5.303  -4.399  1.00 22.00           C  
-ATOM   2634  CD  ARG A 362      85.860   4.480  -3.142  1.00 22.88           C  
-ATOM   2635  NE  ARG A 362      86.763   4.934  -2.093  1.00 24.92           N  
-ATOM   2636  CZ  ARG A 362      86.644   4.610  -0.808  1.00 25.21           C  
-ATOM   2637  NH1 ARG A 362      85.652   3.824  -0.407  1.00 24.90           N  
-ATOM   2638  NH2 ARG A 362      87.516   5.078   0.077  1.00 24.41           N  
-ATOM   2639  N   LEU A 363      85.757   3.052  -8.212  1.00 18.61           N  
-ATOM   2640  CA  LEU A 363      85.328   1.909  -9.009  1.00 18.13           C  
-ATOM   2641  C   LEU A 363      84.767   0.767  -8.163  1.00 17.99           C  
-ATOM   2642  O   LEU A 363      84.040  -0.082  -8.666  1.00 18.39           O  
-ATOM   2643  CB  LEU A 363      86.498   1.390  -9.837  1.00 17.67           C  
-ATOM   2644  CG  LEU A 363      87.075   2.349 -10.863  1.00 17.54           C  
-ATOM   2645  CD1 LEU A 363      88.365   1.771 -11.410  1.00 17.65           C  
-ATOM   2646  CD2 LEU A 363      86.052   2.583 -11.967  1.00 17.71           C  
-ATOM   2647  N   GLY A 364      85.146   0.722  -6.892  1.00 18.59           N  
-ATOM   2648  CA  GLY A 364      84.675  -0.341  -6.026  1.00 19.49           C  
-ATOM   2649  C   GLY A 364      85.600  -1.549  -6.067  1.00 20.54           C  
-ATOM   2650  O   GLY A 364      85.209  -2.641  -5.676  1.00 21.70           O  
-ATOM   2651  N   ALA A 365      86.825  -1.364  -6.552  1.00 20.50           N  
-ATOM   2652  CA  ALA A 365      87.793  -2.459  -6.615  1.00 20.21           C  
-ATOM   2653  C   ALA A 365      88.527  -2.571  -5.279  1.00 20.28           C  
-ATOM   2654  O   ALA A 365      88.715  -1.569  -4.588  1.00 21.20           O  
-ATOM   2655  CB  ALA A 365      88.785  -2.222  -7.745  1.00 18.85           C  
-ATOM   2656  N   THR A 366      88.916  -3.784  -4.904  1.00 20.20           N  
-ATOM   2657  CA  THR A 366      89.640  -4.009  -3.654  1.00 20.00           C  
-ATOM   2658  C   THR A 366      91.112  -3.669  -3.871  1.00 20.07           C  
-ATOM   2659  O   THR A 366      91.562  -3.563  -5.015  1.00 19.16           O  
-ATOM   2660  CB  THR A 366      89.597  -5.489  -3.248  1.00 20.13           C  
-ATOM   2661  OG1 THR A 366      90.259  -6.268  -4.256  1.00 20.18           O  
-ATOM   2662  CG2 THR A 366      88.161  -5.969  -3.073  1.00 19.50           C  
-ATOM   2663  N   PRO A 367      91.894  -3.532  -2.780  1.00 21.16           N  
-ATOM   2664  CA  PRO A 367      93.322  -3.214  -2.910  1.00 22.39           C  
-ATOM   2665  C   PRO A 367      94.054  -4.234  -3.796  1.00 24.06           C  
-ATOM   2666  O   PRO A 367      94.913  -3.861  -4.599  1.00 24.07           O  
-ATOM   2667  CB  PRO A 367      93.807  -3.259  -1.464  1.00 21.74           C  
-ATOM   2668  CG  PRO A 367      92.628  -2.721  -0.715  1.00 20.55           C  
-ATOM   2669  CD  PRO A 367      91.482  -3.480  -1.361  1.00 20.51           C  
-ATOM   2670  N   GLU A 368      93.686  -5.510  -3.672  1.00 25.58           N  
-ATOM   2671  CA  GLU A 368      94.289  -6.571  -4.480  1.00 26.44           C  
-ATOM   2672  C   GLU A 368      94.031  -6.313  -5.953  1.00 25.43           C  
-ATOM   2673  O   GLU A 368      94.939  -6.432  -6.777  1.00 25.93           O  
-ATOM   2674  CB  GLU A 368      93.712  -7.943  -4.122  1.00 29.59           C  
-ATOM   2675  CG  GLU A 368      94.338  -8.594  -2.906  1.00 34.27           C  
-ATOM   2676  CD  GLU A 368      93.721  -9.945  -2.578  1.00 37.48           C  
-ATOM   2677  OE1 GLU A 368      93.386 -10.705  -3.518  1.00 38.98           O  
-ATOM   2678  OE2 GLU A 368      93.573 -10.248  -1.372  1.00 39.37           O  
-ATOM   2679  N   GLN A 369      92.784  -5.980  -6.279  1.00 23.99           N  
-ATOM   2680  CA  GLN A 369      92.406  -5.702  -7.658  1.00 22.29           C  
-ATOM   2681  C   GLN A 369      93.135  -4.471  -8.166  1.00 20.72           C  
-ATOM   2682  O   GLN A 369      93.564  -4.428  -9.318  1.00 19.96           O  
-ATOM   2683  CB  GLN A 369      90.888  -5.534  -7.775  1.00 23.01           C  
-ATOM   2684  CG  GLN A 369      90.127  -6.832  -7.522  1.00 23.85           C  
-ATOM   2685  CD  GLN A 369      88.621  -6.650  -7.497  1.00 23.91           C  
-ATOM   2686  OE1 GLN A 369      88.108  -5.690  -6.920  1.00 24.34           O  
-ATOM   2687  NE2 GLN A 369      87.904  -7.583  -8.108  1.00 23.96           N  
-ATOM   2688  N   VAL A 370      93.306  -3.487  -7.288  1.00 20.17           N  
-ATOM   2689  CA  VAL A 370      94.010  -2.254  -7.629  1.00 20.38           C  
-ATOM   2690  C   VAL A 370      95.478  -2.557  -7.955  1.00 20.50           C  
-ATOM   2691  O   VAL A 370      96.014  -2.065  -8.950  1.00 20.22           O  
-ATOM   2692  CB  VAL A 370      93.921  -1.214  -6.478  1.00 19.76           C  
-ATOM   2693  CG1 VAL A 370      94.839  -0.044  -6.740  1.00 18.79           C  
-ATOM   2694  CG2 VAL A 370      92.493  -0.714  -6.338  1.00 19.56           C  
-ATOM   2695  N   LYS A 371      96.111  -3.388  -7.135  1.00 21.51           N  
-ATOM   2696  CA  LYS A 371      97.505  -3.756  -7.350  1.00 23.25           C  
-ATOM   2697  C   LYS A 371      97.666  -4.576  -8.627  1.00 23.75           C  
-ATOM   2698  O   LYS A 371      98.606  -4.365  -9.393  1.00 24.41           O  
-ATOM   2699  CB  LYS A 371      98.056  -4.527  -6.149  1.00 24.65           C  
-ATOM   2700  CG  LYS A 371      99.473  -5.060  -6.368  1.00 29.42           C  
-ATOM   2701  CD  LYS A 371     100.254  -5.274  -5.067  1.00 32.57           C  
-ATOM   2702  CE  LYS A 371      99.558  -6.239  -4.112  1.00 35.15           C  
-ATOM   2703  NZ  LYS A 371      99.295  -7.572  -4.728  1.00 37.99           N  
-ATOM   2704  N   ARG A 372      96.728  -5.486  -8.867  1.00 24.50           N  
-ATOM   2705  CA  ARG A 372      96.764  -6.336 -10.048  1.00 25.00           C  
-ATOM   2706  C   ARG A 372      96.572  -5.527 -11.333  1.00 24.82           C  
-ATOM   2707  O   ARG A 372      97.133  -5.871 -12.374  1.00 24.98           O  
-ATOM   2708  CB  ARG A 372      95.717  -7.452  -9.938  1.00 26.85           C  
-ATOM   2709  CG  ARG A 372      95.874  -8.542 -10.984  1.00 29.85           C  
-ATOM   2710  CD  ARG A 372      94.967  -9.739 -10.721  1.00 32.38           C  
-ATOM   2711  NE  ARG A 372      95.477 -10.639  -9.684  1.00 34.85           N  
-ATOM   2712  CZ  ARG A 372      96.179 -11.750  -9.919  1.00 35.36           C  
-ATOM   2713  NH1 ARG A 372      96.479 -12.116 -11.159  1.00 35.15           N  
-ATOM   2714  NH2 ARG A 372      96.544 -12.526  -8.910  1.00 36.78           N  
-ATOM   2715  N   ILE A 373      95.794  -4.448 -11.264  1.00 23.98           N  
-ATOM   2716  CA  ILE A 373      95.580  -3.600 -12.438  1.00 22.93           C  
-ATOM   2717  C   ILE A 373      96.891  -2.897 -12.794  1.00 22.71           C  
-ATOM   2718  O   ILE A 373      97.264  -2.822 -13.965  1.00 22.33           O  
-ATOM   2719  CB  ILE A 373      94.466  -2.546 -12.196  1.00 22.96           C  
-ATOM   2720  CG1 ILE A 373      93.095  -3.223 -12.190  1.00 23.10           C  
-ATOM   2721  CG2 ILE A 373      94.503  -1.466 -13.271  1.00 21.91           C  
-ATOM   2722  CD1 ILE A 373      91.934  -2.280 -11.920  1.00 23.70           C  
-ATOM   2723  N   LYS A 374      97.588  -2.398 -11.776  1.00 22.80           N  
-ATOM   2724  CA  LYS A 374      98.860  -1.706 -11.962  1.00 22.90           C  
-ATOM   2725  C   LYS A 374      99.928  -2.645 -12.528  1.00 22.69           C  
-ATOM   2726  O   LYS A 374     100.548  -2.349 -13.545  1.00 21.40           O  
-ATOM   2727  CB  LYS A 374      99.337  -1.111 -10.635  1.00 23.21           C  
-ATOM   2728  CG  LYS A 374     100.700  -0.432 -10.706  1.00 24.49           C  
-ATOM   2729  CD  LYS A 374     101.139   0.054  -9.339  1.00 26.06           C  
-ATOM   2730  CE  LYS A 374     101.220  -1.090  -8.342  1.00 27.73           C  
-ATOM   2731  NZ  LYS A 374     101.519  -0.599  -6.970  1.00 28.65           N  
-ATOM   2732  N   GLU A 375     100.113  -3.789 -11.880  1.00 23.64           N  
-ATOM   2733  CA  GLU A 375     101.102  -4.774 -12.314  1.00 25.21           C  
-ATOM   2734  C   GLU A 375     100.897  -5.322 -13.725  1.00 24.59           C  
-ATOM   2735  O   GLU A 375     101.849  -5.429 -14.491  1.00 25.53           O  
-ATOM   2736  CB  GLU A 375     101.160  -5.939 -11.328  1.00 25.85           C  
-ATOM   2737  CG  GLU A 375     101.727  -5.571  -9.977  1.00 30.15           C  
-ATOM   2738  CD  GLU A 375     101.552  -6.671  -8.954  1.00 33.53           C  
-ATOM   2739  OE1 GLU A 375     100.470  -7.302  -8.933  1.00 36.51           O  
-ATOM   2740  OE2 GLU A 375     102.491  -6.903  -8.156  1.00 35.19           O  
-ATOM   2741  N   GLU A 376      99.664  -5.667 -14.070  1.00 24.12           N  
-ATOM   2742  CA  GLU A 376      99.387  -6.235 -15.385  1.00 23.86           C  
-ATOM   2743  C   GLU A 376      99.076  -5.234 -16.486  1.00 23.24           C  
-ATOM   2744  O   GLU A 376      99.290  -5.524 -17.661  1.00 23.45           O  
-ATOM   2745  CB  GLU A 376      98.226  -7.231 -15.301  1.00 24.21           C  
-ATOM   2746  CG  GLU A 376      98.411  -8.360 -14.300  1.00 24.64           C  
-ATOM   2747  CD  GLU A 376      97.184  -9.260 -14.198  1.00 25.99           C  
-ATOM   2748  OE1 GLU A 376      96.103  -8.890 -14.713  1.00 25.23           O  
-ATOM   2749  OE2 GLU A 376      97.299 -10.342 -13.586  1.00 27.16           O  
-ATOM   2750  N   PHE A 377      98.536  -4.079 -16.120  1.00 22.39           N  
-ATOM   2751  CA  PHE A 377      98.160  -3.094 -17.121  1.00 21.67           C  
-ATOM   2752  C   PHE A 377      98.867  -1.745 -17.040  1.00 21.89           C  
-ATOM   2753  O   PHE A 377      98.665  -0.882 -17.901  1.00 22.01           O  
-ATOM   2754  CB  PHE A 377      96.640  -2.907 -17.106  1.00 22.00           C  
-ATOM   2755  CG  PHE A 377      95.874  -4.146 -17.495  1.00 21.75           C  
-ATOM   2756  CD1 PHE A 377      95.494  -5.077 -16.537  1.00 21.97           C  
-ATOM   2757  CD2 PHE A 377      95.553  -4.390 -18.825  1.00 22.06           C  
-ATOM   2758  CE1 PHE A 377      94.807  -6.240 -16.899  1.00 21.88           C  
-ATOM   2759  CE2 PHE A 377      94.867  -5.547 -19.199  1.00 22.63           C  
-ATOM   2760  CZ  PHE A 377      94.494  -6.474 -18.234  1.00 22.25           C  
-ATOM   2761  N   GLY A 378      99.696  -1.563 -16.016  1.00 20.77           N  
-ATOM   2762  CA  GLY A 378     100.419  -0.312 -15.862  1.00 20.81           C  
-ATOM   2763  C   GLY A 378      99.555   0.910 -15.593  1.00 20.99           C  
-ATOM   2764  O   GLY A 378      99.972   2.046 -15.845  1.00 20.93           O  
-ATOM   2765  N   ILE A 379      98.360   0.690 -15.058  1.00 20.75           N  
-ATOM   2766  CA  ILE A 379      97.457   1.792 -14.751  1.00 19.84           C  
-ATOM   2767  C   ILE A 379      97.495   2.070 -13.248  1.00 19.24           C  
-ATOM   2768  O   ILE A 379      97.249   1.177 -12.432  1.00 19.36           O  
-ATOM   2769  CB  ILE A 379      96.013   1.473 -15.207  1.00 20.89           C  
-ATOM   2770  CG1 ILE A 379      95.995   1.189 -16.717  1.00 20.38           C  
-ATOM   2771  CG2 ILE A 379      95.071   2.636 -14.853  1.00 21.15           C  
-ATOM   2772  CD1 ILE A 379      94.685   0.648 -17.235  1.00 18.57           C  
-ATOM   2773  N   TYR A 380      97.850   3.297 -12.891  1.00 18.28           N  
-ATOM   2774  CA  TYR A 380      97.937   3.707 -11.495  1.00 18.77           C  
-ATOM   2775  C   TYR A 380      96.691   4.456 -11.034  1.00 18.12           C  
-ATOM   2776  O   TYR A 380      96.108   5.236 -11.787  1.00 16.78           O  
-ATOM   2777  CB  TYR A 380      99.172   4.590 -11.281  1.00 20.23           C  
-ATOM   2778  CG  TYR A 380     100.472   3.829 -11.361  1.00 21.80           C  
-ATOM   2779  CD1 TYR A 380     100.889   3.234 -12.560  1.00 21.93           C  
-ATOM   2780  CD2 TYR A 380     101.264   3.661 -10.228  1.00 21.51           C  
-ATOM   2781  CE1 TYR A 380     102.059   2.485 -12.619  1.00 23.63           C  
-ATOM   2782  CE2 TYR A 380     102.430   2.918 -10.274  1.00 23.85           C  
-ATOM   2783  CZ  TYR A 380     102.822   2.327 -11.468  1.00 24.33           C  
-ATOM   2784  OH  TYR A 380     103.950   1.545 -11.485  1.00 24.58           O  
-ATOM   2785  N   MET A 381      96.300   4.225  -9.788  1.00 17.27           N  
-ATOM   2786  CA  MET A 381      95.136   4.881  -9.205  1.00 18.30           C  
-ATOM   2787  C   MET A 381      95.289   4.845  -7.692  1.00 17.67           C  
-ATOM   2788  O   MET A 381      96.162   4.155  -7.173  1.00 18.16           O  
-ATOM   2789  CB  MET A 381      93.830   4.190  -9.640  1.00 17.97           C  
-ATOM   2790  CG  MET A 381      93.681   2.727  -9.220  1.00 18.28           C  
-ATOM   2791  SD  MET A 381      92.091   1.996  -9.742  1.00 19.63           S  
-ATOM   2792  CE  MET A 381      92.334   1.807 -11.511  1.00 18.33           C  
-ATOM   2793  N   VAL A 382      94.475   5.620  -6.987  1.00 17.35           N  
-ATOM   2794  CA  VAL A 382      94.541   5.644  -5.533  1.00 16.36           C  
-ATOM   2795  C   VAL A 382      94.149   4.259  -5.016  1.00 17.38           C  
-ATOM   2796  O   VAL A 382      93.287   3.582  -5.595  1.00 16.41           O  
-ATOM   2797  CB  VAL A 382      93.615   6.740  -4.942  1.00 16.07           C  
-ATOM   2798  CG1 VAL A 382      93.739   6.789  -3.424  1.00 14.47           C  
-ATOM   2799  CG2 VAL A 382      93.962   8.094  -5.535  1.00 13.21           C  
-ATOM   2800  N   GLY A 383      94.778   3.856  -3.917  1.00 18.63           N  
-ATOM   2801  CA  GLY A 383      94.538   2.552  -3.320  1.00 18.85           C  
-ATOM   2802  C   GLY A 383      93.106   2.176  -3.011  1.00 19.88           C  
-ATOM   2803  O   GLY A 383      92.807   0.995  -2.850  1.00 21.23           O  
-ATOM   2804  N   ASP A 384      92.222   3.163  -2.908  1.00 20.52           N  
-ATOM   2805  CA  ASP A 384      90.809   2.907  -2.619  1.00 20.19           C  
-ATOM   2806  C   ASP A 384      89.989   2.756  -3.905  1.00 20.34           C  
-ATOM   2807  O   ASP A 384      88.758   2.764  -3.868  1.00 22.21           O  
-ATOM   2808  CB  ASP A 384      90.232   4.038  -1.753  1.00 20.37           C  
-ATOM   2809  CG  ASP A 384      90.177   5.385  -2.482  1.00 21.33           C  
-ATOM   2810  OD1 ASP A 384      90.826   5.551  -3.534  1.00 21.53           O  
-ATOM   2811  OD2 ASP A 384      89.477   6.292  -1.992  1.00 22.59           O  
-ATOM   2812  N   SER A 385      90.691   2.666  -5.034  1.00 18.27           N  
-ATOM   2813  CA  SER A 385      90.107   2.530  -6.368  1.00 17.01           C  
-ATOM   2814  C   SER A 385      89.516   3.827  -6.928  1.00 16.80           C  
-ATOM   2815  O   SER A 385      88.678   3.803  -7.830  1.00 16.52           O  
-ATOM   2816  CB  SER A 385      89.104   1.361  -6.446  1.00 15.99           C  
-ATOM   2817  OG  SER A 385      87.843   1.657  -5.872  1.00 15.77           O  
-ATOM   2818  N   ARG A 386      89.995   4.958  -6.418  1.00 16.88           N  
-ATOM   2819  CA  ARG A 386      89.540   6.270  -6.882  1.00 16.46           C  
-ATOM   2820  C   ARG A 386      90.310   6.641  -8.137  1.00 15.82           C  
-ATOM   2821  O   ARG A 386      91.537   6.557  -8.162  1.00 15.77           O  
-ATOM   2822  CB  ARG A 386      89.808   7.349  -5.831  1.00 17.00           C  
-ATOM   2823  CG  ARG A 386      89.252   8.713  -6.201  1.00 16.20           C  
-ATOM   2824  CD  ARG A 386      89.842   9.810  -5.341  1.00 17.48           C  
-ATOM   2825  NE  ARG A 386      91.122  10.283  -5.855  1.00 19.81           N  
-ATOM   2826  CZ  ARG A 386      91.726  11.392  -5.441  1.00 20.49           C  
-ATOM   2827  NH1 ARG A 386      91.167  12.137  -4.500  1.00 20.64           N  
-ATOM   2828  NH2 ARG A 386      92.873  11.774  -5.992  1.00 20.30           N  
-ATOM   2829  N   ILE A 387      89.596   7.065  -9.170  1.00 15.61           N  
-ATOM   2830  CA  ILE A 387      90.235   7.462 -10.412  1.00 15.21           C  
-ATOM   2831  C   ILE A 387      89.824   8.879 -10.748  1.00 15.15           C  
-ATOM   2832  O   ILE A 387      88.796   9.361 -10.280  1.00 15.09           O  
-ATOM   2833  CB  ILE A 387      89.832   6.560 -11.597  1.00 15.25           C  
-ATOM   2834  CG1 ILE A 387      88.313   6.584 -11.793  1.00 14.69           C  
-ATOM   2835  CG2 ILE A 387      90.346   5.155 -11.382  1.00 15.00           C  
-ATOM   2836  CD1 ILE A 387      87.862   6.055 -13.141  1.00 15.58           C  
-ATOM   2837  N   ASN A 388      90.651   9.546 -11.539  1.00 15.81           N  
-ATOM   2838  CA  ASN A 388      90.370  10.898 -11.979  1.00 16.13           C  
-ATOM   2839  C   ASN A 388      89.935  10.772 -13.431  1.00 16.66           C  
-ATOM   2840  O   ASN A 388      90.707  10.332 -14.287  1.00 15.52           O  
-ATOM   2841  CB  ASN A 388      91.620  11.766 -11.878  1.00 16.92           C  
-ATOM   2842  CG  ASN A 388      91.349  13.213 -12.225  1.00 17.29           C  
-ATOM   2843  OD1 ASN A 388      90.582  13.522 -13.140  1.00 17.62           O  
-ATOM   2844  ND2 ASN A 388      91.977  14.112 -11.493  1.00 18.35           N  
-ATOM   2845  N   ILE A 389      88.685  11.130 -13.692  1.00 17.15           N  
-ATOM   2846  CA  ILE A 389      88.102  11.058 -15.027  1.00 18.50           C  
-ATOM   2847  C   ILE A 389      88.850  11.902 -16.063  1.00 19.46           C  
-ATOM   2848  O   ILE A 389      89.008  11.482 -17.216  1.00 19.22           O  
-ATOM   2849  CB  ILE A 389      86.602  11.457 -14.978  1.00 18.34           C  
-ATOM   2850  CG1 ILE A 389      85.839  10.453 -14.116  1.00 18.42           C  
-ATOM   2851  CG2 ILE A 389      85.995  11.481 -16.373  1.00 19.23           C  
-ATOM   2852  CD1 ILE A 389      85.916   9.032 -14.641  1.00 18.31           C  
-ATOM   2853  N   ALA A 390      89.338  13.068 -15.641  1.00 20.05           N  
-ATOM   2854  CA  ALA A 390      90.064  13.974 -16.529  1.00 21.16           C  
-ATOM   2855  C   ALA A 390      91.345  13.360 -17.102  1.00 22.28           C  
-ATOM   2856  O   ALA A 390      91.784  13.735 -18.187  1.00 23.66           O  
-ATOM   2857  CB  ALA A 390      90.376  15.278 -15.808  1.00 21.21           C  
-ATOM   2858  N   GLY A 391      91.930  12.405 -16.385  1.00 23.47           N  
-ATOM   2859  CA  GLY A 391      93.142  11.758 -16.862  1.00 25.32           C  
-ATOM   2860  C   GLY A 391      92.888  10.715 -17.941  1.00 27.15           C  
-ATOM   2861  O   GLY A 391      93.820  10.055 -18.415  1.00 27.49           O  
-ATOM   2862  N   LEU A 392      91.623  10.568 -18.328  1.00 28.00           N  
-ATOM   2863  CA  LEU A 392      91.204   9.609 -19.346  1.00 28.86           C  
-ATOM   2864  C   LEU A 392      91.083  10.268 -20.718  1.00 29.65           C  
-ATOM   2865  O   LEU A 392      91.109  11.496 -20.832  1.00 30.77           O  
-ATOM   2866  CB  LEU A 392      89.844   9.025 -18.960  1.00 29.79           C  
-ATOM   2867  CG  LEU A 392      89.711   7.610 -18.389  1.00 29.86           C  
-ATOM   2868  CD1 LEU A 392      90.816   7.298 -17.413  1.00 30.85           C  
-ATOM   2869  CD2 LEU A 392      88.347   7.481 -17.727  1.00 29.50           C  
-ATOM   2870  N   ASN A 393      90.945   9.445 -21.755  1.00 29.47           N  
-ATOM   2871  CA  ASN A 393      90.789   9.924 -23.124  1.00 28.79           C  
-ATOM   2872  C   ASN A 393      90.516   8.778 -24.090  1.00 28.40           C  
-ATOM   2873  O   ASN A 393      90.508   7.610 -23.701  1.00 28.27           O  
-ATOM   2874  CB  ASN A 393      92.019  10.723 -23.588  1.00 30.00           C  
-ATOM   2875  CG  ASN A 393      93.289   9.891 -23.623  1.00 30.91           C  
-ATOM   2876  OD1 ASN A 393      93.378   8.888 -24.338  1.00 30.21           O  
-ATOM   2877  ND2 ASN A 393      94.286  10.316 -22.862  1.00 32.60           N  
-ATOM   2878  N   ASP A 394      90.311   9.134 -25.353  1.00 28.48           N  
-ATOM   2879  CA  ASP A 394      90.031   8.191 -26.429  1.00 29.12           C  
-ATOM   2880  C   ASP A 394      90.982   7.001 -26.495  1.00 28.60           C  
-ATOM   2881  O   ASP A 394      90.586   5.901 -26.880  1.00 28.21           O  
-ATOM   2882  CB  ASP A 394      90.088   8.928 -27.767  1.00 31.77           C  
-ATOM   2883  CG  ASP A 394      88.726   9.115 -28.393  1.00 34.84           C  
-ATOM   2884  OD1 ASP A 394      87.837   9.701 -27.733  1.00 36.45           O  
-ATOM   2885  OD2 ASP A 394      88.553   8.680 -29.555  1.00 36.73           O  
-ATOM   2886  N   ASN A 395      92.247   7.238 -26.166  1.00 27.64           N  
-ATOM   2887  CA  ASN A 395      93.253   6.189 -26.207  1.00 26.50           C  
-ATOM   2888  C   ASN A 395      93.388   5.379 -24.930  1.00 25.77           C  
-ATOM   2889  O   ASN A 395      93.723   4.196 -24.980  1.00 27.05           O  
-ATOM   2890  CB  ASN A 395      94.611   6.777 -26.592  1.00 25.79           C  
-ATOM   2891  CG  ASN A 395      94.617   7.353 -27.989  1.00 24.90           C  
-ATOM   2892  OD1 ASN A 395      95.176   8.415 -28.229  1.00 24.92           O  
-ATOM   2893  ND2 ASN A 395      93.984   6.656 -28.921  1.00 24.62           N  
-ATOM   2894  N   THR A 396      93.111   5.991 -23.788  1.00 24.57           N  
-ATOM   2895  CA  THR A 396      93.248   5.283 -22.522  1.00 23.73           C  
-ATOM   2896  C   THR A 396      91.992   4.574 -22.004  1.00 22.94           C  
-ATOM   2897  O   THR A 396      92.089   3.596 -21.257  1.00 23.40           O  
-ATOM   2898  CB  THR A 396      93.848   6.208 -21.450  1.00 24.16           C  
-ATOM   2899  OG1 THR A 396      93.090   7.422 -21.376  1.00 23.98           O  
-ATOM   2900  CG2 THR A 396      95.292   6.553 -21.822  1.00 24.69           C  
-ATOM   2901  N   ILE A 397      90.821   5.031 -22.441  1.00 21.48           N  
-ATOM   2902  CA  ILE A 397      89.552   4.438 -22.022  1.00 20.14           C  
-ATOM   2903  C   ILE A 397      89.427   2.945 -22.365  1.00 19.91           C  
-ATOM   2904  O   ILE A 397      89.046   2.139 -21.509  1.00 19.11           O  
-ATOM   2905  CB  ILE A 397      88.337   5.239 -22.593  1.00 19.37           C  
-ATOM   2906  CG1 ILE A 397      88.138   6.528 -21.789  1.00 18.59           C  
-ATOM   2907  CG2 ILE A 397      87.066   4.389 -22.590  1.00 17.62           C  
-ATOM   2908  CD1 ILE A 397      87.184   7.516 -22.434  1.00 17.82           C  
-ATOM   2909  N   PRO A 398      89.745   2.553 -23.614  1.00 19.80           N  
-ATOM   2910  CA  PRO A 398      89.638   1.138 -23.979  1.00 19.92           C  
-ATOM   2911  C   PRO A 398      90.506   0.251 -23.090  1.00 20.65           C  
-ATOM   2912  O   PRO A 398      90.093  -0.842 -22.687  1.00 21.53           O  
-ATOM   2913  CB  PRO A 398      90.138   1.128 -25.422  1.00 19.72           C  
-ATOM   2914  CG  PRO A 398      89.724   2.460 -25.923  1.00 18.62           C  
-ATOM   2915  CD  PRO A 398      90.133   3.354 -24.789  1.00 18.85           C  
-ATOM   2916  N   ILE A 399      91.681   0.761 -22.741  1.00 20.51           N  
-ATOM   2917  CA  ILE A 399      92.636   0.038 -21.912  1.00 21.04           C  
-ATOM   2918  C   ILE A 399      92.144  -0.166 -20.486  1.00 20.66           C  
-ATOM   2919  O   ILE A 399      92.238  -1.270 -19.952  1.00 19.86           O  
-ATOM   2920  CB  ILE A 399      93.983   0.780 -21.872  1.00 22.07           C  
-ATOM   2921  CG1 ILE A 399      94.406   1.165 -23.293  1.00 21.53           C  
-ATOM   2922  CG2 ILE A 399      95.039  -0.095 -21.209  1.00 21.55           C  
-ATOM   2923  CD1 ILE A 399      95.634   2.042 -23.350  1.00 23.60           C  
-ATOM   2924  N   LEU A 400      91.648   0.909 -19.873  1.00 20.91           N  
-ATOM   2925  CA  LEU A 400      91.124   0.881 -18.501  1.00 21.39           C  
-ATOM   2926  C   LEU A 400      89.910  -0.050 -18.403  1.00 21.52           C  
-ATOM   2927  O   LEU A 400      89.754  -0.788 -17.430  1.00 21.11           O  
-ATOM   2928  CB  LEU A 400      90.705   2.294 -18.068  1.00 21.55           C  
-ATOM   2929  CG  LEU A 400      90.666   2.714 -16.589  1.00 21.49           C  
-ATOM   2930  CD1 LEU A 400      89.410   3.537 -16.345  1.00 20.48           C  
-ATOM   2931  CD2 LEU A 400      90.713   1.527 -15.643  1.00 20.39           C  
-ATOM   2932  N   ALA A 401      89.035   0.027 -19.403  1.00 22.11           N  
-ATOM   2933  CA  ALA A 401      87.837  -0.800 -19.466  1.00 22.58           C  
-ATOM   2934  C   ALA A 401      88.227  -2.277 -19.462  1.00 22.91           C  
-ATOM   2935  O   ALA A 401      87.756  -3.052 -18.621  1.00 22.17           O  
-ATOM   2936  CB  ALA A 401      87.043  -0.467 -20.719  1.00 21.74           C  
-ATOM   2937  N   ARG A 402      89.095  -2.657 -20.397  1.00 23.37           N  
-ATOM   2938  CA  ARG A 402      89.561  -4.036 -20.490  1.00 25.35           C  
-ATOM   2939  C   ARG A 402      90.214  -4.472 -19.175  1.00 24.77           C  
-ATOM   2940  O   ARG A 402      89.986  -5.582 -18.699  1.00 24.94           O  
-ATOM   2941  CB  ARG A 402      90.557  -4.201 -21.642  1.00 27.85           C  
-ATOM   2942  CG  ARG A 402      91.079  -5.623 -21.777  1.00 32.41           C  
-ATOM   2943  CD  ARG A 402      92.428  -5.684 -22.492  1.00 36.39           C  
-ATOM   2944  NE  ARG A 402      93.274  -6.732 -21.918  1.00 38.95           N  
-ATOM   2945  CZ  ARG A 402      93.787  -7.752 -22.600  1.00 39.63           C  
-ATOM   2946  NH1 ARG A 402      93.563  -7.872 -23.903  1.00 39.42           N  
-ATOM   2947  NH2 ARG A 402      94.539  -8.650 -21.970  1.00 40.47           N  
-ATOM   2948  N   ALA A 403      91.003  -3.584 -18.580  1.00 24.29           N  
-ATOM   2949  CA  ALA A 403      91.681  -3.878 -17.320  1.00 24.72           C  
-ATOM   2950  C   ALA A 403      90.686  -4.221 -16.222  1.00 24.82           C  
-ATOM   2951  O   ALA A 403      90.850  -5.212 -15.507  1.00 24.49           O  
-ATOM   2952  CB  ALA A 403      92.544  -2.691 -16.893  1.00 24.97           C  
-ATOM   2953  N   ILE A 404      89.654  -3.395 -16.097  1.00 25.46           N  
-ATOM   2954  CA  ILE A 404      88.619  -3.584 -15.088  1.00 26.43           C  
-ATOM   2955  C   ILE A 404      87.977  -4.958 -15.227  1.00 26.89           C  
-ATOM   2956  O   ILE A 404      87.870  -5.700 -14.252  1.00 26.88           O  
-ATOM   2957  CB  ILE A 404      87.540  -2.479 -15.193  1.00 26.48           C  
-ATOM   2958  CG1 ILE A 404      88.150  -1.123 -14.831  1.00 26.55           C  
-ATOM   2959  CG2 ILE A 404      86.364  -2.790 -14.283  1.00 26.44           C  
-ATOM   2960  CD1 ILE A 404      87.238   0.051 -15.081  1.00 27.26           C  
-ATOM   2961  N   ILE A 405      87.575  -5.299 -16.448  1.00 28.16           N  
-ATOM   2962  CA  ILE A 405      86.946  -6.586 -16.719  1.00 29.57           C  
-ATOM   2963  C   ILE A 405      87.909  -7.739 -16.425  1.00 31.01           C  
-ATOM   2964  O   ILE A 405      87.575  -8.672 -15.684  1.00 31.75           O  
-ATOM   2965  CB  ILE A 405      86.434  -6.666 -18.200  1.00 29.63           C  
-ATOM   2966  CG1 ILE A 405      84.983  -6.183 -18.292  1.00 30.19           C  
-ATOM   2967  CG2 ILE A 405      86.513  -8.087 -18.748  1.00 28.86           C  
-ATOM   2968  CD1 ILE A 405      84.786  -4.739 -17.962  1.00 29.97           C  
-ATOM   2969  N   GLU A 406      89.125  -7.628 -16.944  1.00 31.46           N  
-ATOM   2970  CA  GLU A 406      90.123  -8.669 -16.783  1.00 32.09           C  
-ATOM   2971  C   GLU A 406      90.474  -9.035 -15.349  1.00 31.61           C  
-ATOM   2972  O   GLU A 406      90.703 -10.206 -15.054  1.00 31.95           O  
-ATOM   2973  CB  GLU A 406      91.384  -8.311 -17.559  1.00 34.28           C  
-ATOM   2974  CG  GLU A 406      92.155  -9.524 -18.055  1.00 39.18           C  
-ATOM   2975  CD  GLU A 406      91.386 -10.330 -19.101  1.00 40.90           C  
-ATOM   2976  OE1 GLU A 406      90.590 -11.217 -18.715  1.00 40.96           O  
-ATOM   2977  OE2 GLU A 406      91.588 -10.076 -20.310  1.00 43.27           O  
-ATOM   2978  N   VAL A 407      90.513  -8.048 -14.458  1.00 31.11           N  
-ATOM   2979  CA  VAL A 407      90.850  -8.295 -13.055  1.00 30.37           C  
-ATOM   2980  C   VAL A 407      89.622  -8.734 -12.232  1.00 30.86           C  
-ATOM   2981  O   VAL A 407      89.704  -8.964 -11.020  1.00 30.42           O  
-ATOM   2982  CB  VAL A 407      91.573  -7.064 -12.434  1.00 30.08           C  
-ATOM   2983  CG1 VAL A 407      91.970  -7.332 -11.002  1.00 30.66           C  
-ATOM   2984  CG2 VAL A 407      92.822  -6.736 -13.242  1.00 29.02           C  
-ATOM   2985  N   GLY A 408      88.490  -8.885 -12.911  1.00 30.51           N  
-ATOM   2986  CA  GLY A 408      87.283  -9.337 -12.247  1.00 30.74           C  
-ATOM   2987  C   GLY A 408      86.632  -8.385 -11.270  1.00 31.18           C  
-ATOM   2988  O   GLY A 408      86.332  -8.763 -10.134  1.00 31.32           O  
-ATOM   2989  N   VAL A 409      86.447  -7.142 -11.694  1.00 31.42           N  
-ATOM   2990  CA  VAL A 409      85.791  -6.139 -10.866  1.00 30.98           C  
-ATOM   2991  C   VAL A 409      84.314  -6.144 -11.281  1.00 31.13           C  
-ATOM   2992  O   VAL A 409      84.030  -6.499 -12.451  1.00 30.35           O  
-ATOM   2993  CB  VAL A 409      86.410  -4.730 -11.089  1.00 31.54           C  
-ATOM   2994  CG1 VAL A 409      85.634  -3.662 -10.318  1.00 30.70           C  
-ATOM   2995  CG2 VAL A 409      87.872  -4.724 -10.659  1.00 30.99           C  
-ATOM   2996  OXT VAL A 409      83.455  -5.835 -10.429  1.00 30.84           O  
-TER    2997      VAL A 409                                                      
-ATOM   2998  N   MET B   5      74.402  27.522  18.434  1.00 37.93           N  
-ATOM   2999  CA  MET B   5      75.849  27.423  18.755  1.00 37.60           C  
-ATOM   3000  C   MET B   5      76.566  28.758  18.637  1.00 36.68           C  
-ATOM   3001  O   MET B   5      77.105  29.260  19.615  1.00 36.51           O  
-ATOM   3002  CB  MET B   5      76.538  26.403  17.849  1.00 39.43           C  
-ATOM   3003  CG  MET B   5      76.687  25.023  18.453  1.00 41.40           C  
-ATOM   3004  SD  MET B   5      77.757  24.001  17.433  1.00 44.44           S  
-ATOM   3005  CE  MET B   5      79.225  24.989  17.460  1.00 42.46           C  
-ATOM   3006  N   LEU B   6      76.541  29.350  17.447  1.00 35.59           N  
-ATOM   3007  CA  LEU B   6      77.230  30.615  17.211  1.00 35.10           C  
-ATOM   3008  C   LEU B   6      76.831  31.748  18.153  1.00 35.50           C  
-ATOM   3009  O   LEU B   6      77.603  32.684  18.365  1.00 35.60           O  
-ATOM   3010  CB  LEU B   6      77.090  31.040  15.745  1.00 33.88           C  
-ATOM   3011  CG  LEU B   6      77.564  30.011  14.709  1.00 33.42           C  
-ATOM   3012  CD1 LEU B   6      77.449  30.599  13.314  1.00 32.77           C  
-ATOM   3013  CD2 LEU B   6      78.994  29.560  14.991  1.00 31.97           C  
-ATOM   3014  N   GLY B   7      75.643  31.647  18.741  1.00 35.76           N  
-ATOM   3015  CA  GLY B   7      75.189  32.667  19.667  1.00 36.51           C  
-ATOM   3016  C   GLY B   7      75.989  32.660  20.960  1.00 37.90           C  
-ATOM   3017  O   GLY B   7      75.917  33.604  21.743  1.00 37.83           O  
-ATOM   3018  N   ASN B   8      76.752  31.594  21.180  1.00 38.87           N  
-ATOM   3019  CA  ASN B   8      77.570  31.454  22.378  1.00 40.49           C  
-ATOM   3020  C   ASN B   8      78.954  32.092  22.240  1.00 40.52           C  
-ATOM   3021  O   ASN B   8      79.738  32.086  23.183  1.00 40.36           O  
-ATOM   3022  CB  ASN B   8      77.727  29.978  22.741  1.00 43.13           C  
-ATOM   3023  CG  ASN B   8      76.395  29.285  22.958  1.00 45.79           C  
-ATOM   3024  OD1 ASN B   8      75.573  29.176  22.041  1.00 48.37           O  
-ATOM   3025  ND2 ASN B   8      76.179  28.796  24.170  1.00 47.21           N  
-ATOM   3026  N   LEU B   9      79.249  32.637  21.062  1.00 40.86           N  
-ATOM   3027  CA  LEU B   9      80.534  33.281  20.787  1.00 41.26           C  
-ATOM   3028  C   LEU B   9      80.746  34.580  21.552  1.00 42.69           C  
-ATOM   3029  O   LEU B   9      79.979  35.534  21.400  1.00 43.30           O  
-ATOM   3030  CB  LEU B   9      80.680  33.577  19.304  1.00 39.40           C  
-ATOM   3031  CG  LEU B   9      80.903  32.426  18.330  1.00 38.33           C  
-ATOM   3032  CD1 LEU B   9      80.741  32.943  16.918  1.00 38.09           C  
-ATOM   3033  CD2 LEU B   9      82.289  31.819  18.529  1.00 37.98           C  
-ATOM   3034  N   LYS B  10      81.767  34.612  22.391  1.00 44.03           N  
-ATOM   3035  CA  LYS B  10      82.086  35.825  23.156  1.00 45.79           C  
-ATOM   3036  C   LYS B  10      82.777  36.836  22.233  1.00 46.64           C  
-ATOM   3037  O   LYS B  10      83.443  36.455  21.277  1.00 46.60           O  
-ATOM   3038  CB  LYS B  10      82.993  35.491  24.327  1.00 46.95           C  
-ATOM   3039  CG  LYS B  10      82.377  34.584  25.378  1.00 48.80           C  
-ATOM   3040  CD  LYS B  10      83.364  34.221  26.487  1.00 49.94           C  
-ATOM   3041  CE  LYS B  10      83.916  35.459  27.180  1.00 50.14           C  
-ATOM   3042  NZ  LYS B  10      84.826  35.122  28.314  1.00 50.23           N  
-ATOM   3043  N   PRO B  11      82.575  38.144  22.486  1.00 47.68           N  
-ATOM   3044  CA  PRO B  11      83.188  39.180  21.656  1.00 48.51           C  
-ATOM   3045  C   PRO B  11      84.687  39.226  21.852  1.00 49.26           C  
-ATOM   3046  O   PRO B  11      85.216  39.109  22.970  1.00 48.80           O  
-ATOM   3047  CB  PRO B  11      82.501  40.457  22.139  1.00 48.42           C  
-ATOM   3048  CG  PRO B  11      82.190  40.151  23.545  1.00 48.17           C  
-ATOM   3049  CD  PRO B  11      81.655  38.747  23.447  1.00 47.72           C  
-ATOM   3050  N   GLN B  12      85.369  39.486  20.762  1.00 50.83           N  
-ATOM   3051  CA  GLN B  12      86.820  39.517  20.811  1.00 52.22           C  
-ATOM   3052  C   GLN B  12      87.361  40.952  20.872  1.00 53.18           C  
-ATOM   3053  O   GLN B  12      86.655  41.881  20.551  1.00 53.03           O  
-ATOM   3054  CB  GLN B  12      87.363  38.681  19.627  1.00 51.26           C  
-ATOM   3055  CG  GLN B  12      86.717  37.266  19.524  1.00 51.03           C  
-ATOM   3056  CD  GLN B  12      87.194  36.291  20.626  1.00 51.03           C  
-ATOM   3057  OE1 GLN B  12      88.128  36.597  21.381  1.00 50.93           O  
-ATOM   3058  NE2 GLN B  12      86.607  35.087  20.660  1.00 51.84           N  
-ATOM   3059  N   ALA B  13      88.542  41.120  21.481  1.00 54.24           N  
-ATOM   3060  CA  ALA B  13      89.199  42.413  21.589  1.00 55.14           C  
-ATOM   3061  C   ALA B  13      89.862  42.678  20.235  1.00 55.88           C  
-ATOM   3062  O   ALA B  13      90.673  41.857  19.740  1.00 55.62           O  
-ATOM   3063  CB  ALA B  13      90.237  42.394  22.714  1.00 55.46           C  
-ATOM   3064  N   PRO B  14      89.542  43.834  19.627  1.00 57.03           N  
-ATOM   3065  CA  PRO B  14      90.071  44.275  18.328  1.00 57.28           C  
-ATOM   3066  C   PRO B  14      91.574  44.557  18.344  1.00 57.21           C  
-ATOM   3067  O   PRO B  14      92.188  44.655  19.411  1.00 57.02           O  
-ATOM   3068  CB  PRO B  14      89.286  45.554  18.055  1.00 57.41           C  
-ATOM   3069  CG  PRO B  14      88.006  45.364  18.814  1.00 57.60           C  
-ATOM   3070  CD  PRO B  14      88.508  44.782  20.100  1.00 57.52           C  
-ATOM   3071  N   ASP B  15      92.153  44.715  17.164  1.00 57.43           N  
-ATOM   3072  CA  ASP B  15      93.580  45.014  17.046  1.00 57.30           C  
-ATOM   3073  C   ASP B  15      93.768  46.523  17.184  1.00 57.85           C  
-ATOM   3074  O   ASP B  15      93.413  47.292  16.289  1.00 57.53           O  
-ATOM   3075  CB  ASP B  15      94.127  44.534  15.692  1.00 56.55           C  
-ATOM   3076  CG  ASP B  15      95.653  44.516  15.642  1.00 55.77           C  
-ATOM   3077  OD1 ASP B  15      96.290  45.538  15.976  1.00 55.29           O  
-ATOM   3078  OD2 ASP B  15      96.218  43.473  15.251  1.00 55.51           O  
-ATOM   3079  N   LYS B  16      94.321  46.929  18.321  1.00 58.47           N  
-ATOM   3080  CA  LYS B  16      94.583  48.334  18.627  1.00 59.15           C  
-ATOM   3081  C   LYS B  16      95.277  49.131  17.515  1.00 59.24           C  
-ATOM   3082  O   LYS B  16      94.800  50.197  17.124  1.00 59.41           O  
-ATOM   3083  CB  LYS B  16      95.382  48.458  19.937  1.00 59.89           C  
-ATOM   3084  CG  LYS B  16      96.111  47.184  20.388  1.00 61.00           C  
-ATOM   3085  CD  LYS B  16      97.098  46.680  19.346  1.00 61.18           C  
-ATOM   3086  CE  LYS B  16      97.385  45.202  19.521  1.00 61.43           C  
-ATOM   3087  NZ  LYS B  16      98.152  44.660  18.362  1.00 60.94           N  
-ATOM   3088  N   ILE B  17      96.382  48.607  16.991  1.00 58.99           N  
-ATOM   3089  CA  ILE B  17      97.124  49.295  15.938  1.00 59.38           C  
-ATOM   3090  C   ILE B  17      96.295  49.417  14.664  1.00 59.51           C  
-ATOM   3091  O   ILE B  17      96.204  50.494  14.071  1.00 59.32           O  
-ATOM   3092  CB  ILE B  17      98.450  48.572  15.599  1.00 59.65           C  
-ATOM   3093  CG1 ILE B  17      99.287  48.367  16.866  1.00 59.71           C  
-ATOM   3094  CG2 ILE B  17      99.246  49.390  14.579  1.00 59.62           C  
-ATOM   3095  CD1 ILE B  17     100.573  47.583  16.643  1.00 59.23           C  
-ATOM   3096  N   LEU B  18      95.682  48.312  14.254  1.00 59.88           N  
-ATOM   3097  CA  LEU B  18      94.866  48.300  13.046  1.00 60.74           C  
-ATOM   3098  C   LEU B  18      93.533  49.017  13.251  1.00 61.39           C  
-ATOM   3099  O   LEU B  18      92.826  49.314  12.287  1.00 61.42           O  
-ATOM   3100  CB  LEU B  18      94.647  46.863  12.557  1.00 60.36           C  
-ATOM   3101  CG  LEU B  18      95.916  46.069  12.218  1.00 59.77           C  
-ATOM   3102  CD1 LEU B  18      95.553  44.646  11.822  1.00 59.39           C  
-ATOM   3103  CD2 LEU B  18      96.698  46.757  11.107  1.00 59.12           C  
-ATOM   3104  N   ALA B  19      93.199  49.299  14.506  1.00 62.35           N  
-ATOM   3105  CA  ALA B  19      91.969  50.010  14.833  1.00 63.69           C  
-ATOM   3106  C   ALA B  19      92.126  51.459  14.370  1.00 64.51           C  
-ATOM   3107  O   ALA B  19      91.225  52.024  13.740  1.00 64.67           O  
-ATOM   3108  CB  ALA B  19      91.707  49.955  16.331  1.00 64.12           C  
-ATOM   3109  N   LEU B  20      93.282  52.048  14.670  1.00 65.08           N  
-ATOM   3110  CA  LEU B  20      93.573  53.419  14.266  1.00 65.81           C  
-ATOM   3111  C   LEU B  20      93.515  53.487  12.746  1.00 66.60           C  
-ATOM   3112  O   LEU B  20      93.026  54.463  12.176  1.00 66.65           O  
-ATOM   3113  CB  LEU B  20      94.969  53.844  14.733  1.00 65.82           C  
-ATOM   3114  CG  LEU B  20      95.275  53.924  16.230  1.00 65.72           C  
-ATOM   3115  CD1 LEU B  20      96.696  54.427  16.412  1.00 65.22           C  
-ATOM   3116  CD2 LEU B  20      94.292  54.850  16.926  1.00 65.86           C  
-ATOM   3117  N   MET B  21      94.004  52.429  12.103  1.00 67.62           N  
-ATOM   3118  CA  MET B  21      94.019  52.323  10.647  1.00 68.53           C  
-ATOM   3119  C   MET B  21      92.620  52.612  10.105  1.00 68.60           C  
-ATOM   3120  O   MET B  21      92.468  53.289   9.084  1.00 68.94           O  
-ATOM   3121  CB  MET B  21      94.480  50.917  10.239  1.00 69.48           C  
-ATOM   3122  CG  MET B  21      94.689  50.707   8.749  1.00 70.88           C  
-ATOM   3123  SD  MET B  21      95.369  49.068   8.385  1.00 72.76           S  
-ATOM   3124  CE  MET B  21      93.854  48.122   8.046  1.00 72.45           C  
-ATOM   3125  N   GLY B  22      91.608  52.130  10.821  1.00 68.33           N  
-ATOM   3126  CA  GLY B  22      90.231  52.354  10.422  1.00 68.12           C  
-ATOM   3127  C   GLY B  22      89.742  53.750  10.775  1.00 67.88           C  
-ATOM   3128  O   GLY B  22      89.002  54.364  10.005  1.00 67.90           O  
-ATOM   3129  N   GLU B  23      90.153  54.249  11.937  1.00 67.47           N  
-ATOM   3130  CA  GLU B  23      89.758  55.579  12.397  1.00 67.43           C  
-ATOM   3131  C   GLU B  23      90.236  56.705  11.482  1.00 67.12           C  
-ATOM   3132  O   GLU B  23      89.501  57.657  11.227  1.00 67.39           O  
-ATOM   3133  CB  GLU B  23      90.275  55.832  13.815  1.00 67.87           C  
-ATOM   3134  CG  GLU B  23      89.657  54.940  14.873  1.00 68.78           C  
-ATOM   3135  CD  GLU B  23      90.167  55.252  16.268  1.00 69.72           C  
-ATOM   3136  OE1 GLU B  23      89.897  56.364  16.774  1.00 69.72           O  
-ATOM   3137  OE2 GLU B  23      90.840  54.381  16.861  1.00 70.55           O  
-ATOM   3138  N   PHE B  24      91.475  56.604  11.012  1.00 66.72           N  
-ATOM   3139  CA  PHE B  24      92.057  57.616  10.133  1.00 65.98           C  
-ATOM   3140  C   PHE B  24      91.151  57.861   8.928  1.00 66.04           C  
-ATOM   3141  O   PHE B  24      91.160  58.945   8.344  1.00 66.49           O  
-ATOM   3142  CB  PHE B  24      93.451  57.168   9.669  1.00 64.94           C  
-ATOM   3143  CG  PHE B  24      94.159  58.162   8.785  1.00 63.30           C  
-ATOM   3144  CD1 PHE B  24      94.777  59.278   9.329  1.00 62.18           C  
-ATOM   3145  CD2 PHE B  24      94.220  57.971   7.406  1.00 63.07           C  
-ATOM   3146  CE1 PHE B  24      95.448  60.187   8.518  1.00 61.91           C  
-ATOM   3147  CE2 PHE B  24      94.890  58.877   6.585  1.00 62.23           C  
-ATOM   3148  CZ  PHE B  24      95.505  59.987   7.142  1.00 61.87           C  
-ATOM   3149  N   GLY B  31      93.409  67.886   8.008  1.00 57.71           N  
-ATOM   3150  CA  GLY B  31      94.797  67.918   8.439  1.00 57.94           C  
-ATOM   3151  C   GLY B  31      95.217  66.677   9.209  1.00 57.59           C  
-ATOM   3152  O   GLY B  31      95.960  66.762  10.190  1.00 58.08           O  
-ATOM   3153  N   LYS B  32      94.733  65.521   8.765  1.00 56.41           N  
-ATOM   3154  CA  LYS B  32      95.054  64.257   9.412  1.00 54.85           C  
-ATOM   3155  C   LYS B  32      96.472  63.812   9.065  1.00 53.99           C  
-ATOM   3156  O   LYS B  32      96.909  63.936   7.915  1.00 54.08           O  
-ATOM   3157  CB  LYS B  32      94.074  63.168   8.979  1.00 54.38           C  
-ATOM   3158  CG  LYS B  32      92.615  63.435   9.299  1.00 53.83           C  
-ATOM   3159  CD  LYS B  32      91.732  62.245   8.909  1.00 52.92           C  
-ATOM   3160  CE  LYS B  32      91.562  62.080   7.392  1.00 51.97           C  
-ATOM   3161  NZ  LYS B  32      92.832  61.864   6.640  1.00 51.14           N  
-ATOM   3162  N   ILE B  33      97.178  63.283  10.061  1.00 52.18           N  
-ATOM   3163  CA  ILE B  33      98.540  62.793   9.890  1.00 49.57           C  
-ATOM   3164  C   ILE B  33      98.607  61.372  10.455  1.00 47.27           C  
-ATOM   3165  O   ILE B  33      98.475  61.165  11.660  1.00 45.80           O  
-ATOM   3166  CB  ILE B  33      99.565  63.703  10.617  1.00 50.14           C  
-ATOM   3167  CG1 ILE B  33      99.440  65.145  10.114  1.00 49.83           C  
-ATOM   3168  CG2 ILE B  33     100.985  63.206  10.374  1.00 50.46           C  
-ATOM   3169  CD1 ILE B  33     100.355  66.121  10.817  1.00 49.72           C  
-ATOM   3170  N   ASP B  34      98.768  60.397   9.566  1.00 45.49           N  
-ATOM   3171  CA  ASP B  34      98.843  58.991   9.956  1.00 43.61           C  
-ATOM   3172  C   ASP B  34     100.272  58.578  10.292  1.00 42.11           C  
-ATOM   3173  O   ASP B  34     101.146  58.550   9.422  1.00 41.14           O  
-ATOM   3174  CB  ASP B  34      98.292  58.097   8.838  1.00 43.93           C  
-ATOM   3175  CG  ASP B  34      98.314  56.613   9.194  1.00 44.00           C  
-ATOM   3176  OD1 ASP B  34      98.244  56.265  10.394  1.00 44.27           O  
-ATOM   3177  OD2 ASP B  34      98.395  55.789   8.258  1.00 44.37           O  
-ATOM   3178  N   LEU B  35     100.483  58.235  11.557  1.00 40.69           N  
-ATOM   3179  CA  LEU B  35     101.781  57.805  12.058  1.00 39.25           C  
-ATOM   3180  C   LEU B  35     101.622  56.488  12.817  1.00 38.35           C  
-ATOM   3181  O   LEU B  35     102.419  56.176  13.704  1.00 38.32           O  
-ATOM   3182  CB  LEU B  35     102.340  58.871  13.006  1.00 39.47           C  
-ATOM   3183  CG  LEU B  35     103.413  59.849  12.515  1.00 40.20           C  
-ATOM   3184  CD1 LEU B  35     103.013  60.502  11.205  1.00 39.99           C  
-ATOM   3185  CD2 LEU B  35     103.658  60.898  13.588  1.00 39.54           C  
-ATOM   3186  N   GLY B  36     100.613  55.704  12.444  1.00 37.40           N  
-ATOM   3187  CA  GLY B  36     100.353  54.448  13.128  1.00 35.84           C  
-ATOM   3188  C   GLY B  36     100.965  53.184  12.547  1.00 35.76           C  
-ATOM   3189  O   GLY B  36     102.152  52.905  12.747  1.00 35.68           O  
-ATOM   3190  N   VAL B  37     100.144  52.420  11.826  1.00 34.80           N  
-ATOM   3191  CA  VAL B  37     100.553  51.152  11.227  1.00 32.51           C  
-ATOM   3192  C   VAL B  37     101.942  51.189  10.588  1.00 30.50           C  
-ATOM   3193  O   VAL B  37     102.293  52.126   9.871  1.00 28.76           O  
-ATOM   3194  CB  VAL B  37      99.475  50.608  10.234  1.00 32.69           C  
-ATOM   3195  CG1 VAL B  37      99.379  51.483   8.992  1.00 33.24           C  
-ATOM   3196  CG2 VAL B  37      99.770  49.160   9.862  1.00 33.17           C  
-ATOM   3197  N   GLY B  38     102.723  50.157  10.886  1.00 29.25           N  
-ATOM   3198  CA  GLY B  38     104.080  50.041  10.397  1.00 28.35           C  
-ATOM   3199  C   GLY B  38     104.246  49.702   8.937  1.00 27.67           C  
-ATOM   3200  O   GLY B  38     104.781  48.648   8.581  1.00 27.50           O  
-ATOM   3201  N   VAL B  39     103.789  50.606   8.085  1.00 26.92           N  
-ATOM   3202  CA  VAL B  39     103.906  50.433   6.652  1.00 26.17           C  
-ATOM   3203  C   VAL B  39     104.768  51.586   6.166  1.00 26.13           C  
-ATOM   3204  O   VAL B  39     104.723  52.679   6.733  1.00 25.95           O  
-ATOM   3205  CB  VAL B  39     102.520  50.481   5.971  1.00 26.54           C  
-ATOM   3206  CG1 VAL B  39     102.670  50.737   4.495  1.00 26.96           C  
-ATOM   3207  CG2 VAL B  39     101.786  49.165   6.183  1.00 25.77           C  
-ATOM   3208  N   TYR B  40     105.616  51.325   5.181  1.00 25.83           N  
-ATOM   3209  CA  TYR B  40     106.454  52.376   4.643  1.00 26.64           C  
-ATOM   3210  C   TYR B  40     105.619  53.277   3.728  1.00 27.61           C  
-ATOM   3211  O   TYR B  40     104.814  52.794   2.931  1.00 27.40           O  
-ATOM   3212  CB  TYR B  40     107.645  51.792   3.871  1.00 25.82           C  
-ATOM   3213  CG  TYR B  40     108.385  52.847   3.086  1.00 24.44           C  
-ATOM   3214  CD1 TYR B  40     109.106  53.844   3.735  1.00 23.96           C  
-ATOM   3215  CD2 TYR B  40     108.282  52.906   1.703  1.00 23.78           C  
-ATOM   3216  CE1 TYR B  40     109.689  54.879   3.026  1.00 23.69           C  
-ATOM   3217  CE2 TYR B  40     108.864  53.936   0.988  1.00 24.22           C  
-ATOM   3218  CZ  TYR B  40     109.560  54.920   1.656  1.00 23.86           C  
-ATOM   3219  OH  TYR B  40     110.086  55.973   0.948  1.00 26.81           O  
-ATOM   3220  N   LYS B  41     105.810  54.584   3.857  1.00 28.49           N  
-ATOM   3221  CA  LYS B  41     105.096  55.553   3.039  1.00 29.84           C  
-ATOM   3222  C   LYS B  41     106.114  56.527   2.467  1.00 30.77           C  
-ATOM   3223  O   LYS B  41     107.161  56.760   3.077  1.00 30.83           O  
-ATOM   3224  CB  LYS B  41     104.067  56.321   3.877  1.00 30.49           C  
-ATOM   3225  CG  LYS B  41     102.908  55.476   4.383  1.00 32.38           C  
-ATOM   3226  CD  LYS B  41     101.789  56.329   4.965  1.00 33.79           C  
-ATOM   3227  CE  LYS B  41     102.214  57.005   6.256  1.00 36.11           C  
-ATOM   3228  NZ  LYS B  41     102.479  56.028   7.359  1.00 36.87           N  
-ATOM   3229  N   ASP B  42     105.837  57.058   1.279  1.00 31.82           N  
-ATOM   3230  CA  ASP B  42     106.739  58.017   0.654  1.00 32.52           C  
-ATOM   3231  C   ASP B  42     106.289  59.459   0.918  1.00 33.15           C  
-ATOM   3232  O   ASP B  42     105.246  59.690   1.531  1.00 32.78           O  
-ATOM   3233  CB  ASP B  42     106.914  57.737  -0.858  1.00 31.95           C  
-ATOM   3234  CG  ASP B  42     105.663  58.036  -1.694  1.00 31.54           C  
-ATOM   3235  OD1 ASP B  42     104.662  58.571  -1.175  1.00 30.46           O  
-ATOM   3236  OD2 ASP B  42     105.693  57.737  -2.909  1.00 31.88           O  
-ATOM   3237  N   ALA B  43     107.050  60.413   0.394  1.00 33.73           N  
-ATOM   3238  CA  ALA B  43     106.768  61.833   0.568  1.00 34.47           C  
-ATOM   3239  C   ALA B  43     105.307  62.215   0.344  1.00 34.91           C  
-ATOM   3240  O   ALA B  43     104.788  63.106   1.013  1.00 35.39           O  
-ATOM   3241  CB  ALA B  43     107.667  62.651  -0.348  1.00 34.15           C  
-ATOM   3242  N   THR B  44     104.648  61.545  -0.595  1.00 34.76           N  
-ATOM   3243  CA  THR B  44     103.255  61.845  -0.903  1.00 34.63           C  
-ATOM   3244  C   THR B  44     102.265  60.932  -0.181  1.00 33.77           C  
-ATOM   3245  O   THR B  44     101.145  60.728  -0.654  1.00 34.88           O  
-ATOM   3246  CB  THR B  44     102.998  61.763  -2.420  1.00 35.78           C  
-ATOM   3247  OG1 THR B  44     103.227  60.421  -2.874  1.00 37.91           O  
-ATOM   3248  CG2 THR B  44     103.927  62.702  -3.170  1.00 36.14           C  
-ATOM   3249  N   GLY B  45     102.687  60.355   0.938  1.00 32.25           N  
-ATOM   3250  CA  GLY B  45     101.816  59.476   1.698  1.00 30.46           C  
-ATOM   3251  C   GLY B  45     101.371  58.209   0.990  1.00 29.37           C  
-ATOM   3252  O   GLY B  45     100.317  57.658   1.291  1.00 29.85           O  
-ATOM   3253  N   HIS B  46     102.173  57.724   0.059  1.00 28.71           N  
-ATOM   3254  CA  HIS B  46     101.815  56.510  -0.658  1.00 28.44           C  
-ATOM   3255  C   HIS B  46     102.793  55.386  -0.382  1.00 26.23           C  
-ATOM   3256  O   HIS B  46     103.981  55.626  -0.192  1.00 25.40           O  
-ATOM   3257  CB  HIS B  46     101.778  56.764  -2.165  1.00 31.45           C  
-ATOM   3258  CG  HIS B  46     100.670  57.670  -2.597  1.00 35.76           C  
-ATOM   3259  ND1 HIS B  46     100.863  59.007  -2.872  1.00 36.81           N  
-ATOM   3260  CD2 HIS B  46      99.352  57.433  -2.798  1.00 37.83           C  
-ATOM   3261  CE1 HIS B  46      99.714  59.555  -3.223  1.00 37.71           C  
-ATOM   3262  NE2 HIS B  46      98.781  58.622  -3.186  1.00 38.44           N  
-ATOM   3263  N   THR B  47     102.270  54.167  -0.311  1.00 24.40           N  
-ATOM   3264  CA  THR B  47     103.079  52.968  -0.125  1.00 21.74           C  
-ATOM   3265  C   THR B  47     103.150  52.387  -1.533  1.00 21.79           C  
-ATOM   3266  O   THR B  47     102.215  51.737  -1.994  1.00 21.63           O  
-ATOM   3267  CB  THR B  47     102.389  51.991   0.814  1.00 20.12           C  
-ATOM   3268  OG1 THR B  47     102.157  52.638   2.072  1.00 18.66           O  
-ATOM   3269  CG2 THR B  47     103.244  50.752   1.017  1.00 19.35           C  
-ATOM   3270  N   PRO B  48     104.225  52.697  -2.270  1.00 21.75           N  
-ATOM   3271  CA  PRO B  48     104.379  52.202  -3.637  1.00 21.79           C  
-ATOM   3272  C   PRO B  48     104.833  50.761  -3.782  1.00 21.75           C  
-ATOM   3273  O   PRO B  48     105.226  50.104  -2.817  1.00 21.85           O  
-ATOM   3274  CB  PRO B  48     105.426  53.151  -4.208  1.00 21.87           C  
-ATOM   3275  CG  PRO B  48     106.329  53.346  -3.047  1.00 21.55           C  
-ATOM   3276  CD  PRO B  48     105.361  53.565  -1.904  1.00 21.34           C  
-ATOM   3277  N   ILE B  49     104.759  50.281  -5.015  1.00 21.10           N  
-ATOM   3278  CA  ILE B  49     105.199  48.941  -5.348  1.00 20.87           C  
-ATOM   3279  C   ILE B  49     106.635  49.146  -5.829  1.00 20.78           C  
-ATOM   3280  O   ILE B  49     106.902  50.033  -6.643  1.00 20.28           O  
-ATOM   3281  CB  ILE B  49     104.355  48.335  -6.487  1.00 20.45           C  
-ATOM   3282  CG1 ILE B  49     102.874  48.319  -6.088  1.00 21.24           C  
-ATOM   3283  CG2 ILE B  49     104.849  46.933  -6.811  1.00 19.85           C  
-ATOM   3284  CD1 ILE B  49     101.941  47.837  -7.184  1.00 20.32           C  
-ATOM   3285  N   MET B  50     107.565  48.383  -5.274  1.00 20.39           N  
-ATOM   3286  CA  MET B  50     108.965  48.492  -5.656  1.00 20.26           C  
-ATOM   3287  C   MET B  50     109.188  48.122  -7.123  1.00 20.24           C  
-ATOM   3288  O   MET B  50     108.591  47.173  -7.632  1.00 20.73           O  
-ATOM   3289  CB  MET B  50     109.821  47.632  -4.729  1.00 19.65           C  
-ATOM   3290  CG  MET B  50     109.660  48.027  -3.272  1.00 19.83           C  
-ATOM   3291  SD  MET B  50     110.746  47.181  -2.128  1.00 21.01           S  
-ATOM   3292  CE  MET B  50     112.021  48.435  -1.915  1.00 21.24           C  
-ATOM   3293  N   ARG B  51     110.036  48.889  -7.800  1.00 20.01           N  
-ATOM   3294  CA  ARG B  51     110.340  48.661  -9.210  1.00 20.14           C  
-ATOM   3295  C   ARG B  51     110.606  47.195  -9.571  1.00 19.88           C  
-ATOM   3296  O   ARG B  51     109.972  46.654 -10.481  1.00 20.28           O  
-ATOM   3297  CB  ARG B  51     111.522  49.531  -9.649  1.00 20.10           C  
-ATOM   3298  CG  ARG B  51     111.286  51.022  -9.497  1.00 22.40           C  
-ATOM   3299  CD  ARG B  51     112.495  51.833  -9.954  1.00 24.30           C  
-ATOM   3300  NE  ARG B  51     113.671  51.577  -9.124  1.00 26.38           N  
-ATOM   3301  CZ  ARG B  51     114.035  52.316  -8.079  1.00 26.13           C  
-ATOM   3302  NH1 ARG B  51     113.332  53.386  -7.732  1.00 26.64           N  
-ATOM   3303  NH2 ARG B  51     115.117  51.991  -7.385  1.00 26.47           N  
-ATOM   3304  N   ALA B  52     111.526  46.554  -8.853  1.00 19.16           N  
-ATOM   3305  CA  ALA B  52     111.882  45.153  -9.104  1.00 18.58           C  
-ATOM   3306  C   ALA B  52     110.702  44.211  -8.894  1.00 17.63           C  
-ATOM   3307  O   ALA B  52     110.551  43.223  -9.607  1.00 17.72           O  
-ATOM   3308  CB  ALA B  52     113.056  44.736  -8.218  1.00 17.32           C  
-ATOM   3309  N   VAL B  53     109.870  44.517  -7.908  1.00 17.24           N  
-ATOM   3310  CA  VAL B  53     108.708  43.697  -7.625  1.00 17.38           C  
-ATOM   3311  C   VAL B  53     107.758  43.756  -8.815  1.00 18.53           C  
-ATOM   3312  O   VAL B  53     107.266  42.726  -9.283  1.00 19.60           O  
-ATOM   3313  CB  VAL B  53     107.995  44.165  -6.330  1.00 17.01           C  
-ATOM   3314  CG1 VAL B  53     106.621  43.498  -6.191  1.00 16.41           C  
-ATOM   3315  CG2 VAL B  53     108.862  43.837  -5.117  1.00 15.72           C  
-ATOM   3316  N   HIS B  54     107.557  44.958  -9.345  1.00 19.60           N  
-ATOM   3317  CA  HIS B  54     106.670  45.145 -10.484  1.00 19.83           C  
-ATOM   3318  C   HIS B  54     107.177  44.394 -11.706  1.00 20.22           C  
-ATOM   3319  O   HIS B  54     106.402  43.719 -12.392  1.00 21.60           O  
-ATOM   3320  CB  HIS B  54     106.512  46.625 -10.820  1.00 20.57           C  
-ATOM   3321  CG  HIS B  54     105.492  46.887 -11.880  1.00 21.57           C  
-ATOM   3322  ND1 HIS B  54     105.824  47.187 -13.185  1.00 22.24           N  
-ATOM   3323  CD2 HIS B  54     104.139  46.862 -11.836  1.00 21.02           C  
-ATOM   3324  CE1 HIS B  54     104.721  47.335 -13.894  1.00 22.01           C  
-ATOM   3325  NE2 HIS B  54     103.685  47.143 -13.099  1.00 22.62           N  
-ATOM   3326  N   ALA B  55     108.475  44.511 -11.969  1.00 19.73           N  
-ATOM   3327  CA  ALA B  55     109.099  43.840 -13.109  1.00 18.96           C  
-ATOM   3328  C   ALA B  55     108.992  42.332 -12.938  1.00 18.82           C  
-ATOM   3329  O   ALA B  55     108.831  41.598 -13.915  1.00 19.05           O  
-ATOM   3330  CB  ALA B  55     110.563  44.255 -13.234  1.00 17.67           C  
-ATOM   3331  N   ALA B  56     109.088  41.878 -11.693  1.00 18.68           N  
-ATOM   3332  CA  ALA B  56     108.997  40.461 -11.377  1.00 19.17           C  
-ATOM   3333  C   ALA B  56     107.601  39.934 -11.717  1.00 20.14           C  
-ATOM   3334  O   ALA B  56     107.461  38.870 -12.324  1.00 20.60           O  
-ATOM   3335  CB  ALA B  56     109.312  40.233  -9.911  1.00 19.03           C  
-ATOM   3336  N   GLU B  57     106.570  40.686 -11.341  1.00 20.73           N  
-ATOM   3337  CA  GLU B  57     105.199  40.290 -11.637  1.00 21.36           C  
-ATOM   3338  C   GLU B  57     104.951  40.242 -13.140  1.00 22.61           C  
-ATOM   3339  O   GLU B  57     104.219  39.379 -13.627  1.00 22.31           O  
-ATOM   3340  CB  GLU B  57     104.206  41.234 -10.971  1.00 20.96           C  
-ATOM   3341  CG  GLU B  57     104.061  41.015  -9.479  1.00 21.67           C  
-ATOM   3342  CD  GLU B  57     102.944  41.842  -8.872  1.00 22.50           C  
-ATOM   3343  OE1 GLU B  57     102.882  43.057  -9.135  1.00 22.65           O  
-ATOM   3344  OE2 GLU B  57     102.117  41.272  -8.133  1.00 23.48           O  
-ATOM   3345  N   GLN B  58     105.563  41.171 -13.869  1.00 24.27           N  
-ATOM   3346  CA  GLN B  58     105.423  41.233 -15.321  1.00 26.14           C  
-ATOM   3347  C   GLN B  58     106.057  40.007 -15.963  1.00 26.17           C  
-ATOM   3348  O   GLN B  58     105.534  39.457 -16.937  1.00 26.65           O  
-ATOM   3349  CB  GLN B  58     106.093  42.491 -15.877  1.00 28.30           C  
-ATOM   3350  CG  GLN B  58     105.445  43.791 -15.454  1.00 33.15           C  
-ATOM   3351  CD  GLN B  58     106.102  45.002 -16.093  1.00 36.05           C  
-ATOM   3352  OE1 GLN B  58     106.610  45.888 -15.400  1.00 37.60           O  
-ATOM   3353  NE2 GLN B  58     106.078  45.058 -17.421  1.00 37.34           N  
-ATOM   3354  N   ARG B  59     107.192  39.589 -15.416  1.00 25.59           N  
-ATOM   3355  CA  ARG B  59     107.905  38.433 -15.927  1.00 26.04           C  
-ATOM   3356  C   ARG B  59     107.129  37.168 -15.613  1.00 24.85           C  
-ATOM   3357  O   ARG B  59     107.006  36.281 -16.456  1.00 24.19           O  
-ATOM   3358  CB  ARG B  59     109.320  38.395 -15.335  1.00 28.63           C  
-ATOM   3359  CG  ARG B  59     110.137  39.621 -15.752  1.00 33.13           C  
-ATOM   3360  CD  ARG B  59     111.480  39.764 -15.040  1.00 36.17           C  
-ATOM   3361  NE  ARG B  59     112.126  41.033 -15.388  1.00 38.52           N  
-ATOM   3362  CZ  ARG B  59     113.440  41.201 -15.534  1.00 39.25           C  
-ATOM   3363  NH1 ARG B  59     114.266  40.178 -15.363  1.00 39.27           N  
-ATOM   3364  NH2 ARG B  59     113.930  42.394 -15.853  1.00 39.03           N  
-ATOM   3365  N   MET B  60     106.540  37.125 -14.422  1.00 24.43           N  
-ATOM   3366  CA  MET B  60     105.752  35.974 -13.981  1.00 23.94           C  
-ATOM   3367  C   MET B  60     104.538  35.725 -14.866  1.00 23.58           C  
-ATOM   3368  O   MET B  60     104.232  34.582 -15.196  1.00 23.20           O  
-ATOM   3369  CB  MET B  60     105.299  36.162 -12.536  1.00 23.65           C  
-ATOM   3370  CG  MET B  60     106.410  36.011 -11.514  1.00 23.28           C  
-ATOM   3371  SD  MET B  60     105.834  36.493  -9.889  1.00 23.39           S  
-ATOM   3372  CE  MET B  60     104.371  35.459  -9.731  1.00 23.00           C  
-ATOM   3373  N   LEU B  61     103.863  36.797 -15.268  1.00 24.24           N  
-ATOM   3374  CA  LEU B  61     102.686  36.680 -16.119  1.00 25.71           C  
-ATOM   3375  C   LEU B  61     103.029  35.978 -17.434  1.00 26.30           C  
-ATOM   3376  O   LEU B  61     102.229  35.190 -17.948  1.00 26.98           O  
-ATOM   3377  CB  LEU B  61     102.106  38.061 -16.421  1.00 25.67           C  
-ATOM   3378  CG  LEU B  61     100.595  38.266 -16.273  1.00 27.41           C  
-ATOM   3379  CD1 LEU B  61     100.223  39.597 -16.905  1.00 28.41           C  
-ATOM   3380  CD2 LEU B  61      99.814  37.155 -16.938  1.00 26.77           C  
-ATOM   3381  N   GLU B  62     104.213  36.264 -17.969  1.00 25.96           N  
-ATOM   3382  CA  GLU B  62     104.657  35.670 -19.225  1.00 25.85           C  
-ATOM   3383  C   GLU B  62     105.148  34.236 -19.111  1.00 25.39           C  
-ATOM   3384  O   GLU B  62     104.975  33.450 -20.035  1.00 25.43           O  
-ATOM   3385  CB  GLU B  62     105.794  36.489 -19.843  1.00 26.73           C  
-ATOM   3386  CG  GLU B  62     105.390  37.758 -20.570  1.00 28.46           C  
-ATOM   3387  CD  GLU B  62     106.548  38.381 -21.358  1.00 29.79           C  
-ATOM   3388  OE1 GLU B  62     107.655  37.794 -21.389  1.00 30.52           O  
-ATOM   3389  OE2 GLU B  62     106.350  39.459 -21.955  1.00 29.72           O  
-ATOM   3390  N   THR B  63     105.792  33.909 -17.997  1.00 24.88           N  
-ATOM   3391  CA  THR B  63     106.366  32.585 -17.817  1.00 24.77           C  
-ATOM   3392  C   THR B  63     105.528  31.466 -17.205  1.00 25.80           C  
-ATOM   3393  O   THR B  63     105.729  30.294 -17.534  1.00 26.68           O  
-ATOM   3394  CB  THR B  63     107.714  32.676 -17.076  1.00 24.45           C  
-ATOM   3395  OG1 THR B  63     107.558  33.451 -15.882  1.00 24.60           O  
-ATOM   3396  CG2 THR B  63     108.764  33.333 -17.960  1.00 23.67           C  
-ATOM   3397  N   GLU B  64     104.610  31.796 -16.306  1.00 26.06           N  
-ATOM   3398  CA  GLU B  64     103.787  30.767 -15.674  1.00 25.56           C  
-ATOM   3399  C   GLU B  64     102.753  30.159 -16.622  1.00 24.78           C  
-ATOM   3400  O   GLU B  64     101.940  30.866 -17.208  1.00 24.66           O  
-ATOM   3401  CB  GLU B  64     103.111  31.319 -14.422  1.00 26.83           C  
-ATOM   3402  CG  GLU B  64     104.094  31.844 -13.377  1.00 28.84           C  
-ATOM   3403  CD  GLU B  64     105.141  30.818 -12.987  1.00 30.70           C  
-ATOM   3404  OE1 GLU B  64     104.774  29.797 -12.364  1.00 30.73           O  
-ATOM   3405  OE2 GLU B  64     106.335  31.029 -13.310  1.00 32.45           O  
-ATOM   3406  N   THR B  66     102.783  28.836 -16.743  1.00 24.09           N  
-ATOM   3407  CA  THR B  66     101.876  28.097 -17.615  1.00 22.97           C  
-ATOM   3408  C   THR B  66     100.819  27.292 -16.861  1.00 21.95           C  
-ATOM   3409  O   THR B  66      99.885  26.759 -17.467  1.00 22.73           O  
-ATOM   3410  CB  THR B  66     102.661  27.119 -18.502  1.00 23.45           C  
-ATOM   3411  OG1 THR B  66     103.562  26.350 -17.690  1.00 22.90           O  
-ATOM   3412  CG2 THR B  66     103.439  27.876 -19.561  1.00 23.61           C  
-ATOM   3413  N   THR B  67     100.976  27.192 -15.547  1.00 20.68           N  
-ATOM   3414  CA  THR B  67     100.048  26.439 -14.722  1.00 18.67           C  
-ATOM   3415  C   THR B  67      99.981  27.010 -13.316  1.00 18.72           C  
-ATOM   3416  O   THR B  67     100.863  27.767 -12.892  1.00 18.81           O  
-ATOM   3417  CB  THR B  67     100.477  24.969 -14.618  1.00 18.39           C  
-ATOM   3418  OG1 THR B  67      99.465  24.234 -13.929  1.00 18.74           O  
-ATOM   3419  CG2 THR B  67     101.789  24.839 -13.848  1.00 16.55           C  
-ATOM   3420  N   LYS B  68      98.916  26.659 -12.606  1.00 18.85           N  
-ATOM   3421  CA  LYS B  68      98.715  27.099 -11.234  1.00 18.00           C  
-ATOM   3422  C   LYS B  68      98.363  25.913 -10.340  1.00 18.30           C  
-ATOM   3423  O   LYS B  68      97.714  26.087  -9.302  1.00 18.33           O  
-ATOM   3424  CB  LYS B  68      97.622  28.170 -11.153  1.00 17.14           C  
-ATOM   3425  CG  LYS B  68      98.063  29.562 -11.601  1.00 15.52           C  
-ATOM   3426  CD  LYS B  68      96.927  30.569 -11.460  1.00 13.76           C  
-ATOM   3427  CE  LYS B  68      97.277  31.910 -12.081  1.00 13.32           C  
-ATOM   3428  NZ  LYS B  68      98.331  32.668 -11.339  1.00 11.94           N  
-ATOM   3429  N   THR B  69      98.803  24.717 -10.736  1.00 18.22           N  
-ATOM   3430  CA  THR B  69      98.545  23.499  -9.969  1.00 18.91           C  
-ATOM   3431  C   THR B  69      99.208  23.595  -8.609  1.00 19.36           C  
-ATOM   3432  O   THR B  69     100.018  24.485  -8.363  1.00 20.03           O  
-ATOM   3433  CB  THR B  69      99.160  22.249 -10.616  1.00 19.03           C  
-ATOM   3434  OG1 THR B  69      99.624  22.549 -11.931  1.00 22.09           O  
-ATOM   3435  CG2 THR B  69      98.148  21.138 -10.678  1.00 18.81           C  
-ATOM   3436  N   TYR B  70      98.887  22.646  -7.740  1.00 19.73           N  
-ATOM   3437  CA  TYR B  70      99.474  22.598  -6.414  1.00 20.14           C  
-ATOM   3438  C   TYR B  70     100.977  22.445  -6.576  1.00 20.65           C  
-ATOM   3439  O   TYR B  70     101.437  21.778  -7.504  1.00 20.08           O  
-ATOM   3440  CB  TYR B  70      98.907  21.416  -5.639  1.00 19.68           C  
-ATOM   3441  CG  TYR B  70      97.449  21.578  -5.301  1.00 19.58           C  
-ATOM   3442  CD1 TYR B  70      97.014  22.647  -4.518  1.00 18.04           C  
-ATOM   3443  CD2 TYR B  70      96.507  20.650  -5.732  1.00 18.93           C  
-ATOM   3444  CE1 TYR B  70      95.684  22.780  -4.168  1.00 18.87           C  
-ATOM   3445  CE2 TYR B  70      95.172  20.774  -5.385  1.00 18.92           C  
-ATOM   3446  CZ  TYR B  70      94.767  21.840  -4.601  1.00 18.56           C  
-ATOM   3447  OH  TYR B  70      93.448  21.958  -4.231  1.00 20.07           O  
-ATOM   3448  N   ALA B  71     101.728  23.084  -5.687  1.00 21.39           N  
-ATOM   3449  CA  ALA B  71     103.180  23.048  -5.728  1.00 22.45           C  
-ATOM   3450  C   ALA B  71     103.724  22.417  -4.443  1.00 23.69           C  
-ATOM   3451  O   ALA B  71     103.182  21.422  -3.960  1.00 24.80           O  
-ATOM   3452  CB  ALA B  71     103.724  24.457  -5.925  1.00 21.67           C  
-ATOM   3453  N   GLY B  72     104.789  22.987  -3.889  1.00 24.12           N  
-ATOM   3454  CA  GLY B  72     105.371  22.439  -2.677  1.00 24.02           C  
-ATOM   3455  C   GLY B  72     104.639  22.778  -1.391  1.00 24.33           C  
-ATOM   3456  O   GLY B  72     104.310  23.941  -1.138  1.00 24.68           O  
-ATOM   3457  N   LEU B  73     104.465  21.769  -0.543  1.00 24.09           N  
-ATOM   3458  CA  LEU B  73     103.787  21.909   0.736  1.00 24.31           C  
-ATOM   3459  C   LEU B  73     104.595  22.768   1.712  1.00 24.37           C  
-ATOM   3460  O   LEU B  73     104.028  23.419   2.588  1.00 25.13           O  
-ATOM   3461  CB  LEU B  73     103.532  20.525   1.337  1.00 25.26           C  
-ATOM   3462  CG  LEU B  73     102.725  20.443   2.632  1.00 26.71           C  
-ATOM   3463  CD1 LEU B  73     101.320  20.984   2.401  1.00 27.60           C  
-ATOM   3464  CD2 LEU B  73     102.673  19.001   3.124  1.00 26.32           C  
-ATOM   3465  N   SER B  74     105.915  22.762   1.558  1.00 24.58           N  
-ATOM   3466  CA  SER B  74     106.816  23.547   2.409  1.00 25.24           C  
-ATOM   3467  C   SER B  74     107.309  24.805   1.688  1.00 24.96           C  
-ATOM   3468  O   SER B  74     108.121  25.565   2.226  1.00 25.27           O  
-ATOM   3469  CB  SER B  74     108.035  22.709   2.822  1.00 24.85           C  
-ATOM   3470  OG  SER B  74     107.666  21.576   3.592  1.00 26.49           O  
-ATOM   3471  N   GLY B  75     106.801  25.031   0.481  1.00 25.21           N  
-ATOM   3472  CA  GLY B  75     107.229  26.173  -0.306  1.00 24.25           C  
-ATOM   3473  C   GLY B  75     108.153  25.687  -1.407  1.00 24.21           C  
-ATOM   3474  O   GLY B  75     108.536  24.514  -1.432  1.00 24.50           O  
-ATOM   3475  N   GLU B  76     108.495  26.573  -2.330  1.00 24.01           N  
-ATOM   3476  CA  GLU B  76     109.363  26.221  -3.442  1.00 25.10           C  
-ATOM   3477  C   GLU B  76     110.831  26.275  -3.044  1.00 25.11           C  
-ATOM   3478  O   GLU B  76     111.245  27.159  -2.290  1.00 24.68           O  
-ATOM   3479  CB  GLU B  76     109.116  27.154  -4.631  1.00 26.22           C  
-ATOM   3480  CG  GLU B  76     107.651  27.316  -5.014  1.00 28.53           C  
-ATOM   3481  CD  GLU B  76     106.960  25.992  -5.273  1.00 30.08           C  
-ATOM   3482  OE1 GLU B  76     106.972  25.527  -6.433  1.00 32.84           O  
-ATOM   3483  OE2 GLU B  76     106.404  25.410  -4.319  1.00 29.86           O  
-ATOM   3484  N   PRO B  77     111.642  25.341  -3.573  1.00 25.65           N  
-ATOM   3485  CA  PRO B  77     113.082  25.247  -3.297  1.00 25.95           C  
-ATOM   3486  C   PRO B  77     113.775  26.584  -3.534  1.00 25.43           C  
-ATOM   3487  O   PRO B  77     114.580  27.033  -2.718  1.00 25.56           O  
-ATOM   3488  CB  PRO B  77     113.547  24.194  -4.304  1.00 26.07           C  
-ATOM   3489  CG  PRO B  77     112.370  23.286  -4.398  1.00 26.54           C  
-ATOM   3490  CD  PRO B  77     111.216  24.263  -4.486  1.00 26.03           C  
-ATOM   3491  N   GLU B  78     113.422  27.221  -4.649  1.00 25.33           N  
-ATOM   3492  CA  GLU B  78     113.972  28.518  -5.041  1.00 24.11           C  
-ATOM   3493  C   GLU B  78     113.765  29.532  -3.915  1.00 22.28           C  
-ATOM   3494  O   GLU B  78     114.700  30.209  -3.504  1.00 22.57           O  
-ATOM   3495  CB  GLU B  78     113.283  29.032  -6.315  1.00 27.10           C  
-ATOM   3496  CG  GLU B  78     112.504  27.970  -7.120  1.00 32.69           C  
-ATOM   3497  CD  GLU B  78     111.042  28.358  -7.410  1.00 34.82           C  
-ATOM   3498  OE1 GLU B  78     110.622  29.493  -7.093  1.00 35.92           O  
-ATOM   3499  OE2 GLU B  78     110.305  27.512  -7.960  1.00 37.67           O  
-ATOM   3500  N   PHE B  79     112.540  29.615  -3.403  1.00 20.15           N  
-ATOM   3501  CA  PHE B  79     112.218  30.549  -2.330  1.00 18.62           C  
-ATOM   3502  C   PHE B  79     112.989  30.229  -1.061  1.00 19.15           C  
-ATOM   3503  O   PHE B  79     113.607  31.108  -0.453  1.00 19.59           O  
-ATOM   3504  CB  PHE B  79     110.712  30.530  -2.036  1.00 16.82           C  
-ATOM   3505  CG  PHE B  79     110.292  31.459  -0.924  1.00 15.36           C  
-ATOM   3506  CD1 PHE B  79     110.347  32.840  -1.088  1.00 13.18           C  
-ATOM   3507  CD2 PHE B  79     109.843  30.950   0.295  1.00 15.78           C  
-ATOM   3508  CE1 PHE B  79     109.966  33.694  -0.059  1.00 12.58           C  
-ATOM   3509  CE2 PHE B  79     109.457  31.806   1.334  1.00 14.62           C  
-ATOM   3510  CZ  PHE B  79     109.522  33.179   1.152  1.00 12.84           C  
-ATOM   3511  N   GLN B  80     112.951  28.963  -0.670  1.00 19.59           N  
-ATOM   3512  CA  GLN B  80     113.622  28.503   0.532  1.00 20.26           C  
-ATOM   3513  C   GLN B  80     115.113  28.812   0.524  1.00 20.99           C  
-ATOM   3514  O   GLN B  80     115.652  29.309   1.517  1.00 21.29           O  
-ATOM   3515  CB  GLN B  80     113.410  27.000   0.706  1.00 20.83           C  
-ATOM   3516  CG  GLN B  80     111.953  26.589   0.858  1.00 22.27           C  
-ATOM   3517  CD  GLN B  80     111.782  25.087   0.839  1.00 24.02           C  
-ATOM   3518  OE1 GLN B  80     112.479  24.384   0.105  1.00 24.93           O  
-ATOM   3519  NE2 GLN B  80     110.865  24.582   1.655  1.00 24.47           N  
-ATOM   3520  N   LYS B  81     115.774  28.528  -0.595  1.00 21.51           N  
-ATOM   3521  CA  LYS B  81     117.206  28.763  -0.711  1.00 21.94           C  
-ATOM   3522  C   LYS B  81     117.554  30.243  -0.700  1.00 20.67           C  
-ATOM   3523  O   LYS B  81     118.385  30.678   0.099  1.00 20.51           O  
-ATOM   3524  CB  LYS B  81     117.772  28.096  -1.965  1.00 24.69           C  
-ATOM   3525  CG  LYS B  81     119.289  28.235  -2.085  1.00 29.60           C  
-ATOM   3526  CD  LYS B  81     119.860  27.347  -3.173  1.00 32.70           C  
-ATOM   3527  CE  LYS B  81     121.380  27.429  -3.207  1.00 34.73           C  
-ATOM   3528  NZ  LYS B  81     121.868  28.757  -3.683  1.00 36.75           N  
-ATOM   3529  N   ALA B  82     116.912  31.014  -1.575  1.00 19.64           N  
-ATOM   3530  CA  ALA B  82     117.160  32.452  -1.662  1.00 18.80           C  
-ATOM   3531  C   ALA B  82     116.991  33.131  -0.305  1.00 17.49           C  
-ATOM   3532  O   ALA B  82     117.845  33.911   0.119  1.00 16.37           O  
-ATOM   3533  CB  ALA B  82     116.238  33.088  -2.694  1.00 19.22           C  
-ATOM   3534  N   MET B  83     115.901  32.806   0.381  1.00 17.76           N  
-ATOM   3535  CA  MET B  83     115.616  33.369   1.698  1.00 17.36           C  
-ATOM   3536  C   MET B  83     116.668  32.949   2.717  1.00 17.15           C  
-ATOM   3537  O   MET B  83     117.115  33.764   3.528  1.00 17.65           O  
-ATOM   3538  CB  MET B  83     114.223  32.945   2.178  1.00 17.05           C  
-ATOM   3539  CG  MET B  83     113.085  33.719   1.536  1.00 16.24           C  
-ATOM   3540  SD  MET B  83     113.179  35.484   1.872  1.00 18.34           S  
-ATOM   3541  CE  MET B  83     112.713  35.511   3.599  1.00 16.01           C  
-ATOM   3542  N   GLY B  84     117.058  31.679   2.681  1.00 16.43           N  
-ATOM   3543  CA  GLY B  84     118.067  31.201   3.607  1.00 16.87           C  
-ATOM   3544  C   GLY B  84     119.364  31.974   3.422  1.00 16.53           C  
-ATOM   3545  O   GLY B  84     120.030  32.342   4.392  1.00 16.54           O  
-ATOM   3546  N   GLU B  85     119.699  32.258   2.168  1.00 16.26           N  
-ATOM   3547  CA  GLU B  85     120.909  32.998   1.843  1.00 17.61           C  
-ATOM   3548  C   GLU B  85     120.810  34.467   2.226  1.00 17.00           C  
-ATOM   3549  O   GLU B  85     121.778  35.049   2.720  1.00 16.16           O  
-ATOM   3550  CB  GLU B  85     121.231  32.850   0.358  1.00 19.05           C  
-ATOM   3551  CG  GLU B  85     121.527  31.405  -0.014  1.00 24.39           C  
-ATOM   3552  CD  GLU B  85     122.014  31.237  -1.429  1.00 26.53           C  
-ATOM   3553  OE1 GLU B  85     121.462  31.891  -2.338  1.00 29.01           O  
-ATOM   3554  OE2 GLU B  85     122.949  30.435  -1.639  1.00 29.33           O  
-ATOM   3555  N   LEU B  86     119.638  35.061   2.008  1.00 16.14           N  
-ATOM   3556  CA  LEU B  86     119.418  36.460   2.344  1.00 16.18           C  
-ATOM   3557  C   LEU B  86     119.622  36.685   3.834  1.00 17.01           C  
-ATOM   3558  O   LEU B  86     120.266  37.646   4.248  1.00 17.52           O  
-ATOM   3559  CB  LEU B  86     117.996  36.893   1.960  1.00 15.75           C  
-ATOM   3560  CG  LEU B  86     117.529  38.297   2.389  1.00 15.55           C  
-ATOM   3561  CD1 LEU B  86     118.388  39.389   1.755  1.00 13.68           C  
-ATOM   3562  CD2 LEU B  86     116.079  38.492   2.005  1.00 15.06           C  
-ATOM   3563  N   ILE B  87     119.095  35.770   4.634  1.00 18.22           N  
-ATOM   3564  CA  ILE B  87     119.180  35.877   6.081  1.00 18.86           C  
-ATOM   3565  C   ILE B  87     120.506  35.449   6.703  1.00 19.83           C  
-ATOM   3566  O   ILE B  87     121.142  36.230   7.407  1.00 19.20           O  
-ATOM   3567  CB  ILE B  87     118.013  35.098   6.738  1.00 19.66           C  
-ATOM   3568  CG1 ILE B  87     116.684  35.700   6.277  1.00 20.18           C  
-ATOM   3569  CG2 ILE B  87     118.123  35.114   8.269  1.00 18.20           C  
-ATOM   3570  CD1 ILE B  87     115.490  34.892   6.681  1.00 22.48           C  
-ATOM   3571  N   LEU B  88     120.916  34.212   6.451  1.00 20.74           N  
-ATOM   3572  CA  LEU B  88     122.144  33.687   7.040  1.00 22.92           C  
-ATOM   3573  C   LEU B  88     123.416  33.879   6.223  1.00 24.09           C  
-ATOM   3574  O   LEU B  88     124.519  33.627   6.713  1.00 23.42           O  
-ATOM   3575  CB  LEU B  88     121.958  32.207   7.390  1.00 22.33           C  
-ATOM   3576  CG  LEU B  88     120.851  31.920   8.414  1.00 22.46           C  
-ATOM   3577  CD1 LEU B  88     120.618  30.420   8.534  1.00 21.88           C  
-ATOM   3578  CD2 LEU B  88     121.217  32.525   9.763  1.00 21.56           C  
-ATOM   3579  N   GLY B  89     123.270  34.334   4.986  1.00 25.95           N  
-ATOM   3580  CA  GLY B  89     124.433  34.529   4.147  1.00 29.26           C  
-ATOM   3581  C   GLY B  89     125.197  33.230   3.973  1.00 31.68           C  
-ATOM   3582  O   GLY B  89     124.607  32.164   3.803  1.00 31.20           O  
-ATOM   3583  N   ASP B  90     126.520  33.311   4.049  1.00 34.86           N  
-ATOM   3584  CA  ASP B  90     127.361  32.126   3.896  1.00 37.37           C  
-ATOM   3585  C   ASP B  90     127.350  31.222   5.120  1.00 37.47           C  
-ATOM   3586  O   ASP B  90     128.025  30.194   5.143  1.00 38.63           O  
-ATOM   3587  CB  ASP B  90     128.791  32.523   3.526  1.00 39.79           C  
-ATOM   3588  CG  ASP B  90     128.901  33.009   2.088  1.00 42.42           C  
-ATOM   3589  OD1 ASP B  90     129.077  32.156   1.192  1.00 44.13           O  
-ATOM   3590  OD2 ASP B  90     128.791  34.235   1.853  1.00 42.82           O  
-ATOM   3591  N   GLY B  91     126.586  31.612   6.137  1.00 37.32           N  
-ATOM   3592  CA  GLY B  91     126.478  30.806   7.339  1.00 35.93           C  
-ATOM   3593  C   GLY B  91     125.321  29.831   7.212  1.00 35.13           C  
-ATOM   3594  O   GLY B  91     124.884  29.244   8.206  1.00 35.30           O  
-ATOM   3595  N   LEU B  95     124.813  29.671   5.992  1.00 33.99           N  
-ATOM   3596  CA  LEU B  95     123.695  28.776   5.730  1.00 33.19           C  
-ATOM   3597  C   LEU B  95     124.127  27.332   5.524  1.00 33.62           C  
-ATOM   3598  O   LEU B  95     124.671  26.975   4.479  1.00 33.97           O  
-ATOM   3599  CB  LEU B  95     122.895  29.242   4.511  1.00 31.68           C  
-ATOM   3600  CG  LEU B  95     121.654  28.401   4.179  1.00 30.03           C  
-ATOM   3601  CD1 LEU B  95     120.628  28.515   5.297  1.00 29.28           C  
-ATOM   3602  CD2 LEU B  95     121.055  28.850   2.865  1.00 29.23           C  
-ATOM   3603  N   LYS B  96     123.874  26.506   6.530  1.00 33.80           N  
-ATOM   3604  CA  LYS B  96     124.197  25.090   6.475  1.00 33.64           C  
-ATOM   3605  C   LYS B  96     122.910  24.341   6.133  1.00 33.27           C  
-ATOM   3606  O   LYS B  96     122.135  23.975   7.014  1.00 33.09           O  
-ATOM   3607  CB  LYS B  96     124.744  24.623   7.824  1.00 34.86           C  
-ATOM   3608  CG  LYS B  96     126.004  25.344   8.269  1.00 36.61           C  
-ATOM   3609  CD  LYS B  96     126.428  24.910   9.665  1.00 39.29           C  
-ATOM   3610  CE  LYS B  96     126.788  23.426   9.720  1.00 40.87           C  
-ATOM   3611  NZ  LYS B  96     127.945  23.086   8.839  1.00 42.59           N  
-ATOM   3612  N   SER B  97     122.688  24.119   4.846  1.00 32.62           N  
-ATOM   3613  CA  SER B  97     121.495  23.432   4.374  1.00 33.53           C  
-ATOM   3614  C   SER B  97     121.242  22.062   5.009  1.00 33.75           C  
-ATOM   3615  O   SER B  97     120.098  21.709   5.297  1.00 34.12           O  
-ATOM   3616  CB  SER B  97     121.561  23.280   2.857  1.00 34.15           C  
-ATOM   3617  OG  SER B  97     121.865  24.521   2.247  1.00 36.65           O  
-ATOM   3618  N   GLU B  98     122.306  21.305   5.252  1.00 33.51           N  
-ATOM   3619  CA  GLU B  98     122.159  19.971   5.825  1.00 33.76           C  
-ATOM   3620  C   GLU B  98     121.538  19.950   7.216  1.00 31.66           C  
-ATOM   3621  O   GLU B  98     121.072  18.905   7.671  1.00 31.68           O  
-ATOM   3622  CB  GLU B  98     123.493  19.211   5.819  1.00 36.75           C  
-ATOM   3623  CG  GLU B  98     124.560  19.760   6.754  1.00 41.53           C  
-ATOM   3624  CD  GLU B  98     125.702  18.775   6.977  1.00 44.76           C  
-ATOM   3625  OE1 GLU B  98     125.428  17.565   7.169  1.00 45.75           O  
-ATOM   3626  OE2 GLU B  98     126.875  19.214   6.967  1.00 45.99           O  
-ATOM   3627  N   THR B  99     121.535  21.095   7.889  1.00 29.50           N  
-ATOM   3628  CA  THR B  99     120.957  21.188   9.221  1.00 28.33           C  
-ATOM   3629  C   THR B  99     119.880  22.266   9.306  1.00 26.89           C  
-ATOM   3630  O   THR B  99     119.454  22.633  10.404  1.00 26.57           O  
-ATOM   3631  CB  THR B  99     122.028  21.493  10.275  1.00 28.69           C  
-ATOM   3632  OG1 THR B  99     122.884  22.536   9.795  1.00 29.79           O  
-ATOM   3633  CG2 THR B  99     122.849  20.256  10.578  1.00 29.96           C  
-ATOM   3634  N   THR B 100     119.438  22.770   8.156  1.00 24.91           N  
-ATOM   3635  CA  THR B 100     118.414  23.806   8.135  1.00 23.46           C  
-ATOM   3636  C   THR B 100     117.131  23.346   7.452  1.00 22.44           C  
-ATOM   3637  O   THR B 100     117.164  22.816   6.338  1.00 22.70           O  
-ATOM   3638  CB  THR B 100     118.921  25.088   7.438  1.00 23.18           C  
-ATOM   3639  OG1 THR B 100     120.125  25.536   8.072  1.00 21.75           O  
-ATOM   3640  CG2 THR B 100     117.880  26.193   7.530  1.00 22.41           C  
-ATOM   3641  N   ALA B 101     116.015  23.488   8.161  1.00 21.49           N  
-ATOM   3642  CA  ALA B 101     114.696  23.131   7.637  1.00 19.82           C  
-ATOM   3643  C   ALA B 101     114.028  24.465   7.315  1.00 18.80           C  
-ATOM   3644  O   ALA B 101     114.135  25.417   8.091  1.00 18.72           O  
-ATOM   3645  CB  ALA B 101     113.900  22.369   8.678  1.00 18.01           C  
-ATOM   3646  N   THR B 102     113.363  24.544   6.171  1.00 18.69           N  
-ATOM   3647  CA  THR B 102     112.716  25.782   5.751  1.00 18.55           C  
-ATOM   3648  C   THR B 102     111.243  25.579   5.436  1.00 17.77           C  
-ATOM   3649  O   THR B 102     110.868  24.600   4.786  1.00 18.72           O  
-ATOM   3650  CB  THR B 102     113.413  26.351   4.511  1.00 18.34           C  
-ATOM   3651  OG1 THR B 102     114.828  26.325   4.722  1.00 21.48           O  
-ATOM   3652  CG2 THR B 102     112.983  27.783   4.263  1.00 18.36           C  
-ATOM   3653  N   LEU B 103     110.415  26.529   5.855  1.00 16.23           N  
-ATOM   3654  CA  LEU B 103     108.978  26.440   5.620  1.00 14.73           C  
-ATOM   3655  C   LEU B 103     108.409  27.783   5.171  1.00 13.80           C  
-ATOM   3656  O   LEU B 103     108.537  28.773   5.887  1.00 13.30           O  
-ATOM   3657  CB  LEU B 103     108.282  26.011   6.913  1.00 13.30           C  
-ATOM   3658  CG  LEU B 103     106.978  25.199   6.914  1.00 13.52           C  
-ATOM   3659  CD1 LEU B 103     105.984  25.844   7.880  1.00 11.26           C  
-ATOM   3660  CD2 LEU B 103     106.397  25.074   5.519  1.00 12.21           C  
-ATOM   3661  N   ALA B 104     107.832  27.826   3.971  1.00 13.24           N  
-ATOM   3662  CA  ALA B 104     107.204  29.050   3.463  1.00 12.87           C  
-ATOM   3663  C   ALA B 104     105.913  29.208   4.262  1.00 12.86           C  
-ATOM   3664  O   ALA B 104     105.203  28.225   4.503  1.00 13.57           O  
-ATOM   3665  CB  ALA B 104     106.893  28.927   1.983  1.00 11.99           C  
-ATOM   3666  N   THR B 105     105.622  30.433   4.681  1.00 12.06           N  
-ATOM   3667  CA  THR B 105     104.444  30.694   5.492  1.00 11.73           C  
-ATOM   3668  C   THR B 105     103.599  31.860   4.982  1.00 11.54           C  
-ATOM   3669  O   THR B 105     103.962  32.537   4.011  1.00 11.55           O  
-ATOM   3670  CB  THR B 105     104.859  30.982   6.955  1.00 12.09           C  
-ATOM   3671  OG1 THR B 105     105.801  32.066   6.982  1.00 12.37           O  
-ATOM   3672  CG2 THR B 105     105.499  29.747   7.587  1.00 10.60           C  
-ATOM   3673  N   VAL B 106     102.451  32.060   5.622  1.00 10.36           N  
-ATOM   3674  CA  VAL B 106     101.540  33.145   5.272  1.00  9.34           C  
-ATOM   3675  C   VAL B 106     102.036  34.369   6.048  1.00  9.10           C  
-ATOM   3676  O   VAL B 106     101.591  34.649   7.164  1.00  9.89           O  
-ATOM   3677  CB  VAL B 106     100.053  32.790   5.650  1.00  8.23           C  
-ATOM   3678  CG1 VAL B 106      99.098  33.892   5.202  1.00  7.42           C  
-ATOM   3679  CG2 VAL B 106      99.645  31.478   5.009  1.00  5.57           C  
-ATOM   3680  N   GLY B 107     103.053  35.016   5.495  1.00  9.48           N  
-ATOM   3681  CA  GLY B 107     103.633  36.188   6.121  1.00 10.26           C  
-ATOM   3682  C   GLY B 107     104.479  35.852   7.335  1.00 11.40           C  
-ATOM   3683  O   GLY B 107     104.617  34.686   7.707  1.00 12.63           O  
-ATOM   3684  N   GLY B 108     105.062  36.881   7.944  1.00 11.79           N  
-ATOM   3685  CA  GLY B 108     105.878  36.688   9.128  1.00 11.09           C  
-ATOM   3686  C   GLY B 108     105.047  36.262  10.317  1.00 11.82           C  
-ATOM   3687  O   GLY B 108     105.511  35.504  11.171  1.00 12.38           O  
-ATOM   3688  N   THR B 109     103.818  36.758  10.395  1.00 12.66           N  
-ATOM   3689  CA  THR B 109     102.930  36.390  11.492  1.00 12.35           C  
-ATOM   3690  C   THR B 109     102.677  34.883  11.418  1.00 12.21           C  
-ATOM   3691  O   THR B 109     102.714  34.185  12.435  1.00 13.03           O  
-ATOM   3692  CB  THR B 109     101.590  37.169  11.435  1.00 12.40           C  
-ATOM   3693  OG1 THR B 109     101.860  38.577  11.437  1.00 10.95           O  
-ATOM   3694  CG2 THR B 109     100.713  36.830  12.645  1.00 11.95           C  
-ATOM   3695  N   GLY B 110     102.459  34.382  10.206  1.00 12.76           N  
-ATOM   3696  CA  GLY B 110     102.243  32.959  10.030  1.00 13.44           C  
-ATOM   3697  C   GLY B 110     103.483  32.195  10.467  1.00 14.99           C  
-ATOM   3698  O   GLY B 110     103.386  31.101  11.039  1.00 15.81           O  
-ATOM   3699  N   ALA B 111     104.653  32.785  10.219  1.00 14.29           N  
-ATOM   3700  CA  ALA B 111     105.927  32.172  10.593  1.00 14.00           C  
-ATOM   3701  C   ALA B 111     106.050  32.063  12.104  1.00 13.78           C  
-ATOM   3702  O   ALA B 111     106.548  31.058  12.618  1.00 14.30           O  
-ATOM   3703  CB  ALA B 111     107.095  32.973  10.023  1.00 13.80           C  
-ATOM   3704  N   LEU B 112     105.603  33.098  12.810  1.00 13.39           N  
-ATOM   3705  CA  LEU B 112     105.657  33.115  14.268  1.00 13.99           C  
-ATOM   3706  C   LEU B 112     104.750  32.033  14.846  1.00 14.83           C  
-ATOM   3707  O   LEU B 112     105.193  31.198  15.642  1.00 14.92           O  
-ATOM   3708  CB  LEU B 112     105.240  34.488  14.807  1.00 14.46           C  
-ATOM   3709  CG  LEU B 112     106.148  35.676  14.474  1.00 16.69           C  
-ATOM   3710  CD1 LEU B 112     105.460  36.978  14.864  1.00 17.14           C  
-ATOM   3711  CD2 LEU B 112     107.482  35.535  15.195  1.00 16.56           C  
-ATOM   3712  N   ARG B 113     103.489  32.036  14.418  1.00 15.32           N  
-ATOM   3713  CA  ARG B 113     102.505  31.059  14.876  1.00 16.24           C  
-ATOM   3714  C   ARG B 113     103.022  29.641  14.642  1.00 16.34           C  
-ATOM   3715  O   ARG B 113     103.013  28.807  15.550  1.00 16.84           O  
-ATOM   3716  CB  ARG B 113     101.176  31.280  14.139  1.00 18.03           C  
-ATOM   3717  CG  ARG B 113     100.106  30.220  14.375  1.00 19.43           C  
-ATOM   3718  CD  ARG B 113      99.567  30.217  15.800  1.00 20.68           C  
-ATOM   3719  NE  ARG B 113      98.636  29.107  15.988  1.00 22.05           N  
-ATOM   3720  CZ  ARG B 113      97.328  29.165  15.742  1.00 23.12           C  
-ATOM   3721  NH1 ARG B 113      96.774  30.295  15.307  1.00 21.72           N  
-ATOM   3722  NH2 ARG B 113      96.581  28.072  15.874  1.00 22.63           N  
-ATOM   3723  N   GLN B 114     103.514  29.385  13.435  1.00 16.20           N  
-ATOM   3724  CA  GLN B 114     104.048  28.074  13.080  1.00 16.93           C  
-ATOM   3725  C   GLN B 114     105.276  27.730  13.941  1.00 17.43           C  
-ATOM   3726  O   GLN B 114     105.525  26.558  14.256  1.00 17.06           O  
-ATOM   3727  CB  GLN B 114     104.391  28.058  11.588  1.00 17.37           C  
-ATOM   3728  CG  GLN B 114     103.783  26.915  10.788  1.00 19.21           C  
-ATOM   3729  CD  GLN B 114     102.260  26.878  10.826  1.00 19.57           C  
-ATOM   3730  OE1 GLN B 114     101.640  27.212  11.835  1.00 20.88           O  
-ATOM   3731  NE2 GLN B 114     101.654  26.446   9.731  1.00 18.90           N  
-ATOM   3732  N   ALA B 115     106.016  28.761  14.347  1.00 17.64           N  
-ATOM   3733  CA  ALA B 115     107.200  28.597  15.188  1.00 18.36           C  
-ATOM   3734  C   ALA B 115     106.791  28.133  16.584  1.00 18.45           C  
-ATOM   3735  O   ALA B 115     107.416  27.245  17.173  1.00 18.72           O  
-ATOM   3736  CB  ALA B 115     107.965  29.916  15.281  1.00 17.26           C  
-ATOM   3737  N   LEU B 116     105.727  28.731  17.104  1.00 19.07           N  
-ATOM   3738  CA  LEU B 116     105.217  28.396  18.431  1.00 20.25           C  
-ATOM   3739  C   LEU B 116     104.614  26.993  18.487  1.00 20.74           C  
-ATOM   3740  O   LEU B 116     104.759  26.288  19.491  1.00 20.66           O  
-ATOM   3741  CB  LEU B 116     104.203  29.451  18.883  1.00 18.78           C  
-ATOM   3742  CG  LEU B 116     104.795  30.856  19.042  1.00 18.34           C  
-ATOM   3743  CD1 LEU B 116     103.688  31.888  19.212  1.00 18.53           C  
-ATOM   3744  CD2 LEU B 116     105.763  30.888  20.223  1.00 16.59           C  
-ATOM   3745  N   GLU B 117     103.955  26.592  17.401  1.00 21.64           N  
-ATOM   3746  CA  GLU B 117     103.343  25.266  17.295  1.00 21.59           C  
-ATOM   3747  C   GLU B 117     104.428  24.186  17.232  1.00 21.30           C  
-ATOM   3748  O   GLU B 117     104.319  23.136  17.876  1.00 21.14           O  
-ATOM   3749  CB  GLU B 117     102.462  25.183  16.040  1.00 21.94           C  
-ATOM   3750  CG  GLU B 117     101.234  26.100  16.040  1.00 23.26           C  
-ATOM   3751  CD  GLU B 117     100.076  25.588  16.901  1.00 24.50           C  
-ATOM   3752  OE1 GLU B 117     100.187  24.511  17.520  1.00 26.01           O  
-ATOM   3753  OE2 GLU B 117      99.035  26.271  16.950  1.00 25.69           O  
-ATOM   3754  N   LEU B 118     105.474  24.445  16.450  1.00 20.78           N  
-ATOM   3755  CA  LEU B 118     106.586  23.505  16.311  1.00 20.93           C  
-ATOM   3756  C   LEU B 118     107.261  23.285  17.664  1.00 21.13           C  
-ATOM   3757  O   LEU B 118     107.478  22.150  18.092  1.00 19.50           O  
-ATOM   3758  CB  LEU B 118     107.608  24.051  15.318  1.00 21.12           C  
-ATOM   3759  CG  LEU B 118     108.782  23.144  14.966  1.00 21.17           C  
-ATOM   3760  CD1 LEU B 118     108.268  21.928  14.223  1.00 20.78           C  
-ATOM   3761  CD2 LEU B 118     109.785  23.913  14.115  1.00 21.08           C  
-ATOM   3762  N   ALA B 119     107.561  24.390  18.340  1.00 22.11           N  
-ATOM   3763  CA  ALA B 119     108.209  24.356  19.643  1.00 23.60           C  
-ATOM   3764  C   ALA B 119     107.361  23.642  20.690  1.00 24.89           C  
-ATOM   3765  O   ALA B 119     107.880  22.816  21.438  1.00 24.79           O  
-ATOM   3766  CB  ALA B 119     108.535  25.766  20.100  1.00 22.89           C  
-ATOM   3767  N   ARG B 120     106.064  23.949  20.738  1.00 26.81           N  
-ATOM   3768  CA  ARG B 120     105.161  23.320  21.706  1.00 27.93           C  
-ATOM   3769  C   ARG B 120     105.017  21.820  21.475  1.00 28.13           C  
-ATOM   3770  O   ARG B 120     104.810  21.062  22.422  1.00 26.81           O  
-ATOM   3771  CB  ARG B 120     103.786  23.988  21.707  1.00 28.83           C  
-ATOM   3772  CG  ARG B 120     102.893  23.482  22.828  1.00 31.17           C  
-ATOM   3773  CD  ARG B 120     101.586  24.236  22.902  1.00 33.72           C  
-ATOM   3774  NE  ARG B 120     100.820  24.136  21.664  1.00 36.19           N  
-ATOM   3775  CZ  ARG B 120      99.627  24.691  21.477  1.00 36.44           C  
-ATOM   3776  NH1 ARG B 120      99.058  25.391  22.455  1.00 37.22           N  
-ATOM   3777  NH2 ARG B 120      99.007  24.547  20.313  1.00 36.75           N  
-ATOM   3778  N   MET B 121     105.106  21.400  20.217  1.00 29.44           N  
-ATOM   3779  CA  MET B 121     105.031  19.984  19.885  1.00 31.57           C  
-ATOM   3780  C   MET B 121     106.248  19.273  20.475  1.00 32.38           C  
-ATOM   3781  O   MET B 121     106.133  18.169  21.000  1.00 33.10           O  
-ATOM   3782  CB  MET B 121     104.998  19.777  18.366  1.00 33.25           C  
-ATOM   3783  CG  MET B 121     103.626  19.977  17.739  1.00 36.22           C  
-ATOM   3784  SD  MET B 121     103.606  19.742  15.947  1.00 39.02           S  
-ATOM   3785  CE  MET B 121     103.633  17.980  15.833  1.00 37.75           C  
-ATOM   3786  N   ALA B 122     107.408  19.922  20.396  1.00 32.76           N  
-ATOM   3787  CA  ALA B 122     108.655  19.368  20.916  1.00 33.22           C  
-ATOM   3788  C   ALA B 122     108.787  19.546  22.425  1.00 33.48           C  
-ATOM   3789  O   ALA B 122     109.552  18.833  23.076  1.00 34.50           O  
-ATOM   3790  CB  ALA B 122     109.848  20.010  20.213  1.00 33.44           C  
-ATOM   3791  N   ASN B 123     108.079  20.527  22.969  1.00 33.69           N  
-ATOM   3792  CA  ASN B 123     108.118  20.803  24.397  1.00 33.60           C  
-ATOM   3793  C   ASN B 123     106.771  21.327  24.867  1.00 33.44           C  
-ATOM   3794  O   ASN B 123     106.536  22.532  24.897  1.00 33.55           O  
-ATOM   3795  CB  ASN B 123     109.213  21.821  24.727  1.00 34.68           C  
-ATOM   3796  CG  ASN B 123     109.256  22.173  26.208  1.00 36.49           C  
-ATOM   3797  OD1 ASN B 123     108.657  21.489  27.042  1.00 38.51           O  
-ATOM   3798  ND2 ASN B 123     109.948  23.253  26.541  1.00 37.11           N  
-ATOM   3799  N   PRO B 124     105.873  20.418  25.262  1.00 33.88           N  
-ATOM   3800  CA  PRO B 124     104.533  20.763  25.743  1.00 34.08           C  
-ATOM   3801  C   PRO B 124     104.551  21.747  26.909  1.00 34.56           C  
-ATOM   3802  O   PRO B 124     103.578  22.466  27.130  1.00 34.38           O  
-ATOM   3803  CB  PRO B 124     103.979  19.410  26.180  1.00 34.13           C  
-ATOM   3804  CG  PRO B 124     104.639  18.457  25.228  1.00 34.25           C  
-ATOM   3805  CD  PRO B 124     106.056  18.955  25.224  1.00 33.62           C  
-ATOM   3806  N   ASP B 125     105.655  21.787  27.647  1.00 35.15           N  
-ATOM   3807  CA  ASP B 125     105.758  22.679  28.797  1.00 36.26           C  
-ATOM   3808  C   ASP B 125     106.600  23.931  28.575  1.00 35.76           C  
-ATOM   3809  O   ASP B 125     107.066  24.537  29.537  1.00 36.73           O  
-ATOM   3810  CB  ASP B 125     106.304  21.911  30.003  1.00 37.75           C  
-ATOM   3811  CG  ASP B 125     105.415  20.759  30.411  1.00 39.25           C  
-ATOM   3812  OD1 ASP B 125     104.211  20.995  30.669  1.00 39.61           O  
-ATOM   3813  OD2 ASP B 125     105.923  19.617  30.469  1.00 40.19           O  
-ATOM   3814  N   LEU B 126     106.781  24.342  27.326  1.00 35.30           N  
-ATOM   3815  CA  LEU B 126     107.595  25.522  27.057  1.00 34.62           C  
-ATOM   3816  C   LEU B 126     106.968  26.822  27.544  1.00 33.23           C  
-ATOM   3817  O   LEU B 126     105.747  26.927  27.680  1.00 33.13           O  
-ATOM   3818  CB  LEU B 126     107.953  25.615  25.564  1.00 35.67           C  
-ATOM   3819  CG  LEU B 126     106.992  26.119  24.478  1.00 36.71           C  
-ATOM   3820  CD1 LEU B 126     105.558  25.714  24.780  1.00 36.89           C  
-ATOM   3821  CD2 LEU B 126     107.101  27.625  24.337  1.00 36.96           C  
-ATOM   3822  N   ARG B 129     107.830  27.780  27.870  1.00 31.73           N  
-ATOM   3823  CA  ARG B 129     107.422  29.111  28.309  1.00 29.90           C  
-ATOM   3824  C   ARG B 129     108.112  30.042  27.330  1.00 28.21           C  
-ATOM   3825  O   ARG B 129     109.163  29.701  26.774  1.00 27.78           O  
-ATOM   3826  CB  ARG B 129     107.924  29.421  29.720  1.00 31.60           C  
-ATOM   3827  CG  ARG B 129     107.488  28.445  30.783  1.00 33.74           C  
-ATOM   3828  CD  ARG B 129     107.989  28.881  32.147  1.00 36.20           C  
-ATOM   3829  NE  ARG B 129     107.165  29.932  32.742  1.00 38.04           N  
-ATOM   3830  CZ  ARG B 129     105.993  29.718  33.334  1.00 38.61           C  
-ATOM   3831  NH1 ARG B 129     105.494  28.491  33.407  1.00 39.93           N  
-ATOM   3832  NH2 ARG B 129     105.338  30.722  33.900  1.00 39.52           N  
-ATOM   3833  N   VAL B 133     107.537  31.213  27.111  1.00 26.39           N  
-ATOM   3834  CA  VAL B 133     108.133  32.156  26.181  1.00 24.13           C  
-ATOM   3835  C   VAL B 133     108.467  33.484  26.859  1.00 23.78           C  
-ATOM   3836  O   VAL B 133     107.626  34.082  27.535  1.00 23.01           O  
-ATOM   3837  CB  VAL B 133     107.204  32.407  24.959  1.00 23.18           C  
-ATOM   3838  CG1 VAL B 133     107.911  33.254  23.916  1.00 22.22           C  
-ATOM   3839  CG2 VAL B 133     106.768  31.094  24.348  1.00 21.71           C  
-ATOM   3840  N   PHE B 134     109.724  33.897  26.725  1.00 23.40           N  
-ATOM   3841  CA  PHE B 134     110.197  35.165  27.270  1.00 22.78           C  
-ATOM   3842  C   PHE B 134     110.082  36.197  26.152  1.00 22.45           C  
-ATOM   3843  O   PHE B 134     110.569  35.966  25.044  1.00 22.09           O  
-ATOM   3844  CB  PHE B 134     111.666  35.059  27.697  1.00 22.35           C  
-ATOM   3845  CG  PHE B 134     111.877  34.307  28.981  1.00 22.02           C  
-ATOM   3846  CD1 PHE B 134     111.852  32.920  29.005  1.00 21.55           C  
-ATOM   3847  CD2 PHE B 134     112.106  34.993  30.171  1.00 22.03           C  
-ATOM   3848  CE1 PHE B 134     112.049  32.226  30.191  1.00 21.26           C  
-ATOM   3849  CE2 PHE B 134     112.305  34.303  31.366  1.00 21.66           C  
-ATOM   3850  CZ  PHE B 134     112.276  32.918  31.373  1.00 21.13           C  
-ATOM   3851  N   VAL B 135     109.403  37.307  26.422  1.00 22.77           N  
-ATOM   3852  CA  VAL B 135     109.248  38.367  25.429  1.00 23.57           C  
-ATOM   3853  C   VAL B 135     109.785  39.678  26.000  1.00 24.12           C  
-ATOM   3854  O   VAL B 135     109.792  39.878  27.219  1.00 23.90           O  
-ATOM   3855  CB  VAL B 135     107.771  38.551  24.983  1.00 23.32           C  
-ATOM   3856  CG1 VAL B 135     107.224  37.255  24.403  1.00 23.39           C  
-ATOM   3857  CG2 VAL B 135     106.921  39.025  26.138  1.00 22.82           C  
-ATOM   3858  N   SER B 136     110.260  40.558  25.125  1.00 24.01           N  
-ATOM   3859  CA  SER B 136     110.815  41.828  25.563  1.00 24.08           C  
-ATOM   3860  C   SER B 136     109.783  42.785  26.127  1.00 24.60           C  
-ATOM   3861  O   SER B 136     108.616  42.773  25.725  1.00 25.11           O  
-ATOM   3862  CB  SER B 136     111.582  42.503  24.419  1.00 23.27           C  
-ATOM   3863  OG  SER B 136     110.766  42.734  23.286  1.00 22.86           O  
-ATOM   3864  N   ASP B 137     110.213  43.586  27.091  1.00 24.99           N  
-ATOM   3865  CA  ASP B 137     109.352  44.582  27.699  1.00 25.43           C  
-ATOM   3866  C   ASP B 137     109.752  45.961  27.161  1.00 25.00           C  
-ATOM   3867  O   ASP B 137     110.767  46.523  27.579  1.00 25.53           O  
-ATOM   3868  CB  ASP B 137     109.493  44.541  29.224  1.00 26.31           C  
-ATOM   3869  CG  ASP B 137     108.876  45.748  29.900  1.00 28.61           C  
-ATOM   3870  OD1 ASP B 137     107.689  46.041  29.639  1.00 29.38           O  
-ATOM   3871  OD2 ASP B 137     109.588  46.421  30.675  1.00 30.69           O  
-ATOM   3872  N   PRO B 138     108.984  46.509  26.202  1.00 24.50           N  
-ATOM   3873  CA  PRO B 138     107.776  45.943  25.593  1.00 24.45           C  
-ATOM   3874  C   PRO B 138     108.072  45.165  24.300  1.00 24.47           C  
-ATOM   3875  O   PRO B 138     109.235  44.956  23.926  1.00 24.30           O  
-ATOM   3876  CB  PRO B 138     106.950  47.190  25.297  1.00 24.16           C  
-ATOM   3877  CG  PRO B 138     107.996  48.144  24.831  1.00 24.15           C  
-ATOM   3878  CD  PRO B 138     109.138  47.927  25.819  1.00 24.02           C  
-ATOM   3879  N   THR B 139     107.011  44.754  23.615  1.00 24.42           N  
-ATOM   3880  CA  THR B 139     107.146  44.020  22.368  1.00 24.26           C  
-ATOM   3881  C   THR B 139     105.904  44.212  21.505  1.00 24.19           C  
-ATOM   3882  O   THR B 139     104.928  44.842  21.921  1.00 24.33           O  
-ATOM   3883  CB  THR B 139     107.377  42.506  22.619  1.00 24.41           C  
-ATOM   3884  OG1 THR B 139     107.697  41.849  21.382  1.00 23.90           O  
-ATOM   3885  CG2 THR B 139     106.138  41.852  23.229  1.00 24.22           C  
-ATOM   3886  N   TRP B 140     105.988  43.724  20.273  1.00 24.25           N  
-ATOM   3887  CA  TRP B 140     104.890  43.783  19.315  1.00 23.16           C  
-ATOM   3888  C   TRP B 140     103.722  43.078  20.007  1.00 22.99           C  
-ATOM   3889  O   TRP B 140     103.818  41.896  20.353  1.00 22.94           O  
-ATOM   3890  CB  TRP B 140     105.299  43.023  18.051  1.00 22.86           C  
-ATOM   3891  CG  TRP B 140     104.464  43.284  16.834  1.00 22.15           C  
-ATOM   3892  CD1 TRP B 140     104.064  44.498  16.355  1.00 22.01           C  
-ATOM   3893  CD2 TRP B 140     103.990  42.307  15.899  1.00 21.05           C  
-ATOM   3894  NE1 TRP B 140     103.381  44.339  15.175  1.00 21.67           N  
-ATOM   3895  CE2 TRP B 140     103.321  43.006  14.870  1.00 21.41           C  
-ATOM   3896  CE3 TRP B 140     104.071  40.911  15.826  1.00 20.68           C  
-ATOM   3897  CZ2 TRP B 140     102.736  42.354  13.785  1.00 20.77           C  
-ATOM   3898  CZ3 TRP B 140     103.490  40.265  14.749  1.00 20.05           C  
-ATOM   3899  CH2 TRP B 140     102.831  40.987  13.741  1.00 20.99           C  
-ATOM   3900  N   PRO B 141     102.617  43.800  20.244  1.00 22.68           N  
-ATOM   3901  CA  PRO B 141     101.419  43.266  20.905  1.00 22.80           C  
-ATOM   3902  C   PRO B 141     100.922  41.946  20.328  1.00 22.35           C  
-ATOM   3903  O   PRO B 141     100.476  41.064  21.064  1.00 22.20           O  
-ATOM   3904  CB  PRO B 141     100.398  44.381  20.700  1.00 22.81           C  
-ATOM   3905  CG  PRO B 141     101.250  45.612  20.698  1.00 23.27           C  
-ATOM   3906  CD  PRO B 141     102.404  45.198  19.828  1.00 22.35           C  
-ATOM   3907  N   ASN B 142     101.034  41.799  19.015  1.00 22.50           N  
-ATOM   3908  CA  ASN B 142     100.589  40.587  18.349  1.00 23.36           C  
-ATOM   3909  C   ASN B 142     101.353  39.353  18.806  1.00 23.72           C  
-ATOM   3910  O   ASN B 142     100.902  38.228  18.600  1.00 24.37           O  
-ATOM   3911  CB  ASN B 142     100.675  40.747  16.837  1.00 24.33           C  
-ATOM   3912  CG  ASN B 142      99.892  41.939  16.341  1.00 26.05           C  
-ATOM   3913  OD1 ASN B 142     100.173  43.079  16.714  1.00 28.35           O  
-ATOM   3914  ND2 ASN B 142      98.895  41.688  15.514  1.00 27.33           N  
-ATOM   3915  N   HIS B 143     102.518  39.559  19.414  1.00 23.31           N  
-ATOM   3916  CA  HIS B 143     103.312  38.445  19.923  1.00 22.91           C  
-ATOM   3917  C   HIS B 143     102.547  37.809  21.077  1.00 22.72           C  
-ATOM   3918  O   HIS B 143     102.321  36.600  21.105  1.00 22.75           O  
-ATOM   3919  CB  HIS B 143     104.669  38.931  20.445  1.00 22.00           C  
-ATOM   3920  CG  HIS B 143     105.704  39.120  19.381  1.00 21.18           C  
-ATOM   3921  ND1 HIS B 143     106.595  40.171  19.388  1.00 21.05           N  
-ATOM   3922  CD2 HIS B 143     106.022  38.365  18.304  1.00 20.54           C  
-ATOM   3923  CE1 HIS B 143     107.422  40.053  18.365  1.00 20.09           C  
-ATOM   3924  NE2 HIS B 143     107.096  38.965  17.693  1.00 20.57           N  
-ATOM   3925  N   VAL B 144     102.123  38.648  22.013  1.00 23.28           N  
-ATOM   3926  CA  VAL B 144     101.404  38.186  23.190  1.00 24.61           C  
-ATOM   3927  C   VAL B 144      99.992  37.680  22.907  1.00 24.49           C  
-ATOM   3928  O   VAL B 144      99.550  36.716  23.525  1.00 24.32           O  
-ATOM   3929  CB  VAL B 144     101.369  39.281  24.284  1.00 24.88           C  
-ATOM   3930  CG1 VAL B 144     100.634  38.774  25.519  1.00 24.86           C  
-ATOM   3931  CG2 VAL B 144     102.794  39.691  24.651  1.00 24.66           C  
-ATOM   3932  N   SER B 145      99.288  38.311  21.973  1.00 24.91           N  
-ATOM   3933  CA  SER B 145      97.933  37.879  21.660  1.00 26.37           C  
-ATOM   3934  C   SER B 145      97.928  36.446  21.169  1.00 26.27           C  
-ATOM   3935  O   SER B 145      97.132  35.636  21.638  1.00 27.62           O  
-ATOM   3936  CB  SER B 145      97.283  38.797  20.629  1.00 27.11           C  
-ATOM   3937  OG  SER B 145      98.146  39.009  19.530  1.00 31.53           O  
-ATOM   3938  N   ILE B 146      98.852  36.122  20.270  1.00 26.86           N  
-ATOM   3939  CA  ILE B 146      98.954  34.768  19.725  1.00 26.81           C  
-ATOM   3940  C   ILE B 146      99.316  33.760  20.822  1.00 26.69           C  
-ATOM   3941  O   ILE B 146      98.697  32.703  20.939  1.00 26.67           O  
-ATOM   3942  CB  ILE B 146      99.979  34.701  18.563  1.00 26.82           C  
-ATOM   3943  CG1 ILE B 146      99.566  35.680  17.455  1.00 27.14           C  
-ATOM   3944  CG2 ILE B 146     100.053  33.282  18.001  1.00 26.37           C  
-ATOM   3945  CD1 ILE B 146     100.539  35.777  16.296  1.00 27.19           C  
-ATOM   3946  N   MET B 147     100.291  34.105  21.652  1.00 26.90           N  
-ATOM   3947  CA  MET B 147     100.702  33.225  22.739  1.00 27.24           C  
-ATOM   3948  C   MET B 147      99.547  32.974  23.706  1.00 26.93           C  
-ATOM   3949  O   MET B 147      99.341  31.848  24.153  1.00 26.82           O  
-ATOM   3950  CB  MET B 147     101.913  33.817  23.475  1.00 27.62           C  
-ATOM   3951  CG  MET B 147     103.240  33.570  22.760  1.00 28.25           C  
-ATOM   3952  SD  MET B 147     104.600  34.617  23.315  1.00 28.15           S  
-ATOM   3953  CE  MET B 147     105.222  35.187  21.744  1.00 28.06           C  
-ATOM   3954  N   ASN B 148      98.789  34.021  24.015  1.00 27.27           N  
-ATOM   3955  CA  ASN B 148      97.644  33.903  24.916  1.00 28.53           C  
-ATOM   3956  C   ASN B 148      96.622  32.954  24.295  1.00 28.50           C  
-ATOM   3957  O   ASN B 148      96.147  32.019  24.940  1.00 28.00           O  
-ATOM   3958  CB  ASN B 148      96.999  35.272  25.163  1.00 29.87           C  
-ATOM   3959  CG  ASN B 148      97.820  36.156  26.092  1.00 30.95           C  
-ATOM   3960  OD1 ASN B 148      98.503  35.673  26.998  1.00 32.21           O  
-ATOM   3961  ND2 ASN B 148      97.733  37.463  25.884  1.00 31.65           N  
-ATOM   3962  N   PHE B 149      96.315  33.188  23.024  1.00 28.41           N  
-ATOM   3963  CA  PHE B 149      95.380  32.356  22.281  1.00 28.85           C  
-ATOM   3964  C   PHE B 149      95.793  30.888  22.368  1.00 28.93           C  
-ATOM   3965  O   PHE B 149      94.977  30.021  22.659  1.00 29.88           O  
-ATOM   3966  CB  PHE B 149      95.342  32.803  20.820  1.00 28.81           C  
-ATOM   3967  CG  PHE B 149      94.477  31.952  19.945  1.00 28.63           C  
-ATOM   3968  CD1 PHE B 149      93.095  31.989  20.069  1.00 28.59           C  
-ATOM   3969  CD2 PHE B 149      95.046  31.118  18.990  1.00 28.67           C  
-ATOM   3970  CE1 PHE B 149      92.284  31.208  19.253  1.00 29.80           C  
-ATOM   3971  CE2 PHE B 149      94.247  30.331  18.168  1.00 30.38           C  
-ATOM   3972  CZ  PHE B 149      92.859  30.376  18.301  1.00 30.30           C  
-ATOM   3973  N   MET B 150      97.068  30.613  22.125  1.00 29.11           N  
-ATOM   3974  CA  MET B 150      97.567  29.247  22.187  1.00 29.61           C  
-ATOM   3975  C   MET B 150      97.606  28.704  23.615  1.00 30.22           C  
-ATOM   3976  O   MET B 150      97.641  27.489  23.818  1.00 30.22           O  
-ATOM   3977  CB  MET B 150      98.956  29.170  21.562  1.00 29.50           C  
-ATOM   3978  CG  MET B 150      98.957  29.333  20.054  1.00 29.57           C  
-ATOM   3979  SD  MET B 150     100.617  29.318  19.372  1.00 30.02           S  
-ATOM   3980  CE  MET B 150     101.131  27.638  19.743  1.00 28.15           C  
-ATOM   3981  N   GLY B 151      97.603  29.608  24.593  1.00 30.53           N  
-ATOM   3982  CA  GLY B 151      97.646  29.211  25.990  1.00 30.90           C  
-ATOM   3983  C   GLY B 151      99.051  28.951  26.512  1.00 30.79           C  
-ATOM   3984  O   GLY B 151      99.249  28.110  27.392  1.00 31.68           O  
-ATOM   3985  N   LEU B 152     100.028  29.671  25.971  1.00 30.39           N  
-ATOM   3986  CA  LEU B 152     101.425  29.523  26.376  1.00 29.88           C  
-ATOM   3987  C   LEU B 152     101.792  30.525  27.467  1.00 29.63           C  
-ATOM   3988  O   LEU B 152     101.374  31.684  27.418  1.00 29.48           O  
-ATOM   3989  CB  LEU B 152     102.350  29.715  25.168  1.00 29.26           C  
-ATOM   3990  CG  LEU B 152     102.720  28.509  24.297  1.00 28.93           C  
-ATOM   3991  CD1 LEU B 152     101.530  27.614  24.009  1.00 29.67           C  
-ATOM   3992  CD2 LEU B 152     103.332  29.011  23.008  1.00 29.42           C  
-ATOM   3993  N   PRO B 154     102.550  30.078  28.486  1.00 29.53           N  
-ATOM   3994  CA  PRO B 154     102.987  30.925  29.604  1.00 29.37           C  
-ATOM   3995  C   PRO B 154     104.009  31.947  29.096  1.00 29.60           C  
-ATOM   3996  O   PRO B 154     105.019  31.574  28.495  1.00 29.49           O  
-ATOM   3997  CB  PRO B 154     103.643  29.920  30.553  1.00 29.63           C  
-ATOM   3998  CG  PRO B 154     102.990  28.609  30.202  1.00 28.98           C  
-ATOM   3999  CD  PRO B 154     102.952  28.678  28.709  1.00 29.32           C  
-ATOM   4000  N   VAL B 155     103.753  33.224  29.349  1.00 29.87           N  
-ATOM   4001  CA  VAL B 155     104.633  34.290  28.885  1.00 30.48           C  
-ATOM   4002  C   VAL B 155     105.322  35.065  30.008  1.00 31.09           C  
-ATOM   4003  O   VAL B 155     104.661  35.647  30.873  1.00 30.32           O  
-ATOM   4004  CB  VAL B 155     103.857  35.311  28.017  1.00 30.30           C  
-ATOM   4005  CG1 VAL B 155     104.819  36.280  27.349  1.00 30.19           C  
-ATOM   4006  CG2 VAL B 155     103.008  34.596  26.984  1.00 30.55           C  
-ATOM   4007  N   GLN B 156     106.651  35.078  29.969  1.00 31.69           N  
-ATOM   4008  CA  GLN B 156     107.465  35.807  30.940  1.00 31.94           C  
-ATOM   4009  C   GLN B 156     108.009  36.980  30.132  1.00 31.47           C  
-ATOM   4010  O   GLN B 156     108.144  36.888  28.909  1.00 31.37           O  
-ATOM   4011  CB  GLN B 156     108.669  34.980  31.414  1.00 33.51           C  
-ATOM   4012  CG  GLN B 156     108.469  33.476  31.512  1.00 36.59           C  
-ATOM   4013  CD  GLN B 156     107.849  33.039  32.818  1.00 37.95           C  
-ATOM   4014  OE1 GLN B 156     106.630  33.041  32.970  1.00 40.23           O  
-ATOM   4015  NE2 GLN B 156     108.683  32.620  33.758  1.00 37.62           N  
-ATOM   4016  N   THR B 157     108.340  38.075  30.798  1.00 30.13           N  
-ATOM   4017  CA  THR B 157     108.882  39.222  30.093  1.00 29.29           C  
-ATOM   4018  C   THR B 157     110.266  39.533  30.631  1.00 28.33           C  
-ATOM   4019  O   THR B 157     110.555  39.271  31.800  1.00 28.85           O  
-ATOM   4020  CB  THR B 157     107.992  40.464  30.255  1.00 29.24           C  
-ATOM   4021  OG1 THR B 157     107.850  40.778  31.645  1.00 29.62           O  
-ATOM   4022  CG2 THR B 157     106.621  40.219  29.653  1.00 29.59           C  
-ATOM   4023  N   TYR B 158     111.147  40.005  29.761  1.00 27.09           N  
-ATOM   4024  CA  TYR B 158     112.483  40.376  30.191  1.00 25.51           C  
-ATOM   4025  C   TYR B 158     112.629  41.867  29.971  1.00 25.58           C  
-ATOM   4026  O   TYR B 158     112.024  42.425  29.049  1.00 25.85           O  
-ATOM   4027  CB  TYR B 158     113.581  39.581  29.456  1.00 23.68           C  
-ATOM   4028  CG  TYR B 158     113.624  39.715  27.948  1.00 22.08           C  
-ATOM   4029  CD1 TYR B 158     114.190  40.832  27.338  1.00 21.37           C  
-ATOM   4030  CD2 TYR B 158     113.118  38.706  27.130  1.00 21.86           C  
-ATOM   4031  CE1 TYR B 158     114.252  40.941  25.953  1.00 20.60           C  
-ATOM   4032  CE2 TYR B 158     113.174  38.803  25.747  1.00 20.85           C  
-ATOM   4033  CZ  TYR B 158     113.738  39.924  25.160  1.00 20.89           C  
-ATOM   4034  OH  TYR B 158     113.764  40.032  23.783  1.00 19.06           O  
-ATOM   4035  N   ARG B 159     113.362  42.521  30.866  1.00 25.73           N  
-ATOM   4036  CA  ARG B 159     113.598  43.952  30.768  1.00 25.92           C  
-ATOM   4037  C   ARG B 159     114.360  44.232  29.478  1.00 25.28           C  
-ATOM   4038  O   ARG B 159     115.255  43.481  29.099  1.00 23.58           O  
-ATOM   4039  CB  ARG B 159     114.382  44.451  31.986  1.00 27.33           C  
-ATOM   4040  CG  ARG B 159     113.515  44.701  33.216  1.00 28.11           C  
-ATOM   4041  CD  ARG B 159     114.355  44.978  34.448  1.00 28.02           C  
-ATOM   4042  NE  ARG B 159     115.030  43.771  34.915  1.00 29.18           N  
-ATOM   4043  CZ  ARG B 159     115.934  43.741  35.889  1.00 29.26           C  
-ATOM   4044  NH1 ARG B 159     116.305  44.864  36.489  1.00 29.49           N  
-ATOM   4045  NH2 ARG B 159     116.487  42.589  36.246  1.00 28.13           N  
-ATOM   4046  N   TYR B 160     113.962  45.286  28.782  1.00 25.87           N  
-ATOM   4047  CA  TYR B 160     114.599  45.634  27.529  1.00 26.89           C  
-ATOM   4048  C   TYR B 160     114.682  47.140  27.347  1.00 28.63           C  
-ATOM   4049  O   TYR B 160     115.770  47.681  27.196  1.00 28.99           O  
-ATOM   4050  CB  TYR B 160     113.831  45.001  26.362  1.00 25.89           C  
-ATOM   4051  CG  TYR B 160     114.470  45.219  25.017  1.00 24.21           C  
-ATOM   4052  CD1 TYR B 160     115.501  44.392  24.579  1.00 23.88           C  
-ATOM   4053  CD2 TYR B 160     114.073  46.275  24.198  1.00 23.37           C  
-ATOM   4054  CE1 TYR B 160     116.129  44.612  23.362  1.00 23.89           C  
-ATOM   4055  CE2 TYR B 160     114.693  46.507  22.979  1.00 23.38           C  
-ATOM   4056  CZ  TYR B 160     115.722  45.672  22.565  1.00 24.15           C  
-ATOM   4057  OH  TYR B 160     116.348  45.903  21.363  1.00 23.59           O  
-ATOM   4058  N   PHE B 161     113.539  47.819  27.363  1.00 30.53           N  
-ATOM   4059  CA  PHE B 161     113.523  49.264  27.172  1.00 32.29           C  
-ATOM   4060  C   PHE B 161     113.766  50.041  28.460  1.00 34.82           C  
-ATOM   4061  O   PHE B 161     113.215  49.712  29.517  1.00 35.29           O  
-ATOM   4062  CB  PHE B 161     112.200  49.707  26.552  1.00 31.47           C  
-ATOM   4063  CG  PHE B 161     112.230  51.102  25.997  1.00 30.74           C  
-ATOM   4064  CD1 PHE B 161     113.099  51.432  24.964  1.00 30.36           C  
-ATOM   4065  CD2 PHE B 161     111.378  52.079  26.488  1.00 30.87           C  
-ATOM   4066  CE1 PHE B 161     113.118  52.708  24.428  1.00 29.59           C  
-ATOM   4067  CE2 PHE B 161     111.390  53.366  25.957  1.00 30.68           C  
-ATOM   4068  CZ  PHE B 161     112.262  53.679  24.924  1.00 30.21           C  
-ATOM   4069  N   ASP B 162     114.597  51.072  28.361  1.00 37.26           N  
-ATOM   4070  CA  ASP B 162     114.920  51.931  29.491  1.00 39.29           C  
-ATOM   4071  C   ASP B 162     114.161  53.228  29.252  1.00 39.97           C  
-ATOM   4072  O   ASP B 162     114.602  54.077  28.483  1.00 40.35           O  
-ATOM   4073  CB  ASP B 162     116.431  52.195  29.537  1.00 41.15           C  
-ATOM   4074  CG  ASP B 162     116.868  52.939  30.798  1.00 42.85           C  
-ATOM   4075  OD1 ASP B 162     116.244  53.965  31.156  1.00 43.12           O  
-ATOM   4076  OD2 ASP B 162     117.855  52.500  31.425  1.00 43.82           O  
-ATOM   4077  N   ALA B 163     113.027  53.379  29.926  1.00 41.26           N  
-ATOM   4078  CA  ALA B 163     112.178  54.565  29.782  1.00 41.97           C  
-ATOM   4079  C   ALA B 163     112.898  55.896  29.997  1.00 42.40           C  
-ATOM   4080  O   ALA B 163     112.524  56.910  29.409  1.00 42.85           O  
-ATOM   4081  CB  ALA B 163     110.981  54.462  30.717  1.00 42.36           C  
-ATOM   4082  N   GLU B 164     113.909  55.888  30.860  1.00 42.68           N  
-ATOM   4083  CA  GLU B 164     114.687  57.085  31.160  1.00 42.69           C  
-ATOM   4084  C   GLU B 164     115.581  57.488  29.994  1.00 42.14           C  
-ATOM   4085  O   GLU B 164     115.422  58.563  29.423  1.00 42.52           O  
-ATOM   4086  CB  GLU B 164     115.560  56.845  32.397  1.00 44.44           C  
-ATOM   4087  CG  GLU B 164     116.658  57.891  32.595  1.00 47.06           C  
-ATOM   4088  CD  GLU B 164     117.840  57.384  33.400  1.00 48.31           C  
-ATOM   4089  OE1 GLU B 164     118.015  56.150  33.517  1.00 49.70           O  
-ATOM   4090  OE2 GLU B 164     118.621  58.223  33.913  1.00 48.93           O  
-ATOM   4091  N   THR B 165     116.522  56.614  29.653  1.00 41.04           N  
-ATOM   4092  CA  THR B 165     117.470  56.872  28.576  1.00 39.82           C  
-ATOM   4093  C   THR B 165     116.911  56.627  27.180  1.00 39.15           C  
-ATOM   4094  O   THR B 165     117.550  56.979  26.188  1.00 39.46           O  
-ATOM   4095  CB  THR B 165     118.737  55.995  28.740  1.00 40.02           C  
-ATOM   4096  OG1 THR B 165     118.366  54.611  28.757  1.00 39.71           O  
-ATOM   4097  CG2 THR B 165     119.464  56.329  30.032  1.00 39.73           C  
-ATOM   4098  N   ARG B 166     115.730  56.018  27.108  1.00 37.91           N  
-ATOM   4099  CA  ARG B 166     115.097  55.674  25.836  1.00 36.17           C  
-ATOM   4100  C   ARG B 166     115.957  54.661  25.080  1.00 35.01           C  
-ATOM   4101  O   ARG B 166     115.739  54.408  23.892  1.00 34.96           O  
-ATOM   4102  CB  ARG B 166     114.856  56.910  24.964  1.00 37.44           C  
-ATOM   4103  CG  ARG B 166     113.450  57.479  25.036  1.00 39.08           C  
-ATOM   4104  CD  ARG B 166     113.226  58.335  26.271  1.00 39.95           C  
-ATOM   4105  NE  ARG B 166     111.917  58.987  26.226  1.00 41.40           N  
-ATOM   4106  CZ  ARG B 166     111.646  60.177  26.758  1.00 41.89           C  
-ATOM   4107  NH1 ARG B 166     112.589  60.866  27.389  1.00 42.24           N  
-ATOM   4108  NH2 ARG B 166     110.423  60.681  26.656  1.00 42.19           N  
-ATOM   4109  N   GLY B 167     116.932  54.084  25.775  1.00 33.46           N  
-ATOM   4110  CA  GLY B 167     117.804  53.099  25.167  1.00 31.88           C  
-ATOM   4111  C   GLY B 167     117.470  51.722  25.700  1.00 31.23           C  
-ATOM   4112  O   GLY B 167     116.350  51.474  26.145  1.00 32.15           O  
-ATOM   4113  N   VAL B 168     118.441  50.822  25.675  1.00 30.57           N  
-ATOM   4114  CA  VAL B 168     118.231  49.465  26.163  1.00 29.71           C  
-ATOM   4115  C   VAL B 168     118.777  49.285  27.581  1.00 30.00           C  
-ATOM   4116  O   VAL B 168     119.857  49.778  27.915  1.00 31.31           O  
-ATOM   4117  CB  VAL B 168     118.894  48.427  25.216  1.00 28.49           C  
-ATOM   4118  CG1 VAL B 168     118.822  47.021  25.807  1.00 27.54           C  
-ATOM   4119  CG2 VAL B 168     118.230  48.470  23.849  1.00 27.23           C  
-ATOM   4120  N   ASP B 169     118.004  48.612  28.422  1.00 29.59           N  
-ATOM   4121  CA  ASP B 169     118.396  48.312  29.790  1.00 29.05           C  
-ATOM   4122  C   ASP B 169     119.054  46.935  29.671  1.00 28.64           C  
-ATOM   4123  O   ASP B 169     118.479  45.917  30.050  1.00 28.66           O  
-ATOM   4124  CB  ASP B 169     117.145  48.260  30.677  1.00 30.65           C  
-ATOM   4125  CG  ASP B 169     117.439  47.820  32.106  1.00 31.67           C  
-ATOM   4126  OD1 ASP B 169     118.495  48.189  32.659  1.00 32.85           O  
-ATOM   4127  OD2 ASP B 169     116.594  47.104  32.685  1.00 32.03           O  
-ATOM   4128  N   PHE B 170     120.263  46.910  29.120  1.00 28.28           N  
-ATOM   4129  CA  PHE B 170     120.980  45.659  28.909  1.00 27.87           C  
-ATOM   4130  C   PHE B 170     121.276  44.882  30.186  1.00 28.29           C  
-ATOM   4131  O   PHE B 170     121.227  43.651  30.188  1.00 28.28           O  
-ATOM   4132  CB  PHE B 170     122.262  45.898  28.107  1.00 27.96           C  
-ATOM   4133  CG  PHE B 170     122.822  44.653  27.492  1.00 28.33           C  
-ATOM   4134  CD1 PHE B 170     122.024  43.844  26.690  1.00 28.27           C  
-ATOM   4135  CD2 PHE B 170     124.131  44.259  27.748  1.00 29.08           C  
-ATOM   4136  CE1 PHE B 170     122.518  42.657  26.159  1.00 28.67           C  
-ATOM   4137  CE2 PHE B 170     124.637  43.069  27.218  1.00 28.69           C  
-ATOM   4138  CZ  PHE B 170     123.825  42.268  26.424  1.00 28.76           C  
-ATOM   4139  N   GLU B 171     121.584  45.597  31.265  1.00 28.89           N  
-ATOM   4140  CA  GLU B 171     121.862  44.968  32.552  1.00 29.32           C  
-ATOM   4141  C   GLU B 171     120.640  44.208  33.054  1.00 28.84           C  
-ATOM   4142  O   GLU B 171     120.763  43.101  33.574  1.00 29.52           O  
-ATOM   4143  CB  GLU B 171     122.270  46.014  33.586  1.00 31.50           C  
-ATOM   4144  CG  GLU B 171     123.728  45.933  34.003  1.00 35.21           C  
-ATOM   4145  CD  GLU B 171     124.678  46.258  32.871  1.00 37.62           C  
-ATOM   4146  OE1 GLU B 171     125.016  47.451  32.707  1.00 40.47           O  
-ATOM   4147  OE2 GLU B 171     125.088  45.327  32.146  1.00 39.06           O  
-ATOM   4148  N   GLY B 172     119.463  44.808  32.901  1.00 28.14           N  
-ATOM   4149  CA  GLY B 172     118.237  44.156  33.328  1.00 27.44           C  
-ATOM   4150  C   GLY B 172     117.896  42.968  32.447  1.00 26.92           C  
-ATOM   4151  O   GLY B 172     117.428  41.941  32.934  1.00 26.87           O  
-ATOM   4152  N   MET B 173     118.128  43.115  31.144  1.00 26.76           N  
-ATOM   4153  CA  MET B 173     117.867  42.056  30.169  1.00 26.95           C  
-ATOM   4154  C   MET B 173     118.712  40.814  30.467  1.00 27.86           C  
-ATOM   4155  O   MET B 173     118.206  39.685  30.444  1.00 27.25           O  
-ATOM   4156  CB  MET B 173     118.155  42.565  28.751  1.00 25.49           C  
-ATOM   4157  CG  MET B 173     118.020  41.519  27.654  1.00 24.37           C  
-ATOM   4158  SD  MET B 173     118.157  42.240  26.000  1.00 26.08           S  
-ATOM   4159  CE  MET B 173     118.054  40.775  24.972  1.00 23.91           C  
-ATOM   4160  N   LYS B 174     119.997  41.030  30.744  1.00 28.72           N  
-ATOM   4161  CA  LYS B 174     120.916  39.938  31.058  1.00 29.33           C  
-ATOM   4162  C   LYS B 174     120.476  39.195  32.312  1.00 28.88           C  
-ATOM   4163  O   LYS B 174     120.544  37.966  32.370  1.00 28.36           O  
-ATOM   4164  CB  LYS B 174     122.341  40.459  31.257  1.00 30.26           C  
-ATOM   4165  CG  LYS B 174     123.043  40.888  29.982  1.00 31.53           C  
-ATOM   4166  CD  LYS B 174     124.557  40.919  30.175  1.00 33.49           C  
-ATOM   4167  CE  LYS B 174     125.060  42.215  30.798  1.00 34.61           C  
-ATOM   4168  NZ  LYS B 174     124.418  42.533  32.104  1.00 37.92           N  
-ATOM   4169  N   ALA B 175     120.015  39.952  33.304  1.00 28.88           N  
-ATOM   4170  CA  ALA B 175     119.558  39.392  34.568  1.00 29.74           C  
-ATOM   4171  C   ALA B 175     118.349  38.483  34.372  1.00 30.65           C  
-ATOM   4172  O   ALA B 175     118.365  37.310  34.764  1.00 31.45           O  
-ATOM   4173  CB  ALA B 175     119.218  40.509  35.540  1.00 28.82           C  
-ATOM   4174  N   ASP B 176     117.317  39.024  33.733  1.00 30.83           N  
-ATOM   4175  CA  ASP B 176     116.083  38.290  33.482  1.00 30.66           C  
-ATOM   4176  C   ASP B 176     116.273  37.068  32.595  1.00 31.51           C  
-ATOM   4177  O   ASP B 176     115.677  36.021  32.843  1.00 31.76           O  
-ATOM   4178  CB  ASP B 176     115.029  39.227  32.889  1.00 30.24           C  
-ATOM   4179  CG  ASP B 176     114.691  40.394  33.814  1.00 29.70           C  
-ATOM   4180  OD1 ASP B 176     115.051  40.357  35.010  1.00 29.42           O  
-ATOM   4181  OD2 ASP B 176     114.063  41.358  33.344  1.00 30.01           O  
-ATOM   4182  N   LEU B 177     117.122  37.187  31.581  1.00 32.96           N  
-ATOM   4183  CA  LEU B 177     117.374  36.070  30.673  1.00 33.89           C  
-ATOM   4184  C   LEU B 177     118.129  34.928  31.339  1.00 34.51           C  
-ATOM   4185  O   LEU B 177     117.901  33.759  31.022  1.00 34.10           O  
-ATOM   4186  CB  LEU B 177     118.111  36.537  29.415  1.00 33.48           C  
-ATOM   4187  CG  LEU B 177     117.276  37.395  28.460  1.00 33.59           C  
-ATOM   4188  CD1 LEU B 177     118.109  37.790  27.263  1.00 34.02           C  
-ATOM   4189  CD2 LEU B 177     116.026  36.634  28.019  1.00 33.59           C  
-ATOM   4190  N   ALA B 178     119.004  35.264  32.281  1.00 35.73           N  
-ATOM   4191  CA  ALA B 178     119.789  34.260  32.991  1.00 37.23           C  
-ATOM   4192  C   ALA B 178     118.907  33.345  33.831  1.00 38.28           C  
-ATOM   4193  O   ALA B 178     119.326  32.253  34.220  1.00 38.51           O  
-ATOM   4194  CB  ALA B 178     120.838  34.930  33.865  1.00 37.60           C  
-ATOM   4195  N   ALA B 179     117.687  33.795  34.110  1.00 39.52           N  
-ATOM   4196  CA  ALA B 179     116.737  33.018  34.900  1.00 40.62           C  
-ATOM   4197  C   ALA B 179     115.968  32.001  34.056  1.00 41.70           C  
-ATOM   4198  O   ALA B 179     115.194  31.203  34.592  1.00 42.46           O  
-ATOM   4199  CB  ALA B 179     115.766  33.947  35.614  1.00 40.36           C  
-ATOM   4200  N   ALA B 180     116.137  32.062  32.738  1.00 42.72           N  
-ATOM   4201  CA  ALA B 180     115.458  31.128  31.844  1.00 43.34           C  
-ATOM   4202  C   ALA B 180     116.028  29.734  32.054  1.00 44.16           C  
-ATOM   4203  O   ALA B 180     117.144  29.578  32.555  1.00 45.28           O  
-ATOM   4204  CB  ALA B 180     115.637  31.550  30.394  1.00 43.05           C  
-ATOM   4205  N   LYS B 181     115.263  28.722  31.673  1.00 44.39           N  
-ATOM   4206  CA  LYS B 181     115.709  27.346  31.819  1.00 44.94           C  
-ATOM   4207  C   LYS B 181     115.706  26.659  30.463  1.00 44.34           C  
-ATOM   4208  O   LYS B 181     115.157  27.195  29.497  1.00 44.69           O  
-ATOM   4209  CB  LYS B 181     114.840  26.585  32.835  1.00 46.17           C  
-ATOM   4210  CG  LYS B 181     113.346  26.916  32.826  1.00 48.19           C  
-ATOM   4211  CD  LYS B 181     113.020  28.219  33.579  1.00 49.77           C  
-ATOM   4212  CE  LYS B 181     111.508  28.492  33.588  1.00 50.77           C  
-ATOM   4213  NZ  LYS B 181     111.133  29.812  34.183  1.00 50.23           N  
-ATOM   4214  N   LYS B 182     116.358  25.504  30.372  1.00 43.84           N  
-ATOM   4215  CA  LYS B 182     116.411  24.770  29.113  1.00 43.29           C  
-ATOM   4216  C   LYS B 182     114.990  24.390  28.722  1.00 42.51           C  
-ATOM   4217  O   LYS B 182     114.170  24.045  29.582  1.00 42.70           O  
-ATOM   4218  CB  LYS B 182     117.299  23.524  29.243  1.00 44.10           C  
-ATOM   4219  CG  LYS B 182     116.693  22.389  30.054  1.00 46.19           C  
-ATOM   4220  CD  LYS B 182     117.734  21.347  30.450  1.00 47.52           C  
-ATOM   4221  CE  LYS B 182     118.652  21.865  31.558  1.00 48.47           C  
-ATOM   4222  NZ  LYS B 182     117.892  22.364  32.753  1.00 48.71           N  
-ATOM   4223  N   GLY B 183     114.682  24.502  27.435  1.00 40.75           N  
-ATOM   4224  CA  GLY B 183     113.344  24.176  26.974  1.00 38.64           C  
-ATOM   4225  C   GLY B 183     112.519  25.433  26.776  1.00 37.06           C  
-ATOM   4226  O   GLY B 183     111.504  25.415  26.077  1.00 36.80           O  
-ATOM   4227  N   ASP B 184     112.926  26.516  27.431  1.00 35.24           N  
-ATOM   4228  CA  ASP B 184     112.232  27.789  27.293  1.00 33.44           C  
-ATOM   4229  C   ASP B 184     112.621  28.426  25.971  1.00 31.86           C  
-ATOM   4230  O   ASP B 184     113.656  28.094  25.386  1.00 31.02           O  
-ATOM   4231  CB  ASP B 184     112.601  28.749  28.425  1.00 33.93           C  
-ATOM   4232  CG  ASP B 184     111.963  28.377  29.745  1.00 34.45           C  
-ATOM   4233  OD1 ASP B 184     111.284  27.329  29.837  1.00 34.80           O  
-ATOM   4234  OD2 ASP B 184     112.146  29.153  30.700  1.00 34.76           O  
-ATOM   4235  N   MET B 185     111.797  29.364  25.523  1.00 29.73           N  
-ATOM   4236  CA  MET B 185     112.045  30.058  24.279  1.00 28.02           C  
-ATOM   4237  C   MET B 185     112.189  31.540  24.565  1.00 26.60           C  
-ATOM   4238  O   MET B 185     111.448  32.107  25.372  1.00 25.64           O  
-ATOM   4239  CB  MET B 185     110.892  29.817  23.309  1.00 28.78           C  
-ATOM   4240  CG  MET B 185     111.012  30.548  21.995  1.00 29.55           C  
-ATOM   4241  SD  MET B 185     109.603  30.147  20.949  1.00 33.47           S  
-ATOM   4242  CE  MET B 185     110.249  28.746  20.059  1.00 30.58           C  
-ATOM   4243  N   VAL B 186     113.189  32.152  23.947  1.00 25.27           N  
-ATOM   4244  CA  VAL B 186     113.422  33.574  24.118  1.00 23.54           C  
-ATOM   4245  C   VAL B 186     113.179  34.231  22.772  1.00 21.62           C  
-ATOM   4246  O   VAL B 186     113.809  33.876  21.777  1.00 20.50           O  
-ATOM   4247  CB  VAL B 186     114.855  33.872  24.610  1.00 23.33           C  
-ATOM   4248  CG1 VAL B 186     115.043  35.377  24.804  1.00 23.07           C  
-ATOM   4249  CG2 VAL B 186     115.113  33.145  25.915  1.00 23.53           C  
-ATOM   4250  N   LEU B 187     112.212  35.137  22.741  1.00 20.61           N  
-ATOM   4251  CA  LEU B 187     111.863  35.845  21.524  1.00 19.83           C  
-ATOM   4252  C   LEU B 187     112.680  37.127  21.430  1.00 18.97           C  
-ATOM   4253  O   LEU B 187     112.609  37.983  22.317  1.00 17.37           O  
-ATOM   4254  CB  LEU B 187     110.359  36.153  21.516  1.00 20.99           C  
-ATOM   4255  CG  LEU B 187     109.725  36.881  20.324  1.00 22.02           C  
-ATOM   4256  CD1 LEU B 187     110.008  36.167  19.021  1.00 22.29           C  
-ATOM   4257  CD2 LEU B 187     108.237  36.956  20.549  1.00 23.14           C  
-ATOM   4258  N   LEU B 188     113.489  37.227  20.377  1.00 18.13           N  
-ATOM   4259  CA  LEU B 188     114.326  38.402  20.143  1.00 17.32           C  
-ATOM   4260  C   LEU B 188     113.965  39.032  18.804  1.00 16.19           C  
-ATOM   4261  O   LEU B 188     113.571  38.339  17.868  1.00 15.53           O  
-ATOM   4262  CB  LEU B 188     115.822  38.035  20.084  1.00 17.99           C  
-ATOM   4263  CG  LEU B 188     116.724  37.511  21.213  1.00 18.49           C  
-ATOM   4264  CD1 LEU B 188     116.488  38.272  22.501  1.00 19.30           C  
-ATOM   4265  CD2 LEU B 188     116.533  36.034  21.416  1.00 19.49           C  
-ATOM   4266  N   HIS B 189     114.090  40.350  18.719  1.00 16.18           N  
-ATOM   4267  CA  HIS B 189     113.836  41.058  17.474  1.00 16.68           C  
-ATOM   4268  C   HIS B 189     115.216  41.148  16.829  1.00 16.29           C  
-ATOM   4269  O   HIS B 189     116.162  41.609  17.464  1.00 16.44           O  
-ATOM   4270  CB  HIS B 189     113.282  42.459  17.735  1.00 16.31           C  
-ATOM   4271  CG  HIS B 189     111.951  42.470  18.424  1.00 17.56           C  
-ATOM   4272  ND1 HIS B 189     110.828  43.047  17.871  1.00 16.18           N  
-ATOM   4273  CD2 HIS B 189     111.572  42.009  19.640  1.00 18.34           C  
-ATOM   4274  CE1 HIS B 189     109.820  42.949  18.715  1.00 16.08           C  
-ATOM   4275  NE2 HIS B 189     110.244  42.322  19.798  1.00 17.02           N  
-ATOM   4276  N   GLY B 190     115.339  40.675  15.593  1.00 16.73           N  
-ATOM   4277  CA  GLY B 190     116.619  40.689  14.900  1.00 17.43           C  
-ATOM   4278  C   GLY B 190     117.247  42.060  14.748  1.00 17.95           C  
-ATOM   4279  O   GLY B 190     118.465  42.219  14.878  1.00 18.41           O  
-ATOM   4280  N   CYS B 191     116.407  43.049  14.473  1.00 17.74           N  
-ATOM   4281  CA  CYS B 191     116.844  44.428  14.295  1.00 18.71           C  
-ATOM   4282  C   CYS B 191     115.588  45.281  14.273  1.00 18.84           C  
-ATOM   4283  O   CYS B 191     114.482  44.739  14.285  1.00 19.56           O  
-ATOM   4284  CB  CYS B 191     117.580  44.580  12.960  1.00 18.77           C  
-ATOM   4285  SG  CYS B 191     116.552  44.245  11.492  1.00 19.32           S  
-ATOM   4286  N   CYS B 192     115.757  46.599  14.271  1.00 19.54           N  
-ATOM   4287  CA  CYS B 192     114.638  47.540  14.215  1.00 21.21           C  
-ATOM   4288  C   CYS B 192     113.497  47.129  15.154  1.00 21.11           C  
-ATOM   4289  O   CYS B 192     112.375  46.843  14.718  1.00 19.99           O  
-ATOM   4290  CB  CYS B 192     114.140  47.629  12.775  1.00 21.99           C  
-ATOM   4291  SG  CYS B 192     115.480  47.731  11.566  1.00 25.40           S  
-ATOM   4292  N   HIS B 193     113.802  47.117  16.447  1.00 21.39           N  
-ATOM   4293  CA  HIS B 193     112.860  46.720  17.480  1.00 21.58           C  
-ATOM   4294  C   HIS B 193     111.516  47.437  17.449  1.00 21.96           C  
-ATOM   4295  O   HIS B 193     111.438  48.649  17.625  1.00 22.50           O  
-ATOM   4296  CB  HIS B 193     113.501  46.872  18.861  1.00 21.27           C  
-ATOM   4297  CG  HIS B 193     112.657  46.350  19.982  1.00 22.15           C  
-ATOM   4298  ND1 HIS B 193     111.676  47.107  20.584  1.00 22.89           N  
-ATOM   4299  CD2 HIS B 193     112.646  45.153  20.613  1.00 22.49           C  
-ATOM   4300  CE1 HIS B 193     111.099  46.400  21.540  1.00 22.62           C  
-ATOM   4301  NE2 HIS B 193     111.669  45.210  21.577  1.00 21.83           N  
-ATOM   4302  N   ASN B 194     110.460  46.660  17.239  1.00 21.94           N  
-ATOM   4303  CA  ASN B 194     109.091  47.166  17.214  1.00 21.67           C  
-ATOM   4304  C   ASN B 194     108.567  46.915  18.630  1.00 22.11           C  
-ATOM   4305  O   ASN B 194     108.583  45.771  19.102  1.00 22.44           O  
-ATOM   4306  CB  ASN B 194     108.275  46.367  16.187  1.00 21.39           C  
-ATOM   4307  CG  ASN B 194     106.896  46.945  15.951  1.00 21.99           C  
-ATOM   4308  OD1 ASN B 194     106.449  47.818  16.691  1.00 21.90           O  
-ATOM   4309  ND2 ASN B 194     106.217  46.469  14.912  1.00 20.77           N  
-ATOM   4310  N   PRO B 195     108.006  47.943  19.298  1.00 22.38           N  
-ATOM   4311  CA  PRO B 195     107.768  49.345  18.931  1.00 22.41           C  
-ATOM   4312  C   PRO B 195     108.777  50.424  19.372  1.00 21.92           C  
-ATOM   4313  O   PRO B 195     108.610  51.590  19.023  1.00 21.38           O  
-ATOM   4314  CB  PRO B 195     106.436  49.608  19.617  1.00 22.13           C  
-ATOM   4315  CG  PRO B 195     106.667  48.967  20.945  1.00 21.34           C  
-ATOM   4316  CD  PRO B 195     107.348  47.645  20.587  1.00 21.61           C  
-ATOM   4317  N   THR B 196     109.807  50.055  20.127  1.00 21.61           N  
-ATOM   4318  CA  THR B 196     110.755  51.050  20.638  1.00 21.15           C  
-ATOM   4319  C   THR B 196     111.780  51.704  19.718  1.00 21.94           C  
-ATOM   4320  O   THR B 196     112.095  52.891  19.882  1.00 22.29           O  
-ATOM   4321  CB  THR B 196     111.516  50.518  21.856  1.00 19.91           C  
-ATOM   4322  OG1 THR B 196     112.397  49.466  21.450  1.00 17.97           O  
-ATOM   4323  CG2 THR B 196     110.543  49.999  22.897  1.00 20.07           C  
-ATOM   4324  N   GLY B 197     112.349  50.928  18.805  1.00 21.76           N  
-ATOM   4325  CA  GLY B 197     113.368  51.460  17.921  1.00 22.05           C  
-ATOM   4326  C   GLY B 197     114.741  51.372  18.574  1.00 22.40           C  
-ATOM   4327  O   GLY B 197     115.732  51.823  18.001  1.00 23.19           O  
-ATOM   4328  N   ALA B 198     114.794  50.816  19.787  1.00 22.68           N  
-ATOM   4329  CA  ALA B 198     116.039  50.650  20.546  1.00 22.36           C  
-ATOM   4330  C   ALA B 198     116.636  49.300  20.175  1.00 22.20           C  
-ATOM   4331  O   ALA B 198     115.965  48.278  20.302  1.00 21.87           O  
-ATOM   4332  CB  ALA B 198     115.762  50.708  22.049  1.00 22.17           C  
-ATOM   4333  N   ASN B 199     117.901  49.293  19.757  1.00 21.54           N  
-ATOM   4334  CA  ASN B 199     118.544  48.056  19.326  1.00 21.68           C  
-ATOM   4335  C   ASN B 199     119.842  47.666  20.015  1.00 21.70           C  
-ATOM   4336  O   ASN B 199     120.571  48.510  20.533  1.00 21.76           O  
-ATOM   4337  CB  ASN B 199     118.779  48.106  17.817  1.00 20.21           C  
-ATOM   4338  CG  ASN B 199     117.508  48.382  17.045  1.00 19.37           C  
-ATOM   4339  OD1 ASN B 199     116.556  47.599  17.095  1.00 19.55           O  
-ATOM   4340  ND2 ASN B 199     117.474  49.506  16.346  1.00 17.73           N  
-ATOM   4341  N   LEU B 200     120.127  46.367  19.993  1.00 22.52           N  
-ATOM   4342  CA  LEU B 200     121.337  45.818  20.588  1.00 23.90           C  
-ATOM   4343  C   LEU B 200     122.509  45.978  19.636  1.00 25.33           C  
-ATOM   4344  O   LEU B 200     122.330  45.936  18.415  1.00 25.96           O  
-ATOM   4345  CB  LEU B 200     121.170  44.324  20.878  1.00 23.19           C  
-ATOM   4346  CG  LEU B 200     120.172  43.854  21.937  1.00 24.38           C  
-ATOM   4347  CD1 LEU B 200     120.133  42.337  21.938  1.00 23.85           C  
-ATOM   4348  CD2 LEU B 200     120.561  44.374  23.315  1.00 23.73           C  
-ATOM   4349  N   THR B 201     123.699  46.175  20.197  1.00 26.49           N  
-ATOM   4350  CA  THR B 201     124.918  46.295  19.405  1.00 27.38           C  
-ATOM   4351  C   THR B 201     125.437  44.870  19.238  1.00 27.74           C  
-ATOM   4352  O   THR B 201     125.008  43.958  19.956  1.00 27.80           O  
-ATOM   4353  CB  THR B 201     125.991  47.109  20.130  1.00 27.32           C  
-ATOM   4354  OG1 THR B 201     126.379  46.420  21.326  1.00 28.91           O  
-ATOM   4355  CG2 THR B 201     125.475  48.498  20.473  1.00 27.95           C  
-ATOM   4356  N   LEU B 202     126.401  44.681  18.347  1.00 27.70           N  
-ATOM   4357  CA  LEU B 202     126.926  43.350  18.116  1.00 28.17           C  
-ATOM   4358  C   LEU B 202     127.602  42.777  19.351  1.00 28.31           C  
-ATOM   4359  O   LEU B 202     127.594  41.565  19.558  1.00 28.29           O  
-ATOM   4360  CB  LEU B 202     127.870  43.332  16.920  1.00 28.51           C  
-ATOM   4361  CG  LEU B 202     128.074  41.909  16.402  1.00 29.98           C  
-ATOM   4362  CD1 LEU B 202     126.726  41.340  15.974  1.00 29.74           C  
-ATOM   4363  CD2 LEU B 202     129.065  41.892  15.245  1.00 30.81           C  
-ATOM   4364  N   ASP B 203     128.166  43.646  20.183  1.00 29.39           N  
-ATOM   4365  CA  ASP B 203     128.824  43.194  21.405  1.00 30.11           C  
-ATOM   4366  C   ASP B 203     127.781  42.683  22.385  1.00 29.38           C  
-ATOM   4367  O   ASP B 203     127.985  41.657  23.036  1.00 29.10           O  
-ATOM   4368  CB  ASP B 203     129.641  44.320  22.032  1.00 32.78           C  
-ATOM   4369  CG  ASP B 203     130.845  44.689  21.198  1.00 35.58           C  
-ATOM   4370  OD1 ASP B 203     130.682  45.492  20.255  1.00 38.99           O  
-ATOM   4371  OD2 ASP B 203     131.947  44.164  21.468  1.00 37.20           O  
-ATOM   4372  N   GLN B 204     126.651  43.386  22.460  1.00 28.14           N  
-ATOM   4373  CA  GLN B 204     125.555  42.989  23.339  1.00 26.76           C  
-ATOM   4374  C   GLN B 204     124.970  41.658  22.854  1.00 25.67           C  
-ATOM   4375  O   GLN B 204     124.577  40.817  23.660  1.00 24.95           O  
-ATOM   4376  CB  GLN B 204     124.485  44.084  23.386  1.00 27.16           C  
-ATOM   4377  CG  GLN B 204     124.996  45.390  23.991  1.00 27.45           C  
-ATOM   4378  CD  GLN B 204     123.954  46.488  24.032  1.00 28.13           C  
-ATOM   4379  OE1 GLN B 204     123.233  46.719  23.062  1.00 28.71           O  
-ATOM   4380  NE2 GLN B 204     123.892  47.197  25.148  1.00 29.15           N  
-ATOM   4381  N   TRP B 205     124.964  41.457  21.539  1.00 24.90           N  
-ATOM   4382  CA  TRP B 205     124.464  40.222  20.941  1.00 24.70           C  
-ATOM   4383  C   TRP B 205     125.335  39.034  21.338  1.00 25.13           C  
-ATOM   4384  O   TRP B 205     124.824  37.966  21.690  1.00 24.66           O  
-ATOM   4385  CB  TRP B 205     124.440  40.333  19.417  1.00 24.40           C  
-ATOM   4386  CG  TRP B 205     123.205  40.961  18.852  1.00 24.77           C  
-ATOM   4387  CD1 TRP B 205     123.115  42.165  18.219  1.00 24.54           C  
-ATOM   4388  CD2 TRP B 205     121.901  40.371  18.780  1.00 24.93           C  
-ATOM   4389  NE1 TRP B 205     121.843  42.357  17.743  1.00 24.46           N  
-ATOM   4390  CE2 TRP B 205     121.075  41.274  18.072  1.00 25.08           C  
-ATOM   4391  CE3 TRP B 205     121.353  39.167  19.242  1.00 24.70           C  
-ATOM   4392  CZ2 TRP B 205     119.726  41.005  17.806  1.00 25.44           C  
-ATOM   4393  CZ3 TRP B 205     120.012  38.898  18.979  1.00 25.70           C  
-ATOM   4394  CH2 TRP B 205     119.213  39.816  18.267  1.00 26.30           C  
-ATOM   4395  N   ALA B 206     126.651  39.219  21.270  1.00 25.58           N  
-ATOM   4396  CA  ALA B 206     127.600  38.168  21.634  1.00 26.29           C  
-ATOM   4397  C   ALA B 206     127.381  37.784  23.092  1.00 26.51           C  
-ATOM   4398  O   ALA B 206     127.438  36.609  23.457  1.00 26.08           O  
-ATOM   4399  CB  ALA B 206     129.026  38.647  21.419  1.00 25.96           C  
-ATOM   4400  N   GLU B 207     127.103  38.792  23.912  1.00 27.46           N  
-ATOM   4401  CA  GLU B 207     126.846  38.608  25.336  1.00 29.03           C  
-ATOM   4402  C   GLU B 207     125.567  37.783  25.535  1.00 29.16           C  
-ATOM   4403  O   GLU B 207     125.505  36.905  26.397  1.00 29.28           O  
-ATOM   4404  CB  GLU B 207     126.696  39.972  26.000  1.00 29.99           C  
-ATOM   4405  CG  GLU B 207     126.493  39.914  27.489  1.00 33.63           C  
-ATOM   4406  CD  GLU B 207     127.716  40.364  28.257  1.00 34.91           C  
-ATOM   4407  OE1 GLU B 207     128.281  41.424  27.897  1.00 34.92           O  
-ATOM   4408  OE2 GLU B 207     128.097  39.659  29.221  1.00 35.30           O  
-ATOM   4409  N   ILE B 208     124.550  38.075  24.731  1.00 29.39           N  
-ATOM   4410  CA  ILE B 208     123.284  37.359  24.794  1.00 29.46           C  
-ATOM   4411  C   ILE B 208     123.480  35.901  24.387  1.00 29.51           C  
-ATOM   4412  O   ILE B 208     122.876  35.002  24.980  1.00 29.55           O  
-ATOM   4413  CB  ILE B 208     122.219  38.029  23.901  1.00 29.63           C  
-ATOM   4414  CG1 ILE B 208     121.831  39.386  24.494  1.00 29.52           C  
-ATOM   4415  CG2 ILE B 208     120.993  37.138  23.753  1.00 30.04           C  
-ATOM   4416  CD1 ILE B 208     121.305  39.307  25.920  1.00 29.85           C  
-ATOM   4417  N   ALA B 209     124.347  35.667  23.404  1.00 29.45           N  
-ATOM   4418  CA  ALA B 209     124.636  34.311  22.933  1.00 29.70           C  
-ATOM   4419  C   ALA B 209     125.212  33.463  24.062  1.00 29.85           C  
-ATOM   4420  O   ALA B 209     124.922  32.272  24.163  1.00 29.39           O  
-ATOM   4421  CB  ALA B 209     125.603  34.349  21.762  1.00 29.68           C  
-ATOM   4422  N   SER B 210     126.029  34.088  24.906  1.00 30.66           N  
-ATOM   4423  CA  SER B 210     126.641  33.413  26.046  1.00 31.53           C  
-ATOM   4424  C   SER B 210     125.572  32.939  27.022  1.00 31.62           C  
-ATOM   4425  O   SER B 210     125.591  31.793  27.475  1.00 31.21           O  
-ATOM   4426  CB  SER B 210     127.595  34.361  26.761  1.00 31.82           C  
-ATOM   4427  OG  SER B 210     128.541  34.881  25.846  1.00 35.23           O  
-ATOM   4428  N   ILE B 211     124.640  33.831  27.344  1.00 32.16           N  
-ATOM   4429  CA  ILE B 211     123.550  33.509  28.258  1.00 32.81           C  
-ATOM   4430  C   ILE B 211     122.696  32.382  27.684  1.00 32.89           C  
-ATOM   4431  O   ILE B 211     122.403  31.407  28.376  1.00 32.54           O  
-ATOM   4432  CB  ILE B 211     122.673  34.746  28.542  1.00 32.73           C  
-ATOM   4433  CG1 ILE B 211     123.489  35.785  29.315  1.00 33.49           C  
-ATOM   4434  CG2 ILE B 211     121.442  34.353  29.340  1.00 32.76           C  
-ATOM   4435  CD1 ILE B 211     122.777  37.103  29.534  1.00 33.86           C  
-ATOM   4436  N   LEU B 212     122.350  32.494  26.402  1.00 33.22           N  
-ATOM   4437  CA  LEU B 212     121.536  31.483  25.734  1.00 33.47           C  
-ATOM   4438  C   LEU B 212     122.169  30.097  25.784  1.00 34.39           C  
-ATOM   4439  O   LEU B 212     121.475  29.102  26.016  1.00 33.84           O  
-ATOM   4440  CB  LEU B 212     121.246  31.886  24.286  1.00 32.01           C  
-ATOM   4441  CG  LEU B 212     120.279  33.060  24.103  1.00 31.31           C  
-ATOM   4442  CD1 LEU B 212     120.135  33.381  22.629  1.00 31.03           C  
-ATOM   4443  CD2 LEU B 212     118.926  32.734  24.705  1.00 30.48           C  
-ATOM   4444  N   GLU B 213     123.480  30.024  25.568  1.00 36.00           N  
-ATOM   4445  CA  GLU B 213     124.166  28.738  25.608  1.00 37.76           C  
-ATOM   4446  C   GLU B 213     124.285  28.211  27.040  1.00 37.14           C  
-ATOM   4447  O   GLU B 213     124.175  27.006  27.266  1.00 36.79           O  
-ATOM   4448  CB  GLU B 213     125.528  28.795  24.888  1.00 40.62           C  
-ATOM   4449  CG  GLU B 213     126.506  29.863  25.376  1.00 45.31           C  
-ATOM   4450  CD  GLU B 213     127.760  29.999  24.502  1.00 47.37           C  
-ATOM   4451  OE1 GLU B 213     127.738  29.598  23.314  1.00 48.17           O  
-ATOM   4452  OE2 GLU B 213     128.775  30.530  25.008  1.00 48.60           O  
-ATOM   4453  N   LYS B 214     124.440  29.114  28.005  1.00 36.90           N  
-ATOM   4454  CA  LYS B 214     124.542  28.724  29.409  1.00 37.56           C  
-ATOM   4455  C   LYS B 214     123.227  28.174  29.956  1.00 37.28           C  
-ATOM   4456  O   LYS B 214     123.238  27.278  30.800  1.00 38.19           O  
-ATOM   4457  CB  LYS B 214     124.974  29.905  30.280  1.00 39.46           C  
-ATOM   4458  CG  LYS B 214     126.440  30.288  30.154  1.00 43.42           C  
-ATOM   4459  CD  LYS B 214     126.798  31.469  31.067  1.00 45.64           C  
-ATOM   4460  CE  LYS B 214     126.129  32.766  30.613  1.00 46.97           C  
-ATOM   4461  NZ  LYS B 214     126.465  33.930  31.483  1.00 47.08           N  
-ATOM   4462  N   THR B 215     122.102  28.731  29.505  1.00 36.05           N  
-ATOM   4463  CA  THR B 215     120.782  28.299  29.968  1.00 33.61           C  
-ATOM   4464  C   THR B 215     120.128  27.234  29.097  1.00 32.97           C  
-ATOM   4465  O   THR B 215     119.227  26.531  29.549  1.00 33.43           O  
-ATOM   4466  CB  THR B 215     119.809  29.484  30.080  1.00 33.39           C  
-ATOM   4467  OG1 THR B 215     119.723  30.157  28.817  1.00 33.41           O  
-ATOM   4468  CG2 THR B 215     120.276  30.462  31.142  1.00 33.77           C  
-ATOM   4469  N   GLY B 216     120.561  27.130  27.846  1.00 31.44           N  
-ATOM   4470  CA  GLY B 216     119.983  26.147  26.946  1.00 29.86           C  
-ATOM   4471  C   GLY B 216     118.629  26.564  26.389  1.00 29.53           C  
-ATOM   4472  O   GLY B 216     117.873  25.729  25.883  1.00 29.85           O  
-ATOM   4473  N   ALA B 217     118.306  27.850  26.504  1.00 28.58           N  
-ATOM   4474  CA  ALA B 217     117.042  28.374  25.999  1.00 27.31           C  
-ATOM   4475  C   ALA B 217     117.100  28.469  24.478  1.00 26.77           C  
-ATOM   4476  O   ALA B 217     118.135  28.823  23.909  1.00 26.99           O  
-ATOM   4477  CB  ALA B 217     116.758  29.743  26.599  1.00 26.96           C  
-ATOM   4478  N   LEU B 218     115.989  28.142  23.827  1.00 25.43           N  
-ATOM   4479  CA  LEU B 218     115.896  28.188  22.373  1.00 23.96           C  
-ATOM   4480  C   LEU B 218     115.517  29.583  21.899  1.00 23.13           C  
-ATOM   4481  O   LEU B 218     114.499  30.136  22.321  1.00 23.40           O  
-ATOM   4482  CB  LEU B 218     114.852  27.179  21.881  1.00 23.94           C  
-ATOM   4483  CG  LEU B 218     114.421  27.188  20.406  1.00 23.84           C  
-ATOM   4484  CD1 LEU B 218     115.591  26.924  19.472  1.00 22.54           C  
-ATOM   4485  CD2 LEU B 218     113.356  26.129  20.209  1.00 23.60           C  
-ATOM   4486  N   PRO B 219     116.371  30.207  21.077  1.00 22.35           N  
-ATOM   4487  CA  PRO B 219     116.039  31.546  20.588  1.00 21.31           C  
-ATOM   4488  C   PRO B 219     115.132  31.515  19.354  1.00 20.26           C  
-ATOM   4489  O   PRO B 219     115.299  30.681  18.453  1.00 20.38           O  
-ATOM   4490  CB  PRO B 219     117.407  32.126  20.245  1.00 20.40           C  
-ATOM   4491  CG  PRO B 219     118.145  30.920  19.755  1.00 21.42           C  
-ATOM   4492  CD  PRO B 219     117.776  29.874  20.781  1.00 21.52           C  
-ATOM   4493  N   LEU B 220     114.125  32.380  19.367  1.00 18.52           N  
-ATOM   4494  CA  LEU B 220     113.204  32.533  18.255  1.00 17.27           C  
-ATOM   4495  C   LEU B 220     113.445  33.981  17.857  1.00 16.91           C  
-ATOM   4496  O   LEU B 220     113.254  34.897  18.663  1.00 16.13           O  
-ATOM   4497  CB  LEU B 220     111.753  32.330  18.704  1.00 17.68           C  
-ATOM   4498  CG  LEU B 220     110.643  32.809  17.759  1.00 16.33           C  
-ATOM   4499  CD1 LEU B 220     110.794  32.208  16.376  1.00 15.91           C  
-ATOM   4500  CD2 LEU B 220     109.292  32.463  18.348  1.00 16.80           C  
-ATOM   4501  N   ILE B 221     113.932  34.186  16.642  1.00 16.32           N  
-ATOM   4502  CA  ILE B 221     114.225  35.528  16.179  1.00 15.35           C  
-ATOM   4503  C   ILE B 221     113.184  36.011  15.190  1.00 15.50           C  
-ATOM   4504  O   ILE B 221     112.895  35.346  14.197  1.00 15.89           O  
-ATOM   4505  CB  ILE B 221     115.646  35.596  15.551  1.00 16.08           C  
-ATOM   4506  CG1 ILE B 221     116.697  35.208  16.603  1.00 16.33           C  
-ATOM   4507  CG2 ILE B 221     115.927  36.984  14.997  1.00 14.09           C  
-ATOM   4508  CD1 ILE B 221     118.094  35.075  16.070  1.00 15.52           C  
-ATOM   4509  N   ASP B 222     112.578  37.147  15.510  1.00 16.02           N  
-ATOM   4510  CA  ASP B 222     111.581  37.766  14.650  1.00 16.21           C  
-ATOM   4511  C   ASP B 222     112.373  38.737  13.776  1.00 16.48           C  
-ATOM   4512  O   ASP B 222     112.886  39.751  14.270  1.00 15.99           O  
-ATOM   4513  CB  ASP B 222     110.554  38.525  15.511  1.00 16.45           C  
-ATOM   4514  CG  ASP B 222     109.378  39.066  14.703  1.00 16.42           C  
-ATOM   4515  OD1 ASP B 222     109.443  39.106  13.459  1.00 17.01           O  
-ATOM   4516  OD2 ASP B 222     108.373  39.464  15.324  1.00 16.52           O  
-ATOM   4517  N   LEU B 223     112.490  38.413  12.493  1.00 16.92           N  
-ATOM   4518  CA  LEU B 223     113.222  39.239  11.539  1.00 17.35           C  
-ATOM   4519  C   LEU B 223     112.225  39.825  10.546  1.00 17.21           C  
-ATOM   4520  O   LEU B 223     111.992  39.260   9.474  1.00 17.32           O  
-ATOM   4521  CB  LEU B 223     114.261  38.382  10.805  1.00 19.27           C  
-ATOM   4522  CG  LEU B 223     115.342  39.080   9.970  1.00 20.79           C  
-ATOM   4523  CD1 LEU B 223     116.208  39.963  10.862  1.00 21.14           C  
-ATOM   4524  CD2 LEU B 223     116.200  38.034   9.280  1.00 21.65           C  
-ATOM   4525  N   ALA B 224     111.666  40.982  10.885  1.00 17.53           N  
-ATOM   4526  CA  ALA B 224     110.665  41.620  10.034  1.00 17.76           C  
-ATOM   4527  C   ALA B 224     111.118  42.863   9.273  1.00 18.41           C  
-ATOM   4528  O   ALA B 224     110.473  43.264   8.299  1.00 18.34           O  
-ATOM   4529  CB  ALA B 224     109.427  41.941  10.859  1.00 17.52           C  
-ATOM   4530  N   TYR B 225     112.221  43.470   9.702  1.00 19.31           N  
-ATOM   4531  CA  TYR B 225     112.713  44.687   9.057  1.00 18.94           C  
-ATOM   4532  C   TYR B 225     114.152  44.646   8.538  1.00 17.93           C  
-ATOM   4533  O   TYR B 225     114.862  45.652   8.616  1.00 17.08           O  
-ATOM   4534  CB  TYR B 225     112.554  45.881  10.008  1.00 19.68           C  
-ATOM   4535  CG  TYR B 225     111.120  46.296  10.245  1.00 20.83           C  
-ATOM   4536  CD1 TYR B 225     110.477  47.171   9.372  1.00 20.22           C  
-ATOM   4537  CD2 TYR B 225     110.403  45.811  11.341  1.00 21.16           C  
-ATOM   4538  CE1 TYR B 225     109.162  47.552   9.582  1.00 20.94           C  
-ATOM   4539  CE2 TYR B 225     109.081  46.188  11.560  1.00 20.66           C  
-ATOM   4540  CZ  TYR B 225     108.468  47.057  10.677  1.00 21.17           C  
-ATOM   4541  OH  TYR B 225     107.161  47.433  10.871  1.00 21.67           O  
-ATOM   4542  N   GLN B 226     114.581  43.509   7.997  1.00 17.01           N  
-ATOM   4543  CA  GLN B 226     115.941  43.408   7.475  1.00 16.03           C  
-ATOM   4544  C   GLN B 226     116.105  44.365   6.290  1.00 15.78           C  
-ATOM   4545  O   GLN B 226     115.458  44.211   5.251  1.00 15.30           O  
-ATOM   4546  CB  GLN B 226     116.276  41.977   7.044  1.00 14.55           C  
-ATOM   4547  CG  GLN B 226     117.723  41.824   6.589  1.00 14.51           C  
-ATOM   4548  CD  GLN B 226     118.073  40.426   6.102  1.00 15.34           C  
-ATOM   4549  OE1 GLN B 226     117.218  39.542   6.034  1.00 15.45           O  
-ATOM   4550  NE2 GLN B 226     119.339  40.224   5.754  1.00 14.45           N  
-ATOM   4551  N   GLY B 227     116.973  45.353   6.463  1.00 15.59           N  
-ATOM   4552  CA  GLY B 227     117.210  46.337   5.423  1.00 16.25           C  
-ATOM   4553  C   GLY B 227     116.752  47.733   5.820  1.00 16.99           C  
-ATOM   4554  O   GLY B 227     117.103  48.704   5.166  1.00 16.95           O  
-ATOM   4555  N   PHE B 228     115.992  47.846   6.903  1.00 16.73           N  
-ATOM   4556  CA  PHE B 228     115.505  49.147   7.352  1.00 17.77           C  
-ATOM   4557  C   PHE B 228     116.346  49.786   8.451  1.00 17.49           C  
-ATOM   4558  O   PHE B 228     116.140  50.942   8.796  1.00 18.36           O  
-ATOM   4559  CB  PHE B 228     114.052  49.042   7.817  1.00 18.16           C  
-ATOM   4560  CG  PHE B 228     113.058  49.005   6.695  1.00 19.42           C  
-ATOM   4561  CD1 PHE B 228     112.523  50.185   6.186  1.00 20.92           C  
-ATOM   4562  CD2 PHE B 228     112.644  47.798   6.154  1.00 20.17           C  
-ATOM   4563  CE1 PHE B 228     111.587  50.162   5.151  1.00 21.14           C  
-ATOM   4564  CE2 PHE B 228     111.710  47.765   5.122  1.00 21.78           C  
-ATOM   4565  CZ  PHE B 228     111.180  48.953   4.619  1.00 21.61           C  
-ATOM   4566  N   GLY B 229     117.248  49.016   9.042  1.00 17.95           N  
-ATOM   4567  CA  GLY B 229     118.093  49.546  10.094  1.00 18.47           C  
-ATOM   4568  C   GLY B 229     119.356  50.180   9.536  1.00 20.04           C  
-ATOM   4569  O   GLY B 229     119.366  51.361   9.192  1.00 19.70           O  
-ATOM   4570  N   ASP B 230     120.420  49.386   9.444  1.00 20.40           N  
-ATOM   4571  CA  ASP B 230     121.704  49.845   8.938  1.00 20.85           C  
-ATOM   4572  C   ASP B 230     122.107  49.234   7.594  1.00 20.87           C  
-ATOM   4573  O   ASP B 230     123.154  49.572   7.049  1.00 23.46           O  
-ATOM   4574  CB  ASP B 230     122.795  49.567   9.971  1.00 21.09           C  
-ATOM   4575  CG  ASP B 230     122.579  50.326  11.266  1.00 22.67           C  
-ATOM   4576  OD1 ASP B 230     122.614  51.574  11.248  1.00 24.71           O  
-ATOM   4577  OD2 ASP B 230     122.383  49.675  12.312  1.00 24.49           O  
-ATOM   4578  N   GLY B 231     121.289  48.335   7.058  1.00 19.88           N  
-ATOM   4579  CA  GLY B 231     121.613  47.716   5.783  1.00 17.47           C  
-ATOM   4580  C   GLY B 231     121.257  46.245   5.782  1.00 16.73           C  
-ATOM   4581  O   GLY B 231     121.178  45.641   6.850  1.00 16.95           O  
-ATOM   4582  N   LEU B 233     121.033  45.673   4.600  1.00 16.01           N  
-ATOM   4583  CA  LEU B 233     120.678  44.258   4.469  1.00 15.36           C  
-ATOM   4584  C   LEU B 233     121.578  43.329   5.256  1.00 15.75           C  
-ATOM   4585  O   LEU B 233     121.103  42.554   6.086  1.00 16.07           O  
-ATOM   4586  CB  LEU B 233     120.712  43.822   3.007  1.00 14.83           C  
-ATOM   4587  CG  LEU B 233     119.481  44.078   2.153  1.00 14.80           C  
-ATOM   4588  CD1 LEU B 233     119.812  43.763   0.713  1.00 13.19           C  
-ATOM   4589  CD2 LEU B 233     118.323  43.223   2.654  1.00 14.52           C  
-ATOM   4590  N   GLU B 234     122.876  43.389   4.969  1.00 16.02           N  
-ATOM   4591  CA  GLU B 234     123.849  42.545   5.645  1.00 16.10           C  
-ATOM   4592  C   GLU B 234     123.990  42.907   7.116  1.00 16.56           C  
-ATOM   4593  O   GLU B 234     123.937  42.033   7.980  1.00 17.62           O  
-ATOM   4594  CB  GLU B 234     125.215  42.625   4.953  1.00 14.86           C  
-ATOM   4595  CG  GLU B 234     125.199  42.297   3.465  1.00 14.41           C  
-ATOM   4596  CD  GLU B 234     124.675  40.898   3.148  1.00 15.39           C  
-ATOM   4597  OE1 GLU B 234     124.785  39.989   3.996  1.00 15.56           O  
-ATOM   4598  OE2 GLU B 234     124.161  40.699   2.031  1.00 16.31           O  
-ATOM   4599  N   GLU B 235     124.111  44.199   7.404  1.00 17.60           N  
-ATOM   4600  CA  GLU B 235     124.285  44.652   8.780  1.00 18.23           C  
-ATOM   4601  C   GLU B 235     123.117  44.302   9.701  1.00 17.80           C  
-ATOM   4602  O   GLU B 235     123.324  43.963  10.869  1.00 18.16           O  
-ATOM   4603  CB  GLU B 235     124.589  46.153   8.812  1.00 20.54           C  
-ATOM   4604  CG  GLU B 235     125.078  46.680  10.167  1.00 25.06           C  
-ATOM   4605  CD  GLU B 235     126.261  45.898  10.725  1.00 29.05           C  
-ATOM   4606  OE1 GLU B 235     127.228  45.639   9.968  1.00 30.91           O  
-ATOM   4607  OE2 GLU B 235     126.219  45.538  11.926  1.00 30.31           O  
-ATOM   4608  N   ASP B 236     121.897  44.340   9.176  1.00 17.04           N  
-ATOM   4609  CA  ASP B 236     120.723  44.016   9.981  1.00 17.06           C  
-ATOM   4610  C   ASP B 236     120.618  42.542  10.340  1.00 17.09           C  
-ATOM   4611  O   ASP B 236     119.895  42.176  11.264  1.00 17.14           O  
-ATOM   4612  CB  ASP B 236     119.446  44.481   9.290  1.00 17.27           C  
-ATOM   4613  CG  ASP B 236     119.331  45.991   9.243  1.00 17.52           C  
-ATOM   4614  OD1 ASP B 236     120.100  46.673   9.948  1.00 17.89           O  
-ATOM   4615  OD2 ASP B 236     118.476  46.504   8.499  1.00 17.35           O  
-ATOM   4616  N   ALA B 237     121.333  41.701   9.599  1.00 16.97           N  
-ATOM   4617  CA  ALA B 237     121.340  40.261   9.848  1.00 17.00           C  
-ATOM   4618  C   ALA B 237     122.522  39.831  10.740  1.00 16.41           C  
-ATOM   4619  O   ALA B 237     122.580  38.689  11.198  1.00 15.41           O  
-ATOM   4620  CB  ALA B 237     121.374  39.505   8.521  1.00 16.35           C  
-ATOM   4621  N   ALA B 238     123.427  40.768  11.024  1.00 16.85           N  
-ATOM   4622  CA  ALA B 238     124.620  40.509  11.836  1.00 16.25           C  
-ATOM   4623  C   ALA B 238     124.353  39.780  13.150  1.00 16.20           C  
-ATOM   4624  O   ALA B 238     125.021  38.787  13.462  1.00 16.65           O  
-ATOM   4625  CB  ALA B 238     125.375  41.816  12.103  1.00 15.27           C  
-ATOM   4626  N   GLY B 239     123.393  40.279  13.922  1.00 15.44           N  
-ATOM   4627  CA  GLY B 239     123.058  39.659  15.192  1.00 15.14           C  
-ATOM   4628  C   GLY B 239     122.492  38.256  15.035  1.00 15.30           C  
-ATOM   4629  O   GLY B 239     122.809  37.360  15.822  1.00 15.01           O  
-ATOM   4630  N   THR B 240     121.663  38.066  14.012  1.00 14.96           N  
-ATOM   4631  CA  THR B 240     121.045  36.773  13.736  1.00 15.98           C  
-ATOM   4632  C   THR B 240     122.117  35.757  13.349  1.00 15.79           C  
-ATOM   4633  O   THR B 240     122.119  34.622  13.826  1.00 15.01           O  
-ATOM   4634  CB  THR B 240     119.990  36.893  12.605  1.00 15.99           C  
-ATOM   4635  OG1 THR B 240     118.995  37.856  12.980  1.00 17.39           O  
-ATOM   4636  CG2 THR B 240     119.311  35.563  12.355  1.00 15.79           C  
-ATOM   4637  N   ARG B 241     123.054  36.192  12.518  1.00 16.45           N  
-ATOM   4638  CA  ARG B 241     124.150  35.340  12.072  1.00 17.00           C  
-ATOM   4639  C   ARG B 241     125.065  34.971  13.236  1.00 17.02           C  
-ATOM   4640  O   ARG B 241     125.597  33.868  13.291  1.00 18.08           O  
-ATOM   4641  CB  ARG B 241     124.921  36.037  10.951  1.00 16.61           C  
-ATOM   4642  CG  ARG B 241     124.036  36.298   9.748  1.00 16.85           C  
-ATOM   4643  CD  ARG B 241     124.717  37.072   8.643  1.00 16.54           C  
-ATOM   4644  NE  ARG B 241     123.827  37.169   7.486  1.00 17.17           N  
-ATOM   4645  CZ  ARG B 241     124.037  37.944   6.429  1.00 17.18           C  
-ATOM   4646  NH1 ARG B 241     125.122  38.703   6.363  1.00 17.17           N  
-ATOM   4647  NH2 ARG B 241     123.139  37.981   5.455  1.00 16.92           N  
-ATOM   4648  N   LEU B 242     125.196  35.876  14.197  1.00 18.22           N  
-ATOM   4649  CA  LEU B 242     126.021  35.615  15.362  1.00 19.53           C  
-ATOM   4650  C   LEU B 242     125.383  34.520  16.231  1.00 20.34           C  
-ATOM   4651  O   LEU B 242     126.072  33.595  16.660  1.00 21.58           O  
-ATOM   4652  CB  LEU B 242     126.254  36.906  16.161  1.00 19.48           C  
-ATOM   4653  CG  LEU B 242     127.282  36.810  17.298  1.00 20.42           C  
-ATOM   4654  CD1 LEU B 242     128.079  38.092  17.410  1.00 20.44           C  
-ATOM   4655  CD2 LEU B 242     126.607  36.474  18.615  1.00 20.14           C  
-ATOM   4656  N   ILE B 243     124.079  34.617  16.495  1.00 20.99           N  
-ATOM   4657  CA  ILE B 243     123.398  33.596  17.301  1.00 20.77           C  
-ATOM   4658  C   ILE B 243     123.418  32.257  16.570  1.00 21.07           C  
-ATOM   4659  O   ILE B 243     123.620  31.220  17.191  1.00 21.64           O  
-ATOM   4660  CB  ILE B 243     121.912  33.975  17.661  1.00 21.17           C  
-ATOM   4661  CG1 ILE B 243     121.866  34.905  18.874  1.00 20.57           C  
-ATOM   4662  CG2 ILE B 243     121.092  32.723  18.029  1.00 18.74           C  
-ATOM   4663  CD1 ILE B 243     122.448  36.243  18.631  1.00 22.82           C  
-ATOM   4664  N   ALA B 244     123.258  32.291  15.252  1.00 21.41           N  
-ATOM   4665  CA  ALA B 244     123.240  31.075  14.444  1.00 23.34           C  
-ATOM   4666  C   ALA B 244     124.573  30.323  14.430  1.00 25.43           C  
-ATOM   4667  O   ALA B 244     124.609  29.108  14.203  1.00 25.72           O  
-ATOM   4668  CB  ALA B 244     122.802  31.397  13.023  1.00 21.42           C  
-ATOM   4669  N   SER B 245     125.671  31.043  14.620  1.00 27.14           N  
-ATOM   4670  CA  SER B 245     126.979  30.409  14.621  1.00 29.12           C  
-ATOM   4671  C   SER B 245     127.313  29.920  16.017  1.00 29.73           C  
-ATOM   4672  O   SER B 245     128.093  28.991  16.188  1.00 31.04           O  
-ATOM   4673  CB  SER B 245     128.043  31.390  14.135  1.00 29.44           C  
-ATOM   4674  OG  SER B 245     128.016  32.563  14.916  1.00 32.15           O  
-ATOM   4675  N   ARG B 246     126.729  30.566  17.016  1.00 30.80           N  
-ATOM   4676  CA  ARG B 246     126.962  30.195  18.400  1.00 31.78           C  
-ATOM   4677  C   ARG B 246     126.039  29.074  18.880  1.00 31.52           C  
-ATOM   4678  O   ARG B 246     126.499  28.015  19.297  1.00 32.72           O  
-ATOM   4679  CB  ARG B 246     126.799  31.421  19.299  1.00 33.91           C  
-ATOM   4680  CG  ARG B 246     128.016  32.313  19.372  1.00 37.38           C  
-ATOM   4681  CD  ARG B 246     128.694  32.178  20.731  1.00 41.82           C  
-ATOM   4682  NE  ARG B 246     128.881  33.487  21.362  1.00 45.49           N  
-ATOM   4683  CZ  ARG B 246     129.374  33.680  22.583  1.00 46.33           C  
-ATOM   4684  NH1 ARG B 246     129.741  32.650  23.338  1.00 47.39           N  
-ATOM   4685  NH2 ARG B 246     129.501  34.917  23.049  1.00 47.33           N  
-ATOM   4686  N   ILE B 247     124.736  29.323  18.824  1.00 30.34           N  
-ATOM   4687  CA  ILE B 247     123.730  28.375  19.274  1.00 28.56           C  
-ATOM   4688  C   ILE B 247     123.402  27.348  18.194  1.00 28.27           C  
-ATOM   4689  O   ILE B 247     123.009  27.707  17.084  1.00 28.55           O  
-ATOM   4690  CB  ILE B 247     122.457  29.128  19.702  1.00 29.24           C  
-ATOM   4691  CG1 ILE B 247     122.833  30.266  20.664  1.00 29.19           C  
-ATOM   4692  CG2 ILE B 247     121.451  28.181  20.341  1.00 27.80           C  
-ATOM   4693  CD1 ILE B 247     123.720  29.838  21.827  1.00 29.54           C  
-ATOM   4694  N   PRO B 248     123.543  26.049  18.521  1.00 27.64           N  
-ATOM   4695  CA  PRO B 248     123.279  24.918  17.617  1.00 27.37           C  
-ATOM   4696  C   PRO B 248     121.841  24.758  17.106  1.00 26.95           C  
-ATOM   4697  O   PRO B 248     121.617  24.189  16.030  1.00 26.59           O  
-ATOM   4698  CB  PRO B 248     123.703  23.713  18.456  1.00 27.24           C  
-ATOM   4699  CG  PRO B 248     123.436  24.163  19.858  1.00 26.93           C  
-ATOM   4700  CD  PRO B 248     123.989  25.561  19.838  1.00 27.07           C  
-ATOM   4701  N   GLU B 249     120.877  25.261  17.869  1.00 26.00           N  
-ATOM   4702  CA  GLU B 249     119.474  25.151  17.501  1.00 25.56           C  
-ATOM   4703  C   GLU B 249     118.802  26.515  17.632  1.00 24.16           C  
-ATOM   4704  O   GLU B 249     118.786  27.101  18.709  1.00 24.26           O  
-ATOM   4705  CB  GLU B 249     118.804  24.133  18.420  1.00 26.88           C  
-ATOM   4706  CG  GLU B 249     117.482  23.593  17.936  1.00 29.71           C  
-ATOM   4707  CD  GLU B 249     116.948  22.506  18.852  1.00 31.42           C  
-ATOM   4708  OE1 GLU B 249     116.414  22.839  19.934  1.00 32.69           O  
-ATOM   4709  OE2 GLU B 249     117.074  21.315  18.495  1.00 31.63           O  
-ATOM   4710  N   VAL B 250     118.251  27.021  16.536  1.00 23.19           N  
-ATOM   4711  CA  VAL B 250     117.596  28.326  16.548  1.00 22.07           C  
-ATOM   4712  C   VAL B 250     116.487  28.417  15.507  1.00 20.88           C  
-ATOM   4713  O   VAL B 250     116.562  27.798  14.449  1.00 21.33           O  
-ATOM   4714  CB  VAL B 250     118.647  29.489  16.373  1.00 23.52           C  
-ATOM   4715  CG1 VAL B 250     119.803  29.041  15.507  1.00 25.17           C  
-ATOM   4716  CG2 VAL B 250     118.010  30.747  15.773  1.00 23.18           C  
-ATOM   4717  N   LEU B 251     115.439  29.162  15.838  1.00 19.47           N  
-ATOM   4718  CA  LEU B 251     114.301  29.358  14.947  1.00 17.61           C  
-ATOM   4719  C   LEU B 251     114.272  30.812  14.477  1.00 15.42           C  
-ATOM   4720  O   LEU B 251     114.477  31.728  15.274  1.00 13.91           O  
-ATOM   4721  CB  LEU B 251     112.998  29.036  15.693  1.00 17.99           C  
-ATOM   4722  CG  LEU B 251     112.372  27.635  15.648  1.00 18.72           C  
-ATOM   4723  CD1 LEU B 251     113.415  26.539  15.752  1.00 18.60           C  
-ATOM   4724  CD2 LEU B 251     111.344  27.523  16.769  1.00 17.92           C  
-ATOM   4725  N   ILE B 252     114.018  31.030  13.191  1.00 14.34           N  
-ATOM   4726  CA  ILE B 252     113.951  32.392  12.659  1.00 14.40           C  
-ATOM   4727  C   ILE B 252     112.676  32.584  11.849  1.00 14.09           C  
-ATOM   4728  O   ILE B 252     112.422  31.842  10.902  1.00 14.81           O  
-ATOM   4729  CB  ILE B 252     115.165  32.729  11.748  1.00 14.47           C  
-ATOM   4730  CG1 ILE B 252     116.482  32.516  12.498  1.00 13.87           C  
-ATOM   4731  CG2 ILE B 252     115.072  34.173  11.268  1.00 13.84           C  
-ATOM   4732  CD1 ILE B 252     117.704  32.511  11.592  1.00 15.09           C  
-ATOM   4733  N   ALA B 253     111.864  33.559  12.249  1.00 14.72           N  
-ATOM   4734  CA  ALA B 253     110.611  33.879  11.565  1.00 14.65           C  
-ATOM   4735  C   ALA B 253     110.852  35.157  10.762  1.00 15.15           C  
-ATOM   4736  O   ALA B 253     111.002  36.243  11.338  1.00 15.23           O  
-ATOM   4737  CB  ALA B 253     109.502  34.090  12.581  1.00 13.26           C  
-ATOM   4738  N   ALA B 254     110.918  35.023   9.441  1.00 13.99           N  
-ATOM   4739  CA  ALA B 254     111.177  36.165   8.572  1.00 14.16           C  
-ATOM   4740  C   ALA B 254     109.959  36.647   7.786  1.00 14.61           C  
-ATOM   4741  O   ALA B 254     109.130  35.849   7.340  1.00 14.75           O  
-ATOM   4742  CB  ALA B 254     112.317  35.836   7.613  1.00 13.72           C  
-ATOM   4743  N   SER B 255     109.891  37.956   7.574  1.00 13.90           N  
-ATOM   4744  CA  SER B 255     108.800  38.565   6.834  1.00 13.12           C  
-ATOM   4745  C   SER B 255     109.322  39.298   5.608  1.00 13.77           C  
-ATOM   4746  O   SER B 255     110.332  40.000   5.683  1.00 15.13           O  
-ATOM   4747  CB  SER B 255     108.060  39.561   7.723  1.00 12.80           C  
-ATOM   4748  OG  SER B 255     107.092  40.284   6.981  1.00 13.63           O  
-ATOM   4749  N   CYS B 256     108.635  39.131   4.483  1.00 13.66           N  
-ATOM   4750  CA  CYS B 256     109.000  39.809   3.243  1.00 12.82           C  
-ATOM   4751  C   CYS B 256     108.026  40.963   2.994  1.00 12.24           C  
-ATOM   4752  O   CYS B 256     108.124  41.658   1.983  1.00 10.21           O  
-ATOM   4753  CB  CYS B 256     108.929  38.847   2.058  1.00 13.37           C  
-ATOM   4754  SG  CYS B 256     109.982  37.402   2.188  1.00 15.05           S  
-ATOM   4755  N   SER B 257     107.104  41.174   3.933  1.00 12.81           N  
-ATOM   4756  CA  SER B 257     106.095  42.222   3.809  1.00 13.08           C  
-ATOM   4757  C   SER B 257     106.639  43.631   3.658  1.00 13.98           C  
-ATOM   4758  O   SER B 257     106.269  44.342   2.719  1.00 15.45           O  
-ATOM   4759  CB  SER B 257     105.123  42.185   4.991  1.00 12.27           C  
-ATOM   4760  OG  SER B 257     104.388  40.974   5.015  1.00 12.87           O  
-ATOM   4761  N   LYS B 258     107.527  44.029   4.563  1.00 13.23           N  
-ATOM   4762  CA  LYS B 258     108.074  45.374   4.530  1.00 13.40           C  
-ATOM   4763  C   LYS B 258     109.297  45.603   3.637  1.00 13.87           C  
-ATOM   4764  O   LYS B 258     109.332  46.592   2.896  1.00 14.47           O  
-ATOM   4765  CB  LYS B 258     108.315  45.878   5.954  1.00 14.18           C  
-ATOM   4766  CG  LYS B 258     107.038  45.969   6.791  1.00 13.76           C  
-ATOM   4767  CD  LYS B 258     107.061  45.028   7.980  1.00 13.75           C  
-ATOM   4768  CE  LYS B 258     105.790  45.184   8.818  1.00 16.05           C  
-ATOM   4769  NZ  LYS B 258     105.914  44.540  10.132  1.00 15.95           N  
-ATOM   4770  N   ASN B 259     110.274  44.697   3.653  1.00 12.66           N  
-ATOM   4771  CA  ASN B 259     111.449  44.904   2.812  1.00 12.99           C  
-ATOM   4772  C   ASN B 259     111.245  44.689   1.305  1.00 12.91           C  
-ATOM   4773  O   ASN B 259     112.042  45.172   0.496  1.00 13.13           O  
-ATOM   4774  CB  ASN B 259     112.701  44.190   3.358  1.00 14.15           C  
-ATOM   4775  CG  ASN B 259     112.579  42.680   3.384  1.00 15.30           C  
-ATOM   4776  OD1 ASN B 259     111.634  42.095   2.847  1.00 16.11           O  
-ATOM   4777  ND2 ASN B 259     113.554  42.035   4.012  1.00 15.06           N  
-ATOM   4778  N   PHE B 260     110.170  43.999   0.924  1.00 12.46           N  
-ATOM   4779  CA  PHE B 260     109.851  43.802  -0.493  1.00 11.86           C  
-ATOM   4780  C   PHE B 260     108.571  44.568  -0.858  1.00 12.63           C  
-ATOM   4781  O   PHE B 260     108.140  44.564  -2.016  1.00 12.79           O  
-ATOM   4782  CB  PHE B 260     109.691  42.315  -0.841  1.00 12.40           C  
-ATOM   4783  CG  PHE B 260     110.997  41.580  -1.001  1.00 12.07           C  
-ATOM   4784  CD1 PHE B 260     111.617  40.981   0.097  1.00 10.75           C  
-ATOM   4785  CD2 PHE B 260     111.613  41.494  -2.250  1.00 10.79           C  
-ATOM   4786  CE1 PHE B 260     112.832  40.307  -0.049  1.00 10.47           C  
-ATOM   4787  CE2 PHE B 260     112.823  40.825  -2.404  1.00 10.28           C  
-ATOM   4788  CZ  PHE B 260     113.433  40.230  -1.302  1.00 10.37           C  
-ATOM   4789  N   GLY B 261     107.960  45.206   0.138  1.00 12.56           N  
-ATOM   4790  CA  GLY B 261     106.743  45.973  -0.083  1.00 13.26           C  
-ATOM   4791  C   GLY B 261     105.549  45.178  -0.588  1.00 13.68           C  
-ATOM   4792  O   GLY B 261     104.683  45.722  -1.282  1.00 14.05           O  
-ATOM   4793  N   ILE B 262     105.475  43.905  -0.213  1.00 13.32           N  
-ATOM   4794  CA  ILE B 262     104.382  43.028  -0.646  1.00 13.36           C  
-ATOM   4795  C   ILE B 262     103.500  42.581   0.518  1.00 13.35           C  
-ATOM   4796  O   ILE B 262     103.042  41.444   0.559  1.00 14.22           O  
-ATOM   4797  CB  ILE B 262     104.927  41.775  -1.381  1.00 11.99           C  
-ATOM   4798  CG1 ILE B 262     105.982  41.078  -0.516  1.00 10.83           C  
-ATOM   4799  CG2 ILE B 262     105.503  42.163  -2.742  1.00 10.60           C  
-ATOM   4800  CD1 ILE B 262     106.606  39.874  -1.178  1.00 11.65           C  
-ATOM   4801  N   TYR B 263     103.242  43.505   1.437  1.00 14.47           N  
-ATOM   4802  CA  TYR B 263     102.428  43.271   2.633  1.00 15.07           C  
-ATOM   4803  C   TYR B 263     101.202  42.363   2.433  1.00 16.18           C  
-ATOM   4804  O   TYR B 263     101.057  41.351   3.123  1.00 16.48           O  
-ATOM   4805  CB  TYR B 263     101.946  44.613   3.214  1.00 14.64           C  
-ATOM   4806  CG  TYR B 263     102.983  45.716   3.289  1.00 14.66           C  
-ATOM   4807  CD1 TYR B 263     103.329  46.456   2.153  1.00 14.46           C  
-ATOM   4808  CD2 TYR B 263     103.607  46.036   4.495  1.00 14.50           C  
-ATOM   4809  CE1 TYR B 263     104.269  47.483   2.216  1.00 13.36           C  
-ATOM   4810  CE2 TYR B 263     104.549  47.065   4.569  1.00 13.60           C  
-ATOM   4811  CZ  TYR B 263     104.875  47.781   3.426  1.00 14.03           C  
-ATOM   4812  OH  TYR B 263     105.816  48.787   3.495  1.00 14.72           O  
-ATOM   4813  N   ARG B 264     100.321  42.735   1.503  1.00 16.34           N  
-ATOM   4814  CA  ARG B 264      99.089  41.976   1.243  1.00 17.08           C  
-ATOM   4815  C   ARG B 264      99.245  40.599   0.585  1.00 17.12           C  
-ATOM   4816  O   ARG B 264      98.275  39.836   0.521  1.00 17.56           O  
-ATOM   4817  CB  ARG B 264      98.083  42.820   0.440  1.00 15.61           C  
-ATOM   4818  CG  ARG B 264      98.519  43.134  -0.990  1.00 16.00           C  
-ATOM   4819  CD  ARG B 264      97.468  43.933  -1.763  1.00 15.15           C  
-ATOM   4820  NE  ARG B 264      97.102  45.166  -1.069  1.00 14.13           N  
-ATOM   4821  CZ  ARG B 264      96.220  46.058  -1.515  1.00 12.72           C  
-ATOM   4822  NH1 ARG B 264      95.616  45.883  -2.681  1.00 10.86           N  
-ATOM   4823  NH2 ARG B 264      95.960  47.141  -0.798  1.00 11.14           N  
-ATOM   4824  N   GLU B 265     100.439  40.280   0.084  1.00 15.72           N  
-ATOM   4825  CA  GLU B 265     100.661  38.979  -0.555  1.00 15.29           C  
-ATOM   4826  C   GLU B 265     100.797  37.850   0.468  1.00 14.45           C  
-ATOM   4827  O   GLU B 265     100.544  36.681   0.166  1.00 14.18           O  
-ATOM   4828  CB  GLU B 265     101.897  39.016  -1.457  1.00 16.55           C  
-ATOM   4829  CG  GLU B 265     101.834  40.060  -2.567  1.00 17.88           C  
-ATOM   4830  CD  GLU B 265     100.759  39.789  -3.605  1.00 19.91           C  
-ATOM   4831  OE1 GLU B 265     100.259  38.647  -3.712  1.00 21.32           O  
-ATOM   4832  OE2 GLU B 265     100.419  40.731  -4.340  1.00 21.26           O  
-ATOM   4833  N   ARG B 266     101.189  38.214   1.683  1.00 13.52           N  
-ATOM   4834  CA  ARG B 266     101.359  37.267   2.772  1.00 13.23           C  
-ATOM   4835  C   ARG B 266     102.477  36.267   2.469  1.00 14.19           C  
-ATOM   4836  O   ARG B 266     102.242  35.091   2.156  1.00 13.45           O  
-ATOM   4837  CB  ARG B 266     100.036  36.561   3.086  1.00 12.24           C  
-ATOM   4838  CG  ARG B 266      98.837  37.500   3.225  1.00 10.55           C  
-ATOM   4839  CD  ARG B 266      99.122  38.703   4.119  1.00  9.22           C  
-ATOM   4840  NE  ARG B 266      99.393  38.332   5.507  1.00 10.08           N  
-ATOM   4841  CZ  ARG B 266     100.325  38.902   6.269  1.00 10.66           C  
-ATOM   4842  NH1 ARG B 266     101.089  39.875   5.787  1.00  9.47           N  
-ATOM   4843  NH2 ARG B 266     100.495  38.500   7.516  1.00 10.26           N  
-ATOM   4844  N   THR B 267     103.709  36.747   2.586  1.00 14.07           N  
-ATOM   4845  CA  THR B 267     104.863  35.913   2.326  1.00 14.64           C  
-ATOM   4846  C   THR B 267     105.975  36.115   3.347  1.00 14.06           C  
-ATOM   4847  O   THR B 267     106.348  37.244   3.681  1.00 14.18           O  
-ATOM   4848  CB  THR B 267     105.367  36.074   0.864  1.00 14.37           C  
-ATOM   4849  OG1 THR B 267     106.796  36.170   0.831  1.00 17.24           O  
-ATOM   4850  CG2 THR B 267     104.749  37.274   0.204  1.00 13.85           C  
-ATOM   4851  N   GLY B 268     106.429  34.995   3.890  1.00 13.82           N  
-ATOM   4852  CA  GLY B 268     107.495  34.969   4.874  1.00 12.86           C  
-ATOM   4853  C   GLY B 268     107.899  33.515   5.001  1.00 13.18           C  
-ATOM   4854  O   GLY B 268     107.417  32.672   4.237  1.00 12.36           O  
-ATOM   4855  N   CYS B 269     108.793  33.200   5.926  1.00 14.52           N  
-ATOM   4856  CA  CYS B 269     109.192  31.814   6.103  1.00 16.02           C  
-ATOM   4857  C   CYS B 269     109.828  31.549   7.452  1.00 15.46           C  
-ATOM   4858  O   CYS B 269     110.344  32.460   8.108  1.00 15.65           O  
-ATOM   4859  CB  CYS B 269     110.117  31.346   4.973  1.00 18.78           C  
-ATOM   4860  SG  CYS B 269     111.819  31.880   5.095  1.00 25.24           S  
-ATOM   4861  N   LEU B 270     109.724  30.303   7.892  1.00 14.98           N  
-ATOM   4862  CA  LEU B 270     110.288  29.891   9.160  1.00 14.54           C  
-ATOM   4863  C   LEU B 270     111.496  29.035   8.860  1.00 15.13           C  
-ATOM   4864  O   LEU B 270     111.430  28.133   8.020  1.00 15.28           O  
-ATOM   4865  CB  LEU B 270     109.266  29.084   9.961  1.00 14.08           C  
-ATOM   4866  CG  LEU B 270     109.749  28.466  11.275  1.00 14.61           C  
-ATOM   4867  CD1 LEU B 270     110.113  29.547  12.275  1.00 13.94           C  
-ATOM   4868  CD2 LEU B 270     108.670  27.556  11.832  1.00 15.50           C  
-ATOM   4869  N   LEU B 271     112.610  29.346   9.514  1.00 16.03           N  
-ATOM   4870  CA  LEU B 271     113.840  28.589   9.342  1.00 15.16           C  
-ATOM   4871  C   LEU B 271     114.134  27.916  10.670  1.00 15.16           C  
-ATOM   4872  O   LEU B 271     114.056  28.553  11.726  1.00 13.57           O  
-ATOM   4873  CB  LEU B 271     114.984  29.526   8.970  1.00 16.09           C  
-ATOM   4874  CG  LEU B 271     114.799  30.320   7.678  1.00 17.65           C  
-ATOM   4875  CD1 LEU B 271     115.641  31.574   7.741  1.00 19.31           C  
-ATOM   4876  CD2 LEU B 271     115.163  29.476   6.466  1.00 18.31           C  
-ATOM   4877  N   ALA B 272     114.413  26.617  10.618  1.00 16.08           N  
-ATOM   4878  CA  ALA B 272     114.727  25.840  11.814  1.00 17.18           C  
-ATOM   4879  C   ALA B 272     116.144  25.290  11.698  1.00 18.05           C  
-ATOM   4880  O   ALA B 272     116.398  24.382  10.901  1.00 17.35           O  
-ATOM   4881  CB  ALA B 272     113.732  24.699  11.983  1.00 16.31           C  
-ATOM   4882  N   LEU B 273     117.074  25.894  12.433  1.00 19.78           N  
-ATOM   4883  CA  LEU B 273     118.470  25.458  12.422  1.00 20.72           C  
-ATOM   4884  C   LEU B 273     118.628  24.380  13.482  1.00 21.30           C  
-ATOM   4885  O   LEU B 273     118.348  24.609  14.659  1.00 21.30           O  
-ATOM   4886  CB  LEU B 273     119.422  26.618  12.715  1.00 20.83           C  
-ATOM   4887  CG  LEU B 273     119.195  27.973  12.039  1.00 22.05           C  
-ATOM   4888  CD1 LEU B 273     120.516  28.714  12.012  1.00 22.35           C  
-ATOM   4889  CD2 LEU B 273     118.661  27.820  10.632  1.00 22.43           C  
-ATOM   4890  N   CYS B 274     119.090  23.212  13.055  1.00 22.72           N  
-ATOM   4891  CA  CYS B 274     119.266  22.065  13.937  1.00 24.80           C  
-ATOM   4892  C   CYS B 274     120.730  21.646  14.059  1.00 25.65           C  
-ATOM   4893  O   CYS B 274     121.558  21.969  13.205  1.00 25.32           O  
-ATOM   4894  CB  CYS B 274     118.439  20.896  13.405  1.00 24.72           C  
-ATOM   4895  SG  CYS B 274     116.781  21.375  12.835  1.00 26.10           S  
-ATOM   4896  N   ALA B 275     121.033  20.914  15.123  1.00 27.00           N  
-ATOM   4897  CA  ALA B 275     122.384  20.435  15.388  1.00 28.53           C  
-ATOM   4898  C   ALA B 275     122.869  19.365  14.407  1.00 29.59           C  
-ATOM   4899  O   ALA B 275     124.064  19.271  14.133  1.00 30.67           O  
-ATOM   4900  CB  ALA B 275     122.484  19.927  16.815  1.00 28.57           C  
-ATOM   4901  N   ASP B 276     121.955  18.554  13.885  1.00 30.10           N  
-ATOM   4902  CA  ASP B 276     122.335  17.511  12.938  1.00 31.14           C  
-ATOM   4903  C   ASP B 276     121.271  17.287  11.878  1.00 31.28           C  
-ATOM   4904  O   ASP B 276     120.126  17.709  12.042  1.00 31.41           O  
-ATOM   4905  CB  ASP B 276     122.638  16.199  13.665  1.00 32.28           C  
-ATOM   4906  CG  ASP B 276     121.541  15.796  14.619  1.00 33.30           C  
-ATOM   4907  OD1 ASP B 276     120.562  15.173  14.169  1.00 34.19           O  
-ATOM   4908  OD2 ASP B 276     121.657  16.111  15.821  1.00 35.51           O  
-ATOM   4909  N   ALA B 277     121.648  16.581  10.816  1.00 31.46           N  
-ATOM   4910  CA  ALA B 277     120.754  16.291   9.698  1.00 31.80           C  
-ATOM   4911  C   ALA B 277     119.528  15.472  10.089  1.00 31.94           C  
-ATOM   4912  O   ALA B 277     118.455  15.638   9.511  1.00 32.29           O  
-ATOM   4913  CB  ALA B 277     121.519  15.596   8.585  1.00 31.40           C  
-ATOM   4914  N   ALA B 278     119.683  14.588  11.068  1.00 32.21           N  
-ATOM   4915  CA  ALA B 278     118.574  13.757  11.521  1.00 32.03           C  
-ATOM   4916  C   ALA B 278     117.472  14.632  12.110  1.00 32.22           C  
-ATOM   4917  O   ALA B 278     116.312  14.510  11.728  1.00 33.25           O  
-ATOM   4918  CB  ALA B 278     119.055  12.748  12.541  1.00 31.10           C  
-ATOM   4919  N   THR B 279     117.842  15.529  13.020  1.00 32.35           N  
-ATOM   4920  CA  THR B 279     116.879  16.431  13.647  1.00 32.30           C  
-ATOM   4921  C   THR B 279     116.297  17.355  12.582  1.00 32.27           C  
-ATOM   4922  O   THR B 279     115.138  17.770  12.664  1.00 32.01           O  
-ATOM   4923  CB  THR B 279     117.539  17.296  14.739  1.00 32.23           C  
-ATOM   4924  OG1 THR B 279     118.381  16.477  15.557  1.00 33.75           O  
-ATOM   4925  CG2 THR B 279     116.487  17.936  15.617  1.00 32.57           C  
-ATOM   4926  N   ARG B 280     117.113  17.673  11.582  1.00 31.89           N  
-ATOM   4927  CA  ARG B 280     116.690  18.533  10.493  1.00 32.46           C  
-ATOM   4928  C   ARG B 280     115.541  17.865   9.747  1.00 32.90           C  
-ATOM   4929  O   ARG B 280     114.548  18.510   9.409  1.00 32.85           O  
-ATOM   4930  CB  ARG B 280     117.861  18.795   9.552  1.00 33.82           C  
-ATOM   4931  CG  ARG B 280     117.557  19.776   8.446  1.00 36.21           C  
-ATOM   4932  CD  ARG B 280     117.350  19.078   7.127  1.00 38.55           C  
-ATOM   4933  NE  ARG B 280     116.635  19.940   6.197  1.00 43.29           N  
-ATOM   4934  CZ  ARG B 280     116.914  20.054   4.903  1.00 45.17           C  
-ATOM   4935  NH1 ARG B 280     117.926  19.381   4.371  1.00 46.45           N  
-ATOM   4936  NH2 ARG B 280     116.191  20.868   4.147  1.00 45.93           N  
-ATOM   4937  N   GLU B 281     115.676  16.564   9.512  1.00 32.97           N  
-ATOM   4938  CA  GLU B 281     114.648  15.791   8.827  1.00 32.73           C  
-ATOM   4939  C   GLU B 281     113.369  15.768   9.657  1.00 30.55           C  
-ATOM   4940  O   GLU B 281     112.271  15.896   9.116  1.00 30.35           O  
-ATOM   4941  CB  GLU B 281     115.143  14.367   8.574  1.00 35.47           C  
-ATOM   4942  CG  GLU B 281     116.239  14.282   7.521  1.00 40.82           C  
-ATOM   4943  CD  GLU B 281     117.228  13.145   7.775  1.00 44.98           C  
-ATOM   4944  OE1 GLU B 281     116.819  12.089   8.319  1.00 46.57           O  
-ATOM   4945  OE2 GLU B 281     118.424  13.315   7.433  1.00 46.68           O  
-ATOM   4946  N   LEU B 282     113.516  15.617  10.970  1.00 28.41           N  
-ATOM   4947  CA  LEU B 282     112.369  15.596  11.873  1.00 27.28           C  
-ATOM   4948  C   LEU B 282     111.621  16.924  11.818  1.00 26.01           C  
-ATOM   4949  O   LEU B 282     110.394  16.955  11.655  1.00 25.76           O  
-ATOM   4950  CB  LEU B 282     112.811  15.335  13.318  1.00 27.26           C  
-ATOM   4951  CG  LEU B 282     112.977  13.895  13.803  1.00 27.92           C  
-ATOM   4952  CD1 LEU B 282     113.685  13.885  15.149  1.00 27.73           C  
-ATOM   4953  CD2 LEU B 282     111.615  13.228  13.912  1.00 27.61           C  
-ATOM   4954  N   ALA B 283     112.373  18.014  11.953  1.00 23.67           N  
-ATOM   4955  CA  ALA B 283     111.815  19.355  11.941  1.00 21.55           C  
-ATOM   4956  C   ALA B 283     111.116  19.649  10.625  1.00 21.01           C  
-ATOM   4957  O   ALA B 283     109.978  20.116  10.614  1.00 21.43           O  
-ATOM   4958  CB  ALA B 283     112.903  20.379  12.209  1.00 20.87           C  
-ATOM   4959  N   GLN B 284     111.775  19.320   9.518  1.00 19.71           N  
-ATOM   4960  CA  GLN B 284     111.213  19.562   8.200  1.00 19.57           C  
-ATOM   4961  C   GLN B 284     109.878  18.852   8.037  1.00 19.63           C  
-ATOM   4962  O   GLN B 284     108.914  19.437   7.532  1.00 19.98           O  
-ATOM   4963  CB  GLN B 284     112.179  19.115   7.107  1.00 19.44           C  
-ATOM   4964  CG  GLN B 284     111.784  19.595   5.722  1.00 21.50           C  
-ATOM   4965  CD  GLN B 284     111.697  21.111   5.632  1.00 22.72           C  
-ATOM   4966  OE1 GLN B 284     112.710  21.800   5.512  1.00 24.02           O  
-ATOM   4967  NE2 GLN B 284     110.483  21.637   5.698  1.00 24.18           N  
-ATOM   4968  N   GLY B 285     109.816  17.600   8.478  1.00 18.54           N  
-ATOM   4969  CA  GLY B 285     108.583  16.843   8.370  1.00 17.80           C  
-ATOM   4970  C   GLY B 285     107.459  17.434   9.205  1.00 17.87           C  
-ATOM   4971  O   GLY B 285     106.318  17.526   8.744  1.00 17.73           O  
-ATOM   4972  N   ALA B 286     107.779  17.838  10.433  1.00 17.16           N  
-ATOM   4973  CA  ALA B 286     106.796  18.419  11.340  1.00 17.31           C  
-ATOM   4974  C   ALA B 286     106.298  19.772  10.840  1.00 18.11           C  
-ATOM   4975  O   ALA B 286     105.151  20.146  11.080  1.00 18.31           O  
-ATOM   4976  CB  ALA B 286     107.389  18.559  12.731  1.00 16.56           C  
-ATOM   4977  N   MET B 287     107.175  20.512  10.171  1.00 18.16           N  
-ATOM   4978  CA  MET B 287     106.825  21.816   9.634  1.00 18.16           C  
-ATOM   4979  C   MET B 287     105.875  21.664   8.447  1.00 17.75           C  
-ATOM   4980  O   MET B 287     104.902  22.409   8.322  1.00 17.00           O  
-ATOM   4981  CB  MET B 287     108.093  22.583   9.236  1.00 19.99           C  
-ATOM   4982  CG  MET B 287     108.874  23.154  10.425  1.00 20.78           C  
-ATOM   4983  SD  MET B 287     110.565  23.666   9.980  1.00 26.38           S  
-ATOM   4984  CE  MET B 287     110.338  25.363   9.551  1.00 22.67           C  
-ATOM   4985  N   ALA B 288     106.150  20.684   7.591  1.00 17.08           N  
-ATOM   4986  CA  ALA B 288     105.309  20.415   6.428  1.00 17.62           C  
-ATOM   4987  C   ALA B 288     103.929  19.976   6.923  1.00 18.78           C  
-ATOM   4988  O   ALA B 288     102.895  20.405   6.404  1.00 19.47           O  
-ATOM   4989  CB  ALA B 288     105.931  19.330   5.575  1.00 16.33           C  
-ATOM   4990  N   PHE B 289     103.932  19.131   7.950  1.00 18.86           N  
-ATOM   4991  CA  PHE B 289     102.713  18.627   8.568  1.00 17.44           C  
-ATOM   4992  C   PHE B 289     101.873  19.812   9.067  1.00 17.89           C  
-ATOM   4993  O   PHE B 289     100.658  19.859   8.852  1.00 18.37           O  
-ATOM   4994  CB  PHE B 289     103.095  17.702   9.727  1.00 17.00           C  
-ATOM   4995  CG  PHE B 289     101.933  17.228  10.548  1.00 17.81           C  
-ATOM   4996  CD1 PHE B 289     101.114  16.203  10.093  1.00 17.38           C  
-ATOM   4997  CD2 PHE B 289     101.664  17.802  11.786  1.00 17.97           C  
-ATOM   4998  CE1 PHE B 289     100.042  15.757  10.857  1.00 17.98           C  
-ATOM   4999  CE2 PHE B 289     100.589  17.361  12.559  1.00 18.65           C  
-ATOM   5000  CZ  PHE B 289      99.779  16.337  12.094  1.00 18.16           C  
-ATOM   5001  N   LEU B 290     102.537  20.775   9.701  1.00 17.84           N  
-ATOM   5002  CA  LEU B 290     101.891  21.972  10.239  1.00 18.20           C  
-ATOM   5003  C   LEU B 290     101.141  22.782   9.181  1.00 18.05           C  
-ATOM   5004  O   LEU B 290     100.042  23.277   9.441  1.00 17.22           O  
-ATOM   5005  CB  LEU B 290     102.922  22.844  10.957  1.00 18.21           C  
-ATOM   5006  CG  LEU B 290     102.898  22.863  12.486  1.00 18.91           C  
-ATOM   5007  CD1 LEU B 290     102.428  21.547  13.064  1.00 20.21           C  
-ATOM   5008  CD2 LEU B 290     104.271  23.220  13.000  1.00 18.72           C  
-ATOM   5009  N   ASN B 291     101.731  22.923   7.996  1.00 17.60           N  
-ATOM   5010  CA  ASN B 291     101.084  23.655   6.907  1.00 17.59           C  
-ATOM   5011  C   ASN B 291      99.897  22.849   6.407  1.00 17.90           C  
-ATOM   5012  O   ASN B 291      98.818  23.389   6.153  1.00 18.73           O  
-ATOM   5013  CB  ASN B 291     102.047  23.868   5.736  1.00 17.06           C  
-ATOM   5014  CG  ASN B 291     102.752  25.202   5.792  1.00 16.72           C  
-ATOM   5015  OD1 ASN B 291     102.690  25.910   6.799  1.00 16.45           O  
-ATOM   5016  ND2 ASN B 291     103.428  25.557   4.708  1.00 15.43           N  
-ATOM   5017  N   ARG B 292     100.096  21.544   6.290  1.00 17.76           N  
-ATOM   5018  CA  ARG B 292      99.059  20.650   5.804  1.00 18.97           C  
-ATOM   5019  C   ARG B 292      97.786  20.702   6.659  1.00 18.29           C  
-ATOM   5020  O   ARG B 292      96.684  20.824   6.126  1.00 18.85           O  
-ATOM   5021  CB  ARG B 292      99.613  19.221   5.725  1.00 20.79           C  
-ATOM   5022  CG  ARG B 292      98.826  18.282   4.824  1.00 24.09           C  
-ATOM   5023  CD  ARG B 292      99.678  17.109   4.346  1.00 27.19           C  
-ATOM   5024  NE  ARG B 292      99.979  16.155   5.410  1.00 31.19           N  
-ATOM   5025  CZ  ARG B 292     101.192  15.672   5.680  1.00 33.21           C  
-ATOM   5026  NH1 ARG B 292     102.250  16.054   4.969  1.00 34.38           N  
-ATOM   5027  NH2 ARG B 292     101.343  14.776   6.648  1.00 33.99           N  
-ATOM   5028  N   GLN B 293      97.945  20.690   7.977  1.00 17.03           N  
-ATOM   5029  CA  GLN B 293      96.805  20.700   8.892  1.00 17.34           C  
-ATOM   5030  C   GLN B 293      96.161  22.071   9.110  1.00 17.05           C  
-ATOM   5031  O   GLN B 293      95.063  22.163   9.664  1.00 17.05           O  
-ATOM   5032  CB  GLN B 293      97.207  20.108  10.255  1.00 17.80           C  
-ATOM   5033  CG  GLN B 293      97.958  18.772  10.192  1.00 19.31           C  
-ATOM   5034  CD  GLN B 293      97.244  17.717   9.360  1.00 18.70           C  
-ATOM   5035  OE1 GLN B 293      96.049  17.502   9.500  1.00 21.40           O  
-ATOM   5036  NE2 GLN B 293      97.981  17.057   8.490  1.00 19.55           N  
-ATOM   5037  N   THR B 294      96.849  23.132   8.700  1.00 16.21           N  
-ATOM   5038  CA  THR B 294      96.332  24.484   8.883  1.00 14.86           C  
-ATOM   5039  C   THR B 294      95.668  25.084   7.647  1.00 13.54           C  
-ATOM   5040  O   THR B 294      94.636  25.727   7.758  1.00 13.74           O  
-ATOM   5041  CB  THR B 294      97.443  25.436   9.393  1.00 15.21           C  
-ATOM   5042  OG1 THR B 294      98.077  24.847  10.541  1.00 14.06           O  
-ATOM   5043  CG2 THR B 294      96.859  26.796   9.772  1.00 12.91           C  
-ATOM   5044  N   TYR B 295      96.258  24.881   6.474  1.00 13.19           N  
-ATOM   5045  CA  TYR B 295      95.705  25.427   5.232  1.00 13.04           C  
-ATOM   5046  C   TYR B 295      96.211  24.710   3.989  1.00 13.61           C  
-ATOM   5047  O   TYR B 295      96.045  25.194   2.866  1.00 12.64           O  
-ATOM   5048  CB  TYR B 295      96.012  26.926   5.122  1.00 13.08           C  
-ATOM   5049  CG  TYR B 295      97.435  27.300   5.477  1.00 14.08           C  
-ATOM   5050  CD1 TYR B 295      98.511  26.882   4.688  1.00 14.44           C  
-ATOM   5051  CD2 TYR B 295      97.708  28.054   6.614  1.00 14.69           C  
-ATOM   5052  CE1 TYR B 295      99.824  27.203   5.029  1.00 15.57           C  
-ATOM   5053  CE2 TYR B 295      99.020  28.380   6.965  1.00 16.10           C  
-ATOM   5054  CZ  TYR B 295     100.070  27.954   6.167  1.00 15.26           C  
-ATOM   5055  OH  TYR B 295     101.355  28.296   6.510  1.00 15.51           O  
-ATOM   5056  N   SER B 296      96.817  23.546   4.188  1.00 15.15           N  
-ATOM   5057  CA  SER B 296      97.350  22.769   3.080  1.00 18.02           C  
-ATOM   5058  C   SER B 296      98.597  23.493   2.548  1.00 18.61           C  
-ATOM   5059  O   SER B 296      99.542  23.713   3.301  1.00 21.37           O  
-ATOM   5060  CB  SER B 296      96.277  22.601   1.996  1.00 18.14           C  
-ATOM   5061  OG  SER B 296      96.449  21.411   1.259  1.00 20.70           O  
-ATOM   5062  N   PHE B 297      98.577  23.926   1.294  1.00 18.48           N  
-ATOM   5063  CA  PHE B 297      99.723  24.606   0.695  1.00 17.99           C  
-ATOM   5064  C   PHE B 297      99.802  26.098   1.019  1.00 18.15           C  
-ATOM   5065  O   PHE B 297      98.783  26.747   1.275  1.00 18.34           O  
-ATOM   5066  CB  PHE B 297      99.686  24.444  -0.823  1.00 17.70           C  
-ATOM   5067  CG  PHE B 297      99.605  23.023  -1.274  1.00 18.58           C  
-ATOM   5068  CD1 PHE B 297      98.370  22.413  -1.460  1.00 18.56           C  
-ATOM   5069  CD2 PHE B 297     100.762  22.295  -1.532  1.00 18.92           C  
-ATOM   5070  CE1 PHE B 297      98.285  21.100  -1.897  1.00 17.89           C  
-ATOM   5071  CE2 PHE B 297     100.689  20.981  -1.971  1.00 19.38           C  
-ATOM   5072  CZ  PHE B 297      99.443  20.382  -2.155  1.00 19.04           C  
-ATOM   5073  N   PRO B 298     101.025  26.652   1.057  1.00 17.44           N  
-ATOM   5074  CA  PRO B 298     101.228  28.076   1.346  1.00 16.22           C  
-ATOM   5075  C   PRO B 298     101.006  28.894   0.064  1.00 15.33           C  
-ATOM   5076  O   PRO B 298     101.099  28.361  -1.042  1.00 14.48           O  
-ATOM   5077  CB  PRO B 298     102.683  28.116   1.805  1.00 16.61           C  
-ATOM   5078  CG  PRO B 298     103.323  27.064   0.945  1.00 17.01           C  
-ATOM   5079  CD  PRO B 298     102.317  25.935   1.030  1.00 17.65           C  
-ATOM   5080  N   PRO B 299     100.664  30.188   0.198  1.00 14.90           N  
-ATOM   5081  CA  PRO B 299     100.439  31.021  -0.994  1.00 14.75           C  
-ATOM   5082  C   PRO B 299     101.694  31.182  -1.858  1.00 15.51           C  
-ATOM   5083  O   PRO B 299     102.793  31.415  -1.355  1.00 16.98           O  
-ATOM   5084  CB  PRO B 299      99.924  32.338  -0.407  1.00 13.68           C  
-ATOM   5085  CG  PRO B 299     100.475  32.351   0.980  1.00 14.54           C  
-ATOM   5086  CD  PRO B 299     100.342  30.925   1.430  1.00 14.14           C  
-ATOM   5087  N   PHE B 300     101.503  31.061  -3.165  1.00 15.37           N  
-ATOM   5088  CA  PHE B 300     102.570  31.118  -4.155  1.00 13.73           C  
-ATOM   5089  C   PHE B 300     103.022  32.480  -4.699  1.00 14.44           C  
-ATOM   5090  O   PHE B 300     104.227  32.713  -4.860  1.00 14.24           O  
-ATOM   5091  CB  PHE B 300     102.166  30.203  -5.322  1.00 12.77           C  
-ATOM   5092  CG  PHE B 300     103.133  30.190  -6.476  1.00 13.31           C  
-ATOM   5093  CD1 PHE B 300     104.173  29.259  -6.521  1.00 13.13           C  
-ATOM   5094  CD2 PHE B 300     102.983  31.083  -7.541  1.00 12.63           C  
-ATOM   5095  CE1 PHE B 300     105.047  29.218  -7.605  1.00 11.03           C  
-ATOM   5096  CE2 PHE B 300     103.851  31.049  -8.628  1.00 11.32           C  
-ATOM   5097  CZ  PHE B 300     104.885  30.114  -8.660  1.00 11.07           C  
-ATOM   5098  N   HIS B 301     102.078  33.373  -4.983  1.00 13.06           N  
-ATOM   5099  CA  HIS B 301     102.409  34.658  -5.589  1.00 13.58           C  
-ATOM   5100  C   HIS B 301     103.553  35.502  -5.012  1.00 14.30           C  
-ATOM   5101  O   HIS B 301     104.438  35.927  -5.755  1.00 14.74           O  
-ATOM   5102  CB  HIS B 301     101.159  35.529  -5.764  1.00 12.99           C  
-ATOM   5103  CG  HIS B 301     101.347  36.641  -6.749  1.00 12.73           C  
-ATOM   5104  ND1 HIS B 301     101.424  36.424  -8.109  1.00 13.25           N  
-ATOM   5105  CD2 HIS B 301     101.543  37.968  -6.572  1.00 12.58           C  
-ATOM   5106  CE1 HIS B 301     101.665  37.566  -8.727  1.00 12.04           C  
-ATOM   5107  NE2 HIS B 301     101.741  38.518  -7.816  1.00 12.33           N  
-ATOM   5108  N   GLY B 302     103.513  35.781  -3.715  1.00 14.06           N  
-ATOM   5109  CA  GLY B 302     104.549  36.590  -3.096  1.00 14.43           C  
-ATOM   5110  C   GLY B 302     105.892  35.897  -3.016  1.00 14.82           C  
-ATOM   5111  O   GLY B 302     106.930  36.521  -3.230  1.00 15.67           O  
-ATOM   5112  N   ALA B 303     105.874  34.601  -2.718  1.00 15.01           N  
-ATOM   5113  CA  ALA B 303     107.096  33.802  -2.616  1.00 14.32           C  
-ATOM   5114  C   ALA B 303     107.825  33.772  -3.958  1.00 14.86           C  
-ATOM   5115  O   ALA B 303     109.057  33.826  -4.016  1.00 15.22           O  
-ATOM   5116  CB  ALA B 303     106.755  32.384  -2.171  1.00 12.44           C  
-ATOM   5117  N   LYS B 304     107.051  33.688  -5.034  1.00 15.28           N  
-ATOM   5118  CA  LYS B 304     107.595  33.656  -6.388  1.00 15.37           C  
-ATOM   5119  C   LYS B 304     108.211  35.008  -6.747  1.00 15.83           C  
-ATOM   5120  O   LYS B 304     109.250  35.065  -7.404  1.00 16.10           O  
-ATOM   5121  CB  LYS B 304     106.491  33.293  -7.383  1.00 15.14           C  
-ATOM   5122  CG  LYS B 304     106.959  33.106  -8.805  1.00 16.07           C  
-ATOM   5123  CD  LYS B 304     108.044  32.060  -8.885  1.00 16.51           C  
-ATOM   5124  CE  LYS B 304     108.469  31.826 -10.317  1.00 16.42           C  
-ATOM   5125  NZ  LYS B 304     109.562  30.821 -10.367  1.00 17.98           N  
-ATOM   5126  N   ILE B 305     107.564  36.093  -6.325  1.00 15.05           N  
-ATOM   5127  CA  ILE B 305     108.073  37.433  -6.602  1.00 14.76           C  
-ATOM   5128  C   ILE B 305     109.437  37.569  -5.937  1.00 14.69           C  
-ATOM   5129  O   ILE B 305     110.416  37.966  -6.578  1.00 14.46           O  
-ATOM   5130  CB  ILE B 305     107.125  38.540  -6.058  1.00 14.47           C  
-ATOM   5131  CG1 ILE B 305     105.848  38.608  -6.899  1.00 13.82           C  
-ATOM   5132  CG2 ILE B 305     107.829  39.890  -6.047  1.00 12.21           C  
-ATOM   5133  CD1 ILE B 305     104.821  39.592  -6.375  1.00 12.49           C  
-ATOM   5134  N   VAL B 306     109.493  37.187  -4.665  1.00 13.46           N  
-ATOM   5135  CA  VAL B 306     110.719  37.262  -3.885  1.00 13.63           C  
-ATOM   5136  C   VAL B 306     111.880  36.459  -4.476  1.00 14.51           C  
-ATOM   5137  O   VAL B 306     112.983  36.989  -4.623  1.00 14.91           O  
-ATOM   5138  CB  VAL B 306     110.475  36.846  -2.413  1.00 12.70           C  
-ATOM   5139  CG1 VAL B 306     111.797  36.741  -1.665  1.00 13.13           C  
-ATOM   5140  CG2 VAL B 306     109.567  37.856  -1.728  1.00 10.63           C  
-ATOM   5141  N   SER B 307     111.643  35.199  -4.834  1.00 16.09           N  
-ATOM   5142  CA  SER B 307     112.715  34.379  -5.396  1.00 16.86           C  
-ATOM   5143  C   SER B 307     113.138  34.886  -6.777  1.00 17.61           C  
-ATOM   5144  O   SER B 307     114.311  34.787  -7.145  1.00 19.00           O  
-ATOM   5145  CB  SER B 307     112.317  32.903  -5.450  1.00 16.24           C  
-ATOM   5146  OG  SER B 307     111.322  32.670  -6.425  1.00 18.50           O  
-ATOM   5147  N   THR B 308     112.192  35.439  -7.532  1.00 17.39           N  
-ATOM   5148  CA  THR B 308     112.494  35.983  -8.854  1.00 17.02           C  
-ATOM   5149  C   THR B 308     113.427  37.186  -8.704  1.00 17.64           C  
-ATOM   5150  O   THR B 308     114.387  37.337  -9.460  1.00 18.31           O  
-ATOM   5151  CB  THR B 308     111.214  36.435  -9.585  1.00 16.28           C  
-ATOM   5152  OG1 THR B 308     110.388  35.297  -9.850  1.00 15.83           O  
-ATOM   5153  CG2 THR B 308     111.557  37.127 -10.899  1.00 16.75           C  
-ATOM   5154  N   VAL B 309     113.131  38.049  -7.736  1.00 17.11           N  
-ATOM   5155  CA  VAL B 309     113.953  39.224  -7.503  1.00 16.84           C  
-ATOM   5156  C   VAL B 309     115.341  38.788  -7.053  1.00 16.92           C  
-ATOM   5157  O   VAL B 309     116.340  39.156  -7.658  1.00 16.76           O  
-ATOM   5158  CB  VAL B 309     113.331  40.156  -6.432  1.00 17.11           C  
-ATOM   5159  CG1 VAL B 309     114.281  41.316  -6.114  1.00 15.31           C  
-ATOM   5160  CG2 VAL B 309     111.986  40.694  -6.923  1.00 15.87           C  
-ATOM   5161  N   LEU B 310     115.375  37.936  -6.035  1.00 17.39           N  
-ATOM   5162  CA  LEU B 310     116.613  37.433  -5.462  1.00 17.28           C  
-ATOM   5163  C   LEU B 310     117.528  36.627  -6.379  1.00 18.01           C  
-ATOM   5164  O   LEU B 310     118.743  36.683  -6.220  1.00 19.09           O  
-ATOM   5165  CB  LEU B 310     116.306  36.633  -4.197  1.00 15.92           C  
-ATOM   5166  CG  LEU B 310     116.371  37.360  -2.850  1.00 15.28           C  
-ATOM   5167  CD1 LEU B 310     116.177  38.853  -3.017  1.00 15.75           C  
-ATOM   5168  CD2 LEU B 310     115.354  36.774  -1.892  1.00 13.04           C  
-ATOM   5169  N   THR B 311     116.968  35.889  -7.333  1.00 18.45           N  
-ATOM   5170  CA  THR B 311     117.796  35.082  -8.230  1.00 17.97           C  
-ATOM   5171  C   THR B 311     118.104  35.731  -9.578  1.00 18.08           C  
-ATOM   5172  O   THR B 311     118.815  35.157 -10.400  1.00 18.68           O  
-ATOM   5173  CB  THR B 311     117.179  33.687  -8.468  1.00 17.93           C  
-ATOM   5174  OG1 THR B 311     115.885  33.830  -9.066  1.00 19.30           O  
-ATOM   5175  CG2 THR B 311     117.052  32.934  -7.152  1.00 17.40           C  
-ATOM   5176  N   THR B 312     117.557  36.916  -9.816  1.00 18.46           N  
-ATOM   5177  CA  THR B 312     117.803  37.628 -11.061  1.00 18.20           C  
-ATOM   5178  C   THR B 312     118.678  38.838 -10.736  1.00 19.17           C  
-ATOM   5179  O   THR B 312     118.177  39.875 -10.298  1.00 19.29           O  
-ATOM   5180  CB  THR B 312     116.491  38.103 -11.697  1.00 17.56           C  
-ATOM   5181  OG1 THR B 312     115.590  36.995 -11.826  1.00 18.05           O  
-ATOM   5182  CG2 THR B 312     116.757  38.687 -13.070  1.00 17.73           C  
-ATOM   5183  N   PRO B 313     119.994  38.737 -10.999  1.00 19.92           N  
-ATOM   5184  CA  PRO B 313     120.991  39.786 -10.747  1.00 20.26           C  
-ATOM   5185  C   PRO B 313     120.526  41.228 -10.971  1.00 19.87           C  
-ATOM   5186  O   PRO B 313     120.697  42.083 -10.100  1.00 19.34           O  
-ATOM   5187  CB  PRO B 313     122.128  39.392 -11.690  1.00 20.52           C  
-ATOM   5188  CG  PRO B 313     122.100  37.904 -11.596  1.00 20.00           C  
-ATOM   5189  CD  PRO B 313     120.613  37.604 -11.714  1.00 19.95           C  
-ATOM   5190  N   GLU B 314     119.939  41.492 -12.131  1.00 20.45           N  
-ATOM   5191  CA  GLU B 314     119.450  42.828 -12.457  1.00 21.42           C  
-ATOM   5192  C   GLU B 314     118.367  43.291 -11.484  1.00 20.74           C  
-ATOM   5193  O   GLU B 314     118.365  44.445 -11.043  1.00 21.00           O  
-ATOM   5194  CB  GLU B 314     118.902  42.843 -13.885  1.00 23.91           C  
-ATOM   5195  CG  GLU B 314     118.258  44.151 -14.300  1.00 26.42           C  
-ATOM   5196  CD  GLU B 314     117.761  44.141 -15.735  1.00 28.69           C  
-ATOM   5197  OE1 GLU B 314     117.504  43.045 -16.283  1.00 29.29           O  
-ATOM   5198  OE2 GLU B 314     117.620  45.242 -16.310  1.00 30.31           O  
-ATOM   5199  N   LEU B 315     117.447  42.386 -11.161  1.00 19.55           N  
-ATOM   5200  CA  LEU B 315     116.353  42.683 -10.243  1.00 18.94           C  
-ATOM   5201  C   LEU B 315     116.835  42.856  -8.802  1.00 18.53           C  
-ATOM   5202  O   LEU B 315     116.421  43.797  -8.119  1.00 18.60           O  
-ATOM   5203  CB  LEU B 315     115.273  41.598 -10.337  1.00 18.20           C  
-ATOM   5204  CG  LEU B 315     114.047  41.864 -11.227  1.00 18.20           C  
-ATOM   5205  CD1 LEU B 315     114.381  42.760 -12.396  1.00 17.11           C  
-ATOM   5206  CD2 LEU B 315     113.447  40.550 -11.708  1.00 17.33           C  
-ATOM   5207  N   ARG B 316     117.724  41.973  -8.351  1.00 18.51           N  
-ATOM   5208  CA  ARG B 316     118.265  42.049  -6.993  1.00 19.08           C  
-ATOM   5209  C   ARG B 316     119.004  43.369  -6.801  1.00 18.92           C  
-ATOM   5210  O   ARG B 316     118.869  44.025  -5.765  1.00 18.80           O  
-ATOM   5211  CB  ARG B 316     119.225  40.886  -6.717  1.00 20.63           C  
-ATOM   5212  CG  ARG B 316     119.557  40.668  -5.231  1.00 23.01           C  
-ATOM   5213  CD  ARG B 316     120.772  39.758  -5.079  1.00 26.48           C  
-ATOM   5214  NE  ARG B 316     120.706  38.867  -3.916  1.00 30.86           N  
-ATOM   5215  CZ  ARG B 316     121.085  39.194  -2.682  1.00 31.87           C  
-ATOM   5216  NH1 ARG B 316     121.559  40.407  -2.419  1.00 34.36           N  
-ATOM   5217  NH2 ARG B 316     121.028  38.291  -1.713  1.00 32.03           N  
-ATOM   5218  N   ALA B 317     119.763  43.768  -7.817  1.00 18.63           N  
-ATOM   5219  CA  ALA B 317     120.520  45.012  -7.765  1.00 18.66           C  
-ATOM   5220  C   ALA B 317     119.608  46.222  -7.587  1.00 19.13           C  
-ATOM   5221  O   ALA B 317     119.818  47.029  -6.677  1.00 19.58           O  
-ATOM   5222  CB  ALA B 317     121.379  45.166  -9.012  1.00 17.42           C  
-ATOM   5223  N   ASP B 318     118.581  46.340  -8.425  1.00 19.92           N  
-ATOM   5224  CA  ASP B 318     117.662  47.473  -8.325  1.00 21.11           C  
-ATOM   5225  C   ASP B 318     116.890  47.467  -6.999  1.00 20.87           C  
-ATOM   5226  O   ASP B 318     116.621  48.531  -6.419  1.00 19.99           O  
-ATOM   5227  CB  ASP B 318     116.690  47.519  -9.509  1.00 22.57           C  
-ATOM   5228  CG  ASP B 318     115.778  48.741  -9.467  1.00 24.75           C  
-ATOM   5229  OD1 ASP B 318     116.298  49.872  -9.366  1.00 26.55           O  
-ATOM   5230  OD2 ASP B 318     114.544  48.575  -9.505  1.00 26.22           O  
-ATOM   5231  N   TRP B 319     116.537  46.271  -6.529  1.00 20.25           N  
-ATOM   5232  CA  TRP B 319     115.827  46.125  -5.263  1.00 19.75           C  
-ATOM   5233  C   TRP B 319     116.693  46.635  -4.118  1.00 19.65           C  
-ATOM   5234  O   TRP B 319     116.210  47.378  -3.259  1.00 19.45           O  
-ATOM   5235  CB  TRP B 319     115.450  44.661  -5.003  1.00 19.43           C  
-ATOM   5236  CG  TRP B 319     114.988  44.408  -3.590  1.00 18.88           C  
-ATOM   5237  CD1 TRP B 319     113.878  44.928  -2.979  1.00 18.90           C  
-ATOM   5238  CD2 TRP B 319     115.639  43.597  -2.605  1.00 19.01           C  
-ATOM   5239  NE1 TRP B 319     113.803  44.494  -1.677  1.00 18.46           N  
-ATOM   5240  CE2 TRP B 319     114.874  43.672  -1.419  1.00 18.61           C  
-ATOM   5241  CE3 TRP B 319     116.804  42.811  -2.608  1.00 18.44           C  
-ATOM   5242  CZ2 TRP B 319     115.225  42.995  -0.246  1.00 18.88           C  
-ATOM   5243  CZ3 TRP B 319     117.156  42.133  -1.436  1.00 19.12           C  
-ATOM   5244  CH2 TRP B 319     116.366  42.232  -0.273  1.00 18.74           C  
-ATOM   5245  N   MET B 320     117.964  46.232  -4.101  1.00 19.61           N  
-ATOM   5246  CA  MET B 320     118.876  46.670  -3.049  1.00 19.55           C  
-ATOM   5247  C   MET B 320     119.019  48.185  -3.082  1.00 18.30           C  
-ATOM   5248  O   MET B 320     119.007  48.832  -2.038  1.00 18.64           O  
-ATOM   5249  CB  MET B 320     120.246  45.994  -3.178  1.00 21.24           C  
-ATOM   5250  CG  MET B 320     120.221  44.489  -2.929  1.00 24.17           C  
-ATOM   5251  SD  MET B 320     121.838  43.655  -3.004  1.00 29.02           S  
-ATOM   5252  CE  MET B 320     122.160  43.671  -4.752  1.00 27.81           C  
-ATOM   5253  N   ALA B 321     119.068  48.754  -4.284  1.00 17.03           N  
-ATOM   5254  CA  ALA B 321     119.210  50.197  -4.441  1.00 16.09           C  
-ATOM   5255  C   ALA B 321     117.996  50.947  -3.919  1.00 16.75           C  
-ATOM   5256  O   ALA B 321     118.127  51.977  -3.249  1.00 16.88           O  
-ATOM   5257  CB  ALA B 321     119.454  50.546  -5.899  1.00 14.79           C  
-ATOM   5258  N   GLU B 322     116.807  50.437  -4.224  1.00 17.78           N  
-ATOM   5259  CA  GLU B 322     115.581  51.087  -3.777  1.00 17.52           C  
-ATOM   5260  C   GLU B 322     115.418  50.979  -2.268  1.00 17.73           C  
-ATOM   5261  O   GLU B 322     115.003  51.937  -1.614  1.00 18.06           O  
-ATOM   5262  CB  GLU B 322     114.362  50.508  -4.493  1.00 18.86           C  
-ATOM   5263  CG  GLU B 322     113.104  51.345  -4.286  1.00 20.10           C  
-ATOM   5264  CD  GLU B 322     111.906  50.875  -5.099  1.00 20.23           C  
-ATOM   5265  OE1 GLU B 322     112.078  50.140  -6.095  1.00 19.37           O  
-ATOM   5266  OE2 GLU B 322     110.777  51.265  -4.738  1.00 21.30           O  
-ATOM   5267  N   LEU B 323     115.749  49.815  -1.721  1.00 18.50           N  
-ATOM   5268  CA  LEU B 323     115.649  49.586  -0.282  1.00 20.31           C  
-ATOM   5269  C   LEU B 323     116.625  50.516   0.455  1.00 21.38           C  
-ATOM   5270  O   LEU B 323     116.292  51.074   1.501  1.00 21.51           O  
-ATOM   5271  CB  LEU B 323     115.931  48.111   0.046  1.00 19.88           C  
-ATOM   5272  CG  LEU B 323     115.751  47.634   1.491  1.00 19.64           C  
-ATOM   5273  CD1 LEU B 323     114.362  47.973   2.010  1.00 19.58           C  
-ATOM   5274  CD2 LEU B 323     115.991  46.140   1.561  1.00 18.66           C  
-ATOM   5275  N   GLU B 324     117.801  50.729  -0.132  1.00 22.52           N  
-ATOM   5276  CA  GLU B 324     118.814  51.610   0.447  1.00 23.68           C  
-ATOM   5277  C   GLU B 324     118.306  53.050   0.467  1.00 22.82           C  
-ATOM   5278  O   GLU B 324     118.519  53.781   1.437  1.00 21.76           O  
-ATOM   5279  CB  GLU B 324     120.118  51.515  -0.357  1.00 26.57           C  
-ATOM   5280  CG  GLU B 324     121.159  52.602  -0.063  1.00 30.45           C  
-ATOM   5281  CD  GLU B 324     121.684  52.587   1.370  1.00 33.33           C  
-ATOM   5282  OE1 GLU B 324     121.443  51.600   2.098  1.00 34.24           O  
-ATOM   5283  OE2 GLU B 324     122.348  53.572   1.768  1.00 35.32           O  
-ATOM   5284  N   ALA B 325     117.626  53.441  -0.606  1.00 22.85           N  
-ATOM   5285  CA  ALA B 325     117.059  54.780  -0.730  1.00 23.95           C  
-ATOM   5286  C   ALA B 325     116.026  55.025   0.371  1.00 24.52           C  
-ATOM   5287  O   ALA B 325     115.993  56.099   0.979  1.00 25.68           O  
-ATOM   5288  CB  ALA B 325     116.421  54.956  -2.100  1.00 24.26           C  
-ATOM   5289  N   VAL B 326     115.181  54.029   0.616  1.00 24.02           N  
-ATOM   5290  CA  VAL B 326     114.160  54.110   1.658  1.00 23.13           C  
-ATOM   5291  C   VAL B 326     114.852  54.294   3.006  1.00 23.55           C  
-ATOM   5292  O   VAL B 326     114.545  55.217   3.761  1.00 23.23           O  
-ATOM   5293  CB  VAL B 326     113.317  52.811   1.688  1.00 22.76           C  
-ATOM   5294  CG1 VAL B 326     112.458  52.754   2.932  1.00 21.43           C  
-ATOM   5295  CG2 VAL B 326     112.455  52.721   0.438  1.00 21.39           C  
-ATOM   5296  N   ARG B 327     115.806  53.412   3.274  1.00 25.10           N  
-ATOM   5297  CA  ARG B 327     116.597  53.403   4.501  1.00 26.92           C  
-ATOM   5298  C   ARG B 327     117.230  54.768   4.773  1.00 27.35           C  
-ATOM   5299  O   ARG B 327     117.013  55.360   5.828  1.00 27.61           O  
-ATOM   5300  CB  ARG B 327     117.688  52.346   4.349  1.00 27.91           C  
-ATOM   5301  CG  ARG B 327     118.575  52.064   5.550  1.00 29.59           C  
-ATOM   5302  CD  ARG B 327     119.643  51.074   5.109  1.00 31.38           C  
-ATOM   5303  NE  ARG B 327     119.025  50.052   4.264  1.00 35.25           N  
-ATOM   5304  CZ  ARG B 327     119.661  49.264   3.405  1.00 35.54           C  
-ATOM   5305  NH1 ARG B 327     120.973  49.363   3.233  1.00 36.24           N  
-ATOM   5306  NH2 ARG B 327     118.968  48.378   2.705  1.00 34.45           N  
-ATOM   5307  N   SER B 328     118.000  55.265   3.812  1.00 28.52           N  
-ATOM   5308  CA  SER B 328     118.662  56.561   3.941  1.00 29.82           C  
-ATOM   5309  C   SER B 328     117.659  57.690   4.172  1.00 29.78           C  
-ATOM   5310  O   SER B 328     117.877  58.570   5.015  1.00 29.59           O  
-ATOM   5311  CB  SER B 328     119.472  56.849   2.678  1.00 30.83           C  
-ATOM   5312  OG  SER B 328     120.350  55.775   2.393  1.00 34.02           O  
-ATOM   5313  N   GLY B 329     116.559  57.651   3.423  1.00 30.26           N  
-ATOM   5314  CA  GLY B 329     115.524  58.662   3.543  1.00 30.09           C  
-ATOM   5315  C   GLY B 329     114.967  58.751   4.950  1.00 30.09           C  
-ATOM   5316  O   GLY B 329     114.900  59.836   5.525  1.00 30.55           O  
-ATOM   5317  N   MET B 330     114.596  57.608   5.516  1.00 30.10           N  
-ATOM   5318  CA  MET B 330     114.045  57.570   6.863  1.00 30.55           C  
-ATOM   5319  C   MET B 330     115.048  58.106   7.877  1.00 31.01           C  
-ATOM   5320  O   MET B 330     114.687  58.844   8.794  1.00 29.81           O  
-ATOM   5321  CB  MET B 330     113.639  56.146   7.240  1.00 30.77           C  
-ATOM   5322  CG  MET B 330     112.494  55.576   6.421  1.00 32.05           C  
-ATOM   5323  SD  MET B 330     111.680  54.184   7.259  1.00 33.48           S  
-ATOM   5324  CE  MET B 330     113.127  53.219   7.845  1.00 33.90           C  
-ATOM   5325  N   LEU B 331     116.313  57.744   7.693  1.00 32.22           N  
-ATOM   5326  CA  LEU B 331     117.382  58.185   8.578  1.00 33.66           C  
-ATOM   5327  C   LEU B 331     117.482  59.711   8.542  1.00 34.61           C  
-ATOM   5328  O   LEU B 331     117.681  60.355   9.576  1.00 34.55           O  
-ATOM   5329  CB  LEU B 331     118.701  57.544   8.149  1.00 34.29           C  
-ATOM   5330  CG  LEU B 331     119.609  57.035   9.268  1.00 35.05           C  
-ATOM   5331  CD1 LEU B 331     120.638  56.089   8.686  1.00 35.87           C  
-ATOM   5332  CD2 LEU B 331     120.279  58.198   9.988  1.00 35.92           C  
-ATOM   5333  N   ARG B 332     117.313  60.279   7.350  1.00 35.95           N  
-ATOM   5334  CA  ARG B 332     117.353  61.724   7.163  1.00 37.26           C  
-ATOM   5335  C   ARG B 332     116.205  62.353   7.946  1.00 37.38           C  
-ATOM   5336  O   ARG B 332     116.391  63.360   8.635  1.00 37.82           O  
-ATOM   5337  CB  ARG B 332     117.209  62.085   5.682  1.00 39.17           C  
-ATOM   5338  CG  ARG B 332     117.260  63.585   5.406  1.00 42.80           C  
-ATOM   5339  CD  ARG B 332     116.674  63.952   4.042  1.00 45.14           C  
-ATOM   5340  NE  ARG B 332     117.355  63.284   2.933  1.00 47.88           N  
-ATOM   5341  CZ  ARG B 332     116.749  62.491   2.050  1.00 49.36           C  
-ATOM   5342  NH1 ARG B 332     115.445  62.251   2.146  1.00 50.20           N  
-ATOM   5343  NH2 ARG B 332     117.448  61.930   1.072  1.00 49.27           N  
-ATOM   5344  N   LEU B 333     115.024  61.744   7.845  1.00 36.62           N  
-ATOM   5345  CA  LEU B 333     113.841  62.232   8.540  1.00 36.27           C  
-ATOM   5346  C   LEU B 333     114.053  62.275  10.045  1.00 36.63           C  
-ATOM   5347  O   LEU B 333     113.708  63.265  10.685  1.00 37.25           O  
-ATOM   5348  CB  LEU B 333     112.620  61.371   8.211  1.00 35.22           C  
-ATOM   5349  CG  LEU B 333     112.034  61.479   6.801  1.00 34.73           C  
-ATOM   5350  CD1 LEU B 333     111.072  60.326   6.545  1.00 34.75           C  
-ATOM   5351  CD2 LEU B 333     111.332  62.816   6.632  1.00 34.47           C  
-ATOM   5352  N   ARG B 334     114.644  61.222  10.604  1.00 37.25           N  
-ATOM   5353  CA  ARG B 334     114.896  61.161  12.046  1.00 38.98           C  
-ATOM   5354  C   ARG B 334     115.746  62.348  12.492  1.00 40.94           C  
-ATOM   5355  O   ARG B 334     115.433  63.011  13.484  1.00 41.12           O  
-ATOM   5356  CB  ARG B 334     115.600  59.856  12.434  1.00 37.78           C  
-ATOM   5357  CG  ARG B 334     114.951  58.602  11.887  1.00 37.03           C  
-ATOM   5358  CD  ARG B 334     115.539  57.357  12.515  1.00 36.03           C  
-ATOM   5359  NE  ARG B 334     114.954  57.105  13.826  1.00 35.93           N  
-ATOM   5360  CZ  ARG B 334     114.048  56.167  14.076  1.00 35.11           C  
-ATOM   5361  NH1 ARG B 334     113.627  55.360  13.116  1.00 34.95           N  
-ATOM   5362  NH2 ARG B 334     113.572  56.024  15.301  1.00 36.85           N  
-ATOM   5363  N   GLU B 335     116.818  62.617  11.752  1.00 43.24           N  
-ATOM   5364  CA  GLU B 335     117.700  63.734  12.066  1.00 45.67           C  
-ATOM   5365  C   GLU B 335     116.960  65.064  11.963  1.00 46.71           C  
-ATOM   5366  O   GLU B 335     117.145  65.944  12.803  1.00 46.76           O  
-ATOM   5367  CB  GLU B 335     118.923  63.725  11.151  1.00 46.44           C  
-ATOM   5368  CG  GLU B 335     119.846  62.544  11.407  1.00 48.20           C  
-ATOM   5369  CD  GLU B 335     121.038  62.498  10.472  1.00 49.15           C  
-ATOM   5370  OE1 GLU B 335     121.427  63.556   9.930  1.00 50.83           O  
-ATOM   5371  OE2 GLU B 335     121.593  61.395  10.286  1.00 49.81           O  
-ATOM   5372  N   GLN B 336     116.113  65.201  10.945  1.00 48.25           N  
-ATOM   5373  CA  GLN B 336     115.333  66.422  10.763  1.00 50.64           C  
-ATOM   5374  C   GLN B 336     114.446  66.635  11.986  1.00 51.08           C  
-ATOM   5375  O   GLN B 336     114.443  67.716  12.579  1.00 51.67           O  
-ATOM   5376  CB  GLN B 336     114.445  66.335   9.519  1.00 52.19           C  
-ATOM   5377  CG  GLN B 336     115.188  66.244   8.198  1.00 55.74           C  
-ATOM   5378  CD  GLN B 336     114.248  66.325   7.002  1.00 57.89           C  
-ATOM   5379  OE1 GLN B 336     114.241  65.446   6.136  1.00 58.77           O  
-ATOM   5380  NE2 GLN B 336     113.445  67.383   6.954  1.00 58.34           N  
-ATOM   5381  N   LEU B 337     113.716  65.590  12.365  1.00 51.05           N  
-ATOM   5382  CA  LEU B 337     112.816  65.641  13.512  1.00 51.29           C  
-ATOM   5383  C   LEU B 337     113.561  65.995  14.791  1.00 51.67           C  
-ATOM   5384  O   LEU B 337     113.094  66.823  15.574  1.00 51.75           O  
-ATOM   5385  CB  LEU B 337     112.079  64.307  13.672  1.00 50.64           C  
-ATOM   5386  CG  LEU B 337     110.969  64.163  14.722  1.00 50.21           C  
-ATOM   5387  CD1 LEU B 337     111.546  63.804  16.072  1.00 50.11           C  
-ATOM   5388  CD2 LEU B 337     110.120  65.425  14.788  1.00 50.00           C  
-ATOM   5389  N   ALA B 338     114.715  65.370  15.001  1.00 51.96           N  
-ATOM   5390  CA  ALA B 338     115.519  65.636  16.187  1.00 52.88           C  
-ATOM   5391  C   ALA B 338     115.916  67.112  16.223  1.00 54.09           C  
-ATOM   5392  O   ALA B 338     115.731  67.788  17.239  1.00 54.34           O  
-ATOM   5393  CB  ALA B 338     116.753  64.754  16.196  1.00 51.98           C  
-ATOM   5394  N   GLY B 339     116.409  67.615  15.092  1.00 55.18           N  
-ATOM   5395  CA  GLY B 339     116.828  69.003  14.999  1.00 56.32           C  
-ATOM   5396  C   GLY B 339     115.701  69.980  15.268  1.00 57.11           C  
-ATOM   5397  O   GLY B 339     115.840  70.894  16.081  1.00 56.82           O  
-ATOM   5398  N   GLU B 340     114.577  69.773  14.592  1.00 58.42           N  
-ATOM   5399  CA  GLU B 340     113.405  70.623  14.749  1.00 60.34           C  
-ATOM   5400  C   GLU B 340     113.036  70.714  16.224  1.00 61.08           C  
-ATOM   5401  O   GLU B 340     112.884  71.808  16.768  1.00 61.31           O  
-ATOM   5402  CB  GLU B 340     112.227  70.031  13.973  1.00 61.54           C  
-ATOM   5403  CG  GLU B 340     111.089  71.005  13.706  1.00 63.77           C  
-ATOM   5404  CD  GLU B 340     111.408  71.999  12.599  1.00 65.33           C  
-ATOM   5405  OE1 GLU B 340     112.012  71.596  11.577  1.00 65.91           O  
-ATOM   5406  OE2 GLU B 340     111.041  73.185  12.742  1.00 66.41           O  
-ATOM   5407  N   LEU B 341     112.911  69.558  16.868  1.00 62.44           N  
-ATOM   5408  CA  LEU B 341     112.560  69.500  18.282  1.00 63.69           C  
-ATOM   5409  C   LEU B 341     113.588  70.211  19.145  1.00 64.61           C  
-ATOM   5410  O   LEU B 341     113.227  70.895  20.098  1.00 64.72           O  
-ATOM   5411  CB  LEU B 341     112.376  68.051  18.746  1.00 63.32           C  
-ATOM   5412  CG  LEU B 341     111.006  67.429  18.455  1.00 62.82           C  
-ATOM   5413  CD1 LEU B 341     110.975  65.978  18.900  1.00 62.59           C  
-ATOM   5414  CD2 LEU B 341     109.928  68.223  19.170  1.00 62.50           C  
-ATOM   5415  N   ARG B 342     114.861  70.074  18.792  1.00 65.83           N  
-ATOM   5416  CA  ARG B 342     115.934  70.721  19.537  1.00 67.58           C  
-ATOM   5417  C   ARG B 342     115.708  72.233  19.583  1.00 68.45           C  
-ATOM   5418  O   ARG B 342     115.756  72.849  20.651  1.00 68.56           O  
-ATOM   5419  CB  ARG B 342     117.283  70.416  18.883  1.00 68.21           C  
-ATOM   5420  CG  ARG B 342     118.479  71.079  19.546  1.00 69.13           C  
-ATOM   5421  CD  ARG B 342     119.755  70.794  18.768  1.00 69.97           C  
-ATOM   5422  NE  ARG B 342     120.919  71.417  19.390  1.00 70.76           N  
-ATOM   5423  CZ  ARG B 342     122.052  70.781  19.673  1.00 70.96           C  
-ATOM   5424  NH1 ARG B 342     122.187  69.489  19.394  1.00 70.81           N  
-ATOM   5425  NH2 ARG B 342     123.052  71.439  20.242  1.00 70.87           N  
-ATOM   5426  N   ASP B 343     115.426  72.821  18.425  1.00 69.29           N  
-ATOM   5427  CA  ASP B 343     115.196  74.255  18.322  1.00 70.12           C  
-ATOM   5428  C   ASP B 343     114.004  74.708  19.163  1.00 70.27           C  
-ATOM   5429  O   ASP B 343     114.088  75.703  19.883  1.00 70.58           O  
-ATOM   5430  CB  ASP B 343     114.970  74.662  16.861  1.00 71.42           C  
-ATOM   5431  CG  ASP B 343     116.149  74.303  15.959  1.00 72.99           C  
-ATOM   5432  OD1 ASP B 343     117.211  73.876  16.467  1.00 73.79           O  
-ATOM   5433  OD2 ASP B 343     116.004  74.453  14.723  1.00 73.83           O  
-ATOM   5434  N   LEU B 344     112.904  73.965  19.072  1.00 70.08           N  
-ATOM   5435  CA  LEU B 344     111.687  74.294  19.810  1.00 69.92           C  
-ATOM   5436  C   LEU B 344     111.769  74.064  21.314  1.00 70.07           C  
-ATOM   5437  O   LEU B 344     111.250  74.863  22.094  1.00 70.30           O  
-ATOM   5438  CB  LEU B 344     110.493  73.523  19.240  1.00 69.39           C  
-ATOM   5439  CG  LEU B 344     110.042  73.905  17.831  1.00 69.12           C  
-ATOM   5440  CD1 LEU B 344     108.923  72.986  17.387  1.00 69.08           C  
-ATOM   5441  CD2 LEU B 344     109.585  75.353  17.806  1.00 68.98           C  
-ATOM   5442  N   SER B 345     112.401  72.972  21.724  1.00 70.29           N  
-ATOM   5443  CA  SER B 345     112.520  72.654  23.141  1.00 70.70           C  
-ATOM   5444  C   SER B 345     113.665  73.412  23.797  1.00 70.76           C  
-ATOM   5445  O   SER B 345     113.650  73.647  25.009  1.00 70.99           O  
-ATOM   5446  CB  SER B 345     112.724  71.147  23.335  1.00 71.04           C  
-ATOM   5447  OG  SER B 345     113.952  70.715  22.769  1.00 71.15           O  
-ATOM   5448  N   GLY B 346     114.652  73.794  22.993  1.00 70.73           N  
-ATOM   5449  CA  GLY B 346     115.806  74.499  23.519  1.00 70.77           C  
-ATOM   5450  C   GLY B 346     116.625  73.541  24.363  1.00 70.48           C  
-ATOM   5451  O   GLY B 346     117.338  73.948  25.282  1.00 70.46           O  
-ATOM   5452  N   SER B 347     116.504  72.256  24.048  1.00 70.38           N  
-ATOM   5453  CA  SER B 347     117.213  71.202  24.758  1.00 70.04           C  
-ATOM   5454  C   SER B 347     117.442  70.037  23.803  1.00 69.70           C  
-ATOM   5455  O   SER B 347     117.082  70.106  22.627  1.00 69.58           O  
-ATOM   5456  CB  SER B 347     116.391  70.739  25.967  1.00 70.19           C  
-ATOM   5457  OG  SER B 347     115.154  70.160  25.576  1.00 69.42           O  
-ATOM   5458  N   ASP B 348     118.045  68.965  24.304  1.00 69.30           N  
-ATOM   5459  CA  ASP B 348     118.304  67.796  23.473  1.00 68.87           C  
-ATOM   5460  C   ASP B 348     117.749  66.504  24.064  1.00 67.68           C  
-ATOM   5461  O   ASP B 348     118.225  65.414  23.750  1.00 67.95           O  
-ATOM   5462  CB  ASP B 348     119.799  67.664  23.189  1.00 70.12           C  
-ATOM   5463  CG  ASP B 348     120.288  68.692  22.187  1.00 71.66           C  
-ATOM   5464  OD1 ASP B 348     120.055  68.490  20.975  1.00 71.90           O  
-ATOM   5465  OD2 ASP B 348     120.893  69.703  22.610  1.00 72.65           O  
-ATOM   5466  N   ARG B 349     116.719  66.633  24.894  1.00 65.98           N  
-ATOM   5467  CA  ARG B 349     116.084  65.478  25.521  1.00 63.98           C  
-ATOM   5468  C   ARG B 349     115.670  64.469  24.456  1.00 62.30           C  
-ATOM   5469  O   ARG B 349     115.874  63.267  24.609  1.00 62.35           O  
-ATOM   5470  CB  ARG B 349     114.838  65.909  26.303  1.00 64.74           C  
-ATOM   5471  CG  ARG B 349     115.107  66.771  27.527  1.00 64.98           C  
-ATOM   5472  CD  ARG B 349     113.809  67.120  28.250  1.00 64.86           C  
-ATOM   5473  NE  ARG B 349     112.964  68.036  27.482  1.00 64.83           N  
-ATOM   5474  CZ  ARG B 349     111.740  67.750  27.047  1.00 64.65           C  
-ATOM   5475  NH1 ARG B 349     111.200  66.561  27.284  1.00 64.61           N  
-ATOM   5476  NH2 ARG B 349     111.056  68.656  26.363  1.00 64.61           N  
-ATOM   5477  N   PHE B 350     115.137  64.982  23.352  1.00 59.93           N  
-ATOM   5478  CA  PHE B 350     114.668  64.149  22.253  1.00 57.81           C  
-ATOM   5479  C   PHE B 350     115.764  63.629  21.326  1.00 55.63           C  
-ATOM   5480  O   PHE B 350     115.476  63.149  20.228  1.00 55.56           O  
-ATOM   5481  CB  PHE B 350     113.602  64.901  21.453  1.00 58.81           C  
-ATOM   5482  CG  PHE B 350     112.442  65.364  22.287  1.00 60.26           C  
-ATOM   5483  CD1 PHE B 350     111.371  64.514  22.546  1.00 60.59           C  
-ATOM   5484  CD2 PHE B 350     112.433  66.641  22.840  1.00 60.91           C  
-ATOM   5485  CE1 PHE B 350     110.307  64.928  23.344  1.00 60.89           C  
-ATOM   5486  CE2 PHE B 350     111.374  67.065  23.640  1.00 61.41           C  
-ATOM   5487  CZ  PHE B 350     110.308  66.205  23.892  1.00 61.26           C  
-ATOM   5488  N   GLY B 351     117.008  63.672  21.789  1.00 52.90           N  
-ATOM   5489  CA  GLY B 351     118.115  63.199  20.978  1.00 50.31           C  
-ATOM   5490  C   GLY B 351     117.969  61.748  20.560  1.00 48.45           C  
-ATOM   5491  O   GLY B 351     118.314  61.384  19.433  1.00 47.94           O  
-ATOM   5492  N   PHE B 352     117.414  60.933  21.455  1.00 46.80           N  
-ATOM   5493  CA  PHE B 352     117.208  59.503  21.218  1.00 45.05           C  
-ATOM   5494  C   PHE B 352     116.606  59.172  19.854  1.00 43.86           C  
-ATOM   5495  O   PHE B 352     116.856  58.096  19.305  1.00 43.16           O  
-ATOM   5496  CB  PHE B 352     116.333  58.895  22.326  1.00 45.87           C  
-ATOM   5497  CG  PHE B 352     114.937  59.473  22.400  1.00 46.38           C  
-ATOM   5498  CD1 PHE B 352     113.904  58.942  21.632  1.00 46.71           C  
-ATOM   5499  CD2 PHE B 352     114.659  60.548  23.238  1.00 46.59           C  
-ATOM   5500  CE1 PHE B 352     112.614  59.474  21.696  1.00 47.24           C  
-ATOM   5501  CE2 PHE B 352     113.370  61.088  23.309  1.00 47.25           C  
-ATOM   5502  CZ  PHE B 352     112.348  60.550  22.536  1.00 47.44           C  
-ATOM   5503  N   VAL B 353     115.814  60.095  19.316  1.00 42.35           N  
-ATOM   5504  CA  VAL B 353     115.168  59.906  18.022  1.00 41.21           C  
-ATOM   5505  C   VAL B 353     116.183  59.654  16.905  1.00 40.67           C  
-ATOM   5506  O   VAL B 353     115.927  58.866  15.994  1.00 40.32           O  
-ATOM   5507  CB  VAL B 353     114.278  61.119  17.656  1.00 40.64           C  
-ATOM   5508  CG1 VAL B 353     113.560  60.874  16.336  1.00 40.75           C  
-ATOM   5509  CG2 VAL B 353     113.269  61.380  18.758  1.00 40.51           C  
-ATOM   5510  N   ALA B 354     117.340  60.302  16.994  1.00 39.41           N  
-ATOM   5511  CA  ALA B 354     118.380  60.142  15.987  1.00 38.61           C  
-ATOM   5512  C   ALA B 354     119.181  58.855  16.164  1.00 38.29           C  
-ATOM   5513  O   ALA B 354     119.806  58.379  15.220  1.00 38.09           O  
-ATOM   5514  CB  ALA B 354     119.304  61.339  16.003  1.00 38.76           C  
-ATOM   5515  N   GLU B 355     119.183  58.311  17.379  1.00 38.22           N  
-ATOM   5516  CA  GLU B 355     119.923  57.082  17.670  1.00 38.30           C  
-ATOM   5517  C   GLU B 355     119.108  55.815  17.426  1.00 37.19           C  
-ATOM   5518  O   GLU B 355     119.668  54.735  17.204  1.00 36.08           O  
-ATOM   5519  CB  GLU B 355     120.445  57.092  19.107  1.00 40.27           C  
-ATOM   5520  CG  GLU B 355     121.662  57.977  19.326  1.00 44.41           C  
-ATOM   5521  CD  GLU B 355     121.378  59.446  19.072  1.00 47.64           C  
-ATOM   5522  OE1 GLU B 355     120.537  60.019  19.798  1.00 49.45           O  
-ATOM   5523  OE2 GLU B 355     121.994  60.028  18.151  1.00 49.30           O  
-ATOM   5524  N   HIS B 356     117.787  55.934  17.522  1.00 35.70           N  
-ATOM   5525  CA  HIS B 356     116.912  54.795  17.292  1.00 34.37           C  
-ATOM   5526  C   HIS B 356     117.043  54.387  15.832  1.00 34.56           C  
-ATOM   5527  O   HIS B 356     117.332  55.214  14.969  1.00 34.82           O  
-ATOM   5528  CB  HIS B 356     115.456  55.144  17.625  1.00 31.93           C  
-ATOM   5529  CG  HIS B 356     115.150  55.113  19.090  1.00 30.15           C  
-ATOM   5530  ND1 HIS B 356     113.987  55.630  19.620  1.00 29.96           N  
-ATOM   5531  CD2 HIS B 356     115.854  54.628  20.141  1.00 29.56           C  
-ATOM   5532  CE1 HIS B 356     113.989  55.468  20.931  1.00 29.17           C  
-ATOM   5533  NE2 HIS B 356     115.110  54.863  21.271  1.00 28.94           N  
-ATOM   5534  N   ARG B 357     116.855  53.109  15.555  1.00 34.64           N  
-ATOM   5535  CA  ARG B 357     116.969  52.639  14.190  1.00 35.21           C  
-ATOM   5536  C   ARG B 357     115.755  51.790  13.830  1.00 34.45           C  
-ATOM   5537  O   ARG B 357     115.309  50.948  14.615  1.00 34.23           O  
-ATOM   5538  CB  ARG B 357     118.265  51.842  14.021  1.00 36.92           C  
-ATOM   5539  CG  ARG B 357     118.831  51.912  12.625  1.00 39.53           C  
-ATOM   5540  CD  ARG B 357     119.232  53.338  12.263  1.00 40.73           C  
-ATOM   5541  NE  ARG B 357     120.606  53.642  12.647  1.00 42.01           N  
-ATOM   5542  CZ  ARG B 357     120.985  54.745  13.284  1.00 43.38           C  
-ATOM   5543  NH1 ARG B 357     120.090  55.658  13.646  1.00 43.44           N  
-ATOM   5544  NH2 ARG B 357     122.265  54.925  13.582  1.00 44.29           N  
-ATOM   5545  N   GLY B 358     115.209  52.037  12.649  1.00 33.72           N  
-ATOM   5546  CA  GLY B 358     114.053  51.292  12.200  1.00 33.27           C  
-ATOM   5547  C   GLY B 358     112.918  52.177  11.728  1.00 33.14           C  
-ATOM   5548  O   GLY B 358     113.098  53.360  11.437  1.00 32.59           O  
-ATOM   5549  N   MET B 359     111.734  51.588  11.665  1.00 33.40           N  
-ATOM   5550  CA  MET B 359     110.540  52.287  11.220  1.00 34.14           C  
-ATOM   5551  C   MET B 359     109.895  53.084  12.352  1.00 33.91           C  
-ATOM   5552  O   MET B 359     109.357  54.175  12.138  1.00 32.92           O  
-ATOM   5553  CB  MET B 359     109.535  51.260  10.697  1.00 34.96           C  
-ATOM   5554  CG  MET B 359     108.338  51.842   9.991  1.00 36.63           C  
-ATOM   5555  SD  MET B 359     108.454  51.555   8.233  1.00 39.88           S  
-ATOM   5556  CE  MET B 359     107.480  50.117   8.095  1.00 39.57           C  
-ATOM   5557  N   PHE B 360     109.993  52.546  13.563  1.00 33.97           N  
-ATOM   5558  CA  PHE B 360     109.366  53.151  14.726  1.00 34.08           C  
-ATOM   5559  C   PHE B 360     110.289  53.789  15.742  1.00 35.58           C  
-ATOM   5560  O   PHE B 360     111.513  53.650  15.690  1.00 35.91           O  
-ATOM   5561  CB  PHE B 360     108.524  52.099  15.448  1.00 31.99           C  
-ATOM   5562  CG  PHE B 360     107.737  51.224  14.526  1.00 29.88           C  
-ATOM   5563  CD1 PHE B 360     106.584  51.694  13.919  1.00 28.39           C  
-ATOM   5564  CD2 PHE B 360     108.151  49.925  14.269  1.00 29.26           C  
-ATOM   5565  CE1 PHE B 360     105.858  50.886  13.070  1.00 27.90           C  
-ATOM   5566  CE2 PHE B 360     107.430  49.108  13.419  1.00 28.90           C  
-ATOM   5567  CZ  PHE B 360     106.280  49.587  12.820  1.00 28.41           C  
-ATOM   5568  N   SER B 361     109.656  54.462  16.694  1.00 37.48           N  
-ATOM   5569  CA  SER B 361     110.332  55.135  17.786  1.00 39.68           C  
-ATOM   5570  C   SER B 361     109.222  55.541  18.745  1.00 41.40           C  
-ATOM   5571  O   SER B 361     108.152  55.975  18.308  1.00 41.81           O  
-ATOM   5572  CB  SER B 361     111.061  56.384  17.270  1.00 39.38           C  
-ATOM   5573  OG  SER B 361     111.969  56.905  18.228  1.00 38.12           O  
-ATOM   5574  N   ARG B 362     109.427  55.305  20.034  1.00 43.62           N  
-ATOM   5575  CA  ARG B 362     108.440  55.701  21.031  1.00 46.28           C  
-ATOM   5576  C   ARG B 362     108.926  57.000  21.656  1.00 47.95           C  
-ATOM   5577  O   ARG B 362     110.096  57.111  22.032  1.00 48.54           O  
-ATOM   5578  CB  ARG B 362     108.283  54.633  22.110  1.00 46.28           C  
-ATOM   5579  CG  ARG B 362     107.684  53.343  21.608  1.00 47.21           C  
-ATOM   5580  CD  ARG B 362     106.633  52.822  22.565  1.00 47.72           C  
-ATOM   5581  NE  ARG B 362     107.151  52.644  23.917  1.00 48.51           N  
-ATOM   5582  CZ  ARG B 362     106.687  51.749  24.783  1.00 48.91           C  
-ATOM   5583  NH1 ARG B 362     105.708  50.924  24.434  1.00 48.79           N  
-ATOM   5584  NH2 ARG B 362     107.219  51.661  25.995  1.00 49.57           N  
-ATOM   5585  N   LEU B 363     108.053  57.998  21.719  1.00 49.58           N  
-ATOM   5586  CA  LEU B 363     108.428  59.279  22.301  1.00 51.01           C  
-ATOM   5587  C   LEU B 363     108.465  59.200  23.823  1.00 52.47           C  
-ATOM   5588  O   LEU B 363     109.538  59.172  24.429  1.00 52.34           O  
-ATOM   5589  CB  LEU B 363     107.465  60.379  21.850  1.00 50.45           C  
-ATOM   5590  CG  LEU B 363     107.432  60.676  20.353  1.00 50.11           C  
-ATOM   5591  CD1 LEU B 363     106.536  61.875  20.101  1.00 50.07           C  
-ATOM   5592  CD2 LEU B 363     108.840  60.948  19.840  1.00 50.24           C  
-ATOM   5593  N   GLY B 364     107.284  59.141  24.430  1.00 53.95           N  
-ATOM   5594  CA  GLY B 364     107.186  59.071  25.876  1.00 55.68           C  
-ATOM   5595  C   GLY B 364     105.854  59.606  26.360  1.00 57.01           C  
-ATOM   5596  O   GLY B 364     105.485  59.426  27.519  1.00 56.88           O  
-ATOM   5597  N   ALA B 365     105.135  60.270  25.460  1.00 58.54           N  
-ATOM   5598  CA  ALA B 365     103.832  60.842  25.772  1.00 60.85           C  
-ATOM   5599  C   ALA B 365     102.897  59.823  26.420  1.00 62.23           C  
-ATOM   5600  O   ALA B 365     102.784  58.683  25.962  1.00 62.34           O  
-ATOM   5601  CB  ALA B 365     103.196  61.415  24.509  1.00 60.81           C  
-ATOM   5602  N   THR B 366     102.241  60.245  27.496  1.00 63.95           N  
-ATOM   5603  CA  THR B 366     101.307  59.399  28.223  1.00 65.47           C  
-ATOM   5604  C   THR B 366     100.021  59.236  27.411  1.00 66.64           C  
-ATOM   5605  O   THR B 366      99.739  60.040  26.512  1.00 66.33           O  
-ATOM   5606  CB  THR B 366     100.978  60.012  29.602  1.00 65.83           C  
-ATOM   5607  OG1 THR B 366     100.327  61.280  29.430  1.00 66.01           O  
-ATOM   5608  CG2 THR B 366     102.249  60.195  30.418  1.00 65.93           C  
-ATOM   5609  N   PRO B 367      99.193  58.235  27.757  1.00 67.79           N  
-ATOM   5610  CA  PRO B 367      97.930  57.969  27.059  1.00 69.18           C  
-ATOM   5611  C   PRO B 367      97.029  59.186  26.848  1.00 70.53           C  
-ATOM   5612  O   PRO B 367      96.505  59.395  25.751  1.00 70.48           O  
-ATOM   5613  CB  PRO B 367      97.264  56.907  27.942  1.00 68.82           C  
-ATOM   5614  CG  PRO B 367      97.918  57.092  29.288  1.00 68.34           C  
-ATOM   5615  CD  PRO B 367      99.343  57.322  28.902  1.00 67.80           C  
-ATOM   5616  N   GLU B 368      96.863  59.995  27.889  1.00 72.29           N  
-ATOM   5617  CA  GLU B 368      96.018  61.181  27.795  1.00 74.02           C  
-ATOM   5618  C   GLU B 368      96.574  62.194  26.794  1.00 74.87           C  
-ATOM   5619  O   GLU B 368      95.822  62.765  25.998  1.00 74.72           O  
-ATOM   5620  CB  GLU B 368      95.813  61.815  29.178  1.00 74.63           C  
-ATOM   5621  CG  GLU B 368      97.092  62.211  29.918  1.00 75.43           C  
-ATOM   5622  CD  GLU B 368      97.331  63.717  29.954  1.00 75.90           C  
-ATOM   5623  OE1 GLU B 368      96.408  64.495  29.614  1.00 75.72           O  
-ATOM   5624  OE2 GLU B 368      98.451  64.124  30.336  1.00 76.16           O  
-ATOM   5625  N   GLN B 369      97.892  62.385  26.812  1.00 75.93           N  
-ATOM   5626  CA  GLN B 369      98.548  63.317  25.898  1.00 76.68           C  
-ATOM   5627  C   GLN B 369      98.360  62.832  24.468  1.00 77.38           C  
-ATOM   5628  O   GLN B 369      97.966  63.598  23.587  1.00 77.72           O  
-ATOM   5629  CB  GLN B 369     100.042  63.410  26.201  1.00 76.22           C  
-ATOM   5630  CG  GLN B 369     100.377  63.932  27.576  1.00 76.10           C  
-ATOM   5631  CD  GLN B 369     101.866  64.107  27.762  1.00 76.08           C  
-ATOM   5632  OE1 GLN B 369     102.580  63.161  28.093  1.00 76.07           O  
-ATOM   5633  NE2 GLN B 369     102.348  65.312  27.523  1.00 75.87           N  
-ATOM   5634  N   VAL B 370      98.640  61.549  24.252  1.00 77.75           N  
-ATOM   5635  CA  VAL B 370      98.502  60.923  22.943  1.00 78.31           C  
-ATOM   5636  C   VAL B 370      97.094  61.162  22.394  1.00 79.21           C  
-ATOM   5637  O   VAL B 370      96.930  61.615  21.258  1.00 79.12           O  
-ATOM   5638  CB  VAL B 370      98.761  59.395  23.030  1.00 77.93           C  
-ATOM   5639  CG1 VAL B 370      98.543  58.737  21.680  1.00 77.75           C  
-ATOM   5640  CG2 VAL B 370     100.172  59.127  23.523  1.00 77.37           C  
-ATOM   5641  N   LYS B 371      96.085  60.883  23.217  1.00 80.02           N  
-ATOM   5642  CA  LYS B 371      94.690  61.060  22.824  1.00 80.90           C  
-ATOM   5643  C   LYS B 371      94.365  62.501  22.433  1.00 81.38           C  
-ATOM   5644  O   LYS B 371      93.730  62.739  21.401  1.00 81.37           O  
-ATOM   5645  CB  LYS B 371      93.759  60.577  23.941  1.00 81.04           C  
-ATOM   5646  CG  LYS B 371      92.277  60.825  23.683  1.00 81.10           C  
-ATOM   5647  CD  LYS B 371      91.390  59.927  24.542  1.00 81.69           C  
-ATOM   5648  CE  LYS B 371      91.781  59.969  26.015  1.00 82.12           C  
-ATOM   5649  NZ  LYS B 371      90.887  59.127  26.856  1.00 82.17           N  
-ATOM   5650  N   ARG B 372      94.806  63.458  23.245  1.00 81.75           N  
-ATOM   5651  CA  ARG B 372      94.556  64.868  22.954  1.00 82.14           C  
-ATOM   5652  C   ARG B 372      95.113  65.225  21.581  1.00 82.08           C  
-ATOM   5653  O   ARG B 372      94.429  65.847  20.765  1.00 82.08           O  
-ATOM   5654  CB  ARG B 372      95.181  65.768  24.027  1.00 82.68           C  
-ATOM   5655  CG  ARG B 372      94.539  65.625  25.401  1.00 83.62           C  
-ATOM   5656  CD  ARG B 372      94.948  66.746  26.343  1.00 83.92           C  
-ATOM   5657  NE  ARG B 372      96.364  66.699  26.697  1.00 84.43           N  
-ATOM   5658  CZ  ARG B 372      96.980  67.619  27.434  1.00 84.81           C  
-ATOM   5659  NH1 ARG B 372      96.308  68.668  27.897  1.00 84.51           N  
-ATOM   5660  NH2 ARG B 372      98.266  67.484  27.727  1.00 85.24           N  
-ATOM   5661  N   ILE B 373      96.334  64.764  21.316  1.00 81.84           N  
-ATOM   5662  CA  ILE B 373      97.020  65.010  20.052  1.00 81.29           C  
-ATOM   5663  C   ILE B 373      96.175  64.620  18.834  1.00 81.41           C  
-ATOM   5664  O   ILE B 373      95.991  65.420  17.913  1.00 81.07           O  
-ATOM   5665  CB  ILE B 373      98.378  64.254  20.004  1.00 81.11           C  
-ATOM   5666  CG1 ILE B 373      99.316  64.774  21.095  1.00 80.95           C  
-ATOM   5667  CG2 ILE B 373      99.045  64.430  18.657  1.00 81.02           C  
-ATOM   5668  CD1 ILE B 373     100.687  64.119  21.092  1.00 80.37           C  
-ATOM   5669  N   LYS B 374      95.630  63.408  18.847  1.00 81.73           N  
-ATOM   5670  CA  LYS B 374      94.825  62.928  17.726  1.00 82.17           C  
-ATOM   5671  C   LYS B 374      93.453  63.584  17.595  1.00 81.89           C  
-ATOM   5672  O   LYS B 374      93.046  63.972  16.496  1.00 81.64           O  
-ATOM   5673  CB  LYS B 374      94.676  61.400  17.781  1.00 82.78           C  
-ATOM   5674  CG  LYS B 374      94.077  60.861  19.075  1.00 83.53           C  
-ATOM   5675  CD  LYS B 374      93.912  59.347  19.038  1.00 84.22           C  
-ATOM   5676  CE  LYS B 374      92.942  58.920  17.948  1.00 84.63           C  
-ATOM   5677  NZ  LYS B 374      91.591  59.520  18.134  1.00 85.20           N  
-ATOM   5678  N   GLU B 375      92.764  63.754  18.718  1.00 81.64           N  
-ATOM   5679  CA  GLU B 375      91.425  64.339  18.722  1.00 81.21           C  
-ATOM   5680  C   GLU B 375      91.322  65.799  18.282  1.00 81.09           C  
-ATOM   5681  O   GLU B 375      90.217  66.299  18.065  1.00 81.13           O  
-ATOM   5682  CB  GLU B 375      90.774  64.163  20.096  1.00 80.97           C  
-ATOM   5683  CG  GLU B 375      90.546  62.709  20.490  1.00 80.49           C  
-ATOM   5684  CD  GLU B 375      89.823  62.557  21.816  1.00 80.13           C  
-ATOM   5685  OE1 GLU B 375      89.993  63.425  22.700  1.00 79.93           O  
-ATOM   5686  OE2 GLU B 375      89.089  61.558  21.975  1.00 79.72           O  
-ATOM   5687  N   GLU B 376      92.455  66.476  18.134  1.00 80.85           N  
-ATOM   5688  CA  GLU B 376      92.441  67.877  17.725  1.00 80.57           C  
-ATOM   5689  C   GLU B 376      93.457  68.202  16.634  1.00 80.04           C  
-ATOM   5690  O   GLU B 376      93.165  68.980  15.725  1.00 80.03           O  
-ATOM   5691  CB  GLU B 376      92.662  68.781  18.941  1.00 81.30           C  
-ATOM   5692  CG  GLU B 376      93.991  68.565  19.639  1.00 82.59           C  
-ATOM   5693  CD  GLU B 376      94.055  69.220  21.000  1.00 83.56           C  
-ATOM   5694  OE1 GLU B 376      94.461  70.400  21.079  1.00 84.56           O  
-ATOM   5695  OE2 GLU B 376      93.705  68.550  21.996  1.00 83.93           O  
-ATOM   5696  N   PHE B 377      94.648  67.609  16.724  1.00 79.12           N  
-ATOM   5697  CA  PHE B 377      95.701  67.846  15.738  1.00 77.75           C  
-ATOM   5698  C   PHE B 377      95.579  66.906  14.543  1.00 76.72           C  
-ATOM   5699  O   PHE B 377      96.262  67.084  13.532  1.00 76.83           O  
-ATOM   5700  CB  PHE B 377      97.083  67.698  16.374  1.00 77.85           C  
-ATOM   5701  CG  PHE B 377      97.333  68.646  17.507  1.00 78.19           C  
-ATOM   5702  CD1 PHE B 377      97.272  70.021  17.309  1.00 78.69           C  
-ATOM   5703  CD2 PHE B 377      97.632  68.165  18.776  1.00 78.51           C  
-ATOM   5704  CE1 PHE B 377      97.507  70.903  18.360  1.00 79.30           C  
-ATOM   5705  CE2 PHE B 377      97.869  69.035  19.836  1.00 78.96           C  
-ATOM   5706  CZ  PHE B 377      97.807  70.408  19.628  1.00 79.40           C  
-ATOM   5707  N   GLY B 378      94.739  65.885  14.683  1.00 75.12           N  
-ATOM   5708  CA  GLY B 378      94.532  64.937  13.604  1.00 72.98           C  
-ATOM   5709  C   GLY B 378      95.701  64.010  13.337  1.00 71.23           C  
-ATOM   5710  O   GLY B 378      95.692  63.278  12.348  1.00 71.11           O  
-ATOM   5711  N   ILE B 379      96.702  64.032  14.211  1.00 69.38           N  
-ATOM   5712  CA  ILE B 379      97.875  63.175  14.054  1.00 67.47           C  
-ATOM   5713  C   ILE B 379      97.763  61.926  14.938  1.00 65.33           C  
-ATOM   5714  O   ILE B 379      97.809  62.000  16.167  1.00 64.32           O  
-ATOM   5715  CB  ILE B 379      99.199  63.965  14.290  1.00 68.00           C  
-ATOM   5716  CG1 ILE B 379     100.384  63.012  14.453  1.00 68.33           C  
-ATOM   5717  CG2 ILE B 379      99.061  64.924  15.453  1.00 67.77           C  
-ATOM   5718  CD1 ILE B 379     101.704  63.724  14.603  1.00 68.74           C  
-ATOM   5719  N   TYR B 380      97.596  60.781  14.286  1.00 63.19           N  
-ATOM   5720  CA  TYR B 380      97.428  59.508  14.972  1.00 61.07           C  
-ATOM   5721  C   TYR B 380      98.710  58.702  15.176  1.00 58.12           C  
-ATOM   5722  O   TYR B 380      99.406  58.364  14.213  1.00 57.91           O  
-ATOM   5723  CB  TYR B 380      96.417  58.643  14.209  1.00 63.14           C  
-ATOM   5724  CG  TYR B 380      95.152  59.366  13.800  1.00 65.53           C  
-ATOM   5725  CD1 TYR B 380      94.060  59.448  14.665  1.00 66.67           C  
-ATOM   5726  CD2 TYR B 380      95.041  59.959  12.542  1.00 66.45           C  
-ATOM   5727  CE1 TYR B 380      92.885  60.103  14.288  1.00 67.98           C  
-ATOM   5728  CE2 TYR B 380      93.873  60.616  12.153  1.00 67.76           C  
-ATOM   5729  CZ  TYR B 380      92.799  60.684  13.028  1.00 68.54           C  
-ATOM   5730  OH  TYR B 380      91.642  61.327  12.641  1.00 69.15           O  
-ATOM   5731  N   MET B 381      98.995  58.380  16.433  1.00 54.24           N  
-ATOM   5732  CA  MET B 381     100.152  57.573  16.802  1.00 50.21           C  
-ATOM   5733  C   MET B 381      99.621  56.528  17.776  1.00 47.53           C  
-ATOM   5734  O   MET B 381      98.643  56.779  18.474  1.00 47.37           O  
-ATOM   5735  CB  MET B 381     101.246  58.423  17.456  1.00 49.59           C  
-ATOM   5736  CG  MET B 381     100.863  59.075  18.770  1.00 49.08           C  
-ATOM   5737  SD  MET B 381     102.266  59.899  19.568  1.00 49.34           S  
-ATOM   5738  CE  MET B 381     102.361  61.399  18.606  1.00 48.54           C  
-ATOM   5739  N   VAL B 382     100.234  55.350  17.798  1.00 44.81           N  
-ATOM   5740  CA  VAL B 382      99.785  54.276  18.678  1.00 42.07           C  
-ATOM   5741  C   VAL B 382      99.748  54.748  20.133  1.00 41.40           C  
-ATOM   5742  O   VAL B 382     100.606  55.520  20.568  1.00 41.63           O  
-ATOM   5743  CB  VAL B 382     100.673  53.011  18.528  1.00 41.64           C  
-ATOM   5744  CG1 VAL B 382     100.140  51.877  19.386  1.00 41.06           C  
-ATOM   5745  CG2 VAL B 382     100.719  52.570  17.074  1.00 40.65           C  
-ATOM   5746  N   GLY B 383      98.749  54.269  20.873  1.00 40.25           N  
-ATOM   5747  CA  GLY B 383      98.554  54.642  22.268  1.00 38.36           C  
-ATOM   5748  C   GLY B 383      99.765  54.750  23.178  1.00 37.23           C  
-ATOM   5749  O   GLY B 383      99.760  55.542  24.120  1.00 37.28           O  
-ATOM   5750  N   ASP B 384     100.793  53.951  22.916  1.00 35.93           N  
-ATOM   5751  CA  ASP B 384     102.007  53.972  23.729  1.00 34.52           C  
-ATOM   5752  C   ASP B 384     103.024  54.995  23.215  1.00 34.10           C  
-ATOM   5753  O   ASP B 384     104.202  54.938  23.563  1.00 34.88           O  
-ATOM   5754  CB  ASP B 384     102.639  52.574  23.781  1.00 33.31           C  
-ATOM   5755  CG  ASP B 384     103.076  52.062  22.410  1.00 32.78           C  
-ATOM   5756  OD1 ASP B 384     102.697  52.647  21.372  1.00 31.30           O  
-ATOM   5757  OD2 ASP B 384     103.812  51.057  22.374  1.00 33.18           O  
-ATOM   5758  N   SER B 385     102.546  55.926  22.392  1.00 33.13           N  
-ATOM   5759  CA  SER B 385     103.358  56.981  21.782  1.00 31.90           C  
-ATOM   5760  C   SER B 385     104.320  56.473  20.707  1.00 30.89           C  
-ATOM   5761  O   SER B 385     105.359  57.094  20.452  1.00 31.49           O  
-ATOM   5762  CB  SER B 385     104.105  57.818  22.836  1.00 31.67           C  
-ATOM   5763  OG  SER B 385     105.304  57.201  23.284  1.00 31.41           O  
-ATOM   5764  N   ARG B 386     103.977  55.352  20.074  1.00 28.54           N  
-ATOM   5765  CA  ARG B 386     104.819  54.818  19.009  1.00 26.42           C  
-ATOM   5766  C   ARG B 386     104.465  55.571  17.733  1.00 26.14           C  
-ATOM   5767  O   ARG B 386     103.283  55.703  17.387  1.00 24.34           O  
-ATOM   5768  CB  ARG B 386     104.581  53.320  18.788  1.00 25.68           C  
-ATOM   5769  CG  ARG B 386     105.569  52.695  17.790  1.00 23.86           C  
-ATOM   5770  CD  ARG B 386     105.095  51.350  17.253  1.00 22.22           C  
-ATOM   5771  NE  ARG B 386     104.141  51.478  16.156  1.00 20.40           N  
-ATOM   5772  CZ  ARG B 386     103.555  50.454  15.540  1.00 19.49           C  
-ATOM   5773  NH1 ARG B 386     103.808  49.207  15.909  1.00 18.22           N  
-ATOM   5774  NH2 ARG B 386     102.759  50.674  14.506  1.00 20.36           N  
-ATOM   5775  N   ILE B 387     105.487  56.090  17.060  1.00 25.65           N  
-ATOM   5776  CA  ILE B 387     105.289  56.822  15.821  1.00 25.78           C  
-ATOM   5777  C   ILE B 387     106.055  56.166  14.683  1.00 25.87           C  
-ATOM   5778  O   ILE B 387     107.150  55.635  14.879  1.00 26.62           O  
-ATOM   5779  CB  ILE B 387     105.740  58.302  15.943  1.00 26.16           C  
-ATOM   5780  CG1 ILE B 387     107.230  58.389  16.281  1.00 26.55           C  
-ATOM   5781  CG2 ILE B 387     104.936  59.012  17.014  1.00 27.00           C  
-ATOM   5782  CD1 ILE B 387     107.779  59.800  16.239  1.00 26.85           C  
-ATOM   5783  N   ASN B 388     105.449  56.158  13.505  1.00 25.98           N  
-ATOM   5784  CA  ASN B 388     106.079  55.604  12.319  1.00 26.99           C  
-ATOM   5785  C   ASN B 388     106.766  56.811  11.688  1.00 28.05           C  
-ATOM   5786  O   ASN B 388     106.101  57.646  11.059  1.00 28.07           O  
-ATOM   5787  CB  ASN B 388     105.009  55.030  11.375  1.00 26.93           C  
-ATOM   5788  CG  ASN B 388     105.586  54.508  10.066  1.00 27.52           C  
-ATOM   5789  OD1 ASN B 388     106.750  54.740   9.741  1.00 29.87           O  
-ATOM   5790  ND2 ASN B 388     104.766  53.806   9.303  1.00 28.20           N  
-ATOM   5791  N   ILE B 389     108.083  56.923  11.859  1.00 29.06           N  
-ATOM   5792  CA  ILE B 389     108.804  58.074  11.309  1.00 30.31           C  
-ATOM   5793  C   ILE B 389     108.652  58.205   9.798  1.00 30.61           C  
-ATOM   5794  O   ILE B 389     108.741  59.305   9.260  1.00 30.46           O  
-ATOM   5795  CB  ILE B 389     110.314  58.114  11.726  1.00 31.19           C  
-ATOM   5796  CG1 ILE B 389     111.077  56.923  11.155  1.00 31.88           C  
-ATOM   5797  CG2 ILE B 389     110.457  58.199  13.247  1.00 30.58           C  
-ATOM   5798  CD1 ILE B 389     111.621  57.176   9.768  1.00 33.23           C  
-ATOM   5799  N   ALA B 390     108.389  57.090   9.122  1.00 31.76           N  
-ATOM   5800  CA  ALA B 390     108.204  57.096   7.673  1.00 33.37           C  
-ATOM   5801  C   ALA B 390     106.967  57.918   7.288  1.00 35.47           C  
-ATOM   5802  O   ALA B 390     106.779  58.267   6.118  1.00 34.75           O  
-ATOM   5803  CB  ALA B 390     108.076  55.676   7.158  1.00 33.46           C  
-ATOM   5804  N   GLY B 391     106.132  58.219   8.282  1.00 37.41           N  
-ATOM   5805  CA  GLY B 391     104.933  59.002   8.053  1.00 40.07           C  
-ATOM   5806  C   GLY B 391     105.179  60.502   8.063  1.00 41.97           C  
-ATOM   5807  O   GLY B 391     104.271  61.286   7.777  1.00 43.06           O  
-ATOM   5808  N   LEU B 392     106.397  60.915   8.400  1.00 42.96           N  
-ATOM   5809  CA  LEU B 392     106.729  62.334   8.438  1.00 43.94           C  
-ATOM   5810  C   LEU B 392     107.386  62.813   7.155  1.00 45.17           C  
-ATOM   5811  O   LEU B 392     107.728  62.016   6.280  1.00 45.30           O  
-ATOM   5812  CB  LEU B 392     107.654  62.647   9.616  1.00 43.67           C  
-ATOM   5813  CG  LEU B 392     107.084  62.700  11.035  1.00 44.00           C  
-ATOM   5814  CD1 LEU B 392     105.788  63.501  11.029  1.00 44.22           C  
-ATOM   5815  CD2 LEU B 392     106.846  61.307  11.573  1.00 44.59           C  
-ATOM   5816  N   ASN B 393     107.518  64.132   7.042  1.00 47.09           N  
-ATOM   5817  CA  ASN B 393     108.161  64.789   5.908  1.00 48.67           C  
-ATOM   5818  C   ASN B 393     108.460  66.224   6.304  1.00 49.80           C  
-ATOM   5819  O   ASN B 393     108.111  66.649   7.403  1.00 49.61           O  
-ATOM   5820  CB  ASN B 393     107.307  64.729   4.628  1.00 48.84           C  
-ATOM   5821  CG  ASN B 393     105.958  65.409   4.775  1.00 49.67           C  
-ATOM   5822  OD1 ASN B 393     105.807  66.381   5.514  1.00 49.74           O  
-ATOM   5823  ND2 ASN B 393     104.970  64.909   4.043  1.00 49.32           N  
-ATOM   5824  N   ASP B 394     109.090  66.968   5.404  1.00 52.25           N  
-ATOM   5825  CA  ASP B 394     109.467  68.359   5.658  1.00 54.49           C  
-ATOM   5826  C   ASP B 394     108.324  69.234   6.180  1.00 55.47           C  
-ATOM   5827  O   ASP B 394     108.526  70.061   7.068  1.00 55.62           O  
-ATOM   5828  CB  ASP B 394     110.052  68.985   4.386  1.00 55.23           C  
-ATOM   5829  CG  ASP B 394     111.073  68.086   3.705  1.00 56.12           C  
-ATOM   5830  OD1 ASP B 394     112.095  67.739   4.335  1.00 56.06           O  
-ATOM   5831  OD2 ASP B 394     110.842  67.720   2.531  1.00 57.23           O  
-ATOM   5832  N   ASN B 395     107.129  69.033   5.633  1.00 56.36           N  
-ATOM   5833  CA  ASN B 395     105.950  69.806   6.016  1.00 57.13           C  
-ATOM   5834  C   ASN B 395     105.429  69.421   7.400  1.00 57.18           C  
-ATOM   5835  O   ASN B 395     105.293  70.266   8.286  1.00 57.13           O  
-ATOM   5836  CB  ASN B 395     104.809  69.597   5.003  1.00 58.37           C  
-ATOM   5837  CG  ASN B 395     105.280  69.618   3.554  1.00 59.54           C  
-ATOM   5838  OD1 ASN B 395     106.229  68.923   3.185  1.00 60.73           O  
-ATOM   5839  ND2 ASN B 395     104.590  70.382   2.718  1.00 60.03           N  
-ATOM   5840  N   THR B 396     105.144  68.137   7.578  1.00 57.21           N  
-ATOM   5841  CA  THR B 396     104.592  67.624   8.824  1.00 57.25           C  
-ATOM   5842  C   THR B 396     105.519  67.548  10.037  1.00 57.53           C  
-ATOM   5843  O   THR B 396     105.038  67.550  11.173  1.00 57.43           O  
-ATOM   5844  CB  THR B 396     103.932  66.253   8.599  1.00 57.23           C  
-ATOM   5845  OG1 THR B 396     104.895  65.330   8.073  1.00 57.11           O  
-ATOM   5846  CG2 THR B 396     102.785  66.382   7.611  1.00 57.06           C  
-ATOM   5847  N   ILE B 397     106.832  67.494   9.815  1.00 57.92           N  
-ATOM   5848  CA  ILE B 397     107.781  67.409  10.929  1.00 58.31           C  
-ATOM   5849  C   ILE B 397     107.676  68.572  11.916  1.00 59.08           C  
-ATOM   5850  O   ILE B 397     107.467  68.345  13.110  1.00 58.87           O  
-ATOM   5851  CB  ILE B 397     109.244  67.221  10.450  1.00 57.84           C  
-ATOM   5852  CG1 ILE B 397     109.445  65.786   9.955  1.00 57.23           C  
-ATOM   5853  CG2 ILE B 397     110.223  67.519  11.584  1.00 57.56           C  
-ATOM   5854  CD1 ILE B 397     110.810  65.521   9.365  1.00 57.26           C  
-ATOM   5855  N   PRO B 398     107.818  69.828  11.443  1.00 60.05           N  
-ATOM   5856  CA  PRO B 398     107.714  70.953  12.379  1.00 60.63           C  
-ATOM   5857  C   PRO B 398     106.343  70.987  13.056  1.00 61.01           C  
-ATOM   5858  O   PRO B 398     106.238  71.316  14.237  1.00 60.77           O  
-ATOM   5859  CB  PRO B 398     107.956  72.173  11.482  1.00 60.38           C  
-ATOM   5860  CG  PRO B 398     107.527  71.710  10.130  1.00 60.29           C  
-ATOM   5861  CD  PRO B 398     108.081  70.314  10.077  1.00 60.29           C  
-ATOM   5862  N   ILE B 399     105.309  70.600  12.314  1.00 61.83           N  
-ATOM   5863  CA  ILE B 399     103.945  70.561  12.837  1.00 63.12           C  
-ATOM   5864  C   ILE B 399     103.895  69.586  14.016  1.00 64.17           C  
-ATOM   5865  O   ILE B 399     103.380  69.920  15.085  1.00 64.06           O  
-ATOM   5866  CB  ILE B 399     102.938  70.102  11.753  1.00 62.82           C  
-ATOM   5867  CG1 ILE B 399     103.046  71.000  10.518  1.00 62.16           C  
-ATOM   5868  CG2 ILE B 399     101.515  70.139  12.302  1.00 62.96           C  
-ATOM   5869  CD1 ILE B 399     102.182  70.557   9.365  1.00 61.58           C  
-ATOM   5870  N   LEU B 400     104.448  68.390  13.814  1.00 65.24           N  
-ATOM   5871  CA  LEU B 400     104.493  67.368  14.855  1.00 66.62           C  
-ATOM   5872  C   LEU B 400     105.280  67.908  16.041  1.00 67.79           C  
-ATOM   5873  O   LEU B 400     104.790  67.912  17.170  1.00 67.68           O  
-ATOM   5874  CB  LEU B 400     105.166  66.089  14.327  1.00 66.75           C  
-ATOM   5875  CG  LEU B 400     105.710  65.070  15.346  1.00 66.57           C  
-ATOM   5876  CD1 LEU B 400     104.595  64.513  16.208  1.00 66.73           C  
-ATOM   5877  CD2 LEU B 400     106.432  63.943  14.635  1.00 66.58           C  
-ATOM   5878  N   ALA B 401     106.494  68.377  15.763  1.00 69.42           N  
-ATOM   5879  CA  ALA B 401     107.386  68.927  16.779  1.00 71.15           C  
-ATOM   5880  C   ALA B 401     106.661  69.938  17.662  1.00 72.35           C  
-ATOM   5881  O   ALA B 401     106.702  69.849  18.892  1.00 72.47           O  
-ATOM   5882  CB  ALA B 401     108.596  69.574  16.115  1.00 70.94           C  
-ATOM   5883  N   ARG B 402     105.980  70.883  17.025  1.00 73.53           N  
-ATOM   5884  CA  ARG B 402     105.232  71.903  17.744  1.00 74.87           C  
-ATOM   5885  C   ARG B 402     104.091  71.275  18.533  1.00 75.16           C  
-ATOM   5886  O   ARG B 402     103.867  71.622  19.694  1.00 75.03           O  
-ATOM   5887  CB  ARG B 402     104.678  72.943  16.771  1.00 75.75           C  
-ATOM   5888  CG  ARG B 402     105.444  74.255  16.776  1.00 76.85           C  
-ATOM   5889  CD  ARG B 402     104.691  75.357  16.035  1.00 77.34           C  
-ATOM   5890  NE  ARG B 402     103.264  75.427  16.369  1.00 78.08           N  
-ATOM   5891  CZ  ARG B 402     102.755  75.438  17.602  1.00 78.16           C  
-ATOM   5892  NH1 ARG B 402     103.540  75.370  18.669  1.00 77.83           N  
-ATOM   5893  NH2 ARG B 402     101.441  75.508  17.767  1.00 78.59           N  
-ATOM   5894  N   ALA B 403     103.402  70.323  17.908  1.00 75.51           N  
-ATOM   5895  CA  ALA B 403     102.277  69.636  18.534  1.00 75.89           C  
-ATOM   5896  C   ALA B 403     102.659  68.947  19.836  1.00 76.06           C  
-ATOM   5897  O   ALA B 403     101.908  69.005  20.812  1.00 76.16           O  
-ATOM   5898  CB  ALA B 403     101.657  68.637  17.568  1.00 76.06           C  
-ATOM   5899  N   ILE B 404     103.825  68.307  19.870  1.00 76.35           N  
-ATOM   5900  CA  ILE B 404     104.248  67.631  21.091  1.00 77.10           C  
-ATOM   5901  C   ILE B 404     104.629  68.664  22.148  1.00 77.54           C  
-ATOM   5902  O   ILE B 404     104.490  68.416  23.345  1.00 77.75           O  
-ATOM   5903  CB  ILE B 404     105.413  66.614  20.867  1.00 77.13           C  
-ATOM   5904  CG1 ILE B 404     106.777  67.249  21.150  1.00 77.37           C  
-ATOM   5905  CG2 ILE B 404     105.371  66.058  19.454  1.00 77.29           C  
-ATOM   5906  CD1 ILE B 404     107.906  66.239  21.249  1.00 76.97           C  
-ATOM   5907  N   ILE B 405     105.100  69.824  21.700  1.00 78.26           N  
-ATOM   5908  CA  ILE B 405     105.482  70.898  22.613  1.00 79.12           C  
-ATOM   5909  C   ILE B 405     104.226  71.415  23.313  1.00 79.45           C  
-ATOM   5910  O   ILE B 405     104.196  71.555  24.537  1.00 79.16           O  
-ATOM   5911  CB  ILE B 405     106.177  72.063  21.858  1.00 79.41           C  
-ATOM   5912  CG1 ILE B 405     107.518  71.599  21.277  1.00 79.67           C  
-ATOM   5913  CG2 ILE B 405     106.388  73.257  22.784  1.00 79.70           C  
-ATOM   5914  CD1 ILE B 405     108.530  71.133  22.318  1.00 79.54           C  
-ATOM   5915  N   GLU B 406     103.180  71.648  22.526  1.00 79.91           N  
-ATOM   5916  CA  GLU B 406     101.912  72.143  23.045  1.00 80.52           C  
-ATOM   5917  C   GLU B 406     101.232  71.143  23.970  1.00 80.81           C  
-ATOM   5918  O   GLU B 406     100.530  71.533  24.906  1.00 81.03           O  
-ATOM   5919  CB  GLU B 406     100.975  72.516  21.893  1.00 80.95           C  
-ATOM   5920  CG  GLU B 406     101.569  73.539  20.937  1.00 81.84           C  
-ATOM   5921  CD  GLU B 406     102.258  74.679  21.665  1.00 82.12           C  
-ATOM   5922  OE1 GLU B 406     101.583  75.385  22.445  1.00 82.54           O  
-ATOM   5923  OE2 GLU B 406     103.479  74.862  21.467  1.00 82.00           O  
-ATOM   5924  N   VAL B 407     101.426  69.856  23.700  1.00 80.81           N  
-ATOM   5925  CA  VAL B 407     100.834  68.820  24.535  1.00 80.65           C  
-ATOM   5926  C   VAL B 407     101.636  68.709  25.834  1.00 80.65           C  
-ATOM   5927  O   VAL B 407     101.207  68.057  26.789  1.00 80.69           O  
-ATOM   5928  CB  VAL B 407     100.770  67.456  23.794  1.00 80.59           C  
-ATOM   5929  CG1 VAL B 407     102.079  66.693  23.929  1.00 80.65           C  
-ATOM   5930  CG2 VAL B 407      99.596  66.639  24.304  1.00 80.81           C  
-ATOM   5931  N   GLY B 408     102.804  69.349  25.847  1.00 80.70           N  
-ATOM   5932  CA  GLY B 408     103.668  69.362  27.017  1.00 81.59           C  
-ATOM   5933  C   GLY B 408     103.947  68.014  27.649  1.00 81.95           C  
-ATOM   5934  O   GLY B 408     104.190  67.031  26.945  1.00 82.20           O  
-ATOM   5935  N   VAL B 409     103.959  67.992  28.980  1.00 82.39           N  
-ATOM   5936  CA  VAL B 409     104.200  66.786  29.769  1.00 83.01           C  
-ATOM   5937  C   VAL B 409     104.185  67.155  31.256  1.00 83.31           C  
-ATOM   5938  O   VAL B 409     104.467  68.334  31.571  1.00 83.44           O  
-ATOM   5939  CB  VAL B 409     105.557  66.105  29.406  1.00 83.20           C  
-ATOM   5940  CG1 VAL B 409     106.740  66.949  29.879  1.00 83.44           C  
-ATOM   5941  CG2 VAL B 409     105.619  64.696  29.979  1.00 83.09           C  
-ATOM   5942  OXT VAL B 409     103.869  66.273  32.085  1.00 83.49           O  
-TER    5943      VAL B 409                                                      
-HETATM 5944  N1  PLP A 413      87.691  19.754   0.318  1.00 14.48           N  
-HETATM 5945  C2  PLP A 413      87.682  18.892  -0.735  1.00 14.24           C  
-HETATM 5946  C2A PLP A 413      86.740  17.695  -0.738  1.00 13.63           C  
-HETATM 5947  C3  PLP A 413      88.488  19.114  -1.795  1.00 14.15           C  
-HETATM 5948  O3  PLP A 413      88.464  18.202  -2.827  1.00 14.79           O  
-HETATM 5949  C4  PLP A 413      89.336  20.239  -1.803  1.00 14.43           C  
-HETATM 5950  C4A PLP A 413      90.146  20.485  -2.895  1.00 15.32           C  
-HETATM 5951  C5  PLP A 413      89.316  21.107  -0.696  1.00 14.40           C  
-HETATM 5952  C6  PLP A 413      88.493  20.842   0.345  1.00 13.78           C  
-HETATM 5953  C5A PLP A 413      90.190  22.352  -0.580  1.00 15.28           C  
-HETATM 5954  O4P PLP A 413      91.110  22.778  -1.562  1.00 15.96           O  
-HETATM 5955  P   PLP A 413      92.063  23.971  -1.253  1.00 14.31           P  
-HETATM 5956  O1P PLP A 413      91.481  25.207  -1.783  1.00 15.25           O  
-HETATM 5957  O2P PLP A 413      93.201  23.556  -2.257  1.00 14.56           O  
-HETATM 5958  O3P PLP A 413      92.509  23.949   0.150  1.00 11.77           O  
-HETATM 5959  N1  PLP B 413     106.623  41.039  13.660  1.00 14.63           N  
-HETATM 5960  C2  PLP B 413     106.838  42.375  13.652  1.00 15.25           C  
-HETATM 5961  C2A PLP B 413     107.472  43.043  14.848  1.00 15.62           C  
-HETATM 5962  C3  PLP B 413     106.534  43.110  12.566  1.00 15.52           C  
-HETATM 5963  O3  PLP B 413     106.761  44.466  12.622  1.00 15.61           O  
-HETATM 5964  C4  PLP B 413     106.004  42.479  11.428  1.00 16.10           C  
-HETATM 5965  C4A PLP B 413     105.747  43.188  10.247  1.00 15.42           C  
-HETATM 5966  C5  PLP B 413     105.794  41.084  11.474  1.00 16.37           C  
-HETATM 5967  C6  PLP B 413     106.109  40.398  12.588  1.00 15.33           C  
-HETATM 5968  C5A PLP B 413     105.252  40.308  10.295  1.00 17.43           C  
-HETATM 5969  O4P PLP B 413     104.158  40.858   9.627  1.00 18.93           O  
-HETATM 5970  P   PLP B 413     103.536  40.096   8.395  1.00 20.21           P  
-HETATM 5971  O1P PLP B 413     104.614  39.744   7.453  1.00 21.30           O  
-HETATM 5972  O2P PLP B 413     102.624  41.200   7.670  1.00 21.40           O  
-HETATM 5973  O3P PLP B 413     102.710  39.003   8.942  1.00 20.34           O  
-HETATM 5974  C1  HCI B 414     102.941  47.254  12.985  1.00 26.85           C  
-HETATM 5975  O1  HCI B 414     103.373  46.993  14.121  1.00 27.56           O  
-HETATM 5976  O2  HCI B 414     102.195  48.227  12.766  1.00 28.06           O  
-HETATM 5977  C2  HCI B 414     103.330  46.351  11.831  1.00 26.52           C  
-HETATM 5978  C3  HCI B 414     102.164  46.031  10.900  1.00 26.16           C  
-HETATM 5979  C1' HCI B 414     101.205  45.009  11.445  1.00 25.87           C  
-HETATM 5980  C2' HCI B 414     101.128  43.743  10.874  1.00 26.78           C  
-HETATM 5981  C3' HCI B 414     100.235  42.788  11.367  1.00 27.16           C  
-HETATM 5982  C4' HCI B 414      99.408  43.104  12.446  1.00 26.80           C  
-HETATM 5983  C5' HCI B 414      99.478  44.368  13.024  1.00 26.29           C  
-HETATM 5984  C6' HCI B 414     100.373  45.311  12.521  1.00 26.09           C  
-HETATM 5985  O   HOH A 414      83.276  25.286  -4.992  1.00 14.46           O  
-HETATM 5986  O   HOH A 415      83.652  16.958  -2.728  1.00 17.61           O  
-HETATM 5987  O   HOH A 416      78.825  14.022   2.269  1.00 19.89           O  
-HETATM 5988  O   HOH A 417      87.163  25.145  -6.614  1.00 14.98           O  
-HETATM 5989  O   HOH A 418      88.092  31.751 -18.900  1.00 20.80           O  
-HETATM 5990  O   HOH A 419      82.308  20.317  -3.172  1.00 26.81           O  
-HETATM 5991  O   HOH A 420      93.551  29.222 -13.880  1.00 22.10           O  
-HETATM 5992  O   HOH A 421      98.224  34.152 -16.034  1.00 27.94           O  
-HETATM 5993  O   HOH A 422      99.232  40.389 -11.247  1.00 47.22           O  
-HETATM 5994  O   HOH A 423      82.246  28.030  -4.611  1.00 38.50           O  
-HETATM 5995  O   HOH A 424      93.177  28.349  -4.501  1.00 10.17           O  
-HETATM 5996  O   HOH A 425      92.293  40.757   2.362  1.00 38.74           O  
-HETATM 5997  O   HOH A 426      79.023  36.876   1.476  1.00 44.23           O  
-HETATM 5998  O   HOH A 427      96.112  26.113 -13.478  1.00 16.66           O  
-HETATM 5999  O   HOH A 428      72.623  32.073  15.066  1.00 50.66           O  
-HETATM 6000  O   HOH A 429      70.735  29.920   7.079  1.00 33.39           O  
-HETATM 6001  O   HOH A 430      97.647  45.118  -4.659  1.00 25.14           O  
-HETATM 6002  O   HOH A 431      82.022  14.539   4.833  1.00 18.64           O  
-HETATM 6003  O   HOH A 432      92.329  10.020  -8.529  1.00 30.25           O  
-HETATM 6004  O   HOH A 433      85.216   8.295   6.754  1.00 24.84           O  
-HETATM 6005  O   HOH A 434     100.324  21.372 -15.722  1.00 39.03           O  
-HETATM 6006  O   HOH A 435      88.984  27.022  18.694  1.00 56.34           O  
-HETATM 6007  O   HOH A 436      95.414  40.614   2.271  1.00 19.55           O  
-HETATM 6008  O   HOH A 437      79.316   3.629   3.875  1.00 42.15           O  
-HETATM 6009  O   HOH A 438      83.815  13.522  -7.938  1.00 28.13           O  
-HETATM 6010  O   HOH A 439     100.418  46.597 -10.458  1.00 20.12           O  
-HETATM 6011  O   HOH A 440      84.945  16.271  -8.093  1.00 23.53           O  
-HETATM 6012  O   HOH A 441      75.261  22.000  -3.088  1.00 11.04           O  
-HETATM 6013  O   HOH A 442      86.473  23.783   0.264  1.00 18.05           O  
-HETATM 6014  O   HOH A 443      99.952  29.994  10.511  1.00 17.88           O  
-HETATM 6015  O   HOH A 444      96.855  42.510   3.836  1.00 23.81           O  
-HETATM 6016  O   HOH A 445      86.526  45.264  -2.537  1.00 33.01           O  
-HETATM 6017  O   HOH A 446      79.133  36.222  -7.955  1.00 36.00           O  
-HETATM 6018  O   HOH A 447      98.003   2.133  -8.412  1.00 33.41           O  
-HETATM 6019  O   HOH A 448      88.649  41.224  -3.938  1.00 36.73           O  
-HETATM 6020  O   HOH A 449      96.343  34.326  -3.150  1.00 25.60           O  
-HETATM 6021  O   HOH A 450      91.222  40.575  -2.707  1.00 44.50           O  
-HETATM 6022  O   HOH A 451      80.146  27.085 -16.117  1.00 32.51           O  
-HETATM 6023  O   HOH A 452      69.998  26.018  -7.961  1.00 23.61           O  
-HETATM 6024  O   HOH A 453     101.108  35.774 -12.401  1.00 24.46           O  
-HETATM 6025  O   HOH A 454      93.061  27.368 -20.848  1.00 34.29           O  
-HETATM 6026  O   HOH A 455      78.026  -1.569 -17.389  1.00 30.76           O  
-HETATM 6027  O   HOH A 456      70.020  22.192  12.798  1.00 29.25           O  
-HETATM 6028  O   HOH A 457      93.689  34.341  -2.075  1.00 47.50           O  
-HETATM 6029  O   HOH A 458      92.407  45.715 -10.264  1.00 50.54           O  
-HETATM 6030  O   HOH A 459      96.287  49.125  -5.685  1.00 35.77           O  
-HETATM 6031  O   HOH A 460      89.933  44.782   8.551  1.00 43.11           O  
-HETATM 6032  O   HOH A 461      91.431  23.514 -13.026  1.00 29.09           O  
-HETATM 6033  O   HOH A 462      89.706  46.654   2.805  1.00 41.52           O  
-HETATM 6034  O   HOH A 463      70.659   6.572  -2.653  1.00 34.36           O  
-HETATM 6035  O   HOH A 464      88.809  36.076 -21.020  1.00 54.70           O  
-HETATM 6036  O   HOH A 465      71.789   9.217  -4.545  1.00 14.00           O  
-HETATM 6037  O   HOH A 466      79.466  24.727 -14.870  1.00 26.19           O  
-HETATM 6038  O   HOH A 467      72.459  33.987   3.076  1.00 44.44           O  
-HETATM 6039  O   HOH A 468      72.841   2.846  -3.730  1.00 44.77           O  
-HETATM 6040  O   HOH A 469      92.017  14.908  -3.798  1.00 22.01           O  
-HETATM 6041  O   HOH A 470      91.522  34.050   0.164  1.00 29.81           O  
-HETATM 6042  O   HOH A 471      62.938  19.836   5.149  1.00 37.36           O  
-HETATM 6043  O   HOH A 472      87.293  18.329 -19.988  1.00 51.18           O  
-HETATM 6044  O   HOH A 473      92.664  29.912   6.445  1.00 11.46           O  
-HETATM 6045  O   HOH A 474      98.528  43.467  -6.660  1.00 40.72           O  
-HETATM 6046  O   HOH A 475      77.081  16.438  -7.562  1.00 30.55           O  
-HETATM 6047  O   HOH A 476      93.579  28.289  11.886  1.00 60.83           O  
-HETATM 6048  O   HOH A 477      84.670  28.803  -6.019  1.00 28.00           O  
-HETATM 6049  O   HOH A 478      97.879  24.614  14.233  1.00 38.16           O  
-HETATM 6050  O   HOH A 479      94.418  14.184 -19.287  1.00 38.06           O  
-HETATM 6051  O   HOH A 480      76.174  15.161  -2.899  1.00 31.87           O  
-HETATM 6052  O   HOH A 481      93.881  35.211 -21.394  1.00 39.94           O  
-HETATM 6053  O   HOH A 482      99.383  -9.466 -10.396  1.00 33.54           O  
-HETATM 6054  O   HOH A 483      75.475   9.237  -7.593  1.00 32.00           O  
-HETATM 6055  O   HOH A 484      90.532  18.140  -8.036  1.00 55.88           O  
-HETATM 6056  O   HOH A 485      71.746  24.953  12.749  1.00 32.19           O  
-HETATM 6057  O   HOH A 486      90.354  11.747  -1.530  1.00 50.91           O  
-HETATM 6058  O   HOH A 487      90.685   8.933  -1.931  1.00 45.86           O  
-HETATM 6059  O   HOH A 488     104.837  -5.867 -13.803  1.00 31.44           O  
-HETATM 6060  O   HOH A 489      99.192  33.457  -3.874  1.00 14.07           O  
-HETATM 6061  O   HOH A 490      75.183  18.415  -8.775  1.00 38.35           O  
-HETATM 6062  O   HOH A 491      96.704  -1.382  -4.441  1.00 61.92           O  
-HETATM 6063  O   HOH A 492      85.237  -5.707  -6.335  1.00 25.45           O  
-HETATM 6064  O   HOH A 493      66.873   4.916   7.578  1.00 40.14           O  
-HETATM 6065  O   HOH A 494      96.346   0.568 -10.007  1.00 18.61           O  
-HETATM 6066  O   HOH A 495      76.015   0.616 -18.520  1.00 59.83           O  
-HETATM 6067  O   HOH A 496      72.984  20.257  -5.524  1.00 20.49           O  
-HETATM 6068  O   HOH A 497      88.121  42.815   6.426  1.00 36.01           O  
-HETATM 6069  O   HOH A 498      74.466  16.799  -4.430  1.00 32.85           O  
-HETATM 6070  O   HOH A 499      90.551  -0.482  -2.606  1.00 27.24           O  
-HETATM 6071  O   HOH A 500      61.324  16.356  -0.999  1.00 62.46           O  
-HETATM 6072  O   HOH A 501      72.990  40.494  -0.941  1.00 51.55           O  
-HETATM 6073  O   HOH A 502     103.376  52.047  -7.095  1.00 26.66           O  
-HETATM 6074  O   HOH A 503      92.596  24.317 -15.373  1.00 47.28           O  
-HETATM 6075  O   HOH A 504      81.044  42.120  -5.481  1.00 53.63           O  
-HETATM 6076  O   HOH A 505      81.594  15.225 -14.551  1.00 40.44           O  
-HETATM 6077  O   HOH A 506      67.100  29.572   7.387  1.00 49.25           O  
-HETATM 6078  O   HOH A 507      66.048  10.653  -4.703  1.00 33.81           O  
-HETATM 6079  O   HOH A 508      76.004  11.944  -8.386  1.00 52.06           O  
-HETATM 6080  O   HOH A 509      96.614  14.493  12.372  1.00 41.25           O  
-HETATM 6081  O   HOH A 510      97.562  27.505 -19.719  1.00 49.28           O  
-HETATM 6082  O   HOH A 511      65.594  15.229  -6.598  1.00 24.14           O  
-HETATM 6083  O   HOH A 512      69.782   2.441   1.416  1.00 52.31           O  
-HETATM 6084  O   HOH A 513      90.311  15.709 -19.931  1.00 33.98           O  
-HETATM 6085  O   HOH A 514      75.251   6.761  14.274  1.00 57.55           O  
-HETATM 6086  O   HOH A 515      81.867  10.497  20.402  1.00 55.60           O  
-HETATM 6087  O   HOH A 516      97.198   4.715  -2.505  1.00 35.65           O  
-HETATM 6088  O   HOH A 517      95.366   9.271 -20.365  1.00 46.31           O  
-HETATM 6089  O   HOH A 518      87.315  42.683   9.495  1.00 51.37           O  
-HETATM 6090  O   HOH A 519     101.558  19.509 -25.391  1.00 56.68           O  
-HETATM 6091  O   HOH A 520      75.242  10.686 -18.446  1.00 65.22           O  
-HETATM 6092  O   HOH A 521      85.056  18.217  21.723  1.00 41.54           O  
-HETATM 6093  O   HOH A 522      89.880  39.239  -0.400  1.00 29.61           O  
-HETATM 6094  O   HOH A 523      98.188  40.809  -6.117  1.00 27.51           O  
-HETATM 6095  O   HOH A 524      75.422   0.686 -12.434  1.00 40.26           O  
-HETATM 6096  O   HOH A 525     101.394   9.033   4.548  1.00 50.75           O  
-HETATM 6097  O   HOH A 526      93.515  28.701  14.593  1.00 34.25           O  
-HETATM 6098  O   HOH A 527      88.459  -2.543 -25.194  1.00 32.52           O  
-HETATM 6099  O   HOH A 528      77.642  14.450  -0.516  1.00 33.05           O  
-HETATM 6100  O   HOH A 529     112.014   0.575 -22.084  1.00 38.04           O  
-HETATM 6101  O   HOH A 530      88.947   8.046   1.958  1.00 35.81           O  
-HETATM 6102  O   HOH A 531      88.457  14.085  21.922  1.00 49.22           O  
-HETATM 6103  O   HOH A 532      78.564   4.155  10.513  1.00 36.12           O  
-HETATM 6104  O   HOH A 533      72.278  14.176  -7.766  1.00 43.32           O  
-HETATM 6105  O   HOH A 534      90.959  25.029 -17.570  1.00 34.85           O  
-HETATM 6106  O   HOH A 535      77.046   5.132 -22.154  1.00 55.38           O  
-HETATM 6107  O   HOH A 536      68.194  15.814  -7.893  1.00 24.64           O  
-HETATM 6108  O   HOH A 537      96.127  31.121 -20.286  1.00 50.15           O  
-HETATM 6109  O   HOH A 538      93.666  22.994  17.588  1.00 48.28           O  
-HETATM 6110  O   HOH A 539      74.563  17.413 -16.397  1.00 38.69           O  
-HETATM 6111  O   HOH A 540      60.657  11.330   3.520  1.00 35.01           O  
-HETATM 6112  O   HOH A 541      74.882  14.696  -8.882  1.00 44.13           O  
-HETATM 6113  O   HOH A 542      91.958  38.288   0.764  1.00 28.39           O  
-HETATM 6114  O   HOH A 543      89.738  20.226  20.903  1.00 48.64           O  
-HETATM 6115  O   HOH A 544     101.903  12.466  10.451  1.00 37.34           O  
-HETATM 6116  O   HOH A 545      92.475  -9.671  -7.690  1.00 63.39           O  
-HETATM 6117  O   HOH A 546      88.433  44.174  -4.263  1.00 50.88           O  
-HETATM 6118  O   HOH A 547     106.572  -3.461 -14.304  1.00 59.10           O  
-HETATM 6119  O   HOH A 548      76.794   0.923   3.165  1.00 62.18           O  
-HETATM 6120  O   HOH A 549      69.404   6.254 -11.037  1.00 55.99           O  
-HETATM 6121  O   HOH A 550      98.038  13.735  15.109  1.00 47.88           O  
-HETATM 6122  O   HOH A 551      80.123   4.079   8.115  1.00 40.03           O  
-HETATM 6123  O   HOH A 552      63.553   7.693   1.498  1.00 62.29           O  
-HETATM 6124  O   HOH A 553      91.298  19.390 -23.673  1.00 56.93           O  
-HETATM 6125  O   HOH A 554      72.954  10.063 -15.829  1.00 53.37           O  
-HETATM 6126  O   HOH A 555      94.162  37.715 -22.608  1.00 42.75           O  
-HETATM 6127  O   HOH A 556      80.898  26.111 -23.077  1.00 43.72           O  
-HETATM 6128  O   HOH A 557     109.550   5.060 -22.328  1.00 64.89           O  
-HETATM 6129  O   HOH A 558      77.022   0.999 -25.340  1.00 39.90           O  
-HETATM 6130  O   HOH A 559      98.869  -0.823  -5.990  1.00 40.43           O  
-HETATM 6131  O   HOH A 560      91.046  14.088 -22.101  1.00 43.56           O  
-HETATM 6132  O   HOH A 561      72.910  14.269 -11.584  1.00 37.39           O  
-HETATM 6133  O   HOH A 562      91.572  43.651 -11.775  1.00 56.42           O  
-HETATM 6134  O   HOH A 563      96.040  12.143  15.884  1.00 61.11           O  
-HETATM 6135  O   HOH A 564      79.157  39.100   4.869  1.00 54.71           O  
-HETATM 6136  O   HOH A 565      68.707   4.592  13.992  1.00 48.35           O  
-HETATM 6137  O   HOH A 566      65.924  35.057  14.595  1.00 55.17           O  
-HETATM 6138  O   HOH A 567      87.155  42.810 -20.435  1.00 50.40           O  
-HETATM 6139  O   HOH A 568      97.622   9.001 -22.767  1.00 49.92           O  
-HETATM 6140  O   HOH A 569      82.038  15.541  23.665  1.00 50.89           O  
-HETATM 6141  O   HOH A 570      99.677  19.561 -13.661  1.00 45.68           O  
-HETATM 6142  O   HOH A 571      70.420  32.650  -8.125  1.00 59.19           O  
-HETATM 6143  O   HOH A 572     109.464  -2.727 -15.007  1.00 50.74           O  
-HETATM 6144  O   HOH A 573      85.637   3.591   2.575  1.00 47.84           O  
-HETATM 6145  O   HOH A 574      99.590  11.246  -8.636  1.00 52.52           O  
-HETATM 6146  O   HOH A 575      71.257   0.729   4.767  1.00 55.68           O  
-HETATM 6147  O   HOH A 576      70.132  38.454  -2.882  1.00 52.77           O  
-HETATM 6148  O   HOH A 577      71.189  -0.675   9.894  1.00 60.11           O  
-HETATM 6149  O   HOH A 578     101.507  -1.604  -4.185  1.00 55.10           O  
-HETATM 6150  O   HOH A 579      83.906   4.106   8.856  1.00 50.90           O  
-HETATM 6151  O   HOH A 580      82.145  42.414  13.655  1.00 65.84           O  
-HETATM 6152  O   HOH A 581      64.697  10.867  -1.655  1.00 52.33           O  
-HETATM 6153  O   HOH A 582      66.259  33.456  -9.066  1.00 45.76           O  
-HETATM 6154  O   HOH A 583      93.788 -13.690  -2.735  1.00 62.15           O  
-HETATM 6155  O   HOH A 584      71.193   1.435  -1.617  1.00 63.12           O  
-HETATM 6156  O   HOH A 585     101.670  -9.948  -8.283  1.00 64.85           O  
-HETATM 6157  O   HOH B 415      99.702  23.629 -18.867  1.00 54.24           O  
-HETATM 6158  O   HOH B 416      97.944  39.359  14.173  1.00 36.53           O  
-HETATM 6159  O   HOH B 417     113.000  41.005   7.513  1.00 17.73           O  
-HETATM 6160  O   HOH B 418     110.899  44.066  15.068  1.00 25.12           O  
-HETATM 6161  O   HOH B 419     114.174  41.662  21.666  1.00 22.34           O  
-HETATM 6162  O   HOH B 420     110.006  42.628   5.870  1.00 17.04           O  
-HETATM 6163  O   HOH B 421     113.255  47.745  -6.760  1.00 16.66           O  
-HETATM 6164  O   HOH B 422     113.243  42.870  12.632  1.00 30.11           O  
-HETATM 6165  O   HOH B 423     106.571  46.187  -3.786  1.00 17.30           O  
-HETATM 6166  O   HOH B 424     103.528  45.738  -9.290  1.00 48.94           O  
-HETATM 6167  O   HOH B 425     101.791  38.731 -11.797  1.00 23.24           O  
-HETATM 6168  O   HOH B 426     114.308  38.963   5.830  1.00 34.66           O  
-HETATM 6169  O   HOH B 427     103.882  39.686   2.747  1.00 13.98           O  
-HETATM 6170  O   HOH B 428     104.508  26.469  -2.627  1.00 23.23           O  
-HETATM 6171  O   HOH B 429     116.949  27.966   3.512  1.00 26.02           O  
-HETATM 6172  O   HOH B 430     103.319  48.078  -1.747  1.00 17.03           O  
-HETATM 6173  O   HOH B 431     118.891  20.056  16.805  1.00 23.59           O  
-HETATM 6174  O   HOH B 432     122.759  26.948  14.065  1.00 38.21           O  
-HETATM 6175  O   HOH B 433     102.046  29.732 -11.539  1.00 13.94           O  
-HETATM 6176  O   HOH B 434     110.005  40.216  22.036  1.00 30.88           O  
-HETATM 6177  O   HOH B 435     103.323  53.958  14.902  1.00 23.93           O  
-HETATM 6178  O   HOH B 436     105.508  43.207  26.330  1.00 32.30           O  
-HETATM 6179  O   HOH B 437      99.576  53.674  -1.198  1.00 35.32           O  
-HETATM 6180  O   HOH B 438     101.594  22.383  18.857  1.00 44.16           O  
-HETATM 6181  O   HOH B 439     101.782  26.971  -3.488  1.00 21.71           O  
-HETATM 6182  O   HOH B 440     112.353  47.292  30.145  1.00 26.61           O  
-HETATM 6183  O   HOH B 441     112.016  50.182  14.754  1.00 26.83           O  
-HETATM 6184  O   HOH B 442     100.555  33.108 -16.826  1.00 54.42           O  
-HETATM 6185  O   HOH B 443     110.871  48.735  12.457  1.00 21.85           O  
-HETATM 6186  O   HOH B 444     119.993  40.482  13.295  1.00 15.06           O  
-HETATM 6187  O   HOH B 445     108.491  38.266  11.071  1.00  9.14           O  
-HETATM 6188  O   HOH B 446      93.412  28.477   8.935  1.00 31.24           O  
-HETATM 6189  O   HOH B 447     100.087  24.773  -3.983  1.00 19.69           O  
-HETATM 6190  O   HOH B 448     105.150  32.640   1.403  1.00 33.80           O  
-HETATM 6191  O   HOH B 449     101.181  32.316 -11.271  1.00 28.51           O  
-HETATM 6192  O   HOH B 450     118.391  48.022  14.044  1.00 30.58           O  
-HETATM 6193  O   HOH B 451      99.224  26.387  12.522  1.00 28.23           O  
-HETATM 6194  O   HOH B 452     112.621  39.037   3.683  1.00 26.26           O  
-HETATM 6195  O   HOH B 453     109.367  47.850 -12.883  1.00 33.78           O  
-HETATM 6196  O   HOH B 454      98.653  36.768  -2.388  1.00 28.29           O  
-HETATM 6197  O   HOH B 455     120.549  47.003  12.652  1.00 41.26           O  
-HETATM 6198  O   HOH B 456     107.617  21.440  -0.368  1.00 35.27           O  
-HETATM 6199  O   HOH B 457     119.001  51.448  17.839  1.00 39.13           O  
-HETATM 6200  O   HOH B 458     107.785  29.260  -1.754  1.00 29.30           O  
-HETATM 6201  O   HOH B 459     101.433  33.800  -9.069  1.00 13.61           O  
-HETATM 6202  O   HOH B 460     109.265  51.748  -1.726  1.00 49.06           O  
-HETATM 6203  O   HOH B 461     104.854  29.288  -1.389  1.00 31.84           O  
-HETATM 6204  O   HOH B 462     113.891  48.354  32.271  1.00 39.06           O  
-HETATM 6205  O   HOH B 463     115.634  54.519  11.270  1.00 39.62           O  
-HETATM 6206  O   HOH B 464     105.577  15.659   6.572  1.00 26.25           O  
-HETATM 6207  O   HOH B 465     127.839  38.061  12.564  1.00 36.99           O  
-HETATM 6208  O   HOH B 466     102.117  18.738  -4.778  1.00 31.21           O  
-HETATM 6209  O   HOH B 467     123.193  41.783  -8.561  1.00 32.28           O  
-HETATM 6210  O   HOH B 468     122.675  48.076  -5.818  1.00 31.00           O  
-HETATM 6211  O   HOH B 469     106.988  66.537  26.579  1.00 42.89           O  
-HETATM 6212  O   HOH B 470     122.305  25.358  10.488  1.00 46.09           O  
-HETATM 6213  O   HOH B 471     117.872  40.302 -15.692  1.00 56.47           O  
-HETATM 6214  O   HOH B 472     109.467  42.669 -16.482  1.00 46.13           O  
-HETATM 6215  O   HOH B 473     121.899  46.881   1.854  1.00 60.95           O  
-HETATM 6216  O   HOH B 474     111.533  58.044   3.880  1.00 37.72           O  
-HETATM 6217  O   HOH B 475      90.777  64.644  14.952  1.00 46.43           O  
-HETATM 6218  O   HOH B 476      95.657  70.210  24.058  1.00 64.67           O  
-HETATM 6219  O   HOH B 477     119.479  35.528  -1.852  1.00 32.43           O  
-HETATM 6220  O   HOH B 478      97.607  60.425  18.881  1.00 53.52           O  
-HETATM 6221  O   HOH B 479     109.070  30.235  -4.977  1.00 39.02           O  
-HETATM 6222  O   HOH B 480     100.946  35.117  -2.544  1.00 43.75           O  
-HETATM 6223  O   HOH B 481     119.265  47.431   0.155  1.00 33.86           O  
-HETATM 6224  O   HOH B 482     108.356  52.093  -6.326  1.00 51.25           O  
-HETATM 6225  O   HOH B 483     120.792  27.296  23.771  1.00 32.77           O  
-HETATM 6226  O   HOH B 484     103.342  34.159  -0.569  1.00 52.73           O  
-HETATM 6227  O   HOH B 485     108.610  33.565 -13.372  1.00 44.25           O  
-HETATM 6228  O   HOH B 486     104.252  27.454 -14.366  1.00 43.16           O  
-HETATM 6229  O   HOH B 487     104.832  19.049  -1.311  1.00 45.04           O  
-HETATM 6230  O   HOH B 488     107.238  49.196   1.009  1.00 27.10           O  
-HETATM 6231  O   HOH B 489     122.213  49.185  22.962  1.00 35.02           O  
-HETATM 6232  O   HOH B 490     121.973  27.395   8.487  1.00 43.36           O  
-HETATM 6233  O   HOH B 491     101.707  30.565   8.065  1.00 32.44           O  
-HETATM 6234  O   HOH B 492     104.822  59.802   4.415  1.00 36.84           O  
-HETATM 6235  O   HOH B 493     118.208  44.852  18.236  1.00 36.29           O  
-HETATM 6236  O   HOH B 494     102.902  49.425  20.334  1.00 37.72           O  
-HETATM 6237  O   HOH B 495     120.821  65.749  20.186  1.00 56.14           O  
-HETATM 6238  O   HOH B 496     122.479  43.114  13.682  1.00 24.74           O  
-HETATM 6239  O   HOH B 497     120.416  44.703  16.028  1.00 60.78           O  
-HETATM 6240  O   HOH B 498     117.559  30.080  -4.621  1.00 28.39           O  
-HETATM 6241  O   HOH B 499     108.906  58.810   4.154  1.00 52.29           O  
-HETATM 6242  O   HOH B 500     107.015  19.535   1.647  1.00 32.98           O  
-HETATM 6243  O   HOH B 501     115.817  43.276  19.812  1.00 40.33           O  
-HETATM 6244  O   HOH B 502     103.879  47.112  22.813  1.00 44.30           O  
-HETATM 6245  O   HOH B 503     101.008  54.152  -4.002  1.00 36.36           O  
-HETATM 6246  O   HOH B 504      99.395  27.758  30.352  1.00 49.60           O  
-HETATM 6247  O   HOH B 505     111.169  41.649  33.659  1.00 55.08           O  
-HETATM 6248  O   HOH B 506     109.592  43.803  32.985  1.00 64.61           O  
-HETATM 6249  O   HOH B 507     108.696  62.064   3.521  1.00 53.08           O  
-HETATM 6250  O   HOH B 508     123.656  52.076  14.687  1.00 44.39           O  
-HETATM 6251  O   HOH B 509     126.724  37.244   2.856  1.00 40.66           O  
-HETATM 6252  O   HOH B 510     111.708  15.438   6.273  1.00 39.96           O  
-HETATM 6253  O   HOH B 511     123.159  42.162  34.581  1.00 24.45           O  
-HETATM 6254  O   HOH B 512     131.541  31.243   0.207  1.00 30.99           O  
-HETATM 6255  O   HOH B 513     101.008  56.040  26.326  1.00 42.43           O  
-HETATM 6256  O   HOH B 514      94.976  18.833   5.023  1.00 47.52           O  
-HETATM 6257  O   HOH B 515     118.409  26.036  21.666  1.00 47.37           O  
-HETATM 6258  O   HOH B 516     119.622  47.602 -11.687  1.00 52.12           O  
-HETATM 6259  O   HOH B 517      73.129  29.898  18.704  1.00 53.81           O  
-HETATM 6260  O   HOH B 518      97.840  14.621   6.891  1.00 46.16           O  
-HETATM 6261  O   HOH B 519      82.787  50.040  21.213  1.00 54.11           O  
-HETATM 6262  O   HOH B 520      94.903  20.361  -0.740  1.00 34.98           O  
-HETATM 6263  O   HOH B 521     125.735  32.231  10.791  1.00 33.66           O  
-HETATM 6264  O   HOH B 522     100.848  54.762   9.527  1.00 42.49           O  
-HETATM 6265  O   HOH B 523     117.551  53.524   9.332  1.00 31.93           O  
-HETATM 6266  O   HOH B 524     129.772  47.303   9.499  1.00 39.26           O  
-HETATM 6267  O   HOH B 525     108.629  14.888  12.171  1.00 31.40           O  
-HETATM 6268  O   HOH B 526      83.176  37.815  18.872  1.00 27.68           O  
-HETATM 6269  O   HOH B 527     114.256  72.952  31.167  1.00 60.13           O  
-HETATM 6270  O   HOH B 528     118.935  16.935   5.418  1.00 43.57           O  
-HETATM 6271  O   HOH B 529     124.606  16.482  10.472  1.00 51.99           O  
-HETATM 6272  O   HOH B 530     122.890  41.739  -0.258  1.00 51.54           O  
-HETATM 6273  O   HOH B 531     104.159  45.008  24.703  1.00 44.37           O  
-HETATM 6274  O   HOH B 532     110.058  48.353   1.056  1.00 36.24           O  
-HETATM 6275  O   HOH B 533     109.030  40.507 -19.427  1.00 44.20           O  
-HETATM 6276  O   HOH B 534      98.463  41.163  23.379  1.00 64.20           O  
-HETATM 6277  O   HOH B 535     110.393  37.304 -18.054  1.00 44.63           O  
-HETATM 6278  O   HOH B 536     108.010  26.223  35.027  1.00 39.93           O  
-HETATM 6279  O   HOH B 537     112.472  32.145  35.475  1.00 55.70           O  
-HETATM 6280  O   HOH B 538      94.749  68.167  30.208  1.00 53.83           O  
-HETATM 6281  O   HOH B 539     125.000  28.538  11.074  1.00 57.14           O  
-HETATM 6282  O   HOH B 540     110.911  34.054  34.394  1.00 55.82           O  
-HETATM 6283  O   HOH B 541     116.135  24.700   0.568  1.00 61.22           O  
-HETATM 6284  O   HOH B 542     119.271  25.081  32.486  1.00 44.76           O  
-HETATM 6285  O   HOH B 543     126.136  16.318  22.030  1.00 55.81           O  
-HETATM 6286  O   HOH B 544      96.494  24.556  17.655  1.00 61.07           O  
-HETATM 6287  O   HOH B 545      95.678  71.447   5.200  1.00 39.51           O  
-HETATM 6288  O   HOH B 546     112.724  54.108  -2.547  1.00 42.11           O  
-HETATM 6289  O   HOH B 547     115.652  18.670  -6.939  1.00 51.86           O  
-HETATM 6290  O   HOH B 548     107.483  29.530 -19.330  1.00 51.53           O  
-HETATM 6291  O   HOH B 549     130.592  35.792  20.394  1.00 46.72           O  
-HETATM 6292  O   HOH B 550     119.770  33.626  -3.791  1.00 63.50           O  
-HETATM 6293  O   HOH B 551     119.606  45.566 -18.691  1.00 61.06           O  
-HETATM 6294  O   HOH B 552     117.836  28.489  -7.077  1.00 58.44           O  
-HETATM 6295  O   HOH B 553     123.064  37.382   1.967  1.00 51.95           O  
-HETATM 6296  O   HOH B 554     122.459  24.420  13.026  1.00 42.01           O  
-HETATM 6297  O   HOH B 555     121.287  51.118  24.614  1.00 48.41           O  
-HETATM 6298  O   HOH B 556     123.783  68.784  21.901  1.00 55.28           O  
-HETATM 6299  O   HOH B 557     118.510  17.803   2.135  1.00 55.42           O  
-HETATM 6300  O   HOH B 558     120.229  54.291  32.797  1.00 57.49           O  
-HETATM 6301  O   HOH B 559     105.012  77.215  20.103  1.00 59.52           O  
-HETATM 6302  O   HOH B 560     129.307  47.843  12.403  1.00 50.70           O  
-HETATM 6303  O   HOH B 561     124.380  23.008  14.575  1.00 59.77           O  
-HETATM 6304  O   HOH B 562     131.218  30.383   2.788  1.00 63.06           O  
-HETATM 6305  O   HOH B 563     115.261  34.061 -11.724  1.00 55.99           O  
-HETATM 6306  O   HOH B 564     108.785  64.992  27.856  1.00 50.17           O  
-HETATM 6307  O   HOH B 565     116.736  47.771  35.451  1.00 63.21           O  
-HETATM 6308  O   HOH B 566     100.980  33.957  29.911  1.00 54.75           O  
-HETATM 6309  O   HOH B 567      73.683  30.582  24.422  1.00 60.00           O  
-HETATM 6310  O   HOH B 568     109.101  52.922 -12.114  1.00 59.09           O  
-HETATM 6311  O   HOH B 569     109.357  76.573  21.560  1.00 50.02           O  
-HETATM 6312  O   HOH B 570     123.828  44.552  15.928  1.00 53.77           O  
-CONECT 1823 5950                                                                
-CONECT 4769 5965                                                                
-CONECT 5944 5945 5952                                                           
-CONECT 5945 5944 5946 5947                                                      
-CONECT 5946 5945                                                                
-CONECT 5947 5945 5948 5949                                                      
-CONECT 5948 5947                                                                
-CONECT 5949 5947 5950 5951                                                      
-CONECT 5950 1823 5949                                                           
-CONECT 5951 5949 5952 5953                                                      
-CONECT 5952 5944 5951                                                           
-CONECT 5953 5951 5954                                                           
-CONECT 5954 5953 5955                                                           
-CONECT 5955 5954 5956 5957 5958                                                 
-CONECT 5956 5955                                                                
-CONECT 5957 5955                                                                
-CONECT 5958 5955                                                                
-CONECT 5959 5960 5967                                                           
-CONECT 5960 5959 5961 5962                                                      
-CONECT 5961 5960                                                                
-CONECT 5962 5960 5963 5964                                                      
-CONECT 5963 5962                                                                
-CONECT 5964 5962 5965 5966                                                      
-CONECT 5965 4769 5964                                                           
-CONECT 5966 5964 5967 5968                                                      
-CONECT 5967 5959 5966                                                           
-CONECT 5968 5966 5969                                                           
-CONECT 5969 5968 5970                                                           
-CONECT 5970 5969 5971 5972 5973                                                 
-CONECT 5971 5970                                                                
-CONECT 5972 5970                                                                
-CONECT 5973 5970                                                                
-CONECT 5974 5975 5976 5977                                                      
-CONECT 5975 5974                                                                
-CONECT 5976 5974                                                                
-CONECT 5977 5974 5978                                                           
-CONECT 5978 5977 5979                                                           
-CONECT 5979 5978 5980 5984                                                      
-CONECT 5980 5979 5981                                                           
-CONECT 5981 5980 5982                                                           
-CONECT 5982 5981 5983                                                           
-CONECT 5983 5982 5984                                                           
-CONECT 5984 5979 5983                                                           
-MASTER      296    0    3   28   26   47    9    9 6310    2   43   62          
-END                                                                             
diff --git a/plip/test/pdb/1bju.pdb b/plip/test/pdb/1bju.pdb
deleted file mode 100644
index ae36824..0000000
--- a/plip/test/pdb/1bju.pdb
+++ /dev/null
@@ -1,2217 +0,0 @@
-HEADER    SERINE PROTEASE                         29-JUN-98   1BJU              
-TITLE     BETA-TRYPSIN COMPLEXED WITH ACPU                                      
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: BETA-TRYPSIN;                                              
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 EC: 3.4.21.4;                                                        
-COMPND   5 OTHER_DETAILS: ACPU INHIBITED, ROOM TEMPERATURE 295 K                
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
-SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
-SOURCE   4 ORGANISM_TAXID: 9913;                                                
-SOURCE   5 ORGAN: PANCREAS                                                      
-KEYWDS    HYDROLASE, SERINE PROTEASE, DIGESTION, PANCREAS, ZYMOGEN              
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    S.PRESNELL,G.PATIL,C.MURA,K.JUDE,J.CONLEY,C.KAM,J.BERTRAND,           
-AUTHOR   2 J.POWERS,L.WILLIAMS                                                  
-REVDAT   3   24-FEB-09 1BJU    1       VERSN                                    
-REVDAT   2   13-JAN-99 1BJU    3       REMARK HEADER LINK   ATOM                
-REVDAT   2 2                   3       FORMUL JRNL   KEYWDS SHEET               
-REVDAT   2 3                   3       CONECT                                   
-REVDAT   1   02-DEC-98 1BJU    0                                                
-JRNL        AUTH   S.R.PRESNELL,G.S.PATIL,C.MURA,K.M.JUDE,J.M.CONLEY,           
-JRNL        AUTH 2 J.A.BERTRAND,C.M.KAM,J.C.POWERS,L.D.WILLIAMS                 
-JRNL        TITL   OXYANION-MEDIATED INHIBITION OF SERINE PROTEASES.            
-JRNL        REF    BIOCHEMISTRY                  V.  37 17068 1998              
-JRNL        REFN                   ISSN 0006-2960                               
-JRNL        PMID   9836602                                                      
-JRNL        DOI    10.1021/BI981636U                                            
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   W.BODE,P.SCHWAGER                                            
-REMARK   1  TITL   THE REFINED CRYSTAL STRUCTURE OF BOVINE                      
-REMARK   1  TITL 2 BETA-TRYPSIN AT 1.8 A RESOLUTION. II.                        
-REMARK   1  TITL 3 CRYSTALLOGRAPHIC REFINEMENT, CALCIUM BINDING SITE,           
-REMARK   1  TITL 4 BENZAMIDINE BINDING SITE AND ACTIVE SITE AT PH 7.0           
-REMARK   1  REF    J.MOL.BIOL.                   V.  98   693 1975              
-REMARK   1  REFN                   ISSN 0022-2836                               
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : X-PLOR 3.1                                           
-REMARK   3   AUTHORS     : BRUNGER                                              
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
-REMARK   3   NUMBER OF REFLECTIONS             : 28730                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
-REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
-REMARK   3   R VALUE            (WORKING SET) : 0.171                           
-REMARK   3   FREE R VALUE                     : NULL                            
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
-REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
-REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
-REMARK   3   BIN FREE R VALUE                    : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 1629                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 29                                      
-REMARK   3   SOLVENT ATOMS            : 97                                      
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
-REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.012                           
-REMARK   3   BOND ANGLES            (DEGREES) : 2.64                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
-REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PARAM19X.PRO                                   
-REMARK   3  PARAMETER FILE  2  : NULL                                           
-REMARK   3  PARAMETER FILE  3  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : TOPH19.PRO                                     
-REMARK   3  TOPOLOGY FILE  2   : NULL                                           
-REMARK   3  TOPOLOGY FILE  3   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1BJU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : AUG-93                             
-REMARK 200  TEMPERATURE           (KELVIN) : 293                                
-REMARK 200  PH                             : 6.0                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : N                                  
-REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
-REMARK 200  MONOCHROMATOR                  : NI FILTER                          
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
-REMARK 200  DETECTOR MANUFACTURER          : XUONG-HAMLIN MULTIWIRE             
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SDMS                               
-REMARK 200  DATA SCALING SOFTWARE          : SDMS                               
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28730                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 7.000                              
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
-REMARK 200  DATA REDUNDANCY                : 7.100                              
-REMARK 200  R MERGE                    (I) : 0.11000                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2000                             
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.72                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
-REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
-REMARK 200 STARTING MODEL: 3PTB                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9 M AMMONIUM SULFATE, 0.005 M          
-REMARK 280  MES, 0.001 M CACL2, 0.0025 M BENZAMIDINE, PH 6.0                    
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.42000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.91500            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.24500            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       33.91500            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.42000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.24500            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    TRP A  51   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
-REMARK 500    TRP A  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES          
-REMARK 500    TYR A  59   CB  -  CG  -  CD2 ANGL. DEV. =  -5.5 DEGREES          
-REMARK 500    TRP A 141   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
-REMARK 500    TRP A 141   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES          
-REMARK 500    TRP A 215   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES          
-REMARK 500    TRP A 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
-REMARK 500    TRP A 237   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES          
-REMARK 500    TRP A 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASP A  71      -78.32   -127.24                                   
-REMARK 500    ASN A 115     -163.79   -161.24                                   
-REMARK 500    SER A 214      -65.83   -123.59                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A 538        DISTANCE =  6.22 ANGSTROMS                       
-REMARK 525    HOH A 571        DISTANCE =  7.04 ANGSTROMS                       
-REMARK 525    HOH A 653        DISTANCE =  5.82 ANGSTROMS                       
-REMARK 620                                                                      
-REMARK 620 METAL COORDINATION                                                   
-REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
-REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              CA A 246  CA                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 GLU A  70   OE1                                                    
-REMARK 620 2 ASN A  72   O    86.5                                              
-REMARK 620 3 VAL A  75   O   157.1  83.0                                        
-REMARK 620 4 GLU A  80   OE2 104.1 160.3  92.2                                  
-REMARK 620 5 HOH A 552   O    87.3  88.1 112.5  76.0                            
-REMARK 620 6 HOH A 551   O    79.0 101.5  83.2  96.9 162.7                      
-REMARK 620 N                    1     2     3     4     5                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 246                  
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 901                 
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GP6 A 910                 
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 300                 
-REMARK 999                                                                      
-REMARK 999 SEQUENCE                                                             
-REMARK 999                                                                      
-REMARK 999 THE TRYPSIN RESIDUE NUMBERING USED IN THIS ENTRY IS BASED            
-REMARK 999 ON THE CHYMOTRYPSINOGEN NUMBERING SYSTEM.                            
-DBREF  1BJU A   16   245  UNP    P00760   TRY1_BOVIN      21    243             
-SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO          
-SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
-SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
-SEQRES   4 A  223  HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU          
-SEQRES   5 A  223  ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE          
-SEQRES   6 A  223  SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER          
-SEQRES   7 A  223  ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS          
-SEQRES   8 A  223  SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER          
-SEQRES   9 A  223  LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU          
-SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER          
-SEQRES  11 A  223  TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU          
-SEQRES  12 A  223  SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE          
-SEQRES  13 A  223  THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY          
-SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
-SEQRES  15 A  223  CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER          
-SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
-SEQRES  17 A  223  VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA          
-SEQRES  18 A  223  SER ASN                                                      
-HET     CA  A 246       1                                                       
-HET    SO4  A 901       5                                                       
-HET    GP6  A 910      20                                                       
-HET    DMS  A 300       4                                                       
-HETNAM      CA CALCIUM ION                                                      
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM     GP6 1-(4-AMIDINOPHENYL)-3-(4-CHLOROPHENYL)UREA                       
-HETNAM     DMS DIMETHYL SULFOXIDE                                               
-FORMUL   2   CA    CA 2+                                                        
-FORMUL   3  SO4    O4 S 2-                                                      
-FORMUL   4  GP6    C14 H13 CL N4 O                                              
-FORMUL   5  DMS    C2 H6 O S                                                    
-FORMUL   6  HOH   *97(H2 O)                                                     
-HELIX    1   1 ALA A   56  CYS A   58  5                                   3    
-HELIX    2   2 ASP A  165  ALA A  171  1                                   7    
-HELIX    3   3 VAL A  231  ASN A  233  5                                   3    
-HELIX    4   4 VAL A  235  ALA A  243  1                                   9    
-SHEET    1   A 7 GLN A  81  SER A  84  0                                        
-SHEET    2   A 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
-SHEET    3   A 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
-SHEET    4   A 7 HIS A  40  ASN A  48 -1  N  GLY A  44   O  VAL A  31           
-SHEET    5   A 7 TRP A  51  SER A  54 -1  N  VAL A  53   O  SER A  45           
-SHEET    6   A 7 MET A 104  LEU A 108 -1  N  ILE A 106   O  VAL A  52           
-SHEET    7   A 7 ALA A  85  VAL A  90 -1  N  ILE A  89   O  LEU A 105           
-SHEET    1   B 2 GLN A 135  GLY A 140  0                                        
-SHEET    2   B 2 LYS A 156  PRO A 161 -1  N  ALA A 160   O  CYS A 136           
-SHEET    1   C 1 MET A 180  ALA A 183  0                                        
-SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.01  
-SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.01  
-SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.02  
-SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.03  
-SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.02  
-SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.00  
-LINK        CA    CA A 246                 OE1 GLU A  70     1555   1555  2.26  
-LINK        CA    CA A 246                 O   ASN A  72     1555   1555  2.29  
-LINK        CA    CA A 246                 O   VAL A  75     1555   1555  2.24  
-LINK        CA    CA A 246                 OE2 GLU A  80     1555   1555  2.31  
-LINK        CA    CA A 246                 O   HOH A 552     1555   1555  2.18  
-LINK        CA    CA A 246                 O   HOH A 551     1555   1555  2.22  
-SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  80                    
-SITE     2 AC1  6 HOH A 551  HOH A 552                                          
-SITE     1 AC2  5 HIS A  57  GLN A 192  GLY A 193  SER A 195                    
-SITE     2 AC2  5 GP6 A 910                                                     
-SITE     1 AC3 12 HIS A  57  LEU A  99  ASP A 189  SER A 190                    
-SITE     2 AC3 12 GLN A 192  SER A 195  TRP A 215  GLY A 216                    
-SITE     3 AC3 12 GLY A 219  GLY A 226  HOH A 513  SO4 A 901                    
-SITE     1 AC4  7 ARG A  66  ILE A  73  VAL A  90  HIS A  91                    
-SITE     2 AC4  7 TYR A  94  HOH A 551  HOH A 630                               
-CRYST1   54.840   58.490   67.830  90.00  90.00  90.00 P 21 21 21    4          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.018235  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.017097  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.014743        0.00000                         
-ATOM      1  N   ILE A  16      -8.210   9.510  20.478  1.00  6.27           N  
-ATOM      2  CA  ILE A  16      -8.175   8.627  19.313  1.00  7.69           C  
-ATOM      3  C   ILE A  16      -9.430   8.900  18.477  1.00  7.28           C  
-ATOM      4  O   ILE A  16     -10.540   8.814  19.013  1.00  5.17           O  
-ATOM      5  CB  ILE A  16      -8.171   7.125  19.764  1.00  5.20           C  
-ATOM      6  CG1 ILE A  16      -6.908   6.787  20.549  1.00  6.11           C  
-ATOM      7  CG2 ILE A  16      -8.267   6.207  18.530  1.00  6.34           C  
-ATOM      8  CD1 ILE A  16      -5.591   6.774  19.748  1.00  7.68           C  
-ATOM      9  N   VAL A  17      -9.279   9.196  17.186  1.00  5.73           N  
-ATOM     10  CA  VAL A  17     -10.404   9.439  16.272  1.00  6.40           C  
-ATOM     11  C   VAL A  17     -10.586   8.183  15.430  1.00  7.50           C  
-ATOM     12  O   VAL A  17      -9.630   7.647  14.866  1.00  6.71           O  
-ATOM     13  CB  VAL A  17     -10.123  10.615  15.304  1.00  8.95           C  
-ATOM     14  CG1 VAL A  17     -11.366  10.905  14.475  1.00  7.98           C  
-ATOM     15  CG2 VAL A  17      -9.725  11.848  16.091  1.00  7.01           C  
-ATOM     16  N   GLY A  18     -11.811   7.683  15.370  1.00  7.40           N  
-ATOM     17  CA  GLY A  18     -12.132   6.544  14.528  1.00  9.11           C  
-ATOM     18  C   GLY A  18     -11.620   5.200  15.043  1.00 11.28           C  
-ATOM     19  O   GLY A  18     -11.434   4.268  14.240  1.00 12.17           O  
-ATOM     20  N   GLY A  19     -11.410   5.073  16.355  1.00  8.73           N  
-ATOM     21  CA  GLY A  19     -10.916   3.833  16.923  1.00 11.65           C  
-ATOM     22  C   GLY A  19     -12.034   3.070  17.616  1.00 11.93           C  
-ATOM     23  O   GLY A  19     -13.216   3.297  17.337  1.00 13.01           O  
-ATOM     24  N   TYR A  20     -11.725   2.149  18.518  1.00  7.58           N  
-ATOM     25  CA  TYR A  20     -12.742   1.342  19.158  1.00  8.99           C  
-ATOM     26  C   TYR A  20     -12.418   1.328  20.638  1.00  7.74           C  
-ATOM     27  O   TYR A  20     -11.332   1.742  21.043  1.00  7.95           O  
-ATOM     28  CB  TYR A  20     -12.746  -0.095  18.551  1.00  6.54           C  
-ATOM     29  CG  TYR A  20     -11.425  -0.833  18.653  1.00  6.16           C  
-ATOM     30  CD1 TYR A  20     -10.397  -0.549  17.755  1.00  8.61           C  
-ATOM     31  CD2 TYR A  20     -11.237  -1.792  19.645  1.00  8.71           C  
-ATOM     32  CE1 TYR A  20      -9.180  -1.216  17.851  1.00  8.15           C  
-ATOM     33  CE2 TYR A  20     -10.023  -2.465  19.746  1.00  9.22           C  
-ATOM     34  CZ  TYR A  20      -9.006  -2.168  18.848  1.00  7.57           C  
-ATOM     35  OH  TYR A  20      -7.789  -2.819  18.934  1.00 14.71           O  
-ATOM     36  N   THR A  21     -13.352   0.931  21.481  1.00  9.76           N  
-ATOM     37  CA  THR A  21     -13.135   0.859  22.904  1.00  9.12           C  
-ATOM     38  C   THR A  21     -12.255  -0.346  23.171  1.00  9.21           C  
-ATOM     39  O   THR A  21     -12.635  -1.468  22.819  1.00  9.44           O  
-ATOM     40  CB  THR A  21     -14.514   0.742  23.563  1.00 10.65           C  
-ATOM     41  OG1 THR A  21     -15.211   1.935  23.167  1.00 12.84           O  
-ATOM     42  CG2 THR A  21     -14.446   0.551  25.073  1.00 15.19           C  
-ATOM     43  N   CYS A  22     -11.108  -0.144  23.806  1.00  9.67           N  
-ATOM     44  CA  CYS A  22     -10.151  -1.216  24.000  1.00  9.22           C  
-ATOM     45  C   CYS A  22     -10.668  -2.387  24.810  1.00  9.25           C  
-ATOM     46  O   CYS A  22     -10.411  -3.541  24.486  1.00  8.98           O  
-ATOM     47  CB  CYS A  22      -8.928  -0.713  24.715  1.00 10.69           C  
-ATOM     48  SG  CYS A  22      -8.000   0.623  23.930  1.00  8.00           S  
-ATOM     49  N   GLY A  23     -11.394  -2.114  25.879  1.00 10.39           N  
-ATOM     50  CA  GLY A  23     -11.813  -3.126  26.802  1.00  9.12           C  
-ATOM     51  C   GLY A  23     -10.924  -2.930  28.021  1.00  9.25           C  
-ATOM     52  O   GLY A  23      -9.721  -2.682  27.904  1.00  7.55           O  
-ATOM     53  N   ALA A  24     -11.495  -3.035  29.212  1.00 10.66           N  
-ATOM     54  CA  ALA A  24     -10.735  -2.757  30.424  1.00 11.45           C  
-ATOM     55  C   ALA A  24      -9.521  -3.653  30.624  1.00 13.94           C  
-ATOM     56  O   ALA A  24      -9.549  -4.897  30.614  1.00 14.09           O  
-ATOM     57  CB  ALA A  24     -11.604  -2.910  31.651  1.00 13.35           C  
-ATOM     58  N   ASN A  25      -8.399  -2.968  30.806  1.00 14.39           N  
-ATOM     59  CA  ASN A  25      -7.107  -3.561  31.080  1.00 14.87           C  
-ATOM     60  C   ASN A  25      -6.578  -4.474  29.986  1.00 14.24           C  
-ATOM     61  O   ASN A  25      -5.733  -5.336  30.231  1.00 14.25           O  
-ATOM     62  CB  ASN A  25      -7.177  -4.306  32.408  1.00 17.40           C  
-ATOM     63  CG  ASN A  25      -7.667  -3.420  33.552  1.00 22.88           C  
-ATOM     64  OD1 ASN A  25      -7.192  -2.305  33.801  1.00 25.59           O  
-ATOM     65  ND2 ASN A  25      -8.693  -3.846  34.268  1.00 20.67           N  
-ATOM     66  N   THR A  26      -7.014  -4.281  28.747  1.00 11.78           N  
-ATOM     67  CA  THR A  26      -6.466  -5.067  27.657  1.00 10.14           C  
-ATOM     68  C   THR A  26      -5.164  -4.441  27.208  1.00  9.51           C  
-ATOM     69  O   THR A  26      -4.442  -5.020  26.397  1.00 10.92           O  
-ATOM     70  CB  THR A  26      -7.481  -5.106  26.516  1.00 11.56           C  
-ATOM     71  OG1 THR A  26      -7.812  -3.761  26.155  1.00  9.08           O  
-ATOM     72  CG2 THR A  26      -8.749  -5.828  26.946  1.00 13.47           C  
-ATOM     73  N   VAL A  27      -4.798  -3.225  27.656  1.00  7.87           N  
-ATOM     74  CA  VAL A  27      -3.568  -2.569  27.241  1.00  7.14           C  
-ATOM     75  C   VAL A  27      -2.834  -2.329  28.557  1.00  8.04           C  
-ATOM     76  O   VAL A  27      -2.781  -1.191  29.033  1.00  8.53           O  
-ATOM     77  CB  VAL A  27      -3.894  -1.221  26.521  1.00  8.70           C  
-ATOM     78  CG1 VAL A  27      -2.600  -0.667  25.978  1.00 10.11           C  
-ATOM     79  CG2 VAL A  27      -4.824  -1.386  25.316  1.00  8.34           C  
-ATOM     80  N   PRO A  28      -2.200  -3.299  29.211  1.00  8.15           N  
-ATOM     81  CA  PRO A  28      -1.786  -3.172  30.619  1.00  6.26           C  
-ATOM     82  C   PRO A  28      -0.597  -2.243  30.885  1.00  6.64           C  
-ATOM     83  O   PRO A  28      -0.268  -1.905  32.025  1.00  6.48           O  
-ATOM     84  CB  PRO A  28      -1.544  -4.618  31.025  1.00  8.20           C  
-ATOM     85  CG  PRO A  28      -1.077  -5.274  29.743  1.00  6.80           C  
-ATOM     86  CD  PRO A  28      -1.999  -4.660  28.703  1.00  7.07           C  
-ATOM     87  N   TYR A  29       0.100  -1.835  29.819  1.00  5.22           N  
-ATOM     88  CA  TYR A  29       1.252  -0.955  29.917  1.00  6.31           C  
-ATOM     89  C   TYR A  29       0.852   0.511  29.755  1.00  5.80           C  
-ATOM     90  O   TYR A  29       1.685   1.415  29.904  1.00  5.92           O  
-ATOM     91  CB  TYR A  29       2.303  -1.316  28.837  1.00  4.78           C  
-ATOM     92  CG  TYR A  29       1.722  -1.469  27.444  1.00  5.47           C  
-ATOM     93  CD1 TYR A  29       1.475  -0.358  26.640  1.00  4.88           C  
-ATOM     94  CD2 TYR A  29       1.386  -2.747  27.001  1.00  6.12           C  
-ATOM     95  CE1 TYR A  29       0.866  -0.514  25.391  1.00  6.74           C  
-ATOM     96  CE2 TYR A  29       0.783  -2.915  25.748  1.00  7.39           C  
-ATOM     97  CZ  TYR A  29       0.518  -1.799  24.957  1.00  7.63           C  
-ATOM     98  OH  TYR A  29      -0.097  -1.964  23.729  1.00  7.67           O  
-ATOM     99  N   GLN A  30      -0.417   0.794  29.441  1.00  5.31           N  
-ATOM    100  CA  GLN A  30      -0.851   2.165  29.172  1.00  6.35           C  
-ATOM    101  C   GLN A  30      -0.938   2.915  30.481  1.00  7.29           C  
-ATOM    102  O   GLN A  30      -1.493   2.385  31.458  1.00  7.33           O  
-ATOM    103  CB  GLN A  30      -2.212   2.122  28.469  1.00  5.18           C  
-ATOM    104  CG  GLN A  30      -2.909   3.468  28.362  1.00  8.19           C  
-ATOM    105  CD  GLN A  30      -2.431   4.383  27.247  1.00 11.12           C  
-ATOM    106  OE1 GLN A  30      -2.210   5.579  27.426  1.00 13.85           O  
-ATOM    107  NE2 GLN A  30      -2.293   3.907  26.032  1.00  8.80           N  
-ATOM    108  N   VAL A  31      -0.402   4.135  30.505  1.00  3.98           N  
-ATOM    109  CA  VAL A  31      -0.398   4.940  31.707  1.00  7.57           C  
-ATOM    110  C   VAL A  31      -1.133   6.254  31.427  1.00  5.83           C  
-ATOM    111  O   VAL A  31      -1.125   6.716  30.283  1.00  3.97           O  
-ATOM    112  CB  VAL A  31       1.123   5.082  32.049  1.00 10.43           C  
-ATOM    113  CG1 VAL A  31       1.538   6.451  32.514  1.00  9.49           C  
-ATOM    114  CG2 VAL A  31       1.403   4.028  33.105  1.00 12.42           C  
-ATOM    115  N   SER A  32      -1.747   6.876  32.435  1.00  3.33           N  
-ATOM    116  CA  SER A  32      -2.295   8.217  32.297  1.00  4.00           C  
-ATOM    117  C   SER A  32      -1.411   9.070  33.218  1.00  7.30           C  
-ATOM    118  O   SER A  32      -1.049   8.637  34.333  1.00  6.61           O  
-ATOM    119  CB  SER A  32      -3.732   8.245  32.788  1.00  4.39           C  
-ATOM    120  OG  SER A  32      -4.250   9.572  32.968  1.00  7.28           O  
-ATOM    121  N   LEU A  33      -1.013  10.253  32.753  1.00  6.62           N  
-ATOM    122  CA  LEU A  33      -0.229  11.176  33.551  1.00  5.84           C  
-ATOM    123  C   LEU A  33      -1.268  12.194  34.029  1.00  7.97           C  
-ATOM    124  O   LEU A  33      -2.024  12.774  33.223  1.00  6.70           O  
-ATOM    125  CB  LEU A  33       0.850  11.845  32.686  1.00  3.98           C  
-ATOM    126  CG  LEU A  33       1.877  10.949  32.015  1.00  8.38           C  
-ATOM    127  CD1 LEU A  33       2.947  11.817  31.384  1.00  8.17           C  
-ATOM    128  CD2 LEU A  33       2.502  10.000  33.034  1.00  5.66           C  
-ATOM    129  N   ASN A  34      -1.301  12.411  35.339  1.00  5.75           N  
-ATOM    130  CA  ASN A  34      -2.300  13.252  35.969  1.00  6.32           C  
-ATOM    131  C   ASN A  34      -1.690  14.393  36.774  1.00  8.28           C  
-ATOM    132  O   ASN A  34      -0.745  14.196  37.559  1.00  9.69           O  
-ATOM    133  CB  ASN A  34      -3.149  12.360  36.864  1.00  5.71           C  
-ATOM    134  CG  ASN A  34      -4.348  13.009  37.529  1.00  8.23           C  
-ATOM    135  OD1 ASN A  34      -4.185  13.811  38.453  1.00  8.25           O  
-ATOM    136  ND2 ASN A  34      -5.584  12.734  37.098  1.00  5.85           N  
-ATOM    137  N   SER A  35      -2.176  15.616  36.603  1.00  7.89           N  
-ATOM    138  CA  SER A  35      -1.708  16.696  37.463  1.00  9.71           C  
-ATOM    139  C   SER A  35      -2.974  17.348  37.997  1.00  8.95           C  
-ATOM    140  O   SER A  35      -3.111  18.559  37.884  1.00 10.28           O  
-ATOM    141  CB  SER A  35      -0.862  17.659  36.608  1.00 10.72           C  
-ATOM    142  OG  SER A  35      -1.582  18.192  35.472  1.00 12.92           O  
-ATOM    143  N   GLY A  38      -3.965  16.590  38.462  1.00  7.83           N  
-ATOM    144  CA  GLY A  38      -5.275  17.130  38.853  1.00  7.40           C  
-ATOM    145  C   GLY A  38      -6.339  16.771  37.804  1.00  8.53           C  
-ATOM    146  O   GLY A  38      -7.544  16.893  38.012  1.00 11.03           O  
-ATOM    147  N   TYR A  39      -5.866  16.275  36.655  1.00  7.71           N  
-ATOM    148  CA  TYR A  39      -6.654  15.896  35.489  1.00  9.26           C  
-ATOM    149  C   TYR A  39      -5.706  15.108  34.567  1.00  9.27           C  
-ATOM    150  O   TYR A  39      -4.466  15.221  34.685  1.00  7.47           O  
-ATOM    151  CB  TYR A  39      -7.168  17.155  34.743  1.00 10.50           C  
-ATOM    152  CG  TYR A  39      -6.062  18.182  34.482  1.00 12.02           C  
-ATOM    153  CD1 TYR A  39      -5.786  19.157  35.456  1.00 14.15           C  
-ATOM    154  CD2 TYR A  39      -5.292  18.132  33.310  1.00 11.97           C  
-ATOM    155  CE1 TYR A  39      -4.747  20.063  35.271  1.00 14.40           C  
-ATOM    156  CE2 TYR A  39      -4.252  19.041  33.122  1.00 11.49           C  
-ATOM    157  CZ  TYR A  39      -3.993  19.985  34.101  1.00 14.94           C  
-ATOM    158  OH  TYR A  39      -2.927  20.846  33.904  1.00 18.35           O  
-ATOM    159  N   HIS A  40      -6.247  14.293  33.660  1.00  8.97           N  
-ATOM    160  CA  HIS A  40      -5.447  13.558  32.684  1.00  7.27           C  
-ATOM    161  C   HIS A  40      -4.883  14.563  31.705  1.00  7.76           C  
-ATOM    162  O   HIS A  40      -5.697  15.284  31.103  1.00  5.95           O  
-ATOM    163  CB  HIS A  40      -6.302  12.557  31.877  1.00  7.01           C  
-ATOM    164  CG  HIS A  40      -5.585  11.936  30.656  1.00  7.76           C  
-ATOM    165  ND1 HIS A  40      -4.736  10.919  30.622  1.00  8.26           N  
-ATOM    166  CD2 HIS A  40      -5.712  12.378  29.353  1.00  7.76           C  
-ATOM    167  CE1 HIS A  40      -4.343  10.717  29.385  1.00  9.80           C  
-ATOM    168  NE2 HIS A  40      -4.939  11.609  28.631  1.00  8.87           N  
-ATOM    169  N   PHE A  41      -3.571  14.617  31.466  1.00  8.05           N  
-ATOM    170  CA  PHE A  41      -3.066  15.507  30.430  1.00  7.51           C  
-ATOM    171  C   PHE A  41      -2.218  14.792  29.369  1.00  9.02           C  
-ATOM    172  O   PHE A  41      -1.970  15.362  28.316  1.00  7.09           O  
-ATOM    173  CB  PHE A  41      -2.243  16.647  31.070  1.00  9.92           C  
-ATOM    174  CG  PHE A  41      -0.937  16.275  31.751  1.00  8.81           C  
-ATOM    175  CD1 PHE A  41      -0.933  15.896  33.092  1.00  6.92           C  
-ATOM    176  CD2 PHE A  41       0.264  16.303  31.023  1.00  8.81           C  
-ATOM    177  CE1 PHE A  41       0.276  15.541  33.700  1.00  6.93           C  
-ATOM    178  CE2 PHE A  41       1.461  15.944  31.643  1.00  7.88           C  
-ATOM    179  CZ  PHE A  41       1.468  15.563  32.979  1.00  8.64           C  
-ATOM    180  N   CYS A  42      -1.763  13.549  29.563  1.00  7.79           N  
-ATOM    181  CA  CYS A  42      -0.947  12.848  28.576  1.00  7.21           C  
-ATOM    182  C   CYS A  42      -0.945  11.364  28.912  1.00  6.93           C  
-ATOM    183  O   CYS A  42      -1.335  10.985  30.024  1.00  7.96           O  
-ATOM    184  CB  CYS A  42       0.522  13.331  28.591  1.00  5.93           C  
-ATOM    185  SG  CYS A  42       0.887  14.744  27.517  1.00  6.61           S  
-ATOM    186  N   GLY A  43      -0.610  10.530  27.937  1.00  5.78           N  
-ATOM    187  CA  GLY A  43      -0.469   9.110  28.165  1.00  3.84           C  
-ATOM    188  C   GLY A  43       1.003   8.804  28.395  1.00  4.51           C  
-ATOM    189  O   GLY A  43       1.878   9.696  28.381  1.00  4.70           O  
-ATOM    190  N   GLY A  44       1.330   7.545  28.649  1.00  5.47           N  
-ATOM    191  CA  GLY A  44       2.721   7.122  28.761  1.00  2.48           C  
-ATOM    192  C   GLY A  44       2.732   5.615  28.671  1.00  5.74           C  
-ATOM    193  O   GLY A  44       1.634   5.041  28.619  1.00  4.79           O  
-ATOM    194  N   SER A  45       3.904   4.973  28.705  1.00  4.60           N  
-ATOM    195  CA  SER A  45       4.017   3.514  28.654  1.00  7.17           C  
-ATOM    196  C   SER A  45       4.909   3.051  29.794  1.00  7.98           C  
-ATOM    197  O   SER A  45       5.997   3.623  29.999  1.00  8.66           O  
-ATOM    198  CB  SER A  45       4.679   3.034  27.370  1.00  8.19           C  
-ATOM    199  OG  SER A  45       3.981   3.511  26.249  1.00 11.90           O  
-ATOM    200  N   LEU A  46       4.484   2.046  30.559  1.00  8.55           N  
-ATOM    201  CA  LEU A  46       5.305   1.512  31.628  1.00  8.22           C  
-ATOM    202  C   LEU A  46       6.376   0.607  31.018  1.00 11.25           C  
-ATOM    203  O   LEU A  46       6.026  -0.370  30.336  1.00 11.59           O  
-ATOM    204  CB  LEU A  46       4.408   0.729  32.570  1.00  9.72           C  
-ATOM    205  CG  LEU A  46       5.029   0.260  33.879  1.00  7.34           C  
-ATOM    206  CD1 LEU A  46       5.283   1.455  34.798  1.00  9.20           C  
-ATOM    207  CD2 LEU A  46       4.095  -0.770  34.513  1.00 11.28           C  
-ATOM    208  N   ILE A  47       7.681   0.842  31.213  1.00 11.24           N  
-ATOM    209  CA  ILE A  47       8.691  -0.017  30.579  1.00 12.80           C  
-ATOM    210  C   ILE A  47       9.415  -0.918  31.562  1.00 12.51           C  
-ATOM    211  O   ILE A  47      10.263  -1.711  31.165  1.00 12.89           O  
-ATOM    212  CB  ILE A  47       9.773   0.791  29.805  1.00 13.06           C  
-ATOM    213  CG1 ILE A  47      10.463   1.823  30.705  1.00 13.44           C  
-ATOM    214  CG2 ILE A  47       9.081   1.361  28.548  1.00 15.60           C  
-ATOM    215  CD1 ILE A  47      11.590   2.637  30.015  1.00 15.05           C  
-ATOM    216  N   ASN A  48       9.176  -0.751  32.853  1.00 11.96           N  
-ATOM    217  CA  ASN A  48       9.595  -1.708  33.876  1.00 13.64           C  
-ATOM    218  C   ASN A  48       8.893  -1.269  35.142  1.00 14.14           C  
-ATOM    219  O   ASN A  48       8.150  -0.280  35.053  1.00 15.15           O  
-ATOM    220  CB  ASN A  48      11.115  -1.732  34.099  1.00 13.90           C  
-ATOM    221  CG  ASN A  48      11.819  -0.502  34.635  1.00 16.33           C  
-ATOM    222  OD1 ASN A  48      11.349   0.289  35.455  1.00 20.66           O  
-ATOM    223  ND2 ASN A  48      13.041  -0.335  34.177  1.00 18.88           N  
-ATOM    224  N   SER A  49       9.059  -1.865  36.331  1.00 12.74           N  
-ATOM    225  CA  SER A  49       8.225  -1.470  37.456  1.00 11.21           C  
-ATOM    226  C   SER A  49       8.455  -0.083  38.007  1.00 10.88           C  
-ATOM    227  O   SER A  49       7.671   0.377  38.836  1.00 13.51           O  
-ATOM    228  CB  SER A  49       8.388  -2.466  38.583  1.00 10.89           C  
-ATOM    229  OG  SER A  49       9.760  -2.696  38.800  1.00 13.85           O  
-ATOM    230  N   GLN A  50       9.505   0.635  37.648  1.00 10.18           N  
-ATOM    231  CA  GLN A  50       9.677   1.942  38.220  1.00 10.41           C  
-ATOM    232  C   GLN A  50       9.849   3.029  37.168  1.00  9.18           C  
-ATOM    233  O   GLN A  50      10.012   4.192  37.546  1.00 10.38           O  
-ATOM    234  CB  GLN A  50      10.871   1.853  39.173  1.00 14.04           C  
-ATOM    235  CG  GLN A  50      10.615   2.808  40.323  1.00 20.73           C  
-ATOM    236  CD  GLN A  50      11.521   2.651  41.530  1.00 23.07           C  
-ATOM    237  OE1 GLN A  50      12.426   1.809  41.572  1.00 25.54           O  
-ATOM    238  NE2 GLN A  50      11.305   3.506  42.527  1.00 21.99           N  
-ATOM    239  N   TRP A  51       9.784   2.758  35.855  1.00  7.28           N  
-ATOM    240  CA  TRP A  51      10.003   3.797  34.858  1.00  5.58           C  
-ATOM    241  C   TRP A  51       8.914   3.878  33.804  1.00  5.78           C  
-ATOM    242  O   TRP A  51       8.378   2.858  33.360  1.00  4.27           O  
-ATOM    243  CB  TRP A  51      11.335   3.555  34.163  1.00  4.96           C  
-ATOM    244  CG  TRP A  51      12.525   3.883  35.059  1.00  6.50           C  
-ATOM    245  CD1 TRP A  51      13.095   2.958  35.896  1.00  9.19           C  
-ATOM    246  CD2 TRP A  51      13.155   5.102  35.106  1.00  7.93           C  
-ATOM    247  NE1 TRP A  51      14.104   3.591  36.474  1.00  9.77           N  
-ATOM    248  CE2 TRP A  51      14.180   4.863  36.033  1.00  9.21           C  
-ATOM    249  CE3 TRP A  51      13.023   6.360  34.508  1.00  8.51           C  
-ATOM    250  CZ2 TRP A  51      15.082   5.878  36.367  1.00  8.90           C  
-ATOM    251  CZ3 TRP A  51      13.926   7.367  34.846  1.00 10.87           C  
-ATOM    252  CH2 TRP A  51      14.950   7.129  35.769  1.00 10.75           C  
-ATOM    253  N   VAL A  52       8.575   5.096  33.394  1.00  4.44           N  
-ATOM    254  CA  VAL A  52       7.545   5.358  32.382  1.00  6.03           C  
-ATOM    255  C   VAL A  52       8.198   6.161  31.265  1.00  5.25           C  
-ATOM    256  O   VAL A  52       9.047   7.015  31.555  1.00  4.42           O  
-ATOM    257  CB  VAL A  52       6.374   6.169  33.026  1.00  7.30           C  
-ATOM    258  CG1 VAL A  52       5.493   6.889  31.984  1.00  7.04           C  
-ATOM    259  CG2 VAL A  52       5.517   5.184  33.818  1.00  8.08           C  
-ATOM    260  N   VAL A  53       7.869   5.880  29.994  1.00  4.56           N  
-ATOM    261  CA  VAL A  53       8.370   6.724  28.916  1.00  6.49           C  
-ATOM    262  C   VAL A  53       7.171   7.499  28.364  1.00  6.77           C  
-ATOM    263  O   VAL A  53       6.046   6.967  28.324  1.00  6.75           O  
-ATOM    264  CB  VAL A  53       9.070   5.817  27.852  1.00  9.69           C  
-ATOM    265  CG1 VAL A  53       8.093   4.839  27.262  1.00 13.83           C  
-ATOM    266  CG2 VAL A  53       9.633   6.662  26.729  1.00 13.86           C  
-ATOM    267  N   SER A  54       7.342   8.788  28.056  1.00  3.22           N  
-ATOM    268  CA  SER A  54       6.262   9.576  27.497  1.00  2.91           C  
-ATOM    269  C   SER A  54       6.911  10.552  26.536  1.00  4.02           C  
-ATOM    270  O   SER A  54       8.083  10.402  26.163  1.00  5.32           O  
-ATOM    271  CB  SER A  54       5.533  10.307  28.626  1.00  2.00           C  
-ATOM    272  OG  SER A  54       4.354  11.003  28.159  1.00  2.53           O  
-ATOM    273  N   ALA A  55       6.183  11.580  26.107  1.00  4.19           N  
-ATOM    274  CA  ALA A  55       6.670  12.595  25.185  1.00  3.54           C  
-ATOM    275  C   ALA A  55       7.236  13.753  26.005  1.00  5.28           C  
-ATOM    276  O   ALA A  55       6.664  14.176  27.025  1.00  4.33           O  
-ATOM    277  CB  ALA A  55       5.519  13.129  24.323  1.00  3.55           C  
-ATOM    278  N   ALA A  56       8.357  14.327  25.563  1.00  4.69           N  
-ATOM    279  CA  ALA A  56       8.982  15.430  26.280  1.00  4.49           C  
-ATOM    280  C   ALA A  56       8.059  16.644  26.271  1.00  5.36           C  
-ATOM    281  O   ALA A  56       8.073  17.419  27.237  1.00  3.18           O  
-ATOM    282  CB  ALA A  56      10.273  15.842  25.625  1.00  2.00           C  
-ATOM    283  N   HIS A  57       7.214  16.858  25.236  1.00  5.47           N  
-ATOM    284  CA  HIS A  57       6.272  17.965  25.280  1.00  5.68           C  
-ATOM    285  C   HIS A  57       5.177  17.751  26.321  1.00  7.17           C  
-ATOM    286  O   HIS A  57       4.359  18.646  26.516  1.00  9.44           O  
-ATOM    287  CB  HIS A  57       5.620  18.223  23.908  1.00  7.52           C  
-ATOM    288  CG  HIS A  57       4.463  17.376  23.378  1.00  8.58           C  
-ATOM    289  ND1 HIS A  57       4.497  16.432  22.429  1.00 11.33           N  
-ATOM    290  CD2 HIS A  57       3.136  17.524  23.734  1.00  9.25           C  
-ATOM    291  CE1 HIS A  57       3.270  16.009  22.195  1.00 10.10           C  
-ATOM    292  NE2 HIS A  57       2.468  16.680  22.991  1.00 10.91           N  
-ATOM    293  N   CYS A  58       5.085  16.616  26.996  1.00  6.40           N  
-ATOM    294  CA  CYS A  58       4.150  16.422  28.088  1.00  9.26           C  
-ATOM    295  C   CYS A  58       4.784  16.837  29.426  1.00 11.43           C  
-ATOM    296  O   CYS A  58       4.157  16.681  30.480  1.00 13.17           O  
-ATOM    297  CB  CYS A  58       3.783  14.972  28.195  1.00  7.29           C  
-ATOM    298  SG  CYS A  58       2.752  14.415  26.835  1.00  6.61           S  
-ATOM    299  N   TYR A  59       6.025  17.324  29.470  1.00 10.42           N  
-ATOM    300  CA  TYR A  59       6.678  17.610  30.733  1.00 10.20           C  
-ATOM    301  C   TYR A  59       5.936  18.662  31.557  1.00 12.98           C  
-ATOM    302  O   TYR A  59       5.569  19.721  31.031  1.00 12.10           O  
-ATOM    303  CB  TYR A  59       8.141  18.054  30.445  1.00 10.51           C  
-ATOM    304  CG  TYR A  59       8.793  18.699  31.671  1.00  9.34           C  
-ATOM    305  CD1 TYR A  59       9.340  17.971  32.745  1.00 10.74           C  
-ATOM    306  CD2 TYR A  59       8.716  20.086  31.729  1.00 12.71           C  
-ATOM    307  CE1 TYR A  59       9.792  18.667  33.874  1.00 11.58           C  
-ATOM    308  CE2 TYR A  59       9.164  20.767  32.848  1.00 14.07           C  
-ATOM    309  CZ  TYR A  59       9.693  20.068  33.904  1.00 15.04           C  
-ATOM    310  OH  TYR A  59      10.036  20.886  34.968  1.00 22.15           O  
-ATOM    311  N   LYS A  60       5.792  18.375  32.864  1.00 12.48           N  
-ATOM    312  CA  LYS A  60       5.191  19.258  33.855  1.00 14.62           C  
-ATOM    313  C   LYS A  60       5.850  18.916  35.173  1.00 15.96           C  
-ATOM    314  O   LYS A  60       6.300  17.771  35.324  1.00 15.86           O  
-ATOM    315  CB  LYS A  60       3.731  18.992  34.137  1.00 15.81           C  
-ATOM    316  CG  LYS A  60       2.748  19.333  33.083  1.00 20.08           C  
-ATOM    317  CD  LYS A  60       1.428  19.319  33.786  1.00 19.30           C  
-ATOM    318  CE  LYS A  60       0.402  19.678  32.762  1.00 22.27           C  
-ATOM    319  NZ  LYS A  60      -0.875  19.589  33.423  1.00 25.56           N  
-ATOM    320  N   SER A  61       5.910  19.798  36.175  1.00 18.43           N  
-ATOM    321  CA  SER A  61       6.362  19.353  37.496  1.00 19.97           C  
-ATOM    322  C   SER A  61       5.139  18.772  38.191  1.00 19.95           C  
-ATOM    323  O   SER A  61       4.009  19.089  37.806  1.00 21.59           O  
-ATOM    324  CB  SER A  61       6.890  20.522  38.297  1.00 22.00           C  
-ATOM    325  OG  SER A  61       6.022  21.651  38.155  1.00 25.49           O  
-ATOM    326  N   GLY A  62       5.239  17.901  39.185  1.00 21.68           N  
-ATOM    327  CA  GLY A  62       4.036  17.448  39.895  1.00 21.33           C  
-ATOM    328  C   GLY A  62       3.194  16.389  39.176  1.00 21.27           C  
-ATOM    329  O   GLY A  62       1.959  16.375  39.270  1.00 23.70           O  
-ATOM    330  N   ILE A  63       3.843  15.428  38.531  1.00 18.59           N  
-ATOM    331  CA  ILE A  63       3.136  14.401  37.787  1.00 15.65           C  
-ATOM    332  C   ILE A  63       2.782  13.259  38.733  1.00 15.27           C  
-ATOM    333  O   ILE A  63       3.616  12.790  39.535  1.00 13.81           O  
-ATOM    334  CB  ILE A  63       4.061  13.892  36.628  1.00 16.10           C  
-ATOM    335  CG1 ILE A  63       4.309  15.010  35.626  1.00 16.48           C  
-ATOM    336  CG2 ILE A  63       3.450  12.679  35.947  1.00 16.59           C  
-ATOM    337  CD1 ILE A  63       5.310  14.707  34.454  1.00 13.98           C  
-ATOM    338  N   GLN A  64       1.549  12.774  38.661  1.00 12.80           N  
-ATOM    339  CA  GLN A  64       1.181  11.560  39.359  1.00 10.32           C  
-ATOM    340  C   GLN A  64       0.914  10.546  38.246  1.00  9.09           C  
-ATOM    341  O   GLN A  64       0.125  10.857  37.346  1.00 11.39           O  
-ATOM    342  CB  GLN A  64      -0.079  11.767  40.179  1.00 11.32           C  
-ATOM    343  CG  GLN A  64      -0.331  10.458  40.905  1.00 11.81           C  
-ATOM    344  CD  GLN A  64      -1.638  10.399  41.664  1.00 14.97           C  
-ATOM    345  OE1 GLN A  64      -1.673  10.112  42.854  1.00 19.59           O  
-ATOM    346  NE2 GLN A  64      -2.785  10.698  41.110  1.00 10.63           N  
-ATOM    347  N   VAL A  65       1.509   9.353  38.266  1.00  8.87           N  
-ATOM    348  CA  VAL A  65       1.310   8.346  37.222  1.00  9.77           C  
-ATOM    349  C   VAL A  65       0.161   7.423  37.644  1.00 10.85           C  
-ATOM    350  O   VAL A  65       0.155   6.918  38.785  1.00 10.92           O  
-ATOM    351  CB  VAL A  65       2.606   7.551  37.046  1.00  9.79           C  
-ATOM    352  CG1 VAL A  65       2.428   6.397  36.049  1.00 10.13           C  
-ATOM    353  CG2 VAL A  65       3.679   8.494  36.528  1.00  9.72           C  
-ATOM    354  N   ARG A  66      -0.816   7.184  36.757  1.00  8.24           N  
-ATOM    355  CA  ARG A  66      -1.955   6.370  37.114  1.00  6.90           C  
-ATOM    356  C   ARG A  66      -1.952   5.156  36.205  1.00  8.85           C  
-ATOM    357  O   ARG A  66      -2.052   5.276  34.977  1.00  6.50           O  
-ATOM    358  CB  ARG A  66      -3.214   7.202  36.948  1.00  7.27           C  
-ATOM    359  CG  ARG A  66      -3.236   8.406  37.910  1.00  6.78           C  
-ATOM    360  CD  ARG A  66      -4.618   9.080  37.976  1.00  8.13           C  
-ATOM    361  NE  ARG A  66      -4.740   9.802  39.245  1.00  9.71           N  
-ATOM    362  CZ  ARG A  66      -5.911   9.938  39.877  1.00 14.18           C  
-ATOM    363  NH1 ARG A  66      -7.043   9.458  39.340  1.00 13.91           N  
-ATOM    364  NH2 ARG A  66      -5.922  10.478  41.103  1.00 13.97           N  
-ATOM    365  N   LEU A  67      -1.726   4.003  36.837  1.00  8.49           N  
-ATOM    366  CA  LEU A  67      -1.595   2.709  36.180  1.00  9.07           C  
-ATOM    367  C   LEU A  67      -2.851   1.888  36.364  1.00  9.37           C  
-ATOM    368  O   LEU A  67      -3.606   2.124  37.302  1.00 10.81           O  
-ATOM    369  CB  LEU A  67      -0.432   1.920  36.771  1.00  9.63           C  
-ATOM    370  CG  LEU A  67       0.964   2.565  36.791  1.00 14.66           C  
-ATOM    371  CD1 LEU A  67       1.168   3.393  38.028  1.00 15.87           C  
-ATOM    372  CD2 LEU A  67       2.019   1.512  36.963  1.00 17.98           C  
-ATOM    373  N   GLY A  69      -3.088   0.867  35.543  1.00  8.78           N  
-ATOM    374  CA  GLY A  69      -4.245  -0.012  35.692  1.00  9.14           C  
-ATOM    375  C   GLY A  69      -5.585   0.683  35.446  1.00 11.24           C  
-ATOM    376  O   GLY A  69      -6.635   0.215  35.932  1.00  9.57           O  
-ATOM    377  N   GLU A  70      -5.573   1.781  34.682  1.00  8.49           N  
-ATOM    378  CA  GLU A  70      -6.783   2.539  34.383  1.00  8.26           C  
-ATOM    379  C   GLU A  70      -7.621   2.058  33.204  1.00  9.49           C  
-ATOM    380  O   GLU A  70      -7.107   1.588  32.180  1.00  8.48           O  
-ATOM    381  CB  GLU A  70      -6.410   4.003  34.108  1.00  8.67           C  
-ATOM    382  CG  GLU A  70      -6.015   4.843  35.332  1.00  8.04           C  
-ATOM    383  CD  GLU A  70      -7.206   5.304  36.150  1.00 11.14           C  
-ATOM    384  OE1 GLU A  70      -8.315   4.778  36.003  1.00 13.14           O  
-ATOM    385  OE2 GLU A  70      -7.087   6.241  36.929  1.00 10.46           O  
-ATOM    386  N   ASP A  71      -8.935   2.181  33.337  1.00  7.64           N  
-ATOM    387  CA  ASP A  71      -9.769   2.058  32.165  1.00  8.90           C  
-ATOM    388  C   ASP A  71     -10.610   3.324  32.197  1.00  9.89           C  
-ATOM    389  O   ASP A  71     -10.275   4.296  31.513  1.00  9.97           O  
-ATOM    390  CB  ASP A  71     -10.698   0.841  32.182  1.00  8.14           C  
-ATOM    391  CG  ASP A  71     -11.383   0.731  30.818  1.00 12.07           C  
-ATOM    392  OD1 ASP A  71     -10.762   1.006  29.783  1.00  8.99           O  
-ATOM    393  OD2 ASP A  71     -12.542   0.347  30.763  1.00  9.28           O  
-ATOM    394  N   ASN A  72     -11.657   3.418  33.019  1.00  7.71           N  
-ATOM    395  CA  ASN A  72     -12.361   4.666  33.106  1.00  8.11           C  
-ATOM    396  C   ASN A  72     -11.518   5.588  33.991  1.00  8.32           C  
-ATOM    397  O   ASN A  72     -11.278   5.305  35.193  1.00  8.80           O  
-ATOM    398  CB  ASN A  72     -13.737   4.450  33.721  1.00  7.20           C  
-ATOM    399  CG  ASN A  72     -14.580   5.693  33.565  1.00 11.02           C  
-ATOM    400  OD1 ASN A  72     -14.149   6.797  33.922  1.00 11.16           O  
-ATOM    401  ND2 ASN A  72     -15.787   5.607  33.055  1.00  9.84           N  
-ATOM    402  N   ILE A  73     -10.992   6.677  33.443  1.00  6.52           N  
-ATOM    403  CA  ILE A  73     -10.183   7.591  34.262  1.00  8.91           C  
-ATOM    404  C   ILE A  73     -10.978   8.487  35.218  1.00  8.78           C  
-ATOM    405  O   ILE A  73     -10.368   9.213  36.022  1.00  8.70           O  
-ATOM    406  CB  ILE A  73      -9.301   8.548  33.415  1.00 11.34           C  
-ATOM    407  CG1 ILE A  73     -10.150   9.298  32.392  1.00 10.19           C  
-ATOM    408  CG2 ILE A  73      -8.153   7.727  32.811  1.00 11.43           C  
-ATOM    409  CD1 ILE A  73      -9.264  10.351  31.689  1.00 15.06           C  
-ATOM    410  N   ASN A  74     -12.308   8.496  35.165  1.00  6.19           N  
-ATOM    411  CA  ASN A  74     -13.103   9.276  36.095  1.00  7.72           C  
-ATOM    412  C   ASN A  74     -13.725   8.431  37.182  1.00  7.71           C  
-ATOM    413  O   ASN A  74     -14.399   8.958  38.065  1.00  6.92           O  
-ATOM    414  CB  ASN A  74     -14.213  10.029  35.325  1.00  8.25           C  
-ATOM    415  CG  ASN A  74     -13.716  11.365  34.774  1.00 10.17           C  
-ATOM    416  OD1 ASN A  74     -12.888  12.048  35.405  1.00 10.51           O  
-ATOM    417  ND2 ASN A  74     -14.144  11.798  33.596  1.00  9.79           N  
-ATOM    418  N   VAL A  75     -13.538   7.105  37.167  1.00  8.74           N  
-ATOM    419  CA  VAL A  75     -14.182   6.225  38.147  1.00  8.18           C  
-ATOM    420  C   VAL A  75     -13.138   5.264  38.719  1.00  9.05           C  
-ATOM    421  O   VAL A  75     -12.244   4.811  37.991  1.00  7.97           O  
-ATOM    422  CB  VAL A  75     -15.340   5.433  37.443  1.00 11.52           C  
-ATOM    423  CG1 VAL A  75     -16.099   4.554  38.441  1.00 11.32           C  
-ATOM    424  CG2 VAL A  75     -16.353   6.407  36.860  1.00  8.79           C  
-ATOM    425  N   VAL A  76     -13.133   4.984  40.021  1.00 11.53           N  
-ATOM    426  CA  VAL A  76     -12.203   4.050  40.627  1.00 11.22           C  
-ATOM    427  C   VAL A  76     -12.907   2.720  40.452  1.00 13.13           C  
-ATOM    428  O   VAL A  76     -14.030   2.520  40.939  1.00 13.76           O  
-ATOM    429  CB  VAL A  76     -11.980   4.420  42.114  1.00 13.13           C  
-ATOM    430  CG1 VAL A  76     -11.225   3.338  42.846  1.00 12.56           C  
-ATOM    431  CG2 VAL A  76     -11.099   5.661  42.182  1.00 10.33           C  
-ATOM    432  N   GLU A  77     -12.247   1.834  39.716  1.00 13.08           N  
-ATOM    433  CA  GLU A  77     -12.837   0.559  39.361  1.00 14.45           C  
-ATOM    434  C   GLU A  77     -12.125  -0.598  40.035  1.00 17.04           C  
-ATOM    435  O   GLU A  77     -12.564  -1.741  39.903  1.00 18.94           O  
-ATOM    436  CB  GLU A  77     -12.796   0.363  37.848  1.00 15.00           C  
-ATOM    437  CG  GLU A  77     -13.662   1.418  37.160  1.00 17.09           C  
-ATOM    438  CD  GLU A  77     -13.626   1.367  35.652  1.00 18.53           C  
-ATOM    439  OE1 GLU A  77     -12.542   1.462  35.093  1.00 17.49           O  
-ATOM    440  OE2 GLU A  77     -14.671   1.306  35.025  1.00 19.88           O  
-ATOM    441  N   GLY A  78     -10.997  -0.394  40.713  1.00 17.96           N  
-ATOM    442  CA  GLY A  78     -10.383  -1.462  41.471  1.00 19.65           C  
-ATOM    443  C   GLY A  78      -9.026  -1.917  40.976  1.00 20.98           C  
-ATOM    444  O   GLY A  78      -8.340  -2.576  41.754  1.00 21.63           O  
-ATOM    445  N   ASN A  79      -8.569  -1.679  39.746  1.00 19.27           N  
-ATOM    446  CA  ASN A  79      -7.230  -2.152  39.394  1.00 19.71           C  
-ATOM    447  C   ASN A  79      -6.150  -1.073  39.379  1.00 16.33           C  
-ATOM    448  O   ASN A  79      -5.019  -1.320  38.950  1.00 13.26           O  
-ATOM    449  CB  ASN A  79      -7.238  -2.819  38.018  1.00 24.63           C  
-ATOM    450  CG  ASN A  79      -7.853  -4.197  38.080  1.00 28.25           C  
-ATOM    451  OD1 ASN A  79      -7.246  -5.170  38.513  1.00 32.15           O  
-ATOM    452  ND2 ASN A  79      -9.083  -4.357  37.632  1.00 31.63           N  
-ATOM    453  N   GLU A  80      -6.456   0.128  39.849  1.00 13.89           N  
-ATOM    454  CA  GLU A  80      -5.533   1.237  39.710  1.00 12.27           C  
-ATOM    455  C   GLU A  80      -4.418   1.248  40.735  1.00 11.58           C  
-ATOM    456  O   GLU A  80      -4.562   0.720  41.837  1.00 13.12           O  
-ATOM    457  CB  GLU A  80      -6.268   2.545  39.824  1.00 10.97           C  
-ATOM    458  CG  GLU A  80      -7.408   2.766  38.841  1.00  9.90           C  
-ATOM    459  CD  GLU A  80      -8.795   2.357  39.291  1.00 14.60           C  
-ATOM    460  OE1 GLU A  80      -8.985   1.575  40.230  1.00 10.87           O  
-ATOM    461  OE2 GLU A  80      -9.746   2.792  38.639  1.00 11.94           O  
-ATOM    462  N   GLN A  81      -3.288   1.837  40.358  1.00 11.63           N  
-ATOM    463  CA  GLN A  81      -2.171   2.121  41.256  1.00 10.54           C  
-ATOM    464  C   GLN A  81      -1.839   3.556  40.901  1.00 10.97           C  
-ATOM    465  O   GLN A  81      -1.648   3.850  39.705  1.00 11.50           O  
-ATOM    466  CB  GLN A  81      -0.959   1.267  40.970  1.00 12.21           C  
-ATOM    467  CG  GLN A  81      -1.245  -0.197  41.202  1.00 13.91           C  
-ATOM    468  CD  GLN A  81      -0.061  -1.098  40.904  1.00 15.67           C  
-ATOM    469  OE1 GLN A  81       1.080  -0.869  41.338  1.00 17.32           O  
-ATOM    470  NE2 GLN A  81      -0.316  -2.182  40.202  1.00 12.85           N  
-ATOM    471  N   PHE A  82      -1.811   4.489  41.854  1.00 10.03           N  
-ATOM    472  CA  PHE A  82      -1.501   5.887  41.592  1.00 10.36           C  
-ATOM    473  C   PHE A  82      -0.184   6.070  42.328  1.00 11.07           C  
-ATOM    474  O   PHE A  82      -0.114   5.844  43.543  1.00 13.28           O  
-ATOM    475  CB  PHE A  82      -2.545   6.824  42.198  1.00 11.74           C  
-ATOM    476  CG  PHE A  82      -3.997   6.624  41.767  1.00 13.43           C  
-ATOM    477  CD1 PHE A  82      -4.329   6.068  40.526  1.00 14.47           C  
-ATOM    478  CD2 PHE A  82      -5.012   7.060  42.621  1.00 14.83           C  
-ATOM    479  CE1 PHE A  82      -5.663   5.956  40.141  1.00 15.25           C  
-ATOM    480  CE2 PHE A  82      -6.347   6.938  42.221  1.00 17.16           C  
-ATOM    481  CZ  PHE A  82      -6.676   6.391  40.987  1.00 13.63           C  
-ATOM    482  N   ILE A  83       0.888   6.403  41.623  1.00  8.04           N  
-ATOM    483  CA  ILE A  83       2.222   6.537  42.206  1.00  9.33           C  
-ATOM    484  C   ILE A  83       2.779   7.889  41.760  1.00  9.89           C  
-ATOM    485  O   ILE A  83       2.738   8.195  40.559  1.00  9.46           O  
-ATOM    486  CB  ILE A  83       3.087   5.360  41.685  1.00 10.99           C  
-ATOM    487  CG1 ILE A  83       2.420   4.027  42.008  1.00 10.83           C  
-ATOM    488  CG2 ILE A  83       4.469   5.420  42.317  1.00 14.41           C  
-ATOM    489  CD1 ILE A  83       3.037   2.794  41.371  1.00 10.85           C  
-ATOM    490  N   SER A  84       3.333   8.760  42.601  1.00  8.40           N  
-ATOM    491  CA  SER A  84       3.837  10.021  42.075  1.00  9.67           C  
-ATOM    492  C   SER A  84       5.244   9.872  41.480  1.00  8.48           C  
-ATOM    493  O   SER A  84       5.986   8.951  41.836  1.00 10.23           O  
-ATOM    494  CB  SER A  84       3.841  11.100  43.181  1.00 13.64           C  
-ATOM    495  OG  SER A  84       4.570  10.741  44.349  1.00 23.21           O  
-ATOM    496  N   ALA A  85       5.624  10.757  40.565  1.00  7.83           N  
-ATOM    497  CA  ALA A  85       6.934  10.737  39.943  1.00 10.23           C  
-ATOM    498  C   ALA A  85       8.017  11.271  40.889  1.00 11.25           C  
-ATOM    499  O   ALA A  85       7.738  12.167  41.704  1.00 11.11           O  
-ATOM    500  CB  ALA A  85       6.887  11.588  38.695  1.00  9.85           C  
-ATOM    501  N   SER A  86       9.231  10.729  40.924  1.00 11.98           N  
-ATOM    502  CA  SER A  86      10.273  11.256  41.776  1.00 12.93           C  
-ATOM    503  C   SER A  86      11.234  12.067  40.929  1.00 14.20           C  
-ATOM    504  O   SER A  86      11.826  13.027  41.443  1.00 14.54           O  
-ATOM    505  CB  SER A  86      11.021  10.119  42.455  1.00 14.12           C  
-ATOM    506  OG  SER A  86      11.525   9.159  41.539  1.00 14.33           O  
-ATOM    507  N   LYS A  87      11.392  11.721  39.645  1.00 11.94           N  
-ATOM    508  CA  LYS A  87      12.305  12.425  38.746  1.00 13.97           C  
-ATOM    509  C   LYS A  87      11.703  12.375  37.346  1.00 12.48           C  
-ATOM    510  O   LYS A  87      11.099  11.358  36.967  1.00 15.34           O  
-ATOM    511  CB  LYS A  87      13.689  11.776  38.555  1.00 15.34           C  
-ATOM    512  CG  LYS A  87      14.415  11.285  39.766  1.00 24.05           C  
-ATOM    513  CD  LYS A  87      15.760  10.679  39.383  1.00 28.45           C  
-ATOM    514  CE  LYS A  87      16.277   9.998  40.656  1.00 30.50           C  
-ATOM    515  NZ  LYS A  87      17.617   9.453  40.521  1.00 31.15           N  
-ATOM    516  N   SER A  88      11.881  13.442  36.583  1.00 10.99           N  
-ATOM    517  CA  SER A  88      11.537  13.473  35.173  1.00 11.18           C  
-ATOM    518  C   SER A  88      12.816  13.795  34.418  1.00 10.34           C  
-ATOM    519  O   SER A  88      13.589  14.633  34.891  1.00 10.77           O  
-ATOM    520  CB  SER A  88      10.515  14.543  34.941  1.00 14.58           C  
-ATOM    521  OG  SER A  88       9.299  14.142  35.555  1.00 19.75           O  
-ATOM    522  N   ILE A  89      13.140  13.166  33.285  1.00  7.43           N  
-ATOM    523  CA  ILE A  89      14.352  13.433  32.529  1.00  6.45           C  
-ATOM    524  C   ILE A  89      13.928  13.639  31.085  1.00  6.83           C  
-ATOM    525  O   ILE A  89      13.542  12.699  30.396  1.00  7.22           O  
-ATOM    526  CB  ILE A  89      15.321  12.241  32.637  1.00  6.02           C  
-ATOM    527  CG1 ILE A  89      15.788  12.127  34.085  1.00  9.32           C  
-ATOM    528  CG2 ILE A  89      16.516  12.423  31.687  1.00  6.06           C  
-ATOM    529  CD1 ILE A  89      16.304  10.744  34.504  1.00  7.92           C  
-ATOM    530  N   VAL A  90      13.954  14.865  30.591  1.00  6.48           N  
-ATOM    531  CA  VAL A  90      13.588  15.115  29.196  1.00  6.18           C  
-ATOM    532  C   VAL A  90      14.838  14.794  28.387  1.00  6.82           C  
-ATOM    533  O   VAL A  90      15.958  14.970  28.895  1.00  7.18           O  
-ATOM    534  CB  VAL A  90      13.163  16.597  29.078  1.00  5.96           C  
-ATOM    535  CG1 VAL A  90      13.081  17.091  27.620  1.00  2.00           C  
-ATOM    536  CG2 VAL A  90      11.801  16.709  29.744  1.00  6.44           C  
-ATOM    537  N   HIS A  91      14.689  14.282  27.162  1.00  5.64           N  
-ATOM    538  CA  HIS A  91      15.832  13.966  26.320  1.00  5.80           C  
-ATOM    539  C   HIS A  91      16.774  15.166  26.212  1.00  7.61           C  
-ATOM    540  O   HIS A  91      16.295  16.288  26.007  1.00  7.65           O  
-ATOM    541  CB  HIS A  91      15.378  13.584  24.906  1.00  5.71           C  
-ATOM    542  CG  HIS A  91      16.537  13.019  24.100  1.00  6.55           C  
-ATOM    543  ND1 HIS A  91      17.419  13.655  23.315  1.00  7.39           N  
-ATOM    544  CD2 HIS A  91      16.886  11.688  24.121  1.00  6.09           C  
-ATOM    545  CE1 HIS A  91      18.282  12.755  22.879  1.00  6.79           C  
-ATOM    546  NE2 HIS A  91      17.952  11.588  23.371  1.00  8.62           N  
-ATOM    547  N   PRO A  92      18.103  15.026  26.298  1.00  8.03           N  
-ATOM    548  CA  PRO A  92      18.994  16.170  26.294  1.00  9.77           C  
-ATOM    549  C   PRO A  92      18.919  17.015  25.021  1.00  9.17           C  
-ATOM    550  O   PRO A  92      19.216  18.207  25.086  1.00  8.76           O  
-ATOM    551  CB  PRO A  92      20.374  15.555  26.581  1.00  9.19           C  
-ATOM    552  CG  PRO A  92      20.219  14.095  26.291  1.00 12.21           C  
-ATOM    553  CD  PRO A  92      18.807  13.842  26.797  1.00  8.29           C  
-ATOM    554  N   SER A  93      18.574  16.418  23.874  1.00  9.50           N  
-ATOM    555  CA  SER A  93      18.422  17.184  22.635  1.00  9.40           C  
-ATOM    556  C   SER A  93      16.995  17.497  22.215  1.00  8.26           C  
-ATOM    557  O   SER A  93      16.740  17.785  21.039  1.00  7.69           O  
-ATOM    558  CB  SER A  93      19.119  16.435  21.517  1.00 11.09           C  
-ATOM    559  OG  SER A  93      20.403  16.073  21.991  1.00 16.72           O  
-ATOM    560  N   TYR A  94      16.033  17.470  23.150  1.00  6.65           N  
-ATOM    561  CA  TYR A  94      14.677  17.803  22.786  1.00  6.61           C  
-ATOM    562  C   TYR A  94      14.626  19.242  22.287  1.00  7.29           C  
-ATOM    563  O   TYR A  94      15.138  20.146  22.963  1.00  7.12           O  
-ATOM    564  CB  TYR A  94      13.740  17.654  23.995  1.00  3.45           C  
-ATOM    565  CG  TYR A  94      12.335  18.202  23.743  1.00  3.47           C  
-ATOM    566  CD1 TYR A  94      11.572  17.732  22.652  1.00  4.33           C  
-ATOM    567  CD2 TYR A  94      11.802  19.159  24.598  1.00  4.32           C  
-ATOM    568  CE1 TYR A  94      10.282  18.223  22.422  1.00  5.30           C  
-ATOM    569  CE2 TYR A  94      10.498  19.656  24.378  1.00  6.34           C  
-ATOM    570  CZ  TYR A  94       9.762  19.181  23.290  1.00  5.80           C  
-ATOM    571  OH  TYR A  94       8.493  19.664  23.058  1.00  5.91           O  
-ATOM    572  N   ASN A  95      14.056  19.441  21.094  1.00  7.28           N  
-ATOM    573  CA  ASN A  95      13.850  20.776  20.564  1.00  7.05           C  
-ATOM    574  C   ASN A  95      12.342  21.066  20.483  1.00  7.91           C  
-ATOM    575  O   ASN A  95      11.624  20.509  19.631  1.00  8.93           O  
-ATOM    576  CB  ASN A  95      14.470  20.852  19.192  1.00 11.02           C  
-ATOM    577  CG  ASN A  95      14.406  22.242  18.575  1.00 13.30           C  
-ATOM    578  OD1 ASN A  95      13.467  23.007  18.751  1.00 16.22           O  
-ATOM    579  ND2 ASN A  95      15.383  22.612  17.769  1.00 15.55           N  
-ATOM    580  N   SER A  96      11.788  21.943  21.323  1.00  5.41           N  
-ATOM    581  CA  SER A  96      10.348  22.171  21.307  1.00  7.96           C  
-ATOM    582  C   SER A  96       9.825  22.870  20.047  1.00  8.69           C  
-ATOM    583  O   SER A  96       8.615  22.897  19.736  1.00 12.44           O  
-ATOM    584  CB  SER A  96       9.979  22.968  22.546  1.00 11.21           C  
-ATOM    585  OG  SER A  96      10.609  24.247  22.585  1.00 13.46           O  
-ATOM    586  N   ASN A  97      10.709  23.462  19.264  1.00  8.23           N  
-ATOM    587  CA  ASN A  97      10.276  24.100  18.040  1.00 11.35           C  
-ATOM    588  C   ASN A  97      10.083  23.129  16.886  1.00 13.62           C  
-ATOM    589  O   ASN A  97       9.071  23.258  16.169  1.00 15.13           O  
-ATOM    590  CB  ASN A  97      11.273  25.156  17.658  1.00 12.15           C  
-ATOM    591  CG  ASN A  97      11.166  26.339  18.614  1.00 14.08           C  
-ATOM    592  OD1 ASN A  97      12.174  26.992  18.841  1.00 16.60           O  
-ATOM    593  ND2 ASN A  97      10.020  26.734  19.168  1.00 10.56           N  
-ATOM    594  N   THR A  98      10.962  22.131  16.757  1.00 10.34           N  
-ATOM    595  CA  THR A  98      10.868  21.132  15.706  1.00 10.66           C  
-ATOM    596  C   THR A  98      10.209  19.833  16.147  1.00 10.28           C  
-ATOM    597  O   THR A  98       9.749  19.041  15.325  1.00 11.01           O  
-ATOM    598  CB  THR A  98      12.278  20.840  15.178  1.00 12.14           C  
-ATOM    599  OG1 THR A  98      13.067  20.325  16.255  1.00 10.76           O  
-ATOM    600  CG2 THR A  98      12.936  22.103  14.626  1.00 13.37           C  
-ATOM    601  N   LEU A  99      10.185  19.619  17.471  1.00  8.66           N  
-ATOM    602  CA  LEU A  99       9.726  18.421  18.175  1.00  8.81           C  
-ATOM    603  C   LEU A  99      10.630  17.234  17.888  1.00  7.48           C  
-ATOM    604  O   LEU A  99      10.301  16.067  18.073  1.00  9.33           O  
-ATOM    605  CB  LEU A  99       8.266  18.099  17.813  1.00 11.04           C  
-ATOM    606  CG  LEU A  99       7.284  19.115  18.409  1.00 11.83           C  
-ATOM    607  CD1 LEU A  99       5.921  18.751  17.945  1.00 11.83           C  
-ATOM    608  CD2 LEU A  99       7.228  19.061  19.909  1.00 10.56           C  
-ATOM    609  N   ASN A 100      11.869  17.513  17.475  1.00  6.60           N  
-ATOM    610  CA  ASN A 100      12.833  16.450  17.285  1.00  6.17           C  
-ATOM    611  C   ASN A 100      13.198  15.958  18.686  1.00  6.80           C  
-ATOM    612  O   ASN A 100      13.349  16.778  19.605  1.00  6.89           O  
-ATOM    613  CB  ASN A 100      14.082  16.967  16.616  1.00  8.51           C  
-ATOM    614  CG  ASN A 100      14.972  15.860  16.069  1.00  6.92           C  
-ATOM    615  OD1 ASN A 100      14.581  14.711  15.841  1.00  9.61           O  
-ATOM    616  ND2 ASN A 100      16.204  16.188  15.779  1.00  8.43           N  
-ATOM    617  N   ASN A 101      13.285  14.633  18.851  1.00  4.60           N  
-ATOM    618  CA  ASN A 101      13.604  13.993  20.123  1.00  5.14           C  
-ATOM    619  C   ASN A 101      12.550  14.236  21.200  1.00  5.41           C  
-ATOM    620  O   ASN A 101      12.853  14.474  22.381  1.00  6.52           O  
-ATOM    621  CB  ASN A 101      14.947  14.460  20.665  1.00  6.50           C  
-ATOM    622  CG  ASN A 101      16.091  14.327  19.686  1.00  6.08           C  
-ATOM    623  OD1 ASN A 101      16.739  15.310  19.343  1.00 11.92           O  
-ATOM    624  ND2 ASN A 101      16.454  13.164  19.199  1.00  3.39           N  
-ATOM    625  N   ASP A 102      11.289  14.085  20.812  1.00  2.50           N  
-ATOM    626  CA  ASP A 102      10.185  14.266  21.742  1.00  3.39           C  
-ATOM    627  C   ASP A 102       9.963  13.022  22.608  1.00  4.83           C  
-ATOM    628  O   ASP A 102       9.118  12.153  22.355  1.00  4.45           O  
-ATOM    629  CB  ASP A 102       8.944  14.616  20.923  1.00  2.00           C  
-ATOM    630  CG  ASP A 102       7.756  15.041  21.761  1.00  3.47           C  
-ATOM    631  OD1 ASP A 102       7.882  15.306  22.950  1.00  3.49           O  
-ATOM    632  OD2 ASP A 102       6.648  15.099  21.242  1.00  4.01           O  
-ATOM    633  N   ILE A 103      10.751  12.865  23.674  1.00  4.92           N  
-ATOM    634  CA  ILE A 103      10.696  11.683  24.517  1.00  4.56           C  
-ATOM    635  C   ILE A 103      11.227  12.057  25.899  1.00  5.98           C  
-ATOM    636  O   ILE A 103      12.112  12.933  26.031  1.00  8.50           O  
-ATOM    637  CB  ILE A 103      11.551  10.545  23.827  1.00  5.11           C  
-ATOM    638  CG1 ILE A 103      11.449   9.284  24.662  1.00  6.26           C  
-ATOM    639  CG2 ILE A 103      13.028  10.962  23.654  1.00  7.49           C  
-ATOM    640  CD1 ILE A 103      12.088   8.044  23.979  1.00  6.11           C  
-ATOM    641  N   MET A 104      10.664  11.476  26.943  1.00  4.18           N  
-ATOM    642  CA  MET A 104      11.108  11.729  28.301  1.00  6.63           C  
-ATOM    643  C   MET A 104      10.888  10.491  29.149  1.00  5.56           C  
-ATOM    644  O   MET A 104      10.024   9.670  28.834  1.00  6.70           O  
-ATOM    645  CB  MET A 104      10.350  12.896  28.945  1.00  9.07           C  
-ATOM    646  CG  MET A 104       8.915  12.709  29.368  1.00 15.92           C  
-ATOM    647  SD  MET A 104       8.331  14.178  30.261  1.00 16.40           S  
-ATOM    648  CE  MET A 104       9.346  13.936  31.681  1.00 21.28           C  
-ATOM    649  N   LEU A 105      11.688  10.341  30.197  1.00  5.19           N  
-ATOM    650  CA  LEU A 105      11.600   9.227  31.131  1.00  5.06           C  
-ATOM    651  C   LEU A 105      11.077   9.777  32.453  1.00  4.79           C  
-ATOM    652  O   LEU A 105      11.426  10.895  32.854  1.00  5.37           O  
-ATOM    653  CB  LEU A 105      12.982   8.611  31.336  1.00  5.54           C  
-ATOM    654  CG  LEU A 105      13.403   7.327  30.600  1.00 13.07           C  
-ATOM    655  CD1 LEU A 105      12.598   7.108  29.361  1.00 13.91           C  
-ATOM    656  CD2 LEU A 105      14.883   7.412  30.294  1.00 10.01           C  
-ATOM    657  N   ILE A 106      10.213   9.024  33.114  1.00  4.92           N  
-ATOM    658  CA  ILE A 106       9.659   9.417  34.408  1.00  5.91           C  
-ATOM    659  C   ILE A 106       9.951   8.284  35.369  1.00  6.28           C  
-ATOM    660  O   ILE A 106       9.571   7.144  35.104  1.00  6.25           O  
-ATOM    661  CB  ILE A 106       8.145   9.633  34.302  1.00  4.20           C  
-ATOM    662  CG1 ILE A 106       7.814  10.875  33.503  1.00  6.05           C  
-ATOM    663  CG2 ILE A 106       7.587   9.868  35.709  1.00  8.78           C  
-ATOM    664  CD1 ILE A 106       6.344  10.882  33.037  1.00  8.81           C  
-ATOM    665  N   LYS A 107      10.627   8.549  36.470  1.00  7.00           N  
-ATOM    666  CA  LYS A 107      10.835   7.510  37.472  1.00  7.95           C  
-ATOM    667  C   LYS A 107       9.730   7.601  38.537  1.00  6.77           C  
-ATOM    668  O   LYS A 107       9.402   8.681  39.044  1.00  9.44           O  
-ATOM    669  CB  LYS A 107      12.229   7.685  38.132  1.00  5.82           C  
-ATOM    670  CG  LYS A 107      12.546   6.586  39.153  1.00  7.85           C  
-ATOM    671  CD  LYS A 107      13.963   6.600  39.675  1.00  8.01           C  
-ATOM    672  CE  LYS A 107      14.210   5.408  40.610  1.00  8.89           C  
-ATOM    673  NZ  LYS A 107      15.624   5.101  40.735  1.00 13.36           N  
-ATOM    674  N   LEU A 108       9.158   6.480  38.932  1.00  8.26           N  
-ATOM    675  CA  LEU A 108       8.150   6.401  39.980  1.00 10.58           C  
-ATOM    676  C   LEU A 108       8.777   6.390  41.384  1.00 12.99           C  
-ATOM    677  O   LEU A 108       9.852   5.807  41.602  1.00 11.25           O  
-ATOM    678  CB  LEU A 108       7.330   5.124  39.793  1.00  9.49           C  
-ATOM    679  CG  LEU A 108       6.675   4.911  38.440  1.00  9.76           C  
-ATOM    680  CD1 LEU A 108       5.908   3.615  38.420  1.00  9.26           C  
-ATOM    681  CD2 LEU A 108       5.774   6.066  38.160  1.00  9.48           C  
-ATOM    682  N   LYS A 109       8.102   6.991  42.370  1.00 13.60           N  
-ATOM    683  CA  LYS A 109       8.591   6.993  43.750  1.00 16.97           C  
-ATOM    684  C   LYS A 109       8.753   5.608  44.361  1.00 14.94           C  
-ATOM    685  O   LYS A 109       9.620   5.385  45.203  1.00 15.15           O  
-ATOM    686  CB  LYS A 109       7.665   7.784  44.658  1.00 20.00           C  
-ATOM    687  CG  LYS A 109       7.930   9.247  44.450  1.00 26.44           C  
-ATOM    688  CD  LYS A 109       7.379  10.058  45.603  1.00 30.56           C  
-ATOM    689  CE  LYS A 109       7.719  11.546  45.414  1.00 32.73           C  
-ATOM    690  NZ  LYS A 109       7.039  12.064  44.244  1.00 34.40           N  
-ATOM    691  N   SER A 110       7.922   4.663  43.963  1.00 14.68           N  
-ATOM    692  CA  SER A 110       8.002   3.300  44.410  1.00 16.49           C  
-ATOM    693  C   SER A 110       7.646   2.438  43.216  1.00 16.58           C  
-ATOM    694  O   SER A 110       6.982   2.904  42.285  1.00 18.59           O  
-ATOM    695  CB  SER A 110       7.021   3.077  45.559  1.00 19.79           C  
-ATOM    696  OG  SER A 110       5.829   3.855  45.475  1.00 25.72           O  
-ATOM    697  N   ALA A 111       8.112   1.205  43.199  1.00 16.04           N  
-ATOM    698  CA  ALA A 111       7.827   0.322  42.100  1.00 15.08           C  
-ATOM    699  C   ALA A 111       6.354  -0.051  42.070  1.00 15.79           C  
-ATOM    700  O   ALA A 111       5.695  -0.136  43.113  1.00 15.44           O  
-ATOM    701  CB  ALA A 111       8.664  -0.923  42.250  1.00 15.40           C  
-ATOM    702  N   ALA A 112       5.807  -0.168  40.868  1.00 13.92           N  
-ATOM    703  CA  ALA A 112       4.456  -0.650  40.655  1.00 15.71           C  
-ATOM    704  C   ALA A 112       4.420  -2.147  40.954  1.00 16.05           C  
-ATOM    705  O   ALA A 112       5.455  -2.819  40.855  1.00 17.25           O  
-ATOM    706  CB  ALA A 112       4.051  -0.442  39.196  1.00 12.10           C  
-ATOM    707  N   SER A 113       3.263  -2.705  41.319  1.00 18.09           N  
-ATOM    708  CA  SER A 113       3.112  -4.143  41.491  1.00 18.19           C  
-ATOM    709  C   SER A 113       2.670  -4.662  40.130  1.00 19.14           C  
-ATOM    710  O   SER A 113       1.579  -4.288  39.677  1.00 19.85           O  
-ATOM    711  CB  SER A 113       2.036  -4.427  42.508  1.00 19.69           C  
-ATOM    712  OG  SER A 113       2.322  -3.758  43.726  1.00 28.99           O  
-ATOM    713  N   LEU A 114       3.458  -5.471  39.438  1.00 19.94           N  
-ATOM    714  CA  LEU A 114       3.127  -5.946  38.111  1.00 22.56           C  
-ATOM    715  C   LEU A 114       2.342  -7.257  38.154  1.00 26.68           C  
-ATOM    716  O   LEU A 114       2.585  -8.119  38.996  1.00 29.80           O  
-ATOM    717  CB  LEU A 114       4.449  -6.050  37.370  1.00 20.67           C  
-ATOM    718  CG  LEU A 114       4.876  -4.933  36.400  1.00 21.05           C  
-ATOM    719  CD1 LEU A 114       4.639  -3.576  36.968  1.00 21.78           C  
-ATOM    720  CD2 LEU A 114       6.346  -5.085  36.106  1.00 22.99           C  
-ATOM    721  N   ASN A 115       1.374  -7.463  37.266  1.00 29.84           N  
-ATOM    722  CA  ASN A 115       0.410  -8.567  37.265  1.00 31.57           C  
-ATOM    723  C   ASN A 115      -0.184  -8.672  35.855  1.00 31.35           C  
-ATOM    724  O   ASN A 115       0.422  -8.111  34.939  1.00 32.66           O  
-ATOM    725  CB  ASN A 115      -0.688  -8.274  38.301  1.00 34.37           C  
-ATOM    726  CG  ASN A 115      -1.378  -6.933  38.075  1.00 38.97           C  
-ATOM    727  OD1 ASN A 115      -2.174  -6.792  37.146  1.00 39.84           O  
-ATOM    728  ND2 ASN A 115      -1.077  -5.891  38.843  1.00 38.31           N  
-ATOM    729  N   SER A 116      -1.298  -9.340  35.546  1.00 30.38           N  
-ATOM    730  CA  SER A 116      -1.769  -9.423  34.164  1.00 31.67           C  
-ATOM    731  C   SER A 116      -2.400  -8.136  33.633  1.00 30.52           C  
-ATOM    732  O   SER A 116      -2.394  -7.849  32.433  1.00 30.57           O  
-ATOM    733  CB  SER A 116      -2.779 -10.570  34.047  1.00 33.69           C  
-ATOM    734  OG  SER A 116      -3.681 -10.576  35.158  1.00 36.11           O  
-ATOM    735  N   ARG A 117      -2.963  -7.359  34.554  1.00 29.13           N  
-ATOM    736  CA  ARG A 117      -3.613  -6.117  34.209  1.00 27.12           C  
-ATOM    737  C   ARG A 117      -2.686  -4.924  34.307  1.00 25.33           C  
-ATOM    738  O   ARG A 117      -3.042  -3.876  33.749  1.00 26.44           O  
-ATOM    739  CB  ARG A 117      -4.814  -5.937  35.114  1.00 29.56           C  
-ATOM    740  CG  ARG A 117      -5.841  -7.025  34.788  1.00 34.25           C  
-ATOM    741  CD  ARG A 117      -7.089  -6.854  35.635  1.00 39.62           C  
-ATOM    742  NE  ARG A 117      -8.103  -7.860  35.327  1.00 44.72           N  
-ATOM    743  CZ  ARG A 117      -8.951  -7.757  34.278  1.00 47.90           C  
-ATOM    744  NH1 ARG A 117      -8.890  -6.701  33.446  1.00 47.09           N  
-ATOM    745  NH2 ARG A 117      -9.880  -8.712  34.087  1.00 49.32           N  
-ATOM    746  N   VAL A 118      -1.552  -4.984  35.024  1.00 19.39           N  
-ATOM    747  CA  VAL A 118      -0.584  -3.886  35.024  1.00 16.88           C  
-ATOM    748  C   VAL A 118       0.702  -4.600  34.677  1.00 14.34           C  
-ATOM    749  O   VAL A 118       1.205  -5.380  35.482  1.00 12.36           O  
-ATOM    750  CB  VAL A 118      -0.435  -3.172  36.407  1.00 13.85           C  
-ATOM    751  CG1 VAL A 118       0.642  -2.085  36.334  1.00 15.11           C  
-ATOM    752  CG2 VAL A 118      -1.736  -2.471  36.777  1.00 16.93           C  
-ATOM    753  N   ALA A 119       1.254  -4.337  33.499  1.00 12.46           N  
-ATOM    754  CA  ALA A 119       2.417  -5.055  33.000  1.00 11.93           C  
-ATOM    755  C   ALA A 119       3.282  -4.092  32.216  1.00 12.89           C  
-ATOM    756  O   ALA A 119       2.753  -3.070  31.775  1.00 15.11           O  
-ATOM    757  CB  ALA A 119       1.960  -6.152  32.071  1.00 12.10           C  
-ATOM    758  N   SER A 120       4.577  -4.346  32.038  1.00 12.39           N  
-ATOM    759  CA  SER A 120       5.419  -3.463  31.250  1.00 13.92           C  
-ATOM    760  C   SER A 120       5.477  -3.890  29.798  1.00 13.65           C  
-ATOM    761  O   SER A 120       5.086  -5.013  29.468  1.00 14.45           O  
-ATOM    762  CB  SER A 120       6.812  -3.457  31.844  1.00 14.87           C  
-ATOM    763  OG  SER A 120       7.252  -4.786  32.074  1.00 19.12           O  
-ATOM    764  N   ILE A 121       5.941  -3.031  28.896  1.00 13.36           N  
-ATOM    765  CA  ILE A 121       6.059  -3.349  27.483  1.00 11.80           C  
-ATOM    766  C   ILE A 121       7.546  -3.350  27.180  1.00 13.44           C  
-ATOM    767  O   ILE A 121       8.305  -2.512  27.688  1.00 14.89           O  
-ATOM    768  CB  ILE A 121       5.283  -2.279  26.649  1.00 11.06           C  
-ATOM    769  CG1 ILE A 121       5.344  -2.609  25.179  1.00 12.83           C  
-ATOM    770  CG2 ILE A 121       5.826  -0.882  26.961  1.00 10.16           C  
-ATOM    771  CD1 ILE A 121       4.530  -3.888  24.852  1.00 11.82           C  
-ATOM    772  N   SER A 122       7.977  -4.292  26.359  1.00 12.00           N  
-ATOM    773  CA  SER A 122       9.378  -4.397  26.014  1.00 14.74           C  
-ATOM    774  C   SER A 122       9.793  -3.314  25.041  1.00 13.25           C  
-ATOM    775  O   SER A 122       9.029  -2.894  24.168  1.00 11.24           O  
-ATOM    776  CB  SER A 122       9.668  -5.731  25.353  1.00 17.28           C  
-ATOM    777  OG  SER A 122       9.260  -6.834  26.152  1.00 25.80           O  
-ATOM    778  N   LEU A 123      11.046  -2.927  25.202  1.00 11.83           N  
-ATOM    779  CA  LEU A 123      11.687  -2.000  24.294  1.00 11.68           C  
-ATOM    780  C   LEU A 123      12.116  -2.790  23.061  1.00 11.44           C  
-ATOM    781  O   LEU A 123      12.386  -3.996  23.145  1.00 11.16           O  
-ATOM    782  CB  LEU A 123      12.912  -1.388  24.977  1.00 11.15           C  
-ATOM    783  CG  LEU A 123      12.663  -0.435  26.149  1.00 11.11           C  
-ATOM    784  CD1 LEU A 123      14.016   0.062  26.667  1.00 14.83           C  
-ATOM    785  CD2 LEU A 123      11.805   0.752  25.689  1.00 12.47           C  
-ATOM    786  N   PRO A 124      12.186  -2.195  21.890  1.00 10.39           N  
-ATOM    787  CA  PRO A 124      12.496  -2.924  20.673  1.00 13.04           C  
-ATOM    788  C   PRO A 124      13.967  -3.267  20.477  1.00 14.87           C  
-ATOM    789  O   PRO A 124      14.834  -2.529  20.932  1.00 15.68           O  
-ATOM    790  CB  PRO A 124      11.935  -2.027  19.595  1.00 10.12           C  
-ATOM    791  CG  PRO A 124      12.164  -0.654  20.133  1.00 11.43           C  
-ATOM    792  CD  PRO A 124      11.845  -0.790  21.634  1.00  8.57           C  
-ATOM    793  N   THR A 125      14.304  -4.371  19.823  1.00 15.00           N  
-ATOM    794  CA  THR A 125      15.687  -4.601  19.453  1.00 18.40           C  
-ATOM    795  C   THR A 125      15.908  -4.193  18.003  1.00 17.24           C  
-ATOM    796  O   THR A 125      17.052  -4.177  17.555  1.00 18.20           O  
-ATOM    797  CB  THR A 125      16.060  -6.093  19.647  1.00 20.21           C  
-ATOM    798  OG1 THR A 125      14.984  -6.904  19.203  1.00 24.98           O  
-ATOM    799  CG2 THR A 125      16.346  -6.393  21.106  1.00 23.18           C  
-ATOM    800  N   SER A 127      14.881  -3.858  17.209  1.00 16.92           N  
-ATOM    801  CA  SER A 127      15.030  -3.489  15.798  1.00 15.86           C  
-ATOM    802  C   SER A 127      14.017  -2.393  15.536  1.00 15.24           C  
-ATOM    803  O   SER A 127      13.078  -2.247  16.318  1.00 16.71           O  
-ATOM    804  CB  SER A 127      14.675  -4.628  14.848  1.00 16.15           C  
-ATOM    805  OG  SER A 127      15.278  -5.823  15.318  1.00 29.06           O  
-ATOM    806  N   CYS A 128      14.160  -1.609  14.474  1.00 13.86           N  
-ATOM    807  CA  CYS A 128      13.185  -0.593  14.145  1.00 12.05           C  
-ATOM    808  C   CYS A 128      12.111  -1.283  13.339  1.00 12.61           C  
-ATOM    809  O   CYS A 128      12.433  -2.188  12.578  1.00 16.73           O  
-ATOM    810  CB  CYS A 128      13.796   0.478  13.307  1.00 10.55           C  
-ATOM    811  SG  CYS A 128      15.040   1.359  14.241  1.00 12.18           S  
-ATOM    812  N   ALA A 129      10.845  -0.944  13.473  1.00 12.17           N  
-ATOM    813  CA  ALA A 129       9.823  -1.590  12.682  1.00 13.96           C  
-ATOM    814  C   ALA A 129       9.786  -0.994  11.275  1.00 15.44           C  
-ATOM    815  O   ALA A 129      10.159   0.159  11.060  1.00 16.61           O  
-ATOM    816  CB  ALA A 129       8.484  -1.401  13.366  1.00 13.76           C  
-ATOM    817  N   SER A 131       9.368  -1.751  10.283  1.00 16.01           N  
-ATOM    818  CA  SER A 131       9.323  -1.282   8.916  1.00 16.53           C  
-ATOM    819  C   SER A 131       7.917  -0.820   8.543  1.00 14.77           C  
-ATOM    820  O   SER A 131       6.911  -1.202   9.148  1.00 13.69           O  
-ATOM    821  CB  SER A 131       9.748  -2.421   7.984  1.00 18.03           C  
-ATOM    822  OG  SER A 131      11.069  -2.885   8.300  1.00 25.57           O  
-ATOM    823  N   ALA A 132       7.876   0.021   7.512  1.00 16.48           N  
-ATOM    824  CA  ALA A 132       6.659   0.499   6.881  1.00 15.44           C  
-ATOM    825  C   ALA A 132       5.774  -0.682   6.522  1.00 16.21           C  
-ATOM    826  O   ALA A 132       6.275  -1.729   6.110  1.00 19.76           O  
-ATOM    827  CB  ALA A 132       7.012   1.241   5.608  1.00 16.00           C  
-ATOM    828  N   GLY A 133       4.489  -0.590   6.791  1.00 14.13           N  
-ATOM    829  CA  GLY A 133       3.575  -1.648   6.461  1.00 14.08           C  
-ATOM    830  C   GLY A 133       3.231  -2.479   7.674  1.00 15.55           C  
-ATOM    831  O   GLY A 133       2.209  -3.161   7.631  1.00 17.14           O  
-ATOM    832  N   THR A 134       4.016  -2.475   8.763  1.00 16.04           N  
-ATOM    833  CA  THR A 134       3.678  -3.252   9.962  1.00 15.91           C  
-ATOM    834  C   THR A 134       2.463  -2.589  10.633  1.00 14.39           C  
-ATOM    835  O   THR A 134       2.436  -1.354  10.750  1.00 12.98           O  
-ATOM    836  CB  THR A 134       4.871  -3.263  10.975  1.00 19.37           C  
-ATOM    837  OG1 THR A 134       6.058  -3.628  10.274  1.00 21.22           O  
-ATOM    838  CG2 THR A 134       4.660  -4.265  12.094  1.00 16.92           C  
-ATOM    839  N   GLN A 135       1.478  -3.370  11.056  1.00 12.38           N  
-ATOM    840  CA  GLN A 135       0.275  -2.857  11.680  1.00 14.82           C  
-ATOM    841  C   GLN A 135       0.598  -2.695  13.168  1.00 15.20           C  
-ATOM    842  O   GLN A 135       1.195  -3.601  13.769  1.00 14.34           O  
-ATOM    843  CB  GLN A 135      -0.858  -3.869  11.441  1.00 20.06           C  
-ATOM    844  CG  GLN A 135      -2.297  -3.601  11.901  1.00 26.27           C  
-ATOM    845  CD  GLN A 135      -3.088  -2.598  11.062  1.00 34.38           C  
-ATOM    846  OE1 GLN A 135      -2.534  -1.729  10.390  1.00 37.68           O  
-ATOM    847  NE2 GLN A 135      -4.420  -2.599  11.058  1.00 35.98           N  
-ATOM    848  N   CYS A 136       0.234  -1.566  13.778  1.00 11.73           N  
-ATOM    849  CA  CYS A 136       0.524  -1.283  15.185  1.00 11.38           C  
-ATOM    850  C   CYS A 136      -0.731  -0.888  15.959  1.00  9.03           C  
-ATOM    851  O   CYS A 136      -1.751  -0.559  15.355  1.00 10.37           O  
-ATOM    852  CB  CYS A 136       1.515  -0.147  15.280  1.00  9.44           C  
-ATOM    853  SG  CYS A 136       3.038  -0.427  14.358  1.00 10.43           S  
-ATOM    854  N   LEU A 137      -0.693  -0.891  17.287  1.00  6.87           N  
-ATOM    855  CA  LEU A 137      -1.815  -0.533  18.139  1.00  5.47           C  
-ATOM    856  C   LEU A 137      -1.449   0.754  18.865  1.00  7.05           C  
-ATOM    857  O   LEU A 137      -0.419   0.808  19.573  1.00  6.76           O  
-ATOM    858  CB  LEU A 137      -2.060  -1.609  19.185  1.00  6.98           C  
-ATOM    859  CG  LEU A 137      -3.194  -1.394  20.172  1.00 10.08           C  
-ATOM    860  CD1 LEU A 137      -4.547  -1.451  19.433  1.00  7.03           C  
-ATOM    861  CD2 LEU A 137      -3.133  -2.483  21.238  1.00  8.69           C  
-ATOM    862  N   ILE A 138      -2.273   1.771  18.663  1.00  4.20           N  
-ATOM    863  CA  ILE A 138      -2.092   3.064  19.295  1.00  3.31           C  
-ATOM    864  C   ILE A 138      -3.245   3.185  20.286  1.00  5.47           C  
-ATOM    865  O   ILE A 138      -4.379   2.800  19.935  1.00  5.10           O  
-ATOM    866  CB  ILE A 138      -2.169   4.172  18.225  1.00  5.22           C  
-ATOM    867  CG1 ILE A 138      -1.044   3.927  17.225  1.00  6.82           C  
-ATOM    868  CG2 ILE A 138      -2.073   5.581  18.863  1.00  4.83           C  
-ATOM    869  CD1 ILE A 138      -1.286   4.582  15.839  1.00 10.22           C  
-ATOM    870  N   SER A 139      -3.030   3.719  21.493  1.00  4.71           N  
-ATOM    871  CA  SER A 139      -4.128   3.833  22.441  1.00  5.12           C  
-ATOM    872  C   SER A 139      -4.057   5.131  23.253  1.00  6.62           C  
-ATOM    873  O   SER A 139      -2.958   5.705  23.382  1.00  6.97           O  
-ATOM    874  CB  SER A 139      -4.104   2.610  23.366  1.00  3.99           C  
-ATOM    875  OG  SER A 139      -2.802   2.374  23.871  1.00  5.18           O  
-ATOM    876  N   GLY A 140      -5.183   5.633  23.789  1.00  5.22           N  
-ATOM    877  CA  GLY A 140      -5.135   6.812  24.623  1.00  4.59           C  
-ATOM    878  C   GLY A 140      -6.540   7.308  24.940  1.00  7.36           C  
-ATOM    879  O   GLY A 140      -7.540   6.811  24.399  1.00  6.71           O  
-ATOM    880  N   TRP A 141      -6.632   8.288  25.846  1.00  8.00           N  
-ATOM    881  CA  TRP A 141      -7.888   8.897  26.269  1.00  7.38           C  
-ATOM    882  C   TRP A 141      -8.053  10.278  25.610  1.00  8.82           C  
-ATOM    883  O   TRP A 141      -8.745  11.161  26.136  1.00  9.44           O  
-ATOM    884  CB  TRP A 141      -7.905   9.063  27.819  1.00  8.39           C  
-ATOM    885  CG  TRP A 141      -7.961   7.766  28.626  1.00  8.06           C  
-ATOM    886  CD1 TRP A 141      -9.171   7.178  28.919  1.00  9.63           C  
-ATOM    887  CD2 TRP A 141      -6.899   7.072  29.155  1.00  8.00           C  
-ATOM    888  NE1 TRP A 141      -8.879   6.109  29.640  1.00  8.55           N  
-ATOM    889  CE2 TRP A 141      -7.551   6.001  29.801  1.00  7.57           C  
-ATOM    890  CE3 TRP A 141      -5.498   7.172  29.202  1.00  7.16           C  
-ATOM    891  CZ2 TRP A 141      -6.821   5.027  30.495  1.00  8.38           C  
-ATOM    892  CZ3 TRP A 141      -4.783   6.196  29.904  1.00  7.87           C  
-ATOM    893  CH2 TRP A 141      -5.438   5.136  30.542  1.00  6.21           C  
-ATOM    894  N   GLY A 142      -7.402  10.548  24.478  1.00  7.44           N  
-ATOM    895  CA  GLY A 142      -7.507  11.861  23.847  1.00  7.92           C  
-ATOM    896  C   GLY A 142      -8.805  12.080  23.097  1.00  8.95           C  
-ATOM    897  O   GLY A 142      -9.692  11.217  23.045  1.00  8.86           O  
-ATOM    898  N   ASN A 143      -8.900  13.256  22.476  1.00 10.47           N  
-ATOM    899  CA  ASN A 143     -10.055  13.638  21.668  1.00 10.86           C  
-ATOM    900  C   ASN A 143     -10.459  12.605  20.595  1.00 10.54           C  
-ATOM    901  O   ASN A 143      -9.616  11.953  19.932  1.00 10.37           O  
-ATOM    902  CB  ASN A 143      -9.753  14.963  20.992  1.00 10.86           C  
-ATOM    903  CG  ASN A 143     -10.950  15.710  20.431  1.00 12.80           C  
-ATOM    904  OD1 ASN A 143     -10.799  16.788  19.864  1.00 16.47           O  
-ATOM    905  ND2 ASN A 143     -12.208  15.325  20.567  1.00 11.06           N  
-ATOM    906  N   THR A 144     -11.774  12.390  20.468  1.00 11.38           N  
-ATOM    907  CA  THR A 144     -12.269  11.431  19.487  1.00 12.99           C  
-ATOM    908  C   THR A 144     -12.869  12.103  18.251  1.00 14.75           C  
-ATOM    909  O   THR A 144     -13.452  11.422  17.393  1.00 12.71           O  
-ATOM    910  CB  THR A 144     -13.344  10.489  20.122  1.00 13.62           C  
-ATOM    911  OG1 THR A 144     -14.408  11.324  20.599  1.00 14.20           O  
-ATOM    912  CG2 THR A 144     -12.784   9.612  21.245  1.00 10.79           C  
-ATOM    913  N   LYS A 145     -12.764  13.426  18.081  1.00 15.88           N  
-ATOM    914  CA  LYS A 145     -13.405  14.099  16.957  1.00 19.52           C  
-ATOM    915  C   LYS A 145     -12.389  14.937  16.168  1.00 20.40           C  
-ATOM    916  O   LYS A 145     -11.478  15.504  16.773  1.00 19.67           O  
-ATOM    917  CB  LYS A 145     -14.529  14.991  17.506  1.00 23.67           C  
-ATOM    918  CG  LYS A 145     -15.572  14.301  18.408  1.00 28.36           C  
-ATOM    919  CD  LYS A 145     -16.440  13.302  17.647  1.00 35.06           C  
-ATOM    920  CE  LYS A 145     -17.355  12.420  18.537  1.00 38.94           C  
-ATOM    921  NZ  LYS A 145     -16.653  11.315  19.189  1.00 41.05           N  
-ATOM    922  N   SER A 146     -12.450  15.047  14.838  1.00 22.88           N  
-ATOM    923  CA  SER A 146     -11.520  15.905  14.094  1.00 26.19           C  
-ATOM    924  C   SER A 146     -12.006  17.341  13.965  1.00 27.15           C  
-ATOM    925  O   SER A 146     -11.285  18.250  13.516  1.00 28.75           O  
-ATOM    926  CB  SER A 146     -11.294  15.317  12.712  1.00 26.30           C  
-ATOM    927  OG  SER A 146     -12.478  14.685  12.228  1.00 32.84           O  
-ATOM    928  N   SER A 147     -13.273  17.533  14.319  1.00 28.21           N  
-ATOM    929  CA  SER A 147     -13.888  18.836  14.360  1.00 29.88           C  
-ATOM    930  C   SER A 147     -14.697  18.839  15.647  1.00 28.95           C  
-ATOM    931  O   SER A 147     -15.536  17.967  15.895  1.00 28.99           O  
-ATOM    932  CB  SER A 147     -14.761  19.008  13.121  1.00 31.44           C  
-ATOM    933  OG  SER A 147     -13.880  19.063  11.986  1.00 37.22           O  
-ATOM    934  N   GLY A 148     -14.413  19.783  16.522  1.00 27.87           N  
-ATOM    935  CA  GLY A 148     -15.113  19.817  17.795  1.00 27.38           C  
-ATOM    936  C   GLY A 148     -14.344  18.970  18.800  1.00 26.00           C  
-ATOM    937  O   GLY A 148     -13.251  18.459  18.518  1.00 25.16           O  
-ATOM    938  N   THR A 149     -14.905  18.803  19.990  1.00 23.73           N  
-ATOM    939  CA  THR A 149     -14.216  18.123  21.070  1.00 22.99           C  
-ATOM    940  C   THR A 149     -15.140  17.218  21.877  1.00 21.36           C  
-ATOM    941  O   THR A 149     -16.266  17.605  22.220  1.00 21.73           O  
-ATOM    942  CB  THR A 149     -13.579  19.227  21.935  1.00 22.74           C  
-ATOM    943  OG1 THR A 149     -12.562  19.818  21.133  1.00 27.67           O  
-ATOM    944  CG2 THR A 149     -13.020  18.730  23.236  1.00 21.86           C  
-ATOM    945  N   SER A 150     -14.655  15.994  22.127  1.00 18.38           N  
-ATOM    946  CA  SER A 150     -15.321  15.041  22.986  1.00 17.25           C  
-ATOM    947  C   SER A 150     -14.225  14.097  23.456  1.00 16.83           C  
-ATOM    948  O   SER A 150     -13.538  13.433  22.653  1.00 17.77           O  
-ATOM    949  CB  SER A 150     -16.364  14.258  22.244  1.00 17.94           C  
-ATOM    950  OG  SER A 150     -17.232  13.610  23.163  1.00 20.79           O  
-ATOM    951  N   TYR A 151     -13.995  14.174  24.756  1.00 14.39           N  
-ATOM    952  CA  TYR A 151     -12.985  13.366  25.381  1.00 13.29           C  
-ATOM    953  C   TYR A 151     -13.661  12.183  26.036  1.00 11.49           C  
-ATOM    954  O   TYR A 151     -14.679  12.361  26.707  1.00 11.20           O  
-ATOM    955  CB  TYR A 151     -12.253  14.201  26.388  1.00 13.55           C  
-ATOM    956  CG  TYR A 151     -11.152  15.023  25.738  1.00 19.64           C  
-ATOM    957  CD1 TYR A 151     -11.450  16.183  25.028  1.00 21.68           C  
-ATOM    958  CD2 TYR A 151      -9.820  14.628  25.908  1.00 20.52           C  
-ATOM    959  CE1 TYR A 151     -10.421  16.956  24.493  1.00 21.15           C  
-ATOM    960  CE2 TYR A 151      -8.790  15.393  25.374  1.00 22.59           C  
-ATOM    961  CZ  TYR A 151      -9.105  16.555  24.672  1.00 23.04           C  
-ATOM    962  OH  TYR A 151      -8.094  17.375  24.209  1.00 27.44           O  
-ATOM    963  N   PRO A 152     -13.236  10.947  25.775  1.00 11.33           N  
-ATOM    964  CA  PRO A 152     -13.863   9.761  26.335  1.00 10.90           C  
-ATOM    965  C   PRO A 152     -13.382   9.533  27.758  1.00 11.79           C  
-ATOM    966  O   PRO A 152     -12.338  10.035  28.163  1.00 14.08           O  
-ATOM    967  CB  PRO A 152     -13.462   8.686  25.345  1.00 10.12           C  
-ATOM    968  CG  PRO A 152     -12.030   9.099  25.027  1.00 10.50           C  
-ATOM    969  CD  PRO A 152     -12.146  10.593  24.866  1.00  9.99           C  
-ATOM    970  N   ASP A 153     -14.125   8.782  28.536  1.00 11.86           N  
-ATOM    971  CA  ASP A 153     -13.631   8.431  29.844  1.00 11.48           C  
-ATOM    972  C   ASP A 153     -12.874   7.102  29.830  1.00  9.83           C  
-ATOM    973  O   ASP A 153     -12.027   6.853  30.698  1.00 11.08           O  
-ATOM    974  CB  ASP A 153     -14.851   8.417  30.801  1.00 15.54           C  
-ATOM    975  CG  ASP A 153     -15.549   9.786  30.880  1.00 24.46           C  
-ATOM    976  OD1 ASP A 153     -14.888  10.816  31.039  1.00 24.47           O  
-ATOM    977  OD2 ASP A 153     -16.778   9.850  30.734  1.00 30.73           O  
-ATOM    978  N   VAL A 154     -13.139   6.210  28.867  1.00  7.78           N  
-ATOM    979  CA  VAL A 154     -12.509   4.893  28.794  1.00  7.60           C  
-ATOM    980  C   VAL A 154     -11.488   4.863  27.657  1.00  7.97           C  
-ATOM    981  O   VAL A 154     -11.608   5.625  26.682  1.00  7.29           O  
-ATOM    982  CB  VAL A 154     -13.557   3.744  28.572  1.00 11.15           C  
-ATOM    983  CG1 VAL A 154     -14.552   3.756  29.721  1.00  8.98           C  
-ATOM    984  CG2 VAL A 154     -14.329   3.907  27.267  1.00  8.83           C  
-ATOM    985  N   LEU A 155     -10.516   3.968  27.745  1.00  5.57           N  
-ATOM    986  CA  LEU A 155      -9.409   3.916  26.802  1.00  6.43           C  
-ATOM    987  C   LEU A 155      -9.851   3.494  25.399  1.00  7.49           C  
-ATOM    988  O   LEU A 155     -10.638   2.548  25.232  1.00  9.94           O  
-ATOM    989  CB  LEU A 155      -8.371   2.961  27.400  1.00  5.82           C  
-ATOM    990  CG  LEU A 155      -7.020   2.857  26.704  1.00  6.43           C  
-ATOM    991  CD1 LEU A 155      -6.304   4.202  26.778  1.00  3.87           C  
-ATOM    992  CD2 LEU A 155      -6.194   1.762  27.365  1.00  6.64           C  
-ATOM    993  N   LYS A 156      -9.417   4.236  24.381  1.00  7.37           N  
-ATOM    994  CA  LYS A 156      -9.710   3.920  22.993  1.00  5.31           C  
-ATOM    995  C   LYS A 156      -8.459   3.355  22.338  1.00  6.07           C  
-ATOM    996  O   LYS A 156      -7.322   3.678  22.728  1.00  5.65           O  
-ATOM    997  CB  LYS A 156     -10.161   5.193  22.261  1.00  5.08           C  
-ATOM    998  CG  LYS A 156     -11.425   5.800  22.838  1.00  6.96           C  
-ATOM    999  CD  LYS A 156     -12.594   4.958  22.441  1.00 11.63           C  
-ATOM   1000  CE  LYS A 156     -13.824   5.387  23.186  1.00 15.96           C  
-ATOM   1001  NZ  LYS A 156     -14.918   4.552  22.727  1.00 16.73           N  
-ATOM   1002  N   CYS A 157      -8.648   2.532  21.311  1.00  5.73           N  
-ATOM   1003  CA  CYS A 157      -7.566   1.834  20.641  1.00  5.64           C  
-ATOM   1004  C   CYS A 157      -7.705   2.047  19.147  1.00  6.46           C  
-ATOM   1005  O   CYS A 157      -8.830   2.271  18.655  1.00  6.98           O  
-ATOM   1006  CB  CYS A 157      -7.633   0.326  20.904  1.00  7.11           C  
-ATOM   1007  SG  CYS A 157      -6.910  -0.221  22.465  1.00  5.63           S  
-ATOM   1008  N   LEU A 158      -6.599   1.952  18.396  1.00  5.30           N  
-ATOM   1009  CA  LEU A 158      -6.650   2.089  16.943  1.00  6.63           C  
-ATOM   1010  C   LEU A 158      -5.563   1.203  16.384  1.00  5.96           C  
-ATOM   1011  O   LEU A 158      -4.453   1.212  16.915  1.00  7.06           O  
-ATOM   1012  CB  LEU A 158      -6.348   3.532  16.475  1.00  7.79           C  
-ATOM   1013  CG  LEU A 158      -6.218   3.816  14.959  1.00  8.80           C  
-ATOM   1014  CD1 LEU A 158      -7.565   3.658  14.263  1.00 10.38           C  
-ATOM   1015  CD2 LEU A 158      -5.736   5.232  14.751  1.00 11.17           C  
-ATOM   1016  N   LYS A 159      -5.834   0.424  15.349  1.00  5.88           N  
-ATOM   1017  CA  LYS A 159      -4.809  -0.377  14.694  1.00  7.16           C  
-ATOM   1018  C   LYS A 159      -4.435   0.422  13.475  1.00  8.16           C  
-ATOM   1019  O   LYS A 159      -5.337   0.871  12.762  1.00  9.91           O  
-ATOM   1020  CB  LYS A 159      -5.354  -1.721  14.266  1.00  8.87           C  
-ATOM   1021  CG  LYS A 159      -5.685  -2.552  15.501  1.00 10.82           C  
-ATOM   1022  CD  LYS A 159      -6.142  -3.976  15.162  1.00 13.79           C  
-ATOM   1023  CE  LYS A 159      -6.316  -4.785  16.450  1.00 14.72           C  
-ATOM   1024  NZ  LYS A 159      -6.622  -6.180  16.166  1.00 17.13           N  
-ATOM   1025  N   ALA A 160      -3.163   0.642  13.197  1.00  8.76           N  
-ATOM   1026  CA  ALA A 160      -2.765   1.493  12.082  1.00  9.71           C  
-ATOM   1027  C   ALA A 160      -1.410   1.055  11.556  1.00  9.34           C  
-ATOM   1028  O   ALA A 160      -0.558   0.653  12.351  1.00  9.17           O  
-ATOM   1029  CB  ALA A 160      -2.630   2.943  12.519  1.00 10.65           C  
-ATOM   1030  N   PRO A 161      -1.146   1.105  10.251  1.00  8.74           N  
-ATOM   1031  CA  PRO A 161       0.142   0.758   9.685  1.00  7.75           C  
-ATOM   1032  C   PRO A 161       1.179   1.851   9.822  1.00  7.81           C  
-ATOM   1033  O   PRO A 161       0.850   3.041   9.790  1.00  7.66           O  
-ATOM   1034  CB  PRO A 161      -0.163   0.447   8.226  1.00  8.59           C  
-ATOM   1035  CG  PRO A 161      -1.284   1.456   7.914  1.00  9.22           C  
-ATOM   1036  CD  PRO A 161      -2.126   1.372   9.195  1.00  7.92           C  
-ATOM   1037  N   ILE A 162       2.454   1.491   9.926  1.00  9.46           N  
-ATOM   1038  CA  ILE A 162       3.522   2.478   9.780  1.00  8.41           C  
-ATOM   1039  C   ILE A 162       3.614   2.807   8.291  1.00 10.29           C  
-ATOM   1040  O   ILE A 162       3.593   1.911   7.431  1.00  8.64           O  
-ATOM   1041  CB  ILE A 162       4.852   1.909  10.290  1.00  8.68           C  
-ATOM   1042  CG1 ILE A 162       4.725   1.698  11.805  1.00  8.72           C  
-ATOM   1043  CG2 ILE A 162       6.009   2.860   9.958  1.00  5.78           C  
-ATOM   1044  CD1 ILE A 162       5.990   1.100  12.440  1.00 10.73           C  
-ATOM   1045  N   LEU A 163       3.709   4.080   7.950  1.00  9.27           N  
-ATOM   1046  CA  LEU A 163       3.785   4.527   6.582  1.00 10.98           C  
-ATOM   1047  C   LEU A 163       5.221   4.647   6.115  1.00 12.05           C  
-ATOM   1048  O   LEU A 163       6.153   4.706   6.939  1.00 11.85           O  
-ATOM   1049  CB  LEU A 163       3.047   5.857   6.510  1.00 12.70           C  
-ATOM   1050  CG  LEU A 163       1.563   5.891   6.094  1.00 17.26           C  
-ATOM   1051  CD1 LEU A 163       0.808   4.657   6.502  1.00 19.44           C  
-ATOM   1052  CD2 LEU A 163       0.947   7.108   6.738  1.00 17.05           C  
-ATOM   1053  N   SER A 164       5.443   4.651   4.793  1.00 11.74           N  
-ATOM   1054  CA  SER A 164       6.796   4.764   4.276  1.00 12.65           C  
-ATOM   1055  C   SER A 164       7.374   6.111   4.637  1.00 14.61           C  
-ATOM   1056  O   SER A 164       6.615   7.087   4.683  1.00 12.92           O  
-ATOM   1057  CB  SER A 164       6.840   4.643   2.747  1.00 13.93           C  
-ATOM   1058  OG  SER A 164       5.983   5.601   2.135  1.00 13.92           O  
-ATOM   1059  N   ASP A 165       8.688   6.240   4.824  1.00 16.04           N  
-ATOM   1060  CA  ASP A 165       9.203   7.548   5.167  1.00 21.36           C  
-ATOM   1061  C   ASP A 165       9.080   8.498   3.979  1.00 19.88           C  
-ATOM   1062  O   ASP A 165       9.019   9.709   4.196  1.00 19.11           O  
-ATOM   1063  CB  ASP A 165      10.658   7.418   5.669  1.00 26.72           C  
-ATOM   1064  CG  ASP A 165      10.756   6.742   7.060  1.00 34.41           C  
-ATOM   1065  OD1 ASP A 165      10.289   7.261   8.102  1.00 37.44           O  
-ATOM   1066  OD2 ASP A 165      11.333   5.651   7.119  1.00 37.97           O  
-ATOM   1067  N   SER A 166       8.909   8.059   2.721  1.00 19.42           N  
-ATOM   1068  CA  SER A 166       8.725   9.009   1.641  1.00 19.93           C  
-ATOM   1069  C   SER A 166       7.295   9.517   1.663  1.00 19.30           C  
-ATOM   1070  O   SER A 166       7.097  10.707   1.398  1.00 19.61           O  
-ATOM   1071  CB  SER A 166       9.021   8.370   0.294  1.00 23.01           C  
-ATOM   1072  OG  SER A 166       8.220   7.226   0.050  1.00 28.86           O  
-ATOM   1073  N   SER A 167       6.276   8.718   2.008  1.00 16.30           N  
-ATOM   1074  CA  SER A 167       4.956   9.302   2.077  1.00 17.19           C  
-ATOM   1075  C   SER A 167       4.855  10.204   3.307  1.00 15.70           C  
-ATOM   1076  O   SER A 167       4.209  11.253   3.239  1.00 15.00           O  
-ATOM   1077  CB  SER A 167       3.882   8.202   2.092  1.00 18.71           C  
-ATOM   1078  OG  SER A 167       3.951   7.224   3.117  1.00 27.89           O  
-ATOM   1079  N   CYS A 168       5.560   9.893   4.407  1.00 15.67           N  
-ATOM   1080  CA  CYS A 168       5.594  10.728   5.613  1.00 13.58           C  
-ATOM   1081  C   CYS A 168       6.190  12.113   5.289  1.00 15.32           C  
-ATOM   1082  O   CYS A 168       5.614  13.182   5.571  1.00 15.73           O  
-ATOM   1083  CB  CYS A 168       6.423   9.983   6.656  1.00 11.04           C  
-ATOM   1084  SG  CYS A 168       6.383  10.758   8.284  1.00 10.70           S  
-ATOM   1085  N   LYS A 169       7.323  12.112   4.585  1.00 14.50           N  
-ATOM   1086  CA  LYS A 169       7.979  13.330   4.157  1.00 16.48           C  
-ATOM   1087  C   LYS A 169       7.205  14.096   3.098  1.00 17.69           C  
-ATOM   1088  O   LYS A 169       7.303  15.328   3.102  1.00 22.03           O  
-ATOM   1089  CB  LYS A 169       9.361  12.994   3.640  1.00 18.45           C  
-ATOM   1090  CG  LYS A 169      10.340  12.833   4.772  1.00 21.37           C  
-ATOM   1091  CD  LYS A 169      11.719  12.612   4.190  1.00 28.10           C  
-ATOM   1092  CE  LYS A 169      12.810  13.134   5.130  1.00 32.84           C  
-ATOM   1093  NZ  LYS A 169      12.853  12.465   6.423  1.00 36.64           N  
-ATOM   1094  N   SER A 170       6.439  13.473   2.210  1.00 16.81           N  
-ATOM   1095  CA  SER A 170       5.573  14.195   1.283  1.00 18.05           C  
-ATOM   1096  C   SER A 170       4.417  14.852   2.010  1.00 17.80           C  
-ATOM   1097  O   SER A 170       3.991  15.943   1.632  1.00 18.42           O  
-ATOM   1098  CB  SER A 170       4.984  13.267   0.263  1.00 20.62           C  
-ATOM   1099  OG  SER A 170       6.057  12.624  -0.401  1.00 29.86           O  
-ATOM   1100  N   ALA A 171       3.889  14.219   3.070  1.00 15.68           N  
-ATOM   1101  CA  ALA A 171       2.814  14.812   3.847  1.00 14.21           C  
-ATOM   1102  C   ALA A 171       3.302  16.021   4.632  1.00 12.58           C  
-ATOM   1103  O   ALA A 171       2.560  16.992   4.834  1.00 15.82           O  
-ATOM   1104  CB  ALA A 171       2.257  13.803   4.841  1.00 13.32           C  
-ATOM   1105  N   TYR A 172       4.539  16.002   5.126  1.00 12.63           N  
-ATOM   1106  CA  TYR A 172       5.094  17.058   5.975  1.00 11.54           C  
-ATOM   1107  C   TYR A 172       6.476  17.486   5.485  1.00 12.60           C  
-ATOM   1108  O   TYR A 172       7.502  17.233   6.160  1.00 11.84           O  
-ATOM   1109  CB  TYR A 172       5.203  16.552   7.427  1.00 11.38           C  
-ATOM   1110  CG  TYR A 172       3.873  16.223   8.097  1.00 12.54           C  
-ATOM   1111  CD1 TYR A 172       3.051  17.267   8.518  1.00 11.61           C  
-ATOM   1112  CD2 TYR A 172       3.493  14.896   8.318  1.00 10.94           C  
-ATOM   1113  CE1 TYR A 172       1.850  16.996   9.161  1.00 11.27           C  
-ATOM   1114  CE2 TYR A 172       2.282  14.619   8.965  1.00 10.53           C  
-ATOM   1115  CZ  TYR A 172       1.465  15.677   9.387  1.00 13.16           C  
-ATOM   1116  OH  TYR A 172       0.275  15.452  10.062  1.00 11.54           O  
-ATOM   1117  N   PRO A 173       6.583  18.113   4.304  1.00 12.66           N  
-ATOM   1118  CA  PRO A 173       7.845  18.563   3.721  1.00 13.40           C  
-ATOM   1119  C   PRO A 173       8.682  19.345   4.722  1.00 12.47           C  
-ATOM   1120  O   PRO A 173       8.163  20.176   5.452  1.00 13.98           O  
-ATOM   1121  CB  PRO A 173       7.470  19.428   2.544  1.00 14.29           C  
-ATOM   1122  CG  PRO A 173       6.095  18.944   2.186  1.00 14.17           C  
-ATOM   1123  CD  PRO A 173       5.465  18.649   3.530  1.00 14.30           C  
-ATOM   1124  N   GLY A 174       9.943  18.968   4.867  1.00 10.85           N  
-ATOM   1125  CA  GLY A 174      10.869  19.754   5.650  1.00 13.39           C  
-ATOM   1126  C   GLY A 174      10.717  19.621   7.148  1.00 14.39           C  
-ATOM   1127  O   GLY A 174      11.437  20.326   7.864  1.00 16.79           O  
-ATOM   1128  N   GLN A 175       9.837  18.731   7.634  1.00 12.25           N  
-ATOM   1129  CA  GLN A 175       9.558  18.585   9.051  1.00 11.35           C  
-ATOM   1130  C   GLN A 175       9.879  17.221   9.634  1.00 11.26           C  
-ATOM   1131  O   GLN A 175       9.899  17.051  10.854  1.00 11.65           O  
-ATOM   1132  CB  GLN A 175       8.105  18.864   9.282  1.00 11.32           C  
-ATOM   1133  CG  GLN A 175       7.733  20.304   8.970  1.00 14.13           C  
-ATOM   1134  CD  GLN A 175       6.255  20.411   8.735  1.00 16.78           C  
-ATOM   1135  OE1 GLN A 175       5.728  20.280   7.621  1.00 23.31           O  
-ATOM   1136  NE2 GLN A 175       5.552  20.580   9.831  1.00 14.39           N  
-ATOM   1137  N   ILE A 176      10.091  16.180   8.836  1.00 10.68           N  
-ATOM   1138  CA  ILE A 176      10.329  14.849   9.395  1.00 10.85           C  
-ATOM   1139  C   ILE A 176      11.826  14.578   9.546  1.00 12.80           C  
-ATOM   1140  O   ILE A 176      12.565  14.501   8.536  1.00 13.79           O  
-ATOM   1141  CB  ILE A 176       9.671  13.795   8.470  1.00  8.93           C  
-ATOM   1142  CG1 ILE A 176       8.174  14.099   8.297  1.00  9.15           C  
-ATOM   1143  CG2 ILE A 176       9.894  12.406   9.058  1.00  6.18           C  
-ATOM   1144  CD1 ILE A 176       7.293  14.076   9.587  1.00  8.72           C  
-ATOM   1145  N   THR A 177      12.279  14.347  10.779  1.00 10.08           N  
-ATOM   1146  CA  THR A 177      13.674  14.040  11.022  1.00  8.30           C  
-ATOM   1147  C   THR A 177      13.844  12.514  11.084  1.00  8.13           C  
-ATOM   1148  O   THR A 177      12.879  11.734  11.030  1.00  8.38           O  
-ATOM   1149  CB  THR A 177      14.150  14.688  12.360  1.00  9.16           C  
-ATOM   1150  OG1 THR A 177      13.475  13.992  13.415  1.00  8.04           O  
-ATOM   1151  CG2 THR A 177      13.872  16.184  12.448  1.00  7.26           C  
-ATOM   1152  N   SER A 178      15.043  12.005  11.268  1.00  6.35           N  
-ATOM   1153  CA  SER A 178      15.239  10.580  11.357  1.00  7.10           C  
-ATOM   1154  C   SER A 178      14.703   9.994  12.643  1.00  7.13           C  
-ATOM   1155  O   SER A 178      14.674   8.769  12.797  1.00 11.58           O  
-ATOM   1156  CB  SER A 178      16.723  10.280  11.236  1.00 11.34           C  
-ATOM   1157  OG  SER A 178      17.396  11.100  12.175  1.00 17.56           O  
-ATOM   1158  N   ASN A 179      14.262  10.802  13.606  1.00  6.39           N  
-ATOM   1159  CA  ASN A 179      13.742  10.290  14.861  1.00  5.71           C  
-ATOM   1160  C   ASN A 179      12.220  10.293  14.858  1.00  6.18           C  
-ATOM   1161  O   ASN A 179      11.577  10.200  15.916  1.00  5.84           O  
-ATOM   1162  CB  ASN A 179      14.240  11.148  15.961  1.00  4.73           C  
-ATOM   1163  CG  ASN A 179      15.748  11.140  15.988  1.00  7.58           C  
-ATOM   1164  OD1 ASN A 179      16.384  10.089  16.050  1.00 10.26           O  
-ATOM   1165  ND2 ASN A 179      16.374  12.302  15.938  1.00  8.59           N  
-ATOM   1166  N   MET A 180      11.599  10.366  13.675  1.00  5.03           N  
-ATOM   1167  CA  MET A 180      10.154  10.407  13.611  1.00  5.91           C  
-ATOM   1168  C   MET A 180       9.689   9.418  12.572  1.00  6.24           C  
-ATOM   1169  O   MET A 180      10.475   9.108  11.662  1.00  5.88           O  
-ATOM   1170  CB  MET A 180       9.659  11.767  13.175  1.00  3.48           C  
-ATOM   1171  CG  MET A 180      10.002  12.910  14.092  1.00  7.93           C  
-ATOM   1172  SD  MET A 180       9.610  14.491  13.306  1.00  9.64           S  
-ATOM   1173  CE  MET A 180      10.365  15.538  14.523  1.00 11.62           C  
-ATOM   1174  N   PHE A 181       8.474   8.882  12.696  1.00  5.19           N  
-ATOM   1175  CA  PHE A 181       7.865   8.123  11.589  1.00  6.70           C  
-ATOM   1176  C   PHE A 181       6.383   8.472  11.558  1.00  6.14           C  
-ATOM   1177  O   PHE A 181       5.834   8.983  12.547  1.00  7.66           O  
-ATOM   1178  CB  PHE A 181       7.999   6.566  11.744  1.00  7.10           C  
-ATOM   1179  CG  PHE A 181       7.322   5.873  12.941  1.00  7.38           C  
-ATOM   1180  CD1 PHE A 181       6.005   5.423  12.856  1.00  6.48           C  
-ATOM   1181  CD2 PHE A 181       8.033   5.701  14.125  1.00  8.75           C  
-ATOM   1182  CE1 PHE A 181       5.395   4.810  13.948  1.00  4.66           C  
-ATOM   1183  CE2 PHE A 181       7.424   5.087  15.222  1.00  9.10           C  
-ATOM   1184  CZ  PHE A 181       6.103   4.641  15.138  1.00  5.29           C  
-ATOM   1185  N   CYS A 182       5.710   8.198  10.445  1.00  7.50           N  
-ATOM   1186  CA  CYS A 182       4.295   8.456  10.336  1.00  4.86           C  
-ATOM   1187  C   CYS A 182       3.571   7.131  10.414  1.00  6.33           C  
-ATOM   1188  O   CYS A 182       4.073   6.092   9.967  1.00  5.70           O  
-ATOM   1189  CB  CYS A 182       3.933   9.095   9.007  1.00  5.73           C  
-ATOM   1190  SG  CYS A 182       4.438  10.825   8.821  1.00  8.47           S  
-ATOM   1191  N   ALA A 183       2.395   7.137  11.012  1.00  5.12           N  
-ATOM   1192  CA  ALA A 183       1.545   5.963  11.007  1.00  7.67           C  
-ATOM   1193  C   ALA A 183       0.130   6.481  10.884  1.00  7.25           C  
-ATOM   1194  O   ALA A 183      -0.212   7.596  11.315  1.00 11.02           O  
-ATOM   1195  CB  ALA A 183       1.668   5.141  12.304  1.00  3.49           C  
-ATOM   1196  N   GLY A 184A     -0.677   5.723  10.169  1.00  9.20           N  
-ATOM   1197  CA  GLY A 184A     -2.033   6.147   9.986  1.00  8.86           C  
-ATOM   1198  C   GLY A 184A     -2.519   5.861   8.579  1.00 10.79           C  
-ATOM   1199  O   GLY A 184A     -2.079   4.912   7.925  1.00  9.03           O  
-ATOM   1200  N   TYR A 184      -3.473   6.674   8.152  1.00 10.49           N  
-ATOM   1201  CA  TYR A 184      -4.187   6.461   6.898  1.00 12.40           C  
-ATOM   1202  C   TYR A 184      -4.152   7.780   6.159  1.00 12.69           C  
-ATOM   1203  O   TYR A 184      -4.692   8.765   6.653  1.00 13.67           O  
-ATOM   1204  CB  TYR A 184      -5.639   6.073   7.188  1.00 11.04           C  
-ATOM   1205  CG  TYR A 184      -5.742   4.775   7.958  1.00 11.61           C  
-ATOM   1206  CD1 TYR A 184      -5.707   4.777   9.350  1.00  9.03           C  
-ATOM   1207  CD2 TYR A 184      -5.803   3.575   7.251  1.00 11.75           C  
-ATOM   1208  CE1 TYR A 184      -5.713   3.564  10.042  1.00 12.63           C  
-ATOM   1209  CE2 TYR A 184      -5.825   2.363   7.942  1.00 14.20           C  
-ATOM   1210  CZ  TYR A 184      -5.774   2.363   9.333  1.00 12.51           C  
-ATOM   1211  OH  TYR A 184      -5.786   1.141   9.989  1.00 14.85           O  
-ATOM   1212  N   LEU A 185      -3.598   7.859   4.957  1.00 13.46           N  
-ATOM   1213  CA  LEU A 185      -3.562   9.121   4.231  1.00 15.23           C  
-ATOM   1214  C   LEU A 185      -4.940   9.603   3.811  1.00 16.75           C  
-ATOM   1215  O   LEU A 185      -5.122  10.794   3.544  1.00 17.99           O  
-ATOM   1216  CB  LEU A 185      -2.673   8.991   3.001  1.00 15.01           C  
-ATOM   1217  CG  LEU A 185      -1.219   8.685   3.278  1.00 16.60           C  
-ATOM   1218  CD1 LEU A 185      -0.432   8.741   2.009  1.00 16.37           C  
-ATOM   1219  CD2 LEU A 185      -0.623   9.748   4.187  1.00 18.84           C  
-ATOM   1220  N   GLU A 186      -5.962   8.755   3.770  1.00 18.63           N  
-ATOM   1221  CA  GLU A 186      -7.288   9.271   3.500  1.00 22.34           C  
-ATOM   1222  C   GLU A 186      -7.950   9.863   4.727  1.00 22.10           C  
-ATOM   1223  O   GLU A 186      -9.028  10.435   4.603  1.00 25.42           O  
-ATOM   1224  CB  GLU A 186      -8.146   8.176   2.907  1.00 26.56           C  
-ATOM   1225  CG  GLU A 186      -7.569   7.742   1.532  1.00 37.78           C  
-ATOM   1226  CD  GLU A 186      -7.152   8.856   0.553  1.00 41.87           C  
-ATOM   1227  OE1 GLU A 186      -8.004   9.539  -0.020  1.00 44.68           O  
-ATOM   1228  OE2 GLU A 186      -5.955   9.121   0.380  1.00 42.62           O  
-ATOM   1229  N   GLY A 187      -7.326   9.845   5.909  1.00 20.41           N  
-ATOM   1230  CA  GLY A 187      -7.890  10.494   7.078  1.00 17.48           C  
-ATOM   1231  C   GLY A 187      -8.918   9.604   7.751  1.00 16.56           C  
-ATOM   1232  O   GLY A 187      -8.989   8.405   7.484  1.00 16.51           O  
-ATOM   1233  N   GLY A 188A     -9.686  10.125   8.696  1.00 13.41           N  
-ATOM   1234  CA  GLY A 188A    -10.730   9.342   9.308  1.00 11.67           C  
-ATOM   1235  C   GLY A 188A    -10.300   8.636  10.565  1.00 12.37           C  
-ATOM   1236  O   GLY A 188A    -11.112   8.520  11.469  1.00 13.52           O  
-ATOM   1237  N   LYS A 188      -9.052   8.209  10.689  1.00 12.39           N  
-ATOM   1238  CA  LYS A 188      -8.601   7.430  11.832  1.00 12.09           C  
-ATOM   1239  C   LYS A 188      -7.225   7.949  12.238  1.00 11.12           C  
-ATOM   1240  O   LYS A 188      -6.336   8.012  11.378  1.00  9.76           O  
-ATOM   1241  CB  LYS A 188      -8.494   5.964  11.440  1.00 14.45           C  
-ATOM   1242  CG  LYS A 188      -9.792   5.280  11.045  1.00 17.70           C  
-ATOM   1243  CD  LYS A 188      -9.482   3.814  10.991  1.00 22.32           C  
-ATOM   1244  CE  LYS A 188     -10.752   3.007  10.898  1.00 28.23           C  
-ATOM   1245  NZ  LYS A 188     -10.576   1.803  11.691  1.00 34.46           N  
-ATOM   1246  N   ASP A 189      -6.984   8.276  13.517  1.00  8.08           N  
-ATOM   1247  CA  ASP A 189      -5.737   8.904  13.915  1.00  6.61           C  
-ATOM   1248  C   ASP A 189      -5.674   9.023  15.425  1.00  6.88           C  
-ATOM   1249  O   ASP A 189      -6.694   8.837  16.100  1.00  9.66           O  
-ATOM   1250  CB  ASP A 189      -5.653  10.314  13.311  1.00  5.61           C  
-ATOM   1251  CG  ASP A 189      -4.304  10.993  13.307  1.00  7.18           C  
-ATOM   1252  OD1 ASP A 189      -3.298  10.459  13.760  1.00  7.08           O  
-ATOM   1253  OD2 ASP A 189      -4.232  12.112  12.829  1.00  7.86           O  
-ATOM   1254  N   SER A 190      -4.519   9.314  16.006  1.00  4.50           N  
-ATOM   1255  CA  SER A 190      -4.504   9.685  17.411  1.00  4.83           C  
-ATOM   1256  C   SER A 190      -4.824  11.196  17.442  1.00  5.48           C  
-ATOM   1257  O   SER A 190      -4.990  11.815  16.371  1.00  7.66           O  
-ATOM   1258  CB  SER A 190      -3.120   9.398  18.014  1.00  4.90           C  
-ATOM   1259  OG  SER A 190      -2.075   9.962  17.217  1.00  7.33           O  
-ATOM   1260  N   CYS A 191      -4.892  11.875  18.583  1.00  5.55           N  
-ATOM   1261  CA  CYS A 191      -5.268  13.284  18.609  1.00  7.20           C  
-ATOM   1262  C   CYS A 191      -4.794  13.914  19.909  1.00  6.83           C  
-ATOM   1263  O   CYS A 191      -4.100  13.277  20.699  1.00  7.03           O  
-ATOM   1264  CB  CYS A 191      -6.769  13.385  18.476  1.00  7.89           C  
-ATOM   1265  SG  CYS A 191      -7.441  14.997  17.981  1.00 10.19           S  
-ATOM   1266  N   GLN A 192      -5.114  15.182  20.176  1.00  7.87           N  
-ATOM   1267  CA  GLN A 192      -4.718  15.851  21.397  1.00  9.18           C  
-ATOM   1268  C   GLN A 192      -5.182  15.074  22.635  1.00  8.91           C  
-ATOM   1269  O   GLN A 192      -6.321  14.575  22.703  1.00 11.13           O  
-ATOM   1270  CB  GLN A 192      -5.300  17.268  21.391  1.00 13.40           C  
-ATOM   1271  CG  GLN A 192      -4.566  18.210  20.414  1.00 21.29           C  
-ATOM   1272  CD  GLN A 192      -4.943  18.154  18.931  1.00 24.75           C  
-ATOM   1273  OE1 GLN A 192      -4.116  18.326  18.029  1.00 29.75           O  
-ATOM   1274  NE2 GLN A 192      -6.188  17.968  18.540  1.00 25.22           N  
-ATOM   1275  N   GLY A 193      -4.328  14.948  23.648  1.00  8.20           N  
-ATOM   1276  CA  GLY A 193      -4.661  14.167  24.819  1.00  4.67           C  
-ATOM   1277  C   GLY A 193      -4.184  12.738  24.695  1.00  6.59           C  
-ATOM   1278  O   GLY A 193      -4.203  11.989  25.691  1.00  7.85           O  
-ATOM   1279  N   ASP A 194      -3.823  12.304  23.481  1.00  5.23           N  
-ATOM   1280  CA  ASP A 194      -3.234  10.988  23.265  1.00  3.10           C  
-ATOM   1281  C   ASP A 194      -1.732  11.105  23.386  1.00  2.84           C  
-ATOM   1282  O   ASP A 194      -1.051  10.099  23.553  1.00  2.14           O  
-ATOM   1283  CB  ASP A 194      -3.535  10.454  21.885  1.00  3.63           C  
-ATOM   1284  CG  ASP A 194      -4.985  10.037  21.744  1.00  6.12           C  
-ATOM   1285  OD1 ASP A 194      -5.547   9.463  22.672  1.00  6.74           O  
-ATOM   1286  OD2 ASP A 194      -5.588  10.260  20.698  1.00  2.33           O  
-ATOM   1287  N   SER A 195      -1.177  12.331  23.325  1.00  3.90           N  
-ATOM   1288  CA  SER A 195       0.256  12.620  23.427  1.00  4.95           C  
-ATOM   1289  C   SER A 195       0.993  11.851  24.498  1.00  3.86           C  
-ATOM   1290  O   SER A 195       0.489  11.709  25.609  1.00  5.84           O  
-ATOM   1291  CB  SER A 195       0.464  14.093  23.699  1.00  6.06           C  
-ATOM   1292  OG  SER A 195       0.354  14.753  22.448  1.00 10.88           O  
-ATOM   1293  N   GLY A 196       2.156  11.327  24.148  1.00  2.00           N  
-ATOM   1294  CA  GLY A 196       2.966  10.579  25.100  1.00  2.00           C  
-ATOM   1295  C   GLY A 196       2.595   9.118  25.147  1.00  2.00           C  
-ATOM   1296  O   GLY A 196       3.365   8.312  25.666  1.00  5.22           O  
-ATOM   1297  N   GLY A 197       1.484   8.693  24.557  1.00  2.72           N  
-ATOM   1298  CA  GLY A 197       1.069   7.304  24.636  1.00  3.81           C  
-ATOM   1299  C   GLY A 197       1.814   6.367  23.686  1.00  4.30           C  
-ATOM   1300  O   GLY A 197       2.602   6.800  22.836  1.00  6.39           O  
-ATOM   1301  N   PRO A 198       1.599   5.062  23.817  1.00  5.07           N  
-ATOM   1302  CA  PRO A 198       2.255   3.993  23.047  1.00  4.90           C  
-ATOM   1303  C   PRO A 198       1.797   3.728  21.614  1.00  7.19           C  
-ATOM   1304  O   PRO A 198       0.625   3.895  21.278  1.00  7.14           O  
-ATOM   1305  CB  PRO A 198       2.055   2.772  23.918  1.00  2.90           C  
-ATOM   1306  CG  PRO A 198       0.702   2.981  24.548  1.00  6.05           C  
-ATOM   1307  CD  PRO A 198       0.623   4.506  24.749  1.00  4.22           C  
-ATOM   1308  N   VAL A 199       2.738   3.294  20.770  1.00  5.28           N  
-ATOM   1309  CA  VAL A 199       2.458   2.721  19.460  1.00  5.42           C  
-ATOM   1310  C   VAL A 199       3.212   1.393  19.599  1.00  7.62           C  
-ATOM   1311  O   VAL A 199       4.443   1.395  19.718  1.00  6.95           O  
-ATOM   1312  CB  VAL A 199       3.078   3.525  18.290  1.00  7.81           C  
-ATOM   1313  CG1 VAL A 199       2.714   2.839  16.978  1.00  7.41           C  
-ATOM   1314  CG2 VAL A 199       2.544   4.936  18.273  1.00  5.50           C  
-ATOM   1315  N   VAL A 200       2.519   0.254  19.635  1.00  7.65           N  
-ATOM   1316  CA  VAL A 200       3.115  -1.052  19.886  1.00  7.25           C  
-ATOM   1317  C   VAL A 200       2.951  -1.865  18.615  1.00  6.94           C  
-ATOM   1318  O   VAL A 200       1.843  -1.932  18.084  1.00  5.69           O  
-ATOM   1319  CB  VAL A 200       2.381  -1.722  21.113  1.00  6.27           C  
-ATOM   1320  CG1 VAL A 200       2.752  -3.190  21.297  1.00  9.55           C  
-ATOM   1321  CG2 VAL A 200       2.859  -1.039  22.396  1.00  6.88           C  
-ATOM   1322  N   CYS A 201       4.025  -2.493  18.152  1.00  7.14           N  
-ATOM   1323  CA  CYS A 201       4.020  -3.285  16.920  1.00 10.47           C  
-ATOM   1324  C   CYS A 201       4.760  -4.556  17.275  1.00 11.54           C  
-ATOM   1325  O   CYS A 201       5.849  -4.487  17.857  1.00 10.76           O  
-ATOM   1326  CB  CYS A 201       4.773  -2.563  15.793  1.00  9.46           C  
-ATOM   1327  SG  CYS A 201       4.491  -0.760  15.734  1.00  8.79           S  
-ATOM   1328  N   SER A 202       4.151  -5.714  17.054  1.00 12.14           N  
-ATOM   1329  CA  SER A 202       4.746  -7.006  17.377  1.00 15.11           C  
-ATOM   1330  C   SER A 202       5.177  -7.098  18.847  1.00 16.34           C  
-ATOM   1331  O   SER A 202       6.226  -7.644  19.198  1.00 18.03           O  
-ATOM   1332  CB  SER A 202       5.933  -7.244  16.438  1.00 14.87           C  
-ATOM   1333  OG  SER A 202       5.468  -7.129  15.094  1.00 16.83           O  
-ATOM   1334  N   GLY A 203       4.362  -6.527  19.741  1.00 15.28           N  
-ATOM   1335  CA  GLY A 203       4.594  -6.662  21.163  1.00 14.57           C  
-ATOM   1336  C   GLY A 203       5.743  -5.808  21.655  1.00 13.69           C  
-ATOM   1337  O   GLY A 203       6.164  -5.992  22.800  1.00 15.44           O  
-ATOM   1338  N   LYS A 204       6.278  -4.871  20.867  1.00 10.60           N  
-ATOM   1339  CA  LYS A 204       7.375  -4.023  21.335  1.00 11.72           C  
-ATOM   1340  C   LYS A 204       6.951  -2.552  21.200  1.00 10.53           C  
-ATOM   1341  O   LYS A 204       6.163  -2.193  20.296  1.00  8.61           O  
-ATOM   1342  CB  LYS A 204       8.650  -4.250  20.493  1.00 12.09           C  
-ATOM   1343  CG  LYS A 204       9.145  -5.726  20.456  1.00 16.97           C  
-ATOM   1344  CD  LYS A 204       9.573  -6.294  21.824  1.00 17.70           C  
-ATOM   1345  CE  LYS A 204       9.743  -7.842  21.859  1.00 22.56           C  
-ATOM   1346  NZ  LYS A 204      11.006  -8.318  21.309  1.00 21.99           N  
-ATOM   1347  N   LEU A 209       7.426  -1.691  22.100  1.00  6.90           N  
-ATOM   1348  CA  LEU A 209       7.115  -0.265  22.001  1.00  4.98           C  
-ATOM   1349  C   LEU A 209       7.910   0.333  20.846  1.00  5.26           C  
-ATOM   1350  O   LEU A 209       9.143   0.373  20.911  1.00  6.83           O  
-ATOM   1351  CB  LEU A 209       7.481   0.439  23.306  1.00  5.40           C  
-ATOM   1352  CG  LEU A 209       7.207   1.942  23.340  1.00  4.20           C  
-ATOM   1353  CD1 LEU A 209       5.702   2.198  23.255  1.00  2.18           C  
-ATOM   1354  CD2 LEU A 209       7.825   2.510  24.594  1.00  5.78           C  
-ATOM   1355  N   GLN A 210       7.270   0.754  19.754  1.00  4.04           N  
-ATOM   1356  CA  GLN A 210       7.970   1.354  18.627  1.00  5.51           C  
-ATOM   1357  C   GLN A 210       7.813   2.865  18.509  1.00  4.36           C  
-ATOM   1358  O   GLN A 210       8.661   3.547  17.891  1.00  4.51           O  
-ATOM   1359  CB  GLN A 210       7.497   0.748  17.290  1.00  5.80           C  
-ATOM   1360  CG  GLN A 210       7.990  -0.685  17.099  1.00  5.36           C  
-ATOM   1361  CD  GLN A 210       9.485  -0.881  16.820  1.00 11.81           C  
-ATOM   1362  OE1 GLN A 210       9.984  -2.014  16.813  1.00 10.12           O  
-ATOM   1363  NE2 GLN A 210      10.336   0.091  16.551  1.00 11.39           N  
-ATOM   1364  N   GLY A 211       6.759   3.436  19.083  1.00  4.05           N  
-ATOM   1365  CA  GLY A 211       6.538   4.871  18.922  1.00  3.31           C  
-ATOM   1366  C   GLY A 211       5.865   5.479  20.136  1.00  4.46           C  
-ATOM   1367  O   GLY A 211       5.299   4.766  20.982  1.00  4.49           O  
-ATOM   1368  N   ILE A 212       5.915   6.813  20.165  1.00  3.87           N  
-ATOM   1369  CA  ILE A 212       5.293   7.628  21.204  1.00  4.45           C  
-ATOM   1370  C   ILE A 212       4.468   8.638  20.438  1.00  3.11           C  
-ATOM   1371  O   ILE A 212       4.970   9.260  19.503  1.00  2.31           O  
-ATOM   1372  CB  ILE A 212       6.358   8.377  22.054  1.00  8.21           C  
-ATOM   1373  CG1 ILE A 212       7.220   7.320  22.723  1.00  8.45           C  
-ATOM   1374  CG2 ILE A 212       5.739   9.295  23.106  1.00  4.80           C  
-ATOM   1375  CD1 ILE A 212       8.409   7.943  23.433  1.00 13.68           C  
-ATOM   1376  N   VAL A 213       3.195   8.814  20.783  1.00  4.44           N  
-ATOM   1377  CA  VAL A 213       2.330   9.791  20.125  1.00  3.32           C  
-ATOM   1378  C   VAL A 213       2.989  11.164  20.300  1.00  3.59           C  
-ATOM   1379  O   VAL A 213       3.193  11.579  21.446  1.00  4.65           O  
-ATOM   1380  CB  VAL A 213       0.930   9.755  20.784  1.00  2.38           C  
-ATOM   1381  CG1 VAL A 213       0.070  10.820  20.126  1.00  2.22           C  
-ATOM   1382  CG2 VAL A 213       0.297   8.353  20.662  1.00  2.00           C  
-ATOM   1383  N   SER A 214       3.305  11.858  19.208  1.00  3.45           N  
-ATOM   1384  CA  SER A 214       4.029  13.096  19.297  1.00  4.25           C  
-ATOM   1385  C   SER A 214       3.295  14.255  18.640  1.00  5.56           C  
-ATOM   1386  O   SER A 214       2.896  15.156  19.373  1.00  9.42           O  
-ATOM   1387  CB  SER A 214       5.399  12.863  18.678  1.00  6.62           C  
-ATOM   1388  OG  SER A 214       6.213  14.030  18.628  1.00 10.73           O  
-ATOM   1389  N   TRP A 215       3.058  14.333  17.327  1.00  4.82           N  
-ATOM   1390  CA  TRP A 215       2.390  15.485  16.774  1.00  5.22           C  
-ATOM   1391  C   TRP A 215       1.674  15.153  15.463  1.00  7.06           C  
-ATOM   1392  O   TRP A 215       1.581  13.988  15.074  1.00  5.16           O  
-ATOM   1393  CB  TRP A 215       3.416  16.603  16.550  1.00  6.04           C  
-ATOM   1394  CG  TRP A 215       4.529  16.344  15.526  1.00  4.26           C  
-ATOM   1395  CD1 TRP A 215       5.679  15.694  15.859  1.00  4.80           C  
-ATOM   1396  CD2 TRP A 215       4.555  16.816  14.231  1.00  7.71           C  
-ATOM   1397  NE1 TRP A 215       6.444  15.767  14.790  1.00  5.44           N  
-ATOM   1398  CE2 TRP A 215       5.821  16.423  13.804  1.00  6.71           C  
-ATOM   1399  CE3 TRP A 215       3.690  17.522  13.376  1.00  8.54           C  
-ATOM   1400  CZ2 TRP A 215       6.260  16.720  12.519  1.00  9.74           C  
-ATOM   1401  CZ3 TRP A 215       4.125  17.820  12.088  1.00 10.31           C  
-ATOM   1402  CH2 TRP A 215       5.402  17.425  11.661  1.00  7.56           C  
-ATOM   1403  N   GLY A 216       1.093  16.157  14.788  1.00  8.49           N  
-ATOM   1404  CA  GLY A 216       0.381  15.987  13.518  1.00  9.93           C  
-ATOM   1405  C   GLY A 216      -0.362  17.288  13.210  1.00 11.95           C  
-ATOM   1406  O   GLY A 216      -0.436  18.134  14.121  1.00 11.17           O  
-ATOM   1407  N   SER A 217      -0.908  17.543  12.024  1.00  9.43           N  
-ATOM   1408  CA  SER A 217      -1.638  18.788  11.813  1.00 10.62           C  
-ATOM   1409  C   SER A 217      -3.107  18.474  12.024  1.00  9.24           C  
-ATOM   1410  O   SER A 217      -3.649  17.719  11.212  1.00 10.17           O  
-ATOM   1411  CB  SER A 217      -1.446  19.304  10.389  1.00 11.65           C  
-ATOM   1412  OG  SER A 217      -0.056  19.390  10.106  1.00 23.47           O  
-ATOM   1413  N   GLY A 219      -3.806  18.969  13.043  1.00  8.81           N  
-ATOM   1414  CA  GLY A 219      -5.189  18.558  13.241  1.00 10.63           C  
-ATOM   1415  C   GLY A 219      -5.198  17.059  13.552  1.00 10.90           C  
-ATOM   1416  O   GLY A 219      -4.146  16.476  13.884  1.00 12.88           O  
-ATOM   1417  N   CYS A 220      -6.348  16.415  13.421  1.00  9.60           N  
-ATOM   1418  CA  CYS A 220      -6.439  14.996  13.690  1.00  7.09           C  
-ATOM   1419  C   CYS A 220      -7.280  14.406  12.595  1.00  9.06           C  
-ATOM   1420  O   CYS A 220      -8.324  14.971  12.254  1.00  9.41           O  
-ATOM   1421  CB  CYS A 220      -7.135  14.716  15.013  1.00  9.94           C  
-ATOM   1422  SG  CYS A 220      -6.313  15.525  16.417  1.00 10.79           S  
-ATOM   1423  N   ALA A 221A     -6.854  13.248  12.088  1.00  9.64           N  
-ATOM   1424  CA  ALA A 221A     -7.585  12.452  11.129  1.00  9.86           C  
-ATOM   1425  C   ALA A 221A     -7.909  13.179   9.826  1.00 13.81           C  
-ATOM   1426  O   ALA A 221A     -8.833  12.778   9.110  1.00 12.55           O  
-ATOM   1427  CB  ALA A 221A     -8.896  11.946  11.784  1.00  8.96           C  
-ATOM   1428  N   GLN A 221      -7.103  14.176   9.482  1.00 13.41           N  
-ATOM   1429  CA  GLN A 221      -7.298  14.985   8.301  1.00 15.56           C  
-ATOM   1430  C   GLN A 221      -6.697  14.277   7.095  1.00 14.83           C  
-ATOM   1431  O   GLN A 221      -5.702  13.553   7.219  1.00 13.19           O  
-ATOM   1432  CB  GLN A 221      -6.607  16.323   8.500  1.00 18.50           C  
-ATOM   1433  CG  GLN A 221      -7.490  17.523   8.339  1.00 29.10           C  
-ATOM   1434  CD  GLN A 221      -8.150  17.954   9.628  1.00 33.70           C  
-ATOM   1435  OE1 GLN A 221      -9.112  17.357  10.111  1.00 35.81           O  
-ATOM   1436  NE2 GLN A 221      -7.671  19.033  10.247  1.00 38.87           N  
-ATOM   1437  N   LYS A 222      -7.226  14.506   5.895  1.00 16.31           N  
-ATOM   1438  CA  LYS A 222      -6.694  13.872   4.705  1.00 18.00           C  
-ATOM   1439  C   LYS A 222      -5.269  14.356   4.452  1.00 17.30           C  
-ATOM   1440  O   LYS A 222      -4.953  15.539   4.541  1.00 20.95           O  
-ATOM   1441  CB  LYS A 222      -7.578  14.192   3.493  1.00 20.59           C  
-ATOM   1442  CG  LYS A 222      -7.048  13.392   2.316  1.00 28.08           C  
-ATOM   1443  CD  LYS A 222      -7.725  13.569   0.957  1.00 33.55           C  
-ATOM   1444  CE  LYS A 222      -6.784  12.993  -0.121  1.00 37.90           C  
-ATOM   1445  NZ  LYS A 222      -6.326  11.640   0.170  1.00 40.44           N  
-ATOM   1446  N   ASN A 223      -4.387  13.414   4.179  1.00 16.17           N  
-ATOM   1447  CA  ASN A 223      -2.971  13.596   3.898  1.00 16.85           C  
-ATOM   1448  C   ASN A 223      -2.177  14.189   5.042  1.00 16.79           C  
-ATOM   1449  O   ASN A 223      -1.086  14.735   4.841  1.00 16.52           O  
-ATOM   1450  CB  ASN A 223      -2.740  14.475   2.685  1.00 21.85           C  
-ATOM   1451  CG  ASN A 223      -3.288  13.902   1.401  1.00 27.23           C  
-ATOM   1452  OD1 ASN A 223      -3.197  12.711   1.114  1.00 30.53           O  
-ATOM   1453  ND2 ASN A 223      -3.954  14.708   0.579  1.00 30.04           N  
-ATOM   1454  N   LYS A 224      -2.679  14.122   6.277  1.00 14.59           N  
-ATOM   1455  CA  LYS A 224      -1.921  14.595   7.412  1.00 13.39           C  
-ATOM   1456  C   LYS A 224      -1.941  13.504   8.486  1.00 13.88           C  
-ATOM   1457  O   LYS A 224      -2.689  13.602   9.470  1.00 14.12           O  
-ATOM   1458  CB  LYS A 224      -2.543  15.916   7.918  1.00 17.91           C  
-ATOM   1459  CG  LYS A 224      -2.347  17.129   6.988  1.00 18.91           C  
-ATOM   1460  CD  LYS A 224      -0.847  17.416   6.884  1.00 24.74           C  
-ATOM   1461  CE  LYS A 224      -0.527  18.570   5.919  1.00 28.00           C  
-ATOM   1462  NZ  LYS A 224       0.897  18.853   5.864  1.00 28.20           N  
-ATOM   1463  N   PRO A 225      -1.176  12.402   8.323  1.00 13.37           N  
-ATOM   1464  CA  PRO A 225      -1.117  11.286   9.272  1.00 10.84           C  
-ATOM   1465  C   PRO A 225      -0.488  11.688  10.610  1.00 10.78           C  
-ATOM   1466  O   PRO A 225       0.110  12.766  10.717  1.00  8.62           O  
-ATOM   1467  CB  PRO A 225      -0.321  10.232   8.549  1.00 11.05           C  
-ATOM   1468  CG  PRO A 225       0.659  11.053   7.717  1.00 11.55           C  
-ATOM   1469  CD  PRO A 225      -0.269  12.147   7.199  1.00 13.60           C  
-ATOM   1470  N   GLY A 226      -0.547  10.824  11.626  1.00  8.40           N  
-ATOM   1471  CA  GLY A 226       0.060  11.156  12.900  1.00  7.16           C  
-ATOM   1472  C   GLY A 226       1.563  10.975  12.786  1.00  7.53           C  
-ATOM   1473  O   GLY A 226       2.042  10.112  12.033  1.00  8.20           O  
-ATOM   1474  N   VAL A 227       2.341  11.757  13.546  1.00  4.70           N  
-ATOM   1475  CA  VAL A 227       3.796  11.651  13.543  1.00  5.97           C  
-ATOM   1476  C   VAL A 227       4.204  11.211  14.952  1.00  6.28           C  
-ATOM   1477  O   VAL A 227       3.635  11.676  15.953  1.00  5.64           O  
-ATOM   1478  CB  VAL A 227       4.460  12.982  13.208  1.00  7.76           C  
-ATOM   1479  CG1 VAL A 227       5.982  12.760  13.157  1.00 10.94           C  
-ATOM   1480  CG2 VAL A 227       3.941  13.514  11.875  1.00  7.01           C  
-ATOM   1481  N   TYR A 228       5.157  10.275  14.999  1.00  5.61           N  
-ATOM   1482  CA  TYR A 228       5.526   9.559  16.205  1.00  5.70           C  
-ATOM   1483  C   TYR A 228       7.030   9.541  16.418  1.00  6.21           C  
-ATOM   1484  O   TYR A 228       7.790   9.456  15.447  1.00  7.01           O  
-ATOM   1485  CB  TYR A 228       4.968   8.109  16.076  1.00  4.81           C  
-ATOM   1486  CG  TYR A 228       3.443   8.031  15.918  1.00  3.80           C  
-ATOM   1487  CD1 TYR A 228       2.655   7.991  17.072  1.00  4.76           C  
-ATOM   1488  CD2 TYR A 228       2.819   8.077  14.666  1.00  3.86           C  
-ATOM   1489  CE1 TYR A 228       1.264   8.014  16.990  1.00  4.96           C  
-ATOM   1490  CE2 TYR A 228       1.424   8.105  14.579  1.00  2.85           C  
-ATOM   1491  CZ  TYR A 228       0.661   8.079  15.743  1.00  5.93           C  
-ATOM   1492  OH  TYR A 228      -0.712   8.132  15.714  1.00  5.26           O  
-ATOM   1493  N   THR A 229       7.456   9.585  17.679  1.00  6.16           N  
-ATOM   1494  CA  THR A 229       8.856   9.460  18.041  1.00  5.40           C  
-ATOM   1495  C   THR A 229       9.241   8.017  17.786  1.00  5.02           C  
-ATOM   1496  O   THR A 229       8.529   7.096  18.189  1.00  6.37           O  
-ATOM   1497  CB  THR A 229       9.097   9.792  19.543  1.00  5.22           C  
-ATOM   1498  OG1 THR A 229       8.446  11.035  19.811  1.00  5.67           O  
-ATOM   1499  CG2 THR A 229      10.598   9.881  19.874  1.00  2.86           C  
-ATOM   1500  N   LYS A 230      10.380   7.831  17.133  1.00  5.10           N  
-ATOM   1501  CA  LYS A 230      10.887   6.545  16.703  1.00  5.17           C  
-ATOM   1502  C   LYS A 230      11.703   5.982  17.864  1.00  7.15           C  
-ATOM   1503  O   LYS A 230      12.913   6.233  17.947  1.00  7.32           O  
-ATOM   1504  CB  LYS A 230      11.732   6.786  15.402  1.00  2.80           C  
-ATOM   1505  CG  LYS A 230      12.093   5.567  14.496  1.00 10.00           C  
-ATOM   1506  CD  LYS A 230      12.644   6.042  13.108  1.00 14.02           C  
-ATOM   1507  CE  LYS A 230      11.763   5.834  11.829  1.00 22.86           C  
-ATOM   1508  NZ  LYS A 230      11.837   6.821  10.719  1.00 26.53           N  
-ATOM   1509  N   VAL A 231      11.072   5.181  18.754  1.00  6.94           N  
-ATOM   1510  CA  VAL A 231      11.713   4.687  19.977  1.00  7.40           C  
-ATOM   1511  C   VAL A 231      12.940   3.816  19.696  1.00  6.91           C  
-ATOM   1512  O   VAL A 231      13.871   3.827  20.511  1.00  5.86           O  
-ATOM   1513  CB  VAL A 231      10.692   3.880  20.845  1.00  6.49           C  
-ATOM   1514  CG1 VAL A 231      11.351   3.389  22.138  1.00  5.66           C  
-ATOM   1515  CG2 VAL A 231       9.534   4.785  21.277  1.00  3.91           C  
-ATOM   1516  N   CYS A 232      13.082   3.096  18.569  1.00  8.47           N  
-ATOM   1517  CA  CYS A 232      14.274   2.271  18.394  1.00  8.49           C  
-ATOM   1518  C   CYS A 232      15.549   3.105  18.329  1.00 10.22           C  
-ATOM   1519  O   CYS A 232      16.629   2.624  18.690  1.00 10.97           O  
-ATOM   1520  CB  CYS A 232      14.124   1.409  17.153  1.00  7.56           C  
-ATOM   1521  SG  CYS A 232      13.955   2.356  15.619  1.00 10.51           S  
-ATOM   1522  N   ASN A 233      15.483   4.419  18.060  1.00  7.57           N  
-ATOM   1523  CA  ASN A 233      16.694   5.227  18.040  1.00  7.53           C  
-ATOM   1524  C   ASN A 233      17.149   5.595  19.438  1.00  9.07           C  
-ATOM   1525  O   ASN A 233      18.289   6.050  19.612  1.00  9.15           O  
-ATOM   1526  CB  ASN A 233      16.484   6.527  17.295  1.00  8.15           C  
-ATOM   1527  CG  ASN A 233      16.272   6.344  15.802  1.00 13.44           C  
-ATOM   1528  OD1 ASN A 233      16.364   5.238  15.268  1.00 12.06           O  
-ATOM   1529  ND2 ASN A 233      15.984   7.431  15.088  1.00 13.34           N  
-ATOM   1530  N   TYR A 234      16.307   5.362  20.456  1.00  8.10           N  
-ATOM   1531  CA  TYR A 234      16.606   5.825  21.811  1.00  7.22           C  
-ATOM   1532  C   TYR A 234      16.907   4.757  22.829  1.00  9.56           C  
-ATOM   1533  O   TYR A 234      17.125   5.052  24.005  1.00  9.35           O  
-ATOM   1534  CB  TYR A 234      15.430   6.651  22.329  1.00  7.23           C  
-ATOM   1535  CG  TYR A 234      15.204   7.906  21.500  1.00  6.82           C  
-ATOM   1536  CD1 TYR A 234      15.988   9.043  21.704  1.00  4.54           C  
-ATOM   1537  CD2 TYR A 234      14.233   7.881  20.498  1.00  3.52           C  
-ATOM   1538  CE1 TYR A 234      15.813  10.173  20.907  1.00  6.69           C  
-ATOM   1539  CE2 TYR A 234      14.055   9.000  19.690  1.00  6.84           C  
-ATOM   1540  CZ  TYR A 234      14.836  10.132  19.901  1.00  7.74           C  
-ATOM   1541  OH  TYR A 234      14.627  11.244  19.107  1.00 11.10           O  
-ATOM   1542  N   VAL A 235      16.953   3.496  22.404  1.00  9.29           N  
-ATOM   1543  CA  VAL A 235      17.099   2.386  23.330  1.00  8.54           C  
-ATOM   1544  C   VAL A 235      18.374   2.474  24.176  1.00  9.97           C  
-ATOM   1545  O   VAL A 235      18.297   2.234  25.388  1.00  9.34           O  
-ATOM   1546  CB  VAL A 235      16.997   1.101  22.473  1.00  7.92           C  
-ATOM   1547  CG1 VAL A 235      17.324  -0.125  23.265  1.00  9.41           C  
-ATOM   1548  CG2 VAL A 235      15.533   0.923  22.035  1.00  8.60           C  
-ATOM   1549  N   SER A 236      19.533   2.851  23.639  1.00  9.83           N  
-ATOM   1550  CA  SER A 236      20.733   2.966  24.460  1.00 11.86           C  
-ATOM   1551  C   SER A 236      20.617   4.120  25.441  1.00 11.49           C  
-ATOM   1552  O   SER A 236      21.020   3.976  26.617  1.00 12.31           O  
-ATOM   1553  CB  SER A 236      21.966   3.183  23.600  1.00 10.33           C  
-ATOM   1554  OG  SER A 236      21.602   4.003  22.492  1.00 25.79           O  
-ATOM   1555  N   TRP A 237      19.999   5.240  25.017  1.00  9.65           N  
-ATOM   1556  CA  TRP A 237      19.809   6.341  25.969  1.00 10.66           C  
-ATOM   1557  C   TRP A 237      18.887   5.899  27.101  1.00  8.16           C  
-ATOM   1558  O   TRP A 237      19.185   6.154  28.268  1.00 10.60           O  
-ATOM   1559  CB  TRP A 237      19.204   7.602  25.302  1.00  9.85           C  
-ATOM   1560  CG  TRP A 237      18.779   8.693  26.306  1.00  9.33           C  
-ATOM   1561  CD1 TRP A 237      19.678   9.442  27.022  1.00  9.69           C  
-ATOM   1562  CD2 TRP A 237      17.477   9.029  26.597  1.00 10.18           C  
-ATOM   1563  NE1 TRP A 237      18.957  10.257  27.765  1.00  9.60           N  
-ATOM   1564  CE2 TRP A 237      17.649  10.048  27.549  1.00  9.74           C  
-ATOM   1565  CE3 TRP A 237      16.197   8.633  26.197  1.00  8.64           C  
-ATOM   1566  CZ2 TRP A 237      16.545  10.688  28.115  1.00 11.10           C  
-ATOM   1567  CZ3 TRP A 237      15.098   9.273  26.766  1.00 10.85           C  
-ATOM   1568  CH2 TRP A 237      15.264  10.297  27.722  1.00  9.77           C  
-ATOM   1569  N   ILE A 238      17.784   5.225  26.822  1.00  8.95           N  
-ATOM   1570  CA  ILE A 238      16.880   4.772  27.872  1.00  7.16           C  
-ATOM   1571  C   ILE A 238      17.591   3.815  28.822  1.00 10.00           C  
-ATOM   1572  O   ILE A 238      17.575   4.057  30.033  1.00  8.25           O  
-ATOM   1573  CB  ILE A 238      15.663   4.085  27.235  1.00  8.21           C  
-ATOM   1574  CG1 ILE A 238      14.887   5.115  26.410  1.00  9.09           C  
-ATOM   1575  CG2 ILE A 238      14.818   3.439  28.304  1.00  7.45           C  
-ATOM   1576  CD1 ILE A 238      13.707   4.551  25.634  1.00  8.04           C  
-ATOM   1577  N   LYS A 239      18.232   2.760  28.310  1.00 10.67           N  
-ATOM   1578  CA  LYS A 239      18.900   1.771  29.146  1.00 12.85           C  
-ATOM   1579  C   LYS A 239      19.976   2.394  30.031  1.00 13.33           C  
-ATOM   1580  O   LYS A 239      20.069   2.088  31.231  1.00 12.91           O  
-ATOM   1581  CB  LYS A 239      19.551   0.703  28.290  1.00 14.24           C  
-ATOM   1582  CG  LYS A 239      18.677  -0.090  27.329  1.00 20.20           C  
-ATOM   1583  CD  LYS A 239      17.696  -1.035  27.975  1.00 28.70           C  
-ATOM   1584  CE  LYS A 239      17.337  -2.150  26.986  1.00 33.51           C  
-ATOM   1585  NZ  LYS A 239      16.341  -3.073  27.529  1.00 38.05           N  
-ATOM   1586  N   GLN A 240      20.785   3.292  29.465  1.00 13.11           N  
-ATOM   1587  CA  GLN A 240      21.819   3.967  30.222  1.00 16.13           C  
-ATOM   1588  C   GLN A 240      21.247   4.876  31.311  1.00 15.07           C  
-ATOM   1589  O   GLN A 240      21.764   4.908  32.448  1.00 13.23           O  
-ATOM   1590  CB  GLN A 240      22.692   4.797  29.283  1.00 20.76           C  
-ATOM   1591  CG  GLN A 240      23.915   4.063  28.739  1.00 32.09           C  
-ATOM   1592  CD  GLN A 240      23.712   3.018  27.638  1.00 38.36           C  
-ATOM   1593  OE1 GLN A 240      24.299   3.125  26.565  1.00 41.96           O  
-ATOM   1594  NE2 GLN A 240      22.952   1.935  27.774  1.00 41.15           N  
-ATOM   1595  N   THR A 241      20.172   5.606  30.985  1.00 12.47           N  
-ATOM   1596  CA  THR A 241      19.602   6.507  31.964  1.00 11.21           C  
-ATOM   1597  C   THR A 241      18.965   5.699  33.097  1.00 12.06           C  
-ATOM   1598  O   THR A 241      19.216   5.998  34.269  1.00 12.47           O  
-ATOM   1599  CB  THR A 241      18.585   7.435  31.267  1.00 12.22           C  
-ATOM   1600  OG1 THR A 241      19.285   8.123  30.234  1.00  9.19           O  
-ATOM   1601  CG2 THR A 241      17.976   8.458  32.212  1.00 10.23           C  
-ATOM   1602  N   ILE A 242      18.212   4.626  32.826  1.00 11.75           N  
-ATOM   1603  CA  ILE A 242      17.642   3.790  33.878  1.00 15.41           C  
-ATOM   1604  C   ILE A 242      18.758   3.123  34.666  1.00 15.26           C  
-ATOM   1605  O   ILE A 242      18.613   2.889  35.869  1.00 17.30           O  
-ATOM   1606  CB  ILE A 242      16.724   2.712  33.282  1.00 15.99           C  
-ATOM   1607  CG1 ILE A 242      15.557   3.394  32.627  1.00 16.38           C  
-ATOM   1608  CG2 ILE A 242      16.220   1.743  34.371  1.00 20.08           C  
-ATOM   1609  CD1 ILE A 242      14.677   2.338  31.908  1.00 20.55           C  
-ATOM   1610  N   ALA A 243      19.894   2.813  34.053  1.00 14.30           N  
-ATOM   1611  CA  ALA A 243      20.979   2.192  34.808  1.00 15.30           C  
-ATOM   1612  C   ALA A 243      21.609   3.109  35.836  1.00 15.99           C  
-ATOM   1613  O   ALA A 243      22.203   2.620  36.792  1.00 18.95           O  
-ATOM   1614  CB  ALA A 243      22.085   1.730  33.871  1.00 15.57           C  
-ATOM   1615  N   SER A 244      21.507   4.421  35.683  1.00 16.71           N  
-ATOM   1616  CA  SER A 244      22.200   5.318  36.575  1.00 18.98           C  
-ATOM   1617  C   SER A 244      21.250   6.216  37.339  1.00 18.99           C  
-ATOM   1618  O   SER A 244      21.719   7.249  37.840  1.00 20.22           O  
-ATOM   1619  CB  SER A 244      23.135   6.190  35.774  1.00 22.12           C  
-ATOM   1620  OG  SER A 244      23.834   5.509  34.737  1.00 28.33           O  
-ATOM   1621  N   ASN A 245      19.945   5.942  37.483  1.00 19.67           N  
-ATOM   1622  CA  ASN A 245      19.063   6.905  38.120  1.00 17.94           C  
-ATOM   1623  C   ASN A 245      17.963   6.308  38.982  1.00 17.61           C  
-ATOM   1624  O   ASN A 245      17.194   7.050  39.581  1.00 18.62           O  
-ATOM   1625  CB  ASN A 245      18.423   7.805  37.049  1.00 15.10           C  
-ATOM   1626  CG  ASN A 245      19.371   8.795  36.412  1.00 14.70           C  
-ATOM   1627  OD1 ASN A 245      19.995   8.565  35.375  1.00 14.76           O  
-ATOM   1628  ND2 ASN A 245      19.503   9.964  37.006  1.00 15.12           N  
-ATOM   1629  OXT ASN A 245      17.848   5.108  39.108  1.00 17.47           O  
-TER    1630      ASN A 245                                                      
-HETATM 1631 CA    CA A 246     -10.281   4.349  37.022  1.00 12.55          CA  
-HETATM 1632  S   SO4 A 901      -1.510  17.496  23.249  1.00 29.81           S  
-HETATM 1633  O1  SO4 A 901      -2.303  17.445  24.404  1.00 28.35           O  
-HETATM 1634  O2  SO4 A 901      -0.129  17.510  23.534  1.00 32.70           O  
-HETATM 1635  O3  SO4 A 901      -1.846  16.354  22.466  1.00 34.73           O  
-HETATM 1636  O4  SO4 A 901      -1.794  18.660  22.490  1.00 34.05           O  
-HETATM 1637  N1  GP6 A 910      -2.799  13.984  14.449  1.00 11.34           N  
-HETATM 1638  N2  GP6 A 910      -2.006  12.213  15.666  1.00 13.91           N  
-HETATM 1639  C1  GP6 A 910      -2.301  13.508  15.582  1.00 10.23           C  
-HETATM 1640  C2  GP6 A 910      -1.887  14.370  16.605  1.00 10.14           C  
-HETATM 1641  C3  GP6 A 910      -1.937  15.761  16.467  1.00 11.14           C  
-HETATM 1642  C4  GP6 A 910      -1.541  16.611  17.504  1.00 11.20           C  
-HETATM 1643  C5  GP6 A 910      -1.078  16.086  18.720  1.00 15.83           C  
-HETATM 1644  C6  GP6 A 910      -1.027  14.699  18.866  1.00 12.39           C  
-HETATM 1645  C7  GP6 A 910      -1.425  13.863  17.820  1.00  9.07           C  
-HETATM 1646  N3  GP6 A 910      -0.672  16.876  19.746  1.00 19.39           N  
-HETATM 1647  C8  GP6 A 910       0.240  17.860  19.651  1.00 21.22           C  
-HETATM 1648  O1  GP6 A 910       0.774  18.199  18.584  1.00 21.77           O  
-HETATM 1649  N4  GP6 A 910       0.531  18.453  20.815  1.00 23.75           N  
-HETATM 1650  C9  GP6 A 910       1.546  19.294  21.074  1.00 24.91           C  
-HETATM 1651  C10 GP6 A 910       1.398  20.238  22.094  1.00 24.80           C  
-HETATM 1652  C11 GP6 A 910       2.444  21.108  22.411  1.00 25.49           C  
-HETATM 1653  C12 GP6 A 910       3.641  21.047  21.698  1.00 27.19           C  
-HETATM 1654  C13 GP6 A 910       3.794  20.119  20.675  1.00 28.40           C  
-HETATM 1655  C14 GP6 A 910       2.750  19.247  20.362  1.00 27.25           C  
-HETATM 1656 CL   GP6 A 910       4.950  22.099  22.054  1.00 30.61          CL  
-HETATM 1657  S   DMS A 300     -10.891   9.082  39.735  1.00 31.45           S  
-HETATM 1658  O   DMS A 300      -9.578   8.484  39.866  1.00 28.98           O  
-HETATM 1659  C1  DMS A 300     -11.518   9.443  41.354  1.00 29.41           C  
-HETATM 1660  C2  DMS A 300     -10.674  10.741  39.142  1.00 25.64           C  
-HETATM 1661  O   HOH A 501      -3.960   9.458  26.635  1.00  7.00           O  
-HETATM 1662  O   HOH A 502      -0.934   0.533  22.476  1.00  7.09           O  
-HETATM 1663  O   HOH A 503       4.911   5.903  25.302  1.00 11.68           O  
-HETATM 1664  O   HOH A 504      -2.051   7.930  24.883  1.00  6.12           O  
-HETATM 1665  O   HOH A 505       5.368  -6.887  33.376  1.00 26.76           O  
-HETATM 1666  O   HOH A 506      -7.581   8.976  36.672  1.00 10.52           O  
-HETATM 1667  O   HOH A 507      -5.812  10.616  35.059  1.00  9.39           O  
-HETATM 1668  O   HOH A 508      -9.378   8.476  22.746  1.00  3.43           O  
-HETATM 1669  O   HOH A 509     -12.040   6.479  18.729  1.00 17.88           O  
-HETATM 1670  O   HOH A 510     -11.656   0.405  27.177  1.00 14.18           O  
-HETATM 1671  O   HOH A 511      -8.159  -0.125  30.036  1.00 20.04           O  
-HETATM 1672  O   HOH A 512      -3.435   3.346  33.348  1.00 12.31           O  
-HETATM 1673  O   HOH A 513       0.768  11.548  16.616  1.00  8.12           O  
-HETATM 1674  O   HOH A 514      -3.892   8.815  10.260  1.00 13.63           O  
-HETATM 1675  O   HOH A 515      -4.771  11.488   9.947  1.00 14.85           O  
-HETATM 1676  O   HOH A 516      -4.660  15.068  10.846  1.00 22.54           O  
-HETATM 1677  O   HOH A 517      -2.649   3.406   5.482  1.00 22.86           O  
-HETATM 1678  O   HOH A 518       7.249   7.083   8.299  1.00 13.49           O  
-HETATM 1679  O   HOH A 519       8.474  -4.491  16.827  1.00 18.98           O  
-HETATM 1680  O   HOH A 520      10.956   2.697  16.744  1.00  7.06           O  
-HETATM 1681  O   HOH A 522      -8.733   0.068  14.575  1.00 11.42           O  
-HETATM 1682  O   HOH A 523     -14.010  -0.190  28.421  1.00 10.01           O  
-HETATM 1683  O   HOH A 524      -4.683  -1.752  32.718  1.00 18.26           O  
-HETATM 1684  O   HOH A 525      -5.797  -1.336  29.468  1.00 15.59           O  
-HETATM 1685  O   HOH A 526      -4.525   0.695  31.446  1.00 19.80           O  
-HETATM 1686  O   HOH A 527      -1.358   0.391  33.203  1.00 15.35           O  
-HETATM 1687  O   HOH A 528      -0.773  -4.602  22.947  1.00 25.80           O  
-HETATM 1688  O   HOH A 529      -8.328  13.737  38.065  1.00 20.36           O  
-HETATM 1689  O   HOH A 530      16.304   2.891  38.543  1.00 18.39           O  
-HETATM 1690  O   HOH A 531      10.193  -4.417  36.556  1.00 29.39           O  
-HETATM 1691  O   HOH A 532       7.605  21.476  24.971  1.00 14.42           O  
-HETATM 1692  O   HOH A 533       8.956  26.202  21.545  1.00 23.39           O  
-HETATM 1693  O   HOH A 534      13.594  24.646  21.943  1.00 36.06           O  
-HETATM 1694  O   HOH A 535      -2.291   3.362  44.378  1.00 25.63           O  
-HETATM 1695  O   HOH A 536      19.517   9.415  22.474  1.00 19.79           O  
-HETATM 1696  O   HOH A 537      20.026   6.240  22.104  1.00 17.49           O  
-HETATM 1697  O   HOH A 538      24.402  15.169  26.685  1.00 29.16           O  
-HETATM 1698  O   HOH A 540      12.398  22.738  26.139  1.00 17.73           O  
-HETATM 1699  O   HOH A 541      13.464  22.522  23.678  1.00 18.58           O  
-HETATM 1700  O   HOH A 542      11.261  20.805  27.694  1.00 19.58           O  
-HETATM 1701  O   HOH A 543       8.541  20.252  27.396  1.00 24.16           O  
-HETATM 1702  O   HOH A 545      11.316  12.948  17.641  1.00  8.92           O  
-HETATM 1703  O   HOH A 546       8.744  13.864  17.255  1.00 14.22           O  
-HETATM 1704  O   HOH A 548      -2.118  20.163  15.200  1.00 22.69           O  
-HETATM 1705  O   HOH A 549      -1.744  22.958  14.783  1.00 27.36           O  
-HETATM 1706  O   HOH A 550      -1.103  22.627  11.800  1.00 42.67           O  
-HETATM 1707  O   HOH A 551      -9.605   6.145  38.147  1.00 13.56           O  
-HETATM 1708  O   HOH A 552     -10.305   2.452  35.953  1.00 14.83           O  
-HETATM 1709  O   HOH A 553      -9.085  -0.013  37.161  1.00 17.30           O  
-HETATM 1710  O   HOH A 554     -10.165  -2.175  35.948  1.00 21.39           O  
-HETATM 1711  O   HOH A 557     -16.718   0.504  28.497  1.00 26.63           O  
-HETATM 1712  O   HOH A 558     -14.147   8.932  16.610  1.00 20.94           O  
-HETATM 1713  O   HOH A 562       2.344   1.639   4.883  1.00 21.71           O  
-HETATM 1714  O   HOH A 563      -0.386   1.667   4.501  1.00 32.67           O  
-HETATM 1715  O   HOH A 567       3.150  -8.429  34.636  1.00 28.49           O  
-HETATM 1716  O   HOH A 570      19.250  -0.481  32.048  1.00 24.26           O  
-HETATM 1717  O   HOH A 571      17.121  -3.781  38.769  1.00 33.84           O  
-HETATM 1718  O   HOH A 580      10.917  24.912  25.488  1.00 38.62           O  
-HETATM 1719  O   HOH A 581      -2.102   7.991  13.412  1.00  9.63           O  
-HETATM 1720  O   HOH A 582     -16.400   2.738  33.203  1.00 41.09           O  
-HETATM 1721  O   HOH A 583      -3.030  -3.031  39.996  1.00 22.68           O  
-HETATM 1722  O   HOH A 590       1.364   0.260  43.796  1.00 31.85           O  
-HETATM 1723  O   HOH A 593      -1.364  22.691  23.257  1.00 33.19           O  
-HETATM 1724  O   HOH A 598       3.352   4.420   2.819  1.00 31.89           O  
-HETATM 1725  O   HOH A 599      -8.564  18.376  12.973  1.00 23.49           O  
-HETATM 1726  O   HOH A 604     -16.135   0.515  20.349  1.00 32.42           O  
-HETATM 1727  O   HOH A 606       9.952  16.157   5.889  1.00 23.18           O  
-HETATM 1728  O   HOH A 609      10.125  19.157  12.465  1.00 19.83           O  
-HETATM 1729  O   HOH A 610       3.942   1.312  44.708  1.00 29.53           O  
-HETATM 1730  O   HOH A 611       5.612  -6.477  40.918  1.00 38.04           O  
-HETATM 1731  O   HOH A 617       2.122  11.774   1.579  1.00 35.06           O  
-HETATM 1732  O   HOH A 620     -14.304  -2.884  29.065  1.00 34.47           O  
-HETATM 1733  O   HOH A 621      -9.067  13.982  34.007  1.00 22.14           O  
-HETATM 1734  O   HOH A 622      -8.175  16.141  31.088  1.00 29.59           O  
-HETATM 1735  O   HOH A 623      10.128   0.347  45.834  1.00 30.49           O  
-HETATM 1736  O   HOH A 628       0.194   2.404  44.991  1.00 35.92           O  
-HETATM 1737  O   HOH A 630      17.921  20.748  24.349  1.00 35.92           O  
-HETATM 1738  O   HOH A 632       1.826  -5.500  15.587  1.00 30.76           O  
-HETATM 1739  O   HOH A 641     -10.140  12.191  35.925  1.00 30.12           O  
-HETATM 1740  O   HOH A 653      23.753  12.631  25.467  1.00 42.17           O  
-HETATM 1741  O   HOH A 656     -14.793  13.292  29.545  1.00 21.19           O  
-HETATM 1742  O   HOH A 657      16.165  20.025  15.633  1.00 27.02           O  
-HETATM 1743  O   HOH A 658     -11.918  22.665  15.868  1.00 24.06           O  
-HETATM 1744  O   HOH A 660      -8.591  18.628  19.419  1.00 37.79           O  
-HETATM 1745  O   HOH A 661     -10.352  18.172  16.556  1.00 39.37           O  
-HETATM 1746  O   HOH A 664      12.793  -4.038  27.479  1.00 29.24           O  
-HETATM 1747  O   HOH A 666       6.605  24.863  22.288  1.00 29.87           O  
-HETATM 1748  O   HOH A 667     -11.181   1.471  14.159  1.00 20.90           O  
-HETATM 1749  O   HOH A 668      -8.321   0.477  11.618  1.00 36.16           O  
-HETATM 1750  O   HOH A 670      -0.606  15.153  40.408  1.00 39.63           O  
-HETATM 1751  O   HOH A 673      12.771  22.813   6.978  1.00 37.19           O  
-HETATM 1752  O   HOH A 676       2.452  21.271  37.636  1.00 39.70           O  
-HETATM 1753  O   HOH A 680       3.364   8.301  45.441  1.00 39.99           O  
-HETATM 1754  O   HOH A 682       6.528  21.521  15.280  1.00 30.45           O  
-HETATM 1755  O   HOH A 684      -9.725  16.004   5.667  1.00 35.43           O  
-HETATM 1756  O   HOH A 685      19.610   3.234  20.657  1.00 38.75           O  
-HETATM 1757  O   HOH A 686       5.040  21.311  25.910  1.00 41.75           O  
-CONECT   48 1007                                                                
-CONECT  185  298                                                                
-CONECT  298  185                                                                
-CONECT  384 1631                                                                
-CONECT  397 1631                                                                
-CONECT  421 1631                                                                
-CONECT  461 1631                                                                
-CONECT  811 1521                                                                
-CONECT  853 1327                                                                
-CONECT 1007   48                                                                
-CONECT 1084 1190                                                                
-CONECT 1190 1084                                                                
-CONECT 1265 1422                                                                
-CONECT 1327  853                                                                
-CONECT 1422 1265                                                                
-CONECT 1521  811                                                                
-CONECT 1631  384  397  421  461                                                 
-CONECT 1631 1707 1708                                                           
-CONECT 1632 1633 1634 1635 1636                                                 
-CONECT 1633 1632                                                                
-CONECT 1634 1632                                                                
-CONECT 1635 1632                                                                
-CONECT 1636 1632                                                                
-CONECT 1637 1639                                                                
-CONECT 1638 1639                                                                
-CONECT 1639 1637 1638 1640                                                      
-CONECT 1640 1639 1641 1645                                                      
-CONECT 1641 1640 1642                                                           
-CONECT 1642 1641 1643                                                           
-CONECT 1643 1642 1644 1646                                                      
-CONECT 1644 1643 1645                                                           
-CONECT 1645 1640 1644                                                           
-CONECT 1646 1643 1647                                                           
-CONECT 1647 1646 1648 1649                                                      
-CONECT 1648 1647                                                                
-CONECT 1649 1647 1650                                                           
-CONECT 1650 1649 1651 1655                                                      
-CONECT 1651 1650 1652                                                           
-CONECT 1652 1651 1653                                                           
-CONECT 1653 1652 1654 1656                                                      
-CONECT 1654 1653 1655                                                           
-CONECT 1655 1650 1654                                                           
-CONECT 1656 1653                                                                
-CONECT 1657 1658 1659 1660                                                      
-CONECT 1658 1657                                                                
-CONECT 1659 1657                                                                
-CONECT 1660 1657                                                                
-CONECT 1707 1631                                                                
-CONECT 1708 1631                                                                
-MASTER      307    0    4    4   10    0    9    6 1756    1   49   18          
-END                                                                             
diff --git a/plip/test/pdb/1bma.pdb b/plip/test/pdb/1bma.pdb
deleted file mode 100644
index 294818a..0000000
--- a/plip/test/pdb/1bma.pdb
+++ /dev/null
@@ -1,2569 +0,0 @@
-HEADER    HYDROLASE/HYDROLASE INHIBITOR           01-MAY-95   1BMA              
-TITLE     BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC     
-TITLE    2 ELASTASE                                                             
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER 1;                
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 SYNONYM: ELASTASE-1;                                                 
-COMPND   5 EC: 3.4.21.36                                                        
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
-SOURCE   3 ORGANISM_COMMON: PIGS,SWINE,WILD BOAR;                               
-SOURCE   4 ORGANISM_TAXID: 9823;                                                
-SOURCE   5 ORGAN: PANCREAS                                                      
-KEYWDS    SERINE PROTEASE,METAL-BINDING, PROTEASE, SECRETED, ZYMOGEN,           
-KEYWDS   2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    E.PEISACH,D.CASEBIER,S.L.GALLION,P.FURTH,G.A.PETSKO,J.C.HOGAN JR.,    
-AUTHOR   2 D.RINGE                                                              
-REVDAT   4   13-JUL-11 1BMA    1       VERSN                                    
-REVDAT   3   24-FEB-09 1BMA    1       VERSN                                    
-REVDAT   2   01-APR-03 1BMA    1       JRNL                                     
-REVDAT   1   07-DEC-95 1BMA    0                                                
-JRNL        AUTH   E.PEISACH,D.CASEBIER,S.L.GALLION,P.FURTH,G.A.PETSKO,         
-JRNL        AUTH 2 J.C.HOGAN JR.,D.RINGE                                        
-JRNL        TITL   INTERACTION OF A PEPTIDOMIMETIC AMINIMIDE INHIBITOR WITH     
-JRNL        TITL 2 ELASTASE.                                                    
-JRNL        REF    SCIENCE                       V. 269    66 1995              
-JRNL        REFN                   ISSN 0036-8075                               
-JRNL        PMID   7604279                                                      
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   C.MATTOS,D.A.GIAMMONA,G.A.PETSKO,D.RINGE                     
-REMARK   1  TITL   STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC 
-REMARK   1  TITL 2 ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES  
-REMARK   1  TITL 3 WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS            
-REMARK   1  REF    BIOCHEMISTRY                  V.  34  3193 1995              
-REMARK   1  REFN                   ISSN 0006-2960                               
-REMARK   1 REFERENCE 2                                                          
-REMARK   1  AUTH   I.LI DE LA SIERRA,E.PAPAMICHAEL,C.SAKARELOS,J.-L.DIMICOLI,   
-REMARK   1  AUTH 2 T.PRANGE                                                     
-REMARK   1  TITL   INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3 (TFLA)    
-REMARK   1  TITL 2 WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8       
-REMARK   1  TITL 3 ANGSTROMS                                                    
-REMARK   1  REF    J.MOL.RECOG.                  V.   3    36 1990              
-REMARK   1  REFN                   ISSN 0952-3499                               
-REMARK   1 REFERENCE 3                                                          
-REMARK   1  AUTH   E.MEYER,G.COLE,R.RADHAKRISHNAN,O.EPP                         
-REMARK   1  TITL   STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT 1.65      
-REMARK   1  TITL 2 ANGSTROMS RESOLUTION                                         
-REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.B      V.  44    26 1988              
-REMARK   1  REFN                   ISSN 0108-7681                               
-REMARK   1 REFERENCE 4                                                          
-REMARK   1  AUTH   E.MEYER,R.RADHAKRISHNAN,G.COLE,L.G.PRESTA                    
-REMARK   1  TITL   STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH  
-REMARK   1  TITL 2 PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION     
-REMARK   1  REF    J.MOL.BIOL.                   V. 189   533 1986              
-REMARK   1  REFN                   ISSN 0022-2836                               
-REMARK   1 REFERENCE 5                                                          
-REMARK   1  AUTH   D.L.HUGHES,L.C.DIECKER,L.C.BIETH,J.-L.DIMICOLI               
-REMARK   1  TITL   CRYSTALLOGRAPHIC STUDY OF THE BINDING OF A TRI-FLUOROACETYL  
-REMARK   1  TITL 2 DIPEPTIDE ANILIDE INHIBITOR WITH ELASTASE                    
-REMARK   1  REF    J.MOL.BIOL.                   V. 162   645 1982              
-REMARK   1  REFN                   ISSN 0022-2836                               
-REMARK   1 REFERENCE 6                                                          
-REMARK   1  AUTH   J.-L.DIMICOLI,A.RENAUD,J.BIETH                               
-REMARK   1  TITL   THE INDIRECT MECHANISM OF ACTION OF THE TRIFLUOROACETYL      
-REMARK   1  TITL 2 PEPTIDES ON ELASTASE                                         
-REMARK   1  REF    EUR.J.BIOCHEM.                V. 107   423 1980              
-REMARK   1  REFN                   ISSN 0014-2956                               
-REMARK   1 REFERENCE 7                                                          
-REMARK   1  AUTH   L.SAWYER,C.M.SHOTTON,J.W.CAMPBELL,P.L.WENDELL,H.MUIRHEAD,    
-REMARK   1  AUTH 2 H.C.WATSON,R.DIAMOND,R.C.LADNER                              
-REMARK   1  TITL   THE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC       
-REMARK   1  TITL 2 ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE   
-REMARK   1  TITL 3 STRUCTURE OF ALPHA-CHYMOTRYPSIN                              
-REMARK   1  REF    J.MOL.BIOL.                   V. 118   137 1978              
-REMARK   1  REFN                   ISSN 0022-2836                               
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : X-PLOR 3.1                                           
-REMARK   3   AUTHORS     : BRUNGER                                              
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 58.7                           
-REMARK   3   NUMBER OF REFLECTIONS             : 44505                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
-REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
-REMARK   3   R VALUE            (WORKING SET) : 0.192                           
-REMARK   3   FREE R VALUE                     : NULL                            
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
-REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
-REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
-REMARK   3   BIN FREE R VALUE                    : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 1822                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 43                                      
-REMARK   3   SOLVENT ATOMS            : 134                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.50                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
-REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.015                           
-REMARK   3   BOND ANGLES            (DEGREES) : 2.70                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.80                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.01                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1BMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-94                          
-REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
-REMARK 200  PH                             : NULL                               
-REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : N                                  
-REMARK 200  RADIATION SOURCE               : NULL                               
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5148                             
-REMARK 200  MONOCHROMATOR                  : NI FILTER                          
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : NULL                               
-REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
-REMARK 200  DATA SCALING SOFTWARE          : NULL                               
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39545                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 58.7                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : 0.06300                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
-REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 43.84                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: THE INHIBITOR WAS SOAKED INTO THE        
-REMARK 280  GROWN CRYSTALS USING A 4 MM STOCK SOLUTION OF THE INHIBITOR IN      
-REMARK 280  10% ACETONITRILE.                                                   
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.08000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.76000            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.84000            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.76000            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.08000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.84000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
-REMARK 500    HIS A  60   NE2   HIS A  60   CD2    -0.073                       
-REMARK 500    HIS A  75   NE2   HIS A  75   CD2    -0.070                       
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    TRP A  27   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
-REMARK 500    TRP A  27   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
-REMARK 500    ARG A  36   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
-REMARK 500    TRP A  41   CD1 -  CG  -  CD2 ANGL. DEV. =   7.3 DEGREES          
-REMARK 500    TRP A  41   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
-REMARK 500    ARG A  51   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
-REMARK 500    TRP A  54   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES          
-REMARK 500    TRP A  54   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
-REMARK 500    ARG A  64   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
-REMARK 500    TRP A  98   CD1 -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES          
-REMARK 500    TRP A  98   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES          
-REMARK 500    TRP A 147   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
-REMARK 500    TRP A 147   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
-REMARK 500    ARG A 151   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
-REMARK 500    ARG A 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
-REMARK 500    TRP A 179   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
-REMARK 500    TRP A 179   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
-REMARK 500    ARG A 226   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
-REMARK 500    ARG A 240   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
-REMARK 500    TRP A 247   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
-REMARK 500    TRP A 247   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    HIS A  75      -55.40   -129.50                                   
-REMARK 500    TYR A 178     -113.73   -104.95                                   
-REMARK 500    SER A 203      135.31    -37.60                                   
-REMARK 500    SER A 222      -56.81   -120.48                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 600                                                                      
-REMARK 600 HETEROGEN                                                            
-REMARK 600 NOTE THAT SUBCOMPONENT MBH IS REFERRED TO AS MBA IN THE PAPER        
-REMARK 600 CITED IN THE JRNL RECORDS ABOVE.                                     
-REMARK 620                                                                      
-REMARK 620 METAL COORDINATION                                                   
-REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              CA A 280  CA                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 GLU A  84   OE2                                                    
-REMARK 620 2 GLN A  79   O    93.3                                              
-REMARK 620 3 HOH A 355   O    84.6  90.9                                        
-REMARK 620 4 ASN A  81   OD1  83.2  93.3 167.3                                  
-REMARK 620 5 GLU A  74   OE1  94.5 163.5 104.3  73.2                            
-REMARK 620 6 ASN A  76   O   169.8  87.8 105.6  86.5  82.0                      
-REMARK 620 7 GLU A  74   OE2  95.9 150.8  62.5 115.3  42.2  88.0                
-REMARK 620 N                    1     2     3     4     5     6                 
-REMARK 630                                                                      
-REMARK 630 MOLECULE TYPE: NULL                                                  
-REMARK 630 MOLECULE NAME: (1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL)       
-REMARK 630 PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2-[(TRIFLUOROACETYL)      
-REMARK 630 AMINO]PENTANOYL}DIAZANIUM                                            
-REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
-REMARK 630                                                                      
-REMARK 630   M RES C SSSEQI                                                     
-REMARK 630     0QH A   256                                                      
-REMARK 630 SOURCE: NULL                                                         
-REMARK 630 TAXONOMY: NULL                                                       
-REMARK 630 SUBCOMP:    TFA LEU MBH ISO                                          
-REMARK 630 DETAILS: NULL                                                        
-REMARK 700                                                                      
-REMARK 700 SHEET                                                                
-REMARK 700 THE SHEETS PRESENTED AS *S1* AND *S2* IN SHEET RECORDS               
-REMARK 700 BELOW ARE ACTUALLY TWO SIX-STRANDED BETA-BARRELS.  THIS IS           
-REMARK 700 REPRESENTED BY TWO SEVEN-STRANDED SHEETS IN WHICH THE FIRST          
-REMARK 700 AND LAST STRANDS OF EACH SHEET ARE IDENTICAL.                        
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 280                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 290                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QH A 256                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CAT                                                 
-REMARK 800 EVIDENCE_CODE: AUTHOR                                                
-REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD                                    
-REMARK 999                                                                      
-REMARK 999 SEQUENCE                                                             
-REMARK 999 THE RESIDUE NUMBERING SCHEME FOR THE PROTEIN IS SEQUENTIAL           
-REMARK 999 STARTING WITH VAL A 16 AND ENDING WITH ASN A 255.                    
-REMARK 999                                                                      
-REMARK 999 THE IDENTITY OF ASN A 81 AGREES WITH THE SEQUENCES OF                
-REMARK 999 SEVERAL OTHER ELASTASE STRUCTURES.  THE AUTHORS, THEREFORE,          
-REMARK 999 BELIEVE IT TO BE CORRECT.                                            
-DBREF  1BMA A   16   255  UNP    P00772   CELA1_PIG       27    266             
-SEQADV 1BMA ASN A   81  UNP  P00772    ASP    92 CONFLICT                       
-SEQRES   1 A  240  VAL VAL GLY GLY THR GLU ALA GLN ARG ASN SER TRP PRO          
-SEQRES   2 A  240  SER GLN ILE SER LEU GLN TYR ARG SER GLY SER SER TRP          
-SEQRES   3 A  240  ALA HIS THR CYS GLY GLY THR LEU ILE ARG GLN ASN TRP          
-SEQRES   4 A  240  VAL MET THR ALA ALA HIS CYS VAL ASP ARG GLU LEU THR          
-SEQRES   5 A  240  PHE ARG VAL VAL VAL GLY GLU HIS ASN LEU ASN GLN ASN          
-SEQRES   6 A  240  ASN GLY THR GLU GLN TYR VAL GLY VAL GLN LYS ILE VAL          
-SEQRES   7 A  240  VAL HIS PRO TYR TRP ASN THR ASP ASP VAL ALA ALA GLY          
-SEQRES   8 A  240  TYR ASP ILE ALA LEU LEU ARG LEU ALA GLN SER VAL THR          
-SEQRES   9 A  240  LEU ASN SER TYR VAL GLN LEU GLY VAL LEU PRO ARG ALA          
-SEQRES  10 A  240  GLY THR ILE LEU ALA ASN ASN SER PRO CYS TYR ILE THR          
-SEQRES  11 A  240  GLY TRP GLY LEU THR ARG THR ASN GLY GLN LEU ALA GLN          
-SEQRES  12 A  240  THR LEU GLN GLN ALA TYR LEU PRO THR VAL ASP TYR ALA          
-SEQRES  13 A  240  ILE CYS SER SER SER SER TYR TRP GLY SER THR VAL LYS          
-SEQRES  14 A  240  ASN SER MET VAL CYS ALA GLY GLY ASP GLY VAL ARG SER          
-SEQRES  15 A  240  GLY CYS GLN GLY ASP SER GLY GLY PRO LEU HIS CYS LEU          
-SEQRES  16 A  240  VAL ASN GLY GLN TYR ALA VAL HIS GLY VAL THR SER PHE          
-SEQRES  17 A  240  VAL SER ARG LEU GLY CYS ASN VAL THR ARG LYS PRO THR          
-SEQRES  18 A  240  VAL PHE THR ARG VAL SER ALA TYR ILE SER TRP ILE ASN          
-SEQRES  19 A  240  ASN VAL ILE ALA SER ASN                                      
-HET     CA  A 280       1                                                       
-HET    SO4  A 290       5                                                       
-HET    0QH  A 256      37                                                       
-HETNAM      CA CALCIUM ION                                                      
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM     0QH (1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL)                  
-HETNAM   2 0QH  PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2-                   
-HETNAM   3 0QH  [(TRIFLUOROACETYL)AMINO]PENTANOYL}DIAZANIUM                     
-FORMUL   2   CA    CA 2+                                                        
-FORMUL   3  SO4    O4 S 2-                                                      
-FORMUL   4  0QH    C27 H36 F3 N4 O3 1+                                          
-FORMUL   5  HOH   *134(H2 O)                                                    
-HELIX    1  H1 ASP A  169  SER A  175  1                                   7    
-HELIX    2  H2 TYR A  244  ASN A  255  1                                  12    
-SHEET    1  S1 7 SER A  29  SER A  37  0                                        
-SHEET    2  S1 7 SER A  40  ILE A  50 -1                                        
-SHEET    3  S1 7 ASN A  53  ALA A  59 -1                                        
-SHEET    4  S1 7 ASP A 108  GLN A 116 -1                                        
-SHEET    5  S1 7 GLU A  84  HIS A  95 -1                                        
-SHEET    6  S1 7 PHE A  68  GLY A  73 -1                                        
-SHEET    7  S1 7 SER A  29  SER A  37 -1                                        
-SHEET    1  S2 7 ASN A 139  THR A 150  0                                        
-SHEET    2  S2 7 GLY A 154  VAL A 168 -1                                        
-SHEET    3  S2 7 SER A 186  VAL A 195 -1                                        
-SHEET    4  S2 7 ASN A 230  VAL A 241 -1                                        
-SHEET    5  S2 7 HIS A 218  VAL A 224 -1                                        
-SHEET    6  S2 7 SER A 203  CYS A 209 -1                                        
-SHEET    7  S2 7 SER A 140  THR A 150 -1                                        
-SHEET    1  S3 3 GLY A 154  ALA A 157  0                                        
-SHEET    2  S3 3 TRP A 147  LEU A 149 -1                                        
-SHEET    3  S3 3 GLN A 200  ASP A 202 -1                                        
-SSBOND   1 CYS A   45    CYS A   61                          1555   1555  2.02  
-SSBOND   2 CYS A  142    CYS A  209                          1555   1555  2.01  
-SSBOND   3 CYS A  173    CYS A  189                          1555   1555  2.01  
-SSBOND   4 CYS A  199    CYS A  229                          1555   1555  2.01  
-LINK        CA    CA A 280                 OE2 GLU A  84     1555   1555  2.51  
-LINK        CA    CA A 280                 O   GLN A  79     1555   1555  2.37  
-LINK        CA    CA A 280                 O   HOH A 355     1555   1555  2.53  
-LINK        CA    CA A 280                 OD1 ASN A  81     1555   1555  2.52  
-LINK        CA    CA A 280                 OE1 GLU A  74     1555   1555  2.50  
-LINK        CA    CA A 280                 O   ASN A  76     1555   1555  2.37  
-LINK        CA    CA A 280                 OE2 GLU A  74     1555   1555  3.09  
-SITE     1 AC1  6 GLU A  74  ASN A  76  GLN A  79  ASN A  81                    
-SITE     2 AC1  6 GLU A  84  HOH A 355                                          
-SITE     1 AC2  5 GLY A 133  ARG A 151  ARG A 240  HOH A 340                    
-SITE     2 AC2  5 HOH A 345                                                     
-SITE     1 AC3 17 GLU A  65  LEU A  66  THR A  67  VAL A 103                    
-SITE     2 AC3 17 THR A 152  THR A 182  CYS A 199  GLN A 200                    
-SITE     3 AC3 17 SER A 203  THR A 221  SER A 222  PHE A 223                    
-SITE     4 AC3 17 VAL A 224  SER A 225  ARG A 226  GLY A 228                    
-SITE     5 AC3 17 CYS A 229                                                     
-SITE     1 CAT  3 ASP A 108  HIS A  60  SER A 203                               
-CRYST1   52.160   57.680   75.520  90.00  90.00  90.00 P 21 21 21    4          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.019172  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.017337  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.013242        0.00000                         
-ATOM      1  N   VAL A  16      41.593  32.726  35.179  1.00  5.92           N  
-ATOM      2  CA  VAL A  16      40.667  33.462  36.045  1.00  5.90           C  
-ATOM      3  C   VAL A  16      39.544  34.005  35.167  1.00  9.05           C  
-ATOM      4  O   VAL A  16      39.830  34.764  34.220  1.00 10.48           O  
-ATOM      5  CB  VAL A  16      41.446  34.646  36.763  1.00  3.34           C  
-ATOM      6  CG1 VAL A  16      40.479  35.497  37.575  1.00  5.02           C  
-ATOM      7  CG2 VAL A  16      42.485  34.116  37.761  1.00  7.03           C  
-ATOM      8  N   VAL A  17      38.276  33.667  35.460  1.00  9.38           N  
-ATOM      9  CA  VAL A  17      37.124  34.221  34.774  1.00  8.32           C  
-ATOM     10  C   VAL A  17      36.701  35.486  35.515  1.00 10.66           C  
-ATOM     11  O   VAL A  17      36.731  35.504  36.741  1.00 10.27           O  
-ATOM     12  CB  VAL A  17      35.956  33.225  34.766  1.00  6.81           C  
-ATOM     13  CG1 VAL A  17      34.839  33.738  33.857  1.00  6.95           C  
-ATOM     14  CG2 VAL A  17      36.405  31.908  34.179  1.00  7.97           C  
-ATOM     15  N   GLY A  18      36.334  36.574  34.832  1.00  9.48           N  
-ATOM     16  CA  GLY A  18      35.822  37.755  35.533  1.00 10.87           C  
-ATOM     17  C   GLY A  18      36.915  38.523  36.270  1.00 12.24           C  
-ATOM     18  O   GLY A  18      36.678  39.227  37.249  1.00 14.40           O  
-ATOM     19  N   GLY A  19      38.145  38.374  35.824  1.00 12.48           N  
-ATOM     20  CA  GLY A  19      39.268  39.043  36.456  1.00 14.94           C  
-ATOM     21  C   GLY A  19      39.626  40.361  35.784  1.00 16.65           C  
-ATOM     22  O   GLY A  19      38.950  40.814  34.852  1.00 18.12           O  
-ATOM     23  N   THR A  20      40.656  41.023  36.329  1.00 17.53           N  
-ATOM     24  CA  THR A  20      41.215  42.247  35.786  1.00 18.60           C  
-ATOM     25  C   THR A  20      42.711  42.021  35.745  1.00 18.76           C  
-ATOM     26  O   THR A  20      43.229  41.126  36.410  1.00 18.06           O  
-ATOM     27  CB  THR A  20      40.854  43.488  36.671  1.00 18.53           C  
-ATOM     28  OG1 THR A  20      41.161  43.234  38.028  1.00 21.90           O  
-ATOM     29  CG2 THR A  20      39.362  43.783  36.615  1.00 20.28           C  
-ATOM     30  N   GLU A  21      43.465  42.806  34.977  1.00 17.36           N  
-ATOM     31  CA  GLU A  21      44.865  42.555  34.859  1.00 16.71           C  
-ATOM     32  C   GLU A  21      45.574  42.977  36.145  1.00 17.00           C  
-ATOM     33  O   GLU A  21      45.219  44.002  36.718  1.00 16.14           O  
-ATOM     34  CB  GLU A  21      45.362  43.317  33.667  1.00 20.43           C  
-ATOM     35  CG  GLU A  21      46.829  43.020  33.446  1.00 24.72           C  
-ATOM     36  CD  GLU A  21      47.475  43.832  32.343  1.00 30.35           C  
-ATOM     37  OE1 GLU A  21      46.815  44.064  31.332  1.00 32.22           O  
-ATOM     38  OE2 GLU A  21      48.640  44.213  32.503  1.00 34.58           O  
-ATOM     39  N   ALA A  22      46.507  42.201  36.690  1.00 13.57           N  
-ATOM     40  CA  ALA A  22      47.254  42.613  37.877  1.00 16.53           C  
-ATOM     41  C   ALA A  22      48.413  43.574  37.541  1.00 19.25           C  
-ATOM     42  O   ALA A  22      48.936  43.546  36.410  1.00 19.34           O  
-ATOM     43  CB  ALA A  22      47.850  41.387  38.565  1.00 12.65           C  
-ATOM     44  N   GLN A  23      48.800  44.479  38.475  1.00 22.53           N  
-ATOM     45  CA  GLN A  23      50.009  45.296  38.310  1.00 26.37           C  
-ATOM     46  C   GLN A  23      51.263  44.409  38.378  1.00 27.67           C  
-ATOM     47  O   GLN A  23      51.187  43.347  38.997  1.00 23.66           O  
-ATOM     48  CB  GLN A  23      50.168  46.320  39.400  1.00 31.17           C  
-ATOM     49  CG  GLN A  23      49.159  47.429  39.421  1.00 42.19           C  
-ATOM     50  CD  GLN A  23      49.687  48.673  40.142  1.00 49.58           C  
-ATOM     51  OE1 GLN A  23      50.904  48.913  40.285  1.00 52.36           O  
-ATOM     52  NE2 GLN A  23      48.727  49.492  40.591  1.00 51.67           N  
-ATOM     53  N   ARG A  24      52.431  44.788  37.800  1.00 29.51           N  
-ATOM     54  CA  ARG A  24      53.641  43.953  37.789  1.00 30.30           C  
-ATOM     55  C   ARG A  24      54.183  43.386  39.081  1.00 31.38           C  
-ATOM     56  O   ARG A  24      54.587  42.235  39.151  1.00 34.00           O  
-ATOM     57  CB  ARG A  24      54.840  44.668  37.206  1.00 30.16           C  
-ATOM     58  CG  ARG A  24      54.679  44.883  35.770  1.00 28.35           C  
-ATOM     59  CD  ARG A  24      55.881  45.609  35.209  1.00 27.43           C  
-ATOM     60  NE  ARG A  24      55.515  45.740  33.820  1.00 28.29           N  
-ATOM     61  CZ  ARG A  24      55.724  44.756  32.944  1.00 28.28           C  
-ATOM     62  NH1 ARG A  24      56.320  43.610  33.293  1.00 27.96           N  
-ATOM     63  NH2 ARG A  24      55.172  44.852  31.736  1.00 28.73           N  
-ATOM     64  N   ASN A  25      54.279  44.201  40.117  1.00 32.39           N  
-ATOM     65  CA  ASN A  25      54.869  43.760  41.380  1.00 33.61           C  
-ATOM     66  C   ASN A  25      53.824  43.580  42.473  1.00 31.97           C  
-ATOM     67  O   ASN A  25      54.141  43.602  43.671  1.00 29.55           O  
-ATOM     68  CB  ASN A  25      55.929  44.795  41.809  1.00 37.80           C  
-ATOM     69  CG  ASN A  25      55.409  46.225  41.994  1.00 40.56           C  
-ATOM     70  OD1 ASN A  25      54.300  46.613  41.600  1.00 42.11           O  
-ATOM     71  ND2 ASN A  25      56.249  47.031  42.633  1.00 44.06           N  
-ATOM     72  N   SER A  26      52.568  43.425  42.030  1.00 28.95           N  
-ATOM     73  CA  SER A  26      51.480  43.244  42.956  1.00 27.48           C  
-ATOM     74  C   SER A  26      51.550  41.881  43.640  1.00 24.98           C  
-ATOM     75  O   SER A  26      51.345  41.838  44.862  1.00 24.86           O  
-ATOM     76  CB  SER A  26      50.145  43.400  42.220  1.00 29.77           C  
-ATOM     77  OG  SER A  26      49.576  44.692  42.384  1.00 32.18           O  
-ATOM     78  N   TRP A  27      51.894  40.773  42.943  1.00 19.00           N  
-ATOM     79  CA  TRP A  27      51.827  39.462  43.577  1.00 15.63           C  
-ATOM     80  C   TRP A  27      53.117  38.694  43.339  1.00 13.92           C  
-ATOM     81  O   TRP A  27      53.144  37.728  42.595  1.00 12.13           O  
-ATOM     82  CB  TRP A  27      50.596  38.703  43.019  1.00 11.96           C  
-ATOM     83  CG  TRP A  27      49.263  39.463  43.147  1.00 11.14           C  
-ATOM     84  CD1 TRP A  27      48.655  40.009  42.035  1.00 11.57           C  
-ATOM     85  CD2 TRP A  27      48.540  39.681  44.301  1.00 13.48           C  
-ATOM     86  NE1 TRP A  27      47.556  40.562  42.482  1.00 10.27           N  
-ATOM     87  CE2 TRP A  27      47.439  40.401  43.808  1.00 10.92           C  
-ATOM     88  CE3 TRP A  27      48.623  39.397  45.681  1.00 13.18           C  
-ATOM     89  CZ2 TRP A  27      46.423  40.836  44.680  1.00 10.34           C  
-ATOM     90  CZ3 TRP A  27      47.605  39.840  46.538  1.00 11.90           C  
-ATOM     91  CH2 TRP A  27      46.513  40.551  46.040  1.00 10.77           C  
-ATOM     92  N   PRO A  28      54.229  39.090  43.951  1.00 11.86           N  
-ATOM     93  CA  PRO A  28      55.548  38.663  43.566  1.00 12.64           C  
-ATOM     94  C   PRO A  28      55.962  37.263  44.017  1.00 11.81           C  
-ATOM     95  O   PRO A  28      57.054  36.803  43.660  1.00 11.52           O  
-ATOM     96  CB  PRO A  28      56.413  39.809  44.089  1.00 14.52           C  
-ATOM     97  CG  PRO A  28      55.730  40.196  45.376  1.00 12.82           C  
-ATOM     98  CD  PRO A  28      54.281  40.117  44.984  1.00 11.25           C  
-ATOM     99  N   SER A  29      55.096  36.568  44.781  1.00  9.76           N  
-ATOM    100  CA  SER A  29      55.334  35.159  45.098  1.00  9.96           C  
-ATOM    101  C   SER A  29      54.674  34.231  44.069  1.00  9.91           C  
-ATOM    102  O   SER A  29      54.900  33.017  44.093  1.00  9.94           O  
-ATOM    103  CB  SER A  29      54.789  34.832  46.503  1.00  8.62           C  
-ATOM    104  OG  SER A  29      53.364  34.849  46.566  1.00 12.43           O  
-ATOM    105  N   GLN A  30      53.845  34.765  43.154  1.00  8.00           N  
-ATOM    106  CA  GLN A  30      53.241  33.980  42.087  1.00  8.57           C  
-ATOM    107  C   GLN A  30      54.294  33.417  41.123  1.00 10.02           C  
-ATOM    108  O   GLN A  30      55.207  34.132  40.697  1.00 10.78           O  
-ATOM    109  CB  GLN A  30      52.264  34.846  41.275  1.00 10.17           C  
-ATOM    110  CG  GLN A  30      51.653  34.201  40.027  1.00  8.01           C  
-ATOM    111  CD  GLN A  30      50.507  33.288  40.306  1.00  9.07           C  
-ATOM    112  OE1 GLN A  30      49.469  33.711  40.810  1.00 10.33           O  
-ATOM    113  NE2 GLN A  30      50.621  32.014  39.953  1.00 10.31           N  
-ATOM    114  N   ILE A  31      54.210  32.116  40.793  1.00  8.92           N  
-ATOM    115  CA  ILE A  31      55.088  31.545  39.777  1.00  6.99           C  
-ATOM    116  C   ILE A  31      54.240  30.889  38.673  1.00  7.32           C  
-ATOM    117  O   ILE A  31      53.032  30.629  38.858  1.00  6.13           O  
-ATOM    118  CB  ILE A  31      56.136  30.486  40.429  1.00  9.28           C  
-ATOM    119  CG1 ILE A  31      55.501  29.162  40.903  1.00  7.00           C  
-ATOM    120  CG2 ILE A  31      56.814  31.169  41.627  1.00  8.47           C  
-ATOM    121  CD1 ILE A  31      55.220  28.102  39.818  1.00  8.11           C  
-ATOM    122  N   SER A  32      54.850  30.664  37.482  1.00  8.48           N  
-ATOM    123  CA  SER A  32      54.240  29.916  36.392  1.00  9.14           C  
-ATOM    124  C   SER A  32      54.994  28.595  36.331  1.00  7.06           C  
-ATOM    125  O   SER A  32      56.212  28.571  36.246  1.00  8.01           O  
-ATOM    126  CB  SER A  32      54.410  30.660  35.057  1.00  9.53           C  
-ATOM    127  OG  SER A  32      54.099  29.861  33.919  1.00 10.59           O  
-ATOM    128  N   LEU A  33      54.275  27.494  36.373  1.00  9.59           N  
-ATOM    129  CA  LEU A  33      54.858  26.166  36.265  1.00  9.76           C  
-ATOM    130  C   LEU A  33      54.588  25.764  34.825  1.00 10.03           C  
-ATOM    131  O   LEU A  33      53.451  25.728  34.380  1.00  8.61           O  
-ATOM    132  CB  LEU A  33      54.176  25.127  37.197  1.00 10.56           C  
-ATOM    133  CG  LEU A  33      54.678  23.658  37.079  1.00  9.91           C  
-ATOM    134  CD1 LEU A  33      56.085  23.543  37.617  1.00  7.64           C  
-ATOM    135  CD2 LEU A  33      53.734  22.732  37.820  1.00 12.30           C  
-ATOM    136  N   GLN A  34      55.645  25.383  34.129  1.00 12.13           N  
-ATOM    137  CA  GLN A  34      55.609  25.150  32.694  1.00 13.18           C  
-ATOM    138  C   GLN A  34      56.151  23.795  32.353  1.00 11.91           C  
-ATOM    139  O   GLN A  34      57.055  23.357  33.054  1.00 13.44           O  
-ATOM    140  CB  GLN A  34      56.479  26.194  31.955  1.00 12.93           C  
-ATOM    141  CG  GLN A  34      55.982  27.572  32.291  1.00 12.27           C  
-ATOM    142  CD  GLN A  34      56.605  28.671  31.492  1.00 13.36           C  
-ATOM    143  OE1 GLN A  34      57.616  28.521  30.808  1.00 13.40           O  
-ATOM    144  NE2 GLN A  34      55.926  29.794  31.626  1.00 11.34           N  
-ATOM    145  N   TYR A  35      55.675  23.147  31.306  1.00 11.44           N  
-ATOM    146  CA  TYR A  35      56.313  21.907  30.895  1.00 14.14           C  
-ATOM    147  C   TYR A  35      56.852  22.024  29.466  1.00 14.38           C  
-ATOM    148  O   TYR A  35      56.391  22.859  28.695  1.00 13.75           O  
-ATOM    149  CB  TYR A  35      55.327  20.761  30.987  1.00 13.02           C  
-ATOM    150  CG  TYR A  35      54.128  20.842  30.062  1.00 19.19           C  
-ATOM    151  CD1 TYR A  35      53.089  21.733  30.324  1.00 20.94           C  
-ATOM    152  CD2 TYR A  35      54.087  20.023  28.922  1.00 22.45           C  
-ATOM    153  CE1 TYR A  35      52.006  21.816  29.452  1.00 23.87           C  
-ATOM    154  CE2 TYR A  35      52.999  20.103  28.049  1.00 22.05           C  
-ATOM    155  CZ  TYR A  35      51.964  20.998  28.321  1.00 24.06           C  
-ATOM    156  OH  TYR A  35      50.865  21.061  27.476  1.00 25.35           O  
-ATOM    157  N   ARG A  36      57.832  21.217  29.075  1.00 16.04           N  
-ATOM    158  CA  ARG A  36      58.391  21.298  27.740  1.00 19.73           C  
-ATOM    159  C   ARG A  36      57.462  20.582  26.795  1.00 22.34           C  
-ATOM    160  O   ARG A  36      56.908  19.520  27.036  1.00 22.37           O  
-ATOM    161  CB  ARG A  36      59.757  20.698  27.755  1.00 21.39           C  
-ATOM    162  CG  ARG A  36      60.578  21.142  26.575  1.00 24.73           C  
-ATOM    163  CD  ARG A  36      62.004  20.688  26.765  1.00 30.91           C  
-ATOM    164  NE  ARG A  36      62.103  19.297  27.236  1.00 38.05           N  
-ATOM    165  CZ  ARG A  36      61.826  18.166  26.523  1.00 39.47           C  
-ATOM    166  NH1 ARG A  36      61.391  18.177  25.242  1.00 43.28           N  
-ATOM    167  NH2 ARG A  36      62.026  16.974  27.092  1.00 37.49           N  
-ATOM    168  N   SER A  37      57.147  21.355  25.786  1.00 25.25           N  
-ATOM    169  CA  SER A  37      56.184  20.971  24.794  1.00 32.58           C  
-ATOM    170  C   SER A  37      56.928  21.157  23.477  1.00 37.49           C  
-ATOM    171  O   SER A  37      57.067  22.276  22.947  1.00 38.55           O  
-ATOM    172  CB  SER A  37      55.010  21.909  24.986  1.00 34.35           C  
-ATOM    173  OG  SER A  37      53.918  21.576  24.154  1.00 39.18           O  
-ATOM    174  N   GLY A  38      57.490  20.028  23.009  1.00 39.31           N  
-ATOM    175  CA  GLY A  38      58.282  19.988  21.792  1.00 40.50           C  
-ATOM    176  C   GLY A  38      59.594  20.740  21.968  1.00 42.41           C  
-ATOM    177  O   GLY A  38      60.516  20.339  22.693  1.00 42.97           O  
-ATOM    178  N   SER A  39      59.595  21.879  21.277  1.00 42.87           N  
-ATOM    179  CA  SER A  39      60.731  22.796  21.262  1.00 44.46           C  
-ATOM    180  C   SER A  39      60.594  23.962  22.239  1.00 43.55           C  
-ATOM    181  O   SER A  39      61.551  24.647  22.607  1.00 45.39           O  
-ATOM    182  CB  SER A  39      60.874  23.321  19.850  1.00 47.58           C  
-ATOM    183  OG  SER A  39      59.583  23.585  19.282  1.00 51.23           O  
-ATOM    184  N   SER A  40      59.345  24.174  22.644  1.00 41.15           N  
-ATOM    185  CA  SER A  40      58.971  25.266  23.518  1.00 38.12           C  
-ATOM    186  C   SER A  40      58.493  24.800  24.901  1.00 33.55           C  
-ATOM    187  O   SER A  40      58.634  23.624  25.245  1.00 32.42           O  
-ATOM    188  CB  SER A  40      57.905  26.050  22.768  1.00 40.19           C  
-ATOM    189  OG  SER A  40      56.915  25.159  22.253  1.00 45.65           O  
-ATOM    190  N   TRP A  41      57.967  25.752  25.687  1.00 27.38           N  
-ATOM    191  CA  TRP A  41      57.496  25.523  27.043  1.00 22.42           C  
-ATOM    192  C   TRP A  41      56.114  26.091  27.135  1.00 19.86           C  
-ATOM    193  O   TRP A  41      55.904  27.195  26.677  1.00 21.58           O  
-ATOM    194  CB  TRP A  41      58.348  26.242  28.014  1.00 22.39           C  
-ATOM    195  CG  TRP A  41      59.743  25.673  28.140  1.00 23.61           C  
-ATOM    196  CD1 TRP A  41      60.790  26.138  27.371  1.00 22.48           C  
-ATOM    197  CD2 TRP A  41      60.106  24.685  29.028  1.00 24.55           C  
-ATOM    198  NE1 TRP A  41      61.828  25.437  27.779  1.00 25.26           N  
-ATOM    199  CE2 TRP A  41      61.481  24.564  28.756  1.00 25.15           C  
-ATOM    200  CE3 TRP A  41      59.498  23.894  30.019  1.00 24.05           C  
-ATOM    201  CZ2 TRP A  41      62.247  23.644  29.482  1.00 24.19           C  
-ATOM    202  CZ3 TRP A  41      60.279  22.981  30.736  1.00 21.92           C  
-ATOM    203  CH2 TRP A  41      61.635  22.859  30.471  1.00 23.76           C  
-ATOM    204  N   ALA A  42      55.153  25.389  27.704  1.00 16.35           N  
-ATOM    205  CA  ALA A  42      53.776  25.840  27.824  1.00 15.04           C  
-ATOM    206  C   ALA A  42      53.388  25.995  29.315  1.00 14.44           C  
-ATOM    207  O   ALA A  42      53.767  25.155  30.145  1.00 13.83           O  
-ATOM    208  CB  ALA A  42      52.825  24.815  27.202  1.00 13.91           C  
-ATOM    209  N   HIS A  43      52.632  27.039  29.679  1.00 11.49           N  
-ATOM    210  CA  HIS A  43      52.146  27.185  31.048  1.00 12.37           C  
-ATOM    211  C   HIS A  43      51.090  26.108  31.347  1.00 10.74           C  
-ATOM    212  O   HIS A  43      50.169  25.878  30.566  1.00 11.37           O  
-ATOM    213  CB  HIS A  43      51.548  28.584  31.205  1.00 12.11           C  
-ATOM    214  CG  HIS A  43      50.789  28.830  32.491  1.00 11.84           C  
-ATOM    215  ND1 HIS A  43      51.312  29.320  33.609  1.00 11.21           N  
-ATOM    216  CD2 HIS A  43      49.454  28.549  32.701  1.00 12.94           C  
-ATOM    217  CE1 HIS A  43      50.340  29.340  34.491  1.00 12.11           C  
-ATOM    218  NE2 HIS A  43      49.227  28.879  33.948  1.00 10.55           N  
-ATOM    219  N   THR A  44      51.215  25.400  32.464  1.00  9.11           N  
-ATOM    220  CA  THR A  44      50.175  24.476  32.872  1.00  9.74           C  
-ATOM    221  C   THR A  44      49.510  24.819  34.228  1.00  7.13           C  
-ATOM    222  O   THR A  44      48.329  24.556  34.440  1.00  7.38           O  
-ATOM    223  CB  THR A  44      50.822  23.066  32.851  1.00 10.48           C  
-ATOM    224  OG1 THR A  44      49.727  22.191  32.998  1.00 14.23           O  
-ATOM    225  CG2 THR A  44      51.867  22.787  33.920  1.00 12.75           C  
-ATOM    226  N   CYS A  45      50.235  25.490  35.116  1.00  6.51           N  
-ATOM    227  CA  CYS A  45      49.773  25.700  36.485  1.00  6.29           C  
-ATOM    228  C   CYS A  45      50.423  26.923  37.125  1.00  5.70           C  
-ATOM    229  O   CYS A  45      51.443  27.401  36.620  1.00  4.80           O  
-ATOM    230  CB  CYS A  45      50.122  24.446  37.382  1.00  8.42           C  
-ATOM    231  SG  CYS A  45      48.919  23.107  37.188  1.00 10.15           S  
-ATOM    232  N   GLY A  46      49.794  27.434  38.193  1.00  6.07           N  
-ATOM    233  CA  GLY A  46      50.444  28.450  38.978  1.00  7.86           C  
-ATOM    234  C   GLY A  46      51.105  27.748  40.178  1.00 10.78           C  
-ATOM    235  O   GLY A  46      51.065  26.510  40.318  1.00 11.22           O  
-ATOM    236  N   GLY A  47      51.711  28.548  41.043  1.00  6.54           N  
-ATOM    237  CA  GLY A  47      52.285  28.063  42.289  1.00  6.80           C  
-ATOM    238  C   GLY A  47      52.661  29.272  43.136  1.00  7.93           C  
-ATOM    239  O   GLY A  47      52.493  30.423  42.702  1.00  9.16           O  
-ATOM    240  N   THR A  48      53.219  29.016  44.305  1.00  7.69           N  
-ATOM    241  CA  THR A  48      53.681  30.047  45.215  1.00  8.22           C  
-ATOM    242  C   THR A  48      55.117  29.798  45.606  1.00  9.03           C  
-ATOM    243  O   THR A  48      55.466  28.710  46.049  1.00 10.78           O  
-ATOM    244  CB  THR A  48      52.811  30.066  46.470  1.00 10.32           C  
-ATOM    245  OG1 THR A  48      51.476  30.319  46.073  1.00  9.40           O  
-ATOM    246  CG2 THR A  48      53.206  31.179  47.448  1.00  9.14           C  
-ATOM    247  N   LEU A  49      56.018  30.767  45.471  1.00  9.93           N  
-ATOM    248  CA  LEU A  49      57.386  30.650  45.934  1.00 10.04           C  
-ATOM    249  C   LEU A  49      57.389  30.698  47.474  1.00 10.76           C  
-ATOM    250  O   LEU A  49      56.894  31.661  48.042  1.00  9.70           O  
-ATOM    251  CB  LEU A  49      58.216  31.805  45.323  1.00  9.80           C  
-ATOM    252  CG  LEU A  49      59.709  31.758  45.631  1.00 12.10           C  
-ATOM    253  CD1 LEU A  49      60.337  30.629  44.818  1.00 10.75           C  
-ATOM    254  CD2 LEU A  49      60.348  33.111  45.320  1.00 12.86           C  
-ATOM    255  N   ILE A  50      57.843  29.663  48.187  1.00 10.28           N  
-ATOM    256  CA  ILE A  50      57.774  29.700  49.641  1.00 11.21           C  
-ATOM    257  C   ILE A  50      59.150  29.768  50.263  1.00 10.60           C  
-ATOM    258  O   ILE A  50      59.280  30.150  51.428  1.00 11.17           O  
-ATOM    259  CB  ILE A  50      57.008  28.470  50.241  1.00 10.84           C  
-ATOM    260  CG1 ILE A  50      57.635  27.146  49.819  1.00 12.83           C  
-ATOM    261  CG2 ILE A  50      55.545  28.694  49.943  1.00  8.94           C  
-ATOM    262  CD1 ILE A  50      56.887  25.953  50.437  1.00 19.56           C  
-ATOM    263  N   ARG A  51      60.179  29.331  49.538  1.00 11.39           N  
-ATOM    264  CA  ARG A  51      61.572  29.479  49.921  1.00 14.84           C  
-ATOM    265  C   ARG A  51      62.311  29.843  48.642  1.00 14.15           C  
-ATOM    266  O   ARG A  51      61.754  29.654  47.574  1.00 15.83           O  
-ATOM    267  CB  ARG A  51      62.252  28.189  50.447  1.00 15.49           C  
-ATOM    268  CG  ARG A  51      61.749  27.603  51.730  1.00 20.57           C  
-ATOM    269  CD  ARG A  51      61.836  28.700  52.749  1.00 26.75           C  
-ATOM    270  NE  ARG A  51      61.483  28.198  54.067  1.00 36.70           N  
-ATOM    271  CZ  ARG A  51      60.229  28.103  54.521  1.00 40.23           C  
-ATOM    272  NH1 ARG A  51      59.155  28.467  53.810  1.00 44.96           N  
-ATOM    273  NH2 ARG A  51      60.048  27.549  55.715  1.00 45.37           N  
-ATOM    274  N   GLN A  52      63.559  30.313  48.677  1.00 14.77           N  
-ATOM    275  CA  GLN A  52      64.315  30.613  47.475  1.00 17.69           C  
-ATOM    276  C   GLN A  52      64.508  29.415  46.557  1.00 17.94           C  
-ATOM    277  O   GLN A  52      64.717  29.568  45.362  1.00 16.30           O  
-ATOM    278  CB  GLN A  52      65.684  31.156  47.836  1.00 22.60           C  
-ATOM    279  CG  GLN A  52      65.565  32.611  48.259  1.00 31.18           C  
-ATOM    280  CD  GLN A  52      66.887  33.323  48.580  1.00 38.73           C  
-ATOM    281  OE1 GLN A  52      67.126  33.760  49.719  1.00 43.53           O  
-ATOM    282  NE2 GLN A  52      67.782  33.472  47.599  1.00 39.25           N  
-ATOM    283  N   ASN A  53      64.408  28.203  47.090  1.00 15.33           N  
-ATOM    284  CA  ASN A  53      64.510  27.011  46.265  1.00 16.68           C  
-ATOM    285  C   ASN A  53      63.330  26.053  46.454  1.00 14.98           C  
-ATOM    286  O   ASN A  53      63.459  24.884  46.119  1.00 13.92           O  
-ATOM    287  CB  ASN A  53      65.830  26.296  46.572  1.00 17.35           C  
-ATOM    288  CG  ASN A  53      66.052  25.916  48.036  1.00 18.96           C  
-ATOM    289  OD1 ASN A  53      66.934  25.116  48.326  1.00 24.48           O  
-ATOM    290  ND2 ASN A  53      65.351  26.389  49.059  1.00 19.62           N  
-ATOM    291  N   TRP A  54      62.187  26.485  47.000  1.00 11.60           N  
-ATOM    292  CA  TRP A  54      61.013  25.626  47.134  1.00 11.68           C  
-ATOM    293  C   TRP A  54      59.781  26.386  46.654  1.00 10.70           C  
-ATOM    294  O   TRP A  54      59.648  27.594  46.913  1.00 11.59           O  
-ATOM    295  CB  TRP A  54      60.775  25.158  48.617  1.00 11.66           C  
-ATOM    296  CG  TRP A  54      61.683  24.023  49.131  1.00 14.01           C  
-ATOM    297  CD1 TRP A  54      62.831  24.286  49.837  1.00 16.95           C  
-ATOM    298  CD2 TRP A  54      61.487  22.654  48.953  1.00 16.32           C  
-ATOM    299  NE1 TRP A  54      63.376  23.106  50.101  1.00 17.14           N  
-ATOM    300  CE2 TRP A  54      62.619  22.108  49.598  1.00 16.55           C  
-ATOM    301  CE3 TRP A  54      60.541  21.809  48.355  1.00 14.98           C  
-ATOM    302  CZ2 TRP A  54      62.823  20.732  49.657  1.00 14.78           C  
-ATOM    303  CZ3 TRP A  54      60.753  20.430  48.420  1.00 18.60           C  
-ATOM    304  CH2 TRP A  54      61.880  19.901  49.063  1.00 16.24           C  
-ATOM    305  N   VAL A  55      58.943  25.673  45.877  1.00  9.81           N  
-ATOM    306  CA  VAL A  55      57.666  26.154  45.334  1.00 10.27           C  
-ATOM    307  C   VAL A  55      56.517  25.268  45.825  1.00 10.57           C  
-ATOM    308  O   VAL A  55      56.636  24.045  45.875  1.00 11.53           O  
-ATOM    309  CB  VAL A  55      57.697  26.160  43.748  1.00 11.35           C  
-ATOM    310  CG1 VAL A  55      56.318  26.081  43.062  1.00 11.56           C  
-ATOM    311  CG2 VAL A  55      58.243  27.503  43.327  1.00 10.32           C  
-ATOM    312  N   MET A  56      55.386  25.846  46.219  1.00  8.66           N  
-ATOM    313  CA  MET A  56      54.227  25.076  46.603  1.00  7.44           C  
-ATOM    314  C   MET A  56      53.219  25.081  45.458  1.00 10.16           C  
-ATOM    315  O   MET A  56      52.927  26.154  44.924  1.00  9.25           O  
-ATOM    316  CB  MET A  56      53.670  25.703  47.875  1.00  9.29           C  
-ATOM    317  CG  MET A  56      52.377  25.079  48.372  1.00 10.71           C  
-ATOM    318  SD  MET A  56      51.700  25.886  49.852  1.00 13.02           S  
-ATOM    319  CE  MET A  56      51.288  27.566  49.430  1.00  9.38           C  
-ATOM    320  N   THR A  57      52.628  23.952  45.055  1.00  8.68           N  
-ATOM    321  CA  THR A  57      51.655  23.921  43.955  1.00  6.91           C  
-ATOM    322  C   THR A  57      50.646  22.812  44.262  1.00  7.86           C  
-ATOM    323  O   THR A  57      50.679  22.256  45.374  1.00  7.97           O  
-ATOM    324  CB  THR A  57      52.436  23.702  42.597  1.00  5.11           C  
-ATOM    325  OG1 THR A  57      51.496  23.956  41.567  1.00  5.03           O  
-ATOM    326  CG2 THR A  57      52.996  22.303  42.379  1.00  5.45           C  
-ATOM    327  N   ALA A  58      49.721  22.481  43.359  1.00  8.02           N  
-ATOM    328  CA  ALA A  58      48.786  21.380  43.583  1.00  8.76           C  
-ATOM    329  C   ALA A  58      49.418  20.058  43.095  1.00 10.42           C  
-ATOM    330  O   ALA A  58      50.202  20.041  42.128  1.00  8.70           O  
-ATOM    331  CB  ALA A  58      47.485  21.629  42.817  1.00  7.33           C  
-ATOM    332  N   ALA A  59      49.157  18.938  43.792  1.00  9.16           N  
-ATOM    333  CA  ALA A  59      49.627  17.641  43.341  1.00  8.74           C  
-ATOM    334  C   ALA A  59      49.083  17.230  41.957  1.00  9.94           C  
-ATOM    335  O   ALA A  59      49.797  16.613  41.149  1.00  9.40           O  
-ATOM    336  CB  ALA A  59      49.212  16.591  44.328  1.00  9.97           C  
-ATOM    337  N   HIS A  60      47.853  17.606  41.585  1.00  9.12           N  
-ATOM    338  CA  HIS A  60      47.349  17.225  40.272  1.00 10.21           C  
-ATOM    339  C   HIS A  60      48.119  17.919  39.140  1.00  9.84           C  
-ATOM    340  O   HIS A  60      48.018  17.452  38.006  1.00 10.59           O  
-ATOM    341  CB  HIS A  60      45.823  17.534  40.124  1.00  9.52           C  
-ATOM    342  CG  HIS A  60      45.355  18.977  39.952  1.00 12.03           C  
-ATOM    343  ND1 HIS A  60      44.765  19.764  40.861  1.00 13.28           N  
-ATOM    344  CD2 HIS A  60      45.448  19.698  38.779  1.00 11.66           C  
-ATOM    345  CE1 HIS A  60      44.505  20.915  40.306  1.00 12.79           C  
-ATOM    346  NE2 HIS A  60      44.916  20.850  39.061  1.00 13.95           N  
-ATOM    347  N   CYS A  61      48.885  18.995  39.406  1.00  7.85           N  
-ATOM    348  CA  CYS A  61      49.713  19.651  38.388  1.00  9.63           C  
-ATOM    349  C   CYS A  61      50.914  18.793  37.965  1.00 11.75           C  
-ATOM    350  O   CYS A  61      51.460  18.975  36.873  1.00 11.07           O  
-ATOM    351  CB  CYS A  61      50.279  20.995  38.878  1.00  9.53           C  
-ATOM    352  SG  CYS A  61      48.981  22.231  39.006  1.00  9.56           S  
-ATOM    353  N   VAL A  62      51.372  17.885  38.838  1.00 11.98           N  
-ATOM    354  CA  VAL A  62      52.538  17.079  38.543  1.00 13.47           C  
-ATOM    355  C   VAL A  62      52.177  15.599  38.430  1.00 14.50           C  
-ATOM    356  O   VAL A  62      53.049  14.733  38.528  1.00 15.98           O  
-ATOM    357  CB  VAL A  62      53.637  17.283  39.615  1.00 14.34           C  
-ATOM    358  CG1 VAL A  62      54.198  18.694  39.437  1.00 14.68           C  
-ATOM    359  CG2 VAL A  62      53.117  17.128  41.041  1.00 15.60           C  
-ATOM    360  N   ASP A  63      50.899  15.278  38.187  1.00 14.73           N  
-ATOM    361  CA  ASP A  63      50.545  13.889  37.961  1.00 19.22           C  
-ATOM    362  C   ASP A  63      51.208  13.313  36.716  1.00 20.60           C  
-ATOM    363  O   ASP A  63      51.656  12.159  36.748  1.00 22.54           O  
-ATOM    364  CB  ASP A  63      49.029  13.724  37.841  1.00 18.62           C  
-ATOM    365  CG  ASP A  63      48.279  13.565  39.174  1.00 18.39           C  
-ATOM    366  OD1 ASP A  63      48.843  13.089  40.164  1.00 18.09           O  
-ATOM    367  OD2 ASP A  63      47.100  13.916  39.199  1.00 18.27           O  
-ATOM    368  N   ARG A  64      51.318  14.065  35.615  1.00 20.95           N  
-ATOM    369  CA  ARG A  64      52.016  13.547  34.448  1.00 21.05           C  
-ATOM    370  C   ARG A  64      53.499  13.775  34.581  1.00 20.06           C  
-ATOM    371  O   ARG A  64      53.971  14.823  35.033  1.00 22.98           O  
-ATOM    372  CB  ARG A  64      51.526  14.202  33.157  1.00 25.12           C  
-ATOM    373  CG  ARG A  64      50.231  13.593  32.567  1.00 34.24           C  
-ATOM    374  CD  ARG A  64      50.160  12.057  32.234  1.00 44.22           C  
-ATOM    375  NE  ARG A  64      51.129  11.521  31.257  1.00 53.66           N  
-ATOM    376  CZ  ARG A  64      50.832  11.172  29.978  1.00 57.48           C  
-ATOM    377  NH1 ARG A  64      49.601  11.283  29.442  1.00 58.71           N  
-ATOM    378  NH2 ARG A  64      51.800  10.675  29.203  1.00 57.72           N  
-ATOM    379  N   GLU A  65      54.238  12.753  34.165  1.00 17.07           N  
-ATOM    380  CA  GLU A  65      55.679  12.742  34.250  1.00 17.82           C  
-ATOM    381  C   GLU A  65      56.333  13.452  33.078  1.00 19.64           C  
-ATOM    382  O   GLU A  65      56.778  12.820  32.122  1.00 20.83           O  
-ATOM    383  CB  GLU A  65      56.143  11.299  34.335  1.00 18.50           C  
-ATOM    384  CG  GLU A  65      55.616  10.706  35.633  1.00 20.29           C  
-ATOM    385  CD  GLU A  65      56.362   9.473  36.085  1.00 17.04           C  
-ATOM    386  OE1 GLU A  65      57.553   9.583  36.382  1.00 17.50           O  
-ATOM    387  OE2 GLU A  65      55.729   8.427  36.140  1.00 19.42           O  
-ATOM    388  N   LEU A  66      56.420  14.785  33.220  1.00 15.92           N  
-ATOM    389  CA  LEU A  66      56.848  15.716  32.176  1.00 15.64           C  
-ATOM    390  C   LEU A  66      58.095  16.424  32.660  1.00 16.72           C  
-ATOM    391  O   LEU A  66      58.454  16.286  33.833  1.00 16.69           O  
-ATOM    392  CB  LEU A  66      55.757  16.768  31.946  1.00 17.74           C  
-ATOM    393  CG  LEU A  66      54.328  16.332  31.660  1.00 18.78           C  
-ATOM    394  CD1 LEU A  66      53.378  17.487  31.846  1.00 21.80           C  
-ATOM    395  CD2 LEU A  66      54.222  15.831  30.257  1.00 20.48           C  
-ATOM    396  N   THR A  67      58.774  17.160  31.774  1.00 13.72           N  
-ATOM    397  CA  THR A  67      59.883  18.010  32.146  1.00 15.03           C  
-ATOM    398  C   THR A  67      59.310  19.379  32.563  1.00 15.54           C  
-ATOM    399  O   THR A  67      58.695  20.086  31.764  1.00 16.15           O  
-ATOM    400  CB  THR A  67      60.871  18.249  30.983  1.00 16.91           C  
-ATOM    401  OG1 THR A  67      61.456  17.006  30.642  1.00 19.43           O  
-ATOM    402  CG2 THR A  67      61.986  19.202  31.361  1.00 16.06           C  
-ATOM    403  N   PHE A  68      59.563  19.798  33.809  1.00 14.23           N  
-ATOM    404  CA  PHE A  68      58.984  21.009  34.356  1.00 12.00           C  
-ATOM    405  C   PHE A  68      60.057  22.023  34.658  1.00 11.66           C  
-ATOM    406  O   PHE A  68      61.182  21.699  35.038  1.00 12.35           O  
-ATOM    407  CB  PHE A  68      58.227  20.727  35.660  1.00 10.94           C  
-ATOM    408  CG  PHE A  68      56.966  19.891  35.537  1.00 10.22           C  
-ATOM    409  CD1 PHE A  68      55.824  20.423  34.932  1.00 10.34           C  
-ATOM    410  CD2 PHE A  68      56.952  18.589  36.055  1.00 13.17           C  
-ATOM    411  CE1 PHE A  68      54.669  19.641  34.855  1.00 12.14           C  
-ATOM    412  CE2 PHE A  68      55.785  17.811  35.969  1.00  8.93           C  
-ATOM    413  CZ  PHE A  68      54.648  18.339  35.372  1.00 12.34           C  
-ATOM    414  N   ARG A  69      59.656  23.281  34.477  1.00 11.68           N  
-ATOM    415  CA  ARG A  69      60.474  24.403  34.916  1.00 11.50           C  
-ATOM    416  C   ARG A  69      59.529  25.414  35.583  1.00  8.81           C  
-ATOM    417  O   ARG A  69      58.320  25.415  35.394  1.00 10.24           O  
-ATOM    418  CB  ARG A  69      61.213  25.098  33.743  1.00 11.76           C  
-ATOM    419  CG  ARG A  69      60.364  25.979  32.846  1.00 14.86           C  
-ATOM    420  CD  ARG A  69      61.293  26.707  31.895  1.00 16.28           C  
-ATOM    421  NE  ARG A  69      60.420  27.583  31.120  1.00 19.92           N  
-ATOM    422  CZ  ARG A  69      60.875  28.394  30.165  1.00 21.52           C  
-ATOM    423  NH1 ARG A  69      62.162  28.451  29.840  1.00 20.39           N  
-ATOM    424  NH2 ARG A  69      60.016  29.192  29.543  1.00 20.72           N  
-ATOM    425  N   VAL A  70      60.129  26.315  36.347  1.00 11.12           N  
-ATOM    426  CA  VAL A  70      59.422  27.336  37.099  1.00 10.60           C  
-ATOM    427  C   VAL A  70      59.950  28.655  36.558  1.00  9.31           C  
-ATOM    428  O   VAL A  70      61.156  28.828  36.334  1.00 10.93           O  
-ATOM    429  CB  VAL A  70      59.753  27.097  38.634  1.00  9.18           C  
-ATOM    430  CG1 VAL A  70      59.743  28.373  39.455  1.00 13.34           C  
-ATOM    431  CG2 VAL A  70      58.721  26.109  39.166  1.00  6.24           C  
-ATOM    432  N   VAL A  71      58.992  29.549  36.368  1.00  8.89           N  
-ATOM    433  CA  VAL A  71      59.338  30.909  36.017  1.00 11.93           C  
-ATOM    434  C   VAL A  71      58.852  31.852  37.120  1.00 11.92           C  
-ATOM    435  O   VAL A  71      57.655  31.937  37.432  1.00 12.15           O  
-ATOM    436  CB  VAL A  71      58.702  31.317  34.647  1.00 14.02           C  
-ATOM    437  CG1 VAL A  71      59.272  32.677  34.251  1.00 10.96           C  
-ATOM    438  CG2 VAL A  71      59.011  30.289  33.563  1.00 13.43           C  
-ATOM    439  N   VAL A  72      59.804  32.566  37.744  1.00 13.18           N  
-ATOM    440  CA  VAL A  72      59.451  33.594  38.734  1.00 12.34           C  
-ATOM    441  C   VAL A  72      59.636  34.991  38.089  1.00 14.36           C  
-ATOM    442  O   VAL A  72      60.312  35.152  37.048  1.00 13.27           O  
-ATOM    443  CB  VAL A  72      60.327  33.453  40.043  1.00 11.92           C  
-ATOM    444  CG1 VAL A  72      60.168  32.062  40.595  1.00 12.55           C  
-ATOM    445  CG2 VAL A  72      61.794  33.651  39.807  1.00 11.27           C  
-ATOM    446  N   GLY A  73      58.974  36.008  38.646  1.00 11.87           N  
-ATOM    447  CA  GLY A  73      59.073  37.371  38.121  1.00 14.08           C  
-ATOM    448  C   GLY A  73      58.387  37.512  36.773  1.00 15.09           C  
-ATOM    449  O   GLY A  73      58.735  38.353  35.952  1.00 13.12           O  
-ATOM    450  N   GLU A  74      57.377  36.673  36.557  1.00 14.89           N  
-ATOM    451  CA  GLU A  74      56.680  36.658  35.300  1.00 15.18           C  
-ATOM    452  C   GLU A  74      55.441  37.519  35.345  1.00 15.13           C  
-ATOM    453  O   GLU A  74      54.729  37.580  36.343  1.00 15.30           O  
-ATOM    454  CB  GLU A  74      56.305  35.201  34.918  1.00 15.63           C  
-ATOM    455  CG  GLU A  74      55.658  34.857  33.578  1.00 14.24           C  
-ATOM    456  CD  GLU A  74      56.448  35.409  32.404  1.00 17.13           C  
-ATOM    457  OE1 GLU A  74      56.479  36.597  32.299  1.00 16.38           O  
-ATOM    458  OE2 GLU A  74      57.040  34.708  31.606  1.00 19.38           O  
-ATOM    459  N   HIS A  75      55.228  38.237  34.232  1.00 15.92           N  
-ATOM    460  CA  HIS A  75      53.987  38.963  34.068  1.00 14.16           C  
-ATOM    461  C   HIS A  75      53.300  38.688  32.718  1.00 15.24           C  
-ATOM    462  O   HIS A  75      52.114  38.343  32.754  1.00 13.71           O  
-ATOM    463  CB  HIS A  75      54.285  40.426  34.247  1.00 16.58           C  
-ATOM    464  CG  HIS A  75      53.004  41.234  34.238  1.00 18.47           C  
-ATOM    465  ND1 HIS A  75      52.022  41.152  35.121  1.00 19.99           N  
-ATOM    466  CD2 HIS A  75      52.667  42.159  33.285  1.00 19.29           C  
-ATOM    467  CE1 HIS A  75      51.097  41.991  34.744  1.00 21.94           C  
-ATOM    468  NE2 HIS A  75      51.491  42.588  33.645  1.00 23.35           N  
-ATOM    469  N   ASN A  76      53.936  38.875  31.533  1.00 12.62           N  
-ATOM    470  CA  ASN A  76      53.282  38.553  30.275  1.00 12.88           C  
-ATOM    471  C   ASN A  76      53.830  37.233  29.786  1.00 13.49           C  
-ATOM    472  O   ASN A  76      55.021  37.202  29.520  1.00 14.57           O  
-ATOM    473  CB  ASN A  76      53.557  39.636  29.227  1.00 14.38           C  
-ATOM    474  CG  ASN A  76      52.816  39.356  27.917  1.00 16.99           C  
-ATOM    475  OD1 ASN A  76      52.985  38.314  27.303  1.00 18.07           O  
-ATOM    476  ND2 ASN A  76      51.957  40.205  27.375  1.00 18.06           N  
-ATOM    477  N   LEU A  77      53.074  36.138  29.618  1.00 13.10           N  
-ATOM    478  CA  LEU A  77      53.654  34.856  29.191  1.00 16.26           C  
-ATOM    479  C   LEU A  77      54.349  34.840  27.835  1.00 18.78           C  
-ATOM    480  O   LEU A  77      55.335  34.135  27.607  1.00 16.87           O  
-ATOM    481  CB  LEU A  77      52.587  33.746  29.171  1.00 12.97           C  
-ATOM    482  CG  LEU A  77      52.036  33.309  30.510  1.00 12.19           C  
-ATOM    483  CD1 LEU A  77      50.886  32.342  30.314  1.00 10.63           C  
-ATOM    484  CD2 LEU A  77      53.160  32.685  31.334  1.00 11.40           C  
-ATOM    485  N   ASN A  78      53.889  35.718  26.964  1.00 22.18           N  
-ATOM    486  CA  ASN A  78      54.380  35.717  25.614  1.00 27.02           C  
-ATOM    487  C   ASN A  78      55.407  36.791  25.304  1.00 29.22           C  
-ATOM    488  O   ASN A  78      55.888  36.812  24.167  1.00 31.27           O  
-ATOM    489  CB  ASN A  78      53.136  35.808  24.724  1.00 30.95           C  
-ATOM    490  CG  ASN A  78      52.153  34.665  24.993  1.00 34.09           C  
-ATOM    491  OD1 ASN A  78      51.008  34.856  25.420  1.00 36.04           O  
-ATOM    492  ND2 ASN A  78      52.594  33.422  24.807  1.00 35.73           N  
-ATOM    493  N   GLN A  79      55.796  37.686  26.230  1.00 29.09           N  
-ATOM    494  CA  GLN A  79      56.730  38.787  25.929  1.00 27.70           C  
-ATOM    495  C   GLN A  79      57.879  38.885  26.904  1.00 26.60           C  
-ATOM    496  O   GLN A  79      57.615  38.583  28.052  1.00 20.79           O  
-ATOM    497  CB  GLN A  79      56.043  40.128  25.981  1.00 31.97           C  
-ATOM    498  CG  GLN A  79      55.124  40.432  24.818  1.00 40.38           C  
-ATOM    499  CD  GLN A  79      54.257  41.660  25.083  1.00 45.18           C  
-ATOM    500  OE1 GLN A  79      54.605  42.525  25.898  1.00 49.79           O  
-ATOM    501  NE2 GLN A  79      53.099  41.765  24.418  1.00 45.59           N  
-ATOM    502  N   ASN A  80      59.125  39.256  26.607  1.00 24.38           N  
-ATOM    503  CA  ASN A  80      60.093  39.436  27.672  1.00 26.13           C  
-ATOM    504  C   ASN A  80      59.733  40.691  28.492  1.00 24.82           C  
-ATOM    505  O   ASN A  80      59.459  41.770  27.975  1.00 24.22           O  
-ATOM    506  CB  ASN A  80      61.525  39.577  27.110  1.00 31.06           C  
-ATOM    507  CG  ASN A  80      62.609  39.916  28.160  1.00 36.12           C  
-ATOM    508  OD1 ASN A  80      62.814  39.231  29.174  1.00 37.74           O  
-ATOM    509  ND2 ASN A  80      63.332  41.026  27.967  1.00 40.37           N  
-ATOM    510  N   ASN A  81      59.733  40.517  29.813  1.00 20.88           N  
-ATOM    511  CA  ASN A  81      59.400  41.570  30.751  1.00 20.77           C  
-ATOM    512  C   ASN A  81      60.699  42.125  31.344  1.00 18.80           C  
-ATOM    513  O   ASN A  81      60.704  43.163  31.979  1.00 19.83           O  
-ATOM    514  CB  ASN A  81      58.474  40.983  31.844  1.00 19.80           C  
-ATOM    515  CG  ASN A  81      57.062  40.605  31.402  1.00 20.20           C  
-ATOM    516  OD1 ASN A  81      56.685  39.438  31.377  1.00 20.33           O  
-ATOM    517  ND2 ASN A  81      56.187  41.530  31.047  1.00 19.34           N  
-ATOM    518  N   GLY A  82      61.862  41.502  31.165  1.00 18.50           N  
-ATOM    519  CA  GLY A  82      63.105  41.965  31.737  1.00 17.86           C  
-ATOM    520  C   GLY A  82      63.188  41.609  33.213  1.00 19.09           C  
-ATOM    521  O   GLY A  82      64.088  42.084  33.890  1.00 20.72           O  
-ATOM    522  N   THR A  83      62.286  40.781  33.764  1.00 19.40           N  
-ATOM    523  CA  THR A  83      62.275  40.417  35.187  1.00 19.01           C  
-ATOM    524  C   THR A  83      62.283  38.924  35.505  1.00 18.98           C  
-ATOM    525  O   THR A  83      62.373  38.506  36.664  1.00 19.69           O  
-ATOM    526  CB  THR A  83      61.045  41.054  35.821  1.00 16.10           C  
-ATOM    527  OG1 THR A  83      59.922  40.569  35.104  1.00 14.11           O  
-ATOM    528  CG2 THR A  83      61.070  42.588  35.751  1.00 16.91           C  
-ATOM    529  N   GLU A  84      62.245  38.082  34.466  1.00 17.88           N  
-ATOM    530  CA  GLU A  84      62.045  36.648  34.637  1.00 14.65           C  
-ATOM    531  C   GLU A  84      63.292  35.900  35.014  1.00 13.47           C  
-ATOM    532  O   GLU A  84      64.387  36.258  34.588  1.00 13.80           O  
-ATOM    533  CB  GLU A  84      61.499  35.997  33.363  1.00 12.10           C  
-ATOM    534  CG  GLU A  84      60.237  36.570  32.736  1.00 14.64           C  
-ATOM    535  CD  GLU A  84      60.445  37.752  31.775  1.00 16.56           C  
-ATOM    536  OE1 GLU A  84      61.402  38.528  31.859  1.00 15.47           O  
-ATOM    537  OE2 GLU A  84      59.621  37.917  30.905  1.00 16.61           O  
-ATOM    538  N   GLN A  85      63.147  34.915  35.913  1.00 12.34           N  
-ATOM    539  CA  GLN A  85      64.221  33.966  36.198  1.00 12.18           C  
-ATOM    540  C   GLN A  85      63.605  32.598  35.922  1.00 13.70           C  
-ATOM    541  O   GLN A  85      62.467  32.345  36.316  1.00 13.20           O  
-ATOM    542  CB  GLN A  85      64.674  34.008  37.637  1.00 14.90           C  
-ATOM    543  CG  GLN A  85      65.380  35.285  38.054  1.00 17.26           C  
-ATOM    544  CD  GLN A  85      65.518  35.351  39.570  1.00 20.93           C  
-ATOM    545  OE1 GLN A  85      66.202  34.524  40.171  1.00 22.56           O  
-ATOM    546  NE2 GLN A  85      64.883  36.312  40.242  1.00 20.29           N  
-ATOM    547  N   TYR A  86      64.354  31.744  35.217  1.00 14.34           N  
-ATOM    548  CA  TYR A  86      63.891  30.436  34.741  1.00 16.35           C  
-ATOM    549  C   TYR A  86      64.717  29.364  35.424  1.00 16.89           C  
-ATOM    550  O   TYR A  86      65.946  29.361  35.275  1.00 18.78           O  
-ATOM    551  CB  TYR A  86      64.096  30.294  33.259  1.00 16.32           C  
-ATOM    552  CG  TYR A  86      63.416  31.357  32.429  1.00 19.72           C  
-ATOM    553  CD1 TYR A  86      62.099  31.182  32.060  1.00 18.48           C  
-ATOM    554  CD2 TYR A  86      64.098  32.516  32.052  1.00 20.37           C  
-ATOM    555  CE1 TYR A  86      61.448  32.162  31.315  1.00 20.31           C  
-ATOM    556  CE2 TYR A  86      63.451  33.499  31.301  1.00 19.67           C  
-ATOM    557  CZ  TYR A  86      62.128  33.308  30.944  1.00 20.73           C  
-ATOM    558  OH  TYR A  86      61.442  34.288  30.249  1.00 27.36           O  
-ATOM    559  N   VAL A  87      64.095  28.450  36.183  1.00 15.67           N  
-ATOM    560  CA  VAL A  87      64.884  27.451  36.906  1.00 15.58           C  
-ATOM    561  C   VAL A  87      64.223  26.079  36.822  1.00 14.33           C  
-ATOM    562  O   VAL A  87      63.008  25.999  36.714  1.00 12.05           O  
-ATOM    563  CB  VAL A  87      65.089  27.968  38.386  1.00 15.09           C  
-ATOM    564  CG1 VAL A  87      63.770  28.218  39.073  1.00 17.81           C  
-ATOM    565  CG2 VAL A  87      65.878  26.938  39.180  1.00 14.82           C  
-ATOM    566  N   GLY A  88      65.029  25.001  36.778  1.00 15.60           N  
-ATOM    567  CA  GLY A  88      64.545  23.626  36.675  1.00 15.91           C  
-ATOM    568  C   GLY A  88      64.036  23.095  38.002  1.00 15.26           C  
-ATOM    569  O   GLY A  88      64.387  23.586  39.078  1.00 13.64           O  
-ATOM    570  N   VAL A  89      63.131  22.124  37.918  1.00 14.94           N  
-ATOM    571  CA  VAL A  89      62.621  21.446  39.101  1.00 16.34           C  
-ATOM    572  C   VAL A  89      63.521  20.237  39.296  1.00 19.56           C  
-ATOM    573  O   VAL A  89      63.700  19.406  38.406  1.00 21.89           O  
-ATOM    574  CB  VAL A  89      61.175  21.005  38.884  1.00 11.51           C  
-ATOM    575  CG1 VAL A  89      60.647  20.192  40.048  1.00 13.75           C  
-ATOM    576  CG2 VAL A  89      60.328  22.252  38.793  1.00  9.94           C  
-ATOM    577  N   GLN A  90      64.189  20.204  40.429  1.00 20.26           N  
-ATOM    578  CA  GLN A  90      65.034  19.096  40.765  1.00 22.28           C  
-ATOM    579  C   GLN A  90      64.294  17.969  41.535  1.00 24.14           C  
-ATOM    580  O   GLN A  90      64.680  16.807  41.382  1.00 25.96           O  
-ATOM    581  CB  GLN A  90      66.142  19.683  41.550  1.00 23.58           C  
-ATOM    582  CG  GLN A  90      67.113  18.705  42.144  1.00 30.44           C  
-ATOM    583  CD  GLN A  90      68.064  19.491  43.008  1.00 33.80           C  
-ATOM    584  OE1 GLN A  90      67.753  19.879  44.134  1.00 36.82           O  
-ATOM    585  NE2 GLN A  90      69.237  19.779  42.454  1.00 36.91           N  
-ATOM    586  N   LYS A  91      63.262  18.187  42.371  1.00 20.69           N  
-ATOM    587  CA  LYS A  91      62.648  17.102  43.128  1.00 18.40           C  
-ATOM    588  C   LYS A  91      61.197  17.458  43.376  1.00 17.81           C  
-ATOM    589  O   LYS A  91      60.920  18.610  43.681  1.00 17.02           O  
-ATOM    590  CB  LYS A  91      63.404  16.948  44.427  1.00 20.25           C  
-ATOM    591  CG  LYS A  91      62.840  15.904  45.357  1.00 26.29           C  
-ATOM    592  CD  LYS A  91      63.591  15.895  46.677  1.00 29.77           C  
-ATOM    593  CE  LYS A  91      63.339  14.527  47.326  1.00 32.95           C  
-ATOM    594  NZ  LYS A  91      64.038  13.442  46.641  1.00 36.98           N  
-ATOM    595  N   ILE A  92      60.266  16.514  43.214  1.00 14.26           N  
-ATOM    596  CA  ILE A  92      58.838  16.726  43.403  1.00 16.37           C  
-ATOM    597  C   ILE A  92      58.401  15.863  44.592  1.00 16.51           C  
-ATOM    598  O   ILE A  92      58.598  14.641  44.563  1.00 17.95           O  
-ATOM    599  CB  ILE A  92      58.097  16.311  42.112  1.00 15.64           C  
-ATOM    600  CG1 ILE A  92      58.510  17.276  40.968  1.00 16.74           C  
-ATOM    601  CG2 ILE A  92      56.580  16.304  42.348  1.00 14.98           C  
-ATOM    602  CD1 ILE A  92      57.997  16.971  39.532  1.00 20.78           C  
-ATOM    603  N   VAL A  93      57.797  16.491  45.617  1.00 13.52           N  
-ATOM    604  CA  VAL A  93      57.362  15.804  46.824  1.00 12.48           C  
-ATOM    605  C   VAL A  93      55.886  16.028  46.841  1.00 12.62           C  
-ATOM    606  O   VAL A  93      55.421  17.117  47.128  1.00 14.90           O  
-ATOM    607  CB  VAL A  93      58.034  16.409  48.107  1.00  8.83           C  
-ATOM    608  CG1 VAL A  93      57.629  15.621  49.341  1.00  9.55           C  
-ATOM    609  CG2 VAL A  93      59.555  16.361  47.987  1.00 10.27           C  
-ATOM    610  N   VAL A  94      55.103  15.022  46.489  1.00 12.74           N  
-ATOM    611  CA  VAL A  94      53.657  15.132  46.518  1.00 13.20           C  
-ATOM    612  C   VAL A  94      53.193  14.687  47.910  1.00 14.69           C  
-ATOM    613  O   VAL A  94      53.896  13.885  48.542  1.00 12.47           O  
-ATOM    614  CB  VAL A  94      53.061  14.222  45.373  1.00 16.43           C  
-ATOM    615  CG1 VAL A  94      51.556  14.174  45.405  1.00 15.01           C  
-ATOM    616  CG2 VAL A  94      53.417  14.836  44.013  1.00 15.46           C  
-ATOM    617  N   HIS A  95      52.081  15.208  48.467  1.00 12.87           N  
-ATOM    618  CA  HIS A  95      51.562  14.729  49.747  1.00 14.54           C  
-ATOM    619  C   HIS A  95      51.364  13.200  49.686  1.00 15.11           C  
-ATOM    620  O   HIS A  95      50.773  12.732  48.701  1.00 13.56           O  
-ATOM    621  CB  HIS A  95      50.230  15.412  50.049  1.00 13.95           C  
-ATOM    622  CG  HIS A  95      49.864  15.175  51.497  1.00 16.11           C  
-ATOM    623  ND1 HIS A  95      49.373  14.062  52.040  1.00 14.83           N  
-ATOM    624  CD2 HIS A  95      50.077  16.080  52.510  1.00 16.56           C  
-ATOM    625  CE1 HIS A  95      49.288  14.251  53.348  1.00 16.92           C  
-ATOM    626  NE2 HIS A  95      49.711  15.458  53.612  1.00 17.35           N  
-ATOM    627  N   PRO A  96      51.849  12.377  50.656  1.00 15.94           N  
-ATOM    628  CA  PRO A  96      51.682  10.906  50.715  1.00 16.06           C  
-ATOM    629  C   PRO A  96      50.288  10.339  50.474  1.00 15.65           C  
-ATOM    630  O   PRO A  96      50.147   9.247  49.935  1.00 17.84           O  
-ATOM    631  CB  PRO A  96      52.206  10.520  52.097  1.00 16.71           C  
-ATOM    632  CG  PRO A  96      53.231  11.588  52.459  1.00 16.31           C  
-ATOM    633  CD  PRO A  96      52.671  12.844  51.797  1.00 16.37           C  
-ATOM    634  N   TYR A  97      49.246  11.060  50.904  1.00 12.74           N  
-ATOM    635  CA  TYR A  97      47.875  10.656  50.747  1.00 12.92           C  
-ATOM    636  C   TYR A  97      47.122  11.114  49.509  1.00 14.08           C  
-ATOM    637  O   TYR A  97      45.918  10.844  49.445  1.00 12.62           O  
-ATOM    638  CB  TYR A  97      47.086  11.125  51.937  1.00 19.96           C  
-ATOM    639  CG  TYR A  97      47.419  10.449  53.244  1.00 24.42           C  
-ATOM    640  CD1 TYR A  97      47.972   9.169  53.262  1.00 29.05           C  
-ATOM    641  CD2 TYR A  97      47.116  11.098  54.441  1.00 28.57           C  
-ATOM    642  CE1 TYR A  97      48.214   8.515  54.478  1.00 30.89           C  
-ATOM    643  CE2 TYR A  97      47.357  10.458  55.662  1.00 31.11           C  
-ATOM    644  CZ  TYR A  97      47.899   9.168  55.673  1.00 31.62           C  
-ATOM    645  OH  TYR A  97      48.088   8.514  56.878  1.00 33.38           O  
-ATOM    646  N   TRP A  98      47.783  11.833  48.568  1.00 13.04           N  
-ATOM    647  CA  TRP A  98      47.155  12.347  47.348  1.00 12.00           C  
-ATOM    648  C   TRP A  98      46.665  11.184  46.522  1.00 12.60           C  
-ATOM    649  O   TRP A  98      47.422  10.250  46.298  1.00 13.84           O  
-ATOM    650  CB  TRP A  98      48.157  13.169  46.445  1.00 10.27           C  
-ATOM    651  CG  TRP A  98      47.633  13.510  45.018  1.00  9.10           C  
-ATOM    652  CD1 TRP A  98      48.301  13.079  43.898  1.00  9.83           C  
-ATOM    653  CD2 TRP A  98      46.490  14.212  44.682  1.00  8.83           C  
-ATOM    654  NE1 TRP A  98      47.583  13.495  42.864  1.00  7.05           N  
-ATOM    655  CE2 TRP A  98      46.512  14.161  43.285  1.00  8.87           C  
-ATOM    656  CE3 TRP A  98      45.436  14.874  45.319  1.00  9.49           C  
-ATOM    657  CZ2 TRP A  98      45.512  14.741  42.521  1.00 10.25           C  
-ATOM    658  CZ3 TRP A  98      44.425  15.458  44.549  1.00 12.16           C  
-ATOM    659  CH2 TRP A  98      44.462  15.398  43.155  1.00 11.86           C  
-ATOM    660  N   ASN A  99      45.457  11.209  46.028  1.00 14.58           N  
-ATOM    661  CA  ASN A  99      45.017  10.129  45.157  1.00 16.39           C  
-ATOM    662  C   ASN A  99      44.429  10.790  43.941  1.00 14.46           C  
-ATOM    663  O   ASN A  99      43.391  11.435  44.072  1.00 14.41           O  
-ATOM    664  CB  ASN A  99      43.966   9.302  45.883  1.00 18.94           C  
-ATOM    665  CG  ASN A  99      43.326   8.185  45.093  1.00 20.89           C  
-ATOM    666  OD1 ASN A  99      43.688   7.903  43.951  1.00 24.09           O  
-ATOM    667  ND2 ASN A  99      42.336   7.557  45.732  1.00 24.14           N  
-ATOM    668  N   THR A 100      45.076  10.624  42.786  1.00 15.80           N  
-ATOM    669  CA  THR A 100      44.608  11.181  41.502  1.00 18.40           C  
-ATOM    670  C   THR A 100      43.146  10.900  41.123  1.00 19.39           C  
-ATOM    671  O   THR A 100      42.462  11.748  40.532  1.00 20.77           O  
-ATOM    672  CB  THR A 100      45.432  10.654  40.351  1.00 19.59           C  
-ATOM    673  OG1 THR A 100      46.784  10.591  40.746  1.00 26.80           O  
-ATOM    674  CG2 THR A 100      45.218  11.522  39.143  1.00 22.76           C  
-ATOM    675  N   ASP A 101      42.670   9.693  41.471  1.00 20.22           N  
-ATOM    676  CA  ASP A 101      41.285   9.239  41.235  1.00 22.75           C  
-ATOM    677  C   ASP A 101      40.234   9.804  42.210  1.00 25.03           C  
-ATOM    678  O   ASP A 101      39.035   9.498  42.075  1.00 23.02           O  
-ATOM    679  CB  ASP A 101      41.132   7.708  41.349  1.00 24.56           C  
-ATOM    680  CG  ASP A 101      42.027   6.808  40.511  1.00 28.77           C  
-ATOM    681  OD1 ASP A 101      42.446   7.214  39.420  1.00 29.77           O  
-ATOM    682  OD2 ASP A 101      42.279   5.687  40.975  1.00 31.95           O  
-ATOM    683  N   ASP A 102      40.685  10.572  43.235  1.00 23.36           N  
-ATOM    684  CA  ASP A 102      39.788  11.180  44.201  1.00 22.91           C  
-ATOM    685  C   ASP A 102      40.272  12.575  44.630  1.00 22.59           C  
-ATOM    686  O   ASP A 102      40.711  12.725  45.774  1.00 21.87           O  
-ATOM    687  CB  ASP A 102      39.715  10.218  45.352  1.00 22.88           C  
-ATOM    688  CG  ASP A 102      38.567  10.408  46.325  1.00 26.98           C  
-ATOM    689  OD1 ASP A 102      37.798  11.372  46.219  1.00 22.46           O  
-ATOM    690  OD2 ASP A 102      38.468   9.544  47.203  1.00 28.88           O  
-ATOM    691  N   VAL A 103      40.207  13.631  43.770  1.00 20.22           N  
-ATOM    692  CA  VAL A 103      40.590  14.990  44.190  1.00 18.18           C  
-ATOM    693  C   VAL A 103      39.676  15.478  45.338  1.00 15.07           C  
-ATOM    694  O   VAL A 103      40.099  16.273  46.166  1.00 14.46           O  
-ATOM    695  CB  VAL A 103      40.533  15.972  42.915  1.00 19.44           C  
-ATOM    696  CG1 VAL A 103      39.125  16.374  42.552  1.00 19.05           C  
-ATOM    697  CG2 VAL A 103      41.252  17.269  43.206  1.00 17.32           C  
-ATOM    698  N   ALA A 104      38.442  14.967  45.449  1.00 12.49           N  
-ATOM    699  CA  ALA A 104      37.510  15.367  46.482  1.00 13.00           C  
-ATOM    700  C   ALA A 104      37.913  14.831  47.846  1.00 11.56           C  
-ATOM    701  O   ALA A 104      37.409  15.291  48.867  1.00 11.63           O  
-ATOM    702  CB  ALA A 104      36.125  14.865  46.138  1.00 13.61           C  
-ATOM    703  N   ALA A 105      38.850  13.880  47.903  1.00 12.38           N  
-ATOM    704  CA  ALA A 105      39.424  13.466  49.171  1.00 12.37           C  
-ATOM    705  C   ALA A 105      40.428  14.478  49.778  1.00 12.90           C  
-ATOM    706  O   ALA A 105      40.738  14.402  50.975  1.00 13.39           O  
-ATOM    707  CB  ALA A 105      40.153  12.138  48.997  1.00 12.90           C  
-ATOM    708  N   GLY A 106      40.932  15.450  49.004  1.00 11.80           N  
-ATOM    709  CA  GLY A 106      41.878  16.431  49.511  1.00 11.28           C  
-ATOM    710  C   GLY A 106      43.291  16.009  49.180  1.00 10.14           C  
-ATOM    711  O   GLY A 106      43.517  15.221  48.264  1.00 10.55           O  
-ATOM    712  N   TYR A 107      44.221  16.539  49.991  1.00  6.45           N  
-ATOM    713  CA  TYR A 107      45.660  16.363  49.895  1.00  7.59           C  
-ATOM    714  C   TYR A 107      46.191  16.831  48.550  1.00  5.93           C  
-ATOM    715  O   TYR A 107      47.220  16.349  48.084  1.00  8.21           O  
-ATOM    716  CB  TYR A 107      46.098  14.873  50.119  1.00 10.07           C  
-ATOM    717  CG  TYR A 107      45.495  14.301  51.410  1.00 14.76           C  
-ATOM    718  CD1 TYR A 107      45.975  14.689  52.667  1.00 14.99           C  
-ATOM    719  CD2 TYR A 107      44.403  13.430  51.318  1.00 16.34           C  
-ATOM    720  CE1 TYR A 107      45.347  14.211  53.819  1.00 19.58           C  
-ATOM    721  CE2 TYR A 107      43.772  12.941  52.449  1.00 16.99           C  
-ATOM    722  CZ  TYR A 107      44.250  13.342  53.691  1.00 21.33           C  
-ATOM    723  OH  TYR A 107      43.601  12.881  54.828  1.00 28.40           O  
-ATOM    724  N   ASP A 108      45.542  17.824  47.956  1.00  6.59           N  
-ATOM    725  CA  ASP A 108      46.017  18.293  46.666  1.00  6.83           C  
-ATOM    726  C   ASP A 108      47.061  19.380  46.853  1.00  7.13           C  
-ATOM    727  O   ASP A 108      46.795  20.575  46.695  1.00  7.22           O  
-ATOM    728  CB  ASP A 108      44.835  18.832  45.808  1.00  5.74           C  
-ATOM    729  CG  ASP A 108      45.130  18.984  44.297  1.00  7.46           C  
-ATOM    730  OD1 ASP A 108      46.207  18.606  43.862  1.00  6.32           O  
-ATOM    731  OD2 ASP A 108      44.261  19.453  43.571  1.00  7.77           O  
-ATOM    732  N   ILE A 109      48.278  18.894  47.151  1.00  6.43           N  
-ATOM    733  CA  ILE A 109      49.434  19.753  47.427  1.00  7.64           C  
-ATOM    734  C   ILE A 109      50.714  18.997  47.168  1.00  7.56           C  
-ATOM    735  O   ILE A 109      50.848  17.790  47.384  1.00  9.28           O  
-ATOM    736  CB  ILE A 109      49.313  20.299  48.927  1.00  8.14           C  
-ATOM    737  CG1 ILE A 109      50.424  21.328  49.224  1.00  8.97           C  
-ATOM    738  CG2 ILE A 109      49.366  19.129  49.951  1.00  6.47           C  
-ATOM    739  CD1 ILE A 109      50.035  22.216  50.449  1.00 10.00           C  
-ATOM    740  N   ALA A 110      51.673  19.768  46.661  1.00  7.57           N  
-ATOM    741  CA  ALA A 110      52.975  19.254  46.297  1.00  8.22           C  
-ATOM    742  C   ALA A 110      54.005  20.354  46.456  1.00  9.78           C  
-ATOM    743  O   ALA A 110      53.710  21.540  46.305  1.00 10.61           O  
-ATOM    744  CB  ALA A 110      52.957  18.783  44.842  1.00  7.05           C  
-ATOM    745  N   LEU A 111      55.214  19.961  46.827  1.00  8.38           N  
-ATOM    746  CA  LEU A 111      56.315  20.876  46.979  1.00 11.26           C  
-ATOM    747  C   LEU A 111      57.401  20.545  45.961  1.00 11.28           C  
-ATOM    748  O   LEU A 111      57.808  19.398  45.844  1.00 11.78           O  
-ATOM    749  CB  LEU A 111      56.900  20.778  48.401  1.00 11.52           C  
-ATOM    750  CG  LEU A 111      55.944  21.119  49.543  1.00 14.90           C  
-ATOM    751  CD1 LEU A 111      56.650  20.874  50.874  1.00 16.48           C  
-ATOM    752  CD2 LEU A 111      55.506  22.572  49.439  1.00 13.34           C  
-ATOM    753  N   LEU A 112      57.916  21.532  45.234  1.00 12.10           N  
-ATOM    754  CA  LEU A 112      58.928  21.349  44.211  1.00 11.77           C  
-ATOM    755  C   LEU A 112      60.230  21.991  44.671  1.00 13.64           C  
-ATOM    756  O   LEU A 112      60.290  23.170  45.037  1.00 10.84           O  
-ATOM    757  CB  LEU A 112      58.482  22.015  42.905  1.00 12.17           C  
-ATOM    758  CG  LEU A 112      57.063  21.837  42.415  1.00 15.40           C  
-ATOM    759  CD1 LEU A 112      56.876  22.538  41.085  1.00 15.49           C  
-ATOM    760  CD2 LEU A 112      56.775  20.368  42.294  1.00 15.15           C  
-ATOM    761  N   ARG A 113      61.283  21.186  44.757  1.00 13.46           N  
-ATOM    762  CA  ARG A 113      62.589  21.715  45.050  1.00 15.28           C  
-ATOM    763  C   ARG A 113      63.244  22.124  43.733  1.00 16.51           C  
-ATOM    764  O   ARG A 113      63.374  21.346  42.790  1.00 15.93           O  
-ATOM    765  CB  ARG A 113      63.388  20.649  45.748  1.00 19.45           C  
-ATOM    766  CG  ARG A 113      64.692  21.189  46.234  1.00 24.78           C  
-ATOM    767  CD  ARG A 113      65.510  19.963  46.464  1.00 35.00           C  
-ATOM    768  NE  ARG A 113      66.833  20.308  46.929  1.00 44.46           N  
-ATOM    769  CZ  ARG A 113      67.054  20.648  48.211  1.00 50.93           C  
-ATOM    770  NH1 ARG A 113      66.056  20.699  49.111  1.00 53.94           N  
-ATOM    771  NH2 ARG A 113      68.294  20.957  48.614  1.00 52.42           N  
-ATOM    772  N   LEU A 114      63.656  23.382  43.675  1.00 14.59           N  
-ATOM    773  CA  LEU A 114      64.286  23.948  42.517  1.00 12.96           C  
-ATOM    774  C   LEU A 114      65.750  23.621  42.431  1.00 14.45           C  
-ATOM    775  O   LEU A 114      66.429  23.426  43.427  1.00 15.35           O  
-ATOM    776  CB  LEU A 114      64.085  25.448  42.528  1.00 14.52           C  
-ATOM    777  CG  LEU A 114      62.643  25.929  42.734  1.00 13.04           C  
-ATOM    778  CD1 LEU A 114      62.618  27.433  42.664  1.00 13.89           C  
-ATOM    779  CD2 LEU A 114      61.727  25.354  41.681  1.00 15.27           C  
-ATOM    780  N   ALA A 115      66.225  23.591  41.180  1.00 15.90           N  
-ATOM    781  CA  ALA A 115      67.574  23.190  40.869  1.00 16.86           C  
-ATOM    782  C   ALA A 115      68.522  24.228  41.395  1.00 19.93           C  
-ATOM    783  O   ALA A 115      69.664  23.887  41.715  1.00 22.92           O  
-ATOM    784  CB  ALA A 115      67.763  23.068  39.383  1.00 14.10           C  
-ATOM    785  N   GLN A 116      68.097  25.490  41.479  1.00 21.12           N  
-ATOM    786  CA  GLN A 116      68.882  26.472  42.201  1.00 24.08           C  
-ATOM    787  C   GLN A 116      68.024  27.514  42.898  1.00 20.84           C  
-ATOM    788  O   GLN A 116      66.823  27.610  42.679  1.00 18.27           O  
-ATOM    789  CB  GLN A 116      69.904  27.171  41.267  1.00 30.47           C  
-ATOM    790  CG  GLN A 116      69.588  28.237  40.206  1.00 40.70           C  
-ATOM    791  CD  GLN A 116      70.645  29.381  40.178  1.00 48.56           C  
-ATOM    792  OE1 GLN A 116      71.846  29.204  40.474  1.00 51.81           O  
-ATOM    793  NE2 GLN A 116      70.236  30.621  39.855  1.00 50.77           N  
-ATOM    794  N   SER A 117      68.648  28.236  43.834  1.00 20.21           N  
-ATOM    795  CA  SER A 117      67.993  29.326  44.525  1.00 22.03           C  
-ATOM    796  C   SER A 117      67.726  30.546  43.645  1.00 20.51           C  
-ATOM    797  O   SER A 117      68.607  30.978  42.906  1.00 21.61           O  
-ATOM    798  CB  SER A 117      68.848  29.713  45.693  1.00 23.40           C  
-ATOM    799  OG  SER A 117      68.736  28.667  46.645  1.00 29.17           O  
-ATOM    800  N   VAL A 118      66.505  31.076  43.634  1.00 18.92           N  
-ATOM    801  CA  VAL A 118      66.219  32.272  42.862  1.00 17.04           C  
-ATOM    802  C   VAL A 118      66.682  33.466  43.689  1.00 18.16           C  
-ATOM    803  O   VAL A 118      66.958  33.359  44.893  1.00 18.57           O  
-ATOM    804  CB  VAL A 118      64.691  32.408  42.520  1.00 15.99           C  
-ATOM    805  CG1 VAL A 118      64.306  31.212  41.662  1.00 13.34           C  
-ATOM    806  CG2 VAL A 118      63.798  32.454  43.740  1.00 14.89           C  
-ATOM    807  N   THR A 119      66.874  34.578  42.987  1.00 17.98           N  
-ATOM    808  CA  THR A 119      67.293  35.837  43.544  1.00 18.88           C  
-ATOM    809  C   THR A 119      66.071  36.651  43.921  1.00 18.24           C  
-ATOM    810  O   THR A 119      65.197  36.845  43.074  1.00 19.28           O  
-ATOM    811  CB  THR A 119      68.136  36.574  42.489  1.00 22.39           C  
-ATOM    812  OG1 THR A 119      69.324  35.787  42.316  1.00 24.41           O  
-ATOM    813  CG2 THR A 119      68.409  38.046  42.866  1.00 23.47           C  
-ATOM    814  N   LEU A 120      65.997  37.164  45.156  1.00 17.66           N  
-ATOM    815  CA  LEU A 120      64.844  37.945  45.535  1.00 17.16           C  
-ATOM    816  C   LEU A 120      65.043  39.410  45.223  1.00 17.89           C  
-ATOM    817  O   LEU A 120      66.140  39.954  45.375  1.00 21.02           O  
-ATOM    818  CB  LEU A 120      64.553  37.758  47.023  1.00 17.06           C  
-ATOM    819  CG  LEU A 120      64.308  36.343  47.568  1.00 19.10           C  
-ATOM    820  CD1 LEU A 120      63.883  36.470  49.023  1.00 18.54           C  
-ATOM    821  CD2 LEU A 120      63.208  35.620  46.823  1.00 18.38           C  
-ATOM    822  N   ASN A 121      63.967  40.037  44.751  1.00 17.23           N  
-ATOM    823  CA  ASN A 121      63.949  41.455  44.410  1.00 18.56           C  
-ATOM    824  C   ASN A 121      62.526  41.982  44.418  1.00 18.33           C  
-ATOM    825  O   ASN A 121      61.669  41.268  44.947  1.00 19.10           O  
-ATOM    826  CB  ASN A 121      64.608  41.669  43.030  1.00 18.33           C  
-ATOM    827  CG  ASN A 121      64.039  40.875  41.875  1.00 18.25           C  
-ATOM    828  OD1 ASN A 121      62.827  40.853  41.666  1.00 19.36           O  
-ATOM    829  ND2 ASN A 121      64.922  40.227  41.111  1.00 18.49           N  
-ATOM    830  N   SER A 122      62.109  43.135  43.864  1.00 20.06           N  
-ATOM    831  CA  SER A 122      60.701  43.535  44.000  1.00 21.56           C  
-ATOM    832  C   SER A 122      59.689  42.720  43.200  1.00 21.71           C  
-ATOM    833  O   SER A 122      58.476  42.816  43.410  1.00 23.08           O  
-ATOM    834  CB  SER A 122      60.540  44.987  43.627  1.00 25.51           C  
-ATOM    835  OG  SER A 122      61.304  45.281  42.466  1.00 35.65           O  
-ATOM    836  N   TYR A 123      60.216  41.903  42.277  1.00 19.93           N  
-ATOM    837  CA  TYR A 123      59.418  41.039  41.431  1.00 17.77           C  
-ATOM    838  C   TYR A 123      59.332  39.622  41.935  1.00 15.04           C  
-ATOM    839  O   TYR A 123      58.436  38.902  41.513  1.00 14.16           O  
-ATOM    840  CB  TYR A 123      60.006  40.982  40.052  1.00 19.11           C  
-ATOM    841  CG  TYR A 123      60.098  42.388  39.530  1.00 21.65           C  
-ATOM    842  CD1 TYR A 123      58.899  43.020  39.158  1.00 25.24           C  
-ATOM    843  CD2 TYR A 123      61.335  43.032  39.445  1.00 21.72           C  
-ATOM    844  CE1 TYR A 123      58.945  44.334  38.689  1.00 25.01           C  
-ATOM    845  CE2 TYR A 123      61.380  44.348  38.971  1.00 22.05           C  
-ATOM    846  CZ  TYR A 123      60.184  44.980  38.603  1.00 24.94           C  
-ATOM    847  OH  TYR A 123      60.168  46.280  38.139  1.00 26.91           O  
-ATOM    848  N   VAL A 124      60.314  39.232  42.751  1.00 14.56           N  
-ATOM    849  CA  VAL A 124      60.462  37.886  43.301  1.00 15.79           C  
-ATOM    850  C   VAL A 124      60.566  37.920  44.837  1.00 13.33           C  
-ATOM    851  O   VAL A 124      61.586  38.272  45.424  1.00 13.49           O  
-ATOM    852  CB  VAL A 124      61.736  37.207  42.666  1.00 14.02           C  
-ATOM    853  CG1 VAL A 124      61.857  35.756  43.122  1.00 14.00           C  
-ATOM    854  CG2 VAL A 124      61.628  37.221  41.137  1.00 12.98           C  
-ATOM    855  N   GLN A 125      59.480  37.525  45.504  1.00 15.12           N  
-ATOM    856  CA  GLN A 125      59.396  37.532  46.964  1.00 14.25           C  
-ATOM    857  C   GLN A 125      58.761  36.258  47.480  1.00 14.18           C  
-ATOM    858  O   GLN A 125      57.963  35.658  46.781  1.00 12.99           O  
-ATOM    859  CB  GLN A 125      58.540  38.710  47.464  1.00 16.30           C  
-ATOM    860  CG  GLN A 125      59.202  40.063  47.285  1.00 22.28           C  
-ATOM    861  CD  GLN A 125      60.382  40.270  48.215  1.00 27.01           C  
-ATOM    862  OE1 GLN A 125      60.210  40.216  49.432  1.00 32.30           O  
-ATOM    863  NE2 GLN A 125      61.614  40.482  47.752  1.00 30.01           N  
-ATOM    864  N   LEU A 126      59.072  35.839  48.699  1.00 12.49           N  
-ATOM    865  CA  LEU A 126      58.465  34.650  49.243  1.00 13.35           C  
-ATOM    866  C   LEU A 126      57.043  34.954  49.700  1.00 12.59           C  
-ATOM    867  O   LEU A 126      56.705  36.045  50.161  1.00 11.18           O  
-ATOM    868  CB  LEU A 126      59.297  34.118  50.426  1.00 12.23           C  
-ATOM    869  CG  LEU A 126      60.799  33.912  50.317  1.00 13.20           C  
-ATOM    870  CD1 LEU A 126      61.319  33.196  51.553  1.00 14.55           C  
-ATOM    871  CD2 LEU A 126      61.109  33.120  49.080  1.00 15.07           C  
-ATOM    872  N   GLY A 127      56.200  33.941  49.540  1.00 11.33           N  
-ATOM    873  CA  GLY A 127      54.836  33.975  49.957  1.00 11.54           C  
-ATOM    874  C   GLY A 127      54.753  33.786  51.454  1.00 13.23           C  
-ATOM    875  O   GLY A 127      55.547  33.052  52.038  1.00 14.89           O  
-ATOM    876  N   VAL A 128      53.807  34.474  52.086  1.00 12.47           N  
-ATOM    877  CA  VAL A 128      53.651  34.406  53.529  1.00 12.66           C  
-ATOM    878  C   VAL A 128      52.649  33.269  53.788  1.00 10.38           C  
-ATOM    879  O   VAL A 128      51.526  33.321  53.297  1.00 12.45           O  
-ATOM    880  CB  VAL A 128      53.125  35.792  54.025  1.00 12.62           C  
-ATOM    881  CG1 VAL A 128      52.798  35.658  55.512  1.00 16.46           C  
-ATOM    882  CG2 VAL A 128      54.153  36.918  53.813  1.00 12.26           C  
-ATOM    883  N   LEU A 129      53.000  32.231  54.574  1.00 12.38           N  
-ATOM    884  CA  LEU A 129      52.053  31.181  54.933  1.00 12.53           C  
-ATOM    885  C   LEU A 129      51.234  31.506  56.197  1.00 14.42           C  
-ATOM    886  O   LEU A 129      51.762  32.177  57.100  1.00 14.93           O  
-ATOM    887  CB  LEU A 129      52.850  29.870  55.106  1.00 13.25           C  
-ATOM    888  CG  LEU A 129      53.533  29.362  53.833  1.00 14.57           C  
-ATOM    889  CD1 LEU A 129      54.094  28.008  54.108  1.00 16.71           C  
-ATOM    890  CD2 LEU A 129      52.563  29.223  52.681  1.00 14.81           C  
-ATOM    891  N   PRO A 130      49.960  31.099  56.339  1.00 12.78           N  
-ATOM    892  CA  PRO A 130      49.205  31.212  57.581  1.00 14.50           C  
-ATOM    893  C   PRO A 130      49.726  30.305  58.703  1.00 14.51           C  
-ATOM    894  O   PRO A 130      50.451  29.329  58.494  1.00 13.22           O  
-ATOM    895  CB  PRO A 130      47.772  30.904  57.177  1.00 12.12           C  
-ATOM    896  CG  PRO A 130      47.960  29.939  56.033  1.00 13.92           C  
-ATOM    897  CD  PRO A 130      49.144  30.506  55.289  1.00 13.35           C  
-ATOM    898  N   ARG A 131      49.411  30.670  59.949  1.00 16.06           N  
-ATOM    899  CA  ARG A 131      49.723  29.766  61.050  1.00 17.91           C  
-ATOM    900  C   ARG A 131      48.784  28.578  60.973  1.00 13.67           C  
-ATOM    901  O   ARG A 131      47.649  28.714  60.483  1.00 12.92           O  
-ATOM    902  CB  ARG A 131      49.560  30.491  62.409  1.00 25.93           C  
-ATOM    903  CG  ARG A 131      50.680  31.554  62.612  1.00 39.42           C  
-ATOM    904  CD  ARG A 131      52.152  31.030  62.666  1.00 50.12           C  
-ATOM    905  NE  ARG A 131      53.162  32.110  62.659  1.00 60.31           N  
-ATOM    906  CZ  ARG A 131      54.278  32.132  63.441  1.00 65.68           C  
-ATOM    907  NH1 ARG A 131      54.577  31.147  64.316  1.00 66.88           N  
-ATOM    908  NH2 ARG A 131      55.123  33.181  63.366  1.00 68.80           N  
-ATOM    909  N   ALA A 132      49.280  27.411  61.418  1.00 14.22           N  
-ATOM    910  CA  ALA A 132      48.519  26.156  61.393  1.00 14.01           C  
-ATOM    911  C   ALA A 132      47.173  26.231  62.081  1.00 15.78           C  
-ATOM    912  O   ALA A 132      47.078  26.816  63.162  1.00 14.01           O  
-ATOM    913  CB  ALA A 132      49.287  25.045  62.070  1.00 16.06           C  
-ATOM    914  N   GLY A 133      46.109  25.699  61.454  1.00 12.42           N  
-ATOM    915  CA  GLY A 133      44.789  25.646  62.036  1.00 11.40           C  
-ATOM    916  C   GLY A 133      43.905  26.836  61.751  1.00 11.68           C  
-ATOM    917  O   GLY A 133      42.712  26.772  62.027  1.00 12.16           O  
-ATOM    918  N   THR A 134      44.469  27.938  61.230  1.00 12.27           N  
-ATOM    919  CA  THR A 134      43.715  29.150  60.918  1.00 12.85           C  
-ATOM    920  C   THR A 134      42.583  28.894  59.957  1.00 11.47           C  
-ATOM    921  O   THR A 134      42.803  28.385  58.867  1.00 11.69           O  
-ATOM    922  CB  THR A 134      44.648  30.227  60.295  1.00 13.66           C  
-ATOM    923  OG1 THR A 134      45.687  30.503  61.219  1.00 17.97           O  
-ATOM    924  CG2 THR A 134      43.926  31.533  60.032  1.00 17.08           C  
-ATOM    925  N   ILE A 135      41.384  29.252  60.348  1.00  9.47           N  
-ATOM    926  CA  ILE A 135      40.189  29.186  59.540  1.00 10.97           C  
-ATOM    927  C   ILE A 135      39.715  30.642  59.371  1.00 14.31           C  
-ATOM    928  O   ILE A 135      39.593  31.399  60.338  1.00 14.95           O  
-ATOM    929  CB  ILE A 135      39.094  28.352  60.262  1.00 11.95           C  
-ATOM    930  CG1 ILE A 135      39.633  26.968  60.584  1.00 14.79           C  
-ATOM    931  CG2 ILE A 135      37.824  28.320  59.428  1.00 14.04           C  
-ATOM    932  CD1 ILE A 135      39.932  26.005  59.446  1.00 18.18           C  
-ATOM    933  N   LEU A 136      39.430  31.092  58.150  1.00 15.33           N  
-ATOM    934  CA  LEU A 136      38.900  32.423  57.908  1.00 15.29           C  
-ATOM    935  C   LEU A 136      37.394  32.465  58.111  1.00 16.06           C  
-ATOM    936  O   LEU A 136      36.653  31.499  57.870  1.00 15.28           O  
-ATOM    937  CB  LEU A 136      39.216  32.880  56.461  1.00 16.04           C  
-ATOM    938  CG  LEU A 136      40.704  32.930  56.113  1.00 18.11           C  
-ATOM    939  CD1 LEU A 136      40.897  33.096  54.617  1.00 21.51           C  
-ATOM    940  CD2 LEU A 136      41.353  34.040  56.921  1.00 19.80           C  
-ATOM    941  N   ALA A 137      36.917  33.627  58.553  1.00 16.01           N  
-ATOM    942  CA  ALA A 137      35.481  33.798  58.649  1.00 17.87           C  
-ATOM    943  C   ALA A 137      34.844  33.866  57.247  1.00 18.01           C  
-ATOM    944  O   ALA A 137      35.507  34.108  56.239  1.00 16.27           O  
-ATOM    945  CB  ALA A 137      35.174  35.088  59.415  1.00 18.28           C  
-ATOM    946  N   ASN A 138      33.532  33.622  57.203  1.00 18.60           N  
-ATOM    947  CA  ASN A 138      32.733  33.695  56.001  1.00 18.18           C  
-ATOM    948  C   ASN A 138      32.894  35.101  55.484  1.00 19.27           C  
-ATOM    949  O   ASN A 138      32.994  36.085  56.229  1.00 17.88           O  
-ATOM    950  CB  ASN A 138      31.262  33.470  56.276  1.00 17.20           C  
-ATOM    951  CG  ASN A 138      30.433  33.247  55.024  1.00 20.09           C  
-ATOM    952  OD1 ASN A 138      30.676  32.313  54.261  1.00 19.28           O  
-ATOM    953  ND2 ASN A 138      29.436  34.094  54.767  1.00 20.96           N  
-ATOM    954  N   ASN A 139      32.995  35.108  54.165  1.00 18.73           N  
-ATOM    955  CA  ASN A 139      33.154  36.302  53.365  1.00 20.28           C  
-ATOM    956  C   ASN A 139      34.413  37.113  53.609  1.00 19.05           C  
-ATOM    957  O   ASN A 139      34.368  38.332  53.490  1.00 19.23           O  
-ATOM    958  CB  ASN A 139      31.929  37.170  53.556  1.00 25.51           C  
-ATOM    959  CG  ASN A 139      31.584  37.807  52.234  1.00 34.05           C  
-ATOM    960  OD1 ASN A 139      30.958  37.179  51.377  1.00 40.16           O  
-ATOM    961  ND2 ASN A 139      32.015  39.048  52.015  1.00 40.04           N  
-ATOM    962  N   SER A 140      35.543  36.481  53.963  1.00 15.70           N  
-ATOM    963  CA  SER A 140      36.798  37.186  54.122  1.00 14.52           C  
-ATOM    964  C   SER A 140      37.315  37.619  52.773  1.00 15.11           C  
-ATOM    965  O   SER A 140      37.031  36.951  51.785  1.00 14.47           O  
-ATOM    966  CB  SER A 140      37.867  36.321  54.772  1.00 16.20           C  
-ATOM    967  OG  SER A 140      37.468  36.086  56.112  1.00 18.16           O  
-ATOM    968  N   PRO A 141      38.003  38.759  52.678  1.00 14.63           N  
-ATOM    969  CA  PRO A 141      38.577  39.279  51.444  1.00 13.41           C  
-ATOM    970  C   PRO A 141      39.807  38.525  51.000  1.00 10.55           C  
-ATOM    971  O   PRO A 141      40.833  38.470  51.675  1.00 11.01           O  
-ATOM    972  CB  PRO A 141      38.831  40.740  51.769  1.00 14.54           C  
-ATOM    973  CG  PRO A 141      39.189  40.734  53.232  1.00 15.28           C  
-ATOM    974  CD  PRO A 141      38.095  39.783  53.731  1.00 16.40           C  
-ATOM    975  N   CYS A 142      39.669  37.908  49.826  1.00 11.19           N  
-ATOM    976  CA  CYS A 142      40.765  37.156  49.211  1.00 10.27           C  
-ATOM    977  C   CYS A 142      40.805  37.452  47.732  1.00 10.86           C  
-ATOM    978  O   CYS A 142      39.767  37.785  47.149  1.00 12.76           O  
-ATOM    979  CB  CYS A 142      40.548  35.673  49.362  1.00 12.32           C  
-ATOM    980  SG  CYS A 142      40.395  35.106  51.066  1.00 11.55           S  
-ATOM    981  N   TYR A 143      41.991  37.399  47.132  1.00  9.25           N  
-ATOM    982  CA  TYR A 143      42.160  37.538  45.699  1.00  7.77           C  
-ATOM    983  C   TYR A 143      42.678  36.232  45.103  1.00  9.84           C  
-ATOM    984  O   TYR A 143      43.627  35.658  45.663  1.00  9.61           O  
-ATOM    985  CB  TYR A 143      43.191  38.602  45.349  1.00  8.46           C  
-ATOM    986  CG  TYR A 143      42.556  39.960  45.490  1.00 15.49           C  
-ATOM    987  CD1 TYR A 143      42.505  40.616  46.728  1.00 20.51           C  
-ATOM    988  CD2 TYR A 143      41.972  40.533  44.365  1.00 18.94           C  
-ATOM    989  CE1 TYR A 143      41.852  41.855  46.833  1.00 22.21           C  
-ATOM    990  CE2 TYR A 143      41.327  41.768  44.467  1.00 25.19           C  
-ATOM    991  CZ  TYR A 143      41.275  42.414  45.699  1.00 25.16           C  
-ATOM    992  OH  TYR A 143      40.644  43.636  45.777  1.00 31.74           O  
-ATOM    993  N   ILE A 144      42.116  35.757  43.968  1.00  8.83           N  
-ATOM    994  CA  ILE A 144      42.751  34.637  43.247  1.00  8.16           C  
-ATOM    995  C   ILE A 144      43.617  35.210  42.158  1.00  8.94           C  
-ATOM    996  O   ILE A 144      43.264  36.216  41.529  1.00  9.58           O  
-ATOM    997  CB  ILE A 144      41.669  33.658  42.648  1.00  7.84           C  
-ATOM    998  CG1 ILE A 144      42.414  32.453  42.000  1.00  9.60           C  
-ATOM    999  CG2 ILE A 144      40.755  34.349  41.648  1.00  5.35           C  
-ATOM   1000  CD1 ILE A 144      41.552  31.284  41.473  1.00  6.07           C  
-ATOM   1001  N   THR A 145      44.789  34.652  41.924  1.00  7.93           N  
-ATOM   1002  CA  THR A 145      45.569  35.137  40.804  1.00  7.74           C  
-ATOM   1003  C   THR A 145      45.991  34.012  39.845  1.00 10.60           C  
-ATOM   1004  O   THR A 145      46.172  32.873  40.276  1.00  9.17           O  
-ATOM   1005  CB  THR A 145      46.858  35.918  41.281  1.00  5.71           C  
-ATOM   1006  OG1 THR A 145      47.622  35.116  42.173  1.00  5.47           O  
-ATOM   1007  CG2 THR A 145      46.444  37.275  41.846  1.00  8.19           C  
-ATOM   1008  N   GLY A 146      46.149  34.299  38.540  1.00  8.12           N  
-ATOM   1009  CA  GLY A 146      46.676  33.295  37.629  1.00  9.19           C  
-ATOM   1010  C   GLY A 146      46.537  33.671  36.155  1.00  9.69           C  
-ATOM   1011  O   GLY A 146      45.903  34.677  35.803  1.00  8.92           O  
-ATOM   1012  N   TRP A 147      47.140  32.807  35.319  1.00  7.68           N  
-ATOM   1013  CA  TRP A 147      47.144  32.956  33.862  1.00  7.80           C  
-ATOM   1014  C   TRP A 147      46.212  31.971  33.164  1.00  9.38           C  
-ATOM   1015  O   TRP A 147      46.263  31.821  31.952  1.00 11.53           O  
-ATOM   1016  CB  TRP A 147      48.558  32.739  33.306  1.00  8.48           C  
-ATOM   1017  CG  TRP A 147      49.620  33.790  33.632  1.00  9.39           C  
-ATOM   1018  CD1 TRP A 147      49.780  34.882  32.834  1.00 10.04           C  
-ATOM   1019  CD2 TRP A 147      50.541  33.740  34.652  1.00 10.02           C  
-ATOM   1020  NE1 TRP A 147      50.813  35.519  33.335  1.00  8.45           N  
-ATOM   1021  CE2 TRP A 147      51.303  34.896  34.408  1.00  9.41           C  
-ATOM   1022  CE3 TRP A 147      50.865  32.913  35.729  1.00  7.37           C  
-ATOM   1023  CZ2 TRP A 147      52.386  35.235  35.229  1.00 11.23           C  
-ATOM   1024  CZ3 TRP A 147      51.953  33.253  36.548  1.00  7.18           C  
-ATOM   1025  CH2 TRP A 147      52.716  34.408  36.308  1.00  8.91           C  
-ATOM   1026  N   GLY A 148      45.346  31.299  33.929  1.00  9.69           N  
-ATOM   1027  CA  GLY A 148      44.410  30.330  33.395  1.00  7.88           C  
-ATOM   1028  C   GLY A 148      43.335  30.928  32.510  1.00  9.49           C  
-ATOM   1029  O   GLY A 148      43.270  32.144  32.321  1.00 10.20           O  
-ATOM   1030  N   LEU A 149      42.438  30.060  32.037  1.00  7.76           N  
-ATOM   1031  CA  LEU A 149      41.387  30.425  31.092  1.00  7.74           C  
-ATOM   1032  C   LEU A 149      40.533  31.537  31.615  1.00  8.88           C  
-ATOM   1033  O   LEU A 149      40.138  31.552  32.795  1.00  9.52           O  
-ATOM   1034  CB  LEU A 149      40.429  29.279  30.782  1.00  7.94           C  
-ATOM   1035  CG  LEU A 149      40.950  27.945  30.363  1.00  9.90           C  
-ATOM   1036  CD1 LEU A 149      39.772  27.102  29.900  1.00 12.79           C  
-ATOM   1037  CD2 LEU A 149      42.009  28.104  29.318  1.00 10.28           C  
-ATOM   1038  N   THR A 150      40.270  32.468  30.710  1.00  8.87           N  
-ATOM   1039  CA  THR A 150      39.468  33.607  31.094  1.00 10.03           C  
-ATOM   1040  C   THR A 150      37.977  33.426  30.858  1.00 10.87           C  
-ATOM   1041  O   THR A 150      37.150  34.270  31.235  1.00 10.66           O  
-ATOM   1042  CB  THR A 150      40.028  34.863  30.362  1.00 10.23           C  
-ATOM   1043  OG1 THR A 150      39.856  34.692  28.967  1.00 14.19           O  
-ATOM   1044  CG2 THR A 150      41.491  35.069  30.621  1.00  9.13           C  
-ATOM   1045  N   ARG A 151      37.589  32.297  30.250  1.00 11.55           N  
-ATOM   1046  CA  ARG A 151      36.199  31.916  30.057  1.00 12.27           C  
-ATOM   1047  C   ARG A 151      36.241  30.399  30.140  1.00 10.58           C  
-ATOM   1048  O   ARG A 151      37.274  29.796  29.839  1.00 11.78           O  
-ATOM   1049  CB  ARG A 151      35.622  32.208  28.642  1.00 19.17           C  
-ATOM   1050  CG  ARG A 151      35.542  33.557  27.934  1.00 26.69           C  
-ATOM   1051  CD  ARG A 151      34.361  34.465  28.283  1.00 34.03           C  
-ATOM   1052  NE  ARG A 151      33.052  33.811  28.152  1.00 39.13           N  
-ATOM   1053  CZ  ARG A 151      32.061  34.233  27.333  1.00 39.58           C  
-ATOM   1054  NH1 ARG A 151      32.169  35.307  26.524  1.00 40.73           N  
-ATOM   1055  NH2 ARG A 151      30.897  33.581  27.372  1.00 38.69           N  
-ATOM   1056  N   THR A 152      35.125  29.758  30.488  1.00 11.92           N  
-ATOM   1057  CA  THR A 152      34.967  28.299  30.424  1.00 12.16           C  
-ATOM   1058  C   THR A 152      35.237  27.895  28.963  1.00 14.05           C  
-ATOM   1059  O   THR A 152      34.671  28.486  28.039  1.00 14.86           O  
-ATOM   1060  CB  THR A 152      33.536  27.922  30.815  1.00  9.41           C  
-ATOM   1061  OG1 THR A 152      33.409  28.313  32.174  1.00 14.56           O  
-ATOM   1062  CG2 THR A 152      33.199  26.458  30.680  1.00 11.59           C  
-ATOM   1063  N   ASN A 153      36.126  26.926  28.749  1.00 14.23           N  
-ATOM   1064  CA  ASN A 153      36.538  26.475  27.424  1.00 14.96           C  
-ATOM   1065  C   ASN A 153      37.083  27.596  26.559  1.00 14.95           C  
-ATOM   1066  O   ASN A 153      36.934  27.509  25.339  1.00 15.11           O  
-ATOM   1067  CB  ASN A 153      35.370  25.809  26.676  1.00 19.04           C  
-ATOM   1068  CG  ASN A 153      34.910  24.544  27.381  1.00 23.80           C  
-ATOM   1069  OD1 ASN A 153      35.706  23.653  27.729  1.00 24.64           O  
-ATOM   1070  ND2 ASN A 153      33.596  24.510  27.614  1.00 25.16           N  
-ATOM   1071  N   GLY A 154      37.682  28.633  27.180  1.00 13.63           N  
-ATOM   1072  CA  GLY A 154      38.293  29.745  26.469  1.00 11.62           C  
-ATOM   1073  C   GLY A 154      39.772  29.503  26.257  1.00 13.55           C  
-ATOM   1074  O   GLY A 154      40.259  28.392  25.990  1.00 15.18           O  
-ATOM   1075  N   GLN A 155      40.527  30.570  26.353  1.00 14.43           N  
-ATOM   1076  CA  GLN A 155      41.966  30.447  26.288  1.00 15.79           C  
-ATOM   1077  C   GLN A 155      42.712  31.081  27.468  1.00 13.66           C  
-ATOM   1078  O   GLN A 155      42.148  31.866  28.224  1.00 10.24           O  
-ATOM   1079  CB  GLN A 155      42.494  31.050  24.978  1.00 21.59           C  
-ATOM   1080  CG  GLN A 155      42.034  32.419  24.521  1.00 29.39           C  
-ATOM   1081  CD  GLN A 155      42.764  32.889  23.260  1.00 34.23           C  
-ATOM   1082  OE1 GLN A 155      43.277  32.111  22.451  1.00 36.53           O  
-ATOM   1083  NE2 GLN A 155      42.853  34.200  23.067  1.00 36.81           N  
-ATOM   1084  N   LEU A 156      43.990  30.734  27.655  1.00 14.13           N  
-ATOM   1085  CA  LEU A 156      44.836  31.289  28.717  1.00 14.79           C  
-ATOM   1086  C   LEU A 156      44.989  32.798  28.626  1.00 16.90           C  
-ATOM   1087  O   LEU A 156      44.858  33.409  27.550  1.00 16.83           O  
-ATOM   1088  CB  LEU A 156      46.234  30.698  28.671  1.00 15.94           C  
-ATOM   1089  CG  LEU A 156      46.337  29.193  28.964  1.00 19.73           C  
-ATOM   1090  CD1 LEU A 156      47.807  28.814  28.724  1.00 20.30           C  
-ATOM   1091  CD2 LEU A 156      45.865  28.823  30.392  1.00 16.92           C  
-ATOM   1092  N   ALA A 157      45.223  33.437  29.764  1.00 15.33           N  
-ATOM   1093  CA  ALA A 157      45.495  34.858  29.753  1.00 15.51           C  
-ATOM   1094  C   ALA A 157      46.947  35.040  29.333  1.00 16.07           C  
-ATOM   1095  O   ALA A 157      47.813  34.194  29.633  1.00 17.90           O  
-ATOM   1096  CB  ALA A 157      45.296  35.403  31.140  1.00 12.82           C  
-ATOM   1097  N   GLN A 158      47.257  36.120  28.610  1.00 15.47           N  
-ATOM   1098  CA  GLN A 158      48.664  36.437  28.362  1.00 17.41           C  
-ATOM   1099  C   GLN A 158      49.301  37.143  29.552  1.00 13.63           C  
-ATOM   1100  O   GLN A 158      50.479  36.973  29.807  1.00 14.94           O  
-ATOM   1101  CB  GLN A 158      48.861  37.368  27.215  1.00 24.31           C  
-ATOM   1102  CG  GLN A 158      48.408  36.857  25.859  1.00 36.06           C  
-ATOM   1103  CD  GLN A 158      48.489  37.906  24.729  1.00 42.49           C  
-ATOM   1104  OE1 GLN A 158      47.839  37.725  23.689  1.00 46.00           O  
-ATOM   1105  NE2 GLN A 158      49.244  39.021  24.843  1.00 44.51           N  
-ATOM   1106  N   THR A 159      48.564  37.994  30.273  1.00 14.16           N  
-ATOM   1107  CA  THR A 159      49.082  38.719  31.431  1.00 13.59           C  
-ATOM   1108  C   THR A 159      48.386  38.250  32.721  1.00 12.30           C  
-ATOM   1109  O   THR A 159      47.212  37.843  32.687  1.00 13.30           O  
-ATOM   1110  CB  THR A 159      48.863  40.238  31.206  1.00 14.21           C  
-ATOM   1111  OG1 THR A 159      47.474  40.482  31.134  1.00 16.33           O  
-ATOM   1112  CG2 THR A 159      49.479  40.707  29.901  1.00 15.33           C  
-ATOM   1113  N   LEU A 160      49.072  38.369  33.880  1.00 11.84           N  
-ATOM   1114  CA  LEU A 160      48.496  37.890  35.143  1.00 12.23           C  
-ATOM   1115  C   LEU A 160      47.179  38.597  35.455  1.00 11.95           C  
-ATOM   1116  O   LEU A 160      47.063  39.809  35.272  1.00 12.78           O  
-ATOM   1117  CB  LEU A 160      49.509  38.104  36.293  1.00 11.08           C  
-ATOM   1118  CG  LEU A 160      49.146  37.580  37.676  1.00 10.58           C  
-ATOM   1119  CD1 LEU A 160      49.052  36.061  37.608  1.00  8.70           C  
-ATOM   1120  CD2 LEU A 160      50.203  37.943  38.681  1.00 10.14           C  
-ATOM   1121  N   GLN A 161      46.164  37.806  35.817  1.00  8.13           N  
-ATOM   1122  CA  GLN A 161      44.839  38.318  36.151  1.00  9.83           C  
-ATOM   1123  C   GLN A 161      44.583  38.159  37.638  1.00 10.91           C  
-ATOM   1124  O   GLN A 161      45.180  37.282  38.280  1.00 11.00           O  
-ATOM   1125  CB  GLN A 161      43.691  37.548  35.461  1.00 10.26           C  
-ATOM   1126  CG  GLN A 161      43.752  37.452  33.946  1.00 12.31           C  
-ATOM   1127  CD  GLN A 161      43.575  38.796  33.267  1.00 13.11           C  
-ATOM   1128  OE1 GLN A 161      42.483  39.358  33.324  1.00 15.12           O  
-ATOM   1129  NE2 GLN A 161      44.620  39.310  32.628  1.00 15.95           N  
-ATOM   1130  N   GLN A 162      43.699  38.982  38.181  1.00 10.49           N  
-ATOM   1131  CA  GLN A 162      43.262  38.785  39.556  1.00 13.38           C  
-ATOM   1132  C   GLN A 162      41.767  39.000  39.660  1.00 12.98           C  
-ATOM   1133  O   GLN A 162      41.156  39.715  38.864  1.00 13.63           O  
-ATOM   1134  CB  GLN A 162      43.981  39.738  40.506  1.00 14.26           C  
-ATOM   1135  CG  GLN A 162      43.684  41.172  40.198  1.00 18.96           C  
-ATOM   1136  CD  GLN A 162      44.422  42.100  41.114  1.00 17.04           C  
-ATOM   1137  OE1 GLN A 162      45.636  42.113  41.175  1.00 18.54           O  
-ATOM   1138  NE2 GLN A 162      43.661  42.902  41.825  1.00 19.42           N  
-ATOM   1139  N   ALA A 163      41.127  38.327  40.599  1.00 13.23           N  
-ATOM   1140  CA  ALA A 163      39.695  38.494  40.792  1.00 13.22           C  
-ATOM   1141  C   ALA A 163      39.435  38.497  42.288  1.00 11.36           C  
-ATOM   1142  O   ALA A 163      40.101  37.777  43.036  1.00 11.21           O  
-ATOM   1143  CB  ALA A 163      38.880  37.350  40.176  1.00 14.42           C  
-ATOM   1144  N   TYR A 164      38.474  39.311  42.731  1.00 11.67           N  
-ATOM   1145  CA  TYR A 164      38.141  39.408  44.130  1.00 11.56           C  
-ATOM   1146  C   TYR A 164      37.231  38.243  44.395  1.00 10.80           C  
-ATOM   1147  O   TYR A 164      36.176  38.123  43.775  1.00 12.70           O  
-ATOM   1148  CB  TYR A 164      37.448  40.710  44.359  1.00 12.54           C  
-ATOM   1149  CG  TYR A 164      37.040  40.933  45.788  1.00 13.95           C  
-ATOM   1150  CD1 TYR A 164      38.014  41.027  46.791  1.00 17.97           C  
-ATOM   1151  CD2 TYR A 164      35.687  41.029  46.070  1.00 16.75           C  
-ATOM   1152  CE1 TYR A 164      37.615  41.220  48.101  1.00 18.03           C  
-ATOM   1153  CE2 TYR A 164      35.281  41.224  47.391  1.00 21.27           C  
-ATOM   1154  CZ  TYR A 164      36.248  41.318  48.402  1.00 22.57           C  
-ATOM   1155  OH  TYR A 164      35.833  41.496  49.724  1.00 26.64           O  
-ATOM   1156  N   LEU A 165      37.643  37.397  45.335  1.00  9.07           N  
-ATOM   1157  CA  LEU A 165      36.957  36.131  45.560  1.00 10.37           C  
-ATOM   1158  C   LEU A 165      36.810  35.914  47.063  1.00 11.29           C  
-ATOM   1159  O   LEU A 165      37.644  35.248  47.661  1.00 11.27           O  
-ATOM   1160  CB  LEU A 165      37.787  34.976  44.930  1.00 12.38           C  
-ATOM   1161  CG  LEU A 165      37.093  33.893  44.101  1.00 11.95           C  
-ATOM   1162  CD1 LEU A 165      36.540  34.532  42.852  1.00  9.43           C  
-ATOM   1163  CD2 LEU A 165      38.062  32.782  43.751  1.00  8.65           C  
-ATOM   1164  N   PRO A 166      35.818  36.492  47.729  1.00 11.82           N  
-ATOM   1165  CA  PRO A 166      35.583  36.361  49.163  1.00 13.01           C  
-ATOM   1166  C   PRO A 166      35.260  34.957  49.614  1.00 13.63           C  
-ATOM   1167  O   PRO A 166      34.616  34.224  48.863  1.00 12.83           O  
-ATOM   1168  CB  PRO A 166      34.462  37.318  49.422  1.00 15.56           C  
-ATOM   1169  CG  PRO A 166      33.694  37.392  48.119  1.00 16.69           C  
-ATOM   1170  CD  PRO A 166      34.823  37.368  47.118  1.00 14.04           C  
-ATOM   1171  N   THR A 167      35.620  34.550  50.821  1.00 14.28           N  
-ATOM   1172  CA  THR A 167      35.421  33.166  51.166  1.00 12.03           C  
-ATOM   1173  C   THR A 167      33.984  32.783  51.463  1.00 13.99           C  
-ATOM   1174  O   THR A 167      33.121  33.622  51.727  1.00 13.60           O  
-ATOM   1175  CB  THR A 167      36.327  32.814  52.346  1.00 14.28           C  
-ATOM   1176  OG1 THR A 167      35.813  33.542  53.453  1.00 12.69           O  
-ATOM   1177  CG2 THR A 167      37.805  33.108  52.083  1.00 14.31           C  
-ATOM   1178  N   VAL A 168      33.710  31.477  51.351  1.00 12.25           N  
-ATOM   1179  CA  VAL A 168      32.398  30.889  51.637  1.00 13.80           C  
-ATOM   1180  C   VAL A 168      32.787  29.872  52.697  1.00 16.47           C  
-ATOM   1181  O   VAL A 168      33.563  28.951  52.386  1.00 16.50           O  
-ATOM   1182  CB  VAL A 168      31.794  30.139  50.415  1.00 11.38           C  
-ATOM   1183  CG1 VAL A 168      30.432  29.638  50.754  1.00 12.27           C  
-ATOM   1184  CG2 VAL A 168      31.689  31.048  49.222  1.00 14.01           C  
-ATOM   1185  N   ASP A 169      32.285  29.980  53.941  1.00 16.38           N  
-ATOM   1186  CA  ASP A 169      32.769  29.053  54.947  1.00 18.65           C  
-ATOM   1187  C   ASP A 169      32.266  27.632  54.746  1.00 17.74           C  
-ATOM   1188  O   ASP A 169      31.359  27.388  53.953  1.00 17.72           O  
-ATOM   1189  CB  ASP A 169      32.409  29.582  56.344  1.00 19.48           C  
-ATOM   1190  CG  ASP A 169      30.968  29.641  56.817  1.00 24.59           C  
-ATOM   1191  OD1 ASP A 169      30.079  29.046  56.217  1.00 26.31           O  
-ATOM   1192  OD2 ASP A 169      30.738  30.291  57.834  1.00 24.58           O  
-ATOM   1193  N   TYR A 170      32.844  26.713  55.507  1.00 18.85           N  
-ATOM   1194  CA  TYR A 170      32.610  25.308  55.315  1.00 19.40           C  
-ATOM   1195  C   TYR A 170      31.175  24.909  55.488  1.00 20.05           C  
-ATOM   1196  O   TYR A 170      30.680  24.097  54.705  1.00 18.83           O  
-ATOM   1197  CB  TYR A 170      33.506  24.536  56.265  1.00 21.04           C  
-ATOM   1198  CG  TYR A 170      33.214  23.051  56.250  1.00 23.14           C  
-ATOM   1199  CD1 TYR A 170      33.602  22.282  55.145  1.00 26.72           C  
-ATOM   1200  CD2 TYR A 170      32.532  22.469  57.332  1.00 26.68           C  
-ATOM   1201  CE1 TYR A 170      33.314  20.920  55.119  1.00 25.93           C  
-ATOM   1202  CE2 TYR A 170      32.241  21.102  57.307  1.00 27.72           C  
-ATOM   1203  CZ  TYR A 170      32.645  20.334  56.199  1.00 28.85           C  
-ATOM   1204  OH  TYR A 170      32.446  18.960  56.205  1.00 27.20           O  
-ATOM   1205  N   ALA A 171      30.485  25.483  56.457  1.00 19.61           N  
-ATOM   1206  CA  ALA A 171      29.101  25.118  56.673  1.00 21.92           C  
-ATOM   1207  C   ALA A 171      28.224  25.480  55.490  1.00 23.01           C  
-ATOM   1208  O   ALA A 171      27.300  24.738  55.163  1.00 24.62           O  
-ATOM   1209  CB  ALA A 171      28.552  25.819  57.901  1.00 22.12           C  
-ATOM   1210  N   ILE A 172      28.501  26.598  54.811  1.00 22.62           N  
-ATOM   1211  CA  ILE A 172      27.740  26.953  53.626  1.00 22.20           C  
-ATOM   1212  C   ILE A 172      28.229  26.155  52.417  1.00 21.87           C  
-ATOM   1213  O   ILE A 172      27.414  25.602  51.661  1.00 23.60           O  
-ATOM   1214  CB  ILE A 172      27.877  28.447  53.367  1.00 23.58           C  
-ATOM   1215  CG1 ILE A 172      27.265  29.244  54.528  1.00 26.43           C  
-ATOM   1216  CG2 ILE A 172      27.127  28.796  52.093  1.00 23.26           C  
-ATOM   1217  CD1 ILE A 172      27.460  30.777  54.480  1.00 29.86           C  
-ATOM   1218  N   CYS A 173      29.550  26.023  52.248  1.00 20.25           N  
-ATOM   1219  CA  CYS A 173      30.085  25.356  51.077  1.00 19.04           C  
-ATOM   1220  C   CYS A 173      29.723  23.876  50.994  1.00 18.75           C  
-ATOM   1221  O   CYS A 173      29.491  23.342  49.908  1.00 16.80           O  
-ATOM   1222  CB  CYS A 173      31.593  25.525  51.061  1.00 17.25           C  
-ATOM   1223  SG  CYS A 173      32.221  25.307  49.374  1.00 14.89           S  
-ATOM   1224  N   SER A 174      29.611  23.206  52.138  1.00 18.61           N  
-ATOM   1225  CA  SER A 174      29.246  21.819  52.096  1.00 19.62           C  
-ATOM   1226  C   SER A 174      27.756  21.616  52.240  1.00 19.20           C  
-ATOM   1227  O   SER A 174      27.318  20.478  52.376  1.00 20.88           O  
-ATOM   1228  CB  SER A 174      30.015  21.085  53.173  1.00 19.00           C  
-ATOM   1229  OG  SER A 174      29.675  21.542  54.466  1.00 23.92           O  
-ATOM   1230  N   SER A 175      26.928  22.660  52.158  1.00 19.31           N  
-ATOM   1231  CA  SER A 175      25.500  22.463  52.244  1.00 19.81           C  
-ATOM   1232  C   SER A 175      25.071  21.940  50.890  1.00 22.90           C  
-ATOM   1233  O   SER A 175      25.757  22.156  49.872  1.00 22.99           O  
-ATOM   1234  CB  SER A 175      24.782  23.757  52.557  1.00 17.66           C  
-ATOM   1235  OG  SER A 175      24.702  24.666  51.472  1.00 22.90           O  
-ATOM   1236  N   SER A 176      23.950  21.222  50.843  1.00 25.07           N  
-ATOM   1237  CA  SER A 176      23.537  20.574  49.607  1.00 27.40           C  
-ATOM   1238  C   SER A 176      23.314  21.487  48.400  1.00 26.86           C  
-ATOM   1239  O   SER A 176      23.465  21.041  47.265  1.00 28.07           O  
-ATOM   1240  CB  SER A 176      22.275  19.739  49.916  1.00 30.02           C  
-ATOM   1241  OG  SER A 176      21.199  20.458  50.511  1.00 36.25           O  
-ATOM   1242  N   SER A 177      23.023  22.778  48.556  1.00 27.00           N  
-ATOM   1243  CA  SER A 177      22.851  23.663  47.403  1.00 27.03           C  
-ATOM   1244  C   SER A 177      24.156  24.169  46.760  1.00 25.15           C  
-ATOM   1245  O   SER A 177      24.150  24.736  45.662  1.00 24.45           O  
-ATOM   1246  CB  SER A 177      21.947  24.858  47.831  1.00 29.12           C  
-ATOM   1247  OG  SER A 177      22.066  25.296  49.188  1.00 35.57           O  
-ATOM   1248  N   TYR A 178      25.282  23.972  47.467  1.00 22.58           N  
-ATOM   1249  CA  TYR A 178      26.628  24.306  47.009  1.00 19.15           C  
-ATOM   1250  C   TYR A 178      27.369  23.040  46.614  1.00 17.43           C  
-ATOM   1251  O   TYR A 178      26.943  22.403  45.659  1.00 16.91           O  
-ATOM   1252  CB  TYR A 178      27.403  25.033  48.110  1.00 19.85           C  
-ATOM   1253  CG  TYR A 178      26.936  26.453  48.295  1.00 19.44           C  
-ATOM   1254  CD1 TYR A 178      25.648  26.697  48.769  1.00 20.35           C  
-ATOM   1255  CD2 TYR A 178      27.804  27.490  47.954  1.00 21.19           C  
-ATOM   1256  CE1 TYR A 178      25.208  28.000  48.907  1.00 23.84           C  
-ATOM   1257  CE2 TYR A 178      27.372  28.796  48.082  1.00 21.78           C  
-ATOM   1258  CZ  TYR A 178      26.078  29.036  48.552  1.00 25.26           C  
-ATOM   1259  OH  TYR A 178      25.630  30.337  48.640  1.00 29.53           O  
-ATOM   1260  N   TRP A 179      28.438  22.590  47.283  1.00 15.81           N  
-ATOM   1261  CA  TRP A 179      29.178  21.425  46.843  1.00 14.58           C  
-ATOM   1262  C   TRP A 179      28.825  20.158  47.577  1.00 15.60           C  
-ATOM   1263  O   TRP A 179      29.259  19.074  47.206  1.00 15.80           O  
-ATOM   1264  CB  TRP A 179      30.638  21.704  47.014  1.00 10.68           C  
-ATOM   1265  CG  TRP A 179      31.306  22.452  45.874  1.00 13.09           C  
-ATOM   1266  CD1 TRP A 179      31.641  23.789  45.945  1.00 12.92           C  
-ATOM   1267  CD2 TRP A 179      31.699  21.873  44.701  1.00 13.86           C  
-ATOM   1268  NE1 TRP A 179      32.262  24.051  44.808  1.00 12.64           N  
-ATOM   1269  CE2 TRP A 179      32.326  22.956  44.034  1.00 12.99           C  
-ATOM   1270  CE3 TRP A 179      31.605  20.616  44.123  1.00 13.14           C  
-ATOM   1271  CZ2 TRP A 179      32.881  22.776  42.753  1.00 12.21           C  
-ATOM   1272  CZ3 TRP A 179      32.149  20.444  42.847  1.00 15.91           C  
-ATOM   1273  CH2 TRP A 179      32.782  21.503  42.166  1.00 14.09           C  
-ATOM   1274  N   GLY A 180      28.074  20.277  48.664  1.00 15.83           N  
-ATOM   1275  CA  GLY A 180      27.719  19.125  49.483  1.00 16.58           C  
-ATOM   1276  C   GLY A 180      28.944  18.478  50.082  1.00 18.19           C  
-ATOM   1277  O   GLY A 180      29.944  19.129  50.416  1.00 18.94           O  
-ATOM   1278  N   SER A 181      28.839  17.145  50.120  1.00 19.51           N  
-ATOM   1279  CA  SER A 181      29.881  16.222  50.565  1.00 20.26           C  
-ATOM   1280  C   SER A 181      31.235  16.299  49.891  1.00 17.73           C  
-ATOM   1281  O   SER A 181      32.232  15.824  50.432  1.00 18.28           O  
-ATOM   1282  CB  SER A 181      29.466  14.766  50.390  1.00 22.21           C  
-ATOM   1283  OG  SER A 181      28.769  14.312  51.523  1.00 28.46           O  
-ATOM   1284  N   THR A 182      31.291  16.821  48.682  1.00 16.34           N  
-ATOM   1285  CA  THR A 182      32.539  16.864  47.951  1.00 15.15           C  
-ATOM   1286  C   THR A 182      33.515  17.765  48.670  1.00 13.10           C  
-ATOM   1287  O   THR A 182      34.690  17.421  48.625  1.00 14.50           O  
-ATOM   1288  CB  THR A 182      32.200  17.336  46.539  1.00 17.28           C  
-ATOM   1289  OG1 THR A 182      31.377  16.291  46.046  1.00 18.72           O  
-ATOM   1290  CG2 THR A 182      33.375  17.574  45.620  1.00 17.98           C  
-ATOM   1291  N   VAL A 183      33.120  18.855  49.356  1.00 11.33           N  
-ATOM   1292  CA  VAL A 183      34.165  19.646  50.033  1.00 12.21           C  
-ATOM   1293  C   VAL A 183      34.349  19.158  51.448  1.00 12.41           C  
-ATOM   1294  O   VAL A 183      33.427  18.725  52.124  1.00 15.19           O  
-ATOM   1295  CB  VAL A 183      33.888  21.174  50.102  1.00 14.68           C  
-ATOM   1296  CG1 VAL A 183      33.857  21.630  48.660  1.00 16.16           C  
-ATOM   1297  CG2 VAL A 183      32.628  21.552  50.801  1.00 16.59           C  
-ATOM   1298  N   LYS A 184      35.610  19.128  51.798  1.00 11.85           N  
-ATOM   1299  CA  LYS A 184      36.046  18.708  53.104  1.00 12.76           C  
-ATOM   1300  C   LYS A 184      36.480  19.966  53.849  1.00 14.30           C  
-ATOM   1301  O   LYS A 184      36.728  21.024  53.275  1.00 12.58           O  
-ATOM   1302  CB  LYS A 184      37.248  17.747  53.006  1.00 10.65           C  
-ATOM   1303  CG  LYS A 184      37.052  16.560  52.054  1.00 14.86           C  
-ATOM   1304  CD  LYS A 184      35.784  15.804  52.402  1.00 15.58           C  
-ATOM   1305  CE  LYS A 184      35.466  14.618  51.488  1.00 18.57           C  
-ATOM   1306  NZ  LYS A 184      35.004  15.001  50.158  1.00 16.58           N  
-ATOM   1307  N   ASN A 185      36.630  19.812  55.162  1.00 15.07           N  
-ATOM   1308  CA  ASN A 185      37.134  20.869  56.020  1.00 17.39           C  
-ATOM   1309  C   ASN A 185      38.643  21.147  55.792  1.00 14.69           C  
-ATOM   1310  O   ASN A 185      39.116  22.198  56.234  1.00 14.25           O  
-ATOM   1311  CB  ASN A 185      36.834  20.492  57.497  1.00 22.38           C  
-ATOM   1312  CG  ASN A 185      37.098  21.662  58.459  1.00 29.56           C  
-ATOM   1313  OD1 ASN A 185      37.642  21.428  59.538  1.00 34.55           O  
-ATOM   1314  ND2 ASN A 185      36.810  22.950  58.173  1.00 31.07           N  
-ATOM   1315  N   SER A 186      39.416  20.274  55.081  1.00 10.71           N  
-ATOM   1316  CA  SER A 186      40.789  20.543  54.657  1.00  9.08           C  
-ATOM   1317  C   SER A 186      40.816  21.433  53.386  1.00  8.56           C  
-ATOM   1318  O   SER A 186      41.870  21.577  52.757  1.00  8.90           O  
-ATOM   1319  CB  SER A 186      41.531  19.237  54.341  1.00  9.04           C  
-ATOM   1320  OG  SER A 186      40.846  18.549  53.296  1.00 10.97           O  
-ATOM   1321  N   MET A 187      39.692  22.023  52.979  1.00  7.52           N  
-ATOM   1322  CA  MET A 187      39.585  22.867  51.804  1.00 10.21           C  
-ATOM   1323  C   MET A 187      38.993  24.237  52.154  1.00 12.42           C  
-ATOM   1324  O   MET A 187      38.270  24.386  53.138  1.00 11.96           O  
-ATOM   1325  CB  MET A 187      38.671  22.216  50.791  1.00 10.94           C  
-ATOM   1326  CG  MET A 187      39.204  20.911  50.205  1.00 11.39           C  
-ATOM   1327  SD  MET A 187      37.858  20.000  49.438  1.00 10.12           S  
-ATOM   1328  CE  MET A 187      38.604  18.454  49.020  1.00 10.58           C  
-ATOM   1329  N   VAL A 188      39.304  25.263  51.350  1.00 12.50           N  
-ATOM   1330  CA  VAL A 188      38.697  26.598  51.432  1.00 13.07           C  
-ATOM   1331  C   VAL A 188      37.879  26.815  50.155  1.00 11.00           C  
-ATOM   1332  O   VAL A 188      38.297  26.453  49.077  1.00 13.48           O  
-ATOM   1333  CB  VAL A 188      39.768  27.717  51.529  1.00 13.39           C  
-ATOM   1334  CG1 VAL A 188      39.170  29.107  51.572  1.00 13.79           C  
-ATOM   1335  CG2 VAL A 188      40.536  27.482  52.798  1.00 12.84           C  
-ATOM   1336  N   CYS A 189      36.697  27.373  50.265  1.00 12.00           N  
-ATOM   1337  CA  CYS A 189      35.841  27.710  49.152  1.00 11.22           C  
-ATOM   1338  C   CYS A 189      35.862  29.210  49.013  1.00 12.82           C  
-ATOM   1339  O   CYS A 189      35.793  29.898  50.024  1.00 11.42           O  
-ATOM   1340  CB  CYS A 189      34.411  27.300  49.402  1.00 13.78           C  
-ATOM   1341  SG  CYS A 189      34.212  25.515  49.558  1.00 12.57           S  
-ATOM   1342  N   ALA A 190      35.977  29.752  47.793  1.00 11.38           N  
-ATOM   1343  CA  ALA A 190      35.901  31.199  47.611  1.00 10.48           C  
-ATOM   1344  C   ALA A 190      35.139  31.493  46.321  1.00 10.01           C  
-ATOM   1345  O   ALA A 190      35.229  30.723  45.356  1.00 10.78           O  
-ATOM   1346  CB  ALA A 190      37.304  31.764  47.552  1.00  7.99           C  
-ATOM   1347  N   GLY A 191      34.278  32.528  46.318  1.00  9.54           N  
-ATOM   1348  CA  GLY A 191      33.535  32.923  45.138  1.00 10.94           C  
-ATOM   1349  C   GLY A 191      32.145  32.340  45.049  1.00 11.49           C  
-ATOM   1350  O   GLY A 191      31.391  32.402  46.015  1.00 15.03           O  
-ATOM   1351  N   GLY A 192      31.795  31.810  43.883  1.00 11.09           N  
-ATOM   1352  CA  GLY A 192      30.468  31.222  43.705  1.00 11.75           C  
-ATOM   1353  C   GLY A 192      29.407  32.187  43.205  1.00 13.13           C  
-ATOM   1354  O   GLY A 192      28.250  31.816  43.138  1.00 12.39           O  
-ATOM   1355  N   ASP A 193      29.761  33.422  42.839  1.00 14.59           N  
-ATOM   1356  CA  ASP A 193      28.770  34.392  42.363  1.00 16.42           C  
-ATOM   1357  C   ASP A 193      28.282  34.182  40.922  1.00 17.95           C  
-ATOM   1358  O   ASP A 193      27.339  34.831  40.484  1.00 20.10           O  
-ATOM   1359  CB  ASP A 193      29.326  35.854  42.519  1.00 17.13           C  
-ATOM   1360  CG  ASP A 193      30.544  36.360  41.725  1.00 19.55           C  
-ATOM   1361  OD1 ASP A 193      31.034  35.665  40.846  1.00 19.13           O  
-ATOM   1362  OD2 ASP A 193      31.043  37.457  41.995  1.00 20.30           O  
-ATOM   1363  N   GLY A 194      28.878  33.264  40.170  1.00 17.24           N  
-ATOM   1364  CA  GLY A 194      28.495  33.016  38.790  1.00 17.43           C  
-ATOM   1365  C   GLY A 194      29.245  33.916  37.820  1.00 18.50           C  
-ATOM   1366  O   GLY A 194      29.095  33.748  36.617  1.00 21.56           O  
-ATOM   1367  N   VAL A 195      30.084  34.850  38.281  1.00 16.91           N  
-ATOM   1368  CA  VAL A 195      30.838  35.793  37.447  1.00 16.26           C  
-ATOM   1369  C   VAL A 195      32.346  35.605  37.463  1.00 15.66           C  
-ATOM   1370  O   VAL A 195      33.052  35.707  36.457  1.00 15.31           O  
-ATOM   1371  CB  VAL A 195      30.553  37.275  37.882  1.00 15.62           C  
-ATOM   1372  CG1 VAL A 195      31.218  38.227  36.885  1.00 12.84           C  
-ATOM   1373  CG2 VAL A 195      29.042  37.511  37.993  1.00 17.52           C  
-ATOM   1374  N   ARG A 196      32.829  35.354  38.673  1.00 14.43           N  
-ATOM   1375  CA  ARG A 196      34.244  35.333  38.967  1.00 13.75           C  
-ATOM   1376  C   ARG A 196      34.619  33.972  39.483  1.00 10.11           C  
-ATOM   1377  O   ARG A 196      33.910  33.436  40.322  1.00 11.55           O  
-ATOM   1378  CB  ARG A 196      34.598  36.365  40.036  1.00 16.23           C  
-ATOM   1379  CG  ARG A 196      34.460  37.700  39.378  1.00 21.25           C  
-ATOM   1380  CD  ARG A 196      34.743  38.820  40.316  1.00 20.80           C  
-ATOM   1381  NE  ARG A 196      33.700  38.932  41.323  1.00 21.73           N  
-ATOM   1382  CZ  ARG A 196      33.610  40.024  42.086  1.00 22.00           C  
-ATOM   1383  NH1 ARG A 196      34.467  41.054  41.927  1.00 20.62           N  
-ATOM   1384  NH2 ARG A 196      32.717  40.033  43.077  1.00 21.75           N  
-ATOM   1385  N   SER A 197      35.713  33.421  38.988  1.00 10.11           N  
-ATOM   1386  CA  SER A 197      36.198  32.147  39.479  1.00  9.45           C  
-ATOM   1387  C   SER A 197      37.592  31.883  39.001  1.00  6.91           C  
-ATOM   1388  O   SER A 197      38.159  32.562  38.140  1.00  9.22           O  
-ATOM   1389  CB  SER A 197      35.297  31.007  38.996  1.00 12.93           C  
-ATOM   1390  OG  SER A 197      35.336  30.935  37.577  1.00 20.65           O  
-ATOM   1391  N   GLY A 198      38.160  30.827  39.565  1.00  7.32           N  
-ATOM   1392  CA  GLY A 198      39.364  30.208  39.003  1.00  8.03           C  
-ATOM   1393  C   GLY A 198      38.972  29.406  37.764  1.00  7.77           C  
-ATOM   1394  O   GLY A 198      37.780  29.191  37.521  1.00 11.00           O  
-ATOM   1395  N   CYS A 199      39.901  28.961  36.939  1.00  8.22           N  
-ATOM   1396  CA  CYS A 199      39.509  28.154  35.759  1.00  8.73           C  
-ATOM   1397  C   CYS A 199      40.744  27.340  35.398  1.00  8.78           C  
-ATOM   1398  O   CYS A 199      41.796  27.568  35.999  1.00 10.58           O  
-ATOM   1399  CB  CYS A 199      39.096  29.056  34.534  1.00  9.70           C  
-ATOM   1400  SG  CYS A 199      37.954  28.233  33.374  1.00 10.88           S  
-ATOM   1401  N   GLN A 200      40.713  26.389  34.451  1.00 10.41           N  
-ATOM   1402  CA  GLN A 200      41.885  25.592  34.095  1.00  9.08           C  
-ATOM   1403  C   GLN A 200      43.107  26.415  33.856  1.00  9.28           C  
-ATOM   1404  O   GLN A 200      42.942  27.456  33.234  1.00 10.66           O  
-ATOM   1405  CB  GLN A 200      41.655  24.810  32.835  1.00 15.06           C  
-ATOM   1406  CG  GLN A 200      40.680  23.683  33.098  1.00 23.03           C  
-ATOM   1407  CD  GLN A 200      39.292  24.017  32.633  1.00 28.01           C  
-ATOM   1408  OE1 GLN A 200      38.840  23.535  31.590  1.00 34.19           O  
-ATOM   1409  NE2 GLN A 200      38.569  24.812  33.404  1.00 30.17           N  
-ATOM   1410  N   GLY A 201      44.286  26.022  34.354  1.00  5.85           N  
-ATOM   1411  CA  GLY A 201      45.546  26.785  34.241  1.00  7.92           C  
-ATOM   1412  C   GLY A 201      45.821  27.690  35.457  1.00  5.59           C  
-ATOM   1413  O   GLY A 201      46.904  28.245  35.569  1.00  8.61           O  
-ATOM   1414  N   ASP A 202      44.808  27.926  36.298  1.00  7.47           N  
-ATOM   1415  CA  ASP A 202      44.988  28.610  37.575  1.00  6.56           C  
-ATOM   1416  C   ASP A 202      45.353  27.604  38.678  1.00  9.54           C  
-ATOM   1417  O   ASP A 202      45.887  27.999  39.703  1.00  6.94           O  
-ATOM   1418  CB  ASP A 202      43.733  29.345  38.003  1.00  6.07           C  
-ATOM   1419  CG  ASP A 202      43.380  30.501  37.103  1.00  4.86           C  
-ATOM   1420  OD1 ASP A 202      44.282  31.198  36.652  1.00  8.85           O  
-ATOM   1421  OD2 ASP A 202      42.199  30.695  36.860  1.00  7.20           O  
-ATOM   1422  N   SER A 203      45.120  26.301  38.460  1.00 12.03           N  
-ATOM   1423  CA  SER A 203      45.496  25.184  39.340  1.00 11.28           C  
-ATOM   1424  C   SER A 203      46.832  25.356  40.015  1.00  8.97           C  
-ATOM   1425  O   SER A 203      47.781  25.791  39.370  1.00  7.68           O  
-ATOM   1426  CB  SER A 203      45.580  23.890  38.534  1.00 13.93           C  
-ATOM   1427  OG  SER A 203      44.314  23.381  38.110  1.00 16.67           O  
-ATOM   1428  N   GLY A 204      46.951  25.077  41.300  1.00  7.04           N  
-ATOM   1429  CA  GLY A 204      48.247  25.158  41.935  1.00  6.36           C  
-ATOM   1430  C   GLY A 204      48.566  26.524  42.502  1.00  7.46           C  
-ATOM   1431  O   GLY A 204      49.417  26.631  43.396  1.00  6.58           O  
-ATOM   1432  N   GLY A 205      47.878  27.567  41.978  1.00  7.72           N  
-ATOM   1433  CA  GLY A 205      48.228  28.922  42.354  1.00  6.49           C  
-ATOM   1434  C   GLY A 205      47.653  29.337  43.694  1.00  7.96           C  
-ATOM   1435  O   GLY A 205      46.865  28.597  44.306  1.00  9.08           O  
-ATOM   1436  N   PRO A 206      48.010  30.549  44.151  1.00  7.38           N  
-ATOM   1437  CA  PRO A 206      47.538  31.146  45.403  1.00  6.75           C  
-ATOM   1438  C   PRO A 206      46.131  31.751  45.478  1.00  7.46           C  
-ATOM   1439  O   PRO A 206      45.570  32.262  44.485  1.00  6.98           O  
-ATOM   1440  CB  PRO A 206      48.619  32.164  45.712  1.00  3.94           C  
-ATOM   1441  CG  PRO A 206      48.841  32.717  44.308  1.00  7.28           C  
-ATOM   1442  CD  PRO A 206      48.937  31.463  43.457  1.00  4.71           C  
-ATOM   1443  N   LEU A 207      45.556  31.637  46.682  1.00  6.01           N  
-ATOM   1444  CA  LEU A 207      44.400  32.439  47.073  1.00  6.18           C  
-ATOM   1445  C   LEU A 207      45.077  33.308  48.157  1.00  7.30           C  
-ATOM   1446  O   LEU A 207      45.624  32.791  49.148  1.00  7.76           O  
-ATOM   1447  CB  LEU A 207      43.247  31.589  47.693  1.00  5.97           C  
-ATOM   1448  CG  LEU A 207      41.992  32.358  48.218  1.00  4.05           C  
-ATOM   1449  CD1 LEU A 207      41.246  33.024  47.068  1.00  6.67           C  
-ATOM   1450  CD2 LEU A 207      41.077  31.399  48.970  1.00  7.99           C  
-ATOM   1451  N   HIS A 208      45.156  34.627  47.931  1.00  7.62           N  
-ATOM   1452  CA  HIS A 208      45.818  35.576  48.844  1.00  7.94           C  
-ATOM   1453  C   HIS A 208      44.728  36.187  49.672  1.00  8.26           C  
-ATOM   1454  O   HIS A 208      43.806  36.778  49.103  1.00  8.96           O  
-ATOM   1455  CB  HIS A 208      46.483  36.740  48.138  1.00  6.17           C  
-ATOM   1456  CG  HIS A 208      47.324  36.319  46.959  1.00  9.32           C  
-ATOM   1457  ND1 HIS A 208      48.604  35.971  46.999  1.00  8.26           N  
-ATOM   1458  CD2 HIS A 208      46.916  36.270  45.636  1.00 10.85           C  
-ATOM   1459  CE1 HIS A 208      49.011  35.724  45.759  1.00 10.58           C  
-ATOM   1460  NE2 HIS A 208      47.979  35.909  44.963  1.00 12.70           N  
-ATOM   1461  N   CYS A 209      44.794  36.094  51.003  1.00 10.31           N  
-ATOM   1462  CA  CYS A 209      43.768  36.662  51.874  1.00  9.59           C  
-ATOM   1463  C   CYS A 209      44.396  37.619  52.867  1.00 10.04           C  
-ATOM   1464  O   CYS A 209      45.472  37.361  53.397  1.00  9.32           O  
-ATOM   1465  CB  CYS A 209      43.045  35.584  52.653  1.00 10.10           C  
-ATOM   1466  SG  CYS A 209      42.199  34.388  51.566  1.00 10.46           S  
-ATOM   1467  N   LEU A 210      43.710  38.746  53.064  1.00 12.01           N  
-ATOM   1468  CA  LEU A 210      44.150  39.791  53.975  1.00 16.22           C  
-ATOM   1469  C   LEU A 210      43.758  39.469  55.432  1.00 16.11           C  
-ATOM   1470  O   LEU A 210      42.593  39.391  55.823  1.00 16.56           O  
-ATOM   1471  CB  LEU A 210      43.540  41.143  53.518  1.00 18.02           C  
-ATOM   1472  CG  LEU A 210      44.065  42.433  54.201  1.00 21.65           C  
-ATOM   1473  CD1 LEU A 210      45.570  42.555  53.951  1.00 22.49           C  
-ATOM   1474  CD2 LEU A 210      43.335  43.663  53.655  1.00 21.54           C  
-ATOM   1475  N   VAL A 211      44.793  39.255  56.242  1.00 16.99           N  
-ATOM   1476  CA  VAL A 211      44.675  38.906  57.646  1.00 19.04           C  
-ATOM   1477  C   VAL A 211      45.700  39.779  58.367  1.00 18.36           C  
-ATOM   1478  O   VAL A 211      46.889  39.687  58.062  1.00 18.05           O  
-ATOM   1479  CB  VAL A 211      45.020  37.417  57.848  1.00 22.08           C  
-ATOM   1480  CG1 VAL A 211      45.077  37.062  59.313  1.00 23.93           C  
-ATOM   1481  CG2 VAL A 211      43.955  36.568  57.209  1.00 22.44           C  
-ATOM   1482  N   ASN A 212      45.276  40.627  59.315  1.00 18.74           N  
-ATOM   1483  CA  ASN A 212      46.155  41.475  60.132  1.00 19.98           C  
-ATOM   1484  C   ASN A 212      47.094  42.352  59.310  1.00 17.73           C  
-ATOM   1485  O   ASN A 212      48.302  42.401  59.529  1.00 18.87           O  
-ATOM   1486  CB  ASN A 212      47.006  40.618  61.097  1.00 23.71           C  
-ATOM   1487  CG  ASN A 212      46.182  39.752  62.055  1.00 29.76           C  
-ATOM   1488  OD1 ASN A 212      46.465  38.561  62.278  1.00 32.63           O  
-ATOM   1489  ND2 ASN A 212      45.134  40.342  62.634  1.00 31.27           N  
-ATOM   1490  N   GLY A 213      46.493  42.964  58.294  1.00 14.91           N  
-ATOM   1491  CA  GLY A 213      47.178  43.897  57.444  1.00 11.87           C  
-ATOM   1492  C   GLY A 213      48.185  43.275  56.525  1.00 14.76           C  
-ATOM   1493  O   GLY A 213      48.959  43.999  55.912  1.00 15.07           O  
-ATOM   1494  N   GLN A 214      48.179  41.950  56.359  1.00 14.17           N  
-ATOM   1495  CA  GLN A 214      49.205  41.263  55.586  1.00 15.43           C  
-ATOM   1496  C   GLN A 214      48.533  40.284  54.615  1.00 14.62           C  
-ATOM   1497  O   GLN A 214      47.610  39.603  55.041  1.00 14.30           O  
-ATOM   1498  CB  GLN A 214      50.066  40.555  56.605  1.00 15.94           C  
-ATOM   1499  CG  GLN A 214      51.264  39.860  56.048  1.00 19.80           C  
-ATOM   1500  CD  GLN A 214      52.128  39.170  57.107  1.00 20.39           C  
-ATOM   1501  OE1 GLN A 214      53.320  39.473  57.259  1.00 24.35           O  
-ATOM   1502  NE2 GLN A 214      51.558  38.197  57.822  1.00 22.43           N  
-ATOM   1503  N   TYR A 215      48.833  40.202  53.315  1.00 14.11           N  
-ATOM   1504  CA  TYR A 215      48.265  39.149  52.483  1.00 13.61           C  
-ATOM   1505  C   TYR A 215      48.968  37.829  52.723  1.00 12.39           C  
-ATOM   1506  O   TYR A 215      50.180  37.793  52.619  1.00 14.64           O  
-ATOM   1507  CB  TYR A 215      48.425  39.498  51.061  1.00 14.44           C  
-ATOM   1508  CG  TYR A 215      47.258  40.356  50.629  1.00 17.88           C  
-ATOM   1509  CD1 TYR A 215      46.036  39.744  50.371  1.00 16.16           C  
-ATOM   1510  CD2 TYR A 215      47.408  41.735  50.451  1.00 21.97           C  
-ATOM   1511  CE1 TYR A 215      44.961  40.494  49.925  1.00 19.19           C  
-ATOM   1512  CE2 TYR A 215      46.325  42.500  50.006  1.00 24.30           C  
-ATOM   1513  CZ  TYR A 215      45.117  41.856  49.746  1.00 24.11           C  
-ATOM   1514  OH  TYR A 215      44.033  42.565  49.282  1.00 30.65           O  
-ATOM   1515  N   ALA A 216      48.285  36.763  53.100  1.00 11.17           N  
-ATOM   1516  CA  ALA A 216      48.944  35.488  53.251  1.00  8.90           C  
-ATOM   1517  C   ALA A 216      48.295  34.521  52.289  1.00  9.12           C  
-ATOM   1518  O   ALA A 216      47.155  34.705  51.878  1.00  6.94           O  
-ATOM   1519  CB  ALA A 216      48.780  34.987  54.667  1.00  9.71           C  
-ATOM   1520  N   VAL A 217      49.005  33.475  51.896  1.00  9.17           N  
-ATOM   1521  CA  VAL A 217      48.483  32.483  50.937  1.00  9.15           C  
-ATOM   1522  C   VAL A 217      47.743  31.400  51.731  1.00  8.85           C  
-ATOM   1523  O   VAL A 217      48.356  30.558  52.388  1.00 10.09           O  
-ATOM   1524  CB  VAL A 217      49.665  31.869  50.140  1.00 12.18           C  
-ATOM   1525  CG1 VAL A 217      49.106  30.837  49.159  1.00 11.76           C  
-ATOM   1526  CG2 VAL A 217      50.492  32.965  49.462  1.00 10.13           C  
-ATOM   1527  N   HIS A 218      46.408  31.436  51.679  1.00  7.84           N  
-ATOM   1528  CA  HIS A 218      45.553  30.528  52.425  1.00  7.30           C  
-ATOM   1529  C   HIS A 218      45.050  29.356  51.584  1.00  8.46           C  
-ATOM   1530  O   HIS A 218      44.526  28.366  52.131  1.00  8.23           O  
-ATOM   1531  CB  HIS A 218      44.340  31.284  52.967  1.00  8.92           C  
-ATOM   1532  CG  HIS A 218      44.628  32.019  54.279  1.00 10.64           C  
-ATOM   1533  ND1 HIS A 218      44.180  31.691  55.493  1.00 10.75           N  
-ATOM   1534  CD2 HIS A 218      45.483  33.092  54.419  1.00 14.34           C  
-ATOM   1535  CE1 HIS A 218      44.743  32.506  56.359  1.00 14.78           C  
-ATOM   1536  NE2 HIS A 218      45.531  33.354  55.706  1.00 12.41           N  
-ATOM   1537  N   GLY A 219      45.180  29.445  50.250  1.00  7.23           N  
-ATOM   1538  CA  GLY A 219      44.659  28.367  49.401  1.00  6.28           C  
-ATOM   1539  C   GLY A 219      45.628  27.993  48.288  1.00  5.34           C  
-ATOM   1540  O   GLY A 219      46.475  28.794  47.905  1.00  6.80           O  
-ATOM   1541  N   VAL A 220      45.573  26.746  47.822  1.00  7.32           N  
-ATOM   1542  CA  VAL A 220      46.273  26.292  46.615  1.00  5.62           C  
-ATOM   1543  C   VAL A 220      45.097  25.897  45.701  1.00  6.97           C  
-ATOM   1544  O   VAL A 220      44.303  25.011  46.059  1.00  5.93           O  
-ATOM   1545  CB  VAL A 220      47.187  25.074  46.930  1.00  6.49           C  
-ATOM   1546  CG1 VAL A 220      47.723  24.488  45.651  1.00  7.98           C  
-ATOM   1547  CG2 VAL A 220      48.425  25.493  47.714  1.00  7.83           C  
-ATOM   1548  N   THR A 221      44.896  26.517  44.525  1.00  6.24           N  
-ATOM   1549  CA  THR A 221      43.697  26.257  43.694  1.00  7.32           C  
-ATOM   1550  C   THR A 221      43.632  24.790  43.246  1.00  7.97           C  
-ATOM   1551  O   THR A 221      44.609  24.220  42.746  1.00  8.36           O  
-ATOM   1552  CB  THR A 221      43.699  27.186  42.439  1.00  9.07           C  
-ATOM   1553  OG1 THR A 221      43.998  28.538  42.827  1.00  9.53           O  
-ATOM   1554  CG2 THR A 221      42.359  27.127  41.752  1.00  5.81           C  
-ATOM   1555  N   SER A 222      42.478  24.167  43.465  1.00  8.65           N  
-ATOM   1556  CA  SER A 222      42.342  22.742  43.256  1.00  9.57           C  
-ATOM   1557  C   SER A 222      41.283  22.365  42.225  1.00  9.40           C  
-ATOM   1558  O   SER A 222      41.618  21.664  41.264  1.00 11.94           O  
-ATOM   1559  CB  SER A 222      42.014  22.028  44.615  1.00 10.44           C  
-ATOM   1560  OG  SER A 222      41.964  20.601  44.518  1.00  7.17           O  
-ATOM   1561  N   PHE A 223      40.015  22.755  42.350  1.00  8.26           N  
-ATOM   1562  CA  PHE A 223      39.055  22.358  41.358  1.00  9.14           C  
-ATOM   1563  C   PHE A 223      37.867  23.321  41.302  1.00 10.35           C  
-ATOM   1564  O   PHE A 223      37.628  24.147  42.198  1.00  9.64           O  
-ATOM   1565  CB  PHE A 223      38.609  20.871  41.646  1.00 11.15           C  
-ATOM   1566  CG  PHE A 223      37.853  20.540  42.948  1.00 11.44           C  
-ATOM   1567  CD1 PHE A 223      36.468  20.640  42.988  1.00 10.26           C  
-ATOM   1568  CD2 PHE A 223      38.546  20.139  44.094  1.00 12.61           C  
-ATOM   1569  CE1 PHE A 223      35.764  20.354  44.151  1.00  9.32           C  
-ATOM   1570  CE2 PHE A 223      37.825  19.861  45.254  1.00  9.67           C  
-ATOM   1571  CZ  PHE A 223      36.444  19.968  45.285  1.00  9.35           C  
-ATOM   1572  N   VAL A 224      37.205  23.238  40.143  1.00  7.66           N  
-ATOM   1573  CA  VAL A 224      35.974  23.926  39.837  1.00  8.11           C  
-ATOM   1574  C   VAL A 224      34.993  22.874  39.315  1.00  8.11           C  
-ATOM   1575  O   VAL A 224      35.315  21.698  39.126  1.00  9.71           O  
-ATOM   1576  CB  VAL A 224      36.170  25.046  38.756  1.00  8.31           C  
-ATOM   1577  CG1 VAL A 224      36.999  26.192  39.339  1.00  8.77           C  
-ATOM   1578  CG2 VAL A 224      36.889  24.517  37.531  1.00 10.84           C  
-ATOM   1579  N   SER A 225      33.761  23.296  39.101  1.00 10.38           N  
-ATOM   1580  CA  SER A 225      32.715  22.444  38.562  1.00 12.28           C  
-ATOM   1581  C   SER A 225      33.063  21.936  37.174  1.00 14.77           C  
-ATOM   1582  O   SER A 225      33.660  22.645  36.369  1.00 12.00           O  
-ATOM   1583  CB  SER A 225      31.448  23.248  38.492  1.00 14.44           C  
-ATOM   1584  OG  SER A 225      30.392  22.488  37.935  1.00 13.00           O  
-ATOM   1585  N   ARG A 226      32.699  20.687  36.902  1.00 17.12           N  
-ATOM   1586  CA  ARG A 226      32.858  20.143  35.565  1.00 18.88           C  
-ATOM   1587  C   ARG A 226      31.826  20.845  34.693  1.00 18.19           C  
-ATOM   1588  O   ARG A 226      32.024  20.845  33.488  1.00 19.46           O  
-ATOM   1589  CB AARG A 226      32.636  18.611  35.532  0.50 18.28           C  
-ATOM   1590  CB BARG A 226      32.590  18.632  35.482  0.50 18.93           C  
-ATOM   1591  CG AARG A 226      31.274  18.031  35.871  0.50 19.97           C  
-ATOM   1592  CG BARG A 226      31.198  18.143  35.851  0.50 21.01           C  
-ATOM   1593  CD AARG A 226      31.123  16.550  35.440  0.50 21.61           C  
-ATOM   1594  CD BARG A 226      30.827  16.839  35.111  0.50 23.47           C  
-ATOM   1595  NE AARG A 226      29.720  16.126  35.490  0.50 19.41           N  
-ATOM   1596  NE BARG A 226      29.972  15.985  35.932  0.50 20.33           N  
-ATOM   1597  CZ AARG A 226      28.822  16.412  34.535  0.50 19.53           C  
-ATOM   1598  CZ BARG A 226      30.508  15.244  36.903  0.50 19.45           C  
-ATOM   1599  NH1AARG A 226      29.112  17.100  33.426  0.50 18.71           N  
-ATOM   1600  NH1BARG A 226      31.826  15.276  37.111  0.50 22.46           N  
-ATOM   1601  NH2AARG A 226      27.558  16.055  34.720  0.50 20.95           N  
-ATOM   1602  NH2BARG A 226      29.738  14.534  37.714  0.50 11.80           N  
-ATOM   1603  N   LEU A 227      30.761  21.462  35.235  1.00 17.41           N  
-ATOM   1604  CA  LEU A 227      29.799  22.189  34.417  1.00 18.32           C  
-ATOM   1605  C   LEU A 227      30.280  23.526  33.867  1.00 19.58           C  
-ATOM   1606  O   LEU A 227      29.765  24.026  32.857  1.00 21.27           O  
-ATOM   1607  CB  LEU A 227      28.570  22.446  35.200  1.00 19.76           C  
-ATOM   1608  CG  LEU A 227      27.946  21.156  35.747  1.00 24.84           C  
-ATOM   1609  CD1 LEU A 227      26.872  21.537  36.753  1.00 27.60           C  
-ATOM   1610  CD2 LEU A 227      27.428  20.276  34.617  1.00 23.53           C  
-ATOM   1611  N   GLY A 228      31.285  24.109  34.509  1.00 16.77           N  
-ATOM   1612  CA  GLY A 228      31.799  25.392  34.104  1.00 13.99           C  
-ATOM   1613  C   GLY A 228      32.636  25.950  35.224  1.00 10.47           C  
-ATOM   1614  O   GLY A 228      32.480  25.567  36.365  1.00 10.66           O  
-ATOM   1615  N   CYS A 229      33.551  26.837  34.870  1.00 10.47           N  
-ATOM   1616  CA  CYS A 229      34.368  27.501  35.845  1.00  9.12           C  
-ATOM   1617  C   CYS A 229      33.579  28.478  36.699  1.00  9.74           C  
-ATOM   1618  O   CYS A 229      33.635  28.351  37.904  1.00 11.86           O  
-ATOM   1619  CB  CYS A 229      35.461  28.201  35.116  1.00  5.24           C  
-ATOM   1620  SG  CYS A 229      36.647  27.064  34.364  1.00  9.50           S  
-ATOM   1621  N   ASN A 230      32.806  29.430  36.175  1.00 12.90           N  
-ATOM   1622  CA  ASN A 230      32.052  30.403  36.965  1.00 11.67           C  
-ATOM   1623  C   ASN A 230      30.624  29.969  37.036  1.00 13.70           C  
-ATOM   1624  O   ASN A 230      29.784  30.262  36.200  1.00 18.68           O  
-ATOM   1625  CB  ASN A 230      32.150  31.779  36.328  1.00 12.51           C  
-ATOM   1626  CG  ASN A 230      31.776  31.810  34.847  1.00 14.26           C  
-ATOM   1627  OD1 ASN A 230      32.319  31.047  34.041  1.00 13.98           O  
-ATOM   1628  ND2 ASN A 230      30.828  32.648  34.433  1.00 14.78           N  
-ATOM   1629  N   VAL A 231      30.309  29.176  38.027  1.00 15.22           N  
-ATOM   1630  CA  VAL A 231      28.962  28.665  38.205  1.00 17.57           C  
-ATOM   1631  C   VAL A 231      28.460  29.105  39.581  1.00 18.17           C  
-ATOM   1632  O   VAL A 231      29.160  29.026  40.604  1.00 18.32           O  
-ATOM   1633  CB  VAL A 231      29.033  27.119  38.028  1.00 18.26           C  
-ATOM   1634  CG1 VAL A 231      27.718  26.430  38.416  1.00 19.20           C  
-ATOM   1635  CG2 VAL A 231      29.253  26.822  36.552  1.00 18.38           C  
-ATOM   1636  N   THR A 232      27.252  29.684  39.547  1.00 19.07           N  
-ATOM   1637  CA  THR A 232      26.557  30.130  40.750  1.00 22.11           C  
-ATOM   1638  C   THR A 232      26.427  28.953  41.724  1.00 21.83           C  
-ATOM   1639  O   THR A 232      26.035  27.833  41.361  1.00 21.80           O  
-ATOM   1640  CB  THR A 232      25.152  30.674  40.380  1.00 23.60           C  
-ATOM   1641  OG1 THR A 232      25.324  31.816  39.534  1.00 26.85           O  
-ATOM   1642  CG2 THR A 232      24.377  31.112  41.603  1.00 26.52           C  
-ATOM   1643  N   ARG A 233      26.805  29.244  42.976  1.00 20.88           N  
-ATOM   1644  CA  ARG A 233      26.821  28.277  44.076  1.00 21.90           C  
-ATOM   1645  C   ARG A 233      27.770  27.111  43.913  1.00 19.36           C  
-ATOM   1646  O   ARG A 233      27.629  26.100  44.590  1.00 18.62           O  
-ATOM   1647  CB  ARG A 233      25.423  27.699  44.343  1.00 25.56           C  
-ATOM   1648  CG  ARG A 233      24.583  28.792  44.884  1.00 29.13           C  
-ATOM   1649  CD  ARG A 233      23.164  28.370  45.144  1.00 37.78           C  
-ATOM   1650  NE  ARG A 233      22.633  29.481  45.910  1.00 47.82           N  
-ATOM   1651  CZ  ARG A 233      22.098  30.584  45.350  1.00 53.44           C  
-ATOM   1652  NH1 ARG A 233      21.979  30.739  44.010  1.00 54.84           N  
-ATOM   1653  NH2 ARG A 233      21.777  31.606  46.168  1.00 56.42           N  
-ATOM   1654  N   LYS A 234      28.756  27.231  43.015  1.00 16.50           N  
-ATOM   1655  CA  LYS A 234      29.833  26.254  42.974  1.00 14.24           C  
-ATOM   1656  C   LYS A 234      31.094  27.079  43.073  1.00 12.98           C  
-ATOM   1657  O   LYS A 234      31.812  27.264  42.098  1.00 11.14           O  
-ATOM   1658  CB  LYS A 234      29.881  25.453  41.686  1.00 13.88           C  
-ATOM   1659  CG  LYS A 234      28.765  24.457  41.559  1.00 20.97           C  
-ATOM   1660  CD  LYS A 234      29.059  23.243  42.404  1.00 24.77           C  
-ATOM   1661  CE  LYS A 234      27.987  22.184  42.249  1.00 31.09           C  
-ATOM   1662  NZ  LYS A 234      26.726  22.697  42.765  1.00 35.24           N  
-ATOM   1663  N   PRO A 235      31.448  27.607  44.239  1.00 12.98           N  
-ATOM   1664  CA  PRO A 235      32.662  28.391  44.392  1.00 11.47           C  
-ATOM   1665  C   PRO A 235      33.895  27.618  44.007  1.00 10.04           C  
-ATOM   1666  O   PRO A 235      33.837  26.388  43.918  1.00  9.33           O  
-ATOM   1667  CB  PRO A 235      32.591  28.818  45.835  1.00 11.41           C  
-ATOM   1668  CG  PRO A 235      31.722  27.811  46.523  1.00 13.56           C  
-ATOM   1669  CD  PRO A 235      30.701  27.457  45.487  1.00 11.50           C  
-ATOM   1670  N   THR A 236      34.982  28.324  43.701  1.00  7.10           N  
-ATOM   1671  CA  THR A 236      36.247  27.684  43.400  1.00  7.02           C  
-ATOM   1672  C   THR A 236      36.744  27.023  44.699  1.00  8.02           C  
-ATOM   1673  O   THR A 236      36.590  27.597  45.793  1.00  7.37           O  
-ATOM   1674  CB  THR A 236      37.265  28.728  42.925  1.00  5.25           C  
-ATOM   1675  OG1 THR A 236      36.707  29.407  41.795  1.00  8.21           O  
-ATOM   1676  CG2 THR A 236      38.580  28.104  42.538  1.00  2.88           C  
-ATOM   1677  N   VAL A 237      37.346  25.819  44.586  1.00  6.84           N  
-ATOM   1678  CA  VAL A 237      37.793  25.077  45.766  1.00  7.14           C  
-ATOM   1679  C   VAL A 237      39.310  24.989  45.794  1.00  7.29           C  
-ATOM   1680  O   VAL A 237      39.975  24.661  44.795  1.00  7.33           O  
-ATOM   1681  CB  VAL A 237      37.184  23.639  45.789  1.00  7.85           C  
-ATOM   1682  CG1 VAL A 237      37.542  22.927  47.128  1.00  8.17           C  
-ATOM   1683  CG2 VAL A 237      35.682  23.721  45.640  1.00  9.59           C  
-ATOM   1684  N   PHE A 238      39.836  25.268  47.011  1.00  7.55           N  
-ATOM   1685  CA  PHE A 238      41.248  25.374  47.286  1.00  5.97           C  
-ATOM   1686  C   PHE A 238      41.704  24.385  48.358  1.00  6.46           C  
-ATOM   1687  O   PHE A 238      40.933  24.045  49.248  1.00  8.93           O  
-ATOM   1688  CB  PHE A 238      41.577  26.786  47.779  1.00  7.26           C  
-ATOM   1689  CG  PHE A 238      41.203  27.888  46.803  1.00  7.68           C  
-ATOM   1690  CD1 PHE A 238      39.888  28.361  46.738  1.00  8.41           C  
-ATOM   1691  CD2 PHE A 238      42.187  28.379  45.927  1.00  5.27           C  
-ATOM   1692  CE1 PHE A 238      39.554  29.319  45.788  1.00  6.40           C  
-ATOM   1693  CE2 PHE A 238      41.836  29.339  44.976  1.00  5.48           C  
-ATOM   1694  CZ  PHE A 238      40.528  29.801  44.914  1.00  6.98           C  
-ATOM   1695  N   THR A 239      42.930  23.878  48.300  1.00  5.52           N  
-ATOM   1696  CA  THR A 239      43.525  23.120  49.397  1.00  6.64           C  
-ATOM   1697  C   THR A 239      43.773  24.150  50.507  1.00  7.11           C  
-ATOM   1698  O   THR A 239      44.362  25.190  50.204  1.00  7.28           O  
-ATOM   1699  CB  THR A 239      44.839  22.513  48.957  1.00  5.02           C  
-ATOM   1700  OG1 THR A 239      44.467  21.693  47.867  1.00  7.25           O  
-ATOM   1701  CG2 THR A 239      45.551  21.690  49.984  1.00  8.52           C  
-ATOM   1702  N   ARG A 240      43.355  23.877  51.761  1.00  7.86           N  
-ATOM   1703  CA  ARG A 240      43.561  24.827  52.848  1.00  6.80           C  
-ATOM   1704  C   ARG A 240      44.978  24.704  53.338  1.00  7.30           C  
-ATOM   1705  O   ARG A 240      45.380  23.731  53.990  1.00 10.68           O  
-ATOM   1706  CB  ARG A 240      42.520  24.564  53.993  1.00  8.62           C  
-ATOM   1707  CG  ARG A 240      42.716  25.564  55.145  1.00  8.87           C  
-ATOM   1708  CD  ARG A 240      41.536  25.653  56.067  1.00  8.61           C  
-ATOM   1709  NE  ARG A 240      41.221  24.374  56.687  1.00 11.56           N  
-ATOM   1710  CZ  ARG A 240      41.903  23.795  57.693  1.00  9.55           C  
-ATOM   1711  NH1 ARG A 240      42.978  24.334  58.250  1.00  8.42           N  
-ATOM   1712  NH2 ARG A 240      41.432  22.638  58.178  1.00  8.69           N  
-ATOM   1713  N   VAL A 241      45.804  25.730  53.047  1.00  6.78           N  
-ATOM   1714  CA  VAL A 241      47.224  25.673  53.358  1.00  7.67           C  
-ATOM   1715  C   VAL A 241      47.477  25.524  54.872  1.00  7.96           C  
-ATOM   1716  O   VAL A 241      48.393  24.794  55.248  1.00  7.52           O  
-ATOM   1717  CB  VAL A 241      47.932  26.945  52.800  1.00  8.15           C  
-ATOM   1718  CG1 VAL A 241      49.359  27.081  53.289  1.00  5.92           C  
-ATOM   1719  CG2 VAL A 241      47.919  26.850  51.265  1.00  6.16           C  
-ATOM   1720  N   SER A 242      46.633  26.129  55.732  1.00  6.90           N  
-ATOM   1721  CA  SER A 242      46.862  26.061  57.180  1.00  9.87           C  
-ATOM   1722  C   SER A 242      46.687  24.647  57.739  1.00 11.50           C  
-ATOM   1723  O   SER A 242      47.135  24.390  58.850  1.00 10.55           O  
-ATOM   1724  CB  SER A 242      45.909  27.017  57.926  1.00  6.38           C  
-ATOM   1725  OG  SER A 242      44.558  26.626  57.971  1.00  7.15           O  
-ATOM   1726  N   ALA A 243      46.080  23.711  56.973  1.00 11.57           N  
-ATOM   1727  CA  ALA A 243      45.964  22.335  57.399  1.00 11.12           C  
-ATOM   1728  C   ALA A 243      47.248  21.578  57.116  1.00 11.17           C  
-ATOM   1729  O   ALA A 243      47.410  20.456  57.591  1.00 13.38           O  
-ATOM   1730  CB  ALA A 243      44.809  21.659  56.669  1.00  8.87           C  
-ATOM   1731  N   TYR A 244      48.231  22.171  56.442  1.00  8.71           N  
-ATOM   1732  CA  TYR A 244      49.429  21.466  56.001  1.00  9.59           C  
-ATOM   1733  C   TYR A 244      50.741  22.034  56.457  1.00  9.55           C  
-ATOM   1734  O   TYR A 244      51.796  21.637  55.969  1.00 10.53           O  
-ATOM   1735  CB  TYR A 244      49.437  21.389  54.445  1.00  9.85           C  
-ATOM   1736  CG  TYR A 244      48.266  20.543  53.912  1.00 11.66           C  
-ATOM   1737  CD1 TYR A 244      48.373  19.146  53.905  1.00 11.24           C  
-ATOM   1738  CD2 TYR A 244      47.065  21.160  53.517  1.00  8.56           C  
-ATOM   1739  CE1 TYR A 244      47.283  18.375  53.511  1.00  9.19           C  
-ATOM   1740  CE2 TYR A 244      45.975  20.388  53.133  1.00  6.79           C  
-ATOM   1741  CZ  TYR A 244      46.101  19.005  53.137  1.00  8.12           C  
-ATOM   1742  OH  TYR A 244      45.004  18.234  52.809  1.00 10.18           O  
-ATOM   1743  N   ILE A 245      50.728  22.928  57.441  1.00 11.15           N  
-ATOM   1744  CA  ILE A 245      51.951  23.617  57.834  1.00 11.13           C  
-ATOM   1745  C   ILE A 245      53.013  22.684  58.391  1.00 10.97           C  
-ATOM   1746  O   ILE A 245      54.177  22.828  58.026  1.00 11.37           O  
-ATOM   1747  CB  ILE A 245      51.557  24.735  58.842  1.00  9.25           C  
-ATOM   1748  CG1 ILE A 245      50.595  25.722  58.155  1.00 10.37           C  
-ATOM   1749  CG2 ILE A 245      52.831  25.389  59.412  1.00 10.03           C  
-ATOM   1750  CD1 ILE A 245      51.125  26.399  56.881  1.00 11.86           C  
-ATOM   1751  N   SER A 246      52.652  21.695  59.223  1.00 12.45           N  
-ATOM   1752  CA  SER A 246      53.628  20.737  59.730  1.00 11.85           C  
-ATOM   1753  C   SER A 246      54.232  19.877  58.649  1.00 11.14           C  
-ATOM   1754  O   SER A 246      55.438  19.646  58.683  1.00 13.26           O  
-ATOM   1755  CB  SER A 246      52.986  19.821  60.742  1.00 17.42           C  
-ATOM   1756  OG  SER A 246      52.876  20.618  61.884  1.00 25.47           O  
-ATOM   1757  N   TRP A 247      53.436  19.436  57.656  1.00 11.38           N  
-ATOM   1758  CA  TRP A 247      53.987  18.615  56.574  1.00 10.46           C  
-ATOM   1759  C   TRP A 247      54.981  19.446  55.762  1.00 12.43           C  
-ATOM   1760  O   TRP A 247      56.126  19.023  55.545  1.00 10.24           O  
-ATOM   1761  CB  TRP A 247      52.812  18.090  55.707  1.00 10.33           C  
-ATOM   1762  CG  TRP A 247      53.261  17.313  54.467  1.00 14.12           C  
-ATOM   1763  CD1 TRP A 247      53.714  16.023  54.550  1.00 15.22           C  
-ATOM   1764  CD2 TRP A 247      53.360  17.829  53.179  1.00 14.99           C  
-ATOM   1765  NE1 TRP A 247      54.129  15.729  53.320  1.00 15.11           N  
-ATOM   1766  CE2 TRP A 247      53.946  16.760  52.474  1.00 14.91           C  
-ATOM   1767  CE3 TRP A 247      53.042  19.022  52.516  1.00 15.78           C  
-ATOM   1768  CZ2 TRP A 247      54.234  16.862  51.111  1.00 13.51           C  
-ATOM   1769  CZ3 TRP A 247      53.332  19.115  51.144  1.00 16.23           C  
-ATOM   1770  CH2 TRP A 247      53.922  18.049  50.455  1.00 16.23           C  
-ATOM   1771  N   ILE A 248      54.572  20.698  55.405  1.00 13.24           N  
-ATOM   1772  CA  ILE A 248      55.437  21.603  54.640  1.00 13.46           C  
-ATOM   1773  C   ILE A 248      56.740  21.840  55.356  1.00 13.85           C  
-ATOM   1774  O   ILE A 248      57.794  21.685  54.756  1.00 15.18           O  
-ATOM   1775  CB  ILE A 248      54.751  22.959  54.394  1.00 11.46           C  
-ATOM   1776  CG1 ILE A 248      53.573  22.727  53.471  1.00 10.52           C  
-ATOM   1777  CG2 ILE A 248      55.735  23.964  53.791  1.00 13.13           C  
-ATOM   1778  CD1 ILE A 248      52.650  23.931  53.358  1.00 13.12           C  
-ATOM   1779  N   ASN A 249      56.708  22.167  56.643  1.00 15.66           N  
-ATOM   1780  CA  ASN A 249      57.966  22.361  57.335  1.00 18.53           C  
-ATOM   1781  C   ASN A 249      58.814  21.119  57.539  1.00 16.43           C  
-ATOM   1782  O   ASN A 249      60.031  21.260  57.491  1.00 17.80           O  
-ATOM   1783  CB  ASN A 249      57.724  23.020  58.681  1.00 21.46           C  
-ATOM   1784  CG  ASN A 249      57.244  24.449  58.519  1.00 22.86           C  
-ATOM   1785  OD1 ASN A 249      56.449  24.895  59.330  1.00 29.97           O  
-ATOM   1786  ND2 ASN A 249      57.638  25.244  57.531  1.00 26.91           N  
-ATOM   1787  N   ASN A 250      58.213  19.930  57.696  1.00 16.83           N  
-ATOM   1788  CA  ASN A 250      58.941  18.651  57.807  1.00 16.47           C  
-ATOM   1789  C   ASN A 250      59.611  18.253  56.486  1.00 16.56           C  
-ATOM   1790  O   ASN A 250      60.651  17.609  56.494  1.00 16.74           O  
-ATOM   1791  CB  ASN A 250      57.970  17.526  58.243  1.00 13.56           C  
-ATOM   1792  CG  ASN A 250      57.466  17.622  59.681  1.00 15.43           C  
-ATOM   1793  OD1 ASN A 250      56.398  17.164  60.074  1.00 18.41           O  
-ATOM   1794  ND2 ASN A 250      58.233  18.199  60.557  1.00 14.31           N  
-ATOM   1795  N   VAL A 251      59.059  18.618  55.314  1.00 17.64           N  
-ATOM   1796  CA  VAL A 251      59.696  18.335  54.019  1.00 16.18           C  
-ATOM   1797  C   VAL A 251      60.857  19.283  53.790  1.00 17.67           C  
-ATOM   1798  O   VAL A 251      61.933  18.839  53.397  1.00 18.03           O  
-ATOM   1799  CB  VAL A 251      58.690  18.486  52.860  1.00 15.59           C  
-ATOM   1800  CG1 VAL A 251      59.319  18.240  51.489  1.00 12.59           C  
-ATOM   1801  CG2 VAL A 251      57.588  17.488  53.087  1.00 13.13           C  
-ATOM   1802  N   ILE A 252      60.702  20.573  54.053  1.00 19.04           N  
-ATOM   1803  CA  ILE A 252      61.769  21.530  53.775  1.00 25.61           C  
-ATOM   1804  C   ILE A 252      63.003  21.300  54.650  1.00 29.58           C  
-ATOM   1805  O   ILE A 252      64.137  21.321  54.168  1.00 31.98           O  
-ATOM   1806  CB  ILE A 252      61.160  22.946  53.947  1.00 25.94           C  
-ATOM   1807  CG1 ILE A 252      60.223  23.219  52.786  1.00 26.02           C  
-ATOM   1808  CG2 ILE A 252      62.248  24.007  53.990  1.00 28.18           C  
-ATOM   1809  CD1 ILE A 252      59.431  24.496  53.108  1.00 31.12           C  
-ATOM   1810  N   ALA A 253      62.773  21.069  55.941  1.00 33.64           N  
-ATOM   1811  CA  ALA A 253      63.826  20.729  56.888  1.00 39.90           C  
-ATOM   1812  C   ALA A 253      64.486  19.356  56.643  1.00 44.78           C  
-ATOM   1813  O   ALA A 253      65.631  19.154  57.073  1.00 46.42           O  
-ATOM   1814  CB  ALA A 253      63.273  20.715  58.302  1.00 37.88           C  
-ATOM   1815  N   SER A 254      63.845  18.359  55.999  1.00 48.99           N  
-ATOM   1816  CA  SER A 254      64.540  17.101  55.772  1.00 52.68           C  
-ATOM   1817  C   SER A 254      65.070  16.922  54.351  1.00 55.19           C  
-ATOM   1818  O   SER A 254      65.847  15.987  54.133  1.00 56.64           O  
-ATOM   1819  CB  SER A 254      63.621  15.919  56.142  1.00 53.68           C  
-ATOM   1820  OG  SER A 254      62.413  15.811  55.394  1.00 55.52           O  
-ATOM   1821  N   ASN A 255      64.721  17.786  53.381  1.00 57.18           N  
-ATOM   1822  CA  ASN A 255      65.204  17.656  52.004  1.00 59.60           C  
-ATOM   1823  C   ASN A 255      66.166  18.765  51.639  1.00 60.68           C  
-ATOM   1824  O   ASN A 255      65.878  19.922  51.956  1.00 63.35           O  
-ATOM   1825  CB  ASN A 255      64.083  17.715  50.981  1.00 60.00           C  
-ATOM   1826  CG  ASN A 255      63.104  16.556  51.026  1.00 60.85           C  
-ATOM   1827  OD1 ASN A 255      63.035  15.771  50.087  1.00 61.78           O  
-ATOM   1828  ND2 ASN A 255      62.301  16.382  52.075  1.00 60.59           N  
-ATOM   1829  OXT ASN A 255      67.187  18.458  51.029  1.00 62.36           O  
-TER    1830      ASN A 255                                                      
-HETATM 1831 CA    CA A 280      57.314  37.378  30.072  1.00 20.84          CA  
-HETATM 1832  S   SO4 A 290      43.528  21.842  61.312  1.00 42.65           S  
-HETATM 1833  O1  SO4 A 290      43.862  22.938  60.486  1.00 41.10           O  
-HETATM 1834  O2  SO4 A 290      44.637  20.950  61.397  1.00 43.95           O  
-HETATM 1835  O3  SO4 A 290      42.382  21.153  60.795  1.00 41.19           O  
-HETATM 1836  O4  SO4 A 290      43.258  22.304  62.628  1.00 44.27           O  
-HETATM 1837  C1  0QH A 256      41.149  23.354  37.644  1.00 31.55           C  
-HETATM 1838  C2  0QH A 256      41.347  24.616  38.562  1.00 29.79           C  
-HETATM 1839  O   0QH A 256      40.738  23.466  36.483  1.00 31.48           O  
-HETATM 1840  F1  0QH A 256      41.871  24.392  39.754  1.00 30.45           F  
-HETATM 1841  F2  0QH A 256      42.130  25.537  38.058  1.00 27.87           F  
-HETATM 1842  F3  0QH A 256      40.210  25.231  38.787  1.00 30.74           F  
-HETATM 1843  N   0QH A 256      41.428  22.136  38.149  1.00 32.72           N  
-HETATM 1844  CA  0QH A 256      40.800  20.919  37.702  1.00 35.06           C  
-HETATM 1845  C   0QH A 256      39.307  21.048  37.435  1.00 37.47           C  
-HETATM 1846  O1  0QH A 256      38.514  21.565  38.211  1.00 36.15           O  
-HETATM 1847  CB  0QH A 256      41.100  19.869  38.747  1.00 34.44           C  
-HETATM 1848  CG  0QH A 256      41.280  18.443  38.288  1.00 36.76           C  
-HETATM 1849  CD1 0QH A 256      42.225  18.333  37.087  1.00 36.80           C  
-HETATM 1850  CD2 0QH A 256      41.811  17.676  39.479  1.00 38.25           C  
-HETATM 1851  N1  0QH A 256      37.773  20.686  35.406  1.00 44.05           N  
-HETATM 1852  N2  0QH A 256      39.121  20.568  36.190  1.00 41.52           N  
-HETATM 1853  C3  0QH A 256      37.712  22.117  34.940  1.00 46.64           C  
-HETATM 1854  C11 0QH A 256      36.522  22.554  34.080  1.00 51.49           C  
-HETATM 1855  C21 0QH A 256      35.753  23.641  34.490  1.00 50.39           C  
-HETATM 1856  C31 0QH A 256      34.724  24.077  33.677  1.00 52.00           C  
-HETATM 1857  C4  0QH A 256      34.426  23.461  32.459  1.00 53.48           C  
-HETATM 1858  C5  0QH A 256      35.179  22.373  32.039  1.00 54.08           C  
-HETATM 1859  C6  0QH A 256      36.225  21.923  32.850  1.00 54.40           C  
-HETATM 1860  C1M 0QH A 256      38.160  19.713  34.316  1.00 46.35           C  
-HETATM 1861  CA2 0QH A 256      36.531  20.238  36.106  1.00 42.79           C  
-HETATM 1862  CA1 0QH A 256      36.544  18.892  36.812  1.00 41.97           C  
-HETATM 1863  O2  0QH A 256      36.668  17.792  36.251  1.00 40.89           O  
-HETATM 1864  C12 0QH A 256      36.195  18.351  39.070  1.00 41.34           C  
-HETATM 1865  N11 0QH A 256      36.432  19.241  38.103  1.00 41.27           N  
-HETATM 1866  C22 0QH A 256      36.820  17.094  39.138  1.00 41.18           C  
-HETATM 1867  C32 0QH A 256      36.529  16.229  40.207  1.00 42.70           C  
-HETATM 1868  C41 0QH A 256      35.613  16.613  41.216  1.00 40.91           C  
-HETATM 1869  C51 0QH A 256      35.007  17.872  41.125  1.00 42.28           C  
-HETATM 1870  C61 0QH A 256      35.290  18.723  40.059  1.00 41.35           C  
-HETATM 1871  C1' 0QH A 256      35.273  15.697  42.414  1.00 38.52           C  
-HETATM 1872  C2' 0QH A 256      35.742  14.242  42.251  1.00 36.76           C  
-HETATM 1873  C3' 0QH A 256      33.777  15.691  42.501  1.00 38.27           C  
-HETATM 1874  O   HOH A 301      32.882  26.020  39.606  1.00 17.65           O  
-HETATM 1875  O   HOH A 302      32.442  29.522  40.356  1.00 21.49           O  
-HETATM 1876  O   HOH A 303      31.364  32.109  40.271  1.00 14.39           O  
-HETATM 1877  O   HOH A 304      34.013  31.083  41.939  1.00 14.29           O  
-HETATM 1878  O   HOH A 305      35.685  27.451  53.086  1.00 14.08           O  
-HETATM 1879  O   HOH A 306      35.231  24.442  53.127  1.00 28.89           O  
-HETATM 1880  O   HOH A 307      35.490  31.094  55.192  1.00 19.23           O  
-HETATM 1881  O   HOH A 308      39.761  29.106  55.841  1.00 14.63           O  
-HETATM 1882  O   HOH A 309      53.144  39.621  37.336  1.00 26.14           O  
-HETATM 1883  O   HOH A 310      57.464  42.102  35.337  1.00 30.84           O  
-HETATM 1884  O   HOH A 311      56.295  39.174  39.811  1.00 21.08           O  
-HETATM 1885  O   HOH A 312      45.452  30.812  42.008  1.00  6.92           O  
-HETATM 1886  O   HOH A 313      47.449  30.520  39.380  1.00  6.92           O  
-HETATM 1887  O   HOH A 314      48.283  30.372  36.744  1.00 10.12           O  
-HETATM 1888  O   HOH A 315      50.127  28.060  45.624  1.00  9.45           O  
-HETATM 1889  O   HOH A 316      42.549  29.375  56.136  1.00 12.87           O  
-HETATM 1890  O   HOH A 317      45.102  28.273  54.960  1.00  9.55           O  
-HETATM 1891  O   HOH A 318      41.167  18.810  46.507  1.00 11.18           O  
-HETATM 1892  O   HOH A 319      42.862  19.540  48.578  1.00  9.49           O  
-HETATM 1893  O   HOH A 320      42.969  19.206  51.337  1.00 13.03           O  
-HETATM 1894  O   HOH A 321      57.440  35.699  40.935  1.00 14.74           O  
-HETATM 1895  O   HOH A 322      55.936  34.579  38.033  1.00 23.30           O  
-HETATM 1896  O   HOH A 323      52.785  39.989  40.333  1.00 25.89           O  
-HETATM 1897  O   HOH A 324      33.689  36.733  43.984  1.00 22.09           O  
-HETATM 1898  O   HOH A 325      32.752  34.434  42.638  1.00 19.00           O  
-HETATM 1899  O   HOH A 326      61.296  18.059  35.669  1.00 30.78           O  
-HETATM 1900  O   HOH A 327      60.418  37.615  50.653  1.00 26.97           O  
-HETATM 1901  O   HOH A 328      52.092  36.358  50.688  1.00 17.16           O  
-HETATM 1902  O   HOH A 329      32.883  31.561  31.264  1.00 23.33           O  
-HETATM 1903  O   HOH A 330      43.307  12.818  47.113  1.00 10.74           O  
-HETATM 1904  O   HOH A 331      36.720  37.088  32.045  1.00 23.95           O  
-HETATM 1905  O   HOH A 332      43.583  34.271  34.093  1.00  8.71           O  
-HETATM 1906  O   HOH A 333      64.151  38.662  38.603  1.00 17.67           O  
-HETATM 1907  O   HOH A 334      52.858  37.863  46.914  1.00 23.65           O  
-HETATM 1908  O   HOH A 335      50.321  18.976  58.535  1.00 26.76           O  
-HETATM 1909  O   HOH A 336      40.093  37.345  33.628  1.00 25.03           O  
-HETATM 1910  O   HOH A 337      32.158  36.439  33.842  1.00 28.27           O  
-HETATM 1911  O   HOH A 338      54.965  37.964  49.272  1.00 44.50           O  
-HETATM 1912  O   HOH A 339      48.863  37.454  57.934  1.00 30.43           O  
-HETATM 1913  O   HOH A 340      41.448  24.662  62.587  1.00 24.01           O  
-HETATM 1914  O   HOH A 341      61.601  23.704  58.048  1.00 33.41           O  
-HETATM 1915  O   HOH A 342      66.904  32.764  34.214  1.00 30.56           O  
-HETATM 1916  O   HOH A 343      49.238  33.132  26.847  1.00 35.15           O  
-HETATM 1917  O   HOH A 344      47.105  44.440  40.996  1.00 20.82           O  
-HETATM 1918  O   HOH A 345      47.069  22.275  61.044  1.00 31.32           O  
-HETATM 1919  O   HOH A 346      34.646  30.080  59.205  1.00 27.77           O  
-HETATM 1920  O   HOH A 347      43.223  10.806  49.056  1.00 30.40           O  
-HETATM 1921  O   HOH A 348      67.980  25.297  36.489  1.00 28.90           O  
-HETATM 1922  O   HOH A 349      68.279  36.872  47.286  1.00 33.84           O  
-HETATM 1923  O   HOH A 350      52.212  27.533  62.384  1.00 28.11           O  
-HETATM 1924  O   HOH A 351      57.507  31.607  53.559  1.00 40.44           O  
-HETATM 1925  O   HOH A 352      50.195  37.258  48.866  1.00 31.37           O  
-HETATM 1926  O   HOH A 353      64.855  31.038  51.212  1.00 39.73           O  
-HETATM 1927  O   HOH A 354      48.078  43.679  46.695  1.00 44.90           O  
-HETATM 1928  O   HOH A 355      58.415  35.335  29.066  1.00 27.17           O  
-HETATM 1929  O   HOH A 356      45.710  38.988  29.308  1.00 38.47           O  
-HETATM 1930  O   HOH A 357      51.043  14.003  41.579  1.00 21.25           O  
-HETATM 1931  O   HOH A 358      67.908  23.479  45.499  1.00 32.89           O  
-HETATM 1932  O   HOH A 359      61.233  13.914  42.154  1.00 33.27           O  
-HETATM 1933  O   HOH A 360      36.842  25.273  30.915  1.00 13.93           O  
-HETATM 1934  O   HOH A 361      56.471  41.206  37.704  1.00 27.85           O  
-HETATM 1935  O   HOH A 362      44.959  29.044  25.226  1.00 33.57           O  
-HETATM 1936  O   HOH A 363      38.998  33.020  26.805  1.00 20.64           O  
-HETATM 1937  O   HOH A 364      64.429  26.904  30.756  1.00 27.82           O  
-HETATM 1938  O   HOH A 365      49.235  16.475  56.392  1.00 29.93           O  
-HETATM 1939  O   HOH A 366      44.125  17.192  55.905  1.00 39.61           O  
-HETATM 1940  O   HOH A 367      49.797  21.805  60.380  1.00 27.84           O  
-HETATM 1941  O   HOH A 368      50.024  19.785  34.563  1.00 30.97           O  
-HETATM 1942  O   HOH A 369      46.429  32.844  24.842  1.00 41.62           O  
-HETATM 1943  O   HOH A 370      47.931  33.256  60.045  1.00 28.11           O  
-HETATM 1944  O   HOH A 371      41.806  45.255  34.043  1.00 30.30           O  
-HETATM 1945  O   HOH A 372      63.874  21.873  33.271  1.00 41.07           O  
-HETATM 1946  O   HOH A 373      56.782  32.378  30.107  1.00 26.11           O  
-HETATM 1947  O   HOH A 374      47.243  34.732  57.808  1.00 23.62           O  
-HETATM 1948  O   HOH A 375      37.066  28.697  55.048  1.00 34.12           O  
-HETATM 1949  O   HOH A 376      37.249  25.085  56.044  1.00 40.37           O  
-HETATM 1950  O   HOH A 377      28.275  17.000  45.695  1.00 37.97           O  
-HETATM 1951  O   HOH A 378      42.408  40.137  59.903  1.00 44.03           O  
-HETATM 1952  O   HOH A 379      49.251  46.251  34.415  1.00 43.84           O  
-HETATM 1953  O   HOH A 380      54.093  37.592  39.323  1.00 34.41           O  
-HETATM 1954  O   HOH A 381      48.187  22.582  30.415  1.00 39.01           O  
-HETATM 1955  O   HOH A 382      51.483  31.033  26.492  1.00 51.83           O  
-HETATM 1956  O   HOH A 383      56.607  12.499  46.037  1.00 23.19           O  
-HETATM 1957  O   HOH A 384      55.626  11.776  48.780  1.00 40.69           O  
-HETATM 1958  O   HOH A 385      52.534  35.789  59.363  1.00 38.05           O  
-HETATM 1959  O   HOH A 386      35.031  27.253  57.241  1.00 29.30           O  
-HETATM 1960  O   HOH A 387      32.125  31.879  59.654  1.00 34.45           O  
-HETATM 1961  O   HOH A 388      28.198  29.575  58.752  1.00 42.72           O  
-HETATM 1962  O   HOH A 389      45.086  35.683  25.607  1.00 31.08           O  
-HETATM 1963  O   HOH A 390      32.348  34.623  31.387  1.00 31.83           O  
-HETATM 1964  O   HOH A 391      38.765  35.716  59.975  1.00 31.57           O  
-HETATM 1965  O   HOH A 392      44.103  41.461  30.834  1.00 49.81           O  
-HETATM 1966  O   HOH A 393      41.972  15.911  53.072  1.00 32.93           O  
-HETATM 1967  O   HOH A 394      28.002  18.208  53.733  1.00 35.56           O  
-HETATM 1968  O   HOH A 395      44.375  23.297  35.373  1.00 22.03           O  
-HETATM 1969  O   HOH A 396      30.702  31.211  29.539  1.00 51.18           O  
-HETATM 1970  O   HOH A 397      30.494  28.541  32.709  1.00 49.36           O  
-HETATM 1971  O   HOH A 398      56.412  21.054  62.131  1.00 43.25           O  
-HETATM 1972  O   HOH A 399      44.542  44.447  44.699  1.00 48.81           O  
-HETATM 1973  O   HOH A 400      31.898  26.937  58.945  1.00 37.09           O  
-HETATM 1974  O   HOH A 401      37.218  41.186  40.473  1.00 38.21           O  
-HETATM 1975  O   HOH A 402      26.032  29.330  36.708  1.00 41.30           O  
-HETATM 1976  O   HOH A 403      26.133  32.573  45.021  1.00 40.73           O  
-HETATM 1977  O   HOH A 404      55.838  42.729  28.694  1.00 41.47           O  
-HETATM 1978  O   HOH A 405      42.852  35.753  27.210  1.00 41.44           O  
-HETATM 1979  O   HOH A 406      52.225  44.186  55.156  1.00 45.19           O  
-HETATM 1980  O   HOH A 407      41.877  18.854  58.058  1.00 45.51           O  
-HETATM 1981  O   HOH A 408      26.732  21.589  55.886  1.00 47.70           O  
-HETATM 1982  O   HOH A 409      32.690  16.791  53.773  1.00 39.34           O  
-HETATM 1983  O   HOH A 410      58.623  17.123  24.197  1.00 44.44           O  
-HETATM 1984  O   HOH A 411      65.260  20.092  24.330  1.00 37.78           O  
-HETATM 1985  O   HOH A 412      45.751   7.536  49.944  1.00 45.48           O  
-HETATM 1986  O   HOH A 413      57.867  17.562  29.038  1.00 39.83           O  
-HETATM 1987  O   HOH A 414      28.283  22.782  30.998  1.00 43.50           O  
-HETATM 1988  O   HOH A 415      67.326  26.052  33.737  1.00 65.89           O  
-HETATM 1989  O   HOH A 416      58.019  14.849  36.117  1.00 20.44           O  
-HETATM 1990  O   HOH A 417      51.753  33.322  44.908  1.00 39.55           O  
-HETATM 1991  O   HOH A 418      56.671  43.846  45.568  1.00 48.93           O  
-HETATM 1992  O   HOH A 419      39.120  23.034  61.598  1.00 42.00           O  
-HETATM 1993  O   HOH A 420      41.306  15.026  56.005  1.00 47.08           O  
-HETATM 1994  O   HOH A 421      26.653  15.602  48.462  1.00 44.38           O  
-HETATM 1995  O   HOH A 422      25.367  17.571  33.210  1.00 40.94           O  
-HETATM 1996  O   HOH A 423      42.962  20.877  34.581  1.00 39.92           O  
-HETATM 1997  O   HOH A 424      63.325  17.648  23.374  1.00 51.93           O  
-HETATM 1998  O   HOH A 425      51.125  42.005  52.466  1.00 33.24           O  
-HETATM 1999  O   HOH A 426      44.781   6.738  38.029  1.00 35.75           O  
-HETATM 2000  O   HOH A 427      40.801  45.034  42.972  1.00 37.80           O  
-HETATM 2001  O   HOH A 428      41.185  41.488  32.038  1.00 41.78           O  
-HETATM 2002  O   HOH A 429      50.800  44.806  30.573  1.00 46.30           O  
-HETATM 2003  O   HOH A 430      57.885  37.456  52.108  1.00 38.46           O  
-HETATM 2004  O   HOH A 431      22.145  21.543  53.132  1.00 41.38           O  
-HETATM 2005  O   HOH A 432      41.352  34.096  61.758  1.00 45.89           O  
-HETATM 2006  O   HOH A 433      48.397   9.654  43.158  1.00 40.50           O  
-HETATM 2007  O   HOH A 434      42.265  45.255  31.328  1.00 40.72           O  
-CONECT  231  352                                                                
-CONECT  352  231                                                                
-CONECT  457 1831                                                                
-CONECT  458 1831                                                                
-CONECT  472 1831                                                                
-CONECT  496 1831                                                                
-CONECT  516 1831                                                                
-CONECT  537 1831                                                                
-CONECT  980 1466                                                                
-CONECT 1223 1341                                                                
-CONECT 1341 1223                                                                
-CONECT 1400 1620                                                                
-CONECT 1466  980                                                                
-CONECT 1620 1400                                                                
-CONECT 1831  457  458  472  496                                                 
-CONECT 1831  516  537 1928                                                      
-CONECT 1832 1833 1834 1835 1836                                                 
-CONECT 1833 1832                                                                
-CONECT 1834 1832                                                                
-CONECT 1835 1832                                                                
-CONECT 1836 1832                                                                
-CONECT 1837 1838 1839 1843                                                      
-CONECT 1838 1837 1840 1841 1842                                                 
-CONECT 1839 1837                                                                
-CONECT 1840 1838                                                                
-CONECT 1841 1838                                                                
-CONECT 1842 1838                                                                
-CONECT 1843 1837 1844                                                           
-CONECT 1844 1843 1845 1847                                                      
-CONECT 1845 1844 1846 1852                                                      
-CONECT 1846 1845                                                                
-CONECT 1847 1844 1848                                                           
-CONECT 1848 1847 1849 1850                                                      
-CONECT 1849 1848                                                                
-CONECT 1850 1848                                                                
-CONECT 1851 1852 1853 1860 1861                                                 
-CONECT 1852 1845 1851                                                           
-CONECT 1853 1851 1854                                                           
-CONECT 1854 1853 1855 1859                                                      
-CONECT 1855 1854 1856                                                           
-CONECT 1856 1855 1857                                                           
-CONECT 1857 1856 1858                                                           
-CONECT 1858 1857 1859                                                           
-CONECT 1859 1854 1858                                                           
-CONECT 1860 1851                                                                
-CONECT 1861 1851 1862                                                           
-CONECT 1862 1861 1863 1865                                                      
-CONECT 1863 1862                                                                
-CONECT 1864 1865 1866 1870                                                      
-CONECT 1865 1862 1864                                                           
-CONECT 1866 1864 1867                                                           
-CONECT 1867 1866 1868                                                           
-CONECT 1868 1867 1869 1871                                                      
-CONECT 1869 1868 1870                                                           
-CONECT 1870 1864 1869                                                           
-CONECT 1871 1868 1872 1873                                                      
-CONECT 1872 1871                                                                
-CONECT 1873 1871                                                                
-CONECT 1928 1831                                                                
-MASTER      392    0    3    2   17    0   10    6 1999    1   59   19          
-END                                                                             
diff --git a/plip/test/pdb/1eve.pdb b/plip/test/pdb/1eve.pdb
deleted file mode 100644
index aef08ad..0000000
--- a/plip/test/pdb/1eve.pdb
+++ /dev/null
@@ -1,5376 +0,0 @@
-HEADER    SERINE HYDROLASE                        04-MAR-98   1EVE              
-TITLE     THREE DIMENSIONAL STRUCTURE OF THE ANTI-ALZHEIMER DRUG, E2020         
-TITLE    2 (ARICEPT), COMPLEXED WITH ITS TARGET ACETYLCHOLINESTERASE            
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 EC: 3.1.1.7                                                          
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;                            
-SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
-SOURCE   4 ORGANISM_TAXID: 7787;                                                
-SOURCE   5 VARIANT: G2 FORM;                                                    
-SOURCE   6 ORGAN: ELECTRIC ORGAN;                                               
-SOURCE   7 TISSUE: ELECTROPLAQUE                                                
-KEYWDS    ALZHEIMER'S DISEASE, DRUG, SERINE HYDROLASE, ALPHA/BETA HYDROLASE,    
-KEYWDS   2 NEUROTRANSMITTER CLEAVAGE, CATALYTIC TRIAD, GLYCOSYLATED PROTEIN     
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    G.KRYGER,I.SILMAN,J.L.SUSSMAN                                         
-REVDAT   4   13-JUL-11 1EVE    1       VERSN                                    
-REVDAT   3   24-FEB-09 1EVE    1       VERSN                                    
-REVDAT   2   22-MAR-99 1EVE    1       JRNL                                     
-REVDAT   1   20-JAN-99 1EVE    0                                                
-JRNL        AUTH   G.KRYGER,I.SILMAN,J.L.SUSSMAN                                
-JRNL        TITL   STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH E2020       
-JRNL        TITL 2 (ARICEPT): IMPLICATIONS FOR THE DESIGN OF NEW ANTI-ALZHEIMER 
-JRNL        TITL 3 DRUGS.                                                       
-JRNL        REF    STRUCTURE FOLD.DES.           V.   7   297 1999              
-JRNL        REFN                   ISSN 0969-2126                               
-JRNL        PMID   10368299                                                     
-JRNL        DOI    10.1016/S0969-2126(99)80040-9                                
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   Y.KAWAKAMI,A.INOUE,T.KAWAI,M.WAKITA,H.SUGIMOTO,A.J.HOPFINGER 
-REMARK   1  TITL   THE RATIONALE FOR E2020 AS A POTENT ACETYLCHOLINESTERASE     
-REMARK   1  TITL 2 INHIBITOR                                                    
-REMARK   1  REF    BIOORG.MED.CHEM.              V.   4  1429 1996              
-REMARK   1  REFN                   ISSN 0968-0896                               
-REMARK   1 REFERENCE 2                                                          
-REMARK   1  AUTH   J.L.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN,L.TOKER,     
-REMARK   1  AUTH 2 I.SILMAN                                                     
-REMARK   1  TITL   ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM TORPEDO        
-REMARK   1  TITL 2 CALIFORNICA: A PROTOTYPIC ACETYLCHOLINE-BINDING PROTEIN      
-REMARK   1  REF    SCIENCE                       V. 253   872 1991              
-REMARK   1  REFN                   ISSN 0036-8075                               
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : X-PLOR 3.851                                         
-REMARK   3   AUTHORS     : BRUNGER                                              
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.3                           
-REMARK   3   NUMBER OF REFLECTIONS             : 34240                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.188                           
-REMARK   3   FREE R VALUE                     : 0.228                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.800                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1976                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.70                        
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5288                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
-REMARK   3   BIN FREE R VALUE                    : 0.3670                       
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 295                          
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 4254                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 98                                      
-REMARK   3   SOLVENT ATOMS            : 396                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 39.10                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.30                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 1.06000                                              
-REMARK   3    B22 (A**2) : 1.06000                                              
-REMARK   3    B33 (A**2) : -2.13000                                             
-REMARK   3    B12 (A**2) : -0.48000                                             
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.30                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 30.00                           
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.005                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.97                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.100 ; 1.500                
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.590 ; 2.000                
-REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.130 ; 2.000                
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.880 ; 2.500                
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
-REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
-REMARK   3  PARAMETER FILE  3  : CBH3.PARAM                                     
-REMARK   3  PARAMETER FILE  4  : LEARN.E2020                                    
-REMARK   3  PARAMETER FILE  5  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
-REMARK   3  TOPOLOGY FILE  2   : TOPH11.WAT                                     
-REMARK   3  TOPOLOGY FILE  3   : E2020.TOP                                      
-REMARK   3  TOPOLOGY FILE  4   : CBH3-P.CHO                                     
-REMARK   3  TOPOLOGY FILE  5   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
-REMARK   4                                                                      
-REMARK   4 1EVE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : MAY-97                             
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 5.8                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : N                                  
-REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
-REMARK 200  MONOCHROMATOR                  : NI FILTER                          
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
-REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34266                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : 0.05000                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : 0.25200                            
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
-REMARK 200 STARTING MODEL: PDB ENTRY 2ACE                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 68.00                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.8                                   
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -Y,X-Y,Z+1/3                                            
-REMARK 290       3555   -X+Y,-X,Z+2/3                                           
-REMARK 290       4555   Y,X,-Z                                                  
-REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
-REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.63200            
-REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       91.26400            
-REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       91.26400            
-REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       45.63200            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 300 REMARK: TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IS A G2 DIMER IN    
-REMARK 300 SOLUTION (SEE SUSSMAN 1988). THE ASYMMETRIC UNIT CONTAINS            
-REMARK 300 A MONOMER, WITH THE CRYSTALLOGRAPHIC TWO-FOLD AXIS RELATING          
-REMARK 300 THE TWO MONOMERS IN A DIMER. THIS STRUCTURE IS MORE                  
-REMARK 300 COMPLETE THAN THE STARTING MODEL OF THE NATIVE STRUCTURE             
-REMARK 300 (PDB ID 2ACE). RESIDUES THAT ARE NOT SEEN IN THE CRYSTAL             
-REMARK 300 STRUCTURE DUE TO DISORDER INCLUDE THE N-TERMINAL RESIDUE             
-REMARK 300 ASP 1 AND THE C-TERMINAL RESIDUES AFTER THR 535. THR 535             
-REMARK 300 IS THE LAST RESIDUE OBSERVED AT THE C-TERMINUS. THE LIGAND           
-REMARK 300 SEEN IN THE STRUCTURE, E2020 (DONEPEZIL, ARICEPT), IS A              
-REMARK 300 POTENT REVERSIBLE ACHE INHIBITOR WHICH IS AN FDA APPROVED            
-REMARK 300 DRUG FOR THE SYMPTOMATIC TREATMENT OF ALZHEIMER'S DISEASE            
-REMARK 300 (SEE KAWAKAMI 1996). THE CHIRAL INHIBITOR WAS SOAKED AS A            
-REMARK 300 RACEMATE BUT ONLY THE R FORM SEEMS TO BIND TO THE ENZYME             
-REMARK 300 ACCORDING TO THE X-RAY DIFFRACTION EXPERIMENT.                       
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 375                                                                      
-REMARK 375 SPECIAL POSITION                                                     
-REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
-REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
-REMARK 375 POSITIONS.                                                           
-REMARK 375                                                                      
-REMARK 375 ATOM RES CSSEQI                                                      
-REMARK 375      HOH A1381  LIES ON A SPECIAL POSITION.                          
-REMARK 375      HOH A1382  LIES ON A SPECIAL POSITION.                          
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     ASP A     1                                                      
-REMARK 465     ALA A   536                                                      
-REMARK 465     CYS A   537                                                      
-REMARK 465     ASP A   538                                                      
-REMARK 465     GLY A   539                                                      
-REMARK 465     GLU A   540                                                      
-REMARK 465     LEU A   541                                                      
-REMARK 465     SER A   542                                                      
-REMARK 465     SER A   543                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     ASP A   2    CG   OD1  OD2                                       
-REMARK 470     HIS A   3    CG   ND1  CD2  CE1  NE2                             
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    HIS A   3      -94.75   -131.86                                   
-REMARK 500    SER A  24      -24.45     74.01                                   
-REMARK 500    SER A  25     -165.83   -101.45                                   
-REMARK 500    PRO A  39       40.38    -74.51                                   
-REMARK 500    PHE A  45      -13.15     80.73                                   
-REMARK 500    ALA A  60       52.02   -116.78                                   
-REMARK 500    SER A 108       81.90   -161.75                                   
-REMARK 500    ALA A 164       72.79   -156.57                                   
-REMARK 500    SER A 200     -112.92     55.47                                   
-REMARK 500    SER A 291      -71.17    -57.73                                   
-REMARK 500    THR A 317     -162.98   -163.72                                   
-REMARK 500    ASP A 326       77.34   -119.92                                   
-REMARK 500    HIS A 362       20.32    -79.31                                   
-REMARK 500    ASP A 380       66.96   -159.21                                   
-REMARK 500    VAL A 400      -66.25   -126.27                                   
-REMARK 500    LYS A 498      -63.59    -90.42                                   
-REMARK 500    ARG A 515       70.10     49.62                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A1035        DISTANCE =  5.22 ANGSTROMS                       
-REMARK 525    HOH A1098        DISTANCE =  5.14 ANGSTROMS                       
-REMARK 650                                                                      
-REMARK 650 HELIX                                                                
-REMARK 650 THE ENZYME IS A GPI-ANCHORED DIMER, THE TWO MONOMERS IN THE          
-REMARK 650 DIMER ARE RELATED BY CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AND          
-REMARK 650 GENERATE A FOUR HELIX BUNDLE A365-A375 AND A518-A535.                
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: CAT                                                 
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.                                   
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: IHB                                                 
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: INHIBITOR BINDING SITE.                            
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3001                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3002                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3003                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3004                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3005                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E20 A 2001                
-DBREF  1EVE A    1   543  UNP    P04058   ACES_TORCA      22    564             
-SEQRES   1 A  543  ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY          
-SEQRES   2 A  543  LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS          
-SEQRES   3 A  543  ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO          
-SEQRES   4 A  543  VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS          
-SEQRES   5 A  543  PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN          
-SEQRES   6 A  543  ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE          
-SEQRES   7 A  543  SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER          
-SEQRES   8 A  543  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO          
-SEQRES   9 A  543  ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY          
-SEQRES  10 A  543  GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR          
-SEQRES  11 A  543  ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU          
-SEQRES  12 A  543  VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU          
-SEQRES  13 A  543  ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY          
-SEQRES  14 A  543  LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP          
-SEQRES  15 A  543  ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR          
-SEQRES  16 A  543  ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET          
-SEQRES  17 A  543  HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG          
-SEQRES  18 A  543  ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA          
-SEQRES  19 A  543  SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU          
-SEQRES  20 A  543  LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU          
-SEQRES  21 A  543  GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU          
-SEQRES  22 A  543  LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER          
-SEQRES  23 A  543  ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU          
-SEQRES  24 A  543  PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY          
-SEQRES  25 A  543  ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS          
-SEQRES  26 A  543  ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY          
-SEQRES  27 A  543  PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP          
-SEQRES  28 A  543  PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN          
-SEQRES  29 A  543  ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP          
-SEQRES  30 A  543  TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY          
-SEQRES  31 A  543  LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO          
-SEQRES  32 A  543  LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN          
-SEQRES  33 A  543  GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN          
-SEQRES  34 A  543  LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR          
-SEQRES  35 A  543  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU          
-SEQRES  36 A  543  LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG          
-SEQRES  37 A  543  ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN          
-SEQRES  38 A  543  PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU          
-SEQRES  39 A  543  PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR          
-SEQRES  40 A  543  GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET          
-SEQRES  41 A  543  CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN          
-SEQRES  42 A  543  ALA THR ALA CYS ASP GLY GLU LEU SER SER                      
-MODRES 1EVE ASN A   59  ASN  GLYCOSYLATION SITE                                 
-MODRES 1EVE ASN A  416  ASN  GLYCOSYLATION SITE                                 
-MODRES 1EVE ASN A  533  ASN  GLYCOSYLATION SITE                                 
-MODRES 1EVE ASN A  457  ASN  GLYCOSYLATION SITE                                 
-HET    NAG  A3001      14                                                       
-HET    NAG  A3002      14                                                       
-HET    NAG  A3003      14                                                       
-HET    NAG  A3004      14                                                       
-HET    NAG  A3005      14                                                       
-HET    E20  A2001      28                                                       
-HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
-HETNAM     E20 1-BENZYL-4-[(5,6-DIMETHOXY-1-INDANON-2-YL)                       
-HETNAM   2 E20  METHYL]PIPERIDINE                                               
-HETSYN     E20 E2020                                                            
-FORMUL   2  NAG    5(C8 H15 N O6)                                               
-FORMUL   6  E20    C24 H29 N O3                                                 
-FORMUL   7  HOH   *396(H2 O)                                                    
-HELIX    1   1 GLY A   41  MET A   43  5                                   3    
-HELIX    2   2 SER A   79  TRP A   84  1                                   6    
-HELIX    3   3 ASP A  128  TYR A  130  5                                   3    
-HELIX    4   4 LYS A  133  GLU A  139  1                                   7    
-HELIX    5   5 GLY A  151  PHE A  155  1                                   5    
-HELIX    6   6 VAL A  168  PHE A  187  1                                  20    
-HELIX    7   7 ALA A  201  LEU A  211  1                                  11    
-HELIX    8   8 PRO A  213  LEU A  218  1                                   6    
-HELIX    9   9 VAL A  238  LEU A  252  1                                  15    
-HELIX   10  10 ASP A  259  GLU A  268  1                                  10    
-HELIX   11  11 PRO A  271  VAL A  281  1                                  11    
-HELIX   12  12 LEU A  305  SER A  311  1                                   7    
-HELIX   13  13 SER A  329  GLY A  335  1                                   7    
-HELIX   14  14 ARG A  349  SER A  359  1                                  11    
-HELIX   15  15 ASP A  365  GLN A  374  1                                  10    
-HELIX   16  16 GLY A  384  ASN A  399  1                                  16    
-HELIX   17  17 ILE A  401  PHE A  414  1                                  14    
-HELIX   18  18 GLU A  434  MET A  436  5                                   3    
-HELIX   19  19 ILE A  444  VAL A  447  1                                   4    
-HELIX   20  20 LEU A  450  LEU A  452  5                                   3    
-HELIX   21  21 LYS A  454  LEU A  456  5                                   3    
-HELIX   22  22 ALA A  460  THR A  479  1                                  20    
-HELIX   23  23 VAL A  518  ASN A  525  1                                   8    
-HELIX   24  24 PHE A  527  ASN A  533  1                                   7    
-SHEET    1   A 3 LEU A   6  THR A  10  0                                        
-SHEET    2   A 3 GLY A  13  MET A  16 -1  N  VAL A  15   O  VAL A   8           
-SHEET    3   A 3 VAL A  57  ALA A  60  1  N  TRP A  58   O  LYS A  14           
-SHEET    1   B11 MET A  16  PRO A  21  0                                        
-SHEET    2   B11 HIS A  26  PRO A  34 -1  O  ALA A  29   N  THR A  18           
-SHEET    3   B11 TYR A  96  PRO A 102 -1  N  ILE A  99   O  PHE A  30           
-SHEET    4   B11 VAL A 142  SER A 147 -1  N  LEU A 143   O  TRP A 100           
-SHEET    5   B11 THR A 109  TYR A 116  1  N  MET A 112   O  VAL A 142           
-SHEET    6   B11 THR A 193  GLU A 199  1  O  THR A 195   N  VAL A 113           
-SHEET    7   B11 ARG A 220  SER A 226  1  N  ILE A 223   O  ILE A 196           
-SHEET    8   B11 GLN A 318  ASN A 324  1  N  GLY A 322   O  LEU A 224           
-SHEET    9   B11 GLY A 417  PHE A 423  1  N  TYR A 421   O  LEU A 321           
-SHEET   10   B11 PHE A 502  LEU A 505  1  N  ILE A 503   O  LEU A 420           
-SHEET   11   B11 MET A 510  GLN A 514 -1  N  HIS A 513   O  PHE A 502           
-SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.03  
-SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.03  
-SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.03  
-LINK         C1  NAG A3001                 ND2 ASN A  59     1555   1555  1.46  
-LINK         C1  NAG A3002                 ND2 ASN A 416     1555   1555  1.44  
-LINK         O4  NAG A3002                 C1  NAG A3003     1555   1555  1.41  
-LINK         C1  NAG A3004                 ND2 ASN A 533     1555   1555  1.46  
-LINK         C1  NAG A3005                 ND2 ASN A 457     1555   1555  1.46  
-CISPEP   1 SER A  103    PRO A  104          0        -0.32                     
-SITE     1 CAT  3 SER A 200  GLU A 327  HIS A 440                               
-SITE     1 IHB  3 TRP A  84  PHE A 330  TRP A 279                               
-SITE     1 AC1  5 ASN A  59  SER A  61  THR A  62  HOH A1320                    
-SITE     2 AC1  5 HOH A1323                                                     
-SITE     1 AC2  5 ASN A 416  HOH A1282  HOH A1340  HOH A1341                    
-SITE     2 AC2  5 NAG A3003                                                     
-SITE     1 AC3  2 HOH A1343  NAG A3002                                          
-SITE     1 AC4  1 ASN A 533                                                     
-SITE     1 AC5  2 ASN A 457  HOH A1230                                          
-SITE     1 AC6 11 TRP A  84  TYR A 121  GLU A 199  TRP A 279                    
-SITE     2 AC6 11 LEU A 282  PHE A 290  PHE A 330  PHE A 331                    
-SITE     3 AC6 11 HOH A1159  HOH A1254  HOH A1349                               
-CRYST1  111.925  111.925  136.896  90.00  90.00 120.00 P 31 2 1      6          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.008935  0.005158  0.000000        0.00000                         
-SCALE2      0.000000  0.010317  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.007305        0.00000                         
-ATOM      1  N   ASP A   2     -15.406  83.928  29.132  0.50 28.67           N  
-ATOM      2  CA  ASP A   2     -14.671  84.265  30.386  0.50 34.56           C  
-ATOM      3  C   ASP A   2     -14.854  85.736  30.761  0.50 37.62           C  
-ATOM      4  O   ASP A   2     -15.210  86.561  29.914  0.50 34.18           O  
-ATOM      5  CB  ASP A   2     -13.190  83.937  30.230  0.50 33.58           C  
-ATOM      6  N   HIS A   3     -14.600  86.058  32.029  0.50 39.53           N  
-ATOM      7  CA  HIS A   3     -14.751  87.427  32.514  0.50 41.80           C  
-ATOM      8  C   HIS A   3     -13.567  87.966  33.330  0.50 45.28           C  
-ATOM      9  O   HIS A   3     -12.597  88.467  32.759  0.50 45.33           O  
-ATOM     10  CB  HIS A   3     -16.055  87.560  33.305  0.50 34.92           C  
-ATOM     11  N   SER A   4     -13.649  87.856  34.656  1.00 52.49           N  
-ATOM     12  CA  SER A   4     -12.607  88.358  35.560  1.00 51.14           C  
-ATOM     13  C   SER A   4     -11.444  87.398  35.837  1.00 49.77           C  
-ATOM     14  O   SER A   4     -11.493  86.214  35.496  1.00 47.86           O  
-ATOM     15  CB  SER A   4     -13.241  88.793  36.891  1.00 54.12           C  
-ATOM     16  OG  SER A   4     -12.284  89.363  37.773  1.00 59.66           O  
-ATOM     17  N   GLU A   5     -10.404  87.939  36.473  1.00 46.31           N  
-ATOM     18  CA  GLU A   5      -9.199  87.196  36.839  1.00 42.27           C  
-ATOM     19  C   GLU A   5      -9.462  86.192  37.966  1.00 40.59           C  
-ATOM     20  O   GLU A   5      -8.748  85.200  38.111  1.00 39.25           O  
-ATOM     21  CB  GLU A   5      -8.105  88.184  37.261  1.00 40.50           C  
-ATOM     22  CG  GLU A   5      -6.813  87.545  37.746  1.00 41.93           C  
-ATOM     23  CD  GLU A   5      -5.725  88.563  38.036  1.00 45.67           C  
-ATOM     24  OE1 GLU A   5      -6.029  89.627  38.618  1.00 48.99           O  
-ATOM     25  OE2 GLU A   5      -4.558  88.293  37.682  1.00 43.89           O  
-ATOM     26  N   LEU A   6     -10.496  86.459  38.757  1.00 37.43           N  
-ATOM     27  CA  LEU A   6     -10.861  85.593  39.869  1.00 30.38           C  
-ATOM     28  C   LEU A   6     -11.912  84.564  39.472  1.00 28.34           C  
-ATOM     29  O   LEU A   6     -12.521  83.928  40.328  1.00 27.81           O  
-ATOM     30  CB  LEU A   6     -11.375  86.428  41.041  1.00 28.99           C  
-ATOM     31  CG  LEU A   6     -10.411  87.460  41.622  1.00 27.92           C  
-ATOM     32  CD1 LEU A   6     -11.109  88.213  42.743  1.00 26.75           C  
-ATOM     33  CD2 LEU A   6      -9.143  86.779  42.132  1.00 24.60           C  
-ATOM     34  N   LEU A   7     -12.132  84.413  38.171  1.00 28.29           N  
-ATOM     35  CA  LEU A   7     -13.105  83.454  37.676  1.00 28.05           C  
-ATOM     36  C   LEU A   7     -12.413  82.433  36.777  1.00 30.43           C  
-ATOM     37  O   LEU A   7     -11.830  82.785  35.748  1.00 33.86           O  
-ATOM     38  CB  LEU A   7     -14.218  84.172  36.911  1.00 31.63           C  
-ATOM     39  CG  LEU A   7     -15.382  83.292  36.448  1.00 38.00           C  
-ATOM     40  CD1 LEU A   7     -16.128  82.734  37.654  1.00 36.66           C  
-ATOM     41  CD2 LEU A   7     -16.319  84.099  35.564  1.00 42.94           C  
-ATOM     42  N   VAL A   8     -12.451  81.170  37.190  1.00 28.11           N  
-ATOM     43  CA  VAL A   8     -11.831  80.100  36.418  1.00 24.30           C  
-ATOM     44  C   VAL A   8     -12.853  79.017  36.100  1.00 22.10           C  
-ATOM     45  O   VAL A   8     -13.571  78.551  36.981  1.00 20.96           O  
-ATOM     46  CB  VAL A   8     -10.627  79.480  37.173  1.00 19.94           C  
-ATOM     47  CG1 VAL A   8     -10.035  78.325  36.382  1.00 13.18           C  
-ATOM     48  CG2 VAL A   8      -9.562  80.539  37.419  1.00 17.56           C  
-ATOM     49  N   ASN A   9     -12.940  78.652  34.826  1.00 30.21           N  
-ATOM     50  CA  ASN A   9     -13.868  77.619  34.393  1.00 31.33           C  
-ATOM     51  C   ASN A   9     -13.094  76.309  34.273  1.00 32.01           C  
-ATOM     52  O   ASN A   9     -12.256  76.149  33.382  1.00 37.54           O  
-ATOM     53  CB  ASN A   9     -14.510  78.003  33.055  1.00 35.76           C  
-ATOM     54  CG  ASN A   9     -15.616  77.044  32.631  1.00 47.47           C  
-ATOM     55  OD1 ASN A   9     -15.907  76.911  31.441  1.00 54.98           O  
-ATOM     56  ND2 ASN A   9     -16.241  76.378  33.600  1.00 38.74           N  
-ATOM     57  N   THR A  10     -13.346  75.399  35.209  1.00 25.27           N  
-ATOM     58  CA  THR A  10     -12.676  74.104  35.227  1.00 24.33           C  
-ATOM     59  C   THR A  10     -13.577  72.978  34.730  1.00 23.29           C  
-ATOM     60  O   THR A  10     -14.771  73.173  34.503  1.00 26.53           O  
-ATOM     61  CB  THR A  10     -12.165  73.736  36.646  1.00 22.04           C  
-ATOM     62  OG1 THR A  10     -13.256  73.288  37.458  1.00 19.69           O  
-ATOM     63  CG2 THR A  10     -11.517  74.939  37.310  1.00 21.63           C  
-ATOM     64  N   LYS A  11     -12.989  71.797  34.574  1.00 23.62           N  
-ATOM     65  CA  LYS A  11     -13.709  70.616  34.115  1.00 22.58           C  
-ATOM     66  C   LYS A  11     -14.766  70.176  35.123  1.00 21.95           C  
-ATOM     67  O   LYS A  11     -15.659  69.395  34.793  1.00 24.43           O  
-ATOM     68  CB  LYS A  11     -12.724  69.475  33.849  1.00 25.94           C  
-ATOM     69  CG  LYS A  11     -11.708  69.781  32.751  1.00 24.34           C  
-ATOM     70  CD  LYS A  11     -10.627  68.718  32.681  1.00 27.34           C  
-ATOM     71  CE  LYS A  11      -9.663  68.981  31.537  1.00 24.10           C  
-ATOM     72  NZ  LYS A  11      -8.614  67.928  31.458  1.00 27.68           N  
-ATOM     73  N   SER A  12     -14.648  70.668  36.353  1.00 27.18           N  
-ATOM     74  CA  SER A  12     -15.598  70.351  37.416  1.00 28.44           C  
-ATOM     75  C   SER A  12     -16.652  71.452  37.556  1.00 28.23           C  
-ATOM     76  O   SER A  12     -17.725  71.228  38.120  1.00 24.24           O  
-ATOM     77  CB  SER A  12     -14.865  70.161  38.745  1.00 32.09           C  
-ATOM     78  OG  SER A  12     -14.108  68.965  38.747  1.00 38.82           O  
-ATOM     79  N   GLY A  13     -16.333  72.641  37.046  1.00 27.22           N  
-ATOM     80  CA  GLY A  13     -17.252  73.765  37.119  1.00 23.99           C  
-ATOM     81  C   GLY A  13     -16.529  75.084  37.316  1.00 28.13           C  
-ATOM     82  O   GLY A  13     -15.300  75.127  37.336  1.00 31.49           O  
-ATOM     83  N   LYS A  14     -17.286  76.169  37.459  1.00 31.18           N  
-ATOM     84  CA  LYS A  14     -16.694  77.489  37.657  1.00 32.18           C  
-ATOM     85  C   LYS A  14     -16.349  77.717  39.125  1.00 31.96           C  
-ATOM     86  O   LYS A  14     -17.085  77.296  40.019  1.00 28.38           O  
-ATOM     87  CB  LYS A  14     -17.632  78.589  37.153  1.00 38.02           C  
-ATOM     88  CG  LYS A  14     -17.797  78.634  35.639  1.00 47.85           C  
-ATOM     89  CD  LYS A  14     -18.701  79.785  35.212  1.00 54.66           C  
-ATOM     90  CE  LYS A  14     -18.827  79.877  33.696  1.00 59.05           C  
-ATOM     91  NZ  LYS A  14     -19.629  81.063  33.276  1.00 59.60           N  
-ATOM     92  N   VAL A  15     -15.222  78.384  39.359  1.00 31.47           N  
-ATOM     93  CA  VAL A  15     -14.739  78.676  40.707  1.00 31.17           C  
-ATOM     94  C   VAL A  15     -14.408  80.164  40.852  1.00 30.49           C  
-ATOM     95  O   VAL A  15     -13.758  80.747  39.985  1.00 36.39           O  
-ATOM     96  CB  VAL A  15     -13.464  77.837  41.025  1.00 31.34           C  
-ATOM     97  CG1 VAL A  15     -12.854  78.268  42.338  1.00 34.36           C  
-ATOM     98  CG2 VAL A  15     -13.803  76.355  41.082  1.00 32.70           C  
-ATOM     99  N   MET A  16     -14.859  80.770  41.949  1.00 26.55           N  
-ATOM    100  CA  MET A  16     -14.596  82.184  42.212  1.00 27.93           C  
-ATOM    101  C   MET A  16     -13.589  82.357  43.350  1.00 27.19           C  
-ATOM    102  O   MET A  16     -13.820  81.905  44.473  1.00 26.94           O  
-ATOM    103  CB  MET A  16     -15.901  82.920  42.549  1.00 37.43           C  
-ATOM    104  CG  MET A  16     -15.741  84.413  42.882  1.00 45.41           C  
-ATOM    105  SD  MET A  16     -15.159  85.453  41.515  1.00 54.92           S  
-ATOM    106  CE  MET A  16     -16.721  86.013  40.838  1.00 56.10           C  
-ATOM    107  N   GLY A  17     -12.482  83.031  43.055  1.00 21.15           N  
-ATOM    108  CA  GLY A  17     -11.454  83.256  44.055  1.00 24.14           C  
-ATOM    109  C   GLY A  17     -11.547  84.608  44.736  1.00 25.33           C  
-ATOM    110  O   GLY A  17     -12.587  85.270  44.686  1.00 29.67           O  
-ATOM    111  N   THR A  18     -10.448  85.020  45.364  1.00 24.92           N  
-ATOM    112  CA  THR A  18     -10.381  86.292  46.074  1.00 27.24           C  
-ATOM    113  C   THR A  18      -8.979  86.883  45.993  1.00 27.80           C  
-ATOM    114  O   THR A  18      -7.990  86.147  45.956  1.00 30.22           O  
-ATOM    115  CB  THR A  18     -10.786  86.124  47.569  1.00 32.62           C  
-ATOM    116  OG1 THR A  18     -10.607  87.364  48.268  1.00 40.31           O  
-ATOM    117  CG2 THR A  18      -9.954  85.036  48.244  1.00 26.80           C  
-ATOM    118  N   ARG A  19      -8.899  88.211  45.942  1.00 31.78           N  
-ATOM    119  CA  ARG A  19      -7.612  88.897  45.874  1.00 35.99           C  
-ATOM    120  C   ARG A  19      -7.022  88.999  47.282  1.00 35.98           C  
-ATOM    121  O   ARG A  19      -7.624  89.587  48.184  1.00 40.30           O  
-ATOM    122  CB  ARG A  19      -7.768  90.279  45.229  1.00 37.13           C  
-ATOM    123  CG  ARG A  19      -6.450  90.940  44.828  1.00 48.77           C  
-ATOM    124  CD  ARG A  19      -6.682  92.045  43.798  1.00 54.98           C  
-ATOM    125  NE  ARG A  19      -5.454  92.752  43.420  1.00 61.38           N  
-ATOM    126  CZ  ARG A  19      -4.580  92.333  42.507  1.00 60.88           C  
-ATOM    127  NH1 ARG A  19      -4.772  91.196  41.857  1.00 63.26           N  
-ATOM    128  NH2 ARG A  19      -3.514  93.073  42.229  1.00 60.29           N  
-ATOM    129  N   VAL A  20      -5.857  88.384  47.462  1.00 35.05           N  
-ATOM    130  CA  VAL A  20      -5.167  88.355  48.747  1.00 32.71           C  
-ATOM    131  C   VAL A  20      -3.914  89.232  48.775  1.00 30.07           C  
-ATOM    132  O   VAL A  20      -3.112  89.211  47.843  1.00 30.64           O  
-ATOM    133  CB  VAL A  20      -4.780  86.894  49.113  1.00 30.40           C  
-ATOM    134  CG1 VAL A  20      -3.999  86.849  50.417  1.00 42.17           C  
-ATOM    135  CG2 VAL A  20      -6.031  86.040  49.227  1.00 23.12           C  
-ATOM    136  N   PRO A  21      -3.747  90.033  49.844  1.00 31.52           N  
-ATOM    137  CA  PRO A  21      -2.591  90.926  50.012  1.00 34.94           C  
-ATOM    138  C   PRO A  21      -1.336  90.128  50.365  1.00 36.37           C  
-ATOM    139  O   PRO A  21      -1.383  89.237  51.212  1.00 41.30           O  
-ATOM    140  CB  PRO A  21      -3.009  91.818  51.188  1.00 31.60           C  
-ATOM    141  CG  PRO A  21      -4.509  91.738  51.188  1.00 35.84           C  
-ATOM    142  CD  PRO A  21      -4.753  90.291  50.888  1.00 31.68           C  
-ATOM    143  N   VAL A  22      -0.225  90.433  49.702  1.00 35.95           N  
-ATOM    144  CA  VAL A  22       1.035  89.740  49.958  1.00 35.08           C  
-ATOM    145  C   VAL A  22       2.210  90.696  49.803  1.00 36.32           C  
-ATOM    146  O   VAL A  22       2.519  91.122  48.690  1.00 37.53           O  
-ATOM    147  CB  VAL A  22       1.278  88.571  48.967  1.00 34.60           C  
-ATOM    148  CG1 VAL A  22       2.399  87.679  49.482  1.00 27.54           C  
-ATOM    149  CG2 VAL A  22       0.013  87.772  48.732  1.00 37.91           C  
-ATOM    150  N   LEU A  23       2.865  91.016  50.918  1.00 37.77           N  
-ATOM    151  CA  LEU A  23       4.027  91.904  50.931  1.00 43.60           C  
-ATOM    152  C   LEU A  23       3.868  93.144  50.041  1.00 51.29           C  
-ATOM    153  O   LEU A  23       4.599  93.309  49.058  1.00 52.34           O  
-ATOM    154  CB  LEU A  23       5.272  91.121  50.508  1.00 36.52           C  
-ATOM    155  CG  LEU A  23       5.500  89.764  51.173  1.00 32.03           C  
-ATOM    156  CD1 LEU A  23       6.670  89.062  50.515  1.00 29.19           C  
-ATOM    157  CD2 LEU A  23       5.738  89.944  52.661  1.00 37.51           C  
-ATOM    158  N   SER A  24       2.891  93.987  50.373  1.00 53.70           N  
-ATOM    159  CA  SER A  24       2.604  95.219  49.628  1.00 54.78           C  
-ATOM    160  C   SER A  24       1.918  95.020  48.273  1.00 52.07           C  
-ATOM    161  O   SER A  24       1.242  95.923  47.777  1.00 56.81           O  
-ATOM    162  CB  SER A  24       3.873  96.066  49.465  1.00 56.46           C  
-ATOM    163  OG  SER A  24       4.376  96.473  50.729  1.00 64.88           O  
-ATOM    164  N   SER A  25       2.092  93.844  47.677  1.00 48.21           N  
-ATOM    165  CA  SER A  25       1.478  93.533  46.388  1.00 41.56           C  
-ATOM    166  C   SER A  25       0.240  92.657  46.604  1.00 38.66           C  
-ATOM    167  O   SER A  25      -0.261  92.555  47.726  1.00 33.43           O  
-ATOM    168  CB  SER A  25       2.491  92.832  45.483  1.00 43.09           C  
-ATOM    169  OG  SER A  25       1.992  92.693  44.168  1.00 42.79           O  
-ATOM    170  N   HIS A  26      -0.270  92.045  45.535  1.00 38.65           N  
-ATOM    171  CA  HIS A  26      -1.457  91.190  45.629  1.00 41.41           C  
-ATOM    172  C   HIS A  26      -1.415  90.013  44.654  1.00 40.06           C  
-ATOM    173  O   HIS A  26      -0.762  90.082  43.611  1.00 42.74           O  
-ATOM    174  CB  HIS A  26      -2.733  91.995  45.331  1.00 51.36           C  
-ATOM    175  CG  HIS A  26      -3.027  93.084  46.317  1.00 63.89           C  
-ATOM    176  ND1 HIS A  26      -3.859  92.901  47.402  1.00 68.51           N  
-ATOM    177  CD2 HIS A  26      -2.630  94.379  46.365  1.00 66.86           C  
-ATOM    178  CE1 HIS A  26      -3.962  94.034  48.074  1.00 69.08           C  
-ATOM    179  NE2 HIS A  26      -3.225  94.945  47.466  1.00 71.31           N  
-ATOM    180  N   ILE A  27      -2.109  88.932  45.013  1.00 36.86           N  
-ATOM    181  CA  ILE A  27      -2.218  87.735  44.170  1.00 32.45           C  
-ATOM    182  C   ILE A  27      -3.602  87.116  44.349  1.00 28.39           C  
-ATOM    183  O   ILE A  27      -4.388  87.565  45.180  1.00 29.63           O  
-ATOM    184  CB  ILE A  27      -1.155  86.645  44.481  1.00 33.61           C  
-ATOM    185  CG1 ILE A  27      -1.345  86.087  45.889  1.00 36.42           C  
-ATOM    186  CG2 ILE A  27       0.253  87.176  44.258  1.00 38.29           C  
-ATOM    187  CD1 ILE A  27      -0.493  84.877  46.160  1.00 38.09           C  
-ATOM    188  N   SER A  28      -3.893  86.079  43.571  1.00 26.44           N  
-ATOM    189  CA  SER A  28      -5.188  85.407  43.639  1.00 28.97           C  
-ATOM    190  C   SER A  28      -5.160  84.161  44.517  1.00 29.40           C  
-ATOM    191  O   SER A  28      -4.123  83.514  44.661  1.00 31.49           O  
-ATOM    192  CB  SER A  28      -5.663  85.024  42.236  1.00 29.17           C  
-ATOM    193  OG  SER A  28      -5.612  86.132  41.359  1.00 33.73           O  
-ATOM    194  N   ALA A  29      -6.315  83.818  45.078  1.00 27.60           N  
-ATOM    195  CA  ALA A  29      -6.436  82.648  45.934  1.00 24.46           C  
-ATOM    196  C   ALA A  29      -7.776  81.943  45.748  1.00 26.44           C  
-ATOM    197  O   ALA A  29      -8.843  82.548  45.863  1.00 29.34           O  
-ATOM    198  CB  ALA A  29      -6.238  83.037  47.393  1.00 26.18           C  
-ATOM    199  N   PHE A  30      -7.701  80.660  45.422  1.00 23.41           N  
-ATOM    200  CA  PHE A  30      -8.877  79.831  45.224  1.00 26.29           C  
-ATOM    201  C   PHE A  30      -8.855  78.810  46.349  1.00 27.55           C  
-ATOM    202  O   PHE A  30      -8.205  77.771  46.254  1.00 30.19           O  
-ATOM    203  CB  PHE A  30      -8.820  79.162  43.849  1.00 25.58           C  
-ATOM    204  CG  PHE A  30      -8.781  80.141  42.714  1.00 24.47           C  
-ATOM    205  CD1 PHE A  30      -7.579  80.721  42.323  1.00 25.66           C  
-ATOM    206  CD2 PHE A  30      -9.953  80.524  42.070  1.00 21.44           C  
-ATOM    207  CE1 PHE A  30      -7.543  81.676  41.308  1.00 28.22           C  
-ATOM    208  CE2 PHE A  30      -9.931  81.477  41.053  1.00 23.27           C  
-ATOM    209  CZ  PHE A  30      -8.722  82.057  40.672  1.00 23.14           C  
-ATOM    210  N   LEU A  31      -9.557  79.136  47.426  1.00 26.52           N  
-ATOM    211  CA  LEU A  31      -9.595  78.294  48.607  1.00 24.09           C  
-ATOM    212  C   LEU A  31     -10.834  77.419  48.751  1.00 22.67           C  
-ATOM    213  O   LEU A  31     -11.953  77.857  48.497  1.00 26.17           O  
-ATOM    214  CB  LEU A  31      -9.439  79.175  49.847  1.00 21.60           C  
-ATOM    215  CG  LEU A  31      -8.340  80.237  49.754  1.00 15.70           C  
-ATOM    216  CD1 LEU A  31      -8.346  81.105  51.007  1.00 15.84           C  
-ATOM    217  CD2 LEU A  31      -6.984  79.579  49.548  1.00 16.39           C  
-ATOM    218  N   GLY A  32     -10.618  76.177  49.170  1.00 24.65           N  
-ATOM    219  CA  GLY A  32     -11.715  75.250  49.380  1.00 26.80           C  
-ATOM    220  C   GLY A  32     -12.382  74.697  48.140  1.00 26.92           C  
-ATOM    221  O   GLY A  32     -13.605  74.712  48.038  1.00 32.10           O  
-ATOM    222  N   ILE A  33     -11.587  74.226  47.187  1.00 27.32           N  
-ATOM    223  CA  ILE A  33     -12.135  73.641  45.969  1.00 25.04           C  
-ATOM    224  C   ILE A  33     -12.249  72.136  46.194  1.00 27.00           C  
-ATOM    225  O   ILE A  33     -11.267  71.477  46.531  1.00 28.62           O  
-ATOM    226  CB  ILE A  33     -11.221  73.899  44.749  1.00 24.40           C  
-ATOM    227  CG1 ILE A  33     -11.081  75.404  44.502  1.00 20.81           C  
-ATOM    228  CG2 ILE A  33     -11.782  73.201  43.515  1.00 17.33           C  
-ATOM    229  CD1 ILE A  33     -10.091  75.757  43.414  1.00 24.16           C  
-ATOM    230  N   PRO A  34     -13.462  71.579  46.039  1.00 26.39           N  
-ATOM    231  CA  PRO A  34     -13.673  70.142  46.232  1.00 24.57           C  
-ATOM    232  C   PRO A  34     -13.116  69.301  45.080  1.00 28.16           C  
-ATOM    233  O   PRO A  34     -13.358  69.592  43.907  1.00 35.07           O  
-ATOM    234  CB  PRO A  34     -15.193  70.043  46.324  1.00 25.97           C  
-ATOM    235  CG  PRO A  34     -15.644  71.116  45.388  1.00 17.90           C  
-ATOM    236  CD  PRO A  34     -14.728  72.264  45.730  1.00 19.50           C  
-ATOM    237  N   PHE A  35     -12.326  68.288  45.422  1.00 25.89           N  
-ATOM    238  CA  PHE A  35     -11.755  67.401  44.416  1.00 25.14           C  
-ATOM    239  C   PHE A  35     -12.344  66.000  44.548  1.00 27.39           C  
-ATOM    240  O   PHE A  35     -12.031  65.103  43.759  1.00 30.45           O  
-ATOM    241  CB  PHE A  35     -10.221  67.365  44.517  1.00 28.41           C  
-ATOM    242  CG  PHE A  35      -9.698  66.885  45.846  1.00 24.26           C  
-ATOM    243  CD1 PHE A  35      -9.585  65.523  46.116  1.00 27.62           C  
-ATOM    244  CD2 PHE A  35      -9.296  67.792  46.818  1.00 23.58           C  
-ATOM    245  CE1 PHE A  35      -9.080  65.073  47.333  1.00 21.98           C  
-ATOM    246  CE2 PHE A  35      -8.788  67.349  48.040  1.00 27.64           C  
-ATOM    247  CZ  PHE A  35      -8.681  65.988  48.296  1.00 22.09           C  
-ATOM    248  N   ALA A  36     -13.205  65.824  45.548  1.00 22.34           N  
-ATOM    249  CA  ALA A  36     -13.851  64.540  45.797  1.00 25.38           C  
-ATOM    250  C   ALA A  36     -15.209  64.726  46.461  1.00 25.30           C  
-ATOM    251  O   ALA A  36     -15.532  65.809  46.955  1.00 27.77           O  
-ATOM    252  CB  ALA A  36     -12.962  63.661  46.676  1.00 21.16           C  
-ATOM    253  N   GLU A  37     -16.020  63.675  46.418  1.00 25.22           N  
-ATOM    254  CA  GLU A  37     -17.337  63.685  47.041  1.00 22.92           C  
-ATOM    255  C   GLU A  37     -17.115  63.511  48.538  1.00 27.31           C  
-ATOM    256  O   GLU A  37     -16.239  62.744  48.951  1.00 22.99           O  
-ATOM    257  CB  GLU A  37     -18.190  62.525  46.512  1.00 15.75           C  
-ATOM    258  CG  GLU A  37     -18.890  62.801  45.192  1.00 16.85           C  
-ATOM    259  CD  GLU A  37     -19.933  63.890  45.314  1.00 27.07           C  
-ATOM    260  OE1 GLU A  37     -20.963  63.651  45.981  1.00 28.35           O  
-ATOM    261  OE2 GLU A  37     -19.723  64.987  44.754  1.00 34.76           O  
-ATOM    262  N   PRO A  38     -17.878  64.244  49.368  1.00 30.13           N  
-ATOM    263  CA  PRO A  38     -17.760  64.161  50.832  1.00 28.59           C  
-ATOM    264  C   PRO A  38     -17.781  62.702  51.292  1.00 29.67           C  
-ATOM    265  O   PRO A  38     -18.760  61.993  51.074  1.00 32.92           O  
-ATOM    266  CB  PRO A  38     -18.997  64.917  51.305  1.00 26.99           C  
-ATOM    267  CG  PRO A  38     -19.134  65.983  50.267  1.00 26.87           C  
-ATOM    268  CD  PRO A  38     -18.908  65.223  48.981  1.00 26.55           C  
-ATOM    269  N   PRO A  39     -16.681  62.232  51.910  1.00 29.14           N  
-ATOM    270  CA  PRO A  39     -16.537  60.858  52.411  1.00 27.40           C  
-ATOM    271  C   PRO A  39     -17.327  60.590  53.687  1.00 31.46           C  
-ATOM    272  O   PRO A  39     -16.855  59.900  54.593  1.00 31.60           O  
-ATOM    273  CB  PRO A  39     -15.037  60.757  52.656  1.00 26.61           C  
-ATOM    274  CG  PRO A  39     -14.705  62.128  53.136  1.00 25.77           C  
-ATOM    275  CD  PRO A  39     -15.454  63.008  52.162  1.00 26.71           C  
-ATOM    276  N   VAL A  40     -18.540  61.129  53.740  1.00 31.26           N  
-ATOM    277  CA  VAL A  40     -19.418  60.976  54.889  1.00 29.16           C  
-ATOM    278  C   VAL A  40     -20.383  59.806  54.733  1.00 32.27           C  
-ATOM    279  O   VAL A  40     -20.581  59.286  53.632  1.00 32.76           O  
-ATOM    280  CB  VAL A  40     -20.239  62.264  55.121  1.00 28.22           C  
-ATOM    281  CG1 VAL A  40     -19.316  63.423  55.476  1.00 27.12           C  
-ATOM    282  CG2 VAL A  40     -21.053  62.602  53.873  1.00 16.51           C  
-ATOM    283  N   GLY A  41     -20.971  59.394  55.855  1.00 35.13           N  
-ATOM    284  CA  GLY A  41     -21.934  58.307  55.858  1.00 33.81           C  
-ATOM    285  C   GLY A  41     -21.396  56.929  55.525  1.00 36.50           C  
-ATOM    286  O   GLY A  41     -20.431  56.466  56.130  1.00 40.41           O  
-ATOM    287  N   ASN A  42     -22.026  56.278  54.549  1.00 40.54           N  
-ATOM    288  CA  ASN A  42     -21.637  54.935  54.125  1.00 40.60           C  
-ATOM    289  C   ASN A  42     -20.280  54.948  53.450  1.00 37.18           C  
-ATOM    290  O   ASN A  42     -19.634  53.909  53.328  1.00 34.59           O  
-ATOM    291  CB  ASN A  42     -22.663  54.357  53.147  1.00 52.99           C  
-ATOM    292  CG  ASN A  42     -24.083  54.483  53.645  1.00 65.20           C  
-ATOM    293  OD1 ASN A  42     -24.917  55.152  53.031  1.00 67.79           O  
-ATOM    294  ND2 ASN A  42     -24.367  53.843  54.773  1.00 70.34           N  
-ATOM    295  N   MET A  43     -19.864  56.124  52.991  1.00 31.22           N  
-ATOM    296  CA  MET A  43     -18.583  56.260  52.323  1.00 34.35           C  
-ATOM    297  C   MET A  43     -17.385  56.414  53.250  1.00 31.74           C  
-ATOM    298  O   MET A  43     -16.249  56.513  52.783  1.00 30.88           O  
-ATOM    299  CB  MET A  43     -18.635  57.394  51.306  1.00 38.69           C  
-ATOM    300  CG  MET A  43     -19.611  57.132  50.181  1.00 36.92           C  
-ATOM    301  SD  MET A  43     -19.088  57.959  48.689  1.00 60.77           S  
-ATOM    302  CE  MET A  43     -19.306  59.664  49.165  1.00 48.41           C  
-ATOM    303  N   ARG A  44     -17.635  56.427  54.558  1.00 29.82           N  
-ATOM    304  CA  ARG A  44     -16.552  56.537  55.528  1.00 28.53           C  
-ATOM    305  C   ARG A  44     -15.704  55.272  55.402  1.00 30.16           C  
-ATOM    306  O   ARG A  44     -16.243  54.169  55.306  1.00 31.52           O  
-ATOM    307  CB  ARG A  44     -17.097  56.664  56.956  1.00 28.51           C  
-ATOM    308  CG  ARG A  44     -16.008  56.857  58.008  1.00 30.42           C  
-ATOM    309  CD  ARG A  44     -16.518  56.688  59.436  1.00 28.64           C  
-ATOM    310  NE  ARG A  44     -17.225  57.860  59.948  1.00 29.51           N  
-ATOM    311  CZ  ARG A  44     -17.725  57.952  61.179  1.00 25.88           C  
-ATOM    312  NH1 ARG A  44     -17.600  56.941  62.031  1.00 18.81           N  
-ATOM    313  NH2 ARG A  44     -18.355  59.054  61.561  1.00 26.40           N  
-ATOM    314  N   PHE A  45     -14.385  55.453  55.341  1.00 28.90           N  
-ATOM    315  CA  PHE A  45     -13.415  54.363  55.211  1.00 29.64           C  
-ATOM    316  C   PHE A  45     -13.276  53.875  53.773  1.00 28.12           C  
-ATOM    317  O   PHE A  45     -12.344  53.141  53.452  1.00 30.56           O  
-ATOM    318  CB  PHE A  45     -13.762  53.176  56.124  1.00 33.35           C  
-ATOM    319  CG  PHE A  45     -13.865  53.531  57.584  1.00 36.71           C  
-ATOM    320  CD1 PHE A  45     -12.841  54.224  58.223  1.00 35.54           C  
-ATOM    321  CD2 PHE A  45     -14.990  53.170  58.319  1.00 37.27           C  
-ATOM    322  CE1 PHE A  45     -12.937  54.552  59.574  1.00 36.20           C  
-ATOM    323  CE2 PHE A  45     -15.095  53.494  59.669  1.00 40.21           C  
-ATOM    324  CZ  PHE A  45     -14.066  54.187  60.298  1.00 36.23           C  
-ATOM    325  N   ARG A  46     -14.206  54.284  52.914  1.00 31.76           N  
-ATOM    326  CA  ARG A  46     -14.198  53.893  51.504  1.00 35.58           C  
-ATOM    327  C   ARG A  46     -13.245  54.734  50.664  1.00 32.76           C  
-ATOM    328  O   ARG A  46     -12.812  55.812  51.079  1.00 33.35           O  
-ATOM    329  CB  ARG A  46     -15.602  54.025  50.908  1.00 42.32           C  
-ATOM    330  CG  ARG A  46     -16.430  52.759  50.894  1.00 48.84           C  
-ATOM    331  CD  ARG A  46     -17.765  53.028  50.213  1.00 58.41           C  
-ATOM    332  NE  ARG A  46     -18.475  51.802  49.859  1.00 72.99           N  
-ATOM    333  CZ  ARG A  46     -18.216  51.067  48.779  1.00 80.38           C  
-ATOM    334  NH1 ARG A  46     -17.258  51.423  47.931  1.00 80.76           N  
-ATOM    335  NH2 ARG A  46     -18.926  49.973  48.534  1.00 84.59           N  
-ATOM    336  N   ARG A  47     -12.940  54.236  49.468  1.00 30.84           N  
-ATOM    337  CA  ARG A  47     -12.071  54.945  48.533  1.00 29.91           C  
-ATOM    338  C   ARG A  47     -12.763  56.248  48.135  1.00 25.96           C  
-ATOM    339  O   ARG A  47     -13.992  56.332  48.128  1.00 27.15           O  
-ATOM    340  CB  ARG A  47     -11.837  54.108  47.268  1.00 29.69           C  
-ATOM    341  CG  ARG A  47     -10.973  52.883  47.454  1.00 37.80           C  
-ATOM    342  CD  ARG A  47     -10.697  52.207  46.117  1.00 41.81           C  
-ATOM    343  NE  ARG A  47      -9.565  51.286  46.207  1.00 52.56           N  
-ATOM    344  CZ  ARG A  47      -9.635  50.036  46.659  1.00 54.44           C  
-ATOM    345  NH1 ARG A  47     -10.791  49.526  47.064  1.00 55.10           N  
-ATOM    346  NH2 ARG A  47      -8.536  49.298  46.732  1.00 54.67           N  
-ATOM    347  N   PRO A  48     -11.985  57.289  47.812  1.00 25.06           N  
-ATOM    348  CA  PRO A  48     -12.598  58.559  47.419  1.00 24.18           C  
-ATOM    349  C   PRO A  48     -13.284  58.477  46.051  1.00 26.31           C  
-ATOM    350  O   PRO A  48     -12.824  57.765  45.153  1.00 23.22           O  
-ATOM    351  CB  PRO A  48     -11.403  59.512  47.396  1.00 19.85           C  
-ATOM    352  CG  PRO A  48     -10.270  58.611  46.993  1.00 16.51           C  
-ATOM    353  CD  PRO A  48     -10.515  57.398  47.847  1.00 20.79           C  
-ATOM    354  N   GLU A  49     -14.415  59.163  45.926  1.00 24.85           N  
-ATOM    355  CA  GLU A  49     -15.166  59.212  44.676  1.00 30.27           C  
-ATOM    356  C   GLU A  49     -14.973  60.622  44.128  1.00 28.14           C  
-ATOM    357  O   GLU A  49     -14.946  61.585  44.890  1.00 27.41           O  
-ATOM    358  CB  GLU A  49     -16.653  58.943  44.927  1.00 30.92           C  
-ATOM    359  CG  GLU A  49     -16.955  57.567  45.513  1.00 48.89           C  
-ATOM    360  CD  GLU A  49     -16.737  56.436  44.521  1.00 59.22           C  
-ATOM    361  OE1 GLU A  49     -17.698  56.090  43.804  1.00 67.08           O  
-ATOM    362  OE2 GLU A  49     -15.616  55.884  44.464  1.00 64.72           O  
-ATOM    363  N   PRO A  50     -14.789  60.759  42.807  1.00 29.06           N  
-ATOM    364  CA  PRO A  50     -14.593  62.075  42.188  1.00 26.33           C  
-ATOM    365  C   PRO A  50     -15.773  63.009  42.438  1.00 26.29           C  
-ATOM    366  O   PRO A  50     -16.927  62.583  42.404  1.00 30.99           O  
-ATOM    367  CB  PRO A  50     -14.467  61.733  40.703  1.00 29.27           C  
-ATOM    368  CG  PRO A  50     -13.868  60.358  40.723  1.00 33.55           C  
-ATOM    369  CD  PRO A  50     -14.676  59.687  41.802  1.00 32.96           C  
-ATOM    370  N   LYS A  51     -15.478  64.277  42.699  1.00 25.91           N  
-ATOM    371  CA  LYS A  51     -16.518  65.271  42.949  1.00 27.45           C  
-ATOM    372  C   LYS A  51     -17.383  65.480  41.709  1.00 34.22           C  
-ATOM    373  O   LYS A  51     -16.877  65.869  40.653  1.00 34.82           O  
-ATOM    374  CB  LYS A  51     -15.882  66.602  43.356  1.00 23.83           C  
-ATOM    375  CG  LYS A  51     -16.863  67.750  43.540  1.00 23.58           C  
-ATOM    376  CD  LYS A  51     -17.800  67.518  44.707  1.00 26.03           C  
-ATOM    377  CE  LYS A  51     -18.757  68.685  44.881  1.00 26.46           C  
-ATOM    378  NZ  LYS A  51     -19.725  68.455  45.991  1.00 41.52           N  
-ATOM    379  N   LYS A  52     -18.680  65.204  41.836  1.00 35.51           N  
-ATOM    380  CA  LYS A  52     -19.609  65.393  40.726  1.00 33.83           C  
-ATOM    381  C   LYS A  52     -19.553  66.861  40.328  1.00 34.81           C  
-ATOM    382  O   LYS A  52     -19.646  67.742  41.183  1.00 35.97           O  
-ATOM    383  CB  LYS A  52     -21.047  65.060  41.137  1.00 37.15           C  
-ATOM    384  CG  LYS A  52     -21.309  63.624  41.550  1.00 43.69           C  
-ATOM    385  CD  LYS A  52     -22.810  63.413  41.729  1.00 55.87           C  
-ATOM    386  CE  LYS A  52     -23.154  62.752  43.057  1.00 56.58           C  
-ATOM    387  NZ  LYS A  52     -22.737  61.322  43.116  1.00 62.76           N  
-ATOM    388  N   PRO A  53     -19.369  67.143  39.028  1.00 34.98           N  
-ATOM    389  CA  PRO A  53     -19.302  68.523  38.539  1.00 33.81           C  
-ATOM    390  C   PRO A  53     -20.508  69.338  39.001  1.00 36.07           C  
-ATOM    391  O   PRO A  53     -21.625  68.820  39.096  1.00 35.03           O  
-ATOM    392  CB  PRO A  53     -19.289  68.337  37.025  1.00 34.81           C  
-ATOM    393  CG  PRO A  53     -18.530  67.057  36.864  1.00 37.65           C  
-ATOM    394  CD  PRO A  53     -19.165  66.187  37.926  1.00 35.69           C  
-ATOM    395  N   TRP A  54     -20.265  70.602  39.328  1.00 34.35           N  
-ATOM    396  CA  TRP A  54     -21.326  71.485  39.802  1.00 37.95           C  
-ATOM    397  C   TRP A  54     -21.723  72.547  38.784  1.00 43.22           C  
-ATOM    398  O   TRP A  54     -20.932  72.926  37.919  1.00 43.06           O  
-ATOM    399  CB  TRP A  54     -20.907  72.165  41.114  1.00 30.55           C  
-ATOM    400  CG  TRP A  54     -19.617  72.927  41.009  1.00 27.37           C  
-ATOM    401  CD1 TRP A  54     -19.460  74.225  40.607  1.00 24.17           C  
-ATOM    402  CD2 TRP A  54     -18.300  72.428  41.279  1.00 26.67           C  
-ATOM    403  NE1 TRP A  54     -18.126  74.560  40.606  1.00 27.83           N  
-ATOM    404  CE2 TRP A  54     -17.392  73.479  41.015  1.00 25.64           C  
-ATOM    405  CE3 TRP A  54     -17.798  71.194  41.720  1.00 27.07           C  
-ATOM    406  CZ2 TRP A  54     -16.009  73.333  41.176  1.00 26.30           C  
-ATOM    407  CZ3 TRP A  54     -16.422  71.050  41.880  1.00 22.21           C  
-ATOM    408  CH2 TRP A  54     -15.545  72.116  41.609  1.00 23.22           C  
-ATOM    409  N   SER A  55     -22.965  73.007  38.892  1.00 46.84           N  
-ATOM    410  CA  SER A  55     -23.484  74.049  38.017  1.00 51.37           C  
-ATOM    411  C   SER A  55     -23.392  75.368  38.773  1.00 48.87           C  
-ATOM    412  O   SER A  55     -23.471  75.393  40.002  1.00 48.98           O  
-ATOM    413  CB  SER A  55     -24.937  73.760  37.633  1.00 59.31           C  
-ATOM    414  OG  SER A  55     -25.028  72.608  36.809  1.00 71.42           O  
-ATOM    415  N   GLY A  56     -23.207  76.459  38.039  1.00 44.94           N  
-ATOM    416  CA  GLY A  56     -23.094  77.756  38.677  1.00 41.25           C  
-ATOM    417  C   GLY A  56     -21.676  77.992  39.160  1.00 39.00           C  
-ATOM    418  O   GLY A  56     -20.765  77.248  38.801  1.00 37.01           O  
-ATOM    419  N   VAL A  57     -21.493  79.011  39.994  1.00 35.99           N  
-ATOM    420  CA  VAL A  57     -20.172  79.356  40.517  1.00 35.65           C  
-ATOM    421  C   VAL A  57     -19.951  78.910  41.963  1.00 36.78           C  
-ATOM    422  O   VAL A  57     -20.773  79.173  42.842  1.00 39.18           O  
-ATOM    423  CB  VAL A  57     -19.912  80.879  40.418  1.00 36.82           C  
-ATOM    424  CG1 VAL A  57     -18.524  81.216  40.928  1.00 35.44           C  
-ATOM    425  CG2 VAL A  57     -20.073  81.347  38.980  1.00 39.55           C  
-ATOM    426  N   TRP A  58     -18.827  78.238  42.197  1.00 34.56           N  
-ATOM    427  CA  TRP A  58     -18.472  77.760  43.527  1.00 32.11           C  
-ATOM    428  C   TRP A  58     -17.720  78.873  44.253  1.00 32.18           C  
-ATOM    429  O   TRP A  58     -16.757  79.421  43.716  1.00 30.09           O  
-ATOM    430  CB  TRP A  58     -17.582  76.514  43.418  1.00 33.53           C  
-ATOM    431  CG  TRP A  58     -17.287  75.846  44.735  1.00 37.07           C  
-ATOM    432  CD1 TRP A  58     -16.333  76.207  45.647  1.00 33.28           C  
-ATOM    433  CD2 TRP A  58     -17.958  74.703  45.290  1.00 39.96           C  
-ATOM    434  NE1 TRP A  58     -16.372  75.367  46.734  1.00 34.43           N  
-ATOM    435  CE2 TRP A  58     -17.359  74.434  46.542  1.00 38.70           C  
-ATOM    436  CE3 TRP A  58     -19.006  73.882  44.851  1.00 42.01           C  
-ATOM    437  CZ2 TRP A  58     -17.773  73.376  47.363  1.00 37.33           C  
-ATOM    438  CZ3 TRP A  58     -19.419  72.828  45.667  1.00 43.69           C  
-ATOM    439  CH2 TRP A  58     -18.801  72.587  46.909  1.00 39.95           C  
-ATOM    440  N   ASN A  59     -18.181  79.228  45.452  1.00 32.16           N  
-ATOM    441  CA  ASN A  59     -17.528  80.274  46.241  1.00 34.63           C  
-ATOM    442  C   ASN A  59     -16.250  79.716  46.871  1.00 36.34           C  
-ATOM    443  O   ASN A  59     -16.300  78.922  47.814  1.00 38.82           O  
-ATOM    444  CB  ASN A  59     -18.471  80.816  47.328  1.00 38.53           C  
-ATOM    445  CG  ASN A  59     -17.865  81.984  48.101  1.00 44.80           C  
-ATOM    446  OD1 ASN A  59     -17.021  82.709  47.573  1.00 46.59           O  
-ATOM    447  ND2 ASN A  59     -18.290  82.164  49.353  1.00 53.87           N  
-ATOM    448  N   ALA A  60     -15.108  80.126  46.327  1.00 34.69           N  
-ATOM    449  CA  ALA A  60     -13.812  79.671  46.817  1.00 30.56           C  
-ATOM    450  C   ALA A  60     -12.999  80.837  47.368  1.00 30.58           C  
-ATOM    451  O   ALA A  60     -11.845  81.045  46.983  1.00 30.49           O  
-ATOM    452  CB  ALA A  60     -13.047  78.969  45.702  1.00 24.73           C  
-ATOM    453  N   SER A  61     -13.612  81.597  48.267  1.00 30.39           N  
-ATOM    454  CA  SER A  61     -12.955  82.746  48.871  1.00 33.24           C  
-ATOM    455  C   SER A  61     -12.457  82.448  50.281  1.00 33.05           C  
-ATOM    456  O   SER A  61     -11.553  83.121  50.776  1.00 28.84           O  
-ATOM    457  CB  SER A  61     -13.912  83.935  48.897  1.00 33.92           C  
-ATOM    458  OG  SER A  61     -15.120  83.583  49.546  1.00 42.39           O  
-ATOM    459  N   THR A  62     -13.058  81.451  50.928  1.00 33.36           N  
-ATOM    460  CA  THR A  62     -12.669  81.082  52.287  1.00 37.42           C  
-ATOM    461  C   THR A  62     -12.086  79.671  52.403  1.00 36.17           C  
-ATOM    462  O   THR A  62     -12.344  78.806  51.562  1.00 36.92           O  
-ATOM    463  CB  THR A  62     -13.856  81.217  53.270  1.00 37.22           C  
-ATOM    464  OG1 THR A  62     -14.958  80.420  52.817  1.00 42.94           O  
-ATOM    465  CG2 THR A  62     -14.296  82.664  53.378  1.00 41.94           C  
-ATOM    466  N   TYR A  63     -11.282  79.461  53.444  1.00 30.37           N  
-ATOM    467  CA  TYR A  63     -10.659  78.166  53.709  1.00 27.27           C  
-ATOM    468  C   TYR A  63     -11.699  77.088  53.997  1.00 28.25           C  
-ATOM    469  O   TYR A  63     -12.756  77.362  54.566  1.00 36.13           O  
-ATOM    470  CB  TYR A  63      -9.719  78.268  54.910  1.00 26.36           C  
-ATOM    471  CG  TYR A  63      -8.272  78.533  54.578  1.00 23.04           C  
-ATOM    472  CD1 TYR A  63      -7.696  78.028  53.413  1.00 24.07           C  
-ATOM    473  CD2 TYR A  63      -7.461  79.251  55.457  1.00 28.16           C  
-ATOM    474  CE1 TYR A  63      -6.342  78.228  53.136  1.00 26.88           C  
-ATOM    475  CE2 TYR A  63      -6.109  79.458  55.189  1.00 25.08           C  
-ATOM    476  CZ  TYR A  63      -5.555  78.943  54.030  1.00 24.44           C  
-ATOM    477  OH  TYR A  63      -4.216  79.129  53.771  1.00 30.49           O  
-ATOM    478  N   PRO A  64     -11.403  75.836  53.615  1.00 24.47           N  
-ATOM    479  CA  PRO A  64     -12.331  74.730  53.847  1.00 24.90           C  
-ATOM    480  C   PRO A  64     -12.237  74.196  55.273  1.00 28.89           C  
-ATOM    481  O   PRO A  64     -11.477  74.711  56.095  1.00 29.48           O  
-ATOM    482  CB  PRO A  64     -11.847  73.687  52.845  1.00 21.94           C  
-ATOM    483  CG  PRO A  64     -10.371  73.874  52.886  1.00 16.60           C  
-ATOM    484  CD  PRO A  64     -10.238  75.384  52.832  1.00 24.02           C  
-ATOM    485  N   ASN A  65     -13.032  73.170  55.557  1.00 28.35           N  
-ATOM    486  CA  ASN A  65     -13.033  72.525  56.862  1.00 28.45           C  
-ATOM    487  C   ASN A  65     -11.823  71.601  56.929  1.00 30.42           C  
-ATOM    488  O   ASN A  65     -11.344  71.114  55.903  1.00 29.43           O  
-ATOM    489  CB  ASN A  65     -14.299  71.679  57.055  1.00 29.86           C  
-ATOM    490  CG  ASN A  65     -15.551  72.514  57.256  1.00 35.36           C  
-ATOM    491  OD1 ASN A  65     -16.666  72.082  56.961  1.00 39.39           O  
-ATOM    492  ND2 ASN A  65     -15.364  73.733  57.742  1.00 38.54           N  
-ATOM    493  N   ASN A  66     -11.322  71.371  58.137  1.00 28.66           N  
-ATOM    494  CA  ASN A  66     -10.188  70.479  58.327  1.00 24.29           C  
-ATOM    495  C   ASN A  66     -10.736  69.094  58.641  1.00 21.20           C  
-ATOM    496  O   ASN A  66     -11.835  68.968  59.172  1.00 24.78           O  
-ATOM    497  CB  ASN A  66      -9.297  70.978  59.468  1.00 23.71           C  
-ATOM    498  CG  ASN A  66      -8.646  72.313  59.158  1.00 29.40           C  
-ATOM    499  OD1 ASN A  66      -8.441  73.133  60.051  1.00 33.81           O  
-ATOM    500  ND2 ASN A  66      -8.308  72.535  57.888  1.00 28.08           N  
-ATOM    501  N   CYS A  67      -9.993  68.055  58.275  1.00 22.16           N  
-ATOM    502  CA  CYS A  67     -10.431  66.688  58.532  1.00 20.67           C  
-ATOM    503  C   CYS A  67     -10.445  66.379  60.026  1.00 23.35           C  
-ATOM    504  O   CYS A  67      -9.725  67.008  60.803  1.00 20.47           O  
-ATOM    505  CB  CYS A  67      -9.538  65.687  57.792  1.00 22.16           C  
-ATOM    506  SG  CYS A  67      -9.597  65.844  55.977  1.00 25.45           S  
-ATOM    507  N   GLN A  68     -11.307  65.444  60.422  1.00 22.67           N  
-ATOM    508  CA  GLN A  68     -11.422  65.034  61.817  1.00 22.44           C  
-ATOM    509  C   GLN A  68     -10.102  64.453  62.297  1.00 23.09           C  
-ATOM    510  O   GLN A  68      -9.590  63.494  61.720  1.00 19.88           O  
-ATOM    511  CB  GLN A  68     -12.541  64.004  61.985  1.00 24.12           C  
-ATOM    512  CG  GLN A  68     -13.946  64.569  61.826  1.00 28.52           C  
-ATOM    513  CD  GLN A  68     -14.422  65.395  63.019  1.00 30.01           C  
-ATOM    514  OE1 GLN A  68     -15.607  65.701  63.125  1.00 34.85           O  
-ATOM    515  NE2 GLN A  68     -13.510  65.750  63.922  1.00 34.85           N  
-ATOM    516  N   GLN A  69      -9.573  65.019  63.377  1.00 23.06           N  
-ATOM    517  CA  GLN A  69      -8.294  64.577  63.916  1.00 24.68           C  
-ATOM    518  C   GLN A  69      -8.157  64.878  65.401  1.00 22.74           C  
-ATOM    519  O   GLN A  69      -8.948  65.626  65.972  1.00 24.68           O  
-ATOM    520  CB  GLN A  69      -7.169  65.298  63.178  1.00 24.25           C  
-ATOM    521  CG  GLN A  69      -7.244  66.803  63.345  1.00 17.43           C  
-ATOM    522  CD  GLN A  69      -6.322  67.550  62.410  1.00 25.23           C  
-ATOM    523  OE1 GLN A  69      -5.166  67.817  62.738  1.00 24.71           O  
-ATOM    524  NE2 GLN A  69      -6.841  67.929  61.250  1.00 19.69           N  
-ATOM    525  N   TYR A  70      -7.129  64.293  66.008  1.00 25.60           N  
-ATOM    526  CA  TYR A  70      -6.826  64.495  67.418  1.00 26.70           C  
-ATOM    527  C   TYR A  70      -6.290  65.917  67.560  1.00 28.42           C  
-ATOM    528  O   TYR A  70      -5.520  66.383  66.717  1.00 26.81           O  
-ATOM    529  CB  TYR A  70      -5.777  63.472  67.861  1.00 25.65           C  
-ATOM    530  CG  TYR A  70      -5.131  63.739  69.203  1.00 29.73           C  
-ATOM    531  CD1 TYR A  70      -5.725  63.302  70.387  1.00 31.34           C  
-ATOM    532  CD2 TYR A  70      -3.894  64.382  69.284  1.00 29.40           C  
-ATOM    533  CE1 TYR A  70      -5.101  63.492  71.619  1.00 30.74           C  
-ATOM    534  CE2 TYR A  70      -3.261  64.576  70.508  1.00 33.41           C  
-ATOM    535  CZ  TYR A  70      -3.868  64.127  71.669  1.00 38.10           C  
-ATOM    536  OH  TYR A  70      -3.226  64.295  72.871  1.00 42.40           O  
-ATOM    537  N   VAL A  71      -6.731  66.616  68.599  1.00 26.56           N  
-ATOM    538  CA  VAL A  71      -6.293  67.986  68.832  1.00 24.15           C  
-ATOM    539  C   VAL A  71      -5.331  68.073  70.014  1.00 28.73           C  
-ATOM    540  O   VAL A  71      -5.621  67.580  71.108  1.00 29.93           O  
-ATOM    541  CB  VAL A  71      -7.497  68.932  69.058  1.00 23.86           C  
-ATOM    542  CG1 VAL A  71      -7.016  70.347  69.326  1.00 17.46           C  
-ATOM    543  CG2 VAL A  71      -8.420  68.909  67.844  1.00 18.19           C  
-ATOM    544  N   ASP A  72      -4.176  68.684  69.766  1.00 29.24           N  
-ATOM    545  CA  ASP A  72      -3.139  68.862  70.777  1.00 26.50           C  
-ATOM    546  C   ASP A  72      -3.611  69.862  71.829  1.00 33.60           C  
-ATOM    547  O   ASP A  72      -3.873  71.022  71.523  1.00 34.30           O  
-ATOM    548  CB  ASP A  72      -1.860  69.381  70.110  1.00 24.64           C  
-ATOM    549  CG  ASP A  72      -0.650  69.363  71.035  1.00 24.68           C  
-ATOM    550  OD1 ASP A  72      -0.737  69.843  72.184  1.00 27.15           O  
-ATOM    551  OD2 ASP A  72       0.413  68.884  70.596  1.00 27.37           O  
-ATOM    552  N   GLU A  73      -3.718  69.401  73.069  1.00 38.88           N  
-ATOM    553  CA  GLU A  73      -4.138  70.253  74.176  1.00 40.37           C  
-ATOM    554  C   GLU A  73      -3.142  70.158  75.333  1.00 40.56           C  
-ATOM    555  O   GLU A  73      -3.479  70.452  76.479  1.00 40.62           O  
-ATOM    556  CB  GLU A  73      -5.537  69.863  74.658  1.00 39.68           C  
-ATOM    557  CG  GLU A  73      -6.656  70.166  73.673  1.00 47.44           C  
-ATOM    558  CD  GLU A  73      -8.030  69.840  74.232  1.00 54.00           C  
-ATOM    559  OE1 GLU A  73      -8.238  68.698  74.693  1.00 56.31           O  
-ATOM    560  OE2 GLU A  73      -8.906  70.729  74.215  1.00 63.89           O  
-ATOM    561  N   GLN A  74      -1.908  69.772  75.022  1.00 37.22           N  
-ATOM    562  CA  GLN A  74      -0.874  69.635  76.038  1.00 32.62           C  
-ATOM    563  C   GLN A  74      -0.385  70.957  76.614  1.00 29.56           C  
-ATOM    564  O   GLN A  74      -0.075  71.041  77.801  1.00 33.75           O  
-ATOM    565  CB  GLN A  74       0.300  68.824  75.495  1.00 27.31           C  
-ATOM    566  CG  GLN A  74      -0.059  67.382  75.200  1.00 41.68           C  
-ATOM    567  CD  GLN A  74      -0.640  66.668  76.408  1.00 52.56           C  
-ATOM    568  OE1 GLN A  74       0.089  66.272  77.317  1.00 61.00           O  
-ATOM    569  NE2 GLN A  74      -1.961  66.508  76.428  1.00 49.43           N  
-ATOM    570  N   PHE A  75      -0.312  71.985  75.774  1.00 26.31           N  
-ATOM    571  CA  PHE A  75       0.141  73.307  76.211  1.00 27.66           C  
-ATOM    572  C   PHE A  75      -0.816  74.373  75.682  1.00 28.07           C  
-ATOM    573  O   PHE A  75      -0.517  75.057  74.704  1.00 27.63           O  
-ATOM    574  CB  PHE A  75       1.562  73.590  75.702  1.00 18.10           C  
-ATOM    575  CG  PHE A  75       2.530  72.473  75.957  1.00 18.09           C  
-ATOM    576  CD1 PHE A  75       3.061  72.270  77.224  1.00 15.42           C  
-ATOM    577  CD2 PHE A  75       2.893  71.605  74.931  1.00 16.54           C  
-ATOM    578  CE1 PHE A  75       3.938  71.215  77.468  1.00 21.37           C  
-ATOM    579  CE2 PHE A  75       3.771  70.545  75.166  1.00 20.66           C  
-ATOM    580  CZ  PHE A  75       4.293  70.351  76.436  1.00 17.22           C  
-ATOM    581  N   PRO A  76      -1.992  74.516  76.321  1.00 35.24           N  
-ATOM    582  CA  PRO A  76      -3.011  75.495  75.926  1.00 34.48           C  
-ATOM    583  C   PRO A  76      -2.476  76.925  75.879  1.00 39.79           C  
-ATOM    584  O   PRO A  76      -1.786  77.375  76.800  1.00 40.84           O  
-ATOM    585  CB  PRO A  76      -4.071  75.329  77.012  1.00 29.40           C  
-ATOM    586  CG  PRO A  76      -3.951  73.882  77.370  1.00 30.19           C  
-ATOM    587  CD  PRO A  76      -2.460  73.720  77.468  1.00 32.66           C  
-ATOM    588  N   GLY A  77      -2.788  77.625  74.790  1.00 38.54           N  
-ATOM    589  CA  GLY A  77      -2.331  78.992  74.622  1.00 40.20           C  
-ATOM    590  C   GLY A  77      -0.943  79.088  74.013  1.00 38.24           C  
-ATOM    591  O   GLY A  77      -0.569  80.132  73.471  1.00 43.55           O  
-ATOM    592  N   PHE A  78      -0.180  77.999  74.099  1.00 29.15           N  
-ATOM    593  CA  PHE A  78       1.171  77.956  73.555  1.00 22.65           C  
-ATOM    594  C   PHE A  78       1.128  77.835  72.033  1.00 23.50           C  
-ATOM    595  O   PHE A  78       0.635  76.844  71.495  1.00 27.27           O  
-ATOM    596  CB  PHE A  78       1.946  76.789  74.170  1.00 22.84           C  
-ATOM    597  CG  PHE A  78       3.409  76.812  73.867  1.00 21.71           C  
-ATOM    598  CD1 PHE A  78       4.182  77.915  74.208  1.00 21.08           C  
-ATOM    599  CD2 PHE A  78       4.014  75.744  73.219  1.00 19.81           C  
-ATOM    600  CE1 PHE A  78       5.536  77.955  73.906  1.00 20.09           C  
-ATOM    601  CE2 PHE A  78       5.364  75.774  72.913  1.00 15.88           C  
-ATOM    602  CZ  PHE A  78       6.128  76.880  73.255  1.00 23.34           C  
-ATOM    603  N   SER A  79       1.653  78.847  71.349  1.00 26.06           N  
-ATOM    604  CA  SER A  79       1.663  78.882  69.890  1.00 25.49           C  
-ATOM    605  C   SER A  79       2.479  77.757  69.258  1.00 25.88           C  
-ATOM    606  O   SER A  79       2.116  77.248  68.200  1.00 27.58           O  
-ATOM    607  CB  SER A  79       2.186  80.234  69.400  1.00 22.86           C  
-ATOM    608  OG  SER A  79       3.521  80.450  69.825  1.00 27.53           O  
-ATOM    609  N   GLY A  80       3.571  77.369  69.915  1.00 25.57           N  
-ATOM    610  CA  GLY A  80       4.434  76.317  69.404  1.00 25.20           C  
-ATOM    611  C   GLY A  80       3.750  74.997  69.104  1.00 23.02           C  
-ATOM    612  O   GLY A  80       4.158  74.275  68.191  1.00 23.62           O  
-ATOM    613  N   SER A  81       2.705  74.688  69.864  1.00 20.17           N  
-ATOM    614  CA  SER A  81       1.968  73.446  69.682  1.00 22.23           C  
-ATOM    615  C   SER A  81       0.621  73.650  68.992  1.00 25.34           C  
-ATOM    616  O   SER A  81       0.125  72.754  68.310  1.00 23.04           O  
-ATOM    617  CB  SER A  81       1.761  72.758  71.034  1.00 23.82           C  
-ATOM    618  OG  SER A  81       1.108  73.614  71.959  1.00 13.70           O  
-ATOM    619  N   GLU A  82       0.030  74.829  69.167  1.00 28.40           N  
-ATOM    620  CA  GLU A  82      -1.267  75.123  68.565  1.00 25.01           C  
-ATOM    621  C   GLU A  82      -1.193  75.558  67.104  1.00 24.09           C  
-ATOM    622  O   GLU A  82      -2.209  75.553  66.405  1.00 24.62           O  
-ATOM    623  CB  GLU A  82      -2.019  76.164  69.393  1.00 25.91           C  
-ATOM    624  CG  GLU A  82      -2.412  75.673  70.774  1.00 31.37           C  
-ATOM    625  CD  GLU A  82      -3.261  76.672  71.534  1.00 42.10           C  
-ATOM    626  OE1 GLU A  82      -3.016  77.891  71.408  1.00 51.99           O  
-ATOM    627  OE2 GLU A  82      -4.173  76.235  72.268  1.00 43.09           O  
-ATOM    628  N   MET A  83       0.003  75.920  66.643  1.00 21.30           N  
-ATOM    629  CA  MET A  83       0.196  76.334  65.254  1.00 20.02           C  
-ATOM    630  C   MET A  83       0.031  75.135  64.310  1.00 22.19           C  
-ATOM    631  O   MET A  83      -0.076  75.295  63.087  1.00 16.97           O  
-ATOM    632  CB  MET A  83       1.581  76.959  65.067  1.00 17.65           C  
-ATOM    633  CG  MET A  83       2.740  75.994  65.240  1.00 17.33           C  
-ATOM    634  SD  MET A  83       4.357  76.762  65.008  1.00 23.36           S  
-ATOM    635  CE  MET A  83       4.561  76.584  63.263  1.00 14.76           C  
-ATOM    636  N   TRP A  84       0.030  73.938  64.893  1.00 18.27           N  
-ATOM    637  CA  TRP A  84      -0.120  72.702  64.142  1.00 18.35           C  
-ATOM    638  C   TRP A  84      -1.546  72.166  64.252  1.00 19.37           C  
-ATOM    639  O   TRP A  84      -1.942  71.281  63.494  1.00 23.73           O  
-ATOM    640  CB  TRP A  84       0.881  71.657  64.643  1.00 20.76           C  
-ATOM    641  CG  TRP A  84       2.313  72.117  64.597  1.00 21.50           C  
-ATOM    642  CD1 TRP A  84       3.105  72.450  65.665  1.00 22.33           C  
-ATOM    643  CD2 TRP A  84       3.131  72.271  63.431  1.00 20.27           C  
-ATOM    644  NE1 TRP A  84       4.364  72.797  65.231  1.00 18.82           N  
-ATOM    645  CE2 TRP A  84       4.410  72.696  63.866  1.00 21.26           C  
-ATOM    646  CE3 TRP A  84       2.910  72.091  62.057  1.00 15.77           C  
-ATOM    647  CZ2 TRP A  84       5.461  72.942  62.976  1.00 16.84           C  
-ATOM    648  CZ3 TRP A  84       3.958  72.339  61.173  1.00 15.19           C  
-ATOM    649  CH2 TRP A  84       5.216  72.759  61.638  1.00 19.00           C  
-ATOM    650  N   ASN A  85      -2.314  72.708  65.194  1.00 17.98           N  
-ATOM    651  CA  ASN A  85      -3.702  72.293  65.406  1.00 17.50           C  
-ATOM    652  C   ASN A  85      -4.615  72.860  64.332  1.00 18.73           C  
-ATOM    653  O   ASN A  85      -4.304  73.880  63.721  1.00 25.61           O  
-ATOM    654  CB  ASN A  85      -4.216  72.795  66.761  1.00 18.81           C  
-ATOM    655  CG  ASN A  85      -3.852  71.881  67.908  1.00 17.78           C  
-ATOM    656  OD1 ASN A  85      -3.588  70.696  67.721  1.00 20.32           O  
-ATOM    657  ND2 ASN A  85      -3.850  72.431  69.112  1.00 14.32           N  
-ATOM    658  N   PRO A  86      -5.766  72.207  64.097  1.00 16.51           N  
-ATOM    659  CA  PRO A  86      -6.747  72.648  63.097  1.00 17.19           C  
-ATOM    660  C   PRO A  86      -7.187  74.074  63.415  1.00 20.61           C  
-ATOM    661  O   PRO A  86      -7.594  74.354  64.544  1.00 20.35           O  
-ATOM    662  CB  PRO A  86      -7.907  71.679  63.315  1.00 13.50           C  
-ATOM    663  CG  PRO A  86      -7.231  70.440  63.768  1.00 19.03           C  
-ATOM    664  CD  PRO A  86      -6.189  70.944  64.728  1.00 16.75           C  
-ATOM    665  N   ASN A  87      -7.067  74.979  62.446  1.00 21.32           N  
-ATOM    666  CA  ASN A  87      -7.464  76.371  62.659  1.00 20.07           C  
-ATOM    667  C   ASN A  87      -8.823  76.683  62.033  1.00 24.87           C  
-ATOM    668  O   ASN A  87      -9.264  77.834  62.001  1.00 28.03           O  
-ATOM    669  CB  ASN A  87      -6.385  77.329  62.150  1.00 20.97           C  
-ATOM    670  CG  ASN A  87      -6.109  77.167  60.674  1.00 29.45           C  
-ATOM    671  OD1 ASN A  87      -6.339  76.103  60.099  1.00 33.38           O  
-ATOM    672  ND2 ASN A  87      -5.613  78.227  60.049  1.00 26.85           N  
-ATOM    673  N   ARG A  88      -9.477  75.634  61.547  1.00 23.50           N  
-ATOM    674  CA  ARG A  88     -10.798  75.733  60.944  1.00 25.05           C  
-ATOM    675  C   ARG A  88     -11.673  74.666  61.596  1.00 27.04           C  
-ATOM    676  O   ARG A  88     -11.172  73.784  62.297  1.00 31.04           O  
-ATOM    677  CB  ARG A  88     -10.724  75.506  59.430  1.00 24.92           C  
-ATOM    678  CG  ARG A  88     -10.502  76.776  58.614  1.00 26.09           C  
-ATOM    679  CD  ARG A  88     -11.722  77.684  58.721  1.00 35.43           C  
-ATOM    680  NE  ARG A  88     -11.594  78.932  57.973  1.00 39.43           N  
-ATOM    681  CZ  ARG A  88     -10.715  79.892  58.248  1.00 52.01           C  
-ATOM    682  NH1 ARG A  88      -9.859  79.762  59.255  1.00 51.57           N  
-ATOM    683  NH2 ARG A  88     -10.716  81.011  57.533  1.00 60.52           N  
-ATOM    684  N   GLU A  89     -12.980  74.758  61.393  1.00 30.13           N  
-ATOM    685  CA  GLU A  89     -13.896  73.789  61.978  1.00 29.60           C  
-ATOM    686  C   GLU A  89     -13.626  72.404  61.392  1.00 25.19           C  
-ATOM    687  O   GLU A  89     -13.346  72.276  60.200  1.00 27.46           O  
-ATOM    688  CB  GLU A  89     -15.338  74.216  61.708  1.00 39.38           C  
-ATOM    689  CG  GLU A  89     -16.376  73.435  62.484  1.00 56.57           C  
-ATOM    690  CD  GLU A  89     -17.781  73.925  62.210  1.00 66.96           C  
-ATOM    691  OE1 GLU A  89     -18.045  75.128  62.434  1.00 71.89           O  
-ATOM    692  OE2 GLU A  89     -18.618  73.108  61.766  1.00 66.96           O  
-ATOM    693  N   MET A  90     -13.651  71.378  62.237  1.00 18.35           N  
-ATOM    694  CA  MET A  90     -13.413  70.013  61.776  1.00 18.57           C  
-ATOM    695  C   MET A  90     -14.685  69.369  61.243  1.00 20.37           C  
-ATOM    696  O   MET A  90     -15.775  69.584  61.777  1.00 25.62           O  
-ATOM    697  CB  MET A  90     -12.824  69.138  62.889  1.00 21.43           C  
-ATOM    698  CG  MET A  90     -11.389  69.470  63.271  1.00 24.55           C  
-ATOM    699  SD  MET A  90     -10.672  68.229  64.370  1.00 26.45           S  
-ATOM    700  CE  MET A  90     -11.572  68.535  65.857  1.00 25.39           C  
-ATOM    701  N   SER A  91     -14.530  68.559  60.200  1.00 19.90           N  
-ATOM    702  CA  SER A  91     -15.650  67.870  59.569  1.00 21.58           C  
-ATOM    703  C   SER A  91     -15.135  66.735  58.705  1.00 23.55           C  
-ATOM    704  O   SER A  91     -13.991  66.767  58.252  1.00 22.29           O  
-ATOM    705  CB  SER A  91     -16.441  68.843  58.689  1.00 24.37           C  
-ATOM    706  OG  SER A  91     -17.459  68.177  57.962  1.00 24.38           O  
-ATOM    707  N   GLU A  92     -15.972  65.724  58.490  1.00 24.45           N  
-ATOM    708  CA  GLU A  92     -15.589  64.602  57.640  1.00 24.56           C  
-ATOM    709  C   GLU A  92     -15.629  65.047  56.181  1.00 26.97           C  
-ATOM    710  O   GLU A  92     -15.027  64.414  55.316  1.00 29.36           O  
-ATOM    711  CB  GLU A  92     -16.492  63.398  57.872  1.00 25.15           C  
-ATOM    712  CG  GLU A  92     -16.172  62.662  59.152  1.00 23.88           C  
-ATOM    713  CD  GLU A  92     -16.930  61.369  59.266  1.00 29.94           C  
-ATOM    714  OE1 GLU A  92     -16.430  60.345  58.772  1.00 28.22           O  
-ATOM    715  OE2 GLU A  92     -18.028  61.369  59.849  1.00 27.06           O  
-ATOM    716  N   ASP A  93     -16.375  66.120  55.917  1.00 27.99           N  
-ATOM    717  CA  ASP A  93     -16.464  66.711  54.586  1.00 26.49           C  
-ATOM    718  C   ASP A  93     -15.275  67.671  54.591  1.00 26.72           C  
-ATOM    719  O   ASP A  93     -15.417  68.856  54.914  1.00 29.13           O  
-ATOM    720  CB  ASP A  93     -17.783  67.480  54.437  1.00 29.31           C  
-ATOM    721  CG  ASP A  93     -17.888  68.236  53.117  1.00 29.45           C  
-ATOM    722  OD1 ASP A  93     -17.140  67.920  52.169  1.00 38.28           O  
-ATOM    723  OD2 ASP A  93     -18.727  69.155  53.027  1.00 39.36           O  
-ATOM    724  N   CYS A  94     -14.101  67.142  54.257  1.00 27.22           N  
-ATOM    725  CA  CYS A  94     -12.873  67.927  54.285  1.00 29.42           C  
-ATOM    726  C   CYS A  94     -11.979  67.806  53.054  1.00 29.72           C  
-ATOM    727  O   CYS A  94     -10.925  68.443  52.987  1.00 33.70           O  
-ATOM    728  CB  CYS A  94     -12.068  67.534  55.523  1.00 22.91           C  
-ATOM    729  SG  CYS A  94     -11.583  65.774  55.568  1.00 23.92           S  
-ATOM    730  N   LEU A  95     -12.388  66.994  52.086  1.00 23.90           N  
-ATOM    731  CA  LEU A  95     -11.593  66.804  50.877  1.00 24.06           C  
-ATOM    732  C   LEU A  95     -11.635  67.985  49.911  1.00 21.32           C  
-ATOM    733  O   LEU A  95     -12.377  67.985  48.925  1.00 19.26           O  
-ATOM    734  CB  LEU A  95     -11.981  65.493  50.193  1.00 17.18           C  
-ATOM    735  CG  LEU A  95     -11.701  64.299  51.115  1.00 21.93           C  
-ATOM    736  CD1 LEU A  95     -12.056  62.983  50.432  1.00 19.12           C  
-ATOM    737  CD2 LEU A  95     -10.231  64.317  51.537  1.00 10.36           C  
-ATOM    738  N   TYR A  96     -10.810  68.987  50.212  1.00 17.14           N  
-ATOM    739  CA  TYR A  96     -10.715  70.203  49.412  1.00 16.77           C  
-ATOM    740  C   TYR A  96      -9.259  70.585  49.159  1.00 15.75           C  
-ATOM    741  O   TYR A  96      -8.348  70.055  49.792  1.00 14.55           O  
-ATOM    742  CB  TYR A  96     -11.421  71.356  50.132  1.00 19.55           C  
-ATOM    743  CG  TYR A  96     -12.899  71.125  50.361  1.00 23.21           C  
-ATOM    744  CD1 TYR A  96     -13.347  70.377  51.445  1.00 17.02           C  
-ATOM    745  CD2 TYR A  96     -13.848  71.630  49.476  1.00 24.54           C  
-ATOM    746  CE1 TYR A  96     -14.704  70.134  51.639  1.00 28.08           C  
-ATOM    747  CE2 TYR A  96     -15.205  71.395  49.659  1.00 23.51           C  
-ATOM    748  CZ  TYR A  96     -15.627  70.644  50.739  1.00 24.21           C  
-ATOM    749  OH  TYR A  96     -16.968  70.398  50.911  1.00 26.91           O  
-ATOM    750  N   LEU A  97      -9.041  71.497  48.219  1.00 19.16           N  
-ATOM    751  CA  LEU A  97      -7.691  71.957  47.911  1.00 19.13           C  
-ATOM    752  C   LEU A  97      -7.649  73.475  47.749  1.00 16.01           C  
-ATOM    753  O   LEU A  97      -8.655  74.105  47.430  1.00 19.59           O  
-ATOM    754  CB  LEU A  97      -7.124  71.230  46.684  1.00 18.22           C  
-ATOM    755  CG  LEU A  97      -7.819  71.236  45.324  1.00 21.10           C  
-ATOM    756  CD1 LEU A  97      -7.489  72.510  44.568  1.00 25.46           C  
-ATOM    757  CD2 LEU A  97      -7.334  70.035  44.529  1.00 23.76           C  
-ATOM    758  N   ASN A  98      -6.489  74.059  48.025  1.00 16.50           N  
-ATOM    759  CA  ASN A  98      -6.302  75.503  47.943  1.00 19.00           C  
-ATOM    760  C   ASN A  98      -5.242  75.843  46.897  1.00 20.75           C  
-ATOM    761  O   ASN A  98      -4.204  75.192  46.824  1.00 22.28           O  
-ATOM    762  CB  ASN A  98      -5.884  76.041  49.316  1.00 21.54           C  
-ATOM    763  CG  ASN A  98      -6.698  75.433  50.456  1.00 22.55           C  
-ATOM    764  OD1 ASN A  98      -7.889  75.705  50.597  1.00 22.66           O  
-ATOM    765  ND2 ASN A  98      -6.057  74.589  51.258  1.00 18.79           N  
-ATOM    766  N   ILE A  99      -5.501  76.874  46.097  1.00 20.64           N  
-ATOM    767  CA  ILE A  99      -4.572  77.274  45.043  1.00 22.55           C  
-ATOM    768  C   ILE A  99      -4.237  78.762  45.098  1.00 22.29           C  
-ATOM    769  O   ILE A  99      -5.130  79.601  45.168  1.00 21.92           O  
-ATOM    770  CB  ILE A  99      -5.157  76.990  43.634  1.00 21.94           C  
-ATOM    771  CG1 ILE A  99      -5.779  75.594  43.572  1.00 24.44           C  
-ATOM    772  CG2 ILE A  99      -4.064  77.112  42.580  1.00 20.24           C  
-ATOM    773  CD1 ILE A  99      -6.478  75.292  42.259  1.00 21.15           C  
-ATOM    774  N   TRP A 100      -2.947  79.080  45.060  1.00 24.47           N  
-ATOM    775  CA  TRP A 100      -2.485  80.465  45.068  1.00 27.32           C  
-ATOM    776  C   TRP A 100      -1.902  80.742  43.693  1.00 29.03           C  
-ATOM    777  O   TRP A 100      -0.928  80.110  43.281  1.00 31.55           O  
-ATOM    778  CB  TRP A 100      -1.436  80.700  46.158  1.00 26.38           C  
-ATOM    779  CG  TRP A 100      -2.025  80.825  47.531  1.00 28.86           C  
-ATOM    780  CD1 TRP A 100      -2.463  81.972  48.136  1.00 26.49           C  
-ATOM    781  CD2 TRP A 100      -2.239  79.768  48.472  1.00 27.08           C  
-ATOM    782  NE1 TRP A 100      -2.936  81.692  49.396  1.00 22.75           N  
-ATOM    783  CE2 TRP A 100      -2.811  80.347  49.629  1.00 28.41           C  
-ATOM    784  CE3 TRP A 100      -2.003  78.387  48.453  1.00 29.50           C  
-ATOM    785  CZ2 TRP A 100      -3.152  79.591  50.756  1.00 30.23           C  
-ATOM    786  CZ3 TRP A 100      -2.341  77.635  49.575  1.00 34.38           C  
-ATOM    787  CH2 TRP A 100      -2.910  78.241  50.710  1.00 32.16           C  
-ATOM    788  N   VAL A 101      -2.539  81.659  42.971  1.00 28.32           N  
-ATOM    789  CA  VAL A 101      -2.125  82.022  41.621  1.00 26.65           C  
-ATOM    790  C   VAL A 101      -1.575  83.443  41.564  1.00 29.66           C  
-ATOM    791  O   VAL A 101      -2.249  84.391  41.969  1.00 31.13           O  
-ATOM    792  CB  VAL A 101      -3.322  81.916  40.638  1.00 24.56           C  
-ATOM    793  CG1 VAL A 101      -2.892  82.260  39.222  1.00 17.47           C  
-ATOM    794  CG2 VAL A 101      -3.926  80.526  40.686  1.00 21.15           C  
-ATOM    795  N   PRO A 102      -0.329  83.606  41.081  1.00 30.13           N  
-ATOM    796  CA  PRO A 102       0.265  84.945  40.987  1.00 35.91           C  
-ATOM    797  C   PRO A 102      -0.522  85.831  40.014  1.00 35.55           C  
-ATOM    798  O   PRO A 102      -1.199  85.328  39.116  1.00 32.40           O  
-ATOM    799  CB  PRO A 102       1.691  84.658  40.505  1.00 28.74           C  
-ATOM    800  CG  PRO A 102       1.573  83.350  39.801  1.00 28.31           C  
-ATOM    801  CD  PRO A 102       0.640  82.573  40.686  1.00 26.38           C  
-ATOM    802  N   SER A 103      -0.459  87.143  40.223  1.00 39.90           N  
-ATOM    803  CA  SER A 103      -1.185  88.098  39.387  1.00 38.08           C  
-ATOM    804  C   SER A 103      -0.231  89.029  38.628  1.00 36.63           C  
-ATOM    805  O   SER A 103       0.696  89.588  39.215  1.00 39.16           O  
-ATOM    806  CB  SER A 103      -2.158  88.907  40.251  1.00 37.07           C  
-ATOM    807  OG  SER A 103      -2.955  89.775  39.466  1.00 43.57           O  
-ATOM    808  N   PRO A 104      -0.459  89.217  37.315  1.00 38.02           N  
-ATOM    809  CA  PRO A 104      -1.523  88.630  36.488  1.00 35.11           C  
-ATOM    810  C   PRO A 104      -1.418  87.108  36.345  1.00 33.70           C  
-ATOM    811  O   PRO A 104      -0.327  86.543  36.458  1.00 26.25           O  
-ATOM    812  CB  PRO A 104      -1.324  89.316  35.132  1.00 36.36           C  
-ATOM    813  CG  PRO A 104      -0.613  90.597  35.478  1.00 40.88           C  
-ATOM    814  CD  PRO A 104       0.368  90.134  36.507  1.00 33.99           C  
-ATOM    815  N   ARG A 105      -2.550  86.459  36.080  1.00 31.76           N  
-ATOM    816  CA  ARG A 105      -2.589  85.007  35.918  1.00 33.30           C  
-ATOM    817  C   ARG A 105      -1.611  84.570  34.829  1.00 38.54           C  
-ATOM    818  O   ARG A 105      -1.675  85.059  33.697  1.00 46.17           O  
-ATOM    819  CB  ARG A 105      -4.006  84.547  35.554  1.00 25.80           C  
-ATOM    820  CG  ARG A 105      -4.169  83.034  35.487  1.00 25.67           C  
-ATOM    821  CD  ARG A 105      -5.487  82.626  34.846  1.00 19.89           C  
-ATOM    822  NE  ARG A 105      -6.652  83.122  35.571  1.00 24.93           N  
-ATOM    823  CZ  ARG A 105      -7.903  83.027  35.127  1.00 32.65           C  
-ATOM    824  NH1 ARG A 105      -8.155  82.456  33.956  1.00 38.14           N  
-ATOM    825  NH2 ARG A 105      -8.907  83.497  35.850  1.00 29.71           N  
-ATOM    826  N   PRO A 106      -0.669  83.669  35.169  1.00 41.47           N  
-ATOM    827  CA  PRO A 106       0.317  83.184  34.194  1.00 36.49           C  
-ATOM    828  C   PRO A 106      -0.333  82.292  33.140  1.00 32.77           C  
-ATOM    829  O   PRO A 106      -1.528  81.988  33.220  1.00 29.49           O  
-ATOM    830  CB  PRO A 106       1.305  82.411  35.068  1.00 30.90           C  
-ATOM    831  CG  PRO A 106       0.428  81.871  36.155  1.00 35.39           C  
-ATOM    832  CD  PRO A 106      -0.444  83.056  36.491  1.00 38.08           C  
-ATOM    833  N   LYS A 107       0.447  81.898  32.139  1.00 33.26           N  
-ATOM    834  CA  LYS A 107      -0.068  81.050  31.069  1.00 33.82           C  
-ATOM    835  C   LYS A 107       0.315  79.588  31.277  1.00 30.95           C  
-ATOM    836  O   LYS A 107      -0.505  78.691  31.089  1.00 27.31           O  
-ATOM    837  CB  LYS A 107       0.434  81.543  29.705  1.00 36.34           C  
-ATOM    838  CG  LYS A 107       0.165  83.021  29.436  1.00 37.75           C  
-ATOM    839  CD  LYS A 107      -1.321  83.346  29.531  1.00 41.34           C  
-ATOM    840  CE  LYS A 107      -1.574  84.837  29.386  1.00 38.19           C  
-ATOM    841  NZ  LYS A 107      -3.017  85.171  29.526  1.00 39.05           N  
-ATOM    842  N   SER A 108       1.565  79.355  31.667  1.00 28.53           N  
-ATOM    843  CA  SER A 108       2.049  78.003  31.903  1.00 30.66           C  
-ATOM    844  C   SER A 108       3.315  78.041  32.748  1.00 33.72           C  
-ATOM    845  O   SER A 108       4.434  77.972  32.223  1.00 36.65           O  
-ATOM    846  CB  SER A 108       2.321  77.299  30.572  1.00 33.26           C  
-ATOM    847  OG  SER A 108       2.607  75.924  30.758  1.00 36.34           O  
-ATOM    848  N   THR A 109       3.133  78.161  34.060  1.00 27.16           N  
-ATOM    849  CA  THR A 109       4.265  78.211  34.977  1.00 32.90           C  
-ATOM    850  C   THR A 109       4.321  76.990  35.900  1.00 32.83           C  
-ATOM    851  O   THR A 109       3.363  76.215  35.988  1.00 29.54           O  
-ATOM    852  CB  THR A 109       4.257  79.513  35.818  1.00 29.12           C  
-ATOM    853  OG1 THR A 109       5.508  79.650  36.509  1.00 33.63           O  
-ATOM    854  CG2 THR A 109       3.121  79.493  36.828  1.00 20.30           C  
-ATOM    855  N   THR A 110       5.451  76.834  36.585  1.00 27.27           N  
-ATOM    856  CA  THR A 110       5.672  75.719  37.499  1.00 23.35           C  
-ATOM    857  C   THR A 110       4.616  75.587  38.596  1.00 24.73           C  
-ATOM    858  O   THR A 110       4.168  76.577  39.179  1.00 22.86           O  
-ATOM    859  CB  THR A 110       7.060  75.818  38.138  1.00 19.38           C  
-ATOM    860  OG1 THR A 110       8.045  75.944  37.105  1.00 25.05           O  
-ATOM    861  CG2 THR A 110       7.353  74.586  38.971  1.00 20.67           C  
-ATOM    862  N   VAL A 111       4.238  74.343  38.874  1.00 22.87           N  
-ATOM    863  CA  VAL A 111       3.236  74.030  39.883  1.00 19.15           C  
-ATOM    864  C   VAL A 111       3.848  73.216  41.023  1.00 24.02           C  
-ATOM    865  O   VAL A 111       4.685  72.342  40.791  1.00 23.06           O  
-ATOM    866  CB  VAL A 111       2.073  73.232  39.258  1.00  9.88           C  
-ATOM    867  CG1 VAL A 111       1.040  72.873  40.313  1.00 21.52           C  
-ATOM    868  CG2 VAL A 111       1.432  74.039  38.151  1.00 10.49           C  
-ATOM    869  N   MET A 112       3.446  73.532  42.253  1.00 21.55           N  
-ATOM    870  CA  MET A 112       3.930  72.828  43.439  1.00 17.45           C  
-ATOM    871  C   MET A 112       2.740  72.437  44.305  1.00 19.77           C  
-ATOM    872  O   MET A 112       1.921  73.282  44.662  1.00 25.21           O  
-ATOM    873  CB  MET A 112       4.891  73.706  44.246  1.00 16.85           C  
-ATOM    874  CG  MET A 112       6.230  73.986  43.565  1.00 13.23           C  
-ATOM    875  SD  MET A 112       7.311  75.072  44.543  1.00 21.13           S  
-ATOM    876  CE  MET A 112       8.163  73.882  45.581  1.00 18.74           C  
-ATOM    877  N   VAL A 113       2.627  71.148  44.610  1.00 22.35           N  
-ATOM    878  CA  VAL A 113       1.534  70.649  45.435  1.00 17.63           C  
-ATOM    879  C   VAL A 113       2.050  70.230  46.808  1.00 21.72           C  
-ATOM    880  O   VAL A 113       2.853  69.305  46.928  1.00 16.96           O  
-ATOM    881  CB  VAL A 113       0.812  69.457  44.767  1.00 13.56           C  
-ATOM    882  CG1 VAL A 113      -0.404  69.057  45.585  1.00 14.73           C  
-ATOM    883  CG2 VAL A 113       0.395  69.821  43.351  1.00  8.49           C  
-ATOM    884  N   TRP A 114       1.606  70.952  47.832  1.00 21.75           N  
-ATOM    885  CA  TRP A 114       1.983  70.693  49.213  1.00 16.57           C  
-ATOM    886  C   TRP A 114       1.127  69.600  49.848  1.00 17.93           C  
-ATOM    887  O   TRP A 114      -0.099  69.593  49.708  1.00 17.97           O  
-ATOM    888  CB  TRP A 114       1.868  71.982  50.034  1.00 13.68           C  
-ATOM    889  CG  TRP A 114       2.113  71.785  51.506  1.00 18.76           C  
-ATOM    890  CD1 TRP A 114       1.188  71.865  52.515  1.00 17.25           C  
-ATOM    891  CD2 TRP A 114       3.360  71.461  52.131  1.00 14.28           C  
-ATOM    892  NE1 TRP A 114       1.784  71.607  53.726  1.00 12.67           N  
-ATOM    893  CE2 TRP A 114       3.115  71.357  53.522  1.00 14.87           C  
-ATOM    894  CE3 TRP A 114       4.661  71.252  51.652  1.00  2.55           C  
-ATOM    895  CZ2 TRP A 114       4.124  71.051  54.440  1.00 12.29           C  
-ATOM    896  CZ3 TRP A 114       5.665  70.949  52.562  1.00  7.22           C  
-ATOM    897  CH2 TRP A 114       5.390  70.853  53.944  1.00 15.81           C  
-ATOM    898  N   ILE A 115       1.790  68.680  50.542  1.00 20.36           N  
-ATOM    899  CA  ILE A 115       1.121  67.585  51.240  1.00 16.82           C  
-ATOM    900  C   ILE A 115       1.547  67.680  52.707  1.00 16.83           C  
-ATOM    901  O   ILE A 115       2.688  67.378  53.051  1.00 13.54           O  
-ATOM    902  CB  ILE A 115       1.524  66.205  50.663  1.00 19.06           C  
-ATOM    903  CG1 ILE A 115       1.179  66.138  49.170  1.00 20.40           C  
-ATOM    904  CG2 ILE A 115       0.812  65.088  51.423  1.00 12.74           C  
-ATOM    905  CD1 ILE A 115       1.577  64.841  48.497  1.00 14.82           C  
-ATOM    906  N   TYR A 116       0.629  68.121  53.561  1.00 15.45           N  
-ATOM    907  CA  TYR A 116       0.915  68.288  54.981  1.00 14.35           C  
-ATOM    908  C   TYR A 116       1.272  67.020  55.756  1.00 15.96           C  
-ATOM    909  O   TYR A 116       0.896  65.910  55.375  1.00 16.77           O  
-ATOM    910  CB  TYR A 116      -0.237  69.031  55.679  1.00 13.65           C  
-ATOM    911  CG  TYR A 116      -1.587  68.336  55.647  1.00 15.40           C  
-ATOM    912  CD1 TYR A 116      -1.814  67.160  56.368  1.00 20.00           C  
-ATOM    913  CD2 TYR A 116      -2.647  68.870  54.922  1.00 10.73           C  
-ATOM    914  CE1 TYR A 116      -3.064  66.537  56.365  1.00 12.01           C  
-ATOM    915  CE2 TYR A 116      -3.902  68.255  54.913  1.00 11.42           C  
-ATOM    916  CZ  TYR A 116      -4.101  67.092  55.635  1.00 14.30           C  
-ATOM    917  OH  TYR A 116      -5.334  66.485  55.620  1.00 16.91           O  
-ATOM    918  N   GLY A 117       2.011  67.209  56.848  1.00 18.69           N  
-ATOM    919  CA  GLY A 117       2.410  66.100  57.699  1.00 15.85           C  
-ATOM    920  C   GLY A 117       1.487  65.945  58.900  1.00 17.16           C  
-ATOM    921  O   GLY A 117       0.373  66.473  58.908  1.00 13.27           O  
-ATOM    922  N   GLY A 118       1.942  65.212  59.912  1.00 13.75           N  
-ATOM    923  CA  GLY A 118       1.128  65.007  61.098  1.00 11.83           C  
-ATOM    924  C   GLY A 118       0.932  63.547  61.472  1.00 15.63           C  
-ATOM    925  O   GLY A 118      -0.115  63.177  62.010  1.00 17.41           O  
-ATOM    926  N   GLY A 119       1.913  62.713  61.129  1.00 11.30           N  
-ATOM    927  CA  GLY A 119       1.873  61.295  61.449  1.00 10.73           C  
-ATOM    928  C   GLY A 119       0.694  60.498  60.927  1.00 14.12           C  
-ATOM    929  O   GLY A 119       0.388  59.434  61.461  1.00 20.42           O  
-ATOM    930  N   PHE A 120       0.047  61.005  59.881  1.00 16.52           N  
-ATOM    931  CA  PHE A 120      -1.115  60.359  59.264  1.00 15.45           C  
-ATOM    932  C   PHE A 120      -2.350  60.341  60.158  1.00 19.75           C  
-ATOM    933  O   PHE A 120      -3.383  59.792  59.770  1.00 22.06           O  
-ATOM    934  CB  PHE A 120      -0.793  58.930  58.802  1.00 11.75           C  
-ATOM    935  CG  PHE A 120       0.262  58.854  57.733  1.00 10.69           C  
-ATOM    936  CD1 PHE A 120      -0.018  59.251  56.430  1.00  6.65           C  
-ATOM    937  CD2 PHE A 120       1.537  58.377  58.029  1.00 11.00           C  
-ATOM    938  CE1 PHE A 120       0.957  59.174  55.434  1.00  9.71           C  
-ATOM    939  CE2 PHE A 120       2.520  58.296  57.040  1.00  9.46           C  
-ATOM    940  CZ  PHE A 120       2.227  58.696  55.742  1.00 12.95           C  
-ATOM    941  N   TYR A 121      -2.241  60.928  61.351  1.00 18.85           N  
-ATOM    942  CA  TYR A 121      -3.362  60.985  62.293  1.00 18.91           C  
-ATOM    943  C   TYR A 121      -3.864  62.423  62.443  1.00 19.80           C  
-ATOM    944  O   TYR A 121      -4.841  62.682  63.150  1.00 18.02           O  
-ATOM    945  CB  TYR A 121      -2.948  60.436  63.671  1.00 16.47           C  
-ATOM    946  CG  TYR A 121      -2.050  61.359  64.470  1.00 16.74           C  
-ATOM    947  CD1 TYR A 121      -2.589  62.341  65.307  1.00 18.93           C  
-ATOM    948  CD2 TYR A 121      -0.664  61.277  64.363  1.00 18.12           C  
-ATOM    949  CE1 TYR A 121      -1.764  63.226  66.013  1.00 12.92           C  
-ATOM    950  CE2 TYR A 121       0.169  62.150  65.061  1.00 11.04           C  
-ATOM    951  CZ  TYR A 121      -0.384  63.123  65.883  1.00 19.23           C  
-ATOM    952  OH  TYR A 121       0.451  63.985  66.564  1.00 16.41           O  
-ATOM    953  N   SER A 122      -3.176  63.356  61.793  1.00 19.76           N  
-ATOM    954  CA  SER A 122      -3.545  64.762  61.865  1.00 16.55           C  
-ATOM    955  C   SER A 122      -2.905  65.590  60.761  1.00 20.21           C  
-ATOM    956  O   SER A 122      -2.120  65.085  59.953  1.00 16.82           O  
-ATOM    957  CB  SER A 122      -3.137  65.342  63.218  1.00 18.39           C  
-ATOM    958  OG  SER A 122      -1.732  65.305  63.368  1.00 14.15           O  
-ATOM    959  N   GLY A 123      -3.233  66.879  60.762  1.00 20.10           N  
-ATOM    960  CA  GLY A 123      -2.708  67.799  59.772  1.00 24.15           C  
-ATOM    961  C   GLY A 123      -3.811  68.606  59.112  1.00 25.62           C  
-ATOM    962  O   GLY A 123      -4.956  68.161  59.037  1.00 23.29           O  
-ATOM    963  N   SER A 124      -3.464  69.798  58.635  1.00 23.40           N  
-ATOM    964  CA  SER A 124      -4.419  70.675  57.967  1.00 17.75           C  
-ATOM    965  C   SER A 124      -3.693  71.502  56.916  1.00 21.23           C  
-ATOM    966  O   SER A 124      -2.558  71.923  57.132  1.00 23.70           O  
-ATOM    967  CB  SER A 124      -5.096  71.607  58.976  1.00 17.17           C  
-ATOM    968  OG  SER A 124      -5.802  70.873  59.962  1.00 23.97           O  
-ATOM    969  N   SER A 125      -4.336  71.706  55.769  1.00 22.39           N  
-ATOM    970  CA  SER A 125      -3.747  72.493  54.685  1.00 26.61           C  
-ATOM    971  C   SER A 125      -3.979  73.988  54.883  1.00 29.60           C  
-ATOM    972  O   SER A 125      -3.413  74.817  54.168  1.00 31.47           O  
-ATOM    973  CB  SER A 125      -4.346  72.073  53.344  1.00 29.82           C  
-ATOM    974  OG  SER A 125      -5.727  72.385  53.279  1.00 26.15           O  
-ATOM    975  N   THR A 126      -4.808  74.321  55.868  1.00 28.99           N  
-ATOM    976  CA  THR A 126      -5.159  75.702  56.161  1.00 22.80           C  
-ATOM    977  C   THR A 126      -4.289  76.401  57.211  1.00 22.44           C  
-ATOM    978  O   THR A 126      -4.545  77.555  57.553  1.00 22.53           O  
-ATOM    979  CB  THR A 126      -6.633  75.788  56.589  1.00 20.08           C  
-ATOM    980  OG1 THR A 126      -6.813  75.052  57.802  1.00 21.01           O  
-ATOM    981  CG2 THR A 126      -7.537  75.189  55.514  1.00 16.02           C  
-ATOM    982  N   LEU A 127      -3.258  75.719  57.708  1.00 21.64           N  
-ATOM    983  CA  LEU A 127      -2.371  76.299  58.721  1.00 21.62           C  
-ATOM    984  C   LEU A 127      -1.641  77.541  58.214  1.00 26.23           C  
-ATOM    985  O   LEU A 127      -1.394  77.680  57.016  1.00 31.41           O  
-ATOM    986  CB  LEU A 127      -1.337  75.272  59.196  1.00 18.38           C  
-ATOM    987  CG  LEU A 127      -1.798  73.933  59.780  1.00 20.22           C  
-ATOM    988  CD1 LEU A 127      -0.572  73.169  60.265  1.00 11.06           C  
-ATOM    989  CD2 LEU A 127      -2.785  74.142  60.921  1.00 11.32           C  
-ATOM    990  N   ASP A 128      -1.278  78.425  59.141  1.00 25.11           N  
-ATOM    991  CA  ASP A 128      -0.569  79.657  58.812  1.00 25.00           C  
-ATOM    992  C   ASP A 128       0.794  79.411  58.171  1.00 27.95           C  
-ATOM    993  O   ASP A 128       1.184  80.135  57.256  1.00 29.08           O  
-ATOM    994  CB  ASP A 128      -0.405  80.539  60.057  1.00 32.45           C  
-ATOM    995  CG  ASP A 128      -1.687  81.284  60.433  1.00 34.36           C  
-ATOM    996  OD1 ASP A 128      -2.791  80.713  60.309  1.00 37.10           O  
-ATOM    997  OD2 ASP A 128      -1.582  82.451  60.864  1.00 34.71           O  
-ATOM    998  N   VAL A 129       1.522  78.408  58.664  1.00 27.62           N  
-ATOM    999  CA  VAL A 129       2.837  78.080  58.106  1.00 24.51           C  
-ATOM   1000  C   VAL A 129       2.744  77.440  56.728  1.00 27.28           C  
-ATOM   1001  O   VAL A 129       3.767  77.224  56.073  1.00 36.44           O  
-ATOM   1002  CB  VAL A 129       3.676  77.138  59.015  1.00 23.04           C  
-ATOM   1003  CG1 VAL A 129       4.505  77.951  59.988  1.00 17.64           C  
-ATOM   1004  CG2 VAL A 129       2.780  76.140  59.748  1.00 20.94           C  
-ATOM   1005  N   TYR A 130       1.523  77.118  56.302  1.00 23.77           N  
-ATOM   1006  CA  TYR A 130       1.295  76.508  54.994  1.00 23.34           C  
-ATOM   1007  C   TYR A 130       0.690  77.499  53.999  1.00 27.00           C  
-ATOM   1008  O   TYR A 130       0.261  77.105  52.918  1.00 30.91           O  
-ATOM   1009  CB  TYR A 130       0.381  75.279  55.110  1.00 21.28           C  
-ATOM   1010  CG  TYR A 130       0.916  74.145  55.967  1.00 12.66           C  
-ATOM   1011  CD1 TYR A 130       2.264  74.073  56.323  1.00 12.58           C  
-ATOM   1012  CD2 TYR A 130       0.066  73.145  56.428  1.00 12.39           C  
-ATOM   1013  CE1 TYR A 130       2.746  73.036  57.118  1.00 19.96           C  
-ATOM   1014  CE2 TYR A 130       0.537  72.105  57.221  1.00 17.67           C  
-ATOM   1015  CZ  TYR A 130       1.874  72.057  57.564  1.00 18.50           C  
-ATOM   1016  OH  TYR A 130       2.331  71.034  58.356  1.00 19.96           O  
-ATOM   1017  N   ASN A 131       0.654  78.779  54.367  1.00 29.39           N  
-ATOM   1018  CA  ASN A 131       0.106  79.817  53.492  1.00 30.67           C  
-ATOM   1019  C   ASN A 131       1.024  79.972  52.285  1.00 27.86           C  
-ATOM   1020  O   ASN A 131       2.073  80.607  52.371  1.00 26.20           O  
-ATOM   1021  CB  ASN A 131      -0.005  81.145  54.247  1.00 29.22           C  
-ATOM   1022  CG  ASN A 131      -0.866  82.178  53.519  1.00 30.19           C  
-ATOM   1023  OD1 ASN A 131      -1.453  81.872  52.484  1.00 38.03           O  
-ATOM   1024  ND2 ASN A 131      -0.939  83.397  54.049  1.00 28.46           N  
-ATOM   1025  N   GLY A 132       0.608  79.402  51.159  1.00 28.62           N  
-ATOM   1026  CA  GLY A 132       1.417  79.452  49.955  1.00 33.93           C  
-ATOM   1027  C   GLY A 132       1.454  80.751  49.178  1.00 34.20           C  
-ATOM   1028  O   GLY A 132       2.000  80.784  48.076  1.00 37.68           O  
-ATOM   1029  N   LYS A 133       0.919  81.824  49.749  1.00 34.46           N  
-ATOM   1030  CA  LYS A 133       0.903  83.106  49.056  1.00 32.74           C  
-ATOM   1031  C   LYS A 133       2.274  83.768  48.936  1.00 31.78           C  
-ATOM   1032  O   LYS A 133       2.530  84.485  47.967  1.00 35.14           O  
-ATOM   1033  CB  LYS A 133      -0.101  84.067  49.700  1.00 32.50           C  
-ATOM   1034  CG  LYS A 133       0.334  84.667  51.018  1.00 28.85           C  
-ATOM   1035  CD  LYS A 133      -0.716  85.634  51.524  1.00 26.66           C  
-ATOM   1036  CE  LYS A 133      -0.244  86.371  52.757  1.00 24.58           C  
-ATOM   1037  NZ  LYS A 133      -1.305  87.265  53.289  1.00 33.33           N  
-ATOM   1038  N   TYR A 134       3.155  83.520  49.903  1.00 29.38           N  
-ATOM   1039  CA  TYR A 134       4.497  84.105  49.883  1.00 28.15           C  
-ATOM   1040  C   TYR A 134       5.375  83.417  48.850  1.00 24.85           C  
-ATOM   1041  O   TYR A 134       6.164  84.064  48.165  1.00 27.34           O  
-ATOM   1042  CB  TYR A 134       5.161  83.989  51.257  1.00 28.53           C  
-ATOM   1043  CG  TYR A 134       4.325  84.542  52.378  1.00 33.68           C  
-ATOM   1044  CD1 TYR A 134       4.046  85.905  52.457  1.00 31.84           C  
-ATOM   1045  CD2 TYR A 134       3.784  83.698  53.345  1.00 34.66           C  
-ATOM   1046  CE1 TYR A 134       3.247  86.414  53.468  1.00 34.76           C  
-ATOM   1047  CE2 TYR A 134       2.982  84.196  54.364  1.00 36.83           C  
-ATOM   1048  CZ  TYR A 134       2.716  85.555  54.419  1.00 40.41           C  
-ATOM   1049  OH  TYR A 134       1.916  86.053  55.421  1.00 46.68           O  
-ATOM   1050  N   LEU A 135       5.226  82.100  48.748  1.00 24.36           N  
-ATOM   1051  CA  LEU A 135       6.006  81.297  47.817  1.00 25.34           C  
-ATOM   1052  C   LEU A 135       5.513  81.506  46.389  1.00 27.49           C  
-ATOM   1053  O   LEU A 135       6.313  81.670  45.465  1.00 31.50           O  
-ATOM   1054  CB  LEU A 135       5.928  79.818  48.220  1.00 19.99           C  
-ATOM   1055  CG  LEU A 135       6.781  78.768  47.498  1.00 26.13           C  
-ATOM   1056  CD1 LEU A 135       8.221  79.230  47.317  1.00 20.74           C  
-ATOM   1057  CD2 LEU A 135       6.736  77.480  48.298  1.00 20.00           C  
-ATOM   1058  N   ALA A 136       4.194  81.537  46.224  1.00 24.35           N  
-ATOM   1059  CA  ALA A 136       3.582  81.738  44.917  1.00 27.82           C  
-ATOM   1060  C   ALA A 136       3.965  83.102  44.342  1.00 31.09           C  
-ATOM   1061  O   ALA A 136       4.330  83.213  43.170  1.00 30.61           O  
-ATOM   1062  CB  ALA A 136       2.064  81.613  45.023  1.00 21.77           C  
-ATOM   1063  N   TYR A 137       3.922  84.124  45.193  1.00 31.26           N  
-ATOM   1064  CA  TYR A 137       4.248  85.490  44.797  1.00 29.05           C  
-ATOM   1065  C   TYR A 137       5.743  85.702  44.549  1.00 28.86           C  
-ATOM   1066  O   TYR A 137       6.139  86.188  43.488  1.00 30.23           O  
-ATOM   1067  CB  TYR A 137       3.743  86.475  45.862  1.00 30.53           C  
-ATOM   1068  CG  TYR A 137       4.200  87.902  45.655  1.00 34.44           C  
-ATOM   1069  CD1 TYR A 137       3.645  88.693  44.649  1.00 35.30           C  
-ATOM   1070  CD2 TYR A 137       5.219  88.449  46.439  1.00 33.16           C  
-ATOM   1071  CE1 TYR A 137       4.097  89.989  44.422  1.00 34.75           C  
-ATOM   1072  CE2 TYR A 137       5.679  89.746  46.220  1.00 31.28           C  
-ATOM   1073  CZ  TYR A 137       5.115  90.509  45.209  1.00 36.67           C  
-ATOM   1074  OH  TYR A 137       5.578  91.784  44.974  1.00 33.94           O  
-ATOM   1075  N   THR A 138       6.567  85.326  45.523  1.00 24.87           N  
-ATOM   1076  CA  THR A 138       8.010  85.501  45.416  1.00 24.86           C  
-ATOM   1077  C   THR A 138       8.640  84.722  44.270  1.00 28.95           C  
-ATOM   1078  O   THR A 138       9.393  85.286  43.472  1.00 30.58           O  
-ATOM   1079  CB  THR A 138       8.724  85.105  46.726  1.00 19.30           C  
-ATOM   1080  OG1 THR A 138       8.143  85.821  47.821  1.00 24.14           O  
-ATOM   1081  CG2 THR A 138      10.208  85.436  46.650  1.00 15.79           C  
-ATOM   1082  N   GLU A 139       8.320  83.433  44.189  1.00 31.60           N  
-ATOM   1083  CA  GLU A 139       8.883  82.559  43.164  1.00 31.98           C  
-ATOM   1084  C   GLU A 139       8.116  82.430  41.857  1.00 33.58           C  
-ATOM   1085  O   GLU A 139       8.565  81.735  40.944  1.00 35.97           O  
-ATOM   1086  CB  GLU A 139       9.146  81.174  43.747  1.00 28.99           C  
-ATOM   1087  CG  GLU A 139      10.264  81.163  44.769  1.00 27.25           C  
-ATOM   1088  CD  GLU A 139      11.560  81.711  44.208  1.00 20.76           C  
-ATOM   1089  OE1 GLU A 139      11.989  81.265  43.121  1.00 25.81           O  
-ATOM   1090  OE2 GLU A 139      12.151  82.591  44.859  1.00 23.98           O  
-ATOM   1091  N   GLU A 140       6.960  83.081  41.773  1.00 32.70           N  
-ATOM   1092  CA  GLU A 140       6.148  83.049  40.563  1.00 32.00           C  
-ATOM   1093  C   GLU A 140       5.697  81.625  40.211  1.00 32.59           C  
-ATOM   1094  O   GLU A 140       5.896  81.154  39.088  1.00 34.45           O  
-ATOM   1095  CB  GLU A 140       6.942  83.676  39.406  1.00 41.87           C  
-ATOM   1096  CG  GLU A 140       6.133  83.994  38.157  1.00 56.54           C  
-ATOM   1097  CD  GLU A 140       5.078  85.060  38.391  1.00 67.27           C  
-ATOM   1098  OE1 GLU A 140       5.363  86.043  39.113  1.00 71.67           O  
-ATOM   1099  OE2 GLU A 140       3.965  84.913  37.840  1.00 70.80           O  
-ATOM   1100  N   VAL A 141       5.122  80.930  41.190  1.00 28.73           N  
-ATOM   1101  CA  VAL A 141       4.627  79.567  40.981  1.00 22.03           C  
-ATOM   1102  C   VAL A 141       3.161  79.467  41.392  1.00 23.58           C  
-ATOM   1103  O   VAL A 141       2.627  80.360  42.050  1.00 18.14           O  
-ATOM   1104  CB  VAL A 141       5.432  78.503  41.795  1.00 20.42           C  
-ATOM   1105  CG1 VAL A 141       6.900  78.499  41.391  1.00 18.74           C  
-ATOM   1106  CG2 VAL A 141       5.291  78.748  43.288  1.00 16.16           C  
-ATOM   1107  N   VAL A 142       2.501  78.395  40.963  1.00 28.37           N  
-ATOM   1108  CA  VAL A 142       1.108  78.164  41.326  1.00 24.76           C  
-ATOM   1109  C   VAL A 142       1.172  77.169  42.479  1.00 25.27           C  
-ATOM   1110  O   VAL A 142       1.489  75.997  42.280  1.00 31.77           O  
-ATOM   1111  CB  VAL A 142       0.297  77.566  40.158  1.00 21.42           C  
-ATOM   1112  CG1 VAL A 142      -1.134  77.326  40.587  1.00 13.03           C  
-ATOM   1113  CG2 VAL A 142       0.322  78.511  38.968  1.00 24.35           C  
-ATOM   1114  N   LEU A 143       0.936  77.662  43.691  1.00 26.16           N  
-ATOM   1115  CA  LEU A 143       0.992  76.829  44.885  1.00 20.56           C  
-ATOM   1116  C   LEU A 143      -0.347  76.184  45.221  1.00 20.06           C  
-ATOM   1117  O   LEU A 143      -1.332  76.867  45.474  1.00 21.34           O  
-ATOM   1118  CB  LEU A 143       1.501  77.659  46.074  1.00 18.53           C  
-ATOM   1119  CG  LEU A 143       2.173  76.957  47.263  1.00 19.40           C  
-ATOM   1120  CD1 LEU A 143       1.181  76.141  48.068  1.00 12.99           C  
-ATOM   1121  CD2 LEU A 143       3.311  76.080  46.767  1.00 19.64           C  
-ATOM   1122  N   VAL A 144      -0.366  74.855  45.225  1.00 21.07           N  
-ATOM   1123  CA  VAL A 144      -1.566  74.095  45.561  1.00 18.49           C  
-ATOM   1124  C   VAL A 144      -1.296  73.328  46.852  1.00 20.64           C  
-ATOM   1125  O   VAL A 144      -0.176  72.876  47.084  1.00 16.43           O  
-ATOM   1126  CB  VAL A 144      -1.928  73.051  44.464  1.00 16.25           C  
-ATOM   1127  CG1 VAL A 144      -3.174  72.268  44.866  1.00  7.11           C  
-ATOM   1128  CG2 VAL A 144      -2.141  73.727  43.125  1.00 14.43           C  
-ATOM   1129  N   SER A 145      -2.305  73.231  47.711  1.00 17.74           N  
-ATOM   1130  CA  SER A 145      -2.178  72.480  48.951  1.00 17.21           C  
-ATOM   1131  C   SER A 145      -3.416  71.609  49.041  1.00 15.75           C  
-ATOM   1132  O   SER A 145      -4.539  72.103  49.055  1.00 16.69           O  
-ATOM   1133  CB  SER A 145      -2.056  73.401  50.171  1.00 17.76           C  
-ATOM   1134  OG  SER A 145      -3.239  74.145  50.406  1.00 21.21           O  
-ATOM   1135  N   LEU A 146      -3.204  70.301  48.999  1.00 17.95           N  
-ATOM   1136  CA  LEU A 146      -4.303  69.354  49.069  1.00 17.00           C  
-ATOM   1137  C   LEU A 146      -4.645  69.013  50.517  1.00 21.16           C  
-ATOM   1138  O   LEU A 146      -4.128  69.624  51.452  1.00 16.14           O  
-ATOM   1139  CB  LEU A 146      -3.950  68.083  48.270  1.00 19.30           C  
-ATOM   1140  CG  LEU A 146      -2.626  67.338  48.515  1.00 14.59           C  
-ATOM   1141  CD1 LEU A 146      -2.710  66.433  49.742  1.00  5.63           C  
-ATOM   1142  CD2 LEU A 146      -2.294  66.499  47.297  1.00 10.59           C  
-ATOM   1143  N   SER A 147      -5.555  68.062  50.685  1.00 19.32           N  
-ATOM   1144  CA  SER A 147      -5.958  67.595  52.000  1.00 20.18           C  
-ATOM   1145  C   SER A 147      -6.331  66.133  51.841  1.00 19.41           C  
-ATOM   1146  O   SER A 147      -6.702  65.691  50.750  1.00 22.70           O  
-ATOM   1147  CB  SER A 147      -7.142  68.398  52.548  1.00 15.42           C  
-ATOM   1148  OG  SER A 147      -8.340  68.115  51.848  1.00 21.45           O  
-ATOM   1149  N   TYR A 148      -6.179  65.375  52.916  1.00 18.84           N  
-ATOM   1150  CA  TYR A 148      -6.503  63.961  52.888  1.00 17.54           C  
-ATOM   1151  C   TYR A 148      -6.990  63.512  54.254  1.00 18.21           C  
-ATOM   1152  O   TYR A 148      -6.678  64.131  55.272  1.00 19.82           O  
-ATOM   1153  CB  TYR A 148      -5.287  63.137  52.444  1.00 14.14           C  
-ATOM   1154  CG  TYR A 148      -4.069  63.265  53.334  1.00 14.91           C  
-ATOM   1155  CD1 TYR A 148      -3.218  64.368  53.237  1.00 16.55           C  
-ATOM   1156  CD2 TYR A 148      -3.757  62.274  54.260  1.00 15.09           C  
-ATOM   1157  CE1 TYR A 148      -2.084  64.475  54.038  1.00 13.73           C  
-ATOM   1158  CE2 TYR A 148      -2.630  62.371  55.066  1.00 12.87           C  
-ATOM   1159  CZ  TYR A 148      -1.795  63.469  54.953  1.00 16.96           C  
-ATOM   1160  OH  TYR A 148      -0.666  63.544  55.743  1.00 12.62           O  
-ATOM   1161  N   ARG A 149      -7.792  62.455  54.262  1.00 18.96           N  
-ATOM   1162  CA  ARG A 149      -8.329  61.916  55.500  1.00 17.37           C  
-ATOM   1163  C   ARG A 149      -7.216  61.299  56.339  1.00 22.26           C  
-ATOM   1164  O   ARG A 149      -6.414  60.501  55.844  1.00 21.39           O  
-ATOM   1165  CB  ARG A 149      -9.407  60.870  55.204  1.00 12.43           C  
-ATOM   1166  CG  ARG A 149     -10.741  61.442  54.761  1.00 13.12           C  
-ATOM   1167  CD  ARG A 149     -11.704  60.339  54.330  1.00 19.63           C  
-ATOM   1168  NE  ARG A 149     -11.387  59.805  53.005  1.00 23.19           N  
-ATOM   1169  CZ  ARG A 149     -11.914  58.698  52.484  1.00 21.75           C  
-ATOM   1170  NH1 ARG A 149     -12.795  57.977  53.166  1.00 19.65           N  
-ATOM   1171  NH2 ARG A 149     -11.566  58.318  51.264  1.00 22.56           N  
-ATOM   1172  N   VAL A 150      -7.152  61.717  57.600  1.00 21.80           N  
-ATOM   1173  CA  VAL A 150      -6.156  61.217  58.539  1.00 19.06           C  
-ATOM   1174  C   VAL A 150      -6.821  60.321  59.583  1.00 24.39           C  
-ATOM   1175  O   VAL A 150      -8.041  60.159  59.586  1.00 23.41           O  
-ATOM   1176  CB  VAL A 150      -5.408  62.373  59.246  1.00 15.69           C  
-ATOM   1177  CG1 VAL A 150      -4.543  63.126  58.250  1.00 13.90           C  
-ATOM   1178  CG2 VAL A 150      -6.394  63.316  59.914  1.00  9.88           C  
-ATOM   1179  N   GLY A 151      -6.011  59.744  60.466  1.00 24.93           N  
-ATOM   1180  CA  GLY A 151      -6.530  58.866  61.498  1.00 22.18           C  
-ATOM   1181  C   GLY A 151      -7.186  57.631  60.919  1.00 26.01           C  
-ATOM   1182  O   GLY A 151      -6.822  57.172  59.834  1.00 30.93           O  
-ATOM   1183  N   ALA A 152      -8.167  57.099  61.640  1.00 22.52           N  
-ATOM   1184  CA  ALA A 152      -8.891  55.910  61.206  1.00 22.99           C  
-ATOM   1185  C   ALA A 152      -9.707  56.198  59.950  1.00 24.84           C  
-ATOM   1186  O   ALA A 152      -9.830  55.339  59.074  1.00 21.18           O  
-ATOM   1187  CB  ALA A 152      -9.801  55.415  62.321  1.00 22.76           C  
-ATOM   1188  N   PHE A 153     -10.232  57.420  59.862  1.00 24.63           N  
-ATOM   1189  CA  PHE A 153     -11.044  57.863  58.730  1.00 21.83           C  
-ATOM   1190  C   PHE A 153     -10.319  57.685  57.402  1.00 20.28           C  
-ATOM   1191  O   PHE A 153     -10.931  57.310  56.401  1.00 19.95           O  
-ATOM   1192  CB  PHE A 153     -11.434  59.334  58.900  1.00 25.79           C  
-ATOM   1193  CG  PHE A 153     -12.056  59.644  60.230  1.00 30.92           C  
-ATOM   1194  CD1 PHE A 153     -13.420  59.455  60.438  1.00 30.63           C  
-ATOM   1195  CD2 PHE A 153     -11.273  60.105  61.286  1.00 31.23           C  
-ATOM   1196  CE1 PHE A 153     -13.994  59.719  61.681  1.00 28.66           C  
-ATOM   1197  CE2 PHE A 153     -11.837  60.372  62.532  1.00 22.34           C  
-ATOM   1198  CZ  PHE A 153     -13.200  60.178  62.728  1.00 29.32           C  
-ATOM   1199  N   GLY A 154      -9.014  57.938  57.397  1.00 18.27           N  
-ATOM   1200  CA  GLY A 154      -8.257  57.798  56.169  1.00 17.84           C  
-ATOM   1201  C   GLY A 154      -7.362  56.579  56.087  1.00 19.88           C  
-ATOM   1202  O   GLY A 154      -6.883  56.244  55.002  1.00 23.98           O  
-ATOM   1203  N   PHE A 155      -7.156  55.883  57.202  1.00 17.67           N  
-ATOM   1204  CA  PHE A 155      -6.264  54.734  57.173  1.00 16.58           C  
-ATOM   1205  C   PHE A 155      -6.673  53.446  57.883  1.00 17.19           C  
-ATOM   1206  O   PHE A 155      -5.825  52.581  58.124  1.00 20.91           O  
-ATOM   1207  CB  PHE A 155      -4.860  55.166  57.610  1.00 13.60           C  
-ATOM   1208  CG  PHE A 155      -4.231  56.176  56.689  1.00 17.19           C  
-ATOM   1209  CD1 PHE A 155      -3.647  55.775  55.489  1.00 14.90           C  
-ATOM   1210  CD2 PHE A 155      -4.265  57.533  56.996  1.00 12.25           C  
-ATOM   1211  CE1 PHE A 155      -3.113  56.707  54.608  1.00 12.74           C  
-ATOM   1212  CE2 PHE A 155      -3.731  58.474  56.118  1.00 17.18           C  
-ATOM   1213  CZ  PHE A 155      -3.155  58.057  54.922  1.00 12.63           C  
-ATOM   1214  N   LEU A 156      -7.955  53.302  58.217  1.00 17.25           N  
-ATOM   1215  CA  LEU A 156      -8.424  52.067  58.853  1.00 20.33           C  
-ATOM   1216  C   LEU A 156      -8.250  50.990  57.787  1.00 20.55           C  
-ATOM   1217  O   LEU A 156      -8.703  51.167  56.653  1.00 22.02           O  
-ATOM   1218  CB  LEU A 156      -9.900  52.168  59.240  1.00 26.88           C  
-ATOM   1219  CG  LEU A 156     -10.453  50.938  59.969  1.00 30.86           C  
-ATOM   1220  CD1 LEU A 156     -10.033  50.963  61.433  1.00 23.41           C  
-ATOM   1221  CD2 LEU A 156     -11.961  50.911  59.860  1.00 30.86           C  
-ATOM   1222  N   ALA A 157      -7.601  49.883  58.137  1.00 21.07           N  
-ATOM   1223  CA  ALA A 157      -7.353  48.829  57.159  1.00 22.84           C  
-ATOM   1224  C   ALA A 157      -7.815  47.415  57.495  1.00 26.12           C  
-ATOM   1225  O   ALA A 157      -7.414  46.832  58.500  1.00 27.47           O  
-ATOM   1226  CB  ALA A 157      -5.878  48.810  56.791  1.00 18.03           C  
-ATOM   1227  N   LEU A 158      -8.621  46.857  56.594  1.00 30.47           N  
-ATOM   1228  CA  LEU A 158      -9.143  45.498  56.710  1.00 25.56           C  
-ATOM   1229  C   LEU A 158      -9.008  44.887  55.318  1.00 28.21           C  
-ATOM   1230  O   LEU A 158      -9.971  44.840  54.552  1.00 37.22           O  
-ATOM   1231  CB  LEU A 158     -10.610  45.520  57.153  1.00 25.06           C  
-ATOM   1232  CG  LEU A 158     -10.866  45.954  58.601  1.00 30.81           C  
-ATOM   1233  CD1 LEU A 158     -12.350  46.187  58.823  1.00 27.73           C  
-ATOM   1234  CD2 LEU A 158     -10.330  44.908  59.573  1.00 23.03           C  
-ATOM   1235  N   HIS A 159      -7.789  44.460  54.995  1.00 31.55           N  
-ATOM   1236  CA  HIS A 159      -7.456  43.876  53.696  1.00 36.94           C  
-ATOM   1237  C   HIS A 159      -8.417  42.774  53.259  1.00 44.87           C  
-ATOM   1238  O   HIS A 159      -8.630  41.796  53.977  1.00 47.99           O  
-ATOM   1239  CB  HIS A 159      -6.017  43.352  53.710  1.00 37.45           C  
-ATOM   1240  CG  HIS A 159      -5.484  43.010  52.353  1.00 37.76           C  
-ATOM   1241  ND1 HIS A 159      -5.530  43.889  51.292  1.00 36.20           N  
-ATOM   1242  CD2 HIS A 159      -4.896  41.884  51.883  1.00 35.53           C  
-ATOM   1243  CE1 HIS A 159      -4.994  43.319  50.227  1.00 44.49           C  
-ATOM   1244  NE2 HIS A 159      -4.603  42.102  50.558  1.00 41.19           N  
-ATOM   1245  N   GLY A 160      -8.974  42.939  52.063  1.00 46.32           N  
-ATOM   1246  CA  GLY A 160      -9.923  41.975  51.536  1.00 46.49           C  
-ATOM   1247  C   GLY A 160     -11.309  42.587  51.451  1.00 45.57           C  
-ATOM   1248  O   GLY A 160     -12.155  42.136  50.675  1.00 48.06           O  
-ATOM   1249  N   SER A 161     -11.534  43.620  52.259  1.00 43.88           N  
-ATOM   1250  CA  SER A 161     -12.807  44.328  52.295  1.00 43.49           C  
-ATOM   1251  C   SER A 161     -12.761  45.532  51.368  1.00 45.57           C  
-ATOM   1252  O   SER A 161     -11.727  46.189  51.246  1.00 50.03           O  
-ATOM   1253  CB  SER A 161     -13.115  44.796  53.718  1.00 40.70           C  
-ATOM   1254  OG  SER A 161     -14.246  45.649  53.735  1.00 44.05           O  
-ATOM   1255  N   GLN A 162     -13.885  45.819  50.720  1.00 44.53           N  
-ATOM   1256  CA  GLN A 162     -13.967  46.954  49.810  1.00 43.89           C  
-ATOM   1257  C   GLN A 162     -14.604  48.164  50.483  1.00 38.75           C  
-ATOM   1258  O   GLN A 162     -14.729  49.225  49.876  1.00 38.30           O  
-ATOM   1259  CB  GLN A 162     -14.734  46.576  48.538  1.00 51.24           C  
-ATOM   1260  CG  GLN A 162     -14.028  45.534  47.667  1.00 56.11           C  
-ATOM   1261  CD  GLN A 162     -12.612  45.941  47.275  1.00 61.55           C  
-ATOM   1262  OE1 GLN A 162     -12.373  47.077  46.855  1.00 60.68           O  
-ATOM   1263  NE2 GLN A 162     -11.667  45.018  47.419  1.00 60.88           N  
-ATOM   1264  N   GLU A 163     -15.009  47.996  51.739  1.00 40.22           N  
-ATOM   1265  CA  GLU A 163     -15.623  49.080  52.499  1.00 43.30           C  
-ATOM   1266  C   GLU A 163     -14.563  49.853  53.278  1.00 41.80           C  
-ATOM   1267  O   GLU A 163     -14.748  51.029  53.594  1.00 44.04           O  
-ATOM   1268  CB  GLU A 163     -16.687  48.536  53.456  1.00 47.52           C  
-ATOM   1269  CG  GLU A 163     -17.814  47.757  52.781  1.00 52.44           C  
-ATOM   1270  CD  GLU A 163     -18.521  48.542  51.681  1.00 53.93           C  
-ATOM   1271  OE1 GLU A 163     -18.837  49.736  51.890  1.00 52.34           O  
-ATOM   1272  OE2 GLU A 163     -18.766  47.955  50.605  1.00 53.72           O  
-ATOM   1273  N   ALA A 164     -13.455  49.178  53.577  1.00 37.27           N  
-ATOM   1274  CA  ALA A 164     -12.336  49.770  54.306  1.00 35.08           C  
-ATOM   1275  C   ALA A 164     -11.062  48.988  53.983  1.00 34.64           C  
-ATOM   1276  O   ALA A 164     -10.565  48.221  54.811  1.00 35.29           O  
-ATOM   1277  CB  ALA A 164     -12.611  49.748  55.813  1.00 29.26           C  
-ATOM   1278  N   PRO A 165     -10.530  49.158  52.758  1.00 34.65           N  
-ATOM   1279  CA  PRO A 165      -9.312  48.470  52.314  1.00 32.42           C  
-ATOM   1280  C   PRO A 165      -8.034  49.069  52.898  1.00 31.96           C  
-ATOM   1281  O   PRO A 165      -7.018  48.382  53.031  1.00 30.61           O  
-ATOM   1282  CB  PRO A 165      -9.362  48.653  50.798  1.00 33.19           C  
-ATOM   1283  CG  PRO A 165      -9.960  50.019  50.658  1.00 30.69           C  
-ATOM   1284  CD  PRO A 165     -11.085  49.994  51.673  1.00 29.82           C  
-ATOM   1285  N   GLY A 166      -8.106  50.350  53.249  1.00 33.20           N  
-ATOM   1286  CA  GLY A 166      -6.962  51.053  53.792  1.00 26.28           C  
-ATOM   1287  C   GLY A 166      -6.345  51.924  52.717  1.00 27.02           C  
-ATOM   1288  O   GLY A 166      -6.703  51.809  51.545  1.00 25.25           O  
-ATOM   1289  N   ASN A 167      -5.446  52.819  53.123  1.00 27.10           N  
-ATOM   1290  CA  ASN A 167      -4.752  53.723  52.206  1.00 23.29           C  
-ATOM   1291  C   ASN A 167      -5.637  54.738  51.493  1.00 18.91           C  
-ATOM   1292  O   ASN A 167      -5.183  55.415  50.569  1.00 16.64           O  
-ATOM   1293  CB  ASN A 167      -3.968  52.921  51.161  1.00 17.45           C  
-ATOM   1294  CG  ASN A 167      -2.834  52.130  51.769  1.00 20.42           C  
-ATOM   1295  OD1 ASN A 167      -2.277  52.518  52.793  1.00 24.01           O  
-ATOM   1296  ND2 ASN A 167      -2.484  51.017  51.142  1.00 16.85           N  
-ATOM   1297  N   VAL A 168      -6.888  54.867  51.927  1.00 16.88           N  
-ATOM   1298  CA  VAL A 168      -7.793  55.807  51.276  1.00 21.58           C  
-ATOM   1299  C   VAL A 168      -7.344  57.254  51.456  1.00 22.25           C  
-ATOM   1300  O   VAL A 168      -7.681  58.118  50.649  1.00 29.63           O  
-ATOM   1301  CB  VAL A 168      -9.268  55.608  51.718  1.00 16.91           C  
-ATOM   1302  CG1 VAL A 168      -9.714  54.181  51.419  1.00 16.78           C  
-ATOM   1303  CG2 VAL A 168      -9.454  55.935  53.189  1.00 11.70           C  
-ATOM   1304  N   GLY A 169      -6.544  57.499  52.492  1.00 15.61           N  
-ATOM   1305  CA  GLY A 169      -6.028  58.832  52.744  1.00 17.21           C  
-ATOM   1306  C   GLY A 169      -5.006  59.167  51.671  1.00 15.60           C  
-ATOM   1307  O   GLY A 169      -4.855  60.328  51.282  1.00 14.97           O  
-ATOM   1308  N   LEU A 170      -4.290  58.140  51.213  1.00 12.90           N  
-ATOM   1309  CA  LEU A 170      -3.297  58.286  50.158  1.00 11.96           C  
-ATOM   1310  C   LEU A 170      -4.019  58.442  48.821  1.00 17.31           C  
-ATOM   1311  O   LEU A 170      -3.555  59.164  47.944  1.00 18.26           O  
-ATOM   1312  CB  LEU A 170      -2.377  57.064  50.117  1.00 11.18           C  
-ATOM   1313  CG  LEU A 170      -1.311  56.976  51.208  1.00 11.70           C  
-ATOM   1314  CD1 LEU A 170      -0.614  55.625  51.155  1.00  4.23           C  
-ATOM   1315  CD2 LEU A 170      -0.313  58.109  51.033  1.00  2.00           C  
-ATOM   1316  N   LEU A 171      -5.153  57.757  48.670  1.00 22.19           N  
-ATOM   1317  CA  LEU A 171      -5.947  57.849  47.448  1.00 24.46           C  
-ATOM   1318  C   LEU A 171      -6.563  59.247  47.336  1.00 26.86           C  
-ATOM   1319  O   LEU A 171      -6.768  59.751  46.230  1.00 26.64           O  
-ATOM   1320  CB  LEU A 171      -7.037  56.775  47.419  1.00 19.09           C  
-ATOM   1321  CG  LEU A 171      -6.577  55.317  47.338  1.00 24.69           C  
-ATOM   1322  CD1 LEU A 171      -7.782  54.401  47.323  1.00 18.21           C  
-ATOM   1323  CD2 LEU A 171      -5.728  55.091  46.098  1.00 14.63           C  
-ATOM   1324  N   ASP A 172      -6.844  59.871  48.483  1.00 24.38           N  
-ATOM   1325  CA  ASP A 172      -7.392  61.229  48.514  1.00 23.98           C  
-ATOM   1326  C   ASP A 172      -6.362  62.164  47.881  1.00 24.89           C  
-ATOM   1327  O   ASP A 172      -6.703  63.035  47.081  1.00 32.22           O  
-ATOM   1328  CB  ASP A 172      -7.644  61.697  49.955  1.00 18.23           C  
-ATOM   1329  CG  ASP A 172      -8.817  60.994  50.622  1.00 22.39           C  
-ATOM   1330  OD1 ASP A 172      -9.476  60.132  49.999  1.00 24.04           O  
-ATOM   1331  OD2 ASP A 172      -9.084  61.317  51.797  1.00 21.64           O  
-ATOM   1332  N   GLN A 173      -5.100  61.971  48.258  1.00 19.89           N  
-ATOM   1333  CA  GLN A 173      -4.002  62.776  47.741  1.00 21.35           C  
-ATOM   1334  C   GLN A 173      -3.856  62.551  46.238  1.00 16.63           C  
-ATOM   1335  O   GLN A 173      -3.610  63.493  45.485  1.00 20.02           O  
-ATOM   1336  CB  GLN A 173      -2.693  62.394  48.434  1.00 19.67           C  
-ATOM   1337  CG  GLN A 173      -2.690  62.581  49.940  1.00 17.57           C  
-ATOM   1338  CD  GLN A 173      -1.420  62.062  50.594  1.00 18.23           C  
-ATOM   1339  OE1 GLN A 173      -0.367  61.986  49.962  1.00 23.86           O  
-ATOM   1340  NE2 GLN A 173      -1.520  61.674  51.853  1.00 12.22           N  
-ATOM   1341  N   ARG A 174      -4.019  61.300  45.813  1.00 17.05           N  
-ATOM   1342  CA  ARG A 174      -3.902  60.938  44.408  1.00 16.16           C  
-ATOM   1343  C   ARG A 174      -4.993  61.597  43.571  1.00 14.89           C  
-ATOM   1344  O   ARG A 174      -4.734  62.028  42.448  1.00 23.20           O  
-ATOM   1345  CB  ARG A 174      -3.957  59.417  44.236  1.00 15.34           C  
-ATOM   1346  CG  ARG A 174      -3.934  58.959  42.781  1.00 14.80           C  
-ATOM   1347  CD  ARG A 174      -4.206  57.472  42.657  1.00 11.93           C  
-ATOM   1348  NE  ARG A 174      -3.075  56.672  43.114  1.00 10.18           N  
-ATOM   1349  CZ  ARG A 174      -3.069  55.344  43.190  1.00 17.90           C  
-ATOM   1350  NH1 ARG A 174      -4.144  54.647  42.851  1.00 12.28           N  
-ATOM   1351  NH2 ARG A 174      -1.965  54.709  43.551  1.00 13.87           N  
-ATOM   1352  N   MET A 175      -6.205  61.676  44.118  1.00 14.76           N  
-ATOM   1353  CA  MET A 175      -7.323  62.283  43.407  1.00 17.14           C  
-ATOM   1354  C   MET A 175      -7.146  63.791  43.305  1.00 20.08           C  
-ATOM   1355  O   MET A 175      -7.635  64.418  42.367  1.00 24.86           O  
-ATOM   1356  CB  MET A 175      -8.650  61.945  44.086  1.00 21.10           C  
-ATOM   1357  CG  MET A 175      -9.871  62.312  43.255  1.00 22.06           C  
-ATOM   1358  SD  MET A 175     -11.381  61.569  43.874  1.00 27.18           S  
-ATOM   1359  CE  MET A 175     -11.119  59.867  43.409  1.00 19.77           C  
-ATOM   1360  N   ALA A 176      -6.464  64.371  44.288  1.00 19.79           N  
-ATOM   1361  CA  ALA A 176      -6.199  65.803  44.294  1.00 16.64           C  
-ATOM   1362  C   ALA A 176      -5.128  66.058  43.237  1.00 21.90           C  
-ATOM   1363  O   ALA A 176      -5.190  67.047  42.500  1.00 18.48           O  
-ATOM   1364  CB  ALA A 176      -5.709  66.247  45.668  1.00 12.38           C  
-ATOM   1365  N   LEU A 177      -4.165  65.139  43.150  1.00 18.07           N  
-ATOM   1366  CA  LEU A 177      -3.088  65.236  42.172  1.00 18.80           C  
-ATOM   1367  C   LEU A 177      -3.663  65.052  40.769  1.00 19.49           C  
-ATOM   1368  O   LEU A 177      -3.199  65.679  39.812  1.00 15.41           O  
-ATOM   1369  CB  LEU A 177      -2.024  64.167  42.426  1.00 16.27           C  
-ATOM   1370  CG  LEU A 177      -1.083  64.355  43.615  1.00 17.09           C  
-ATOM   1371  CD1 LEU A 177      -0.077  63.212  43.647  1.00 11.22           C  
-ATOM   1372  CD2 LEU A 177      -0.367  65.692  43.511  1.00 21.00           C  
-ATOM   1373  N   GLN A 178      -4.672  64.188  40.663  1.00 17.65           N  
-ATOM   1374  CA  GLN A 178      -5.337  63.909  39.395  1.00 23.03           C  
-ATOM   1375  C   GLN A 178      -6.151  65.129  38.980  1.00 23.91           C  
-ATOM   1376  O   GLN A 178      -6.296  65.415  37.791  1.00 29.75           O  
-ATOM   1377  CB  GLN A 178      -6.262  62.694  39.534  1.00 23.74           C  
-ATOM   1378  CG  GLN A 178      -7.047  62.324  38.272  1.00 24.54           C  
-ATOM   1379  CD  GLN A 178      -6.179  61.739  37.183  1.00 23.03           C  
-ATOM   1380  OE1 GLN A 178      -5.727  60.604  37.285  1.00 30.77           O  
-ATOM   1381  NE2 GLN A 178      -5.940  62.512  36.130  1.00 16.71           N  
-ATOM   1382  N   TRP A 179      -6.683  65.841  39.971  1.00 18.07           N  
-ATOM   1383  CA  TRP A 179      -7.477  67.030  39.713  1.00 13.59           C  
-ATOM   1384  C   TRP A 179      -6.548  68.152  39.259  1.00 20.86           C  
-ATOM   1385  O   TRP A 179      -6.933  68.995  38.450  1.00 24.32           O  
-ATOM   1386  CB  TRP A 179      -8.239  67.444  40.970  1.00 17.61           C  
-ATOM   1387  CG  TRP A 179      -9.307  68.444  40.706  1.00 18.26           C  
-ATOM   1388  CD1 TRP A 179     -10.625  68.188  40.460  1.00 22.34           C  
-ATOM   1389  CD2 TRP A 179      -9.154  69.866  40.645  1.00 17.25           C  
-ATOM   1390  NE1 TRP A 179     -11.303  69.362  40.248  1.00 22.47           N  
-ATOM   1391  CE2 TRP A 179     -10.426  70.408  40.356  1.00 15.04           C  
-ATOM   1392  CE3 TRP A 179      -8.065  70.733  40.804  1.00 15.65           C  
-ATOM   1393  CZ2 TRP A 179     -10.642  71.782  40.226  1.00 13.57           C  
-ATOM   1394  CZ3 TRP A 179      -8.280  72.101  40.674  1.00 15.61           C  
-ATOM   1395  CH2 TRP A 179      -9.561  72.610  40.386  1.00 16.59           C  
-ATOM   1396  N   VAL A 180      -5.334  68.166  39.803  1.00 17.99           N  
-ATOM   1397  CA  VAL A 180      -4.337  69.164  39.438  1.00 19.14           C  
-ATOM   1398  C   VAL A 180      -3.881  68.889  38.005  1.00 23.50           C  
-ATOM   1399  O   VAL A 180      -3.738  69.808  37.199  1.00 29.24           O  
-ATOM   1400  CB  VAL A 180      -3.123  69.115  40.398  1.00 18.20           C  
-ATOM   1401  CG1 VAL A 180      -1.958  69.922  39.842  1.00  5.61           C  
-ATOM   1402  CG2 VAL A 180      -3.524  69.649  41.755  1.00 17.88           C  
-ATOM   1403  N   HIS A 181      -3.684  67.614  37.686  1.00 20.98           N  
-ATOM   1404  CA  HIS A 181      -3.258  67.210  36.351  1.00 22.99           C  
-ATOM   1405  C   HIS A 181      -4.319  67.596  35.321  1.00 25.14           C  
-ATOM   1406  O   HIS A 181      -3.999  68.088  34.239  1.00 31.11           O  
-ATOM   1407  CB  HIS A 181      -3.023  65.694  36.317  1.00 21.95           C  
-ATOM   1408  CG  HIS A 181      -2.790  65.141  34.943  1.00 27.83           C  
-ATOM   1409  ND1 HIS A 181      -3.808  64.641  34.158  1.00 29.15           N  
-ATOM   1410  CD2 HIS A 181      -1.654  64.992  34.221  1.00 26.65           C  
-ATOM   1411  CE1 HIS A 181      -3.310  64.207  33.015  1.00 29.33           C  
-ATOM   1412  NE2 HIS A 181      -2.005  64.408  33.028  1.00 25.54           N  
-ATOM   1413  N   ASP A 182      -5.582  67.407  35.692  1.00 24.40           N  
-ATOM   1414  CA  ASP A 182      -6.701  67.702  34.814  1.00 21.08           C  
-ATOM   1415  C   ASP A 182      -7.108  69.174  34.711  1.00 21.55           C  
-ATOM   1416  O   ASP A 182      -7.446  69.642  33.624  1.00 28.52           O  
-ATOM   1417  CB  ASP A 182      -7.925  66.871  35.232  1.00 14.98           C  
-ATOM   1418  CG  ASP A 182      -7.705  65.365  35.093  1.00 19.69           C  
-ATOM   1419  OD1 ASP A 182      -6.740  64.944  34.421  1.00 23.29           O  
-ATOM   1420  OD2 ASP A 182      -8.512  64.595  35.658  1.00 23.20           O  
-ATOM   1421  N   ASN A 183      -7.029  69.917  35.812  1.00 20.44           N  
-ATOM   1422  CA  ASN A 183      -7.476  71.310  35.806  1.00 19.51           C  
-ATOM   1423  C   ASN A 183      -6.495  72.453  36.057  1.00 20.69           C  
-ATOM   1424  O   ASN A 183      -6.842  73.607  35.798  1.00 26.66           O  
-ATOM   1425  CB  ASN A 183      -8.633  71.472  36.792  1.00 21.24           C  
-ATOM   1426  CG  ASN A 183      -9.759  70.497  36.540  1.00 24.05           C  
-ATOM   1427  OD1 ASN A 183     -10.794  70.859  35.992  1.00 26.07           O  
-ATOM   1428  ND2 ASN A 183      -9.566  69.254  36.950  1.00 25.46           N  
-ATOM   1429  N   ILE A 184      -5.292  72.166  36.545  1.00 17.02           N  
-ATOM   1430  CA  ILE A 184      -4.343  73.243  36.842  1.00 23.27           C  
-ATOM   1431  C   ILE A 184      -4.025  74.191  35.678  1.00 30.18           C  
-ATOM   1432  O   ILE A 184      -3.644  75.343  35.898  1.00 30.11           O  
-ATOM   1433  CB  ILE A 184      -3.030  72.712  37.489  1.00 19.63           C  
-ATOM   1434  CG1 ILE A 184      -2.401  73.803  38.365  1.00 24.96           C  
-ATOM   1435  CG2 ILE A 184      -2.038  72.251  36.428  1.00 18.17           C  
-ATOM   1436  CD1 ILE A 184      -3.305  74.277  39.507  1.00 14.49           C  
-ATOM   1437  N   GLN A 185      -4.221  73.716  34.451  1.00 30.40           N  
-ATOM   1438  CA  GLN A 185      -3.960  74.516  33.258  1.00 28.48           C  
-ATOM   1439  C   GLN A 185      -4.818  75.783  33.228  1.00 25.98           C  
-ATOM   1440  O   GLN A 185      -4.338  76.855  32.870  1.00 26.92           O  
-ATOM   1441  CB  GLN A 185      -4.216  73.682  31.998  1.00 29.22           C  
-ATOM   1442  CG  GLN A 185      -5.638  73.147  31.893  1.00 31.30           C  
-ATOM   1443  CD  GLN A 185      -5.843  72.216  30.713  1.00 35.20           C  
-ATOM   1444  OE1 GLN A 185      -5.554  71.026  30.794  1.00 31.92           O  
-ATOM   1445  NE2 GLN A 185      -6.376  72.750  29.621  1.00 35.62           N  
-ATOM   1446  N   PHE A 186      -6.074  75.662  33.649  1.00 28.18           N  
-ATOM   1447  CA  PHE A 186      -7.003  76.792  33.656  1.00 23.80           C  
-ATOM   1448  C   PHE A 186      -6.613  77.886  34.646  1.00 25.14           C  
-ATOM   1449  O   PHE A 186      -7.073  79.023  34.534  1.00 29.78           O  
-ATOM   1450  CB  PHE A 186      -8.426  76.295  33.913  1.00 18.41           C  
-ATOM   1451  CG  PHE A 186      -8.870  75.228  32.945  1.00 21.55           C  
-ATOM   1452  CD1 PHE A 186      -8.966  75.502  31.585  1.00 20.87           C  
-ATOM   1453  CD2 PHE A 186      -9.140  73.937  33.386  1.00 22.19           C  
-ATOM   1454  CE1 PHE A 186      -9.318  74.506  30.678  1.00 27.12           C  
-ATOM   1455  CE2 PHE A 186      -9.493  72.931  32.483  1.00 19.69           C  
-ATOM   1456  CZ  PHE A 186      -9.581  73.218  31.128  1.00 25.44           C  
-ATOM   1457  N   PHE A 187      -5.753  77.540  35.602  1.00 27.48           N  
-ATOM   1458  CA  PHE A 187      -5.275  78.495  36.602  1.00 24.88           C  
-ATOM   1459  C   PHE A 187      -3.886  79.015  36.218  1.00 26.26           C  
-ATOM   1460  O   PHE A 187      -3.236  79.707  37.004  1.00 29.32           O  
-ATOM   1461  CB  PHE A 187      -5.220  77.847  37.991  1.00 20.30           C  
-ATOM   1462  CG  PHE A 187      -6.558  77.398  38.509  1.00 18.82           C  
-ATOM   1463  CD1 PHE A 187      -7.069  76.151  38.166  1.00 16.71           C  
-ATOM   1464  CD2 PHE A 187      -7.306  78.221  39.345  1.00 20.50           C  
-ATOM   1465  CE1 PHE A 187      -8.306  75.728  38.647  1.00 20.66           C  
-ATOM   1466  CE2 PHE A 187      -8.546  77.807  39.832  1.00 19.67           C  
-ATOM   1467  CZ  PHE A 187      -9.046  76.559  39.482  1.00 20.01           C  
-ATOM   1468  N   GLY A 188      -3.433  78.668  35.014  1.00 23.50           N  
-ATOM   1469  CA  GLY A 188      -2.132  79.113  34.540  1.00 20.25           C  
-ATOM   1470  C   GLY A 188      -0.965  78.219  34.921  1.00 18.13           C  
-ATOM   1471  O   GLY A 188       0.197  78.592  34.757  1.00 20.19           O  
-ATOM   1472  N   GLY A 189      -1.278  77.037  35.436  1.00 17.51           N  
-ATOM   1473  CA  GLY A 189      -0.243  76.108  35.830  1.00 11.99           C  
-ATOM   1474  C   GLY A 189       0.093  75.142  34.715  1.00 15.83           C  
-ATOM   1475  O   GLY A 189      -0.743  74.851  33.860  1.00 16.79           O  
-ATOM   1476  N   ASP A 190       1.330  74.657  34.727  1.00 18.19           N  
-ATOM   1477  CA  ASP A 190       1.821  73.705  33.740  1.00 16.46           C  
-ATOM   1478  C   ASP A 190       1.671  72.279  34.295  1.00 20.01           C  
-ATOM   1479  O   ASP A 190       2.368  71.895  35.239  1.00 22.26           O  
-ATOM   1480  CB  ASP A 190       3.295  74.006  33.428  1.00 12.80           C  
-ATOM   1481  CG  ASP A 190       3.872  73.113  32.332  1.00 20.40           C  
-ATOM   1482  OD1 ASP A 190       3.111  72.344  31.703  1.00 16.21           O  
-ATOM   1483  OD2 ASP A 190       5.099  73.189  32.096  1.00 16.76           O  
-ATOM   1484  N   PRO A 191       0.760  71.479  33.714  1.00 23.21           N  
-ATOM   1485  CA  PRO A 191       0.516  70.098  34.148  1.00 20.39           C  
-ATOM   1486  C   PRO A 191       1.740  69.208  33.930  1.00 20.71           C  
-ATOM   1487  O   PRO A 191       1.856  68.147  34.545  1.00 22.18           O  
-ATOM   1488  CB  PRO A 191      -0.644  69.648  33.252  1.00 18.81           C  
-ATOM   1489  CG  PRO A 191      -1.295  70.926  32.827  1.00 26.62           C  
-ATOM   1490  CD  PRO A 191      -0.122  71.824  32.584  1.00 24.77           C  
-ATOM   1491  N   LYS A 192       2.627  69.642  33.035  1.00 21.79           N  
-ATOM   1492  CA  LYS A 192       3.853  68.914  32.704  1.00 22.19           C  
-ATOM   1493  C   LYS A 192       4.943  69.157  33.740  1.00 20.84           C  
-ATOM   1494  O   LYS A 192       5.919  68.410  33.815  1.00 21.38           O  
-ATOM   1495  CB  LYS A 192       4.399  69.359  31.341  1.00 22.12           C  
-ATOM   1496  CG  LYS A 192       3.418  69.300  30.187  1.00 32.49           C  
-ATOM   1497  CD  LYS A 192       4.103  69.634  28.862  1.00 35.10           C  
-ATOM   1498  CE  LYS A 192       4.663  71.054  28.825  1.00 38.44           C  
-ATOM   1499  NZ  LYS A 192       3.596  72.096  28.836  1.00 46.24           N  
-ATOM   1500  N   THR A 193       4.791  70.223  34.517  1.00 24.27           N  
-ATOM   1501  CA  THR A 193       5.785  70.567  35.519  1.00 25.96           C  
-ATOM   1502  C   THR A 193       5.164  70.735  36.900  1.00 20.38           C  
-ATOM   1503  O   THR A 193       5.101  71.841  37.439  1.00 19.88           O  
-ATOM   1504  CB  THR A 193       6.553  71.846  35.109  1.00 25.78           C  
-ATOM   1505  OG1 THR A 193       6.989  71.719  33.750  1.00 33.14           O  
-ATOM   1506  CG2 THR A 193       7.779  72.043  35.987  1.00 30.57           C  
-ATOM   1507  N   VAL A 194       4.717  69.616  37.466  1.00 15.87           N  
-ATOM   1508  CA  VAL A 194       4.112  69.594  38.793  1.00 15.85           C  
-ATOM   1509  C   VAL A 194       5.045  68.917  39.792  1.00 17.78           C  
-ATOM   1510  O   VAL A 194       5.409  67.752  39.625  1.00 18.71           O  
-ATOM   1511  CB  VAL A 194       2.761  68.834  38.799  1.00 19.83           C  
-ATOM   1512  CG1 VAL A 194       2.220  68.741  40.219  1.00  8.39           C  
-ATOM   1513  CG2 VAL A 194       1.751  69.528  37.896  1.00 17.89           C  
-ATOM   1514  N   THR A 195       5.456  69.661  40.812  1.00 17.88           N  
-ATOM   1515  CA  THR A 195       6.326  69.124  41.847  1.00 19.24           C  
-ATOM   1516  C   THR A 195       5.530  68.910  43.122  1.00 21.65           C  
-ATOM   1517  O   THR A 195       4.875  69.831  43.609  1.00 21.29           O  
-ATOM   1518  CB  THR A 195       7.500  70.075  42.159  1.00 12.90           C  
-ATOM   1519  OG1 THR A 195       8.389  70.113  41.039  1.00 21.31           O  
-ATOM   1520  CG2 THR A 195       8.275  69.596  43.385  1.00  8.74           C  
-ATOM   1521  N   ILE A 196       5.546  67.686  43.639  1.00 14.45           N  
-ATOM   1522  CA  ILE A 196       4.846  67.410  44.883  1.00 13.65           C  
-ATOM   1523  C   ILE A 196       5.848  67.455  46.027  1.00 11.94           C  
-ATOM   1524  O   ILE A 196       6.939  66.888  45.934  1.00  9.50           O  
-ATOM   1525  CB  ILE A 196       4.104  66.056  44.865  1.00 12.49           C  
-ATOM   1526  CG1 ILE A 196       5.084  64.888  44.761  1.00  8.83           C  
-ATOM   1527  CG2 ILE A 196       3.114  66.029  43.717  1.00 19.69           C  
-ATOM   1528  CD1 ILE A 196       4.422  63.538  44.941  1.00 10.07           C  
-ATOM   1529  N   PHE A 197       5.518  68.216  47.065  1.00 13.52           N  
-ATOM   1530  CA  PHE A 197       6.392  68.324  48.222  1.00 14.50           C  
-ATOM   1531  C   PHE A 197       5.613  68.258  49.522  1.00 16.87           C  
-ATOM   1532  O   PHE A 197       4.463  68.691  49.593  1.00 19.87           O  
-ATOM   1533  CB  PHE A 197       7.279  69.586  48.152  1.00 18.09           C  
-ATOM   1534  CG  PHE A 197       6.540  70.891  48.319  1.00 16.40           C  
-ATOM   1535  CD1 PHE A 197       5.376  71.159  47.607  1.00 20.89           C  
-ATOM   1536  CD2 PHE A 197       7.039  71.873  49.174  1.00 17.59           C  
-ATOM   1537  CE1 PHE A 197       4.720  72.385  47.745  1.00 18.52           C  
-ATOM   1538  CE2 PHE A 197       6.388  73.104  49.317  1.00 16.81           C  
-ATOM   1539  CZ  PHE A 197       5.227  73.358  48.600  1.00 10.18           C  
-ATOM   1540  N   GLY A 198       6.235  67.671  50.540  1.00 19.28           N  
-ATOM   1541  CA  GLY A 198       5.590  67.544  51.834  1.00 21.79           C  
-ATOM   1542  C   GLY A 198       6.587  67.344  52.956  1.00 23.25           C  
-ATOM   1543  O   GLY A 198       7.758  67.047  52.710  1.00 22.73           O  
-ATOM   1544  N   GLU A 199       6.123  67.501  54.192  1.00 21.01           N  
-ATOM   1545  CA  GLU A 199       6.985  67.341  55.356  1.00 21.95           C  
-ATOM   1546  C   GLU A 199       6.502  66.222  56.268  1.00 18.81           C  
-ATOM   1547  O   GLU A 199       5.305  66.053  56.475  1.00 22.78           O  
-ATOM   1548  CB  GLU A 199       7.075  68.663  56.131  1.00 23.02           C  
-ATOM   1549  CG  GLU A 199       8.063  68.665  57.296  1.00 18.30           C  
-ATOM   1550  CD  GLU A 199       7.457  68.215  58.623  1.00 22.54           C  
-ATOM   1551  OE1 GLU A 199       6.215  68.134  58.742  1.00 23.92           O  
-ATOM   1552  OE2 GLU A 199       8.232  67.950  59.561  1.00 17.75           O  
-ATOM   1553  N   SER A 200       7.458  65.481  56.820  1.00 15.00           N  
-ATOM   1554  CA  SER A 200       7.194  64.371  57.729  1.00 17.44           C  
-ATOM   1555  C   SER A 200       6.255  63.349  57.086  1.00 19.65           C  
-ATOM   1556  O   SER A 200       6.643  62.692  56.120  1.00 19.51           O  
-ATOM   1557  CB  SER A 200       6.646  64.899  59.060  1.00 10.27           C  
-ATOM   1558  OG  SER A 200       6.741  63.916  60.072  1.00 20.44           O  
-ATOM   1559  N   ALA A 201       5.033  63.209  57.608  1.00 18.62           N  
-ATOM   1560  CA  ALA A 201       4.065  62.268  57.044  1.00 17.57           C  
-ATOM   1561  C   ALA A 201       3.811  62.640  55.580  1.00 20.65           C  
-ATOM   1562  O   ALA A 201       3.552  61.773  54.744  1.00 21.76           O  
-ATOM   1563  CB  ALA A 201       2.756  62.301  57.841  1.00  8.30           C  
-ATOM   1564  N   GLY A 202       3.925  63.937  55.287  1.00 17.69           N  
-ATOM   1565  CA  GLY A 202       3.732  64.438  53.938  1.00 14.83           C  
-ATOM   1566  C   GLY A 202       4.894  64.067  53.039  1.00 16.77           C  
-ATOM   1567  O   GLY A 202       4.706  63.829  51.849  1.00 17.44           O  
-ATOM   1568  N   GLY A 203       6.098  64.032  53.609  1.00 19.15           N  
-ATOM   1569  CA  GLY A 203       7.289  63.670  52.857  1.00 13.03           C  
-ATOM   1570  C   GLY A 203       7.304  62.176  52.581  1.00 14.69           C  
-ATOM   1571  O   GLY A 203       7.840  61.724  51.570  1.00 19.25           O  
-ATOM   1572  N   ALA A 204       6.723  61.407  53.498  1.00 13.39           N  
-ATOM   1573  CA  ALA A 204       6.639  59.959  53.356  1.00 12.70           C  
-ATOM   1574  C   ALA A 204       5.625  59.676  52.253  1.00 15.24           C  
-ATOM   1575  O   ALA A 204       5.825  58.783  51.429  1.00 17.57           O  
-ATOM   1576  CB  ALA A 204       6.191  59.321  54.676  1.00  7.65           C  
-ATOM   1577  N   SER A 205       4.553  60.472  52.239  1.00 18.46           N  
-ATOM   1578  CA  SER A 205       3.485  60.369  51.247  1.00 18.01           C  
-ATOM   1579  C   SER A 205       4.056  60.596  49.851  1.00 20.77           C  
-ATOM   1580  O   SER A 205       3.740  59.860  48.915  1.00 21.35           O  
-ATOM   1581  CB  SER A 205       2.412  61.424  51.520  1.00 13.05           C  
-ATOM   1582  OG  SER A 205       1.717  61.168  52.727  1.00 16.44           O  
-ATOM   1583  N   VAL A 206       4.890  61.628  49.725  1.00 17.85           N  
-ATOM   1584  CA  VAL A 206       5.532  61.972  48.458  1.00 12.42           C  
-ATOM   1585  C   VAL A 206       6.317  60.765  47.956  1.00 17.44           C  
-ATOM   1586  O   VAL A 206       6.203  60.378  46.791  1.00 20.31           O  
-ATOM   1587  CB  VAL A 206       6.477  63.195  48.631  1.00 13.02           C  
-ATOM   1588  CG1 VAL A 206       7.336  63.403  47.391  1.00  3.81           C  
-ATOM   1589  CG2 VAL A 206       5.661  64.448  48.924  1.00  4.85           C  
-ATOM   1590  N   GLY A 207       7.080  60.154  48.860  1.00 18.50           N  
-ATOM   1591  CA  GLY A 207       7.868  58.984  48.516  1.00 18.81           C  
-ATOM   1592  C   GLY A 207       6.978  57.801  48.180  1.00 22.65           C  
-ATOM   1593  O   GLY A 207       7.348  56.947  47.374  1.00 22.95           O  
-ATOM   1594  N   MET A 208       5.800  57.752  48.795  1.00 22.78           N  
-ATOM   1595  CA  MET A 208       4.854  56.673  48.540  1.00 21.68           C  
-ATOM   1596  C   MET A 208       4.227  56.829  47.155  1.00 23.38           C  
-ATOM   1597  O   MET A 208       3.879  55.841  46.512  1.00 27.89           O  
-ATOM   1598  CB  MET A 208       3.785  56.622  49.633  1.00 15.58           C  
-ATOM   1599  CG  MET A 208       4.336  56.152  50.981  1.00 20.92           C  
-ATOM   1600  SD  MET A 208       3.163  56.233  52.346  1.00 19.24           S  
-ATOM   1601  CE  MET A 208       3.958  55.172  53.530  1.00 16.40           C  
-ATOM   1602  N   HIS A 209       4.110  58.070  46.688  1.00 22.97           N  
-ATOM   1603  CA  HIS A 209       3.551  58.330  45.368  1.00 18.38           C  
-ATOM   1604  C   HIS A 209       4.604  58.039  44.311  1.00 20.84           C  
-ATOM   1605  O   HIS A 209       4.270  57.731  43.167  1.00 19.41           O  
-ATOM   1606  CB  HIS A 209       3.059  59.773  45.260  1.00 15.41           C  
-ATOM   1607  CG  HIS A 209       1.816  60.042  46.052  1.00 20.20           C  
-ATOM   1608  ND1 HIS A 209       0.689  59.256  45.954  1.00 22.97           N  
-ATOM   1609  CD2 HIS A 209       1.529  61.002  46.961  1.00 22.16           C  
-ATOM   1610  CE1 HIS A 209      -0.242  59.718  46.769  1.00 18.24           C  
-ATOM   1611  NE2 HIS A 209       0.243  60.779  47.391  1.00 19.72           N  
-ATOM   1612  N   ILE A 210       5.874  58.142  44.702  1.00 20.50           N  
-ATOM   1613  CA  ILE A 210       6.987  57.858  43.802  1.00 13.30           C  
-ATOM   1614  C   ILE A 210       7.040  56.351  43.577  1.00 17.09           C  
-ATOM   1615  O   ILE A 210       7.353  55.887  42.481  1.00 20.34           O  
-ATOM   1616  CB  ILE A 210       8.335  58.335  44.404  1.00 15.02           C  
-ATOM   1617  CG1 ILE A 210       8.419  59.862  44.374  1.00  6.69           C  
-ATOM   1618  CG2 ILE A 210       9.519  57.719  43.656  1.00 14.14           C  
-ATOM   1619  CD1 ILE A 210       9.668  60.416  45.030  1.00 14.60           C  
-ATOM   1620  N   LEU A 211       6.701  55.598  44.620  1.00 21.46           N  
-ATOM   1621  CA  LEU A 211       6.708  54.139  44.570  1.00 21.12           C  
-ATOM   1622  C   LEU A 211       5.463  53.540  43.915  1.00 23.27           C  
-ATOM   1623  O   LEU A 211       5.565  52.613  43.113  1.00 24.34           O  
-ATOM   1624  CB  LEU A 211       6.867  53.563  45.981  1.00 16.49           C  
-ATOM   1625  CG  LEU A 211       8.198  53.771  46.710  1.00 16.44           C  
-ATOM   1626  CD1 LEU A 211       8.040  53.370  48.162  1.00 14.37           C  
-ATOM   1627  CD2 LEU A 211       9.302  52.966  46.056  1.00 17.71           C  
-ATOM   1628  N   SER A 212       4.294  54.071  44.256  1.00 25.97           N  
-ATOM   1629  CA  SER A 212       3.026  53.575  43.720  1.00 25.52           C  
-ATOM   1630  C   SER A 212       2.802  53.908  42.245  1.00 30.18           C  
-ATOM   1631  O   SER A 212       2.705  55.080  41.872  1.00 34.07           O  
-ATOM   1632  CB  SER A 212       1.861  54.114  44.551  1.00 20.64           C  
-ATOM   1633  OG  SER A 212       0.628  53.565  44.128  1.00 18.44           O  
-ATOM   1634  N   PRO A 213       2.689  52.871  41.391  1.00 30.98           N  
-ATOM   1635  CA  PRO A 213       2.470  53.033  39.947  1.00 28.07           C  
-ATOM   1636  C   PRO A 213       1.200  53.800  39.582  1.00 27.41           C  
-ATOM   1637  O   PRO A 213       1.142  54.454  38.539  1.00 29.71           O  
-ATOM   1638  CB  PRO A 213       2.437  51.587  39.440  1.00 27.89           C  
-ATOM   1639  CG  PRO A 213       2.032  50.792  40.643  1.00 31.04           C  
-ATOM   1640  CD  PRO A 213       2.822  51.446  41.737  1.00 25.82           C  
-ATOM   1641  N   GLY A 214       0.197  53.742  40.454  1.00 21.83           N  
-ATOM   1642  CA  GLY A 214      -1.043  54.449  40.199  1.00 17.63           C  
-ATOM   1643  C   GLY A 214      -0.940  55.937  40.477  1.00 21.65           C  
-ATOM   1644  O   GLY A 214      -1.896  56.677  40.251  1.00 21.69           O  
-ATOM   1645  N   SER A 215       0.223  56.383  40.948  1.00 20.46           N  
-ATOM   1646  CA  SER A 215       0.432  57.794  41.262  1.00 18.13           C  
-ATOM   1647  C   SER A 215       1.586  58.432  40.492  1.00 18.09           C  
-ATOM   1648  O   SER A 215       1.622  59.646  40.326  1.00 22.63           O  
-ATOM   1649  CB  SER A 215       0.684  57.970  42.765  1.00 20.15           C  
-ATOM   1650  OG  SER A 215      -0.401  57.502  43.544  1.00 18.81           O  
-ATOM   1651  N   ARG A 216       2.509  57.606  40.009  1.00 18.69           N  
-ATOM   1652  CA  ARG A 216       3.699  58.071  39.292  1.00 21.46           C  
-ATOM   1653  C   ARG A 216       3.496  59.047  38.138  1.00 23.09           C  
-ATOM   1654  O   ARG A 216       4.240  60.019  38.012  1.00 28.27           O  
-ATOM   1655  CB  ARG A 216       4.498  56.883  38.759  1.00 16.16           C  
-ATOM   1656  CG  ARG A 216       4.909  55.884  39.809  1.00 17.09           C  
-ATOM   1657  CD  ARG A 216       5.738  54.790  39.177  1.00 14.90           C  
-ATOM   1658  NE  ARG A 216       5.918  53.649  40.063  1.00 20.43           N  
-ATOM   1659  CZ  ARG A 216       6.424  52.482  39.680  1.00 24.63           C  
-ATOM   1660  NH1 ARG A 216       6.807  52.300  38.423  1.00 27.87           N  
-ATOM   1661  NH2 ARG A 216       6.538  51.494  40.551  1.00 23.09           N  
-ATOM   1662  N   ASP A 217       2.499  58.792  37.297  1.00 25.73           N  
-ATOM   1663  CA  ASP A 217       2.256  59.631  36.123  1.00 27.55           C  
-ATOM   1664  C   ASP A 217       1.621  60.985  36.392  1.00 24.58           C  
-ATOM   1665  O   ASP A 217       1.635  61.852  35.519  1.00 26.92           O  
-ATOM   1666  CB  ASP A 217       1.391  58.878  35.106  1.00 26.64           C  
-ATOM   1667  CG  ASP A 217       1.941  57.496  34.753  1.00 23.28           C  
-ATOM   1668  OD1 ASP A 217       3.063  57.131  35.175  1.00 19.87           O  
-ATOM   1669  OD2 ASP A 217       1.233  56.768  34.033  1.00 19.04           O  
-ATOM   1670  N   LEU A 218       1.088  61.170  37.596  1.00 23.19           N  
-ATOM   1671  CA  LEU A 218       0.411  62.411  37.959  1.00 19.47           C  
-ATOM   1672  C   LEU A 218       1.284  63.607  38.351  1.00 20.40           C  
-ATOM   1673  O   LEU A 218       0.764  64.705  38.558  1.00 21.38           O  
-ATOM   1674  CB  LEU A 218      -0.623  62.137  39.050  1.00 17.32           C  
-ATOM   1675  CG  LEU A 218      -1.662  61.068  38.710  1.00 23.30           C  
-ATOM   1676  CD1 LEU A 218      -2.557  60.833  39.912  1.00 25.32           C  
-ATOM   1677  CD2 LEU A 218      -2.484  61.481  37.492  1.00 20.94           C  
-ATOM   1678  N   PHE A 219       2.598  63.417  38.433  1.00 13.89           N  
-ATOM   1679  CA  PHE A 219       3.487  64.519  38.804  1.00 13.52           C  
-ATOM   1680  C   PHE A 219       4.852  64.390  38.141  1.00 10.05           C  
-ATOM   1681  O   PHE A 219       5.243  63.310  37.712  1.00 15.58           O  
-ATOM   1682  CB  PHE A 219       3.637  64.605  40.333  1.00 12.59           C  
-ATOM   1683  CG  PHE A 219       4.271  63.389  40.950  1.00 12.07           C  
-ATOM   1684  CD1 PHE A 219       3.514  62.252  41.210  1.00 13.46           C  
-ATOM   1685  CD2 PHE A 219       5.636  63.365  41.224  1.00  6.29           C  
-ATOM   1686  CE1 PHE A 219       4.109  61.104  41.730  1.00 14.08           C  
-ATOM   1687  CE2 PHE A 219       6.241  62.223  41.745  1.00  6.56           C  
-ATOM   1688  CZ  PHE A 219       5.477  61.090  41.996  1.00  5.33           C  
-ATOM   1689  N   ARG A 220       5.582  65.499  38.089  1.00 11.91           N  
-ATOM   1690  CA  ARG A 220       6.904  65.539  37.474  1.00 15.99           C  
-ATOM   1691  C   ARG A 220       8.031  65.207  38.445  1.00 24.07           C  
-ATOM   1692  O   ARG A 220       8.682  64.169  38.314  1.00 29.20           O  
-ATOM   1693  CB  ARG A 220       7.151  66.923  36.864  1.00 19.53           C  
-ATOM   1694  CG  ARG A 220       8.421  67.036  36.042  1.00 18.23           C  
-ATOM   1695  CD  ARG A 220       8.344  66.157  34.809  1.00 31.79           C  
-ATOM   1696  NE  ARG A 220       9.513  66.318  33.949  1.00 36.27           N  
-ATOM   1697  CZ  ARG A 220       9.675  67.307  33.075  1.00 35.81           C  
-ATOM   1698  NH1 ARG A 220       8.744  68.241  32.932  1.00 34.37           N  
-ATOM   1699  NH2 ARG A 220      10.775  67.353  32.336  1.00 29.53           N  
-ATOM   1700  N   ARG A 221       8.266  66.108  39.400  1.00 23.78           N  
-ATOM   1701  CA  ARG A 221       9.326  65.953  40.395  1.00 16.67           C  
-ATOM   1702  C   ARG A 221       8.779  65.862  41.818  1.00 17.64           C  
-ATOM   1703  O   ARG A 221       7.570  65.963  42.033  1.00 16.68           O  
-ATOM   1704  CB  ARG A 221      10.304  67.122  40.295  1.00 16.46           C  
-ATOM   1705  CG  ARG A 221      11.218  67.063  39.097  1.00 24.36           C  
-ATOM   1706  CD  ARG A 221      12.064  68.316  38.984  1.00 23.73           C  
-ATOM   1707  NE  ARG A 221      11.442  69.317  38.122  1.00 31.95           N  
-ATOM   1708  CZ  ARG A 221      11.508  69.307  36.793  1.00 27.81           C  
-ATOM   1709  NH1 ARG A 221      12.174  68.353  36.160  1.00 20.32           N  
-ATOM   1710  NH2 ARG A 221      10.892  70.247  36.090  1.00 34.51           N  
-ATOM   1711  N   ALA A 222       9.677  65.707  42.791  1.00 14.67           N  
-ATOM   1712  CA  ALA A 222       9.266  65.587  44.184  1.00 20.02           C  
-ATOM   1713  C   ALA A 222      10.286  66.083  45.202  1.00 22.53           C  
-ATOM   1714  O   ALA A 222      11.498  65.988  44.992  1.00 18.38           O  
-ATOM   1715  CB  ALA A 222       8.895  64.142  44.486  1.00 21.98           C  
-ATOM   1716  N   ILE A 223       9.767  66.618  46.307  1.00 21.01           N  
-ATOM   1717  CA  ILE A 223      10.582  67.123  47.412  1.00 19.40           C  
-ATOM   1718  C   ILE A 223      10.098  66.485  48.719  1.00 17.50           C  
-ATOM   1719  O   ILE A 223       8.907  66.526  49.042  1.00 15.13           O  
-ATOM   1720  CB  ILE A 223      10.500  68.666  47.527  1.00 17.96           C  
-ATOM   1721  CG1 ILE A 223      11.114  69.324  46.292  1.00 12.69           C  
-ATOM   1722  CG2 ILE A 223      11.217  69.149  48.784  1.00 11.21           C  
-ATOM   1723  CD1 ILE A 223      10.981  70.826  46.279  1.00 12.60           C  
-ATOM   1724  N   LEU A 224      11.024  65.874  49.450  1.00 12.53           N  
-ATOM   1725  CA  LEU A 224      10.704  65.219  50.713  1.00 10.23           C  
-ATOM   1726  C   LEU A 224      11.436  65.883  51.880  1.00 10.81           C  
-ATOM   1727  O   LEU A 224      12.662  65.882  51.936  1.00 11.49           O  
-ATOM   1728  CB  LEU A 224      11.064  63.731  50.653  1.00  8.29           C  
-ATOM   1729  CG  LEU A 224      10.439  62.842  49.573  1.00  8.98           C  
-ATOM   1730  CD1 LEU A 224      11.063  63.111  48.214  1.00  3.61           C  
-ATOM   1731  CD2 LEU A 224      10.654  61.394  49.955  1.00  4.94           C  
-ATOM   1732  N   GLN A 225      10.674  66.443  52.815  1.00 16.49           N  
-ATOM   1733  CA  GLN A 225      11.243  67.116  53.981  1.00 12.93           C  
-ATOM   1734  C   GLN A 225      11.009  66.320  55.268  1.00 19.11           C  
-ATOM   1735  O   GLN A 225       9.864  66.073  55.651  1.00 16.43           O  
-ATOM   1736  CB  GLN A 225      10.625  68.511  54.122  1.00 17.71           C  
-ATOM   1737  CG  GLN A 225      10.878  69.430  52.931  1.00 20.66           C  
-ATOM   1738  CD  GLN A 225       9.972  70.649  52.922  1.00 22.73           C  
-ATOM   1739  OE1 GLN A 225       9.462  71.042  51.875  1.00 27.90           O  
-ATOM   1740  NE2 GLN A 225       9.766  71.250  54.089  1.00 22.00           N  
-ATOM   1741  N   SER A 226      12.099  65.911  55.917  1.00 16.14           N  
-ATOM   1742  CA  SER A 226      12.034  65.159  57.172  1.00 16.30           C  
-ATOM   1743  C   SER A 226      11.074  63.977  57.104  1.00 16.97           C  
-ATOM   1744  O   SER A 226      10.362  63.689  58.066  1.00 20.43           O  
-ATOM   1745  CB  SER A 226      11.612  66.086  58.318  1.00 13.29           C  
-ATOM   1746  OG  SER A 226      12.473  67.206  58.427  1.00  9.35           O  
-ATOM   1747  N   GLY A 227      11.064  63.291  55.966  1.00 17.69           N  
-ATOM   1748  CA  GLY A 227      10.174  62.156  55.798  1.00 13.10           C  
-ATOM   1749  C   GLY A 227      10.601  61.249  54.666  1.00 17.04           C  
-ATOM   1750  O   GLY A 227      11.161  61.699  53.663  1.00 16.68           O  
-ATOM   1751  N   SER A 228      10.290  59.965  54.812  1.00 17.59           N  
-ATOM   1752  CA  SER A 228      10.659  58.962  53.820  1.00 16.13           C  
-ATOM   1753  C   SER A 228       9.589  57.870  53.819  1.00 13.91           C  
-ATOM   1754  O   SER A 228       8.968  57.607  54.848  1.00 14.72           O  
-ATOM   1755  CB  SER A 228      12.019  58.367  54.201  1.00 11.08           C  
-ATOM   1756  OG  SER A 228      12.594  57.661  53.129  1.00 26.61           O  
-ATOM   1757  N   PRO A 229       9.334  57.241  52.660  1.00 18.09           N  
-ATOM   1758  CA  PRO A 229       8.310  56.190  52.640  1.00 21.36           C  
-ATOM   1759  C   PRO A 229       8.626  54.986  53.531  1.00 18.14           C  
-ATOM   1760  O   PRO A 229       7.719  54.370  54.081  1.00 17.84           O  
-ATOM   1761  CB  PRO A 229       8.239  55.809  51.156  1.00 18.68           C  
-ATOM   1762  CG  PRO A 229       9.604  56.158  50.635  1.00 17.05           C  
-ATOM   1763  CD  PRO A 229       9.873  57.476  51.309  1.00 13.01           C  
-ATOM   1764  N   ASN A 230       9.912  54.708  53.726  1.00 18.82           N  
-ATOM   1765  CA  ASN A 230      10.350  53.573  54.537  1.00 16.63           C  
-ATOM   1766  C   ASN A 230      10.541  53.850  56.032  1.00 17.00           C  
-ATOM   1767  O   ASN A 230      11.219  53.084  56.721  1.00 23.35           O  
-ATOM   1768  CB  ASN A 230      11.646  52.999  53.964  1.00 14.36           C  
-ATOM   1769  CG  ASN A 230      12.779  54.010  53.964  1.00 15.11           C  
-ATOM   1770  OD1 ASN A 230      12.617  55.130  53.493  1.00 11.05           O  
-ATOM   1771  ND2 ASN A 230      13.925  53.622  54.515  1.00 18.17           N  
-ATOM   1772  N   CYS A 231       9.975  54.944  56.534  1.00 16.52           N  
-ATOM   1773  CA  CYS A 231      10.097  55.268  57.955  1.00 17.47           C  
-ATOM   1774  C   CYS A 231       9.372  54.205  58.777  1.00 19.49           C  
-ATOM   1775  O   CYS A 231       8.265  53.792  58.429  1.00 18.07           O  
-ATOM   1776  CB  CYS A 231       9.520  56.654  58.250  1.00 14.46           C  
-ATOM   1777  SG  CYS A 231      10.593  58.029  57.751  1.00 18.24           S  
-ATOM   1778  N   PRO A 232       9.988  53.752  59.884  1.00 18.85           N  
-ATOM   1779  CA  PRO A 232       9.394  52.725  60.753  1.00 16.50           C  
-ATOM   1780  C   PRO A 232       7.964  52.997  61.228  1.00 16.97           C  
-ATOM   1781  O   PRO A 232       7.236  52.066  61.578  1.00 20.41           O  
-ATOM   1782  CB  PRO A 232      10.387  52.645  61.922  1.00 13.20           C  
-ATOM   1783  CG  PRO A 232      11.053  53.994  61.920  1.00 17.13           C  
-ATOM   1784  CD  PRO A 232      11.251  54.251  60.451  1.00 11.61           C  
-ATOM   1785  N   TRP A 233       7.558  54.263  61.197  1.00 17.57           N  
-ATOM   1786  CA  TRP A 233       6.222  54.686  61.623  1.00 13.49           C  
-ATOM   1787  C   TRP A 233       5.265  54.958  60.454  1.00 14.76           C  
-ATOM   1788  O   TRP A 233       4.059  55.089  60.651  1.00 18.32           O  
-ATOM   1789  CB  TRP A 233       6.348  55.959  62.466  1.00  9.50           C  
-ATOM   1790  CG  TRP A 233       7.149  57.040  61.781  1.00  9.96           C  
-ATOM   1791  CD1 TRP A 233       8.489  57.277  61.917  1.00 14.61           C  
-ATOM   1792  CD2 TRP A 233       6.674  57.984  60.811  1.00 13.60           C  
-ATOM   1793  NE1 TRP A 233       8.877  58.299  61.086  1.00 15.16           N  
-ATOM   1794  CE2 TRP A 233       7.787  58.754  60.395  1.00 13.08           C  
-ATOM   1795  CE3 TRP A 233       5.416  58.254  60.249  1.00 10.88           C  
-ATOM   1796  CZ2 TRP A 233       7.682  59.774  59.444  1.00 14.14           C  
-ATOM   1797  CZ3 TRP A 233       5.312  59.269  59.302  1.00 12.14           C  
-ATOM   1798  CH2 TRP A 233       6.442  60.017  58.910  1.00 13.51           C  
-ATOM   1799  N   ALA A 234       5.813  55.065  59.247  1.00 14.86           N  
-ATOM   1800  CA  ALA A 234       5.028  55.370  58.050  1.00 14.76           C  
-ATOM   1801  C   ALA A 234       4.055  54.308  57.556  1.00 14.99           C  
-ATOM   1802  O   ALA A 234       3.075  54.642  56.898  1.00 17.29           O  
-ATOM   1803  CB  ALA A 234       5.953  55.803  56.915  1.00 16.87           C  
-ATOM   1804  N   SER A 235       4.313  53.037  57.857  1.00 19.26           N  
-ATOM   1805  CA  SER A 235       3.418  51.970  57.404  1.00 18.31           C  
-ATOM   1806  C   SER A 235       3.417  50.708  58.261  1.00 21.31           C  
-ATOM   1807  O   SER A 235       4.326  50.475  59.060  1.00 21.73           O  
-ATOM   1808  CB  SER A 235       3.737  51.584  55.958  1.00 16.50           C  
-ATOM   1809  OG  SER A 235       5.007  50.968  55.863  1.00 13.24           O  
-ATOM   1810  N   VAL A 236       2.375  49.900  58.079  1.00 21.17           N  
-ATOM   1811  CA  VAL A 236       2.214  48.640  58.800  1.00 21.93           C  
-ATOM   1812  C   VAL A 236       1.749  47.546  57.838  1.00 23.89           C  
-ATOM   1813  O   VAL A 236       1.281  47.830  56.732  1.00 24.31           O  
-ATOM   1814  CB  VAL A 236       1.180  48.753  59.962  1.00 21.45           C  
-ATOM   1815  CG1 VAL A 236       1.661  49.735  61.012  1.00 19.52           C  
-ATOM   1816  CG2 VAL A 236      -0.192  49.166  59.430  1.00 10.99           C  
-ATOM   1817  N   SER A 237       1.896  46.294  58.258  1.00 27.93           N  
-ATOM   1818  CA  SER A 237       1.484  45.154  57.445  1.00 24.82           C  
-ATOM   1819  C   SER A 237      -0.040  45.076  57.429  1.00 27.58           C  
-ATOM   1820  O   SER A 237      -0.710  45.805  58.166  1.00 30.87           O  
-ATOM   1821  CB  SER A 237       2.067  43.857  58.017  1.00 19.45           C  
-ATOM   1822  OG  SER A 237       1.606  43.624  59.336  1.00 22.87           O  
-ATOM   1823  N   VAL A 238      -0.588  44.200  56.588  1.00 26.24           N  
-ATOM   1824  CA  VAL A 238      -2.040  44.043  56.509  1.00 25.00           C  
-ATOM   1825  C   VAL A 238      -2.574  43.363  57.765  1.00 19.62           C  
-ATOM   1826  O   VAL A 238      -3.682  43.655  58.208  1.00 25.33           O  
-ATOM   1827  CB  VAL A 238      -2.482  43.252  55.247  1.00 23.24           C  
-ATOM   1828  CG1 VAL A 238      -2.128  44.030  53.991  1.00 26.49           C  
-ATOM   1829  CG2 VAL A 238      -1.832  41.886  55.214  1.00 27.48           C  
-ATOM   1830  N   ALA A 239      -1.769  42.472  58.342  1.00 19.01           N  
-ATOM   1831  CA  ALA A 239      -2.144  41.756  59.556  1.00 19.21           C  
-ATOM   1832  C   ALA A 239      -2.197  42.730  60.727  1.00 23.64           C  
-ATOM   1833  O   ALA A 239      -3.151  42.718  61.506  1.00 25.18           O  
-ATOM   1834  CB  ALA A 239      -1.149  40.639  59.845  1.00 18.24           C  
-ATOM   1835  N   GLU A 240      -1.176  43.580  60.839  1.00 25.19           N  
-ATOM   1836  CA  GLU A 240      -1.118  44.571  61.911  1.00 23.48           C  
-ATOM   1837  C   GLU A 240      -2.226  45.616  61.755  1.00 23.53           C  
-ATOM   1838  O   GLU A 240      -2.828  46.048  62.742  1.00 18.96           O  
-ATOM   1839  CB  GLU A 240       0.257  45.246  61.945  1.00 19.61           C  
-ATOM   1840  CG  GLU A 240       0.407  46.350  62.995  1.00 21.31           C  
-ATOM   1841  CD  GLU A 240       0.241  45.871  64.435  1.00 23.61           C  
-ATOM   1842  OE1 GLU A 240       0.112  44.653  64.679  1.00 29.21           O  
-ATOM   1843  OE2 GLU A 240       0.246  46.729  65.339  1.00 28.73           O  
-ATOM   1844  N   GLY A 241      -2.492  46.006  60.510  1.00 22.07           N  
-ATOM   1845  CA  GLY A 241      -3.537  46.976  60.237  1.00 25.97           C  
-ATOM   1846  C   GLY A 241      -4.882  46.408  60.650  1.00 26.14           C  
-ATOM   1847  O   GLY A 241      -5.715  47.103  61.228  1.00 21.96           O  
-ATOM   1848  N   ARG A 242      -5.072  45.122  60.373  1.00 24.93           N  
-ATOM   1849  CA  ARG A 242      -6.301  44.425  60.718  1.00 24.28           C  
-ATOM   1850  C   ARG A 242      -6.428  44.346  62.235  1.00 27.04           C  
-ATOM   1851  O   ARG A 242      -7.466  44.699  62.796  1.00 26.62           O  
-ATOM   1852  CB  ARG A 242      -6.284  43.022  60.112  1.00 25.74           C  
-ATOM   1853  CG  ARG A 242      -7.391  42.111  60.597  1.00 33.78           C  
-ATOM   1854  CD  ARG A 242      -7.494  40.876  59.722  1.00 36.51           C  
-ATOM   1855  NE  ARG A 242      -8.026  41.193  58.396  1.00 30.36           N  
-ATOM   1856  CZ  ARG A 242      -9.314  41.398  58.133  1.00 33.06           C  
-ATOM   1857  NH1 ARG A 242     -10.215  41.315  59.104  1.00 25.97           N  
-ATOM   1858  NH2 ARG A 242      -9.702  41.683  56.897  1.00 23.71           N  
-ATOM   1859  N   ARG A 243      -5.345  43.929  62.888  1.00 25.99           N  
-ATOM   1860  CA  ARG A 243      -5.299  43.797  64.341  1.00 27.20           C  
-ATOM   1861  C   ARG A 243      -5.707  45.107  65.017  1.00 26.19           C  
-ATOM   1862  O   ARG A 243      -6.480  45.099  65.976  1.00 26.76           O  
-ATOM   1863  CB  ARG A 243      -3.884  43.420  64.777  1.00 32.03           C  
-ATOM   1864  CG  ARG A 243      -3.802  42.686  66.097  1.00 31.59           C  
-ATOM   1865  CD  ARG A 243      -2.662  43.215  66.946  1.00 29.88           C  
-ATOM   1866  NE  ARG A 243      -3.107  44.286  67.837  1.00 38.47           N  
-ATOM   1867  CZ  ARG A 243      -2.532  45.479  67.928  1.00 30.09           C  
-ATOM   1868  NH1 ARG A 243      -1.481  45.774  67.181  1.00 39.54           N  
-ATOM   1869  NH2 ARG A 243      -2.997  46.373  68.786  1.00 37.58           N  
-ATOM   1870  N   ARG A 244      -5.190  46.224  64.502  1.00 22.72           N  
-ATOM   1871  CA  ARG A 244      -5.496  47.549  65.041  1.00 21.72           C  
-ATOM   1872  C   ARG A 244      -6.939  47.962  64.785  1.00 20.51           C  
-ATOM   1873  O   ARG A 244      -7.536  48.665  65.596  1.00 24.33           O  
-ATOM   1874  CB  ARG A 244      -4.552  48.609  64.461  1.00 15.12           C  
-ATOM   1875  CG  ARG A 244      -3.106  48.435  64.859  1.00 15.02           C  
-ATOM   1876  CD  ARG A 244      -2.233  49.571  64.356  1.00 10.08           C  
-ATOM   1877  NE  ARG A 244      -0.821  49.265  64.566  1.00 10.68           N  
-ATOM   1878  CZ  ARG A 244       0.178  50.135  64.456  1.00 13.22           C  
-ATOM   1879  NH1 ARG A 244      -0.053  51.401  64.134  1.00 11.08           N  
-ATOM   1880  NH2 ARG A 244       1.419  49.728  64.662  1.00 10.98           N  
-ATOM   1881  N   ALA A 245      -7.481  47.547  63.644  1.00 21.22           N  
-ATOM   1882  CA  ALA A 245      -8.857  47.869  63.283  1.00 19.32           C  
-ATOM   1883  C   ALA A 245      -9.825  47.132  64.201  1.00 24.67           C  
-ATOM   1884  O   ALA A 245     -10.804  47.711  64.676  1.00 25.82           O  
-ATOM   1885  CB  ALA A 245      -9.117  47.505  61.837  1.00 28.10           C  
-ATOM   1886  N   VAL A 246      -9.534  45.856  64.457  1.00 25.52           N  
-ATOM   1887  CA  VAL A 246     -10.354  45.030  65.335  1.00 26.57           C  
-ATOM   1888  C   VAL A 246     -10.255  45.561  66.769  1.00 31.87           C  
-ATOM   1889  O   VAL A 246     -11.249  45.577  67.502  1.00 36.00           O  
-ATOM   1890  CB  VAL A 246      -9.899  43.552  65.304  1.00 31.28           C  
-ATOM   1891  CG1 VAL A 246     -10.720  42.720  66.280  1.00 29.98           C  
-ATOM   1892  CG2 VAL A 246     -10.035  42.992  63.895  1.00 31.13           C  
-ATOM   1893  N   GLU A 247      -9.061  46.014  67.150  1.00 25.10           N  
-ATOM   1894  CA  GLU A 247      -8.837  46.555  68.485  1.00 29.27           C  
-ATOM   1895  C   GLU A 247      -9.621  47.853  68.658  1.00 28.29           C  
-ATOM   1896  O   GLU A 247     -10.154  48.126  69.734  1.00 33.22           O  
-ATOM   1897  CB  GLU A 247      -7.343  46.794  68.730  1.00 29.71           C  
-ATOM   1898  CG  GLU A 247      -6.978  47.096  70.188  1.00 33.44           C  
-ATOM   1899  CD  GLU A 247      -7.361  45.975  71.151  1.00 40.76           C  
-ATOM   1900  OE1 GLU A 247      -7.394  44.795  70.735  1.00 42.69           O  
-ATOM   1901  OE2 GLU A 247      -7.625  46.276  72.334  1.00 40.57           O  
-ATOM   1902  N   LEU A 248      -9.717  48.637  67.588  1.00 25.62           N  
-ATOM   1903  CA  LEU A 248     -10.458  49.891  67.639  1.00 25.27           C  
-ATOM   1904  C   LEU A 248     -11.922  49.567  67.897  1.00 26.55           C  
-ATOM   1905  O   LEU A 248     -12.603  50.277  68.638  1.00 30.48           O  
-ATOM   1906  CB  LEU A 248     -10.320  50.661  66.322  1.00 23.25           C  
-ATOM   1907  CG  LEU A 248     -11.006  52.030  66.271  1.00 20.07           C  
-ATOM   1908  CD1 LEU A 248     -10.304  52.998  67.213  1.00 26.04           C  
-ATOM   1909  CD2 LEU A 248     -10.997  52.571  64.847  1.00 19.56           C  
-ATOM   1910  N   GLY A 249     -12.385  48.471  67.299  1.00 27.03           N  
-ATOM   1911  CA  GLY A 249     -13.764  48.051  67.468  1.00 28.97           C  
-ATOM   1912  C   GLY A 249     -14.050  47.570  68.876  1.00 27.39           C  
-ATOM   1913  O   GLY A 249     -15.111  47.854  69.434  1.00 25.72           O  
-ATOM   1914  N   ARG A 250     -13.091  46.858  69.456  1.00 27.19           N  
-ATOM   1915  CA  ARG A 250     -13.230  46.335  70.809  1.00 32.18           C  
-ATOM   1916  C   ARG A 250     -13.351  47.485  71.808  1.00 32.40           C  
-ATOM   1917  O   ARG A 250     -14.067  47.380  72.804  1.00 37.98           O  
-ATOM   1918  CB  ARG A 250     -12.015  45.482  71.161  1.00 37.63           C  
-ATOM   1919  CG  ARG A 250     -12.311  44.320  72.088  1.00 45.45           C  
-ATOM   1920  CD  ARG A 250     -11.025  43.629  72.512  1.00 53.22           C  
-ATOM   1921  NE  ARG A 250     -10.124  43.376  71.388  1.00 64.96           N  
-ATOM   1922  CZ  ARG A 250     -10.086  42.249  70.681  1.00 67.17           C  
-ATOM   1923  NH1 ARG A 250     -10.902  41.241  70.967  1.00 64.48           N  
-ATOM   1924  NH2 ARG A 250      -9.213  42.123  69.692  1.00 67.47           N  
-ATOM   1925  N   ASN A 251     -12.655  48.585  71.525  1.00 32.30           N  
-ATOM   1926  CA  ASN A 251     -12.672  49.768  72.385  1.00 28.56           C  
-ATOM   1927  C   ASN A 251     -14.001  50.512  72.340  1.00 29.74           C  
-ATOM   1928  O   ASN A 251     -14.306  51.302  73.233  1.00 28.54           O  
-ATOM   1929  CB  ASN A 251     -11.543  50.730  71.989  1.00 29.83           C  
-ATOM   1930  CG  ASN A 251     -10.212  50.380  72.638  1.00 24.66           C  
-ATOM   1931  OD1 ASN A 251      -9.753  51.078  73.535  1.00 23.72           O  
-ATOM   1932  ND2 ASN A 251      -9.596  49.294  72.194  1.00 20.11           N  
-ATOM   1933  N   LEU A 252     -14.786  50.257  71.298  1.00 34.81           N  
-ATOM   1934  CA  LEU A 252     -16.074  50.917  71.121  1.00 37.37           C  
-ATOM   1935  C   LEU A 252     -17.275  49.981  71.244  1.00 39.70           C  
-ATOM   1936  O   LEU A 252     -18.380  50.319  70.813  1.00 44.22           O  
-ATOM   1937  CB  LEU A 252     -16.093  51.642  69.775  1.00 29.68           C  
-ATOM   1938  CG  LEU A 252     -15.126  52.825  69.682  1.00 29.01           C  
-ATOM   1939  CD1 LEU A 252     -14.907  53.226  68.235  1.00 25.46           C  
-ATOM   1940  CD2 LEU A 252     -15.659  53.990  70.503  1.00 27.29           C  
-ATOM   1941  N   ASN A 253     -17.051  48.820  71.862  1.00 43.51           N  
-ATOM   1942  CA  ASN A 253     -18.090  47.811  72.079  1.00 45.01           C  
-ATOM   1943  C   ASN A 253     -18.782  47.409  70.777  1.00 45.11           C  
-ATOM   1944  O   ASN A 253     -20.011  47.430  70.679  1.00 49.74           O  
-ATOM   1945  CB  ASN A 253     -19.121  48.316  73.098  1.00 49.76           C  
-ATOM   1946  CG  ASN A 253     -18.476  48.854  74.367  1.00 57.71           C  
-ATOM   1947  OD1 ASN A 253     -18.794  49.958  74.815  1.00 60.00           O  
-ATOM   1948  ND2 ASN A 253     -17.558  48.082  74.945  1.00 57.23           N  
-ATOM   1949  N   CYS A 254     -17.980  47.058  69.777  1.00 41.11           N  
-ATOM   1950  CA  CYS A 254     -18.496  46.654  68.474  1.00 38.44           C  
-ATOM   1951  C   CYS A 254     -18.615  45.145  68.342  1.00 40.09           C  
-ATOM   1952  O   CYS A 254     -18.042  44.388  69.131  1.00 39.53           O  
-ATOM   1953  CB  CYS A 254     -17.582  47.151  67.344  1.00 39.82           C  
-ATOM   1954  SG  CYS A 254     -17.609  48.936  66.984  1.00 37.78           S  
-ATOM   1955  N   ASN A 255     -19.358  44.725  67.322  1.00 40.23           N  
-ATOM   1956  CA  ASN A 255     -19.538  43.314  67.018  1.00 43.33           C  
-ATOM   1957  C   ASN A 255     -18.310  42.960  66.185  1.00 41.73           C  
-ATOM   1958  O   ASN A 255     -18.054  43.592  65.163  1.00 43.38           O  
-ATOM   1959  CB  ASN A 255     -20.812  43.113  66.197  1.00 46.81           C  
-ATOM   1960  CG  ASN A 255     -21.162  41.651  66.017  1.00 47.23           C  
-ATOM   1961  OD1 ASN A 255     -20.563  40.957  65.198  1.00 54.70           O  
-ATOM   1962  ND2 ASN A 255     -22.128  41.174  66.789  1.00 46.87           N  
-ATOM   1963  N   LEU A 256     -17.548  41.963  66.623  1.00 40.57           N  
-ATOM   1964  CA  LEU A 256     -16.327  41.584  65.917  1.00 41.72           C  
-ATOM   1965  C   LEU A 256     -16.388  40.255  65.164  1.00 46.82           C  
-ATOM   1966  O   LEU A 256     -15.350  39.717  64.770  1.00 49.80           O  
-ATOM   1967  CB  LEU A 256     -15.155  41.556  66.907  1.00 41.19           C  
-ATOM   1968  CG  LEU A 256     -14.954  42.772  67.822  1.00 40.05           C  
-ATOM   1969  CD1 LEU A 256     -13.869  42.469  68.842  1.00 35.13           C  
-ATOM   1970  CD2 LEU A 256     -14.606  44.010  67.010  1.00 33.51           C  
-ATOM   1971  N   ASN A 257     -17.595  39.746  64.930  1.00 50.63           N  
-ATOM   1972  CA  ASN A 257     -17.770  38.467  64.235  1.00 52.72           C  
-ATOM   1973  C   ASN A 257     -17.434  38.493  62.747  1.00 50.09           C  
-ATOM   1974  O   ASN A 257     -17.153  37.452  62.151  1.00 47.34           O  
-ATOM   1975  CB  ASN A 257     -19.195  37.944  64.428  1.00 57.90           C  
-ATOM   1976  CG  ASN A 257     -19.528  37.681  65.885  1.00 63.29           C  
-ATOM   1977  OD1 ASN A 257     -18.671  37.262  66.669  1.00 58.98           O  
-ATOM   1978  ND2 ASN A 257     -20.783  37.923  66.257  1.00 64.03           N  
-ATOM   1979  N   SER A 258     -17.462  39.681  62.152  1.00 48.70           N  
-ATOM   1980  CA  SER A 258     -17.161  39.834  60.734  1.00 43.66           C  
-ATOM   1981  C   SER A 258     -16.716  41.255  60.437  1.00 42.13           C  
-ATOM   1982  O   SER A 258     -16.906  42.159  61.253  1.00 40.37           O  
-ATOM   1983  CB  SER A 258     -18.401  39.521  59.896  1.00 42.43           C  
-ATOM   1984  OG  SER A 258     -19.432  40.460  60.155  1.00 38.43           O  
-ATOM   1985  N   ASP A 259     -16.128  41.446  59.261  1.00 42.47           N  
-ATOM   1986  CA  ASP A 259     -15.679  42.766  58.838  1.00 42.47           C  
-ATOM   1987  C   ASP A 259     -16.885  43.647  58.550  1.00 43.85           C  
-ATOM   1988  O   ASP A 259     -16.889  44.826  58.895  1.00 46.13           O  
-ATOM   1989  CB  ASP A 259     -14.800  42.669  57.589  1.00 42.19           C  
-ATOM   1990  CG  ASP A 259     -13.431  42.078  57.874  1.00 48.87           C  
-ATOM   1991  OD1 ASP A 259     -13.140  41.743  59.045  1.00 56.86           O  
-ATOM   1992  OD2 ASP A 259     -12.637  41.956  56.918  1.00 50.00           O  
-ATOM   1993  N   GLU A 260     -17.911  43.059  57.934  1.00 48.78           N  
-ATOM   1994  CA  GLU A 260     -19.139  43.780  57.595  1.00 48.95           C  
-ATOM   1995  C   GLU A 260     -19.798  44.372  58.835  1.00 46.05           C  
-ATOM   1996  O   GLU A 260     -20.415  45.438  58.769  1.00 49.03           O  
-ATOM   1997  CB  GLU A 260     -20.137  42.863  56.876  1.00 54.61           C  
-ATOM   1998  CG  GLU A 260     -19.790  42.525  55.422  1.00 68.29           C  
-ATOM   1999  CD  GLU A 260     -18.600  41.583  55.280  1.00 76.81           C  
-ATOM   2000  OE1 GLU A 260     -18.474  40.638  56.090  1.00 76.80           O  
-ATOM   2001  OE2 GLU A 260     -17.797  41.781  54.342  1.00 81.15           O  
-ATOM   2002  N   GLU A 261     -19.655  43.682  59.964  1.00 42.76           N  
-ATOM   2003  CA  GLU A 261     -20.239  44.149  61.214  1.00 44.95           C  
-ATOM   2004  C   GLU A 261     -19.347  45.116  61.981  1.00 42.82           C  
-ATOM   2005  O   GLU A 261     -19.847  45.984  62.700  1.00 40.10           O  
-ATOM   2006  CB  GLU A 261     -20.642  42.973  62.100  1.00 52.79           C  
-ATOM   2007  CG  GLU A 261     -21.844  42.215  61.568  1.00 60.90           C  
-ATOM   2008  CD  GLU A 261     -22.502  41.359  62.623  1.00 62.12           C  
-ATOM   2009  OE1 GLU A 261     -23.367  41.887  63.357  1.00 61.56           O  
-ATOM   2010  OE2 GLU A 261     -22.156  40.162  62.718  1.00 64.64           O  
-ATOM   2011  N   LEU A 262     -18.033  44.964  61.834  1.00 39.42           N  
-ATOM   2012  CA  LEU A 262     -17.085  45.852  62.500  1.00 32.30           C  
-ATOM   2013  C   LEU A 262     -17.196  47.239  61.880  1.00 29.91           C  
-ATOM   2014  O   LEU A 262     -17.357  48.233  62.590  1.00 28.66           O  
-ATOM   2015  CB  LEU A 262     -15.653  45.326  62.348  1.00 30.76           C  
-ATOM   2016  CG  LEU A 262     -14.522  46.213  62.881  1.00 20.45           C  
-ATOM   2017  CD1 LEU A 262     -14.770  46.579  64.330  1.00 15.25           C  
-ATOM   2018  CD2 LEU A 262     -13.194  45.490  62.738  1.00 24.48           C  
-ATOM   2019  N   ILE A 263     -17.157  47.281  60.549  1.00 26.83           N  
-ATOM   2020  CA  ILE A 263     -17.249  48.524  59.791  1.00 31.95           C  
-ATOM   2021  C   ILE A 263     -18.591  49.224  59.997  1.00 32.60           C  
-ATOM   2022  O   ILE A 263     -18.634  50.446  60.144  1.00 36.36           O  
-ATOM   2023  CB  ILE A 263     -17.012  48.277  58.281  1.00 31.78           C  
-ATOM   2024  CG1 ILE A 263     -15.639  47.632  58.075  1.00 26.38           C  
-ATOM   2025  CG2 ILE A 263     -17.094  49.590  57.505  1.00 26.81           C  
-ATOM   2026  CD1 ILE A 263     -15.383  47.162  56.663  1.00 26.34           C  
-ATOM   2027  N   HIS A 264     -19.679  48.454  60.011  1.00 39.26           N  
-ATOM   2028  CA  HIS A 264     -21.009  49.026  60.213  1.00 42.53           C  
-ATOM   2029  C   HIS A 264     -21.047  49.754  61.552  1.00 44.12           C  
-ATOM   2030  O   HIS A 264     -21.609  50.849  61.661  1.00 48.46           O  
-ATOM   2031  CB  HIS A 264     -22.088  47.937  60.183  1.00 51.90           C  
-ATOM   2032  CG  HIS A 264     -23.457  48.435  60.535  1.00 67.28           C  
-ATOM   2033  ND1 HIS A 264     -24.082  48.123  61.724  1.00 73.28           N  
-ATOM   2034  CD2 HIS A 264     -24.333  49.201  59.841  1.00 69.74           C  
-ATOM   2035  CE1 HIS A 264     -25.283  48.672  61.747  1.00 73.29           C  
-ATOM   2036  NE2 HIS A 264     -25.459  49.333  60.617  1.00 73.20           N  
-ATOM   2037  N   CYS A 265     -20.424  49.143  62.558  1.00 40.87           N  
-ATOM   2038  CA  CYS A 265     -20.363  49.711  63.898  1.00 38.33           C  
-ATOM   2039  C   CYS A 265     -19.534  50.995  63.910  1.00 35.52           C  
-ATOM   2040  O   CYS A 265     -19.997  52.037  64.382  1.00 31.47           O  
-ATOM   2041  CB  CYS A 265     -19.771  48.691  64.873  1.00 38.92           C  
-ATOM   2042  SG  CYS A 265     -19.561  49.306  66.574  1.00 40.02           S  
-ATOM   2043  N   LEU A 266     -18.329  50.918  63.348  1.00 28.75           N  
-ATOM   2044  CA  LEU A 266     -17.422  52.059  63.286  1.00 27.08           C  
-ATOM   2045  C   LEU A 266     -17.997  53.229  62.484  1.00 30.27           C  
-ATOM   2046  O   LEU A 266     -17.574  54.371  62.658  1.00 32.50           O  
-ATOM   2047  CB  LEU A 266     -16.071  51.624  62.706  1.00 19.64           C  
-ATOM   2048  CG  LEU A 266     -15.301  50.566  63.506  1.00 15.88           C  
-ATOM   2049  CD1 LEU A 266     -14.045  50.160  62.761  1.00  6.01           C  
-ATOM   2050  CD2 LEU A 266     -14.954  51.101  64.890  1.00 15.35           C  
-ATOM   2051  N   ARG A 267     -18.964  52.942  61.616  1.00 33.15           N  
-ATOM   2052  CA  ARG A 267     -19.594  53.978  60.803  1.00 35.42           C  
-ATOM   2053  C   ARG A 267     -20.717  54.696  61.544  1.00 37.88           C  
-ATOM   2054  O   ARG A 267     -21.009  55.857  61.253  1.00 39.55           O  
-ATOM   2055  CB  ARG A 267     -20.124  53.397  59.490  1.00 34.45           C  
-ATOM   2056  CG  ARG A 267     -19.053  53.150  58.444  1.00 31.76           C  
-ATOM   2057  CD  ARG A 267     -19.666  52.793  57.101  1.00 31.99           C  
-ATOM   2058  NE  ARG A 267     -18.648  52.644  56.065  1.00 36.70           N  
-ATOM   2059  CZ  ARG A 267     -18.616  51.654  55.177  1.00 34.74           C  
-ATOM   2060  NH1 ARG A 267     -19.554  50.715  55.190  1.00 36.16           N  
-ATOM   2061  NH2 ARG A 267     -17.636  51.592  54.288  1.00 23.42           N  
-ATOM   2062  N   GLU A 268     -21.363  54.001  62.478  1.00 39.53           N  
-ATOM   2063  CA  GLU A 268     -22.445  54.603  63.253  1.00 44.55           C  
-ATOM   2064  C   GLU A 268     -21.902  55.513  64.348  1.00 42.21           C  
-ATOM   2065  O   GLU A 268     -22.567  56.466  64.757  1.00 45.98           O  
-ATOM   2066  CB  GLU A 268     -23.361  53.527  63.853  1.00 47.52           C  
-ATOM   2067  CG  GLU A 268     -24.466  53.046  62.909  1.00 56.24           C  
-ATOM   2068  CD  GLU A 268     -25.408  54.169  62.481  1.00 64.87           C  
-ATOM   2069  OE1 GLU A 268     -26.235  54.610  63.311  1.00 69.94           O  
-ATOM   2070  OE2 GLU A 268     -25.321  54.612  61.315  1.00 61.82           O  
-ATOM   2071  N   LYS A 269     -20.678  55.232  64.794  1.00 39.60           N  
-ATOM   2072  CA  LYS A 269     -20.036  56.021  65.840  1.00 36.50           C  
-ATOM   2073  C   LYS A 269     -19.664  57.418  65.350  1.00 35.86           C  
-ATOM   2074  O   LYS A 269     -19.267  57.598  64.197  1.00 39.35           O  
-ATOM   2075  CB  LYS A 269     -18.783  55.308  66.360  1.00 32.68           C  
-ATOM   2076  CG  LYS A 269     -19.034  53.992  67.100  1.00 34.10           C  
-ATOM   2077  CD  LYS A 269     -19.965  54.175  68.295  1.00 46.98           C  
-ATOM   2078  CE  LYS A 269     -19.912  52.991  69.259  1.00 49.91           C  
-ATOM   2079  NZ  LYS A 269     -20.260  51.693  68.619  1.00 57.38           N  
-ATOM   2080  N   LYS A 270     -19.826  58.407  66.224  1.00 35.46           N  
-ATOM   2081  CA  LYS A 270     -19.493  59.787  65.894  1.00 37.34           C  
-ATOM   2082  C   LYS A 270     -17.977  59.925  65.735  1.00 37.91           C  
-ATOM   2083  O   LYS A 270     -17.217  59.134  66.293  1.00 38.40           O  
-ATOM   2084  CB  LYS A 270     -20.025  60.740  66.974  1.00 40.07           C  
-ATOM   2085  CG  LYS A 270     -21.495  61.114  66.791  1.00 52.32           C  
-ATOM   2086  CD  LYS A 270     -21.992  62.067  67.871  1.00 59.83           C  
-ATOM   2087  CE  LYS A 270     -22.319  61.334  69.165  1.00 68.22           C  
-ATOM   2088  NZ  LYS A 270     -22.782  62.261  70.239  1.00 72.15           N  
-ATOM   2089  N   PRO A 271     -17.522  60.923  64.954  1.00 33.52           N  
-ATOM   2090  CA  PRO A 271     -16.096  61.166  64.711  1.00 31.56           C  
-ATOM   2091  C   PRO A 271     -15.208  61.167  65.953  1.00 29.20           C  
-ATOM   2092  O   PRO A 271     -14.234  60.416  66.023  1.00 29.86           O  
-ATOM   2093  CB  PRO A 271     -16.107  62.531  64.026  1.00 32.08           C  
-ATOM   2094  CG  PRO A 271     -17.360  62.479  63.230  1.00 28.04           C  
-ATOM   2095  CD  PRO A 271     -18.342  61.908  64.228  1.00 32.68           C  
-ATOM   2096  N   GLN A 272     -15.572  61.979  66.944  1.00 26.74           N  
-ATOM   2097  CA  GLN A 272     -14.794  62.095  68.175  1.00 25.10           C  
-ATOM   2098  C   GLN A 272     -14.723  60.812  69.006  1.00 22.32           C  
-ATOM   2099  O   GLN A 272     -13.849  60.671  69.859  1.00 21.54           O  
-ATOM   2100  CB  GLN A 272     -15.315  63.259  69.023  1.00 29.36           C  
-ATOM   2101  CG  GLN A 272     -14.394  63.673  70.172  1.00 30.96           C  
-ATOM   2102  CD  GLN A 272     -12.953  63.862  69.734  1.00 32.44           C  
-ATOM   2103  OE1 GLN A 272     -12.673  64.586  68.780  1.00 37.38           O  
-ATOM   2104  NE2 GLN A 272     -12.036  63.212  70.428  1.00 30.28           N  
-ATOM   2105  N   GLU A 273     -15.623  59.872  68.736  1.00 27.16           N  
-ATOM   2106  CA  GLU A 273     -15.642  58.605  69.460  1.00 30.70           C  
-ATOM   2107  C   GLU A 273     -14.463  57.728  69.057  1.00 29.65           C  
-ATOM   2108  O   GLU A 273     -13.873  57.045  69.897  1.00 34.07           O  
-ATOM   2109  CB  GLU A 273     -16.962  57.865  69.227  1.00 30.88           C  
-ATOM   2110  CG  GLU A 273     -18.182  58.611  69.750  1.00 35.42           C  
-ATOM   2111  CD  GLU A 273     -19.432  57.753  69.776  1.00 35.88           C  
-ATOM   2112  OE1 GLU A 273     -19.396  56.661  70.377  1.00 42.16           O  
-ATOM   2113  OE2 GLU A 273     -20.457  58.176  69.205  1.00 41.91           O  
-ATOM   2114  N   LEU A 274     -14.123  57.757  67.771  1.00 29.96           N  
-ATOM   2115  CA  LEU A 274     -13.002  56.977  67.259  1.00 31.07           C  
-ATOM   2116  C   LEU A 274     -11.682  57.620  67.676  1.00 30.07           C  
-ATOM   2117  O   LEU A 274     -10.717  56.925  67.996  1.00 31.10           O  
-ATOM   2118  CB  LEU A 274     -13.066  56.856  65.729  1.00 29.65           C  
-ATOM   2119  CG  LEU A 274     -14.089  55.890  65.121  1.00 24.26           C  
-ATOM   2120  CD1 LEU A 274     -15.495  56.399  65.346  1.00 32.05           C  
-ATOM   2121  CD2 LEU A 274     -13.827  55.751  63.636  1.00 29.16           C  
-ATOM   2122  N   ILE A 275     -11.661  58.950  67.689  1.00 20.10           N  
-ATOM   2123  CA  ILE A 275     -10.471  59.707  68.059  1.00 19.40           C  
-ATOM   2124  C   ILE A 275     -10.089  59.521  69.531  1.00 21.93           C  
-ATOM   2125  O   ILE A 275      -8.911  59.355  69.856  1.00 20.40           O  
-ATOM   2126  CB  ILE A 275     -10.661  61.204  67.746  1.00 16.36           C  
-ATOM   2127  CG1 ILE A 275     -10.858  61.391  66.238  1.00 13.20           C  
-ATOM   2128  CG2 ILE A 275      -9.458  62.008  68.228  1.00 16.89           C  
-ATOM   2129  CD1 ILE A 275     -11.305  62.782  65.836  1.00  9.85           C  
-ATOM   2130  N   ASP A 276     -11.086  59.518  70.412  1.00 19.19           N  
-ATOM   2131  CA  ASP A 276     -10.841  59.352  71.840  1.00 16.93           C  
-ATOM   2132  C   ASP A 276     -10.135  58.057  72.218  1.00 19.59           C  
-ATOM   2133  O   ASP A 276      -9.409  58.019  73.211  1.00 27.36           O  
-ATOM   2134  CB  ASP A 276     -12.147  59.465  72.626  1.00 17.36           C  
-ATOM   2135  CG  ASP A 276     -12.645  60.890  72.735  1.00 16.64           C  
-ATOM   2136  OD1 ASP A 276     -11.822  61.827  72.674  1.00 22.44           O  
-ATOM   2137  OD2 ASP A 276     -13.867  61.072  72.899  1.00 23.77           O  
-ATOM   2138  N   VAL A 277     -10.339  57.002  71.432  1.00 18.37           N  
-ATOM   2139  CA  VAL A 277      -9.716  55.704  71.715  1.00 16.35           C  
-ATOM   2140  C   VAL A 277      -8.641  55.303  70.706  1.00 17.92           C  
-ATOM   2141  O   VAL A 277      -8.052  54.220  70.800  1.00 16.24           O  
-ATOM   2142  CB  VAL A 277     -10.775  54.578  71.778  1.00 17.95           C  
-ATOM   2143  CG1 VAL A 277     -11.789  54.867  72.874  1.00  8.84           C  
-ATOM   2144  CG2 VAL A 277     -11.468  54.420  70.427  1.00 13.33           C  
-ATOM   2145  N   GLU A 278      -8.380  56.199  69.761  1.00 17.81           N  
-ATOM   2146  CA  GLU A 278      -7.405  55.990  68.691  1.00 21.16           C  
-ATOM   2147  C   GLU A 278      -6.046  55.432  69.123  1.00 22.35           C  
-ATOM   2148  O   GLU A 278      -5.542  54.485  68.522  1.00 21.82           O  
-ATOM   2149  CB  GLU A 278      -7.198  57.308  67.934  1.00 23.29           C  
-ATOM   2150  CG  GLU A 278      -6.251  57.222  66.756  1.00 26.65           C  
-ATOM   2151  CD  GLU A 278      -6.017  58.564  66.091  1.00 21.84           C  
-ATOM   2152  OE1 GLU A 278      -6.983  59.335  65.924  1.00 20.83           O  
-ATOM   2153  OE2 GLU A 278      -4.858  58.842  65.724  1.00 27.33           O  
-ATOM   2154  N   TRP A 279      -5.471  56.010  70.172  1.00 25.18           N  
-ATOM   2155  CA  TRP A 279      -4.158  55.604  70.665  1.00 20.31           C  
-ATOM   2156  C   TRP A 279      -4.113  54.264  71.397  1.00 23.46           C  
-ATOM   2157  O   TRP A 279      -3.050  53.654  71.520  1.00 21.20           O  
-ATOM   2158  CB  TRP A 279      -3.592  56.707  71.555  1.00 15.41           C  
-ATOM   2159  CG  TRP A 279      -3.619  58.045  70.890  1.00 19.11           C  
-ATOM   2160  CD1 TRP A 279      -4.591  58.997  71.008  1.00 16.99           C  
-ATOM   2161  CD2 TRP A 279      -2.648  58.572  69.976  1.00 14.91           C  
-ATOM   2162  NE1 TRP A 279      -4.287  60.084  70.224  1.00 19.81           N  
-ATOM   2163  CE2 TRP A 279      -3.101  59.852  69.578  1.00 16.43           C  
-ATOM   2164  CE3 TRP A 279      -1.440  58.089  69.452  1.00 18.23           C  
-ATOM   2165  CZ2 TRP A 279      -2.389  60.657  68.679  1.00 19.10           C  
-ATOM   2166  CZ3 TRP A 279      -0.729  58.890  68.556  1.00 19.14           C  
-ATOM   2167  CH2 TRP A 279      -1.209  60.160  68.180  1.00 21.45           C  
-ATOM   2168  N   ASN A 280      -5.272  53.794  71.846  1.00 23.30           N  
-ATOM   2169  CA  ASN A 280      -5.365  52.535  72.579  1.00 19.66           C  
-ATOM   2170  C   ASN A 280      -4.966  51.292  71.778  1.00 19.91           C  
-ATOM   2171  O   ASN A 280      -4.681  50.243  72.363  1.00 19.50           O  
-ATOM   2172  CB  ASN A 280      -6.785  52.363  73.135  1.00 21.33           C  
-ATOM   2173  CG  ASN A 280      -7.208  53.517  74.046  1.00 25.52           C  
-ATOM   2174  OD1 ASN A 280      -6.415  54.399  74.360  1.00 24.62           O  
-ATOM   2175  ND2 ASN A 280      -8.467  53.510  74.466  1.00 18.66           N  
-ATOM   2176  N   VAL A 281      -4.903  51.425  70.454  1.00 22.58           N  
-ATOM   2177  CA  VAL A 281      -4.566  50.301  69.577  1.00 21.37           C  
-ATOM   2178  C   VAL A 281      -3.082  50.059  69.292  1.00 22.83           C  
-ATOM   2179  O   VAL A 281      -2.738  49.085  68.619  1.00 21.69           O  
-ATOM   2180  CB  VAL A 281      -5.318  50.389  68.221  1.00 26.87           C  
-ATOM   2181  CG1 VAL A 281      -6.804  50.635  68.451  1.00 20.03           C  
-ATOM   2182  CG2 VAL A 281      -4.714  51.472  67.335  1.00 18.79           C  
-ATOM   2183  N   LEU A 282      -2.208  50.951  69.761  1.00 24.22           N  
-ATOM   2184  CA  LEU A 282      -0.770  50.776  69.548  1.00 20.11           C  
-ATOM   2185  C   LEU A 282      -0.362  49.456  70.195  1.00 22.64           C  
-ATOM   2186  O   LEU A 282      -0.777  49.154  71.315  1.00 30.38           O  
-ATOM   2187  CB  LEU A 282       0.035  51.930  70.161  1.00 24.21           C  
-ATOM   2188  CG  LEU A 282       0.292  53.201  69.342  1.00 21.26           C  
-ATOM   2189  CD1 LEU A 282       1.016  54.239  70.188  1.00 28.00           C  
-ATOM   2190  CD2 LEU A 282       1.107  52.870  68.120  1.00 32.52           C  
-ATOM   2191  N   PRO A 283       0.429  48.636  69.484  1.00 24.25           N  
-ATOM   2192  CA  PRO A 283       0.874  47.342  70.011  1.00 26.56           C  
-ATOM   2193  C   PRO A 283       1.869  47.440  71.162  1.00 28.31           C  
-ATOM   2194  O   PRO A 283       1.884  46.588  72.052  1.00 29.64           O  
-ATOM   2195  CB  PRO A 283       1.501  46.679  68.786  1.00 19.61           C  
-ATOM   2196  CG  PRO A 283       2.061  47.839  68.037  1.00 18.93           C  
-ATOM   2197  CD  PRO A 283       0.944  48.850  68.120  1.00 21.24           C  
-ATOM   2198  N   PHE A 284       2.683  48.493  71.152  1.00 30.86           N  
-ATOM   2199  CA  PHE A 284       3.694  48.684  72.184  1.00 29.11           C  
-ATOM   2200  C   PHE A 284       3.624  50.063  72.826  1.00 30.91           C  
-ATOM   2201  O   PHE A 284       2.958  50.971  72.324  1.00 28.92           O  
-ATOM   2202  CB  PHE A 284       5.100  48.528  71.589  1.00 31.23           C  
-ATOM   2203  CG  PHE A 284       5.268  47.329  70.698  1.00 37.33           C  
-ATOM   2204  CD1 PHE A 284       5.203  46.040  71.218  1.00 36.72           C  
-ATOM   2205  CD2 PHE A 284       5.519  47.493  69.337  1.00 35.88           C  
-ATOM   2206  CE1 PHE A 284       5.388  44.930  70.394  1.00 43.63           C  
-ATOM   2207  CE2 PHE A 284       5.705  46.393  68.506  1.00 38.94           C  
-ATOM   2208  CZ  PHE A 284       5.640  45.108  69.035  1.00 44.08           C  
-ATOM   2209  N   ASP A 285       4.309  50.192  73.957  1.00 28.27           N  
-ATOM   2210  CA  ASP A 285       4.417  51.455  74.670  1.00 26.59           C  
-ATOM   2211  C   ASP A 285       5.575  52.107  73.916  1.00 25.14           C  
-ATOM   2212  O   ASP A 285       6.709  51.619  73.959  1.00 18.19           O  
-ATOM   2213  CB  ASP A 285       4.783  51.200  76.139  1.00 32.06           C  
-ATOM   2214  CG  ASP A 285       4.978  52.482  76.935  1.00 30.02           C  
-ATOM   2215  OD1 ASP A 285       4.534  53.561  76.479  1.00 28.94           O  
-ATOM   2216  OD2 ASP A 285       5.578  52.403  78.029  1.00 24.30           O  
-ATOM   2217  N   SER A 286       5.285  53.184  73.196  1.00 26.61           N  
-ATOM   2218  CA  SER A 286       6.320  53.818  72.395  1.00 26.44           C  
-ATOM   2219  C   SER A 286       6.096  55.282  72.055  1.00 22.34           C  
-ATOM   2220  O   SER A 286       5.065  55.869  72.381  1.00 26.31           O  
-ATOM   2221  CB  SER A 286       6.461  53.039  71.088  1.00 31.86           C  
-ATOM   2222  OG  SER A 286       5.209  52.966  70.420  1.00 23.80           O  
-ATOM   2223  N   ILE A 287       7.101  55.864  71.408  1.00 16.59           N  
-ATOM   2224  CA  ILE A 287       7.043  57.245  70.956  1.00 22.87           C  
-ATOM   2225  C   ILE A 287       7.282  57.216  69.446  1.00 23.85           C  
-ATOM   2226  O   ILE A 287       7.858  56.255  68.921  1.00 18.27           O  
-ATOM   2227  CB  ILE A 287       8.100  58.147  71.657  1.00 22.85           C  
-ATOM   2228  CG1 ILE A 287       9.503  57.556  71.512  1.00 21.71           C  
-ATOM   2229  CG2 ILE A 287       7.739  58.345  73.120  1.00 18.15           C  
-ATOM   2230  CD1 ILE A 287      10.587  58.372  72.191  1.00 22.31           C  
-ATOM   2231  N   PHE A 288       6.813  58.252  68.754  1.00 17.67           N  
-ATOM   2232  CA  PHE A 288       6.953  58.359  67.302  1.00 17.28           C  
-ATOM   2233  C   PHE A 288       6.297  57.171  66.592  1.00 17.22           C  
-ATOM   2234  O   PHE A 288       6.844  56.607  65.640  1.00 18.34           O  
-ATOM   2235  CB  PHE A 288       8.427  58.495  66.897  1.00 16.03           C  
-ATOM   2236  CG  PHE A 288       8.655  59.399  65.706  1.00 19.36           C  
-ATOM   2237  CD1 PHE A 288       7.732  59.465  64.665  1.00 17.46           C  
-ATOM   2238  CD2 PHE A 288       9.797  60.187  65.632  1.00 14.85           C  
-ATOM   2239  CE1 PHE A 288       7.942  60.300  63.572  1.00 13.44           C  
-ATOM   2240  CE2 PHE A 288      10.015  61.024  64.540  1.00 21.65           C  
-ATOM   2241  CZ  PHE A 288       9.079  61.078  63.506  1.00 14.68           C  
-ATOM   2242  N   ARG A 289       5.138  56.773  67.110  1.00 13.91           N  
-ATOM   2243  CA  ARG A 289       4.351  55.680  66.554  1.00 12.20           C  
-ATOM   2244  C   ARG A 289       2.898  56.132  66.543  1.00 14.29           C  
-ATOM   2245  O   ARG A 289       2.392  56.681  67.528  1.00 11.41           O  
-ATOM   2246  CB  ARG A 289       4.510  54.398  67.375  1.00  7.98           C  
-ATOM   2247  CG  ARG A 289       5.879  53.749  67.250  1.00  5.45           C  
-ATOM   2248  CD  ARG A 289       6.183  53.360  65.801  1.00  6.76           C  
-ATOM   2249  NE  ARG A 289       7.452  52.646  65.687  1.00 11.20           N  
-ATOM   2250  CZ  ARG A 289       8.639  53.240  65.632  1.00 15.15           C  
-ATOM   2251  NH1 ARG A 289       8.734  54.562  65.675  1.00 12.25           N  
-ATOM   2252  NH2 ARG A 289       9.736  52.501  65.560  1.00 10.57           N  
-ATOM   2253  N   PHE A 290       2.242  55.925  65.406  1.00 16.89           N  
-ATOM   2254  CA  PHE A 290       0.860  56.340  65.222  1.00 14.54           C  
-ATOM   2255  C   PHE A 290      -0.016  55.161  64.814  1.00 13.32           C  
-ATOM   2256  O   PHE A 290       0.426  54.249  64.118  1.00 17.63           O  
-ATOM   2257  CB  PHE A 290       0.823  57.469  64.186  1.00 15.61           C  
-ATOM   2258  CG  PHE A 290       1.985  58.437  64.313  1.00 15.21           C  
-ATOM   2259  CD1 PHE A 290       2.063  59.319  65.388  1.00 10.36           C  
-ATOM   2260  CD2 PHE A 290       3.026  58.425  63.383  1.00 13.00           C  
-ATOM   2261  CE1 PHE A 290       3.156  60.171  65.538  1.00  8.77           C  
-ATOM   2262  CE2 PHE A 290       4.125  59.274  63.524  1.00  8.08           C  
-ATOM   2263  CZ  PHE A 290       4.190  60.147  64.602  1.00  5.75           C  
-ATOM   2264  N   SER A 291      -1.263  55.189  65.267  1.00 19.75           N  
-ATOM   2265  CA  SER A 291      -2.227  54.119  65.016  1.00 26.91           C  
-ATOM   2266  C   SER A 291      -2.560  53.733  63.574  1.00 27.18           C  
-ATOM   2267  O   SER A 291      -2.203  52.645  63.119  1.00 23.86           O  
-ATOM   2268  CB  SER A 291      -3.524  54.411  65.768  1.00 24.29           C  
-ATOM   2269  OG  SER A 291      -3.290  54.488  67.157  1.00 19.46           O  
-ATOM   2270  N   PHE A 292      -3.281  54.603  62.874  1.00 22.98           N  
-ATOM   2271  CA  PHE A 292      -3.690  54.317  61.506  1.00 20.20           C  
-ATOM   2272  C   PHE A 292      -2.831  54.998  60.456  1.00 20.12           C  
-ATOM   2273  O   PHE A 292      -2.951  56.193  60.198  1.00 22.43           O  
-ATOM   2274  CB  PHE A 292      -5.172  54.642  61.344  1.00 18.36           C  
-ATOM   2275  CG  PHE A 292      -6.028  53.987  62.384  1.00 20.90           C  
-ATOM   2276  CD1 PHE A 292      -6.427  52.661  62.240  1.00 25.30           C  
-ATOM   2277  CD2 PHE A 292      -6.366  54.665  63.549  1.00 21.87           C  
-ATOM   2278  CE1 PHE A 292      -7.143  52.016  63.244  1.00 18.65           C  
-ATOM   2279  CE2 PHE A 292      -7.081  54.032  64.559  1.00 24.37           C  
-ATOM   2280  CZ  PHE A 292      -7.469  52.702  64.405  1.00 25.40           C  
-ATOM   2281  N   VAL A 293      -1.964  54.195  59.853  1.00 17.67           N  
-ATOM   2282  CA  VAL A 293      -1.027  54.640  58.835  1.00 19.55           C  
-ATOM   2283  C   VAL A 293      -1.155  53.743  57.593  1.00 23.81           C  
-ATOM   2284  O   VAL A 293      -1.869  52.738  57.622  1.00 27.35           O  
-ATOM   2285  CB  VAL A 293       0.425  54.571  59.388  1.00 17.21           C  
-ATOM   2286  CG1 VAL A 293       0.603  55.552  60.538  1.00 11.25           C  
-ATOM   2287  CG2 VAL A 293       0.739  53.161  59.868  1.00 11.76           C  
-ATOM   2288  N   PRO A 294      -0.507  54.122  56.473  1.00 21.89           N  
-ATOM   2289  CA  PRO A 294      -0.557  53.338  55.234  1.00 18.27           C  
-ATOM   2290  C   PRO A 294      -0.179  51.868  55.434  1.00 20.21           C  
-ATOM   2291  O   PRO A 294       0.693  51.547  56.236  1.00 18.76           O  
-ATOM   2292  CB  PRO A 294       0.469  54.045  54.354  1.00 15.42           C  
-ATOM   2293  CG  PRO A 294       0.301  55.467  54.743  1.00 19.11           C  
-ATOM   2294  CD  PRO A 294       0.208  55.396  56.250  1.00 16.84           C  
-ATOM   2295  N   VAL A 295      -0.860  50.980  54.716  1.00 21.93           N  
-ATOM   2296  CA  VAL A 295      -0.594  49.545  54.797  1.00 23.18           C  
-ATOM   2297  C   VAL A 295       0.005  48.997  53.505  1.00 24.08           C  
-ATOM   2298  O   VAL A 295      -0.250  49.518  52.419  1.00 25.86           O  
-ATOM   2299  CB  VAL A 295      -1.878  48.743  55.097  1.00 21.53           C  
-ATOM   2300  CG1 VAL A 295      -2.337  49.006  56.511  1.00 37.23           C  
-ATOM   2301  CG2 VAL A 295      -2.974  49.105  54.108  1.00 22.08           C  
-ATOM   2302  N   ILE A 296       0.823  47.956  53.633  1.00 20.19           N  
-ATOM   2303  CA  ILE A 296       1.433  47.313  52.471  1.00 23.71           C  
-ATOM   2304  C   ILE A 296       0.402  46.295  51.976  1.00 25.61           C  
-ATOM   2305  O   ILE A 296       0.480  45.105  52.281  1.00 21.77           O  
-ATOM   2306  CB  ILE A 296       2.759  46.618  52.858  1.00 22.29           C  
-ATOM   2307  CG1 ILE A 296       3.661  47.606  53.603  1.00 18.54           C  
-ATOM   2308  CG2 ILE A 296       3.468  46.094  51.614  1.00 22.54           C  
-ATOM   2309  CD1 ILE A 296       3.859  48.936  52.877  1.00 15.33           C  
-ATOM   2310  N   ASP A 297      -0.580  46.799  51.233  1.00 26.08           N  
-ATOM   2311  CA  ASP A 297      -1.688  46.000  50.717  1.00 27.48           C  
-ATOM   2312  C   ASP A 297      -1.463  45.107  49.501  1.00 31.34           C  
-ATOM   2313  O   ASP A 297      -2.152  44.100  49.335  1.00 32.79           O  
-ATOM   2314  CB  ASP A 297      -2.915  46.899  50.480  1.00 23.88           C  
-ATOM   2315  CG  ASP A 297      -2.654  48.036  49.480  1.00 29.74           C  
-ATOM   2316  OD1 ASP A 297      -1.487  48.267  49.088  1.00 25.29           O  
-ATOM   2317  OD2 ASP A 297      -3.637  48.712  49.089  1.00 29.16           O  
-ATOM   2318  N   GLY A 298      -0.505  45.466  48.656  1.00 33.02           N  
-ATOM   2319  CA  GLY A 298      -0.257  44.679  47.462  1.00 28.86           C  
-ATOM   2320  C   GLY A 298      -0.906  45.342  46.257  1.00 30.24           C  
-ATOM   2321  O   GLY A 298      -0.783  44.863  45.130  1.00 29.95           O  
-ATOM   2322  N   GLU A 299      -1.618  46.440  46.509  1.00 27.79           N  
-ATOM   2323  CA  GLU A 299      -2.291  47.202  45.465  1.00 28.61           C  
-ATOM   2324  C   GLU A 299      -1.604  48.558  45.302  1.00 29.13           C  
-ATOM   2325  O   GLU A 299      -0.932  48.795  44.295  1.00 31.92           O  
-ATOM   2326  CB  GLU A 299      -3.770  47.377  45.806  1.00 33.62           C  
-ATOM   2327  CG  GLU A 299      -4.550  46.066  45.800  1.00 54.72           C  
-ATOM   2328  CD  GLU A 299      -5.984  46.209  46.284  1.00 65.19           C  
-ATOM   2329  OE1 GLU A 299      -6.557  47.316  46.176  1.00 71.92           O  
-ATOM   2330  OE2 GLU A 299      -6.541  45.202  46.773  1.00 67.65           O  
-ATOM   2331  N   PHE A 300      -1.754  49.433  46.299  1.00 27.39           N  
-ATOM   2332  CA  PHE A 300      -1.123  50.753  46.266  1.00 20.98           C  
-ATOM   2333  C   PHE A 300       0.385  50.530  46.245  1.00 20.50           C  
-ATOM   2334  O   PHE A 300       1.127  51.259  45.589  1.00 24.21           O  
-ATOM   2335  CB  PHE A 300      -1.519  51.581  47.496  1.00 18.68           C  
-ATOM   2336  CG  PHE A 300      -1.226  53.054  47.359  1.00 13.94           C  
-ATOM   2337  CD1 PHE A 300       0.060  53.550  47.567  1.00 13.28           C  
-ATOM   2338  CD2 PHE A 300      -2.237  53.944  47.010  1.00 12.50           C  
-ATOM   2339  CE1 PHE A 300       0.332  54.911  47.427  1.00  3.62           C  
-ATOM   2340  CE2 PHE A 300      -1.978  55.305  46.867  1.00  2.00           C  
-ATOM   2341  CZ  PHE A 300      -0.690  55.789  47.076  1.00  8.32           C  
-ATOM   2342  N   PHE A 301       0.821  49.519  46.988  1.00 22.00           N  
-ATOM   2343  CA  PHE A 301       2.223  49.136  47.053  1.00 19.99           C  
-ATOM   2344  C   PHE A 301       2.239  47.690  46.555  1.00 24.85           C  
-ATOM   2345  O   PHE A 301       1.759  46.796  47.242  1.00 25.98           O  
-ATOM   2346  CB  PHE A 301       2.736  49.197  48.498  1.00 19.90           C  
-ATOM   2347  CG  PHE A 301       2.629  50.560  49.130  1.00 21.14           C  
-ATOM   2348  CD1 PHE A 301       3.437  51.610  48.697  1.00 20.40           C  
-ATOM   2349  CD2 PHE A 301       1.729  50.792  50.169  1.00 14.32           C  
-ATOM   2350  CE1 PHE A 301       3.352  52.870  49.291  1.00 24.29           C  
-ATOM   2351  CE2 PHE A 301       1.635  52.050  50.771  1.00 14.13           C  
-ATOM   2352  CZ  PHE A 301       2.448  53.090  50.332  1.00 15.88           C  
-ATOM   2353  N   PRO A 302       2.742  47.454  45.328  1.00 26.36           N  
-ATOM   2354  CA  PRO A 302       2.818  46.120  44.721  1.00 28.04           C  
-ATOM   2355  C   PRO A 302       3.450  45.054  45.614  1.00 25.32           C  
-ATOM   2356  O   PRO A 302       2.920  43.947  45.740  1.00 24.93           O  
-ATOM   2357  CB  PRO A 302       3.648  46.379  43.467  1.00 28.23           C  
-ATOM   2358  CG  PRO A 302       3.189  47.739  43.068  1.00 23.38           C  
-ATOM   2359  CD  PRO A 302       3.241  48.472  44.387  1.00 27.30           C  
-ATOM   2360  N   THR A 303       4.590  45.393  46.214  1.00 26.88           N  
-ATOM   2361  CA  THR A 303       5.318  44.493  47.112  1.00 28.30           C  
-ATOM   2362  C   THR A 303       5.912  45.315  48.262  1.00 28.16           C  
-ATOM   2363  O   THR A 303       5.588  46.498  48.410  1.00 24.99           O  
-ATOM   2364  CB  THR A 303       6.457  43.746  46.373  1.00 31.13           C  
-ATOM   2365  OG1 THR A 303       7.363  44.690  45.793  1.00 28.18           O  
-ATOM   2366  CG2 THR A 303       5.898  42.859  45.275  1.00 32.62           C  
-ATOM   2367  N   SER A 304       6.769  44.695  49.076  1.00 23.24           N  
-ATOM   2368  CA  SER A 304       7.398  45.393  50.201  1.00 23.93           C  
-ATOM   2369  C   SER A 304       8.168  46.618  49.710  1.00 22.81           C  
-ATOM   2370  O   SER A 304       8.742  46.594  48.621  1.00 20.74           O  
-ATOM   2371  CB  SER A 304       8.343  44.458  50.961  1.00 25.56           C  
-ATOM   2372  OG  SER A 304       9.471  44.108  50.177  1.00 27.86           O  
-ATOM   2373  N   LEU A 305       8.171  47.684  50.509  1.00 19.44           N  
-ATOM   2374  CA  LEU A 305       8.863  48.918  50.145  1.00 18.92           C  
-ATOM   2375  C   LEU A 305      10.343  48.692  49.847  1.00 21.41           C  
-ATOM   2376  O   LEU A 305      10.908  49.314  48.949  1.00 22.21           O  
-ATOM   2377  CB  LEU A 305       8.714  49.960  51.258  1.00 20.32           C  
-ATOM   2378  CG  LEU A 305       7.284  50.333  51.662  1.00 21.29           C  
-ATOM   2379  CD1 LEU A 305       7.324  51.415  52.720  1.00 18.89           C  
-ATOM   2380  CD2 LEU A 305       6.498  50.804  50.457  1.00 23.23           C  
-ATOM   2381  N   GLU A 306      10.956  47.781  50.598  1.00 23.33           N  
-ATOM   2382  CA  GLU A 306      12.368  47.466  50.435  1.00 18.69           C  
-ATOM   2383  C   GLU A 306      12.626  46.755  49.116  1.00 22.67           C  
-ATOM   2384  O   GLU A 306      13.563  47.107  48.400  1.00 23.86           O  
-ATOM   2385  CB  GLU A 306      12.868  46.612  51.602  1.00 14.77           C  
-ATOM   2386  CG  GLU A 306      14.355  46.251  51.542  1.00 24.13           C  
-ATOM   2387  CD  GLU A 306      15.292  47.458  51.577  1.00 30.62           C  
-ATOM   2388  OE1 GLU A 306      14.845  48.582  51.899  1.00 32.17           O  
-ATOM   2389  OE2 GLU A 306      16.493  47.273  51.285  1.00 34.11           O  
-ATOM   2390  N   SER A 307      11.796  45.764  48.792  1.00 23.45           N  
-ATOM   2391  CA  SER A 307      11.955  45.025  47.542  1.00 26.26           C  
-ATOM   2392  C   SER A 307      11.740  45.949  46.342  1.00 26.09           C  
-ATOM   2393  O   SER A 307      12.403  45.797  45.313  1.00 29.09           O  
-ATOM   2394  CB  SER A 307      11.001  43.828  47.484  1.00 22.66           C  
-ATOM   2395  OG  SER A 307       9.649  44.231  47.377  1.00 37.59           O  
-ATOM   2396  N   MET A 308      10.828  46.912  46.489  1.00 23.14           N  
-ATOM   2397  CA  MET A 308      10.548  47.884  45.434  1.00 20.46           C  
-ATOM   2398  C   MET A 308      11.756  48.795  45.261  1.00 23.43           C  
-ATOM   2399  O   MET A 308      12.179  49.069  44.140  1.00 32.98           O  
-ATOM   2400  CB  MET A 308       9.313  48.728  45.771  1.00 18.08           C  
-ATOM   2401  CG  MET A 308       7.993  47.997  45.614  1.00 14.95           C  
-ATOM   2402  SD  MET A 308       6.562  49.059  45.897  1.00 22.13           S  
-ATOM   2403  CE  MET A 308       6.612  50.052  44.424  1.00 14.69           C  
-ATOM   2404  N   LEU A 309      12.316  49.247  46.381  1.00 26.37           N  
-ATOM   2405  CA  LEU A 309      13.489  50.120  46.364  1.00 27.64           C  
-ATOM   2406  C   LEU A 309      14.710  49.425  45.767  1.00 26.26           C  
-ATOM   2407  O   LEU A 309      15.500  50.050  45.060  1.00 26.53           O  
-ATOM   2408  CB  LEU A 309      13.811  50.621  47.775  1.00 27.23           C  
-ATOM   2409  CG  LEU A 309      12.920  51.736  48.331  1.00 28.43           C  
-ATOM   2410  CD1 LEU A 309      13.298  52.017  49.776  1.00 26.76           C  
-ATOM   2411  CD2 LEU A 309      13.069  52.996  47.487  1.00 22.97           C  
-ATOM   2412  N   ASN A 310      14.843  48.127  46.035  1.00 28.77           N  
-ATOM   2413  CA  ASN A 310      15.959  47.336  45.523  1.00 29.33           C  
-ATOM   2414  C   ASN A 310      15.884  47.086  44.019  1.00 27.61           C  
-ATOM   2415  O   ASN A 310      16.895  47.177  43.320  1.00 24.43           O  
-ATOM   2416  CB  ASN A 310      16.043  45.992  46.254  1.00 32.00           C  
-ATOM   2417  CG  ASN A 310      16.746  46.100  47.591  1.00 39.80           C  
-ATOM   2418  OD1 ASN A 310      17.794  46.734  47.699  1.00 44.09           O  
-ATOM   2419  ND2 ASN A 310      16.178  45.474  48.617  1.00 49.25           N  
-ATOM   2420  N   SER A 311      14.683  46.786  43.530  1.00 26.90           N  
-ATOM   2421  CA  SER A 311      14.473  46.495  42.115  1.00 25.65           C  
-ATOM   2422  C   SER A 311      14.325  47.720  41.222  1.00 28.53           C  
-ATOM   2423  O   SER A 311      14.290  47.593  39.994  1.00 36.86           O  
-ATOM   2424  CB  SER A 311      13.257  45.577  41.940  1.00 25.89           C  
-ATOM   2425  OG  SER A 311      12.078  46.168  42.459  1.00 33.30           O  
-ATOM   2426  N   GLY A 312      14.261  48.904  41.827  1.00 26.79           N  
-ATOM   2427  CA  GLY A 312      14.105  50.121  41.046  1.00 21.05           C  
-ATOM   2428  C   GLY A 312      12.670  50.287  40.577  1.00 21.42           C  
-ATOM   2429  O   GLY A 312      12.405  50.934  39.565  1.00 19.59           O  
-ATOM   2430  N   ASN A 313      11.746  49.678  41.313  1.00 22.04           N  
-ATOM   2431  CA  ASN A 313      10.329  49.744  40.994  1.00 20.97           C  
-ATOM   2432  C   ASN A 313       9.737  51.033  41.556  1.00 24.34           C  
-ATOM   2433  O   ASN A 313       9.058  51.032  42.588  1.00 26.08           O  
-ATOM   2434  CB  ASN A 313       9.604  48.520  41.566  1.00 22.38           C  
-ATOM   2435  CG  ASN A 313       8.212  48.338  40.985  1.00 23.49           C  
-ATOM   2436  OD1 ASN A 313       7.789  49.086  40.106  1.00 30.24           O  
-ATOM   2437  ND2 ASN A 313       7.497  47.333  41.472  1.00 27.97           N  
-ATOM   2438  N   PHE A 314      10.037  52.138  40.883  1.00 27.05           N  
-ATOM   2439  CA  PHE A 314       9.551  53.455  41.277  1.00 24.63           C  
-ATOM   2440  C   PHE A 314       9.791  54.465  40.166  1.00 23.51           C  
-ATOM   2441  O   PHE A 314      10.522  54.191  39.213  1.00 21.93           O  
-ATOM   2442  CB  PHE A 314      10.206  53.926  42.588  1.00 17.60           C  
-ATOM   2443  CG  PHE A 314      11.707  53.794  42.613  1.00 13.91           C  
-ATOM   2444  CD1 PHE A 314      12.515  54.699  41.934  1.00 10.31           C  
-ATOM   2445  CD2 PHE A 314      12.311  52.764  43.326  1.00 12.93           C  
-ATOM   2446  CE1 PHE A 314      13.904  54.583  41.964  1.00 11.88           C  
-ATOM   2447  CE2 PHE A 314      13.701  52.637  43.364  1.00 12.79           C  
-ATOM   2448  CZ  PHE A 314      14.499  53.549  42.681  1.00 15.17           C  
-ATOM   2449  N   LYS A 315       9.169  55.631  40.298  1.00 24.35           N  
-ATOM   2450  CA  LYS A 315       9.296  56.692  39.312  1.00 18.99           C  
-ATOM   2451  C   LYS A 315      10.714  57.248  39.265  1.00 20.64           C  
-ATOM   2452  O   LYS A 315      11.281  57.624  40.295  1.00 18.48           O  
-ATOM   2453  CB  LYS A 315       8.305  57.818  39.621  1.00 19.35           C  
-ATOM   2454  CG  LYS A 315       8.268  58.925  38.580  1.00 16.15           C  
-ATOM   2455  CD  LYS A 315       7.378  60.072  39.024  1.00 22.13           C  
-ATOM   2456  CE  LYS A 315       7.299  61.170  37.970  1.00 21.49           C  
-ATOM   2457  NZ  LYS A 315       6.591  60.742  36.732  1.00 28.96           N  
-ATOM   2458  N   LYS A 316      11.291  57.248  38.066  1.00 20.44           N  
-ATOM   2459  CA  LYS A 316      12.634  57.773  37.844  1.00 20.64           C  
-ATOM   2460  C   LYS A 316      12.511  59.245  37.475  1.00 22.19           C  
-ATOM   2461  O   LYS A 316      11.959  59.590  36.429  1.00 29.62           O  
-ATOM   2462  CB  LYS A 316      13.340  57.019  36.718  1.00 21.26           C  
-ATOM   2463  CG  LYS A 316      13.913  55.668  37.112  1.00 28.96           C  
-ATOM   2464  CD  LYS A 316      12.870  54.578  37.116  1.00 35.23           C  
-ATOM   2465  CE  LYS A 316      13.518  53.219  37.300  1.00 38.38           C  
-ATOM   2466  NZ  LYS A 316      12.538  52.123  37.064  1.00 53.97           N  
-ATOM   2467  N   THR A 317      13.007  60.107  38.356  1.00 20.70           N  
-ATOM   2468  CA  THR A 317      12.951  61.550  38.157  1.00 14.67           C  
-ATOM   2469  C   THR A 317      13.942  62.216  39.116  1.00 16.54           C  
-ATOM   2470  O   THR A 317      14.864  61.558  39.608  1.00 16.37           O  
-ATOM   2471  CB  THR A 317      11.501  62.081  38.378  1.00 15.62           C  
-ATOM   2472  OG1 THR A 317      11.451  63.495  38.143  1.00 19.04           O  
-ATOM   2473  CG2 THR A 317      11.004  61.763  39.786  1.00  7.82           C  
-ATOM   2474  N   GLN A 318      13.799  63.521  39.339  1.00 19.97           N  
-ATOM   2475  CA  GLN A 318      14.693  64.222  40.256  1.00 23.55           C  
-ATOM   2476  C   GLN A 318      14.006  64.415  41.604  1.00 24.52           C  
-ATOM   2477  O   GLN A 318      12.797  64.653  41.667  1.00 30.19           O  
-ATOM   2478  CB  GLN A 318      15.095  65.599  39.710  1.00 22.16           C  
-ATOM   2479  CG  GLN A 318      15.762  65.598  38.345  1.00 28.80           C  
-ATOM   2480  CD  GLN A 318      14.768  65.478  37.206  1.00 34.07           C  
-ATOM   2481  OE1 GLN A 318      13.785  66.215  37.144  1.00 32.57           O  
-ATOM   2482  NE2 GLN A 318      15.017  64.545  36.300  1.00 35.67           N  
-ATOM   2483  N   ILE A 319      14.774  64.288  42.681  1.00 23.58           N  
-ATOM   2484  CA  ILE A 319      14.239  64.491  44.022  1.00 23.20           C  
-ATOM   2485  C   ILE A 319      15.142  65.409  44.833  1.00 23.26           C  
-ATOM   2486  O   ILE A 319      16.362  65.435  44.647  1.00 22.26           O  
-ATOM   2487  CB  ILE A 319      14.062  63.168  44.817  1.00 17.72           C  
-ATOM   2488  CG1 ILE A 319      15.412  62.472  45.003  1.00 19.85           C  
-ATOM   2489  CG2 ILE A 319      13.021  62.273  44.151  1.00 12.36           C  
-ATOM   2490  CD1 ILE A 319      15.392  61.338  46.001  1.00 21.72           C  
-ATOM   2491  N   LEU A 320      14.518  66.192  45.705  1.00 19.27           N  
-ATOM   2492  CA  LEU A 320      15.237  67.095  46.588  1.00 20.71           C  
-ATOM   2493  C   LEU A 320      14.674  66.779  47.966  1.00 19.40           C  
-ATOM   2494  O   LEU A 320      13.470  66.887  48.193  1.00 20.20           O  
-ATOM   2495  CB  LEU A 320      14.985  68.558  46.211  1.00 21.00           C  
-ATOM   2496  CG  LEU A 320      15.816  69.605  46.960  1.00 21.99           C  
-ATOM   2497  CD1 LEU A 320      15.934  70.873  46.125  1.00 12.56           C  
-ATOM   2498  CD2 LEU A 320      15.204  69.901  48.317  1.00 18.91           C  
-ATOM   2499  N   LEU A 321      15.543  66.340  48.867  1.00 17.68           N  
-ATOM   2500  CA  LEU A 321      15.125  65.979  50.211  1.00 13.69           C  
-ATOM   2501  C   LEU A 321      16.201  66.277  51.243  1.00 15.79           C  
-ATOM   2502  O   LEU A 321      17.349  66.572  50.902  1.00 15.21           O  
-ATOM   2503  CB  LEU A 321      14.745  64.491  50.261  1.00 12.19           C  
-ATOM   2504  CG  LEU A 321      15.831  63.413  50.152  1.00 14.63           C  
-ATOM   2505  CD1 LEU A 321      15.163  62.048  50.194  1.00  9.15           C  
-ATOM   2506  CD2 LEU A 321      16.648  63.566  48.871  1.00 12.02           C  
-ATOM   2507  N   GLY A 322      15.821  66.194  52.511  1.00 14.42           N  
-ATOM   2508  CA  GLY A 322      16.765  66.456  53.577  1.00 14.47           C  
-ATOM   2509  C   GLY A 322      16.124  66.308  54.933  1.00 15.33           C  
-ATOM   2510  O   GLY A 322      14.945  65.962  55.035  1.00 17.44           O  
-ATOM   2511  N   VAL A 323      16.898  66.597  55.975  1.00 15.74           N  
-ATOM   2512  CA  VAL A 323      16.419  66.479  57.348  1.00 13.54           C  
-ATOM   2513  C   VAL A 323      16.873  67.646  58.221  1.00 16.58           C  
-ATOM   2514  O   VAL A 323      17.738  68.428  57.833  1.00 17.63           O  
-ATOM   2515  CB  VAL A 323      16.928  65.165  58.002  1.00  5.53           C  
-ATOM   2516  CG1 VAL A 323      16.406  63.955  57.250  1.00  8.51           C  
-ATOM   2517  CG2 VAL A 323      18.449  65.143  58.033  1.00 11.35           C  
-ATOM   2518  N   ASN A 324      16.233  67.789  59.377  1.00 19.39           N  
-ATOM   2519  CA  ASN A 324      16.592  68.825  60.339  1.00 17.12           C  
-ATOM   2520  C   ASN A 324      17.581  68.203  61.318  1.00 18.18           C  
-ATOM   2521  O   ASN A 324      17.628  66.981  61.469  1.00 19.41           O  
-ATOM   2522  CB  ASN A 324      15.356  69.330  61.090  1.00 13.28           C  
-ATOM   2523  CG  ASN A 324      14.433  70.164  60.215  1.00  7.60           C  
-ATOM   2524  OD1 ASN A 324      14.685  70.359  59.028  1.00 12.33           O  
-ATOM   2525  ND2 ASN A 324      13.354  70.656  60.805  1.00 10.94           N  
-ATOM   2526  N   LYS A 325      18.346  69.045  62.005  1.00 23.82           N  
-ATOM   2527  CA  LYS A 325      19.351  68.570  62.951  1.00 21.11           C  
-ATOM   2528  C   LYS A 325      18.828  67.775  64.155  1.00 21.41           C  
-ATOM   2529  O   LYS A 325      19.379  66.722  64.487  1.00 18.23           O  
-ATOM   2530  CB  LYS A 325      20.209  69.740  63.432  1.00 20.54           C  
-ATOM   2531  CG  LYS A 325      21.376  69.314  64.294  1.00 17.00           C  
-ATOM   2532  CD  LYS A 325      22.057  70.503  64.924  1.00 27.13           C  
-ATOM   2533  CE  LYS A 325      23.094  70.033  65.919  1.00 32.97           C  
-ATOM   2534  NZ  LYS A 325      22.470  69.127  66.928  1.00 39.76           N  
-ATOM   2535  N   ASP A 326      17.775  68.272  64.803  1.00 25.64           N  
-ATOM   2536  CA  ASP A 326      17.208  67.610  65.983  1.00 22.95           C  
-ATOM   2537  C   ASP A 326      15.743  67.210  65.774  1.00 23.17           C  
-ATOM   2538  O   ASP A 326      14.823  67.845  66.304  1.00 25.40           O  
-ATOM   2539  CB  ASP A 326      17.329  68.527  67.209  1.00 19.42           C  
-ATOM   2540  CG  ASP A 326      18.717  69.138  67.353  1.00 13.83           C  
-ATOM   2541  OD1 ASP A 326      19.687  68.385  67.576  1.00 15.29           O  
-ATOM   2542  OD2 ASP A 326      18.841  70.374  67.223  1.00 14.63           O  
-ATOM   2543  N   GLU A 327      15.547  66.122  65.035  1.00 23.62           N  
-ATOM   2544  CA  GLU A 327      14.218  65.602  64.707  1.00 19.85           C  
-ATOM   2545  C   GLU A 327      13.472  64.912  65.844  1.00 19.19           C  
-ATOM   2546  O   GLU A 327      12.241  64.943  65.885  1.00 30.47           O  
-ATOM   2547  CB  GLU A 327      14.317  64.620  63.534  1.00 21.52           C  
-ATOM   2548  CG  GLU A 327      14.956  65.187  62.276  1.00 19.84           C  
-ATOM   2549  CD  GLU A 327      13.959  65.830  61.329  1.00 23.42           C  
-ATOM   2550  OE1 GLU A 327      12.936  66.381  61.787  1.00 19.62           O  
-ATOM   2551  OE2 GLU A 327      14.202  65.779  60.110  1.00 26.89           O  
-ATOM   2552  N   GLY A 328      14.207  64.278  66.754  1.00 19.43           N  
-ATOM   2553  CA  GLY A 328      13.570  63.556  67.846  1.00 20.53           C  
-ATOM   2554  C   GLY A 328      13.045  64.300  69.065  1.00 23.52           C  
-ATOM   2555  O   GLY A 328      12.197  63.765  69.784  1.00 25.26           O  
-ATOM   2556  N   SER A 329      13.507  65.530  69.286  1.00 20.73           N  
-ATOM   2557  CA  SER A 329      13.094  66.316  70.452  1.00 22.79           C  
-ATOM   2558  C   SER A 329      11.593  66.437  70.695  1.00 22.02           C  
-ATOM   2559  O   SER A 329      11.129  66.253  71.821  1.00 30.39           O  
-ATOM   2560  CB  SER A 329      13.737  67.706  70.423  1.00 17.89           C  
-ATOM   2561  OG  SER A 329      13.433  68.397  69.226  1.00 26.61           O  
-ATOM   2562  N   PHE A 330      10.840  66.722  69.637  1.00 23.81           N  
-ATOM   2563  CA  PHE A 330       9.385  66.885  69.715  1.00 20.58           C  
-ATOM   2564  C   PHE A 330       8.681  65.689  70.350  1.00 18.35           C  
-ATOM   2565  O   PHE A 330       7.762  65.847  71.153  1.00 21.68           O  
-ATOM   2566  CB  PHE A 330       8.809  67.097  68.307  1.00 23.95           C  
-ATOM   2567  CG  PHE A 330       7.876  68.275  68.193  1.00 25.29           C  
-ATOM   2568  CD1 PHE A 330       6.999  68.600  69.227  1.00 27.09           C  
-ATOM   2569  CD2 PHE A 330       7.884  69.069  67.050  1.00 20.97           C  
-ATOM   2570  CE1 PHE A 330       6.147  69.702  69.122  1.00 25.76           C  
-ATOM   2571  CE2 PHE A 330       7.038  70.174  66.935  1.00 20.51           C  
-ATOM   2572  CZ  PHE A 330       6.169  70.491  67.971  1.00 23.59           C  
-ATOM   2573  N   PHE A 331       9.149  64.496  70.002  1.00 18.28           N  
-ATOM   2574  CA  PHE A 331       8.565  63.248  70.475  1.00 17.88           C  
-ATOM   2575  C   PHE A 331       8.984  62.832  71.876  1.00 20.54           C  
-ATOM   2576  O   PHE A 331       8.240  62.136  72.568  1.00 29.60           O  
-ATOM   2577  CB  PHE A 331       8.844  62.153  69.446  1.00 13.39           C  
-ATOM   2578  CG  PHE A 331       8.438  62.546  68.058  1.00 16.82           C  
-ATOM   2579  CD1 PHE A 331       9.286  63.323  67.268  1.00  7.68           C  
-ATOM   2580  CD2 PHE A 331       7.171  62.236  67.579  1.00  9.84           C  
-ATOM   2581  CE1 PHE A 331       8.875  63.792  66.028  1.00 11.86           C  
-ATOM   2582  CE2 PHE A 331       6.750  62.699  66.341  1.00 12.22           C  
-ATOM   2583  CZ  PHE A 331       7.603  63.482  65.563  1.00 17.31           C  
-ATOM   2584  N   LEU A 332      10.170  63.259  72.293  1.00 17.50           N  
-ATOM   2585  CA  LEU A 332      10.661  62.948  73.629  1.00 14.93           C  
-ATOM   2586  C   LEU A 332       9.930  63.835  74.634  1.00 16.99           C  
-ATOM   2587  O   LEU A 332       9.666  63.427  75.765  1.00 22.10           O  
-ATOM   2588  CB  LEU A 332      12.165  63.191  73.708  1.00 15.38           C  
-ATOM   2589  CG  LEU A 332      13.057  62.242  72.909  1.00 10.18           C  
-ATOM   2590  CD1 LEU A 332      14.456  62.822  72.791  1.00 11.96           C  
-ATOM   2591  CD2 LEU A 332      13.084  60.880  73.571  1.00  7.49           C  
-ATOM   2592  N   LEU A 333       9.588  65.042  74.197  1.00 15.01           N  
-ATOM   2593  CA  LEU A 333       8.874  66.001  75.026  1.00 14.15           C  
-ATOM   2594  C   LEU A 333       7.451  65.543  75.309  1.00 18.85           C  
-ATOM   2595  O   LEU A 333       6.895  65.848  76.361  1.00 24.04           O  
-ATOM   2596  CB  LEU A 333       8.831  67.358  74.329  1.00 11.30           C  
-ATOM   2597  CG  LEU A 333       7.956  68.421  74.990  1.00 16.51           C  
-ATOM   2598  CD1 LEU A 333       8.547  68.814  76.323  1.00 11.14           C  
-ATOM   2599  CD2 LEU A 333       7.840  69.629  74.086  1.00 16.58           C  
-ATOM   2600  N   TYR A 334       6.864  64.813  74.364  1.00 21.52           N  
-ATOM   2601  CA  TYR A 334       5.496  64.337  74.512  1.00 20.21           C  
-ATOM   2602  C   TYR A 334       5.287  62.959  75.132  1.00 24.56           C  
-ATOM   2603  O   TYR A 334       4.178  62.654  75.569  1.00 35.64           O  
-ATOM   2604  CB  TYR A 334       4.764  64.404  73.169  1.00 18.50           C  
-ATOM   2605  CG  TYR A 334       4.228  65.774  72.835  1.00 17.65           C  
-ATOM   2606  CD1 TYR A 334       5.090  66.827  72.529  1.00 19.70           C  
-ATOM   2607  CD2 TYR A 334       2.858  66.023  72.837  1.00 13.12           C  
-ATOM   2608  CE1 TYR A 334       4.600  68.094  72.235  1.00 10.68           C  
-ATOM   2609  CE2 TYR A 334       2.358  67.286  72.544  1.00 16.55           C  
-ATOM   2610  CZ  TYR A 334       3.231  68.318  72.244  1.00 15.14           C  
-ATOM   2611  OH  TYR A 334       2.729  69.571  71.958  1.00 12.97           O  
-ATOM   2612  N   GLY A 335       6.327  62.133  75.207  1.00 23.57           N  
-ATOM   2613  CA  GLY A 335       6.121  60.810  75.772  1.00 30.48           C  
-ATOM   2614  C   GLY A 335       7.230  60.163  76.577  1.00 35.01           C  
-ATOM   2615  O   GLY A 335       7.004  59.118  77.195  1.00 41.49           O  
-ATOM   2616  N   ALA A 336       8.421  60.751  76.563  1.00 25.67           N  
-ATOM   2617  CA  ALA A 336       9.539  60.189  77.307  1.00 24.91           C  
-ATOM   2618  C   ALA A 336       9.668  60.815  78.698  1.00 28.37           C  
-ATOM   2619  O   ALA A 336       9.575  62.035  78.857  1.00 25.84           O  
-ATOM   2620  CB  ALA A 336      10.831  60.356  76.519  1.00 17.84           C  
-ATOM   2621  N   PRO A 337       9.860  59.977  79.730  1.00 28.72           N  
-ATOM   2622  CA  PRO A 337      10.003  60.444  81.113  1.00 28.10           C  
-ATOM   2623  C   PRO A 337      11.269  61.277  81.344  1.00 24.89           C  
-ATOM   2624  O   PRO A 337      12.363  60.891  80.924  1.00 23.24           O  
-ATOM   2625  CB  PRO A 337      10.034  59.137  81.907  1.00 30.53           C  
-ATOM   2626  CG  PRO A 337      10.666  58.168  80.935  1.00 26.46           C  
-ATOM   2627  CD  PRO A 337       9.936  58.505  79.663  1.00 27.63           C  
-ATOM   2628  N   GLY A 338      11.107  62.424  82.000  1.00 17.23           N  
-ATOM   2629  CA  GLY A 338      12.241  63.288  82.281  1.00 17.37           C  
-ATOM   2630  C   GLY A 338      12.277  64.539  81.424  1.00 19.59           C  
-ATOM   2631  O   GLY A 338      13.072  65.449  81.670  1.00 21.81           O  
-ATOM   2632  N   PHE A 339      11.410  64.583  80.417  1.00 22.09           N  
-ATOM   2633  CA  PHE A 339      11.331  65.718  79.504  1.00 19.47           C  
-ATOM   2634  C   PHE A 339      10.127  66.596  79.796  1.00 22.76           C  
-ATOM   2635  O   PHE A 339       9.024  66.103  80.054  1.00 26.89           O  
-ATOM   2636  CB  PHE A 339      11.242  65.241  78.048  1.00 17.65           C  
-ATOM   2637  CG  PHE A 339      12.462  64.513  77.569  1.00 12.98           C  
-ATOM   2638  CD1 PHE A 339      12.574  63.139  77.734  1.00 14.30           C  
-ATOM   2639  CD2 PHE A 339      13.500  65.200  76.952  1.00 14.75           C  
-ATOM   2640  CE1 PHE A 339      13.701  62.459  77.291  1.00 14.68           C  
-ATOM   2641  CE2 PHE A 339      14.633  64.529  76.504  1.00  8.93           C  
-ATOM   2642  CZ  PHE A 339      14.734  63.157  76.675  1.00 15.48           C  
-ATOM   2643  N   SER A 340      10.352  67.904  79.741  1.00 21.47           N  
-ATOM   2644  CA  SER A 340       9.302  68.887  79.957  1.00 19.89           C  
-ATOM   2645  C   SER A 340       9.654  70.169  79.212  1.00 18.76           C  
-ATOM   2646  O   SER A 340      10.826  70.474  78.987  1.00 16.26           O  
-ATOM   2647  CB  SER A 340       9.062  69.148  81.449  1.00 21.27           C  
-ATOM   2648  OG  SER A 340      10.262  69.381  82.153  1.00 27.52           O  
-ATOM   2649  N   LYS A 341       8.621  70.883  78.785  1.00 13.15           N  
-ATOM   2650  CA  LYS A 341       8.772  72.111  78.019  1.00 17.91           C  
-ATOM   2651  C   LYS A 341       9.508  73.224  78.752  1.00 18.79           C  
-ATOM   2652  O   LYS A 341      10.283  73.965  78.145  1.00 19.54           O  
-ATOM   2653  CB  LYS A 341       7.388  72.618  77.588  1.00 22.21           C  
-ATOM   2654  CG  LYS A 341       7.417  73.786  76.607  1.00 23.65           C  
-ATOM   2655  CD  LYS A 341       6.023  74.277  76.274  1.00 24.72           C  
-ATOM   2656  CE  LYS A 341       5.394  75.049  77.424  1.00 35.29           C  
-ATOM   2657  NZ  LYS A 341       6.098  76.335  77.676  1.00 37.56           N  
-ATOM   2658  N   ASP A 342       9.323  73.303  80.066  1.00 24.03           N  
-ATOM   2659  CA  ASP A 342       9.933  74.382  80.837  1.00 23.37           C  
-ATOM   2660  C   ASP A 342      11.204  74.113  81.645  1.00 20.50           C  
-ATOM   2661  O   ASP A 342      11.678  74.998  82.351  1.00 19.17           O  
-ATOM   2662  CB  ASP A 342       8.864  75.070  81.695  1.00 27.92           C  
-ATOM   2663  CG  ASP A 342       7.764  75.675  80.860  1.00 29.86           C  
-ATOM   2664  OD1 ASP A 342       8.070  76.315  79.843  1.00 39.39           O  
-ATOM   2665  OD2 ASP A 342       6.590  75.495  81.211  1.00 40.20           O  
-ATOM   2666  N   SER A 343      11.749  72.905  81.552  1.00 20.43           N  
-ATOM   2667  CA  SER A 343      12.991  72.591  82.253  1.00 20.61           C  
-ATOM   2668  C   SER A 343      14.050  72.273  81.198  1.00 23.02           C  
-ATOM   2669  O   SER A 343      13.714  71.980  80.046  1.00 19.90           O  
-ATOM   2670  CB  SER A 343      12.822  71.394  83.190  1.00 24.60           C  
-ATOM   2671  OG  SER A 343      12.853  70.166  82.488  1.00 29.85           O  
-ATOM   2672  N   GLU A 344      15.323  72.350  81.584  1.00 25.98           N  
-ATOM   2673  CA  GLU A 344      16.436  72.054  80.679  1.00 23.76           C  
-ATOM   2674  C   GLU A 344      16.397  70.588  80.257  1.00 24.25           C  
-ATOM   2675  O   GLU A 344      17.115  70.177  79.345  1.00 23.17           O  
-ATOM   2676  CB  GLU A 344      17.766  72.354  81.370  1.00 30.92           C  
-ATOM   2677  CG  GLU A 344      18.584  73.453  80.710  1.00 44.41           C  
-ATOM   2678  CD  GLU A 344      19.962  73.594  81.338  1.00 56.86           C  
-ATOM   2679  OE1 GLU A 344      20.046  74.041  82.504  1.00 65.39           O  
-ATOM   2680  OE2 GLU A 344      20.961  73.252  80.667  1.00 59.88           O  
-ATOM   2681  N   SER A 345      15.564  69.812  80.951  1.00 23.75           N  
-ATOM   2682  CA  SER A 345      15.375  68.388  80.700  1.00 24.76           C  
-ATOM   2683  C   SER A 345      16.655  67.555  80.671  1.00 27.27           C  
-ATOM   2684  O   SER A 345      16.909  66.822  79.714  1.00 31.40           O  
-ATOM   2685  CB  SER A 345      14.554  68.167  79.429  1.00  9.49           C  
-ATOM   2686  OG  SER A 345      13.264  68.740  79.552  1.00 25.12           O  
-ATOM   2687  N   LYS A 346      17.464  67.682  81.720  1.00 27.68           N  
-ATOM   2688  CA  LYS A 346      18.695  66.911  81.831  1.00 26.38           C  
-ATOM   2689  C   LYS A 346      18.235  65.503  82.200  1.00 28.30           C  
-ATOM   2690  O   LYS A 346      17.486  65.315  83.160  1.00 35.26           O  
-ATOM   2691  CB  LYS A 346      19.609  67.499  82.907  1.00 30.62           C  
-ATOM   2692  CG  LYS A 346      20.117  68.897  82.576  1.00 34.94           C  
-ATOM   2693  CD  LYS A 346      20.981  69.459  83.702  1.00 48.17           C  
-ATOM   2694  CE  LYS A 346      21.457  70.875  83.384  1.00 50.56           C  
-ATOM   2695  NZ  LYS A 346      22.334  71.436  84.450  1.00 48.93           N  
-ATOM   2696  N   ILE A 347      18.643  64.526  81.399  1.00 31.29           N  
-ATOM   2697  CA  ILE A 347      18.226  63.142  81.597  1.00 31.58           C  
-ATOM   2698  C   ILE A 347      19.161  62.259  82.425  1.00 33.12           C  
-ATOM   2699  O   ILE A 347      20.378  62.233  82.215  1.00 29.43           O  
-ATOM   2700  CB  ILE A 347      17.916  62.482  80.219  1.00 29.93           C  
-ATOM   2701  CG1 ILE A 347      16.759  63.223  79.551  1.00 26.22           C  
-ATOM   2702  CG2 ILE A 347      17.541  61.021  80.374  1.00 28.61           C  
-ATOM   2703  CD1 ILE A 347      15.512  63.302  80.413  1.00 22.97           C  
-ATOM   2704  N   SER A 348      18.565  61.536  83.372  1.00 34.23           N  
-ATOM   2705  CA  SER A 348      19.300  60.626  84.243  1.00 34.19           C  
-ATOM   2706  C   SER A 348      19.538  59.311  83.513  1.00 39.71           C  
-ATOM   2707  O   SER A 348      18.845  58.997  82.545  1.00 44.66           O  
-ATOM   2708  CB  SER A 348      18.512  60.357  85.529  1.00 30.95           C  
-ATOM   2709  OG  SER A 348      17.317  59.642  85.265  1.00 25.75           O  
-ATOM   2710  N   ARG A 349      20.509  58.542  83.994  1.00 42.44           N  
-ATOM   2711  CA  ARG A 349      20.842  57.256  83.401  1.00 40.30           C  
-ATOM   2712  C   ARG A 349      19.615  56.348  83.358  1.00 42.79           C  
-ATOM   2713  O   ARG A 349      19.416  55.606  82.399  1.00 38.90           O  
-ATOM   2714  CB  ARG A 349      21.950  56.588  84.214  1.00 47.40           C  
-ATOM   2715  CG  ARG A 349      22.632  55.465  83.483  1.00 48.50           C  
-ATOM   2716  CD  ARG A 349      23.404  56.018  82.310  1.00 46.19           C  
-ATOM   2717  NE  ARG A 349      23.697  54.984  81.328  1.00 47.31           N  
-ATOM   2718  CZ  ARG A 349      23.882  55.219  80.034  1.00 48.72           C  
-ATOM   2719  NH1 ARG A 349      23.811  56.456  79.559  1.00 40.64           N  
-ATOM   2720  NH2 ARG A 349      24.116  54.210  79.207  1.00 56.42           N  
-ATOM   2721  N   GLU A 350      18.795  56.419  84.402  1.00 47.29           N  
-ATOM   2722  CA  GLU A 350      17.584  55.611  84.502  1.00 51.85           C  
-ATOM   2723  C   GLU A 350      16.550  56.017  83.453  1.00 48.05           C  
-ATOM   2724  O   GLU A 350      15.906  55.157  82.850  1.00 50.26           O  
-ATOM   2725  CB  GLU A 350      16.976  55.718  85.907  1.00 60.73           C  
-ATOM   2726  CG  GLU A 350      17.746  54.963  86.999  1.00 68.81           C  
-ATOM   2727  CD  GLU A 350      19.161  55.478  87.204  1.00 73.03           C  
-ATOM   2728  OE1 GLU A 350      19.332  56.694  87.436  1.00 69.29           O  
-ATOM   2729  OE2 GLU A 350      20.103  54.660  87.139  1.00 79.71           O  
-ATOM   2730  N   ASP A 351      16.396  57.325  83.241  1.00 44.12           N  
-ATOM   2731  CA  ASP A 351      15.439  57.835  82.259  1.00 40.27           C  
-ATOM   2732  C   ASP A 351      15.927  57.619  80.831  1.00 35.30           C  
-ATOM   2733  O   ASP A 351      15.124  57.529  79.903  1.00 33.33           O  
-ATOM   2734  CB  ASP A 351      15.144  59.320  82.501  1.00 40.34           C  
-ATOM   2735  CG  ASP A 351      14.088  59.542  83.571  1.00 44.01           C  
-ATOM   2736  OD1 ASP A 351      13.263  58.632  83.800  1.00 47.55           O  
-ATOM   2737  OD2 ASP A 351      14.071  60.636  84.173  1.00 43.45           O  
-ATOM   2738  N   PHE A 352      17.244  57.537  80.663  1.00 33.11           N  
-ATOM   2739  CA  PHE A 352      17.835  57.315  79.350  1.00 28.88           C  
-ATOM   2740  C   PHE A 352      17.469  55.913  78.869  1.00 33.83           C  
-ATOM   2741  O   PHE A 352      17.026  55.734  77.735  1.00 37.94           O  
-ATOM   2742  CB  PHE A 352      19.353  57.457  79.422  1.00 24.91           C  
-ATOM   2743  CG  PHE A 352      20.042  57.255  78.103  1.00 21.76           C  
-ATOM   2744  CD1 PHE A 352      20.155  58.305  77.198  1.00 18.58           C  
-ATOM   2745  CD2 PHE A 352      20.574  56.016  77.763  1.00 19.11           C  
-ATOM   2746  CE1 PHE A 352      20.787  58.126  75.972  1.00 15.23           C  
-ATOM   2747  CE2 PHE A 352      21.208  55.825  76.539  1.00 16.07           C  
-ATOM   2748  CZ  PHE A 352      21.315  56.884  75.641  1.00 18.39           C  
-ATOM   2749  N   MET A 353      17.668  54.929  79.746  1.00 38.81           N  
-ATOM   2750  CA  MET A 353      17.357  53.528  79.464  1.00 39.33           C  
-ATOM   2751  C   MET A 353      15.871  53.379  79.138  1.00 39.20           C  
-ATOM   2752  O   MET A 353      15.488  52.554  78.306  1.00 40.39           O  
-ATOM   2753  CB  MET A 353      17.698  52.660  80.680  1.00 51.73           C  
-ATOM   2754  CG  MET A 353      19.175  52.614  81.048  1.00 60.17           C  
-ATOM   2755  SD  MET A 353      20.117  51.473  80.028  1.00 76.12           S  
-ATOM   2756  CE  MET A 353      20.140  50.008  81.095  1.00 69.58           C  
-ATOM   2757  N   SER A 354      15.041  54.170  79.818  1.00 31.96           N  
-ATOM   2758  CA  SER A 354      13.598  54.153  79.602  1.00 32.05           C  
-ATOM   2759  C   SER A 354      13.267  54.772  78.247  1.00 31.03           C  
-ATOM   2760  O   SER A 354      12.351  54.327  77.554  1.00 30.25           O  
-ATOM   2761  CB  SER A 354      12.884  54.932  80.707  1.00 29.36           C  
-ATOM   2762  OG  SER A 354      13.067  54.309  81.965  1.00 47.94           O  
-ATOM   2763  N   GLY A 355      14.026  55.804  77.885  1.00 25.30           N  
-ATOM   2764  CA  GLY A 355      13.822  56.478  76.620  1.00 21.62           C  
-ATOM   2765  C   GLY A 355      14.132  55.560  75.455  1.00 22.17           C  
-ATOM   2766  O   GLY A 355      13.409  55.553  74.462  1.00 23.89           O  
-ATOM   2767  N   VAL A 356      15.195  54.769  75.587  1.00 20.30           N  
-ATOM   2768  CA  VAL A 356      15.606  53.834  74.542  1.00 23.74           C  
-ATOM   2769  C   VAL A 356      14.507  52.806  74.278  1.00 27.02           C  
-ATOM   2770  O   VAL A 356      14.192  52.499  73.128  1.00 29.51           O  
-ATOM   2771  CB  VAL A 356      16.908  53.093  74.935  1.00 21.87           C  
-ATOM   2772  CG1 VAL A 356      17.296  52.078  73.861  1.00 18.08           C  
-ATOM   2773  CG2 VAL A 356      18.028  54.094  75.152  1.00 21.56           C  
-ATOM   2774  N   LYS A 357      13.915  52.304  75.357  1.00 31.84           N  
-ATOM   2775  CA  LYS A 357      12.847  51.312  75.286  1.00 34.16           C  
-ATOM   2776  C   LYS A 357      11.677  51.828  74.450  1.00 30.92           C  
-ATOM   2777  O   LYS A 357      11.146  51.110  73.601  1.00 34.25           O  
-ATOM   2778  CB  LYS A 357      12.366  50.981  76.703  1.00 39.71           C  
-ATOM   2779  CG  LYS A 357      12.415  49.502  77.074  1.00 37.09           C  
-ATOM   2780  CD  LYS A 357      11.391  48.695  76.296  1.00 42.01           C  
-ATOM   2781  CE  LYS A 357      11.081  47.374  76.992  1.00 44.84           C  
-ATOM   2782  NZ  LYS A 357      12.252  46.453  77.085  1.00 54.53           N  
-ATOM   2783  N   LEU A 358      11.302  53.085  74.683  1.00 23.95           N  
-ATOM   2784  CA  LEU A 358      10.197  53.719  73.973  1.00 20.76           C  
-ATOM   2785  C   LEU A 358      10.531  54.062  72.522  1.00 18.74           C  
-ATOM   2786  O   LEU A 358       9.651  54.059  71.663  1.00 20.20           O  
-ATOM   2787  CB  LEU A 358       9.775  55.003  74.696  1.00 18.44           C  
-ATOM   2788  CG  LEU A 358       9.219  54.951  76.122  1.00 19.29           C  
-ATOM   2789  CD1 LEU A 358       8.945  56.365  76.605  1.00 10.13           C  
-ATOM   2790  CD2 LEU A 358       7.951  54.121  76.167  1.00 11.80           C  
-ATOM   2791  N   SER A 359      11.798  54.369  72.261  1.00 17.24           N  
-ATOM   2792  CA  SER A 359      12.247  54.754  70.926  1.00 17.40           C  
-ATOM   2793  C   SER A 359      12.360  53.602  69.936  1.00 19.12           C  
-ATOM   2794  O   SER A 359      12.168  53.788  68.735  1.00 20.11           O  
-ATOM   2795  CB  SER A 359      13.581  55.488  71.016  1.00 19.39           C  
-ATOM   2796  OG  SER A 359      13.458  56.646  71.818  1.00 18.46           O  
-ATOM   2797  N   VAL A 360      12.686  52.418  70.443  1.00 18.78           N  
-ATOM   2798  CA  VAL A 360      12.825  51.232  69.607  1.00 20.14           C  
-ATOM   2799  C   VAL A 360      11.958  50.132  70.219  1.00 21.94           C  
-ATOM   2800  O   VAL A 360      12.469  49.142  70.740  1.00 27.10           O  
-ATOM   2801  CB  VAL A 360      14.298  50.761  69.554  1.00 18.00           C  
-ATOM   2802  CG1 VAL A 360      14.518  49.872  68.344  1.00 19.50           C  
-ATOM   2803  CG2 VAL A 360      15.245  51.953  69.527  1.00 17.78           C  
-ATOM   2804  N   PRO A 361      10.624  50.286  70.132  1.00 26.37           N  
-ATOM   2805  CA  PRO A 361       9.658  49.326  70.679  1.00 30.73           C  
-ATOM   2806  C   PRO A 361       9.778  47.888  70.177  1.00 35.51           C  
-ATOM   2807  O   PRO A 361       9.648  46.946  70.962  1.00 31.43           O  
-ATOM   2808  CB  PRO A 361       8.313  49.953  70.302  1.00 31.05           C  
-ATOM   2809  CG  PRO A 361       8.619  50.668  69.033  1.00 29.08           C  
-ATOM   2810  CD  PRO A 361       9.929  51.333  69.366  1.00 31.11           C  
-ATOM   2811  N   HIS A 362      10.051  47.724  68.885  1.00 42.45           N  
-ATOM   2812  CA  HIS A 362      10.178  46.399  68.280  1.00 52.62           C  
-ATOM   2813  C   HIS A 362      11.529  45.712  68.531  1.00 51.89           C  
-ATOM   2814  O   HIS A 362      11.892  44.769  67.823  1.00 50.60           O  
-ATOM   2815  CB  HIS A 362       9.898  46.480  66.771  1.00 60.50           C  
-ATOM   2816  CG  HIS A 362      10.890  47.309  66.008  1.00 72.05           C  
-ATOM   2817  ND1 HIS A 362      10.813  48.683  65.930  1.00 75.36           N  
-ATOM   2818  CD2 HIS A 362      11.969  46.952  65.271  1.00 75.49           C  
-ATOM   2819  CE1 HIS A 362      11.800  49.137  65.178  1.00 78.42           C  
-ATOM   2820  NE2 HIS A 362      12.516  48.107  64.765  1.00 76.08           N  
-ATOM   2821  N   ALA A 363      12.245  46.156  69.563  1.00 47.91           N  
-ATOM   2822  CA  ALA A 363      13.552  45.591  69.888  1.00 44.86           C  
-ATOM   2823  C   ALA A 363      13.590  44.768  71.168  1.00 39.97           C  
-ATOM   2824  O   ALA A 363      12.842  45.024  72.105  1.00 42.15           O  
-ATOM   2825  CB  ALA A 363      14.593  46.696  69.962  1.00 41.99           C  
-ATOM   2826  N   ASN A 364      14.481  43.780  71.190  1.00 35.39           N  
-ATOM   2827  CA  ASN A 364      14.672  42.921  72.353  1.00 33.25           C  
-ATOM   2828  C   ASN A 364      15.771  43.511  73.246  1.00 34.31           C  
-ATOM   2829  O   ASN A 364      16.255  44.614  72.986  1.00 35.93           O  
-ATOM   2830  CB  ASN A 364      15.024  41.489  71.916  1.00 31.16           C  
-ATOM   2831  CG  ASN A 364      16.316  41.398  71.098  1.00 31.25           C  
-ATOM   2832  OD1 ASN A 364      16.858  42.419  70.682  1.00 28.17           O  
-ATOM   2833  ND2 ASN A 364      16.817  40.188  70.879  1.00 36.17           N  
-ATOM   2834  N   ASP A 365      16.177  42.779  74.281  1.00 35.13           N  
-ATOM   2835  CA  ASP A 365      17.212  43.263  75.198  1.00 37.32           C  
-ATOM   2836  C   ASP A 365      18.591  43.485  74.582  1.00 31.86           C  
-ATOM   2837  O   ASP A 365      19.268  44.456  74.916  1.00 32.83           O  
-ATOM   2838  CB  ASP A 365      17.321  42.354  76.424  1.00 44.88           C  
-ATOM   2839  CG  ASP A 365      16.139  42.502  77.364  1.00 54.80           C  
-ATOM   2840  OD1 ASP A 365      15.795  43.650  77.722  1.00 57.17           O  
-ATOM   2841  OD2 ASP A 365      15.551  41.469  77.742  1.00 65.54           O  
-ATOM   2842  N   LEU A 366      19.013  42.586  73.697  1.00 28.33           N  
-ATOM   2843  CA  LEU A 366      20.313  42.717  73.045  1.00 24.77           C  
-ATOM   2844  C   LEU A 366      20.273  43.970  72.168  1.00 26.05           C  
-ATOM   2845  O   LEU A 366      21.243  44.726  72.098  1.00 27.98           O  
-ATOM   2846  CB  LEU A 366      20.606  41.491  72.176  1.00 26.15           C  
-ATOM   2847  CG  LEU A 366      22.039  40.952  72.085  1.00 23.12           C  
-ATOM   2848  CD1 LEU A 366      22.139  40.083  70.842  1.00 31.01           C  
-ATOM   2849  CD2 LEU A 366      23.067  42.063  72.013  1.00 29.83           C  
-ATOM   2850  N   GLY A 367      19.135  44.179  71.511  1.00 24.85           N  
-ATOM   2851  CA  GLY A 367      18.958  45.341  70.661  1.00 22.11           C  
-ATOM   2852  C   GLY A 367      18.984  46.624  71.469  1.00 23.20           C  
-ATOM   2853  O   GLY A 367      19.563  47.618  71.037  1.00 22.88           O  
-ATOM   2854  N   LEU A 368      18.373  46.597  72.653  1.00 23.94           N  
-ATOM   2855  CA  LEU A 368      18.335  47.762  73.535  1.00 22.01           C  
-ATOM   2856  C   LEU A 368      19.742  48.102  74.007  1.00 26.12           C  
-ATOM   2857  O   LEU A 368      20.106  49.275  74.110  1.00 29.07           O  
-ATOM   2858  CB  LEU A 368      17.446  47.493  74.747  1.00 25.26           C  
-ATOM   2859  CG  LEU A 368      15.952  47.294  74.489  1.00 22.55           C  
-ATOM   2860  CD1 LEU A 368      15.262  46.922  75.788  1.00 21.54           C  
-ATOM   2861  CD2 LEU A 368      15.343  48.556  73.895  1.00 22.14           C  
-ATOM   2862  N   ASP A 369      20.522  47.063  74.300  1.00 24.42           N  
-ATOM   2863  CA  ASP A 369      21.902  47.225  74.740  1.00 26.94           C  
-ATOM   2864  C   ASP A 369      22.752  47.746  73.588  1.00 23.98           C  
-ATOM   2865  O   ASP A 369      23.655  48.554  73.792  1.00 25.07           O  
-ATOM   2866  CB  ASP A 369      22.469  45.888  75.231  1.00 29.65           C  
-ATOM   2867  CG  ASP A 369      22.020  45.537  76.639  1.00 30.41           C  
-ATOM   2868  OD1 ASP A 369      21.098  46.192  77.173  1.00 34.29           O  
-ATOM   2869  OD2 ASP A 369      22.606  44.602  77.219  1.00 39.79           O  
-ATOM   2870  N   ALA A 370      22.448  47.280  72.381  1.00 17.72           N  
-ATOM   2871  CA  ALA A 370      23.174  47.690  71.191  1.00 15.35           C  
-ATOM   2872  C   ALA A 370      22.970  49.174  70.922  1.00 17.88           C  
-ATOM   2873  O   ALA A 370      23.927  49.885  70.604  1.00 20.57           O  
-ATOM   2874  CB  ALA A 370      22.725  46.872  69.998  1.00 20.16           C  
-ATOM   2875  N   VAL A 371      21.726  49.636  71.063  1.00 14.76           N  
-ATOM   2876  CA  VAL A 371      21.390  51.044  70.837  1.00 16.12           C  
-ATOM   2877  C   VAL A 371      22.091  51.913  71.876  1.00 18.54           C  
-ATOM   2878  O   VAL A 371      22.687  52.943  71.544  1.00 18.55           O  
-ATOM   2879  CB  VAL A 371      19.854  51.293  70.927  1.00 19.23           C  
-ATOM   2880  CG1 VAL A 371      19.541  52.790  70.833  1.00  8.54           C  
-ATOM   2881  CG2 VAL A 371      19.133  50.536  69.826  1.00  5.64           C  
-ATOM   2882  N   THR A 372      22.031  51.471  73.128  1.00 17.13           N  
-ATOM   2883  CA  THR A 372      22.643  52.186  74.238  1.00 19.63           C  
-ATOM   2884  C   THR A 372      24.156  52.293  74.038  1.00 22.04           C  
-ATOM   2885  O   THR A 372      24.730  53.370  74.168  1.00 23.67           O  
-ATOM   2886  CB  THR A 372      22.325  51.485  75.581  1.00 24.29           C  
-ATOM   2887  OG1 THR A 372      20.904  51.407  75.752  1.00 24.14           O  
-ATOM   2888  CG2 THR A 372      22.910  52.257  76.748  1.00 20.80           C  
-ATOM   2889  N   LEU A 373      24.783  51.188  73.653  1.00 21.91           N  
-ATOM   2890  CA  LEU A 373      26.222  51.159  73.428  1.00 21.39           C  
-ATOM   2891  C   LEU A 373      26.598  52.173  72.351  1.00 26.68           C  
-ATOM   2892  O   LEU A 373      27.567  52.921  72.499  1.00 32.99           O  
-ATOM   2893  CB  LEU A 373      26.656  49.760  72.984  1.00 19.83           C  
-ATOM   2894  CG  LEU A 373      28.157  49.537  72.799  1.00 22.36           C  
-ATOM   2895  CD1 LEU A 373      28.797  49.309  74.154  1.00 16.86           C  
-ATOM   2896  CD2 LEU A 373      28.409  48.348  71.887  1.00 26.59           C  
-ATOM   2897  N   GLN A 374      25.796  52.214  71.289  1.00 25.71           N  
-ATOM   2898  CA  GLN A 374      26.021  53.110  70.158  1.00 23.94           C  
-ATOM   2899  C   GLN A 374      25.971  54.596  70.513  1.00 22.67           C  
-ATOM   2900  O   GLN A 374      26.716  55.401  69.953  1.00 19.97           O  
-ATOM   2901  CB  GLN A 374      24.996  52.809  69.059  1.00 23.14           C  
-ATOM   2902  CG  GLN A 374      25.160  53.619  67.777  1.00 19.71           C  
-ATOM   2903  CD  GLN A 374      26.456  53.316  67.040  1.00 21.85           C  
-ATOM   2904  OE1 GLN A 374      26.935  54.135  66.261  1.00 37.51           O  
-ATOM   2905  NE2 GLN A 374      27.018  52.133  67.269  1.00 25.91           N  
-ATOM   2906  N   TYR A 375      25.105  54.956  71.454  1.00 25.17           N  
-ATOM   2907  CA  TYR A 375      24.948  56.352  71.843  1.00 22.51           C  
-ATOM   2908  C   TYR A 375      25.458  56.731  73.232  1.00 26.35           C  
-ATOM   2909  O   TYR A 375      25.110  57.796  73.748  1.00 33.47           O  
-ATOM   2910  CB  TYR A 375      23.475  56.750  71.712  1.00 24.00           C  
-ATOM   2911  CG  TYR A 375      22.994  56.830  70.283  1.00 22.48           C  
-ATOM   2912  CD1 TYR A 375      22.540  55.693  69.610  1.00 21.78           C  
-ATOM   2913  CD2 TYR A 375      23.016  58.041  69.591  1.00 21.83           C  
-ATOM   2914  CE1 TYR A 375      22.125  55.763  68.284  1.00 14.38           C  
-ATOM   2915  CE2 TYR A 375      22.605  58.120  68.271  1.00 18.72           C  
-ATOM   2916  CZ  TYR A 375      22.163  56.981  67.625  1.00 16.86           C  
-ATOM   2917  OH  TYR A 375      21.771  57.079  66.319  1.00 18.10           O  
-ATOM   2918  N   THR A 376      26.306  55.899  73.827  1.00 23.68           N  
-ATOM   2919  CA  THR A 376      26.809  56.200  75.160  1.00 19.50           C  
-ATOM   2920  C   THR A 376      28.302  56.458  75.256  1.00 21.99           C  
-ATOM   2921  O   THR A 376      29.123  55.755  74.659  1.00 25.47           O  
-ATOM   2922  CB  THR A 376      26.425  55.105  76.179  1.00 19.06           C  
-ATOM   2923  OG1 THR A 376      25.000  54.989  76.236  1.00 31.48           O  
-ATOM   2924  CG2 THR A 376      26.922  55.456  77.568  1.00 17.25           C  
-ATOM   2925  N   ASP A 377      28.629  57.507  76.004  1.00 25.87           N  
-ATOM   2926  CA  ASP A 377      30.004  57.902  76.263  1.00 24.00           C  
-ATOM   2927  C   ASP A 377      30.289  57.339  77.650  1.00 25.80           C  
-ATOM   2928  O   ASP A 377      29.875  57.917  78.655  1.00 26.25           O  
-ATOM   2929  CB  ASP A 377      30.114  59.431  76.275  1.00 20.32           C  
-ATOM   2930  CG  ASP A 377      31.530  59.924  76.543  1.00 28.42           C  
-ATOM   2931  OD1 ASP A 377      32.472  59.106  76.599  1.00 27.92           O  
-ATOM   2932  OD2 ASP A 377      31.702  61.148  76.701  1.00 27.75           O  
-ATOM   2933  N   TRP A 378      30.963  56.193  77.695  1.00 23.91           N  
-ATOM   2934  CA  TRP A 378      31.280  55.533  78.958  1.00 27.69           C  
-ATOM   2935  C   TRP A 378      32.318  56.258  79.811  1.00 29.73           C  
-ATOM   2936  O   TRP A 378      32.524  55.917  80.976  1.00 34.03           O  
-ATOM   2937  CB  TRP A 378      31.686  54.082  78.702  1.00 24.08           C  
-ATOM   2938  CG  TRP A 378      30.584  53.304  78.058  1.00 36.25           C  
-ATOM   2939  CD1 TRP A 378      30.532  52.869  76.764  1.00 40.19           C  
-ATOM   2940  CD2 TRP A 378      29.346  52.911  78.664  1.00 36.65           C  
-ATOM   2941  NE1 TRP A 378      29.335  52.235  76.525  1.00 41.01           N  
-ATOM   2942  CE2 TRP A 378      28.589  52.246  77.674  1.00 37.43           C  
-ATOM   2943  CE3 TRP A 378      28.802  53.060  79.947  1.00 37.28           C  
-ATOM   2944  CZ2 TRP A 378      27.313  51.729  77.926  1.00 39.69           C  
-ATOM   2945  CZ3 TRP A 378      27.533  52.546  80.199  1.00 40.44           C  
-ATOM   2946  CH2 TRP A 378      26.804  51.888  79.191  1.00 44.38           C  
-ATOM   2947  N   MET A 379      32.952  57.270  79.226  1.00 35.10           N  
-ATOM   2948  CA  MET A 379      33.950  58.070  79.922  1.00 39.94           C  
-ATOM   2949  C   MET A 379      33.222  59.096  80.795  1.00 40.94           C  
-ATOM   2950  O   MET A 379      33.805  59.667  81.714  1.00 49.20           O  
-ATOM   2951  CB  MET A 379      34.841  58.786  78.899  1.00 46.87           C  
-ATOM   2952  CG  MET A 379      36.128  59.376  79.460  1.00 61.06           C  
-ATOM   2953  SD  MET A 379      37.396  58.141  79.806  1.00 67.59           S  
-ATOM   2954  CE  MET A 379      38.313  58.162  78.244  1.00 70.54           C  
-ATOM   2955  N   ASP A 380      31.934  59.294  80.515  1.00 42.19           N  
-ATOM   2956  CA  ASP A 380      31.096  60.252  81.237  1.00 41.53           C  
-ATOM   2957  C   ASP A 380      29.629  59.852  81.028  1.00 41.82           C  
-ATOM   2958  O   ASP A 380      28.858  60.574  80.395  1.00 40.63           O  
-ATOM   2959  CB  ASP A 380      31.355  61.664  80.687  1.00 39.57           C  
-ATOM   2960  CG  ASP A 380      30.681  62.759  81.506  1.00 45.82           C  
-ATOM   2961  OD1 ASP A 380      30.453  62.572  82.723  1.00 53.75           O  
-ATOM   2962  OD2 ASP A 380      30.394  63.824  80.925  1.00 41.73           O  
-ATOM   2963  N   ASP A 381      29.253  58.700  81.583  1.00 45.91           N  
-ATOM   2964  CA  ASP A 381      27.900  58.158  81.442  1.00 47.55           C  
-ATOM   2965  C   ASP A 381      26.764  58.821  82.232  1.00 49.89           C  
-ATOM   2966  O   ASP A 381      25.591  58.662  81.882  1.00 41.53           O  
-ATOM   2967  CB  ASP A 381      27.910  56.646  81.713  1.00 49.69           C  
-ATOM   2968  CG  ASP A 381      28.383  56.301  83.116  1.00 55.25           C  
-ATOM   2969  OD1 ASP A 381      29.582  56.498  83.414  1.00 58.36           O  
-ATOM   2970  OD2 ASP A 381      27.554  55.819  83.916  1.00 57.69           O  
-ATOM   2971  N   ASN A 382      27.100  59.548  83.295  1.00 55.43           N  
-ATOM   2972  CA  ASN A 382      26.079  60.212  84.109  1.00 56.79           C  
-ATOM   2973  C   ASN A 382      25.853  61.682  83.760  1.00 53.99           C  
-ATOM   2974  O   ASN A 382      25.348  62.454  84.577  1.00 57.35           O  
-ATOM   2975  CB  ASN A 382      26.390  60.053  85.602  1.00 58.49           C  
-ATOM   2976  CG  ASN A 382      26.201  58.625  86.090  1.00 59.95           C  
-ATOM   2977  OD1 ASN A 382      27.103  58.034  86.685  1.00 66.01           O  
-ATOM   2978  ND2 ASN A 382      25.020  58.064  85.840  1.00 52.69           N  
-ATOM   2979  N   ASN A 383      26.211  62.056  82.534  1.00 48.26           N  
-ATOM   2980  CA  ASN A 383      26.042  63.424  82.051  1.00 40.92           C  
-ATOM   2981  C   ASN A 383      24.595  63.631  81.599  1.00 36.97           C  
-ATOM   2982  O   ASN A 383      24.132  62.979  80.663  1.00 35.65           O  
-ATOM   2983  CB  ASN A 383      26.996  63.681  80.881  1.00 40.13           C  
-ATOM   2984  CG  ASN A 383      27.020  65.138  80.450  1.00 39.07           C  
-ATOM   2985  OD1 ASN A 383      26.003  65.828  80.473  1.00 39.85           O  
-ATOM   2986  ND2 ASN A 383      28.191  65.608  80.045  1.00 35.95           N  
-ATOM   2987  N   GLY A 384      23.904  64.563  82.253  1.00 35.19           N  
-ATOM   2988  CA  GLY A 384      22.513  64.849  81.934  1.00 31.43           C  
-ATOM   2989  C   GLY A 384      22.259  65.438  80.557  1.00 29.90           C  
-ATOM   2990  O   GLY A 384      21.239  65.141  79.928  1.00 29.79           O  
-ATOM   2991  N   ILE A 385      23.167  66.295  80.100  1.00 28.04           N  
-ATOM   2992  CA  ILE A 385      23.040  66.920  78.789  1.00 25.46           C  
-ATOM   2993  C   ILE A 385      23.379  65.932  77.673  1.00 31.06           C  
-ATOM   2994  O   ILE A 385      22.742  65.945  76.619  1.00 34.17           O  
-ATOM   2995  CB  ILE A 385      23.919  68.182  78.684  1.00 20.38           C  
-ATOM   2996  CG1 ILE A 385      23.341  69.281  79.579  1.00 20.85           C  
-ATOM   2997  CG2 ILE A 385      24.007  68.661  77.244  1.00 13.86           C  
-ATOM   2998  CD1 ILE A 385      24.159  70.557  79.602  1.00 18.48           C  
-ATOM   2999  N   LYS A 386      24.368  65.071  77.911  1.00 33.99           N  
-ATOM   3000  CA  LYS A 386      24.764  64.069  76.922  1.00 30.90           C  
-ATOM   3001  C   LYS A 386      23.688  63.003  76.755  1.00 29.06           C  
-ATOM   3002  O   LYS A 386      23.468  62.501  75.649  1.00 31.82           O  
-ATOM   3003  CB  LYS A 386      26.095  63.415  77.298  1.00 28.81           C  
-ATOM   3004  CG  LYS A 386      27.301  64.214  76.861  1.00 32.76           C  
-ATOM   3005  CD  LYS A 386      28.605  63.540  77.240  1.00 41.33           C  
-ATOM   3006  CE  LYS A 386      29.783  64.404  76.814  1.00 36.71           C  
-ATOM   3007  NZ  LYS A 386      31.083  63.824  77.227  1.00 43.43           N  
-ATOM   3008  N   ASN A 387      23.022  62.664  77.856  1.00 27.80           N  
-ATOM   3009  CA  ASN A 387      21.957  61.672  77.833  1.00 25.10           C  
-ATOM   3010  C   ASN A 387      20.729  62.226  77.120  1.00 26.23           C  
-ATOM   3011  O   ASN A 387      20.047  61.501  76.395  1.00 26.87           O  
-ATOM   3012  CB  ASN A 387      21.596  61.238  79.256  1.00 30.49           C  
-ATOM   3013  CG  ASN A 387      22.654  60.350  79.884  1.00 31.34           C  
-ATOM   3014  OD1 ASN A 387      23.457  59.728  79.188  1.00 37.89           O  
-ATOM   3015  ND2 ASN A 387      22.655  60.280  81.209  1.00 34.76           N  
-ATOM   3016  N   ARG A 388      20.462  63.514  77.322  1.00 21.31           N  
-ATOM   3017  CA  ARG A 388      19.324  64.173  76.694  1.00 19.75           C  
-ATOM   3018  C   ARG A 388      19.546  64.264  75.184  1.00 21.22           C  
-ATOM   3019  O   ARG A 388      18.688  63.862  74.392  1.00 21.40           O  
-ATOM   3020  CB  ARG A 388      19.133  65.576  77.277  1.00 18.62           C  
-ATOM   3021  CG  ARG A 388      17.931  66.321  76.711  1.00 21.65           C  
-ATOM   3022  CD  ARG A 388      18.336  67.646  76.096  1.00 18.73           C  
-ATOM   3023  NE  ARG A 388      18.685  68.637  77.105  1.00 24.69           N  
-ATOM   3024  CZ  ARG A 388      19.676  69.515  76.982  1.00 20.49           C  
-ATOM   3025  NH1 ARG A 388      20.429  69.530  75.894  1.00 12.93           N  
-ATOM   3026  NH2 ARG A 388      19.898  70.399  77.945  1.00 32.79           N  
-ATOM   3027  N   ASP A 389      20.715  64.767  74.798  1.00 18.06           N  
-ATOM   3028  CA  ASP A 389      21.074  64.922  73.394  1.00 19.68           C  
-ATOM   3029  C   ASP A 389      21.243  63.596  72.667  1.00 20.69           C  
-ATOM   3030  O   ASP A 389      20.945  63.496  71.474  1.00 22.44           O  
-ATOM   3031  CB  ASP A 389      22.353  65.749  73.269  1.00 19.15           C  
-ATOM   3032  CG  ASP A 389      22.153  67.192  73.667  1.00 16.54           C  
-ATOM   3033  OD1 ASP A 389      20.987  67.624  73.771  1.00 18.08           O  
-ATOM   3034  OD2 ASP A 389      23.163  67.896  73.865  1.00 21.92           O  
-ATOM   3035  N   GLY A 390      21.742  62.592  73.384  1.00 17.97           N  
-ATOM   3036  CA  GLY A 390      21.941  61.280  72.796  1.00 23.52           C  
-ATOM   3037  C   GLY A 390      20.613  60.619  72.471  1.00 22.59           C  
-ATOM   3038  O   GLY A 390      20.475  59.935  71.454  1.00 26.38           O  
-ATOM   3039  N   LEU A 391      19.629  60.856  73.332  1.00 19.15           N  
-ATOM   3040  CA  LEU A 391      18.292  60.301  73.172  1.00 17.52           C  
-ATOM   3041  C   LEU A 391      17.564  61.007  72.027  1.00 19.74           C  
-ATOM   3042  O   LEU A 391      16.743  60.407  71.332  1.00 23.01           O  
-ATOM   3043  CB  LEU A 391      17.527  60.458  74.483  1.00 11.98           C  
-ATOM   3044  CG  LEU A 391      16.417  59.462  74.796  1.00 19.14           C  
-ATOM   3045  CD1 LEU A 391      16.830  58.054  74.405  1.00 23.66           C  
-ATOM   3046  CD2 LEU A 391      16.096  59.543  76.288  1.00 22.13           C  
-ATOM   3047  N   ASP A 392      17.898  62.279  71.824  1.00 21.77           N  
-ATOM   3048  CA  ASP A 392      17.313  63.085  70.759  1.00 19.93           C  
-ATOM   3049  C   ASP A 392      17.828  62.534  69.426  1.00 18.00           C  
-ATOM   3050  O   ASP A 392      17.069  62.414  68.462  1.00 24.87           O  
-ATOM   3051  CB  ASP A 392      17.734  64.549  70.935  1.00 24.03           C  
-ATOM   3052  CG  ASP A 392      16.985  65.505  70.011  1.00 31.87           C  
-ATOM   3053  OD1 ASP A 392      16.433  65.073  68.976  1.00 35.41           O  
-ATOM   3054  OD2 ASP A 392      16.961  66.713  70.323  1.00 27.59           O  
-ATOM   3055  N   ASP A 393      19.111  62.179  69.391  1.00 18.03           N  
-ATOM   3056  CA  ASP A 393      19.731  61.623  68.194  1.00 15.52           C  
-ATOM   3057  C   ASP A 393      19.168  60.246  67.873  1.00 20.85           C  
-ATOM   3058  O   ASP A 393      18.982  59.909  66.710  1.00 26.22           O  
-ATOM   3059  CB  ASP A 393      21.247  61.534  68.364  1.00 17.36           C  
-ATOM   3060  CG  ASP A 393      21.929  62.887  68.290  1.00 22.75           C  
-ATOM   3061  OD1 ASP A 393      21.372  63.813  67.667  1.00 27.61           O  
-ATOM   3062  OD2 ASP A 393      23.040  63.017  68.843  1.00 31.12           O  
-ATOM   3063  N   ILE A 394      18.885  59.461  68.908  1.00 19.47           N  
-ATOM   3064  CA  ILE A 394      18.331  58.121  68.736  1.00 20.16           C  
-ATOM   3065  C   ILE A 394      16.974  58.165  68.033  1.00 19.13           C  
-ATOM   3066  O   ILE A 394      16.753  57.452  67.054  1.00 23.57           O  
-ATOM   3067  CB  ILE A 394      18.184  57.397  70.101  1.00 21.64           C  
-ATOM   3068  CG1 ILE A 394      19.567  57.096  70.682  1.00 12.50           C  
-ATOM   3069  CG2 ILE A 394      17.371  56.115  69.951  1.00 16.11           C  
-ATOM   3070  CD1 ILE A 394      19.544  56.453  72.045  1.00 12.95           C  
-ATOM   3071  N   VAL A 395      16.085  59.024  68.524  1.00 18.86           N  
-ATOM   3072  CA  VAL A 395      14.743  59.160  67.960  1.00 15.94           C  
-ATOM   3073  C   VAL A 395      14.775  59.719  66.538  1.00 16.37           C  
-ATOM   3074  O   VAL A 395      14.077  59.220  65.653  1.00 18.13           O  
-ATOM   3075  CB  VAL A 395      13.847  60.052  68.865  1.00 20.43           C  
-ATOM   3076  CG1 VAL A 395      12.439  60.167  68.291  1.00 14.35           C  
-ATOM   3077  CG2 VAL A 395      13.788  59.472  70.269  1.00 12.05           C  
-ATOM   3078  N   GLY A 396      15.606  60.736  66.322  1.00 13.00           N  
-ATOM   3079  CA  GLY A 396      15.716  61.345  65.010  1.00  8.44           C  
-ATOM   3080  C   GLY A 396      16.348  60.435  63.971  1.00 14.91           C  
-ATOM   3081  O   GLY A 396      15.865  60.349  62.844  1.00 19.53           O  
-ATOM   3082  N   ASP A 397      17.424  59.751  64.351  1.00 12.09           N  
-ATOM   3083  CA  ASP A 397      18.121  58.853  63.440  1.00  9.17           C  
-ATOM   3084  C   ASP A 397      17.281  57.638  63.090  1.00  9.65           C  
-ATOM   3085  O   ASP A 397      17.159  57.285  61.923  1.00 15.77           O  
-ATOM   3086  CB  ASP A 397      19.459  58.406  64.038  1.00 12.12           C  
-ATOM   3087  CG  ASP A 397      20.439  59.555  64.221  1.00 12.58           C  
-ATOM   3088  OD1 ASP A 397      20.194  60.662  63.707  1.00 17.21           O  
-ATOM   3089  OD2 ASP A 397      21.466  59.352  64.891  1.00 15.81           O  
-ATOM   3090  N   HIS A 398      16.686  57.011  64.101  1.00 10.14           N  
-ATOM   3091  CA  HIS A 398      15.857  55.830  63.888  1.00 14.82           C  
-ATOM   3092  C   HIS A 398      14.582  56.108  63.088  1.00 16.75           C  
-ATOM   3093  O   HIS A 398      14.220  55.340  62.196  1.00 22.88           O  
-ATOM   3094  CB  HIS A 398      15.471  55.206  65.233  1.00  4.25           C  
-ATOM   3095  CG  HIS A 398      14.466  54.103  65.116  1.00  8.92           C  
-ATOM   3096  ND1 HIS A 398      14.709  52.948  64.406  1.00 12.02           N  
-ATOM   3097  CD2 HIS A 398      13.200  53.999  65.582  1.00 14.71           C  
-ATOM   3098  CE1 HIS A 398      13.636  52.179  64.436  1.00  9.36           C  
-ATOM   3099  NE2 HIS A 398      12.705  52.793  65.143  1.00  7.66           N  
-ATOM   3100  N   ASN A 399      13.922  57.219  63.398  1.00 15.88           N  
-ATOM   3101  CA  ASN A 399      12.668  57.567  62.755  1.00 11.42           C  
-ATOM   3102  C   ASN A 399      12.684  58.449  61.513  1.00 14.31           C  
-ATOM   3103  O   ASN A 399      11.779  58.350  60.682  1.00 13.06           O  
-ATOM   3104  CB  ASN A 399      11.733  58.176  63.792  1.00 10.03           C  
-ATOM   3105  CG  ASN A 399      11.337  57.187  64.873  1.00 15.73           C  
-ATOM   3106  OD1 ASN A 399      10.588  56.245  64.618  1.00 13.74           O  
-ATOM   3107  ND2 ASN A 399      11.830  57.404  66.089  1.00 13.92           N  
-ATOM   3108  N   VAL A 400      13.692  59.303  61.371  1.00 14.94           N  
-ATOM   3109  CA  VAL A 400      13.735  60.205  60.219  1.00 11.55           C  
-ATOM   3110  C   VAL A 400      15.012  60.175  59.386  1.00 14.05           C  
-ATOM   3111  O   VAL A 400      14.993  59.783  58.219  1.00 17.05           O  
-ATOM   3112  CB  VAL A 400      13.485  61.676  60.647  1.00 11.07           C  
-ATOM   3113  CG1 VAL A 400      13.552  62.597  59.434  1.00  7.38           C  
-ATOM   3114  CG2 VAL A 400      12.144  61.809  61.348  1.00 10.88           C  
-ATOM   3115  N   ILE A 401      16.113  60.611  59.986  1.00 16.00           N  
-ATOM   3116  CA  ILE A 401      17.391  60.687  59.294  1.00 14.03           C  
-ATOM   3117  C   ILE A 401      17.882  59.422  58.603  1.00 18.65           C  
-ATOM   3118  O   ILE A 401      18.104  59.438  57.395  1.00 19.59           O  
-ATOM   3119  CB  ILE A 401      18.491  61.255  60.216  1.00 15.45           C  
-ATOM   3120  CG1 ILE A 401      18.068  62.641  60.726  1.00  7.74           C  
-ATOM   3121  CG2 ILE A 401      19.810  61.337  59.466  1.00  8.37           C  
-ATOM   3122  CD1 ILE A 401      19.095  63.342  61.576  1.00 12.71           C  
-ATOM   3123  N   CYS A 402      18.035  58.329  59.346  1.00 18.10           N  
-ATOM   3124  CA  CYS A 402      18.525  57.092  58.743  1.00 17.39           C  
-ATOM   3125  C   CYS A 402      17.609  56.467  57.708  1.00 21.15           C  
-ATOM   3126  O   CYS A 402      18.084  56.044  56.654  1.00 26.83           O  
-ATOM   3127  CB  CYS A 402      18.956  56.082  59.800  1.00 20.58           C  
-ATOM   3128  SG  CYS A 402      20.412  56.678  60.709  1.00 20.91           S  
-ATOM   3129  N   PRO A 403      16.302  56.329  58.008  1.00 22.25           N  
-ATOM   3130  CA  PRO A 403      15.454  55.738  56.970  1.00 20.73           C  
-ATOM   3131  C   PRO A 403      15.486  56.595  55.700  1.00 22.58           C  
-ATOM   3132  O   PRO A 403      15.458  56.062  54.588  1.00 24.09           O  
-ATOM   3133  CB  PRO A 403      14.065  55.693  57.624  1.00 14.23           C  
-ATOM   3134  CG  PRO A 403      14.165  56.619  58.790  1.00 23.23           C  
-ATOM   3135  CD  PRO A 403      15.565  56.428  59.276  1.00 17.14           C  
-ATOM   3136  N   LEU A 404      15.600  57.915  55.867  1.00 20.42           N  
-ATOM   3137  CA  LEU A 404      15.676  58.814  54.717  1.00 17.13           C  
-ATOM   3138  C   LEU A 404      16.984  58.583  53.971  1.00 18.75           C  
-ATOM   3139  O   LEU A 404      16.997  58.549  52.744  1.00 17.35           O  
-ATOM   3140  CB  LEU A 404      15.559  60.286  55.134  1.00 17.91           C  
-ATOM   3141  CG  LEU A 404      15.694  61.318  53.999  1.00 15.72           C  
-ATOM   3142  CD1 LEU A 404      14.589  62.363  54.072  1.00  5.07           C  
-ATOM   3143  CD2 LEU A 404      17.062  61.979  54.040  1.00 11.39           C  
-ATOM   3144  N   MET A 405      18.075  58.397  54.713  1.00 19.39           N  
-ATOM   3145  CA  MET A 405      19.379  58.155  54.100  1.00 15.95           C  
-ATOM   3146  C   MET A 405      19.392  56.839  53.333  1.00 18.96           C  
-ATOM   3147  O   MET A 405      20.119  56.698  52.346  1.00 21.18           O  
-ATOM   3148  CB  MET A 405      20.503  58.167  55.139  1.00 11.59           C  
-ATOM   3149  CG  MET A 405      20.847  59.549  55.662  1.00 15.28           C  
-ATOM   3150  SD  MET A 405      21.056  60.765  54.345  1.00 23.73           S  
-ATOM   3151  CE  MET A 405      22.513  60.152  53.553  1.00 18.99           C  
-ATOM   3152  N   HIS A 406      18.585  55.883  53.785  1.00 18.45           N  
-ATOM   3153  CA  HIS A 406      18.497  54.593  53.117  1.00 20.39           C  
-ATOM   3154  C   HIS A 406      17.779  54.813  51.791  1.00 19.31           C  
-ATOM   3155  O   HIS A 406      18.257  54.385  50.743  1.00 29.14           O  
-ATOM   3156  CB  HIS A 406      17.733  53.584  53.977  1.00 20.95           C  
-ATOM   3157  CG  HIS A 406      17.637  52.221  53.365  1.00 24.86           C  
-ATOM   3158  ND1 HIS A 406      18.737  51.412  53.176  1.00 22.39           N  
-ATOM   3159  CD2 HIS A 406      16.573  51.524  52.896  1.00 13.86           C  
-ATOM   3160  CE1 HIS A 406      18.357  50.275  52.621  1.00 16.01           C  
-ATOM   3161  NE2 HIS A 406      17.049  50.320  52.440  1.00 18.50           N  
-ATOM   3162  N   PHE A 407      16.651  55.515  51.849  1.00 15.23           N  
-ATOM   3163  CA  PHE A 407      15.859  55.821  50.662  1.00 19.62           C  
-ATOM   3164  C   PHE A 407      16.693  56.618  49.650  1.00 19.03           C  
-ATOM   3165  O   PHE A 407      16.625  56.361  48.450  1.00 19.06           O  
-ATOM   3166  CB  PHE A 407      14.597  56.607  51.062  1.00  9.93           C  
-ATOM   3167  CG  PHE A 407      13.822  57.156  49.894  1.00 15.56           C  
-ATOM   3168  CD1 PHE A 407      12.998  56.331  49.135  1.00 16.40           C  
-ATOM   3169  CD2 PHE A 407      13.926  58.500  49.545  1.00 12.44           C  
-ATOM   3170  CE1 PHE A 407      12.289  56.839  48.043  1.00 10.28           C  
-ATOM   3171  CE2 PHE A 407      13.224  59.015  48.457  1.00 11.20           C  
-ATOM   3172  CZ  PHE A 407      12.405  58.183  47.706  1.00 12.33           C  
-ATOM   3173  N   VAL A 408      17.495  57.559  50.147  1.00 14.70           N  
-ATOM   3174  CA  VAL A 408      18.343  58.391  49.294  1.00 21.12           C  
-ATOM   3175  C   VAL A 408      19.333  57.546  48.499  1.00 23.06           C  
-ATOM   3176  O   VAL A 408      19.434  57.679  47.280  1.00 25.43           O  
-ATOM   3177  CB  VAL A 408      19.148  59.433  50.114  1.00 22.57           C  
-ATOM   3178  CG1 VAL A 408      20.031  60.259  49.198  1.00 28.79           C  
-ATOM   3179  CG2 VAL A 408      18.215  60.351  50.862  1.00 39.71           C  
-ATOM   3180  N   ASN A 409      20.056  56.674  49.194  1.00 24.39           N  
-ATOM   3181  CA  ASN A 409      21.042  55.818  48.550  1.00 25.35           C  
-ATOM   3182  C   ASN A 409      20.432  54.807  47.584  1.00 29.31           C  
-ATOM   3183  O   ASN A 409      21.012  54.527  46.533  1.00 32.19           O  
-ATOM   3184  CB  ASN A 409      21.907  55.114  49.601  1.00 25.52           C  
-ATOM   3185  CG  ASN A 409      22.946  56.045  50.221  1.00 32.54           C  
-ATOM   3186  OD1 ASN A 409      23.978  56.340  49.616  1.00 31.62           O  
-ATOM   3187  ND2 ASN A 409      22.673  56.507  51.436  1.00 29.02           N  
-ATOM   3188  N   LYS A 410      19.254  54.288  47.923  1.00 26.49           N  
-ATOM   3189  CA  LYS A 410      18.583  53.313  47.068  1.00 26.62           C  
-ATOM   3190  C   LYS A 410      17.989  53.977  45.827  1.00 28.41           C  
-ATOM   3191  O   LYS A 410      18.067  53.430  44.726  1.00 28.68           O  
-ATOM   3192  CB  LYS A 410      17.471  52.583  47.831  1.00 25.06           C  
-ATOM   3193  CG  LYS A 410      17.903  51.955  49.145  1.00 31.13           C  
-ATOM   3194  CD  LYS A 410      19.011  50.926  48.977  1.00 29.07           C  
-ATOM   3195  CE  LYS A 410      18.472  49.570  48.589  1.00 22.79           C  
-ATOM   3196  NZ  LYS A 410      19.557  48.551  48.654  1.00 26.58           N  
-ATOM   3197  N   TYR A 411      17.414  55.162  46.009  1.00 25.09           N  
-ATOM   3198  CA  TYR A 411      16.796  55.886  44.908  1.00 26.55           C  
-ATOM   3199  C   TYR A 411      17.807  56.417  43.899  1.00 28.39           C  
-ATOM   3200  O   TYR A 411      17.609  56.282  42.695  1.00 31.92           O  
-ATOM   3201  CB  TYR A 411      15.946  57.050  45.426  1.00 21.01           C  
-ATOM   3202  CG  TYR A 411      15.165  57.733  44.327  1.00 19.12           C  
-ATOM   3203  CD1 TYR A 411      13.900  57.274  43.965  1.00 20.67           C  
-ATOM   3204  CD2 TYR A 411      15.709  58.803  43.612  1.00 10.05           C  
-ATOM   3205  CE1 TYR A 411      13.196  57.854  42.916  1.00 24.75           C  
-ATOM   3206  CE2 TYR A 411      15.013  59.391  42.562  1.00 16.25           C  
-ATOM   3207  CZ  TYR A 411      13.757  58.908  42.219  1.00 22.80           C  
-ATOM   3208  OH  TYR A 411      13.062  59.462  41.170  1.00 28.21           O  
-ATOM   3209  N   THR A 412      18.875  57.030  44.400  1.00 26.37           N  
-ATOM   3210  CA  THR A 412      19.915  57.615  43.560  1.00 21.65           C  
-ATOM   3211  C   THR A 412      20.503  56.641  42.539  1.00 24.60           C  
-ATOM   3212  O   THR A 412      20.880  57.048  41.440  1.00 27.51           O  
-ATOM   3213  CB  THR A 412      21.029  58.235  44.433  1.00 15.76           C  
-ATOM   3214  OG1 THR A 412      20.456  59.259  45.252  1.00 20.00           O  
-ATOM   3215  CG2 THR A 412      22.127  58.856  43.579  1.00 13.50           C  
-ATOM   3216  N   LYS A 413      20.521  55.355  42.881  1.00 23.65           N  
-ATOM   3217  CA  LYS A 413      21.058  54.326  41.997  1.00 30.24           C  
-ATOM   3218  C   LYS A 413      20.297  54.234  40.671  1.00 32.75           C  
-ATOM   3219  O   LYS A 413      20.901  53.998  39.623  1.00 33.54           O  
-ATOM   3220  CB  LYS A 413      21.046  52.972  42.706  1.00 36.59           C  
-ATOM   3221  CG  LYS A 413      22.020  51.960  42.128  1.00 51.60           C  
-ATOM   3222  CD  LYS A 413      22.066  50.678  42.956  1.00 60.93           C  
-ATOM   3223  CE  LYS A 413      22.398  50.948  44.428  1.00 68.82           C  
-ATOM   3224  NZ  LYS A 413      23.715  51.626  44.634  1.00 70.40           N  
-ATOM   3225  N   PHE A 414      18.979  54.429  40.723  1.00 31.10           N  
-ATOM   3226  CA  PHE A 414      18.128  54.375  39.531  1.00 29.88           C  
-ATOM   3227  C   PHE A 414      17.566  55.745  39.145  1.00 30.94           C  
-ATOM   3228  O   PHE A 414      17.053  55.928  38.040  1.00 28.99           O  
-ATOM   3229  CB  PHE A 414      16.948  53.427  39.758  1.00 31.00           C  
-ATOM   3230  CG  PHE A 414      17.338  51.990  39.930  1.00 34.80           C  
-ATOM   3231  CD1 PHE A 414      17.421  51.145  38.832  1.00 36.93           C  
-ATOM   3232  CD2 PHE A 414      17.592  51.473  41.193  1.00 37.08           C  
-ATOM   3233  CE1 PHE A 414      17.750  49.803  38.989  1.00 42.67           C  
-ATOM   3234  CE2 PHE A 414      17.922  50.133  41.361  1.00 41.79           C  
-ATOM   3235  CZ  PHE A 414      18.000  49.296  40.256  1.00 46.60           C  
-ATOM   3236  N   GLY A 415      17.682  56.705  40.058  1.00 33.12           N  
-ATOM   3237  CA  GLY A 415      17.157  58.039  39.833  1.00 26.61           C  
-ATOM   3238  C   GLY A 415      17.789  58.860  38.731  1.00 26.12           C  
-ATOM   3239  O   GLY A 415      18.707  58.412  38.039  1.00 28.37           O  
-ATOM   3240  N   ASN A 416      17.309  60.093  38.602  1.00 26.53           N  
-ATOM   3241  CA  ASN A 416      17.788  61.009  37.578  1.00 25.04           C  
-ATOM   3242  C   ASN A 416      18.321  62.323  38.154  1.00 25.95           C  
-ATOM   3243  O   ASN A 416      18.545  63.287  37.423  1.00 26.27           O  
-ATOM   3244  CB  ASN A 416      16.657  61.289  36.579  1.00 30.52           C  
-ATOM   3245  CG  ASN A 416      17.140  62.008  35.337  1.00 32.90           C  
-ATOM   3246  OD1 ASN A 416      16.452  62.879  34.806  1.00 36.91           O  
-ATOM   3247  ND2 ASN A 416      18.336  61.648  34.883  1.00 29.77           N  
-ATOM   3248  N   GLY A 417      18.534  62.359  39.463  1.00 26.82           N  
-ATOM   3249  CA  GLY A 417      19.040  63.571  40.080  1.00 24.54           C  
-ATOM   3250  C   GLY A 417      18.591  63.703  41.517  1.00 22.59           C  
-ATOM   3251  O   GLY A 417      17.396  63.758  41.793  1.00 26.47           O  
-ATOM   3252  N   THR A 418      19.554  63.766  42.431  1.00 19.48           N  
-ATOM   3253  CA  THR A 418      19.255  63.882  43.847  1.00 16.03           C  
-ATOM   3254  C   THR A 418      19.992  65.055  44.479  1.00 18.55           C  
-ATOM   3255  O   THR A 418      21.162  65.289  44.191  1.00 16.19           O  
-ATOM   3256  CB  THR A 418      19.654  62.595  44.596  1.00 21.23           C  
-ATOM   3257  OG1 THR A 418      18.992  61.469  44.004  1.00 23.63           O  
-ATOM   3258  CG2 THR A 418      19.272  62.684  46.072  1.00  9.78           C  
-ATOM   3259  N   TYR A 419      19.287  65.793  45.331  1.00 14.77           N  
-ATOM   3260  CA  TYR A 419      19.854  66.930  46.048  1.00 16.15           C  
-ATOM   3261  C   TYR A 419      19.497  66.784  47.523  1.00 18.45           C  
-ATOM   3262  O   TYR A 419      18.321  66.786  47.881  1.00 21.66           O  
-ATOM   3263  CB  TYR A 419      19.326  68.250  45.478  1.00 14.77           C  
-ATOM   3264  CG  TYR A 419      19.831  68.525  44.082  1.00 21.02           C  
-ATOM   3265  CD1 TYR A 419      21.046  69.181  43.877  1.00 22.63           C  
-ATOM   3266  CD2 TYR A 419      19.118  68.093  42.963  1.00 18.96           C  
-ATOM   3267  CE1 TYR A 419      21.541  69.397  42.596  1.00 20.91           C  
-ATOM   3268  CE2 TYR A 419      19.604  68.303  41.673  1.00 20.68           C  
-ATOM   3269  CZ  TYR A 419      20.816  68.956  41.498  1.00 23.89           C  
-ATOM   3270  OH  TYR A 419      21.303  69.167  40.228  1.00 28.09           O  
-ATOM   3271  N   LEU A 420      20.519  66.625  48.364  1.00 16.32           N  
-ATOM   3272  CA  LEU A 420      20.326  66.442  49.801  1.00 18.46           C  
-ATOM   3273  C   LEU A 420      20.749  67.650  50.642  1.00 19.36           C  
-ATOM   3274  O   LEU A 420      21.778  68.269  50.382  1.00 18.00           O  
-ATOM   3275  CB  LEU A 420      21.077  65.186  50.267  1.00 15.05           C  
-ATOM   3276  CG  LEU A 420      20.906  64.712  51.717  1.00 15.67           C  
-ATOM   3277  CD1 LEU A 420      19.483  64.223  51.970  1.00  8.34           C  
-ATOM   3278  CD2 LEU A 420      21.903  63.601  52.000  1.00  3.78           C  
-ATOM   3279  N   TYR A 421      19.948  67.971  51.657  1.00 22.06           N  
-ATOM   3280  CA  TYR A 421      20.245  69.093  52.546  1.00 21.76           C  
-ATOM   3281  C   TYR A 421      20.182  68.690  54.019  1.00 24.20           C  
-ATOM   3282  O   TYR A 421      19.570  67.679  54.380  1.00 18.32           O  
-ATOM   3283  CB  TYR A 421      19.277  70.261  52.299  1.00 19.53           C  
-ATOM   3284  CG  TYR A 421      17.857  70.028  52.783  1.00 19.82           C  
-ATOM   3285  CD1 TYR A 421      17.519  70.194  54.128  1.00 21.51           C  
-ATOM   3286  CD2 TYR A 421      16.851  69.656  51.896  1.00 19.46           C  
-ATOM   3287  CE1 TYR A 421      16.215  69.992  54.577  1.00 22.03           C  
-ATOM   3288  CE2 TYR A 421      15.540  69.453  52.335  1.00 17.95           C  
-ATOM   3289  CZ  TYR A 421      15.232  69.621  53.676  1.00 19.47           C  
-ATOM   3290  OH  TYR A 421      13.951  69.407  54.120  1.00 14.82           O  
-ATOM   3291  N   PHE A 422      20.797  69.514  54.863  1.00 24.19           N  
-ATOM   3292  CA  PHE A 422      20.810  69.294  56.304  1.00 20.03           C  
-ATOM   3293  C   PHE A 422      20.487  70.633  56.946  1.00 21.27           C  
-ATOM   3294  O   PHE A 422      21.371  71.469  57.142  1.00 24.98           O  
-ATOM   3295  CB  PHE A 422      22.182  68.794  56.774  1.00 16.52           C  
-ATOM   3296  CG  PHE A 422      22.240  68.450  58.246  1.00 20.05           C  
-ATOM   3297  CD1 PHE A 422      21.653  67.281  58.726  1.00 26.21           C  
-ATOM   3298  CD2 PHE A 422      22.896  69.285  59.148  1.00 22.91           C  
-ATOM   3299  CE1 PHE A 422      21.718  66.946  60.082  1.00 20.79           C  
-ATOM   3300  CE2 PHE A 422      22.966  68.958  60.504  1.00 25.08           C  
-ATOM   3301  CZ  PHE A 422      22.375  67.784  60.968  1.00 20.59           C  
-ATOM   3302  N   PHE A 423      19.204  70.850  57.216  1.00 17.78           N  
-ATOM   3303  CA  PHE A 423      18.741  72.086  57.831  1.00 18.85           C  
-ATOM   3304  C   PHE A 423      19.128  72.087  59.307  1.00 23.11           C  
-ATOM   3305  O   PHE A 423      18.572  71.327  60.104  1.00 26.91           O  
-ATOM   3306  CB  PHE A 423      17.222  72.215  57.671  1.00 19.37           C  
-ATOM   3307  CG  PHE A 423      16.680  73.544  58.105  1.00 24.87           C  
-ATOM   3308  CD1 PHE A 423      16.761  74.647  57.263  1.00 21.19           C  
-ATOM   3309  CD2 PHE A 423      16.107  73.701  59.363  1.00 20.55           C  
-ATOM   3310  CE1 PHE A 423      16.282  75.889  57.667  1.00 18.82           C  
-ATOM   3311  CE2 PHE A 423      15.625  74.940  59.778  1.00 20.03           C  
-ATOM   3312  CZ  PHE A 423      15.714  76.037  58.926  1.00 13.26           C  
-ATOM   3313  N   ASN A 424      20.082  72.942  59.666  1.00 22.99           N  
-ATOM   3314  CA  ASN A 424      20.543  73.018  61.046  1.00 25.94           C  
-ATOM   3315  C   ASN A 424      20.564  74.428  61.631  1.00 24.56           C  
-ATOM   3316  O   ASN A 424      21.477  74.793  62.375  1.00 32.49           O  
-ATOM   3317  CB  ASN A 424      21.917  72.346  61.190  1.00 24.25           C  
-ATOM   3318  CG  ASN A 424      23.003  73.038  60.385  1.00 22.82           C  
-ATOM   3319  OD1 ASN A 424      22.729  73.918  59.569  1.00 24.62           O  
-ATOM   3320  ND2 ASN A 424      24.247  72.643  60.615  1.00 28.96           N  
-ATOM   3321  N   HIS A 425      19.550  75.217  61.303  1.00 19.88           N  
-ATOM   3322  CA  HIS A 425      19.462  76.566  61.832  1.00 21.35           C  
-ATOM   3323  C   HIS A 425      18.286  76.695  62.793  1.00 26.17           C  
-ATOM   3324  O   HIS A 425      17.163  76.299  62.472  1.00 31.09           O  
-ATOM   3325  CB  HIS A 425      19.313  77.592  60.710  1.00 22.63           C  
-ATOM   3326  CG  HIS A 425      19.166  78.999  61.203  1.00 23.61           C  
-ATOM   3327  ND1 HIS A 425      20.216  79.706  61.749  1.00 30.59           N  
-ATOM   3328  CD2 HIS A 425      18.085  79.810  61.283  1.00 21.00           C  
-ATOM   3329  CE1 HIS A 425      19.787  80.891  62.148  1.00 32.32           C  
-ATOM   3330  NE2 HIS A 425      18.498  80.979  61.876  1.00 24.99           N  
-ATOM   3331  N   ARG A 426      18.547  77.240  63.976  1.00 23.30           N  
-ATOM   3332  CA  ARG A 426      17.489  77.436  64.956  1.00 26.82           C  
-ATOM   3333  C   ARG A 426      16.931  78.853  64.845  1.00 27.06           C  
-ATOM   3334  O   ARG A 426      17.664  79.834  64.999  1.00 27.11           O  
-ATOM   3335  CB  ARG A 426      18.000  77.199  66.375  1.00 33.09           C  
-ATOM   3336  CG  ARG A 426      16.889  77.167  67.401  1.00 31.37           C  
-ATOM   3337  CD  ARG A 426      17.423  76.990  68.796  1.00 40.38           C  
-ATOM   3338  NE  ARG A 426      16.410  76.445  69.698  1.00 40.51           N  
-ATOM   3339  CZ  ARG A 426      15.356  77.119  70.152  1.00 40.64           C  
-ATOM   3340  NH1 ARG A 426      15.154  78.382  69.797  1.00 49.86           N  
-ATOM   3341  NH2 ARG A 426      14.502  76.527  70.972  1.00 40.19           N  
-ATOM   3342  N   ALA A 427      15.633  78.948  64.572  1.00 25.13           N  
-ATOM   3343  CA  ALA A 427      14.963  80.237  64.445  1.00 26.24           C  
-ATOM   3344  C   ALA A 427      15.073  81.014  65.755  1.00 31.86           C  
-ATOM   3345  O   ALA A 427      14.802  80.484  66.835  1.00 38.21           O  
-ATOM   3346  CB  ALA A 427      13.500  80.041  64.053  1.00 19.97           C  
-ATOM   3347  N   SER A 428      15.509  82.264  65.645  1.00 31.81           N  
-ATOM   3348  CA  SER A 428      15.695  83.146  66.791  1.00 33.06           C  
-ATOM   3349  C   SER A 428      14.419  83.426  67.582  1.00 32.84           C  
-ATOM   3350  O   SER A 428      14.476  83.714  68.778  1.00 35.72           O  
-ATOM   3351  CB  SER A 428      16.316  84.465  66.325  1.00 33.73           C  
-ATOM   3352  OG  SER A 428      15.553  85.036  65.274  1.00 26.66           O  
-ATOM   3353  N   ASN A 429      13.274  83.326  66.914  1.00 32.09           N  
-ATOM   3354  CA  ASN A 429      11.984  83.589  67.546  1.00 30.09           C  
-ATOM   3355  C   ASN A 429      11.221  82.317  67.928  1.00 31.81           C  
-ATOM   3356  O   ASN A 429      10.027  82.369  68.238  1.00 30.19           O  
-ATOM   3357  CB  ASN A 429      11.121  84.453  66.619  1.00 33.50           C  
-ATOM   3358  CG  ASN A 429      10.778  83.751  65.310  1.00 38.39           C  
-ATOM   3359  OD1 ASN A 429      11.553  82.940  64.797  1.00 37.87           O  
-ATOM   3360  ND2 ASN A 429       9.607  84.057  64.770  1.00 38.79           N  
-ATOM   3361  N   LEU A 430      11.912  81.180  67.901  1.00 26.91           N  
-ATOM   3362  CA  LEU A 430      11.306  79.895  68.233  1.00 27.62           C  
-ATOM   3363  C   LEU A 430      10.870  79.871  69.702  1.00 31.11           C  
-ATOM   3364  O   LEU A 430      11.676  80.102  70.603  1.00 30.03           O  
-ATOM   3365  CB  LEU A 430      12.298  78.768  67.915  1.00 27.74           C  
-ATOM   3366  CG  LEU A 430      11.854  77.303  67.904  1.00 24.02           C  
-ATOM   3367  CD1 LEU A 430      10.444  77.163  67.377  1.00 29.60           C  
-ATOM   3368  CD2 LEU A 430      12.819  76.501  67.057  1.00 25.22           C  
-ATOM   3369  N   VAL A 431       9.582  79.617  69.929  1.00 28.86           N  
-ATOM   3370  CA  VAL A 431       9.018  79.592  71.279  1.00 25.86           C  
-ATOM   3371  C   VAL A 431       9.346  78.367  72.135  1.00 25.85           C  
-ATOM   3372  O   VAL A 431       9.192  78.406  73.358  1.00 27.03           O  
-ATOM   3373  CB  VAL A 431       7.480  79.818  71.265  1.00 28.08           C  
-ATOM   3374  CG1 VAL A 431       7.160  81.219  70.763  1.00 21.64           C  
-ATOM   3375  CG2 VAL A 431       6.791  78.774  70.397  1.00 29.46           C  
-ATOM   3376  N   TRP A 432       9.789  77.285  71.502  1.00 24.16           N  
-ATOM   3377  CA  TRP A 432      10.147  76.069  72.232  1.00 24.69           C  
-ATOM   3378  C   TRP A 432      11.496  76.243  72.943  1.00 24.46           C  
-ATOM   3379  O   TRP A 432      12.319  77.069  72.536  1.00 25.12           O  
-ATOM   3380  CB  TRP A 432      10.202  74.865  71.283  1.00 21.38           C  
-ATOM   3381  CG  TRP A 432       8.865  74.444  70.735  1.00 17.82           C  
-ATOM   3382  CD1 TRP A 432       8.385  74.681  69.478  1.00 20.16           C  
-ATOM   3383  CD2 TRP A 432       7.849  73.697  71.417  1.00 22.51           C  
-ATOM   3384  NE1 TRP A 432       7.137  74.125  69.335  1.00 22.80           N  
-ATOM   3385  CE2 TRP A 432       6.781  73.516  70.509  1.00 23.88           C  
-ATOM   3386  CE3 TRP A 432       7.735  73.162  72.708  1.00 27.09           C  
-ATOM   3387  CZ2 TRP A 432       5.613  72.823  70.851  1.00 19.15           C  
-ATOM   3388  CZ3 TRP A 432       6.572  72.471  73.047  1.00 22.51           C  
-ATOM   3389  CH2 TRP A 432       5.528  72.310  72.120  1.00 21.32           C  
-ATOM   3390  N   PRO A 433      11.736  75.468  74.018  1.00 21.30           N  
-ATOM   3391  CA  PRO A 433      12.990  75.549  74.777  1.00 19.48           C  
-ATOM   3392  C   PRO A 433      14.227  75.213  73.946  1.00 22.97           C  
-ATOM   3393  O   PRO A 433      14.159  74.416  73.009  1.00 27.40           O  
-ATOM   3394  CB  PRO A 433      12.767  74.548  75.911  1.00 15.78           C  
-ATOM   3395  CG  PRO A 433      11.822  73.548  75.305  1.00 18.70           C  
-ATOM   3396  CD  PRO A 433      10.847  74.440  74.591  1.00 18.20           C  
-ATOM   3397  N   GLU A 434      15.352  75.825  74.310  1.00 27.31           N  
-ATOM   3398  CA  GLU A 434      16.628  75.643  73.616  1.00 23.91           C  
-ATOM   3399  C   GLU A 434      17.089  74.191  73.492  1.00 23.65           C  
-ATOM   3400  O   GLU A 434      17.749  73.834  72.512  1.00 25.81           O  
-ATOM   3401  CB  GLU A 434      17.733  76.450  74.312  1.00 32.69           C  
-ATOM   3402  CG  GLU A 434      17.472  77.951  74.441  1.00 52.21           C  
-ATOM   3403  CD  GLU A 434      17.493  78.688  73.109  1.00 62.02           C  
-ATOM   3404  OE1 GLU A 434      18.478  78.535  72.350  1.00 63.65           O  
-ATOM   3405  OE2 GLU A 434      16.529  79.436  72.830  1.00 69.65           O  
-ATOM   3406  N   TRP A 435      16.736  73.355  74.467  1.00 22.09           N  
-ATOM   3407  CA  TRP A 435      17.157  71.956  74.452  1.00 21.65           C  
-ATOM   3408  C   TRP A 435      16.625  71.148  73.269  1.00 24.30           C  
-ATOM   3409  O   TRP A 435      17.189  70.113  72.914  1.00 23.76           O  
-ATOM   3410  CB  TRP A 435      16.831  71.260  75.786  1.00 17.96           C  
-ATOM   3411  CG  TRP A 435      15.379  70.930  76.038  1.00 20.55           C  
-ATOM   3412  CD1 TRP A 435      14.504  71.634  76.811  1.00 26.28           C  
-ATOM   3413  CD2 TRP A 435      14.654  69.784  75.560  1.00 19.64           C  
-ATOM   3414  NE1 TRP A 435      13.284  71.003  76.849  1.00 20.06           N  
-ATOM   3415  CE2 TRP A 435      13.346  69.866  76.092  1.00 15.29           C  
-ATOM   3416  CE3 TRP A 435      14.984  68.697  74.738  1.00 23.43           C  
-ATOM   3417  CZ2 TRP A 435      12.363  68.901  75.830  1.00 20.68           C  
-ATOM   3418  CZ3 TRP A 435      14.006  67.735  74.475  1.00 21.08           C  
-ATOM   3419  CH2 TRP A 435      12.711  67.847  75.022  1.00 17.63           C  
-ATOM   3420  N   MET A 436      15.548  71.632  72.657  1.00 25.68           N  
-ATOM   3421  CA  MET A 436      14.944  70.959  71.511  1.00 23.55           C  
-ATOM   3422  C   MET A 436      15.697  71.242  70.202  1.00 23.86           C  
-ATOM   3423  O   MET A 436      15.575  70.485  69.239  1.00 25.75           O  
-ATOM   3424  CB  MET A 436      13.463  71.343  71.402  1.00 19.77           C  
-ATOM   3425  CG  MET A 436      12.629  70.843  72.581  1.00 11.34           C  
-ATOM   3426  SD  MET A 436      10.887  71.298  72.565  1.00 21.43           S  
-ATOM   3427  CE  MET A 436      10.229  70.087  71.410  1.00 16.53           C  
-ATOM   3428  N   GLY A 437      16.486  72.319  70.191  1.00 22.42           N  
-ATOM   3429  CA  GLY A 437      17.275  72.690  69.024  1.00 22.60           C  
-ATOM   3430  C   GLY A 437      16.499  72.982  67.751  1.00 25.82           C  
-ATOM   3431  O   GLY A 437      15.512  73.725  67.770  1.00 28.05           O  
-ATOM   3432  N   VAL A 438      16.986  72.437  66.634  1.00 22.57           N  
-ATOM   3433  CA  VAL A 438      16.355  72.601  65.320  1.00 16.57           C  
-ATOM   3434  C   VAL A 438      15.292  71.507  65.217  1.00 16.92           C  
-ATOM   3435  O   VAL A 438      15.537  70.401  64.723  1.00 13.85           O  
-ATOM   3436  CB  VAL A 438      17.391  72.457  64.187  1.00 14.27           C  
-ATOM   3437  CG1 VAL A 438      16.772  72.828  62.853  1.00  9.18           C  
-ATOM   3438  CG2 VAL A 438      18.608  73.323  64.486  1.00 11.73           C  
-ATOM   3439  N   ILE A 439      14.101  71.856  65.682  1.00 17.32           N  
-ATOM   3440  CA  ILE A 439      12.951  70.961  65.756  1.00 15.97           C  
-ATOM   3441  C   ILE A 439      12.297  70.486  64.456  1.00 22.35           C  
-ATOM   3442  O   ILE A 439      12.299  71.179  63.434  1.00 22.47           O  
-ATOM   3443  CB  ILE A 439      11.885  71.588  66.684  1.00 18.18           C  
-ATOM   3444  CG1 ILE A 439      12.560  72.055  67.977  1.00 13.18           C  
-ATOM   3445  CG2 ILE A 439      10.794  70.586  67.015  1.00 16.72           C  
-ATOM   3446  CD1 ILE A 439      11.710  72.954  68.810  1.00 14.02           C  
-ATOM   3447  N   HIS A 440      11.736  69.281  64.542  1.00 20.71           N  
-ATOM   3448  CA  HIS A 440      11.031  68.600  63.464  1.00 19.55           C  
-ATOM   3449  C   HIS A 440       9.871  69.465  62.985  1.00 22.42           C  
-ATOM   3450  O   HIS A 440       8.911  69.691  63.725  1.00 26.68           O  
-ATOM   3451  CB  HIS A 440      10.519  67.254  64.006  1.00 18.94           C  
-ATOM   3452  CG  HIS A 440       9.679  66.465  63.047  1.00 17.09           C  
-ATOM   3453  ND1 HIS A 440      10.221  65.662  62.066  1.00 12.11           N  
-ATOM   3454  CD2 HIS A 440       8.339  66.280  62.982  1.00 13.34           C  
-ATOM   3455  CE1 HIS A 440       9.253  65.012  61.443  1.00 13.97           C  
-ATOM   3456  NE2 HIS A 440       8.102  65.368  61.983  1.00 19.47           N  
-ATOM   3457  N   GLY A 441       9.990  69.975  61.762  1.00 23.55           N  
-ATOM   3458  CA  GLY A 441       8.938  70.801  61.194  1.00 21.98           C  
-ATOM   3459  C   GLY A 441       9.218  72.290  61.168  1.00 21.68           C  
-ATOM   3460  O   GLY A 441       8.437  73.055  60.603  1.00 22.17           O  
-ATOM   3461  N   TYR A 442      10.347  72.708  61.732  1.00 23.13           N  
-ATOM   3462  CA  TYR A 442      10.678  74.128  61.768  1.00 21.17           C  
-ATOM   3463  C   TYR A 442      11.532  74.689  60.634  1.00 18.81           C  
-ATOM   3464  O   TYR A 442      12.211  75.703  60.788  1.00 21.76           O  
-ATOM   3465  CB  TYR A 442      11.191  74.528  63.155  1.00 19.90           C  
-ATOM   3466  CG  TYR A 442      10.043  74.640  64.130  1.00 19.00           C  
-ATOM   3467  CD1 TYR A 442       9.539  73.513  64.778  1.00 16.04           C  
-ATOM   3468  CD2 TYR A 442       9.386  75.855  64.322  1.00 14.00           C  
-ATOM   3469  CE1 TYR A 442       8.404  73.592  65.583  1.00 11.86           C  
-ATOM   3470  CE2 TYR A 442       8.253  75.943  65.122  1.00 18.25           C  
-ATOM   3471  CZ  TYR A 442       7.768  74.809  65.749  1.00 15.77           C  
-ATOM   3472  OH  TYR A 442       6.643  74.893  66.536  1.00 22.90           O  
-ATOM   3473  N   GLU A 443      11.467  74.022  59.488  1.00 22.40           N  
-ATOM   3474  CA  GLU A 443      12.162  74.458  58.283  1.00 18.84           C  
-ATOM   3475  C   GLU A 443      11.041  74.900  57.345  1.00 20.57           C  
-ATOM   3476  O   GLU A 443      11.266  75.646  56.392  1.00 26.99           O  
-ATOM   3477  CB  GLU A 443      12.958  73.313  57.642  1.00 18.49           C  
-ATOM   3478  CG  GLU A 443      12.159  72.353  56.745  1.00 13.48           C  
-ATOM   3479  CD  GLU A 443      11.229  71.424  57.513  1.00 18.48           C  
-ATOM   3480  OE1 GLU A 443      11.342  71.340  58.752  1.00 21.04           O  
-ATOM   3481  OE2 GLU A 443      10.381  70.768  56.873  1.00 15.52           O  
-ATOM   3482  N   ILE A 444       9.833  74.420  57.643  1.00 19.57           N  
-ATOM   3483  CA  ILE A 444       8.633  74.717  56.873  1.00 21.94           C  
-ATOM   3484  C   ILE A 444       8.422  76.218  56.759  1.00 21.37           C  
-ATOM   3485  O   ILE A 444       8.130  76.726  55.679  1.00 23.79           O  
-ATOM   3486  CB  ILE A 444       7.378  74.071  57.522  1.00 19.63           C  
-ATOM   3487  CG1 ILE A 444       7.538  72.549  57.588  1.00 17.86           C  
-ATOM   3488  CG2 ILE A 444       6.122  74.425  56.733  1.00 20.07           C  
-ATOM   3489  CD1 ILE A 444       6.359  71.836  58.222  1.00 10.24           C  
-ATOM   3490  N   GLU A 445       8.583  76.925  57.874  1.00 21.70           N  
-ATOM   3491  CA  GLU A 445       8.408  78.371  57.880  1.00 21.50           C  
-ATOM   3492  C   GLU A 445       9.374  79.056  56.919  1.00 21.73           C  
-ATOM   3493  O   GLU A 445       9.060  80.106  56.360  1.00 22.79           O  
-ATOM   3494  CB  GLU A 445       8.531  78.937  59.299  1.00 25.04           C  
-ATOM   3495  CG  GLU A 445       9.739  78.462  60.093  1.00 27.02           C  
-ATOM   3496  CD  GLU A 445       9.639  78.806  61.575  1.00 26.19           C  
-ATOM   3497  OE1 GLU A 445       8.597  78.502  62.193  1.00 16.93           O  
-ATOM   3498  OE2 GLU A 445      10.603  79.376  62.124  1.00 26.56           O  
-ATOM   3499  N   PHE A 446      10.529  78.435  56.691  1.00 18.10           N  
-ATOM   3500  CA  PHE A 446      11.517  78.982  55.769  1.00 21.82           C  
-ATOM   3501  C   PHE A 446      11.166  78.617  54.328  1.00 21.32           C  
-ATOM   3502  O   PHE A 446      11.429  79.383  53.404  1.00 23.12           O  
-ATOM   3503  CB  PHE A 446      12.918  78.495  56.133  1.00 25.55           C  
-ATOM   3504  CG  PHE A 446      13.424  79.050  57.434  1.00 30.80           C  
-ATOM   3505  CD1 PHE A 446      13.049  78.474  58.644  1.00 30.82           C  
-ATOM   3506  CD2 PHE A 446      14.251  80.169  57.452  1.00 31.69           C  
-ATOM   3507  CE1 PHE A 446      13.488  79.007  59.855  1.00 31.70           C  
-ATOM   3508  CE2 PHE A 446      14.695  80.709  58.657  1.00 29.82           C  
-ATOM   3509  CZ  PHE A 446      14.313  80.127  59.860  1.00 25.20           C  
-ATOM   3510  N   VAL A 447      10.551  77.451  54.150  1.00 22.06           N  
-ATOM   3511  CA  VAL A 447      10.133  76.986  52.831  1.00 19.28           C  
-ATOM   3512  C   VAL A 447       8.962  77.843  52.339  1.00 20.81           C  
-ATOM   3513  O   VAL A 447       8.905  78.211  51.164  1.00 22.03           O  
-ATOM   3514  CB  VAL A 447       9.723  75.488  52.873  1.00 21.82           C  
-ATOM   3515  CG1 VAL A 447       8.984  75.084  51.599  1.00 13.95           C  
-ATOM   3516  CG2 VAL A 447      10.957  74.619  53.059  1.00 16.20           C  
-ATOM   3517  N   PHE A 448       8.054  78.184  53.252  1.00 17.70           N  
-ATOM   3518  CA  PHE A 448       6.893  79.000  52.912  1.00 19.94           C  
-ATOM   3519  C   PHE A 448       7.118  80.515  53.019  1.00 20.42           C  
-ATOM   3520  O   PHE A 448       6.181  81.305  52.903  1.00 19.03           O  
-ATOM   3521  CB  PHE A 448       5.670  78.553  53.715  1.00 11.24           C  
-ATOM   3522  CG  PHE A 448       5.030  77.305  53.185  1.00 13.04           C  
-ATOM   3523  CD1 PHE A 448       5.614  76.061  53.401  1.00 16.77           C  
-ATOM   3524  CD2 PHE A 448       3.853  77.374  52.445  1.00 17.99           C  
-ATOM   3525  CE1 PHE A 448       5.035  74.900  52.887  1.00 15.01           C  
-ATOM   3526  CE2 PHE A 448       3.264  76.219  51.926  1.00 14.68           C  
-ATOM   3527  CZ  PHE A 448       3.859  74.981  52.148  1.00 15.80           C  
-ATOM   3528  N   GLY A 449       8.370  80.903  53.244  1.00 24.13           N  
-ATOM   3529  CA  GLY A 449       8.729  82.309  53.315  1.00 23.48           C  
-ATOM   3530  C   GLY A 449       8.172  83.181  54.422  1.00 26.71           C  
-ATOM   3531  O   GLY A 449       8.015  84.387  54.230  1.00 23.36           O  
-ATOM   3532  N   LEU A 450       7.878  82.590  55.576  1.00 30.30           N  
-ATOM   3533  CA  LEU A 450       7.366  83.348  56.720  1.00 29.62           C  
-ATOM   3534  C   LEU A 450       8.321  84.465  57.166  1.00 27.30           C  
-ATOM   3535  O   LEU A 450       7.871  85.520  57.608  1.00 28.09           O  
-ATOM   3536  CB  LEU A 450       7.053  82.417  57.902  1.00 30.20           C  
-ATOM   3537  CG  LEU A 450       5.756  81.598  57.890  1.00 27.45           C  
-ATOM   3538  CD1 LEU A 450       4.560  82.512  58.012  1.00 23.72           C  
-ATOM   3539  CD2 LEU A 450       5.661  80.764  56.626  1.00 31.89           C  
-ATOM   3540  N   PRO A 451       9.650  84.240  57.078  1.00 23.92           N  
-ATOM   3541  CA  PRO A 451      10.616  85.269  57.482  1.00 27.79           C  
-ATOM   3542  C   PRO A 451      10.531  86.594  56.717  1.00 30.19           C  
-ATOM   3543  O   PRO A 451      11.098  87.597  57.151  1.00 32.40           O  
-ATOM   3544  CB  PRO A 451      11.957  84.578  57.245  1.00 22.73           C  
-ATOM   3545  CG  PRO A 451      11.651  83.165  57.567  1.00 23.67           C  
-ATOM   3546  CD  PRO A 451      10.348  82.961  56.844  1.00 23.05           C  
-ATOM   3547  N   LEU A 452       9.851  86.596  55.572  1.00 31.24           N  
-ATOM   3548  CA  LEU A 452       9.715  87.817  54.783  1.00 33.59           C  
-ATOM   3549  C   LEU A 452       8.721  88.765  55.449  1.00 37.64           C  
-ATOM   3550  O   LEU A 452       8.784  89.981  55.255  1.00 42.16           O  
-ATOM   3551  CB  LEU A 452       9.260  87.515  53.352  1.00 32.69           C  
-ATOM   3552  CG  LEU A 452       9.967  86.450  52.508  1.00 35.23           C  
-ATOM   3553  CD1 LEU A 452       9.729  86.772  51.039  1.00 33.32           C  
-ATOM   3554  CD2 LEU A 452      11.455  86.399  52.797  1.00 29.77           C  
-ATOM   3555  N   VAL A 453       7.792  88.199  56.217  1.00 37.23           N  
-ATOM   3556  CA  VAL A 453       6.788  88.984  56.929  1.00 39.05           C  
-ATOM   3557  C   VAL A 453       7.410  89.575  58.193  1.00 44.65           C  
-ATOM   3558  O   VAL A 453       7.606  88.879  59.190  1.00 43.51           O  
-ATOM   3559  CB  VAL A 453       5.561  88.127  57.303  1.00 36.10           C  
-ATOM   3560  CG1 VAL A 453       4.536  88.962  58.052  1.00 32.73           C  
-ATOM   3561  CG2 VAL A 453       4.941  87.544  56.055  1.00 31.92           C  
-ATOM   3562  N   LYS A 454       7.715  90.868  58.127  1.00 49.05           N  
-ATOM   3563  CA  LYS A 454       8.334  91.615  59.219  1.00 51.28           C  
-ATOM   3564  C   LYS A 454       7.656  91.464  60.585  1.00 49.05           C  
-ATOM   3565  O   LYS A 454       8.333  91.357  61.609  1.00 45.37           O  
-ATOM   3566  CB  LYS A 454       8.414  93.094  58.827  1.00 60.54           C  
-ATOM   3567  CG  LYS A 454       8.854  94.040  59.931  1.00 72.01           C  
-ATOM   3568  CD  LYS A 454       8.669  95.483  59.489  1.00 82.56           C  
-ATOM   3569  CE  LYS A 454       8.914  96.457  60.627  1.00 87.58           C  
-ATOM   3570  NZ  LYS A 454       8.722  97.864  60.181  1.00 90.18           N  
-ATOM   3571  N   GLU A 455       6.325  91.421  60.591  1.00 49.01           N  
-ATOM   3572  CA  GLU A 455       5.551  91.297  61.827  1.00 48.74           C  
-ATOM   3573  C   GLU A 455       5.792  89.992  62.595  1.00 48.78           C  
-ATOM   3574  O   GLU A 455       5.270  89.815  63.697  1.00 52.19           O  
-ATOM   3575  CB  GLU A 455       4.046  91.432  61.540  1.00 54.87           C  
-ATOM   3576  CG  GLU A 455       3.615  92.734  60.868  1.00 69.30           C  
-ATOM   3577  CD  GLU A 455       3.720  92.686  59.353  1.00 77.58           C  
-ATOM   3578  OE1 GLU A 455       2.829  92.084  58.712  1.00 86.08           O  
-ATOM   3579  OE2 GLU A 455       4.687  93.254  58.803  1.00 75.60           O  
-ATOM   3580  N   LEU A 456       6.586  89.089  62.025  1.00 48.59           N  
-ATOM   3581  CA  LEU A 456       6.856  87.806  62.665  1.00 44.25           C  
-ATOM   3582  C   LEU A 456       8.153  87.717  63.474  1.00 46.00           C  
-ATOM   3583  O   LEU A 456       8.528  86.638  63.938  1.00 48.88           O  
-ATOM   3584  CB  LEU A 456       6.768  86.675  61.638  1.00 42.02           C  
-ATOM   3585  CG  LEU A 456       5.382  86.483  61.014  1.00 41.71           C  
-ATOM   3586  CD1 LEU A 456       5.424  85.357  60.002  1.00 38.45           C  
-ATOM   3587  CD2 LEU A 456       4.346  86.194  62.096  1.00 35.29           C  
-ATOM   3588  N   ASN A 457       8.826  88.853  63.642  1.00 46.81           N  
-ATOM   3589  CA  ASN A 457      10.058  88.940  64.429  1.00 46.49           C  
-ATOM   3590  C   ASN A 457      11.251  88.085  63.978  1.00 44.55           C  
-ATOM   3591  O   ASN A 457      11.996  87.582  64.821  1.00 48.22           O  
-ATOM   3592  CB  ASN A 457       9.770  88.639  65.913  1.00 50.57           C  
-ATOM   3593  CG  ASN A 457       8.685  89.529  66.510  1.00 56.51           C  
-ATOM   3594  OD1 ASN A 457       8.442  90.642  66.035  1.00 54.49           O  
-ATOM   3595  ND2 ASN A 457       8.047  89.021  67.567  1.00 60.80           N  
-ATOM   3596  N   TYR A 458      11.433  87.891  62.674  1.00 38.82           N  
-ATOM   3597  CA  TYR A 458      12.584  87.115  62.193  1.00 33.89           C  
-ATOM   3598  C   TYR A 458      13.757  88.063  61.952  1.00 35.51           C  
-ATOM   3599  O   TYR A 458      13.562  89.272  61.824  1.00 40.71           O  
-ATOM   3600  CB  TYR A 458      12.260  86.374  60.888  1.00 33.18           C  
-ATOM   3601  CG  TYR A 458      11.395  85.140  61.042  1.00 24.79           C  
-ATOM   3602  CD1 TYR A 458      11.966  83.890  61.284  1.00 22.27           C  
-ATOM   3603  CD2 TYR A 458      10.006  85.219  60.928  1.00 25.34           C  
-ATOM   3604  CE1 TYR A 458      11.174  82.745  61.408  1.00 16.88           C  
-ATOM   3605  CE2 TYR A 458       9.205  84.085  61.049  1.00 20.75           C  
-ATOM   3606  CZ  TYR A 458       9.794  82.851  61.290  1.00 25.71           C  
-ATOM   3607  OH  TYR A 458       9.003  81.730  61.420  1.00 20.21           O  
-ATOM   3608  N   THR A 459      14.972  87.524  61.903  1.00 34.17           N  
-ATOM   3609  CA  THR A 459      16.150  88.355  61.654  1.00 33.85           C  
-ATOM   3610  C   THR A 459      16.342  88.569  60.152  1.00 36.05           C  
-ATOM   3611  O   THR A 459      15.643  87.971  59.335  1.00 41.88           O  
-ATOM   3612  CB  THR A 459      17.449  87.741  62.242  1.00 33.94           C  
-ATOM   3613  OG1 THR A 459      17.772  86.526  61.553  1.00 35.75           O  
-ATOM   3614  CG2 THR A 459      17.288  87.456  63.728  1.00 25.85           C  
-ATOM   3615  N   ALA A 460      17.294  89.427  59.798  1.00 39.20           N  
-ATOM   3616  CA  ALA A 460      17.590  89.728  58.403  1.00 37.63           C  
-ATOM   3617  C   ALA A 460      18.147  88.508  57.677  1.00 39.98           C  
-ATOM   3618  O   ALA A 460      17.720  88.192  56.565  1.00 41.17           O  
-ATOM   3619  CB  ALA A 460      18.574  90.884  58.315  1.00 35.39           C  
-ATOM   3620  N   GLU A 461      19.101  87.826  58.308  1.00 44.71           N  
-ATOM   3621  CA  GLU A 461      19.710  86.640  57.714  1.00 47.15           C  
-ATOM   3622  C   GLU A 461      18.716  85.493  57.568  1.00 42.57           C  
-ATOM   3623  O   GLU A 461      18.871  84.640  56.694  1.00 41.02           O  
-ATOM   3624  CB  GLU A 461      20.961  86.190  58.486  1.00 52.11           C  
-ATOM   3625  CG  GLU A 461      20.933  86.409  59.992  1.00 60.61           C  
-ATOM   3626  CD  GLU A 461      21.386  87.805  60.390  1.00 62.21           C  
-ATOM   3627  OE1 GLU A 461      22.579  88.120  60.193  1.00 64.17           O  
-ATOM   3628  OE2 GLU A 461      20.554  88.586  60.899  1.00 58.89           O  
-ATOM   3629  N   GLU A 462      17.693  85.481  58.419  1.00 38.78           N  
-ATOM   3630  CA  GLU A 462      16.669  84.448  58.348  1.00 34.38           C  
-ATOM   3631  C   GLU A 462      15.750  84.702  57.162  1.00 35.48           C  
-ATOM   3632  O   GLU A 462      15.124  83.777  56.643  1.00 38.36           O  
-ATOM   3633  CB  GLU A 462      15.888  84.366  59.657  1.00 26.00           C  
-ATOM   3634  CG  GLU A 462      16.723  83.760  60.767  1.00 27.51           C  
-ATOM   3635  CD  GLU A 462      16.005  83.668  62.097  1.00 29.13           C  
-ATOM   3636  OE1 GLU A 462      15.099  84.490  62.369  1.00 29.55           O  
-ATOM   3637  OE2 GLU A 462      16.374  82.772  62.884  1.00 21.54           O  
-ATOM   3638  N   GLU A 463      15.677  85.960  56.736  1.00 38.01           N  
-ATOM   3639  CA  GLU A 463      14.870  86.322  55.578  1.00 36.89           C  
-ATOM   3640  C   GLU A 463      15.667  85.918  54.343  1.00 34.36           C  
-ATOM   3641  O   GLU A 463      15.114  85.381  53.383  1.00 34.36           O  
-ATOM   3642  CB  GLU A 463      14.597  87.828  55.542  1.00 40.93           C  
-ATOM   3643  CG  GLU A 463      13.917  88.283  54.250  1.00 44.71           C  
-ATOM   3644  CD  GLU A 463      13.659  89.778  54.176  1.00 45.39           C  
-ATOM   3645  OE1 GLU A 463      14.116  90.527  55.065  1.00 53.29           O  
-ATOM   3646  OE2 GLU A 463      12.993  90.204  53.209  1.00 43.17           O  
-ATOM   3647  N   ALA A 464      16.975  86.166  54.395  1.00 29.19           N  
-ATOM   3648  CA  ALA A 464      17.880  85.839  53.303  1.00 26.89           C  
-ATOM   3649  C   ALA A 464      17.908  84.333  53.098  1.00 26.33           C  
-ATOM   3650  O   ALA A 464      17.966  83.854  51.964  1.00 32.02           O  
-ATOM   3651  CB  ALA A 464      19.276  86.358  53.608  1.00 28.36           C  
-ATOM   3652  N   LEU A 465      17.859  83.597  54.205  1.00 20.77           N  
-ATOM   3653  CA  LEU A 465      17.866  82.143  54.170  1.00 19.34           C  
-ATOM   3654  C   LEU A 465      16.561  81.650  53.559  1.00 21.19           C  
-ATOM   3655  O   LEU A 465      16.573  80.834  52.641  1.00 25.83           O  
-ATOM   3656  CB  LEU A 465      18.034  81.576  55.582  1.00 21.87           C  
-ATOM   3657  CG  LEU A 465      17.943  80.054  55.728  1.00 21.01           C  
-ATOM   3658  CD1 LEU A 465      18.961  79.375  54.827  1.00 19.48           C  
-ATOM   3659  CD2 LEU A 465      18.159  79.668  57.182  1.00 16.84           C  
-ATOM   3660  N   SER A 466      15.441  82.165  54.058  1.00 14.11           N  
-ATOM   3661  CA  SER A 466      14.128  81.785  53.551  1.00 20.49           C  
-ATOM   3662  C   SER A 466      14.021  82.039  52.049  1.00 27.12           C  
-ATOM   3663  O   SER A 466      13.453  81.225  51.325  1.00 33.74           O  
-ATOM   3664  CB  SER A 466      13.030  82.554  54.288  1.00 19.68           C  
-ATOM   3665  OG  SER A 466      11.758  82.312  53.717  1.00 22.32           O  
-ATOM   3666  N   ARG A 467      14.574  83.162  51.588  1.00 28.13           N  
-ATOM   3667  CA  ARG A 467      14.540  83.511  50.169  1.00 27.07           C  
-ATOM   3668  C   ARG A 467      15.422  82.576  49.355  1.00 24.50           C  
-ATOM   3669  O   ARG A 467      15.112  82.258  48.207  1.00 23.21           O  
-ATOM   3670  CB  ARG A 467      14.985  84.958  49.956  1.00 24.51           C  
-ATOM   3671  CG  ARG A 467      13.947  85.988  50.359  1.00 25.54           C  
-ATOM   3672  CD  ARG A 467      14.429  87.408  50.076  1.00 25.75           C  
-ATOM   3673  NE  ARG A 467      13.409  88.407  50.392  1.00 30.40           N  
-ATOM   3674  CZ  ARG A 467      12.364  88.687  49.615  1.00 33.83           C  
-ATOM   3675  NH1 ARG A 467      12.189  88.050  48.466  1.00 32.87           N  
-ATOM   3676  NH2 ARG A 467      11.470  89.587  50.004  1.00 29.83           N  
-ATOM   3677  N   ARG A 468      16.515  82.133  49.967  1.00 24.02           N  
-ATOM   3678  CA  ARG A 468      17.455  81.229  49.319  1.00 27.23           C  
-ATOM   3679  C   ARG A 468      16.817  79.848  49.181  1.00 28.29           C  
-ATOM   3680  O   ARG A 468      16.922  79.207  48.134  1.00 27.06           O  
-ATOM   3681  CB  ARG A 468      18.736  81.131  50.149  1.00 28.87           C  
-ATOM   3682  CG  ARG A 468      19.999  81.066  49.323  1.00 30.71           C  
-ATOM   3683  CD  ARG A 468      21.234  81.127  50.201  1.00 34.34           C  
-ATOM   3684  NE  ARG A 468      21.718  79.792  50.547  1.00 40.43           N  
-ATOM   3685  CZ  ARG A 468      21.815  79.325  51.787  1.00 44.17           C  
-ATOM   3686  NH1 ARG A 468      21.457  80.076  52.818  1.00 45.87           N  
-ATOM   3687  NH2 ARG A 468      22.298  78.108  51.997  1.00 45.74           N  
-ATOM   3688  N   ILE A 469      16.137  79.413  50.239  1.00 25.08           N  
-ATOM   3689  CA  ILE A 469      15.467  78.121  50.257  1.00 20.86           C  
-ATOM   3690  C   ILE A 469      14.289  78.127  49.297  1.00 22.31           C  
-ATOM   3691  O   ILE A 469      14.149  77.215  48.484  1.00 26.15           O  
-ATOM   3692  CB  ILE A 469      14.983  77.747  51.677  1.00 17.53           C  
-ATOM   3693  CG1 ILE A 469      16.189  77.467  52.577  1.00 14.41           C  
-ATOM   3694  CG2 ILE A 469      14.072  76.523  51.632  1.00 15.38           C  
-ATOM   3695  CD1 ILE A 469      15.824  77.094  53.996  1.00 19.86           C  
-ATOM   3696  N   MET A 470      13.456  79.162  49.380  1.00 19.00           N  
-ATOM   3697  CA  MET A 470      12.300  79.263  48.499  1.00 23.36           C  
-ATOM   3698  C   MET A 470      12.733  79.184  47.044  1.00 26.72           C  
-ATOM   3699  O   MET A 470      12.077  78.535  46.226  1.00 26.07           O  
-ATOM   3700  CB  MET A 470      11.543  80.571  48.723  1.00 19.03           C  
-ATOM   3701  CG  MET A 470      10.617  80.560  49.917  1.00 26.78           C  
-ATOM   3702  SD  MET A 470       9.421  81.900  49.825  1.00 29.30           S  
-ATOM   3703  CE  MET A 470      10.506  83.315  50.066  1.00 22.16           C  
-ATOM   3704  N   HIS A 471      13.855  79.826  46.734  1.00 25.74           N  
-ATOM   3705  CA  HIS A 471      14.359  79.829  45.373  1.00 28.30           C  
-ATOM   3706  C   HIS A 471      14.936  78.475  44.970  1.00 28.71           C  
-ATOM   3707  O   HIS A 471      14.864  78.100  43.801  1.00 31.77           O  
-ATOM   3708  CB  HIS A 471      15.382  80.948  45.165  1.00 30.50           C  
-ATOM   3709  CG  HIS A 471      15.551  81.333  43.731  1.00 32.15           C  
-ATOM   3710  ND1 HIS A 471      14.608  82.064  43.044  1.00 38.28           N  
-ATOM   3711  CD2 HIS A 471      16.522  81.035  42.835  1.00 30.34           C  
-ATOM   3712  CE1 HIS A 471      14.982  82.194  41.787  1.00 37.25           C  
-ATOM   3713  NE2 HIS A 471      16.141  81.582  41.632  1.00 33.45           N  
-ATOM   3714  N   TYR A 472      15.514  77.749  45.926  1.00 28.54           N  
-ATOM   3715  CA  TYR A 472      16.063  76.421  45.644  1.00 26.84           C  
-ATOM   3716  C   TYR A 472      14.899  75.510  45.269  1.00 28.09           C  
-ATOM   3717  O   TYR A 472      14.923  74.841  44.237  1.00 30.46           O  
-ATOM   3718  CB  TYR A 472      16.772  75.841  46.870  1.00 27.53           C  
-ATOM   3719  CG  TYR A 472      18.168  76.368  47.120  1.00 36.12           C  
-ATOM   3720  CD1 TYR A 472      18.999  76.743  46.063  1.00 36.10           C  
-ATOM   3721  CD2 TYR A 472      18.672  76.464  48.421  1.00 34.78           C  
-ATOM   3722  CE1 TYR A 472      20.298  77.196  46.295  1.00 33.33           C  
-ATOM   3723  CE2 TYR A 472      19.966  76.915  48.663  1.00 35.09           C  
-ATOM   3724  CZ  TYR A 472      20.773  77.279  47.597  1.00 37.40           C  
-ATOM   3725  OH  TYR A 472      22.052  77.727  47.832  1.00 40.90           O  
-ATOM   3726  N   TRP A 473      13.876  75.517  46.120  1.00 25.13           N  
-ATOM   3727  CA  TRP A 473      12.671  74.717  45.928  1.00 25.58           C  
-ATOM   3728  C   TRP A 473      11.973  75.021  44.600  1.00 25.02           C  
-ATOM   3729  O   TRP A 473      11.654  74.109  43.835  1.00 24.41           O  
-ATOM   3730  CB  TRP A 473      11.693  74.971  47.079  1.00 21.47           C  
-ATOM   3731  CG  TRP A 473      11.817  74.031  48.252  1.00 23.16           C  
-ATOM   3732  CD1 TRP A 473      10.797  73.345  48.854  1.00 19.98           C  
-ATOM   3733  CD2 TRP A 473      13.000  73.718  48.999  1.00 21.20           C  
-ATOM   3734  NE1 TRP A 473      11.269  72.638  49.931  1.00 19.61           N  
-ATOM   3735  CE2 TRP A 473      12.616  72.846  50.045  1.00 19.56           C  
-ATOM   3736  CE3 TRP A 473      14.348  74.091  48.891  1.00 23.54           C  
-ATOM   3737  CZ2 TRP A 473      13.530  72.342  50.979  1.00 15.66           C  
-ATOM   3738  CZ3 TRP A 473      15.258  73.588  49.821  1.00 24.01           C  
-ATOM   3739  CH2 TRP A 473      14.841  72.723  50.852  1.00 19.17           C  
-ATOM   3740  N   ALA A 474      11.748  76.304  44.330  1.00 23.63           N  
-ATOM   3741  CA  ALA A 474      11.076  76.736  43.108  1.00 21.99           C  
-ATOM   3742  C   ALA A 474      11.879  76.462  41.843  1.00 22.32           C  
-ATOM   3743  O   ALA A 474      11.320  76.025  40.838  1.00 25.45           O  
-ATOM   3744  CB  ALA A 474      10.739  78.199  43.194  1.00 19.52           C  
-ATOM   3745  N   THR A 475      13.180  76.738  41.890  1.00 20.18           N  
-ATOM   3746  CA  THR A 475      14.053  76.515  40.743  1.00 20.66           C  
-ATOM   3747  C   THR A 475      14.171  75.024  40.450  1.00 24.94           C  
-ATOM   3748  O   THR A 475      14.242  74.620  39.288  1.00 31.14           O  
-ATOM   3749  CB  THR A 475      15.447  77.117  40.978  1.00 22.20           C  
-ATOM   3750  OG1 THR A 475      15.316  78.529  41.178  1.00 25.79           O  
-ATOM   3751  CG2 THR A 475      16.360  76.863  39.780  1.00 14.76           C  
-ATOM   3752  N   PHE A 476      14.186  74.212  41.504  1.00 24.40           N  
-ATOM   3753  CA  PHE A 476      14.267  72.764  41.352  1.00 20.41           C  
-ATOM   3754  C   PHE A 476      12.975  72.253  40.724  1.00 23.37           C  
-ATOM   3755  O   PHE A 476      13.000  71.409  39.833  1.00 26.03           O  
-ATOM   3756  CB  PHE A 476      14.474  72.083  42.709  1.00 21.20           C  
-ATOM   3757  CG  PHE A 476      14.202  70.603  42.689  1.00 21.26           C  
-ATOM   3758  CD1 PHE A 476      15.177  69.709  42.261  1.00 17.05           C  
-ATOM   3759  CD2 PHE A 476      12.948  70.108  43.046  1.00 17.55           C  
-ATOM   3760  CE1 PHE A 476      14.908  68.348  42.184  1.00 21.02           C  
-ATOM   3761  CE2 PHE A 476      12.669  68.748  42.972  1.00 17.08           C  
-ATOM   3762  CZ  PHE A 476      13.650  67.867  42.539  1.00 22.75           C  
-ATOM   3763  N   ALA A 477      11.846  72.754  41.214  1.00 21.13           N  
-ATOM   3764  CA  ALA A 477      10.541  72.347  40.708  1.00 23.15           C  
-ATOM   3765  C   ALA A 477      10.398  72.683  39.226  1.00 28.45           C  
-ATOM   3766  O   ALA A 477       9.825  71.911  38.454  1.00 24.55           O  
-ATOM   3767  CB  ALA A 477       9.440  73.026  41.509  1.00 17.51           C  
-ATOM   3768  N   LYS A 478      10.939  73.836  38.843  1.00 28.50           N  
-ATOM   3769  CA  LYS A 478      10.878  74.315  37.470  1.00 28.71           C  
-ATOM   3770  C   LYS A 478      11.825  73.577  36.520  1.00 30.45           C  
-ATOM   3771  O   LYS A 478      11.421  73.175  35.427  1.00 31.43           O  
-ATOM   3772  CB  LYS A 478      11.179  75.820  37.440  1.00 30.94           C  
-ATOM   3773  CG  LYS A 478      11.128  76.454  36.055  1.00 44.38           C  
-ATOM   3774  CD  LYS A 478      11.487  77.937  36.097  1.00 51.80           C  
-ATOM   3775  CE  LYS A 478      11.401  78.567  34.711  1.00 58.09           C  
-ATOM   3776  NZ  LYS A 478      11.703  80.030  34.715  1.00 60.85           N  
-ATOM   3777  N   THR A 479      13.058  73.340  36.964  1.00 26.45           N  
-ATOM   3778  CA  THR A 479      14.063  72.702  36.120  1.00 24.32           C  
-ATOM   3779  C   THR A 479      14.518  71.292  36.490  1.00 28.99           C  
-ATOM   3780  O   THR A 479      14.796  70.476  35.612  1.00 32.99           O  
-ATOM   3781  CB  THR A 479      15.320  73.588  36.037  1.00 27.55           C  
-ATOM   3782  OG1 THR A 479      16.039  73.525  37.277  1.00 25.10           O  
-ATOM   3783  CG2 THR A 479      14.932  75.043  35.765  1.00 21.43           C  
-ATOM   3784  N   GLY A 480      14.629  71.022  37.785  1.00 27.82           N  
-ATOM   3785  CA  GLY A 480      15.092  69.722  38.239  1.00 17.92           C  
-ATOM   3786  C   GLY A 480      16.456  69.900  38.879  1.00 19.20           C  
-ATOM   3787  O   GLY A 480      17.117  68.930  39.246  1.00 17.51           O  
-ATOM   3788  N   ASN A 481      16.854  71.165  39.012  1.00 21.56           N  
-ATOM   3789  CA  ASN A 481      18.127  71.569  39.596  1.00 26.27           C  
-ATOM   3790  C   ASN A 481      17.842  72.851  40.390  1.00 26.48           C  
-ATOM   3791  O   ASN A 481      17.364  73.839  39.833  1.00 35.68           O  
-ATOM   3792  CB  ASN A 481      19.136  71.844  38.469  1.00 21.87           C  
-ATOM   3793  CG  ASN A 481      20.543  72.130  38.980  1.00 27.96           C  
-ATOM   3794  OD1 ASN A 481      20.759  72.382  40.165  1.00 36.60           O  
-ATOM   3795  ND2 ASN A 481      21.511  72.095  38.073  1.00 29.34           N  
-ATOM   3796  N   PRO A 482      18.117  72.843  41.708  1.00 26.11           N  
-ATOM   3797  CA  PRO A 482      17.887  74.002  42.578  1.00 23.71           C  
-ATOM   3798  C   PRO A 482      18.796  75.184  42.257  1.00 25.83           C  
-ATOM   3799  O   PRO A 482      18.523  76.315  42.664  1.00 24.38           O  
-ATOM   3800  CB  PRO A 482      18.188  73.442  43.964  1.00 20.95           C  
-ATOM   3801  CG  PRO A 482      19.289  72.476  43.685  1.00 14.16           C  
-ATOM   3802  CD  PRO A 482      18.748  71.749  42.470  1.00 23.32           C  
-ATOM   3803  N   ASN A 483      19.876  74.908  41.530  1.00 32.19           N  
-ATOM   3804  CA  ASN A 483      20.848  75.926  41.146  1.00 30.87           C  
-ATOM   3805  C   ASN A 483      20.453  76.696  39.903  1.00 31.46           C  
-ATOM   3806  O   ASN A 483      19.997  76.119  38.918  1.00 27.59           O  
-ATOM   3807  CB  ASN A 483      22.219  75.293  40.923  1.00 27.26           C  
-ATOM   3808  CG  ASN A 483      22.775  74.662  42.177  1.00 32.87           C  
-ATOM   3809  OD1 ASN A 483      22.978  75.340  43.187  1.00 34.27           O  
-ATOM   3810  ND2 ASN A 483      23.014  73.357  42.128  1.00 29.04           N  
-ATOM   3811  N   GLU A 484      20.642  78.010  39.967  1.00 39.25           N  
-ATOM   3812  CA  GLU A 484      20.343  78.907  38.857  1.00 43.35           C  
-ATOM   3813  C   GLU A 484      21.429  78.699  37.798  1.00 37.88           C  
-ATOM   3814  O   GLU A 484      22.622  78.756  38.107  1.00 37.96           O  
-ATOM   3815  CB  GLU A 484      20.370  80.358  39.355  1.00 50.77           C  
-ATOM   3816  CG  GLU A 484      19.870  81.394  38.362  1.00 54.95           C  
-ATOM   3817  CD  GLU A 484      18.362  81.490  38.336  1.00 57.90           C  
-ATOM   3818  OE1 GLU A 484      17.718  80.624  37.708  1.00 65.49           O  
-ATOM   3819  OE2 GLU A 484      17.819  82.433  38.948  1.00 59.84           O  
-ATOM   3820  N   PRO A 485      21.033  78.421  36.545  0.50 36.28           N  
-ATOM   3821  CA  PRO A 485      22.010  78.208  35.472  0.50 34.05           C  
-ATOM   3822  C   PRO A 485      22.892  79.437  35.251  0.50 35.17           C  
-ATOM   3823  O   PRO A 485      22.390  80.559  35.136  0.50 35.44           O  
-ATOM   3824  CB  PRO A 485      21.127  77.913  34.258  0.50 32.72           C  
-ATOM   3825  CG  PRO A 485      19.857  78.656  34.567  0.50 36.10           C  
-ATOM   3826  CD  PRO A 485      19.657  78.339  36.023  0.50 34.93           C  
-ATOM   3827  N   HIS A 486      24.205  79.217  35.248  0.50 31.98           N  
-ATOM   3828  CA  HIS A 486      25.186  80.284  35.049  0.50 34.44           C  
-ATOM   3829  C   HIS A 486      25.102  81.400  36.094  0.50 35.92           C  
-ATOM   3830  O   HIS A 486      25.218  82.584  35.770  0.50 37.20           O  
-ATOM   3831  CB  HIS A 486      25.067  80.866  33.633  0.50 34.64           C  
-ATOM   3832  CG  HIS A 486      25.373  79.882  32.549  0.50 35.14           C  
-ATOM   3833  ND1 HIS A 486      26.364  78.930  32.665  0.50 36.08           N  
-ATOM   3834  CD2 HIS A 486      24.823  79.703  31.325  0.50 36.35           C  
-ATOM   3835  CE1 HIS A 486      26.411  78.208  31.560  0.50 35.51           C  
-ATOM   3836  NE2 HIS A 486      25.487  78.657  30.732  0.50 37.68           N  
-ATOM   3837  N   SER A 487      24.894  81.010  37.348  0.50 34.04           N  
-ATOM   3838  CA  SER A 487      24.811  81.960  38.450  0.50 28.39           C  
-ATOM   3839  C   SER A 487      26.188  82.106  39.092  0.50 28.04           C  
-ATOM   3840  O   SER A 487      27.065  81.265  38.890  0.50 27.11           O  
-ATOM   3841  CB  SER A 487      23.794  81.474  39.482  0.50 25.56           C  
-ATOM   3842  OG  SER A 487      23.713  82.353  40.590  0.50 28.05           O  
-ATOM   3843  N   GLN A 488      26.383  83.183  39.846  0.50 29.08           N  
-ATOM   3844  CA  GLN A 488      27.663  83.425  40.505  0.50 33.38           C  
-ATOM   3845  C   GLN A 488      27.706  82.921  41.945  0.50 34.42           C  
-ATOM   3846  O   GLN A 488      28.760  82.941  42.584  0.50 31.91           O  
-ATOM   3847  CB  GLN A 488      28.013  84.914  40.459  0.50 33.44           C  
-ATOM   3848  CG  GLN A 488      28.280  85.444  39.058  0.50 36.77           C  
-ATOM   3849  CD  GLN A 488      29.414  84.712  38.363  0.50 40.54           C  
-ATOM   3850  OE1 GLN A 488      30.585  85.055  38.526  0.50 42.01           O  
-ATOM   3851  NE2 GLN A 488      29.070  83.694  37.585  0.50 41.95           N  
-ATOM   3852  N   GLU A 489      26.563  82.455  42.442  0.50 34.84           N  
-ATOM   3853  CA  GLU A 489      26.463  81.947  43.807  0.50 35.84           C  
-ATOM   3854  C   GLU A 489      27.104  80.569  43.950  0.50 36.95           C  
-ATOM   3855  O   GLU A 489      27.542  79.972  42.964  0.50 35.69           O  
-ATOM   3856  CB  GLU A 489      24.997  81.887  44.243  0.50 33.03           C  
-ATOM   3857  CG  GLU A 489      24.251  83.208  44.115  0.50 37.08           C  
-ATOM   3858  CD  GLU A 489      24.931  84.347  44.856  0.50 42.26           C  
-ATOM   3859  OE1 GLU A 489      25.055  84.268  46.098  0.50 43.95           O  
-ATOM   3860  OE2 GLU A 489      25.340  85.325  44.196  0.50 41.46           O  
-ATOM   3861  N   SER A 490      27.168  80.078  45.186  1.00 43.41           N  
-ATOM   3862  CA  SER A 490      27.752  78.764  45.469  1.00 46.55           C  
-ATOM   3863  C   SER A 490      26.844  77.660  44.928  1.00 44.55           C  
-ATOM   3864  O   SER A 490      25.619  77.737  45.052  1.00 41.03           O  
-ATOM   3865  CB  SER A 490      27.957  78.577  46.976  1.00 45.31           C  
-ATOM   3866  OG  SER A 490      28.793  79.586  47.514  1.00 51.80           O  
-ATOM   3867  N   LYS A 491      27.447  76.631  44.340  1.00 41.33           N  
-ATOM   3868  CA  LYS A 491      26.679  75.530  43.769  1.00 39.27           C  
-ATOM   3869  C   LYS A 491      26.387  74.378  44.723  1.00 36.68           C  
-ATOM   3870  O   LYS A 491      27.281  73.882  45.410  1.00 40.99           O  
-ATOM   3871  CB  LYS A 491      27.362  74.996  42.506  1.00 43.64           C  
-ATOM   3872  CG  LYS A 491      27.568  76.050  41.431  1.00 56.34           C  
-ATOM   3873  CD  LYS A 491      26.267  76.782  41.137  1.00 64.58           C  
-ATOM   3874  CE  LYS A 491      26.499  78.006  40.269  1.00 70.97           C  
-ATOM   3875  NZ  LYS A 491      25.243  78.789  40.132  1.00 78.94           N  
-ATOM   3876  N   TRP A 492      25.116  73.984  44.768  1.00 32.50           N  
-ATOM   3877  CA  TRP A 492      24.650  72.874  45.596  1.00 24.81           C  
-ATOM   3878  C   TRP A 492      24.979  71.610  44.807  1.00 24.09           C  
-ATOM   3879  O   TRP A 492      24.392  71.353  43.758  1.00 30.92           O  
-ATOM   3880  CB  TRP A 492      23.133  72.997  45.818  1.00 25.72           C  
-ATOM   3881  CG  TRP A 492      22.482  71.903  46.649  1.00 25.82           C  
-ATOM   3882  CD1 TRP A 492      23.001  70.673  46.963  1.00 25.80           C  
-ATOM   3883  CD2 TRP A 492      21.178  71.943  47.239  1.00 16.47           C  
-ATOM   3884  NE1 TRP A 492      22.100  69.950  47.702  1.00 23.42           N  
-ATOM   3885  CE2 TRP A 492      20.971  70.702  47.887  1.00 19.06           C  
-ATOM   3886  CE3 TRP A 492      20.159  72.906  47.281  1.00 13.08           C  
-ATOM   3887  CZ2 TRP A 492      19.786  70.397  48.570  1.00 16.74           C  
-ATOM   3888  CZ3 TRP A 492      18.980  72.604  47.961  1.00 18.43           C  
-ATOM   3889  CH2 TRP A 492      18.805  71.354  48.596  1.00 10.07           C  
-ATOM   3890  N   PRO A 493      25.924  70.802  45.309  1.00 29.54           N  
-ATOM   3891  CA  PRO A 493      26.335  69.562  44.642  1.00 29.88           C  
-ATOM   3892  C   PRO A 493      25.225  68.537  44.441  1.00 31.20           C  
-ATOM   3893  O   PRO A 493      24.262  68.464  45.207  1.00 33.18           O  
-ATOM   3894  CB  PRO A 493      27.408  69.011  45.583  1.00 27.41           C  
-ATOM   3895  CG  PRO A 493      27.946  70.232  46.249  1.00 37.04           C  
-ATOM   3896  CD  PRO A 493      26.697  71.004  46.543  1.00 30.31           C  
-ATOM   3897  N   LEU A 494      25.368  67.753  43.382  1.00 29.97           N  
-ATOM   3898  CA  LEU A 494      24.421  66.699  43.079  1.00 30.76           C  
-ATOM   3899  C   LEU A 494      24.865  65.508  43.936  1.00 31.08           C  
-ATOM   3900  O   LEU A 494      26.065  65.268  44.107  1.00 27.30           O  
-ATOM   3901  CB  LEU A 494      24.492  66.358  41.583  1.00 28.51           C  
-ATOM   3902  CG  LEU A 494      23.548  65.326  40.961  1.00 28.70           C  
-ATOM   3903  CD1 LEU A 494      22.101  65.761  41.109  1.00 20.48           C  
-ATOM   3904  CD2 LEU A 494      23.891  65.158  39.494  1.00 30.22           C  
-ATOM   3905  N   PHE A 495      23.903  64.835  44.556  1.00 29.36           N  
-ATOM   3906  CA  PHE A 495      24.191  63.671  45.384  1.00 23.62           C  
-ATOM   3907  C   PHE A 495      24.315  62.442  44.477  1.00 23.68           C  
-ATOM   3908  O   PHE A 495      23.363  62.063  43.782  1.00 26.62           O  
-ATOM   3909  CB  PHE A 495      23.058  63.441  46.391  1.00 26.54           C  
-ATOM   3910  CG  PHE A 495      23.236  62.194  47.250  1.00 24.47           C  
-ATOM   3911  CD1 PHE A 495      22.970  60.931  46.713  1.00 20.76           C  
-ATOM   3912  CD2 PHE A 495      23.657  62.321  48.576  1.00 22.78           C  
-ATOM   3913  CE1 PHE A 495      23.128  59.789  47.505  1.00 20.24           C  
-ATOM   3914  CE2 PHE A 495      23.815  61.179  49.369  1.00 24.31           C  
-ATOM   3915  CZ  PHE A 495      23.550  59.913  48.834  1.00 20.02           C  
-ATOM   3916  N   THR A 496      25.495  61.847  44.492  1.00 24.17           N  
-ATOM   3917  CA  THR A 496      25.782  60.651  43.678  1.00 25.86           C  
-ATOM   3918  C   THR A 496      26.111  59.461  44.590  1.00 28.51           C  
-ATOM   3919  O   THR A 496      26.533  59.637  45.742  1.00 30.61           O  
-ATOM   3920  CB  THR A 496      26.964  60.915  42.744  1.00 25.70           C  
-ATOM   3921  OG1 THR A 496      28.133  61.184  43.504  1.00 25.58           O  
-ATOM   3922  CG2 THR A 496      26.737  62.109  41.815  1.00 22.52           C  
-ATOM   3923  N   THR A 497      25.903  58.285  44.025  1.00 30.55           N  
-ATOM   3924  CA  THR A 497      26.116  56.996  44.708  1.00 36.95           C  
-ATOM   3925  C   THR A 497      27.549  56.851  45.234  1.00 36.65           C  
-ATOM   3926  O   THR A 497      27.800  56.134  46.213  1.00 38.29           O  
-ATOM   3927  CB  THR A 497      25.889  55.838  43.730  1.00 38.98           C  
-ATOM   3928  OG1 THR A 497      24.538  55.819  43.299  1.00 44.67           O  
-ATOM   3929  CG2 THR A 497      26.195  54.470  44.344  1.00 40.75           C  
-ATOM   3930  N   LYS A 498      28.455  57.537  44.569  1.00 38.08           N  
-ATOM   3931  CA  LYS A 498      29.893  57.466  44.881  1.00 38.07           C  
-ATOM   3932  C   LYS A 498      30.315  58.517  45.905  1.00 37.94           C  
-ATOM   3933  O   LYS A 498      30.754  58.179  47.002  1.00 39.72           O  
-ATOM   3934  CB  LYS A 498      30.704  57.690  43.603  1.00 44.97           C  
-ATOM   3935  CG  LYS A 498      32.218  57.659  43.825  1.00 55.95           C  
-ATOM   3936  CD  LYS A 498      33.001  58.020  42.560  1.00 61.04           C  
-ATOM   3937  CE  LYS A 498      34.516  58.030  42.766  1.00 55.14           C  
-ATOM   3938  NZ  LYS A 498      35.250  58.511  41.586  1.00 55.36           N  
-ATOM   3939  N   GLU A 499      30.183  59.788  45.531  1.00 39.98           N  
-ATOM   3940  CA  GLU A 499      30.572  60.908  46.389  1.00 40.46           C  
-ATOM   3941  C   GLU A 499      29.655  61.111  47.599  1.00 40.92           C  
-ATOM   3942  O   GLU A 499      30.130  61.378  48.705  1.00 41.48           O  
-ATOM   3943  CB  GLU A 499      30.641  62.197  45.564  1.00 49.77           C  
-ATOM   3944  CG  GLU A 499      31.463  62.093  44.279  1.00 56.83           C  
-ATOM   3945  CD  GLU A 499      32.957  62.017  44.532  1.00 63.91           C  
-ATOM   3946  OE1 GLU A 499      33.463  60.911  44.827  1.00 65.27           O  
-ATOM   3947  OE2 GLU A 499      33.629  63.066  44.421  1.00 69.14           O  
-ATOM   3948  N   GLN A 500      28.345  61.012  47.374  1.00 37.62           N  
-ATOM   3949  CA  GLN A 500      27.340  61.170  48.429  1.00 30.81           C  
-ATOM   3950  C   GLN A 500      27.366  62.538  49.117  1.00 31.18           C  
-ATOM   3951  O   GLN A 500      27.288  62.633  50.341  1.00 34.17           O  
-ATOM   3952  CB  GLN A 500      27.481  60.044  49.459  1.00 31.32           C  
-ATOM   3953  CG  GLN A 500      27.164  58.662  48.905  1.00 33.70           C  
-ATOM   3954  CD  GLN A 500      27.569  57.545  49.845  1.00 38.05           C  
-ATOM   3955  OE1 GLN A 500      28.540  56.835  49.597  1.00 42.77           O  
-ATOM   3956  NE2 GLN A 500      26.810  57.369  50.918  1.00 38.72           N  
-ATOM   3957  N   LYS A 501      27.427  63.595  48.313  1.00 27.05           N  
-ATOM   3958  CA  LYS A 501      27.476  64.961  48.825  1.00 27.15           C  
-ATOM   3959  C   LYS A 501      26.124  65.564  49.213  1.00 29.77           C  
-ATOM   3960  O   LYS A 501      25.078  65.213  48.657  1.00 25.56           O  
-ATOM   3961  CB  LYS A 501      28.145  65.888  47.802  1.00 29.96           C  
-ATOM   3962  CG  LYS A 501      29.572  65.523  47.430  1.00 32.46           C  
-ATOM   3963  CD  LYS A 501      30.129  66.518  46.421  1.00 26.27           C  
-ATOM   3964  CE  LYS A 501      31.573  66.208  46.067  1.00 28.30           C  
-ATOM   3965  NZ  LYS A 501      32.115  67.183  45.080  1.00 33.79           N  
-ATOM   3966  N   PHE A 502      26.174  66.494  50.163  1.00 24.15           N  
-ATOM   3967  CA  PHE A 502      24.997  67.212  50.639  1.00 20.55           C  
-ATOM   3968  C   PHE A 502      25.451  68.571  51.166  1.00 22.42           C  
-ATOM   3969  O   PHE A 502      26.650  68.847  51.227  1.00 19.11           O  
-ATOM   3970  CB  PHE A 502      24.250  66.419  51.725  1.00 23.39           C  
-ATOM   3971  CG  PHE A 502      24.948  66.376  53.059  1.00 19.83           C  
-ATOM   3972  CD1 PHE A 502      25.865  65.372  53.348  1.00 15.19           C  
-ATOM   3973  CD2 PHE A 502      24.669  67.330  54.034  1.00 14.59           C  
-ATOM   3974  CE1 PHE A 502      26.493  65.316  54.588  1.00 11.58           C  
-ATOM   3975  CE2 PHE A 502      25.291  67.285  55.277  1.00 16.76           C  
-ATOM   3976  CZ  PHE A 502      26.206  66.274  55.554  1.00 21.73           C  
-ATOM   3977  N   ILE A 503      24.502  69.428  51.525  1.00 19.72           N  
-ATOM   3978  CA  ILE A 503      24.855  70.745  52.042  1.00 25.64           C  
-ATOM   3979  C   ILE A 503      24.097  71.086  53.315  1.00 26.27           C  
-ATOM   3980  O   ILE A 503      23.087  70.461  53.639  1.00 25.40           O  
-ATOM   3981  CB  ILE A 503      24.562  71.881  51.021  1.00 25.04           C  
-ATOM   3982  CG1 ILE A 503      23.057  71.999  50.765  1.00 20.85           C  
-ATOM   3983  CG2 ILE A 503      25.316  71.640  49.728  1.00 25.59           C  
-ATOM   3984  CD1 ILE A 503      22.641  73.324  50.171  1.00 25.99           C  
-ATOM   3985  N   ASP A 504      24.619  72.064  54.047  1.00 28.96           N  
-ATOM   3986  CA  ASP A 504      23.980  72.541  55.263  1.00 30.37           C  
-ATOM   3987  C   ASP A 504      23.095  73.697  54.822  1.00 30.02           C  
-ATOM   3988  O   ASP A 504      23.485  74.493  53.965  1.00 32.84           O  
-ATOM   3989  CB  ASP A 504      25.014  73.049  56.277  1.00 29.74           C  
-ATOM   3990  CG  ASP A 504      25.817  71.934  56.918  1.00 29.32           C  
-ATOM   3991  OD1 ASP A 504      25.392  70.764  56.865  1.00 36.44           O  
-ATOM   3992  OD2 ASP A 504      26.877  72.238  57.498  1.00 37.58           O  
-ATOM   3993  N   LEU A 505      21.896  73.768  55.383  1.00 29.97           N  
-ATOM   3994  CA  LEU A 505      20.969  74.831  55.044  1.00 26.71           C  
-ATOM   3995  C   LEU A 505      20.788  75.752  56.248  1.00 28.19           C  
-ATOM   3996  O   LEU A 505      19.872  75.577  57.049  1.00 30.93           O  
-ATOM   3997  CB  LEU A 505      19.636  74.230  54.602  1.00 26.66           C  
-ATOM   3998  CG  LEU A 505      18.966  74.819  53.362  1.00 26.89           C  
-ATOM   3999  CD1 LEU A 505      19.939  74.875  52.188  1.00 22.48           C  
-ATOM   4000  CD2 LEU A 505      17.760  73.970  53.012  1.00 23.98           C  
-ATOM   4001  N   ASN A 506      21.697  76.712  56.384  1.00 30.06           N  
-ATOM   4002  CA  ASN A 506      21.654  77.671  57.485  1.00 31.49           C  
-ATOM   4003  C   ASN A 506      21.997  79.089  57.030  1.00 34.35           C  
-ATOM   4004  O   ASN A 506      22.095  79.358  55.833  1.00 40.67           O  
-ATOM   4005  CB  ASN A 506      22.583  77.230  58.622  1.00 27.57           C  
-ATOM   4006  CG  ASN A 506      23.970  76.853  58.138  1.00 24.69           C  
-ATOM   4007  OD1 ASN A 506      24.590  77.594  57.376  1.00 24.09           O  
-ATOM   4008  ND2 ASN A 506      24.458  75.692  58.560  1.00 19.78           N  
-ATOM   4009  N   THR A 507      22.200  79.985  57.992  1.00 38.55           N  
-ATOM   4010  CA  THR A 507      22.514  81.384  57.705  1.00 39.73           C  
-ATOM   4011  C   THR A 507      23.970  81.667  57.314  1.00 40.91           C  
-ATOM   4012  O   THR A 507      24.282  82.754  56.825  1.00 43.03           O  
-ATOM   4013  CB  THR A 507      22.106  82.292  58.889  1.00 37.31           C  
-ATOM   4014  OG1 THR A 507      22.674  81.785  60.103  1.00 38.66           O  
-ATOM   4015  CG2 THR A 507      20.592  82.337  59.029  1.00 29.05           C  
-ATOM   4016  N   GLU A 508      24.856  80.702  57.546  1.00 41.98           N  
-ATOM   4017  CA  GLU A 508      26.270  80.848  57.198  1.00 46.48           C  
-ATOM   4018  C   GLU A 508      26.504  80.464  55.734  1.00 49.18           C  
-ATOM   4019  O   GLU A 508      25.649  79.832  55.112  1.00 48.38           O  
-ATOM   4020  CB  GLU A 508      27.140  79.973  58.112  1.00 49.17           C  
-ATOM   4021  CG  GLU A 508      27.393  80.548  59.506  1.00 59.66           C  
-ATOM   4022  CD  GLU A 508      26.170  80.514  60.403  1.00 66.57           C  
-ATOM   4023  OE1 GLU A 508      25.730  79.403  60.762  1.00 71.20           O  
-ATOM   4024  OE2 GLU A 508      25.658  81.597  60.758  1.00 67.55           O  
-ATOM   4025  N   PRO A 509      27.653  80.871  55.152  1.00 50.19           N  
-ATOM   4026  CA  PRO A 509      27.937  80.531  53.753  1.00 49.68           C  
-ATOM   4027  C   PRO A 509      27.894  79.019  53.521  1.00 49.85           C  
-ATOM   4028  O   PRO A 509      28.350  78.239  54.361  1.00 48.44           O  
-ATOM   4029  CB  PRO A 509      29.338  81.120  53.533  1.00 47.63           C  
-ATOM   4030  CG  PRO A 509      29.927  81.172  54.914  1.00 46.78           C  
-ATOM   4031  CD  PRO A 509      28.760  81.656  55.725  1.00 50.39           C  
-ATOM   4032  N   MET A 510      27.325  78.619  52.385  1.00 51.04           N  
-ATOM   4033  CA  MET A 510      27.178  77.211  52.035  1.00 48.08           C  
-ATOM   4034  C   MET A 510      28.434  76.382  52.236  1.00 47.72           C  
-ATOM   4035  O   MET A 510      29.523  76.757  51.799  1.00 50.85           O  
-ATOM   4036  CB  MET A 510      26.708  77.058  50.588  1.00 49.94           C  
-ATOM   4037  CG  MET A 510      26.451  75.613  50.173  1.00 48.15           C  
-ATOM   4038  SD  MET A 510      26.221  75.419  48.399  1.00 44.63           S  
-ATOM   4039  CE  MET A 510      24.531  75.905  48.227  1.00 36.55           C  
-ATOM   4040  N   LYS A 511      28.264  75.254  52.914  1.00 46.98           N  
-ATOM   4041  CA  LYS A 511      29.358  74.332  53.176  1.00 46.26           C  
-ATOM   4042  C   LYS A 511      28.920  72.951  52.688  1.00 44.96           C  
-ATOM   4043  O   LYS A 511      27.778  72.540  52.911  1.00 43.79           O  
-ATOM   4044  CB  LYS A 511      29.675  74.316  54.672  1.00 47.69           C  
-ATOM   4045  CG  LYS A 511      30.802  73.385  55.083  1.00 59.88           C  
-ATOM   4046  CD  LYS A 511      31.265  73.706  56.490  1.00 72.01           C  
-ATOM   4047  CE  LYS A 511      32.124  74.967  56.511  1.00 75.84           C  
-ATOM   4048  NZ  LYS A 511      31.794  75.832  57.679  1.00 79.98           N  
-ATOM   4049  N   VAL A 512      29.823  72.254  52.004  1.00 39.62           N  
-ATOM   4050  CA  VAL A 512      29.534  70.929  51.462  1.00 32.11           C  
-ATOM   4051  C   VAL A 512      30.174  69.805  52.272  1.00 31.15           C  
-ATOM   4052  O   VAL A 512      31.348  69.880  52.638  1.00 31.02           O  
-ATOM   4053  CB  VAL A 512      29.995  70.825  49.987  1.00 35.49           C  
-ATOM   4054  CG1 VAL A 512      29.682  69.448  49.419  1.00 25.40           C  
-ATOM   4055  CG2 VAL A 512      29.325  71.909  49.154  1.00 33.82           C  
-ATOM   4056  N   HIS A 513      29.388  68.762  52.539  1.00 29.21           N  
-ATOM   4057  CA  HIS A 513      29.846  67.598  53.299  1.00 27.43           C  
-ATOM   4058  C   HIS A 513      29.541  66.312  52.539  1.00 25.88           C  
-ATOM   4059  O   HIS A 513      28.967  66.348  51.450  1.00 25.89           O  
-ATOM   4060  CB  HIS A 513      29.152  67.540  54.663  1.00 34.96           C  
-ATOM   4061  CG  HIS A 513      29.267  68.800  55.460  1.00 35.67           C  
-ATOM   4062  ND1 HIS A 513      30.411  69.141  56.149  1.00 38.05           N  
-ATOM   4063  CD2 HIS A 513      28.382  69.799  55.679  1.00 30.60           C  
-ATOM   4064  CE1 HIS A 513      30.225  70.296  56.761  1.00 36.36           C  
-ATOM   4065  NE2 HIS A 513      29.003  70.718  56.490  1.00 33.02           N  
-ATOM   4066  N   GLN A 514      29.923  65.179  53.126  1.00 30.62           N  
-ATOM   4067  CA  GLN A 514      29.691  63.869  52.522  1.00 31.52           C  
-ATOM   4068  C   GLN A 514      29.235  62.848  53.555  1.00 28.72           C  
-ATOM   4069  O   GLN A 514      29.534  62.977  54.742  1.00 32.04           O  
-ATOM   4070  CB  GLN A 514      30.964  63.342  51.857  1.00 36.39           C  
-ATOM   4071  CG  GLN A 514      31.458  64.151  50.678  1.00 45.81           C  
-ATOM   4072  CD  GLN A 514      32.749  63.596  50.115  1.00 49.65           C  
-ATOM   4073  OE1 GLN A 514      33.799  63.666  50.755  1.00 58.27           O  
-ATOM   4074  NE2 GLN A 514      32.675  63.029  48.917  1.00 49.26           N  
-ATOM   4075  N   ARG A 515      28.510  61.836  53.083  1.00 32.40           N  
-ATOM   4076  CA  ARG A 515      28.010  60.745  53.919  1.00 30.56           C  
-ATOM   4077  C   ARG A 515      27.289  61.201  55.193  1.00 27.90           C  
-ATOM   4078  O   ARG A 515      27.785  61.002  56.308  1.00 25.13           O  
-ATOM   4079  CB  ARG A 515      29.162  59.803  54.267  1.00 36.92           C  
-ATOM   4080  CG  ARG A 515      29.860  59.189  53.062  1.00 45.57           C  
-ATOM   4081  CD  ARG A 515      31.014  58.312  53.509  1.00 51.92           C  
-ATOM   4082  NE  ARG A 515      31.764  57.753  52.389  1.00 58.66           N  
-ATOM   4083  CZ  ARG A 515      31.774  56.465  52.056  1.00 64.98           C  
-ATOM   4084  NH1 ARG A 515      31.067  55.584  52.752  1.00 69.48           N  
-ATOM   4085  NH2 ARG A 515      32.508  56.053  51.032  1.00 65.32           N  
-ATOM   4086  N   LEU A 516      26.104  61.782  55.012  1.00 25.84           N  
-ATOM   4087  CA  LEU A 516      25.288  62.287  56.112  1.00 23.45           C  
-ATOM   4088  C   LEU A 516      24.975  61.215  57.152  1.00 23.93           C  
-ATOM   4089  O   LEU A 516      24.239  60.268  56.882  1.00 25.95           O  
-ATOM   4090  CB  LEU A 516      23.991  62.905  55.571  1.00 21.92           C  
-ATOM   4091  CG  LEU A 516      22.963  63.486  56.548  1.00 26.26           C  
-ATOM   4092  CD1 LEU A 516      23.630  64.439  57.519  1.00 30.79           C  
-ATOM   4093  CD2 LEU A 516      21.860  64.200  55.781  1.00 16.66           C  
-ATOM   4094  N   ARG A 517      25.580  61.374  58.329  1.00 24.42           N  
-ATOM   4095  CA  ARG A 517      25.418  60.471  59.468  1.00 22.03           C  
-ATOM   4096  C   ARG A 517      25.568  58.988  59.146  1.00 23.90           C  
-ATOM   4097  O   ARG A 517      24.736  58.177  59.550  1.00 29.16           O  
-ATOM   4098  CB  ARG A 517      24.082  60.735  60.181  1.00 24.87           C  
-ATOM   4099  CG  ARG A 517      23.949  62.152  60.725  1.00 29.35           C  
-ATOM   4100  CD  ARG A 517      22.697  62.334  61.568  1.00 26.69           C  
-ATOM   4101  NE  ARG A 517      22.776  61.629  62.845  1.00 33.14           N  
-ATOM   4102  CZ  ARG A 517      23.537  62.005  63.872  1.00 30.09           C  
-ATOM   4103  NH1 ARG A 517      24.298  63.087  63.778  1.00 33.49           N  
-ATOM   4104  NH2 ARG A 517      23.529  61.309  64.999  1.00 19.33           N  
-ATOM   4105  N   VAL A 518      26.634  58.633  58.431  1.00 24.26           N  
-ATOM   4106  CA  VAL A 518      26.875  57.232  58.079  1.00 25.61           C  
-ATOM   4107  C   VAL A 518      27.160  56.359  59.287  1.00 25.58           C  
-ATOM   4108  O   VAL A 518      26.695  55.225  59.352  1.00 31.25           O  
-ATOM   4109  CB  VAL A 518      28.045  57.053  57.089  1.00 24.86           C  
-ATOM   4110  CG1 VAL A 518      27.547  57.216  55.675  1.00 28.36           C  
-ATOM   4111  CG2 VAL A 518      29.177  58.031  57.403  1.00 15.19           C  
-ATOM   4112  N   GLN A 519      27.917  56.894  60.241  1.00 27.58           N  
-ATOM   4113  CA  GLN A 519      28.276  56.158  61.450  1.00 30.00           C  
-ATOM   4114  C   GLN A 519      27.034  55.585  62.112  1.00 27.28           C  
-ATOM   4115  O   GLN A 519      26.935  54.374  62.325  1.00 29.38           O  
-ATOM   4116  CB  GLN A 519      28.982  57.079  62.446  1.00 40.25           C  
-ATOM   4117  CG  GLN A 519      30.258  57.727  61.931  1.00 48.26           C  
-ATOM   4118  CD  GLN A 519      31.389  56.737  61.683  1.00 51.42           C  
-ATOM   4119  OE1 GLN A 519      32.414  57.100  61.109  1.00 49.32           O  
-ATOM   4120  NE2 GLN A 519      31.214  55.488  62.117  1.00 46.38           N  
-ATOM   4121  N   MET A 520      26.077  56.465  62.400  1.00 22.68           N  
-ATOM   4122  CA  MET A 520      24.837  56.068  63.046  1.00 24.44           C  
-ATOM   4123  C   MET A 520      23.904  55.291  62.128  1.00 23.55           C  
-ATOM   4124  O   MET A 520      23.255  54.343  62.567  1.00 30.20           O  
-ATOM   4125  CB  MET A 520      24.109  57.294  63.602  1.00 25.74           C  
-ATOM   4126  CG  MET A 520      24.876  58.064  64.673  1.00 33.93           C  
-ATOM   4127  SD  MET A 520      25.421  57.065  66.084  1.00 39.49           S  
-ATOM   4128  CE  MET A 520      27.206  57.171  65.897  1.00 48.81           C  
-ATOM   4129  N   CYS A 521      23.845  55.678  60.856  1.00 20.70           N  
-ATOM   4130  CA  CYS A 521      22.956  55.009  59.916  1.00 14.68           C  
-ATOM   4131  C   CYS A 521      23.411  53.631  59.453  1.00 18.82           C  
-ATOM   4132  O   CYS A 521      22.592  52.852  58.962  1.00 22.57           O  
-ATOM   4133  CB  CYS A 521      22.604  55.920  58.741  1.00 17.85           C  
-ATOM   4134  SG  CYS A 521      21.629  57.379  59.245  1.00 20.15           S  
-ATOM   4135  N   VAL A 522      24.700  53.322  59.602  1.00 13.08           N  
-ATOM   4136  CA  VAL A 522      25.188  51.988  59.251  1.00 15.76           C  
-ATOM   4137  C   VAL A 522      24.648  51.077  60.355  1.00 18.69           C  
-ATOM   4138  O   VAL A 522      24.311  49.919  60.119  1.00 23.91           O  
-ATOM   4139  CB  VAL A 522      26.737  51.901  59.231  1.00 17.06           C  
-ATOM   4140  CG1 VAL A 522      27.183  50.444  59.124  1.00 14.00           C  
-ATOM   4141  CG2 VAL A 522      27.293  52.683  58.056  1.00 15.90           C  
-ATOM   4142  N   PHE A 523      24.545  51.634  61.558  1.00 20.78           N  
-ATOM   4143  CA  PHE A 523      24.029  50.907  62.706  1.00 18.76           C  
-ATOM   4144  C   PHE A 523      22.529  50.660  62.574  1.00 16.61           C  
-ATOM   4145  O   PHE A 523      22.064  49.545  62.777  1.00 22.07           O  
-ATOM   4146  CB  PHE A 523      24.319  51.682  63.997  1.00 15.71           C  
-ATOM   4147  CG  PHE A 523      23.603  51.138  65.202  1.00 15.44           C  
-ATOM   4148  CD1 PHE A 523      24.101  50.033  65.884  1.00 16.62           C  
-ATOM   4149  CD2 PHE A 523      22.421  51.725  65.650  1.00 16.22           C  
-ATOM   4150  CE1 PHE A 523      23.432  49.518  66.994  1.00 16.28           C  
-ATOM   4151  CE2 PHE A 523      21.742  51.216  66.761  1.00 14.12           C  
-ATOM   4152  CZ  PHE A 523      22.250  50.111  67.432  1.00 18.11           C  
-ATOM   4153  N   TRP A 524      21.774  51.698  62.230  1.00 14.38           N  
-ATOM   4154  CA  TRP A 524      20.323  51.573  62.099  1.00 14.53           C  
-ATOM   4155  C   TRP A 524      19.841  50.814  60.867  1.00 15.69           C  
-ATOM   4156  O   TRP A 524      18.889  50.036  60.953  1.00 18.95           O  
-ATOM   4157  CB  TRP A 524      19.661  52.955  62.113  1.00 16.44           C  
-ATOM   4158  CG  TRP A 524      19.695  53.634  63.443  1.00 16.68           C  
-ATOM   4159  CD1 TRP A 524      20.468  54.703  63.800  1.00 18.06           C  
-ATOM   4160  CD2 TRP A 524      18.925  53.289  64.602  1.00 17.27           C  
-ATOM   4161  NE1 TRP A 524      20.228  55.044  65.107  1.00 19.04           N  
-ATOM   4162  CE2 TRP A 524      19.289  54.193  65.628  1.00 19.92           C  
-ATOM   4163  CE3 TRP A 524      17.966  52.301  64.877  1.00 16.05           C  
-ATOM   4164  CZ2 TRP A 524      18.728  54.141  66.912  1.00 16.87           C  
-ATOM   4165  CZ3 TRP A 524      17.407  52.248  66.153  1.00 12.81           C  
-ATOM   4166  CH2 TRP A 524      17.793  53.165  67.156  1.00 13.53           C  
-ATOM   4167  N   ASN A 525      20.495  51.042  59.730  1.00 20.44           N  
-ATOM   4168  CA  ASN A 525      20.103  50.409  58.473  1.00 21.45           C  
-ATOM   4169  C   ASN A 525      20.757  49.066  58.166  1.00 23.71           C  
-ATOM   4170  O   ASN A 525      20.170  48.237  57.470  1.00 26.44           O  
-ATOM   4171  CB  ASN A 525      20.344  51.369  57.304  1.00 20.94           C  
-ATOM   4172  CG  ASN A 525      19.584  52.681  57.451  1.00 24.34           C  
-ATOM   4173  OD1 ASN A 525      18.418  52.689  57.844  1.00 31.76           O  
-ATOM   4174  ND2 ASN A 525      20.246  53.794  57.151  1.00 33.15           N  
-ATOM   4175  N   GLN A 526      21.960  48.842  58.685  1.00 24.65           N  
-ATOM   4176  CA  GLN A 526      22.663  47.595  58.416  1.00 28.14           C  
-ATOM   4177  C   GLN A 526      22.894  46.668  59.610  1.00 29.68           C  
-ATOM   4178  O   GLN A 526      22.603  45.474  59.522  1.00 35.62           O  
-ATOM   4179  CB  GLN A 526      23.986  47.895  57.705  1.00 34.94           C  
-ATOM   4180  CG  GLN A 526      23.802  48.583  56.354  1.00 52.96           C  
-ATOM   4181  CD  GLN A 526      25.030  49.355  55.905  1.00 66.72           C  
-ATOM   4182  OE1 GLN A 526      26.121  48.795  55.770  1.00 72.49           O  
-ATOM   4183  NE2 GLN A 526      24.855  50.654  55.667  1.00 69.52           N  
-ATOM   4184  N   PHE A 527      23.374  47.206  60.731  1.00 27.44           N  
-ATOM   4185  CA  PHE A 527      23.657  46.370  61.897  1.00 26.00           C  
-ATOM   4186  C   PHE A 527      22.472  45.931  62.760  1.00 26.04           C  
-ATOM   4187  O   PHE A 527      22.249  44.731  62.938  1.00 30.21           O  
-ATOM   4188  CB  PHE A 527      24.734  47.006  62.783  1.00 21.25           C  
-ATOM   4189  CG  PHE A 527      25.131  46.146  63.952  1.00 17.99           C  
-ATOM   4190  CD1 PHE A 527      25.900  45.002  63.759  1.00 17.53           C  
-ATOM   4191  CD2 PHE A 527      24.703  46.457  65.239  1.00 16.64           C  
-ATOM   4192  CE1 PHE A 527      26.234  44.178  64.829  1.00 16.67           C  
-ATOM   4193  CE2 PHE A 527      25.032  45.637  66.314  1.00 17.61           C  
-ATOM   4194  CZ  PHE A 527      25.799  44.495  66.107  1.00 15.21           C  
-ATOM   4195  N   LEU A 528      21.752  46.893  63.334  1.00 17.93           N  
-ATOM   4196  CA  LEU A 528      20.608  46.592  64.191  1.00 16.74           C  
-ATOM   4197  C   LEU A 528      19.585  45.641  63.566  1.00 21.24           C  
-ATOM   4198  O   LEU A 528      19.193  44.662  64.199  1.00 24.65           O  
-ATOM   4199  CB  LEU A 528      19.922  47.872  64.676  1.00 11.19           C  
-ATOM   4200  CG  LEU A 528      18.778  47.616  65.664  1.00 13.11           C  
-ATOM   4201  CD1 LEU A 528      19.304  46.905  66.908  1.00 13.16           C  
-ATOM   4202  CD2 LEU A 528      18.097  48.917  66.043  1.00  6.93           C  
-ATOM   4203  N   PRO A 529      19.133  45.913  62.326  1.00 20.87           N  
-ATOM   4204  CA  PRO A 529      18.158  45.011  61.707  1.00 25.95           C  
-ATOM   4205  C   PRO A 529      18.676  43.574  61.575  1.00 31.40           C  
-ATOM   4206  O   PRO A 529      17.900  42.620  61.636  1.00 34.38           O  
-ATOM   4207  CB  PRO A 529      17.891  45.670  60.349  1.00 21.28           C  
-ATOM   4208  CG  PRO A 529      19.124  46.465  60.093  1.00 28.65           C  
-ATOM   4209  CD  PRO A 529      19.413  47.052  61.438  1.00 22.23           C  
-ATOM   4210  N   LYS A 530      19.992  43.425  61.433  1.00 31.15           N  
-ATOM   4211  CA  LYS A 530      20.601  42.103  61.320  1.00 31.04           C  
-ATOM   4212  C   LYS A 530      20.679  41.424  62.689  1.00 33.38           C  
-ATOM   4213  O   LYS A 530      20.565  40.203  62.791  1.00 34.10           O  
-ATOM   4214  CB  LYS A 530      21.999  42.200  60.711  1.00 31.64           C  
-ATOM   4215  CG  LYS A 530      22.643  40.849  60.476  1.00 35.43           C  
-ATOM   4216  CD  LYS A 530      24.017  40.966  59.846  1.00 40.40           C  
-ATOM   4217  CE  LYS A 530      24.579  39.582  59.543  1.00 43.69           C  
-ATOM   4218  NZ  LYS A 530      25.911  39.634  58.888  1.00 42.23           N  
-ATOM   4219  N   LEU A 531      20.877  42.223  63.736  1.00 32.40           N  
-ATOM   4220  CA  LEU A 531      20.962  41.711  65.099  1.00 27.92           C  
-ATOM   4221  C   LEU A 531      19.587  41.237  65.560  1.00 31.32           C  
-ATOM   4222  O   LEU A 531      19.444  40.119  66.047  1.00 33.97           O  
-ATOM   4223  CB  LEU A 531      21.501  42.800  66.037  1.00 30.25           C  
-ATOM   4224  CG  LEU A 531      21.722  42.490  67.523  1.00 29.34           C  
-ATOM   4225  CD1 LEU A 531      22.754  43.447  68.084  1.00 27.97           C  
-ATOM   4226  CD2 LEU A 531      20.421  42.588  68.318  1.00 30.98           C  
-ATOM   4227  N   LEU A 532      18.586  42.102  65.408  1.00 33.24           N  
-ATOM   4228  CA  LEU A 532      17.214  41.790  65.798  1.00 35.82           C  
-ATOM   4229  C   LEU A 532      16.676  40.604  65.005  1.00 40.38           C  
-ATOM   4230  O   LEU A 532      15.840  39.842  65.496  1.00 40.47           O  
-ATOM   4231  CB  LEU A 532      16.306  43.002  65.572  1.00 29.63           C  
-ATOM   4232  CG  LEU A 532      16.555  44.246  66.422  1.00 28.70           C  
-ATOM   4233  CD1 LEU A 532      15.683  45.394  65.924  1.00 22.37           C  
-ATOM   4234  CD2 LEU A 532      16.279  43.942  67.882  1.00 17.82           C  
-ATOM   4235  N   ASN A 533      17.156  40.463  63.774  1.00 43.95           N  
-ATOM   4236  CA  ASN A 533      16.739  39.375  62.902  1.00 53.78           C  
-ATOM   4237  C   ASN A 533      17.313  38.027  63.344  1.00 58.50           C  
-ATOM   4238  O   ASN A 533      16.636  37.002  63.257  1.00 64.85           O  
-ATOM   4239  CB  ASN A 533      17.152  39.676  61.459  1.00 55.47           C  
-ATOM   4240  CG  ASN A 533      16.933  38.503  60.536  1.00 57.60           C  
-ATOM   4241  OD1 ASN A 533      17.778  37.613  60.463  1.00 59.74           O  
-ATOM   4242  ND2 ASN A 533      15.805  38.505  59.830  1.00 62.81           N  
-ATOM   4243  N   ALA A 534      18.560  38.034  63.810  1.00 60.83           N  
-ATOM   4244  CA  ALA A 534      19.220  36.813  64.261  1.00 62.51           C  
-ATOM   4245  C   ALA A 534      18.645  36.318  65.588  1.00 68.51           C  
-ATOM   4246  O   ALA A 534      18.716  35.126  65.899  1.00 71.60           O  
-ATOM   4247  CB  ALA A 534      20.715  37.042  64.387  1.00 63.87           C  
-ATOM   4248  N   THR A 535      18.079  37.240  66.366  1.00 71.80           N  
-ATOM   4249  CA  THR A 535      17.486  36.909  67.659  1.00 72.61           C  
-ATOM   4250  C   THR A 535      15.971  37.141  67.657  1.00 77.50           C  
-ATOM   4251  O   THR A 535      15.254  36.231  67.186  1.00 81.09           O  
-ATOM   4252  CB  THR A 535      18.152  37.710  68.811  1.00 68.46           C  
-ATOM   4253  OG1 THR A 535      18.143  39.111  68.506  1.00 59.46           O  
-ATOM   4254  CG2 THR A 535      19.581  37.251  69.024  1.00 67.80           C  
-TER    4255      THR A 535                                                      
-HETATM 4256  C1  NAG A3001     -19.059  83.350  49.722  0.70 49.79           C  
-HETATM 4257  C2  NAG A3001     -18.186  84.325  50.525  0.70 47.53           C  
-HETATM 4258  C3  NAG A3001     -17.892  85.575  49.698  0.70 51.06           C  
-HETATM 4259  C4  NAG A3001     -19.194  86.271  49.299  0.70 50.60           C  
-HETATM 4260  C5  NAG A3001     -20.219  85.248  48.792  0.70 50.07           C  
-HETATM 4261  C6  NAG A3001     -20.859  85.714  47.486  0.70 49.26           C  
-HETATM 4262  C7  NAG A3001     -18.627  84.065  52.907  0.70 50.51           C  
-HETATM 4263  C8  NAG A3001     -19.378  84.562  54.135  0.70 48.39           C  
-HETATM 4264  N2  NAG A3001     -18.855  84.711  51.763  0.70 47.95           N  
-HETATM 4265  O3  NAG A3001     -17.169  85.226  48.536  0.70 60.43           O  
-HETATM 4266  O4  NAG A3001     -19.728  86.981  50.398  0.70 47.97           O  
-HETATM 4267  O5  NAG A3001     -19.567  83.998  48.551  0.70 51.22           O  
-HETATM 4268  O6  NAG A3001     -21.726  84.718  46.988  0.70 46.05           O  
-HETATM 4269  O7  NAG A3001     -17.865  83.103  52.989  0.70 52.81           O  
-HETATM 4270  C1  NAG A3002      18.913  62.313  33.738  0.70 23.77           C  
-HETATM 4271  C2  NAG A3002      20.418  62.076  33.718  0.70 23.51           C  
-HETATM 4272  C3  NAG A3002      21.035  62.656  32.448  0.70 26.64           C  
-HETATM 4273  C4  NAG A3002      20.277  62.175  31.209  0.70 30.09           C  
-HETATM 4274  C5  NAG A3002      18.784  62.442  31.353  0.70 29.38           C  
-HETATM 4275  C6  NAG A3002      18.007  61.888  30.158  0.70 28.41           C  
-HETATM 4276  C7  NAG A3002      21.426  61.985  35.928  0.70 22.38           C  
-HETATM 4277  C8  NAG A3002      22.042  62.748  37.094  0.70 14.48           C  
-HETATM 4278  N2  NAG A3002      21.027  62.707  34.882  0.70 22.59           N  
-HETATM 4279  O3  NAG A3002      22.390  62.260  32.359  0.70 24.73           O  
-HETATM 4280  O4  NAG A3002      20.758  62.842  30.060  0.70 37.06           O  
-HETATM 4281  O5  NAG A3002      18.320  61.810  32.543  0.70 26.57           O  
-HETATM 4282  O6  NAG A3002      18.107  60.481  30.113  0.70 29.96           O  
-HETATM 4283  O7  NAG A3002      21.309  60.757  35.972  0.70 22.13           O  
-HETATM 4284  C1  NAG A3003      21.413  62.009  29.127  0.70 37.76           C  
-HETATM 4285  C2  NAG A3003      21.616  62.771  27.822  0.70 37.48           C  
-HETATM 4286  C3  NAG A3003      22.450  61.949  26.842  0.70 40.46           C  
-HETATM 4287  C4  NAG A3003      23.737  61.472  27.505  0.70 38.74           C  
-HETATM 4288  C5  NAG A3003      23.416  60.728  28.798  0.70 38.66           C  
-HETATM 4289  C6  NAG A3003      24.689  60.303  29.522  0.70 38.53           C  
-HETATM 4290  C7  NAG A3003      19.806  64.279  27.262  0.70 40.36           C  
-HETATM 4291  C8  NAG A3003      18.438  64.461  26.623  0.70 39.61           C  
-HETATM 4292  N2  NAG A3003      20.318  63.052  27.232  0.70 36.48           N  
-HETATM 4293  O3  NAG A3003      22.762  62.722  25.699  0.70 38.59           O  
-HETATM 4294  O4  NAG A3003      24.446  60.627  26.626  0.70 41.12           O  
-HETATM 4295  O5  NAG A3003      22.670  61.590  29.655  0.70 38.60           O  
-HETATM 4296  O6  NAG A3003      25.380  61.440  29.994  0.70 37.49           O  
-HETATM 4297  O7  NAG A3003      20.400  65.236  27.765  0.70 43.30           O  
-HETATM 4298  C1  NAG A3004      15.232  37.266  59.323  0.70 68.05           C  
-HETATM 4299  C2  NAG A3004      16.211  36.557  58.391  0.70 69.18           C  
-HETATM 4300  C3  NAG A3004      15.590  35.267  57.877  0.70 71.12           C  
-HETATM 4301  C4  NAG A3004      15.147  34.403  59.058  0.70 71.70           C  
-HETATM 4302  C5  NAG A3004      14.209  35.193  59.975  0.70 71.46           C  
-HETATM 4303  C6  NAG A3004      13.836  34.378  61.210  0.70 68.31           C  
-HETATM 4304  C7  NAG A3004      17.829  37.676  56.977  0.70 68.13           C  
-HETATM 4305  C8  NAG A3004      18.087  38.603  55.798  0.70 65.13           C  
-HETATM 4306  N2  NAG A3004      16.556  37.425  57.276  0.70 69.53           N  
-HETATM 4307  O3  NAG A3004      16.527  34.565  57.084  0.70 72.65           O  
-HETATM 4308  O4  NAG A3004      14.497  33.241  58.594  0.70 74.49           O  
-HETATM 4309  O5  NAG A3004      14.863  36.398  60.397  0.70 70.97           O  
-HETATM 4310  O6  NAG A3004      14.986  34.090  61.975  0.70 63.82           O  
-HETATM 4311  O7  NAG A3004      18.768  37.184  57.608  0.70 67.70           O  
-HETATM 4312  C1  NAG A3005       6.918  89.701  68.204  0.70 55.28           C  
-HETATM 4313  C2  NAG A3005       5.888  88.646  68.629  0.70 53.79           C  
-HETATM 4314  C3  NAG A3005       4.787  89.257  69.495  0.70 54.28           C  
-HETATM 4315  C4  NAG A3005       5.397  90.035  70.648  0.70 54.48           C  
-HETATM 4316  C5  NAG A3005       6.343  91.095  70.100  0.70 53.89           C  
-HETATM 4317  C6  NAG A3005       6.973  91.907  71.231  0.70 52.23           C  
-HETATM 4318  C7  NAG A3005       5.413  86.751  67.197  0.70 51.96           C  
-HETATM 4319  C8  NAG A3005       4.744  86.226  65.935  0.70 47.84           C  
-HETATM 4320  N2  NAG A3005       5.285  88.051  67.446  0.70 51.03           N  
-HETATM 4321  O3  NAG A3005       3.948  88.238  70.001  0.70 57.88           O  
-HETATM 4322  O4  NAG A3005       4.380  90.637  71.422  0.70 52.54           O  
-HETATM 4323  O5  NAG A3005       7.376  90.441  69.349  0.70 55.29           O  
-HETATM 4324  O6  NAG A3005       7.671  91.059  72.118  0.70 52.45           O  
-HETATM 4325  O7  NAG A3005       6.043  85.992  67.936  0.70 55.38           O  
-HETATM 4326  C1  E20 A2001       1.057  60.056  71.240  1.00 26.85           C  
-HETATM 4327  C2  E20 A2001       0.188  61.079  71.628  1.00 22.90           C  
-HETATM 4328  C3  E20 A2001       0.347  62.415  71.171  1.00 21.66           C  
-HETATM 4329  C4  E20 A2001       1.447  62.720  70.270  1.00 15.86           C  
-HETATM 4330  C5  E20 A2001       2.306  61.665  69.881  1.00 18.21           C  
-HETATM 4331  C6  E20 A2001       2.140  60.371  70.362  1.00 24.60           C  
-HETATM 4332  C7  E20 A2001       3.365  62.094  69.016  1.00 25.58           C  
-HETATM 4333  C8  E20 A2001       3.086  63.590  68.740  1.00 21.53           C  
-HETATM 4334  C9  E20 A2001       1.839  63.992  69.558  1.00 17.21           C  
-HETATM 4335  C10 E20 A2001       4.105  64.576  69.245  1.00 18.02           C  
-HETATM 4336  C11 E20 A2001       4.307  65.848  68.533  1.00 18.84           C  
-HETATM 4337  C12 E20 A2001       5.006  65.637  67.195  1.00 15.13           C  
-HETATM 4338  C13 E20 A2001       5.161  66.919  66.425  1.00 19.67           C  
-HETATM 4339  N14 E20 A2001       3.854  67.635  66.237  1.00 18.93           N  
-HETATM 4340  C15 E20 A2001       3.177  67.997  67.535  1.00 13.92           C  
-HETATM 4341  C16 E20 A2001       3.004  66.708  68.390  1.00 13.21           C  
-HETATM 4342  C17 E20 A2001       3.743  68.943  65.483  1.00 20.75           C  
-HETATM 4343  C18 E20 A2001       3.992  68.847  63.988  1.00 17.17           C  
-HETATM 4344  C19 E20 A2001       2.864  68.675  63.126  1.00 18.68           C  
-HETATM 4345  C20 E20 A2001       3.052  68.432  61.723  1.00 21.92           C  
-HETATM 4346  C21 E20 A2001       4.345  68.390  61.195  1.00 14.62           C  
-HETATM 4347  C22 E20 A2001       5.479  68.598  62.046  1.00 19.28           C  
-HETATM 4348  C23 E20 A2001       5.310  68.869  63.440  1.00 13.50           C  
-HETATM 4349  O24 E20 A2001       4.325  61.375  68.615  1.00 28.32           O  
-HETATM 4350  O25 E20 A2001       0.890  58.762  71.644  1.00 29.40           O  
-HETATM 4351  C26 E20 A2001       1.842  57.647  71.265  1.00 21.15           C  
-HETATM 4352  O27 E20 A2001      -0.925  61.025  72.321  1.00 22.73           O  
-HETATM 4353  C28 E20 A2001      -1.434  59.862  72.928  1.00 31.57           C  
-HETATM 4354  O   HOH A1001      -3.039  52.153  43.840  1.00 28.13           O  
-HETATM 4355  O   HOH A1002      -1.142  50.931  41.739  1.00 42.80           O  
-HETATM 4356  O   HOH A1003      -4.832  56.357  38.946  1.00 43.51           O  
-HETATM 4357  O   HOH A1004      -4.363  58.274  36.236  1.00 35.56           O  
-HETATM 4358  O   HOH A1005      -0.054  57.622  37.633  1.00 30.84           O  
-HETATM 4359  O   HOH A1006       2.701  54.471  36.256  1.00 16.48           O  
-HETATM 4360  O   HOH A1007       9.945  56.135  35.744  1.00 21.68           O  
-HETATM 4361  O   HOH A1008       9.214  50.819  36.911  1.00 22.60           O  
-HETATM 4362  O   HOH A1009      13.821  49.329  36.673  1.00 38.28           O  
-HETATM 4363  O   HOH A1010      10.612  46.340  38.691  1.00 35.71           O  
-HETATM 4364  O   HOH A1011       9.851  44.535  43.277  1.00 24.38           O  
-HETATM 4365  O   HOH A1012       9.771  40.496  46.490  1.00 39.88           O  
-HETATM 4366  O   HOH A1013       7.312  41.467  49.111  1.00 26.54           O  
-HETATM 4367  O   HOH A1014       4.628  41.463  51.761  1.00 27.60           O  
-HETATM 4368  O   HOH A1015       2.530  42.455  50.144  1.00 31.09           O  
-HETATM 4369  O   HOH A1016      -0.021  41.468  50.778  1.00 43.34           O  
-HETATM 4370  O   HOH A1017       1.369  43.543  54.480  1.00 27.29           O  
-HETATM 4371  O   HOH A1018       4.118  43.881  55.383  1.00 20.63           O  
-HETATM 4372  O   HOH A1019       6.158  44.377  53.493  1.00 22.30           O  
-HETATM 4373  O   HOH A1020       7.135  47.172  53.501  1.00 12.39           O  
-HETATM 4374  O   HOH A1021       6.186  48.582  55.706  1.00 22.89           O  
-HETATM 4375  O   HOH A1022       5.751  46.277  57.824  1.00 44.02           O  
-HETATM 4376  O   HOH A1023       7.303  48.885  58.887  1.00 10.58           O  
-HETATM 4377  O   HOH A1024       9.600  49.951  57.337  1.00 42.28           O  
-HETATM 4378  O   HOH A1025      12.748  51.463  58.911  1.00 34.13           O  
-HETATM 4379  O   HOH A1026      15.176  51.382  56.057  1.00 44.29           O  
-HETATM 4380  O   HOH A1027      12.993  50.057  53.833  1.00 42.98           O  
-HETATM 4381  O   HOH A1028      14.145  47.328  55.887  1.00 52.19           O  
-HETATM 4382  O   HOH A1029      17.042  49.094  56.475  1.00 55.53           O  
-HETATM 4383  O   HOH A1030      15.213  47.884  59.319  1.00 47.97           O  
-HETATM 4384  O   HOH A1031      15.059  46.982  62.610  1.00 40.52           O  
-HETATM 4385  O   HOH A1032      15.830  49.789  63.058  1.00 41.49           O  
-HETATM 4386  O   HOH A1033      15.632  53.017  61.398  1.00 22.04           O  
-HETATM 4387  O   HOH A1034       9.984  49.188  62.201  1.00 47.68           O  
-HETATM 4388  O   HOH A1035       8.128  46.117  62.262  1.00 44.30           O  
-HETATM 4389  O   HOH A1036       5.027  47.901  62.553  1.00 14.82           O  
-HETATM 4390  O   HOH A1037       4.763  50.631  61.929  1.00 10.89           O  
-HETATM 4391  O   HOH A1038       3.393  51.999  63.973  1.00 19.15           O  
-HETATM 4392  O   HOH A1039       2.941  54.488  62.986  1.00 13.26           O  
-HETATM 4393  O   HOH A1040      -1.621  57.675  62.119  1.00 14.33           O  
-HETATM 4394  O   HOH A1041      -3.982  57.468  63.495  1.00 12.72           O  
-HETATM 4395  O   HOH A1042      -2.413  57.607  66.124  1.00 18.87           O  
-HETATM 4396  O   HOH A1043      -6.630  61.847  64.799  1.00 18.75           O  
-HETATM 4397  O   HOH A1044      -8.660  61.082  63.100  1.00 30.68           O  
-HETATM 4398  O   HOH A1045      -9.127  58.366  64.096  1.00 15.55           O  
-HETATM 4399  O   HOH A1046      -9.511  62.476  59.050  1.00 17.12           O  
-HETATM 4400  O   HOH A1047     -12.171  63.431  58.685  1.00 14.70           O  
-HETATM 4401  O   HOH A1048     -13.228  62.668  56.249  1.00 34.55           O  
-HETATM 4402  O   HOH A1049     -14.822  60.308  56.639  1.00 18.20           O  
-HETATM 4403  O   HOH A1050     -13.364  58.101  55.957  1.00 14.16           O  
-HETATM 4404  O   HOH A1051      -9.867  52.436  54.274  1.00 24.52           O  
-HETATM 4405  O   HOH A1052      -4.174  52.152  55.832  1.00 18.94           O  
-HETATM 4406  O   HOH A1053      -3.622  50.797  60.068  1.00 32.02           O  
-HETATM 4407  O   HOH A1054      -6.310  49.789  60.937  1.00 25.01           O  
-HETATM 4408  O   HOH A1055      -5.621  45.359  57.018  1.00 32.31           O  
-HETATM 4409  O   HOH A1056      -6.383  46.662  50.653  1.00 44.52           O  
-HETATM 4410  O   HOH A1057      -9.079  45.234  50.321  1.00 28.49           O  
-HETATM 4411  O   HOH A1058      -6.402  50.710  48.677  1.00 43.92           O  
-HETATM 4412  O   HOH A1059     -13.706  51.504  49.045  1.00 24.51           O  
-HETATM 4413  O   HOH A1060     -16.679  48.989  45.678  1.00 57.13           O  
-HETATM 4414  O   HOH A1061     -20.159  51.851  51.434  1.00 50.76           O  
-HETATM 4415  O   HOH A1062     -23.084  51.907  56.847  1.00 45.63           O  
-HETATM 4416  O   HOH A1063     -20.057  59.623  58.761  1.00 26.50           O  
-HETATM 4417  O   HOH A1064     -21.691  59.416  62.105  1.00 51.50           O  
-HETATM 4418  O   HOH A1065     -17.480  64.206  66.823  1.00 44.67           O  
-HETATM 4419  O   HOH A1066     -21.362  60.107  72.496  1.00 61.87           O  
-HETATM 4420  O   HOH A1067     -18.888  53.113  72.285  1.00 66.63           O  
-HETATM 4421  O   HOH A1068      23.445  55.506  45.793  1.00 61.07           O  
-HETATM 4422  O   HOH A1069      15.239  33.728  67.879  1.00 55.45           O  
-HETATM 4423  O   HOH A1070      16.609  74.243  77.229  1.00 26.76           O  
-HETATM 4424  O   HOH A1071     -23.397  51.951  59.523  1.00 72.02           O  
-HETATM 4425  O   HOH A1072     -22.038  46.681  66.898  1.00 26.44           O  
-HETATM 4426  O   HOH A1073     -25.869  40.710  65.033  1.00 69.93           O  
-HETATM 4427  O   HOH A1074     -19.782  63.484  60.117  1.00 55.84           O  
-HETATM 4428  O   HOH A1075     -22.537  46.251  57.341  1.00 72.48           O  
-HETATM 4429  O   HOH A1076     -17.654  39.252  68.528  1.00 55.41           O  
-HETATM 4430  O   HOH A1077     -13.260  40.807  62.522  1.00 31.64           O  
-HETATM 4431  O   HOH A1078      -7.220  42.248  67.128  1.00 38.34           O  
-HETATM 4432  O   HOH A1079      -1.975  39.910  64.187  1.00 32.68           O  
-HETATM 4433  O   HOH A1080       0.637  41.870  63.507  1.00 24.51           O  
-HETATM 4434  O   HOH A1081       1.852  43.404  67.237  1.00 39.17           O  
-HETATM 4435  O   HOH A1082       3.854  44.886  65.645  1.00 31.48           O  
-HETATM 4436  O   HOH A1083       3.372  47.669  64.870  1.00 15.27           O  
-HETATM 4437  O   HOH A1084       3.390  46.083  60.938  1.00 21.80           O  
-HETATM 4438  O   HOH A1085       4.069  43.689  62.752  1.00 35.11           O  
-HETATM 4439  O   HOH A1086       0.741  40.697  56.917  1.00 39.54           O  
-HETATM 4440  O   HOH A1087      12.038  42.569  50.992  1.00 54.45           O  
-HETATM 4441  O   HOH A1088      14.878  42.502  47.885  1.00 53.47           O  
-HETATM 4442  O   HOH A1089      21.033  47.533  51.816  1.00 55.65           O  
-HETATM 4443  O   HOH A1090      21.551  52.215  53.374  1.00 27.03           O  
-HETATM 4444  O   HOH A1091      23.095  54.783  54.830  1.00 21.55           O  
-HETATM 4445  O   HOH A1092      26.167  54.356  52.959  1.00 33.28           O  
-HETATM 4446  O   HOH A1093      28.765  54.071  51.396  1.00 43.92           O  
-HETATM 4447  O   HOH A1094      31.428  55.388  47.920  1.00 39.93           O  
-HETATM 4448  O   HOH A1095      30.937  58.589  49.657  1.00 27.23           O  
-HETATM 4449  O   HOH A1096      25.250  61.958  52.287  1.00 11.67           O  
-HETATM 4450  O   HOH A1097      26.885  63.945  58.894  1.00 29.90           O  
-HETATM 4451  O   HOH A1098      25.290  66.320  59.701  1.00 27.08           O  
-HETATM 4452  O   HOH A1099      26.780  69.005  59.029  1.00 30.84           O  
-HETATM 4453  O   HOH A1100      29.466  67.566  60.536  1.00 48.28           O  
-HETATM 4454  O   HOH A1101      24.903  70.365  63.021  1.00 22.36           O  
-HETATM 4455  O   HOH A1102      25.392  72.667  64.833  1.00 35.59           O  
-HETATM 4456  O   HOH A1103      22.589  73.718  65.454  1.00 33.47           O  
-HETATM 4457  O   HOH A1104      21.106  71.717  68.031  1.00 29.89           O  
-HETATM 4458  O   HOH A1105      20.173  74.606  67.976  1.00 35.57           O  
-HETATM 4459  O   HOH A1106      19.296  75.528  70.729  1.00 47.99           O  
-HETATM 4460  O   HOH A1107      20.974  71.978  71.724  1.00 16.90           O  
-HETATM 4461  O   HOH A1108      21.443  69.302  70.333  1.00 42.49           O  
-HETATM 4462  O   HOH A1109      18.554  67.647  72.572  1.00 17.98           O  
-HETATM 4463  O   HOH A1110      22.423  72.290  75.348  1.00 41.83           O  
-HETATM 4464  O   HOH A1111      25.995  68.319  82.527  1.00 35.88           O  
-HETATM 4465  O   HOH A1112      21.355  63.904  85.658  1.00 30.98           O  
-HETATM 4466  O   HOH A1113      22.482  60.529  86.159  1.00 51.35           O  
-HETATM 4467  O   HOH A1114      18.714  62.513  88.852  1.00 52.36           O  
-HETATM 4468  O   HOH A1115      17.962  64.381  86.532  1.00 48.90           O  
-HETATM 4469  O   HOH A1116      15.613  63.019  84.314  1.00 39.45           O  
-HETATM 4470  O   HOH A1117      11.471  61.619  85.328  1.00 48.32           O  
-HETATM 4471  O   HOH A1118      15.388  58.924  87.468  1.00 49.59           O  
-HETATM 4472  O   HOH A1119      21.079  59.497  39.846  1.00 65.26           O  
-HETATM 4473  O   HOH A1120      17.448  49.883  77.747  1.00 66.94           O  
-HETATM 4474  O   HOH A1121      18.931  44.588  79.031  1.00 61.23           O  
-HETATM 4475  O   HOH A1122       8.991  50.257  77.674  1.00 50.87           O  
-HETATM 4476  O   HOH A1123      12.952  43.999  75.389  1.00 47.05           O  
-HETATM 4477  O   HOH A1124      11.581  46.372  74.046  1.00 39.88           O  
-HETATM 4478  O   HOH A1125       8.408  49.512  74.500  1.00 37.98           O  
-HETATM 4479  O   HOH A1126       5.329  47.295  75.160  1.00 32.35           O  
-HETATM 4480  O   HOH A1127      -1.455  47.083  73.684  1.00 36.27           O  
-HETATM 4481  O   HOH A1128      -3.767  46.424  71.768  1.00 31.11           O  
-HETATM 4482  O   HOH A1129      -6.900  48.865  73.475  1.00 35.55           O  
-HETATM 4483  O   HOH A1130     -21.513  60.871  47.213  1.00 73.26           O  
-HETATM 4484  O   HOH A1131      -9.269  50.072  77.298  1.00 38.90           O  
-HETATM 4485  O   HOH A1132     -11.368  52.165  76.921  1.00 32.13           O  
-HETATM 4486  O   HOH A1133      -9.911  55.432  76.240  1.00 26.26           O  
-HETATM 4487  O   HOH A1134      -6.637  56.912  73.161  1.00 23.59           O  
-HETATM 4488  O   HOH A1135      -7.343  60.850  71.606  1.00 25.55           O  
-HETATM 4489  O   HOH A1136     -10.310  66.004  68.451  1.00 26.32           O  
-HETATM 4490  O   HOH A1137     -11.350  72.445  65.721  1.00 33.59           O  
-HETATM 4491  O   HOH A1138      -7.486  73.378  67.206  1.00 33.52           O  
-HETATM 4492  O   HOH A1139      -5.927  75.182  69.283  1.00 29.76           O  
-HETATM 4493  O   HOH A1140      -5.850  77.121  66.170  1.00 40.94           O  
-HETATM 4494  O   HOH A1141      -3.360  76.293  63.892  1.00 30.08           O  
-HETATM 4495  O   HOH A1142      -2.313  78.278  62.134  1.00 32.37           O  
-HETATM 4496  O   HOH A1143       0.517  77.512  61.697  1.00 17.56           O  
-HETATM 4497  O   HOH A1144       1.920  83.227  61.207  1.00 39.77           O  
-HETATM 4498  O   HOH A1145       0.079  83.450  57.528  1.00 32.73           O  
-HETATM 4499  O   HOH A1146      -4.682  80.853  58.162  1.00 41.31           O  
-HETATM 4500  O   HOH A1147      -6.449  83.525  54.185  1.00 43.47           O  
-HETATM 4501  O   HOH A1148      -4.184  83.197  51.882  1.00 23.23           O  
-HETATM 4502  O   HOH A1149      -4.167  85.525  53.668  1.00 37.15           O  
-HETATM 4503  O   HOH A1150     -11.299  85.481  52.179  1.00 69.47           O  
-HETATM 4504  O   HOH A1151      -9.928  82.510  54.724  1.00 46.61           O  
-HETATM 4505  O   HOH A1152      -2.790  80.072  56.158  1.00 34.81           O  
-HETATM 4506  O   HOH A1153     -14.388  76.563  57.161  1.00 44.92           O  
-HETATM 4507  O   HOH A1154     -14.643  77.693  60.740  1.00 49.01           O  
-HETATM 4508  O   HOH A1155     -14.584  71.667  65.072  1.00 34.81           O  
-HETATM 4509  O   HOH A1156      -3.986  70.125  61.883  1.00 20.24           O  
-HETATM 4510  O   HOH A1157      -0.509  69.658  61.913  1.00 15.31           O  
-HETATM 4511  O   HOH A1158      -0.107  67.628  63.836  1.00 14.26           O  
-HETATM 4512  O   HOH A1159       1.917  66.004  64.819  1.00 23.99           O  
-HETATM 4513  O   HOH A1160       4.586  65.274  63.157  1.00 27.33           O  
-HETATM 4514  O   HOH A1161       4.378  63.858  60.785  1.00 15.65           O  
-HETATM 4515  O   HOH A1162      -0.549  63.456  58.517  1.00  7.43           O  
-HETATM 4516  O   HOH A1163       0.112  69.397  59.093  1.00 11.91           O  
-HETATM 4517  O   HOH A1164       3.925  69.208  57.411  1.00  6.85           O  
-HETATM 4518  O   HOH A1165      10.704  68.845  59.288  1.00 13.29           O  
-HETATM 4519  O   HOH A1166       7.881  75.762  60.590  1.00 18.95           O  
-HETATM 4520  O   HOH A1167      14.244  76.868  62.935  1.00 35.36           O  
-HETATM 4521  O   HOH A1168       9.992  80.204  64.902  1.00 34.65           O  
-HETATM 4522  O   HOH A1169       8.008  79.244  67.220  1.00 19.50           O  
-HETATM 4523  O   HOH A1170       5.926  82.489  67.802  1.00 63.52           O  
-HETATM 4524  O   HOH A1171       2.597  81.442  72.817  1.00 58.22           O  
-HETATM 4525  O   HOH A1172       4.172  75.648  82.378  1.00 86.67           O  
-HETATM 4526  O   HOH A1173       8.378  76.968  75.762  1.00 27.89           O  
-HETATM 4527  O   HOH A1174      10.882  77.053  77.935  1.00 35.39           O  
-HETATM 4528  O   HOH A1175      13.571  76.394  79.184  1.00 33.79           O  
-HETATM 4529  O   HOH A1176      14.703  77.666  76.694  1.00 30.97           O  
-HETATM 4530  O   HOH A1177      12.787  79.696  74.815  1.00 23.91           O  
-HETATM 4531  O   HOH A1178      12.283  83.677  71.933  1.00 42.96           O  
-HETATM 4532  O   HOH A1179      16.687  80.768  69.638  1.00 43.34           O  
-HETATM 4533  O   HOH A1180      -4.421  70.855  33.712  1.00 35.54           O  
-HETATM 4534  O   HOH A1181      19.822  84.559  62.390  1.00 33.70           O  
-HETATM 4535  O   HOH A1182      23.026  79.081  61.354  1.00 31.31           O  
-HETATM 4536  O   HOH A1183      24.535  77.037  63.241  1.00 38.33           O  
-HETATM 4537  O   HOH A1184      28.086  75.353  58.347  1.00 44.87           O  
-HETATM 4538  O   HOH A1185      23.943  77.690  54.056  1.00 33.16           O  
-HETATM 4539  O   HOH A1186      21.235  82.851  53.188  1.00 41.07           O  
-HETATM 4540  O   HOH A1187      21.431  84.465  55.756  1.00 28.85           O  
-HETATM 4541  O   HOH A1188      22.984  86.353  54.895  1.00 41.36           O  
-HETATM 4542  O   HOH A1189      18.901  85.408  49.921  1.00 21.38           O  
-HETATM 4543  O   HOH A1190      16.641  86.579  46.711  1.00 39.08           O  
-HETATM 4544  O   HOH A1191      13.495  86.378  46.657  1.00 22.95           O  
-HETATM 4545  O   HOH A1192      12.834  83.637  47.321  1.00 19.48           O  
-HETATM 4546  O   HOH A1193      11.838  86.885  43.838  1.00 44.41           O  
-HETATM 4547  O   HOH A1194      11.671  79.923  39.972  1.00 34.45           O  
-HETATM 4548  O   HOH A1195       8.885  80.620  36.937  1.00 28.03           O  
-HETATM 4549  O   HOH A1196       7.871  78.430  34.665  1.00 38.85           O  
-HETATM 4550  O   HOH A1197       7.193  75.960  33.273  1.00 33.66           O  
-HETATM 4551  O   HOH A1198      10.119  74.885  33.351  1.00 29.71           O  
-HETATM 4552  O   HOH A1199      11.497  70.994  33.581  1.00 35.33           O  
-HETATM 4553  O   HOH A1200      11.685  64.814  35.168  1.00 32.34           O  
-HETATM 4554  O   HOH A1201       9.533  62.202  35.350  1.00 30.34           O  
-HETATM 4555  O   HOH A1202       4.058  64.607  34.885  1.00 19.42           O  
-HETATM 4556  O   HOH A1203       3.821  67.198  36.172  1.00 15.88           O  
-HETATM 4557  O   HOH A1204      -0.010  66.637  36.285  1.00 24.99           O  
-HETATM 4558  O   HOH A1205      -0.670  66.674  39.581  1.00 17.93           O  
-HETATM 4559  O   HOH A1206       0.281  69.636  28.923  1.00 32.77           O  
-HETATM 4560  O   HOH A1207       0.421  72.563  28.939  1.00 63.78           O  
-HETATM 4561  O   HOH A1208      -2.342  71.660  29.037  1.00 37.47           O  
-HETATM 4562  O   HOH A1209      -0.592  75.476  30.836  1.00 43.92           O  
-HETATM 4563  O   HOH A1210       3.462  81.586  31.884  1.00 28.64           O  
-HETATM 4564  O   HOH A1211       2.125  87.039  37.044  1.00 27.46           O  
-HETATM 4565  O   HOH A1212      -3.929  85.636  39.361  1.00 20.31           O  
-HETATM 4566  O   HOH A1213      -6.114  84.211  38.347  1.00 41.84           O  
-HETATM 4567  O   HOH A1214      -4.911  88.369  34.521  1.00 39.60           O  
-HETATM 4568  O   HOH A1215      -1.636  92.581  38.406  1.00 50.75           O  
-HETATM 4569  O   HOH A1216      -2.087  95.857  42.861  1.00 48.16           O  
-HETATM 4570  O   HOH A1217      -5.921  95.400  44.619  1.00 61.53           O  
-HETATM 4571  O   HOH A1218      -6.284  88.882  42.117  1.00 38.56           O  
-HETATM 4572  O   HOH A1219       0.114  93.491  51.895  1.00 41.45           O  
-HETATM 4573  O   HOH A1220       1.555  89.996  53.898  1.00 22.20           O  
-HETATM 4574  O   HOH A1221     -11.395  65.893  34.582  1.00 61.77           O  
-HETATM 4575  O   HOH A1222       9.897  46.915  53.309  1.00 23.74           O  
-HETATM 4576  O   HOH A1223      11.817  91.387  56.559  1.00 59.09           O  
-HETATM 4577  O   HOH A1224      10.349  91.066  52.840  1.00 47.16           O  
-HETATM 4578  O   HOH A1225      16.697  88.869  51.773  1.00 33.27           O  
-HETATM 4579  O   HOH A1226      17.720  89.943  54.328  1.00 44.20           O  
-HETATM 4580  O   HOH A1227      10.247  88.711  60.043  1.00 40.12           O  
-HETATM 4581  O   HOH A1228      14.076  87.110  66.382  1.00 38.36           O  
-HETATM 4582  O   HOH A1229      13.097  86.717  69.506  1.00 39.23           O  
-HETATM 4583  O   HOH A1230      10.434  90.529  72.764  1.00 49.29           O  
-HETATM 4584  O   HOH A1231     -15.381  72.522  53.769  1.00 55.89           O  
-HETATM 4585  O   HOH A1232      -3.879  73.393  73.068  1.00 32.33           O  
-HETATM 4586  O   HOH A1233      -1.160  72.535  72.903  1.00 19.85           O  
-HETATM 4587  O   HOH A1234       0.379  70.207  68.013  1.00 18.94           O  
-HETATM 4588  O   HOH A1235      -1.053  68.614  66.349  1.00 14.63           O  
-HETATM 4589  O   HOH A1236      -0.910  66.034  67.504  1.00 24.89           O  
-HETATM 4590  O   HOH A1237       0.421  63.429  74.908  1.00 18.94           O  
-HETATM 4591  O   HOH A1238      -2.036  63.305  76.574  1.00 35.00           O  
-HETATM 4592  O   HOH A1239       2.438  64.553  76.518  1.00 34.17           O  
-HETATM 4593  O   HOH A1240       2.703  67.276  77.070  1.00 40.23           O  
-HETATM 4594  O   HOH A1241       5.667  67.235  78.223  1.00 39.17           O  
-HETATM 4595  O   HOH A1242       7.466  63.781  78.548  1.00 21.05           O  
-HETATM 4596  O   HOH A1243      13.310  59.591  78.649  1.00 40.83           O  
-HETATM 4597  O   HOH A1244      11.829  67.460  83.192  1.00 24.75           O  
-HETATM 4598  O   HOH A1245      16.806  69.310  84.273  1.00 41.96           O  
-HETATM 4599  O   HOH A1246      10.727  78.062  83.113  1.00 41.57           O  
-HETATM 4600  O   HOH A1247      -3.742  68.719  78.460  1.00 27.21           O  
-HETATM 4601  O   HOH A1248      -5.892  66.315  30.971  1.00 46.92           O  
-HETATM 4602  O   HOH A1249      -0.714  56.790  73.625  1.00 35.56           O  
-HETATM 4603  O   HOH A1250       1.860  53.823  73.645  1.00 46.21           O  
-HETATM 4604  O   HOH A1251       3.448  50.717  69.031  1.00 15.07           O  
-HETATM 4605  O   HOH A1252       7.961  49.450  65.908  1.00 36.09           O  
-HETATM 4606  O   HOH A1253      10.564  55.984  68.245  1.00 18.60           O  
-HETATM 4607  O   HOH A1254       5.745  60.322  70.632  0.50  8.76           O  
-HETATM 4608  O   HOH A1255       3.971  60.298  73.308  1.00 34.74           O  
-HETATM 4609  O   HOH A1256      24.662  57.922  54.959  1.00 37.91           O  
-HETATM 4610  O   HOH A1257      14.179  39.821  75.451  1.00 45.13           O  
-HETATM 4611  O   HOH A1258      25.568  44.356  77.161  1.00 46.42           O  
-HETATM 4612  O   HOH A1259      25.929  47.627  76.678  1.00 38.77           O  
-HETATM 4613  O   HOH A1260      23.717  51.451  80.322  1.00 43.38           O  
-HETATM 4614  O   HOH A1261      24.392  55.167  86.828  1.00 75.05           O  
-HETATM 4615  O   HOH A1262      30.127  59.464  84.680  1.00 68.94           O  
-HETATM 4616  O   HOH A1263      34.175  62.338  77.604  1.00 29.09           O  
-HETATM 4617  O   HOH A1264      25.396  60.846  68.088  1.00 52.38           O  
-HETATM 4618  O   HOH A1265      26.891  59.404  62.479  1.00 38.84           O  
-HETATM 4619  O   HOH A1266      30.622  52.810  63.440  1.00 34.08           O  
-HETATM 4620  O   HOH A1267      19.879  63.333  64.974  1.00 31.95           O  
-HETATM 4621  O   HOH A1268      21.741  65.321  63.380  1.00 33.14           O  
-HETATM 4622  O   HOH A1269      22.701  66.128  66.770  1.00 53.10           O  
-HETATM 4623  O   HOH A1270      17.307  64.057  66.138  1.00 16.85           O  
-HETATM 4624  O   HOH A1271      11.909  67.422  66.914  1.00 28.30           O  
-HETATM 4625  O   HOH A1272       7.328  52.685  56.162  1.00 17.11           O  
-HETATM 4626  O   HOH A1273      15.123  43.479  61.669  1.00 33.15           O  
-HETATM 4627  O   HOH A1274      19.797  48.226  44.964  1.00 57.15           O  
-HETATM 4628  O   HOH A1275      18.173  50.656  45.045  1.00 33.83           O  
-HETATM 4629  O   HOH A1276      25.005  59.168  52.048  1.00 37.63           O  
-HETATM 4630  O   HOH A1277      19.569  67.690  38.452  1.00 32.51           O  
-HETATM 4631  O   HOH A1278      28.233  57.906  41.162  1.00 40.24           O  
-HETATM 4632  O   HOH A1279      25.300  58.661  40.681  1.00 23.55           O  
-HETATM 4633  O   HOH A1280      22.145  62.315  41.341  1.00 16.63           O  
-HETATM 4634  O   HOH A1281      18.442  60.336  41.650  1.00 16.82           O  
-HETATM 4635  O   HOH A1282      21.562  58.084  37.344  1.00 49.79           O  
-HETATM 4636  O   HOH A1283      24.675  59.601  35.247  1.00 31.43           O  
-HETATM 4637  O   HOH A1284      25.634  63.037  35.083  1.00 42.26           O  
-HETATM 4638  O   HOH A1285      22.452  83.532  47.449  1.00 42.47           O  
-HETATM 4639  O   HOH A1286      19.331  65.518  36.511  1.00 30.21           O  
-HETATM 4640  O   HOH A1287      24.580  69.886  40.011  1.00 39.17           O  
-HETATM 4641  O   HOH A1288      24.228  73.702  38.174  1.00 41.36           O  
-HETATM 4642  O   HOH A1289      18.235  75.188  36.866  1.00 38.69           O  
-HETATM 4643  O   HOH A1290      22.538  78.407  43.467  1.00 67.28           O  
-HETATM 4644  O   HOH A1291      24.126  79.199  46.601  1.00 36.25           O  
-HETATM 4645  O   HOH A1292      18.277  80.285  45.953  1.00 21.21           O  
-HETATM 4646  O   HOH A1293      29.951  74.558  46.713  1.00 42.17           O  
-HETATM 4647  O   HOH A1294      32.536  69.794  46.338  1.00 49.28           O  
-HETATM 4648  O   HOH A1295      34.358  66.946  48.161  1.00 51.09           O  
-HETATM 4649  O   HOH A1296      34.898  65.514  45.344  1.00 42.87           O  
-HETATM 4650  O   HOH A1297      28.455  65.762  42.510  1.00 35.24           O  
-HETATM 4651  O   HOH A1298      27.795  63.467  45.302  1.00 38.60           O  
-HETATM 4652  O   HOH A1299      23.358  67.291  47.487  1.00 18.39           O  
-HETATM 4653  O   HOH A1300      33.303  68.876  55.845  1.00 64.13           O  
-HETATM 4654  O   HOH A1301      30.926  81.406  45.928  1.00 56.87           O  
-HETATM 4655  O   HOH A1302       7.121  92.572  47.862  1.00 41.76           O  
-HETATM 4656  O   HOH A1303      19.128  90.819  62.092  1.00 64.88           O  
-HETATM 4657  O   HOH A1304     -15.291  74.870  50.139  1.00 73.48           O  
-HETATM 4658  O   HOH A1305       4.228  80.834  51.025  1.00 18.06           O  
-HETATM 4659  O   HOH A1306      -1.870  75.771  52.236  1.00 42.04           O  
-HETATM 4660  O   HOH A1307      -1.355  69.802  52.104  1.00 21.49           O  
-HETATM 4661  O   HOH A1308      -8.059  71.559  52.095  1.00 27.04           O  
-HETATM 4662  O   HOH A1309      -7.093  70.539  55.942  1.00 21.20           O  
-HETATM 4663  O   HOH A1310      -7.027  68.039  57.284  1.00 23.10           O  
-HETATM 4664  O   HOH A1311     -19.042  72.623  50.918  1.00 58.74           O  
-HETATM 4665  O   HOH A1312     -15.153  67.649  48.733  1.00 32.40           O  
-HETATM 4666  O   HOH A1313     -17.981  68.722  48.423  1.00 28.57           O  
-HETATM 4667  O   HOH A1314     -20.395  69.414  50.328  1.00 38.32           O  
-HETATM 4668  O   HOH A1315     -25.307  71.523  40.803  1.00 59.00           O  
-HETATM 4669  O   HOH A1316     -21.889  69.027  42.307  1.00 38.24           O  
-HETATM 4670  O   HOH A1317     -22.376  74.858  43.754  1.00 37.17           O  
-HETATM 4671  O   HOH A1318     -23.276  77.592  43.397  1.00 32.56           O  
-HETATM 4672  O   HOH A1319     -23.966  80.374  41.830  1.00 45.10           O  
-HETATM 4673  O   HOH A1320     -22.049  82.580  47.917  1.00 57.75           O  
-HETATM 4674  O   HOH A1321     -18.692  77.943  49.672  1.00 41.54           O  
-HETATM 4675  O   HOH A1322     -20.181  76.890  47.048  1.00 35.75           O  
-HETATM 4676  O   HOH A1323     -19.483  82.303  54.801  1.00 42.61           O  
-HETATM 4677  O   HOH A1324     -20.047  75.365  37.075  1.00 23.26           O  
-HETATM 4678  O   HOH A1325     -22.185  70.933  35.120  1.00 35.12           O  
-HETATM 4679  O   HOH A1326     -18.851  71.513  33.897  1.00 41.48           O  
-HETATM 4680  O   HOH A1327     -17.136  66.993  33.248  1.00 54.97           O  
-HETATM 4681  O   HOH A1328     -11.841  62.852  34.752  1.00 32.26           O  
-HETATM 4682  O   HOH A1329      -9.186  65.223  32.085  1.00 37.25           O  
-HETATM 4683  O   HOH A1330     -11.905  67.554  36.963  1.00 21.16           O  
-HETATM 4684  O   HOH A1331     -12.434  64.964  41.141  1.00 38.32           O  
-HETATM 4685  O   HOH A1332     -15.988  66.272  36.330  1.00 53.61           O  
-HETATM 4686  O   HOH A1333     -18.724  60.476  41.955  1.00 42.11           O  
-HETATM 4687  O   HOH A1334      19.133  79.331  43.229  1.00 32.82           O  
-HETATM 4688  O   HOH A1335     -21.367  62.556  49.834  1.00 52.45           O  
-HETATM 4689  O   HOH A1336     -15.329  60.143  48.448  1.00 29.54           O  
-HETATM 4690  O   HOH A1337     -16.861  44.648  54.045  1.00 41.24           O  
-HETATM 4691  O   HOH A1338      16.568  58.011  35.578  1.00 20.92           O  
-HETATM 4692  O   HOH A1339      15.974  59.478  32.177  1.00 28.90           O  
-HETATM 4693  O   HOH A1340      17.005  57.671  30.061  1.00 34.13           O  
-HETATM 4694  O   HOH A1341      19.499  58.777  34.774  1.00 36.93           O  
-HETATM 4695  O   HOH A1342       4.806  46.885  40.007  1.00 57.03           O  
-HETATM 4696  O   HOH A1343      24.210  59.331  24.207  1.00 51.19           O  
-HETATM 4697  O   HOH A1344      18.733  54.536  35.794  1.00 49.49           O  
-HETATM 4698  O   HOH A1345     -12.883  77.174  29.784  1.00 49.55           O  
-HETATM 4699  O   HOH A1346     -20.212  83.521  34.946  1.00 57.43           O  
-HETATM 4700  O   HOH A1347      -0.387  65.114  72.733  1.00 27.39           O  
-HETATM 4701  O   HOH A1348      -3.396  66.636  73.732  1.00 24.29           O  
-HETATM 4702  O   HOH A1349      -3.774  69.349  29.958  1.00 35.37           O  
-HETATM 4703  O   HOH A1350      -0.338  66.240  70.224  1.00 31.18           O  
-HETATM 4704  O   HOH A1351      -3.918  68.281  65.647  1.00 45.47           O  
-HETATM 4705  O   HOH A1352     -14.738  77.423  52.103  1.00 72.19           O  
-HETATM 4706  O   HOH A1353      -9.499  70.354  54.174  1.00 44.27           O  
-HETATM 4707  O   HOH A1354       4.995  79.126  67.364  1.00 32.09           O  
-HETATM 4708  O   HOH A1355     -17.800  65.476  60.805  1.00 40.71           O  
-HETATM 4709  O   HOH A1356     -15.013  66.462  51.445  1.00 24.71           O  
-HETATM 4710  O   HOH A1357      -7.475  58.060  44.276  1.00 38.77           O  
-HETATM 4711  O   HOH A1358       7.305  70.747  38.797  1.00 37.15           O  
-HETATM 4712  O   HOH A1359      13.693  69.111  56.731  1.00 21.91           O  
-HETATM 4713  O   HOH A1360      -4.561  40.420  62.480  1.00 38.51           O  
-HETATM 4714  O   HOH A1361      -5.707  40.557  56.620  1.00 50.92           O  
-HETATM 4715  O   HOH A1362     -12.602  37.962  61.908  1.00 60.65           O  
-HETATM 4716  O   HOH A1363     -24.108  55.808  58.443  1.00 67.97           O  
-HETATM 4717  O   HOH A1364     -22.319  46.055  63.957  1.00 41.05           O  
-HETATM 4718  O   HOH A1365     -14.635  66.109  66.910  1.00 38.18           O  
-HETATM 4719  O   HOH A1366     -15.102  58.375  72.812  1.00 58.93           O  
-HETATM 4720  O   HOH A1367       6.588  62.801  34.760  1.00 32.64           O  
-HETATM 4721  O   HOH A1368      19.525  65.817  68.295  1.00 34.03           O  
-HETATM 4722  O   HOH A1369      21.074  78.808  64.752  1.00 29.92           O  
-HETATM 4723  O   HOH A1370      11.886  56.166  83.950  1.00 48.33           O  
-HETATM 4724  O   HOH A1371       9.913  44.355  70.941  1.00 48.76           O  
-HETATM 4725  O   HOH A1372      18.273  39.461  74.436  1.00 39.44           O  
-HETATM 4726  O   HOH A1373      30.606  57.189  71.843  1.00 34.49           O  
-HETATM 4727  O   HOH A1374      23.807  66.504  85.286  1.00 72.32           O  
-HETATM 4728  O   HOH A1375      12.537  59.829  57.012  1.00 44.41           O  
-HETATM 4729  O   HOH A1376      30.611  78.054  56.326  1.00 43.57           O  
-HETATM 4730  O   HOH A1377      26.713  76.156  55.880  1.00 68.81           O  
-HETATM 4731  O   HOH A1378       1.196  64.441  34.644  1.00 45.02           O  
-HETATM 4732  O   HOH A1379      18.038  84.175  47.522  0.50 33.19           O  
-HETATM 4733  O   HOH A1380      17.994  32.398  66.671  1.00 12.19           O  
-HETATM 4734  O   HOH A1381      30.173  52.236  68.423  0.50  5.46           O  
-HETATM 4735  O   HOH A1382      27.746  48.125  68.453  0.50  3.81           O  
-HETATM 4736  O   HOH A1383      -9.898  56.333  44.700  1.00 41.43           O  
-HETATM 4737  O   HOH A1384      -8.033  53.049  44.344  1.00 47.74           O  
-HETATM 4738  O   HOH A1385      -5.728  59.145  39.706  1.00 40.32           O  
-HETATM 4739  O   HOH A1386      -7.855  59.586  41.701  1.00 52.48           O  
-HETATM 4740  O   HOH A1387      -9.160  62.196  35.073  1.00 68.69           O  
-HETATM 4741  O   HOH A1388       5.947  57.755  35.404  1.00 52.11           O  
-HETATM 4742  O   HOH A1389      13.109  52.418  34.238  1.00 63.31           O  
-HETATM 4743  O   HOH A1390     -20.105  56.795  58.898  1.00 41.45           O  
-HETATM 4744  O   HOH A1391     -24.457  57.803  53.771  1.00 68.42           O  
-HETATM 4745  O   HOH A1392      10.318  52.680  78.999  1.00 43.79           O  
-HETATM 4746  O   HOH A1393      -8.189  65.546  70.889  1.00 63.68           O  
-HETATM 4747  O   HOH A1394      14.052  80.936  71.171  1.00 52.30           O  
-HETATM 4748  O   HOH A1395      -3.091  67.355  31.798  1.00 61.19           O  
-HETATM 4749  O   HOH A1396      19.167  82.958  65.119  1.00 66.78           O  
-CONECT  447 4256                                                                
-CONECT  506  729                                                                
-CONECT  729  506                                                                
-CONECT 1954 2042                                                                
-CONECT 2042 1954                                                                
-CONECT 3128 4134                                                                
-CONECT 3247 4270                                                                
-CONECT 3595 4312                                                                
-CONECT 4134 3128                                                                
-CONECT 4242 4298                                                                
-CONECT 4256  447 4257 4267                                                      
-CONECT 4257 4256 4258 4264                                                      
-CONECT 4258 4257 4259 4265                                                      
-CONECT 4259 4258 4260 4266                                                      
-CONECT 4260 4259 4261 4267                                                      
-CONECT 4261 4260 4268                                                           
-CONECT 4262 4263 4264 4269                                                      
-CONECT 4263 4262                                                                
-CONECT 4264 4257 4262                                                           
-CONECT 4265 4258                                                                
-CONECT 4266 4259                                                                
-CONECT 4267 4256 4260                                                           
-CONECT 4268 4261                                                                
-CONECT 4269 4262                                                                
-CONECT 4270 3247 4271 4281                                                      
-CONECT 4271 4270 4272 4278                                                      
-CONECT 4272 4271 4273 4279                                                      
-CONECT 4273 4272 4274 4280                                                      
-CONECT 4274 4273 4275 4281                                                      
-CONECT 4275 4274 4282                                                           
-CONECT 4276 4277 4278 4283                                                      
-CONECT 4277 4276                                                                
-CONECT 4278 4271 4276                                                           
-CONECT 4279 4272                                                                
-CONECT 4280 4273 4284                                                           
-CONECT 4281 4270 4274                                                           
-CONECT 4282 4275                                                                
-CONECT 4283 4276                                                                
-CONECT 4284 4280 4285 4295                                                      
-CONECT 4285 4284 4286 4292                                                      
-CONECT 4286 4285 4287 4293                                                      
-CONECT 4287 4286 4288 4294                                                      
-CONECT 4288 4287 4289 4295                                                      
-CONECT 4289 4288 4296                                                           
-CONECT 4290 4291 4292 4297                                                      
-CONECT 4291 4290                                                                
-CONECT 4292 4285 4290                                                           
-CONECT 4293 4286                                                                
-CONECT 4294 4287                                                                
-CONECT 4295 4284 4288                                                           
-CONECT 4296 4289                                                                
-CONECT 4297 4290                                                                
-CONECT 4298 4242 4299 4309                                                      
-CONECT 4299 4298 4300 4306                                                      
-CONECT 4300 4299 4301 4307                                                      
-CONECT 4301 4300 4302 4308                                                      
-CONECT 4302 4301 4303 4309                                                      
-CONECT 4303 4302 4310                                                           
-CONECT 4304 4305 4306 4311                                                      
-CONECT 4305 4304                                                                
-CONECT 4306 4299 4304                                                           
-CONECT 4307 4300                                                                
-CONECT 4308 4301                                                                
-CONECT 4309 4298 4302                                                           
-CONECT 4310 4303                                                                
-CONECT 4311 4304                                                                
-CONECT 4312 3595 4313 4323                                                      
-CONECT 4313 4312 4314 4320                                                      
-CONECT 4314 4313 4315 4321                                                      
-CONECT 4315 4314 4316 4322                                                      
-CONECT 4316 4315 4317 4323                                                      
-CONECT 4317 4316 4324                                                           
-CONECT 4318 4319 4320 4325                                                      
-CONECT 4319 4318                                                                
-CONECT 4320 4313 4318                                                           
-CONECT 4321 4314                                                                
-CONECT 4322 4315                                                                
-CONECT 4323 4312 4316                                                           
-CONECT 4324 4317                                                                
-CONECT 4325 4318                                                                
-CONECT 4326 4327 4331 4350                                                      
-CONECT 4327 4326 4328 4352                                                      
-CONECT 4328 4327 4329                                                           
-CONECT 4329 4328 4330 4334                                                      
-CONECT 4330 4329 4331 4332                                                      
-CONECT 4331 4326 4330                                                           
-CONECT 4332 4330 4333 4349                                                      
-CONECT 4333 4332 4334 4335                                                      
-CONECT 4334 4329 4333                                                           
-CONECT 4335 4333 4336                                                           
-CONECT 4336 4335 4337 4341                                                      
-CONECT 4337 4336 4338                                                           
-CONECT 4338 4337 4339                                                           
-CONECT 4339 4338 4340 4342                                                      
-CONECT 4340 4339 4341                                                           
-CONECT 4341 4336 4340                                                           
-CONECT 4342 4339 4343                                                           
-CONECT 4343 4342 4344 4348                                                      
-CONECT 4344 4343 4345                                                           
-CONECT 4345 4344 4346                                                           
-CONECT 4346 4345 4347                                                           
-CONECT 4347 4346 4348                                                           
-CONECT 4348 4343 4347                                                           
-CONECT 4349 4332                                                                
-CONECT 4350 4326 4351                                                           
-CONECT 4351 4350                                                                
-CONECT 4352 4327 4353                                                           
-CONECT 4353 4352                                                                
-MASTER      361    0    6   24   14    0   12    6 4748    1  108   42          
-END                                                                             
diff --git a/plip/test/pdb/1h2t.pdb b/plip/test/pdb/1h2t.pdb
deleted file mode 100644
index 42eaaf6..0000000
--- a/plip/test/pdb/1h2t.pdb
+++ /dev/null
@@ -1,7978 +0,0 @@
-HEADER    NUCLEAR PROTEIN                         16-AUG-02   1H2T              
-TITLE     STRUCTURE OF THE HUMAN NUCLEAR CAP-BINDING-COMPLEX (CBC) IN           
-TITLE    2 COMPLEX WITH A CAP ANALOGUE M7GPPPG                                  
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: 80 KDA NUCLEAR CAP BINDING PROTEIN;                        
-COMPND   3 CHAIN: C;                                                            
-COMPND   4 FRAGMENT: MIF4G DOMAIN, RESIDUES 20-653,701-790;                     
-COMPND   5 SYNONYM: NCBP 80 KDA SUBUNIT, CBP80;                                 
-COMPND   6 ENGINEERED: YES;                                                     
-COMPND   7 MUTATION: YES;                                                       
-COMPND   8 OTHER_DETAILS: DELETION OF THE FIRST 19 RESIDUES IN                  
-COMPND   9  N-TERMINAL AND DELETION OF RESIDUES 653-701 REPLACED BY A           
-COMPND  10  GLYCINE, ENGINEERED MUTATION ALA 479 SER;                           
-COMPND  11 MOL_ID: 2;                                                           
-COMPND  12 MOLECULE: 20 KDA NUCLEAR CAP BINDING PROTEIN;                        
-COMPND  13 CHAIN: Z;                                                            
-COMPND  14 SYNONYM: CBP20, NCBP 20 KDA SUBUNIT, NCBP INTERACTING                
-COMPND  15  PROTEIN 1, NIP1;                                                    
-COMPND  16 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7111;                                       
-SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
-SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
-SOURCE   9 MOL_ID: 2;                                                           
-SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
-SOURCE  12 ORGANISM_TAXID: 9606;                                                
-SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE  14 EXPRESSION_SYSTEM_TAXID: 511693;                                     
-SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
-SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PRSETA                                    
-KEYWDS    M7GCAP, CAP-BINDING-COMPLEX, RNP DOMAIN, MIF4G DOMAIN, RNA            
-KEYWDS   2 MATURATION, RNA EXPORT, NUCLEAR PROTEIN, RNA-BINDING                 
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    C.MAZZA,A.SEGREF,I.W.MATTAJ,S.CUSACK                                  
-REVDAT   3   24-FEB-09 1H2T    1       VERSN                                    
-REVDAT   2   05-DEC-02 1H2T    1       REMARK                                   
-REVDAT   1   17-OCT-02 1H2T    0                                                
-JRNL        AUTH   C.MAZZA,A.SEGREF,I.W.MATTAJ,S.CUSACK                         
-JRNL        TITL   LARGE-SCALE INDUCED FIT RECOGNITION OF AN                    
-JRNL        TITL 2 M(7)GPPPG CAP ANALOGUE BY THE HUMAN NUCLEAR                  
-JRNL        TITL 3 CAP-BINDING COMPLEX                                          
-JRNL        REF    EMBO J.                       V.  21  5548 2002              
-JRNL        REFN                   ISSN 0261-4189                               
-JRNL        PMID   12374755                                                     
-JRNL        DOI    10.1093/EMBOJ/CDF538                                         
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   C.MAZZA,A.SEGREF,I.MATTAJ,S.CUSACK                           
-REMARK   1  TITL   CO-CRYSTALLIZATION OF THE HUMAN NUCLEAR                      
-REMARK   1  TITL 2 CAP-BINDING COMPLEX WITH A M7GPPPG CAP ANALOGUE              
-REMARK   1  TITL 3 USING PROTEIN ENGINEERING                                    
-REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  58  2194 2002              
-REMARK   1  REFN                   ISSN 0907-4449                               
-REMARK   1  PMID   12454499                                                     
-REMARK   1  DOI    10.1107/S0907444902015445                                    
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS 1.0                                              
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : NULL                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.76                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2842357.86                     
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.000000                       
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
-REMARK   3   NUMBER OF REFLECTIONS             : 68137                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.232                           
-REMARK   3   FREE R VALUE                     : 0.269                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
-REMARK   3   FREE R VALUE TEST SET COUNT      : 3419                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.1                         
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10454                        
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.310                        
-REMARK   3   BIN FREE R VALUE                    : 0.344                        
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.2                          
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 577                          
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 6939                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 52                                      
-REMARK   3   SOLVENT ATOMS            : 365                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 30.7                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.5                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -3.75                                                
-REMARK   3    B22 (A**2) : -3.75                                                
-REMARK   3    B33 (A**2) : 7.51                                                 
-REMARK   3    B12 (A**2) : -0.27                                                
-REMARK   3    B13 (A**2) : 0.00                                                 
-REMARK   3    B23 (A**2) : 0.00                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.29                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.35                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.33                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.006                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.1                             
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.4                            
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.11  ; 1.50                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.27  ; 2.00                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.40  ; 3.00                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.57  ; 4.00                 
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : FLAT MODEL                                           
-REMARK   3   KSOL        : 0.361995                                             
-REMARK   3   BSOL        : 55.6133                                              
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
-REMARK   3  PARAMETER FILE  2  : DNA-RNA-MULTI-ENDO.PARAM                       
-REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
-REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
-REMARK   3  PARAMETER FILE  5  : ATP_GTP.PAR                                    
-REMARK   3  PARAMETER FILE  6  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
-REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
-REMARK   3  TOPOLOGY FILE  3   : DNA-RNA-MULTI-ENDO.TOP                         
-REMARK   3  TOPOLOGY FILE  4   : WATER.TOP                                      
-REMARK   3  TOPOLOGY FILE  5   : ATP_GTP.TOP                                    
-REMARK   3  TOPOLOGY FILE  6   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 20 - 28 AND 528 - 537 FROM       
-REMARK   3  CHAIN C ARE DISORDERED. RESIDUES 1 - 5 AND 151 - 156 FROM           
-REMARK   3  CHAIN Z ARE DISORDERED.                                             
-REMARK   4                                                                      
-REMARK   4 1H2T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-AUG-02.                  
-REMARK 100 THE PDBE ID CODE IS EBI-11235.                                       
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-01                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
-REMARK 200  PH                             : 6.00                               
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ESRF                               
-REMARK 200  BEAMLINE                       : ID14-4                             
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393                             
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : ADSC                               
-REMARK 200  DETECTOR MANUFACTURER          : NULL                               
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
-REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63766                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
-REMARK 200  DATA REDUNDANCY                : 7.000                              
-REMARK 200  R MERGE                    (I) : 0.07900                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.39800                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: MOLREP                                                
-REMARK 200 STARTING MODEL: PDB ENTRY 1H6K                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS  (%): 57.4                                       
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9                      
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 TO 1 % PEG 4000,                    
-REMARK 280  100 MM MES PH6, 75 TO 100 MM MAGNESIUM FORMATE                      
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -Y,X-Y,Z+1/3                                            
-REMARK 290       3555   -X+Y,-X,Z+2/3                                           
-REMARK 290       4555   Y,X,-Z                                                  
-REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
-REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.77000            
-REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      105.54000            
-REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      105.54000            
-REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       52.77000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 300                                                                      
-REMARK 300 DETAILS:THE COMPLEX IS A HETERODIMER FORMED BY                       
-REMARK 300 CHAINS CAND Z.                                                       
-REMARK 350                                                                      
-REMARK 350 GENERATING THE BIOMOLECULE                                           
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE:  1                                                      
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PQS                                                   
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, Z                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 400                                                                      
-REMARK 400 COMPOUND                                                             
-REMARK 400  THE CAP-BINDING PROTEIN (CBC) COMPLEX IS AN HETERODIMER             
-REMARK 400  OF CBP80 AND CBP20.                                                 
-REMARK 400                                                                      
-REMARK 400  CHAIN C ENGINEERED DELETION OF THE FIRST 19 RESIDUES IN N-TERMINAL  
-REMARK 400  AND DELETION OF RESIDUES 653-701 REPLACED BY A GLYCINE              
-REMARK 400                                                                      
-REMARK 400  ENGINEERED MUTATION ALA 479 SER                                     
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     LYS C    20                                                      
-REMARK 465     THR C    21                                                      
-REMARK 465     SER C    22                                                      
-REMARK 465     ASP C    23                                                      
-REMARK 465     ALA C    24                                                      
-REMARK 465     ASN C    25                                                      
-REMARK 465     GLU C    26                                                      
-REMARK 465     THR C    27                                                      
-REMARK 465     GLU C    28                                                      
-REMARK 465     ASN C   528                                                      
-REMARK 465     GLN C   529                                                      
-REMARK 465     ASP C   530                                                      
-REMARK 465     ASP C   531                                                      
-REMARK 465     ASP C   532                                                      
-REMARK 465     ASP C   533                                                      
-REMARK 465     ASP C   534                                                      
-REMARK 465     GLU C   535                                                      
-REMARK 465     GLY C   536                                                      
-REMARK 465     PHE C   537                                                      
-REMARK 465     MET Z     1                                                      
-REMARK 465     SER Z     2                                                      
-REMARK 465     GLY Z     3                                                      
-REMARK 465     GLY Z     4                                                      
-REMARK 465     LYS Z   151                                                      
-REMARK 465     LEU Z   152                                                      
-REMARK 465     ALA Z   153                                                      
-REMARK 465     GLN Z   154                                                      
-REMARK 465     ASN Z   155                                                      
-REMARK 465     GLN Z   156                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     PRO C 527    O                                                   
-REMARK 470     GLY Z 150    O                                                   
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    TYR C  64       35.77   -141.75                                   
-REMARK 500    ASN C 120       57.99    -96.82                                   
-REMARK 500    LYS C 188       43.16   -142.31                                   
-REMARK 500    SER C 386      -38.32   -142.18                                   
-REMARK 500    SER C 460     -110.50   -148.35                                   
-REMARK 500    THR C 472        0.50    -69.06                                   
-REMARK 500    PRO C 481       66.30    -67.42                                   
-REMARK 500    SER C 491     -177.39    -58.06                                   
-REMARK 500    SER C 494       53.34    -94.88                                   
-REMARK 500    LYS C 511       85.14     52.17                                   
-REMARK 500    ASP C 523       33.32    -71.88                                   
-REMARK 500    ALA C 555       13.22   -146.93                                   
-REMARK 500    ALA C 556       10.40    -64.47                                   
-REMARK 500    LYS C 557      -70.85    -74.60                                   
-REMARK 500    PHE C 569       44.57    -93.60                                   
-REMARK 500    ASP Z  12       57.44   -147.64                                   
-REMARK 500    ASP Z 141      173.34    -59.31                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP Z1151                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7MG Z1152                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 1H6K   RELATED DB: PDB                                   
-REMARK 900  NUCLEAR CAP BINDING COMPLEX                                         
-REMARK 900 RELATED ID: 1H2U   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE HUMAN NUCLEAR CAP-BINDING-                         
-REMARK 900  COMPLEX (CBC) IN COMPLEX WIHT A CAP                                 
-REMARK 900  ANALOGUE M7GPPPG                                                    
-REMARK 900 RELATED ID: 1H2V   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE HUMAN NUCLEAR CAP-BINDING-                         
-REMARK 900  COMPLEX (CBC)                                                       
-REMARK 999                                                                      
-REMARK 999 SEQUENCE                                                             
-REMARK 999  DELETION OF THE FIRST 19 RESIDUES IN N-TERMINAL AND DELETION OF     
-REMARK 999  RESIDUES 653-701 REPLACED BY A GLYCINE FOR CHAIN C                  
-DBREF  1H2T C   20   652  UNP    Q09161   CB80_HUMAN      20    652             
-DBREF  1H2T C  653   653  PDB    1H2T     1H2T           653    653             
-DBREF  1H2T C  702   790  UNP    Q09161   CB80_HUMAN     702    790             
-DBREF  1H2T Z    1   156  UNP    P52298   CB20_HUMAN       1    156             
-SEQADV 1H2T SER C  479  UNP  Q09161    ALA   479 ENGINEERED MUTATION            
-SEQRES   1 C  723  LYS THR SER ASP ALA ASN GLU THR GLU ASP HIS LEU GLU          
-SEQRES   2 C  723  SER LEU ILE CYS LYS VAL GLY GLU LYS SER ALA CYS SER          
-SEQRES   3 C  723  LEU GLU SER ASN LEU GLU GLY LEU ALA GLY VAL LEU GLU          
-SEQRES   4 C  723  ALA ASP LEU PRO ASN TYR LYS SER LYS ILE LEU ARG LEU          
-SEQRES   5 C  723  LEU CYS THR VAL ALA ARG LEU LEU PRO GLU LYS LEU THR          
-SEQRES   6 C  723  ILE TYR THR THR LEU VAL GLY LEU LEU ASN ALA ARG ASN          
-SEQRES   7 C  723  TYR ASN PHE GLY GLY GLU PHE VAL GLU ALA MET ILE ARG          
-SEQRES   8 C  723  GLN LEU LYS GLU SER LEU LYS ALA ASN ASN TYR ASN GLU          
-SEQRES   9 C  723  ALA VAL TYR LEU VAL ARG PHE LEU SER ASP LEU VAL ASN          
-SEQRES  10 C  723  CYS HIS VAL ILE ALA ALA PRO SER MET VAL ALA MET PHE          
-SEQRES  11 C  723  GLU ASN PHE VAL SER VAL THR GLN GLU GLU ASP VAL PRO          
-SEQRES  12 C  723  GLN VAL ARG ARG ASP TRP TYR VAL TYR ALA PHE LEU SER          
-SEQRES  13 C  723  SER LEU PRO TRP VAL GLY LYS GLU LEU TYR GLU LYS LYS          
-SEQRES  14 C  723  ASP ALA GLU MET ASP ARG ILE PHE ALA ASN THR GLU SER          
-SEQRES  15 C  723  TYR LEU LYS ARG ARG GLN LYS THR HIS VAL PRO MET LEU          
-SEQRES  16 C  723  GLN VAL TRP THR ALA ASP LYS PRO HIS PRO GLN GLU GLU          
-SEQRES  17 C  723  TYR LEU ASP CYS LEU TRP ALA GLN ILE GLN LYS LEU LYS          
-SEQRES  18 C  723  LYS ASP ARG TRP GLN GLU ARG HIS ILE LEU ARG PRO TYR          
-SEQRES  19 C  723  LEU ALA PHE ASP SER ILE LEU CYS GLU ALA LEU GLN HIS          
-SEQRES  20 C  723  ASN LEU PRO PRO PHE THR PRO PRO PRO HIS THR GLU ASP          
-SEQRES  21 C  723  SER VAL TYR PRO MET PRO ARG VAL ILE PHE ARG MET PHE          
-SEQRES  22 C  723  ASP TYR THR ASP ASP PRO GLU GLY PRO VAL MET PRO GLY          
-SEQRES  23 C  723  SER HIS SER VAL GLU ARG PHE VAL ILE GLU GLU ASN LEU          
-SEQRES  24 C  723  HIS CYS ILE ILE LYS SER HIS TRP LYS GLU ARG LYS THR          
-SEQRES  25 C  723  CYS ALA ALA GLN LEU VAL SER TYR PRO GLY LYS ASN LYS          
-SEQRES  26 C  723  ILE PRO LEU ASN TYR HIS ILE VAL GLU VAL ILE PHE ALA          
-SEQRES  27 C  723  GLU LEU PHE GLN LEU PRO ALA PRO PRO HIS ILE ASP VAL          
-SEQRES  28 C  723  MET TYR THR THR LEU LEU ILE GLU LEU CYS LYS LEU GLN          
-SEQRES  29 C  723  PRO GLY SER LEU PRO GLN VAL LEU ALA GLN ALA THR GLU          
-SEQRES  30 C  723  MET LEU TYR MET ARG LEU ASP THR MET ASN THR THR CYS          
-SEQRES  31 C  723  VAL ASP ARG PHE ILE ASN TRP PHE SER HIS HIS LEU SER          
-SEQRES  32 C  723  ASN PHE GLN PHE ARG TRP SER TRP GLU ASP TRP SER ASP          
-SEQRES  33 C  723  CYS LEU SER GLN ASP PRO GLU SER PRO LYS PRO LYS PHE          
-SEQRES  34 C  723  VAL ARG GLU VAL LEU GLU LYS CYS MET ARG LEU SER TYR          
-SEQRES  35 C  723  HIS GLN ARG ILE LEU ASP ILE VAL PRO PRO THR PHE SER          
-SEQRES  36 C  723  ALA LEU CYS PRO SER ASN PRO THR CYS ILE TYR LYS TYR          
-SEQRES  37 C  723  GLY ASP GLU SER SER ASN SER LEU PRO GLY HIS SER VAL          
-SEQRES  38 C  723  ALA LEU CYS LEU ALA VAL ALA PHE LYS SER LYS ALA THR          
-SEQRES  39 C  723  ASN ASP GLU ILE PHE SER ILE LEU LYS ASP VAL PRO ASN          
-SEQRES  40 C  723  PRO ASN GLN ASP ASP ASP ASP ASP GLU GLY PHE SER PHE          
-SEQRES  41 C  723  ASN PRO LEU LYS ILE GLU VAL PHE VAL GLN THR LEU LEU          
-SEQRES  42 C  723  HIS LEU ALA ALA LYS SER PHE SER HIS SER PHE SER ALA          
-SEQRES  43 C  723  LEU ALA LYS PHE HIS GLU VAL PHE LYS THR LEU ALA GLU          
-SEQRES  44 C  723  SER ASP GLU GLY LYS LEU HIS VAL LEU ARG VAL MET PHE          
-SEQRES  45 C  723  GLU VAL TRP ARG ASN HIS PRO GLN MET ILE ALA VAL LEU          
-SEQRES  46 C  723  VAL ASP LYS MET ILE ARG THR GLN ILE VAL ASP CYS ALA          
-SEQRES  47 C  723  ALA VAL ALA ASN TRP ILE PHE SER SER GLU LEU SER ARG          
-SEQRES  48 C  723  ASP PHE THR ARG LEU PHE VAL TRP GLU ILE LEU HIS SER          
-SEQRES  49 C  723  THR ILE ARG LYS MET ASN LYS HIS VAL GLY ALA GLN SER          
-SEQRES  50 C  723  GLU GLN LYS ASN LEU PHE LEU VAL ILE PHE GLN ARG PHE          
-SEQRES  51 C  723  ILE MET ILE LEU THR GLU HIS LEU VAL ARG CYS GLU THR          
-SEQRES  52 C  723  ASP GLY THR SER VAL LEU THR PRO TRP TYR LYS ASN CYS          
-SEQRES  53 C  723  ILE GLU ARG LEU GLN GLN ILE PHE LEU GLN HIS HIS GLN          
-SEQRES  54 C  723  ILE ILE GLN GLN TYR MET VAL THR LEU GLU ASN LEU LEU          
-SEQRES  55 C  723  PHE THR ALA GLU LEU ASP PRO HIS ILE LEU ALA VAL PHE          
-SEQRES  56 C  723  GLN GLN PHE CYS ALA LEU GLN ALA                              
-SEQRES   1 Z  156  MET SER GLY GLY LEU LEU LYS ALA LEU ARG SER ASP SER          
-SEQRES   2 Z  156  TYR VAL GLU LEU SER GLN TYR ARG ASP GLN HIS PHE ARG          
-SEQRES   3 Z  156  GLY ASP ASN GLU GLU GLN GLU LYS LEU LEU LYS LYS SER          
-SEQRES   4 Z  156  CYS THR LEU TYR VAL GLY ASN LEU SER PHE TYR THR THR          
-SEQRES   5 Z  156  GLU GLU GLN ILE TYR GLU LEU PHE SER LYS SER GLY ASP          
-SEQRES   6 Z  156  ILE LYS LYS ILE ILE MET GLY LEU ASP LYS MET LYS LYS          
-SEQRES   7 Z  156  THR ALA CYS GLY PHE CYS PHE VAL GLU TYR TYR SER ARG          
-SEQRES   8 Z  156  ALA ASP ALA GLU ASN ALA MET ARG TYR ILE ASN GLY THR          
-SEQRES   9 Z  156  ARG LEU ASP ASP ARG ILE ILE ARG THR ASP TRP ASP ALA          
-SEQRES  10 Z  156  GLY PHE LYS GLU GLY ARG GLN TYR GLY ARG GLY ARG SER          
-SEQRES  11 Z  156  GLY GLY GLN VAL ARG ASP GLU TYR ARG GLN ASP TYR ASP          
-SEQRES  12 Z  156  ALA GLY ARG GLY GLY TYR GLY LYS LEU ALA GLN ASN GLN          
-HET    GDP  Z1151      28                                                       
-HET    7MG  Z1152      24                                                       
-HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
-HETNAM     7MG 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE                      
-FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
-FORMUL   3  7MG    C11 H18 N5 O8 P                                              
-FORMUL   4  HOH   *365(H2 O1)                                                   
-HELIX    1   1 ASP C   29  VAL C   38  1                                  10    
-HELIX    2   2 SER C   45  LEU C   79  1                                  35    
-HELIX    3   3 LYS C   82  ASN C   97  1                                  16    
-HELIX    4   4 ASN C   97  ALA C  118  1                                  22    
-HELIX    5   5 ASN C  120  CYS C  137  1                                  18    
-HELIX    6   6 ALA C  141  SER C  154  1                                  14    
-HELIX    7   7 VAL C  155  GLU C  158  5                                   4    
-HELIX    8   8 PRO C  162  SER C  175  1                                  14    
-HELIX    9   9 SER C  176  ARG C  206  1                                  31    
-HELIX   10  10 HIS C  210  GLN C  215  1                                   6    
-HELIX   11  11 GLU C  227  ASP C  242  1                                  16    
-HELIX   12  12 ARG C  251  ALA C  255  5                                   5    
-HELIX   13  13 PHE C  256  GLU C  262  1                                   7    
-HELIX   14  14 ASP C  293  ASP C  297  5                                   5    
-HELIX   15  15 SER C  308  TRP C  326  1                                  19    
-HELIX   16  16 GLU C  328  SER C  338  1                                  11    
-HELIX   17  17 PRO C  346  PHE C  360  1                                  15    
-HELIX   18  18 ILE C  368  GLN C  383  1                                  16    
-HELIX   19  19 SER C  386  ARG C  401  1                                  16    
-HELIX   20  20 LEU C  402  THR C  404  5                                   3    
-HELIX   21  21 ASN C  406  ASN C  423  1                                  18    
-HELIX   22  22 SER C  429  LEU C  437  5                                   9    
-HELIX   23  23 SER C  443  LEU C  459  1                                  17    
-HELIX   24  24 TYR C  461  VAL C  469  1                                   9    
-HELIX   25  25 PRO C  470  CYS C  477  5                                   8    
-HELIX   26  26 GLY C  497  SER C  510  1                                  14    
-HELIX   27  27 THR C  513  LEU C  521  1                                   9    
-HELIX   28  28 LYS C  522  VAL C  524  5                                   3    
-HELIX   29  29 ASN C  540  LEU C  552  1                                  13    
-HELIX   30  30 HIS C  553  ALA C  556  5                                   4    
-HELIX   31  31 SER C  558  PHE C  569  1                                  12    
-HELIX   32  32 PHE C  569  ALA C  577  1                                   9    
-HELIX   33  33 SER C  579  ARG C  595  1                                  17    
-HELIX   34  34 HIS C  597  THR C  611  1                                  15    
-HELIX   35  35 ASP C  615  SER C  625  1                                  11    
-HELIX   36  36 SER C  626  SER C  629  5                                   4    
-HELIX   37  37 ARG C  634  HIS C  651  1                                  18    
-HELIX   38  38 ALA C  702  ASP C  731  1                                  30    
-HELIX   39  39 THR C  737  HIS C  754  1                                  18    
-HELIX   40  40 HIS C  754  GLN C  759  1                                   6    
-HELIX   41  41 TYR C  761  LEU C  769  1                                   9    
-HELIX   42  42 ASP C  775  LEU C  788  1                                  14    
-HELIX   43  43 LEU Z    6  SER Z   11  1                                   6    
-HELIX   44  44 ASP Z   12  GLU Z   16  5                                   5    
-HELIX   45  45 ASP Z   28  LYS Z   37  1                                  10    
-HELIX   46  46 THR Z   52  SER Z   61  1                                  10    
-HELIX   47  47 LYS Z   62  GLY Z   64  5                                   3    
-HELIX   48  48 SER Z   90  ILE Z  101  1                                  12    
-HELIX   49  49 GLN Z  133  TYR Z  138  5                                   6    
-HELIX   50  50 ALA Z  144  GLY Z  147  5                                   4    
-SHEET    1  ZA 4 ILE Z  66  LEU Z  73  0                                        
-SHEET    2  ZA 4 ALA Z  80  TYR Z  88 -1  N  CYS Z  81   O  GLY Z  72           
-SHEET    3  ZA 4 THR Z  41  GLY Z  45 -1  O  LEU Z  42   N  VAL Z  86           
-SHEET    4  ZA 4 ARG Z 112  TRP Z 115 -1  O  ARG Z 112   N  GLY Z  45           
-SHEET    1  ZB 2 ARG Z 105  LEU Z 106  0                                        
-SHEET    2  ZB 2 ARG Z 109  ILE Z 110 -1  O  ARG Z 109   N  LEU Z 106           
-LINK         O3B GDP Z1151                 P   7MG Z1152     1555   1555  1.62  
-CISPEP   1 LYS C  221    PRO C  222          0         0.91                     
-CISPEP   2 LEU C  362    PRO C  363          0         0.46                     
-SITE     1 AC1  7 GLU C  58  TYR Z  20  ARG Z 127  VAL Z 134                    
-SITE     2 AC1  7 TYR Z 138  7MG Z1152  HOH Z2063                               
-SITE     1 AC2 15 TYR Z  20  ASP Z  22  TYR Z  43  PHE Z  83                    
-SITE     2 AC2 15 ARG Z 112  ASP Z 114  TRP Z 115  ASP Z 116                    
-SITE     3 AC2 15 ARG Z 123  TYR Z 125  ARG Z 127  GLN Z 133                    
-SITE     4 AC2 15 VAL Z 134  GDP Z1151  HOH Z2062                               
-CRYST1  112.780  112.780  158.310  90.00  90.00 120.00 P 31 2 1      6          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.008867  0.005119  0.000000        0.00000                         
-SCALE2      0.000000  0.010238  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.006317        0.00000                         
-ATOM      1  N   ASP C  29     -10.273  66.097  84.276  1.00 60.59           N  
-ATOM      2  CA  ASP C  29     -11.351  65.112  83.958  1.00 59.79           C  
-ATOM      3  C   ASP C  29     -12.548  65.829  83.335  1.00 58.28           C  
-ATOM      4  O   ASP C  29     -12.802  65.701  82.136  1.00 56.36           O  
-ATOM      5  CB  ASP C  29     -11.792  64.386  85.232  1.00 63.66           C  
-ATOM      6  CG  ASP C  29     -12.668  63.173  84.947  1.00 68.89           C  
-ATOM      7  OD1 ASP C  29     -13.147  62.544  85.917  1.00 70.88           O  
-ATOM      8  OD2 ASP C  29     -12.871  62.844  83.759  1.00 72.08           O  
-ATOM      9  N   HIS C  30     -13.276  66.587  84.154  1.00 56.24           N  
-ATOM     10  CA  HIS C  30     -14.447  67.326  83.683  1.00 55.10           C  
-ATOM     11  C   HIS C  30     -14.064  68.415  82.684  1.00 52.97           C  
-ATOM     12  O   HIS C  30     -14.603  68.479  81.578  1.00 51.85           O  
-ATOM     13  CB  HIS C  30     -15.186  67.966  84.860  1.00 56.41           C  
-ATOM     14  CG  HIS C  30     -16.354  68.809  84.448  1.00 59.37           C  
-ATOM     15  ND1 HIS C  30     -17.435  68.297  83.761  1.00 58.08           N  
-ATOM     16  CD2 HIS C  30     -16.604  70.130  84.614  1.00 57.57           C  
-ATOM     17  CE1 HIS C  30     -18.300  69.266  83.522  1.00 57.75           C  
-ATOM     18  NE2 HIS C  30     -17.820  70.388  84.029  1.00 57.29           N  
-ATOM     19  N   LEU C  31     -13.137  69.272  83.091  1.00 50.42           N  
-ATOM     20  CA  LEU C  31     -12.671  70.358  82.243  1.00 49.52           C  
-ATOM     21  C   LEU C  31     -12.026  69.832  80.971  1.00 48.50           C  
-ATOM     22  O   LEU C  31     -12.167  70.428  79.905  1.00 47.50           O  
-ATOM     23  CB  LEU C  31     -11.666  71.227  83.004  1.00 49.48           C  
-ATOM     24  CG  LEU C  31     -12.160  72.610  83.440  1.00 54.81           C  
-ATOM     25  CD1 LEU C  31     -13.531  72.493  84.086  1.00 55.53           C  
-ATOM     26  CD2 LEU C  31     -11.153  73.229  84.400  1.00 57.26           C  
-ATOM     27  N   GLU C  32     -11.314  68.715  81.084  1.00 46.75           N  
-ATOM     28  CA  GLU C  32     -10.657  68.141  79.923  1.00 45.50           C  
-ATOM     29  C   GLU C  32     -11.692  67.669  78.912  1.00 44.61           C  
-ATOM     30  O   GLU C  32     -11.510  67.826  77.703  1.00 43.27           O  
-ATOM     31  CB  GLU C  32      -9.752  66.975  80.328  1.00 44.13           C  
-ATOM     32  CG  GLU C  32      -9.050  66.326  79.142  1.00 46.85           C  
-ATOM     33  CD  GLU C  32      -7.982  65.324  79.547  1.00 50.94           C  
-ATOM     34  OE1 GLU C  32      -7.568  64.517  78.685  1.00 49.94           O  
-ATOM     35  OE2 GLU C  32      -7.552  65.349  80.722  1.00 52.56           O  
-ATOM     36  N   SER C  33     -12.782  67.098  79.409  1.00 43.88           N  
-ATOM     37  CA  SER C  33     -13.838  66.611  78.537  1.00 44.24           C  
-ATOM     38  C   SER C  33     -14.529  67.769  77.829  1.00 45.74           C  
-ATOM     39  O   SER C  33     -14.843  67.677  76.640  1.00 45.07           O  
-ATOM     40  CB  SER C  33     -14.863  65.815  79.338  1.00 41.58           C  
-ATOM     41  OG  SER C  33     -15.875  65.316  78.486  1.00 47.45           O  
-ATOM     42  N   LEU C  34     -14.762  68.861  78.557  1.00 45.29           N  
-ATOM     43  CA  LEU C  34     -15.424  70.025  77.975  1.00 46.01           C  
-ATOM     44  C   LEU C  34     -14.617  70.604  76.816  1.00 45.30           C  
-ATOM     45  O   LEU C  34     -15.143  70.803  75.722  1.00 47.84           O  
-ATOM     46  CB  LEU C  34     -15.636  71.103  79.038  1.00 45.77           C  
-ATOM     47  CG  LEU C  34     -16.624  70.757  80.152  1.00 46.72           C  
-ATOM     48  CD1 LEU C  34     -16.452  71.721  81.309  1.00 47.57           C  
-ATOM     49  CD2 LEU C  34     -18.037  70.801  79.611  1.00 46.90           C  
-ATOM     50  N   ILE C  35     -13.339  70.865  77.065  1.00 43.97           N  
-ATOM     51  CA  ILE C  35     -12.442  71.427  76.064  1.00 43.40           C  
-ATOM     52  C   ILE C  35     -12.291  70.522  74.835  1.00 44.36           C  
-ATOM     53  O   ILE C  35     -12.290  71.004  73.706  1.00 41.60           O  
-ATOM     54  CB  ILE C  35     -11.051  71.701  76.694  1.00 42.64           C  
-ATOM     55  CG1 ILE C  35     -11.204  72.716  77.833  1.00 42.31           C  
-ATOM     56  CG2 ILE C  35     -10.076  72.214  75.647  1.00 36.60           C  
-ATOM     57  CD1 ILE C  35      -9.898  73.096  78.522  1.00 46.20           C  
-ATOM     58  N   CYS C  36     -12.177  69.214  75.067  1.00 44.89           N  
-ATOM     59  CA  CYS C  36     -12.021  68.235  73.991  1.00 47.72           C  
-ATOM     60  C   CYS C  36     -13.287  67.988  73.177  1.00 48.58           C  
-ATOM     61  O   CYS C  36     -13.212  67.566  72.021  1.00 48.95           O  
-ATOM     62  CB  CYS C  36     -11.545  66.891  74.557  1.00 47.39           C  
-ATOM     63  SG  CYS C  36      -9.812  66.850  75.078  1.00 52.22           S  
-ATOM     64  N   LYS C  37     -14.444  68.233  73.783  1.00 49.09           N  
-ATOM     65  CA  LYS C  37     -15.710  68.008  73.103  1.00 50.90           C  
-ATOM     66  C   LYS C  37     -16.237  69.196  72.297  1.00 51.53           C  
-ATOM     67  O   LYS C  37     -17.031  69.012  71.375  1.00 52.66           O  
-ATOM     68  CB  LYS C  37     -16.773  67.563  74.110  1.00 51.91           C  
-ATOM     69  CG  LYS C  37     -16.608  66.127  74.593  1.00 57.46           C  
-ATOM     70  CD  LYS C  37     -17.881  65.641  75.262  1.00 59.42           C  
-ATOM     71  CE  LYS C  37     -17.802  64.170  75.634  1.00 62.45           C  
-ATOM     72  NZ  LYS C  37     -19.114  63.694  76.169  1.00 65.64           N  
-ATOM     73  N   VAL C  38     -15.807  70.406  72.641  1.00 50.79           N  
-ATOM     74  CA  VAL C  38     -16.268  71.590  71.928  1.00 51.48           C  
-ATOM     75  C   VAL C  38     -15.965  71.460  70.434  1.00 53.73           C  
-ATOM     76  O   VAL C  38     -14.823  71.212  70.032  1.00 53.72           O  
-ATOM     77  CB  VAL C  38     -15.610  72.875  72.487  1.00 49.19           C  
-ATOM     78  CG1 VAL C  38     -14.117  72.860  72.221  1.00 42.06           C  
-ATOM     79  CG2 VAL C  38     -16.263  74.104  71.875  1.00 48.32           C  
-ATOM     80  N   GLY C  39     -17.002  71.612  69.618  1.00 55.00           N  
-ATOM     81  CA  GLY C  39     -16.832  71.499  68.182  1.00 56.37           C  
-ATOM     82  C   GLY C  39     -17.424  70.213  67.635  1.00 57.31           C  
-ATOM     83  O   GLY C  39     -17.481  70.007  66.422  1.00 58.21           O  
-ATOM     84  N   GLU C  40     -17.869  69.336  68.523  1.00 57.39           N  
-ATOM     85  CA  GLU C  40     -18.455  68.081  68.076  1.00 59.74           C  
-ATOM     86  C   GLU C  40     -19.977  68.190  67.932  1.00 61.04           C  
-ATOM     87  O   GLU C  40     -20.541  69.290  67.925  1.00 58.43           O  
-ATOM     88  CB  GLU C  40     -18.110  66.954  69.057  1.00 60.15           C  
-ATOM     89  CG  GLU C  40     -16.630  66.863  69.420  1.00 63.10           C  
-ATOM     90  CD  GLU C  40     -16.323  65.701  70.356  1.00 64.90           C  
-ATOM     91  OE1 GLU C  40     -17.110  65.473  71.300  1.00 69.66           O  
-ATOM     92  OE2 GLU C  40     -15.293  65.021  70.158  1.00 63.13           O  
-ATOM     93  N   LYS C  41     -20.617  67.029  67.808  1.00 63.55           N  
-ATOM     94  CA  LYS C  41     -22.067  66.904  67.676  1.00 66.95           C  
-ATOM     95  C   LYS C  41     -22.788  67.741  68.730  1.00 67.87           C  
-ATOM     96  O   LYS C  41     -22.631  67.506  69.931  1.00 69.00           O  
-ATOM     97  CB  LYS C  41     -22.469  65.433  67.849  1.00 71.43           C  
-ATOM     98  CG  LYS C  41     -21.980  64.819  69.169  1.00 74.90           C  
-ATOM     99  CD  LYS C  41     -22.468  63.385  69.381  1.00 80.36           C  
-ATOM    100  CE  LYS C  41     -21.916  62.798  70.687  1.00 81.65           C  
-ATOM    101  NZ  LYS C  41     -22.377  61.402  70.965  1.00 81.91           N  
-ATOM    102  N   SER C  42     -23.584  68.710  68.291  1.00 67.82           N  
-ATOM    103  CA  SER C  42     -24.303  69.555  69.237  1.00 68.30           C  
-ATOM    104  C   SER C  42     -25.568  70.161  68.651  1.00 68.44           C  
-ATOM    105  O   SER C  42     -25.611  70.526  67.474  1.00 67.48           O  
-ATOM    106  CB  SER C  42     -23.389  70.677  69.742  1.00 67.75           C  
-ATOM    107  OG  SER C  42     -24.073  71.533  70.645  1.00 68.92           O  
-ATOM    108  N   ALA C  43     -26.598  70.266  69.485  1.00 68.97           N  
-ATOM    109  CA  ALA C  43     -27.865  70.845  69.065  1.00 69.22           C  
-ATOM    110  C   ALA C  43     -27.691  72.352  68.891  1.00 68.97           C  
-ATOM    111  O   ALA C  43     -28.514  73.016  68.262  1.00 69.72           O  
-ATOM    112  CB  ALA C  43     -28.944  70.554  70.104  1.00 69.47           C  
-ATOM    113  N   CYS C  44     -26.611  72.884  69.453  1.00 68.60           N  
-ATOM    114  CA  CYS C  44     -26.321  74.309  69.353  1.00 67.56           C  
-ATOM    115  C   CYS C  44     -25.226  74.556  68.327  1.00 65.96           C  
-ATOM    116  O   CYS C  44     -24.528  73.629  67.917  1.00 66.51           O  
-ATOM    117  CB  CYS C  44     -25.868  74.858  70.706  1.00 67.07           C  
-ATOM    118  SG  CYS C  44     -27.054  74.634  72.029  1.00 73.00           S  
-ATOM    119  N   SER C  45     -25.076  75.811  67.921  1.00 65.05           N  
-ATOM    120  CA  SER C  45     -24.056  76.179  66.949  1.00 63.24           C  
-ATOM    121  C   SER C  45     -22.682  76.158  67.609  1.00 62.54           C  
-ATOM    122  O   SER C  45     -22.570  76.105  68.836  1.00 61.57           O  
-ATOM    123  CB  SER C  45     -24.330  77.577  66.388  1.00 62.38           C  
-ATOM    124  OG  SER C  45     -24.206  78.561  67.397  1.00 60.33           O  
-ATOM    125  N   LEU C  46     -21.642  76.201  66.781  1.00 61.74           N  
-ATOM    126  CA  LEU C  46     -20.266  76.188  67.260  1.00 58.61           C  
-ATOM    127  C   LEU C  46     -19.961  77.453  68.052  1.00 57.56           C  
-ATOM    128  O   LEU C  46     -19.424  77.387  69.156  1.00 56.67           O  
-ATOM    129  CB  LEU C  46     -19.304  76.075  66.075  1.00 55.45           C  
-ATOM    130  CG  LEU C  46     -17.804  76.078  66.385  1.00 53.65           C  
-ATOM    131  CD1 LEU C  46     -17.458  74.908  67.307  1.00 48.06           C  
-ATOM    132  CD2 LEU C  46     -17.025  75.982  65.082  1.00 48.99           C  
-ATOM    133  N   GLU C  47     -20.304  78.605  67.481  1.00 57.19           N  
-ATOM    134  CA  GLU C  47     -20.058  79.881  68.142  1.00 56.51           C  
-ATOM    135  C   GLU C  47     -20.749  79.901  69.494  1.00 54.44           C  
-ATOM    136  O   GLU C  47     -20.206  80.416  70.471  1.00 54.72           O  
-ATOM    137  CB  GLU C  47     -20.569  81.045  67.285  1.00 60.34           C  
-ATOM    138  CG  GLU C  47     -19.943  81.108  65.899  1.00 66.55           C  
-ATOM    139  CD  GLU C  47     -20.550  80.104  64.936  1.00 70.14           C  
-ATOM    140  OE1 GLU C  47     -19.957  79.884  63.856  1.00 72.86           O  
-ATOM    141  OE2 GLU C  47     -21.622  79.544  65.254  1.00 70.58           O  
-ATOM    142  N   SER C  48     -21.947  79.329  69.539  1.00 51.80           N  
-ATOM    143  CA  SER C  48     -22.722  79.265  70.767  1.00 52.82           C  
-ATOM    144  C   SER C  48     -21.948  78.445  71.798  1.00 53.16           C  
-ATOM    145  O   SER C  48     -21.709  78.903  72.916  1.00 53.23           O  
-ATOM    146  CB  SER C  48     -24.082  78.618  70.489  1.00 54.33           C  
-ATOM    147  OG  SER C  48     -24.849  78.482  71.672  1.00 56.65           O  
-ATOM    148  N   ASN C  49     -21.548  77.237  71.412  1.00 51.40           N  
-ATOM    149  CA  ASN C  49     -20.797  76.369  72.307  1.00 51.26           C  
-ATOM    150  C   ASN C  49     -19.470  76.987  72.724  1.00 50.56           C  
-ATOM    151  O   ASN C  49     -19.054  76.845  73.873  1.00 51.66           O  
-ATOM    152  CB  ASN C  49     -20.563  75.012  71.647  1.00 50.42           C  
-ATOM    153  CG  ASN C  49     -21.825  74.184  71.574  1.00 53.30           C  
-ATOM    154  OD1 ASN C  49     -21.943  73.284  70.745  1.00 57.86           O  
-ATOM    155  ND2 ASN C  49     -22.775  74.476  72.454  1.00 52.54           N  
-ATOM    156  N   LEU C  50     -18.809  77.676  71.795  1.00 49.58           N  
-ATOM    157  CA  LEU C  50     -17.535  78.318  72.092  1.00 48.04           C  
-ATOM    158  C   LEU C  50     -17.704  79.361  73.187  1.00 48.81           C  
-ATOM    159  O   LEU C  50     -16.995  79.341  74.192  1.00 47.15           O  
-ATOM    160  CB  LEU C  50     -16.958  78.982  70.837  1.00 46.77           C  
-ATOM    161  CG  LEU C  50     -16.345  78.074  69.766  1.00 50.65           C  
-ATOM    162  CD1 LEU C  50     -15.919  78.903  68.563  1.00 48.96           C  
-ATOM    163  CD2 LEU C  50     -15.147  77.346  70.350  1.00 49.76           C  
-ATOM    164  N   GLU C  51     -18.647  80.278  72.993  1.00 49.20           N  
-ATOM    165  CA  GLU C  51     -18.883  81.319  73.982  1.00 49.77           C  
-ATOM    166  C   GLU C  51     -19.337  80.676  75.290  1.00 48.28           C  
-ATOM    167  O   GLU C  51     -18.996  81.143  76.377  1.00 47.47           O  
-ATOM    168  CB  GLU C  51     -19.944  82.301  73.480  1.00 54.41           C  
-ATOM    169  CG  GLU C  51     -19.820  83.688  74.093  1.00 63.07           C  
-ATOM    170  CD  GLU C  51     -18.418  84.264  73.941  1.00 70.02           C  
-ATOM    171  OE1 GLU C  51     -17.921  84.312  72.794  1.00 71.05           O  
-ATOM    172  OE2 GLU C  51     -17.816  84.667  74.964  1.00 71.77           O  
-ATOM    173  N   GLY C  52     -20.101  79.594  75.177  1.00 48.16           N  
-ATOM    174  CA  GLY C  52     -20.569  78.890  76.362  1.00 47.76           C  
-ATOM    175  C   GLY C  52     -19.428  78.260  77.154  1.00 47.17           C  
-ATOM    176  O   GLY C  52     -19.482  78.171  78.388  1.00 46.86           O  
-ATOM    177  N   LEU C  53     -18.391  77.815  76.445  1.00 44.47           N  
-ATOM    178  CA  LEU C  53     -17.232  77.206  77.091  1.00 41.80           C  
-ATOM    179  C   LEU C  53     -16.300  78.280  77.646  1.00 40.56           C  
-ATOM    180  O   LEU C  53     -15.710  78.111  78.710  1.00 40.39           O  
-ATOM    181  CB  LEU C  53     -16.469  76.318  76.098  1.00 41.70           C  
-ATOM    182  CG  LEU C  53     -15.203  75.615  76.611  1.00 40.41           C  
-ATOM    183  CD1 LEU C  53     -15.525  74.803  77.868  1.00 37.55           C  
-ATOM    184  CD2 LEU C  53     -14.642  74.703  75.523  1.00 40.11           C  
-ATOM    185  N   ALA C  54     -16.152  79.380  76.917  1.00 39.44           N  
-ATOM    186  CA  ALA C  54     -15.296  80.458  77.381  1.00 40.97           C  
-ATOM    187  C   ALA C  54     -15.797  80.909  78.757  1.00 42.14           C  
-ATOM    188  O   ALA C  54     -15.006  81.176  79.661  1.00 40.74           O  
-ATOM    189  CB  ALA C  54     -15.331  81.625  76.398  1.00 40.43           C  
-ATOM    190  N   GLY C  55     -17.118  80.969  78.905  1.00 41.12           N  
-ATOM    191  CA  GLY C  55     -17.696  81.385  80.164  1.00 43.36           C  
-ATOM    192  C   GLY C  55     -17.354  80.429  81.287  1.00 44.16           C  
-ATOM    193  O   GLY C  55     -16.922  80.860  82.358  1.00 43.78           O  
-ATOM    194  N   VAL C  56     -17.536  79.133  81.035  1.00 43.93           N  
-ATOM    195  CA  VAL C  56     -17.259  78.094  82.024  1.00 44.04           C  
-ATOM    196  C   VAL C  56     -15.793  78.068  82.456  1.00 43.64           C  
-ATOM    197  O   VAL C  56     -15.492  77.875  83.636  1.00 43.20           O  
-ATOM    198  CB  VAL C  56     -17.651  76.698  81.481  1.00 43.34           C  
-ATOM    199  CG1 VAL C  56     -17.452  75.637  82.549  1.00 42.80           C  
-ATOM    200  CG2 VAL C  56     -19.090  76.716  81.022  1.00 43.85           C  
-ATOM    201  N   LEU C  57     -14.885  78.264  81.505  1.00 44.24           N  
-ATOM    202  CA  LEU C  57     -13.458  78.262  81.815  1.00 44.91           C  
-ATOM    203  C   LEU C  57     -13.074  79.500  82.622  1.00 46.46           C  
-ATOM    204  O   LEU C  57     -12.285  79.415  83.564  1.00 45.76           O  
-ATOM    205  CB  LEU C  57     -12.626  78.200  80.530  1.00 44.04           C  
-ATOM    206  CG  LEU C  57     -12.711  76.909  79.709  1.00 45.24           C  
-ATOM    207  CD1 LEU C  57     -11.917  77.061  78.418  1.00 44.42           C  
-ATOM    208  CD2 LEU C  57     -12.176  75.746  80.534  1.00 45.60           C  
-ATOM    209  N   GLU C  58     -13.634  80.649  82.257  1.00 47.21           N  
-ATOM    210  CA  GLU C  58     -13.325  81.885  82.971  1.00 47.97           C  
-ATOM    211  C   GLU C  58     -13.671  81.731  84.448  1.00 47.11           C  
-ATOM    212  O   GLU C  58     -12.915  82.146  85.328  1.00 48.12           O  
-ATOM    213  CB  GLU C  58     -14.118  83.059  82.402  1.00 47.02           C  
-ATOM    214  CG  GLU C  58     -13.576  84.393  82.870  1.00 51.98           C  
-ATOM    215  CD  GLU C  58     -14.507  85.550  82.596  1.00 55.62           C  
-ATOM    216  OE1 GLU C  58     -14.055  86.703  82.764  1.00 59.47           O  
-ATOM    217  OE2 GLU C  58     -15.681  85.313  82.227  1.00 54.46           O  
-ATOM    218  N   ALA C  59     -14.825  81.126  84.701  1.00 47.09           N  
-ATOM    219  CA  ALA C  59     -15.314  80.899  86.054  1.00 48.38           C  
-ATOM    220  C   ALA C  59     -14.410  79.962  86.853  1.00 48.32           C  
-ATOM    221  O   ALA C  59     -14.306  80.084  88.071  1.00 49.41           O  
-ATOM    222  CB  ALA C  59     -16.734  80.331  85.998  1.00 45.50           C  
-ATOM    223  N   ASP C  60     -13.755  79.025  86.177  1.00 48.90           N  
-ATOM    224  CA  ASP C  60     -12.884  78.093  86.876  1.00 48.14           C  
-ATOM    225  C   ASP C  60     -11.439  78.541  86.904  1.00 47.77           C  
-ATOM    226  O   ASP C  60     -10.588  77.825  87.414  1.00 49.36           O  
-ATOM    227  CB  ASP C  60     -12.966  76.695  86.257  1.00 50.34           C  
-ATOM    228  CG  ASP C  60     -14.290  76.013  86.529  1.00 54.94           C  
-ATOM    229  OD1 ASP C  60     -14.827  76.183  87.643  1.00 59.38           O  
-ATOM    230  OD2 ASP C  60     -14.785  75.293  85.638  1.00 57.20           O  
-ATOM    231  N   LEU C  61     -11.155  79.722  86.370  1.00 47.53           N  
-ATOM    232  CA  LEU C  61      -9.782  80.224  86.367  1.00 48.93           C  
-ATOM    233  C   LEU C  61      -9.179  80.419  87.755  1.00 50.53           C  
-ATOM    234  O   LEU C  61      -7.998  80.135  87.970  1.00 51.50           O  
-ATOM    235  CB  LEU C  61      -9.684  81.544  85.601  1.00 48.25           C  
-ATOM    236  CG  LEU C  61      -9.652  81.450  84.077  1.00 47.64           C  
-ATOM    237  CD1 LEU C  61      -9.436  82.839  83.501  1.00 44.30           C  
-ATOM    238  CD2 LEU C  61      -8.528  80.514  83.637  1.00 50.66           C  
-ATOM    239  N   PRO C  62      -9.971  80.927  88.713  1.00 51.15           N  
-ATOM    240  CA  PRO C  62      -9.427  81.129  90.059  1.00 51.06           C  
-ATOM    241  C   PRO C  62      -8.978  79.842  90.746  1.00 50.75           C  
-ATOM    242  O   PRO C  62      -7.965  79.833  91.442  1.00 51.67           O  
-ATOM    243  CB  PRO C  62     -10.575  81.817  90.797  1.00 52.75           C  
-ATOM    244  CG  PRO C  62     -11.798  81.308  90.086  1.00 54.38           C  
-ATOM    245  CD  PRO C  62     -11.370  81.388  88.641  1.00 51.86           C  
-ATOM    246  N   ASN C  63      -9.718  78.756  90.539  1.00 50.18           N  
-ATOM    247  CA  ASN C  63      -9.374  77.481  91.167  1.00 50.51           C  
-ATOM    248  C   ASN C  63      -8.649  76.454  90.282  1.00 50.48           C  
-ATOM    249  O   ASN C  63      -8.084  75.491  90.800  1.00 48.87           O  
-ATOM    250  CB  ASN C  63     -10.636  76.821  91.746  1.00 50.78           C  
-ATOM    251  CG  ASN C  63     -11.316  77.677  92.801  1.00 50.28           C  
-ATOM    252  OD1 ASN C  63     -10.757  78.672  93.267  1.00 50.13           O  
-ATOM    253  ND2 ASN C  63     -12.528  77.290  93.187  1.00 45.15           N  
-ATOM    254  N   TYR C  64      -8.667  76.646  88.963  1.00 50.41           N  
-ATOM    255  CA  TYR C  64      -8.024  75.697  88.052  1.00 49.37           C  
-ATOM    256  C   TYR C  64      -7.318  76.339  86.862  1.00 48.31           C  
-ATOM    257  O   TYR C  64      -7.311  75.773  85.764  1.00 47.07           O  
-ATOM    258  CB  TYR C  64      -9.057  74.691  87.530  1.00 54.10           C  
-ATOM    259  CG  TYR C  64      -9.676  73.824  88.604  1.00 62.25           C  
-ATOM    260  CD1 TYR C  64      -8.888  72.966  89.371  1.00 65.34           C  
-ATOM    261  CD2 TYR C  64     -11.045  73.879  88.872  1.00 65.60           C  
-ATOM    262  CE1 TYR C  64      -9.447  72.185  90.384  1.00 70.09           C  
-ATOM    263  CE2 TYR C  64     -11.614  73.103  89.882  1.00 69.18           C  
-ATOM    264  CZ  TYR C  64     -10.807  72.260  90.634  1.00 71.58           C  
-ATOM    265  OH  TYR C  64     -11.348  71.500  91.649  1.00 75.18           O  
-ATOM    266  N   LYS C  65      -6.714  77.504  87.070  1.00 45.71           N  
-ATOM    267  CA  LYS C  65      -6.019  78.174  85.979  1.00 42.17           C  
-ATOM    268  C   LYS C  65      -4.893  77.313  85.424  1.00 41.68           C  
-ATOM    269  O   LYS C  65      -4.701  77.227  84.207  1.00 40.24           O  
-ATOM    270  CB  LYS C  65      -5.433  79.507  86.435  1.00 38.93           C  
-ATOM    271  CG  LYS C  65      -4.621  80.187  85.338  1.00 39.76           C  
-ATOM    272  CD  LYS C  65      -4.201  81.590  85.724  1.00 46.92           C  
-ATOM    273  CE  LYS C  65      -3.198  81.584  86.859  1.00 50.41           C  
-ATOM    274  NZ  LYS C  65      -2.805  82.976  87.208  1.00 51.87           N  
-ATOM    275  N   SER C  66      -4.146  76.690  86.329  1.00 38.91           N  
-ATOM    276  CA  SER C  66      -3.023  75.852  85.954  1.00 39.25           C  
-ATOM    277  C   SER C  66      -3.462  74.691  85.072  1.00 38.72           C  
-ATOM    278  O   SER C  66      -2.837  74.401  84.057  1.00 40.53           O  
-ATOM    279  CB  SER C  66      -2.334  75.321  87.211  1.00 39.12           C  
-ATOM    280  OG  SER C  66      -1.100  74.721  86.881  1.00 44.49           O  
-ATOM    281  N   LYS C  67      -4.537  74.027  85.469  1.00 39.10           N  
-ATOM    282  CA  LYS C  67      -5.053  72.904  84.706  1.00 40.20           C  
-ATOM    283  C   LYS C  67      -5.613  73.378  83.363  1.00 41.68           C  
-ATOM    284  O   LYS C  67      -5.496  72.681  82.357  1.00 40.45           O  
-ATOM    285  CB  LYS C  67      -6.139  72.194  85.510  1.00 40.67           C  
-ATOM    286  CG  LYS C  67      -6.745  70.977  84.831  1.00 46.22           C  
-ATOM    287  CD  LYS C  67      -7.687  70.263  85.789  1.00 53.45           C  
-ATOM    288  CE  LYS C  67      -8.250  68.985  85.182  1.00 58.44           C  
-ATOM    289  NZ  LYS C  67      -9.029  68.204  86.190  1.00 59.33           N  
-ATOM    290  N   ILE C  68      -6.221  74.563  83.347  1.00 40.70           N  
-ATOM    291  CA  ILE C  68      -6.788  75.089  82.112  1.00 39.66           C  
-ATOM    292  C   ILE C  68      -5.687  75.470  81.124  1.00 38.04           C  
-ATOM    293  O   ILE C  68      -5.814  75.223  79.923  1.00 39.10           O  
-ATOM    294  CB  ILE C  68      -7.711  76.303  82.387  1.00 38.90           C  
-ATOM    295  CG1 ILE C  68      -8.923  75.841  83.205  1.00 37.42           C  
-ATOM    296  CG2 ILE C  68      -8.200  76.908  81.070  1.00 38.34           C  
-ATOM    297  CD1 ILE C  68      -9.840  76.960  83.665  1.00 43.76           C  
-ATOM    298  N   LEU C  69      -4.601  76.047  81.631  1.00 37.98           N  
-ATOM    299  CA  LEU C  69      -3.478  76.436  80.781  1.00 36.17           C  
-ATOM    300  C   LEU C  69      -2.825  75.200  80.152  1.00 37.54           C  
-ATOM    301  O   LEU C  69      -2.473  75.208  78.971  1.00 35.48           O  
-ATOM    302  CB  LEU C  69      -2.434  77.201  81.590  1.00 34.52           C  
-ATOM    303  CG  LEU C  69      -2.635  78.701  81.855  1.00 39.45           C  
-ATOM    304  CD1 LEU C  69      -1.621  79.194  82.886  1.00 31.90           C  
-ATOM    305  CD2 LEU C  69      -2.466  79.478  80.552  1.00 37.69           C  
-ATOM    306  N   ARG C  70      -2.660  74.146  80.950  1.00 35.64           N  
-ATOM    307  CA  ARG C  70      -2.053  72.918  80.464  1.00 34.68           C  
-ATOM    308  C   ARG C  70      -2.924  72.274  79.397  1.00 32.19           C  
-ATOM    309  O   ARG C  70      -2.431  71.888  78.342  1.00 29.80           O  
-ATOM    310  CB  ARG C  70      -1.839  71.913  81.608  1.00 36.62           C  
-ATOM    311  CG  ARG C  70      -1.312  70.547  81.135  1.00 36.69           C  
-ATOM    312  CD  ARG C  70      -0.998  69.627  82.305  1.00 32.05           C  
-ATOM    313  NE  ARG C  70      -2.155  69.437  83.173  1.00 35.25           N  
-ATOM    314  CZ  ARG C  70      -3.189  68.652  82.890  1.00 37.04           C  
-ATOM    315  NH1 ARG C  70      -3.218  67.968  81.757  1.00 34.63           N  
-ATOM    316  NH2 ARG C  70      -4.201  68.555  83.742  1.00 34.76           N  
-ATOM    317  N   LEU C  71      -4.216  72.148  79.687  1.00 30.30           N  
-ATOM    318  CA  LEU C  71      -5.141  71.533  78.752  1.00 32.26           C  
-ATOM    319  C   LEU C  71      -5.180  72.283  77.417  1.00 34.06           C  
-ATOM    320  O   LEU C  71      -5.191  71.657  76.359  1.00 36.53           O  
-ATOM    321  CB  LEU C  71      -6.538  71.447  79.375  1.00 29.58           C  
-ATOM    322  CG  LEU C  71      -6.705  70.425  80.510  1.00 30.49           C  
-ATOM    323  CD1 LEU C  71      -8.108  70.542  81.107  1.00 28.18           C  
-ATOM    324  CD2 LEU C  71      -6.465  69.001  79.977  1.00 27.84           C  
-ATOM    325  N   LEU C  72      -5.181  73.612  77.460  1.00 34.15           N  
-ATOM    326  CA  LEU C  72      -5.202  74.395  76.223  1.00 35.52           C  
-ATOM    327  C   LEU C  72      -3.908  74.225  75.422  1.00 35.67           C  
-ATOM    328  O   LEU C  72      -3.949  74.102  74.197  1.00 34.48           O  
-ATOM    329  CB  LEU C  72      -5.458  75.880  76.520  1.00 32.97           C  
-ATOM    330  CG  LEU C  72      -6.873  76.182  77.027  1.00 34.17           C  
-ATOM    331  CD1 LEU C  72      -7.027  77.663  77.334  1.00 36.26           C  
-ATOM    332  CD2 LEU C  72      -7.887  75.744  75.985  1.00 36.68           C  
-ATOM    333  N   CYS C  73      -2.764  74.215  76.106  1.00 34.49           N  
-ATOM    334  CA  CYS C  73      -1.488  74.025  75.416  1.00 33.07           C  
-ATOM    335  C   CYS C  73      -1.451  72.634  74.797  1.00 32.31           C  
-ATOM    336  O   CYS C  73      -0.858  72.424  73.736  1.00 30.18           O  
-ATOM    337  CB  CYS C  73      -0.318  74.155  76.384  1.00 35.34           C  
-ATOM    338  SG  CYS C  73       0.212  75.835  76.698  1.00 42.42           S  
-ATOM    339  N   THR C  74      -2.094  71.687  75.473  1.00 31.21           N  
-ATOM    340  CA  THR C  74      -2.146  70.311  75.002  1.00 31.99           C  
-ATOM    341  C   THR C  74      -2.984  70.153  73.726  1.00 29.65           C  
-ATOM    342  O   THR C  74      -2.518  69.537  72.775  1.00 29.39           O  
-ATOM    343  CB  THR C  74      -2.668  69.378  76.113  1.00 35.22           C  
-ATOM    344  OG1 THR C  74      -1.827  69.524  77.265  1.00 38.06           O  
-ATOM    345  CG2 THR C  74      -2.631  67.915  75.671  1.00 36.56           C  
-ATOM    346  N   VAL C  75      -4.202  70.695  73.679  1.00 29.74           N  
-ATOM    347  CA  VAL C  75      -4.979  70.557  72.440  1.00 30.58           C  
-ATOM    348  C   VAL C  75      -4.304  71.317  71.300  1.00 31.02           C  
-ATOM    349  O   VAL C  75      -4.434  70.941  70.137  1.00 34.15           O  
-ATOM    350  CB  VAL C  75      -6.438  71.045  72.582  1.00 31.24           C  
-ATOM    351  CG1 VAL C  75      -7.197  70.126  73.545  1.00 30.26           C  
-ATOM    352  CG2 VAL C  75      -6.474  72.492  73.042  1.00 32.46           C  
-ATOM    353  N   ALA C  76      -3.557  72.365  71.630  1.00 29.36           N  
-ATOM    354  CA  ALA C  76      -2.860  73.136  70.607  1.00 30.96           C  
-ATOM    355  C   ALA C  76      -1.793  72.266  69.947  1.00 32.47           C  
-ATOM    356  O   ALA C  76      -1.539  72.370  68.741  1.00 31.41           O  
-ATOM    357  CB  ALA C  76      -2.214  74.368  71.221  1.00 24.05           C  
-ATOM    358  N   ARG C  77      -1.187  71.396  70.751  1.00 31.48           N  
-ATOM    359  CA  ARG C  77      -0.136  70.499  70.289  1.00 30.25           C  
-ATOM    360  C   ARG C  77      -0.617  69.164  69.710  1.00 28.22           C  
-ATOM    361  O   ARG C  77      -0.014  68.634  68.771  1.00 29.24           O  
-ATOM    362  CB  ARG C  77       0.830  70.228  71.449  1.00 31.66           C  
-ATOM    363  CG  ARG C  77       1.970  69.269  71.139  1.00 34.90           C  
-ATOM    364  CD  ARG C  77       2.903  69.136  72.343  1.00 42.66           C  
-ATOM    365  NE  ARG C  77       2.223  68.600  73.528  1.00 44.54           N  
-ATOM    366  CZ  ARG C  77       2.079  67.302  73.793  1.00 44.49           C  
-ATOM    367  NH1 ARG C  77       2.570  66.393  72.960  1.00 46.79           N  
-ATOM    368  NH2 ARG C  77       1.447  66.906  74.894  1.00 41.28           N  
-ATOM    369  N   LEU C  78      -1.706  68.631  70.249  1.00 26.37           N  
-ATOM    370  CA  LEU C  78      -2.198  67.324  69.823  1.00 27.45           C  
-ATOM    371  C   LEU C  78      -3.455  67.279  68.966  1.00 27.15           C  
-ATOM    372  O   LEU C  78      -3.774  66.236  68.410  1.00 25.76           O  
-ATOM    373  CB  LEU C  78      -2.422  66.436  71.059  1.00 29.66           C  
-ATOM    374  CG  LEU C  78      -1.195  66.187  71.943  1.00 31.10           C  
-ATOM    375  CD1 LEU C  78      -1.606  65.342  73.135  1.00 30.16           C  
-ATOM    376  CD2 LEU C  78      -0.089  65.491  71.152  1.00 28.90           C  
-ATOM    377  N   LEU C  79      -4.177  68.388  68.870  1.00 28.26           N  
-ATOM    378  CA  LEU C  79      -5.398  68.422  68.061  1.00 28.85           C  
-ATOM    379  C   LEU C  79      -5.305  69.507  66.975  1.00 28.11           C  
-ATOM    380  O   LEU C  79      -6.164  70.384  66.892  1.00 27.65           O  
-ATOM    381  CB  LEU C  79      -6.604  68.689  68.963  1.00 30.17           C  
-ATOM    382  CG  LEU C  79      -7.453  67.527  69.498  1.00 38.88           C  
-ATOM    383  CD1 LEU C  79      -6.590  66.403  70.011  1.00 37.91           C  
-ATOM    384  CD2 LEU C  79      -8.369  68.056  70.596  1.00 35.95           C  
-ATOM    385  N   PRO C  80      -4.260  69.457  66.133  1.00 27.42           N  
-ATOM    386  CA  PRO C  80      -4.119  70.469  65.083  1.00 28.93           C  
-ATOM    387  C   PRO C  80      -5.294  70.546  64.114  1.00 29.56           C  
-ATOM    388  O   PRO C  80      -5.572  71.611  63.572  1.00 30.35           O  
-ATOM    389  CB  PRO C  80      -2.799  70.091  64.400  1.00 26.90           C  
-ATOM    390  CG  PRO C  80      -2.691  68.617  64.644  1.00 23.10           C  
-ATOM    391  CD  PRO C  80      -3.159  68.480  66.072  1.00 24.65           C  
-ATOM    392  N   GLU C  81      -5.992  69.431  63.914  1.00 29.41           N  
-ATOM    393  CA  GLU C  81      -7.137  69.411  63.010  1.00 29.30           C  
-ATOM    394  C   GLU C  81      -8.255  70.328  63.510  1.00 29.96           C  
-ATOM    395  O   GLU C  81      -9.192  70.610  62.772  1.00 30.50           O  
-ATOM    396  CB  GLU C  81      -7.684  67.992  62.860  1.00 28.65           C  
-ATOM    397  CG  GLU C  81      -8.082  67.366  64.183  1.00 34.28           C  
-ATOM    398  CD  GLU C  81      -6.992  66.479  64.769  1.00 34.49           C  
-ATOM    399  OE1 GLU C  81      -5.806  66.871  64.740  1.00 27.67           O  
-ATOM    400  OE2 GLU C  81      -7.332  65.382  65.266  1.00 35.96           O  
-ATOM    401  N   LYS C  82      -8.146  70.800  64.751  1.00 28.59           N  
-ATOM    402  CA  LYS C  82      -9.163  71.677  65.333  1.00 30.49           C  
-ATOM    403  C   LYS C  82      -8.585  73.034  65.716  1.00 30.34           C  
-ATOM    404  O   LYS C  82      -9.156  73.750  66.534  1.00 31.57           O  
-ATOM    405  CB  LYS C  82      -9.791  71.012  66.568  1.00 32.07           C  
-ATOM    406  CG  LYS C  82     -10.694  69.827  66.234  1.00 30.08           C  
-ATOM    407  CD  LYS C  82     -11.140  69.068  67.477  1.00 37.69           C  
-ATOM    408  CE  LYS C  82     -12.121  69.866  68.330  1.00 37.73           C  
-ATOM    409  NZ  LYS C  82     -12.656  69.028  69.440  1.00 37.99           N  
-ATOM    410  N   LEU C  83      -7.451  73.363  65.105  1.00 29.66           N  
-ATOM    411  CA  LEU C  83      -6.712  74.607  65.319  1.00 31.84           C  
-ATOM    412  C   LEU C  83      -7.519  75.901  65.471  1.00 32.73           C  
-ATOM    413  O   LEU C  83      -7.351  76.630  66.450  1.00 32.16           O  
-ATOM    414  CB  LEU C  83      -5.707  74.780  64.176  1.00 29.57           C  
-ATOM    415  CG  LEU C  83      -4.944  76.093  64.014  1.00 34.30           C  
-ATOM    416  CD1 LEU C  83      -4.086  76.355  65.236  1.00 36.52           C  
-ATOM    417  CD2 LEU C  83      -4.082  76.011  62.766  1.00 33.98           C  
-ATOM    418  N   THR C  84      -8.380  76.193  64.499  1.00 31.66           N  
-ATOM    419  CA  THR C  84      -9.171  77.422  64.538  1.00 30.92           C  
-ATOM    420  C   THR C  84     -10.238  77.402  65.615  1.00 30.73           C  
-ATOM    421  O   THR C  84     -10.662  78.451  66.096  1.00 28.86           O  
-ATOM    422  CB  THR C  84      -9.842  77.703  63.177  1.00 28.43           C  
-ATOM    423  OG1 THR C  84     -10.722  76.623  62.836  1.00 27.18           O  
-ATOM    424  CG2 THR C  84      -8.791  77.847  62.105  1.00 18.95           C  
-ATOM    425  N   ILE C  85     -10.679  76.211  65.995  1.00 30.41           N  
-ATOM    426  CA  ILE C  85     -11.685  76.099  67.038  1.00 31.97           C  
-ATOM    427  C   ILE C  85     -11.077  76.525  68.378  1.00 34.11           C  
-ATOM    428  O   ILE C  85     -11.685  77.288  69.136  1.00 34.06           O  
-ATOM    429  CB  ILE C  85     -12.213  74.651  67.127  1.00 32.03           C  
-ATOM    430  CG1 ILE C  85     -13.084  74.350  65.906  1.00 29.65           C  
-ATOM    431  CG2 ILE C  85     -13.014  74.442  68.413  1.00 33.50           C  
-ATOM    432  CD1 ILE C  85     -13.433  72.867  65.744  1.00 32.24           C  
-ATOM    433  N   TYR C  86      -9.867  76.046  68.656  1.00 33.81           N  
-ATOM    434  CA  TYR C  86      -9.198  76.365  69.913  1.00 32.25           C  
-ATOM    435  C   TYR C  86      -8.533  77.731  69.941  1.00 32.38           C  
-ATOM    436  O   TYR C  86      -8.411  78.329  71.008  1.00 30.63           O  
-ATOM    437  CB  TYR C  86      -8.193  75.260  70.280  1.00 27.76           C  
-ATOM    438  CG  TYR C  86      -8.895  73.969  70.634  1.00 30.86           C  
-ATOM    439  CD1 TYR C  86      -9.839  73.933  71.661  1.00 26.47           C  
-ATOM    440  CD2 TYR C  86      -8.668  72.801  69.906  1.00 27.06           C  
-ATOM    441  CE1 TYR C  86     -10.541  72.775  71.949  1.00 26.75           C  
-ATOM    442  CE2 TYR C  86      -9.361  71.637  70.188  1.00 24.59           C  
-ATOM    443  CZ  TYR C  86     -10.300  71.629  71.212  1.00 32.39           C  
-ATOM    444  OH  TYR C  86     -11.012  70.480  71.489  1.00 34.78           O  
-ATOM    445  N   THR C  87      -8.106  78.241  68.788  1.00 33.31           N  
-ATOM    446  CA  THR C  87      -7.498  79.567  68.779  1.00 33.39           C  
-ATOM    447  C   THR C  87      -8.609  80.566  69.102  1.00 33.12           C  
-ATOM    448  O   THR C  87      -8.386  81.560  69.795  1.00 31.95           O  
-ATOM    449  CB  THR C  87      -6.852  79.916  67.415  1.00 34.91           C  
-ATOM    450  OG1 THR C  87      -7.786  79.671  66.357  1.00 35.83           O  
-ATOM    451  CG2 THR C  87      -5.585  79.085  67.204  1.00 36.43           C  
-ATOM    452  N   THR C  88      -9.812  80.285  68.614  1.00 33.06           N  
-ATOM    453  CA  THR C  88     -10.945  81.163  68.892  1.00 35.39           C  
-ATOM    454  C   THR C  88     -11.243  81.135  70.399  1.00 36.67           C  
-ATOM    455  O   THR C  88     -11.423  82.186  71.014  1.00 38.17           O  
-ATOM    456  CB  THR C  88     -12.211  80.734  68.095  1.00 34.03           C  
-ATOM    457  OG1 THR C  88     -11.935  80.804  66.689  1.00 32.19           O  
-ATOM    458  CG2 THR C  88     -13.397  81.663  68.414  1.00 39.90           C  
-ATOM    459  N   LEU C  89     -11.279  79.939  70.989  1.00 35.56           N  
-ATOM    460  CA  LEU C  89     -11.539  79.789  72.420  1.00 35.21           C  
-ATOM    461  C   LEU C  89     -10.550  80.611  73.227  1.00 35.94           C  
-ATOM    462  O   LEU C  89     -10.932  81.276  74.186  1.00 37.63           O  
-ATOM    463  CB  LEU C  89     -11.453  78.313  72.838  1.00 34.13           C  
-ATOM    464  CG  LEU C  89     -11.626  77.951  74.324  1.00 35.98           C  
-ATOM    465  CD1 LEU C  89     -12.943  78.511  74.858  1.00 37.29           C  
-ATOM    466  CD2 LEU C  89     -11.593  76.432  74.486  1.00 29.98           C  
-ATOM    467  N   VAL C  90      -9.280  80.570  72.837  1.00 36.66           N  
-ATOM    468  CA  VAL C  90      -8.249  81.328  73.530  1.00 36.24           C  
-ATOM    469  C   VAL C  90      -8.523  82.825  73.359  1.00 39.82           C  
-ATOM    470  O   VAL C  90      -8.372  83.614  74.304  1.00 39.34           O  
-ATOM    471  CB  VAL C  90      -6.845  80.981  72.985  1.00 33.41           C  
-ATOM    472  CG1 VAL C  90      -5.798  81.888  73.608  1.00 28.32           C  
-ATOM    473  CG2 VAL C  90      -6.510  79.519  73.299  1.00 31.79           C  
-ATOM    474  N   GLY C  91      -8.933  83.212  72.154  1.00 39.42           N  
-ATOM    475  CA  GLY C  91      -9.236  84.611  71.897  1.00 39.45           C  
-ATOM    476  C   GLY C  91     -10.342  85.135  72.796  1.00 39.65           C  
-ATOM    477  O   GLY C  91     -10.236  86.237  73.340  1.00 39.89           O  
-ATOM    478  N   LEU C  92     -11.404  84.346  72.950  1.00 39.37           N  
-ATOM    479  CA  LEU C  92     -12.533  84.718  73.792  1.00 40.63           C  
-ATOM    480  C   LEU C  92     -12.140  84.808  75.274  1.00 43.93           C  
-ATOM    481  O   LEU C  92     -12.616  85.690  75.996  1.00 44.66           O  
-ATOM    482  CB  LEU C  92     -13.673  83.711  73.620  1.00 38.36           C  
-ATOM    483  CG  LEU C  92     -14.292  83.636  72.219  1.00 40.35           C  
-ATOM    484  CD1 LEU C  92     -15.460  82.665  72.217  1.00 37.14           C  
-ATOM    485  CD2 LEU C  92     -14.751  85.021  71.790  1.00 36.39           C  
-ATOM    486  N   LEU C  93     -11.277  83.899  75.725  1.00 44.37           N  
-ATOM    487  CA  LEU C  93     -10.819  83.907  77.111  1.00 44.06           C  
-ATOM    488  C   LEU C  93      -9.893  85.096  77.321  1.00 44.60           C  
-ATOM    489  O   LEU C  93      -9.918  85.732  78.382  1.00 43.66           O  
-ATOM    490  CB  LEU C  93     -10.071  82.610  77.444  1.00 43.88           C  
-ATOM    491  CG  LEU C  93     -10.882  81.428  77.981  1.00 46.26           C  
-ATOM    492  CD1 LEU C  93     -12.079  81.177  77.095  1.00 51.93           C  
-ATOM    493  CD2 LEU C  93      -9.998  80.186  78.050  1.00 50.33           C  
-ATOM    494  N   ASN C  94      -9.083  85.392  76.305  1.00 44.89           N  
-ATOM    495  CA  ASN C  94      -8.141  86.506  76.364  1.00 45.77           C  
-ATOM    496  C   ASN C  94      -8.864  87.840  76.453  1.00 46.79           C  
-ATOM    497  O   ASN C  94      -8.373  88.786  77.076  1.00 45.14           O  
-ATOM    498  CB  ASN C  94      -7.249  86.524  75.130  1.00 44.84           C  
-ATOM    499  CG  ASN C  94      -6.275  87.682  75.145  1.00 50.21           C  
-ATOM    500  OD1 ASN C  94      -5.467  87.817  76.067  1.00 51.13           O  
-ATOM    501  ND2 ASN C  94      -6.346  88.530  74.124  1.00 49.64           N  
-ATOM    502  N   ALA C  95     -10.020  87.905  75.802  1.00 46.72           N  
-ATOM    503  CA  ALA C  95     -10.842  89.105  75.788  1.00 49.53           C  
-ATOM    504  C   ALA C  95     -11.415  89.336  77.176  1.00 49.81           C  
-ATOM    505  O   ALA C  95     -11.481  90.469  77.647  1.00 51.12           O  
-ATOM    506  CB  ALA C  95     -11.974  88.953  74.773  1.00 45.89           C  
-ATOM    507  N   ARG C  96     -11.830  88.255  77.828  1.00 49.78           N  
-ATOM    508  CA  ARG C  96     -12.393  88.348  79.167  1.00 49.78           C  
-ATOM    509  C   ARG C  96     -11.297  88.507  80.205  1.00 49.35           C  
-ATOM    510  O   ARG C  96     -11.508  89.123  81.244  1.00 50.23           O  
-ATOM    511  CB  ARG C  96     -13.194  87.094  79.503  1.00 51.46           C  
-ATOM    512  CG  ARG C  96     -14.328  86.785  78.554  1.00 50.25           C  
-ATOM    513  CD  ARG C  96     -15.204  85.692  79.139  1.00 52.37           C  
-ATOM    514  NE  ARG C  96     -16.247  85.272  78.215  1.00 51.72           N  
-ATOM    515  CZ  ARG C  96     -17.374  84.677  78.587  1.00 52.79           C  
-ATOM    516  NH1 ARG C  96     -17.605  84.436  79.871  1.00 57.00           N  
-ATOM    517  NH2 ARG C  96     -18.268  84.324  77.674  1.00 51.03           N  
-ATOM    518  N   ASN C  97     -10.124  87.951  79.922  1.00 48.73           N  
-ATOM    519  CA  ASN C  97      -9.016  88.017  80.869  1.00 45.81           C  
-ATOM    520  C   ASN C  97      -7.656  88.135  80.190  1.00 43.86           C  
-ATOM    521  O   ASN C  97      -7.023  87.131  79.859  1.00 42.93           O  
-ATOM    522  CB  ASN C  97      -9.039  86.778  81.766  1.00 44.59           C  
-ATOM    523  CG  ASN C  97      -8.145  86.923  82.973  1.00 41.38           C  
-ATOM    524  OD1 ASN C  97      -6.963  87.238  82.847  1.00 44.18           O  
-ATOM    525  ND2 ASN C  97      -8.705  86.694  84.154  1.00 45.70           N  
-ATOM    526  N   TYR C  98      -7.214  89.375  80.005  1.00 43.13           N  
-ATOM    527  CA  TYR C  98      -5.943  89.690  79.361  1.00 42.96           C  
-ATOM    528  C   TYR C  98      -4.746  89.014  80.017  1.00 43.97           C  
-ATOM    529  O   TYR C  98      -3.775  88.658  79.343  1.00 43.51           O  
-ATOM    530  CB  TYR C  98      -5.726  91.198  79.381  1.00 42.85           C  
-ATOM    531  CG  TYR C  98      -4.465  91.647  78.689  1.00 42.09           C  
-ATOM    532  CD1 TYR C  98      -4.387  91.680  77.299  1.00 42.18           C  
-ATOM    533  CD2 TYR C  98      -3.348  92.037  79.423  1.00 43.78           C  
-ATOM    534  CE1 TYR C  98      -3.233  92.092  76.657  1.00 40.16           C  
-ATOM    535  CE2 TYR C  98      -2.178  92.452  78.788  1.00 43.41           C  
-ATOM    536  CZ  TYR C  98      -2.130  92.477  77.404  1.00 45.76           C  
-ATOM    537  OH  TYR C  98      -0.981  92.885  76.763  1.00 48.18           O  
-ATOM    538  N   ASN C  99      -4.809  88.870  81.337  1.00 43.53           N  
-ATOM    539  CA  ASN C  99      -3.733  88.246  82.093  1.00 43.82           C  
-ATOM    540  C   ASN C  99      -3.620  86.780  81.694  1.00 41.63           C  
-ATOM    541  O   ASN C  99      -2.538  86.306  81.358  1.00 40.58           O  
-ATOM    542  CB  ASN C  99      -4.001  88.355  83.603  1.00 47.03           C  
-ATOM    543  CG  ASN C  99      -3.960  89.793  84.108  1.00 50.92           C  
-ATOM    544  OD1 ASN C  99      -4.355  90.082  85.242  1.00 52.55           O  
-ATOM    545  ND2 ASN C  99      -3.472  90.698  83.269  1.00 51.71           N  
-ATOM    546  N   PHE C 100      -4.737  86.065  81.728  1.00 40.07           N  
-ATOM    547  CA  PHE C 100      -4.719  84.660  81.351  1.00 43.04           C  
-ATOM    548  C   PHE C 100      -4.159  84.496  79.937  1.00 43.03           C  
-ATOM    549  O   PHE C 100      -3.418  83.558  79.658  1.00 42.22           O  
-ATOM    550  CB  PHE C 100      -6.120  84.055  81.402  1.00 42.83           C  
-ATOM    551  CG  PHE C 100      -6.166  82.641  80.913  1.00 48.56           C  
-ATOM    552  CD1 PHE C 100      -5.702  81.602  81.712  1.00 49.41           C  
-ATOM    553  CD2 PHE C 100      -6.597  82.354  79.623  1.00 48.24           C  
-ATOM    554  CE1 PHE C 100      -5.668  80.294  81.228  1.00 52.52           C  
-ATOM    555  CE2 PHE C 100      -6.565  81.056  79.134  1.00 49.62           C  
-ATOM    556  CZ  PHE C 100      -6.097  80.023  79.938  1.00 49.71           C  
-ATOM    557  N   GLY C 101      -4.518  85.421  79.049  1.00 45.54           N  
-ATOM    558  CA  GLY C 101      -4.042  85.365  77.676  1.00 44.59           C  
-ATOM    559  C   GLY C 101      -2.532  85.450  77.591  1.00 44.12           C  
-ATOM    560  O   GLY C 101      -1.904  84.771  76.774  1.00 45.42           O  
-ATOM    561  N   GLY C 102      -1.945  86.290  78.436  1.00 42.76           N  
-ATOM    562  CA  GLY C 102      -0.499  86.442  78.438  1.00 42.45           C  
-ATOM    563  C   GLY C 102       0.202  85.213  78.996  1.00 42.24           C  
-ATOM    564  O   GLY C 102       1.290  84.845  78.559  1.00 39.57           O  
-ATOM    565  N   GLU C 103      -0.418  84.576  79.981  1.00 43.10           N  
-ATOM    566  CA  GLU C 103       0.165  83.378  80.559  1.00 43.94           C  
-ATOM    567  C   GLU C 103       0.108  82.246  79.537  1.00 42.65           C  
-ATOM    568  O   GLU C 103       1.079  81.504  79.376  1.00 41.32           O  
-ATOM    569  CB  GLU C 103      -0.578  82.977  81.833  1.00 46.73           C  
-ATOM    570  CG  GLU C 103      -0.009  83.610  83.088  1.00 53.57           C  
-ATOM    571  CD  GLU C 103      -0.613  83.031  84.350  1.00 57.22           C  
-ATOM    572  OE1 GLU C 103      -1.751  83.414  84.692  1.00 57.45           O  
-ATOM    573  OE2 GLU C 103       0.049  82.183  84.992  1.00 61.51           O  
-ATOM    574  N   PHE C 104      -1.026  82.124  78.846  1.00 41.21           N  
-ATOM    575  CA  PHE C 104      -1.185  81.080  77.836  1.00 40.34           C  
-ATOM    576  C   PHE C 104      -0.107  81.194  76.771  1.00 39.01           C  
-ATOM    577  O   PHE C 104       0.552  80.207  76.429  1.00 40.69           O  
-ATOM    578  CB  PHE C 104      -2.557  81.159  77.159  1.00 36.25           C  
-ATOM    579  CG  PHE C 104      -2.726  80.169  76.040  1.00 35.48           C  
-ATOM    580  CD1 PHE C 104      -2.929  78.812  76.316  1.00 33.06           C  
-ATOM    581  CD2 PHE C 104      -2.610  80.577  74.708  1.00 32.97           C  
-ATOM    582  CE1 PHE C 104      -3.013  77.864  75.279  1.00 28.78           C  
-ATOM    583  CE2 PHE C 104      -2.689  79.646  73.663  1.00 30.73           C  
-ATOM    584  CZ  PHE C 104      -2.891  78.283  73.949  1.00 30.78           C  
-ATOM    585  N   VAL C 105       0.078  82.400  76.251  1.00 38.72           N  
-ATOM    586  CA  VAL C 105       1.072  82.639  75.209  1.00 38.70           C  
-ATOM    587  C   VAL C 105       2.490  82.323  75.679  1.00 39.13           C  
-ATOM    588  O   VAL C 105       3.285  81.706  74.957  1.00 37.63           O  
-ATOM    589  CB  VAL C 105       1.006  84.105  74.720  1.00 40.79           C  
-ATOM    590  CG1 VAL C 105       2.079  84.365  73.677  1.00 35.16           C  
-ATOM    591  CG2 VAL C 105      -0.376  84.388  74.137  1.00 39.73           C  
-ATOM    592  N   GLU C 106       2.808  82.754  76.892  1.00 39.72           N  
-ATOM    593  CA  GLU C 106       4.128  82.508  77.457  1.00 39.81           C  
-ATOM    594  C   GLU C 106       4.330  80.994  77.536  1.00 36.64           C  
-ATOM    595  O   GLU C 106       5.383  80.474  77.171  1.00 38.03           O  
-ATOM    596  CB  GLU C 106       4.220  83.118  78.856  1.00 43.08           C  
-ATOM    597  CG  GLU C 106       5.634  83.195  79.411  1.00 54.81           C  
-ATOM    598  CD  GLU C 106       5.666  83.608  80.879  1.00 65.29           C  
-ATOM    599  OE1 GLU C 106       5.225  82.809  81.740  1.00 62.46           O  
-ATOM    600  OE2 GLU C 106       6.131  84.736  81.165  1.00 69.97           O  
-ATOM    601  N   ALA C 107       3.305  80.297  78.006  1.00 33.50           N  
-ATOM    602  CA  ALA C 107       3.344  78.842  78.133  1.00 34.13           C  
-ATOM    603  C   ALA C 107       3.573  78.150  76.781  1.00 34.35           C  
-ATOM    604  O   ALA C 107       4.277  77.137  76.702  1.00 35.32           O  
-ATOM    605  CB  ALA C 107       2.045  78.349  78.756  1.00 30.84           C  
-ATOM    606  N   MET C 108       2.984  78.707  75.726  1.00 33.91           N  
-ATOM    607  CA  MET C 108       3.116  78.154  74.378  1.00 33.69           C  
-ATOM    608  C   MET C 108       4.541  78.247  73.883  1.00 32.28           C  
-ATOM    609  O   MET C 108       5.072  77.293  73.328  1.00 32.93           O  
-ATOM    610  CB  MET C 108       2.187  78.881  73.398  1.00 31.35           C  
-ATOM    611  CG  MET C 108       0.727  78.489  73.528  1.00 33.26           C  
-ATOM    612  SD  MET C 108       0.465  76.765  73.060  1.00 36.63           S  
-ATOM    613  CE  MET C 108       0.684  76.917  71.227  1.00 30.28           C  
-ATOM    614  N   ILE C 109       5.155  79.408  74.071  1.00 35.76           N  
-ATOM    615  CA  ILE C 109       6.535  79.612  73.649  1.00 36.52           C  
-ATOM    616  C   ILE C 109       7.439  78.613  74.374  1.00 37.30           C  
-ATOM    617  O   ILE C 109       8.317  78.010  73.764  1.00 37.65           O  
-ATOM    618  CB  ILE C 109       7.006  81.058  73.959  1.00 41.12           C  
-ATOM    619  CG1 ILE C 109       6.192  82.054  73.136  1.00 45.48           C  
-ATOM    620  CG2 ILE C 109       8.493  81.215  73.644  1.00 38.52           C  
-ATOM    621  CD1 ILE C 109       6.350  81.883  71.633  1.00 51.15           C  
-ATOM    622  N   ARG C 110       7.223  78.438  75.676  1.00 37.77           N  
-ATOM    623  CA  ARG C 110       8.025  77.486  76.445  1.00 38.16           C  
-ATOM    624  C   ARG C 110       7.873  76.066  75.902  1.00 36.60           C  
-ATOM    625  O   ARG C 110       8.857  75.349  75.758  1.00 37.38           O  
-ATOM    626  CB  ARG C 110       7.638  77.499  77.931  1.00 40.82           C  
-ATOM    627  CG  ARG C 110       8.249  78.638  78.738  1.00 47.67           C  
-ATOM    628  CD  ARG C 110       8.244  78.312  80.237  1.00 51.28           C  
-ATOM    629  NE  ARG C 110       6.895  78.237  80.799  1.00 51.89           N  
-ATOM    630  CZ  ARG C 110       6.121  79.297  81.017  1.00 49.23           C  
-ATOM    631  NH1 ARG C 110       6.565  80.514  80.724  1.00 49.96           N  
-ATOM    632  NH2 ARG C 110       4.901  79.140  81.517  1.00 45.41           N  
-ATOM    633  N   GLN C 111       6.643  75.655  75.614  1.00 35.33           N  
-ATOM    634  CA  GLN C 111       6.419  74.317  75.076  1.00 35.79           C  
-ATOM    635  C   GLN C 111       7.117  74.155  73.725  1.00 36.26           C  
-ATOM    636  O   GLN C 111       7.629  73.081  73.404  1.00 34.93           O  
-ATOM    637  CB  GLN C 111       4.924  74.045  74.909  1.00 38.18           C  
-ATOM    638  CG  GLN C 111       4.615  72.693  74.252  1.00 41.17           C  
-ATOM    639  CD  GLN C 111       5.187  71.512  75.034  1.00 47.61           C  
-ATOM    640  OE1 GLN C 111       4.925  71.365  76.227  1.00 45.86           O  
-ATOM    641  NE2 GLN C 111       5.967  70.666  74.361  1.00 46.18           N  
-ATOM    642  N   LEU C 112       7.148  75.226  72.939  1.00 36.06           N  
-ATOM    643  CA  LEU C 112       7.782  75.172  71.626  1.00 37.65           C  
-ATOM    644  C   LEU C 112       9.271  74.869  71.729  1.00 39.72           C  
-ATOM    645  O   LEU C 112       9.779  73.999  71.017  1.00 39.46           O  
-ATOM    646  CB  LEU C 112       7.569  76.490  70.873  1.00 35.20           C  
-ATOM    647  CG  LEU C 112       8.316  76.699  69.551  1.00 37.73           C  
-ATOM    648  CD1 LEU C 112       8.027  75.554  68.590  1.00 30.21           C  
-ATOM    649  CD2 LEU C 112       7.888  78.034  68.943  1.00 39.05           C  
-ATOM    650  N   LYS C 113       9.972  75.585  72.607  1.00 41.00           N  
-ATOM    651  CA  LYS C 113      11.407  75.366  72.790  1.00 41.86           C  
-ATOM    652  C   LYS C 113      11.659  73.942  73.269  1.00 41.58           C  
-ATOM    653  O   LYS C 113      12.582  73.269  72.802  1.00 41.54           O  
-ATOM    654  CB  LYS C 113      11.983  76.363  73.805  1.00 45.63           C  
-ATOM    655  CG  LYS C 113      11.814  77.820  73.395  1.00 51.26           C  
-ATOM    656  CD  LYS C 113      12.395  78.788  74.426  1.00 59.33           C  
-ATOM    657  CE  LYS C 113      13.910  78.655  74.537  1.00 60.95           C  
-ATOM    658  NZ  LYS C 113      14.591  78.920  73.233  1.00 66.66           N  
-ATOM    659  N   GLU C 114      10.841  73.479  74.205  1.00 39.81           N  
-ATOM    660  CA  GLU C 114      10.997  72.123  74.701  1.00 40.10           C  
-ATOM    661  C   GLU C 114      10.730  71.092  73.598  1.00 39.34           C  
-ATOM    662  O   GLU C 114      11.378  70.041  73.552  1.00 36.67           O  
-ATOM    663  CB  GLU C 114      10.069  71.888  75.896  1.00 39.40           C  
-ATOM    664  CG  GLU C 114      10.799  71.913  77.241  1.00 54.38           C  
-ATOM    665  CD  GLU C 114      11.791  73.072  77.365  1.00 60.33           C  
-ATOM    666  OE1 GLU C 114      11.352  74.245  77.454  1.00 62.28           O  
-ATOM    667  OE2 GLU C 114      13.015  72.803  77.366  1.00 61.51           O  
-ATOM    668  N   SER C 115       9.782  71.386  72.708  1.00 38.03           N  
-ATOM    669  CA  SER C 115       9.469  70.460  71.623  1.00 35.69           C  
-ATOM    670  C   SER C 115      10.630  70.363  70.650  1.00 34.01           C  
-ATOM    671  O   SER C 115      10.996  69.275  70.219  1.00 33.95           O  
-ATOM    672  CB  SER C 115       8.201  70.893  70.886  1.00 36.27           C  
-ATOM    673  OG  SER C 115       7.049  70.572  71.648  1.00 37.34           O  
-ATOM    674  N   LEU C 116      11.208  71.508  70.313  1.00 34.81           N  
-ATOM    675  CA  LEU C 116      12.346  71.563  69.402  1.00 38.54           C  
-ATOM    676  C   LEU C 116      13.552  70.870  70.049  1.00 41.63           C  
-ATOM    677  O   LEU C 116      14.271  70.091  69.408  1.00 40.96           O  
-ATOM    678  CB  LEU C 116      12.686  73.028  69.090  1.00 36.98           C  
-ATOM    679  CG  LEU C 116      11.615  73.820  68.333  1.00 36.88           C  
-ATOM    680  CD1 LEU C 116      11.891  75.317  68.409  1.00 36.60           C  
-ATOM    681  CD2 LEU C 116      11.585  73.352  66.890  1.00 36.00           C  
-ATOM    682  N   LYS C 117      13.759  71.159  71.331  1.00 43.64           N  
-ATOM    683  CA  LYS C 117      14.862  70.581  72.087  1.00 44.48           C  
-ATOM    684  C   LYS C 117      14.776  69.056  72.091  1.00 43.93           C  
-ATOM    685  O   LYS C 117      15.796  68.368  72.036  1.00 46.37           O  
-ATOM    686  CB  LYS C 117      14.837  71.128  73.519  1.00 50.03           C  
-ATOM    687  CG  LYS C 117      15.967  70.644  74.423  1.00 58.41           C  
-ATOM    688  CD  LYS C 117      15.926  71.370  75.766  1.00 64.05           C  
-ATOM    689  CE  LYS C 117      16.962  70.821  76.738  1.00 68.04           C  
-ATOM    690  NZ  LYS C 117      18.353  70.989  76.234  1.00 69.16           N  
-ATOM    691  N   ALA C 118      13.558  68.529  72.134  1.00 41.27           N  
-ATOM    692  CA  ALA C 118      13.341  67.085  72.150  1.00 38.47           C  
-ATOM    693  C   ALA C 118      13.234  66.490  70.743  1.00 37.84           C  
-ATOM    694  O   ALA C 118      12.845  65.327  70.577  1.00 37.26           O  
-ATOM    695  CB  ALA C 118      12.072  66.761  72.953  1.00 36.73           C  
-ATOM    696  N   ASN C 119      13.578  67.284  69.734  1.00 37.06           N  
-ATOM    697  CA  ASN C 119      13.504  66.836  68.345  1.00 36.15           C  
-ATOM    698  C   ASN C 119      12.079  66.499  67.907  1.00 34.48           C  
-ATOM    699  O   ASN C 119      11.881  65.674  67.018  1.00 33.31           O  
-ATOM    700  CB  ASN C 119      14.391  65.600  68.105  1.00 36.76           C  
-ATOM    701  CG  ASN C 119      15.872  65.899  68.237  1.00 36.78           C  
-ATOM    702  OD1 ASN C 119      16.377  66.880  67.688  1.00 37.99           O  
-ATOM    703  ND2 ASN C 119      16.581  65.037  68.954  1.00 39.13           N  
-ATOM    704  N   ASN C 120      11.085  67.113  68.541  1.00 32.86           N  
-ATOM    705  CA  ASN C 120       9.701  66.872  68.156  1.00 33.67           C  
-ATOM    706  C   ASN C 120       9.254  67.982  67.212  1.00 32.49           C  
-ATOM    707  O   ASN C 120       8.279  68.694  67.475  1.00 34.13           O  
-ATOM    708  CB  ASN C 120       8.795  66.835  69.382  1.00 35.37           C  
-ATOM    709  CG  ASN C 120       9.036  65.613  70.232  1.00 46.55           C  
-ATOM    710  OD1 ASN C 120       8.965  64.482  69.745  1.00 50.10           O  
-ATOM    711  ND2 ASN C 120       9.325  65.828  71.513  1.00 44.81           N  
-ATOM    712  N   TYR C 121       9.977  68.116  66.110  1.00 31.70           N  
-ATOM    713  CA  TYR C 121       9.682  69.141  65.124  1.00 33.49           C  
-ATOM    714  C   TYR C 121       8.299  68.973  64.538  1.00 32.71           C  
-ATOM    715  O   TYR C 121       7.646  69.958  64.190  1.00 34.01           O  
-ATOM    716  CB  TYR C 121      10.740  69.120  64.020  1.00 34.13           C  
-ATOM    717  CG  TYR C 121      12.089  69.608  64.499  1.00 35.28           C  
-ATOM    718  CD1 TYR C 121      12.350  70.972  64.647  1.00 36.49           C  
-ATOM    719  CD2 TYR C 121      13.086  68.703  64.864  1.00 35.03           C  
-ATOM    720  CE1 TYR C 121      13.571  71.426  65.152  1.00 37.48           C  
-ATOM    721  CE2 TYR C 121      14.309  69.143  65.370  1.00 39.35           C  
-ATOM    722  CZ  TYR C 121      14.544  70.504  65.514  1.00 41.23           C  
-ATOM    723  OH  TYR C 121      15.742  70.937  66.032  1.00 42.00           O  
-ATOM    724  N   ASN C 122       7.832  67.734  64.448  1.00 33.81           N  
-ATOM    725  CA  ASN C 122       6.511  67.506  63.887  1.00 34.93           C  
-ATOM    726  C   ASN C 122       5.447  68.195  64.734  1.00 34.62           C  
-ATOM    727  O   ASN C 122       4.556  68.855  64.191  1.00 34.79           O  
-ATOM    728  CB  ASN C 122       6.240  65.999  63.736  1.00 36.43           C  
-ATOM    729  CG  ASN C 122       6.955  65.400  62.519  1.00 41.40           C  
-ATOM    730  OD1 ASN C 122       7.200  64.193  62.447  1.00 47.67           O  
-ATOM    731  ND2 ASN C 122       7.287  66.250  61.556  1.00 45.13           N  
-ATOM    732  N   GLU C 123       5.536  68.066  66.058  1.00 33.44           N  
-ATOM    733  CA  GLU C 123       4.566  68.726  66.938  1.00 32.44           C  
-ATOM    734  C   GLU C 123       4.856  70.223  67.050  1.00 30.17           C  
-ATOM    735  O   GLU C 123       3.956  71.028  67.314  1.00 29.94           O  
-ATOM    736  CB  GLU C 123       4.588  68.113  68.346  1.00 36.32           C  
-ATOM    737  CG  GLU C 123       4.302  66.634  68.369  1.00 39.83           C  
-ATOM    738  CD  GLU C 123       4.009  66.128  69.761  1.00 48.49           C  
-ATOM    739  OE1 GLU C 123       4.703  66.554  70.712  1.00 47.22           O  
-ATOM    740  OE2 GLU C 123       3.085  65.301  69.900  1.00 50.64           O  
-ATOM    741  N   ALA C 124       6.122  70.586  66.871  1.00 28.91           N  
-ATOM    742  CA  ALA C 124       6.534  71.980  66.937  1.00 29.45           C  
-ATOM    743  C   ALA C 124       5.777  72.803  65.891  1.00 30.68           C  
-ATOM    744  O   ALA C 124       5.379  73.943  66.157  1.00 29.96           O  
-ATOM    745  CB  ALA C 124       8.025  72.085  66.699  1.00 26.54           C  
-ATOM    746  N   VAL C 125       5.572  72.217  64.709  1.00 30.20           N  
-ATOM    747  CA  VAL C 125       4.864  72.908  63.636  1.00 30.42           C  
-ATOM    748  C   VAL C 125       3.446  73.251  64.046  1.00 28.81           C  
-ATOM    749  O   VAL C 125       2.983  74.350  63.779  1.00 27.56           O  
-ATOM    750  CB  VAL C 125       4.782  72.071  62.332  1.00 30.45           C  
-ATOM    751  CG1 VAL C 125       4.151  72.912  61.220  1.00 33.12           C  
-ATOM    752  CG2 VAL C 125       6.159  71.628  61.902  1.00 38.07           C  
-ATOM    753  N   TYR C 126       2.748  72.323  64.698  1.00 27.40           N  
-ATOM    754  CA  TYR C 126       1.381  72.625  65.097  1.00 27.94           C  
-ATOM    755  C   TYR C 126       1.357  73.800  66.073  1.00 31.42           C  
-ATOM    756  O   TYR C 126       0.428  74.609  66.044  1.00 32.01           O  
-ATOM    757  CB  TYR C 126       0.699  71.400  65.714  1.00 25.70           C  
-ATOM    758  CG  TYR C 126       0.800  70.152  64.869  1.00 29.53           C  
-ATOM    759  CD1 TYR C 126       0.639  70.202  63.479  1.00 33.00           C  
-ATOM    760  CD2 TYR C 126       1.066  68.915  65.456  1.00 27.99           C  
-ATOM    761  CE1 TYR C 126       0.749  69.039  62.694  1.00 31.63           C  
-ATOM    762  CE2 TYR C 126       1.171  67.752  64.685  1.00 31.22           C  
-ATOM    763  CZ  TYR C 126       1.015  67.822  63.310  1.00 30.72           C  
-ATOM    764  OH  TYR C 126       1.134  66.678  62.558  1.00 33.81           O  
-ATOM    765  N   LEU C 127       2.377  73.903  66.928  1.00 31.83           N  
-ATOM    766  CA  LEU C 127       2.434  75.005  67.881  1.00 32.45           C  
-ATOM    767  C   LEU C 127       2.672  76.319  67.130  1.00 31.96           C  
-ATOM    768  O   LEU C 127       2.050  77.328  67.432  1.00 32.41           O  
-ATOM    769  CB  LEU C 127       3.545  74.775  68.917  1.00 31.74           C  
-ATOM    770  CG  LEU C 127       3.392  73.556  69.845  1.00 33.66           C  
-ATOM    771  CD1 LEU C 127       4.638  73.424  70.725  1.00 36.44           C  
-ATOM    772  CD2 LEU C 127       2.154  73.711  70.716  1.00 31.83           C  
-ATOM    773  N   VAL C 128       3.581  76.311  66.162  1.00 33.10           N  
-ATOM    774  CA  VAL C 128       3.845  77.518  65.385  1.00 32.74           C  
-ATOM    775  C   VAL C 128       2.569  77.976  64.669  1.00 32.06           C  
-ATOM    776  O   VAL C 128       2.288  79.171  64.602  1.00 31.89           O  
-ATOM    777  CB  VAL C 128       4.961  77.304  64.335  1.00 31.39           C  
-ATOM    778  CG1 VAL C 128       5.073  78.542  63.437  1.00 30.87           C  
-ATOM    779  CG2 VAL C 128       6.296  77.059  65.032  1.00 32.75           C  
-ATOM    780  N   ARG C 129       1.800  77.032  64.138  1.00 30.21           N  
-ATOM    781  CA  ARG C 129       0.557  77.379  63.457  1.00 30.52           C  
-ATOM    782  C   ARG C 129      -0.476  77.901  64.439  1.00 32.47           C  
-ATOM    783  O   ARG C 129      -1.292  78.770  64.090  1.00 32.03           O  
-ATOM    784  CB  ARG C 129      -0.033  76.168  62.743  1.00 31.32           C  
-ATOM    785  CG  ARG C 129       0.730  75.736  61.517  1.00 36.09           C  
-ATOM    786  CD  ARG C 129       0.007  74.617  60.784  1.00 33.57           C  
-ATOM    787  NE  ARG C 129       0.905  73.986  59.826  1.00 30.00           N  
-ATOM    788  CZ  ARG C 129       0.785  72.737  59.402  1.00 30.48           C  
-ATOM    789  NH1 ARG C 129      -0.207  71.974  59.848  1.00 32.76           N  
-ATOM    790  NH2 ARG C 129       1.683  72.244  58.561  1.00 32.13           N  
-ATOM    791  N   PHE C 130      -0.465  77.359  65.657  1.00 29.71           N  
-ATOM    792  CA  PHE C 130      -1.418  77.795  66.659  1.00 31.30           C  
-ATOM    793  C   PHE C 130      -1.130  79.243  67.058  1.00 33.41           C  
-ATOM    794  O   PHE C 130      -2.056  80.037  67.255  1.00 33.77           O  
-ATOM    795  CB  PHE C 130      -1.381  76.885  67.894  1.00 29.98           C  
-ATOM    796  CG  PHE C 130      -2.579  77.043  68.782  1.00 32.39           C  
-ATOM    797  CD1 PHE C 130      -2.650  78.084  69.705  1.00 31.54           C  
-ATOM    798  CD2 PHE C 130      -3.660  76.182  68.662  1.00 26.02           C  
-ATOM    799  CE1 PHE C 130      -3.792  78.260  70.496  1.00 28.39           C  
-ATOM    800  CE2 PHE C 130      -4.799  76.351  69.446  1.00 30.43           C  
-ATOM    801  CZ  PHE C 130      -4.864  77.393  70.364  1.00 28.65           C  
-ATOM    802  N   LEU C 131       0.151  79.581  67.172  1.00 32.96           N  
-ATOM    803  CA  LEU C 131       0.553  80.936  67.531  1.00 34.56           C  
-ATOM    804  C   LEU C 131       0.196  81.910  66.405  1.00 36.03           C  
-ATOM    805  O   LEU C 131      -0.211  83.051  66.656  1.00 36.06           O  
-ATOM    806  CB  LEU C 131       2.055  80.984  67.781  1.00 34.31           C  
-ATOM    807  CG  LEU C 131       2.586  80.200  68.989  1.00 33.93           C  
-ATOM    808  CD1 LEU C 131       4.107  80.238  68.996  1.00 28.44           C  
-ATOM    809  CD2 LEU C 131       2.028  80.790  70.268  1.00 34.20           C  
-ATOM    810  N   SER C 132       0.364  81.453  65.169  1.00 34.35           N  
-ATOM    811  CA  SER C 132       0.058  82.265  63.995  1.00 38.19           C  
-ATOM    812  C   SER C 132      -1.428  82.625  63.919  1.00 37.05           C  
-ATOM    813  O   SER C 132      -1.789  83.784  63.777  1.00 37.24           O  
-ATOM    814  CB  SER C 132       0.458  81.515  62.720  1.00 36.70           C  
-ATOM    815  OG  SER C 132       1.841  81.217  62.726  1.00 37.67           O  
-ATOM    816  N   ASP C 133      -2.289  81.624  64.015  1.00 38.36           N  
-ATOM    817  CA  ASP C 133      -3.716  81.873  63.935  1.00 38.22           C  
-ATOM    818  C   ASP C 133      -4.188  82.729  65.102  1.00 40.31           C  
-ATOM    819  O   ASP C 133      -5.208  83.408  64.993  1.00 39.82           O  
-ATOM    820  CB  ASP C 133      -4.490  80.552  63.899  1.00 34.16           C  
-ATOM    821  CG  ASP C 133      -5.897  80.716  63.343  1.00 35.77           C  
-ATOM    822  OD1 ASP C 133      -6.029  81.304  62.248  1.00 35.59           O  
-ATOM    823  OD2 ASP C 133      -6.866  80.265  63.987  1.00 29.61           O  
-ATOM    824  N   LEU C 134      -3.450  82.700  66.212  1.00 40.75           N  
-ATOM    825  CA  LEU C 134      -3.811  83.497  67.386  1.00 40.89           C  
-ATOM    826  C   LEU C 134      -3.795  84.982  67.045  1.00 41.41           C  
-ATOM    827  O   LEU C 134      -4.460  85.787  67.700  1.00 39.95           O  
-ATOM    828  CB  LEU C 134      -2.851  83.226  68.547  1.00 38.32           C  
-ATOM    829  CG  LEU C 134      -3.194  82.015  69.413  1.00 35.11           C  
-ATOM    830  CD1 LEU C 134      -2.141  81.861  70.491  1.00 35.55           C  
-ATOM    831  CD2 LEU C 134      -4.575  82.202  70.035  1.00 34.87           C  
-ATOM    832  N   VAL C 135      -3.015  85.337  66.027  1.00 42.69           N  
-ATOM    833  CA  VAL C 135      -2.932  86.719  65.564  1.00 44.18           C  
-ATOM    834  C   VAL C 135      -4.320  87.133  65.059  1.00 44.44           C  
-ATOM    835  O   VAL C 135      -4.823  88.212  65.386  1.00 43.52           O  
-ATOM    836  CB  VAL C 135      -1.908  86.853  64.421  1.00 44.75           C  
-ATOM    837  CG1 VAL C 135      -1.938  88.267  63.844  1.00 44.73           C  
-ATOM    838  CG2 VAL C 135      -0.521  86.529  64.945  1.00 44.21           C  
-ATOM    839  N   ASN C 136      -4.943  86.251  64.283  1.00 44.35           N  
-ATOM    840  CA  ASN C 136      -6.275  86.512  63.746  1.00 44.92           C  
-ATOM    841  C   ASN C 136      -7.281  86.672  64.873  1.00 44.54           C  
-ATOM    842  O   ASN C 136      -8.302  87.334  64.711  1.00 46.22           O  
-ATOM    843  CB  ASN C 136      -6.724  85.366  62.833  1.00 41.63           C  
-ATOM    844  CG  ASN C 136      -5.770  85.138  61.673  1.00 43.63           C  
-ATOM    845  OD1 ASN C 136      -5.363  86.085  61.003  1.00 45.62           O  
-ATOM    846  ND2 ASN C 136      -5.412  83.879  61.427  1.00 36.53           N  
-ATOM    847  N   CYS C 137      -6.982  86.061  66.013  1.00 43.99           N  
-ATOM    848  CA  CYS C 137      -7.859  86.108  67.173  1.00 43.90           C  
-ATOM    849  C   CYS C 137      -7.545  87.299  68.076  1.00 43.76           C  
-ATOM    850  O   CYS C 137      -8.107  87.432  69.162  1.00 43.69           O  
-ATOM    851  CB  CYS C 137      -7.737  84.791  67.954  1.00 42.58           C  
-ATOM    852  SG  CYS C 137      -8.270  83.320  67.011  1.00 42.76           S  
-ATOM    853  N   HIS C 138      -6.647  88.161  67.605  1.00 45.07           N  
-ATOM    854  CA  HIS C 138      -6.213  89.349  68.335  1.00 47.41           C  
-ATOM    855  C   HIS C 138      -5.657  89.007  69.710  1.00 46.56           C  
-ATOM    856  O   HIS C 138      -5.930  89.688  70.703  1.00 46.52           O  
-ATOM    857  CB  HIS C 138      -7.362  90.360  68.459  1.00 53.48           C  
-ATOM    858  CG  HIS C 138      -7.791  90.941  67.146  1.00 63.51           C  
-ATOM    859  ND1 HIS C 138      -6.927  91.628  66.318  1.00 67.22           N  
-ATOM    860  CD2 HIS C 138      -8.980  90.901  66.499  1.00 66.66           C  
-ATOM    861  CE1 HIS C 138      -7.565  91.982  65.216  1.00 69.29           C  
-ATOM    862  NE2 HIS C 138      -8.812  91.552  65.300  1.00 69.44           N  
-ATOM    863  N   VAL C 139      -4.871  87.938  69.757  1.00 44.87           N  
-ATOM    864  CA  VAL C 139      -4.246  87.510  70.999  1.00 41.05           C  
-ATOM    865  C   VAL C 139      -2.771  87.842  70.890  1.00 39.11           C  
-ATOM    866  O   VAL C 139      -2.138  88.226  71.872  1.00 39.48           O  
-ATOM    867  CB  VAL C 139      -4.399  85.993  71.227  1.00 41.40           C  
-ATOM    868  CG1 VAL C 139      -3.581  85.565  72.446  1.00 39.26           C  
-ATOM    869  CG2 VAL C 139      -5.862  85.645  71.418  1.00 37.83           C  
-ATOM    870  N   ILE C 140      -2.229  87.694  69.686  1.00 36.03           N  
-ATOM    871  CA  ILE C 140      -0.828  87.989  69.454  1.00 36.85           C  
-ATOM    872  C   ILE C 140      -0.697  89.073  68.405  1.00 39.87           C  
-ATOM    873  O   ILE C 140      -1.409  89.065  67.402  1.00 40.85           O  
-ATOM    874  CB  ILE C 140      -0.051  86.725  69.001  1.00 34.22           C  
-ATOM    875  CG1 ILE C 140      -0.017  85.711  70.156  1.00 32.82           C  
-ATOM    876  CG2 ILE C 140       1.378  87.100  68.564  1.00 27.55           C  
-ATOM    877  CD1 ILE C 140       0.721  84.420  69.833  1.00 29.77           C  
-ATOM    878  N   ALA C 141       0.220  90.005  68.651  1.00 42.24           N  
-ATOM    879  CA  ALA C 141       0.461  91.122  67.741  1.00 43.11           C  
-ATOM    880  C   ALA C 141       1.150  90.642  66.473  1.00 42.74           C  
-ATOM    881  O   ALA C 141       2.138  89.914  66.539  1.00 42.33           O  
-ATOM    882  CB  ALA C 141       1.314  92.189  68.433  1.00 42.38           C  
-ATOM    883  N   ALA C 142       0.630  91.064  65.321  1.00 43.10           N  
-ATOM    884  CA  ALA C 142       1.180  90.671  64.028  1.00 42.93           C  
-ATOM    885  C   ALA C 142       2.689  90.859  63.937  1.00 44.31           C  
-ATOM    886  O   ALA C 142       3.396  89.980  63.445  1.00 46.83           O  
-ATOM    887  CB  ALA C 142       0.484  91.445  62.906  1.00 42.55           C  
-ATOM    888  N   PRO C 143       3.205  92.014  64.394  1.00 44.31           N  
-ATOM    889  CA  PRO C 143       4.647  92.275  64.345  1.00 43.67           C  
-ATOM    890  C   PRO C 143       5.467  91.197  65.052  1.00 44.07           C  
-ATOM    891  O   PRO C 143       6.567  90.852  64.608  1.00 42.74           O  
-ATOM    892  CB  PRO C 143       4.769  93.635  65.030  1.00 43.54           C  
-ATOM    893  CG  PRO C 143       3.502  94.305  64.650  1.00 43.48           C  
-ATOM    894  CD  PRO C 143       2.482  93.210  64.866  1.00 45.12           C  
-ATOM    895  N   SER C 144       4.935  90.685  66.162  1.00 44.92           N  
-ATOM    896  CA  SER C 144       5.616  89.642  66.931  1.00 45.10           C  
-ATOM    897  C   SER C 144       5.859  88.404  66.076  1.00 44.26           C  
-ATOM    898  O   SER C 144       6.974  87.879  66.039  1.00 44.85           O  
-ATOM    899  CB  SER C 144       4.793  89.253  68.163  1.00 46.87           C  
-ATOM    900  OG  SER C 144       4.767  90.295  69.119  1.00 49.39           O  
-ATOM    901  N   MET C 145       4.811  87.939  65.391  1.00 44.51           N  
-ATOM    902  CA  MET C 145       4.917  86.762  64.527  1.00 43.97           C  
-ATOM    903  C   MET C 145       5.845  87.010  63.356  1.00 43.74           C  
-ATOM    904  O   MET C 145       6.598  86.120  62.959  1.00 42.49           O  
-ATOM    905  CB  MET C 145       3.548  86.337  63.985  1.00 45.88           C  
-ATOM    906  CG  MET C 145       2.725  85.443  64.919  1.00 48.65           C  
-ATOM    907  SD  MET C 145       3.655  84.031  65.592  1.00 47.74           S  
-ATOM    908  CE  MET C 145       4.186  83.205  64.116  1.00 44.95           C  
-ATOM    909  N   VAL C 146       5.787  88.214  62.793  1.00 43.24           N  
-ATOM    910  CA  VAL C 146       6.646  88.539  61.663  1.00 42.39           C  
-ATOM    911  C   VAL C 146       8.094  88.476  62.118  1.00 41.89           C  
-ATOM    912  O   VAL C 146       8.958  87.996  61.395  1.00 41.97           O  
-ATOM    913  CB  VAL C 146       6.356  89.959  61.103  1.00 43.81           C  
-ATOM    914  CG1 VAL C 146       7.371  90.307  60.028  1.00 41.29           C  
-ATOM    915  CG2 VAL C 146       4.943  90.023  60.529  1.00 38.34           C  
-ATOM    916  N   ALA C 147       8.349  88.959  63.329  1.00 43.31           N  
-ATOM    917  CA  ALA C 147       9.699  88.963  63.886  1.00 45.02           C  
-ATOM    918  C   ALA C 147      10.196  87.539  64.099  1.00 44.83           C  
-ATOM    919  O   ALA C 147      11.347  87.216  63.800  1.00 46.60           O  
-ATOM    920  CB  ALA C 147       9.716  89.722  65.203  1.00 44.93           C  
-ATOM    921  N   MET C 148       9.328  86.683  64.620  1.00 44.96           N  
-ATOM    922  CA  MET C 148       9.718  85.299  64.851  1.00 44.89           C  
-ATOM    923  C   MET C 148      10.015  84.597  63.529  1.00 43.96           C  
-ATOM    924  O   MET C 148      11.039  83.920  63.395  1.00 41.88           O  
-ATOM    925  CB  MET C 148       8.620  84.544  65.587  1.00 45.63           C  
-ATOM    926  CG  MET C 148       9.005  83.116  65.938  1.00 49.07           C  
-ATOM    927  SD  MET C 148       7.672  82.313  66.804  1.00 50.81           S  
-ATOM    928  CE  MET C 148       7.628  83.321  68.260  1.00 46.38           C  
-ATOM    929  N   PHE C 149       9.125  84.757  62.550  1.00 42.99           N  
-ATOM    930  CA  PHE C 149       9.339  84.117  61.259  1.00 43.30           C  
-ATOM    931  C   PHE C 149      10.657  84.542  60.616  1.00 43.64           C  
-ATOM    932  O   PHE C 149      11.295  83.741  59.932  1.00 43.69           O  
-ATOM    933  CB  PHE C 149       8.158  84.377  60.314  1.00 41.75           C  
-ATOM    934  CG  PHE C 149       6.940  83.540  60.627  1.00 42.50           C  
-ATOM    935  CD1 PHE C 149       7.074  82.193  60.968  1.00 44.66           C  
-ATOM    936  CD2 PHE C 149       5.667  84.088  60.577  1.00 41.05           C  
-ATOM    937  CE1 PHE C 149       5.957  81.410  61.257  1.00 42.42           C  
-ATOM    938  CE2 PHE C 149       4.540  83.314  60.863  1.00 43.84           C  
-ATOM    939  CZ  PHE C 149       4.686  81.970  61.204  1.00 42.73           C  
-ATOM    940  N   GLU C 150      11.068  85.791  60.837  1.00 43.80           N  
-ATOM    941  CA  GLU C 150      12.335  86.274  60.292  1.00 44.64           C  
-ATOM    942  C   GLU C 150      13.461  85.407  60.867  1.00 42.86           C  
-ATOM    943  O   GLU C 150      14.376  84.999  60.154  1.00 41.97           O  
-ATOM    944  CB  GLU C 150      12.574  87.751  60.671  1.00 48.53           C  
-ATOM    945  CG  GLU C 150      11.492  88.729  60.186  1.00 56.17           C  
-ATOM    946  CD  GLU C 150      11.741  90.187  60.610  1.00 63.64           C  
-ATOM    947  OE1 GLU C 150      11.917  90.449  61.821  1.00 65.94           O  
-ATOM    948  OE2 GLU C 150      11.752  91.077  59.730  1.00 65.14           O  
-ATOM    949  N   ASN C 151      13.384  85.125  62.164  1.00 43.64           N  
-ATOM    950  CA  ASN C 151      14.396  84.304  62.814  1.00 44.09           C  
-ATOM    951  C   ASN C 151      14.337  82.866  62.308  1.00 43.77           C  
-ATOM    952  O   ASN C 151      15.342  82.157  62.317  1.00 43.59           O  
-ATOM    953  CB  ASN C 151      14.222  84.347  64.332  1.00 47.47           C  
-ATOM    954  CG  ASN C 151      14.390  85.749  64.893  1.00 51.56           C  
-ATOM    955  OD1 ASN C 151      15.354  86.443  64.569  1.00 52.91           O  
-ATOM    956  ND2 ASN C 151      13.454  86.170  65.740  1.00 54.03           N  
-ATOM    957  N   PHE C 152      13.157  82.437  61.869  1.00 42.01           N  
-ATOM    958  CA  PHE C 152      13.008  81.091  61.325  1.00 40.05           C  
-ATOM    959  C   PHE C 152      13.768  81.027  60.001  1.00 39.44           C  
-ATOM    960  O   PHE C 152      14.613  80.151  59.798  1.00 38.53           O  
-ATOM    961  CB  PHE C 152      11.532  80.762  61.089  1.00 37.62           C  
-ATOM    962  CG  PHE C 152      10.850  80.122  62.263  1.00 37.66           C  
-ATOM    963  CD1 PHE C 152      11.062  80.585  63.560  1.00 37.86           C  
-ATOM    964  CD2 PHE C 152       9.965  79.066  62.069  1.00 37.09           C  
-ATOM    965  CE1 PHE C 152      10.402  80.007  64.644  1.00 37.31           C  
-ATOM    966  CE2 PHE C 152       9.301  78.484  63.144  1.00 35.51           C  
-ATOM    967  CZ  PHE C 152       9.521  78.957  64.436  1.00 36.40           C  
-ATOM    968  N   VAL C 153      13.481  81.972  59.108  1.00 39.18           N  
-ATOM    969  CA  VAL C 153      14.137  82.001  57.804  1.00 38.69           C  
-ATOM    970  C   VAL C 153      15.643  82.217  57.940  1.00 40.03           C  
-ATOM    971  O   VAL C 153      16.414  81.729  57.120  1.00 40.12           O  
-ATOM    972  CB  VAL C 153      13.518  83.098  56.891  1.00 41.39           C  
-ATOM    973  CG1 VAL C 153      14.148  83.059  55.504  1.00 39.58           C  
-ATOM    974  CG2 VAL C 153      12.013  82.879  56.779  1.00 40.46           C  
-ATOM    975  N   SER C 154      16.073  82.925  58.980  1.00 41.78           N  
-ATOM    976  CA  SER C 154      17.509  83.143  59.160  1.00 44.82           C  
-ATOM    977  C   SER C 154      18.233  81.809  59.331  1.00 44.90           C  
-ATOM    978  O   SER C 154      19.439  81.720  59.099  1.00 45.50           O  
-ATOM    979  CB  SER C 154      17.788  84.036  60.373  1.00 46.25           C  
-ATOM    980  OG  SER C 154      17.452  83.385  61.587  1.00 58.12           O  
-ATOM    981  N   VAL C 155      17.503  80.767  59.728  1.00 43.33           N  
-ATOM    982  CA  VAL C 155      18.118  79.451  59.907  1.00 41.52           C  
-ATOM    983  C   VAL C 155      18.731  78.958  58.592  1.00 42.26           C  
-ATOM    984  O   VAL C 155      19.706  78.209  58.595  1.00 41.68           O  
-ATOM    985  CB  VAL C 155      17.085  78.409  60.425  1.00 37.76           C  
-ATOM    986  CG1 VAL C 155      17.649  76.997  60.318  1.00 36.50           C  
-ATOM    987  CG2 VAL C 155      16.733  78.711  61.880  1.00 37.57           C  
-ATOM    988  N   THR C 156      18.159  79.380  57.468  1.00 43.18           N  
-ATOM    989  CA  THR C 156      18.674  78.981  56.159  1.00 45.43           C  
-ATOM    990  C   THR C 156      20.029  79.637  55.906  1.00 48.52           C  
-ATOM    991  O   THR C 156      20.736  79.277  54.964  1.00 48.61           O  
-ATOM    992  CB  THR C 156      17.723  79.399  55.021  1.00 46.41           C  
-ATOM    993  OG1 THR C 156      17.564  80.823  55.026  1.00 41.86           O  
-ATOM    994  CG2 THR C 156      16.365  78.738  55.192  1.00 42.98           C  
-ATOM    995  N   GLN C 157      20.381  80.607  56.747  1.00 51.07           N  
-ATOM    996  CA  GLN C 157      21.653  81.310  56.614  1.00 54.54           C  
-ATOM    997  C   GLN C 157      22.771  80.588  57.358  1.00 54.76           C  
-ATOM    998  O   GLN C 157      23.943  80.744  57.021  1.00 55.40           O  
-ATOM    999  CB  GLN C 157      21.535  82.748  57.136  1.00 59.57           C  
-ATOM   1000  CG  GLN C 157      20.688  83.672  56.268  1.00 63.33           C  
-ATOM   1001  CD  GLN C 157      21.265  83.854  54.877  1.00 70.47           C  
-ATOM   1002  OE1 GLN C 157      21.391  82.894  54.114  1.00 72.64           O  
-ATOM   1003  NE2 GLN C 157      21.623  85.091  54.539  1.00 74.36           N  
-ATOM   1004  N   GLU C 158      22.408  79.801  58.368  1.00 53.70           N  
-ATOM   1005  CA  GLU C 158      23.400  79.055  59.141  1.00 53.95           C  
-ATOM   1006  C   GLU C 158      24.262  78.226  58.195  1.00 53.95           C  
-ATOM   1007  O   GLU C 158      23.766  77.685  57.209  1.00 54.33           O  
-ATOM   1008  CB  GLU C 158      22.715  78.123  60.141  1.00 50.78           C  
-ATOM   1009  CG  GLU C 158      21.725  78.803  61.063  1.00 48.34           C  
-ATOM   1010  CD  GLU C 158      21.102  77.839  62.050  1.00 48.52           C  
-ATOM   1011  OE1 GLU C 158      20.230  78.268  62.831  1.00 49.73           O  
-ATOM   1012  OE2 GLU C 158      21.489  76.651  62.048  1.00 47.44           O  
-ATOM   1013  N   GLU C 159      25.552  78.126  58.498  1.00 54.82           N  
-ATOM   1014  CA  GLU C 159      26.464  77.355  57.660  1.00 54.43           C  
-ATOM   1015  C   GLU C 159      26.803  75.995  58.254  1.00 52.07           C  
-ATOM   1016  O   GLU C 159      26.782  75.811  59.469  1.00 52.20           O  
-ATOM   1017  CB  GLU C 159      27.766  78.129  57.424  1.00 60.27           C  
-ATOM   1018  CG  GLU C 159      27.602  79.427  56.653  1.00 66.67           C  
-ATOM   1019  CD  GLU C 159      28.902  79.893  56.025  1.00 72.63           C  
-ATOM   1020  OE1 GLU C 159      29.367  79.237  55.066  1.00 76.16           O  
-ATOM   1021  OE2 GLU C 159      29.460  80.910  56.493  1.00 77.07           O  
-ATOM   1022  N   ASP C 160      27.120  75.045  57.384  1.00 50.59           N  
-ATOM   1023  CA  ASP C 160      27.487  73.706  57.813  1.00 49.07           C  
-ATOM   1024  C   ASP C 160      26.436  73.044  58.700  1.00 47.13           C  
-ATOM   1025  O   ASP C 160      26.763  72.482  59.744  1.00 45.39           O  
-ATOM   1026  CB  ASP C 160      28.825  73.750  58.554  1.00 53.97           C  
-ATOM   1027  CG  ASP C 160      29.897  74.490  57.777  1.00 57.73           C  
-ATOM   1028  OD1 ASP C 160      30.147  74.121  56.611  1.00 61.60           O  
-ATOM   1029  OD2 ASP C 160      30.493  75.438  58.335  1.00 63.89           O  
-ATOM   1030  N   VAL C 161      25.172  73.136  58.300  1.00 45.99           N  
-ATOM   1031  CA  VAL C 161      24.083  72.497  59.037  1.00 43.50           C  
-ATOM   1032  C   VAL C 161      23.276  71.706  58.014  1.00 42.37           C  
-ATOM   1033  O   VAL C 161      23.191  72.100  56.849  1.00 41.92           O  
-ATOM   1034  CB  VAL C 161      23.167  73.525  59.733  1.00 43.70           C  
-ATOM   1035  CG1 VAL C 161      23.943  74.258  60.811  1.00 42.01           C  
-ATOM   1036  CG2 VAL C 161      22.612  74.500  58.716  1.00 42.00           C  
-ATOM   1037  N   PRO C 162      22.676  70.579  58.429  1.00 40.74           N  
-ATOM   1038  CA  PRO C 162      21.884  69.743  57.517  1.00 39.02           C  
-ATOM   1039  C   PRO C 162      20.804  70.516  56.757  1.00 36.42           C  
-ATOM   1040  O   PRO C 162      20.178  71.415  57.302  1.00 36.40           O  
-ATOM   1041  CB  PRO C 162      21.270  68.698  58.452  1.00 42.45           C  
-ATOM   1042  CG  PRO C 162      22.258  68.641  59.607  1.00 37.36           C  
-ATOM   1043  CD  PRO C 162      22.578  70.085  59.814  1.00 38.48           C  
-ATOM   1044  N   GLN C 163      20.598  70.165  55.494  1.00 35.03           N  
-ATOM   1045  CA  GLN C 163      19.559  70.809  54.698  1.00 32.95           C  
-ATOM   1046  C   GLN C 163      18.205  70.525  55.352  1.00 29.95           C  
-ATOM   1047  O   GLN C 163      17.321  71.384  55.331  1.00 30.94           O  
-ATOM   1048  CB  GLN C 163      19.564  70.276  53.252  1.00 32.64           C  
-ATOM   1049  CG  GLN C 163      18.329  70.667  52.428  1.00 35.17           C  
-ATOM   1050  CD  GLN C 163      18.483  70.401  50.923  1.00 31.84           C  
-ATOM   1051  OE1 GLN C 163      19.389  70.922  50.277  1.00 37.94           O  
-ATOM   1052  NE2 GLN C 163      17.590  69.593  50.370  1.00 30.44           N  
-ATOM   1053  N   VAL C 164      18.042  69.331  55.932  1.00 28.23           N  
-ATOM   1054  CA  VAL C 164      16.778  68.979  56.579  1.00 26.40           C  
-ATOM   1055  C   VAL C 164      16.461  69.875  57.765  1.00 27.99           C  
-ATOM   1056  O   VAL C 164      15.312  69.953  58.198  1.00 27.57           O  
-ATOM   1057  CB  VAL C 164      16.727  67.486  57.044  1.00 27.31           C  
-ATOM   1058  CG1 VAL C 164      16.649  66.578  55.832  1.00 20.52           C  
-ATOM   1059  CG2 VAL C 164      17.935  67.143  57.915  1.00 24.73           C  
-ATOM   1060  N   ARG C 165      17.475  70.553  58.292  1.00 28.71           N  
-ATOM   1061  CA  ARG C 165      17.269  71.480  59.404  1.00 30.94           C  
-ATOM   1062  C   ARG C 165      16.679  72.762  58.812  1.00 30.96           C  
-ATOM   1063  O   ARG C 165      15.670  73.294  59.293  1.00 30.74           O  
-ATOM   1064  CB  ARG C 165      18.603  71.816  60.090  1.00 31.44           C  
-ATOM   1065  CG  ARG C 165      18.500  72.963  61.084  1.00 33.58           C  
-ATOM   1066  CD  ARG C 165      19.874  73.463  61.550  1.00 38.27           C  
-ATOM   1067  NE  ARG C 165      19.727  74.626  62.424  1.00 34.63           N  
-ATOM   1068  CZ  ARG C 165      19.262  74.576  63.667  1.00 36.05           C  
-ATOM   1069  NH1 ARG C 165      18.908  73.415  64.199  1.00 40.95           N  
-ATOM   1070  NH2 ARG C 165      19.110  75.693  64.369  1.00 37.27           N  
-ATOM   1071  N   ARG C 166      17.342  73.256  57.771  1.00 31.51           N  
-ATOM   1072  CA  ARG C 166      16.918  74.470  57.088  1.00 32.72           C  
-ATOM   1073  C   ARG C 166      15.517  74.292  56.516  1.00 31.21           C  
-ATOM   1074  O   ARG C 166      14.697  75.211  56.574  1.00 30.65           O  
-ATOM   1075  CB  ARG C 166      17.895  74.806  55.955  1.00 32.46           C  
-ATOM   1076  CG  ARG C 166      19.336  74.957  56.400  1.00 37.10           C  
-ATOM   1077  CD  ARG C 166      20.194  75.483  55.260  1.00 45.13           C  
-ATOM   1078  NE  ARG C 166      21.612  75.529  55.601  1.00 49.16           N  
-ATOM   1079  CZ  ARG C 166      22.503  74.615  55.224  1.00 54.23           C  
-ATOM   1080  NH1 ARG C 166      22.124  73.577  54.487  1.00 51.20           N  
-ATOM   1081  NH2 ARG C 166      23.777  74.741  55.583  1.00 55.03           N  
-ATOM   1082  N   ASP C 167      15.256  73.114  55.953  1.00 30.13           N  
-ATOM   1083  CA  ASP C 167      13.953  72.819  55.373  1.00 29.10           C  
-ATOM   1084  C   ASP C 167      12.836  72.924  56.404  1.00 31.35           C  
-ATOM   1085  O   ASP C 167      11.794  73.529  56.137  1.00 31.08           O  
-ATOM   1086  CB  ASP C 167      13.916  71.407  54.779  1.00 26.28           C  
-ATOM   1087  CG  ASP C 167      14.772  71.258  53.535  1.00 28.55           C  
-ATOM   1088  OD1 ASP C 167      15.260  72.271  52.993  1.00 26.23           O  
-ATOM   1089  OD2 ASP C 167      14.953  70.109  53.089  1.00 27.65           O  
-ATOM   1090  N   TRP C 168      13.040  72.341  57.584  1.00 29.84           N  
-ATOM   1091  CA  TRP C 168      11.984  72.378  58.577  1.00 29.34           C  
-ATOM   1092  C   TRP C 168      11.529  73.773  58.960  1.00 30.26           C  
-ATOM   1093  O   TRP C 168      10.325  74.023  59.050  1.00 28.52           O  
-ATOM   1094  CB  TRP C 168      12.359  71.638  59.855  1.00 24.87           C  
-ATOM   1095  CG  TRP C 168      11.173  71.578  60.752  1.00 21.88           C  
-ATOM   1096  CD1 TRP C 168      10.131  70.694  60.673  1.00 19.97           C  
-ATOM   1097  CD2 TRP C 168      10.817  72.528  61.766  1.00 29.13           C  
-ATOM   1098  NE1 TRP C 168       9.147  71.045  61.566  1.00 27.24           N  
-ATOM   1099  CE2 TRP C 168       9.541  72.167  62.250  1.00 26.88           C  
-ATOM   1100  CE3 TRP C 168      11.451  73.657  62.307  1.00 31.80           C  
-ATOM   1101  CZ2 TRP C 168       8.883  72.896  63.251  1.00 28.70           C  
-ATOM   1102  CZ3 TRP C 168      10.796  74.383  63.297  1.00 29.89           C  
-ATOM   1103  CH2 TRP C 168       9.525  73.999  63.758  1.00 30.82           C  
-ATOM   1104  N   TYR C 169      12.481  74.668  59.219  1.00 31.13           N  
-ATOM   1105  CA  TYR C 169      12.139  76.034  59.601  1.00 31.98           C  
-ATOM   1106  C   TYR C 169      11.413  76.740  58.461  1.00 31.46           C  
-ATOM   1107  O   TYR C 169      10.504  77.532  58.699  1.00 33.93           O  
-ATOM   1108  CB  TYR C 169      13.401  76.810  60.026  1.00 33.47           C  
-ATOM   1109  CG  TYR C 169      13.765  76.582  61.484  1.00 32.68           C  
-ATOM   1110  CD1 TYR C 169      13.141  77.307  62.494  1.00 33.12           C  
-ATOM   1111  CD2 TYR C 169      14.666  75.577  61.856  1.00 33.94           C  
-ATOM   1112  CE1 TYR C 169      13.396  77.037  63.841  1.00 37.83           C  
-ATOM   1113  CE2 TYR C 169      14.923  75.295  63.199  1.00 32.97           C  
-ATOM   1114  CZ  TYR C 169      14.284  76.027  64.185  1.00 36.32           C  
-ATOM   1115  OH  TYR C 169      14.501  75.740  65.514  1.00 36.88           O  
-ATOM   1116  N   VAL C 170      11.807  76.447  57.226  1.00 30.33           N  
-ATOM   1117  CA  VAL C 170      11.140  77.048  56.080  1.00 31.49           C  
-ATOM   1118  C   VAL C 170       9.704  76.516  56.027  1.00 29.65           C  
-ATOM   1119  O   VAL C 170       8.757  77.278  55.835  1.00 31.98           O  
-ATOM   1120  CB  VAL C 170      11.879  76.725  54.755  1.00 28.27           C  
-ATOM   1121  CG1 VAL C 170      11.025  77.152  53.556  1.00 32.55           C  
-ATOM   1122  CG2 VAL C 170      13.203  77.472  54.720  1.00 31.85           C  
-ATOM   1123  N   TYR C 171       9.551  75.211  56.230  1.00 29.00           N  
-ATOM   1124  CA  TYR C 171       8.235  74.573  56.223  1.00 27.55           C  
-ATOM   1125  C   TYR C 171       7.325  75.107  57.325  1.00 28.97           C  
-ATOM   1126  O   TYR C 171       6.123  75.320  57.110  1.00 30.37           O  
-ATOM   1127  CB  TYR C 171       8.380  73.062  56.395  1.00 25.09           C  
-ATOM   1128  CG  TYR C 171       7.058  72.323  56.401  1.00 27.71           C  
-ATOM   1129  CD1 TYR C 171       6.314  72.177  55.228  1.00 25.10           C  
-ATOM   1130  CD2 TYR C 171       6.557  71.753  57.575  1.00 26.97           C  
-ATOM   1131  CE1 TYR C 171       5.110  71.474  55.218  1.00 26.71           C  
-ATOM   1132  CE2 TYR C 171       5.352  71.054  57.580  1.00 24.56           C  
-ATOM   1133  CZ  TYR C 171       4.634  70.913  56.392  1.00 31.10           C  
-ATOM   1134  OH  TYR C 171       3.457  70.200  56.358  1.00 32.41           O  
-ATOM   1135  N   ALA C 172       7.889  75.301  58.513  1.00 28.24           N  
-ATOM   1136  CA  ALA C 172       7.112  75.798  59.635  1.00 29.92           C  
-ATOM   1137  C   ALA C 172       6.529  77.167  59.272  1.00 30.63           C  
-ATOM   1138  O   ALA C 172       5.368  77.457  59.561  1.00 32.73           O  
-ATOM   1139  CB  ALA C 172       7.990  75.901  60.885  1.00 27.03           C  
-ATOM   1140  N   PHE C 173       7.336  77.993  58.620  1.00 32.03           N  
-ATOM   1141  CA  PHE C 173       6.910  79.328  58.211  1.00 33.03           C  
-ATOM   1142  C   PHE C 173       5.806  79.237  57.164  1.00 32.75           C  
-ATOM   1143  O   PHE C 173       4.669  79.621  57.428  1.00 34.33           O  
-ATOM   1144  CB  PHE C 173       8.127  80.100  57.677  1.00 36.41           C  
-ATOM   1145  CG  PHE C 173       7.789  81.354  56.914  1.00 38.42           C  
-ATOM   1146  CD1 PHE C 173       6.969  82.333  57.466  1.00 39.93           C  
-ATOM   1147  CD2 PHE C 173       8.336  81.570  55.648  1.00 41.31           C  
-ATOM   1148  CE1 PHE C 173       6.698  83.521  56.767  1.00 42.98           C  
-ATOM   1149  CE2 PHE C 173       8.074  82.751  54.938  1.00 42.14           C  
-ATOM   1150  CZ  PHE C 173       7.253  83.729  55.500  1.00 41.34           C  
-ATOM   1151  N   LEU C 174       6.132  78.690  55.996  1.00 33.84           N  
-ATOM   1152  CA  LEU C 174       5.167  78.566  54.903  1.00 32.48           C  
-ATOM   1153  C   LEU C 174       3.837  77.896  55.241  1.00 32.28           C  
-ATOM   1154  O   LEU C 174       2.779  78.403  54.854  1.00 31.74           O  
-ATOM   1155  CB  LEU C 174       5.807  77.834  53.720  1.00 31.01           C  
-ATOM   1156  CG  LEU C 174       7.024  78.513  53.083  1.00 31.58           C  
-ATOM   1157  CD1 LEU C 174       7.522  77.664  51.922  1.00 30.27           C  
-ATOM   1158  CD2 LEU C 174       6.654  79.908  52.599  1.00 32.21           C  
-ATOM   1159  N   SER C 175       3.878  76.769  55.954  1.00 31.65           N  
-ATOM   1160  CA  SER C 175       2.651  76.056  56.290  1.00 29.18           C  
-ATOM   1161  C   SER C 175       1.772  76.814  57.273  1.00 29.98           C  
-ATOM   1162  O   SER C 175       0.634  76.417  57.527  1.00 31.28           O  
-ATOM   1163  CB  SER C 175       2.966  74.639  56.812  1.00 34.19           C  
-ATOM   1164  OG  SER C 175       3.735  74.658  58.000  1.00 31.47           O  
-ATOM   1165  N   SER C 176       2.290  77.917  57.809  1.00 31.02           N  
-ATOM   1166  CA  SER C 176       1.524  78.766  58.723  1.00 32.69           C  
-ATOM   1167  C   SER C 176       0.756  79.837  57.921  1.00 33.38           C  
-ATOM   1168  O   SER C 176      -0.328  80.267  58.306  1.00 32.67           O  
-ATOM   1169  CB  SER C 176       2.455  79.486  59.717  1.00 34.54           C  
-ATOM   1170  OG  SER C 176       3.025  78.600  60.667  1.00 36.58           O  
-ATOM   1171  N   LEU C 177       1.328  80.249  56.796  1.00 35.56           N  
-ATOM   1172  CA  LEU C 177       0.743  81.293  55.951  1.00 36.40           C  
-ATOM   1173  C   LEU C 177      -0.740  81.154  55.580  1.00 37.41           C  
-ATOM   1174  O   LEU C 177      -1.470  82.151  55.574  1.00 38.08           O  
-ATOM   1175  CB  LEU C 177       1.592  81.460  54.685  1.00 36.80           C  
-ATOM   1176  CG  LEU C 177       3.053  81.835  54.977  1.00 39.94           C  
-ATOM   1177  CD1 LEU C 177       3.783  82.217  53.690  1.00 40.03           C  
-ATOM   1178  CD2 LEU C 177       3.086  83.002  55.950  1.00 41.46           C  
-ATOM   1179  N   PRO C 178      -1.209  79.928  55.267  1.00 36.44           N  
-ATOM   1180  CA  PRO C 178      -2.625  79.771  54.909  1.00 35.88           C  
-ATOM   1181  C   PRO C 178      -3.552  80.381  55.960  1.00 36.94           C  
-ATOM   1182  O   PRO C 178      -4.613  80.914  55.636  1.00 38.06           O  
-ATOM   1183  CB  PRO C 178      -2.787  78.254  54.802  1.00 36.83           C  
-ATOM   1184  CG  PRO C 178      -1.423  77.820  54.272  1.00 35.79           C  
-ATOM   1185  CD  PRO C 178      -0.488  78.645  55.142  1.00 36.17           C  
-ATOM   1186  N   TRP C 179      -3.131  80.305  57.219  1.00 35.31           N  
-ATOM   1187  CA  TRP C 179      -3.905  80.827  58.335  1.00 33.54           C  
-ATOM   1188  C   TRP C 179      -3.670  82.307  58.648  1.00 32.78           C  
-ATOM   1189  O   TRP C 179      -4.618  83.055  58.877  1.00 31.23           O  
-ATOM   1190  CB  TRP C 179      -3.609  79.997  59.598  1.00 29.79           C  
-ATOM   1191  CG  TRP C 179      -4.262  78.657  59.580  1.00 24.57           C  
-ATOM   1192  CD1 TRP C 179      -5.521  78.361  59.993  1.00 20.53           C  
-ATOM   1193  CD2 TRP C 179      -3.727  77.449  59.023  1.00 26.32           C  
-ATOM   1194  NE1 TRP C 179      -5.816  77.043  59.725  1.00 24.60           N  
-ATOM   1195  CE2 TRP C 179      -4.730  76.460  59.130  1.00 22.42           C  
-ATOM   1196  CE3 TRP C 179      -2.500  77.107  58.446  1.00 25.34           C  
-ATOM   1197  CZ2 TRP C 179      -4.544  75.148  58.677  1.00 25.85           C  
-ATOM   1198  CZ3 TRP C 179      -2.313  75.803  57.994  1.00 29.12           C  
-ATOM   1199  CH2 TRP C 179      -3.330  74.841  58.115  1.00 27.97           C  
-ATOM   1200  N   VAL C 180      -2.407  82.724  58.643  1.00 32.68           N  
-ATOM   1201  CA  VAL C 180      -2.054  84.090  59.011  1.00 33.42           C  
-ATOM   1202  C   VAL C 180      -1.400  84.953  57.924  1.00 32.98           C  
-ATOM   1203  O   VAL C 180      -1.053  86.105  58.176  1.00 31.90           O  
-ATOM   1204  CB  VAL C 180      -1.101  84.052  60.219  1.00 30.56           C  
-ATOM   1205  CG1 VAL C 180       0.293  83.691  59.748  1.00 31.46           C  
-ATOM   1206  CG2 VAL C 180      -1.107  85.379  60.949  1.00 32.72           C  
-ATOM   1207  N   GLY C 181      -1.223  84.397  56.732  1.00 33.33           N  
-ATOM   1208  CA  GLY C 181      -0.596  85.142  55.654  1.00 36.51           C  
-ATOM   1209  C   GLY C 181      -1.199  86.519  55.420  1.00 38.73           C  
-ATOM   1210  O   GLY C 181      -0.482  87.520  55.396  1.00 39.89           O  
-ATOM   1211  N   LYS C 182      -2.515  86.568  55.250  1.00 39.61           N  
-ATOM   1212  CA  LYS C 182      -3.216  87.819  55.003  1.00 44.16           C  
-ATOM   1213  C   LYS C 182      -2.880  88.859  56.060  1.00 46.28           C  
-ATOM   1214  O   LYS C 182      -2.349  89.927  55.750  1.00 45.72           O  
-ATOM   1215  CB  LYS C 182      -4.730  87.581  54.981  1.00 45.71           C  
-ATOM   1216  CG  LYS C 182      -5.538  88.801  54.566  1.00 52.95           C  
-ATOM   1217  CD  LYS C 182      -7.033  88.510  54.588  1.00 56.90           C  
-ATOM   1218  CE  LYS C 182      -7.843  89.736  54.185  1.00 61.16           C  
-ATOM   1219  NZ  LYS C 182      -9.314  89.517  54.319  1.00 60.01           N  
-ATOM   1220  N   GLU C 183      -3.180  88.539  57.313  1.00 47.47           N  
-ATOM   1221  CA  GLU C 183      -2.914  89.464  58.403  1.00 48.25           C  
-ATOM   1222  C   GLU C 183      -1.475  89.951  58.422  1.00 48.04           C  
-ATOM   1223  O   GLU C 183      -1.230  91.146  58.547  1.00 47.67           O  
-ATOM   1224  CB  GLU C 183      -3.256  88.816  59.744  1.00 52.05           C  
-ATOM   1225  CG  GLU C 183      -3.159  89.755  60.927  1.00 56.00           C  
-ATOM   1226  CD  GLU C 183      -4.023  90.989  60.761  1.00 61.20           C  
-ATOM   1227  OE1 GLU C 183      -5.127  90.870  60.184  1.00 62.41           O  
-ATOM   1228  OE2 GLU C 183      -3.603  92.074  61.215  1.00 62.07           O  
-ATOM   1229  N   LEU C 184      -0.521  89.034  58.283  1.00 48.95           N  
-ATOM   1230  CA  LEU C 184       0.894  89.403  58.314  1.00 50.14           C  
-ATOM   1231  C   LEU C 184       1.304  90.357  57.203  1.00 52.90           C  
-ATOM   1232  O   LEU C 184       2.152  91.230  57.399  1.00 51.28           O  
-ATOM   1233  CB  LEU C 184       1.782  88.160  58.240  1.00 49.28           C  
-ATOM   1234  CG  LEU C 184       1.685  87.137  59.371  1.00 47.08           C  
-ATOM   1235  CD1 LEU C 184       2.820  86.137  59.217  1.00 45.73           C  
-ATOM   1236  CD2 LEU C 184       1.767  87.827  60.723  1.00 44.40           C  
-ATOM   1237  N   TYR C 185       0.709  90.179  56.031  1.00 54.63           N  
-ATOM   1238  CA  TYR C 185       1.028  91.018  54.888  1.00 57.13           C  
-ATOM   1239  C   TYR C 185       0.380  92.399  55.034  1.00 57.60           C  
-ATOM   1240  O   TYR C 185       1.014  93.424  54.779  1.00 57.62           O  
-ATOM   1241  CB  TYR C 185       0.550  90.334  53.607  1.00 58.75           C  
-ATOM   1242  CG  TYR C 185       1.431  90.585  52.413  1.00 61.51           C  
-ATOM   1243  CD1 TYR C 185       2.756  90.152  52.398  1.00 63.83           C  
-ATOM   1244  CD2 TYR C 185       0.940  91.258  51.291  1.00 66.21           C  
-ATOM   1245  CE1 TYR C 185       3.577  90.384  51.294  1.00 66.58           C  
-ATOM   1246  CE2 TYR C 185       1.747  91.495  50.182  1.00 67.38           C  
-ATOM   1247  CZ  TYR C 185       3.064  91.058  50.190  1.00 69.78           C  
-ATOM   1248  OH  TYR C 185       3.864  91.307  49.095  1.00 74.60           O  
-ATOM   1249  N   GLU C 186      -0.878  92.422  55.466  1.00 58.46           N  
-ATOM   1250  CA  GLU C 186      -1.599  93.677  55.642  1.00 58.73           C  
-ATOM   1251  C   GLU C 186      -1.012  94.559  56.743  1.00 58.29           C  
-ATOM   1252  O   GLU C 186      -1.418  95.712  56.891  1.00 59.14           O  
-ATOM   1253  CB  GLU C 186      -3.075  93.401  55.949  1.00 61.26           C  
-ATOM   1254  CG  GLU C 186      -3.784  92.562  54.894  1.00 69.73           C  
-ATOM   1255  CD  GLU C 186      -5.266  92.377  55.182  1.00 74.25           C  
-ATOM   1256  OE1 GLU C 186      -5.621  92.108  56.351  1.00 77.16           O  
-ATOM   1257  OE2 GLU C 186      -6.073  92.493  54.235  1.00 74.77           O  
-ATOM   1258  N   LYS C 187      -0.060  94.026  57.508  1.00 56.51           N  
-ATOM   1259  CA  LYS C 187       0.558  94.784  58.594  1.00 53.92           C  
-ATOM   1260  C   LYS C 187       2.046  95.022  58.401  1.00 52.99           C  
-ATOM   1261  O   LYS C 187       2.572  96.043  58.825  1.00 52.82           O  
-ATOM   1262  CB  LYS C 187       0.344  94.074  59.932  1.00 53.73           C  
-ATOM   1263  CG  LYS C 187      -1.100  94.005  60.386  1.00 55.06           C  
-ATOM   1264  CD  LYS C 187      -1.661  95.389  60.644  1.00 57.68           C  
-ATOM   1265  CE  LYS C 187      -3.075  95.310  61.188  1.00 56.42           C  
-ATOM   1266  NZ  LYS C 187      -3.613  96.667  61.479  1.00 64.68           N  
-ATOM   1267  N   LYS C 188       2.727  94.075  57.769  1.00 53.47           N  
-ATOM   1268  CA  LYS C 188       4.164  94.197  57.539  1.00 54.48           C  
-ATOM   1269  C   LYS C 188       4.556  93.641  56.175  1.00 54.71           C  
-ATOM   1270  O   LYS C 188       5.560  92.943  56.055  1.00 54.77           O  
-ATOM   1271  CB  LYS C 188       4.944  93.447  58.627  1.00 55.11           C  
-ATOM   1272  CG  LYS C 188       4.693  93.931  60.050  1.00 55.74           C  
-ATOM   1273  CD  LYS C 188       5.223  95.340  60.285  1.00 62.51           C  
-ATOM   1274  CE  LYS C 188       4.848  95.836  61.681  1.00 66.74           C  
-ATOM   1275  NZ  LYS C 188       5.301  97.233  61.946  1.00 70.30           N  
-ATOM   1276  N   ASP C 189       3.769  93.952  55.149  1.00 56.00           N  
-ATOM   1277  CA  ASP C 189       4.056  93.463  53.799  1.00 57.21           C  
-ATOM   1278  C   ASP C 189       5.503  93.733  53.418  1.00 55.89           C  
-ATOM   1279  O   ASP C 189       6.108  92.973  52.663  1.00 56.85           O  
-ATOM   1280  CB  ASP C 189       3.124  94.120  52.773  1.00 61.26           C  
-ATOM   1281  CG  ASP C 189       3.299  95.626  52.704  1.00 64.63           C  
-ATOM   1282  OD1 ASP C 189       3.001  96.306  53.712  1.00 66.99           O  
-ATOM   1283  OD2 ASP C 189       3.739  96.124  51.643  1.00 64.94           O  
-ATOM   1284  N   ALA C 190       6.058  94.819  53.945  1.00 55.70           N  
-ATOM   1285  CA  ALA C 190       7.441  95.173  53.660  1.00 54.47           C  
-ATOM   1286  C   ALA C 190       8.367  94.136  54.285  1.00 54.84           C  
-ATOM   1287  O   ALA C 190       9.296  93.647  53.637  1.00 53.47           O  
-ATOM   1288  CB  ALA C 190       7.752  96.553  54.207  1.00 54.49           C  
-ATOM   1289  N   GLU C 191       8.122  93.807  55.550  1.00 54.54           N  
-ATOM   1290  CA  GLU C 191       8.941  92.807  56.219  1.00 53.19           C  
-ATOM   1291  C   GLU C 191       8.709  91.432  55.595  1.00 50.74           C  
-ATOM   1292  O   GLU C 191       9.645  90.652  55.424  1.00 50.25           O  
-ATOM   1293  CB  GLU C 191       8.631  92.755  57.721  1.00 57.48           C  
-ATOM   1294  CG  GLU C 191       9.305  93.848  58.543  1.00 63.24           C  
-ATOM   1295  CD  GLU C 191       8.535  95.156  58.537  1.00 67.61           C  
-ATOM   1296  OE1 GLU C 191       8.231  95.669  57.440  1.00 71.25           O  
-ATOM   1297  OE2 GLU C 191       8.235  95.674  59.634  1.00 72.90           O  
-ATOM   1298  N   MET C 192       7.462  91.141  55.246  1.00 49.05           N  
-ATOM   1299  CA  MET C 192       7.130  89.859  54.639  1.00 49.28           C  
-ATOM   1300  C   MET C 192       7.803  89.645  53.285  1.00 49.37           C  
-ATOM   1301  O   MET C 192       8.106  88.513  52.914  1.00 50.12           O  
-ATOM   1302  CB  MET C 192       5.613  89.717  54.496  1.00 45.74           C  
-ATOM   1303  CG  MET C 192       4.901  89.493  55.817  1.00 46.74           C  
-ATOM   1304  SD  MET C 192       5.496  87.992  56.660  1.00 45.25           S  
-ATOM   1305  CE  MET C 192       4.840  86.734  55.567  1.00 44.46           C  
-ATOM   1306  N   ASP C 193       8.044  90.722  52.546  1.00 49.79           N  
-ATOM   1307  CA  ASP C 193       8.689  90.592  51.245  1.00 50.11           C  
-ATOM   1308  C   ASP C 193      10.170  90.251  51.386  1.00 50.43           C  
-ATOM   1309  O   ASP C 193      10.734  89.556  50.538  1.00 48.40           O  
-ATOM   1310  CB  ASP C 193       8.522  91.878  50.428  1.00 52.89           C  
-ATOM   1311  CG  ASP C 193       7.180  91.950  49.728  1.00 55.13           C  
-ATOM   1312  OD1 ASP C 193       6.905  91.070  48.888  1.00 55.63           O  
-ATOM   1313  OD2 ASP C 193       6.396  92.878  50.013  1.00 60.93           O  
-ATOM   1314  N   ARG C 194      10.805  90.738  52.450  1.00 50.32           N  
-ATOM   1315  CA  ARG C 194      12.221  90.436  52.661  1.00 51.54           C  
-ATOM   1316  C   ARG C 194      12.345  88.950  52.978  1.00 49.99           C  
-ATOM   1317  O   ARG C 194      13.244  88.262  52.491  1.00 49.33           O  
-ATOM   1318  CB  ARG C 194      12.798  91.246  53.826  1.00 54.46           C  
-ATOM   1319  CG  ARG C 194      12.624  92.745  53.702  1.00 62.29           C  
-ATOM   1320  CD  ARG C 194      13.533  93.480  54.675  1.00 67.73           C  
-ATOM   1321  NE  ARG C 194      13.196  94.897  54.780  1.00 73.64           N  
-ATOM   1322  CZ  ARG C 194      12.184  95.372  55.501  1.00 77.14           C  
-ATOM   1323  NH1 ARG C 194      11.410  94.542  56.185  1.00 79.68           N  
-ATOM   1324  NH2 ARG C 194      11.944  96.676  55.539  1.00 80.10           N  
-ATOM   1325  N   ILE C 195      11.425  88.461  53.799  1.00 49.90           N  
-ATOM   1326  CA  ILE C 195      11.412  87.057  54.183  1.00 48.93           C  
-ATOM   1327  C   ILE C 195      11.205  86.161  52.960  1.00 48.43           C  
-ATOM   1328  O   ILE C 195      11.897  85.160  52.792  1.00 48.20           O  
-ATOM   1329  CB  ILE C 195      10.301  86.792  55.220  1.00 49.24           C  
-ATOM   1330  CG1 ILE C 195      10.522  87.681  56.450  1.00 47.44           C  
-ATOM   1331  CG2 ILE C 195      10.287  85.324  55.607  1.00 48.68           C  
-ATOM   1332  CD1 ILE C 195      11.928  87.595  57.034  1.00 51.08           C  
-ATOM   1333  N   PHE C 196      10.263  86.539  52.100  1.00 48.79           N  
-ATOM   1334  CA  PHE C 196       9.965  85.777  50.890  1.00 47.78           C  
-ATOM   1335  C   PHE C 196      11.142  85.746  49.934  1.00 46.52           C  
-ATOM   1336  O   PHE C 196      11.346  84.765  49.218  1.00 47.54           O  
-ATOM   1337  CB  PHE C 196       8.739  86.367  50.195  1.00 50.61           C  
-ATOM   1338  CG  PHE C 196       7.446  85.748  50.634  1.00 54.28           C  
-ATOM   1339  CD1 PHE C 196       6.844  84.757  49.872  1.00 56.83           C  
-ATOM   1340  CD2 PHE C 196       6.844  86.131  51.827  1.00 57.44           C  
-ATOM   1341  CE1 PHE C 196       5.661  84.155  50.293  1.00 57.88           C  
-ATOM   1342  CE2 PHE C 196       5.661  85.533  52.258  1.00 57.00           C  
-ATOM   1343  CZ  PHE C 196       5.070  84.545  51.490  1.00 57.87           C  
-ATOM   1344  N   ALA C 197      11.914  86.826  49.920  1.00 46.54           N  
-ATOM   1345  CA  ALA C 197      13.089  86.914  49.060  1.00 45.48           C  
-ATOM   1346  C   ALA C 197      14.114  85.877  49.507  1.00 43.56           C  
-ATOM   1347  O   ALA C 197      14.633  85.100  48.703  1.00 42.97           O  
-ATOM   1348  CB  ALA C 197      13.702  88.320  49.141  1.00 44.05           C  
-ATOM   1349  N   ASN C 198      14.409  85.888  50.800  1.00 42.46           N  
-ATOM   1350  CA  ASN C 198      15.365  84.956  51.378  1.00 42.70           C  
-ATOM   1351  C   ASN C 198      14.856  83.530  51.245  1.00 41.70           C  
-ATOM   1352  O   ASN C 198      15.620  82.611  50.963  1.00 42.32           O  
-ATOM   1353  CB  ASN C 198      15.591  85.301  52.848  1.00 42.40           C  
-ATOM   1354  CG  ASN C 198      16.264  86.645  53.027  1.00 45.84           C  
-ATOM   1355  OD1 ASN C 198      16.100  87.305  54.053  1.00 51.93           O  
-ATOM   1356  ND2 ASN C 198      17.036  87.054  52.031  1.00 46.00           N  
-ATOM   1357  N   THR C 199      13.557  83.347  51.450  1.00 41.87           N  
-ATOM   1358  CA  THR C 199      12.961  82.023  51.327  1.00 41.76           C  
-ATOM   1359  C   THR C 199      13.133  81.485  49.907  1.00 40.76           C  
-ATOM   1360  O   THR C 199      13.610  80.370  49.712  1.00 40.62           O  
-ATOM   1361  CB  THR C 199      11.465  82.063  51.678  1.00 39.45           C  
-ATOM   1362  OG1 THR C 199      11.318  82.451  53.047  1.00 42.04           O  
-ATOM   1363  CG2 THR C 199      10.825  80.697  51.479  1.00 41.15           C  
-ATOM   1364  N   GLU C 200      12.752  82.287  48.917  1.00 41.49           N  
-ATOM   1365  CA  GLU C 200      12.865  81.873  47.525  1.00 42.01           C  
-ATOM   1366  C   GLU C 200      14.306  81.575  47.143  1.00 42.33           C  
-ATOM   1367  O   GLU C 200      14.583  80.573  46.489  1.00 42.97           O  
-ATOM   1368  CB  GLU C 200      12.288  82.955  46.606  1.00 45.07           C  
-ATOM   1369  CG  GLU C 200      12.373  82.630  45.124  1.00 46.62           C  
-ATOM   1370  CD  GLU C 200      11.453  83.501  44.286  1.00 53.44           C  
-ATOM   1371  OE1 GLU C 200      11.501  84.741  44.433  1.00 53.29           O  
-ATOM   1372  OE2 GLU C 200      10.679  82.942  43.477  1.00 60.10           O  
-ATOM   1373  N   SER C 201      15.231  82.440  47.552  1.00 42.68           N  
-ATOM   1374  CA  SER C 201      16.633  82.211  47.231  1.00 42.95           C  
-ATOM   1375  C   SER C 201      17.066  80.861  47.801  1.00 42.30           C  
-ATOM   1376  O   SER C 201      17.759  80.095  47.133  1.00 40.24           O  
-ATOM   1377  CB  SER C 201      17.511  83.332  47.797  1.00 45.53           C  
-ATOM   1378  OG  SER C 201      17.445  83.380  49.212  1.00 52.92           O  
-ATOM   1379  N   TYR C 202      16.652  80.568  49.033  1.00 41.41           N  
-ATOM   1380  CA  TYR C 202      17.002  79.289  49.658  1.00 40.95           C  
-ATOM   1381  C   TYR C 202      16.440  78.100  48.883  1.00 39.40           C  
-ATOM   1382  O   TYR C 202      17.158  77.161  48.568  1.00 39.86           O  
-ATOM   1383  CB  TYR C 202      16.485  79.212  51.101  1.00 40.01           C  
-ATOM   1384  CG  TYR C 202      16.661  77.831  51.710  1.00 41.56           C  
-ATOM   1385  CD1 TYR C 202      17.935  77.315  51.963  1.00 44.33           C  
-ATOM   1386  CD2 TYR C 202      15.560  77.007  51.949  1.00 41.62           C  
-ATOM   1387  CE1 TYR C 202      18.109  76.009  52.427  1.00 43.44           C  
-ATOM   1388  CE2 TYR C 202      15.723  75.698  52.413  1.00 41.78           C  
-ATOM   1389  CZ  TYR C 202      17.001  75.206  52.645  1.00 43.22           C  
-ATOM   1390  OH  TYR C 202      17.179  73.906  53.063  1.00 41.31           O  
-ATOM   1391  N   LEU C 203      15.145  78.139  48.592  1.00 40.44           N  
-ATOM   1392  CA  LEU C 203      14.494  77.055  47.865  1.00 41.10           C  
-ATOM   1393  C   LEU C 203      15.173  76.790  46.531  1.00 42.34           C  
-ATOM   1394  O   LEU C 203      15.221  75.652  46.056  1.00 41.26           O  
-ATOM   1395  CB  LEU C 203      13.016  77.392  47.649  1.00 40.43           C  
-ATOM   1396  CG  LEU C 203      12.223  77.468  48.958  1.00 39.85           C  
-ATOM   1397  CD1 LEU C 203      10.825  78.002  48.700  1.00 40.93           C  
-ATOM   1398  CD2 LEU C 203      12.158  76.085  49.579  1.00 35.26           C  
-ATOM   1399  N   LYS C 204      15.711  77.847  45.935  1.00 44.25           N  
-ATOM   1400  CA  LYS C 204      16.388  77.719  44.658  1.00 45.33           C  
-ATOM   1401  C   LYS C 204      17.698  76.952  44.754  1.00 44.63           C  
-ATOM   1402  O   LYS C 204      18.110  76.322  43.792  1.00 43.92           O  
-ATOM   1403  CB  LYS C 204      16.646  79.099  44.050  1.00 47.67           C  
-ATOM   1404  CG  LYS C 204      15.411  79.751  43.455  1.00 50.17           C  
-ATOM   1405  CD  LYS C 204      15.753  81.100  42.849  1.00 57.11           C  
-ATOM   1406  CE  LYS C 204      14.562  81.700  42.124  1.00 61.01           C  
-ATOM   1407  NZ  LYS C 204      14.180  80.889  40.933  1.00 65.10           N  
-ATOM   1408  N   ARG C 205      18.353  76.978  45.908  1.00 46.27           N  
-ATOM   1409  CA  ARG C 205      19.623  76.269  46.021  1.00 47.34           C  
-ATOM   1410  C   ARG C 205      19.572  74.887  46.674  1.00 47.04           C  
-ATOM   1411  O   ARG C 205      20.595  74.200  46.736  1.00 47.42           O  
-ATOM   1412  CB  ARG C 205      20.665  77.152  46.724  1.00 50.47           C  
-ATOM   1413  CG  ARG C 205      20.238  77.761  48.055  1.00 56.68           C  
-ATOM   1414  CD  ARG C 205      21.259  78.808  48.513  1.00 59.19           C  
-ATOM   1415  NE  ARG C 205      20.824  79.535  49.703  1.00 60.39           N  
-ATOM   1416  CZ  ARG C 205      20.877  79.052  50.941  1.00 61.49           C  
-ATOM   1417  NH1 ARG C 205      21.357  77.836  51.170  1.00 61.43           N  
-ATOM   1418  NH2 ARG C 205      20.436  79.786  51.953  1.00 62.35           N  
-ATOM   1419  N   ARG C 206      18.394  74.468  47.136  1.00 45.23           N  
-ATOM   1420  CA  ARG C 206      18.258  73.151  47.772  1.00 42.78           C  
-ATOM   1421  C   ARG C 206      18.627  72.004  46.835  1.00 41.19           C  
-ATOM   1422  O   ARG C 206      18.475  72.114  45.623  1.00 40.86           O  
-ATOM   1423  CB  ARG C 206      16.819  72.923  48.255  1.00 40.52           C  
-ATOM   1424  CG  ARG C 206      16.356  73.876  49.334  1.00 40.04           C  
-ATOM   1425  CD  ARG C 206      14.907  73.613  49.714  1.00 36.72           C  
-ATOM   1426  NE  ARG C 206      14.708  72.304  50.332  1.00 35.34           N  
-ATOM   1427  CZ  ARG C 206      13.930  71.343  49.832  1.00 36.73           C  
-ATOM   1428  NH1 ARG C 206      13.275  71.527  48.688  1.00 30.49           N  
-ATOM   1429  NH2 ARG C 206      13.770  70.206  50.502  1.00 29.46           N  
-ATOM   1430  N   GLN C 207      19.115  70.908  47.410  1.00 40.01           N  
-ATOM   1431  CA  GLN C 207      19.461  69.709  46.647  1.00 40.66           C  
-ATOM   1432  C   GLN C 207      18.170  68.902  46.541  1.00 39.58           C  
-ATOM   1433  O   GLN C 207      17.335  68.966  47.443  1.00 40.30           O  
-ATOM   1434  CB  GLN C 207      20.503  68.876  47.397  1.00 41.84           C  
-ATOM   1435  CG  GLN C 207      21.815  69.589  47.653  1.00 47.07           C  
-ATOM   1436  CD  GLN C 207      22.546  69.952  46.376  1.00 50.15           C  
-ATOM   1437  OE1 GLN C 207      22.801  71.129  46.107  1.00 55.62           O  
-ATOM   1438  NE2 GLN C 207      22.887  68.942  45.576  1.00 51.23           N  
-ATOM   1439  N   LYS C 208      18.012  68.137  45.464  1.00 37.87           N  
-ATOM   1440  CA  LYS C 208      16.806  67.334  45.258  1.00 36.98           C  
-ATOM   1441  C   LYS C 208      17.170  65.877  45.056  1.00 37.08           C  
-ATOM   1442  O   LYS C 208      16.381  65.085  44.534  1.00 38.97           O  
-ATOM   1443  CB  LYS C 208      16.044  67.837  44.035  1.00 39.14           C  
-ATOM   1444  CG  LYS C 208      15.711  69.320  44.082  1.00 40.89           C  
-ATOM   1445  CD  LYS C 208      14.643  69.621  45.127  1.00 44.93           C  
-ATOM   1446  CE  LYS C 208      14.287  71.102  45.132  1.00 45.69           C  
-ATOM   1447  NZ  LYS C 208      13.900  71.572  43.773  1.00 42.97           N  
-ATOM   1448  N   THR C 209      18.374  65.531  45.483  1.00 35.61           N  
-ATOM   1449  CA  THR C 209      18.890  64.177  45.355  1.00 33.38           C  
-ATOM   1450  C   THR C 209      17.935  63.121  45.912  1.00 31.56           C  
-ATOM   1451  O   THR C 209      17.894  61.988  45.429  1.00 30.25           O  
-ATOM   1452  CB  THR C 209      20.238  64.060  46.086  1.00 34.61           C  
-ATOM   1453  OG1 THR C 209      21.066  65.172  45.725  1.00 36.77           O  
-ATOM   1454  CG2 THR C 209      20.934  62.761  45.723  1.00 32.92           C  
-ATOM   1455  N   HIS C 210      17.165  63.497  46.929  1.00 31.95           N  
-ATOM   1456  CA  HIS C 210      16.220  62.574  47.562  1.00 30.74           C  
-ATOM   1457  C   HIS C 210      14.960  62.246  46.760  1.00 30.35           C  
-ATOM   1458  O   HIS C 210      14.431  61.142  46.849  1.00 32.08           O  
-ATOM   1459  CB  HIS C 210      15.784  63.123  48.922  1.00 30.69           C  
-ATOM   1460  CG  HIS C 210      15.252  64.522  48.873  1.00 28.38           C  
-ATOM   1461  ND1 HIS C 210      16.066  65.622  48.719  1.00 28.35           N  
-ATOM   1462  CD2 HIS C 210      13.986  65.002  48.971  1.00 27.06           C  
-ATOM   1463  CE1 HIS C 210      15.330  66.720  48.729  1.00 27.91           C  
-ATOM   1464  NE2 HIS C 210      14.064  66.371  48.882  1.00 30.63           N  
-ATOM   1465  N   VAL C 211      14.487  63.207  45.980  1.00 33.06           N  
-ATOM   1466  CA  VAL C 211      13.256  63.049  45.203  1.00 33.09           C  
-ATOM   1467  C   VAL C 211      13.004  61.698  44.550  1.00 32.07           C  
-ATOM   1468  O   VAL C 211      11.996  61.052  44.829  1.00 32.57           O  
-ATOM   1469  CB  VAL C 211      13.151  64.147  44.126  1.00 33.25           C  
-ATOM   1470  CG1 VAL C 211      11.914  63.928  43.263  1.00 28.94           C  
-ATOM   1471  CG2 VAL C 211      13.103  65.504  44.800  1.00 31.30           C  
-ATOM   1472  N   PRO C 212      13.918  61.239  43.684  1.00 32.97           N  
-ATOM   1473  CA  PRO C 212      13.720  59.948  43.015  1.00 31.07           C  
-ATOM   1474  C   PRO C 212      13.474  58.771  43.953  1.00 30.76           C  
-ATOM   1475  O   PRO C 212      12.840  57.789  43.573  1.00 32.97           O  
-ATOM   1476  CB  PRO C 212      15.009  59.776  42.200  1.00 33.96           C  
-ATOM   1477  CG  PRO C 212      15.468  61.184  41.974  1.00 32.31           C  
-ATOM   1478  CD  PRO C 212      15.225  61.812  43.319  1.00 35.37           C  
-ATOM   1479  N   MET C 213      13.982  58.854  45.175  1.00 29.74           N  
-ATOM   1480  CA  MET C 213      13.795  57.752  46.115  1.00 29.78           C  
-ATOM   1481  C   MET C 213      12.452  57.795  46.865  1.00 27.45           C  
-ATOM   1482  O   MET C 213      12.038  56.799  47.446  1.00 27.24           O  
-ATOM   1483  CB  MET C 213      14.944  57.730  47.130  1.00 27.84           C  
-ATOM   1484  CG  MET C 213      14.798  56.676  48.214  1.00 32.28           C  
-ATOM   1485  SD  MET C 213      16.170  56.666  49.384  1.00 39.09           S  
-ATOM   1486  CE  MET C 213      17.147  55.354  48.693  1.00 25.49           C  
-ATOM   1487  N   LEU C 214      11.768  58.934  46.831  1.00 28.15           N  
-ATOM   1488  CA  LEU C 214      10.500  59.089  47.552  1.00 27.73           C  
-ATOM   1489  C   LEU C 214       9.225  59.178  46.691  1.00 28.84           C  
-ATOM   1490  O   LEU C 214       8.110  59.225  47.233  1.00 26.69           O  
-ATOM   1491  CB  LEU C 214      10.591  60.328  48.444  1.00 27.39           C  
-ATOM   1492  CG  LEU C 214      11.808  60.395  49.379  1.00 22.16           C  
-ATOM   1493  CD1 LEU C 214      11.843  61.745  50.082  1.00 22.87           C  
-ATOM   1494  CD2 LEU C 214      11.751  59.262  50.376  1.00 19.69           C  
-ATOM   1495  N   GLN C 215       9.382  59.221  45.367  1.00 24.49           N  
-ATOM   1496  CA  GLN C 215       8.229  59.298  44.463  1.00 25.55           C  
-ATOM   1497  C   GLN C 215       7.504  57.967  44.297  1.00 22.89           C  
-ATOM   1498  O   GLN C 215       8.128  56.941  44.048  1.00 23.20           O  
-ATOM   1499  CB  GLN C 215       8.657  59.777  43.074  1.00 25.61           C  
-ATOM   1500  CG  GLN C 215       9.128  61.209  43.006  1.00 23.28           C  
-ATOM   1501  CD  GLN C 215       9.557  61.586  41.605  1.00 28.23           C  
-ATOM   1502  OE1 GLN C 215      10.319  60.857  40.964  1.00 28.84           O  
-ATOM   1503  NE2 GLN C 215       9.073  62.717  41.121  1.00 24.06           N  
-ATOM   1504  N   VAL C 216       6.180  57.963  44.430  1.00 22.87           N  
-ATOM   1505  CA  VAL C 216       5.459  56.703  44.248  1.00 21.45           C  
-ATOM   1506  C   VAL C 216       5.473  56.308  42.747  1.00 23.45           C  
-ATOM   1507  O   VAL C 216       5.426  55.127  42.410  1.00 24.96           O  
-ATOM   1508  CB  VAL C 216       3.995  56.813  44.782  1.00 22.44           C  
-ATOM   1509  CG1 VAL C 216       3.211  55.570  44.409  1.00 16.49           C  
-ATOM   1510  CG2 VAL C 216       4.005  56.992  46.329  1.00 19.88           C  
-ATOM   1511  N   TRP C 217       5.549  57.300  41.860  1.00 24.97           N  
-ATOM   1512  CA  TRP C 217       5.607  57.067  40.400  1.00 29.80           C  
-ATOM   1513  C   TRP C 217       6.716  57.903  39.766  1.00 30.57           C  
-ATOM   1514  O   TRP C 217       6.934  59.042  40.160  1.00 33.21           O  
-ATOM   1515  CB  TRP C 217       4.297  57.471  39.709  1.00 29.76           C  
-ATOM   1516  CG  TRP C 217       3.123  56.596  40.014  1.00 33.93           C  
-ATOM   1517  CD1 TRP C 217       2.875  55.350  39.514  1.00 32.20           C  
-ATOM   1518  CD2 TRP C 217       2.028  56.906  40.885  1.00 31.26           C  
-ATOM   1519  NE1 TRP C 217       1.691  54.864  40.018  1.00 31.16           N  
-ATOM   1520  CE2 TRP C 217       1.150  55.799  40.861  1.00 30.48           C  
-ATOM   1521  CE3 TRP C 217       1.704  58.014  41.682  1.00 25.23           C  
-ATOM   1522  CZ2 TRP C 217      -0.039  55.766  41.602  1.00 29.03           C  
-ATOM   1523  CZ3 TRP C 217       0.518  57.983  42.420  1.00 29.25           C  
-ATOM   1524  CH2 TRP C 217      -0.337  56.866  42.373  1.00 27.67           C  
-ATOM   1525  N   THR C 218       7.414  57.354  38.779  1.00 33.26           N  
-ATOM   1526  CA  THR C 218       8.456  58.129  38.108  1.00 34.32           C  
-ATOM   1527  C   THR C 218       7.840  59.041  37.035  1.00 34.07           C  
-ATOM   1528  O   THR C 218       8.299  60.168  36.811  1.00 33.63           O  
-ATOM   1529  CB  THR C 218       9.523  57.217  37.449  1.00 35.31           C  
-ATOM   1530  OG1 THR C 218       8.899  56.334  36.516  1.00 41.94           O  
-ATOM   1531  CG2 THR C 218      10.248  56.397  38.494  1.00 39.99           C  
-ATOM   1532  N   ALA C 219       6.790  58.556  36.382  1.00 32.94           N  
-ATOM   1533  CA  ALA C 219       6.115  59.336  35.350  1.00 34.20           C  
-ATOM   1534  C   ALA C 219       5.593  60.654  35.905  1.00 35.74           C  
-ATOM   1535  O   ALA C 219       5.131  60.713  37.050  1.00 37.26           O  
-ATOM   1536  CB  ALA C 219       4.958  58.523  34.758  1.00 35.75           C  
-ATOM   1537  N   ASP C 220       5.676  61.722  35.113  1.00 34.82           N  
-ATOM   1538  CA  ASP C 220       5.182  63.007  35.580  1.00 34.00           C  
-ATOM   1539  C   ASP C 220       3.777  63.249  35.022  1.00 34.68           C  
-ATOM   1540  O   ASP C 220       3.239  64.356  35.107  1.00 33.15           O  
-ATOM   1541  CB  ASP C 220       6.139  64.140  35.186  1.00 33.18           C  
-ATOM   1542  CG  ASP C 220       6.067  64.500  33.718  1.00 35.34           C  
-ATOM   1543  OD1 ASP C 220       6.118  63.588  32.865  1.00 37.36           O  
-ATOM   1544  OD2 ASP C 220       5.970  65.709  33.421  1.00 38.88           O  
-ATOM   1545  N   LYS C 221       3.185  62.189  34.478  1.00 33.59           N  
-ATOM   1546  CA  LYS C 221       1.840  62.263  33.918  1.00 35.80           C  
-ATOM   1547  C   LYS C 221       1.003  61.065  34.353  1.00 33.44           C  
-ATOM   1548  O   LYS C 221       1.491  59.932  34.387  1.00 36.38           O  
-ATOM   1549  CB  LYS C 221       1.911  62.304  32.384  1.00 39.20           C  
-ATOM   1550  CG  LYS C 221       1.175  63.472  31.768  1.00 36.97           C  
-ATOM   1551  CD  LYS C 221       1.752  64.808  32.205  1.00 36.02           C  
-ATOM   1552  CE  LYS C 221       0.833  65.934  31.763  1.00 42.99           C  
-ATOM   1553  NZ  LYS C 221       1.257  67.293  32.189  1.00 46.19           N  
-ATOM   1554  N   PRO C 222      -0.273  61.295  34.704  1.00 31.47           N  
-ATOM   1555  CA  PRO C 222      -0.989  62.574  34.707  1.00 30.72           C  
-ATOM   1556  C   PRO C 222      -0.679  63.548  35.847  1.00 31.33           C  
-ATOM   1557  O   PRO C 222      -1.051  64.717  35.771  1.00 32.10           O  
-ATOM   1558  CB  PRO C 222      -2.459  62.146  34.700  1.00 33.82           C  
-ATOM   1559  CG  PRO C 222      -2.441  60.871  35.436  1.00 34.42           C  
-ATOM   1560  CD  PRO C 222      -1.213  60.175  34.891  1.00 31.25           C  
-ATOM   1561  N   HIS C 223       0.012  63.094  36.889  1.00 29.67           N  
-ATOM   1562  CA  HIS C 223       0.318  63.980  38.007  1.00 28.38           C  
-ATOM   1563  C   HIS C 223       1.767  63.879  38.451  1.00 29.45           C  
-ATOM   1564  O   HIS C 223       2.265  62.802  38.769  1.00 30.89           O  
-ATOM   1565  CB  HIS C 223      -0.573  63.660  39.209  1.00 25.63           C  
-ATOM   1566  CG  HIS C 223      -2.037  63.658  38.898  1.00 25.51           C  
-ATOM   1567  ND1 HIS C 223      -2.778  64.815  38.795  1.00 27.00           N  
-ATOM   1568  CD2 HIS C 223      -2.895  62.637  38.666  1.00 19.17           C  
-ATOM   1569  CE1 HIS C 223      -4.032  64.504  38.515  1.00 28.74           C  
-ATOM   1570  NE2 HIS C 223      -4.128  63.189  38.432  1.00 25.33           N  
-ATOM   1571  N   PRO C 224       2.470  65.010  38.458  1.00 27.78           N  
-ATOM   1572  CA  PRO C 224       3.858  64.973  38.888  1.00 29.27           C  
-ATOM   1573  C   PRO C 224       3.826  64.730  40.404  1.00 30.04           C  
-ATOM   1574  O   PRO C 224       2.952  65.250  41.101  1.00 28.10           O  
-ATOM   1575  CB  PRO C 224       4.359  66.378  38.561  1.00 25.93           C  
-ATOM   1576  CG  PRO C 224       3.425  66.847  37.474  1.00 34.47           C  
-ATOM   1577  CD  PRO C 224       2.107  66.342  37.955  1.00 28.14           C  
-ATOM   1578  N   GLN C 225       4.746  63.914  40.898  1.00 29.06           N  
-ATOM   1579  CA  GLN C 225       4.843  63.661  42.329  1.00 27.54           C  
-ATOM   1580  C   GLN C 225       5.920  64.666  42.762  1.00 29.10           C  
-ATOM   1581  O   GLN C 225       7.123  64.414  42.603  1.00 29.74           O  
-ATOM   1582  CB  GLN C 225       5.275  62.215  42.554  1.00 24.67           C  
-ATOM   1583  CG  GLN C 225       4.324  61.183  41.903  1.00 26.47           C  
-ATOM   1584  CD  GLN C 225       2.861  61.327  42.354  1.00 33.29           C  
-ATOM   1585  OE1 GLN C 225       2.523  61.056  43.512  1.00 25.91           O  
-ATOM   1586  NE2 GLN C 225       1.991  61.756  41.432  1.00 24.13           N  
-ATOM   1587  N   GLU C 226       5.474  65.807  43.287  1.00 26.22           N  
-ATOM   1588  CA  GLU C 226       6.353  66.909  43.666  1.00 30.39           C  
-ATOM   1589  C   GLU C 226       6.992  66.889  45.056  1.00 31.68           C  
-ATOM   1590  O   GLU C 226       6.386  66.416  46.021  1.00 29.35           O  
-ATOM   1591  CB  GLU C 226       5.590  68.231  43.547  1.00 28.77           C  
-ATOM   1592  CG  GLU C 226       4.836  68.443  42.244  1.00 40.04           C  
-ATOM   1593  CD  GLU C 226       3.987  69.703  42.285  1.00 42.15           C  
-ATOM   1594  OE1 GLU C 226       4.546  70.776  42.589  1.00 50.52           O  
-ATOM   1595  OE2 GLU C 226       2.765  69.621  42.023  1.00 51.52           O  
-ATOM   1596  N   GLU C 227       8.199  67.456  45.138  1.00 30.92           N  
-ATOM   1597  CA  GLU C 227       8.951  67.572  46.391  1.00 31.64           C  
-ATOM   1598  C   GLU C 227       8.100  68.500  47.266  1.00 31.63           C  
-ATOM   1599  O   GLU C 227       7.694  69.574  46.811  1.00 30.55           O  
-ATOM   1600  CB  GLU C 227      10.323  68.199  46.096  1.00 31.46           C  
-ATOM   1601  CG  GLU C 227      11.452  67.851  47.082  1.00 33.61           C  
-ATOM   1602  CD  GLU C 227      11.468  68.733  48.312  1.00 30.70           C  
-ATOM   1603  OE1 GLU C 227      10.922  69.850  48.240  1.00 29.30           O  
-ATOM   1604  OE2 GLU C 227      12.046  68.314  49.343  1.00 30.58           O  
-ATOM   1605  N   TYR C 228       7.836  68.102  48.513  1.00 29.93           N  
-ATOM   1606  CA  TYR C 228       6.970  68.887  49.401  1.00 26.88           C  
-ATOM   1607  C   TYR C 228       7.196  70.399  49.528  1.00 28.03           C  
-ATOM   1608  O   TYR C 228       6.226  71.161  49.657  1.00 27.42           O  
-ATOM   1609  CB  TYR C 228       6.927  68.261  50.814  1.00 24.99           C  
-ATOM   1610  CG  TYR C 228       8.028  68.676  51.777  1.00 26.17           C  
-ATOM   1611  CD1 TYR C 228       9.363  68.358  51.530  1.00 27.79           C  
-ATOM   1612  CD2 TYR C 228       7.720  69.327  52.973  1.00 32.33           C  
-ATOM   1613  CE1 TYR C 228      10.367  68.672  52.464  1.00 29.58           C  
-ATOM   1614  CE2 TYR C 228       8.708  69.645  53.905  1.00 29.99           C  
-ATOM   1615  CZ  TYR C 228      10.026  69.312  53.645  1.00 30.76           C  
-ATOM   1616  OH  TYR C 228      10.993  69.612  54.574  1.00 29.42           O  
-ATOM   1617  N   LEU C 229       8.447  70.852  49.516  1.00 26.69           N  
-ATOM   1618  CA  LEU C 229       8.687  72.283  49.644  1.00 29.04           C  
-ATOM   1619  C   LEU C 229       8.396  73.044  48.352  1.00 29.60           C  
-ATOM   1620  O   LEU C 229       7.886  74.165  48.395  1.00 31.28           O  
-ATOM   1621  CB  LEU C 229      10.118  72.561  50.119  1.00 27.83           C  
-ATOM   1622  CG  LEU C 229      10.298  72.486  51.641  1.00 33.19           C  
-ATOM   1623  CD1 LEU C 229      11.771  72.637  52.014  1.00 37.07           C  
-ATOM   1624  CD2 LEU C 229       9.469  73.576  52.300  1.00 33.07           C  
-ATOM   1625  N   ASP C 230       8.710  72.446  47.209  1.00 30.13           N  
-ATOM   1626  CA  ASP C 230       8.431  73.112  45.943  1.00 33.17           C  
-ATOM   1627  C   ASP C 230       6.918  73.222  45.776  1.00 31.50           C  
-ATOM   1628  O   ASP C 230       6.412  74.218  45.274  1.00 33.77           O  
-ATOM   1629  CB  ASP C 230       9.052  72.341  44.769  1.00 33.72           C  
-ATOM   1630  CG  ASP C 230      10.570  72.509  44.700  1.00 38.93           C  
-ATOM   1631  OD1 ASP C 230      11.050  73.629  44.965  1.00 41.37           O  
-ATOM   1632  OD2 ASP C 230      11.283  71.538  44.371  1.00 38.31           O  
-ATOM   1633  N   CYS C 231       6.191  72.208  46.227  1.00 31.64           N  
-ATOM   1634  CA  CYS C 231       4.738  72.229  46.113  1.00 30.17           C  
-ATOM   1635  C   CYS C 231       4.144  73.315  46.998  1.00 31.53           C  
-ATOM   1636  O   CYS C 231       3.363  74.149  46.534  1.00 31.22           O  
-ATOM   1637  CB  CYS C 231       4.152  70.877  46.508  1.00 31.27           C  
-ATOM   1638  SG  CYS C 231       2.414  70.676  46.102  1.00 28.14           S  
-ATOM   1639  N   LEU C 232       4.518  73.307  48.274  1.00 30.30           N  
-ATOM   1640  CA  LEU C 232       3.998  74.291  49.213  1.00 28.73           C  
-ATOM   1641  C   LEU C 232       4.309  75.719  48.767  1.00 28.26           C  
-ATOM   1642  O   LEU C 232       3.471  76.614  48.894  1.00 27.26           O  
-ATOM   1643  CB  LEU C 232       4.578  74.036  50.607  1.00 27.67           C  
-ATOM   1644  CG  LEU C 232       4.168  74.971  51.743  1.00 28.11           C  
-ATOM   1645  CD1 LEU C 232       2.653  75.130  51.774  1.00 23.60           C  
-ATOM   1646  CD2 LEU C 232       4.692  74.395  53.066  1.00 28.51           C  
-ATOM   1647  N   TRP C 233       5.516  75.934  48.258  1.00 28.09           N  
-ATOM   1648  CA  TRP C 233       5.911  77.259  47.775  1.00 31.66           C  
-ATOM   1649  C   TRP C 233       4.959  77.702  46.649  1.00 32.81           C  
-ATOM   1650  O   TRP C 233       4.488  78.837  46.631  1.00 33.55           O  
-ATOM   1651  CB  TRP C 233       7.354  77.228  47.260  1.00 32.11           C  
-ATOM   1652  CG  TRP C 233       7.806  78.512  46.601  1.00 38.74           C  
-ATOM   1653  CD1 TRP C 233       8.020  78.718  45.263  1.00 36.87           C  
-ATOM   1654  CD2 TRP C 233       8.096  79.763  47.249  1.00 33.32           C  
-ATOM   1655  NE1 TRP C 233       8.425  80.014  45.042  1.00 36.78           N  
-ATOM   1656  CE2 TRP C 233       8.481  80.676  46.240  1.00 33.20           C  
-ATOM   1657  CE3 TRP C 233       8.066  80.198  48.577  1.00 35.39           C  
-ATOM   1658  CZ2 TRP C 233       8.835  82.002  46.522  1.00 34.32           C  
-ATOM   1659  CZ3 TRP C 233       8.419  81.519  48.859  1.00 38.45           C  
-ATOM   1660  CH2 TRP C 233       8.799  82.403  47.831  1.00 37.99           C  
-ATOM   1661  N   ALA C 234       4.675  76.796  45.723  1.00 32.09           N  
-ATOM   1662  CA  ALA C 234       3.769  77.097  44.618  1.00 35.90           C  
-ATOM   1663  C   ALA C 234       2.361  77.423  45.143  1.00 36.84           C  
-ATOM   1664  O   ALA C 234       1.694  78.324  44.635  1.00 37.66           O  
-ATOM   1665  CB  ALA C 234       3.710  75.910  43.658  1.00 30.78           C  
-ATOM   1666  N   GLN C 235       1.917  76.695  46.166  1.00 36.64           N  
-ATOM   1667  CA  GLN C 235       0.595  76.922  46.742  1.00 34.47           C  
-ATOM   1668  C   GLN C 235       0.533  78.276  47.424  1.00 34.29           C  
-ATOM   1669  O   GLN C 235      -0.489  78.963  47.370  1.00 34.76           O  
-ATOM   1670  CB  GLN C 235       0.260  75.823  47.751  1.00 33.27           C  
-ATOM   1671  CG  GLN C 235       0.331  74.417  47.160  1.00 29.12           C  
-ATOM   1672  CD  GLN C 235       0.212  73.331  48.219  1.00 28.87           C  
-ATOM   1673  OE1 GLN C 235       0.859  73.404  49.257  1.00 29.67           O  
-ATOM   1674  NE2 GLN C 235      -0.611  72.315  47.955  1.00 28.93           N  
-ATOM   1675  N   ILE C 236       1.619  78.648  48.089  1.00 33.79           N  
-ATOM   1676  CA  ILE C 236       1.676  79.931  48.765  1.00 34.59           C  
-ATOM   1677  C   ILE C 236       1.766  81.061  47.726  1.00 36.72           C  
-ATOM   1678  O   ILE C 236       1.234  82.152  47.939  1.00 34.00           O  
-ATOM   1679  CB  ILE C 236       2.890  80.002  49.722  1.00 34.52           C  
-ATOM   1680  CG1 ILE C 236       2.722  78.983  50.857  1.00 33.59           C  
-ATOM   1681  CG2 ILE C 236       3.036  81.412  50.287  1.00 31.13           C  
-ATOM   1682  CD1 ILE C 236       1.496  79.208  51.719  1.00 30.65           C  
-ATOM   1683  N   GLN C 237       2.442  80.796  46.609  1.00 36.25           N  
-ATOM   1684  CA  GLN C 237       2.569  81.796  45.552  1.00 38.97           C  
-ATOM   1685  C   GLN C 237       1.170  82.077  45.019  1.00 38.47           C  
-ATOM   1686  O   GLN C 237       0.790  83.231  44.820  1.00 38.56           O  
-ATOM   1687  CB  GLN C 237       3.463  81.282  44.415  1.00 39.60           C  
-ATOM   1688  CG  GLN C 237       4.951  81.155  44.756  1.00 44.97           C  
-ATOM   1689  CD  GLN C 237       5.659  82.496  44.900  1.00 48.48           C  
-ATOM   1690  OE1 GLN C 237       5.358  83.286  45.798  1.00 51.10           O  
-ATOM   1691  NE2 GLN C 237       6.611  82.755  44.012  1.00 49.29           N  
-ATOM   1692  N   LYS C 238       0.402  81.012  44.805  1.00 39.11           N  
-ATOM   1693  CA  LYS C 238      -0.958  81.150  44.309  1.00 39.86           C  
-ATOM   1694  C   LYS C 238      -1.815  81.904  45.317  1.00 40.79           C  
-ATOM   1695  O   LYS C 238      -2.653  82.720  44.936  1.00 42.24           O  
-ATOM   1696  CB  LYS C 238      -1.571  79.779  44.021  1.00 40.54           C  
-ATOM   1697  CG  LYS C 238      -3.059  79.826  43.744  1.00 42.39           C  
-ATOM   1698  CD  LYS C 238      -3.585  78.483  43.282  1.00 46.89           C  
-ATOM   1699  CE  LYS C 238      -5.104  78.434  43.388  1.00 49.60           C  
-ATOM   1700  NZ  LYS C 238      -5.753  79.633  42.766  1.00 55.97           N  
-ATOM   1701  N   LEU C 239      -1.602  81.636  46.603  1.00 38.75           N  
-ATOM   1702  CA  LEU C 239      -2.361  82.321  47.638  1.00 38.06           C  
-ATOM   1703  C   LEU C 239      -2.024  83.819  47.649  1.00 38.80           C  
-ATOM   1704  O   LEU C 239      -2.918  84.667  47.749  1.00 37.01           O  
-ATOM   1705  CB  LEU C 239      -2.063  81.720  49.018  1.00 37.20           C  
-ATOM   1706  CG  LEU C 239      -2.800  82.388  50.186  1.00 36.45           C  
-ATOM   1707  CD1 LEU C 239      -4.299  82.313  49.949  1.00 32.65           C  
-ATOM   1708  CD2 LEU C 239      -2.435  81.714  51.504  1.00 31.75           C  
-ATOM   1709  N   LYS C 240      -0.735  84.133  47.560  1.00 37.92           N  
-ATOM   1710  CA  LYS C 240      -0.281  85.521  47.565  1.00 42.99           C  
-ATOM   1711  C   LYS C 240      -0.836  86.264  46.344  1.00 44.44           C  
-ATOM   1712  O   LYS C 240      -1.244  87.422  46.439  1.00 44.34           O  
-ATOM   1713  CB  LYS C 240       1.251  85.574  47.558  1.00 43.37           C  
-ATOM   1714  CG  LYS C 240       1.841  86.978  47.655  1.00 49.14           C  
-ATOM   1715  CD  LYS C 240       3.361  86.932  47.592  1.00 51.06           C  
-ATOM   1716  CE  LYS C 240       3.971  88.323  47.619  1.00 54.74           C  
-ATOM   1717  NZ  LYS C 240       5.450  88.285  47.431  1.00 56.60           N  
-ATOM   1718  N   LYS C 241      -0.861  85.582  45.205  1.00 45.26           N  
-ATOM   1719  CA  LYS C 241      -1.373  86.173  43.981  1.00 47.66           C  
-ATOM   1720  C   LYS C 241      -2.859  86.473  44.127  1.00 47.33           C  
-ATOM   1721  O   LYS C 241      -3.365  87.398  43.499  1.00 47.76           O  
-ATOM   1722  CB  LYS C 241      -1.141  85.229  42.804  1.00 46.88           C  
-ATOM   1723  CG  LYS C 241      -1.656  85.750  41.493  1.00 50.05           C  
-ATOM   1724  CD  LYS C 241      -1.373  84.764  40.384  1.00 54.68           C  
-ATOM   1725  CE  LYS C 241      -1.880  85.274  39.048  1.00 55.48           C  
-ATOM   1726  NZ  LYS C 241      -1.520  84.333  37.959  1.00 56.00           N  
-ATOM   1727  N   ASP C 242      -3.547  85.698  44.965  1.00 47.84           N  
-ATOM   1728  CA  ASP C 242      -4.978  85.894  45.193  1.00 45.45           C  
-ATOM   1729  C   ASP C 242      -5.249  86.814  46.366  1.00 44.11           C  
-ATOM   1730  O   ASP C 242      -6.305  86.730  46.985  1.00 44.47           O  
-ATOM   1731  CB  ASP C 242      -5.685  84.562  45.448  1.00 47.86           C  
-ATOM   1732  CG  ASP C 242      -5.572  83.611  44.285  1.00 50.25           C  
-ATOM   1733  OD1 ASP C 242      -5.480  84.093  43.138  1.00 57.36           O  
-ATOM   1734  OD2 ASP C 242      -5.589  82.384  44.515  1.00 51.05           O  
-ATOM   1735  N   ARG C 243      -4.296  87.691  46.667  1.00 45.57           N  
-ATOM   1736  CA  ARG C 243      -4.432  88.643  47.769  1.00 46.62           C  
-ATOM   1737  C   ARG C 243      -4.649  87.945  49.106  1.00 45.52           C  
-ATOM   1738  O   ARG C 243      -5.379  88.447  49.969  1.00 42.42           O  
-ATOM   1739  CB  ARG C 243      -5.599  89.603  47.516  1.00 49.31           C  
-ATOM   1740  CG  ARG C 243      -5.430  90.516  46.318  1.00 58.86           C  
-ATOM   1741  CD  ARG C 243      -6.256  90.030  45.143  1.00 68.10           C  
-ATOM   1742  NE  ARG C 243      -6.843  91.143  44.401  1.00 74.06           N  
-ATOM   1743  CZ  ARG C 243      -7.756  91.975  44.899  1.00 77.16           C  
-ATOM   1744  NH1 ARG C 243      -8.192  91.820  46.145  1.00 76.52           N  
-ATOM   1745  NH2 ARG C 243      -8.234  92.964  44.153  1.00 74.34           N  
-ATOM   1746  N   TRP C 244      -4.019  86.784  49.264  1.00 45.18           N  
-ATOM   1747  CA  TRP C 244      -4.120  86.001  50.489  1.00 44.39           C  
-ATOM   1748  C   TRP C 244      -5.547  85.595  50.833  1.00 45.03           C  
-ATOM   1749  O   TRP C 244      -5.953  85.655  51.993  1.00 46.05           O  
-ATOM   1750  CB  TRP C 244      -3.506  86.770  51.659  1.00 37.73           C  
-ATOM   1751  CG  TRP C 244      -2.081  87.159  51.412  1.00 47.13           C  
-ATOM   1752  CD1 TRP C 244      -1.619  88.390  51.037  1.00 45.90           C  
-ATOM   1753  CD2 TRP C 244      -0.934  86.298  51.461  1.00 49.77           C  
-ATOM   1754  NE1 TRP C 244      -0.257  88.349  50.848  1.00 47.85           N  
-ATOM   1755  CE2 TRP C 244       0.189  87.077  51.101  1.00 50.50           C  
-ATOM   1756  CE3 TRP C 244      -0.747  84.944  51.774  1.00 53.49           C  
-ATOM   1757  CZ2 TRP C 244       1.484  86.547  51.043  1.00 50.97           C  
-ATOM   1758  CZ3 TRP C 244       0.542  84.415  51.714  1.00 52.58           C  
-ATOM   1759  CH2 TRP C 244       1.640  85.220  51.351  1.00 53.11           C  
-ATOM   1760  N   GLN C 245      -6.304  85.172  49.827  1.00 45.75           N  
-ATOM   1761  CA  GLN C 245      -7.677  84.744  50.055  1.00 47.40           C  
-ATOM   1762  C   GLN C 245      -7.880  83.272  49.697  1.00 46.47           C  
-ATOM   1763  O   GLN C 245      -7.709  82.880  48.543  1.00 48.55           O  
-ATOM   1764  CB  GLN C 245      -8.644  85.607  49.233  1.00 51.69           C  
-ATOM   1765  CG  GLN C 245      -8.747  87.064  49.687  1.00 57.35           C  
-ATOM   1766  CD  GLN C 245      -9.589  87.240  50.944  1.00 63.82           C  
-ATOM   1767  OE1 GLN C 245      -9.673  88.338  51.502  1.00 64.25           O  
-ATOM   1768  NE2 GLN C 245     -10.224  86.157  51.392  1.00 66.57           N  
-ATOM   1769  N   GLU C 246      -8.219  82.450  50.684  1.00 44.67           N  
-ATOM   1770  CA  GLU C 246      -8.476  81.037  50.415  1.00 44.10           C  
-ATOM   1771  C   GLU C 246      -9.916  80.724  50.820  1.00 41.80           C  
-ATOM   1772  O   GLU C 246     -10.496  81.421  51.644  1.00 41.17           O  
-ATOM   1773  CB  GLU C 246      -7.457  80.127  51.132  1.00 42.59           C  
-ATOM   1774  CG  GLU C 246      -7.296  80.334  52.622  1.00 43.57           C  
-ATOM   1775  CD  GLU C 246      -8.478  79.826  53.411  1.00 42.40           C  
-ATOM   1776  OE1 GLU C 246      -8.778  78.618  53.317  1.00 43.28           O  
-ATOM   1777  OE2 GLU C 246      -9.105  80.638  54.125  1.00 47.57           O  
-ATOM   1778  N   ARG C 247     -10.486  79.676  50.238  1.00 41.88           N  
-ATOM   1779  CA  ARG C 247     -11.883  79.322  50.476  1.00 42.53           C  
-ATOM   1780  C   ARG C 247     -12.183  78.073  51.295  1.00 42.06           C  
-ATOM   1781  O   ARG C 247     -13.291  77.539  51.201  1.00 41.86           O  
-ATOM   1782  CB  ARG C 247     -12.583  79.176  49.124  1.00 46.25           C  
-ATOM   1783  CG  ARG C 247     -12.721  80.467  48.323  1.00 52.34           C  
-ATOM   1784  CD  ARG C 247     -12.641  80.186  46.822  1.00 58.80           C  
-ATOM   1785  NE  ARG C 247     -13.113  78.842  46.483  1.00 62.21           N  
-ATOM   1786  CZ  ARG C 247     -14.368  78.422  46.628  1.00 63.56           C  
-ATOM   1787  NH1 ARG C 247     -15.297  79.242  47.105  1.00 64.51           N  
-ATOM   1788  NH2 ARG C 247     -14.694  77.175  46.307  1.00 64.38           N  
-ATOM   1789  N   HIS C 248     -11.239  77.608  52.106  1.00 40.18           N  
-ATOM   1790  CA  HIS C 248     -11.504  76.393  52.860  1.00 37.25           C  
-ATOM   1791  C   HIS C 248     -11.536  76.497  54.378  1.00 37.35           C  
-ATOM   1792  O   HIS C 248     -12.474  76.025  55.002  1.00 35.17           O  
-ATOM   1793  CB  HIS C 248     -10.504  75.305  52.477  1.00 35.00           C  
-ATOM   1794  CG  HIS C 248     -10.665  74.052  53.277  1.00 38.28           C  
-ATOM   1795  ND1 HIS C 248     -11.727  73.191  53.096  1.00 28.75           N  
-ATOM   1796  CD2 HIS C 248      -9.967  73.575  54.337  1.00 28.14           C  
-ATOM   1797  CE1 HIS C 248     -11.682  72.244  54.015  1.00 30.48           C  
-ATOM   1798  NE2 HIS C 248     -10.625  72.454  54.782  1.00 29.78           N  
-ATOM   1799  N   ILE C 249     -10.511  77.109  54.960  1.00 39.03           N  
-ATOM   1800  CA  ILE C 249     -10.393  77.223  56.404  1.00 41.11           C  
-ATOM   1801  C   ILE C 249     -11.590  77.817  57.148  1.00 43.25           C  
-ATOM   1802  O   ILE C 249     -12.122  78.870  56.784  1.00 42.87           O  
-ATOM   1803  CB  ILE C 249      -9.118  78.014  56.768  1.00 40.95           C  
-ATOM   1804  CG1 ILE C 249      -7.897  77.326  56.142  1.00 40.57           C  
-ATOM   1805  CG2 ILE C 249      -8.957  78.089  58.279  1.00 41.85           C  
-ATOM   1806  CD1 ILE C 249      -6.629  78.141  56.196  1.00 34.25           C  
-ATOM   1807  N   LEU C 250     -12.024  77.108  58.183  1.00 43.09           N  
-ATOM   1808  CA  LEU C 250     -13.124  77.572  59.008  1.00 43.18           C  
-ATOM   1809  C   LEU C 250     -12.499  78.460  60.068  1.00 43.55           C  
-ATOM   1810  O   LEU C 250     -11.525  78.075  60.715  1.00 43.06           O  
-ATOM   1811  CB  LEU C 250     -13.855  76.397  59.664  1.00 43.70           C  
-ATOM   1812  CG  LEU C 250     -14.804  75.611  58.754  1.00 45.07           C  
-ATOM   1813  CD1 LEU C 250     -15.504  74.540  59.561  1.00 44.31           C  
-ATOM   1814  CD2 LEU C 250     -15.833  76.551  58.129  1.00 45.12           C  
-ATOM   1815  N   ARG C 251     -13.053  79.658  60.229  1.00 41.77           N  
-ATOM   1816  CA  ARG C 251     -12.537  80.614  61.193  1.00 41.60           C  
-ATOM   1817  C   ARG C 251     -13.665  81.129  62.090  1.00 41.87           C  
-ATOM   1818  O   ARG C 251     -14.227  82.197  61.845  1.00 40.72           O  
-ATOM   1819  CB  ARG C 251     -11.880  81.768  60.439  1.00 40.34           C  
-ATOM   1820  CG  ARG C 251     -10.837  81.318  59.420  1.00 37.27           C  
-ATOM   1821  CD  ARG C 251     -10.362  82.482  58.566  1.00 33.35           C  
-ATOM   1822  NE  ARG C 251      -9.465  82.066  57.490  1.00 35.09           N  
-ATOM   1823  CZ  ARG C 251      -8.138  82.018  57.585  1.00 36.17           C  
-ATOM   1824  NH1 ARG C 251      -7.530  82.357  58.719  1.00 38.89           N  
-ATOM   1825  NH2 ARG C 251      -7.414  81.652  56.534  1.00 30.30           N  
-ATOM   1826  N   PRO C 252     -14.007  80.368  63.146  1.00 42.77           N  
-ATOM   1827  CA  PRO C 252     -15.070  80.723  64.092  1.00 43.15           C  
-ATOM   1828  C   PRO C 252     -14.938  82.106  64.709  1.00 43.50           C  
-ATOM   1829  O   PRO C 252     -15.937  82.716  65.087  1.00 45.36           O  
-ATOM   1830  CB  PRO C 252     -14.983  79.614  65.138  1.00 42.58           C  
-ATOM   1831  CG  PRO C 252     -14.535  78.443  64.322  1.00 40.69           C  
-ATOM   1832  CD  PRO C 252     -13.444  79.049  63.477  1.00 39.95           C  
-ATOM   1833  N   TYR C 253     -13.708  82.595  64.807  1.00 43.43           N  
-ATOM   1834  CA  TYR C 253     -13.451  83.900  65.397  1.00 45.47           C  
-ATOM   1835  C   TYR C 253     -13.978  85.083  64.588  1.00 46.78           C  
-ATOM   1836  O   TYR C 253     -14.056  86.205  65.095  1.00 46.02           O  
-ATOM   1837  CB  TYR C 253     -11.953  84.066  65.650  1.00 47.21           C  
-ATOM   1838  CG  TYR C 253     -11.063  83.631  64.510  1.00 45.74           C  
-ATOM   1839  CD1 TYR C 253     -10.804  84.478  63.436  1.00 48.16           C  
-ATOM   1840  CD2 TYR C 253     -10.448  82.381  64.527  1.00 46.35           C  
-ATOM   1841  CE1 TYR C 253      -9.944  84.095  62.407  1.00 46.56           C  
-ATOM   1842  CE2 TYR C 253      -9.587  81.984  63.505  1.00 46.81           C  
-ATOM   1843  CZ  TYR C 253      -9.336  82.845  62.449  1.00 48.58           C  
-ATOM   1844  OH  TYR C 253      -8.463  82.462  61.451  1.00 45.24           O  
-ATOM   1845  N   LEU C 254     -14.334  84.838  63.332  1.00 46.75           N  
-ATOM   1846  CA  LEU C 254     -14.859  85.905  62.497  1.00 48.21           C  
-ATOM   1847  C   LEU C 254     -16.268  86.265  62.955  1.00 48.20           C  
-ATOM   1848  O   LEU C 254     -16.792  87.322  62.614  1.00 48.64           O  
-ATOM   1849  CB  LEU C 254     -14.868  85.480  61.025  1.00 47.59           C  
-ATOM   1850  CG  LEU C 254     -13.491  85.369  60.358  1.00 47.35           C  
-ATOM   1851  CD1 LEU C 254     -13.665  85.036  58.884  1.00 43.14           C  
-ATOM   1852  CD2 LEU C 254     -12.723  86.675  60.518  1.00 41.90           C  
-ATOM   1853  N   ALA C 255     -16.870  85.377  63.740  1.00 48.84           N  
-ATOM   1854  CA  ALA C 255     -18.210  85.596  64.266  1.00 48.43           C  
-ATOM   1855  C   ALA C 255     -18.152  86.367  65.587  1.00 49.32           C  
-ATOM   1856  O   ALA C 255     -19.186  86.740  66.134  1.00 49.22           O  
-ATOM   1857  CB  ALA C 255     -18.913  84.263  64.470  1.00 47.74           C  
-ATOM   1858  N   PHE C 256     -16.943  86.598  66.094  1.00 48.89           N  
-ATOM   1859  CA  PHE C 256     -16.764  87.330  67.347  1.00 49.80           C  
-ATOM   1860  C   PHE C 256     -15.922  88.579  67.131  1.00 49.75           C  
-ATOM   1861  O   PHE C 256     -15.178  88.997  68.011  1.00 49.00           O  
-ATOM   1862  CB  PHE C 256     -16.090  86.446  68.404  1.00 47.23           C  
-ATOM   1863  CG  PHE C 256     -16.855  85.196  68.719  1.00 46.74           C  
-ATOM   1864  CD1 PHE C 256     -16.575  84.008  68.052  1.00 45.14           C  
-ATOM   1865  CD2 PHE C 256     -17.886  85.213  69.649  1.00 46.02           C  
-ATOM   1866  CE1 PHE C 256     -17.308  82.860  68.299  1.00 41.09           C  
-ATOM   1867  CE2 PHE C 256     -18.628  84.064  69.902  1.00 45.98           C  
-ATOM   1868  CZ  PHE C 256     -18.334  82.884  69.223  1.00 48.07           C  
-ATOM   1869  N   ASP C 257     -16.041  89.174  65.953  1.00 51.74           N  
-ATOM   1870  CA  ASP C 257     -15.280  90.374  65.637  1.00 55.03           C  
-ATOM   1871  C   ASP C 257     -15.533  91.491  66.654  1.00 55.59           C  
-ATOM   1872  O   ASP C 257     -14.649  92.305  66.926  1.00 55.10           O  
-ATOM   1873  CB  ASP C 257     -15.623  90.847  64.219  1.00 58.95           C  
-ATOM   1874  CG  ASP C 257     -14.920  92.134  63.847  1.00 61.46           C  
-ATOM   1875  OD1 ASP C 257     -15.391  93.210  64.272  1.00 66.87           O  
-ATOM   1876  OD2 ASP C 257     -13.892  92.073  63.140  1.00 67.05           O  
-ATOM   1877  N   SER C 258     -16.735  91.524  67.221  1.00 55.96           N  
-ATOM   1878  CA  SER C 258     -17.071  92.540  68.213  1.00 58.06           C  
-ATOM   1879  C   SER C 258     -16.147  92.433  69.426  1.00 58.37           C  
-ATOM   1880  O   SER C 258     -15.463  93.390  69.795  1.00 58.37           O  
-ATOM   1881  CB  SER C 258     -18.519  92.369  68.681  1.00 58.72           C  
-ATOM   1882  OG  SER C 258     -19.415  92.377  67.587  1.00 65.13           O  
-ATOM   1883  N   ILE C 259     -16.136  91.250  70.031  1.00 57.94           N  
-ATOM   1884  CA  ILE C 259     -15.334  90.974  71.214  1.00 57.58           C  
-ATOM   1885  C   ILE C 259     -13.831  91.028  70.968  1.00 57.77           C  
-ATOM   1886  O   ILE C 259     -13.107  91.746  71.657  1.00 57.13           O  
-ATOM   1887  CB  ILE C 259     -15.678  89.586  71.780  1.00 58.64           C  
-ATOM   1888  CG1 ILE C 259     -17.196  89.440  71.907  1.00 58.57           C  
-ATOM   1889  CG2 ILE C 259     -15.021  89.404  73.139  1.00 59.83           C  
-ATOM   1890  CD1 ILE C 259     -17.640  88.058  72.331  1.00 58.86           C  
-ATOM   1891  N   LEU C 260     -13.367  90.263  69.987  1.00 57.73           N  
-ATOM   1892  CA  LEU C 260     -11.943  90.204  69.671  1.00 58.48           C  
-ATOM   1893  C   LEU C 260     -11.308  91.530  69.269  1.00 60.10           C  
-ATOM   1894  O   LEU C 260     -10.178  91.825  69.657  1.00 59.63           O  
-ATOM   1895  CB  LEU C 260     -11.705  89.163  68.577  1.00 53.20           C  
-ATOM   1896  CG  LEU C 260     -12.148  87.761  68.998  1.00 50.26           C  
-ATOM   1897  CD1 LEU C 260     -12.082  86.819  67.821  1.00 40.90           C  
-ATOM   1898  CD2 LEU C 260     -11.274  87.278  70.147  1.00 42.63           C  
-ATOM   1899  N   CYS C 261     -12.024  92.331  68.489  1.00 62.93           N  
-ATOM   1900  CA  CYS C 261     -11.485  93.615  68.055  1.00 66.00           C  
-ATOM   1901  C   CYS C 261     -11.160  94.521  69.234  1.00 66.69           C  
-ATOM   1902  O   CYS C 261     -10.162  95.243  69.218  1.00 66.93           O  
-ATOM   1903  CB  CYS C 261     -12.463  94.313  67.109  1.00 67.73           C  
-ATOM   1904  SG  CYS C 261     -12.519  93.557  65.464  1.00 77.17           S  
-ATOM   1905  N   GLU C 262     -12.000  94.475  70.261  1.00 67.99           N  
-ATOM   1906  CA  GLU C 262     -11.781  95.294  71.443  1.00 69.56           C  
-ATOM   1907  C   GLU C 262     -10.916  94.571  72.471  1.00 69.02           C  
-ATOM   1908  O   GLU C 262     -10.912  94.928  73.650  1.00 69.83           O  
-ATOM   1909  CB  GLU C 262     -13.122  95.687  72.070  1.00 72.55           C  
-ATOM   1910  CG  GLU C 262     -13.993  96.534  71.154  1.00 79.12           C  
-ATOM   1911  CD  GLU C 262     -15.117  97.227  71.895  1.00 83.04           C  
-ATOM   1912  OE1 GLU C 262     -15.945  96.526  72.513  1.00 85.96           O  
-ATOM   1913  OE2 GLU C 262     -15.168  98.476  71.857  1.00 84.99           O  
-ATOM   1914  N   ALA C 263     -10.177  93.560  72.017  1.00 67.54           N  
-ATOM   1915  CA  ALA C 263      -9.307  92.788  72.903  1.00 65.18           C  
-ATOM   1916  C   ALA C 263      -7.850  93.176  72.702  1.00 63.01           C  
-ATOM   1917  O   ALA C 263      -7.391  93.336  71.568  1.00 62.63           O  
-ATOM   1918  CB  ALA C 263      -9.485  91.293  72.649  1.00 64.75           C  
-ATOM   1919  N   LEU C 264      -7.124  93.329  73.804  1.00 60.98           N  
-ATOM   1920  CA  LEU C 264      -5.720  93.696  73.725  1.00 59.29           C  
-ATOM   1921  C   LEU C 264      -4.853  92.511  73.330  1.00 57.52           C  
-ATOM   1922  O   LEU C 264      -5.098  91.375  73.732  1.00 56.92           O  
-ATOM   1923  CB  LEU C 264      -5.235  94.281  75.052  1.00 61.93           C  
-ATOM   1924  CG  LEU C 264      -5.533  95.767  75.274  1.00 63.87           C  
-ATOM   1925  CD1 LEU C 264      -7.036  96.007  75.301  1.00 64.96           C  
-ATOM   1926  CD2 LEU C 264      -4.894  96.216  76.576  1.00 64.90           C  
-ATOM   1927  N   GLN C 265      -3.830  92.795  72.536  1.00 55.58           N  
-ATOM   1928  CA  GLN C 265      -2.921  91.771  72.052  1.00 54.65           C  
-ATOM   1929  C   GLN C 265      -1.663  91.662  72.899  1.00 52.57           C  
-ATOM   1930  O   GLN C 265      -1.378  92.528  73.728  1.00 51.36           O  
-ATOM   1931  CB  GLN C 265      -2.551  92.079  70.604  1.00 55.33           C  
-ATOM   1932  CG  GLN C 265      -3.752  92.069  69.680  1.00 62.50           C  
-ATOM   1933  CD  GLN C 265      -3.583  92.995  68.499  1.00 66.47           C  
-ATOM   1934  OE1 GLN C 265      -2.627  92.876  67.731  1.00 69.40           O  
-ATOM   1935  NE2 GLN C 265      -4.513  93.931  68.347  1.00 70.03           N  
-ATOM   1936  N   HIS C 266      -0.914  90.587  72.676  1.00 50.11           N  
-ATOM   1937  CA  HIS C 266       0.320  90.338  73.407  1.00 48.46           C  
-ATOM   1938  C   HIS C 266       1.490  90.244  72.437  1.00 49.16           C  
-ATOM   1939  O   HIS C 266       1.334  89.803  71.295  1.00 48.84           O  
-ATOM   1940  CB  HIS C 266       0.205  89.030  74.181  1.00 45.22           C  
-ATOM   1941  CG  HIS C 266      -0.976  88.965  75.097  1.00 38.00           C  
-ATOM   1942  ND1 HIS C 266      -0.947  89.459  76.383  1.00 33.65           N  
-ATOM   1943  CD2 HIS C 266      -2.211  88.434  74.925  1.00 37.52           C  
-ATOM   1944  CE1 HIS C 266      -2.110  89.228  76.966  1.00 37.51           C  
-ATOM   1945  NE2 HIS C 266      -2.896  88.608  76.103  1.00 39.69           N  
-ATOM   1946  N   ASN C 267       2.663  90.658  72.892  1.00 49.85           N  
-ATOM   1947  CA  ASN C 267       3.851  90.596  72.062  1.00 52.41           C  
-ATOM   1948  C   ASN C 267       4.633  89.320  72.339  1.00 54.10           C  
-ATOM   1949  O   ASN C 267       4.660  88.826  73.462  1.00 53.72           O  
-ATOM   1950  CB  ASN C 267       4.732  91.812  72.324  1.00 53.88           C  
-ATOM   1951  CG  ASN C 267       4.063  93.105  71.916  1.00 55.89           C  
-ATOM   1952  OD1 ASN C 267       3.604  93.239  70.784  1.00 56.64           O  
-ATOM   1953  ND2 ASN C 267       4.003  94.065  72.835  1.00 56.34           N  
-ATOM   1954  N   LEU C 268       5.255  88.771  71.305  1.00 56.32           N  
-ATOM   1955  CA  LEU C 268       6.048  87.563  71.480  1.00 58.32           C  
-ATOM   1956  C   LEU C 268       7.502  87.951  71.695  1.00 59.26           C  
-ATOM   1957  O   LEU C 268       8.074  88.723  70.919  1.00 60.82           O  
-ATOM   1958  CB  LEU C 268       5.943  86.647  70.256  1.00 57.42           C  
-ATOM   1959  CG  LEU C 268       4.629  85.894  70.033  1.00 56.49           C  
-ATOM   1960  CD1 LEU C 268       4.743  85.071  68.763  1.00 55.93           C  
-ATOM   1961  CD2 LEU C 268       4.322  84.994  71.221  1.00 54.14           C  
-ATOM   1962  N   PRO C 269       8.118  87.429  72.763  1.00 59.10           N  
-ATOM   1963  CA  PRO C 269       9.519  87.747  73.040  1.00 58.80           C  
-ATOM   1964  C   PRO C 269      10.379  87.263  71.875  1.00 57.99           C  
-ATOM   1965  O   PRO C 269      10.033  86.286  71.216  1.00 58.15           O  
-ATOM   1966  CB  PRO C 269       9.797  86.972  74.326  1.00 57.47           C  
-ATOM   1967  CG  PRO C 269       8.905  85.775  74.189  1.00 57.94           C  
-ATOM   1968  CD  PRO C 269       7.621  86.400  73.694  1.00 59.33           C  
-ATOM   1969  N   PRO C 270      11.496  87.951  71.595  1.00 57.52           N  
-ATOM   1970  CA  PRO C 270      12.379  87.549  70.497  1.00 57.37           C  
-ATOM   1971  C   PRO C 270      12.622  86.039  70.538  1.00 56.86           C  
-ATOM   1972  O   PRO C 270      12.874  85.467  71.602  1.00 55.47           O  
-ATOM   1973  CB  PRO C 270      13.648  88.350  70.770  1.00 57.89           C  
-ATOM   1974  CG  PRO C 270      13.101  89.623  71.347  1.00 60.31           C  
-ATOM   1975  CD  PRO C 270      12.049  89.113  72.314  1.00 58.38           C  
-ATOM   1976  N   PHE C 271      12.534  85.398  69.380  1.00 56.73           N  
-ATOM   1977  CA  PHE C 271      12.732  83.960  69.304  1.00 56.35           C  
-ATOM   1978  C   PHE C 271      14.069  83.598  68.674  1.00 55.90           C  
-ATOM   1979  O   PHE C 271      14.430  84.106  67.611  1.00 56.07           O  
-ATOM   1980  CB  PHE C 271      11.587  83.315  68.513  1.00 56.84           C  
-ATOM   1981  CG  PHE C 271      11.672  81.816  68.438  1.00 56.05           C  
-ATOM   1982  CD1 PHE C 271      12.405  81.192  67.430  1.00 53.61           C  
-ATOM   1983  CD2 PHE C 271      11.047  81.027  69.399  1.00 56.16           C  
-ATOM   1984  CE1 PHE C 271      12.515  79.803  67.379  1.00 50.67           C  
-ATOM   1985  CE2 PHE C 271      11.152  79.637  69.358  1.00 55.98           C  
-ATOM   1986  CZ  PHE C 271      11.890  79.025  68.343  1.00 54.44           C  
-ATOM   1987  N   THR C 272      14.806  82.722  69.344  1.00 54.67           N  
-ATOM   1988  CA  THR C 272      16.096  82.282  68.840  1.00 54.22           C  
-ATOM   1989  C   THR C 272      16.034  80.773  68.646  1.00 53.26           C  
-ATOM   1990  O   THR C 272      15.876  80.015  69.604  1.00 53.56           O  
-ATOM   1991  CB  THR C 272      17.226  82.618  69.818  1.00 53.94           C  
-ATOM   1992  OG1 THR C 272      17.150  84.003  70.173  1.00 56.59           O  
-ATOM   1993  CG2 THR C 272      18.581  82.344  69.175  1.00 54.80           C  
-ATOM   1994  N   PRO C 273      16.148  80.320  67.392  1.00 51.81           N  
-ATOM   1995  CA  PRO C 273      16.098  78.889  67.103  1.00 51.05           C  
-ATOM   1996  C   PRO C 273      17.235  78.154  67.789  1.00 49.42           C  
-ATOM   1997  O   PRO C 273      18.393  78.546  67.673  1.00 49.20           O  
-ATOM   1998  CB  PRO C 273      16.207  78.844  65.583  1.00 50.98           C  
-ATOM   1999  CG  PRO C 273      17.083  80.021  65.288  1.00 54.73           C  
-ATOM   2000  CD  PRO C 273      16.488  81.087  66.180  1.00 53.48           C  
-ATOM   2001  N   PRO C 274      16.912  77.089  68.535  1.00 49.00           N  
-ATOM   2002  CA  PRO C 274      17.943  76.313  69.229  1.00 47.70           C  
-ATOM   2003  C   PRO C 274      18.990  75.858  68.220  1.00 48.15           C  
-ATOM   2004  O   PRO C 274      18.654  75.281  67.184  1.00 47.25           O  
-ATOM   2005  CB  PRO C 274      17.158  75.148  69.819  1.00 45.08           C  
-ATOM   2006  CG  PRO C 274      15.818  75.775  70.115  1.00 47.97           C  
-ATOM   2007  CD  PRO C 274      15.563  76.596  68.865  1.00 46.41           C  
-ATOM   2008  N   PRO C 275      20.274  76.128  68.502  1.00 47.85           N  
-ATOM   2009  CA  PRO C 275      21.384  75.753  67.622  1.00 47.47           C  
-ATOM   2010  C   PRO C 275      21.410  74.274  67.276  1.00 46.15           C  
-ATOM   2011  O   PRO C 275      20.923  73.438  68.030  1.00 46.50           O  
-ATOM   2012  CB  PRO C 275      22.616  76.171  68.421  1.00 48.22           C  
-ATOM   2013  CG  PRO C 275      22.115  77.357  69.194  1.00 49.31           C  
-ATOM   2014  CD  PRO C 275      20.769  76.867  69.676  1.00 47.68           C  
-ATOM   2015  N   HIS C 276      21.978  73.966  66.119  1.00 44.82           N  
-ATOM   2016  CA  HIS C 276      22.099  72.594  65.661  1.00 44.10           C  
-ATOM   2017  C   HIS C 276      23.153  71.849  66.491  1.00 45.72           C  
-ATOM   2018  O   HIS C 276      24.231  72.383  66.744  1.00 46.46           O  
-ATOM   2019  CB  HIS C 276      22.512  72.578  64.186  1.00 37.71           C  
-ATOM   2020  CG  HIS C 276      22.966  71.236  63.708  1.00 38.74           C  
-ATOM   2021  ND1 HIS C 276      22.118  70.153  63.619  1.00 39.77           N  
-ATOM   2022  CD2 HIS C 276      24.190  70.788  63.343  1.00 35.29           C  
-ATOM   2023  CE1 HIS C 276      22.802  69.094  63.222  1.00 38.91           C  
-ATOM   2024  NE2 HIS C 276      24.062  69.453  63.049  1.00 35.21           N  
-ATOM   2025  N   THR C 277      22.837  70.627  66.917  1.00 46.59           N  
-ATOM   2026  CA  THR C 277      23.781  69.810  67.687  1.00 47.23           C  
-ATOM   2027  C   THR C 277      23.862  68.404  67.081  1.00 49.00           C  
-ATOM   2028  O   THR C 277      22.988  68.003  66.305  1.00 47.94           O  
-ATOM   2029  CB  THR C 277      23.379  69.690  69.188  1.00 44.77           C  
-ATOM   2030  OG1 THR C 277      22.200  68.889  69.321  1.00 44.66           O  
-ATOM   2031  CG2 THR C 277      23.122  71.067  69.783  1.00 46.94           C  
-ATOM   2032  N   GLU C 278      24.915  67.665  67.423  1.00 49.74           N  
-ATOM   2033  CA  GLU C 278      25.085  66.317  66.898  1.00 51.04           C  
-ATOM   2034  C   GLU C 278      23.934  65.415  67.317  1.00 49.13           C  
-ATOM   2035  O   GLU C 278      23.752  64.335  66.767  1.00 50.39           O  
-ATOM   2036  CB  GLU C 278      26.418  65.713  67.360  1.00 55.92           C  
-ATOM   2037  CG  GLU C 278      27.644  66.371  66.731  1.00 62.58           C  
-ATOM   2038  CD  GLU C 278      28.874  65.466  66.726  1.00 69.86           C  
-ATOM   2039  OE1 GLU C 278      28.839  64.418  66.044  1.00 73.19           O  
-ATOM   2040  OE2 GLU C 278      29.874  65.804  67.399  1.00 72.50           O  
-ATOM   2041  N   ASP C 279      23.159  65.859  68.296  1.00 47.37           N  
-ATOM   2042  CA  ASP C 279      22.021  65.078  68.757  1.00 46.63           C  
-ATOM   2043  C   ASP C 279      20.695  65.580  68.158  1.00 43.88           C  
-ATOM   2044  O   ASP C 279      19.615  65.159  68.572  1.00 42.46           O  
-ATOM   2045  CB  ASP C 279      21.964  65.095  70.288  1.00 52.17           C  
-ATOM   2046  CG  ASP C 279      23.013  64.186  70.920  1.00 59.16           C  
-ATOM   2047  OD1 ASP C 279      24.221  64.478  70.792  1.00 61.15           O  
-ATOM   2048  OD2 ASP C 279      22.629  63.167  71.538  1.00 64.34           O  
-ATOM   2049  N   SER C 280      20.788  66.479  67.181  1.00 41.30           N  
-ATOM   2050  CA  SER C 280      19.601  67.029  66.526  1.00 39.21           C  
-ATOM   2051  C   SER C 280      19.074  66.065  65.470  1.00 36.70           C  
-ATOM   2052  O   SER C 280      19.836  65.547  64.648  1.00 36.31           O  
-ATOM   2053  CB  SER C 280      19.924  68.374  65.869  1.00 40.13           C  
-ATOM   2054  OG  SER C 280      20.256  69.359  66.834  1.00 41.32           O  
-ATOM   2055  N   VAL C 281      17.772  65.813  65.502  1.00 35.16           N  
-ATOM   2056  CA  VAL C 281      17.159  64.915  64.531  1.00 34.50           C  
-ATOM   2057  C   VAL C 281      16.023  65.659  63.853  1.00 33.48           C  
-ATOM   2058  O   VAL C 281      15.098  66.129  64.516  1.00 34.20           O  
-ATOM   2059  CB  VAL C 281      16.611  63.651  65.207  1.00 34.47           C  
-ATOM   2060  CG1 VAL C 281      16.051  62.693  64.154  1.00 34.90           C  
-ATOM   2061  CG2 VAL C 281      17.721  62.979  66.017  1.00 33.24           C  
-ATOM   2062  N   TYR C 282      16.092  65.774  62.532  1.00 31.32           N  
-ATOM   2063  CA  TYR C 282      15.057  66.496  61.811  1.00 29.43           C  
-ATOM   2064  C   TYR C 282      14.227  65.588  60.910  1.00 28.16           C  
-ATOM   2065  O   TYR C 282      14.670  64.506  60.521  1.00 28.53           O  
-ATOM   2066  CB  TYR C 282      15.691  67.623  60.985  1.00 30.33           C  
-ATOM   2067  CG  TYR C 282      16.692  68.463  61.757  1.00 32.63           C  
-ATOM   2068  CD1 TYR C 282      18.059  68.171  61.714  1.00 34.66           C  
-ATOM   2069  CD2 TYR C 282      16.275  69.546  62.530  1.00 34.62           C  
-ATOM   2070  CE1 TYR C 282      18.986  68.942  62.422  1.00 32.52           C  
-ATOM   2071  CE2 TYR C 282      17.191  70.325  63.243  1.00 34.72           C  
-ATOM   2072  CZ  TYR C 282      18.546  70.016  63.184  1.00 34.57           C  
-ATOM   2073  OH  TYR C 282      19.457  70.775  63.891  1.00 33.39           O  
-ATOM   2074  N   PRO C 283      13.001  66.018  60.571  1.00 27.27           N  
-ATOM   2075  CA  PRO C 283      12.150  65.199  59.705  1.00 27.23           C  
-ATOM   2076  C   PRO C 283      12.813  64.989  58.334  1.00 25.17           C  
-ATOM   2077  O   PRO C 283      13.540  65.856  57.845  1.00 23.50           O  
-ATOM   2078  CB  PRO C 283      10.868  66.038  59.578  1.00 27.31           C  
-ATOM   2079  CG  PRO C 283      10.863  66.883  60.821  1.00 27.29           C  
-ATOM   2080  CD  PRO C 283      12.323  67.280  60.924  1.00 25.90           C  
-ATOM   2081  N   MET C 284      12.581  63.828  57.741  1.00 24.26           N  
-ATOM   2082  CA  MET C 284      13.101  63.540  56.413  1.00 26.48           C  
-ATOM   2083  C   MET C 284      12.275  64.374  55.435  1.00 27.78           C  
-ATOM   2084  O   MET C 284      11.167  64.826  55.764  1.00 25.21           O  
-ATOM   2085  CB  MET C 284      12.893  62.069  56.038  1.00 29.05           C  
-ATOM   2086  CG  MET C 284      13.689  61.068  56.846  1.00 36.68           C  
-ATOM   2087  SD  MET C 284      13.441  59.364  56.317  1.00 36.59           S  
-ATOM   2088  CE  MET C 284      11.893  58.939  57.198  1.00 40.82           C  
-ATOM   2089  N   PRO C 285      12.811  64.609  54.228  1.00 27.97           N  
-ATOM   2090  CA  PRO C 285      12.037  65.390  53.263  1.00 27.33           C  
-ATOM   2091  C   PRO C 285      10.916  64.489  52.739  1.00 26.04           C  
-ATOM   2092  O   PRO C 285      10.988  63.257  52.860  1.00 25.35           O  
-ATOM   2093  CB  PRO C 285      13.067  65.726  52.178  1.00 25.33           C  
-ATOM   2094  CG  PRO C 285      13.993  64.557  52.225  1.00 28.78           C  
-ATOM   2095  CD  PRO C 285      14.172  64.353  53.722  1.00 27.22           C  
-ATOM   2096  N   ARG C 286       9.891  65.095  52.150  1.00 24.80           N  
-ATOM   2097  CA  ARG C 286       8.773  64.326  51.627  1.00 24.97           C  
-ATOM   2098  C   ARG C 286       8.470  64.633  50.156  1.00 26.03           C  
-ATOM   2099  O   ARG C 286       8.994  65.588  49.590  1.00 24.45           O  
-ATOM   2100  CB  ARG C 286       7.525  64.614  52.474  1.00 24.35           C  
-ATOM   2101  CG  ARG C 286       7.670  64.214  53.954  1.00 30.99           C  
-ATOM   2102  CD  ARG C 286       6.385  64.459  54.743  1.00 25.29           C  
-ATOM   2103  NE  ARG C 286       6.058  65.883  54.879  1.00 33.96           N  
-ATOM   2104  CZ  ARG C 286       6.667  66.729  55.712  1.00 34.45           C  
-ATOM   2105  NH1 ARG C 286       7.649  66.311  56.497  1.00 33.51           N  
-ATOM   2106  NH2 ARG C 286       6.275  67.998  55.781  1.00 32.86           N  
-ATOM   2107  N   VAL C 287       7.634  63.798  49.548  1.00 26.55           N  
-ATOM   2108  CA  VAL C 287       7.181  63.999  48.175  1.00 26.22           C  
-ATOM   2109  C   VAL C 287       5.657  63.870  48.251  1.00 26.15           C  
-ATOM   2110  O   VAL C 287       5.130  62.901  48.804  1.00 23.18           O  
-ATOM   2111  CB  VAL C 287       7.736  62.936  47.201  1.00 26.10           C  
-ATOM   2112  CG1 VAL C 287       6.938  62.959  45.917  1.00 30.58           C  
-ATOM   2113  CG2 VAL C 287       9.204  63.225  46.881  1.00 27.52           C  
-ATOM   2114  N   ILE C 288       4.952  64.854  47.705  1.00 26.84           N  
-ATOM   2115  CA  ILE C 288       3.498  64.847  47.739  1.00 25.53           C  
-ATOM   2116  C   ILE C 288       2.811  63.814  46.845  1.00 26.16           C  
-ATOM   2117  O   ILE C 288       2.943  63.852  45.620  1.00 24.45           O  
-ATOM   2118  CB  ILE C 288       2.941  66.222  47.373  1.00 26.76           C  
-ATOM   2119  CG1 ILE C 288       3.622  67.309  48.219  1.00 23.75           C  
-ATOM   2120  CG2 ILE C 288       1.423  66.211  47.560  1.00 29.01           C  
-ATOM   2121  CD1 ILE C 288       3.386  67.191  49.736  1.00 20.44           C  
-ATOM   2122  N   PHE C 289       2.076  62.889  47.464  1.00 24.28           N  
-ATOM   2123  CA  PHE C 289       1.323  61.876  46.717  1.00 25.98           C  
-ATOM   2124  C   PHE C 289       0.202  62.601  45.959  1.00 26.94           C  
-ATOM   2125  O   PHE C 289      -0.458  63.488  46.519  1.00 23.10           O  
-ATOM   2126  CB  PHE C 289       0.688  60.866  47.674  1.00 24.93           C  
-ATOM   2127  CG  PHE C 289      -0.120  59.791  46.990  1.00 24.94           C  
-ATOM   2128  CD1 PHE C 289       0.514  58.751  46.296  1.00 23.35           C  
-ATOM   2129  CD2 PHE C 289      -1.519  59.811  47.044  1.00 24.25           C  
-ATOM   2130  CE1 PHE C 289      -0.222  57.753  45.670  1.00 19.86           C  
-ATOM   2131  CE2 PHE C 289      -2.281  58.813  46.417  1.00 22.53           C  
-ATOM   2132  CZ  PHE C 289      -1.634  57.781  45.729  1.00 24.47           C  
-ATOM   2133  N   ARG C 290      -0.015  62.236  44.698  1.00 24.66           N  
-ATOM   2134  CA  ARG C 290      -1.079  62.875  43.925  1.00 28.29           C  
-ATOM   2135  C   ARG C 290      -1.638  61.918  42.874  1.00 29.90           C  
-ATOM   2136  O   ARG C 290      -0.892  61.351  42.071  1.00 29.72           O  
-ATOM   2137  CB  ARG C 290      -0.563  64.154  43.249  1.00 27.60           C  
-ATOM   2138  CG  ARG C 290      -1.645  64.981  42.529  1.00 28.05           C  
-ATOM   2139  CD  ARG C 290      -2.739  65.466  43.484  1.00 28.50           C  
-ATOM   2140  NE  ARG C 290      -2.206  66.328  44.537  1.00 27.77           N  
-ATOM   2141  CZ  ARG C 290      -2.511  66.212  45.826  1.00 24.48           C  
-ATOM   2142  NH1 ARG C 290      -3.347  65.266  46.222  1.00 21.28           N  
-ATOM   2143  NH2 ARG C 290      -1.975  67.042  46.713  1.00 23.67           N  
-ATOM   2144  N   MET C 291      -2.952  61.714  42.905  1.00 29.12           N  
-ATOM   2145  CA  MET C 291      -3.593  60.836  41.935  1.00 29.11           C  
-ATOM   2146  C   MET C 291      -4.924  61.394  41.394  1.00 31.18           C  
-ATOM   2147  O   MET C 291      -5.422  60.908  40.382  1.00 34.92           O  
-ATOM   2148  CB  MET C 291      -3.809  59.435  42.535  1.00 26.61           C  
-ATOM   2149  CG  MET C 291      -4.933  59.330  43.566  1.00 23.99           C  
-ATOM   2150  SD  MET C 291      -5.178  57.638  44.177  1.00 28.95           S  
-ATOM   2151  CE  MET C 291      -6.003  56.858  42.778  1.00 32.32           C  
-ATOM   2152  N   PHE C 292      -5.482  62.421  42.040  1.00 30.78           N  
-ATOM   2153  CA  PHE C 292      -6.764  63.008  41.607  1.00 29.48           C  
-ATOM   2154  C   PHE C 292      -6.723  64.478  41.180  1.00 29.60           C  
-ATOM   2155  O   PHE C 292      -5.898  65.256  41.644  1.00 27.79           O  
-ATOM   2156  CB  PHE C 292      -7.813  62.944  42.733  1.00 28.32           C  
-ATOM   2157  CG  PHE C 292      -8.313  61.573  43.053  1.00 27.60           C  
-ATOM   2158  CD1 PHE C 292      -8.647  60.677  42.042  1.00 27.21           C  
-ATOM   2159  CD2 PHE C 292      -8.533  61.204  44.383  1.00 27.28           C  
-ATOM   2160  CE1 PHE C 292      -9.199  59.433  42.346  1.00 34.54           C  
-ATOM   2161  CE2 PHE C 292      -9.086  59.963  44.704  1.00 26.14           C  
-ATOM   2162  CZ  PHE C 292      -9.422  59.075  43.685  1.00 33.78           C  
-ATOM   2163  N   ASP C 293      -7.642  64.851  40.293  1.00 31.08           N  
-ATOM   2164  CA  ASP C 293      -7.812  66.246  39.884  1.00 30.97           C  
-ATOM   2165  C   ASP C 293      -9.322  66.417  39.683  1.00 30.96           C  
-ATOM   2166  O   ASP C 293     -10.059  65.430  39.669  1.00 26.82           O  
-ATOM   2167  CB  ASP C 293      -7.026  66.591  38.612  1.00 35.55           C  
-ATOM   2168  CG  ASP C 293      -7.501  65.835  37.394  1.00 35.39           C  
-ATOM   2169  OD1 ASP C 293      -6.634  65.360  36.638  1.00 42.98           O  
-ATOM   2170  OD2 ASP C 293      -8.722  65.720  37.175  1.00 38.95           O  
-ATOM   2171  N   TYR C 294      -9.789  67.653  39.554  1.00 32.99           N  
-ATOM   2172  CA  TYR C 294     -11.223  67.888  39.397  1.00 36.48           C  
-ATOM   2173  C   TYR C 294     -11.911  67.050  38.311  1.00 36.84           C  
-ATOM   2174  O   TYR C 294     -13.103  66.781  38.418  1.00 38.18           O  
-ATOM   2175  CB  TYR C 294     -11.499  69.378  39.151  1.00 39.19           C  
-ATOM   2176  CG  TYR C 294     -11.139  69.862  37.763  1.00 46.43           C  
-ATOM   2177  CD1 TYR C 294      -9.808  70.008  37.373  1.00 48.36           C  
-ATOM   2178  CD2 TYR C 294     -12.138  70.167  36.835  1.00 49.53           C  
-ATOM   2179  CE1 TYR C 294      -9.478  70.446  36.093  1.00 54.36           C  
-ATOM   2180  CE2 TYR C 294     -11.822  70.605  35.554  1.00 50.14           C  
-ATOM   2181  CZ  TYR C 294     -10.491  70.744  35.187  1.00 56.29           C  
-ATOM   2182  OH  TYR C 294     -10.169  71.182  33.918  1.00 60.37           O  
-ATOM   2183  N   THR C 295     -11.174  66.618  37.284  1.00 37.36           N  
-ATOM   2184  CA  THR C 295     -11.778  65.833  36.204  1.00 34.65           C  
-ATOM   2185  C   THR C 295     -12.084  64.395  36.585  1.00 35.30           C  
-ATOM   2186  O   THR C 295     -12.679  63.655  35.800  1.00 33.34           O  
-ATOM   2187  CB  THR C 295     -10.892  65.787  34.922  1.00 37.01           C  
-ATOM   2188  OG1 THR C 295      -9.930  64.729  35.029  1.00 36.24           O  
-ATOM   2189  CG2 THR C 295     -10.179  67.104  34.710  1.00 31.92           C  
-ATOM   2190  N   ASP C 296     -11.670  63.976  37.772  1.00 33.04           N  
-ATOM   2191  CA  ASP C 296     -11.953  62.610  38.183  1.00 31.71           C  
-ATOM   2192  C   ASP C 296     -13.332  62.578  38.847  1.00 31.11           C  
-ATOM   2193  O   ASP C 296     -13.902  61.515  39.073  1.00 29.44           O  
-ATOM   2194  CB  ASP C 296     -10.870  62.088  39.149  1.00 31.81           C  
-ATOM   2195  CG  ASP C 296      -9.519  61.888  38.465  1.00 34.95           C  
-ATOM   2196  OD1 ASP C 296      -9.499  61.263  37.388  1.00 34.31           O  
-ATOM   2197  OD2 ASP C 296      -8.480  62.344  38.995  1.00 31.45           O  
-ATOM   2198  N   ASP C 297     -13.857  63.754  39.162  1.00 33.48           N  
-ATOM   2199  CA  ASP C 297     -15.176  63.857  39.784  1.00 36.42           C  
-ATOM   2200  C   ASP C 297     -15.960  64.984  39.105  1.00 34.95           C  
-ATOM   2201  O   ASP C 297     -16.216  66.024  39.700  1.00 34.58           O  
-ATOM   2202  CB  ASP C 297     -15.018  64.127  41.285  1.00 36.34           C  
-ATOM   2203  CG  ASP C 297     -16.343  64.149  42.018  1.00 40.01           C  
-ATOM   2204  OD1 ASP C 297     -17.231  63.335  41.682  1.00 42.42           O  
-ATOM   2205  OD2 ASP C 297     -16.485  64.975  42.942  1.00 38.46           O  
-ATOM   2206  N   PRO C 298     -16.356  64.780  37.841  1.00 37.94           N  
-ATOM   2207  CA  PRO C 298     -17.105  65.789  37.082  1.00 42.26           C  
-ATOM   2208  C   PRO C 298     -18.464  66.177  37.658  1.00 44.03           C  
-ATOM   2209  O   PRO C 298     -18.805  67.359  37.723  1.00 45.13           O  
-ATOM   2210  CB  PRO C 298     -17.206  65.160  35.691  1.00 43.47           C  
-ATOM   2211  CG  PRO C 298     -17.275  63.702  35.996  1.00 40.70           C  
-ATOM   2212  CD  PRO C 298     -16.218  63.537  37.064  1.00 39.22           C  
-ATOM   2213  N   GLU C 299     -19.227  65.184  38.092  1.00 46.94           N  
-ATOM   2214  CA  GLU C 299     -20.549  65.439  38.639  1.00 50.70           C  
-ATOM   2215  C   GLU C 299     -20.543  65.753  40.131  1.00 51.03           C  
-ATOM   2216  O   GLU C 299     -21.557  65.586  40.806  1.00 52.54           O  
-ATOM   2217  CB  GLU C 299     -21.468  64.242  38.346  1.00 57.85           C  
-ATOM   2218  CG  GLU C 299     -22.128  64.267  36.953  1.00 63.44           C  
-ATOM   2219  CD  GLU C 299     -21.130  64.377  35.799  1.00 69.78           C  
-ATOM   2220  OE1 GLU C 299     -20.356  63.420  35.575  1.00 72.55           O  
-ATOM   2221  OE2 GLU C 299     -21.123  65.424  35.111  1.00 72.09           O  
-ATOM   2222  N   GLY C 300     -19.405  66.221  40.641  1.00 50.22           N  
-ATOM   2223  CA  GLY C 300     -19.308  66.552  42.054  1.00 46.81           C  
-ATOM   2224  C   GLY C 300     -18.700  67.924  42.274  1.00 44.41           C  
-ATOM   2225  O   GLY C 300     -18.382  68.609  41.307  1.00 45.74           O  
-ATOM   2226  N   PRO C 301     -18.541  68.364  43.532  1.00 42.65           N  
-ATOM   2227  CA  PRO C 301     -17.956  69.675  43.846  1.00 41.47           C  
-ATOM   2228  C   PRO C 301     -16.579  69.790  43.182  1.00 41.27           C  
-ATOM   2229  O   PRO C 301     -15.855  68.797  43.076  1.00 42.55           O  
-ATOM   2230  CB  PRO C 301     -17.860  69.653  45.367  1.00 42.07           C  
-ATOM   2231  CG  PRO C 301     -18.988  68.762  45.767  1.00 39.46           C  
-ATOM   2232  CD  PRO C 301     -18.905  67.644  44.763  1.00 41.20           C  
-ATOM   2233  N   VAL C 302     -16.213  70.988  42.739  1.00 40.53           N  
-ATOM   2234  CA  VAL C 302     -14.927  71.177  42.067  1.00 40.99           C  
-ATOM   2235  C   VAL C 302     -13.759  70.934  43.017  1.00 39.26           C  
-ATOM   2236  O   VAL C 302     -13.613  71.621  44.024  1.00 40.59           O  
-ATOM   2237  CB  VAL C 302     -14.815  72.594  41.462  1.00 42.80           C  
-ATOM   2238  CG1 VAL C 302     -13.473  72.766  40.763  1.00 44.82           C  
-ATOM   2239  CG2 VAL C 302     -15.953  72.819  40.473  1.00 45.19           C  
-ATOM   2240  N   MET C 303     -12.938  69.943  42.689  1.00 36.99           N  
-ATOM   2241  CA  MET C 303     -11.794  69.594  43.511  1.00 35.01           C  
-ATOM   2242  C   MET C 303     -10.707  70.667  43.478  1.00 34.94           C  
-ATOM   2243  O   MET C 303     -10.247  71.065  42.403  1.00 32.42           O  
-ATOM   2244  CB  MET C 303     -11.201  68.263  43.043  1.00 35.93           C  
-ATOM   2245  CG  MET C 303     -10.103  67.729  43.962  1.00 39.74           C  
-ATOM   2246  SD  MET C 303      -9.387  66.197  43.375  1.00 39.16           S  
-ATOM   2247  CE  MET C 303     -10.809  65.140  43.384  1.00 42.31           C  
-ATOM   2248  N   PRO C 304     -10.294  71.159  44.662  1.00 33.98           N  
-ATOM   2249  CA  PRO C 304      -9.249  72.183  44.756  1.00 32.17           C  
-ATOM   2250  C   PRO C 304      -8.012  71.658  44.018  1.00 31.68           C  
-ATOM   2251  O   PRO C 304      -7.691  70.472  44.118  1.00 33.58           O  
-ATOM   2252  CB  PRO C 304      -9.024  72.299  46.263  1.00 36.13           C  
-ATOM   2253  CG  PRO C 304     -10.382  72.013  46.822  1.00 35.43           C  
-ATOM   2254  CD  PRO C 304     -10.844  70.840  45.993  1.00 34.10           C  
-ATOM   2255  N   GLY C 305      -7.331  72.532  43.282  1.00 30.75           N  
-ATOM   2256  CA  GLY C 305      -6.159  72.128  42.515  1.00 30.09           C  
-ATOM   2257  C   GLY C 305      -4.896  71.770  43.287  1.00 32.13           C  
-ATOM   2258  O   GLY C 305      -4.680  72.203  44.424  1.00 30.97           O  
-ATOM   2259  N   SER C 306      -4.043  70.979  42.651  1.00 31.70           N  
-ATOM   2260  CA  SER C 306      -2.805  70.549  43.275  1.00 33.50           C  
-ATOM   2261  C   SER C 306      -1.978  71.709  43.807  1.00 33.17           C  
-ATOM   2262  O   SER C 306      -1.260  71.560  44.788  1.00 32.01           O  
-ATOM   2263  CB  SER C 306      -1.990  69.720  42.285  1.00 34.24           C  
-ATOM   2264  OG  SER C 306      -2.659  68.498  42.025  1.00 37.56           O  
-ATOM   2265  N   HIS C 307      -2.090  72.876  43.181  1.00 32.11           N  
-ATOM   2266  CA  HIS C 307      -1.325  74.014  43.651  1.00 30.95           C  
-ATOM   2267  C   HIS C 307      -2.103  75.040  44.472  1.00 31.03           C  
-ATOM   2268  O   HIS C 307      -1.675  76.188  44.594  1.00 29.44           O  
-ATOM   2269  CB  HIS C 307      -0.582  74.686  42.486  1.00 35.68           C  
-ATOM   2270  CG  HIS C 307       0.659  73.958  42.066  1.00 40.88           C  
-ATOM   2271  ND1 HIS C 307       1.533  74.452  41.120  1.00 46.59           N  
-ATOM   2272  CD2 HIS C 307       1.184  72.780  42.479  1.00 44.84           C  
-ATOM   2273  CE1 HIS C 307       2.541  73.612  40.970  1.00 46.88           C  
-ATOM   2274  NE2 HIS C 307       2.353  72.588  41.784  1.00 47.59           N  
-ATOM   2275  N   SER C 308      -3.225  74.624  45.064  1.00 31.76           N  
-ATOM   2276  CA  SER C 308      -4.001  75.523  45.921  1.00 32.72           C  
-ATOM   2277  C   SER C 308      -3.748  75.190  47.399  1.00 33.04           C  
-ATOM   2278  O   SER C 308      -3.522  74.022  47.747  1.00 32.42           O  
-ATOM   2279  CB  SER C 308      -5.502  75.402  45.630  1.00 35.73           C  
-ATOM   2280  OG  SER C 308      -6.023  74.143  46.032  1.00 38.71           O  
-ATOM   2281  N   VAL C 309      -3.777  76.207  48.263  1.00 33.60           N  
-ATOM   2282  CA  VAL C 309      -3.575  75.995  49.694  1.00 33.99           C  
-ATOM   2283  C   VAL C 309      -4.724  75.179  50.279  1.00 33.41           C  
-ATOM   2284  O   VAL C 309      -4.569  74.514  51.311  1.00 33.88           O  
-ATOM   2285  CB  VAL C 309      -3.474  77.328  50.484  1.00 36.88           C  
-ATOM   2286  CG1 VAL C 309      -2.119  77.970  50.255  1.00 36.56           C  
-ATOM   2287  CG2 VAL C 309      -4.603  78.270  50.075  1.00 37.24           C  
-ATOM   2288  N   GLU C 310      -5.883  75.230  49.628  1.00 31.64           N  
-ATOM   2289  CA  GLU C 310      -7.021  74.464  50.108  1.00 30.44           C  
-ATOM   2290  C   GLU C 310      -6.692  72.965  50.057  1.00 29.60           C  
-ATOM   2291  O   GLU C 310      -6.972  72.226  51.000  1.00 30.49           O  
-ATOM   2292  CB  GLU C 310      -8.275  74.765  49.275  1.00 33.23           C  
-ATOM   2293  CG  GLU C 310      -8.855  76.168  49.487  1.00 36.69           C  
-ATOM   2294  CD  GLU C 310      -8.266  77.217  48.551  1.00 41.14           C  
-ATOM   2295  OE1 GLU C 310      -7.210  76.956  47.934  1.00 40.88           O  
-ATOM   2296  OE2 GLU C 310      -8.859  78.316  48.444  1.00 43.44           O  
-ATOM   2297  N   ARG C 311      -6.095  72.521  48.957  1.00 26.65           N  
-ATOM   2298  CA  ARG C 311      -5.737  71.115  48.814  1.00 26.79           C  
-ATOM   2299  C   ARG C 311      -4.779  70.726  49.942  1.00 24.10           C  
-ATOM   2300  O   ARG C 311      -4.911  69.660  50.518  1.00 24.39           O  
-ATOM   2301  CB  ARG C 311      -5.054  70.858  47.460  1.00 20.52           C  
-ATOM   2302  CG  ARG C 311      -4.971  69.389  47.048  1.00 22.91           C  
-ATOM   2303  CD  ARG C 311      -6.368  68.792  46.871  1.00 25.34           C  
-ATOM   2304  NE  ARG C 311      -6.359  67.464  46.254  1.00 23.07           N  
-ATOM   2305  CZ  ARG C 311      -6.128  67.226  44.968  1.00 26.88           C  
-ATOM   2306  NH1 ARG C 311      -5.886  68.230  44.142  1.00 24.43           N  
-ATOM   2307  NH2 ARG C 311      -6.141  65.982  44.506  1.00 20.47           N  
-ATOM   2308  N   PHE C 312      -3.818  71.599  50.225  1.00 23.80           N  
-ATOM   2309  CA  PHE C 312      -2.828  71.374  51.270  1.00 27.87           C  
-ATOM   2310  C   PHE C 312      -3.458  71.245  52.655  1.00 26.82           C  
-ATOM   2311  O   PHE C 312      -3.148  70.317  53.406  1.00 27.66           O  
-ATOM   2312  CB  PHE C 312      -1.812  72.522  51.288  1.00 29.29           C  
-ATOM   2313  CG  PHE C 312      -0.866  72.473  52.453  1.00 32.80           C  
-ATOM   2314  CD1 PHE C 312       0.155  71.526  52.498  1.00 34.00           C  
-ATOM   2315  CD2 PHE C 312      -1.031  73.342  53.534  1.00 33.13           C  
-ATOM   2316  CE1 PHE C 312       1.006  71.434  53.611  1.00 35.16           C  
-ATOM   2317  CE2 PHE C 312      -0.191  73.264  54.654  1.00 33.66           C  
-ATOM   2318  CZ  PHE C 312       0.831  72.305  54.694  1.00 33.04           C  
-ATOM   2319  N   VAL C 313      -4.339  72.182  52.988  1.00 26.72           N  
-ATOM   2320  CA  VAL C 313      -5.011  72.194  54.283  1.00 26.66           C  
-ATOM   2321  C   VAL C 313      -5.921  70.984  54.473  1.00 27.83           C  
-ATOM   2322  O   VAL C 313      -5.919  70.339  55.533  1.00 27.54           O  
-ATOM   2323  CB  VAL C 313      -5.792  73.522  54.449  1.00 30.80           C  
-ATOM   2324  CG1 VAL C 313      -6.558  73.550  55.773  1.00 27.18           C  
-ATOM   2325  CG2 VAL C 313      -4.799  74.686  54.388  1.00 28.65           C  
-ATOM   2326  N   ILE C 314      -6.685  70.672  53.434  1.00 27.93           N  
-ATOM   2327  CA  ILE C 314      -7.598  69.543  53.450  1.00 25.62           C  
-ATOM   2328  C   ILE C 314      -6.847  68.253  53.767  1.00 26.19           C  
-ATOM   2329  O   ILE C 314      -7.207  67.516  54.688  1.00 26.75           O  
-ATOM   2330  CB  ILE C 314      -8.285  69.391  52.077  1.00 24.10           C  
-ATOM   2331  CG1 ILE C 314      -9.282  70.532  51.863  1.00 28.94           C  
-ATOM   2332  CG2 ILE C 314      -8.943  68.050  51.967  1.00 18.87           C  
-ATOM   2333  CD1 ILE C 314      -9.858  70.570  50.455  1.00 28.43           C  
-ATOM   2334  N   GLU C 315      -5.798  67.990  52.995  1.00 25.13           N  
-ATOM   2335  CA  GLU C 315      -5.000  66.788  53.165  1.00 25.44           C  
-ATOM   2336  C   GLU C 315      -4.293  66.716  54.520  1.00 24.42           C  
-ATOM   2337  O   GLU C 315      -4.262  65.660  55.155  1.00 25.51           O  
-ATOM   2338  CB  GLU C 315      -3.987  66.675  52.015  1.00 24.26           C  
-ATOM   2339  CG  GLU C 315      -4.677  66.579  50.652  1.00 29.78           C  
-ATOM   2340  CD  GLU C 315      -3.773  66.044  49.563  1.00 31.76           C  
-ATOM   2341  OE1 GLU C 315      -2.660  66.587  49.403  1.00 38.42           O  
-ATOM   2342  OE2 GLU C 315      -4.180  65.084  48.869  1.00 34.74           O  
-ATOM   2343  N   GLU C 316      -3.743  67.844  54.949  1.00 23.69           N  
-ATOM   2344  CA  GLU C 316      -3.045  67.954  56.217  1.00 24.70           C  
-ATOM   2345  C   GLU C 316      -3.998  67.677  57.383  1.00 23.68           C  
-ATOM   2346  O   GLU C 316      -3.629  67.010  58.337  1.00 23.53           O  
-ATOM   2347  CB  GLU C 316      -2.430  69.357  56.337  1.00 25.06           C  
-ATOM   2348  CG  GLU C 316      -1.872  69.717  57.710  1.00 36.63           C  
-ATOM   2349  CD  GLU C 316      -0.553  69.034  58.019  1.00 36.81           C  
-ATOM   2350  OE1 GLU C 316      -0.179  68.085  57.297  1.00 37.72           O  
-ATOM   2351  OE2 GLU C 316       0.108  69.441  58.991  1.00 38.47           O  
-ATOM   2352  N   ASN C 317      -5.228  68.179  57.300  1.00 25.24           N  
-ATOM   2353  CA  ASN C 317      -6.199  67.947  58.366  1.00 25.64           C  
-ATOM   2354  C   ASN C 317      -6.667  66.498  58.389  1.00 22.61           C  
-ATOM   2355  O   ASN C 317      -6.853  65.928  59.461  1.00 21.04           O  
-ATOM   2356  CB  ASN C 317      -7.419  68.869  58.227  1.00 29.49           C  
-ATOM   2357  CG  ASN C 317      -7.115  70.300  58.619  1.00 29.34           C  
-ATOM   2358  OD1 ASN C 317      -6.145  70.567  59.321  1.00 31.14           O  
-ATOM   2359  ND2 ASN C 317      -7.957  71.229  58.179  1.00 30.48           N  
-ATOM   2360  N   LEU C 318      -6.858  65.899  57.214  1.00 22.20           N  
-ATOM   2361  CA  LEU C 318      -7.306  64.514  57.157  1.00 21.39           C  
-ATOM   2362  C   LEU C 318      -6.186  63.571  57.656  1.00 22.84           C  
-ATOM   2363  O   LEU C 318      -6.464  62.557  58.302  1.00 24.24           O  
-ATOM   2364  CB  LEU C 318      -7.754  64.141  55.727  1.00 20.76           C  
-ATOM   2365  CG  LEU C 318      -9.002  64.874  55.171  1.00 26.06           C  
-ATOM   2366  CD1 LEU C 318      -9.195  64.544  53.691  1.00 23.53           C  
-ATOM   2367  CD2 LEU C 318     -10.251  64.491  55.954  1.00 20.22           C  
-ATOM   2368  N   HIS C 319      -4.931  63.899  57.356  1.00 21.89           N  
-ATOM   2369  CA  HIS C 319      -3.812  63.084  57.832  1.00 22.29           C  
-ATOM   2370  C   HIS C 319      -3.819  63.190  59.364  1.00 22.17           C  
-ATOM   2371  O   HIS C 319      -3.618  62.197  60.064  1.00 21.29           O  
-ATOM   2372  CB  HIS C 319      -2.457  63.620  57.328  1.00 20.50           C  
-ATOM   2373  CG  HIS C 319      -2.110  63.220  55.927  1.00 19.18           C  
-ATOM   2374  ND1 HIS C 319      -1.900  61.908  55.551  1.00 24.43           N  
-ATOM   2375  CD2 HIS C 319      -1.880  63.968  54.819  1.00 24.89           C  
-ATOM   2376  CE1 HIS C 319      -1.556  61.867  54.274  1.00 24.94           C  
-ATOM   2377  NE2 HIS C 319      -1.536  63.104  53.807  1.00 25.65           N  
-ATOM   2378  N   CYS C 320      -4.053  64.407  59.862  1.00 21.52           N  
-ATOM   2379  CA  CYS C 320      -4.066  64.659  61.301  1.00 24.10           C  
-ATOM   2380  C   CYS C 320      -5.155  63.885  62.018  1.00 23.97           C  
-ATOM   2381  O   CYS C 320      -4.932  63.348  63.105  1.00 24.60           O  
-ATOM   2382  CB  CYS C 320      -4.191  66.154  61.576  1.00 20.16           C  
-ATOM   2383  SG  CYS C 320      -2.612  67.017  61.336  1.00 26.08           S  
-ATOM   2384  N   ILE C 321      -6.327  63.816  61.397  1.00 23.29           N  
-ATOM   2385  CA  ILE C 321      -7.455  63.088  61.954  1.00 21.07           C  
-ATOM   2386  C   ILE C 321      -7.085  61.608  62.100  1.00 22.39           C  
-ATOM   2387  O   ILE C 321      -7.349  60.978  63.136  1.00 19.24           O  
-ATOM   2388  CB  ILE C 321      -8.689  63.242  61.027  1.00 26.46           C  
-ATOM   2389  CG1 ILE C 321      -9.238  64.667  61.144  1.00 24.38           C  
-ATOM   2390  CG2 ILE C 321      -9.751  62.193  61.354  1.00 21.47           C  
-ATOM   2391  CD1 ILE C 321     -10.319  65.008  60.127  1.00 26.03           C  
-ATOM   2392  N   ILE C 322      -6.472  61.050  61.062  1.00 19.85           N  
-ATOM   2393  CA  ILE C 322      -6.079  59.648  61.102  1.00 21.78           C  
-ATOM   2394  C   ILE C 322      -5.030  59.439  62.200  1.00 23.00           C  
-ATOM   2395  O   ILE C 322      -5.040  58.431  62.909  1.00 25.40           O  
-ATOM   2396  CB  ILE C 322      -5.504  59.197  59.732  1.00 19.17           C  
-ATOM   2397  CG1 ILE C 322      -6.644  59.087  58.714  1.00 16.98           C  
-ATOM   2398  CG2 ILE C 322      -4.746  57.874  59.876  1.00 16.12           C  
-ATOM   2399  CD1 ILE C 322      -6.195  58.864  57.277  1.00 22.16           C  
-ATOM   2400  N   LYS C 323      -4.128  60.404  62.324  1.00 24.30           N  
-ATOM   2401  CA  LYS C 323      -3.064  60.368  63.315  1.00 24.65           C  
-ATOM   2402  C   LYS C 323      -3.648  60.333  64.728  1.00 24.70           C  
-ATOM   2403  O   LYS C 323      -3.151  59.615  65.595  1.00 24.86           O  
-ATOM   2404  CB  LYS C 323      -2.165  61.593  63.133  1.00 26.78           C  
-ATOM   2405  CG  LYS C 323      -1.129  61.811  64.231  1.00 36.42           C  
-ATOM   2406  CD  LYS C 323      -0.111  62.861  63.795  1.00 42.72           C  
-ATOM   2407  CE  LYS C 323       0.315  63.754  64.953  1.00 48.30           C  
-ATOM   2408  NZ  LYS C 323      -0.832  64.554  65.476  1.00 49.78           N  
-ATOM   2409  N   SER C 324      -4.711  61.099  64.948  1.00 23.68           N  
-ATOM   2410  CA  SER C 324      -5.375  61.143  66.246  1.00 24.74           C  
-ATOM   2411  C   SER C 324      -6.181  59.893  66.564  1.00 25.87           C  
-ATOM   2412  O   SER C 324      -6.149  59.404  67.694  1.00 26.83           O  
-ATOM   2413  CB  SER C 324      -6.340  62.334  66.326  1.00 23.48           C  
-ATOM   2414  OG  SER C 324      -5.642  63.560  66.316  1.00 24.72           O  
-ATOM   2415  N   HIS C 325      -6.883  59.358  65.568  1.00 23.22           N  
-ATOM   2416  CA  HIS C 325      -7.758  58.225  65.818  1.00 23.43           C  
-ATOM   2417  C   HIS C 325      -7.405  56.891  65.183  1.00 24.01           C  
-ATOM   2418  O   HIS C 325      -8.276  56.029  65.057  1.00 24.06           O  
-ATOM   2419  CB  HIS C 325      -9.187  58.628  65.419  1.00 24.65           C  
-ATOM   2420  CG  HIS C 325      -9.624  59.945  65.991  1.00 28.69           C  
-ATOM   2421  ND1 HIS C 325     -10.115  60.076  67.273  1.00 29.97           N  
-ATOM   2422  CD2 HIS C 325      -9.595  61.195  65.471  1.00 29.76           C  
-ATOM   2423  CE1 HIS C 325     -10.368  61.350  67.517  1.00 26.16           C  
-ATOM   2424  NE2 HIS C 325     -10.060  62.051  66.442  1.00 27.74           N  
-ATOM   2425  N   TRP C 326      -6.140  56.688  64.823  1.00 24.27           N  
-ATOM   2426  CA  TRP C 326      -5.766  55.432  64.175  1.00 25.79           C  
-ATOM   2427  C   TRP C 326      -6.086  54.138  64.937  1.00 24.88           C  
-ATOM   2428  O   TRP C 326      -6.277  53.104  64.316  1.00 24.63           O  
-ATOM   2429  CB  TRP C 326      -4.277  55.448  63.786  1.00 28.13           C  
-ATOM   2430  CG  TRP C 326      -3.336  55.416  64.953  1.00 28.70           C  
-ATOM   2431  CD1 TRP C 326      -2.978  56.457  65.753  1.00 30.20           C  
-ATOM   2432  CD2 TRP C 326      -2.681  54.262  65.477  1.00 29.73           C  
-ATOM   2433  NE1 TRP C 326      -2.138  56.025  66.749  1.00 33.06           N  
-ATOM   2434  CE2 TRP C 326      -1.939  54.677  66.601  1.00 33.85           C  
-ATOM   2435  CE3 TRP C 326      -2.650  52.912  65.103  1.00 30.24           C  
-ATOM   2436  CZ2 TRP C 326      -1.172  53.788  67.361  1.00 35.56           C  
-ATOM   2437  CZ3 TRP C 326      -1.889  52.027  65.852  1.00 33.02           C  
-ATOM   2438  CH2 TRP C 326      -1.158  52.470  66.971  1.00 36.89           C  
-ATOM   2439  N   LYS C 327      -6.150  54.179  66.269  1.00 25.43           N  
-ATOM   2440  CA  LYS C 327      -6.453  52.971  67.051  1.00 23.11           C  
-ATOM   2441  C   LYS C 327      -7.940  52.574  67.046  1.00 25.60           C  
-ATOM   2442  O   LYS C 327      -8.281  51.411  67.304  1.00 24.82           O  
-ATOM   2443  CB  LYS C 327      -5.976  53.142  68.507  1.00 25.65           C  
-ATOM   2444  CG  LYS C 327      -4.473  53.439  68.647  1.00 17.86           C  
-ATOM   2445  CD  LYS C 327      -4.011  53.497  70.111  1.00 22.70           C  
-ATOM   2446  CE  LYS C 327      -4.545  54.723  70.869  1.00 26.11           C  
-ATOM   2447  NZ  LYS C 327      -3.988  56.017  70.363  1.00 28.29           N  
-ATOM   2448  N   GLU C 328      -8.816  53.531  66.740  1.00 24.24           N  
-ATOM   2449  CA  GLU C 328     -10.269  53.283  66.717  1.00 25.95           C  
-ATOM   2450  C   GLU C 328     -10.769  53.424  65.274  1.00 24.92           C  
-ATOM   2451  O   GLU C 328     -11.120  54.524  64.847  1.00 23.82           O  
-ATOM   2452  CB  GLU C 328     -10.969  54.312  67.601  1.00 27.05           C  
-ATOM   2453  CG  GLU C 328     -10.505  54.332  69.045  1.00 33.01           C  
-ATOM   2454  CD  GLU C 328     -11.290  53.371  69.916  1.00 37.73           C  
-ATOM   2455  OE1 GLU C 328     -11.917  52.437  69.371  1.00 39.43           O  
-ATOM   2456  OE2 GLU C 328     -11.274  53.545  71.151  1.00 38.98           O  
-ATOM   2457  N   ARG C 329     -10.806  52.321  64.533  1.00 25.84           N  
-ATOM   2458  CA  ARG C 329     -11.201  52.363  63.128  1.00 27.36           C  
-ATOM   2459  C   ARG C 329     -12.583  52.939  62.842  1.00 29.06           C  
-ATOM   2460  O   ARG C 329     -12.762  53.653  61.854  1.00 26.71           O  
-ATOM   2461  CB  ARG C 329     -11.087  50.969  62.514  1.00 28.14           C  
-ATOM   2462  CG  ARG C 329     -12.131  49.993  63.002  1.00 32.14           C  
-ATOM   2463  CD  ARG C 329     -11.643  48.589  62.801  1.00 30.62           C  
-ATOM   2464  NE  ARG C 329     -12.733  47.643  62.620  1.00 26.61           N  
-ATOM   2465  CZ  ARG C 329     -12.614  46.335  62.794  1.00 31.54           C  
-ATOM   2466  NH1 ARG C 329     -11.447  45.812  63.166  1.00 30.31           N  
-ATOM   2467  NH2 ARG C 329     -13.661  45.548  62.583  1.00 32.20           N  
-ATOM   2468  N   LYS C 330     -13.561  52.637  63.689  1.00 28.27           N  
-ATOM   2469  CA  LYS C 330     -14.911  53.161  63.461  1.00 30.28           C  
-ATOM   2470  C   LYS C 330     -14.956  54.655  63.717  1.00 29.16           C  
-ATOM   2471  O   LYS C 330     -15.575  55.416  62.965  1.00 31.05           O  
-ATOM   2472  CB  LYS C 330     -15.917  52.460  64.367  1.00 33.53           C  
-ATOM   2473  CG  LYS C 330     -17.000  51.735  63.601  1.00 42.06           C  
-ATOM   2474  CD  LYS C 330     -17.792  50.794  64.486  1.00 43.48           C  
-ATOM   2475  CE  LYS C 330     -18.876  50.097  63.666  1.00 53.10           C  
-ATOM   2476  NZ  LYS C 330     -18.320  49.435  62.440  1.00 50.29           N  
-ATOM   2477  N   THR C 331     -14.294  55.075  64.787  1.00 28.40           N  
-ATOM   2478  CA  THR C 331     -14.253  56.485  65.144  1.00 28.02           C  
-ATOM   2479  C   THR C 331     -13.414  57.260  64.129  1.00 28.71           C  
-ATOM   2480  O   THR C 331     -13.681  58.429  63.843  1.00 29.76           O  
-ATOM   2481  CB  THR C 331     -13.637  56.678  66.553  1.00 32.54           C  
-ATOM   2482  OG1 THR C 331     -14.503  56.097  67.536  1.00 38.35           O  
-ATOM   2483  CG2 THR C 331     -13.445  58.148  66.865  1.00 30.27           C  
-ATOM   2484  N   CYS C 332     -12.384  56.615  63.594  1.00 26.36           N  
-ATOM   2485  CA  CYS C 332     -11.524  57.291  62.635  1.00 25.03           C  
-ATOM   2486  C   CYS C 332     -12.321  57.589  61.363  1.00 22.56           C  
-ATOM   2487  O   CYS C 332     -12.284  58.700  60.841  1.00 21.77           O  
-ATOM   2488  CB  CYS C 332     -10.298  56.427  62.304  1.00 22.18           C  
-ATOM   2489  SG  CYS C 332      -9.038  57.334  61.413  1.00 25.30           S  
-ATOM   2490  N   ALA C 333     -13.064  56.592  60.888  1.00 22.87           N  
-ATOM   2491  CA  ALA C 333     -13.870  56.743  59.681  1.00 23.75           C  
-ATOM   2492  C   ALA C 333     -14.941  57.812  59.863  1.00 24.51           C  
-ATOM   2493  O   ALA C 333     -15.220  58.572  58.944  1.00 24.70           O  
-ATOM   2494  CB  ALA C 333     -14.521  55.407  59.308  1.00 22.59           C  
-ATOM   2495  N   ALA C 334     -15.542  57.864  61.050  1.00 24.63           N  
-ATOM   2496  CA  ALA C 334     -16.578  58.858  61.327  1.00 23.55           C  
-ATOM   2497  C   ALA C 334     -15.999  60.277  61.341  1.00 23.85           C  
-ATOM   2498  O   ALA C 334     -16.621  61.223  60.837  1.00 23.70           O  
-ATOM   2499  CB  ALA C 334     -17.262  58.553  62.674  1.00 19.47           C  
-ATOM   2500  N   GLN C 335     -14.821  60.436  61.933  1.00 21.26           N  
-ATOM   2501  CA  GLN C 335     -14.198  61.754  61.973  1.00 22.62           C  
-ATOM   2502  C   GLN C 335     -13.790  62.239  60.572  1.00 22.11           C  
-ATOM   2503  O   GLN C 335     -13.876  63.428  60.275  1.00 25.33           O  
-ATOM   2504  CB  GLN C 335     -12.974  61.738  62.879  1.00 23.60           C  
-ATOM   2505  CG  GLN C 335     -13.313  61.562  64.343  1.00 32.53           C  
-ATOM   2506  CD  GLN C 335     -14.294  62.600  64.833  1.00 39.53           C  
-ATOM   2507  OE1 GLN C 335     -14.011  63.799  64.820  1.00 40.38           O  
-ATOM   2508  NE2 GLN C 335     -15.466  62.143  65.266  1.00 43.42           N  
-ATOM   2509  N   LEU C 336     -13.333  61.324  59.723  1.00 22.54           N  
-ATOM   2510  CA  LEU C 336     -12.940  61.684  58.358  1.00 25.31           C  
-ATOM   2511  C   LEU C 336     -14.191  62.127  57.585  1.00 25.99           C  
-ATOM   2512  O   LEU C 336     -14.204  63.173  56.958  1.00 27.31           O  
-ATOM   2513  CB  LEU C 336     -12.279  60.482  57.652  1.00 21.38           C  
-ATOM   2514  CG  LEU C 336     -10.868  60.120  58.159  1.00 23.43           C  
-ATOM   2515  CD1 LEU C 336     -10.439  58.760  57.617  1.00 23.00           C  
-ATOM   2516  CD2 LEU C 336      -9.887  61.187  57.731  1.00 14.94           C  
-ATOM   2517  N   VAL C 337     -15.247  61.328  57.661  1.00 28.54           N  
-ATOM   2518  CA  VAL C 337     -16.496  61.626  56.968  1.00 30.23           C  
-ATOM   2519  C   VAL C 337     -17.198  62.910  57.425  1.00 30.36           C  
-ATOM   2520  O   VAL C 337     -17.884  63.557  56.633  1.00 29.98           O  
-ATOM   2521  CB  VAL C 337     -17.482  60.440  57.097  1.00 33.32           C  
-ATOM   2522  CG1 VAL C 337     -18.887  60.860  56.641  1.00 35.69           C  
-ATOM   2523  CG2 VAL C 337     -16.985  59.279  56.255  1.00 29.36           C  
-ATOM   2524  N   SER C 338     -17.032  63.282  58.689  1.00 26.72           N  
-ATOM   2525  CA  SER C 338     -17.669  64.494  59.193  1.00 28.81           C  
-ATOM   2526  C   SER C 338     -16.757  65.708  59.060  1.00 27.13           C  
-ATOM   2527  O   SER C 338     -17.061  66.766  59.586  1.00 28.57           O  
-ATOM   2528  CB  SER C 338     -18.075  64.326  60.670  1.00 28.73           C  
-ATOM   2529  OG  SER C 338     -16.936  64.275  61.509  1.00 32.69           O  
-ATOM   2530  N   TYR C 339     -15.646  65.566  58.348  1.00 29.79           N  
-ATOM   2531  CA  TYR C 339     -14.716  66.676  58.188  1.00 30.11           C  
-ATOM   2532  C   TYR C 339     -15.392  67.926  57.646  1.00 33.02           C  
-ATOM   2533  O   TYR C 339     -16.038  67.879  56.605  1.00 33.82           O  
-ATOM   2534  CB  TYR C 339     -13.583  66.285  57.255  1.00 27.91           C  
-ATOM   2535  CG  TYR C 339     -12.611  67.397  57.013  1.00 28.70           C  
-ATOM   2536  CD1 TYR C 339     -11.806  67.875  58.034  1.00 28.25           C  
-ATOM   2537  CD2 TYR C 339     -12.487  67.977  55.750  1.00 33.42           C  
-ATOM   2538  CE1 TYR C 339     -10.899  68.897  57.811  1.00 31.43           C  
-ATOM   2539  CE2 TYR C 339     -11.572  69.002  55.515  1.00 23.24           C  
-ATOM   2540  CZ  TYR C 339     -10.783  69.451  56.546  1.00 27.88           C  
-ATOM   2541  OH  TYR C 339      -9.849  70.432  56.307  1.00 28.64           O  
-ATOM   2542  N   PRO C 340     -15.235  69.068  58.342  1.00 34.09           N  
-ATOM   2543  CA  PRO C 340     -15.843  70.333  57.923  1.00 37.38           C  
-ATOM   2544  C   PRO C 340     -14.955  71.289  57.117  1.00 39.58           C  
-ATOM   2545  O   PRO C 340     -13.724  71.274  57.220  1.00 39.85           O  
-ATOM   2546  CB  PRO C 340     -16.279  70.939  59.248  1.00 36.42           C  
-ATOM   2547  CG  PRO C 340     -15.109  70.593  60.125  1.00 37.79           C  
-ATOM   2548  CD  PRO C 340     -14.808  69.142  59.753  1.00 37.57           C  
-ATOM   2549  N   GLY C 341     -15.608  72.129  56.320  1.00 39.43           N  
-ATOM   2550  CA  GLY C 341     -14.901  73.098  55.506  1.00 39.74           C  
-ATOM   2551  C   GLY C 341     -15.801  74.279  55.190  1.00 41.47           C  
-ATOM   2552  O   GLY C 341     -17.025  74.195  55.346  1.00 41.06           O  
-ATOM   2553  N   LYS C 342     -15.206  75.384  54.748  1.00 41.44           N  
-ATOM   2554  CA  LYS C 342     -15.986  76.570  54.425  1.00 43.25           C  
-ATOM   2555  C   LYS C 342     -16.841  76.371  53.169  1.00 43.12           C  
-ATOM   2556  O   LYS C 342     -17.934  76.917  53.071  1.00 44.22           O  
-ATOM   2557  CB  LYS C 342     -15.076  77.784  54.232  1.00 43.13           C  
-ATOM   2558  CG  LYS C 342     -15.859  79.046  53.903  1.00 44.98           C  
-ATOM   2559  CD  LYS C 342     -15.014  80.050  53.152  1.00 47.66           C  
-ATOM   2560  CE  LYS C 342     -13.907  80.611  54.008  1.00 40.39           C  
-ATOM   2561  NZ  LYS C 342     -13.062  81.517  53.187  1.00 43.15           N  
-ATOM   2562  N   ASN C 343     -16.336  75.598  52.212  1.00 43.28           N  
-ATOM   2563  CA  ASN C 343     -17.068  75.325  50.975  1.00 44.18           C  
-ATOM   2564  C   ASN C 343     -17.061  73.833  50.665  1.00 44.14           C  
-ATOM   2565  O   ASN C 343     -16.157  73.113  51.091  1.00 44.72           O  
-ATOM   2566  CB  ASN C 343     -16.458  76.116  49.811  1.00 45.02           C  
-ATOM   2567  CG  ASN C 343     -16.856  77.584  49.835  1.00 44.96           C  
-ATOM   2568  OD1 ASN C 343     -18.036  77.915  49.710  1.00 45.15           O  
-ATOM   2569  ND2 ASN C 343     -15.876  78.470  50.001  1.00 45.10           N  
-ATOM   2570  N   LYS C 344     -18.065  73.364  49.932  1.00 44.03           N  
-ATOM   2571  CA  LYS C 344     -18.146  71.942  49.611  1.00 43.88           C  
-ATOM   2572  C   LYS C 344     -16.953  71.449  48.809  1.00 40.76           C  
-ATOM   2573  O   LYS C 344     -16.401  72.173  47.984  1.00 40.91           O  
-ATOM   2574  CB  LYS C 344     -19.433  71.614  48.854  1.00 49.74           C  
-ATOM   2575  CG  LYS C 344     -20.691  71.714  49.694  1.00 58.32           C  
-ATOM   2576  CD  LYS C 344     -21.767  70.764  49.186  1.00 64.95           C  
-ATOM   2577  CE  LYS C 344     -21.335  69.308  49.345  1.00 66.78           C  
-ATOM   2578  NZ  LYS C 344     -22.412  68.367  48.934  1.00 67.83           N  
-ATOM   2579  N   ILE C 345     -16.559  70.208  49.074  1.00 37.64           N  
-ATOM   2580  CA  ILE C 345     -15.435  69.589  48.390  1.00 31.53           C  
-ATOM   2581  C   ILE C 345     -15.797  68.142  48.153  1.00 30.87           C  
-ATOM   2582  O   ILE C 345     -16.718  67.622  48.773  1.00 29.24           O  
-ATOM   2583  CB  ILE C 345     -14.147  69.637  49.245  1.00 31.59           C  
-ATOM   2584  CG1 ILE C 345     -14.392  68.962  50.603  1.00 30.41           C  
-ATOM   2585  CG2 ILE C 345     -13.698  71.079  49.427  1.00 21.68           C  
-ATOM   2586  CD1 ILE C 345     -13.186  68.961  51.539  1.00 27.78           C  
-ATOM   2587  N   PRO C 346     -15.097  67.480  47.219  1.00 29.76           N  
-ATOM   2588  CA  PRO C 346     -15.376  66.075  46.934  1.00 29.68           C  
-ATOM   2589  C   PRO C 346     -14.668  65.218  47.993  1.00 30.62           C  
-ATOM   2590  O   PRO C 346     -13.766  64.444  47.678  1.00 30.62           O  
-ATOM   2591  CB  PRO C 346     -14.808  65.893  45.530  1.00 25.05           C  
-ATOM   2592  CG  PRO C 346     -13.651  66.843  45.503  1.00 27.82           C  
-ATOM   2593  CD  PRO C 346     -14.143  68.053  46.247  1.00 29.15           C  
-ATOM   2594  N   LEU C 347     -15.116  65.371  49.241  1.00 32.26           N  
-ATOM   2595  CA  LEU C 347     -14.549  64.684  50.402  1.00 30.56           C  
-ATOM   2596  C   LEU C 347     -14.179  63.217  50.218  1.00 29.00           C  
-ATOM   2597  O   LEU C 347     -13.073  62.831  50.575  1.00 28.05           O  
-ATOM   2598  CB  LEU C 347     -15.477  64.837  51.623  1.00 29.65           C  
-ATOM   2599  CG  LEU C 347     -14.863  64.404  52.964  1.00 30.30           C  
-ATOM   2600  CD1 LEU C 347     -13.624  65.228  53.195  1.00 23.65           C  
-ATOM   2601  CD2 LEU C 347     -15.852  64.581  54.130  1.00 29.14           C  
-ATOM   2602  N   ASN C 348     -15.083  62.399  49.678  1.00 28.15           N  
-ATOM   2603  CA  ASN C 348     -14.789  60.979  49.465  1.00 27.92           C  
-ATOM   2604  C   ASN C 348     -13.490  60.790  48.686  1.00 28.47           C  
-ATOM   2605  O   ASN C 348     -12.726  59.860  48.958  1.00 24.49           O  
-ATOM   2606  CB  ASN C 348     -15.901  60.267  48.683  1.00 32.53           C  
-ATOM   2607  CG  ASN C 348     -17.149  60.015  49.509  1.00 35.84           C  
-ATOM   2608  OD1 ASN C 348     -17.095  59.878  50.731  1.00 33.18           O  
-ATOM   2609  ND2 ASN C 348     -18.286  59.930  48.831  1.00 39.78           N  
-ATOM   2610  N   TYR C 349     -13.259  61.663  47.707  1.00 28.21           N  
-ATOM   2611  CA  TYR C 349     -12.053  61.580  46.900  1.00 28.23           C  
-ATOM   2612  C   TYR C 349     -10.845  61.983  47.730  1.00 27.30           C  
-ATOM   2613  O   TYR C 349      -9.797  61.349  47.655  1.00 24.25           O  
-ATOM   2614  CB  TYR C 349     -12.148  62.474  45.651  1.00 24.75           C  
-ATOM   2615  CG  TYR C 349     -13.007  61.871  44.560  1.00 29.08           C  
-ATOM   2616  CD1 TYR C 349     -14.402  61.946  44.617  1.00 28.04           C  
-ATOM   2617  CD2 TYR C 349     -12.430  61.148  43.524  1.00 31.82           C  
-ATOM   2618  CE1 TYR C 349     -15.201  61.303  43.666  1.00 30.83           C  
-ATOM   2619  CE2 TYR C 349     -13.218  60.499  42.570  1.00 35.13           C  
-ATOM   2620  CZ  TYR C 349     -14.604  60.580  42.651  1.00 34.33           C  
-ATOM   2621  OH  TYR C 349     -15.387  59.907  41.740  1.00 26.85           O  
-ATOM   2622  N   HIS C 350     -10.995  63.046  48.511  1.00 25.89           N  
-ATOM   2623  CA  HIS C 350      -9.896  63.508  49.344  1.00 26.55           C  
-ATOM   2624  C   HIS C 350      -9.525  62.435  50.374  1.00 24.31           C  
-ATOM   2625  O   HIS C 350      -8.339  62.185  50.619  1.00 25.04           O  
-ATOM   2626  CB  HIS C 350     -10.274  64.809  50.049  1.00 25.93           C  
-ATOM   2627  CG  HIS C 350     -10.398  65.986  49.131  1.00 31.77           C  
-ATOM   2628  ND1 HIS C 350      -9.372  66.399  48.308  1.00 29.90           N  
-ATOM   2629  CD2 HIS C 350     -11.413  66.862  48.935  1.00 32.92           C  
-ATOM   2630  CE1 HIS C 350      -9.751  67.477  47.643  1.00 32.84           C  
-ATOM   2631  NE2 HIS C 350     -10.984  67.780  48.006  1.00 28.03           N  
-ATOM   2632  N   ILE C 351     -10.537  61.794  50.950  1.00 21.90           N  
-ATOM   2633  CA  ILE C 351     -10.314  60.755  51.949  1.00 24.45           C  
-ATOM   2634  C   ILE C 351      -9.559  59.549  51.387  1.00 25.64           C  
-ATOM   2635  O   ILE C 351      -8.552  59.128  51.962  1.00 24.35           O  
-ATOM   2636  CB  ILE C 351     -11.655  60.295  52.575  1.00 22.21           C  
-ATOM   2637  CG1 ILE C 351     -12.206  61.416  53.468  1.00 18.46           C  
-ATOM   2638  CG2 ILE C 351     -11.469  58.997  53.362  1.00 22.33           C  
-ATOM   2639  CD1 ILE C 351     -13.656  61.150  53.991  1.00 19.95           C  
-ATOM   2640  N   VAL C 352     -10.042  58.995  50.273  1.00 24.21           N  
-ATOM   2641  CA  VAL C 352      -9.382  57.858  49.657  1.00 23.54           C  
-ATOM   2642  C   VAL C 352      -7.960  58.240  49.225  1.00 23.09           C  
-ATOM   2643  O   VAL C 352      -7.035  57.464  49.381  1.00 21.94           O  
-ATOM   2644  CB  VAL C 352     -10.193  57.334  48.442  1.00 26.36           C  
-ATOM   2645  CG1 VAL C 352      -9.329  56.434  47.551  1.00 23.13           C  
-ATOM   2646  CG2 VAL C 352     -11.398  56.549  48.951  1.00 23.49           C  
-ATOM   2647  N   GLU C 353      -7.791  59.445  48.697  1.00 25.00           N  
-ATOM   2648  CA  GLU C 353      -6.478  59.894  48.262  1.00 25.83           C  
-ATOM   2649  C   GLU C 353      -5.477  59.986  49.434  1.00 25.16           C  
-ATOM   2650  O   GLU C 353      -4.344  59.527  49.337  1.00 21.51           O  
-ATOM   2651  CB  GLU C 353      -6.586  61.254  47.573  1.00 23.83           C  
-ATOM   2652  CG  GLU C 353      -5.264  61.704  46.957  1.00 29.27           C  
-ATOM   2653  CD  GLU C 353      -5.428  62.771  45.891  1.00 32.22           C  
-ATOM   2654  OE1 GLU C 353      -6.307  63.644  46.053  1.00 34.99           O  
-ATOM   2655  OE2 GLU C 353      -4.674  62.741  44.894  1.00 31.82           O  
-ATOM   2656  N   VAL C 354      -5.920  60.576  50.538  1.00 25.23           N  
-ATOM   2657  CA  VAL C 354      -5.080  60.734  51.715  1.00 23.86           C  
-ATOM   2658  C   VAL C 354      -4.680  59.361  52.259  1.00 23.25           C  
-ATOM   2659  O   VAL C 354      -3.535  59.150  52.673  1.00 20.62           O  
-ATOM   2660  CB  VAL C 354      -5.823  61.587  52.770  1.00 25.36           C  
-ATOM   2661  CG1 VAL C 354      -5.292  61.337  54.177  1.00 23.95           C  
-ATOM   2662  CG2 VAL C 354      -5.664  63.041  52.409  1.00 24.11           C  
-ATOM   2663  N   ILE C 355      -5.617  58.422  52.230  1.00 23.09           N  
-ATOM   2664  CA  ILE C 355      -5.325  57.084  52.704  1.00 21.56           C  
-ATOM   2665  C   ILE C 355      -4.266  56.408  51.835  1.00 23.30           C  
-ATOM   2666  O   ILE C 355      -3.328  55.809  52.358  1.00 22.41           O  
-ATOM   2667  CB  ILE C 355      -6.617  56.242  52.782  1.00 20.72           C  
-ATOM   2668  CG1 ILE C 355      -7.458  56.757  53.964  1.00 24.05           C  
-ATOM   2669  CG2 ILE C 355      -6.297  54.729  52.950  1.00 17.42           C  
-ATOM   2670  CD1 ILE C 355      -8.755  55.987  54.204  1.00 20.78           C  
-ATOM   2671  N   PHE C 356      -4.405  56.492  50.513  1.00 22.20           N  
-ATOM   2672  CA  PHE C 356      -3.408  55.872  49.655  1.00 24.02           C  
-ATOM   2673  C   PHE C 356      -2.070  56.588  49.802  1.00 22.71           C  
-ATOM   2674  O   PHE C 356      -1.018  55.962  49.694  1.00 23.38           O  
-ATOM   2675  CB  PHE C 356      -3.865  55.843  48.188  1.00 23.84           C  
-ATOM   2676  CG  PHE C 356      -4.812  54.719  47.892  1.00 26.18           C  
-ATOM   2677  CD1 PHE C 356      -4.482  53.423  48.246  1.00 19.55           C  
-ATOM   2678  CD2 PHE C 356      -6.056  54.958  47.329  1.00 27.40           C  
-ATOM   2679  CE1 PHE C 356      -5.372  52.391  48.049  1.00 26.88           C  
-ATOM   2680  CE2 PHE C 356      -6.950  53.921  47.130  1.00 25.90           C  
-ATOM   2681  CZ  PHE C 356      -6.611  52.644  47.494  1.00 23.16           C  
-ATOM   2682  N   ALA C 357      -2.121  57.889  50.073  1.00 21.78           N  
-ATOM   2683  CA  ALA C 357      -0.915  58.685  50.268  1.00 23.08           C  
-ATOM   2684  C   ALA C 357      -0.137  58.165  51.475  1.00 24.18           C  
-ATOM   2685  O   ALA C 357       1.099  58.170  51.472  1.00 24.92           O  
-ATOM   2686  CB  ALA C 357      -1.282  60.152  50.475  1.00 20.76           C  
-ATOM   2687  N   GLU C 358      -0.855  57.721  52.506  1.00 22.21           N  
-ATOM   2688  CA  GLU C 358      -0.203  57.179  53.688  1.00 23.33           C  
-ATOM   2689  C   GLU C 358       0.309  55.771  53.395  1.00 23.99           C  
-ATOM   2690  O   GLU C 358       1.462  55.449  53.682  1.00 22.43           O  
-ATOM   2691  CB  GLU C 358      -1.166  57.152  54.892  1.00 16.71           C  
-ATOM   2692  CG  GLU C 358      -1.551  58.567  55.391  1.00 19.21           C  
-ATOM   2693  CD  GLU C 358      -1.946  58.620  56.879  1.00 20.91           C  
-ATOM   2694  OE1 GLU C 358      -1.825  57.593  57.570  1.00 19.41           O  
-ATOM   2695  OE2 GLU C 358      -2.370  59.701  57.355  1.00 17.90           O  
-ATOM   2696  N   LEU C 359      -0.552  54.934  52.815  1.00 23.66           N  
-ATOM   2697  CA  LEU C 359      -0.176  53.562  52.502  1.00 23.32           C  
-ATOM   2698  C   LEU C 359       1.038  53.487  51.591  1.00 22.91           C  
-ATOM   2699  O   LEU C 359       1.865  52.583  51.728  1.00 22.80           O  
-ATOM   2700  CB  LEU C 359      -1.324  52.812  51.808  1.00 22.25           C  
-ATOM   2701  CG  LEU C 359      -0.967  51.357  51.477  1.00 25.64           C  
-ATOM   2702  CD1 LEU C 359      -0.735  50.601  52.779  1.00 19.55           C  
-ATOM   2703  CD2 LEU C 359      -2.075  50.686  50.658  1.00 23.94           C  
-ATOM   2704  N   PHE C 360       1.122  54.428  50.652  1.00 21.32           N  
-ATOM   2705  CA  PHE C 360       2.212  54.442  49.685  1.00 23.86           C  
-ATOM   2706  C   PHE C 360       3.379  55.357  50.051  1.00 22.78           C  
-ATOM   2707  O   PHE C 360       4.331  55.485  49.280  1.00 25.94           O  
-ATOM   2708  CB  PHE C 360       1.663  54.817  48.290  1.00 21.84           C  
-ATOM   2709  CG  PHE C 360       0.664  53.823  47.746  1.00 22.20           C  
-ATOM   2710  CD1 PHE C 360       0.859  52.458  47.929  1.00 20.82           C  
-ATOM   2711  CD2 PHE C 360      -0.473  54.251  47.064  1.00 23.62           C  
-ATOM   2712  CE1 PHE C 360      -0.068  51.531  47.445  1.00 23.55           C  
-ATOM   2713  CE2 PHE C 360      -1.402  53.334  46.576  1.00 22.77           C  
-ATOM   2714  CZ  PHE C 360      -1.197  51.970  46.768  1.00 19.58           C  
-ATOM   2715  N   GLN C 361       3.324  55.977  51.226  1.00 23.07           N  
-ATOM   2716  CA  GLN C 361       4.391  56.876  51.639  1.00 22.99           C  
-ATOM   2717  C   GLN C 361       5.736  56.160  51.741  1.00 24.26           C  
-ATOM   2718  O   GLN C 361       5.834  55.028  52.232  1.00 25.06           O  
-ATOM   2719  CB  GLN C 361       4.076  57.544  52.988  1.00 27.03           C  
-ATOM   2720  CG  GLN C 361       5.138  58.588  53.399  1.00 25.08           C  
-ATOM   2721  CD  GLN C 361       4.811  59.319  54.689  1.00 30.24           C  
-ATOM   2722  OE1 GLN C 361       4.468  60.500  54.673  1.00 30.54           O  
-ATOM   2723  NE2 GLN C 361       4.918  58.619  55.814  1.00 26.49           N  
-ATOM   2724  N   LEU C 362       6.772  56.840  51.268  1.00 25.02           N  
-ATOM   2725  CA  LEU C 362       8.133  56.307  51.308  1.00 25.20           C  
-ATOM   2726  C   LEU C 362       8.931  57.211  52.243  1.00 23.83           C  
-ATOM   2727  O   LEU C 362       8.784  58.431  52.202  1.00 23.72           O  
-ATOM   2728  CB  LEU C 362       8.747  56.301  49.895  1.00 22.69           C  
-ATOM   2729  CG  LEU C 362       8.044  55.350  48.912  1.00 22.76           C  
-ATOM   2730  CD1 LEU C 362       8.680  55.413  47.533  1.00 23.83           C  
-ATOM   2731  CD2 LEU C 362       8.099  53.929  49.457  1.00 19.31           C  
-ATOM   2732  N   PRO C 363       9.776  56.629  53.117  1.00 24.05           N  
-ATOM   2733  CA  PRO C 363      10.075  55.206  53.321  1.00 24.60           C  
-ATOM   2734  C   PRO C 363       8.895  54.363  53.792  1.00 22.58           C  
-ATOM   2735  O   PRO C 363       8.688  53.252  53.316  1.00 25.44           O  
-ATOM   2736  CB  PRO C 363      11.176  55.218  54.398  1.00 25.13           C  
-ATOM   2737  CG  PRO C 363      11.774  56.575  54.295  1.00 23.14           C  
-ATOM   2738  CD  PRO C 363      10.570  57.455  54.042  1.00 22.23           C  
-ATOM   2739  N   ALA C 364       8.121  54.882  54.735  1.00 23.68           N  
-ATOM   2740  CA  ALA C 364       7.029  54.086  55.269  1.00 21.88           C  
-ATOM   2741  C   ALA C 364       5.759  54.825  55.634  1.00 19.65           C  
-ATOM   2742  O   ALA C 364       5.751  56.049  55.805  1.00 23.03           O  
-ATOM   2743  CB  ALA C 364       7.534  53.294  56.512  1.00 25.43           C  
-ATOM   2744  N   PRO C 365       4.650  54.076  55.754  1.00 20.54           N  
-ATOM   2745  CA  PRO C 365       3.359  54.664  56.120  1.00 20.35           C  
-ATOM   2746  C   PRO C 365       3.446  55.146  57.577  1.00 20.79           C  
-ATOM   2747  O   PRO C 365       4.273  54.668  58.351  1.00 21.63           O  
-ATOM   2748  CB  PRO C 365       2.382  53.483  56.003  1.00 21.62           C  
-ATOM   2749  CG  PRO C 365       3.062  52.528  55.054  1.00 24.76           C  
-ATOM   2750  CD  PRO C 365       4.514  52.632  55.459  1.00 17.10           C  
-ATOM   2751  N   PRO C 366       2.596  56.101  57.965  1.00 22.30           N  
-ATOM   2752  CA  PRO C 366       2.650  56.571  59.354  1.00 24.38           C  
-ATOM   2753  C   PRO C 366       2.158  55.500  60.333  1.00 23.78           C  
-ATOM   2754  O   PRO C 366       2.548  55.513  61.487  1.00 26.34           O  
-ATOM   2755  CB  PRO C 366       1.730  57.800  59.349  1.00 24.27           C  
-ATOM   2756  CG  PRO C 366       1.852  58.308  57.933  1.00 24.93           C  
-ATOM   2757  CD  PRO C 366       1.820  57.027  57.121  1.00 27.68           C  
-ATOM   2758  N   HIS C 367       1.326  54.570  59.857  1.00 21.99           N  
-ATOM   2759  CA  HIS C 367       0.753  53.514  60.698  1.00 23.00           C  
-ATOM   2760  C   HIS C 367       0.876  52.135  60.049  1.00 22.96           C  
-ATOM   2761  O   HIS C 367       1.141  52.019  58.844  1.00 24.31           O  
-ATOM   2762  CB  HIS C 367      -0.736  53.822  60.952  1.00 23.12           C  
-ATOM   2763  CG  HIS C 367      -0.992  55.241  61.360  1.00 24.23           C  
-ATOM   2764  ND1 HIS C 367      -0.627  55.735  62.594  1.00 24.61           N  
-ATOM   2765  CD2 HIS C 367      -1.491  56.293  60.667  1.00 26.69           C  
-ATOM   2766  CE1 HIS C 367      -0.881  57.031  62.641  1.00 24.20           C  
-ATOM   2767  NE2 HIS C 367      -1.404  57.395  61.485  1.00 26.82           N  
-ATOM   2768  N   ILE C 368       0.676  51.089  60.843  1.00 21.31           N  
-ATOM   2769  CA  ILE C 368       0.749  49.724  60.326  1.00 21.84           C  
-ATOM   2770  C   ILE C 368      -0.167  49.587  59.100  1.00 23.33           C  
-ATOM   2771  O   ILE C 368      -1.306  50.061  59.107  1.00 24.22           O  
-ATOM   2772  CB  ILE C 368       0.376  48.695  61.426  1.00 23.13           C  
-ATOM   2773  CG1 ILE C 368       0.580  47.272  60.903  1.00 24.90           C  
-ATOM   2774  CG2 ILE C 368      -1.049  48.922  61.906  1.00 21.22           C  
-ATOM   2775  CD1 ILE C 368       0.409  46.180  61.970  1.00 25.68           C  
-ATOM   2776  N   ASP C 369       0.350  48.963  58.042  1.00 22.79           N  
-ATOM   2777  CA  ASP C 369      -0.372  48.805  56.782  1.00 22.38           C  
-ATOM   2778  C   ASP C 369      -1.798  48.257  56.871  1.00 24.14           C  
-ATOM   2779  O   ASP C 369      -2.708  48.789  56.242  1.00 21.68           O  
-ATOM   2780  CB  ASP C 369       0.414  47.906  55.826  1.00 26.73           C  
-ATOM   2781  CG  ASP C 369       1.783  48.459  55.475  1.00 30.38           C  
-ATOM   2782  OD1 ASP C 369       2.330  49.273  56.246  1.00 36.65           O  
-ATOM   2783  OD2 ASP C 369       2.325  48.057  54.427  1.00 35.53           O  
-ATOM   2784  N   VAL C 370      -1.988  47.191  57.640  1.00 24.08           N  
-ATOM   2785  CA  VAL C 370      -3.306  46.579  57.753  1.00 25.65           C  
-ATOM   2786  C   VAL C 370      -4.430  47.518  58.237  1.00 27.47           C  
-ATOM   2787  O   VAL C 370      -5.599  47.302  57.913  1.00 30.79           O  
-ATOM   2788  CB  VAL C 370      -3.246  45.305  58.639  1.00 24.45           C  
-ATOM   2789  CG1 VAL C 370      -3.046  45.678  60.096  1.00 23.30           C  
-ATOM   2790  CG2 VAL C 370      -4.512  44.467  58.440  1.00 24.63           C  
-ATOM   2791  N   MET C 371      -4.081  48.558  58.992  1.00 26.00           N  
-ATOM   2792  CA  MET C 371      -5.075  49.512  59.484  1.00 26.07           C  
-ATOM   2793  C   MET C 371      -5.805  50.212  58.322  1.00 27.20           C  
-ATOM   2794  O   MET C 371      -7.016  50.486  58.397  1.00 22.10           O  
-ATOM   2795  CB  MET C 371      -4.408  50.580  60.363  1.00 25.23           C  
-ATOM   2796  CG  MET C 371      -5.358  51.680  60.877  1.00 28.52           C  
-ATOM   2797  SD  MET C 371      -5.755  52.991  59.689  1.00 32.73           S  
-ATOM   2798  CE  MET C 371      -4.261  54.015  59.879  1.00 31.96           C  
-ATOM   2799  N   TYR C 372      -5.066  50.509  57.257  1.00 22.41           N  
-ATOM   2800  CA  TYR C 372      -5.661  51.191  56.120  1.00 24.79           C  
-ATOM   2801  C   TYR C 372      -6.712  50.339  55.410  1.00 24.62           C  
-ATOM   2802  O   TYR C 372      -7.685  50.867  54.883  1.00 25.69           O  
-ATOM   2803  CB  TYR C 372      -4.571  51.637  55.143  1.00 21.17           C  
-ATOM   2804  CG  TYR C 372      -3.598  52.615  55.777  1.00 21.51           C  
-ATOM   2805  CD1 TYR C 372      -3.992  53.916  56.094  1.00 21.41           C  
-ATOM   2806  CD2 TYR C 372      -2.300  52.224  56.100  1.00 21.05           C  
-ATOM   2807  CE1 TYR C 372      -3.108  54.814  56.724  1.00 23.98           C  
-ATOM   2808  CE2 TYR C 372      -1.404  53.111  56.728  1.00 20.60           C  
-ATOM   2809  CZ  TYR C 372      -1.814  54.399  57.035  1.00 19.59           C  
-ATOM   2810  OH  TYR C 372      -0.922  55.270  57.640  1.00 21.06           O  
-ATOM   2811  N   THR C 373      -6.513  49.026  55.400  1.00 24.48           N  
-ATOM   2812  CA  THR C 373      -7.459  48.120  54.765  1.00 24.59           C  
-ATOM   2813  C   THR C 373      -8.793  48.139  55.517  1.00 25.55           C  
-ATOM   2814  O   THR C 373      -9.860  48.281  54.918  1.00 25.30           O  
-ATOM   2815  CB  THR C 373      -6.919  46.674  54.756  1.00 27.18           C  
-ATOM   2816  OG1 THR C 373      -5.662  46.643  54.063  1.00 28.46           O  
-ATOM   2817  CG2 THR C 373      -7.924  45.718  54.052  1.00 21.60           C  
-ATOM   2818  N   THR C 374      -8.713  47.991  56.834  1.00 25.44           N  
-ATOM   2819  CA  THR C 374      -9.892  47.975  57.677  1.00 27.27           C  
-ATOM   2820  C   THR C 374     -10.538  49.356  57.720  1.00 26.29           C  
-ATOM   2821  O   THR C 374     -11.756  49.469  57.790  1.00 26.85           O  
-ATOM   2822  CB  THR C 374      -9.534  47.508  59.100  1.00 26.69           C  
-ATOM   2823  OG1 THR C 374      -8.733  46.323  59.017  1.00 33.37           O  
-ATOM   2824  CG2 THR C 374     -10.786  47.156  59.876  1.00 28.77           C  
-ATOM   2825  N   LEU C 375      -9.722  50.402  57.666  1.00 25.69           N  
-ATOM   2826  CA  LEU C 375     -10.230  51.765  57.673  1.00 25.03           C  
-ATOM   2827  C   LEU C 375     -11.074  52.025  56.410  1.00 26.48           C  
-ATOM   2828  O   LEU C 375     -12.119  52.674  56.472  1.00 22.86           O  
-ATOM   2829  CB  LEU C 375      -9.079  52.774  57.732  1.00 24.26           C  
-ATOM   2830  CG  LEU C 375      -9.514  54.246  57.650  1.00 25.79           C  
-ATOM   2831  CD1 LEU C 375     -10.519  54.572  58.760  1.00 29.01           C  
-ATOM   2832  CD2 LEU C 375      -8.298  55.156  57.772  1.00 25.89           C  
-ATOM   2833  N   LEU C 376     -10.616  51.529  55.265  1.00 24.44           N  
-ATOM   2834  CA  LEU C 376     -11.381  51.735  54.035  1.00 25.12           C  
-ATOM   2835  C   LEU C 376     -12.695  50.938  54.087  1.00 26.58           C  
-ATOM   2836  O   LEU C 376     -13.724  51.354  53.547  1.00 25.71           O  
-ATOM   2837  CB  LEU C 376     -10.550  51.329  52.819  1.00 20.10           C  
-ATOM   2838  CG  LEU C 376      -9.470  52.325  52.377  1.00 21.22           C  
-ATOM   2839  CD1 LEU C 376      -8.571  51.655  51.344  1.00 18.61           C  
-ATOM   2840  CD2 LEU C 376     -10.117  53.600  51.777  1.00 18.90           C  
-ATOM   2841  N   ILE C 377     -12.661  49.781  54.735  1.00 28.33           N  
-ATOM   2842  CA  ILE C 377     -13.870  48.980  54.858  1.00 28.27           C  
-ATOM   2843  C   ILE C 377     -14.883  49.751  55.713  1.00 28.54           C  
-ATOM   2844  O   ILE C 377     -16.064  49.824  55.369  1.00 30.43           O  
-ATOM   2845  CB  ILE C 377     -13.552  47.608  55.494  1.00 28.22           C  
-ATOM   2846  CG1 ILE C 377     -12.818  46.736  54.466  1.00 24.40           C  
-ATOM   2847  CG2 ILE C 377     -14.833  46.923  55.986  1.00 27.09           C  
-ATOM   2848  CD1 ILE C 377     -12.249  45.427  55.053  1.00 22.06           C  
-ATOM   2849  N   GLU C 378     -14.418  50.331  56.817  1.00 26.55           N  
-ATOM   2850  CA  GLU C 378     -15.288  51.104  57.702  1.00 27.54           C  
-ATOM   2851  C   GLU C 378     -15.861  52.328  56.981  1.00 27.03           C  
-ATOM   2852  O   GLU C 378     -16.966  52.769  57.285  1.00 27.98           O  
-ATOM   2853  CB  GLU C 378     -14.523  51.576  58.952  1.00 28.29           C  
-ATOM   2854  CG  GLU C 378     -14.113  50.478  59.947  1.00 31.89           C  
-ATOM   2855  CD  GLU C 378     -15.297  49.806  60.651  1.00 38.90           C  
-ATOM   2856  OE1 GLU C 378     -16.412  50.379  60.654  1.00 36.10           O  
-ATOM   2857  OE2 GLU C 378     -15.108  48.708  61.218  1.00 38.49           O  
-ATOM   2858  N   LEU C 379     -15.093  52.905  56.061  1.00 24.95           N  
-ATOM   2859  CA  LEU C 379     -15.570  54.058  55.302  1.00 26.71           C  
-ATOM   2860  C   LEU C 379     -16.638  53.631  54.289  1.00 28.57           C  
-ATOM   2861  O   LEU C 379     -17.606  54.347  54.059  1.00 28.41           O  
-ATOM   2862  CB  LEU C 379     -14.410  54.756  54.590  1.00 26.26           C  
-ATOM   2863  CG  LEU C 379     -13.503  55.544  55.542  1.00 22.92           C  
-ATOM   2864  CD1 LEU C 379     -12.127  55.749  54.915  1.00 18.24           C  
-ATOM   2865  CD2 LEU C 379     -14.165  56.880  55.895  1.00 24.77           C  
-ATOM   2866  N   CYS C 380     -16.457  52.464  53.686  1.00 28.81           N  
-ATOM   2867  CA  CYS C 380     -17.433  51.948  52.738  1.00 30.21           C  
-ATOM   2868  C   CYS C 380     -18.770  51.746  53.468  1.00 30.50           C  
-ATOM   2869  O   CYS C 380     -19.843  52.005  52.920  1.00 29.63           O  
-ATOM   2870  CB  CYS C 380     -16.947  50.616  52.158  1.00 31.10           C  
-ATOM   2871  SG  CYS C 380     -15.686  50.793  50.863  1.00 32.98           S  
-ATOM   2872  N   LYS C 381     -18.685  51.308  54.720  1.00 27.20           N  
-ATOM   2873  CA  LYS C 381     -19.862  51.068  55.538  1.00 26.67           C  
-ATOM   2874  C   LYS C 381     -20.586  52.344  55.897  1.00 27.65           C  
-ATOM   2875  O   LYS C 381     -21.803  52.345  56.068  1.00 26.84           O  
-ATOM   2876  CB  LYS C 381     -19.475  50.365  56.829  1.00 22.77           C  
-ATOM   2877  CG  LYS C 381     -19.165  48.909  56.669  1.00 27.54           C  
-ATOM   2878  CD  LYS C 381     -18.716  48.359  58.000  1.00 32.70           C  
-ATOM   2879  CE  LYS C 381     -18.832  46.864  58.031  1.00 36.39           C  
-ATOM   2880  NZ  LYS C 381     -18.505  46.370  59.394  1.00 41.38           N  
-ATOM   2881  N   LEU C 382     -19.826  53.424  56.001  1.00 25.92           N  
-ATOM   2882  CA  LEU C 382     -20.361  54.715  56.381  1.00 28.94           C  
-ATOM   2883  C   LEU C 382     -20.931  55.541  55.229  1.00 29.26           C  
-ATOM   2884  O   LEU C 382     -21.815  56.367  55.431  1.00 31.46           O  
-ATOM   2885  CB  LEU C 382     -19.259  55.494  57.088  1.00 28.04           C  
-ATOM   2886  CG  LEU C 382     -19.648  56.411  58.229  1.00 35.63           C  
-ATOM   2887  CD1 LEU C 382     -20.541  55.669  59.234  1.00 31.53           C  
-ATOM   2888  CD2 LEU C 382     -18.369  56.892  58.877  1.00 33.24           C  
-ATOM   2889  N   GLN C 383     -20.411  55.330  54.026  1.00 28.76           N  
-ATOM   2890  CA  GLN C 383     -20.873  56.052  52.838  1.00 30.35           C  
-ATOM   2891  C   GLN C 383     -21.121  55.004  51.775  1.00 31.35           C  
-ATOM   2892  O   GLN C 383     -20.533  55.051  50.687  1.00 32.51           O  
-ATOM   2893  CB  GLN C 383     -19.798  57.025  52.350  1.00 30.97           C  
-ATOM   2894  CG  GLN C 383     -19.467  58.129  53.331  1.00 33.30           C  
-ATOM   2895  CD  GLN C 383     -20.485  59.248  53.293  1.00 42.56           C  
-ATOM   2896  OE1 GLN C 383     -20.345  60.194  52.521  1.00 42.70           O  
-ATOM   2897  NE2 GLN C 383     -21.527  59.136  54.115  1.00 45.27           N  
-ATOM   2898  N   PRO C 384     -22.013  54.047  52.070  1.00 31.57           N  
-ATOM   2899  CA  PRO C 384     -22.369  52.944  51.173  1.00 33.11           C  
-ATOM   2900  C   PRO C 384     -22.773  53.341  49.760  1.00 32.76           C  
-ATOM   2901  O   PRO C 384     -22.531  52.602  48.823  1.00 34.91           O  
-ATOM   2902  CB  PRO C 384     -23.515  52.248  51.908  1.00 32.54           C  
-ATOM   2903  CG  PRO C 384     -23.354  52.676  53.323  1.00 38.95           C  
-ATOM   2904  CD  PRO C 384     -22.951  54.105  53.201  1.00 33.60           C  
-ATOM   2905  N   GLY C 385     -23.385  54.507  49.613  1.00 35.26           N  
-ATOM   2906  CA  GLY C 385     -23.824  54.937  48.297  1.00 39.30           C  
-ATOM   2907  C   GLY C 385     -22.829  55.724  47.462  1.00 41.81           C  
-ATOM   2908  O   GLY C 385     -23.138  56.081  46.323  1.00 41.13           O  
-ATOM   2909  N   SER C 386     -21.638  55.985  47.998  1.00 40.62           N  
-ATOM   2910  CA  SER C 386     -20.655  56.761  47.252  1.00 39.48           C  
-ATOM   2911  C   SER C 386     -19.181  56.350  47.374  1.00 38.74           C  
-ATOM   2912  O   SER C 386     -18.458  56.382  46.382  1.00 40.04           O  
-ATOM   2913  CB  SER C 386     -20.812  58.238  47.615  1.00 39.31           C  
-ATOM   2914  OG  SER C 386     -20.882  58.409  49.021  1.00 47.05           O  
-ATOM   2915  N   LEU C 387     -18.748  55.948  48.569  1.00 36.68           N  
-ATOM   2916  CA  LEU C 387     -17.352  55.568  48.804  1.00 33.65           C  
-ATOM   2917  C   LEU C 387     -16.895  54.363  47.984  1.00 31.46           C  
-ATOM   2918  O   LEU C 387     -15.849  54.412  47.356  1.00 29.45           O  
-ATOM   2919  CB  LEU C 387     -17.119  55.300  50.302  1.00 33.15           C  
-ATOM   2920  CG  LEU C 387     -15.711  55.286  50.923  1.00 35.06           C  
-ATOM   2921  CD1 LEU C 387     -14.860  54.184  50.334  1.00 33.26           C  
-ATOM   2922  CD2 LEU C 387     -15.072  56.640  50.728  1.00 33.75           C  
-ATOM   2923  N   PRO C 388     -17.664  53.260  47.992  1.00 31.48           N  
-ATOM   2924  CA  PRO C 388     -17.282  52.070  47.225  1.00 32.52           C  
-ATOM   2925  C   PRO C 388     -16.946  52.350  45.752  1.00 34.95           C  
-ATOM   2926  O   PRO C 388     -16.048  51.717  45.181  1.00 32.88           O  
-ATOM   2927  CB  PRO C 388     -18.499  51.163  47.373  1.00 33.12           C  
-ATOM   2928  CG  PRO C 388     -18.990  51.505  48.742  1.00 33.01           C  
-ATOM   2929  CD  PRO C 388     -18.893  53.008  48.768  1.00 31.64           C  
-ATOM   2930  N   GLN C 389     -17.673  53.293  45.150  1.00 33.31           N  
-ATOM   2931  CA  GLN C 389     -17.462  53.656  43.750  1.00 33.75           C  
-ATOM   2932  C   GLN C 389     -16.181  54.477  43.587  1.00 32.29           C  
-ATOM   2933  O   GLN C 389     -15.449  54.315  42.611  1.00 29.55           O  
-ATOM   2934  CB  GLN C 389     -18.634  54.487  43.197  1.00 34.45           C  
-ATOM   2935  CG  GLN C 389     -19.999  53.814  43.217  1.00 46.15           C  
-ATOM   2936  CD  GLN C 389     -20.802  54.120  44.477  1.00 52.73           C  
-ATOM   2937  OE1 GLN C 389     -20.454  53.689  45.582  1.00 51.02           O  
-ATOM   2938  NE2 GLN C 389     -21.887  54.873  44.311  1.00 54.42           N  
-ATOM   2939  N   VAL C 390     -15.938  55.392  44.520  1.00 30.84           N  
-ATOM   2940  CA  VAL C 390     -14.740  56.213  44.456  1.00 31.10           C  
-ATOM   2941  C   VAL C 390     -13.521  55.301  44.626  1.00 30.83           C  
-ATOM   2942  O   VAL C 390     -12.494  55.501  43.976  1.00 30.94           O  
-ATOM   2943  CB  VAL C 390     -14.773  57.317  45.539  1.00 31.23           C  
-ATOM   2944  CG1 VAL C 390     -13.437  58.051  45.607  1.00 29.79           C  
-ATOM   2945  CG2 VAL C 390     -15.891  58.317  45.205  1.00 34.03           C  
-ATOM   2946  N   LEU C 391     -13.668  54.270  45.453  1.00 28.23           N  
-ATOM   2947  CA  LEU C 391     -12.585  53.332  45.719  1.00 30.67           C  
-ATOM   2948  C   LEU C 391     -12.318  52.403  44.547  1.00 31.60           C  
-ATOM   2949  O   LEU C 391     -11.160  52.104  44.250  1.00 31.06           O  
-ATOM   2950  CB  LEU C 391     -12.891  52.505  46.973  1.00 26.21           C  
-ATOM   2951  CG  LEU C 391     -11.812  51.529  47.459  1.00 31.05           C  
-ATOM   2952  CD1 LEU C 391     -10.489  52.280  47.713  1.00 25.28           C  
-ATOM   2953  CD2 LEU C 391     -12.286  50.849  48.734  1.00 26.09           C  
-ATOM   2954  N   ALA C 392     -13.381  51.924  43.900  1.00 30.48           N  
-ATOM   2955  CA  ALA C 392     -13.224  51.038  42.749  1.00 31.47           C  
-ATOM   2956  C   ALA C 392     -12.513  51.816  41.658  1.00 30.91           C  
-ATOM   2957  O   ALA C 392     -11.657  51.284  40.949  1.00 32.93           O  
-ATOM   2958  CB  ALA C 392     -14.581  50.568  42.244  1.00 33.85           C  
-ATOM   2959  N   GLN C 393     -12.885  53.085  41.543  1.00 28.84           N  
-ATOM   2960  CA  GLN C 393     -12.322  53.991  40.564  1.00 30.62           C  
-ATOM   2961  C   GLN C 393     -10.828  54.207  40.838  1.00 31.88           C  
-ATOM   2962  O   GLN C 393     -10.007  54.138  39.922  1.00 32.90           O  
-ATOM   2963  CB  GLN C 393     -13.063  55.329  40.627  1.00 28.35           C  
-ATOM   2964  CG  GLN C 393     -12.689  56.296  39.535  1.00 27.25           C  
-ATOM   2965  CD  GLN C 393     -13.318  57.655  39.721  1.00 28.69           C  
-ATOM   2966  OE1 GLN C 393     -14.205  57.827  40.553  1.00 37.01           O  
-ATOM   2967  NE2 GLN C 393     -12.865  58.636  38.944  1.00 35.86           N  
-ATOM   2968  N   ALA C 394     -10.481  54.469  42.096  1.00 29.89           N  
-ATOM   2969  CA  ALA C 394      -9.081  54.682  42.466  1.00 28.50           C  
-ATOM   2970  C   ALA C 394      -8.288  53.416  42.190  1.00 28.01           C  
-ATOM   2971  O   ALA C 394      -7.145  53.471  41.736  1.00 29.38           O  
-ATOM   2972  CB  ALA C 394      -8.963  55.059  43.947  1.00 26.36           C  
-ATOM   2973  N   THR C 395      -8.899  52.269  42.461  1.00 25.66           N  
-ATOM   2974  CA  THR C 395      -8.234  51.001  42.236  1.00 26.90           C  
-ATOM   2975  C   THR C 395      -7.977  50.806  40.745  1.00 31.12           C  
-ATOM   2976  O   THR C 395      -6.968  50.204  40.350  1.00 30.87           O  
-ATOM   2977  CB  THR C 395      -9.079  49.839  42.758  1.00 26.27           C  
-ATOM   2978  OG1 THR C 395      -9.194  49.940  44.181  1.00 31.82           O  
-ATOM   2979  CG2 THR C 395      -8.440  48.500  42.398  1.00 24.68           C  
-ATOM   2980  N   GLU C 396      -8.893  51.310  39.924  1.00 29.91           N  
-ATOM   2981  CA  GLU C 396      -8.752  51.200  38.480  1.00 31.68           C  
-ATOM   2982  C   GLU C 396      -7.593  52.095  38.075  1.00 30.88           C  
-ATOM   2983  O   GLU C 396      -6.720  51.685  37.311  1.00 30.18           O  
-ATOM   2984  CB  GLU C 396     -10.049  51.647  37.787  1.00 32.79           C  
-ATOM   2985  CG  GLU C 396      -9.979  51.777  36.276  1.00 40.25           C  
-ATOM   2986  CD  GLU C 396      -9.575  50.490  35.580  1.00 46.21           C  
-ATOM   2987  OE1 GLU C 396     -10.112  49.412  35.916  1.00 49.88           O  
-ATOM   2988  OE2 GLU C 396      -8.717  50.561  34.681  1.00 51.98           O  
-ATOM   2989  N   MET C 397      -7.580  53.316  38.603  1.00 31.67           N  
-ATOM   2990  CA  MET C 397      -6.516  54.263  38.292  1.00 34.05           C  
-ATOM   2991  C   MET C 397      -5.131  53.749  38.713  1.00 34.37           C  
-ATOM   2992  O   MET C 397      -4.186  53.806  37.928  1.00 36.03           O  
-ATOM   2993  CB  MET C 397      -6.819  55.612  38.942  1.00 33.54           C  
-ATOM   2994  CG  MET C 397      -7.989  56.328  38.290  1.00 40.83           C  
-ATOM   2995  SD  MET C 397      -8.769  57.583  39.321  1.00 38.89           S  
-ATOM   2996  CE  MET C 397      -7.543  58.870  39.313  1.00 39.53           C  
-ATOM   2997  N   LEU C 398      -5.012  53.231  39.934  1.00 33.20           N  
-ATOM   2998  CA  LEU C 398      -3.729  52.703  40.409  1.00 32.19           C  
-ATOM   2999  C   LEU C 398      -3.236  51.603  39.464  1.00 32.18           C  
-ATOM   3000  O   LEU C 398      -2.049  51.537  39.136  1.00 32.95           O  
-ATOM   3001  CB  LEU C 398      -3.861  52.135  41.836  1.00 25.38           C  
-ATOM   3002  CG  LEU C 398      -4.204  53.107  42.975  1.00 24.69           C  
-ATOM   3003  CD1 LEU C 398      -4.357  52.323  44.262  1.00 26.87           C  
-ATOM   3004  CD2 LEU C 398      -3.127  54.178  43.125  1.00 25.06           C  
-ATOM   3005  N   TYR C 399      -4.146  50.733  39.040  1.00 31.31           N  
-ATOM   3006  CA  TYR C 399      -3.787  49.655  38.121  1.00 32.03           C  
-ATOM   3007  C   TYR C 399      -3.217  50.211  36.815  1.00 31.87           C  
-ATOM   3008  O   TYR C 399      -2.147  49.800  36.364  1.00 32.36           O  
-ATOM   3009  CB  TYR C 399      -5.009  48.803  37.781  1.00 32.18           C  
-ATOM   3010  CG  TYR C 399      -4.737  47.735  36.738  1.00 31.14           C  
-ATOM   3011  CD1 TYR C 399      -4.272  46.482  37.110  1.00 31.52           C  
-ATOM   3012  CD2 TYR C 399      -4.918  47.993  35.376  1.00 29.49           C  
-ATOM   3013  CE1 TYR C 399      -3.996  45.503  36.157  1.00 34.44           C  
-ATOM   3014  CE2 TYR C 399      -4.638  47.022  34.413  1.00 29.12           C  
-ATOM   3015  CZ  TYR C 399      -4.182  45.780  34.813  1.00 33.96           C  
-ATOM   3016  OH  TYR C 399      -3.941  44.796  33.880  1.00 36.87           O  
-ATOM   3017  N   MET C 400      -3.942  51.148  36.213  1.00 31.93           N  
-ATOM   3018  CA  MET C 400      -3.535  51.749  34.945  1.00 33.14           C  
-ATOM   3019  C   MET C 400      -2.257  52.594  35.006  1.00 34.91           C  
-ATOM   3020  O   MET C 400      -1.715  52.989  33.967  1.00 32.31           O  
-ATOM   3021  CB  MET C 400      -4.672  52.613  34.394  1.00 34.80           C  
-ATOM   3022  CG  MET C 400      -5.878  51.831  33.885  1.00 40.49           C  
-ATOM   3023  SD  MET C 400      -5.448  50.728  32.507  1.00 47.18           S  
-ATOM   3024  CE  MET C 400      -6.497  49.309  32.850  1.00 43.13           C  
-ATOM   3025  N   ARG C 401      -1.782  52.898  36.210  1.00 33.49           N  
-ATOM   3026  CA  ARG C 401      -0.566  53.695  36.336  1.00 32.35           C  
-ATOM   3027  C   ARG C 401       0.590  52.865  36.883  1.00 30.70           C  
-ATOM   3028  O   ARG C 401       1.657  53.394  37.196  1.00 34.12           O  
-ATOM   3029  CB  ARG C 401      -0.834  54.906  37.232  1.00 32.45           C  
-ATOM   3030  CG  ARG C 401      -1.878  55.827  36.643  1.00 33.95           C  
-ATOM   3031  CD  ARG C 401      -2.268  56.973  37.554  1.00 33.98           C  
-ATOM   3032  NE  ARG C 401      -3.477  57.617  37.047  1.00 28.72           N  
-ATOM   3033  CZ  ARG C 401      -4.134  58.591  37.660  1.00 33.30           C  
-ATOM   3034  NH1 ARG C 401      -3.706  59.061  38.831  1.00 34.61           N  
-ATOM   3035  NH2 ARG C 401      -5.222  59.101  37.096  1.00 30.49           N  
-ATOM   3036  N   LEU C 402       0.371  51.560  36.963  1.00 28.95           N  
-ATOM   3037  CA  LEU C 402       1.347  50.622  37.492  1.00 33.05           C  
-ATOM   3038  C   LEU C 402       2.710  50.553  36.807  1.00 34.85           C  
-ATOM   3039  O   LEU C 402       3.682  50.125  37.430  1.00 36.11           O  
-ATOM   3040  CB  LEU C 402       0.740  49.214  37.523  1.00 28.78           C  
-ATOM   3041  CG  LEU C 402      -0.008  48.748  38.784  1.00 35.37           C  
-ATOM   3042  CD1 LEU C 402      -0.687  47.413  38.521  1.00 22.75           C  
-ATOM   3043  CD2 LEU C 402       0.970  48.607  39.953  1.00 27.18           C  
-ATOM   3044  N   ASP C 403       2.796  50.964  35.544  1.00 37.40           N  
-ATOM   3045  CA  ASP C 403       4.072  50.882  34.828  1.00 38.72           C  
-ATOM   3046  C   ASP C 403       5.249  51.613  35.485  1.00 37.07           C  
-ATOM   3047  O   ASP C 403       6.364  51.102  35.477  1.00 38.45           O  
-ATOM   3048  CB  ASP C 403       3.927  51.356  33.370  1.00 40.28           C  
-ATOM   3049  CG  ASP C 403       3.099  50.401  32.513  1.00 43.12           C  
-ATOM   3050  OD1 ASP C 403       3.184  49.175  32.724  1.00 39.61           O  
-ATOM   3051  OD2 ASP C 403       2.372  50.881  31.614  1.00 49.37           O  
-ATOM   3052  N   THR C 404       5.029  52.801  36.042  1.00 35.70           N  
-ATOM   3053  CA  THR C 404       6.136  53.506  36.680  1.00 34.15           C  
-ATOM   3054  C   THR C 404       6.026  53.547  38.201  1.00 33.82           C  
-ATOM   3055  O   THR C 404       6.725  54.320  38.843  1.00 31.24           O  
-ATOM   3056  CB  THR C 404       6.284  54.965  36.180  1.00 34.58           C  
-ATOM   3057  OG1 THR C 404       5.261  55.784  36.759  1.00 36.31           O  
-ATOM   3058  CG2 THR C 404       6.197  55.029  34.652  1.00 38.43           C  
-ATOM   3059  N   MET C 405       5.156  52.720  38.775  1.00 33.57           N  
-ATOM   3060  CA  MET C 405       4.994  52.696  40.228  1.00 33.04           C  
-ATOM   3061  C   MET C 405       6.158  51.967  40.914  1.00 31.86           C  
-ATOM   3062  O   MET C 405       6.552  50.873  40.509  1.00 28.63           O  
-ATOM   3063  CB  MET C 405       3.672  52.019  40.620  1.00 32.25           C  
-ATOM   3064  CG  MET C 405       3.358  52.089  42.129  1.00 29.05           C  
-ATOM   3065  SD  MET C 405       1.749  51.385  42.620  1.00 29.99           S  
-ATOM   3066  CE  MET C 405       0.925  52.823  43.329  1.00 31.21           C  
-ATOM   3067  N   ASN C 406       6.687  52.575  41.971  1.00 32.64           N  
-ATOM   3068  CA  ASN C 406       7.801  51.982  42.709  1.00 31.72           C  
-ATOM   3069  C   ASN C 406       7.435  50.641  43.337  1.00 30.36           C  
-ATOM   3070  O   ASN C 406       6.372  50.497  43.939  1.00 31.69           O  
-ATOM   3071  CB  ASN C 406       8.284  52.944  43.793  1.00 31.89           C  
-ATOM   3072  CG  ASN C 406       9.639  52.554  44.347  1.00 34.37           C  
-ATOM   3073  OD1 ASN C 406       9.742  51.729  45.253  1.00 33.54           O  
-ATOM   3074  ND2 ASN C 406      10.693  53.136  43.783  1.00 30.61           N  
-ATOM   3075  N   THR C 407       8.340  49.672  43.202  1.00 28.25           N  
-ATOM   3076  CA  THR C 407       8.156  48.321  43.723  1.00 28.05           C  
-ATOM   3077  C   THR C 407       7.697  48.231  45.187  1.00 29.17           C  
-ATOM   3078  O   THR C 407       6.919  47.337  45.542  1.00 29.57           O  
-ATOM   3079  CB  THR C 407       9.469  47.485  43.560  1.00 28.12           C  
-ATOM   3080  OG1 THR C 407       9.749  47.289  42.168  1.00 31.72           O  
-ATOM   3081  CG2 THR C 407       9.336  46.123  44.219  1.00 30.03           C  
-ATOM   3082  N   THR C 408       8.195  49.115  46.048  1.00 27.35           N  
-ATOM   3083  CA  THR C 408       7.777  49.060  47.449  1.00 29.02           C  
-ATOM   3084  C   THR C 408       6.265  49.346  47.528  1.00 28.13           C  
-ATOM   3085  O   THR C 408       5.523  48.626  48.196  1.00 27.91           O  
-ATOM   3086  CB  THR C 408       8.590  50.069  48.322  1.00 31.00           C  
-ATOM   3087  OG1 THR C 408       9.954  49.629  48.391  1.00 30.91           O  
-ATOM   3088  CG2 THR C 408       8.022  50.176  49.760  1.00 24.87           C  
-ATOM   3089  N   CYS C 409       5.819  50.379  46.822  1.00 27.99           N  
-ATOM   3090  CA  CYS C 409       4.405  50.743  46.797  1.00 28.82           C  
-ATOM   3091  C   CYS C 409       3.538  49.670  46.138  1.00 28.66           C  
-ATOM   3092  O   CYS C 409       2.414  49.421  46.578  1.00 29.81           O  
-ATOM   3093  CB  CYS C 409       4.233  52.058  46.056  1.00 27.88           C  
-ATOM   3094  SG  CYS C 409       5.253  53.367  46.707  1.00 27.59           S  
-ATOM   3095  N   VAL C 410       4.051  49.040  45.080  1.00 28.08           N  
-ATOM   3096  CA  VAL C 410       3.305  47.978  44.400  1.00 25.55           C  
-ATOM   3097  C   VAL C 410       3.035  46.820  45.365  1.00 27.51           C  
-ATOM   3098  O   VAL C 410       1.943  46.239  45.362  1.00 26.51           O  
-ATOM   3099  CB  VAL C 410       4.075  47.457  43.149  1.00 26.83           C  
-ATOM   3100  CG1 VAL C 410       3.305  46.326  42.471  1.00 27.85           C  
-ATOM   3101  CG2 VAL C 410       4.284  48.590  42.174  1.00 21.37           C  
-ATOM   3102  N   ASP C 411       4.031  46.477  46.186  1.00 26.62           N  
-ATOM   3103  CA  ASP C 411       3.878  45.406  47.177  1.00 25.84           C  
-ATOM   3104  C   ASP C 411       2.706  45.705  48.145  1.00 26.52           C  
-ATOM   3105  O   ASP C 411       1.932  44.809  48.504  1.00 24.40           O  
-ATOM   3106  CB  ASP C 411       5.157  45.250  48.014  1.00 29.88           C  
-ATOM   3107  CG  ASP C 411       6.260  44.475  47.293  1.00 31.53           C  
-ATOM   3108  OD1 ASP C 411       6.396  44.590  46.058  1.00 31.02           O  
-ATOM   3109  OD2 ASP C 411       7.009  43.751  47.973  1.00 34.67           O  
-ATOM   3110  N   ARG C 412       2.603  46.960  48.578  1.00 25.04           N  
-ATOM   3111  CA  ARG C 412       1.542  47.377  49.499  1.00 26.51           C  
-ATOM   3112  C   ARG C 412       0.160  47.378  48.829  1.00 25.82           C  
-ATOM   3113  O   ARG C 412      -0.847  47.047  49.450  1.00 25.32           O  
-ATOM   3114  CB  ARG C 412       1.878  48.756  50.066  1.00 27.74           C  
-ATOM   3115  CG  ARG C 412       3.182  48.749  50.890  1.00 29.75           C  
-ATOM   3116  CD  ARG C 412       3.479  50.108  51.480  1.00 33.44           C  
-ATOM   3117  NE  ARG C 412       4.828  50.185  52.028  1.00 28.98           N  
-ATOM   3118  CZ  ARG C 412       5.494  51.321  52.178  1.00 27.95           C  
-ATOM   3119  NH1 ARG C 412       4.932  52.475  51.819  1.00 23.35           N  
-ATOM   3120  NH2 ARG C 412       6.724  51.302  52.674  1.00 24.26           N  
-ATOM   3121  N   PHE C 413       0.151  47.741  47.555  1.00 25.10           N  
-ATOM   3122  CA  PHE C 413      -1.040  47.783  46.720  1.00 25.92           C  
-ATOM   3123  C   PHE C 413      -1.536  46.341  46.615  1.00 26.10           C  
-ATOM   3124  O   PHE C 413      -2.689  46.044  46.940  1.00 27.72           O  
-ATOM   3125  CB  PHE C 413      -0.629  48.360  45.353  1.00 24.99           C  
-ATOM   3126  CG  PHE C 413      -1.744  48.470  44.343  1.00 29.86           C  
-ATOM   3127  CD1 PHE C 413      -3.086  48.305  44.711  1.00 30.61           C  
-ATOM   3128  CD2 PHE C 413      -1.442  48.755  43.009  1.00 27.86           C  
-ATOM   3129  CE1 PHE C 413      -4.109  48.418  43.769  1.00 24.93           C  
-ATOM   3130  CE2 PHE C 413      -2.459  48.874  42.042  1.00 31.08           C  
-ATOM   3131  CZ  PHE C 413      -3.794  48.706  42.421  1.00 30.42           C  
-ATOM   3132  N   ILE C 414      -0.648  45.446  46.188  1.00 26.61           N  
-ATOM   3133  CA  ILE C 414      -0.958  44.021  46.053  1.00 25.85           C  
-ATOM   3134  C   ILE C 414      -1.531  43.449  47.344  1.00 27.89           C  
-ATOM   3135  O   ILE C 414      -2.528  42.706  47.326  1.00 29.54           O  
-ATOM   3136  CB  ILE C 414       0.320  43.186  45.720  1.00 27.80           C  
-ATOM   3137  CG1 ILE C 414       0.792  43.481  44.299  1.00 27.15           C  
-ATOM   3138  CG2 ILE C 414       0.045  41.682  45.894  1.00 22.41           C  
-ATOM   3139  CD1 ILE C 414       2.193  42.900  43.983  1.00 30.34           C  
-ATOM   3140  N   ASN C 415      -0.876  43.760  48.463  1.00 26.05           N  
-ATOM   3141  CA  ASN C 415      -1.317  43.254  49.754  1.00 27.40           C  
-ATOM   3142  C   ASN C 415      -2.642  43.862  50.209  1.00 25.68           C  
-ATOM   3143  O   ASN C 415      -3.426  43.203  50.876  1.00 27.70           O  
-ATOM   3144  CB  ASN C 415      -0.246  43.484  50.832  1.00 27.38           C  
-ATOM   3145  CG  ASN C 415       0.898  42.481  50.755  1.00 34.16           C  
-ATOM   3146  OD1 ASN C 415       0.680  41.275  50.672  1.00 40.74           O  
-ATOM   3147  ND2 ASN C 415       2.123  42.981  50.802  1.00 38.36           N  
-ATOM   3148  N   TRP C 416      -2.882  45.122  49.868  1.00 29.12           N  
-ATOM   3149  CA  TRP C 416      -4.137  45.768  50.248  1.00 29.09           C  
-ATOM   3150  C   TRP C 416      -5.289  45.210  49.406  1.00 27.90           C  
-ATOM   3151  O   TRP C 416      -6.270  44.692  49.931  1.00 26.49           O  
-ATOM   3152  CB  TRP C 416      -4.088  47.282  50.029  1.00 25.33           C  
-ATOM   3153  CG  TRP C 416      -5.496  47.869  50.003  1.00 30.71           C  
-ATOM   3154  CD1 TRP C 416      -6.368  47.961  51.057  1.00 25.02           C  
-ATOM   3155  CD2 TRP C 416      -6.233  48.284  48.841  1.00 27.75           C  
-ATOM   3156  NE1 TRP C 416      -7.604  48.391  50.620  1.00 26.19           N  
-ATOM   3157  CE2 TRP C 416      -7.548  48.595  49.265  1.00 31.22           C  
-ATOM   3158  CE3 TRP C 416      -5.912  48.415  47.485  1.00 25.24           C  
-ATOM   3159  CZ2 TRP C 416      -8.543  49.030  48.373  1.00 29.81           C  
-ATOM   3160  CZ3 TRP C 416      -6.896  48.846  46.599  1.00 28.50           C  
-ATOM   3161  CH2 TRP C 416      -8.199  49.147  47.049  1.00 32.64           C  
-ATOM   3162  N   PHE C 417      -5.146  45.334  48.093  1.00 27.11           N  
-ATOM   3163  CA  PHE C 417      -6.164  44.887  47.161  1.00 29.17           C  
-ATOM   3164  C   PHE C 417      -6.616  43.455  47.447  1.00 30.31           C  
-ATOM   3165  O   PHE C 417      -7.820  43.213  47.603  1.00 32.15           O  
-ATOM   3166  CB  PHE C 417      -5.648  45.037  45.723  1.00 28.76           C  
-ATOM   3167  CG  PHE C 417      -6.692  44.792  44.666  1.00 28.11           C  
-ATOM   3168  CD1 PHE C 417      -7.906  45.482  44.686  1.00 35.77           C  
-ATOM   3169  CD2 PHE C 417      -6.473  43.855  43.663  1.00 29.84           C  
-ATOM   3170  CE1 PHE C 417      -8.894  45.235  43.717  1.00 34.52           C  
-ATOM   3171  CE2 PHE C 417      -7.448  43.600  42.689  1.00 31.46           C  
-ATOM   3172  CZ  PHE C 417      -8.661  44.288  42.717  1.00 34.48           C  
-ATOM   3173  N   SER C 418      -5.676  42.514  47.552  1.00 27.44           N  
-ATOM   3174  CA  SER C 418      -6.035  41.126  47.820  1.00 27.90           C  
-ATOM   3175  C   SER C 418      -6.765  40.976  49.153  1.00 29.68           C  
-ATOM   3176  O   SER C 418      -7.765  40.258  49.245  1.00 27.85           O  
-ATOM   3177  CB  SER C 418      -4.793  40.214  47.811  1.00 28.68           C  
-ATOM   3178  OG  SER C 418      -3.854  40.598  48.804  1.00 30.94           O  
-ATOM   3179  N   HIS C 419      -6.257  41.639  50.186  1.00 27.28           N  
-ATOM   3180  CA  HIS C 419      -6.889  41.554  51.492  1.00 28.52           C  
-ATOM   3181  C   HIS C 419      -8.300  42.144  51.399  1.00 29.41           C  
-ATOM   3182  O   HIS C 419      -9.266  41.582  51.918  1.00 30.41           O  
-ATOM   3183  CB  HIS C 419      -6.066  42.313  52.533  1.00 27.07           C  
-ATOM   3184  CG  HIS C 419      -6.513  42.068  53.938  1.00 29.42           C  
-ATOM   3185  ND1 HIS C 419      -5.999  42.757  55.016  1.00 28.43           N  
-ATOM   3186  CD2 HIS C 419      -7.427  41.207  54.442  1.00 27.26           C  
-ATOM   3187  CE1 HIS C 419      -6.579  42.331  56.124  1.00 25.48           C  
-ATOM   3188  NE2 HIS C 419      -7.450  41.391  55.805  1.00 26.91           N  
-ATOM   3189  N   HIS C 420      -8.404  43.279  50.723  1.00 30.31           N  
-ATOM   3190  CA  HIS C 420      -9.681  43.950  50.517  1.00 31.96           C  
-ATOM   3191  C   HIS C 420     -10.653  42.991  49.806  1.00 33.65           C  
-ATOM   3192  O   HIS C 420     -11.793  42.794  50.252  1.00 34.42           O  
-ATOM   3193  CB  HIS C 420      -9.458  45.212  49.674  1.00 30.43           C  
-ATOM   3194  CG  HIS C 420     -10.717  45.935  49.314  1.00 34.47           C  
-ATOM   3195  ND1 HIS C 420     -11.443  46.669  50.226  1.00 32.63           N  
-ATOM   3196  CD2 HIS C 420     -11.403  45.998  48.148  1.00 33.15           C  
-ATOM   3197  CE1 HIS C 420     -12.524  47.150  49.639  1.00 33.31           C  
-ATOM   3198  NE2 HIS C 420     -12.524  46.756  48.379  1.00 34.17           N  
-ATOM   3199  N   LEU C 421     -10.198  42.387  48.711  1.00 33.32           N  
-ATOM   3200  CA  LEU C 421     -11.027  41.449  47.953  1.00 33.19           C  
-ATOM   3201  C   LEU C 421     -11.558  40.303  48.785  1.00 32.34           C  
-ATOM   3202  O   LEU C 421     -12.696  39.869  48.596  1.00 33.06           O  
-ATOM   3203  CB  LEU C 421     -10.252  40.865  46.777  1.00 34.18           C  
-ATOM   3204  CG  LEU C 421     -10.086  41.790  45.584  1.00 29.03           C  
-ATOM   3205  CD1 LEU C 421      -9.252  41.098  44.534  1.00 35.11           C  
-ATOM   3206  CD2 LEU C 421     -11.451  42.162  45.040  1.00 33.81           C  
-ATOM   3207  N   SER C 422     -10.737  39.814  49.707  1.00 32.58           N  
-ATOM   3208  CA  SER C 422     -11.134  38.705  50.568  1.00 30.33           C  
-ATOM   3209  C   SER C 422     -12.238  39.091  51.564  1.00 31.49           C  
-ATOM   3210  O   SER C 422     -12.841  38.227  52.201  1.00 31.38           O  
-ATOM   3211  CB  SER C 422      -9.923  38.176  51.342  1.00 33.86           C  
-ATOM   3212  OG  SER C 422      -9.582  39.038  52.415  1.00 32.98           O  
-ATOM   3213  N   ASN C 423     -12.492  40.385  51.713  1.00 31.60           N  
-ATOM   3214  CA  ASN C 423     -13.532  40.847  52.631  1.00 31.42           C  
-ATOM   3215  C   ASN C 423     -14.834  41.135  51.894  1.00 32.17           C  
-ATOM   3216  O   ASN C 423     -15.846  41.474  52.510  1.00 32.35           O  
-ATOM   3217  CB  ASN C 423     -13.057  42.094  53.375  1.00 28.33           C  
-ATOM   3218  CG  ASN C 423     -12.296  41.751  54.632  1.00 32.37           C  
-ATOM   3219  OD1 ASN C 423     -12.882  41.632  55.709  1.00 33.85           O  
-ATOM   3220  ND2 ASN C 423     -10.985  41.551  54.501  1.00 29.48           N  
-ATOM   3221  N   PHE C 424     -14.793  40.982  50.574  1.00 33.02           N  
-ATOM   3222  CA  PHE C 424     -15.948  41.206  49.720  1.00 33.69           C  
-ATOM   3223  C   PHE C 424     -16.132  40.106  48.676  1.00 34.48           C  
-ATOM   3224  O   PHE C 424     -16.308  40.376  47.485  1.00 34.55           O  
-ATOM   3225  CB  PHE C 424     -15.829  42.567  49.050  1.00 36.42           C  
-ATOM   3226  CG  PHE C 424     -15.910  43.709  50.018  1.00 40.06           C  
-ATOM   3227  CD1 PHE C 424     -17.144  44.113  50.529  1.00 37.43           C  
-ATOM   3228  CD2 PHE C 424     -14.759  44.354  50.452  1.00 35.05           C  
-ATOM   3229  CE1 PHE C 424     -17.227  45.143  51.459  1.00 37.71           C  
-ATOM   3230  CE2 PHE C 424     -14.828  45.393  51.388  1.00 38.78           C  
-ATOM   3231  CZ  PHE C 424     -16.066  45.787  51.892  1.00 40.18           C  
-ATOM   3232  N   GLN C 425     -16.082  38.863  49.140  1.00 33.61           N  
-ATOM   3233  CA  GLN C 425     -16.292  37.706  48.286  1.00 37.06           C  
-ATOM   3234  C   GLN C 425     -15.408  37.617  47.042  1.00 38.90           C  
-ATOM   3235  O   GLN C 425     -15.786  36.980  46.059  1.00 40.07           O  
-ATOM   3236  CB  GLN C 425     -17.770  37.650  47.865  1.00 39.05           C  
-ATOM   3237  CG  GLN C 425     -18.772  37.639  49.023  1.00 30.00           C  
-ATOM   3238  CD  GLN C 425     -18.926  38.993  49.713  1.00 29.42           C  
-ATOM   3239  OE1 GLN C 425     -19.130  40.019  49.064  1.00 31.48           O  
-ATOM   3240  NE2 GLN C 425     -18.841  38.991  51.038  1.00 28.86           N  
-ATOM   3241  N   PHE C 426     -14.235  38.242  47.086  1.00 39.72           N  
-ATOM   3242  CA  PHE C 426     -13.299  38.211  45.960  1.00 38.96           C  
-ATOM   3243  C   PHE C 426     -13.943  38.670  44.670  1.00 38.16           C  
-ATOM   3244  O   PHE C 426     -13.501  38.298  43.583  1.00 39.49           O  
-ATOM   3245  CB  PHE C 426     -12.735  36.793  45.769  1.00 37.55           C  
-ATOM   3246  CG  PHE C 426     -11.837  36.344  46.883  1.00 38.20           C  
-ATOM   3247  CD1 PHE C 426     -10.557  36.884  47.019  1.00 35.96           C  
-ATOM   3248  CD2 PHE C 426     -12.271  35.393  47.809  1.00 36.84           C  
-ATOM   3249  CE1 PHE C 426      -9.720  36.486  48.057  1.00 31.03           C  
-ATOM   3250  CE2 PHE C 426     -11.438  34.986  48.858  1.00 38.15           C  
-ATOM   3251  CZ  PHE C 426     -10.157  35.538  48.979  1.00 34.96           C  
-ATOM   3252  N   ARG C 427     -14.982  39.486  44.792  1.00 39.14           N  
-ATOM   3253  CA  ARG C 427     -15.683  40.012  43.625  1.00 37.91           C  
-ATOM   3254  C   ARG C 427     -14.908  41.143  42.947  1.00 37.61           C  
-ATOM   3255  O   ARG C 427     -14.526  42.127  43.585  1.00 37.15           O  
-ATOM   3256  CB  ARG C 427     -17.087  40.514  44.024  1.00 41.59           C  
-ATOM   3257  CG  ARG C 427     -18.083  39.398  44.328  1.00 49.71           C  
-ATOM   3258  CD  ARG C 427     -19.500  39.908  44.657  1.00 57.29           C  
-ATOM   3259  NE  ARG C 427     -19.595  40.534  45.976  1.00 60.68           N  
-ATOM   3260  CZ  ARG C 427     -19.361  41.821  46.220  1.00 63.16           C  
-ATOM   3261  NH1 ARG C 427     -19.020  42.641  45.234  1.00 64.50           N  
-ATOM   3262  NH2 ARG C 427     -19.459  42.286  47.459  1.00 64.59           N  
-ATOM   3263  N   TRP C 428     -14.695  41.007  41.642  1.00 36.36           N  
-ATOM   3264  CA  TRP C 428     -13.979  42.016  40.880  1.00 36.34           C  
-ATOM   3265  C   TRP C 428     -14.162  41.755  39.386  1.00 36.61           C  
-ATOM   3266  O   TRP C 428     -14.282  40.611  38.955  1.00 37.00           O  
-ATOM   3267  CB  TRP C 428     -12.488  41.998  41.256  1.00 36.11           C  
-ATOM   3268  CG  TRP C 428     -11.720  43.122  40.649  1.00 34.65           C  
-ATOM   3269  CD1 TRP C 428     -10.846  43.046  39.604  1.00 36.30           C  
-ATOM   3270  CD2 TRP C 428     -11.840  44.514  40.972  1.00 33.24           C  
-ATOM   3271  NE1 TRP C 428     -10.424  44.303  39.245  1.00 36.27           N  
-ATOM   3272  CE2 TRP C 428     -11.021  45.224  40.069  1.00 34.69           C  
-ATOM   3273  CE3 TRP C 428     -12.568  45.230  41.932  1.00 34.62           C  
-ATOM   3274  CZ2 TRP C 428     -10.906  46.620  40.096  1.00 31.56           C  
-ATOM   3275  CZ3 TRP C 428     -12.453  46.621  41.959  1.00 36.78           C  
-ATOM   3276  CH2 TRP C 428     -11.627  47.300  41.042  1.00 33.93           C  
-ATOM   3277  N   SER C 429     -14.188  42.826  38.606  1.00 37.80           N  
-ATOM   3278  CA  SER C 429     -14.366  42.732  37.161  1.00 41.37           C  
-ATOM   3279  C   SER C 429     -13.022  42.569  36.460  1.00 40.45           C  
-ATOM   3280  O   SER C 429     -12.555  43.481  35.789  1.00 41.97           O  
-ATOM   3281  CB  SER C 429     -15.054  43.998  36.647  1.00 43.72           C  
-ATOM   3282  OG  SER C 429     -14.291  45.149  36.974  1.00 53.46           O  
-ATOM   3283  N   TRP C 430     -12.414  41.399  36.607  1.00 43.09           N  
-ATOM   3284  CA  TRP C 430     -11.113  41.132  36.007  1.00 44.19           C  
-ATOM   3285  C   TRP C 430     -11.009  41.441  34.520  1.00 46.37           C  
-ATOM   3286  O   TRP C 430      -9.952  41.858  34.053  1.00 46.08           O  
-ATOM   3287  CB  TRP C 430     -10.712  39.685  36.266  1.00 43.57           C  
-ATOM   3288  CG  TRP C 430     -10.660  39.359  37.727  1.00 46.44           C  
-ATOM   3289  CD1 TRP C 430     -11.622  38.732  38.466  1.00 44.69           C  
-ATOM   3290  CD2 TRP C 430      -9.602  39.685  38.639  1.00 45.66           C  
-ATOM   3291  NE1 TRP C 430     -11.230  38.647  39.782  1.00 45.05           N  
-ATOM   3292  CE2 TRP C 430      -9.994  39.225  39.916  1.00 44.93           C  
-ATOM   3293  CE3 TRP C 430      -8.363  40.326  38.501  1.00 47.45           C  
-ATOM   3294  CZ2 TRP C 430      -9.189  39.382  41.049  1.00 44.86           C  
-ATOM   3295  CZ3 TRP C 430      -7.560  40.483  39.633  1.00 46.87           C  
-ATOM   3296  CH2 TRP C 430      -7.979  40.012  40.887  1.00 44.14           C  
-ATOM   3297  N   GLU C 431     -12.095  41.248  33.773  1.00 48.79           N  
-ATOM   3298  CA  GLU C 431     -12.069  41.525  32.338  1.00 49.96           C  
-ATOM   3299  C   GLU C 431     -11.693  42.970  32.034  1.00 49.98           C  
-ATOM   3300  O   GLU C 431     -11.258  43.283  30.927  1.00 49.47           O  
-ATOM   3301  CB  GLU C 431     -13.414  41.183  31.681  1.00 54.08           C  
-ATOM   3302  CG  GLU C 431     -14.656  41.591  32.465  1.00 63.71           C  
-ATOM   3303  CD  GLU C 431     -14.953  40.659  33.627  1.00 67.29           C  
-ATOM   3304  OE1 GLU C 431     -14.907  39.425  33.421  1.00 71.61           O  
-ATOM   3305  OE2 GLU C 431     -15.241  41.162  34.736  1.00 68.58           O  
-ATOM   3306  N   ASP C 432     -11.857  43.859  33.008  1.00 49.72           N  
-ATOM   3307  CA  ASP C 432     -11.484  45.251  32.796  1.00 49.71           C  
-ATOM   3308  C   ASP C 432      -9.956  45.365  32.736  1.00 49.09           C  
-ATOM   3309  O   ASP C 432      -9.416  46.392  32.319  1.00 46.21           O  
-ATOM   3310  CB  ASP C 432     -12.034  46.139  33.918  1.00 55.23           C  
-ATOM   3311  CG  ASP C 432     -13.474  46.569  33.671  1.00 61.05           C  
-ATOM   3312  OD1 ASP C 432     -14.346  45.686  33.534  1.00 63.20           O  
-ATOM   3313  OD2 ASP C 432     -13.734  47.792  33.610  1.00 66.37           O  
-ATOM   3314  N   TRP C 433      -9.269  44.301  33.147  1.00 48.89           N  
-ATOM   3315  CA  TRP C 433      -7.809  44.278  33.139  1.00 50.36           C  
-ATOM   3316  C   TRP C 433      -7.236  43.218  32.189  1.00 51.57           C  
-ATOM   3317  O   TRP C 433      -6.148  42.688  32.424  1.00 50.72           O  
-ATOM   3318  CB  TRP C 433      -7.270  44.040  34.559  1.00 45.85           C  
-ATOM   3319  CG  TRP C 433      -7.607  45.133  35.542  1.00 41.95           C  
-ATOM   3320  CD1 TRP C 433      -8.122  46.360  35.257  1.00 40.07           C  
-ATOM   3321  CD2 TRP C 433      -7.420  45.099  36.962  1.00 37.31           C  
-ATOM   3322  NE1 TRP C 433      -8.270  47.096  36.407  1.00 40.31           N  
-ATOM   3323  CE2 TRP C 433      -7.847  46.345  37.469  1.00 37.18           C  
-ATOM   3324  CE3 TRP C 433      -6.935  44.136  37.855  1.00 36.38           C  
-ATOM   3325  CZ2 TRP C 433      -7.802  46.656  38.832  1.00 33.07           C  
-ATOM   3326  CZ3 TRP C 433      -6.892  44.446  39.211  1.00 36.74           C  
-ATOM   3327  CH2 TRP C 433      -7.325  45.697  39.683  1.00 33.07           C  
-ATOM   3328  N   SER C 434      -7.971  42.910  31.122  1.00 53.37           N  
-ATOM   3329  CA  SER C 434      -7.524  41.924  30.138  1.00 54.33           C  
-ATOM   3330  C   SER C 434      -6.285  42.411  29.372  1.00 54.41           C  
-ATOM   3331  O   SER C 434      -5.510  41.610  28.848  1.00 54.83           O  
-ATOM   3332  CB  SER C 434      -8.657  41.615  29.149  1.00 56.34           C  
-ATOM   3333  OG  SER C 434      -9.623  40.748  29.723  1.00 59.96           O  
-ATOM   3334  N   ASP C 435      -6.106  43.730  29.329  1.00 54.55           N  
-ATOM   3335  CA  ASP C 435      -4.981  44.360  28.641  1.00 55.18           C  
-ATOM   3336  C   ASP C 435      -3.621  43.822  29.100  1.00 56.28           C  
-ATOM   3337  O   ASP C 435      -2.602  44.038  28.437  1.00 57.00           O  
-ATOM   3338  CB  ASP C 435      -5.042  45.885  28.841  1.00 53.51           C  
-ATOM   3339  CG  ASP C 435      -4.642  46.326  30.261  1.00 51.41           C  
-ATOM   3340  OD1 ASP C 435      -4.946  45.614  31.240  1.00 40.23           O  
-ATOM   3341  OD2 ASP C 435      -4.030  47.407  30.401  1.00 47.76           O  
-ATOM   3342  N   CYS C 436      -3.618  43.110  30.224  1.00 55.85           N  
-ATOM   3343  CA  CYS C 436      -2.400  42.541  30.795  1.00 55.67           C  
-ATOM   3344  C   CYS C 436      -2.059  41.174  30.201  1.00 56.30           C  
-ATOM   3345  O   CYS C 436      -0.902  40.748  30.223  1.00 55.82           O  
-ATOM   3346  CB  CYS C 436      -2.555  42.387  32.311  1.00 51.61           C  
-ATOM   3347  SG  CYS C 436      -3.465  40.901  32.827  1.00 47.48           S  
-ATOM   3348  N   LEU C 437      -3.076  40.484  29.695  1.00 56.88           N  
-ATOM   3349  CA  LEU C 437      -2.894  39.160  29.112  1.00 57.21           C  
-ATOM   3350  C   LEU C 437      -2.011  39.202  27.867  1.00 56.83           C  
-ATOM   3351  O   LEU C 437      -1.279  38.256  27.583  1.00 57.89           O  
-ATOM   3352  CB  LEU C 437      -4.254  38.552  28.757  1.00 57.70           C  
-ATOM   3353  CG  LEU C 437      -5.280  38.427  29.888  1.00 59.02           C  
-ATOM   3354  CD1 LEU C 437      -6.570  37.844  29.338  1.00 59.21           C  
-ATOM   3355  CD2 LEU C 437      -4.730  37.549  30.994  1.00 56.20           C  
-ATOM   3356  N   SER C 438      -2.073  40.307  27.133  1.00 57.23           N  
-ATOM   3357  CA  SER C 438      -1.284  40.451  25.917  1.00 58.69           C  
-ATOM   3358  C   SER C 438       0.061  41.141  26.144  1.00 58.78           C  
-ATOM   3359  O   SER C 438       0.711  41.564  25.188  1.00 59.09           O  
-ATOM   3360  CB  SER C 438      -2.074  41.231  24.865  1.00 58.61           C  
-ATOM   3361  OG  SER C 438      -2.169  42.601  25.217  1.00 61.18           O  
-ATOM   3362  N   GLN C 439       0.480  41.261  27.401  1.00 58.04           N  
-ATOM   3363  CA  GLN C 439       1.755  41.906  27.689  1.00 56.61           C  
-ATOM   3364  C   GLN C 439       2.797  40.896  28.140  1.00 56.01           C  
-ATOM   3365  O   GLN C 439       2.494  39.726  28.381  1.00 55.16           O  
-ATOM   3366  CB  GLN C 439       1.604  42.968  28.782  1.00 55.93           C  
-ATOM   3367  CG  GLN C 439       0.729  44.164  28.434  1.00 57.30           C  
-ATOM   3368  CD  GLN C 439       0.784  45.241  29.511  1.00 57.60           C  
-ATOM   3369  OE1 GLN C 439       0.807  44.935  30.702  1.00 57.47           O  
-ATOM   3370  NE2 GLN C 439       0.801  46.504  29.095  1.00 56.09           N  
-ATOM   3371  N   ASP C 440       4.032  41.367  28.249  1.00 55.60           N  
-ATOM   3372  CA  ASP C 440       5.132  40.538  28.709  1.00 54.34           C  
-ATOM   3373  C   ASP C 440       4.770  40.147  30.138  1.00 53.35           C  
-ATOM   3374  O   ASP C 440       4.444  41.009  30.951  1.00 53.50           O  
-ATOM   3375  CB  ASP C 440       6.426  41.354  28.703  1.00 55.61           C  
-ATOM   3376  CG  ASP C 440       7.640  40.533  29.098  1.00 59.09           C  
-ATOM   3377  OD1 ASP C 440       7.571  39.798  30.104  1.00 57.57           O  
-ATOM   3378  OD2 ASP C 440       8.675  40.634  28.406  1.00 66.57           O  
-ATOM   3379  N   PRO C 441       4.819  38.845  30.461  1.00 52.56           N  
-ATOM   3380  CA  PRO C 441       4.491  38.340  31.801  1.00 51.55           C  
-ATOM   3381  C   PRO C 441       5.266  39.007  32.944  1.00 51.56           C  
-ATOM   3382  O   PRO C 441       4.848  38.936  34.106  1.00 51.59           O  
-ATOM   3383  CB  PRO C 441       4.804  36.846  31.694  1.00 52.28           C  
-ATOM   3384  CG  PRO C 441       4.543  36.548  30.258  1.00 52.58           C  
-ATOM   3385  CD  PRO C 441       5.154  37.735  29.552  1.00 51.98           C  
-ATOM   3386  N   GLU C 442       6.386  39.647  32.608  1.00 50.45           N  
-ATOM   3387  CA  GLU C 442       7.242  40.318  33.587  1.00 48.66           C  
-ATOM   3388  C   GLU C 442       6.823  41.770  33.770  1.00 46.50           C  
-ATOM   3389  O   GLU C 442       7.231  42.426  34.727  1.00 46.35           O  
-ATOM   3390  CB  GLU C 442       8.704  40.296  33.127  1.00 52.45           C  
-ATOM   3391  CG  GLU C 442       9.233  38.943  32.674  1.00 62.14           C  
-ATOM   3392  CD  GLU C 442      10.652  39.030  32.115  1.00 68.46           C  
-ATOM   3393  OE1 GLU C 442      10.891  39.868  31.215  1.00 66.35           O  
-ATOM   3394  OE2 GLU C 442      11.524  38.257  32.575  1.00 71.77           O  
-ATOM   3395  N   SER C 443       6.028  42.271  32.831  1.00 45.23           N  
-ATOM   3396  CA  SER C 443       5.543  43.648  32.868  1.00 44.41           C  
-ATOM   3397  C   SER C 443       4.733  43.856  34.160  1.00 41.56           C  
-ATOM   3398  O   SER C 443       4.139  42.919  34.684  1.00 41.42           O  
-ATOM   3399  CB  SER C 443       4.684  43.913  31.631  1.00 44.96           C  
-ATOM   3400  OG  SER C 443       4.638  45.292  31.327  1.00 52.50           O  
-ATOM   3401  N   PRO C 444       4.701  45.090  34.684  1.00 41.23           N  
-ATOM   3402  CA  PRO C 444       3.980  45.440  35.920  1.00 40.18           C  
-ATOM   3403  C   PRO C 444       2.540  44.937  36.082  1.00 40.04           C  
-ATOM   3404  O   PRO C 444       2.229  44.234  37.050  1.00 40.68           O  
-ATOM   3405  CB  PRO C 444       4.055  46.965  35.944  1.00 38.12           C  
-ATOM   3406  CG  PRO C 444       5.355  47.250  35.219  1.00 42.99           C  
-ATOM   3407  CD  PRO C 444       5.271  46.295  34.053  1.00 39.30           C  
-ATOM   3408  N   LYS C 445       1.664  45.296  35.149  1.00 38.96           N  
-ATOM   3409  CA  LYS C 445       0.258  44.892  35.233  1.00 39.61           C  
-ATOM   3410  C   LYS C 445       0.017  43.388  35.332  1.00 39.97           C  
-ATOM   3411  O   LYS C 445      -0.627  42.917  36.276  1.00 40.81           O  
-ATOM   3412  CB  LYS C 445      -0.530  45.479  34.060  1.00 37.72           C  
-ATOM   3413  CG  LYS C 445      -0.576  46.990  34.089  1.00 28.46           C  
-ATOM   3414  CD  LYS C 445      -1.470  47.554  33.005  1.00 37.18           C  
-ATOM   3415  CE  LYS C 445      -1.347  49.067  32.957  1.00 36.94           C  
-ATOM   3416  NZ  LYS C 445      -2.050  49.666  31.792  1.00 38.11           N  
-ATOM   3417  N   PRO C 446       0.530  42.602  34.370  1.00 41.66           N  
-ATOM   3418  CA  PRO C 446       0.290  41.162  34.484  1.00 40.98           C  
-ATOM   3419  C   PRO C 446       0.923  40.574  35.738  1.00 40.61           C  
-ATOM   3420  O   PRO C 446       0.363  39.681  36.372  1.00 42.24           O  
-ATOM   3421  CB  PRO C 446       0.890  40.606  33.187  1.00 40.51           C  
-ATOM   3422  CG  PRO C 446       1.915  41.630  32.808  1.00 40.60           C  
-ATOM   3423  CD  PRO C 446       1.217  42.921  33.106  1.00 40.73           C  
-ATOM   3424  N   LYS C 447       2.097  41.074  36.098  1.00 40.24           N  
-ATOM   3425  CA  LYS C 447       2.772  40.586  37.293  1.00 38.31           C  
-ATOM   3426  C   LYS C 447       1.932  40.908  38.536  1.00 34.59           C  
-ATOM   3427  O   LYS C 447       1.807  40.090  39.446  1.00 34.66           O  
-ATOM   3428  CB  LYS C 447       4.155  41.234  37.409  1.00 38.37           C  
-ATOM   3429  CG  LYS C 447       4.929  40.832  38.654  1.00 35.09           C  
-ATOM   3430  CD  LYS C 447       6.331  41.429  38.638  1.00 42.32           C  
-ATOM   3431  CE  LYS C 447       6.974  41.333  40.013  1.00 41.65           C  
-ATOM   3432  NZ  LYS C 447       6.874  39.969  40.589  1.00 45.53           N  
-ATOM   3433  N   PHE C 448       1.378  42.114  38.561  1.00 34.87           N  
-ATOM   3434  CA  PHE C 448       0.534  42.573  39.663  1.00 35.10           C  
-ATOM   3435  C   PHE C 448      -0.645  41.614  39.837  1.00 35.10           C  
-ATOM   3436  O   PHE C 448      -0.888  41.097  40.932  1.00 36.25           O  
-ATOM   3437  CB  PHE C 448       0.034  43.992  39.364  1.00 33.76           C  
-ATOM   3438  CG  PHE C 448      -1.072  44.451  40.272  1.00 38.12           C  
-ATOM   3439  CD1 PHE C 448      -0.823  44.732  41.614  1.00 36.99           C  
-ATOM   3440  CD2 PHE C 448      -2.373  44.583  39.790  1.00 35.92           C  
-ATOM   3441  CE1 PHE C 448      -1.859  45.135  42.466  1.00 35.98           C  
-ATOM   3442  CE2 PHE C 448      -3.410  44.984  40.630  1.00 37.85           C  
-ATOM   3443  CZ  PHE C 448      -3.150  45.260  41.974  1.00 37.67           C  
-ATOM   3444  N   VAL C 449      -1.363  41.359  38.746  1.00 35.97           N  
-ATOM   3445  CA  VAL C 449      -2.504  40.448  38.783  1.00 34.50           C  
-ATOM   3446  C   VAL C 449      -2.073  39.092  39.325  1.00 35.25           C  
-ATOM   3447  O   VAL C 449      -2.733  38.534  40.200  1.00 36.48           O  
-ATOM   3448  CB  VAL C 449      -3.133  40.279  37.369  1.00 35.23           C  
-ATOM   3449  CG1 VAL C 449      -4.261  39.260  37.402  1.00 33.17           C  
-ATOM   3450  CG2 VAL C 449      -3.661  41.626  36.876  1.00 30.13           C  
-ATOM   3451  N   ARG C 450      -0.952  38.566  38.836  1.00 36.52           N  
-ATOM   3452  CA  ARG C 450      -0.487  37.265  39.317  1.00 36.82           C  
-ATOM   3453  C   ARG C 450      -0.180  37.263  40.808  1.00 35.22           C  
-ATOM   3454  O   ARG C 450      -0.465  36.285  41.507  1.00 35.75           O  
-ATOM   3455  CB  ARG C 450       0.770  36.801  38.565  1.00 42.43           C  
-ATOM   3456  CG  ARG C 450       0.529  36.263  37.163  1.00 47.35           C  
-ATOM   3457  CD  ARG C 450       1.612  35.246  36.791  1.00 52.70           C  
-ATOM   3458  NE  ARG C 450       2.957  35.769  37.028  1.00 52.86           N  
-ATOM   3459  CZ  ARG C 450       3.518  36.744  36.319  1.00 48.84           C  
-ATOM   3460  NH1 ARG C 450       2.855  37.309  35.319  1.00 47.15           N  
-ATOM   3461  NH2 ARG C 450       4.744  37.157  36.609  1.00 46.22           N  
-ATOM   3462  N   GLU C 451       0.429  38.334  41.302  1.00 34.13           N  
-ATOM   3463  CA  GLU C 451       0.754  38.385  42.726  1.00 33.06           C  
-ATOM   3464  C   GLU C 451      -0.538  38.493  43.550  1.00 29.27           C  
-ATOM   3465  O   GLU C 451      -0.679  37.847  44.590  1.00 31.67           O  
-ATOM   3466  CB  GLU C 451       1.692  39.567  43.025  1.00 35.93           C  
-ATOM   3467  CG  GLU C 451       3.064  39.510  42.326  1.00 34.18           C  
-ATOM   3468  CD  GLU C 451       4.000  38.453  42.901  1.00 42.54           C  
-ATOM   3469  OE1 GLU C 451       3.715  37.920  43.997  1.00 42.80           O  
-ATOM   3470  OE2 GLU C 451       5.034  38.166  42.258  1.00 47.21           O  
-ATOM   3471  N   VAL C 452      -1.484  39.293  43.075  1.00 31.29           N  
-ATOM   3472  CA  VAL C 452      -2.771  39.461  43.768  1.00 31.43           C  
-ATOM   3473  C   VAL C 452      -3.487  38.117  43.874  1.00 32.94           C  
-ATOM   3474  O   VAL C 452      -3.913  37.708  44.958  1.00 33.51           O  
-ATOM   3475  CB  VAL C 452      -3.683  40.450  43.011  1.00 32.38           C  
-ATOM   3476  CG1 VAL C 452      -5.103  40.420  43.601  1.00 31.11           C  
-ATOM   3477  CG2 VAL C 452      -3.100  41.859  43.098  1.00 28.00           C  
-ATOM   3478  N   LEU C 453      -3.606  37.427  42.742  1.00 34.86           N  
-ATOM   3479  CA  LEU C 453      -4.261  36.122  42.705  1.00 36.61           C  
-ATOM   3480  C   LEU C 453      -3.562  35.161  43.646  1.00 35.95           C  
-ATOM   3481  O   LEU C 453      -4.202  34.358  44.327  1.00 35.68           O  
-ATOM   3482  CB  LEU C 453      -4.243  35.559  41.275  1.00 38.84           C  
-ATOM   3483  CG  LEU C 453      -5.065  36.381  40.282  1.00 36.97           C  
-ATOM   3484  CD1 LEU C 453      -5.009  35.773  38.888  1.00 41.84           C  
-ATOM   3485  CD2 LEU C 453      -6.500  36.440  40.786  1.00 42.76           C  
-ATOM   3486  N   GLU C 454      -2.237  35.250  43.682  1.00 36.63           N  
-ATOM   3487  CA  GLU C 454      -1.445  34.390  44.548  1.00 37.19           C  
-ATOM   3488  C   GLU C 454      -1.763  34.698  46.013  1.00 35.14           C  
-ATOM   3489  O   GLU C 454      -1.881  33.799  46.839  1.00 34.68           O  
-ATOM   3490  CB  GLU C 454       0.046  34.614  44.272  1.00 41.16           C  
-ATOM   3491  CG  GLU C 454       0.965  33.601  44.931  1.00 47.11           C  
-ATOM   3492  CD  GLU C 454       2.438  33.845  44.618  1.00 49.09           C  
-ATOM   3493  OE1 GLU C 454       2.790  33.973  43.423  1.00 47.35           O  
-ATOM   3494  OE2 GLU C 454       3.244  33.903  45.571  1.00 50.45           O  
-ATOM   3495  N   LYS C 455      -1.895  35.982  46.324  1.00 35.71           N  
-ATOM   3496  CA  LYS C 455      -2.213  36.424  47.679  1.00 35.52           C  
-ATOM   3497  C   LYS C 455      -3.639  36.026  48.052  1.00 35.58           C  
-ATOM   3498  O   LYS C 455      -3.920  35.685  49.196  1.00 35.19           O  
-ATOM   3499  CB  LYS C 455      -2.067  37.947  47.784  1.00 34.32           C  
-ATOM   3500  CG  LYS C 455      -0.633  38.437  47.893  1.00 40.03           C  
-ATOM   3501  CD  LYS C 455      -0.010  37.990  49.205  1.00 44.05           C  
-ATOM   3502  CE  LYS C 455       1.439  38.429  49.317  1.00 46.41           C  
-ATOM   3503  NZ  LYS C 455       2.034  37.912  50.576  1.00 53.96           N  
-ATOM   3504  N   CYS C 456      -4.545  36.084  47.085  1.00 35.92           N  
-ATOM   3505  CA  CYS C 456      -5.926  35.707  47.357  1.00 37.29           C  
-ATOM   3506  C   CYS C 456      -5.996  34.225  47.702  1.00 36.85           C  
-ATOM   3507  O   CYS C 456      -6.728  33.837  48.607  1.00 37.24           O  
-ATOM   3508  CB  CYS C 456      -6.817  36.016  46.153  1.00 34.19           C  
-ATOM   3509  SG  CYS C 456      -7.003  37.773  45.840  1.00 35.39           S  
-ATOM   3510  N   MET C 457      -5.207  33.405  47.005  1.00 38.22           N  
-ATOM   3511  CA  MET C 457      -5.203  31.962  47.257  1.00 37.27           C  
-ATOM   3512  C   MET C 457      -4.756  31.643  48.675  1.00 37.51           C  
-ATOM   3513  O   MET C 457      -5.273  30.724  49.308  1.00 37.18           O  
-ATOM   3514  CB  MET C 457      -4.290  31.233  46.257  1.00 41.00           C  
-ATOM   3515  CG  MET C 457      -4.324  29.703  46.393  1.00 46.77           C  
-ATOM   3516  SD  MET C 457      -3.270  28.777  45.225  1.00 52.87           S  
-ATOM   3517  CE  MET C 457      -1.748  28.619  46.192  1.00 47.22           C  
-ATOM   3518  N   ARG C 458      -3.784  32.395  49.178  1.00 39.31           N  
-ATOM   3519  CA  ARG C 458      -3.295  32.164  50.537  1.00 38.46           C  
-ATOM   3520  C   ARG C 458      -4.376  32.414  51.586  1.00 38.82           C  
-ATOM   3521  O   ARG C 458      -4.312  31.894  52.708  1.00 35.79           O  
-ATOM   3522  CB  ARG C 458      -2.115  33.070  50.846  1.00 38.74           C  
-ATOM   3523  CG  ARG C 458      -0.811  32.722  50.156  1.00 47.19           C  
-ATOM   3524  CD  ARG C 458       0.299  33.285  51.012  1.00 51.02           C  
-ATOM   3525  NE  ARG C 458       1.591  33.350  50.356  1.00 53.16           N  
-ATOM   3526  CZ  ARG C 458       2.683  33.810  50.951  1.00 52.26           C  
-ATOM   3527  NH1 ARG C 458       2.622  34.239  52.211  1.00 42.19           N  
-ATOM   3528  NH2 ARG C 458       3.830  33.841  50.289  1.00 54.00           N  
-ATOM   3529  N   LEU C 459      -5.345  33.244  51.219  1.00 39.16           N  
-ATOM   3530  CA  LEU C 459      -6.457  33.578  52.096  1.00 41.39           C  
-ATOM   3531  C   LEU C 459      -7.640  32.654  51.793  1.00 43.69           C  
-ATOM   3532  O   LEU C 459      -8.695  32.769  52.409  1.00 45.28           O  
-ATOM   3533  CB  LEU C 459      -6.871  35.041  51.870  1.00 34.87           C  
-ATOM   3534  CG  LEU C 459      -5.858  36.129  52.253  1.00 32.65           C  
-ATOM   3535  CD1 LEU C 459      -6.217  37.449  51.600  1.00 28.40           C  
-ATOM   3536  CD2 LEU C 459      -5.816  36.268  53.770  1.00 24.55           C  
-ATOM   3537  N   SER C 460      -7.457  31.747  50.835  1.00 46.10           N  
-ATOM   3538  CA  SER C 460      -8.507  30.804  50.432  1.00 48.74           C  
-ATOM   3539  C   SER C 460      -7.909  29.463  49.963  1.00 49.05           C  
-ATOM   3540  O   SER C 460      -7.386  28.693  50.768  1.00 48.50           O  
-ATOM   3541  CB  SER C 460      -9.343  31.429  49.310  1.00 48.04           C  
-ATOM   3542  OG  SER C 460     -10.376  30.553  48.904  1.00 53.36           O  
-ATOM   3543  N   TYR C 461      -8.010  29.188  48.664  1.00 51.39           N  
-ATOM   3544  CA  TYR C 461      -7.453  27.972  48.063  1.00 54.05           C  
-ATOM   3545  C   TYR C 461      -7.399  28.061  46.540  1.00 54.17           C  
-ATOM   3546  O   TYR C 461      -8.035  28.927  45.937  1.00 53.19           O  
-ATOM   3547  CB  TYR C 461      -8.220  26.711  48.495  1.00 57.12           C  
-ATOM   3548  CG  TYR C 461      -9.724  26.792  48.412  1.00 64.10           C  
-ATOM   3549  CD1 TYR C 461     -10.462  27.437  49.406  1.00 66.49           C  
-ATOM   3550  CD2 TYR C 461     -10.415  26.202  47.354  1.00 67.68           C  
-ATOM   3551  CE1 TYR C 461     -11.850  27.490  49.351  1.00 70.06           C  
-ATOM   3552  CE2 TYR C 461     -11.807  26.250  47.287  1.00 71.52           C  
-ATOM   3553  CZ  TYR C 461     -12.517  26.895  48.289  1.00 72.32           C  
-ATOM   3554  OH  TYR C 461     -13.893  26.953  48.229  1.00 77.06           O  
-ATOM   3555  N   HIS C 462      -6.630  27.163  45.929  1.00 55.54           N  
-ATOM   3556  CA  HIS C 462      -6.434  27.136  44.478  1.00 57.65           C  
-ATOM   3557  C   HIS C 462      -7.709  27.160  43.644  1.00 58.77           C  
-ATOM   3558  O   HIS C 462      -7.928  28.081  42.851  1.00 58.85           O  
-ATOM   3559  CB  HIS C 462      -5.607  25.906  44.078  1.00 59.27           C  
-ATOM   3560  CG  HIS C 462      -5.177  25.903  42.642  1.00 61.98           C  
-ATOM   3561  ND1 HIS C 462      -4.715  24.773  42.005  1.00 62.79           N  
-ATOM   3562  CD2 HIS C 462      -5.116  26.901  41.725  1.00 63.17           C  
-ATOM   3563  CE1 HIS C 462      -4.388  25.072  40.759  1.00 62.88           C  
-ATOM   3564  NE2 HIS C 462      -4.622  26.357  40.564  1.00 59.51           N  
-ATOM   3565  N   GLN C 463      -8.540  26.137  43.814  1.00 60.02           N  
-ATOM   3566  CA  GLN C 463      -9.780  26.028  43.056  1.00 60.18           C  
-ATOM   3567  C   GLN C 463     -10.704  27.232  43.230  1.00 59.86           C  
-ATOM   3568  O   GLN C 463     -11.410  27.621  42.298  1.00 60.05           O  
-ATOM   3569  CB  GLN C 463     -10.519  24.746  43.444  1.00 61.90           C  
-ATOM   3570  CG  GLN C 463     -11.615  24.380  42.465  1.00 64.98           C  
-ATOM   3571  CD  GLN C 463     -11.110  24.360  41.032  1.00 66.45           C  
-ATOM   3572  OE1 GLN C 463     -10.196  23.606  40.695  1.00 67.46           O  
-ATOM   3573  NE2 GLN C 463     -11.701  25.195  40.182  1.00 65.85           N  
-ATOM   3574  N   ARG C 464     -10.693  27.824  44.420  1.00 59.01           N  
-ATOM   3575  CA  ARG C 464     -11.534  28.984  44.703  1.00 58.88           C  
-ATOM   3576  C   ARG C 464     -11.162  30.125  43.760  1.00 57.93           C  
-ATOM   3577  O   ARG C 464     -12.013  30.667  43.051  1.00 57.88           O  
-ATOM   3578  CB  ARG C 464     -11.331  29.439  46.153  1.00 60.21           C  
-ATOM   3579  CG  ARG C 464     -12.575  29.965  46.859  1.00 61.20           C  
-ATOM   3580  CD  ARG C 464     -13.262  31.103  46.121  1.00 64.92           C  
-ATOM   3581  NE  ARG C 464     -14.221  31.783  46.991  1.00 67.79           N  
-ATOM   3582  CZ  ARG C 464     -15.160  32.628  46.573  1.00 68.52           C  
-ATOM   3583  NH1 ARG C 464     -15.287  32.905  45.284  1.00 70.49           N  
-ATOM   3584  NH2 ARG C 464     -15.963  33.213  47.450  1.00 71.25           N  
-ATOM   3585  N   ILE C 465      -9.878  30.471  43.755  1.00 57.25           N  
-ATOM   3586  CA  ILE C 465      -9.358  31.557  42.926  1.00 57.26           C  
-ATOM   3587  C   ILE C 465      -9.476  31.256  41.438  1.00 57.78           C  
-ATOM   3588  O   ILE C 465      -9.664  32.156  40.614  1.00 56.95           O  
-ATOM   3589  CB  ILE C 465      -7.865  31.836  43.254  1.00 57.30           C  
-ATOM   3590  CG1 ILE C 465      -7.685  31.993  44.767  1.00 51.90           C  
-ATOM   3591  CG2 ILE C 465      -7.388  33.095  42.528  1.00 53.90           C  
-ATOM   3592  CD1 ILE C 465      -8.564  33.052  45.380  1.00 48.83           C  
-ATOM   3593  N   LEU C 466      -9.361  29.982  41.096  1.00 59.62           N  
-ATOM   3594  CA  LEU C 466      -9.444  29.571  39.707  1.00 61.21           C  
-ATOM   3595  C   LEU C 466     -10.857  29.773  39.166  1.00 61.32           C  
-ATOM   3596  O   LEU C 466     -11.059  29.836  37.953  1.00 62.65           O  
-ATOM   3597  CB  LEU C 466      -9.029  28.105  39.577  1.00 63.13           C  
-ATOM   3598  CG  LEU C 466      -8.537  27.655  38.200  1.00 63.39           C  
-ATOM   3599  CD1 LEU C 466      -7.371  28.526  37.738  1.00 59.72           C  
-ATOM   3600  CD2 LEU C 466      -8.116  26.197  38.282  1.00 64.79           C  
-ATOM   3601  N   ASP C 467     -11.831  29.886  40.066  1.00 61.50           N  
-ATOM   3602  CA  ASP C 467     -13.219  30.080  39.655  1.00 61.57           C  
-ATOM   3603  C   ASP C 467     -13.673  31.535  39.655  1.00 61.08           C  
-ATOM   3604  O   ASP C 467     -14.564  31.901  38.891  1.00 61.29           O  
-ATOM   3605  CB  ASP C 467     -14.168  29.254  40.535  1.00 61.19           C  
-ATOM   3606  CG  ASP C 467     -14.023  27.756  40.305  1.00 63.70           C  
-ATOM   3607  OD1 ASP C 467     -13.924  27.344  39.126  1.00 64.17           O  
-ATOM   3608  OD2 ASP C 467     -14.014  26.995  41.297  1.00 60.95           O  
-ATOM   3609  N   ILE C 468     -13.060  32.363  40.496  1.00 60.10           N  
-ATOM   3610  CA  ILE C 468     -13.434  33.773  40.573  1.00 59.91           C  
-ATOM   3611  C   ILE C 468     -12.885  34.580  39.401  1.00 59.55           C  
-ATOM   3612  O   ILE C 468     -13.285  35.722  39.189  1.00 60.18           O  
-ATOM   3613  CB  ILE C 468     -12.928  34.425  41.878  1.00 60.15           C  
-ATOM   3614  CG1 ILE C 468     -11.409  34.600  41.814  1.00 61.20           C  
-ATOM   3615  CG2 ILE C 468     -13.304  33.554  43.071  1.00 60.51           C  
-ATOM   3616  CD1 ILE C 468     -10.833  35.434  42.935  1.00 61.12           C  
-ATOM   3617  N   VAL C 469     -11.968  33.987  38.643  1.00 59.08           N  
-ATOM   3618  CA  VAL C 469     -11.368  34.670  37.500  1.00 59.26           C  
-ATOM   3619  C   VAL C 469     -11.853  34.123  36.159  1.00 59.66           C  
-ATOM   3620  O   VAL C 469     -12.148  32.932  36.031  1.00 59.44           O  
-ATOM   3621  CB  VAL C 469      -9.825  34.557  37.523  1.00 58.61           C  
-ATOM   3622  CG1 VAL C 469      -9.280  35.096  38.838  1.00 56.69           C  
-ATOM   3623  CG2 VAL C 469      -9.405  33.104  37.324  1.00 55.02           C  
-ATOM   3624  N   PRO C 470     -11.937  34.994  35.139  1.00 60.07           N  
-ATOM   3625  CA  PRO C 470     -12.383  34.583  33.805  1.00 61.17           C  
-ATOM   3626  C   PRO C 470     -11.448  33.523  33.236  1.00 62.51           C  
-ATOM   3627  O   PRO C 470     -10.283  33.434  33.628  1.00 62.49           O  
-ATOM   3628  CB  PRO C 470     -12.323  35.881  33.003  1.00 59.77           C  
-ATOM   3629  CG  PRO C 470     -12.598  36.924  34.038  1.00 59.77           C  
-ATOM   3630  CD  PRO C 470     -11.757  36.455  35.199  1.00 59.82           C  
-ATOM   3631  N   PRO C 471     -11.948  32.700  32.303  1.00 63.58           N  
-ATOM   3632  CA  PRO C 471     -11.136  31.646  31.689  1.00 62.76           C  
-ATOM   3633  C   PRO C 471      -9.835  32.191  31.101  1.00 61.32           C  
-ATOM   3634  O   PRO C 471      -8.798  31.532  31.147  1.00 60.01           O  
-ATOM   3635  CB  PRO C 471     -12.068  31.079  30.623  1.00 64.32           C  
-ATOM   3636  CG  PRO C 471     -13.422  31.239  31.256  1.00 65.63           C  
-ATOM   3637  CD  PRO C 471     -13.341  32.641  31.822  1.00 64.27           C  
-ATOM   3638  N   THR C 472      -9.900  33.402  30.558  1.00 61.49           N  
-ATOM   3639  CA  THR C 472      -8.733  34.039  29.961  1.00 62.42           C  
-ATOM   3640  C   THR C 472      -7.662  34.442  30.979  1.00 62.67           C  
-ATOM   3641  O   THR C 472      -6.629  34.997  30.606  1.00 62.97           O  
-ATOM   3642  CB  THR C 472      -9.144  35.292  29.157  1.00 63.08           C  
-ATOM   3643  OG1 THR C 472     -10.018  36.106  29.951  1.00 61.40           O  
-ATOM   3644  CG2 THR C 472      -9.850  34.892  27.868  1.00 63.59           C  
-ATOM   3645  N   PHE C 473      -7.911  34.161  32.257  1.00 62.29           N  
-ATOM   3646  CA  PHE C 473      -6.973  34.495  33.329  1.00 61.61           C  
-ATOM   3647  C   PHE C 473      -6.466  33.254  34.060  1.00 62.24           C  
-ATOM   3648  O   PHE C 473      -5.657  33.358  34.982  1.00 61.65           O  
-ATOM   3649  CB  PHE C 473      -7.630  35.428  34.355  1.00 59.09           C  
-ATOM   3650  CG  PHE C 473      -7.710  36.862  33.918  1.00 54.99           C  
-ATOM   3651  CD1 PHE C 473      -8.546  37.243  32.878  1.00 52.45           C  
-ATOM   3652  CD2 PHE C 473      -6.942  37.837  34.554  1.00 53.73           C  
-ATOM   3653  CE1 PHE C 473      -8.621  38.575  32.471  1.00 52.90           C  
-ATOM   3654  CE2 PHE C 473      -7.007  39.169  34.158  1.00 51.89           C  
-ATOM   3655  CZ  PHE C 473      -7.849  39.541  33.113  1.00 53.43           C  
-ATOM   3656  N   SER C 474      -6.946  32.084  33.655  1.00 61.96           N  
-ATOM   3657  CA  SER C 474      -6.539  30.832  34.288  1.00 62.26           C  
-ATOM   3658  C   SER C 474      -5.020  30.684  34.321  1.00 62.02           C  
-ATOM   3659  O   SER C 474      -4.463  30.063  35.227  1.00 61.69           O  
-ATOM   3660  CB  SER C 474      -7.152  29.648  33.541  1.00 63.31           C  
-ATOM   3661  OG  SER C 474      -6.815  29.688  32.164  1.00 65.00           O  
-ATOM   3662  N   ALA C 475      -4.358  31.259  33.325  1.00 62.72           N  
-ATOM   3663  CA  ALA C 475      -2.906  31.193  33.227  1.00 62.88           C  
-ATOM   3664  C   ALA C 475      -2.229  32.008  34.325  1.00 62.29           C  
-ATOM   3665  O   ALA C 475      -1.212  31.591  34.880  1.00 62.76           O  
-ATOM   3666  CB  ALA C 475      -2.455  31.691  31.855  1.00 63.07           C  
-ATOM   3667  N   LEU C 476      -2.798  33.169  34.637  1.00 61.42           N  
-ATOM   3668  CA  LEU C 476      -2.238  34.043  35.662  1.00 59.39           C  
-ATOM   3669  C   LEU C 476      -2.499  33.553  37.082  1.00 58.54           C  
-ATOM   3670  O   LEU C 476      -2.027  34.155  38.044  1.00 57.89           O  
-ATOM   3671  CB  LEU C 476      -2.779  35.464  35.502  1.00 58.99           C  
-ATOM   3672  CG  LEU C 476      -2.284  36.263  34.292  1.00 61.47           C  
-ATOM   3673  CD1 LEU C 476      -2.718  35.580  33.004  1.00 63.83           C  
-ATOM   3674  CD2 LEU C 476      -2.837  37.674  34.354  1.00 62.34           C  
-ATOM   3675  N   CYS C 477      -3.244  32.459  37.212  1.00 57.76           N  
-ATOM   3676  CA  CYS C 477      -3.551  31.905  38.526  1.00 57.22           C  
-ATOM   3677  C   CYS C 477      -2.372  31.125  39.090  1.00 57.69           C  
-ATOM   3678  O   CYS C 477      -1.542  30.613  38.344  1.00 59.21           O  
-ATOM   3679  CB  CYS C 477      -4.778  30.994  38.450  1.00 56.74           C  
-ATOM   3680  SG  CYS C 477      -6.339  31.872  38.213  1.00 60.03           S  
-ATOM   3681  N   PRO C 478      -2.280  31.033  40.424  1.00 57.51           N  
-ATOM   3682  CA  PRO C 478      -1.182  30.305  41.062  1.00 57.51           C  
-ATOM   3683  C   PRO C 478      -1.292  28.796  40.885  1.00 59.70           C  
-ATOM   3684  O   PRO C 478      -2.386  28.231  40.948  1.00 60.34           O  
-ATOM   3685  CB  PRO C 478      -1.293  30.732  42.522  1.00 55.53           C  
-ATOM   3686  CG  PRO C 478      -2.758  30.950  42.691  1.00 53.49           C  
-ATOM   3687  CD  PRO C 478      -3.132  31.686  41.433  1.00 53.80           C  
-ATOM   3688  N   SER C 479      -0.157  28.145  40.654  1.00 59.81           N  
-ATOM   3689  CA  SER C 479      -0.149  26.704  40.481  1.00 60.20           C  
-ATOM   3690  C   SER C 479      -0.574  26.075  41.798  1.00 60.75           C  
-ATOM   3691  O   SER C 479      -0.576  26.733  42.838  1.00 59.82           O  
-ATOM   3692  CB  SER C 479       1.250  26.217  40.084  1.00 60.05           C  
-ATOM   3693  OG  SER C 479       2.195  26.478  41.106  1.00 62.52           O  
-ATOM   3694  N   ASN C 480      -0.941  24.803  41.755  1.00 61.47           N  
-ATOM   3695  CA  ASN C 480      -1.373  24.116  42.957  1.00 63.32           C  
-ATOM   3696  C   ASN C 480      -0.168  23.830  43.854  1.00 64.05           C  
-ATOM   3697  O   ASN C 480       0.786  23.178  43.435  1.00 64.53           O  
-ATOM   3698  CB  ASN C 480      -2.092  22.822  42.575  1.00 65.67           C  
-ATOM   3699  CG  ASN C 480      -2.929  22.266  43.707  1.00 67.70           C  
-ATOM   3700  OD1 ASN C 480      -3.688  22.995  44.349  1.00 67.60           O  
-ATOM   3701  ND2 ASN C 480      -2.804  20.968  43.951  1.00 69.23           N  
-ATOM   3702  N   PRO C 481      -0.198  24.327  45.102  1.00 64.74           N  
-ATOM   3703  CA  PRO C 481       0.867  24.159  46.100  1.00 65.14           C  
-ATOM   3704  C   PRO C 481       1.062  22.735  46.602  1.00 66.26           C  
-ATOM   3705  O   PRO C 481       0.836  22.441  47.777  1.00 66.45           O  
-ATOM   3706  CB  PRO C 481       0.439  25.103  47.216  1.00 64.42           C  
-ATOM   3707  CG  PRO C 481      -1.049  25.018  47.151  1.00 64.06           C  
-ATOM   3708  CD  PRO C 481      -1.307  25.117  45.664  1.00 63.78           C  
-ATOM   3709  N   THR C 482       1.502  21.858  45.709  1.00 67.46           N  
-ATOM   3710  CA  THR C 482       1.725  20.465  46.060  1.00 68.33           C  
-ATOM   3711  C   THR C 482       3.193  20.156  46.314  1.00 69.62           C  
-ATOM   3712  O   THR C 482       4.078  20.661  45.621  1.00 69.28           O  
-ATOM   3713  CB  THR C 482       1.211  19.547  44.956  1.00 67.87           C  
-ATOM   3714  OG1 THR C 482       1.650  20.043  43.687  1.00 70.11           O  
-ATOM   3715  CG2 THR C 482      -0.306  19.494  44.979  1.00 67.38           C  
-ATOM   3716  N   CYS C 483       3.432  19.319  47.320  1.00 70.44           N  
-ATOM   3717  CA  CYS C 483       4.773  18.904  47.710  1.00 72.01           C  
-ATOM   3718  C   CYS C 483       5.506  18.202  46.568  1.00 72.92           C  
-ATOM   3719  O   CYS C 483       4.889  17.746  45.601  1.00 72.87           O  
-ATOM   3720  CB  CYS C 483       4.682  17.969  48.917  1.00 72.88           C  
-ATOM   3721  SG  CYS C 483       6.261  17.364  49.528  1.00 79.01           S  
-ATOM   3722  N   ILE C 484       6.828  18.129  46.684  1.00 73.34           N  
-ATOM   3723  CA  ILE C 484       7.652  17.476  45.674  1.00 74.07           C  
-ATOM   3724  C   ILE C 484       8.646  16.529  46.332  1.00 75.66           C  
-ATOM   3725  O   ILE C 484       9.425  16.932  47.197  1.00 74.65           O  
-ATOM   3726  CB  ILE C 484       8.436  18.502  44.823  1.00 71.68           C  
-ATOM   3727  CG1 ILE C 484       7.466  19.311  43.961  1.00 68.60           C  
-ATOM   3728  CG2 ILE C 484       9.449  17.786  43.944  1.00 70.52           C  
-ATOM   3729  CD1 ILE C 484       8.140  20.335  43.078  1.00 67.17           C  
-ATOM   3730  N   TYR C 485       8.606  15.266  45.920  1.00 77.45           N  
-ATOM   3731  CA  TYR C 485       9.504  14.256  46.458  1.00 79.95           C  
-ATOM   3732  C   TYR C 485      10.361  13.691  45.327  1.00 81.73           C  
-ATOM   3733  O   TYR C 485       9.841  13.254  44.299  1.00 81.41           O  
-ATOM   3734  CB  TYR C 485       8.704  13.130  47.106  1.00 79.96           C  
-ATOM   3735  CG  TYR C 485       9.514  12.251  48.030  1.00 82.41           C  
-ATOM   3736  CD1 TYR C 485       8.990  11.057  48.519  1.00 84.14           C  
-ATOM   3737  CD2 TYR C 485      10.796  12.622  48.435  1.00 83.43           C  
-ATOM   3738  CE1 TYR C 485       9.719  10.252  49.389  1.00 85.57           C  
-ATOM   3739  CE2 TYR C 485      11.533  11.826  49.304  1.00 85.87           C  
-ATOM   3740  CZ  TYR C 485      10.988  10.642  49.778  1.00 86.57           C  
-ATOM   3741  OH  TYR C 485      11.709   9.850  50.643  1.00 88.10           O  
-ATOM   3742  N   LYS C 486      11.676  13.708  45.522  1.00 83.45           N  
-ATOM   3743  CA  LYS C 486      12.604  13.201  44.518  1.00 85.56           C  
-ATOM   3744  C   LYS C 486      12.665  11.680  44.606  1.00 86.67           C  
-ATOM   3745  O   LYS C 486      13.012  11.005  43.640  1.00 86.05           O  
-ATOM   3746  CB  LYS C 486      13.995  13.800  44.751  1.00 85.94           C  
-ATOM   3747  CG  LYS C 486      14.957  13.658  43.584  1.00 86.39           C  
-ATOM   3748  CD  LYS C 486      16.214  14.482  43.823  1.00 86.31           C  
-ATOM   3749  CE  LYS C 486      17.088  14.542  42.583  1.00 86.93           C  
-ATOM   3750  NZ  LYS C 486      18.250  15.451  42.785  1.00 87.46           N  
-ATOM   3751  N   TYR C 487      12.311  11.156  45.776  1.00 88.25           N  
-ATOM   3752  CA  TYR C 487      12.320   9.720  46.032  1.00 90.82           C  
-ATOM   3753  C   TYR C 487      10.897   9.200  46.231  1.00 92.67           C  
-ATOM   3754  O   TYR C 487      10.645   8.377  47.113  1.00 92.55           O  
-ATOM   3755  CB  TYR C 487      13.148   9.430  47.287  1.00 90.48           C  
-ATOM   3756  CG  TYR C 487      14.556   9.981  47.242  1.00 90.34           C  
-ATOM   3757  CD1 TYR C 487      15.234  10.298  48.417  1.00 89.43           C  
-ATOM   3758  CD2 TYR C 487      15.217  10.175  46.026  1.00 90.79           C  
-ATOM   3759  CE1 TYR C 487      16.533  10.796  48.386  1.00 90.01           C  
-ATOM   3760  CE2 TYR C 487      16.518  10.670  45.983  1.00 89.77           C  
-ATOM   3761  CZ  TYR C 487      17.169  10.979  47.167  1.00 90.46           C  
-ATOM   3762  OH  TYR C 487      18.455  11.469  47.133  1.00 89.54           O  
-ATOM   3763  N   GLY C 488       9.972   9.682  45.407  1.00 94.64           N  
-ATOM   3764  CA  GLY C 488       8.587   9.260  45.523  1.00 97.17           C  
-ATOM   3765  C   GLY C 488       8.203   8.119  44.598  1.00 98.96           C  
-ATOM   3766  O   GLY C 488       9.048   7.306  44.218  1.00 99.27           O  
-ATOM   3767  N   ASP C 489       6.923   8.059  44.239  1.00100.43           N  
-ATOM   3768  CA  ASP C 489       6.413   7.013  43.357  1.00101.82           C  
-ATOM   3769  C   ASP C 489       6.717   7.323  41.893  1.00102.46           C  
-ATOM   3770  O   ASP C 489       6.117   6.744  40.989  1.00102.74           O  
-ATOM   3771  CB  ASP C 489       4.899   6.846  43.548  1.00102.87           C  
-ATOM   3772  CG  ASP C 489       4.528   6.428  44.964  1.00104.04           C  
-ATOM   3773  OD1 ASP C 489       4.971   5.346  45.403  1.00105.07           O  
-ATOM   3774  OD2 ASP C 489       3.792   7.181  45.638  1.00104.42           O  
-ATOM   3775  N   GLU C 490       7.650   8.245  41.671  1.00103.08           N  
-ATOM   3776  CA  GLU C 490       8.059   8.634  40.324  1.00103.95           C  
-ATOM   3777  C   GLU C 490       9.564   8.423  40.194  1.00103.93           C  
-ATOM   3778  O   GLU C 490      10.094   8.251  39.093  1.00103.74           O  
-ATOM   3779  CB  GLU C 490       7.736  10.111  40.069  1.00104.90           C  
-ATOM   3780  CG  GLU C 490       8.217  10.626  38.714  1.00106.55           C  
-ATOM   3781  CD  GLU C 490       8.246  12.143  38.634  1.00108.05           C  
-ATOM   3782  OE1 GLU C 490       8.968  12.766  39.441  1.00108.36           O  
-ATOM   3783  OE2 GLU C 490       7.549  12.710  37.764  1.00108.69           O  
-ATOM   3784  N   SER C 491      10.243   8.442  41.337  1.00103.91           N  
-ATOM   3785  CA  SER C 491      11.688   8.268  41.391  1.00103.89           C  
-ATOM   3786  C   SER C 491      12.123   6.946  40.775  1.00104.15           C  
-ATOM   3787  O   SER C 491      11.304   6.183  40.260  1.00104.46           O  
-ATOM   3788  CB  SER C 491      12.169   8.331  42.843  1.00103.94           C  
-ATOM   3789  OG  SER C 491      11.661   7.244  43.599  1.00104.20           O  
-ATOM   3790  N   SER C 492      13.425   6.685  40.833  1.00103.90           N  
-ATOM   3791  CA  SER C 492      13.991   5.455  40.299  1.00103.47           C  
-ATOM   3792  C   SER C 492      14.989   4.870  41.295  1.00103.10           C  
-ATOM   3793  O   SER C 492      15.486   5.572  42.178  1.00102.93           O  
-ATOM   3794  CB  SER C 492      14.681   5.724  38.957  1.00103.29           C  
-ATOM   3795  OG  SER C 492      15.717   6.680  39.091  1.00103.28           O  
-ATOM   3796  N   ASN C 493      15.267   3.579  41.156  1.00102.69           N  
-ATOM   3797  CA  ASN C 493      16.205   2.904  42.043  1.00102.12           C  
-ATOM   3798  C   ASN C 493      17.635   3.363  41.768  1.00101.43           C  
-ATOM   3799  O   ASN C 493      18.547   3.088  42.549  1.00101.16           O  
-ATOM   3800  CB  ASN C 493      16.093   1.381  41.872  1.00102.80           C  
-ATOM   3801  CG  ASN C 493      16.231   0.932  40.419  1.00103.06           C  
-ATOM   3802  OD1 ASN C 493      16.140  -0.261  40.119  1.00103.31           O  
-ATOM   3803  ND2 ASN C 493      16.449   1.882  39.514  1.00102.83           N  
-ATOM   3804  N   SER C 494      17.819   4.071  40.658  1.00100.46           N  
-ATOM   3805  CA  SER C 494      19.133   4.573  40.273  1.00 99.33           C  
-ATOM   3806  C   SER C 494      19.345   6.010  40.747  1.00 98.78           C  
-ATOM   3807  O   SER C 494      19.689   6.892  39.957  1.00 98.86           O  
-ATOM   3808  CB  SER C 494      19.299   4.491  38.751  1.00 98.88           C  
-ATOM   3809  OG  SER C 494      18.252   5.170  38.081  1.00 96.86           O  
-ATOM   3810  N   LEU C 495      19.140   6.235  42.042  1.00 97.97           N  
-ATOM   3811  CA  LEU C 495      19.307   7.559  42.634  1.00 96.98           C  
-ATOM   3812  C   LEU C 495      20.205   7.522  43.863  1.00 96.53           C  
-ATOM   3813  O   LEU C 495      20.112   6.611  44.686  1.00 96.35           O  
-ATOM   3814  CB  LEU C 495      17.950   8.143  43.031  1.00 97.20           C  
-ATOM   3815  CG  LEU C 495      17.028   8.612  41.904  1.00 97.74           C  
-ATOM   3816  CD1 LEU C 495      15.679   9.002  42.484  1.00 98.03           C  
-ATOM   3817  CD2 LEU C 495      17.661   9.788  41.173  1.00 96.94           C  
-ATOM   3818  N   PRO C 496      21.087   8.523  44.004  1.00 96.03           N  
-ATOM   3819  CA  PRO C 496      22.010   8.618  45.138  1.00 95.77           C  
-ATOM   3820  C   PRO C 496      21.281   8.537  46.480  1.00 95.66           C  
-ATOM   3821  O   PRO C 496      20.378   9.329  46.752  1.00 95.97           O  
-ATOM   3822  CB  PRO C 496      22.671   9.976  44.925  1.00 95.69           C  
-ATOM   3823  CG  PRO C 496      22.695  10.100  43.434  1.00 95.50           C  
-ATOM   3824  CD  PRO C 496      21.316   9.623  43.050  1.00 96.08           C  
-ATOM   3825  N   GLY C 497      21.675   7.575  47.310  1.00 95.18           N  
-ATOM   3826  CA  GLY C 497      21.055   7.417  48.615  1.00 94.68           C  
-ATOM   3827  C   GLY C 497      19.569   7.130  48.549  1.00 94.33           C  
-ATOM   3828  O   GLY C 497      18.838   7.347  49.517  1.00 94.31           O  
-ATOM   3829  N   HIS C 498      19.122   6.636  47.401  1.00 94.06           N  
-ATOM   3830  CA  HIS C 498      17.718   6.312  47.196  1.00 94.17           C  
-ATOM   3831  C   HIS C 498      17.165   5.421  48.308  1.00 94.35           C  
-ATOM   3832  O   HIS C 498      16.296   5.835  49.078  1.00 94.26           O  
-ATOM   3833  CB  HIS C 498      17.544   5.613  45.847  1.00 94.27           C  
-ATOM   3834  CG  HIS C 498      16.151   5.134  45.593  1.00 94.91           C  
-ATOM   3835  ND1 HIS C 498      15.076   5.990  45.498  1.00 95.79           N  
-ATOM   3836  CD2 HIS C 498      15.654   3.885  45.429  1.00 95.54           C  
-ATOM   3837  CE1 HIS C 498      13.976   5.290  45.287  1.00 96.75           C  
-ATOM   3838  NE2 HIS C 498      14.299   4.010  45.240  1.00 95.72           N  
-ATOM   3839  N   SER C 499      17.676   4.197  48.382  1.00 94.24           N  
-ATOM   3840  CA  SER C 499      17.235   3.230  49.381  1.00 94.73           C  
-ATOM   3841  C   SER C 499      17.424   3.699  50.822  1.00 94.66           C  
-ATOM   3842  O   SER C 499      16.669   3.302  51.711  1.00 94.75           O  
-ATOM   3843  CB  SER C 499      17.967   1.899  49.175  1.00 95.38           C  
-ATOM   3844  OG  SER C 499      19.373   2.075  49.221  1.00 96.81           O  
-ATOM   3845  N   VAL C 500      18.427   4.540  51.054  1.00 94.77           N  
-ATOM   3846  CA  VAL C 500      18.700   5.046  52.399  1.00 95.07           C  
-ATOM   3847  C   VAL C 500      17.544   5.894  52.925  1.00 95.14           C  
-ATOM   3848  O   VAL C 500      17.227   5.866  54.117  1.00 95.06           O  
-ATOM   3849  CB  VAL C 500      19.985   5.900  52.427  1.00 94.82           C  
-ATOM   3850  CG1 VAL C 500      20.311   6.302  53.860  1.00 94.67           C  
-ATOM   3851  CG2 VAL C 500      21.138   5.122  51.813  1.00 94.54           C  
-ATOM   3852  N   ALA C 501      16.922   6.649  52.027  1.00 95.09           N  
-ATOM   3853  CA  ALA C 501      15.799   7.504  52.389  1.00 94.97           C  
-ATOM   3854  C   ALA C 501      14.552   6.655  52.595  1.00 94.42           C  
-ATOM   3855  O   ALA C 501      13.781   6.875  53.531  1.00 94.05           O  
-ATOM   3856  CB  ALA C 501      15.553   8.534  51.292  1.00 95.94           C  
-ATOM   3857  N   LEU C 502      14.364   5.684  51.707  1.00 93.89           N  
-ATOM   3858  CA  LEU C 502      13.217   4.788  51.773  1.00 93.21           C  
-ATOM   3859  C   LEU C 502      13.187   4.092  53.129  1.00 92.82           C  
-ATOM   3860  O   LEU C 502      12.121   3.746  53.641  1.00 92.89           O  
-ATOM   3861  CB  LEU C 502      13.299   3.751  50.651  1.00 92.14           C  
-ATOM   3862  CG  LEU C 502      13.550   4.312  49.246  1.00 91.40           C  
-ATOM   3863  CD1 LEU C 502      13.638   3.164  48.258  1.00 91.14           C  
-ATOM   3864  CD2 LEU C 502      12.439   5.278  48.854  1.00 90.39           C  
-ATOM   3865  N   CYS C 503      14.368   3.894  53.706  1.00 92.40           N  
-ATOM   3866  CA  CYS C 503      14.491   3.251  55.008  1.00 91.81           C  
-ATOM   3867  C   CYS C 503      14.168   4.260  56.106  1.00 91.15           C  
-ATOM   3868  O   CYS C 503      13.707   3.894  57.187  1.00 91.05           O  
-ATOM   3869  CB  CYS C 503      15.909   2.706  55.198  1.00 92.60           C  
-ATOM   3870  SG  CYS C 503      16.373   1.407  54.022  1.00 94.92           S  
-ATOM   3871  N   LEU C 504      14.418   5.534  55.821  1.00 90.16           N  
-ATOM   3872  CA  LEU C 504      14.138   6.596  56.778  1.00 89.06           C  
-ATOM   3873  C   LEU C 504      12.633   6.807  56.878  1.00 88.42           C  
-ATOM   3874  O   LEU C 504      12.101   7.050  57.962  1.00 87.86           O  
-ATOM   3875  CB  LEU C 504      14.815   7.896  56.340  1.00 88.06           C  
-ATOM   3876  CG  LEU C 504      16.333   7.963  56.511  1.00 86.69           C  
-ATOM   3877  CD1 LEU C 504      16.883   9.122  55.702  1.00 85.36           C  
-ATOM   3878  CD2 LEU C 504      16.678   8.110  57.990  1.00 84.84           C  
-ATOM   3879  N   ALA C 505      11.955   6.709  55.737  1.00 88.03           N  
-ATOM   3880  CA  ALA C 505      10.508   6.883  55.675  1.00 87.54           C  
-ATOM   3881  C   ALA C 505       9.840   5.978  56.700  1.00 87.28           C  
-ATOM   3882  O   ALA C 505       8.897   6.379  57.386  1.00 87.48           O  
-ATOM   3883  CB  ALA C 505      10.004   6.549  54.277  1.00 87.47           C  
-ATOM   3884  N   VAL C 506      10.342   4.753  56.800  1.00 86.41           N  
-ATOM   3885  CA  VAL C 506       9.803   3.779  57.737  1.00 85.40           C  
-ATOM   3886  C   VAL C 506      10.265   4.108  59.155  1.00 85.09           C  
-ATOM   3887  O   VAL C 506       9.559   3.841  60.128  1.00 85.21           O  
-ATOM   3888  CB  VAL C 506      10.273   2.355  57.375  1.00 85.47           C  
-ATOM   3889  CG1 VAL C 506       9.539   1.332  58.224  1.00 85.71           C  
-ATOM   3890  CG2 VAL C 506      10.049   2.093  55.893  1.00 84.35           C  
-ATOM   3891  N   ALA C 507      11.457   4.690  59.257  1.00 84.45           N  
-ATOM   3892  CA  ALA C 507      12.041   5.062  60.542  1.00 83.97           C  
-ATOM   3893  C   ALA C 507      11.208   6.138  61.227  1.00 83.36           C  
-ATOM   3894  O   ALA C 507      10.978   6.089  62.438  1.00 82.56           O  
-ATOM   3895  CB  ALA C 507      13.468   5.559  60.337  1.00 84.38           C  
-ATOM   3896  N   PHE C 508      10.770   7.114  60.440  1.00 83.41           N  
-ATOM   3897  CA  PHE C 508       9.957   8.210  60.950  1.00 83.21           C  
-ATOM   3898  C   PHE C 508       8.574   7.693  61.332  1.00 84.06           C  
-ATOM   3899  O   PHE C 508       8.028   8.074  62.369  1.00 83.78           O  
-ATOM   3900  CB  PHE C 508       9.845   9.315  59.892  1.00 80.00           C  
-ATOM   3901  CG  PHE C 508      11.108  10.121  59.715  1.00 76.01           C  
-ATOM   3902  CD1 PHE C 508      11.514  10.536  58.449  1.00 74.41           C  
-ATOM   3903  CD2 PHE C 508      11.878  10.487  60.816  1.00 73.03           C  
-ATOM   3904  CE1 PHE C 508      12.666  11.305  58.285  1.00 70.03           C  
-ATOM   3905  CE2 PHE C 508      13.031  11.257  60.661  1.00 69.80           C  
-ATOM   3906  CZ  PHE C 508      13.424  11.665  59.394  1.00 69.12           C  
-ATOM   3907  N   LYS C 509       8.020   6.814  60.498  1.00 84.75           N  
-ATOM   3908  CA  LYS C 509       6.703   6.234  60.754  1.00 85.08           C  
-ATOM   3909  C   LYS C 509       6.711   5.409  62.038  1.00 85.73           C  
-ATOM   3910  O   LYS C 509       5.793   5.504  62.853  1.00 86.01           O  
-ATOM   3911  CB  LYS C 509       6.267   5.347  59.581  1.00 83.12           C  
-ATOM   3912  CG  LYS C 509       5.988   6.098  58.284  1.00 81.99           C  
-ATOM   3913  CD  LYS C 509       5.665   5.134  57.149  1.00 80.12           C  
-ATOM   3914  CE  LYS C 509       5.375   5.866  55.845  1.00 81.02           C  
-ATOM   3915  NZ  LYS C 509       4.129   6.681  55.910  1.00 82.10           N  
-ATOM   3916  N   SER C 510       7.755   4.605  62.218  1.00 86.32           N  
-ATOM   3917  CA  SER C 510       7.872   3.763  63.404  1.00 87.18           C  
-ATOM   3918  C   SER C 510       8.227   4.570  64.648  1.00 87.24           C  
-ATOM   3919  O   SER C 510       8.536   4.002  65.696  1.00 87.50           O  
-ATOM   3920  CB  SER C 510       8.929   2.681  63.178  1.00 87.49           C  
-ATOM   3921  OG  SER C 510      10.203   3.257  62.950  1.00 91.26           O  
-ATOM   3922  N   LYS C 511       8.183   5.893  64.528  1.00 87.26           N  
-ATOM   3923  CA  LYS C 511       8.498   6.774  65.645  1.00 87.19           C  
-ATOM   3924  C   LYS C 511       9.848   6.416  66.259  1.00 87.30           C  
-ATOM   3925  O   LYS C 511       9.917   5.667  67.232  1.00 87.50           O  
-ATOM   3926  CB  LYS C 511       7.398   6.679  66.707  1.00 87.05           C  
-ATOM   3927  CG  LYS C 511       7.662   7.503  67.953  1.00 88.48           C  
-ATOM   3928  CD  LYS C 511       7.904   8.967  67.612  1.00 90.55           C  
-ATOM   3929  CE  LYS C 511       8.291   9.767  68.847  1.00 90.07           C  
-ATOM   3930  NZ  LYS C 511       8.604  11.181  68.506  1.00 89.31           N  
-ATOM   3931  N   ALA C 512      10.919   6.956  65.683  1.00 87.36           N  
-ATOM   3932  CA  ALA C 512      12.269   6.691  66.168  1.00 87.57           C  
-ATOM   3933  C   ALA C 512      12.841   7.901  66.900  1.00 87.76           C  
-ATOM   3934  O   ALA C 512      12.173   8.926  67.035  1.00 87.97           O  
-ATOM   3935  CB  ALA C 512      13.171   6.318  64.999  1.00 87.31           C  
-ATOM   3936  N   THR C 513      14.073   7.776  67.382  1.00 87.67           N  
-ATOM   3937  CA  THR C 513      14.722   8.880  68.081  1.00 88.15           C  
-ATOM   3938  C   THR C 513      15.860   9.410  67.222  1.00 87.57           C  
-ATOM   3939  O   THR C 513      16.193   8.820  66.192  1.00 88.45           O  
-ATOM   3940  CB  THR C 513      15.293   8.444  69.455  1.00 89.49           C  
-ATOM   3941  OG1 THR C 513      15.844   9.587  70.126  1.00 90.67           O  
-ATOM   3942  CG2 THR C 513      16.386   7.394  69.278  1.00 89.48           C  
-ATOM   3943  N   ASN C 514      16.453  10.522  67.642  1.00 86.35           N  
-ATOM   3944  CA  ASN C 514      17.554  11.112  66.892  1.00 85.51           C  
-ATOM   3945  C   ASN C 514      18.657  10.086  66.667  1.00 85.37           C  
-ATOM   3946  O   ASN C 514      19.070   9.843  65.532  1.00 85.07           O  
-ATOM   3947  CB  ASN C 514      18.117  12.327  67.636  1.00 83.32           C  
-ATOM   3948  CG  ASN C 514      17.127  13.475  67.710  1.00 80.41           C  
-ATOM   3949  OD1 ASN C 514      16.649  13.959  66.687  1.00 74.67           O  
-ATOM   3950  ND2 ASN C 514      16.818  13.917  68.925  1.00 80.97           N  
-ATOM   3951  N   ASP C 515      19.119   9.479  67.756  1.00 85.56           N  
-ATOM   3952  CA  ASP C 515      20.180   8.480  67.697  1.00 85.79           C  
-ATOM   3953  C   ASP C 515      19.880   7.402  66.660  1.00 85.55           C  
-ATOM   3954  O   ASP C 515      20.782   6.913  65.981  1.00 85.17           O  
-ATOM   3955  CB  ASP C 515      20.370   7.846  69.076  1.00 86.66           C  
-ATOM   3956  CG  ASP C 515      20.515   8.883  70.175  1.00 89.49           C  
-ATOM   3957  OD1 ASP C 515      19.529   9.609  70.436  1.00 90.02           O  
-ATOM   3958  OD2 ASP C 515      21.611   8.980  70.770  1.00 89.15           O  
-ATOM   3959  N   GLU C 516      18.608   7.040  66.534  1.00 85.19           N  
-ATOM   3960  CA  GLU C 516      18.206   6.024  65.572  1.00 84.73           C  
-ATOM   3961  C   GLU C 516      18.387   6.522  64.144  1.00 84.01           C  
-ATOM   3962  O   GLU C 516      18.986   5.835  63.318  1.00 83.68           O  
-ATOM   3963  CB  GLU C 516      16.747   5.625  65.799  1.00 87.05           C  
-ATOM   3964  CG  GLU C 516      16.502   4.884  67.103  1.00 89.38           C  
-ATOM   3965  CD  GLU C 516      15.060   4.443  67.253  1.00 92.76           C  
-ATOM   3966  OE1 GLU C 516      14.577   3.693  66.376  1.00 93.50           O  
-ATOM   3967  OE2 GLU C 516      14.413   4.844  68.245  1.00 93.21           O  
-ATOM   3968  N   ILE C 517      17.869   7.714  63.857  1.00 83.45           N  
-ATOM   3969  CA  ILE C 517      17.988   8.295  62.521  1.00 82.16           C  
-ATOM   3970  C   ILE C 517      19.457   8.556  62.187  1.00 81.58           C  
-ATOM   3971  O   ILE C 517      19.868   8.462  61.027  1.00 80.99           O  
-ATOM   3972  CB  ILE C 517      17.183   9.624  62.398  1.00 81.75           C  
-ATOM   3973  CG1 ILE C 517      15.685   9.326  62.295  1.00 79.32           C  
-ATOM   3974  CG2 ILE C 517      17.615  10.397  61.157  1.00 80.87           C  
-ATOM   3975  CD1 ILE C 517      15.088   8.706  63.531  1.00 77.63           C  
-ATOM   3976  N   PHE C 518      20.246   8.881  63.207  1.00 80.89           N  
-ATOM   3977  CA  PHE C 518      21.667   9.140  63.011  1.00 80.51           C  
-ATOM   3978  C   PHE C 518      22.361   7.922  62.412  1.00 81.28           C  
-ATOM   3979  O   PHE C 518      23.030   8.019  61.382  1.00 81.92           O  
-ATOM   3980  CB  PHE C 518      22.340   9.497  64.340  1.00 77.91           C  
-ATOM   3981  CG  PHE C 518      22.355  10.969  64.642  1.00 74.40           C  
-ATOM   3982  CD1 PHE C 518      22.786  11.882  63.683  1.00 73.13           C  
-ATOM   3983  CD2 PHE C 518      21.967  11.442  65.890  1.00 71.19           C  
-ATOM   3984  CE1 PHE C 518      22.832  13.243  63.963  1.00 69.88           C  
-ATOM   3985  CE2 PHE C 518      22.009  12.802  66.179  1.00 69.83           C  
-ATOM   3986  CZ  PHE C 518      22.443  13.704  65.213  1.00 69.87           C  
-ATOM   3987  N   SER C 519      22.189   6.776  63.066  1.00 81.61           N  
-ATOM   3988  CA  SER C 519      22.801   5.528  62.624  1.00 81.61           C  
-ATOM   3989  C   SER C 519      22.281   5.093  61.252  1.00 80.91           C  
-ATOM   3990  O   SER C 519      22.964   4.387  60.511  1.00 80.64           O  
-ATOM   3991  CB  SER C 519      22.538   4.429  63.661  1.00 81.95           C  
-ATOM   3992  OG  SER C 519      23.428   3.340  63.493  1.00 85.17           O  
-ATOM   3993  N   ILE C 520      21.072   5.525  60.915  1.00 80.53           N  
-ATOM   3994  CA  ILE C 520      20.468   5.178  59.635  1.00 80.30           C  
-ATOM   3995  C   ILE C 520      21.090   6.001  58.519  1.00 81.15           C  
-ATOM   3996  O   ILE C 520      21.135   5.572  57.367  1.00 81.09           O  
-ATOM   3997  CB  ILE C 520      18.951   5.440  59.662  1.00 79.33           C  
-ATOM   3998  CG1 ILE C 520      18.324   4.652  60.813  1.00 76.77           C  
-ATOM   3999  CG2 ILE C 520      18.324   5.056  58.323  1.00 76.02           C  
-ATOM   4000  CD1 ILE C 520      16.895   5.017  61.099  1.00 78.11           C  
-ATOM   4001  N   LEU C 521      21.565   7.190  58.872  1.00 82.52           N  
-ATOM   4002  CA  LEU C 521      22.187   8.086  57.908  1.00 84.25           C  
-ATOM   4003  C   LEU C 521      23.652   7.729  57.708  1.00 85.40           C  
-ATOM   4004  O   LEU C 521      24.354   8.368  56.927  1.00 86.23           O  
-ATOM   4005  CB  LEU C 521      22.072   9.537  58.379  1.00 83.68           C  
-ATOM   4006  CG  LEU C 521      20.668  10.143  58.391  1.00 83.09           C  
-ATOM   4007  CD1 LEU C 521      20.725  11.534  58.999  1.00 82.36           C  
-ATOM   4008  CD2 LEU C 521      20.116  10.196  56.976  1.00 80.77           C  
-ATOM   4009  N   LYS C 522      24.108   6.704  58.420  1.00 86.60           N  
-ATOM   4010  CA  LYS C 522      25.490   6.254  58.318  1.00 87.49           C  
-ATOM   4011  C   LYS C 522      25.738   5.592  56.965  1.00 88.41           C  
-ATOM   4012  O   LYS C 522      26.791   5.779  56.356  1.00 88.46           O  
-ATOM   4013  CB  LYS C 522      25.802   5.255  59.435  1.00 86.74           C  
-ATOM   4014  CG  LYS C 522      25.796   5.841  60.838  1.00 86.65           C  
-ATOM   4015  CD  LYS C 522      27.082   6.593  61.139  1.00 86.98           C  
-ATOM   4016  CE  LYS C 522      27.170   6.942  62.619  1.00 87.81           C  
-ATOM   4017  NZ  LYS C 522      28.496   7.513  62.992  1.00 87.63           N  
-ATOM   4018  N   ASP C 523      24.756   4.827  56.496  1.00 89.53           N  
-ATOM   4019  CA  ASP C 523      24.863   4.120  55.222  1.00 90.51           C  
-ATOM   4020  C   ASP C 523      24.787   5.043  54.012  1.00 90.86           C  
-ATOM   4021  O   ASP C 523      24.272   4.654  52.961  1.00 90.92           O  
-ATOM   4022  CB  ASP C 523      23.762   3.062  55.113  1.00 91.91           C  
-ATOM   4023  CG  ASP C 523      23.748   2.111  56.291  1.00 93.97           C  
-ATOM   4024  OD1 ASP C 523      24.803   1.507  56.581  1.00 95.40           O  
-ATOM   4025  OD2 ASP C 523      22.681   1.966  56.926  1.00 95.63           O  
-ATOM   4026  N   VAL C 524      25.305   6.258  54.156  1.00 91.32           N  
-ATOM   4027  CA  VAL C 524      25.284   7.225  53.067  1.00 91.96           C  
-ATOM   4028  C   VAL C 524      26.695   7.584  52.607  1.00 92.33           C  
-ATOM   4029  O   VAL C 524      27.531   8.001  53.411  1.00 91.71           O  
-ATOM   4030  CB  VAL C 524      24.565   8.521  53.492  1.00 92.14           C  
-ATOM   4031  CG1 VAL C 524      24.397   9.439  52.289  1.00 91.81           C  
-ATOM   4032  CG2 VAL C 524      23.217   8.189  54.113  1.00 91.45           C  
-ATOM   4033  N   PRO C 525      26.976   7.426  51.302  1.00 93.01           N  
-ATOM   4034  CA  PRO C 525      28.292   7.738  50.735  1.00 93.75           C  
-ATOM   4035  C   PRO C 525      28.568   9.239  50.759  1.00 94.45           C  
-ATOM   4036  O   PRO C 525      27.637  10.044  50.808  1.00 94.86           O  
-ATOM   4037  CB  PRO C 525      28.188   7.194  49.315  1.00 93.39           C  
-ATOM   4038  CG  PRO C 525      26.751   7.436  48.984  1.00 93.41           C  
-ATOM   4039  CD  PRO C 525      26.054   6.968  50.247  1.00 93.16           C  
-ATOM   4040  N   ASN C 526      29.844   9.611  50.720  1.00 94.72           N  
-ATOM   4041  CA  ASN C 526      30.223  11.018  50.750  1.00 94.91           C  
-ATOM   4042  C   ASN C 526      30.770  11.472  49.398  1.00 95.17           C  
-ATOM   4043  O   ASN C 526      31.980  11.440  49.162  1.00 95.03           O  
-ATOM   4044  CB  ASN C 526      31.272  11.252  51.838  1.00 95.10           C  
-ATOM   4045  CG  ASN C 526      31.455  12.718  52.160  1.00 95.76           C  
-ATOM   4046  OD1 ASN C 526      31.751  13.527  51.282  1.00 97.59           O  
-ATOM   4047  ND2 ASN C 526      31.279  13.071  53.428  1.00 95.69           N  
-ATOM   4048  N   PRO C 527      29.879  11.910  48.492  1.00 95.61           N  
-ATOM   4049  CA  PRO C 527      30.279  12.371  47.159  1.00 95.82           C  
-ATOM   4050  C   PRO C 527      31.106  13.656  47.192  1.00 95.60           C  
-ATOM   4051  CB  PRO C 527      28.939  12.553  46.447  1.00 95.95           C  
-ATOM   4052  CG  PRO C 527      28.038  12.994  47.558  1.00 95.45           C  
-ATOM   4053  CD  PRO C 527      28.422  12.044  48.676  1.00 95.99           C  
-ATOM   4054  N   SER C 538      32.310  18.746  59.507  1.00 84.14           N  
-ATOM   4055  CA  SER C 538      32.145  17.921  58.274  1.00 84.35           C  
-ATOM   4056  C   SER C 538      30.865  18.297  57.525  1.00 84.12           C  
-ATOM   4057  O   SER C 538      29.984  18.956  58.079  1.00 84.17           O  
-ATOM   4058  CB  SER C 538      32.127  16.431  58.637  1.00 84.02           C  
-ATOM   4059  OG  SER C 538      31.132  16.143  59.604  1.00 84.33           O  
-ATOM   4060  N   PHE C 539      30.770  17.877  56.265  1.00 83.48           N  
-ATOM   4061  CA  PHE C 539      29.607  18.178  55.434  1.00 82.60           C  
-ATOM   4062  C   PHE C 539      29.335  17.093  54.396  1.00 82.60           C  
-ATOM   4063  O   PHE C 539      30.144  16.871  53.493  1.00 82.71           O  
-ATOM   4064  CB  PHE C 539      29.807  19.518  54.718  1.00 81.26           C  
-ATOM   4065  CG  PHE C 539      28.793  19.791  53.641  1.00 79.93           C  
-ATOM   4066  CD1 PHE C 539      27.446  19.936  53.954  1.00 79.13           C  
-ATOM   4067  CD2 PHE C 539      29.183  19.883  52.309  1.00 77.85           C  
-ATOM   4068  CE1 PHE C 539      26.502  20.168  52.954  1.00 77.73           C  
-ATOM   4069  CE2 PHE C 539      28.247  20.114  51.304  1.00 77.14           C  
-ATOM   4070  CZ  PHE C 539      26.905  20.257  51.627  1.00 75.61           C  
-ATOM   4071  N   ASN C 540      28.193  16.424  54.525  1.00 82.34           N  
-ATOM   4072  CA  ASN C 540      27.806  15.371  53.588  1.00 81.78           C  
-ATOM   4073  C   ASN C 540      26.507  15.807  52.906  1.00 81.03           C  
-ATOM   4074  O   ASN C 540      25.436  15.766  53.512  1.00 81.57           O  
-ATOM   4075  CB  ASN C 540      27.589  14.048  54.333  1.00 82.45           C  
-ATOM   4076  CG  ASN C 540      27.607  12.843  53.407  1.00 84.04           C  
-ATOM   4077  OD1 ASN C 540      26.901  12.808  52.397  1.00 83.71           O  
-ATOM   4078  ND2 ASN C 540      28.417  11.844  53.750  1.00 84.79           N  
-ATOM   4079  N   PRO C 541      26.589  16.225  51.632  1.00 79.76           N  
-ATOM   4080  CA  PRO C 541      25.437  16.681  50.847  1.00 78.56           C  
-ATOM   4081  C   PRO C 541      24.271  15.705  50.730  1.00 77.71           C  
-ATOM   4082  O   PRO C 541      23.111  16.098  50.854  1.00 78.02           O  
-ATOM   4083  CB  PRO C 541      26.056  17.005  49.488  1.00 77.94           C  
-ATOM   4084  CG  PRO C 541      27.186  16.035  49.403  1.00 79.40           C  
-ATOM   4085  CD  PRO C 541      27.789  16.141  50.782  1.00 79.35           C  
-ATOM   4086  N   LEU C 542      24.576  14.435  50.491  1.00 76.47           N  
-ATOM   4087  CA  LEU C 542      23.530  13.435  50.344  1.00 74.80           C  
-ATOM   4088  C   LEU C 542      22.804  13.143  51.654  1.00 73.50           C  
-ATOM   4089  O   LEU C 542      21.582  13.004  51.666  1.00 73.98           O  
-ATOM   4090  CB  LEU C 542      24.112  12.141  49.771  1.00 75.84           C  
-ATOM   4091  CG  LEU C 542      23.088  11.100  49.312  1.00 75.59           C  
-ATOM   4092  CD1 LEU C 542      22.206  11.696  48.226  1.00 73.57           C  
-ATOM   4093  CD2 LEU C 542      23.810   9.864  48.796  1.00 75.25           C  
-ATOM   4094  N   LYS C 543      23.548  13.049  52.753  1.00 72.22           N  
-ATOM   4095  CA  LYS C 543      22.942  12.778  54.058  1.00 71.24           C  
-ATOM   4096  C   LYS C 543      21.875  13.816  54.402  1.00 70.79           C  
-ATOM   4097  O   LYS C 543      20.799  13.475  54.902  1.00 71.13           O  
-ATOM   4098  CB  LYS C 543      24.003  12.766  55.164  1.00 71.21           C  
-ATOM   4099  CG  LYS C 543      24.937  11.570  55.135  1.00 73.95           C  
-ATOM   4100  CD  LYS C 543      25.809  11.535  56.379  1.00 74.85           C  
-ATOM   4101  CE  LYS C 543      26.766  10.354  56.361  1.00 76.87           C  
-ATOM   4102  NZ  LYS C 543      27.605  10.311  57.595  1.00 78.70           N  
-ATOM   4103  N   ILE C 544      22.183  15.081  54.138  1.00 69.18           N  
-ATOM   4104  CA  ILE C 544      21.258  16.173  54.408  1.00 67.63           C  
-ATOM   4105  C   ILE C 544      20.054  16.113  53.468  1.00 67.17           C  
-ATOM   4106  O   ILE C 544      18.918  16.313  53.893  1.00 66.30           O  
-ATOM   4107  CB  ILE C 544      21.963  17.541  54.254  1.00 65.25           C  
-ATOM   4108  CG1 ILE C 544      23.003  17.710  55.366  1.00 63.35           C  
-ATOM   4109  CG2 ILE C 544      20.945  18.665  54.292  1.00 64.01           C  
-ATOM   4110  CD1 ILE C 544      23.846  18.963  55.244  1.00 61.07           C  
-ATOM   4111  N   GLU C 545      20.306  15.820  52.196  1.00 66.66           N  
-ATOM   4112  CA  GLU C 545      19.238  15.743  51.213  1.00 66.73           C  
-ATOM   4113  C   GLU C 545      18.195  14.681  51.553  1.00 68.41           C  
-ATOM   4114  O   GLU C 545      16.997  14.962  51.536  1.00 69.04           O  
-ATOM   4115  CB  GLU C 545      19.817  15.465  49.827  1.00 64.47           C  
-ATOM   4116  CG  GLU C 545      18.759  15.273  48.761  1.00 64.36           C  
-ATOM   4117  CD  GLU C 545      19.346  15.071  47.382  1.00 67.15           C  
-ATOM   4118  OE1 GLU C 545      20.203  14.176  47.233  1.00 68.24           O  
-ATOM   4119  OE2 GLU C 545      18.949  15.801  46.446  1.00 69.69           O  
-ATOM   4120  N   VAL C 546      18.645  13.467  51.862  1.00 68.30           N  
-ATOM   4121  CA  VAL C 546      17.724  12.381  52.190  1.00 68.08           C  
-ATOM   4122  C   VAL C 546      16.999  12.621  53.510  1.00 67.74           C  
-ATOM   4123  O   VAL C 546      15.861  12.185  53.686  1.00 67.91           O  
-ATOM   4124  CB  VAL C 546      18.450  11.006  52.272  1.00 68.04           C  
-ATOM   4125  CG1 VAL C 546      19.112  10.683  50.941  1.00 64.19           C  
-ATOM   4126  CG2 VAL C 546      19.475  11.020  53.397  1.00 67.68           C  
-ATOM   4127  N   PHE C 547      17.661  13.311  54.436  1.00 67.51           N  
-ATOM   4128  CA  PHE C 547      17.072  13.606  55.739  1.00 66.98           C  
-ATOM   4129  C   PHE C 547      15.949  14.634  55.622  1.00 67.28           C  
-ATOM   4130  O   PHE C 547      14.924  14.528  56.300  1.00 67.27           O  
-ATOM   4131  CB  PHE C 547      18.137  14.136  56.698  1.00 66.81           C  
-ATOM   4132  CG  PHE C 547      17.595  14.546  58.041  1.00 64.81           C  
-ATOM   4133  CD1 PHE C 547      17.032  13.607  58.898  1.00 63.10           C  
-ATOM   4134  CD2 PHE C 547      17.657  15.872  58.456  1.00 63.93           C  
-ATOM   4135  CE1 PHE C 547      16.543  13.982  60.151  1.00 61.33           C  
-ATOM   4136  CE2 PHE C 547      17.169  16.254  59.708  1.00 61.55           C  
-ATOM   4137  CZ  PHE C 547      16.613  15.309  60.554  1.00 59.79           C  
-ATOM   4138  N   VAL C 548      16.153  15.628  54.763  1.00 66.41           N  
-ATOM   4139  CA  VAL C 548      15.167  16.682  54.552  1.00 66.16           C  
-ATOM   4140  C   VAL C 548      14.055  16.227  53.606  1.00 65.91           C  
-ATOM   4141  O   VAL C 548      12.871  16.329  53.929  1.00 65.02           O  
-ATOM   4142  CB  VAL C 548      15.836  17.960  53.981  1.00 65.38           C  
-ATOM   4143  CG1 VAL C 548      14.780  19.014  53.672  1.00 61.84           C  
-ATOM   4144  CG2 VAL C 548      16.844  18.504  54.988  1.00 60.01           C  
-ATOM   4145  N   GLN C 549      14.450  15.727  52.440  1.00 65.93           N  
-ATOM   4146  CA  GLN C 549      13.508  15.243  51.439  1.00 65.43           C  
-ATOM   4147  C   GLN C 549      12.531  14.225  52.008  1.00 66.32           C  
-ATOM   4148  O   GLN C 549      11.447  14.026  51.461  1.00 68.42           O  
-ATOM   4149  CB  GLN C 549      14.274  14.617  50.279  1.00 63.68           C  
-ATOM   4150  CG  GLN C 549      14.751  15.622  49.259  1.00 63.55           C  
-ATOM   4151  CD  GLN C 549      13.761  15.787  48.132  1.00 62.44           C  
-ATOM   4152  OE1 GLN C 549      12.575  15.521  48.302  1.00 64.97           O  
-ATOM   4153  NE2 GLN C 549      14.239  16.233  46.973  1.00 63.99           N  
-ATOM   4154  N   THR C 550      12.917  13.582  53.104  1.00 65.88           N  
-ATOM   4155  CA  THR C 550      12.068  12.580  53.736  1.00 66.08           C  
-ATOM   4156  C   THR C 550      11.313  13.131  54.939  1.00 66.07           C  
-ATOM   4157  O   THR C 550      10.140  12.817  55.140  1.00 66.45           O  
-ATOM   4158  CB  THR C 550      12.896  11.360  54.198  1.00 65.77           C  
-ATOM   4159  OG1 THR C 550      13.458  10.705  53.053  1.00 66.38           O  
-ATOM   4160  CG2 THR C 550      12.024  10.377  54.962  1.00 63.37           C  
-ATOM   4161  N   LEU C 551      11.985  13.945  55.744  1.00 65.21           N  
-ATOM   4162  CA  LEU C 551      11.346  14.506  56.920  1.00 64.76           C  
-ATOM   4163  C   LEU C 551      10.257  15.490  56.525  1.00 64.82           C  
-ATOM   4164  O   LEU C 551       9.239  15.590  57.204  1.00 65.17           O  
-ATOM   4165  CB  LEU C 551      12.377  15.194  57.818  1.00 64.20           C  
-ATOM   4166  CG  LEU C 551      11.865  15.698  59.170  1.00 63.65           C  
-ATOM   4167  CD1 LEU C 551      11.127  14.593  59.909  1.00 65.41           C  
-ATOM   4168  CD2 LEU C 551      13.037  16.186  59.993  1.00 65.49           C  
-ATOM   4169  N   LEU C 552      10.464  16.207  55.424  1.00 64.27           N  
-ATOM   4170  CA  LEU C 552       9.470  17.173  54.965  1.00 64.44           C  
-ATOM   4171  C   LEU C 552       8.282  16.497  54.290  1.00 65.33           C  
-ATOM   4172  O   LEU C 552       7.132  16.859  54.534  1.00 65.70           O  
-ATOM   4173  CB  LEU C 552      10.089  18.181  53.989  1.00 60.02           C  
-ATOM   4174  CG  LEU C 552      11.019  19.262  54.544  1.00 56.89           C  
-ATOM   4175  CD1 LEU C 552      11.407  20.200  53.417  1.00 55.88           C  
-ATOM   4176  CD2 LEU C 552      10.332  20.032  55.659  1.00 56.14           C  
-ATOM   4177  N   HIS C 553       8.564  15.516  53.441  1.00 66.48           N  
-ATOM   4178  CA  HIS C 553       7.510  14.812  52.724  1.00 67.36           C  
-ATOM   4179  C   HIS C 553       6.522  14.136  53.663  1.00 67.54           C  
-ATOM   4180  O   HIS C 553       5.316  14.187  53.435  1.00 68.03           O  
-ATOM   4181  CB  HIS C 553       8.122  13.780  51.773  1.00 68.03           C  
-ATOM   4182  CG  HIS C 553       7.110  12.988  51.002  1.00 69.38           C  
-ATOM   4183  ND1 HIS C 553       6.412  11.934  51.551  1.00 68.80           N  
-ATOM   4184  CD2 HIS C 553       6.675  13.103  49.724  1.00 67.66           C  
-ATOM   4185  CE1 HIS C 553       5.592  11.432  50.644  1.00 68.93           C  
-ATOM   4186  NE2 HIS C 553       5.732  12.123  49.527  1.00 68.28           N  
-ATOM   4187  N   LEU C 554       7.031  13.516  54.723  1.00 67.94           N  
-ATOM   4188  CA  LEU C 554       6.176  12.826  55.682  1.00 69.17           C  
-ATOM   4189  C   LEU C 554       5.503  13.790  56.656  1.00 69.41           C  
-ATOM   4190  O   LEU C 554       5.024  13.384  57.717  1.00 70.26           O  
-ATOM   4191  CB  LEU C 554       6.986  11.787  56.464  1.00 69.34           C  
-ATOM   4192  CG  LEU C 554       7.800  10.799  55.622  1.00 70.90           C  
-ATOM   4193  CD1 LEU C 554       8.414   9.751  56.537  1.00 70.89           C  
-ATOM   4194  CD2 LEU C 554       6.917  10.144  54.572  1.00 68.37           C  
-ATOM   4195  N   ALA C 555       5.467  15.067  56.289  1.00 69.00           N  
-ATOM   4196  CA  ALA C 555       4.849  16.086  57.129  1.00 67.79           C  
-ATOM   4197  C   ALA C 555       4.220  17.163  56.254  1.00 66.92           C  
-ATOM   4198  O   ALA C 555       3.849  18.234  56.736  1.00 66.89           O  
-ATOM   4199  CB  ALA C 555       5.889  16.700  58.056  1.00 68.07           C  
-ATOM   4200  N   ALA C 556       4.099  16.860  54.965  1.00 66.26           N  
-ATOM   4201  CA  ALA C 556       3.528  17.779  53.988  1.00 66.14           C  
-ATOM   4202  C   ALA C 556       2.055  18.080  54.252  1.00 66.76           C  
-ATOM   4203  O   ALA C 556       1.381  18.685  53.413  1.00 66.67           O  
-ATOM   4204  CB  ALA C 556       3.696  17.202  52.587  1.00 64.06           C  
-ATOM   4205  N   LYS C 557       1.559  17.661  55.414  1.00 66.84           N  
-ATOM   4206  CA  LYS C 557       0.162  17.884  55.765  1.00 66.98           C  
-ATOM   4207  C   LYS C 557      -0.111  19.336  56.147  1.00 65.79           C  
-ATOM   4208  O   LYS C 557      -0.761  20.063  55.398  1.00 66.22           O  
-ATOM   4209  CB  LYS C 557      -0.258  16.954  56.908  1.00 69.03           C  
-ATOM   4210  CG  LYS C 557      -1.754  16.986  57.198  1.00 73.57           C  
-ATOM   4211  CD  LYS C 557      -2.176  15.896  58.171  1.00 76.62           C  
-ATOM   4212  CE  LYS C 557      -3.688  15.906  58.368  1.00 78.64           C  
-ATOM   4213  NZ  LYS C 557      -4.154  14.826  59.282  1.00 79.63           N  
-ATOM   4214  N   SER C 558       0.387  19.757  57.307  1.00 63.96           N  
-ATOM   4215  CA  SER C 558       0.181  21.127  57.767  1.00 62.12           C  
-ATOM   4216  C   SER C 558       1.471  21.770  58.271  1.00 60.90           C  
-ATOM   4217  O   SER C 558       2.513  21.115  58.361  1.00 59.51           O  
-ATOM   4218  CB  SER C 558      -0.861  21.155  58.886  1.00 61.08           C  
-ATOM   4219  OG  SER C 558      -0.354  20.546  60.061  1.00 61.84           O  
-ATOM   4220  N   PHE C 559       1.390  23.056  58.601  1.00 58.89           N  
-ATOM   4221  CA  PHE C 559       2.545  23.787  59.104  1.00 57.12           C  
-ATOM   4222  C   PHE C 559       2.991  23.204  60.447  1.00 59.10           C  
-ATOM   4223  O   PHE C 559       4.192  23.037  60.689  1.00 58.39           O  
-ATOM   4224  CB  PHE C 559       2.215  25.282  59.256  1.00 50.02           C  
-ATOM   4225  CG  PHE C 559       2.142  26.041  57.947  1.00 40.83           C  
-ATOM   4226  CD1 PHE C 559       2.393  25.405  56.729  1.00 38.47           C  
-ATOM   4227  CD2 PHE C 559       1.822  27.400  57.938  1.00 35.98           C  
-ATOM   4228  CE1 PHE C 559       2.330  26.109  55.518  1.00 35.19           C  
-ATOM   4229  CE2 PHE C 559       1.754  28.117  56.744  1.00 34.90           C  
-ATOM   4230  CZ  PHE C 559       2.007  27.470  55.525  1.00 37.62           C  
-ATOM   4231  N   SER C 560       2.029  22.890  61.315  1.00 58.99           N  
-ATOM   4232  CA  SER C 560       2.353  22.314  62.618  1.00 59.63           C  
-ATOM   4233  C   SER C 560       3.017  20.940  62.471  1.00 59.94           C  
-ATOM   4234  O   SER C 560       3.806  20.529  63.326  1.00 59.26           O  
-ATOM   4235  CB  SER C 560       1.095  22.194  63.486  1.00 58.81           C  
-ATOM   4236  OG  SER C 560       0.772  23.433  64.095  1.00 59.08           O  
-ATOM   4237  N   HIS C 561       2.692  20.237  61.388  1.00 60.22           N  
-ATOM   4238  CA  HIS C 561       3.267  18.921  61.122  1.00 61.64           C  
-ATOM   4239  C   HIS C 561       4.752  19.057  60.808  1.00 61.17           C  
-ATOM   4240  O   HIS C 561       5.556  18.181  61.140  1.00 61.70           O  
-ATOM   4241  CB  HIS C 561       2.552  18.251  59.944  1.00 65.03           C  
-ATOM   4242  CG  HIS C 561       1.346  17.458  60.342  1.00 69.18           C  
-ATOM   4243  ND1 HIS C 561       0.352  17.967  61.150  1.00 71.00           N  
-ATOM   4244  CD2 HIS C 561       0.971  16.193  60.037  1.00 70.74           C  
-ATOM   4245  CE1 HIS C 561      -0.582  17.050  61.326  1.00 71.36           C  
-ATOM   4246  NE2 HIS C 561      -0.231  15.964  60.661  1.00 70.45           N  
-ATOM   4247  N   SER C 562       5.111  20.163  60.163  1.00 59.53           N  
-ATOM   4248  CA  SER C 562       6.496  20.420  59.812  1.00 57.67           C  
-ATOM   4249  C   SER C 562       7.247  20.971  61.021  1.00 57.44           C  
-ATOM   4250  O   SER C 562       8.353  20.524  61.335  1.00 56.53           O  
-ATOM   4251  CB  SER C 562       6.553  21.402  58.648  1.00 56.50           C  
-ATOM   4252  OG  SER C 562       5.835  20.891  57.538  1.00 54.80           O  
-ATOM   4253  N   PHE C 563       6.640  21.934  61.706  1.00 56.29           N  
-ATOM   4254  CA  PHE C 563       7.259  22.533  62.880  1.00 57.37           C  
-ATOM   4255  C   PHE C 563       7.533  21.482  63.955  1.00 58.56           C  
-ATOM   4256  O   PHE C 563       8.564  21.529  64.630  1.00 59.28           O  
-ATOM   4257  CB  PHE C 563       6.356  23.629  63.456  1.00 55.51           C  
-ATOM   4258  CG  PHE C 563       6.133  24.797  62.526  1.00 57.24           C  
-ATOM   4259  CD1 PHE C 563       5.113  25.712  62.776  1.00 56.36           C  
-ATOM   4260  CD2 PHE C 563       6.942  24.991  61.411  1.00 53.15           C  
-ATOM   4261  CE1 PHE C 563       4.904  26.800  61.931  1.00 55.96           C  
-ATOM   4262  CE2 PHE C 563       6.739  26.076  60.563  1.00 53.19           C  
-ATOM   4263  CZ  PHE C 563       5.720  26.982  60.823  1.00 53.79           C  
-ATOM   4264  N   SER C 564       6.610  20.536  64.116  1.00 59.22           N  
-ATOM   4265  CA  SER C 564       6.765  19.487  65.123  1.00 59.53           C  
-ATOM   4266  C   SER C 564       7.837  18.479  64.715  1.00 59.17           C  
-ATOM   4267  O   SER C 564       8.389  17.774  65.560  1.00 59.93           O  
-ATOM   4268  CB  SER C 564       5.427  18.771  65.369  1.00 59.73           C  
-ATOM   4269  OG  SER C 564       4.928  18.167  64.185  1.00 62.10           O  
-ATOM   4270  N   ALA C 565       8.127  18.418  63.419  1.00 59.21           N  
-ATOM   4271  CA  ALA C 565       9.148  17.515  62.900  1.00 60.83           C  
-ATOM   4272  C   ALA C 565      10.531  18.133  63.121  1.00 62.87           C  
-ATOM   4273  O   ALA C 565      11.464  17.453  63.558  1.00 63.67           O  
-ATOM   4274  CB  ALA C 565       8.922  17.261  61.409  1.00 58.01           C  
-ATOM   4275  N   LEU C 566      10.656  19.424  62.820  1.00 63.49           N  
-ATOM   4276  CA  LEU C 566      11.922  20.125  62.990  1.00 64.61           C  
-ATOM   4277  C   LEU C 566      12.314  20.148  64.460  1.00 65.79           C  
-ATOM   4278  O   LEU C 566      13.483  19.983  64.802  1.00 65.87           O  
-ATOM   4279  CB  LEU C 566      11.814  21.562  62.482  1.00 63.88           C  
-ATOM   4280  CG  LEU C 566      11.323  21.770  61.052  1.00 63.06           C  
-ATOM   4281  CD1 LEU C 566      11.254  23.259  60.771  1.00 65.18           C  
-ATOM   4282  CD2 LEU C 566      12.246  21.078  60.072  1.00 60.52           C  
-ATOM   4283  N   ALA C 567      11.330  20.356  65.328  1.00 67.21           N  
-ATOM   4284  CA  ALA C 567      11.587  20.408  66.760  1.00 68.85           C  
-ATOM   4285  C   ALA C 567      11.955  19.033  67.304  1.00 69.85           C  
-ATOM   4286  O   ALA C 567      12.781  18.918  68.212  1.00 69.86           O  
-ATOM   4287  CB  ALA C 567      10.365  20.952  67.489  1.00 69.01           C  
-ATOM   4288  N   LYS C 568      11.347  17.992  66.743  1.00 70.54           N  
-ATOM   4289  CA  LYS C 568      11.615  16.629  67.187  1.00 71.61           C  
-ATOM   4290  C   LYS C 568      13.053  16.237  66.858  1.00 71.87           C  
-ATOM   4291  O   LYS C 568      13.841  15.929  67.757  1.00 70.83           O  
-ATOM   4292  CB  LYS C 568      10.640  15.651  66.522  1.00 72.81           C  
-ATOM   4293  CG  LYS C 568      10.658  14.246  67.118  1.00 75.46           C  
-ATOM   4294  CD  LYS C 568       9.690  13.308  66.396  1.00 78.02           C  
-ATOM   4295  CE  LYS C 568       8.235  13.756  66.540  1.00 79.12           C  
-ATOM   4296  NZ  LYS C 568       7.768  13.764  67.958  1.00 79.79           N  
-ATOM   4297  N   PHE C 569      13.391  16.253  65.571  1.00 71.71           N  
-ATOM   4298  CA  PHE C 569      14.738  15.906  65.130  1.00 72.32           C  
-ATOM   4299  C   PHE C 569      15.610  17.154  64.999  1.00 71.98           C  
-ATOM   4300  O   PHE C 569      16.342  17.321  64.020  1.00 71.37           O  
-ATOM   4301  CB  PHE C 569      14.682  15.157  63.797  1.00 73.62           C  
-ATOM   4302  CG  PHE C 569      13.789  13.951  63.826  1.00 77.48           C  
-ATOM   4303  CD1 PHE C 569      12.494  14.017  63.326  1.00 78.63           C  
-ATOM   4304  CD2 PHE C 569      14.225  12.760  64.397  1.00 77.24           C  
-ATOM   4305  CE1 PHE C 569      11.644  12.916  63.396  1.00 79.39           C  
-ATOM   4306  CE2 PHE C 569      13.382  11.654  64.471  1.00 77.49           C  
-ATOM   4307  CZ  PHE C 569      12.090  11.733  63.970  1.00 78.04           C  
-ATOM   4308  N   HIS C 570      15.519  18.023  66.002  1.00 71.55           N  
-ATOM   4309  CA  HIS C 570      16.282  19.262  66.038  1.00 71.11           C  
-ATOM   4310  C   HIS C 570      17.764  18.977  66.251  1.00 70.67           C  
-ATOM   4311  O   HIS C 570      18.621  19.664  65.698  1.00 70.40           O  
-ATOM   4312  CB  HIS C 570      15.748  20.162  67.156  1.00 71.78           C  
-ATOM   4313  CG  HIS C 570      16.547  21.409  67.368  1.00 72.78           C  
-ATOM   4314  ND1 HIS C 570      17.681  21.442  68.151  1.00 73.19           N  
-ATOM   4315  CD2 HIS C 570      16.377  22.667  66.897  1.00 73.07           C  
-ATOM   4316  CE1 HIS C 570      18.174  22.667  68.155  1.00 74.30           C  
-ATOM   4317  NE2 HIS C 570      17.402  23.430  67.401  1.00 74.21           N  
-ATOM   4318  N   GLU C 571      18.059  17.958  67.052  1.00 70.13           N  
-ATOM   4319  CA  GLU C 571      19.440  17.584  67.322  1.00 69.16           C  
-ATOM   4320  C   GLU C 571      20.101  17.114  66.037  1.00 67.51           C  
-ATOM   4321  O   GLU C 571      21.282  17.368  65.806  1.00 67.70           O  
-ATOM   4322  CB  GLU C 571      19.504  16.464  68.358  1.00 71.46           C  
-ATOM   4323  CG  GLU C 571      20.926  16.104  68.757  1.00 77.18           C  
-ATOM   4324  CD  GLU C 571      20.995  14.866  69.623  1.00 81.53           C  
-ATOM   4325  OE1 GLU C 571      20.300  14.823  70.661  1.00 83.92           O  
-ATOM   4326  OE2 GLU C 571      21.749  13.936  69.266  1.00 84.18           O  
-ATOM   4327  N   VAL C 572      19.331  16.424  65.202  1.00 65.58           N  
-ATOM   4328  CA  VAL C 572      19.847  15.924  63.939  1.00 64.11           C  
-ATOM   4329  C   VAL C 572      20.138  17.077  62.990  1.00 63.07           C  
-ATOM   4330  O   VAL C 572      21.164  17.083  62.315  1.00 63.17           O  
-ATOM   4331  CB  VAL C 572      18.850  14.968  63.258  1.00 63.75           C  
-ATOM   4332  CG1 VAL C 572      19.445  14.436  61.965  1.00 63.92           C  
-ATOM   4333  CG2 VAL C 572      18.501  13.823  64.195  1.00 65.70           C  
-ATOM   4334  N   PHE C 573      19.233  18.052  62.933  1.00 61.96           N  
-ATOM   4335  CA  PHE C 573      19.431  19.200  62.056  1.00 61.13           C  
-ATOM   4336  C   PHE C 573      20.710  19.950  62.408  1.00 61.72           C  
-ATOM   4337  O   PHE C 573      21.552  20.189  61.545  1.00 61.99           O  
-ATOM   4338  CB  PHE C 573      18.241  20.166  62.131  1.00 57.48           C  
-ATOM   4339  CG  PHE C 573      17.140  19.850  61.159  1.00 51.00           C  
-ATOM   4340  CD1 PHE C 573      16.010  19.147  61.565  1.00 50.24           C  
-ATOM   4341  CD2 PHE C 573      17.248  20.234  59.828  1.00 46.42           C  
-ATOM   4342  CE1 PHE C 573      15.004  18.831  60.661  1.00 47.01           C  
-ATOM   4343  CE2 PHE C 573      16.251  19.924  58.913  1.00 48.02           C  
-ATOM   4344  CZ  PHE C 573      15.123  19.219  59.331  1.00 46.61           C  
-ATOM   4345  N   LYS C 574      20.849  20.321  63.678  1.00 62.66           N  
-ATOM   4346  CA  LYS C 574      22.026  21.050  64.138  1.00 64.79           C  
-ATOM   4347  C   LYS C 574      23.312  20.350  63.712  1.00 66.01           C  
-ATOM   4348  O   LYS C 574      24.253  20.991  63.241  1.00 66.52           O  
-ATOM   4349  CB  LYS C 574      21.998  21.201  65.665  1.00 64.43           C  
-ATOM   4350  CG  LYS C 574      20.860  22.063  66.183  1.00 64.99           C  
-ATOM   4351  CD  LYS C 574      20.924  23.476  65.614  1.00 65.78           C  
-ATOM   4352  CE  LYS C 574      22.110  24.257  66.160  1.00 65.70           C  
-ATOM   4353  NZ  LYS C 574      21.981  24.496  67.623  1.00 67.13           N  
-ATOM   4354  N   THR C 575      23.343  19.030  63.873  1.00 66.24           N  
-ATOM   4355  CA  THR C 575      24.514  18.247  63.505  1.00 66.58           C  
-ATOM   4356  C   THR C 575      24.771  18.307  62.000  1.00 65.77           C  
-ATOM   4357  O   THR C 575      25.861  18.677  61.564  1.00 65.94           O  
-ATOM   4358  CB  THR C 575      24.352  16.770  63.924  1.00 67.73           C  
-ATOM   4359  OG1 THR C 575      24.043  16.700  65.323  1.00 70.60           O  
-ATOM   4360  CG2 THR C 575      25.642  16.002  63.666  1.00 69.24           C  
-ATOM   4361  N   LEU C 576      23.765  17.950  61.210  1.00 64.86           N  
-ATOM   4362  CA  LEU C 576      23.896  17.956  59.756  1.00 64.66           C  
-ATOM   4363  C   LEU C 576      24.126  19.337  59.153  1.00 63.84           C  
-ATOM   4364  O   LEU C 576      24.713  19.457  58.075  1.00 63.89           O  
-ATOM   4365  CB  LEU C 576      22.652  17.346  59.106  1.00 66.29           C  
-ATOM   4366  CG  LEU C 576      22.549  15.827  58.974  1.00 68.31           C  
-ATOM   4367  CD1 LEU C 576      22.613  15.183  60.345  1.00 68.93           C  
-ATOM   4368  CD2 LEU C 576      21.246  15.472  58.268  1.00 67.62           C  
-ATOM   4369  N   ALA C 577      23.656  20.376  59.837  1.00 62.56           N  
-ATOM   4370  CA  ALA C 577      23.802  21.736  59.332  1.00 61.17           C  
-ATOM   4371  C   ALA C 577      24.734  22.616  60.159  1.00 60.84           C  
-ATOM   4372  O   ALA C 577      24.557  23.835  60.207  1.00 60.17           O  
-ATOM   4373  CB  ALA C 577      22.430  22.392  59.227  1.00 60.43           C  
-ATOM   4374  N   GLU C 578      25.727  22.006  60.802  1.00 60.27           N  
-ATOM   4375  CA  GLU C 578      26.674  22.769  61.611  1.00 59.42           C  
-ATOM   4376  C   GLU C 578      27.497  23.675  60.707  1.00 57.22           C  
-ATOM   4377  O   GLU C 578      27.881  24.777  61.090  1.00 56.27           O  
-ATOM   4378  CB  GLU C 578      27.615  21.834  62.376  1.00 63.18           C  
-ATOM   4379  CG  GLU C 578      28.509  22.558  63.378  1.00 68.23           C  
-ATOM   4380  CD  GLU C 578      29.468  21.630  64.103  1.00 73.19           C  
-ATOM   4381  OE1 GLU C 578      30.069  22.073  65.106  1.00 75.51           O  
-ATOM   4382  OE2 GLU C 578      29.628  20.467  63.670  1.00 75.79           O  
-ATOM   4383  N   SER C 579      27.755  23.191  59.499  1.00 56.14           N  
-ATOM   4384  CA  SER C 579      28.529  23.917  58.503  1.00 56.02           C  
-ATOM   4385  C   SER C 579      27.694  25.001  57.828  1.00 56.82           C  
-ATOM   4386  O   SER C 579      26.467  25.006  57.939  1.00 56.16           O  
-ATOM   4387  CB  SER C 579      29.032  22.928  57.451  1.00 53.75           C  
-ATOM   4388  OG  SER C 579      29.446  23.588  56.271  1.00 54.43           O  
-ATOM   4389  N   ASP C 580      28.355  25.928  57.139  1.00 56.79           N  
-ATOM   4390  CA  ASP C 580      27.629  26.969  56.428  1.00 57.06           C  
-ATOM   4391  C   ASP C 580      27.096  26.350  55.147  1.00 56.50           C  
-ATOM   4392  O   ASP C 580      26.002  26.678  54.696  1.00 56.40           O  
-ATOM   4393  CB  ASP C 580      28.531  28.160  56.091  1.00 58.32           C  
-ATOM   4394  CG  ASP C 580      28.781  29.062  57.288  1.00 59.70           C  
-ATOM   4395  OD1 ASP C 580      27.855  29.244  58.108  1.00 59.61           O  
-ATOM   4396  OD2 ASP C 580      29.900  29.604  57.404  1.00 64.10           O  
-ATOM   4397  N   GLU C 581      27.878  25.453  54.562  1.00 56.20           N  
-ATOM   4398  CA  GLU C 581      27.459  24.776  53.346  1.00 56.93           C  
-ATOM   4399  C   GLU C 581      26.301  23.861  53.724  1.00 55.26           C  
-ATOM   4400  O   GLU C 581      25.455  23.535  52.894  1.00 53.55           O  
-ATOM   4401  CB  GLU C 581      28.604  23.938  52.773  1.00 61.28           C  
-ATOM   4402  CG  GLU C 581      29.849  24.731  52.413  1.00 68.98           C  
-ATOM   4403  CD  GLU C 581      30.970  23.840  51.899  1.00 76.52           C  
-ATOM   4404  OE1 GLU C 581      31.454  22.981  52.672  1.00 78.50           O  
-ATOM   4405  OE2 GLU C 581      31.363  23.996  50.720  1.00 78.56           O  
-ATOM   4406  N   GLY C 582      26.288  23.443  54.987  1.00 55.21           N  
-ATOM   4407  CA  GLY C 582      25.236  22.576  55.481  1.00 55.32           C  
-ATOM   4408  C   GLY C 582      23.918  23.325  55.544  1.00 55.54           C  
-ATOM   4409  O   GLY C 582      22.886  22.822  55.095  1.00 56.11           O  
-ATOM   4410  N   LYS C 583      23.955  24.533  56.098  1.00 54.07           N  
-ATOM   4411  CA  LYS C 583      22.762  25.354  56.209  1.00 53.11           C  
-ATOM   4412  C   LYS C 583      22.269  25.709  54.813  1.00 53.11           C  
-ATOM   4413  O   LYS C 583      21.080  25.599  54.521  1.00 51.43           O  
-ATOM   4414  CB  LYS C 583      23.066  26.632  56.993  1.00 51.86           C  
-ATOM   4415  CG  LYS C 583      23.663  26.395  58.365  1.00 50.79           C  
-ATOM   4416  CD  LYS C 583      23.978  27.716  59.042  1.00 53.70           C  
-ATOM   4417  CE  LYS C 583      25.015  27.559  60.144  1.00 55.02           C  
-ATOM   4418  NZ  LYS C 583      24.541  26.747  61.295  1.00 59.21           N  
-ATOM   4419  N   LEU C 584      23.189  26.125  53.947  1.00 52.57           N  
-ATOM   4420  CA  LEU C 584      22.825  26.497  52.586  1.00 53.04           C  
-ATOM   4421  C   LEU C 584      22.218  25.346  51.802  1.00 54.00           C  
-ATOM   4422  O   LEU C 584      21.444  25.566  50.867  1.00 54.38           O  
-ATOM   4423  CB  LEU C 584      24.039  27.025  51.823  1.00 52.27           C  
-ATOM   4424  CG  LEU C 584      24.571  28.402  52.223  1.00 55.41           C  
-ATOM   4425  CD1 LEU C 584      25.707  28.786  51.278  1.00 54.96           C  
-ATOM   4426  CD2 LEU C 584      23.455  29.442  52.161  1.00 54.67           C  
-ATOM   4427  N   HIS C 585      22.574  24.119  52.169  1.00 54.47           N  
-ATOM   4428  CA  HIS C 585      22.045  22.953  51.471  1.00 54.45           C  
-ATOM   4429  C   HIS C 585      20.656  22.614  52.001  1.00 54.08           C  
-ATOM   4430  O   HIS C 585      19.770  22.215  51.243  1.00 54.09           O  
-ATOM   4431  CB  HIS C 585      22.983  21.754  51.639  1.00 52.82           C  
-ATOM   4432  CG  HIS C 585      22.726  20.656  50.656  1.00 49.35           C  
-ATOM   4433  ND1 HIS C 585      22.741  20.863  49.294  1.00 47.89           N  
-ATOM   4434  CD2 HIS C 585      22.420  19.349  50.836  1.00 51.49           C  
-ATOM   4435  CE1 HIS C 585      22.454  19.731  48.676  1.00 50.16           C  
-ATOM   4436  NE2 HIS C 585      22.254  18.797  49.589  1.00 49.93           N  
-ATOM   4437  N   VAL C 586      20.478  22.772  53.310  1.00 54.70           N  
-ATOM   4438  CA  VAL C 586      19.193  22.517  53.949  1.00 54.58           C  
-ATOM   4439  C   VAL C 586      18.147  23.406  53.280  1.00 54.97           C  
-ATOM   4440  O   VAL C 586      17.018  22.984  53.046  1.00 57.86           O  
-ATOM   4441  CB  VAL C 586      19.245  22.848  55.460  1.00 54.58           C  
-ATOM   4442  CG1 VAL C 586      17.849  22.766  56.071  1.00 54.19           C  
-ATOM   4443  CG2 VAL C 586      20.177  21.881  56.168  1.00 54.92           C  
-ATOM   4444  N   LEU C 587      18.538  24.636  52.965  1.00 54.47           N  
-ATOM   4445  CA  LEU C 587      17.645  25.587  52.317  1.00 53.41           C  
-ATOM   4446  C   LEU C 587      17.386  25.202  50.870  1.00 54.62           C  
-ATOM   4447  O   LEU C 587      16.259  25.314  50.381  1.00 54.11           O  
-ATOM   4448  CB  LEU C 587      18.252  26.990  52.368  1.00 45.85           C  
-ATOM   4449  CG  LEU C 587      18.364  27.576  53.775  1.00 46.90           C  
-ATOM   4450  CD1 LEU C 587      19.222  28.833  53.753  1.00 40.25           C  
-ATOM   4451  CD2 LEU C 587      16.962  27.873  54.309  1.00 42.35           C  
-ATOM   4452  N   ARG C 588      18.438  24.752  50.190  1.00 55.21           N  
-ATOM   4453  CA  ARG C 588      18.345  24.361  48.790  1.00 55.09           C  
-ATOM   4454  C   ARG C 588      17.474  23.130  48.585  1.00 55.71           C  
-ATOM   4455  O   ARG C 588      16.774  23.018  47.578  1.00 54.86           O  
-ATOM   4456  CB  ARG C 588      19.743  24.110  48.220  1.00 55.50           C  
-ATOM   4457  CG  ARG C 588      19.753  23.608  46.783  1.00 58.12           C  
-ATOM   4458  CD  ARG C 588      21.161  23.655  46.205  1.00 63.06           C  
-ATOM   4459  NE  ARG C 588      22.152  23.205  47.179  1.00 66.65           N  
-ATOM   4460  CZ  ARG C 588      23.174  23.943  47.601  1.00 66.90           C  
-ATOM   4461  NH1 ARG C 588      23.351  25.172  47.132  1.00 68.44           N  
-ATOM   4462  NH2 ARG C 588      24.010  23.463  48.511  1.00 66.78           N  
-ATOM   4463  N   VAL C 589      17.528  22.201  49.533  1.00 56.26           N  
-ATOM   4464  CA  VAL C 589      16.721  20.990  49.440  1.00 58.85           C  
-ATOM   4465  C   VAL C 589      15.277  21.362  49.778  1.00 58.89           C  
-ATOM   4466  O   VAL C 589      14.353  21.094  49.009  1.00 58.31           O  
-ATOM   4467  CB  VAL C 589      17.224  19.900  50.425  1.00 59.14           C  
-ATOM   4468  CG1 VAL C 589      16.322  18.672  50.361  1.00 62.90           C  
-ATOM   4469  CG2 VAL C 589      18.655  19.511  50.078  1.00 61.97           C  
-ATOM   4470  N   MET C 590      15.099  21.996  50.930  1.00 59.39           N  
-ATOM   4471  CA  MET C 590      13.780  22.421  51.376  1.00 59.90           C  
-ATOM   4472  C   MET C 590      13.037  23.162  50.258  1.00 58.83           C  
-ATOM   4473  O   MET C 590      11.828  23.012  50.114  1.00 59.81           O  
-ATOM   4474  CB  MET C 590      13.931  23.293  52.627  1.00 59.46           C  
-ATOM   4475  CG  MET C 590      12.649  23.872  53.180  1.00 62.43           C  
-ATOM   4476  SD  MET C 590      12.301  25.457  52.433  1.00 63.49           S  
-ATOM   4477  CE  MET C 590      13.489  26.472  53.300  1.00 62.63           C  
-ATOM   4478  N   PHE C 591      13.767  23.930  49.452  1.00 58.71           N  
-ATOM   4479  CA  PHE C 591      13.172  24.680  48.343  1.00 58.60           C  
-ATOM   4480  C   PHE C 591      12.720  23.764  47.207  1.00 59.55           C  
-ATOM   4481  O   PHE C 591      11.646  23.954  46.635  1.00 59.56           O  
-ATOM   4482  CB  PHE C 591      14.171  25.696  47.787  1.00 56.84           C  
-ATOM   4483  CG  PHE C 591      13.644  26.487  46.624  1.00 56.73           C  
-ATOM   4484  CD1 PHE C 591      12.627  27.418  46.804  1.00 56.77           C  
-ATOM   4485  CD2 PHE C 591      14.150  26.290  45.344  1.00 56.48           C  
-ATOM   4486  CE1 PHE C 591      12.122  28.142  45.723  1.00 55.16           C  
-ATOM   4487  CE2 PHE C 591      13.650  27.009  44.257  1.00 54.20           C  
-ATOM   4488  CZ  PHE C 591      12.635  27.936  44.449  1.00 55.79           C  
-ATOM   4489  N   GLU C 592      13.552  22.782  46.872  1.00 60.00           N  
-ATOM   4490  CA  GLU C 592      13.231  21.838  45.807  1.00 59.01           C  
-ATOM   4491  C   GLU C 592      12.069  20.935  46.218  1.00 57.47           C  
-ATOM   4492  O   GLU C 592      11.505  20.220  45.394  1.00 58.86           O  
-ATOM   4493  CB  GLU C 592      14.462  20.993  45.467  1.00 61.28           C  
-ATOM   4494  CG  GLU C 592      15.628  21.807  44.911  1.00 65.56           C  
-ATOM   4495  CD  GLU C 592      16.861  20.967  44.625  1.00 69.91           C  
-ATOM   4496  OE1 GLU C 592      17.341  20.280  45.553  1.00 68.86           O  
-ATOM   4497  OE2 GLU C 592      17.352  20.999  43.475  1.00 71.97           O  
-ATOM   4498  N   VAL C 593      11.718  20.976  47.498  1.00 55.99           N  
-ATOM   4499  CA  VAL C 593      10.620  20.176  48.028  1.00 54.66           C  
-ATOM   4500  C   VAL C 593       9.325  20.985  48.109  1.00 55.22           C  
-ATOM   4501  O   VAL C 593       8.232  20.438  47.954  1.00 56.78           O  
-ATOM   4502  CB  VAL C 593      10.956  19.653  49.441  1.00 53.72           C  
-ATOM   4503  CG1 VAL C 593       9.730  19.007  50.079  1.00 48.57           C  
-ATOM   4504  CG2 VAL C 593      12.092  18.654  49.359  1.00 53.69           C  
-ATOM   4505  N   TRP C 594       9.457  22.289  48.341  1.00 54.01           N  
-ATOM   4506  CA  TRP C 594       8.303  23.169  48.473  1.00 53.22           C  
-ATOM   4507  C   TRP C 594       8.342  24.409  47.596  1.00 53.56           C  
-ATOM   4508  O   TRP C 594       7.877  25.467  48.014  1.00 54.12           O  
-ATOM   4509  CB  TRP C 594       8.168  23.612  49.923  1.00 50.29           C  
-ATOM   4510  CG  TRP C 594       7.713  22.536  50.838  1.00 46.36           C  
-ATOM   4511  CD1 TRP C 594       8.377  22.045  51.920  1.00 46.01           C  
-ATOM   4512  CD2 TRP C 594       6.443  21.881  50.812  1.00 48.07           C  
-ATOM   4513  NE1 TRP C 594       7.595  21.129  52.583  1.00 49.07           N  
-ATOM   4514  CE2 TRP C 594       6.401  21.009  51.921  1.00 49.42           C  
-ATOM   4515  CE3 TRP C 594       5.333  21.946  49.959  1.00 47.88           C  
-ATOM   4516  CZ2 TRP C 594       5.289  20.214  52.205  1.00 50.46           C  
-ATOM   4517  CZ3 TRP C 594       4.229  21.155  50.240  1.00 47.22           C  
-ATOM   4518  CH2 TRP C 594       4.216  20.300  51.353  1.00 48.68           C  
-ATOM   4519  N   ARG C 595       8.877  24.288  46.386  1.00 53.80           N  
-ATOM   4520  CA  ARG C 595       8.966  25.438  45.496  1.00 53.84           C  
-ATOM   4521  C   ARG C 595       7.631  25.837  44.873  1.00 54.29           C  
-ATOM   4522  O   ARG C 595       7.541  26.858  44.192  1.00 53.95           O  
-ATOM   4523  CB  ARG C 595      10.001  25.181  44.399  1.00 54.91           C  
-ATOM   4524  CG  ARG C 595       9.745  23.954  43.539  1.00 59.20           C  
-ATOM   4525  CD  ARG C 595      10.912  23.750  42.585  1.00 60.42           C  
-ATOM   4526  NE  ARG C 595      11.094  24.915  41.722  1.00 63.86           N  
-ATOM   4527  CZ  ARG C 595      12.245  25.257  41.152  1.00 63.61           C  
-ATOM   4528  NH1 ARG C 595      13.331  24.526  41.355  1.00 63.60           N  
-ATOM   4529  NH2 ARG C 595      12.309  26.333  40.378  1.00 63.77           N  
-ATOM   4530  N   ASN C 596       6.598  25.032  45.096  1.00 53.82           N  
-ATOM   4531  CA  ASN C 596       5.275  25.338  44.556  1.00 53.53           C  
-ATOM   4532  C   ASN C 596       4.360  25.833  45.675  1.00 51.97           C  
-ATOM   4533  O   ASN C 596       3.187  26.127  45.453  1.00 52.26           O  
-ATOM   4534  CB  ASN C 596       4.653  24.095  43.913  1.00 55.99           C  
-ATOM   4535  CG  ASN C 596       5.435  23.602  42.712  1.00 59.33           C  
-ATOM   4536  OD1 ASN C 596       5.754  24.369  41.801  1.00 60.41           O  
-ATOM   4537  ND2 ASN C 596       5.740  22.310  42.700  1.00 62.40           N  
-ATOM   4538  N   HIS C 597       4.918  25.922  46.877  1.00 49.51           N  
-ATOM   4539  CA  HIS C 597       4.183  26.349  48.060  1.00 46.23           C  
-ATOM   4540  C   HIS C 597       5.000  27.449  48.758  1.00 42.65           C  
-ATOM   4541  O   HIS C 597       5.537  27.246  49.842  1.00 42.14           O  
-ATOM   4542  CB  HIS C 597       3.992  25.136  48.982  1.00 46.26           C  
-ATOM   4543  CG  HIS C 597       3.008  25.345  50.093  1.00 49.23           C  
-ATOM   4544  ND1 HIS C 597       2.360  26.544  50.312  1.00 48.61           N  
-ATOM   4545  CD2 HIS C 597       2.576  24.505  51.065  1.00 48.54           C  
-ATOM   4546  CE1 HIS C 597       1.577  26.431  51.370  1.00 48.19           C  
-ATOM   4547  NE2 HIS C 597       1.691  25.203  51.847  1.00 43.59           N  
-ATOM   4548  N   PRO C 598       5.091  28.634  48.134  1.00 42.06           N  
-ATOM   4549  CA  PRO C 598       5.832  29.798  48.643  1.00 41.40           C  
-ATOM   4550  C   PRO C 598       5.581  30.181  50.101  1.00 39.91           C  
-ATOM   4551  O   PRO C 598       6.476  30.693  50.766  1.00 40.24           O  
-ATOM   4552  CB  PRO C 598       5.432  30.906  47.674  1.00 41.28           C  
-ATOM   4553  CG  PRO C 598       5.231  30.154  46.397  1.00 40.11           C  
-ATOM   4554  CD  PRO C 598       4.452  28.952  46.845  1.00 38.68           C  
-ATOM   4555  N   GLN C 599       4.374  29.924  50.598  1.00 39.84           N  
-ATOM   4556  CA  GLN C 599       4.013  30.248  51.979  1.00 37.13           C  
-ATOM   4557  C   GLN C 599       4.674  29.264  52.936  1.00 36.75           C  
-ATOM   4558  O   GLN C 599       5.060  29.619  54.049  1.00 34.99           O  
-ATOM   4559  CB  GLN C 599       2.487  30.180  52.156  1.00 39.95           C  
-ATOM   4560  CG  GLN C 599       1.955  30.868  53.407  1.00 34.90           C  
-ATOM   4561  CD  GLN C 599       0.513  30.477  53.721  1.00 36.19           C  
-ATOM   4562  OE1 GLN C 599      -0.213  29.982  52.858  1.00 34.58           O  
-ATOM   4563  NE2 GLN C 599       0.096  30.700  54.963  1.00 29.23           N  
-ATOM   4564  N   MET C 600       4.770  28.011  52.509  1.00 37.20           N  
-ATOM   4565  CA  MET C 600       5.409  26.989  53.324  1.00 36.75           C  
-ATOM   4566  C   MET C 600       6.907  27.325  53.429  1.00 35.02           C  
-ATOM   4567  O   MET C 600       7.509  27.200  54.494  1.00 33.84           O  
-ATOM   4568  CB  MET C 600       5.205  25.610  52.683  1.00 40.34           C  
-ATOM   4569  CG  MET C 600       6.016  24.477  53.296  1.00 41.67           C  
-ATOM   4570  SD  MET C 600       5.608  24.072  54.986  1.00 50.91           S  
-ATOM   4571  CE  MET C 600       4.605  22.587  54.742  1.00 52.70           C  
-ATOM   4572  N   ILE C 601       7.503  27.761  52.327  1.00 36.20           N  
-ATOM   4573  CA  ILE C 601       8.923  28.114  52.353  1.00 38.50           C  
-ATOM   4574  C   ILE C 601       9.165  29.186  53.408  1.00 37.98           C  
-ATOM   4575  O   ILE C 601      10.064  29.062  54.239  1.00 40.20           O  
-ATOM   4576  CB  ILE C 601       9.412  28.653  50.993  1.00 36.45           C  
-ATOM   4577  CG1 ILE C 601       9.152  27.618  49.897  1.00 38.20           C  
-ATOM   4578  CG2 ILE C 601      10.917  28.951  51.068  1.00 38.78           C  
-ATOM   4579  CD1 ILE C 601       9.500  28.095  48.502  1.00 38.75           C  
-ATOM   4580  N   ALA C 602       8.342  30.229  53.380  1.00 39.82           N  
-ATOM   4581  CA  ALA C 602       8.455  31.336  54.326  1.00 38.53           C  
-ATOM   4582  C   ALA C 602       8.416  30.880  55.776  1.00 39.20           C  
-ATOM   4583  O   ALA C 602       9.319  31.196  56.560  1.00 39.28           O  
-ATOM   4584  CB  ALA C 602       7.345  32.344  54.074  1.00 37.74           C  
-ATOM   4585  N   VAL C 603       7.367  30.142  56.135  1.00 38.30           N  
-ATOM   4586  CA  VAL C 603       7.214  29.660  57.509  1.00 39.56           C  
-ATOM   4587  C   VAL C 603       8.318  28.678  57.924  1.00 39.23           C  
-ATOM   4588  O   VAL C 603       8.698  28.617  59.094  1.00 40.54           O  
-ATOM   4589  CB  VAL C 603       5.822  29.010  57.718  1.00 41.40           C  
-ATOM   4590  CG1 VAL C 603       4.722  30.068  57.516  1.00 39.83           C  
-ATOM   4591  CG2 VAL C 603       5.619  27.858  56.739  1.00 40.58           C  
-ATOM   4592  N   LEU C 604       8.833  27.910  56.971  1.00 40.12           N  
-ATOM   4593  CA  LEU C 604       9.902  26.963  57.279  1.00 40.51           C  
-ATOM   4594  C   LEU C 604      11.196  27.733  57.538  1.00 39.80           C  
-ATOM   4595  O   LEU C 604      11.897  27.463  58.514  1.00 39.83           O  
-ATOM   4596  CB  LEU C 604      10.099  25.965  56.128  1.00 41.65           C  
-ATOM   4597  CG  LEU C 604       9.009  24.903  55.955  1.00 40.44           C  
-ATOM   4598  CD1 LEU C 604       9.282  24.073  54.710  1.00 39.69           C  
-ATOM   4599  CD2 LEU C 604       8.956  24.018  57.190  1.00 40.92           C  
-ATOM   4600  N   VAL C 605      11.502  28.705  56.679  1.00 40.27           N  
-ATOM   4601  CA  VAL C 605      12.713  29.501  56.856  1.00 39.16           C  
-ATOM   4602  C   VAL C 605      12.693  30.241  58.191  1.00 41.07           C  
-ATOM   4603  O   VAL C 605      13.699  30.281  58.911  1.00 40.93           O  
-ATOM   4604  CB  VAL C 605      12.891  30.536  55.726  1.00 39.87           C  
-ATOM   4605  CG1 VAL C 605      14.144  31.382  55.985  1.00 38.59           C  
-ATOM   4606  CG2 VAL C 605      13.022  29.832  54.390  1.00 33.14           C  
-ATOM   4607  N   ASP C 606      11.545  30.822  58.527  1.00 40.06           N  
-ATOM   4608  CA  ASP C 606      11.418  31.561  59.774  1.00 40.02           C  
-ATOM   4609  C   ASP C 606      11.608  30.654  60.988  1.00 40.35           C  
-ATOM   4610  O   ASP C 606      12.220  31.047  61.982  1.00 39.57           O  
-ATOM   4611  CB  ASP C 606      10.055  32.266  59.825  1.00 42.77           C  
-ATOM   4612  CG  ASP C 606       9.713  32.773  61.209  1.00 45.57           C  
-ATOM   4613  OD1 ASP C 606       9.196  31.979  62.023  1.00 49.93           O  
-ATOM   4614  OD2 ASP C 606       9.971  33.961  61.490  1.00 47.38           O  
-ATOM   4615  N   LYS C 607      11.099  29.431  60.901  1.00 41.44           N  
-ATOM   4616  CA  LYS C 607      11.228  28.490  62.005  1.00 41.78           C  
-ATOM   4617  C   LYS C 607      12.682  28.018  62.189  1.00 41.60           C  
-ATOM   4618  O   LYS C 607      13.191  27.970  63.311  1.00 40.63           O  
-ATOM   4619  CB  LYS C 607      10.304  27.288  61.778  1.00 42.58           C  
-ATOM   4620  CG  LYS C 607      10.093  26.437  63.016  1.00 42.16           C  
-ATOM   4621  CD  LYS C 607       9.422  27.219  64.143  1.00 45.25           C  
-ATOM   4622  CE  LYS C 607       8.014  27.654  63.773  1.00 48.62           C  
-ATOM   4623  NZ  LYS C 607       7.345  28.355  64.914  1.00 52.36           N  
-ATOM   4624  N   MET C 608      13.353  27.684  61.091  1.00 41.68           N  
-ATOM   4625  CA  MET C 608      14.740  27.226  61.170  1.00 45.72           C  
-ATOM   4626  C   MET C 608      15.637  28.283  61.806  1.00 46.75           C  
-ATOM   4627  O   MET C 608      16.489  27.968  62.635  1.00 47.46           O  
-ATOM   4628  CB  MET C 608      15.263  26.864  59.779  1.00 43.92           C  
-ATOM   4629  CG  MET C 608      14.519  25.707  59.147  1.00 47.12           C  
-ATOM   4630  SD  MET C 608      15.109  25.299  57.503  1.00 50.07           S  
-ATOM   4631  CE  MET C 608      14.740  26.792  56.629  1.00 57.60           C  
-ATOM   4632  N   ILE C 609      15.434  29.539  61.423  1.00 47.55           N  
-ATOM   4633  CA  ILE C 609      16.222  30.623  61.983  1.00 44.81           C  
-ATOM   4634  C   ILE C 609      15.980  30.736  63.480  1.00 45.44           C  
-ATOM   4635  O   ILE C 609      16.920  30.738  64.268  1.00 45.20           O  
-ATOM   4636  CB  ILE C 609      15.871  31.967  61.320  1.00 45.12           C  
-ATOM   4637  CG1 ILE C 609      16.268  31.926  59.844  1.00 42.61           C  
-ATOM   4638  CG2 ILE C 609      16.569  33.105  62.045  1.00 36.59           C  
-ATOM   4639  CD1 ILE C 609      15.956  33.177  59.096  1.00 42.83           C  
-ATOM   4640  N   ARG C 610      14.715  30.815  63.875  1.00 45.56           N  
-ATOM   4641  CA  ARG C 610      14.384  30.951  65.288  1.00 46.74           C  
-ATOM   4642  C   ARG C 610      14.879  29.812  66.172  1.00 47.53           C  
-ATOM   4643  O   ARG C 610      15.086  30.006  67.372  1.00 46.20           O  
-ATOM   4644  CB  ARG C 610      12.876  31.120  65.463  1.00 46.93           C  
-ATOM   4645  CG  ARG C 610      12.354  32.443  64.941  1.00 46.72           C  
-ATOM   4646  CD  ARG C 610      10.843  32.516  65.057  1.00 44.29           C  
-ATOM   4647  NE  ARG C 610      10.325  33.760  64.500  1.00 39.08           N  
-ATOM   4648  CZ  ARG C 610      10.374  34.934  65.115  1.00 37.36           C  
-ATOM   4649  NH1 ARG C 610      10.915  35.037  66.322  1.00 36.06           N  
-ATOM   4650  NH2 ARG C 610       9.879  36.009  64.519  1.00 35.69           N  
-ATOM   4651  N   THR C 611      15.062  28.629  65.592  1.00 48.37           N  
-ATOM   4652  CA  THR C 611      15.541  27.485  66.363  1.00 49.91           C  
-ATOM   4653  C   THR C 611      17.017  27.181  66.086  1.00 51.50           C  
-ATOM   4654  O   THR C 611      17.530  26.134  66.477  1.00 51.61           O  
-ATOM   4655  CB  THR C 611      14.685  26.216  66.092  1.00 48.19           C  
-ATOM   4656  OG1 THR C 611      14.574  25.994  64.682  1.00 45.04           O  
-ATOM   4657  CG2 THR C 611      13.297  26.376  66.687  1.00 48.30           C  
-ATOM   4658  N   GLN C 612      17.692  28.111  65.414  1.00 52.93           N  
-ATOM   4659  CA  GLN C 612      19.112  27.978  65.097  1.00 54.21           C  
-ATOM   4660  C   GLN C 612      19.457  26.855  64.122  1.00 54.59           C  
-ATOM   4661  O   GLN C 612      20.588  26.371  64.114  1.00 55.00           O  
-ATOM   4662  CB  GLN C 612      19.935  27.790  66.382  1.00 56.34           C  
-ATOM   4663  CG  GLN C 612      19.986  29.005  67.313  1.00 61.66           C  
-ATOM   4664  CD  GLN C 612      18.706  29.211  68.112  1.00 67.62           C  
-ATOM   4665  OE1 GLN C 612      18.292  28.340  68.881  1.00 70.36           O  
-ATOM   4666  NE2 GLN C 612      18.075  30.369  67.937  1.00 69.46           N  
-ATOM   4667  N   ILE C 613      18.494  26.434  63.306  1.00 53.99           N  
-ATOM   4668  CA  ILE C 613      18.750  25.380  62.328  1.00 52.50           C  
-ATOM   4669  C   ILE C 613      19.616  25.995  61.238  1.00 51.44           C  
-ATOM   4670  O   ILE C 613      20.476  25.337  60.653  1.00 52.46           O  
-ATOM   4671  CB  ILE C 613      17.444  24.848  61.710  1.00 52.21           C  
-ATOM   4672  CG1 ILE C 613      16.553  24.250  62.803  1.00 55.05           C  
-ATOM   4673  CG2 ILE C 613      17.754  23.815  60.643  1.00 51.77           C  
-ATOM   4674  CD1 ILE C 613      17.188  23.133  63.588  1.00 57.19           C  
-ATOM   4675  N   VAL C 614      19.355  27.264  60.951  1.00 49.91           N  
-ATOM   4676  CA  VAL C 614      20.139  28.015  59.983  1.00 46.45           C  
-ATOM   4677  C   VAL C 614      20.241  29.409  60.568  1.00 44.27           C  
-ATOM   4678  O   VAL C 614      19.650  29.691  61.618  1.00 43.16           O  
-ATOM   4679  CB  VAL C 614      19.485  28.089  58.585  1.00 47.63           C  
-ATOM   4680  CG1 VAL C 614      19.397  26.707  57.982  1.00 49.46           C  
-ATOM   4681  CG2 VAL C 614      18.114  28.745  58.670  1.00 49.49           C  
-ATOM   4682  N   ASP C 615      20.998  30.275  59.908  1.00 41.76           N  
-ATOM   4683  CA  ASP C 615      21.163  31.640  60.391  1.00 41.79           C  
-ATOM   4684  C   ASP C 615      20.708  32.643  59.347  1.00 39.59           C  
-ATOM   4685  O   ASP C 615      20.446  32.285  58.200  1.00 39.32           O  
-ATOM   4686  CB  ASP C 615      22.627  31.902  60.761  1.00 44.47           C  
-ATOM   4687  CG  ASP C 615      23.585  31.535  59.643  1.00 48.24           C  
-ATOM   4688  OD1 ASP C 615      23.443  32.075  58.527  1.00 51.73           O  
-ATOM   4689  OD2 ASP C 615      24.482  30.698  59.879  1.00 59.16           O  
-ATOM   4690  N   CYS C 616      20.617  33.903  59.750  1.00 39.10           N  
-ATOM   4691  CA  CYS C 616      20.185  34.949  58.841  1.00 39.16           C  
-ATOM   4692  C   CYS C 616      21.130  35.092  57.650  1.00 38.97           C  
-ATOM   4693  O   CYS C 616      20.688  35.335  56.527  1.00 37.05           O  
-ATOM   4694  CB  CYS C 616      20.056  36.265  59.608  1.00 39.89           C  
-ATOM   4695  SG  CYS C 616      18.778  36.198  60.911  1.00 45.55           S  
-ATOM   4696  N   ALA C 617      22.430  34.919  57.892  1.00 38.82           N  
-ATOM   4697  CA  ALA C 617      23.425  35.032  56.823  1.00 37.72           C  
-ATOM   4698  C   ALA C 617      23.237  33.977  55.742  1.00 36.22           C  
-ATOM   4699  O   ALA C 617      23.349  34.272  54.552  1.00 38.32           O  
-ATOM   4700  CB  ALA C 617      24.852  34.942  57.403  1.00 37.90           C  
-ATOM   4701  N   ALA C 618      22.963  32.743  56.144  1.00 35.83           N  
-ATOM   4702  CA  ALA C 618      22.756  31.680  55.162  1.00 36.78           C  
-ATOM   4703  C   ALA C 618      21.487  31.959  54.350  1.00 35.64           C  
-ATOM   4704  O   ALA C 618      21.431  31.693  53.146  1.00 35.63           O  
-ATOM   4705  CB  ALA C 618      22.651  30.324  55.862  1.00 37.20           C  
-ATOM   4706  N   VAL C 619      20.462  32.484  55.014  1.00 35.11           N  
-ATOM   4707  CA  VAL C 619      19.218  32.796  54.319  1.00 35.39           C  
-ATOM   4708  C   VAL C 619      19.462  33.918  53.311  1.00 34.78           C  
-ATOM   4709  O   VAL C 619      18.986  33.852  52.182  1.00 35.35           O  
-ATOM   4710  CB  VAL C 619      18.088  33.189  55.318  1.00 31.78           C  
-ATOM   4711  CG1 VAL C 619      16.884  33.740  54.565  1.00 35.95           C  
-ATOM   4712  CG2 VAL C 619      17.662  31.960  56.111  1.00 28.12           C  
-ATOM   4713  N   ALA C 620      20.221  34.936  53.703  1.00 35.73           N  
-ATOM   4714  CA  ALA C 620      20.520  36.038  52.786  1.00 36.06           C  
-ATOM   4715  C   ALA C 620      21.290  35.528  51.560  1.00 37.97           C  
-ATOM   4716  O   ALA C 620      21.058  35.982  50.436  1.00 37.48           O  
-ATOM   4717  CB  ALA C 620      21.324  37.114  53.504  1.00 34.70           C  
-ATOM   4718  N   ASN C 621      22.211  34.590  51.768  1.00 40.26           N  
-ATOM   4719  CA  ASN C 621      22.961  34.048  50.639  1.00 41.25           C  
-ATOM   4720  C   ASN C 621      22.045  33.199  49.774  1.00 40.97           C  
-ATOM   4721  O   ASN C 621      22.101  33.252  48.546  1.00 41.27           O  
-ATOM   4722  CB  ASN C 621      24.142  33.205  51.119  1.00 41.98           C  
-ATOM   4723  CG  ASN C 621      25.326  34.052  51.524  1.00 45.59           C  
-ATOM   4724  OD1 ASN C 621      25.767  34.925  50.771  1.00 46.67           O  
-ATOM   4725  ND2 ASN C 621      25.849  33.803  52.718  1.00 44.09           N  
-ATOM   4726  N   TRP C 622      21.196  32.419  50.429  1.00 41.53           N  
-ATOM   4727  CA  TRP C 622      20.254  31.551  49.734  1.00 41.73           C  
-ATOM   4728  C   TRP C 622      19.362  32.361  48.789  1.00 42.14           C  
-ATOM   4729  O   TRP C 622      19.093  31.950  47.663  1.00 41.81           O  
-ATOM   4730  CB  TRP C 622      19.416  30.800  50.771  1.00 44.73           C  
-ATOM   4731  CG  TRP C 622      18.258  30.034  50.213  1.00 48.70           C  
-ATOM   4732  CD1 TRP C 622      18.307  28.932  49.406  1.00 50.65           C  
-ATOM   4733  CD2 TRP C 622      16.874  30.304  50.441  1.00 50.85           C  
-ATOM   4734  NE1 TRP C 622      17.033  28.494  49.123  1.00 49.18           N  
-ATOM   4735  CE2 TRP C 622      16.135  29.319  49.746  1.00 52.62           C  
-ATOM   4736  CE3 TRP C 622      16.183  31.281  51.170  1.00 52.52           C  
-ATOM   4737  CZ2 TRP C 622      14.736  29.286  49.757  1.00 52.58           C  
-ATOM   4738  CZ3 TRP C 622      14.791  31.246  51.180  1.00 52.96           C  
-ATOM   4739  CH2 TRP C 622      14.085  30.253  50.478  1.00 48.89           C  
-ATOM   4740  N   ILE C 623      18.921  33.529  49.241  1.00 42.72           N  
-ATOM   4741  CA  ILE C 623      18.062  34.382  48.425  1.00 42.01           C  
-ATOM   4742  C   ILE C 623      18.717  34.859  47.139  1.00 41.91           C  
-ATOM   4743  O   ILE C 623      18.047  35.063  46.120  1.00 38.22           O  
-ATOM   4744  CB  ILE C 623      17.577  35.587  49.236  1.00 43.39           C  
-ATOM   4745  CG1 ILE C 623      16.430  35.129  50.136  1.00 46.92           C  
-ATOM   4746  CG2 ILE C 623      17.156  36.731  48.303  1.00 37.40           C  
-ATOM   4747  CD1 ILE C 623      16.011  36.144  51.151  1.00 55.16           C  
-ATOM   4748  N   PHE C 624      20.029  35.044  47.176  1.00 43.11           N  
-ATOM   4749  CA  PHE C 624      20.718  35.476  45.975  1.00 44.60           C  
-ATOM   4750  C   PHE C 624      21.313  34.299  45.200  1.00 45.26           C  
-ATOM   4751  O   PHE C 624      21.949  34.487  44.167  1.00 46.06           O  
-ATOM   4752  CB  PHE C 624      21.796  36.500  46.326  1.00 43.78           C  
-ATOM   4753  CG  PHE C 624      21.241  37.818  46.784  1.00 40.57           C  
-ATOM   4754  CD1 PHE C 624      20.786  37.982  48.083  1.00 41.08           C  
-ATOM   4755  CD2 PHE C 624      21.134  38.883  45.902  1.00 40.87           C  
-ATOM   4756  CE1 PHE C 624      20.228  39.193  48.498  1.00 41.29           C  
-ATOM   4757  CE2 PHE C 624      20.577  40.099  46.307  1.00 37.97           C  
-ATOM   4758  CZ  PHE C 624      20.122  40.252  47.606  1.00 40.54           C  
-ATOM   4759  N   SER C 625      21.083  33.084  45.687  1.00 46.89           N  
-ATOM   4760  CA  SER C 625      21.606  31.886  45.025  1.00 48.72           C  
-ATOM   4761  C   SER C 625      20.991  31.697  43.641  1.00 49.23           C  
-ATOM   4762  O   SER C 625      19.905  32.201  43.361  1.00 50.66           O  
-ATOM   4763  CB  SER C 625      21.344  30.641  45.878  1.00 47.31           C  
-ATOM   4764  OG  SER C 625      19.971  30.296  45.876  1.00 53.38           O  
-ATOM   4765  N   SER C 626      21.688  30.968  42.776  1.00 50.35           N  
-ATOM   4766  CA  SER C 626      21.211  30.737  41.415  1.00 50.24           C  
-ATOM   4767  C   SER C 626      19.951  29.875  41.376  1.00 50.56           C  
-ATOM   4768  O   SER C 626      19.211  29.889  40.390  1.00 49.73           O  
-ATOM   4769  CB  SER C 626      22.316  30.088  40.568  1.00 51.92           C  
-ATOM   4770  OG  SER C 626      22.657  28.798  41.047  1.00 51.30           O  
-ATOM   4771  N   GLU C 627      19.715  29.131  42.453  1.00 52.29           N  
-ATOM   4772  CA  GLU C 627      18.542  28.263  42.565  1.00 53.38           C  
-ATOM   4773  C   GLU C 627      17.224  29.045  42.548  1.00 53.46           C  
-ATOM   4774  O   GLU C 627      16.214  28.568  42.026  1.00 53.48           O  
-ATOM   4775  CB  GLU C 627      18.612  27.443  43.856  1.00 56.03           C  
-ATOM   4776  CG  GLU C 627      19.576  26.258  43.828  1.00 63.68           C  
-ATOM   4777  CD  GLU C 627      21.035  26.669  43.794  1.00 68.10           C  
-ATOM   4778  OE1 GLU C 627      21.480  27.235  42.771  1.00 69.83           O  
-ATOM   4779  OE2 GLU C 627      21.739  26.422  44.796  1.00 71.43           O  
-ATOM   4780  N   LEU C 628      17.239  30.239  43.132  1.00 52.48           N  
-ATOM   4781  CA  LEU C 628      16.055  31.092  43.195  1.00 51.59           C  
-ATOM   4782  C   LEU C 628      16.110  32.194  42.157  1.00 51.60           C  
-ATOM   4783  O   LEU C 628      15.302  33.116  42.181  1.00 51.92           O  
-ATOM   4784  CB  LEU C 628      15.930  31.730  44.581  1.00 51.67           C  
-ATOM   4785  CG  LEU C 628      15.284  30.909  45.695  1.00 49.79           C  
-ATOM   4786  CD1 LEU C 628      16.036  29.602  45.904  1.00 53.00           C  
-ATOM   4787  CD2 LEU C 628      15.275  31.738  46.962  1.00 46.34           C  
-ATOM   4788  N   SER C 629      17.063  32.096  41.241  1.00 51.80           N  
-ATOM   4789  CA  SER C 629      17.221  33.111  40.212  1.00 51.69           C  
-ATOM   4790  C   SER C 629      15.956  33.314  39.389  1.00 51.89           C  
-ATOM   4791  O   SER C 629      15.675  34.425  38.939  1.00 51.53           O  
-ATOM   4792  CB  SER C 629      18.379  32.743  39.285  1.00 53.61           C  
-ATOM   4793  OG  SER C 629      18.580  33.756  38.315  1.00 53.48           O  
-ATOM   4794  N   ARG C 630      15.199  32.239  39.193  1.00 52.58           N  
-ATOM   4795  CA  ARG C 630      13.970  32.303  38.413  1.00 53.35           C  
-ATOM   4796  C   ARG C 630      12.802  32.916  39.181  1.00 52.17           C  
-ATOM   4797  O   ARG C 630      11.884  33.463  38.574  1.00 50.72           O  
-ATOM   4798  CB  ARG C 630      13.577  30.908  37.919  1.00 57.91           C  
-ATOM   4799  CG  ARG C 630      14.572  30.281  36.957  1.00 64.77           C  
-ATOM   4800  CD  ARG C 630      14.045  28.963  36.405  1.00 71.72           C  
-ATOM   4801  NE  ARG C 630      12.861  29.156  35.570  1.00 79.63           N  
-ATOM   4802  CZ  ARG C 630      12.852  29.851  34.434  1.00 83.91           C  
-ATOM   4803  NH1 ARG C 630      13.967  30.421  33.993  1.00 86.18           N  
-ATOM   4804  NH2 ARG C 630      11.730  29.980  33.736  1.00 84.47           N  
-ATOM   4805  N   ASP C 631      12.837  32.820  40.509  1.00 51.25           N  
-ATOM   4806  CA  ASP C 631      11.779  33.378  41.354  1.00 50.79           C  
-ATOM   4807  C   ASP C 631      12.262  34.617  42.101  1.00 49.30           C  
-ATOM   4808  O   ASP C 631      11.616  35.069  43.044  1.00 49.43           O  
-ATOM   4809  CB  ASP C 631      11.310  32.348  42.387  1.00 52.46           C  
-ATOM   4810  CG  ASP C 631      10.650  31.142  41.755  1.00 55.03           C  
-ATOM   4811  OD1 ASP C 631       9.810  31.325  40.848  1.00 57.27           O  
-ATOM   4812  OD2 ASP C 631      10.966  30.013  42.175  1.00 54.20           O  
-ATOM   4813  N   PHE C 632      13.394  35.160  41.665  1.00 46.91           N  
-ATOM   4814  CA  PHE C 632      14.007  36.326  42.293  1.00 43.48           C  
-ATOM   4815  C   PHE C 632      13.130  37.580  42.265  1.00 42.38           C  
-ATOM   4816  O   PHE C 632      13.245  38.440  43.140  1.00 40.53           O  
-ATOM   4817  CB  PHE C 632      15.350  36.609  41.613  1.00 37.99           C  
-ATOM   4818  CG  PHE C 632      16.224  37.593  42.347  1.00 35.26           C  
-ATOM   4819  CD1 PHE C 632      16.767  37.275  43.596  1.00 40.41           C  
-ATOM   4820  CD2 PHE C 632      16.551  38.809  41.769  1.00 29.21           C  
-ATOM   4821  CE1 PHE C 632      17.631  38.159  44.255  1.00 31.57           C  
-ATOM   4822  CE2 PHE C 632      17.414  39.700  42.420  1.00 34.63           C  
-ATOM   4823  CZ  PHE C 632      17.954  39.370  43.665  1.00 30.40           C  
-ATOM   4824  N   THR C 633      12.261  37.693  41.264  1.00 42.14           N  
-ATOM   4825  CA  THR C 633      11.390  38.863  41.165  1.00 41.94           C  
-ATOM   4826  C   THR C 633      10.041  38.667  41.867  1.00 41.23           C  
-ATOM   4827  O   THR C 633       9.249  39.607  41.968  1.00 41.80           O  
-ATOM   4828  CB  THR C 633      11.130  39.251  39.695  1.00 42.56           C  
-ATOM   4829  OG1 THR C 633      10.603  38.123  38.988  1.00 49.47           O  
-ATOM   4830  CG2 THR C 633      12.417  39.705  39.024  1.00 43.33           C  
-ATOM   4831  N   ARG C 634       9.787  37.454  42.356  1.00 40.92           N  
-ATOM   4832  CA  ARG C 634       8.528  37.151  43.049  1.00 39.79           C  
-ATOM   4833  C   ARG C 634       8.522  37.686  44.483  1.00 38.78           C  
-ATOM   4834  O   ARG C 634       9.525  37.600  45.188  1.00 38.81           O  
-ATOM   4835  CB  ARG C 634       8.280  35.638  43.074  1.00 37.27           C  
-ATOM   4836  CG  ARG C 634       8.127  35.008  41.698  1.00 37.73           C  
-ATOM   4837  CD  ARG C 634       7.870  33.515  41.808  1.00 41.47           C  
-ATOM   4838  NE  ARG C 634       6.538  33.220  42.324  1.00 40.92           N  
-ATOM   4839  CZ  ARG C 634       6.146  32.017  42.727  1.00 46.09           C  
-ATOM   4840  NH1 ARG C 634       6.990  30.991  42.677  1.00 43.04           N  
-ATOM   4841  NH2 ARG C 634       4.910  31.836  43.172  1.00 42.67           N  
-ATOM   4842  N   LEU C 635       7.377  38.216  44.913  1.00 38.30           N  
-ATOM   4843  CA  LEU C 635       7.229  38.789  46.254  1.00 37.31           C  
-ATOM   4844  C   LEU C 635       7.626  37.953  47.451  1.00 35.39           C  
-ATOM   4845  O   LEU C 635       8.119  38.499  48.434  1.00 33.41           O  
-ATOM   4846  CB  LEU C 635       5.787  39.246  46.497  1.00 42.64           C  
-ATOM   4847  CG  LEU C 635       5.416  40.683  46.137  1.00 46.68           C  
-ATOM   4848  CD1 LEU C 635       5.557  40.883  44.631  1.00 47.00           C  
-ATOM   4849  CD2 LEU C 635       3.987  40.971  46.600  1.00 42.79           C  
-ATOM   4850  N   PHE C 636       7.398  36.645  47.407  1.00 35.51           N  
-ATOM   4851  CA  PHE C 636       7.723  35.843  48.580  1.00 35.54           C  
-ATOM   4852  C   PHE C 636       9.195  35.881  48.935  1.00 35.28           C  
-ATOM   4853  O   PHE C 636       9.558  35.779  50.105  1.00 35.73           O  
-ATOM   4854  CB  PHE C 636       7.252  34.394  48.422  1.00 36.73           C  
-ATOM   4855  CG  PHE C 636       8.122  33.553  47.546  1.00 38.22           C  
-ATOM   4856  CD1 PHE C 636       7.980  33.581  46.162  1.00 42.34           C  
-ATOM   4857  CD2 PHE C 636       9.069  32.705  48.110  1.00 39.02           C  
-ATOM   4858  CE1 PHE C 636       8.774  32.767  45.347  1.00 42.81           C  
-ATOM   4859  CE2 PHE C 636       9.862  31.894  47.315  1.00 41.15           C  
-ATOM   4860  CZ  PHE C 636       9.714  31.923  45.925  1.00 42.42           C  
-ATOM   4861  N   VAL C 637      10.041  36.036  47.924  1.00 34.74           N  
-ATOM   4862  CA  VAL C 637      11.476  36.098  48.153  1.00 35.48           C  
-ATOM   4863  C   VAL C 637      11.828  37.306  49.022  1.00 33.28           C  
-ATOM   4864  O   VAL C 637      12.557  37.186  50.001  1.00 32.33           O  
-ATOM   4865  CB  VAL C 637      12.246  36.182  46.807  1.00 38.43           C  
-ATOM   4866  CG1 VAL C 637      13.712  36.536  47.045  1.00 41.28           C  
-ATOM   4867  CG2 VAL C 637      12.143  34.841  46.080  1.00 38.66           C  
-ATOM   4868  N   TRP C 638      11.287  38.466  48.676  1.00 32.16           N  
-ATOM   4869  CA  TRP C 638      11.582  39.676  49.427  1.00 32.76           C  
-ATOM   4870  C   TRP C 638      10.897  39.712  50.793  1.00 33.03           C  
-ATOM   4871  O   TRP C 638      11.404  40.322  51.737  1.00 29.23           O  
-ATOM   4872  CB  TRP C 638      11.238  40.892  48.561  1.00 31.66           C  
-ATOM   4873  CG  TRP C 638      11.968  40.788  47.266  1.00 33.28           C  
-ATOM   4874  CD1 TRP C 638      11.461  40.379  46.068  1.00 32.96           C  
-ATOM   4875  CD2 TRP C 638      13.385  40.912  47.080  1.00 34.63           C  
-ATOM   4876  NE1 TRP C 638      12.474  40.225  45.150  1.00 31.57           N  
-ATOM   4877  CE2 TRP C 638      13.666  40.546  45.747  1.00 38.81           C  
-ATOM   4878  CE3 TRP C 638      14.445  41.293  47.916  1.00 38.32           C  
-ATOM   4879  CZ2 TRP C 638      14.970  40.543  45.227  1.00 37.95           C  
-ATOM   4880  CZ3 TRP C 638      15.741  41.290  47.401  1.00 41.95           C  
-ATOM   4881  CH2 TRP C 638      15.990  40.917  46.067  1.00 33.54           C  
-ATOM   4882  N   GLU C 639       9.755  39.041  50.907  1.00 32.25           N  
-ATOM   4883  CA  GLU C 639       9.070  38.983  52.193  1.00 33.29           C  
-ATOM   4884  C   GLU C 639       9.939  38.135  53.149  1.00 30.68           C  
-ATOM   4885  O   GLU C 639      10.108  38.471  54.328  1.00 28.67           O  
-ATOM   4886  CB  GLU C 639       7.669  38.368  52.018  1.00 36.19           C  
-ATOM   4887  CG  GLU C 639       6.797  39.157  51.031  1.00 48.86           C  
-ATOM   4888  CD  GLU C 639       5.355  38.667  50.932  1.00 54.87           C  
-ATOM   4889  OE1 GLU C 639       5.134  37.452  50.726  1.00 58.07           O  
-ATOM   4890  OE2 GLU C 639       4.442  39.514  51.046  1.00 59.49           O  
-ATOM   4891  N   ILE C 640      10.489  37.040  52.632  1.00 29.56           N  
-ATOM   4892  CA  ILE C 640      11.353  36.179  53.443  1.00 30.79           C  
-ATOM   4893  C   ILE C 640      12.612  36.958  53.864  1.00 28.80           C  
-ATOM   4894  O   ILE C 640      13.008  36.923  55.024  1.00 30.19           O  
-ATOM   4895  CB  ILE C 640      11.776  34.892  52.662  1.00 30.72           C  
-ATOM   4896  CG1 ILE C 640      10.544  34.009  52.429  1.00 34.04           C  
-ATOM   4897  CG2 ILE C 640      12.849  34.114  53.443  1.00 28.47           C  
-ATOM   4898  CD1 ILE C 640      10.809  32.726  51.655  1.00 25.63           C  
-ATOM   4899  N   LEU C 641      13.221  37.672  52.920  1.00 28.86           N  
-ATOM   4900  CA  LEU C 641      14.423  38.451  53.224  1.00 31.11           C  
-ATOM   4901  C   LEU C 641      14.134  39.465  54.324  1.00 30.58           C  
-ATOM   4902  O   LEU C 641      14.818  39.504  55.345  1.00 31.55           O  
-ATOM   4903  CB  LEU C 641      14.921  39.207  51.984  1.00 29.40           C  
-ATOM   4904  CG  LEU C 641      16.236  39.961  52.250  1.00 32.15           C  
-ATOM   4905  CD1 LEU C 641      17.333  38.963  52.609  1.00 31.32           C  
-ATOM   4906  CD2 LEU C 641      16.649  40.767  51.037  1.00 27.96           C  
-ATOM   4907  N   HIS C 642      13.107  40.282  54.110  1.00 31.92           N  
-ATOM   4908  CA  HIS C 642      12.756  41.295  55.087  1.00 32.59           C  
-ATOM   4909  C   HIS C 642      12.365  40.705  56.424  1.00 31.13           C  
-ATOM   4910  O   HIS C 642      12.654  41.292  57.462  1.00 29.20           O  
-ATOM   4911  CB  HIS C 642      11.674  42.223  54.517  1.00 35.76           C  
-ATOM   4912  CG  HIS C 642      12.207  43.143  53.462  1.00 41.52           C  
-ATOM   4913  ND1 HIS C 642      13.183  44.082  53.730  1.00 46.33           N  
-ATOM   4914  CD2 HIS C 642      12.004  43.184  52.124  1.00 43.70           C  
-ATOM   4915  CE1 HIS C 642      13.562  44.654  52.601  1.00 44.25           C  
-ATOM   4916  NE2 HIS C 642      12.864  44.125  51.611  1.00 44.53           N  
-ATOM   4917  N   SER C 643      11.732  39.534  56.414  1.00 30.32           N  
-ATOM   4918  CA  SER C 643      11.370  38.911  57.679  1.00 31.43           C  
-ATOM   4919  C   SER C 643      12.657  38.477  58.381  1.00 32.49           C  
-ATOM   4920  O   SER C 643      12.766  38.540  59.603  1.00 31.30           O  
-ATOM   4921  CB  SER C 643      10.472  37.691  57.459  1.00 32.33           C  
-ATOM   4922  OG  SER C 643      10.250  37.030  58.693  1.00 34.97           O  
-ATOM   4923  N   THR C 644      13.634  38.037  57.594  1.00 33.58           N  
-ATOM   4924  CA  THR C 644      14.914  37.602  58.147  1.00 33.05           C  
-ATOM   4925  C   THR C 644      15.662  38.790  58.778  1.00 32.12           C  
-ATOM   4926  O   THR C 644      16.180  38.693  59.896  1.00 31.80           O  
-ATOM   4927  CB  THR C 644      15.793  36.955  57.050  1.00 35.35           C  
-ATOM   4928  OG1 THR C 644      15.055  35.907  56.411  1.00 32.67           O  
-ATOM   4929  CG2 THR C 644      17.074  36.364  57.657  1.00 34.60           C  
-ATOM   4930  N   ILE C 645      15.706  39.913  58.067  1.00 29.32           N  
-ATOM   4931  CA  ILE C 645      16.375  41.099  58.584  1.00 29.17           C  
-ATOM   4932  C   ILE C 645      15.683  41.571  59.867  1.00 31.34           C  
-ATOM   4933  O   ILE C 645      16.344  41.967  60.823  1.00 31.73           O  
-ATOM   4934  CB  ILE C 645      16.369  42.244  57.544  1.00 26.28           C  
-ATOM   4935  CG1 ILE C 645      17.157  41.808  56.300  1.00 26.90           C  
-ATOM   4936  CG2 ILE C 645      16.965  43.504  58.145  1.00 23.33           C  
-ATOM   4937  CD1 ILE C 645      16.993  42.703  55.092  1.00 21.75           C  
-ATOM   4938  N   ARG C 646      14.354  41.520  59.898  1.00 32.06           N  
-ATOM   4939  CA  ARG C 646      13.629  41.945  61.089  1.00 31.14           C  
-ATOM   4940  C   ARG C 646      14.025  41.114  62.306  1.00 32.12           C  
-ATOM   4941  O   ARG C 646      14.259  41.662  63.387  1.00 32.00           O  
-ATOM   4942  CB  ARG C 646      12.110  41.875  60.865  1.00 32.55           C  
-ATOM   4943  CG  ARG C 646      11.574  43.020  59.995  1.00 35.07           C  
-ATOM   4944  CD  ARG C 646      10.077  43.246  60.189  1.00 32.89           C  
-ATOM   4945  NE  ARG C 646       9.264  42.089  59.803  1.00 37.77           N  
-ATOM   4946  CZ  ARG C 646       9.020  41.729  58.542  1.00 42.85           C  
-ATOM   4947  NH1 ARG C 646       9.527  42.431  57.534  1.00 43.39           N  
-ATOM   4948  NH2 ARG C 646       8.260  40.670  58.284  1.00 40.96           N  
-ATOM   4949  N   LYS C 647      14.106  39.798  62.139  1.00 32.48           N  
-ATOM   4950  CA  LYS C 647      14.495  38.934  63.248  1.00 34.07           C  
-ATOM   4951  C   LYS C 647      15.894  39.319  63.731  1.00 35.00           C  
-ATOM   4952  O   LYS C 647      16.147  39.389  64.930  1.00 35.06           O  
-ATOM   4953  CB  LYS C 647      14.469  37.459  62.824  1.00 34.29           C  
-ATOM   4954  CG  LYS C 647      13.070  36.849  62.801  1.00 39.83           C  
-ATOM   4955  CD  LYS C 647      13.092  35.349  62.513  1.00 32.54           C  
-ATOM   4956  CE  LYS C 647      13.270  35.065  61.043  1.00 32.43           C  
-ATOM   4957  NZ  LYS C 647      12.071  35.449  60.265  1.00 36.19           N  
-ATOM   4958  N   MET C 648      16.795  39.581  62.787  1.00 35.86           N  
-ATOM   4959  CA  MET C 648      18.165  39.976  63.114  1.00 36.79           C  
-ATOM   4960  C   MET C 648      18.188  41.299  63.872  1.00 36.47           C  
-ATOM   4961  O   MET C 648      18.999  41.487  64.783  1.00 36.47           O  
-ATOM   4962  CB  MET C 648      19.009  40.117  61.840  1.00 34.37           C  
-ATOM   4963  CG  MET C 648      20.424  40.619  62.103  1.00 38.82           C  
-ATOM   4964  SD  MET C 648      21.376  39.513  63.174  1.00 47.61           S  
-ATOM   4965  CE  MET C 648      21.857  38.302  61.977  1.00 40.02           C  
-ATOM   4966  N   ASN C 649      17.306  42.215  63.485  1.00 36.61           N  
-ATOM   4967  CA  ASN C 649      17.230  43.517  64.134  1.00 38.82           C  
-ATOM   4968  C   ASN C 649      16.795  43.362  65.601  1.00 40.91           C  
-ATOM   4969  O   ASN C 649      17.061  44.228  66.433  1.00 40.17           O  
-ATOM   4970  CB  ASN C 649      16.244  44.428  63.386  1.00 37.76           C  
-ATOM   4971  CG  ASN C 649      16.738  44.835  61.987  1.00 38.94           C  
-ATOM   4972  OD1 ASN C 649      15.992  45.442  61.212  1.00 37.12           O  
-ATOM   4973  ND2 ASN C 649      17.989  44.515  61.668  1.00 28.97           N  
-ATOM   4974  N   LYS C 650      16.133  42.253  65.921  1.00 44.49           N  
-ATOM   4975  CA  LYS C 650      15.692  42.016  67.296  1.00 48.96           C  
-ATOM   4976  C   LYS C 650      16.712  41.251  68.146  1.00 51.08           C  
-ATOM   4977  O   LYS C 650      16.591  41.210  69.371  1.00 50.34           O  
-ATOM   4978  CB  LYS C 650      14.351  41.276  67.317  1.00 50.60           C  
-ATOM   4979  CG  LYS C 650      13.183  42.097  66.779  1.00 57.24           C  
-ATOM   4980  CD  LYS C 650      11.855  41.368  66.939  1.00 61.96           C  
-ATOM   4981  CE  LYS C 650      10.688  42.239  66.481  1.00 66.10           C  
-ATOM   4982  NZ  LYS C 650       9.362  41.567  66.649  1.00 68.97           N  
-ATOM   4983  N   HIS C 651      17.707  40.643  67.503  1.00 53.00           N  
-ATOM   4984  CA  HIS C 651      18.736  39.904  68.237  1.00 55.57           C  
-ATOM   4985  C   HIS C 651      19.499  40.877  69.127  1.00 56.16           C  
-ATOM   4986  O   HIS C 651      20.086  41.842  68.645  1.00 56.21           O  
-ATOM   4987  CB  HIS C 651      19.722  39.223  67.278  1.00 58.41           C  
-ATOM   4988  CG  HIS C 651      19.161  38.033  66.561  1.00 64.14           C  
-ATOM   4989  ND1 HIS C 651      19.889  37.314  65.636  1.00 65.10           N  
-ATOM   4990  CD2 HIS C 651      17.945  37.438  66.625  1.00 66.10           C  
-ATOM   4991  CE1 HIS C 651      19.147  36.329  65.161  1.00 66.22           C  
-ATOM   4992  NE2 HIS C 651      17.963  36.382  65.745  1.00 68.76           N  
-ATOM   4993  N   VAL C 652      19.488  40.614  70.428  1.00 57.92           N  
-ATOM   4994  CA  VAL C 652      20.165  41.468  71.399  1.00 58.67           C  
-ATOM   4995  C   VAL C 652      21.675  41.229  71.439  1.00 58.56           C  
-ATOM   4996  O   VAL C 652      22.135  40.088  71.450  1.00 58.79           O  
-ATOM   4997  CB  VAL C 652      19.585  41.242  72.809  1.00 61.02           C  
-ATOM   4998  CG1 VAL C 652      19.686  39.770  73.176  1.00 62.15           C  
-ATOM   4999  CG2 VAL C 652      20.321  42.108  73.825  1.00 60.77           C  
-ATOM   5000  N   GLY C 653      22.440  42.317  71.462  1.00 58.95           N  
-ATOM   5001  CA  GLY C 653      23.887  42.208  71.499  1.00 58.37           C  
-ATOM   5002  C   GLY C 653      24.476  41.557  70.261  1.00 58.87           C  
-ATOM   5003  O   GLY C 653      25.433  40.784  70.357  1.00 59.16           O  
-ATOM   5004  N   ALA C 702      23.918  41.870  69.094  1.00 57.95           N  
-ATOM   5005  CA  ALA C 702      24.405  41.297  67.844  1.00 56.84           C  
-ATOM   5006  C   ALA C 702      24.693  42.365  66.791  1.00 56.11           C  
-ATOM   5007  O   ALA C 702      24.477  42.149  65.598  1.00 54.21           O  
-ATOM   5008  CB  ALA C 702      23.391  40.294  67.309  1.00 55.95           C  
-ATOM   5009  N   GLN C 703      25.192  43.514  67.235  1.00 55.85           N  
-ATOM   5010  CA  GLN C 703      25.501  44.611  66.324  1.00 55.41           C  
-ATOM   5011  C   GLN C 703      26.390  44.179  65.161  1.00 52.79           C  
-ATOM   5012  O   GLN C 703      26.138  44.534  64.007  1.00 51.96           O  
-ATOM   5013  CB  GLN C 703      26.191  45.742  67.077  1.00 58.56           C  
-ATOM   5014  CG  GLN C 703      25.406  46.287  68.242  1.00 66.72           C  
-ATOM   5015  CD  GLN C 703      26.106  47.463  68.890  1.00 72.70           C  
-ATOM   5016  OE1 GLN C 703      25.635  48.010  69.888  1.00 76.63           O  
-ATOM   5017  NE2 GLN C 703      27.240  47.863  68.320  1.00 73.69           N  
-ATOM   5018  N   SER C 704      27.438  43.423  65.472  1.00 50.00           N  
-ATOM   5019  CA  SER C 704      28.366  42.950  64.449  1.00 46.85           C  
-ATOM   5020  C   SER C 704      27.660  42.058  63.429  1.00 45.12           C  
-ATOM   5021  O   SER C 704      27.821  42.235  62.219  1.00 42.89           O  
-ATOM   5022  CB  SER C 704      29.519  42.177  65.098  1.00 48.51           C  
-ATOM   5023  OG  SER C 704      30.349  41.576  64.116  1.00 51.91           O  
-ATOM   5024  N   GLU C 705      26.882  41.100  63.924  1.00 41.95           N  
-ATOM   5025  CA  GLU C 705      26.157  40.182  63.053  1.00 42.64           C  
-ATOM   5026  C   GLU C 705      25.139  40.926  62.183  1.00 39.81           C  
-ATOM   5027  O   GLU C 705      24.983  40.625  60.994  1.00 39.80           O  
-ATOM   5028  CB  GLU C 705      25.445  39.120  63.892  1.00 45.94           C  
-ATOM   5029  CG  GLU C 705      24.935  37.940  63.078  1.00 57.50           C  
-ATOM   5030  CD  GLU C 705      24.363  36.829  63.940  1.00 61.96           C  
-ATOM   5031  OE1 GLU C 705      23.837  35.842  63.373  1.00 62.98           O  
-ATOM   5032  OE2 GLU C 705      24.444  36.945  65.183  1.00 67.03           O  
-ATOM   5033  N   GLN C 706      24.455  41.894  62.788  1.00 36.20           N  
-ATOM   5034  CA  GLN C 706      23.456  42.697  62.094  1.00 33.97           C  
-ATOM   5035  C   GLN C 706      24.152  43.498  60.991  1.00 32.94           C  
-ATOM   5036  O   GLN C 706      23.740  43.469  59.833  1.00 31.94           O  
-ATOM   5037  CB  GLN C 706      22.757  43.634  63.093  1.00 31.73           C  
-ATOM   5038  CG  GLN C 706      21.755  44.631  62.480  1.00 30.48           C  
-ATOM   5039  CD  GLN C 706      21.102  45.527  63.532  1.00 33.92           C  
-ATOM   5040  OE1 GLN C 706      19.887  45.742  63.519  1.00 36.02           O  
-ATOM   5041  NE2 GLN C 706      21.911  46.055  64.445  1.00 28.03           N  
-ATOM   5042  N   LYS C 707      25.224  44.195  61.351  1.00 31.87           N  
-ATOM   5043  CA  LYS C 707      25.958  44.985  60.375  1.00 32.11           C  
-ATOM   5044  C   LYS C 707      26.427  44.103  59.224  1.00 31.03           C  
-ATOM   5045  O   LYS C 707      26.317  44.479  58.055  1.00 29.73           O  
-ATOM   5046  CB  LYS C 707      27.160  45.676  61.025  1.00 31.93           C  
-ATOM   5047  CG  LYS C 707      27.925  46.578  60.069  1.00 31.62           C  
-ATOM   5048  CD  LYS C 707      28.984  47.391  60.788  1.00 29.12           C  
-ATOM   5049  CE  LYS C 707      29.641  48.381  59.836  1.00 36.31           C  
-ATOM   5050  NZ  LYS C 707      30.546  49.338  60.534  1.00 35.80           N  
-ATOM   5051  N   ASN C 708      26.941  42.925  59.553  1.00 31.05           N  
-ATOM   5052  CA  ASN C 708      27.418  42.015  58.527  1.00 33.29           C  
-ATOM   5053  C   ASN C 708      26.284  41.526  57.633  1.00 32.05           C  
-ATOM   5054  O   ASN C 708      26.483  41.303  56.441  1.00 29.72           O  
-ATOM   5055  CB  ASN C 708      28.152  40.830  59.164  1.00 37.65           C  
-ATOM   5056  CG  ASN C 708      29.545  41.211  59.676  1.00 43.73           C  
-ATOM   5057  OD1 ASN C 708      30.216  40.420  60.345  1.00 45.70           O  
-ATOM   5058  ND2 ASN C 708      29.982  42.426  59.356  1.00 38.04           N  
-ATOM   5059  N   LEU C 709      25.094  41.351  58.202  1.00 32.59           N  
-ATOM   5060  CA  LEU C 709      23.961  40.919  57.388  1.00 32.80           C  
-ATOM   5061  C   LEU C 709      23.722  41.963  56.289  1.00 31.59           C  
-ATOM   5062  O   LEU C 709      23.567  41.618  55.120  1.00 33.10           O  
-ATOM   5063  CB  LEU C 709      22.693  40.753  58.244  1.00 35.87           C  
-ATOM   5064  CG  LEU C 709      21.423  40.286  57.505  1.00 36.20           C  
-ATOM   5065  CD1 LEU C 709      21.644  38.907  56.910  1.00 36.49           C  
-ATOM   5066  CD2 LEU C 709      20.231  40.260  58.458  1.00 36.66           C  
-ATOM   5067  N   PHE C 710      23.709  43.242  56.657  1.00 30.42           N  
-ATOM   5068  CA  PHE C 710      23.485  44.301  55.672  1.00 28.93           C  
-ATOM   5069  C   PHE C 710      24.629  44.425  54.657  1.00 31.20           C  
-ATOM   5070  O   PHE C 710      24.391  44.661  53.465  1.00 30.91           O  
-ATOM   5071  CB  PHE C 710      23.264  45.648  56.369  1.00 28.47           C  
-ATOM   5072  CG  PHE C 710      21.908  45.787  56.998  1.00 26.96           C  
-ATOM   5073  CD1 PHE C 710      21.740  45.616  58.370  1.00 28.58           C  
-ATOM   5074  CD2 PHE C 710      20.786  46.072  56.211  1.00 25.67           C  
-ATOM   5075  CE1 PHE C 710      20.458  45.730  58.959  1.00 28.76           C  
-ATOM   5076  CE2 PHE C 710      19.506  46.186  56.792  1.00 27.96           C  
-ATOM   5077  CZ  PHE C 710      19.349  46.013  58.166  1.00 23.51           C  
-ATOM   5078  N   LEU C 711      25.869  44.279  55.123  1.00 30.88           N  
-ATOM   5079  CA  LEU C 711      27.012  44.353  54.216  1.00 31.34           C  
-ATOM   5080  C   LEU C 711      26.888  43.292  53.121  1.00 31.43           C  
-ATOM   5081  O   LEU C 711      27.030  43.588  51.934  1.00 31.74           O  
-ATOM   5082  CB  LEU C 711      28.324  44.175  54.998  1.00 30.40           C  
-ATOM   5083  CG  LEU C 711      28.609  45.378  55.902  1.00 23.63           C  
-ATOM   5084  CD1 LEU C 711      29.906  45.201  56.675  1.00 28.06           C  
-ATOM   5085  CD2 LEU C 711      28.658  46.615  55.035  1.00 25.65           C  
-ATOM   5086  N   VAL C 712      26.616  42.059  53.532  1.00 33.07           N  
-ATOM   5087  CA  VAL C 712      26.453  40.948  52.602  1.00 34.82           C  
-ATOM   5088  C   VAL C 712      25.345  41.228  51.588  1.00 34.87           C  
-ATOM   5089  O   VAL C 712      25.532  41.030  50.381  1.00 34.20           O  
-ATOM   5090  CB  VAL C 712      26.116  39.648  53.355  1.00 38.05           C  
-ATOM   5091  CG1 VAL C 712      25.880  38.514  52.362  1.00 44.04           C  
-ATOM   5092  CG2 VAL C 712      27.250  39.294  54.293  1.00 45.84           C  
-ATOM   5093  N   ILE C 713      24.195  41.694  52.074  1.00 33.68           N  
-ATOM   5094  CA  ILE C 713      23.089  42.004  51.177  1.00 30.90           C  
-ATOM   5095  C   ILE C 713      23.503  43.056  50.159  1.00 30.33           C  
-ATOM   5096  O   ILE C 713      23.273  42.873  48.963  1.00 30.44           O  
-ATOM   5097  CB  ILE C 713      21.842  42.482  51.958  1.00 30.87           C  
-ATOM   5098  CG1 ILE C 713      21.324  41.336  52.831  1.00 30.13           C  
-ATOM   5099  CG2 ILE C 713      20.765  42.961  50.986  1.00 28.84           C  
-ATOM   5100  CD1 ILE C 713      20.229  41.739  53.811  1.00 34.25           C  
-ATOM   5101  N   PHE C 714      24.125  44.143  50.617  1.00 28.50           N  
-ATOM   5102  CA  PHE C 714      24.562  45.186  49.690  1.00 30.17           C  
-ATOM   5103  C   PHE C 714      25.572  44.646  48.674  1.00 32.19           C  
-ATOM   5104  O   PHE C 714      25.499  44.970  47.490  1.00 32.00           O  
-ATOM   5105  CB  PHE C 714      25.167  46.384  50.437  1.00 27.42           C  
-ATOM   5106  CG  PHE C 714      24.159  47.180  51.230  1.00 31.81           C  
-ATOM   5107  CD1 PHE C 714      22.926  47.527  50.676  1.00 33.27           C  
-ATOM   5108  CD2 PHE C 714      24.433  47.567  52.539  1.00 28.46           C  
-ATOM   5109  CE1 PHE C 714      21.974  48.248  51.422  1.00 30.74           C  
-ATOM   5110  CE2 PHE C 714      23.489  48.287  53.294  1.00 29.89           C  
-ATOM   5111  CZ  PHE C 714      22.259  48.625  52.733  1.00 26.28           C  
-ATOM   5112  N   GLN C 715      26.506  43.813  49.125  1.00 34.44           N  
-ATOM   5113  CA  GLN C 715      27.488  43.253  48.204  1.00 36.32           C  
-ATOM   5114  C   GLN C 715      26.810  42.464  47.098  1.00 36.20           C  
-ATOM   5115  O   GLN C 715      27.060  42.711  45.921  1.00 37.11           O  
-ATOM   5116  CB  GLN C 715      28.474  42.339  48.935  1.00 37.82           C  
-ATOM   5117  CG  GLN C 715      29.589  43.081  49.640  1.00 45.01           C  
-ATOM   5118  CD  GLN C 715      30.779  42.183  49.926  1.00 49.66           C  
-ATOM   5119  OE1 GLN C 715      30.685  41.241  50.713  1.00 50.31           O  
-ATOM   5120  NE2 GLN C 715      31.904  42.465  49.274  1.00 47.06           N  
-ATOM   5121  N   ARG C 716      25.958  41.512  47.480  1.00 36.80           N  
-ATOM   5122  CA  ARG C 716      25.247  40.692  46.506  1.00 36.64           C  
-ATOM   5123  C   ARG C 716      24.484  41.563  45.505  1.00 35.51           C  
-ATOM   5124  O   ARG C 716      24.485  41.275  44.310  1.00 37.31           O  
-ATOM   5125  CB  ARG C 716      24.278  39.733  47.211  1.00 38.33           C  
-ATOM   5126  CG  ARG C 716      24.886  38.951  48.374  1.00 44.29           C  
-ATOM   5127  CD  ARG C 716      26.001  37.978  47.968  1.00 49.40           C  
-ATOM   5128  NE  ARG C 716      25.525  36.901  47.107  1.00 52.17           N  
-ATOM   5129  CZ  ARG C 716      25.453  36.979  45.779  1.00 56.91           C  
-ATOM   5130  NH1 ARG C 716      25.834  38.087  45.153  1.00 56.40           N  
-ATOM   5131  NH2 ARG C 716      24.999  35.949  45.073  1.00 55.07           N  
-ATOM   5132  N   PHE C 717      23.838  42.626  45.988  1.00 36.12           N  
-ATOM   5133  CA  PHE C 717      23.090  43.535  45.105  1.00 33.41           C  
-ATOM   5134  C   PHE C 717      24.047  44.258  44.148  1.00 33.26           C  
-ATOM   5135  O   PHE C 717      23.818  44.319  42.941  1.00 30.95           O  
-ATOM   5136  CB  PHE C 717      22.320  44.595  45.919  1.00 30.48           C  
-ATOM   5137  CG  PHE C 717      20.877  44.233  46.225  1.00 30.48           C  
-ATOM   5138  CD1 PHE C 717      19.968  43.991  45.199  1.00 31.71           C  
-ATOM   5139  CD2 PHE C 717      20.431  44.153  47.543  1.00 24.46           C  
-ATOM   5140  CE1 PHE C 717      18.630  43.670  45.482  1.00 31.18           C  
-ATOM   5141  CE2 PHE C 717      19.103  43.836  47.836  1.00 34.24           C  
-ATOM   5142  CZ  PHE C 717      18.200  43.593  46.801  1.00 30.10           C  
-ATOM   5143  N   ILE C 718      25.111  44.830  44.705  1.00 33.25           N  
-ATOM   5144  CA  ILE C 718      26.091  45.550  43.899  1.00 34.22           C  
-ATOM   5145  C   ILE C 718      26.635  44.648  42.798  1.00 34.91           C  
-ATOM   5146  O   ILE C 718      26.780  45.073  41.651  1.00 37.30           O  
-ATOM   5147  CB  ILE C 718      27.262  46.067  44.773  1.00 32.71           C  
-ATOM   5148  CG1 ILE C 718      26.724  47.080  45.786  1.00 32.59           C  
-ATOM   5149  CG2 ILE C 718      28.332  46.719  43.894  1.00 29.66           C  
-ATOM   5150  CD1 ILE C 718      27.703  47.495  46.855  1.00 34.85           C  
-ATOM   5151  N   MET C 719      26.905  43.396  43.144  1.00 35.83           N  
-ATOM   5152  CA  MET C 719      27.437  42.441  42.186  1.00 37.80           C  
-ATOM   5153  C   MET C 719      26.455  42.090  41.069  1.00 38.61           C  
-ATOM   5154  O   MET C 719      26.801  42.168  39.888  1.00 38.49           O  
-ATOM   5155  CB  MET C 719      27.864  41.154  42.903  1.00 40.33           C  
-ATOM   5156  CG  MET C 719      28.527  40.134  41.983  1.00 51.92           C  
-ATOM   5157  SD  MET C 719      28.781  38.516  42.758  1.00 65.35           S  
-ATOM   5158  CE  MET C 719      27.330  37.609  42.132  1.00 61.83           C  
-ATOM   5159  N   ILE C 720      25.231  41.703  41.417  1.00 38.19           N  
-ATOM   5160  CA  ILE C 720      24.293  41.338  40.360  1.00 37.86           C  
-ATOM   5161  C   ILE C 720      23.894  42.538  39.526  1.00 35.89           C  
-ATOM   5162  O   ILE C 720      23.693  42.423  38.324  1.00 39.00           O  
-ATOM   5163  CB  ILE C 720      23.047  40.641  40.913  1.00 38.84           C  
-ATOM   5164  CG1 ILE C 720      22.259  41.586  41.811  1.00 39.40           C  
-ATOM   5165  CG2 ILE C 720      23.465  39.415  41.682  1.00 41.28           C  
-ATOM   5166  CD1 ILE C 720      21.040  40.952  42.401  1.00 43.53           C  
-ATOM   5167  N   LEU C 721      23.788  43.701  40.151  1.00 35.76           N  
-ATOM   5168  CA  LEU C 721      23.445  44.904  39.401  1.00 35.73           C  
-ATOM   5169  C   LEU C 721      24.592  45.284  38.453  1.00 36.53           C  
-ATOM   5170  O   LEU C 721      24.362  45.653  37.297  1.00 35.96           O  
-ATOM   5171  CB  LEU C 721      23.158  46.069  40.356  1.00 33.60           C  
-ATOM   5172  CG  LEU C 721      21.806  46.029  41.081  1.00 32.24           C  
-ATOM   5173  CD1 LEU C 721      21.797  47.048  42.219  1.00 26.99           C  
-ATOM   5174  CD2 LEU C 721      20.676  46.324  40.087  1.00 31.90           C  
-ATOM   5175  N   THR C 722      25.825  45.203  38.945  1.00 36.44           N  
-ATOM   5176  CA  THR C 722      26.983  45.540  38.119  1.00 38.81           C  
-ATOM   5177  C   THR C 722      27.086  44.621  36.905  1.00 38.56           C  
-ATOM   5178  O   THR C 722      27.320  45.080  35.789  1.00 38.76           O  
-ATOM   5179  CB  THR C 722      28.299  45.452  38.922  1.00 39.62           C  
-ATOM   5180  OG1 THR C 722      28.283  46.437  39.963  1.00 35.62           O  
-ATOM   5181  CG2 THR C 722      29.506  45.704  38.005  1.00 40.85           C  
-ATOM   5182  N   GLU C 723      26.909  43.326  37.128  1.00 39.06           N  
-ATOM   5183  CA  GLU C 723      26.972  42.357  36.049  1.00 43.08           C  
-ATOM   5184  C   GLU C 723      25.967  42.731  34.959  1.00 45.07           C  
-ATOM   5185  O   GLU C 723      26.301  42.758  33.775  1.00 45.36           O  
-ATOM   5186  CB  GLU C 723      26.665  40.970  36.594  1.00 45.96           C  
-ATOM   5187  CG  GLU C 723      26.418  39.938  35.529  1.00 55.54           C  
-ATOM   5188  CD  GLU C 723      26.034  38.603  36.117  1.00 61.88           C  
-ATOM   5189  OE1 GLU C 723      25.072  38.563  36.916  1.00 65.90           O  
-ATOM   5190  OE2 GLU C 723      26.692  37.595  35.784  1.00 67.05           O  
-ATOM   5191  N   HIS C 724      24.737  43.028  35.369  1.00 45.29           N  
-ATOM   5192  CA  HIS C 724      23.692  43.423  34.430  1.00 43.62           C  
-ATOM   5193  C   HIS C 724      24.095  44.682  33.662  1.00 44.13           C  
-ATOM   5194  O   HIS C 724      24.028  44.723  32.436  1.00 43.23           O  
-ATOM   5195  CB  HIS C 724      22.384  43.694  35.178  1.00 41.72           C  
-ATOM   5196  CG  HIS C 724      21.275  44.196  34.303  1.00 38.31           C  
-ATOM   5197  ND1 HIS C 724      20.459  43.355  33.576  1.00 35.30           N  
-ATOM   5198  CD2 HIS C 724      20.858  45.456  34.030  1.00 37.75           C  
-ATOM   5199  CE1 HIS C 724      19.586  44.076  32.895  1.00 37.62           C  
-ATOM   5200  NE2 HIS C 724      19.806  45.353  33.151  1.00 37.73           N  
-ATOM   5201  N   LEU C 725      24.512  45.708  34.396  1.00 44.29           N  
-ATOM   5202  CA  LEU C 725      24.904  46.978  33.800  1.00 47.32           C  
-ATOM   5203  C   LEU C 725      26.087  46.872  32.844  1.00 50.97           C  
-ATOM   5204  O   LEU C 725      26.150  47.595  31.845  1.00 50.26           O  
-ATOM   5205  CB  LEU C 725      25.211  47.991  34.903  1.00 45.36           C  
-ATOM   5206  CG  LEU C 725      23.985  48.386  35.736  1.00 45.54           C  
-ATOM   5207  CD1 LEU C 725      24.404  49.154  36.978  1.00 41.57           C  
-ATOM   5208  CD2 LEU C 725      23.042  49.217  34.870  1.00 45.21           C  
-ATOM   5209  N   VAL C 726      27.026  45.983  33.157  1.00 53.05           N  
-ATOM   5210  CA  VAL C 726      28.193  45.790  32.304  1.00 56.49           C  
-ATOM   5211  C   VAL C 726      27.782  45.010  31.055  1.00 58.10           C  
-ATOM   5212  O   VAL C 726      28.149  45.363  29.934  1.00 58.29           O  
-ATOM   5213  CB  VAL C 726      29.304  45.015  33.043  1.00 56.92           C  
-ATOM   5214  CG1 VAL C 726      30.432  44.669  32.077  1.00 60.30           C  
-ATOM   5215  CG2 VAL C 726      29.842  45.855  34.191  1.00 55.21           C  
-ATOM   5216  N   ARG C 727      27.006  43.955  31.262  1.00 59.36           N  
-ATOM   5217  CA  ARG C 727      26.533  43.121  30.167  1.00 61.18           C  
-ATOM   5218  C   ARG C 727      25.676  43.919  29.183  1.00 61.87           C  
-ATOM   5219  O   ARG C 727      25.614  43.590  28.000  1.00 61.97           O  
-ATOM   5220  CB  ARG C 727      25.748  41.943  30.742  1.00 61.65           C  
-ATOM   5221  CG  ARG C 727      25.183  40.968  29.732  1.00 64.24           C  
-ATOM   5222  CD  ARG C 727      24.746  39.714  30.466  1.00 68.68           C  
-ATOM   5223  NE  ARG C 727      23.930  40.054  31.631  1.00 74.88           N  
-ATOM   5224  CZ  ARG C 727      23.667  39.226  32.639  1.00 75.52           C  
-ATOM   5225  NH1 ARG C 727      24.158  37.994  32.633  1.00 75.41           N  
-ATOM   5226  NH2 ARG C 727      22.910  39.631  33.654  1.00 74.79           N  
-ATOM   5227  N   CYS C 728      25.021  44.970  29.674  1.00 62.75           N  
-ATOM   5228  CA  CYS C 728      24.187  45.827  28.830  1.00 63.58           C  
-ATOM   5229  C   CYS C 728      25.053  46.813  28.053  1.00 65.09           C  
-ATOM   5230  O   CYS C 728      24.652  47.331  27.013  1.00 65.83           O  
-ATOM   5231  CB  CYS C 728      23.182  46.617  29.676  1.00 62.35           C  
-ATOM   5232  SG  CYS C 728      21.786  45.665  30.305  1.00 58.04           S  
-ATOM   5233  N   GLU C 729      26.238  47.086  28.579  1.00 65.83           N  
-ATOM   5234  CA  GLU C 729      27.152  48.006  27.929  1.00 67.28           C  
-ATOM   5235  C   GLU C 729      28.029  47.240  26.948  1.00 66.78           C  
-ATOM   5236  O   GLU C 729      28.464  47.785  25.939  1.00 66.65           O  
-ATOM   5237  CB  GLU C 729      28.018  48.704  28.977  1.00 69.86           C  
-ATOM   5238  CG  GLU C 729      29.163  49.513  28.398  1.00 76.43           C  
-ATOM   5239  CD  GLU C 729      30.085  50.057  29.471  1.00 80.75           C  
-ATOM   5240  OE1 GLU C 729      30.510  49.264  30.341  1.00 82.11           O  
-ATOM   5241  OE2 GLU C 729      30.386  51.270  29.443  1.00 81.65           O  
-ATOM   5242  N   THR C 730      28.273  45.968  27.251  1.00 67.05           N  
-ATOM   5243  CA  THR C 730      29.102  45.112  26.411  1.00 67.15           C  
-ATOM   5244  C   THR C 730      28.291  44.504  25.273  1.00 67.37           C  
-ATOM   5245  O   THR C 730      28.809  44.298  24.177  1.00 67.99           O  
-ATOM   5246  CB  THR C 730      29.732  43.961  27.234  1.00 68.35           C  
-ATOM   5247  OG1 THR C 730      30.523  44.506  28.299  1.00 68.18           O  
-ATOM   5248  CG2 THR C 730      30.621  43.093  26.349  1.00 70.23           C  
-ATOM   5249  N   ASP C 731      27.022  44.212  25.538  1.00 66.81           N  
-ATOM   5250  CA  ASP C 731      26.148  43.630  24.524  1.00 65.76           C  
-ATOM   5251  C   ASP C 731      25.192  44.674  23.954  1.00 64.86           C  
-ATOM   5252  O   ASP C 731      24.331  44.354  23.137  1.00 65.00           O  
-ATOM   5253  CB  ASP C 731      25.340  42.472  25.114  1.00 67.22           C  
-ATOM   5254  CG  ASP C 731      26.221  41.353  25.642  1.00 72.58           C  
-ATOM   5255  OD1 ASP C 731      26.983  41.592  26.604  1.00 78.05           O  
-ATOM   5256  OD2 ASP C 731      26.153  40.234  25.095  1.00 71.48           O  
-ATOM   5257  N   GLY C 732      25.351  45.922  24.385  1.00 64.78           N  
-ATOM   5258  CA  GLY C 732      24.485  46.988  23.907  1.00 64.77           C  
-ATOM   5259  C   GLY C 732      23.019  46.605  23.998  1.00 65.47           C  
-ATOM   5260  O   GLY C 732      22.285  46.695  23.014  1.00 66.07           O  
-ATOM   5261  N   THR C 733      22.596  46.174  25.184  1.00 65.41           N  
-ATOM   5262  CA  THR C 733      21.214  45.757  25.425  1.00 64.28           C  
-ATOM   5263  C   THR C 733      20.487  46.776  26.294  1.00 62.27           C  
-ATOM   5264  O   THR C 733      21.077  47.758  26.751  1.00 62.51           O  
-ATOM   5265  CB  THR C 733      21.151  44.400  26.156  1.00 65.24           C  
-ATOM   5266  OG1 THR C 733      22.337  43.645  25.878  1.00 68.89           O  
-ATOM   5267  CG2 THR C 733      19.932  43.606  25.696  1.00 66.52           C  
-ATOM   5268  N   SER C 734      19.203  46.528  26.530  1.00 61.32           N  
-ATOM   5269  CA  SER C 734      18.388  47.420  27.347  1.00 58.82           C  
-ATOM   5270  C   SER C 734      18.721  47.293  28.832  1.00 55.16           C  
-ATOM   5271  O   SER C 734      18.738  46.190  29.387  1.00 54.25           O  
-ATOM   5272  CB  SER C 734      16.902  47.122  27.135  1.00 60.67           C  
-ATOM   5273  OG  SER C 734      16.101  47.973  27.937  1.00 64.04           O  
-ATOM   5274  N   VAL C 735      18.987  48.430  29.467  1.00 52.46           N  
-ATOM   5275  CA  VAL C 735      19.313  48.469  30.893  1.00 49.69           C  
-ATOM   5276  C   VAL C 735      18.048  48.364  31.738  1.00 47.23           C  
-ATOM   5277  O   VAL C 735      17.958  47.547  32.655  1.00 46.88           O  
-ATOM   5278  CB  VAL C 735      20.023  49.784  31.265  1.00 49.24           C  
-ATOM   5279  CG1 VAL C 735      20.300  49.817  32.759  1.00 49.63           C  
-ATOM   5280  CG2 VAL C 735      21.317  49.917  30.475  1.00 52.37           C  
-ATOM   5281  N   LEU C 736      17.072  49.200  31.411  1.00 45.40           N  
-ATOM   5282  CA  LEU C 736      15.809  49.234  32.127  1.00 44.55           C  
-ATOM   5283  C   LEU C 736      14.844  48.090  31.807  1.00 42.86           C  
-ATOM   5284  O   LEU C 736      13.780  48.309  31.235  1.00 44.15           O  
-ATOM   5285  CB  LEU C 736      15.118  50.575  31.874  1.00 44.28           C  
-ATOM   5286  CG  LEU C 736      15.884  51.812  32.358  1.00 47.92           C  
-ATOM   5287  CD1 LEU C 736      15.068  53.068  32.069  1.00 46.69           C  
-ATOM   5288  CD2 LEU C 736      16.164  51.694  33.858  1.00 47.07           C  
-ATOM   5289  N   THR C 737      15.214  46.873  32.185  1.00 42.05           N  
-ATOM   5290  CA  THR C 737      14.355  45.710  31.965  1.00 39.42           C  
-ATOM   5291  C   THR C 737      13.528  45.452  33.228  1.00 39.94           C  
-ATOM   5292  O   THR C 737      13.872  45.920  34.315  1.00 36.72           O  
-ATOM   5293  CB  THR C 737      15.177  44.444  31.683  1.00 37.65           C  
-ATOM   5294  OG1 THR C 737      15.967  44.125  32.835  1.00 39.94           O  
-ATOM   5295  CG2 THR C 737      16.093  44.654  30.480  1.00 38.64           C  
-ATOM   5296  N   PRO C 738      12.422  44.701  33.101  1.00 41.79           N  
-ATOM   5297  CA  PRO C 738      11.610  44.432  34.291  1.00 41.29           C  
-ATOM   5298  C   PRO C 738      12.451  43.852  35.422  1.00 40.40           C  
-ATOM   5299  O   PRO C 738      12.218  44.153  36.595  1.00 38.75           O  
-ATOM   5300  CB  PRO C 738      10.545  43.455  33.776  1.00 41.85           C  
-ATOM   5301  CG  PRO C 738      11.204  42.816  32.568  1.00 44.41           C  
-ATOM   5302  CD  PRO C 738      11.879  43.996  31.926  1.00 40.93           C  
-ATOM   5303  N   TRP C 739      13.429  43.023  35.066  1.00 39.79           N  
-ATOM   5304  CA  TRP C 739      14.306  42.411  36.059  1.00 37.64           C  
-ATOM   5305  C   TRP C 739      15.103  43.502  36.764  1.00 37.94           C  
-ATOM   5306  O   TRP C 739      15.237  43.496  37.988  1.00 38.15           O  
-ATOM   5307  CB  TRP C 739      15.278  41.424  35.403  1.00 36.80           C  
-ATOM   5308  CG  TRP C 739      16.165  40.732  36.394  1.00 38.27           C  
-ATOM   5309  CD1 TRP C 739      15.897  39.574  37.066  1.00 38.27           C  
-ATOM   5310  CD2 TRP C 739      17.429  41.199  36.890  1.00 34.65           C  
-ATOM   5311  NE1 TRP C 739      16.912  39.292  37.951  1.00 38.09           N  
-ATOM   5312  CE2 TRP C 739      17.864  40.275  37.862  1.00 35.63           C  
-ATOM   5313  CE3 TRP C 739      18.232  42.313  36.608  1.00 40.54           C  
-ATOM   5314  CZ2 TRP C 739      19.069  40.429  38.560  1.00 37.62           C  
-ATOM   5315  CZ3 TRP C 739      19.432  42.468  37.304  1.00 39.11           C  
-ATOM   5316  CH2 TRP C 739      19.836  41.529  38.267  1.00 36.19           C  
-ATOM   5317  N   TYR C 740      15.626  44.444  35.985  1.00 37.31           N  
-ATOM   5318  CA  TYR C 740      16.419  45.528  36.550  1.00 37.32           C  
-ATOM   5319  C   TYR C 740      15.586  46.445  37.445  1.00 36.57           C  
-ATOM   5320  O   TYR C 740      16.040  46.846  38.520  1.00 35.71           O  
-ATOM   5321  CB  TYR C 740      17.061  46.366  35.442  1.00 28.84           C  
-ATOM   5322  CG  TYR C 740      17.804  47.569  35.978  1.00 31.19           C  
-ATOM   5323  CD1 TYR C 740      19.043  47.427  36.604  1.00 33.29           C  
-ATOM   5324  CD2 TYR C 740      17.239  48.845  35.918  1.00 33.88           C  
-ATOM   5325  CE1 TYR C 740      19.705  48.530  37.160  1.00 31.98           C  
-ATOM   5326  CE2 TYR C 740      17.884  49.947  36.472  1.00 34.76           C  
-ATOM   5327  CZ  TYR C 740      19.117  49.785  37.092  1.00 37.72           C  
-ATOM   5328  OH  TYR C 740      19.755  50.876  37.648  1.00 37.51           O  
-ATOM   5329  N   LYS C 741      14.382  46.784  36.990  1.00 35.21           N  
-ATOM   5330  CA  LYS C 741      13.494  47.658  37.749  1.00 35.27           C  
-ATOM   5331  C   LYS C 741      13.294  47.088  39.149  1.00 34.59           C  
-ATOM   5332  O   LYS C 741      13.375  47.806  40.140  1.00 33.96           O  
-ATOM   5333  CB  LYS C 741      12.140  47.793  37.045  1.00 38.79           C  
-ATOM   5334  CG  LYS C 741      11.297  48.973  37.545  1.00 42.28           C  
-ATOM   5335  CD  LYS C 741       9.997  49.113  36.758  1.00 47.86           C  
-ATOM   5336  CE  LYS C 741       8.863  48.326  37.398  1.00 46.99           C  
-ATOM   5337  NZ  LYS C 741       8.556  48.857  38.760  1.00 44.13           N  
-ATOM   5338  N   ASN C 742      13.039  45.787  39.220  1.00 33.61           N  
-ATOM   5339  CA  ASN C 742      12.853  45.128  40.500  1.00 35.12           C  
-ATOM   5340  C   ASN C 742      14.151  45.133  41.321  1.00 34.84           C  
-ATOM   5341  O   ASN C 742      14.173  45.600  42.465  1.00 35.84           O  
-ATOM   5342  CB  ASN C 742      12.402  43.679  40.299  1.00 32.48           C  
-ATOM   5343  CG  ASN C 742      12.261  42.925  41.618  1.00 40.31           C  
-ATOM   5344  OD1 ASN C 742      11.393  43.235  42.444  1.00 39.32           O  
-ATOM   5345  ND2 ASN C 742      13.128  41.940  41.829  1.00 39.11           N  
-ATOM   5346  N   CYS C 743      15.231  44.625  40.735  1.00 33.41           N  
-ATOM   5347  CA  CYS C 743      16.488  44.557  41.459  1.00 32.03           C  
-ATOM   5348  C   CYS C 743      16.897  45.894  42.064  1.00 29.68           C  
-ATOM   5349  O   CYS C 743      17.138  45.990  43.265  1.00 28.17           O  
-ATOM   5350  CB  CYS C 743      17.607  44.039  40.560  1.00 35.88           C  
-ATOM   5351  SG  CYS C 743      19.014  43.449  41.530  1.00 40.52           S  
-ATOM   5352  N   ILE C 744      16.952  46.929  41.237  1.00 27.00           N  
-ATOM   5353  CA  ILE C 744      17.341  48.245  41.715  1.00 29.38           C  
-ATOM   5354  C   ILE C 744      16.357  48.811  42.741  1.00 30.87           C  
-ATOM   5355  O   ILE C 744      16.758  49.529  43.653  1.00 30.33           O  
-ATOM   5356  CB  ILE C 744      17.480  49.246  40.541  1.00 33.03           C  
-ATOM   5357  CG1 ILE C 744      18.223  50.499  41.009  1.00 34.39           C  
-ATOM   5358  CG2 ILE C 744      16.100  49.616  39.991  1.00 30.99           C  
-ATOM   5359  CD1 ILE C 744      19.660  50.245  41.396  1.00 30.63           C  
-ATOM   5360  N   GLU C 745      15.073  48.489  42.600  1.00 30.98           N  
-ATOM   5361  CA  GLU C 745      14.091  49.014  43.539  1.00 29.66           C  
-ATOM   5362  C   GLU C 745      14.082  48.215  44.837  1.00 26.74           C  
-ATOM   5363  O   GLU C 745      13.732  48.745  45.883  1.00 25.43           O  
-ATOM   5364  CB  GLU C 745      12.699  49.093  42.878  1.00 27.12           C  
-ATOM   5365  CG  GLU C 745      12.507  50.401  42.099  1.00 32.88           C  
-ATOM   5366  CD  GLU C 745      11.331  50.386  41.131  1.00 33.85           C  
-ATOM   5367  OE1 GLU C 745      10.378  49.596  41.322  1.00 33.43           O  
-ATOM   5368  OE2 GLU C 745      11.360  51.187  40.176  1.00 41.40           O  
-ATOM   5369  N   ARG C 746      14.491  46.948  44.772  1.00 27.73           N  
-ATOM   5370  CA  ARG C 746      14.579  46.107  45.969  1.00 27.63           C  
-ATOM   5371  C   ARG C 746      15.781  46.548  46.814  1.00 29.51           C  
-ATOM   5372  O   ARG C 746      15.790  46.382  48.035  1.00 29.45           O  
-ATOM   5373  CB  ARG C 746      14.720  44.627  45.601  1.00 28.61           C  
-ATOM   5374  CG  ARG C 746      13.476  44.014  44.954  1.00 30.01           C  
-ATOM   5375  CD  ARG C 746      12.221  44.197  45.825  1.00 32.00           C  
-ATOM   5376  NE  ARG C 746      11.045  43.532  45.261  1.00 31.26           N  
-ATOM   5377  CZ  ARG C 746       9.855  43.492  45.853  1.00 34.67           C  
-ATOM   5378  NH1 ARG C 746       9.679  44.082  47.026  1.00 31.25           N  
-ATOM   5379  NH2 ARG C 746       8.840  42.854  45.284  1.00 36.51           N  
-ATOM   5380  N   LEU C 747      16.791  47.113  46.153  1.00 29.20           N  
-ATOM   5381  CA  LEU C 747      17.976  47.603  46.855  1.00 25.83           C  
-ATOM   5382  C   LEU C 747      17.516  48.867  47.563  1.00 26.06           C  
-ATOM   5383  O   LEU C 747      17.798  49.075  48.750  1.00 24.31           O  
-ATOM   5384  CB  LEU C 747      19.099  47.951  45.874  1.00 23.25           C  
-ATOM   5385  CG  LEU C 747      20.271  48.699  46.525  1.00 24.62           C  
-ATOM   5386  CD1 LEU C 747      20.807  47.871  47.698  1.00 19.59           C  
-ATOM   5387  CD2 LEU C 747      21.383  48.935  45.500  1.00 27.03           C  
-ATOM   5388  N   GLN C 748      16.813  49.710  46.810  1.00 21.85           N  
-ATOM   5389  CA  GLN C 748      16.262  50.943  47.347  1.00 24.94           C  
-ATOM   5390  C   GLN C 748      15.402  50.612  48.573  1.00 24.24           C  
-ATOM   5391  O   GLN C 748      15.480  51.291  49.594  1.00 23.32           O  
-ATOM   5392  CB  GLN C 748      15.409  51.642  46.278  1.00 24.95           C  
-ATOM   5393  CG  GLN C 748      14.491  52.768  46.792  1.00 26.13           C  
-ATOM   5394  CD  GLN C 748      13.499  53.222  45.730  1.00 30.62           C  
-ATOM   5395  OE1 GLN C 748      13.244  52.495  44.766  1.00 24.19           O  
-ATOM   5396  NE2 GLN C 748      12.931  54.413  45.903  1.00 30.18           N  
-ATOM   5397  N   GLN C 749      14.594  49.556  48.464  1.00 26.18           N  
-ATOM   5398  CA  GLN C 749      13.710  49.146  49.550  1.00 28.26           C  
-ATOM   5399  C   GLN C 749      14.464  48.779  50.833  1.00 29.37           C  
-ATOM   5400  O   GLN C 749      13.960  49.010  51.933  1.00 29.09           O  
-ATOM   5401  CB  GLN C 749      12.833  47.966  49.104  1.00 29.61           C  
-ATOM   5402  CG  GLN C 749      11.896  47.423  50.188  1.00 30.09           C  
-ATOM   5403  CD  GLN C 749      10.941  46.360  49.663  1.00 30.74           C  
-ATOM   5404  OE1 GLN C 749      11.351  45.410  48.994  1.00 30.57           O  
-ATOM   5405  NE2 GLN C 749       9.658  46.515  49.967  1.00 30.67           N  
-ATOM   5406  N   ILE C 750      15.656  48.202  50.702  1.00 28.83           N  
-ATOM   5407  CA  ILE C 750      16.428  47.837  51.890  1.00 27.48           C  
-ATOM   5408  C   ILE C 750      16.731  49.110  52.673  1.00 26.48           C  
-ATOM   5409  O   ILE C 750      16.543  49.168  53.893  1.00 25.19           O  
-ATOM   5410  CB  ILE C 750      17.768  47.148  51.513  1.00 30.46           C  
-ATOM   5411  CG1 ILE C 750      17.489  45.826  50.795  1.00 31.35           C  
-ATOM   5412  CG2 ILE C 750      18.613  46.897  52.767  1.00 22.86           C  
-ATOM   5413  CD1 ILE C 750      16.762  44.807  51.660  1.00 31.34           C  
-ATOM   5414  N   PHE C 751      17.195  50.135  51.964  1.00 24.47           N  
-ATOM   5415  CA  PHE C 751      17.525  51.401  52.596  1.00 26.08           C  
-ATOM   5416  C   PHE C 751      16.290  52.055  53.216  1.00 28.37           C  
-ATOM   5417  O   PHE C 751      16.326  52.534  54.353  1.00 25.04           O  
-ATOM   5418  CB  PHE C 751      18.121  52.371  51.572  1.00 29.30           C  
-ATOM   5419  CG  PHE C 751      19.551  52.093  51.213  1.00 30.73           C  
-ATOM   5420  CD1 PHE C 751      20.575  52.352  52.124  1.00 31.49           C  
-ATOM   5421  CD2 PHE C 751      19.879  51.639  49.938  1.00 29.86           C  
-ATOM   5422  CE1 PHE C 751      21.908  52.172  51.772  1.00 29.63           C  
-ATOM   5423  CE2 PHE C 751      21.202  51.456  49.569  1.00 34.59           C  
-ATOM   5424  CZ  PHE C 751      22.226  51.725  50.492  1.00 33.50           C  
-ATOM   5425  N   LEU C 752      15.205  52.093  52.449  1.00 28.29           N  
-ATOM   5426  CA  LEU C 752      13.975  52.709  52.926  1.00 29.11           C  
-ATOM   5427  C   LEU C 752      13.472  52.010  54.177  1.00 28.67           C  
-ATOM   5428  O   LEU C 752      13.186  52.651  55.186  1.00 29.92           O  
-ATOM   5429  CB  LEU C 752      12.880  52.660  51.853  1.00 27.44           C  
-ATOM   5430  CG  LEU C 752      13.053  53.479  50.568  1.00 28.94           C  
-ATOM   5431  CD1 LEU C 752      11.864  53.209  49.652  1.00 28.78           C  
-ATOM   5432  CD2 LEU C 752      13.161  54.964  50.887  1.00 19.26           C  
-ATOM   5433  N   GLN C 753      13.382  50.689  54.115  1.00 28.69           N  
-ATOM   5434  CA  GLN C 753      12.857  49.939  55.237  1.00 31.21           C  
-ATOM   5435  C   GLN C 753      13.703  49.926  56.506  1.00 32.06           C  
-ATOM   5436  O   GLN C 753      13.165  49.771  57.593  1.00 31.78           O  
-ATOM   5437  CB  GLN C 753      12.533  48.506  54.805  1.00 32.18           C  
-ATOM   5438  CG  GLN C 753      11.946  47.675  55.932  1.00 43.04           C  
-ATOM   5439  CD  GLN C 753      11.249  46.414  55.457  1.00 47.95           C  
-ATOM   5440  OE1 GLN C 753      10.914  45.540  56.268  1.00 47.81           O  
-ATOM   5441  NE2 GLN C 753      11.013  46.313  54.145  1.00 45.92           N  
-ATOM   5442  N   HIS C 754      15.014  50.117  56.382  1.00 32.26           N  
-ATOM   5443  CA  HIS C 754      15.885  50.077  57.554  1.00 31.73           C  
-ATOM   5444  C   HIS C 754      16.821  51.265  57.644  1.00 32.11           C  
-ATOM   5445  O   HIS C 754      17.931  51.145  58.171  1.00 32.98           O  
-ATOM   5446  CB  HIS C 754      16.710  48.791  57.515  1.00 32.26           C  
-ATOM   5447  CG  HIS C 754      15.889  47.558  57.297  1.00 28.59           C  
-ATOM   5448  ND1 HIS C 754      15.128  46.985  58.294  1.00 31.01           N  
-ATOM   5449  CD2 HIS C 754      15.662  46.821  56.183  1.00 28.88           C  
-ATOM   5450  CE1 HIS C 754      14.467  45.951  57.804  1.00 28.95           C  
-ATOM   5451  NE2 HIS C 754      14.772  45.830  56.524  1.00 32.01           N  
-ATOM   5452  N   HIS C 755      16.372  52.420  57.162  1.00 31.63           N  
-ATOM   5453  CA  HIS C 755      17.228  53.598  57.158  1.00 31.23           C  
-ATOM   5454  C   HIS C 755      17.865  53.996  58.484  1.00 33.28           C  
-ATOM   5455  O   HIS C 755      19.045  54.349  58.520  1.00 32.98           O  
-ATOM   5456  CB  HIS C 755      16.501  54.791  56.525  1.00 32.59           C  
-ATOM   5457  CG  HIS C 755      15.280  55.237  57.262  1.00 35.89           C  
-ATOM   5458  ND1 HIS C 755      15.331  56.111  58.327  1.00 38.55           N  
-ATOM   5459  CD2 HIS C 755      13.969  54.956  57.070  1.00 40.41           C  
-ATOM   5460  CE1 HIS C 755      14.105  56.352  58.757  1.00 39.98           C  
-ATOM   5461  NE2 HIS C 755      13.259  55.663  58.010  1.00 41.46           N  
-ATOM   5462  N   GLN C 756      17.116  53.937  59.577  1.00 33.29           N  
-ATOM   5463  CA  GLN C 756      17.696  54.322  60.855  1.00 34.24           C  
-ATOM   5464  C   GLN C 756      18.910  53.467  61.225  1.00 31.65           C  
-ATOM   5465  O   GLN C 756      19.939  53.992  61.634  1.00 32.03           O  
-ATOM   5466  CB  GLN C 756      16.651  54.244  61.964  1.00 39.61           C  
-ATOM   5467  CG  GLN C 756      17.195  54.675  63.306  1.00 43.04           C  
-ATOM   5468  CD  GLN C 756      16.140  55.285  64.201  1.00 51.28           C  
-ATOM   5469  OE1 GLN C 756      16.452  55.790  65.280  1.00 51.53           O  
-ATOM   5470  NE2 GLN C 756      14.882  55.245  63.760  1.00 52.57           N  
-ATOM   5471  N   ILE C 757      18.789  52.151  61.091  1.00 31.27           N  
-ATOM   5472  CA  ILE C 757      19.905  51.257  61.393  1.00 30.77           C  
-ATOM   5473  C   ILE C 757      21.083  51.487  60.440  1.00 31.69           C  
-ATOM   5474  O   ILE C 757      22.224  51.673  60.872  1.00 31.98           O  
-ATOM   5475  CB  ILE C 757      19.473  49.781  61.290  1.00 33.27           C  
-ATOM   5476  CG1 ILE C 757      18.574  49.428  62.479  1.00 34.99           C  
-ATOM   5477  CG2 ILE C 757      20.711  48.863  61.226  1.00 32.72           C  
-ATOM   5478  CD1 ILE C 757      17.771  48.149  62.287  1.00 37.27           C  
-ATOM   5479  N   ILE C 758      20.794  51.483  59.143  1.00 30.20           N  
-ATOM   5480  CA  ILE C 758      21.813  51.656  58.119  1.00 29.38           C  
-ATOM   5481  C   ILE C 758      22.611  52.947  58.234  1.00 31.80           C  
-ATOM   5482  O   ILE C 758      23.774  53.005  57.814  1.00 29.28           O  
-ATOM   5483  CB  ILE C 758      21.181  51.548  56.731  1.00 26.42           C  
-ATOM   5484  CG1 ILE C 758      20.572  50.148  56.588  1.00 21.37           C  
-ATOM   5485  CG2 ILE C 758      22.223  51.842  55.662  1.00 25.87           C  
-ATOM   5486  CD1 ILE C 758      19.657  49.957  55.405  1.00 21.83           C  
-ATOM   5487  N   GLN C 759      21.988  53.973  58.806  1.00 31.98           N  
-ATOM   5488  CA  GLN C 759      22.633  55.270  59.008  1.00 35.11           C  
-ATOM   5489  C   GLN C 759      23.902  55.140  59.859  1.00 34.76           C  
-ATOM   5490  O   GLN C 759      24.821  55.953  59.752  1.00 34.57           O  
-ATOM   5491  CB  GLN C 759      21.668  56.233  59.708  1.00 40.75           C  
-ATOM   5492  CG  GLN C 759      21.021  57.289  58.818  1.00 50.38           C  
-ATOM   5493  CD  GLN C 759      21.636  58.663  59.011  1.00 57.29           C  
-ATOM   5494  OE1 GLN C 759      22.736  58.937  58.531  1.00 58.49           O  
-ATOM   5495  NE2 GLN C 759      20.928  59.534  59.727  1.00 60.55           N  
-ATOM   5496  N   GLN C 760      23.935  54.123  60.712  1.00 33.79           N  
-ATOM   5497  CA  GLN C 760      25.073  53.873  61.592  1.00 35.27           C  
-ATOM   5498  C   GLN C 760      26.276  53.326  60.827  1.00 36.81           C  
-ATOM   5499  O   GLN C 760      27.398  53.285  61.350  1.00 34.95           O  
-ATOM   5500  CB  GLN C 760      24.694  52.843  62.651  1.00 37.07           C  
-ATOM   5501  CG  GLN C 760      23.378  53.091  63.358  1.00 41.73           C  
-ATOM   5502  CD  GLN C 760      23.027  51.950  64.296  1.00 42.61           C  
-ATOM   5503  OE1 GLN C 760      23.103  52.083  65.519  1.00 47.19           O  
-ATOM   5504  NE2 GLN C 760      22.655  50.811  63.723  1.00 43.67           N  
-ATOM   5505  N   TYR C 761      26.024  52.889  59.597  1.00 33.74           N  
-ATOM   5506  CA  TYR C 761      27.052  52.303  58.756  1.00 35.18           C  
-ATOM   5507  C   TYR C 761      27.552  53.262  57.678  1.00 33.63           C  
-ATOM   5508  O   TYR C 761      28.241  52.834  56.761  1.00 34.93           O  
-ATOM   5509  CB  TYR C 761      26.492  51.051  58.061  1.00 34.92           C  
-ATOM   5510  CG  TYR C 761      25.764  50.066  58.963  1.00 34.49           C  
-ATOM   5511  CD1 TYR C 761      24.769  49.226  58.444  1.00 34.38           C  
-ATOM   5512  CD2 TYR C 761      26.084  49.947  60.314  1.00 34.18           C  
-ATOM   5513  CE1 TYR C 761      24.112  48.292  59.245  1.00 26.62           C  
-ATOM   5514  CE2 TYR C 761      25.435  49.013  61.131  1.00 30.60           C  
-ATOM   5515  CZ  TYR C 761      24.450  48.188  60.586  1.00 34.18           C  
-ATOM   5516  OH  TYR C 761      23.810  47.257  61.376  1.00 26.75           O  
-ATOM   5517  N   MET C 762      27.211  54.545  57.777  1.00 33.18           N  
-ATOM   5518  CA  MET C 762      27.610  55.522  56.765  1.00 33.13           C  
-ATOM   5519  C   MET C 762      29.086  55.542  56.332  1.00 32.97           C  
-ATOM   5520  O   MET C 762      29.380  55.541  55.136  1.00 31.85           O  
-ATOM   5521  CB  MET C 762      27.199  56.933  57.201  1.00 38.67           C  
-ATOM   5522  CG  MET C 762      25.721  57.263  56.967  1.00 47.34           C  
-ATOM   5523  SD  MET C 762      25.237  57.087  55.220  1.00 54.61           S  
-ATOM   5524  CE  MET C 762      26.395  58.168  54.467  1.00 38.87           C  
-ATOM   5525  N   VAL C 763      30.001  55.577  57.295  1.00 32.49           N  
-ATOM   5526  CA  VAL C 763      31.431  55.619  56.991  1.00 33.44           C  
-ATOM   5527  C   VAL C 763      31.875  54.359  56.259  1.00 32.06           C  
-ATOM   5528  O   VAL C 763      32.478  54.427  55.190  1.00 34.37           O  
-ATOM   5529  CB  VAL C 763      32.251  55.805  58.287  1.00 35.28           C  
-ATOM   5530  CG1 VAL C 763      33.756  55.707  58.003  1.00 32.74           C  
-ATOM   5531  CG2 VAL C 763      31.916  57.168  58.890  1.00 34.26           C  
-ATOM   5532  N   THR C 764      31.555  53.209  56.832  1.00 32.55           N  
-ATOM   5533  CA  THR C 764      31.903  51.936  56.222  1.00 32.47           C  
-ATOM   5534  C   THR C 764      31.344  51.806  54.803  1.00 32.68           C  
-ATOM   5535  O   THR C 764      32.003  51.255  53.920  1.00 30.65           O  
-ATOM   5536  CB  THR C 764      31.377  50.773  57.063  1.00 33.02           C  
-ATOM   5537  OG1 THR C 764      32.006  50.800  58.353  1.00 35.61           O  
-ATOM   5538  CG2 THR C 764      31.668  49.439  56.383  1.00 28.60           C  
-ATOM   5539  N   LEU C 765      30.135  52.312  54.581  1.00 30.15           N  
-ATOM   5540  CA  LEU C 765      29.522  52.209  53.260  1.00 30.06           C  
-ATOM   5541  C   LEU C 765      30.158  53.124  52.223  1.00 29.28           C  
-ATOM   5542  O   LEU C 765      30.363  52.715  51.082  1.00 30.58           O  
-ATOM   5543  CB  LEU C 765      28.009  52.485  53.342  1.00 30.79           C  
-ATOM   5544  CG  LEU C 765      27.155  51.459  54.104  1.00 30.04           C  
-ATOM   5545  CD1 LEU C 765      25.696  51.917  54.099  1.00 30.99           C  
-ATOM   5546  CD2 LEU C 765      27.284  50.073  53.461  1.00 26.07           C  
-ATOM   5547  N   GLU C 766      30.460  54.359  52.611  1.00 29.36           N  
-ATOM   5548  CA  GLU C 766      31.070  55.315  51.690  1.00 33.56           C  
-ATOM   5549  C   GLU C 766      32.507  54.939  51.341  1.00 34.57           C  
-ATOM   5550  O   GLU C 766      32.966  55.199  50.229  1.00 36.51           O  
-ATOM   5551  CB  GLU C 766      31.075  56.720  52.293  1.00 37.60           C  
-ATOM   5552  CG  GLU C 766      29.707  57.245  52.650  1.00 46.16           C  
-ATOM   5553  CD  GLU C 766      29.761  58.637  53.228  1.00 51.26           C  
-ATOM   5554  OE1 GLU C 766      30.597  58.864  54.128  1.00 52.09           O  
-ATOM   5555  OE2 GLU C 766      28.968  59.497  52.784  1.00 56.63           O  
-ATOM   5556  N   ASN C 767      33.207  54.327  52.291  1.00 34.47           N  
-ATOM   5557  CA  ASN C 767      34.594  53.927  52.085  1.00 32.94           C  
-ATOM   5558  C   ASN C 767      34.780  52.571  51.405  1.00 32.68           C  
-ATOM   5559  O   ASN C 767      35.623  52.439  50.523  1.00 33.21           O  
-ATOM   5560  CB  ASN C 767      35.348  53.892  53.420  1.00 27.68           C  
-ATOM   5561  CG  ASN C 767      35.657  55.267  53.960  1.00 29.55           C  
-ATOM   5562  OD1 ASN C 767      35.773  56.238  53.214  1.00 41.12           O  
-ATOM   5563  ND2 ASN C 767      35.824  55.353  55.274  1.00 41.72           N  
-ATOM   5564  N   LEU C 768      33.995  51.569  51.800  1.00 30.70           N  
-ATOM   5565  CA  LEU C 768      34.172  50.230  51.250  1.00 31.57           C  
-ATOM   5566  C   LEU C 768      33.207  49.683  50.183  1.00 34.43           C  
-ATOM   5567  O   LEU C 768      33.625  48.885  49.338  1.00 32.76           O  
-ATOM   5568  CB  LEU C 768      34.268  49.230  52.417  1.00 28.83           C  
-ATOM   5569  CG  LEU C 768      35.318  49.576  53.499  1.00 27.79           C  
-ATOM   5570  CD1 LEU C 768      35.343  48.511  54.594  1.00 23.74           C  
-ATOM   5571  CD2 LEU C 768      36.699  49.702  52.857  1.00 24.30           C  
-ATOM   5572  N   LEU C 769      31.937  50.094  50.194  1.00 34.44           N  
-ATOM   5573  CA  LEU C 769      30.989  49.548  49.213  1.00 35.85           C  
-ATOM   5574  C   LEU C 769      30.437  50.504  48.156  1.00 35.57           C  
-ATOM   5575  O   LEU C 769      30.600  50.271  46.957  1.00 36.61           O  
-ATOM   5576  CB  LEU C 769      29.811  48.875  49.934  1.00 34.94           C  
-ATOM   5577  CG  LEU C 769      30.105  47.645  50.801  1.00 35.64           C  
-ATOM   5578  CD1 LEU C 769      28.791  47.067  51.307  1.00 30.30           C  
-ATOM   5579  CD2 LEU C 769      30.869  46.593  49.995  1.00 30.98           C  
-ATOM   5580  N   PHE C 770      29.764  51.563  48.587  1.00 34.57           N  
-ATOM   5581  CA  PHE C 770      29.199  52.514  47.636  1.00 32.77           C  
-ATOM   5582  C   PHE C 770      30.149  53.677  47.385  1.00 34.00           C  
-ATOM   5583  O   PHE C 770      29.943  54.799  47.861  1.00 30.81           O  
-ATOM   5584  CB  PHE C 770      27.835  53.010  48.132  1.00 29.18           C  
-ATOM   5585  CG  PHE C 770      26.798  51.920  48.214  1.00 27.15           C  
-ATOM   5586  CD1 PHE C 770      26.604  51.217  49.398  1.00 20.56           C  
-ATOM   5587  CD2 PHE C 770      26.024  51.587  47.096  1.00 25.94           C  
-ATOM   5588  CE1 PHE C 770      25.652  50.198  49.480  1.00 24.93           C  
-ATOM   5589  CE2 PHE C 770      25.069  50.573  47.162  1.00 25.60           C  
-ATOM   5590  CZ  PHE C 770      24.883  49.873  48.366  1.00 25.79           C  
-ATOM   5591  N   THR C 771      31.185  53.379  46.604  1.00 35.84           N  
-ATOM   5592  CA  THR C 771      32.236  54.327  46.258  1.00 38.93           C  
-ATOM   5593  C   THR C 771      32.029  54.898  44.860  1.00 41.33           C  
-ATOM   5594  O   THR C 771      31.173  54.429  44.106  1.00 41.40           O  
-ATOM   5595  CB  THR C 771      33.612  53.633  46.295  1.00 39.02           C  
-ATOM   5596  OG1 THR C 771      33.675  52.652  45.253  1.00 38.82           O  
-ATOM   5597  CG2 THR C 771      33.817  52.924  47.633  1.00 34.72           C  
-ATOM   5598  N   ALA C 772      32.835  55.900  44.513  1.00 42.90           N  
-ATOM   5599  CA  ALA C 772      32.746  56.539  43.204  1.00 43.09           C  
-ATOM   5600  C   ALA C 772      33.062  55.583  42.062  1.00 42.71           C  
-ATOM   5601  O   ALA C 772      32.913  55.935  40.901  1.00 45.78           O  
-ATOM   5602  CB  ALA C 772      33.675  57.742  43.145  1.00 44.39           C  
-ATOM   5603  N   GLU C 773      33.491  54.371  42.383  1.00 42.71           N  
-ATOM   5604  CA  GLU C 773      33.810  53.394  41.346  1.00 42.93           C  
-ATOM   5605  C   GLU C 773      32.572  52.679  40.806  1.00 42.40           C  
-ATOM   5606  O   GLU C 773      32.586  52.150  39.693  1.00 41.27           O  
-ATOM   5607  CB  GLU C 773      34.783  52.341  41.886  1.00 45.80           C  
-ATOM   5608  CG  GLU C 773      36.157  52.871  42.246  1.00 51.89           C  
-ATOM   5609  CD  GLU C 773      37.076  51.778  42.758  1.00 58.45           C  
-ATOM   5610  OE1 GLU C 773      38.277  52.058  42.976  1.00 58.46           O  
-ATOM   5611  OE2 GLU C 773      36.593  50.640  42.946  1.00 59.07           O  
-ATOM   5612  N   LEU C 774      31.509  52.645  41.601  1.00 40.16           N  
-ATOM   5613  CA  LEU C 774      30.289  51.971  41.174  1.00 40.61           C  
-ATOM   5614  C   LEU C 774      29.600  52.662  40.011  1.00 38.08           C  
-ATOM   5615  O   LEU C 774      29.701  53.876  39.836  1.00 38.88           O  
-ATOM   5616  CB  LEU C 774      29.292  51.861  42.334  1.00 42.70           C  
-ATOM   5617  CG  LEU C 774      29.689  50.938  43.479  1.00 45.72           C  
-ATOM   5618  CD1 LEU C 774      28.521  50.820  44.446  1.00 45.72           C  
-ATOM   5619  CD2 LEU C 774      30.076  49.573  42.924  1.00 49.58           C  
-ATOM   5620  N   ASP C 775      28.919  51.867  39.198  1.00 38.13           N  
-ATOM   5621  CA  ASP C 775      28.161  52.412  38.084  1.00 38.67           C  
-ATOM   5622  C   ASP C 775      27.200  53.419  38.743  1.00 37.78           C  
-ATOM   5623  O   ASP C 775      26.543  53.099  39.723  1.00 36.52           O  
-ATOM   5624  CB  ASP C 775      27.386  51.284  37.393  1.00 39.95           C  
-ATOM   5625  CG  ASP C 775      26.548  51.777  36.229  1.00 43.20           C  
-ATOM   5626  OD1 ASP C 775      25.607  52.571  36.453  1.00 40.09           O  
-ATOM   5627  OD2 ASP C 775      26.837  51.367  35.088  1.00 49.97           O  
-ATOM   5628  N   PRO C 776      27.130  54.651  38.221  1.00 38.02           N  
-ATOM   5629  CA  PRO C 776      26.247  55.675  38.789  1.00 38.54           C  
-ATOM   5630  C   PRO C 776      24.807  55.239  39.089  1.00 39.57           C  
-ATOM   5631  O   PRO C 776      24.147  55.820  39.948  1.00 40.25           O  
-ATOM   5632  CB  PRO C 776      26.327  56.816  37.767  1.00 38.13           C  
-ATOM   5633  CG  PRO C 776      26.801  56.134  36.499  1.00 41.10           C  
-ATOM   5634  CD  PRO C 776      27.797  55.145  37.006  1.00 37.97           C  
-ATOM   5635  N   HIS C 777      24.333  54.216  38.389  1.00 40.01           N  
-ATOM   5636  CA  HIS C 777      22.984  53.696  38.591  1.00 40.21           C  
-ATOM   5637  C   HIS C 777      22.841  53.159  40.015  1.00 39.19           C  
-ATOM   5638  O   HIS C 777      21.849  53.426  40.693  1.00 37.51           O  
-ATOM   5639  CB  HIS C 777      22.701  52.566  37.596  1.00 40.08           C  
-ATOM   5640  CG  HIS C 777      22.392  53.038  36.210  1.00 51.20           C  
-ATOM   5641  ND1 HIS C 777      22.642  52.272  35.091  1.00 55.67           N  
-ATOM   5642  CD2 HIS C 777      21.810  54.176  35.763  1.00 56.28           C  
-ATOM   5643  CE1 HIS C 777      22.227  52.917  34.015  1.00 57.84           C  
-ATOM   5644  NE2 HIS C 777      21.718  54.075  34.395  1.00 59.51           N  
-ATOM   5645  N   ILE C 778      23.851  52.408  40.452  1.00 38.32           N  
-ATOM   5646  CA  ILE C 778      23.875  51.806  41.775  1.00 36.42           C  
-ATOM   5647  C   ILE C 778      24.202  52.865  42.805  1.00 37.99           C  
-ATOM   5648  O   ILE C 778      23.501  53.018  43.805  1.00 38.76           O  
-ATOM   5649  CB  ILE C 778      24.937  50.695  41.850  1.00 36.71           C  
-ATOM   5650  CG1 ILE C 778      24.690  49.666  40.743  1.00 33.20           C  
-ATOM   5651  CG2 ILE C 778      24.893  50.012  43.211  1.00 34.80           C  
-ATOM   5652  CD1 ILE C 778      25.753  48.587  40.662  1.00 34.91           C  
-ATOM   5653  N   LEU C 779      25.268  53.611  42.543  1.00 38.08           N  
-ATOM   5654  CA  LEU C 779      25.714  54.657  43.448  1.00 34.94           C  
-ATOM   5655  C   LEU C 779      24.613  55.668  43.764  1.00 32.66           C  
-ATOM   5656  O   LEU C 779      24.538  56.191  44.873  1.00 30.76           O  
-ATOM   5657  CB  LEU C 779      26.906  55.387  42.846  1.00 35.39           C  
-ATOM   5658  CG  LEU C 779      27.522  56.481  43.716  1.00 40.18           C  
-ATOM   5659  CD1 LEU C 779      28.039  55.865  45.020  1.00 39.47           C  
-ATOM   5660  CD2 LEU C 779      28.656  57.163  42.950  1.00 39.28           C  
-ATOM   5661  N   ALA C 780      23.765  55.950  42.785  1.00 30.96           N  
-ATOM   5662  CA  ALA C 780      22.688  56.917  42.990  1.00 30.79           C  
-ATOM   5663  C   ALA C 780      21.735  56.493  44.112  1.00 28.39           C  
-ATOM   5664  O   ALA C 780      21.231  57.333  44.850  1.00 29.68           O  
-ATOM   5665  CB  ALA C 780      21.914  57.123  41.691  1.00 31.01           C  
-ATOM   5666  N   VAL C 781      21.487  55.193  44.236  1.00 29.40           N  
-ATOM   5667  CA  VAL C 781      20.594  54.696  45.279  1.00 29.98           C  
-ATOM   5668  C   VAL C 781      21.159  55.025  46.662  1.00 31.15           C  
-ATOM   5669  O   VAL C 781      20.413  55.396  47.566  1.00 31.86           O  
-ATOM   5670  CB  VAL C 781      20.373  53.175  45.139  1.00 32.63           C  
-ATOM   5671  CG1 VAL C 781      19.419  52.672  46.230  1.00 29.84           C  
-ATOM   5672  CG2 VAL C 781      19.802  52.867  43.759  1.00 29.07           C  
-ATOM   5673  N   PHE C 782      22.476  54.904  46.820  1.00 30.63           N  
-ATOM   5674  CA  PHE C 782      23.124  55.219  48.091  1.00 30.57           C  
-ATOM   5675  C   PHE C 782      23.117  56.724  48.348  1.00 30.10           C  
-ATOM   5676  O   PHE C 782      22.911  57.173  49.480  1.00 30.20           O  
-ATOM   5677  CB  PHE C 782      24.578  54.719  48.100  1.00 32.36           C  
-ATOM   5678  CG  PHE C 782      25.346  55.110  49.338  1.00 28.55           C  
-ATOM   5679  CD1 PHE C 782      25.017  54.568  50.586  1.00 30.20           C  
-ATOM   5680  CD2 PHE C 782      26.377  56.044  49.262  1.00 28.22           C  
-ATOM   5681  CE1 PHE C 782      25.703  54.959  51.741  1.00 28.65           C  
-ATOM   5682  CE2 PHE C 782      27.072  56.442  50.405  1.00 27.23           C  
-ATOM   5683  CZ  PHE C 782      26.734  55.901  51.649  1.00 31.86           C  
-ATOM   5684  N   GLN C 783      23.351  57.510  47.302  1.00 29.14           N  
-ATOM   5685  CA  GLN C 783      23.360  58.962  47.458  1.00 31.08           C  
-ATOM   5686  C   GLN C 783      21.960  59.478  47.801  1.00 30.51           C  
-ATOM   5687  O   GLN C 783      21.812  60.475  48.512  1.00 30.85           O  
-ATOM   5688  CB  GLN C 783      23.849  59.643  46.176  1.00 35.30           C  
-ATOM   5689  CG  GLN C 783      25.230  59.199  45.707  1.00 40.42           C  
-ATOM   5690  CD  GLN C 783      25.539  59.690  44.304  1.00 47.10           C  
-ATOM   5691  OE1 GLN C 783      24.786  59.426  43.366  1.00 48.07           O  
-ATOM   5692  NE2 GLN C 783      26.645  60.414  44.154  1.00 49.12           N  
-ATOM   5693  N   GLN C 784      20.934  58.813  47.276  1.00 30.24           N  
-ATOM   5694  CA  GLN C 784      19.554  59.212  47.560  1.00 28.94           C  
-ATOM   5695  C   GLN C 784      19.306  58.955  49.043  1.00 26.74           C  
-ATOM   5696  O   GLN C 784      18.762  59.797  49.741  1.00 27.87           O  
-ATOM   5697  CB  GLN C 784      18.568  58.395  46.708  1.00 24.32           C  
-ATOM   5698  CG  GLN C 784      18.644  58.716  45.219  1.00 29.44           C  
-ATOM   5699  CD  GLN C 784      18.091  57.601  44.342  1.00 32.10           C  
-ATOM   5700  OE1 GLN C 784      17.585  56.588  44.835  1.00 32.15           O  
-ATOM   5701  NE2 GLN C 784      18.188  57.786  43.032  1.00 33.66           N  
-ATOM   5702  N   PHE C 785      19.725  57.783  49.508  1.00 26.58           N  
-ATOM   5703  CA  PHE C 785      19.559  57.383  50.900  1.00 28.10           C  
-ATOM   5704  C   PHE C 785      20.189  58.400  51.846  1.00 29.37           C  
-ATOM   5705  O   PHE C 785      19.600  58.780  52.856  1.00 31.73           O  
-ATOM   5706  CB  PHE C 785      20.183  55.990  51.124  1.00 28.39           C  
-ATOM   5707  CG  PHE C 785      20.468  55.680  52.564  1.00 33.58           C  
-ATOM   5708  CD1 PHE C 785      19.429  55.547  53.483  1.00 32.43           C  
-ATOM   5709  CD2 PHE C 785      21.785  55.565  53.016  1.00 38.40           C  
-ATOM   5710  CE1 PHE C 785      19.691  55.307  54.834  1.00 35.02           C  
-ATOM   5711  CE2 PHE C 785      22.058  55.325  54.375  1.00 38.73           C  
-ATOM   5712  CZ  PHE C 785      21.005  55.199  55.280  1.00 34.25           C  
-ATOM   5713  N   CYS C 786      21.385  58.854  51.506  1.00 31.07           N  
-ATOM   5714  CA  CYS C 786      22.089  59.828  52.325  1.00 32.30           C  
-ATOM   5715  C   CYS C 786      21.370  61.179  52.340  1.00 32.04           C  
-ATOM   5716  O   CYS C 786      21.409  61.902  53.342  1.00 27.95           O  
-ATOM   5717  CB  CYS C 786      23.519  59.996  51.802  1.00 38.60           C  
-ATOM   5718  SG  CYS C 786      24.665  60.871  52.901  1.00 62.28           S  
-ATOM   5719  N   ALA C 787      20.719  61.530  51.233  1.00 31.13           N  
-ATOM   5720  CA  ALA C 787      20.009  62.809  51.171  1.00 31.62           C  
-ATOM   5721  C   ALA C 787      18.813  62.889  52.134  1.00 30.82           C  
-ATOM   5722  O   ALA C 787      18.318  63.975  52.417  1.00 33.87           O  
-ATOM   5723  CB  ALA C 787      19.539  63.089  49.734  1.00 30.51           C  
-ATOM   5724  N   LEU C 788      18.351  61.751  52.641  1.00 29.62           N  
-ATOM   5725  CA  LEU C 788      17.205  61.745  53.552  1.00 28.74           C  
-ATOM   5726  C   LEU C 788      17.451  62.432  54.889  1.00 30.92           C  
-ATOM   5727  O   LEU C 788      16.490  62.829  55.567  1.00 30.43           O  
-ATOM   5728  CB  LEU C 788      16.743  60.311  53.808  1.00 24.95           C  
-ATOM   5729  CG  LEU C 788      16.263  59.532  52.579  1.00 27.74           C  
-ATOM   5730  CD1 LEU C 788      15.845  58.130  52.999  1.00 24.61           C  
-ATOM   5731  CD2 LEU C 788      15.094  60.267  51.923  1.00 31.62           C  
-ATOM   5732  N   GLN C 789      18.723  62.568  55.274  1.00 30.61           N  
-ATOM   5733  CA  GLN C 789      19.071  63.214  56.539  1.00 33.47           C  
-ATOM   5734  C   GLN C 789      20.251  64.170  56.389  1.00 36.64           C  
-ATOM   5735  O   GLN C 789      20.819  64.638  57.382  1.00 34.50           O  
-ATOM   5736  CB  GLN C 789      19.378  62.158  57.604  1.00 34.60           C  
-ATOM   5737  CG  GLN C 789      18.147  61.368  58.038  1.00 33.96           C  
-ATOM   5738  CD  GLN C 789      17.209  62.195  58.898  1.00 36.05           C  
-ATOM   5739  OE1 GLN C 789      17.345  62.239  60.122  1.00 37.71           O  
-ATOM   5740  NE2 GLN C 789      16.264  62.873  58.260  1.00 29.92           N  
-ATOM   5741  N   ALA C 790      20.615  64.456  55.140  1.00 37.93           N  
-ATOM   5742  CA  ALA C 790      21.716  65.378  54.851  1.00 40.17           C  
-ATOM   5743  C   ALA C 790      21.178  66.808  54.886  1.00 40.56           C  
-ATOM   5744  O   ALA C 790      19.934  66.960  54.866  1.00 41.77           O  
-ATOM   5745  CB  ALA C 790      22.309  65.085  53.466  1.00 36.27           C  
-ATOM   5746  OXT ALA C 790      21.994  67.756  54.914  1.00 41.52           O  
-TER    5747      ALA C 790                                                      
-ATOM   5748  N   LEU Z   5      -0.639  64.348  76.796  1.00 58.08           N  
-ATOM   5749  CA  LEU Z   5      -1.606  63.224  76.619  1.00 59.39           C  
-ATOM   5750  C   LEU Z   5      -3.061  63.627  76.874  1.00 58.33           C  
-ATOM   5751  O   LEU Z   5      -3.359  64.349  77.826  1.00 58.07           O  
-ATOM   5752  CB  LEU Z   5      -1.236  62.060  77.545  1.00 61.95           C  
-ATOM   5753  CG  LEU Z   5      -0.111  61.120  77.094  1.00 65.67           C  
-ATOM   5754  CD1 LEU Z   5       0.377  60.275  78.265  1.00 63.04           C  
-ATOM   5755  CD2 LEU Z   5      -0.621  60.232  75.969  1.00 64.79           C  
-ATOM   5756  N   LEU Z   6      -3.958  63.151  76.013  1.00 57.14           N  
-ATOM   5757  CA  LEU Z   6      -5.391  63.427  76.130  1.00 56.31           C  
-ATOM   5758  C   LEU Z   6      -6.167  62.115  76.201  1.00 55.15           C  
-ATOM   5759  O   LEU Z   6      -5.919  61.200  75.417  1.00 55.44           O  
-ATOM   5760  CB  LEU Z   6      -5.885  64.254  74.933  1.00 52.95           C  
-ATOM   5761  CG  LEU Z   6      -5.426  65.715  74.891  1.00 52.09           C  
-ATOM   5762  CD1 LEU Z   6      -5.814  66.359  73.567  1.00 47.37           C  
-ATOM   5763  CD2 LEU Z   6      -6.048  66.468  76.058  1.00 49.41           C  
-ATOM   5764  N   LYS Z   7      -7.102  62.032  77.144  1.00 54.47           N  
-ATOM   5765  CA  LYS Z   7      -7.920  60.836  77.330  1.00 54.01           C  
-ATOM   5766  C   LYS Z   7      -8.556  60.351  76.026  1.00 53.04           C  
-ATOM   5767  O   LYS Z   7      -8.589  59.149  75.752  1.00 52.71           O  
-ATOM   5768  CB  LYS Z   7      -9.022  61.112  78.361  1.00 56.37           C  
-ATOM   5769  CG  LYS Z   7     -10.043  59.991  78.491  1.00 60.68           C  
-ATOM   5770  CD  LYS Z   7     -11.251  60.443  79.290  1.00 65.07           C  
-ATOM   5771  CE  LYS Z   7     -12.333  59.377  79.317  1.00 68.43           C  
-ATOM   5772  NZ  LYS Z   7     -13.575  59.864  79.994  1.00 71.77           N  
-ATOM   5773  N   ALA Z   8      -9.051  61.293  75.226  1.00 51.14           N  
-ATOM   5774  CA  ALA Z   8      -9.699  60.975  73.956  1.00 48.64           C  
-ATOM   5775  C   ALA Z   8      -8.760  60.283  72.971  1.00 46.33           C  
-ATOM   5776  O   ALA Z   8      -9.163  59.362  72.260  1.00 45.97           O  
-ATOM   5777  CB  ALA Z   8     -10.259  62.248  73.332  1.00 52.27           C  
-ATOM   5778  N   LEU Z   9      -7.510  60.728  72.934  1.00 43.16           N  
-ATOM   5779  CA  LEU Z   9      -6.522  60.151  72.031  1.00 41.87           C  
-ATOM   5780  C   LEU Z   9      -5.991  58.802  72.516  1.00 40.44           C  
-ATOM   5781  O   LEU Z   9      -5.442  58.027  71.737  1.00 39.31           O  
-ATOM   5782  CB  LEU Z   9      -5.358  61.127  71.844  1.00 40.41           C  
-ATOM   5783  CG  LEU Z   9      -5.738  62.486  71.257  1.00 39.78           C  
-ATOM   5784  CD1 LEU Z   9      -4.484  63.326  71.046  1.00 41.17           C  
-ATOM   5785  CD2 LEU Z   9      -6.471  62.280  69.945  1.00 38.53           C  
-ATOM   5786  N   ARG Z  10      -6.163  58.528  73.807  1.00 39.45           N  
-ATOM   5787  CA  ARG Z  10      -5.711  57.268  74.389  1.00 37.73           C  
-ATOM   5788  C   ARG Z  10      -6.713  56.147  74.173  1.00 36.00           C  
-ATOM   5789  O   ARG Z  10      -6.384  54.973  74.354  1.00 35.66           O  
-ATOM   5790  CB  ARG Z  10      -5.465  57.426  75.890  1.00 40.65           C  
-ATOM   5791  CG  ARG Z  10      -4.150  58.087  76.239  1.00 47.00           C  
-ATOM   5792  CD  ARG Z  10      -3.772  57.744  77.671  1.00 54.94           C  
-ATOM   5793  NE  ARG Z  10      -4.729  58.305  78.620  1.00 62.10           N  
-ATOM   5794  CZ  ARG Z  10      -4.831  59.607  78.883  1.00 67.17           C  
-ATOM   5795  NH1 ARG Z  10      -4.029  60.472  78.272  1.00 69.52           N  
-ATOM   5796  NH2 ARG Z  10      -5.741  60.048  79.741  1.00 64.97           N  
-ATOM   5797  N   SER Z  11      -7.930  56.507  73.781  1.00 32.60           N  
-ATOM   5798  CA  SER Z  11      -8.978  55.524  73.560  1.00 31.07           C  
-ATOM   5799  C   SER Z  11      -8.503  54.352  72.696  1.00 31.37           C  
-ATOM   5800  O   SER Z  11      -7.954  54.540  71.601  1.00 27.53           O  
-ATOM   5801  CB  SER Z  11     -10.189  56.210  72.925  1.00 31.22           C  
-ATOM   5802  OG  SER Z  11     -11.271  55.311  72.815  1.00 34.12           O  
-ATOM   5803  N   ASP Z  12      -8.732  53.138  73.193  1.00 30.79           N  
-ATOM   5804  CA  ASP Z  12      -8.304  51.926  72.499  1.00 30.52           C  
-ATOM   5805  C   ASP Z  12      -9.323  50.817  72.802  1.00 30.92           C  
-ATOM   5806  O   ASP Z  12      -8.959  49.752  73.297  1.00 30.04           O  
-ATOM   5807  CB  ASP Z  12      -6.900  51.545  73.017  1.00 31.59           C  
-ATOM   5808  CG  ASP Z  12      -6.105  50.663  72.041  1.00 32.48           C  
-ATOM   5809  OD1 ASP Z  12      -6.570  50.393  70.910  1.00 30.77           O  
-ATOM   5810  OD2 ASP Z  12      -4.988  50.244  72.416  1.00 34.13           O  
-ATOM   5811  N   SER Z  13     -10.594  51.062  72.478  1.00 31.04           N  
-ATOM   5812  CA  SER Z  13     -11.668  50.106  72.764  1.00 31.34           C  
-ATOM   5813  C   SER Z  13     -11.498  48.689  72.215  1.00 32.52           C  
-ATOM   5814  O   SER Z  13     -11.979  47.722  72.825  1.00 29.54           O  
-ATOM   5815  CB  SER Z  13     -13.018  50.670  72.285  1.00 34.96           C  
-ATOM   5816  OG  SER Z  13     -13.159  50.588  70.873  1.00 32.50           O  
-ATOM   5817  N   TYR Z  14     -10.828  48.556  71.074  1.00 29.57           N  
-ATOM   5818  CA  TYR Z  14     -10.652  47.243  70.464  1.00 29.52           C  
-ATOM   5819  C   TYR Z  14      -9.702  46.338  71.230  1.00 29.74           C  
-ATOM   5820  O   TYR Z  14      -9.716  45.119  71.055  1.00 29.56           O  
-ATOM   5821  CB  TYR Z  14     -10.156  47.383  69.019  1.00 31.60           C  
-ATOM   5822  CG  TYR Z  14     -11.217  47.892  68.074  1.00 33.95           C  
-ATOM   5823  CD1 TYR Z  14     -11.659  49.218  68.129  1.00 35.46           C  
-ATOM   5824  CD2 TYR Z  14     -11.824  47.034  67.166  1.00 37.11           C  
-ATOM   5825  CE1 TYR Z  14     -12.684  49.670  67.302  1.00 32.20           C  
-ATOM   5826  CE2 TYR Z  14     -12.846  47.475  66.338  1.00 40.75           C  
-ATOM   5827  CZ  TYR Z  14     -13.271  48.792  66.410  1.00 35.57           C  
-ATOM   5828  OH  TYR Z  14     -14.290  49.215  65.587  1.00 40.46           O  
-ATOM   5829  N   VAL Z  15      -8.893  46.935  72.093  1.00 31.20           N  
-ATOM   5830  CA  VAL Z  15      -7.914  46.191  72.873  1.00 35.19           C  
-ATOM   5831  C   VAL Z  15      -8.421  45.852  74.281  1.00 38.09           C  
-ATOM   5832  O   VAL Z  15      -7.785  45.101  75.024  1.00 37.91           O  
-ATOM   5833  CB  VAL Z  15      -6.591  46.999  72.942  1.00 31.86           C  
-ATOM   5834  CG1 VAL Z  15      -5.582  46.306  73.827  1.00 36.68           C  
-ATOM   5835  CG2 VAL Z  15      -6.024  47.158  71.531  1.00 33.33           C  
-ATOM   5836  N   GLU Z  16      -9.574  46.405  74.643  1.00 39.82           N  
-ATOM   5837  CA  GLU Z  16     -10.153  46.148  75.957  1.00 39.54           C  
-ATOM   5838  C   GLU Z  16     -10.535  44.680  76.117  1.00 38.72           C  
-ATOM   5839  O   GLU Z  16     -10.783  43.973  75.140  1.00 37.30           O  
-ATOM   5840  CB  GLU Z  16     -11.390  47.026  76.178  1.00 42.78           C  
-ATOM   5841  CG  GLU Z  16     -11.070  48.496  76.389  1.00 53.00           C  
-ATOM   5842  CD  GLU Z  16     -12.299  49.317  76.747  1.00 62.95           C  
-ATOM   5843  OE1 GLU Z  16     -12.968  48.987  77.754  1.00 69.94           O  
-ATOM   5844  OE2 GLU Z  16     -12.594  50.293  76.023  1.00 68.85           O  
-ATOM   5845  N   LEU Z  17     -10.581  44.229  77.364  1.00 39.21           N  
-ATOM   5846  CA  LEU Z  17     -10.939  42.850  77.665  1.00 39.64           C  
-ATOM   5847  C   LEU Z  17     -12.421  42.665  77.362  1.00 38.48           C  
-ATOM   5848  O   LEU Z  17     -13.189  43.623  77.422  1.00 38.46           O  
-ATOM   5849  CB  LEU Z  17     -10.676  42.558  79.146  1.00 41.81           C  
-ATOM   5850  CG  LEU Z  17      -9.260  42.856  79.645  1.00 42.89           C  
-ATOM   5851  CD1 LEU Z  17      -9.229  42.800  81.159  1.00 48.71           C  
-ATOM   5852  CD2 LEU Z  17      -8.280  41.868  79.047  1.00 40.95           C  
-ATOM   5853  N   SER Z  18     -12.820  41.447  77.017  1.00 37.72           N  
-ATOM   5854  CA  SER Z  18     -14.224  41.173  76.743  1.00 40.18           C  
-ATOM   5855  C   SER Z  18     -14.821  40.672  78.052  1.00 42.13           C  
-ATOM   5856  O   SER Z  18     -14.163  40.717  79.095  1.00 44.27           O  
-ATOM   5857  CB  SER Z  18     -14.379  40.101  75.656  1.00 37.35           C  
-ATOM   5858  OG  SER Z  18     -14.082  38.805  76.153  1.00 42.71           O  
-ATOM   5859  N   GLN Z  19     -16.062  40.204  78.007  1.00 43.13           N  
-ATOM   5860  CA  GLN Z  19     -16.715  39.698  79.209  1.00 46.24           C  
-ATOM   5861  C   GLN Z  19     -16.467  38.205  79.394  1.00 45.38           C  
-ATOM   5862  O   GLN Z  19     -16.826  37.630  80.421  1.00 46.92           O  
-ATOM   5863  CB  GLN Z  19     -18.227  39.959  79.154  1.00 47.54           C  
-ATOM   5864  CG  GLN Z  19     -18.611  41.436  79.124  1.00 57.12           C  
-ATOM   5865  CD  GLN Z  19     -18.227  42.174  80.394  1.00 65.20           C  
-ATOM   5866  OE1 GLN Z  19     -18.692  41.839  81.486  1.00 71.68           O  
-ATOM   5867  NE2 GLN Z  19     -17.376  43.187  80.257  1.00 66.05           N  
-ATOM   5868  N   TYR Z  20     -15.853  37.574  78.402  1.00 45.52           N  
-ATOM   5869  CA  TYR Z  20     -15.576  36.150  78.490  1.00 46.15           C  
-ATOM   5870  C   TYR Z  20     -14.507  35.834  79.517  1.00 48.24           C  
-ATOM   5871  O   TYR Z  20     -13.543  36.579  79.683  1.00 47.76           O  
-ATOM   5872  CB  TYR Z  20     -15.103  35.597  77.154  1.00 47.00           C  
-ATOM   5873  CG  TYR Z  20     -14.826  34.115  77.209  1.00 46.28           C  
-ATOM   5874  CD1 TYR Z  20     -15.838  33.196  76.952  1.00 45.90           C  
-ATOM   5875  CD2 TYR Z  20     -13.561  33.627  77.549  1.00 42.84           C  
-ATOM   5876  CE1 TYR Z  20     -15.603  31.825  77.027  1.00 45.56           C  
-ATOM   5877  CE2 TYR Z  20     -13.316  32.255  77.632  1.00 40.74           C  
-ATOM   5878  CZ  TYR Z  20     -14.342  31.361  77.365  1.00 41.65           C  
-ATOM   5879  OH  TYR Z  20     -14.119  30.008  77.414  1.00 38.71           O  
-ATOM   5880  N   ARG Z  21     -14.688  34.711  80.199  1.00 49.92           N  
-ATOM   5881  CA  ARG Z  21     -13.724  34.252  81.178  1.00 52.49           C  
-ATOM   5882  C   ARG Z  21     -13.795  32.747  81.321  1.00 54.08           C  
-ATOM   5883  O   ARG Z  21     -14.851  32.185  81.615  1.00 54.69           O  
-ATOM   5884  CB  ARG Z  21     -13.937  34.954  82.516  1.00 50.28           C  
-ATOM   5885  CG  ARG Z  21     -13.080  36.200  82.620  1.00 51.78           C  
-ATOM   5886  CD  ARG Z  21     -13.755  37.277  83.418  1.00 53.25           C  
-ATOM   5887  NE  ARG Z  21     -13.029  38.543  83.367  1.00 50.49           N  
-ATOM   5888  CZ  ARG Z  21     -12.744  39.210  82.253  1.00 48.30           C  
-ATOM   5889  NH1 ARG Z  21     -13.108  38.740  81.062  1.00 36.75           N  
-ATOM   5890  NH2 ARG Z  21     -12.114  40.372  82.339  1.00 47.51           N  
-ATOM   5891  N   ASP Z  22     -12.657  32.104  81.073  1.00 55.73           N  
-ATOM   5892  CA  ASP Z  22     -12.541  30.655  81.155  1.00 58.55           C  
-ATOM   5893  C   ASP Z  22     -13.012  30.200  82.531  1.00 59.67           C  
-ATOM   5894  O   ASP Z  22     -12.416  30.554  83.551  1.00 59.74           O  
-ATOM   5895  CB  ASP Z  22     -11.083  30.230  80.943  1.00 59.59           C  
-ATOM   5896  CG  ASP Z  22     -10.955  28.803  80.436  1.00 60.55           C  
-ATOM   5897  OD1 ASP Z  22     -11.811  27.959  80.774  1.00 59.54           O  
-ATOM   5898  OD2 ASP Z  22      -9.987  28.519  79.702  1.00 62.45           O  
-ATOM   5899  N   GLN Z  23     -14.089  29.424  82.552  1.00 61.38           N  
-ATOM   5900  CA  GLN Z  23     -14.642  28.922  83.803  1.00 63.26           C  
-ATOM   5901  C   GLN Z  23     -13.798  27.766  84.323  1.00 64.50           C  
-ATOM   5902  O   GLN Z  23     -13.812  27.462  85.516  1.00 64.99           O  
-ATOM   5903  CB  GLN Z  23     -16.086  28.464  83.588  1.00 62.78           C  
-ATOM   5904  CG  GLN Z  23     -17.060  29.065  84.581  1.00 64.34           C  
-ATOM   5905  CD  GLN Z  23     -16.853  30.559  84.744  1.00 65.48           C  
-ATOM   5906  OE1 GLN Z  23     -16.841  31.305  83.765  1.00 62.22           O  
-ATOM   5907  NE2 GLN Z  23     -16.684  31.004  85.988  1.00 65.56           N  
-ATOM   5908  N   HIS Z  24     -13.066  27.127  83.414  1.00 65.67           N  
-ATOM   5909  CA  HIS Z  24     -12.199  26.004  83.758  1.00 67.02           C  
-ATOM   5910  C   HIS Z  24     -10.818  26.507  84.159  1.00 67.12           C  
-ATOM   5911  O   HIS Z  24      -9.953  25.723  84.550  1.00 67.23           O  
-ATOM   5912  CB  HIS Z  24     -12.062  25.044  82.571  1.00 68.96           C  
-ATOM   5913  CG  HIS Z  24     -13.319  24.301  82.238  1.00 73.93           C  
-ATOM   5914  ND1 HIS Z  24     -13.434  23.498  81.121  1.00 76.23           N  
-ATOM   5915  CD2 HIS Z  24     -14.508  24.222  82.882  1.00 74.85           C  
-ATOM   5916  CE1 HIS Z  24     -14.639  22.957  81.093  1.00 77.84           C  
-ATOM   5917  NE2 HIS Z  24     -15.311  23.380  82.151  1.00 78.17           N  
-ATOM   5918  N   PHE Z  25     -10.617  27.818  84.050  1.00 67.19           N  
-ATOM   5919  CA  PHE Z  25      -9.342  28.435  84.403  1.00 66.46           C  
-ATOM   5920  C   PHE Z  25      -9.037  28.167  85.868  1.00 67.50           C  
-ATOM   5921  O   PHE Z  25      -9.742  28.648  86.754  1.00 67.60           O  
-ATOM   5922  CB  PHE Z  25      -9.398  29.946  84.169  1.00 62.96           C  
-ATOM   5923  CG  PHE Z  25      -8.130  30.670  84.545  1.00 57.56           C  
-ATOM   5924  CD1 PHE Z  25      -6.989  30.562  83.756  1.00 52.73           C  
-ATOM   5925  CD2 PHE Z  25      -8.082  31.469  85.682  1.00 52.60           C  
-ATOM   5926  CE1 PHE Z  25      -5.822  31.242  84.097  1.00 49.63           C  
-ATOM   5927  CE2 PHE Z  25      -6.916  32.153  86.031  1.00 50.15           C  
-ATOM   5928  CZ  PHE Z  25      -5.787  32.039  85.236  1.00 47.09           C  
-ATOM   5929  N   ARG Z  26      -7.984  27.397  86.113  1.00 68.80           N  
-ATOM   5930  CA  ARG Z  26      -7.574  27.054  87.469  1.00 69.81           C  
-ATOM   5931  C   ARG Z  26      -7.002  28.293  88.150  1.00 68.96           C  
-ATOM   5932  O   ARG Z  26      -5.784  28.444  88.248  1.00 70.41           O  
-ATOM   5933  CB  ARG Z  26      -6.506  25.953  87.431  1.00 72.69           C  
-ATOM   5934  CG  ARG Z  26      -6.737  24.793  88.396  1.00 78.32           C  
-ATOM   5935  CD  ARG Z  26      -7.866  23.887  87.921  1.00 82.64           C  
-ATOM   5936  NE  ARG Z  26      -8.056  22.730  88.795  1.00 87.41           N  
-ATOM   5937  CZ  ARG Z  26      -8.896  21.729  88.538  1.00 90.01           C  
-ATOM   5938  NH1 ARG Z  26      -9.627  21.739  87.430  1.00 90.32           N  
-ATOM   5939  NH2 ARG Z  26      -9.006  20.716  89.388  1.00 91.46           N  
-ATOM   5940  N   GLY Z  27      -7.874  29.180  88.617  1.00 66.98           N  
-ATOM   5941  CA  GLY Z  27      -7.399  30.381  89.276  1.00 65.51           C  
-ATOM   5942  C   GLY Z  27      -8.473  31.428  89.478  1.00 64.63           C  
-ATOM   5943  O   GLY Z  27      -9.591  31.296  88.979  1.00 63.47           O  
-ATOM   5944  N   ASP Z  28      -8.118  32.476  90.212  1.00 64.85           N  
-ATOM   5945  CA  ASP Z  28      -9.029  33.573  90.515  1.00 65.95           C  
-ATOM   5946  C   ASP Z  28      -9.321  34.452  89.292  1.00 66.27           C  
-ATOM   5947  O   ASP Z  28      -8.627  34.371  88.278  1.00 65.66           O  
-ATOM   5948  CB  ASP Z  28      -8.430  34.418  91.641  1.00 69.27           C  
-ATOM   5949  CG  ASP Z  28      -9.296  35.598  92.011  1.00 72.39           C  
-ATOM   5950  OD1 ASP Z  28     -10.472  35.387  92.377  1.00 73.82           O  
-ATOM   5951  OD2 ASP Z  28      -8.796  36.739  91.936  1.00 76.75           O  
-ATOM   5952  N   ASN Z  29     -10.355  35.284  89.390  1.00 66.30           N  
-ATOM   5953  CA  ASN Z  29     -10.723  36.175  88.293  1.00 66.51           C  
-ATOM   5954  C   ASN Z  29      -9.680  37.272  88.144  1.00 66.16           C  
-ATOM   5955  O   ASN Z  29      -9.237  37.577  87.036  1.00 66.19           O  
-ATOM   5956  CB  ASN Z  29     -12.085  36.823  88.546  1.00 65.87           C  
-ATOM   5957  CG  ASN Z  29     -12.514  37.733  87.406  1.00 66.54           C  
-ATOM   5958  OD1 ASN Z  29     -12.865  37.262  86.324  1.00 66.88           O  
-ATOM   5959  ND2 ASN Z  29     -12.470  39.042  87.638  1.00 62.82           N  
-ATOM   5960  N   GLU Z  30      -9.305  37.868  89.271  1.00 66.18           N  
-ATOM   5961  CA  GLU Z  30      -8.308  38.931  89.291  1.00 66.67           C  
-ATOM   5962  C   GLU Z  30      -7.008  38.436  88.672  1.00 66.11           C  
-ATOM   5963  O   GLU Z  30      -6.259  39.208  88.071  1.00 66.46           O  
-ATOM   5964  CB  GLU Z  30      -8.041  39.373  90.728  1.00 69.28           C  
-ATOM   5965  CG  GLU Z  30      -6.827  40.280  90.887  1.00 76.47           C  
-ATOM   5966  CD  GLU Z  30      -6.364  40.396  92.335  1.00 83.39           C  
-ATOM   5967  OE1 GLU Z  30      -5.352  41.088  92.584  1.00 85.58           O  
-ATOM   5968  OE2 GLU Z  30      -7.009  39.793  93.223  1.00 85.41           O  
-ATOM   5969  N   GLU Z  31      -6.739  37.146  88.832  1.00 64.72           N  
-ATOM   5970  CA  GLU Z  31      -5.526  36.558  88.288  1.00 64.14           C  
-ATOM   5971  C   GLU Z  31      -5.658  36.302  86.788  1.00 61.80           C  
-ATOM   5972  O   GLU Z  31      -4.700  36.492  86.032  1.00 61.54           O  
-ATOM   5973  CB  GLU Z  31      -5.206  35.243  89.004  1.00 67.08           C  
-ATOM   5974  CG  GLU Z  31      -3.783  34.755  88.771  1.00 74.68           C  
-ATOM   5975  CD  GLU Z  31      -3.531  33.384  89.363  1.00 80.26           C  
-ATOM   5976  OE1 GLU Z  31      -3.791  33.199  90.573  1.00 82.90           O  
-ATOM   5977  OE2 GLU Z  31      -3.068  32.494  88.615  1.00 83.57           O  
-ATOM   5978  N   GLN Z  32      -6.841  35.862  86.362  1.00 58.85           N  
-ATOM   5979  CA  GLN Z  32      -7.083  35.587  84.949  1.00 56.64           C  
-ATOM   5980  C   GLN Z  32      -6.963  36.870  84.135  1.00 55.42           C  
-ATOM   5981  O   GLN Z  32      -6.423  36.863  83.027  1.00 53.96           O  
-ATOM   5982  CB  GLN Z  32      -8.472  34.975  84.740  1.00 53.50           C  
-ATOM   5983  CG  GLN Z  32      -8.782  34.675  83.276  1.00 52.15           C  
-ATOM   5984  CD  GLN Z  32     -10.044  33.856  83.079  1.00 50.94           C  
-ATOM   5985  OE1 GLN Z  32     -10.451  33.588  81.949  1.00 50.73           O  
-ATOM   5986  NE2 GLN Z  32     -10.667  33.450  84.178  1.00 55.06           N  
-ATOM   5987  N   GLU Z  33      -7.466  37.968  84.692  1.00 54.88           N  
-ATOM   5988  CA  GLU Z  33      -7.405  39.259  84.017  1.00 54.49           C  
-ATOM   5989  C   GLU Z  33      -5.957  39.735  83.977  1.00 54.69           C  
-ATOM   5990  O   GLU Z  33      -5.526  40.364  83.007  1.00 54.21           O  
-ATOM   5991  CB  GLU Z  33      -8.267  40.297  84.745  1.00 52.95           C  
-ATOM   5992  CG  GLU Z  33      -9.752  39.944  84.837  1.00 51.16           C  
-ATOM   5993  CD  GLU Z  33     -10.616  41.146  85.202  1.00 52.83           C  
-ATOM   5994  OE1 GLU Z  33     -10.086  42.103  85.799  1.00 50.47           O  
-ATOM   5995  OE2 GLU Z  33     -11.831  41.133  84.902  1.00 55.69           O  
-ATOM   5996  N   LYS Z  34      -5.212  39.424  85.034  1.00 54.03           N  
-ATOM   5997  CA  LYS Z  34      -3.809  39.814  85.129  1.00 53.07           C  
-ATOM   5998  C   LYS Z  34      -3.020  39.222  83.965  1.00 50.67           C  
-ATOM   5999  O   LYS Z  34      -2.106  39.857  83.438  1.00 51.98           O  
-ATOM   6000  CB  LYS Z  34      -3.220  39.338  86.460  1.00 55.72           C  
-ATOM   6001  CG  LYS Z  34      -1.808  39.836  86.749  1.00 61.42           C  
-ATOM   6002  CD  LYS Z  34      -1.445  39.609  88.215  1.00 67.21           C  
-ATOM   6003  CE  LYS Z  34      -0.034  40.086  88.540  1.00 68.92           C  
-ATOM   6004  NZ  LYS Z  34       1.006  39.289  87.830  1.00 69.49           N  
-ATOM   6005  N   LEU Z  35      -3.388  38.009  83.566  1.00 47.85           N  
-ATOM   6006  CA  LEU Z  35      -2.731  37.321  82.461  1.00 46.90           C  
-ATOM   6007  C   LEU Z  35      -3.246  37.819  81.109  1.00 46.90           C  
-ATOM   6008  O   LEU Z  35      -2.488  37.907  80.139  1.00 47.47           O  
-ATOM   6009  CB  LEU Z  35      -2.963  35.811  82.569  1.00 44.47           C  
-ATOM   6010  CG  LEU Z  35      -2.330  35.082  83.762  1.00 44.12           C  
-ATOM   6011  CD1 LEU Z  35      -2.731  33.607  83.755  1.00 36.81           C  
-ATOM   6012  CD2 LEU Z  35      -0.811  35.222  83.692  1.00 44.77           C  
-ATOM   6013  N   LEU Z  36      -4.538  38.133  81.052  1.00 44.17           N  
-ATOM   6014  CA  LEU Z  36      -5.155  38.616  79.827  1.00 42.18           C  
-ATOM   6015  C   LEU Z  36      -4.552  39.950  79.405  1.00 41.10           C  
-ATOM   6016  O   LEU Z  36      -4.309  40.174  78.218  1.00 39.57           O  
-ATOM   6017  CB  LEU Z  36      -6.669  38.769  80.021  1.00 41.42           C  
-ATOM   6018  CG  LEU Z  36      -7.531  37.502  80.048  1.00 38.55           C  
-ATOM   6019  CD1 LEU Z  36      -8.936  37.845  80.536  1.00 37.65           C  
-ATOM   6020  CD2 LEU Z  36      -7.585  36.889  78.659  1.00 38.58           C  
-ATOM   6021  N   LYS Z  37      -4.303  40.818  80.385  1.00 40.17           N  
-ATOM   6022  CA  LYS Z  37      -3.739  42.145  80.147  1.00 41.34           C  
-ATOM   6023  C   LYS Z  37      -2.268  42.180  79.731  1.00 42.56           C  
-ATOM   6024  O   LYS Z  37      -1.728  43.253  79.443  1.00 41.47           O  
-ATOM   6025  CB  LYS Z  37      -3.918  43.020  81.386  1.00 44.85           C  
-ATOM   6026  CG  LYS Z  37      -5.354  43.407  81.673  1.00 51.33           C  
-ATOM   6027  CD  LYS Z  37      -5.447  44.268  82.927  1.00 53.43           C  
-ATOM   6028  CE  LYS Z  37      -6.888  44.648  83.229  1.00 59.70           C  
-ATOM   6029  NZ  LYS Z  37      -7.000  45.442  84.488  1.00 64.13           N  
-ATOM   6030  N   LYS Z  38      -1.617  41.022  79.710  1.00 42.07           N  
-ATOM   6031  CA  LYS Z  38      -0.217  40.958  79.311  1.00 42.47           C  
-ATOM   6032  C   LYS Z  38      -0.037  39.837  78.303  1.00 42.03           C  
-ATOM   6033  O   LYS Z  38       1.078  39.540  77.881  1.00 41.57           O  
-ATOM   6034  CB  LYS Z  38       0.700  40.711  80.520  1.00 46.88           C  
-ATOM   6035  CG  LYS Z  38       0.842  41.894  81.483  1.00 47.92           C  
-ATOM   6036  CD  LYS Z  38      -0.356  41.997  82.408  1.00 59.32           C  
-ATOM   6037  CE  LYS Z  38      -0.185  43.079  83.461  1.00 60.90           C  
-ATOM   6038  NZ  LYS Z  38      -1.262  42.969  84.488  1.00 62.72           N  
-ATOM   6039  N   SER Z  39      -1.146  39.220  77.910  1.00 41.08           N  
-ATOM   6040  CA  SER Z  39      -1.095  38.123  76.956  1.00 39.38           C  
-ATOM   6041  C   SER Z  39      -0.709  38.548  75.546  1.00 38.96           C  
-ATOM   6042  O   SER Z  39      -0.876  39.701  75.155  1.00 36.80           O  
-ATOM   6043  CB  SER Z  39      -2.438  37.403  76.909  1.00 38.44           C  
-ATOM   6044  OG  SER Z  39      -2.420  36.369  75.942  1.00 47.49           O  
-ATOM   6045  N   CYS Z  40      -0.174  37.588  74.800  1.00 39.11           N  
-ATOM   6046  CA  CYS Z  40       0.237  37.772  73.416  1.00 38.83           C  
-ATOM   6047  C   CYS Z  40      -0.511  36.685  72.658  1.00 37.94           C  
-ATOM   6048  O   CYS Z  40      -0.227  36.397  71.496  1.00 37.75           O  
-ATOM   6049  CB  CYS Z  40       1.742  37.549  73.260  1.00 39.54           C  
-ATOM   6050  SG  CYS Z  40       2.775  38.747  74.114  1.00 40.54           S  
-ATOM   6051  N   THR Z  41      -1.470  36.076  73.343  1.00 38.88           N  
-ATOM   6052  CA  THR Z  41      -2.265  35.010  72.749  1.00 38.43           C  
-ATOM   6053  C   THR Z  41      -3.717  35.437  72.592  1.00 37.75           C  
-ATOM   6054  O   THR Z  41      -4.317  35.993  73.510  1.00 37.33           O  
-ATOM   6055  CB  THR Z  41      -2.225  33.739  73.614  1.00 39.49           C  
-ATOM   6056  OG1 THR Z  41      -0.863  33.331  73.812  1.00 41.69           O  
-ATOM   6057  CG2 THR Z  41      -3.005  32.617  72.935  1.00 39.42           C  
-ATOM   6058  N   LEU Z  42      -4.280  35.165  71.424  1.00 38.30           N  
-ATOM   6059  CA  LEU Z  42      -5.665  35.512  71.151  1.00 38.27           C  
-ATOM   6060  C   LEU Z  42      -6.509  34.294  70.793  1.00 38.24           C  
-ATOM   6061  O   LEU Z  42      -6.028  33.334  70.183  1.00 38.50           O  
-ATOM   6062  CB  LEU Z  42      -5.741  36.514  69.994  1.00 37.59           C  
-ATOM   6063  CG  LEU Z  42      -4.974  37.828  70.167  1.00 41.32           C  
-ATOM   6064  CD1 LEU Z  42      -5.037  38.624  68.875  1.00 43.80           C  
-ATOM   6065  CD2 LEU Z  42      -5.563  38.629  71.323  1.00 39.93           C  
-ATOM   6066  N   TYR Z  43      -7.772  34.344  71.195  1.00 37.42           N  
-ATOM   6067  CA  TYR Z  43      -8.728  33.301  70.866  1.00 35.99           C  
-ATOM   6068  C   TYR Z  43      -9.423  33.852  69.626  1.00 33.16           C  
-ATOM   6069  O   TYR Z  43      -9.723  35.032  69.571  1.00 33.92           O  
-ATOM   6070  CB  TYR Z  43      -9.753  33.126  71.992  1.00 36.67           C  
-ATOM   6071  CG  TYR Z  43     -11.038  32.474  71.531  1.00 41.81           C  
-ATOM   6072  CD1 TYR Z  43     -11.114  31.096  71.326  1.00 41.56           C  
-ATOM   6073  CD2 TYR Z  43     -12.171  33.245  71.253  1.00 42.71           C  
-ATOM   6074  CE1 TYR Z  43     -12.288  30.501  70.855  1.00 45.09           C  
-ATOM   6075  CE2 TYR Z  43     -13.346  32.661  70.777  1.00 43.49           C  
-ATOM   6076  CZ  TYR Z  43     -13.396  31.292  70.580  1.00 44.51           C  
-ATOM   6077  OH  TYR Z  43     -14.544  30.719  70.088  1.00 44.60           O  
-ATOM   6078  N   VAL Z  44      -9.668  33.008  68.636  1.00 34.02           N  
-ATOM   6079  CA  VAL Z  44     -10.329  33.439  67.416  1.00 35.65           C  
-ATOM   6080  C   VAL Z  44     -11.578  32.595  67.244  1.00 36.25           C  
-ATOM   6081  O   VAL Z  44     -11.495  31.375  67.205  1.00 36.31           O  
-ATOM   6082  CB  VAL Z  44      -9.425  33.242  66.186  1.00 37.39           C  
-ATOM   6083  CG1 VAL Z  44     -10.099  33.824  64.959  1.00 38.57           C  
-ATOM   6084  CG2 VAL Z  44      -8.071  33.904  66.420  1.00 36.71           C  
-ATOM   6085  N   GLY Z  45     -12.732  33.246  67.131  1.00 36.51           N  
-ATOM   6086  CA  GLY Z  45     -13.969  32.507  66.985  1.00 34.29           C  
-ATOM   6087  C   GLY Z  45     -14.713  32.691  65.682  1.00 34.64           C  
-ATOM   6088  O   GLY Z  45     -14.378  33.562  64.872  1.00 32.63           O  
-ATOM   6089  N   ASN Z  46     -15.729  31.845  65.502  1.00 33.53           N  
-ATOM   6090  CA  ASN Z  46     -16.612  31.839  64.339  1.00 32.95           C  
-ATOM   6091  C   ASN Z  46     -15.943  31.431  63.035  1.00 34.30           C  
-ATOM   6092  O   ASN Z  46     -16.363  31.827  61.948  1.00 32.78           O  
-ATOM   6093  CB  ASN Z  46     -17.304  33.202  64.178  1.00 31.48           C  
-ATOM   6094  CG  ASN Z  46     -18.502  33.134  63.238  1.00 33.92           C  
-ATOM   6095  OD1 ASN Z  46     -19.116  32.076  63.083  1.00 31.32           O  
-ATOM   6096  ND2 ASN Z  46     -18.849  34.260  62.619  1.00 33.64           N  
-ATOM   6097  N   LEU Z  47     -14.907  30.613  63.153  1.00 37.16           N  
-ATOM   6098  CA  LEU Z  47     -14.192  30.128  61.988  1.00 39.42           C  
-ATOM   6099  C   LEU Z  47     -14.954  29.007  61.303  1.00 40.23           C  
-ATOM   6100  O   LEU Z  47     -15.687  28.252  61.939  1.00 39.61           O  
-ATOM   6101  CB  LEU Z  47     -12.809  29.604  62.392  1.00 37.76           C  
-ATOM   6102  CG  LEU Z  47     -11.807  30.627  62.932  1.00 38.00           C  
-ATOM   6103  CD1 LEU Z  47     -10.550  29.904  63.389  1.00 37.06           C  
-ATOM   6104  CD2 LEU Z  47     -11.476  31.647  61.840  1.00 36.01           C  
-ATOM   6105  N   SER Z  48     -14.767  28.912  59.995  1.00 42.45           N  
-ATOM   6106  CA  SER Z  48     -15.380  27.862  59.200  1.00 45.00           C  
-ATOM   6107  C   SER Z  48     -14.647  26.566  59.538  1.00 45.44           C  
-ATOM   6108  O   SER Z  48     -13.467  26.590  59.903  1.00 44.04           O  
-ATOM   6109  CB  SER Z  48     -15.209  28.174  57.715  1.00 46.65           C  
-ATOM   6110  OG  SER Z  48     -15.515  27.044  56.922  1.00 56.28           O  
-ATOM   6111  N   PHE Z  49     -15.336  25.438  59.418  1.00 46.61           N  
-ATOM   6112  CA  PHE Z  49     -14.722  24.149  59.722  1.00 49.25           C  
-ATOM   6113  C   PHE Z  49     -13.646  23.761  58.718  1.00 50.70           C  
-ATOM   6114  O   PHE Z  49     -12.803  22.915  59.011  1.00 51.08           O  
-ATOM   6115  CB  PHE Z  49     -15.773  23.037  59.770  1.00 51.04           C  
-ATOM   6116  CG  PHE Z  49     -16.589  23.014  61.035  1.00 51.38           C  
-ATOM   6117  CD1 PHE Z  49     -17.441  21.944  61.298  1.00 50.84           C  
-ATOM   6118  CD2 PHE Z  49     -16.516  24.051  61.959  1.00 48.74           C  
-ATOM   6119  CE1 PHE Z  49     -18.204  21.909  62.463  1.00 48.66           C  
-ATOM   6120  CE2 PHE Z  49     -17.278  24.019  63.123  1.00 47.62           C  
-ATOM   6121  CZ  PHE Z  49     -18.120  22.949  63.375  1.00 47.41           C  
-ATOM   6122  N   TYR Z  50     -13.675  24.357  57.530  1.00 51.81           N  
-ATOM   6123  CA  TYR Z  50     -12.667  24.031  56.532  1.00 54.38           C  
-ATOM   6124  C   TYR Z  50     -11.581  25.101  56.456  1.00 53.56           C  
-ATOM   6125  O   TYR Z  50     -10.776  25.128  55.524  1.00 52.40           O  
-ATOM   6126  CB  TYR Z  50     -13.318  23.790  55.158  1.00 60.81           C  
-ATOM   6127  CG  TYR Z  50     -13.753  25.014  54.380  1.00 67.73           C  
-ATOM   6128  CD1 TYR Z  50     -12.820  25.824  53.721  1.00 71.74           C  
-ATOM   6129  CD2 TYR Z  50     -15.106  25.334  54.257  1.00 72.84           C  
-ATOM   6130  CE1 TYR Z  50     -13.223  26.915  52.957  1.00 72.36           C  
-ATOM   6131  CE2 TYR Z  50     -15.522  26.425  53.495  1.00 75.46           C  
-ATOM   6132  CZ  TYR Z  50     -14.576  27.209  52.848  1.00 76.45           C  
-ATOM   6133  OH  TYR Z  50     -14.990  28.285  52.092  1.00 79.88           O  
-ATOM   6134  N   THR Z  51     -11.566  25.976  57.457  1.00 52.80           N  
-ATOM   6135  CA  THR Z  51     -10.565  27.032  57.551  1.00 50.90           C  
-ATOM   6136  C   THR Z  51      -9.284  26.348  58.005  1.00 49.18           C  
-ATOM   6137  O   THR Z  51      -9.280  25.637  59.005  1.00 49.27           O  
-ATOM   6138  CB  THR Z  51     -10.963  28.099  58.599  1.00 51.09           C  
-ATOM   6139  OG1 THR Z  51     -12.094  28.838  58.120  1.00 51.08           O  
-ATOM   6140  CG2 THR Z  51      -9.802  29.056  58.862  1.00 48.59           C  
-ATOM   6141  N   THR Z  52      -8.197  26.572  57.280  1.00 47.21           N  
-ATOM   6142  CA  THR Z  52      -6.936  25.928  57.616  1.00 45.74           C  
-ATOM   6143  C   THR Z  52      -5.938  26.786  58.381  1.00 43.77           C  
-ATOM   6144  O   THR Z  52      -6.021  28.010  58.396  1.00 42.77           O  
-ATOM   6145  CB  THR Z  52      -6.258  25.402  56.345  1.00 44.55           C  
-ATOM   6146  OG1 THR Z  52      -5.905  26.502  55.499  1.00 45.43           O  
-ATOM   6147  CG2 THR Z  52      -7.215  24.480  55.586  1.00 44.55           C  
-ATOM   6148  N   GLU Z  53      -4.998  26.113  59.031  1.00 43.66           N  
-ATOM   6149  CA  GLU Z  53      -3.950  26.777  59.790  1.00 42.04           C  
-ATOM   6150  C   GLU Z  53      -3.165  27.719  58.872  1.00 40.93           C  
-ATOM   6151  O   GLU Z  53      -2.723  28.787  59.300  1.00 40.60           O  
-ATOM   6152  CB  GLU Z  53      -3.018  25.722  60.391  1.00 43.05           C  
-ATOM   6153  CG  GLU Z  53      -1.805  26.273  61.119  1.00 47.71           C  
-ATOM   6154  CD  GLU Z  53      -0.872  25.170  61.591  1.00 51.07           C  
-ATOM   6155  OE1 GLU Z  53      -0.666  24.208  60.820  1.00 49.34           O  
-ATOM   6156  OE2 GLU Z  53      -0.342  25.267  62.722  1.00 50.51           O  
-ATOM   6157  N   GLU Z  54      -3.010  27.324  57.608  1.00 39.23           N  
-ATOM   6158  CA  GLU Z  54      -2.291  28.125  56.620  1.00 39.66           C  
-ATOM   6159  C   GLU Z  54      -3.010  29.443  56.341  1.00 40.15           C  
-ATOM   6160  O   GLU Z  54      -2.374  30.485  56.195  1.00 39.18           O  
-ATOM   6161  CB  GLU Z  54      -2.144  27.356  55.304  1.00 42.89           C  
-ATOM   6162  CG  GLU Z  54      -1.242  26.127  55.367  1.00 51.39           C  
-ATOM   6163  CD  GLU Z  54      -1.838  24.999  56.188  1.00 57.40           C  
-ATOM   6164  OE1 GLU Z  54      -3.023  24.669  55.951  1.00 52.34           O  
-ATOM   6165  OE2 GLU Z  54      -1.122  24.448  57.060  1.00 57.26           O  
-ATOM   6166  N   GLN Z  55      -4.336  29.386  56.247  1.00 38.54           N  
-ATOM   6167  CA  GLN Z  55      -5.135  30.578  55.994  1.00 37.07           C  
-ATOM   6168  C   GLN Z  55      -5.079  31.502  57.212  1.00 33.79           C  
-ATOM   6169  O   GLN Z  55      -5.023  32.720  57.075  1.00 35.50           O  
-ATOM   6170  CB  GLN Z  55      -6.591  30.192  55.702  1.00 36.90           C  
-ATOM   6171  CG  GLN Z  55      -6.746  29.214  54.562  1.00 37.05           C  
-ATOM   6172  CD  GLN Z  55      -8.169  28.727  54.398  1.00 37.71           C  
-ATOM   6173  OE1 GLN Z  55      -8.783  28.236  55.348  1.00 36.86           O  
-ATOM   6174  NE2 GLN Z  55      -8.700  28.849  53.186  1.00 39.10           N  
-ATOM   6175  N   ILE Z  56      -5.089  30.919  58.403  1.00 31.26           N  
-ATOM   6176  CA  ILE Z  56      -5.034  31.713  59.618  1.00 31.71           C  
-ATOM   6177  C   ILE Z  56      -3.673  32.391  59.723  1.00 34.13           C  
-ATOM   6178  O   ILE Z  56      -3.564  33.516  60.220  1.00 33.80           O  
-ATOM   6179  CB  ILE Z  56      -5.274  30.841  60.855  1.00 32.27           C  
-ATOM   6180  CG1 ILE Z  56      -6.698  30.288  60.811  1.00 35.88           C  
-ATOM   6181  CG2 ILE Z  56      -5.038  31.642  62.121  1.00 28.78           C  
-ATOM   6182  CD1 ILE Z  56      -7.031  29.359  61.961  1.00 42.90           C  
-ATOM   6183  N   TYR Z  57      -2.639  31.703  59.247  1.00 33.14           N  
-ATOM   6184  CA  TYR Z  57      -1.293  32.249  59.267  1.00 32.23           C  
-ATOM   6185  C   TYR Z  57      -1.206  33.467  58.360  1.00 30.50           C  
-ATOM   6186  O   TYR Z  57      -0.664  34.498  58.743  1.00 29.69           O  
-ATOM   6187  CB  TYR Z  57      -0.289  31.196  58.800  1.00 33.15           C  
-ATOM   6188  CG  TYR Z  57       0.564  30.644  59.912  1.00 39.11           C  
-ATOM   6189  CD1 TYR Z  57       1.649  31.372  60.419  1.00 40.55           C  
-ATOM   6190  CD2 TYR Z  57       0.281  29.405  60.475  1.00 37.89           C  
-ATOM   6191  CE1 TYR Z  57       2.425  30.870  61.462  1.00 40.42           C  
-ATOM   6192  CE2 TYR Z  57       1.048  28.895  61.516  1.00 41.85           C  
-ATOM   6193  CZ  TYR Z  57       2.116  29.631  62.005  1.00 41.56           C  
-ATOM   6194  OH  TYR Z  57       2.860  29.124  63.041  1.00 42.56           O  
-ATOM   6195  N   GLU Z  58      -1.755  33.338  57.158  1.00 28.37           N  
-ATOM   6196  CA  GLU Z  58      -1.721  34.404  56.182  1.00 27.62           C  
-ATOM   6197  C   GLU Z  58      -2.456  35.644  56.648  1.00 30.43           C  
-ATOM   6198  O   GLU Z  58      -1.988  36.768  56.441  1.00 29.63           O  
-ATOM   6199  CB  GLU Z  58      -2.318  33.926  54.862  1.00 24.17           C  
-ATOM   6200  CG  GLU Z  58      -2.209  34.965  53.760  1.00 28.03           C  
-ATOM   6201  CD  GLU Z  58      -0.766  35.177  53.310  1.00 32.33           C  
-ATOM   6202  OE1 GLU Z  58       0.130  34.484  53.834  1.00 37.67           O  
-ATOM   6203  OE2 GLU Z  58      -0.517  36.025  52.431  1.00 31.64           O  
-ATOM   6204  N   LEU Z  59      -3.610  35.445  57.280  1.00 31.06           N  
-ATOM   6205  CA  LEU Z  59      -4.389  36.580  57.750  1.00 28.82           C  
-ATOM   6206  C   LEU Z  59      -3.781  37.247  58.968  1.00 26.37           C  
-ATOM   6207  O   LEU Z  59      -3.517  38.447  58.961  1.00 27.76           O  
-ATOM   6208  CB  LEU Z  59      -5.830  36.171  58.085  1.00 25.62           C  
-ATOM   6209  CG  LEU Z  59      -6.686  37.329  58.639  1.00 28.29           C  
-ATOM   6210  CD1 LEU Z  59      -6.648  38.505  57.659  1.00 18.06           C  
-ATOM   6211  CD2 LEU Z  59      -8.129  36.867  58.873  1.00 21.23           C  
-ATOM   6212  N   PHE Z  60      -3.566  36.476  60.020  1.00 26.44           N  
-ATOM   6213  CA  PHE Z  60      -3.043  37.044  61.246  1.00 28.20           C  
-ATOM   6214  C   PHE Z  60      -1.596  37.543  61.232  1.00 30.34           C  
-ATOM   6215  O   PHE Z  60      -1.179  38.253  62.145  1.00 31.73           O  
-ATOM   6216  CB  PHE Z  60      -3.289  36.070  62.400  1.00 29.18           C  
-ATOM   6217  CG  PHE Z  60      -4.715  36.094  62.904  1.00 32.36           C  
-ATOM   6218  CD1 PHE Z  60      -5.743  35.509  62.165  1.00 33.11           C  
-ATOM   6219  CD2 PHE Z  60      -5.035  36.765  64.090  1.00 33.18           C  
-ATOM   6220  CE1 PHE Z  60      -7.077  35.594  62.599  1.00 31.05           C  
-ATOM   6221  CE2 PHE Z  60      -6.369  36.858  64.536  1.00 29.25           C  
-ATOM   6222  CZ  PHE Z  60      -7.387  36.271  63.787  1.00 30.20           C  
-ATOM   6223  N   SER Z  61      -0.830  37.199  60.200  1.00 30.36           N  
-ATOM   6224  CA  SER Z  61       0.546  37.673  60.124  1.00 32.25           C  
-ATOM   6225  C   SER Z  61       0.580  39.145  59.705  1.00 32.79           C  
-ATOM   6226  O   SER Z  61       1.609  39.815  59.829  1.00 31.58           O  
-ATOM   6227  CB  SER Z  61       1.351  36.834  59.127  1.00 34.81           C  
-ATOM   6228  OG  SER Z  61       1.573  35.528  59.628  1.00 41.64           O  
-ATOM   6229  N   LYS Z  62      -0.549  39.651  59.215  1.00 31.25           N  
-ATOM   6230  CA  LYS Z  62      -0.613  41.047  58.798  1.00 28.97           C  
-ATOM   6231  C   LYS Z  62      -0.426  42.028  59.946  1.00 27.81           C  
-ATOM   6232  O   LYS Z  62      -0.214  43.219  59.722  1.00 29.56           O  
-ATOM   6233  CB  LYS Z  62      -1.927  41.325  58.075  1.00 29.21           C  
-ATOM   6234  CG  LYS Z  62      -1.963  40.694  56.708  1.00 27.36           C  
-ATOM   6235  CD  LYS Z  62      -3.321  40.813  56.064  1.00 31.52           C  
-ATOM   6236  CE  LYS Z  62      -3.309  40.165  54.691  1.00 35.03           C  
-ATOM   6237  NZ  LYS Z  62      -2.473  40.952  53.748  1.00 33.77           N  
-ATOM   6238  N   SER Z  63      -0.495  41.547  61.179  1.00 29.07           N  
-ATOM   6239  CA  SER Z  63      -0.290  42.449  62.310  1.00 30.39           C  
-ATOM   6240  C   SER Z  63       1.040  42.152  63.019  1.00 32.11           C  
-ATOM   6241  O   SER Z  63       1.422  42.848  63.964  1.00 34.25           O  
-ATOM   6242  CB  SER Z  63      -1.460  42.350  63.309  1.00 28.08           C  
-ATOM   6243  OG  SER Z  63      -1.496  41.095  63.961  1.00 34.11           O  
-ATOM   6244  N   GLY Z  64       1.746  41.122  62.560  1.00 33.66           N  
-ATOM   6245  CA  GLY Z  64       3.019  40.777  63.178  1.00 33.91           C  
-ATOM   6246  C   GLY Z  64       3.374  39.305  63.078  1.00 33.84           C  
-ATOM   6247  O   GLY Z  64       2.597  38.504  62.555  1.00 34.69           O  
-ATOM   6248  N   ASP Z  65       4.541  38.938  63.600  1.00 34.29           N  
-ATOM   6249  CA  ASP Z  65       5.006  37.557  63.523  1.00 35.42           C  
-ATOM   6250  C   ASP Z  65       4.343  36.633  64.514  1.00 32.39           C  
-ATOM   6251  O   ASP Z  65       4.298  36.898  65.708  1.00 31.87           O  
-ATOM   6252  CB  ASP Z  65       6.523  37.491  63.699  1.00 38.92           C  
-ATOM   6253  CG  ASP Z  65       7.233  38.566  62.922  1.00 44.43           C  
-ATOM   6254  OD1 ASP Z  65       7.472  39.644  63.509  1.00 53.09           O  
-ATOM   6255  OD2 ASP Z  65       7.530  38.344  61.728  1.00 49.09           O  
-ATOM   6256  N   ILE Z  66       3.844  35.531  63.979  1.00 34.42           N  
-ATOM   6257  CA  ILE Z  66       3.152  34.517  64.751  1.00 35.39           C  
-ATOM   6258  C   ILE Z  66       4.091  33.441  65.289  1.00 37.07           C  
-ATOM   6259  O   ILE Z  66       4.867  32.852  64.542  1.00 37.34           O  
-ATOM   6260  CB  ILE Z  66       2.077  33.853  63.883  1.00 31.50           C  
-ATOM   6261  CG1 ILE Z  66       0.986  34.877  63.565  1.00 28.78           C  
-ATOM   6262  CG2 ILE Z  66       1.524  32.620  64.574  1.00 28.91           C  
-ATOM   6263  CD1 ILE Z  66      -0.070  34.364  62.634  1.00 31.11           C  
-ATOM   6264  N   LYS Z  67       4.007  33.198  66.591  1.00 39.56           N  
-ATOM   6265  CA  LYS Z  67       4.822  32.190  67.242  1.00 40.91           C  
-ATOM   6266  C   LYS Z  67       4.192  30.804  67.084  1.00 43.21           C  
-ATOM   6267  O   LYS Z  67       4.880  29.843  66.722  1.00 43.53           O  
-ATOM   6268  CB  LYS Z  67       4.973  32.521  68.721  1.00 40.44           C  
-ATOM   6269  CG  LYS Z  67       5.822  31.519  69.477  1.00 41.14           C  
-ATOM   6270  CD  LYS Z  67       5.987  31.937  70.920  1.00 40.00           C  
-ATOM   6271  CE  LYS Z  67       6.852  30.943  71.668  1.00 44.96           C  
-ATOM   6272  NZ  LYS Z  67       7.029  31.351  73.078  1.00 45.38           N  
-ATOM   6273  N   LYS Z  68       2.888  30.705  67.349  1.00 42.84           N  
-ATOM   6274  CA  LYS Z  68       2.175  29.433  67.221  1.00 43.55           C  
-ATOM   6275  C   LYS Z  68       0.649  29.570  67.061  1.00 42.96           C  
-ATOM   6276  O   LYS Z  68       0.028  30.454  67.648  1.00 42.43           O  
-ATOM   6277  CB  LYS Z  68       2.470  28.541  68.432  1.00 42.71           C  
-ATOM   6278  CG  LYS Z  68       1.910  27.123  68.298  1.00 49.05           C  
-ATOM   6279  CD  LYS Z  68       2.259  26.248  69.500  1.00 55.40           C  
-ATOM   6280  CE  LYS Z  68       1.712  24.827  69.324  1.00 60.23           C  
-ATOM   6281  NZ  LYS Z  68       1.943  23.966  70.526  1.00 65.23           N  
-ATOM   6282  N   ILE Z  69       0.067  28.669  66.269  1.00 43.01           N  
-ATOM   6283  CA  ILE Z  69      -1.375  28.623  66.014  1.00 43.63           C  
-ATOM   6284  C   ILE Z  69      -1.900  27.226  66.355  1.00 44.76           C  
-ATOM   6285  O   ILE Z  69      -1.483  26.237  65.750  1.00 45.15           O  
-ATOM   6286  CB  ILE Z  69      -1.692  28.909  64.532  1.00 43.41           C  
-ATOM   6287  CG1 ILE Z  69      -1.428  30.382  64.226  1.00 44.59           C  
-ATOM   6288  CG2 ILE Z  69      -3.130  28.519  64.213  1.00 41.02           C  
-ATOM   6289  CD1 ILE Z  69      -1.597  30.738  62.777  1.00 46.77           C  
-ATOM   6290  N   ILE Z  70      -2.821  27.158  67.313  1.00 43.75           N  
-ATOM   6291  CA  ILE Z  70      -3.403  25.892  67.743  1.00 42.84           C  
-ATOM   6292  C   ILE Z  70      -4.873  25.781  67.339  1.00 43.53           C  
-ATOM   6293  O   ILE Z  70      -5.731  26.430  67.933  1.00 41.07           O  
-ATOM   6294  CB  ILE Z  70      -3.296  25.744  69.275  1.00 42.50           C  
-ATOM   6295  CG1 ILE Z  70      -1.822  25.801  69.687  1.00 40.92           C  
-ATOM   6296  CG2 ILE Z  70      -3.943  24.438  69.721  1.00 41.25           C  
-ATOM   6297  CD1 ILE Z  70      -1.591  25.721  71.156  1.00 46.54           C  
-ATOM   6298  N   MET Z  71      -5.160  24.953  66.336  1.00 43.72           N  
-ATOM   6299  CA  MET Z  71      -6.532  24.771  65.860  1.00 46.74           C  
-ATOM   6300  C   MET Z  71      -7.443  24.098  66.880  1.00 46.60           C  
-ATOM   6301  O   MET Z  71      -7.035  23.164  67.573  1.00 45.30           O  
-ATOM   6302  CB  MET Z  71      -6.547  23.952  64.568  1.00 46.94           C  
-ATOM   6303  CG  MET Z  71      -5.751  24.573  63.439  1.00 51.92           C  
-ATOM   6304  SD  MET Z  71      -6.328  26.211  62.979  1.00 54.45           S  
-ATOM   6305  CE  MET Z  71      -7.311  25.843  61.520  1.00 52.15           C  
-ATOM   6306  N   GLY Z  72      -8.677  24.595  66.969  1.00 47.85           N  
-ATOM   6307  CA  GLY Z  72      -9.658  24.033  67.883  1.00 48.91           C  
-ATOM   6308  C   GLY Z  72     -10.207  22.758  67.275  1.00 51.19           C  
-ATOM   6309  O   GLY Z  72     -10.613  22.741  66.107  1.00 50.95           O  
-ATOM   6310  N   LEU Z  73     -10.236  21.688  68.062  1.00 52.95           N  
-ATOM   6311  CA  LEU Z  73     -10.700  20.399  67.565  1.00 54.70           C  
-ATOM   6312  C   LEU Z  73     -11.837  19.793  68.378  1.00 55.12           C  
-ATOM   6313  O   LEU Z  73     -11.982  20.055  69.576  1.00 53.77           O  
-ATOM   6314  CB  LEU Z  73      -9.525  19.415  67.543  1.00 55.39           C  
-ATOM   6315  CG  LEU Z  73      -8.200  19.930  66.971  1.00 57.49           C  
-ATOM   6316  CD1 LEU Z  73      -7.081  18.959  67.320  1.00 57.51           C  
-ATOM   6317  CD2 LEU Z  73      -8.313  20.116  65.463  1.00 58.07           C  
-ATOM   6318  N   ASP Z  74     -12.639  18.970  67.709  1.00 57.15           N  
-ATOM   6319  CA  ASP Z  74     -13.759  18.290  68.352  1.00 59.23           C  
-ATOM   6320  C   ASP Z  74     -13.172  17.249  69.300  1.00 60.15           C  
-ATOM   6321  O   ASP Z  74     -12.455  16.345  68.871  1.00 59.83           O  
-ATOM   6322  CB  ASP Z  74     -14.639  17.620  67.291  1.00 61.20           C  
-ATOM   6323  CG  ASP Z  74     -15.896  17.008  67.874  1.00 61.40           C  
-ATOM   6324  OD1 ASP Z  74     -16.903  16.925  67.143  1.00 63.32           O  
-ATOM   6325  OD2 ASP Z  74     -15.877  16.603  69.056  1.00 65.06           O  
-ATOM   6326  N   LYS Z  75     -13.478  17.383  70.587  1.00 61.98           N  
-ATOM   6327  CA  LYS Z  75     -12.954  16.475  71.602  1.00 64.39           C  
-ATOM   6328  C   LYS Z  75     -13.153  14.989  71.315  1.00 67.10           C  
-ATOM   6329  O   LYS Z  75     -12.549  14.142  71.972  1.00 67.41           O  
-ATOM   6330  CB  LYS Z  75     -13.553  16.810  72.966  1.00 62.22           C  
-ATOM   6331  CG  LYS Z  75     -12.827  16.143  74.109  1.00 60.47           C  
-ATOM   6332  CD  LYS Z  75     -13.219  16.754  75.434  1.00 63.90           C  
-ATOM   6333  CE  LYS Z  75     -12.313  16.251  76.545  1.00 64.05           C  
-ATOM   6334  NZ  LYS Z  75     -12.639  16.872  77.855  1.00 65.81           N  
-ATOM   6335  N   MET Z  76     -13.994  14.669  70.337  1.00 68.77           N  
-ATOM   6336  CA  MET Z  76     -14.241  13.276  69.996  1.00 71.19           C  
-ATOM   6337  C   MET Z  76     -13.776  12.954  68.583  1.00 71.60           C  
-ATOM   6338  O   MET Z  76     -12.910  12.103  68.389  1.00 71.84           O  
-ATOM   6339  CB  MET Z  76     -15.730  12.951  70.146  1.00 74.86           C  
-ATOM   6340  CG  MET Z  76     -16.291  13.264  71.531  1.00 80.53           C  
-ATOM   6341  SD  MET Z  76     -15.252  12.635  72.877  1.00 87.03           S  
-ATOM   6342  CE  MET Z  76     -15.824  10.928  72.991  1.00 86.25           C  
-ATOM   6343  N   LYS Z  77     -14.349  13.635  67.596  1.00 71.61           N  
-ATOM   6344  CA  LYS Z  77     -13.979  13.404  66.204  1.00 71.79           C  
-ATOM   6345  C   LYS Z  77     -12.571  13.932  65.937  1.00 71.60           C  
-ATOM   6346  O   LYS Z  77     -11.928  13.557  64.952  1.00 71.47           O  
-ATOM   6347  CB  LYS Z  77     -14.977  14.097  65.268  1.00 71.66           C  
-ATOM   6348  CG  LYS Z  77     -16.429  13.697  65.490  1.00 72.84           C  
-ATOM   6349  CD  LYS Z  77     -17.357  14.372  64.487  1.00 73.77           C  
-ATOM   6350  CE  LYS Z  77     -18.810  13.981  64.733  1.00 75.09           C  
-ATOM   6351  NZ  LYS Z  77     -19.746  14.583  63.738  1.00 73.89           N  
-ATOM   6352  N   LYS Z  78     -12.101  14.801  66.828  1.00 71.59           N  
-ATOM   6353  CA  LYS Z  78     -10.781  15.414  66.713  1.00 70.75           C  
-ATOM   6354  C   LYS Z  78     -10.584  16.096  65.365  1.00 69.15           C  
-ATOM   6355  O   LYS Z  78      -9.571  15.906  64.693  1.00 68.90           O  
-ATOM   6356  CB  LYS Z  78      -9.685  14.374  66.956  1.00 72.03           C  
-ATOM   6357  CG  LYS Z  78      -9.657  13.875  68.389  1.00 73.20           C  
-ATOM   6358  CD  LYS Z  78      -8.395  13.093  68.684  1.00 77.10           C  
-ATOM   6359  CE  LYS Z  78      -8.360  12.647  70.135  1.00 78.21           C  
-ATOM   6360  NZ  LYS Z  78      -7.069  11.979  70.467  1.00 81.86           N  
-ATOM   6361  N   THR Z  79     -11.575  16.894  64.981  1.00 67.80           N  
-ATOM   6362  CA  THR Z  79     -11.543  17.638  63.731  1.00 65.91           C  
-ATOM   6363  C   THR Z  79     -11.803  19.113  64.036  1.00 64.26           C  
-ATOM   6364  O   THR Z  79     -12.341  19.445  65.096  1.00 62.77           O  
-ATOM   6365  CB  THR Z  79     -12.614  17.122  62.751  1.00 65.38           C  
-ATOM   6366  OG1 THR Z  79     -13.900  17.161  63.380  1.00 66.79           O  
-ATOM   6367  CG2 THR Z  79     -12.310  15.699  62.335  1.00 64.52           C  
-ATOM   6368  N   ALA Z  80     -11.412  19.990  63.115  1.00 62.68           N  
-ATOM   6369  CA  ALA Z  80     -11.606  21.426  63.293  1.00 61.23           C  
-ATOM   6370  C   ALA Z  80     -13.069  21.716  63.617  1.00 60.07           C  
-ATOM   6371  O   ALA Z  80     -13.959  21.434  62.805  1.00 58.81           O  
-ATOM   6372  CB  ALA Z  80     -11.191  22.165  62.027  1.00 59.25           C  
-ATOM   6373  N   CYS Z  81     -13.318  22.271  64.803  1.00 59.29           N  
-ATOM   6374  CA  CYS Z  81     -14.683  22.578  65.211  1.00 57.70           C  
-ATOM   6375  C   CYS Z  81     -15.090  24.052  65.178  1.00 56.66           C  
-ATOM   6376  O   CYS Z  81     -16.163  24.406  65.677  1.00 57.91           O  
-ATOM   6377  CB  CYS Z  81     -14.988  21.973  66.593  1.00 56.52           C  
-ATOM   6378  SG  CYS Z  81     -13.972  22.495  67.975  1.00 63.24           S  
-ATOM   6379  N   GLY Z  82     -14.254  24.909  64.593  1.00 53.84           N  
-ATOM   6380  CA  GLY Z  82     -14.624  26.313  64.472  1.00 51.18           C  
-ATOM   6381  C   GLY Z  82     -13.935  27.391  65.289  1.00 49.80           C  
-ATOM   6382  O   GLY Z  82     -14.506  28.467  65.498  1.00 47.59           O  
-ATOM   6383  N   PHE Z  83     -12.715  27.133  65.747  1.00 48.37           N  
-ATOM   6384  CA  PHE Z  83     -11.997  28.135  66.527  1.00 46.78           C  
-ATOM   6385  C   PHE Z  83     -10.515  27.795  66.627  1.00 46.98           C  
-ATOM   6386  O   PHE Z  83     -10.105  26.693  66.269  1.00 47.12           O  
-ATOM   6387  CB  PHE Z  83     -12.611  28.247  67.924  1.00 43.59           C  
-ATOM   6388  CG  PHE Z  83     -12.166  27.173  68.878  1.00 42.74           C  
-ATOM   6389  CD1 PHE Z  83     -11.091  27.398  69.731  1.00 38.14           C  
-ATOM   6390  CD2 PHE Z  83     -12.818  25.938  68.927  1.00 39.32           C  
-ATOM   6391  CE1 PHE Z  83     -10.669  26.422  70.620  1.00 42.72           C  
-ATOM   6392  CE2 PHE Z  83     -12.404  24.944  69.816  1.00 40.30           C  
-ATOM   6393  CZ  PHE Z  83     -11.326  25.186  70.666  1.00 43.61           C  
-ATOM   6394  N   CYS Z  84      -9.713  28.744  67.104  1.00 45.50           N  
-ATOM   6395  CA  CYS Z  84      -8.281  28.511  67.250  1.00 44.96           C  
-ATOM   6396  C   CYS Z  84      -7.615  29.523  68.176  1.00 44.49           C  
-ATOM   6397  O   CYS Z  84      -8.248  30.469  68.663  1.00 45.21           O  
-ATOM   6398  CB  CYS Z  84      -7.589  28.566  65.884  1.00 44.09           C  
-ATOM   6399  SG  CYS Z  84      -7.282  30.244  65.262  1.00 42.85           S  
-ATOM   6400  N   PHE Z  85      -6.332  29.295  68.429  1.00 42.39           N  
-ATOM   6401  CA  PHE Z  85      -5.542  30.191  69.246  1.00 40.78           C  
-ATOM   6402  C   PHE Z  85      -4.382  30.659  68.381  1.00 40.10           C  
-ATOM   6403  O   PHE Z  85      -3.837  29.900  67.580  1.00 40.90           O  
-ATOM   6404  CB  PHE Z  85      -5.011  29.490  70.495  1.00 42.12           C  
-ATOM   6405  CG  PHE Z  85      -6.070  29.174  71.505  1.00 45.99           C  
-ATOM   6406  CD1 PHE Z  85      -6.705  27.929  71.510  1.00 47.90           C  
-ATOM   6407  CD2 PHE Z  85      -6.463  30.134  72.433  1.00 44.57           C  
-ATOM   6408  CE1 PHE Z  85      -7.721  27.648  72.430  1.00 47.58           C  
-ATOM   6409  CE2 PHE Z  85      -7.471  29.866  73.350  1.00 46.42           C  
-ATOM   6410  CZ  PHE Z  85      -8.103  28.618  73.348  1.00 46.52           C  
-ATOM   6411  N   VAL Z  86      -4.039  31.928  68.524  1.00 39.47           N  
-ATOM   6412  CA  VAL Z  86      -2.947  32.527  67.777  1.00 38.22           C  
-ATOM   6413  C   VAL Z  86      -2.053  33.235  68.784  1.00 38.37           C  
-ATOM   6414  O   VAL Z  86      -2.503  34.137  69.499  1.00 36.63           O  
-ATOM   6415  CB  VAL Z  86      -3.455  33.572  66.750  1.00 38.82           C  
-ATOM   6416  CG1 VAL Z  86      -2.268  34.176  65.987  1.00 34.87           C  
-ATOM   6417  CG2 VAL Z  86      -4.430  32.919  65.785  1.00 35.19           C  
-ATOM   6418  N   GLU Z  87      -0.797  32.809  68.850  1.00 36.80           N  
-ATOM   6419  CA  GLU Z  87       0.151  33.414  69.769  1.00 37.64           C  
-ATOM   6420  C   GLU Z  87       1.190  34.232  69.004  1.00 37.47           C  
-ATOM   6421  O   GLU Z  87       1.792  33.763  68.032  1.00 36.01           O  
-ATOM   6422  CB  GLU Z  87       0.838  32.334  70.614  1.00 39.28           C  
-ATOM   6423  CG  GLU Z  87       1.945  32.878  71.504  1.00 44.14           C  
-ATOM   6424  CD  GLU Z  87       2.647  31.799  72.308  1.00 47.76           C  
-ATOM   6425  OE1 GLU Z  87       2.672  30.634  71.845  1.00 45.63           O  
-ATOM   6426  OE2 GLU Z  87       3.184  32.125  73.392  1.00 39.58           O  
-ATOM   6427  N   TYR Z  88       1.369  35.472  69.440  1.00 37.70           N  
-ATOM   6428  CA  TYR Z  88       2.332  36.375  68.828  1.00 38.51           C  
-ATOM   6429  C   TYR Z  88       3.566  36.433  69.723  1.00 39.42           C  
-ATOM   6430  O   TYR Z  88       3.532  35.982  70.870  1.00 39.69           O  
-ATOM   6431  CB  TYR Z  88       1.728  37.778  68.701  1.00 35.56           C  
-ATOM   6432  CG  TYR Z  88       0.700  37.906  67.601  1.00 34.95           C  
-ATOM   6433  CD1 TYR Z  88       1.089  38.101  66.275  1.00 30.16           C  
-ATOM   6434  CD2 TYR Z  88      -0.667  37.818  67.882  1.00 31.94           C  
-ATOM   6435  CE1 TYR Z  88       0.142  38.206  65.252  1.00 33.22           C  
-ATOM   6436  CE2 TYR Z  88      -1.625  37.923  66.863  1.00 28.33           C  
-ATOM   6437  CZ  TYR Z  88      -1.214  38.115  65.555  1.00 29.52           C  
-ATOM   6438  OH  TYR Z  88      -2.153  38.200  64.550  1.00 28.84           O  
-ATOM   6439  N   TYR Z  89       4.652  36.981  69.190  1.00 39.29           N  
-ATOM   6440  CA  TYR Z  89       5.881  37.121  69.953  1.00 40.07           C  
-ATOM   6441  C   TYR Z  89       5.806  38.357  70.844  1.00 40.67           C  
-ATOM   6442  O   TYR Z  89       6.307  38.348  71.969  1.00 42.45           O  
-ATOM   6443  CB  TYR Z  89       7.079  37.205  69.000  1.00 42.26           C  
-ATOM   6444  CG  TYR Z  89       7.487  35.855  68.447  1.00 36.64           C  
-ATOM   6445  CD1 TYR Z  89       8.133  34.920  69.258  1.00 37.62           C  
-ATOM   6446  CD2 TYR Z  89       7.195  35.496  67.130  1.00 38.06           C  
-ATOM   6447  CE1 TYR Z  89       8.476  33.657  68.773  1.00 36.06           C  
-ATOM   6448  CE2 TYR Z  89       7.533  34.232  66.635  1.00 36.96           C  
-ATOM   6449  CZ  TYR Z  89       8.171  33.322  67.466  1.00 37.14           C  
-ATOM   6450  OH  TYR Z  89       8.495  32.072  67.001  1.00 44.88           O  
-ATOM   6451  N   SER Z  90       5.168  39.416  70.348  1.00 40.01           N  
-ATOM   6452  CA  SER Z  90       5.035  40.638  71.131  1.00 38.63           C  
-ATOM   6453  C   SER Z  90       3.582  41.062  71.324  1.00 37.30           C  
-ATOM   6454  O   SER Z  90       2.714  40.813  70.482  1.00 36.35           O  
-ATOM   6455  CB  SER Z  90       5.814  41.781  70.480  1.00 40.83           C  
-ATOM   6456  OG  SER Z  90       5.130  42.290  69.353  1.00 44.71           O  
-ATOM   6457  N   ARG Z  91       3.340  41.708  72.455  1.00 37.20           N  
-ATOM   6458  CA  ARG Z  91       2.024  42.198  72.834  1.00 36.06           C  
-ATOM   6459  C   ARG Z  91       1.459  43.200  71.829  1.00 33.28           C  
-ATOM   6460  O   ARG Z  91       0.262  43.202  71.545  1.00 32.59           O  
-ATOM   6461  CB  ARG Z  91       2.111  42.867  74.205  1.00 37.04           C  
-ATOM   6462  CG  ARG Z  91       0.855  43.618  74.622  1.00 37.73           C  
-ATOM   6463  CD  ARG Z  91      -0.292  42.676  74.927  1.00 37.02           C  
-ATOM   6464  NE  ARG Z  91      -1.405  43.410  75.515  1.00 42.80           N  
-ATOM   6465  CZ  ARG Z  91      -2.426  42.851  76.152  1.00 42.35           C  
-ATOM   6466  NH1 ARG Z  91      -2.492  41.534  76.291  1.00 42.76           N  
-ATOM   6467  NH2 ARG Z  91      -3.374  43.620  76.667  1.00 46.74           N  
-ATOM   6468  N   ALA Z  92       2.327  44.057  71.308  1.00 32.28           N  
-ATOM   6469  CA  ALA Z  92       1.911  45.075  70.357  1.00 32.22           C  
-ATOM   6470  C   ALA Z  92       1.311  44.459  69.101  1.00 32.27           C  
-ATOM   6471  O   ALA Z  92       0.360  44.988  68.544  1.00 31.84           O  
-ATOM   6472  CB  ALA Z  92       3.084  45.951  69.997  1.00 31.64           C  
-ATOM   6473  N   ASP Z  93       1.863  43.336  68.659  1.00 32.47           N  
-ATOM   6474  CA  ASP Z  93       1.357  42.690  67.455  1.00 32.69           C  
-ATOM   6475  C   ASP Z  93      -0.020  42.072  67.694  1.00 32.48           C  
-ATOM   6476  O   ASP Z  93      -0.876  42.091  66.818  1.00 31.55           O  
-ATOM   6477  CB  ASP Z  93       2.343  41.621  66.971  1.00 32.25           C  
-ATOM   6478  CG  ASP Z  93       3.655  42.219  66.486  1.00 35.76           C  
-ATOM   6479  OD1 ASP Z  93       3.754  43.460  66.454  1.00 31.26           O  
-ATOM   6480  OD2 ASP Z  93       4.582  41.455  66.130  1.00 35.36           O  
-ATOM   6481  N   ALA Z  94      -0.224  41.510  68.877  1.00 32.71           N  
-ATOM   6482  CA  ALA Z  94      -1.513  40.916  69.204  1.00 33.44           C  
-ATOM   6483  C   ALA Z  94      -2.550  42.041  69.249  1.00 33.06           C  
-ATOM   6484  O   ALA Z  94      -3.686  41.879  68.783  1.00 32.63           O  
-ATOM   6485  CB  ALA Z  94      -1.444  40.210  70.560  1.00 29.29           C  
-ATOM   6486  N   GLU Z  95      -2.157  43.179  69.814  1.00 31.80           N  
-ATOM   6487  CA  GLU Z  95      -3.076  44.305  69.906  1.00 31.38           C  
-ATOM   6488  C   GLU Z  95      -3.529  44.775  68.518  1.00 30.10           C  
-ATOM   6489  O   GLU Z  95      -4.710  45.063  68.317  1.00 29.12           O  
-ATOM   6490  CB  GLU Z  95      -2.437  45.464  70.657  1.00 29.11           C  
-ATOM   6491  CG  GLU Z  95      -2.024  45.138  72.083  1.00 36.78           C  
-ATOM   6492  CD  GLU Z  95      -1.397  46.327  72.796  1.00 39.14           C  
-ATOM   6493  OE1 GLU Z  95      -0.632  47.087  72.156  1.00 44.08           O  
-ATOM   6494  OE2 GLU Z  95      -1.659  46.499  74.001  1.00 46.42           O  
-ATOM   6495  N   ASN Z  96      -2.611  44.846  67.556  1.00 27.92           N  
-ATOM   6496  CA  ASN Z  96      -3.026  45.298  66.235  1.00 28.70           C  
-ATOM   6497  C   ASN Z  96      -3.939  44.292  65.546  1.00 26.06           C  
-ATOM   6498  O   ASN Z  96      -4.691  44.652  64.652  1.00 25.04           O  
-ATOM   6499  CB  ASN Z  96      -1.815  45.658  65.370  1.00 26.77           C  
-ATOM   6500  CG  ASN Z  96      -1.289  47.044  65.677  1.00 28.43           C  
-ATOM   6501  OD1 ASN Z  96      -2.065  47.980  65.917  1.00 27.82           O  
-ATOM   6502  ND2 ASN Z  96       0.026  47.193  65.668  1.00 30.22           N  
-ATOM   6503  N   ALA Z  97      -3.879  43.028  65.953  1.00 26.86           N  
-ATOM   6504  CA  ALA Z  97      -4.791  42.040  65.381  1.00 26.91           C  
-ATOM   6505  C   ALA Z  97      -6.178  42.328  66.003  1.00 26.84           C  
-ATOM   6506  O   ALA Z  97      -7.213  42.212  65.341  1.00 26.14           O  
-ATOM   6507  CB  ALA Z  97      -4.336  40.629  65.731  1.00 26.72           C  
-ATOM   6508  N   MET Z  98      -6.182  42.711  67.277  1.00 25.41           N  
-ATOM   6509  CA  MET Z  98      -7.428  43.029  67.967  1.00 27.31           C  
-ATOM   6510  C   MET Z  98      -8.082  44.280  67.373  1.00 27.91           C  
-ATOM   6511  O   MET Z  98      -9.300  44.341  67.255  1.00 28.98           O  
-ATOM   6512  CB  MET Z  98      -7.173  43.234  69.462  1.00 26.67           C  
-ATOM   6513  CG  MET Z  98      -6.903  41.946  70.225  1.00 27.67           C  
-ATOM   6514  SD  MET Z  98      -8.334  40.813  70.246  1.00 35.14           S  
-ATOM   6515  CE  MET Z  98      -9.235  41.532  71.611  1.00 30.74           C  
-ATOM   6516  N   ARG Z  99      -7.268  45.269  66.999  1.00 26.21           N  
-ATOM   6517  CA  ARG Z  99      -7.764  46.514  66.413  1.00 25.43           C  
-ATOM   6518  C   ARG Z  99      -8.203  46.421  64.951  1.00 25.21           C  
-ATOM   6519  O   ARG Z  99      -9.189  47.051  64.549  1.00 25.59           O  
-ATOM   6520  CB  ARG Z  99      -6.686  47.601  66.459  1.00 27.06           C  
-ATOM   6521  CG  ARG Z  99      -6.201  48.000  67.825  1.00 21.78           C  
-ATOM   6522  CD  ARG Z  99      -5.162  49.109  67.712  1.00 23.63           C  
-ATOM   6523  NE  ARG Z  99      -4.685  49.487  69.032  1.00 27.08           N  
-ATOM   6524  CZ  ARG Z  99      -3.449  49.273  69.467  1.00 30.87           C  
-ATOM   6525  NH1 ARG Z  99      -2.549  48.695  68.676  1.00 24.63           N  
-ATOM   6526  NH2 ARG Z  99      -3.129  49.592  70.712  1.00 29.97           N  
-ATOM   6527  N   TYR Z 100      -7.481  45.638  64.156  1.00 23.59           N  
-ATOM   6528  CA  TYR Z 100      -7.761  45.590  62.724  1.00 25.46           C  
-ATOM   6529  C   TYR Z 100      -8.117  44.295  62.032  1.00 27.48           C  
-ATOM   6530  O   TYR Z 100      -8.552  44.327  60.875  1.00 28.64           O  
-ATOM   6531  CB  TYR Z 100      -6.587  46.234  61.982  1.00 23.95           C  
-ATOM   6532  CG  TYR Z 100      -6.163  47.544  62.605  1.00 19.32           C  
-ATOM   6533  CD1 TYR Z 100      -7.039  48.630  62.651  1.00 21.88           C  
-ATOM   6534  CD2 TYR Z 100      -4.906  47.684  63.191  1.00 17.38           C  
-ATOM   6535  CE1 TYR Z 100      -6.671  49.821  63.273  1.00 19.02           C  
-ATOM   6536  CE2 TYR Z 100      -4.533  48.865  63.813  1.00 17.37           C  
-ATOM   6537  CZ  TYR Z 100      -5.420  49.927  63.855  1.00 21.53           C  
-ATOM   6538  OH  TYR Z 100      -5.063  51.084  64.506  1.00 19.27           O  
-ATOM   6539  N   ILE Z 101      -7.931  43.158  62.691  1.00 27.67           N  
-ATOM   6540  CA  ILE Z 101      -8.269  41.903  62.042  1.00 27.09           C  
-ATOM   6541  C   ILE Z 101      -9.601  41.427  62.585  1.00 27.76           C  
-ATOM   6542  O   ILE Z 101     -10.438  40.891  61.859  1.00 28.58           O  
-ATOM   6543  CB  ILE Z 101      -7.169  40.846  62.270  1.00 29.39           C  
-ATOM   6544  CG1 ILE Z 101      -5.889  41.288  61.542  1.00 29.07           C  
-ATOM   6545  CG2 ILE Z 101      -7.630  39.486  61.746  1.00 25.28           C  
-ATOM   6546  CD1 ILE Z 101      -4.735  40.305  61.666  1.00 35.10           C  
-ATOM   6547  N   ASN Z 102      -9.779  41.657  63.875  1.00 27.88           N  
-ATOM   6548  CA  ASN Z 102     -10.986  41.319  64.596  1.00 29.23           C  
-ATOM   6549  C   ASN Z 102     -12.174  41.965  63.873  1.00 29.52           C  
-ATOM   6550  O   ASN Z 102     -12.090  43.103  63.428  1.00 28.62           O  
-ATOM   6551  CB  ASN Z 102     -10.857  41.864  66.019  1.00 31.24           C  
-ATOM   6552  CG  ASN Z 102     -12.059  41.548  66.888  1.00 34.17           C  
-ATOM   6553  OD1 ASN Z 102     -12.825  40.614  66.621  1.00 37.70           O  
-ATOM   6554  ND2 ASN Z 102     -12.218  42.319  67.952  1.00 35.59           N  
-ATOM   6555  N   GLY Z 103     -13.275  41.235  63.743  1.00 29.54           N  
-ATOM   6556  CA  GLY Z 103     -14.425  41.801  63.061  1.00 29.81           C  
-ATOM   6557  C   GLY Z 103     -14.303  41.876  61.542  1.00 29.61           C  
-ATOM   6558  O   GLY Z 103     -15.081  42.576  60.915  1.00 26.44           O  
-ATOM   6559  N   THR Z 104     -13.324  41.189  60.944  1.00 29.31           N  
-ATOM   6560  CA  THR Z 104     -13.202  41.195  59.485  1.00 27.90           C  
-ATOM   6561  C   THR Z 104     -13.352  39.759  58.984  1.00 28.96           C  
-ATOM   6562  O   THR Z 104     -13.492  38.831  59.783  1.00 27.07           O  
-ATOM   6563  CB  THR Z 104     -11.856  41.801  58.982  1.00 29.61           C  
-ATOM   6564  OG1 THR Z 104     -10.769  40.936  59.330  1.00 25.16           O  
-ATOM   6565  CG2 THR Z 104     -11.635  43.181  59.587  1.00 25.39           C  
-ATOM   6566  N   ARG Z 105     -13.306  39.565  57.669  1.00 29.65           N  
-ATOM   6567  CA  ARG Z 105     -13.527  38.231  57.108  1.00 34.46           C  
-ATOM   6568  C   ARG Z 105     -12.357  37.275  56.870  1.00 37.76           C  
-ATOM   6569  O   ARG Z 105     -11.227  37.674  56.559  1.00 36.51           O  
-ATOM   6570  CB  ARG Z 105     -14.338  38.349  55.800  1.00 33.24           C  
-ATOM   6571  CG  ARG Z 105     -15.727  38.964  55.990  1.00 36.60           C  
-ATOM   6572  CD  ARG Z 105     -16.569  38.924  54.711  1.00 39.84           C  
-ATOM   6573  NE  ARG Z 105     -17.751  39.778  54.824  1.00 43.63           N  
-ATOM   6574  CZ  ARG Z 105     -18.908  39.410  55.366  1.00 46.78           C  
-ATOM   6575  NH1 ARG Z 105     -19.066  38.184  55.852  1.00 43.31           N  
-ATOM   6576  NH2 ARG Z 105     -19.912  40.278  55.422  1.00 50.13           N  
-ATOM   6577  N   LEU Z 106     -12.681  35.994  57.016  1.00 39.37           N  
-ATOM   6578  CA  LEU Z 106     -11.764  34.886  56.806  1.00 40.11           C  
-ATOM   6579  C   LEU Z 106     -12.692  33.792  56.274  1.00 40.86           C  
-ATOM   6580  O   LEU Z 106     -13.516  33.253  57.020  1.00 38.89           O  
-ATOM   6581  CB  LEU Z 106     -11.137  34.447  58.127  1.00 40.33           C  
-ATOM   6582  CG  LEU Z 106      -9.722  33.869  58.045  1.00 45.00           C  
-ATOM   6583  CD1 LEU Z 106      -9.432  33.040  59.292  1.00 40.15           C  
-ATOM   6584  CD2 LEU Z 106      -9.585  33.017  56.802  1.00 47.93           C  
-ATOM   6585  N   ASP Z 107     -12.573  33.487  54.983  1.00 43.54           N  
-ATOM   6586  CA  ASP Z 107     -13.425  32.489  54.329  1.00 44.76           C  
-ATOM   6587  C   ASP Z 107     -14.860  33.016  54.246  1.00 46.00           C  
-ATOM   6588  O   ASP Z 107     -15.836  32.270  54.386  1.00 45.36           O  
-ATOM   6589  CB  ASP Z 107     -13.391  31.164  55.094  1.00 49.12           C  
-ATOM   6590  CG  ASP Z 107     -12.262  30.252  54.638  1.00 54.50           C  
-ATOM   6591  OD1 ASP Z 107     -11.981  29.261  55.349  1.00 55.96           O  
-ATOM   6592  OD2 ASP Z 107     -11.666  30.522  53.569  1.00 55.27           O  
-ATOM   6593  N   ASP Z 108     -14.961  34.321  54.017  1.00 45.13           N  
-ATOM   6594  CA  ASP Z 108     -16.228  35.027  53.898  1.00 44.14           C  
-ATOM   6595  C   ASP Z 108     -17.051  35.021  55.179  1.00 42.19           C  
-ATOM   6596  O   ASP Z 108     -18.255  35.269  55.153  1.00 43.33           O  
-ATOM   6597  CB  ASP Z 108     -17.051  34.467  52.729  1.00 47.01           C  
-ATOM   6598  CG  ASP Z 108     -18.240  35.351  52.380  1.00 48.73           C  
-ATOM   6599  OD1 ASP Z 108     -18.073  36.588  52.380  1.00 47.28           O  
-ATOM   6600  OD2 ASP Z 108     -19.335  34.813  52.103  1.00 53.67           O  
-ATOM   6601  N   ARG Z 109     -16.392  34.748  56.301  1.00 41.22           N  
-ATOM   6602  CA  ARG Z 109     -17.048  34.745  57.603  1.00 38.41           C  
-ATOM   6603  C   ARG Z 109     -16.433  35.840  58.478  1.00 37.95           C  
-ATOM   6604  O   ARG Z 109     -15.219  36.022  58.470  1.00 36.50           O  
-ATOM   6605  CB  ARG Z 109     -16.856  33.396  58.303  1.00 38.36           C  
-ATOM   6606  CG  ARG Z 109     -17.351  32.170  57.538  1.00 39.78           C  
-ATOM   6607  CD  ARG Z 109     -17.070  30.906  58.341  1.00 38.71           C  
-ATOM   6608  NE  ARG Z 109     -17.789  30.895  59.614  1.00 45.85           N  
-ATOM   6609  CZ  ARG Z 109     -19.040  30.466  59.766  1.00 46.53           C  
-ATOM   6610  NH1 ARG Z 109     -19.710  30.002  58.722  1.00 46.55           N  
-ATOM   6611  NH2 ARG Z 109     -19.626  30.517  60.956  1.00 43.44           N  
-ATOM   6612  N   ILE Z 110     -17.272  36.569  59.215  1.00 36.70           N  
-ATOM   6613  CA  ILE Z 110     -16.798  37.608  60.125  1.00 36.31           C  
-ATOM   6614  C   ILE Z 110     -16.261  36.872  61.358  1.00 37.34           C  
-ATOM   6615  O   ILE Z 110     -17.003  36.172  62.050  1.00 35.37           O  
-ATOM   6616  CB  ILE Z 110     -17.954  38.552  60.570  1.00 38.51           C  
-ATOM   6617  CG1 ILE Z 110     -18.464  39.368  59.375  1.00 35.56           C  
-ATOM   6618  CG2 ILE Z 110     -17.488  39.470  61.699  1.00 32.98           C  
-ATOM   6619  CD1 ILE Z 110     -17.451  40.377  58.809  1.00 34.86           C  
-ATOM   6620  N   ILE Z 111     -14.970  37.003  61.630  1.00 36.65           N  
-ATOM   6621  CA  ILE Z 111     -14.405  36.324  62.787  1.00 34.28           C  
-ATOM   6622  C   ILE Z 111     -14.282  37.276  63.965  1.00 32.87           C  
-ATOM   6623  O   ILE Z 111     -14.278  38.487  63.803  1.00 33.08           O  
-ATOM   6624  CB  ILE Z 111     -13.019  35.733  62.476  1.00 37.49           C  
-ATOM   6625  CG1 ILE Z 111     -12.025  36.863  62.197  1.00 36.22           C  
-ATOM   6626  CG2 ILE Z 111     -13.121  34.775  61.291  1.00 31.58           C  
-ATOM   6627  CD1 ILE Z 111     -10.607  36.397  61.994  1.00 42.88           C  
-ATOM   6628  N   ARG Z 112     -14.187  36.712  65.157  1.00 34.91           N  
-ATOM   6629  CA  ARG Z 112     -14.062  37.499  66.373  1.00 35.13           C  
-ATOM   6630  C   ARG Z 112     -12.804  37.098  67.137  1.00 33.93           C  
-ATOM   6631  O   ARG Z 112     -12.504  35.916  67.276  1.00 34.17           O  
-ATOM   6632  CB  ARG Z 112     -15.287  37.285  67.270  1.00 35.21           C  
-ATOM   6633  CG  ARG Z 112     -15.096  37.825  68.669  1.00 38.03           C  
-ATOM   6634  CD  ARG Z 112     -16.343  37.692  69.524  1.00 42.18           C  
-ATOM   6635  NE  ARG Z 112     -16.014  37.735  70.947  1.00 44.13           N  
-ATOM   6636  CZ  ARG Z 112     -15.591  36.685  71.647  1.00 47.70           C  
-ATOM   6637  NH1 ARG Z 112     -15.454  35.504  71.056  1.00 48.47           N  
-ATOM   6638  NH2 ARG Z 112     -15.296  36.814  72.936  1.00 48.25           N  
-ATOM   6639  N   THR Z 113     -12.065  38.086  67.625  1.00 32.56           N  
-ATOM   6640  CA  THR Z 113     -10.864  37.793  68.389  1.00 32.55           C  
-ATOM   6641  C   THR Z 113     -11.086  38.256  69.822  1.00 33.27           C  
-ATOM   6642  O   THR Z 113     -11.856  39.175  70.064  1.00 31.86           O  
-ATOM   6643  CB  THR Z 113      -9.625  38.501  67.789  1.00 32.83           C  
-ATOM   6644  OG1 THR Z 113      -9.771  39.927  67.894  1.00 30.92           O  
-ATOM   6645  CG2 THR Z 113      -9.453  38.103  66.322  1.00 28.18           C  
-ATOM   6646  N   ASP Z 114     -10.426  37.598  70.767  1.00 34.25           N  
-ATOM   6647  CA  ASP Z 114     -10.535  37.950  72.177  1.00 34.91           C  
-ATOM   6648  C   ASP Z 114      -9.217  37.608  72.857  1.00 35.75           C  
-ATOM   6649  O   ASP Z 114      -8.533  36.658  72.455  1.00 37.51           O  
-ATOM   6650  CB  ASP Z 114     -11.686  37.165  72.829  1.00 34.24           C  
-ATOM   6651  CG  ASP Z 114     -11.891  37.519  74.295  1.00 33.48           C  
-ATOM   6652  OD1 ASP Z 114     -11.888  38.723  74.631  1.00 38.95           O  
-ATOM   6653  OD2 ASP Z 114     -12.065  36.591  75.114  1.00 40.87           O  
-ATOM   6654  N   TRP Z 115      -8.847  38.387  73.866  1.00 35.80           N  
-ATOM   6655  CA  TRP Z 115      -7.621  38.116  74.596  1.00 37.72           C  
-ATOM   6656  C   TRP Z 115      -7.778  36.757  75.266  1.00 40.00           C  
-ATOM   6657  O   TRP Z 115      -8.894  36.366  75.636  1.00 40.65           O  
-ATOM   6658  CB  TRP Z 115      -7.377  39.189  75.662  1.00 35.59           C  
-ATOM   6659  CG  TRP Z 115      -6.923  40.501  75.097  1.00 37.57           C  
-ATOM   6660  CD1 TRP Z 115      -7.624  41.675  75.066  1.00 38.92           C  
-ATOM   6661  CD2 TRP Z 115      -5.677  40.760  74.435  1.00 35.59           C  
-ATOM   6662  NE1 TRP Z 115      -6.892  42.648  74.422  1.00 36.66           N  
-ATOM   6663  CE2 TRP Z 115      -5.695  42.114  74.024  1.00 35.15           C  
-ATOM   6664  CE3 TRP Z 115      -4.547  39.978  74.146  1.00 34.68           C  
-ATOM   6665  CZ2 TRP Z 115      -4.623  42.705  73.335  1.00 36.45           C  
-ATOM   6666  CZ3 TRP Z 115      -3.480  40.568  73.458  1.00 37.03           C  
-ATOM   6667  CH2 TRP Z 115      -3.528  41.918  73.062  1.00 31.27           C  
-ATOM   6668  N   ASP Z 116      -6.674  36.027  75.400  1.00 39.60           N  
-ATOM   6669  CA  ASP Z 116      -6.705  34.724  76.048  1.00 41.91           C  
-ATOM   6670  C   ASP Z 116      -5.653  34.700  77.154  1.00 43.52           C  
-ATOM   6671  O   ASP Z 116      -4.588  35.307  77.020  1.00 43.41           O  
-ATOM   6672  CB  ASP Z 116      -6.432  33.620  75.032  1.00 41.35           C  
-ATOM   6673  CG  ASP Z 116      -6.742  32.247  75.582  1.00 47.38           C  
-ATOM   6674  OD1 ASP Z 116      -5.801  31.444  75.772  1.00 47.84           O  
-ATOM   6675  OD2 ASP Z 116      -7.937  31.979  75.831  1.00 46.91           O  
-ATOM   6676  N   ALA Z 117      -5.950  34.004  78.247  1.00 44.57           N  
-ATOM   6677  CA  ALA Z 117      -5.026  33.934  79.375  1.00 44.45           C  
-ATOM   6678  C   ALA Z 117      -3.753  33.136  79.081  1.00 44.27           C  
-ATOM   6679  O   ALA Z 117      -2.748  33.306  79.762  1.00 42.68           O  
-ATOM   6680  CB  ALA Z 117      -5.740  33.350  80.594  1.00 46.58           C  
-ATOM   6681  N   GLY Z 118      -3.800  32.275  78.066  1.00 46.06           N  
-ATOM   6682  CA  GLY Z 118      -2.653  31.450  77.706  1.00 46.31           C  
-ATOM   6683  C   GLY Z 118      -3.071  30.009  77.437  1.00 48.19           C  
-ATOM   6684  O   GLY Z 118      -3.905  29.465  78.158  1.00 47.49           O  
-ATOM   6685  N   PHE Z 119      -2.499  29.387  76.406  1.00 49.89           N  
-ATOM   6686  CA  PHE Z 119      -2.842  28.009  76.052  1.00 52.64           C  
-ATOM   6687  C   PHE Z 119      -2.412  26.948  77.064  1.00 54.34           C  
-ATOM   6688  O   PHE Z 119      -1.393  27.086  77.743  1.00 54.68           O  
-ATOM   6689  CB  PHE Z 119      -2.241  27.630  74.703  1.00 53.99           C  
-ATOM   6690  CG  PHE Z 119      -2.491  26.195  74.320  1.00 58.38           C  
-ATOM   6691  CD1 PHE Z 119      -3.732  25.792  73.841  1.00 61.41           C  
-ATOM   6692  CD2 PHE Z 119      -1.498  25.235  74.483  1.00 60.89           C  
-ATOM   6693  CE1 PHE Z 119      -3.983  24.449  73.532  1.00 62.21           C  
-ATOM   6694  CE2 PHE Z 119      -1.737  23.891  74.177  1.00 59.75           C  
-ATOM   6695  CZ  PHE Z 119      -2.982  23.498  73.701  1.00 61.55           C  
-ATOM   6696  N   LYS Z 120      -3.199  25.880  77.141  1.00 54.62           N  
-ATOM   6697  CA  LYS Z 120      -2.922  24.756  78.030  1.00 54.82           C  
-ATOM   6698  C   LYS Z 120      -3.463  23.506  77.341  1.00 55.10           C  
-ATOM   6699  O   LYS Z 120      -4.335  23.599  76.473  1.00 53.85           O  
-ATOM   6700  CB  LYS Z 120      -3.614  24.947  79.380  1.00 54.67           C  
-ATOM   6701  CG  LYS Z 120      -3.144  26.159  80.177  1.00 57.41           C  
-ATOM   6702  CD  LYS Z 120      -1.714  26.003  80.682  1.00 60.90           C  
-ATOM   6703  CE  LYS Z 120      -1.347  27.126  81.647  1.00 63.73           C  
-ATOM   6704  NZ  LYS Z 120       0.018  26.973  82.229  1.00 66.29           N  
-ATOM   6705  N   GLU Z 121      -2.945  22.339  77.711  1.00 55.10           N  
-ATOM   6706  CA  GLU Z 121      -3.412  21.100  77.097  1.00 55.44           C  
-ATOM   6707  C   GLU Z 121      -4.892  20.873  77.367  1.00 54.06           C  
-ATOM   6708  O   GLU Z 121      -5.354  21.005  78.499  1.00 52.70           O  
-ATOM   6709  CB  GLU Z 121      -2.612  19.901  77.607  1.00 56.81           C  
-ATOM   6710  CG  GLU Z 121      -1.684  19.323  76.566  1.00 61.46           C  
-ATOM   6711  CD  GLU Z 121      -2.388  19.066  75.248  1.00 63.54           C  
-ATOM   6712  OE1 GLU Z 121      -3.452  18.411  75.260  1.00 61.87           O  
-ATOM   6713  OE2 GLU Z 121      -1.870  19.518  74.202  1.00 65.95           O  
-ATOM   6714  N   GLY Z 122      -5.629  20.530  76.316  1.00 54.95           N  
-ATOM   6715  CA  GLY Z 122      -7.056  20.292  76.460  1.00 54.77           C  
-ATOM   6716  C   GLY Z 122      -7.910  21.478  76.041  1.00 53.24           C  
-ATOM   6717  O   GLY Z 122      -9.052  21.307  75.604  1.00 53.57           O  
-ATOM   6718  N   ARG Z 123      -7.358  22.682  76.164  1.00 52.36           N  
-ATOM   6719  CA  ARG Z 123      -8.094  23.885  75.803  1.00 50.87           C  
-ATOM   6720  C   ARG Z 123      -8.332  24.017  74.311  1.00 50.32           C  
-ATOM   6721  O   ARG Z 123      -9.016  24.938  73.870  1.00 49.86           O  
-ATOM   6722  CB  ARG Z 123      -7.368  25.125  76.309  1.00 48.40           C  
-ATOM   6723  CG  ARG Z 123      -7.401  25.287  77.810  1.00 49.32           C  
-ATOM   6724  CD  ARG Z 123      -7.181  26.739  78.162  1.00 52.89           C  
-ATOM   6725  NE  ARG Z 123      -8.216  27.580  77.566  1.00 52.99           N  
-ATOM   6726  CZ  ARG Z 123      -8.064  28.873  77.293  1.00 53.16           C  
-ATOM   6727  NH1 ARG Z 123      -6.914  29.482  77.560  1.00 48.68           N  
-ATOM   6728  NH2 ARG Z 123      -9.062  29.557  76.746  1.00 45.87           N  
-ATOM   6729  N   GLN Z 124      -7.777  23.097  73.531  1.00 50.24           N  
-ATOM   6730  CA  GLN Z 124      -7.953  23.140  72.086  1.00 50.33           C  
-ATOM   6731  C   GLN Z 124      -9.144  22.300  71.635  1.00 50.33           C  
-ATOM   6732  O   GLN Z 124      -9.407  22.182  70.438  1.00 50.12           O  
-ATOM   6733  CB  GLN Z 124      -6.700  22.630  71.374  1.00 51.65           C  
-ATOM   6734  CG  GLN Z 124      -6.492  21.124  71.480  1.00 50.32           C  
-ATOM   6735  CD  GLN Z 124      -5.637  20.729  72.666  1.00 52.84           C  
-ATOM   6736  OE1 GLN Z 124      -5.882  21.151  73.797  1.00 51.13           O  
-ATOM   6737  NE2 GLN Z 124      -4.621  19.908  72.411  1.00 55.56           N  
-ATOM   6738  N   TYR Z 125      -9.862  21.712  72.585  1.00 50.85           N  
-ATOM   6739  CA  TYR Z 125     -11.003  20.872  72.239  1.00 52.32           C  
-ATOM   6740  C   TYR Z 125     -12.347  21.523  72.531  1.00 52.38           C  
-ATOM   6741  O   TYR Z 125     -12.461  22.359  73.423  1.00 51.34           O  
-ATOM   6742  CB  TYR Z 125     -10.914  19.533  72.980  1.00 53.85           C  
-ATOM   6743  CG  TYR Z 125      -9.665  18.748  72.660  1.00 56.18           C  
-ATOM   6744  CD1 TYR Z 125      -8.672  18.552  73.623  1.00 56.51           C  
-ATOM   6745  CD2 TYR Z 125      -9.469  18.208  71.388  1.00 57.77           C  
-ATOM   6746  CE1 TYR Z 125      -7.510  17.835  73.325  1.00 57.40           C  
-ATOM   6747  CE2 TYR Z 125      -8.316  17.491  71.077  1.00 61.64           C  
-ATOM   6748  CZ  TYR Z 125      -7.342  17.309  72.047  1.00 61.74           C  
-ATOM   6749  OH  TYR Z 125      -6.201  16.612  71.724  1.00 65.79           O  
-ATOM   6750  N   GLY Z 126     -13.363  21.139  71.765  1.00 54.25           N  
-ATOM   6751  CA  GLY Z 126     -14.691  21.684  71.983  1.00 56.62           C  
-ATOM   6752  C   GLY Z 126     -15.274  21.168  73.289  1.00 57.93           C  
-ATOM   6753  O   GLY Z 126     -15.335  19.955  73.515  1.00 58.30           O  
-ATOM   6754  N   ARG Z 127     -15.687  22.086  74.157  1.00 57.98           N  
-ATOM   6755  CA  ARG Z 127     -16.269  21.713  75.440  1.00 59.14           C  
-ATOM   6756  C   ARG Z 127     -17.756  21.384  75.297  1.00 60.97           C  
-ATOM   6757  O   ARG Z 127     -18.468  21.233  76.292  1.00 60.70           O  
-ATOM   6758  CB  ARG Z 127     -16.080  22.844  76.451  1.00 57.48           C  
-ATOM   6759  CG  ARG Z 127     -14.636  23.095  76.799  1.00 56.33           C  
-ATOM   6760  CD  ARG Z 127     -14.475  24.310  77.687  1.00 58.13           C  
-ATOM   6761  NE  ARG Z 127     -13.070  24.557  78.004  1.00 57.43           N  
-ATOM   6762  CZ  ARG Z 127     -12.629  25.616  78.675  1.00 58.37           C  
-ATOM   6763  NH1 ARG Z 127     -13.484  26.533  79.100  1.00 53.75           N  
-ATOM   6764  NH2 ARG Z 127     -11.334  25.756  78.928  1.00 60.21           N  
-ATOM   6765  N   GLY Z 128     -18.214  21.270  74.053  1.00 62.15           N  
-ATOM   6766  CA  GLY Z 128     -19.609  20.957  73.803  1.00 63.39           C  
-ATOM   6767  C   GLY Z 128     -19.933  19.491  74.037  1.00 64.36           C  
-ATOM   6768  O   GLY Z 128     -19.130  18.611  73.719  1.00 63.66           O  
-ATOM   6769  N   ARG Z 129     -21.116  19.232  74.590  1.00 64.51           N  
-ATOM   6770  CA  ARG Z 129     -21.566  17.873  74.876  1.00 65.45           C  
-ATOM   6771  C   ARG Z 129     -21.365  16.950  73.670  1.00 64.41           C  
-ATOM   6772  O   ARG Z 129     -20.951  15.803  73.820  1.00 64.74           O  
-ATOM   6773  CB  ARG Z 129     -23.045  17.892  75.273  1.00 69.72           C  
-ATOM   6774  CG  ARG Z 129     -23.574  16.586  75.858  1.00 76.59           C  
-ATOM   6775  CD  ARG Z 129     -25.069  16.684  76.168  1.00 81.95           C  
-ATOM   6776  NE  ARG Z 129     -25.567  15.503  76.873  1.00 86.70           N  
-ATOM   6777  CZ  ARG Z 129     -26.847  15.289  77.170  1.00 89.48           C  
-ATOM   6778  NH1 ARG Z 129     -27.770  16.178  76.820  1.00 90.58           N  
-ATOM   6779  NH2 ARG Z 129     -27.207  14.186  77.818  1.00 88.87           N  
-ATOM   6780  N   SER Z 130     -21.654  17.457  72.477  1.00 63.10           N  
-ATOM   6781  CA  SER Z 130     -21.499  16.674  71.253  1.00 63.20           C  
-ATOM   6782  C   SER Z 130     -20.046  16.615  70.781  1.00 62.93           C  
-ATOM   6783  O   SER Z 130     -19.730  15.944  69.793  1.00 62.31           O  
-ATOM   6784  CB  SER Z 130     -22.360  17.270  70.140  1.00 64.14           C  
-ATOM   6785  OG  SER Z 130     -21.999  18.620  69.895  1.00 69.65           O  
-ATOM   6786  N   GLY Z 131     -19.165  17.327  71.480  1.00 62.27           N  
-ATOM   6787  CA  GLY Z 131     -17.763  17.327  71.103  1.00 61.62           C  
-ATOM   6788  C   GLY Z 131     -17.249  18.665  70.600  1.00 60.05           C  
-ATOM   6789  O   GLY Z 131     -16.157  19.089  70.979  1.00 61.63           O  
-ATOM   6790  N   GLY Z 132     -18.026  19.326  69.744  1.00 58.08           N  
-ATOM   6791  CA  GLY Z 132     -17.620  20.619  69.214  1.00 54.36           C  
-ATOM   6792  C   GLY Z 132     -17.758  21.734  70.235  1.00 52.14           C  
-ATOM   6793  O   GLY Z 132     -17.814  21.480  71.440  1.00 51.13           O  
-ATOM   6794  N   GLN Z 133     -17.816  22.974  69.758  1.00 50.56           N  
-ATOM   6795  CA  GLN Z 133     -17.945  24.125  70.648  1.00 50.45           C  
-ATOM   6796  C   GLN Z 133     -19.337  24.240  71.271  1.00 49.55           C  
-ATOM   6797  O   GLN Z 133     -20.336  23.867  70.658  1.00 49.54           O  
-ATOM   6798  CB  GLN Z 133     -17.611  25.426  69.901  1.00 48.91           C  
-ATOM   6799  CG  GLN Z 133     -16.118  25.745  69.821  1.00 46.74           C  
-ATOM   6800  CD  GLN Z 133     -15.834  27.136  69.260  1.00 42.25           C  
-ATOM   6801  OE1 GLN Z 133     -15.885  27.359  68.049  1.00 44.97           O  
-ATOM   6802  NE2 GLN Z 133     -15.540  28.079  70.147  1.00 39.56           N  
-ATOM   6803  N   VAL Z 134     -19.385  24.762  72.491  1.00 48.84           N  
-ATOM   6804  CA  VAL Z 134     -20.631  24.947  73.221  1.00 51.63           C  
-ATOM   6805  C   VAL Z 134     -21.700  25.661  72.384  1.00 52.31           C  
-ATOM   6806  O   VAL Z 134     -22.818  25.159  72.229  1.00 50.51           O  
-ATOM   6807  CB  VAL Z 134     -20.386  25.763  74.513  1.00 52.45           C  
-ATOM   6808  CG1 VAL Z 134     -21.700  26.024  75.233  1.00 52.11           C  
-ATOM   6809  CG2 VAL Z 134     -19.427  25.018  75.417  1.00 53.44           C  
-ATOM   6810  N   ARG Z 135     -21.340  26.827  71.851  1.00 51.70           N  
-ATOM   6811  CA  ARG Z 135     -22.244  27.634  71.044  1.00 53.61           C  
-ATOM   6812  C   ARG Z 135     -23.009  26.837  69.988  1.00 54.35           C  
-ATOM   6813  O   ARG Z 135     -24.188  27.098  69.744  1.00 54.11           O  
-ATOM   6814  CB  ARG Z 135     -21.473  28.769  70.350  1.00 55.37           C  
-ATOM   6815  CG  ARG Z 135     -22.373  29.757  69.604  1.00 62.75           C  
-ATOM   6816  CD  ARG Z 135     -21.590  30.830  68.838  1.00 69.68           C  
-ATOM   6817  NE  ARG Z 135     -20.862  30.289  67.689  1.00 72.26           N  
-ATOM   6818  CZ  ARG Z 135     -20.238  31.032  66.778  1.00 74.27           C  
-ATOM   6819  NH1 ARG Z 135     -20.250  32.357  66.872  1.00 75.09           N  
-ATOM   6820  NH2 ARG Z 135     -19.599  30.452  65.769  1.00 71.27           N  
-ATOM   6821  N   ASP Z 136     -22.346  25.875  69.356  1.00 53.54           N  
-ATOM   6822  CA  ASP Z 136     -22.997  25.084  68.319  1.00 56.64           C  
-ATOM   6823  C   ASP Z 136     -24.117  24.197  68.850  1.00 58.39           C  
-ATOM   6824  O   ASP Z 136     -24.950  23.707  68.084  1.00 58.47           O  
-ATOM   6825  CB  ASP Z 136     -21.966  24.237  67.579  1.00 56.89           C  
-ATOM   6826  CG  ASP Z 136     -20.933  25.083  66.871  1.00 57.29           C  
-ATOM   6827  OD1 ASP Z 136     -20.018  25.591  67.552  1.00 56.73           O  
-ATOM   6828  OD2 ASP Z 136     -21.050  25.252  65.638  1.00 55.56           O  
-ATOM   6829  N   GLU Z 137     -24.131  24.004  70.163  1.00 59.82           N  
-ATOM   6830  CA  GLU Z 137     -25.141  23.181  70.812  1.00 61.77           C  
-ATOM   6831  C   GLU Z 137     -26.493  23.889  70.832  1.00 62.90           C  
-ATOM   6832  O   GLU Z 137     -27.537  23.244  70.944  1.00 62.16           O  
-ATOM   6833  CB  GLU Z 137     -24.720  22.879  72.251  1.00 62.50           C  
-ATOM   6834  CG  GLU Z 137     -24.680  21.407  72.604  1.00 68.30           C  
-ATOM   6835  CD  GLU Z 137     -23.421  20.714  72.116  1.00 71.74           C  
-ATOM   6836  OE1 GLU Z 137     -23.336  19.477  72.252  1.00 74.44           O  
-ATOM   6837  OE2 GLU Z 137     -22.512  21.402  71.604  1.00 78.14           O  
-ATOM   6838  N   TYR Z 138     -26.472  25.214  70.708  1.00 63.15           N  
-ATOM   6839  CA  TYR Z 138     -27.700  25.996  70.760  1.00 63.98           C  
-ATOM   6840  C   TYR Z 138     -28.156  26.655  69.460  1.00 64.76           C  
-ATOM   6841  O   TYR Z 138     -29.331  26.977  69.318  1.00 65.72           O  
-ATOM   6842  CB  TYR Z 138     -27.579  27.079  71.837  1.00 63.46           C  
-ATOM   6843  CG  TYR Z 138     -27.165  26.564  73.197  1.00 65.03           C  
-ATOM   6844  CD1 TYR Z 138     -25.847  26.189  73.449  1.00 66.08           C  
-ATOM   6845  CD2 TYR Z 138     -28.094  26.441  74.230  1.00 65.91           C  
-ATOM   6846  CE1 TYR Z 138     -25.461  25.703  74.697  1.00 69.73           C  
-ATOM   6847  CE2 TYR Z 138     -27.722  25.954  75.483  1.00 69.27           C  
-ATOM   6848  CZ  TYR Z 138     -26.404  25.586  75.710  1.00 70.95           C  
-ATOM   6849  OH  TYR Z 138     -26.031  25.093  76.943  1.00 71.86           O  
-ATOM   6850  N   ARG Z 139     -27.252  26.864  68.511  1.00 65.74           N  
-ATOM   6851  CA  ARG Z 139     -27.657  27.518  67.270  1.00 66.45           C  
-ATOM   6852  C   ARG Z 139     -28.765  26.759  66.536  1.00 66.49           C  
-ATOM   6853  O   ARG Z 139     -28.718  25.534  66.400  1.00 65.82           O  
-ATOM   6854  CB  ARG Z 139     -26.446  27.744  66.361  1.00 66.16           C  
-ATOM   6855  CG  ARG Z 139     -25.755  26.498  65.891  1.00 65.81           C  
-ATOM   6856  CD  ARG Z 139     -24.430  26.855  65.251  1.00 62.95           C  
-ATOM   6857  NE  ARG Z 139     -23.929  25.753  64.446  1.00 63.27           N  
-ATOM   6858  CZ  ARG Z 139     -24.529  25.314  63.346  1.00 62.37           C  
-ATOM   6859  NH1 ARG Z 139     -25.646  25.894  62.925  1.00 62.82           N  
-ATOM   6860  NH2 ARG Z 139     -24.024  24.288  62.678  1.00 63.15           N  
-ATOM   6861  N   GLN Z 140     -29.763  27.510  66.073  1.00 66.50           N  
-ATOM   6862  CA  GLN Z 140     -30.925  26.953  65.380  1.00 67.00           C  
-ATOM   6863  C   GLN Z 140     -30.744  26.894  63.866  1.00 66.53           C  
-ATOM   6864  O   GLN Z 140     -31.170  25.943  63.209  1.00 66.37           O  
-ATOM   6865  CB  GLN Z 140     -32.159  27.810  65.683  1.00 68.18           C  
-ATOM   6866  CG  GLN Z 140     -32.258  28.292  67.123  1.00 68.40           C  
-ATOM   6867  CD  GLN Z 140     -33.196  27.457  67.966  1.00 69.34           C  
-ATOM   6868  OE1 GLN Z 140     -33.325  27.680  69.168  1.00 70.79           O  
-ATOM   6869  NE2 GLN Z 140     -33.864  26.495  67.342  1.00 69.84           N  
-ATOM   6870  N   ASP Z 141     -30.117  27.932  63.328  1.00 66.41           N  
-ATOM   6871  CA  ASP Z 141     -29.878  28.069  61.897  1.00 65.14           C  
-ATOM   6872  C   ASP Z 141     -29.059  26.947  61.281  1.00 63.24           C  
-ATOM   6873  O   ASP Z 141     -28.536  26.078  61.979  1.00 63.09           O  
-ATOM   6874  CB  ASP Z 141     -29.158  29.383  61.636  1.00 68.76           C  
-ATOM   6875  CG  ASP Z 141     -27.764  29.400  62.234  1.00 73.84           C  
-ATOM   6876  OD1 ASP Z 141     -27.641  29.207  63.463  1.00 75.96           O  
-ATOM   6877  OD2 ASP Z 141     -26.792  29.599  61.473  1.00 77.25           O  
-ATOM   6878  N   TYR Z 142     -28.952  26.988  59.957  1.00 60.73           N  
-ATOM   6879  CA  TYR Z 142     -28.175  26.010  59.205  1.00 59.63           C  
-ATOM   6880  C   TYR Z 142     -26.905  26.712  58.730  1.00 58.59           C  
-ATOM   6881  O   TYR Z 142     -26.950  27.563  57.840  1.00 58.43           O  
-ATOM   6882  CB  TYR Z 142     -28.968  25.512  57.995  1.00 58.33           C  
-ATOM   6883  CG  TYR Z 142     -28.166  24.655  57.034  1.00 56.23           C  
-ATOM   6884  CD1 TYR Z 142     -27.949  23.299  57.281  1.00 54.71           C  
-ATOM   6885  CD2 TYR Z 142     -27.632  25.206  55.870  1.00 56.18           C  
-ATOM   6886  CE1 TYR Z 142     -27.223  22.512  56.387  1.00 54.93           C  
-ATOM   6887  CE2 TYR Z 142     -26.905  24.433  54.973  1.00 58.50           C  
-ATOM   6888  CZ  TYR Z 142     -26.706  23.089  55.232  1.00 57.69           C  
-ATOM   6889  OH  TYR Z 142     -25.999  22.335  54.322  1.00 57.39           O  
-ATOM   6890  N   ASP Z 143     -25.776  26.358  59.335  1.00 57.58           N  
-ATOM   6891  CA  ASP Z 143     -24.494  26.960  58.982  1.00 55.39           C  
-ATOM   6892  C   ASP Z 143     -23.676  25.996  58.126  1.00 53.09           C  
-ATOM   6893  O   ASP Z 143     -23.064  25.064  58.640  1.00 50.55           O  
-ATOM   6894  CB  ASP Z 143     -23.716  27.313  60.251  1.00 55.23           C  
-ATOM   6895  CG  ASP Z 143     -22.544  28.235  59.980  1.00 54.48           C  
-ATOM   6896  OD1 ASP Z 143     -22.011  28.196  58.851  1.00 50.96           O  
-ATOM   6897  OD2 ASP Z 143     -22.149  28.988  60.898  1.00 53.31           O  
-ATOM   6898  N   ALA Z 144     -23.677  26.224  56.817  1.00 52.94           N  
-ATOM   6899  CA  ALA Z 144     -22.935  25.375  55.892  1.00 53.84           C  
-ATOM   6900  C   ALA Z 144     -21.475  25.214  56.326  1.00 54.22           C  
-ATOM   6901  O   ALA Z 144     -20.869  24.165  56.108  1.00 54.65           O  
-ATOM   6902  CB  ALA Z 144     -23.001  25.960  54.481  1.00 49.99           C  
-ATOM   6903  N   GLY Z 145     -20.922  26.254  56.945  1.00 53.93           N  
-ATOM   6904  CA  GLY Z 145     -19.537  26.206  57.382  1.00 53.76           C  
-ATOM   6905  C   GLY Z 145     -19.345  25.696  58.796  1.00 53.83           C  
-ATOM   6906  O   GLY Z 145     -18.235  25.730  59.329  1.00 53.08           O  
-ATOM   6907  N   ARG Z 146     -20.424  25.217  59.407  1.00 53.53           N  
-ATOM   6908  CA  ARG Z 146     -20.363  24.705  60.768  1.00 53.39           C  
-ATOM   6909  C   ARG Z 146     -21.009  23.334  60.891  1.00 54.73           C  
-ATOM   6910  O   ARG Z 146     -21.403  22.918  61.982  1.00 53.23           O  
-ATOM   6911  CB  ARG Z 146     -21.043  25.683  61.718  1.00 53.18           C  
-ATOM   6912  CG  ARG Z 146     -20.206  26.893  62.040  1.00 53.10           C  
-ATOM   6913  CD  ARG Z 146     -19.655  26.769  63.440  1.00 53.27           C  
-ATOM   6914  NE  ARG Z 146     -18.672  27.802  63.716  1.00 53.60           N  
-ATOM   6915  CZ  ARG Z 146     -18.011  27.918  64.860  1.00 53.50           C  
-ATOM   6916  NH1 ARG Z 146     -18.230  27.062  65.851  1.00 47.78           N  
-ATOM   6917  NH2 ARG Z 146     -17.118  28.886  65.003  1.00 55.10           N  
-ATOM   6918  N   GLY Z 147     -21.114  22.639  59.762  1.00 56.29           N  
-ATOM   6919  CA  GLY Z 147     -21.702  21.312  59.760  1.00 59.56           C  
-ATOM   6920  C   GLY Z 147     -23.191  21.281  59.470  1.00 60.97           C  
-ATOM   6921  O   GLY Z 147     -23.736  20.233  59.130  1.00 61.17           O  
-ATOM   6922  N   GLY Z 148     -23.851  22.425  59.611  1.00 62.15           N  
-ATOM   6923  CA  GLY Z 148     -25.276  22.487  59.352  1.00 63.62           C  
-ATOM   6924  C   GLY Z 148     -26.062  23.009  60.535  1.00 64.47           C  
-ATOM   6925  O   GLY Z 148     -25.948  24.179  60.894  1.00 65.00           O  
-ATOM   6926  N   TYR Z 149     -26.852  22.133  61.149  1.00 65.05           N  
-ATOM   6927  CA  TYR Z 149     -27.686  22.496  62.290  1.00 64.47           C  
-ATOM   6928  C   TYR Z 149     -26.943  22.342  63.616  1.00 64.34           C  
-ATOM   6929  O   TYR Z 149     -25.755  22.034  63.633  1.00 63.98           O  
-ATOM   6930  CB  TYR Z 149     -28.941  21.620  62.293  1.00 65.47           C  
-ATOM   6931  CG  TYR Z 149     -29.733  21.675  60.998  1.00 67.34           C  
-ATOM   6932  CD1 TYR Z 149     -30.590  22.745  60.722  1.00 65.40           C  
-ATOM   6933  CD2 TYR Z 149     -29.620  20.657  60.044  1.00 66.91           C  
-ATOM   6934  CE1 TYR Z 149     -31.318  22.797  59.527  1.00 67.34           C  
-ATOM   6935  CE2 TYR Z 149     -30.341  20.700  58.846  1.00 65.97           C  
-ATOM   6936  CZ  TYR Z 149     -31.188  21.772  58.595  1.00 67.63           C  
-ATOM   6937  OH  TYR Z 149     -31.904  21.819  57.417  1.00 67.28           O  
-ATOM   6938  N   GLY Z 150     -27.649  22.561  64.723  1.00 63.76           N  
-ATOM   6939  CA  GLY Z 150     -27.036  22.432  66.034  1.00 62.77           C  
-ATOM   6940  C   GLY Z 150     -27.311  21.080  66.667  1.00 62.33           C  
-TER    6941      GLY Z 150                                                      
-HETATM 6942  PB  GDP Z1151     -16.624  27.706  76.589  1.00 56.33           P  
-HETATM 6943  O1B GDP Z1151     -16.028  28.973  76.028  1.00 58.07           O  
-HETATM 6944  O2B GDP Z1151     -15.895  26.958  77.673  1.00 62.13           O  
-HETATM 6945  O3B GDP Z1151     -16.881  26.681  75.375  1.00 54.39           O  
-HETATM 6946  O3A GDP Z1151     -18.076  28.047  77.203  1.00 62.28           O  
-HETATM 6947  PA  GDP Z1151     -19.235  29.118  76.879  1.00 62.04           P  
-HETATM 6948  O1A GDP Z1151     -19.858  28.787  75.540  1.00 63.42           O  
-HETATM 6949  O2A GDP Z1151     -18.702  30.508  77.125  1.00 59.72           O  
-HETATM 6950  O5' GDP Z1151     -20.296  28.787  78.025  1.00 70.03           O  
-HETATM 6951  C5' GDP Z1151     -21.633  29.344  77.970  1.00 79.28           C  
-HETATM 6952  C4' GDP Z1151     -22.479  28.859  79.136  1.00 82.54           C  
-HETATM 6953  O4' GDP Z1151     -23.824  29.402  78.974  1.00 84.19           O  
-HETATM 6954  C3' GDP Z1151     -22.638  27.342  79.251  1.00 84.59           C  
-HETATM 6955  O3' GDP Z1151     -22.670  26.962  80.626  1.00 83.32           O  
-HETATM 6956  C2' GDP Z1151     -23.987  27.073  78.583  1.00 82.43           C  
-HETATM 6957  O2' GDP Z1151     -24.651  25.927  79.080  1.00 84.31           O  
-HETATM 6958  C1' GDP Z1151     -24.767  28.348  78.906  1.00 81.48           C  
-HETATM 6959  N9  GDP Z1151     -25.765  28.681  77.890  1.00 78.97           N  
-HETATM 6960  C8  GDP Z1151     -27.131  28.694  78.055  1.00 76.78           C  
-HETATM 6961  N7  GDP Z1151     -27.776  29.027  76.971  1.00 73.01           N  
-HETATM 6962  C5  GDP Z1151     -26.780  29.251  76.029  1.00 75.61           C  
-HETATM 6963  C6  GDP Z1151     -26.874  29.645  74.668  1.00 74.59           C  
-HETATM 6964  O6  GDP Z1151     -27.890  29.879  73.999  1.00 74.48           O  
-HETATM 6965  N1  GDP Z1151     -25.619  29.760  74.082  1.00 73.55           N  
-HETATM 6966  C2  GDP Z1151     -24.423  29.529  74.718  1.00 75.20           C  
-HETATM 6967  N2  GDP Z1151     -23.313  29.698  73.980  1.00 74.09           N  
-HETATM 6968  N3  GDP Z1151     -24.321  29.160  75.985  1.00 74.89           N  
-HETATM 6969  C4  GDP Z1151     -25.531  29.042  76.577  1.00 76.06           C  
-HETATM 6970  P   7MG Z1152     -16.051  26.281  74.048  1.00 56.47           P  
-HETATM 6971  OP1 7MG Z1152     -16.106  27.434  73.064  1.00 51.16           O  
-HETATM 6972  OP2 7MG Z1152     -16.512  24.910  73.604  1.00 49.31           O  
-HETATM 6973  O5' 7MG Z1152     -14.556  26.154  74.587  1.00 51.94           O  
-HETATM 6974  C5' 7MG Z1152     -13.488  25.692  73.730  1.00 48.85           C  
-HETATM 6975  C4' 7MG Z1152     -12.208  26.446  74.035  1.00 48.03           C  
-HETATM 6976  O4' 7MG Z1152     -12.293  27.789  73.490  1.00 47.93           O  
-HETATM 6977  C3' 7MG Z1152     -11.882  26.601  75.517  1.00 49.04           C  
-HETATM 6978  O3' 7MG Z1152     -10.476  26.509  75.715  1.00 53.22           O  
-HETATM 6979  C2' 7MG Z1152     -12.361  28.016  75.836  1.00 48.20           C  
-HETATM 6980  O2' 7MG Z1152     -11.672  28.625  76.915  1.00 43.00           O  
-HETATM 6981  C1' 7MG Z1152     -12.088  28.739  74.519  1.00 45.93           C  
-HETATM 6982  N9  7MG Z1152     -12.959  29.884  74.264  1.00 48.16           N  
-HETATM 6983  C8  7MG Z1152     -14.247  29.852  73.789  1.00 47.37           C  
-HETATM 6984  N7  7MG Z1152     -14.787  31.097  73.638  1.00 48.17           N  
-HETATM 6985  C5  7MG Z1152     -13.756  31.938  74.047  1.00 45.32           C  
-HETATM 6986  C6  7MG Z1152     -13.719  33.354  74.112  1.00 44.72           C  
-HETATM 6987  O6  7MG Z1152     -14.596  34.162  73.792  1.00 48.63           O  
-HETATM 6988  N1  7MG Z1152     -12.501  33.814  74.602  1.00 46.08           N  
-HETATM 6989  C2  7MG Z1152     -11.445  33.018  74.973  1.00 45.59           C  
-HETATM 6990  N2  7MG Z1152     -10.354  33.660  75.429  1.00 38.08           N  
-HETATM 6991  N3  7MG Z1152     -11.458  31.694  74.906  1.00 42.87           N  
-HETATM 6992  C4  7MG Z1152     -12.636  31.221  74.441  1.00 46.29           C  
-HETATM 6993  CM7 7MG Z1152     -16.116  31.436  73.163  1.00 42.72           C  
-HETATM 6994  O   HOH C2001     -13.439  66.385  87.576  1.00 51.39           O  
-HETATM 6995  O   HOH C2002     -11.396  65.132  71.393  1.00 39.12           O  
-HETATM 6996  O   HOH C2003     -11.207  65.068  68.770  1.00 46.10           O  
-HETATM 6997  O   HOH C2004     -22.637  72.798  66.277  1.00 58.02           O  
-HETATM 6998  O   HOH C2005     -17.654  83.310  83.347  1.00 48.62           O  
-HETATM 6999  O   HOH C2006       4.440  64.392  66.376  1.00 55.92           O  
-HETATM 7000  O   HOH C2007      -1.869  61.767  69.144  1.00 38.17           O  
-HETATM 7001  O   HOH C2008     -12.123  67.864  62.516  1.00 36.13           O  
-HETATM 7002  O   HOH C2009      -5.931  78.489  90.311  1.00 62.79           O  
-HETATM 7003  O   HOH C2010      -7.302  81.767  93.944  1.00 54.05           O  
-HETATM 7004  O   HOH C2011      -8.256  78.683  94.450  1.00 45.49           O  
-HETATM 7005  O   HOH C2012      -3.934  85.794  88.132  1.00 59.61           O  
-HETATM 7006  O   HOH C2013      -4.114  76.846  89.350  1.00 42.40           O  
-HETATM 7007  O   HOH C2014      -5.130  74.005  88.332  1.00 37.42           O  
-HETATM 7008  O   HOH C2015      -1.531  67.717  79.633  1.00 48.82           O  
-HETATM 7009  O   HOH C2016       4.357  66.030  58.573  1.00 58.83           O  
-HETATM 7010  O   HOH C2017       7.526  64.070  66.403  1.00 48.75           O  
-HETATM 7011  O   HOH C2018      -0.233  63.959  60.280  1.00 42.20           O  
-HETATM 7012  O   HOH C2019      26.574  73.286  63.703  1.00 54.17           O  
-HETATM 7013  O   HOH C2020      -3.148  73.156  66.856  1.00 26.25           O  
-HETATM 7014  O   HOH C2021       1.589  71.107  74.324  1.00 40.63           O  
-HETATM 7015  O   HOH C2022       0.522  66.131  67.650  1.00 43.02           O  
-HETATM 7016  O   HOH C2023      -3.063  63.947  67.738  1.00 35.17           O  
-HETATM 7017  O   HOH C2024      -5.385  72.556  67.798  1.00 27.90           O  
-HETATM 7018  O   HOH C2025      -5.817  72.730  61.086  1.00 30.17           O  
-HETATM 7019  O   HOH C2026     -10.779  69.531  60.931  1.00 46.90           O  
-HETATM 7020  O   HOH C2027      -9.406  74.207  62.371  1.00 47.98           O  
-HETATM 7021  O   HOH C2028      -8.549  87.937  72.300  1.00 39.51           O  
-HETATM 7022  O   HOH C2029     -15.537  86.410  75.613  1.00 44.58           O  
-HETATM 7023  O   HOH C2030      -4.103  92.324  86.806  1.00 59.14           O  
-HETATM 7024  O   HOH C2031      -1.084  90.823  82.427  1.00 51.44           O  
-HETATM 7025  O   HOH C2032       2.780  80.859  81.889  1.00 53.26           O  
-HETATM 7026  O   HOH C2033       1.089  58.799  37.928  1.00 54.04           O  
-HETATM 7027  O   HOH C2034      16.672  69.387  67.939  1.00 33.53           O  
-HETATM 7028  O   HOH C2035       4.761  68.658  60.997  1.00 46.14           O  
-HETATM 7029  O   HOH C2036       9.719  65.324  64.614  1.00 36.98           O  
-HETATM 7030  O   HOH C2037       8.310  63.430  59.354  1.00 40.52           O  
-HETATM 7031  O   HOH C2038       7.371  68.688  60.639  1.00 25.90           O  
-HETATM 7032  O   HOH C2039       6.560  67.926  71.739  1.00 47.77           O  
-HETATM 7033  O   HOH C2040       0.903  66.755  60.016  1.00 44.23           O  
-HETATM 7034  O   HOH C2041      -2.030  73.282  64.413  1.00 38.18           O  
-HETATM 7035  O   HOH C2042      25.572  75.729  64.086  1.00 49.39           O  
-HETATM 7036  O   HOH C2043      -2.697  72.571  61.586  1.00 42.63           O  
-HETATM 7037  O   HOH C2044      14.204  59.547  60.868  1.00 63.68           O  
-HETATM 7038  O   HOH C2045       8.659  59.706  57.855  1.00 37.43           O  
-HETATM 7039  O   HOH C2046       8.371  61.126  55.763  1.00 32.48           O  
-HETATM 7040  O   HOH C2047       3.824  64.303  52.075  1.00 37.20           O  
-HETATM 7041  O   HOH C2048      -7.007  67.322  32.371  1.00 59.03           O  
-HETATM 7042  O   HOH C2049      -6.909  71.916  38.975  1.00 59.13           O  
-HETATM 7043  O   HOH C2050      -4.712  86.004  58.127  1.00 47.65           O  
-HETATM 7044  O   HOH C2051       0.540  61.209  59.766  1.00 39.29           O  
-HETATM 7045  O   HOH C2052     -20.091  55.541  62.895  1.00 40.35           O  
-HETATM 7046  O   HOH C2053      16.929  86.769  60.801  1.00 65.84           O  
-HETATM 7047  O   HOH C2054     -19.841  61.745  63.166  1.00 52.45           O  
-HETATM 7048  O   HOH C2055     -18.629  66.984  52.322  1.00 60.11           O  
-HETATM 7049  O   HOH C2056      19.802  80.761  62.986  1.00 48.70           O  
-HETATM 7050  O   HOH C2057      27.512  75.391  54.650  1.00 63.70           O  
-HETATM 7051  O   HOH C2058       3.979  52.016  62.163  1.00 49.50           O  
-HETATM 7052  O   HOH C2059       3.494  44.070  60.271  1.00 46.22           O  
-HETATM 7053  O   HOH C2060     -20.839  51.357  60.120  1.00 50.18           O  
-HETATM 7054  O   HOH C2061      15.989  67.974  51.982  1.00 34.96           O  
-HETATM 7055  O   HOH C2062     -16.098  47.491  48.001  1.00 54.73           O  
-HETATM 7056  O   HOH C2063     -13.932  52.708  37.579  1.00 53.73           O  
-HETATM 7057  O   HOH C2064      16.404  73.989  66.257  1.00 44.57           O  
-HETATM 7058  O   HOH C2065       1.788  41.835  55.256  1.00 54.27           O  
-HETATM 7059  O   HOH C2066      -7.654  74.662  60.486  1.00 40.63           O  
-HETATM 7060  O   HOH C2067      -3.768  83.996  55.199  1.00 52.59           O  
-HETATM 7061  O   HOH C2068     -18.653  46.727  47.822  1.00 56.23           O  
-HETATM 7062  O   HOH C2069      -6.581  89.067  58.006  1.00 61.71           O  
-HETATM 7063  O   HOH C2070       5.229  97.706  49.289  1.00 64.03           O  
-HETATM 7064  O   HOH C2071       5.386  33.280  38.430  1.00 64.36           O  
-HETATM 7065  O   HOH C2072      14.251  85.988  45.890  1.00 56.97           O  
-HETATM 7066  O   HOH C2073      10.277  86.432  46.668  1.00 53.82           O  
-HETATM 7067  O   HOH C2074      13.328  73.768  46.612  1.00 31.16           O  
-HETATM 7068  O   HOH C2075      19.998  68.264  43.529  1.00 40.51           O  
-HETATM 7069  O   HOH C2076      18.965  61.188  42.709  1.00 47.20           O  
-HETATM 7070  O   HOH C2077      22.847  66.192  47.387  1.00 50.30           O  
-HETATM 7071  O   HOH C2078      19.110  66.252  48.646  1.00 47.00           O  
-HETATM 7072  O   HOH C2079       6.574  59.210  49.360  1.00 22.22           O  
-HETATM 7073  O   HOH C2080       8.756  55.806  41.555  1.00 38.74           O  
-HETATM 7074  O   HOH C2081       4.752  60.245  45.228  1.00 24.53           O  
-HETATM 7075  O   HOH C2082       6.430  62.087  39.192  1.00 43.52           O  
-HETATM 7076  O   HOH C2083       5.795  61.092  32.228  1.00 38.69           O  
-HETATM 7077  O   HOH C2084       7.112  67.975  35.813  1.00 59.23           O  
-HETATM 7078  O   HOH C2085       2.103  69.857  31.407  1.00 55.13           O  
-HETATM 7079  O   HOH C2086      -0.176  60.819  38.123  1.00 61.55           O  
-HETATM 7080  O   HOH C2087       2.525  65.805  43.725  1.00 26.94           O  
-HETATM 7081  O   HOH C2088       1.026  67.351  41.068  1.00 31.22           O  
-HETATM 7082  O   HOH C2089       0.779  67.811  43.866  1.00 33.95           O  
-HETATM 7083  O   HOH C2090       9.293  68.808  42.682  1.00 47.73           O  
-HETATM 7084  O   HOH C2091      10.655  69.628  57.185  1.00 30.79           O  
-HETATM 7085  O   HOH C2092      13.143  68.349  54.564  1.00 25.85           O  
-HETATM 7086  O   HOH C2093       4.019  70.471  51.390  1.00 25.81           O  
-HETATM 7087  O   HOH C2094      10.871  76.130  44.146  1.00 47.70           O  
-HETATM 7088  O   HOH C2095       2.057  78.841  42.081  1.00 42.10           O  
-HETATM 7089  O   HOH C2096      -0.120  69.504  48.663  1.00 27.28           O  
-HETATM 7090  O   HOH C2097       2.071  70.958  49.692  1.00 30.48           O  
-HETATM 7091  O   HOH C2098      -0.224  89.959  47.974  1.00 48.02           O  
-HETATM 7092  O   HOH C2099      -1.746  90.016  42.697  1.00 66.27           O  
-HETATM 7093  O   HOH C2100      -6.051  80.730  46.851  1.00 46.64           O  
-HETATM 7094  O   HOH C2101      18.925  35.522  41.574  1.00 39.05           O  
-HETATM 7095  O   HOH C2102      19.260  37.198  40.046  1.00 44.52           O  
-HETATM 7096  O   HOH C2103     -11.224  80.718  55.289  1.00 36.23           O  
-HETATM 7097  O   HOH C2104      -9.054  83.663  53.932  1.00 41.52           O  
-HETATM 7098  O   HOH C2105     -11.105  74.545  59.228  1.00 43.29           O  
-HETATM 7099  O   HOH C2106     -18.675  89.451  68.933  1.00 54.91           O  
-HETATM 7100  O   HOH C2107      -7.169  94.010  68.731  1.00 42.09           O  
-HETATM 7101  O   HOH C2108      20.654  80.120  66.325  1.00 47.97           O  
-HETATM 7102  O   HOH C2109      22.791  76.058  64.515  1.00 44.88           O  
-HETATM 7103  O   HOH C2110      30.526  45.394  46.597  1.00 39.43           O  
-HETATM 7104  O   HOH C2111      18.950  71.691  66.920  1.00 47.97           O  
-HETATM 7105  O   HOH C2112      12.433  65.103  63.673  1.00 42.76           O  
-HETATM 7106  O   HOH C2113      14.054  61.987  61.013  1.00 42.30           O  
-HETATM 7107  O   HOH C2114      13.210  68.405  57.426  1.00 27.83           O  
-HETATM 7108  O   HOH C2115      11.192  61.661  59.339  1.00 31.80           O  
-HETATM 7109  O   HOH C2116       8.912  63.630  56.943  1.00 29.59           O  
-HETATM 7110  O   HOH C2117       3.966  68.631  53.305  1.00 30.38           O  
-HETATM 7111  O   HOH C2118       8.133  68.526  58.037  1.00 29.98           O  
-HETATM 7112  O   HOH C2119       7.280  61.246  51.004  1.00 24.58           O  
-HETATM 7113  O   HOH C2120       4.484  60.399  48.068  1.00 23.05           O  
-HETATM 7114  O   HOH C2121      -1.805  63.300  48.852  1.00 28.54           O  
-HETATM 7115  O   HOH C2122       1.650  62.910  50.272  1.00 23.68           O  
-HETATM 7116  O   HOH C2123      -6.149  65.316  34.194  1.00 46.74           O  
-HETATM 7117  O   HOH C2124      15.703  51.269  63.814  1.00 38.72           O  
-HETATM 7118  O   HOH C2125     -12.534  71.965  32.273  1.00 55.96           O  
-HETATM 7119  O   HOH C2126      -8.128  69.664  40.773  1.00 52.97           O  
-HETATM 7120  O   HOH C2127      -6.341  61.683  37.523  1.00 34.72           O  
-HETATM 7121  O   HOH C2128     -17.859  64.542  44.987  1.00 46.21           O  
-HETATM 7122  O   HOH C2129     -16.022  68.773  39.572  1.00 56.80           O  
-HETATM 7123  O   HOH C2130     -13.924  67.660  41.479  1.00 35.77           O  
-HETATM 7124  O   HOH C2131      -5.226  68.036  41.495  1.00 41.55           O  
-HETATM 7125  O   HOH C2132      -4.574  70.481  39.660  1.00 40.39           O  
-HETATM 7126  O   HOH C2133      -0.501  69.308  45.982  1.00 29.02           O  
-HETATM 7127  O   HOH C2134      -1.338  67.580  39.576  1.00 40.79           O  
-HETATM 7128  O   HOH C2135      -3.888  74.004  41.101  1.00 40.59           O  
-HETATM 7129  O   HOH C2136      -0.447  68.273  53.090  1.00 52.77           O  
-HETATM 7130  O   HOH C2137      -0.594  67.721  50.599  1.00 34.56           O  
-HETATM 7131  O   HOH C2138      -3.984  69.674  60.798  1.00 40.94           O  
-HETATM 7132  O   HOH C2139      -8.902  73.847  58.158  1.00 38.41           O  
-HETATM 7133  O   HOH C2140       1.054  61.060  57.139  1.00 45.29           O  
-HETATM 7134  O   HOH C2141      -0.643  63.894  51.274  1.00 30.52           O  
-HETATM 7135  O   HOH C2142      -3.586  64.919  64.850  1.00 26.32           O  
-HETATM 7136  O   HOH C2143      -3.647  59.244  69.357  1.00 40.84           O  
-HETATM 7137  O   HOH C2144      -5.916  56.617  67.978  1.00 25.46           O  
-HETATM 7138  O   HOH C2145     -10.024  57.978  68.712  1.00 37.60           O  
-HETATM 7139  O   HOH C2146      -9.851  64.701  66.381  1.00 33.04           O  
-HETATM 7140  O   HOH C2147      -8.152  53.448  61.941  1.00 21.66           O  
-HETATM 7141  O   HOH C2148      -9.362  49.798  65.369  1.00 25.26           O  
-HETATM 7142  O   HOH C2149      -1.372  56.085  70.608  1.00 45.53           O  
-HETATM 7143  O   HOH C2150     -17.735  54.560  61.506  1.00 28.18           O  
-HETATM 7144  O   HOH C2151     -13.759  52.922  66.801  1.00 28.49           O  
-HETATM 7145  O   HOH C2152     -19.386  60.694  60.533  1.00 39.11           O  
-HETATM 7146  O   HOH C2153     -13.932  65.831  61.331  1.00 36.68           O  
-HETATM 7147  O   HOH C2154     -16.989  60.008  65.879  1.00 52.65           O  
-HETATM 7148  O   HOH C2155     -18.000  66.243  56.073  1.00 32.15           O  
-HETATM 7149  O   HOH C2156     -16.142  69.432  53.956  1.00 49.49           O  
-HETATM 7150  O   HOH C2157     -11.983  71.923  59.025  1.00 40.96           O  
-HETATM 7151  O   HOH C2158     -13.957  74.117  51.514  1.00 37.42           O  
-HETATM 7152  O   HOH C2159     -14.178  73.197  46.552  1.00 50.93           O  
-HETATM 7153  O   HOH C2160     -17.927  69.258  51.520  1.00 36.96           O  
-HETATM 7154  O   HOH C2161     -19.095  65.985  49.499  1.00 65.30           O  
-HETATM 7155  O   HOH C2162     -16.999  63.071  47.034  1.00 49.38           O  
-HETATM 7156  O   HOH C2163     -18.354  60.486  46.232  1.00 37.89           O  
-HETATM 7157  O   HOH C2164     -18.259  63.482  49.188  1.00 35.56           O  
-HETATM 7158  O   HOH C2165      -6.928  65.033  48.274  1.00 30.33           O  
-HETATM 7159  O   HOH C2166       2.693  59.667  50.410  1.00 41.41           O  
-HETATM 7160  O   HOH C2167      -2.094  59.896  59.929  1.00 30.92           O  
-HETATM 7161  O   HOH C2168       4.738  61.744  52.029  1.00 33.32           O  
-HETATM 7162  O   HOH C2169       8.963  60.905  53.226  1.00 25.42           O  
-HETATM 7163  O   HOH C2170       9.774  50.754  53.784  1.00 41.40           O  
-HETATM 7164  O   HOH C2171       8.625  57.093  57.146  1.00 35.15           O  
-HETATM 7165  O   HOH C2172       4.378  52.364  59.573  1.00 44.80           O  
-HETATM 7166  O   HOH C2173       6.874  56.368  59.041  1.00 42.28           O  
-HETATM 7167  O   HOH C2174       0.784  54.190  64.359  1.00 38.28           O  
-HETATM 7168  O   HOH C2175       0.666  51.702  63.634  1.00 37.94           O  
-HETATM 7169  O   HOH C2176       2.765  46.155  58.060  1.00 44.34           O  
-HETATM 7170  O   HOH C2177       3.732  50.464  58.066  1.00 45.08           O  
-HETATM 7171  O   HOH C2178      -3.310  48.177  53.621  1.00 30.24           O  
-HETATM 7172  O   HOH C2179       4.961  48.176  54.453  1.00 45.65           O  
-HETATM 7173  O   HOH C2180       1.336  45.982  53.003  1.00 35.83           O  
-HETATM 7174  O   HOH C2181      -4.214  44.615  54.763  1.00 31.65           O  
-HETATM 7175  O   HOH C2182     -17.875  52.375  59.825  1.00 24.81           O  
-HETATM 7176  O   HOH C2183     -18.628  43.997  58.516  1.00 40.37           O  
-HETATM 7177  O   HOH C2184     -23.736  56.929  51.192  1.00 46.94           O  
-HETATM 7178  O   HOH C2185     -19.512  58.389  44.313  1.00 55.53           O  
-HETATM 7179  O   HOH C2186     -15.194  48.779  46.113  1.00 46.37           O  
-HETATM 7180  O   HOH C2187     -13.158  50.304  38.583  1.00 44.27           O  
-HETATM 7181  O   HOH C2188      -0.022  52.489  40.330  1.00 25.74           O  
-HETATM 7182  O   HOH C2189       0.889  52.285  33.804  1.00 32.87           O  
-HETATM 7183  O   HOH C2190      -1.062  59.245  39.854  1.00 26.94           O  
-HETATM 7184  O   HOH C2191      -4.115  56.960  34.136  1.00 39.39           O  
-HETATM 7185  O   HOH C2192       2.665  55.210  35.648  1.00 36.42           O  
-HETATM 7186  O   HOH C2193       5.712  48.860  38.632  1.00 31.13           O  
-HETATM 7187  O   HOH C2194       0.643  49.293  30.291  1.00 42.30           O  
-HETATM 7188  O   HOH C2195      10.746  55.815  44.450  1.00 33.14           O  
-HETATM 7189  O   HOH C2196       8.996  45.578  39.663  1.00 53.15           O  
-HETATM 7190  O   HOH C2197      11.610  50.320  46.582  1.00 28.84           O  
-HETATM 7191  O   HOH C2198       6.356  47.262  50.727  1.00 42.18           O  
-HETATM 7192  O   HOH C2199       7.193  41.313  48.791  1.00 42.30           O  
-HETATM 7193  O   HOH C2200       7.453  44.334  50.266  1.00 39.63           O  
-HETATM 7194  O   HOH C2201       5.896  44.155  43.622  1.00 32.52           O  
-HETATM 7195  O   HOH C2202      -1.149  46.785  52.052  1.00 21.69           O  
-HETATM 7196  O   HOH C2203       0.313  40.494  53.351  1.00 49.73           O  
-HETATM 7197  O   HOH C2204      -3.520  39.720  51.346  1.00 34.33           O  
-HETATM 7198  O   HOH C2205     -14.801  46.037  46.215  1.00 55.74           O  
-HETATM 7199  O   HOH C2206      -9.953  47.758  52.148  1.00 26.72           O  
-HETATM 7200  O   HOH C2207     -12.757  35.528  52.700  1.00 41.64           O  
-HETATM 7201  O   HOH C2208     -15.112  43.038  56.412  1.00 33.64           O  
-HETATM 7202  O   HOH C2209     -16.987  42.528  54.605  1.00 51.32           O  
-HETATM 7203  O   HOH C2210     -15.744  37.952  51.633  1.00 37.17           O  
-HETATM 7204  O   HOH C2211     -17.891  35.512  44.754  1.00 47.35           O  
-HETATM 7205  O   HOH C2212     -21.162  38.480  46.536  1.00 51.02           O  
-HETATM 7206  O   HOH C2213     -20.770  45.351  48.267  1.00 41.62           O  
-HETATM 7207  O   HOH C2214       9.104  37.673  29.511  1.00 70.43           O  
-HETATM 7208  O   HOH C2215      11.832  39.517  34.941  1.00 45.74           O  
-HETATM 7209  O   HOH C2216       4.027  44.804  39.405  1.00 32.70           O  
-HETATM 7210  O   HOH C2217       3.030  33.917  39.387  1.00 64.62           O  
-HETATM 7211  O   HOH C2218       2.096  37.485  45.978  1.00 42.76           O  
-HETATM 7212  O   HOH C2219       4.426  35.465  41.989  1.00 53.89           O  
-HETATM 7213  O   HOH C2220       5.128  35.830  45.298  1.00 33.94           O  
-HETATM 7214  O   HOH C2221      -2.870  37.243  51.312  1.00 30.51           O  
-HETATM 7215  O   HOH C2222      -3.033  29.741  53.115  1.00 48.73           O  
-HETATM 7216  O   HOH C2223      -4.709  27.976  51.659  1.00 49.24           O  
-HETATM 7217  O   HOH C2224      -3.285  26.548  38.057  1.00 55.97           O  
-HETATM 7218  O   HOH C2225      19.117  17.853  43.854  1.00 54.62           O  
-HETATM 7219  O   HOH C2226      11.851   4.633  42.552  1.00 53.01           O  
-HETATM 7220  O   HOH C2227      19.134   1.051  52.023  1.00 59.33           O  
-HETATM 7221  O   HOH C2228      24.180   4.787  50.274  1.00 61.61           O  
-HETATM 7222  O   HOH C2229       1.176  18.740  50.335  1.00 50.94           O  
-HETATM 7223  O   HOH C2230       6.724  19.831  55.430  1.00 63.80           O  
-HETATM 7224  O   HOH C2231      10.132  24.107  64.958  1.00 45.90           O  
-HETATM 7225  O   HOH C2232      13.010  23.186  66.331  1.00 51.86           O  
-HETATM 7226  O   HOH C2233      16.968  24.610  45.520  1.00 55.48           O  
-HETATM 7227  O   HOH C2234      11.952  20.849  43.042  1.00 57.91           O  
-HETATM 7228  O   HOH C2235       9.492  27.484  39.865  1.00 68.18           O  
-HETATM 7229  O   HOH C2236       6.537  22.229  45.661  1.00 59.28           O  
-HETATM 7230  O   HOH C2237       2.021  29.129  49.073  1.00 42.61           O  
-HETATM 7231  O   HOH C2238      -0.487  29.250  50.443  1.00 48.06           O  
-HETATM 7232  O   HOH C2239      10.418  33.844  56.095  1.00 33.41           O  
-HETATM 7233  O   HOH C2240      20.536  34.318  62.874  1.00 39.43           O  
-HETATM 7234  O   HOH C2241      23.551  35.735  60.219  1.00 56.42           O  
-HETATM 7235  O   HOH C2242      17.636  26.703  46.961  1.00 52.36           O  
-HETATM 7236  O   HOH C2243      18.508  34.387  43.653  1.00 41.98           O  
-HETATM 7237  O   HOH C2244      21.440  35.117  40.965  1.00 50.85           O  
-HETATM 7238  O   HOH C2245       5.989  35.234  52.113  1.00 50.58           O  
-HETATM 7239  O   HOH C2246       8.258  40.141  55.513  1.00 40.28           O  
-HETATM 7240  O   HOH C2247      13.854  44.388  49.335  1.00 25.67           O  
-HETATM 7241  O   HOH C2248      14.522  37.544  66.172  1.00 48.58           O  
-HETATM 7242  O   HOH C2249      12.524  34.558  57.933  1.00 29.02           O  
-HETATM 7243  O   HOH C2250      13.090  45.948  62.009  1.00 37.74           O  
-HETATM 7244  O   HOH C2251      15.628  34.680  65.807  1.00 44.76           O  
-HETATM 7245  O   HOH C2252      24.587  46.792  64.016  1.00 28.71           O  
-HETATM 7246  O   HOH C2253      25.058  37.998  59.755  1.00 43.69           O  
-HETATM 7247  O   HOH C2254      18.101  46.833  65.531  1.00 44.72           O  
-HETATM 7248  O   HOH C2255      21.673  48.427  65.488  1.00 42.63           O  
-HETATM 7249  O   HOH C2256      29.156  50.913  62.440  1.00 51.18           O  
-HETATM 7250  O   HOH C2257      33.147  47.893  62.123  1.00 52.24           O  
-HETATM 7251  O   HOH C2258      29.973  43.342  45.372  1.00 40.81           O  
-HETATM 7252  O   HOH C2259      29.267  49.045  39.465  1.00 33.99           O  
-HETATM 7253  O   HOH C2260      22.962  40.095  36.985  1.00 42.18           O  
-HETATM 7254  O   HOH C2261      20.092  40.461  34.078  1.00 50.70           O  
-HETATM 7255  O   HOH C2262      31.022  51.467  26.018  1.00 55.21           O  
-HETATM 7256  O   HOH C2263      18.885  43.387  28.787  1.00 50.98           O  
-HETATM 7257  O   HOH C2264      15.479  41.711  39.729  1.00 56.60           O  
-HETATM 7258  O   HOH C2265      18.349  53.127  37.932  1.00 37.29           O  
-HETATM 7259  O   HOH C2266       6.031  46.313  38.773  1.00 36.85           O  
-HETATM 7260  O   HOH C2267       8.819  42.467  42.450  1.00 47.63           O  
-HETATM 7261  O   HOH C2268       9.089  52.236  39.226  1.00 41.14           O  
-HETATM 7262  O   HOH C2269      15.547  53.226  42.056  1.00 48.39           O  
-HETATM 7263  O   HOH C2270      11.171  52.624  57.499  1.00 44.13           O  
-HETATM 7264  O   HOH C2271       8.753  48.324  52.694  1.00 34.58           O  
-HETATM 7265  O   HOH C2272      14.520  48.398  60.460  1.00 50.42           O  
-HETATM 7266  O   HOH C2273      18.383  57.779  57.632  1.00 54.06           O  
-HETATM 7267  O   HOH C2274      10.699  55.190  58.255  1.00 36.77           O  
-HETATM 7268  O   HOH C2275      14.291  53.043  59.811  1.00 36.55           O  
-HETATM 7269  O   HOH C2276      15.812  50.767  60.930  1.00 33.09           O  
-HETATM 7270  O   HOH C2277      26.960  57.384  60.690  1.00 44.37           O  
-HETATM 7271  O   HOH C2278      22.041  62.114  60.243  1.00 62.22           O  
-HETATM 7272  O   HOH C2279      27.625  54.567  63.710  1.00 47.06           O  
-HETATM 7273  O   HOH C2280      29.264  55.575  59.981  1.00 34.66           O  
-HETATM 7274  O   HOH C2281      30.306  53.010  59.800  1.00 31.09           O  
-HETATM 7275  O   HOH C2282      35.106  50.156  58.069  1.00 51.95           O  
-HETATM 7276  O   HOH C2283      28.368  59.606  49.884  1.00 57.29           O  
-HETATM 7277  O   HOH C2284      26.312  60.587  50.785  1.00 63.08           O  
-HETATM 7278  O   HOH C2285      37.154  54.267  49.514  1.00 41.85           O  
-HETATM 7279  O   HOH C2286      33.921  48.194  46.759  1.00 34.03           O  
-HETATM 7280  O   HOH C2287      31.353  48.052  46.041  1.00 36.47           O  
-HETATM 7281  O   HOH C2288      40.173  51.210  44.227  1.00 51.33           O  
-HETATM 7282  O   HOH C2289      31.681  51.696  37.152  1.00 38.98           O  
-HETATM 7283  O   HOH C2290      38.842  54.436  43.268  1.00 35.94           O  
-HETATM 7284  O   HOH C2291      25.434  52.475  33.045  1.00 52.45           O  
-HETATM 7285  O   HOH C2292      24.438  58.942  40.056  1.00 59.52           O  
-HETATM 7286  O   HOH C2293      19.367  54.868  39.930  1.00 45.61           O  
-HETATM 7287  O   HOH C2294      23.720  62.334  49.173  1.00 44.51           O  
-HETATM 7288  O   HOH C2295      17.115  55.050  42.032  1.00 50.77           O  
-HETATM 7289  O   HOH C2296      17.476  57.163  40.207  1.00 55.89           O  
-HETATM 7290  O   HOH C2297      15.566  54.980  44.095  1.00 29.66           O  
-HETATM 7291  O   HOH C2298      19.784  59.309  55.508  1.00 36.39           O  
-HETATM 7292  O   HOH C2299      22.429  60.904  56.037  1.00 48.37           O  
-HETATM 7293  O   HOH C2300      18.536  66.469  52.604  1.00 39.55           O  
-HETATM 7294  O   HOH C2301      18.312  64.615  61.111  1.00 28.28           O  
-HETATM 7295  O   HOH C2302      20.383  65.172  59.987  1.00 39.48           O  
-HETATM 7296  O   HOH Z2001      -9.382  56.576  76.622  1.00 40.42           O  
-HETATM 7297  O   HOH Z2002      -9.602  63.831  76.251  1.00 44.08           O  
-HETATM 7298  O   HOH Z2003     -11.694  58.961  70.698  1.00 58.50           O  
-HETATM 7299  O   HOH Z2004      -7.819  56.660  69.978  1.00 34.21           O  
-HETATM 7300  O   HOH Z2005      -8.737  50.464  69.777  1.00 30.36           O  
-HETATM 7301  O   HOH Z2006     -14.764  48.489  69.878  1.00 38.01           O  
-HETATM 7302  O   HOH Z2007     -15.930  49.868  67.770  1.00 46.40           O  
-HETATM 7303  O   HOH Z2008      -6.545  45.447  77.844  1.00 55.27           O  
-HETATM 7304  O   HOH Z2009     -10.052  46.195  79.389  1.00 41.26           O  
-HETATM 7305  O   HOH Z2010     -14.136  42.473  81.267  1.00 59.26           O  
-HETATM 7306  O   HOH Z2011     -10.506  39.580  77.203  1.00 33.86           O  
-HETATM 7307  O   HOH Z2012     -11.442  36.842  77.997  1.00 41.25           O  
-HETATM 7308  O   HOH Z2013      -8.118  30.417  80.208  1.00 44.56           O  
-HETATM 7309  O   HOH Z2014     -11.653  31.531  86.205  1.00 50.11           O  
-HETATM 7310  O   HOH Z2015      -9.822  22.953  82.450  1.00 58.88           O  
-HETATM 7311  O   HOH Z2016     -13.380  61.311  69.643  1.00 47.76           O  
-HETATM 7312  O   HOH Z2017      -1.041  32.300  86.713  1.00 65.88           O  
-HETATM 7313  O   HOH Z2018      -0.451  36.400  79.723  1.00 38.85           O  
-HETATM 7314  O   HOH Z2019      -0.746  30.639  74.292  1.00 37.31           O  
-HETATM 7315  O   HOH Z2020       0.199  34.713  75.646  1.00 41.27           O  
-HETATM 7316  O   HOH Z2021       1.507  30.717  76.596  1.00 67.97           O  
-HETATM 7317  O   HOH Z2022     -12.138  25.405  62.247  1.00 55.19           O  
-HETATM 7318  O   HOH Z2023     -15.204  29.107  54.805  1.00 58.73           O  
-HETATM 7319  O   HOH Z2024       0.082  43.905  55.326  1.00 36.88           O  
-HETATM 7320  O   HOH Z2025     -13.163  31.246  58.891  1.00 43.94           O  
-HETATM 7321  O   HOH Z2026       5.756  33.072  60.483  1.00 49.88           O  
-HETATM 7322  O   HOH Z2027      -5.156  23.249  59.598  1.00 43.36           O  
-HETATM 7323  O   HOH Z2028       1.667  27.005  64.424  1.00 43.30           O  
-HETATM 7324  O   HOH Z2029       5.272  30.047  63.221  1.00 39.92           O  
-HETATM 7325  O   HOH Z2030       1.902  33.465  56.055  1.00 42.42           O  
-HETATM 7326  O   HOH Z2031       0.779  37.564  56.115  1.00 40.16           O  
-HETATM 7327  O   HOH Z2032      -2.169  43.901  53.936  1.00 40.11           O  
-HETATM 7328  O   HOH Z2033       0.213  45.194  58.090  1.00 30.37           O  
-HETATM 7329  O   HOH Z2034       2.019  45.146  65.015  1.00 26.46           O  
-HETATM 7330  O   HOH Z2035       1.900  50.185  68.068  1.00 43.25           O  
-HETATM 7331  O   HOH Z2036       3.990  35.291  61.463  1.00 38.49           O  
-HETATM 7332  O   HOH Z2037      -1.372  28.875  70.044  1.00 49.60           O  
-HETATM 7333  O   HOH Z2038      -2.961  22.962  65.960  1.00 53.02           O  
-HETATM 7334  O   HOH Z2039      -4.858  21.396  67.241  1.00 48.13           O  
-HETATM 7335  O   HOH Z2040       4.063  28.263  72.627  1.00 43.19           O  
-HETATM 7336  O   HOH Z2041       4.275  34.459  73.455  1.00 49.91           O  
-HETATM 7337  O   HOH Z2042       0.315  29.097  72.285  1.00 50.72           O  
-HETATM 7338  O   HOH Z2043       5.598  36.566  74.014  1.00 48.34           O  
-HETATM 7339  O   HOH Z2044       5.192  44.466  72.245  1.00 56.31           O  
-HETATM 7340  O   HOH Z2045       4.857  39.062  67.360  1.00 28.58           O  
-HETATM 7341  O   HOH Z2046       1.294  50.062  65.537  1.00 30.30           O  
-HETATM 7342  O   HOH Z2047       0.082  47.929  69.131  1.00 35.19           O  
-HETATM 7343  O   HOH Z2048     -15.788  40.793  66.417  1.00 41.21           O  
-HETATM 7344  O   HOH Z2049     -15.633  44.248  58.934  1.00 29.70           O  
-HETATM 7345  O   HOH Z2050     -21.614  41.221  57.723  1.00 54.77           O  
-HETATM 7346  O   HOH Z2051      -9.376  36.943  54.578  1.00 32.17           O  
-HETATM 7347  O   HOH Z2052      -9.918  40.008  56.928  1.00 26.08           O  
-HETATM 7348  O   HOH Z2053     -14.734  33.928  50.726  1.00 49.87           O  
-HETATM 7349  O   HOH Z2054     -20.151  33.451  55.395  1.00 55.83           O  
-HETATM 7350  O   HOH Z2055     -20.180  35.839  58.952  1.00 38.29           O  
-HETATM 7351  O   HOH Z2056     -16.963  33.559  69.040  1.00 49.05           O  
-HETATM 7352  O   HOH Z2057      -8.439  32.672  78.380  1.00 45.94           O  
-HETATM 7353  O   HOH Z2058      -0.193  29.082  78.703  1.00 43.21           O  
-HETATM 7354  O   HOH Z2059     -11.722  22.878  75.503  1.00 39.46           O  
-HETATM 7355  O   HOH Z2060      -9.806  23.214  79.050  1.00 51.01           O  
-HETATM 7356  O   HOH Z2061     -20.880  21.031  69.119  1.00 55.75           O  
-HETATM 7357  O   HOH Z2062     -18.802  27.907  72.313  1.00 41.31           O  
-HETATM 7358  O   HOH Z2063     -17.521  30.983  79.336  1.00 42.98           O  
-CONECT 6942 6943 6944 6945 6946                                                 
-CONECT 6943 6942                                                                
-CONECT 6944 6942                                                                
-CONECT 6945 6942 6970                                                           
-CONECT 6946 6942 6947                                                           
-CONECT 6947 6946 6948 6949 6950                                                 
-CONECT 6948 6947                                                                
-CONECT 6949 6947                                                                
-CONECT 6950 6947 6951                                                           
-CONECT 6951 6950 6952                                                           
-CONECT 6952 6951 6953 6954                                                      
-CONECT 6953 6952 6958                                                           
-CONECT 6954 6952 6955 6956                                                      
-CONECT 6955 6954                                                                
-CONECT 6956 6954 6957 6958                                                      
-CONECT 6957 6956                                                                
-CONECT 6958 6953 6956 6959                                                      
-CONECT 6959 6958 6960 6969                                                      
-CONECT 6960 6959 6961                                                           
-CONECT 6961 6960 6962                                                           
-CONECT 6962 6961 6963 6969                                                      
-CONECT 6963 6962 6964 6965                                                      
-CONECT 6964 6963                                                                
-CONECT 6965 6963 6966                                                           
-CONECT 6966 6965 6967 6968                                                      
-CONECT 6967 6966                                                                
-CONECT 6968 6966 6969                                                           
-CONECT 6969 6959 6962 6968                                                      
-CONECT 6970 6945 6971 6972 6973                                                 
-CONECT 6971 6970                                                                
-CONECT 6972 6970                                                                
-CONECT 6973 6970 6974                                                           
-CONECT 6974 6973 6975                                                           
-CONECT 6975 6974 6976 6977                                                      
-CONECT 6976 6975 6981                                                           
-CONECT 6977 6975 6978 6979                                                      
-CONECT 6978 6977                                                                
-CONECT 6979 6977 6980 6981                                                      
-CONECT 6980 6979                                                                
-CONECT 6981 6976 6979 6982                                                      
-CONECT 6982 6981 6983 6992                                                      
-CONECT 6983 6982 6984                                                           
-CONECT 6984 6983 6985 6993                                                      
-CONECT 6985 6984 6986 6992                                                      
-CONECT 6986 6985 6987 6988                                                      
-CONECT 6987 6986                                                                
-CONECT 6988 6986 6989                                                           
-CONECT 6989 6988 6990 6991                                                      
-CONECT 6990 6989                                                                
-CONECT 6991 6989 6992                                                           
-CONECT 6992 6982 6985 6991                                                      
-CONECT 6993 6984                                                                
-MASTER      364    0    2   50    6    0    6    6 7356    2   52   68          
-END                                                                             
diff --git a/plip/test/pdb/1hii.pdb b/plip/test/pdb/1hii.pdb
deleted file mode 100644
index 72c207c..0000000
--- a/plip/test/pdb/1hii.pdb
+++ /dev/null
@@ -1,2163 +0,0 @@
-HEADER    HYDROLASE (ASPARTIC PROTEINASE)         31-MAR-95   1HII              
-TITLE     COMPARATIVE ANALYSIS OF THE X-RAY STRUCTURES OF HIV-1 AND             
-TITLE    2 HIV-2 PROTEASES IN COMPLEX WITH CGP 53820, A NOVEL                   
-TITLE    3 PSEUDOSYMMETRIC INHIBITOR                                            
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: HIV-2 PROTEASE;                                            
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 EC: 3.4.23.-;                                                        
-COMPND   5 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 2;                 
-SOURCE   3 ORGANISM_TAXID: 11709;                                               
-SOURCE   4 CELL_LINE: S2;                                                       
-SOURCE   5 GENE: POL;                                                           
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PT7Q10H;                                  
-SOURCE   9 EXPRESSION_SYSTEM_GENE: POL                                          
-KEYWDS    ASPARTATE PROTEASE, INHIBITED, HIV, HYDROLASE (ASPARTIC               
-KEYWDS   2 PROTEINASE)                                                          
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    J.P.PRIESTLE,M.G.GRUETTER                                             
-REVDAT   3   24-FEB-09 1HII    1       VERSN                                    
-REVDAT   2   01-APR-03 1HII    1       JRNL                                     
-REVDAT   1   10-JUL-95 1HII    0                                                
-JRNL        AUTH   J.P.PRIESTLE,A.FASSLER,J.ROSEL,M.TINTELNOT-BLOMLEY,          
-JRNL        AUTH 2 P.STROP,M.G.GRUTTER                                          
-JRNL        TITL   COMPARATIVE ANALYSIS OF THE X-RAY STRUCTURES OF              
-JRNL        TITL 2 HIV-1 AND HIV-2 PROTEASES IN COMPLEX WITH CGP                
-JRNL        TITL 3 53820, A NOVEL PSEUDOSYMMETRIC INHIBITOR.                    
-JRNL        REF    STRUCTURE                     V.   3   381 1995              
-JRNL        REFN                   ISSN 0969-2126                               
-JRNL        PMID   7613867                                                      
-JRNL        DOI    10.1016/S0969-2126(01)00169-1                                
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   A.FASSLER,J.ROSEL,M.TINTELNOT-BLOMLEY,E.ALTERI,              
-REMARK   1  AUTH 2 G.BOLD,M.LANG                                                
-REMARK   1  TITL   NOVEL PSEUDOSYMMETRIC INHIBITORS OF HIV-1 PROTEASE           
-REMARK   1  REF    BIOORG.MED.CHEM.LETT.         V.   3  2837 1993              
-REMARK   1  REFN                   ISSN 0960-894X                               
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : TNT, X-PLOR                                          
-REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
-REMARK   3   NUMBER OF REFLECTIONS             : 8879                           
-REMARK   3                                                                      
-REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
-REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
-REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.138                           
-REMARK   3   R VALUE            (WORKING SET) : NULL                            
-REMARK   3   FREE R VALUE                     : NULL                            
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
-REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
-REMARK   3                                                                      
-REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
-REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
-REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
-REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
-REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
-REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
-REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 1510                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 51                                      
-REMARK   3   SOLVENT ATOMS            : 194                                     
-REMARK   3                                                                      
-REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
-REMARK   3   BOND LENGTHS                 (A) : 0.012 ; NULL  ; NULL            
-REMARK   3   BOND ANGLES            (DEGREES) : 2.000 ; NULL  ; NULL            
-REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
-REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
-REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
-REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
-REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
-REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
-REMARK   3                                                                      
-REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : NULL                                                 
-REMARK   3   KSOL        : NULL                                                 
-REMARK   3   BSOL        : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  RESTRAINT LIBRARIES.                                                
-REMARK   3   STEREOCHEMISTRY : NULL                                             
-REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1HII COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : FEB-93                             
-REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
-REMARK 200  PH                             : NULL                               
-REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : N                                  
-REMARK 200  RADIATION SOURCE               : NULL                               
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
-REMARK 200  DETECTOR MANUFACTURER          : ENRAF-NONIUS FAST                  
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES                             
-REMARK 200  DATA SCALING SOFTWARE          : NULL                               
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9517                               
-REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
-REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
-REMARK 200  DATA REDUNDANCY                : 4.130                              
-REMARK 200  R MERGE                    (I) : 0.05100                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
-REMARK 200 SOFTWARE USED: X-PLOR                                                
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 50.50                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       16.70000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.75000            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.10000            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.75000            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.70000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.10000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 300 REMARK: MTRIX                                                        
-REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW                
-REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE               
-REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE            
-REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL              
-REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED               
-REMARK 300  SECOND.                                                             
-REMARK 300                                                                      
-REMARK 300            APPLIED TO           TRANSFORMED TO                       
-REMARK 300  MTRIX      RESIDUES               RESIDUES         RMSD             
-REMARK 300    M1   A    1  ..  A   99     B    1  ..  B   99   0.479            
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 5090 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 9470 ANGSTROM**2                        
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 400                                                                      
-REMARK 400 COMPOUND                                                             
-REMARK 400 COMPND                                                               
-REMARK 400   MOLECULE: HIV-2 PROTEASE. ROD ISOLATE.                             
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH B 174        DISTANCE =  6.50 ANGSTROMS                       
-REMARK 600                                                                      
-REMARK 600 HETEROGEN                                                            
-REMARK 600 SOURCE 1                                                             
-REMARK 600   MOLECULE_NAME: CGP 53820. PSEUDOSYMMETRIC                          
-REMARK 600   TRANSITION-STATE ANALOG.                                           
-REMARK 600 SOURCE 2                                                             
-REMARK 600   MOLECULE_NAME: SULFATE ION (SO4). PSEUDOSYMMETRIC                  
-REMARK 600   TRANSITION-STATE ANALOG.                                           
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: CAT                                                 
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: NULL                                               
-REMARK 800 SITE_IDENTIFIER: S2                                                  
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: NULL                                               
-REMARK 800 SITE_IDENTIFIER: S1                                                  
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: NULL                                               
-REMARK 800 SITE_IDENTIFIER: S1P                                                 
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: NULL                                               
-REMARK 800 SITE_IDENTIFIER: S2P                                                 
-REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
-REMARK 800 SITE_DESCRIPTION: NULL                                               
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 100                 
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 100                 
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C20 B 101                 
-DBREF  1HII A    1    99  UNP    P04584   POL_HV2RO       86    184             
-DBREF  1HII B    1    99  UNP    P04584   POL_HV2RO       86    184             
-SEQRES   1 A   99  PRO GLN PHE SER LEU TRP LYS ARG PRO VAL VAL THR ALA          
-SEQRES   2 A   99  TYR ILE GLU GLY GLN PRO VAL GLU VAL LEU LEU ASP THR          
-SEQRES   3 A   99  GLY ALA ASP ASP SER ILE VAL ALA GLY ILE GLU LEU GLY          
-SEQRES   4 A   99  ASN ASN TYR SER PRO LYS ILE VAL GLY GLY ILE GLY GLY          
-SEQRES   5 A   99  PHE ILE ASN THR LYS GLU TYR LYS ASN VAL GLU ILE GLU          
-SEQRES   6 A   99  VAL LEU ASN LYS LYS VAL ARG ALA THR ILE MET THR GLY          
-SEQRES   7 A   99  ASP THR PRO ILE ASN ILE PHE GLY ARG ASN ILE LEU THR          
-SEQRES   8 A   99  ALA LEU GLY MET SER LEU ASN LEU                              
-SEQRES   1 B   99  PRO GLN PHE SER LEU TRP LYS ARG PRO VAL VAL THR ALA          
-SEQRES   2 B   99  TYR ILE GLU GLY GLN PRO VAL GLU VAL LEU LEU ASP THR          
-SEQRES   3 B   99  GLY ALA ASP ASP SER ILE VAL ALA GLY ILE GLU LEU GLY          
-SEQRES   4 B   99  ASN ASN TYR SER PRO LYS ILE VAL GLY GLY ILE GLY GLY          
-SEQRES   5 B   99  PHE ILE ASN THR LYS GLU TYR LYS ASN VAL GLU ILE GLU          
-SEQRES   6 B   99  VAL LEU ASN LYS LYS VAL ARG ALA THR ILE MET THR GLY          
-SEQRES   7 B   99  ASP THR PRO ILE ASN ILE PHE GLY ARG ASN ILE LEU THR          
-SEQRES   8 B   99  ALA LEU GLY MET SER LEU ASN LEU                              
-HET    SO4  A 100       5                                                       
-HET    SO4  B 100       5                                                       
-HET    C20  B 101      41                                                       
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM     C20 ACETYL-NH-VAL-CYCLOHEXYL-CH2[NCH2CHOH]CH2-BENZYL-VAL-            
-HETNAM   2 C20  NH-ACETYL                                                       
-HETSYN     C20 CGP 53820                                                        
-FORMUL   3  SO4    2(O4 S 2-)                                                   
-FORMUL   5  C20    C31 H51 N5 O5                                                
-FORMUL   6  HOH   *194(H2 O)                                                    
-HELIX    1   1 ARG A   87  LEU A   93  1                                   7    
-HELIX    2   2 ARG B   87  LEU B   93  1                                   7    
-SHEET    1   A 4 GLN A  18  LEU A  23  0                                        
-SHEET    2   A 4 VAL A  10  ILE A  15 -1  N  ILE A  15   O  GLN A  18           
-SHEET    3   A 4 VAL A  62  VAL A  66 -1  N  GLU A  65   O  TYR A  14           
-SHEET    4   A 4 LYS A  69  ALA A  73 -1  N  ALA A  73   O  VAL A  62           
-SHEET    1   B 3 TYR A  42  GLY A  48  0                                        
-SHEET    2   B 3 PHE A  53  TYR A  59 -1  N  GLU A  58   O  SER A  43           
-SHEET    3   B 3 ILE A  75  THR A  77 -1  N  THR A  77   O  LYS A  57           
-SHEET    1   C 2 SER A  96  ASN A  98  0                                        
-SHEET    2   C 2 SER B  96  ASN B  98 -1  N  ASN B  98   O  SER A  96           
-SHEET    1   D 4 GLN B  18  LEU B  23  0                                        
-SHEET    2   D 4 VAL B  10  ILE B  15 -1  N  ILE B  15   O  GLN B  18           
-SHEET    3   D 4 VAL B  62  VAL B  66 -1  N  GLU B  65   O  TYR B  14           
-SHEET    4   D 4 LYS B  69  ALA B  73 -1  N  ALA B  73   O  VAL B  62           
-SHEET    1   E 3 SER B  43  GLY B  49  0                                        
-SHEET    2   E 3 GLY B  52  TYR B  59 -1  N  GLU B  58   O  SER B  43           
-SHEET    3   E 3 ILE B  75  THR B  77 -1  N  THR B  77   O  LYS B  57           
-SITE     1 CAT  2 ASP A  25  ASP B  25                                          
-SITE     1  S2  6 ILE A  50  ALA B  28  ASP B  30  ILE B  32                    
-SITE     2  S2  6 VAL B  47  ILE B  84                                          
-SITE     1  S1  9 ARG A   8  LEU A  23  THR A  80  PRO A  81                    
-SITE     2  S1  9 ILE A  82  ILE A  84  GLY B  27  GLY B  49                    
-SITE     3  S1  9 ILE B  50                                                     
-SITE     1 S1P  9 GLY A  27  GLY A  49  ILE A  50  ARG B   8                    
-SITE     2 S1P  9 LEU B  23  THR B  80  PRO B  81  ILE B  82                    
-SITE     3 S1P  9 ILE B  84                                                     
-SITE     1 S2P  6 ALA A  28  ASP A  30  ILE A  32  VAL A  47                    
-SITE     2 S2P  6 ILE A  84  ILE B  50                                          
-SITE     1 AC1  6 LYS A  69  THR A  74  ASN A  88  HOH A 112                    
-SITE     2 AC1  6 HOH A 128  HOH A 174                                          
-SITE     1 AC2  4 PRO A   1  GLN A   2  ARG B   8  HOH B 171                    
-SITE     1 AC3 16 ASP A  25  GLY A  27  ALA A  28  ASP A  29                    
-SITE     2 AC3 16 GLY A  48  GLY A  49  ILE A  82  ASP B  25                    
-SITE     3 AC3 16 GLY B  27  ALA B  28  ASP B  29  VAL B  47                    
-SITE     4 AC3 16 GLY B  48  GLY B  49  ILE B  50  HOH B 102                    
-CRYST1   33.400   64.200   99.500  90.00  90.00  90.00 P 21 21 21    8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.029940  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.015576  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.010050        0.00000                         
-MTRIX1   1  0.263360 -0.907330  0.327720       35.48000    1                    
-MTRIX2   1 -0.908970 -0.347180 -0.230730       58.68000    1                    
-MTRIX3   1  0.323130 -0.237120 -0.916170       26.44000    1                    
-ATOM      1  N   PRO A   1      37.834  22.218  10.685  1.00 28.94           N  
-ATOM      2  CA  PRO A   1      37.587  23.580  11.228  1.00 28.74           C  
-ATOM      3  C   PRO A   1      36.599  23.522  12.381  1.00 27.84           C  
-ATOM      4  O   PRO A   1      35.642  22.760  12.351  1.00 28.42           O  
-ATOM      5  CB  PRO A   1      37.049  24.454  10.099  1.00 29.26           C  
-ATOM      6  CG  PRO A   1      37.781  23.933   8.944  1.00 31.88           C  
-ATOM      7  CD  PRO A   1      37.757  22.408   9.197  1.00 30.80           C  
-ATOM      8  N   GLN A   2      36.850  24.306  13.412  1.00 27.63           N  
-ATOM      9  CA  GLN A   2      35.963  24.318  14.551  1.00 28.09           C  
-ATOM     10  C   GLN A   2      35.411  25.722  14.720  1.00 24.98           C  
-ATOM     11  O   GLN A   2      36.139  26.676  14.546  1.00 26.73           O  
-ATOM     12  CB  GLN A   2      36.708  23.880  15.820  1.00 31.75           C  
-ATOM     13  CG  GLN A   2      35.797  23.882  17.058  1.00 48.39           C  
-ATOM     14  CD  GLN A   2      36.488  23.440  18.339  1.00 54.13           C  
-ATOM     15  OE1 GLN A   2      37.018  22.326  18.422  1.00 61.45           O  
-ATOM     16  NE2 GLN A   2      36.437  24.288  19.361  1.00 50.58           N  
-ATOM     17  N   PHE A   3      34.109  25.845  14.954  1.00 22.24           N  
-ATOM     18  CA  PHE A   3      33.508  27.150  15.181  1.00 19.57           C  
-ATOM     19  C   PHE A   3      33.099  27.139  16.638  1.00 17.63           C  
-ATOM     20  O   PHE A   3      32.297  26.295  17.043  1.00 15.47           O  
-ATOM     21  CB  PHE A   3      32.301  27.375  14.270  1.00 22.75           C  
-ATOM     22  CG  PHE A   3      32.659  27.462  12.815  1.00 17.04           C  
-ATOM     23  CD1 PHE A   3      32.887  26.309  12.069  1.00 21.23           C  
-ATOM     24  CD2 PHE A   3      32.816  28.689  12.202  1.00 19.01           C  
-ATOM     25  CE1 PHE A   3      33.266  26.381  10.731  1.00 21.03           C  
-ATOM     26  CE2 PHE A   3      33.192  28.770  10.864  1.00 19.22           C  
-ATOM     27  CZ  PHE A   3      33.421  27.619  10.129  1.00 19.97           C  
-ATOM     28  N   SER A   4      33.675  28.060  17.417  1.00 16.16           N  
-ATOM     29  CA  SER A   4      33.424  28.165  18.860  1.00 16.58           C  
-ATOM     30  C   SER A   4      32.064  28.750  19.247  1.00 14.73           C  
-ATOM     31  O   SER A   4      31.641  28.629  20.382  1.00 19.20           O  
-ATOM     32  CB  SER A   4      34.532  28.975  19.519  1.00 12.85           C  
-ATOM     33  OG  SER A   4      34.549  30.297  19.039  1.00 17.60           O  
-ATOM     34  N   LEU A   5      31.429  29.438  18.315  1.00 12.97           N  
-ATOM     35  CA  LEU A   5      30.114  30.030  18.483  1.00 11.18           C  
-ATOM     36  C   LEU A   5      30.076  31.305  19.270  1.00 14.26           C  
-ATOM     37  O   LEU A   5      28.996  31.803  19.539  1.00 16.29           O  
-ATOM     38  CB  LEU A   5      29.090  29.036  19.019  1.00  6.32           C  
-ATOM     39  CG  LEU A   5      28.956  27.737  18.208  1.00 14.03           C  
-ATOM     40  CD1 LEU A   5      28.065  26.749  18.960  1.00 11.98           C  
-ATOM     41  CD2 LEU A   5      28.430  27.998  16.785  1.00  8.28           C  
-ATOM     42  N   TRP A   6      31.237  31.850  19.641  1.00 15.29           N  
-ATOM     43  CA  TRP A   6      31.239  33.138  20.349  1.00 15.12           C  
-ATOM     44  C   TRP A   6      30.830  34.196  19.328  1.00 14.88           C  
-ATOM     45  O   TRP A   6      30.350  35.247  19.692  1.00 19.32           O  
-ATOM     46  CB  TRP A   6      32.599  33.479  20.978  1.00 14.98           C  
-ATOM     47  CG  TRP A   6      32.894  32.602  22.139  1.00 13.79           C  
-ATOM     48  CD1 TRP A   6      33.687  31.521  22.132  1.00 20.37           C  
-ATOM     49  CD2 TRP A   6      32.314  32.690  23.441  1.00 23.50           C  
-ATOM     50  NE1 TRP A   6      33.639  30.883  23.357  1.00 24.31           N  
-ATOM     51  CE2 TRP A   6      32.803  31.573  24.186  1.00 22.92           C  
-ATOM     52  CE3 TRP A   6      31.435  33.571  24.073  1.00 28.68           C  
-ATOM     53  CZ2 TRP A   6      32.440  31.333  25.513  1.00 18.70           C  
-ATOM     54  CZ3 TRP A   6      31.068  33.336  25.414  1.00 31.49           C  
-ATOM     55  CH2 TRP A   6      31.571  32.217  26.109  1.00 24.51           C  
-ATOM     56  N   LYS A   7      31.053  33.923  18.049  1.00 15.42           N  
-ATOM     57  CA  LYS A   7      30.623  34.838  16.993  1.00 16.83           C  
-ATOM     58  C   LYS A   7      29.717  33.989  16.098  1.00 14.40           C  
-ATOM     59  O   LYS A   7      29.728  32.764  16.202  1.00 13.12           O  
-ATOM     60  CB  LYS A   7      31.829  35.357  16.199  1.00 23.43           C  
-ATOM     61  CG  LYS A   7      32.934  36.007  17.050  1.00 34.36           C  
-ATOM     62  CD  LYS A   7      32.879  37.553  17.057  1.00 49.16           C  
-ATOM     63  CE  LYS A   7      31.720  38.166  17.886  1.00 55.07           C  
-ATOM     64  NZ  LYS A   7      31.767  37.834  19.351  1.00 59.66           N  
-ATOM     65  N   ARG A   8      28.910  34.637  15.266  1.00 15.07           N  
-ATOM     66  CA  ARG A   8      28.033  33.951  14.309  1.00 13.70           C  
-ATOM     67  C   ARG A   8      28.905  33.109  13.366  1.00 13.88           C  
-ATOM     68  O   ARG A   8      29.894  33.603  12.836  1.00 12.66           O  
-ATOM     69  CB  ARG A   8      27.222  34.996  13.532  1.00 12.95           C  
-ATOM     70  CG  ARG A   8      25.788  35.057  13.979  1.00 14.44           C  
-ATOM     71  CD  ARG A   8      25.240  36.413  14.265  1.00 19.85           C  
-ATOM     72  NE  ARG A   8      24.725  37.060  13.076  1.00 28.34           N  
-ATOM     73  CZ  ARG A   8      23.668  37.873  13.035  1.00 31.69           C  
-ATOM     74  NH1 ARG A   8      22.958  38.150  14.121  1.00 25.38           N  
-ATOM     75  NH2 ARG A   8      23.380  38.496  11.898  1.00 38.95           N  
-ATOM     76  N   PRO A   9      28.602  31.800  13.207  1.00 14.63           N  
-ATOM     77  CA  PRO A   9      29.392  30.923  12.328  1.00 12.85           C  
-ATOM     78  C   PRO A   9      29.107  31.211  10.841  1.00 14.51           C  
-ATOM     79  O   PRO A   9      28.306  30.547  10.193  1.00 16.67           O  
-ATOM     80  CB  PRO A   9      28.942  29.520  12.752  1.00 10.72           C  
-ATOM     81  CG  PRO A   9      27.503  29.738  13.078  1.00 11.90           C  
-ATOM     82  CD  PRO A   9      27.475  31.070  13.821  1.00 10.21           C  
-ATOM     83  N   VAL A  10      29.773  32.227  10.323  1.00 14.65           N  
-ATOM     84  CA  VAL A  10      29.609  32.676   8.955  1.00 16.81           C  
-ATOM     85  C   VAL A  10      30.826  32.366   8.075  1.00 18.64           C  
-ATOM     86  O   VAL A  10      31.961  32.590   8.480  1.00 19.11           O  
-ATOM     87  CB  VAL A  10      29.351  34.198   8.969  1.00 20.30           C  
-ATOM     88  CG1 VAL A  10      29.416  34.784   7.568  1.00 24.25           C  
-ATOM     89  CG2 VAL A  10      27.993  34.487   9.614  1.00 17.11           C  
-ATOM     90  N   VAL A  11      30.587  31.831   6.883  1.00 19.40           N  
-ATOM     91  CA  VAL A  11      31.665  31.521   5.941  1.00 17.34           C  
-ATOM     92  C   VAL A  11      31.232  31.954   4.544  1.00 18.94           C  
-ATOM     93  O   VAL A  11      30.069  32.343   4.317  1.00 18.21           O  
-ATOM     94  CB  VAL A  11      32.016  29.993   5.912  1.00 20.36           C  
-ATOM     95  CG1 VAL A  11      32.585  29.542   7.257  1.00 21.41           C  
-ATOM     96  CG2 VAL A  11      30.784  29.170   5.546  1.00 14.69           C  
-ATOM     97  N   THR A  12      32.168  31.902   3.609  1.00 17.57           N  
-ATOM     98  CA  THR A  12      31.868  32.260   2.239  1.00 16.62           C  
-ATOM     99  C   THR A  12      31.604  30.994   1.440  1.00 14.78           C  
-ATOM    100  O   THR A  12      32.345  30.027   1.550  1.00 16.13           O  
-ATOM    101  CB  THR A  12      33.025  33.043   1.630  1.00 21.41           C  
-ATOM    102  OG1 THR A  12      33.235  34.221   2.415  1.00 24.60           O  
-ATOM    103  CG2 THR A  12      32.719  33.431   0.186  1.00 24.69           C  
-ATOM    104  N   ALA A  13      30.504  30.972   0.707  1.00 12.83           N  
-ATOM    105  CA  ALA A  13      30.165  29.820  -0.113  1.00 17.95           C  
-ATOM    106  C   ALA A  13      29.980  30.250  -1.576  1.00 19.12           C  
-ATOM    107  O   ALA A  13      29.745  31.431  -1.879  1.00 16.16           O  
-ATOM    108  CB  ALA A  13      28.887  29.125   0.423  1.00 15.59           C  
-ATOM    109  N   TYR A  14      30.121  29.284  -2.477  1.00 19.09           N  
-ATOM    110  CA  TYR A  14      29.948  29.532  -3.908  1.00 18.17           C  
-ATOM    111  C   TYR A  14      28.809  28.674  -4.373  1.00 17.07           C  
-ATOM    112  O   TYR A  14      28.872  27.457  -4.271  1.00 17.93           O  
-ATOM    113  CB  TYR A  14      31.217  29.179  -4.676  1.00 13.69           C  
-ATOM    114  CG  TYR A  14      32.337  30.098  -4.335  1.00 19.72           C  
-ATOM    115  CD1 TYR A  14      33.143  29.855  -3.227  1.00 27.28           C  
-ATOM    116  CD2 TYR A  14      32.555  31.261  -5.065  1.00 24.63           C  
-ATOM    117  CE1 TYR A  14      34.133  30.749  -2.851  1.00 31.91           C  
-ATOM    118  CE2 TYR A  14      33.549  32.165  -4.696  1.00 27.83           C  
-ATOM    119  CZ  TYR A  14      34.331  31.901  -3.588  1.00 31.23           C  
-ATOM    120  OH  TYR A  14      35.327  32.780  -3.213  1.00 44.29           O  
-ATOM    121  N   ILE A  15      27.743  29.322  -4.814  1.00 17.42           N  
-ATOM    122  CA  ILE A  15      26.544  28.639  -5.301  1.00 16.49           C  
-ATOM    123  C   ILE A  15      26.513  28.884  -6.807  1.00 16.61           C  
-ATOM    124  O   ILE A  15      26.226  29.991  -7.242  1.00 17.58           O  
-ATOM    125  CB  ILE A  15      25.312  29.248  -4.634  1.00 15.17           C  
-ATOM    126  CG1 ILE A  15      25.402  29.009  -3.112  1.00 23.46           C  
-ATOM    127  CG2 ILE A  15      24.049  28.663  -5.214  1.00  9.83           C  
-ATOM    128  CD1 ILE A  15      24.447  29.849  -2.302  1.00 20.18           C  
-ATOM    129  N   GLU A  16      26.888  27.866  -7.584  1.00 16.92           N  
-ATOM    130  CA  GLU A  16      26.960  27.962  -9.044  1.00 16.83           C  
-ATOM    131  C   GLU A  16      27.913  29.089  -9.420  1.00 19.38           C  
-ATOM    132  O   GLU A  16      27.627  29.916 -10.298  1.00 21.03           O  
-ATOM    133  CB  GLU A  16      25.588  28.222  -9.666  1.00 11.07           C  
-ATOM    134  CG  GLU A  16      24.548  27.130  -9.435  1.00 21.10           C  
-ATOM    135  CD  GLU A  16      24.834  25.794 -10.114  1.00 28.51           C  
-ATOM    136  OE1 GLU A  16      25.812  25.663 -10.878  1.00 36.11           O  
-ATOM    137  OE2 GLU A  16      24.049  24.848  -9.890  1.00 30.06           O  
-ATOM    138  N   GLY A  17      29.027  29.148  -8.700  1.00 20.16           N  
-ATOM    139  CA  GLY A  17      30.039  30.157  -8.948  1.00 22.21           C  
-ATOM    140  C   GLY A  17      29.853  31.495  -8.231  1.00 23.07           C  
-ATOM    141  O   GLY A  17      30.817  32.228  -8.043  1.00 24.98           O  
-ATOM    142  N   GLN A  18      28.637  31.810  -7.805  1.00 19.71           N  
-ATOM    143  CA  GLN A  18      28.392  33.088  -7.159  1.00 20.96           C  
-ATOM    144  C   GLN A  18      28.767  33.050  -5.659  1.00 22.28           C  
-ATOM    145  O   GLN A  18      28.221  32.254  -4.882  1.00 21.48           O  
-ATOM    146  CB  GLN A  18      26.921  33.455  -7.351  1.00 26.30           C  
-ATOM    147  CG  GLN A  18      26.311  32.995  -8.686  1.00 42.33           C  
-ATOM    148  CD  GLN A  18      24.784  33.210  -8.773  1.00 55.39           C  
-ATOM    149  OE1 GLN A  18      24.307  34.330  -9.002  1.00 60.33           O  
-ATOM    150  NE2 GLN A  18      24.018  32.136  -8.582  1.00 56.45           N  
-ATOM    151  N   PRO A  19      29.699  33.921  -5.232  1.00 21.36           N  
-ATOM    152  CA  PRO A  19      30.171  34.017  -3.844  1.00 20.10           C  
-ATOM    153  C   PRO A  19      29.081  34.587  -2.937  1.00 21.37           C  
-ATOM    154  O   PRO A  19      28.514  35.640  -3.226  1.00 25.01           O  
-ATOM    155  CB  PRO A  19      31.333  35.019  -3.935  1.00 21.06           C  
-ATOM    156  CG  PRO A  19      31.596  35.186  -5.421  1.00 21.15           C  
-ATOM    157  CD  PRO A  19      30.264  35.007  -6.047  1.00 21.25           C  
-ATOM    158  N   VAL A  20      28.836  33.948  -1.809  1.00 18.94           N  
-ATOM    159  CA  VAL A  20      27.821  34.426  -0.900  1.00 20.02           C  
-ATOM    160  C   VAL A  20      28.279  34.154   0.551  1.00 19.96           C  
-ATOM    161  O   VAL A  20      29.046  33.254   0.807  1.00 21.75           O  
-ATOM    162  CB  VAL A  20      26.489  33.747  -1.243  1.00 24.13           C  
-ATOM    163  CG1 VAL A  20      26.585  32.257  -0.999  1.00 28.66           C  
-ATOM    164  CG2 VAL A  20      25.373  34.344  -0.481  1.00 28.90           C  
-ATOM    165  N   GLU A  21      27.929  35.028   1.476  1.00 19.63           N  
-ATOM    166  CA  GLU A  21      28.316  34.842   2.867  1.00 17.06           C  
-ATOM    167  C   GLU A  21      27.109  34.169   3.485  1.00 16.33           C  
-ATOM    168  O   GLU A  21      25.990  34.678   3.346  1.00 15.38           O  
-ATOM    169  CB  GLU A  21      28.530  36.203   3.500  1.00 22.90           C  
-ATOM    170  CG  GLU A  21      29.578  36.232   4.580  1.00 45.43           C  
-ATOM    171  CD  GLU A  21      31.002  36.125   4.038  1.00 58.38           C  
-ATOM    172  OE1 GLU A  21      31.197  36.269   2.800  1.00 63.42           O  
-ATOM    173  OE2 GLU A  21      31.929  35.906   4.864  1.00 62.09           O  
-ATOM    174  N   VAL A  22      27.310  33.001   4.087  1.00 15.04           N  
-ATOM    175  CA  VAL A  22      26.208  32.247   4.702  1.00 15.47           C  
-ATOM    176  C   VAL A  22      26.459  31.901   6.167  1.00 14.30           C  
-ATOM    177  O   VAL A  22      27.609  31.718   6.583  1.00 13.28           O  
-ATOM    178  CB  VAL A  22      25.947  30.896   3.970  1.00 13.04           C  
-ATOM    179  CG1 VAL A  22      25.511  31.143   2.571  1.00 13.39           C  
-ATOM    180  CG2 VAL A  22      27.199  30.030   3.971  1.00 14.24           C  
-ATOM    181  N   LEU A  23      25.358  31.727   6.900  1.00 13.88           N  
-ATOM    182  CA  LEU A  23      25.363  31.355   8.309  1.00 12.07           C  
-ATOM    183  C   LEU A  23      25.153  29.853   8.378  1.00 10.67           C  
-ATOM    184  O   LEU A  23      24.196  29.337   7.791  1.00  8.36           O  
-ATOM    185  CB  LEU A  23      24.185  32.046   9.046  1.00 17.15           C  
-ATOM    186  CG  LEU A  23      23.878  31.709  10.531  1.00 12.45           C  
-ATOM    187  CD1 LEU A  23      25.051  32.103  11.330  1.00  8.26           C  
-ATOM    188  CD2 LEU A  23      22.699  32.497  11.043  1.00 15.36           C  
-ATOM    189  N   LEU A  24      26.024  29.145   9.095  1.00 11.57           N  
-ATOM    190  CA  LEU A  24      25.896  27.693   9.247  1.00 10.84           C  
-ATOM    191  C   LEU A  24      24.875  27.522  10.361  1.00 10.54           C  
-ATOM    192  O   LEU A  24      25.178  27.708  11.525  1.00 10.52           O  
-ATOM    193  CB  LEU A  24      27.245  27.066   9.598  1.00  8.46           C  
-ATOM    194  CG  LEU A  24      28.312  27.452   8.560  1.00 10.20           C  
-ATOM    195  CD1 LEU A  24      29.689  26.943   8.982  1.00  9.77           C  
-ATOM    196  CD2 LEU A  24      27.905  26.934   7.195  1.00  7.47           C  
-ATOM    197  N   ASP A  25      23.699  27.038  10.000  1.00 11.81           N  
-ATOM    198  CA  ASP A  25      22.587  26.948  10.923  1.00 11.26           C  
-ATOM    199  C   ASP A  25      22.021  25.553  11.259  1.00 11.70           C  
-ATOM    200  O   ASP A  25      21.313  24.961  10.454  1.00  9.72           O  
-ATOM    201  CB  ASP A  25      21.489  27.831  10.325  1.00 13.03           C  
-ATOM    202  CG  ASP A  25      20.367  28.183  11.290  1.00 17.95           C  
-ATOM    203  OD1 ASP A  25      20.270  27.655  12.433  1.00 15.69           O  
-ATOM    204  OD2 ASP A  25      19.558  29.010  10.865  1.00 19.65           O  
-ATOM    205  N   THR A  26      22.253  25.114  12.502  1.00  9.98           N  
-ATOM    206  CA  THR A  26      21.757  23.830  12.963  1.00 11.28           C  
-ATOM    207  C   THR A  26      20.247  23.881  13.259  1.00 13.22           C  
-ATOM    208  O   THR A  26      19.618  22.846  13.334  1.00 14.55           O  
-ATOM    209  CB  THR A  26      22.547  23.292  14.213  1.00 12.26           C  
-ATOM    210  OG1 THR A  26      22.277  24.098  15.363  1.00 12.92           O  
-ATOM    211  CG2 THR A  26      24.074  23.290  13.935  1.00 10.89           C  
-ATOM    212  N   GLY A  27      19.662  25.074  13.406  1.00 13.31           N  
-ATOM    213  CA  GLY A  27      18.230  25.181  13.672  1.00 10.54           C  
-ATOM    214  C   GLY A  27      17.404  25.455  12.415  1.00 12.66           C  
-ATOM    215  O   GLY A  27      16.302  26.033  12.474  1.00 11.29           O  
-ATOM    216  N   ALA A  28      17.976  25.133  11.255  1.00 10.82           N  
-ATOM    217  CA  ALA A  28      17.253  25.295   9.993  1.00 12.90           C  
-ATOM    218  C   ALA A  28      17.223  23.958   9.243  1.00 13.95           C  
-ATOM    219  O   ALA A  28      18.263  23.318   9.081  1.00 14.01           O  
-ATOM    220  CB  ALA A  28      17.897  26.369   9.110  1.00  8.39           C  
-ATOM    221  N   ASP A  29      16.032  23.525   8.821  1.00 15.87           N  
-ATOM    222  CA  ASP A  29      15.906  22.285   8.038  1.00 19.37           C  
-ATOM    223  C   ASP A  29      16.409  22.538   6.622  1.00 17.50           C  
-ATOM    224  O   ASP A  29      17.036  21.666   6.038  1.00 18.49           O  
-ATOM    225  CB  ASP A  29      14.451  21.811   7.919  1.00 15.77           C  
-ATOM    226  CG  ASP A  29      13.813  21.514   9.266  1.00 22.59           C  
-ATOM    227  OD1 ASP A  29      14.537  21.276  10.256  1.00 21.07           O  
-ATOM    228  OD2 ASP A  29      12.564  21.524   9.329  1.00 22.67           O  
-ATOM    229  N   ASP A  30      16.161  23.744   6.110  1.00 16.75           N  
-ATOM    230  CA  ASP A  30      16.541  24.118   4.744  1.00 17.33           C  
-ATOM    231  C   ASP A  30      17.562  25.247   4.640  1.00 16.91           C  
-ATOM    232  O   ASP A  30      17.930  25.865   5.646  1.00 19.16           O  
-ATOM    233  CB  ASP A  30      15.299  24.545   3.944  1.00 17.54           C  
-ATOM    234  CG  ASP A  30      14.141  23.602   4.133  1.00 23.47           C  
-ATOM    235  OD1 ASP A  30      14.308  22.393   3.881  1.00 27.93           O  
-ATOM    236  OD2 ASP A  30      13.067  24.067   4.575  1.00 29.76           O  
-ATOM    237  N   SER A  31      17.999  25.506   3.405  1.00 15.80           N  
-ATOM    238  CA  SER A  31      18.960  26.558   3.094  1.00 12.47           C  
-ATOM    239  C   SER A  31      18.232  27.601   2.269  1.00 13.11           C  
-ATOM    240  O   SER A  31      17.473  27.265   1.353  1.00 14.00           O  
-ATOM    241  CB  SER A  31      20.140  25.984   2.318  1.00 11.15           C  
-ATOM    242  OG  SER A  31      20.816  25.017   3.098  1.00 13.72           O  
-ATOM    243  N   ILE A  32      18.379  28.858   2.652  1.00 13.11           N  
-ATOM    244  CA  ILE A  32      17.716  29.930   1.936  1.00 15.70           C  
-ATOM    245  C   ILE A  32      18.710  31.064   1.718  1.00 19.35           C  
-ATOM    246  O   ILE A  32      19.436  31.455   2.649  1.00 19.95           O  
-ATOM    247  CB  ILE A  32      16.403  30.375   2.639  1.00 16.22           C  
-ATOM    248  CG1 ILE A  32      15.997  31.774   2.182  1.00 17.05           C  
-ATOM    249  CG2 ILE A  32      16.568  30.320   4.109  1.00 20.63           C  
-ATOM    250  CD1 ILE A  32      14.570  31.938   1.831  1.00 22.84           C  
-ATOM    251  N   VAL A  33      18.764  31.544   0.474  1.00 17.64           N  
-ATOM    252  CA  VAL A  33      19.692  32.570   0.064  1.00 18.41           C  
-ATOM    253  C   VAL A  33      18.968  33.680  -0.674  1.00 20.93           C  
-ATOM    254  O   VAL A  33      18.008  33.431  -1.395  1.00 22.55           O  
-ATOM    255  CB  VAL A  33      20.787  31.958  -0.861  1.00 19.99           C  
-ATOM    256  CG1 VAL A  33      21.740  33.015  -1.351  1.00 17.25           C  
-ATOM    257  CG2 VAL A  33      21.573  30.872  -0.108  1.00 20.38           C  
-ATOM    258  N   ALA A  34      19.459  34.900  -0.488  1.00 21.17           N  
-ATOM    259  CA  ALA A  34      18.904  36.086  -1.120  1.00 20.60           C  
-ATOM    260  C   ALA A  34      19.903  36.638  -2.123  1.00 21.51           C  
-ATOM    261  O   ALA A  34      21.098  36.340  -2.066  1.00 24.07           O  
-ATOM    262  CB  ALA A  34      18.621  37.143  -0.055  1.00 13.67           C  
-ATOM    263  N   GLY A  35      19.407  37.385  -3.093  1.00 24.93           N  
-ATOM    264  CA  GLY A  35      20.303  38.017  -4.045  1.00 26.41           C  
-ATOM    265  C   GLY A  35      20.984  37.243  -5.150  1.00 28.66           C  
-ATOM    266  O   GLY A  35      21.903  37.785  -5.758  1.00 30.52           O  
-ATOM    267  N   ILE A  36      20.618  35.988  -5.400  1.00 28.03           N  
-ATOM    268  CA  ILE A  36      21.253  35.263  -6.504  1.00 28.59           C  
-ATOM    269  C   ILE A  36      20.226  34.773  -7.507  1.00 27.99           C  
-ATOM    270  O   ILE A  36      19.085  34.507  -7.151  1.00 27.85           O  
-ATOM    271  CB  ILE A  36      22.110  34.067  -6.033  1.00 33.17           C  
-ATOM    272  CG1 ILE A  36      21.257  33.016  -5.333  1.00 33.81           C  
-ATOM    273  CG2 ILE A  36      23.203  34.539  -5.090  1.00 36.66           C  
-ATOM    274  CD1 ILE A  36      22.015  31.752  -5.064  1.00 43.43           C  
-ATOM    275  N   GLU A  37      20.613  34.694  -8.774  1.00 31.39           N  
-ATOM    276  CA  GLU A  37      19.684  34.227  -9.803  1.00 30.95           C  
-ATOM    277  C   GLU A  37      20.037  32.796 -10.159  1.00 26.97           C  
-ATOM    278  O   GLU A  37      21.179  32.516 -10.504  1.00 30.24           O  
-ATOM    279  CB  GLU A  37      19.764  35.111 -11.041  1.00 37.99           C  
-ATOM    280  CG  GLU A  37      18.421  35.654 -11.511  1.00 52.35           C  
-ATOM    281  CD  GLU A  37      17.788  36.621 -10.520  1.00 60.80           C  
-ATOM    282  OE1 GLU A  37      18.177  37.812 -10.533  1.00 65.64           O  
-ATOM    283  OE2 GLU A  37      16.899  36.192  -9.740  1.00 64.16           O  
-ATOM    284  N   LEU A  38      19.065  31.894 -10.081  1.00 24.46           N  
-ATOM    285  CA  LEU A  38      19.322  30.493 -10.379  1.00 23.23           C  
-ATOM    286  C   LEU A  38      18.579  29.903 -11.571  1.00 22.86           C  
-ATOM    287  O   LEU A  38      18.775  28.727 -11.911  1.00 21.49           O  
-ATOM    288  CB  LEU A  38      19.135  29.614  -9.134  1.00 22.45           C  
-ATOM    289  CG  LEU A  38      20.268  29.728  -8.098  1.00 22.31           C  
-ATOM    290  CD1 LEU A  38      19.902  28.965  -6.820  1.00 22.15           C  
-ATOM    291  CD2 LEU A  38      21.593  29.233  -8.698  1.00  9.79           C  
-ATOM    292  N   GLY A  39      17.725  30.697 -12.205  1.00 20.13           N  
-ATOM    293  CA  GLY A  39      17.028  30.187 -13.359  1.00 17.61           C  
-ATOM    294  C   GLY A  39      15.570  29.831 -13.212  1.00 20.80           C  
-ATOM    295  O   GLY A  39      14.895  30.164 -12.236  1.00 18.31           O  
-ATOM    296  N   ASN A  40      15.112  29.039 -14.172  1.00 22.90           N  
-ATOM    297  CA  ASN A  40      13.711  28.651 -14.263  1.00 23.35           C  
-ATOM    298  C   ASN A  40      13.284  27.269 -13.711  1.00 20.63           C  
-ATOM    299  O   ASN A  40      12.091  27.007 -13.589  1.00 19.45           O  
-ATOM    300  CB  ASN A  40      13.269  28.816 -15.734  1.00 23.52           C  
-ATOM    301  CG  ASN A  40      11.765  28.833 -15.894  1.00 24.79           C  
-ATOM    302  OD1 ASN A  40      11.216  28.105 -16.699  1.00 36.08           O  
-ATOM    303  ND2 ASN A  40      11.086  29.634 -15.093  1.00 23.10           N  
-ATOM    304  N   ASN A  41      14.235  26.409 -13.348  1.00 17.11           N  
-ATOM    305  CA  ASN A  41      13.894  25.103 -12.824  1.00 17.58           C  
-ATOM    306  C   ASN A  41      13.598  25.133 -11.310  1.00 17.95           C  
-ATOM    307  O   ASN A  41      14.326  24.559 -10.495  1.00 17.01           O  
-ATOM    308  CB  ASN A  41      14.994  24.099 -13.164  1.00 17.12           C  
-ATOM    309  CG  ASN A  41      14.575  22.652 -12.915  1.00 26.32           C  
-ATOM    310  OD1 ASN A  41      13.389  22.327 -12.743  1.00 30.02           O  
-ATOM    311  ND2 ASN A  41      15.554  21.773 -12.887  1.00 30.69           N  
-ATOM    312  N   TYR A  42      12.478  25.741 -10.948  1.00 14.56           N  
-ATOM    313  CA  TYR A  42      12.126  25.840  -9.560  1.00 16.41           C  
-ATOM    314  C   TYR A  42      10.644  25.622  -9.380  1.00 18.38           C  
-ATOM    315  O   TYR A  42       9.882  25.772 -10.330  1.00 17.90           O  
-ATOM    316  CB  TYR A  42      12.480  27.249  -9.018  1.00 10.95           C  
-ATOM    317  CG  TYR A  42      11.642  28.387  -9.595  1.00 12.70           C  
-ATOM    318  CD1 TYR A  42      10.356  28.676  -9.090  1.00 12.04           C  
-ATOM    319  CD2 TYR A  42      12.091  29.112 -10.698  1.00 15.18           C  
-ATOM    320  CE1 TYR A  42       9.543  29.640  -9.689  1.00 13.90           C  
-ATOM    321  CE2 TYR A  42      11.292  30.087 -11.305  1.00 12.41           C  
-ATOM    322  CZ  TYR A  42      10.027  30.344 -10.802  1.00 19.74           C  
-ATOM    323  OH  TYR A  42       9.255  31.297 -11.427  1.00 17.28           O  
-ATOM    324  N   SER A  43      10.258  25.291  -8.147  1.00 19.66           N  
-ATOM    325  CA  SER A  43       8.865  25.163  -7.747  1.00 21.63           C  
-ATOM    326  C   SER A  43       8.767  26.121  -6.550  1.00 21.20           C  
-ATOM    327  O   SER A  43       9.762  26.357  -5.868  1.00 20.58           O  
-ATOM    328  CB  SER A  43       8.516  23.731  -7.330  1.00 21.02           C  
-ATOM    329  OG  SER A  43       9.591  23.139  -6.643  1.00 30.11           O  
-ATOM    330  N   PRO A  44       7.633  26.822  -6.404  1.00 21.66           N  
-ATOM    331  CA  PRO A  44       7.414  27.761  -5.304  1.00 22.43           C  
-ATOM    332  C   PRO A  44       7.240  26.955  -4.021  1.00 22.95           C  
-ATOM    333  O   PRO A  44       6.638  25.883  -4.043  1.00 24.99           O  
-ATOM    334  CB  PRO A  44       6.106  28.443  -5.712  1.00 24.63           C  
-ATOM    335  CG  PRO A  44       5.378  27.353  -6.429  1.00 24.54           C  
-ATOM    336  CD  PRO A  44       6.479  26.826  -7.322  1.00 20.56           C  
-ATOM    337  N   LYS A  45       7.747  27.473  -2.912  1.00 23.90           N  
-ATOM    338  CA  LYS A  45       7.677  26.777  -1.632  1.00 25.25           C  
-ATOM    339  C   LYS A  45       7.423  27.798  -0.524  1.00 23.78           C  
-ATOM    340  O   LYS A  45       7.778  28.964  -0.660  1.00 23.33           O  
-ATOM    341  CB  LYS A  45       9.019  26.089  -1.376  1.00 29.18           C  
-ATOM    342  CG  LYS A  45       8.933  24.775  -0.664  1.00 38.87           C  
-ATOM    343  CD  LYS A  45       8.200  23.770  -1.524  1.00 47.05           C  
-ATOM    344  CE  LYS A  45       8.508  22.340  -1.081  1.00 56.72           C  
-ATOM    345  NZ  LYS A  45       8.030  21.313  -2.052  1.00 64.65           N  
-ATOM    346  N   ILE A  46       6.787  27.365   0.557  1.00 22.57           N  
-ATOM    347  CA  ILE A  46       6.534  28.253   1.699  1.00 26.44           C  
-ATOM    348  C   ILE A  46       7.474  27.806   2.789  1.00 24.48           C  
-ATOM    349  O   ILE A  46       7.640  26.613   3.002  1.00 27.97           O  
-ATOM    350  CB  ILE A  46       5.097  28.119   2.277  1.00 32.01           C  
-ATOM    351  CG1 ILE A  46       4.067  28.491   1.217  1.00 38.58           C  
-ATOM    352  CG2 ILE A  46       4.910  29.069   3.457  1.00 26.98           C  
-ATOM    353  CD1 ILE A  46       4.147  29.926   0.793  1.00 37.32           C  
-ATOM    354  N   VAL A  47       8.131  28.739   3.452  1.00 23.71           N  
-ATOM    355  CA  VAL A  47       9.011  28.358   4.536  1.00 24.07           C  
-ATOM    356  C   VAL A  47       8.642  29.196   5.761  1.00 21.79           C  
-ATOM    357  O   VAL A  47       8.311  30.380   5.646  1.00 19.02           O  
-ATOM    358  CB  VAL A  47      10.516  28.455   4.126  1.00 25.59           C  
-ATOM    359  CG1 VAL A  47      11.006  29.879   4.125  1.00 34.34           C  
-ATOM    360  CG2 VAL A  47      11.347  27.610   5.050  1.00 29.95           C  
-ATOM    361  N   GLY A  48       8.577  28.542   6.914  1.00 22.55           N  
-ATOM    362  CA  GLY A  48       8.211  29.238   8.137  1.00 21.39           C  
-ATOM    363  C   GLY A  48       9.349  29.406   9.113  1.00 21.96           C  
-ATOM    364  O   GLY A  48      10.178  28.506   9.266  1.00 23.74           O  
-ATOM    365  N   GLY A  49       9.376  30.554   9.777  1.00 21.16           N  
-ATOM    366  CA  GLY A  49      10.408  30.847  10.743  1.00 21.30           C  
-ATOM    367  C   GLY A  49       9.790  31.391  12.003  1.00 22.58           C  
-ATOM    368  O   GLY A  49       8.623  31.142  12.286  1.00 21.80           O  
-ATOM    369  N   ILE A  50      10.537  32.206  12.738  1.00 23.79           N  
-ATOM    370  CA  ILE A  50      10.002  32.750  13.975  1.00 24.13           C  
-ATOM    371  C   ILE A  50       8.921  33.830  13.833  1.00 25.92           C  
-ATOM    372  O   ILE A  50       7.975  33.856  14.620  1.00 31.08           O  
-ATOM    373  CB  ILE A  50      11.132  33.148  14.989  1.00 21.82           C  
-ATOM    374  CG1 ILE A  50      10.739  32.710  16.384  1.00 20.03           C  
-ATOM    375  CG2 ILE A  50      11.388  34.636  15.008  1.00 15.57           C  
-ATOM    376  CD1 ILE A  50      11.733  33.125  17.371  1.00 31.41           C  
-ATOM    377  N   GLY A  51       8.998  34.688  12.827  1.00 21.53           N  
-ATOM    378  CA  GLY A  51       7.955  35.692  12.742  1.00 21.00           C  
-ATOM    379  C   GLY A  51       6.813  35.384  11.791  1.00 23.88           C  
-ATOM    380  O   GLY A  51       5.884  36.169  11.691  1.00 30.31           O  
-ATOM    381  N   GLY A  52       6.850  34.235  11.128  1.00 22.60           N  
-ATOM    382  CA  GLY A  52       5.817  33.897  10.165  1.00 22.52           C  
-ATOM    383  C   GLY A  52       6.360  33.116   8.970  1.00 22.68           C  
-ATOM    384  O   GLY A  52       7.419  32.503   9.054  1.00 25.13           O  
-ATOM    385  N   PHE A  53       5.664  33.155   7.846  1.00 22.81           N  
-ATOM    386  CA  PHE A  53       6.088  32.411   6.661  1.00 23.34           C  
-ATOM    387  C   PHE A  53       6.522  33.323   5.548  1.00 23.50           C  
-ATOM    388  O   PHE A  53       6.243  34.516   5.590  1.00 28.26           O  
-ATOM    389  CB  PHE A  53       4.938  31.572   6.133  1.00 20.09           C  
-ATOM    390  CG  PHE A  53       4.438  30.551   7.100  1.00 22.36           C  
-ATOM    391  CD1 PHE A  53       3.479  30.886   8.046  1.00 20.68           C  
-ATOM    392  CD2 PHE A  53       4.912  29.245   7.049  1.00 22.84           C  
-ATOM    393  CE1 PHE A  53       2.998  29.933   8.930  1.00 25.02           C  
-ATOM    394  CE2 PHE A  53       4.443  28.285   7.920  1.00 23.74           C  
-ATOM    395  CZ  PHE A  53       3.484  28.624   8.868  1.00 27.29           C  
-ATOM    396  N   ILE A  54       7.258  32.785   4.584  1.00 23.01           N  
-ATOM    397  CA  ILE A  54       7.681  33.557   3.420  1.00 22.00           C  
-ATOM    398  C   ILE A  54       7.711  32.631   2.222  1.00 22.83           C  
-ATOM    399  O   ILE A  54       7.900  31.437   2.388  1.00 24.18           O  
-ATOM    400  CB  ILE A  54       9.081  34.186   3.569  1.00 24.20           C  
-ATOM    401  CG1 ILE A  54      10.171  33.120   3.663  1.00 17.00           C  
-ATOM    402  CG2 ILE A  54       9.115  35.109   4.744  1.00 25.47           C  
-ATOM    403  CD1 ILE A  54      11.551  33.727   3.561  1.00 18.06           C  
-ATOM    404  N   ASN A  55       7.491  33.185   1.029  1.00 25.80           N  
-ATOM    405  CA  ASN A  55       7.509  32.430  -0.235  1.00 23.62           C  
-ATOM    406  C   ASN A  55       8.939  32.362  -0.666  1.00 20.22           C  
-ATOM    407  O   ASN A  55       9.713  33.281  -0.410  1.00 22.89           O  
-ATOM    408  CB  ASN A  55       6.743  33.166  -1.334  1.00 26.51           C  
-ATOM    409  CG  ASN A  55       5.308  33.384  -0.978  1.00 36.13           C  
-ATOM    410  OD1 ASN A  55       4.683  32.544  -0.346  1.00 42.81           O  
-ATOM    411  ND2 ASN A  55       4.766  34.518  -1.377  1.00 45.39           N  
-ATOM    412  N   THR A  56       9.280  31.299  -1.356  1.00 17.06           N  
-ATOM    413  CA  THR A  56      10.626  31.110  -1.837  1.00 17.52           C  
-ATOM    414  C   THR A  56      10.536  30.328  -3.146  1.00 20.29           C  
-ATOM    415  O   THR A  56       9.464  29.811  -3.526  1.00 18.75           O  
-ATOM    416  CB  THR A  56      11.423  30.243  -0.851  1.00 20.86           C  
-ATOM    417  OG1 THR A  56      10.761  28.972  -0.709  1.00 18.97           O  
-ATOM    418  CG2 THR A  56      11.543  30.932   0.524  1.00 16.38           C  
-ATOM    419  N   LYS A  57      11.649  30.261  -3.858  1.00 19.32           N  
-ATOM    420  CA  LYS A  57      11.687  29.479  -5.076  1.00 18.80           C  
-ATOM    421  C   LYS A  57      12.638  28.382  -4.701  1.00 16.97           C  
-ATOM    422  O   LYS A  57      13.721  28.658  -4.210  1.00 20.73           O  
-ATOM    423  CB  LYS A  57      12.214  30.307  -6.232  1.00 19.80           C  
-ATOM    424  CG  LYS A  57      11.252  31.411  -6.652  1.00 19.30           C  
-ATOM    425  CD  LYS A  57      11.859  32.228  -7.745  1.00 23.97           C  
-ATOM    426  CE  LYS A  57      10.842  33.113  -8.404  1.00 38.52           C  
-ATOM    427  NZ  LYS A  57      11.417  33.677  -9.675  1.00 50.08           N  
-ATOM    428  N   GLU A  58      12.202  27.143  -4.837  1.00 15.68           N  
-ATOM    429  CA  GLU A  58      13.040  26.018  -4.483  1.00 14.81           C  
-ATOM    430  C   GLU A  58      13.742  25.372  -5.684  1.00 17.35           C  
-ATOM    431  O   GLU A  58      13.099  24.806  -6.578  1.00 17.49           O  
-ATOM    432  CB  GLU A  58      12.218  24.970  -3.730  1.00 15.33           C  
-ATOM    433  CG  GLU A  58      13.019  23.719  -3.402  1.00 18.43           C  
-ATOM    434  CD  GLU A  58      12.166  22.577  -2.904  1.00 24.57           C  
-ATOM    435  OE1 GLU A  58      11.230  22.152  -3.617  1.00 34.15           O  
-ATOM    436  OE2 GLU A  58      12.456  22.073  -1.809  1.00 31.74           O  
-ATOM    437  N   TYR A  59      15.069  25.456  -5.680  1.00 16.28           N  
-ATOM    438  CA  TYR A  59      15.908  24.886  -6.715  1.00 13.95           C  
-ATOM    439  C   TYR A  59      16.556  23.617  -6.157  1.00 16.57           C  
-ATOM    440  O   TYR A  59      17.190  23.651  -5.114  1.00 18.18           O  
-ATOM    441  CB  TYR A  59      16.992  25.885  -7.085  1.00  7.75           C  
-ATOM    442  CG  TYR A  59      16.468  27.135  -7.756  1.00  7.51           C  
-ATOM    443  CD1 TYR A  59      16.044  28.218  -7.003  1.00  5.52           C  
-ATOM    444  CD2 TYR A  59      16.378  27.221  -9.152  1.00  8.24           C  
-ATOM    445  CE1 TYR A  59      15.549  29.365  -7.611  1.00  8.08           C  
-ATOM    446  CE2 TYR A  59      15.887  28.355  -9.765  1.00  9.91           C  
-ATOM    447  CZ  TYR A  59      15.473  29.421  -8.989  1.00 12.41           C  
-ATOM    448  OH  TYR A  59      14.992  30.555  -9.597  1.00 14.43           O  
-ATOM    449  N   LYS A  60      16.424  22.501  -6.857  1.00 16.25           N  
-ATOM    450  CA  LYS A  60      17.019  21.275  -6.376  1.00 17.91           C  
-ATOM    451  C   LYS A  60      18.294  20.976  -7.112  1.00 18.49           C  
-ATOM    452  O   LYS A  60      18.491  21.463  -8.203  1.00 20.24           O  
-ATOM    453  CB  LYS A  60      16.030  20.104  -6.504  1.00 20.47           C  
-ATOM    454  CG  LYS A  60      14.860  20.228  -5.540  1.00 25.61           C  
-ATOM    455  CD  LYS A  60      14.061  18.957  -5.422  1.00 27.56           C  
-ATOM    456  CE  LYS A  60      13.254  18.971  -4.131  1.00 37.37           C  
-ATOM    457  NZ  LYS A  60      14.167  19.024  -2.933  1.00 40.85           N  
-ATOM    458  N   ASN A  61      19.214  20.272  -6.460  1.00 19.80           N  
-ATOM    459  CA  ASN A  61      20.459  19.877  -7.107  1.00 25.67           C  
-ATOM    460  C   ASN A  61      21.394  20.993  -7.552  1.00 28.46           C  
-ATOM    461  O   ASN A  61      22.026  20.892  -8.610  1.00 30.29           O  
-ATOM    462  CB  ASN A  61      20.178  18.974  -8.317  1.00 32.71           C  
-ATOM    463  CG  ASN A  61      20.810  17.614  -8.168  1.00 45.62           C  
-ATOM    464  OD1 ASN A  61      21.977  17.408  -8.520  1.00 54.41           O  
-ATOM    465  ND2 ASN A  61      20.063  16.685  -7.589  1.00 51.76           N  
-ATOM    466  N   VAL A  62      21.521  22.018  -6.719  1.00 27.06           N  
-ATOM    467  CA  VAL A  62      22.392  23.151  -6.996  1.00 23.96           C  
-ATOM    468  C   VAL A  62      23.824  22.827  -6.574  1.00 23.00           C  
-ATOM    469  O   VAL A  62      24.065  22.248  -5.506  1.00 22.97           O  
-ATOM    470  CB  VAL A  62      21.879  24.393  -6.238  1.00 22.54           C  
-ATOM    471  CG1 VAL A  62      22.796  25.593  -6.443  1.00 17.13           C  
-ATOM    472  CG2 VAL A  62      20.461  24.685  -6.680  1.00 26.69           C  
-ATOM    473  N   GLU A  63      24.773  23.172  -7.425  1.00 22.31           N  
-ATOM    474  CA  GLU A  63      26.165  22.920  -7.110  1.00 24.98           C  
-ATOM    475  C   GLU A  63      26.687  23.957  -6.097  1.00 23.21           C  
-ATOM    476  O   GLU A  63      26.682  25.153  -6.375  1.00 20.79           O  
-ATOM    477  CB  GLU A  63      27.000  22.950  -8.376  1.00 25.79           C  
-ATOM    478  CG  GLU A  63      28.448  22.767  -8.087  1.00 35.84           C  
-ATOM    479  CD  GLU A  63      29.301  23.147  -9.254  1.00 46.86           C  
-ATOM    480  OE1 GLU A  63      29.065  22.591 -10.346  1.00 51.01           O  
-ATOM    481  OE2 GLU A  63      30.200  23.999  -9.074  1.00 52.48           O  
-ATOM    482  N   ILE A  64      27.241  23.477  -4.983  1.00 23.33           N  
-ATOM    483  CA  ILE A  64      27.718  24.348  -3.903  1.00 21.38           C  
-ATOM    484  C   ILE A  64      29.147  24.044  -3.480  1.00 20.71           C  
-ATOM    485  O   ILE A  64      29.499  22.886  -3.295  1.00 20.06           O  
-ATOM    486  CB  ILE A  64      26.768  24.220  -2.654  1.00 21.90           C  
-ATOM    487  CG1 ILE A  64      25.363  24.682  -3.013  1.00 17.73           C  
-ATOM    488  CG2 ILE A  64      27.292  25.041  -1.475  1.00 19.85           C  
-ATOM    489  CD1 ILE A  64      24.316  23.935  -2.289  1.00 21.82           C  
-ATOM    490  N   GLU A  65      29.963  25.086  -3.358  1.00 18.64           N  
-ATOM    491  CA  GLU A  65      31.328  24.921  -2.923  1.00 18.41           C  
-ATOM    492  C   GLU A  65      31.440  25.678  -1.622  1.00 17.84           C  
-ATOM    493  O   GLU A  65      31.133  26.876  -1.573  1.00 18.44           O  
-ATOM    494  CB  GLU A  65      32.288  25.513  -3.948  1.00 23.11           C  
-ATOM    495  CG  GLU A  65      32.306  24.688  -5.228  1.00 42.40           C  
-ATOM    496  CD  GLU A  65      33.181  25.300  -6.297  1.00 53.74           C  
-ATOM    497  OE1 GLU A  65      32.826  26.402  -6.793  1.00 58.77           O  
-ATOM    498  OE2 GLU A  65      34.213  24.682  -6.646  1.00 55.74           O  
-ATOM    499  N   VAL A  66      31.761  24.987  -0.543  1.00 15.97           N  
-ATOM    500  CA  VAL A  66      31.874  25.642   0.724  1.00 16.05           C  
-ATOM    501  C   VAL A  66      32.859  24.830   1.571  1.00 17.27           C  
-ATOM    502  O   VAL A  66      32.889  23.603   1.489  1.00 15.84           O  
-ATOM    503  CB  VAL A  66      30.512  25.766   1.449  1.00 19.82           C  
-ATOM    504  CG1 VAL A  66      29.878  24.389   1.624  1.00 22.04           C  
-ATOM    505  CG2 VAL A  66      30.654  26.484   2.801  1.00 15.58           C  
-ATOM    506  N   LEU A  67      33.731  25.536   2.303  1.00 15.27           N  
-ATOM    507  CA  LEU A  67      34.734  24.906   3.142  1.00 17.14           C  
-ATOM    508  C   LEU A  67      35.539  23.838   2.409  1.00 16.83           C  
-ATOM    509  O   LEU A  67      35.778  22.789   2.939  1.00 16.18           O  
-ATOM    510  CB  LEU A  67      34.092  24.332   4.428  1.00 15.98           C  
-ATOM    511  CG  LEU A  67      33.691  25.412   5.456  1.00 16.19           C  
-ATOM    512  CD1 LEU A  67      32.700  24.918   6.494  1.00 15.67           C  
-ATOM    513  CD2 LEU A  67      34.932  25.945   6.133  1.00 14.97           C  
-ATOM    514  N   ASN A  68      35.927  24.151   1.181  1.00 17.21           N  
-ATOM    515  CA  ASN A  68      36.686  23.232   0.331  1.00 18.08           C  
-ATOM    516  C   ASN A  68      35.959  21.965  -0.055  1.00 17.15           C  
-ATOM    517  O   ASN A  68      36.590  21.042  -0.532  1.00 19.42           O  
-ATOM    518  CB  ASN A  68      38.029  22.845   0.971  1.00 16.07           C  
-ATOM    519  CG  ASN A  68      38.926  24.029   1.169  1.00 17.25           C  
-ATOM    520  OD1 ASN A  68      38.764  25.063   0.522  1.00 15.60           O  
-ATOM    521  ND2 ASN A  68      39.845  23.915   2.107  1.00 24.64           N  
-ATOM    522  N   LYS A  69      34.659  21.904   0.191  1.00 19.01           N  
-ATOM    523  CA  LYS A  69      33.873  20.735  -0.164  1.00 20.57           C  
-ATOM    524  C   LYS A  69      32.916  21.136  -1.283  1.00 22.34           C  
-ATOM    525  O   LYS A  69      32.495  22.306  -1.346  1.00 23.78           O  
-ATOM    526  CB  LYS A  69      33.053  20.237   1.034  1.00 25.97           C  
-ATOM    527  CG  LYS A  69      33.847  19.642   2.185  1.00 29.75           C  
-ATOM    528  CD  LYS A  69      34.461  18.320   1.787  1.00 41.78           C  
-ATOM    529  CE  LYS A  69      35.226  17.689   2.955  1.00 52.88           C  
-ATOM    530  NZ  LYS A  69      34.337  17.425   4.138  1.00 58.10           N  
-ATOM    531  N   LYS A  70      32.571  20.178  -2.151  1.00 21.45           N  
-ATOM    532  CA  LYS A  70      31.653  20.428  -3.249  1.00 22.21           C  
-ATOM    533  C   LYS A  70      30.463  19.507  -3.084  1.00 21.54           C  
-ATOM    534  O   LYS A  70      30.639  18.300  -3.023  1.00 23.88           O  
-ATOM    535  CB  LYS A  70      32.302  20.149  -4.598  1.00 29.50           C  
-ATOM    536  CG  LYS A  70      31.334  20.357  -5.770  1.00 44.29           C  
-ATOM    537  CD  LYS A  70      31.918  19.916  -7.112  1.00 58.78           C  
-ATOM    538  CE  LYS A  70      33.008  20.862  -7.632  1.00 68.39           C  
-ATOM    539  NZ  LYS A  70      33.415  20.529  -9.045  1.00 74.56           N  
-ATOM    540  N   VAL A  71      29.259  20.070  -3.031  1.00 20.50           N  
-ATOM    541  CA  VAL A  71      28.035  19.292  -2.861  1.00 22.15           C  
-ATOM    542  C   VAL A  71      26.922  19.801  -3.768  1.00 21.23           C  
-ATOM    543  O   VAL A  71      26.986  20.922  -4.269  1.00 20.82           O  
-ATOM    544  CB  VAL A  71      27.517  19.320  -1.370  1.00 22.93           C  
-ATOM    545  CG1 VAL A  71      28.593  18.854  -0.423  1.00 23.31           C  
-ATOM    546  CG2 VAL A  71      27.085  20.703  -0.970  1.00 20.50           C  
-ATOM    547  N   ARG A  72      25.946  18.946  -4.043  1.00 21.04           N  
-ATOM    548  CA  ARG A  72      24.798  19.347  -4.854  1.00 25.43           C  
-ATOM    549  C   ARG A  72      23.697  19.280  -3.808  1.00 23.51           C  
-ATOM    550  O   ARG A  72      23.581  18.265  -3.127  1.00 24.41           O  
-ATOM    551  CB  ARG A  72      24.501  18.333  -5.968  1.00 30.15           C  
-ATOM    552  CG  ARG A  72      25.533  18.277  -7.051  1.00 37.73           C  
-ATOM    553  CD  ARG A  72      24.959  18.711  -8.391  1.00 49.15           C  
-ATOM    554  NE  ARG A  72      26.002  19.277  -9.246  1.00 57.06           N  
-ATOM    555  CZ  ARG A  72      25.778  19.917 -10.389  1.00 62.92           C  
-ATOM    556  NH1 ARG A  72      24.536  20.068 -10.835  1.00 65.51           N  
-ATOM    557  NH2 ARG A  72      26.798  20.456 -11.058  1.00 62.44           N  
-ATOM    558  N   ALA A  73      22.945  20.358  -3.633  1.00 21.95           N  
-ATOM    559  CA  ALA A  73      21.889  20.359  -2.624  1.00 19.94           C  
-ATOM    560  C   ALA A  73      20.778  21.310  -2.989  1.00 14.93           C  
-ATOM    561  O   ALA A  73      20.923  22.107  -3.909  1.00 13.28           O  
-ATOM    562  CB  ALA A  73      22.475  20.741  -1.256  1.00 21.21           C  
-ATOM    563  N   THR A  74      19.637  21.159  -2.329  1.00 14.26           N  
-ATOM    564  CA  THR A  74      18.505  22.042  -2.558  1.00 12.68           C  
-ATOM    565  C   THR A  74      18.745  23.398  -1.897  1.00 15.26           C  
-ATOM    566  O   THR A  74      19.163  23.499  -0.724  1.00 15.99           O  
-ATOM    567  CB  THR A  74      17.225  21.433  -2.021  1.00 13.66           C  
-ATOM    568  OG1 THR A  74      16.962  20.210  -2.726  1.00 20.00           O  
-ATOM    569  CG2 THR A  74      16.029  22.412  -2.232  1.00  9.29           C  
-ATOM    570  N   ILE A  75      18.481  24.449  -2.655  1.00 15.48           N  
-ATOM    571  CA  ILE A  75      18.638  25.818  -2.198  1.00 16.57           C  
-ATOM    572  C   ILE A  75      17.351  26.582  -2.475  1.00 16.72           C  
-ATOM    573  O   ILE A  75      16.709  26.384  -3.507  1.00 21.22           O  
-ATOM    574  CB  ILE A  75      19.811  26.517  -2.964  1.00 19.60           C  
-ATOM    575  CG1 ILE A  75      21.157  25.953  -2.487  1.00 21.27           C  
-ATOM    576  CG2 ILE A  75      19.775  28.040  -2.769  1.00 14.67           C  
-ATOM    577  CD1 ILE A  75      21.492  26.335  -1.042  1.00 27.28           C  
-ATOM    578  N   MET A  76      16.941  27.431  -1.553  1.00 16.90           N  
-ATOM    579  CA  MET A  76      15.757  28.231  -1.792  1.00 17.22           C  
-ATOM    580  C   MET A  76      16.174  29.672  -1.853  1.00 20.18           C  
-ATOM    581  O   MET A  76      17.101  30.082  -1.127  1.00 19.42           O  
-ATOM    582  CB  MET A  76      14.764  28.068  -0.677  1.00 15.13           C  
-ATOM    583  CG  MET A  76      14.424  26.621  -0.441  1.00 33.12           C  
-ATOM    584  SD  MET A  76      13.040  26.427   0.602  1.00 39.97           S  
-ATOM    585  CE  MET A  76      12.604  24.724   0.184  1.00 48.65           C  
-ATOM    586  N   THR A  77      15.537  30.434  -2.738  1.00 18.43           N  
-ATOM    587  CA  THR A  77      15.827  31.848  -2.838  1.00 17.26           C  
-ATOM    588  C   THR A  77      14.607  32.601  -2.348  1.00 17.15           C  
-ATOM    589  O   THR A  77      13.462  32.204  -2.599  1.00 17.24           O  
-ATOM    590  CB  THR A  77      16.203  32.297  -4.255  1.00 17.37           C  
-ATOM    591  OG1 THR A  77      15.111  32.072  -5.157  1.00 25.23           O  
-ATOM    592  CG2 THR A  77      17.465  31.552  -4.743  1.00 17.38           C  
-ATOM    593  N   GLY A  78      14.856  33.665  -1.606  1.00 16.07           N  
-ATOM    594  CA  GLY A  78      13.776  34.448  -1.081  1.00 18.75           C  
-ATOM    595  C   GLY A  78      14.311  35.560  -0.224  1.00 21.12           C  
-ATOM    596  O   GLY A  78      15.511  35.672  -0.016  1.00 21.58           O  
-ATOM    597  N   ASP A  79      13.390  36.344   0.318  1.00 25.72           N  
-ATOM    598  CA  ASP A  79      13.698  37.504   1.122  1.00 28.69           C  
-ATOM    599  C   ASP A  79      14.121  37.179   2.536  1.00 27.36           C  
-ATOM    600  O   ASP A  79      13.324  37.197   3.473  1.00 28.99           O  
-ATOM    601  CB  ASP A  79      12.501  38.449   1.133  1.00 39.42           C  
-ATOM    602  CG  ASP A  79      12.875  39.842   1.590  1.00 54.64           C  
-ATOM    603  OD1 ASP A  79      13.678  40.492   0.874  1.00 60.31           O  
-ATOM    604  OD2 ASP A  79      12.391  40.280   2.666  1.00 67.61           O  
-ATOM    605  N   THR A  80      15.393  36.876   2.680  1.00 24.74           N  
-ATOM    606  CA  THR A  80      15.925  36.568   3.971  1.00 22.27           C  
-ATOM    607  C   THR A  80      16.976  37.644   4.270  1.00 23.08           C  
-ATOM    608  O   THR A  80      17.680  38.125   3.374  1.00 19.81           O  
-ATOM    609  CB  THR A  80      16.511  35.137   4.007  1.00 20.88           C  
-ATOM    610  OG1 THR A  80      17.167  34.932   5.268  1.00 22.92           O  
-ATOM    611  CG2 THR A  80      17.495  34.906   2.850  1.00 19.39           C  
-ATOM    612  N   PRO A  81      17.049  38.073   5.538  1.00 23.73           N  
-ATOM    613  CA  PRO A  81      17.995  39.096   5.988  1.00 20.85           C  
-ATOM    614  C   PRO A  81      19.420  38.575   6.020  1.00 20.31           C  
-ATOM    615  O   PRO A  81      20.376  39.352   5.907  1.00 24.08           O  
-ATOM    616  CB  PRO A  81      17.528  39.389   7.410  1.00 23.45           C  
-ATOM    617  CG  PRO A  81      16.112  38.789   7.496  1.00 28.26           C  
-ATOM    618  CD  PRO A  81      16.216  37.580   6.653  1.00 22.54           C  
-ATOM    619  N   ILE A  82      19.560  37.265   6.184  1.00 17.19           N  
-ATOM    620  CA  ILE A  82      20.860  36.613   6.291  1.00 18.52           C  
-ATOM    621  C   ILE A  82      20.764  35.346   5.466  1.00 17.53           C  
-ATOM    622  O   ILE A  82      19.723  34.695   5.439  1.00 19.32           O  
-ATOM    623  CB  ILE A  82      21.128  36.186   7.812  1.00 22.78           C  
-ATOM    624  CG1 ILE A  82      20.958  37.374   8.740  1.00 26.73           C  
-ATOM    625  CG2 ILE A  82      22.568  35.693   8.044  1.00 21.52           C  
-ATOM    626  CD1 ILE A  82      21.188  37.017  10.162  1.00 42.09           C  
-ATOM    627  N   ASN A  83      21.832  34.991   4.774  1.00 17.76           N  
-ATOM    628  CA  ASN A  83      21.838  33.750   4.009  1.00 14.97           C  
-ATOM    629  C   ASN A  83      22.105  32.595   4.948  1.00 15.70           C  
-ATOM    630  O   ASN A  83      23.100  32.584   5.684  1.00 14.88           O  
-ATOM    631  CB  ASN A  83      22.876  33.811   2.914  1.00 16.14           C  
-ATOM    632  CG  ASN A  83      22.606  34.937   1.941  1.00 17.60           C  
-ATOM    633  OD1 ASN A  83      21.445  35.224   1.618  1.00 13.48           O  
-ATOM    634  ND2 ASN A  83      23.658  35.613   1.513  1.00  9.07           N  
-ATOM    635  N   ILE A  84      21.209  31.621   4.891  1.00 16.70           N  
-ATOM    636  CA  ILE A  84      21.217  30.429   5.727  1.00 15.19           C  
-ATOM    637  C   ILE A  84      21.564  29.129   4.971  1.00 15.44           C  
-ATOM    638  O   ILE A  84      20.995  28.840   3.918  1.00 19.03           O  
-ATOM    639  CB  ILE A  84      19.781  30.181   6.320  1.00 15.30           C  
-ATOM    640  CG1 ILE A  84      19.265  31.382   7.132  1.00 12.48           C  
-ATOM    641  CG2 ILE A  84      19.752  28.942   7.172  1.00 12.58           C  
-ATOM    642  CD1 ILE A  84      20.130  31.723   8.269  1.00 16.52           C  
-ATOM    643  N   PHE A  85      22.453  28.330   5.557  1.00 16.43           N  
-ATOM    644  CA  PHE A  85      22.824  26.987   5.074  1.00 15.18           C  
-ATOM    645  C   PHE A  85      22.369  26.077   6.247  1.00 13.31           C  
-ATOM    646  O   PHE A  85      23.028  26.037   7.299  1.00 13.92           O  
-ATOM    647  CB  PHE A  85      24.340  26.878   4.883  1.00 11.60           C  
-ATOM    648  CG  PHE A  85      24.802  27.039   3.457  1.00 15.70           C  
-ATOM    649  CD1 PHE A  85      24.013  27.681   2.514  1.00  8.70           C  
-ATOM    650  CD2 PHE A  85      26.045  26.531   3.060  1.00 11.06           C  
-ATOM    651  CE1 PHE A  85      24.455  27.810   1.213  1.00 16.98           C  
-ATOM    652  CE2 PHE A  85      26.486  26.665   1.760  1.00 10.97           C  
-ATOM    653  CZ  PHE A  85      25.691  27.303   0.836  1.00  9.90           C  
-ATOM    654  N   GLY A  86      21.211  25.438   6.089  1.00 14.40           N  
-ATOM    655  CA  GLY A  86      20.655  24.587   7.128  1.00 12.11           C  
-ATOM    656  C   GLY A  86      21.196  23.164   7.120  1.00 14.26           C  
-ATOM    657  O   GLY A  86      22.189  22.881   6.450  1.00 15.79           O  
-ATOM    658  N   ARG A  87      20.509  22.244   7.801  1.00 12.69           N  
-ATOM    659  CA  ARG A  87      20.960  20.861   7.910  1.00 12.38           C  
-ATOM    660  C   ARG A  87      21.123  20.048   6.616  1.00 14.77           C  
-ATOM    661  O   ARG A  87      21.967  19.151   6.568  1.00 15.68           O  
-ATOM    662  CB  ARG A  87      20.096  20.103   8.910  1.00  7.39           C  
-ATOM    663  CG  ARG A  87      20.162  20.668  10.315  1.00 12.19           C  
-ATOM    664  CD  ARG A  87      19.387  19.825  11.342  1.00 12.45           C  
-ATOM    665  NE  ARG A  87      17.953  19.840  11.057  1.00 11.36           N  
-ATOM    666  CZ  ARG A  87      17.283  18.842  10.483  1.00 13.50           C  
-ATOM    667  NH1 ARG A  87      17.892  17.719  10.117  1.00 11.35           N  
-ATOM    668  NH2 ARG A  87      15.979  18.962  10.306  1.00 13.91           N  
-ATOM    669  N   ASN A  88      20.349  20.342   5.572  1.00 14.24           N  
-ATOM    670  CA  ASN A  88      20.491  19.586   4.337  1.00 15.73           C  
-ATOM    671  C   ASN A  88      21.898  19.765   3.790  1.00 13.88           C  
-ATOM    672  O   ASN A  88      22.452  18.870   3.177  1.00 13.36           O  
-ATOM    673  CB  ASN A  88      19.448  19.993   3.285  1.00 13.45           C  
-ATOM    674  CG  ASN A  88      19.624  21.407   2.819  1.00 16.88           C  
-ATOM    675  OD1 ASN A  88      19.800  22.299   3.623  1.00 15.65           O  
-ATOM    676  ND2 ASN A  88      19.600  21.616   1.512  1.00 16.00           N  
-ATOM    677  N   ILE A  89      22.511  20.904   4.086  1.00 12.56           N  
-ATOM    678  CA  ILE A  89      23.855  21.152   3.612  1.00 12.42           C  
-ATOM    679  C   ILE A  89      24.902  20.741   4.644  1.00 13.74           C  
-ATOM    680  O   ILE A  89      25.945  20.173   4.285  1.00 16.54           O  
-ATOM    681  CB  ILE A  89      24.036  22.648   3.152  1.00 20.61           C  
-ATOM    682  CG1 ILE A  89      23.291  22.871   1.828  1.00 14.55           C  
-ATOM    683  CG2 ILE A  89      25.529  23.008   2.987  1.00 18.96           C  
-ATOM    684  CD1 ILE A  89      23.470  24.232   1.256  1.00 11.41           C  
-ATOM    685  N   LEU A  90      24.634  21.013   5.920  1.00 12.99           N  
-ATOM    686  CA  LEU A  90      25.564  20.639   6.990  1.00 12.41           C  
-ATOM    687  C   LEU A  90      25.839  19.122   7.051  1.00 14.67           C  
-ATOM    688  O   LEU A  90      26.998  18.716   7.288  1.00 15.32           O  
-ATOM    689  CB  LEU A  90      25.068  21.136   8.349  1.00  8.82           C  
-ATOM    690  CG  LEU A  90      24.868  22.648   8.512  1.00 12.75           C  
-ATOM    691  CD1 LEU A  90      24.445  22.968   9.942  1.00 10.90           C  
-ATOM    692  CD2 LEU A  90      26.133  23.395   8.163  1.00  9.14           C  
-ATOM    693  N   THR A  91      24.801  18.290   6.875  1.00 13.18           N  
-ATOM    694  CA  THR A  91      24.983  16.828   6.888  1.00 15.98           C  
-ATOM    695  C   THR A  91      25.772  16.370   5.661  1.00 17.36           C  
-ATOM    696  O   THR A  91      26.578  15.446   5.748  1.00 19.36           O  
-ATOM    697  CB  THR A  91      23.659  16.041   6.890  1.00 15.88           C  
-ATOM    698  OG1 THR A  91      22.835  16.496   5.812  1.00 21.69           O  
-ATOM    699  CG2 THR A  91      22.952  16.203   8.175  1.00 12.12           C  
-ATOM    700  N   ALA A  92      25.544  17.014   4.519  1.00 16.91           N  
-ATOM    701  CA  ALA A  92      26.270  16.665   3.306  1.00 17.41           C  
-ATOM    702  C   ALA A  92      27.739  16.956   3.532  1.00 16.89           C  
-ATOM    703  O   ALA A  92      28.586  16.231   3.051  1.00 18.20           O  
-ATOM    704  CB  ALA A  92      25.740  17.444   2.081  1.00 11.67           C  
-ATOM    705  N   LEU A  93      28.044  17.990   4.302  1.00 17.81           N  
-ATOM    706  CA  LEU A  93      29.437  18.336   4.558  1.00 16.87           C  
-ATOM    707  C   LEU A  93      30.062  17.385   5.568  1.00 18.32           C  
-ATOM    708  O   LEU A  93      31.270  17.171   5.561  1.00 20.68           O  
-ATOM    709  CB  LEU A  93      29.564  19.779   5.066  1.00 16.90           C  
-ATOM    710  CG  LEU A  93      28.974  20.902   4.204  1.00 22.98           C  
-ATOM    711  CD1 LEU A  93      29.101  22.266   4.902  1.00 15.18           C  
-ATOM    712  CD2 LEU A  93      29.684  20.914   2.848  1.00 23.59           C  
-ATOM    713  N   GLY A  94      29.231  16.774   6.407  1.00 18.43           N  
-ATOM    714  CA  GLY A  94      29.765  15.901   7.440  1.00 15.34           C  
-ATOM    715  C   GLY A  94      30.058  16.755   8.663  1.00 19.00           C  
-ATOM    716  O   GLY A  94      30.943  16.452   9.445  1.00 22.71           O  
-ATOM    717  N   MET A  95      29.287  17.810   8.863  1.00 18.73           N  
-ATOM    718  CA  MET A  95      29.505  18.684  10.001  1.00 17.95           C  
-ATOM    719  C   MET A  95      28.646  18.242  11.198  1.00 19.00           C  
-ATOM    720  O   MET A  95      27.550  17.703  11.026  1.00 22.51           O  
-ATOM    721  CB  MET A  95      29.219  20.125   9.583  1.00 16.42           C  
-ATOM    722  CG  MET A  95      29.653  21.168  10.587  1.00 29.80           C  
-ATOM    723  SD  MET A  95      30.065  22.770   9.879  1.00 33.71           S  
-ATOM    724  CE  MET A  95      29.408  22.608   8.337  1.00 18.24           C  
-ATOM    725  N   SER A  96      29.164  18.378  12.408  1.00 15.30           N  
-ATOM    726  CA  SER A  96      28.390  17.968  13.552  1.00 15.58           C  
-ATOM    727  C   SER A  96      28.445  19.004  14.639  1.00 17.55           C  
-ATOM    728  O   SER A  96      29.261  19.936  14.580  1.00 18.46           O  
-ATOM    729  CB  SER A  96      28.931  16.657  14.105  1.00 18.75           C  
-ATOM    730  OG  SER A  96      30.274  16.812  14.532  1.00 18.51           O  
-ATOM    731  N   LEU A  97      27.540  18.874  15.607  1.00 18.34           N  
-ATOM    732  CA  LEU A  97      27.509  19.777  16.747  1.00 19.88           C  
-ATOM    733  C   LEU A  97      28.009  18.903  17.911  1.00 22.13           C  
-ATOM    734  O   LEU A  97      27.454  17.842  18.175  1.00 22.10           O  
-ATOM    735  CB  LEU A  97      26.095  20.312  16.975  1.00 23.53           C  
-ATOM    736  CG  LEU A  97      25.820  21.384  18.031  1.00 19.17           C  
-ATOM    737  CD1 LEU A  97      26.546  22.676  17.718  1.00 16.66           C  
-ATOM    738  CD2 LEU A  97      24.334  21.613  18.040  1.00 20.21           C  
-ATOM    739  N   ASN A  98      29.075  19.346  18.572  1.00 22.24           N  
-ATOM    740  CA  ASN A  98      29.703  18.582  19.626  1.00 24.95           C  
-ATOM    741  C   ASN A  98      29.644  19.185  21.009  1.00 27.12           C  
-ATOM    742  O   ASN A  98      29.816  20.394  21.178  1.00 26.95           O  
-ATOM    743  CB  ASN A  98      31.152  18.312  19.226  1.00 24.84           C  
-ATOM    744  CG  ASN A  98      31.254  17.684  17.846  1.00 32.49           C  
-ATOM    745  OD1 ASN A  98      30.878  16.538  17.645  1.00 42.14           O  
-ATOM    746  ND2 ASN A  98      31.690  18.461  16.877  1.00 40.27           N  
-ATOM    747  N   LEU A  99      29.370  18.325  21.990  1.00 30.94           N  
-ATOM    748  CA  LEU A  99      29.295  18.705  23.398  1.00 35.08           C  
-ATOM    749  C   LEU A  99      30.408  17.920  24.066  1.00 35.22           C  
-ATOM    750  O   LEU A  99      31.148  18.512  24.865  1.00 39.69           O  
-ATOM    751  CB  LEU A  99      27.951  18.282  24.021  1.00 39.08           C  
-ATOM    752  CG  LEU A  99      27.386  19.086  25.211  1.00 40.71           C  
-ATOM    753  CD1 LEU A  99      26.403  18.224  25.943  1.00 40.87           C  
-ATOM    754  CD2 LEU A  99      28.454  19.589  26.176  1.00 40.12           C  
-ATOM    755  OXT LEU A  99      30.523  16.716  23.771  1.00 37.94           O  
-TER     756      LEU A  99                                                      
-ATOM    757  N   PRO B   1      29.360  14.314  23.693  1.00 33.72           N  
-ATOM    758  CA  PRO B   1      28.497  13.539  22.745  1.00 32.41           C  
-ATOM    759  C   PRO B   1      28.229  14.409  21.531  1.00 29.94           C  
-ATOM    760  O   PRO B   1      28.333  15.631  21.635  1.00 28.31           O  
-ATOM    761  CB  PRO B   1      27.193  13.199  23.466  1.00 31.04           C  
-ATOM    762  CG  PRO B   1      27.044  14.349  24.393  1.00 31.55           C  
-ATOM    763  CD  PRO B   1      28.473  14.511  24.903  1.00 34.52           C  
-ATOM    764  N   GLN B   2      27.897  13.808  20.392  1.00 25.44           N  
-ATOM    765  CA  GLN B   2      27.644  14.639  19.226  1.00 24.35           C  
-ATOM    766  C   GLN B   2      26.287  14.501  18.555  1.00 21.89           C  
-ATOM    767  O   GLN B   2      25.615  13.499  18.716  1.00 23.69           O  
-ATOM    768  CB  GLN B   2      28.767  14.491  18.194  1.00 26.75           C  
-ATOM    769  CG  GLN B   2      28.744  13.231  17.398  1.00 36.65           C  
-ATOM    770  CD  GLN B   2      29.844  13.193  16.353  1.00 42.25           C  
-ATOM    771  OE1 GLN B   2      31.023  13.420  16.663  1.00 40.48           O  
-ATOM    772  NE2 GLN B   2      29.472  12.862  15.113  1.00 38.73           N  
-ATOM    773  N   PHE B   3      25.898  15.556  17.842  1.00 20.52           N  
-ATOM    774  CA  PHE B   3      24.652  15.646  17.093  1.00 20.09           C  
-ATOM    775  C   PHE B   3      25.101  15.638  15.631  1.00 20.39           C  
-ATOM    776  O   PHE B   3      25.779  16.571  15.180  1.00 19.28           O  
-ATOM    777  CB  PHE B   3      23.925  16.967  17.411  1.00 20.55           C  
-ATOM    778  CG  PHE B   3      23.404  17.058  18.829  1.00 26.38           C  
-ATOM    779  CD1 PHE B   3      24.221  17.508  19.863  1.00 19.25           C  
-ATOM    780  CD2 PHE B   3      22.102  16.653  19.134  1.00 23.73           C  
-ATOM    781  CE1 PHE B   3      23.754  17.543  21.182  1.00 19.08           C  
-ATOM    782  CE2 PHE B   3      21.630  16.682  20.438  1.00 21.66           C  
-ATOM    783  CZ  PHE B   3      22.457  17.124  21.466  1.00 21.72           C  
-ATOM    784  N   SER B   4      24.724  14.598  14.897  1.00 19.42           N  
-ATOM    785  CA  SER B   4      25.126  14.453  13.489  1.00 21.67           C  
-ATOM    786  C   SER B   4      24.275  15.271  12.479  1.00 19.94           C  
-ATOM    787  O   SER B   4      24.561  15.319  11.272  1.00 20.45           O  
-ATOM    788  CB  SER B   4      25.128  12.974  13.123  1.00 17.37           C  
-ATOM    789  OG  SER B   4      23.825  12.460  13.296  1.00 30.30           O  
-ATOM    790  N   LEU B   5      23.208  15.880  12.993  1.00 18.91           N  
-ATOM    791  CA  LEU B   5      22.323  16.730  12.204  1.00 16.06           C  
-ATOM    792  C   LEU B   5      21.416  16.075  11.158  1.00 18.07           C  
-ATOM    793  O   LEU B   5      20.719  16.777  10.433  1.00 18.67           O  
-ATOM    794  CB  LEU B   5      23.101  17.920  11.624  1.00 13.91           C  
-ATOM    795  CG  LEU B   5      23.992  18.678  12.630  1.00 13.01           C  
-ATOM    796  CD1 LEU B   5      24.718  19.798  11.946  1.00 10.79           C  
-ATOM    797  CD2 LEU B   5      23.171  19.207  13.787  1.00  4.07           C  
-ATOM    798  N   TRP B   6      21.411  14.746  11.060  1.00 20.20           N  
-ATOM    799  CA  TRP B   6      20.468  14.080  10.138  1.00 20.37           C  
-ATOM    800  C   TRP B   6      19.042  14.370  10.645  1.00 20.68           C  
-ATOM    801  O   TRP B   6      18.106  14.415   9.869  1.00 25.60           O  
-ATOM    802  CB  TRP B   6      20.714  12.573  10.081  1.00 19.85           C  
-ATOM    803  CG  TRP B   6      22.055  12.223   9.527  1.00 21.39           C  
-ATOM    804  CD1 TRP B   6      23.139  11.727  10.216  1.00 21.92           C  
-ATOM    805  CD2 TRP B   6      22.465  12.340   8.155  1.00 29.27           C  
-ATOM    806  NE1 TRP B   6      24.199  11.525   9.354  1.00 27.95           N  
-ATOM    807  CE2 TRP B   6      23.815  11.892   8.085  1.00 29.88           C  
-ATOM    808  CE3 TRP B   6      21.827  12.779   6.974  1.00 21.88           C  
-ATOM    809  CZ2 TRP B   6      24.534  11.869   6.876  1.00 21.35           C  
-ATOM    810  CZ3 TRP B   6      22.548  12.755   5.771  1.00 22.83           C  
-ATOM    811  CH2 TRP B   6      23.888  12.302   5.737  1.00 24.09           C  
-ATOM    812  N   LYS B   7      18.899  14.597  11.950  1.00 19.76           N  
-ATOM    813  CA  LYS B   7      17.623  14.950  12.579  1.00 20.02           C  
-ATOM    814  C   LYS B   7      17.852  16.296  13.278  1.00 18.43           C  
-ATOM    815  O   LYS B   7      18.994  16.628  13.600  1.00 19.61           O  
-ATOM    816  CB  LYS B   7      17.292  13.982  13.714  1.00 24.43           C  
-ATOM    817  CG  LYS B   7      17.171  12.538  13.378  1.00 39.71           C  
-ATOM    818  CD  LYS B   7      17.213  11.734  14.686  1.00 51.26           C  
-ATOM    819  CE  LYS B   7      16.900  10.256  14.440  1.00 60.81           C  
-ATOM    820  NZ  LYS B   7      15.533  10.062  13.831  1.00 63.97           N  
-ATOM    821  N   ARG B   8      16.779  17.022  13.589  1.00 15.76           N  
-ATOM    822  CA  ARG B   8      16.897  18.275  14.329  1.00 11.19           C  
-ATOM    823  C   ARG B   8      17.594  17.968  15.674  1.00 12.95           C  
-ATOM    824  O   ARG B   8      17.244  16.982  16.336  1.00 11.07           O  
-ATOM    825  CB  ARG B   8      15.519  18.833  14.642  1.00 10.49           C  
-ATOM    826  CG  ARG B   8      14.773  19.346  13.441  1.00 16.57           C  
-ATOM    827  CD  ARG B   8      13.506  20.054  13.839  1.00 14.54           C  
-ATOM    828  NE  ARG B   8      12.820  20.625  12.684  1.00 20.44           N  
-ATOM    829  CZ  ARG B   8      11.599  21.153  12.706  1.00 24.77           C  
-ATOM    830  NH1 ARG B   8      10.900  21.178  13.830  1.00 22.23           N  
-ATOM    831  NH2 ARG B   8      11.109  21.748  11.623  1.00 22.51           N  
-ATOM    832  N   PRO B   9      18.626  18.759  16.058  1.00 10.20           N  
-ATOM    833  CA  PRO B   9      19.332  18.527  17.320  1.00 11.84           C  
-ATOM    834  C   PRO B   9      18.473  18.994  18.522  1.00 16.71           C  
-ATOM    835  O   PRO B   9      18.575  20.144  19.001  1.00 15.02           O  
-ATOM    836  CB  PRO B   9      20.624  19.330  17.145  1.00 11.63           C  
-ATOM    837  CG  PRO B   9      20.199  20.491  16.304  1.00  6.25           C  
-ATOM    838  CD  PRO B   9      19.252  19.859  15.290  1.00  7.23           C  
-ATOM    839  N   VAL B  10      17.561  18.109  18.928  1.00 16.47           N  
-ATOM    840  CA  VAL B  10      16.637  18.388  20.016  1.00 18.51           C  
-ATOM    841  C   VAL B  10      16.992  17.628  21.291  1.00 21.56           C  
-ATOM    842  O   VAL B  10      17.368  16.458  21.227  1.00 26.24           O  
-ATOM    843  CB  VAL B  10      15.196  18.033  19.628  1.00 15.52           C  
-ATOM    844  CG1 VAL B  10      14.292  18.195  20.830  1.00 22.62           C  
-ATOM    845  CG2 VAL B  10      14.706  18.929  18.537  1.00  7.12           C  
-ATOM    846  N   VAL B  11      16.876  18.296  22.432  1.00 20.46           N  
-ATOM    847  CA  VAL B  11      17.162  17.690  23.729  1.00 19.91           C  
-ATOM    848  C   VAL B  11      16.113  18.154  24.736  1.00 18.13           C  
-ATOM    849  O   VAL B  11      15.320  19.046  24.461  1.00 18.63           O  
-ATOM    850  CB  VAL B  11      18.598  18.074  24.290  1.00 21.10           C  
-ATOM    851  CG1 VAL B  11      19.685  17.547  23.406  1.00 23.75           C  
-ATOM    852  CG2 VAL B  11      18.759  19.592  24.435  1.00 23.49           C  
-ATOM    853  N   THR B  12      16.083  17.500  25.879  1.00 19.70           N  
-ATOM    854  CA  THR B  12      15.188  17.877  26.942  1.00 22.82           C  
-ATOM    855  C   THR B  12      15.999  18.709  27.902  1.00 23.16           C  
-ATOM    856  O   THR B  12      16.978  18.228  28.435  1.00 26.29           O  
-ATOM    857  CB  THR B  12      14.699  16.661  27.689  1.00 26.79           C  
-ATOM    858  OG1 THR B  12      13.842  15.905  26.822  1.00 31.79           O  
-ATOM    859  CG2 THR B  12      13.954  17.067  28.983  1.00 31.25           C  
-ATOM    860  N   ALA B  13      15.632  19.967  28.101  1.00 24.02           N  
-ATOM    861  CA  ALA B  13      16.367  20.827  29.033  1.00 25.54           C  
-ATOM    862  C   ALA B  13      15.489  21.138  30.236  1.00 23.62           C  
-ATOM    863  O   ALA B  13      14.268  21.110  30.132  1.00 24.25           O  
-ATOM    864  CB  ALA B  13      16.794  22.127  28.334  1.00 19.87           C  
-ATOM    865  N   TYR B  14      16.098  21.350  31.397  1.00 24.35           N  
-ATOM    866  CA  TYR B  14      15.317  21.722  32.577  1.00 24.37           C  
-ATOM    867  C   TYR B  14      15.598  23.197  32.829  1.00 22.42           C  
-ATOM    868  O   TYR B  14      16.753  23.599  32.984  1.00 25.04           O  
-ATOM    869  CB  TYR B  14      15.704  20.884  33.795  1.00 26.61           C  
-ATOM    870  CG  TYR B  14      15.478  19.424  33.552  1.00 31.72           C  
-ATOM    871  CD1 TYR B  14      16.431  18.673  32.865  1.00 34.12           C  
-ATOM    872  CD2 TYR B  14      14.259  18.827  33.870  1.00 33.98           C  
-ATOM    873  CE1 TYR B  14      16.178  17.377  32.479  1.00 38.50           C  
-ATOM    874  CE2 TYR B  14      13.987  17.524  33.497  1.00 38.41           C  
-ATOM    875  CZ  TYR B  14      14.953  16.800  32.790  1.00 43.80           C  
-ATOM    876  OH  TYR B  14      14.700  15.510  32.358  1.00 50.57           O  
-ATOM    877  N   ILE B  15      14.558  24.007  32.773  1.00 17.26           N  
-ATOM    878  CA  ILE B  15      14.688  25.426  32.995  1.00 19.90           C  
-ATOM    879  C   ILE B  15      14.023  25.724  34.323  1.00 22.65           C  
-ATOM    880  O   ILE B  15      12.809  25.597  34.450  1.00 22.82           O  
-ATOM    881  CB  ILE B  15      14.028  26.179  31.849  1.00 19.43           C  
-ATOM    882  CG1 ILE B  15      14.794  25.848  30.558  1.00 19.78           C  
-ATOM    883  CG2 ILE B  15      13.990  27.645  32.144  1.00 17.70           C  
-ATOM    884  CD1 ILE B  15      14.217  26.428  29.357  1.00 25.21           C  
-ATOM    885  N   GLU B  16      14.842  26.055  35.325  1.00 25.52           N  
-ATOM    886  CA  GLU B  16      14.378  26.323  36.686  1.00 24.97           C  
-ATOM    887  C   GLU B  16      13.557  25.121  37.117  1.00 25.44           C  
-ATOM    888  O   GLU B  16      12.432  25.261  37.596  1.00 26.54           O  
-ATOM    889  CB  GLU B  16      13.534  27.603  36.746  1.00 25.41           C  
-ATOM    890  CG  GLU B  16      14.332  28.899  36.546  1.00 24.63           C  
-ATOM    891  CD  GLU B  16      15.365  29.132  37.636  1.00 28.49           C  
-ATOM    892  OE1 GLU B  16      15.231  28.550  38.727  1.00 36.59           O  
-ATOM    893  OE2 GLU B  16      16.315  29.907  37.425  1.00 33.93           O  
-ATOM    894  N   GLY B  17      14.051  23.943  36.766  1.00 23.79           N  
-ATOM    895  CA  GLY B  17      13.367  22.718  37.134  1.00 28.71           C  
-ATOM    896  C   GLY B  17      12.313  22.097  36.223  1.00 29.81           C  
-ATOM    897  O   GLY B  17      11.971  20.935  36.422  1.00 31.96           O  
-ATOM    898  N   GLN B  18      11.764  22.864  35.280  1.00 31.05           N  
-ATOM    899  CA  GLN B  18      10.752  22.375  34.333  1.00 31.31           C  
-ATOM    900  C   GLN B  18      11.384  21.740  33.078  1.00 28.77           C  
-ATOM    901  O   GLN B  18      12.260  22.340  32.475  1.00 26.30           O  
-ATOM    902  CB  GLN B  18       9.890  23.550  33.858  1.00 36.82           C  
-ATOM    903  CG  GLN B  18       8.799  24.003  34.805  1.00 52.93           C  
-ATOM    904  CD  GLN B  18       7.814  24.945  34.118  1.00 61.71           C  
-ATOM    905  OE1 GLN B  18       6.693  24.554  33.775  1.00 68.59           O  
-ATOM    906  NE2 GLN B  18       8.224  26.189  33.923  1.00 59.57           N  
-ATOM    907  N   PRO B  19      10.971  20.517  32.692  1.00 28.40           N  
-ATOM    908  CA  PRO B  19      11.527  19.867  31.495  1.00 28.16           C  
-ATOM    909  C   PRO B  19      10.881  20.484  30.260  1.00 27.39           C  
-ATOM    910  O   PRO B  19       9.683  20.720  30.245  1.00 27.46           O  
-ATOM    911  CB  PRO B  19      11.091  18.410  31.664  1.00 31.36           C  
-ATOM    912  CG  PRO B  19       9.760  18.537  32.338  1.00 29.97           C  
-ATOM    913  CD  PRO B  19      10.074  19.590  33.404  1.00 32.61           C  
-ATOM    914  N   VAL B  20      11.677  20.773  29.236  1.00 30.03           N  
-ATOM    915  CA  VAL B  20      11.178  21.387  28.000  1.00 28.04           C  
-ATOM    916  C   VAL B  20      12.040  20.867  26.833  1.00 26.11           C  
-ATOM    917  O   VAL B  20      13.233  20.596  27.014  1.00 23.55           O  
-ATOM    918  CB  VAL B  20      11.241  22.953  28.118  1.00 25.44           C  
-ATOM    919  CG1 VAL B  20      12.652  23.420  28.226  1.00 32.80           C  
-ATOM    920  CG2 VAL B  20      10.598  23.611  26.955  1.00 29.23           C  
-ATOM    921  N   GLU B  21      11.437  20.624  25.672  1.00 25.16           N  
-ATOM    922  CA  GLU B  21      12.230  20.156  24.533  1.00 24.27           C  
-ATOM    923  C   GLU B  21      12.714  21.429  23.861  1.00 23.22           C  
-ATOM    924  O   GLU B  21      11.936  22.382  23.680  1.00 22.50           O  
-ATOM    925  CB  GLU B  21      11.412  19.331  23.536  1.00 28.76           C  
-ATOM    926  CG  GLU B  21      10.631  18.167  24.137  1.00 48.98           C  
-ATOM    927  CD  GLU B  21      11.497  17.223  24.946  1.00 59.46           C  
-ATOM    928  OE1 GLU B  21      12.649  16.977  24.523  1.00 66.86           O  
-ATOM    929  OE2 GLU B  21      11.027  16.733  26.003  1.00 60.78           O  
-ATOM    930  N   VAL B  22      14.005  21.477  23.559  1.00 18.75           N  
-ATOM    931  CA  VAL B  22      14.585  22.646  22.918  1.00 17.33           C  
-ATOM    932  C   VAL B  22      15.449  22.238  21.715  1.00 17.74           C  
-ATOM    933  O   VAL B  22      16.089  21.176  21.721  1.00 17.69           O  
-ATOM    934  CB  VAL B  22      15.460  23.504  23.929  1.00 14.93           C  
-ATOM    935  CG1 VAL B  22      14.623  23.960  25.103  1.00 13.83           C  
-ATOM    936  CG2 VAL B  22      16.681  22.720  24.419  1.00 11.97           C  
-ATOM    937  N   LEU B  23      15.479  23.112  20.715  1.00 15.46           N  
-ATOM    938  CA  LEU B  23      16.258  22.934  19.505  1.00 13.31           C  
-ATOM    939  C   LEU B  23      17.616  23.653  19.685  1.00 13.55           C  
-ATOM    940  O   LEU B  23      17.630  24.844  19.993  1.00 13.77           O  
-ATOM    941  CB  LEU B  23      15.482  23.580  18.341  1.00 13.41           C  
-ATOM    942  CG  LEU B  23      16.135  23.739  16.957  1.00 11.57           C  
-ATOM    943  CD1 LEU B  23      16.550  22.384  16.422  1.00  8.70           C  
-ATOM    944  CD2 LEU B  23      15.180  24.411  16.002  1.00  9.18           C  
-ATOM    945  N   LEU B  24      18.739  22.941  19.535  1.00 14.86           N  
-ATOM    946  CA  LEU B  24      20.094  23.548  19.640  1.00 14.04           C  
-ATOM    947  C   LEU B  24      20.325  24.323  18.325  1.00 14.69           C  
-ATOM    948  O   LEU B  24      20.438  23.749  17.227  1.00 14.88           O  
-ATOM    949  CB  LEU B  24      21.148  22.471  19.882  1.00 13.61           C  
-ATOM    950  CG  LEU B  24      20.851  21.620  21.132  1.00 20.52           C  
-ATOM    951  CD1 LEU B  24      22.013  20.689  21.405  1.00 21.06           C  
-ATOM    952  CD2 LEU B  24      20.610  22.512  22.373  1.00 10.74           C  
-ATOM    953  N   ASP B  25      20.461  25.632  18.451  1.00 11.65           N  
-ATOM    954  CA  ASP B  25      20.492  26.453  17.272  1.00 11.50           C  
-ATOM    955  C   ASP B  25      21.639  27.445  17.096  1.00 13.28           C  
-ATOM    956  O   ASP B  25      21.599  28.580  17.620  1.00 15.31           O  
-ATOM    957  CB  ASP B  25      19.133  27.157  17.294  1.00 14.48           C  
-ATOM    958  CG  ASP B  25      18.860  27.991  16.078  1.00 18.62           C  
-ATOM    959  OD1 ASP B  25      19.684  28.052  15.156  1.00 25.46           O  
-ATOM    960  OD2 ASP B  25      17.787  28.613  16.067  1.00 20.90           O  
-ATOM    961  N   THR B  26      22.606  27.062  16.266  1.00 11.47           N  
-ATOM    962  CA  THR B  26      23.757  27.918  15.953  1.00 10.03           C  
-ATOM    963  C   THR B  26      23.365  29.155  15.120  1.00 11.97           C  
-ATOM    964  O   THR B  26      24.142  30.126  15.033  1.00 11.23           O  
-ATOM    965  CB  THR B  26      24.848  27.134  15.195  1.00 18.81           C  
-ATOM    966  OG1 THR B  26      24.326  26.645  13.935  1.00 12.27           O  
-ATOM    967  CG2 THR B  26      25.352  25.968  16.073  1.00  8.41           C  
-ATOM    968  N   GLY B  27      22.170  29.134  14.519  1.00 10.28           N  
-ATOM    969  CA  GLY B  27      21.717  30.272  13.725  1.00  8.95           C  
-ATOM    970  C   GLY B  27      20.953  31.257  14.580  1.00 12.36           C  
-ATOM    971  O   GLY B  27      20.397  32.227  14.058  1.00 11.49           O  
-ATOM    972  N   ALA B  28      20.929  31.021  15.893  1.00 11.71           N  
-ATOM    973  CA  ALA B  28      20.210  31.911  16.796  1.00 11.28           C  
-ATOM    974  C   ALA B  28      21.138  32.659  17.755  1.00 13.24           C  
-ATOM    975  O   ALA B  28      22.024  32.061  18.369  1.00 13.25           O  
-ATOM    976  CB  ALA B  28      19.178  31.114  17.583  1.00 11.32           C  
-ATOM    977  N   ASP B  29      20.951  33.965  17.892  1.00 13.35           N  
-ATOM    978  CA  ASP B  29      21.803  34.724  18.812  1.00 15.34           C  
-ATOM    979  C   ASP B  29      21.342  34.542  20.252  1.00 15.36           C  
-ATOM    980  O   ASP B  29      22.158  34.451  21.170  1.00 16.72           O  
-ATOM    981  CB  ASP B  29      21.756  36.213  18.490  1.00 13.72           C  
-ATOM    982  CG  ASP B  29      22.320  36.553  17.114  1.00 16.23           C  
-ATOM    983  OD1 ASP B  29      23.169  35.818  16.559  1.00 19.93           O  
-ATOM    984  OD2 ASP B  29      21.931  37.609  16.603  1.00 20.89           O  
-ATOM    985  N   ASP B  30      20.022  34.463  20.422  1.00 14.94           N  
-ATOM    986  CA  ASP B  30      19.353  34.345  21.731  1.00 15.54           C  
-ATOM    987  C   ASP B  30      18.607  33.030  21.863  1.00 13.81           C  
-ATOM    988  O   ASP B  30      18.435  32.300  20.893  1.00 11.76           O  
-ATOM    989  CB  ASP B  30      18.299  35.458  21.872  1.00 19.84           C  
-ATOM    990  CG  ASP B  30      18.845  36.817  21.519  1.00 25.03           C  
-ATOM    991  OD1 ASP B  30      19.840  37.237  22.143  1.00 31.63           O  
-ATOM    992  OD2 ASP B  30      18.304  37.444  20.596  1.00 26.71           O  
-ATOM    993  N   SER B  31      18.072  32.822  23.048  1.00 11.02           N  
-ATOM    994  CA  SER B  31      17.314  31.637  23.381  1.00 13.74           C  
-ATOM    995  C   SER B  31      15.867  32.077  23.663  1.00 14.01           C  
-ATOM    996  O   SER B  31      15.621  33.057  24.354  1.00 15.45           O  
-ATOM    997  CB  SER B  31      17.953  30.952  24.603  1.00 10.74           C  
-ATOM    998  OG  SER B  31      19.320  30.681  24.342  1.00 11.82           O  
-ATOM    999  N   ILE B  32      14.912  31.372  23.092  1.00 14.26           N  
-ATOM   1000  CA  ILE B  32      13.526  31.737  23.263  1.00 16.30           C  
-ATOM   1001  C   ILE B  32      12.731  30.477  23.564  1.00 16.08           C  
-ATOM   1002  O   ILE B  32      12.744  29.530  22.793  1.00 18.33           O  
-ATOM   1003  CB  ILE B  32      12.988  32.418  21.990  1.00 19.09           C  
-ATOM   1004  CG1 ILE B  32      13.962  33.505  21.559  1.00 22.35           C  
-ATOM   1005  CG2 ILE B  32      11.593  33.025  22.234  1.00  9.81           C  
-ATOM   1006  CD1 ILE B  32      13.506  34.257  20.357  1.00 30.18           C  
-ATOM   1007  N   VAL B  33      12.010  30.511  24.679  1.00 17.94           N  
-ATOM   1008  CA  VAL B  33      11.204  29.405  25.162  1.00 18.84           C  
-ATOM   1009  C   VAL B  33       9.755  29.868  25.346  1.00 20.94           C  
-ATOM   1010  O   VAL B  33       9.487  31.051  25.581  1.00 23.75           O  
-ATOM   1011  CB  VAL B  33      11.814  28.871  26.499  1.00 19.43           C  
-ATOM   1012  CG1 VAL B  33      10.953  27.826  27.116  1.00 26.07           C  
-ATOM   1013  CG2 VAL B  33      13.151  28.235  26.211  1.00 23.40           C  
-ATOM   1014  N   ALA B  34       8.806  28.969  25.158  1.00 20.80           N  
-ATOM   1015  CA  ALA B  34       7.418  29.337  25.339  1.00 20.37           C  
-ATOM   1016  C   ALA B  34       6.889  28.550  26.513  1.00 22.87           C  
-ATOM   1017  O   ALA B  34       7.445  27.516  26.867  1.00 22.79           O  
-ATOM   1018  CB  ALA B  34       6.638  29.012  24.093  1.00 14.68           C  
-ATOM   1019  N   GLY B  35       5.852  29.068  27.160  1.00 26.27           N  
-ATOM   1020  CA  GLY B  35       5.231  28.351  28.271  1.00 29.28           C  
-ATOM   1021  C   GLY B  35       5.941  28.187  29.602  1.00 30.61           C  
-ATOM   1022  O   GLY B  35       5.793  27.162  30.272  1.00 32.53           O  
-ATOM   1023  N   ILE B  36       6.687  29.200  30.002  1.00 30.13           N  
-ATOM   1024  CA  ILE B  36       7.419  29.176  31.259  1.00 31.35           C  
-ATOM   1025  C   ILE B  36       7.057  30.527  31.851  1.00 30.44           C  
-ATOM   1026  O   ILE B  36       7.136  31.545  31.160  1.00 30.92           O  
-ATOM   1027  CB  ILE B  36       8.958  29.105  31.003  1.00 34.95           C  
-ATOM   1028  CG1 ILE B  36       9.299  27.841  30.221  1.00 41.84           C  
-ATOM   1029  CG2 ILE B  36       9.725  29.048  32.312  1.00 34.53           C  
-ATOM   1030  CD1 ILE B  36       8.957  26.549  30.932  1.00 45.07           C  
-ATOM   1031  N   GLU B  37       6.593  30.550  33.089  1.00 29.13           N  
-ATOM   1032  CA  GLU B  37       6.225  31.813  33.703  1.00 26.83           C  
-ATOM   1033  C   GLU B  37       7.289  32.117  34.707  1.00 24.81           C  
-ATOM   1034  O   GLU B  37       7.341  31.489  35.746  1.00 25.39           O  
-ATOM   1035  CB  GLU B  37       4.869  31.690  34.362  1.00 30.91           C  
-ATOM   1036  CG  GLU B  37       3.736  31.556  33.363  1.00 37.81           C  
-ATOM   1037  CD  GLU B  37       2.384  31.501  34.035  1.00 51.59           C  
-ATOM   1038  OE1 GLU B  37       2.287  30.922  35.153  1.00 53.28           O  
-ATOM   1039  OE2 GLU B  37       1.417  32.039  33.442  1.00 57.66           O  
-ATOM   1040  N   LEU B  38       8.157  33.070  34.385  1.00 23.61           N  
-ATOM   1041  CA  LEU B  38       9.267  33.405  35.273  1.00 18.01           C  
-ATOM   1042  C   LEU B  38       9.095  34.685  36.105  1.00 17.13           C  
-ATOM   1043  O   LEU B  38      10.030  35.098  36.791  1.00 14.22           O  
-ATOM   1044  CB  LEU B  38      10.583  33.453  34.469  1.00 17.38           C  
-ATOM   1045  CG  LEU B  38      11.059  32.159  33.806  1.00 20.23           C  
-ATOM   1046  CD1 LEU B  38      12.131  32.462  32.786  1.00 17.45           C  
-ATOM   1047  CD2 LEU B  38      11.592  31.163  34.855  1.00 16.62           C  
-ATOM   1048  N   GLY B  39       7.915  35.298  36.066  1.00 13.94           N  
-ATOM   1049  CA  GLY B  39       7.731  36.494  36.851  1.00 15.82           C  
-ATOM   1050  C   GLY B  39       7.824  37.802  36.063  1.00 16.18           C  
-ATOM   1051  O   GLY B  39       8.026  37.809  34.852  1.00 14.91           O  
-ATOM   1052  N   ASN B  40       7.749  38.921  36.772  1.00 14.65           N  
-ATOM   1053  CA  ASN B  40       7.746  40.196  36.098  1.00 15.68           C  
-ATOM   1054  C   ASN B  40       9.068  40.953  36.036  1.00 15.89           C  
-ATOM   1055  O   ASN B  40       9.087  42.092  35.580  1.00 16.29           O  
-ATOM   1056  CB  ASN B  40       6.617  41.089  36.637  1.00 13.60           C  
-ATOM   1057  CG  ASN B  40       6.843  41.519  38.089  1.00 24.59           C  
-ATOM   1058  OD1 ASN B  40       7.960  41.468  38.617  1.00 24.78           O  
-ATOM   1059  ND2 ASN B  40       5.771  41.932  38.743  1.00 27.96           N  
-ATOM   1060  N   ASN B  41      10.174  40.330  36.429  1.00 14.87           N  
-ATOM   1061  CA  ASN B  41      11.439  41.040  36.345  1.00 14.16           C  
-ATOM   1062  C   ASN B  41      12.147  40.700  35.048  1.00 13.68           C  
-ATOM   1063  O   ASN B  41      13.145  39.995  35.045  1.00 14.62           O  
-ATOM   1064  CB  ASN B  41      12.361  40.715  37.526  1.00 17.27           C  
-ATOM   1065  CG  ASN B  41      13.617  41.597  37.555  1.00 23.02           C  
-ATOM   1066  OD1 ASN B  41      14.626  41.252  38.163  1.00 29.21           O  
-ATOM   1067  ND2 ASN B  41      13.538  42.753  36.939  1.00 21.99           N  
-ATOM   1068  N   TYR B  42      11.706  41.287  33.953  1.00 14.17           N  
-ATOM   1069  CA  TYR B  42      12.303  41.007  32.649  1.00 14.22           C  
-ATOM   1070  C   TYR B  42      12.481  42.289  31.895  1.00 13.60           C  
-ATOM   1071  O   TYR B  42      11.955  43.321  32.286  1.00 13.45           O  
-ATOM   1072  CB  TYR B  42      11.356  40.122  31.838  1.00  7.84           C  
-ATOM   1073  CG  TYR B  42       9.989  40.742  31.617  1.00 11.58           C  
-ATOM   1074  CD1 TYR B  42       9.757  41.602  30.529  1.00 16.87           C  
-ATOM   1075  CD2 TYR B  42       8.932  40.491  32.496  1.00 11.47           C  
-ATOM   1076  CE1 TYR B  42       8.508  42.197  30.323  1.00 13.84           C  
-ATOM   1077  CE2 TYR B  42       7.684  41.075  32.306  1.00 13.15           C  
-ATOM   1078  CZ  TYR B  42       7.475  41.930  31.216  1.00 19.94           C  
-ATOM   1079  OH  TYR B  42       6.233  42.519  31.024  1.00 18.22           O  
-ATOM   1080  N   SER B  43      13.174  42.220  30.773  1.00 15.69           N  
-ATOM   1081  CA  SER B  43      13.308  43.413  29.964  1.00 17.58           C  
-ATOM   1082  C   SER B  43      12.575  43.101  28.673  1.00 17.61           C  
-ATOM   1083  O   SER B  43      12.743  42.014  28.098  1.00 17.05           O  
-ATOM   1084  CB  SER B  43      14.771  43.745  29.647  1.00 24.31           C  
-ATOM   1085  OG  SER B  43      15.571  43.825  30.815  1.00 35.66           O  
-ATOM   1086  N   PRO B  44      11.718  44.017  28.224  1.00 16.37           N  
-ATOM   1087  CA  PRO B  44      10.973  43.808  26.978  1.00 16.28           C  
-ATOM   1088  C   PRO B  44      11.969  43.885  25.805  1.00 19.05           C  
-ATOM   1089  O   PRO B  44      12.860  44.728  25.808  1.00 18.90           O  
-ATOM   1090  CB  PRO B  44      10.010  44.988  26.970  1.00 16.56           C  
-ATOM   1091  CG  PRO B  44       9.876  45.353  28.465  1.00 19.32           C  
-ATOM   1092  CD  PRO B  44      11.286  45.240  28.917  1.00 11.73           C  
-ATOM   1093  N   LYS B  45      11.872  42.966  24.852  1.00 20.45           N  
-ATOM   1094  CA  LYS B  45      12.774  42.963  23.701  1.00 19.53           C  
-ATOM   1095  C   LYS B  45      11.954  42.607  22.483  1.00 20.66           C  
-ATOM   1096  O   LYS B  45      10.803  42.199  22.588  1.00 19.37           O  
-ATOM   1097  CB  LYS B  45      13.845  41.870  23.845  1.00 17.37           C  
-ATOM   1098  CG  LYS B  45      14.830  42.056  24.960  1.00 23.67           C  
-ATOM   1099  CD  LYS B  45      15.802  43.160  24.630  1.00 33.13           C  
-ATOM   1100  CE  LYS B  45      17.140  42.956  25.334  1.00 38.61           C  
-ATOM   1101  NZ  LYS B  45      17.036  43.287  26.771  1.00 50.57           N  
-ATOM   1102  N   ILE B  46      12.569  42.745  21.323  1.00 21.68           N  
-ATOM   1103  CA  ILE B  46      11.950  42.362  20.072  1.00 22.80           C  
-ATOM   1104  C   ILE B  46      13.007  41.497  19.399  1.00 24.49           C  
-ATOM   1105  O   ILE B  46      14.199  41.774  19.493  1.00 27.08           O  
-ATOM   1106  CB  ILE B  46      11.575  43.586  19.222  1.00 25.64           C  
-ATOM   1107  CG1 ILE B  46      10.271  44.176  19.764  1.00 29.09           C  
-ATOM   1108  CG2 ILE B  46      11.384  43.190  17.766  1.00 28.89           C  
-ATOM   1109  CD1 ILE B  46       9.775  45.375  19.023  1.00 38.96           C  
-ATOM   1110  N   VAL B  47      12.595  40.377  18.836  1.00 24.86           N  
-ATOM   1111  CA  VAL B  47      13.543  39.517  18.169  1.00 22.69           C  
-ATOM   1112  C   VAL B  47      12.997  39.271  16.772  1.00 22.91           C  
-ATOM   1113  O   VAL B  47      11.786  39.165  16.585  1.00 21.61           O  
-ATOM   1114  CB  VAL B  47      13.742  38.189  18.963  1.00 26.54           C  
-ATOM   1115  CG1 VAL B  47      14.534  37.175  18.144  1.00 26.43           C  
-ATOM   1116  CG2 VAL B  47      14.504  38.487  20.269  1.00 27.91           C  
-ATOM   1117  N   GLY B  48      13.888  39.295  15.784  1.00 22.08           N  
-ATOM   1118  CA  GLY B  48      13.482  39.050  14.416  1.00 19.71           C  
-ATOM   1119  C   GLY B  48      14.097  37.779  13.866  1.00 20.92           C  
-ATOM   1120  O   GLY B  48      15.144  37.316  14.333  1.00 18.03           O  
-ATOM   1121  N   GLY B  49      13.371  37.158  12.947  1.00 20.00           N  
-ATOM   1122  CA  GLY B  49      13.842  35.957  12.283  1.00 21.11           C  
-ATOM   1123  C   GLY B  49      13.273  35.975  10.870  1.00 20.15           C  
-ATOM   1124  O   GLY B  49      13.052  37.030  10.283  1.00 18.14           O  
-ATOM   1125  N   ILE B  50      13.061  34.804  10.309  1.00 21.70           N  
-ATOM   1126  CA  ILE B  50      12.465  34.674   8.981  1.00 25.14           C  
-ATOM   1127  C   ILE B  50      11.015  35.093   9.243  1.00 26.53           C  
-ATOM   1128  O   ILE B  50      10.499  34.866  10.346  1.00 30.90           O  
-ATOM   1129  CB  ILE B  50      12.516  33.166   8.541  1.00 22.91           C  
-ATOM   1130  CG1 ILE B  50      13.894  32.812   7.989  1.00 23.32           C  
-ATOM   1131  CG2 ILE B  50      11.359  32.789   7.638  1.00 27.59           C  
-ATOM   1132  CD1 ILE B  50      14.293  33.539   6.771  1.00 14.77           C  
-ATOM   1133  N   GLY B  51      10.394  35.794   8.309  1.00 25.84           N  
-ATOM   1134  CA  GLY B  51       9.005  36.174   8.500  1.00 23.63           C  
-ATOM   1135  C   GLY B  51       8.687  37.394   9.336  1.00 23.26           C  
-ATOM   1136  O   GLY B  51       7.558  37.841   9.319  1.00 25.67           O  
-ATOM   1137  N   GLY B  52       9.635  37.926  10.094  1.00 25.23           N  
-ATOM   1138  CA  GLY B  52       9.323  39.100  10.903  1.00 25.46           C  
-ATOM   1139  C   GLY B  52       9.861  39.145  12.330  1.00 26.22           C  
-ATOM   1140  O   GLY B  52      10.829  38.464  12.671  1.00 27.43           O  
-ATOM   1141  N   PHE B  53       9.159  39.887  13.182  1.00 27.19           N  
-ATOM   1142  CA  PHE B  53       9.540  40.113  14.581  1.00 25.69           C  
-ATOM   1143  C   PHE B  53       8.514  39.654  15.600  1.00 24.96           C  
-ATOM   1144  O   PHE B  53       7.331  39.568  15.297  1.00 26.87           O  
-ATOM   1145  CB  PHE B  53       9.792  41.620  14.818  1.00 28.28           C  
-ATOM   1146  CG  PHE B  53      10.998  42.151  14.096  1.00 31.16           C  
-ATOM   1147  CD1 PHE B  53      10.917  42.507  12.745  1.00 35.41           C  
-ATOM   1148  CD2 PHE B  53      12.229  42.218  14.736  1.00 28.50           C  
-ATOM   1149  CE1 PHE B  53      12.051  42.907  12.046  1.00 34.96           C  
-ATOM   1150  CE2 PHE B  53      13.371  42.617  14.051  1.00 31.38           C  
-ATOM   1151  CZ  PHE B  53      13.282  42.961  12.699  1.00 33.02           C  
-ATOM   1152  N   ILE B  54       8.979  39.365  16.811  1.00 20.85           N  
-ATOM   1153  CA  ILE B  54       8.103  38.979  17.902  1.00 18.11           C  
-ATOM   1154  C   ILE B  54       8.588  39.690  19.169  1.00 19.33           C  
-ATOM   1155  O   ILE B  54       9.761  40.102  19.267  1.00 21.41           O  
-ATOM   1156  CB  ILE B  54       8.050  37.448  18.146  1.00 19.40           C  
-ATOM   1157  CG1 ILE B  54       9.427  36.886  18.523  1.00  8.86           C  
-ATOM   1158  CG2 ILE B  54       7.464  36.715  16.897  1.00 20.52           C  
-ATOM   1159  CD1 ILE B  54       9.324  35.504  19.151  1.00 12.20           C  
-ATOM   1160  N   ASN B  55       7.664  39.925  20.091  1.00 16.66           N  
-ATOM   1161  CA  ASN B  55       7.996  40.562  21.346  1.00 17.08           C  
-ATOM   1162  C   ASN B  55       8.384  39.473  22.303  1.00 17.80           C  
-ATOM   1163  O   ASN B  55       7.749  38.401  22.345  1.00 20.52           O  
-ATOM   1164  CB  ASN B  55       6.803  41.319  21.885  1.00 20.33           C  
-ATOM   1165  CG  ASN B  55       6.477  42.507  21.039  1.00 24.41           C  
-ATOM   1166  OD1 ASN B  55       7.260  43.442  20.936  1.00 33.90           O  
-ATOM   1167  ND2 ASN B  55       5.368  42.437  20.351  1.00 35.59           N  
-ATOM   1168  N   THR B  56       9.437  39.709  23.055  1.00 13.66           N  
-ATOM   1169  CA  THR B  56       9.886  38.712  23.997  1.00 16.09           C  
-ATOM   1170  C   THR B  56      10.111  39.396  25.341  1.00 16.05           C  
-ATOM   1171  O   THR B  56      10.122  40.634  25.426  1.00 16.49           O  
-ATOM   1172  CB  THR B  56      11.211  38.111  23.530  1.00 14.83           C  
-ATOM   1173  OG1 THR B  56      12.189  39.159  23.515  1.00 19.22           O  
-ATOM   1174  CG2 THR B  56      11.078  37.491  22.104  1.00  6.26           C  
-ATOM   1175  N   LYS B  57      10.289  38.575  26.373  1.00 15.33           N  
-ATOM   1176  CA  LYS B  57      10.556  39.021  27.726  1.00 13.93           C  
-ATOM   1177  C   LYS B  57      11.855  38.336  28.096  1.00 13.44           C  
-ATOM   1178  O   LYS B  57      11.918  37.118  28.107  1.00 12.45           O  
-ATOM   1179  CB  LYS B  57       9.463  38.564  28.681  1.00 15.86           C  
-ATOM   1180  CG  LYS B  57       8.102  39.163  28.370  1.00 13.62           C  
-ATOM   1181  CD  LYS B  57       7.057  38.611  29.303  1.00 17.14           C  
-ATOM   1182  CE  LYS B  57       5.691  39.215  29.010  1.00 22.32           C  
-ATOM   1183  NZ  LYS B  57       4.730  38.733  30.023  1.00 32.73           N  
-ATOM   1184  N   GLU B  58      12.897  39.127  28.354  1.00 12.52           N  
-ATOM   1185  CA  GLU B  58      14.202  38.596  28.700  1.00 11.32           C  
-ATOM   1186  C   GLU B  58      14.481  38.533  30.196  1.00 10.39           C  
-ATOM   1187  O   GLU B  58      14.331  39.531  30.904  1.00  9.72           O  
-ATOM   1188  CB  GLU B  58      15.274  39.424  28.005  1.00 10.81           C  
-ATOM   1189  CG  GLU B  58      16.699  39.177  28.481  1.00 20.70           C  
-ATOM   1190  CD  GLU B  58      17.656  40.225  27.951  1.00 27.32           C  
-ATOM   1191  OE1 GLU B  58      17.830  41.263  28.622  1.00 33.76           O  
-ATOM   1192  OE2 GLU B  58      18.212  40.023  26.854  1.00 32.21           O  
-ATOM   1193  N   TYR B  59      14.905  37.358  30.654  1.00 10.56           N  
-ATOM   1194  CA  TYR B  59      15.265  37.118  32.038  1.00  9.96           C  
-ATOM   1195  C   TYR B  59      16.748  36.751  32.076  1.00 13.52           C  
-ATOM   1196  O   TYR B  59      17.241  36.016  31.210  1.00 12.69           O  
-ATOM   1197  CB  TYR B  59      14.472  35.937  32.599  1.00 12.83           C  
-ATOM   1198  CG  TYR B  59      12.980  36.148  32.578  1.00 16.51           C  
-ATOM   1199  CD1 TYR B  59      12.247  35.897  31.406  1.00 19.25           C  
-ATOM   1200  CD2 TYR B  59      12.302  36.622  33.703  1.00 11.52           C  
-ATOM   1201  CE1 TYR B  59      10.866  36.119  31.345  1.00 18.15           C  
-ATOM   1202  CE2 TYR B  59      10.905  36.844  33.654  1.00 16.24           C  
-ATOM   1203  CZ  TYR B  59      10.203  36.590  32.469  1.00 15.89           C  
-ATOM   1204  OH  TYR B  59       8.852  36.806  32.393  1.00 12.36           O  
-ATOM   1205  N   LYS B  60      17.445  37.250  33.095  1.00 13.84           N  
-ATOM   1206  CA  LYS B  60      18.861  36.980  33.289  1.00 15.29           C  
-ATOM   1207  C   LYS B  60      19.028  35.943  34.394  1.00 12.01           C  
-ATOM   1208  O   LYS B  60      18.143  35.777  35.216  1.00 12.58           O  
-ATOM   1209  CB  LYS B  60      19.555  38.252  33.761  1.00 19.87           C  
-ATOM   1210  CG  LYS B  60      19.414  39.409  32.838  1.00 30.71           C  
-ATOM   1211  CD  LYS B  60      20.719  39.655  32.105  1.00 39.76           C  
-ATOM   1212  CE  LYS B  60      20.636  40.946  31.302  1.00 39.36           C  
-ATOM   1213  NZ  LYS B  60      21.850  41.120  30.467  1.00 53.15           N  
-ATOM   1214  N   ASN B  61      20.127  35.204  34.355  1.00 12.46           N  
-ATOM   1215  CA  ASN B  61      20.470  34.246  35.411  1.00 13.93           C  
-ATOM   1216  C   ASN B  61      19.499  33.128  35.643  1.00 15.53           C  
-ATOM   1217  O   ASN B  61      19.243  32.729  36.788  1.00 17.45           O  
-ATOM   1218  CB  ASN B  61      20.715  34.979  36.747  1.00 14.94           C  
-ATOM   1219  CG  ASN B  61      21.889  35.937  36.683  1.00 20.28           C  
-ATOM   1220  OD1 ASN B  61      22.932  35.615  36.116  1.00 23.17           O  
-ATOM   1221  ND2 ASN B  61      21.719  37.128  37.238  1.00 27.20           N  
-ATOM   1222  N   VAL B  62      18.937  32.612  34.573  1.00 15.66           N  
-ATOM   1223  CA  VAL B  62      17.996  31.525  34.694  1.00 15.33           C  
-ATOM   1224  C   VAL B  62      18.768  30.202  34.754  1.00 16.24           C  
-ATOM   1225  O   VAL B  62      19.751  30.024  34.032  1.00 15.96           O  
-ATOM   1226  CB  VAL B  62      17.036  31.548  33.503  1.00 15.08           C  
-ATOM   1227  CG1 VAL B  62      16.063  30.380  33.604  1.00 17.16           C  
-ATOM   1228  CG2 VAL B  62      16.261  32.872  33.491  1.00  9.15           C  
-ATOM   1229  N   GLU B  63      18.328  29.280  35.615  1.00 17.81           N  
-ATOM   1230  CA  GLU B  63      18.988  27.987  35.758  1.00 19.81           C  
-ATOM   1231  C   GLU B  63      18.604  27.052  34.626  1.00 21.07           C  
-ATOM   1232  O   GLU B  63      17.426  26.751  34.433  1.00 21.35           O  
-ATOM   1233  CB  GLU B  63      18.615  27.315  37.069  1.00 24.56           C  
-ATOM   1234  CG  GLU B  63      19.198  25.907  37.212  1.00 37.49           C  
-ATOM   1235  CD  GLU B  63      18.450  25.028  38.220  1.00 50.13           C  
-ATOM   1236  OE1 GLU B  63      17.201  25.108  38.316  1.00 56.24           O  
-ATOM   1237  OE2 GLU B  63      19.120  24.239  38.922  1.00 58.45           O  
-ATOM   1238  N   ILE B  64      19.606  26.557  33.910  1.00 23.08           N  
-ATOM   1239  CA  ILE B  64      19.387  25.641  32.808  1.00 22.88           C  
-ATOM   1240  C   ILE B  64      20.271  24.412  32.970  1.00 24.84           C  
-ATOM   1241  O   ILE B  64      21.475  24.518  33.249  1.00 20.87           O  
-ATOM   1242  CB  ILE B  64      19.692  26.311  31.431  1.00 22.16           C  
-ATOM   1243  CG1 ILE B  64      18.644  27.381  31.134  1.00 23.87           C  
-ATOM   1244  CG2 ILE B  64      19.693  25.265  30.310  1.00 17.49           C  
-ATOM   1245  CD1 ILE B  64      19.227  28.754  30.858  1.00 31.90           C  
-ATOM   1246  N   GLU B  65      19.639  23.247  32.836  1.00 27.33           N  
-ATOM   1247  CA  GLU B  65      20.327  21.957  32.891  1.00 27.41           C  
-ATOM   1248  C   GLU B  65      20.075  21.193  31.580  1.00 25.13           C  
-ATOM   1249  O   GLU B  65      18.921  21.004  31.167  1.00 23.84           O  
-ATOM   1250  CB  GLU B  65      19.836  21.124  34.056  1.00 28.02           C  
-ATOM   1251  CG  GLU B  65      20.685  19.893  34.240  1.00 42.49           C  
-ATOM   1252  CD  GLU B  65      20.268  19.079  35.434  1.00 54.34           C  
-ATOM   1253  OE1 GLU B  65      19.763  19.669  36.414  1.00 58.80           O  
-ATOM   1254  OE2 GLU B  65      20.444  17.846  35.392  1.00 64.93           O  
-ATOM   1255  N   VAL B  66      21.162  20.799  30.917  1.00 23.71           N  
-ATOM   1256  CA  VAL B  66      21.086  20.067  29.662  1.00 23.50           C  
-ATOM   1257  C   VAL B  66      22.087  18.955  29.740  1.00 23.08           C  
-ATOM   1258  O   VAL B  66      23.287  19.200  29.900  1.00 20.76           O  
-ATOM   1259  CB  VAL B  66      21.448  20.951  28.430  1.00 27.04           C  
-ATOM   1260  CG1 VAL B  66      21.339  20.145  27.154  1.00 27.07           C  
-ATOM   1261  CG2 VAL B  66      20.527  22.167  28.350  1.00 27.49           C  
-ATOM   1262  N   LEU B  67      21.595  17.729  29.581  1.00 24.53           N  
-ATOM   1263  CA  LEU B  67      22.431  16.531  29.635  1.00 27.80           C  
-ATOM   1264  C   LEU B  67      23.417  16.623  30.812  1.00 29.10           C  
-ATOM   1265  O   LEU B  67      24.641  16.544  30.657  1.00 29.51           O  
-ATOM   1266  CB  LEU B  67      23.154  16.282  28.293  1.00 29.17           C  
-ATOM   1267  CG  LEU B  67      22.268  15.822  27.123  1.00 26.67           C  
-ATOM   1268  CD1 LEU B  67      23.085  15.869  25.813  1.00 23.29           C  
-ATOM   1269  CD2 LEU B  67      21.646  14.453  27.362  1.00 18.28           C  
-ATOM   1270  N   ASN B  68      22.860  16.883  31.985  1.00 31.72           N  
-ATOM   1271  CA  ASN B  68      23.651  16.976  33.195  1.00 36.29           C  
-ATOM   1272  C   ASN B  68      24.672  18.099  33.279  1.00 34.97           C  
-ATOM   1273  O   ASN B  68      25.695  17.947  33.943  1.00 37.37           O  
-ATOM   1274  CB  ASN B  68      24.335  15.637  33.494  1.00 43.64           C  
-ATOM   1275  CG  ASN B  68      23.819  15.007  34.756  1.00 51.51           C  
-ATOM   1276  OD1 ASN B  68      22.820  14.288  34.736  1.00 58.71           O  
-ATOM   1277  ND2 ASN B  68      24.468  15.306  35.879  1.00 61.46           N  
-ATOM   1278  N   LYS B  69      24.461  19.185  32.554  1.00 32.49           N  
-ATOM   1279  CA  LYS B  69      25.357  20.329  32.669  1.00 33.06           C  
-ATOM   1280  C   LYS B  69      24.444  21.408  33.205  1.00 31.38           C  
-ATOM   1281  O   LYS B  69      23.261  21.427  32.868  1.00 34.01           O  
-ATOM   1282  CB  LYS B  69      25.935  20.733  31.315  1.00 37.19           C  
-ATOM   1283  CG  LYS B  69      26.789  19.658  30.685  1.00 50.64           C  
-ATOM   1284  CD  LYS B  69      28.167  19.581  31.321  1.00 59.07           C  
-ATOM   1285  CE  LYS B  69      29.071  20.661  30.769  1.00 63.47           C  
-ATOM   1286  NZ  LYS B  69      29.434  20.378  29.343  1.00 70.63           N  
-ATOM   1287  N   LYS B  70      24.937  22.222  34.126  1.00 30.83           N  
-ATOM   1288  CA  LYS B  70      24.122  23.298  34.679  1.00 30.15           C  
-ATOM   1289  C   LYS B  70      24.779  24.640  34.500  1.00 28.15           C  
-ATOM   1290  O   LYS B  70      25.885  24.839  34.974  1.00 31.37           O  
-ATOM   1291  CB  LYS B  70      23.862  23.105  36.174  1.00 32.80           C  
-ATOM   1292  CG  LYS B  70      22.547  22.444  36.510  1.00 41.42           C  
-ATOM   1293  CD  LYS B  70      22.422  22.294  38.015  1.00 54.39           C  
-ATOM   1294  CE  LYS B  70      21.147  21.556  38.424  1.00 61.64           C  
-ATOM   1295  NZ  LYS B  70      20.969  21.435  39.915  1.00 62.77           N  
-ATOM   1296  N   VAL B  71      24.078  25.563  33.850  1.00 26.14           N  
-ATOM   1297  CA  VAL B  71      24.570  26.924  33.645  1.00 22.33           C  
-ATOM   1298  C   VAL B  71      23.434  27.880  34.019  1.00 21.79           C  
-ATOM   1299  O   VAL B  71      22.299  27.438  34.240  1.00 21.50           O  
-ATOM   1300  CB  VAL B  71      24.967  27.183  32.156  1.00 20.18           C  
-ATOM   1301  CG1 VAL B  71      26.154  26.327  31.758  1.00 20.52           C  
-ATOM   1302  CG2 VAL B  71      23.779  26.922  31.232  1.00  7.61           C  
-ATOM   1303  N   ARG B  72      23.761  29.154  34.177  1.00 20.19           N  
-ATOM   1304  CA  ARG B  72      22.786  30.211  34.448  1.00 21.96           C  
-ATOM   1305  C   ARG B  72      22.955  31.054  33.197  1.00 20.29           C  
-ATOM   1306  O   ARG B  72      24.079  31.375  32.807  1.00 21.00           O  
-ATOM   1307  CB  ARG B  72      23.211  31.033  35.656  1.00 20.71           C  
-ATOM   1308  CG  ARG B  72      22.973  30.340  36.984  1.00 30.41           C  
-ATOM   1309  CD  ARG B  72      21.754  30.893  37.682  1.00 39.13           C  
-ATOM   1310  NE  ARG B  72      21.317  29.936  38.689  1.00 35.58           N  
-ATOM   1311  CZ  ARG B  72      20.120  29.914  39.274  1.00 36.21           C  
-ATOM   1312  NH1 ARG B  72      19.166  30.820  39.005  1.00 33.72           N  
-ATOM   1313  NH2 ARG B  72      19.846  28.896  40.084  1.00 41.08           N  
-ATOM   1314  N   ALA B  73      21.862  31.378  32.531  1.00 18.96           N  
-ATOM   1315  CA  ALA B  73      21.992  32.131  31.293  1.00 19.15           C  
-ATOM   1316  C   ALA B  73      20.792  33.017  31.072  1.00 17.91           C  
-ATOM   1317  O   ALA B  73      19.825  32.960  31.837  1.00 17.93           O  
-ATOM   1318  CB  ALA B  73      22.148  31.145  30.134  1.00 19.18           C  
-ATOM   1319  N   THR B  74      20.880  33.860  30.048  1.00 16.94           N  
-ATOM   1320  CA  THR B  74      19.792  34.744  29.686  1.00 16.48           C  
-ATOM   1321  C   THR B  74      18.831  33.940  28.842  1.00 16.91           C  
-ATOM   1322  O   THR B  74      19.244  33.147  28.006  1.00 15.97           O  
-ATOM   1323  CB  THR B  74      20.307  35.963  28.955  1.00 18.59           C  
-ATOM   1324  OG1 THR B  74      21.272  36.595  29.804  1.00 20.09           O  
-ATOM   1325  CG2 THR B  74      19.157  36.934  28.625  1.00 12.84           C  
-ATOM   1326  N   ILE B  75      17.544  34.132  29.067  1.00 18.16           N  
-ATOM   1327  CA  ILE B  75      16.525  33.371  28.340  1.00 19.26           C  
-ATOM   1328  C   ILE B  75      15.363  34.322  28.049  1.00 18.71           C  
-ATOM   1329  O   ILE B  75      15.116  35.252  28.819  1.00 19.37           O  
-ATOM   1330  CB  ILE B  75      16.059  32.178  29.244  1.00 19.06           C  
-ATOM   1331  CG1 ILE B  75      16.555  30.848  28.688  1.00 24.11           C  
-ATOM   1332  CG2 ILE B  75      14.555  32.141  29.385  1.00 16.72           C  
-ATOM   1333  CD1 ILE B  75      15.557  30.216  27.708  1.00 22.30           C  
-ATOM   1334  N   MET B  76      14.685  34.130  26.924  1.00 16.04           N  
-ATOM   1335  CA  MET B  76      13.549  34.978  26.598  1.00 13.61           C  
-ATOM   1336  C   MET B  76      12.332  34.091  26.463  1.00 16.15           C  
-ATOM   1337  O   MET B  76      12.463  32.882  26.172  1.00 15.61           O  
-ATOM   1338  CB  MET B  76      13.764  35.688  25.268  1.00 12.68           C  
-ATOM   1339  CG  MET B  76      14.858  36.707  25.271  1.00 16.88           C  
-ATOM   1340  SD  MET B  76      15.007  37.409  23.625  1.00 23.60           S  
-ATOM   1341  CE  MET B  76      16.112  38.720  23.954  1.00 24.85           C  
-ATOM   1342  N   THR B  77      11.175  34.633  26.820  1.00 13.33           N  
-ATOM   1343  CA  THR B  77       9.937  33.899  26.623  1.00 13.92           C  
-ATOM   1344  C   THR B  77       9.176  34.703  25.561  1.00 13.69           C  
-ATOM   1345  O   THR B  77       9.330  35.932  25.438  1.00 13.95           O  
-ATOM   1346  CB  THR B  77       9.098  33.706  27.906  1.00 11.90           C  
-ATOM   1347  OG1 THR B  77       8.600  34.967  28.384  1.00 15.85           O  
-ATOM   1348  CG2 THR B  77       9.929  33.035  28.966  1.00  7.47           C  
-ATOM   1349  N   GLY B  78       8.426  33.998  24.735  1.00 15.61           N  
-ATOM   1350  CA  GLY B  78       7.669  34.643  23.684  1.00 14.15           C  
-ATOM   1351  C   GLY B  78       6.947  33.557  22.933  1.00 15.70           C  
-ATOM   1352  O   GLY B  78       7.195  32.348  23.130  1.00 17.68           O  
-ATOM   1353  N   ASP B  79       6.037  33.974  22.080  1.00 15.45           N  
-ATOM   1354  CA  ASP B  79       5.263  33.037  21.311  1.00 14.93           C  
-ATOM   1355  C   ASP B  79       6.121  32.435  20.198  1.00 15.54           C  
-ATOM   1356  O   ASP B  79       6.183  32.961  19.114  1.00 19.13           O  
-ATOM   1357  CB  ASP B  79       4.046  33.764  20.737  1.00 14.46           C  
-ATOM   1358  CG  ASP B  79       3.140  32.847  19.935  1.00 21.99           C  
-ATOM   1359  OD1 ASP B  79       3.347  31.617  19.958  1.00 24.27           O  
-ATOM   1360  OD2 ASP B  79       2.217  33.360  19.272  1.00 20.29           O  
-ATOM   1361  N   THR B  80       6.782  31.322  20.468  1.00 16.68           N  
-ATOM   1362  CA  THR B  80       7.599  30.687  19.464  1.00 16.86           C  
-ATOM   1363  C   THR B  80       7.039  29.295  19.221  1.00 22.31           C  
-ATOM   1364  O   THR B  80       6.596  28.625  20.157  1.00 20.93           O  
-ATOM   1365  CB  THR B  80       9.087  30.602  19.904  1.00 19.74           C  
-ATOM   1366  OG1 THR B  80       9.841  29.902  18.907  1.00 25.16           O  
-ATOM   1367  CG2 THR B  80       9.229  29.877  21.241  1.00 11.83           C  
-ATOM   1368  N   PRO B  81       7.060  28.830  17.959  1.00 24.03           N  
-ATOM   1369  CA  PRO B  81       6.545  27.499  17.624  1.00 23.13           C  
-ATOM   1370  C   PRO B  81       7.446  26.425  18.203  1.00 26.27           C  
-ATOM   1371  O   PRO B  81       6.977  25.359  18.611  1.00 30.65           O  
-ATOM   1372  CB  PRO B  81       6.608  27.479  16.106  1.00 24.04           C  
-ATOM   1373  CG  PRO B  81       6.706  28.941  15.703  1.00 29.95           C  
-ATOM   1374  CD  PRO B  81       7.562  29.520  16.761  1.00 26.28           C  
-ATOM   1375  N   ILE B  82       8.743  26.710  18.276  1.00 25.48           N  
-ATOM   1376  CA  ILE B  82       9.692  25.743  18.820  1.00 22.12           C  
-ATOM   1377  C   ILE B  82      10.580  26.464  19.828  1.00 18.52           C  
-ATOM   1378  O   ILE B  82      10.871  27.637  19.642  1.00 18.07           O  
-ATOM   1379  CB  ILE B  82      10.597  25.140  17.677  1.00 25.19           C  
-ATOM   1380  CG1 ILE B  82       9.743  24.577  16.543  1.00 30.37           C  
-ATOM   1381  CG2 ILE B  82      11.395  23.964  18.194  1.00 26.88           C  
-ATOM   1382  CD1 ILE B  82      10.549  23.921  15.428  1.00 41.92           C  
-ATOM   1383  N   ASN B  83      10.939  25.802  20.928  1.00 15.97           N  
-ATOM   1384  CA  ASN B  83      11.851  26.407  21.907  1.00 15.88           C  
-ATOM   1385  C   ASN B  83      13.290  26.327  21.335  1.00 15.30           C  
-ATOM   1386  O   ASN B  83      13.731  25.292  20.829  1.00 16.92           O  
-ATOM   1387  CB  ASN B  83      11.765  25.681  23.247  1.00 16.68           C  
-ATOM   1388  CG  ASN B  83      10.363  25.603  23.760  1.00 20.56           C  
-ATOM   1389  OD1 ASN B  83       9.631  26.592  23.733  1.00 18.19           O  
-ATOM   1390  ND2 ASN B  83       9.943  24.409  24.171  1.00 16.63           N  
-ATOM   1391  N   ILE B  84      14.029  27.412  21.453  1.00 14.22           N  
-ATOM   1392  CA  ILE B  84      15.365  27.505  20.889  1.00 15.29           C  
-ATOM   1393  C   ILE B  84      16.445  27.870  21.920  1.00 14.25           C  
-ATOM   1394  O   ILE B  84      16.253  28.797  22.716  1.00 13.25           O  
-ATOM   1395  CB  ILE B  84      15.407  28.682  19.793  1.00 22.41           C  
-ATOM   1396  CG1 ILE B  84      14.434  28.421  18.642  1.00 20.64           C  
-ATOM   1397  CG2 ILE B  84      16.836  28.947  19.277  1.00 16.47           C  
-ATOM   1398  CD1 ILE B  84      14.788  27.187  17.901  1.00 36.00           C  
-ATOM   1399  N   PHE B  85      17.564  27.146  21.890  1.00 11.23           N  
-ATOM   1400  CA  PHE B  85      18.727  27.480  22.700  1.00 10.49           C  
-ATOM   1401  C   PHE B  85      19.691  27.958  21.647  1.00 11.49           C  
-ATOM   1402  O   PHE B  85      20.126  27.164  20.795  1.00 11.37           O  
-ATOM   1403  CB  PHE B  85      19.316  26.291  23.436  1.00  6.71           C  
-ATOM   1404  CG  PHE B  85      18.676  26.047  24.773  1.00 12.14           C  
-ATOM   1405  CD1 PHE B  85      17.541  26.793  25.167  1.00 14.35           C  
-ATOM   1406  CD2 PHE B  85      19.190  25.083  25.634  1.00 15.06           C  
-ATOM   1407  CE1 PHE B  85      16.931  26.584  26.403  1.00 18.00           C  
-ATOM   1408  CE2 PHE B  85      18.591  24.848  26.889  1.00 21.22           C  
-ATOM   1409  CZ  PHE B  85      17.456  25.602  27.276  1.00 20.84           C  
-ATOM   1410  N   GLY B  86      19.947  29.265  21.667  1.00  9.91           N  
-ATOM   1411  CA  GLY B  86      20.836  29.890  20.711  1.00  9.00           C  
-ATOM   1412  C   GLY B  86      22.264  29.924  21.217  1.00  9.70           C  
-ATOM   1413  O   GLY B  86      22.565  29.346  22.278  1.00  7.17           O  
-ATOM   1414  N   ARG B  87      23.133  30.629  20.489  1.00  8.91           N  
-ATOM   1415  CA  ARG B  87      24.561  30.698  20.807  1.00 13.33           C  
-ATOM   1416  C   ARG B  87      24.965  31.122  22.230  1.00 14.85           C  
-ATOM   1417  O   ARG B  87      25.967  30.626  22.755  1.00 16.22           O  
-ATOM   1418  CB  ARG B  87      25.315  31.525  19.765  1.00  9.71           C  
-ATOM   1419  CG  ARG B  87      25.360  30.925  18.332  1.00  9.38           C  
-ATOM   1420  CD  ARG B  87      26.244  31.821  17.426  1.00 14.93           C  
-ATOM   1421  NE  ARG B  87      25.722  33.186  17.313  1.00  8.89           N  
-ATOM   1422  CZ  ARG B  87      26.228  34.272  17.906  1.00 13.23           C  
-ATOM   1423  NH1 ARG B  87      27.311  34.218  18.686  1.00 10.31           N  
-ATOM   1424  NH2 ARG B  87      25.594  35.420  17.767  1.00  8.27           N  
-ATOM   1425  N   ASN B  88      24.164  31.957  22.889  1.00 14.84           N  
-ATOM   1426  CA  ASN B  88      24.519  32.367  24.256  1.00 17.63           C  
-ATOM   1427  C   ASN B  88      24.544  31.163  25.211  1.00 18.43           C  
-ATOM   1428  O   ASN B  88      25.397  31.072  26.085  1.00 21.22           O  
-ATOM   1429  CB  ASN B  88      23.598  33.468  24.781  1.00 13.83           C  
-ATOM   1430  CG  ASN B  88      22.205  32.968  25.063  1.00 17.78           C  
-ATOM   1431  OD1 ASN B  88      21.565  32.356  24.208  1.00 15.51           O  
-ATOM   1432  ND2 ASN B  88      21.736  33.203  26.271  1.00 14.09           N  
-ATOM   1433  N   ILE B  89      23.654  30.206  25.001  1.00 18.69           N  
-ATOM   1434  CA  ILE B  89      23.635  29.019  25.836  1.00 16.67           C  
-ATOM   1435  C   ILE B  89      24.587  27.948  25.295  1.00 16.34           C  
-ATOM   1436  O   ILE B  89      25.221  27.227  26.063  1.00 17.29           O  
-ATOM   1437  CB  ILE B  89      22.206  28.455  25.987  1.00 15.74           C  
-ATOM   1438  CG1 ILE B  89      21.381  29.363  26.912  1.00 12.11           C  
-ATOM   1439  CG2 ILE B  89      22.246  27.051  26.551  1.00 13.91           C  
-ATOM   1440  CD1 ILE B  89      19.901  28.980  27.022  1.00 18.32           C  
-ATOM   1441  N   LEU B  90      24.717  27.848  23.979  1.00 18.63           N  
-ATOM   1442  CA  LEU B  90      25.629  26.837  23.419  1.00 15.26           C  
-ATOM   1443  C   LEU B  90      27.079  27.110  23.858  1.00 14.63           C  
-ATOM   1444  O   LEU B  90      27.817  26.168  24.188  1.00 15.28           O  
-ATOM   1445  CB  LEU B  90      25.531  26.797  21.887  1.00 15.43           C  
-ATOM   1446  CG  LEU B  90      24.107  26.645  21.325  1.00 17.91           C  
-ATOM   1447  CD1 LEU B  90      24.102  26.608  19.789  1.00  9.54           C  
-ATOM   1448  CD2 LEU B  90      23.471  25.408  21.892  1.00  9.37           C  
-ATOM   1449  N   THR B  91      27.491  28.378  23.901  1.00 12.81           N  
-ATOM   1450  CA  THR B  91      28.857  28.691  24.316  1.00 14.97           C  
-ATOM   1451  C   THR B  91      29.054  28.399  25.797  1.00 18.75           C  
-ATOM   1452  O   THR B  91      30.083  27.863  26.200  1.00 20.42           O  
-ATOM   1453  CB  THR B  91      29.204  30.145  24.070  1.00 11.10           C  
-ATOM   1454  OG1 THR B  91      28.195  30.962  24.656  1.00 19.93           O  
-ATOM   1455  CG2 THR B  91      29.274  30.428  22.586  1.00 15.14           C  
-ATOM   1456  N   ALA B  92      28.026  28.688  26.592  1.00 20.51           N  
-ATOM   1457  CA  ALA B  92      28.078  28.451  28.040  1.00 22.46           C  
-ATOM   1458  C   ALA B  92      28.240  26.972  28.315  1.00 23.38           C  
-ATOM   1459  O   ALA B  92      28.795  26.581  29.344  1.00 26.99           O  
-ATOM   1460  CB  ALA B  92      26.792  28.965  28.707  1.00 17.17           C  
-ATOM   1461  N   LEU B  93      27.688  26.145  27.431  1.00 24.77           N  
-ATOM   1462  CA  LEU B  93      27.782  24.694  27.591  1.00 22.32           C  
-ATOM   1463  C   LEU B  93      29.085  24.158  27.001  1.00 23.55           C  
-ATOM   1464  O   LEU B  93      29.436  23.010  27.222  1.00 27.21           O  
-ATOM   1465  CB  LEU B  93      26.576  23.979  26.954  1.00 17.89           C  
-ATOM   1466  CG  LEU B  93      25.157  24.154  27.541  1.00 21.47           C  
-ATOM   1467  CD1 LEU B  93      24.115  23.545  26.603  1.00 19.59           C  
-ATOM   1468  CD2 LEU B  93      25.039  23.528  28.922  1.00 20.21           C  
-ATOM   1469  N   GLY B  94      29.798  24.990  26.247  1.00 22.83           N  
-ATOM   1470  CA  GLY B  94      31.047  24.551  25.645  1.00 21.54           C  
-ATOM   1471  C   GLY B  94      30.883  23.809  24.338  1.00 22.18           C  
-ATOM   1472  O   GLY B  94      31.789  23.090  23.900  1.00 22.00           O  
-ATOM   1473  N   MET B  95      29.731  23.972  23.699  1.00 21.18           N  
-ATOM   1474  CA  MET B  95      29.483  23.318  22.420  1.00 22.63           C  
-ATOM   1475  C   MET B  95      30.194  24.009  21.267  1.00 21.99           C  
-ATOM   1476  O   MET B  95      30.496  25.198  21.337  1.00 22.81           O  
-ATOM   1477  CB  MET B  95      27.992  23.260  22.119  1.00 22.63           C  
-ATOM   1478  CG  MET B  95      27.268  22.177  22.888  1.00 28.42           C  
-ATOM   1479  SD  MET B  95      25.615  21.933  22.277  1.00 34.68           S  
-ATOM   1480  CE  MET B  95      24.755  21.636  23.773  1.00 44.32           C  
-ATOM   1481  N   SER B  96      30.497  23.245  20.221  1.00 19.27           N  
-ATOM   1482  CA  SER B  96      31.159  23.801  19.053  1.00 17.14           C  
-ATOM   1483  C   SER B  96      30.636  23.047  17.833  1.00 17.41           C  
-ATOM   1484  O   SER B  96      30.113  21.934  17.941  1.00 16.88           O  
-ATOM   1485  CB  SER B  96      32.682  23.654  19.177  1.00 13.30           C  
-ATOM   1486  OG  SER B  96      33.039  22.284  19.219  1.00 18.45           O  
-ATOM   1487  N   LEU B  97      30.755  23.679  16.677  1.00 16.15           N  
-ATOM   1488  CA  LEU B  97      30.299  23.118  15.417  1.00 19.36           C  
-ATOM   1489  C   LEU B  97      31.586  22.696  14.723  1.00 19.88           C  
-ATOM   1490  O   LEU B  97      32.495  23.524  14.536  1.00 21.20           O  
-ATOM   1491  CB  LEU B  97      29.593  24.226  14.649  1.00 17.60           C  
-ATOM   1492  CG  LEU B  97      28.787  23.990  13.394  1.00 15.93           C  
-ATOM   1493  CD1 LEU B  97      27.714  22.911  13.608  1.00 15.55           C  
-ATOM   1494  CD2 LEU B  97      28.155  25.322  13.070  1.00 12.14           C  
-ATOM   1495  N   ASN B  98      31.689  21.417  14.372  1.00 20.07           N  
-ATOM   1496  CA  ASN B  98      32.929  20.917  13.772  1.00 23.23           C  
-ATOM   1497  C   ASN B  98      32.807  20.249  12.424  1.00 24.85           C  
-ATOM   1498  O   ASN B  98      31.773  19.676  12.097  1.00 24.30           O  
-ATOM   1499  CB  ASN B  98      33.605  19.947  14.730  1.00 22.33           C  
-ATOM   1500  CG  ASN B  98      33.924  20.595  16.066  1.00 28.39           C  
-ATOM   1501  OD1 ASN B  98      33.039  20.831  16.874  1.00 22.86           O  
-ATOM   1502  ND2 ASN B  98      35.188  20.898  16.291  1.00 32.61           N  
-ATOM   1503  N   LEU B  99      33.909  20.291  11.688  1.00 25.16           N  
-ATOM   1504  CA  LEU B  99      34.028  19.705  10.366  1.00 26.22           C  
-ATOM   1505  C   LEU B  99      35.438  19.139  10.347  1.00 27.19           C  
-ATOM   1506  O   LEU B  99      35.585  17.930  10.098  1.00 31.13           O  
-ATOM   1507  CB  LEU B  99      33.935  20.793   9.287  1.00 25.70           C  
-ATOM   1508  CG  LEU B  99      33.470  20.399   7.885  1.00 26.60           C  
-ATOM   1509  CD1 LEU B  99      34.188  21.293   6.926  1.00 30.02           C  
-ATOM   1510  CD2 LEU B  99      33.781  18.942   7.538  1.00 29.53           C  
-ATOM   1511  OXT LEU B  99      36.381  19.924  10.578  1.00 26.18           O  
-TER    1512      LEU B  99                                                      
-HETATM 1513  S   SO4 A 100      18.458  17.993  -0.310  1.00 53.82           S  
-HETATM 1514  O1  SO4 A 100      19.073  16.775   0.132  1.00 57.72           O  
-HETATM 1515  O2  SO4 A 100      18.127  17.855  -1.688  1.00 58.86           O  
-HETATM 1516  O3  SO4 A 100      17.237  18.164   0.425  1.00 57.04           O  
-HETATM 1517  O4  SO4 A 100      19.332  19.137  -0.134  1.00 42.12           O  
-HETATM 1518  S   SO4 B 100       7.406  21.493  12.343  1.00 74.77           S  
-HETATM 1519  O1  SO4 B 100       6.248  21.923  13.068  1.00 78.58           O  
-HETATM 1520  O2  SO4 B 100       8.006  20.418  13.069  1.00 74.06           O  
-HETATM 1521  O3  SO4 B 100       7.029  21.043  11.025  1.00 74.01           O  
-HETATM 1522  O4  SO4 B 100       8.300  22.599  12.218  1.00 76.00           O  
-HETATM 1523  C1  C20 B 101      18.542  37.227  14.994  1.00 12.85           C  
-HETATM 1524  C2  C20 B 101      18.321  35.770  15.416  1.00 14.63           C  
-HETATM 1525  O3  C20 B 101      19.244  35.111  15.921  1.00 16.95           O  
-HETATM 1526  N4  C20 B 101      17.098  35.276  15.224  1.00 15.46           N  
-HETATM 1527  C5  C20 B 101      16.794  33.868  15.455  1.00 13.42           C  
-HETATM 1528  C6  C20 B 101      15.773  33.717  16.622  1.00 13.54           C  
-HETATM 1529  C7  C20 B 101      15.402  32.240  16.869  1.00 11.09           C  
-HETATM 1530  C8  C20 B 101      16.358  34.341  17.912  1.00 17.68           C  
-HETATM 1531  C9  C20 B 101      16.304  33.148  14.183  1.00 18.58           C  
-HETATM 1532  O10 C20 B 101      15.163  33.356  13.736  1.00 12.73           O  
-HETATM 1533  N11 C20 B 101      17.173  32.313  13.610  1.00 11.84           N  
-HETATM 1534  C12 C20 B 101      16.853  31.533  12.416  1.00 11.27           C  
-HETATM 1535  C13 C20 B 101      17.713  31.996  11.253  1.00 23.62           C  
-HETATM 1536  C14 C20 B 101      17.670  33.494  11.054  1.00 23.08           C  
-HETATM 1537  C15 C20 B 101      18.479  34.398  11.909  1.00 24.70           C  
-HETATM 1538  C16 C20 B 101      18.381  35.774  11.693  1.00 29.55           C  
-HETATM 1539  C17 C20 B 101      17.550  36.299  10.679  1.00 26.81           C  
-HETATM 1540  C18 C20 B 101      16.777  35.472   9.850  1.00 23.32           C  
-HETATM 1541  C19 C20 B 101      16.812  34.085   9.999  1.00 23.91           C  
-HETATM 1542  C20 C20 B 101      17.072  30.015  12.629  1.00 12.13           C  
-HETATM 1543  O21 C20 B 101      18.339  29.746  13.215  1.00 20.69           O  
-HETATM 1544  C22 C20 B 101      16.106  29.424  13.614  1.00 17.09           C  
-HETATM 1545  N23 C20 B 101      14.808  29.230  13.057  1.00 20.70           N  
-HETATM 1546  C24 C20 B 101      14.137  28.421  14.049  1.00 20.50           C  
-HETATM 1547  C25 C20 B 101      12.683  28.379  13.656  1.00 24.09           C  
-HETATM 1548  C26 C20 B 101      11.787  28.873  14.775  1.00 26.30           C  
-HETATM 1549  C27 C20 B 101      10.339  28.793  14.404  1.00 29.64           C  
-HETATM 1550  C28 C20 B 101       9.976  27.385  14.050  1.00 28.85           C  
-HETATM 1551  C29 C20 B 101      10.867  26.839  12.954  1.00 22.52           C  
-HETATM 1552  C30 C20 B 101      12.299  26.945  13.351  1.00 21.91           C  
-HETATM 1553  N31 C20 B 101      14.940  28.565  11.776  1.00 17.80           N  
-HETATM 1554  C32 C20 B 101      14.288  28.996  10.692  1.00 21.81           C  
-HETATM 1555  O33 C20 B 101      13.743  30.107  10.623  1.00 18.43           O  
-HETATM 1556  C34 C20 B 101      14.241  28.036   9.501  1.00 19.75           C  
-HETATM 1557  N35 C20 B 101      12.979  27.304   9.480  1.00 19.67           N  
-HETATM 1558  C36 C20 B 101      14.468  28.809   8.167  1.00 17.89           C  
-HETATM 1559  C37 C20 B 101      15.720  29.682   8.241  1.00 14.34           C  
-HETATM 1560  C38 C20 B 101      14.630  27.813   7.028  1.00 14.79           C  
-HETATM 1561  C39 C20 B 101      12.929  25.981   9.621  1.00 25.74           C  
-HETATM 1562  O40 C20 B 101      13.943  25.276   9.760  1.00 22.57           O  
-HETATM 1563  C41 C20 B 101      11.579  25.288   9.590  1.00 24.19           C  
-HETATM 1564  O   HOH A 101      31.398  30.538  15.634  1.00 16.03           O  
-HETATM 1565  O   HOH A 102      16.887  23.798   1.067  1.00 16.81           O  
-HETATM 1566  O   HOH A 103      29.706  26.817  -7.062  1.00 17.12           O  
-HETATM 1567  O   HOH A 104      32.002  27.056  22.256  1.00 18.54           O  
-HETATM 1568  O   HOH A 105      17.119  26.770 -12.963  1.00 19.18           O  
-HETATM 1569  O   HOH A 106      14.789  23.573  12.459  1.00 21.57           O  
-HETATM 1570  O   HOH A 107      16.909  21.748  12.776  1.00 23.11           O  
-HETATM 1571  O   HOH A 108      33.547  32.419  17.467  1.00 24.09           O  
-HETATM 1572  O   HOH A 109      24.316  36.386   5.061  1.00 24.59           O  
-HETATM 1573  O   HOH A 110      11.916  22.470  -6.640  1.00 25.20           O  
-HETATM 1574  O   HOH A 111      34.008  28.237   2.413  1.00 27.32           O  
-HETATM 1575  O   HOH A 112      19.097  18.513  -4.386  1.00 27.61           O  
-HETATM 1576  O   HOH A 113      14.104  22.465  -8.528  1.00 29.43           O  
-HETATM 1577  O   HOH A 114      26.379  37.521   0.885  1.00 30.54           O  
-HETATM 1578  O   HOH A 115      13.357  34.139  -4.666  1.00 30.64           O  
-HETATM 1579  O   HOH A 116      17.457  16.424  -6.254  1.00 31.88           O  
-HETATM 1580  O   HOH A 117      35.637  26.245  -0.500  1.00 32.02           O  
-HETATM 1581  O   HOH A 118      20.460  37.661   2.846  1.00 34.05           O  
-HETATM 1582  O   HOH A 119       8.815  25.843   7.350  1.00 34.46           O  
-HETATM 1583  O   HOH A 120      11.041  34.269  -3.560  1.00 35.11           O  
-HETATM 1584  O   HOH A 121      27.183  13.723   7.758  1.00 35.67           O  
-HETATM 1585  O   HOH A 122       7.652  25.782  10.115  1.00 36.63           O  
-HETATM 1586  O   HOH A 123       7.336  36.084   1.305  1.00 37.26           O  
-HETATM 1587  O   HOH A 124      31.065  36.389  12.490  1.00 37.48           O  
-HETATM 1588  O   HOH A 125      17.201  18.906   6.493  1.00 39.17           O  
-HETATM 1589  O   HOH A 126      14.454  17.855   6.920  1.00 40.28           O  
-HETATM 1590  O   HOH A 127       7.170  31.289  -4.198  1.00 40.28           O  
-HETATM 1591  O   HOH A 128      22.004  17.720   0.229  1.00 41.72           O  
-HETATM 1592  O   HOH A 129      11.344  20.743  -8.543  1.00 42.33           O  
-HETATM 1593  O   HOH A 130      16.816  28.637 -16.402  1.00 42.53           O  
-HETATM 1594  O   HOH A 131      34.689  31.227   4.787  1.00 42.58           O  
-HETATM 1595  O   HOH A 132      28.454  38.002  11.250  1.00 42.77           O  
-HETATM 1596  O   HOH A 133      33.914  17.474  -1.745  1.00 42.98           O  
-HETATM 1597  O   HOH A 134      28.968  37.551  15.281  1.00 43.10           O  
-HETATM 1598  O   HOH A 135      16.244  32.656  -8.190  1.00 43.53           O  
-HETATM 1599  O   HOH A 136      12.106  25.620 -16.459  1.00 43.55           O  
-HETATM 1600  O   HOH A 137      11.151  22.472   6.947  1.00 44.15           O  
-HETATM 1601  O   HOH A 138      21.200  26.142 -11.290  1.00 45.10           O  
-HETATM 1602  O   HOH A 139      36.499  25.905  -8.574  1.00 45.15           O  
-HETATM 1603  O   HOH A 140       3.271  34.909   8.498  1.00 45.64           O  
-HETATM 1604  O   HOH A 141      26.105  38.113  10.117  1.00 45.90           O  
-HETATM 1605  O   HOH A 142      34.134  25.386  21.489  1.00 46.12           O  
-HETATM 1606  O   HOH A 143      26.923  16.108  -3.329  1.00 46.41           O  
-HETATM 1607  O   HOH A 144      33.471  15.958   8.807  1.00 47.44           O  
-HETATM 1608  O   HOH A 145      23.175  37.344  -0.806  1.00 47.81           O  
-HETATM 1609  O   HOH A 146       4.831  30.586  -2.491  1.00 48.43           O  
-HETATM 1610  O   HOH A 147      13.807  19.879  -0.375  1.00 49.49           O  
-HETATM 1611  O   HOH A 148      35.512  24.482  -3.584  1.00 49.73           O  
-HETATM 1612  O   HOH A 149      13.811  19.531  -9.860  1.00 49.81           O  
-HETATM 1613  O   HOH A 150      23.987  16.179  -0.582  1.00 50.44           O  
-HETATM 1614  O   HOH A 151       5.453  36.610   7.184  1.00 50.85           O  
-HETATM 1615  O   HOH A 152       9.326  19.250  -3.356  1.00 51.51           O  
-HETATM 1616  O   HOH A 153      16.478  33.285 -11.436  1.00 51.52           O  
-HETATM 1617  O   HOH A 154      22.611  15.252   2.903  1.00 51.61           O  
-HETATM 1618  O   HOH A 155      10.522  35.999  -0.117  1.00 51.76           O  
-HETATM 1619  O   HOH A 156       7.881  23.024  -4.334  1.00 51.77           O  
-HETATM 1620  O   HOH A 157      32.556  16.577  12.410  1.00 51.78           O  
-HETATM 1621  O   HOH A 158      16.408  22.866 -10.091  1.00 51.92           O  
-HETATM 1622  O   HOH A 159      27.135  23.933 -12.095  1.00 52.26           O  
-HETATM 1623  O   HOH A 160       6.657  29.770  11.885  1.00 53.11           O  
-HETATM 1624  O   HOH A 161      34.530  28.845  -7.436  1.00 53.62           O  
-HETATM 1625  O   HOH A 162      34.794  33.704   6.873  1.00 54.41           O  
-HETATM 1626  O   HOH A 163       5.334  31.520  14.115  1.00 54.46           O  
-HETATM 1627  O   HOH A 164      15.721  21.399   1.954  1.00 54.57           O  
-HETATM 1628  O   HOH A 165      33.463  31.535  -8.578  1.00 54.58           O  
-HETATM 1629  O   HOH A 166      10.819  18.666  -0.643  1.00 56.00           O  
-HETATM 1630  O   HOH A 167      24.163  38.257   3.101  1.00 56.04           O  
-HETATM 1631  O   HOH A 168      10.309  21.773   1.337  1.00 56.96           O  
-HETATM 1632  O   HOH A 169      16.324  37.627  -3.551  1.00 58.21           O  
-HETATM 1633  O   HOH A 170      35.463  27.922  -5.141  1.00 59.25           O  
-HETATM 1634  O   HOH A 171       5.685  22.807  -2.801  1.00 59.61           O  
-HETATM 1635  O   HOH A 172      15.183  19.566   4.238  1.00 59.91           O  
-HETATM 1636  O   HOH A 173      36.510  26.944  18.889  1.00 59.93           O  
-HETATM 1637  O   HOH A 174      15.572  16.468  -2.062  1.00 60.65           O  
-HETATM 1638  O   HOH A 175       5.655  25.094   6.026  1.00 61.19           O  
-HETATM 1639  O   HOH A 176      25.605  30.688 -11.993  1.00 61.30           O  
-HETATM 1640  O   HOH A 177       8.654  33.572  -4.589  1.00 62.18           O  
-HETATM 1641  O   HOH A 178      15.390  16.337   4.144  1.00 63.22           O  
-HETATM 1642  O   HOH A 179      24.750  22.635 -11.203  1.00 63.38           O  
-HETATM 1643  O   HOH A 180       9.372  40.335   1.170  1.00 64.75           O  
-HETATM 1644  O   HOH A 181      18.540  34.764  -4.101  1.00 65.34           O  
-HETATM 1645  O   HOH A 182      26.711  36.489  -6.151  1.00 66.18           O  
-HETATM 1646  O   HOH A 183      16.690  19.671 -10.585  1.00 66.53           O  
-HETATM 1647  O   HOH A 184      11.372  18.930  10.094  1.00 68.04           O  
-HETATM 1648  O   HOH A 185      17.125  40.394   1.900  1.00 68.65           O  
-HETATM 1649  O   HOH A 186      30.360  37.895   6.695  1.00 69.41           O  
-HETATM 1650  O   HOH A 187       2.765  35.410   4.358  1.00 72.71           O  
-HETATM 1651  O   HOH A 188      35.254  35.818  -2.722  1.00 77.76           O  
-HETATM 1652  O   HOH B 102      13.393  32.580  12.018  1.00 14.35           O  
-HETATM 1653  O   HOH B 103      21.135  15.934  15.236  1.00 14.58           O  
-HETATM 1654  O   HOH B 104      23.193  34.012  28.391  1.00 15.63           O  
-HETATM 1655  O   HOH B 105      24.117  32.861  15.257  1.00 16.81           O  
-HETATM 1656  O   HOH B 106      18.659  34.938  25.273  1.00 17.26           O  
-HETATM 1657  O   HOH B 107      21.204  12.846  13.782  1.00 19.98           O  
-HETATM 1658  O   HOH B 108      16.597  23.637  36.096  1.00 20.58           O  
-HETATM 1659  O   HOH B 109       4.294  30.616  17.446  1.00 22.41           O  
-HETATM 1660  O   HOH B 110      26.698  15.537   9.947  1.00 23.11           O  
-HETATM 1661  O   HOH B 111      24.058  12.350  16.497  1.00 23.17           O  
-HETATM 1662  O   HOH B 112      22.002  34.484  14.234  1.00 23.19           O  
-HETATM 1663  O   HOH B 113      27.413  11.127  21.295  1.00 23.69           O  
-HETATM 1664  O   HOH B 114       8.666  43.848  23.582  1.00 24.35           O  
-HETATM 1665  O   HOH B 115      14.732  46.455  26.680  1.00 25.31           O  
-HETATM 1666  O   HOH B 116      16.513  41.241  31.952  1.00 25.38           O  
-HETATM 1667  O   HOH B 117       7.585  34.619  31.395  1.00 26.11           O  
-HETATM 1668  O   HOH B 118       4.475  39.266  19.087  1.00 27.42           O  
-HETATM 1669  O   HOH B 119      17.252  29.097  40.742  1.00 28.32           O  
-HETATM 1670  O   HOH B 120      22.070  35.819  32.518  1.00 28.44           O  
-HETATM 1671  O   HOH B 121       5.866  36.646  21.596  1.00 28.50           O  
-HETATM 1672  O   HOH B 122       8.629  21.275  25.264  1.00 28.54           O  
-HETATM 1673  O   HOH B 123      25.776  10.167  24.059  1.00 28.80           O  
-HETATM 1674  O   HOH B 124      14.962  15.316  16.408  1.00 30.03           O  
-HETATM 1675  O   HOH B 125      10.241  22.975  21.564  1.00 30.62           O  
-HETATM 1676  O   HOH B 126       7.299  26.376  21.788  1.00 31.52           O  
-HETATM 1677  O   HOH B 127      19.018  16.992  29.413  1.00 35.69           O  
-HETATM 1678  O   HOH B 128      19.766  39.422  17.664  1.00 36.49           O  
-HETATM 1679  O   HOH B 129      14.899  45.013  21.516  1.00 37.24           O  
-HETATM 1680  O   HOH B 130      15.733  39.058  34.637  1.00 37.43           O  
-HETATM 1681  O   HOH B 131       7.193  24.597  25.849  1.00 37.57           O  
-HETATM 1682  O   HOH B 132       6.433  35.751  27.205  1.00 38.14           O  
-HETATM 1683  O   HOH B 133      12.857  46.298  32.675  1.00 38.35           O  
-HETATM 1684  O   HOH B 134      10.726  37.715  37.518  1.00 39.04           O  
-HETATM 1685  O   HOH B 135       6.211  38.007  25.179  1.00 39.67           O  
-HETATM 1686  O   HOH B 136      14.261  39.974  10.831  1.00 40.06           O  
-HETATM 1687  O   HOH B 137      24.635  35.439  21.647  1.00 40.14           O  
-HETATM 1688  O   HOH B 138      16.598  39.858  12.135  1.00 40.54           O  
-HETATM 1689  O   HOH B 139       3.068  31.094  37.839  1.00 41.38           O  
-HETATM 1690  O   HOH B 140      15.649  46.688  23.862  1.00 41.52           O  
-HETATM 1691  O   HOH B 141      26.701  29.644  33.964  1.00 41.59           O  
-HETATM 1692  O   HOH B 142       2.457  29.287  16.023  1.00 41.64           O  
-HETATM 1693  O   HOH B 143      16.801  40.029  16.005  1.00 42.14           O  
-HETATM 1694  O   HOH B 144      15.036  46.716  31.174  1.00 42.27           O  
-HETATM 1695  O   HOH B 145      32.474  27.448  25.005  1.00 42.60           O  
-HETATM 1696  O   HOH B 146      28.201  32.421  27.222  1.00 42.64           O  
-HETATM 1697  O   HOH B 147      15.291  35.238  36.510  1.00 42.65           O  
-HETATM 1698  O   HOH B 148      19.700  17.258  32.181  1.00 45.13           O  
-HETATM 1699  O   HOH B 149      28.007  37.127  19.100  1.00 45.19           O  
-HETATM 1700  O   HOH B 150      17.455  21.093  36.826  1.00 45.98           O  
-HETATM 1701  O   HOH B 151      12.229  36.810   6.634  1.00 46.34           O  
-HETATM 1702  O   HOH B 152      31.969  25.253  29.473  1.00 46.38           O  
-HETATM 1703  O   HOH B 153       2.823  33.240  23.940  1.00 46.94           O  
-HETATM 1704  O   HOH B 154       2.905  29.193  12.973  1.00 47.06           O  
-HETATM 1705  O   HOH B 155       5.025  32.445  26.196  1.00 47.51           O  
-HETATM 1706  O   HOH B 156      12.076  16.961  16.219  1.00 47.82           O  
-HETATM 1707  O   HOH B 157       5.359  38.291  13.748  1.00 48.01           O  
-HETATM 1708  O   HOH B 158       2.301  28.927  31.238  1.00 48.06           O  
-HETATM 1709  O   HOH B 159      24.410  35.635  29.826  1.00 49.51           O  
-HETATM 1710  O   HOH B 160      26.409  31.273  31.294  1.00 50.20           O  
-HETATM 1711  O   HOH B 161      14.043  12.106  12.169  1.00 50.54           O  
-HETATM 1712  O   HOH B 162       3.749  28.895  21.153  1.00 50.63           O  
-HETATM 1713  O   HOH B 163      32.957  21.868  22.052  1.00 51.45           O  
-HETATM 1714  O   HOH B 164      21.380  39.781  26.898  1.00 51.50           O  
-HETATM 1715  O   HOH B 165      14.203  26.343  40.318  1.00 51.61           O  
-HETATM 1716  O   HOH B 166       6.370  25.290  13.217  1.00 51.93           O  
-HETATM 1717  O   HOH B 167      20.953  36.548  24.356  1.00 51.97           O  
-HETATM 1718  O   HOH B 168      13.681  15.666  12.314  1.00 52.30           O  
-HETATM 1719  O   HOH B 169      23.069  38.409  28.992  1.00 52.78           O  
-HETATM 1720  O   HOH B 170      10.035  39.483  39.515  1.00 55.69           O  
-HETATM 1721  O   HOH B 171       7.605  22.541   8.829  1.00 55.78           O  
-HETATM 1722  O   HOH B 172      29.238  28.286  31.359  1.00 56.14           O  
-HETATM 1723  O   HOH B 173       0.617  31.148  14.683  1.00 57.04           O  
-HETATM 1724  O   HOH B 174       1.385  33.788  27.115  1.00 57.62           O  
-HETATM 1725  O   HOH B 175      32.865  11.000  15.513  1.00 57.71           O  
-HETATM 1726  O   HOH B 176       6.312  39.816  11.696  1.00 57.73           O  
-HETATM 1727  O   HOH B 177      24.313  34.303  33.065  1.00 58.03           O  
-HETATM 1728  O   HOH B 178      29.166   9.474  16.530  1.00 58.70           O  
-HETATM 1729  O   HOH B 179      23.063  36.525  26.915  1.00 58.72           O  
-HETATM 1730  O   HOH B 180      14.318  15.000  23.557  1.00 59.07           O  
-HETATM 1731  O   HOH B 181      16.336  32.538  38.289  1.00 59.51           O  
-HETATM 1732  O   HOH B 182      25.620  37.339  20.114  1.00 59.66           O  
-HETATM 1733  O   HOH B 183      13.724  37.762  37.703  1.00 60.29           O  
-HETATM 1734  O   HOH B 184      17.162  41.594  39.091  1.00 61.00           O  
-HETATM 1735  O   HOH B 185       6.456  28.085  34.136  1.00 61.14           O  
-HETATM 1736  O   HOH B 186      25.542  32.537  28.729  1.00 61.40           O  
-HETATM 1737  O   HOH B 187      10.830  27.098  34.481  1.00 62.14           O  
-HETATM 1738  O   HOH B 188       7.284  38.110   5.886  1.00 62.17           O  
-HETATM 1739  O   HOH B 189      11.581  19.858  16.234  1.00 62.73           O  
-HETATM 1740  O   HOH B 190       9.454  17.717  27.987  1.00 64.24           O  
-HETATM 1741  O   HOH B 191      12.099  15.384  18.565  1.00 64.69           O  
-HETATM 1742  O   HOH B 192       7.557  23.644  20.706  1.00 65.03           O  
-HETATM 1743  O   HOH B 193       7.381  19.399  26.874  1.00 66.83           O  
-HETATM 1744  O   HOH B 194      36.848  19.254  13.779  1.00 66.92           O  
-HETATM 1745  O   HOH B 195       1.469  36.216  19.793  1.00 67.36           O  
-HETATM 1746  O   HOH B 196      32.050  28.041  28.514  1.00 68.11           O  
-HETATM 1747  O   HOH B 197       3.493  35.441  30.060  1.00 68.99           O  
-HETATM 1748  O   HOH B 198      -0.008  28.151  32.511  1.00 69.06           O  
-HETATM 1749  O   HOH B 199       2.303  40.848  28.316  1.00 71.32           O  
-HETATM 1750  O   HOH B 200      13.198   8.627  13.077  1.00 71.32           O  
-HETATM 1751  O   HOH B 201      23.230  38.306  33.915  1.00 72.80           O  
-HETATM 1752  O   HOH B 202       3.168  31.588  30.276  1.00 72.81           O  
-HETATM 1753  O   HOH B 203      13.109  38.745   8.199  1.00 75.48           O  
-HETATM 1754  O   HOH B 204      20.434  39.699  20.694  1.00 78.37           O  
-HETATM 1755  O   HOH B 205       4.009  36.286  23.900  1.00 78.52           O  
-HETATM 1756  O   HOH B 206       1.275  25.760  31.247  1.00 79.12           O  
-HETATM 1757  O   HOH B 207      16.794  42.031  18.749  1.00 79.67           O  
-CONECT 1513 1514 1515 1516 1517                                                 
-CONECT 1514 1513                                                                
-CONECT 1515 1513                                                                
-CONECT 1516 1513                                                                
-CONECT 1517 1513                                                                
-CONECT 1518 1519 1520 1521 1522                                                 
-CONECT 1519 1518                                                                
-CONECT 1520 1518                                                                
-CONECT 1521 1518                                                                
-CONECT 1522 1518                                                                
-CONECT 1523 1524                                                                
-CONECT 1524 1523 1525 1526                                                      
-CONECT 1525 1524                                                                
-CONECT 1526 1524 1527                                                           
-CONECT 1527 1526 1528 1531                                                      
-CONECT 1528 1527 1529 1530                                                      
-CONECT 1529 1528                                                                
-CONECT 1530 1528                                                                
-CONECT 1531 1527 1532 1533                                                      
-CONECT 1532 1531                                                                
-CONECT 1533 1531 1534                                                           
-CONECT 1534 1533 1535 1542                                                      
-CONECT 1535 1534 1536                                                           
-CONECT 1536 1535 1537 1541                                                      
-CONECT 1537 1536 1538                                                           
-CONECT 1538 1537 1539                                                           
-CONECT 1539 1538 1540                                                           
-CONECT 1540 1539 1541                                                           
-CONECT 1541 1536 1540                                                           
-CONECT 1542 1534 1543 1544                                                      
-CONECT 1543 1542                                                                
-CONECT 1544 1542 1545                                                           
-CONECT 1545 1544 1546 1553                                                      
-CONECT 1546 1545 1547                                                           
-CONECT 1547 1546 1548 1552                                                      
-CONECT 1548 1547 1549                                                           
-CONECT 1549 1548 1550                                                           
-CONECT 1550 1549 1551                                                           
-CONECT 1551 1550 1552                                                           
-CONECT 1552 1547 1551                                                           
-CONECT 1553 1545 1554                                                           
-CONECT 1554 1553 1555 1556                                                      
-CONECT 1555 1554                                                                
-CONECT 1556 1554 1557 1558                                                      
-CONECT 1557 1556 1561                                                           
-CONECT 1558 1556 1559 1560                                                      
-CONECT 1559 1558                                                                
-CONECT 1560 1558                                                                
-CONECT 1561 1557 1562 1563                                                      
-CONECT 1562 1561                                                                
-CONECT 1563 1561                                                                
-MASTER      245    0    3    2   16    0   18    9 1755    2   51   16          
-END                                                                             
diff --git a/plip/test/pdb/1hvi.pdb b/plip/test/pdb/1hvi.pdb
deleted file mode 100644
index ed1d520..0000000
--- a/plip/test/pdb/1hvi.pdb
+++ /dev/null
@@ -1,2409 +0,0 @@
-HEADER    HYDROLASE(ACID PROTEASE)                26-JAN-94   1HVI              
-TITLE     INFLUENCE OF STEREOCHEMISTRY ON ACTIVITY AND BINDING MODES            
-TITLE    2 FOR C2 SYMMETRY-BASED DIOL INHIBITORS OF HIV-1 PROTEASE              
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: HIV-1 PROTEASE;                                            
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
-SOURCE   3 ORGANISM_TAXID: 11676;                                               
-SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
-KEYWDS    HYDROLASE(ACID PROTEASE)                                              
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    T.N.BHAT,M.V.HOSUR,E.T.BALDWIN,J.W.ERICKSON                           
-REVDAT   2   24-FEB-09 1HVI    1       VERSN                                    
-REVDAT   1   30-APR-94 1HVI    0                                                
-JRNL        AUTH   M.V.HOSUR,T.N.BHAT,D.KEMPF,E.T.BALDWIN,B.LIU,                
-JRNL        AUTH 2 S.GULNIK,N.E.WIDEBURG,D.W.NORBECK,K.APPELT,                  
-JRNL        AUTH 3 J.W.ERICKSON                                                 
-JRNL        TITL   INFLUENCE OF STEREOCHEMISTRY ON ACTIVITY AND                 
-JRNL        TITL 2 BINDING MODES FOR C2 SYMMETRY-BASED DIOL                     
-JRNL        TITL 3 INHIBITORS OF HIV-1 PROTEASE                                 
-JRNL        REF    J.AM.CHEM.SOC.                V. 116   847 1994              
-JRNL        REFN                   ISSN 0002-7863                               
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   A.WLODAWER,J.W.ERICKSON                                      
-REMARK   1  TITL   STRUCTURE-BASED INHIBITORS OF HIV-1 PROTEASE                 
-REMARK   1  REF    ANNU.REV.BIOCHEM.             V.  62   543 1993              
-REMARK   1  REFN                   ISSN 0066-4154                               
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : X-PLOR                                               
-REMARK   3   AUTHORS     : BRUNGER                                              
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
-REMARK   3   NUMBER OF REFLECTIONS             : 17998                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
-REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
-REMARK   3   R VALUE            (WORKING SET) : 0.181                           
-REMARK   3   FREE R VALUE                     : NULL                            
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
-REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
-REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
-REMARK   3   BIN FREE R VALUE                    : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 1846                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 116                                     
-REMARK   3   SOLVENT ATOMS            : 3                                       
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
-REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.014                           
-REMARK   3   BOND ANGLES            (DEGREES) : 2.60                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
-REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1HVI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : NULL                               
-REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
-REMARK 200  PH                             : NULL                               
-REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
-REMARK 200  RADIATION SOURCE               : NULL                               
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
-REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : NULL                               
-REMARK 200  DETECTOR MANUFACTURER          : NULL                               
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
-REMARK 200  DATA SCALING SOFTWARE          : NULL                               
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
-REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
-REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
-REMARK 200 SOFTWARE USED: X-PLOR                                                
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 44.94                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.99000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.15500            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.82500            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       31.15500            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.99000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.82500            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 5250 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 9130 ANGSTROM**2                        
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
-REMARK 500    TRP A   6   CE2   TRP A   6   CD2     0.079                       
-REMARK 500    TRP A  42   CE2   TRP A  42   CD2     0.074                       
-REMARK 500    TRP B   6   CE2   TRP B   6   CD2     0.087                       
-REMARK 500    TRP B  42   CE2   TRP B  42   CD2     0.077                       
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    ARG A  41   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
-REMARK 500    MET B  46   CA  -  CB  -  CG  ANGL. DEV. = -11.4 DEGREES          
-REMARK 500    ARG B  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A77 A 800                 
-DBREF  1HVI A    1    99  UNP    P03368   POL_HV1PV       69    167             
-DBREF  1HVI B    1    99  UNP    P03368   POL_HV1PV       69    167             
-SEQRES   1 A   99  PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE          
-SEQRES   2 A   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
-SEQRES   3 A   99  GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO          
-SEQRES   4 A   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
-SEQRES   5 A   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU          
-SEQRES   6 A   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
-SEQRES   7 A   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
-SEQRES   8 A   99  GLN ILE GLY CYS THR LEU ASN PHE                              
-SEQRES   1 B   99  PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE          
-SEQRES   2 B   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
-SEQRES   3 B   99  GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO          
-SEQRES   4 B   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
-SEQRES   5 B   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU          
-SEQRES   6 B   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
-SEQRES   7 B   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
-SEQRES   8 B   99  GLN ILE GLY CYS THR LEU ASN PHE                              
-HET    A77  A 800     116                                                       
-HETNAM     A77 N-{1-BENZYL-(2R,3S)-2,3-DIHYDROXY-4-[3-METHYL-2-(3-              
-HETNAM   2 A77  METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRYLAMINO]-5-            
-HETNAM   3 A77  PHENYL-PENTYL}-3-METHYL-2-(3-METHYL-3-PYRIDIN-2-                
-HETNAM   4 A77  YLMETHYL-UREIDO)-BUTYRAMIDE                                     
-FORMUL   3  A77    C44 H58 N8 O6                                                
-FORMUL   4  HOH   *(H2 O)                                                       
-HELIX    1   1 GLY A   86  THR A   91  1                                   6    
-HELIX    2   2 GLY B   86  THR B   91  1                                   6    
-SHEET    1   A 4 GLN A   2  ILE A   3  0                                        
-SHEET    2   A 4 THR B  96  ASN B  98 -1  O  LEU B  97   N  ILE A   3           
-SHEET    3   A 4 THR A  96  ASN A  98 -1  O  THR A  96   N  ASN B  98           
-SHEET    4   A 4 GLN B   2  ILE B   3 -1  N  ILE B   3   O  LEU A  97           
-SITE     1 AC1 18 ARG A   8  ASP A  25  GLY A  27  ALA A  28                    
-SITE     2 AC1 18 ASP A  29  GLY A  48  GLY A  49  ILE A  50                    
-SITE     3 AC1 18 VAL A  82  HOH A 415  ARG B   8  ASP B  25                    
-SITE     4 AC1 18 GLY B  27  ALA B  28  ASP B  29  GLY B  48                    
-SITE     5 AC1 18 GLY B  49  PRO B  81                                          
-CRYST1   51.980   59.650   62.310  90.00  90.00  90.00 P 21 21 21    8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.019238  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.016764  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.016049        0.00000                         
-ATOM      1  N   PRO A   1      -3.609   7.549  33.926  1.00 27.71           N  
-ATOM      2  CA  PRO A   1      -2.655   6.720  34.710  1.00 27.34           C  
-ATOM      3  C   PRO A   1      -1.219   6.969  34.289  1.00 27.56           C  
-ATOM      4  O   PRO A   1      -1.000   7.590  33.270  1.00 29.50           O  
-ATOM      5  CB  PRO A   1      -3.028   5.271  34.444  1.00 27.00           C  
-ATOM      6  CG  PRO A   1      -3.683   5.350  33.091  1.00 26.56           C  
-ATOM      7  CD  PRO A   1      -4.487   6.638  33.180  1.00 26.27           C  
-ATOM      8  H2  PRO A   1      -4.150   8.229  34.498  1.00 15.00           H  
-ATOM      9  H3  PRO A   1      -3.079   8.144  33.239  1.00 15.00           H  
-ATOM     10  N   GLN A   2      -0.281   6.475  35.087  1.00 28.29           N  
-ATOM     11  CA  GLN A   2       1.115   6.384  34.643  1.00 26.47           C  
-ATOM     12  C   GLN A   2       1.475   4.934  34.363  1.00 26.06           C  
-ATOM     13  O   GLN A   2       1.525   4.091  35.247  1.00 26.49           O  
-ATOM     14  CB  GLN A   2       2.088   6.929  35.709  1.00 28.28           C  
-ATOM     15  CG  GLN A   2       3.547   6.763  35.234  1.00 33.61           C  
-ATOM     16  CD  GLN A   2       4.535   7.615  36.004  1.00 36.82           C  
-ATOM     17  OE1 GLN A   2       4.636   8.815  35.868  1.00 38.65           O  
-ATOM     18  NE2 GLN A   2       5.280   6.979  36.876  1.00 39.02           N  
-ATOM     19  H   GLN A   2      -0.523   6.029  35.947  1.00 15.00           H  
-ATOM     20 HE21 GLN A   2       5.871   7.566  37.432  1.00  0.00           H  
-ATOM     21 HE22 GLN A   2       5.318   5.990  36.943  1.00  0.00           H  
-ATOM     22  N   ILE A   3       1.698   4.657  33.095  1.00 23.44           N  
-ATOM     23  CA  ILE A   3       2.009   3.268  32.738  1.00 20.83           C  
-ATOM     24  C   ILE A   3       3.505   3.043  32.515  1.00 20.66           C  
-ATOM     25  O   ILE A   3       4.218   3.727  31.790  1.00 19.79           O  
-ATOM     26  CB  ILE A   3       1.177   2.900  31.499  1.00 21.44           C  
-ATOM     27  CG1 ILE A   3      -0.303   3.139  31.829  1.00 24.58           C  
-ATOM     28  CG2 ILE A   3       1.380   1.449  31.026  1.00 19.03           C  
-ATOM     29  CD1 ILE A   3      -1.243   2.982  30.637  1.00 29.25           C  
-ATOM     30  H   ILE A   3       1.698   5.397  32.414  1.00 15.00           H  
-ATOM     31  N   THR A   4       3.992   2.040  33.209  1.00 18.69           N  
-ATOM     32  CA  THR A   4       5.380   1.639  32.956  1.00 17.49           C  
-ATOM     33  C   THR A   4       5.462   0.593  31.843  1.00 18.07           C  
-ATOM     34  O   THR A   4       4.482   0.047  31.361  1.00 18.93           O  
-ATOM     35  CB  THR A   4       6.020   1.070  34.240  1.00 17.65           C  
-ATOM     36  OG1 THR A   4       5.281  -0.065  34.690  1.00 16.37           O  
-ATOM     37  CG2 THR A   4       6.081   2.112  35.360  1.00 17.72           C  
-ATOM     38  H   THR A   4       3.372   1.504  33.786  1.00 15.00           H  
-ATOM     39  HG1 THR A   4       4.407   0.202  34.999  1.00 15.00           H  
-ATOM     40  N   LEU A   5       6.664   0.337  31.403  1.00 16.85           N  
-ATOM     41  CA  LEU A   5       6.764  -0.488  30.197  1.00 16.82           C  
-ATOM     42  C   LEU A   5       7.419  -1.847  30.384  1.00 18.37           C  
-ATOM     43  O   LEU A   5       7.907  -2.489  29.463  1.00 17.51           O  
-ATOM     44  CB  LEU A   5       7.498   0.365  29.142  1.00 16.31           C  
-ATOM     45  CG  LEU A   5       6.723   1.650  28.814  1.00 14.76           C  
-ATOM     46  CD1 LEU A   5       7.608   2.610  28.037  1.00 16.19           C  
-ATOM     47  CD2 LEU A   5       5.442   1.327  28.053  1.00 17.31           C  
-ATOM     48  H   LEU A   5       7.466   0.768  31.819  1.00 15.00           H  
-ATOM     49  N   TRP A   6       7.406  -2.307  31.638  1.00 17.85           N  
-ATOM     50  CA  TRP A   6       7.944  -3.639  31.884  1.00 17.67           C  
-ATOM     51  C   TRP A   6       7.106  -4.699  31.243  1.00 19.61           C  
-ATOM     52  O   TRP A   6       7.592  -5.708  30.780  1.00 22.70           O  
-ATOM     53  CB  TRP A   6       8.048  -3.909  33.405  1.00 20.76           C  
-ATOM     54  CG  TRP A   6       8.908  -2.869  34.112  1.00 20.29           C  
-ATOM     55  CD1 TRP A   6       8.439  -1.741  34.823  1.00 24.48           C  
-ATOM     56  CD2 TRP A   6      10.311  -2.758  34.158  1.00 20.08           C  
-ATOM     57  NE1 TRP A   6       9.442  -0.935  35.298  1.00 23.47           N  
-ATOM     58  CE2 TRP A   6      10.619  -1.515  34.915  1.00 18.94           C  
-ATOM     59  CE3 TRP A   6      11.356  -3.535  33.644  1.00 20.78           C  
-ATOM     60  CZ2 TRP A   6      11.950  -1.128  35.112  1.00 20.96           C  
-ATOM     61  CZ3 TRP A   6      12.673  -3.108  33.870  1.00 24.13           C  
-ATOM     62  CH2 TRP A   6      12.967  -1.928  34.588  1.00 24.50           C  
-ATOM     63  H   TRP A   6       6.920  -1.791  32.344  1.00 15.00           H  
-ATOM     64  HE1 TRP A   6       9.339  -0.085  35.779  1.00 15.00           H  
-ATOM     65  N   GLN A   7       5.814  -4.432  31.151  1.00 18.16           N  
-ATOM     66  CA  GLN A   7       4.962  -5.251  30.280  1.00 20.97           C  
-ATOM     67  C   GLN A   7       4.435  -4.518  29.057  1.00 21.12           C  
-ATOM     68  O   GLN A   7       4.388  -3.300  29.056  1.00 23.42           O  
-ATOM     69  CB  GLN A   7       3.716  -5.586  31.013  1.00 24.95           C  
-ATOM     70  CG  GLN A   7       3.979  -6.416  32.242  1.00 39.22           C  
-ATOM     71  CD  GLN A   7       2.813  -6.087  33.129  1.00 47.01           C  
-ATOM     72  OE1 GLN A   7       2.794  -5.111  33.858  1.00 53.83           O  
-ATOM     73  NE2 GLN A   7       1.778  -6.891  33.022  1.00 49.27           N  
-ATOM     74  H   GLN A   7       5.457  -3.641  31.653  1.00 15.00           H  
-ATOM     75 HE21 GLN A   7       0.993  -6.672  33.591  1.00  0.00           H  
-ATOM     76 HE22 GLN A   7       1.763  -7.662  32.395  1.00  0.00           H  
-ATOM     77  N   ARG A   8       3.965  -5.244  28.032  1.00 18.84           N  
-ATOM     78  CA  ARG A   8       3.237  -4.538  26.954  1.00 17.03           C  
-ATOM     79  C   ARG A   8       2.107  -3.611  27.461  1.00 18.95           C  
-ATOM     80  O   ARG A   8       1.327  -4.020  28.310  1.00 19.89           O  
-ATOM     81  CB  ARG A   8       2.617  -5.576  26.013  1.00 15.38           C  
-ATOM     82  CG  ARG A   8       3.669  -6.348  25.258  1.00 15.83           C  
-ATOM     83  CD  ARG A   8       3.094  -7.303  24.238  1.00 21.27           C  
-ATOM     84  NE  ARG A   8       4.178  -8.074  23.616  1.00 25.46           N  
-ATOM     85  CZ  ARG A   8       4.020  -9.380  23.294  1.00 28.12           C  
-ATOM     86  NH1 ARG A   8       2.873 -10.011  23.547  1.00 30.67           N  
-ATOM     87  NH2 ARG A   8       4.997 -10.063  22.689  1.00 28.11           N  
-ATOM     88  H   ARG A   8       4.014  -6.245  28.076  1.00 15.00           H  
-ATOM     89  HE  ARG A   8       5.038  -7.614  23.396  1.00 15.00           H  
-ATOM     90 HH11 ARG A   8       2.128  -9.514  23.988  1.00  0.00           H  
-ATOM     91 HH12 ARG A   8       2.741 -10.980  23.303  1.00  0.00           H  
-ATOM     92 HH21 ARG A   8       5.855  -9.598  22.493  1.00  0.00           H  
-ATOM     93 HH22 ARG A   8       4.900 -11.027  22.411  1.00  0.00           H  
-ATOM     94  N   PRO A   9       2.056  -2.370  26.976  1.00 17.32           N  
-ATOM     95  CA  PRO A   9       1.006  -1.434  27.428  1.00 18.82           C  
-ATOM     96  C   PRO A   9      -0.378  -1.638  26.809  1.00 18.58           C  
-ATOM     97  O   PRO A   9      -0.944  -0.863  26.050  1.00 18.11           O  
-ATOM     98  CB  PRO A   9       1.630  -0.070  27.131  1.00 15.85           C  
-ATOM     99  CG  PRO A   9       2.482  -0.344  25.906  1.00 17.78           C  
-ATOM    100  CD  PRO A   9       3.066  -1.731  26.150  1.00 17.38           C  
-ATOM    101  N   LEU A  10      -0.916  -2.776  27.211  1.00 19.09           N  
-ATOM    102  CA  LEU A  10      -2.258  -3.160  26.791  1.00 21.12           C  
-ATOM    103  C   LEU A  10      -3.359  -2.644  27.658  1.00 23.07           C  
-ATOM    104  O   LEU A  10      -3.399  -2.871  28.850  1.00 27.33           O  
-ATOM    105  CB  LEU A  10      -2.404  -4.661  26.825  1.00 22.81           C  
-ATOM    106  CG  LEU A  10      -1.502  -5.363  25.819  1.00 25.56           C  
-ATOM    107  CD1 LEU A  10      -1.230  -6.815  26.263  1.00 26.30           C  
-ATOM    108  CD2 LEU A  10      -2.086  -5.226  24.413  1.00 23.40           C  
-ATOM    109  H   LEU A  10      -0.398  -3.322  27.873  1.00 15.00           H  
-ATOM    110  N   VAL A  11      -4.289  -1.964  27.036  1.00 21.27           N  
-ATOM    111  CA  VAL A  11      -5.448  -1.541  27.813  1.00 19.07           C  
-ATOM    112  C   VAL A  11      -6.773  -2.027  27.239  1.00 19.15           C  
-ATOM    113  O   VAL A  11      -6.843  -2.622  26.185  1.00 19.07           O  
-ATOM    114  CB  VAL A  11      -5.432  -0.007  27.908  1.00 20.07           C  
-ATOM    115  CG1 VAL A  11      -4.178   0.504  28.638  1.00 20.11           C  
-ATOM    116  CG2 VAL A  11      -5.544   0.636  26.515  1.00 20.26           C  
-ATOM    117  H   VAL A  11      -4.178  -1.770  26.057  1.00 15.00           H  
-ATOM    118  N   THR A  12      -7.842  -1.746  27.963  1.00 19.73           N  
-ATOM    119  CA  THR A  12      -9.200  -2.011  27.447  1.00 21.11           C  
-ATOM    120  C   THR A  12      -9.806  -0.800  26.774  1.00 20.90           C  
-ATOM    121  O   THR A  12      -9.835   0.324  27.254  1.00 20.50           O  
-ATOM    122  CB  THR A  12     -10.186  -2.470  28.561  1.00 24.28           C  
-ATOM    123  OG1 THR A  12      -9.694  -3.683  29.154  1.00 29.75           O  
-ATOM    124  CG2 THR A  12     -11.625  -2.751  28.079  1.00 24.26           C  
-ATOM    125  H   THR A  12      -7.711  -1.263  28.827  1.00 15.00           H  
-ATOM    126  HG1 THR A  12      -9.032  -3.466  29.817  1.00 15.00           H  
-ATOM    127  N   ILE A  13     -10.296  -1.055  25.590  1.00 20.38           N  
-ATOM    128  CA  ILE A  13     -11.019   0.007  24.889  1.00 21.25           C  
-ATOM    129  C   ILE A  13     -12.488  -0.372  24.715  1.00 23.00           C  
-ATOM    130  O   ILE A  13     -12.860  -1.539  24.701  1.00 22.85           O  
-ATOM    131  CB  ILE A  13     -10.347   0.293  23.511  1.00 21.10           C  
-ATOM    132  CG1 ILE A  13     -10.431  -0.887  22.525  1.00 22.00           C  
-ATOM    133  CG2 ILE A  13      -8.879   0.729  23.714  1.00 19.06           C  
-ATOM    134  CD1 ILE A  13      -9.880  -0.636  21.119  1.00 21.87           C  
-ATOM    135  H   ILE A  13     -10.234  -1.989  25.228  1.00 15.00           H  
-ATOM    136  N   LYS A  14     -13.311   0.642  24.570  1.00 23.47           N  
-ATOM    137  CA  LYS A  14     -14.649   0.298  24.078  1.00 25.75           C  
-ATOM    138  C   LYS A  14     -14.990   0.935  22.753  1.00 26.25           C  
-ATOM    139  O   LYS A  14     -14.871   2.134  22.516  1.00 25.77           O  
-ATOM    140  CB  LYS A  14     -15.755   0.642  25.081  1.00 29.28           C  
-ATOM    141  CG  LYS A  14     -17.142   0.166  24.612  1.00 34.08           C  
-ATOM    142  CD  LYS A  14     -18.308   0.698  25.439  1.00 40.14           C  
-ATOM    143  CE  LYS A  14     -18.330   0.313  26.923  1.00 44.70           C  
-ATOM    144  NZ  LYS A  14     -19.603   0.770  27.537  1.00 47.69           N  
-ATOM    145  H   LYS A  14     -12.979   1.577  24.711  1.00  0.00           H  
-ATOM    146  HZ1 LYS A  14     -19.697   1.798  27.409  1.00  0.00           H  
-ATOM    147  HZ2 LYS A  14     -20.403   0.289  27.078  1.00  0.00           H  
-ATOM    148  HZ3 LYS A  14     -19.599   0.544  28.552  1.00  0.00           H  
-ATOM    149  N   ILE A  15     -15.420   0.054  21.873  1.00 28.16           N  
-ATOM    150  CA  ILE A  15     -15.729   0.480  20.518  1.00 27.74           C  
-ATOM    151  C   ILE A  15     -16.903  -0.302  19.966  1.00 30.77           C  
-ATOM    152  O   ILE A  15     -17.018  -1.495  20.184  1.00 29.75           O  
-ATOM    153  CB  ILE A  15     -14.482   0.324  19.614  1.00 28.32           C  
-ATOM    154  CG1 ILE A  15     -14.787   0.904  18.214  1.00 28.69           C  
-ATOM    155  CG2 ILE A  15     -13.959  -1.129  19.557  1.00 24.05           C  
-ATOM    156  CD1 ILE A  15     -13.600   1.205  17.307  1.00 30.55           C  
-ATOM    157  H   ILE A  15     -15.499  -0.908  22.159  1.00 15.00           H  
-ATOM    158  N   GLY A  16     -17.816   0.396  19.280  1.00 32.95           N  
-ATOM    159  CA  GLY A  16     -19.007  -0.294  18.753  1.00 35.00           C  
-ATOM    160  C   GLY A  16     -19.931  -0.934  19.800  1.00 35.90           C  
-ATOM    161  O   GLY A  16     -20.750  -1.786  19.521  1.00 38.10           O  
-ATOM    162  H   GLY A  16     -17.678   1.373  19.096  1.00 15.00           H  
-ATOM    163  N   GLY A  17     -19.753  -0.524  21.060  1.00 37.13           N  
-ATOM    164  CA  GLY A  17     -20.368  -1.291  22.159  1.00 36.08           C  
-ATOM    165  C   GLY A  17     -19.637  -2.569  22.580  1.00 37.27           C  
-ATOM    166  O   GLY A  17     -20.000  -3.297  23.484  1.00 39.17           O  
-ATOM    167  H   GLY A  17     -19.156   0.256  21.243  1.00 15.00           H  
-ATOM    168  N   GLN A  18     -18.553  -2.851  21.896  1.00 36.22           N  
-ATOM    169  CA  GLN A  18     -17.706  -3.957  22.319  1.00 36.25           C  
-ATOM    170  C   GLN A  18     -16.500  -3.557  23.167  1.00 32.62           C  
-ATOM    171  O   GLN A  18     -15.882  -2.510  23.041  1.00 30.71           O  
-ATOM    172  CB  GLN A  18     -17.210  -4.703  21.058  1.00 43.17           C  
-ATOM    173  CG  GLN A  18     -18.214  -5.632  20.341  1.00 53.19           C  
-ATOM    174  CD  GLN A  18     -18.417  -6.960  21.085  1.00 59.72           C  
-ATOM    175  OE1 GLN A  18     -17.991  -8.049  20.710  1.00 63.24           O  
-ATOM    176  NE2 GLN A  18     -19.071  -6.879  22.228  1.00 62.41           N  
-ATOM    177  H   GLN A  18     -18.261  -2.263  21.142  1.00 15.00           H  
-ATOM    178 HE21 GLN A  18     -18.881  -7.537  22.957  1.00  0.00           H  
-ATOM    179 HE22 GLN A  18     -19.659  -6.099  22.440  1.00  0.00           H  
-ATOM    180  N   LEU A  19     -16.170  -4.481  24.037  1.00 27.59           N  
-ATOM    181  CA  LEU A  19     -14.924  -4.345  24.793  1.00 27.59           C  
-ATOM    182  C   LEU A  19     -13.715  -5.055  24.153  1.00 26.57           C  
-ATOM    183  O   LEU A  19     -13.770  -6.227  23.817  1.00 29.44           O  
-ATOM    184  CB  LEU A  19     -15.208  -4.924  26.192  1.00 27.95           C  
-ATOM    185  CG  LEU A  19     -15.140  -3.972  27.385  1.00 31.29           C  
-ATOM    186  CD1 LEU A  19     -15.994  -2.711  27.240  1.00 26.44           C  
-ATOM    187  CD2 LEU A  19     -15.470  -4.766  28.645  1.00 30.76           C  
-ATOM    188  H   LEU A  19     -16.734  -5.302  24.108  1.00 15.00           H  
-ATOM    189  N   LYS A  20     -12.618  -4.341  23.976  1.00 23.16           N  
-ATOM    190  CA  LYS A  20     -11.430  -5.031  23.457  1.00 21.60           C  
-ATOM    191  C   LYS A  20     -10.176  -4.633  24.156  1.00 19.25           C  
-ATOM    192  O   LYS A  20     -10.139  -3.669  24.886  1.00 22.22           O  
-ATOM    193  CB  LYS A  20     -11.186  -4.707  21.986  1.00 22.70           C  
-ATOM    194  CG  LYS A  20     -12.259  -5.310  21.106  1.00 28.02           C  
-ATOM    195  CD  LYS A  20     -12.138  -4.943  19.637  1.00 34.55           C  
-ATOM    196  CE  LYS A  20     -13.158  -5.770  18.848  1.00 38.32           C  
-ATOM    197  NZ  LYS A  20     -12.856  -7.215  18.931  1.00 38.41           N  
-ATOM    198  H   LYS A  20     -12.623  -3.365  24.213  1.00 15.00           H  
-ATOM    199  HZ1 LYS A  20     -12.818  -7.513  19.927  1.00 15.00           H  
-ATOM    200  HZ2 LYS A  20     -13.599  -7.751  18.438  1.00 15.00           H  
-ATOM    201  HZ3 LYS A  20     -11.940  -7.401  18.477  1.00 15.00           H  
-ATOM    202  N   GLU A  21      -9.132  -5.370  23.912  1.00 17.94           N  
-ATOM    203  CA  GLU A  21      -7.836  -4.921  24.417  1.00 21.77           C  
-ATOM    204  C   GLU A  21      -6.957  -4.348  23.351  1.00 19.58           C  
-ATOM    205  O   GLU A  21      -6.912  -4.846  22.246  1.00 21.01           O  
-ATOM    206  CB  GLU A  21      -7.007  -6.062  24.949  1.00 24.02           C  
-ATOM    207  CG  GLU A  21      -7.542  -6.489  26.287  1.00 39.23           C  
-ATOM    208  CD  GLU A  21      -6.360  -6.839  27.146  1.00 47.75           C  
-ATOM    209  OE1 GLU A  21      -5.430  -7.481  26.621  1.00 50.96           O  
-ATOM    210  OE2 GLU A  21      -6.375  -6.451  28.329  1.00 51.74           O  
-ATOM    211  H   GLU A  21      -9.241  -6.199  23.359  1.00 15.00           H  
-ATOM    212  N   ALA A  22      -6.236  -3.315  23.683  1.00 17.57           N  
-ATOM    213  CA  ALA A  22      -5.373  -2.754  22.654  1.00 16.56           C  
-ATOM    214  C   ALA A  22      -4.042  -2.250  23.152  1.00 17.33           C  
-ATOM    215  O   ALA A  22      -3.870  -1.927  24.321  1.00 18.74           O  
-ATOM    216  CB  ALA A  22      -6.067  -1.617  21.905  1.00 14.48           C  
-ATOM    217  H   ALA A  22      -6.330  -2.923  24.600  1.00 15.00           H  
-ATOM    218  N   LEU A  23      -3.094  -2.188  22.228  1.00 16.02           N  
-ATOM    219  CA  LEU A  23      -1.748  -1.723  22.595  1.00 15.62           C  
-ATOM    220  C   LEU A  23      -1.576  -0.232  22.417  1.00 15.90           C  
-ATOM    221  O   LEU A  23      -1.807   0.306  21.343  1.00 15.71           O  
-ATOM    222  CB  LEU A  23      -0.761  -2.451  21.681  1.00 14.95           C  
-ATOM    223  CG  LEU A  23       0.752  -2.261  21.844  1.00 17.32           C  
-ATOM    224  CD1 LEU A  23       1.302  -3.007  23.067  1.00 16.53           C  
-ATOM    225  CD2 LEU A  23       1.438  -2.825  20.586  1.00 18.55           C  
-ATOM    226  H   LEU A  23      -3.311  -2.454  21.285  1.00 15.00           H  
-ATOM    227  N   LEU A  24      -1.154   0.431  23.487  1.00 14.38           N  
-ATOM    228  CA  LEU A  24      -0.826   1.848  23.297  1.00 15.18           C  
-ATOM    229  C   LEU A  24       0.534   2.084  22.622  1.00 14.34           C  
-ATOM    230  O   LEU A  24       1.599   1.787  23.150  1.00 13.20           O  
-ATOM    231  CB  LEU A  24      -0.862   2.546  24.669  1.00 18.16           C  
-ATOM    232  CG  LEU A  24      -2.183   2.389  25.423  1.00 18.31           C  
-ATOM    233  CD1 LEU A  24      -2.079   3.087  26.786  1.00 21.66           C  
-ATOM    234  CD2 LEU A  24      -3.309   2.986  24.608  1.00 19.29           C  
-ATOM    235  H   LEU A  24      -1.060  -0.040  24.370  1.00 15.00           H  
-ATOM    236  N   ASP A  25       0.475   2.580  21.393  1.00 12.60           N  
-ATOM    237  CA  ASP A  25       1.676   2.485  20.575  1.00 12.76           C  
-ATOM    238  C   ASP A  25       2.184   3.803  20.035  1.00 15.30           C  
-ATOM    239  O   ASP A  25       1.771   4.298  19.004  1.00 14.22           O  
-ATOM    240  CB  ASP A  25       1.337   1.515  19.445  1.00 15.16           C  
-ATOM    241  CG  ASP A  25       2.511   1.076  18.571  1.00 18.23           C  
-ATOM    242  OD1 ASP A  25       3.667   1.441  18.783  1.00 15.70           O  
-ATOM    243  OD2 ASP A  25       2.231   0.324  17.658  1.00 19.69           O  
-ATOM    244  H   ASP A  25      -0.405   2.860  20.992  1.00 15.00           H  
-ATOM    245  N   THR A  26       3.176   4.363  20.735  1.00 13.74           N  
-ATOM    246  CA  THR A  26       3.747   5.618  20.243  1.00 13.76           C  
-ATOM    247  C   THR A  26       4.504   5.535  18.906  1.00 14.95           C  
-ATOM    248  O   THR A  26       4.746   6.505  18.218  1.00 14.86           O  
-ATOM    249  CB  THR A  26       4.662   6.215  21.294  1.00 12.03           C  
-ATOM    250  OG1 THR A  26       5.746   5.308  21.512  1.00 12.58           O  
-ATOM    251  CG2 THR A  26       3.900   6.448  22.605  1.00 10.10           C  
-ATOM    252  H   THR A  26       3.463   3.957  21.607  1.00 15.00           H  
-ATOM    253  HG1 THR A  26       6.582   5.775  21.348  1.00 15.00           H  
-ATOM    254  N   GLY A  27       4.845   4.315  18.521  1.00 14.85           N  
-ATOM    255  CA  GLY A  27       5.491   4.116  17.214  1.00 14.02           C  
-ATOM    256  C   GLY A  27       4.585   3.876  16.037  1.00 15.06           C  
-ATOM    257  O   GLY A  27       5.010   3.549  14.946  1.00 16.22           O  
-ATOM    258  H   GLY A  27       4.621   3.558  19.126  1.00 15.00           H  
-ATOM    259  N   ALA A  28       3.297   4.039  16.279  1.00 13.90           N  
-ATOM    260  CA  ALA A  28       2.337   3.976  15.182  1.00 15.29           C  
-ATOM    261  C   ALA A  28       1.673   5.330  14.889  1.00 15.47           C  
-ATOM    262  O   ALA A  28       1.155   6.011  15.767  1.00 15.23           O  
-ATOM    263  CB  ALA A  28       1.223   2.960  15.460  1.00 12.70           C  
-ATOM    264  H   ALA A  28       2.981   4.272  17.201  1.00 15.00           H  
-ATOM    265  N   ASP A  29       1.659   5.708  13.610  1.00 13.14           N  
-ATOM    266  CA  ASP A  29       0.883   6.915  13.298  1.00 12.62           C  
-ATOM    267  C   ASP A  29      -0.636   6.738  13.375  1.00 13.03           C  
-ATOM    268  O   ASP A  29      -1.388   7.623  13.728  1.00 15.20           O  
-ATOM    269  CB  ASP A  29       1.129   7.374  11.866  1.00 14.81           C  
-ATOM    270  CG  ASP A  29       2.518   7.902  11.605  1.00 18.38           C  
-ATOM    271  OD1 ASP A  29       3.383   7.845  12.461  1.00 17.61           O  
-ATOM    272  OD2 ASP A  29       2.719   8.388  10.506  1.00 21.07           O  
-ATOM    273  H   ASP A  29       2.193   5.189  12.934  1.00 15.00           H  
-ATOM    274  N   ASP A  30      -1.072   5.541  13.018  1.00 13.43           N  
-ATOM    275  CA  ASP A  30      -2.505   5.278  12.941  1.00 14.59           C  
-ATOM    276  C   ASP A  30      -2.968   4.147  13.849  1.00 14.15           C  
-ATOM    277  O   ASP A  30      -2.221   3.366  14.397  1.00 15.25           O  
-ATOM    278  CB  ASP A  30      -2.862   4.866  11.505  1.00 17.85           C  
-ATOM    279  CG  ASP A  30      -2.384   5.891  10.479  1.00 21.13           C  
-ATOM    280  OD1 ASP A  30      -2.964   6.959  10.399  1.00 23.45           O  
-ATOM    281  OD2 ASP A  30      -1.409   5.626   9.781  1.00 26.19           O  
-ATOM    282  H   ASP A  30      -0.403   4.839  12.783  1.00 15.00           H  
-ATOM    283  N   THR A  31      -4.266   4.108  13.987  1.00 14.92           N  
-ATOM    284  CA  THR A  31      -4.988   3.097  14.770  1.00 14.80           C  
-ATOM    285  C   THR A  31      -5.549   2.027  13.853  1.00 15.76           C  
-ATOM    286  O   THR A  31      -6.324   2.260  12.928  1.00 16.17           O  
-ATOM    287  CB  THR A  31      -6.150   3.756  15.611  1.00 13.09           C  
-ATOM    288  OG1 THR A  31      -5.577   4.717  16.518  1.00 15.14           O  
-ATOM    289  CG2 THR A  31      -7.026   2.778  16.399  1.00  9.96           C  
-ATOM    290  H   THR A  31      -4.785   4.800  13.481  1.00 15.00           H  
-ATOM    291  HG1 THR A  31      -5.220   5.466  16.018  1.00 15.00           H  
-ATOM    292  N   VAL A  32      -5.060   0.831  14.167  1.00 17.42           N  
-ATOM    293  CA  VAL A  32      -5.405  -0.408  13.468  1.00 17.43           C  
-ATOM    294  C   VAL A  32      -6.015  -1.474  14.380  1.00 17.60           C  
-ATOM    295  O   VAL A  32      -5.389  -2.001  15.285  1.00 18.16           O  
-ATOM    296  CB  VAL A  32      -4.176  -1.018  12.784  1.00 16.74           C  
-ATOM    297  CG1 VAL A  32      -4.641  -1.997  11.694  1.00 18.49           C  
-ATOM    298  CG2 VAL A  32      -3.322   0.041  12.143  1.00 20.85           C  
-ATOM    299  H   VAL A  32      -4.453   0.785  14.963  1.00 15.00           H  
-ATOM    300  N   LEU A  33      -7.275  -1.777  14.115  1.00 16.37           N  
-ATOM    301  CA  LEU A  33      -7.931  -2.868  14.830  1.00 16.93           C  
-ATOM    302  C   LEU A  33      -8.152  -4.146  14.042  1.00 17.32           C  
-ATOM    303  O   LEU A  33      -8.262  -4.202  12.828  1.00 15.96           O  
-ATOM    304  CB  LEU A  33      -9.268  -2.378  15.338  1.00 17.15           C  
-ATOM    305  CG  LEU A  33      -9.104  -1.085  16.123  1.00 19.31           C  
-ATOM    306  CD1 LEU A  33     -10.501  -0.645  16.461  1.00 20.23           C  
-ATOM    307  CD2 LEU A  33      -8.207  -1.200  17.373  1.00 20.16           C  
-ATOM    308  H   LEU A  33      -7.745  -1.300  13.371  1.00 15.00           H  
-ATOM    309  N   GLU A  34      -8.213  -5.222  14.780  1.00 18.22           N  
-ATOM    310  CA  GLU A  34      -8.632  -6.450  14.122  1.00 24.06           C  
-ATOM    311  C   GLU A  34      -9.985  -6.397  13.410  1.00 24.12           C  
-ATOM    312  O   GLU A  34     -10.887  -5.628  13.695  1.00 19.86           O  
-ATOM    313  CB  GLU A  34      -8.625  -7.586  15.160  1.00 29.24           C  
-ATOM    314  CG  GLU A  34      -9.823  -7.606  16.152  1.00 38.60           C  
-ATOM    315  CD  GLU A  34      -9.409  -8.198  17.507  1.00 43.19           C  
-ATOM    316  OE1 GLU A  34      -8.313  -8.783  17.621  1.00 44.63           O  
-ATOM    317  OE2 GLU A  34     -10.180  -8.030  18.460  1.00 43.27           O  
-ATOM    318  H   GLU A  34      -8.062  -5.160  15.771  1.00 15.00           H  
-ATOM    319  N   GLU A  35     -10.089  -7.276  12.432  1.00 27.02           N  
-ATOM    320  CA  GLU A  35     -11.366  -7.441  11.741  1.00 32.40           C  
-ATOM    321  C   GLU A  35     -12.638  -7.437  12.593  1.00 31.82           C  
-ATOM    322  O   GLU A  35     -12.918  -8.279  13.414  1.00 33.89           O  
-ATOM    323  CB  GLU A  35     -11.328  -8.746  10.948  1.00 37.09           C  
-ATOM    324  CG  GLU A  35     -10.219  -8.883   9.893  1.00 46.83           C  
-ATOM    325  CD  GLU A  35     -10.526  -8.078   8.653  1.00 52.89           C  
-ATOM    326  OE1 GLU A  35     -11.627  -7.518   8.545  1.00 55.39           O  
-ATOM    327  OE2 GLU A  35      -9.650  -8.030   7.787  1.00 56.66           O  
-ATOM    328  H   GLU A  35      -9.295  -7.852  12.223  1.00 15.00           H  
-ATOM    329  N   MET A  36     -13.434  -6.434  12.347  1.00 32.69           N  
-ATOM    330  CA  MET A  36     -14.773  -6.376  12.924  1.00 32.66           C  
-ATOM    331  C   MET A  36     -15.732  -5.585  12.039  1.00 35.24           C  
-ATOM    332  O   MET A  36     -15.372  -4.845  11.114  1.00 34.96           O  
-ATOM    333  CB  MET A  36     -14.683  -5.720  14.313  1.00 32.39           C  
-ATOM    334  CG  MET A  36     -14.279  -4.244  14.280  1.00 34.33           C  
-ATOM    335  SD  MET A  36     -13.897  -3.543  15.895  1.00 35.03           S  
-ATOM    336  CE  MET A  36     -15.532  -3.781  16.608  1.00 38.56           C  
-ATOM    337  H   MET A  36     -12.999  -5.636  11.944  1.00 15.00           H  
-ATOM    338  N   SER A  37     -17.003  -5.778  12.323  1.00 36.16           N  
-ATOM    339  CA  SER A  37     -17.987  -4.927  11.637  1.00 36.42           C  
-ATOM    340  C   SER A  37     -18.354  -3.717  12.435  1.00 35.67           C  
-ATOM    341  O   SER A  37     -18.817  -3.747  13.554  1.00 36.42           O  
-ATOM    342  CB  SER A  37     -19.277  -5.681  11.305  1.00 37.87           C  
-ATOM    343  OG  SER A  37     -19.613  -6.593  12.366  1.00 43.60           O  
-ATOM    344  H   SER A  37     -17.304  -6.398  13.049  1.00  0.00           H  
-ATOM    345  HG  SER A  37     -20.406  -6.292  12.835  1.00  0.00           H  
-ATOM    346  N   LEU A  38     -18.069  -2.611  11.813  1.00 35.20           N  
-ATOM    347  CA  LEU A  38     -18.454  -1.365  12.459  1.00 35.46           C  
-ATOM    348  C   LEU A  38     -19.546  -0.760  11.611  1.00 36.89           C  
-ATOM    349  O   LEU A  38     -19.567  -0.946  10.400  1.00 37.01           O  
-ATOM    350  CB  LEU A  38     -17.228  -0.425  12.515  1.00 32.66           C  
-ATOM    351  CG  LEU A  38     -16.160  -0.787  13.555  1.00 31.46           C  
-ATOM    352  CD1 LEU A  38     -14.934   0.113  13.417  1.00 26.05           C  
-ATOM    353  CD2 LEU A  38     -16.748  -0.704  14.966  1.00 28.65           C  
-ATOM    354  H   LEU A  38     -17.695  -2.606  10.890  1.00 15.00           H  
-ATOM    355  N   PRO A  39     -20.471  -0.057  12.243  1.00 38.86           N  
-ATOM    356  CA  PRO A  39     -21.420   0.655  11.391  1.00 41.54           C  
-ATOM    357  C   PRO A  39     -20.805   1.897  10.688  1.00 41.71           C  
-ATOM    358  O   PRO A  39     -19.957   2.633  11.166  1.00 43.42           O  
-ATOM    359  CB  PRO A  39     -22.564   0.883  12.401  1.00 41.58           C  
-ATOM    360  CG  PRO A  39     -21.868   1.085  13.748  1.00 41.49           C  
-ATOM    361  CD  PRO A  39     -20.697   0.112  13.675  1.00 40.05           C  
-ATOM    362  N   GLY A  40     -21.255   2.105   9.465  1.00 40.87           N  
-ATOM    363  CA  GLY A  40     -20.631   3.191   8.715  1.00 38.39           C  
-ATOM    364  C   GLY A  40     -20.157   2.804   7.333  1.00 37.72           C  
-ATOM    365  O   GLY A  40     -19.980   1.662   6.949  1.00 34.49           O  
-ATOM    366  H   GLY A  40     -21.920   1.472   9.078  1.00 15.00           H  
-ATOM    367  N   ARG A  41     -19.961   3.848   6.567  1.00 38.11           N  
-ATOM    368  CA  ARG A  41     -19.310   3.544   5.297  1.00 41.68           C  
-ATOM    369  C   ARG A  41     -17.795   3.437   5.468  1.00 39.34           C  
-ATOM    370  O   ARG A  41     -17.238   4.045   6.369  1.00 40.11           O  
-ATOM    371  CB  ARG A  41     -19.600   4.676   4.307  1.00 48.37           C  
-ATOM    372  CG  ARG A  41     -21.080   4.957   3.978  1.00 58.44           C  
-ATOM    373  CD  ARG A  41     -21.786   5.971   4.897  1.00 65.88           C  
-ATOM    374  NE  ARG A  41     -22.892   5.357   5.643  1.00 72.49           N  
-ATOM    375  CZ  ARG A  41     -22.997   5.516   6.970  1.00 76.21           C  
-ATOM    376  NH1 ARG A  41     -22.095   6.267   7.639  1.00 77.52           N  
-ATOM    377  NH2 ARG A  41     -24.018   4.891   7.580  1.00 77.49           N  
-ATOM    378  H   ARG A  41     -20.004   4.770   6.937  1.00  0.00           H  
-ATOM    379  HE  ARG A  41     -23.569   4.808   5.153  1.00  0.00           H  
-ATOM    380 HH11 ARG A  41     -21.338   6.676   7.128  1.00  0.00           H  
-ATOM    381 HH12 ARG A  41     -22.149   6.444   8.626  1.00  0.00           H  
-ATOM    382 HH21 ARG A  41     -24.668   4.397   7.004  1.00  0.00           H  
-ATOM    383 HH22 ARG A  41     -24.163   4.871   8.574  1.00  0.00           H  
-ATOM    384  N   TRP A  42     -17.132   2.687   4.606  1.00 35.94           N  
-ATOM    385  CA  TRP A  42     -15.667   2.666   4.705  1.00 32.22           C  
-ATOM    386  C   TRP A  42     -14.941   2.713   3.368  1.00 32.38           C  
-ATOM    387  O   TRP A  42     -15.490   2.410   2.320  1.00 34.44           O  
-ATOM    388  CB  TRP A  42     -15.200   1.443   5.524  1.00 29.79           C  
-ATOM    389  CG  TRP A  42     -15.587   0.161   4.827  1.00 28.83           C  
-ATOM    390  CD1 TRP A  42     -16.777  -0.547   5.032  1.00 28.82           C  
-ATOM    391  CD2 TRP A  42     -14.891  -0.570   3.848  1.00 26.94           C  
-ATOM    392  NE1 TRP A  42     -16.871  -1.661   4.268  1.00 27.77           N  
-ATOM    393  CE2 TRP A  42     -15.739  -1.739   3.513  1.00 27.44           C  
-ATOM    394  CE3 TRP A  42     -13.665  -0.412   3.191  1.00 30.38           C  
-ATOM    395  CZ2 TRP A  42     -15.301  -2.663   2.550  1.00 27.39           C  
-ATOM    396  CZ3 TRP A  42     -13.249  -1.355   2.228  1.00 30.86           C  
-ATOM    397  CH2 TRP A  42     -14.059  -2.464   1.920  1.00 31.62           C  
-ATOM    398  H   TRP A  42     -17.616   2.133   3.934  1.00 15.00           H  
-ATOM    399  HE1 TRP A  42     -17.619  -2.295   4.278  1.00 15.00           H  
-ATOM    400  N   LYS A  43     -13.673   3.075   3.424  1.00 31.27           N  
-ATOM    401  CA  LYS A  43     -12.873   3.050   2.179  1.00 31.37           C  
-ATOM    402  C   LYS A  43     -11.705   2.114   2.278  1.00 27.96           C  
-ATOM    403  O   LYS A  43     -11.090   2.018   3.324  1.00 24.17           O  
-ATOM    404  CB  LYS A  43     -12.225   4.398   1.868  1.00 34.98           C  
-ATOM    405  CG  LYS A  43     -13.252   5.522   1.867  1.00 45.60           C  
-ATOM    406  CD  LYS A  43     -12.911   6.622   2.892  1.00 50.00           C  
-ATOM    407  CE  LYS A  43     -14.165   7.431   3.239  1.00 54.08           C  
-ATOM    408  NZ  LYS A  43     -13.734   8.661   3.912  1.00 55.79           N  
-ATOM    409  H   LYS A  43     -13.294   3.345   4.312  1.00 15.00           H  
-ATOM    410  HZ1 LYS A  43     -13.052   9.161   3.306  1.00 15.00           H  
-ATOM    411  HZ2 LYS A  43     -14.557   9.273   4.083  1.00 15.00           H  
-ATOM    412  HZ3 LYS A  43     -13.281   8.422   4.816  1.00 15.00           H  
-ATOM    413  N   PRO A  44     -11.397   1.438   1.177  1.00 26.46           N  
-ATOM    414  CA  PRO A  44     -10.175   0.621   1.188  1.00 26.52           C  
-ATOM    415  C   PRO A  44      -8.912   1.471   1.372  1.00 25.22           C  
-ATOM    416  O   PRO A  44      -8.751   2.501   0.738  1.00 27.91           O  
-ATOM    417  CB  PRO A  44     -10.178   0.013  -0.233  1.00 26.27           C  
-ATOM    418  CG  PRO A  44     -11.588   0.166  -0.795  1.00 26.18           C  
-ATOM    419  CD  PRO A  44     -12.098   1.425  -0.112  1.00 26.69           C  
-ATOM    420  N   LYS A  45      -8.006   1.021   2.212  1.00 22.19           N  
-ATOM    421  CA  LYS A  45      -6.709   1.678   2.287  1.00 19.92           C  
-ATOM    422  C   LYS A  45      -5.579   0.687   2.411  1.00 19.37           C  
-ATOM    423  O   LYS A  45      -5.791  -0.466   2.728  1.00 20.06           O  
-ATOM    424  CB  LYS A  45      -6.719   2.573   3.515  1.00 24.14           C  
-ATOM    425  CG  LYS A  45      -5.823   3.789   3.345  1.00 32.72           C  
-ATOM    426  CD  LYS A  45      -5.680   4.576   4.645  1.00 39.30           C  
-ATOM    427  CE  LYS A  45      -4.467   4.205   5.508  1.00 43.97           C  
-ATOM    428  NZ  LYS A  45      -3.241   4.881   5.027  1.00 46.94           N  
-ATOM    429  H   LYS A  45      -8.235   0.249   2.813  1.00 15.00           H  
-ATOM    430  HZ1 LYS A  45      -3.085   4.632   4.029  1.00 15.00           H  
-ATOM    431  HZ2 LYS A  45      -3.352   5.911   5.116  1.00 15.00           H  
-ATOM    432  HZ3 LYS A  45      -2.426   4.569   5.593  1.00 15.00           H  
-ATOM    433  N   MET A  46      -4.365   1.146   2.187  1.00 19.78           N  
-ATOM    434  CA  MET A  46      -3.195   0.332   2.550  1.00 23.88           C  
-ATOM    435  C   MET A  46      -2.380   0.977   3.652  1.00 22.42           C  
-ATOM    436  O   MET A  46      -2.183   2.180   3.656  1.00 22.70           O  
-ATOM    437  CB  MET A  46      -2.148   0.233   1.436  1.00 26.24           C  
-ATOM    438  CG  MET A  46      -2.672  -0.252   0.091  1.00 35.20           C  
-ATOM    439  SD  MET A  46      -2.906  -2.009   0.093  1.00 42.53           S  
-ATOM    440  CE  MET A  46      -1.157  -2.384   0.129  1.00 39.84           C  
-ATOM    441  H   MET A  46      -4.257   2.075   1.843  1.00 15.00           H  
-ATOM    442  N   ILE A  47      -1.888   0.157   4.568  1.00 21.26           N  
-ATOM    443  CA  ILE A  47      -0.874   0.661   5.517  1.00 20.93           C  
-ATOM    444  C   ILE A  47       0.253  -0.323   5.711  1.00 19.34           C  
-ATOM    445  O   ILE A  47       0.118  -1.524   5.538  1.00 20.88           O  
-ATOM    446  CB  ILE A  47      -1.407   1.007   6.914  1.00 23.38           C  
-ATOM    447  CG1 ILE A  47      -2.519   0.094   7.342  1.00 26.63           C  
-ATOM    448  CG2 ILE A  47      -1.837   2.453   7.112  1.00 25.99           C  
-ATOM    449  CD1 ILE A  47      -1.927  -0.968   8.237  1.00 26.52           C  
-ATOM    450  H   ILE A  47      -2.173  -0.806   4.550  1.00 15.00           H  
-ATOM    451  N   GLY A  48       1.383   0.242   6.036  1.00 16.51           N  
-ATOM    452  CA  GLY A  48       2.583  -0.568   6.129  1.00 17.32           C  
-ATOM    453  C   GLY A  48       3.273  -0.530   7.471  1.00 18.37           C  
-ATOM    454  O   GLY A  48       3.063   0.316   8.330  1.00 17.37           O  
-ATOM    455  H   GLY A  48       1.390   1.221   6.240  1.00 15.00           H  
-ATOM    456  N   GLY A  49       4.144  -1.495   7.581  1.00 18.76           N  
-ATOM    457  CA  GLY A  49       5.085  -1.483   8.698  1.00 19.95           C  
-ATOM    458  C   GLY A  49       6.200  -2.487   8.475  1.00 21.05           C  
-ATOM    459  O   GLY A  49       6.551  -2.813   7.353  1.00 21.58           O  
-ATOM    460  H   GLY A  49       4.139  -2.226   6.893  1.00 15.00           H  
-ATOM    461  N   ILE A  50       6.738  -3.048   9.544  1.00 20.56           N  
-ATOM    462  CA  ILE A  50       7.680  -4.156   9.353  1.00 21.91           C  
-ATOM    463  C   ILE A  50       7.004  -5.325   8.643  1.00 22.35           C  
-ATOM    464  O   ILE A  50       5.877  -5.743   8.887  1.00 23.80           O  
-ATOM    465  CB  ILE A  50       8.211  -4.613  10.722  1.00 21.88           C  
-ATOM    466  CG1 ILE A  50       9.085  -3.580  11.431  1.00 22.61           C  
-ATOM    467  CG2 ILE A  50       8.964  -5.940  10.648  1.00 23.95           C  
-ATOM    468  CD1 ILE A  50      10.508  -3.439  10.869  1.00 22.61           C  
-ATOM    469  H   ILE A  50       6.398  -2.789  10.450  1.00 15.00           H  
-ATOM    470  N   GLY A  51       7.739  -5.800   7.678  1.00 23.68           N  
-ATOM    471  CA  GLY A  51       7.178  -6.931   6.943  1.00 23.00           C  
-ATOM    472  C   GLY A  51       6.443  -6.590   5.675  1.00 23.90           C  
-ATOM    473  O   GLY A  51       6.284  -7.419   4.802  1.00 26.78           O  
-ATOM    474  H   GLY A  51       8.609  -5.368   7.441  1.00 15.00           H  
-ATOM    475  N   GLY A  52       5.992  -5.341   5.596  1.00 22.20           N  
-ATOM    476  CA  GLY A  52       5.253  -4.917   4.411  1.00 21.13           C  
-ATOM    477  C   GLY A  52       3.914  -4.232   4.658  1.00 21.76           C  
-ATOM    478  O   GLY A  52       3.671  -3.558   5.656  1.00 20.75           O  
-ATOM    479  H   GLY A  52       6.184  -4.693   6.335  1.00 15.00           H  
-ATOM    480  N   PHE A  53       3.057  -4.404   3.657  1.00 20.28           N  
-ATOM    481  CA  PHE A  53       1.760  -3.691   3.590  1.00 19.38           C  
-ATOM    482  C   PHE A  53       0.582  -4.607   3.793  1.00 20.39           C  
-ATOM    483  O   PHE A  53       0.564  -5.742   3.335  1.00 20.69           O  
-ATOM    484  CB  PHE A  53       1.515  -3.043   2.206  1.00 17.92           C  
-ATOM    485  CG  PHE A  53       2.393  -1.843   2.000  1.00 16.41           C  
-ATOM    486  CD1 PHE A  53       3.675  -2.002   1.457  1.00 17.28           C  
-ATOM    487  CD2 PHE A  53       1.940  -0.574   2.433  1.00 21.52           C  
-ATOM    488  CE1 PHE A  53       4.528  -0.885   1.361  1.00 20.60           C  
-ATOM    489  CE2 PHE A  53       2.799   0.547   2.337  1.00 23.48           C  
-ATOM    490  CZ  PHE A  53       4.100   0.389   1.800  1.00 19.13           C  
-ATOM    491  H   PHE A  53       3.321  -5.025   2.917  1.00 15.00           H  
-ATOM    492  N   ILE A  54      -0.428  -4.073   4.474  1.00 20.17           N  
-ATOM    493  CA  ILE A  54      -1.699  -4.786   4.475  1.00 18.57           C  
-ATOM    494  C   ILE A  54      -2.854  -3.934   3.968  1.00 18.56           C  
-ATOM    495  O   ILE A  54      -2.840  -2.713   3.948  1.00 19.42           O  
-ATOM    496  CB  ILE A  54      -2.022  -5.360   5.877  1.00 19.94           C  
-ATOM    497  CG1 ILE A  54      -2.126  -4.310   6.968  1.00 17.69           C  
-ATOM    498  CG2 ILE A  54      -1.012  -6.425   6.302  1.00 20.12           C  
-ATOM    499  CD1 ILE A  54      -2.842  -4.794   8.227  1.00 19.46           C  
-ATOM    500  H   ILE A  54      -0.315  -3.177   4.914  1.00 15.00           H  
-ATOM    501  N   LYS A  55      -3.888  -4.616   3.544  1.00 21.29           N  
-ATOM    502  CA  LYS A  55      -5.103  -3.863   3.191  1.00 21.50           C  
-ATOM    503  C   LYS A  55      -6.060  -3.749   4.343  1.00 19.47           C  
-ATOM    504  O   LYS A  55      -6.360  -4.716   5.039  1.00 19.33           O  
-ATOM    505  CB  LYS A  55      -5.866  -4.554   2.058  1.00 26.74           C  
-ATOM    506  CG  LYS A  55      -5.003  -4.719   0.805  1.00 32.55           C  
-ATOM    507  CD  LYS A  55      -5.617  -5.620  -0.276  1.00 36.84           C  
-ATOM    508  CE  LYS A  55      -6.901  -5.069  -0.893  1.00 38.29           C  
-ATOM    509  NZ  LYS A  55      -7.327  -6.026  -1.922  1.00 43.39           N  
-ATOM    510  H   LYS A  55      -3.862  -5.618   3.536  1.00 15.00           H  
-ATOM    511  HZ1 LYS A  55      -7.448  -6.964  -1.487  1.00 15.00           H  
-ATOM    512  HZ2 LYS A  55      -8.230  -5.719  -2.336  1.00 15.00           H  
-ATOM    513  HZ3 LYS A  55      -6.602  -6.085  -2.665  1.00 15.00           H  
-ATOM    514  N   VAL A  56      -6.498  -2.519   4.533  1.00 18.56           N  
-ATOM    515  CA  VAL A  56      -7.434  -2.236   5.626  1.00 18.30           C  
-ATOM    516  C   VAL A  56      -8.708  -1.492   5.204  1.00 19.26           C  
-ATOM    517  O   VAL A  56      -8.771  -0.821   4.185  1.00 21.37           O  
-ATOM    518  CB  VAL A  56      -6.704  -1.427   6.708  1.00 18.08           C  
-ATOM    519  CG1 VAL A  56      -5.663  -2.295   7.413  1.00 16.36           C  
-ATOM    520  CG2 VAL A  56      -6.135  -0.107   6.166  1.00 18.39           C  
-ATOM    521  H   VAL A  56      -6.188  -1.796   3.908  1.00 15.00           H  
-ATOM    522  N   ARG A  57      -9.738  -1.602   6.020  1.00 19.17           N  
-ATOM    523  CA  ARG A  57     -10.909  -0.748   5.802  1.00 19.84           C  
-ATOM    524  C   ARG A  57     -10.813   0.483   6.651  1.00 20.81           C  
-ATOM    525  O   ARG A  57     -10.619   0.422   7.853  1.00 21.36           O  
-ATOM    526  CB  ARG A  57     -12.201  -1.440   6.239  1.00 22.79           C  
-ATOM    527  CG  ARG A  57     -12.500  -2.771   5.555  1.00 28.72           C  
-ATOM    528  CD  ARG A  57     -13.858  -3.292   6.032  1.00 35.43           C  
-ATOM    529  NE  ARG A  57     -13.748  -4.602   6.663  1.00 43.69           N  
-ATOM    530  CZ  ARG A  57     -14.161  -4.801   7.933  1.00 48.39           C  
-ATOM    531  NH1 ARG A  57     -14.728  -3.800   8.640  1.00 49.31           N  
-ATOM    532  NH2 ARG A  57     -13.996  -6.018   8.484  1.00 49.29           N  
-ATOM    533  H   ARG A  57      -9.658  -2.197   6.821  1.00 15.00           H  
-ATOM    534  HE  ARG A  57     -13.339  -5.357   6.150  1.00 15.00           H  
-ATOM    535 HH11 ARG A  57     -14.853  -2.908   8.206  1.00  0.00           H  
-ATOM    536 HH12 ARG A  57     -15.033  -3.913   9.593  1.00  0.00           H  
-ATOM    537 HH21 ARG A  57     -13.566  -6.745   7.949  1.00  0.00           H  
-ATOM    538 HH22 ARG A  57     -14.296  -6.210   9.419  1.00  0.00           H  
-ATOM    539  N   GLN A  58     -10.938   1.617   6.020  1.00 20.12           N  
-ATOM    540  CA  GLN A  58     -10.920   2.864   6.799  1.00 21.95           C  
-ATOM    541  C   GLN A  58     -12.293   3.415   7.201  1.00 23.35           C  
-ATOM    542  O   GLN A  58     -13.123   3.759   6.371  1.00 25.39           O  
-ATOM    543  CB  GLN A  58     -10.189   3.922   5.982  1.00 20.95           C  
-ATOM    544  CG  GLN A  58     -10.134   5.235   6.752  1.00 26.62           C  
-ATOM    545  CD  GLN A  58      -9.441   6.306   5.966  1.00 27.71           C  
-ATOM    546  OE1 GLN A  58      -8.267   6.299   5.701  1.00 28.40           O  
-ATOM    547  NE2 GLN A  58     -10.193   7.300   5.610  1.00 31.58           N  
-ATOM    548  H   GLN A  58     -11.022   1.621   5.020  1.00 15.00           H  
-ATOM    549 HE21 GLN A  58      -9.736   8.023   5.106  1.00  0.00           H  
-ATOM    550 HE22 GLN A  58     -11.166   7.339   5.805  1.00  0.00           H  
-ATOM    551  N   TYR A  59     -12.466   3.541   8.508  1.00 20.81           N  
-ATOM    552  CA  TYR A  59     -13.613   4.218   9.110  1.00 22.77           C  
-ATOM    553  C   TYR A  59     -13.260   5.532   9.791  1.00 24.76           C  
-ATOM    554  O   TYR A  59     -12.437   5.643  10.687  1.00 25.36           O  
-ATOM    555  CB  TYR A  59     -14.228   3.337  10.204  1.00 19.72           C  
-ATOM    556  CG  TYR A  59     -14.898   2.088   9.697  1.00 19.61           C  
-ATOM    557  CD1 TYR A  59     -14.126   0.936   9.457  1.00 19.33           C  
-ATOM    558  CD2 TYR A  59     -16.305   2.069   9.511  1.00 18.69           C  
-ATOM    559  CE1 TYR A  59     -14.760  -0.247   9.040  1.00 20.46           C  
-ATOM    560  CE2 TYR A  59     -16.935   0.884   9.093  1.00 19.72           C  
-ATOM    561  CZ  TYR A  59     -16.154  -0.265   8.865  1.00 19.59           C  
-ATOM    562  OH  TYR A  59     -16.751  -1.449   8.497  1.00 23.47           O  
-ATOM    563  H   TYR A  59     -11.769   3.148   9.117  1.00 15.00           H  
-ATOM    564  HH  TYR A  59     -17.685  -1.254   8.335  1.00 15.00           H  
-ATOM    565  N   ASP A  60     -13.908   6.571   9.339  1.00 27.44           N  
-ATOM    566  CA  ASP A  60     -13.691   7.872   9.991  1.00 29.22           C  
-ATOM    567  C   ASP A  60     -14.703   8.261  11.063  1.00 28.18           C  
-ATOM    568  O   ASP A  60     -15.795   7.741  11.172  1.00 26.44           O  
-ATOM    569  CB  ASP A  60     -13.704   9.011   8.955  1.00 32.45           C  
-ATOM    570  CG  ASP A  60     -12.685   8.830   7.851  1.00 35.00           C  
-ATOM    571  OD1 ASP A  60     -11.515   8.577   8.124  1.00 37.83           O  
-ATOM    572  OD2 ASP A  60     -13.080   8.950   6.702  1.00 38.92           O  
-ATOM    573  H   ASP A  60     -14.588   6.451   8.621  1.00 15.00           H  
-ATOM    574  N   GLN A  61     -14.297   9.231  11.859  1.00 28.05           N  
-ATOM    575  CA  GLN A  61     -15.127   9.774  12.932  1.00 31.25           C  
-ATOM    576  C   GLN A  61     -15.813   8.766  13.870  1.00 29.64           C  
-ATOM    577  O   GLN A  61     -16.933   8.895  14.334  1.00 28.72           O  
-ATOM    578  CB  GLN A  61     -16.080  10.847  12.364  1.00 34.05           C  
-ATOM    579  CG  GLN A  61     -15.740  12.256  12.901  1.00 43.14           C  
-ATOM    580  CD  GLN A  61     -16.840  13.283  12.550  1.00 50.50           C  
-ATOM    581  OE1 GLN A  61     -17.692  13.718  13.302  1.00 51.93           O  
-ATOM    582  NE2 GLN A  61     -16.826  13.728  11.317  1.00 53.24           N  
-ATOM    583  H   GLN A  61     -13.389   9.609  11.695  1.00 15.00           H  
-ATOM    584 HE21 GLN A  61     -17.587  14.323  11.087  1.00  0.00           H  
-ATOM    585 HE22 GLN A  61     -16.133  13.479  10.654  1.00  0.00           H  
-ATOM    586  N   ILE A  62     -15.041   7.721  14.161  1.00 26.97           N  
-ATOM    587  CA  ILE A  62     -15.488   6.699  15.115  1.00 24.32           C  
-ATOM    588  C   ILE A  62     -15.197   7.071  16.559  1.00 24.62           C  
-ATOM    589  O   ILE A  62     -14.098   7.454  16.939  1.00 22.41           O  
-ATOM    590  CB  ILE A  62     -14.785   5.361  14.797  1.00 24.50           C  
-ATOM    591  CG1 ILE A  62     -15.158   4.790  13.422  1.00 26.88           C  
-ATOM    592  CG2 ILE A  62     -14.946   4.259  15.852  1.00 21.58           C  
-ATOM    593  CD1 ILE A  62     -16.631   4.396  13.270  1.00 29.80           C  
-ATOM    594  H   ILE A  62     -14.110   7.677  13.793  1.00 15.00           H  
-ATOM    595  N   LEU A  63     -16.253   6.912  17.355  1.00 23.72           N  
-ATOM    596  CA  LEU A  63     -16.145   7.015  18.812  1.00 24.76           C  
-ATOM    597  C   LEU A  63     -15.490   5.820  19.482  1.00 23.09           C  
-ATOM    598  O   LEU A  63     -15.899   4.674  19.415  1.00 22.96           O  
-ATOM    599  CB  LEU A  63     -17.536   7.255  19.403  1.00 26.40           C  
-ATOM    600  CG  LEU A  63     -17.564   8.122  20.672  1.00 34.24           C  
-ATOM    601  CD1 LEU A  63     -19.012   8.505  20.962  1.00 36.69           C  
-ATOM    602  CD2 LEU A  63     -16.930   7.483  21.918  1.00 35.59           C  
-ATOM    603  H   LEU A  63     -17.135   6.682  16.934  1.00  0.00           H  
-ATOM    604  N   ILE A  64     -14.421   6.142  20.153  1.00 23.13           N  
-ATOM    605  CA  ILE A  64     -13.749   5.112  20.934  1.00 25.29           C  
-ATOM    606  C   ILE A  64     -13.455   5.586  22.362  1.00 25.90           C  
-ATOM    607  O   ILE A  64     -13.167   6.741  22.655  1.00 24.57           O  
-ATOM    608  CB  ILE A  64     -12.471   4.724  20.172  1.00 26.29           C  
-ATOM    609  CG1 ILE A  64     -11.582   3.695  20.865  1.00 25.09           C  
-ATOM    610  CG2 ILE A  64     -11.702   6.001  19.798  1.00 26.03           C  
-ATOM    611  CD1 ILE A  64     -10.560   3.133  19.880  1.00 27.87           C  
-ATOM    612  H   ILE A  64     -14.067   7.082  20.102  1.00  0.00           H  
-ATOM    613  N   GLU A  65     -13.554   4.638  23.273  1.00 24.59           N  
-ATOM    614  CA  GLU A  65     -13.192   5.048  24.632  1.00 23.96           C  
-ATOM    615  C   GLU A  65     -12.022   4.279  25.223  1.00 22.16           C  
-ATOM    616  O   GLU A  65     -11.994   3.065  25.311  1.00 23.38           O  
-ATOM    617  CB  GLU A  65     -14.471   4.907  25.411  1.00 26.71           C  
-ATOM    618  CG  GLU A  65     -14.528   5.598  26.751  1.00 35.02           C  
-ATOM    619  CD  GLU A  65     -15.864   5.206  27.308  1.00 38.12           C  
-ATOM    620  OE1 GLU A  65     -16.894   5.625  26.769  1.00 39.32           O  
-ATOM    621  OE2 GLU A  65     -15.860   4.438  28.264  1.00 44.66           O  
-ATOM    622  H   GLU A  65     -13.886   3.727  23.012  1.00 15.00           H  
-ATOM    623  N   ILE A  66     -11.010   5.011  25.583  1.00 20.47           N  
-ATOM    624  CA  ILE A  66      -9.772   4.354  26.003  1.00 21.43           C  
-ATOM    625  C   ILE A  66      -9.543   4.621  27.463  1.00 22.32           C  
-ATOM    626  O   ILE A  66      -9.390   5.766  27.862  1.00 21.56           O  
-ATOM    627  CB  ILE A  66      -8.573   4.890  25.185  1.00 21.43           C  
-ATOM    628  CG1 ILE A  66      -8.767   4.586  23.683  1.00 22.79           C  
-ATOM    629  CG2 ILE A  66      -7.203   4.333  25.625  1.00 18.30           C  
-ATOM    630  CD1 ILE A  66      -8.508   5.775  22.760  1.00 25.09           C  
-ATOM    631  H   ILE A  66     -11.088   6.009  25.504  1.00 15.00           H  
-ATOM    632  N   CYS A  67      -9.625   3.561  28.283  1.00 23.95           N  
-ATOM    633  CA  CYS A  67      -9.639   3.779  29.759  1.00 25.81           C  
-ATOM    634  C   CYS A  67     -10.569   4.867  30.280  1.00 25.78           C  
-ATOM    635  O   CYS A  67     -10.216   5.771  31.022  1.00 27.75           O  
-ATOM    636  CB  CYS A  67      -8.238   4.104  30.307  1.00 28.11           C  
-ATOM    637  SG  CYS A  67      -7.092   2.710  30.224  1.00 34.88           S  
-ATOM    638  H   CYS A  67      -9.653   2.638  27.889  1.00 15.00           H  
-ATOM    639  N   GLY A  68     -11.786   4.812  29.774  1.00 26.85           N  
-ATOM    640  CA  GLY A  68     -12.726   5.890  30.099  1.00 29.30           C  
-ATOM    641  C   GLY A  68     -12.470   7.280  29.522  1.00 27.77           C  
-ATOM    642  O   GLY A  68     -13.086   8.265  29.855  1.00 31.55           O  
-ATOM    643  H   GLY A  68     -12.066   4.009  29.239  1.00 15.00           H  
-ATOM    644  N   HIS A  69     -11.523   7.374  28.628  1.00 25.68           N  
-ATOM    645  CA  HIS A  69     -11.391   8.665  27.938  1.00 25.43           C  
-ATOM    646  C   HIS A  69     -11.936   8.574  26.527  1.00 25.56           C  
-ATOM    647  O   HIS A  69     -11.585   7.679  25.781  1.00 27.37           O  
-ATOM    648  CB  HIS A  69      -9.911   9.032  27.800  1.00 27.26           C  
-ATOM    649  CG  HIS A  69      -9.293   9.326  29.136  1.00 28.11           C  
-ATOM    650  ND1 HIS A  69      -8.698  10.474  29.444  1.00 32.18           N  
-ATOM    651  CD2 HIS A  69      -9.237   8.501  30.255  1.00 30.53           C  
-ATOM    652  CE1 HIS A  69      -8.272  10.395  30.734  1.00 29.99           C  
-ATOM    653  NE2 HIS A  69      -8.608   9.181  31.228  1.00 28.92           N  
-ATOM    654  H   HIS A  69     -10.962   6.577  28.397  1.00 15.00           H  
-ATOM    655  HD1 HIS A  69      -8.508  11.251  28.874  1.00 15.00           H  
-ATOM    656  HE2 HIS A  69      -8.457   8.876  32.142  1.00 15.00           H  
-ATOM    657  N   LYS A  70     -12.797   9.502  26.166  1.00 26.44           N  
-ATOM    658  CA  LYS A  70     -13.302   9.531  24.771  1.00 28.01           C  
-ATOM    659  C   LYS A  70     -12.380  10.089  23.696  1.00 25.80           C  
-ATOM    660  O   LYS A  70     -11.743  11.119  23.834  1.00 26.61           O  
-ATOM    661  CB  LYS A  70     -14.614  10.314  24.693  1.00 30.29           C  
-ATOM    662  CG  LYS A  70     -15.629   9.489  25.447  1.00 37.71           C  
-ATOM    663  CD  LYS A  70     -16.989  10.140  25.624  1.00 45.22           C  
-ATOM    664  CE  LYS A  70     -17.856   9.084  26.323  1.00 53.65           C  
-ATOM    665  NZ  LYS A  70     -19.275   9.485  26.355  1.00 59.52           N  
-ATOM    666  H   LYS A  70     -13.068  10.197  26.826  1.00 15.00           H  
-ATOM    667  HZ1 LYS A  70     -19.363  10.396  26.849  1.00 15.00           H  
-ATOM    668  HZ2 LYS A  70     -19.634   9.580  25.384  1.00 15.00           H  
-ATOM    669  HZ3 LYS A  70     -19.826   8.764  26.862  1.00 15.00           H  
-ATOM    670  N   ALA A  71     -12.346   9.369  22.602  1.00 23.30           N  
-ATOM    671  CA  ALA A  71     -11.662   9.915  21.435  1.00 22.11           C  
-ATOM    672  C   ALA A  71     -12.542   9.700  20.243  1.00 21.95           C  
-ATOM    673  O   ALA A  71     -13.288   8.732  20.176  1.00 23.33           O  
-ATOM    674  CB  ALA A  71     -10.293   9.261  21.222  1.00 19.68           C  
-ATOM    675  H   ALA A  71     -12.767   8.459  22.577  1.00 15.00           H  
-ATOM    676  N   ILE A  72     -12.492  10.660  19.327  1.00 20.66           N  
-ATOM    677  CA  ILE A  72     -13.266  10.487  18.076  1.00 20.93           C  
-ATOM    678  C   ILE A  72     -12.397  10.673  16.842  1.00 19.64           C  
-ATOM    679  O   ILE A  72     -11.858  11.744  16.577  1.00 19.08           O  
-ATOM    680  CB  ILE A  72     -14.515  11.414  17.985  1.00 22.76           C  
-ATOM    681  CG1 ILE A  72     -15.428  11.308  19.221  1.00 19.08           C  
-ATOM    682  CG2 ILE A  72     -15.338  11.178  16.685  1.00 21.77           C  
-ATOM    683  CD1 ILE A  72     -16.545  12.328  19.195  1.00 18.53           C  
-ATOM    684  H   ILE A  72     -11.880  11.439  19.500  1.00 15.00           H  
-ATOM    685  N   GLY A  73     -12.234   9.565  16.123  1.00 16.35           N  
-ATOM    686  CA  GLY A  73     -11.250   9.635  15.045  1.00 16.58           C  
-ATOM    687  C   GLY A  73     -11.315   8.499  14.059  1.00 17.25           C  
-ATOM    688  O   GLY A  73     -12.215   7.683  14.060  1.00 17.52           O  
-ATOM    689  H   GLY A  73     -12.728   8.727  16.380  1.00 15.00           H  
-ATOM    690  N   THR A  74     -10.311   8.478  13.199  1.00 18.81           N  
-ATOM    691  CA  THR A  74     -10.209   7.419  12.171  1.00 18.10           C  
-ATOM    692  C   THR A  74      -9.663   6.124  12.699  1.00 19.58           C  
-ATOM    693  O   THR A  74      -8.638   6.053  13.370  1.00 21.06           O  
-ATOM    694  CB  THR A  74      -9.269   7.830  11.027  1.00 18.64           C  
-ATOM    695  OG1 THR A  74      -9.791   9.006  10.422  1.00 22.66           O  
-ATOM    696  CG2 THR A  74      -9.087   6.788   9.914  1.00 18.39           C  
-ATOM    697  H   THR A  74      -9.595   9.171  13.298  1.00 15.00           H  
-ATOM    698  HG1 THR A  74     -10.600   8.772   9.954  1.00 15.00           H  
-ATOM    699  N   VAL A  75     -10.363   5.085  12.336  1.00 17.46           N  
-ATOM    700  CA  VAL A  75      -9.922   3.755  12.729  1.00 19.72           C  
-ATOM    701  C   VAL A  75      -9.774   2.879  11.496  1.00 19.18           C  
-ATOM    702  O   VAL A  75     -10.641   2.783  10.644  1.00 20.15           O  
-ATOM    703  CB  VAL A  75     -10.980   3.190  13.699  1.00 19.79           C  
-ATOM    704  CG1 VAL A  75     -10.805   1.694  13.903  1.00 23.90           C  
-ATOM    705  CG2 VAL A  75     -10.979   3.925  15.051  1.00 21.22           C  
-ATOM    706  H   VAL A  75     -11.219   5.220  11.830  1.00 15.00           H  
-ATOM    707  N   LEU A  76      -8.632   2.246  11.413  1.00 18.34           N  
-ATOM    708  CA  LEU A  76      -8.505   1.246  10.357  1.00 17.04           C  
-ATOM    709  C   LEU A  76      -8.804  -0.181  10.887  1.00 18.67           C  
-ATOM    710  O   LEU A  76      -8.399  -0.574  11.971  1.00 19.96           O  
-ATOM    711  CB  LEU A  76      -7.066   1.324   9.824  1.00 16.57           C  
-ATOM    712  CG  LEU A  76      -6.550   2.725   9.522  1.00 18.82           C  
-ATOM    713  CD1 LEU A  76      -5.071   2.642   9.233  1.00 21.58           C  
-ATOM    714  CD2 LEU A  76      -7.239   3.355   8.317  1.00 20.90           C  
-ATOM    715  H   LEU A  76      -7.922   2.343  12.116  1.00 15.00           H  
-ATOM    716  N   VAL A  77      -9.537  -0.954  10.104  1.00 18.59           N  
-ATOM    717  CA  VAL A  77      -9.799  -2.363  10.436  1.00 20.05           C  
-ATOM    718  C   VAL A  77      -9.216  -3.338   9.402  1.00 19.29           C  
-ATOM    719  O   VAL A  77      -9.379  -3.188   8.205  1.00 19.38           O  
-ATOM    720  CB  VAL A  77     -11.337  -2.613  10.566  1.00 21.10           C  
-ATOM    721  CG1 VAL A  77     -11.656  -4.092  10.772  1.00 20.54           C  
-ATOM    722  CG2 VAL A  77     -11.972  -1.782  11.695  1.00 22.03           C  
-ATOM    723  H   VAL A  77      -9.934  -0.528   9.285  1.00 15.00           H  
-ATOM    724  N   GLY A  78      -8.544  -4.351   9.889  1.00 17.76           N  
-ATOM    725  CA  GLY A  78      -7.915  -5.286   8.965  1.00 20.81           C  
-ATOM    726  C   GLY A  78      -7.119  -6.333   9.697  1.00 21.05           C  
-ATOM    727  O   GLY A  78      -7.171  -6.453  10.904  1.00 21.00           O  
-ATOM    728  H   GLY A  78      -8.448  -4.436  10.889  1.00 15.00           H  
-ATOM    729  N   PRO A  79      -6.383  -7.127   8.953  1.00 23.59           N  
-ATOM    730  CA  PRO A  79      -5.745  -8.325   9.566  1.00 24.92           C  
-ATOM    731  C   PRO A  79      -4.432  -8.063  10.338  1.00 25.42           C  
-ATOM    732  O   PRO A  79      -3.351  -8.576  10.077  1.00 27.28           O  
-ATOM    733  CB  PRO A  79      -5.567  -9.233   8.320  1.00 25.27           C  
-ATOM    734  CG  PRO A  79      -5.265  -8.220   7.204  1.00 24.81           C  
-ATOM    735  CD  PRO A  79      -6.185  -7.021   7.510  1.00 24.32           C  
-ATOM    736  N   THR A  80      -4.563  -7.196  11.340  1.00 24.94           N  
-ATOM    737  CA  THR A  80      -3.413  -6.929  12.226  1.00 23.07           C  
-ATOM    738  C   THR A  80      -3.202  -8.045  13.257  1.00 21.78           C  
-ATOM    739  O   THR A  80      -4.154  -8.572  13.805  1.00 22.02           O  
-ATOM    740  CB  THR A  80      -3.600  -5.533  12.928  1.00 21.64           C  
-ATOM    741  OG1 THR A  80      -2.489  -5.260  13.811  1.00 22.96           O  
-ATOM    742  CG2 THR A  80      -4.940  -5.396  13.664  1.00 19.35           C  
-ATOM    743  H   THR A  80      -5.485  -6.848  11.531  1.00 15.00           H  
-ATOM    744  HG1 THR A  80      -2.786  -4.729  14.572  1.00 15.00           H  
-ATOM    745  N   PRO A  81      -1.936  -8.397  13.539  1.00 21.34           N  
-ATOM    746  CA  PRO A  81      -1.696  -9.319  14.661  1.00 22.53           C  
-ATOM    747  C   PRO A  81      -2.291  -8.888  16.032  1.00 25.08           C  
-ATOM    748  O   PRO A  81      -2.604  -9.691  16.897  1.00 26.39           O  
-ATOM    749  CB  PRO A  81      -0.165  -9.358  14.736  1.00 21.23           C  
-ATOM    750  CG  PRO A  81       0.374  -8.841  13.406  1.00 21.84           C  
-ATOM    751  CD  PRO A  81      -0.713  -7.932  12.872  1.00 20.69           C  
-ATOM    752  N   VAL A  82      -2.417  -7.563  16.211  1.00 24.84           N  
-ATOM    753  CA  VAL A  82      -2.818  -6.956  17.507  1.00 23.32           C  
-ATOM    754  C   VAL A  82      -3.553  -5.640  17.323  1.00 19.45           C  
-ATOM    755  O   VAL A  82      -3.209  -4.864  16.448  1.00 17.68           O  
-ATOM    756  CB  VAL A  82      -1.533  -6.698  18.367  1.00 27.29           C  
-ATOM    757  CG1 VAL A  82      -0.555  -5.782  17.640  1.00 28.27           C  
-ATOM    758  CG2 VAL A  82      -1.794  -6.099  19.758  1.00 29.38           C  
-ATOM    759  H   VAL A  82      -2.164  -6.954  15.460  1.00 15.00           H  
-ATOM    760  N   ASN A  83      -4.545  -5.399  18.157  1.00 15.20           N  
-ATOM    761  CA  ASN A  83      -5.162  -4.081  18.149  1.00 15.65           C  
-ATOM    762  C   ASN A  83      -4.226  -3.007  18.633  1.00 16.61           C  
-ATOM    763  O   ASN A  83      -3.666  -3.099  19.719  1.00 17.61           O  
-ATOM    764  CB  ASN A  83      -6.365  -3.990  19.078  1.00 17.18           C  
-ATOM    765  CG  ASN A  83      -7.430  -4.970  18.691  1.00 18.67           C  
-ATOM    766  OD1 ASN A  83      -7.792  -5.134  17.559  1.00 20.50           O  
-ATOM    767  ND2 ASN A  83      -7.997  -5.626  19.656  1.00 15.48           N  
-ATOM    768  H   ASN A  83      -4.774  -6.091  18.847  1.00 15.00           H  
-ATOM    769 HD21 ASN A  83      -8.731  -6.253  19.422  1.00  0.00           H  
-ATOM    770 HD22 ASN A  83      -7.707  -5.493  20.605  1.00  0.00           H  
-ATOM    771  N   ILE A  84      -4.081  -2.003  17.780  1.00 15.43           N  
-ATOM    772  CA  ILE A  84      -3.103  -0.931  17.995  1.00 17.15           C  
-ATOM    773  C   ILE A  84      -3.777   0.413  18.127  1.00 16.11           C  
-ATOM    774  O   ILE A  84      -4.510   0.823  17.256  1.00 18.00           O  
-ATOM    775  CB  ILE A  84      -2.160  -0.832  16.773  1.00 20.25           C  
-ATOM    776  CG1 ILE A  84      -1.337  -2.086  16.451  1.00 21.31           C  
-ATOM    777  CG2 ILE A  84      -1.231   0.409  16.831  1.00 20.13           C  
-ATOM    778  CD1 ILE A  84      -0.274  -2.312  17.495  1.00 27.80           C  
-ATOM    779  H   ILE A  84      -4.599  -2.037  16.918  1.00 15.00           H  
-ATOM    780  N   ILE A  85      -3.494   1.097  19.220  1.00 16.16           N  
-ATOM    781  CA  ILE A  85      -3.877   2.492  19.292  1.00 13.61           C  
-ATOM    782  C   ILE A  85      -2.693   3.388  18.952  1.00 13.86           C  
-ATOM    783  O   ILE A  85      -1.704   3.452  19.669  1.00 15.09           O  
-ATOM    784  CB  ILE A  85      -4.405   2.837  20.698  1.00 13.58           C  
-ATOM    785  CG1 ILE A  85      -5.537   1.927  21.180  1.00 16.38           C  
-ATOM    786  CG2 ILE A  85      -4.889   4.296  20.748  1.00 14.67           C  
-ATOM    787  CD1 ILE A  85      -6.768   1.959  20.256  1.00 17.20           C  
-ATOM    788  H   ILE A  85      -2.911   0.688  19.928  1.00 15.00           H  
-ATOM    789  N   GLY A  86      -2.814   4.082  17.826  1.00 13.34           N  
-ATOM    790  CA  GLY A  86      -1.718   4.971  17.423  1.00 13.24           C  
-ATOM    791  C   GLY A  86      -1.863   6.412  17.831  1.00 11.11           C  
-ATOM    792  O   GLY A  86      -2.831   6.834  18.440  1.00 11.48           O  
-ATOM    793  H   GLY A  86      -3.676   4.026  17.323  1.00 15.00           H  
-ATOM    794  N   ARG A  87      -0.873   7.174  17.414  1.00 11.65           N  
-ATOM    795  CA  ARG A  87      -0.838   8.612  17.743  1.00 13.30           C  
-ATOM    796  C   ARG A  87      -2.015   9.479  17.393  1.00 14.45           C  
-ATOM    797  O   ARG A  87      -2.291  10.421  18.107  1.00 14.07           O  
-ATOM    798  CB  ARG A  87       0.404   9.338  17.211  1.00 12.91           C  
-ATOM    799  CG  ARG A  87       1.716   8.783  17.766  1.00 11.29           C  
-ATOM    800  CD  ARG A  87       2.918   9.671  17.432  1.00 14.08           C  
-ATOM    801  NE  ARG A  87       3.171   9.653  15.994  1.00 16.04           N  
-ATOM    802  CZ  ARG A  87       2.736  10.626  15.184  1.00 18.82           C  
-ATOM    803  NH1 ARG A  87       2.162  11.733  15.662  1.00 15.55           N  
-ATOM    804  NH2 ARG A  87       2.858  10.458  13.869  1.00 21.26           N  
-ATOM    805  H   ARG A  87      -0.106   6.732  16.936  1.00 15.00           H  
-ATOM    806  HE  ARG A  87       3.600   8.847  15.594  1.00 15.00           H  
-ATOM    807 HH11 ARG A  87       2.073  11.832  16.649  1.00  0.00           H  
-ATOM    808 HH12 ARG A  87       1.817  12.460  15.065  1.00  0.00           H  
-ATOM    809 HH21 ARG A  87       3.275   9.624  13.509  1.00  0.00           H  
-ATOM    810 HH22 ARG A  87       2.536  11.171  13.238  1.00  0.00           H  
-ATOM    811  N   ASN A  88      -2.756   9.145  16.328  1.00 15.26           N  
-ATOM    812  CA  ASN A  88      -4.025   9.873  16.077  1.00 15.06           C  
-ATOM    813  C   ASN A  88      -5.065   9.947  17.228  1.00 16.11           C  
-ATOM    814  O   ASN A  88      -5.761  10.934  17.439  1.00 17.19           O  
-ATOM    815  CB  ASN A  88      -4.704   9.399  14.759  1.00 12.37           C  
-ATOM    816  CG  ASN A  88      -5.308   8.030  14.859  1.00 13.93           C  
-ATOM    817  OD1 ASN A  88      -4.673   7.063  15.192  1.00 15.35           O  
-ATOM    818  ND2 ASN A  88      -6.584   7.939  14.605  1.00 13.21           N  
-ATOM    819  H   ASN A  88      -2.463   8.374  15.759  1.00 15.00           H  
-ATOM    820 HD21 ASN A  88      -7.033   7.049  14.661  1.00  0.00           H  
-ATOM    821 HD22 ASN A  88      -7.118   8.741  14.340  1.00  0.00           H  
-ATOM    822  N   LEU A  89      -5.137   8.851  17.984  1.00 14.96           N  
-ATOM    823  CA  LEU A  89      -6.001   8.902  19.179  1.00 15.55           C  
-ATOM    824  C   LEU A  89      -5.250   9.117  20.496  1.00 15.52           C  
-ATOM    825  O   LEU A  89      -5.760   9.715  21.421  1.00 17.54           O  
-ATOM    826  CB  LEU A  89      -6.830   7.624  19.295  1.00 15.48           C  
-ATOM    827  CG  LEU A  89      -7.671   7.266  18.064  1.00 17.22           C  
-ATOM    828  CD1 LEU A  89      -8.371   5.934  18.261  1.00 18.04           C  
-ATOM    829  CD2 LEU A  89      -8.687   8.341  17.718  1.00 18.47           C  
-ATOM    830  H   LEU A  89      -4.581   8.049  17.753  1.00 15.00           H  
-ATOM    831  N   LEU A  90      -3.977   8.672  20.576  1.00 14.72           N  
-ATOM    832  CA  LEU A  90      -3.210   9.041  21.782  1.00 14.60           C  
-ATOM    833  C   LEU A  90      -3.104  10.530  22.122  1.00 16.02           C  
-ATOM    834  O   LEU A  90      -3.161  10.950  23.263  1.00 14.58           O  
-ATOM    835  CB  LEU A  90      -1.789   8.473  21.755  1.00 13.92           C  
-ATOM    836  CG  LEU A  90      -1.690   6.947  21.703  1.00 11.48           C  
-ATOM    837  CD1 LEU A  90      -0.232   6.548  21.492  1.00 12.42           C  
-ATOM    838  CD2 LEU A  90      -2.311   6.293  22.918  1.00 11.55           C  
-ATOM    839  H   LEU A  90      -3.607   8.067  19.865  1.00 15.00           H  
-ATOM    840  N   THR A  91      -2.980  11.341  21.078  1.00 15.56           N  
-ATOM    841  CA  THR A  91      -3.003  12.794  21.277  1.00 15.71           C  
-ATOM    842  C   THR A  91      -4.310  13.372  21.781  1.00 16.35           C  
-ATOM    843  O   THR A  91      -4.355  14.248  22.624  1.00 17.99           O  
-ATOM    844  CB  THR A  91      -2.618  13.546  19.981  1.00 15.91           C  
-ATOM    845  OG1 THR A  91      -3.574  13.247  18.975  1.00 15.35           O  
-ATOM    846  CG2 THR A  91      -1.195  13.245  19.482  1.00 11.53           C  
-ATOM    847  H   THR A  91      -2.885  10.967  20.152  1.00 15.00           H  
-ATOM    848  HG1 THR A  91      -3.587  13.962  18.327  1.00 15.00           H  
-ATOM    849  N   GLN A  92      -5.406  12.825  21.283  1.00 18.17           N  
-ATOM    850  CA  GLN A  92      -6.732  13.213  21.794  1.00 17.46           C  
-ATOM    851  C   GLN A  92      -6.978  12.987  23.279  1.00 17.68           C  
-ATOM    852  O   GLN A  92      -7.565  13.795  23.960  1.00 19.10           O  
-ATOM    853  CB  GLN A  92      -7.867  12.506  21.028  1.00 17.91           C  
-ATOM    854  CG  GLN A  92      -7.882  12.844  19.539  1.00 18.73           C  
-ATOM    855  CD  GLN A  92      -9.209  12.434  18.946  1.00 21.37           C  
-ATOM    856  OE1 GLN A  92     -10.223  12.295  19.596  1.00 22.69           O  
-ATOM    857  NE2 GLN A  92      -9.225  12.240  17.648  1.00 20.57           N  
-ATOM    858  H   GLN A  92      -5.296  12.184  20.525  1.00 15.00           H  
-ATOM    859 HE21 GLN A  92     -10.115  12.047  17.229  1.00  0.00           H  
-ATOM    860 HE22 GLN A  92      -8.391  12.291  17.109  1.00  0.00           H  
-ATOM    861  N   ILE A  93      -6.468  11.873  23.792  1.00 18.53           N  
-ATOM    862  CA  ILE A  93      -6.550  11.664  25.250  1.00 20.06           C  
-ATOM    863  C   ILE A  93      -5.388  12.224  26.114  1.00 20.92           C  
-ATOM    864  O   ILE A  93      -5.188  11.924  27.276  1.00 24.78           O  
-ATOM    865  CB  ILE A  93      -6.735  10.162  25.532  1.00 18.80           C  
-ATOM    866  CG1 ILE A  93      -5.467   9.338  25.230  1.00 19.90           C  
-ATOM    867  CG2 ILE A  93      -7.964   9.600  24.795  1.00 20.28           C  
-ATOM    868  CD1 ILE A  93      -5.599   7.880  25.692  1.00 20.77           C  
-ATOM    869  H   ILE A  93      -6.079  11.197  23.164  1.00 15.00           H  
-ATOM    870  N   GLY A  94      -4.577  13.058  25.526  1.00 18.65           N  
-ATOM    871  CA  GLY A  94      -3.549  13.718  26.325  1.00 18.09           C  
-ATOM    872  C   GLY A  94      -2.374  12.863  26.726  1.00 19.27           C  
-ATOM    873  O   GLY A  94      -1.695  13.059  27.715  1.00 19.93           O  
-ATOM    874  H   GLY A  94      -4.730  13.301  24.568  1.00 15.00           H  
-ATOM    875  N   CYS A  95      -2.113  11.878  25.889  1.00 17.79           N  
-ATOM    876  CA  CYS A  95      -0.972  11.021  26.207  1.00 18.67           C  
-ATOM    877  C   CYS A  95       0.411  11.564  25.910  1.00 18.57           C  
-ATOM    878  O   CYS A  95       0.731  12.066  24.845  1.00 18.45           O  
-ATOM    879  CB  CYS A  95      -1.220   9.720  25.459  1.00 19.95           C  
-ATOM    880  SG  CYS A  95      -0.324   8.320  26.076  1.00 26.87           S  
-ATOM    881  H   CYS A  95      -2.670  11.764  25.063  1.00 15.00           H  
-ATOM    882  N   THR A  96       1.257  11.472  26.905  1.00 17.81           N  
-ATOM    883  CA  THR A  96       2.667  11.828  26.674  1.00 18.40           C  
-ATOM    884  C   THR A  96       3.625  10.726  27.075  1.00 18.90           C  
-ATOM    885  O   THR A  96       3.312   9.827  27.841  1.00 19.54           O  
-ATOM    886  CB  THR A  96       3.126  13.148  27.402  1.00 21.43           C  
-ATOM    887  OG1 THR A  96       2.953  13.085  28.841  1.00 21.52           O  
-ATOM    888  CG2 THR A  96       2.426  14.395  26.865  1.00 19.80           C  
-ATOM    889  H   THR A  96       0.942  11.141  27.799  1.00 15.00           H  
-ATOM    890  HG1 THR A  96       2.083  13.408  29.108  1.00 15.00           H  
-ATOM    891  N   LEU A  97       4.829  10.846  26.543  1.00 20.05           N  
-ATOM    892  CA  LEU A  97       5.970  10.076  27.053  1.00 21.73           C  
-ATOM    893  C   LEU A  97       6.826  10.868  28.016  1.00 20.95           C  
-ATOM    894  O   LEU A  97       7.244  11.994  27.785  1.00 20.90           O  
-ATOM    895  CB  LEU A  97       6.960   9.674  25.931  1.00 22.98           C  
-ATOM    896  CG  LEU A  97       6.702   8.417  25.088  1.00 26.54           C  
-ATOM    897  CD1 LEU A  97       7.707   8.399  23.934  1.00 26.81           C  
-ATOM    898  CD2 LEU A  97       6.770   7.116  25.923  1.00 25.48           C  
-ATOM    899  H   LEU A  97       4.971  11.563  25.856  1.00 15.00           H  
-ATOM    900  N   ASN A  98       7.129  10.218  29.115  1.00 22.02           N  
-ATOM    901  CA  ASN A  98       7.964  10.897  30.110  1.00 21.67           C  
-ATOM    902  C   ASN A  98       9.119  10.076  30.631  1.00 21.17           C  
-ATOM    903  O   ASN A  98       8.998   8.909  30.918  1.00 19.80           O  
-ATOM    904  CB  ASN A  98       7.085  11.264  31.309  1.00 24.46           C  
-ATOM    905  CG  ASN A  98       5.938  12.162  30.886  1.00 25.56           C  
-ATOM    906  OD1 ASN A  98       4.803  11.783  30.720  1.00 28.54           O  
-ATOM    907  ND2 ASN A  98       6.227  13.419  30.764  1.00 25.81           N  
-ATOM    908  H   ASN A  98       6.694   9.327  29.287  1.00 15.00           H  
-ATOM    909 HD21 ASN A  98       5.457  14.021  30.536  1.00  0.00           H  
-ATOM    910 HD22 ASN A  98       7.142  13.780  30.889  1.00  0.00           H  
-ATOM    911  N   PHE A  99      10.243  10.723  30.760  1.00 23.35           N  
-ATOM    912  CA  PHE A  99      11.398  10.152  31.501  1.00 27.08           C  
-ATOM    913  C   PHE A  99      12.431  11.194  31.955  1.00 29.54           C  
-ATOM    914  O   PHE A  99      13.608  10.866  32.201  1.00 32.04           O  
-ATOM    915  CB  PHE A  99      12.115   9.036  30.710  1.00 27.18           C  
-ATOM    916  CG  PHE A  99      12.734   9.553  29.435  1.00 30.14           C  
-ATOM    917  CD1 PHE A  99      11.928   9.722  28.281  1.00 29.15           C  
-ATOM    918  CD2 PHE A  99      14.102   9.920  29.430  1.00 29.52           C  
-ATOM    919  CE1 PHE A  99      12.500  10.283  27.118  1.00 31.92           C  
-ATOM    920  CE2 PHE A  99      14.664  10.474  28.263  1.00 32.00           C  
-ATOM    921  CZ  PHE A  99      13.865  10.657  27.111  1.00 30.64           C  
-ATOM    922  OXT PHE A  99      12.077  12.390  31.979  1.00 32.36           O  
-ATOM    923  H   PHE A  99      10.285  11.639  30.363  1.00 15.00           H  
-TER     924      PHE A  99                                                      
-ATOM    925  N   PRO B   1      12.631  14.527  30.445  1.00 33.83           N  
-ATOM    926  CA  PRO B   1      11.813  15.241  29.428  1.00 31.63           C  
-ATOM    927  C   PRO B   1      10.424  14.640  29.186  1.00 30.58           C  
-ATOM    928  O   PRO B   1      10.199  13.459  29.375  1.00 29.65           O  
-ATOM    929  CB  PRO B   1      12.639  15.245  28.134  1.00 32.48           C  
-ATOM    930  CG  PRO B   1      13.551  14.042  28.307  1.00 33.88           C  
-ATOM    931  CD  PRO B   1      13.902  14.155  29.788  1.00 32.93           C  
-ATOM    932  H2  PRO B   1      12.802  15.106  31.294  1.00 15.00           H  
-ATOM    933  H3  PRO B   1      12.158  13.649  30.780  1.00 15.00           H  
-ATOM    934  N   GLN B   2       9.515  15.512  28.778  1.00 29.86           N  
-ATOM    935  CA  GLN B   2       8.204  15.071  28.306  1.00 31.34           C  
-ATOM    936  C   GLN B   2       8.081  15.222  26.796  1.00 32.34           C  
-ATOM    937  O   GLN B   2       8.229  16.295  26.231  1.00 32.92           O  
-ATOM    938  CB  GLN B   2       7.116  15.931  28.926  1.00 31.06           C  
-ATOM    939  CG  GLN B   2       5.738  15.739  28.289  1.00 36.78           C  
-ATOM    940  CD  GLN B   2       4.614  16.162  29.216  1.00 43.19           C  
-ATOM    941  OE1 GLN B   2       4.428  15.694  30.329  1.00 43.42           O  
-ATOM    942  NE2 GLN B   2       3.802  17.076  28.720  1.00 45.57           N  
-ATOM    943  H   GLN B   2       9.733  16.485  28.709  1.00 15.00           H  
-ATOM    944 HE21 GLN B   2       3.031  17.320  29.302  1.00  0.00           H  
-ATOM    945 HE22 GLN B   2       3.903  17.477  27.816  1.00  0.00           H  
-ATOM    946  N   ILE B   3       7.779  14.104  26.169  1.00 30.38           N  
-ATOM    947  CA  ILE B   3       7.555  14.093  24.725  1.00 27.00           C  
-ATOM    948  C   ILE B   3       6.090  13.962  24.358  1.00 25.29           C  
-ATOM    949  O   ILE B   3       5.339  13.071  24.727  1.00 23.66           O  
-ATOM    950  CB  ILE B   3       8.393  12.972  24.140  1.00 26.68           C  
-ATOM    951  CG1 ILE B   3       9.825  13.186  24.628  1.00 28.99           C  
-ATOM    952  CG2 ILE B   3       8.338  12.968  22.617  1.00 27.20           C  
-ATOM    953  CD1 ILE B   3      10.849  12.201  24.098  1.00 30.75           C  
-ATOM    954  H   ILE B   3       7.660  13.270  26.714  1.00 15.00           H  
-ATOM    955  N   THR B   4       5.668  14.979  23.632  1.00 24.55           N  
-ATOM    956  CA  THR B   4       4.308  14.916  23.082  1.00 23.04           C  
-ATOM    957  C   THR B   4       4.275  14.082  21.795  1.00 21.95           C  
-ATOM    958  O   THR B   4       5.282  13.755  21.163  1.00 20.72           O  
-ATOM    959  CB  THR B   4       3.720  16.338  22.791  1.00 25.45           C  
-ATOM    960  OG1 THR B   4       4.415  16.992  21.701  1.00 25.34           O  
-ATOM    961  CG2 THR B   4       3.733  17.230  24.039  1.00 21.51           C  
-ATOM    962  H   THR B   4       6.322  15.684  23.349  1.00 15.00           H  
-ATOM    963  HG1 THR B   4       5.258  17.346  22.022  1.00 15.00           H  
-ATOM    964  N   LEU B   5       3.054  13.746  21.444  1.00 20.72           N  
-ATOM    965  CA  LEU B   5       2.896  12.827  20.314  1.00 21.03           C  
-ATOM    966  C   LEU B   5       2.289  13.423  19.036  1.00 21.17           C  
-ATOM    967  O   LEU B   5       1.818  12.724  18.160  1.00 20.71           O  
-ATOM    968  CB  LEU B   5       2.066  11.613  20.812  1.00 19.44           C  
-ATOM    969  CG  LEU B   5       2.768  10.789  21.925  1.00 20.76           C  
-ATOM    970  CD1 LEU B   5       1.792   9.758  22.447  1.00 18.20           C  
-ATOM    971  CD2 LEU B   5       4.112  10.166  21.457  1.00 17.78           C  
-ATOM    972  H   LEU B   5       2.269  14.060  21.979  1.00 15.00           H  
-ATOM    973  N   TRP B   6       2.295  14.760  18.926  1.00 20.49           N  
-ATOM    974  CA  TRP B   6       1.861  15.409  17.662  1.00 19.64           C  
-ATOM    975  C   TRP B   6       2.658  15.013  16.433  1.00 20.19           C  
-ATOM    976  O   TRP B   6       2.163  14.819  15.334  1.00 21.05           O  
-ATOM    977  CB  TRP B   6       2.031  16.914  17.740  1.00 19.54           C  
-ATOM    978  CG  TRP B   6       1.273  17.503  18.893  1.00 22.24           C  
-ATOM    979  CD1 TRP B   6       1.846  18.109  20.034  1.00 22.86           C  
-ATOM    980  CD2 TRP B   6      -0.126  17.615  19.034  1.00 22.64           C  
-ATOM    981  NE1 TRP B   6       0.890  18.594  20.878  1.00 23.49           N  
-ATOM    982  CE2 TRP B   6      -0.344  18.331  20.329  1.00 22.63           C  
-ATOM    983  CE3 TRP B   6      -1.233  17.233  18.246  1.00 21.26           C  
-ATOM    984  CZ2 TRP B   6      -1.668  18.610  20.733  1.00 22.76           C  
-ATOM    985  CZ3 TRP B   6      -2.535  17.533  18.687  1.00 24.61           C  
-ATOM    986  CH2 TRP B   6      -2.749  18.213  19.911  1.00 24.55           C  
-ATOM    987  H   TRP B   6       2.651  15.294  19.692  1.00 15.00           H  
-ATOM    988  HE1 TRP B   6       1.055  19.097  21.714  1.00 15.00           H  
-ATOM    989  N   GLN B   7       3.940  14.863  16.684  1.00 20.83           N  
-ATOM    990  CA  GLN B   7       4.838  14.279  15.700  1.00 22.45           C  
-ATOM    991  C   GLN B   7       5.362  12.928  16.129  1.00 21.44           C  
-ATOM    992  O   GLN B   7       5.212  12.521  17.264  1.00 19.28           O  
-ATOM    993  CB  GLN B   7       6.049  15.178  15.575  1.00 29.05           C  
-ATOM    994  CG  GLN B   7       5.977  16.211  14.445  1.00 42.84           C  
-ATOM    995  CD  GLN B   7       5.170  17.444  14.790  1.00 49.54           C  
-ATOM    996  OE1 GLN B   7       5.340  18.126  15.787  1.00 55.16           O  
-ATOM    997  NE2 GLN B   7       4.292  17.777  13.872  1.00 54.23           N  
-ATOM    998  H   GLN B   7       4.299  15.155  17.576  1.00 15.00           H  
-ATOM    999 HE21 GLN B   7       3.768  18.622  14.016  1.00  0.00           H  
-ATOM   1000 HE22 GLN B   7       4.141  17.238  13.053  1.00  0.00           H  
-ATOM   1001  N   ARG B   8       6.014  12.233  15.208  1.00 19.68           N  
-ATOM   1002  CA  ARG B   8       6.612  10.961  15.643  1.00 19.99           C  
-ATOM   1003  C   ARG B   8       7.684  11.164  16.695  1.00 18.80           C  
-ATOM   1004  O   ARG B   8       8.481  12.053  16.476  1.00 20.58           O  
-ATOM   1005  CB  ARG B   8       7.310  10.267  14.476  1.00 18.16           C  
-ATOM   1006  CG  ARG B   8       6.335   9.955  13.369  1.00 20.78           C  
-ATOM   1007  CD  ARG B   8       6.989   9.184  12.246  1.00 19.38           C  
-ATOM   1008  NE  ARG B   8       5.964   8.884  11.248  1.00 23.77           N  
-ATOM   1009  CZ  ARG B   8       6.200   9.087   9.952  1.00 23.03           C  
-ATOM   1010  NH1 ARG B   8       7.420   9.463   9.550  1.00 24.02           N  
-ATOM   1011  NH2 ARG B   8       5.181   8.926   9.110  1.00 21.43           N  
-ATOM   1012  H   ARG B   8       6.065  12.566  14.266  1.00 15.00           H  
-ATOM   1013  HE  ARG B   8       5.068   8.556  11.548  1.00 15.00           H  
-ATOM   1014 HH11 ARG B   8       8.142   9.540  10.237  1.00  0.00           H  
-ATOM   1015 HH12 ARG B   8       7.663   9.681   8.607  1.00  0.00           H  
-ATOM   1016 HH21 ARG B   8       4.314   8.595   9.481  1.00  0.00           H  
-ATOM   1017 HH22 ARG B   8       5.237   9.123   8.131  1.00  0.00           H  
-ATOM   1018  N   PRO B   9       7.716  10.389  17.787  1.00 17.87           N  
-ATOM   1019  CA  PRO B   9       8.718  10.646  18.832  1.00 18.14           C  
-ATOM   1020  C   PRO B   9      10.138  10.250  18.492  1.00 17.76           C  
-ATOM   1021  O   PRO B   9      10.689   9.305  19.016  1.00 18.06           O  
-ATOM   1022  CB  PRO B   9       8.094   9.873  20.011  1.00 18.53           C  
-ATOM   1023  CG  PRO B   9       7.318   8.726  19.398  1.00 16.28           C  
-ATOM   1024  CD  PRO B   9       6.743   9.379  18.162  1.00 16.54           C  
-ATOM   1025  N   LEU B  10      10.722  11.015  17.570  1.00 18.72           N  
-ATOM   1026  CA  LEU B  10      12.150  10.840  17.183  1.00 23.49           C  
-ATOM   1027  C   LEU B  10      13.177  11.550  18.062  1.00 24.64           C  
-ATOM   1028  O   LEU B  10      13.128  12.742  18.316  1.00 27.96           O  
-ATOM   1029  CB  LEU B  10      12.401  11.268  15.717  1.00 22.39           C  
-ATOM   1030  CG  LEU B  10      11.576  10.409  14.752  1.00 24.75           C  
-ATOM   1031  CD1 LEU B  10      11.453  11.097  13.401  1.00 31.34           C  
-ATOM   1032  CD2 LEU B  10      12.155   9.012  14.615  1.00 25.31           C  
-ATOM   1033  H   LEU B  10      10.171  11.762  17.194  1.00 15.00           H  
-ATOM   1034  N   VAL B  11      14.112  10.782  18.557  1.00 24.01           N  
-ATOM   1035  CA  VAL B  11      15.126  11.433  19.376  1.00 23.09           C  
-ATOM   1036  C   VAL B  11      16.507  11.049  18.885  1.00 24.63           C  
-ATOM   1037  O   VAL B  11      16.646  10.108  18.114  1.00 24.02           O  
-ATOM   1038  CB  VAL B  11      14.965  11.013  20.856  1.00 22.95           C  
-ATOM   1039  CG1 VAL B  11      13.617  11.464  21.399  1.00 21.99           C  
-ATOM   1040  CG2 VAL B  11      15.251   9.531  21.109  1.00 20.27           C  
-ATOM   1041  H   VAL B  11      14.096   9.794  18.379  1.00 15.00           H  
-ATOM   1042  N   THR B  12      17.525  11.771  19.377  1.00 25.94           N  
-ATOM   1043  CA  THR B  12      18.930  11.344  19.109  1.00 27.08           C  
-ATOM   1044  C   THR B  12      19.483  10.291  20.019  1.00 26.05           C  
-ATOM   1045  O   THR B  12      19.451  10.373  21.238  1.00 28.02           O  
-ATOM   1046  CB  THR B  12      19.971  12.495  19.163  1.00 28.25           C  
-ATOM   1047  OG1 THR B  12      19.562  13.547  18.293  1.00 31.87           O  
-ATOM   1048  CG2 THR B  12      21.383  12.083  18.750  1.00 28.63           C  
-ATOM   1049  H   THR B  12      17.318  12.583  19.915  1.00 15.00           H  
-ATOM   1050  HG1 THR B  12      20.248  14.219  18.236  1.00 15.00           H  
-ATOM   1051  N   ILE B  13      20.047   9.293  19.380  1.00 25.79           N  
-ATOM   1052  CA  ILE B  13      20.765   8.302  20.165  1.00 25.20           C  
-ATOM   1053  C   ILE B  13      22.246   8.272  19.802  1.00 29.02           C  
-ATOM   1054  O   ILE B  13      22.694   8.576  18.706  1.00 28.99           O  
-ATOM   1055  CB  ILE B  13      20.125   6.906  19.979  1.00 23.36           C  
-ATOM   1056  CG1 ILE B  13      20.276   6.421  18.531  1.00 22.20           C  
-ATOM   1057  CG2 ILE B  13      18.646   6.918  20.409  1.00 18.49           C  
-ATOM   1058  CD1 ILE B  13      20.176   4.915  18.316  1.00 22.44           C  
-ATOM   1059  H   ILE B  13      20.001   9.258  18.379  1.00 15.00           H  
-ATOM   1060  N   LYS B  14      23.013   7.887  20.780  1.00 31.62           N  
-ATOM   1061  CA  LYS B  14      24.406   7.634  20.456  1.00 35.97           C  
-ATOM   1062  C   LYS B  14      24.705   6.144  20.539  1.00 36.18           C  
-ATOM   1063  O   LYS B  14      24.410   5.447  21.503  1.00 34.56           O  
-ATOM   1064  CB  LYS B  14      25.348   8.464  21.363  1.00 42.19           C  
-ATOM   1065  CG  LYS B  14      25.002   9.948  21.697  1.00 51.01           C  
-ATOM   1066  CD  LYS B  14      23.940  10.165  22.822  1.00 58.33           C  
-ATOM   1067  CE  LYS B  14      23.564  11.608  23.260  1.00 63.06           C  
-ATOM   1068  NZ  LYS B  14      24.555  12.233  24.168  1.00 65.36           N  
-ATOM   1069  H   LYS B  14      22.612   7.756  21.691  1.00  0.00           H  
-ATOM   1070  HZ1 LYS B  14      25.487  12.246  23.706  1.00  0.00           H  
-ATOM   1071  HZ2 LYS B  14      24.262  13.208  24.382  1.00  0.00           H  
-ATOM   1072  HZ3 LYS B  14      24.614  11.686  25.050  1.00  0.00           H  
-ATOM   1073  N   ILE B  15      25.273   5.637  19.474  1.00 38.28           N  
-ATOM   1074  CA  ILE B  15      25.653   4.224  19.471  1.00 41.86           C  
-ATOM   1075  C   ILE B  15      26.984   4.023  18.767  1.00 45.72           C  
-ATOM   1076  O   ILE B  15      27.296   4.659  17.782  1.00 47.90           O  
-ATOM   1077  CB  ILE B  15      24.551   3.377  18.843  1.00 40.17           C  
-ATOM   1078  CG1 ILE B  15      24.993   1.917  18.832  1.00 42.75           C  
-ATOM   1079  CG2 ILE B  15      24.181   3.870  17.443  1.00 41.14           C  
-ATOM   1080  CD1 ILE B  15      24.063   0.950  18.113  1.00 43.05           C  
-ATOM   1081  H   ILE B  15      25.392   6.221  18.665  1.00 15.00           H  
-ATOM   1082  N   GLY B  16      27.848   3.194  19.330  1.00 50.22           N  
-ATOM   1083  CA  GLY B  16      29.251   3.208  18.845  1.00 52.01           C  
-ATOM   1084  C   GLY B  16      29.949   4.580  18.744  1.00 52.91           C  
-ATOM   1085  O   GLY B  16      30.737   4.845  17.854  1.00 55.36           O  
-ATOM   1086  H   GLY B  16      27.551   2.626  20.096  1.00 15.00           H  
-ATOM   1087  N   GLY B  17      29.592   5.502  19.641  1.00 53.80           N  
-ATOM   1088  CA  GLY B  17      30.106   6.870  19.437  1.00 54.16           C  
-ATOM   1089  C   GLY B  17      29.610   7.672  18.220  1.00 55.59           C  
-ATOM   1090  O   GLY B  17      29.957   8.822  17.992  1.00 55.83           O  
-ATOM   1091  H   GLY B  17      28.985   5.260  20.402  1.00 15.00           H  
-ATOM   1092  N   GLN B  18      28.713   7.040  17.457  1.00 55.45           N  
-ATOM   1093  CA  GLN B  18      27.943   7.826  16.477  1.00 54.76           C  
-ATOM   1094  C   GLN B  18      26.486   8.175  16.838  1.00 52.28           C  
-ATOM   1095  O   GLN B  18      25.737   7.445  17.472  1.00 51.19           O  
-ATOM   1096  CB  GLN B  18      28.039   7.169  15.085  1.00 57.07           C  
-ATOM   1097  CG  GLN B  18      27.386   5.798  14.932  1.00 60.51           C  
-ATOM   1098  CD  GLN B  18      27.747   5.178  13.606  1.00 63.45           C  
-ATOM   1099  OE1 GLN B  18      28.399   5.707  12.728  1.00 66.43           O  
-ATOM   1100  NE2 GLN B  18      27.309   3.965  13.448  1.00 64.74           N  
-ATOM   1101  H   GLN B  18      28.491   6.078  17.616  1.00 15.00           H  
-ATOM   1102 HE21 GLN B  18      27.576   3.483  12.623  1.00  0.00           H  
-ATOM   1103 HE22 GLN B  18      26.732   3.543  14.138  1.00  0.00           H  
-ATOM   1104  N   LEU B  19      26.124   9.378  16.417  1.00 48.93           N  
-ATOM   1105  CA  LEU B  19      24.758   9.860  16.637  1.00 46.42           C  
-ATOM   1106  C   LEU B  19      23.785   9.407  15.570  1.00 44.00           C  
-ATOM   1107  O   LEU B  19      24.042   9.508  14.386  1.00 45.82           O  
-ATOM   1108  CB  LEU B  19      24.686  11.397  16.626  1.00 46.67           C  
-ATOM   1109  CG  LEU B  19      25.176  12.152  17.864  1.00 47.26           C  
-ATOM   1110  CD1 LEU B  19      26.683  12.069  18.002  1.00 49.38           C  
-ATOM   1111  CD2 LEU B  19      24.744  13.617  17.801  1.00 48.59           C  
-ATOM   1112  H   LEU B  19      26.765   9.913  15.873  1.00 15.00           H  
-ATOM   1113  N   LYS B  20      22.638   8.928  16.004  1.00 40.29           N  
-ATOM   1114  CA  LYS B  20      21.544   8.646  15.060  1.00 34.40           C  
-ATOM   1115  C   LYS B  20      20.178   9.110  15.529  1.00 31.41           C  
-ATOM   1116  O   LYS B  20      19.947   9.427  16.682  1.00 30.75           O  
-ATOM   1117  CB  LYS B  20      21.490   7.141  14.817  1.00 35.39           C  
-ATOM   1118  CG  LYS B  20      22.632   6.614  13.962  1.00 38.95           C  
-ATOM   1119  CD  LYS B  20      22.647   5.089  13.904  1.00 46.08           C  
-ATOM   1120  CE  LYS B  20      23.316   4.523  12.636  1.00 50.51           C  
-ATOM   1121  NZ  LYS B  20      24.633   5.146  12.403  1.00 55.85           N  
-ATOM   1122  H   LYS B  20      22.535   8.777  16.990  1.00 15.00           H  
-ATOM   1123  HZ1 LYS B  20      25.226   5.030  13.249  1.00 15.00           H  
-ATOM   1124  HZ2 LYS B  20      25.093   4.689  11.590  1.00 15.00           H  
-ATOM   1125  HZ3 LYS B  20      24.509   6.159  12.204  1.00 15.00           H  
-ATOM   1126  N   GLU B  21      19.233   9.128  14.623  1.00 29.28           N  
-ATOM   1127  CA  GLU B  21      17.897   9.328  15.182  1.00 30.30           C  
-ATOM   1128  C   GLU B  21      17.033   8.070  15.220  1.00 28.83           C  
-ATOM   1129  O   GLU B  21      17.114   7.175  14.378  1.00 27.30           O  
-ATOM   1130  CB  GLU B  21      17.125  10.458  14.497  1.00 36.99           C  
-ATOM   1131  CG  GLU B  21      16.549  10.078  13.121  1.00 47.88           C  
-ATOM   1132  CD  GLU B  21      15.573  11.134  12.611  1.00 53.92           C  
-ATOM   1133  OE1 GLU B  21      15.215  12.036  13.382  1.00 57.19           O  
-ATOM   1134  OE2 GLU B  21      15.171  11.046  11.439  1.00 56.46           O  
-ATOM   1135  H   GLU B  21      19.425   8.913  13.662  1.00 15.00           H  
-ATOM   1136  N   ALA B  22      16.221   8.024  16.268  1.00 23.95           N  
-ATOM   1137  CA  ALA B  22      15.423   6.826  16.524  1.00 20.36           C  
-ATOM   1138  C   ALA B  22      14.055   7.119  17.121  1.00 19.24           C  
-ATOM   1139  O   ALA B  22      13.828   8.119  17.783  1.00 21.32           O  
-ATOM   1140  CB  ALA B  22      16.206   5.865  17.418  1.00 17.58           C  
-ATOM   1141  H   ALA B  22      16.252   8.782  16.929  1.00 15.00           H  
-ATOM   1142  N   LEU B  23      13.136   6.225  16.822  1.00 17.35           N  
-ATOM   1143  CA  LEU B  23      11.727   6.346  17.244  1.00 14.61           C  
-ATOM   1144  C   LEU B  23      11.502   5.693  18.610  1.00 15.40           C  
-ATOM   1145  O   LEU B  23      11.741   4.504  18.777  1.00 14.72           O  
-ATOM   1146  CB  LEU B  23      10.899   5.582  16.187  1.00 14.93           C  
-ATOM   1147  CG  LEU B  23       9.380   5.676  16.319  1.00 18.29           C  
-ATOM   1148  CD1 LEU B  23       8.859   7.021  15.847  1.00 19.80           C  
-ATOM   1149  CD2 LEU B  23       8.699   4.546  15.546  1.00 19.00           C  
-ATOM   1150  H   LEU B  23      13.413   5.417  16.298  1.00 15.00           H  
-ATOM   1151  N   LEU B  24      11.031   6.483  19.574  1.00 14.37           N  
-ATOM   1152  CA  LEU B  24      10.628   5.848  20.835  1.00 15.97           C  
-ATOM   1153  C   LEU B  24       9.295   5.128  20.756  1.00 15.83           C  
-ATOM   1154  O   LEU B  24       8.233   5.697  20.569  1.00 17.35           O  
-ATOM   1155  CB  LEU B  24      10.587   6.854  22.001  1.00 15.23           C  
-ATOM   1156  CG  LEU B  24      11.845   7.699  22.108  1.00 13.88           C  
-ATOM   1157  CD1 LEU B  24      11.593   8.839  23.074  1.00 15.41           C  
-ATOM   1158  CD2 LEU B  24      13.081   6.873  22.437  1.00 15.02           C  
-ATOM   1159  H   LEU B  24      10.926   7.468  19.399  1.00 15.00           H  
-ATOM   1160  N   ASP B  25       9.400   3.813  20.854  1.00 14.35           N  
-ATOM   1161  CA  ASP B  25       8.249   3.007  20.515  1.00 15.09           C  
-ATOM   1162  C   ASP B  25       7.755   2.089  21.615  1.00 15.29           C  
-ATOM   1163  O   ASP B  25       8.260   1.021  21.906  1.00 16.52           O  
-ATOM   1164  CB  ASP B  25       8.674   2.247  19.254  1.00 15.88           C  
-ATOM   1165  CG  ASP B  25       7.549   1.481  18.605  1.00 16.67           C  
-ATOM   1166  OD1 ASP B  25       6.376   1.543  19.029  1.00 17.60           O  
-ATOM   1167  OD2 ASP B  25       7.890   0.802  17.648  1.00 20.40           O  
-ATOM   1168  H   ASP B  25      10.292   3.381  21.033  1.00 15.00           H  
-ATOM   1169  N   THR B  26       6.649   2.506  22.199  1.00 14.61           N  
-ATOM   1170  CA  THR B  26       6.076   1.646  23.242  1.00 14.22           C  
-ATOM   1171  C   THR B  26       5.381   0.389  22.804  1.00 15.45           C  
-ATOM   1172  O   THR B  26       5.078  -0.491  23.584  1.00 15.74           O  
-ATOM   1173  CB  THR B  26       5.088   2.408  24.107  1.00 14.52           C  
-ATOM   1174  OG1 THR B  26       3.978   2.800  23.322  1.00 15.63           O  
-ATOM   1175  CG2 THR B  26       5.749   3.639  24.721  1.00 13.20           C  
-ATOM   1176  H   THR B  26       6.282   3.420  22.004  1.00 15.00           H  
-ATOM   1177  HG1 THR B  26       3.168   2.444  23.718  1.00 15.00           H  
-ATOM   1178  N   GLY B  27       5.132   0.307  21.499  1.00 14.11           N  
-ATOM   1179  CA  GLY B  27       4.572  -0.936  20.935  1.00 15.58           C  
-ATOM   1180  C   GLY B  27       5.544  -2.001  20.363  1.00 17.56           C  
-ATOM   1181  O   GLY B  27       5.170  -3.060  19.895  1.00 21.31           O  
-ATOM   1182  H   GLY B  27       5.358   1.095  20.932  1.00 15.00           H  
-ATOM   1183  N   ALA B  28       6.830  -1.696  20.444  1.00 14.42           N  
-ATOM   1184  CA  ALA B  28       7.862  -2.675  20.073  1.00 14.12           C  
-ATOM   1185  C   ALA B  28       8.378  -3.425  21.304  1.00 15.54           C  
-ATOM   1186  O   ALA B  28       8.817  -2.839  22.290  1.00 17.70           O  
-ATOM   1187  CB  ALA B  28       9.048  -1.959  19.404  1.00  8.74           C  
-ATOM   1188  H   ALA B  28       7.106  -0.839  20.879  1.00 15.00           H  
-ATOM   1189  N   ASP B  29       8.354  -4.740  21.259  1.00 13.15           N  
-ATOM   1190  CA  ASP B  29       9.060  -5.377  22.393  1.00 14.28           C  
-ATOM   1191  C   ASP B  29      10.588  -5.245  22.383  1.00 16.81           C  
-ATOM   1192  O   ASP B  29      11.299  -5.265  23.382  1.00 17.39           O  
-ATOM   1193  CB  ASP B  29       8.858  -6.894  22.405  1.00 15.75           C  
-ATOM   1194  CG  ASP B  29       7.474  -7.361  22.685  1.00 15.71           C  
-ATOM   1195  OD1 ASP B  29       6.606  -6.554  23.026  1.00 19.28           O  
-ATOM   1196  OD2 ASP B  29       7.285  -8.570  22.590  1.00 18.18           O  
-ATOM   1197  H   ASP B  29       7.851  -5.197  20.515  1.00 15.00           H  
-ATOM   1198  N   ASP B  30      11.074  -5.141  21.156  1.00 17.17           N  
-ATOM   1199  CA  ASP B  30      12.502  -5.172  20.841  1.00 17.85           C  
-ATOM   1200  C   ASP B  30      12.982  -3.865  20.277  1.00 17.39           C  
-ATOM   1201  O   ASP B  30      12.203  -3.041  19.828  1.00 18.49           O  
-ATOM   1202  CB  ASP B  30      12.774  -6.216  19.748  1.00 22.58           C  
-ATOM   1203  CG  ASP B  30      12.507  -7.612  20.269  1.00 30.07           C  
-ATOM   1204  OD1 ASP B  30      13.152  -8.016  21.254  1.00 35.29           O  
-ATOM   1205  OD2 ASP B  30      11.644  -8.287  19.694  1.00 32.06           O  
-ATOM   1206  H   ASP B  30      10.421  -5.002  20.416  1.00 15.00           H  
-ATOM   1207  N   THR B  31      14.301  -3.741  20.298  1.00 16.19           N  
-ATOM   1208  CA  THR B  31      14.977  -2.650  19.614  1.00 14.50           C  
-ATOM   1209  C   THR B  31      15.572  -3.092  18.293  1.00 15.46           C  
-ATOM   1210  O   THR B  31      16.299  -4.073  18.205  1.00 13.99           O  
-ATOM   1211  CB  THR B  31      16.061  -2.048  20.526  1.00 15.45           C  
-ATOM   1212  OG1 THR B  31      15.380  -1.458  21.640  1.00 14.22           O  
-ATOM   1213  CG2 THR B  31      16.963  -0.985  19.858  1.00 13.88           C  
-ATOM   1214  H   THR B  31      14.814  -4.481  20.735  1.00 15.00           H  
-ATOM   1215  HG1 THR B  31      15.038  -2.150  22.225  1.00 15.00           H  
-ATOM   1216  N   VAL B  32      15.198  -2.334  17.257  1.00 15.47           N  
-ATOM   1217  CA  VAL B  32      15.651  -2.643  15.885  1.00 16.44           C  
-ATOM   1218  C   VAL B  32      16.324  -1.465  15.181  1.00 16.80           C  
-ATOM   1219  O   VAL B  32      15.773  -0.384  15.019  1.00 16.50           O  
-ATOM   1220  CB  VAL B  32      14.494  -3.150  15.001  1.00 15.97           C  
-ATOM   1221  CG1 VAL B  32      15.041  -3.681  13.661  1.00 20.81           C  
-ATOM   1222  CG2 VAL B  32      13.688  -4.268  15.654  1.00 17.71           C  
-ATOM   1223  H   VAL B  32      14.631  -1.528  17.446  1.00 15.00           H  
-ATOM   1224  N   LEU B  33      17.572  -1.694  14.804  1.00 15.98           N  
-ATOM   1225  CA  LEU B  33      18.335  -0.620  14.173  1.00 17.26           C  
-ATOM   1226  C   LEU B  33      18.650  -0.882  12.714  1.00 19.49           C  
-ATOM   1227  O   LEU B  33      18.729  -2.021  12.283  1.00 18.48           O  
-ATOM   1228  CB  LEU B  33      19.691  -0.414  14.820  1.00 18.66           C  
-ATOM   1229  CG  LEU B  33      19.649  -0.154  16.318  1.00 23.81           C  
-ATOM   1230  CD1 LEU B  33      21.070   0.119  16.750  1.00 25.94           C  
-ATOM   1231  CD2 LEU B  33      18.734   1.011  16.705  1.00 25.06           C  
-ATOM   1232  H   LEU B  33      17.960  -2.614  14.908  1.00 15.00           H  
-ATOM   1233  N   GLU B  34      18.816   0.210  11.969  1.00 20.07           N  
-ATOM   1234  CA  GLU B  34      19.234   0.099  10.569  1.00 23.73           C  
-ATOM   1235  C   GLU B  34      20.545  -0.652  10.417  1.00 24.83           C  
-ATOM   1236  O   GLU B  34      21.420  -0.745  11.280  1.00 21.85           O  
-ATOM   1237  CB  GLU B  34      19.407   1.498   9.951  1.00 28.18           C  
-ATOM   1238  CG  GLU B  34      20.582   2.223  10.660  1.00 39.02           C  
-ATOM   1239  CD  GLU B  34      20.903   3.622  10.158  1.00 43.47           C  
-ATOM   1240  OE1 GLU B  34      20.214   4.575  10.540  1.00 45.51           O  
-ATOM   1241  OE2 GLU B  34      21.881   3.756   9.417  1.00 48.37           O  
-ATOM   1242  H   GLU B  34      18.715   1.100  12.421  1.00 15.00           H  
-ATOM   1243  N   GLU B  35      20.661  -1.205   9.229  1.00 26.03           N  
-ATOM   1244  CA  GLU B  35      21.894  -1.934   8.968  1.00 27.61           C  
-ATOM   1245  C   GLU B  35      23.193  -1.150   9.262  1.00 27.60           C  
-ATOM   1246  O   GLU B  35      23.420   0.000   8.924  1.00 26.05           O  
-ATOM   1247  CB  GLU B  35      21.746  -2.464   7.533  1.00 30.92           C  
-ATOM   1248  CG  GLU B  35      22.825  -3.396   7.023  1.00 32.11           C  
-ATOM   1249  CD  GLU B  35      22.813  -4.637   7.854  1.00 34.47           C  
-ATOM   1250  OE1 GLU B  35      21.765  -5.269   7.975  1.00 33.82           O  
-ATOM   1251  OE2 GLU B  35      23.874  -4.960   8.378  1.00 39.04           O  
-ATOM   1252  H   GLU B  35      19.889  -1.152   8.590  1.00 15.00           H  
-ATOM   1253  N   MET B  36      24.026  -1.847  10.013  1.00 28.33           N  
-ATOM   1254  CA  MET B  36      25.357  -1.350  10.383  1.00 31.03           C  
-ATOM   1255  C   MET B  36      26.233  -2.476  10.877  1.00 30.62           C  
-ATOM   1256  O   MET B  36      25.775  -3.544  11.262  1.00 28.27           O  
-ATOM   1257  CB  MET B  36      25.294  -0.261  11.464  1.00 33.94           C  
-ATOM   1258  CG  MET B  36      24.675  -0.683  12.806  1.00 41.05           C  
-ATOM   1259  SD  MET B  36      24.317   0.725  13.884  1.00 43.55           S  
-ATOM   1260  CE  MET B  36      26.024   1.184  14.202  1.00 45.92           C  
-ATOM   1261  H   MET B  36      23.651  -2.653  10.460  1.00 15.00           H  
-ATOM   1262  N   SER B  37      27.527  -2.245  10.810  1.00 33.31           N  
-ATOM   1263  CA  SER B  37      28.397  -3.384  11.159  1.00 36.66           C  
-ATOM   1264  C   SER B  37      29.134  -3.251  12.452  1.00 36.09           C  
-ATOM   1265  O   SER B  37      30.290  -2.885  12.557  1.00 38.36           O  
-ATOM   1266  CB  SER B  37      29.432  -3.705  10.078  1.00 39.08           C  
-ATOM   1267  OG  SER B  37      30.007  -2.480   9.608  1.00 44.49           O  
-ATOM   1268  H   SER B  37      27.904  -1.392  10.458  1.00  0.00           H  
-ATOM   1269  HG  SER B  37      30.867  -2.313  10.024  1.00  0.00           H  
-ATOM   1270  N   LEU B  38      28.379  -3.613  13.451  1.00 35.19           N  
-ATOM   1271  CA  LEU B  38      28.919  -3.787  14.793  1.00 34.52           C  
-ATOM   1272  C   LEU B  38      29.894  -4.949  14.906  1.00 35.74           C  
-ATOM   1273  O   LEU B  38      29.648  -6.019  14.350  1.00 34.28           O  
-ATOM   1274  CB  LEU B  38      27.753  -4.077  15.727  1.00 33.65           C  
-ATOM   1275  CG  LEU B  38      26.793  -2.899  15.863  1.00 34.50           C  
-ATOM   1276  CD1 LEU B  38      25.521  -3.309  16.620  1.00 33.61           C  
-ATOM   1277  CD2 LEU B  38      27.520  -1.685  16.459  1.00 34.16           C  
-ATOM   1278  H   LEU B  38      27.440  -3.891  13.262  1.00 15.00           H  
-ATOM   1279  N   PRO B  39      30.994  -4.694  15.648  1.00 36.84           N  
-ATOM   1280  CA  PRO B  39      31.801  -5.814  16.111  1.00 37.58           C  
-ATOM   1281  C   PRO B  39      31.047  -6.622  17.159  1.00 38.47           C  
-ATOM   1282  O   PRO B  39      30.112  -6.210  17.849  1.00 38.62           O  
-ATOM   1283  CB  PRO B  39      33.049  -5.102  16.668  1.00 36.48           C  
-ATOM   1284  CG  PRO B  39      32.573  -3.765  17.182  1.00 35.67           C  
-ATOM   1285  CD  PRO B  39      31.481  -3.407  16.173  1.00 37.70           C  
-ATOM   1286  N   GLY B  40      31.496  -7.852  17.238  1.00 39.13           N  
-ATOM   1287  CA  GLY B  40      30.709  -8.693  18.115  1.00 41.22           C  
-ATOM   1288  C   GLY B  40      30.154  -9.920  17.448  1.00 43.72           C  
-ATOM   1289  O   GLY B  40      30.077 -10.101  16.246  1.00 44.05           O  
-ATOM   1290  H   GLY B  40      32.265  -8.146  16.670  1.00 15.00           H  
-ATOM   1291  N   ARG B  41      29.784 -10.818  18.325  1.00 45.31           N  
-ATOM   1292  CA  ARG B  41      29.124 -11.998  17.777  1.00 46.63           C  
-ATOM   1293  C   ARG B  41      27.617 -11.755  17.566  1.00 43.42           C  
-ATOM   1294  O   ARG B  41      26.987 -10.994  18.282  1.00 43.37           O  
-ATOM   1295  CB  ARG B  41      29.373 -13.166  18.757  1.00 52.67           C  
-ATOM   1296  CG  ARG B  41      30.849 -13.367  19.142  1.00 59.19           C  
-ATOM   1297  CD  ARG B  41      31.220 -12.842  20.540  1.00 65.64           C  
-ATOM   1298  NE  ARG B  41      32.630 -12.436  20.567  1.00 69.32           N  
-ATOM   1299  CZ  ARG B  41      32.933 -11.139  20.696  1.00 70.53           C  
-ATOM   1300  NH1 ARG B  41      31.994 -10.243  21.048  1.00 70.54           N  
-ATOM   1301  NH2 ARG B  41      34.195 -10.756  20.453  1.00 71.91           N  
-ATOM   1302  H   ARG B  41      29.740 -10.597  19.294  1.00  0.00           H  
-ATOM   1303  HE  ARG B  41      33.344 -13.111  20.382  1.00  0.00           H  
-ATOM   1304 HH11 ARG B  41      31.055 -10.539  21.224  1.00  0.00           H  
-ATOM   1305 HH12 ARG B  41      32.229  -9.269  21.135  1.00  0.00           H  
-ATOM   1306 HH21 ARG B  41      34.868 -11.452  20.205  1.00  0.00           H  
-ATOM   1307 HH22 ARG B  41      34.485  -9.788  20.509  1.00  0.00           H  
-ATOM   1308  N   TRP B  42      27.053 -12.419  16.581  1.00 39.75           N  
-ATOM   1309  CA  TRP B  42      25.604 -12.269  16.472  1.00 37.55           C  
-ATOM   1310  C   TRP B  42      24.818 -13.564  16.313  1.00 35.39           C  
-ATOM   1311  O   TRP B  42      25.334 -14.613  15.992  1.00 36.46           O  
-ATOM   1312  CB  TRP B  42      25.274 -11.248  15.370  1.00 37.24           C  
-ATOM   1313  CG  TRP B  42      25.788 -11.675  14.018  1.00 40.31           C  
-ATOM   1314  CD1 TRP B  42      27.020 -11.307  13.459  1.00 41.97           C  
-ATOM   1315  CD2 TRP B  42      25.166 -12.507  13.065  1.00 40.73           C  
-ATOM   1316  NE1 TRP B  42      27.216 -11.853  12.226  1.00 43.98           N  
-ATOM   1317  CE2 TRP B  42      26.110 -12.603  11.921  1.00 42.29           C  
-ATOM   1318  CE3 TRP B  42      23.932 -13.176  12.991  1.00 41.69           C  
-ATOM   1319  CZ2 TRP B  42      25.741 -13.365  10.799  1.00 42.63           C  
-ATOM   1320  CZ3 TRP B  42      23.598 -13.927  11.849  1.00 42.12           C  
-ATOM   1321  CH2 TRP B  42      24.489 -14.020  10.766  1.00 43.16           C  
-ATOM   1322  H   TRP B  42      27.587 -12.982  15.957  1.00 15.00           H  
-ATOM   1323  HE1 TRP B  42      28.001 -11.707  11.659  1.00 15.00           H  
-ATOM   1324  N   LYS B  43      23.533 -13.476  16.540  1.00 34.00           N  
-ATOM   1325  CA  LYS B  43      22.685 -14.618  16.192  1.00 33.92           C  
-ATOM   1326  C   LYS B  43      21.664 -14.214  15.164  1.00 32.42           C  
-ATOM   1327  O   LYS B  43      21.158 -13.105  15.184  1.00 30.55           O  
-ATOM   1328  CB  LYS B  43      21.872 -15.067  17.400  1.00 38.77           C  
-ATOM   1329  CG  LYS B  43      22.714 -15.480  18.589  1.00 45.28           C  
-ATOM   1330  CD  LYS B  43      21.949 -15.191  19.875  1.00 51.26           C  
-ATOM   1331  CE  LYS B  43      22.878 -15.230  21.091  1.00 54.47           C  
-ATOM   1332  NZ  LYS B  43      22.115 -14.861  22.297  1.00 60.16           N  
-ATOM   1333  H   LYS B  43      23.180 -12.628  16.945  1.00 15.00           H  
-ATOM   1334  HZ1 LYS B  43      21.328 -15.528  22.428  1.00 15.00           H  
-ATOM   1335  HZ2 LYS B  43      22.744 -14.901  23.124  1.00 15.00           H  
-ATOM   1336  HZ3 LYS B  43      21.741 -13.896  22.193  1.00 15.00           H  
-ATOM   1337  N   PRO B  44      21.349 -15.123  14.263  1.00 30.98           N  
-ATOM   1338  CA  PRO B  44      20.285 -14.784  13.311  1.00 29.85           C  
-ATOM   1339  C   PRO B  44      18.911 -14.818  13.970  1.00 28.31           C  
-ATOM   1340  O   PRO B  44      18.632 -15.579  14.883  1.00 29.23           O  
-ATOM   1341  CB  PRO B  44      20.475 -15.899  12.271  1.00 30.33           C  
-ATOM   1342  CG  PRO B  44      20.961 -17.109  13.071  1.00 30.08           C  
-ATOM   1343  CD  PRO B  44      21.860 -16.484  14.125  1.00 31.51           C  
-ATOM   1344  N   LYS B  45      18.044 -13.964  13.480  1.00 25.93           N  
-ATOM   1345  CA  LYS B  45      16.710 -13.983  14.082  1.00 24.97           C  
-ATOM   1346  C   LYS B  45      15.621 -13.455  13.145  1.00 23.08           C  
-ATOM   1347  O   LYS B  45      15.865 -12.679  12.240  1.00 20.96           O  
-ATOM   1348  CB  LYS B  45      16.792 -13.137  15.370  1.00 27.44           C  
-ATOM   1349  CG  LYS B  45      15.709 -13.470  16.372  1.00 32.42           C  
-ATOM   1350  CD  LYS B  45      15.595 -12.387  17.431  1.00 38.13           C  
-ATOM   1351  CE  LYS B  45      14.521 -12.772  18.443  1.00 42.26           C  
-ATOM   1352  NZ  LYS B  45      14.496 -11.748  19.497  1.00 48.41           N  
-ATOM   1353  H   LYS B  45      18.342 -13.236  12.857  1.00 15.00           H  
-ATOM   1354  HZ1 LYS B  45      15.436 -11.674  19.935  1.00 15.00           H  
-ATOM   1355  HZ2 LYS B  45      14.233 -10.831  19.081  1.00 15.00           H  
-ATOM   1356  HZ3 LYS B  45      13.796 -12.013  20.218  1.00 15.00           H  
-ATOM   1357  N   MET B  46      14.391 -13.893  13.369  1.00 23.97           N  
-ATOM   1358  CA  MET B  46      13.262 -13.293  12.631  1.00 25.49           C  
-ATOM   1359  C   MET B  46      12.261 -12.533  13.489  1.00 25.42           C  
-ATOM   1360  O   MET B  46      11.747 -13.046  14.478  1.00 25.91           O  
-ATOM   1361  CB  MET B  46      12.532 -14.357  11.798  1.00 26.83           C  
-ATOM   1362  CG  MET B  46      13.337 -14.345  10.492  1.00 29.61           C  
-ATOM   1363  SD  MET B  46      13.031 -15.701   9.408  1.00 38.58           S  
-ATOM   1364  CE  MET B  46      11.414 -15.225   8.761  1.00 30.39           C  
-ATOM   1365  H   MET B  46      14.257 -14.582  14.086  1.00 15.00           H  
-ATOM   1366  N   ILE B  47      12.026 -11.281  13.090  1.00 22.23           N  
-ATOM   1367  CA  ILE B  47      10.983 -10.531  13.817  1.00 20.36           C  
-ATOM   1368  C   ILE B  47       9.826 -10.051  12.963  1.00 17.62           C  
-ATOM   1369  O   ILE B  47       9.935  -9.818  11.774  1.00 18.53           O  
-ATOM   1370  CB  ILE B  47      11.531  -9.363  14.634  1.00 21.39           C  
-ATOM   1371  CG1 ILE B  47      12.597  -8.588  13.920  1.00 22.83           C  
-ATOM   1372  CG2 ILE B  47      11.978  -9.749  16.032  1.00 24.94           C  
-ATOM   1373  CD1 ILE B  47      11.907  -7.388  13.280  1.00 28.16           C  
-ATOM   1374  H   ILE B  47      12.478 -10.932  12.264  1.00 15.00           H  
-ATOM   1375  N   GLY B  48       8.684  -9.989  13.597  1.00 15.99           N  
-ATOM   1376  CA  GLY B  48       7.481  -9.730  12.843  1.00 15.20           C  
-ATOM   1377  C   GLY B  48       6.919  -8.370  13.101  1.00 17.12           C  
-ATOM   1378  O   GLY B  48       7.176  -7.704  14.095  1.00 17.54           O  
-ATOM   1379  H   GLY B  48       8.643 -10.159  14.583  1.00 15.00           H  
-ATOM   1380  N   GLY B  49       6.115  -7.975  12.160  1.00 16.27           N  
-ATOM   1381  CA  GLY B  49       5.476  -6.676  12.329  1.00 18.73           C  
-ATOM   1382  C   GLY B  49       4.130  -6.673  11.661  1.00 20.54           C  
-ATOM   1383  O   GLY B  49       3.561  -7.726  11.456  1.00 21.43           O  
-ATOM   1384  H   GLY B  49       6.072  -8.503  11.309  1.00 15.00           H  
-ATOM   1385  N   ILE B  50       3.609  -5.530  11.281  1.00 20.33           N  
-ATOM   1386  CA  ILE B  50       2.256  -5.662  10.751  1.00 22.66           C  
-ATOM   1387  C   ILE B  50       2.077  -6.490   9.448  1.00 23.68           C  
-ATOM   1388  O   ILE B  50       1.107  -7.208   9.220  1.00 25.60           O  
-ATOM   1389  CB  ILE B  50       1.607  -4.245  10.733  1.00 24.63           C  
-ATOM   1390  CG1 ILE B  50       0.091  -4.343  10.852  1.00 27.32           C  
-ATOM   1391  CG2 ILE B  50       2.001  -3.387   9.539  1.00 22.28           C  
-ATOM   1392  CD1 ILE B  50      -0.611  -3.039  11.165  1.00 30.11           C  
-ATOM   1393  H   ILE B  50       4.085  -4.661  11.445  1.00 15.00           H  
-ATOM   1394  N   GLY B  51       3.090  -6.393   8.586  1.00 22.33           N  
-ATOM   1395  CA  GLY B  51       2.899  -7.037   7.279  1.00 23.13           C  
-ATOM   1396  C   GLY B  51       3.589  -8.389   7.096  1.00 23.87           C  
-ATOM   1397  O   GLY B  51       3.601  -8.981   6.038  1.00 25.77           O  
-ATOM   1398  H   GLY B  51       3.928  -5.901   8.839  1.00 15.00           H  
-ATOM   1399  N   GLY B  52       4.192  -8.871   8.168  1.00 21.26           N  
-ATOM   1400  CA  GLY B  52       5.003 -10.073   8.059  1.00 18.92           C  
-ATOM   1401  C   GLY B  52       6.336  -9.957   8.785  1.00 18.68           C  
-ATOM   1402  O   GLY B  52       6.531  -9.151   9.681  1.00 16.81           O  
-ATOM   1403  H   GLY B  52       4.096  -8.385   9.036  1.00 15.00           H  
-ATOM   1404  N   PHE B  53       7.251 -10.813   8.393  1.00 18.57           N  
-ATOM   1405  CA  PHE B  53       8.524 -10.946   9.137  1.00 19.13           C  
-ATOM   1406  C   PHE B  53       9.756 -10.527   8.385  1.00 20.58           C  
-ATOM   1407  O   PHE B  53       9.846 -10.615   7.177  1.00 23.17           O  
-ATOM   1408  CB  PHE B  53       8.813 -12.406   9.535  1.00 15.80           C  
-ATOM   1409  CG  PHE B  53       7.882 -12.919  10.595  1.00 16.73           C  
-ATOM   1410  CD1 PHE B  53       6.511 -13.129  10.316  1.00 17.12           C  
-ATOM   1411  CD2 PHE B  53       8.395 -13.127  11.887  1.00 15.33           C  
-ATOM   1412  CE1 PHE B  53       5.640 -13.544  11.341  1.00 16.71           C  
-ATOM   1413  CE2 PHE B  53       7.511 -13.539  12.908  1.00 18.47           C  
-ATOM   1414  CZ  PHE B  53       6.138 -13.744  12.639  1.00 15.71           C  
-ATOM   1415  H   PHE B  53       7.085 -11.380   7.588  1.00 15.00           H  
-ATOM   1416  N   ILE B  54      10.751 -10.103   9.112  1.00 20.93           N  
-ATOM   1417  CA  ILE B  54      12.009  -9.869   8.409  1.00 19.69           C  
-ATOM   1418  C   ILE B  54      13.128 -10.534   9.141  1.00 20.89           C  
-ATOM   1419  O   ILE B  54      13.031 -10.808  10.335  1.00 19.81           O  
-ATOM   1420  CB  ILE B  54      12.350  -8.376   8.319  1.00 19.52           C  
-ATOM   1421  CG1 ILE B  54      12.464  -7.685   9.673  1.00 20.60           C  
-ATOM   1422  CG2 ILE B  54      11.379  -7.576   7.450  1.00 21.33           C  
-ATOM   1423  CD1 ILE B  54      12.992  -6.254   9.502  1.00 23.65           C  
-ATOM   1424  H   ILE B  54      10.636  -9.969  10.100  1.00 15.00           H  
-ATOM   1425  N   LYS B  55      14.203 -10.744   8.392  1.00 21.33           N  
-ATOM   1426  CA  LYS B  55      15.393 -11.283   9.037  1.00 22.83           C  
-ATOM   1427  C   LYS B  55      16.363 -10.250   9.560  1.00 23.13           C  
-ATOM   1428  O   LYS B  55      16.721  -9.275   8.914  1.00 23.20           O  
-ATOM   1429  CB  LYS B  55      16.156 -12.188   8.086  1.00 29.06           C  
-ATOM   1430  CG  LYS B  55      15.355 -13.358   7.506  1.00 36.64           C  
-ATOM   1431  CD  LYS B  55      16.232 -14.242   6.592  1.00 44.69           C  
-ATOM   1432  CE  LYS B  55      15.507 -15.333   5.757  1.00 48.01           C  
-ATOM   1433  NZ  LYS B  55      14.655 -14.770   4.687  1.00 50.11           N  
-ATOM   1434  H   LYS B  55      14.197 -10.468   7.426  1.00 15.00           H  
-ATOM   1435  HZ1 LYS B  55      13.936 -14.148   5.107  1.00 15.00           H  
-ATOM   1436  HZ2 LYS B  55      15.243 -14.224   4.026  1.00 15.00           H  
-ATOM   1437  HZ3 LYS B  55      14.187 -15.546   4.176  1.00 15.00           H  
-ATOM   1438  N   VAL B  56      16.791 -10.502  10.799  1.00 21.91           N  
-ATOM   1439  CA  VAL B  56      17.748  -9.615  11.489  1.00 19.59           C  
-ATOM   1440  C   VAL B  56      18.921 -10.330  12.159  1.00 19.84           C  
-ATOM   1441  O   VAL B  56      18.907 -11.524  12.425  1.00 20.10           O  
-ATOM   1442  CB  VAL B  56      16.992  -8.785  12.551  1.00 17.56           C  
-ATOM   1443  CG1 VAL B  56      15.948  -7.880  11.863  1.00 16.59           C  
-ATOM   1444  CG2 VAL B  56      16.364  -9.680  13.645  1.00 15.55           C  
-ATOM   1445  H   VAL B  56      16.429 -11.308  11.274  1.00 15.00           H  
-ATOM   1446  N   ARG B  57      19.944  -9.542  12.480  1.00 20.58           N  
-ATOM   1447  CA  ARG B  57      20.991 -10.076  13.367  1.00 19.72           C  
-ATOM   1448  C   ARG B  57      20.935  -9.533  14.785  1.00 21.06           C  
-ATOM   1449  O   ARG B  57      20.812  -8.353  15.050  1.00 20.17           O  
-ATOM   1450  CB  ARG B  57      22.375  -9.796  12.810  1.00 18.36           C  
-ATOM   1451  CG  ARG B  57      22.397 -10.178  11.328  1.00 20.74           C  
-ATOM   1452  CD  ARG B  57      23.734  -9.981  10.621  1.00 25.64           C  
-ATOM   1453  NE  ARG B  57      24.365  -8.690  10.908  1.00 27.80           N  
-ATOM   1454  CZ  ARG B  57      24.071  -7.549  10.254  1.00 29.33           C  
-ATOM   1455  NH1 ARG B  57      23.128  -7.569   9.283  1.00 28.47           N  
-ATOM   1456  NH2 ARG B  57      24.752  -6.448  10.643  1.00 26.22           N  
-ATOM   1457  H   ARG B  57      19.934  -8.590  12.161  1.00 15.00           H  
-ATOM   1458  HE  ARG B  57      25.038  -8.659  11.647  1.00 15.00           H  
-ATOM   1459 HH11 ARG B  57      22.705  -8.445   9.050  1.00  0.00           H  
-ATOM   1460 HH12 ARG B  57      22.821  -6.759   8.790  1.00  0.00           H  
-ATOM   1461 HH21 ARG B  57      25.452  -6.577  11.346  1.00  0.00           H  
-ATOM   1462 HH22 ARG B  57      24.616  -5.518  10.302  1.00  0.00           H  
-ATOM   1463  N   GLN B  58      20.984 -10.467  15.705  1.00 21.47           N  
-ATOM   1464  CA  GLN B  58      20.904 -10.160  17.138  1.00 23.59           C  
-ATOM   1465  C   GLN B  58      22.256  -9.994  17.847  1.00 24.05           C  
-ATOM   1466  O   GLN B  58      23.054 -10.907  17.968  1.00 24.41           O  
-ATOM   1467  CB  GLN B  58      20.125 -11.288  17.830  1.00 21.35           C  
-ATOM   1468  CG  GLN B  58      19.909 -10.931  19.279  1.00 24.42           C  
-ATOM   1469  CD  GLN B  58      19.322 -12.061  20.050  1.00 28.04           C  
-ATOM   1470  OE1 GLN B  58      19.716 -12.372  21.150  1.00 34.70           O  
-ATOM   1471  NE2 GLN B  58      18.295 -12.663  19.533  1.00 30.32           N  
-ATOM   1472  H   GLN B  58      21.082 -11.417  15.401  1.00 15.00           H  
-ATOM   1473 HE21 GLN B  58      17.840 -13.336  20.100  1.00  0.00           H  
-ATOM   1474 HE22 GLN B  58      17.986 -12.497  18.601  1.00  0.00           H  
-ATOM   1475  N   TYR B  59      22.434  -8.788  18.354  1.00 24.85           N  
-ATOM   1476  CA  TYR B  59      23.576  -8.463  19.213  1.00 25.95           C  
-ATOM   1477  C   TYR B  59      23.171  -8.246  20.680  1.00 27.01           C  
-ATOM   1478  O   TYR B  59      22.213  -7.562  21.022  1.00 26.97           O  
-ATOM   1479  CB  TYR B  59      24.238  -7.172  18.681  1.00 26.31           C  
-ATOM   1480  CG  TYR B  59      24.807  -7.289  17.265  1.00 28.82           C  
-ATOM   1481  CD1 TYR B  59      23.987  -6.995  16.155  1.00 26.81           C  
-ATOM   1482  CD2 TYR B  59      26.160  -7.668  17.064  1.00 29.08           C  
-ATOM   1483  CE1 TYR B  59      24.497  -7.070  14.850  1.00 29.96           C  
-ATOM   1484  CE2 TYR B  59      26.678  -7.746  15.759  1.00 31.39           C  
-ATOM   1485  CZ  TYR B  59      25.840  -7.446  14.656  1.00 32.51           C  
-ATOM   1486  OH  TYR B  59      26.331  -7.528  13.368  1.00 37.60           O  
-ATOM   1487  H   TYR B  59      21.751  -8.076  18.165  1.00 15.00           H  
-ATOM   1488  HH  TYR B  59      27.274  -7.723  13.442  1.00 15.00           H  
-ATOM   1489  N   ASP B  60      23.920  -8.857  21.572  1.00 28.03           N  
-ATOM   1490  CA  ASP B  60      23.588  -8.627  22.993  1.00 30.18           C  
-ATOM   1491  C   ASP B  60      24.514  -7.674  23.700  1.00 29.96           C  
-ATOM   1492  O   ASP B  60      25.626  -7.470  23.250  1.00 28.71           O  
-ATOM   1493  CB  ASP B  60      23.654  -9.949  23.751  1.00 33.28           C  
-ATOM   1494  CG  ASP B  60      22.603 -10.855  23.168  1.00 39.99           C  
-ATOM   1495  OD1 ASP B  60      21.448 -10.441  23.075  1.00 42.87           O  
-ATOM   1496  OD2 ASP B  60      22.939 -11.974  22.782  1.00 45.24           O  
-ATOM   1497  H   ASP B  60      24.716  -9.378  21.278  1.00 15.00           H  
-ATOM   1498  N   GLN B  61      24.062  -7.108  24.817  1.00 28.21           N  
-ATOM   1499  CA  GLN B  61      24.929  -6.218  25.611  1.00 28.47           C  
-ATOM   1500  C   GLN B  61      25.393  -4.930  24.973  1.00 27.25           C  
-ATOM   1501  O   GLN B  61      26.453  -4.417  25.280  1.00 28.59           O  
-ATOM   1502  CB  GLN B  61      26.260  -6.878  26.022  1.00 33.74           C  
-ATOM   1503  CG  GLN B  61      26.243  -8.258  26.667  1.00 39.66           C  
-ATOM   1504  CD  GLN B  61      25.983  -8.049  28.114  1.00 44.70           C  
-ATOM   1505  OE1 GLN B  61      24.871  -7.846  28.572  1.00 45.45           O  
-ATOM   1506  NE2 GLN B  61      27.074  -8.070  28.849  1.00 44.76           N  
-ATOM   1507  H   GLN B  61      23.126  -7.308  25.107  1.00 15.00           H  
-ATOM   1508 HE21 GLN B  61      26.949  -7.898  29.821  1.00  0.00           H  
-ATOM   1509 HE22 GLN B  61      27.972  -8.225  28.456  1.00  0.00           H  
-ATOM   1510  N   ILE B  62      24.598  -4.408  24.049  1.00 26.42           N  
-ATOM   1511  CA  ILE B  62      24.997  -3.148  23.415  1.00 23.29           C  
-ATOM   1512  C   ILE B  62      24.614  -1.945  24.288  1.00 23.70           C  
-ATOM   1513  O   ILE B  62      23.505  -1.793  24.775  1.00 21.04           O  
-ATOM   1514  CB  ILE B  62      24.362  -3.061  21.975  1.00 22.50           C  
-ATOM   1515  CG1 ILE B  62      24.707  -4.255  21.094  1.00 23.55           C  
-ATOM   1516  CG2 ILE B  62      24.688  -1.823  21.133  1.00 19.92           C  
-ATOM   1517  CD1 ILE B  62      26.188  -4.245  20.670  1.00 24.92           C  
-ATOM   1518  H   ILE B  62      23.704  -4.823  23.869  1.00 15.00           H  
-ATOM   1519  N   LEU B  63      25.588  -1.064  24.449  1.00 23.73           N  
-ATOM   1520  CA  LEU B  63      25.302   0.240  25.057  1.00 25.09           C  
-ATOM   1521  C   LEU B  63      24.758   1.255  24.075  1.00 24.35           C  
-ATOM   1522  O   LEU B  63      25.352   1.628  23.077  1.00 23.63           O  
-ATOM   1523  CB  LEU B  63      26.602   0.776  25.706  1.00 26.91           C  
-ATOM   1524  CG  LEU B  63      26.625   2.093  26.541  1.00 28.69           C  
-ATOM   1525  CD1 LEU B  63      26.758   3.386  25.733  1.00 33.39           C  
-ATOM   1526  CD2 LEU B  63      25.439   2.211  27.474  1.00 29.16           C  
-ATOM   1527  H   LEU B  63      26.476  -1.257  24.025  1.00  0.00           H  
-ATOM   1528  N   ILE B  64      23.590   1.730  24.421  1.00 24.45           N  
-ATOM   1529  CA  ILE B  64      23.061   2.881  23.684  1.00 26.65           C  
-ATOM   1530  C   ILE B  64      22.801   4.024  24.636  1.00 27.12           C  
-ATOM   1531  O   ILE B  64      22.374   3.872  25.765  1.00 31.75           O  
-ATOM   1532  CB  ILE B  64      21.743   2.530  22.937  1.00 25.99           C  
-ATOM   1533  CG1 ILE B  64      21.927   1.399  21.928  1.00 26.08           C  
-ATOM   1534  CG2 ILE B  64      21.134   3.719  22.172  1.00 26.69           C  
-ATOM   1535  CD1 ILE B  64      20.654   1.123  21.131  1.00 27.40           C  
-ATOM   1536  H   ILE B  64      23.126   1.336  25.221  1.00  0.00           H  
-ATOM   1537  N   GLU B  65      23.059   5.201  24.164  1.00 26.17           N  
-ATOM   1538  CA  GLU B  65      22.658   6.303  24.994  1.00 25.80           C  
-ATOM   1539  C   GLU B  65      21.521   7.139  24.423  1.00 25.28           C  
-ATOM   1540  O   GLU B  65      21.547   7.700  23.343  1.00 27.70           O  
-ATOM   1541  CB  GLU B  65      23.941   7.047  25.272  1.00 29.78           C  
-ATOM   1542  CG  GLU B  65      23.769   8.209  26.239  1.00 42.75           C  
-ATOM   1543  CD  GLU B  65      25.118   8.856  26.547  1.00 49.95           C  
-ATOM   1544  OE1 GLU B  65      26.140   8.383  26.026  1.00 53.87           O  
-ATOM   1545  OE2 GLU B  65      25.144   9.829  27.321  1.00 53.94           O  
-ATOM   1546  H   GLU B  65      23.461   5.292  23.249  1.00 15.00           H  
-ATOM   1547  N   ILE B  66      20.463   7.198  25.178  1.00 24.01           N  
-ATOM   1548  CA  ILE B  66      19.251   7.833  24.653  1.00 24.90           C  
-ATOM   1549  C   ILE B  66      18.951   9.144  25.342  1.00 25.94           C  
-ATOM   1550  O   ILE B  66      18.648   9.211  26.537  1.00 23.26           O  
-ATOM   1551  CB  ILE B  66      18.077   6.861  24.864  1.00 26.12           C  
-ATOM   1552  CG1 ILE B  66      18.398   5.440  24.395  1.00 25.80           C  
-ATOM   1553  CG2 ILE B  66      16.717   7.332  24.276  1.00 25.96           C  
-ATOM   1554  CD1 ILE B  66      17.381   4.456  24.939  1.00 26.13           C  
-ATOM   1555  H   ILE B  66      20.487   6.756  26.080  1.00 15.00           H  
-ATOM   1556  N   CYS B  67      19.106  10.227  24.579  1.00 27.77           N  
-ATOM   1557  CA  CYS B  67      18.976  11.561  25.253  1.00 33.22           C  
-ATOM   1558  C   CYS B  67      19.703  11.695  26.607  1.00 33.23           C  
-ATOM   1559  O   CYS B  67      19.174  12.058  27.650  1.00 32.05           O  
-ATOM   1560  CB  CYS B  67      17.504  12.003  25.521  1.00 36.86           C  
-ATOM   1561  SG  CYS B  67      16.475  12.448  24.078  1.00 41.71           S  
-ATOM   1562  H   CYS B  67      19.243  10.124  23.589  1.00 15.00           H  
-ATOM   1563  N   GLY B  68      20.971  11.285  26.556  1.00 34.13           N  
-ATOM   1564  CA  GLY B  68      21.779  11.327  27.778  1.00 33.10           C  
-ATOM   1565  C   GLY B  68      21.657  10.166  28.744  1.00 32.52           C  
-ATOM   1566  O   GLY B  68      22.447   9.978  29.645  1.00 36.48           O  
-ATOM   1567  H   GLY B  68      21.344  10.979  25.683  1.00 15.00           H  
-ATOM   1568  N   HIS B  69      20.631   9.365  28.553  1.00 29.88           N  
-ATOM   1569  CA  HIS B  69      20.490   8.197  29.436  1.00 28.08           C  
-ATOM   1570  C   HIS B  69      21.039   6.902  28.900  1.00 26.52           C  
-ATOM   1571  O   HIS B  69      20.663   6.457  27.830  1.00 26.19           O  
-ATOM   1572  CB  HIS B  69      19.037   7.878  29.684  1.00 26.73           C  
-ATOM   1573  CG  HIS B  69      18.383   9.049  30.322  1.00 28.00           C  
-ATOM   1574  ND1 HIS B  69      17.982   9.060  31.591  1.00 29.89           N  
-ATOM   1575  CD2 HIS B  69      18.060  10.261  29.723  1.00 27.83           C  
-ATOM   1576  CE1 HIS B  69      17.394  10.271  31.817  1.00 30.06           C  
-ATOM   1577  NE2 HIS B  69      17.447  11.006  30.670  1.00 30.20           N  
-ATOM   1578  H   HIS B  69      20.008   9.518  27.782  1.00 15.00           H  
-ATOM   1579  HD1 HIS B  69      18.072   8.341  32.257  1.00 15.00           H  
-ATOM   1580  HE2 HIS B  69      17.121  11.919  30.552  1.00 15.00           H  
-ATOM   1581  N   LYS B  70      21.921   6.291  29.655  1.00 24.94           N  
-ATOM   1582  CA  LYS B  70      22.410   5.015  29.135  1.00 24.78           C  
-ATOM   1583  C   LYS B  70      21.517   3.790  29.327  1.00 24.82           C  
-ATOM   1584  O   LYS B  70      20.794   3.627  30.299  1.00 24.63           O  
-ATOM   1585  CB  LYS B  70      23.797   4.742  29.685  1.00 24.68           C  
-ATOM   1586  CG  LYS B  70      24.661   5.953  29.420  1.00 25.78           C  
-ATOM   1587  CD  LYS B  70      26.075   5.636  29.824  1.00 30.03           C  
-ATOM   1588  CE  LYS B  70      27.003   6.821  29.652  1.00 32.72           C  
-ATOM   1589  NZ  LYS B  70      28.363   6.282  29.750  1.00 37.79           N  
-ATOM   1590  H   LYS B  70      22.160   6.636  30.568  1.00 15.00           H  
-ATOM   1591  HZ1 LYS B  70      28.484   5.523  29.049  1.00 15.00           H  
-ATOM   1592  HZ2 LYS B  70      29.051   7.039  29.563  1.00 15.00           H  
-ATOM   1593  HZ3 LYS B  70      28.520   5.897  30.703  1.00 15.00           H  
-ATOM   1594  N   ALA B  71      21.591   2.920  28.331  1.00 21.69           N  
-ATOM   1595  CA  ALA B  71      20.872   1.663  28.458  1.00 23.01           C  
-ATOM   1596  C   ALA B  71      21.728   0.584  27.825  1.00 22.74           C  
-ATOM   1597  O   ALA B  71      22.520   0.820  26.926  1.00 25.71           O  
-ATOM   1598  CB  ALA B  71      19.447   1.780  27.841  1.00 18.91           C  
-ATOM   1599  H   ALA B  71      22.046   3.179  27.474  1.00 15.00           H  
-ATOM   1600  N   ILE B  72      21.611  -0.605  28.347  1.00 22.08           N  
-ATOM   1601  CA  ILE B  72      22.436  -1.670  27.799  1.00 22.83           C  
-ATOM   1602  C   ILE B  72      21.599  -2.898  27.546  1.00 22.56           C  
-ATOM   1603  O   ILE B  72      20.908  -3.406  28.407  1.00 24.89           O  
-ATOM   1604  CB  ILE B  72      23.646  -2.032  28.709  1.00 24.72           C  
-ATOM   1605  CG1 ILE B  72      24.711  -0.947  28.873  1.00 26.21           C  
-ATOM   1606  CG2 ILE B  72      24.431  -3.242  28.204  1.00 25.26           C  
-ATOM   1607  CD1 ILE B  72      24.365   0.104  29.911  1.00 33.54           C  
-ATOM   1608  H   ILE B  72      20.975  -0.742  29.113  1.00 15.00           H  
-ATOM   1609  N   GLY B  73      21.642  -3.374  26.320  1.00 21.38           N  
-ATOM   1610  CA  GLY B  73      20.831  -4.559  26.043  1.00 21.40           C  
-ATOM   1611  C   GLY B  73      20.922  -5.154  24.649  1.00 20.57           C  
-ATOM   1612  O   GLY B  73      21.839  -4.930  23.884  1.00 19.40           O  
-ATOM   1613  H   GLY B  73      22.213  -2.908  25.636  1.00 15.00           H  
-ATOM   1614  N   THR B  74      19.912  -5.938  24.347  1.00 20.58           N  
-ATOM   1615  CA  THR B  74      19.905  -6.562  23.013  1.00 22.47           C  
-ATOM   1616  C   THR B  74      19.380  -5.629  21.939  1.00 22.68           C  
-ATOM   1617  O   THR B  74      18.333  -4.998  22.043  1.00 20.99           O  
-ATOM   1618  CB  THR B  74      19.034  -7.819  22.973  1.00 22.53           C  
-ATOM   1619  OG1 THR B  74      19.517  -8.731  23.942  1.00 27.08           O  
-ATOM   1620  CG2 THR B  74      19.005  -8.550  21.648  1.00 22.10           C  
-ATOM   1621  H   THR B  74      19.180  -6.080  25.010  1.00 15.00           H  
-ATOM   1622  HG1 THR B  74      19.370  -9.628  23.615  1.00 15.00           H  
-ATOM   1623  N   VAL B  75      20.153  -5.593  20.872  1.00 21.82           N  
-ATOM   1624  CA  VAL B  75      19.775  -4.842  19.675  1.00 22.44           C  
-ATOM   1625  C   VAL B  75      19.716  -5.761  18.474  1.00 20.28           C  
-ATOM   1626  O   VAL B  75      20.576  -6.596  18.279  1.00 18.47           O  
-ATOM   1627  CB  VAL B  75      20.840  -3.770  19.480  1.00 25.57           C  
-ATOM   1628  CG1 VAL B  75      20.872  -3.228  18.056  1.00 28.58           C  
-ATOM   1629  CG2 VAL B  75      20.629  -2.664  20.521  1.00 24.42           C  
-ATOM   1630  H   VAL B  75      21.005  -6.126  20.892  1.00 15.00           H  
-ATOM   1631  N   LEU B  76      18.643  -5.589  17.709  1.00 19.47           N  
-ATOM   1632  CA  LEU B  76      18.480  -6.309  16.432  1.00 20.17           C  
-ATOM   1633  C   LEU B  76      18.822  -5.426  15.242  1.00 19.25           C  
-ATOM   1634  O   LEU B  76      18.439  -4.271  15.153  1.00 19.53           O  
-ATOM   1635  CB  LEU B  76      17.021  -6.789  16.241  1.00 17.39           C  
-ATOM   1636  CG  LEU B  76      16.420  -7.555  17.425  1.00 19.09           C  
-ATOM   1637  CD1 LEU B  76      14.991  -7.935  17.084  1.00 20.77           C  
-ATOM   1638  CD2 LEU B  76      17.178  -8.831  17.774  1.00 20.17           C  
-ATOM   1639  H   LEU B  76      17.956  -4.904  17.964  1.00 15.00           H  
-ATOM   1640  N   VAL B  77      19.589  -5.980  14.340  1.00 19.11           N  
-ATOM   1641  CA  VAL B  77      20.017  -5.148  13.211  1.00 18.79           C  
-ATOM   1642  C   VAL B  77      19.534  -5.720  11.897  1.00 18.67           C  
-ATOM   1643  O   VAL B  77      19.693  -6.891  11.604  1.00 15.83           O  
-ATOM   1644  CB  VAL B  77      21.588  -5.026  13.214  1.00 20.46           C  
-ATOM   1645  CG1 VAL B  77      22.147  -4.320  11.986  1.00 20.34           C  
-ATOM   1646  CG2 VAL B  77      22.055  -4.244  14.444  1.00 18.75           C  
-ATOM   1647  H   VAL B  77      19.944  -6.903  14.505  1.00 15.00           H  
-ATOM   1648  N   GLY B  78      18.969  -4.853  11.096  1.00 19.22           N  
-ATOM   1649  CA  GLY B  78      18.536  -5.321   9.785  1.00 21.59           C  
-ATOM   1650  C   GLY B  78      17.972  -4.223   8.896  1.00 23.75           C  
-ATOM   1651  O   GLY B  78      18.117  -3.041   9.159  1.00 22.90           O  
-ATOM   1652  H   GLY B  78      18.850  -3.904  11.413  1.00 15.00           H  
-ATOM   1653  N   PRO B  79      17.318  -4.646   7.804  1.00 26.68           N  
-ATOM   1654  CA  PRO B  79      16.812  -3.653   6.819  1.00 26.00           C  
-ATOM   1655  C   PRO B  79      15.555  -2.870   7.198  1.00 26.58           C  
-ATOM   1656  O   PRO B  79      14.622  -2.754   6.424  1.00 30.92           O  
-ATOM   1657  CB  PRO B  79      16.565  -4.559   5.603  1.00 25.79           C  
-ATOM   1658  CG  PRO B  79      16.154  -5.909   6.212  1.00 26.27           C  
-ATOM   1659  CD  PRO B  79      17.111  -6.051   7.391  1.00 23.61           C  
-ATOM   1660  N   THR B  80      15.541  -2.285   8.387  1.00 25.73           N  
-ATOM   1661  CA  THR B  80      14.426  -1.363   8.758  1.00 24.33           C  
-ATOM   1662  C   THR B  80      14.495   0.058   8.157  1.00 23.41           C  
-ATOM   1663  O   THR B  80      15.568   0.635   8.034  1.00 23.12           O  
-ATOM   1664  CB  THR B  80      14.337  -1.279  10.327  1.00 23.27           C  
-ATOM   1665  OG1 THR B  80      13.228  -0.471  10.752  1.00 25.06           O  
-ATOM   1666  CG2 THR B  80      15.604  -0.740  10.965  1.00 18.88           C  
-ATOM   1667  H   THR B  80      16.355  -2.395   8.963  1.00 15.00           H  
-ATOM   1668  HG1 THR B  80      13.461   0.005  11.569  1.00 15.00           H  
-ATOM   1669  N   PRO B  81      13.344   0.639   7.785  1.00 24.73           N  
-ATOM   1670  CA  PRO B  81      13.317   2.058   7.371  1.00 26.09           C  
-ATOM   1671  C   PRO B  81      13.734   3.058   8.448  1.00 28.37           C  
-ATOM   1672  O   PRO B  81      14.331   4.110   8.232  1.00 29.26           O  
-ATOM   1673  CB  PRO B  81      11.842   2.328   7.095  1.00 27.14           C  
-ATOM   1674  CG  PRO B  81      11.191   0.976   6.904  1.00 26.94           C  
-ATOM   1675  CD  PRO B  81      12.026   0.018   7.745  1.00 26.37           C  
-ATOM   1676  N   VAL B  82      13.358   2.675   9.673  1.00 26.11           N  
-ATOM   1677  CA  VAL B  82      13.543   3.565  10.829  1.00 22.50           C  
-ATOM   1678  C   VAL B  82      14.248   2.876  12.004  1.00 19.06           C  
-ATOM   1679  O   VAL B  82      14.041   1.705  12.273  1.00 19.01           O  
-ATOM   1680  CB  VAL B  82      12.124   4.086  11.154  1.00 21.94           C  
-ATOM   1681  CG1 VAL B  82      11.130   2.994  11.488  1.00 22.20           C  
-ATOM   1682  CG2 VAL B  82      12.120   5.147  12.224  1.00 27.22           C  
-ATOM   1683  H   VAL B  82      12.930   1.780   9.803  1.00 15.00           H  
-ATOM   1684  N   ASN B  83      15.109   3.603  12.692  1.00 18.29           N  
-ATOM   1685  CA  ASN B  83      15.586   3.036  13.963  1.00 18.49           C  
-ATOM   1686  C   ASN B  83      14.502   3.056  15.077  1.00 16.12           C  
-ATOM   1687  O   ASN B  83      13.842   4.048  15.359  1.00 14.25           O  
-ATOM   1688  CB  ASN B  83      16.795   3.818  14.469  1.00 18.74           C  
-ATOM   1689  CG  ASN B  83      17.986   3.683  13.562  1.00 19.41           C  
-ATOM   1690  OD1 ASN B  83      18.460   2.636  13.223  1.00 19.89           O  
-ATOM   1691  ND2 ASN B  83      18.506   4.793  13.158  1.00 19.08           N  
-ATOM   1692  H   ASN B  83      15.263   4.552  12.418  1.00 15.00           H  
-ATOM   1693 HD21 ASN B  83      19.278   4.725  12.535  1.00  0.00           H  
-ATOM   1694 HD22 ASN B  83      18.167   5.678  13.479  1.00  0.00           H  
-ATOM   1695  N   ILE B  84      14.308   1.900  15.671  1.00 16.17           N  
-ATOM   1696  CA  ILE B  84      13.226   1.763  16.650  1.00 16.35           C  
-ATOM   1697  C   ILE B  84      13.765   1.468  18.026  1.00 16.66           C  
-ATOM   1698  O   ILE B  84      14.399   0.446  18.220  1.00 16.81           O  
-ATOM   1699  CB  ILE B  84      12.312   0.624  16.219  1.00 16.12           C  
-ATOM   1700  CG1 ILE B  84      11.594   0.991  14.929  1.00 16.70           C  
-ATOM   1701  CG2 ILE B  84      11.273   0.244  17.281  1.00 14.00           C  
-ATOM   1702  CD1 ILE B  84      11.084  -0.230  14.166  1.00 17.71           C  
-ATOM   1703  H   ILE B  84      14.868   1.111  15.399  1.00 15.00           H  
-ATOM   1704  N   ILE B  85      13.490   2.365  18.976  1.00 16.59           N  
-ATOM   1705  CA  ILE B  85      13.782   1.997  20.374  1.00 15.78           C  
-ATOM   1706  C   ILE B  85      12.559   1.366  21.064  1.00 14.25           C  
-ATOM   1707  O   ILE B  85      11.521   1.975  21.238  1.00 14.84           O  
-ATOM   1708  CB  ILE B  85      14.308   3.220  21.180  1.00 15.11           C  
-ATOM   1709  CG1 ILE B  85      15.504   3.925  20.537  1.00 14.66           C  
-ATOM   1710  CG2 ILE B  85      14.674   2.806  22.607  1.00 13.31           C  
-ATOM   1711  CD1 ILE B  85      16.644   2.964  20.192  1.00 16.67           C  
-ATOM   1712  H   ILE B  85      12.946   3.179  18.755  1.00 15.00           H  
-ATOM   1713  N   GLY B  86      12.736   0.095  21.423  1.00 14.74           N  
-ATOM   1714  CA  GLY B  86      11.655  -0.693  22.035  1.00 13.57           C  
-ATOM   1715  C   GLY B  86      11.687  -0.782  23.561  1.00 14.00           C  
-ATOM   1716  O   GLY B  86      12.553  -0.236  24.237  1.00 14.82           O  
-ATOM   1717  H   GLY B  86      13.641  -0.308  21.278  1.00 15.00           H  
-ATOM   1718  N   ARG B  87      10.714  -1.511  24.098  1.00 14.37           N  
-ATOM   1719  CA  ARG B  87      10.549  -1.551  25.572  1.00 14.24           C  
-ATOM   1720  C   ARG B  87      11.695  -2.096  26.398  1.00 14.47           C  
-ATOM   1721  O   ARG B  87      11.975  -1.663  27.500  1.00 16.86           O  
-ATOM   1722  CB  ARG B  87       9.282  -2.303  25.945  1.00 13.31           C  
-ATOM   1723  CG  ARG B  87       7.970  -1.692  25.446  1.00 11.04           C  
-ATOM   1724  CD  ARG B  87       6.792  -2.361  26.153  1.00 11.16           C  
-ATOM   1725  NE  ARG B  87       6.655  -3.767  25.778  1.00 14.13           N  
-ATOM   1726  CZ  ARG B  87       7.160  -4.803  26.472  1.00 16.85           C  
-ATOM   1727  NH1 ARG B  87       7.716  -4.600  27.675  1.00 18.32           N  
-ATOM   1728  NH2 ARG B  87       7.142  -6.014  25.909  1.00 17.79           N  
-ATOM   1729  H   ARG B  87      10.031  -1.915  23.481  1.00 15.00           H  
-ATOM   1730  HE  ARG B  87       6.230  -3.963  24.898  1.00 15.00           H  
-ATOM   1731 HH11 ARG B  87       7.605  -3.691  28.072  1.00  0.00           H  
-ATOM   1732 HH12 ARG B  87       8.260  -5.266  28.205  1.00  0.00           H  
-ATOM   1733 HH21 ARG B  87       6.677  -6.143  25.034  1.00  0.00           H  
-ATOM   1734 HH22 ARG B  87       7.599  -6.791  26.346  1.00  0.00           H  
-ATOM   1735  N   ASN B  88      12.439  -3.003  25.796  1.00 15.02           N  
-ATOM   1736  CA  ASN B  88      13.672  -3.467  26.442  1.00 16.39           C  
-ATOM   1737  C   ASN B  88      14.704  -2.412  26.827  1.00 16.93           C  
-ATOM   1738  O   ASN B  88      15.427  -2.548  27.783  1.00 19.64           O  
-ATOM   1739  CB  ASN B  88      14.351  -4.599  25.626  1.00 16.52           C  
-ATOM   1740  CG  ASN B  88      15.028  -4.068  24.367  1.00 16.84           C  
-ATOM   1741  OD1 ASN B  88      14.507  -3.252  23.644  1.00 17.08           O  
-ATOM   1742  ND2 ASN B  88      16.269  -4.424  24.170  1.00 15.19           N  
-ATOM   1743  H   ASN B  88      12.190  -3.292  24.871  1.00 15.00           H  
-ATOM   1744 HD21 ASN B  88      16.780  -4.026  23.410  1.00  0.00           H  
-ATOM   1745 HD22 ASN B  88      16.720  -5.089  24.765  1.00  0.00           H  
-ATOM   1746  N   LEU B  89      14.765  -1.343  26.064  1.00 17.28           N  
-ATOM   1747  CA  LEU B  89      15.634  -0.225  26.457  1.00 16.84           C  
-ATOM   1748  C   LEU B  89      14.923   0.978  27.129  1.00 16.53           C  
-ATOM   1749  O   LEU B  89      15.408   1.678  28.013  1.00 15.60           O  
-ATOM   1750  CB  LEU B  89      16.388   0.237  25.194  1.00 18.54           C  
-ATOM   1751  CG  LEU B  89      17.393  -0.736  24.532  1.00 22.33           C  
-ATOM   1752  CD1 LEU B  89      18.177   0.076  23.487  1.00 24.63           C  
-ATOM   1753  CD2 LEU B  89      18.380  -1.381  25.520  1.00 22.00           C  
-ATOM   1754  H   LEU B  89      14.215  -1.310  25.225  1.00 15.00           H  
-ATOM   1755  N   LEU B  90      13.662   1.162  26.712  1.00 17.28           N  
-ATOM   1756  CA  LEU B  90      12.804   2.196  27.330  1.00 16.51           C  
-ATOM   1757  C   LEU B  90      12.587   2.114  28.847  1.00 16.38           C  
-ATOM   1758  O   LEU B  90      12.609   3.087  29.593  1.00 17.26           O  
-ATOM   1759  CB  LEU B  90      11.414   2.217  26.688  1.00 15.46           C  
-ATOM   1760  CG  LEU B  90      11.361   2.758  25.234  1.00 18.57           C  
-ATOM   1761  CD1 LEU B  90       9.918   2.744  24.730  1.00 18.29           C  
-ATOM   1762  CD2 LEU B  90      11.925   4.165  25.104  1.00 18.91           C  
-ATOM   1763  H   LEU B  90      13.342   0.650  25.909  1.00 15.00           H  
-ATOM   1764  N   THR B  91      12.405   0.884  29.277  1.00 17.74           N  
-ATOM   1765  CA  THR B  91      12.308   0.598  30.718  1.00 16.90           C  
-ATOM   1766  C   THR B  91      13.540   0.992  31.465  1.00 18.63           C  
-ATOM   1767  O   THR B  91      13.473   1.589  32.523  1.00 20.99           O  
-ATOM   1768  CB  THR B  91      12.063  -0.880  31.006  1.00 16.72           C  
-ATOM   1769  OG1 THR B  91      13.064  -1.682  30.386  1.00 20.15           O  
-ATOM   1770  CG2 THR B  91      10.719  -1.363  30.539  1.00 13.06           C  
-ATOM   1771  H   THR B  91      12.315   0.144  28.608  1.00 15.00           H  
-ATOM   1772  HG1 THR B  91      12.724  -2.013  29.542  1.00 15.00           H  
-ATOM   1773  N   GLN B  92      14.689   0.745  30.843  1.00 16.98           N  
-ATOM   1774  CA  GLN B  92      15.925   1.153  31.501  1.00 19.53           C  
-ATOM   1775  C   GLN B  92      16.168   2.629  31.695  1.00 23.27           C  
-ATOM   1776  O   GLN B  92      16.824   3.068  32.636  1.00 26.10           O  
-ATOM   1777  CB  GLN B  92      17.138   0.619  30.770  1.00 17.39           C  
-ATOM   1778  CG  GLN B  92      17.008  -0.880  30.598  1.00 17.44           C  
-ATOM   1779  CD  GLN B  92      18.310  -1.369  30.042  1.00 19.38           C  
-ATOM   1780  OE1 GLN B  92      19.376  -0.825  30.234  1.00 18.78           O  
-ATOM   1781  NE2 GLN B  92      18.235  -2.443  29.307  1.00 23.18           N  
-ATOM   1782  H   GLN B  92      14.675   0.202  30.004  1.00 15.00           H  
-ATOM   1783 HE21 GLN B  92      19.103  -2.842  29.001  1.00  0.00           H  
-ATOM   1784 HE22 GLN B  92      17.356  -2.839  29.050  1.00  0.00           H  
-ATOM   1785  N   ILE B  93      15.601   3.411  30.766  1.00 24.07           N  
-ATOM   1786  CA  ILE B  93      15.706   4.858  30.975  1.00 23.42           C  
-ATOM   1787  C   ILE B  93      14.615   5.529  31.836  1.00 23.24           C  
-ATOM   1788  O   ILE B  93      14.556   6.722  32.053  1.00 23.36           O  
-ATOM   1789  CB  ILE B  93      15.932   5.595  29.637  1.00 24.50           C  
-ATOM   1790  CG1 ILE B  93      14.710   5.691  28.736  1.00 21.63           C  
-ATOM   1791  CG2 ILE B  93      17.167   5.030  28.887  1.00 21.18           C  
-ATOM   1792  CD1 ILE B  93      14.999   6.693  27.632  1.00 23.64           C  
-ATOM   1793  H   ILE B  93      15.183   2.997  29.956  1.00 15.00           H  
-ATOM   1794  N   GLY B  94      13.744   4.683  32.371  1.00 23.13           N  
-ATOM   1795  CA  GLY B  94      12.699   5.183  33.272  1.00 23.18           C  
-ATOM   1796  C   GLY B  94      11.519   5.791  32.578  1.00 22.63           C  
-ATOM   1797  O   GLY B  94      10.876   6.709  33.040  1.00 22.26           O  
-ATOM   1798  H   GLY B  94      13.829   3.705  32.177  1.00 15.00           H  
-ATOM   1799  N   CYS B  95      11.294   5.265  31.381  1.00 22.40           N  
-ATOM   1800  CA  CYS B  95      10.321   5.916  30.511  1.00 19.66           C  
-ATOM   1801  C   CYS B  95       8.920   5.423  30.767  1.00 19.56           C  
-ATOM   1802  O   CYS B  95       8.690   4.225  30.875  1.00 20.06           O  
-ATOM   1803  CB  CYS B  95      10.751   5.673  29.049  1.00 22.95           C  
-ATOM   1804  SG  CYS B  95       9.609   6.358  27.844  1.00 27.54           S  
-ATOM   1805  H   CYS B  95      11.797   4.448  31.093  1.00 15.00           H  
-ATOM   1806  N   THR B  96       7.993   6.371  30.909  1.00 17.32           N  
-ATOM   1807  CA  THR B  96       6.561   6.047  31.118  1.00 18.03           C  
-ATOM   1808  C   THR B  96       5.581   6.704  30.146  1.00 17.79           C  
-ATOM   1809  O   THR B  96       5.836   7.715  29.518  1.00 19.68           O  
-ATOM   1810  CB  THR B  96       6.003   6.352  32.562  1.00 17.91           C  
-ATOM   1811  OG1 THR B  96       6.207   7.696  32.936  1.00 16.70           O  
-ATOM   1812  CG2 THR B  96       6.582   5.484  33.670  1.00 19.85           C  
-ATOM   1813  H   THR B  96       8.287   7.329  30.888  1.00 15.00           H  
-ATOM   1814  HG1 THR B  96       5.477   8.240  32.596  1.00 15.00           H  
-ATOM   1815  N   LEU B  97       4.407   6.087  30.061  1.00 18.64           N  
-ATOM   1816  CA  LEU B  97       3.282   6.705  29.347  1.00 19.05           C  
-ATOM   1817  C   LEU B  97       2.298   7.299  30.293  1.00 19.02           C  
-ATOM   1818  O   LEU B  97       1.831   6.680  31.232  1.00 20.73           O  
-ATOM   1819  CB  LEU B  97       2.447   5.683  28.619  1.00 21.07           C  
-ATOM   1820  CG  LEU B  97       3.001   5.261  27.270  1.00 23.63           C  
-ATOM   1821  CD1 LEU B  97       2.228   4.004  26.823  1.00 24.94           C  
-ATOM   1822  CD2 LEU B  97       2.932   6.401  26.236  1.00 22.54           C  
-ATOM   1823  H   LEU B  97       4.283   5.236  30.577  1.00 15.00           H  
-ATOM   1824  N   ASN B  98       1.987   8.533  30.017  1.00 19.77           N  
-ATOM   1825  CA  ASN B  98       1.109   9.241  30.937  1.00 22.53           C  
-ATOM   1826  C   ASN B  98      -0.067   9.924  30.292  1.00 24.39           C  
-ATOM   1827  O   ASN B  98       0.044  10.687  29.350  1.00 25.00           O  
-ATOM   1828  CB  ASN B  98       1.904  10.317  31.638  1.00 26.30           C  
-ATOM   1829  CG  ASN B  98       2.933   9.687  32.533  1.00 31.01           C  
-ATOM   1830  OD1 ASN B  98       3.830   8.946  32.187  1.00 34.92           O  
-ATOM   1831  ND2 ASN B  98       2.779   9.981  33.784  1.00 35.02           N  
-ATOM   1832  H   ASN B  98       2.470   8.996  29.265  1.00 15.00           H  
-ATOM   1833 HD21 ASN B  98       3.423   9.571  34.434  1.00  0.00           H  
-ATOM   1834 HD22 ASN B  98       2.129  10.665  34.093  1.00  0.00           H  
-ATOM   1835  N   PHE B  99      -1.210   9.657  30.879  1.00 24.06           N  
-ATOM   1836  CA  PHE B  99      -2.402  10.478  30.579  1.00 26.88           C  
-ATOM   1837  C   PHE B  99      -3.451  10.449  31.682  1.00 30.39           C  
-ATOM   1838  O   PHE B  99      -4.553  10.971  31.506  1.00 32.29           O  
-ATOM   1839  CB  PHE B  99      -3.097  10.015  29.308  1.00 21.91           C  
-ATOM   1840  CG  PHE B  99      -3.558   8.589  29.388  1.00 21.11           C  
-ATOM   1841  CD1 PHE B  99      -2.620   7.526  29.292  1.00 22.83           C  
-ATOM   1842  CD2 PHE B  99      -4.933   8.344  29.513  1.00 19.44           C  
-ATOM   1843  CE1 PHE B  99      -3.056   6.189  29.301  1.00 20.85           C  
-ATOM   1844  CE2 PHE B  99      -5.376   7.004  29.523  1.00 24.62           C  
-ATOM   1845  CZ  PHE B  99      -4.444   5.934  29.417  1.00 24.62           C  
-ATOM   1846  OXT PHE B  99      -3.196   9.799  32.713  1.00 33.75           O  
-ATOM   1847  H   PHE B  99      -1.220   8.929  31.561  1.00 15.00           H  
-TER    1848      PHE B  99                                                      
-HETATM 1849  C1  A77 A 800       3.484   3.332  10.744  1.00 19.36           C  
-HETATM 1850  O2  A77 A 800       3.336   4.024  11.730  1.00 16.82           O  
-HETATM 1851  N3  A77 A 800       3.986   3.834   9.598  1.00 21.45           N  
-HETATM 1852  C4  A77 A 800       4.186   3.015   8.397  1.00 22.46           C  
-HETATM 1853  C5  A77 A 800       4.366   5.248   9.533  1.00 23.60           C  
-HETATM 1854  C6  A77 A 800       5.860   5.489   9.574  1.00 28.23           C  
-HETATM 1855  C7  A77 A 800       6.595   5.555   8.390  1.00 28.34           C  
-HETATM 1856  N8  A77 A 800       6.404   5.681  10.778  1.00 29.30           N  
-HETATM 1857  C9  A77 A 800       7.951   5.862   8.490  1.00 34.55           C  
-HETATM 1858  C10 A77 A 800       7.702   5.966  10.862  1.00 28.71           C  
-HETATM 1859  C11 A77 A 800       8.525   6.077   9.751  1.00 30.20           C  
-HETATM 1860  N21 A77 A 800       3.165   2.047  10.748  1.00 17.32           N  
-HETATM 1861  C22 A77 A 800       2.786   1.298  11.960  1.00 17.23           C  
-HETATM 1862  C23 A77 A 800       3.932   0.378  12.380  1.00 17.53           C  
-HETATM 1863  O24 A77 A 800       4.028  -0.768  11.974  1.00 17.24           O  
-HETATM 1864  C25 A77 A 800       1.469   0.526  11.740  1.00 18.10           C  
-HETATM 1865  C26 A77 A 800       1.041  -0.268  12.988  1.00 18.53           C  
-HETATM 1866  C27 A77 A 800       0.334   1.457  11.293  1.00 21.31           C  
-HETATM 1867  N37 A77 A 800       4.847   0.937  13.183  1.00 16.54           N  
-HETATM 1868  C38 A77 A 800       6.139   0.294  13.554  1.00 17.52           C  
-HETATM 1869  C39 A77 A 800       7.277   1.214  13.081  1.00 17.67           C  
-HETATM 1870  C40 A77 A 800       7.580   1.130  11.622  1.00 20.87           C  
-HETATM 1871  C41 A77 A 800       7.184   2.149  10.761  1.00 21.97           C  
-HETATM 1872  C42 A77 A 800       7.454   2.042   9.393  1.00 25.38           C  
-HETATM 1873  C43 A77 A 800       8.129   0.929   8.897  1.00 24.38           C  
-HETATM 1874  C44 A77 A 800       8.534  -0.080   9.783  1.00 27.69           C  
-HETATM 1875  C45 A77 A 800       8.255   0.017  11.147  1.00 21.51           C  
-HETATM 1876  C46 A77 A 800       6.246   0.164  15.076  1.00 16.39           C  
-HETATM 1877  O47 A77 A 800       7.473  -0.492  15.358  1.00 17.49           O  
-HETATM 1878  O48 A77 A 800       5.129  -0.172  17.213  1.00 18.35           O  
-HETATM 1879  C49 A77 A 800       5.012  -0.427  15.813  1.00 18.13           C  
-HETATM 1880  N50 A77 A 800       5.754  -2.802  16.209  1.00 17.31           N  
-HETATM 1881  C51 A77 A 800       4.738  -1.926  15.594  1.00 17.44           C  
-HETATM 1882  C52 A77 A 800       3.349  -2.327  16.127  1.00 17.77           C  
-HETATM 1883  C53 A77 A 800       3.072  -3.822  16.090  1.00 20.09           C  
-HETATM 1884  C54 A77 A 800       3.253  -4.613  17.238  1.00 22.13           C  
-HETATM 1885  C55 A77 A 800       3.044  -6.000  17.178  1.00 22.13           C  
-HETATM 1886  C56 A77 A 800       2.644  -6.619  15.985  1.00 21.36           C  
-HETATM 1887  C57 A77 A 800       2.442  -5.838  14.845  1.00 19.61           C  
-HETATM 1888  C58 A77 A 800       2.658  -4.449  14.899  1.00 20.39           C  
-HETATM 1889  N81 A77 A 800       6.910  -5.919  16.684  1.00 16.89           N  
-HETATM 1890  C82 A77 A 800       7.418  -4.588  16.402  1.00 16.65           C  
-HETATM 1891  C83 A77 A 800       6.432  -3.755  15.559  1.00 18.04           C  
-HETATM 1892  O84 A77 A 800       6.313  -3.944  14.365  1.00 18.77           O  
-HETATM 1893  C85 A77 A 800       8.809  -4.660  15.732  1.00 16.90           C  
-HETATM 1894  C86 A77 A 800       9.366  -3.253  15.463  1.00 16.81           C  
-HETATM 1895  C87 A77 A 800       9.817  -5.422  16.589  1.00 19.25           C  
-HETATM 1896  C97 A77 A 800       6.768  -6.393  17.922  1.00 20.72           C  
-HETATM 1897  O98 A77 A 800       7.143  -5.764  18.901  1.00 19.85           O  
-HETATM 1898  N99 A77 A 800       6.226  -7.635  18.023  1.00 23.02           N  
-HETATM 1899  C2  A77 A 800       5.791  -8.392  16.839  1.00 22.59           C  
-HETATM 1900  C3  A77 A 800       5.994  -8.253  19.345  1.00 22.85           C  
-HETATM 1901  C8  A77 A 800       4.644  -7.870  19.906  1.00 25.07           C  
-HETATM 1902  C12 A77 A 800       3.555  -8.734  19.771  1.00 26.67           C  
-HETATM 1903  N10 A77 A 800       4.555  -6.668  20.511  1.00 32.12           N  
-HETATM 1904  C13 A77 A 800       2.317  -8.344  20.282  1.00 25.95           C  
-HETATM 1905  C14 A77 A 800       3.355  -6.296  20.983  1.00 31.02           C  
-HETATM 1906  C15 A77 A 800       2.211  -7.098  20.901  1.00 28.97           C  
-HETATM 1907  H12 A77 A 800       4.667   3.580   7.598  1.00  0.00           H  
-HETATM 1908  H13 A77 A 800       4.810   2.149   8.614  1.00  0.00           H  
-HETATM 1909  H14 A77 A 800       3.225   2.666   8.023  1.00  0.00           H  
-HETATM 1910  H15 A77 A 800       3.907   5.824  10.334  1.00  0.00           H  
-HETATM 1911  H16 A77 A 800       3.959   5.675   8.617  1.00  0.00           H  
-HETATM 1912  H17 A77 A 800       6.139   5.337   7.444  1.00  0.00           H  
-HETATM 1913  H18 A77 A 800       8.569   5.915   7.598  1.00  0.00           H  
-HETATM 1914  H19 A77 A 800       8.128   6.112  11.847  1.00  0.00           H  
-HETATM 1915  H20 A77 A 800       9.576   6.313   9.868  1.00  0.00           H  
-HETATM 1916  H28 A77 A 800       3.241   1.576   9.866  1.00 15.00           H  
-HETATM 1917  H29 A77 A 800       2.622   1.990  12.785  1.00  0.00           H  
-HETATM 1918  H30 A77 A 800       1.633  -0.191  10.932  1.00  0.00           H  
-HETATM 1919  H31 A77 A 800       0.066  -0.731  12.847  1.00  0.00           H  
-HETATM 1920  H32 A77 A 800       1.750  -1.060  13.233  1.00  0.00           H  
-HETATM 1921  H33 A77 A 800       0.958   0.383  13.857  1.00  0.00           H  
-HETATM 1922  H34 A77 A 800       0.103   2.195  12.063  1.00  0.00           H  
-HETATM 1923  H35 A77 A 800       0.588   1.995  10.378  1.00  0.00           H  
-HETATM 1924  H36 A77 A 800      -0.572   0.888  11.090  1.00  0.00           H  
-HETATM 1925  H59 A77 A 800       4.679   1.879  13.475  1.00 15.00           H  
-HETATM 1926  H60 A77 A 800       6.217  -0.701  13.103  1.00  0.00           H  
-HETATM 1927  H61 A77 A 800       8.220   1.029  13.592  1.00  0.00           H  
-HETATM 1928  H62 A77 A 800       7.032   2.243  13.345  1.00  0.00           H  
-HETATM 1929  H63 A77 A 800       6.655   3.007  11.151  1.00  0.00           H  
-HETATM 1930  H64 A77 A 800       7.143   2.817   8.711  1.00  0.00           H  
-HETATM 1931  H65 A77 A 800       8.332   0.846   7.838  1.00  0.00           H  
-HETATM 1932  H66 A77 A 800       9.064  -0.940   9.402  1.00  0.00           H  
-HETATM 1933  H67 A77 A 800       8.558  -0.759  11.833  1.00  0.00           H  
-HETATM 1934  H68 A77 A 800       6.390   1.176  15.462  1.00  0.00           H  
-HETATM 1935  H69 A77 A 800       7.923  -0.554  14.510  1.00  0.00           H  
-HETATM 1936  H70 A77 A 800       5.952  -0.638  17.406  1.00  0.00           H  
-HETATM 1937  H71 A77 A 800       4.126   0.137  15.516  1.00  0.00           H  
-HETATM 1938  H72 A77 A 800       5.859  -2.796  17.199  1.00 15.00           H  
-HETATM 1939  H73 A77 A 800       4.726  -2.084  14.514  1.00  0.00           H  
-HETATM 1940  H74 A77 A 800       2.565  -1.805  15.575  1.00  0.00           H  
-HETATM 1941  H75 A77 A 800       3.244  -1.997  17.160  1.00  0.00           H  
-HETATM 1942  H76 A77 A 800       3.576  -4.155  18.164  1.00  0.00           H  
-HETATM 1943  H77 A77 A 800       3.197  -6.593  18.060  1.00  0.00           H  
-HETATM 1944  H78 A77 A 800       2.499  -7.692  15.949  1.00  0.00           H  
-HETATM 1945  H79 A77 A 800       2.125  -6.298  13.922  1.00  0.00           H  
-HETATM 1946  H80 A77 A 800       2.512  -3.846  14.014  1.00  0.00           H  
-HETATM 1947  H88 A77 A 800       6.620  -6.524  15.943  1.00 15.00           H  
-HETATM 1948  H89 A77 A 800       7.536  -4.035  17.334  1.00  0.00           H  
-HETATM 1949  H90 A77 A 800       8.709  -5.182  14.779  1.00  0.00           H  
-HETATM 1950  H91 A77 A 800      10.376  -3.302  15.056  1.00  0.00           H  
-HETATM 1951  H92 A77 A 800       8.754  -2.713  14.743  1.00  0.00           H  
-HETATM 1952  H93 A77 A 800       9.406  -2.664  16.380  1.00  0.00           H  
-HETATM 1953  H94 A77 A 800       9.938  -4.949  17.565  1.00  0.00           H  
-HETATM 1954  H95 A77 A 800       9.500  -6.452  16.748  1.00  0.00           H  
-HETATM 1955  H96 A77 A 800      10.794  -5.454  16.106  1.00  0.00           H  
-HETATM 1956  H1  A77 A 800       6.654  -8.752  16.279  1.00  0.00           H  
-HETATM 1957  H10 A77 A 800       5.184  -7.776  16.176  1.00  0.00           H  
-HETATM 1958  H11 A77 A 800       5.185  -9.254  17.120  1.00  0.00           H  
-HETATM 1959  H2  A77 A 800       6.762  -7.948  20.051  1.00  0.00           H  
-HETATM 1960  H3  A77 A 800       6.067  -9.337  19.267  1.00  0.00           H  
-HETATM 1961  H4  A77 A 800       3.667  -9.663  19.244  1.00  0.00           H  
-HETATM 1962  H5  A77 A 800       1.446  -8.984  20.186  1.00  0.00           H  
-HETATM 1963  H6  A77 A 800       3.271  -5.323  21.450  1.00  0.00           H  
-HETATM 1964  H7  A77 A 800       1.267  -6.748  21.299  1.00  0.00           H  
-HETATM 1965  O   HOH A 415       5.245  -3.205  11.955  1.00 15.00           O  
-HETATM 1966  H1  HOH A 415       4.846  -2.390  12.262  1.00  0.00           H  
-HETATM 1967  H2  HOH A 415       5.708  -3.499  12.734  1.00  0.00           H  
-CONECT 1849 1850 1851 1860                                                      
-CONECT 1850 1849                                                                
-CONECT 1851 1849 1852 1853                                                      
-CONECT 1852 1851 1907 1908 1909                                                 
-CONECT 1853 1851 1854 1910 1911                                                 
-CONECT 1854 1853 1855 1856                                                      
-CONECT 1855 1854 1857 1912                                                      
-CONECT 1856 1854 1858                                                           
-CONECT 1857 1855 1859 1913                                                      
-CONECT 1858 1856 1859 1914                                                      
-CONECT 1859 1857 1858 1915                                                      
-CONECT 1860 1849 1861 1916                                                      
-CONECT 1861 1860 1862 1864 1917                                                 
-CONECT 1862 1861 1863 1867                                                      
-CONECT 1863 1862                                                                
-CONECT 1864 1861 1865 1866 1918                                                 
-CONECT 1865 1864 1919 1920 1921                                                 
-CONECT 1866 1864 1922 1923 1924                                                 
-CONECT 1867 1862 1868 1925                                                      
-CONECT 1868 1867 1869 1876 1926                                                 
-CONECT 1869 1868 1870 1927 1928                                                 
-CONECT 1870 1869 1871 1875                                                      
-CONECT 1871 1870 1872 1929                                                      
-CONECT 1872 1871 1873 1930                                                      
-CONECT 1873 1872 1874 1931                                                      
-CONECT 1874 1873 1875 1932                                                      
-CONECT 1875 1870 1874 1933                                                      
-CONECT 1876 1868 1877 1879 1934                                                 
-CONECT 1877 1876 1935                                                           
-CONECT 1878 1879 1936                                                           
-CONECT 1879 1876 1878 1881 1937                                                 
-CONECT 1880 1881 1891 1938                                                      
-CONECT 1881 1879 1880 1882 1939                                                 
-CONECT 1882 1881 1883 1940 1941                                                 
-CONECT 1883 1882 1884 1888                                                      
-CONECT 1884 1883 1885 1942                                                      
-CONECT 1885 1884 1886 1943                                                      
-CONECT 1886 1885 1887 1944                                                      
-CONECT 1887 1886 1888 1945                                                      
-CONECT 1888 1883 1887 1946                                                      
-CONECT 1889 1890 1896 1947                                                      
-CONECT 1890 1889 1891 1893 1948                                                 
-CONECT 1891 1880 1890 1892                                                      
-CONECT 1892 1891                                                                
-CONECT 1893 1890 1894 1895 1949                                                 
-CONECT 1894 1893 1950 1951 1952                                                 
-CONECT 1895 1893 1953 1954 1955                                                 
-CONECT 1896 1889 1897 1898                                                      
-CONECT 1897 1896                                                                
-CONECT 1898 1896 1899 1900                                                      
-CONECT 1899 1898 1956 1957 1958                                                 
-CONECT 1900 1898 1901 1959 1960                                                 
-CONECT 1901 1900 1902 1903                                                      
-CONECT 1902 1901 1904 1961                                                      
-CONECT 1903 1901 1905                                                           
-CONECT 1904 1902 1906 1962                                                      
-CONECT 1905 1903 1906 1963                                                      
-CONECT 1906 1904 1905 1964                                                      
-CONECT 1907 1852                                                                
-CONECT 1908 1852                                                                
-CONECT 1909 1852                                                                
-CONECT 1910 1853                                                                
-CONECT 1911 1853                                                                
-CONECT 1912 1855                                                                
-CONECT 1913 1857                                                                
-CONECT 1914 1858                                                                
-CONECT 1915 1859                                                                
-CONECT 1916 1860                                                                
-CONECT 1917 1861                                                                
-CONECT 1918 1864                                                                
-CONECT 1919 1865                                                                
-CONECT 1920 1865                                                                
-CONECT 1921 1865                                                                
-CONECT 1922 1866                                                                
-CONECT 1923 1866                                                                
-CONECT 1924 1866                                                                
-CONECT 1925 1867                                                                
-CONECT 1926 1868                                                                
-CONECT 1927 1869                                                                
-CONECT 1928 1869                                                                
-CONECT 1929 1871                                                                
-CONECT 1930 1872                                                                
-CONECT 1931 1873                                                                
-CONECT 1932 1874                                                                
-CONECT 1933 1875                                                                
-CONECT 1934 1876                                                                
-CONECT 1935 1877                                                                
-CONECT 1936 1878                                                                
-CONECT 1937 1879                                                                
-CONECT 1938 1880                                                                
-CONECT 1939 1881                                                                
-CONECT 1940 1882                                                                
-CONECT 1941 1882                                                                
-CONECT 1942 1884                                                                
-CONECT 1943 1885                                                                
-CONECT 1944 1886                                                                
-CONECT 1945 1887                                                                
-CONECT 1946 1888                                                                
-CONECT 1947 1889                                                                
-CONECT 1948 1890                                                                
-CONECT 1949 1893                                                                
-CONECT 1950 1894                                                                
-CONECT 1951 1894                                                                
-CONECT 1952 1894                                                                
-CONECT 1953 1895                                                                
-CONECT 1954 1895                                                                
-CONECT 1955 1895                                                                
-CONECT 1956 1899                                                                
-CONECT 1957 1899                                                                
-CONECT 1958 1899                                                                
-CONECT 1959 1900                                                                
-CONECT 1960 1900                                                                
-CONECT 1961 1902                                                                
-CONECT 1962 1904                                                                
-CONECT 1963 1905                                                                
-CONECT 1964 1906                                                                
-MASTER      256    0    1    2    4    0    5    6 1965    2  116   16          
-END                                                                             
diff --git a/plip/test/pdb/1hwu.pdb b/plip/test/pdb/1hwu.pdb
deleted file mode 100644
index dab452c..0000000
--- a/plip/test/pdb/1hwu.pdb
+++ /dev/null
@@ -1,5032 +0,0 @@
-HEADER    SIGNALING PROTEIN                       10-JAN-01   1HWU              
-TITLE     STRUCTURE OF PII PROTEIN FROM HERBASPIRILLUM SEROPEDICAE              
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: PII PROTEIN;                                               
-COMPND   3 CHAIN: A, B, C, D, E, F;                                             
-COMPND   4 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HERBASPIRILLUM SEROPEDICAE;                     
-SOURCE   3 ORGANISM_TAXID: 964;                                                 
-SOURCE   4 GENE: GLNB;                                                          
-SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   7 EXPRESSION_SYSTEM_STRAIN: RB9065(LAMBDA)DE3;                         
-SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28B+                                   
-KEYWDS    HERBASPIRILLUM SEROPEDICAE PII, BETA-ALPHA-BETA MOTIF,                
-KEYWDS   2 SIGNAL TRANSDUCTION PROTEIN, SIGNALING PROTEIN                       
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    E.M.BENELLI,M.BUCK,I.POLIKARPOV,E.M.DE SOUZA,L.M.CRUZ,                
-AUTHOR   2 F.O.PEDROSA                                                          
-REVDAT   2   24-FEB-09 1HWU    1       VERSN                                    
-REVDAT   1   17-JUN-03 1HWU    0                                                
-JRNL        AUTH   E.MACHADO BENELLI,M.BUCK,I.POLIKARPOV,                       
-JRNL        AUTH 2 E.MALTEMPI DE SOUZA,L.M.CRUZ,F.O.PEDROSA                     
-JRNL        TITL   HERBASPIRILLUM SEROPEDICAE SIGNAL TRANSDUCTION               
-JRNL        TITL 2 PROTEIN PII IS STRUCTURALLY SIMILAR TO THE ENTERIC           
-JRNL        TITL 3 GLNK.                                                        
-JRNL        REF    EUR.J.BIOCHEM.                V. 269  3296 2002              
-JRNL        REFN                   ISSN 0014-2956                               
-JRNL        PMID   12084071                                                     
-JRNL        DOI    10.1046/J.1432-1033.2002.03011.X                             
-REMARK   1                                                                      
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : REFMAC                                               
-REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 13.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
-REMARK   3   NUMBER OF REFLECTIONS             : 146413                         
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
-REMARK   3   R VALUE            (WORKING SET) : 0.203                           
-REMARK   3   FREE R VALUE                     : 0.272                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
-REMARK   3   FREE R VALUE TEST SET COUNT      : 5                               
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 4313                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 0                                       
-REMARK   3   SOLVENT ATOMS            : 118                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
-REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
-REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
-REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
-REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
-REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
-REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
-REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
-REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
-REMARK   3                                                                      
-REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
-REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
-REMARK   3                                                                      
-REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
-REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
-REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
-REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
-REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
-REMARK   3                                                                      
-REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
-REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
-REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
-REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
-REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1HWU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-01.                  
-REMARK 100 THE RCSB ID CODE IS RCSB012638.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-98                          
-REMARK 200  TEMPERATURE           (KELVIN) : 120                                
-REMARK 200  PH                             : 6.5                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : LNLS                               
-REMARK 200  BEAMLINE                       : D03B-MX1                           
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.38                               
-REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
-REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36523                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 13.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
-REMARK 200  DATA REDUNDANCY                : 4.000                              
-REMARK 200  R MERGE                    (I) : 0.05700                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.32200                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: AMORE                                                 
-REMARK 200 STARTING MODEL: PDB ENTRY 2PII                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 44.33                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE, MAGNESIUM             
-REMARK 280  ACETATE, METHYLPENTADIOL, PH 6.5, VAPOR DIFFUSION, HANGING          
-REMARK 280  DROP, TEMPERATURE 291K                                              
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.20500            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.47500            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.16000            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.47500            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.20500            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.16000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 6350 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 14150 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 5670 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 13560 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 3                                                       
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 13730 ANGSTROM**2                         
-REMARK 350 SURFACE AREA OF THE COMPLEX: 26000 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, E                               
-REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       78.41000            
-REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -41.16000            
-REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       50.47500            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     ARG A    38                                                      
-REMARK 465     GLN A    39                                                      
-REMARK 465     LYS A    40                                                      
-REMARK 465     GLY A    41                                                      
-REMARK 465     HIS A    42                                                      
-REMARK 465     THR A    43                                                      
-REMARK 465     GLU A    44                                                      
-REMARK 465     LEU A    45                                                      
-REMARK 465     TYR A    46                                                      
-REMARK 465     ARG A    47                                                      
-REMARK 465     GLY A    48                                                      
-REMARK 465     ALA A    49                                                      
-REMARK 465     GLU A    50                                                      
-REMARK 465     GLY B    37                                                      
-REMARK 465     ARG B    38                                                      
-REMARK 465     GLN B    39                                                      
-REMARK 465     LYS B    40                                                      
-REMARK 465     GLY B    41                                                      
-REMARK 465     HIS B    42                                                      
-REMARK 465     GLY B   108                                                      
-REMARK 465     PRO B   109                                                      
-REMARK 465     ASP B   110                                                      
-REMARK 465     ALA B   111                                                      
-REMARK 465     VAL B   112                                                      
-REMARK 465     GLY C    37                                                      
-REMARK 465     ARG C    38                                                      
-REMARK 465     GLN C    39                                                      
-REMARK 465     LYS C    40                                                      
-REMARK 465     GLY C    41                                                      
-REMARK 465     HIS C    42                                                      
-REMARK 465     THR C    43                                                      
-REMARK 465     GLU C    44                                                      
-REMARK 465     LEU C    45                                                      
-REMARK 465     TYR C    46                                                      
-REMARK 465     ARG C    47                                                      
-REMARK 465     GLY C    48                                                      
-REMARK 465     ALA C    49                                                      
-REMARK 465     GLU C    50                                                      
-REMARK 465     TYR C    51                                                      
-REMARK 465     VAL C    52                                                      
-REMARK 465     VAL C    53                                                      
-REMARK 465     ASP C    54                                                      
-REMARK 465     PHE C    55                                                      
-REMARK 465     LEU C    56                                                      
-REMARK 465     GLY D    37                                                      
-REMARK 465     ARG D    38                                                      
-REMARK 465     GLN D    39                                                      
-REMARK 465     LYS D    40                                                      
-REMARK 465     GLY D    41                                                      
-REMARK 465     HIS D    42                                                      
-REMARK 465     THR D    43                                                      
-REMARK 465     GLU D    44                                                      
-REMARK 465     LEU D    45                                                      
-REMARK 465     TYR D    46                                                      
-REMARK 465     ARG D    47                                                      
-REMARK 465     GLY D    48                                                      
-REMARK 465     ALA D    49                                                      
-REMARK 465     PHE E    36                                                      
-REMARK 465     GLY E    37                                                      
-REMARK 465     ARG E    38                                                      
-REMARK 465     GLN E    39                                                      
-REMARK 465     LYS E    40                                                      
-REMARK 465     GLY E    41                                                      
-REMARK 465     HIS E    42                                                      
-REMARK 465     THR E    43                                                      
-REMARK 465     GLU E    44                                                      
-REMARK 465     LEU E    45                                                      
-REMARK 465     TYR E    46                                                      
-REMARK 465     ARG E    47                                                      
-REMARK 465     GLY E    48                                                      
-REMARK 465     ALA E    49                                                      
-REMARK 465     GLU E    50                                                      
-REMARK 465     TYR E    51                                                      
-REMARK 465     VAL E    52                                                      
-REMARK 465     VAL E    53                                                      
-REMARK 465     ASP E    54                                                      
-REMARK 465     PHE E    55                                                      
-REMARK 465     LEU E    56                                                      
-REMARK 465     GLU E   106                                                      
-REMARK 465     THR E   107                                                      
-REMARK 465     GLY E   108                                                      
-REMARK 465     PRO E   109                                                      
-REMARK 465     ASP E   110                                                      
-REMARK 465     ALA E   111                                                      
-REMARK 465     VAL E   112                                                      
-REMARK 465     PHE F    36                                                      
-REMARK 465     GLY F    37                                                      
-REMARK 465     ARG F    38                                                      
-REMARK 465     GLN F    39                                                      
-REMARK 465     LYS F    40                                                      
-REMARK 465     GLY F    41                                                      
-REMARK 465     HIS F    42                                                      
-REMARK 465     THR F    43                                                      
-REMARK 465     GLU F    44                                                      
-REMARK 465     LEU F    45                                                      
-REMARK 465     TYR F    46                                                      
-REMARK 465     ARG F    47                                                      
-REMARK 465     GLY F    48                                                      
-REMARK 465     ALA F    49                                                      
-REMARK 465     GLU F    50                                                      
-REMARK 465     TYR F    51                                                      
-REMARK 465     VAL F    52                                                      
-REMARK 465     VAL F    53                                                      
-REMARK 465     ASP F    54                                                      
-REMARK 465     PHE F    55                                                      
-REMARK 465     LEU F    56                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
-REMARK 470     LYS D  68    CG   CD   CE   NZ                                   
-REMARK 470     LYS F  68    CG   CD   CE   NZ                                   
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
-REMARK 500    ARG B  17   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
-REMARK 500    ARG B  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES          
-REMARK 500    PHE B  92   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
-REMARK 500    ARG B 101   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
-REMARK 500    ARG C  17   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
-REMARK 500    ASP C  88   CB  -  CG  -  OD1 ANGL. DEV. =   8.1 DEGREES          
-REMARK 500    ARG C 103   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
-REMARK 500    LEU D  20   CA  -  CB  -  CG  ANGL. DEV. =  18.0 DEGREES          
-REMARK 500    ARG D 101   NE  -  CZ  -  NH2 ANGL. DEV. =   8.0 DEGREES          
-REMARK 500    ARG D 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
-REMARK 500    ASP D 110   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES          
-REMARK 500    ASP E  14   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
-REMARK 500    VAL F  63   CG1 -  CB  -  CG2 ANGL. DEV. = -10.0 DEGREES          
-REMARK 500    ARG F  82   CD  -  NE  -  CZ  ANGL. DEV. =  18.3 DEGREES          
-REMARK 500    ARG F 101   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
-REMARK 500    ARG F 101   NE  -  CZ  -  NH2 ANGL. DEV. =   4.5 DEGREES          
-REMARK 500    ARG F 103   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASP A  54      -71.60   -103.03                                   
-REMARK 500    THR C  26     -163.03   -126.18                                   
-REMARK 500    THR E  83      -32.13   -135.65                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
-REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
-REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
-REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
-REMARK 500 I=INSERTION CODE).                                                   
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        ANGLE                                           
-REMARK 500    ALA A  21        -10.85                                           
-REMARK 500    LYS A  79         11.63                                           
-REMARK 500    VAL A  96        -10.58                                           
-REMARK 500    PRO B  10        -10.65                                           
-REMARK 500    LYS C  58        -11.78                                           
-REMARK 500    VAL C  64         12.06                                           
-REMARK 500    LYS C  90        -10.03                                           
-REMARK 500    PRO D  57         15.26                                           
-REMARK 500    GLU D  62         10.22                                           
-REMARK 500    VAL D  69         10.01                                           
-REMARK 500    THR F 104         10.89                                           
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 615                                                                      
-REMARK 615 ZERO OCCUPANCY ATOM                                                  
-REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
-REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
-REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
-REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
-REMARK 615   M RES C SSEQI                                                      
-REMARK 615     HOH F  130                                                       
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 2PII   RELATED DB: PDB                                   
-REMARK 900 PII, GLNB PRODUCT                                                    
-DBREF  1HWU A    1   112  UNP    P94852   P94852_HERSE     1    112             
-DBREF  1HWU B    1   112  UNP    P94852   P94852_HERSE     1    112             
-DBREF  1HWU C    1   112  UNP    P94852   P94852_HERSE     1    112             
-DBREF  1HWU D    1   112  UNP    P94852   P94852_HERSE     1    112             
-DBREF  1HWU E    1   112  UNP    P94852   P94852_HERSE     1    112             
-DBREF  1HWU F    1   112  UNP    P94852   P94852_HERSE     1    112             
-SEQRES   1 A  112  MET LYS GLN VAL THR ALA ILE ILE LYS PRO PHE LYS LEU          
-SEQRES   2 A  112  ASP GLU VAL ARG GLU SER LEU ALA GLU VAL GLY VAL THR          
-SEQRES   3 A  112  GLY LEU THR VAL THR GLU VAL LYS GLY PHE GLY ARG GLN          
-SEQRES   4 A  112  LYS GLY HIS THR GLU LEU TYR ARG GLY ALA GLU TYR VAL          
-SEQRES   5 A  112  VAL ASP PHE LEU PRO LYS VAL LYS ILE GLU VAL VAL VAL          
-SEQRES   6 A  112  ASP ASP LYS VAL VAL GLU GLN ALA VAL ASP ALA ILE ILE          
-SEQRES   7 A  112  LYS ALA ALA ARG THR GLY LYS ILE GLY ASP GLY LYS ILE          
-SEQRES   8 A  112  PHE VAL GLN GLU VAL GLU GLN VAL ILE ARG ILE ARG THR          
-SEQRES   9 A  112  GLY GLU THR GLY PRO ASP ALA VAL                              
-SEQRES   1 B  112  MET LYS GLN VAL THR ALA ILE ILE LYS PRO PHE LYS LEU          
-SEQRES   2 B  112  ASP GLU VAL ARG GLU SER LEU ALA GLU VAL GLY VAL THR          
-SEQRES   3 B  112  GLY LEU THR VAL THR GLU VAL LYS GLY PHE GLY ARG GLN          
-SEQRES   4 B  112  LYS GLY HIS THR GLU LEU TYR ARG GLY ALA GLU TYR VAL          
-SEQRES   5 B  112  VAL ASP PHE LEU PRO LYS VAL LYS ILE GLU VAL VAL VAL          
-SEQRES   6 B  112  ASP ASP LYS VAL VAL GLU GLN ALA VAL ASP ALA ILE ILE          
-SEQRES   7 B  112  LYS ALA ALA ARG THR GLY LYS ILE GLY ASP GLY LYS ILE          
-SEQRES   8 B  112  PHE VAL GLN GLU VAL GLU GLN VAL ILE ARG ILE ARG THR          
-SEQRES   9 B  112  GLY GLU THR GLY PRO ASP ALA VAL                              
-SEQRES   1 C  112  MET LYS GLN VAL THR ALA ILE ILE LYS PRO PHE LYS LEU          
-SEQRES   2 C  112  ASP GLU VAL ARG GLU SER LEU ALA GLU VAL GLY VAL THR          
-SEQRES   3 C  112  GLY LEU THR VAL THR GLU VAL LYS GLY PHE GLY ARG GLN          
-SEQRES   4 C  112  LYS GLY HIS THR GLU LEU TYR ARG GLY ALA GLU TYR VAL          
-SEQRES   5 C  112  VAL ASP PHE LEU PRO LYS VAL LYS ILE GLU VAL VAL VAL          
-SEQRES   6 C  112  ASP ASP LYS VAL VAL GLU GLN ALA VAL ASP ALA ILE ILE          
-SEQRES   7 C  112  LYS ALA ALA ARG THR GLY LYS ILE GLY ASP GLY LYS ILE          
-SEQRES   8 C  112  PHE VAL GLN GLU VAL GLU GLN VAL ILE ARG ILE ARG THR          
-SEQRES   9 C  112  GLY GLU THR GLY PRO ASP ALA VAL                              
-SEQRES   1 D  112  MET LYS GLN VAL THR ALA ILE ILE LYS PRO PHE LYS LEU          
-SEQRES   2 D  112  ASP GLU VAL ARG GLU SER LEU ALA GLU VAL GLY VAL THR          
-SEQRES   3 D  112  GLY LEU THR VAL THR GLU VAL LYS GLY PHE GLY ARG GLN          
-SEQRES   4 D  112  LYS GLY HIS THR GLU LEU TYR ARG GLY ALA GLU TYR VAL          
-SEQRES   5 D  112  VAL ASP PHE LEU PRO LYS VAL LYS ILE GLU VAL VAL VAL          
-SEQRES   6 D  112  ASP ASP LYS VAL VAL GLU GLN ALA VAL ASP ALA ILE ILE          
-SEQRES   7 D  112  LYS ALA ALA ARG THR GLY LYS ILE GLY ASP GLY LYS ILE          
-SEQRES   8 D  112  PHE VAL GLN GLU VAL GLU GLN VAL ILE ARG ILE ARG THR          
-SEQRES   9 D  112  GLY GLU THR GLY PRO ASP ALA VAL                              
-SEQRES   1 E  112  MET LYS GLN VAL THR ALA ILE ILE LYS PRO PHE LYS LEU          
-SEQRES   2 E  112  ASP GLU VAL ARG GLU SER LEU ALA GLU VAL GLY VAL THR          
-SEQRES   3 E  112  GLY LEU THR VAL THR GLU VAL LYS GLY PHE GLY ARG GLN          
-SEQRES   4 E  112  LYS GLY HIS THR GLU LEU TYR ARG GLY ALA GLU TYR VAL          
-SEQRES   5 E  112  VAL ASP PHE LEU PRO LYS VAL LYS ILE GLU VAL VAL VAL          
-SEQRES   6 E  112  ASP ASP LYS VAL VAL GLU GLN ALA VAL ASP ALA ILE ILE          
-SEQRES   7 E  112  LYS ALA ALA ARG THR GLY LYS ILE GLY ASP GLY LYS ILE          
-SEQRES   8 E  112  PHE VAL GLN GLU VAL GLU GLN VAL ILE ARG ILE ARG THR          
-SEQRES   9 E  112  GLY GLU THR GLY PRO ASP ALA VAL                              
-SEQRES   1 F  112  MET LYS GLN VAL THR ALA ILE ILE LYS PRO PHE LYS LEU          
-SEQRES   2 F  112  ASP GLU VAL ARG GLU SER LEU ALA GLU VAL GLY VAL THR          
-SEQRES   3 F  112  GLY LEU THR VAL THR GLU VAL LYS GLY PHE GLY ARG GLN          
-SEQRES   4 F  112  LYS GLY HIS THR GLU LEU TYR ARG GLY ALA GLU TYR VAL          
-SEQRES   5 F  112  VAL ASP PHE LEU PRO LYS VAL LYS ILE GLU VAL VAL VAL          
-SEQRES   6 F  112  ASP ASP LYS VAL VAL GLU GLN ALA VAL ASP ALA ILE ILE          
-SEQRES   7 F  112  LYS ALA ALA ARG THR GLY LYS ILE GLY ASP GLY LYS ILE          
-SEQRES   8 F  112  PHE VAL GLN GLU VAL GLU GLN VAL ILE ARG ILE ARG THR          
-SEQRES   9 F  112  GLY GLU THR GLY PRO ASP ALA VAL                              
-FORMUL   7  HOH   *118(H2 O)                                                    
-HELIX    1   1 LYS A    9  PHE A   11  5                                   3    
-HELIX    2   2 LYS A   12  VAL A   23  1                                  12    
-HELIX    3   3 ASP A   66  LYS A   68  5                                   3    
-HELIX    4   4 VAL A   69  ARG A   82  1                                  14    
-HELIX    5   5 GLY A  108  ALA A  111  5                                   4    
-HELIX    6   6 LYS B    9  PHE B   11  5                                   3    
-HELIX    7   7 LYS B   12  VAL B   23  1                                  12    
-HELIX    8   8 ASP B   66  LYS B   68  5                                   3    
-HELIX    9   9 VAL B   69  ARG B   82  1                                  14    
-HELIX   10  10 LYS C    9  PHE C   11  5                                   3    
-HELIX   11  11 LYS C   12  VAL C   23  1                                  12    
-HELIX   12  12 ASP C   66  LYS C   68  5                                   3    
-HELIX   13  13 VAL C   69  ARG C   82  1                                  14    
-HELIX   14  14 GLY C  108  VAL C  112  5                                   5    
-HELIX   15  15 LYS D    9  PHE D   11  5                                   3    
-HELIX   16  16 LYS D   12  GLU D   22  1                                  11    
-HELIX   17  17 ASP D   66  LYS D   68  5                                   3    
-HELIX   18  18 VAL D   69  ARG D   82  1                                  14    
-HELIX   19  19 GLY D  108  VAL D  112  5                                   5    
-HELIX   20  20 LYS E    9  PHE E   11  5                                   3    
-HELIX   21  21 LYS E   12  VAL E   23  1                                  12    
-HELIX   22  22 ASP E   66  LYS E   68  5                                   3    
-HELIX   23  23 VAL E   69  ARG E   82  1                                  14    
-HELIX   24  24 LYS F   12  VAL F   23  1                                  12    
-HELIX   25  25 ASP F   66  LYS F   68  5                                   3    
-HELIX   26  26 VAL F   69  ARG F   82  1                                  14    
-HELIX   27  27 GLY F  108  VAL F  112  5                                   5    
-SHEET    1   A 5 THR A  29  PHE A  36  0                                        
-SHEET    2   A 5 PHE A  55  VAL A  65 -1  N  LEU A  56   O  GLY A  35           
-SHEET    3   A 5 LYS A   2  ILE A   8 -1  N  LYS A   2   O  VAL A  65           
-SHEET    4   A 5 LYS A  90  GLU A  95 -1  O  LYS A  90   N  ILE A   7           
-SHEET    5   A 5 GLN C  98  ARG C 101 -1  O  GLN C  98   N  VAL A  93           
-SHEET    1   B10 GLN A  98  ARG A 101  0                                        
-SHEET    2   B10 LYS B  90  GLU B  95 -1  N  ILE B  91   O  ILE A 100           
-SHEET    3   B10 LYS B   2  ILE B   8 -1  N  GLN B   3   O  GLN B  94           
-SHEET    4   B10 LEU B  56  VAL B  65 -1  O  VAL B  59   N  ILE B   8           
-SHEET    5   B10 LEU B  28  GLY B  35 -1  O  THR B  29   N  GLU B  62           
-SHEET    6   B10 THR C  29  PHE C  36 -1  N  LYS C  34   O  VAL B  30           
-SHEET    7   B10 LYS C  58  VAL C  65 -1  N  LYS C  58   O  VAL C  33           
-SHEET    8   B10 LYS C   2  ILE C   8 -1  O  LYS C   2   N  VAL C  65           
-SHEET    9   B10 LYS C  90  GLU C  95 -1  O  LYS C  90   N  ILE C   7           
-SHEET   10   B10 GLN B  98  ARG B 101 -1  O  GLN B  98   N  VAL C  93           
-SHEET    1   C 2 GLU B  44  TYR B  46  0                                        
-SHEET    2   C 2 ALA B  49  TYR B  51 -1  O  ALA B  49   N  TYR B  46           
-SHEET    1   D 5 THR D  29  GLY D  35  0                                        
-SHEET    2   D 5 LEU D  56  VAL D  65 -1  N  LEU D  56   O  GLY D  35           
-SHEET    3   D 5 LYS D   2  ILE D   8 -1  N  LYS D   2   O  VAL D  65           
-SHEET    4   D 5 LYS D  90  GLU D  95 -1  O  LYS D  90   N  ILE D   7           
-SHEET    5   D 5 GLN F  98  ARG F 101 -1  O  GLN F  98   N  VAL D  93           
-SHEET    1   E 5 GLN D  98  ARG D 101  0                                        
-SHEET    2   E 5 LYS E  90  GLU E  95 -1  N  ILE E  91   O  ILE D 100           
-SHEET    3   E 5 LYS E   2  ILE E   8 -1  N  GLN E   3   O  GLN E  94           
-SHEET    4   E 5 LYS E  58  VAL E  65 -1  O  VAL E  59   N  ILE E   8           
-SHEET    5   E 5 THR E  29  VAL E  33 -1  O  THR E  29   N  GLU E  62           
-SHEET    1   F 5 GLN E  98  ARG E 101  0                                        
-SHEET    2   F 5 GLY F  89  GLU F  95 -1  O  ILE F  91   N  ILE E 100           
-SHEET    3   F 5 LYS F   2  ILE F   8 -1  O  GLN F   3   N  GLN F  94           
-SHEET    4   F 5 LYS F  58  VAL F  65 -1  N  VAL F  59   O  ILE F   8           
-SHEET    5   F 5 THR F  29  VAL F  33 -1  O  THR F  29   N  GLU F  62           
-CRYST1   78.410   82.320  100.950  90.00  90.00  90.00 P 21 21 21   24          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.012753  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.012148  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.009906        0.00000                         
-ATOM      1  N   MET A   1      21.209  48.051  38.701  1.00 43.54           N  
-ATOM      2  CA  MET A   1      20.652  46.739  38.287  1.00 42.21           C  
-ATOM      3  C   MET A   1      21.670  45.963  37.454  1.00 39.93           C  
-ATOM      4  O   MET A   1      22.518  46.540  36.821  1.00 40.22           O  
-ATOM      5  CB  MET A   1      19.294  46.787  37.576  1.00 43.51           C  
-ATOM      6  CG  MET A   1      18.214  47.214  38.604  1.00 46.88           C  
-ATOM      7  SD  MET A   1      17.490  48.753  37.986  1.00 67.32           S  
-ATOM      8  CE  MET A   1      18.854  49.678  37.326  1.00 62.64           C  
-ATOM      9  N   LYS A   2      21.671  44.662  37.706  1.00 39.65           N  
-ATOM     10  CA  LYS A   2      22.601  43.765  37.034  1.00 40.83           C  
-ATOM     11  C   LYS A   2      21.793  42.774  36.168  1.00 38.53           C  
-ATOM     12  O   LYS A   2      20.778  42.261  36.643  1.00 37.58           O  
-ATOM     13  CB  LYS A   2      23.415  43.024  38.081  1.00 47.94           C  
-ATOM     14  CG  LYS A   2      24.305  43.864  39.045  1.00 41.15           C  
-ATOM     15  CD  LYS A   2      25.234  44.801  38.226  1.00 40.47           C  
-ATOM     16  CE  LYS A   2      26.076  45.599  39.265  1.00 40.87           C  
-ATOM     17  NZ  LYS A   2      26.998  46.535  38.614  1.00 40.28           N  
-ATOM     18  N   GLN A   3      22.311  42.458  34.977  1.00 33.48           N  
-ATOM     19  CA  GLN A   3      21.695  41.325  34.220  1.00 33.61           C  
-ATOM     20  C   GLN A   3      22.536  40.122  34.641  1.00 30.24           C  
-ATOM     21  O   GLN A   3      23.766  40.216  34.577  1.00 31.24           O  
-ATOM     22  CB  GLN A   3      21.939  41.561  32.718  1.00 28.51           C  
-ATOM     23  CG  GLN A   3      21.538  40.292  31.908  1.00 43.86           C  
-ATOM     24  CD  GLN A   3      21.441  40.700  30.432  1.00 34.13           C  
-ATOM     25  OE1 GLN A   3      20.329  40.720  29.949  1.00 51.70           O  
-ATOM     26  NE2 GLN A   3      22.582  41.072  29.878  1.00 44.07           N  
-ATOM     27  N   VAL A   4      21.976  39.014  35.109  1.00 33.53           N  
-ATOM     28  CA  VAL A   4      22.776  37.818  35.355  1.00 33.30           C  
-ATOM     29  C   VAL A   4      22.495  36.841  34.182  1.00 32.04           C  
-ATOM     30  O   VAL A   4      21.355  36.410  34.018  1.00 31.08           O  
-ATOM     31  CB  VAL A   4      22.484  37.214  36.723  1.00 37.97           C  
-ATOM     32  CG1 VAL A   4      23.342  35.986  36.974  1.00 37.58           C  
-ATOM     33  CG2 VAL A   4      22.881  38.214  37.809  1.00 32.81           C  
-ATOM     34  N   THR A   5      23.544  36.407  33.462  1.00 27.26           N  
-ATOM     35  CA  THR A   5      23.365  35.371  32.450  1.00 31.96           C  
-ATOM     36  C   THR A   5      24.032  34.065  32.869  1.00 32.35           C  
-ATOM     37  O   THR A   5      25.209  34.120  33.283  1.00 31.94           O  
-ATOM     38  CB  THR A   5      24.017  35.891  31.114  1.00 32.43           C  
-ATOM     39  OG1 THR A   5      23.264  37.077  30.909  1.00 32.20           O  
-ATOM     40  CG2 THR A   5      23.680  34.866  29.998  1.00 26.11           C  
-ATOM     41  N   ALA A   6      23.449  32.930  32.545  1.00 30.94           N  
-ATOM     42  CA  ALA A   6      24.155  31.662  32.722  1.00 27.61           C  
-ATOM     43  C   ALA A   6      23.873  30.760  31.490  1.00 28.97           C  
-ATOM     44  O   ALA A   6      22.737  30.719  31.009  1.00 27.66           O  
-ATOM     45  CB  ALA A   6      23.702  30.902  33.953  1.00 21.88           C  
-ATOM     46  N   ILE A   7      24.848  29.971  31.137  1.00 24.72           N  
-ATOM     47  CA  ILE A   7      24.751  29.018  30.026  1.00 28.06           C  
-ATOM     48  C   ILE A   7      24.964  27.667  30.679  1.00 28.85           C  
-ATOM     49  O   ILE A   7      26.014  27.500  31.330  1.00 29.45           O  
-ATOM     50  CB  ILE A   7      25.856  29.233  28.977  1.00 32.00           C  
-ATOM     51  CG1 ILE A   7      25.515  30.658  28.407  1.00 40.81           C  
-ATOM     52  CG2 ILE A   7      25.767  28.186  27.845  1.00 29.42           C  
-ATOM     53  CD1 ILE A   7      26.795  31.439  28.329  1.00 49.10           C  
-ATOM     54  N   ILE A   8      23.864  26.925  30.766  1.00 23.25           N  
-ATOM     55  CA  ILE A   8      23.920  25.657  31.517  1.00 24.86           C  
-ATOM     56  C   ILE A   8      23.429  24.528  30.629  1.00 31.36           C  
-ATOM     57  O   ILE A   8      22.891  24.715  29.495  1.00 25.64           O  
-ATOM     58  CB  ILE A   8      22.984  25.823  32.754  1.00 29.78           C  
-ATOM     59  CG1 ILE A   8      21.589  25.986  32.239  1.00 30.81           C  
-ATOM     60  CG2 ILE A   8      23.511  26.918  33.712  1.00 28.67           C  
-ATOM     61  CD1 ILE A   8      20.420  25.917  33.210  1.00 29.37           C  
-ATOM     62  N   LYS A   9      23.607  23.319  31.153  1.00 25.86           N  
-ATOM     63  CA  LYS A   9      23.114  22.159  30.459  1.00 28.42           C  
-ATOM     64  C   LYS A   9      21.587  22.226  30.564  1.00 27.14           C  
-ATOM     65  O   LYS A   9      21.022  22.695  31.552  1.00 30.83           O  
-ATOM     66  CB  LYS A   9      23.659  20.839  31.042  1.00 31.92           C  
-ATOM     67  CG  LYS A   9      25.114  20.574  30.764  1.00 30.48           C  
-ATOM     68  CD  LYS A   9      25.708  19.625  31.782  1.00 33.87           C  
-ATOM     69  CE  LYS A   9      26.384  18.444  31.108  1.00 41.31           C  
-ATOM     70  NZ  LYS A   9      26.725  17.361  32.072  1.00 36.98           N  
-ATOM     71  N   PRO A  10      20.941  21.752  29.481  1.00 26.26           N  
-ATOM     72  CA  PRO A  10      19.487  21.833  29.271  1.00 29.14           C  
-ATOM     73  C   PRO A  10      18.607  21.323  30.418  1.00 27.12           C  
-ATOM     74  O   PRO A  10      17.666  21.983  30.852  1.00 26.84           O  
-ATOM     75  CB  PRO A  10      19.286  21.205  27.940  1.00 29.75           C  
-ATOM     76  CG  PRO A  10      20.485  21.680  27.230  1.00 28.60           C  
-ATOM     77  CD  PRO A  10      21.586  21.940  28.206  1.00 25.49           C  
-ATOM     78  N   PHE A  11      18.945  20.132  30.875  1.00 27.05           N  
-ATOM     79  CA  PHE A  11      18.176  19.441  31.892  1.00 31.58           C  
-ATOM     80  C   PHE A  11      18.403  19.964  33.304  1.00 33.48           C  
-ATOM     81  O   PHE A  11      17.816  19.441  34.263  1.00 32.94           O  
-ATOM     82  CB  PHE A  11      18.408  17.910  31.723  1.00 32.18           C  
-ATOM     83  CG  PHE A  11      17.826  17.340  30.463  1.00 26.07           C  
-ATOM     84  CD1 PHE A  11      18.499  16.384  29.698  1.00 32.95           C  
-ATOM     85  CD2 PHE A  11      16.581  17.767  30.007  1.00 32.15           C  
-ATOM     86  CE1 PHE A  11      17.921  15.884  28.557  1.00 38.80           C  
-ATOM     87  CE2 PHE A  11      16.004  17.283  28.882  1.00 39.09           C  
-ATOM     88  CZ  PHE A  11      16.662  16.325  28.136  1.00 25.49           C  
-ATOM     89  N   LYS A  12      19.267  20.969  33.473  1.00 27.50           N  
-ATOM     90  CA  LYS A  12      19.479  21.576  34.815  1.00 30.19           C  
-ATOM     91  C   LYS A  12      18.570  22.803  34.947  1.00 31.77           C  
-ATOM     92  O   LYS A  12      18.629  23.503  35.951  1.00 27.54           O  
-ATOM     93  CB  LYS A  12      20.942  21.993  35.027  1.00 29.12           C  
-ATOM     94  CG  LYS A  12      21.807  20.956  35.736  1.00 21.39           C  
-ATOM     95  CD  LYS A  12      21.357  20.682  37.164  1.00 28.76           C  
-ATOM     96  CE  LYS A  12      22.122  19.534  37.807  1.00 23.70           C  
-ATOM     97  NZ  LYS A  12      21.939  18.257  37.063  1.00 32.85           N  
-ATOM     98  N   LEU A  13      17.771  23.060  33.917  1.00 27.61           N  
-ATOM     99  CA  LEU A  13      16.911  24.257  33.947  1.00 27.22           C  
-ATOM    100  C   LEU A  13      15.983  24.290  35.161  1.00 25.44           C  
-ATOM    101  O   LEU A  13      16.059  25.229  35.958  1.00 25.25           O  
-ATOM    102  CB  LEU A  13      16.113  24.365  32.611  1.00 27.94           C  
-ATOM    103  CG  LEU A  13      15.398  25.694  32.263  1.00 41.34           C  
-ATOM    104  CD1 LEU A  13      14.356  25.475  31.177  1.00 29.00           C  
-ATOM    105  CD2 LEU A  13      14.768  26.295  33.514  1.00 39.61           C  
-ATOM    106  N   ASP A  14      15.132  23.301  35.307  1.00 24.69           N  
-ATOM    107  CA  ASP A  14      14.156  23.198  36.419  1.00 33.95           C  
-ATOM    108  C   ASP A  14      14.761  23.416  37.819  1.00 30.54           C  
-ATOM    109  O   ASP A  14      14.168  24.100  38.656  1.00 31.03           O  
-ATOM    110  CB  ASP A  14      13.393  21.877  36.312  1.00 40.11           C  
-ATOM    111  CG  ASP A  14      12.396  21.930  35.185  1.00 29.94           C  
-ATOM    112  OD1 ASP A  14      11.734  22.982  35.020  1.00 44.77           O  
-ATOM    113  OD2 ASP A  14      12.267  20.919  34.458  1.00 45.37           O  
-ATOM    114  N   GLU A  15      15.937  22.858  38.063  1.00 33.19           N  
-ATOM    115  CA  GLU A  15      16.611  23.023  39.340  1.00 35.81           C  
-ATOM    116  C   GLU A  15      17.084  24.430  39.534  1.00 35.68           C  
-ATOM    117  O   GLU A  15      16.859  25.025  40.587  1.00 37.64           O  
-ATOM    118  CB  GLU A  15      17.760  22.067  39.451  1.00 35.87           C  
-ATOM    119  CG  GLU A  15      17.338  20.769  40.095  1.00 44.48           C  
-ATOM    120  CD  GLU A  15      18.559  20.037  40.588  1.00 45.42           C  
-ATOM    121  OE1 GLU A  15      19.033  19.119  39.889  1.00 45.80           O  
-ATOM    122  OE2 GLU A  15      19.066  20.374  41.681  1.00 54.47           O  
-ATOM    123  N   VAL A  16      17.726  24.978  38.517  1.00 28.83           N  
-ATOM    124  CA  VAL A  16      18.164  26.341  38.627  1.00 29.30           C  
-ATOM    125  C   VAL A  16      17.016  27.260  38.901  1.00 31.33           C  
-ATOM    126  O   VAL A  16      17.099  28.099  39.796  1.00 30.75           O  
-ATOM    127  CB  VAL A  16      18.855  26.825  37.297  1.00 24.95           C  
-ATOM    128  CG1 VAL A  16      19.282  28.266  37.427  1.00 27.18           C  
-ATOM    129  CG2 VAL A  16      20.059  25.950  36.973  1.00 26.12           C  
-ATOM    130  N   ARG A  17      15.944  27.124  38.116  1.00 28.52           N  
-ATOM    131  CA  ARG A  17      14.752  27.929  38.315  1.00 33.68           C  
-ATOM    132  C   ARG A  17      14.275  27.830  39.754  1.00 31.90           C  
-ATOM    133  O   ARG A  17      14.101  28.841  40.437  1.00 36.63           O  
-ATOM    134  CB  ARG A  17      13.667  27.501  37.346  1.00 31.86           C  
-ATOM    135  CG  ARG A  17      12.367  28.221  37.542  1.00 36.46           C  
-ATOM    136  CD  ARG A  17      11.186  27.365  37.096  1.00 38.83           C  
-ATOM    137  NE  ARG A  17       9.994  28.186  37.156  1.00 48.59           N  
-ATOM    138  CZ  ARG A  17       8.737  27.841  36.829  1.00 45.86           C  
-ATOM    139  NH1 ARG A  17       8.467  26.615  36.376  1.00 43.68           N  
-ATOM    140  NH2 ARG A  17       7.746  28.731  36.970  1.00 52.33           N  
-ATOM    141  N   GLU A  18      14.077  26.581  40.248  1.00 30.59           N  
-ATOM    142  CA  GLU A  18      13.614  26.464  41.641  1.00 42.31           C  
-ATOM    143  C   GLU A  18      14.607  27.067  42.650  1.00 41.69           C  
-ATOM    144  O   GLU A  18      14.203  27.826  43.542  1.00 43.47           O  
-ATOM    145  CB  GLU A  18      13.347  24.989  41.915  1.00 37.60           C  
-ATOM    146  CG  GLU A  18      11.970  24.524  41.468  1.00 68.92           C  
-ATOM    147  CD  GLU A  18      10.850  25.456  41.922  1.00 79.38           C  
-ATOM    148  OE1 GLU A  18      10.467  25.389  43.121  1.00 87.63           O  
-ATOM    149  OE2 GLU A  18      10.373  26.248  41.073  1.00 83.40           O  
-ATOM    150  N   SER A  19      15.902  26.906  42.444  1.00 35.95           N  
-ATOM    151  CA  SER A  19      16.867  27.468  43.400  1.00 40.26           C  
-ATOM    152  C   SER A  19      16.864  28.975  43.399  1.00 41.28           C  
-ATOM    153  O   SER A  19      16.918  29.597  44.472  1.00 37.90           O  
-ATOM    154  CB  SER A  19      18.236  26.847  43.124  1.00 28.51           C  
-ATOM    155  OG  SER A  19      19.292  27.607  43.658  1.00 57.49           O  
-ATOM    156  N   LEU A  20      16.738  29.646  42.241  1.00 35.33           N  
-ATOM    157  CA  LEU A  20      16.567  31.089  42.156  1.00 34.35           C  
-ATOM    158  C   LEU A  20      15.332  31.583  42.938  1.00 38.56           C  
-ATOM    159  O   LEU A  20      15.289  32.668  43.554  1.00 33.58           O  
-ATOM    160  CB  LEU A  20      16.405  31.521  40.673  1.00 30.31           C  
-ATOM    161  CG  LEU A  20      17.565  32.146  39.917  1.00 37.94           C  
-ATOM    162  CD1 LEU A  20      18.775  32.625  40.699  1.00 27.48           C  
-ATOM    163  CD2 LEU A  20      17.984  31.429  38.615  1.00 39.62           C  
-ATOM    164  N   ALA A  21      14.213  30.883  42.740  1.00 35.76           N  
-ATOM    165  CA  ALA A  21      12.932  31.227  43.315  1.00 45.89           C  
-ATOM    166  C   ALA A  21      12.943  31.164  44.871  1.00 46.16           C  
-ATOM    167  O   ALA A  21      12.450  32.094  45.511  1.00 46.01           O  
-ATOM    168  CB  ALA A  21      11.816  30.319  42.852  1.00 48.52           C  
-ATOM    169  N   GLU A  22      13.832  30.338  45.384  1.00 47.09           N  
-ATOM    170  CA  GLU A  22      14.049  30.263  46.812  1.00 57.45           C  
-ATOM    171  C   GLU A  22      14.716  31.562  47.299  1.00 52.42           C  
-ATOM    172  O   GLU A  22      14.617  31.845  48.500  1.00 53.64           O  
-ATOM    173  CB  GLU A  22      14.928  29.133  47.264  1.00 65.09           C  
-ATOM    174  CG  GLU A  22      14.482  27.695  47.300  1.00 88.33           C  
-ATOM    175  CD  GLU A  22      15.748  26.827  47.304  1.00100.14           C  
-ATOM    176  OE1 GLU A  22      15.762  25.763  46.649  1.00107.10           O  
-ATOM    177  OE2 GLU A  22      16.732  27.245  47.965  1.00109.11           O  
-ATOM    178  N   VAL A  23      15.518  32.184  46.472  1.00 45.44           N  
-ATOM    179  CA  VAL A  23      16.169  33.419  46.880  1.00 42.53           C  
-ATOM    180  C   VAL A  23      15.386  34.623  46.376  1.00 42.30           C  
-ATOM    181  O   VAL A  23      15.899  35.735  46.547  1.00 44.92           O  
-ATOM    182  CB  VAL A  23      17.650  33.619  46.585  1.00 52.68           C  
-ATOM    183  CG1 VAL A  23      18.493  32.649  47.417  1.00 47.29           C  
-ATOM    184  CG2 VAL A  23      18.004  33.498  45.102  1.00 46.40           C  
-ATOM    185  N   GLY A  24      14.139  34.400  45.969  1.00 40.04           N  
-ATOM    186  CA  GLY A  24      13.247  35.481  45.523  1.00 44.27           C  
-ATOM    187  C   GLY A  24      13.377  35.954  44.083  1.00 45.47           C  
-ATOM    188  O   GLY A  24      12.985  37.088  43.725  1.00 46.77           O  
-ATOM    189  N   VAL A  25      14.150  35.218  43.288  1.00 44.42           N  
-ATOM    190  CA  VAL A  25      14.421  35.674  41.908  1.00 44.95           C  
-ATOM    191  C   VAL A  25      13.571  34.914  40.906  1.00 39.17           C  
-ATOM    192  O   VAL A  25      13.768  33.707  40.752  1.00 42.18           O  
-ATOM    193  CB  VAL A  25      15.898  35.466  41.523  1.00 38.96           C  
-ATOM    194  CG1 VAL A  25      16.102  35.921  40.060  1.00 51.00           C  
-ATOM    195  CG2 VAL A  25      16.763  36.301  42.457  1.00 45.22           C  
-ATOM    196  N   THR A  26      12.682  35.602  40.203  1.00 37.04           N  
-ATOM    197  CA  THR A  26      11.861  34.957  39.176  1.00 40.10           C  
-ATOM    198  C   THR A  26      11.961  35.895  37.944  1.00 40.61           C  
-ATOM    199  O   THR A  26      12.646  36.929  37.999  1.00 42.36           O  
-ATOM    200  CB  THR A  26      10.395  34.796  39.622  1.00 44.63           C  
-ATOM    201  OG1 THR A  26       9.989  36.119  40.030  1.00 49.52           O  
-ATOM    202  CG2 THR A  26      10.144  33.907  40.819  1.00 50.71           C  
-ATOM    203  N   GLY A  27      11.307  35.646  36.846  1.00 39.86           N  
-ATOM    204  CA  GLY A  27      11.292  36.525  35.679  1.00 40.09           C  
-ATOM    205  C   GLY A  27      12.403  36.103  34.706  1.00 37.06           C  
-ATOM    206  O   GLY A  27      13.091  36.964  34.176  1.00 37.02           O  
-ATOM    207  N   LEU A  28      12.763  34.820  34.755  1.00 32.13           N  
-ATOM    208  CA  LEU A  28      13.779  34.282  33.897  1.00 31.44           C  
-ATOM    209  C   LEU A  28      13.308  34.396  32.433  1.00 28.71           C  
-ATOM    210  O   LEU A  28      12.218  33.985  32.100  1.00 30.26           O  
-ATOM    211  CB  LEU A  28      14.047  32.776  34.079  1.00 31.70           C  
-ATOM    212  CG  LEU A  28      14.384  32.120  35.399  1.00 44.33           C  
-ATOM    213  CD1 LEU A  28      15.051  30.726  35.335  1.00 39.00           C  
-ATOM    214  CD2 LEU A  28      15.250  33.031  36.227  1.00 51.76           C  
-ATOM    215  N   THR A  29      14.279  34.740  31.601  1.00 30.48           N  
-ATOM    216  CA  THR A  29      14.153  34.571  30.126  1.00 30.06           C  
-ATOM    217  C   THR A  29      14.997  33.347  29.686  1.00 25.65           C  
-ATOM    218  O   THR A  29      16.176  33.269  30.063  1.00 25.50           O  
-ATOM    219  CB  THR A  29      14.591  35.830  29.386  1.00 28.37           C  
-ATOM    220  OG1 THR A  29      13.577  36.827  29.499  1.00 31.52           O  
-ATOM    221  CG2 THR A  29      14.859  35.498  27.933  1.00 38.35           C  
-ATOM    222  N   VAL A  30      14.472  32.424  28.914  1.00 23.03           N  
-ATOM    223  CA  VAL A  30      15.181  31.226  28.486  1.00 23.96           C  
-ATOM    224  C   VAL A  30      15.361  31.198  26.965  1.00 25.24           C  
-ATOM    225  O   VAL A  30      14.391  31.372  26.235  1.00 24.27           O  
-ATOM    226  CB  VAL A  30      14.407  29.967  28.903  1.00 21.88           C  
-ATOM    227  CG1 VAL A  30      15.116  28.712  28.402  1.00 23.68           C  
-ATOM    228  CG2 VAL A  30      14.247  29.924  30.414  1.00 26.70           C  
-ATOM    229  N   THR A  31      16.586  30.964  26.518  1.00 24.32           N  
-ATOM    230  CA  THR A  31      16.890  30.821  25.106  1.00 27.63           C  
-ATOM    231  C   THR A  31      17.628  29.502  24.825  1.00 28.02           C  
-ATOM    232  O   THR A  31      18.562  29.163  25.546  1.00 22.52           O  
-ATOM    233  CB  THR A  31      17.863  31.916  24.612  1.00 24.32           C  
-ATOM    234  OG1 THR A  31      17.382  33.214  25.010  1.00 23.60           O  
-ATOM    235  CG2 THR A  31      17.988  31.863  23.100  1.00 23.11           C  
-ATOM    236  N   GLU A  32      17.211  28.774  23.816  1.00 21.39           N  
-ATOM    237  CA  GLU A  32      17.939  27.554  23.421  1.00 26.94           C  
-ATOM    238  C   GLU A  32      19.160  28.007  22.598  1.00 24.56           C  
-ATOM    239  O   GLU A  32      18.996  28.785  21.665  1.00 24.88           O  
-ATOM    240  CB  GLU A  32      17.059  26.633  22.576  1.00 30.63           C  
-ATOM    241  CG  GLU A  32      16.030  25.913  23.426  1.00 38.15           C  
-ATOM    242  CD  GLU A  32      15.214  24.944  22.611  1.00 43.43           C  
-ATOM    243  OE1 GLU A  32      15.828  24.147  21.863  1.00 40.99           O  
-ATOM    244  OE2 GLU A  32      13.969  24.964  22.706  1.00 43.47           O  
-ATOM    245  N   VAL A  33      20.385  27.554  22.899  1.00 22.72           N  
-ATOM    246  CA  VAL A  33      21.574  27.964  22.147  1.00 24.10           C  
-ATOM    247  C   VAL A  33      22.454  26.740  21.892  1.00 23.35           C  
-ATOM    248  O   VAL A  33      22.207  25.681  22.476  1.00 23.76           O  
-ATOM    249  CB  VAL A  33      22.445  28.990  22.936  1.00 28.75           C  
-ATOM    250  CG1 VAL A  33      21.683  30.274  23.181  1.00 26.01           C  
-ATOM    251  CG2 VAL A  33      22.907  28.395  24.251  1.00 27.03           C  
-ATOM    252  N   LYS A  34      23.497  26.886  21.056  1.00 21.14           N  
-ATOM    253  CA  LYS A  34      24.488  25.779  20.817  1.00 22.39           C  
-ATOM    254  C   LYS A  34      25.829  26.171  21.452  1.00 27.02           C  
-ATOM    255  O   LYS A  34      26.138  27.367  21.554  1.00 28.99           O  
-ATOM    256  CB  LYS A  34      24.751  25.517  19.302  1.00 28.05           C  
-ATOM    257  CG  LYS A  34      23.508  25.154  18.493  1.00 31.15           C  
-ATOM    258  CD  LYS A  34      22.698  24.038  19.146  1.00 39.05           C  
-ATOM    259  CE  LYS A  34      21.677  23.426  18.200  1.00 37.60           C  
-ATOM    260  NZ  LYS A  34      21.118  22.149  18.739  1.00 36.68           N  
-ATOM    261  N   GLY A  35      26.573  25.160  21.914  1.00 21.25           N  
-ATOM    262  CA  GLY A  35      27.894  25.274  22.480  1.00 26.94           C  
-ATOM    263  C   GLY A  35      28.720  24.272  21.679  1.00 29.12           C  
-ATOM    264  O   GLY A  35      28.153  23.509  20.889  1.00 30.67           O  
-ATOM    265  N   PHE A  36      30.022  24.246  21.848  1.00 28.59           N  
-ATOM    266  CA  PHE A  36      30.862  23.307  21.116  1.00 31.03           C  
-ATOM    267  C   PHE A  36      31.639  22.390  22.029  1.00 36.58           C  
-ATOM    268  O   PHE A  36      32.277  22.912  22.948  1.00 35.37           O  
-ATOM    269  CB  PHE A  36      31.917  24.091  20.266  1.00 30.01           C  
-ATOM    270  CG  PHE A  36      31.120  24.766  19.162  1.00 33.46           C  
-ATOM    271  CD1 PHE A  36      30.939  26.122  19.120  1.00 38.23           C  
-ATOM    272  CD2 PHE A  36      30.494  23.983  18.196  1.00 34.14           C  
-ATOM    273  CE1 PHE A  36      30.194  26.699  18.113  1.00 41.95           C  
-ATOM    274  CE2 PHE A  36      29.756  24.549  17.196  1.00 35.56           C  
-ATOM    275  CZ  PHE A  36      29.599  25.922  17.152  1.00 36.83           C  
-ATOM    276  N   GLY A  37      31.607  21.090  21.740  1.00 33.07           N  
-ATOM    277  CA  GLY A  37      32.314  20.149  22.607  1.00 35.54           C  
-ATOM    278  C   GLY A  37      33.674  19.863  21.943  1.00 41.97           C  
-ATOM    279  O   GLY A  37      34.486  19.164  22.487  1.00 45.83           O  
-ATOM    280  N   TYR A  51      33.418   8.577  19.577  1.00 45.33           N  
-ATOM    281  CA  TYR A  51      33.164   9.891  18.892  1.00 40.12           C  
-ATOM    282  C   TYR A  51      32.900  11.061  19.838  1.00 31.02           C  
-ATOM    283  O   TYR A  51      31.940  11.040  20.604  1.00 32.64           O  
-ATOM    284  CB  TYR A  51      32.034   9.724  17.901  1.00 37.83           C  
-ATOM    285  CG  TYR A  51      31.568  10.818  17.000  1.00 36.90           C  
-ATOM    286  CD1 TYR A  51      31.959  10.891  15.662  1.00 36.53           C  
-ATOM    287  CD2 TYR A  51      30.653  11.754  17.491  1.00 36.10           C  
-ATOM    288  CE1 TYR A  51      31.468  11.912  14.846  1.00 40.18           C  
-ATOM    289  CE2 TYR A  51      30.165  12.771  16.699  1.00 37.87           C  
-ATOM    290  CZ  TYR A  51      30.594  12.836  15.380  1.00 37.46           C  
-ATOM    291  OH  TYR A  51      30.115  13.837  14.609  1.00 40.24           O  
-ATOM    292  N   VAL A  52      33.653  12.116  19.637  1.00 32.84           N  
-ATOM    293  CA  VAL A  52      33.472  13.305  20.479  1.00 35.39           C  
-ATOM    294  C   VAL A  52      32.429  14.205  19.856  1.00 33.11           C  
-ATOM    295  O   VAL A  52      32.738  14.767  18.810  1.00 33.39           O  
-ATOM    296  CB  VAL A  52      34.834  14.008  20.622  1.00 39.66           C  
-ATOM    297  CG1 VAL A  52      34.673  15.322  21.409  1.00 38.99           C  
-ATOM    298  CG2 VAL A  52      35.778  13.098  21.416  1.00 43.39           C  
-ATOM    299  N   VAL A  53      31.276  14.400  20.466  1.00 32.50           N  
-ATOM    300  CA  VAL A  53      30.268  15.286  19.908  1.00 30.30           C  
-ATOM    301  C   VAL A  53      30.780  16.732  19.870  1.00 34.51           C  
-ATOM    302  O   VAL A  53      31.476  17.166  20.781  1.00 30.78           O  
-ATOM    303  CB  VAL A  53      28.980  15.173  20.728  1.00 33.53           C  
-ATOM    304  CG1 VAL A  53      27.972  16.226  20.282  1.00 35.95           C  
-ATOM    305  CG2 VAL A  53      28.389  13.774  20.622  1.00 29.73           C  
-ATOM    306  N   ASP A  54      30.430  17.472  18.807  1.00 25.98           N  
-ATOM    307  CA  ASP A  54      30.810  18.905  18.636  1.00 27.72           C  
-ATOM    308  C   ASP A  54      29.656  19.838  18.936  1.00 28.64           C  
-ATOM    309  O   ASP A  54      29.648  20.489  19.966  1.00 28.24           O  
-ATOM    310  CB  ASP A  54      31.365  19.161  17.225  1.00 32.05           C  
-ATOM    311  CG  ASP A  54      32.195  20.417  17.207  1.00 39.52           C  
-ATOM    312  OD1 ASP A  54      32.632  20.863  18.299  1.00 37.59           O  
-ATOM    313  OD2 ASP A  54      32.414  20.965  16.105  1.00 34.32           O  
-ATOM    314  N   PHE A  55      28.624  19.913  18.081  1.00 23.56           N  
-ATOM    315  CA  PHE A  55      27.461  20.782  18.332  1.00 28.62           C  
-ATOM    316  C   PHE A  55      26.643  20.284  19.569  1.00 25.48           C  
-ATOM    317  O   PHE A  55      26.153  19.161  19.554  1.00 25.09           O  
-ATOM    318  CB  PHE A  55      26.574  20.826  17.084  1.00 26.21           C  
-ATOM    319  CG  PHE A  55      27.096  21.717  16.017  1.00 31.72           C  
-ATOM    320  CD1 PHE A  55      28.215  21.367  15.290  1.00 34.91           C  
-ATOM    321  CD2 PHE A  55      26.453  22.907  15.757  1.00 33.19           C  
-ATOM    322  CE1 PHE A  55      28.686  22.218  14.338  1.00 43.43           C  
-ATOM    323  CE2 PHE A  55      26.917  23.774  14.786  1.00 33.03           C  
-ATOM    324  CZ  PHE A  55      28.046  23.416  14.085  1.00 28.64           C  
-ATOM    325  N   LEU A  56      26.482  21.101  20.618  1.00 24.43           N  
-ATOM    326  CA  LEU A  56      25.787  20.644  21.859  1.00 25.26           C  
-ATOM    327  C   LEU A  56      24.629  21.551  22.307  1.00 24.55           C  
-ATOM    328  O   LEU A  56      24.690  22.766  22.183  1.00 26.13           O  
-ATOM    329  CB  LEU A  56      26.802  20.511  23.011  1.00 29.60           C  
-ATOM    330  CG  LEU A  56      27.920  19.470  22.807  1.00 38.33           C  
-ATOM    331  CD1 LEU A  56      28.994  19.604  23.887  1.00 39.96           C  
-ATOM    332  CD2 LEU A  56      27.327  18.069  22.788  1.00 39.58           C  
-ATOM    333  N   PRO A  57      23.598  20.912  22.830  1.00 22.07           N  
-ATOM    334  CA  PRO A  57      22.475  21.678  23.381  1.00 26.27           C  
-ATOM    335  C   PRO A  57      22.831  22.548  24.555  1.00 28.66           C  
-ATOM    336  O   PRO A  57      23.469  22.060  25.488  1.00 21.55           O  
-ATOM    337  CB  PRO A  57      21.444  20.635  23.706  1.00 24.53           C  
-ATOM    338  CG  PRO A  57      21.624  19.691  22.576  1.00 25.85           C  
-ATOM    339  CD  PRO A  57      23.000  19.857  21.998  1.00 20.40           C  
-ATOM    340  N   LYS A  58      22.428  23.775  24.614  1.00 27.11           N  
-ATOM    341  CA  LYS A  58      22.643  24.431  25.884  1.00 27.04           C  
-ATOM    342  C   LYS A  58      21.449  25.294  26.065  1.00 28.40           C  
-ATOM    343  O   LYS A  58      20.603  25.424  25.194  1.00 22.85           O  
-ATOM    344  CB  LYS A  58      23.909  25.295  25.943  1.00 24.54           C  
-ATOM    345  CG  LYS A  58      25.199  24.509  25.734  1.00 30.19           C  
-ATOM    346  CD  LYS A  58      25.683  23.866  27.025  1.00 42.60           C  
-ATOM    347  CE  LYS A  58      26.906  23.003  26.785  1.00 52.92           C  
-ATOM    348  NZ  LYS A  58      27.144  22.045  27.899  1.00 43.85           N  
-ATOM    349  N   VAL A  59      21.394  25.882  27.213  1.00 22.96           N  
-ATOM    350  CA  VAL A  59      20.309  26.738  27.506  1.00 24.93           C  
-ATOM    351  C   VAL A  59      20.879  27.981  28.125  1.00 30.10           C  
-ATOM    352  O   VAL A  59      21.735  27.907  28.998  1.00 29.34           O  
-ATOM    353  CB  VAL A  59      19.267  26.018  28.380  1.00 35.78           C  
-ATOM    354  CG1 VAL A  59      18.662  26.992  29.387  1.00 38.18           C  
-ATOM    355  CG2 VAL A  59      18.194  25.390  27.522  1.00 27.27           C  
-ATOM    356  N   LYS A  60      20.413  29.111  27.665  1.00 24.82           N  
-ATOM    357  CA  LYS A  60      20.926  30.361  28.237  1.00 28.70           C  
-ATOM    358  C   LYS A  60      19.733  30.865  29.096  1.00 28.41           C  
-ATOM    359  O   LYS A  60      18.572  30.904  28.614  1.00 26.64           O  
-ATOM    360  CB  LYS A  60      21.198  31.420  27.212  1.00 29.87           C  
-ATOM    361  CG  LYS A  60      21.683  32.756  27.782  1.00 34.06           C  
-ATOM    362  CD  LYS A  60      21.619  33.801  26.705  1.00 33.61           C  
-ATOM    363  CE  LYS A  60      22.970  33.885  26.000  1.00 43.87           C  
-ATOM    364  NZ  LYS A  60      22.821  35.151  25.185  1.00 46.28           N  
-ATOM    365  N   ILE A  61      20.116  31.258  30.284  1.00 23.83           N  
-ATOM    366  CA  ILE A  61      19.144  31.943  31.172  1.00 27.87           C  
-ATOM    367  C   ILE A  61      19.565  33.341  31.463  1.00 23.09           C  
-ATOM    368  O   ILE A  61      20.739  33.635  31.700  1.00 28.66           O  
-ATOM    369  CB  ILE A  61      18.980  31.224  32.531  1.00 39.50           C  
-ATOM    370  CG1 ILE A  61      18.355  29.834  32.269  1.00 35.60           C  
-ATOM    371  CG2 ILE A  61      18.031  31.988  33.443  1.00 44.47           C  
-ATOM    372  CD1 ILE A  61      18.774  29.017  33.518  1.00 52.22           C  
-ATOM    373  N   GLU A  62      18.605  34.270  31.504  1.00 28.75           N  
-ATOM    374  CA  GLU A  62      18.933  35.660  31.726  1.00 27.18           C  
-ATOM    375  C   GLU A  62      17.917  36.285  32.702  1.00 29.23           C  
-ATOM    376  O   GLU A  62      16.713  35.995  32.645  1.00 27.40           O  
-ATOM    377  CB  GLU A  62      18.906  36.545  30.483  1.00 26.54           C  
-ATOM    378  CG  GLU A  62      19.977  36.191  29.422  1.00 31.60           C  
-ATOM    379  CD  GLU A  62      19.561  36.877  28.116  1.00 40.97           C  
-ATOM    380  OE1 GLU A  62      18.398  36.701  27.697  1.00 33.62           O  
-ATOM    381  OE2 GLU A  62      20.378  37.624  27.553  1.00 40.83           O  
-ATOM    382  N   VAL A  63      18.423  36.980  33.710  1.00 29.94           N  
-ATOM    383  CA  VAL A  63      17.537  37.699  34.684  1.00 35.98           C  
-ATOM    384  C   VAL A  63      18.211  39.031  35.074  1.00 36.13           C  
-ATOM    385  O   VAL A  63      19.412  39.142  35.204  1.00 34.79           O  
-ATOM    386  CB  VAL A  63      17.322  37.027  36.047  1.00 40.35           C  
-ATOM    387  CG1 VAL A  63      16.666  35.689  35.925  1.00 53.83           C  
-ATOM    388  CG2 VAL A  63      18.703  36.727  36.721  1.00 39.73           C  
-ATOM    389  N   VAL A  64      17.415  40.055  35.260  1.00 39.61           N  
-ATOM    390  CA  VAL A  64      17.873  41.365  35.686  1.00 40.42           C  
-ATOM    391  C   VAL A  64      17.395  41.505  37.132  1.00 35.33           C  
-ATOM    392  O   VAL A  64      16.254  41.234  37.484  1.00 33.49           O  
-ATOM    393  CB  VAL A  64      17.278  42.408  34.741  1.00 43.82           C  
-ATOM    394  CG1 VAL A  64      17.547  43.815  35.229  1.00 39.26           C  
-ATOM    395  CG2 VAL A  64      17.848  42.218  33.316  1.00 39.09           C  
-ATOM    396  N   VAL A  65      18.320  41.766  38.005  1.00 36.19           N  
-ATOM    397  CA  VAL A  65      18.114  41.888  39.434  1.00 42.21           C  
-ATOM    398  C   VAL A  65      18.668  43.217  39.979  1.00 40.57           C  
-ATOM    399  O   VAL A  65      19.597  43.832  39.461  1.00 32.97           O  
-ATOM    400  CB  VAL A  65      18.759  40.737  40.233  1.00 48.70           C  
-ATOM    401  CG1 VAL A  65      18.058  39.405  39.948  1.00 53.90           C  
-ATOM    402  CG2 VAL A  65      20.245  40.617  39.928  1.00 50.13           C  
-ATOM    403  N   ASP A  66      18.097  43.564  41.150  1.00 46.13           N  
-ATOM    404  CA  ASP A  66      18.726  44.735  41.851  1.00 44.85           C  
-ATOM    405  C   ASP A  66      20.154  44.436  42.197  1.00 39.52           C  
-ATOM    406  O   ASP A  66      20.498  43.283  42.591  1.00 42.34           O  
-ATOM    407  CB  ASP A  66      17.920  44.915  43.171  1.00 58.73           C  
-ATOM    408  CG  ASP A  66      18.450  46.244  43.751  1.00 67.80           C  
-ATOM    409  OD1 ASP A  66      18.725  46.213  44.956  1.00 64.26           O  
-ATOM    410  OD2 ASP A  66      18.566  47.183  42.913  1.00 67.77           O  
-ATOM    411  N   ASP A  67      21.054  45.350  42.308  1.00 43.11           N  
-ATOM    412  CA  ASP A  67      22.448  45.129  42.681  1.00 48.89           C  
-ATOM    413  C   ASP A  67      22.735  44.263  43.883  1.00 48.40           C  
-ATOM    414  O   ASP A  67      23.679  43.450  43.890  1.00 47.17           O  
-ATOM    415  CB  ASP A  67      23.095  46.517  42.843  1.00 57.18           C  
-ATOM    416  CG  ASP A  67      23.289  47.226  41.519  1.00 65.31           C  
-ATOM    417  OD1 ASP A  67      22.766  46.805  40.460  1.00 62.82           O  
-ATOM    418  OD2 ASP A  67      23.993  48.268  41.518  1.00 56.70           O  
-ATOM    419  N   LYS A  68      21.994  44.368  44.968  1.00 49.47           N  
-ATOM    420  CA  LYS A  68      22.293  43.620  46.188  1.00 51.69           C  
-ATOM    421  C   LYS A  68      21.887  42.154  46.129  1.00 56.44           C  
-ATOM    422  O   LYS A  68      22.168  41.456  47.103  1.00 59.61           O  
-ATOM    423  CB  LYS A  68      21.526  44.194  47.376  1.00 60.48           C  
-ATOM    424  CG  LYS A  68      21.259  45.679  47.450  1.00 73.29           C  
-ATOM    425  CD  LYS A  68      19.825  45.881  47.946  1.00 83.03           C  
-ATOM    426  CE  LYS A  68      19.421  47.313  48.212  1.00 82.14           C  
-ATOM    427  NZ  LYS A  68      19.161  48.126  46.998  1.00 85.25           N  
-ATOM    428  N   VAL A  69      21.150  41.674  45.132  1.00 52.02           N  
-ATOM    429  CA  VAL A  69      20.657  40.318  45.033  1.00 48.61           C  
-ATOM    430  C   VAL A  69      21.606  39.447  44.217  1.00 45.69           C  
-ATOM    431  O   VAL A  69      21.528  38.228  44.203  1.00 45.57           O  
-ATOM    432  CB  VAL A  69      19.299  40.379  44.288  1.00 55.09           C  
-ATOM    433  CG1 VAL A  69      18.668  39.029  44.025  1.00 43.79           C  
-ATOM    434  CG2 VAL A  69      18.333  41.244  45.098  1.00 51.80           C  
-ATOM    435  N   VAL A  70      22.510  40.079  43.498  1.00 43.36           N  
-ATOM    436  CA  VAL A  70      23.440  39.414  42.604  1.00 44.51           C  
-ATOM    437  C   VAL A  70      24.185  38.249  43.209  1.00 46.65           C  
-ATOM    438  O   VAL A  70      24.422  37.240  42.529  1.00 38.28           O  
-ATOM    439  CB  VAL A  70      24.497  40.384  42.037  1.00 49.69           C  
-ATOM    440  CG1 VAL A  70      25.404  39.701  41.023  1.00 46.62           C  
-ATOM    441  CG2 VAL A  70      23.819  41.561  41.364  1.00 56.67           C  
-ATOM    442  N   GLU A  71      24.839  38.537  44.362  1.00 44.69           N  
-ATOM    443  CA  GLU A  71      25.593  37.476  45.013  1.00 45.17           C  
-ATOM    444  C   GLU A  71      24.723  36.260  45.297  1.00 37.74           C  
-ATOM    445  O   GLU A  71      25.192  35.151  45.059  1.00 42.72           O  
-ATOM    446  CB  GLU A  71      26.254  37.895  46.335  1.00 58.08           C  
-ATOM    447  CG  GLU A  71      27.737  38.248  46.256  1.00 74.88           C  
-ATOM    448  CD  GLU A  71      28.167  38.971  47.535  1.00 85.89           C  
-ATOM    449  OE1 GLU A  71      27.953  38.424  48.639  1.00 84.26           O  
-ATOM    450  OE2 GLU A  71      28.707  40.096  47.431  1.00 90.74           O  
-ATOM    451  N   GLN A  72      23.554  36.363  45.879  1.00 36.49           N  
-ATOM    452  CA  GLN A  72      22.754  35.183  46.203  1.00 38.70           C  
-ATOM    453  C   GLN A  72      22.091  34.564  44.946  1.00 38.90           C  
-ATOM    454  O   GLN A  72      21.895  33.344  44.920  1.00 38.40           O  
-ATOM    455  CB  GLN A  72      21.700  35.459  47.274  1.00 42.69           C  
-ATOM    456  CG  GLN A  72      20.411  36.117  46.793  1.00 65.30           C  
-ATOM    457  CD  GLN A  72      19.934  37.207  47.754  1.00 79.34           C  
-ATOM    458  OE1 GLN A  72      20.721  37.707  48.579  1.00 75.99           O  
-ATOM    459  NE2 GLN A  72      18.654  37.581  47.652  1.00 76.84           N  
-ATOM    460  N   ALA A  73      21.925  35.368  43.896  1.00 40.73           N  
-ATOM    461  CA  ALA A  73      21.415  34.832  42.617  1.00 39.43           C  
-ATOM    462  C   ALA A  73      22.474  33.944  42.013  1.00 34.68           C  
-ATOM    463  O   ALA A  73      22.247  32.804  41.621  1.00 39.06           O  
-ATOM    464  CB  ALA A  73      21.032  36.024  41.713  1.00 31.93           C  
-ATOM    465  N   VAL A  74      23.721  34.424  41.981  1.00 35.97           N  
-ATOM    466  CA  VAL A  74      24.856  33.653  41.521  1.00 37.31           C  
-ATOM    467  C   VAL A  74      25.092  32.423  42.370  1.00 43.33           C  
-ATOM    468  O   VAL A  74      25.320  31.299  41.860  1.00 41.52           O  
-ATOM    469  CB  VAL A  74      26.090  34.556  41.475  1.00 44.90           C  
-ATOM    470  CG1 VAL A  74      27.375  33.788  41.245  1.00 44.58           C  
-ATOM    471  CG2 VAL A  74      25.832  35.610  40.391  1.00 52.51           C  
-ATOM    472  N   ASP A  75      24.978  32.605  43.696  1.00 39.65           N  
-ATOM    473  CA  ASP A  75      25.096  31.487  44.605  1.00 39.54           C  
-ATOM    474  C   ASP A  75      24.103  30.397  44.288  1.00 33.57           C  
-ATOM    475  O   ASP A  75      24.457  29.198  44.211  1.00 34.35           O  
-ATOM    476  CB  ASP A  75      24.914  31.953  46.081  1.00 54.32           C  
-ATOM    477  CG  ASP A  75      25.204  30.823  47.051  1.00 65.65           C  
-ATOM    478  OD1 ASP A  75      26.229  30.118  46.852  1.00 73.88           O  
-ATOM    479  OD2 ASP A  75      24.443  30.588  48.015  1.00 72.08           O  
-ATOM    480  N   ALA A  76      22.837  30.796  44.146  1.00 30.06           N  
-ATOM    481  CA  ALA A  76      21.809  29.785  43.853  1.00 35.42           C  
-ATOM    482  C   ALA A  76      22.001  29.076  42.497  1.00 33.99           C  
-ATOM    483  O   ALA A  76      21.679  27.893  42.389  1.00 31.90           O  
-ATOM    484  CB  ALA A  76      20.453  30.530  43.908  1.00 34.05           C  
-ATOM    485  N   ILE A  77      22.545  29.774  41.488  1.00 31.10           N  
-ATOM    486  CA  ILE A  77      22.695  29.065  40.188  1.00 39.61           C  
-ATOM    487  C   ILE A  77      23.791  28.015  40.367  1.00 35.06           C  
-ATOM    488  O   ILE A  77      23.659  26.854  39.935  1.00 31.60           O  
-ATOM    489  CB  ILE A  77      23.019  29.976  38.991  1.00 33.56           C  
-ATOM    490  CG1 ILE A  77      21.845  30.899  38.723  1.00 33.14           C  
-ATOM    491  CG2 ILE A  77      23.438  29.177  37.732  1.00 36.17           C  
-ATOM    492  CD1 ILE A  77      22.152  32.245  38.046  1.00 25.60           C  
-ATOM    493  N   ILE A  78      24.872  28.404  41.054  1.00 37.31           N  
-ATOM    494  CA  ILE A  78      25.965  27.475  41.292  1.00 36.00           C  
-ATOM    495  C   ILE A  78      25.494  26.251  42.052  1.00 35.10           C  
-ATOM    496  O   ILE A  78      25.783  25.129  41.613  1.00 34.49           O  
-ATOM    497  CB  ILE A  78      27.162  27.936  42.119  1.00 51.13           C  
-ATOM    498  CG1 ILE A  78      27.590  29.310  41.632  1.00 48.92           C  
-ATOM    499  CG2 ILE A  78      28.290  26.886  42.088  1.00 38.93           C  
-ATOM    500  CD1 ILE A  78      28.716  29.493  40.712  1.00 45.42           C  
-ATOM    501  N   LYS A  79      24.694  26.510  43.077  1.00 36.18           N  
-ATOM    502  CA  LYS A  79      24.307  25.334  43.873  1.00 37.04           C  
-ATOM    503  C   LYS A  79      23.556  24.333  43.001  1.00 35.50           C  
-ATOM    504  O   LYS A  79      23.657  23.167  43.288  1.00 35.79           O  
-ATOM    505  CB  LYS A  79      23.484  25.728  45.093  1.00 47.86           C  
-ATOM    506  CG  LYS A  79      24.385  26.473  46.084  1.00 73.18           C  
-ATOM    507  CD  LYS A  79      23.821  26.710  47.460  1.00 77.98           C  
-ATOM    508  CE  LYS A  79      22.523  27.469  47.563  1.00 81.16           C  
-ATOM    509  NZ  LYS A  79      21.321  26.594  47.447  1.00 90.83           N  
-ATOM    510  N   ALA A  80      22.537  24.748  42.273  1.00 37.38           N  
-ATOM    511  CA  ALA A  80      21.699  23.941  41.421  1.00 35.27           C  
-ATOM    512  C   ALA A  80      22.420  23.308  40.218  1.00 35.06           C  
-ATOM    513  O   ALA A  80      22.284  22.103  39.965  1.00 34.11           O  
-ATOM    514  CB  ALA A  80      20.582  24.872  40.907  1.00 32.33           C  
-ATOM    515  N   ALA A  81      23.343  23.983  39.558  1.00 30.88           N  
-ATOM    516  CA  ALA A  81      23.919  23.376  38.344  1.00 33.03           C  
-ATOM    517  C   ALA A  81      25.221  22.655  38.522  1.00 38.54           C  
-ATOM    518  O   ALA A  81      25.506  21.817  37.654  1.00 38.81           O  
-ATOM    519  CB  ALA A  81      24.058  24.538  37.331  1.00 29.26           C  
-ATOM    520  N   ARG A  82      26.066  22.921  39.540  1.00 37.92           N  
-ATOM    521  CA  ARG A  82      27.404  22.371  39.584  1.00 34.73           C  
-ATOM    522  C   ARG A  82      27.410  20.857  39.694  1.00 33.95           C  
-ATOM    523  O   ARG A  82      26.701  20.343  40.570  1.00 31.47           O  
-ATOM    524  CB  ARG A  82      28.168  22.989  40.772  1.00 28.42           C  
-ATOM    525  CG  ARG A  82      29.506  22.291  41.051  1.00 38.24           C  
-ATOM    526  CD  ARG A  82      30.194  22.966  42.227  1.00 46.44           C  
-ATOM    527  NE  ARG A  82      30.778  24.245  41.829  1.00 46.82           N  
-ATOM    528  CZ  ARG A  82      31.268  25.139  42.688  1.00 54.95           C  
-ATOM    529  NH1 ARG A  82      31.275  24.975  44.007  1.00 54.36           N  
-ATOM    530  NH2 ARG A  82      31.768  26.259  42.192  1.00 47.67           N  
-ATOM    531  N   THR A  83      28.159  20.123  38.863  1.00 34.69           N  
-ATOM    532  CA  THR A  83      28.312  18.689  39.035  1.00 37.57           C  
-ATOM    533  C   THR A  83      29.806  18.342  39.282  1.00 45.30           C  
-ATOM    534  O   THR A  83      30.213  17.209  39.576  1.00 42.47           O  
-ATOM    535  CB  THR A  83      27.935  17.784  37.875  1.00 35.55           C  
-ATOM    536  OG1 THR A  83      28.716  18.204  36.722  1.00 28.23           O  
-ATOM    537  CG2 THR A  83      26.460  17.847  37.617  1.00 35.35           C  
-ATOM    538  N   GLY A  84      30.646  19.313  38.955  1.00 40.44           N  
-ATOM    539  CA  GLY A  84      32.076  19.173  39.120  1.00 41.01           C  
-ATOM    540  C   GLY A  84      32.643  18.599  37.843  1.00 44.60           C  
-ATOM    541  O   GLY A  84      33.843  18.335  37.825  1.00 43.98           O  
-ATOM    542  N   LYS A  85      31.838  18.462  36.771  1.00 44.06           N  
-ATOM    543  CA  LYS A  85      32.404  18.021  35.492  1.00 42.23           C  
-ATOM    544  C   LYS A  85      32.399  19.080  34.402  1.00 40.12           C  
-ATOM    545  O   LYS A  85      31.689  20.082  34.454  1.00 33.64           O  
-ATOM    546  CB  LYS A  85      31.633  16.805  34.970  1.00 53.44           C  
-ATOM    547  CG  LYS A  85      31.280  15.754  35.999  1.00 58.20           C  
-ATOM    548  CD  LYS A  85      32.325  14.699  36.309  1.00 71.37           C  
-ATOM    549  CE  LYS A  85      32.580  14.552  37.805  1.00 78.36           C  
-ATOM    550  NZ  LYS A  85      33.080  13.228  38.263  1.00 80.12           N  
-ATOM    551  N   ILE A  86      33.316  18.905  33.432  1.00 40.34           N  
-ATOM    552  CA  ILE A  86      33.393  19.809  32.284  1.00 40.46           C  
-ATOM    553  C   ILE A  86      32.048  19.886  31.587  1.00 36.04           C  
-ATOM    554  O   ILE A  86      31.245  18.965  31.511  1.00 35.27           O  
-ATOM    555  CB  ILE A  86      34.470  19.248  31.339  1.00 47.66           C  
-ATOM    556  CG1 ILE A  86      34.620  20.059  30.065  1.00 52.29           C  
-ATOM    557  CG2 ILE A  86      34.070  17.818  30.965  1.00 56.51           C  
-ATOM    558  CD1 ILE A  86      35.875  19.683  29.284  1.00 61.09           C  
-ATOM    559  N   GLY A  87      31.582  21.062  31.255  1.00 35.05           N  
-ATOM    560  CA  GLY A  87      30.249  21.193  30.636  1.00 37.01           C  
-ATOM    561  C   GLY A  87      29.253  21.813  31.599  1.00 34.94           C  
-ATOM    562  O   GLY A  87      28.263  22.290  31.049  1.00 33.04           O  
-ATOM    563  N   ASP A  88      29.645  22.111  32.861  1.00 29.94           N  
-ATOM    564  CA  ASP A  88      28.623  22.678  33.745  1.00 26.39           C  
-ATOM    565  C   ASP A  88      28.255  24.092  33.370  1.00 27.67           C  
-ATOM    566  O   ASP A  88      27.158  24.567  33.717  1.00 33.37           O  
-ATOM    567  CB  ASP A  88      29.033  22.661  35.216  1.00 36.91           C  
-ATOM    568  CG  ASP A  88      28.956  21.347  35.968  1.00 35.90           C  
-ATOM    569  OD1 ASP A  88      28.237  20.428  35.608  1.00 30.28           O  
-ATOM    570  OD2 ASP A  88      29.663  21.239  37.006  1.00 42.44           O  
-ATOM    571  N   GLY A  89      29.145  24.819  32.657  1.00 25.82           N  
-ATOM    572  CA  GLY A  89      28.697  26.105  32.182  1.00 24.26           C  
-ATOM    573  C   GLY A  89      29.377  27.270  32.888  1.00 33.11           C  
-ATOM    574  O   GLY A  89      30.312  27.116  33.681  1.00 34.09           O  
-ATOM    575  N   LYS A  90      28.821  28.455  32.588  1.00 28.66           N  
-ATOM    576  CA  LYS A  90      29.426  29.664  33.108  1.00 31.60           C  
-ATOM    577  C   LYS A  90      28.360  30.708  33.411  1.00 33.55           C  
-ATOM    578  O   LYS A  90      27.295  30.647  32.826  1.00 30.42           O  
-ATOM    579  CB  LYS A  90      30.304  30.351  32.086  1.00 35.30           C  
-ATOM    580  CG  LYS A  90      31.760  29.870  32.183  1.00 58.32           C  
-ATOM    581  CD  LYS A  90      32.533  30.465  31.011  1.00 61.16           C  
-ATOM    582  CE  LYS A  90      33.801  29.652  30.760  1.00 64.83           C  
-ATOM    583  NZ  LYS A  90      34.314  29.965  29.391  1.00 77.46           N  
-ATOM    584  N   ILE A  91      28.676  31.628  34.286  1.00 26.54           N  
-ATOM    585  CA  ILE A  91      27.773  32.699  34.612  1.00 25.34           C  
-ATOM    586  C   ILE A  91      28.473  34.029  34.294  1.00 33.64           C  
-ATOM    587  O   ILE A  91      29.687  34.169  34.527  1.00 31.21           O  
-ATOM    588  CB  ILE A  91      27.420  32.669  36.128  1.00 31.80           C  
-ATOM    589  CG1 ILE A  91      26.819  31.310  36.532  1.00 34.34           C  
-ATOM    590  CG2 ILE A  91      26.470  33.812  36.475  1.00 30.19           C  
-ATOM    591  CD1 ILE A  91      26.997  30.972  37.998  1.00 36.86           C  
-ATOM    592  N   PHE A  92      27.734  35.001  33.768  1.00 37.00           N  
-ATOM    593  CA  PHE A  92      28.341  36.324  33.571  1.00 38.31           C  
-ATOM    594  C   PHE A  92      27.462  37.400  34.187  1.00 34.08           C  
-ATOM    595  O   PHE A  92      26.260  37.204  34.272  1.00 38.47           O  
-ATOM    596  CB  PHE A  92      28.501  36.737  32.133  1.00 42.38           C  
-ATOM    597  CG  PHE A  92      28.872  35.669  31.173  1.00 51.28           C  
-ATOM    598  CD1 PHE A  92      30.138  35.106  31.153  1.00 59.83           C  
-ATOM    599  CD2 PHE A  92      27.930  35.237  30.249  1.00 55.38           C  
-ATOM    600  CE1 PHE A  92      30.446  34.127  30.224  1.00 57.97           C  
-ATOM    601  CE2 PHE A  92      28.237  34.274  29.326  1.00 64.07           C  
-ATOM    602  CZ  PHE A  92      29.499  33.705  29.313  1.00 62.50           C  
-ATOM    603  N   VAL A  93      28.021  38.526  34.611  1.00 33.09           N  
-ATOM    604  CA  VAL A  93      27.166  39.553  35.149  1.00 32.76           C  
-ATOM    605  C   VAL A  93      27.570  40.909  34.559  1.00 31.29           C  
-ATOM    606  O   VAL A  93      28.714  41.322  34.643  1.00 33.45           O  
-ATOM    607  CB  VAL A  93      27.162  39.542  36.689  1.00 38.51           C  
-ATOM    608  CG1 VAL A  93      28.316  38.714  37.229  1.00 36.69           C  
-ATOM    609  CG2 VAL A  93      27.219  40.961  37.218  1.00 33.74           C  
-ATOM    610  N   GLN A  94      26.556  41.570  33.959  1.00 33.12           N  
-ATOM    611  CA  GLN A  94      26.722  42.867  33.304  1.00 32.98           C  
-ATOM    612  C   GLN A  94      25.870  43.944  33.918  1.00 35.22           C  
-ATOM    613  O   GLN A  94      24.867  43.685  34.584  1.00 32.58           O  
-ATOM    614  CB  GLN A  94      26.314  42.782  31.828  1.00 38.97           C  
-ATOM    615  CG  GLN A  94      27.156  41.861  30.962  1.00 47.68           C  
-ATOM    616  CD  GLN A  94      26.565  41.578  29.580  1.00 48.81           C  
-ATOM    617  OE1 GLN A  94      25.654  40.768  29.440  1.00 53.26           O  
-ATOM    618  NE2 GLN A  94      26.927  42.141  28.434  1.00 43.62           N  
-ATOM    619  N   GLU A  95      26.277  45.173  33.672  1.00 38.71           N  
-ATOM    620  CA  GLU A  95      25.531  46.296  34.145  1.00 34.09           C  
-ATOM    621  C   GLU A  95      24.342  46.595  33.241  1.00 34.60           C  
-ATOM    622  O   GLU A  95      24.468  46.505  32.012  1.00 37.77           O  
-ATOM    623  CB  GLU A  95      26.475  47.498  34.228  1.00 38.22           C  
-ATOM    624  CG  GLU A  95      25.804  48.843  34.493  1.00 50.16           C  
-ATOM    625  CD  GLU A  95      25.370  49.008  35.923  1.00 56.36           C  
-ATOM    626  OE1 GLU A  95      24.407  49.762  36.189  1.00 58.89           O  
-ATOM    627  OE2 GLU A  95      26.003  48.378  36.808  1.00 53.01           O  
-ATOM    628  N   VAL A  96      23.220  46.959  33.811  1.00 29.47           N  
-ATOM    629  CA  VAL A  96      22.106  47.482  33.073  1.00 33.18           C  
-ATOM    630  C   VAL A  96      21.874  48.938  33.477  1.00 38.83           C  
-ATOM    631  O   VAL A  96      21.375  49.083  34.599  1.00 40.22           O  
-ATOM    632  CB  VAL A  96      20.862  46.642  33.449  1.00 32.90           C  
-ATOM    633  CG1 VAL A  96      19.590  47.230  32.891  1.00 33.94           C  
-ATOM    634  CG2 VAL A  96      21.098  45.211  32.956  1.00 43.20           C  
-ATOM    635  N   GLU A  97      21.855  49.856  32.535  1.00 35.57           N  
-ATOM    636  CA  GLU A  97      21.496  51.225  32.856  1.00 44.29           C  
-ATOM    637  C   GLU A  97      20.036  51.461  33.163  1.00 40.78           C  
-ATOM    638  O   GLU A  97      19.842  52.273  34.069  1.00 42.88           O  
-ATOM    639  CB  GLU A  97      21.814  52.224  31.750  1.00 39.48           C  
-ATOM    640  CG  GLU A  97      23.220  52.261  31.241  1.00 56.99           C  
-ATOM    641  CD  GLU A  97      23.302  53.228  30.057  1.00 63.20           C  
-ATOM    642  OE1 GLU A  97      24.401  53.288  29.478  1.00 70.09           O  
-ATOM    643  OE2 GLU A  97      22.337  53.939  29.690  1.00 67.88           O  
-ATOM    644  N   GLN A  98      19.059  50.895  32.461  1.00 40.06           N  
-ATOM    645  CA  GLN A  98      17.669  51.151  32.877  1.00 40.21           C  
-ATOM    646  C   GLN A  98      16.724  50.004  32.660  1.00 39.06           C  
-ATOM    647  O   GLN A  98      16.978  49.177  31.795  1.00 33.58           O  
-ATOM    648  CB  GLN A  98      17.125  52.411  32.146  1.00 46.03           C  
-ATOM    649  CG  GLN A  98      15.762  52.802  32.703  1.00 59.10           C  
-ATOM    650  CD  GLN A  98      15.771  53.152  34.187  1.00 60.68           C  
-ATOM    651  OE1 GLN A  98      15.851  52.322  35.105  1.00 56.65           O  
-ATOM    652  NE2 GLN A  98      15.674  54.453  34.436  1.00 66.21           N  
-ATOM    653  N   VAL A  99      15.648  49.817  33.380  1.00 39.15           N  
-ATOM    654  CA  VAL A  99      14.702  48.720  33.282  1.00 41.30           C  
-ATOM    655  C   VAL A  99      13.330  49.413  33.374  1.00 43.47           C  
-ATOM    656  O   VAL A  99      13.192  50.392  34.120  1.00 39.36           O  
-ATOM    657  CB  VAL A  99      14.731  47.662  34.404  1.00 49.29           C  
-ATOM    658  CG1 VAL A  99      13.948  46.382  34.070  1.00 36.11           C  
-ATOM    659  CG2 VAL A  99      16.170  47.311  34.723  1.00 42.53           C  
-ATOM    660  N   ILE A 100      12.440  49.071  32.463  1.00 36.72           N  
-ATOM    661  CA  ILE A 100      11.150  49.650  32.284  1.00 37.52           C  
-ATOM    662  C   ILE A 100      10.220  48.457  32.225  1.00 38.83           C  
-ATOM    663  O   ILE A 100      10.451  47.473  31.488  1.00 39.33           O  
-ATOM    664  CB  ILE A 100      11.086  50.638  31.093  1.00 40.25           C  
-ATOM    665  CG1 ILE A 100      12.039  51.801  31.034  1.00 44.65           C  
-ATOM    666  CG2 ILE A 100       9.691  51.329  31.000  1.00 40.44           C  
-ATOM    667  CD1 ILE A 100      13.328  51.770  30.277  1.00 34.82           C  
-ATOM    668  N   ARG A 101       9.121  48.459  32.956  1.00 34.35           N  
-ATOM    669  CA  ARG A 101       8.080  47.465  32.981  1.00 39.68           C  
-ATOM    670  C   ARG A 101       6.933  47.943  32.089  1.00 43.09           C  
-ATOM    671  O   ARG A 101       6.383  49.057  32.113  1.00 41.05           O  
-ATOM    672  CB  ARG A 101       7.707  47.136  34.434  1.00 46.24           C  
-ATOM    673  CG  ARG A 101       6.360  46.509  34.738  1.00 59.53           C  
-ATOM    674  CD  ARG A 101       6.185  46.268  36.251  1.00 63.53           C  
-ATOM    675  NE  ARG A 101       6.554  44.949  36.743  1.00 58.24           N  
-ATOM    676  CZ  ARG A 101       7.383  44.657  37.743  1.00 68.52           C  
-ATOM    677  NH1 ARG A 101       7.999  45.603  38.447  1.00 71.35           N  
-ATOM    678  NH2 ARG A 101       7.637  43.397  38.076  1.00 71.83           N  
-ATOM    679  N   ILE A 102       6.749  47.161  31.008  1.00 42.99           N  
-ATOM    680  CA  ILE A 102       5.862  47.642  29.920  1.00 40.63           C  
-ATOM    681  C   ILE A 102       4.454  47.968  30.396  1.00 38.42           C  
-ATOM    682  O   ILE A 102       3.908  49.040  30.149  1.00 37.96           O  
-ATOM    683  CB  ILE A 102       5.931  46.702  28.715  1.00 28.55           C  
-ATOM    684  CG1 ILE A 102       7.332  46.874  28.040  1.00 28.70           C  
-ATOM    685  CG2 ILE A 102       4.854  47.088  27.693  1.00 29.03           C  
-ATOM    686  CD1 ILE A 102       7.537  45.814  26.954  1.00 33.36           C  
-ATOM    687  N   ARG A 103       3.795  47.059  31.071  1.00 36.47           N  
-ATOM    688  CA  ARG A 103       2.459  47.245  31.567  1.00 41.57           C  
-ATOM    689  C   ARG A 103       2.232  48.529  32.351  1.00 48.88           C  
-ATOM    690  O   ARG A 103       1.259  49.204  32.044  1.00 47.57           O  
-ATOM    691  CB  ARG A 103       2.073  46.036  32.408  1.00 43.58           C  
-ATOM    692  CG  ARG A 103       0.653  46.156  32.939  1.00 52.05           C  
-ATOM    693  CD  ARG A 103       0.218  44.951  33.778  1.00 56.71           C  
-ATOM    694  NE  ARG A 103      -0.989  45.435  34.484  1.00 72.03           N  
-ATOM    695  CZ  ARG A 103      -0.814  46.001  35.684  1.00 71.36           C  
-ATOM    696  NH1 ARG A 103       0.419  46.066  36.185  1.00 82.73           N  
-ATOM    697  NH2 ARG A 103      -1.861  46.460  36.336  1.00 70.41           N  
-ATOM    698  N   THR A 104       3.107  49.003  33.216  1.00 53.19           N  
-ATOM    699  CA  THR A 104       2.783  50.171  34.027  1.00 56.39           C  
-ATOM    700  C   THR A 104       3.604  51.391  33.688  1.00 62.07           C  
-ATOM    701  O   THR A 104       3.132  52.529  33.583  1.00 62.91           O  
-ATOM    702  CB  THR A 104       2.996  49.777  35.499  1.00 58.99           C  
-ATOM    703  OG1 THR A 104       4.249  49.108  35.651  1.00 55.76           O  
-ATOM    704  CG2 THR A 104       1.914  48.807  35.936  1.00 52.91           C  
-ATOM    705  N   GLY A 105       4.885  51.168  33.407  1.00 61.17           N  
-ATOM    706  CA  GLY A 105       5.823  52.267  33.154  1.00 57.36           C  
-ATOM    707  C   GLY A 105       6.750  52.402  34.380  1.00 55.13           C  
-ATOM    708  O   GLY A 105       7.560  53.325  34.390  1.00 55.16           O  
-ATOM    709  N   GLU A 106       6.673  51.482  35.340  1.00 54.77           N  
-ATOM    710  CA  GLU A 106       7.636  51.571  36.447  1.00 58.34           C  
-ATOM    711  C   GLU A 106       9.063  51.346  35.928  1.00 61.58           C  
-ATOM    712  O   GLU A 106       9.395  50.522  35.059  1.00 54.84           O  
-ATOM    713  CB  GLU A 106       7.357  50.589  37.554  1.00 67.48           C  
-ATOM    714  CG  GLU A 106       5.995  50.666  38.252  1.00 72.49           C  
-ATOM    715  CD  GLU A 106       5.869  49.358  39.030  1.00 79.02           C  
-ATOM    716  OE1 GLU A 106       5.092  48.489  38.590  1.00 80.65           O  
-ATOM    717  OE2 GLU A 106       6.574  49.208  40.052  1.00 84.67           O  
-ATOM    718  N   THR A 107       9.955  52.209  36.395  1.00 61.77           N  
-ATOM    719  CA  THR A 107      11.353  52.171  35.981  1.00 62.28           C  
-ATOM    720  C   THR A 107      12.168  51.798  37.225  1.00 68.89           C  
-ATOM    721  O   THR A 107      11.625  51.710  38.342  1.00 67.75           O  
-ATOM    722  CB  THR A 107      11.803  53.493  35.398  1.00 58.69           C  
-ATOM    723  OG1 THR A 107      11.633  54.487  36.421  1.00 71.20           O  
-ATOM    724  CG2 THR A 107      11.026  53.978  34.184  1.00 65.07           C  
-ATOM    725  N   GLY A 108      13.436  51.474  36.994  1.00 71.64           N  
-ATOM    726  CA  GLY A 108      14.353  51.093  38.037  1.00 74.99           C  
-ATOM    727  C   GLY A 108      13.985  49.911  38.901  1.00 79.15           C  
-ATOM    728  O   GLY A 108      13.480  48.862  38.495  1.00 75.26           O  
-ATOM    729  N   PRO A 109      14.237  50.065  40.212  1.00 84.35           N  
-ATOM    730  CA  PRO A 109      14.070  49.000  41.194  1.00 86.95           C  
-ATOM    731  C   PRO A 109      12.624  48.652  41.475  1.00 88.73           C  
-ATOM    732  O   PRO A 109      12.262  47.544  41.871  1.00 88.66           O  
-ATOM    733  CB  PRO A 109      14.870  49.468  42.393  1.00 88.83           C  
-ATOM    734  CG  PRO A 109      15.676  50.642  41.941  1.00 87.98           C  
-ATOM    735  CD  PRO A 109      14.857  51.267  40.844  1.00 85.83           C  
-ATOM    736  N   ASP A 110      11.706  49.530  41.084  1.00 90.60           N  
-ATOM    737  CA  ASP A 110      10.275  49.281  41.076  1.00 90.31           C  
-ATOM    738  C   ASP A 110       9.949  48.335  39.903  1.00 86.91           C  
-ATOM    739  O   ASP A 110       8.989  47.567  39.961  1.00 85.97           O  
-ATOM    740  CB  ASP A 110       9.500  50.586  40.957  1.00101.17           C  
-ATOM    741  CG  ASP A 110      10.024  51.829  41.637  1.00107.26           C  
-ATOM    742  OD1 ASP A 110       9.403  52.920  41.512  1.00108.76           O  
-ATOM    743  OD2 ASP A 110      11.071  51.790  42.318  1.00108.94           O  
-ATOM    744  N   ALA A 111      10.780  48.340  38.854  1.00 81.18           N  
-ATOM    745  CA  ALA A 111      10.596  47.557  37.654  1.00 76.92           C  
-ATOM    746  C   ALA A 111      11.196  46.164  37.744  1.00 77.71           C  
-ATOM    747  O   ALA A 111      10.842  45.327  36.911  1.00 76.44           O  
-ATOM    748  CB  ALA A 111      11.180  48.227  36.404  1.00 51.53           C  
-ATOM    749  N   VAL A 112      12.006  45.895  38.759  1.00 81.04           N  
-ATOM    750  CA  VAL A 112      12.584  44.551  38.854  1.00 85.47           C  
-ATOM    751  C   VAL A 112      11.695  43.601  39.630  1.00 86.99           C  
-ATOM    752  O   VAL A 112      11.735  42.375  39.388  1.00 88.00           O  
-ATOM    753  CB  VAL A 112      13.992  44.639  39.461  1.00 93.15           C  
-ATOM    754  CG1 VAL A 112      14.640  43.273  39.597  1.00 92.24           C  
-ATOM    755  CG2 VAL A 112      14.854  45.582  38.614  1.00 97.01           C  
-TER     756      VAL A 112                                                      
-ATOM    757  N   MET B   1      26.337  54.980  22.299  1.00 51.96           N  
-ATOM    758  CA  MET B   1      25.632  53.857  21.626  1.00 46.48           C  
-ATOM    759  C   MET B   1      24.992  52.978  22.700  1.00 41.80           C  
-ATOM    760  O   MET B   1      25.644  52.664  23.693  1.00 36.03           O  
-ATOM    761  CB  MET B   1      26.611  52.932  20.905  1.00 54.21           C  
-ATOM    762  CG  MET B   1      25.986  52.594  19.542  1.00 73.49           C  
-ATOM    763  SD  MET B   1      26.527  53.856  18.343  1.00 78.14           S  
-ATOM    764  CE  MET B   1      28.298  53.665  18.666  1.00 76.91           C  
-ATOM    765  N   LYS B   2      23.714  52.701  22.528  1.00 41.35           N  
-ATOM    766  CA  LYS B   2      22.998  51.894  23.494  1.00 43.89           C  
-ATOM    767  C   LYS B   2      22.335  50.675  22.831  1.00 42.85           C  
-ATOM    768  O   LYS B   2      21.886  50.815  21.702  1.00 38.26           O  
-ATOM    769  CB  LYS B   2      21.890  52.714  24.147  1.00 41.93           C  
-ATOM    770  CG  LYS B   2      22.405  54.019  24.752  1.00 45.28           C  
-ATOM    771  CD  LYS B   2      22.808  53.824  26.211  1.00 45.44           C  
-ATOM    772  CE  LYS B   2      23.322  55.212  26.689  1.00 49.62           C  
-ATOM    773  NZ  LYS B   2      24.558  55.008  27.478  1.00 46.17           N  
-ATOM    774  N   GLN B   3      22.314  49.578  23.568  1.00 33.80           N  
-ATOM    775  CA  GLN B   3      21.544  48.406  23.158  1.00 37.19           C  
-ATOM    776  C   GLN B   3      20.196  48.435  23.886  1.00 33.99           C  
-ATOM    777  O   GLN B   3      20.244  48.331  25.110  1.00 34.11           O  
-ATOM    778  CB  GLN B   3      22.163  47.053  23.506  1.00 33.90           C  
-ATOM    779  CG  GLN B   3      21.149  45.881  23.241  1.00 31.62           C  
-ATOM    780  CD  GLN B   3      21.992  44.614  23.182  1.00 48.47           C  
-ATOM    781  OE1 GLN B   3      22.175  44.095  22.096  1.00 61.92           O  
-ATOM    782  NE2 GLN B   3      22.519  44.203  24.321  1.00 48.01           N  
-ATOM    783  N   VAL B   4      19.117  48.487  23.129  1.00 32.98           N  
-ATOM    784  CA  VAL B   4      17.805  48.463  23.769  1.00 32.43           C  
-ATOM    785  C   VAL B   4      17.311  47.035  23.612  1.00 31.75           C  
-ATOM    786  O   VAL B   4      17.205  46.616  22.454  1.00 34.62           O  
-ATOM    787  CB  VAL B   4      16.802  49.472  23.142  1.00 34.54           C  
-ATOM    788  CG1 VAL B   4      15.362  49.268  23.578  1.00 34.86           C  
-ATOM    789  CG2 VAL B   4      17.207  50.890  23.509  1.00 37.31           C  
-ATOM    790  N   THR B   5      16.796  46.415  24.651  1.00 31.40           N  
-ATOM    791  CA  THR B   5      16.238  45.081  24.578  1.00 29.13           C  
-ATOM    792  C   THR B   5      14.813  44.988  25.095  1.00 32.28           C  
-ATOM    793  O   THR B   5      14.615  45.536  26.186  1.00 28.09           O  
-ATOM    794  CB  THR B   5      17.068  44.105  25.470  1.00 36.54           C  
-ATOM    795  OG1 THR B   5      18.331  44.010  24.865  1.00 31.15           O  
-ATOM    796  CG2 THR B   5      16.590  42.624  25.398  1.00 33.81           C  
-ATOM    797  N   ALA B   6      13.890  44.346  24.342  1.00 26.87           N  
-ATOM    798  CA  ALA B   6      12.539  44.287  24.916  1.00 25.76           C  
-ATOM    799  C   ALA B   6      12.134  42.814  24.840  1.00 31.41           C  
-ATOM    800  O   ALA B   6      12.479  42.147  23.803  1.00 27.53           O  
-ATOM    801  CB  ALA B   6      11.556  45.170  24.140  1.00 25.75           C  
-ATOM    802  N   ILE B   7      11.374  42.409  25.850  1.00 23.91           N  
-ATOM    803  CA  ILE B   7      10.876  41.000  25.788  1.00 27.67           C  
-ATOM    804  C   ILE B   7       9.372  41.168  25.780  1.00 30.85           C  
-ATOM    805  O   ILE B   7       8.819  41.827  26.694  1.00 30.07           O  
-ATOM    806  CB  ILE B   7      11.207  40.179  27.037  1.00 29.58           C  
-ATOM    807  CG1 ILE B   7      12.676  40.288  27.384  1.00 41.51           C  
-ATOM    808  CG2 ILE B   7      10.643  38.759  27.032  1.00 30.71           C  
-ATOM    809  CD1 ILE B   7      13.707  39.585  26.618  1.00 32.97           C  
-ATOM    810  N   ILE B   8       8.707  40.708  24.709  1.00 26.60           N  
-ATOM    811  CA  ILE B   8       7.338  41.123  24.497  1.00 26.62           C  
-ATOM    812  C   ILE B   8       6.527  39.883  24.117  1.00 26.44           C  
-ATOM    813  O   ILE B   8       7.072  38.857  23.782  1.00 25.97           O  
-ATOM    814  CB  ILE B   8       7.216  42.114  23.297  1.00 30.57           C  
-ATOM    815  CG1 ILE B   8       7.673  41.433  22.002  1.00 26.67           C  
-ATOM    816  CG2 ILE B   8       7.960  43.431  23.540  1.00 26.00           C  
-ATOM    817  CD1 ILE B   8       7.343  42.354  20.763  1.00 32.73           C  
-ATOM    818  N   LYS B   9       5.225  40.074  24.133  1.00 23.48           N  
-ATOM    819  CA  LYS B   9       4.389  38.922  23.694  1.00 27.42           C  
-ATOM    820  C   LYS B   9       4.543  38.776  22.160  1.00 26.36           C  
-ATOM    821  O   LYS B   9       4.744  39.747  21.412  1.00 26.78           O  
-ATOM    822  CB  LYS B   9       2.960  39.157  24.137  1.00 30.55           C  
-ATOM    823  CG  LYS B   9       2.740  39.019  25.656  1.00 36.85           C  
-ATOM    824  CD  LYS B   9       1.332  39.438  26.000  1.00 44.73           C  
-ATOM    825  CE  LYS B   9       1.031  39.231  27.480  1.00 40.03           C  
-ATOM    826  NZ  LYS B   9      -0.048  40.140  27.924  1.00 45.73           N  
-ATOM    827  N   PRO B  10       4.580  37.554  21.680  1.00 30.27           N  
-ATOM    828  CA  PRO B  10       4.912  37.244  20.271  1.00 31.07           C  
-ATOM    829  C   PRO B  10       3.975  37.854  19.227  1.00 28.83           C  
-ATOM    830  O   PRO B  10       4.515  38.427  18.276  1.00 27.06           O  
-ATOM    831  CB  PRO B  10       4.871  35.698  20.198  1.00 31.25           C  
-ATOM    832  CG  PRO B  10       5.200  35.297  21.608  1.00 33.84           C  
-ATOM    833  CD  PRO B  10       4.326  36.303  22.443  1.00 25.35           C  
-ATOM    834  N   PHE B  11       2.704  38.082  19.553  1.00 26.24           N  
-ATOM    835  CA  PHE B  11       1.778  38.665  18.580  1.00 31.82           C  
-ATOM    836  C   PHE B  11       1.904  40.170  18.533  1.00 31.77           C  
-ATOM    837  O   PHE B  11       1.087  40.803  17.867  1.00 33.80           O  
-ATOM    838  CB  PHE B  11       0.347  38.195  18.845  1.00 29.58           C  
-ATOM    839  CG  PHE B  11      -0.120  38.526  20.262  1.00 29.62           C  
-ATOM    840  CD1 PHE B  11      -0.421  39.827  20.599  1.00 29.94           C  
-ATOM    841  CD2 PHE B  11      -0.196  37.520  21.233  1.00 35.09           C  
-ATOM    842  CE1 PHE B  11      -0.866  40.145  21.890  1.00 39.02           C  
-ATOM    843  CE2 PHE B  11      -0.622  37.843  22.516  1.00 41.30           C  
-ATOM    844  CZ  PHE B  11      -0.964  39.151  22.846  1.00 32.33           C  
-ATOM    845  N   LYS B  12       2.832  40.777  19.326  1.00 24.18           N  
-ATOM    846  CA  LYS B  12       2.962  42.216  19.237  1.00 21.37           C  
-ATOM    847  C   LYS B  12       4.148  42.617  18.354  1.00 26.42           C  
-ATOM    848  O   LYS B  12       4.349  43.834  18.111  1.00 27.67           O  
-ATOM    849  CB  LYS B  12       3.197  42.884  20.636  1.00 21.11           C  
-ATOM    850  CG  LYS B  12       1.863  42.744  21.449  1.00 21.36           C  
-ATOM    851  CD  LYS B  12       1.152  44.049  21.031  1.00 35.92           C  
-ATOM    852  CE  LYS B  12      -0.049  44.503  21.788  1.00 32.59           C  
-ATOM    853  NZ  LYS B  12      -0.650  45.792  21.215  1.00 30.70           N  
-ATOM    854  N   LEU B  13       4.924  41.678  17.834  1.00 24.37           N  
-ATOM    855  CA  LEU B  13       6.083  42.015  17.028  1.00 24.03           C  
-ATOM    856  C   LEU B  13       5.816  42.882  15.789  1.00 27.02           C  
-ATOM    857  O   LEU B  13       6.603  43.802  15.515  1.00 28.69           O  
-ATOM    858  CB  LEU B  13       6.818  40.712  16.626  1.00 27.02           C  
-ATOM    859  CG  LEU B  13       8.015  40.882  15.671  1.00 32.83           C  
-ATOM    860  CD1 LEU B  13       9.087  41.758  16.295  1.00 29.85           C  
-ATOM    861  CD2 LEU B  13       8.612  39.541  15.291  1.00 33.09           C  
-ATOM    862  N   ASP B  14       4.779  42.646  15.016  1.00 27.53           N  
-ATOM    863  CA  ASP B  14       4.601  43.488  13.833  1.00 31.62           C  
-ATOM    864  C   ASP B  14       4.309  44.900  14.266  1.00 27.50           C  
-ATOM    865  O   ASP B  14       4.845  45.856  13.712  1.00 26.48           O  
-ATOM    866  CB  ASP B  14       3.487  43.000  12.967  1.00 29.83           C  
-ATOM    867  CG  ASP B  14       3.888  41.727  12.287  1.00 38.68           C  
-ATOM    868  OD1 ASP B  14       5.073  41.553  11.976  1.00 43.03           O  
-ATOM    869  OD2 ASP B  14       2.993  40.880  12.053  1.00 39.45           O  
-ATOM    870  N   GLU B  15       3.456  45.004  15.298  1.00 23.42           N  
-ATOM    871  CA  GLU B  15       3.044  46.288  15.761  1.00 22.48           C  
-ATOM    872  C   GLU B  15       4.202  47.041  16.345  1.00 23.59           C  
-ATOM    873  O   GLU B  15       4.334  48.248  16.174  1.00 29.11           O  
-ATOM    874  CB  GLU B  15       1.921  46.206  16.798  1.00 26.40           C  
-ATOM    875  CG  GLU B  15       1.464  47.549  17.342  1.00 26.78           C  
-ATOM    876  CD  GLU B  15       0.134  47.462  18.074  1.00 30.18           C  
-ATOM    877  OE1 GLU B  15      -0.320  46.333  18.353  1.00 25.77           O  
-ATOM    878  OE2 GLU B  15      -0.447  48.513  18.368  1.00 34.40           O  
-ATOM    879  N   VAL B  16       5.091  46.307  17.059  1.00 24.04           N  
-ATOM    880  CA  VAL B  16       6.263  47.024  17.631  1.00 27.23           C  
-ATOM    881  C   VAL B  16       7.157  47.513  16.497  1.00 30.93           C  
-ATOM    882  O   VAL B  16       7.855  48.522  16.412  1.00 27.20           O  
-ATOM    883  CB  VAL B  16       7.083  46.126  18.632  1.00 28.80           C  
-ATOM    884  CG1 VAL B  16       8.450  46.702  18.898  1.00 32.70           C  
-ATOM    885  CG2 VAL B  16       6.203  46.049  19.915  1.00 27.40           C  
-ATOM    886  N   ARG B  17       7.323  46.617  15.556  1.00 30.82           N  
-ATOM    887  CA  ARG B  17       8.252  46.949  14.457  1.00 34.88           C  
-ATOM    888  C   ARG B  17       7.715  48.147  13.659  1.00 36.89           C  
-ATOM    889  O   ARG B  17       8.490  48.994  13.230  1.00 34.83           O  
-ATOM    890  CB  ARG B  17       8.223  45.683  13.638  1.00 46.68           C  
-ATOM    891  CG  ARG B  17       9.328  45.642  12.628  1.00 55.08           C  
-ATOM    892  CD  ARG B  17       9.078  44.280  11.935  1.00 61.03           C  
-ATOM    893  NE  ARG B  17       9.550  44.491  10.572  1.00 58.98           N  
-ATOM    894  CZ  ARG B  17       9.182  43.710   9.563  1.00 69.74           C  
-ATOM    895  NH1 ARG B  17       8.358  42.677   9.694  1.00 63.00           N  
-ATOM    896  NH2 ARG B  17       9.715  44.036   8.379  1.00 68.45           N  
-ATOM    897  N   GLU B  18       6.420  48.226  13.412  1.00 33.89           N  
-ATOM    898  CA  GLU B  18       5.803  49.396  12.788  1.00 37.48           C  
-ATOM    899  C   GLU B  18       6.007  50.678  13.574  1.00 40.54           C  
-ATOM    900  O   GLU B  18       6.447  51.742  13.067  1.00 37.53           O  
-ATOM    901  CB  GLU B  18       4.332  49.036  12.608  1.00 36.80           C  
-ATOM    902  CG  GLU B  18       3.742  49.280  11.235  1.00 55.46           C  
-ATOM    903  CD  GLU B  18       3.410  50.753  11.091  1.00 70.10           C  
-ATOM    904  OE1 GLU B  18       3.327  51.408  12.157  1.00 73.66           O  
-ATOM    905  OE2 GLU B  18       3.257  51.217   9.938  1.00 82.79           O  
-ATOM    906  N   SER B  19       5.833  50.655  14.900  1.00 34.10           N  
-ATOM    907  CA  SER B  19       6.062  51.819  15.768  1.00 37.28           C  
-ATOM    908  C   SER B  19       7.499  52.321  15.710  1.00 41.77           C  
-ATOM    909  O   SER B  19       7.840  53.520  15.720  1.00 37.55           O  
-ATOM    910  CB  SER B  19       5.563  51.357  17.123  1.00 38.08           C  
-ATOM    911  OG  SER B  19       5.370  52.366  18.066  1.00 43.12           O  
-ATOM    912  N   LEU B  20       8.473  51.391  15.632  1.00 36.99           N  
-ATOM    913  CA  LEU B  20       9.901  51.694  15.649  1.00 38.41           C  
-ATOM    914  C   LEU B  20      10.320  52.372  14.334  1.00 39.03           C  
-ATOM    915  O   LEU B  20      11.105  53.311  14.351  1.00 34.66           O  
-ATOM    916  CB  LEU B  20      10.694  50.400  15.937  1.00 35.57           C  
-ATOM    917  CG  LEU B  20      11.526  50.128  17.170  1.00 46.31           C  
-ATOM    918  CD1 LEU B  20      11.420  51.107  18.313  1.00 38.01           C  
-ATOM    919  CD2 LEU B  20      11.438  48.692  17.704  1.00 39.29           C  
-ATOM    920  N   ALA B  21       9.817  51.901  13.192  1.00 35.84           N  
-ATOM    921  CA  ALA B  21      10.028  52.487  11.883  1.00 42.84           C  
-ATOM    922  C   ALA B  21       9.593  53.960  11.848  1.00 48.07           C  
-ATOM    923  O   ALA B  21      10.385  54.867  11.557  1.00 45.66           O  
-ATOM    924  CB  ALA B  21       9.276  51.627  10.861  1.00 36.72           C  
-ATOM    925  N   GLU B  22       8.465  54.313  12.472  1.00 47.64           N  
-ATOM    926  CA  GLU B  22       7.994  55.684  12.570  1.00 52.11           C  
-ATOM    927  C   GLU B  22       8.962  56.614  13.275  1.00 54.66           C  
-ATOM    928  O   GLU B  22       8.941  57.815  12.961  1.00 56.58           O  
-ATOM    929  CB  GLU B  22       6.638  55.736  13.284  1.00 52.86           C  
-ATOM    930  CG  GLU B  22       5.570  55.078  12.422  1.00 68.80           C  
-ATOM    931  CD  GLU B  22       4.196  55.056  13.077  1.00 75.15           C  
-ATOM    932  OE1 GLU B  22       3.373  54.316  12.479  1.00 79.55           O  
-ATOM    933  OE2 GLU B  22       3.977  55.731  14.107  1.00 66.26           O  
-ATOM    934  N   VAL B  23       9.810  56.134  14.190  1.00 49.36           N  
-ATOM    935  CA  VAL B  23      10.836  56.950  14.787  1.00 45.61           C  
-ATOM    936  C   VAL B  23      12.198  56.669  14.179  1.00 45.26           C  
-ATOM    937  O   VAL B  23      13.271  56.976  14.734  1.00 46.08           O  
-ATOM    938  CB  VAL B  23      10.884  56.912  16.325  1.00 48.47           C  
-ATOM    939  CG1 VAL B  23       9.502  57.236  16.896  1.00 49.38           C  
-ATOM    940  CG2 VAL B  23      11.421  55.640  16.930  1.00 43.86           C  
-ATOM    941  N   GLY B  24      12.215  56.006  13.014  1.00 44.66           N  
-ATOM    942  CA  GLY B  24      13.479  55.798  12.329  1.00 49.70           C  
-ATOM    943  C   GLY B  24      14.347  54.617  12.709  1.00 52.95           C  
-ATOM    944  O   GLY B  24      15.420  54.477  12.094  1.00 49.99           O  
-ATOM    945  N   VAL B  25      13.909  53.724  13.593  1.00 47.51           N  
-ATOM    946  CA  VAL B  25      14.700  52.535  13.968  1.00 43.18           C  
-ATOM    947  C   VAL B  25      14.226  51.331  13.189  1.00 45.04           C  
-ATOM    948  O   VAL B  25      13.013  50.950  13.174  1.00 39.44           O  
-ATOM    949  CB  VAL B  25      14.532  52.423  15.497  1.00 43.25           C  
-ATOM    950  CG1 VAL B  25      15.163  51.190  16.091  1.00 48.44           C  
-ATOM    951  CG2 VAL B  25      15.114  53.667  16.172  1.00 53.28           C  
-ATOM    952  N   THR B  26      15.071  50.756  12.329  1.00 47.68           N  
-ATOM    953  CA  THR B  26      14.681  49.624  11.484  1.00 52.12           C  
-ATOM    954  C   THR B  26      15.501  48.336  11.550  1.00 49.59           C  
-ATOM    955  O   THR B  26      15.069  47.319  10.947  1.00 51.08           O  
-ATOM    956  CB  THR B  26      14.716  50.048   9.989  1.00 56.87           C  
-ATOM    957  OG1 THR B  26      16.034  50.500   9.650  1.00 44.65           O  
-ATOM    958  CG2 THR B  26      13.687  51.113   9.671  1.00 62.82           C  
-ATOM    959  N   GLY B  27      16.747  48.339  11.980  1.00 45.44           N  
-ATOM    960  CA  GLY B  27      17.482  47.036  11.903  1.00 43.74           C  
-ATOM    961  C   GLY B  27      17.219  46.275  13.220  1.00 45.36           C  
-ATOM    962  O   GLY B  27      18.016  46.366  14.166  1.00 49.78           O  
-ATOM    963  N   LEU B  28      16.141  45.506  13.309  1.00 38.68           N  
-ATOM    964  CA  LEU B  28      15.912  44.726  14.521  1.00 35.87           C  
-ATOM    965  C   LEU B  28      16.529  43.336  14.425  1.00 37.15           C  
-ATOM    966  O   LEU B  28      16.440  42.711  13.341  1.00 34.51           O  
-ATOM    967  CB  LEU B  28      14.404  44.557  14.791  1.00 35.41           C  
-ATOM    968  CG  LEU B  28      13.625  45.778  15.247  1.00 45.31           C  
-ATOM    969  CD1 LEU B  28      14.126  47.141  14.805  1.00 55.90           C  
-ATOM    970  CD2 LEU B  28      12.184  45.682  14.721  1.00 56.19           C  
-ATOM    971  N   THR B  29      16.969  42.855  15.608  1.00 29.04           N  
-ATOM    972  CA  THR B  29      17.356  41.442  15.753  1.00 30.38           C  
-ATOM    973  C   THR B  29      16.340  40.793  16.714  1.00 32.28           C  
-ATOM    974  O   THR B  29      16.049  41.298  17.801  1.00 29.49           O  
-ATOM    975  CB  THR B  29      18.757  41.258  16.317  1.00 33.97           C  
-ATOM    976  OG1 THR B  29      19.686  41.877  15.412  1.00 36.77           O  
-ATOM    977  CG2 THR B  29      19.044  39.762  16.477  1.00 42.41           C  
-ATOM    978  N   VAL B  30      15.736  39.756  16.255  1.00 28.86           N  
-ATOM    979  CA  VAL B  30      14.645  38.996  16.842  1.00 28.01           C  
-ATOM    980  C   VAL B  30      15.045  37.571  17.203  1.00 27.59           C  
-ATOM    981  O   VAL B  30      15.556  36.769  16.359  1.00 29.32           O  
-ATOM    982  CB  VAL B  30      13.416  38.994  15.918  1.00 29.43           C  
-ATOM    983  CG1 VAL B  30      12.288  38.122  16.450  1.00 33.33           C  
-ATOM    984  CG2 VAL B  30      12.929  40.446  15.721  1.00 36.96           C  
-ATOM    985  N   THR B  31      14.783  37.239  18.485  1.00 25.21           N  
-ATOM    986  CA  THR B  31      15.110  35.909  19.016  1.00 26.71           C  
-ATOM    987  C   THR B  31      13.860  35.269  19.617  1.00 29.36           C  
-ATOM    988  O   THR B  31      13.085  35.948  20.314  1.00 27.37           O  
-ATOM    989  CB  THR B  31      16.192  35.964  20.111  1.00 24.34           C  
-ATOM    990  OG1 THR B  31      17.367  36.571  19.637  1.00 29.26           O  
-ATOM    991  CG2 THR B  31      16.655  34.534  20.525  1.00 27.22           C  
-ATOM    992  N   GLU B  32      13.529  34.028  19.358  1.00 26.47           N  
-ATOM    993  CA  GLU B  32      12.407  33.356  19.986  1.00 26.53           C  
-ATOM    994  C   GLU B  32      12.870  32.837  21.362  1.00 26.89           C  
-ATOM    995  O   GLU B  32      13.960  32.250  21.456  1.00 26.69           O  
-ATOM    996  CB  GLU B  32      11.954  32.177  19.127  1.00 39.87           C  
-ATOM    997  CG  GLU B  32      12.085  32.456  17.629  1.00 59.77           C  
-ATOM    998  CD  GLU B  32      10.953  33.303  17.086  1.00 75.32           C  
-ATOM    999  OE1 GLU B  32       9.936  33.322  17.821  1.00 77.04           O  
-ATOM   1000  OE2 GLU B  32      11.030  33.923  15.992  1.00 84.67           O  
-ATOM   1001  N   VAL B  33      12.190  33.258  22.427  1.00 24.15           N  
-ATOM   1002  CA  VAL B  33      12.655  32.869  23.748  1.00 24.62           C  
-ATOM   1003  C   VAL B  33      11.440  32.351  24.498  1.00 22.37           C  
-ATOM   1004  O   VAL B  33      10.325  32.348  23.969  1.00 25.30           O  
-ATOM   1005  CB  VAL B  33      13.324  34.081  24.494  1.00 27.93           C  
-ATOM   1006  CG1 VAL B  33      14.583  34.544  23.771  1.00 23.57           C  
-ATOM   1007  CG2 VAL B  33      12.340  35.220  24.625  1.00 22.06           C  
-ATOM   1008  N   LYS B  34      11.629  31.921  25.739  1.00 22.06           N  
-ATOM   1009  CA  LYS B  34      10.554  31.415  26.588  1.00 27.35           C  
-ATOM   1010  C   LYS B  34      10.639  31.993  28.000  1.00 27.73           C  
-ATOM   1011  O   LYS B  34      11.733  32.278  28.508  1.00 27.22           O  
-ATOM   1012  CB  LYS B  34      10.651  29.913  26.890  1.00 30.11           C  
-ATOM   1013  CG  LYS B  34      10.681  28.967  25.689  1.00 38.88           C  
-ATOM   1014  CD  LYS B  34      10.994  27.535  26.107  1.00 51.40           C  
-ATOM   1015  CE  LYS B  34      12.202  27.006  25.353  1.00 61.47           C  
-ATOM   1016  NZ  LYS B  34      13.077  26.161  26.215  1.00 72.08           N  
-ATOM   1017  N   GLY B  35       9.481  32.152  28.635  1.00 28.76           N  
-ATOM   1018  CA  GLY B  35       9.362  32.605  30.005  1.00 30.26           C  
-ATOM   1019  C   GLY B  35       8.605  31.507  30.739  1.00 34.37           C  
-ATOM   1020  O   GLY B  35       8.334  30.458  30.139  1.00 31.22           O  
-ATOM   1021  N   PHE B  36       8.270  31.697  32.009  1.00 42.57           N  
-ATOM   1022  CA  PHE B  36       7.579  30.671  32.733  1.00 44.50           C  
-ATOM   1023  C   PHE B  36       6.149  31.085  33.031  1.00 43.41           C  
-ATOM   1024  O   PHE B  36       5.841  32.283  33.089  1.00 40.86           O  
-ATOM   1025  CB  PHE B  36       8.315  30.340  34.031  1.00 38.05           C  
-ATOM   1026  CG  PHE B  36       9.580  29.593  33.732  1.00 47.90           C  
-ATOM   1027  CD1 PHE B  36       9.529  28.232  33.464  1.00 41.26           C  
-ATOM   1028  CD2 PHE B  36      10.781  30.268  33.704  1.00 43.60           C  
-ATOM   1029  CE1 PHE B  36      10.694  27.549  33.202  1.00 41.79           C  
-ATOM   1030  CE2 PHE B  36      11.942  29.563  33.426  1.00 48.31           C  
-ATOM   1031  CZ  PHE B  36      11.901  28.217  33.195  1.00 37.47           C  
-ATOM   1032  N   THR B  43       2.069  19.824  27.061  1.00 33.77           N  
-ATOM   1033  CA  THR B  43       3.103  18.931  26.521  1.00 37.54           C  
-ATOM   1034  C   THR B  43       3.901  19.657  25.439  1.00 39.22           C  
-ATOM   1035  O   THR B  43       3.336  20.508  24.754  1.00 41.02           O  
-ATOM   1036  CB  THR B  43       2.479  17.652  25.938  1.00 35.66           C  
-ATOM   1037  OG1 THR B  43       1.940  16.919  27.001  1.00 42.56           O  
-ATOM   1038  CG2 THR B  43       3.572  16.769  25.315  1.00 33.87           C  
-ATOM   1039  N   GLU B  44       5.213  19.613  25.479  1.00 32.84           N  
-ATOM   1040  CA  GLU B  44       6.040  20.086  24.380  1.00 36.22           C  
-ATOM   1041  C   GLU B  44       6.997  18.959  24.034  1.00 35.40           C  
-ATOM   1042  O   GLU B  44       7.429  18.162  24.905  1.00 33.78           O  
-ATOM   1043  CB  GLU B  44       6.738  21.408  24.675  1.00 36.79           C  
-ATOM   1044  CG  GLU B  44       7.987  21.623  23.867  1.00 52.54           C  
-ATOM   1045  CD  GLU B  44       8.894  22.751  24.348  1.00 66.05           C  
-ATOM   1046  OE1 GLU B  44      10.142  22.575  24.294  1.00 56.17           O  
-ATOM   1047  OE2 GLU B  44       8.345  23.799  24.782  1.00 52.76           O  
-ATOM   1048  N   LEU B  45       7.499  18.974  22.820  1.00 33.37           N  
-ATOM   1049  CA  LEU B  45       8.481  18.014  22.375  1.00 35.29           C  
-ATOM   1050  C   LEU B  45       9.870  18.627  22.508  1.00 37.20           C  
-ATOM   1051  O   LEU B  45       9.990  19.810  22.198  1.00 40.92           O  
-ATOM   1052  CB  LEU B  45       8.323  17.665  20.913  1.00 41.03           C  
-ATOM   1053  CG  LEU B  45       7.221  16.711  20.467  1.00 50.63           C  
-ATOM   1054  CD1 LEU B  45       7.439  16.522  18.967  1.00 41.48           C  
-ATOM   1055  CD2 LEU B  45       7.252  15.389  21.201  1.00 46.12           C  
-ATOM   1056  N   TYR B  46      10.856  17.877  22.927  1.00 31.72           N  
-ATOM   1057  CA  TYR B  46      12.201  18.376  22.979  1.00 30.85           C  
-ATOM   1058  C   TYR B  46      13.153  17.248  22.567  1.00 26.61           C  
-ATOM   1059  O   TYR B  46      13.302  16.243  23.251  1.00 29.39           O  
-ATOM   1060  CB  TYR B  46      12.539  18.948  24.350  1.00 31.29           C  
-ATOM   1061  CG  TYR B  46      13.959  19.467  24.414  1.00 30.73           C  
-ATOM   1062  CD1 TYR B  46      14.338  20.649  23.781  1.00 30.82           C  
-ATOM   1063  CD2 TYR B  46      14.899  18.754  25.119  1.00 29.29           C  
-ATOM   1064  CE1 TYR B  46      15.659  21.078  23.856  1.00 30.84           C  
-ATOM   1065  CE2 TYR B  46      16.195  19.160  25.184  1.00 28.02           C  
-ATOM   1066  CZ  TYR B  46      16.576  20.319  24.559  1.00 29.68           C  
-ATOM   1067  OH  TYR B  46      17.896  20.710  24.616  1.00 29.06           O  
-ATOM   1068  N   ARG B  47      13.793  17.448  21.404  1.00 27.03           N  
-ATOM   1069  CA  ARG B  47      14.696  16.481  20.777  1.00 26.16           C  
-ATOM   1070  C   ARG B  47      13.941  15.142  20.656  1.00 27.72           C  
-ATOM   1071  O   ARG B  47      14.494  14.080  20.911  1.00 32.69           O  
-ATOM   1072  CB  ARG B  47      16.051  16.410  21.535  1.00 30.67           C  
-ATOM   1073  CG  ARG B  47      16.879  17.697  21.400  1.00 24.58           C  
-ATOM   1074  CD  ARG B  47      18.205  17.642  22.130  1.00 21.05           C  
-ATOM   1075  NE  ARG B  47      19.333  17.847  21.263  1.00 36.05           N  
-ATOM   1076  CZ  ARG B  47      20.250  16.897  21.067  1.00 32.44           C  
-ATOM   1077  NH1 ARG B  47      20.124  15.734  21.677  1.00 69.43           N  
-ATOM   1078  NH2 ARG B  47      21.281  17.102  20.252  1.00 36.45           N  
-ATOM   1079  N   GLY B  48      12.661  15.217  20.287  1.00 30.41           N  
-ATOM   1080  CA  GLY B  48      11.877  14.019  20.010  1.00 36.74           C  
-ATOM   1081  C   GLY B  48      11.068  13.375  21.152  1.00 39.94           C  
-ATOM   1082  O   GLY B  48      10.289  12.466  20.893  1.00 45.34           O  
-ATOM   1083  N   ALA B  49      11.261  13.826  22.388  1.00 31.22           N  
-ATOM   1084  CA  ALA B  49      10.507  13.271  23.489  1.00 30.43           C  
-ATOM   1085  C   ALA B  49       9.536  14.290  24.038  1.00 27.78           C  
-ATOM   1086  O   ALA B  49       9.798  15.479  24.010  1.00 29.04           O  
-ATOM   1087  CB  ALA B  49      11.436  12.769  24.587  1.00 35.62           C  
-ATOM   1088  N   GLU B  50       8.405  13.825  24.550  1.00 25.85           N  
-ATOM   1089  CA  GLU B  50       7.427  14.718  25.108  1.00 28.42           C  
-ATOM   1090  C   GLU B  50       7.799  15.114  26.534  1.00 30.68           C  
-ATOM   1091  O   GLU B  50       8.133  14.214  27.305  1.00 36.46           O  
-ATOM   1092  CB  GLU B  50       6.119  13.919  25.151  1.00 29.57           C  
-ATOM   1093  CG  GLU B  50       5.587  13.873  23.685  1.00 57.65           C  
-ATOM   1094  CD  GLU B  50       4.430  12.912  23.452  1.00 65.69           C  
-ATOM   1095  OE1 GLU B  50       3.473  12.881  24.259  1.00 62.20           O  
-ATOM   1096  OE2 GLU B  50       4.460  12.160  22.440  1.00 78.15           O  
-ATOM   1097  N   TYR B  51       7.575  16.332  26.935  1.00 29.24           N  
-ATOM   1098  CA  TYR B  51       7.844  16.789  28.286  1.00 33.66           C  
-ATOM   1099  C   TYR B  51       6.637  17.626  28.676  1.00 36.88           C  
-ATOM   1100  O   TYR B  51       6.096  18.311  27.787  1.00 35.66           O  
-ATOM   1101  CB  TYR B  51       9.069  17.715  28.444  1.00 25.11           C  
-ATOM   1102  CG  TYR B  51      10.318  16.919  28.276  1.00 24.12           C  
-ATOM   1103  CD1 TYR B  51      10.785  16.646  26.969  1.00 27.01           C  
-ATOM   1104  CD2 TYR B  51      11.050  16.423  29.374  1.00 26.42           C  
-ATOM   1105  CE1 TYR B  51      11.934  15.877  26.724  1.00 25.25           C  
-ATOM   1106  CE2 TYR B  51      12.224  15.683  29.134  1.00 25.52           C  
-ATOM   1107  CZ  TYR B  51      12.631  15.421  27.836  1.00 30.55           C  
-ATOM   1108  OH  TYR B  51      13.767  14.664  27.670  1.00 30.39           O  
-ATOM   1109  N   VAL B  52       6.263  17.534  29.946  1.00 30.06           N  
-ATOM   1110  CA  VAL B  52       5.212  18.435  30.419  1.00 29.42           C  
-ATOM   1111  C   VAL B  52       5.887  19.663  31.036  1.00 29.73           C  
-ATOM   1112  O   VAL B  52       6.760  19.530  31.914  1.00 28.79           O  
-ATOM   1113  CB  VAL B  52       4.261  17.808  31.434  1.00 32.53           C  
-ATOM   1114  CG1 VAL B  52       3.318  18.876  32.001  1.00 39.91           C  
-ATOM   1115  CG2 VAL B  52       3.496  16.666  30.724  1.00 35.06           C  
-ATOM   1116  N   VAL B  53       5.543  20.867  30.599  1.00 25.81           N  
-ATOM   1117  CA  VAL B  53       6.372  22.016  31.037  1.00 24.72           C  
-ATOM   1118  C   VAL B  53       5.428  23.186  31.212  1.00 26.58           C  
-ATOM   1119  O   VAL B  53       4.286  23.160  30.716  1.00 32.03           O  
-ATOM   1120  CB  VAL B  53       7.483  22.426  30.009  1.00 30.03           C  
-ATOM   1121  CG1 VAL B  53       8.481  21.331  29.637  1.00 33.58           C  
-ATOM   1122  CG2 VAL B  53       6.794  22.818  28.672  1.00 40.44           C  
-ATOM   1123  N   ASP B  54       5.870  24.313  31.694  1.00 30.24           N  
-ATOM   1124  CA  ASP B  54       4.943  25.446  31.768  1.00 34.35           C  
-ATOM   1125  C   ASP B  54       5.553  26.713  31.173  1.00 37.56           C  
-ATOM   1126  O   ASP B  54       5.302  27.820  31.635  1.00 35.43           O  
-ATOM   1127  CB  ASP B  54       4.550  25.647  33.234  1.00 45.80           C  
-ATOM   1128  CG  ASP B  54       5.761  26.007  34.091  1.00 56.94           C  
-ATOM   1129  OD1 ASP B  54       6.939  25.777  33.713  1.00 47.39           O  
-ATOM   1130  OD2 ASP B  54       5.495  26.560  35.188  1.00 65.79           O  
-ATOM   1131  N   PHE B  55       6.262  26.572  30.051  1.00 35.35           N  
-ATOM   1132  CA  PHE B  55       6.783  27.691  29.302  1.00 37.45           C  
-ATOM   1133  C   PHE B  55       5.667  28.593  28.744  1.00 36.08           C  
-ATOM   1134  O   PHE B  55       4.658  28.052  28.323  1.00 32.50           O  
-ATOM   1135  CB  PHE B  55       7.615  27.170  28.117  1.00 29.60           C  
-ATOM   1136  CG  PHE B  55       8.871  26.481  28.549  1.00 26.80           C  
-ATOM   1137  CD1 PHE B  55       9.703  27.095  29.484  1.00 38.90           C  
-ATOM   1138  CD2 PHE B  55       9.230  25.273  27.999  1.00 36.81           C  
-ATOM   1139  CE1 PHE B  55      10.871  26.477  29.899  1.00 45.45           C  
-ATOM   1140  CE2 PHE B  55      10.407  24.657  28.408  1.00 39.83           C  
-ATOM   1141  CZ  PHE B  55      11.227  25.254  29.383  1.00 40.40           C  
-ATOM   1142  N   LEU B  56       5.938  29.861  28.563  1.00 34.28           N  
-ATOM   1143  CA  LEU B  56       5.126  30.756  27.736  1.00 38.22           C  
-ATOM   1144  C   LEU B  56       6.125  31.273  26.655  1.00 35.51           C  
-ATOM   1145  O   LEU B  56       7.214  31.713  26.964  1.00 28.19           O  
-ATOM   1146  CB  LEU B  56       4.520  31.973  28.413  1.00 38.73           C  
-ATOM   1147  CG  LEU B  56       3.730  31.908  29.719  1.00 47.76           C  
-ATOM   1148  CD1 LEU B  56       3.262  33.274  30.254  1.00 48.23           C  
-ATOM   1149  CD2 LEU B  56       2.491  31.052  29.560  1.00 42.13           C  
-ATOM   1150  N   PRO B  57       5.698  31.320  25.398  1.00 32.39           N  
-ATOM   1151  CA  PRO B  57       6.597  31.819  24.348  1.00 32.41           C  
-ATOM   1152  C   PRO B  57       6.669  33.321  24.403  1.00 25.90           C  
-ATOM   1153  O   PRO B  57       5.682  34.037  24.579  1.00 24.52           O  
-ATOM   1154  CB  PRO B  57       5.923  31.416  23.047  1.00 35.97           C  
-ATOM   1155  CG  PRO B  57       4.578  30.937  23.404  1.00 37.59           C  
-ATOM   1156  CD  PRO B  57       4.417  30.803  24.892  1.00 33.36           C  
-ATOM   1157  N   LYS B  58       7.798  33.947  24.166  1.00 25.97           N  
-ATOM   1158  CA  LYS B  58       7.956  35.357  24.088  1.00 23.81           C  
-ATOM   1159  C   LYS B  58       8.847  35.675  22.859  1.00 23.51           C  
-ATOM   1160  O   LYS B  58       9.445  34.757  22.366  1.00 20.85           O  
-ATOM   1161  CB  LYS B  58       8.595  35.932  25.356  1.00 34.02           C  
-ATOM   1162  CG  LYS B  58       7.888  35.493  26.681  1.00 36.50           C  
-ATOM   1163  CD  LYS B  58       6.666  36.296  26.966  1.00 45.37           C  
-ATOM   1164  CE  LYS B  58       6.176  36.413  28.413  1.00 53.41           C  
-ATOM   1165  NZ  LYS B  58       4.737  36.949  28.428  1.00 45.36           N  
-ATOM   1166  N   VAL B  59       9.030  36.940  22.563  1.00 21.93           N  
-ATOM   1167  CA  VAL B  59       9.998  37.342  21.549  1.00 25.39           C  
-ATOM   1168  C   VAL B  59      10.879  38.373  22.186  1.00 22.71           C  
-ATOM   1169  O   VAL B  59      10.446  39.272  22.941  1.00 25.12           O  
-ATOM   1170  CB  VAL B  59       9.090  37.859  20.382  1.00 32.87           C  
-ATOM   1171  CG1 VAL B  59       9.609  39.026  19.654  1.00 35.25           C  
-ATOM   1172  CG2 VAL B  59       8.813  36.659  19.458  1.00 29.67           C  
-ATOM   1173  N   LYS B  60      12.166  38.193  21.982  1.00 20.50           N  
-ATOM   1174  CA  LYS B  60      13.103  39.208  22.340  1.00 25.88           C  
-ATOM   1175  C   LYS B  60      13.447  40.011  21.080  1.00 29.05           C  
-ATOM   1176  O   LYS B  60      13.946  39.532  20.022  1.00 30.00           O  
-ATOM   1177  CB  LYS B  60      14.375  38.496  22.857  1.00 24.43           C  
-ATOM   1178  CG  LYS B  60      15.423  39.587  23.079  1.00 26.16           C  
-ATOM   1179  CD  LYS B  60      16.767  39.123  23.575  1.00 31.50           C  
-ATOM   1180  CE  LYS B  60      16.801  38.314  24.806  1.00 38.05           C  
-ATOM   1181  NZ  LYS B  60      18.238  37.856  25.099  1.00 38.83           N  
-ATOM   1182  N   ILE B  61      13.405  41.313  21.236  1.00 26.37           N  
-ATOM   1183  CA  ILE B  61      13.836  42.263  20.191  1.00 29.17           C  
-ATOM   1184  C   ILE B  61      15.084  42.982  20.603  1.00 33.07           C  
-ATOM   1185  O   ILE B  61      15.160  43.301  21.825  1.00 31.10           O  
-ATOM   1186  CB  ILE B  61      12.667  43.279  20.062  1.00 34.53           C  
-ATOM   1187  CG1 ILE B  61      11.552  42.560  19.261  1.00 38.10           C  
-ATOM   1188  CG2 ILE B  61      13.203  44.500  19.326  1.00 44.29           C  
-ATOM   1189  CD1 ILE B  61      10.264  43.416  19.352  1.00 48.17           C  
-ATOM   1190  N   GLU B  62      16.144  43.031  19.743  1.00 26.77           N  
-ATOM   1191  CA  GLU B  62      17.249  43.847  20.208  1.00 31.20           C  
-ATOM   1192  C   GLU B  62      17.608  44.895  19.127  1.00 34.97           C  
-ATOM   1193  O   GLU B  62      17.654  44.496  17.957  1.00 32.08           O  
-ATOM   1194  CB  GLU B  62      18.530  43.038  20.428  1.00 29.99           C  
-ATOM   1195  CG  GLU B  62      18.449  42.109  21.616  1.00 33.08           C  
-ATOM   1196  CD  GLU B  62      19.532  41.046  21.488  1.00 35.71           C  
-ATOM   1197  OE1 GLU B  62      19.528  40.367  20.469  1.00 41.34           O  
-ATOM   1198  OE2 GLU B  62      20.335  40.907  22.426  1.00 39.64           O  
-ATOM   1199  N   VAL B  63      17.890  46.124  19.530  1.00 36.78           N  
-ATOM   1200  CA  VAL B  63      18.288  47.176  18.589  1.00 38.58           C  
-ATOM   1201  C   VAL B  63      19.458  47.923  19.271  1.00 41.44           C  
-ATOM   1202  O   VAL B  63      19.355  48.198  20.459  1.00 39.91           O  
-ATOM   1203  CB  VAL B  63      17.305  48.263  18.165  1.00 44.78           C  
-ATOM   1204  CG1 VAL B  63      15.961  47.836  17.628  1.00 44.50           C  
-ATOM   1205  CG2 VAL B  63      16.893  49.207  19.342  1.00 43.13           C  
-ATOM   1206  N   VAL B  64      20.457  48.265  18.469  1.00 38.96           N  
-ATOM   1207  CA  VAL B  64      21.580  49.043  18.962  1.00 39.88           C  
-ATOM   1208  C   VAL B  64      21.450  50.435  18.346  1.00 42.95           C  
-ATOM   1209  O   VAL B  64      21.591  50.528  17.135  1.00 42.34           O  
-ATOM   1210  CB  VAL B  64      22.935  48.413  18.601  1.00 40.01           C  
-ATOM   1211  CG1 VAL B  64      24.125  49.337  18.745  1.00 45.06           C  
-ATOM   1212  CG2 VAL B  64      23.280  47.184  19.468  1.00 43.14           C  
-ATOM   1213  N   VAL B  65      21.290  51.477  19.153  1.00 41.79           N  
-ATOM   1214  CA  VAL B  65      21.122  52.821  18.610  1.00 41.57           C  
-ATOM   1215  C   VAL B  65      22.013  53.886  19.235  1.00 45.17           C  
-ATOM   1216  O   VAL B  65      22.478  53.777  20.390  1.00 38.18           O  
-ATOM   1217  CB  VAL B  65      19.677  53.336  18.815  1.00 37.39           C  
-ATOM   1218  CG1 VAL B  65      18.699  52.509  17.989  1.00 42.53           C  
-ATOM   1219  CG2 VAL B  65      19.305  53.221  20.318  1.00 39.39           C  
-ATOM   1220  N   ASP B  66      21.902  55.052  18.563  1.00 47.29           N  
-ATOM   1221  CA  ASP B  66      22.599  56.245  19.060  1.00 44.70           C  
-ATOM   1222  C   ASP B  66      21.971  56.726  20.361  1.00 43.44           C  
-ATOM   1223  O   ASP B  66      20.739  56.667  20.539  1.00 42.19           O  
-ATOM   1224  CB  ASP B  66      22.520  57.352  18.014  1.00 60.81           C  
-ATOM   1225  CG  ASP B  66      23.801  58.179  18.055  1.00 74.63           C  
-ATOM   1226  OD1 ASP B  66      23.838  59.150  18.845  1.00 75.55           O  
-ATOM   1227  OD2 ASP B  66      24.728  57.803  17.300  1.00 81.43           O  
-ATOM   1228  N   ASP B  67      22.765  57.239  21.297  1.00 40.64           N  
-ATOM   1229  CA  ASP B  67      22.244  57.666  22.591  1.00 45.85           C  
-ATOM   1230  C   ASP B  67      21.046  58.606  22.513  1.00 48.44           C  
-ATOM   1231  O   ASP B  67      20.149  58.605  23.352  1.00 51.38           O  
-ATOM   1232  CB  ASP B  67      23.338  58.441  23.351  1.00 44.89           C  
-ATOM   1233  CG  ASP B  67      24.482  57.617  23.807  1.00 48.60           C  
-ATOM   1234  OD1 ASP B  67      24.469  56.400  23.577  1.00 49.21           O  
-ATOM   1235  OD2 ASP B  67      25.448  58.138  24.416  1.00 58.15           O  
-ATOM   1236  N   LYS B  68      21.015  59.465  21.512  1.00 49.08           N  
-ATOM   1237  CA  LYS B  68      20.018  60.476  21.298  1.00 56.78           C  
-ATOM   1238  C   LYS B  68      18.661  59.874  20.963  1.00 57.71           C  
-ATOM   1239  O   LYS B  68      17.668  60.560  21.190  1.00 57.59           O  
-ATOM   1240  CB  LYS B  68      20.436  61.412  20.145  1.00 54.57           C  
-ATOM   1241  N   VAL B  69      18.688  58.712  20.341  1.00 56.08           N  
-ATOM   1242  CA  VAL B  69      17.498  58.000  19.871  1.00 54.36           C  
-ATOM   1243  C   VAL B  69      16.866  57.116  20.934  1.00 49.96           C  
-ATOM   1244  O   VAL B  69      15.813  56.577  20.647  1.00 45.02           O  
-ATOM   1245  CB  VAL B  69      17.958  57.173  18.641  1.00 56.67           C  
-ATOM   1246  CG1 VAL B  69      17.040  56.137  18.055  1.00 52.66           C  
-ATOM   1247  CG2 VAL B  69      18.286  58.119  17.462  1.00 54.39           C  
-ATOM   1248  N   VAL B  70      17.463  56.816  22.092  1.00 49.38           N  
-ATOM   1249  CA  VAL B  70      16.979  55.811  23.040  1.00 43.81           C  
-ATOM   1250  C   VAL B  70      15.583  56.078  23.572  1.00 45.92           C  
-ATOM   1251  O   VAL B  70      14.698  55.200  23.671  1.00 40.67           O  
-ATOM   1252  CB  VAL B  70      17.948  55.678  24.245  1.00 45.77           C  
-ATOM   1253  CG1 VAL B  70      17.395  54.783  25.335  1.00 46.22           C  
-ATOM   1254  CG2 VAL B  70      19.273  55.073  23.784  1.00 45.91           C  
-ATOM   1255  N   GLU B  71      15.363  57.333  23.990  1.00 43.91           N  
-ATOM   1256  CA  GLU B  71      14.122  57.668  24.701  1.00 48.33           C  
-ATOM   1257  C   GLU B  71      12.931  57.597  23.752  1.00 41.82           C  
-ATOM   1258  O   GLU B  71      11.897  57.024  24.084  1.00 43.18           O  
-ATOM   1259  CB  GLU B  71      14.164  59.018  25.413  1.00 51.10           C  
-ATOM   1260  CG  GLU B  71      15.392  59.274  26.254  1.00 85.84           C  
-ATOM   1261  CD  GLU B  71      16.102  58.156  26.976  1.00 99.58           C  
-ATOM   1262  OE1 GLU B  71      15.468  57.169  27.430  1.00109.80           O  
-ATOM   1263  OE2 GLU B  71      17.356  58.262  27.103  1.00103.42           O  
-ATOM   1264  N   GLN B  72      13.187  57.994  22.516  1.00 38.74           N  
-ATOM   1265  CA  GLN B  72      12.115  57.823  21.514  1.00 44.16           C  
-ATOM   1266  C   GLN B  72      12.006  56.341  21.091  1.00 38.46           C  
-ATOM   1267  O   GLN B  72      10.893  55.872  20.864  1.00 35.53           O  
-ATOM   1268  CB  GLN B  72      12.308  58.824  20.389  1.00 43.99           C  
-ATOM   1269  CG  GLN B  72      12.888  58.313  19.100  1.00 66.02           C  
-ATOM   1270  CD  GLN B  72      13.833  59.211  18.317  1.00 72.96           C  
-ATOM   1271  OE1 GLN B  72      14.381  60.212  18.798  1.00 70.11           O  
-ATOM   1272  NE2 GLN B  72      14.068  58.843  17.050  1.00 71.25           N  
-ATOM   1273  N   ALA B  73      13.073  55.531  21.130  1.00 38.24           N  
-ATOM   1274  CA  ALA B  73      12.897  54.080  20.793  1.00 41.81           C  
-ATOM   1275  C   ALA B  73      12.077  53.408  21.886  1.00 37.46           C  
-ATOM   1276  O   ALA B  73      11.151  52.641  21.660  1.00 39.86           O  
-ATOM   1277  CB  ALA B  73      14.244  53.343  20.743  1.00 34.40           C  
-ATOM   1278  N   VAL B  74      12.408  53.787  23.155  1.00 38.84           N  
-ATOM   1279  CA  VAL B  74      11.785  53.162  24.316  1.00 37.99           C  
-ATOM   1280  C   VAL B  74      10.282  53.436  24.350  1.00 36.43           C  
-ATOM   1281  O   VAL B  74       9.386  52.587  24.410  1.00 34.54           O  
-ATOM   1282  CB  VAL B  74      12.488  53.536  25.640  1.00 34.25           C  
-ATOM   1283  CG1 VAL B  74      11.591  53.250  26.831  1.00 36.83           C  
-ATOM   1284  CG2 VAL B  74      13.838  52.848  25.763  1.00 39.03           C  
-ATOM   1285  N   ASP B  75       9.968  54.705  24.117  1.00 37.16           N  
-ATOM   1286  CA  ASP B  75       8.610  55.205  24.017  1.00 36.08           C  
-ATOM   1287  C   ASP B  75       7.807  54.484  22.920  1.00 36.47           C  
-ATOM   1288  O   ASP B  75       6.713  53.985  23.117  1.00 36.64           O  
-ATOM   1289  CB  ASP B  75       8.652  56.701  23.658  1.00 52.08           C  
-ATOM   1290  CG  ASP B  75       7.248  57.267  23.594  1.00 60.41           C  
-ATOM   1291  OD1 ASP B  75       6.588  57.194  24.656  1.00 65.02           O  
-ATOM   1292  OD2 ASP B  75       6.832  57.745  22.523  1.00 67.77           O  
-ATOM   1293  N   ALA B  76       8.417  54.366  21.753  1.00 35.30           N  
-ATOM   1294  CA  ALA B  76       7.815  53.608  20.662  1.00 34.49           C  
-ATOM   1295  C   ALA B  76       7.564  52.154  21.082  1.00 32.89           C  
-ATOM   1296  O   ALA B  76       6.445  51.699  20.817  1.00 32.44           O  
-ATOM   1297  CB  ALA B  76       8.720  53.672  19.451  1.00 35.26           C  
-ATOM   1298  N   ILE B  77       8.445  51.474  21.828  1.00 30.24           N  
-ATOM   1299  CA  ILE B  77       8.112  50.054  22.142  1.00 30.64           C  
-ATOM   1300  C   ILE B  77       6.978  49.896  23.131  1.00 35.84           C  
-ATOM   1301  O   ILE B  77       6.011  49.149  23.009  1.00 36.74           O  
-ATOM   1302  CB  ILE B  77       9.376  49.340  22.637  1.00 31.07           C  
-ATOM   1303  CG1 ILE B  77      10.338  49.251  21.427  1.00 32.86           C  
-ATOM   1304  CG2 ILE B  77       9.073  47.921  23.191  1.00 27.54           C  
-ATOM   1305  CD1 ILE B  77      11.804  49.206  21.861  1.00 38.80           C  
-ATOM   1306  N   ILE B  78       7.049  50.757  24.177  1.00 35.94           N  
-ATOM   1307  CA  ILE B  78       6.059  50.723  25.230  1.00 39.04           C  
-ATOM   1308  C   ILE B  78       4.682  50.882  24.636  1.00 37.00           C  
-ATOM   1309  O   ILE B  78       3.779  50.119  24.987  1.00 40.70           O  
-ATOM   1310  CB  ILE B  78       6.258  51.858  26.271  1.00 44.79           C  
-ATOM   1311  CG1 ILE B  78       7.420  51.439  27.195  1.00 43.82           C  
-ATOM   1312  CG2 ILE B  78       5.009  52.142  27.091  1.00 44.09           C  
-ATOM   1313  CD1 ILE B  78       7.710  52.473  28.267  1.00 54.64           C  
-ATOM   1314  N   LYS B  79       4.497  51.948  23.874  1.00 33.62           N  
-ATOM   1315  CA  LYS B  79       3.141  52.184  23.347  1.00 40.97           C  
-ATOM   1316  C   LYS B  79       2.626  51.032  22.477  1.00 41.91           C  
-ATOM   1317  O   LYS B  79       1.425  50.747  22.454  1.00 35.90           O  
-ATOM   1318  CB  LYS B  79       3.128  53.479  22.511  1.00 45.80           C  
-ATOM   1319  CG  LYS B  79       3.142  54.762  23.321  1.00 57.07           C  
-ATOM   1320  CD  LYS B  79       2.782  55.963  22.464  1.00 64.73           C  
-ATOM   1321  CE  LYS B  79       3.889  56.914  22.073  1.00 70.17           C  
-ATOM   1322  NZ  LYS B  79       4.278  57.884  23.145  1.00 70.71           N  
-ATOM   1323  N   ALA B  80       3.511  50.411  21.660  1.00 34.41           N  
-ATOM   1324  CA  ALA B  80       3.050  49.378  20.779  1.00 32.52           C  
-ATOM   1325  C   ALA B  80       2.906  48.042  21.511  1.00 34.33           C  
-ATOM   1326  O   ALA B  80       2.163  47.183  21.014  1.00 34.10           O  
-ATOM   1327  CB  ALA B  80       4.124  49.108  19.672  1.00 26.64           C  
-ATOM   1328  N   ALA B  81       3.775  47.810  22.516  1.00 29.17           N  
-ATOM   1329  CA  ALA B  81       3.715  46.448  23.071  1.00 32.44           C  
-ATOM   1330  C   ALA B  81       2.694  46.301  24.203  1.00 34.81           C  
-ATOM   1331  O   ALA B  81       2.243  45.186  24.546  1.00 32.44           O  
-ATOM   1332  CB  ALA B  81       5.111  46.054  23.564  1.00 30.28           C  
-ATOM   1333  N   ARG B  82       2.295  47.355  24.836  1.00 35.04           N  
-ATOM   1334  CA  ARG B  82       1.378  47.189  25.939  1.00 38.36           C  
-ATOM   1335  C   ARG B  82      -0.047  46.686  25.563  1.00 38.23           C  
-ATOM   1336  O   ARG B  82      -0.720  47.243  24.685  1.00 42.74           O  
-ATOM   1337  CB  ARG B  82       1.327  48.526  26.682  1.00 35.78           C  
-ATOM   1338  CG  ARG B  82       0.514  48.686  27.942  1.00 45.43           C  
-ATOM   1339  CD  ARG B  82       0.444  50.151  28.367  1.00 45.62           C  
-ATOM   1340  NE  ARG B  82       1.642  50.533  29.124  1.00 58.34           N  
-ATOM   1341  CZ  ARG B  82       2.048  51.790  29.398  1.00 63.33           C  
-ATOM   1342  NH1 ARG B  82       1.350  52.824  28.981  1.00 65.55           N  
-ATOM   1343  NH2 ARG B  82       3.164  51.983  30.084  1.00 55.91           N  
-ATOM   1344  N   THR B  83      -0.471  45.602  26.266  1.00 33.94           N  
-ATOM   1345  CA  THR B  83      -1.896  45.151  26.166  1.00 39.79           C  
-ATOM   1346  C   THR B  83      -2.644  45.571  27.425  1.00 43.08           C  
-ATOM   1347  O   THR B  83      -3.883  45.581  27.421  1.00 42.42           O  
-ATOM   1348  CB  THR B  83      -2.125  43.622  26.129  1.00 39.96           C  
-ATOM   1349  OG1 THR B  83      -1.646  43.037  27.347  1.00 40.96           O  
-ATOM   1350  CG2 THR B  83      -1.390  43.024  24.933  1.00 45.31           C  
-ATOM   1351  N   GLY B  84      -1.909  45.906  28.499  1.00 47.03           N  
-ATOM   1352  CA  GLY B  84      -2.522  46.295  29.749  1.00 48.99           C  
-ATOM   1353  C   GLY B  84      -2.670  45.085  30.697  1.00 50.92           C  
-ATOM   1354  O   GLY B  84      -3.178  45.200  31.809  1.00 54.55           O  
-ATOM   1355  N   LYS B  85      -2.209  43.952  30.221  1.00 48.39           N  
-ATOM   1356  CA  LYS B  85      -2.296  42.742  30.963  1.00 44.40           C  
-ATOM   1357  C   LYS B  85      -0.976  42.382  31.599  1.00 50.67           C  
-ATOM   1358  O   LYS B  85       0.061  42.937  31.248  1.00 48.56           O  
-ATOM   1359  CB  LYS B  85      -2.754  41.601  30.056  1.00 46.17           C  
-ATOM   1360  CG  LYS B  85      -4.062  41.852  29.343  1.00 44.52           C  
-ATOM   1361  CD  LYS B  85      -5.237  41.451  30.195  1.00 44.32           C  
-ATOM   1362  CE  LYS B  85      -6.367  42.455  30.108  1.00 55.97           C  
-ATOM   1363  NZ  LYS B  85      -7.615  41.935  30.736  1.00 57.60           N  
-ATOM   1364  N   ILE B  86      -1.015  41.413  32.501  1.00 47.68           N  
-ATOM   1365  CA  ILE B  86       0.173  40.913  33.151  1.00 48.05           C  
-ATOM   1366  C   ILE B  86       0.949  40.106  32.118  1.00 47.53           C  
-ATOM   1367  O   ILE B  86       0.332  39.420  31.310  1.00 44.72           O  
-ATOM   1368  CB  ILE B  86      -0.171  40.037  34.349  1.00 62.27           C  
-ATOM   1369  CG1 ILE B  86      -0.581  40.948  35.509  1.00 63.18           C  
-ATOM   1370  CG2 ILE B  86       0.993  39.155  34.732  1.00 53.77           C  
-ATOM   1371  CD1 ILE B  86      -0.774  40.215  36.819  1.00 68.90           C  
-ATOM   1372  N   GLY B  87       2.284  40.221  32.115  1.00 42.50           N  
-ATOM   1373  CA  GLY B  87       3.058  39.504  31.128  1.00 39.17           C  
-ATOM   1374  C   GLY B  87       3.412  40.373  29.905  1.00 38.29           C  
-ATOM   1375  O   GLY B  87       3.935  39.857  28.924  1.00 34.47           O  
-ATOM   1376  N   ASP B  88       3.119  41.647  29.952  1.00 33.71           N  
-ATOM   1377  CA  ASP B  88       3.443  42.522  28.825  1.00 34.21           C  
-ATOM   1378  C   ASP B  88       4.936  42.566  28.584  1.00 34.65           C  
-ATOM   1379  O   ASP B  88       5.359  42.786  27.455  1.00 31.49           O  
-ATOM   1380  CB  ASP B  88       2.883  43.911  29.077  1.00 38.52           C  
-ATOM   1381  CG  ASP B  88       1.498  44.044  28.515  1.00 37.07           C  
-ATOM   1382  OD1 ASP B  88       0.967  43.070  27.957  1.00 35.78           O  
-ATOM   1383  OD2 ASP B  88       0.937  45.162  28.625  1.00 38.04           O  
-ATOM   1384  N   GLY B  89       5.746  42.358  29.638  1.00 33.81           N  
-ATOM   1385  CA  GLY B  89       7.195  42.317  29.452  1.00 27.87           C  
-ATOM   1386  C   GLY B  89       7.994  43.475  30.092  1.00 28.26           C  
-ATOM   1387  O   GLY B  89       7.535  44.153  31.010  1.00 28.22           O  
-ATOM   1388  N   LYS B  90       9.197  43.646  29.529  1.00 31.84           N  
-ATOM   1389  CA  LYS B  90      10.154  44.619  30.031  1.00 32.64           C  
-ATOM   1390  C   LYS B  90      11.186  45.045  29.004  1.00 31.25           C  
-ATOM   1391  O   LYS B  90      11.519  44.312  28.071  1.00 31.38           O  
-ATOM   1392  CB  LYS B  90      10.932  44.007  31.213  1.00 40.81           C  
-ATOM   1393  CG  LYS B  90      11.723  42.753  30.835  1.00 51.68           C  
-ATOM   1394  CD  LYS B  90      12.576  42.239  31.985  1.00 67.44           C  
-ATOM   1395  CE  LYS B  90      12.939  40.767  31.792  1.00 66.92           C  
-ATOM   1396  NZ  LYS B  90      11.751  39.911  31.534  1.00 67.03           N  
-ATOM   1397  N   ILE B  91      11.665  46.266  29.165  1.00 23.00           N  
-ATOM   1398  CA  ILE B  91      12.681  46.840  28.304  1.00 29.59           C  
-ATOM   1399  C   ILE B  91      13.897  47.152  29.140  1.00 33.76           C  
-ATOM   1400  O   ILE B  91      13.766  47.652  30.258  1.00 32.84           O  
-ATOM   1401  CB  ILE B  91      12.248  48.196  27.668  1.00 33.42           C  
-ATOM   1402  CG1 ILE B  91      10.935  48.030  26.914  1.00 32.23           C  
-ATOM   1403  CG2 ILE B  91      13.318  48.724  26.743  1.00 29.60           C  
-ATOM   1404  CD1 ILE B  91      10.536  49.238  26.103  1.00 34.40           C  
-ATOM   1405  N   PHE B  92      15.079  46.891  28.590  1.00 31.45           N  
-ATOM   1406  CA  PHE B  92      16.259  47.377  29.299  1.00 35.25           C  
-ATOM   1407  C   PHE B  92      17.295  47.882  28.324  1.00 37.88           C  
-ATOM   1408  O   PHE B  92      17.421  47.449  27.179  1.00 34.89           O  
-ATOM   1409  CB  PHE B  92      16.922  46.391  30.252  1.00 41.48           C  
-ATOM   1410  CG  PHE B  92      17.130  45.028  29.709  1.00 33.93           C  
-ATOM   1411  CD1 PHE B  92      16.133  44.129  29.927  1.00 41.17           C  
-ATOM   1412  CD2 PHE B  92      18.270  44.678  29.007  1.00 51.58           C  
-ATOM   1413  CE1 PHE B  92      16.234  42.850  29.480  1.00 50.97           C  
-ATOM   1414  CE2 PHE B  92      18.384  43.391  28.541  1.00 53.45           C  
-ATOM   1415  CZ  PHE B  92      17.356  42.471  28.790  1.00 54.26           C  
-ATOM   1416  N   VAL B  93      18.008  48.843  28.865  1.00 32.92           N  
-ATOM   1417  CA  VAL B  93      19.032  49.581  28.149  1.00 34.83           C  
-ATOM   1418  C   VAL B  93      20.416  49.288  28.680  1.00 35.20           C  
-ATOM   1419  O   VAL B  93      20.658  49.271  29.878  1.00 41.02           O  
-ATOM   1420  CB  VAL B  93      18.704  51.069  28.253  1.00 38.82           C  
-ATOM   1421  CG1 VAL B  93      19.739  51.911  27.523  1.00 41.78           C  
-ATOM   1422  CG2 VAL B  93      17.299  51.343  27.719  1.00 38.88           C  
-ATOM   1423  N   GLN B  94      21.331  49.049  27.748  1.00 35.63           N  
-ATOM   1424  CA  GLN B  94      22.715  48.792  28.094  1.00 38.19           C  
-ATOM   1425  C   GLN B  94      23.670  49.619  27.212  1.00 37.70           C  
-ATOM   1426  O   GLN B  94      23.376  49.955  26.069  1.00 30.20           O  
-ATOM   1427  CB  GLN B  94      23.047  47.319  27.926  1.00 37.34           C  
-ATOM   1428  CG  GLN B  94      22.468  46.424  29.003  1.00 45.49           C  
-ATOM   1429  CD  GLN B  94      22.714  44.955  28.723  1.00 51.14           C  
-ATOM   1430  OE1 GLN B  94      21.975  44.315  27.986  1.00 49.24           O  
-ATOM   1431  NE2 GLN B  94      23.725  44.230  29.210  1.00 54.32           N  
-ATOM   1432  N   GLU B  95      24.806  49.931  27.806  1.00 40.07           N  
-ATOM   1433  CA  GLU B  95      25.840  50.544  26.985  1.00 37.84           C  
-ATOM   1434  C   GLU B  95      26.443  49.522  26.026  1.00 43.82           C  
-ATOM   1435  O   GLU B  95      26.517  48.345  26.370  1.00 42.05           O  
-ATOM   1436  CB  GLU B  95      27.014  51.001  27.857  1.00 49.46           C  
-ATOM   1437  CG  GLU B  95      26.876  52.481  28.218  1.00 66.76           C  
-ATOM   1438  CD  GLU B  95      27.253  53.321  27.003  1.00 67.27           C  
-ATOM   1439  OE1 GLU B  95      28.437  53.258  26.596  1.00 72.18           O  
-ATOM   1440  OE2 GLU B  95      26.375  54.015  26.472  1.00 68.92           O  
-ATOM   1441  N   VAL B  96      26.864  49.974  24.855  1.00 39.60           N  
-ATOM   1442  CA  VAL B  96      27.612  49.194  23.908  1.00 46.22           C  
-ATOM   1443  C   VAL B  96      28.980  49.866  23.749  1.00 49.91           C  
-ATOM   1444  O   VAL B  96      28.871  51.038  23.409  1.00 52.15           O  
-ATOM   1445  CB  VAL B  96      26.884  49.213  22.548  1.00 45.05           C  
-ATOM   1446  CG1 VAL B  96      27.800  48.580  21.530  1.00 49.37           C  
-ATOM   1447  CG2 VAL B  96      25.555  48.450  22.620  1.00 37.89           C  
-ATOM   1448  N   GLU B  97      30.115  49.341  24.178  1.00 47.82           N  
-ATOM   1449  CA  GLU B  97      31.370  50.041  24.016  1.00 50.37           C  
-ATOM   1450  C   GLU B  97      31.789  50.326  22.581  1.00 49.50           C  
-ATOM   1451  O   GLU B  97      32.436  51.339  22.313  1.00 49.33           O  
-ATOM   1452  CB  GLU B  97      32.526  49.262  24.644  1.00 48.35           C  
-ATOM   1453  CG  GLU B  97      32.464  49.096  26.154  1.00 56.65           C  
-ATOM   1454  CD  GLU B  97      33.780  48.518  26.649  1.00 58.90           C  
-ATOM   1455  OE1 GLU B  97      33.885  48.287  27.867  1.00 57.41           O  
-ATOM   1456  OE2 GLU B  97      34.704  48.293  25.839  1.00 59.05           O  
-ATOM   1457  N   GLN B  98      31.478  49.484  21.609  1.00 47.16           N  
-ATOM   1458  CA  GLN B  98      31.965  49.660  20.248  1.00 37.63           C  
-ATOM   1459  C   GLN B  98      31.116  48.841  19.310  1.00 39.33           C  
-ATOM   1460  O   GLN B  98      30.613  47.755  19.685  1.00 40.16           O  
-ATOM   1461  CB  GLN B  98      33.425  49.154  20.187  1.00 55.25           C  
-ATOM   1462  CG  GLN B  98      34.096  49.472  18.848  1.00 65.80           C  
-ATOM   1463  CD  GLN B  98      34.116  50.985  18.626  1.00 79.55           C  
-ATOM   1464  OE1 GLN B  98      33.104  51.613  18.270  1.00 81.31           O  
-ATOM   1465  NE2 GLN B  98      35.298  51.555  18.861  1.00 84.62           N  
-ATOM   1466  N   VAL B  99      30.778  49.393  18.175  1.00 36.92           N  
-ATOM   1467  CA  VAL B  99      30.010  48.745  17.153  1.00 41.06           C  
-ATOM   1468  C   VAL B  99      30.844  48.767  15.857  1.00 44.14           C  
-ATOM   1469  O   VAL B  99      31.309  49.867  15.503  1.00 43.62           O  
-ATOM   1470  CB  VAL B  99      28.678  49.397  16.783  1.00 52.09           C  
-ATOM   1471  CG1 VAL B  99      27.938  48.548  15.745  1.00 41.05           C  
-ATOM   1472  CG2 VAL B  99      27.828  49.656  17.996  1.00 52.22           C  
-ATOM   1473  N   ILE B 100      31.064  47.624  15.244  1.00 42.21           N  
-ATOM   1474  CA  ILE B 100      31.846  47.611  14.013  1.00 49.31           C  
-ATOM   1475  C   ILE B 100      30.972  47.067  12.892  1.00 53.30           C  
-ATOM   1476  O   ILE B 100      30.417  45.991  13.123  1.00 53.98           O  
-ATOM   1477  CB  ILE B 100      33.078  46.703  14.103  1.00 49.46           C  
-ATOM   1478  CG1 ILE B 100      34.086  47.128  15.148  1.00 46.60           C  
-ATOM   1479  CG2 ILE B 100      33.728  46.610  12.704  1.00 50.71           C  
-ATOM   1480  CD1 ILE B 100      33.839  46.753  16.581  1.00 43.23           C  
-ATOM   1481  N   ARG B 101      30.935  47.672  11.717  1.00 52.05           N  
-ATOM   1482  CA  ARG B 101      30.248  47.107  10.560  1.00 51.78           C  
-ATOM   1483  C   ARG B 101      31.275  46.224   9.825  1.00 53.40           C  
-ATOM   1484  O   ARG B 101      32.436  46.587   9.638  1.00 54.23           O  
-ATOM   1485  CB  ARG B 101      29.652  48.172   9.658  1.00 62.33           C  
-ATOM   1486  CG  ARG B 101      28.707  47.596   8.612  1.00 75.77           C  
-ATOM   1487  CD  ARG B 101      28.178  48.551   7.559  1.00 77.93           C  
-ATOM   1488  NE  ARG B 101      27.698  49.781   8.153  1.00 87.16           N  
-ATOM   1489  CZ  ARG B 101      26.666  50.514   7.781  1.00 90.62           C  
-ATOM   1490  NH1 ARG B 101      25.912  50.165   6.747  1.00 97.18           N  
-ATOM   1491  NH2 ARG B 101      26.439  51.609   8.500  1.00 88.41           N  
-ATOM   1492  N   ILE B 102      30.916  45.006   9.538  1.00 48.88           N  
-ATOM   1493  CA  ILE B 102      31.879  44.030   9.016  1.00 56.19           C  
-ATOM   1494  C   ILE B 102      32.385  44.350   7.606  1.00 57.29           C  
-ATOM   1495  O   ILE B 102      33.583  44.381   7.344  1.00 52.99           O  
-ATOM   1496  CB  ILE B 102      31.253  42.620   9.105  1.00 45.79           C  
-ATOM   1497  CG1 ILE B 102      31.217  42.198  10.576  1.00 50.32           C  
-ATOM   1498  CG2 ILE B 102      32.029  41.616   8.280  1.00 48.07           C  
-ATOM   1499  CD1 ILE B 102      30.392  40.953  10.832  1.00 51.86           C  
-ATOM   1500  N   ARG B 103      31.443  44.585   6.700  1.00 56.58           N  
-ATOM   1501  CA  ARG B 103      31.743  44.859   5.287  1.00 65.44           C  
-ATOM   1502  C   ARG B 103      32.835  45.910   5.041  1.00 66.98           C  
-ATOM   1503  O   ARG B 103      33.737  45.752   4.214  1.00 64.79           O  
-ATOM   1504  CB  ARG B 103      30.461  45.299   4.606  1.00 57.19           C  
-ATOM   1505  CG  ARG B 103      30.734  46.234   3.446  1.00 66.64           C  
-ATOM   1506  CD  ARG B 103      29.741  46.006   2.333  1.00 69.21           C  
-ATOM   1507  NE  ARG B 103      28.553  46.811   2.519  1.00 74.58           N  
-ATOM   1508  CZ  ARG B 103      28.477  47.909   3.262  1.00 82.66           C  
-ATOM   1509  NH1 ARG B 103      29.537  48.326   3.927  1.00 83.57           N  
-ATOM   1510  NH2 ARG B 103      27.337  48.591   3.347  1.00 91.72           N  
-ATOM   1511  N   THR B 104      32.706  46.994   5.806  1.00 69.52           N  
-ATOM   1512  CA  THR B 104      33.524  48.180   5.696  1.00 70.77           C  
-ATOM   1513  C   THR B 104      34.619  48.367   6.773  1.00 71.55           C  
-ATOM   1514  O   THR B 104      35.797  48.613   6.457  1.00 71.17           O  
-ATOM   1515  CB  THR B 104      32.627  49.424   5.816  1.00 72.18           C  
-ATOM   1516  OG1 THR B 104      32.057  49.463   7.131  1.00 63.45           O  
-ATOM   1517  CG2 THR B 104      31.520  49.381   4.779  1.00 78.10           C  
-ATOM   1518  N   GLY B 105      34.231  48.255   8.042  1.00 66.66           N  
-ATOM   1519  CA  GLY B 105      35.182  48.575   9.116  1.00 65.41           C  
-ATOM   1520  C   GLY B 105      34.701  49.870   9.758  1.00 64.59           C  
-ATOM   1521  O   GLY B 105      35.302  50.372  10.701  1.00 67.88           O  
-ATOM   1522  N   GLU B 106      33.567  50.382   9.294  1.00 62.84           N  
-ATOM   1523  CA  GLU B 106      32.973  51.545   9.973  1.00 62.23           C  
-ATOM   1524  C   GLU B 106      32.696  51.185  11.427  1.00 65.04           C  
-ATOM   1525  O   GLU B 106      32.466  50.021  11.769  1.00 55.23           O  
-ATOM   1526  CB  GLU B 106      31.713  51.945   9.238  1.00 67.07           C  
-ATOM   1527  CG  GLU B 106      32.003  52.340   7.789  1.00 72.73           C  
-ATOM   1528  CD  GLU B 106      30.735  52.588   6.993  1.00 75.80           C  
-ATOM   1529  OE1 GLU B 106      30.173  51.627   6.416  1.00 81.44           O  
-ATOM   1530  OE2 GLU B 106      30.296  53.757   6.949  1.00 75.79           O  
-ATOM   1531  N   THR B 107      32.829  52.144  12.330  1.00 68.38           N  
-ATOM   1532  CA  THR B 107      32.728  51.947  13.763  1.00 74.04           C  
-ATOM   1533  C   THR B 107      31.996  53.093  14.442  1.00 80.98           C  
-ATOM   1534  O   THR B 107      32.260  54.210  13.991  1.00 80.68           O  
-ATOM   1535  CB  THR B 107      34.153  51.962  14.346  1.00 72.59           C  
-ATOM   1536  OG1 THR B 107      34.726  53.221  13.937  1.00 63.39           O  
-ATOM   1537  CG2 THR B 107      35.058  50.834  13.898  1.00 63.80           C  
-TER    1538      THR B 107                                                      
-ATOM   1539  N   MET C   1      37.150  42.234  31.264  1.00 47.97           N  
-ATOM   1540  CA  MET C   1      36.687  41.208  30.296  1.00 46.05           C  
-ATOM   1541  C   MET C   1      35.534  41.795  29.464  1.00 43.90           C  
-ATOM   1542  O   MET C   1      34.892  42.734  29.966  1.00 35.96           O  
-ATOM   1543  CB  MET C   1      36.197  39.928  30.963  1.00 58.16           C  
-ATOM   1544  CG  MET C   1      37.299  39.089  31.625  1.00 54.51           C  
-ATOM   1545  SD  MET C   1      36.753  38.923  33.359  1.00 75.18           S  
-ATOM   1546  CE  MET C   1      36.775  40.642  33.859  1.00 78.60           C  
-ATOM   1547  N   LYS C   2      35.461  41.315  28.223  1.00 37.86           N  
-ATOM   1548  CA  LYS C   2      34.523  41.800  27.229  1.00 34.42           C  
-ATOM   1549  C   LYS C   2      33.712  40.707  26.655  1.00 33.45           C  
-ATOM   1550  O   LYS C   2      34.144  39.557  26.598  1.00 35.80           O  
-ATOM   1551  CB  LYS C   2      35.265  42.465  26.059  1.00 34.33           C  
-ATOM   1552  CG  LYS C   2      36.294  43.514  26.445  1.00 45.29           C  
-ATOM   1553  CD  LYS C   2      35.589  44.787  26.910  1.00 43.09           C  
-ATOM   1554  CE  LYS C   2      36.476  46.004  26.697  1.00 59.04           C  
-ATOM   1555  NZ  LYS C   2      37.165  46.424  27.952  1.00 52.47           N  
-ATOM   1556  N   GLN C   3      32.491  41.090  26.265  1.00 34.41           N  
-ATOM   1557  CA  GLN C   3      31.641  40.191  25.543  1.00 37.50           C  
-ATOM   1558  C   GLN C   3      31.655  40.690  24.110  1.00 35.88           C  
-ATOM   1559  O   GLN C   3      31.289  41.838  23.822  1.00 36.54           O  
-ATOM   1560  CB  GLN C   3      30.198  40.151  26.057  1.00 38.30           C  
-ATOM   1561  CG  GLN C   3      29.317  39.268  25.172  1.00 37.25           C  
-ATOM   1562  CD  GLN C   3      27.882  39.163  25.625  1.00 51.43           C  
-ATOM   1563  OE1 GLN C   3      27.437  38.113  26.100  1.00 53.68           O  
-ATOM   1564  NE2 GLN C   3      26.974  40.133  25.560  1.00 50.61           N  
-ATOM   1565  N   VAL C   4      32.100  39.811  23.212  1.00 29.95           N  
-ATOM   1566  CA  VAL C   4      32.111  40.176  21.789  1.00 31.29           C  
-ATOM   1567  C   VAL C   4      30.911  39.519  21.096  1.00 32.57           C  
-ATOM   1568  O   VAL C   4      30.775  38.309  21.121  1.00 30.39           O  
-ATOM   1569  CB  VAL C   4      33.431  39.728  21.114  1.00 34.92           C  
-ATOM   1570  CG1 VAL C   4      33.332  39.878  19.594  1.00 34.66           C  
-ATOM   1571  CG2 VAL C   4      34.612  40.531  21.649  1.00 37.66           C  
-ATOM   1572  N   THR C   5      30.044  40.320  20.508  1.00 33.07           N  
-ATOM   1573  CA  THR C   5      28.913  39.732  19.820  1.00 35.73           C  
-ATOM   1574  C   THR C   5      29.050  39.956  18.319  1.00 31.75           C  
-ATOM   1575  O   THR C   5      29.489  41.006  17.869  1.00 33.24           O  
-ATOM   1576  CB  THR C   5      27.580  40.363  20.298  1.00 37.68           C  
-ATOM   1577  OG1 THR C   5      27.407  40.093  21.699  1.00 34.07           O  
-ATOM   1578  CG2 THR C   5      26.408  39.788  19.503  1.00 37.51           C  
-ATOM   1579  N   ALA C   6      28.662  38.961  17.511  1.00 29.39           N  
-ATOM   1580  CA  ALA C   6      28.718  39.122  16.105  1.00 35.79           C  
-ATOM   1581  C   ALA C   6      27.417  38.595  15.514  1.00 32.56           C  
-ATOM   1582  O   ALA C   6      26.983  37.493  15.882  1.00 33.72           O  
-ATOM   1583  CB  ALA C   6      29.923  38.412  15.516  1.00 30.91           C  
-ATOM   1584  N   ILE C   7      26.794  39.321  14.603  1.00 29.89           N  
-ATOM   1585  CA  ILE C   7      25.612  38.834  13.906  1.00 28.80           C  
-ATOM   1586  C   ILE C   7      26.108  38.613  12.476  1.00 35.77           C  
-ATOM   1587  O   ILE C   7      26.518  39.590  11.849  1.00 33.67           O  
-ATOM   1588  CB  ILE C   7      24.448  39.854  13.892  1.00 34.48           C  
-ATOM   1589  CG1 ILE C   7      24.016  40.325  15.268  1.00 43.11           C  
-ATOM   1590  CG2 ILE C   7      23.245  39.256  13.176  1.00 43.00           C  
-ATOM   1591  CD1 ILE C   7      24.717  39.608  16.403  1.00 49.39           C  
-ATOM   1592  N   ILE C   8      26.101  37.411  11.943  1.00 33.86           N  
-ATOM   1593  CA  ILE C   8      26.721  37.095  10.665  1.00 38.67           C  
-ATOM   1594  C   ILE C   8      25.757  36.239   9.864  1.00 35.54           C  
-ATOM   1595  O   ILE C   8      24.758  35.794  10.382  1.00 33.14           O  
-ATOM   1596  CB  ILE C   8      28.058  36.346  10.794  1.00 33.37           C  
-ATOM   1597  CG1 ILE C   8      27.776  35.030  11.574  1.00 38.02           C  
-ATOM   1598  CG2 ILE C   8      29.195  37.129  11.417  1.00 38.45           C  
-ATOM   1599  CD1 ILE C   8      28.943  34.057  11.573  1.00 44.91           C  
-ATOM   1600  N   LYS C   9      26.111  36.016   8.589  1.00 41.14           N  
-ATOM   1601  CA  LYS C   9      25.286  35.166   7.709  1.00 39.71           C  
-ATOM   1602  C   LYS C   9      25.601  33.719   8.111  1.00 31.25           C  
-ATOM   1603  O   LYS C   9      26.719  33.454   8.589  1.00 33.82           O  
-ATOM   1604  CB  LYS C   9      25.641  35.402   6.245  1.00 51.55           C  
-ATOM   1605  CG  LYS C   9      25.059  36.607   5.536  1.00 46.77           C  
-ATOM   1606  CD  LYS C   9      26.000  37.011   4.398  1.00 59.29           C  
-ATOM   1607  CE  LYS C   9      25.360  38.145   3.618  1.00 64.89           C  
-ATOM   1608  NZ  LYS C   9      26.400  39.046   3.048  1.00 73.15           N  
-ATOM   1609  N   PRO C  10      24.623  32.869   8.182  1.00 32.93           N  
-ATOM   1610  CA  PRO C  10      24.788  31.510   8.642  1.00 36.35           C  
-ATOM   1611  C   PRO C  10      25.898  30.714   8.010  1.00 37.72           C  
-ATOM   1612  O   PRO C  10      26.570  29.934   8.724  1.00 35.45           O  
-ATOM   1613  CB  PRO C  10      23.442  30.826   8.452  1.00 32.79           C  
-ATOM   1614  CG  PRO C  10      22.474  31.914   8.289  1.00 37.11           C  
-ATOM   1615  CD  PRO C  10      23.215  33.130   7.804  1.00 35.89           C  
-ATOM   1616  N   PHE C  11      26.132  30.925   6.696  1.00 42.78           N  
-ATOM   1617  CA  PHE C  11      27.140  30.076   6.022  1.00 41.70           C  
-ATOM   1618  C   PHE C  11      28.533  30.460   6.505  1.00 42.30           C  
-ATOM   1619  O   PHE C  11      29.467  29.713   6.234  1.00 40.56           O  
-ATOM   1620  CB  PHE C  11      27.011  30.145   4.514  1.00 53.54           C  
-ATOM   1621  CG  PHE C  11      26.900  31.481   3.854  1.00 65.52           C  
-ATOM   1622  CD1 PHE C  11      28.008  32.179   3.403  1.00 66.09           C  
-ATOM   1623  CD2 PHE C  11      25.649  32.065   3.672  1.00 72.36           C  
-ATOM   1624  CE1 PHE C  11      27.884  33.419   2.790  1.00 58.24           C  
-ATOM   1625  CE2 PHE C  11      25.516  33.300   3.063  1.00 69.30           C  
-ATOM   1626  CZ  PHE C  11      26.639  33.972   2.624  1.00 66.76           C  
-ATOM   1627  N   LYS C  12      28.724  31.618   7.164  1.00 34.93           N  
-ATOM   1628  CA  LYS C  12      30.066  31.911   7.658  1.00 32.95           C  
-ATOM   1629  C   LYS C  12      30.440  31.349   8.998  1.00 37.61           C  
-ATOM   1630  O   LYS C  12      31.557  31.576   9.491  1.00 37.70           O  
-ATOM   1631  CB  LYS C  12      30.193  33.464   7.569  1.00 36.54           C  
-ATOM   1632  CG  LYS C  12      30.240  33.875   6.052  1.00 36.27           C  
-ATOM   1633  CD  LYS C  12      31.610  33.474   5.531  1.00 42.13           C  
-ATOM   1634  CE  LYS C  12      32.112  34.297   4.369  1.00 55.55           C  
-ATOM   1635  NZ  LYS C  12      33.462  33.853   3.883  1.00 62.37           N  
-ATOM   1636  N   LEU C  13      29.507  30.627   9.660  1.00 37.91           N  
-ATOM   1637  CA  LEU C  13      29.771  30.170  11.029  1.00 33.38           C  
-ATOM   1638  C   LEU C  13      31.057  29.367  11.024  1.00 32.92           C  
-ATOM   1639  O   LEU C  13      31.904  29.520  11.913  1.00 32.04           O  
-ATOM   1640  CB  LEU C  13      28.560  29.308  11.487  1.00 27.38           C  
-ATOM   1641  CG  LEU C  13      28.270  29.112  12.960  1.00 41.96           C  
-ATOM   1642  CD1 LEU C  13      27.591  27.790  13.314  1.00 32.18           C  
-ATOM   1643  CD2 LEU C  13      29.462  29.373  13.842  1.00 33.97           C  
-ATOM   1644  N   ASP C  14      31.132  28.365  10.104  1.00 31.58           N  
-ATOM   1645  CA  ASP C  14      32.320  27.513  10.136  1.00 33.66           C  
-ATOM   1646  C   ASP C  14      33.610  28.310  10.013  1.00 32.81           C  
-ATOM   1647  O   ASP C  14      34.536  28.076  10.810  1.00 34.73           O  
-ATOM   1648  CB  ASP C  14      32.253  26.377   9.096  1.00 43.03           C  
-ATOM   1649  CG  ASP C  14      31.179  25.352   9.407  1.00 47.59           C  
-ATOM   1650  OD1 ASP C  14      30.929  25.089  10.625  1.00 50.91           O  
-ATOM   1651  OD2 ASP C  14      30.533  24.818   8.459  1.00 39.83           O  
-ATOM   1652  N   GLU C  15      33.707  29.310   9.164  1.00 29.55           N  
-ATOM   1653  CA  GLU C  15      34.954  30.014   8.942  1.00 34.81           C  
-ATOM   1654  C   GLU C  15      35.276  30.918  10.105  1.00 36.55           C  
-ATOM   1655  O   GLU C  15      36.418  31.050  10.623  1.00 38.44           O  
-ATOM   1656  CB  GLU C  15      34.805  30.797   7.614  1.00 41.08           C  
-ATOM   1657  CG  GLU C  15      34.469  29.861   6.452  1.00 58.40           C  
-ATOM   1658  CD  GLU C  15      34.288  30.582   5.128  1.00 57.83           C  
-ATOM   1659  OE1 GLU C  15      33.288  30.287   4.441  1.00 62.09           O  
-ATOM   1660  OE2 GLU C  15      35.144  31.442   4.785  1.00 66.92           O  
-ATOM   1661  N   VAL C  16      34.131  31.457  10.616  1.00 32.57           N  
-ATOM   1662  CA  VAL C  16      34.345  32.330  11.788  1.00 33.21           C  
-ATOM   1663  C   VAL C  16      34.914  31.569  12.936  1.00 33.11           C  
-ATOM   1664  O   VAL C  16      35.852  31.949  13.633  1.00 35.82           O  
-ATOM   1665  CB  VAL C  16      33.020  33.098  12.073  1.00 41.09           C  
-ATOM   1666  CG1 VAL C  16      33.150  33.847  13.389  1.00 31.60           C  
-ATOM   1667  CG2 VAL C  16      32.749  34.081  10.909  1.00 29.22           C  
-ATOM   1668  N   ARG C  17      34.303  30.373  13.198  1.00 33.80           N  
-ATOM   1669  CA  ARG C  17      34.762  29.663  14.383  1.00 38.78           C  
-ATOM   1670  C   ARG C  17      36.192  29.208  14.169  1.00 38.41           C  
-ATOM   1671  O   ARG C  17      36.917  29.263  15.145  1.00 36.10           O  
-ATOM   1672  CB  ARG C  17      33.788  28.528  14.724  1.00 45.55           C  
-ATOM   1673  CG  ARG C  17      34.396  27.320  15.347  1.00 44.17           C  
-ATOM   1674  CD  ARG C  17      33.399  26.177  15.564  1.00 38.11           C  
-ATOM   1675  NE  ARG C  17      34.029  25.299  16.609  1.00 39.96           N  
-ATOM   1676  CZ  ARG C  17      33.686  24.020  16.711  1.00 41.87           C  
-ATOM   1677  NH1 ARG C  17      32.797  23.580  15.801  1.00 35.01           N  
-ATOM   1678  NH2 ARG C  17      34.221  23.230  17.619  1.00 35.15           N  
-ATOM   1679  N   GLU C  18      36.568  28.881  12.933  1.00 41.21           N  
-ATOM   1680  CA  GLU C  18      37.956  28.461  12.655  1.00 41.99           C  
-ATOM   1681  C   GLU C  18      38.953  29.585  12.867  1.00 39.74           C  
-ATOM   1682  O   GLU C  18      39.935  29.535  13.642  1.00 38.88           O  
-ATOM   1683  CB  GLU C  18      37.998  27.899  11.210  1.00 38.91           C  
-ATOM   1684  CG  GLU C  18      39.399  27.536  10.734  1.00 60.78           C  
-ATOM   1685  CD  GLU C  18      39.984  26.412  11.586  1.00 77.90           C  
-ATOM   1686  OE1 GLU C  18      41.221  26.373  11.779  1.00 81.38           O  
-ATOM   1687  OE2 GLU C  18      39.185  25.566  12.071  1.00 83.04           O  
-ATOM   1688  N   SER C  19      38.612  30.778  12.361  1.00 42.26           N  
-ATOM   1689  CA  SER C  19      39.567  31.892  12.579  1.00 44.94           C  
-ATOM   1690  C   SER C  19      39.641  32.276  14.047  1.00 43.55           C  
-ATOM   1691  O   SER C  19      40.717  32.599  14.577  1.00 43.59           O  
-ATOM   1692  CB  SER C  19      39.136  33.047  11.685  1.00 40.90           C  
-ATOM   1693  OG  SER C  19      39.698  34.214  12.267  1.00 59.83           O  
-ATOM   1694  N   LEU C  20      38.523  32.196  14.789  1.00 39.92           N  
-ATOM   1695  CA  LEU C  20      38.637  32.500  16.242  1.00 42.49           C  
-ATOM   1696  C   LEU C  20      39.594  31.546  16.948  1.00 40.91           C  
-ATOM   1697  O   LEU C  20      40.380  31.859  17.846  1.00 40.77           O  
-ATOM   1698  CB  LEU C  20      37.244  32.388  16.888  1.00 39.20           C  
-ATOM   1699  CG  LEU C  20      36.502  33.619  17.392  1.00 53.24           C  
-ATOM   1700  CD1 LEU C  20      37.290  34.924  17.439  1.00 45.33           C  
-ATOM   1701  CD2 LEU C  20      35.133  33.866  16.782  1.00 35.28           C  
-ATOM   1702  N   ALA C  21      39.423  30.259  16.628  1.00 41.26           N  
-ATOM   1703  CA  ALA C  21      40.159  29.147  17.181  1.00 48.32           C  
-ATOM   1704  C   ALA C  21      41.674  29.305  16.921  1.00 52.26           C  
-ATOM   1705  O   ALA C  21      42.473  28.960  17.788  1.00 53.50           O  
-ATOM   1706  CB  ALA C  21      39.768  27.815  16.583  1.00 43.10           C  
-ATOM   1707  N   GLU C  22      42.023  29.915  15.800  1.00 52.42           N  
-ATOM   1708  CA  GLU C  22      43.409  30.119  15.461  1.00 58.56           C  
-ATOM   1709  C   GLU C  22      44.049  31.208  16.316  1.00 58.43           C  
-ATOM   1710  O   GLU C  22      45.264  31.171  16.440  1.00 59.49           O  
-ATOM   1711  CB  GLU C  22      43.641  30.436  13.978  1.00 59.29           C  
-ATOM   1712  CG  GLU C  22      45.047  29.941  13.606  1.00 80.78           C  
-ATOM   1713  CD  GLU C  22      45.152  28.433  13.807  1.00 82.80           C  
-ATOM   1714  OE1 GLU C  22      44.139  27.756  13.503  1.00 90.29           O  
-ATOM   1715  OE2 GLU C  22      46.203  27.947  14.265  1.00 81.58           O  
-ATOM   1716  N   VAL C  23      43.269  32.101  16.924  1.00 55.07           N  
-ATOM   1717  CA  VAL C  23      43.877  33.049  17.862  1.00 52.41           C  
-ATOM   1718  C   VAL C  23      43.617  32.604  19.296  1.00 48.15           C  
-ATOM   1719  O   VAL C  23      43.681  33.367  20.228  1.00 51.89           O  
-ATOM   1720  CB  VAL C  23      43.427  34.485  17.605  1.00 53.30           C  
-ATOM   1721  CG1 VAL C  23      43.964  34.976  16.256  1.00 49.47           C  
-ATOM   1722  CG2 VAL C  23      41.909  34.575  17.644  1.00 56.09           C  
-ATOM   1723  N   GLY C  24      43.203  31.369  19.501  1.00 48.05           N  
-ATOM   1724  CA  GLY C  24      42.930  30.807  20.786  1.00 48.18           C  
-ATOM   1725  C   GLY C  24      41.582  31.214  21.341  1.00 43.67           C  
-ATOM   1726  O   GLY C  24      41.519  31.138  22.553  1.00 46.85           O  
-ATOM   1727  N   VAL C  25      40.608  31.724  20.624  1.00 46.58           N  
-ATOM   1728  CA  VAL C  25      39.345  32.032  21.330  1.00 47.89           C  
-ATOM   1729  C   VAL C  25      38.327  30.915  21.051  1.00 44.17           C  
-ATOM   1730  O   VAL C  25      37.984  30.641  19.900  1.00 39.78           O  
-ATOM   1731  CB  VAL C  25      38.826  33.463  21.142  1.00 47.38           C  
-ATOM   1732  CG1 VAL C  25      39.266  34.014  19.794  1.00 61.05           C  
-ATOM   1733  CG2 VAL C  25      37.301  33.580  21.281  1.00 44.86           C  
-ATOM   1734  N   THR C  26      37.953  30.188  22.108  1.00 39.96           N  
-ATOM   1735  CA  THR C  26      36.878  29.196  21.926  1.00 44.04           C  
-ATOM   1736  C   THR C  26      35.839  29.527  22.996  1.00 47.54           C  
-ATOM   1737  O   THR C  26      35.942  30.608  23.639  1.00 51.74           O  
-ATOM   1738  CB  THR C  26      37.346  27.744  21.970  1.00 45.60           C  
-ATOM   1739  OG1 THR C  26      37.995  27.621  23.248  1.00 47.86           O  
-ATOM   1740  CG2 THR C  26      38.336  27.352  20.890  1.00 53.62           C  
-ATOM   1741  N   GLY C  27      34.927  28.615  23.305  1.00 39.73           N  
-ATOM   1742  CA  GLY C  27      33.880  28.933  24.277  1.00 35.32           C  
-ATOM   1743  C   GLY C  27      32.831  29.822  23.592  1.00 34.09           C  
-ATOM   1744  O   GLY C  27      32.188  30.614  24.298  1.00 36.36           O  
-ATOM   1745  N   LEU C  28      32.488  29.571  22.332  1.00 31.39           N  
-ATOM   1746  CA  LEU C  28      31.451  30.395  21.676  1.00 31.09           C  
-ATOM   1747  C   LEU C  28      30.044  29.931  22.082  1.00 29.36           C  
-ATOM   1748  O   LEU C  28      29.834  28.717  22.268  1.00 26.39           O  
-ATOM   1749  CB  LEU C  28      31.525  30.107  20.164  1.00 38.09           C  
-ATOM   1750  CG  LEU C  28      32.462  30.988  19.332  1.00 52.17           C  
-ATOM   1751  CD1 LEU C  28      33.802  31.109  19.980  1.00 39.51           C  
-ATOM   1752  CD2 LEU C  28      32.729  30.444  17.933  1.00 41.17           C  
-ATOM   1753  N   THR C  29      29.061  30.811  22.034  1.00 24.66           N  
-ATOM   1754  CA  THR C  29      27.681  30.439  22.155  1.00 33.11           C  
-ATOM   1755  C   THR C  29      26.986  30.848  20.861  1.00 30.23           C  
-ATOM   1756  O   THR C  29      27.268  32.002  20.483  1.00 28.30           O  
-ATOM   1757  CB  THR C  29      27.055  31.251  23.325  1.00 35.35           C  
-ATOM   1758  OG1 THR C  29      27.590  30.683  24.515  1.00 35.48           O  
-ATOM   1759  CG2 THR C  29      25.562  30.911  23.288  1.00 31.49           C  
-ATOM   1760  N   VAL C  30      26.136  30.069  20.273  1.00 30.11           N  
-ATOM   1761  CA  VAL C  30      25.531  30.475  18.975  1.00 26.67           C  
-ATOM   1762  C   VAL C  30      24.023  30.404  19.095  1.00 27.08           C  
-ATOM   1763  O   VAL C  30      23.532  29.382  19.564  1.00 22.25           O  
-ATOM   1764  CB  VAL C  30      25.908  29.428  17.884  1.00 36.47           C  
-ATOM   1765  CG1 VAL C  30      25.031  29.695  16.609  1.00 30.15           C  
-ATOM   1766  CG2 VAL C  30      27.374  29.493  17.559  1.00 31.92           C  
-ATOM   1767  N   THR C  31      23.326  31.394  18.612  1.00 22.60           N  
-ATOM   1768  CA  THR C  31      21.877  31.457  18.626  1.00 19.98           C  
-ATOM   1769  C   THR C  31      21.384  31.804  17.200  1.00 28.98           C  
-ATOM   1770  O   THR C  31      22.026  32.628  16.519  1.00 25.08           O  
-ATOM   1771  CB  THR C  31      21.480  32.702  19.492  1.00 27.43           C  
-ATOM   1772  OG1 THR C  31      22.139  32.557  20.779  1.00 29.33           O  
-ATOM   1773  CG2 THR C  31      19.987  32.726  19.714  1.00 27.39           C  
-ATOM   1774  N   GLU C  32      20.357  31.155  16.745  1.00 24.97           N  
-ATOM   1775  CA  GLU C  32      19.697  31.463  15.467  1.00 33.50           C  
-ATOM   1776  C   GLU C  32      18.726  32.607  15.724  1.00 34.76           C  
-ATOM   1777  O   GLU C  32      18.000  32.595  16.743  1.00 32.17           O  
-ATOM   1778  CB  GLU C  32      18.734  30.343  14.969  1.00 37.00           C  
-ATOM   1779  CG  GLU C  32      19.451  29.023  14.818  1.00 50.63           C  
-ATOM   1780  CD  GLU C  32      18.603  27.803  14.465  1.00 47.26           C  
-ATOM   1781  OE1 GLU C  32      19.085  26.675  14.714  1.00 55.79           O  
-ATOM   1782  OE2 GLU C  32      17.487  28.019  13.986  1.00 59.16           O  
-ATOM   1783  N   VAL C  33      18.932  33.667  14.933  1.00 29.42           N  
-ATOM   1784  CA  VAL C  33      18.134  34.861  15.134  1.00 28.99           C  
-ATOM   1785  C   VAL C  33      17.560  35.235  13.750  1.00 34.71           C  
-ATOM   1786  O   VAL C  33      18.104  34.825  12.713  1.00 35.11           O  
-ATOM   1787  CB  VAL C  33      18.953  36.037  15.719  1.00 34.51           C  
-ATOM   1788  CG1 VAL C  33      19.447  35.667  17.134  1.00 24.73           C  
-ATOM   1789  CG2 VAL C  33      20.129  36.542  14.826  1.00 26.78           C  
-ATOM   1790  N   LYS C  34      16.667  36.173  13.740  1.00 31.99           N  
-ATOM   1791  CA  LYS C  34      16.036  36.741  12.541  1.00 31.86           C  
-ATOM   1792  C   LYS C  34      16.410  38.210  12.520  1.00 32.11           C  
-ATOM   1793  O   LYS C  34      16.144  38.920  13.494  1.00 31.73           O  
-ATOM   1794  CB  LYS C  34      14.515  36.612  12.550  1.00 36.23           C  
-ATOM   1795  CG  LYS C  34      14.077  35.130  12.434  1.00 44.50           C  
-ATOM   1796  CD  LYS C  34      12.572  34.913  12.489  1.00 46.80           C  
-ATOM   1797  CE  LYS C  34      12.224  33.427  12.503  1.00 47.17           C  
-ATOM   1798  NZ  LYS C  34      10.875  33.174  13.100  1.00 63.58           N  
-ATOM   1799  N   GLY C  35      16.942  38.676  11.387  1.00 33.17           N  
-ATOM   1800  CA  GLY C  35      17.312  40.062  11.161  1.00 34.11           C  
-ATOM   1801  C   GLY C  35      16.192  40.718  10.355  1.00 44.90           C  
-ATOM   1802  O   GLY C  35      15.777  40.194   9.313  1.00 49.21           O  
-ATOM   1803  N   PHE C  36      15.601  41.800  10.822  1.00 48.27           N  
-ATOM   1804  CA  PHE C  36      14.581  42.553  10.119  1.00 51.80           C  
-ATOM   1805  C   PHE C  36      15.263  43.841   9.648  1.00 57.80           C  
-ATOM   1806  O   PHE C  36      16.016  44.356  10.447  1.00 55.33           O  
-ATOM   1807  CB  PHE C  36      13.351  43.051  10.934  1.00 38.39           C  
-ATOM   1808  CG  PHE C  36      12.508  41.830  11.230  1.00 49.72           C  
-ATOM   1809  CD1 PHE C  36      12.935  40.905  12.164  1.00 44.19           C  
-ATOM   1810  CD2 PHE C  36      11.336  41.584  10.526  1.00 47.33           C  
-ATOM   1811  CE1 PHE C  36      12.178  39.767  12.429  1.00 60.51           C  
-ATOM   1812  CE2 PHE C  36      10.576  40.466  10.784  1.00 57.53           C  
-ATOM   1813  CZ  PHE C  36      10.990  39.543  11.739  1.00 62.03           C  
-ATOM   1814  N   PRO C  57      17.416  35.028   7.957  1.00 45.57           N  
-ATOM   1815  CA  PRO C  57      17.989  34.172   8.997  1.00 38.92           C  
-ATOM   1816  C   PRO C  57      19.402  34.617   9.237  1.00 39.20           C  
-ATOM   1817  O   PRO C  57      20.147  34.961   8.283  1.00 36.03           O  
-ATOM   1818  CB  PRO C  57      17.920  32.766   8.431  1.00 43.68           C  
-ATOM   1819  CG  PRO C  57      17.656  32.899   6.967  1.00 47.77           C  
-ATOM   1820  CD  PRO C  57      17.092  34.272   6.697  1.00 46.24           C  
-ATOM   1821  N   LYS C  58      19.823  34.882  10.490  1.00 29.82           N  
-ATOM   1822  CA  LYS C  58      21.206  35.153  10.783  1.00 28.02           C  
-ATOM   1823  C   LYS C  58      21.691  34.157  11.881  1.00 29.50           C  
-ATOM   1824  O   LYS C  58      20.873  33.623  12.632  1.00 31.70           O  
-ATOM   1825  CB  LYS C  58      21.488  36.551  11.379  1.00 36.18           C  
-ATOM   1826  CG  LYS C  58      20.998  37.715  10.501  1.00 42.85           C  
-ATOM   1827  CD  LYS C  58      21.952  37.944   9.337  1.00 52.93           C  
-ATOM   1828  CE  LYS C  58      21.466  39.043   8.388  1.00 65.15           C  
-ATOM   1829  NZ  LYS C  58      21.879  38.827   6.960  1.00 58.61           N  
-ATOM   1830  N   VAL C  59      22.953  34.252  12.261  1.00 26.81           N  
-ATOM   1831  CA  VAL C  59      23.467  33.529  13.425  1.00 32.62           C  
-ATOM   1832  C   VAL C  59      24.111  34.550  14.318  1.00 31.43           C  
-ATOM   1833  O   VAL C  59      24.825  35.470  13.809  1.00 32.01           O  
-ATOM   1834  CB  VAL C  59      24.529  32.484  12.978  1.00 35.67           C  
-ATOM   1835  CG1 VAL C  59      25.486  32.018  14.025  1.00 43.75           C  
-ATOM   1836  CG2 VAL C  59      23.765  31.212  12.559  1.00 44.11           C  
-ATOM   1837  N   LYS C  60      23.774  34.543  15.591  1.00 29.55           N  
-ATOM   1838  CA  LYS C  60      24.495  35.412  16.526  1.00 25.47           C  
-ATOM   1839  C   LYS C  60      25.573  34.572  17.217  1.00 30.77           C  
-ATOM   1840  O   LYS C  60      25.287  33.468  17.727  1.00 30.42           O  
-ATOM   1841  CB  LYS C  60      23.610  36.065  17.547  1.00 30.27           C  
-ATOM   1842  CG  LYS C  60      24.349  36.541  18.794  1.00 31.91           C  
-ATOM   1843  CD  LYS C  60      23.375  36.714  19.976  1.00 32.39           C  
-ATOM   1844  CE  LYS C  60      22.625  38.019  19.747  1.00 33.94           C  
-ATOM   1845  NZ  LYS C  60      21.864  38.358  21.004  1.00 44.17           N  
-ATOM   1846  N   ILE C  61      26.762  35.203  17.389  1.00 25.14           N  
-ATOM   1847  CA  ILE C  61      27.822  34.477  18.092  1.00 30.78           C  
-ATOM   1848  C   ILE C  61      28.184  35.327  19.275  1.00 33.12           C  
-ATOM   1849  O   ILE C  61      28.301  36.561  19.193  1.00 36.67           O  
-ATOM   1850  CB  ILE C  61      29.038  34.272  17.157  1.00 43.50           C  
-ATOM   1851  CG1 ILE C  61      28.741  33.398  15.927  1.00 46.86           C  
-ATOM   1852  CG2 ILE C  61      30.168  33.649  17.936  1.00 42.57           C  
-ATOM   1853  CD1 ILE C  61      29.838  33.531  14.873  1.00 43.04           C  
-ATOM   1854  N   GLU C  62      28.390  34.716  20.451  1.00 29.57           N  
-ATOM   1855  CA  GLU C  62      28.740  35.486  21.624  1.00 37.16           C  
-ATOM   1856  C   GLU C  62      29.979  34.838  22.241  1.00 33.63           C  
-ATOM   1857  O   GLU C  62      30.062  33.603  22.312  1.00 33.83           O  
-ATOM   1858  CB  GLU C  62      27.552  35.502  22.633  1.00 34.34           C  
-ATOM   1859  CG  GLU C  62      26.338  36.199  22.038  1.00 38.95           C  
-ATOM   1860  CD  GLU C  62      25.168  36.010  22.999  1.00 48.24           C  
-ATOM   1861  OE1 GLU C  62      24.781  34.852  23.260  1.00 43.51           O  
-ATOM   1862  OE2 GLU C  62      24.631  37.022  23.493  1.00 46.58           O  
-ATOM   1863  N   VAL C  63      30.946  35.623  22.622  1.00 33.79           N  
-ATOM   1864  CA  VAL C  63      32.142  35.080  23.267  1.00 36.62           C  
-ATOM   1865  C   VAL C  63      32.636  36.092  24.307  1.00 37.66           C  
-ATOM   1866  O   VAL C  63      32.512  37.293  24.073  1.00 34.19           O  
-ATOM   1867  CB  VAL C  63      33.208  34.696  22.233  1.00 38.67           C  
-ATOM   1868  CG1 VAL C  63      33.885  35.920  21.609  1.00 39.03           C  
-ATOM   1869  CG2 VAL C  63      34.178  33.793  22.998  1.00 50.81           C  
-ATOM   1870  N   VAL C  64      32.929  35.640  25.509  1.00 34.29           N  
-ATOM   1871  CA  VAL C  64      33.420  36.477  26.590  1.00 38.15           C  
-ATOM   1872  C   VAL C  64      34.928  36.219  26.760  1.00 37.66           C  
-ATOM   1873  O   VAL C  64      35.362  35.061  26.833  1.00 33.08           O  
-ATOM   1874  CB  VAL C  64      32.661  36.228  27.911  1.00 48.52           C  
-ATOM   1875  CG1 VAL C  64      33.360  36.954  29.057  1.00 50.03           C  
-ATOM   1876  CG2 VAL C  64      31.183  36.659  27.813  1.00 42.27           C  
-ATOM   1877  N   VAL C  65      35.741  37.199  26.364  1.00 39.34           N  
-ATOM   1878  CA  VAL C  65      37.175  37.174  26.411  1.00 41.20           C  
-ATOM   1879  C   VAL C  65      37.860  38.193  27.358  1.00 43.53           C  
-ATOM   1880  O   VAL C  65      37.300  39.192  27.823  1.00 37.44           O  
-ATOM   1881  CB  VAL C  65      37.893  37.487  25.074  1.00 39.67           C  
-ATOM   1882  CG1 VAL C  65      37.728  36.335  24.101  1.00 44.48           C  
-ATOM   1883  CG2 VAL C  65      37.388  38.800  24.550  1.00 35.90           C  
-ATOM   1884  N   ASP C  66      39.145  37.854  27.533  1.00 41.84           N  
-ATOM   1885  CA  ASP C  66      40.039  38.694  28.326  1.00 47.29           C  
-ATOM   1886  C   ASP C  66      40.254  39.972  27.520  1.00 46.42           C  
-ATOM   1887  O   ASP C  66      40.454  39.950  26.293  1.00 41.36           O  
-ATOM   1888  CB  ASP C  66      41.418  38.046  28.563  1.00 49.36           C  
-ATOM   1889  CG  ASP C  66      42.169  38.728  29.706  1.00 65.07           C  
-ATOM   1890  OD1 ASP C  66      42.827  39.762  29.514  1.00 61.61           O  
-ATOM   1891  OD2 ASP C  66      42.088  38.240  30.856  1.00 67.88           O  
-ATOM   1892  N   ASP C  67      40.359  41.100  28.227  1.00 49.15           N  
-ATOM   1893  CA  ASP C  67      40.626  42.376  27.567  1.00 50.49           C  
-ATOM   1894  C   ASP C  67      41.862  42.317  26.682  1.00 48.53           C  
-ATOM   1895  O   ASP C  67      42.034  42.939  25.636  1.00 48.48           O  
-ATOM   1896  CB  ASP C  67      40.916  43.506  28.574  1.00 50.15           C  
-ATOM   1897  CG  ASP C  67      39.710  43.830  29.423  1.00 53.61           C  
-ATOM   1898  OD1 ASP C  67      38.603  43.335  29.155  1.00 51.75           O  
-ATOM   1899  OD2 ASP C  67      39.890  44.603  30.394  1.00 61.80           O  
-ATOM   1900  N   LYS C  68      42.841  41.576  27.166  1.00 51.37           N  
-ATOM   1901  CA  LYS C  68      44.098  41.388  26.425  1.00 58.39           C  
-ATOM   1902  C   LYS C  68      43.881  40.774  25.055  1.00 58.70           C  
-ATOM   1903  O   LYS C  68      44.670  41.174  24.182  1.00 56.41           O  
-ATOM   1904  CB  LYS C  68      44.995  40.687  27.421  1.00 59.54           C  
-ATOM   1905  CG  LYS C  68      46.369  40.191  27.098  1.00 72.16           C  
-ATOM   1906  CD  LYS C  68      46.874  39.274  28.219  1.00 78.92           C  
-ATOM   1907  CE  LYS C  68      45.843  38.214  28.588  1.00 83.81           C  
-ATOM   1908  NZ  LYS C  68      46.470  36.975  29.143  1.00 89.35           N  
-ATOM   1909  N   VAL C  69      42.785  40.092  24.664  1.00 57.77           N  
-ATOM   1910  CA  VAL C  69      42.612  39.589  23.309  1.00 53.51           C  
-ATOM   1911  C   VAL C  69      41.450  40.132  22.506  1.00 47.15           C  
-ATOM   1912  O   VAL C  69      41.178  39.601  21.422  1.00 45.09           O  
-ATOM   1913  CB  VAL C  69      42.446  38.048  23.174  1.00 56.84           C  
-ATOM   1914  CG1 VAL C  69      43.799  37.359  23.237  1.00 52.20           C  
-ATOM   1915  CG2 VAL C  69      41.444  37.474  24.159  1.00 40.54           C  
-ATOM   1916  N   VAL C  70      40.775  41.191  22.927  1.00 47.57           N  
-ATOM   1917  CA  VAL C  70      39.581  41.613  22.164  1.00 45.43           C  
-ATOM   1918  C   VAL C  70      39.971  42.023  20.766  1.00 45.70           C  
-ATOM   1919  O   VAL C  70      39.178  41.808  19.854  1.00 42.46           O  
-ATOM   1920  CB  VAL C  70      38.750  42.706  22.866  1.00 51.88           C  
-ATOM   1921  CG1 VAL C  70      37.855  43.516  21.944  1.00 54.46           C  
-ATOM   1922  CG2 VAL C  70      37.808  42.049  23.863  1.00 50.76           C  
-ATOM   1923  N   GLU C  71      41.147  42.655  20.609  1.00 41.59           N  
-ATOM   1924  CA  GLU C  71      41.489  43.207  19.287  1.00 46.69           C  
-ATOM   1925  C   GLU C  71      41.698  42.089  18.266  1.00 42.48           C  
-ATOM   1926  O   GLU C  71      41.142  42.169  17.202  1.00 39.03           O  
-ATOM   1927  CB  GLU C  71      42.760  44.059  19.305  1.00 56.51           C  
-ATOM   1928  CG  GLU C  71      42.713  45.375  20.023  1.00 71.12           C  
-ATOM   1929  CD  GLU C  71      41.923  45.476  21.300  1.00 80.53           C  
-ATOM   1930  OE1 GLU C  71      42.338  45.033  22.392  1.00 83.71           O  
-ATOM   1931  OE2 GLU C  71      40.794  46.039  21.240  1.00 93.69           O  
-ATOM   1932  N   GLN C  72      42.465  41.097  18.652  1.00 47.18           N  
-ATOM   1933  CA  GLN C  72      42.685  39.886  17.916  1.00 51.15           C  
-ATOM   1934  C   GLN C  72      41.373  39.189  17.576  1.00 50.02           C  
-ATOM   1935  O   GLN C  72      41.211  38.835  16.406  1.00 48.44           O  
-ATOM   1936  CB  GLN C  72      43.552  38.916  18.724  1.00 59.95           C  
-ATOM   1937  CG  GLN C  72      44.880  38.622  18.036  1.00 80.49           C  
-ATOM   1938  CD  GLN C  72      45.490  37.314  18.504  1.00 93.65           C  
-ATOM   1939  OE1 GLN C  72      45.056  36.737  19.513  1.00101.95           O  
-ATOM   1940  NE2 GLN C  72      46.504  36.821  17.790  1.00 99.50           N  
-ATOM   1941  N   ALA C  73      40.508  38.997  18.574  1.00 44.48           N  
-ATOM   1942  CA  ALA C  73      39.214  38.326  18.298  1.00 41.68           C  
-ATOM   1943  C   ALA C  73      38.364  39.145  17.337  1.00 42.47           C  
-ATOM   1944  O   ALA C  73      37.847  38.581  16.346  1.00 38.70           O  
-ATOM   1945  CB  ALA C  73      38.474  38.130  19.618  1.00 41.07           C  
-ATOM   1946  N   VAL C  74      38.347  40.493  17.492  1.00 43.26           N  
-ATOM   1947  CA  VAL C  74      37.437  41.234  16.564  1.00 45.85           C  
-ATOM   1948  C   VAL C  74      37.921  41.157  15.117  1.00 44.53           C  
-ATOM   1949  O   VAL C  74      37.243  40.943  14.109  1.00 39.38           O  
-ATOM   1950  CB  VAL C  74      37.288  42.692  17.010  1.00 47.89           C  
-ATOM   1951  CG1 VAL C  74      36.560  43.478  15.915  1.00 47.22           C  
-ATOM   1952  CG2 VAL C  74      36.577  42.822  18.346  1.00 48.82           C  
-ATOM   1953  N   ASP C  75      39.256  41.230  15.029  1.00 47.96           N  
-ATOM   1954  CA  ASP C  75      39.908  41.153  13.737  1.00 50.69           C  
-ATOM   1955  C   ASP C  75      39.766  39.802  13.059  1.00 44.37           C  
-ATOM   1956  O   ASP C  75      39.437  39.639  11.873  1.00 47.65           O  
-ATOM   1957  CB  ASP C  75      41.382  41.538  13.978  1.00 62.41           C  
-ATOM   1958  CG  ASP C  75      41.964  41.799  12.585  1.00 70.63           C  
-ATOM   1959  OD1 ASP C  75      41.566  42.847  12.024  1.00 75.66           O  
-ATOM   1960  OD2 ASP C  75      42.737  40.936  12.144  1.00 74.90           O  
-ATOM   1961  N   ALA C  76      39.900  38.744  13.830  1.00 44.09           N  
-ATOM   1962  CA  ALA C  76      39.635  37.390  13.267  1.00 46.13           C  
-ATOM   1963  C   ALA C  76      38.180  37.261  12.840  1.00 44.29           C  
-ATOM   1964  O   ALA C  76      37.926  36.745  11.749  1.00 40.89           O  
-ATOM   1965  CB  ALA C  76      40.131  36.350  14.237  1.00 43.06           C  
-ATOM   1966  N   ILE C  77      37.193  37.873  13.526  1.00 39.60           N  
-ATOM   1967  CA  ILE C  77      35.825  37.770  13.001  1.00 42.81           C  
-ATOM   1968  C   ILE C  77      35.741  38.549  11.684  1.00 46.30           C  
-ATOM   1969  O   ILE C  77      35.140  38.093  10.689  1.00 41.08           O  
-ATOM   1970  CB  ILE C  77      34.783  38.305  13.996  1.00 43.44           C  
-ATOM   1971  CG1 ILE C  77      34.622  37.391  15.201  1.00 36.75           C  
-ATOM   1972  CG2 ILE C  77      33.425  38.450  13.298  1.00 32.24           C  
-ATOM   1973  CD1 ILE C  77      34.212  38.066  16.482  1.00 43.18           C  
-ATOM   1974  N   ILE C  78      36.229  39.808  11.747  1.00 42.54           N  
-ATOM   1975  CA  ILE C  78      36.194  40.585  10.476  1.00 48.80           C  
-ATOM   1976  C   ILE C  78      36.946  39.816   9.374  1.00 49.47           C  
-ATOM   1977  O   ILE C  78      36.371  39.617   8.317  1.00 45.64           O  
-ATOM   1978  CB  ILE C  78      36.799  41.985  10.519  1.00 57.09           C  
-ATOM   1979  CG1 ILE C  78      35.942  42.960  11.343  1.00 62.01           C  
-ATOM   1980  CG2 ILE C  78      36.975  42.622   9.131  1.00 58.56           C  
-ATOM   1981  CD1 ILE C  78      36.803  44.056  11.967  1.00 56.57           C  
-ATOM   1982  N   LYS C  79      38.163  39.315   9.641  1.00 51.17           N  
-ATOM   1983  CA  LYS C  79      38.847  38.554   8.595  1.00 52.50           C  
-ATOM   1984  C   LYS C  79      37.971  37.489   7.977  1.00 53.82           C  
-ATOM   1985  O   LYS C  79      37.994  37.380   6.735  1.00 51.03           O  
-ATOM   1986  CB  LYS C  79      40.166  37.957   9.101  1.00 57.82           C  
-ATOM   1987  CG  LYS C  79      41.276  38.960   9.277  1.00 69.74           C  
-ATOM   1988  CD  LYS C  79      42.662  38.375   9.371  1.00 79.51           C  
-ATOM   1989  CE  LYS C  79      43.184  38.070  10.748  1.00 81.38           C  
-ATOM   1990  NZ  LYS C  79      42.881  36.704  11.266  1.00 81.03           N  
-ATOM   1991  N   ALA C  80      37.317  36.638   8.810  1.00 46.27           N  
-ATOM   1992  CA  ALA C  80      36.554  35.543   8.196  1.00 44.15           C  
-ATOM   1993  C   ALA C  80      35.176  35.868   7.653  1.00 44.31           C  
-ATOM   1994  O   ALA C  80      34.709  35.103   6.782  1.00 43.46           O  
-ATOM   1995  CB  ALA C  80      36.368  34.438   9.253  1.00 44.07           C  
-ATOM   1996  N   ALA C  81      34.394  36.778   8.258  1.00 41.66           N  
-ATOM   1997  CA  ALA C  81      33.001  36.879   7.744  1.00 51.85           C  
-ATOM   1998  C   ALA C  81      32.784  37.872   6.599  1.00 58.28           C  
-ATOM   1999  O   ALA C  81      31.689  37.985   6.029  1.00 59.61           O  
-ATOM   2000  CB  ALA C  81      32.093  37.285   8.894  1.00 56.42           C  
-ATOM   2001  N   ARG C  82      33.782  38.710   6.347  1.00 61.46           N  
-ATOM   2002  CA  ARG C  82      33.671  39.773   5.375  1.00 73.12           C  
-ATOM   2003  C   ARG C  82      33.628  39.130   3.987  1.00 74.97           C  
-ATOM   2004  O   ARG C  82      34.620  38.578   3.548  1.00 74.97           O  
-ATOM   2005  CB  ARG C  82      34.797  40.818   5.475  1.00 76.04           C  
-ATOM   2006  CG  ARG C  82      34.675  41.945   4.459  1.00 76.96           C  
-ATOM   2007  CD  ARG C  82      35.804  42.947   4.498  1.00 82.09           C  
-ATOM   2008  NE  ARG C  82      35.857  43.694   5.751  1.00 93.67           N  
-ATOM   2009  CZ  ARG C  82      36.662  44.722   5.991  1.00 94.02           C  
-ATOM   2010  NH1 ARG C  82      37.490  45.133   5.039  1.00101.45           N  
-ATOM   2011  NH2 ARG C  82      36.638  45.340   7.158  1.00 93.39           N  
-ATOM   2012  N   THR C  83      32.443  39.100   3.414  1.00 80.62           N  
-ATOM   2013  CA  THR C  83      32.306  38.610   2.044  1.00 86.79           C  
-ATOM   2014  C   THR C  83      32.579  39.850   1.185  1.00 91.53           C  
-ATOM   2015  O   THR C  83      33.465  39.853   0.338  1.00 94.24           O  
-ATOM   2016  CB  THR C  83      30.918  38.051   1.751  1.00 83.73           C  
-ATOM   2017  OG1 THR C  83      30.027  39.164   1.597  1.00 79.74           O  
-ATOM   2018  CG2 THR C  83      30.410  37.176   2.892  1.00 81.71           C  
-ATOM   2019  N   GLY C  84      31.940  40.953   1.571  1.00 93.56           N  
-ATOM   2020  CA  GLY C  84      32.116  42.212   0.859  1.00 96.48           C  
-ATOM   2021  C   GLY C  84      30.795  42.758   0.329  1.00 97.85           C  
-ATOM   2022  O   GLY C  84      30.698  43.962   0.076  1.00 98.55           O  
-ATOM   2023  N   LYS C  85      29.787  41.906   0.157  1.00 98.43           N  
-ATOM   2024  CA  LYS C  85      28.469  42.346  -0.289  1.00 96.56           C  
-ATOM   2025  C   LYS C  85      27.636  42.813   0.898  1.00 94.35           C  
-ATOM   2026  O   LYS C  85      28.012  42.692   2.067  1.00 94.57           O  
-ATOM   2027  CB  LYS C  85      27.765  41.250  -1.087  1.00101.49           C  
-ATOM   2028  CG  LYS C  85      28.614  40.786  -2.263  1.00110.50           C  
-ATOM   2029  CD  LYS C  85      27.828  39.857  -3.178  1.00116.04           C  
-ATOM   2030  CE  LYS C  85      28.365  39.973  -4.600  1.00117.90           C  
-ATOM   2031  NZ  LYS C  85      27.500  39.248  -5.572  1.00118.94           N  
-ATOM   2032  N   ILE C  86      26.555  43.509   0.609  1.00 90.83           N  
-ATOM   2033  CA  ILE C  86      25.647  44.100   1.588  1.00 85.62           C  
-ATOM   2034  C   ILE C  86      25.132  43.044   2.553  1.00 81.28           C  
-ATOM   2035  O   ILE C  86      24.839  41.932   2.104  1.00 80.47           O  
-ATOM   2036  CB  ILE C  86      24.553  44.877   0.838  1.00 86.89           C  
-ATOM   2037  CG1 ILE C  86      23.231  44.980   1.602  1.00 86.36           C  
-ATOM   2038  CG2 ILE C  86      24.258  44.326  -0.556  1.00 89.53           C  
-ATOM   2039  CD1 ILE C  86      23.070  46.339   2.248  1.00 87.02           C  
-ATOM   2040  N   GLY C  87      25.069  43.319   3.859  1.00 73.67           N  
-ATOM   2041  CA  GLY C  87      24.638  42.327   4.822  1.00 67.05           C  
-ATOM   2042  C   GLY C  87      25.637  41.447   5.541  1.00 62.13           C  
-ATOM   2043  O   GLY C  87      25.196  40.565   6.303  1.00 59.21           O  
-ATOM   2044  N   ASP C  88      26.953  41.649   5.492  1.00 56.14           N  
-ATOM   2045  CA  ASP C  88      27.960  40.931   6.246  1.00 55.77           C  
-ATOM   2046  C   ASP C  88      27.784  40.931   7.780  1.00 53.27           C  
-ATOM   2047  O   ASP C  88      28.392  40.134   8.524  1.00 54.71           O  
-ATOM   2048  CB  ASP C  88      29.375  41.425   5.892  1.00 49.61           C  
-ATOM   2049  CG  ASP C  88      29.942  40.928   4.580  1.00 58.37           C  
-ATOM   2050  OD1 ASP C  88      29.392  40.147   3.789  1.00 49.96           O  
-ATOM   2051  OD2 ASP C  88      31.073  41.328   4.245  1.00 62.49           O  
-ATOM   2052  N   GLY C  89      27.049  41.852   8.357  1.00 45.28           N  
-ATOM   2053  CA  GLY C  89      26.662  41.961   9.726  1.00 42.90           C  
-ATOM   2054  C   GLY C  89      27.475  42.917  10.563  1.00 43.74           C  
-ATOM   2055  O   GLY C  89      28.152  43.809  10.007  1.00 40.21           O  
-ATOM   2056  N   LYS C  90      27.269  42.867  11.868  1.00 39.64           N  
-ATOM   2057  CA  LYS C  90      28.009  43.786  12.752  1.00 41.76           C  
-ATOM   2058  C   LYS C  90      28.630  42.972  13.876  1.00 38.86           C  
-ATOM   2059  O   LYS C  90      28.048  41.921  14.207  1.00 39.82           O  
-ATOM   2060  CB  LYS C  90      27.154  44.766  13.556  1.00 38.97           C  
-ATOM   2061  CG  LYS C  90      25.945  45.282  12.811  1.00 59.01           C  
-ATOM   2062  CD  LYS C  90      26.261  46.521  12.001  1.00 58.30           C  
-ATOM   2063  CE  LYS C  90      24.950  47.095  11.426  1.00 59.90           C  
-ATOM   2064  NZ  LYS C  90      24.883  48.558  11.687  1.00 57.86           N  
-ATOM   2065  N   ILE C  91      29.465  43.645  14.593  1.00 33.65           N  
-ATOM   2066  CA  ILE C  91      30.142  43.138  15.790  1.00 34.48           C  
-ATOM   2067  C   ILE C  91      29.914  44.164  16.879  1.00 36.13           C  
-ATOM   2068  O   ILE C  91      29.921  45.373  16.560  1.00 36.33           O  
-ATOM   2069  CB  ILE C  91      31.639  42.915  15.580  1.00 40.71           C  
-ATOM   2070  CG1 ILE C  91      32.006  41.836  14.558  1.00 37.29           C  
-ATOM   2071  CG2 ILE C  91      32.376  42.574  16.880  1.00 36.52           C  
-ATOM   2072  CD1 ILE C  91      33.504  41.881  14.203  1.00 44.44           C  
-ATOM   2073  N   PHE C  92      29.718  43.757  18.131  1.00 32.58           N  
-ATOM   2074  CA  PHE C  92      29.445  44.740  19.177  1.00 32.65           C  
-ATOM   2075  C   PHE C  92      30.353  44.297  20.321  1.00 37.28           C  
-ATOM   2076  O   PHE C  92      30.556  43.080  20.411  1.00 32.97           O  
-ATOM   2077  CB  PHE C  92      28.015  44.746  19.716  1.00 41.08           C  
-ATOM   2078  CG  PHE C  92      26.897  44.774  18.749  1.00 40.49           C  
-ATOM   2079  CD1 PHE C  92      25.989  43.751  18.613  1.00 50.03           C  
-ATOM   2080  CD2 PHE C  92      26.713  45.890  17.930  1.00 51.26           C  
-ATOM   2081  CE1 PHE C  92      24.937  43.785  17.718  1.00 57.17           C  
-ATOM   2082  CE2 PHE C  92      25.682  45.956  16.999  1.00 50.50           C  
-ATOM   2083  CZ  PHE C  92      24.799  44.896  16.892  1.00 62.73           C  
-ATOM   2084  N   VAL C  93      30.783  45.233  21.159  1.00 36.08           N  
-ATOM   2085  CA  VAL C  93      31.713  44.959  22.244  1.00 36.43           C  
-ATOM   2086  C   VAL C  93      31.083  45.542  23.517  1.00 41.83           C  
-ATOM   2087  O   VAL C  93      30.637  46.696  23.450  1.00 39.96           O  
-ATOM   2088  CB  VAL C  93      33.142  45.505  22.059  1.00 36.59           C  
-ATOM   2089  CG1 VAL C  93      34.105  45.209  23.220  1.00 42.51           C  
-ATOM   2090  CG2 VAL C  93      33.787  44.848  20.831  1.00 35.31           C  
-ATOM   2091  N   GLN C  94      31.012  44.786  24.598  1.00 34.77           N  
-ATOM   2092  CA  GLN C  94      30.413  45.313  25.826  1.00 36.66           C  
-ATOM   2093  C   GLN C  94      31.267  44.825  26.991  1.00 38.59           C  
-ATOM   2094  O   GLN C  94      31.838  43.730  26.905  1.00 36.33           O  
-ATOM   2095  CB  GLN C  94      28.994  44.684  26.022  1.00 42.18           C  
-ATOM   2096  CG  GLN C  94      27.885  45.382  25.241  1.00 42.58           C  
-ATOM   2097  CD  GLN C  94      26.586  44.570  25.257  1.00 58.22           C  
-ATOM   2098  OE1 GLN C  94      26.463  43.474  24.694  1.00 50.42           O  
-ATOM   2099  NE2 GLN C  94      25.564  45.102  25.916  1.00 49.40           N  
-ATOM   2100  N   GLU C  95      31.344  45.567  28.053  1.00 39.02           N  
-ATOM   2101  CA  GLU C  95      32.035  45.137  29.244  1.00 43.08           C  
-ATOM   2102  C   GLU C  95      31.312  44.013  29.967  1.00 41.08           C  
-ATOM   2103  O   GLU C  95      30.067  44.007  30.022  1.00 43.47           O  
-ATOM   2104  CB  GLU C  95      31.956  46.310  30.242  1.00 56.01           C  
-ATOM   2105  CG  GLU C  95      33.217  47.098  30.338  1.00 65.68           C  
-ATOM   2106  CD  GLU C  95      34.490  46.340  30.593  1.00 60.89           C  
-ATOM   2107  OE1 GLU C  95      34.575  45.576  31.567  1.00 66.41           O  
-ATOM   2108  OE2 GLU C  95      35.422  46.526  29.785  1.00 65.05           O  
-ATOM   2109  N   VAL C  96      32.089  43.154  30.609  1.00 38.29           N  
-ATOM   2110  CA  VAL C  96      31.533  42.170  31.492  1.00 33.07           C  
-ATOM   2111  C   VAL C  96      32.119  42.454  32.880  1.00 39.77           C  
-ATOM   2112  O   VAL C  96      33.321  42.331  33.066  1.00 46.12           O  
-ATOM   2113  CB  VAL C  96      31.780  40.743  30.984  1.00 39.33           C  
-ATOM   2114  CG1 VAL C  96      31.200  39.750  31.969  1.00 38.45           C  
-ATOM   2115  CG2 VAL C  96      31.203  40.465  29.590  1.00 36.05           C  
-ATOM   2116  N   GLU C  97      31.345  42.717  33.901  1.00 42.92           N  
-ATOM   2117  CA  GLU C  97      31.789  42.912  35.264  1.00 44.93           C  
-ATOM   2118  C   GLU C  97      32.446  41.680  35.903  1.00 45.79           C  
-ATOM   2119  O   GLU C  97      33.618  41.723  36.333  1.00 35.84           O  
-ATOM   2120  CB  GLU C  97      30.608  43.294  36.167  1.00 50.72           C  
-ATOM   2121  CG  GLU C  97      29.895  44.538  35.710  1.00 52.81           C  
-ATOM   2122  CD  GLU C  97      29.226  45.283  36.855  1.00 64.04           C  
-ATOM   2123  OE1 GLU C  97      28.823  46.444  36.589  1.00 69.73           O  
-ATOM   2124  OE2 GLU C  97      29.094  44.762  37.987  1.00 58.13           O  
-ATOM   2125  N   GLN C  98      31.789  40.526  35.705  1.00 40.67           N  
-ATOM   2126  CA  GLN C  98      32.296  39.287  36.233  1.00 40.86           C  
-ATOM   2127  C   GLN C  98      31.923  38.017  35.455  1.00 41.99           C  
-ATOM   2128  O   GLN C  98      30.838  37.974  34.858  1.00 34.89           O  
-ATOM   2129  CB  GLN C  98      31.764  39.085  37.668  1.00 42.28           C  
-ATOM   2130  CG  GLN C  98      32.697  38.093  38.389  1.00 67.40           C  
-ATOM   2131  CD  GLN C  98      34.174  38.434  38.226  1.00 69.97           C  
-ATOM   2132  OE1 GLN C  98      34.933  37.720  37.563  1.00 60.17           O  
-ATOM   2133  NE2 GLN C  98      34.579  39.560  38.823  1.00 77.26           N  
-ATOM   2134  N   VAL C  99      32.859  37.072  35.446  1.00 37.48           N  
-ATOM   2135  CA  VAL C  99      32.688  35.783  34.823  1.00 37.85           C  
-ATOM   2136  C   VAL C  99      32.994  34.701  35.838  1.00 38.31           C  
-ATOM   2137  O   VAL C  99      34.035  34.693  36.549  1.00 38.65           O  
-ATOM   2138  CB  VAL C  99      33.593  35.637  33.573  1.00 47.03           C  
-ATOM   2139  CG1 VAL C  99      33.268  34.305  32.898  1.00 43.13           C  
-ATOM   2140  CG2 VAL C  99      33.378  36.751  32.556  1.00 39.94           C  
-ATOM   2141  N   ILE C 100      32.040  33.763  36.009  1.00 35.12           N  
-ATOM   2142  CA  ILE C 100      32.267  32.659  36.944  1.00 31.42           C  
-ATOM   2143  C   ILE C 100      32.178  31.325  36.233  1.00 36.62           C  
-ATOM   2144  O   ILE C 100      31.141  31.101  35.599  1.00 36.77           O  
-ATOM   2145  CB  ILE C 100      31.215  32.631  38.053  1.00 27.12           C  
-ATOM   2146  CG1 ILE C 100      31.231  33.851  38.985  1.00 34.88           C  
-ATOM   2147  CG2 ILE C 100      31.391  31.421  38.979  1.00 39.00           C  
-ATOM   2148  CD1 ILE C 100      30.235  34.951  38.705  1.00 43.50           C  
-ATOM   2149  N   ARG C 101      33.137  30.437  36.386  1.00 35.74           N  
-ATOM   2150  CA  ARG C 101      33.023  29.061  35.869  1.00 41.49           C  
-ATOM   2151  C   ARG C 101      32.303  28.208  36.902  1.00 42.91           C  
-ATOM   2152  O   ARG C 101      32.724  28.020  38.059  1.00 42.74           O  
-ATOM   2153  CB  ARG C 101      34.389  28.564  35.404  1.00 40.59           C  
-ATOM   2154  CG  ARG C 101      34.590  27.093  35.320  1.00 54.98           C  
-ATOM   2155  CD  ARG C 101      35.716  26.459  34.580  1.00 60.39           C  
-ATOM   2156  NE  ARG C 101      36.906  27.209  34.250  1.00 68.63           N  
-ATOM   2157  CZ  ARG C 101      37.259  27.593  33.031  1.00 74.20           C  
-ATOM   2158  NH1 ARG C 101      36.479  27.281  31.996  1.00 82.40           N  
-ATOM   2159  NH2 ARG C 101      38.378  28.275  32.840  1.00 73.92           N  
-ATOM   2160  N   ILE C 102      31.207  27.566  36.505  1.00 35.10           N  
-ATOM   2161  CA  ILE C 102      30.373  26.794  37.416  1.00 33.66           C  
-ATOM   2162  C   ILE C 102      31.047  25.596  38.093  1.00 33.95           C  
-ATOM   2163  O   ILE C 102      30.886  25.394  39.290  1.00 36.51           O  
-ATOM   2164  CB  ILE C 102      29.036  26.367  36.775  1.00 28.63           C  
-ATOM   2165  CG1 ILE C 102      28.203  27.623  36.504  1.00 35.52           C  
-ATOM   2166  CG2 ILE C 102      28.273  25.355  37.606  1.00 28.26           C  
-ATOM   2167  CD1 ILE C 102      26.866  27.462  35.782  1.00 38.26           C  
-ATOM   2168  N   ARG C 103      31.831  24.828  37.414  1.00 32.53           N  
-ATOM   2169  CA  ARG C 103      32.391  23.554  37.832  1.00 40.05           C  
-ATOM   2170  C   ARG C 103      33.340  23.740  39.026  1.00 45.45           C  
-ATOM   2171  O   ARG C 103      33.321  22.944  39.969  1.00 44.04           O  
-ATOM   2172  CB  ARG C 103      33.090  23.049  36.578  1.00 33.86           C  
-ATOM   2173  CG  ARG C 103      34.093  21.974  36.515  1.00 44.90           C  
-ATOM   2174  CD  ARG C 103      34.899  21.847  35.216  1.00 57.80           C  
-ATOM   2175  NE  ARG C 103      36.179  21.248  35.625  1.00 75.12           N  
-ATOM   2176  CZ  ARG C 103      37.328  21.910  35.726  1.00 83.56           C  
-ATOM   2177  NH1 ARG C 103      37.471  23.199  35.419  1.00 85.24           N  
-ATOM   2178  NH2 ARG C 103      38.415  21.260  36.137  1.00 89.31           N  
-ATOM   2179  N   THR C 104      34.115  24.807  38.972  1.00 39.51           N  
-ATOM   2180  CA  THR C 104      35.161  25.109  39.924  1.00 48.57           C  
-ATOM   2181  C   THR C 104      34.925  26.348  40.746  1.00 49.11           C  
-ATOM   2182  O   THR C 104      35.617  26.530  41.752  1.00 49.91           O  
-ATOM   2183  CB  THR C 104      36.515  25.415  39.228  1.00 45.14           C  
-ATOM   2184  OG1 THR C 104      36.347  26.582  38.423  1.00 50.20           O  
-ATOM   2185  CG2 THR C 104      36.949  24.287  38.310  1.00 42.73           C  
-ATOM   2186  N   GLY C 105      34.102  27.284  40.269  1.00 46.23           N  
-ATOM   2187  CA  GLY C 105      33.918  28.504  41.053  1.00 41.37           C  
-ATOM   2188  C   GLY C 105      35.061  29.480  40.827  1.00 46.20           C  
-ATOM   2189  O   GLY C 105      35.072  30.576  41.409  1.00 45.13           O  
-ATOM   2190  N   GLU C 106      35.995  29.167  39.930  1.00 49.94           N  
-ATOM   2191  CA  GLU C 106      36.959  30.155  39.469  1.00 51.24           C  
-ATOM   2192  C   GLU C 106      36.179  31.380  38.961  1.00 55.69           C  
-ATOM   2193  O   GLU C 106      35.064  31.264  38.410  1.00 51.66           O  
-ATOM   2194  CB  GLU C 106      37.816  29.630  38.331  1.00 43.85           C  
-ATOM   2195  CG  GLU C 106      38.896  28.636  38.768  1.00 56.82           C  
-ATOM   2196  CD  GLU C 106      39.365  27.861  37.552  1.00 61.88           C  
-ATOM   2197  OE1 GLU C 106      38.592  26.959  37.152  1.00 60.00           O  
-ATOM   2198  OE2 GLU C 106      40.461  28.194  37.054  1.00 65.87           O  
-ATOM   2199  N   THR C 107      36.824  32.526  39.069  1.00 55.75           N  
-ATOM   2200  CA  THR C 107      36.200  33.827  38.831  1.00 59.46           C  
-ATOM   2201  C   THR C 107      37.072  34.629  37.903  1.00 64.04           C  
-ATOM   2202  O   THR C 107      38.223  34.226  37.650  1.00 69.25           O  
-ATOM   2203  CB  THR C 107      36.022  34.401  40.249  1.00 65.16           C  
-ATOM   2204  OG1 THR C 107      34.696  34.907  40.458  1.00 73.23           O  
-ATOM   2205  CG2 THR C 107      37.043  35.474  40.575  1.00 63.58           C  
-ATOM   2206  N   GLY C 108      36.604  35.698  37.310  1.00 63.62           N  
-ATOM   2207  CA  GLY C 108      37.353  36.531  36.400  1.00 66.40           C  
-ATOM   2208  C   GLY C 108      38.162  35.878  35.313  1.00 67.21           C  
-ATOM   2209  O   GLY C 108      37.813  34.835  34.766  1.00 62.74           O  
-ATOM   2210  N   PRO C 109      39.300  36.494  34.953  1.00 71.61           N  
-ATOM   2211  CA  PRO C 109      40.186  36.063  33.887  1.00 72.41           C  
-ATOM   2212  C   PRO C 109      40.463  34.590  33.747  1.00 71.65           C  
-ATOM   2213  O   PRO C 109      40.480  34.098  32.628  1.00 72.14           O  
-ATOM   2214  CB  PRO C 109      41.491  36.833  34.160  1.00 73.63           C  
-ATOM   2215  CG  PRO C 109      41.022  38.112  34.771  1.00 73.01           C  
-ATOM   2216  CD  PRO C 109      39.808  37.746  35.585  1.00 73.42           C  
-ATOM   2217  N   ASP C 110      40.613  33.799  34.809  1.00 74.34           N  
-ATOM   2218  CA  ASP C 110      40.813  32.365  34.720  1.00 75.09           C  
-ATOM   2219  C   ASP C 110      39.504  31.583  34.577  1.00 72.60           C  
-ATOM   2220  O   ASP C 110      39.521  30.343  34.597  1.00 71.63           O  
-ATOM   2221  CB  ASP C 110      41.651  31.784  35.851  1.00 87.85           C  
-ATOM   2222  CG  ASP C 110      41.831  32.649  37.070  1.00 96.28           C  
-ATOM   2223  OD1 ASP C 110      41.071  33.614  37.294  1.00106.01           O  
-ATOM   2224  OD2 ASP C 110      42.762  32.373  37.857  1.00 95.41           O  
-ATOM   2225  N   ALA C 111      38.383  32.285  34.446  1.00 65.81           N  
-ATOM   2226  CA  ALA C 111      37.102  31.681  34.145  1.00 60.99           C  
-ATOM   2227  C   ALA C 111      36.896  31.633  32.629  1.00 66.05           C  
-ATOM   2228  O   ALA C 111      36.061  30.868  32.154  1.00 64.96           O  
-ATOM   2229  CB  ALA C 111      35.969  32.441  34.821  1.00 47.42           C  
-ATOM   2230  N   VAL C 112      37.628  32.420  31.839  1.00 70.58           N  
-ATOM   2231  CA  VAL C 112      37.446  32.430  30.396  1.00 78.10           C  
-ATOM   2232  C   VAL C 112      37.467  31.024  29.791  1.00 79.82           C  
-ATOM   2233  O   VAL C 112      36.740  30.816  28.791  1.00 81.31           O  
-ATOM   2234  CB  VAL C 112      38.500  33.284  29.658  1.00 79.72           C  
-ATOM   2235  CG1 VAL C 112      38.479  34.682  30.247  1.00 78.30           C  
-ATOM   2236  CG2 VAL C 112      39.871  32.630  29.764  1.00 85.58           C  
-TER    2237      VAL C 112                                                      
-ATOM   2238  N   MET D   1      68.346  33.483  58.347  1.00 32.30           N  
-ATOM   2239  CA  MET D   1      67.140  33.168  57.583  1.00 36.65           C  
-ATOM   2240  C   MET D   1      66.969  34.104  56.361  1.00 34.63           C  
-ATOM   2241  O   MET D   1      67.355  35.271  56.430  1.00 32.50           O  
-ATOM   2242  CB  MET D   1      65.900  33.271  58.459  1.00 39.52           C  
-ATOM   2243  CG  MET D   1      65.717  32.122  59.439  1.00 50.05           C  
-ATOM   2244  SD  MET D   1      66.595  32.349  60.986  1.00 49.67           S  
-ATOM   2245  CE  MET D   1      65.888  33.894  61.553  1.00 30.82           C  
-ATOM   2246  N   LYS D   2      66.384  33.599  55.274  1.00 32.47           N  
-ATOM   2247  CA  LYS D   2      66.178  34.474  54.134  1.00 35.56           C  
-ATOM   2248  C   LYS D   2      64.743  34.540  53.703  1.00 29.10           C  
-ATOM   2249  O   LYS D   2      64.001  33.565  53.863  1.00 31.53           O  
-ATOM   2250  CB  LYS D   2      66.975  34.012  52.911  1.00 31.02           C  
-ATOM   2251  CG  LYS D   2      68.446  33.694  53.212  1.00 28.30           C  
-ATOM   2252  CD  LYS D   2      69.260  34.955  53.507  1.00 35.88           C  
-ATOM   2253  CE  LYS D   2      70.768  34.694  53.574  1.00 31.84           C  
-ATOM   2254  NZ  LYS D   2      71.508  35.847  54.145  1.00 41.48           N  
-ATOM   2255  N   GLN D   3      64.353  35.688  53.138  1.00 30.26           N  
-ATOM   2256  CA  GLN D   3      63.040  35.734  52.534  1.00 30.38           C  
-ATOM   2257  C   GLN D   3      63.248  35.538  51.041  1.00 35.00           C  
-ATOM   2258  O   GLN D   3      64.043  36.255  50.417  1.00 30.55           O  
-ATOM   2259  CB  GLN D   3      62.298  37.018  52.784  1.00 23.71           C  
-ATOM   2260  CG  GLN D   3      60.998  37.039  52.023  1.00 27.83           C  
-ATOM   2261  CD  GLN D   3      60.113  38.170  52.477  1.00 44.33           C  
-ATOM   2262  OE1 GLN D   3      59.064  37.949  53.086  1.00 51.86           O  
-ATOM   2263  NE2 GLN D   3      60.323  39.475  52.292  1.00 51.16           N  
-ATOM   2264  N   VAL D   4      62.559  34.574  50.484  1.00 36.99           N  
-ATOM   2265  CA  VAL D   4      62.620  34.365  49.043  1.00 30.69           C  
-ATOM   2266  C   VAL D   4      61.292  34.882  48.470  1.00 33.45           C  
-ATOM   2267  O   VAL D   4      60.240  34.449  48.922  1.00 31.60           O  
-ATOM   2268  CB  VAL D   4      62.832  32.899  48.679  1.00 32.85           C  
-ATOM   2269  CG1 VAL D   4      62.750  32.709  47.168  1.00 33.98           C  
-ATOM   2270  CG2 VAL D   4      64.172  32.400  49.209  1.00 36.29           C  
-ATOM   2271  N   THR D   5      61.325  35.802  47.506  1.00 26.43           N  
-ATOM   2272  CA  THR D   5      60.109  36.385  46.912  1.00 33.25           C  
-ATOM   2273  C   THR D   5      60.045  36.138  45.400  1.00 31.31           C  
-ATOM   2274  O   THR D   5      61.042  36.386  44.727  1.00 30.95           O  
-ATOM   2275  CB  THR D   5      60.080  37.922  47.041  1.00 36.54           C  
-ATOM   2276  OG1 THR D   5      60.065  38.294  48.413  1.00 37.33           O  
-ATOM   2277  CG2 THR D   5      58.855  38.467  46.335  1.00 32.67           C  
-ATOM   2278  N   ALA D   6      58.944  35.682  44.846  1.00 34.08           N  
-ATOM   2279  CA  ALA D   6      58.904  35.491  43.391  1.00 36.37           C  
-ATOM   2280  C   ALA D   6      57.683  36.131  42.787  1.00 36.65           C  
-ATOM   2281  O   ALA D   6      56.588  35.956  43.307  1.00 32.93           O  
-ATOM   2282  CB  ALA D   6      58.932  34.013  43.043  1.00 33.08           C  
-ATOM   2283  N   ILE D   7      57.810  36.881  41.679  1.00 31.96           N  
-ATOM   2284  CA  ILE D   7      56.671  37.469  40.974  1.00 33.23           C  
-ATOM   2285  C   ILE D   7      56.455  36.647  39.712  1.00 38.17           C  
-ATOM   2286  O   ILE D   7      57.206  36.791  38.747  1.00 36.01           O  
-ATOM   2287  CB  ILE D   7      56.993  38.938  40.558  1.00 32.87           C  
-ATOM   2288  CG1 ILE D   7      57.454  39.789  41.759  1.00 37.40           C  
-ATOM   2289  CG2 ILE D   7      55.796  39.571  39.876  1.00 31.60           C  
-ATOM   2290  CD1 ILE D   7      56.332  40.163  42.700  1.00 34.26           C  
-ATOM   2291  N   ILE D   8      55.456  35.790  39.695  1.00 32.66           N  
-ATOM   2292  CA  ILE D   8      55.260  34.940  38.515  1.00 32.53           C  
-ATOM   2293  C   ILE D   8      53.936  35.160  37.856  1.00 34.47           C  
-ATOM   2294  O   ILE D   8      53.140  35.951  38.343  1.00 32.08           O  
-ATOM   2295  CB  ILE D   8      55.295  33.457  38.959  1.00 40.44           C  
-ATOM   2296  CG1 ILE D   8      54.268  33.161  40.054  1.00 30.95           C  
-ATOM   2297  CG2 ILE D   8      56.680  33.075  39.440  1.00 42.13           C  
-ATOM   2298  CD1 ILE D   8      53.838  31.712  40.102  1.00 40.04           C  
-ATOM   2299  N   LYS D   9      53.678  34.472  36.728  1.00 35.70           N  
-ATOM   2300  CA  LYS D   9      52.377  34.539  36.015  1.00 33.02           C  
-ATOM   2301  C   LYS D   9      51.404  33.663  36.821  1.00 32.70           C  
-ATOM   2302  O   LYS D   9      51.795  32.620  37.358  1.00 32.67           O  
-ATOM   2303  CB  LYS D   9      52.498  34.031  34.553  1.00 38.87           C  
-ATOM   2304  CG  LYS D   9      53.082  35.026  33.563  1.00 44.45           C  
-ATOM   2305  CD  LYS D   9      54.145  34.368  32.696  1.00 48.35           C  
-ATOM   2306  CE  LYS D   9      54.353  35.113  31.381  1.00 43.69           C  
-ATOM   2307  NZ  LYS D   9      55.631  34.738  30.704  1.00 38.64           N  
-ATOM   2308  N   PRO D  10      50.124  34.075  36.915  1.00 35.57           N  
-ATOM   2309  CA  PRO D  10      49.134  33.354  37.734  1.00 38.64           C  
-ATOM   2310  C   PRO D  10      49.006  31.867  37.482  1.00 44.68           C  
-ATOM   2311  O   PRO D  10      48.865  31.062  38.411  1.00 40.66           O  
-ATOM   2312  CB  PRO D  10      47.842  34.124  37.530  1.00 38.38           C  
-ATOM   2313  CG  PRO D  10      48.360  35.521  37.511  1.00 43.67           C  
-ATOM   2314  CD  PRO D  10      49.803  35.511  37.069  1.00 31.67           C  
-ATOM   2315  N   PHE D  11      49.019  31.506  36.191  1.00 43.49           N  
-ATOM   2316  CA  PHE D  11      48.764  30.126  35.845  1.00 45.07           C  
-ATOM   2317  C   PHE D  11      49.875  29.156  36.308  1.00 39.08           C  
-ATOM   2318  O   PHE D  11      49.593  27.973  36.431  1.00 46.84           O  
-ATOM   2319  CB  PHE D  11      48.351  29.957  34.378  1.00 52.71           C  
-ATOM   2320  CG  PHE D  11      49.381  30.436  33.451  1.00 50.45           C  
-ATOM   2321  CD1 PHE D  11      50.560  29.731  33.307  1.00 51.35           C  
-ATOM   2322  CD2 PHE D  11      49.187  31.604  32.726  1.00 40.67           C  
-ATOM   2323  CE1 PHE D  11      51.543  30.195  32.450  1.00 60.40           C  
-ATOM   2324  CE2 PHE D  11      50.176  32.051  31.863  1.00 57.43           C  
-ATOM   2325  CZ  PHE D  11      51.359  31.355  31.722  1.00 46.00           C  
-ATOM   2326  N   LYS D  12      51.109  29.602  36.558  1.00 36.68           N  
-ATOM   2327  CA  LYS D  12      52.116  28.826  37.168  1.00 36.51           C  
-ATOM   2328  C   LYS D  12      52.012  28.588  38.694  1.00 35.39           C  
-ATOM   2329  O   LYS D  12      52.948  27.969  39.232  1.00 36.12           O  
-ATOM   2330  CB  LYS D  12      53.503  29.503  36.977  1.00 41.53           C  
-ATOM   2331  CG  LYS D  12      53.880  29.473  35.481  1.00 47.67           C  
-ATOM   2332  CD  LYS D  12      53.926  28.033  35.008  1.00 51.57           C  
-ATOM   2333  CE  LYS D  12      54.855  27.773  33.836  1.00 61.36           C  
-ATOM   2334  NZ  LYS D  12      54.631  26.361  33.355  1.00 62.34           N  
-ATOM   2335  N   LEU D  13      51.012  29.022  39.411  1.00 39.55           N  
-ATOM   2336  CA  LEU D  13      51.142  28.944  40.902  1.00 42.44           C  
-ATOM   2337  C   LEU D  13      51.120  27.499  41.434  1.00 37.97           C  
-ATOM   2338  O   LEU D  13      52.075  27.092  42.126  1.00 32.11           O  
-ATOM   2339  CB  LEU D  13      50.057  29.675  41.600  1.00 36.62           C  
-ATOM   2340  CG  LEU D  13      50.207  30.374  42.974  1.00 46.95           C  
-ATOM   2341  CD1 LEU D  13      49.007  30.026  43.802  1.00 43.58           C  
-ATOM   2342  CD2 LEU D  13      51.486  30.306  43.726  1.00 39.01           C  
-ATOM   2343  N   ASP D  14      50.180  26.709  40.922  1.00 39.78           N  
-ATOM   2344  CA  ASP D  14      50.123  25.304  41.405  1.00 44.22           C  
-ATOM   2345  C   ASP D  14      51.437  24.598  41.266  1.00 44.51           C  
-ATOM   2346  O   ASP D  14      51.999  23.955  42.176  1.00 47.26           O  
-ATOM   2347  CB  ASP D  14      49.015  24.509  40.701  1.00 53.76           C  
-ATOM   2348  CG  ASP D  14      47.726  24.789  41.467  1.00 68.38           C  
-ATOM   2349  OD1 ASP D  14      47.711  24.431  42.673  1.00 83.03           O  
-ATOM   2350  OD2 ASP D  14      46.800  25.360  40.857  1.00 77.31           O  
-ATOM   2351  N   GLU D  15      52.005  24.765  40.067  1.00 43.80           N  
-ATOM   2352  CA  GLU D  15      53.292  24.154  39.758  1.00 35.84           C  
-ATOM   2353  C   GLU D  15      54.404  24.568  40.649  1.00 37.96           C  
-ATOM   2354  O   GLU D  15      55.204  23.744  41.084  1.00 37.27           O  
-ATOM   2355  CB  GLU D  15      53.681  24.517  38.305  1.00 49.14           C  
-ATOM   2356  CG  GLU D  15      54.629  23.606  37.590  1.00 64.44           C  
-ATOM   2357  CD  GLU D  15      54.709  23.764  36.075  1.00 73.50           C  
-ATOM   2358  OE1 GLU D  15      53.677  23.929  35.375  1.00 67.87           O  
-ATOM   2359  OE2 GLU D  15      55.842  23.722  35.542  1.00 72.05           O  
-ATOM   2360  N   VAL D  16      54.546  25.901  40.855  1.00 36.80           N  
-ATOM   2361  CA  VAL D  16      55.657  26.315  41.733  1.00 39.05           C  
-ATOM   2362  C   VAL D  16      55.460  25.763  43.145  1.00 37.49           C  
-ATOM   2363  O   VAL D  16      56.401  25.498  43.875  1.00 38.13           O  
-ATOM   2364  CB  VAL D  16      55.607  27.867  41.757  1.00 44.02           C  
-ATOM   2365  CG1 VAL D  16      56.516  28.426  42.820  1.00 43.56           C  
-ATOM   2366  CG2 VAL D  16      55.988  28.392  40.372  1.00 38.87           C  
-ATOM   2367  N   ARG D  17      54.231  25.805  43.626  1.00 41.88           N  
-ATOM   2368  CA  ARG D  17      53.877  25.321  44.946  1.00 45.83           C  
-ATOM   2369  C   ARG D  17      54.290  23.853  45.101  1.00 46.41           C  
-ATOM   2370  O   ARG D  17      54.886  23.527  46.111  1.00 47.17           O  
-ATOM   2371  CB  ARG D  17      52.373  25.515  45.157  1.00 46.36           C  
-ATOM   2372  CG  ARG D  17      51.654  24.451  45.908  1.00 65.30           C  
-ATOM   2373  CD  ARG D  17      51.349  24.664  47.370  1.00 62.00           C  
-ATOM   2374  NE  ARG D  17      50.040  24.011  47.538  1.00 80.10           N  
-ATOM   2375  CZ  ARG D  17      49.336  23.879  48.646  1.00 86.13           C  
-ATOM   2376  NH1 ARG D  17      49.809  24.356  49.790  1.00 91.09           N  
-ATOM   2377  NH2 ARG D  17      48.159  23.254  48.596  1.00 91.04           N  
-ATOM   2378  N   GLU D  18      53.933  22.986  44.174  1.00 52.08           N  
-ATOM   2379  CA  GLU D  18      54.281  21.569  44.172  1.00 53.91           C  
-ATOM   2380  C   GLU D  18      55.769  21.332  44.000  1.00 54.01           C  
-ATOM   2381  O   GLU D  18      56.432  20.650  44.804  1.00 53.95           O  
-ATOM   2382  CB  GLU D  18      53.511  20.818  43.078  1.00 72.37           C  
-ATOM   2383  CG  GLU D  18      53.072  19.418  43.466  1.00 88.63           C  
-ATOM   2384  CD  GLU D  18      54.094  18.307  43.401  1.00 95.08           C  
-ATOM   2385  OE1 GLU D  18      54.623  17.966  42.313  1.00 97.59           O  
-ATOM   2386  OE2 GLU D  18      54.402  17.703  44.460  1.00 97.83           O  
-ATOM   2387  N   SER D  19      56.406  22.117  43.122  1.00 49.20           N  
-ATOM   2388  CA  SER D  19      57.868  21.991  43.030  1.00 48.19           C  
-ATOM   2389  C   SER D  19      58.546  22.404  44.321  1.00 50.86           C  
-ATOM   2390  O   SER D  19      59.597  21.838  44.671  1.00 46.29           O  
-ATOM   2391  CB  SER D  19      58.308  22.767  41.778  1.00 42.15           C  
-ATOM   2392  OG  SER D  19      59.696  23.043  41.831  1.00 59.76           O  
-ATOM   2393  N   LEU D  20      58.110  23.506  44.994  1.00 47.15           N  
-ATOM   2394  CA  LEU D  20      58.735  23.892  46.255  1.00 45.09           C  
-ATOM   2395  C   LEU D  20      58.414  22.837  47.360  1.00 43.44           C  
-ATOM   2396  O   LEU D  20      59.250  22.680  48.236  1.00 41.22           O  
-ATOM   2397  CB  LEU D  20      58.194  25.204  46.764  1.00 41.62           C  
-ATOM   2398  CG  LEU D  20      58.678  26.617  46.675  1.00 49.98           C  
-ATOM   2399  CD1 LEU D  20      60.066  26.709  46.134  1.00 36.95           C  
-ATOM   2400  CD2 LEU D  20      57.693  27.573  46.007  1.00 36.62           C  
-ATOM   2401  N   ALA D  21      57.235  22.240  47.370  1.00 43.29           N  
-ATOM   2402  CA  ALA D  21      56.871  21.232  48.362  1.00 52.62           C  
-ATOM   2403  C   ALA D  21      57.717  19.973  48.300  1.00 56.30           C  
-ATOM   2404  O   ALA D  21      58.270  19.520  49.312  1.00 56.29           O  
-ATOM   2405  CB  ALA D  21      55.398  20.843  48.379  1.00 47.98           C  
-ATOM   2406  N   GLU D  22      58.111  19.579  47.104  1.00 62.95           N  
-ATOM   2407  CA  GLU D  22      59.033  18.477  46.878  1.00 66.10           C  
-ATOM   2408  C   GLU D  22      60.428  18.746  47.420  1.00 64.42           C  
-ATOM   2409  O   GLU D  22      61.194  17.779  47.527  1.00 65.08           O  
-ATOM   2410  CB  GLU D  22      59.110  18.132  45.390  1.00 80.40           C  
-ATOM   2411  CG  GLU D  22      58.025  17.213  44.864  1.00 92.24           C  
-ATOM   2412  CD  GLU D  22      58.368  16.535  43.553  1.00100.18           C  
-ATOM   2413  OE1 GLU D  22      57.490  15.904  42.913  1.00104.77           O  
-ATOM   2414  OE2 GLU D  22      59.539  16.612  43.117  1.00107.23           O  
-ATOM   2415  N   VAL D  23      60.799  19.964  47.799  1.00 58.89           N  
-ATOM   2416  CA  VAL D  23      62.098  20.198  48.420  1.00 54.71           C  
-ATOM   2417  C   VAL D  23      61.846  20.675  49.845  1.00 56.27           C  
-ATOM   2418  O   VAL D  23      62.640  21.332  50.518  1.00 58.62           O  
-ATOM   2419  CB  VAL D  23      63.076  21.124  47.693  1.00 57.30           C  
-ATOM   2420  CG1 VAL D  23      63.443  20.506  46.333  1.00 51.69           C  
-ATOM   2421  CG2 VAL D  23      62.573  22.544  47.487  1.00 47.94           C  
-ATOM   2422  N   GLY D  24      60.653  20.333  50.342  1.00 57.64           N  
-ATOM   2423  CA  GLY D  24      60.251  20.668  51.690  1.00 56.31           C  
-ATOM   2424  C   GLY D  24      59.980  22.097  52.059  1.00 55.04           C  
-ATOM   2425  O   GLY D  24      59.974  22.413  53.257  1.00 51.56           O  
-ATOM   2426  N   VAL D  25      59.760  23.028  51.110  1.00 53.40           N  
-ATOM   2427  CA  VAL D  25      59.409  24.357  51.625  1.00 48.96           C  
-ATOM   2428  C   VAL D  25      57.919  24.449  51.349  1.00 46.86           C  
-ATOM   2429  O   VAL D  25      57.479  24.266  50.205  1.00 47.90           O  
-ATOM   2430  CB  VAL D  25      60.289  25.539  51.250  1.00 55.60           C  
-ATOM   2431  CG1 VAL D  25      61.608  25.113  50.640  1.00 45.06           C  
-ATOM   2432  CG2 VAL D  25      59.601  26.633  50.455  1.00 42.92           C  
-ATOM   2433  N   THR D  26      57.115  24.702  52.387  1.00 43.11           N  
-ATOM   2434  CA  THR D  26      55.678  24.713  52.205  1.00 42.29           C  
-ATOM   2435  C   THR D  26      54.839  25.839  52.793  1.00 42.93           C  
-ATOM   2436  O   THR D  26      53.637  25.848  52.517  1.00 52.02           O  
-ATOM   2437  CB  THR D  26      55.020  23.467  52.811  1.00 46.19           C  
-ATOM   2438  OG1 THR D  26      55.487  23.296  54.162  1.00 50.19           O  
-ATOM   2439  CG2 THR D  26      55.355  22.243  51.966  1.00 47.62           C  
-ATOM   2440  N   GLY D  27      55.303  26.775  53.555  1.00 33.57           N  
-ATOM   2441  CA  GLY D  27      54.283  27.733  53.989  1.00 35.30           C  
-ATOM   2442  C   GLY D  27      54.258  28.932  53.068  1.00 41.90           C  
-ATOM   2443  O   GLY D  27      54.885  29.923  53.411  1.00 43.13           O  
-ATOM   2444  N   LEU D  28      53.576  28.898  51.946  1.00 37.91           N  
-ATOM   2445  CA  LEU D  28      53.658  30.103  51.098  1.00 36.39           C  
-ATOM   2446  C   LEU D  28      52.602  31.197  51.388  1.00 32.18           C  
-ATOM   2447  O   LEU D  28      51.439  30.891  51.706  1.00 34.28           O  
-ATOM   2448  CB  LEU D  28      53.471  29.712  49.607  1.00 36.60           C  
-ATOM   2449  CG  LEU D  28      54.647  29.099  48.857  1.00 50.05           C  
-ATOM   2450  CD1 LEU D  28      55.331  28.028  49.707  1.00 48.53           C  
-ATOM   2451  CD2 LEU D  28      54.191  28.537  47.525  1.00 43.15           C  
-ATOM   2452  N   THR D  29      53.024  32.445  51.268  1.00 26.52           N  
-ATOM   2453  CA  THR D  29      52.050  33.526  51.293  1.00 30.48           C  
-ATOM   2454  C   THR D  29      51.894  33.993  49.838  1.00 29.40           C  
-ATOM   2455  O   THR D  29      52.920  34.378  49.234  1.00 26.17           O  
-ATOM   2456  CB  THR D  29      52.602  34.598  52.249  1.00 30.20           C  
-ATOM   2457  OG1 THR D  29      52.691  33.956  53.538  1.00 36.01           O  
-ATOM   2458  CG2 THR D  29      51.713  35.830  52.226  1.00 31.68           C  
-ATOM   2459  N   VAL D  30      50.675  34.299  49.435  1.00 27.01           N  
-ATOM   2460  CA  VAL D  30      50.442  34.690  48.075  1.00 27.93           C  
-ATOM   2461  C   VAL D  30      49.712  36.013  48.028  1.00 26.47           C  
-ATOM   2462  O   VAL D  30      48.678  36.139  48.678  1.00 25.99           O  
-ATOM   2463  CB  VAL D  30      49.644  33.548  47.363  1.00 39.41           C  
-ATOM   2464  CG1 VAL D  30      49.096  34.060  46.039  1.00 28.90           C  
-ATOM   2465  CG2 VAL D  30      50.492  32.286  47.195  1.00 37.04           C  
-ATOM   2466  N   THR D  31      50.282  36.981  47.311  1.00 24.60           N  
-ATOM   2467  CA  THR D  31      49.597  38.278  47.084  1.00 24.03           C  
-ATOM   2468  C   THR D  31      49.256  38.516  45.590  1.00 28.17           C  
-ATOM   2469  O   THR D  31      50.084  38.181  44.760  1.00 24.58           O  
-ATOM   2470  CB  THR D  31      50.522  39.446  47.499  1.00 33.96           C  
-ATOM   2471  OG1 THR D  31      50.893  39.186  48.871  1.00 27.45           O  
-ATOM   2472  CG2 THR D  31      49.865  40.846  47.492  1.00 22.09           C  
-ATOM   2473  N   GLU D  32      48.112  39.068  45.257  1.00 28.93           N  
-ATOM   2474  CA  GLU D  32      47.821  39.410  43.855  1.00 35.01           C  
-ATOM   2475  C   GLU D  32      48.331  40.818  43.576  1.00 32.67           C  
-ATOM   2476  O   GLU D  32      47.971  41.674  44.388  1.00 34.22           O  
-ATOM   2477  CB  GLU D  32      46.278  39.436  43.692  1.00 36.45           C  
-ATOM   2478  CG  GLU D  32      45.800  37.985  43.690  1.00 50.61           C  
-ATOM   2479  CD  GLU D  32      44.339  37.781  44.022  1.00 71.84           C  
-ATOM   2480  OE1 GLU D  32      43.473  38.649  43.798  1.00 69.99           O  
-ATOM   2481  OE2 GLU D  32      44.020  36.678  44.558  1.00 83.59           O  
-ATOM   2482  N   VAL D  33      49.307  40.975  42.742  1.00 28.76           N  
-ATOM   2483  CA  VAL D  33      49.855  42.294  42.370  1.00 27.07           C  
-ATOM   2484  C   VAL D  33      49.656  42.609  40.880  1.00 28.07           C  
-ATOM   2485  O   VAL D  33      49.241  41.695  40.129  1.00 32.34           O  
-ATOM   2486  CB  VAL D  33      51.370  42.281  42.641  1.00 29.75           C  
-ATOM   2487  CG1 VAL D  33      51.625  41.959  44.144  1.00 27.90           C  
-ATOM   2488  CG2 VAL D  33      52.146  41.324  41.786  1.00 31.23           C  
-ATOM   2489  N   LYS D  34      49.847  43.860  40.461  1.00 31.88           N  
-ATOM   2490  CA  LYS D  34      49.724  44.197  39.004  1.00 30.77           C  
-ATOM   2491  C   LYS D  34      51.007  44.824  38.503  1.00 32.93           C  
-ATOM   2492  O   LYS D  34      51.851  45.334  39.258  1.00 32.61           O  
-ATOM   2493  CB  LYS D  34      48.565  45.150  38.788  1.00 27.22           C  
-ATOM   2494  CG  LYS D  34      47.184  44.667  39.202  1.00 41.23           C  
-ATOM   2495  CD  LYS D  34      46.591  43.809  38.107  1.00 45.33           C  
-ATOM   2496  CE  LYS D  34      45.184  43.357  38.399  1.00 49.44           C  
-ATOM   2497  NZ  LYS D  34      44.127  44.375  38.254  1.00 61.29           N  
-ATOM   2498  N   GLY D  35      51.304  44.676  37.213  1.00 29.66           N  
-ATOM   2499  CA  GLY D  35      52.422  45.337  36.536  1.00 36.06           C  
-ATOM   2500  C   GLY D  35      51.897  45.920  35.183  1.00 35.87           C  
-ATOM   2501  O   GLY D  35      50.899  45.496  34.604  1.00 35.23           O  
-ATOM   2502  N   PHE D  36      52.507  46.998  34.755  1.00 36.11           N  
-ATOM   2503  CA  PHE D  36      52.126  47.676  33.508  1.00 38.40           C  
-ATOM   2504  C   PHE D  36      52.616  46.815  32.357  1.00 43.48           C  
-ATOM   2505  O   PHE D  36      51.829  46.510  31.455  1.00 48.62           O  
-ATOM   2506  CB  PHE D  36      52.787  49.055  33.446  1.00 41.87           C  
-ATOM   2507  CG  PHE D  36      52.184  50.002  34.459  1.00 36.01           C  
-ATOM   2508  CD1 PHE D  36      50.888  50.420  34.287  1.00 32.13           C  
-ATOM   2509  CD2 PHE D  36      52.908  50.416  35.565  1.00 40.98           C  
-ATOM   2510  CE1 PHE D  36      50.263  51.268  35.182  1.00 30.30           C  
-ATOM   2511  CE2 PHE D  36      52.278  51.298  36.452  1.00 37.61           C  
-ATOM   2512  CZ  PHE D  36      50.997  51.710  36.273  1.00 37.09           C  
-ATOM   2513  N   GLU D  50      44.687  57.990  23.720  1.00 47.42           N  
-ATOM   2514  CA  GLU D  50      46.007  58.134  23.111  1.00 40.45           C  
-ATOM   2515  C   GLU D  50      46.930  56.995  23.418  1.00 45.86           C  
-ATOM   2516  O   GLU D  50      47.690  56.570  22.531  1.00 41.02           O  
-ATOM   2517  CB  GLU D  50      46.472  59.498  23.674  1.00 48.00           C  
-ATOM   2518  CG  GLU D  50      47.723  59.975  23.027  1.00 44.97           C  
-ATOM   2519  CD  GLU D  50      48.090  61.446  23.193  1.00 39.35           C  
-ATOM   2520  OE1 GLU D  50      47.347  62.323  23.633  1.00 45.45           O  
-ATOM   2521  OE2 GLU D  50      49.263  61.677  22.854  1.00 38.32           O  
-ATOM   2522  N   TYR D  51      47.035  56.593  24.712  1.00 39.17           N  
-ATOM   2523  CA  TYR D  51      48.115  55.611  25.004  1.00 39.56           C  
-ATOM   2524  C   TYR D  51      47.538  54.690  26.081  1.00 38.97           C  
-ATOM   2525  O   TYR D  51      47.056  55.194  27.136  1.00 33.93           O  
-ATOM   2526  CB  TYR D  51      49.405  56.372  25.340  1.00 37.64           C  
-ATOM   2527  CG  TYR D  51      50.610  55.469  25.264  1.00 44.65           C  
-ATOM   2528  CD1 TYR D  51      50.928  54.661  26.349  1.00 50.96           C  
-ATOM   2529  CD2 TYR D  51      51.400  55.349  24.142  1.00 55.83           C  
-ATOM   2530  CE1 TYR D  51      51.985  53.775  26.320  1.00 58.97           C  
-ATOM   2531  CE2 TYR D  51      52.481  54.468  24.083  1.00 62.70           C  
-ATOM   2532  CZ  TYR D  51      52.767  53.682  25.191  1.00 63.73           C  
-ATOM   2533  OH  TYR D  51      53.828  52.811  25.160  1.00 66.74           O  
-ATOM   2534  N   VAL D  52      47.371  53.424  25.726  1.00 38.12           N  
-ATOM   2535  CA  VAL D  52      46.573  52.487  26.597  1.00 36.67           C  
-ATOM   2536  C   VAL D  52      47.470  51.274  26.780  1.00 40.09           C  
-ATOM   2537  O   VAL D  52      48.068  50.985  25.746  1.00 38.39           O  
-ATOM   2538  CB  VAL D  52      45.305  51.929  25.965  1.00 45.39           C  
-ATOM   2539  CG1 VAL D  52      44.693  50.763  26.765  1.00 47.34           C  
-ATOM   2540  CG2 VAL D  52      44.181  52.923  25.742  1.00 36.90           C  
-ATOM   2541  N   VAL D  53      47.719  50.784  27.999  1.00 38.78           N  
-ATOM   2542  CA  VAL D  53      48.570  49.588  28.075  1.00 36.78           C  
-ATOM   2543  C   VAL D  53      47.853  48.486  28.894  1.00 35.02           C  
-ATOM   2544  O   VAL D  53      46.778  48.657  29.443  1.00 37.53           O  
-ATOM   2545  CB  VAL D  53      49.915  49.826  28.755  1.00 50.18           C  
-ATOM   2546  CG1 VAL D  53      50.773  50.916  28.133  1.00 43.62           C  
-ATOM   2547  CG2 VAL D  53      49.640  50.181  30.222  1.00 42.56           C  
-ATOM   2548  N   ASP D  54      48.236  47.252  28.723  1.00 39.42           N  
-ATOM   2549  CA  ASP D  54      47.788  46.059  29.428  1.00 40.73           C  
-ATOM   2550  C   ASP D  54      48.155  46.269  30.930  1.00 38.13           C  
-ATOM   2551  O   ASP D  54      49.278  46.707  31.178  1.00 35.22           O  
-ATOM   2552  CB  ASP D  54      48.622  44.862  29.001  1.00 44.42           C  
-ATOM   2553  CG  ASP D  54      48.663  44.266  27.618  1.00 56.81           C  
-ATOM   2554  OD1 ASP D  54      47.593  44.213  26.990  1.00 56.09           O  
-ATOM   2555  OD2 ASP D  54      49.712  43.800  27.086  1.00 61.74           O  
-ATOM   2556  N   PHE D  55      47.257  46.092  31.844  1.00 37.86           N  
-ATOM   2557  CA  PHE D  55      47.627  46.103  33.265  1.00 40.07           C  
-ATOM   2558  C   PHE D  55      47.507  44.634  33.738  1.00 38.39           C  
-ATOM   2559  O   PHE D  55      46.404  44.091  33.746  1.00 39.84           O  
-ATOM   2560  CB  PHE D  55      46.614  47.005  33.897  1.00 40.42           C  
-ATOM   2561  CG  PHE D  55      47.012  47.614  35.218  1.00 41.78           C  
-ATOM   2562  CD1 PHE D  55      48.337  47.870  35.529  1.00 39.56           C  
-ATOM   2563  CD2 PHE D  55      46.016  47.956  36.123  1.00 41.27           C  
-ATOM   2564  CE1 PHE D  55      48.696  48.450  36.727  1.00 41.99           C  
-ATOM   2565  CE2 PHE D  55      46.383  48.553  37.331  1.00 43.51           C  
-ATOM   2566  CZ  PHE D  55      47.694  48.775  37.600  1.00 35.66           C  
-ATOM   2567  N   LEU D  56      48.591  43.916  33.824  1.00 30.45           N  
-ATOM   2568  CA  LEU D  56      48.534  42.482  33.938  1.00 35.17           C  
-ATOM   2569  C   LEU D  56      48.555  42.004  35.403  1.00 37.42           C  
-ATOM   2570  O   LEU D  56      49.416  42.442  36.136  1.00 31.67           O  
-ATOM   2571  CB  LEU D  56      49.717  41.824  33.244  1.00 40.96           C  
-ATOM   2572  CG  LEU D  56      49.702  41.954  31.705  1.00 58.71           C  
-ATOM   2573  CD1 LEU D  56      50.946  41.337  31.075  1.00 56.70           C  
-ATOM   2574  CD2 LEU D  56      48.421  41.320  31.161  1.00 61.97           C  
-ATOM   2575  N   PRO D  57      47.807  40.958  35.616  1.00 39.89           N  
-ATOM   2576  CA  PRO D  57      47.734  40.345  36.948  1.00 39.88           C  
-ATOM   2577  C   PRO D  57      48.883  39.405  37.110  1.00 36.22           C  
-ATOM   2578  O   PRO D  57      49.475  38.844  36.146  1.00 36.08           O  
-ATOM   2579  CB  PRO D  57      46.387  39.669  37.059  1.00 42.26           C  
-ATOM   2580  CG  PRO D  57      45.713  39.929  35.743  1.00 48.91           C  
-ATOM   2581  CD  PRO D  57      46.783  40.361  34.741  1.00 44.55           C  
-ATOM   2582  N   LYS D  58      49.651  39.656  38.204  1.00 25.86           N  
-ATOM   2583  CA  LYS D  58      50.707  38.748  38.560  1.00 23.66           C  
-ATOM   2584  C   LYS D  58      50.513  38.170  39.997  1.00 29.28           C  
-ATOM   2585  O   LYS D  58      49.713  38.707  40.706  1.00 27.63           O  
-ATOM   2586  CB  LYS D  58      52.115  39.300  38.423  1.00 37.88           C  
-ATOM   2587  CG  LYS D  58      52.333  39.709  36.960  1.00 54.20           C  
-ATOM   2588  CD  LYS D  58      53.364  40.805  36.718  1.00 61.44           C  
-ATOM   2589  CE  LYS D  58      53.473  41.033  35.203  1.00 67.33           C  
-ATOM   2590  NZ  LYS D  58      53.673  39.700  34.501  1.00 60.77           N  
-ATOM   2591  N   VAL D  59      51.279  37.127  40.275  1.00 29.48           N  
-ATOM   2592  CA  VAL D  59      51.248  36.597  41.639  1.00 34.67           C  
-ATOM   2593  C   VAL D  59      52.620  36.733  42.283  1.00 31.68           C  
-ATOM   2594  O   VAL D  59      53.607  36.441  41.630  1.00 30.38           O  
-ATOM   2595  CB  VAL D  59      50.729  35.143  41.710  1.00 32.72           C  
-ATOM   2596  CG1 VAL D  59      51.083  34.412  42.978  1.00 49.51           C  
-ATOM   2597  CG2 VAL D  59      49.208  35.233  41.567  1.00 26.89           C  
-ATOM   2598  N   LYS D  60      52.605  37.373  43.490  1.00 23.14           N  
-ATOM   2599  CA  LYS D  60      53.760  37.407  44.346  1.00 26.17           C  
-ATOM   2600  C   LYS D  60      53.794  36.264  45.372  1.00 28.67           C  
-ATOM   2601  O   LYS D  60      52.928  36.218  46.299  1.00 30.42           O  
-ATOM   2602  CB  LYS D  60      53.690  38.807  45.063  1.00 20.50           C  
-ATOM   2603  CG  LYS D  60      55.058  38.968  45.795  1.00 35.00           C  
-ATOM   2604  CD  LYS D  60      54.886  40.099  46.831  1.00 42.96           C  
-ATOM   2605  CE  LYS D  60      55.920  41.176  46.753  1.00 45.39           C  
-ATOM   2606  NZ  LYS D  60      55.496  42.435  47.410  1.00 49.08           N  
-ATOM   2607  N   ILE D  61      54.846  35.474  45.474  1.00 26.03           N  
-ATOM   2608  CA  ILE D  61      54.880  34.377  46.498  1.00 25.09           C  
-ATOM   2609  C   ILE D  61      56.061  34.687  47.410  1.00 30.68           C  
-ATOM   2610  O   ILE D  61      57.033  35.313  46.963  1.00 29.58           O  
-ATOM   2611  CB  ILE D  61      55.087  33.018  45.839  1.00 43.25           C  
-ATOM   2612  CG1 ILE D  61      53.860  32.531  45.005  1.00 33.78           C  
-ATOM   2613  CG2 ILE D  61      55.371  31.926  46.860  1.00 40.22           C  
-ATOM   2614  CD1 ILE D  61      54.446  31.548  43.973  1.00 48.73           C  
-ATOM   2615  N   GLU D  62      55.935  34.596  48.719  1.00 25.73           N  
-ATOM   2616  CA  GLU D  62      56.985  34.984  49.692  1.00 27.41           C  
-ATOM   2617  C   GLU D  62      57.107  33.811  50.692  1.00 29.38           C  
-ATOM   2618  O   GLU D  62      56.075  33.164  50.934  1.00 30.63           O  
-ATOM   2619  CB  GLU D  62      56.547  36.207  50.454  1.00 25.45           C  
-ATOM   2620  CG  GLU D  62      56.675  37.528  49.666  1.00 39.36           C  
-ATOM   2621  CD  GLU D  62      55.908  38.643  50.405  1.00 37.76           C  
-ATOM   2622  OE1 GLU D  62      54.816  38.351  50.955  1.00 36.19           O  
-ATOM   2623  OE2 GLU D  62      56.486  39.748  50.367  1.00 42.63           O  
-ATOM   2624  N   VAL D  63      58.329  33.348  50.920  1.00 31.70           N  
-ATOM   2625  CA  VAL D  63      58.534  32.220  51.828  1.00 35.65           C  
-ATOM   2626  C   VAL D  63      59.831  32.555  52.590  1.00 35.46           C  
-ATOM   2627  O   VAL D  63      60.716  33.211  52.027  1.00 34.82           O  
-ATOM   2628  CB  VAL D  63      58.759  30.815  51.245  1.00 37.38           C  
-ATOM   2629  CG1 VAL D  63      57.520  30.247  50.631  1.00 51.33           C  
-ATOM   2630  CG2 VAL D  63      59.876  30.814  50.181  1.00 29.34           C  
-ATOM   2631  N   VAL D  64      59.812  32.316  53.882  1.00 32.47           N  
-ATOM   2632  CA  VAL D  64      60.965  32.548  54.711  1.00 32.38           C  
-ATOM   2633  C   VAL D  64      61.584  31.190  55.020  1.00 34.65           C  
-ATOM   2634  O   VAL D  64      60.867  30.274  55.419  1.00 28.41           O  
-ATOM   2635  CB  VAL D  64      60.662  33.374  55.962  1.00 42.89           C  
-ATOM   2636  CG1 VAL D  64      61.976  33.611  56.707  1.00 39.84           C  
-ATOM   2637  CG2 VAL D  64      60.065  34.721  55.567  1.00 40.44           C  
-ATOM   2638  N   VAL D  65      62.870  31.077  54.739  1.00 32.81           N  
-ATOM   2639  CA  VAL D  65      63.566  29.801  54.781  1.00 33.80           C  
-ATOM   2640  C   VAL D  65      64.972  29.997  55.347  1.00 35.72           C  
-ATOM   2641  O   VAL D  65      65.555  31.069  55.564  1.00 38.83           O  
-ATOM   2642  CB  VAL D  65      63.738  29.043  53.437  1.00 35.28           C  
-ATOM   2643  CG1 VAL D  65      62.421  28.690  52.762  1.00 37.11           C  
-ATOM   2644  CG2 VAL D  65      64.650  29.735  52.435  1.00 31.99           C  
-ATOM   2645  N   ASP D  66      65.497  28.842  55.771  1.00 42.38           N  
-ATOM   2646  CA  ASP D  66      66.842  28.764  56.384  1.00 35.45           C  
-ATOM   2647  C   ASP D  66      67.880  28.986  55.305  1.00 39.27           C  
-ATOM   2648  O   ASP D  66      67.568  28.677  54.146  1.00 39.88           O  
-ATOM   2649  CB  ASP D  66      66.922  27.308  56.931  1.00 48.34           C  
-ATOM   2650  CG  ASP D  66      68.283  27.150  57.599  1.00 52.46           C  
-ATOM   2651  OD1 ASP D  66      69.228  26.702  56.915  1.00 50.33           O  
-ATOM   2652  OD2 ASP D  66      68.316  27.545  58.783  1.00 52.91           O  
-ATOM   2653  N   ASP D  67      68.991  29.622  55.558  1.00 37.39           N  
-ATOM   2654  CA  ASP D  67      70.011  30.014  54.646  1.00 45.60           C  
-ATOM   2655  C   ASP D  67      70.463  28.830  53.790  1.00 53.73           C  
-ATOM   2656  O   ASP D  67      70.564  28.956  52.561  1.00 53.05           O  
-ATOM   2657  CB  ASP D  67      71.213  30.637  55.340  1.00 52.10           C  
-ATOM   2658  CG  ASP D  67      70.915  31.904  56.101  1.00 53.42           C  
-ATOM   2659  OD1 ASP D  67      69.755  32.324  56.229  1.00 50.52           O  
-ATOM   2660  OD2 ASP D  67      71.850  32.541  56.610  1.00 63.71           O  
-ATOM   2661  N   LYS D  68      70.532  27.629  54.389  1.00 53.55           N  
-ATOM   2662  CA  LYS D  68      70.991  26.516  53.566  1.00 54.09           C  
-ATOM   2663  C   LYS D  68      69.945  26.059  52.583  1.00 53.13           C  
-ATOM   2664  O   LYS D  68      70.366  25.235  51.767  1.00 53.48           O  
-ATOM   2665  CB  LYS D  68      71.579  25.414  54.436  1.00 63.20           C  
-ATOM   2666  N   VAL D  69      68.677  26.470  52.551  1.00 51.62           N  
-ATOM   2667  CA  VAL D  69      67.781  25.959  51.512  1.00 43.52           C  
-ATOM   2668  C   VAL D  69      67.544  26.972  50.388  1.00 39.97           C  
-ATOM   2669  O   VAL D  69      66.683  26.755  49.541  1.00 41.46           O  
-ATOM   2670  CB  VAL D  69      66.502  25.397  52.111  1.00 48.81           C  
-ATOM   2671  CG1 VAL D  69      66.544  25.230  53.624  1.00 54.28           C  
-ATOM   2672  CG2 VAL D  69      65.177  26.085  51.802  1.00 51.16           C  
-ATOM   2673  N   VAL D  70      67.976  28.214  50.494  1.00 36.78           N  
-ATOM   2674  CA  VAL D  70      67.692  29.236  49.471  1.00 45.46           C  
-ATOM   2675  C   VAL D  70      67.957  28.723  48.047  1.00 44.87           C  
-ATOM   2676  O   VAL D  70      67.139  28.808  47.134  1.00 44.52           O  
-ATOM   2677  CB  VAL D  70      68.534  30.492  49.731  1.00 43.40           C  
-ATOM   2678  CG1 VAL D  70      68.388  31.522  48.590  1.00 48.79           C  
-ATOM   2679  CG2 VAL D  70      68.174  31.221  51.002  1.00 42.13           C  
-ATOM   2680  N   GLU D  71      69.167  28.188  47.794  1.00 48.23           N  
-ATOM   2681  CA  GLU D  71      69.442  27.667  46.435  1.00 53.33           C  
-ATOM   2682  C   GLU D  71      68.478  26.614  45.944  1.00 50.47           C  
-ATOM   2683  O   GLU D  71      67.997  26.634  44.782  1.00 48.52           O  
-ATOM   2684  CB  GLU D  71      70.890  27.197  46.392  1.00 68.36           C  
-ATOM   2685  CG  GLU D  71      71.924  28.165  45.888  1.00 89.94           C  
-ATOM   2686  CD  GLU D  71      71.803  29.649  46.124  1.00103.81           C  
-ATOM   2687  OE1 GLU D  71      72.401  30.181  47.098  1.00112.63           O  
-ATOM   2688  OE2 GLU D  71      71.126  30.375  45.344  1.00107.76           O  
-ATOM   2689  N   GLN D  72      68.066  25.630  46.745  1.00 46.99           N  
-ATOM   2690  CA  GLN D  72      67.148  24.601  46.223  1.00 46.86           C  
-ATOM   2691  C   GLN D  72      65.772  25.215  45.994  1.00 46.28           C  
-ATOM   2692  O   GLN D  72      65.001  24.786  45.122  1.00 43.89           O  
-ATOM   2693  CB  GLN D  72      67.119  23.343  47.080  1.00 52.44           C  
-ATOM   2694  CG  GLN D  72      66.272  23.265  48.321  1.00 70.93           C  
-ATOM   2695  CD  GLN D  72      66.859  22.370  49.409  1.00 84.98           C  
-ATOM   2696  OE1 GLN D  72      67.626  22.838  50.265  1.00 89.01           O  
-ATOM   2697  NE2 GLN D  72      66.532  21.081  49.420  1.00 85.81           N  
-ATOM   2698  N   ALA D  73      65.387  26.121  46.909  1.00 46.67           N  
-ATOM   2699  CA  ALA D  73      64.146  26.872  46.777  1.00 44.56           C  
-ATOM   2700  C   ALA D  73      64.166  27.699  45.476  1.00 44.53           C  
-ATOM   2701  O   ALA D  73      63.296  27.627  44.631  1.00 41.08           O  
-ATOM   2702  CB  ALA D  73      64.030  27.790  47.995  1.00 43.91           C  
-ATOM   2703  N   VAL D  74      65.180  28.518  45.250  1.00 45.49           N  
-ATOM   2704  CA  VAL D  74      65.298  29.302  44.008  1.00 46.35           C  
-ATOM   2705  C   VAL D  74      65.236  28.441  42.763  1.00 46.93           C  
-ATOM   2706  O   VAL D  74      64.609  28.768  41.742  1.00 44.44           O  
-ATOM   2707  CB  VAL D  74      66.635  30.088  44.080  1.00 47.01           C  
-ATOM   2708  CG1 VAL D  74      67.055  30.665  42.738  1.00 44.42           C  
-ATOM   2709  CG2 VAL D  74      66.514  31.225  45.107  1.00 43.69           C  
-ATOM   2710  N   ASP D  75      65.856  27.252  42.824  1.00 46.72           N  
-ATOM   2711  CA  ASP D  75      65.967  26.287  41.767  1.00 47.06           C  
-ATOM   2712  C   ASP D  75      64.657  25.622  41.421  1.00 49.49           C  
-ATOM   2713  O   ASP D  75      64.256  25.351  40.268  1.00 48.41           O  
-ATOM   2714  CB  ASP D  75      66.964  25.213  42.250  1.00 67.17           C  
-ATOM   2715  CG  ASP D  75      67.506  24.343  41.132  1.00 70.11           C  
-ATOM   2716  OD1 ASP D  75      68.015  24.919  40.153  1.00 72.07           O  
-ATOM   2717  OD2 ASP D  75      67.425  23.103  41.244  1.00 77.35           O  
-ATOM   2718  N   ALA D  76      63.916  25.321  42.514  1.00 42.76           N  
-ATOM   2719  CA  ALA D  76      62.600  24.769  42.343  1.00 41.86           C  
-ATOM   2720  C   ALA D  76      61.685  25.783  41.646  1.00 44.94           C  
-ATOM   2721  O   ALA D  76      60.887  25.335  40.811  1.00 46.61           O  
-ATOM   2722  CB  ALA D  76      62.015  24.310  43.659  1.00 39.99           C  
-ATOM   2723  N   ILE D  77      61.711  27.066  42.039  1.00 38.15           N  
-ATOM   2724  CA  ILE D  77      60.830  28.028  41.364  1.00 37.37           C  
-ATOM   2725  C   ILE D  77      61.197  28.207  39.866  1.00 36.34           C  
-ATOM   2726  O   ILE D  77      60.297  28.242  39.003  1.00 34.94           O  
-ATOM   2727  CB  ILE D  77      60.934  29.399  42.107  1.00 40.01           C  
-ATOM   2728  CG1 ILE D  77      60.389  29.250  43.560  1.00 41.77           C  
-ATOM   2729  CG2 ILE D  77      60.174  30.498  41.362  1.00 32.04           C  
-ATOM   2730  CD1 ILE D  77      60.989  30.332  44.437  1.00 33.50           C  
-ATOM   2731  N   ILE D  78      62.477  28.393  39.589  1.00 39.35           N  
-ATOM   2732  CA  ILE D  78      62.922  28.521  38.188  1.00 47.21           C  
-ATOM   2733  C   ILE D  78      62.453  27.327  37.354  1.00 50.32           C  
-ATOM   2734  O   ILE D  78      61.674  27.498  36.407  1.00 50.54           O  
-ATOM   2735  CB  ILE D  78      64.427  28.610  37.965  1.00 45.26           C  
-ATOM   2736  CG1 ILE D  78      65.009  29.846  38.637  1.00 43.18           C  
-ATOM   2737  CG2 ILE D  78      64.712  28.550  36.459  1.00 47.47           C  
-ATOM   2738  CD1 ILE D  78      65.032  31.096  37.787  1.00 58.08           C  
-ATOM   2739  N   LYS D  79      62.784  26.119  37.786  1.00 55.65           N  
-ATOM   2740  CA  LYS D  79      62.332  24.917  37.109  1.00 57.33           C  
-ATOM   2741  C   LYS D  79      60.837  24.956  36.830  1.00 58.71           C  
-ATOM   2742  O   LYS D  79      60.528  24.510  35.726  1.00 56.97           O  
-ATOM   2743  CB  LYS D  79      62.552  23.607  37.848  1.00 70.59           C  
-ATOM   2744  CG  LYS D  79      63.942  23.059  38.105  1.00 80.25           C  
-ATOM   2745  CD  LYS D  79      63.777  21.813  38.984  1.00 93.54           C  
-ATOM   2746  CE  LYS D  79      65.049  21.281  39.615  1.00100.00           C  
-ATOM   2747  NZ  LYS D  79      64.816  20.103  40.512  1.00101.37           N  
-ATOM   2748  N   ALA D  80      59.962  25.300  37.780  1.00 55.94           N  
-ATOM   2749  CA  ALA D  80      58.538  25.269  37.442  1.00 48.83           C  
-ATOM   2750  C   ALA D  80      57.916  26.511  36.806  1.00 48.23           C  
-ATOM   2751  O   ALA D  80      56.759  26.435  36.374  1.00 48.83           O  
-ATOM   2752  CB  ALA D  80      57.760  24.995  38.716  1.00 47.76           C  
-ATOM   2753  N   ALA D  81      58.477  27.691  36.987  1.00 45.75           N  
-ATOM   2754  CA  ALA D  81      57.895  28.938  36.540  1.00 49.34           C  
-ATOM   2755  C   ALA D  81      58.363  29.385  35.145  1.00 47.84           C  
-ATOM   2756  O   ALA D  81      57.653  30.155  34.498  1.00 44.33           O  
-ATOM   2757  CB  ALA D  81      58.251  30.079  37.505  1.00 49.98           C  
-ATOM   2758  N   ARG D  82      59.508  28.905  34.697  1.00 48.75           N  
-ATOM   2759  CA  ARG D  82      60.101  29.280  33.431  1.00 54.83           C  
-ATOM   2760  C   ARG D  82      59.285  28.766  32.237  1.00 60.12           C  
-ATOM   2761  O   ARG D  82      59.023  27.565  32.220  1.00 63.03           O  
-ATOM   2762  CB  ARG D  82      61.523  28.722  33.249  1.00 51.65           C  
-ATOM   2763  CG  ARG D  82      62.198  29.410  32.073  1.00 55.67           C  
-ATOM   2764  CD  ARG D  82      63.602  28.996  31.772  1.00 59.51           C  
-ATOM   2765  NE  ARG D  82      64.480  29.011  32.933  1.00 67.52           N  
-ATOM   2766  CZ  ARG D  82      65.728  29.445  32.888  1.00 67.88           C  
-ATOM   2767  NH1 ARG D  82      66.208  29.907  31.739  1.00 77.93           N  
-ATOM   2768  NH2 ARG D  82      66.506  29.457  33.950  1.00 73.55           N  
-ATOM   2769  N   THR D  83      58.915  29.622  31.287  1.00 59.86           N  
-ATOM   2770  CA  THR D  83      58.266  29.201  30.065  1.00 60.24           C  
-ATOM   2771  C   THR D  83      59.060  29.538  28.794  1.00 65.70           C  
-ATOM   2772  O   THR D  83      58.832  28.942  27.730  1.00 68.83           O  
-ATOM   2773  CB  THR D  83      56.918  29.885  29.845  1.00 52.65           C  
-ATOM   2774  OG1 THR D  83      57.172  31.282  29.607  1.00 44.78           O  
-ATOM   2775  CG2 THR D  83      55.981  29.761  31.021  1.00 58.93           C  
-ATOM   2776  N   GLY D  84      59.939  30.528  28.841  1.00 64.39           N  
-ATOM   2777  CA  GLY D  84      60.697  30.985  27.683  1.00 62.54           C  
-ATOM   2778  C   GLY D  84      60.109  32.301  27.176  1.00 59.83           C  
-ATOM   2779  O   GLY D  84      60.779  33.098  26.533  1.00 63.61           O  
-ATOM   2780  N   LYS D  85      58.847  32.563  27.492  1.00 53.49           N  
-ATOM   2781  CA  LYS D  85      58.189  33.772  27.094  1.00 52.55           C  
-ATOM   2782  C   LYS D  85      58.583  34.931  28.008  1.00 57.07           C  
-ATOM   2783  O   LYS D  85      59.003  34.799  29.162  1.00 59.73           O  
-ATOM   2784  CB  LYS D  85      56.657  33.708  27.039  1.00 48.37           C  
-ATOM   2785  CG  LYS D  85      56.080  32.461  26.390  1.00 61.56           C  
-ATOM   2786  CD  LYS D  85      56.605  32.206  24.990  1.00 66.72           C  
-ATOM   2787  CE  LYS D  85      57.107  30.769  24.832  1.00 68.95           C  
-ATOM   2788  NZ  LYS D  85      57.145  30.346  23.402  1.00 55.66           N  
-ATOM   2789  N   ILE D  86      58.399  36.119  27.454  1.00 50.94           N  
-ATOM   2790  CA  ILE D  86      58.683  37.331  28.185  1.00 49.45           C  
-ATOM   2791  C   ILE D  86      57.736  37.484  29.361  1.00 50.78           C  
-ATOM   2792  O   ILE D  86      56.560  37.098  29.291  1.00 49.39           O  
-ATOM   2793  CB  ILE D  86      58.555  38.530  27.238  1.00 58.46           C  
-ATOM   2794  CG1 ILE D  86      59.792  38.573  26.337  1.00 64.76           C  
-ATOM   2795  CG2 ILE D  86      58.413  39.835  28.026  1.00 65.44           C  
-ATOM   2796  CD1 ILE D  86      60.934  39.385  26.912  1.00 66.46           C  
-ATOM   2797  N   GLY D  87      58.223  38.026  30.466  1.00 48.07           N  
-ATOM   2798  CA  GLY D  87      57.360  38.240  31.591  1.00 51.69           C  
-ATOM   2799  C   GLY D  87      57.236  37.015  32.496  1.00 45.97           C  
-ATOM   2800  O   GLY D  87      56.263  36.880  33.232  1.00 47.74           O  
-ATOM   2801  N   ASP D  88      58.203  36.107  32.452  1.00 40.30           N  
-ATOM   2802  CA  ASP D  88      58.155  34.939  33.326  1.00 43.98           C  
-ATOM   2803  C   ASP D  88      58.323  35.367  34.777  1.00 41.76           C  
-ATOM   2804  O   ASP D  88      57.927  34.634  35.674  1.00 41.45           O  
-ATOM   2805  CB  ASP D  88      59.224  33.911  32.953  1.00 41.44           C  
-ATOM   2806  CG  ASP D  88      58.773  32.920  31.901  1.00 41.35           C  
-ATOM   2807  OD1 ASP D  88      57.579  32.902  31.581  1.00 43.43           O  
-ATOM   2808  OD2 ASP D  88      59.621  32.151  31.391  1.00 50.36           O  
-ATOM   2809  N   GLY D  89      58.932  36.520  34.998  1.00 40.80           N  
-ATOM   2810  CA  GLY D  89      59.067  37.026  36.361  1.00 39.17           C  
-ATOM   2811  C   GLY D  89      60.492  37.024  36.904  1.00 39.69           C  
-ATOM   2812  O   GLY D  89      61.472  36.708  36.210  1.00 35.16           O  
-ATOM   2813  N   LYS D  90      60.572  37.411  38.180  1.00 32.79           N  
-ATOM   2814  CA  LYS D  90      61.860  37.471  38.908  1.00 30.93           C  
-ATOM   2815  C   LYS D  90      61.774  36.936  40.335  1.00 29.83           C  
-ATOM   2816  O   LYS D  90      60.708  36.853  40.925  1.00 25.65           O  
-ATOM   2817  CB  LYS D  90      62.393  38.895  38.909  1.00 30.21           C  
-ATOM   2818  CG  LYS D  90      62.674  39.463  37.532  1.00 49.03           C  
-ATOM   2819  CD  LYS D  90      63.602  40.650  37.627  1.00 35.96           C  
-ATOM   2820  CE  LYS D  90      63.292  41.673  36.549  1.00 45.17           C  
-ATOM   2821  NZ  LYS D  90      64.371  42.692  36.429  1.00 45.58           N  
-ATOM   2822  N   ILE D  91      62.956  36.589  40.876  1.00 27.78           N  
-ATOM   2823  CA  ILE D  91      63.123  36.107  42.244  1.00 34.46           C  
-ATOM   2824  C   ILE D  91      64.070  37.052  42.965  1.00 36.46           C  
-ATOM   2825  O   ILE D  91      65.096  37.428  42.414  1.00 34.71           O  
-ATOM   2826  CB  ILE D  91      63.721  34.696  42.263  1.00 41.27           C  
-ATOM   2827  CG1 ILE D  91      62.886  33.741  41.400  1.00 37.07           C  
-ATOM   2828  CG2 ILE D  91      63.828  34.185  43.697  1.00 35.76           C  
-ATOM   2829  CD1 ILE D  91      63.279  32.286  41.552  1.00 42.64           C  
-ATOM   2830  N   PHE D  92      63.729  37.444  44.190  1.00 25.20           N  
-ATOM   2831  CA  PHE D  92      64.603  38.301  44.977  1.00 26.46           C  
-ATOM   2832  C   PHE D  92      64.918  37.591  46.331  1.00 34.54           C  
-ATOM   2833  O   PHE D  92      64.042  36.876  46.868  1.00 34.34           O  
-ATOM   2834  CB  PHE D  92      63.982  39.630  45.349  1.00 36.37           C  
-ATOM   2835  CG  PHE D  92      63.299  40.293  44.200  1.00 48.16           C  
-ATOM   2836  CD1 PHE D  92      61.934  40.095  44.041  1.00 48.68           C  
-ATOM   2837  CD2 PHE D  92      64.014  41.047  43.292  1.00 48.54           C  
-ATOM   2838  CE1 PHE D  92      61.282  40.673  42.969  1.00 55.88           C  
-ATOM   2839  CE2 PHE D  92      63.365  41.632  42.226  1.00 46.44           C  
-ATOM   2840  CZ  PHE D  92      62.005  41.455  42.075  1.00 56.11           C  
-ATOM   2841  N   VAL D  93      66.054  37.871  46.894  1.00 33.77           N  
-ATOM   2842  CA  VAL D  93      66.500  37.230  48.137  1.00 34.34           C  
-ATOM   2843  C   VAL D  93      66.882  38.297  49.151  1.00 32.98           C  
-ATOM   2844  O   VAL D  93      67.498  39.301  48.762  1.00 34.10           O  
-ATOM   2845  CB  VAL D  93      67.716  36.306  47.942  1.00 41.64           C  
-ATOM   2846  CG1 VAL D  93      68.083  35.680  49.278  1.00 38.45           C  
-ATOM   2847  CG2 VAL D  93      67.358  35.198  46.930  1.00 39.55           C  
-ATOM   2848  N   GLN D  94      66.270  38.258  50.359  1.00 29.53           N  
-ATOM   2849  CA  GLN D  94      66.609  39.297  51.344  1.00 24.83           C  
-ATOM   2850  C   GLN D  94      66.869  38.627  52.712  1.00 31.55           C  
-ATOM   2851  O   GLN D  94      66.258  37.588  52.933  1.00 28.22           O  
-ATOM   2852  CB  GLN D  94      65.435  40.249  51.569  1.00 32.74           C  
-ATOM   2853  CG  GLN D  94      65.123  41.140  50.413  1.00 44.97           C  
-ATOM   2854  CD  GLN D  94      63.820  41.925  50.548  1.00 41.93           C  
-ATOM   2855  OE1 GLN D  94      62.753  41.419  50.242  1.00 54.66           O  
-ATOM   2856  NE2 GLN D  94      63.957  43.181  50.918  1.00 40.61           N  
-ATOM   2857  N   GLU D  95      67.607  39.306  53.572  1.00 35.84           N  
-ATOM   2858  CA  GLU D  95      67.890  38.723  54.881  1.00 39.92           C  
-ATOM   2859  C   GLU D  95      66.706  38.970  55.843  1.00 35.08           C  
-ATOM   2860  O   GLU D  95      66.075  40.035  55.770  1.00 29.10           O  
-ATOM   2861  CB  GLU D  95      69.135  39.374  55.477  1.00 45.17           C  
-ATOM   2862  CG  GLU D  95      69.781  38.682  56.667  1.00 62.10           C  
-ATOM   2863  CD  GLU D  95      71.247  39.075  56.791  1.00 80.06           C  
-ATOM   2864  OE1 GLU D  95      71.824  38.808  57.868  1.00 81.73           O  
-ATOM   2865  OE2 GLU D  95      71.832  39.643  55.829  1.00 82.86           O  
-ATOM   2866  N   VAL D  96      66.406  37.934  56.645  1.00 32.74           N  
-ATOM   2867  CA  VAL D  96      65.371  38.157  57.697  1.00 30.38           C  
-ATOM   2868  C   VAL D  96      66.008  38.168  59.097  1.00 31.19           C  
-ATOM   2869  O   VAL D  96      66.664  37.178  59.325  1.00 32.14           O  
-ATOM   2870  CB  VAL D  96      64.237  37.183  57.539  1.00 35.23           C  
-ATOM   2871  CG1 VAL D  96      63.169  37.529  58.582  1.00 35.64           C  
-ATOM   2872  CG2 VAL D  96      63.583  37.311  56.145  1.00 31.93           C  
-ATOM   2873  N   GLU D  97      66.025  39.240  59.874  1.00 28.47           N  
-ATOM   2874  CA  GLU D  97      66.800  39.187  61.141  1.00 36.09           C  
-ATOM   2875  C   GLU D  97      66.116  38.245  62.144  1.00 37.20           C  
-ATOM   2876  O   GLU D  97      66.843  37.633  62.883  1.00 36.41           O  
-ATOM   2877  CB  GLU D  97      66.862  40.558  61.830  1.00 35.01           C  
-ATOM   2878  CG  GLU D  97      67.458  41.552  60.867  1.00 53.78           C  
-ATOM   2879  CD  GLU D  97      67.854  42.859  61.493  1.00 52.87           C  
-ATOM   2880  OE1 GLU D  97      67.402  43.183  62.596  1.00 59.83           O  
-ATOM   2881  OE2 GLU D  97      68.650  43.529  60.818  1.00 53.90           O  
-ATOM   2882  N   GLN D  98      64.793  38.122  62.234  1.00 37.27           N  
-ATOM   2883  CA  GLN D  98      64.163  37.233  63.216  1.00 34.05           C  
-ATOM   2884  C   GLN D  98      62.867  36.687  62.643  1.00 33.88           C  
-ATOM   2885  O   GLN D  98      62.255  37.501  61.935  1.00 27.68           O  
-ATOM   2886  CB  GLN D  98      63.742  38.098  64.437  1.00 42.92           C  
-ATOM   2887  CG  GLN D  98      64.873  38.657  65.284  1.00 58.60           C  
-ATOM   2888  CD  GLN D  98      64.572  39.840  66.180  1.00 71.55           C  
-ATOM   2889  OE1 GLN D  98      63.676  40.658  65.990  1.00 69.84           O  
-ATOM   2890  NE2 GLN D  98      65.341  40.014  67.273  1.00 83.89           N  
-ATOM   2891  N   VAL D  99      62.501  35.457  62.968  1.00 24.75           N  
-ATOM   2892  CA  VAL D  99      61.241  34.876  62.655  1.00 26.94           C  
-ATOM   2893  C   VAL D  99      60.644  34.335  63.968  1.00 30.95           C  
-ATOM   2894  O   VAL D  99      61.360  33.708  64.748  1.00 26.71           O  
-ATOM   2895  CB  VAL D  99      61.423  33.726  61.674  1.00 36.12           C  
-ATOM   2896  CG1 VAL D  99      60.099  33.101  61.325  1.00 33.24           C  
-ATOM   2897  CG2 VAL D  99      62.180  34.050  60.384  1.00 45.00           C  
-ATOM   2898  N   ILE D 100      59.353  34.396  64.189  1.00 29.15           N  
-ATOM   2899  CA  ILE D 100      58.674  33.910  65.377  1.00 25.99           C  
-ATOM   2900  C   ILE D 100      57.418  33.211  64.988  1.00 30.45           C  
-ATOM   2901  O   ILE D 100      56.662  33.793  64.165  1.00 27.82           O  
-ATOM   2902  CB  ILE D 100      58.250  35.047  66.335  1.00 32.16           C  
-ATOM   2903  CG1 ILE D 100      59.436  35.877  66.848  1.00 35.68           C  
-ATOM   2904  CG2 ILE D 100      57.580  34.411  67.581  1.00 36.74           C  
-ATOM   2905  CD1 ILE D 100      59.523  37.234  66.170  1.00 44.65           C  
-ATOM   2906  N   ARG D 101      57.274  31.964  65.386  1.00 22.59           N  
-ATOM   2907  CA  ARG D 101      56.040  31.242  65.082  1.00 24.00           C  
-ATOM   2908  C   ARG D 101      55.079  31.612  66.218  1.00 30.39           C  
-ATOM   2909  O   ARG D 101      55.450  31.451  67.422  1.00 26.71           O  
-ATOM   2910  CB  ARG D 101      56.377  29.735  65.066  1.00 31.03           C  
-ATOM   2911  CG  ARG D 101      55.186  28.829  65.006  1.00 29.77           C  
-ATOM   2912  CD  ARG D 101      55.313  27.446  64.374  1.00 40.05           C  
-ATOM   2913  NE  ARG D 101      56.695  26.984  64.150  1.00 54.84           N  
-ATOM   2914  CZ  ARG D 101      57.145  26.475  63.010  1.00 43.16           C  
-ATOM   2915  NH1 ARG D 101      56.315  26.379  61.985  1.00 39.45           N  
-ATOM   2916  NH2 ARG D 101      58.365  26.051  62.726  1.00 44.91           N  
-ATOM   2917  N   ILE D 102      53.917  32.138  65.953  1.00 26.61           N  
-ATOM   2918  CA  ILE D 102      52.922  32.689  66.849  1.00 27.49           C  
-ATOM   2919  C   ILE D 102      52.266  31.628  67.773  1.00 30.76           C  
-ATOM   2920  O   ILE D 102      52.210  31.885  68.981  1.00 27.66           O  
-ATOM   2921  CB  ILE D 102      51.756  33.411  66.118  1.00 21.02           C  
-ATOM   2922  CG1 ILE D 102      52.334  34.698  65.476  1.00 27.42           C  
-ATOM   2923  CG2 ILE D 102      50.538  33.679  66.970  1.00 21.18           C  
-ATOM   2924  CD1 ILE D 102      51.515  35.484  64.531  1.00 20.53           C  
-ATOM   2925  N   ARG D 103      52.015  30.449  67.344  1.00 27.91           N  
-ATOM   2926  CA  ARG D 103      51.329  29.437  68.123  1.00 30.23           C  
-ATOM   2927  C   ARG D 103      52.244  28.914  69.291  1.00 32.49           C  
-ATOM   2928  O   ARG D 103      51.791  28.715  70.419  1.00 29.58           O  
-ATOM   2929  CB  ARG D 103      50.993  28.240  67.270  1.00 23.76           C  
-ATOM   2930  CG  ARG D 103      50.217  27.098  67.908  1.00 33.11           C  
-ATOM   2931  CD  ARG D 103      50.072  25.875  67.054  1.00 37.18           C  
-ATOM   2932  NE  ARG D 103      49.147  24.905  67.664  1.00 46.42           N  
-ATOM   2933  CZ  ARG D 103      49.432  23.619  67.790  1.00 42.58           C  
-ATOM   2934  NH1 ARG D 103      48.589  22.724  68.349  1.00 46.19           N  
-ATOM   2935  NH2 ARG D 103      50.608  23.215  67.342  1.00 37.89           N  
-ATOM   2936  N   THR D 104      53.515  28.790  69.020  1.00 28.96           N  
-ATOM   2937  CA  THR D 104      54.476  28.145  69.877  1.00 35.33           C  
-ATOM   2938  C   THR D 104      55.444  29.156  70.461  1.00 34.19           C  
-ATOM   2939  O   THR D 104      56.172  28.681  71.315  1.00 31.11           O  
-ATOM   2940  CB  THR D 104      55.288  27.042  69.158  1.00 37.86           C  
-ATOM   2941  OG1 THR D 104      56.080  27.684  68.139  1.00 32.02           O  
-ATOM   2942  CG2 THR D 104      54.363  25.962  68.601  1.00 32.11           C  
-ATOM   2943  N   GLY D 105      55.591  30.372  69.929  1.00 25.08           N  
-ATOM   2944  CA  GLY D 105      56.676  31.245  70.409  1.00 26.58           C  
-ATOM   2945  C   GLY D 105      58.054  30.697  69.992  1.00 27.05           C  
-ATOM   2946  O   GLY D 105      59.121  31.222  70.368  1.00 24.91           O  
-ATOM   2947  N   GLU D 106      58.168  29.691  69.138  1.00 27.36           N  
-ATOM   2948  CA  GLU D 106      59.489  29.367  68.568  1.00 29.33           C  
-ATOM   2949  C   GLU D 106      60.129  30.503  67.756  1.00 37.79           C  
-ATOM   2950  O   GLU D 106      59.444  31.284  67.067  1.00 31.70           O  
-ATOM   2951  CB  GLU D 106      59.352  28.215  67.575  1.00 34.90           C  
-ATOM   2952  CG  GLU D 106      59.263  26.855  68.308  1.00 30.59           C  
-ATOM   2953  CD  GLU D 106      58.637  25.897  67.304  1.00 25.99           C  
-ATOM   2954  OE1 GLU D 106      57.479  26.055  66.814  1.00 27.41           O  
-ATOM   2955  OE2 GLU D 106      59.356  24.933  66.985  1.00 26.89           O  
-ATOM   2956  N   THR D 107      61.487  30.538  67.744  1.00 30.96           N  
-ATOM   2957  CA  THR D 107      62.179  31.614  67.075  1.00 34.96           C  
-ATOM   2958  C   THR D 107      63.329  31.034  66.243  1.00 35.55           C  
-ATOM   2959  O   THR D 107      63.704  29.853  66.342  1.00 35.03           O  
-ATOM   2960  CB  THR D 107      62.771  32.726  67.968  1.00 36.69           C  
-ATOM   2961  OG1 THR D 107      63.831  32.056  68.720  1.00 34.09           O  
-ATOM   2962  CG2 THR D 107      61.806  33.382  68.929  1.00 34.99           C  
-ATOM   2963  N   GLY D 108      63.841  31.894  65.355  1.00 35.04           N  
-ATOM   2964  CA  GLY D 108      64.977  31.546  64.541  1.00 32.68           C  
-ATOM   2965  C   GLY D 108      64.795  30.355  63.649  1.00 30.87           C  
-ATOM   2966  O   GLY D 108      63.769  30.143  63.067  1.00 32.30           O  
-ATOM   2967  N   PRO D 109      65.814  29.470  63.628  1.00 32.74           N  
-ATOM   2968  CA  PRO D 109      65.842  28.269  62.856  1.00 29.48           C  
-ATOM   2969  C   PRO D 109      64.748  27.332  63.279  1.00 32.11           C  
-ATOM   2970  O   PRO D 109      64.252  26.594  62.378  1.00 33.77           O  
-ATOM   2971  CB  PRO D 109      67.267  27.659  63.046  1.00 33.08           C  
-ATOM   2972  CG  PRO D 109      68.069  28.785  63.565  1.00 39.03           C  
-ATOM   2973  CD  PRO D 109      67.137  29.765  64.268  1.00 35.95           C  
-ATOM   2974  N   ASP D 110      64.360  27.279  64.586  1.00 30.30           N  
-ATOM   2975  CA  ASP D 110      63.184  26.437  64.944  1.00 28.08           C  
-ATOM   2976  C   ASP D 110      61.843  26.903  64.375  1.00 29.99           C  
-ATOM   2977  O   ASP D 110      60.902  26.133  64.176  1.00 29.83           O  
-ATOM   2978  CB  ASP D 110      63.047  26.626  66.501  1.00 26.37           C  
-ATOM   2979  CG  ASP D 110      64.199  25.792  67.140  1.00 32.97           C  
-ATOM   2980  OD1 ASP D 110      64.451  24.662  66.690  1.00 34.79           O  
-ATOM   2981  OD2 ASP D 110      64.750  26.415  68.032  1.00 37.65           O  
-ATOM   2982  N   ALA D 111      61.717  28.176  63.959  1.00 34.64           N  
-ATOM   2983  CA  ALA D 111      60.497  28.747  63.390  1.00 35.65           C  
-ATOM   2984  C   ALA D 111      60.278  28.683  61.881  1.00 39.22           C  
-ATOM   2985  O   ALA D 111      59.213  29.135  61.353  1.00 36.52           O  
-ATOM   2986  CB  ALA D 111      60.545  30.232  63.872  1.00 32.12           C  
-ATOM   2987  N   VAL D 112      61.218  28.210  61.096  1.00 35.31           N  
-ATOM   2988  CA  VAL D 112      61.031  28.145  59.650  1.00 45.09           C  
-ATOM   2989  C   VAL D 112      60.565  26.769  59.195  1.00 47.58           C  
-ATOM   2990  O   VAL D 112      60.954  25.818  59.945  1.00 48.84           O  
-ATOM   2991  CB  VAL D 112      62.248  28.596  58.850  1.00 42.02           C  
-ATOM   2992  CG1 VAL D 112      62.408  30.115  58.913  1.00 52.87           C  
-ATOM   2993  CG2 VAL D 112      63.537  28.014  59.397  1.00 46.37           C  
-TER    2994      VAL D 112                                                      
-ATOM   2995  N   MET E   1      65.940  51.458  62.268  1.00 38.54           N  
-ATOM   2996  CA  MET E   1      64.534  51.209  61.927  1.00 38.38           C  
-ATOM   2997  C   MET E   1      64.332  49.786  61.449  1.00 33.75           C  
-ATOM   2998  O   MET E   1      65.185  49.210  60.759  1.00 34.00           O  
-ATOM   2999  CB  MET E   1      64.057  52.157  60.832  1.00 39.76           C  
-ATOM   3000  CG  MET E   1      64.489  53.591  61.059  1.00 41.39           C  
-ATOM   3001  SD  MET E   1      63.382  54.473  62.177  1.00 57.87           S  
-ATOM   3002  CE  MET E   1      61.821  53.673  61.806  1.00 64.61           C  
-ATOM   3003  N   LYS E   2      63.210  49.215  61.827  1.00 29.33           N  
-ATOM   3004  CA  LYS E   2      62.940  47.847  61.450  1.00 30.28           C  
-ATOM   3005  C   LYS E   2      61.543  47.739  60.871  1.00 30.19           C  
-ATOM   3006  O   LYS E   2      60.671  48.539  61.188  1.00 33.54           O  
-ATOM   3007  CB  LYS E   2      63.051  46.901  62.638  1.00 34.19           C  
-ATOM   3008  CG  LYS E   2      64.339  47.071  63.414  1.00 34.98           C  
-ATOM   3009  CD  LYS E   2      65.477  46.243  62.810  1.00 36.38           C  
-ATOM   3010  CE  LYS E   2      66.778  46.488  63.563  1.00 42.73           C  
-ATOM   3011  NZ  LYS E   2      67.890  45.663  63.018  1.00 38.22           N  
-ATOM   3012  N   GLN E   3      61.360  46.724  60.075  1.00 30.60           N  
-ATOM   3013  CA  GLN E   3      60.030  46.448  59.576  1.00 30.86           C  
-ATOM   3014  C   GLN E   3      59.578  45.139  60.258  1.00 28.71           C  
-ATOM   3015  O   GLN E   3      60.330  44.157  60.292  1.00 29.40           O  
-ATOM   3016  CB  GLN E   3      59.998  46.342  58.056  1.00 26.48           C  
-ATOM   3017  CG  GLN E   3      58.830  45.493  57.549  1.00 28.70           C  
-ATOM   3018  CD  GLN E   3      58.606  45.673  56.048  1.00 43.26           C  
-ATOM   3019  OE1 GLN E   3      59.047  44.858  55.239  1.00 48.57           O  
-ATOM   3020  NE2 GLN E   3      57.950  46.671  55.466  1.00 47.95           N  
-ATOM   3021  N   VAL E   4      58.384  45.163  60.817  1.00 27.26           N  
-ATOM   3022  CA  VAL E   4      57.735  44.016  61.450  1.00 28.19           C  
-ATOM   3023  C   VAL E   4      56.555  43.642  60.584  1.00 24.86           C  
-ATOM   3024  O   VAL E   4      55.691  44.465  60.290  1.00 24.86           O  
-ATOM   3025  CB  VAL E   4      57.261  44.359  62.861  1.00 28.69           C  
-ATOM   3026  CG1 VAL E   4      56.557  43.173  63.478  1.00 26.62           C  
-ATOM   3027  CG2 VAL E   4      58.414  44.806  63.738  1.00 31.58           C  
-ATOM   3028  N   THR E   5      56.543  42.356  60.194  1.00 23.06           N  
-ATOM   3029  CA  THR E   5      55.555  41.741  59.326  1.00 26.08           C  
-ATOM   3030  C   THR E   5      54.910  40.557  60.035  1.00 27.23           C  
-ATOM   3031  O   THR E   5      55.618  39.667  60.517  1.00 26.28           O  
-ATOM   3032  CB  THR E   5      56.205  41.238  58.023  1.00 33.15           C  
-ATOM   3033  OG1 THR E   5      56.776  42.364  57.338  1.00 31.03           O  
-ATOM   3034  CG2 THR E   5      55.180  40.567  57.132  1.00 27.24           C  
-ATOM   3035  N   ALA E   6      53.583  40.524  60.082  1.00 23.19           N  
-ATOM   3036  CA  ALA E   6      52.910  39.407  60.680  1.00 26.25           C  
-ATOM   3037  C   ALA E   6      51.838  38.941  59.706  1.00 24.60           C  
-ATOM   3038  O   ALA E   6      51.159  39.753  59.084  1.00 26.95           O  
-ATOM   3039  CB  ALA E   6      52.294  39.782  62.019  1.00 23.64           C  
-ATOM   3040  N   ILE E   7      51.711  37.626  59.567  1.00 21.71           N  
-ATOM   3041  CA  ILE E   7      50.666  36.988  58.752  1.00 23.63           C  
-ATOM   3042  C   ILE E   7      49.752  36.283  59.717  1.00 26.78           C  
-ATOM   3043  O   ILE E   7      50.141  35.313  60.374  1.00 25.62           O  
-ATOM   3044  CB  ILE E   7      51.299  36.060  57.695  1.00 28.46           C  
-ATOM   3045  CG1 ILE E   7      52.044  36.899  56.668  1.00 34.42           C  
-ATOM   3046  CG2 ILE E   7      50.252  35.203  57.008  1.00 27.38           C  
-ATOM   3047  CD1 ILE E   7      52.873  36.092  55.697  1.00 44.61           C  
-ATOM   3048  N   ILE E   8      48.522  36.780  59.830  1.00 19.42           N  
-ATOM   3049  CA  ILE E   8      47.585  36.275  60.834  1.00 27.32           C  
-ATOM   3050  C   ILE E   8      46.252  35.890  60.265  1.00 29.83           C  
-ATOM   3051  O   ILE E   8      45.953  36.205  59.114  1.00 25.74           O  
-ATOM   3052  CB  ILE E   8      47.347  37.421  61.883  1.00 25.09           C  
-ATOM   3053  CG1 ILE E   8      46.712  38.663  61.299  1.00 27.54           C  
-ATOM   3054  CG2 ILE E   8      48.681  37.787  62.566  1.00 24.25           C  
-ATOM   3055  CD1 ILE E   8      46.189  39.710  62.276  1.00 34.84           C  
-ATOM   3056  N   LYS E   9      45.405  35.239  61.032  1.00 25.90           N  
-ATOM   3057  CA  LYS E   9      44.023  34.958  60.629  1.00 29.17           C  
-ATOM   3058  C   LYS E   9      43.254  36.262  60.618  1.00 27.54           C  
-ATOM   3059  O   LYS E   9      43.497  37.184  61.427  1.00 26.79           O  
-ATOM   3060  CB  LYS E   9      43.417  33.971  61.667  1.00 33.17           C  
-ATOM   3061  CG  LYS E   9      44.264  32.693  61.685  1.00 32.52           C  
-ATOM   3062  CD  LYS E   9      43.819  31.725  62.771  1.00 29.96           C  
-ATOM   3063  CE  LYS E   9      44.231  30.322  62.411  1.00 41.50           C  
-ATOM   3064  NZ  LYS E   9      44.371  29.528  63.660  1.00 31.11           N  
-ATOM   3065  N   PRO E  10      42.310  36.407  59.669  1.00 28.79           N  
-ATOM   3066  CA  PRO E  10      41.653  37.650  59.378  1.00 25.62           C  
-ATOM   3067  C   PRO E  10      40.795  38.137  60.494  1.00 25.24           C  
-ATOM   3068  O   PRO E  10      40.825  39.340  60.763  1.00 26.42           O  
-ATOM   3069  CB  PRO E  10      40.760  37.413  58.117  1.00 30.00           C  
-ATOM   3070  CG  PRO E  10      40.843  35.949  57.867  1.00 31.93           C  
-ATOM   3071  CD  PRO E  10      41.965  35.353  58.690  1.00 29.97           C  
-ATOM   3072  N   PHE E  11      40.289  37.188  61.301  1.00 29.13           N  
-ATOM   3073  CA  PHE E  11      39.372  37.582  62.406  1.00 30.02           C  
-ATOM   3074  C   PHE E  11      40.164  38.063  63.620  1.00 32.57           C  
-ATOM   3075  O   PHE E  11      39.604  38.612  64.557  1.00 28.48           O  
-ATOM   3076  CB  PHE E  11      38.374  36.419  62.628  1.00 24.31           C  
-ATOM   3077  CG  PHE E  11      39.029  35.167  63.137  1.00 34.96           C  
-ATOM   3078  CD1 PHE E  11      39.662  35.177  64.369  1.00 29.67           C  
-ATOM   3079  CD2 PHE E  11      39.062  33.983  62.398  1.00 34.46           C  
-ATOM   3080  CE1 PHE E  11      40.300  34.076  64.897  1.00 33.03           C  
-ATOM   3081  CE2 PHE E  11      39.707  32.860  62.931  1.00 28.86           C  
-ATOM   3082  CZ  PHE E  11      40.332  32.924  64.128  1.00 29.60           C  
-ATOM   3083  N   LYS E  12      41.519  38.133  63.558  1.00 26.09           N  
-ATOM   3084  CA  LYS E  12      42.356  38.637  64.625  1.00 22.83           C  
-ATOM   3085  C   LYS E  12      42.795  40.048  64.419  1.00 25.88           C  
-ATOM   3086  O   LYS E  12      43.293  40.767  65.298  1.00 26.14           O  
-ATOM   3087  CB  LYS E  12      43.568  37.709  64.767  1.00 22.57           C  
-ATOM   3088  CG  LYS E  12      43.138  36.391  65.513  1.00 27.14           C  
-ATOM   3089  CD  LYS E  12      42.811  36.811  66.969  1.00 34.46           C  
-ATOM   3090  CE  LYS E  12      42.951  35.640  67.956  1.00 31.95           C  
-ATOM   3091  NZ  LYS E  12      42.766  36.138  69.348  1.00 36.22           N  
-ATOM   3092  N   LEU E  13      42.417  40.599  63.240  1.00 20.51           N  
-ATOM   3093  CA  LEU E  13      43.021  41.927  62.938  1.00 23.98           C  
-ATOM   3094  C   LEU E  13      42.671  42.984  64.013  1.00 23.19           C  
-ATOM   3095  O   LEU E  13      43.481  43.788  64.347  1.00 23.45           O  
-ATOM   3096  CB  LEU E  13      42.427  42.409  61.617  1.00 26.31           C  
-ATOM   3097  CG  LEU E  13      43.149  43.455  60.769  1.00 42.37           C  
-ATOM   3098  CD1 LEU E  13      42.134  44.387  60.183  1.00 37.69           C  
-ATOM   3099  CD2 LEU E  13      44.415  44.100  61.248  1.00 41.04           C  
-ATOM   3100  N   ASP E  14      41.398  43.178  64.342  1.00 24.25           N  
-ATOM   3101  CA  ASP E  14      41.015  44.236  65.279  1.00 31.12           C  
-ATOM   3102  C   ASP E  14      41.707  44.092  66.657  1.00 26.42           C  
-ATOM   3103  O   ASP E  14      42.097  45.109  67.240  1.00 25.24           O  
-ATOM   3104  CB  ASP E  14      39.513  44.100  65.598  1.00 34.61           C  
-ATOM   3105  CG  ASP E  14      38.616  44.567  64.454  1.00 52.43           C  
-ATOM   3106  OD1 ASP E  14      39.008  45.287  63.517  1.00 41.80           O  
-ATOM   3107  OD2 ASP E  14      37.430  44.201  64.465  1.00 43.84           O  
-ATOM   3108  N   GLU E  15      41.885  42.839  67.041  1.00 27.33           N  
-ATOM   3109  CA  GLU E  15      42.513  42.555  68.330  1.00 30.12           C  
-ATOM   3110  C   GLU E  15      43.994  42.857  68.301  1.00 29.64           C  
-ATOM   3111  O   GLU E  15      44.581  43.520  69.185  1.00 27.31           O  
-ATOM   3112  CB  GLU E  15      42.266  41.066  68.705  1.00 23.87           C  
-ATOM   3113  CG  GLU E  15      42.745  40.879  70.175  1.00 24.52           C  
-ATOM   3114  CD  GLU E  15      42.334  39.519  70.716  1.00 29.16           C  
-ATOM   3115  OE1 GLU E  15      41.659  38.694  70.052  1.00 25.35           O  
-ATOM   3116  OE2 GLU E  15      42.753  39.277  71.881  1.00 34.14           O  
-ATOM   3117  N   VAL E  16      44.587  42.546  67.115  1.00 28.08           N  
-ATOM   3118  CA  VAL E  16      46.032  42.866  66.969  1.00 20.55           C  
-ATOM   3119  C   VAL E  16      46.157  44.370  66.966  1.00 18.86           C  
-ATOM   3120  O   VAL E  16      47.106  44.942  67.479  1.00 23.88           O  
-ATOM   3121  CB  VAL E  16      46.616  42.167  65.710  1.00 25.34           C  
-ATOM   3122  CG1 VAL E  16      47.970  42.793  65.340  1.00 25.77           C  
-ATOM   3123  CG2 VAL E  16      46.726  40.662  66.089  1.00 21.05           C  
-ATOM   3124  N   ARG E  17      45.283  45.059  66.253  1.00 22.15           N  
-ATOM   3125  CA  ARG E  17      45.422  46.524  66.127  1.00 27.32           C  
-ATOM   3126  C   ARG E  17      45.307  47.209  67.471  1.00 29.69           C  
-ATOM   3127  O   ARG E  17      46.053  48.136  67.786  1.00 29.79           O  
-ATOM   3128  CB  ARG E  17      44.382  47.093  65.165  1.00 32.66           C  
-ATOM   3129  CG  ARG E  17      44.427  48.591  65.088  1.00 53.09           C  
-ATOM   3130  CD  ARG E  17      43.515  49.082  63.999  1.00 67.36           C  
-ATOM   3131  NE  ARG E  17      42.824  50.315  64.389  1.00 81.25           N  
-ATOM   3132  CZ  ARG E  17      41.494  50.449  64.385  1.00 89.14           C  
-ATOM   3133  NH1 ARG E  17      40.734  49.424  64.016  1.00 86.95           N  
-ATOM   3134  NH2 ARG E  17      40.941  51.589  64.741  1.00 92.86           N  
-ATOM   3135  N   GLU E  18      44.372  46.741  68.264  1.00 27.88           N  
-ATOM   3136  CA  GLU E  18      44.149  47.314  69.598  1.00 31.34           C  
-ATOM   3137  C   GLU E  18      45.344  47.040  70.510  1.00 30.32           C  
-ATOM   3138  O   GLU E  18      45.790  47.937  71.242  1.00 30.84           O  
-ATOM   3139  CB  GLU E  18      42.875  46.729  70.239  1.00 39.72           C  
-ATOM   3140  CG  GLU E  18      42.528  47.318  71.604  1.00 56.67           C  
-ATOM   3141  CD  GLU E  18      41.116  47.903  71.583  1.00 66.09           C  
-ATOM   3142  OE1 GLU E  18      40.570  48.084  70.458  1.00 74.96           O  
-ATOM   3143  OE2 GLU E  18      40.545  48.176  72.662  1.00 66.57           O  
-ATOM   3144  N   SER E  19      45.905  45.823  70.477  1.00 26.88           N  
-ATOM   3145  CA  SER E  19      47.077  45.571  71.298  1.00 29.40           C  
-ATOM   3146  C   SER E  19      48.306  46.355  70.801  1.00 35.37           C  
-ATOM   3147  O   SER E  19      49.124  46.765  71.619  1.00 30.71           O  
-ATOM   3148  CB  SER E  19      47.326  44.057  71.368  1.00 30.04           C  
-ATOM   3149  OG  SER E  19      48.430  43.689  70.557  1.00 41.28           O  
-ATOM   3150  N   LEU E  20      48.469  46.579  69.512  1.00 26.65           N  
-ATOM   3151  CA  LEU E  20      49.559  47.392  69.021  1.00 25.63           C  
-ATOM   3152  C   LEU E  20      49.443  48.844  69.472  1.00 25.25           C  
-ATOM   3153  O   LEU E  20      50.427  49.453  69.908  1.00 29.34           O  
-ATOM   3154  CB  LEU E  20      49.672  47.299  67.509  1.00 28.83           C  
-ATOM   3155  CG  LEU E  20      50.481  46.120  66.927  1.00 32.46           C  
-ATOM   3156  CD1 LEU E  20      50.387  46.118  65.416  1.00 29.35           C  
-ATOM   3157  CD2 LEU E  20      51.935  46.179  67.377  1.00 25.23           C  
-ATOM   3158  N   ALA E  21      48.234  49.421  69.367  1.00 25.99           N  
-ATOM   3159  CA  ALA E  21      47.924  50.829  69.766  1.00 31.97           C  
-ATOM   3160  C   ALA E  21      48.233  51.061  71.250  1.00 38.64           C  
-ATOM   3161  O   ALA E  21      48.631  52.164  71.636  1.00 40.62           O  
-ATOM   3162  CB  ALA E  21      46.484  51.166  69.457  1.00 22.96           C  
-ATOM   3163  N   GLU E  22      48.125  50.006  72.061  1.00 38.73           N  
-ATOM   3164  CA  GLU E  22      48.392  50.102  73.490  1.00 42.69           C  
-ATOM   3165  C   GLU E  22      49.828  50.264  73.825  1.00 41.54           C  
-ATOM   3166  O   GLU E  22      50.174  50.771  74.896  1.00 45.61           O  
-ATOM   3167  CB  GLU E  22      47.864  48.881  74.210  1.00 38.73           C  
-ATOM   3168  CG  GLU E  22      46.345  48.814  74.138  1.00 49.31           C  
-ATOM   3169  CD  GLU E  22      45.716  47.846  75.122  1.00 65.48           C  
-ATOM   3170  OE1 GLU E  22      46.443  46.989  75.672  1.00 68.86           O  
-ATOM   3171  OE2 GLU E  22      44.483  47.931  75.328  1.00 67.69           O  
-ATOM   3172  N   VAL E  23      50.629  49.851  72.890  1.00 37.37           N  
-ATOM   3173  CA  VAL E  23      52.029  49.843  73.049  1.00 28.69           C  
-ATOM   3174  C   VAL E  23      52.666  50.963  72.193  1.00 29.40           C  
-ATOM   3175  O   VAL E  23      53.871  51.005  71.941  1.00 36.25           O  
-ATOM   3176  CB  VAL E  23      52.452  48.374  72.779  1.00 44.19           C  
-ATOM   3177  CG1 VAL E  23      53.676  48.353  71.891  1.00 42.78           C  
-ATOM   3178  CG2 VAL E  23      52.718  47.636  74.089  1.00 43.64           C  
-ATOM   3179  N   GLY E  24      51.785  51.844  71.741  1.00 31.41           N  
-ATOM   3180  CA  GLY E  24      52.105  53.078  71.013  1.00 39.48           C  
-ATOM   3181  C   GLY E  24      52.373  52.926  69.498  1.00 42.51           C  
-ATOM   3182  O   GLY E  24      52.934  53.827  68.875  1.00 36.55           O  
-ATOM   3183  N   VAL E  25      52.018  51.833  68.877  1.00 41.49           N  
-ATOM   3184  CA  VAL E  25      52.272  51.621  67.460  1.00 39.91           C  
-ATOM   3185  C   VAL E  25      50.980  51.752  66.673  1.00 40.10           C  
-ATOM   3186  O   VAL E  25      50.068  50.959  66.915  1.00 39.46           O  
-ATOM   3187  CB  VAL E  25      52.861  50.202  67.243  1.00 42.32           C  
-ATOM   3188  CG1 VAL E  25      53.032  49.909  65.745  1.00 47.95           C  
-ATOM   3189  CG2 VAL E  25      54.180  50.046  67.989  1.00 41.92           C  
-ATOM   3190  N   THR E  26      50.799  52.712  65.721  1.00 45.19           N  
-ATOM   3191  CA  THR E  26      49.483  52.798  65.054  1.00 47.21           C  
-ATOM   3192  C   THR E  26      49.443  52.858  63.525  1.00 49.24           C  
-ATOM   3193  O   THR E  26      48.369  52.577  62.987  1.00 52.80           O  
-ATOM   3194  CB  THR E  26      48.723  54.035  65.487  1.00 53.70           C  
-ATOM   3195  OG1 THR E  26      49.608  55.167  65.428  1.00 51.26           O  
-ATOM   3196  CG2 THR E  26      48.191  53.868  66.909  1.00 54.93           C  
-ATOM   3197  N   GLY E  27      50.493  53.209  62.791  1.00 47.61           N  
-ATOM   3198  CA  GLY E  27      50.361  53.260  61.348  1.00 46.89           C  
-ATOM   3199  C   GLY E  27      50.625  51.927  60.628  1.00 47.40           C  
-ATOM   3200  O   GLY E  27      51.673  51.741  60.001  1.00 51.23           O  
-ATOM   3201  N   LEU E  28      49.632  51.023  60.653  1.00 40.50           N  
-ATOM   3202  CA  LEU E  28      49.733  49.736  59.997  1.00 42.10           C  
-ATOM   3203  C   LEU E  28      49.271  49.762  58.522  1.00 36.20           C  
-ATOM   3204  O   LEU E  28      48.355  50.502  58.157  1.00 28.97           O  
-ATOM   3205  CB  LEU E  28      48.864  48.694  60.686  1.00 40.88           C  
-ATOM   3206  CG  LEU E  28      48.654  48.800  62.209  1.00 50.52           C  
-ATOM   3207  CD1 LEU E  28      47.955  47.562  62.755  1.00 46.55           C  
-ATOM   3208  CD2 LEU E  28      49.973  49.017  62.933  1.00 51.18           C  
-ATOM   3209  N   THR E  29      49.918  48.924  57.729  1.00 29.84           N  
-ATOM   3210  CA  THR E  29      49.599  48.673  56.351  1.00 29.02           C  
-ATOM   3211  C   THR E  29      49.108  47.240  56.340  1.00 23.36           C  
-ATOM   3212  O   THR E  29      49.780  46.338  56.861  1.00 27.44           O  
-ATOM   3213  CB  THR E  29      50.815  48.891  55.454  1.00 29.20           C  
-ATOM   3214  OG1 THR E  29      51.255  50.262  55.581  1.00 33.13           O  
-ATOM   3215  CG2 THR E  29      50.463  48.586  54.018  1.00 39.96           C  
-ATOM   3216  N   VAL E  30      47.971  47.037  55.771  1.00 22.46           N  
-ATOM   3217  CA  VAL E  30      47.282  45.763  55.750  1.00 22.74           C  
-ATOM   3218  C   VAL E  30      46.994  45.330  54.303  1.00 28.08           C  
-ATOM   3219  O   VAL E  30      46.409  46.079  53.524  1.00 25.71           O  
-ATOM   3220  CB  VAL E  30      45.975  45.855  56.556  1.00 27.90           C  
-ATOM   3221  CG1 VAL E  30      45.195  44.544  56.468  1.00 28.84           C  
-ATOM   3222  CG2 VAL E  30      46.280  46.209  58.000  1.00 33.69           C  
-ATOM   3223  N   THR E  31      47.440  44.128  53.991  1.00 27.57           N  
-ATOM   3224  CA  THR E  31      47.247  43.522  52.686  1.00 30.74           C  
-ATOM   3225  C   THR E  31      46.558  42.184  52.831  1.00 30.67           C  
-ATOM   3226  O   THR E  31      46.946  41.355  53.654  1.00 27.76           O  
-ATOM   3227  CB  THR E  31      48.586  43.280  51.981  1.00 28.76           C  
-ATOM   3228  OG1 THR E  31      49.406  44.452  52.071  1.00 26.18           O  
-ATOM   3229  CG2 THR E  31      48.339  42.916  50.528  1.00 35.87           C  
-ATOM   3230  N   GLU E  32      45.540  41.959  52.025  1.00 26.84           N  
-ATOM   3231  CA  GLU E  32      44.842  40.695  52.016  1.00 24.22           C  
-ATOM   3232  C   GLU E  32      45.670  39.682  51.227  1.00 29.54           C  
-ATOM   3233  O   GLU E  32      45.938  39.877  50.033  1.00 36.64           O  
-ATOM   3234  CB  GLU E  32      43.423  40.900  51.435  1.00 29.86           C  
-ATOM   3235  CG  GLU E  32      42.450  41.525  52.449  1.00 47.96           C  
-ATOM   3236  CD  GLU E  32      41.275  42.326  51.898  1.00 60.69           C  
-ATOM   3237  OE1 GLU E  32      40.969  42.162  50.704  1.00 54.91           O  
-ATOM   3238  OE2 GLU E  32      40.682  43.108  52.655  1.00 72.34           O  
-ATOM   3239  N   VAL E  33      46.077  38.612  51.892  1.00 25.21           N  
-ATOM   3240  CA  VAL E  33      46.865  37.611  51.206  1.00 25.41           C  
-ATOM   3241  C   VAL E  33      46.221  36.240  51.311  1.00 30.80           C  
-ATOM   3242  O   VAL E  33      45.133  36.093  51.876  1.00 30.48           O  
-ATOM   3243  CB  VAL E  33      48.283  37.613  51.785  1.00 29.84           C  
-ATOM   3244  CG1 VAL E  33      48.908  38.993  51.664  1.00 28.67           C  
-ATOM   3245  CG2 VAL E  33      48.262  37.158  53.230  1.00 32.45           C  
-ATOM   3246  N   LYS E  34      46.895  35.248  50.759  1.00 29.25           N  
-ATOM   3247  CA  LYS E  34      46.426  33.869  50.868  1.00 34.15           C  
-ATOM   3248  C   LYS E  34      47.516  32.938  51.316  1.00 32.90           C  
-ATOM   3249  O   LYS E  34      48.667  33.117  50.929  1.00 30.84           O  
-ATOM   3250  CB  LYS E  34      46.021  33.252  49.520  1.00 38.35           C  
-ATOM   3251  CG  LYS E  34      45.092  34.109  48.690  1.00 45.57           C  
-ATOM   3252  CD  LYS E  34      43.696  34.115  49.282  1.00 53.09           C  
-ATOM   3253  CE  LYS E  34      42.651  34.458  48.237  1.00 66.85           C  
-ATOM   3254  NZ  LYS E  34      42.957  33.855  46.911  1.00 74.17           N  
-ATOM   3255  N   GLY E  35      47.151  31.961  52.123  1.00 32.19           N  
-ATOM   3256  CA  GLY E  35      48.112  31.021  52.602  1.00 43.59           C  
-ATOM   3257  C   GLY E  35      47.747  29.613  52.174  1.00 54.62           C  
-ATOM   3258  O   GLY E  35      46.617  29.355  51.767  1.00 58.59           O  
-ATOM   3259  N   PRO E  57      42.470  32.342  53.425  1.00 44.26           N  
-ATOM   3260  CA  PRO E  57      42.581  33.792  53.474  1.00 40.77           C  
-ATOM   3261  C   PRO E  57      43.291  34.222  54.733  1.00 36.00           C  
-ATOM   3262  O   PRO E  57      43.047  33.635  55.792  1.00 32.99           O  
-ATOM   3263  CB  PRO E  57      41.177  34.335  53.535  1.00 42.84           C  
-ATOM   3264  CG  PRO E  57      40.308  33.146  53.779  1.00 47.20           C  
-ATOM   3265  CD  PRO E  57      41.097  31.866  53.668  1.00 47.87           C  
-ATOM   3266  N   LYS E  58      44.291  35.079  54.636  1.00 29.74           N  
-ATOM   3267  CA  LYS E  58      44.998  35.624  55.802  1.00 24.27           C  
-ATOM   3268  C   LYS E  58      45.126  37.113  55.601  1.00 32.55           C  
-ATOM   3269  O   LYS E  58      44.784  37.650  54.537  1.00 26.63           O  
-ATOM   3270  CB  LYS E  58      46.355  34.911  55.957  1.00 23.07           C  
-ATOM   3271  CG  LYS E  58      46.214  33.489  56.496  1.00 38.79           C  
-ATOM   3272  CD  LYS E  58      47.305  32.501  56.419  1.00 52.72           C  
-ATOM   3273  CE  LYS E  58      47.399  31.644  57.688  1.00 54.99           C  
-ATOM   3274  NZ  LYS E  58      46.119  31.061  58.147  1.00 46.11           N  
-ATOM   3275  N   VAL E  59      45.672  37.828  56.599  1.00 28.12           N  
-ATOM   3276  CA  VAL E  59      45.943  39.242  56.454  1.00 27.93           C  
-ATOM   3277  C   VAL E  59      47.404  39.384  56.770  1.00 27.38           C  
-ATOM   3278  O   VAL E  59      47.940  38.764  57.726  1.00 27.56           O  
-ATOM   3279  CB  VAL E  59      45.035  40.026  57.439  1.00 32.20           C  
-ATOM   3280  CG1 VAL E  59      45.556  41.414  57.728  1.00 43.34           C  
-ATOM   3281  CG2 VAL E  59      43.620  39.980  56.916  1.00 29.09           C  
-ATOM   3282  N   LYS E  60      48.074  40.233  56.014  1.00 24.43           N  
-ATOM   3283  CA  LYS E  60      49.453  40.593  56.293  1.00 24.17           C  
-ATOM   3284  C   LYS E  60      49.438  42.014  56.902  1.00 28.07           C  
-ATOM   3285  O   LYS E  60      48.764  42.904  56.341  1.00 27.88           O  
-ATOM   3286  CB  LYS E  60      50.384  40.558  55.115  1.00 21.08           C  
-ATOM   3287  CG  LYS E  60      51.746  41.084  55.598  1.00 22.60           C  
-ATOM   3288  CD  LYS E  60      52.630  41.478  54.414  1.00 42.39           C  
-ATOM   3289  CE  LYS E  60      52.900  40.437  53.401  1.00 37.14           C  
-ATOM   3290  NZ  LYS E  60      54.013  40.825  52.437  1.00 35.26           N  
-ATOM   3291  N   ILE E  61      50.143  42.154  58.021  1.00 25.07           N  
-ATOM   3292  CA  ILE E  61      50.164  43.490  58.624  1.00 20.36           C  
-ATOM   3293  C   ILE E  61      51.608  43.929  58.553  1.00 22.35           C  
-ATOM   3294  O   ILE E  61      52.479  43.066  58.740  1.00 23.65           O  
-ATOM   3295  CB  ILE E  61      49.601  43.467  60.062  1.00 33.39           C  
-ATOM   3296  CG1 ILE E  61      48.091  43.211  60.147  1.00 28.62           C  
-ATOM   3297  CG2 ILE E  61      49.851  44.796  60.774  1.00 46.29           C  
-ATOM   3298  CD1 ILE E  61      47.719  42.750  61.574  1.00 46.50           C  
-ATOM   3299  N   GLU E  62      51.925  45.198  58.182  1.00 20.71           N  
-ATOM   3300  CA  GLU E  62      53.356  45.549  58.187  1.00 23.23           C  
-ATOM   3301  C   GLU E  62      53.539  46.862  58.950  1.00 30.95           C  
-ATOM   3302  O   GLU E  62      52.708  47.736  58.803  1.00 26.25           O  
-ATOM   3303  CB  GLU E  62      53.883  45.953  56.777  1.00 33.58           C  
-ATOM   3304  CG  GLU E  62      54.058  44.695  55.926  1.00 32.71           C  
-ATOM   3305  CD  GLU E  62      54.104  45.018  54.430  1.00 37.98           C  
-ATOM   3306  OE1 GLU E  62      53.295  45.743  53.827  1.00 34.40           O  
-ATOM   3307  OE2 GLU E  62      54.995  44.496  53.770  1.00 38.12           O  
-ATOM   3308  N   VAL E  63      54.614  46.995  59.765  1.00 31.23           N  
-ATOM   3309  CA  VAL E  63      54.790  48.307  60.396  1.00 33.06           C  
-ATOM   3310  C   VAL E  63      56.310  48.554  60.389  1.00 24.08           C  
-ATOM   3311  O   VAL E  63      57.048  47.598  60.512  1.00 25.41           O  
-ATOM   3312  CB  VAL E  63      54.314  48.448  61.867  1.00 46.96           C  
-ATOM   3313  CG1 VAL E  63      54.109  49.966  62.134  1.00 49.63           C  
-ATOM   3314  CG2 VAL E  63      53.022  47.805  62.269  1.00 47.61           C  
-ATOM   3315  N   VAL E  64      56.685  49.801  60.290  1.00 27.00           N  
-ATOM   3316  CA  VAL E  64      58.059  50.251  60.372  1.00 30.49           C  
-ATOM   3317  C   VAL E  64      58.275  51.012  61.681  1.00 34.03           C  
-ATOM   3318  O   VAL E  64      57.544  51.923  61.989  1.00 35.91           O  
-ATOM   3319  CB  VAL E  64      58.584  51.132  59.217  1.00 36.23           C  
-ATOM   3320  CG1 VAL E  64      60.052  51.493  59.473  1.00 37.51           C  
-ATOM   3321  CG2 VAL E  64      58.470  50.229  57.974  1.00 33.88           C  
-ATOM   3322  N   VAL E  65      59.121  50.458  62.568  1.00 30.29           N  
-ATOM   3323  CA  VAL E  65      59.243  51.155  63.856  1.00 31.25           C  
-ATOM   3324  C   VAL E  65      60.711  51.407  64.169  1.00 32.42           C  
-ATOM   3325  O   VAL E  65      61.604  50.673  63.737  1.00 29.75           O  
-ATOM   3326  CB  VAL E  65      58.595  50.329  64.996  1.00 35.83           C  
-ATOM   3327  CG1 VAL E  65      57.063  50.223  64.925  1.00 35.36           C  
-ATOM   3328  CG2 VAL E  65      59.166  48.905  65.034  1.00 40.71           C  
-ATOM   3329  N   ASP E  66      60.895  52.251  65.172  1.00 38.55           N  
-ATOM   3330  CA  ASP E  66      62.245  52.395  65.777  1.00 39.48           C  
-ATOM   3331  C   ASP E  66      62.795  51.088  66.281  1.00 34.26           C  
-ATOM   3332  O   ASP E  66      62.069  50.245  66.829  1.00 34.13           O  
-ATOM   3333  CB  ASP E  66      62.135  53.409  66.926  1.00 52.17           C  
-ATOM   3334  CG  ASP E  66      63.512  53.856  67.404  1.00 57.12           C  
-ATOM   3335  OD1 ASP E  66      64.067  53.126  68.242  1.00 53.55           O  
-ATOM   3336  OD2 ASP E  66      64.031  54.895  66.943  1.00 65.52           O  
-ATOM   3337  N   ASP E  67      64.093  50.841  66.225  1.00 34.23           N  
-ATOM   3338  CA  ASP E  67      64.678  49.627  66.827  1.00 39.01           C  
-ATOM   3339  C   ASP E  67      64.292  49.276  68.288  1.00 43.79           C  
-ATOM   3340  O   ASP E  67      64.049  48.116  68.668  1.00 38.42           O  
-ATOM   3341  CB  ASP E  67      66.183  49.785  66.819  1.00 41.31           C  
-ATOM   3342  CG  ASP E  67      66.755  49.830  65.410  1.00 50.31           C  
-ATOM   3343  OD1 ASP E  67      66.036  49.898  64.390  1.00 48.57           O  
-ATOM   3344  OD2 ASP E  67      67.987  49.803  65.303  1.00 40.72           O  
-ATOM   3345  N   LYS E  68      64.078  50.292  69.095  1.00 42.24           N  
-ATOM   3346  CA  LYS E  68      63.776  50.114  70.518  1.00 50.18           C  
-ATOM   3347  C   LYS E  68      62.329  49.748  70.743  1.00 47.16           C  
-ATOM   3348  O   LYS E  68      61.958  49.287  71.819  1.00 50.63           O  
-ATOM   3349  CB  LYS E  68      64.183  51.418  71.265  1.00 54.18           C  
-ATOM   3350  CG  LYS E  68      65.622  51.830  71.035  1.00 71.96           C  
-ATOM   3351  CD  LYS E  68      66.222  52.762  72.067  1.00 78.19           C  
-ATOM   3352  CE  LYS E  68      67.686  53.078  71.781  1.00 91.52           C  
-ATOM   3353  NZ  LYS E  68      68.284  53.808  72.943  1.00 97.88           N  
-ATOM   3354  N   VAL E  69      61.487  49.857  69.690  1.00 44.84           N  
-ATOM   3355  CA  VAL E  69      60.086  49.456  69.866  1.00 38.05           C  
-ATOM   3356  C   VAL E  69      59.868  48.034  69.370  1.00 36.54           C  
-ATOM   3357  O   VAL E  69      58.812  47.452  69.589  1.00 38.99           O  
-ATOM   3358  CB  VAL E  69      59.280  50.500  69.103  1.00 42.01           C  
-ATOM   3359  CG1 VAL E  69      57.787  50.280  69.035  1.00 43.76           C  
-ATOM   3360  CG2 VAL E  69      59.507  51.885  69.702  1.00 45.90           C  
-ATOM   3361  N   VAL E  70      60.839  47.388  68.727  1.00 30.24           N  
-ATOM   3362  CA  VAL E  70      60.532  46.093  68.121  1.00 36.00           C  
-ATOM   3363  C   VAL E  70      60.007  45.124  69.153  1.00 36.20           C  
-ATOM   3364  O   VAL E  70      59.075  44.376  68.874  1.00 27.86           O  
-ATOM   3365  CB  VAL E  70      61.754  45.497  67.375  1.00 40.06           C  
-ATOM   3366  CG1 VAL E  70      61.573  44.056  66.898  1.00 33.62           C  
-ATOM   3367  CG2 VAL E  70      61.925  46.406  66.142  1.00 35.29           C  
-ATOM   3368  N   GLU E  71      60.679  44.980  70.310  1.00 28.80           N  
-ATOM   3369  CA  GLU E  71      60.321  43.941  71.270  1.00 30.68           C  
-ATOM   3370  C   GLU E  71      58.856  44.025  71.690  1.00 23.99           C  
-ATOM   3371  O   GLU E  71      58.106  43.056  71.628  1.00 24.08           O  
-ATOM   3372  CB  GLU E  71      61.126  44.044  72.578  1.00 34.97           C  
-ATOM   3373  CG  GLU E  71      62.631  44.085  72.535  1.00 58.62           C  
-ATOM   3374  CD  GLU E  71      63.183  44.408  73.913  1.00 72.27           C  
-ATOM   3375  OE1 GLU E  71      62.746  43.777  74.909  1.00 57.39           O  
-ATOM   3376  OE2 GLU E  71      64.059  45.305  73.995  1.00 69.63           O  
-ATOM   3377  N   GLN E  72      58.479  45.229  72.132  1.00 28.65           N  
-ATOM   3378  CA  GLN E  72      57.097  45.547  72.554  1.00 33.96           C  
-ATOM   3379  C   GLN E  72      56.098  45.079  71.503  1.00 31.40           C  
-ATOM   3380  O   GLN E  72      55.186  44.288  71.796  1.00 32.11           O  
-ATOM   3381  CB  GLN E  72      56.839  47.076  72.639  1.00 40.88           C  
-ATOM   3382  CG  GLN E  72      57.174  47.881  73.868  1.00 56.54           C  
-ATOM   3383  CD  GLN E  72      57.589  49.288  73.486  1.00 52.14           C  
-ATOM   3384  OE1 GLN E  72      56.737  50.159  73.284  1.00 42.59           O  
-ATOM   3385  NE2 GLN E  72      58.838  49.724  73.321  1.00 39.57           N  
-ATOM   3386  N   ALA E  73      56.290  45.588  70.272  1.00 32.55           N  
-ATOM   3387  CA  ALA E  73      55.393  45.285  69.159  1.00 27.69           C  
-ATOM   3388  C   ALA E  73      55.295  43.778  68.889  1.00 22.36           C  
-ATOM   3389  O   ALA E  73      54.178  43.270  68.740  1.00 28.16           O  
-ATOM   3390  CB  ALA E  73      55.848  46.028  67.908  1.00 26.76           C  
-ATOM   3391  N   VAL E  74      56.414  43.043  68.814  1.00 27.07           N  
-ATOM   3392  CA  VAL E  74      56.333  41.600  68.544  1.00 29.33           C  
-ATOM   3393  C   VAL E  74      55.481  40.913  69.602  1.00 31.68           C  
-ATOM   3394  O   VAL E  74      54.595  40.104  69.297  1.00 27.10           O  
-ATOM   3395  CB  VAL E  74      57.735  40.981  68.512  1.00 31.78           C  
-ATOM   3396  CG1 VAL E  74      57.652  39.470  68.595  1.00 32.25           C  
-ATOM   3397  CG2 VAL E  74      58.470  41.417  67.246  1.00 35.95           C  
-ATOM   3398  N   ASP E  75      55.783  41.261  70.883  1.00 30.63           N  
-ATOM   3399  CA  ASP E  75      55.075  40.743  72.029  1.00 34.80           C  
-ATOM   3400  C   ASP E  75      53.585  41.139  71.993  1.00 29.03           C  
-ATOM   3401  O   ASP E  75      52.761  40.345  72.430  1.00 25.89           O  
-ATOM   3402  CB  ASP E  75      55.762  41.184  73.323  1.00 46.38           C  
-ATOM   3403  CG  ASP E  75      57.119  40.480  73.516  1.00 70.85           C  
-ATOM   3404  OD1 ASP E  75      57.317  39.388  72.932  1.00 75.50           O  
-ATOM   3405  OD2 ASP E  75      57.960  41.019  74.258  1.00 82.94           O  
-ATOM   3406  N   ALA E  76      53.268  42.310  71.498  1.00 25.98           N  
-ATOM   3407  CA  ALA E  76      51.878  42.632  71.433  1.00 31.40           C  
-ATOM   3408  C   ALA E  76      51.129  41.872  70.324  1.00 33.83           C  
-ATOM   3409  O   ALA E  76      49.942  41.556  70.486  1.00 28.68           O  
-ATOM   3410  CB  ALA E  76      51.690  44.128  71.246  1.00 24.78           C  
-ATOM   3411  N   ILE E  77      51.783  41.559  69.241  1.00 29.92           N  
-ATOM   3412  CA  ILE E  77      51.174  40.817  68.172  1.00 29.15           C  
-ATOM   3413  C   ILE E  77      50.957  39.392  68.587  1.00 22.81           C  
-ATOM   3414  O   ILE E  77      49.897  38.835  68.307  1.00 23.47           O  
-ATOM   3415  CB  ILE E  77      52.047  40.848  66.907  1.00 26.40           C  
-ATOM   3416  CG1 ILE E  77      51.932  42.223  66.271  1.00 24.90           C  
-ATOM   3417  CG2 ILE E  77      51.641  39.750  65.932  1.00 25.33           C  
-ATOM   3418  CD1 ILE E  77      52.950  42.478  65.181  1.00 36.83           C  
-ATOM   3419  N   ILE E  78      51.926  38.809  69.238  1.00 23.47           N  
-ATOM   3420  CA  ILE E  78      51.836  37.404  69.657  1.00 31.88           C  
-ATOM   3421  C   ILE E  78      50.694  37.151  70.619  1.00 29.08           C  
-ATOM   3422  O   ILE E  78      49.964  36.163  70.468  1.00 30.15           O  
-ATOM   3423  CB  ILE E  78      53.167  36.950  70.286  1.00 40.02           C  
-ATOM   3424  CG1 ILE E  78      54.115  36.389  69.219  1.00 43.54           C  
-ATOM   3425  CG2 ILE E  78      52.909  35.917  71.380  1.00 52.15           C  
-ATOM   3426  CD1 ILE E  78      55.566  36.361  69.641  1.00 43.39           C  
-ATOM   3427  N   LYS E  79      50.531  38.064  71.582  1.00 31.05           N  
-ATOM   3428  CA  LYS E  79      49.480  37.924  72.591  1.00 32.23           C  
-ATOM   3429  C   LYS E  79      48.087  38.023  71.950  1.00 34.35           C  
-ATOM   3430  O   LYS E  79      47.200  37.226  72.259  1.00 35.11           O  
-ATOM   3431  CB  LYS E  79      49.680  38.972  73.696  1.00 28.87           C  
-ATOM   3432  CG  LYS E  79      50.579  38.485  74.838  1.00 41.53           C  
-ATOM   3433  CD  LYS E  79      51.099  39.617  75.712  1.00 48.37           C  
-ATOM   3434  CE  LYS E  79      51.958  39.074  76.845  1.00 58.28           C  
-ATOM   3435  NZ  LYS E  79      52.873  40.112  77.396  1.00 62.89           N  
-ATOM   3436  N   ALA E  80      47.922  38.979  71.054  1.00 27.21           N  
-ATOM   3437  CA  ALA E  80      46.639  39.192  70.420  1.00 29.20           C  
-ATOM   3438  C   ALA E  80      46.307  38.222  69.258  1.00 28.74           C  
-ATOM   3439  O   ALA E  80      45.130  37.912  69.062  1.00 30.86           O  
-ATOM   3440  CB  ALA E  80      46.540  40.622  69.918  1.00 26.75           C  
-ATOM   3441  N   ALA E  81      47.294  37.739  68.490  1.00 28.59           N  
-ATOM   3442  CA  ALA E  81      46.928  36.879  67.345  1.00 25.30           C  
-ATOM   3443  C   ALA E  81      46.838  35.389  67.664  1.00 33.92           C  
-ATOM   3444  O   ALA E  81      46.213  34.636  66.914  1.00 27.79           O  
-ATOM   3445  CB  ALA E  81      47.896  37.118  66.201  1.00 27.62           C  
-ATOM   3446  N   ARG E  82      47.470  34.935  68.749  1.00 29.19           N  
-ATOM   3447  CA  ARG E  82      47.503  33.527  69.135  1.00 26.87           C  
-ATOM   3448  C   ARG E  82      46.133  32.999  69.427  1.00 31.18           C  
-ATOM   3449  O   ARG E  82      45.239  33.701  69.908  1.00 30.31           O  
-ATOM   3450  CB  ARG E  82      48.480  33.373  70.322  1.00 29.61           C  
-ATOM   3451  CG  ARG E  82      48.338  32.117  71.172  1.00 31.60           C  
-ATOM   3452  CD  ARG E  82      49.604  31.889  71.981  1.00 25.44           C  
-ATOM   3453  NE  ARG E  82      50.000  30.493  71.910  1.00 30.40           N  
-ATOM   3454  CZ  ARG E  82      49.265  29.524  72.395  1.00 31.29           C  
-ATOM   3455  NH1 ARG E  82      48.112  29.804  72.970  1.00 22.79           N  
-ATOM   3456  NH2 ARG E  82      49.682  28.281  72.323  1.00 29.85           N  
-ATOM   3457  N   THR E  83      45.971  31.743  69.119  1.00 28.29           N  
-ATOM   3458  CA  THR E  83      44.734  31.037  69.278  1.00 29.16           C  
-ATOM   3459  C   THR E  83      45.043  29.686  69.895  1.00 31.24           C  
-ATOM   3460  O   THR E  83      44.255  29.128  70.661  1.00 28.97           O  
-ATOM   3461  CB  THR E  83      44.063  30.854  67.907  1.00 41.60           C  
-ATOM   3462  OG1 THR E  83      42.643  31.049  68.042  1.00 50.67           O  
-ATOM   3463  CG2 THR E  83      44.323  29.448  67.373  1.00 23.78           C  
-ATOM   3464  N   GLY E  84      46.204  29.147  69.574  1.00 25.75           N  
-ATOM   3465  CA  GLY E  84      46.563  27.847  70.093  1.00 30.42           C  
-ATOM   3466  C   GLY E  84      46.284  26.782  69.030  1.00 33.14           C  
-ATOM   3467  O   GLY E  84      46.614  25.616  69.217  1.00 32.07           O  
-ATOM   3468  N   LYS E  85      45.691  27.191  67.900  1.00 31.22           N  
-ATOM   3469  CA  LYS E  85      45.393  26.277  66.802  1.00 31.76           C  
-ATOM   3470  C   LYS E  85      46.475  26.409  65.702  1.00 37.16           C  
-ATOM   3471  O   LYS E  85      47.083  27.459  65.527  1.00 42.66           O  
-ATOM   3472  CB  LYS E  85      44.041  26.602  66.161  1.00 31.12           C  
-ATOM   3473  CG  LYS E  85      42.811  26.207  66.984  1.00 53.50           C  
-ATOM   3474  CD  LYS E  85      41.551  26.314  66.156  1.00 50.06           C  
-ATOM   3475  CE  LYS E  85      40.323  26.458  67.041  1.00 61.66           C  
-ATOM   3476  NZ  LYS E  85      39.194  27.096  66.313  1.00 74.07           N  
-ATOM   3477  N   ILE E  86      46.715  25.310  64.969  1.00 37.29           N  
-ATOM   3478  CA  ILE E  86      47.711  25.300  63.890  1.00 42.44           C  
-ATOM   3479  C   ILE E  86      47.224  26.278  62.833  1.00 35.88           C  
-ATOM   3480  O   ILE E  86      46.028  26.293  62.497  1.00 37.90           O  
-ATOM   3481  CB  ILE E  86      47.975  23.885  63.358  1.00 52.20           C  
-ATOM   3482  CG1 ILE E  86      48.562  23.021  64.467  1.00 60.19           C  
-ATOM   3483  CG2 ILE E  86      48.911  23.915  62.154  1.00 58.70           C  
-ATOM   3484  CD1 ILE E  86      48.272  21.544  64.309  1.00 47.42           C  
-ATOM   3485  N   GLY E  87      48.117  27.097  62.328  1.00 34.75           N  
-ATOM   3486  CA  GLY E  87      47.801  28.062  61.333  1.00 28.88           C  
-ATOM   3487  C   GLY E  87      47.772  29.491  61.883  1.00 37.37           C  
-ATOM   3488  O   GLY E  87      47.432  30.421  61.168  1.00 30.39           O  
-ATOM   3489  N   ASP E  88      48.145  29.687  63.160  1.00 25.24           N  
-ATOM   3490  CA  ASP E  88      48.090  31.030  63.715  1.00 27.17           C  
-ATOM   3491  C   ASP E  88      48.996  32.018  62.980  1.00 27.87           C  
-ATOM   3492  O   ASP E  88      48.685  33.210  62.987  1.00 27.43           O  
-ATOM   3493  CB  ASP E  88      48.481  31.024  65.181  1.00 27.96           C  
-ATOM   3494  CG  ASP E  88      47.365  30.602  66.102  1.00 35.46           C  
-ATOM   3495  OD1 ASP E  88      46.170  30.621  65.705  1.00 30.71           O  
-ATOM   3496  OD2 ASP E  88      47.675  30.236  67.259  1.00 31.63           O  
-ATOM   3497  N   GLY E  89      50.080  31.608  62.352  1.00 23.37           N  
-ATOM   3498  CA  GLY E  89      50.869  32.594  61.629  1.00 23.77           C  
-ATOM   3499  C   GLY E  89      52.293  32.749  62.153  1.00 27.27           C  
-ATOM   3500  O   GLY E  89      52.734  31.969  63.002  1.00 26.69           O  
-ATOM   3501  N   LYS E  90      52.972  33.751  61.613  1.00 26.48           N  
-ATOM   3502  CA  LYS E  90      54.345  34.031  61.980  1.00 26.51           C  
-ATOM   3503  C   LYS E  90      54.618  35.524  61.955  1.00 26.34           C  
-ATOM   3504  O   LYS E  90      53.874  36.281  61.336  1.00 26.30           O  
-ATOM   3505  CB  LYS E  90      55.354  33.449  60.992  1.00 20.77           C  
-ATOM   3506  CG  LYS E  90      55.178  31.981  60.708  1.00 33.70           C  
-ATOM   3507  CD  LYS E  90      56.508  31.343  60.346  1.00 33.86           C  
-ATOM   3508  CE  LYS E  90      56.320  29.868  60.061  1.00 41.75           C  
-ATOM   3509  NZ  LYS E  90      57.428  29.315  59.227  1.00 26.63           N  
-ATOM   3510  N   ILE E  91      55.680  35.955  62.605  1.00 26.01           N  
-ATOM   3511  CA  ILE E  91      56.091  37.361  62.587  1.00 24.33           C  
-ATOM   3512  C   ILE E  91      57.497  37.394  62.021  1.00 29.59           C  
-ATOM   3513  O   ILE E  91      58.311  36.531  62.459  1.00 26.57           O  
-ATOM   3514  CB  ILE E  91      56.134  37.882  64.041  1.00 27.26           C  
-ATOM   3515  CG1 ILE E  91      54.727  37.827  64.705  1.00 28.28           C  
-ATOM   3516  CG2 ILE E  91      56.560  39.354  63.965  1.00 21.67           C  
-ATOM   3517  CD1 ILE E  91      54.809  37.981  66.260  1.00 33.08           C  
-ATOM   3518  N   PHE E  92      57.830  38.371  61.158  1.00 25.06           N  
-ATOM   3519  CA  PHE E  92      59.221  38.522  60.706  1.00 27.48           C  
-ATOM   3520  C   PHE E  92      59.673  39.948  60.968  1.00 25.63           C  
-ATOM   3521  O   PHE E  92      58.905  40.920  60.915  1.00 27.09           O  
-ATOM   3522  CB  PHE E  92      59.449  38.279  59.224  1.00 33.31           C  
-ATOM   3523  CG  PHE E  92      58.662  37.157  58.716  1.00 28.75           C  
-ATOM   3524  CD1 PHE E  92      57.533  37.429  57.971  1.00 32.74           C  
-ATOM   3525  CD2 PHE E  92      59.059  35.834  58.943  1.00 35.78           C  
-ATOM   3526  CE1 PHE E  92      56.771  36.396  57.475  1.00 40.43           C  
-ATOM   3527  CE2 PHE E  92      58.299  34.794  58.434  1.00 41.14           C  
-ATOM   3528  CZ  PHE E  92      57.146  35.078  57.704  1.00 39.10           C  
-ATOM   3529  N   VAL E  93      60.987  40.023  61.248  1.00 28.90           N  
-ATOM   3530  CA  VAL E  93      61.623  41.307  61.439  1.00 29.30           C  
-ATOM   3531  C   VAL E  93      62.707  41.495  60.383  1.00 28.27           C  
-ATOM   3532  O   VAL E  93      63.506  40.589  60.134  1.00 30.51           O  
-ATOM   3533  CB  VAL E  93      62.194  41.457  62.870  1.00 37.33           C  
-ATOM   3534  CG1 VAL E  93      62.946  42.770  62.973  1.00 32.49           C  
-ATOM   3535  CG2 VAL E  93      61.085  41.361  63.919  1.00 28.63           C  
-ATOM   3536  N   GLN E  94      62.773  42.667  59.780  1.00 28.52           N  
-ATOM   3537  CA  GLN E  94      63.818  42.971  58.794  1.00 33.61           C  
-ATOM   3538  C   GLN E  94      64.348  44.373  58.976  1.00 27.37           C  
-ATOM   3539  O   GLN E  94      63.651  45.253  59.506  1.00 30.00           O  
-ATOM   3540  CB  GLN E  94      63.264  42.887  57.356  1.00 25.25           C  
-ATOM   3541  CG  GLN E  94      62.898  41.515  56.837  1.00 26.32           C  
-ATOM   3542  CD  GLN E  94      62.225  41.525  55.482  1.00 42.09           C  
-ATOM   3543  OE1 GLN E  94      61.306  42.323  55.226  1.00 50.89           O  
-ATOM   3544  NE2 GLN E  94      62.517  40.725  54.462  1.00 45.03           N  
-ATOM   3545  N   GLU E  95      65.564  44.600  58.519  1.00 30.35           N  
-ATOM   3546  CA  GLU E  95      66.183  45.914  58.598  1.00 37.44           C  
-ATOM   3547  C   GLU E  95      65.628  46.837  57.506  1.00 38.22           C  
-ATOM   3548  O   GLU E  95      65.307  46.391  56.402  1.00 33.00           O  
-ATOM   3549  CB  GLU E  95      67.706  45.817  58.366  1.00 48.02           C  
-ATOM   3550  CG  GLU E  95      68.588  46.130  59.559  1.00 59.21           C  
-ATOM   3551  CD  GLU E  95      68.469  47.583  60.024  1.00 52.55           C  
-ATOM   3552  OE1 GLU E  95      69.028  48.480  59.343  1.00 60.87           O  
-ATOM   3553  OE2 GLU E  95      67.821  47.807  61.071  1.00 62.20           O  
-ATOM   3554  N   VAL E  96      65.511  48.113  57.794  1.00 33.28           N  
-ATOM   3555  CA  VAL E  96      65.152  49.115  56.804  1.00 36.91           C  
-ATOM   3556  C   VAL E  96      66.270  50.133  56.778  1.00 38.81           C  
-ATOM   3557  O   VAL E  96      66.518  50.774  57.799  1.00 38.76           O  
-ATOM   3558  CB  VAL E  96      63.843  49.843  57.147  1.00 34.15           C  
-ATOM   3559  CG1 VAL E  96      63.380  50.715  55.989  1.00 31.91           C  
-ATOM   3560  CG2 VAL E  96      62.752  48.833  57.507  1.00 38.74           C  
-ATOM   3561  N   GLU E  97      66.979  50.358  55.646  1.00 37.13           N  
-ATOM   3562  CA  GLU E  97      68.076  51.341  55.799  1.00 38.89           C  
-ATOM   3563  C   GLU E  97      67.572  52.776  55.794  1.00 38.05           C  
-ATOM   3564  O   GLU E  97      68.190  53.623  56.432  1.00 39.19           O  
-ATOM   3565  CB  GLU E  97      69.175  51.192  54.745  1.00 39.49           C  
-ATOM   3566  CG  GLU E  97      68.861  50.367  53.513  1.00 50.68           C  
-ATOM   3567  CD  GLU E  97      70.154  50.089  52.757  1.00 63.26           C  
-ATOM   3568  OE1 GLU E  97      70.569  50.966  51.966  1.00 68.21           O  
-ATOM   3569  OE2 GLU E  97      70.735  49.001  52.946  1.00 63.12           O  
-ATOM   3570  N   GLN E  98      66.498  53.068  55.112  1.00 39.19           N  
-ATOM   3571  CA  GLN E  98      65.993  54.427  55.076  1.00 33.76           C  
-ATOM   3572  C   GLN E  98      64.489  54.464  55.121  1.00 33.21           C  
-ATOM   3573  O   GLN E  98      63.798  53.620  54.539  1.00 31.30           O  
-ATOM   3574  CB  GLN E  98      66.469  55.133  53.779  1.00 43.32           C  
-ATOM   3575  CG  GLN E  98      67.961  55.020  53.415  1.00 58.65           C  
-ATOM   3576  CD  GLN E  98      68.305  55.385  51.967  1.00 74.48           C  
-ATOM   3577  OE1 GLN E  98      67.802  56.378  51.416  1.00 80.67           O  
-ATOM   3578  NE2 GLN E  98      69.128  54.724  51.172  1.00 74.95           N  
-ATOM   3579  N   VAL E  99      63.988  55.462  55.798  1.00 29.53           N  
-ATOM   3580  CA  VAL E  99      62.549  55.706  55.820  1.00 33.23           C  
-ATOM   3581  C   VAL E  99      62.374  57.225  55.556  1.00 40.28           C  
-ATOM   3582  O   VAL E  99      63.034  58.053  56.197  1.00 41.64           O  
-ATOM   3583  CB  VAL E  99      61.889  55.377  57.164  1.00 41.07           C  
-ATOM   3584  CG1 VAL E  99      60.398  55.652  57.112  1.00 41.20           C  
-ATOM   3585  CG2 VAL E  99      62.140  53.923  57.547  1.00 39.51           C  
-ATOM   3586  N   ILE E 100      61.504  57.592  54.614  1.00 38.37           N  
-ATOM   3587  CA  ILE E 100      61.277  58.979  54.289  1.00 38.25           C  
-ATOM   3588  C   ILE E 100      59.788  59.281  54.338  1.00 39.24           C  
-ATOM   3589  O   ILE E 100      58.979  58.510  53.830  1.00 40.09           O  
-ATOM   3590  CB  ILE E 100      61.784  59.320  52.868  1.00 37.89           C  
-ATOM   3591  CG1 ILE E 100      63.260  58.914  52.740  1.00 41.07           C  
-ATOM   3592  CG2 ILE E 100      61.619  60.813  52.566  1.00 38.96           C  
-ATOM   3593  CD1 ILE E 100      63.581  58.120  51.485  1.00 43.26           C  
-ATOM   3594  N   ARG E 101      59.411  60.393  54.942  1.00 32.10           N  
-ATOM   3595  CA  ARG E 101      58.010  60.776  55.057  1.00 33.87           C  
-ATOM   3596  C   ARG E 101      57.777  61.690  53.875  1.00 36.74           C  
-ATOM   3597  O   ARG E 101      58.616  62.596  53.717  1.00 39.50           O  
-ATOM   3598  CB  ARG E 101      57.676  61.473  56.393  1.00 48.76           C  
-ATOM   3599  CG  ARG E 101      56.206  61.840  56.522  1.00 57.03           C  
-ATOM   3600  CD  ARG E 101      55.921  62.800  57.662  1.00 66.74           C  
-ATOM   3601  NE  ARG E 101      56.132  62.204  58.980  1.00 68.97           N  
-ATOM   3602  CZ  ARG E 101      55.315  61.321  59.546  1.00 76.04           C  
-ATOM   3603  NH1 ARG E 101      54.208  60.922  58.915  1.00 78.22           N  
-ATOM   3604  NH2 ARG E 101      55.626  60.845  60.747  1.00 74.16           N  
-ATOM   3605  N   ILE E 102      56.824  61.368  53.012  1.00 39.25           N  
-ATOM   3606  CA  ILE E 102      56.775  62.070  51.716  1.00 40.20           C  
-ATOM   3607  C   ILE E 102      56.466  63.546  51.885  1.00 39.31           C  
-ATOM   3608  O   ILE E 102      57.170  64.386  51.321  1.00 38.33           O  
-ATOM   3609  CB  ILE E 102      55.792  61.378  50.760  1.00 41.14           C  
-ATOM   3610  CG1 ILE E 102      56.367  60.006  50.290  1.00 39.76           C  
-ATOM   3611  CG2 ILE E 102      55.515  62.290  49.564  1.00 41.24           C  
-ATOM   3612  CD1 ILE E 102      55.307  59.203  49.524  1.00 34.04           C  
-ATOM   3613  N   ARG E 103      55.395  63.796  52.624  1.00 37.59           N  
-ATOM   3614  CA  ARG E 103      54.969  65.138  52.933  1.00 46.21           C  
-ATOM   3615  C   ARG E 103      56.099  66.044  53.398  1.00 48.29           C  
-ATOM   3616  O   ARG E 103      56.028  67.164  52.939  1.00 47.73           O  
-ATOM   3617  CB  ARG E 103      53.834  65.179  53.966  1.00 48.45           C  
-ATOM   3618  CG  ARG E 103      53.193  66.561  54.087  1.00 58.06           C  
-ATOM   3619  CD  ARG E 103      52.229  66.656  55.265  1.00 69.45           C  
-ATOM   3620  NE  ARG E 103      51.571  67.950  55.421  1.00 83.26           N  
-ATOM   3621  CZ  ARG E 103      50.688  68.317  56.358  1.00 89.30           C  
-ATOM   3622  NH1 ARG E 103      50.289  67.479  57.316  1.00 87.19           N  
-ATOM   3623  NH2 ARG E 103      50.164  69.549  56.366  1.00 74.58           N  
-ATOM   3624  N   THR E 104      57.029  65.720  54.270  1.00 48.71           N  
-ATOM   3625  CA  THR E 104      57.969  66.692  54.787  1.00 51.91           C  
-ATOM   3626  C   THR E 104      59.399  66.455  54.353  1.00 54.85           C  
-ATOM   3627  O   THR E 104      60.293  67.285  54.592  1.00 55.68           O  
-ATOM   3628  CB  THR E 104      58.000  66.596  56.337  1.00 52.50           C  
-ATOM   3629  OG1 THR E 104      58.245  65.200  56.624  1.00 56.48           O  
-ATOM   3630  CG2 THR E 104      56.672  66.951  56.962  1.00 48.46           C  
-ATOM   3631  N   GLY E 105      59.662  65.206  53.934  1.00 50.69           N  
-ATOM   3632  CA  GLY E 105      61.068  64.869  53.665  1.00 51.64           C  
-ATOM   3633  C   GLY E 105      61.777  64.527  54.976  1.00 51.87           C  
-ATOM   3634  O   GLY E 105      62.968  64.199  54.922  1.00 50.26           O  
-TER    3635      GLY E 105                                                      
-ATOM   3636  N   MET F   1      71.904  45.817  45.519  1.00 80.89           N  
-ATOM   3637  CA  MET F   1      70.589  46.167  44.939  1.00 76.03           C  
-ATOM   3638  C   MET F   1      69.659  46.711  46.010  1.00 66.78           C  
-ATOM   3639  O   MET F   1      69.840  46.406  47.174  1.00 68.31           O  
-ATOM   3640  CB  MET F   1      69.952  44.975  44.260  1.00 86.44           C  
-ATOM   3641  CG  MET F   1      70.037  45.025  42.742  1.00 82.49           C  
-ATOM   3642  SD  MET F   1      71.028  43.679  42.048  1.00 81.36           S  
-ATOM   3643  CE  MET F   1      72.508  43.806  43.039  1.00 68.73           C  
-ATOM   3644  N   LYS F   2      68.665  47.515  45.648  1.00 48.39           N  
-ATOM   3645  CA  LYS F   2      67.851  48.134  46.708  1.00 42.72           C  
-ATOM   3646  C   LYS F   2      66.338  48.203  46.420  1.00 41.44           C  
-ATOM   3647  O   LYS F   2      65.906  48.884  45.481  1.00 29.48           O  
-ATOM   3648  CB  LYS F   2      68.396  49.544  46.959  1.00 36.01           C  
-ATOM   3649  CG  LYS F   2      69.863  49.588  47.304  1.00 44.34           C  
-ATOM   3650  CD  LYS F   2      70.022  49.471  48.794  1.00 39.88           C  
-ATOM   3651  CE  LYS F   2      71.459  49.710  49.234  1.00 37.55           C  
-ATOM   3652  NZ  LYS F   2      71.651  51.091  49.742  1.00 57.52           N  
-ATOM   3653  N   GLN F   3      65.538  47.514  47.207  1.00 33.48           N  
-ATOM   3654  CA  GLN F   3      64.115  47.555  47.008  1.00 30.58           C  
-ATOM   3655  C   GLN F   3      63.620  48.898  47.536  1.00 31.61           C  
-ATOM   3656  O   GLN F   3      63.926  49.278  48.672  1.00 33.64           O  
-ATOM   3657  CB  GLN F   3      63.389  46.423  47.743  1.00 28.61           C  
-ATOM   3658  CG  GLN F   3      61.876  46.526  47.667  1.00 32.82           C  
-ATOM   3659  CD  GLN F   3      61.183  45.181  47.827  1.00 50.84           C  
-ATOM   3660  OE1 GLN F   3      60.802  44.803  48.945  1.00 40.74           O  
-ATOM   3661  NE2 GLN F   3      60.903  44.308  46.870  1.00 49.00           N  
-ATOM   3662  N   VAL F   4      62.870  49.624  46.728  1.00 25.77           N  
-ATOM   3663  CA  VAL F   4      62.315  50.907  47.110  1.00 26.36           C  
-ATOM   3664  C   VAL F   4      60.814  50.732  47.170  1.00 31.33           C  
-ATOM   3665  O   VAL F   4      60.203  50.327  46.185  1.00 32.81           O  
-ATOM   3666  CB  VAL F   4      62.711  52.024  46.151  1.00 38.65           C  
-ATOM   3667  CG1 VAL F   4      62.007  53.312  46.529  1.00 31.22           C  
-ATOM   3668  CG2 VAL F   4      64.231  52.202  46.150  1.00 35.00           C  
-ATOM   3669  N   THR F   5      60.242  51.032  48.316  1.00 26.75           N  
-ATOM   3670  CA  THR F   5      58.798  50.795  48.484  1.00 26.54           C  
-ATOM   3671  C   THR F   5      58.175  52.114  48.802  1.00 29.19           C  
-ATOM   3672  O   THR F   5      58.698  52.807  49.712  1.00 27.94           O  
-ATOM   3673  CB  THR F   5      58.489  49.837  49.673  1.00 36.81           C  
-ATOM   3674  OG1 THR F   5      59.058  48.581  49.304  1.00 32.48           O  
-ATOM   3675  CG2 THR F   5      57.009  49.588  49.828  1.00 25.92           C  
-ATOM   3676  N   ALA F   6      57.062  52.413  48.141  1.00 26.96           N  
-ATOM   3677  CA  ALA F   6      56.410  53.655  48.525  1.00 29.61           C  
-ATOM   3678  C   ALA F   6      54.951  53.324  48.769  1.00 29.56           C  
-ATOM   3679  O   ALA F   6      54.369  52.511  48.061  1.00 34.70           O  
-ATOM   3680  CB  ALA F   6      56.570  54.734  47.438  1.00 26.45           C  
-ATOM   3681  N   ILE F   7      54.326  53.944  49.748  1.00 29.36           N  
-ATOM   3682  CA  ILE F   7      52.916  53.796  50.010  1.00 28.04           C  
-ATOM   3683  C   ILE F   7      52.294  55.155  49.804  1.00 31.52           C  
-ATOM   3684  O   ILE F   7      52.682  56.143  50.424  1.00 33.96           O  
-ATOM   3685  CB  ILE F   7      52.578  53.354  51.461  1.00 43.35           C  
-ATOM   3686  CG1 ILE F   7      53.338  52.091  51.885  1.00 36.16           C  
-ATOM   3687  CG2 ILE F   7      51.081  53.145  51.509  1.00 32.87           C  
-ATOM   3688  CD1 ILE F   7      52.993  50.808  51.184  1.00 43.37           C  
-ATOM   3689  N   ILE F   8      51.412  55.261  48.843  1.00 28.62           N  
-ATOM   3690  CA  ILE F   8      50.919  56.538  48.397  1.00 30.24           C  
-ATOM   3691  C   ILE F   8      49.410  56.535  48.180  1.00 27.70           C  
-ATOM   3692  O   ILE F   8      48.776  55.495  48.200  1.00 27.95           O  
-ATOM   3693  CB  ILE F   8      51.590  56.864  47.031  1.00 33.47           C  
-ATOM   3694  CG1 ILE F   8      51.286  55.737  46.002  1.00 34.13           C  
-ATOM   3695  CG2 ILE F   8      53.079  57.066  47.192  1.00 31.63           C  
-ATOM   3696  CD1 ILE F   8      51.391  56.166  44.545  1.00 33.60           C  
-ATOM   3697  N   LYS F   9      48.873  57.709  47.913  1.00 26.31           N  
-ATOM   3698  CA  LYS F   9      47.476  57.883  47.649  1.00 32.99           C  
-ATOM   3699  C   LYS F   9      47.289  57.426  46.229  1.00 31.84           C  
-ATOM   3700  O   LYS F   9      48.087  57.700  45.314  1.00 27.84           O  
-ATOM   3701  CB  LYS F   9      47.055  59.358  47.748  1.00 37.24           C  
-ATOM   3702  CG  LYS F   9      47.239  59.974  49.130  1.00 45.40           C  
-ATOM   3703  CD  LYS F   9      47.203  61.505  49.113  1.00 42.64           C  
-ATOM   3704  CE  LYS F   9      46.863  62.075  50.501  1.00 58.84           C  
-ATOM   3705  NZ  LYS F   9      47.475  63.418  50.727  1.00 50.03           N  
-ATOM   3706  N   PRO F  10      46.139  56.742  46.069  1.00 31.73           N  
-ATOM   3707  CA  PRO F  10      45.688  56.145  44.785  1.00 35.11           C  
-ATOM   3708  C   PRO F  10      45.714  56.995  43.513  1.00 38.32           C  
-ATOM   3709  O   PRO F  10      46.172  56.529  42.461  1.00 32.88           O  
-ATOM   3710  CB  PRO F  10      44.357  55.526  45.174  1.00 28.08           C  
-ATOM   3711  CG  PRO F  10      44.651  55.020  46.566  1.00 31.85           C  
-ATOM   3712  CD  PRO F  10      45.736  55.854  47.172  1.00 32.06           C  
-ATOM   3713  N   PHE F  11      45.213  58.225  43.632  1.00 36.57           N  
-ATOM   3714  CA  PHE F  11      45.233  59.103  42.460  1.00 37.65           C  
-ATOM   3715  C   PHE F  11      46.684  59.474  42.103  1.00 36.61           C  
-ATOM   3716  O   PHE F  11      46.897  59.862  40.944  1.00 37.46           O  
-ATOM   3717  CB  PHE F  11      44.317  60.338  42.636  1.00 35.93           C  
-ATOM   3718  CG  PHE F  11      44.957  61.403  43.436  1.00 50.40           C  
-ATOM   3719  CD1 PHE F  11      45.676  62.439  42.845  1.00 50.93           C  
-ATOM   3720  CD2 PHE F  11      44.852  61.358  44.814  1.00 54.71           C  
-ATOM   3721  CE1 PHE F  11      46.280  63.412  43.642  1.00 51.91           C  
-ATOM   3722  CE2 PHE F  11      45.446  62.337  45.609  1.00 48.14           C  
-ATOM   3723  CZ  PHE F  11      46.159  63.365  45.021  1.00 46.63           C  
-ATOM   3724  N   LYS F  12      47.679  59.344  42.954  1.00 31.30           N  
-ATOM   3725  CA  LYS F  12      49.028  59.731  42.455  1.00 29.82           C  
-ATOM   3726  C   LYS F  12      49.740  58.611  41.677  1.00 29.41           C  
-ATOM   3727  O   LYS F  12      50.846  58.836  41.175  1.00 28.77           O  
-ATOM   3728  CB  LYS F  12      49.935  60.174  43.586  1.00 33.24           C  
-ATOM   3729  CG  LYS F  12      49.593  61.550  44.157  1.00 35.09           C  
-ATOM   3730  CD  LYS F  12      50.088  62.672  43.252  1.00 33.52           C  
-ATOM   3731  CE  LYS F  12      49.994  64.028  43.920  1.00 32.17           C  
-ATOM   3732  NZ  LYS F  12      50.668  65.081  43.121  1.00 32.37           N  
-ATOM   3733  N   LEU F  13      49.173  57.422  41.562  1.00 27.52           N  
-ATOM   3734  CA  LEU F  13      49.819  56.374  40.827  1.00 27.05           C  
-ATOM   3735  C   LEU F  13      50.410  56.757  39.461  1.00 29.52           C  
-ATOM   3736  O   LEU F  13      51.578  56.514  39.194  1.00 23.21           O  
-ATOM   3737  CB  LEU F  13      48.832  55.217  40.661  1.00 24.69           C  
-ATOM   3738  CG  LEU F  13      49.360  53.802  40.427  1.00 43.48           C  
-ATOM   3739  CD1 LEU F  13      48.800  53.243  39.132  1.00 37.50           C  
-ATOM   3740  CD2 LEU F  13      50.892  53.786  40.404  1.00 26.98           C  
-ATOM   3741  N   ASP F  14      49.554  57.287  38.570  1.00 24.64           N  
-ATOM   3742  CA  ASP F  14      50.075  57.590  37.243  1.00 29.18           C  
-ATOM   3743  C   ASP F  14      51.200  58.614  37.264  1.00 21.37           C  
-ATOM   3744  O   ASP F  14      52.170  58.453  36.516  1.00 22.93           O  
-ATOM   3745  CB  ASP F  14      48.983  58.085  36.326  1.00 28.09           C  
-ATOM   3746  CG  ASP F  14      49.393  57.842  34.884  1.00 28.65           C  
-ATOM   3747  OD1 ASP F  14      49.871  58.792  34.230  1.00 30.16           O  
-ATOM   3748  OD2 ASP F  14      49.224  56.713  34.412  1.00 32.31           O  
-ATOM   3749  N   GLU F  15      51.140  59.627  38.121  1.00 27.42           N  
-ATOM   3750  CA  GLU F  15      52.222  60.646  38.134  1.00 26.99           C  
-ATOM   3751  C   GLU F  15      53.525  60.010  38.604  1.00 29.66           C  
-ATOM   3752  O   GLU F  15      54.586  60.344  38.086  1.00 24.57           O  
-ATOM   3753  CB  GLU F  15      51.820  61.833  39.043  1.00 29.62           C  
-ATOM   3754  CG  GLU F  15      52.641  63.114  38.841  1.00 35.03           C  
-ATOM   3755  CD  GLU F  15      52.174  64.291  39.677  1.00 29.86           C  
-ATOM   3756  OE1 GLU F  15      52.973  65.234  39.868  1.00 38.52           O  
-ATOM   3757  OE2 GLU F  15      51.026  64.279  40.144  1.00 36.64           O  
-ATOM   3758  N   VAL F  16      53.421  59.113  39.571  1.00 25.22           N  
-ATOM   3759  CA  VAL F  16      54.597  58.458  40.081  1.00 26.05           C  
-ATOM   3760  C   VAL F  16      55.170  57.591  38.986  1.00 25.00           C  
-ATOM   3761  O   VAL F  16      56.394  57.514  38.833  1.00 23.05           O  
-ATOM   3762  CB  VAL F  16      54.353  57.586  41.349  1.00 33.46           C  
-ATOM   3763  CG1 VAL F  16      55.591  56.793  41.723  1.00 27.19           C  
-ATOM   3764  CG2 VAL F  16      53.909  58.462  42.504  1.00 24.68           C  
-ATOM   3765  N   ARG F  17      54.349  56.922  38.232  1.00 26.77           N  
-ATOM   3766  CA  ARG F  17      54.814  56.039  37.173  1.00 25.08           C  
-ATOM   3767  C   ARG F  17      55.659  56.784  36.114  1.00 19.69           C  
-ATOM   3768  O   ARG F  17      56.745  56.332  35.732  1.00 25.02           O  
-ATOM   3769  CB  ARG F  17      53.573  55.246  36.698  1.00 26.58           C  
-ATOM   3770  CG  ARG F  17      53.538  54.772  35.267  1.00 26.73           C  
-ATOM   3771  CD  ARG F  17      52.551  55.588  34.493  1.00 31.19           C  
-ATOM   3772  NE  ARG F  17      53.212  55.999  33.287  1.00 34.24           N  
-ATOM   3773  CZ  ARG F  17      53.286  57.222  32.790  1.00 27.44           C  
-ATOM   3774  NH1 ARG F  17      52.710  58.227  33.409  1.00 27.21           N  
-ATOM   3775  NH2 ARG F  17      53.961  57.428  31.668  1.00 31.62           N  
-ATOM   3776  N   GLU F  18      55.143  57.943  35.695  1.00 27.16           N  
-ATOM   3777  CA  GLU F  18      55.787  58.794  34.730  1.00 25.72           C  
-ATOM   3778  C   GLU F  18      57.101  59.436  35.276  1.00 31.46           C  
-ATOM   3779  O   GLU F  18      58.101  59.514  34.565  1.00 27.50           O  
-ATOM   3780  CB  GLU F  18      54.816  59.884  34.237  1.00 24.89           C  
-ATOM   3781  CG  GLU F  18      55.401  60.895  33.269  1.00 26.56           C  
-ATOM   3782  CD  GLU F  18      55.845  60.281  31.965  1.00 24.33           C  
-ATOM   3783  OE1 GLU F  18      55.632  59.060  31.783  1.00 22.92           O  
-ATOM   3784  OE2 GLU F  18      56.402  61.009  31.107  1.00 27.04           O  
-ATOM   3785  N   SER F  19      57.118  59.891  36.527  1.00 23.42           N  
-ATOM   3786  CA  SER F  19      58.313  60.481  37.153  1.00 24.98           C  
-ATOM   3787  C   SER F  19      59.415  59.430  37.268  1.00 22.97           C  
-ATOM   3788  O   SER F  19      60.600  59.768  37.178  1.00 28.13           O  
-ATOM   3789  CB  SER F  19      57.951  61.036  38.538  1.00 30.26           C  
-ATOM   3790  OG  SER F  19      59.042  61.745  39.091  1.00 33.86           O  
-ATOM   3791  N   LEU F  20      59.065  58.185  37.475  1.00 25.64           N  
-ATOM   3792  CA  LEU F  20      60.086  57.142  37.508  1.00 29.10           C  
-ATOM   3793  C   LEU F  20      60.459  56.763  36.087  1.00 29.11           C  
-ATOM   3794  O   LEU F  20      61.616  56.486  35.812  1.00 27.13           O  
-ATOM   3795  CB  LEU F  20      59.573  55.889  38.257  1.00 33.08           C  
-ATOM   3796  CG  LEU F  20      59.470  55.936  39.813  1.00 35.53           C  
-ATOM   3797  CD1 LEU F  20      58.668  54.756  40.342  1.00 26.72           C  
-ATOM   3798  CD2 LEU F  20      60.848  55.957  40.446  1.00 26.16           C  
-ATOM   3799  N   ALA F  21      59.486  56.739  35.171  1.00 24.05           N  
-ATOM   3800  CA  ALA F  21      59.836  56.387  33.774  1.00 28.57           C  
-ATOM   3801  C   ALA F  21      60.859  57.374  33.253  1.00 25.79           C  
-ATOM   3802  O   ALA F  21      61.834  57.078  32.520  1.00 31.84           O  
-ATOM   3803  CB  ALA F  21      58.542  56.424  32.892  1.00 27.99           C  
-ATOM   3804  N   GLU F  22      60.711  58.632  33.699  1.00 25.73           N  
-ATOM   3805  CA  GLU F  22      61.660  59.698  33.314  1.00 32.90           C  
-ATOM   3806  C   GLU F  22      63.117  59.424  33.604  1.00 35.57           C  
-ATOM   3807  O   GLU F  22      64.003  59.812  32.852  1.00 33.11           O  
-ATOM   3808  CB  GLU F  22      61.242  61.014  33.963  1.00 27.22           C  
-ATOM   3809  CG  GLU F  22      60.067  61.714  33.306  1.00 46.42           C  
-ATOM   3810  CD  GLU F  22      59.743  63.035  33.988  1.00 51.66           C  
-ATOM   3811  OE1 GLU F  22      60.470  63.404  34.936  1.00 61.50           O  
-ATOM   3812  OE2 GLU F  22      58.777  63.689  33.575  1.00 52.57           O  
-ATOM   3813  N   VAL F  23      63.276  58.750  34.710  1.00 31.70           N  
-ATOM   3814  CA  VAL F  23      64.562  58.414  35.208  1.00 32.19           C  
-ATOM   3815  C   VAL F  23      64.912  56.997  34.784  1.00 35.55           C  
-ATOM   3816  O   VAL F  23      65.919  56.442  35.238  1.00 35.61           O  
-ATOM   3817  CB  VAL F  23      64.558  58.738  36.742  1.00 43.59           C  
-ATOM   3818  CG1 VAL F  23      65.315  57.667  37.533  1.00 49.26           C  
-ATOM   3819  CG2 VAL F  23      65.174  60.101  36.988  1.00 43.21           C  
-ATOM   3820  N   GLY F  24      64.086  56.379  33.960  1.00 34.26           N  
-ATOM   3821  CA  GLY F  24      64.429  55.098  33.451  1.00 38.49           C  
-ATOM   3822  C   GLY F  24      64.058  53.923  34.348  1.00 41.55           C  
-ATOM   3823  O   GLY F  24      64.534  52.800  34.122  1.00 37.59           O  
-ATOM   3824  N   VAL F  25      63.210  54.125  35.380  1.00 41.67           N  
-ATOM   3825  CA  VAL F  25      62.788  52.983  36.225  1.00 39.12           C  
-ATOM   3826  C   VAL F  25      61.386  52.569  35.797  1.00 33.01           C  
-ATOM   3827  O   VAL F  25      60.451  53.333  35.968  1.00 30.73           O  
-ATOM   3828  CB  VAL F  25      62.783  53.356  37.722  1.00 37.28           C  
-ATOM   3829  CG1 VAL F  25      62.162  52.252  38.556  1.00 29.21           C  
-ATOM   3830  CG2 VAL F  25      64.209  53.634  38.186  1.00 36.31           C  
-ATOM   3831  N   THR F  26      61.239  51.370  35.248  1.00 32.26           N  
-ATOM   3832  CA  THR F  26      59.907  51.002  34.749  1.00 31.58           C  
-ATOM   3833  C   THR F  26      59.340  49.693  35.305  1.00 35.69           C  
-ATOM   3834  O   THR F  26      58.136  49.452  35.167  1.00 41.57           O  
-ATOM   3835  CB  THR F  26      59.893  50.879  33.233  1.00 44.26           C  
-ATOM   3836  OG1 THR F  26      60.940  49.998  32.824  1.00 42.98           O  
-ATOM   3837  CG2 THR F  26      60.091  52.254  32.602  1.00 34.63           C  
-ATOM   3838  N   GLY F  27      60.124  48.833  35.914  1.00 32.13           N  
-ATOM   3839  CA  GLY F  27      59.519  47.592  36.382  1.00 36.94           C  
-ATOM   3840  C   GLY F  27      58.793  47.715  37.715  1.00 34.55           C  
-ATOM   3841  O   GLY F  27      59.261  47.172  38.711  1.00 38.81           O  
-ATOM   3842  N   LEU F  28      57.636  48.421  37.746  1.00 31.34           N  
-ATOM   3843  CA  LEU F  28      56.856  48.641  38.994  1.00 32.09           C  
-ATOM   3844  C   LEU F  28      55.929  47.475  39.355  1.00 34.18           C  
-ATOM   3845  O   LEU F  28      55.305  46.883  38.475  1.00 31.82           O  
-ATOM   3846  CB  LEU F  28      55.872  49.802  38.877  1.00 34.01           C  
-ATOM   3847  CG  LEU F  28      56.368  51.147  38.398  1.00 51.99           C  
-ATOM   3848  CD1 LEU F  28      55.442  52.257  38.860  1.00 44.03           C  
-ATOM   3849  CD2 LEU F  28      57.786  51.393  38.875  1.00 45.61           C  
-ATOM   3850  N   THR F  29      55.839  47.148  40.628  1.00 29.12           N  
-ATOM   3851  CA  THR F  29      54.894  46.129  41.122  1.00 24.64           C  
-ATOM   3852  C   THR F  29      53.927  46.939  42.000  1.00 28.20           C  
-ATOM   3853  O   THR F  29      54.356  47.603  42.939  1.00 29.37           O  
-ATOM   3854  CB  THR F  29      55.601  45.044  41.957  1.00 36.38           C  
-ATOM   3855  OG1 THR F  29      56.417  44.241  41.097  1.00 38.23           O  
-ATOM   3856  CG2 THR F  29      54.581  44.154  42.668  1.00 31.95           C  
-ATOM   3857  N   VAL F  30      52.626  46.872  41.720  1.00 24.17           N  
-ATOM   3858  CA  VAL F  30      51.623  47.648  42.387  1.00 30.09           C  
-ATOM   3859  C   VAL F  30      50.671  46.689  43.176  1.00 31.24           C  
-ATOM   3860  O   VAL F  30      50.171  45.692  42.609  1.00 26.34           O  
-ATOM   3861  CB  VAL F  30      50.767  48.390  41.360  1.00 38.52           C  
-ATOM   3862  CG1 VAL F  30      49.610  49.162  42.007  1.00 31.82           C  
-ATOM   3863  CG2 VAL F  30      51.607  49.270  40.440  1.00 30.92           C  
-ATOM   3864  N   THR F  31      50.488  46.980  44.438  1.00 25.67           N  
-ATOM   3865  CA  THR F  31      49.508  46.243  45.278  1.00 23.90           C  
-ATOM   3866  C   THR F  31      48.527  47.184  45.906  1.00 25.31           C  
-ATOM   3867  O   THR F  31      48.926  48.245  46.381  1.00 26.58           O  
-ATOM   3868  CB  THR F  31      50.312  45.599  46.473  1.00 29.38           C  
-ATOM   3869  OG1 THR F  31      51.404  44.893  45.887  1.00 28.88           O  
-ATOM   3870  CG2 THR F  31      49.433  44.659  47.278  1.00 29.73           C  
-ATOM   3871  N   GLU F  32      47.246  46.895  46.034  1.00 26.31           N  
-ATOM   3872  CA  GLU F  32      46.267  47.714  46.686  1.00 28.34           C  
-ATOM   3873  C   GLU F  32      46.352  47.360  48.188  1.00 30.92           C  
-ATOM   3874  O   GLU F  32      46.402  46.148  48.451  1.00 27.86           O  
-ATOM   3875  CB  GLU F  32      44.823  47.352  46.265  1.00 31.15           C  
-ATOM   3876  CG  GLU F  32      44.473  47.673  44.815  1.00 62.00           C  
-ATOM   3877  CD  GLU F  32      43.479  46.639  44.272  1.00 74.84           C  
-ATOM   3878  OE1 GLU F  32      42.629  46.164  45.076  1.00 81.65           O  
-ATOM   3879  OE2 GLU F  32      43.523  46.266  43.071  1.00 80.71           O  
-ATOM   3880  N   VAL F  33      46.457  48.295  49.087  1.00 32.70           N  
-ATOM   3881  CA  VAL F  33      46.686  47.959  50.496  1.00 31.44           C  
-ATOM   3882  C   VAL F  33      45.794  48.951  51.259  1.00 34.58           C  
-ATOM   3883  O   VAL F  33      45.164  49.793  50.605  1.00 30.19           O  
-ATOM   3884  CB  VAL F  33      48.099  48.150  51.045  1.00 28.61           C  
-ATOM   3885  CG1 VAL F  33      49.180  47.251  50.398  1.00 20.88           C  
-ATOM   3886  CG2 VAL F  33      48.485  49.631  50.929  1.00 25.39           C  
-ATOM   3887  N   LYS F  34      45.585  48.619  52.540  1.00 32.03           N  
-ATOM   3888  CA  LYS F  34      44.786  49.592  53.353  1.00 31.09           C  
-ATOM   3889  C   LYS F  34      45.612  50.138  54.485  1.00 32.10           C  
-ATOM   3890  O   LYS F  34      46.387  49.404  55.129  1.00 27.97           O  
-ATOM   3891  CB  LYS F  34      43.564  48.889  53.916  1.00 39.49           C  
-ATOM   3892  CG  LYS F  34      42.755  48.058  52.931  1.00 44.59           C  
-ATOM   3893  CD  LYS F  34      41.614  47.422  53.744  1.00 51.33           C  
-ATOM   3894  CE  LYS F  34      41.457  45.962  53.359  1.00 68.29           C  
-ATOM   3895  NZ  LYS F  34      40.731  45.789  52.065  1.00 73.31           N  
-ATOM   3896  N   GLY F  35      45.520  51.433  54.740  1.00 32.10           N  
-ATOM   3897  CA  GLY F  35      46.267  52.102  55.785  1.00 42.50           C  
-ATOM   3898  C   GLY F  35      45.401  52.427  57.013  1.00 52.69           C  
-ATOM   3899  O   GLY F  35      44.272  52.931  56.876  1.00 45.23           O  
-ATOM   3900  N   PRO F  57      42.223  53.427  51.589  1.00 48.87           N  
-ATOM   3901  CA  PRO F  57      42.827  52.656  50.494  1.00 41.57           C  
-ATOM   3902  C   PRO F  57      44.091  53.407  50.095  1.00 33.84           C  
-ATOM   3903  O   PRO F  57      44.225  54.617  50.230  1.00 30.73           O  
-ATOM   3904  CB  PRO F  57      41.802  52.629  49.366  1.00 43.72           C  
-ATOM   3905  CG  PRO F  57      40.670  53.505  49.800  1.00 46.60           C  
-ATOM   3906  CD  PRO F  57      41.016  54.160  51.114  1.00 46.58           C  
-ATOM   3907  N   LYS F  58      45.165  52.660  49.889  1.00 31.67           N  
-ATOM   3908  CA  LYS F  58      46.408  53.184  49.438  1.00 29.80           C  
-ATOM   3909  C   LYS F  58      46.866  52.283  48.300  1.00 27.87           C  
-ATOM   3910  O   LYS F  58      46.452  51.171  48.235  1.00 29.76           O  
-ATOM   3911  CB  LYS F  58      47.521  53.156  50.515  1.00 34.67           C  
-ATOM   3912  CG  LYS F  58      47.057  53.865  51.800  1.00 36.54           C  
-ATOM   3913  CD  LYS F  58      47.530  55.285  51.777  1.00 41.51           C  
-ATOM   3914  CE  LYS F  58      46.804  56.151  52.787  1.00 51.09           C  
-ATOM   3915  NZ  LYS F  58      46.944  57.588  52.399  1.00 42.49           N  
-ATOM   3916  N   VAL F  59      47.943  52.790  47.682  1.00 27.41           N  
-ATOM   3917  CA  VAL F  59      48.633  51.918  46.735  1.00 32.82           C  
-ATOM   3918  C   VAL F  59      50.061  51.728  47.176  1.00 29.67           C  
-ATOM   3919  O   VAL F  59      50.742  52.686  47.561  1.00 32.34           O  
-ATOM   3920  CB  VAL F  59      48.594  52.630  45.331  1.00 38.39           C  
-ATOM   3921  CG1 VAL F  59      49.541  51.943  44.391  1.00 40.52           C  
-ATOM   3922  CG2 VAL F  59      47.154  52.512  44.809  1.00 38.05           C  
-ATOM   3923  N   LYS F  60      50.517  50.480  47.180  1.00 27.14           N  
-ATOM   3924  CA  LYS F  60      51.907  50.205  47.423  1.00 28.08           C  
-ATOM   3925  C   LYS F  60      52.590  49.978  46.069  1.00 29.08           C  
-ATOM   3926  O   LYS F  60      52.199  49.090  45.293  1.00 25.14           O  
-ATOM   3927  CB  LYS F  60      52.106  48.979  48.323  1.00 29.09           C  
-ATOM   3928  CG  LYS F  60      53.555  48.616  48.517  1.00 28.92           C  
-ATOM   3929  CD  LYS F  60      53.755  47.191  49.055  1.00 35.53           C  
-ATOM   3930  CE  LYS F  60      53.541  47.124  50.538  1.00 41.70           C  
-ATOM   3931  NZ  LYS F  60      54.026  45.834  51.108  1.00 41.45           N  
-ATOM   3932  N   ILE F  61      53.712  50.706  45.887  1.00 25.68           N  
-ATOM   3933  CA  ILE F  61      54.538  50.410  44.709  1.00 31.67           C  
-ATOM   3934  C   ILE F  61      55.898  49.900  45.126  1.00 31.40           C  
-ATOM   3935  O   ILE F  61      56.417  50.416  46.133  1.00 31.78           O  
-ATOM   3936  CB  ILE F  61      54.743  51.756  43.916  1.00 35.15           C  
-ATOM   3937  CG1 ILE F  61      53.414  52.173  43.239  1.00 26.19           C  
-ATOM   3938  CG2 ILE F  61      55.921  51.636  42.986  1.00 38.58           C  
-ATOM   3939  CD1 ILE F  61      53.611  53.619  42.718  1.00 42.34           C  
-ATOM   3940  N   GLU F  62      56.407  48.814  44.519  1.00 26.28           N  
-ATOM   3941  CA  GLU F  62      57.751  48.396  44.857  1.00 28.81           C  
-ATOM   3942  C   GLU F  62      58.635  48.348  43.614  1.00 30.65           C  
-ATOM   3943  O   GLU F  62      58.098  47.962  42.563  1.00 26.87           O  
-ATOM   3944  CB  GLU F  62      57.658  46.904  45.362  1.00 28.01           C  
-ATOM   3945  CG  GLU F  62      57.027  46.919  46.789  1.00 32.61           C  
-ATOM   3946  CD  GLU F  62      56.525  45.509  47.083  1.00 39.97           C  
-ATOM   3947  OE1 GLU F  62      55.717  44.906  46.343  1.00 39.72           O  
-ATOM   3948  OE2 GLU F  62      57.019  45.020  48.111  1.00 41.02           O  
-ATOM   3949  N   VAL F  63      59.906  48.632  43.626  1.00 27.39           N  
-ATOM   3950  CA  VAL F  63      60.759  48.404  42.470  1.00 32.59           C  
-ATOM   3951  C   VAL F  63      62.132  48.100  43.112  1.00 34.83           C  
-ATOM   3952  O   VAL F  63      62.502  48.576  44.203  1.00 30.54           O  
-ATOM   3953  CB  VAL F  63      60.940  49.634  41.562  1.00 35.44           C  
-ATOM   3954  CG1 VAL F  63      59.714  50.358  41.023  1.00 36.36           C  
-ATOM   3955  CG2 VAL F  63      61.631  50.765  42.324  1.00 26.45           C  
-ATOM   3956  N   VAL F  64      62.826  47.243  42.454  1.00 30.78           N  
-ATOM   3957  CA  VAL F  64      64.167  46.791  42.848  1.00 35.45           C  
-ATOM   3958  C   VAL F  64      65.142  47.410  41.865  1.00 39.72           C  
-ATOM   3959  O   VAL F  64      65.061  47.123  40.655  1.00 42.65           O  
-ATOM   3960  CB  VAL F  64      64.027  45.270  42.836  1.00 38.73           C  
-ATOM   3961  CG1 VAL F  64      65.329  44.579  42.641  1.00 36.47           C  
-ATOM   3962  CG2 VAL F  64      63.236  44.738  44.062  1.00 31.59           C  
-ATOM   3963  N   VAL F  65      65.991  48.354  42.254  1.00 34.84           N  
-ATOM   3964  CA  VAL F  65      66.932  49.017  41.385  1.00 36.41           C  
-ATOM   3965  C   VAL F  65      68.377  48.811  41.822  1.00 42.93           C  
-ATOM   3966  O   VAL F  65      68.752  48.395  42.933  1.00 35.24           O  
-ATOM   3967  CB  VAL F  65      66.664  50.511  41.272  1.00 34.35           C  
-ATOM   3968  CG1 VAL F  65      65.276  50.732  40.685  1.00 36.49           C  
-ATOM   3969  CG2 VAL F  65      66.688  51.303  42.567  1.00 41.21           C  
-ATOM   3970  N   ASP F  66      69.261  49.375  40.966  1.00 41.94           N  
-ATOM   3971  CA  ASP F  66      70.700  49.265  41.224  1.00 37.01           C  
-ATOM   3972  C   ASP F  66      71.048  50.307  42.230  1.00 35.75           C  
-ATOM   3973  O   ASP F  66      70.412  51.375  42.226  1.00 38.19           O  
-ATOM   3974  CB  ASP F  66      71.485  49.373  39.903  1.00 52.77           C  
-ATOM   3975  CG  ASP F  66      72.971  49.492  40.128  1.00 49.22           C  
-ATOM   3976  OD1 ASP F  66      73.466  50.622  40.393  1.00 62.56           O  
-ATOM   3977  OD2 ASP F  66      73.659  48.462  40.085  1.00 55.38           O  
-ATOM   3978  N   ASP F  67      72.067  50.137  43.075  1.00 37.25           N  
-ATOM   3979  CA  ASP F  67      72.371  51.126  44.097  1.00 42.68           C  
-ATOM   3980  C   ASP F  67      72.603  52.541  43.573  1.00 45.18           C  
-ATOM   3981  O   ASP F  67      72.326  53.523  44.291  1.00 44.02           O  
-ATOM   3982  CB  ASP F  67      73.658  50.789  44.880  1.00 43.59           C  
-ATOM   3983  CG  ASP F  67      73.520  49.533  45.713  1.00 49.97           C  
-ATOM   3984  OD1 ASP F  67      72.469  48.856  45.640  1.00 54.03           O  
-ATOM   3985  OD2 ASP F  67      74.475  49.208  46.446  1.00 60.65           O  
-ATOM   3986  N   LYS F  68      73.163  52.661  42.373  1.00 42.37           N  
-ATOM   3987  CA  LYS F  68      73.509  53.958  41.846  1.00 45.47           C  
-ATOM   3988  C   LYS F  68      72.268  54.697  41.363  1.00 44.08           C  
-ATOM   3989  O   LYS F  68      72.345  55.846  40.970  1.00 45.51           O  
-ATOM   3990  CB  LYS F  68      74.519  53.838  40.703  1.00 47.85           C  
-ATOM   3991  N   VAL F  69      71.102  54.036  41.416  1.00 43.62           N  
-ATOM   3992  CA  VAL F  69      69.856  54.656  40.916  1.00 43.13           C  
-ATOM   3993  C   VAL F  69      68.826  54.947  42.004  1.00 37.82           C  
-ATOM   3994  O   VAL F  69      67.792  55.564  41.741  1.00 40.62           O  
-ATOM   3995  CB  VAL F  69      69.220  53.690  39.871  1.00 45.39           C  
-ATOM   3996  CG1 VAL F  69      67.965  54.291  39.254  1.00 47.48           C  
-ATOM   3997  CG2 VAL F  69      70.221  53.351  38.784  1.00 43.53           C  
-ATOM   3998  N   VAL F  70      69.123  54.466  43.245  1.00 38.70           N  
-ATOM   3999  CA  VAL F  70      68.233  54.606  44.400  1.00 35.47           C  
-ATOM   4000  C   VAL F  70      67.865  56.041  44.724  1.00 34.63           C  
-ATOM   4001  O   VAL F  70      66.692  56.348  44.878  1.00 37.51           O  
-ATOM   4002  CB  VAL F  70      68.799  53.930  45.663  1.00 41.38           C  
-ATOM   4003  CG1 VAL F  70      67.985  54.318  46.876  1.00 44.24           C  
-ATOM   4004  CG2 VAL F  70      68.827  52.418  45.508  1.00 38.15           C  
-ATOM   4005  N   GLU F  71      68.839  56.944  44.838  1.00 32.54           N  
-ATOM   4006  CA  GLU F  71      68.494  58.326  45.228  1.00 34.21           C  
-ATOM   4007  C   GLU F  71      67.616  59.054  44.203  1.00 34.74           C  
-ATOM   4008  O   GLU F  71      66.690  59.783  44.567  1.00 35.35           O  
-ATOM   4009  CB  GLU F  71      69.758  59.132  45.502  1.00 46.26           C  
-ATOM   4010  CG  GLU F  71      70.783  58.365  46.313  1.00 70.76           C  
-ATOM   4011  CD  GLU F  71      70.457  58.209  47.808  1.00 78.60           C  
-ATOM   4012  OE1 GLU F  71      70.550  59.215  48.548  1.00 85.72           O  
-ATOM   4013  OE2 GLU F  71      70.123  57.083  48.241  1.00 83.39           O  
-ATOM   4014  N   GLN F  72      67.941  58.845  42.901  1.00 36.81           N  
-ATOM   4015  CA  GLN F  72      67.138  59.413  41.826  1.00 37.60           C  
-ATOM   4016  C   GLN F  72      65.721  58.867  41.933  1.00 29.13           C  
-ATOM   4017  O   GLN F  72      64.743  59.612  41.845  1.00 31.28           O  
-ATOM   4018  CB  GLN F  72      67.651  59.027  40.424  1.00 48.66           C  
-ATOM   4019  CG  GLN F  72      69.114  59.327  40.086  1.00 63.77           C  
-ATOM   4020  CD  GLN F  72      69.543  58.682  38.760  1.00 68.44           C  
-ATOM   4021  OE1 GLN F  72      70.439  57.826  38.760  1.00 64.51           O  
-ATOM   4022  NE2 GLN F  72      69.052  58.932  37.550  1.00 65.50           N  
-ATOM   4023  N   ALA F  73      65.574  57.560  42.116  1.00 32.68           N  
-ATOM   4024  CA  ALA F  73      64.253  57.002  42.212  1.00 30.98           C  
-ATOM   4025  C   ALA F  73      63.463  57.532  43.394  1.00 32.30           C  
-ATOM   4026  O   ALA F  73      62.235  57.713  43.306  1.00 29.15           O  
-ATOM   4027  CB  ALA F  73      64.331  55.473  42.277  1.00 27.66           C  
-ATOM   4028  N   VAL F  74      64.092  57.757  44.547  1.00 35.14           N  
-ATOM   4029  CA  VAL F  74      63.377  58.282  45.715  1.00 34.72           C  
-ATOM   4030  C   VAL F  74      62.908  59.689  45.438  1.00 32.31           C  
-ATOM   4031  O   VAL F  74      61.773  60.079  45.714  1.00 31.70           O  
-ATOM   4032  CB  VAL F  74      64.283  58.220  46.973  1.00 36.04           C  
-ATOM   4033  CG1 VAL F  74      63.621  58.933  48.145  1.00 33.10           C  
-ATOM   4034  CG2 VAL F  74      64.590  56.779  47.345  1.00 34.73           C  
-ATOM   4035  N   ASP F  75      63.793  60.485  44.877  1.00 32.73           N  
-ATOM   4036  CA  ASP F  75      63.516  61.864  44.511  1.00 35.35           C  
-ATOM   4037  C   ASP F  75      62.311  61.952  43.547  1.00 27.76           C  
-ATOM   4038  O   ASP F  75      61.387  62.731  43.754  1.00 29.26           O  
-ATOM   4039  CB  ASP F  75      64.699  62.491  43.773  1.00 36.45           C  
-ATOM   4040  CG  ASP F  75      65.828  62.854  44.707  1.00 65.97           C  
-ATOM   4041  OD1 ASP F  75      65.603  62.874  45.934  1.00 57.04           O  
-ATOM   4042  OD2 ASP F  75      66.928  63.134  44.202  1.00 72.13           O  
-ATOM   4043  N   ALA F  76      62.348  61.138  42.499  1.00 31.38           N  
-ATOM   4044  CA  ALA F  76      61.280  61.125  41.528  1.00 28.46           C  
-ATOM   4045  C   ALA F  76      59.950  60.821  42.195  1.00 26.33           C  
-ATOM   4046  O   ALA F  76      58.943  61.460  41.889  1.00 26.87           O  
-ATOM   4047  CB  ALA F  76      61.560  60.118  40.416  1.00 23.36           C  
-ATOM   4048  N   ILE F  77      59.929  59.854  43.129  1.00 27.63           N  
-ATOM   4049  CA  ILE F  77      58.650  59.498  43.812  1.00 24.46           C  
-ATOM   4050  C   ILE F  77      58.135  60.685  44.636  1.00 23.69           C  
-ATOM   4051  O   ILE F  77      56.964  61.047  44.568  1.00 28.13           O  
-ATOM   4052  CB  ILE F  77      58.805  58.259  44.735  1.00 29.24           C  
-ATOM   4053  CG1 ILE F  77      59.130  57.028  43.884  1.00 28.52           C  
-ATOM   4054  CG2 ILE F  77      57.533  58.036  45.536  1.00 29.19           C  
-ATOM   4055  CD1 ILE F  77      60.012  56.020  44.594  1.00 29.91           C  
-ATOM   4056  N   ILE F  78      59.062  61.282  45.409  1.00 28.14           N  
-ATOM   4057  CA  ILE F  78      58.717  62.431  46.277  1.00 27.28           C  
-ATOM   4058  C   ILE F  78      58.163  63.554  45.466  1.00 33.95           C  
-ATOM   4059  O   ILE F  78      57.129  64.109  45.820  1.00 33.94           O  
-ATOM   4060  CB  ILE F  78      59.925  62.947  47.109  1.00 42.34           C  
-ATOM   4061  CG1 ILE F  78      60.244  61.948  48.223  1.00 40.20           C  
-ATOM   4062  CG2 ILE F  78      59.648  64.326  47.693  1.00 45.80           C  
-ATOM   4063  CD1 ILE F  78      61.513  62.275  48.981  1.00 49.03           C  
-ATOM   4064  N   LYS F  79      58.825  63.944  44.350  1.00 29.09           N  
-ATOM   4065  CA  LYS F  79      58.267  65.040  43.572  1.00 33.88           C  
-ATOM   4066  C   LYS F  79      56.870  64.852  43.005  1.00 34.26           C  
-ATOM   4067  O   LYS F  79      56.027  65.741  42.832  1.00 32.55           O  
-ATOM   4068  CB  LYS F  79      59.277  65.349  42.430  1.00 44.41           C  
-ATOM   4069  CG  LYS F  79      60.581  65.779  43.120  1.00 71.55           C  
-ATOM   4070  CD  LYS F  79      61.241  66.932  42.367  1.00 84.32           C  
-ATOM   4071  CE  LYS F  79      62.760  66.814  42.480  1.00 89.66           C  
-ATOM   4072  NZ  LYS F  79      63.220  65.510  41.908  1.00 92.62           N  
-ATOM   4073  N   ALA F  80      56.549  63.607  42.604  1.00 34.41           N  
-ATOM   4074  CA  ALA F  80      55.276  63.275  42.007  1.00 31.32           C  
-ATOM   4075  C   ALA F  80      54.191  63.026  43.074  1.00 29.76           C  
-ATOM   4076  O   ALA F  80      53.041  63.370  42.823  1.00 32.53           O  
-ATOM   4077  CB  ALA F  80      55.537  61.962  41.237  1.00 31.92           C  
-ATOM   4078  N   ALA F  81      54.525  62.513  44.236  1.00 33.51           N  
-ATOM   4079  CA  ALA F  81      53.512  62.105  45.226  1.00 34.38           C  
-ATOM   4080  C   ALA F  81      53.155  63.134  46.283  1.00 39.53           C  
-ATOM   4081  O   ALA F  81      52.088  63.069  46.921  1.00 47.54           O  
-ATOM   4082  CB  ALA F  81      54.070  60.814  45.867  1.00 35.11           C  
-ATOM   4083  N   ARG F  82      54.030  64.026  46.646  1.00 40.61           N  
-ATOM   4084  CA  ARG F  82      53.845  65.052  47.665  1.00 46.21           C  
-ATOM   4085  C   ARG F  82      52.681  65.966  47.353  1.00 51.51           C  
-ATOM   4086  O   ARG F  82      52.705  66.590  46.258  1.00 55.67           O  
-ATOM   4087  CB  ARG F  82      55.149  65.871  47.742  1.00 53.37           C  
-ATOM   4088  CG  ARG F  82      55.214  66.906  48.857  1.00 54.70           C  
-ATOM   4089  CD  ARG F  82      56.550  67.643  48.841  1.00 54.04           C  
-ATOM   4090  NE  ARG F  82      57.568  67.055  49.639  1.00 44.77           N  
-ATOM   4091  CZ  ARG F  82      58.810  67.214  49.996  1.00 55.98           C  
-ATOM   4092  NH1 ARG F  82      59.482  68.257  49.526  1.00 50.75           N  
-ATOM   4093  NH2 ARG F  82      59.408  66.339  50.842  1.00 50.18           N  
-ATOM   4094  N   THR F  83      51.622  65.984  48.155  1.00 46.04           N  
-ATOM   4095  CA  THR F  83      50.579  66.979  47.919  1.00 48.76           C  
-ATOM   4096  C   THR F  83      50.879  68.076  48.962  1.00 54.64           C  
-ATOM   4097  O   THR F  83      50.516  69.234  48.864  1.00 53.47           O  
-ATOM   4098  CB  THR F  83      49.152  66.491  48.091  1.00 57.88           C  
-ATOM   4099  OG1 THR F  83      48.998  66.161  49.481  1.00 49.19           O  
-ATOM   4100  CG2 THR F  83      48.747  65.302  47.242  1.00 48.40           C  
-ATOM   4101  N   GLY F  84      51.573  67.674  50.042  1.00 55.83           N  
-ATOM   4102  CA  GLY F  84      51.887  68.590  51.117  1.00 55.32           C  
-ATOM   4103  C   GLY F  84      50.746  68.622  52.135  1.00 50.52           C  
-ATOM   4104  O   GLY F  84      50.781  69.380  53.098  1.00 51.09           O  
-ATOM   4105  N   LYS F  85      49.709  67.875  51.882  1.00 48.19           N  
-ATOM   4106  CA  LYS F  85      48.614  67.599  52.768  1.00 51.69           C  
-ATOM   4107  C   LYS F  85      48.992  66.346  53.600  1.00 57.02           C  
-ATOM   4108  O   LYS F  85      49.969  65.592  53.412  1.00 53.04           O  
-ATOM   4109  CB  LYS F  85      47.295  67.293  52.029  1.00 39.89           C  
-ATOM   4110  CG  LYS F  85      46.662  68.489  51.360  1.00 54.65           C  
-ATOM   4111  CD  LYS F  85      45.323  68.108  50.717  1.00 60.45           C  
-ATOM   4112  CE  LYS F  85      44.268  69.182  50.928  1.00 71.53           C  
-ATOM   4113  NZ  LYS F  85      42.925  68.821  50.375  1.00 75.64           N  
-ATOM   4114  N   ILE F  86      48.069  66.071  54.508  1.00 53.79           N  
-ATOM   4115  CA  ILE F  86      48.125  64.948  55.416  1.00 53.56           C  
-ATOM   4116  C   ILE F  86      47.899  63.651  54.655  1.00 52.01           C  
-ATOM   4117  O   ILE F  86      46.981  63.579  53.834  1.00 49.12           O  
-ATOM   4118  CB  ILE F  86      47.054  65.285  56.499  1.00 55.04           C  
-ATOM   4119  CG1 ILE F  86      47.706  65.678  57.822  1.00 56.95           C  
-ATOM   4120  CG2 ILE F  86      45.977  64.230  56.632  1.00 53.37           C  
-ATOM   4121  CD1 ILE F  86      48.839  64.804  58.338  1.00 53.76           C  
-ATOM   4122  N   GLY F  87      48.650  62.594  54.964  1.00 47.27           N  
-ATOM   4123  CA  GLY F  87      48.464  61.300  54.337  1.00 48.80           C  
-ATOM   4124  C   GLY F  87      49.167  61.050  52.996  1.00 43.81           C  
-ATOM   4125  O   GLY F  87      48.838  60.011  52.395  1.00 44.23           O  
-ATOM   4126  N   ASP F  88      50.134  61.860  52.587  1.00 39.99           N  
-ATOM   4127  CA  ASP F  88      50.922  61.633  51.334  1.00 41.20           C  
-ATOM   4128  C   ASP F  88      51.597  60.279  51.305  1.00 43.50           C  
-ATOM   4129  O   ASP F  88      51.679  59.634  50.252  1.00 40.00           O  
-ATOM   4130  CB  ASP F  88      51.954  62.753  51.112  1.00 32.59           C  
-ATOM   4131  CG  ASP F  88      51.332  64.038  50.540  1.00 33.44           C  
-ATOM   4132  OD1 ASP F  88      50.184  63.976  50.070  1.00 34.62           O  
-ATOM   4133  OD2 ASP F  88      51.989  65.095  50.572  1.00 37.24           O  
-ATOM   4134  N   GLY F  89      52.095  59.861  52.470  1.00 45.00           N  
-ATOM   4135  CA  GLY F  89      52.674  58.517  52.552  1.00 39.19           C  
-ATOM   4136  C   GLY F  89      54.164  58.475  52.903  1.00 37.07           C  
-ATOM   4137  O   GLY F  89      54.744  59.488  53.306  1.00 40.93           O  
-ATOM   4138  N   LYS F  90      54.777  57.282  52.754  1.00 35.20           N  
-ATOM   4139  CA  LYS F  90      56.187  57.062  53.037  1.00 33.46           C  
-ATOM   4140  C   LYS F  90      56.859  56.259  51.959  1.00 31.71           C  
-ATOM   4141  O   LYS F  90      56.231  55.650  51.085  1.00 31.86           O  
-ATOM   4142  CB  LYS F  90      56.396  56.270  54.331  1.00 37.26           C  
-ATOM   4143  CG  LYS F  90      56.220  57.088  55.575  1.00 61.08           C  
-ATOM   4144  CD  LYS F  90      54.780  57.102  56.000  1.00 64.32           C  
-ATOM   4145  CE  LYS F  90      54.594  57.796  57.352  1.00 74.44           C  
-ATOM   4146  NZ  LYS F  90      55.403  57.168  58.426  1.00 72.84           N  
-ATOM   4147  N   ILE F  91      58.155  56.262  52.095  1.00 27.81           N  
-ATOM   4148  CA  ILE F  91      59.075  55.540  51.235  1.00 26.66           C  
-ATOM   4149  C   ILE F  91      60.070  54.819  52.145  1.00 32.73           C  
-ATOM   4150  O   ILE F  91      60.655  55.433  53.028  1.00 32.37           O  
-ATOM   4151  CB  ILE F  91      59.838  56.518  50.290  1.00 28.67           C  
-ATOM   4152  CG1 ILE F  91      58.963  57.312  49.325  1.00 37.49           C  
-ATOM   4153  CG2 ILE F  91      60.884  55.751  49.512  1.00 31.54           C  
-ATOM   4154  CD1 ILE F  91      59.727  58.020  48.229  1.00 35.93           C  
-ATOM   4155  N   PHE F  92      60.298  53.546  51.910  1.00 25.42           N  
-ATOM   4156  CA  PHE F  92      61.269  52.727  52.656  1.00 30.87           C  
-ATOM   4157  C   PHE F  92      62.289  52.181  51.685  1.00 32.81           C  
-ATOM   4158  O   PHE F  92      61.965  51.937  50.518  1.00 32.96           O  
-ATOM   4159  CB  PHE F  92      60.595  51.486  53.313  1.00 33.22           C  
-ATOM   4160  CG  PHE F  92      59.314  51.834  54.003  1.00 33.68           C  
-ATOM   4161  CD1 PHE F  92      58.084  51.371  53.587  1.00 45.53           C  
-ATOM   4162  CD2 PHE F  92      59.388  52.646  55.126  1.00 48.69           C  
-ATOM   4163  CE1 PHE F  92      56.947  51.744  54.293  1.00 55.78           C  
-ATOM   4164  CE2 PHE F  92      58.253  53.007  55.817  1.00 39.53           C  
-ATOM   4165  CZ  PHE F  92      57.013  52.557  55.410  1.00 57.19           C  
-ATOM   4166  N   VAL F  93      63.512  51.991  52.142  1.00 30.67           N  
-ATOM   4167  CA  VAL F  93      64.567  51.400  51.308  1.00 28.55           C  
-ATOM   4168  C   VAL F  93      65.171  50.244  52.060  1.00 32.90           C  
-ATOM   4169  O   VAL F  93      65.505  50.340  53.255  1.00 31.23           O  
-ATOM   4170  CB  VAL F  93      65.637  52.437  50.934  1.00 32.64           C  
-ATOM   4171  CG1 VAL F  93      66.811  51.771  50.223  1.00 30.95           C  
-ATOM   4172  CG2 VAL F  93      65.052  53.524  50.051  1.00 31.69           C  
-ATOM   4173  N   GLN F  94      65.321  49.119  51.361  1.00 26.76           N  
-ATOM   4174  CA  GLN F  94      65.873  47.880  51.930  1.00 32.32           C  
-ATOM   4175  C   GLN F  94      66.896  47.246  51.017  1.00 36.14           C  
-ATOM   4176  O   GLN F  94      66.753  47.355  49.791  1.00 31.96           O  
-ATOM   4177  CB  GLN F  94      64.784  46.823  52.141  1.00 33.44           C  
-ATOM   4178  CG  GLN F  94      63.792  47.191  53.235  1.00 35.74           C  
-ATOM   4179  CD  GLN F  94      62.554  46.313  53.268  1.00 47.32           C  
-ATOM   4180  OE1 GLN F  94      61.630  46.477  52.464  1.00 43.29           O  
-ATOM   4181  NE2 GLN F  94      62.316  45.324  54.130  1.00 42.51           N  
-ATOM   4182  N   GLU F  95      67.902  46.596  51.546  1.00 32.98           N  
-ATOM   4183  CA  GLU F  95      68.856  45.829  50.788  1.00 34.64           C  
-ATOM   4184  C   GLU F  95      68.263  44.632  50.105  1.00 35.05           C  
-ATOM   4185  O   GLU F  95      67.437  43.957  50.677  1.00 35.66           O  
-ATOM   4186  CB  GLU F  95      69.936  45.235  51.737  1.00 40.07           C  
-ATOM   4187  CG  GLU F  95      71.353  45.645  51.535  1.00 49.64           C  
-ATOM   4188  CD  GLU F  95      71.767  45.826  50.090  1.00 57.20           C  
-ATOM   4189  OE1 GLU F  95      72.046  46.987  49.707  1.00 67.63           O  
-ATOM   4190  OE2 GLU F  95      71.818  44.842  49.333  1.00 63.10           O  
-ATOM   4191  N   VAL F  96      68.602  44.293  48.870  1.00 34.31           N  
-ATOM   4192  CA  VAL F  96      68.209  43.029  48.277  1.00 37.43           C  
-ATOM   4193  C   VAL F  96      69.531  42.310  48.013  1.00 41.39           C  
-ATOM   4194  O   VAL F  96      70.352  43.006  47.417  1.00 42.54           O  
-ATOM   4195  CB  VAL F  96      67.413  43.090  46.980  1.00 38.15           C  
-ATOM   4196  CG1 VAL F  96      67.305  41.700  46.349  1.00 38.08           C  
-ATOM   4197  CG2 VAL F  96      66.033  43.624  47.308  1.00 37.12           C  
-ATOM   4198  N   GLU F  97      69.698  41.077  48.400  1.00 37.04           N  
-ATOM   4199  CA  GLU F  97      70.985  40.419  48.258  1.00 40.57           C  
-ATOM   4200  C   GLU F  97      71.207  39.801  46.888  1.00 38.23           C  
-ATOM   4201  O   GLU F  97      72.331  39.598  46.427  1.00 38.20           O  
-ATOM   4202  CB  GLU F  97      71.050  39.266  49.319  1.00 44.01           C  
-ATOM   4203  CG  GLU F  97      71.452  39.820  50.692  1.00 58.47           C  
-ATOM   4204  CD  GLU F  97      71.523  38.814  51.827  1.00 56.30           C  
-ATOM   4205  OE1 GLU F  97      71.349  37.594  51.626  1.00 56.00           O  
-ATOM   4206  OE2 GLU F  97      71.759  39.297  52.945  1.00 64.55           O  
-ATOM   4207  N   GLN F  98      70.169  39.148  46.392  1.00 33.07           N  
-ATOM   4208  CA  GLN F  98      70.217  38.562  45.080  1.00 36.02           C  
-ATOM   4209  C   GLN F  98      68.924  38.816  44.282  1.00 42.24           C  
-ATOM   4210  O   GLN F  98      67.809  38.965  44.833  1.00 38.66           O  
-ATOM   4211  CB  GLN F  98      70.438  37.054  45.139  1.00 46.48           C  
-ATOM   4212  CG  GLN F  98      70.700  36.475  43.735  1.00 59.36           C  
-ATOM   4213  CD  GLN F  98      71.904  37.067  42.986  1.00 62.67           C  
-ATOM   4214  OE1 GLN F  98      71.895  38.146  42.352  1.00 49.66           O  
-ATOM   4215  NE2 GLN F  98      72.989  36.288  43.108  1.00 61.82           N  
-ATOM   4216  N   VAL F  99      69.092  38.919  42.952  1.00 31.28           N  
-ATOM   4217  CA  VAL F  99      68.019  39.146  42.013  1.00 38.27           C  
-ATOM   4218  C   VAL F  99      68.238  38.148  40.866  1.00 41.15           C  
-ATOM   4219  O   VAL F  99      69.358  38.016  40.388  1.00 36.03           O  
-ATOM   4220  CB  VAL F  99      67.865  40.560  41.450  1.00 43.92           C  
-ATOM   4221  CG1 VAL F  99      66.700  40.644  40.440  1.00 36.07           C  
-ATOM   4222  CG2 VAL F  99      67.624  41.592  42.549  1.00 40.84           C  
-ATOM   4223  N   ILE F 100      67.230  37.341  40.551  1.00 41.07           N  
-ATOM   4224  CA  ILE F 100      67.291  36.357  39.505  1.00 43.39           C  
-ATOM   4225  C   ILE F 100      66.101  36.532  38.553  1.00 45.74           C  
-ATOM   4226  O   ILE F 100      64.906  36.671  38.878  1.00 39.97           O  
-ATOM   4227  CB  ILE F 100      67.263  34.919  40.007  1.00 41.42           C  
-ATOM   4228  CG1 ILE F 100      68.411  34.690  41.027  1.00 46.43           C  
-ATOM   4229  CG2 ILE F 100      67.452  33.883  38.919  1.00 53.23           C  
-ATOM   4230  CD1 ILE F 100      67.893  33.863  42.174  1.00 54.33           C  
-ATOM   4231  N   ARG F 101      66.555  36.516  37.272  1.00 39.43           N  
-ATOM   4232  CA  ARG F 101      65.525  36.710  36.230  1.00 34.02           C  
-ATOM   4233  C   ARG F 101      65.193  35.297  35.841  1.00 34.51           C  
-ATOM   4234  O   ARG F 101      66.162  34.554  35.569  1.00 41.98           O  
-ATOM   4235  CB  ARG F 101      66.118  37.550  35.093  1.00 50.89           C  
-ATOM   4236  CG  ARG F 101      65.164  38.154  34.125  1.00 39.93           C  
-ATOM   4237  CD  ARG F 101      65.759  38.732  32.802  1.00 49.84           C  
-ATOM   4238  NE  ARG F 101      65.790  40.217  32.960  1.00 44.86           N  
-ATOM   4239  CZ  ARG F 101      66.961  40.831  33.046  1.00 54.31           C  
-ATOM   4240  NH1 ARG F 101      68.052  40.077  32.944  1.00 68.84           N  
-ATOM   4241  NH2 ARG F 101      67.120  42.130  33.207  1.00 59.13           N  
-ATOM   4242  N   ILE F 102      63.966  34.886  35.943  1.00 32.22           N  
-ATOM   4243  CA  ILE F 102      63.535  33.505  35.713  1.00 42.22           C  
-ATOM   4244  C   ILE F 102      63.758  32.959  34.283  1.00 47.36           C  
-ATOM   4245  O   ILE F 102      64.163  31.829  33.991  1.00 44.61           O  
-ATOM   4246  CB  ILE F 102      62.029  33.397  36.072  1.00 38.51           C  
-ATOM   4247  CG1 ILE F 102      61.901  33.500  37.644  1.00 40.61           C  
-ATOM   4248  CG2 ILE F 102      61.400  32.089  35.609  1.00 35.01           C  
-ATOM   4249  CD1 ILE F 102      60.441  33.477  38.113  1.00 35.02           C  
-ATOM   4250  N   ARG F 103      63.251  33.691  33.327  1.00 48.41           N  
-ATOM   4251  CA  ARG F 103      63.333  33.373  31.902  1.00 51.43           C  
-ATOM   4252  C   ARG F 103      64.754  32.998  31.512  1.00 54.34           C  
-ATOM   4253  O   ARG F 103      64.932  31.910  30.934  1.00 56.53           O  
-ATOM   4254  CB  ARG F 103      62.840  34.604  31.167  1.00 53.85           C  
-ATOM   4255  CG  ARG F 103      61.798  34.368  30.087  1.00 70.64           C  
-ATOM   4256  CD  ARG F 103      62.332  34.758  28.726  1.00 60.21           C  
-ATOM   4257  NE  ARG F 103      62.321  36.218  28.558  1.00 64.00           N  
-ATOM   4258  CZ  ARG F 103      63.410  36.833  28.091  1.00 83.18           C  
-ATOM   4259  NH1 ARG F 103      64.535  36.193  27.768  1.00 80.32           N  
-ATOM   4260  NH2 ARG F 103      63.400  38.156  27.946  1.00 89.86           N  
-ATOM   4261  N   THR F 104      65.790  33.730  31.873  1.00 53.65           N  
-ATOM   4262  CA  THR F 104      67.150  33.465  31.448  1.00 56.53           C  
-ATOM   4263  C   THR F 104      68.095  32.841  32.446  1.00 56.82           C  
-ATOM   4264  O   THR F 104      69.282  32.592  32.135  1.00 56.00           O  
-ATOM   4265  CB  THR F 104      67.866  34.787  31.041  1.00 53.65           C  
-ATOM   4266  OG1 THR F 104      67.954  35.583  32.229  1.00 52.25           O  
-ATOM   4267  CG2 THR F 104      67.007  35.500  30.015  1.00 42.43           C  
-ATOM   4268  N   GLY F 105      67.743  32.970  33.724  1.00 55.05           N  
-ATOM   4269  CA  GLY F 105      68.627  32.486  34.789  1.00 47.01           C  
-ATOM   4270  C   GLY F 105      69.676  33.532  35.052  1.00 44.96           C  
-ATOM   4271  O   GLY F 105      70.563  33.283  35.860  1.00 45.44           O  
-ATOM   4272  N   GLU F 106      69.535  34.739  34.469  1.00 45.39           N  
-ATOM   4273  CA  GLU F 106      70.464  35.806  34.835  1.00 47.99           C  
-ATOM   4274  C   GLU F 106      70.301  36.225  36.318  1.00 50.23           C  
-ATOM   4275  O   GLU F 106      69.215  36.371  36.905  1.00 46.69           O  
-ATOM   4276  CB  GLU F 106      70.203  36.972  33.906  1.00 49.04           C  
-ATOM   4277  CG  GLU F 106      70.715  36.875  32.448  1.00 47.49           C  
-ATOM   4278  CD  GLU F 106      70.133  38.088  31.730  1.00 40.85           C  
-ATOM   4279  OE1 GLU F 106      70.856  39.082  31.459  1.00 58.62           O  
-ATOM   4280  OE2 GLU F 106      68.923  38.138  31.461  1.00 48.48           O  
-ATOM   4281  N   THR F 107      71.384  36.739  36.853  1.00 45.28           N  
-ATOM   4282  CA  THR F 107      71.651  37.062  38.229  1.00 46.75           C  
-ATOM   4283  C   THR F 107      72.314  38.406  38.405  1.00 47.45           C  
-ATOM   4284  O   THR F 107      72.838  38.944  37.422  1.00 40.67           O  
-ATOM   4285  CB  THR F 107      72.664  35.936  38.628  1.00 56.67           C  
-ATOM   4286  OG1 THR F 107      71.909  34.956  39.338  1.00 61.48           O  
-ATOM   4287  CG2 THR F 107      73.885  36.416  39.334  1.00 48.01           C  
-ATOM   4288  N   GLY F 108      72.171  39.014  39.575  1.00 45.56           N  
-ATOM   4289  CA  GLY F 108      72.693  40.296  39.930  1.00 47.03           C  
-ATOM   4290  C   GLY F 108      72.444  41.499  39.055  1.00 49.07           C  
-ATOM   4291  O   GLY F 108      71.353  41.737  38.534  1.00 47.82           O  
-ATOM   4292  N   PRO F 109      73.515  42.232  38.740  1.00 55.25           N  
-ATOM   4293  CA  PRO F 109      73.511  43.384  37.831  1.00 52.97           C  
-ATOM   4294  C   PRO F 109      72.727  43.126  36.561  1.00 48.02           C  
-ATOM   4295  O   PRO F 109      71.808  43.835  36.157  1.00 49.44           O  
-ATOM   4296  CB  PRO F 109      74.981  43.621  37.463  1.00 54.31           C  
-ATOM   4297  CG  PRO F 109      75.810  42.705  38.290  1.00 56.54           C  
-ATOM   4298  CD  PRO F 109      74.908  41.979  39.256  1.00 54.67           C  
-ATOM   4299  N   ASP F 110      73.025  42.022  35.912  1.00 43.67           N  
-ATOM   4300  CA  ASP F 110      72.305  41.603  34.715  1.00 45.48           C  
-ATOM   4301  C   ASP F 110      70.804  41.451  34.815  1.00 52.00           C  
-ATOM   4302  O   ASP F 110      70.121  41.289  33.771  1.00 48.26           O  
-ATOM   4303  CB  ASP F 110      72.878  40.209  34.400  1.00 41.02           C  
-ATOM   4304  CG  ASP F 110      74.334  40.255  33.915  1.00 42.56           C  
-ATOM   4305  OD1 ASP F 110      74.974  41.322  33.848  1.00 47.95           O  
-ATOM   4306  OD2 ASP F 110      74.824  39.166  33.548  1.00 40.31           O  
-ATOM   4307  N   ALA F 111      70.234  41.216  36.009  1.00 52.80           N  
-ATOM   4308  CA  ALA F 111      68.824  40.801  36.040  1.00 56.63           C  
-ATOM   4309  C   ALA F 111      67.884  41.915  36.447  1.00 59.10           C  
-ATOM   4310  O   ALA F 111      66.678  41.752  36.287  1.00 58.11           O  
-ATOM   4311  CB  ALA F 111      68.667  39.523  36.839  1.00 56.30           C  
-ATOM   4312  N   VAL F 112      68.407  43.078  36.773  1.00 67.80           N  
-ATOM   4313  CA  VAL F 112      67.541  44.225  37.087  1.00 74.78           C  
-ATOM   4314  C   VAL F 112      66.948  44.827  35.817  1.00 75.64           C  
-ATOM   4315  O   VAL F 112      67.730  45.514  35.116  1.00 77.25           O  
-ATOM   4316  CB  VAL F 112      68.343  45.284  37.871  1.00 77.84           C  
-ATOM   4317  CG1 VAL F 112      67.508  46.521  38.131  1.00 82.64           C  
-ATOM   4318  CG2 VAL F 112      68.834  44.664  39.174  1.00 76.88           C  
-TER    4319      VAL F 112                                                      
-HETATM 4320  O   HOH A 113      24.880  22.943  33.832  1.00 27.88           O  
-HETATM 4321  O   HOH A 114      25.608  20.621  35.226  1.00 25.69           O  
-HETATM 4322  O   HOH A 115      17.691  34.034  27.494  1.00 25.14           O  
-HETATM 4323  O   HOH A 116      31.930  25.046  34.344  1.00 35.59           O  
-HETATM 4324  O   HOH A 117      21.341  18.558  30.258  1.00 29.65           O  
-HETATM 4325  O   HOH A 118      33.613  23.559  32.419  1.00 43.60           O  
-HETATM 4326  O   HOH A 119      16.064  42.078  42.283  1.00 40.92           O  
-HETATM 4327  O   HOH A 120      25.192  48.938  30.638  1.00 35.00           O  
-HETATM 4328  O   HOH A 121      26.958  24.303  29.802  1.00 36.78           O  
-HETATM 4329  O   HOH A 122      12.938  31.344  39.514  1.00 41.29           O  
-HETATM 4330  O   HOH A 123      20.226  24.019  21.217  1.00 34.43           O  
-HETATM 4331  O   HOH A 124      16.491  20.440  36.655  1.00 33.94           O  
-HETATM 4332  O   HOH A 125      24.704  38.997  31.648  1.00 41.22           O  
-HETATM 4333  O   HOH A 126      11.056  21.523  32.006  1.00 59.95           O  
-HETATM 4334  O   HOH A 127      34.943  16.209  33.625  1.00 49.89           O  
-HETATM 4335  O   HOH A 128      29.040  18.728  33.171  1.00 48.40           O  
-HETATM 4336  O   HOH A 129      31.028  26.381  23.413  1.00 35.19           O  
-HETATM 4337  O   HOH A 130      22.915  19.799  42.272  1.00 63.65           O  
-HETATM 4338  O   HOH B 113       4.097  42.618  24.973  1.00 27.91           O  
-HETATM 4339  O   HOH B 114      17.270  39.303  19.732  1.00 33.43           O  
-HETATM 4340  O   HOH B 115      14.870  14.719  25.052  1.00 28.53           O  
-HETATM 4341  O   HOH B 116      -0.541  43.861  17.688  1.00 31.47           O  
-HETATM 4342  O   HOH B 117      11.268  48.781  12.584  1.00 39.94           O  
-HETATM 4343  O   HOH B 118      11.736  17.203  18.588  1.00 43.38           O  
-HETATM 4344  O   HOH B 119      19.657  36.553  21.318  1.00 34.44           O  
-HETATM 4345  O   HOH B 120      18.769  35.440  23.941  1.00 36.27           O  
-HETATM 4346  O   HOH B 121       4.957  44.589  31.810  1.00 36.82           O  
-HETATM 4347  O   HOH B 122      19.977  41.546  25.036  1.00 45.28           O  
-HETATM 4348  O   HOH B 123       3.804  42.706  34.117  1.00 47.01           O  
-HETATM 4349  O   HOH B 124      15.069  29.765  22.129  1.00 30.80           O  
-HETATM 4350  O   HOH B 125      19.899  45.755  26.258  1.00 37.54           O  
-HETATM 4351  O   HOH B 126       1.812  43.067  15.928  1.00 35.30           O  
-HETATM 4352  O   HOH B 127      22.934  14.029  21.685  1.00 62.91           O  
-HETATM 4353  O   HOH B 128       5.917  55.498  17.271  1.00 53.70           O  
-HETATM 4354  O   HOH B 129       8.802  24.218  32.380  1.00 55.44           O  
-HETATM 4355  O   HOH B 130       7.993  10.848  24.475  1.00 37.27           O  
-HETATM 4356  O   HOH B 131      17.695  20.863  20.837  1.00 33.24           O  
-HETATM 4357  O   HOH B 132      14.129  11.561  27.712  1.00 54.44           O  
-HETATM 4358  O   HOH B 133      14.252  19.779  20.076  1.00 38.05           O  
-HETATM 4359  O   HOH B 134      -2.521  48.467  20.218  1.00 44.89           O  
-HETATM 4360  O   HOH B 135      16.767  13.094  19.412  1.00 52.07           O  
-HETATM 4361  O   HOH B 136      -0.723  48.517  22.159  1.00 49.89           O  
-HETATM 4362  O   HOH B 137       0.370  50.986  17.684  1.00 53.26           O  
-HETATM 4363  O   HOH B 138      21.737  42.207  19.347  1.00 59.14           O  
-HETATM 4364  O   HOH C 113      24.616  33.456  20.896  1.00 28.77           O  
-HETATM 4365  O   HOH C 114      28.883  45.586  32.132  1.00 38.59           O  
-HETATM 4366  O   HOH C 115      28.570  37.470   7.759  1.00 42.99           O  
-HETATM 4367  O   HOH C 116      36.442  28.970  18.063  1.00 41.29           O  
-HETATM 4368  O   HOH C 117      21.262  34.421  22.466  1.00 35.14           O  
-HETATM 4369  O   HOH C 118      19.132  29.251  18.673  1.00 35.34           O  
-HETATM 4370  O   HOH C 119      26.683  37.064  28.476  1.00 51.52           O  
-HETATM 4371  O   HOH C 120      32.790  32.660  26.093  1.00 46.63           O  
-HETATM 4372  O   HOH C 121      17.456  31.707  12.083  1.00 54.20           O  
-HETATM 4373  O   HOH C 122      35.283  26.599  18.810  1.00 42.25           O  
-HETATM 4374  O   HOH C 123      43.276  42.975  23.072  1.00 55.77           O  
-HETATM 4375  O   HOH C 124      34.990  25.350  11.973  1.00 54.12           O  
-HETATM 4376  O   HOH D 113      61.404  38.749  30.983  1.00 35.83           O  
-HETATM 4377  O   HOH D 114      52.873  37.498  49.075  1.00 32.24           O  
-HETATM 4378  O   HOH D 115      61.357  23.655  68.264  1.00 30.74           O  
-HETATM 4379  O   HOH D 116      64.496  34.845  65.225  1.00 27.08           O  
-HETATM 4380  O   HOH D 117      61.914  36.536  33.595  1.00 34.47           O  
-HETATM 4381  O   HOH D 118      63.242  22.648  65.944  1.00 33.15           O  
-HETATM 4382  O   HOH D 119      62.607  38.775  49.328  1.00 34.12           O  
-HETATM 4383  O   HOH D 120      45.994  57.934  26.883  1.00 39.69           O  
-HETATM 4384  O   HOH D 121      55.681  24.159  65.838  1.00 36.52           O  
-HETATM 4385  O   HOH D 122      54.917  24.586  48.873  1.00 41.93           O  
-HETATM 4386  O   HOH D 123      63.669  26.138  55.669  1.00 40.72           O  
-HETATM 4387  O   HOH D 124      52.859  43.290  47.842  1.00 40.15           O  
-HETATM 4388  O   HOH D 125      58.744  40.675  49.465  1.00 45.33           O  
-HETATM 4389  O   HOH D 126      55.831  33.932  54.061  1.00 45.05           O  
-HETATM 4390  O   HOH D 127      56.132  32.898  35.663  1.00 38.32           O  
-HETATM 4391  O   HOH D 128      62.567  24.752  61.899  1.00 36.23           O  
-HETATM 4392  O   HOH D 129      55.882  37.596  36.372  1.00 44.01           O  
-HETATM 4393  O   HOH D 130      58.748  23.394  64.981  1.00 48.54           O  
-HETATM 4394  O   HOH D 131      46.771  43.885  44.889  1.00 36.01           O  
-HETATM 4395  O   HOH D 132      50.130  25.827  37.754  1.00 50.88           O  
-HETATM 4396  O   HOH D 133      66.044  25.741  60.325  1.00 45.13           O  
-HETATM 4397  O   HOH D 134      60.506  42.603  50.916  1.00 47.94           O  
-HETATM 4398  O   HOH D 135      56.045  28.168  22.221  1.00 57.87           O  
-HETATM 4399  O   HOH D 136      53.193  47.757  28.938  1.00 45.64           O  
-HETATM 4400  O   HOH D 137      69.139  30.699  58.811  1.00 46.93           O  
-HETATM 4401  O   HOH D 138      66.874  42.038  57.274  1.00 40.22           O  
-HETATM 4402  O   HOH E 113      51.375  26.807  63.388  1.00 26.85           O  
-HETATM 4403  O   HOH E 114      46.500  34.660  63.822  1.00 27.79           O  
-HETATM 4404  O   HOH E 115      51.741  29.942  64.510  1.00 27.16           O  
-HETATM 4405  O   HOH E 116      50.764  44.827  54.417  1.00 29.50           O  
-HETATM 4406  O   HOH E 117      42.364  36.854  72.821  1.00 36.81           O  
-HETATM 4407  O   HOH E 118      39.972  40.974  66.257  1.00 35.29           O  
-HETATM 4408  O   HOH E 119      59.401  42.322  57.941  1.00 32.31           O  
-HETATM 4409  O   HOH E 120      39.192  41.309  63.277  1.00 34.06           O  
-HETATM 4410  O   HOH E 121      52.462  41.332  50.167  1.00 42.81           O  
-HETATM 4411  O   HOH E 122      46.239  39.587  47.352  1.00 39.19           O  
-HETATM 4412  O   HOH E 123      36.249  42.211  65.693  1.00 36.98           O  
-HETATM 4413  O   HOH E 124      54.683  40.099  75.115  1.00 42.27           O  
-HETATM 4414  O   HOH E 125      44.943  35.750  71.718  1.00 43.13           O  
-HETATM 4415  O   HOH E 126      56.524  42.292  54.615  1.00 40.99           O  
-HETATM 4416  O   HOH E 127      41.979  29.433  64.566  1.00 55.60           O  
-HETATM 4417  O   HOH E 128      58.561  30.642  57.281  1.00 43.18           O  
-HETATM 4418  O   HOH E 129      58.828  53.550  66.427  1.00 41.38           O  
-HETATM 4419  O   HOH E 130      60.300  47.604  72.847  1.00 35.97           O  
-HETATM 4420  O   HOH F 113      53.505  46.308  45.358  1.00 32.02           O  
-HETATM 4421  O   HOH F 114      57.772  53.941  35.335  1.00 31.45           O  
-HETATM 4422  O   HOH F 115      50.752  60.134  47.875  1.00 32.12           O  
-HETATM 4423  O   HOH F 116      67.698  46.620  54.396  1.00 41.89           O  
-HETATM 4424  O   HOH F 117      51.605  62.436  56.457  1.00 44.75           O  
-HETATM 4425  O   HOH F 118      48.626  63.503  39.814  1.00 36.79           O  
-HETATM 4426  O   HOH F 119      48.465  60.628  38.979  1.00 38.54           O  
-HETATM 4427  O   HOH F 120      61.637  62.437  37.241  1.00 38.57           O  
-HETATM 4428  O   HOH F 121      55.331  54.054  31.835  1.00 40.78           O  
-HETATM 4429  O   HOH F 122      51.897  44.007  50.616  1.00 37.56           O  
-HETATM 4430  O   HOH F 123      53.931  61.825  54.191  1.00 36.52           O  
-HETATM 4431  O   HOH F 124      70.716  58.195  41.766  1.00 49.76           O  
-HETATM 4432  O   HOH F 125      56.176  52.141  33.956  1.00 57.35           O  
-HETATM 4433  O   HOH F 126      61.532  48.542  50.673  1.00 35.37           O  
-HETATM 4434  O   HOH F 127      68.554  49.718  38.333  1.00 47.44           O  
-HETATM 4435  O   HOH F 128      55.329  47.151  35.834  1.00 45.65           O  
-HETATM 4436  O   HOH F 129      65.259  62.027  40.446  1.00 52.82           O  
-HETATM 4437  O   HOH F 130      58.610  43.229  44.667  0.00 62.79           O  
-MASTER      435    0    0   27   32    0    0    6 4431    6    0   54          
-END                                                                             
diff --git a/plip/test/pdb/1n7g.pdb b/plip/test/pdb/1n7g.pdb
deleted file mode 100644
index 144558b..0000000
--- a/plip/test/pdb/1n7g.pdb
+++ /dev/null
@@ -1,12315 +0,0 @@
-HEADER    LYASE                                   14-NOV-02   1N7G              
-TITLE     CRYSTAL STRUCTURE OF THE GDP-MANNOSE 4,6-DEHYDRATASE                  
-TITLE    2 TERNARY COMPLEX WITH NADPH AND GDP-RHAMNOSE.                         
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: GDP-D-MANNOSE-4,6-DEHYDRATASE;                             
-COMPND   3 CHAIN: A, B, C, D;                                                   
-COMPND   4 EC: 4.2.1.47;                                                        
-COMPND   5 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
-SOURCE   3 ORGANISM_COMMON: THALE CRESS;                                        
-SOURCE   4 ORGANISM_TAXID: 3702;                                                
-SOURCE   5 GENE: MUR1;                                                          
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
-SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
-SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
-KEYWDS    ROSSMANN FOLD, SDR, SHORT-CHAIN DEHYDROGENASE/REDUCTASE,              
-KEYWDS   2 LYASE                                                                
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    A.M.MULICHAK,C.P.BONIN,W.-D.REITER,R.M.GARAVITO                       
-REVDAT   2   24-FEB-09 1N7G    1       VERSN                                    
-REVDAT   1   07-JAN-03 1N7G    0                                                
-JRNL        AUTH   A.M.MULICHAK,C.P.BONIN,W.-D.REITER,R.M.GARAVITO              
-JRNL        TITL   THE STRUCTURE OF THE MUR1 GDP-MANNOSE                        
-JRNL        TITL 2 4,6-DEHYDRATASE FROM A. THALIANA: IMPLICATIONS FOR           
-JRNL        TITL 3 LIGAND BINDING AND SPECIFICITY.                              
-JRNL        REF    BIOCHEMISTRY                  V.  41 15557 2002              
-JRNL        REFN                   ISSN 0006-2960                               
-JRNL        PMID   12501186                                                     
-JRNL        DOI    10.1021/BI0266683                                            
-REMARK   1                                                                      
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS 0.9                                              
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
-REMARK   3   NUMBER OF REFLECTIONS             : 72041                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.201                           
-REMARK   3   FREE R VALUE                     : 0.247                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
-REMARK   3   FREE R VALUE TEST SET COUNT      : 3521                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
-REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
-REMARK   3   BIN FREE R VALUE                    : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 10253                                   
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 306                                     
-REMARK   3   SOLVENT ATOMS            : 475                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
-REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.005                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.15                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.77                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : NULL                                                 
-REMARK   3   KSOL        : NULL                                                 
-REMARK   3   BSOL        : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: MISSING SIDE CHAIN ATOMS FOR              
-REMARK   3  RESIDUES LISTED IN REMARK 470 WERE UNOBSERVED AND WERE NOT          
-REMARK   3  REFINED.                                                            
-REMARK   4                                                                      
-REMARK   4 1N7G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-02.                  
-REMARK 100 THE RCSB ID CODE IS RCSB017613.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-01                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 6.4                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : APS                                
-REMARK 200  BEAMLINE                       : 5ID-B                              
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72438                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : 0.03800                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.5                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : 0.20200                            
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
-REMARK 200 SOFTWARE USED: CNS                                                   
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 47.03                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 400,               
-REMARK 280  IMIDAZOLE BUFFER, PH 6.4, VAPOR DIFFUSION, HANGING DROP,            
-REMARK 280  TEMPERATURE 298K                                                    
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       56.59000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.44500            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.50500            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.44500            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.59000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.50500            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE HOMOTETRAMER                  
-REMARK 300 OBSERVED IN THE ASYMMETRIC UNIT.                                     
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 21230 ANGSTROM**2                         
-REMARK 350 SURFACE AREA OF THE COMPLEX: 41890 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     ALA A     2                                                      
-REMARK 465     SER A     3                                                      
-REMARK 465     GLU A     4                                                      
-REMARK 465     ASN A     5                                                      
-REMARK 465     ASN A     6                                                      
-REMARK 465     GLY A     7                                                      
-REMARK 465     SER A     8                                                      
-REMARK 465     ARG A     9                                                      
-REMARK 465     SER A    10                                                      
-REMARK 465     ASP A    11                                                      
-REMARK 465     SER A    12                                                      
-REMARK 465     GLU A    13                                                      
-REMARK 465     SER A    14                                                      
-REMARK 465     ILE A    15                                                      
-REMARK 465     THR A    16                                                      
-REMARK 465     ALA A    17                                                      
-REMARK 465     PRO A    18                                                      
-REMARK 465     LYS A    19                                                      
-REMARK 465     ALA A    20                                                      
-REMARK 465     ASP A    21                                                      
-REMARK 465     SER A    22                                                      
-REMARK 465     THR A    23                                                      
-REMARK 465     VAL A    24                                                      
-REMARK 465     VAL A    25                                                      
-REMARK 465     GLU A    26                                                      
-REMARK 465     PRO A    27                                                      
-REMARK 465     ILE A    75                                                      
-REMARK 465     ASP A    76                                                      
-REMARK 465     PRO A    77                                                      
-REMARK 465     HIS A    78                                                      
-REMARK 465     ASN A    79                                                      
-REMARK 465     VAL A    80                                                      
-REMARK 465     ASN A    81                                                      
-REMARK 465     ASP A   368                                                      
-REMARK 465     ALA A   369                                                      
-REMARK 465     LYS A   370                                                      
-REMARK 465     GLN A   371                                                      
-REMARK 465     GLN A   372                                                      
-REMARK 465     PRO A   373                                                      
-REMARK 465     LEU A   374                                                      
-REMARK 465     GLU A   375                                                      
-REMARK 465     HIS A   376                                                      
-REMARK 465     HIS A   377                                                      
-REMARK 465     HIS A   378                                                      
-REMARK 465     HIS A   379                                                      
-REMARK 465     HIS A   380                                                      
-REMARK 465     HIS A   381                                                      
-REMARK 465     MET B     1                                                      
-REMARK 465     ALA B     2                                                      
-REMARK 465     SER B     3                                                      
-REMARK 465     GLU B     4                                                      
-REMARK 465     ASN B     5                                                      
-REMARK 465     ASN B     6                                                      
-REMARK 465     GLY B     7                                                      
-REMARK 465     SER B     8                                                      
-REMARK 465     ARG B     9                                                      
-REMARK 465     SER B    10                                                      
-REMARK 465     ASP B    11                                                      
-REMARK 465     SER B    12                                                      
-REMARK 465     GLU B    13                                                      
-REMARK 465     SER B    14                                                      
-REMARK 465     ILE B    15                                                      
-REMARK 465     THR B    16                                                      
-REMARK 465     ALA B    17                                                      
-REMARK 465     PRO B    18                                                      
-REMARK 465     LYS B    19                                                      
-REMARK 465     ALA B    20                                                      
-REMARK 465     ASP B    21                                                      
-REMARK 465     SER B    22                                                      
-REMARK 465     THR B    23                                                      
-REMARK 465     VAL B    24                                                      
-REMARK 465     VAL B    25                                                      
-REMARK 465     GLU B    26                                                      
-REMARK 465     PRO B    27                                                      
-REMARK 465     PRO B    77                                                      
-REMARK 465     HIS B    78                                                      
-REMARK 465     ASN B    79                                                      
-REMARK 465     VAL B    80                                                      
-REMARK 465     ASN B    81                                                      
-REMARK 465     ALA B   369                                                      
-REMARK 465     LYS B   370                                                      
-REMARK 465     GLN B   371                                                      
-REMARK 465     GLN B   372                                                      
-REMARK 465     PRO B   373                                                      
-REMARK 465     LEU B   374                                                      
-REMARK 465     GLU B   375                                                      
-REMARK 465     HIS B   376                                                      
-REMARK 465     HIS B   377                                                      
-REMARK 465     HIS B   378                                                      
-REMARK 465     HIS B   379                                                      
-REMARK 465     HIS B   380                                                      
-REMARK 465     HIS B   381                                                      
-REMARK 465     MET C     1                                                      
-REMARK 465     ALA C     2                                                      
-REMARK 465     SER C     3                                                      
-REMARK 465     GLU C     4                                                      
-REMARK 465     ASN C     5                                                      
-REMARK 465     ASN C     6                                                      
-REMARK 465     GLY C     7                                                      
-REMARK 465     SER C     8                                                      
-REMARK 465     ARG C     9                                                      
-REMARK 465     SER C    10                                                      
-REMARK 465     ASP C    11                                                      
-REMARK 465     SER C    12                                                      
-REMARK 465     GLU C    13                                                      
-REMARK 465     SER C    14                                                      
-REMARK 465     ILE C    15                                                      
-REMARK 465     THR C    16                                                      
-REMARK 465     ALA C    17                                                      
-REMARK 465     PRO C    18                                                      
-REMARK 465     LYS C    19                                                      
-REMARK 465     ALA C    20                                                      
-REMARK 465     ASP C    21                                                      
-REMARK 465     SER C    22                                                      
-REMARK 465     THR C    23                                                      
-REMARK 465     VAL C    24                                                      
-REMARK 465     VAL C    25                                                      
-REMARK 465     GLU C    26                                                      
-REMARK 465     PRO C    27                                                      
-REMARK 465     ASP C    76                                                      
-REMARK 465     PRO C    77                                                      
-REMARK 465     HIS C    78                                                      
-REMARK 465     ASN C    79                                                      
-REMARK 465     VAL C    80                                                      
-REMARK 465     ASN C    81                                                      
-REMARK 465     ASP C   368                                                      
-REMARK 465     ALA C   369                                                      
-REMARK 465     LYS C   370                                                      
-REMARK 465     GLN C   371                                                      
-REMARK 465     GLN C   372                                                      
-REMARK 465     PRO C   373                                                      
-REMARK 465     LEU C   374                                                      
-REMARK 465     GLU C   375                                                      
-REMARK 465     HIS C   376                                                      
-REMARK 465     HIS C   377                                                      
-REMARK 465     HIS C   378                                                      
-REMARK 465     HIS C   379                                                      
-REMARK 465     HIS C   380                                                      
-REMARK 465     HIS C   381                                                      
-REMARK 465     MET D     1                                                      
-REMARK 465     ALA D     2                                                      
-REMARK 465     SER D     3                                                      
-REMARK 465     GLU D     4                                                      
-REMARK 465     ASN D     5                                                      
-REMARK 465     ASN D     6                                                      
-REMARK 465     GLY D     7                                                      
-REMARK 465     SER D     8                                                      
-REMARK 465     ARG D     9                                                      
-REMARK 465     SER D    10                                                      
-REMARK 465     ASP D    11                                                      
-REMARK 465     SER D    12                                                      
-REMARK 465     GLU D    13                                                      
-REMARK 465     SER D    14                                                      
-REMARK 465     ILE D    15                                                      
-REMARK 465     THR D    16                                                      
-REMARK 465     ALA D    17                                                      
-REMARK 465     PRO D    18                                                      
-REMARK 465     LYS D    19                                                      
-REMARK 465     ALA D    20                                                      
-REMARK 465     ASP D    21                                                      
-REMARK 465     SER D    22                                                      
-REMARK 465     THR D    23                                                      
-REMARK 465     VAL D    24                                                      
-REMARK 465     VAL D    25                                                      
-REMARK 465     GLU D    26                                                      
-REMARK 465     PRO D    27                                                      
-REMARK 465     ASP D    76                                                      
-REMARK 465     PRO D    77                                                      
-REMARK 465     HIS D    78                                                      
-REMARK 465     ASN D    79                                                      
-REMARK 465     VAL D    80                                                      
-REMARK 465     ASN D    81                                                      
-REMARK 465     LYS D    82                                                      
-REMARK 465     ALA D    83                                                      
-REMARK 465     LEU D   246                                                      
-REMARK 465     GLY D   247                                                      
-REMARK 465     ASN D   248                                                      
-REMARK 465     LEU D   249                                                      
-REMARK 465     GLN D   250                                                      
-REMARK 465     GLN D   310                                                      
-REMARK 465     ARG D   311                                                      
-REMARK 465     TYR D   312                                                      
-REMARK 465     PHE D   313                                                      
-REMARK 465     ARG D   314                                                      
-REMARK 465     PRO D   315                                                      
-REMARK 465     ALA D   316                                                      
-REMARK 465     GLU D   317                                                      
-REMARK 465     VAL D   318                                                      
-REMARK 465     ASP D   363                                                      
-REMARK 465     ALA D   364                                                      
-REMARK 465     GLY D   365                                                      
-REMARK 465     TYR D   366                                                      
-REMARK 465     MET D   367                                                      
-REMARK 465     ASP D   368                                                      
-REMARK 465     ALA D   369                                                      
-REMARK 465     LYS D   370                                                      
-REMARK 465     GLN D   371                                                      
-REMARK 465     GLN D   372                                                      
-REMARK 465     PRO D   373                                                      
-REMARK 465     LEU D   374                                                      
-REMARK 465     GLU D   375                                                      
-REMARK 465     HIS D   376                                                      
-REMARK 465     HIS D   377                                                      
-REMARK 465     HIS D   378                                                      
-REMARK 465     HIS D   379                                                      
-REMARK 465     HIS D   380                                                      
-REMARK 465     HIS D   381                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     LYS A  82    CG   CD   CE   NZ                                   
-REMARK 470     LYS A  86    CG   CD   CE   NZ                                   
-REMARK 470     LYS A 106    CG   CD   CE   NZ                                   
-REMARK 470     LYS A 243    CG   CD   CE   NZ                                   
-REMARK 470     GLU A 263    CG   CD   OE1  OE2                                  
-REMARK 470     GLU A 272    CG   CD   OE1  OE2                                  
-REMARK 470     GLU A 283    CG   CD   OE1  OE2                                  
-REMARK 470     GLN A 310    CG   CD   OE1  NE2                                  
-REMARK 470     GLU A 330    CG   CD   OE1  OE2                                  
-REMARK 470     LYS A 335    CG   CD   CE   NZ                                   
-REMARK 470     ILE B  75    CG1  CG2  CD1                                       
-REMARK 470     ASP B  76    CG   OD1  OD2                                       
-REMARK 470     LYS B  82    CG   CD   CE   NZ                                   
-REMARK 470     LYS B  86    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 243    CG   CD   CE   NZ                                   
-REMARK 470     GLU B 263    CG   CD   OE1  OE2                                  
-REMARK 470     GLU B 272    CG   CD   OE1  OE2                                  
-REMARK 470     LYS B 303    CG   CD   CE   NZ                                   
-REMARK 470     GLN B 310    CG   CD   OE1  NE2                                  
-REMARK 470     ARG B 311    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     LYS B 329    CG   CD   CE   NZ                                   
-REMARK 470     GLU B 330    CG   CD   OE1  OE2                                  
-REMARK 470     LYS B 335    CG   CD   CE   NZ                                   
-REMARK 470     GLN B 337    CG   CD   OE1  NE2                                  
-REMARK 470     GLU B 341    CG   CD   OE1  OE2                                  
-REMARK 470     ASP B 368    CG   OD1  OD2                                       
-REMARK 470     ILE C  75    CG1  CG2  CD1                                       
-REMARK 470     LYS C  82    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 243    CG   CD   CE   NZ                                   
-REMARK 470     GLU C 263    CG   CD   OE1  OE2                                  
-REMARK 470     GLU C 272    CG   CD   OE1  OE2                                  
-REMARK 470     LYS C 273    CG   CD   CE   NZ                                   
-REMARK 470     GLN C 310    CG   CD   OE1  NE2                                  
-REMARK 470     ARG C 311    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     LYS C 329    CG   CD   CE   NZ                                   
-REMARK 470     GLU C 330    CG   CD   OE1  OE2                                  
-REMARK 470     LYS C 335    CG   CD   CE   NZ                                   
-REMARK 470     GLN C 337    CG   CD   OE1  NE2                                  
-REMARK 470     LYS C 356    CG   CD   CE   NZ                                   
-REMARK 470     TYR D  74    CG   CD1  CD2  CE1  CE2  CZ   OH                    
-REMARK 470     ILE D  75    CG1  CG2  CD1                                       
-REMARK 470     ARG D 235    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     LYS D 237    CG   CD   CE   NZ                                   
-REMARK 470     VAL D 238    CG1  CG2                                            
-REMARK 470     LEU D 240    CG   CD1  CD2                                       
-REMARK 470     THR D 242    OG1  CG2                                            
-REMARK 470     LYS D 243    CG   CD   CE   NZ                                   
-REMARK 470     LEU D 244    CG   CD1  CD2                                       
-REMARK 470     PHE D 245    CG   CD1  CD2  CE1  CE2  CZ                         
-REMARK 470     GLU D 283    CG   CD   OE1  OE2                                  
-REMARK 470     GLU D 289    CG   CD   OE1  OE2                                  
-REMARK 470     LEU D 291    CG   CD1  CD2                                       
-REMARK 470     SER D 294    OG                                                  
-REMARK 470     ASN D 301    CG   OD1  ND2                                       
-REMARK 470     TRP D 302    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
-REMARK 470     TRP D 302    CZ3  CH2                                            
-REMARK 470     LYS D 303    CG   CD   CE   NZ                                   
-REMARK 470     TYR D 305    CG   CD1  CD2  CE1  CE2  CZ   OH                    
-REMARK 470     VAL D 306    CG1  CG2                                            
-REMARK 470     GLU D 307    CG   CD   OE1  OE2                                  
-REMARK 470     ASP D 309    CG   OD1  OD2                                       
-REMARK 470     ASP D 319    CG   OD1  OD2                                       
-REMARK 470     LYS D 329    CG   CD   CE   NZ                                   
-REMARK 470     GLU D 330    CG   CD   OE1  OE2                                  
-REMARK 470     LYS D 335    CG   CD   CE   NZ                                   
-REMARK 470     GLN D 337    CG   CD   OE1  NE2                                  
-REMARK 470     GLU D 341    CG   CD   OE1  OE2                                  
-REMARK 470     ARG D 357    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     GLU D 358    CG   CD   OE1  OE2                                  
-REMARK 470     LYS D 359    CG   CD   CE   NZ                                   
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    GLN A 116   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
-REMARK 500    GLN B 116   N   -  CA  -  C   ANGL. DEV. = -18.1 DEGREES          
-REMARK 500    GLN C 116   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
-REMARK 500    GLN D 116   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ALA A  83       16.87   -179.67                                   
-REMARK 500    ALA A 134      -65.80    -97.22                                   
-REMARK 500    SER A 217      173.74    179.00                                   
-REMARK 500    PHE A 340      -70.13    -48.02                                   
-REMARK 500    ALA B  83      -96.71   -176.70                                   
-REMARK 500    ALA B 134      -73.38    -96.99                                   
-REMARK 500    HIS B 180       68.08   -157.87                                   
-REMARK 500    ALA C  83       67.05   -166.25                                   
-REMARK 500    ALA C 115      159.29    175.86                                   
-REMARK 500    ALA C 134      -69.81    -93.93                                   
-REMARK 500    HIS C 180       70.01   -158.57                                   
-REMARK 500    ASN D  66       10.47   -142.93                                   
-REMARK 500    ALA D 115      162.02    178.79                                   
-REMARK 500    ALA D 134      -71.63    -90.59                                   
-REMARK 500    THR D 242      -62.01    -99.89                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 701                 
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 702                 
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP C 703                 
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP D 704                 
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDR A 801                 
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDR A 802                 
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDR A 803                 
-DBREF  1N7G A    1   373  UNP    P93031   GMD2_ARATH       1    373             
-DBREF  1N7G B    1   373  UNP    P93031   GMD2_ARATH       1    373             
-DBREF  1N7G C    1   373  UNP    P93031   GMD2_ARATH       1    373             
-DBREF  1N7G D    1   373  UNP    P93031   GMD2_ARATH       1    373             
-SEQADV 1N7G LEU A  374  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G GLU A  375  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS A  376  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS A  377  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS A  378  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS A  379  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS A  380  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS A  381  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G LEU B  374  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G GLU B  375  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS B  376  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS B  377  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS B  378  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS B  379  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS B  380  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS B  381  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G LEU C  374  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G GLU C  375  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS C  376  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS C  377  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS C  378  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS C  379  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS C  380  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS C  381  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G LEU D  374  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G GLU D  375  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS D  376  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS D  377  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS D  378  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS D  379  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS D  380  UNP  P93031              EXPRESSION TAG                 
-SEQADV 1N7G HIS D  381  UNP  P93031              EXPRESSION TAG                 
-SEQRES   1 A  381  MET ALA SER GLU ASN ASN GLY SER ARG SER ASP SER GLU          
-SEQRES   2 A  381  SER ILE THR ALA PRO LYS ALA ASP SER THR VAL VAL GLU          
-SEQRES   3 A  381  PRO ARG LYS ILE ALA LEU ILE THR GLY ILE THR GLY GLN          
-SEQRES   4 A  381  ASP GLY SER TYR LEU THR GLU PHE LEU LEU GLY LYS GLY          
-SEQRES   5 A  381  TYR GLU VAL HIS GLY LEU ILE ARG ARG SER SER ASN PHE          
-SEQRES   6 A  381  ASN THR GLN ARG ILE ASN HIS ILE TYR ILE ASP PRO HIS          
-SEQRES   7 A  381  ASN VAL ASN LYS ALA LEU MET LYS LEU HIS TYR ALA ASP          
-SEQRES   8 A  381  LEU THR ASP ALA SER SER LEU ARG ARG TRP ILE ASP VAL          
-SEQRES   9 A  381  ILE LYS PRO ASP GLU VAL TYR ASN LEU ALA ALA GLN SER          
-SEQRES  10 A  381  HIS VAL ALA VAL SER PHE GLU ILE PRO ASP TYR THR ALA          
-SEQRES  11 A  381  ASP VAL VAL ALA THR GLY ALA LEU ARG LEU LEU GLU ALA          
-SEQRES  12 A  381  VAL ARG SER HIS THR ILE ASP SER GLY ARG THR VAL LYS          
-SEQRES  13 A  381  TYR TYR GLN ALA GLY SER SER GLU MET PHE GLY SER THR          
-SEQRES  14 A  381  PRO PRO PRO GLN SER GLU THR THR PRO PHE HIS PRO ARG          
-SEQRES  15 A  381  SER PRO TYR ALA ALA SER LYS CYS ALA ALA HIS TRP TYR          
-SEQRES  16 A  381  THR VAL ASN TYR ARG GLU ALA TYR GLY LEU PHE ALA CYS          
-SEQRES  17 A  381  ASN GLY ILE LEU PHE ASN HIS GLU SER PRO ARG ARG GLY          
-SEQRES  18 A  381  GLU ASN PHE VAL THR ARG LYS ILE THR ARG ALA LEU GLY          
-SEQRES  19 A  381  ARG ILE LYS VAL GLY LEU GLN THR LYS LEU PHE LEU GLY          
-SEQRES  20 A  381  ASN LEU GLN ALA SER ARG ASP TRP GLY PHE ALA GLY ASP          
-SEQRES  21 A  381  TYR VAL GLU ALA MET TRP LEU MET LEU GLN GLN GLU LYS          
-SEQRES  22 A  381  PRO ASP ASP TYR VAL VAL ALA THR GLU GLU GLY HIS THR          
-SEQRES  23 A  381  VAL GLU GLU PHE LEU ASP VAL SER PHE GLY TYR LEU GLY          
-SEQRES  24 A  381  LEU ASN TRP LYS ASP TYR VAL GLU ILE ASP GLN ARG TYR          
-SEQRES  25 A  381  PHE ARG PRO ALA GLU VAL ASP ASN LEU GLN GLY ASP ALA          
-SEQRES  26 A  381  SER LYS ALA LYS GLU VAL LEU GLY TRP LYS PRO GLN VAL          
-SEQRES  27 A  381  GLY PHE GLU LYS LEU VAL LYS MET MET VAL ASP GLU ASP          
-SEQRES  28 A  381  LEU GLU LEU ALA LYS ARG GLU LYS VAL LEU VAL ASP ALA          
-SEQRES  29 A  381  GLY TYR MET ASP ALA LYS GLN GLN PRO LEU GLU HIS HIS          
-SEQRES  30 A  381  HIS HIS HIS HIS                                              
-SEQRES   1 B  381  MET ALA SER GLU ASN ASN GLY SER ARG SER ASP SER GLU          
-SEQRES   2 B  381  SER ILE THR ALA PRO LYS ALA ASP SER THR VAL VAL GLU          
-SEQRES   3 B  381  PRO ARG LYS ILE ALA LEU ILE THR GLY ILE THR GLY GLN          
-SEQRES   4 B  381  ASP GLY SER TYR LEU THR GLU PHE LEU LEU GLY LYS GLY          
-SEQRES   5 B  381  TYR GLU VAL HIS GLY LEU ILE ARG ARG SER SER ASN PHE          
-SEQRES   6 B  381  ASN THR GLN ARG ILE ASN HIS ILE TYR ILE ASP PRO HIS          
-SEQRES   7 B  381  ASN VAL ASN LYS ALA LEU MET LYS LEU HIS TYR ALA ASP          
-SEQRES   8 B  381  LEU THR ASP ALA SER SER LEU ARG ARG TRP ILE ASP VAL          
-SEQRES   9 B  381  ILE LYS PRO ASP GLU VAL TYR ASN LEU ALA ALA GLN SER          
-SEQRES  10 B  381  HIS VAL ALA VAL SER PHE GLU ILE PRO ASP TYR THR ALA          
-SEQRES  11 B  381  ASP VAL VAL ALA THR GLY ALA LEU ARG LEU LEU GLU ALA          
-SEQRES  12 B  381  VAL ARG SER HIS THR ILE ASP SER GLY ARG THR VAL LYS          
-SEQRES  13 B  381  TYR TYR GLN ALA GLY SER SER GLU MET PHE GLY SER THR          
-SEQRES  14 B  381  PRO PRO PRO GLN SER GLU THR THR PRO PHE HIS PRO ARG          
-SEQRES  15 B  381  SER PRO TYR ALA ALA SER LYS CYS ALA ALA HIS TRP TYR          
-SEQRES  16 B  381  THR VAL ASN TYR ARG GLU ALA TYR GLY LEU PHE ALA CYS          
-SEQRES  17 B  381  ASN GLY ILE LEU PHE ASN HIS GLU SER PRO ARG ARG GLY          
-SEQRES  18 B  381  GLU ASN PHE VAL THR ARG LYS ILE THR ARG ALA LEU GLY          
-SEQRES  19 B  381  ARG ILE LYS VAL GLY LEU GLN THR LYS LEU PHE LEU GLY          
-SEQRES  20 B  381  ASN LEU GLN ALA SER ARG ASP TRP GLY PHE ALA GLY ASP          
-SEQRES  21 B  381  TYR VAL GLU ALA MET TRP LEU MET LEU GLN GLN GLU LYS          
-SEQRES  22 B  381  PRO ASP ASP TYR VAL VAL ALA THR GLU GLU GLY HIS THR          
-SEQRES  23 B  381  VAL GLU GLU PHE LEU ASP VAL SER PHE GLY TYR LEU GLY          
-SEQRES  24 B  381  LEU ASN TRP LYS ASP TYR VAL GLU ILE ASP GLN ARG TYR          
-SEQRES  25 B  381  PHE ARG PRO ALA GLU VAL ASP ASN LEU GLN GLY ASP ALA          
-SEQRES  26 B  381  SER LYS ALA LYS GLU VAL LEU GLY TRP LYS PRO GLN VAL          
-SEQRES  27 B  381  GLY PHE GLU LYS LEU VAL LYS MET MET VAL ASP GLU ASP          
-SEQRES  28 B  381  LEU GLU LEU ALA LYS ARG GLU LYS VAL LEU VAL ASP ALA          
-SEQRES  29 B  381  GLY TYR MET ASP ALA LYS GLN GLN PRO LEU GLU HIS HIS          
-SEQRES  30 B  381  HIS HIS HIS HIS                                              
-SEQRES   1 C  381  MET ALA SER GLU ASN ASN GLY SER ARG SER ASP SER GLU          
-SEQRES   2 C  381  SER ILE THR ALA PRO LYS ALA ASP SER THR VAL VAL GLU          
-SEQRES   3 C  381  PRO ARG LYS ILE ALA LEU ILE THR GLY ILE THR GLY GLN          
-SEQRES   4 C  381  ASP GLY SER TYR LEU THR GLU PHE LEU LEU GLY LYS GLY          
-SEQRES   5 C  381  TYR GLU VAL HIS GLY LEU ILE ARG ARG SER SER ASN PHE          
-SEQRES   6 C  381  ASN THR GLN ARG ILE ASN HIS ILE TYR ILE ASP PRO HIS          
-SEQRES   7 C  381  ASN VAL ASN LYS ALA LEU MET LYS LEU HIS TYR ALA ASP          
-SEQRES   8 C  381  LEU THR ASP ALA SER SER LEU ARG ARG TRP ILE ASP VAL          
-SEQRES   9 C  381  ILE LYS PRO ASP GLU VAL TYR ASN LEU ALA ALA GLN SER          
-SEQRES  10 C  381  HIS VAL ALA VAL SER PHE GLU ILE PRO ASP TYR THR ALA          
-SEQRES  11 C  381  ASP VAL VAL ALA THR GLY ALA LEU ARG LEU LEU GLU ALA          
-SEQRES  12 C  381  VAL ARG SER HIS THR ILE ASP SER GLY ARG THR VAL LYS          
-SEQRES  13 C  381  TYR TYR GLN ALA GLY SER SER GLU MET PHE GLY SER THR          
-SEQRES  14 C  381  PRO PRO PRO GLN SER GLU THR THR PRO PHE HIS PRO ARG          
-SEQRES  15 C  381  SER PRO TYR ALA ALA SER LYS CYS ALA ALA HIS TRP TYR          
-SEQRES  16 C  381  THR VAL ASN TYR ARG GLU ALA TYR GLY LEU PHE ALA CYS          
-SEQRES  17 C  381  ASN GLY ILE LEU PHE ASN HIS GLU SER PRO ARG ARG GLY          
-SEQRES  18 C  381  GLU ASN PHE VAL THR ARG LYS ILE THR ARG ALA LEU GLY          
-SEQRES  19 C  381  ARG ILE LYS VAL GLY LEU GLN THR LYS LEU PHE LEU GLY          
-SEQRES  20 C  381  ASN LEU GLN ALA SER ARG ASP TRP GLY PHE ALA GLY ASP          
-SEQRES  21 C  381  TYR VAL GLU ALA MET TRP LEU MET LEU GLN GLN GLU LYS          
-SEQRES  22 C  381  PRO ASP ASP TYR VAL VAL ALA THR GLU GLU GLY HIS THR          
-SEQRES  23 C  381  VAL GLU GLU PHE LEU ASP VAL SER PHE GLY TYR LEU GLY          
-SEQRES  24 C  381  LEU ASN TRP LYS ASP TYR VAL GLU ILE ASP GLN ARG TYR          
-SEQRES  25 C  381  PHE ARG PRO ALA GLU VAL ASP ASN LEU GLN GLY ASP ALA          
-SEQRES  26 C  381  SER LYS ALA LYS GLU VAL LEU GLY TRP LYS PRO GLN VAL          
-SEQRES  27 C  381  GLY PHE GLU LYS LEU VAL LYS MET MET VAL ASP GLU ASP          
-SEQRES  28 C  381  LEU GLU LEU ALA LYS ARG GLU LYS VAL LEU VAL ASP ALA          
-SEQRES  29 C  381  GLY TYR MET ASP ALA LYS GLN GLN PRO LEU GLU HIS HIS          
-SEQRES  30 C  381  HIS HIS HIS HIS                                              
-SEQRES   1 D  381  MET ALA SER GLU ASN ASN GLY SER ARG SER ASP SER GLU          
-SEQRES   2 D  381  SER ILE THR ALA PRO LYS ALA ASP SER THR VAL VAL GLU          
-SEQRES   3 D  381  PRO ARG LYS ILE ALA LEU ILE THR GLY ILE THR GLY GLN          
-SEQRES   4 D  381  ASP GLY SER TYR LEU THR GLU PHE LEU LEU GLY LYS GLY          
-SEQRES   5 D  381  TYR GLU VAL HIS GLY LEU ILE ARG ARG SER SER ASN PHE          
-SEQRES   6 D  381  ASN THR GLN ARG ILE ASN HIS ILE TYR ILE ASP PRO HIS          
-SEQRES   7 D  381  ASN VAL ASN LYS ALA LEU MET LYS LEU HIS TYR ALA ASP          
-SEQRES   8 D  381  LEU THR ASP ALA SER SER LEU ARG ARG TRP ILE ASP VAL          
-SEQRES   9 D  381  ILE LYS PRO ASP GLU VAL TYR ASN LEU ALA ALA GLN SER          
-SEQRES  10 D  381  HIS VAL ALA VAL SER PHE GLU ILE PRO ASP TYR THR ALA          
-SEQRES  11 D  381  ASP VAL VAL ALA THR GLY ALA LEU ARG LEU LEU GLU ALA          
-SEQRES  12 D  381  VAL ARG SER HIS THR ILE ASP SER GLY ARG THR VAL LYS          
-SEQRES  13 D  381  TYR TYR GLN ALA GLY SER SER GLU MET PHE GLY SER THR          
-SEQRES  14 D  381  PRO PRO PRO GLN SER GLU THR THR PRO PHE HIS PRO ARG          
-SEQRES  15 D  381  SER PRO TYR ALA ALA SER LYS CYS ALA ALA HIS TRP TYR          
-SEQRES  16 D  381  THR VAL ASN TYR ARG GLU ALA TYR GLY LEU PHE ALA CYS          
-SEQRES  17 D  381  ASN GLY ILE LEU PHE ASN HIS GLU SER PRO ARG ARG GLY          
-SEQRES  18 D  381  GLU ASN PHE VAL THR ARG LYS ILE THR ARG ALA LEU GLY          
-SEQRES  19 D  381  ARG ILE LYS VAL GLY LEU GLN THR LYS LEU PHE LEU GLY          
-SEQRES  20 D  381  ASN LEU GLN ALA SER ARG ASP TRP GLY PHE ALA GLY ASP          
-SEQRES  21 D  381  TYR VAL GLU ALA MET TRP LEU MET LEU GLN GLN GLU LYS          
-SEQRES  22 D  381  PRO ASP ASP TYR VAL VAL ALA THR GLU GLU GLY HIS THR          
-SEQRES  23 D  381  VAL GLU GLU PHE LEU ASP VAL SER PHE GLY TYR LEU GLY          
-SEQRES  24 D  381  LEU ASN TRP LYS ASP TYR VAL GLU ILE ASP GLN ARG TYR          
-SEQRES  25 D  381  PHE ARG PRO ALA GLU VAL ASP ASN LEU GLN GLY ASP ALA          
-SEQRES  26 D  381  SER LYS ALA LYS GLU VAL LEU GLY TRP LYS PRO GLN VAL          
-SEQRES  27 D  381  GLY PHE GLU LYS LEU VAL LYS MET MET VAL ASP GLU ASP          
-SEQRES  28 D  381  LEU GLU LEU ALA LYS ARG GLU LYS VAL LEU VAL ASP ALA          
-SEQRES  29 D  381  GLY TYR MET ASP ALA LYS GLN GLN PRO LEU GLU HIS HIS          
-SEQRES  30 D  381  HIS HIS HIS HIS                                              
-HET    NDP  A 701      48                                                       
-HET    NDP  B 702      48                                                       
-HET    NDP  C 703      48                                                       
-HET    NDP  D 704      48                                                       
-HET    GDR  A 801      38                                                       
-HET    GDR  A 802      38                                                       
-HET    GDR  A 803      38                                                       
-HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
-HETNAM   2 NDP  PHOSPHATE                                                       
-HETNAM     GDR GUANOSINE-5'-DIPHOSPHATE-RHAMNOSE                                
-FORMUL   5  NDP    4(C21 H30 N7 O17 P3)                                         
-FORMUL   9  GDR    3(C16 H25 N5 O15 P2)                                         
-FORMUL  10  HOH   *475(H2 O)                                                    
-HELIX    1   1 GLY A   38  GLY A   50  1                                  13    
-HELIX    2   2 ASP A   94  LYS A  106  1                                  13    
-HELIX    3   3 HIS A  118  ILE A  125  1                                   8    
-HELIX    4   4 ILE A  125  ALA A  134  1                                  10    
-HELIX    5   5 ALA A  134  GLY A  152  1                                  19    
-HELIX    6   6 GLU A  164  GLY A  167  5                                   4    
-HELIX    7   7 SER A  183  GLY A  204  1                                  22    
-HELIX    8   8 PHE A  224  VAL A  238  1                                  15    
-HELIX    9   9 ALA A  258  LEU A  269  1                                  12    
-HELIX   10  10 VAL A  287  LEU A  298  1                                  12    
-HELIX   11  11 ASN A  301  ASP A  304  5                                   4    
-HELIX   12  12 GLN A  310  PHE A  313  5                                   4    
-HELIX   13  13 ALA A  325  GLY A  333  1                                   9    
-HELIX   14  14 GLY A  339  ASP A  363  1                                  25    
-HELIX   15  15 GLY B   38  GLY B   50  1                                  13    
-HELIX   16  16 ILE B   70  ILE B   75  1                                   6    
-HELIX   17  17 ASP B   94  LYS B  106  1                                  13    
-HELIX   18  18 HIS B  118  ILE B  125  1                                   8    
-HELIX   19  19 ILE B  125  ALA B  134  1                                  10    
-HELIX   20  20 ALA B  134  GLY B  152  1                                  19    
-HELIX   21  21 GLU B  164  GLY B  167  5                                   4    
-HELIX   22  22 SER B  183  GLY B  204  1                                  22    
-HELIX   23  23 PHE B  224  VAL B  238  1                                  15    
-HELIX   24  24 ALA B  258  GLN B  271  1                                  14    
-HELIX   25  25 VAL B  287  LEU B  298  1                                  12    
-HELIX   26  26 ASN B  301  ASP B  304  5                                   4    
-HELIX   27  27 GLN B  310  PHE B  313  5                                   4    
-HELIX   28  28 ALA B  325  GLY B  333  1                                   9    
-HELIX   29  29 GLY B  339  ALA B  364  1                                  26    
-HELIX   30  30 GLY C   38  GLY C   50  1                                  13    
-HELIX   31  31 ILE C   70  ILE C   75  5                                   6    
-HELIX   32  32 ASP C   94  LYS C  106  1                                  13    
-HELIX   33  33 HIS C  118  ILE C  125  1                                   8    
-HELIX   34  34 ILE C  125  ALA C  134  1                                  10    
-HELIX   35  35 ALA C  134  GLY C  152  1                                  19    
-HELIX   36  36 GLU C  164  PHE C  166  5                                   3    
-HELIX   37  37 SER C  183  GLY C  204  1                                  22    
-HELIX   38  38 PHE C  224  VAL C  238  1                                  15    
-HELIX   39  39 ALA C  258  GLN C  271  1                                  14    
-HELIX   40  40 VAL C  287  LEU C  298  1                                  12    
-HELIX   41  41 ASN C  301  ASP C  304  5                                   4    
-HELIX   42  42 GLN C  310  PHE C  313  5                                   4    
-HELIX   43  43 ALA C  325  GLY C  333  1                                   9    
-HELIX   44  44 GLY C  339  ALA C  364  1                                  26    
-HELIX   45  45 GLY D   38  LYS D   51  1                                  14    
-HELIX   46  46 ILE D   70  ILE D   75  1                                   6    
-HELIX   47  47 ASP D   94  LYS D  106  1                                  13    
-HELIX   48  48 HIS D  118  ILE D  125  1                                   8    
-HELIX   49  49 ILE D  125  ALA D  134  1                                  10    
-HELIX   50  50 ALA D  134  GLY D  152  1                                  19    
-HELIX   51  51 GLU D  164  PHE D  166  5                                   3    
-HELIX   52  52 SER D  183  GLY D  204  1                                  22    
-HELIX   53  53 PHE D  224  VAL D  238  1                                  15    
-HELIX   54  54 ALA D  258  LEU D  269  1                                  12    
-HELIX   55  55 THR D  286  LEU D  298  1                                  13    
-HELIX   56  56 ASN D  301  TYR D  305  5                                   5    
-HELIX   57  57 ALA D  325  LEU D  332  1                                   8    
-HELIX   58  58 GLY D  339  VAL D  362  1                                  24    
-SHEET    1   A 7 MET A  85  TYR A  89  0                                        
-SHEET    2   A 7 GLU A  54  ILE A  59  1  N  ILE A  59   O  HIS A  88           
-SHEET    3   A 7 ILE A  30  THR A  34  1  N  ALA A  31   O  HIS A  56           
-SHEET    4   A 7 GLU A 109  ASN A 112  1  O  TYR A 111   N  LEU A  32           
-SHEET    5   A 7 LYS A 156  SER A 162  1  O  LYS A 156   N  VAL A 110           
-SHEET    6   A 7 PHE A 206  LEU A 212  1  O  PHE A 206   N  TYR A 157           
-SHEET    7   A 7 ASP A 276  VAL A 279  1  O  TYR A 277   N  ILE A 211           
-SHEET    1   B 2 HIS A 215  GLU A 216  0                                        
-SHEET    2   B 2 GLY A 256  PHE A 257  1  O  GLY A 256   N  GLU A 216           
-SHEET    1   C 2 LEU A 244  LEU A 246  0                                        
-SHEET    2   C 2 VAL A 306  ILE A 308  1  O  GLU A 307   N  LEU A 244           
-SHEET    1   D 2 SER A 252  ARG A 253  0                                        
-SHEET    2   D 2 HIS A 285  THR A 286 -1  O  HIS A 285   N  ARG A 253           
-SHEET    1   E 7 MET B  85  TYR B  89  0                                        
-SHEET    2   E 7 GLU B  54  ILE B  59  1  N  ILE B  59   O  HIS B  88           
-SHEET    3   E 7 ILE B  30  THR B  34  1  N  ALA B  31   O  HIS B  56           
-SHEET    4   E 7 GLU B 109  ASN B 112  1  O  GLU B 109   N  LEU B  32           
-SHEET    5   E 7 LYS B 156  SER B 162  1  O  LYS B 156   N  VAL B 110           
-SHEET    6   E 7 PHE B 206  LEU B 212  1  O  PHE B 206   N  TYR B 157           
-SHEET    7   E 7 ASP B 276  VAL B 279  1  O  TYR B 277   N  ILE B 211           
-SHEET    1   F 2 HIS B 215  GLU B 216  0                                        
-SHEET    2   F 2 GLY B 256  PHE B 257  1  O  GLY B 256   N  GLU B 216           
-SHEET    1   G 2 LEU B 244  LEU B 246  0                                        
-SHEET    2   G 2 VAL B 306  ILE B 308  1  O  GLU B 307   N  LEU B 246           
-SHEET    1   H 2 SER B 252  ARG B 253  0                                        
-SHEET    2   H 2 HIS B 285  THR B 286 -1  O  HIS B 285   N  ARG B 253           
-SHEET    1   I 7 MET C  85  TYR C  89  0                                        
-SHEET    2   I 7 GLU C  54  ILE C  59  1  N  ILE C  59   O  HIS C  88           
-SHEET    3   I 7 ILE C  30  THR C  34  1  N  ILE C  33   O  HIS C  56           
-SHEET    4   I 7 GLU C 109  ASN C 112  1  O  GLU C 109   N  LEU C  32           
-SHEET    5   I 7 LYS C 156  SER C 162  1  O  TYR C 158   N  VAL C 110           
-SHEET    6   I 7 PHE C 206  LEU C 212  1  O  PHE C 206   N  TYR C 157           
-SHEET    7   I 7 ASP C 276  VAL C 279  1  O  TYR C 277   N  ILE C 211           
-SHEET    1   J 2 HIS C 215  GLU C 216  0                                        
-SHEET    2   J 2 GLY C 256  PHE C 257  1  O  GLY C 256   N  GLU C 216           
-SHEET    1   K 2 LEU C 244  LEU C 246  0                                        
-SHEET    2   K 2 VAL C 306  ILE C 308  1  O  GLU C 307   N  LEU C 246           
-SHEET    1   L 2 SER C 252  ARG C 253  0                                        
-SHEET    2   L 2 HIS C 285  THR C 286 -1  O  HIS C 285   N  ARG C 253           
-SHEET    1   M 7 MET D  85  TYR D  89  0                                        
-SHEET    2   M 7 GLU D  54  ILE D  59  1  N  ILE D  59   O  HIS D  88           
-SHEET    3   M 7 ILE D  30  THR D  34  1  N  ALA D  31   O  HIS D  56           
-SHEET    4   M 7 GLU D 109  ASN D 112  1  O  TYR D 111   N  LEU D  32           
-SHEET    5   M 7 LYS D 156  SER D 162  1  O  LYS D 156   N  VAL D 110           
-SHEET    6   M 7 PHE D 206  LEU D 212  1  O  PHE D 206   N  TYR D 157           
-SHEET    7   M 7 ASP D 276  VAL D 279  1  O  TYR D 277   N  ILE D 211           
-SHEET    1   N 2 HIS D 215  GLU D 216  0                                        
-SHEET    2   N 2 GLY D 256  PHE D 257  1  O  GLY D 256   N  GLU D 216           
-CISPEP   1 PRO A  171    PRO A  172          0         0.00                     
-CISPEP   2 PRO B  171    PRO B  172          0        -0.32                     
-CISPEP   3 PRO C  171    PRO C  172          0        -0.17                     
-CISPEP   4 PRO D  171    PRO D  172          0        -0.14                     
-SITE     1 AC1 39 GLY A  35  THR A  37  GLY A  38  GLN A  39                    
-SITE     2 AC1 39 ASP A  40  ARG A  60  ASP A  91  LEU A  92                    
-SITE     3 AC1 39 LEU A 113  ALA A 114  ALA A 115  SER A 117                    
-SITE     4 AC1 39 TYR A 128  VAL A 132  ALA A 160  GLY A 161                    
-SITE     5 AC1 39 SER A 162  TYR A 185  LYS A 189  LEU A 212                    
-SITE     6 AC1 39 ASN A 214  HIS A 215  ARG A 220  GDR A 801                    
-SITE     7 AC1 39 HOH A 806  HOH A 807  HOH A 810  HOH A 820                    
-SITE     8 AC1 39 HOH A 825  HOH A 837  HOH A 838  HOH A 839                    
-SITE     9 AC1 39 HOH A 847  HOH A 851  HOH A 929  HOH A 931                    
-SITE    10 AC1 39 ARG C  61  SER C  62  SER C  63                               
-SITE     1 AC2 38 GDR A 802  HOH A 862  GLY B  35  THR B  37                    
-SITE     2 AC2 38 GLY B  38  GLN B  39  ASP B  40  ARG B  60                    
-SITE     3 AC2 38 ASP B  91  LEU B  92  LEU B 113  ALA B 114                    
-SITE     4 AC2 38 ALA B 115  SER B 117  TYR B 128  VAL B 132                    
-SITE     5 AC2 38 ALA B 160  GLY B 161  SER B 162  TYR B 185                    
-SITE     6 AC2 38 LYS B 189  LEU B 212  ASN B 214  HIS B 215                    
-SITE     7 AC2 38 ARG B 220  HOH B 705  HOH B 706  HOH B 719                    
-SITE     8 AC2 38 HOH B 721  HOH B 725  HOH B 728  HOH B 733                    
-SITE     9 AC2 38 HOH B 743  HOH B 760  HOH B 778  ARG D  61                    
-SITE    10 AC2 38 SER D  62  SER D  63                                          
-SITE     1 AC3 38 ARG A  61  SER A  62  SER A  63  GDR A 803                    
-SITE     2 AC3 38 HOH A 854  GLY C  35  THR C  37  GLY C  38                    
-SITE     3 AC3 38 GLN C  39  ASP C  40  ARG C  60  ASP C  91                    
-SITE     4 AC3 38 LEU C  92  LEU C 113  ALA C 114  ALA C 115                    
-SITE     5 AC3 38 SER C 117  TYR C 128  VAL C 132  ALA C 160                    
-SITE     6 AC3 38 GLY C 161  SER C 162  TYR C 185  LYS C 189                    
-SITE     7 AC3 38 LEU C 212  ASN C 214  HIS C 215  ARG C 220                    
-SITE     8 AC3 38 HOH C 704  HOH C 719  HOH C 723  HOH C 724                    
-SITE     9 AC3 38 HOH C 726  HOH C 731  HOH C 737  HOH C 747                    
-SITE    10 AC3 38 HOH C 748  HOH C 749                                          
-SITE     1 AC4 38 ARG B  61  SER B  62  SER B  63  GLY D  35                    
-SITE     2 AC4 38 THR D  37  GLY D  38  GLN D  39  ASP D  40                    
-SITE     3 AC4 38 ARG D  60  ASP D  91  LEU D  92  LEU D 113                    
-SITE     4 AC4 38 ALA D 114  ALA D 115  SER D 117  TYR D 128                    
-SITE     5 AC4 38 VAL D 132  ALA D 160  GLY D 161  SER D 162                    
-SITE     6 AC4 38 TYR D 185  LYS D 189  LEU D 212  ASN D 214                    
-SITE     7 AC4 38 HIS D 215  ARG D 220  HOH D 708  HOH D 709                    
-SITE     8 AC4 38 HOH D 712  HOH D 719  HOH D 720  HOH D 721                    
-SITE     9 AC4 38 HOH D 731  HOH D 769  HOH D 779  HOH D 780                    
-SITE    10 AC4 38 HOH D 795  HOH D 800                                          
-SITE     1 AC5 29 SER A 117  HIS A 118  VAL A 119  SER A 162                    
-SITE     2 AC5 29 SER A 163  GLU A 164  TYR A 185  ASN A 214                    
-SITE     3 AC5 29 ARG A 220  ASN A 223  PHE A 224  VAL A 225                    
-SITE     4 AC5 29 LYS A 228  GLY A 247  ASN A 248  ALA A 251                    
-SITE     5 AC5 29 ARG A 253  VAL A 287  TYR A 312  ARG A 314                    
-SITE     6 AC5 29 GLU A 317  NDP A 701  HOH A 822  HOH A 823                    
-SITE     7 AC5 29 HOH A 828  HOH A 832  HOH A 867  HOH A 922                    
-SITE     8 AC5 29 HOH A 931                                                     
-SITE     1 AC6 29 HOH A 858  HOH A 862  SER B 117  HIS B 118                    
-SITE     2 AC6 29 VAL B 119  SER B 162  SER B 163  GLU B 164                    
-SITE     3 AC6 29 TYR B 185  ASN B 214  ARG B 220  ASN B 223                    
-SITE     4 AC6 29 PHE B 224  VAL B 225  LYS B 228  LEU B 246                    
-SITE     5 AC6 29 GLY B 247  ASN B 248  ALA B 251  ARG B 253                    
-SITE     6 AC6 29 VAL B 287  TYR B 312  ARG B 314  GLU B 317                    
-SITE     7 AC6 29 NDP B 702  HOH B 737  HOH B 748  HOH B 751                    
-SITE     8 AC6 29 HOH B 752                                                     
-SITE     1 AC7 30 HOH A 854  HOH A 880  HOH A 916  SER C 117                    
-SITE     2 AC7 30 HIS C 118  VAL C 119  SER C 162  SER C 163                    
-SITE     3 AC7 30 GLU C 164  TYR C 185  ASN C 214  ARG C 220                    
-SITE     4 AC7 30 ASN C 223  PHE C 224  VAL C 225  LYS C 228                    
-SITE     5 AC7 30 LEU C 246  GLY C 247  ASN C 248  ALA C 251                    
-SITE     6 AC7 30 ARG C 253  VAL C 287  TYR C 312  ARG C 314                    
-SITE     7 AC7 30 GLU C 317  NDP C 703  HOH C 722  HOH C 735                    
-SITE     8 AC7 30 HOH C 786  HOH C 830                                          
-CRYST1  113.180  119.010  118.890  90.00  90.00  90.00 P 21 21 21   16          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.008835  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.008403  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.008411        0.00000                         
-ATOM      1  N   ARG A  28       9.966  19.044   4.569  1.00 39.96           N  
-ATOM      2  CA  ARG A  28       9.626  18.582   5.951  1.00 42.24           C  
-ATOM      3  C   ARG A  28      10.080  19.617   6.990  1.00 41.09           C  
-ATOM      4  O   ARG A  28      11.273  19.882   7.129  1.00 40.48           O  
-ATOM      5  CB  ARG A  28      10.308  17.240   6.234  1.00 43.57           C  
-ATOM      6  CG  ARG A  28      10.059  16.699   7.631  1.00 45.39           C  
-ATOM      7  CD  ARG A  28       8.742  15.952   7.727  1.00 46.67           C  
-ATOM      8  NE  ARG A  28       8.849  14.567   7.270  1.00 46.77           N  
-ATOM      9  CZ  ARG A  28       7.833  13.707   7.252  1.00 47.65           C  
-ATOM     10  NH1 ARG A  28       6.630  14.087   7.663  1.00 48.87           N  
-ATOM     11  NH2 ARG A  28       8.016  12.465   6.830  1.00 48.32           N  
-ATOM     12  N   LYS A  29       9.129  20.201   7.715  1.00 39.58           N  
-ATOM     13  CA  LYS A  29       9.462  21.197   8.727  1.00 38.35           C  
-ATOM     14  C   LYS A  29      10.182  20.563   9.905  1.00 36.12           C  
-ATOM     15  O   LYS A  29       9.879  19.440  10.299  1.00 35.79           O  
-ATOM     16  CB  LYS A  29       8.202  21.913   9.218  1.00 40.04           C  
-ATOM     17  CG  LYS A  29       7.994  23.286   8.593  1.00 42.91           C  
-ATOM     18  CD  LYS A  29       6.766  23.976   9.166  1.00 45.06           C  
-ATOM     19  CE  LYS A  29       6.691  25.435   8.733  1.00 46.18           C  
-ATOM     20  NZ  LYS A  29       5.504  26.131   9.322  1.00 48.82           N  
-ATOM     21  N   ILE A  30      11.144  21.288  10.458  1.00 34.61           N  
-ATOM     22  CA  ILE A  30      11.914  20.785  11.587  1.00 33.44           C  
-ATOM     23  C   ILE A  30      11.745  21.649  12.834  1.00 31.20           C  
-ATOM     24  O   ILE A  30      11.927  22.868  12.802  1.00 30.16           O  
-ATOM     25  CB  ILE A  30      13.414  20.703  11.237  1.00 34.26           C  
-ATOM     26  CG1 ILE A  30      13.613  19.818   9.997  1.00 34.64           C  
-ATOM     27  CG2 ILE A  30      14.188  20.138  12.414  1.00 33.06           C  
-ATOM     28  CD1 ILE A  30      15.037  19.801   9.476  1.00 33.50           C  
-ATOM     29  N   ALA A  31      11.391  21.004  13.934  1.00 29.10           N  
-ATOM     30  CA  ALA A  31      11.211  21.713  15.187  1.00 28.77           C  
-ATOM     31  C   ALA A  31      12.199  21.219  16.244  1.00 27.83           C  
-ATOM     32  O   ALA A  31      12.473  20.023  16.348  1.00 27.13           O  
-ATOM     33  CB  ALA A  31       9.784  21.536  15.684  1.00 27.88           C  
-ATOM     34  N   LEU A  32      12.755  22.157  17.000  1.00 27.25           N  
-ATOM     35  CA  LEU A  32      13.675  21.832  18.084  1.00 27.01           C  
-ATOM     36  C   LEU A  32      12.948  22.264  19.344  1.00 25.31           C  
-ATOM     37  O   LEU A  32      12.575  23.424  19.484  1.00 24.59           O  
-ATOM     38  CB  LEU A  32      14.987  22.609  17.961  1.00 26.79           C  
-ATOM     39  CG  LEU A  32      15.971  22.374  19.121  1.00 28.33           C  
-ATOM     40  CD1 LEU A  32      16.290  20.890  19.234  1.00 27.08           C  
-ATOM     41  CD2 LEU A  32      17.248  23.168  18.896  1.00 27.00           C  
-ATOM     42  N   ILE A  33      12.729  21.324  20.250  1.00 26.27           N  
-ATOM     43  CA  ILE A  33      12.032  21.619  21.493  1.00 25.81           C  
-ATOM     44  C   ILE A  33      12.922  21.395  22.714  1.00 26.98           C  
-ATOM     45  O   ILE A  33      13.461  20.306  22.892  1.00 26.90           O  
-ATOM     46  CB  ILE A  33      10.800  20.704  21.674  1.00 25.90           C  
-ATOM     47  CG1 ILE A  33       9.838  20.848  20.493  1.00 26.31           C  
-ATOM     48  CG2 ILE A  33      10.087  21.044  22.986  1.00 24.77           C  
-ATOM     49  CD1 ILE A  33       8.666  19.863  20.538  1.00 21.73           C  
-ATOM     50  N   THR A  34      13.089  22.423  23.542  1.00 27.81           N  
-ATOM     51  CA  THR A  34      13.853  22.260  24.776  1.00 27.87           C  
-ATOM     52  C   THR A  34      12.751  21.928  25.777  1.00 27.96           C  
-ATOM     53  O   THR A  34      11.634  22.428  25.647  1.00 27.63           O  
-ATOM     54  CB  THR A  34      14.564  23.565  25.231  1.00 27.10           C  
-ATOM     55  OG1 THR A  34      13.583  24.557  25.550  1.00 27.04           O  
-ATOM     56  CG2 THR A  34      15.497  24.088  24.136  1.00 24.95           C  
-ATOM     57  N   GLY A  35      13.044  21.080  26.757  1.00 27.63           N  
-ATOM     58  CA  GLY A  35      12.031  20.722  27.732  1.00 25.55           C  
-ATOM     59  C   GLY A  35      10.987  19.790  27.147  1.00 26.21           C  
-ATOM     60  O   GLY A  35       9.816  19.816  27.528  1.00 25.02           O  
-ATOM     61  N   ILE A  36      11.420  18.947  26.218  1.00 26.89           N  
-ATOM     62  CA  ILE A  36      10.523  18.008  25.565  1.00 25.24           C  
-ATOM     63  C   ILE A  36       9.993  16.930  26.514  1.00 25.09           C  
-ATOM     64  O   ILE A  36       8.911  16.395  26.294  1.00 25.79           O  
-ATOM     65  CB  ILE A  36      11.225  17.339  24.343  1.00 23.99           C  
-ATOM     66  CG1 ILE A  36      10.190  16.615  23.475  1.00 24.73           C  
-ATOM     67  CG2 ILE A  36      12.308  16.381  24.818  1.00 24.03           C  
-ATOM     68  CD1 ILE A  36      10.731  16.139  22.110  1.00 21.52           C  
-ATOM     69  N   THR A  37      10.738  16.616  27.573  1.00 25.53           N  
-ATOM     70  CA  THR A  37      10.289  15.587  28.515  1.00 23.72           C  
-ATOM     71  C   THR A  37       9.227  16.080  29.499  1.00 23.92           C  
-ATOM     72  O   THR A  37       8.646  15.287  30.245  1.00 23.03           O  
-ATOM     73  CB  THR A  37      11.455  15.005  29.343  1.00 22.56           C  
-ATOM     74  OG1 THR A  37      12.101  16.060  30.067  1.00 22.16           O  
-ATOM     75  CG2 THR A  37      12.452  14.298  28.445  1.00 21.84           C  
-ATOM     76  N   GLY A  38       8.974  17.382  29.500  1.00 21.88           N  
-ATOM     77  CA  GLY A  38       7.979  17.931  30.404  1.00 23.72           C  
-ATOM     78  C   GLY A  38       6.564  17.772  29.878  1.00 24.40           C  
-ATOM     79  O   GLY A  38       6.360  17.230  28.792  1.00 23.32           O  
-ATOM     80  N   GLN A  39       5.584  18.239  30.646  1.00 24.04           N  
-ATOM     81  CA  GLN A  39       4.188  18.141  30.235  1.00 26.24           C  
-ATOM     82  C   GLN A  39       3.930  18.761  28.864  1.00 27.37           C  
-ATOM     83  O   GLN A  39       3.474  18.081  27.950  1.00 28.57           O  
-ATOM     84  CB  GLN A  39       3.275  18.817  31.259  1.00 24.65           C  
-ATOM     85  CG  GLN A  39       1.838  18.990  30.771  1.00 25.05           C  
-ATOM     86  CD  GLN A  39       0.996  19.861  31.691  1.00 28.61           C  
-ATOM     87  OE1 GLN A  39       0.105  19.374  32.388  1.00 27.14           O  
-ATOM     88  NE2 GLN A  39       1.281  21.160  31.699  1.00 29.18           N  
-ATOM     89  N   ASP A  40       4.215  20.053  28.729  1.00 25.58           N  
-ATOM     90  CA  ASP A  40       3.983  20.754  27.476  1.00 26.15           C  
-ATOM     91  C   ASP A  40       4.770  20.151  26.323  1.00 26.90           C  
-ATOM     92  O   ASP A  40       4.247  20.001  25.221  1.00 26.22           O  
-ATOM     93  CB  ASP A  40       4.341  22.233  27.626  1.00 27.10           C  
-ATOM     94  CG  ASP A  40       3.422  22.962  28.594  1.00 27.94           C  
-ATOM     95  OD1 ASP A  40       2.692  22.287  29.350  1.00 30.33           O  
-ATOM     96  OD2 ASP A  40       3.436  24.212  28.605  1.00 26.71           O  
-ATOM     97  N   GLY A  41       6.029  19.811  26.584  1.00 27.25           N  
-ATOM     98  CA  GLY A  41       6.864  19.231  25.551  1.00 27.22           C  
-ATOM     99  C   GLY A  41       6.278  17.970  24.943  1.00 27.74           C  
-ATOM    100  O   GLY A  41       6.365  17.767  23.730  1.00 28.13           O  
-ATOM    101  N   SER A  42       5.676  17.128  25.781  1.00 27.49           N  
-ATOM    102  CA  SER A  42       5.089  15.875  25.320  1.00 27.38           C  
-ATOM    103  C   SER A  42       3.862  16.101  24.441  1.00 28.70           C  
-ATOM    104  O   SER A  42       3.635  15.348  23.498  1.00 29.18           O  
-ATOM    105  CB  SER A  42       4.735  14.974  26.512  1.00 26.12           C  
-ATOM    106  OG  SER A  42       3.740  15.553  27.336  1.00 26.24           O  
-ATOM    107  N   TYR A  43       3.078  17.133  24.745  1.00 28.01           N  
-ATOM    108  CA  TYR A  43       1.898  17.448  23.946  1.00 28.25           C  
-ATOM    109  C   TYR A  43       2.292  18.157  22.653  1.00 29.15           C  
-ATOM    110  O   TYR A  43       1.737  17.877  21.592  1.00 30.82           O  
-ATOM    111  CB  TYR A  43       0.915  18.324  24.734  1.00 25.87           C  
-ATOM    112  CG  TYR A  43       0.081  17.551  25.734  1.00 25.53           C  
-ATOM    113  CD1 TYR A  43       0.316  17.654  27.109  1.00 25.15           C  
-ATOM    114  CD2 TYR A  43      -0.933  16.694  25.301  1.00 23.67           C  
-ATOM    115  CE1 TYR A  43      -0.444  16.917  28.029  1.00 24.79           C  
-ATOM    116  CE2 TYR A  43      -1.692  15.956  26.206  1.00 25.88           C  
-ATOM    117  CZ  TYR A  43      -1.443  16.072  27.568  1.00 26.90           C  
-ATOM    118  OH  TYR A  43      -2.187  15.330  28.454  1.00 26.41           O  
-ATOM    119  N   LEU A  44       3.249  19.075  22.746  1.00 28.27           N  
-ATOM    120  CA  LEU A  44       3.712  19.810  21.575  1.00 28.92           C  
-ATOM    121  C   LEU A  44       4.345  18.848  20.578  1.00 29.57           C  
-ATOM    122  O   LEU A  44       4.207  19.018  19.365  1.00 29.14           O  
-ATOM    123  CB  LEU A  44       4.734  20.876  21.975  1.00 26.18           C  
-ATOM    124  CG  LEU A  44       5.235  21.779  20.846  1.00 27.35           C  
-ATOM    125  CD1 LEU A  44       4.069  22.549  20.249  1.00 28.65           C  
-ATOM    126  CD2 LEU A  44       6.283  22.737  21.373  1.00 26.27           C  
-ATOM    127  N   THR A  45       5.042  17.840  21.094  1.00 29.98           N  
-ATOM    128  CA  THR A  45       5.681  16.849  20.236  1.00 30.05           C  
-ATOM    129  C   THR A  45       4.606  16.114  19.435  1.00 30.52           C  
-ATOM    130  O   THR A  45       4.691  16.009  18.214  1.00 28.74           O  
-ATOM    131  CB  THR A  45       6.483  15.828  21.064  1.00 30.35           C  
-ATOM    132  OG1 THR A  45       7.532  16.511  21.765  1.00 28.56           O  
-ATOM    133  CG2 THR A  45       7.085  14.747  20.155  1.00 27.90           C  
-ATOM    134  N   GLU A  46       3.590  15.614  20.126  1.00 30.33           N  
-ATOM    135  CA  GLU A  46       2.511  14.907  19.455  1.00 31.50           C  
-ATOM    136  C   GLU A  46       1.831  15.819  18.437  1.00 31.94           C  
-ATOM    137  O   GLU A  46       1.576  15.412  17.311  1.00 34.41           O  
-ATOM    138  CB  GLU A  46       1.490  14.401  20.483  1.00 31.63           C  
-ATOM    139  CG  GLU A  46       2.100  13.448  21.508  1.00 32.41           C  
-ATOM    140  CD  GLU A  46       1.080  12.853  22.459  1.00 35.30           C  
-ATOM    141  OE1 GLU A  46       0.387  13.615  23.164  1.00 37.07           O  
-ATOM    142  OE2 GLU A  46       0.977  11.610  22.506  1.00 37.48           O  
-ATOM    143  N   PHE A  47       1.552  17.057  18.832  1.00 32.03           N  
-ATOM    144  CA  PHE A  47       0.896  18.019  17.951  1.00 30.65           C  
-ATOM    145  C   PHE A  47       1.670  18.267  16.652  1.00 31.08           C  
-ATOM    146  O   PHE A  47       1.085  18.288  15.567  1.00 31.19           O  
-ATOM    147  CB  PHE A  47       0.701  19.352  18.676  1.00 27.84           C  
-ATOM    148  CG  PHE A  47      -0.108  20.354  17.897  1.00 28.25           C  
-ATOM    149  CD1 PHE A  47      -1.484  20.203  17.761  1.00 28.51           C  
-ATOM    150  CD2 PHE A  47       0.507  21.437  17.281  1.00 27.72           C  
-ATOM    151  CE1 PHE A  47      -2.235  21.115  17.022  1.00 29.33           C  
-ATOM    152  CE2 PHE A  47      -0.235  22.356  16.538  1.00 28.17           C  
-ATOM    153  CZ  PHE A  47      -1.609  22.194  16.408  1.00 28.19           C  
-ATOM    154  N   LEU A  48       2.979  18.463  16.772  1.00 29.11           N  
-ATOM    155  CA  LEU A  48       3.829  18.724  15.622  1.00 29.26           C  
-ATOM    156  C   LEU A  48       4.060  17.480  14.772  1.00 30.05           C  
-ATOM    157  O   LEU A  48       4.131  17.567  13.546  1.00 29.68           O  
-ATOM    158  CB  LEU A  48       5.165  19.320  16.085  1.00 30.35           C  
-ATOM    159  CG  LEU A  48       5.061  20.659  16.831  1.00 30.70           C  
-ATOM    160  CD1 LEU A  48       6.442  21.121  17.270  1.00 28.79           C  
-ATOM    161  CD2 LEU A  48       4.409  21.705  15.928  1.00 31.11           C  
-ATOM    162  N   LEU A  49       4.189  16.323  15.413  1.00 31.00           N  
-ATOM    163  CA  LEU A  49       4.373  15.090  14.663  1.00 33.46           C  
-ATOM    164  C   LEU A  49       3.125  14.893  13.817  1.00 35.85           C  
-ATOM    165  O   LEU A  49       3.210  14.495  12.657  1.00 36.75           O  
-ATOM    166  CB  LEU A  49       4.552  13.891  15.597  1.00 31.38           C  
-ATOM    167  CG  LEU A  49       5.917  13.745  16.271  1.00 33.41           C  
-ATOM    168  CD1 LEU A  49       5.899  12.559  17.218  1.00 32.44           C  
-ATOM    169  CD2 LEU A  49       6.992  13.568  15.217  1.00 31.60           C  
-ATOM    170  N   GLY A  50       1.968  15.188  14.406  1.00 36.93           N  
-ATOM    171  CA  GLY A  50       0.711  15.042  13.693  1.00 37.01           C  
-ATOM    172  C   GLY A  50       0.623  16.015  12.533  1.00 38.24           C  
-ATOM    173  O   GLY A  50      -0.195  15.847  11.625  1.00 36.56           O  
-ATOM    174  N   LYS A  51       1.474  17.037  12.570  1.00 38.74           N  
-ATOM    175  CA  LYS A  51       1.517  18.058  11.528  1.00 37.82           C  
-ATOM    176  C   LYS A  51       2.568  17.729  10.475  1.00 37.64           C  
-ATOM    177  O   LYS A  51       2.861  18.548   9.609  1.00 37.75           O  
-ATOM    178  CB  LYS A  51       1.838  19.420  12.144  1.00 38.92           C  
-ATOM    179  CG  LYS A  51       0.730  20.023  12.986  1.00 38.87           C  
-ATOM    180  CD  LYS A  51      -0.334  20.646  12.114  1.00 40.69           C  
-ATOM    181  CE  LYS A  51      -1.363  21.384  12.947  1.00 41.71           C  
-ATOM    182  NZ  LYS A  51      -2.347  22.097  12.084  1.00 43.92           N  
-ATOM    183  N   GLY A  52       3.146  16.536  10.562  1.00 37.21           N  
-ATOM    184  CA  GLY A  52       4.159  16.137   9.603  1.00 36.10           C  
-ATOM    185  C   GLY A  52       5.542  16.709   9.865  1.00 36.35           C  
-ATOM    186  O   GLY A  52       6.371  16.783   8.960  1.00 37.07           O  
-ATOM    187  N   TYR A  53       5.801  17.117  11.102  1.00 35.91           N  
-ATOM    188  CA  TYR A  53       7.106  17.671  11.459  1.00 33.80           C  
-ATOM    189  C   TYR A  53       8.122  16.594  11.815  1.00 32.82           C  
-ATOM    190  O   TYR A  53       7.777  15.454  12.133  1.00 32.98           O  
-ATOM    191  CB  TYR A  53       7.004  18.583  12.684  1.00 32.08           C  
-ATOM    192  CG  TYR A  53       6.614  20.019  12.444  1.00 31.87           C  
-ATOM    193  CD1 TYR A  53       5.337  20.360  12.005  1.00 31.70           C  
-ATOM    194  CD2 TYR A  53       7.502  21.048  12.745  1.00 31.66           C  
-ATOM    195  CE1 TYR A  53       4.950  21.696  11.884  1.00 30.73           C  
-ATOM    196  CE2 TYR A  53       7.128  22.381  12.625  1.00 31.69           C  
-ATOM    197  CZ  TYR A  53       5.853  22.698  12.199  1.00 31.35           C  
-ATOM    198  OH  TYR A  53       5.481  24.021  12.112  1.00 33.68           O  
-ATOM    199  N   GLU A  54       9.386  16.984  11.753  1.00 32.73           N  
-ATOM    200  CA  GLU A  54      10.493  16.133  12.152  1.00 32.96           C  
-ATOM    201  C   GLU A  54      10.784  16.834  13.471  1.00 31.36           C  
-ATOM    202  O   GLU A  54      11.117  18.019  13.485  1.00 30.48           O  
-ATOM    203  CB  GLU A  54      11.679  16.286  11.192  1.00 35.01           C  
-ATOM    204  CG  GLU A  54      12.984  15.679  11.697  1.00 38.19           C  
-ATOM    205  CD  GLU A  54      14.138  15.863  10.718  1.00 41.62           C  
-ATOM    206  OE1 GLU A  54      15.303  15.649  11.118  1.00 42.67           O  
-ATOM    207  OE2 GLU A  54      13.882  16.216   9.545  1.00 45.15           O  
-ATOM    208  N   VAL A  55      10.619  16.129  14.578  1.00 31.94           N  
-ATOM    209  CA  VAL A  55      10.832  16.747  15.876  1.00 29.46           C  
-ATOM    210  C   VAL A  55      12.076  16.281  16.600  1.00 29.05           C  
-ATOM    211  O   VAL A  55      12.337  15.081  16.728  1.00 26.30           O  
-ATOM    212  CB  VAL A  55       9.622  16.516  16.805  1.00 30.31           C  
-ATOM    213  CG1 VAL A  55       9.864  17.184  18.162  1.00 26.18           C  
-ATOM    214  CG2 VAL A  55       8.351  17.053  16.146  1.00 28.48           C  
-ATOM    215  N   HIS A  56      12.835  17.262  17.072  1.00 29.56           N  
-ATOM    216  CA  HIS A  56      14.054  17.027  17.826  1.00 29.84           C  
-ATOM    217  C   HIS A  56      13.832  17.631  19.204  1.00 29.63           C  
-ATOM    218  O   HIS A  56      13.241  18.702  19.330  1.00 31.95           O  
-ATOM    219  CB  HIS A  56      15.238  17.708  17.144  1.00 29.27           C  
-ATOM    220  CG  HIS A  56      15.656  17.048  15.869  1.00 31.01           C  
-ATOM    221  ND1 HIS A  56      16.509  15.967  15.836  1.00 30.86           N  
-ATOM    222  CD2 HIS A  56      15.319  17.301  14.581  1.00 33.41           C  
-ATOM    223  CE1 HIS A  56      16.683  15.585  14.583  1.00 35.10           C  
-ATOM    224  NE2 HIS A  56      15.972  16.377  13.802  1.00 33.39           N  
-ATOM    225  N   GLY A  57      14.283  16.931  20.237  1.00 29.31           N  
-ATOM    226  CA  GLY A  57      14.122  17.431  21.584  1.00 27.16           C  
-ATOM    227  C   GLY A  57      15.414  17.321  22.363  1.00 27.42           C  
-ATOM    228  O   GLY A  57      16.174  16.365  22.192  1.00 28.84           O  
-ATOM    229  N   LEU A  58      15.677  18.307  23.209  1.00 26.15           N  
-ATOM    230  CA  LEU A  58      16.879  18.285  24.027  1.00 25.84           C  
-ATOM    231  C   LEU A  58      16.482  17.720  25.385  1.00 25.15           C  
-ATOM    232  O   LEU A  58      15.487  18.148  25.976  1.00 24.47           O  
-ATOM    233  CB  LEU A  58      17.456  19.698  24.185  1.00 23.10           C  
-ATOM    234  CG  LEU A  58      17.764  20.447  22.881  1.00 24.90           C  
-ATOM    235  CD1 LEU A  58      18.451  21.769  23.169  1.00 25.75           C  
-ATOM    236  CD2 LEU A  58      18.648  19.584  22.015  1.00 25.45           C  
-ATOM    237  N   ILE A  59      17.240  16.741  25.866  1.00 24.85           N  
-ATOM    238  CA  ILE A  59      16.946  16.142  27.160  1.00 25.48           C  
-ATOM    239  C   ILE A  59      18.177  16.138  28.063  1.00 25.82           C  
-ATOM    240  O   ILE A  59      19.316  16.163  27.596  1.00 26.44           O  
-ATOM    241  CB  ILE A  59      16.440  14.682  27.018  1.00 25.90           C  
-ATOM    242  CG1 ILE A  59      17.578  13.769  26.551  1.00 30.03           C  
-ATOM    243  CG2 ILE A  59      15.296  14.615  26.021  1.00 26.15           C  
-ATOM    244  CD1 ILE A  59      17.191  12.289  26.490  1.00 27.53           C  
-ATOM    245  N   ARG A  60      17.937  16.112  29.365  1.00 26.32           N  
-ATOM    246  CA  ARG A  60      19.023  16.081  30.333  1.00 26.32           C  
-ATOM    247  C   ARG A  60      19.411  14.639  30.635  1.00 25.45           C  
-ATOM    248  O   ARG A  60      18.562  13.756  30.671  1.00 25.41           O  
-ATOM    249  CB  ARG A  60      18.598  16.749  31.646  1.00 24.92           C  
-ATOM    250  CG  ARG A  60      18.375  18.248  31.575  1.00 23.85           C  
-ATOM    251  CD  ARG A  60      18.406  18.846  32.977  1.00 25.10           C  
-ATOM    252  NE  ARG A  60      17.282  18.398  33.800  1.00 25.93           N  
-ATOM    253  CZ  ARG A  60      17.112  18.729  35.076  1.00 25.00           C  
-ATOM    254  NH1 ARG A  60      17.996  19.506  35.682  1.00 25.31           N  
-ATOM    255  NH2 ARG A  60      16.047  18.300  35.740  1.00 24.41           N  
-ATOM    256  N   ARG A  61      20.697  14.400  30.841  1.00 26.72           N  
-ATOM    257  CA  ARG A  61      21.148  13.067  31.199  1.00 26.96           C  
-ATOM    258  C   ARG A  61      20.715  12.901  32.657  1.00 28.39           C  
-ATOM    259  O   ARG A  61      20.809  13.843  33.446  1.00 26.82           O  
-ATOM    260  CB  ARG A  61      22.675  12.974  31.088  1.00 27.02           C  
-ATOM    261  CG  ARG A  61      23.252  11.605  31.426  1.00 27.30           C  
-ATOM    262  CD  ARG A  61      23.367  11.366  32.934  1.00 25.92           C  
-ATOM    263  NE  ARG A  61      23.532   9.945  33.219  1.00 28.10           N  
-ATOM    264  CZ  ARG A  61      23.887   9.436  34.395  1.00 30.27           C  
-ATOM    265  NH1 ARG A  61      24.130  10.232  35.434  1.00 31.18           N  
-ATOM    266  NH2 ARG A  61      23.991   8.120  34.533  1.00 30.37           N  
-ATOM    267  N   SER A  62      20.219  11.723  33.016  1.00 28.91           N  
-ATOM    268  CA  SER A  62      19.810  11.497  34.392  1.00 30.10           C  
-ATOM    269  C   SER A  62      20.160  10.076  34.792  1.00 29.44           C  
-ATOM    270  O   SER A  62      20.383   9.222  33.927  1.00 25.89           O  
-ATOM    271  CB  SER A  62      18.309  11.744  34.565  1.00 30.80           C  
-ATOM    272  OG  SER A  62      17.547  10.822  33.814  1.00 37.06           O  
-ATOM    273  N   SER A  63      20.214   9.829  36.100  1.00 27.62           N  
-ATOM    274  CA  SER A  63      20.555   8.506  36.604  1.00 28.60           C  
-ATOM    275  C   SER A  63      19.378   7.547  36.481  1.00 30.50           C  
-ATOM    276  O   SER A  63      19.527   6.341  36.670  1.00 32.11           O  
-ATOM    277  CB  SER A  63      21.007   8.591  38.065  1.00 27.80           C  
-ATOM    278  OG  SER A  63      19.915   8.864  38.930  1.00 24.68           O  
-ATOM    279  N   ASN A  64      18.205   8.090  36.168  1.00 32.55           N  
-ATOM    280  CA  ASN A  64      17.002   7.280  36.018  1.00 34.28           C  
-ATOM    281  C   ASN A  64      16.269   7.603  34.725  1.00 36.51           C  
-ATOM    282  O   ASN A  64      16.586   8.574  34.033  1.00 37.14           O  
-ATOM    283  CB  ASN A  64      16.043   7.508  37.192  1.00 34.15           C  
-ATOM    284  CG  ASN A  64      16.490   6.812  38.460  1.00 35.54           C  
-ATOM    285  OD1 ASN A  64      16.591   5.582  38.506  1.00 36.88           O  
-ATOM    286  ND2 ASN A  64      16.757   7.594  39.502  1.00 33.13           N  
-ATOM    287  N   PHE A  65      15.285   6.769  34.415  1.00 37.88           N  
-ATOM    288  CA  PHE A  65      14.443   6.923  33.236  1.00 38.54           C  
-ATOM    289  C   PHE A  65      13.788   8.302  33.374  1.00 38.52           C  
-ATOM    290  O   PHE A  65      13.157   8.588  34.390  1.00 38.64           O  
-ATOM    291  CB  PHE A  65      13.388   5.808  33.259  1.00 41.43           C  
-ATOM    292  CG  PHE A  65      12.516   5.740  32.032  1.00 44.68           C  
-ATOM    293  CD1 PHE A  65      13.072   5.573  30.766  1.00 45.42           C  
-ATOM    294  CD2 PHE A  65      11.129   5.797  32.153  1.00 45.34           C  
-ATOM    295  CE1 PHE A  65      12.257   5.461  29.639  1.00 44.71           C  
-ATOM    296  CE2 PHE A  65      10.305   5.685  31.032  1.00 44.99           C  
-ATOM    297  CZ  PHE A  65      10.872   5.517  29.774  1.00 45.41           C  
-ATOM    298  N   ASN A  66      13.943   9.163  32.372  1.00 37.51           N  
-ATOM    299  CA  ASN A  66      13.352  10.497  32.453  1.00 38.26           C  
-ATOM    300  C   ASN A  66      12.456  10.848  31.264  1.00 36.20           C  
-ATOM    301  O   ASN A  66      12.029  11.992  31.119  1.00 36.86           O  
-ATOM    302  CB  ASN A  66      14.456  11.550  32.593  1.00 40.46           C  
-ATOM    303  CG  ASN A  66      15.222  11.772  31.302  1.00 45.22           C  
-ATOM    304  OD1 ASN A  66      15.562  10.823  30.590  1.00 46.50           O  
-ATOM    305  ND2 ASN A  66      15.510  13.032  31.001  1.00 47.85           N  
-ATOM    306  N   THR A  67      12.156   9.860  30.429  1.00 34.01           N  
-ATOM    307  CA  THR A  67      11.318  10.089  29.261  1.00 33.22           C  
-ATOM    308  C   THR A  67       9.953   9.420  29.378  1.00 33.24           C  
-ATOM    309  O   THR A  67       9.358   9.030  28.381  1.00 33.85           O  
-ATOM    310  CB  THR A  67      12.016   9.578  27.996  1.00 31.80           C  
-ATOM    311  OG1 THR A  67      12.423   8.220  28.195  1.00 30.88           O  
-ATOM    312  CG2 THR A  67      13.239  10.430  27.687  1.00 29.24           C  
-ATOM    313  N   GLN A  68       9.453   9.305  30.602  1.00 33.12           N  
-ATOM    314  CA  GLN A  68       8.162   8.670  30.838  1.00 31.31           C  
-ATOM    315  C   GLN A  68       7.011   9.270  30.038  1.00 29.77           C  
-ATOM    316  O   GLN A  68       6.095   8.550  29.649  1.00 31.58           O  
-ATOM    317  CB  GLN A  68       7.808   8.702  32.333  1.00 31.73           C  
-ATOM    318  CG  GLN A  68       8.769   7.915  33.234  1.00 32.70           C  
-ATOM    319  CD  GLN A  68       9.977   8.730  33.674  1.00 34.04           C  
-ATOM    320  OE1 GLN A  68      10.549   9.482  32.888  1.00 34.05           O  
-ATOM    321  NE2 GLN A  68      10.376   8.572  34.935  1.00 32.65           N  
-ATOM    322  N   ARG A  69       7.052  10.576  29.784  1.00 28.42           N  
-ATOM    323  CA  ARG A  69       5.975  11.237  29.046  1.00 27.39           C  
-ATOM    324  C   ARG A  69       6.014  11.100  27.531  1.00 28.95           C  
-ATOM    325  O   ARG A  69       4.997  11.292  26.871  1.00 29.96           O  
-ATOM    326  CB  ARG A  69       5.933  12.729  29.363  1.00 25.78           C  
-ATOM    327  CG  ARG A  69       5.549  13.083  30.774  1.00 24.70           C  
-ATOM    328  CD  ARG A  69       5.210  14.559  30.848  1.00 25.65           C  
-ATOM    329  NE  ARG A  69       4.976  14.997  32.218  1.00 24.40           N  
-ATOM    330  CZ  ARG A  69       5.940  15.318  33.074  1.00 25.37           C  
-ATOM    331  NH1 ARG A  69       5.627  15.702  34.303  1.00 22.59           N  
-ATOM    332  NH2 ARG A  69       7.213  15.275  32.700  1.00 24.83           N  
-ATOM    333  N   ILE A  70       7.174  10.780  26.971  1.00 29.78           N  
-ATOM    334  CA  ILE A  70       7.286  10.675  25.522  1.00 31.13           C  
-ATOM    335  C   ILE A  70       7.755   9.317  25.016  1.00 33.84           C  
-ATOM    336  O   ILE A  70       8.011   9.154  23.827  1.00 35.59           O  
-ATOM    337  CB  ILE A  70       8.237  11.759  24.974  1.00 29.13           C  
-ATOM    338  CG1 ILE A  70       9.625  11.596  25.599  1.00 28.41           C  
-ATOM    339  CG2 ILE A  70       7.666  13.138  25.263  1.00 26.56           C  
-ATOM    340  CD1 ILE A  70      10.630  12.642  25.173  1.00 28.72           C  
-ATOM    341  N   ASN A  71       7.862   8.344  25.911  1.00 36.68           N  
-ATOM    342  CA  ASN A  71       8.305   7.009  25.530  1.00 40.43           C  
-ATOM    343  C   ASN A  71       7.388   6.382  24.473  1.00 42.36           C  
-ATOM    344  O   ASN A  71       7.860   5.754  23.529  1.00 44.86           O  
-ATOM    345  CB  ASN A  71       8.355   6.097  26.758  1.00 42.10           C  
-ATOM    346  CG  ASN A  71       9.051   4.775  26.476  1.00 45.30           C  
-ATOM    347  OD1 ASN A  71       8.744   3.752  27.092  1.00 46.49           O  
-ATOM    348  ND2 ASN A  71      10.006   4.794  25.547  1.00 46.60           N  
-ATOM    349  N   HIS A  72       6.080   6.558  24.634  1.00 43.40           N  
-ATOM    350  CA  HIS A  72       5.107   5.997  23.701  1.00 45.31           C  
-ATOM    351  C   HIS A  72       5.183   6.616  22.306  1.00 46.53           C  
-ATOM    352  O   HIS A  72       4.426   6.235  21.415  1.00 48.99           O  
-ATOM    353  CB  HIS A  72       3.689   6.185  24.242  1.00 45.60           C  
-ATOM    354  CG  HIS A  72       3.241   7.613  24.275  1.00 47.21           C  
-ATOM    355  ND1 HIS A  72       3.837   8.562  25.078  1.00 48.92           N  
-ATOM    356  CD2 HIS A  72       2.266   8.259  23.592  1.00 48.53           C  
-ATOM    357  CE1 HIS A  72       3.249   9.730  24.889  1.00 49.14           C  
-ATOM    358  NE2 HIS A  72       2.291   9.574  23.993  1.00 49.17           N  
-ATOM    359  N   ILE A  73       6.080   7.577  22.123  1.00 46.31           N  
-ATOM    360  CA  ILE A  73       6.237   8.238  20.832  1.00 46.88           C  
-ATOM    361  C   ILE A  73       7.568   7.833  20.201  1.00 48.86           C  
-ATOM    362  O   ILE A  73       7.625   7.446  19.037  1.00 49.52           O  
-ATOM    363  CB  ILE A  73       6.239   9.774  20.982  1.00 45.43           C  
-ATOM    364  CG1 ILE A  73       5.031  10.232  21.793  1.00 44.05           C  
-ATOM    365  CG2 ILE A  73       6.205  10.426  19.616  1.00 45.13           C  
-ATOM    366  CD1 ILE A  73       5.080  11.698  22.165  1.00 43.25           C  
-ATOM    367  N   TYR A  74       8.633   7.933  20.992  1.00 50.55           N  
-ATOM    368  CA  TYR A  74       9.989   7.603  20.560  1.00 50.46           C  
-ATOM    369  C   TYR A  74      10.076   6.208  19.955  1.00 51.15           C  
-ATOM    370  O   TYR A  74      10.969   5.927  19.154  1.00 51.05           O  
-ATOM    371  CB  TYR A  74      10.940   7.713  21.757  1.00 51.04           C  
-ATOM    372  CG  TYR A  74      12.399   7.900  21.401  1.00 49.77           C  
-ATOM    373  CD1 TYR A  74      12.780   8.766  20.376  1.00 49.65           C  
-ATOM    374  CD2 TYR A  74      13.402   7.267  22.137  1.00 49.16           C  
-ATOM    375  CE1 TYR A  74      14.119   9.000  20.092  1.00 48.55           C  
-ATOM    376  CE2 TYR A  74      14.750   7.496  21.863  1.00 49.70           C  
-ATOM    377  CZ  TYR A  74      15.100   8.366  20.838  1.00 49.91           C  
-ATOM    378  OH  TYR A  74      16.426   8.615  20.564  1.00 48.23           O  
-ATOM    379  N   LYS A  82       7.766   6.668  13.024  1.00 53.82           N  
-ATOM    380  CA  LYS A  82       8.609   5.926  13.953  1.00 53.66           C  
-ATOM    381  C   LYS A  82      10.091   6.207  13.710  1.00 53.85           C  
-ATOM    382  O   LYS A  82      10.920   5.295  13.755  1.00 54.72           O  
-ATOM    383  CB  LYS A  82       8.330   4.433  13.823  1.00 54.59           C  
-ATOM    384  N   ALA A  83      10.415   7.474  13.453  1.00 52.84           N  
-ATOM    385  CA  ALA A  83      11.792   7.910  13.202  1.00 51.58           C  
-ATOM    386  C   ALA A  83      11.821   9.421  12.950  1.00 50.01           C  
-ATOM    387  O   ALA A  83      12.798   9.967  12.423  1.00 49.95           O  
-ATOM    388  CB  ALA A  83      12.370   7.168  11.995  1.00 52.05           C  
-ATOM    389  N   LEU A  84      10.737  10.086  13.338  1.00 47.45           N  
-ATOM    390  CA  LEU A  84      10.590  11.524  13.162  1.00 45.23           C  
-ATOM    391  C   LEU A  84      10.828  12.283  14.464  1.00 43.07           C  
-ATOM    392  O   LEU A  84      10.763  13.512  14.493  1.00 43.07           O  
-ATOM    393  CB  LEU A  84       9.190  11.830  12.632  1.00 45.34           C  
-ATOM    394  CG  LEU A  84       8.906  11.306  11.223  1.00 46.56           C  
-ATOM    395  CD1 LEU A  84       7.415  11.363  10.928  1.00 46.92           C  
-ATOM    396  CD2 LEU A  84       9.692  12.137  10.218  1.00 44.81           C  
-ATOM    397  N   MET A  85      11.087  11.545  15.541  1.00 40.76           N  
-ATOM    398  CA  MET A  85      11.353  12.152  16.841  1.00 39.58           C  
-ATOM    399  C   MET A  85      12.755  11.763  17.295  1.00 37.68           C  
-ATOM    400  O   MET A  85      13.038  10.585  17.524  1.00 37.61           O  
-ATOM    401  CB  MET A  85      10.334  11.686  17.887  1.00 38.42           C  
-ATOM    402  CG  MET A  85      10.514  12.367  19.235  1.00 42.09           C  
-ATOM    403  SD  MET A  85       9.379  11.793  20.515  1.00 44.64           S  
-ATOM    404  CE  MET A  85      10.515  11.170  21.728  1.00 45.64           C  
-ATOM    405  N   LYS A  86      13.631  12.756  17.418  1.00 34.72           N  
-ATOM    406  CA  LYS A  86      15.006  12.518  17.844  1.00 33.20           C  
-ATOM    407  C   LYS A  86      15.316  13.255  19.148  1.00 31.64           C  
-ATOM    408  O   LYS A  86      14.967  14.428  19.308  1.00 32.06           O  
-ATOM    409  CB  LYS A  86      15.966  12.956  16.750  1.00 32.17           C  
-ATOM    410  N   LEU A  87      15.965  12.559  20.077  1.00 29.43           N  
-ATOM    411  CA  LEU A  87      16.328  13.137  21.369  1.00 27.75           C  
-ATOM    412  C   LEU A  87      17.842  13.299  21.458  1.00 28.25           C  
-ATOM    413  O   LEU A  87      18.593  12.378  21.121  1.00 28.49           O  
-ATOM    414  CB  LEU A  87      15.833  12.240  22.506  1.00 24.31           C  
-ATOM    415  CG  LEU A  87      14.328  11.961  22.506  1.00 24.39           C  
-ATOM    416  CD1 LEU A  87      13.960  11.011  23.642  1.00 25.22           C  
-ATOM    417  CD2 LEU A  87      13.572  13.271  22.637  1.00 24.45           C  
-ATOM    418  N   HIS A  88      18.285  14.472  21.909  1.00 28.88           N  
-ATOM    419  CA  HIS A  88      19.710  14.772  22.039  1.00 26.89           C  
-ATOM    420  C   HIS A  88      20.012  15.302  23.439  1.00 27.85           C  
-ATOM    421  O   HIS A  88      19.188  15.996  24.036  1.00 27.58           O  
-ATOM    422  CB  HIS A  88      20.116  15.827  21.011  1.00 27.67           C  
-ATOM    423  CG  HIS A  88      19.539  15.596  19.652  1.00 29.40           C  
-ATOM    424  ND1 HIS A  88      19.927  14.548  18.847  1.00 32.18           N  
-ATOM    425  CD2 HIS A  88      18.568  16.251  18.974  1.00 30.03           C  
-ATOM    426  CE1 HIS A  88      19.219  14.566  17.732  1.00 31.51           C  
-ATOM    427  NE2 HIS A  88      18.387  15.589  17.785  1.00 29.57           N  
-ATOM    428  N   TYR A  89      21.194  14.977  23.951  1.00 26.75           N  
-ATOM    429  CA  TYR A  89      21.608  15.427  25.273  1.00 27.20           C  
-ATOM    430  C   TYR A  89      22.102  16.861  25.223  1.00 27.18           C  
-ATOM    431  O   TYR A  89      22.919  17.216  24.374  1.00 29.44           O  
-ATOM    432  CB  TYR A  89      22.727  14.539  25.821  1.00 26.34           C  
-ATOM    433  CG  TYR A  89      22.265  13.194  26.306  1.00 25.77           C  
-ATOM    434  CD1 TYR A  89      22.797  12.020  25.776  1.00 26.85           C  
-ATOM    435  CD2 TYR A  89      21.306  13.089  27.313  1.00 27.06           C  
-ATOM    436  CE1 TYR A  89      22.386  10.769  26.240  1.00 28.95           C  
-ATOM    437  CE2 TYR A  89      20.889  11.847  27.781  1.00 27.78           C  
-ATOM    438  CZ  TYR A  89      21.434  10.692  27.240  1.00 28.70           C  
-ATOM    439  OH  TYR A  89      21.031   9.463  27.706  1.00 31.66           O  
-ATOM    440  N   ALA A  90      21.599  17.678  26.143  1.00 26.43           N  
-ATOM    441  CA  ALA A  90      21.986  19.079  26.237  1.00 23.16           C  
-ATOM    442  C   ALA A  90      21.493  19.630  27.570  1.00 21.88           C  
-ATOM    443  O   ALA A  90      20.838  18.921  28.328  1.00 22.25           O  
-ATOM    444  CB  ALA A  90      21.372  19.862  25.087  1.00 21.91           C  
-ATOM    445  N   ASP A  91      21.816  20.885  27.856  1.00 20.38           N  
-ATOM    446  CA  ASP A  91      21.372  21.527  29.088  1.00 21.06           C  
-ATOM    447  C   ASP A  91      21.356  23.038  28.885  1.00 21.80           C  
-ATOM    448  O   ASP A  91      22.261  23.597  28.270  1.00 22.33           O  
-ATOM    449  CB  ASP A  91      22.290  21.156  30.260  1.00 20.77           C  
-ATOM    450  CG  ASP A  91      21.675  21.493  31.606  1.00 21.37           C  
-ATOM    451  OD1 ASP A  91      21.522  22.692  31.919  1.00 26.54           O  
-ATOM    452  OD2 ASP A  91      21.327  20.558  32.349  1.00 25.62           O  
-ATOM    453  N   LEU A  92      20.316  23.695  29.391  1.00 23.72           N  
-ATOM    454  CA  LEU A  92      20.190  25.138  29.243  1.00 24.51           C  
-ATOM    455  C   LEU A  92      21.286  25.931  29.942  1.00 25.27           C  
-ATOM    456  O   LEU A  92      21.429  27.127  29.702  1.00 26.49           O  
-ATOM    457  CB  LEU A  92      18.822  25.612  29.735  1.00 27.10           C  
-ATOM    458  CG  LEU A  92      17.870  26.012  28.601  1.00 30.33           C  
-ATOM    459  CD1 LEU A  92      17.576  24.789  27.733  1.00 31.22           C  
-ATOM    460  CD2 LEU A  92      16.586  26.584  29.177  1.00 31.14           C  
-ATOM    461  N   THR A  93      22.055  25.271  30.803  1.00 23.02           N  
-ATOM    462  CA  THR A  93      23.142  25.936  31.504  1.00 23.69           C  
-ATOM    463  C   THR A  93      24.440  25.727  30.725  1.00 24.17           C  
-ATOM    464  O   THR A  93      25.502  26.185  31.138  1.00 23.84           O  
-ATOM    465  CB  THR A  93      23.329  25.374  32.925  1.00 24.05           C  
-ATOM    466  OG1 THR A  93      23.705  23.994  32.846  1.00 24.00           O  
-ATOM    467  CG2 THR A  93      22.034  25.503  33.724  1.00 24.42           C  
-ATOM    468  N   ASP A  94      24.339  25.035  29.593  1.00 23.45           N  
-ATOM    469  CA  ASP A  94      25.495  24.747  28.743  1.00 25.30           C  
-ATOM    470  C   ASP A  94      25.242  25.297  27.341  1.00 26.26           C  
-ATOM    471  O   ASP A  94      24.635  24.631  26.497  1.00 26.00           O  
-ATOM    472  CB  ASP A  94      25.739  23.231  28.683  1.00 24.07           C  
-ATOM    473  CG  ASP A  94      26.945  22.855  27.825  1.00 26.40           C  
-ATOM    474  OD1 ASP A  94      27.333  21.662  27.834  1.00 25.47           O  
-ATOM    475  OD2 ASP A  94      27.506  23.738  27.141  1.00 26.60           O  
-ATOM    476  N   ALA A  95      25.717  26.518  27.109  1.00 25.72           N  
-ATOM    477  CA  ALA A  95      25.554  27.194  25.828  1.00 27.08           C  
-ATOM    478  C   ALA A  95      26.075  26.358  24.666  1.00 27.85           C  
-ATOM    479  O   ALA A  95      25.442  26.295  23.614  1.00 29.11           O  
-ATOM    480  CB  ALA A  95      26.260  28.559  25.859  1.00 25.89           C  
-ATOM    481  N   SER A  96      27.230  25.724  24.855  1.00 29.39           N  
-ATOM    482  CA  SER A  96      27.816  24.884  23.814  1.00 30.24           C  
-ATOM    483  C   SER A  96      26.838  23.825  23.359  1.00 29.38           C  
-ATOM    484  O   SER A  96      26.590  23.676  22.171  1.00 32.15           O  
-ATOM    485  CB  SER A  96      29.075  24.176  24.318  1.00 30.78           C  
-ATOM    486  OG  SER A  96      30.132  25.086  24.518  1.00 36.35           O  
-ATOM    487  N   SER A  97      26.290  23.086  24.318  1.00 28.97           N  
-ATOM    488  CA  SER A  97      25.354  22.016  24.015  1.00 26.97           C  
-ATOM    489  C   SER A  97      24.197  22.513  23.173  1.00 26.80           C  
-ATOM    490  O   SER A  97      23.720  21.802  22.295  1.00 26.29           O  
-ATOM    491  CB  SER A  97      24.812  21.383  25.305  1.00 25.68           C  
-ATOM    492  OG  SER A  97      23.816  22.192  25.908  1.00 24.19           O  
-ATOM    493  N   LEU A  98      23.744  23.734  23.435  1.00 27.23           N  
-ATOM    494  CA  LEU A  98      22.626  24.286  22.683  1.00 27.92           C  
-ATOM    495  C   LEU A  98      22.990  24.530  21.221  1.00 30.28           C  
-ATOM    496  O   LEU A  98      22.397  23.941  20.317  1.00 30.72           O  
-ATOM    497  CB  LEU A  98      22.162  25.596  23.313  1.00 25.93           C  
-ATOM    498  CG  LEU A  98      21.753  25.533  24.785  1.00 25.38           C  
-ATOM    499  CD1 LEU A  98      21.128  26.869  25.171  1.00 20.65           C  
-ATOM    500  CD2 LEU A  98      20.776  24.390  25.013  1.00 18.47           C  
-ATOM    501  N   ARG A  99      23.969  25.401  21.003  1.00 30.15           N  
-ATOM    502  CA  ARG A  99      24.424  25.751  19.666  1.00 31.52           C  
-ATOM    503  C   ARG A  99      24.790  24.503  18.868  1.00 34.10           C  
-ATOM    504  O   ARG A  99      24.510  24.411  17.671  1.00 34.22           O  
-ATOM    505  CB  ARG A  99      25.636  26.685  19.764  1.00 30.61           C  
-ATOM    506  CG  ARG A  99      26.224  27.116  18.432  1.00 31.39           C  
-ATOM    507  CD  ARG A  99      25.228  27.916  17.602  1.00 32.31           C  
-ATOM    508  NE  ARG A  99      25.742  28.168  16.259  1.00 31.28           N  
-ATOM    509  CZ  ARG A  99      26.728  29.013  15.983  1.00 32.21           C  
-ATOM    510  NH1 ARG A  99      27.308  29.698  16.960  1.00 31.77           N  
-ATOM    511  NH2 ARG A  99      27.144  29.163  14.731  1.00 32.60           N  
-ATOM    512  N   ARG A 100      25.412  23.542  19.542  1.00 35.47           N  
-ATOM    513  CA  ARG A 100      25.828  22.302  18.904  1.00 34.79           C  
-ATOM    514  C   ARG A 100      24.670  21.665  18.148  1.00 36.78           C  
-ATOM    515  O   ARG A 100      24.746  21.462  16.936  1.00 37.62           O  
-ATOM    516  CB  ARG A 100      26.366  21.333  19.960  1.00 35.47           C  
-ATOM    517  CG  ARG A 100      26.790  19.971  19.432  1.00 36.70           C  
-ATOM    518  CD  ARG A 100      27.674  19.261  20.449  1.00 39.15           C  
-ATOM    519  NE  ARG A 100      27.986  17.882  20.081  1.00 40.08           N  
-ATOM    520  CZ  ARG A 100      28.957  17.164  20.641  1.00 41.62           C  
-ATOM    521  NH1 ARG A 100      29.173  15.913  20.252  1.00 42.28           N  
-ATOM    522  NH2 ARG A 100      29.723  17.699  21.583  1.00 39.40           N  
-ATOM    523  N   TRP A 101      23.591  21.368  18.860  1.00 35.23           N  
-ATOM    524  CA  TRP A 101      22.441  20.743  18.236  1.00 34.13           C  
-ATOM    525  C   TRP A 101      21.704  21.629  17.249  1.00 34.28           C  
-ATOM    526  O   TRP A 101      21.093  21.128  16.312  1.00 34.80           O  
-ATOM    527  CB  TRP A 101      21.495  20.215  19.311  1.00 33.78           C  
-ATOM    528  CG  TRP A 101      22.113  19.067  20.013  1.00 32.91           C  
-ATOM    529  CD1 TRP A 101      22.456  18.991  21.332  1.00 32.58           C  
-ATOM    530  CD2 TRP A 101      22.543  17.840  19.414  1.00 33.90           C  
-ATOM    531  NE1 TRP A 101      23.078  17.791  21.591  1.00 29.97           N  
-ATOM    532  CE2 TRP A 101      23.146  17.066  20.431  1.00 33.54           C  
-ATOM    533  CE3 TRP A 101      22.480  17.321  18.114  1.00 33.47           C  
-ATOM    534  CZ2 TRP A 101      23.685  15.796  20.188  1.00 35.26           C  
-ATOM    535  CZ3 TRP A 101      23.017  16.055  17.871  1.00 35.70           C  
-ATOM    536  CH2 TRP A 101      23.612  15.309  18.906  1.00 35.82           C  
-ATOM    537  N   ILE A 102      21.766  22.941  17.441  1.00 33.13           N  
-ATOM    538  CA  ILE A 102      21.097  23.844  16.519  1.00 32.22           C  
-ATOM    539  C   ILE A 102      21.791  23.789  15.157  1.00 33.07           C  
-ATOM    540  O   ILE A 102      21.134  23.839  14.118  1.00 32.03           O  
-ATOM    541  CB  ILE A 102      21.083  25.286  17.064  1.00 30.98           C  
-ATOM    542  CG1 ILE A 102      20.132  25.363  18.263  1.00 31.68           C  
-ATOM    543  CG2 ILE A 102      20.642  26.258  15.983  1.00 29.99           C  
-ATOM    544  CD1 ILE A 102      20.052  26.728  18.917  1.00 27.68           C  
-ATOM    545  N   ASP A 103      23.115  23.670  15.165  1.00 34.18           N  
-ATOM    546  CA  ASP A 103      23.875  23.585  13.920  1.00 36.49           C  
-ATOM    547  C   ASP A 103      23.572  22.279  13.192  1.00 37.33           C  
-ATOM    548  O   ASP A 103      23.226  22.278  12.013  1.00 39.30           O  
-ATOM    549  CB  ASP A 103      25.381  23.665  14.190  1.00 35.88           C  
-ATOM    550  CG  ASP A 103      25.834  25.058  14.579  1.00 36.59           C  
-ATOM    551  OD1 ASP A 103      25.058  26.018  14.378  1.00 37.44           O  
-ATOM    552  OD2 ASP A 103      26.975  25.192  15.075  1.00 39.09           O  
-ATOM    553  N   VAL A 104      23.703  21.168  13.905  1.00 37.01           N  
-ATOM    554  CA  VAL A 104      23.449  19.851  13.339  1.00 36.97           C  
-ATOM    555  C   VAL A 104      22.024  19.682  12.823  1.00 36.26           C  
-ATOM    556  O   VAL A 104      21.806  19.146  11.739  1.00 38.10           O  
-ATOM    557  CB  VAL A 104      23.721  18.747  14.385  1.00 37.46           C  
-ATOM    558  CG1 VAL A 104      23.300  17.388  13.844  1.00 38.88           C  
-ATOM    559  CG2 VAL A 104      25.195  18.737  14.748  1.00 37.95           C  
-ATOM    560  N   ILE A 105      21.057  20.150  13.602  1.00 35.61           N  
-ATOM    561  CA  ILE A 105      19.648  20.020  13.249  1.00 34.02           C  
-ATOM    562  C   ILE A 105      19.139  21.063  12.257  1.00 33.56           C  
-ATOM    563  O   ILE A 105      18.314  20.753  11.399  1.00 33.79           O  
-ATOM    564  CB  ILE A 105      18.766  20.073  14.524  1.00 33.43           C  
-ATOM    565  CG1 ILE A 105      19.204  18.978  15.499  1.00 34.00           C  
-ATOM    566  CG2 ILE A 105      17.290  19.900  14.159  1.00 31.52           C  
-ATOM    567  CD1 ILE A 105      18.539  19.061  16.862  1.00 34.08           C  
-ATOM    568  N   LYS A 106      19.621  22.294  12.374  1.00 32.72           N  
-ATOM    569  CA  LYS A 106      19.183  23.363  11.488  1.00 32.38           C  
-ATOM    570  C   LYS A 106      17.658  23.387  11.509  1.00 33.63           C  
-ATOM    571  O   LYS A 106      17.005  23.200  10.483  1.00 33.89           O  
-ATOM    572  CB  LYS A 106      19.694  23.112  10.070  1.00 32.68           C  
-ATOM    573  N   PRO A 107      17.069  23.613  12.694  1.00 33.39           N  
-ATOM    574  CA  PRO A 107      15.612  23.652  12.837  1.00 31.74           C  
-ATOM    575  C   PRO A 107      14.997  24.916  12.244  1.00 30.15           C  
-ATOM    576  O   PRO A 107      15.664  25.941  12.130  1.00 30.89           O  
-ATOM    577  CB  PRO A 107      15.423  23.582  14.350  1.00 30.80           C  
-ATOM    578  CG  PRO A 107      16.570  24.434  14.834  1.00 32.13           C  
-ATOM    579  CD  PRO A 107      17.730  23.928  13.978  1.00 32.66           C  
-ATOM    580  N   ASP A 108      13.723  24.834  11.873  1.00 30.13           N  
-ATOM    581  CA  ASP A 108      12.998  25.975  11.320  1.00 30.82           C  
-ATOM    582  C   ASP A 108      12.289  26.685  12.471  1.00 30.57           C  
-ATOM    583  O   ASP A 108      12.106  27.901  12.457  1.00 30.33           O  
-ATOM    584  CB  ASP A 108      11.960  25.499  10.292  1.00 31.29           C  
-ATOM    585  CG  ASP A 108      12.588  24.739   9.134  1.00 31.70           C  
-ATOM    586  OD1 ASP A 108      13.377  25.347   8.380  1.00 31.75           O  
-ATOM    587  OD2 ASP A 108      12.298  23.533   8.985  1.00 34.67           O  
-ATOM    588  N   GLU A 109      11.893  25.905  13.472  1.00 31.28           N  
-ATOM    589  CA  GLU A 109      11.199  26.444  14.635  1.00 31.82           C  
-ATOM    590  C   GLU A 109      11.808  25.956  15.947  1.00 30.16           C  
-ATOM    591  O   GLU A 109      12.070  24.767  16.116  1.00 28.79           O  
-ATOM    592  CB  GLU A 109       9.722  26.053  14.587  1.00 31.76           C  
-ATOM    593  CG  GLU A 109       8.982  26.600  13.378  1.00 35.92           C  
-ATOM    594  CD  GLU A 109       7.517  26.196  13.345  1.00 34.08           C  
-ATOM    595  OE1 GLU A 109       6.798  26.673  12.447  1.00 37.60           O  
-ATOM    596  OE2 GLU A 109       7.082  25.405  14.210  1.00 33.48           O  
-ATOM    597  N   VAL A 110      12.029  26.880  16.875  1.00 28.77           N  
-ATOM    598  CA  VAL A 110      12.588  26.530  18.178  1.00 26.69           C  
-ATOM    599  C   VAL A 110      11.614  26.883  19.300  1.00 25.18           C  
-ATOM    600  O   VAL A 110      11.186  28.025  19.427  1.00 25.14           O  
-ATOM    601  CB  VAL A 110      13.931  27.254  18.425  1.00 26.85           C  
-ATOM    602  CG1 VAL A 110      14.398  27.020  19.861  1.00 24.69           C  
-ATOM    603  CG2 VAL A 110      14.976  26.744  17.446  1.00 24.24           C  
-ATOM    604  N   TYR A 111      11.268  25.883  20.104  1.00 26.13           N  
-ATOM    605  CA  TYR A 111      10.349  26.053  21.225  1.00 26.22           C  
-ATOM    606  C   TYR A 111      11.097  25.889  22.552  1.00 25.54           C  
-ATOM    607  O   TYR A 111      11.541  24.793  22.890  1.00 24.54           O  
-ATOM    608  CB  TYR A 111       9.226  25.017  21.133  1.00 26.39           C  
-ATOM    609  CG  TYR A 111       8.292  25.232  19.965  1.00 28.03           C  
-ATOM    610  CD1 TYR A 111       7.154  26.028  20.099  1.00 27.79           C  
-ATOM    611  CD2 TYR A 111       8.557  24.660  18.719  1.00 27.01           C  
-ATOM    612  CE1 TYR A 111       6.296  26.253  19.019  1.00 28.57           C  
-ATOM    613  CE2 TYR A 111       7.708  24.878  17.630  1.00 27.68           C  
-ATOM    614  CZ  TYR A 111       6.581  25.676  17.788  1.00 29.78           C  
-ATOM    615  OH  TYR A 111       5.751  25.915  16.716  1.00 31.99           O  
-ATOM    616  N   ASN A 112      11.240  26.981  23.296  1.00 23.91           N  
-ATOM    617  CA  ASN A 112      11.942  26.926  24.570  1.00 22.45           C  
-ATOM    618  C   ASN A 112      10.983  26.686  25.727  1.00 20.67           C  
-ATOM    619  O   ASN A 112      10.450  27.627  26.303  1.00 19.51           O  
-ATOM    620  CB  ASN A 112      12.717  28.221  24.815  1.00 24.31           C  
-ATOM    621  CG  ASN A 112      13.593  28.142  26.048  1.00 24.54           C  
-ATOM    622  OD1 ASN A 112      14.297  27.152  26.253  1.00 24.15           O  
-ATOM    623  ND2 ASN A 112      13.560  29.185  26.873  1.00 24.22           N  
-ATOM    624  N   LEU A 113      10.761  25.420  26.057  1.00 19.17           N  
-ATOM    625  CA  LEU A 113       9.870  25.081  27.157  1.00 21.55           C  
-ATOM    626  C   LEU A 113      10.683  24.666  28.384  1.00 21.41           C  
-ATOM    627  O   LEU A 113      10.134  24.512  29.468  1.00 24.31           O  
-ATOM    628  CB  LEU A 113       8.944  23.939  26.750  1.00 20.14           C  
-ATOM    629  CG  LEU A 113       8.166  24.112  25.438  1.00 23.29           C  
-ATOM    630  CD1 LEU A 113       7.298  22.881  25.213  1.00 24.36           C  
-ATOM    631  CD2 LEU A 113       7.309  25.364  25.486  1.00 22.66           C  
-ATOM    632  N   ALA A 114      11.990  24.496  28.199  1.00 19.75           N  
-ATOM    633  CA  ALA A 114      12.878  24.074  29.276  1.00 21.76           C  
-ATOM    634  C   ALA A 114      12.910  25.033  30.460  1.00 21.28           C  
-ATOM    635  O   ALA A 114      13.079  26.245  30.297  1.00 23.25           O  
-ATOM    636  CB  ALA A 114      14.281  23.873  28.740  1.00 18.25           C  
-ATOM    637  N   ALA A 115      12.757  24.482  31.656  1.00 22.56           N  
-ATOM    638  CA  ALA A 115      12.782  25.301  32.859  1.00 22.40           C  
-ATOM    639  C   ALA A 115      12.624  24.520  34.147  1.00 22.04           C  
-ATOM    640  O   ALA A 115      12.114  23.400  34.155  1.00 19.85           O  
-ATOM    641  CB  ALA A 115      11.681  26.351  32.789  1.00 21.50           C  
-ATOM    642  N   GLN A 116      13.106  25.128  35.228  1.00 23.25           N  
-ATOM    643  CA  GLN A 116      12.936  24.594  36.570  1.00 21.35           C  
-ATOM    644  C   GLN A 116      11.635  25.360  36.786  1.00 20.93           C  
-ATOM    645  O   GLN A 116      11.645  26.519  37.178  1.00 20.46           O  
-ATOM    646  CB  GLN A 116      14.029  25.111  37.511  1.00 20.41           C  
-ATOM    647  CG  GLN A 116      13.951  24.564  38.942  1.00 17.64           C  
-ATOM    648  CD  GLN A 116      12.588  24.786  39.581  1.00 18.36           C  
-ATOM    649  OE1 GLN A 116      11.683  23.962  39.442  1.00 18.82           O  
-ATOM    650  NE2 GLN A 116      12.431  25.914  40.272  1.00 21.41           N  
-ATOM    651  N   SER A 117      10.520  24.708  36.488  1.00 21.70           N  
-ATOM    652  CA  SER A 117       9.221  25.356  36.546  1.00 22.42           C  
-ATOM    653  C   SER A 117       8.453  25.411  37.858  1.00 21.91           C  
-ATOM    654  O   SER A 117       7.361  25.972  37.898  1.00 22.11           O  
-ATOM    655  CB  SER A 117       8.321  24.741  35.478  1.00 22.61           C  
-ATOM    656  OG  SER A 117       8.083  23.379  35.766  1.00 24.42           O  
-ATOM    657  N   HIS A 118       8.985  24.839  38.928  1.00 23.23           N  
-ATOM    658  CA  HIS A 118       8.243  24.904  40.178  1.00 24.90           C  
-ATOM    659  C   HIS A 118       8.558  26.182  40.947  1.00 22.40           C  
-ATOM    660  O   HIS A 118       9.714  26.485  41.237  1.00 25.26           O  
-ATOM    661  CB  HIS A 118       8.515  23.679  41.044  1.00 26.28           C  
-ATOM    662  CG  HIS A 118       7.431  23.414  42.044  1.00 29.59           C  
-ATOM    663  ND1 HIS A 118       7.298  24.137  43.210  1.00 30.19           N  
-ATOM    664  CD2 HIS A 118       6.384  22.555  42.014  1.00 30.68           C  
-ATOM    665  CE1 HIS A 118       6.215  23.738  43.853  1.00 30.84           C  
-ATOM    666  NE2 HIS A 118       5.642  22.779  43.149  1.00 31.01           N  
-ATOM    667  N   VAL A 119       7.507  26.929  41.264  1.00 23.68           N  
-ATOM    668  CA  VAL A 119       7.623  28.190  41.985  1.00 23.99           C  
-ATOM    669  C   VAL A 119       8.148  28.052  43.416  1.00 25.29           C  
-ATOM    670  O   VAL A 119       9.023  28.817  43.829  1.00 25.81           O  
-ATOM    671  CB  VAL A 119       6.258  28.924  41.998  1.00 24.26           C  
-ATOM    672  CG1 VAL A 119       6.307  30.131  42.914  1.00 23.88           C  
-ATOM    673  CG2 VAL A 119       5.904  29.360  40.577  1.00 23.23           C  
-ATOM    674  N   ALA A 120       7.626  27.086  44.169  1.00 23.86           N  
-ATOM    675  CA  ALA A 120       8.076  26.890  45.549  1.00 25.68           C  
-ATOM    676  C   ALA A 120       9.541  26.466  45.555  1.00 26.09           C  
-ATOM    677  O   ALA A 120      10.347  26.970  46.337  1.00 26.15           O  
-ATOM    678  CB  ALA A 120       7.224  25.836  46.243  1.00 23.05           C  
-ATOM    679  N   VAL A 121       9.879  25.533  44.675  1.00 26.30           N  
-ATOM    680  CA  VAL A 121      11.248  25.061  44.575  1.00 25.31           C  
-ATOM    681  C   VAL A 121      12.189  26.210  44.219  1.00 26.82           C  
-ATOM    682  O   VAL A 121      13.350  26.211  44.633  1.00 27.70           O  
-ATOM    683  CB  VAL A 121      11.371  23.950  43.509  1.00 26.57           C  
-ATOM    684  CG1 VAL A 121      12.824  23.528  43.348  1.00 27.23           C  
-ATOM    685  CG2 VAL A 121      10.516  22.755  43.916  1.00 24.94           C  
-ATOM    686  N   SER A 122      11.692  27.200  43.475  1.00 26.56           N  
-ATOM    687  CA  SER A 122      12.541  28.321  43.077  1.00 26.31           C  
-ATOM    688  C   SER A 122      13.030  29.153  44.262  1.00 26.33           C  
-ATOM    689  O   SER A 122      14.068  29.802  44.172  1.00 25.77           O  
-ATOM    690  CB  SER A 122      11.828  29.220  42.058  1.00 25.12           C  
-ATOM    691  OG  SER A 122      10.860  30.049  42.663  1.00 27.98           O  
-ATOM    692  N   PHE A 123      12.292  29.142  45.370  1.00 27.18           N  
-ATOM    693  CA  PHE A 123      12.729  29.888  46.549  1.00 26.73           C  
-ATOM    694  C   PHE A 123      13.899  29.166  47.219  1.00 26.36           C  
-ATOM    695  O   PHE A 123      14.718  29.793  47.882  1.00 25.81           O  
-ATOM    696  CB  PHE A 123      11.600  30.040  47.571  1.00 25.73           C  
-ATOM    697  CG  PHE A 123      10.506  30.970  47.143  1.00 24.05           C  
-ATOM    698  CD1 PHE A 123       9.357  30.482  46.539  1.00 24.79           C  
-ATOM    699  CD2 PHE A 123      10.614  32.336  47.372  1.00 24.59           C  
-ATOM    700  CE1 PHE A 123       8.327  31.342  46.175  1.00 24.17           C  
-ATOM    701  CE2 PHE A 123       9.589  33.206  47.011  1.00 22.97           C  
-ATOM    702  CZ  PHE A 123       8.447  32.711  46.414  1.00 25.02           C  
-ATOM    703  N   GLU A 124      13.973  27.849  47.038  1.00 28.50           N  
-ATOM    704  CA  GLU A 124      15.042  27.052  47.639  1.00 30.48           C  
-ATOM    705  C   GLU A 124      16.298  27.018  46.786  1.00 29.46           C  
-ATOM    706  O   GLU A 124      17.405  26.933  47.315  1.00 28.92           O  
-ATOM    707  CB  GLU A 124      14.571  25.621  47.893  1.00 34.58           C  
-ATOM    708  CG  GLU A 124      13.293  25.533  48.700  1.00 41.20           C  
-ATOM    709  CD  GLU A 124      13.189  24.238  49.465  1.00 45.10           C  
-ATOM    710  OE1 GLU A 124      13.818  24.139  50.540  1.00 50.17           O  
-ATOM    711  OE2 GLU A 124      12.495  23.315  48.988  1.00 47.82           O  
-ATOM    712  N   ILE A 125      16.128  27.050  45.467  1.00 27.88           N  
-ATOM    713  CA  ILE A 125      17.274  27.059  44.570  1.00 27.14           C  
-ATOM    714  C   ILE A 125      17.132  28.200  43.577  1.00 27.47           C  
-ATOM    715  O   ILE A 125      17.000  27.986  42.372  1.00 26.82           O  
-ATOM    716  CB  ILE A 125      17.439  25.721  43.815  1.00 26.83           C  
-ATOM    717  CG1 ILE A 125      16.113  25.284  43.193  1.00 26.56           C  
-ATOM    718  CG2 ILE A 125      17.961  24.660  44.765  1.00 26.23           C  
-ATOM    719  CD1 ILE A 125      16.276  24.182  42.174  1.00 23.39           C  
-ATOM    720  N   PRO A 126      17.161  29.444  44.084  1.00 27.27           N  
-ATOM    721  CA  PRO A 126      17.032  30.639  43.252  1.00 26.17           C  
-ATOM    722  C   PRO A 126      18.092  30.780  42.172  1.00 25.56           C  
-ATOM    723  O   PRO A 126      17.767  31.073  41.022  1.00 24.79           O  
-ATOM    724  CB  PRO A 126      17.088  31.779  44.274  1.00 26.36           C  
-ATOM    725  CG  PRO A 126      17.946  31.215  45.364  1.00 25.24           C  
-ATOM    726  CD  PRO A 126      17.377  29.819  45.494  1.00 27.78           C  
-ATOM    727  N   ASP A 127      19.355  30.577  42.535  1.00 25.42           N  
-ATOM    728  CA  ASP A 127      20.440  30.721  41.572  1.00 26.34           C  
-ATOM    729  C   ASP A 127      20.305  29.797  40.368  1.00 25.04           C  
-ATOM    730  O   ASP A 127      20.341  30.254  39.223  1.00 22.13           O  
-ATOM    731  CB  ASP A 127      21.793  30.520  42.255  1.00 30.57           C  
-ATOM    732  CG  ASP A 127      22.070  31.582  43.310  1.00 37.73           C  
-ATOM    733  OD1 ASP A 127      21.609  32.733  43.133  1.00 37.03           O  
-ATOM    734  OD2 ASP A 127      22.756  31.275  44.309  1.00 41.77           O  
-ATOM    735  N   TYR A 128      20.151  28.506  40.624  1.00 22.27           N  
-ATOM    736  CA  TYR A 128      19.993  27.537  39.547  1.00 23.30           C  
-ATOM    737  C   TYR A 128      18.767  27.888  38.691  1.00 24.35           C  
-ATOM    738  O   TYR A 128      18.831  27.893  37.461  1.00 22.96           O  
-ATOM    739  CB  TYR A 128      19.817  26.127  40.121  1.00 20.64           C  
-ATOM    740  CG  TYR A 128      19.532  25.086  39.071  1.00 21.52           C  
-ATOM    741  CD1 TYR A 128      20.571  24.477  38.359  1.00 19.24           C  
-ATOM    742  CD2 TYR A 128      18.218  24.742  38.748  1.00 20.82           C  
-ATOM    743  CE1 TYR A 128      20.306  23.554  37.352  1.00 18.98           C  
-ATOM    744  CE2 TYR A 128      17.938  23.827  37.747  1.00 20.19           C  
-ATOM    745  CZ  TYR A 128      18.986  23.236  37.049  1.00 23.34           C  
-ATOM    746  OH  TYR A 128      18.706  22.345  36.041  1.00 25.29           O  
-ATOM    747  N   THR A 129      17.650  28.173  39.352  1.00 23.62           N  
-ATOM    748  CA  THR A 129      16.427  28.508  38.646  1.00 23.25           C  
-ATOM    749  C   THR A 129      16.648  29.687  37.708  1.00 23.44           C  
-ATOM    750  O   THR A 129      16.188  29.672  36.568  1.00 23.70           O  
-ATOM    751  CB  THR A 129      15.289  28.850  39.622  1.00 24.03           C  
-ATOM    752  OG1 THR A 129      14.997  27.706  40.431  1.00 24.71           O  
-ATOM    753  CG2 THR A 129      14.027  29.252  38.856  1.00 23.89           C  
-ATOM    754  N   ALA A 130      17.354  30.703  38.191  1.00 22.05           N  
-ATOM    755  CA  ALA A 130      17.633  31.888  37.389  1.00 21.78           C  
-ATOM    756  C   ALA A 130      18.509  31.541  36.190  1.00 23.27           C  
-ATOM    757  O   ALA A 130      18.215  31.926  35.056  1.00 23.02           O  
-ATOM    758  CB  ALA A 130      18.319  32.944  38.239  1.00 19.69           C  
-ATOM    759  N   ASP A 131      19.580  30.798  36.446  1.00 22.42           N  
-ATOM    760  CA  ASP A 131      20.511  30.411  35.395  1.00 24.34           C  
-ATOM    761  C   ASP A 131      19.839  29.620  34.274  1.00 24.75           C  
-ATOM    762  O   ASP A 131      20.257  29.691  33.119  1.00 25.31           O  
-ATOM    763  CB  ASP A 131      21.662  29.594  35.990  1.00 25.70           C  
-ATOM    764  CG  ASP A 131      22.848  29.485  35.047  1.00 25.56           C  
-ATOM    765  OD1 ASP A 131      23.288  30.523  34.504  1.00 25.24           O  
-ATOM    766  OD2 ASP A 131      23.345  28.362  34.855  1.00 29.46           O  
-ATOM    767  N   VAL A 132      18.796  28.875  34.619  1.00 24.28           N  
-ATOM    768  CA  VAL A 132      18.076  28.069  33.644  1.00 23.38           C  
-ATOM    769  C   VAL A 132      16.926  28.826  32.969  1.00 24.50           C  
-ATOM    770  O   VAL A 132      16.825  28.876  31.742  1.00 23.88           O  
-ATOM    771  CB  VAL A 132      17.483  26.810  34.309  1.00 22.57           C  
-ATOM    772  CG1 VAL A 132      16.666  26.018  33.298  1.00 23.03           C  
-ATOM    773  CG2 VAL A 132      18.590  25.956  34.890  1.00 21.54           C  
-ATOM    774  N   VAL A 133      16.067  29.413  33.791  1.00 23.92           N  
-ATOM    775  CA  VAL A 133      14.888  30.127  33.324  1.00 23.43           C  
-ATOM    776  C   VAL A 133      15.145  31.477  32.657  1.00 24.20           C  
-ATOM    777  O   VAL A 133      14.493  31.812  31.667  1.00 25.34           O  
-ATOM    778  CB  VAL A 133      13.896  30.307  34.489  1.00 21.74           C  
-ATOM    779  CG1 VAL A 133      12.657  31.066  34.031  1.00 19.65           C  
-ATOM    780  CG2 VAL A 133      13.520  28.944  35.039  1.00 19.00           C  
-ATOM    781  N   ALA A 134      16.092  32.245  33.189  1.00 23.72           N  
-ATOM    782  CA  ALA A 134      16.411  33.553  32.633  1.00 23.41           C  
-ATOM    783  C   ALA A 134      17.614  33.520  31.691  1.00 24.49           C  
-ATOM    784  O   ALA A 134      17.477  33.753  30.493  1.00 25.40           O  
-ATOM    785  CB  ALA A 134      16.658  34.550  33.759  1.00 23.71           C  
-ATOM    786  N   THR A 135      18.792  33.224  32.226  1.00 23.24           N  
-ATOM    787  CA  THR A 135      19.994  33.197  31.401  1.00 22.51           C  
-ATOM    788  C   THR A 135      19.946  32.065  30.386  1.00 22.77           C  
-ATOM    789  O   THR A 135      20.464  32.200  29.283  1.00 22.47           O  
-ATOM    790  CB  THR A 135      21.262  33.053  32.266  1.00 21.87           C  
-ATOM    791  OG1 THR A 135      21.277  34.088  33.256  1.00 24.42           O  
-ATOM    792  CG2 THR A 135      22.508  33.187  31.417  1.00 23.14           C  
-ATOM    793  N   GLY A 136      19.322  30.953  30.766  1.00 22.32           N  
-ATOM    794  CA  GLY A 136      19.221  29.813  29.872  1.00 22.26           C  
-ATOM    795  C   GLY A 136      18.469  30.208  28.614  1.00 23.82           C  
-ATOM    796  O   GLY A 136      18.846  29.823  27.509  1.00 22.82           O  
-ATOM    797  N   ALA A 137      17.406  30.988  28.790  1.00 24.22           N  
-ATOM    798  CA  ALA A 137      16.595  31.457  27.674  1.00 25.07           C  
-ATOM    799  C   ALA A 137      17.444  32.378  26.802  1.00 26.31           C  
-ATOM    800  O   ALA A 137      17.364  32.331  25.575  1.00 27.97           O  
-ATOM    801  CB  ALA A 137      15.366  32.199  28.189  1.00 21.29           C  
-ATOM    802  N   LEU A 138      18.271  33.204  27.438  1.00 26.39           N  
-ATOM    803  CA  LEU A 138      19.136  34.113  26.700  1.00 25.83           C  
-ATOM    804  C   LEU A 138      20.186  33.329  25.902  1.00 26.64           C  
-ATOM    805  O   LEU A 138      20.506  33.692  24.771  1.00 26.85           O  
-ATOM    806  CB  LEU A 138      19.811  35.105  27.655  1.00 24.29           C  
-ATOM    807  CG  LEU A 138      20.705  36.191  27.034  1.00 24.93           C  
-ATOM    808  CD1 LEU A 138      19.924  36.995  25.999  1.00 24.47           C  
-ATOM    809  CD2 LEU A 138      21.230  37.113  28.125  1.00 23.41           C  
-ATOM    810  N   ARG A 139      20.706  32.245  26.477  1.00 25.43           N  
-ATOM    811  CA  ARG A 139      21.706  31.434  25.783  1.00 25.24           C  
-ATOM    812  C   ARG A 139      21.132  30.846  24.495  1.00 26.06           C  
-ATOM    813  O   ARG A 139      21.796  30.834  23.456  1.00 25.36           O  
-ATOM    814  CB  ARG A 139      22.197  30.286  26.668  1.00 25.39           C  
-ATOM    815  CG  ARG A 139      22.951  30.712  27.911  1.00 24.90           C  
-ATOM    816  CD  ARG A 139      23.522  29.502  28.636  1.00 22.61           C  
-ATOM    817  NE  ARG A 139      24.242  29.900  29.839  1.00 25.42           N  
-ATOM    818  CZ  ARG A 139      23.704  29.965  31.052  1.00 23.28           C  
-ATOM    819  NH1 ARG A 139      24.444  30.353  32.079  1.00 23.40           N  
-ATOM    820  NH2 ARG A 139      22.440  29.613  31.247  1.00 22.46           N  
-ATOM    821  N   LEU A 140      19.902  30.348  24.573  1.00 23.17           N  
-ATOM    822  CA  LEU A 140      19.250  29.758  23.413  1.00 25.74           C  
-ATOM    823  C   LEU A 140      19.034  30.823  22.334  1.00 26.82           C  
-ATOM    824  O   LEU A 140      19.312  30.587  21.157  1.00 27.30           O  
-ATOM    825  CB  LEU A 140      17.912  29.137  23.822  1.00 24.45           C  
-ATOM    826  CG  LEU A 140      17.259  28.175  22.829  1.00 22.47           C  
-ATOM    827  CD1 LEU A 140      18.207  27.012  22.540  1.00 21.07           C  
-ATOM    828  CD2 LEU A 140      15.938  27.662  23.410  1.00 19.25           C  
-ATOM    829  N   LEU A 141      18.541  31.990  22.744  1.00 27.88           N  
-ATOM    830  CA  LEU A 141      18.307  33.103  21.827  1.00 27.68           C  
-ATOM    831  C   LEU A 141      19.612  33.510  21.146  1.00 28.49           C  
-ATOM    832  O   LEU A 141      19.637  33.784  19.946  1.00 28.62           O  
-ATOM    833  CB  LEU A 141      17.750  34.314  22.581  1.00 26.59           C  
-ATOM    834  CG  LEU A 141      16.288  34.346  23.027  1.00 27.11           C  
-ATOM    835  CD1 LEU A 141      16.119  35.411  24.089  1.00 25.42           C  
-ATOM    836  CD2 LEU A 141      15.378  34.633  21.835  1.00 26.50           C  
-ATOM    837  N   GLU A 142      20.693  33.560  21.918  1.00 27.78           N  
-ATOM    838  CA  GLU A 142      21.990  33.945  21.381  1.00 28.46           C  
-ATOM    839  C   GLU A 142      22.575  32.851  20.493  1.00 29.37           C  
-ATOM    840  O   GLU A 142      23.321  33.136  19.557  1.00 30.17           O  
-ATOM    841  CB  GLU A 142      22.955  34.271  22.523  1.00 29.60           C  
-ATOM    842  CG  GLU A 142      24.370  34.624  22.076  1.00 31.59           C  
-ATOM    843  CD  GLU A 142      24.440  35.867  21.191  1.00 35.09           C  
-ATOM    844  OE1 GLU A 142      23.386  36.479  20.897  1.00 33.56           O  
-ATOM    845  OE2 GLU A 142      25.565  36.231  20.787  1.00 35.88           O  
-ATOM    846  N   ALA A 143      22.239  31.600  20.787  1.00 28.65           N  
-ATOM    847  CA  ALA A 143      22.730  30.481  19.991  1.00 30.72           C  
-ATOM    848  C   ALA A 143      21.983  30.466  18.656  1.00 32.32           C  
-ATOM    849  O   ALA A 143      22.568  30.172  17.615  1.00 32.81           O  
-ATOM    850  CB  ALA A 143      22.521  29.165  20.731  1.00 29.80           C  
-ATOM    851  N   VAL A 144      20.692  30.789  18.694  1.00 32.25           N  
-ATOM    852  CA  VAL A 144      19.884  30.832  17.482  1.00 31.30           C  
-ATOM    853  C   VAL A 144      20.292  32.025  16.623  1.00 32.16           C  
-ATOM    854  O   VAL A 144      20.371  31.912  15.406  1.00 34.91           O  
-ATOM    855  CB  VAL A 144      18.375  30.910  17.821  1.00 29.29           C  
-ATOM    856  CG1 VAL A 144      17.572  31.350  16.604  1.00 28.65           C  
-ATOM    857  CG2 VAL A 144      17.892  29.542  18.281  1.00 26.57           C  
-ATOM    858  N   ARG A 145      20.561  33.165  17.255  1.00 33.56           N  
-ATOM    859  CA  ARG A 145      20.979  34.354  16.518  1.00 32.07           C  
-ATOM    860  C   ARG A 145      22.335  34.114  15.859  1.00 32.69           C  
-ATOM    861  O   ARG A 145      22.544  34.477  14.700  1.00 33.12           O  
-ATOM    862  CB  ARG A 145      21.089  35.569  17.443  1.00 31.41           C  
-ATOM    863  CG  ARG A 145      21.294  36.883  16.691  1.00 33.06           C  
-ATOM    864  CD  ARG A 145      21.722  38.015  17.612  1.00 35.47           C  
-ATOM    865  NE  ARG A 145      23.069  37.796  18.130  1.00 38.98           N  
-ATOM    866  CZ  ARG A 145      24.176  37.847  17.391  1.00 43.52           C  
-ATOM    867  NH1 ARG A 145      24.103  38.120  16.093  1.00 45.20           N  
-ATOM    868  NH2 ARG A 145      25.358  37.603  17.943  1.00 42.71           N  
-ATOM    869  N   SER A 146      23.259  33.510  16.604  1.00 32.32           N  
-ATOM    870  CA  SER A 146      24.590  33.227  16.078  1.00 32.17           C  
-ATOM    871  C   SER A 146      24.489  32.224  14.944  1.00 33.40           C  
-ATOM    872  O   SER A 146      25.274  32.259  13.999  1.00 33.76           O  
-ATOM    873  CB  SER A 146      25.499  32.664  17.173  1.00 31.21           C  
-ATOM    874  OG  SER A 146      25.676  33.605  18.216  1.00 31.86           O  
-ATOM    875  N   HIS A 147      23.517  31.326  15.049  1.00 33.60           N  
-ATOM    876  CA  HIS A 147      23.310  30.313  14.033  1.00 34.44           C  
-ATOM    877  C   HIS A 147      22.818  30.950  12.741  1.00 36.12           C  
-ATOM    878  O   HIS A 147      23.421  30.762  11.689  1.00 37.95           O  
-ATOM    879  CB  HIS A 147      22.297  29.280  14.522  1.00 35.80           C  
-ATOM    880  CG  HIS A 147      21.848  28.319  13.464  1.00 35.88           C  
-ATOM    881  ND1 HIS A 147      22.708  27.442  12.839  1.00 36.64           N  
-ATOM    882  CD2 HIS A 147      20.624  28.087  12.933  1.00 35.60           C  
-ATOM    883  CE1 HIS A 147      22.034  26.710  11.971  1.00 36.05           C  
-ATOM    884  NE2 HIS A 147      20.767  27.081  12.008  1.00 35.51           N  
-ATOM    885  N   THR A 148      21.731  31.710  12.825  1.00 37.10           N  
-ATOM    886  CA  THR A 148      21.159  32.354  11.647  1.00 37.30           C  
-ATOM    887  C   THR A 148      22.110  33.323  10.941  1.00 39.76           C  
-ATOM    888  O   THR A 148      22.012  33.527   9.731  1.00 39.97           O  
-ATOM    889  CB  THR A 148      19.861  33.110  12.000  1.00 35.81           C  
-ATOM    890  OG1 THR A 148      20.135  34.103  12.993  1.00 35.05           O  
-ATOM    891  CG2 THR A 148      18.813  32.149  12.529  1.00 34.41           C  
-ATOM    892  N   ILE A 149      23.031  33.915  11.693  1.00 40.38           N  
-ATOM    893  CA  ILE A 149      23.983  34.858  11.119  1.00 41.27           C  
-ATOM    894  C   ILE A 149      25.145  34.139  10.443  1.00 40.80           C  
-ATOM    895  O   ILE A 149      25.641  34.580   9.407  1.00 41.42           O  
-ATOM    896  CB  ILE A 149      24.542  35.817  12.207  1.00 41.90           C  
-ATOM    897  CG1 ILE A 149      23.452  36.801  12.636  1.00 42.05           C  
-ATOM    898  CG2 ILE A 149      25.761  36.569  11.685  1.00 42.37           C  
-ATOM    899  CD1 ILE A 149      22.889  37.631  11.491  1.00 43.77           C  
-ATOM    900  N   ASP A 150      25.562  33.027  11.032  1.00 39.69           N  
-ATOM    901  CA  ASP A 150      26.675  32.244  10.516  1.00 39.67           C  
-ATOM    902  C   ASP A 150      26.265  31.319   9.372  1.00 41.23           C  
-ATOM    903  O   ASP A 150      27.099  30.910   8.569  1.00 40.54           O  
-ATOM    904  CB  ASP A 150      27.269  31.408  11.644  1.00 39.30           C  
-ATOM    905  CG  ASP A 150      28.525  30.677  11.232  1.00 39.30           C  
-ATOM    906  OD1 ASP A 150      29.539  31.353  10.963  1.00 43.00           O  
-ATOM    907  OD2 ASP A 150      28.501  29.429  11.180  1.00 41.31           O  
-ATOM    908  N   SER A 151      24.979  30.992   9.303  1.00 42.21           N  
-ATOM    909  CA  SER A 151      24.478  30.090   8.274  1.00 42.49           C  
-ATOM    910  C   SER A 151      23.559  30.776   7.279  1.00 42.44           C  
-ATOM    911  O   SER A 151      23.292  30.236   6.206  1.00 43.13           O  
-ATOM    912  CB  SER A 151      23.724  28.930   8.924  1.00 43.25           C  
-ATOM    913  OG  SER A 151      22.540  29.396   9.549  1.00 41.78           O  
-ATOM    914  N   GLY A 152      23.066  31.956   7.640  1.00 41.56           N  
-ATOM    915  CA  GLY A 152      22.170  32.677   6.756  1.00 41.44           C  
-ATOM    916  C   GLY A 152      20.749  32.141   6.802  1.00 40.94           C  
-ATOM    917  O   GLY A 152      19.852  32.683   6.157  1.00 41.43           O  
-ATOM    918  N   ARG A 153      20.539  31.075   7.568  1.00 40.71           N  
-ATOM    919  CA  ARG A 153      19.220  30.468   7.696  1.00 40.02           C  
-ATOM    920  C   ARG A 153      18.279  31.319   8.543  1.00 40.01           C  
-ATOM    921  O   ARG A 153      18.705  32.260   9.213  1.00 40.22           O  
-ATOM    922  CB  ARG A 153      19.333  29.084   8.333  1.00 40.49           C  
-ATOM    923  CG  ARG A 153      20.222  28.112   7.590  1.00 39.64           C  
-ATOM    924  CD  ARG A 153      20.071  26.714   8.169  1.00 39.52           C  
-ATOM    925  NE  ARG A 153      18.676  26.271   8.148  1.00 38.65           N  
-ATOM    926  CZ  ARG A 153      17.825  26.383   9.166  1.00 38.05           C  
-ATOM    927  NH1 ARG A 153      18.212  26.923  10.317  1.00 36.25           N  
-ATOM    928  NH2 ARG A 153      16.574  25.964   9.026  1.00 35.63           N  
-ATOM    929  N   THR A 154      16.996  30.977   8.509  1.00 38.79           N  
-ATOM    930  CA  THR A 154      15.986  31.692   9.282  1.00 39.08           C  
-ATOM    931  C   THR A 154      15.346  30.738  10.293  1.00 36.71           C  
-ATOM    932  O   THR A 154      15.120  29.567   9.992  1.00 36.66           O  
-ATOM    933  CB  THR A 154      14.898  32.277   8.357  1.00 39.94           C  
-ATOM    934  OG1 THR A 154      15.486  33.282   7.524  1.00 43.69           O  
-ATOM    935  CG2 THR A 154      13.770  32.899   9.170  1.00 41.10           C  
-ATOM    936  N   VAL A 155      15.060  31.242  11.489  1.00 33.77           N  
-ATOM    937  CA  VAL A 155      14.468  30.419  12.541  1.00 30.85           C  
-ATOM    938  C   VAL A 155      13.378  31.177  13.292  1.00 30.63           C  
-ATOM    939  O   VAL A 155      13.550  32.350  13.622  1.00 29.59           O  
-ATOM    940  CB  VAL A 155      15.551  29.980  13.571  1.00 30.42           C  
-ATOM    941  CG1 VAL A 155      14.946  29.064  14.619  1.00 30.83           C  
-ATOM    942  CG2 VAL A 155      16.705  29.281  12.861  1.00 29.15           C  
-ATOM    943  N   LYS A 156      12.253  30.514  13.548  1.00 30.15           N  
-ATOM    944  CA  LYS A 156      11.166  31.130  14.304  1.00 31.21           C  
-ATOM    945  C   LYS A 156      11.326  30.643  15.750  1.00 31.33           C  
-ATOM    946  O   LYS A 156      11.543  29.456  15.999  1.00 30.18           O  
-ATOM    947  CB  LYS A 156       9.806  30.736  13.717  1.00 32.33           C  
-ATOM    948  CG  LYS A 156       9.555  31.345  12.332  1.00 34.58           C  
-ATOM    949  CD  LYS A 156       8.106  31.188  11.892  1.00 37.36           C  
-ATOM    950  CE  LYS A 156       7.821  31.993  10.625  1.00 40.68           C  
-ATOM    951  NZ  LYS A 156       6.369  32.003  10.243  1.00 39.07           N  
-ATOM    952  N   TYR A 157      11.214  31.565  16.698  1.00 29.39           N  
-ATOM    953  CA  TYR A 157      11.440  31.248  18.099  1.00 27.63           C  
-ATOM    954  C   TYR A 157      10.253  31.480  19.023  1.00 27.07           C  
-ATOM    955  O   TYR A 157       9.596  32.520  18.967  1.00 27.20           O  
-ATOM    956  CB  TYR A 157      12.630  32.085  18.579  1.00 26.53           C  
-ATOM    957  CG  TYR A 157      13.189  31.746  19.946  1.00 26.10           C  
-ATOM    958  CD1 TYR A 157      14.293  30.906  20.078  1.00 25.96           C  
-ATOM    959  CD2 TYR A 157      12.663  32.328  21.102  1.00 26.50           C  
-ATOM    960  CE1 TYR A 157      14.868  30.660  21.324  1.00 27.02           C  
-ATOM    961  CE2 TYR A 157      13.229  32.088  22.352  1.00 25.15           C  
-ATOM    962  CZ  TYR A 157      14.334  31.258  22.456  1.00 25.97           C  
-ATOM    963  OH  TYR A 157      14.929  31.054  23.681  1.00 26.89           O  
-ATOM    964  N   TYR A 158      10.002  30.507  19.892  1.00 26.56           N  
-ATOM    965  CA  TYR A 158       8.917  30.605  20.858  1.00 25.83           C  
-ATOM    966  C   TYR A 158       9.474  30.561  22.285  1.00 25.27           C  
-ATOM    967  O   TYR A 158      10.251  29.666  22.626  1.00 25.00           O  
-ATOM    968  CB  TYR A 158       7.925  29.454  20.684  1.00 23.89           C  
-ATOM    969  CG  TYR A 158       6.879  29.431  21.773  1.00 24.97           C  
-ATOM    970  CD1 TYR A 158       5.803  30.311  21.746  1.00 27.24           C  
-ATOM    971  CD2 TYR A 158       7.015  28.592  22.882  1.00 23.83           C  
-ATOM    972  CE1 TYR A 158       4.890  30.370  22.794  1.00 24.55           C  
-ATOM    973  CE2 TYR A 158       6.107  28.643  23.936  1.00 23.71           C  
-ATOM    974  CZ  TYR A 158       5.050  29.539  23.886  1.00 23.97           C  
-ATOM    975  OH  TYR A 158       4.165  29.633  24.937  1.00 22.36           O  
-ATOM    976  N   GLN A 159       9.077  31.532  23.105  1.00 24.93           N  
-ATOM    977  CA  GLN A 159       9.500  31.596  24.502  1.00 25.41           C  
-ATOM    978  C   GLN A 159       8.304  31.288  25.377  1.00 25.84           C  
-ATOM    979  O   GLN A 159       7.248  31.909  25.233  1.00 25.49           O  
-ATOM    980  CB  GLN A 159      10.039  32.982  24.852  1.00 27.26           C  
-ATOM    981  CG  GLN A 159      10.235  33.237  26.359  1.00 26.44           C  
-ATOM    982  CD  GLN A 159      11.079  32.175  27.060  1.00 26.38           C  
-ATOM    983  OE1 GLN A 159      11.982  31.584  26.467  1.00 25.41           O  
-ATOM    984  NE2 GLN A 159      10.797  31.950  28.340  1.00 25.28           N  
-ATOM    985  N   ALA A 160       8.472  30.331  26.284  1.00 24.60           N  
-ATOM    986  CA  ALA A 160       7.394  29.931  27.179  1.00 25.20           C  
-ATOM    987  C   ALA A 160       7.243  30.868  28.375  1.00 25.64           C  
-ATOM    988  O   ALA A 160       7.740  30.590  29.470  1.00 24.65           O  
-ATOM    989  CB  ALA A 160       7.618  28.493  27.659  1.00 24.54           C  
-ATOM    990  N   GLY A 161       6.549  31.979  28.147  1.00 26.49           N  
-ATOM    991  CA  GLY A 161       6.307  32.948  29.197  1.00 25.91           C  
-ATOM    992  C   GLY A 161       5.214  32.421  30.104  1.00 26.28           C  
-ATOM    993  O   GLY A 161       4.535  31.450  29.767  1.00 25.00           O  
-ATOM    994  N   SER A 162       5.026  33.067  31.248  1.00 25.89           N  
-ATOM    995  CA  SER A 162       4.030  32.617  32.204  1.00 26.53           C  
-ATOM    996  C   SER A 162       3.258  33.749  32.862  1.00 25.83           C  
-ATOM    997  O   SER A 162       3.767  34.857  33.008  1.00 25.37           O  
-ATOM    998  CB  SER A 162       4.717  31.785  33.284  1.00 26.39           C  
-ATOM    999  OG  SER A 162       3.839  31.538  34.364  1.00 27.42           O  
-ATOM   1000  N   SER A 163       2.025  33.453  33.265  1.00 27.26           N  
-ATOM   1001  CA  SER A 163       1.177  34.432  33.937  1.00 28.05           C  
-ATOM   1002  C   SER A 163       1.806  34.783  35.282  1.00 27.57           C  
-ATOM   1003  O   SER A 163       1.544  35.839  35.855  1.00 28.27           O  
-ATOM   1004  CB  SER A 163      -0.223  33.855  34.147  1.00 26.61           C  
-ATOM   1005  OG  SER A 163      -0.150  32.552  34.688  1.00 25.91           O  
-ATOM   1006  N   GLU A 164       2.647  33.884  35.774  1.00 27.91           N  
-ATOM   1007  CA  GLU A 164       3.334  34.088  37.035  1.00 28.07           C  
-ATOM   1008  C   GLU A 164       4.108  35.414  36.975  1.00 28.68           C  
-ATOM   1009  O   GLU A 164       4.350  36.048  38.002  1.00 28.52           O  
-ATOM   1010  CB  GLU A 164       4.281  32.909  37.282  1.00 29.68           C  
-ATOM   1011  CG  GLU A 164       4.625  32.634  38.732  1.00 31.17           C  
-ATOM   1012  CD  GLU A 164       3.460  32.095  39.533  1.00 31.96           C  
-ATOM   1013  OE1 GLU A 164       2.432  31.720  38.935  1.00 34.59           O  
-ATOM   1014  OE2 GLU A 164       3.576  32.035  40.770  1.00 30.97           O  
-ATOM   1015  N   MET A 165       4.484  35.841  35.770  1.00 27.52           N  
-ATOM   1016  CA  MET A 165       5.225  37.095  35.606  1.00 27.95           C  
-ATOM   1017  C   MET A 165       4.441  38.294  36.140  1.00 29.54           C  
-ATOM   1018  O   MET A 165       5.028  39.259  36.646  1.00 28.82           O  
-ATOM   1019  CB  MET A 165       5.570  37.339  34.132  1.00 25.88           C  
-ATOM   1020  CG  MET A 165       6.492  36.294  33.514  1.00 27.25           C  
-ATOM   1021  SD  MET A 165       6.948  36.666  31.804  1.00 29.52           S  
-ATOM   1022  CE  MET A 165       5.327  36.657  31.011  1.00 27.40           C  
-ATOM   1023  N   PHE A 166       3.117  38.227  36.019  1.00 29.06           N  
-ATOM   1024  CA  PHE A 166       2.246  39.297  36.480  1.00 29.99           C  
-ATOM   1025  C   PHE A 166       2.281  39.373  37.996  1.00 30.93           C  
-ATOM   1026  O   PHE A 166       2.077  40.435  38.579  1.00 31.18           O  
-ATOM   1027  CB  PHE A 166       0.812  39.056  35.995  1.00 29.19           C  
-ATOM   1028  CG  PHE A 166       0.668  39.093  34.501  1.00 27.72           C  
-ATOM   1029  CD1 PHE A 166       0.107  38.020  33.814  1.00 27.65           C  
-ATOM   1030  CD2 PHE A 166       1.117  40.196  33.773  1.00 27.31           C  
-ATOM   1031  CE1 PHE A 166      -0.005  38.040  32.417  1.00 27.77           C  
-ATOM   1032  CE2 PHE A 166       1.010  40.230  32.381  1.00 27.53           C  
-ATOM   1033  CZ  PHE A 166       0.449  39.150  31.702  1.00 28.96           C  
-ATOM   1034  N   GLY A 167       2.542  38.235  38.629  1.00 31.83           N  
-ATOM   1035  CA  GLY A 167       2.617  38.192  40.078  1.00 32.77           C  
-ATOM   1036  C   GLY A 167       1.409  38.761  40.798  1.00 32.95           C  
-ATOM   1037  O   GLY A 167       0.284  38.307  40.588  1.00 32.92           O  
-ATOM   1038  N   SER A 168       1.641  39.763  41.643  1.00 32.72           N  
-ATOM   1039  CA  SER A 168       0.567  40.377  42.416  1.00 33.67           C  
-ATOM   1040  C   SER A 168      -0.241  41.451  41.685  1.00 34.61           C  
-ATOM   1041  O   SER A 168      -1.212  41.966  42.233  1.00 37.09           O  
-ATOM   1042  CB  SER A 168       1.122  40.955  43.721  1.00 31.67           C  
-ATOM   1043  OG  SER A 168       2.057  41.983  43.459  1.00 33.41           O  
-ATOM   1044  N   THR A 169       0.151  41.803  40.463  1.00 35.60           N  
-ATOM   1045  CA  THR A 169      -0.611  42.796  39.706  1.00 35.80           C  
-ATOM   1046  C   THR A 169      -2.013  42.200  39.558  1.00 37.22           C  
-ATOM   1047  O   THR A 169      -2.173  41.106  39.024  1.00 38.10           O  
-ATOM   1048  CB  THR A 169      -0.012  43.028  38.307  1.00 34.90           C  
-ATOM   1049  OG1 THR A 169       1.349  43.466  38.429  1.00 33.01           O  
-ATOM   1050  CG2 THR A 169      -0.811  44.085  37.559  1.00 33.66           C  
-ATOM   1051  N   PRO A 170      -3.047  42.910  40.034  1.00 38.25           N  
-ATOM   1052  CA  PRO A 170      -4.432  42.425  39.954  1.00 38.35           C  
-ATOM   1053  C   PRO A 170      -4.986  42.225  38.542  1.00 38.55           C  
-ATOM   1054  O   PRO A 170      -4.581  42.907  37.602  1.00 39.59           O  
-ATOM   1055  CB  PRO A 170      -5.206  43.474  40.748  1.00 38.86           C  
-ATOM   1056  CG  PRO A 170      -4.435  44.726  40.475  1.00 38.66           C  
-ATOM   1057  CD  PRO A 170      -2.995  44.273  40.594  1.00 37.86           C  
-ATOM   1058  N   PRO A 171      -5.924  41.274  38.380  1.00 38.03           N  
-ATOM   1059  CA  PRO A 171      -6.549  40.963  37.090  1.00 38.74           C  
-ATOM   1060  C   PRO A 171      -7.591  41.998  36.663  1.00 39.93           C  
-ATOM   1061  O   PRO A 171      -7.968  42.866  37.452  1.00 40.73           O  
-ATOM   1062  CB  PRO A 171      -7.170  39.595  37.340  1.00 36.35           C  
-ATOM   1063  CG  PRO A 171      -7.597  39.702  38.758  1.00 37.57           C  
-ATOM   1064  CD  PRO A 171      -6.392  40.337  39.418  1.00 37.95           C  
-ATOM   1065  N   PRO A 172      -8.066  41.918  35.403  1.00 39.66           N  
-ATOM   1066  CA  PRO A 172      -7.657  40.912  34.413  1.00 37.98           C  
-ATOM   1067  C   PRO A 172      -6.270  41.239  33.884  1.00 36.40           C  
-ATOM   1068  O   PRO A 172      -5.906  42.407  33.791  1.00 38.10           O  
-ATOM   1069  CB  PRO A 172      -8.727  41.037  33.337  1.00 38.62           C  
-ATOM   1070  CG  PRO A 172      -9.013  42.510  33.350  1.00 38.60           C  
-ATOM   1071  CD  PRO A 172      -9.097  42.810  34.840  1.00 38.64           C  
-ATOM   1072  N   GLN A 173      -5.495  40.216  33.544  1.00 34.67           N  
-ATOM   1073  CA  GLN A 173      -4.149  40.440  33.036  1.00 31.73           C  
-ATOM   1074  C   GLN A 173      -4.048  40.142  31.549  1.00 31.23           C  
-ATOM   1075  O   GLN A 173      -4.408  39.056  31.104  1.00 30.37           O  
-ATOM   1076  CB  GLN A 173      -3.135  39.577  33.801  1.00 30.28           C  
-ATOM   1077  CG  GLN A 173      -2.977  39.939  35.265  1.00 27.34           C  
-ATOM   1078  CD  GLN A 173      -3.616  38.931  36.196  1.00 26.31           C  
-ATOM   1079  OE1 GLN A 173      -4.286  37.999  35.759  1.00 27.77           O  
-ATOM   1080  NE2 GLN A 173      -3.412  39.117  37.493  1.00 26.81           N  
-ATOM   1081  N   SER A 174      -3.556  41.114  30.788  1.00 31.02           N  
-ATOM   1082  CA  SER A 174      -3.389  40.959  29.349  1.00 31.98           C  
-ATOM   1083  C   SER A 174      -1.911  41.149  28.997  1.00 32.07           C  
-ATOM   1084  O   SER A 174      -1.091  41.391  29.879  1.00 33.92           O  
-ATOM   1085  CB  SER A 174      -4.253  41.977  28.599  1.00 31.30           C  
-ATOM   1086  OG  SER A 174      -3.877  43.305  28.921  1.00 34.07           O  
-ATOM   1087  N   GLU A 175      -1.578  41.044  27.713  1.00 31.37           N  
-ATOM   1088  CA  GLU A 175      -0.193  41.182  27.264  1.00 31.72           C  
-ATOM   1089  C   GLU A 175       0.596  42.334  27.878  1.00 31.87           C  
-ATOM   1090  O   GLU A 175       1.763  42.168  28.237  1.00 33.09           O  
-ATOM   1091  CB  GLU A 175      -0.127  41.337  25.740  1.00 31.92           C  
-ATOM   1092  CG  GLU A 175      -0.563  40.126  24.923  1.00 33.48           C  
-ATOM   1093  CD  GLU A 175      -2.065  39.897  24.942  1.00 34.26           C  
-ATOM   1094  OE1 GLU A 175      -2.817  40.859  25.205  1.00 35.52           O  
-ATOM   1095  OE2 GLU A 175      -2.494  38.754  24.674  1.00 35.98           O  
-ATOM   1096  N   THR A 176      -0.035  43.500  27.994  1.00 32.24           N  
-ATOM   1097  CA  THR A 176       0.643  44.683  28.515  1.00 30.61           C  
-ATOM   1098  C   THR A 176       0.586  44.913  30.021  1.00 29.36           C  
-ATOM   1099  O   THR A 176       1.232  45.823  30.524  1.00 29.02           O  
-ATOM   1100  CB  THR A 176       0.121  45.965  27.820  1.00 31.62           C  
-ATOM   1101  OG1 THR A 176      -1.257  46.172  28.161  1.00 33.15           O  
-ATOM   1102  CG2 THR A 176       0.246  45.840  26.310  1.00 32.74           C  
-ATOM   1103  N   THR A 177      -0.182  44.109  30.746  1.00 29.80           N  
-ATOM   1104  CA  THR A 177      -0.268  44.290  32.189  1.00 28.55           C  
-ATOM   1105  C   THR A 177       1.132  44.282  32.822  1.00 29.00           C  
-ATOM   1106  O   THR A 177       1.972  43.448  32.495  1.00 29.63           O  
-ATOM   1107  CB  THR A 177      -1.144  43.202  32.831  1.00 28.16           C  
-ATOM   1108  OG1 THR A 177      -2.453  43.241  32.242  1.00 30.95           O  
-ATOM   1109  CG2 THR A 177      -1.272  43.432  34.328  1.00 27.26           C  
-ATOM   1110  N   PRO A 178       1.401  45.230  33.729  1.00 28.77           N  
-ATOM   1111  CA  PRO A 178       2.708  45.310  34.386  1.00 30.42           C  
-ATOM   1112  C   PRO A 178       3.092  44.076  35.208  1.00 30.32           C  
-ATOM   1113  O   PRO A 178       2.249  43.472  35.879  1.00 30.14           O  
-ATOM   1114  CB  PRO A 178       2.587  46.575  35.242  1.00 31.23           C  
-ATOM   1115  CG  PRO A 178       1.124  46.634  35.560  1.00 33.01           C  
-ATOM   1116  CD  PRO A 178       0.501  46.288  34.222  1.00 31.40           C  
-ATOM   1117  N   PHE A 179       4.371  43.714  35.148  1.00 28.28           N  
-ATOM   1118  CA  PHE A 179       4.879  42.562  35.889  1.00 29.65           C  
-ATOM   1119  C   PHE A 179       5.278  42.939  37.311  1.00 29.52           C  
-ATOM   1120  O   PHE A 179       5.911  43.968  37.531  1.00 30.60           O  
-ATOM   1121  CB  PHE A 179       6.135  41.964  35.227  1.00 28.38           C  
-ATOM   1122  CG  PHE A 179       5.937  41.475  33.813  1.00 30.09           C  
-ATOM   1123  CD1 PHE A 179       4.732  40.916  33.404  1.00 29.90           C  
-ATOM   1124  CD2 PHE A 179       6.986  41.543  32.899  1.00 30.07           C  
-ATOM   1125  CE1 PHE A 179       4.577  40.434  32.105  1.00 31.46           C  
-ATOM   1126  CE2 PHE A 179       6.842  41.062  31.601  1.00 29.23           C  
-ATOM   1127  CZ  PHE A 179       5.638  40.508  31.203  1.00 31.13           C  
-ATOM   1128  N   HIS A 180       4.907  42.097  38.268  1.00 29.58           N  
-ATOM   1129  CA  HIS A 180       5.294  42.286  39.661  1.00 29.46           C  
-ATOM   1130  C   HIS A 180       5.537  40.881  40.207  1.00 29.15           C  
-ATOM   1131  O   HIS A 180       4.793  40.394  41.063  1.00 28.52           O  
-ATOM   1132  CB  HIS A 180       4.202  42.973  40.484  1.00 30.90           C  
-ATOM   1133  CG  HIS A 180       4.655  43.354  41.861  1.00 31.93           C  
-ATOM   1134  ND1 HIS A 180       4.887  44.661  42.235  1.00 32.73           N  
-ATOM   1135  CD2 HIS A 180       4.984  42.595  42.932  1.00 31.23           C  
-ATOM   1136  CE1 HIS A 180       5.340  44.688  43.476  1.00 31.38           C  
-ATOM   1137  NE2 HIS A 180       5.409  43.447  43.922  1.00 32.16           N  
-ATOM   1138  N   PRO A 181       6.587  40.207  39.706  1.00 28.56           N  
-ATOM   1139  CA  PRO A 181       6.945  38.849  40.123  1.00 28.38           C  
-ATOM   1140  C   PRO A 181       6.991  38.670  41.638  1.00 28.23           C  
-ATOM   1141  O   PRO A 181       7.409  39.567  42.367  1.00 29.38           O  
-ATOM   1142  CB  PRO A 181       8.298  38.624  39.443  1.00 27.42           C  
-ATOM   1143  CG  PRO A 181       8.845  40.001  39.297  1.00 26.28           C  
-ATOM   1144  CD  PRO A 181       7.644  40.778  38.854  1.00 27.91           C  
-ATOM   1145  N   ARG A 182       6.546  37.505  42.100  1.00 26.69           N  
-ATOM   1146  CA  ARG A 182       6.499  37.200  43.523  1.00 26.63           C  
-ATOM   1147  C   ARG A 182       7.384  36.024  43.925  1.00 26.78           C  
-ATOM   1148  O   ARG A 182       7.268  35.500  45.035  1.00 28.44           O  
-ATOM   1149  CB  ARG A 182       5.049  36.925  43.922  1.00 26.02           C  
-ATOM   1150  CG  ARG A 182       4.137  38.115  43.705  1.00 26.68           C  
-ATOM   1151  CD  ARG A 182       4.239  39.100  44.863  1.00 28.14           C  
-ATOM   1152  NE  ARG A 182       3.561  38.579  46.051  1.00 30.34           N  
-ATOM   1153  CZ  ARG A 182       3.568  39.167  47.243  1.00 30.06           C  
-ATOM   1154  NH1 ARG A 182       4.227  40.306  47.421  1.00 28.84           N  
-ATOM   1155  NH2 ARG A 182       2.903  38.621  48.256  1.00 28.79           N  
-ATOM   1156  N   SER A 183       8.267  35.615  43.019  1.00 26.39           N  
-ATOM   1157  CA  SER A 183       9.179  34.503  43.272  1.00 26.18           C  
-ATOM   1158  C   SER A 183      10.361  34.599  42.324  1.00 26.63           C  
-ATOM   1159  O   SER A 183      10.297  35.292  41.305  1.00 29.00           O  
-ATOM   1160  CB  SER A 183       8.479  33.164  43.036  1.00 26.67           C  
-ATOM   1161  OG  SER A 183       8.172  32.995  41.661  1.00 25.18           O  
-ATOM   1162  N   PRO A 184      11.465  33.910  42.651  1.00 25.38           N  
-ATOM   1163  CA  PRO A 184      12.649  33.938  41.791  1.00 23.93           C  
-ATOM   1164  C   PRO A 184      12.284  33.414  40.396  1.00 23.44           C  
-ATOM   1165  O   PRO A 184      12.718  33.951  39.380  1.00 24.41           O  
-ATOM   1166  CB  PRO A 184      13.621  33.018  42.522  1.00 24.95           C  
-ATOM   1167  CG  PRO A 184      13.245  33.225  43.967  1.00 25.64           C  
-ATOM   1168  CD  PRO A 184      11.742  33.193  43.910  1.00 23.94           C  
-ATOM   1169  N   TYR A 185      11.478  32.360  40.361  1.00 23.75           N  
-ATOM   1170  CA  TYR A 185      11.041  31.774  39.100  1.00 23.19           C  
-ATOM   1171  C   TYR A 185      10.359  32.820  38.212  1.00 25.01           C  
-ATOM   1172  O   TYR A 185      10.722  32.997  37.045  1.00 25.93           O  
-ATOM   1173  CB  TYR A 185      10.064  30.632  39.368  1.00 22.03           C  
-ATOM   1174  CG  TYR A 185       9.261  30.233  38.149  1.00 21.97           C  
-ATOM   1175  CD1 TYR A 185       9.784  29.358  37.195  1.00 21.12           C  
-ATOM   1176  CD2 TYR A 185       7.986  30.750  37.939  1.00 21.21           C  
-ATOM   1177  CE1 TYR A 185       9.049  29.009  36.062  1.00 22.16           C  
-ATOM   1178  CE2 TYR A 185       7.248  30.412  36.818  1.00 21.79           C  
-ATOM   1179  CZ  TYR A 185       7.777  29.543  35.881  1.00 22.48           C  
-ATOM   1180  OH  TYR A 185       7.033  29.213  34.769  1.00 21.36           O  
-ATOM   1181  N   ALA A 186       9.368  33.507  38.777  1.00 25.57           N  
-ATOM   1182  CA  ALA A 186       8.616  34.528  38.054  1.00 24.40           C  
-ATOM   1183  C   ALA A 186       9.500  35.671  37.576  1.00 23.83           C  
-ATOM   1184  O   ALA A 186       9.358  36.144  36.453  1.00 26.41           O  
-ATOM   1185  CB  ALA A 186       7.497  35.070  38.932  1.00 23.36           C  
-ATOM   1186  N   ALA A 187      10.407  36.122  38.430  1.00 23.06           N  
-ATOM   1187  CA  ALA A 187      11.294  37.204  38.053  1.00 22.05           C  
-ATOM   1188  C   ALA A 187      12.213  36.727  36.924  1.00 22.14           C  
-ATOM   1189  O   ALA A 187      12.560  37.498  36.036  1.00 20.68           O  
-ATOM   1190  CB  ALA A 187      12.108  37.658  39.256  1.00 24.38           C  
-ATOM   1191  N   SER A 188      12.600  35.455  36.959  1.00 21.69           N  
-ATOM   1192  CA  SER A 188      13.458  34.899  35.917  1.00 21.91           C  
-ATOM   1193  C   SER A 188      12.680  34.797  34.604  1.00 22.52           C  
-ATOM   1194  O   SER A 188      13.251  34.974  33.529  1.00 23.62           O  
-ATOM   1195  CB  SER A 188      13.983  33.524  36.329  1.00 21.37           C  
-ATOM   1196  OG  SER A 188      14.858  33.634  37.437  1.00 21.48           O  
-ATOM   1197  N   LYS A 189      11.386  34.498  34.689  1.00 22.14           N  
-ATOM   1198  CA  LYS A 189      10.561  34.428  33.489  1.00 22.88           C  
-ATOM   1199  C   LYS A 189      10.398  35.840  32.933  1.00 24.44           C  
-ATOM   1200  O   LYS A 189      10.363  36.032  31.720  1.00 25.68           O  
-ATOM   1201  CB  LYS A 189       9.179  33.838  33.789  1.00 22.45           C  
-ATOM   1202  CG  LYS A 189       9.122  32.315  33.817  1.00 23.30           C  
-ATOM   1203  CD  LYS A 189       9.498  31.693  32.473  1.00 20.48           C  
-ATOM   1204  CE  LYS A 189       9.342  30.177  32.522  1.00 20.67           C  
-ATOM   1205  NZ  LYS A 189       9.606  29.518  31.207  1.00 23.41           N  
-ATOM   1206  N   CYS A 190      10.293  36.825  33.825  1.00 24.52           N  
-ATOM   1207  CA  CYS A 190      10.158  38.219  33.405  1.00 25.21           C  
-ATOM   1208  C   CYS A 190      11.414  38.600  32.629  1.00 25.63           C  
-ATOM   1209  O   CYS A 190      11.344  39.297  31.611  1.00 26.48           O  
-ATOM   1210  CB  CYS A 190       9.997  39.152  34.618  1.00 23.61           C  
-ATOM   1211  SG  CYS A 190       8.404  39.040  35.486  1.00 25.06           S  
-ATOM   1212  N   ALA A 191      12.559  38.132  33.120  1.00 25.00           N  
-ATOM   1213  CA  ALA A 191      13.842  38.397  32.480  1.00 23.97           C  
-ATOM   1214  C   ALA A 191      13.880  37.746  31.102  1.00 23.25           C  
-ATOM   1215  O   ALA A 191      14.231  38.386  30.113  1.00 23.97           O  
-ATOM   1216  CB  ALA A 191      14.980  37.863  33.339  1.00 23.64           C  
-ATOM   1217  N   ALA A 192      13.526  36.469  31.041  1.00 22.37           N  
-ATOM   1218  CA  ALA A 192      13.519  35.745  29.775  1.00 23.91           C  
-ATOM   1219  C   ALA A 192      12.593  36.452  28.796  1.00 24.51           C  
-ATOM   1220  O   ALA A 192      12.881  36.537  27.606  1.00 24.55           O  
-ATOM   1221  CB  ALA A 192      13.049  34.314  29.990  1.00 21.71           C  
-ATOM   1222  N   HIS A 193      11.473  36.949  29.313  1.00 24.14           N  
-ATOM   1223  CA  HIS A 193      10.496  37.652  28.499  1.00 24.53           C  
-ATOM   1224  C   HIS A 193      11.144  38.826  27.775  1.00 24.42           C  
-ATOM   1225  O   HIS A 193      11.021  38.968  26.561  1.00 25.23           O  
-ATOM   1226  CB  HIS A 193       9.357  38.174  29.373  1.00 24.12           C  
-ATOM   1227  CG  HIS A 193       8.289  38.884  28.604  1.00 26.02           C  
-ATOM   1228  ND1 HIS A 193       7.210  38.229  28.049  1.00 25.71           N  
-ATOM   1229  CD2 HIS A 193       8.147  40.191  28.275  1.00 24.50           C  
-ATOM   1230  CE1 HIS A 193       6.449  39.102  27.414  1.00 24.06           C  
-ATOM   1231  NE2 HIS A 193       6.995  40.298  27.535  1.00 25.66           N  
-ATOM   1232  N   TRP A 194      11.832  39.669  28.533  1.00 24.58           N  
-ATOM   1233  CA  TRP A 194      12.484  40.838  27.964  1.00 24.97           C  
-ATOM   1234  C   TRP A 194      13.680  40.546  27.068  1.00 24.82           C  
-ATOM   1235  O   TRP A 194      13.926  41.270  26.103  1.00 25.04           O  
-ATOM   1236  CB  TRP A 194      12.857  41.803  29.080  1.00 27.84           C  
-ATOM   1237  CG  TRP A 194      11.653  42.535  29.549  1.00 31.74           C  
-ATOM   1238  CD1 TRP A 194      11.075  42.469  30.781  1.00 32.77           C  
-ATOM   1239  CD2 TRP A 194      10.829  43.400  28.761  1.00 31.80           C  
-ATOM   1240  NE1 TRP A 194       9.936  43.238  30.809  1.00 32.96           N  
-ATOM   1241  CE2 TRP A 194       9.762  43.821  29.581  1.00 33.96           C  
-ATOM   1242  CE3 TRP A 194      10.891  43.862  27.436  1.00 33.67           C  
-ATOM   1243  CZ2 TRP A 194       8.755  44.687  29.121  1.00 36.15           C  
-ATOM   1244  CZ3 TRP A 194       9.888  44.725  26.975  1.00 34.21           C  
-ATOM   1245  CH2 TRP A 194       8.836  45.126  27.820  1.00 36.25           C  
-ATOM   1246  N   TYR A 195      14.420  39.489  27.369  1.00 24.04           N  
-ATOM   1247  CA  TYR A 195      15.553  39.127  26.528  1.00 25.06           C  
-ATOM   1248  C   TYR A 195      14.975  38.784  25.148  1.00 27.35           C  
-ATOM   1249  O   TYR A 195      15.520  39.164  24.105  1.00 26.16           O  
-ATOM   1250  CB  TYR A 195      16.276  37.902  27.109  1.00 24.40           C  
-ATOM   1251  CG  TYR A 195      17.025  38.162  28.405  1.00 22.52           C  
-ATOM   1252  CD1 TYR A 195      17.064  37.199  29.417  1.00 23.80           C  
-ATOM   1253  CD2 TYR A 195      17.723  39.353  28.602  1.00 21.85           C  
-ATOM   1254  CE1 TYR A 195      17.783  37.418  30.591  1.00 21.67           C  
-ATOM   1255  CE2 TYR A 195      18.443  39.584  29.764  1.00 20.34           C  
-ATOM   1256  CZ  TYR A 195      18.472  38.616  30.755  1.00 22.12           C  
-ATOM   1257  OH  TYR A 195      19.201  38.845  31.898  1.00 21.47           O  
-ATOM   1258  N   THR A 196      13.851  38.072  25.172  1.00 26.91           N  
-ATOM   1259  CA  THR A 196      13.157  37.632  23.971  1.00 28.00           C  
-ATOM   1260  C   THR A 196      12.598  38.811  23.177  1.00 29.20           C  
-ATOM   1261  O   THR A 196      12.767  38.877  21.958  1.00 30.71           O  
-ATOM   1262  CB  THR A 196      12.013  36.670  24.337  1.00 25.84           C  
-ATOM   1263  OG1 THR A 196      12.549  35.558  25.063  1.00 31.83           O  
-ATOM   1264  CG2 THR A 196      11.318  36.157  23.088  1.00 25.67           C  
-ATOM   1265  N   VAL A 197      11.930  39.734  23.862  1.00 27.31           N  
-ATOM   1266  CA  VAL A 197      11.384  40.911  23.201  1.00 26.84           C  
-ATOM   1267  C   VAL A 197      12.521  41.741  22.609  1.00 27.22           C  
-ATOM   1268  O   VAL A 197      12.406  42.267  21.503  1.00 28.58           O  
-ATOM   1269  CB  VAL A 197      10.590  41.806  24.182  1.00 25.64           C  
-ATOM   1270  CG1 VAL A 197      10.234  43.130  23.507  1.00 25.99           C  
-ATOM   1271  CG2 VAL A 197       9.326  41.101  24.626  1.00 24.41           C  
-ATOM   1272  N   ASN A 198      13.619  41.843  23.351  1.00 28.12           N  
-ATOM   1273  CA  ASN A 198      14.781  42.614  22.925  1.00 28.16           C  
-ATOM   1274  C   ASN A 198      15.443  42.061  21.662  1.00 28.46           C  
-ATOM   1275  O   ASN A 198      15.872  42.824  20.799  1.00 28.00           O  
-ATOM   1276  CB  ASN A 198      15.814  42.670  24.051  1.00 28.98           C  
-ATOM   1277  CG  ASN A 198      16.945  43.633  23.759  1.00 26.05           C  
-ATOM   1278  OD1 ASN A 198      18.114  43.309  23.950  1.00 29.36           O  
-ATOM   1279  ND2 ASN A 198      16.601  44.830  23.303  1.00 28.99           N  
-ATOM   1280  N   TYR A 199      15.545  40.740  21.554  1.00 28.12           N  
-ATOM   1281  CA  TYR A 199      16.158  40.154  20.371  1.00 28.10           C  
-ATOM   1282  C   TYR A 199      15.278  40.381  19.148  1.00 28.59           C  
-ATOM   1283  O   TYR A 199      15.765  40.443  18.018  1.00 28.36           O  
-ATOM   1284  CB  TYR A 199      16.435  38.660  20.588  1.00 28.45           C  
-ATOM   1285  CG  TYR A 199      17.839  38.401  21.093  1.00 28.26           C  
-ATOM   1286  CD1 TYR A 199      18.339  39.091  22.194  1.00 30.03           C  
-ATOM   1287  CD2 TYR A 199      18.690  37.522  20.430  1.00 30.33           C  
-ATOM   1288  CE1 TYR A 199      19.647  38.920  22.615  1.00 30.54           C  
-ATOM   1289  CE2 TYR A 199      20.002  37.343  20.841  1.00 28.41           C  
-ATOM   1290  CZ  TYR A 199      20.474  38.048  21.932  1.00 31.14           C  
-ATOM   1291  OH  TYR A 199      21.784  37.911  22.323  1.00 31.94           O  
-ATOM   1292  N   ARG A 200      13.980  40.517  19.383  1.00 30.68           N  
-ATOM   1293  CA  ARG A 200      13.031  40.773  18.309  1.00 31.05           C  
-ATOM   1294  C   ARG A 200      13.217  42.216  17.831  1.00 31.90           C  
-ATOM   1295  O   ARG A 200      13.427  42.471  16.647  1.00 32.02           O  
-ATOM   1296  CB  ARG A 200      11.604  40.574  18.819  1.00 32.05           C  
-ATOM   1297  CG  ARG A 200      10.517  40.863  17.791  1.00 32.35           C  
-ATOM   1298  CD  ARG A 200       9.151  40.439  18.316  1.00 30.82           C  
-ATOM   1299  NE  ARG A 200       8.698  41.270  19.427  1.00 30.24           N  
-ATOM   1300  CZ  ARG A 200       8.003  40.812  20.462  1.00 29.54           C  
-ATOM   1301  NH1 ARG A 200       7.686  39.526  20.535  1.00 30.13           N  
-ATOM   1302  NH2 ARG A 200       7.612  41.640  21.420  1.00 27.46           N  
-ATOM   1303  N   GLU A 201      13.159  43.154  18.770  1.00 30.37           N  
-ATOM   1304  CA  GLU A 201      13.308  44.566  18.455  1.00 30.31           C  
-ATOM   1305  C   GLU A 201      14.706  44.963  17.985  1.00 31.48           C  
-ATOM   1306  O   GLU A 201      14.852  45.820  17.114  1.00 34.88           O  
-ATOM   1307  CB  GLU A 201      12.922  45.413  19.671  1.00 30.21           C  
-ATOM   1308  CG  GLU A 201      11.480  45.226  20.116  1.00 29.18           C  
-ATOM   1309  CD  GLU A 201      11.095  46.124  21.276  1.00 28.11           C  
-ATOM   1310  OE1 GLU A 201       9.920  46.079  21.690  1.00 29.91           O  
-ATOM   1311  OE2 GLU A 201      11.959  46.877  21.775  1.00 30.81           O  
-ATOM   1312  N   ALA A 202      15.736  44.344  18.546  1.00 30.46           N  
-ATOM   1313  CA  ALA A 202      17.094  44.687  18.160  1.00 30.50           C  
-ATOM   1314  C   ALA A 202      17.574  44.006  16.888  1.00 31.87           C  
-ATOM   1315  O   ALA A 202      18.213  44.637  16.051  1.00 32.00           O  
-ATOM   1316  CB  ALA A 202      18.054  44.378  19.296  1.00 30.72           C  
-ATOM   1317  N   TYR A 203      17.263  42.725  16.731  1.00 32.07           N  
-ATOM   1318  CA  TYR A 203      17.730  41.994  15.560  1.00 31.57           C  
-ATOM   1319  C   TYR A 203      16.647  41.552  14.589  1.00 32.16           C  
-ATOM   1320  O   TYR A 203      16.941  40.904  13.583  1.00 33.77           O  
-ATOM   1321  CB  TYR A 203      18.534  40.769  16.003  1.00 30.94           C  
-ATOM   1322  CG  TYR A 203      19.633  41.083  16.994  1.00 30.96           C  
-ATOM   1323  CD1 TYR A 203      19.551  40.648  18.317  1.00 30.53           C  
-ATOM   1324  CD2 TYR A 203      20.758  41.808  16.609  1.00 30.88           C  
-ATOM   1325  CE1 TYR A 203      20.565  40.924  19.232  1.00 30.19           C  
-ATOM   1326  CE2 TYR A 203      21.778  42.091  17.517  1.00 31.41           C  
-ATOM   1327  CZ  TYR A 203      21.675  41.643  18.824  1.00 30.11           C  
-ATOM   1328  OH  TYR A 203      22.689  41.900  19.712  1.00 32.21           O  
-ATOM   1329  N   GLY A 204      15.399  41.893  14.881  1.00 32.81           N  
-ATOM   1330  CA  GLY A 204      14.322  41.499  13.992  1.00 33.81           C  
-ATOM   1331  C   GLY A 204      14.078  40.000  13.973  1.00 34.53           C  
-ATOM   1332  O   GLY A 204      13.440  39.482  13.057  1.00 36.00           O  
-ATOM   1333  N   LEU A 205      14.589  39.296  14.978  1.00 33.56           N  
-ATOM   1334  CA  LEU A 205      14.394  37.852  15.069  1.00 33.05           C  
-ATOM   1335  C   LEU A 205      12.915  37.580  15.282  1.00 31.69           C  
-ATOM   1336  O   LEU A 205      12.244  38.300  16.021  1.00 31.29           O  
-ATOM   1337  CB  LEU A 205      15.189  37.268  16.248  1.00 34.01           C  
-ATOM   1338  CG  LEU A 205      14.912  35.804  16.616  1.00 34.41           C  
-ATOM   1339  CD1 LEU A 205      15.372  34.894  15.494  1.00 34.36           C  
-ATOM   1340  CD2 LEU A 205      15.635  35.451  17.911  1.00 35.92           C  
-ATOM   1341  N   PHE A 206      12.405  36.542  14.634  1.00 30.87           N  
-ATOM   1342  CA  PHE A 206      10.999  36.193  14.777  1.00 30.53           C  
-ATOM   1343  C   PHE A 206      10.837  35.456  16.099  1.00 29.69           C  
-ATOM   1344  O   PHE A 206      10.839  34.226  16.141  1.00 28.12           O  
-ATOM   1345  CB  PHE A 206      10.562  35.301  13.617  1.00 32.33           C  
-ATOM   1346  CG  PHE A 206       9.076  35.154  13.492  1.00 31.94           C  
-ATOM   1347  CD1 PHE A 206       8.355  34.411  14.421  1.00 32.44           C  
-ATOM   1348  CD2 PHE A 206       8.396  35.753  12.436  1.00 32.85           C  
-ATOM   1349  CE1 PHE A 206       6.977  34.263  14.300  1.00 33.20           C  
-ATOM   1350  CE2 PHE A 206       7.014  35.612  12.306  1.00 34.00           C  
-ATOM   1351  CZ  PHE A 206       6.304  34.865  13.239  1.00 33.77           C  
-ATOM   1352  N   ALA A 207      10.709  36.218  17.180  1.00 30.01           N  
-ATOM   1353  CA  ALA A 207      10.566  35.638  18.508  1.00 29.71           C  
-ATOM   1354  C   ALA A 207       9.262  36.070  19.151  1.00 29.34           C  
-ATOM   1355  O   ALA A 207       8.966  37.257  19.234  1.00 30.58           O  
-ATOM   1356  CB  ALA A 207      11.741  36.048  19.380  1.00 29.57           C  
-ATOM   1357  N   CYS A 208       8.481  35.099  19.603  1.00 29.17           N  
-ATOM   1358  CA  CYS A 208       7.205  35.392  20.237  1.00 29.35           C  
-ATOM   1359  C   CYS A 208       7.235  34.959  21.688  1.00 27.51           C  
-ATOM   1360  O   CYS A 208       7.916  34.000  22.045  1.00 29.35           O  
-ATOM   1361  CB  CYS A 208       6.066  34.642  19.537  1.00 29.10           C  
-ATOM   1362  SG  CYS A 208       5.931  34.925  17.761  1.00 35.30           S  
-ATOM   1363  N   ASN A 209       6.496  35.673  22.524  1.00 28.15           N  
-ATOM   1364  CA  ASN A 209       6.396  35.322  23.927  1.00 28.45           C  
-ATOM   1365  C   ASN A 209       4.987  34.802  24.171  1.00 28.81           C  
-ATOM   1366  O   ASN A 209       4.011  35.539  24.033  1.00 29.49           O  
-ATOM   1367  CB  ASN A 209       6.641  36.536  24.823  1.00 26.79           C  
-ATOM   1368  CG  ASN A 209       8.107  36.867  24.967  1.00 28.39           C  
-ATOM   1369  OD1 ASN A 209       8.883  36.083  25.522  1.00 25.71           O  
-ATOM   1370  ND2 ASN A 209       8.502  38.036  24.465  1.00 29.18           N  
-ATOM   1371  N   GLY A 210       4.885  33.521  24.503  1.00 27.91           N  
-ATOM   1372  CA  GLY A 210       3.592  32.950  24.806  1.00 27.04           C  
-ATOM   1373  C   GLY A 210       3.404  33.163  26.297  1.00 27.15           C  
-ATOM   1374  O   GLY A 210       4.105  32.556  27.102  1.00 27.33           O  
-ATOM   1375  N   ILE A 211       2.489  34.052  26.668  1.00 27.85           N  
-ATOM   1376  CA  ILE A 211       2.230  34.332  28.072  1.00 25.71           C  
-ATOM   1377  C   ILE A 211       1.086  33.425  28.481  1.00 26.48           C  
-ATOM   1378  O   ILE A 211      -0.081  33.830  28.486  1.00 25.43           O  
-ATOM   1379  CB  ILE A 211       1.840  35.814  28.292  1.00 25.48           C  
-ATOM   1380  CG1 ILE A 211       2.918  36.725  27.704  1.00 24.85           C  
-ATOM   1381  CG2 ILE A 211       1.681  36.101  29.782  1.00 23.38           C  
-ATOM   1382  CD1 ILE A 211       2.685  38.210  27.947  1.00 27.21           C  
-ATOM   1383  N   LEU A 212       1.435  32.185  28.811  1.00 26.51           N  
-ATOM   1384  CA  LEU A 212       0.453  31.189  29.195  1.00 26.34           C  
-ATOM   1385  C   LEU A 212       0.126  31.147  30.677  1.00 26.59           C  
-ATOM   1386  O   LEU A 212       1.004  31.224  31.537  1.00 26.31           O  
-ATOM   1387  CB  LEU A 212       0.907  29.799  28.732  1.00 24.37           C  
-ATOM   1388  CG  LEU A 212       0.613  29.428  27.270  1.00 25.83           C  
-ATOM   1389  CD1 LEU A 212       1.213  30.462  26.330  1.00 25.20           C  
-ATOM   1390  CD2 LEU A 212       1.167  28.043  26.977  1.00 23.47           C  
-ATOM   1391  N   PHE A 213      -1.163  31.038  30.963  1.00 27.03           N  
-ATOM   1392  CA  PHE A 213      -1.618  30.937  32.331  1.00 24.93           C  
-ATOM   1393  C   PHE A 213      -1.578  29.454  32.657  1.00 25.29           C  
-ATOM   1394  O   PHE A 213      -1.320  28.631  31.771  1.00 24.11           O  
-ATOM   1395  CB  PHE A 213      -3.026  31.513  32.459  1.00 23.81           C  
-ATOM   1396  CG  PHE A 213      -3.042  33.012  32.526  1.00 24.98           C  
-ATOM   1397  CD1 PHE A 213      -2.488  33.772  31.497  1.00 25.14           C  
-ATOM   1398  CD2 PHE A 213      -3.547  33.665  33.644  1.00 23.15           C  
-ATOM   1399  CE1 PHE A 213      -2.430  35.156  31.586  1.00 23.83           C  
-ATOM   1400  CE2 PHE A 213      -3.496  35.048  33.742  1.00 22.62           C  
-ATOM   1401  CZ  PHE A 213      -2.935  35.796  32.714  1.00 23.30           C  
-ATOM   1402  N   ASN A 214      -1.815  29.115  33.919  1.00 23.78           N  
-ATOM   1403  CA  ASN A 214      -1.769  27.726  34.356  1.00 25.90           C  
-ATOM   1404  C   ASN A 214      -2.512  26.759  33.439  1.00 27.10           C  
-ATOM   1405  O   ASN A 214      -3.657  27.004  33.053  1.00 28.44           O  
-ATOM   1406  CB  ASN A 214      -2.343  27.591  35.774  1.00 25.90           C  
-ATOM   1407  CG  ASN A 214      -1.546  28.361  36.817  1.00 26.39           C  
-ATOM   1408  OD1 ASN A 214      -1.360  29.576  36.707  1.00 26.56           O  
-ATOM   1409  ND2 ASN A 214      -1.080  27.656  37.844  1.00 26.61           N  
-ATOM   1410  N   HIS A 215      -1.845  25.668  33.077  1.00 27.33           N  
-ATOM   1411  CA  HIS A 215      -2.469  24.633  32.265  1.00 25.84           C  
-ATOM   1412  C   HIS A 215      -2.011  23.272  32.765  1.00 26.67           C  
-ATOM   1413  O   HIS A 215      -0.818  23.038  32.991  1.00 26.51           O  
-ATOM   1414  CB  HIS A 215      -2.186  24.807  30.762  1.00 23.54           C  
-ATOM   1415  CG  HIS A 215      -0.767  25.135  30.427  1.00 22.55           C  
-ATOM   1416  ND1 HIS A 215      -0.233  26.392  30.600  1.00 22.07           N  
-ATOM   1417  CD2 HIS A 215       0.211  24.385  29.870  1.00 21.15           C  
-ATOM   1418  CE1 HIS A 215       1.012  26.404  30.159  1.00 20.85           C  
-ATOM   1419  NE2 HIS A 215       1.305  25.197  29.711  1.00 22.80           N  
-ATOM   1420  N   GLU A 216      -2.986  22.389  32.952  1.00 27.17           N  
-ATOM   1421  CA  GLU A 216      -2.757  21.056  33.482  1.00 28.47           C  
-ATOM   1422  C   GLU A 216      -3.160  19.943  32.514  1.00 28.64           C  
-ATOM   1423  O   GLU A 216      -3.619  20.193  31.400  1.00 29.81           O  
-ATOM   1424  CB  GLU A 216      -3.548  20.894  34.788  1.00 29.18           C  
-ATOM   1425  CG  GLU A 216      -3.848  22.209  35.515  1.00 29.30           C  
-ATOM   1426  CD  GLU A 216      -2.600  22.877  36.069  1.00 27.46           C  
-ATOM   1427  OE1 GLU A 216      -2.307  24.025  35.683  1.00 26.83           O  
-ATOM   1428  OE2 GLU A 216      -1.909  22.254  36.896  1.00 30.84           O  
-ATOM   1429  N   SER A 217      -2.993  18.707  32.971  1.00 28.49           N  
-ATOM   1430  CA  SER A 217      -3.317  17.529  32.182  1.00 27.67           C  
-ATOM   1431  C   SER A 217      -2.973  16.304  33.018  1.00 27.68           C  
-ATOM   1432  O   SER A 217      -2.414  16.423  34.107  1.00 27.18           O  
-ATOM   1433  CB  SER A 217      -2.479  17.509  30.903  1.00 28.58           C  
-ATOM   1434  OG  SER A 217      -1.116  17.256  31.205  1.00 28.53           O  
-ATOM   1435  N   PRO A 218      -3.315  15.107  32.526  1.00 28.70           N  
-ATOM   1436  CA  PRO A 218      -2.995  13.897  33.293  1.00 27.99           C  
-ATOM   1437  C   PRO A 218      -1.479  13.676  33.373  1.00 28.15           C  
-ATOM   1438  O   PRO A 218      -1.013  12.816  34.111  1.00 27.96           O  
-ATOM   1439  CB  PRO A 218      -3.701  12.792  32.504  1.00 28.67           C  
-ATOM   1440  CG  PRO A 218      -4.882  13.524  31.880  1.00 27.24           C  
-ATOM   1441  CD  PRO A 218      -4.231  14.801  31.411  1.00 27.43           C  
-ATOM   1442  N   ARG A 219      -0.722  14.463  32.610  1.00 28.57           N  
-ATOM   1443  CA  ARG A 219       0.738  14.360  32.577  1.00 28.57           C  
-ATOM   1444  C   ARG A 219       1.398  15.437  33.428  1.00 27.96           C  
-ATOM   1445  O   ARG A 219       2.617  15.551  33.456  1.00 28.13           O  
-ATOM   1446  CB  ARG A 219       1.249  14.508  31.141  1.00 29.34           C  
-ATOM   1447  CG  ARG A 219       0.629  13.545  30.141  1.00 30.70           C  
-ATOM   1448  CD  ARG A 219       1.186  13.775  28.741  1.00 28.58           C  
-ATOM   1449  NE  ARG A 219       0.393  13.081  27.732  1.00 27.95           N  
-ATOM   1450  CZ  ARG A 219       0.592  13.182  26.423  1.00 29.61           C  
-ATOM   1451  NH1 ARG A 219      -0.188  12.511  25.584  1.00 28.54           N  
-ATOM   1452  NH2 ARG A 219       1.569  13.950  25.950  1.00 23.96           N  
-ATOM   1453  N   ARG A 220       0.584  16.241  34.099  1.00 28.55           N  
-ATOM   1454  CA  ARG A 220       1.081  17.320  34.943  1.00 27.51           C  
-ATOM   1455  C   ARG A 220       1.993  16.787  36.046  1.00 26.58           C  
-ATOM   1456  O   ARG A 220       1.808  15.672  36.524  1.00 24.69           O  
-ATOM   1457  CB  ARG A 220      -0.106  18.065  35.556  1.00 26.94           C  
-ATOM   1458  CG  ARG A 220       0.252  19.243  36.445  1.00 26.00           C  
-ATOM   1459  CD  ARG A 220       1.105  20.274  35.731  1.00 24.26           C  
-ATOM   1460  NE  ARG A 220       0.759  21.631  36.143  1.00 22.35           N  
-ATOM   1461  CZ  ARG A 220       1.573  22.678  36.047  1.00 22.84           C  
-ATOM   1462  NH1 ARG A 220       2.792  22.529  35.559  1.00 25.05           N  
-ATOM   1463  NH2 ARG A 220       1.158  23.879  36.420  1.00 22.76           N  
-ATOM   1464  N   GLY A 221       2.984  17.586  36.432  1.00 26.76           N  
-ATOM   1465  CA  GLY A 221       3.894  17.174  37.487  1.00 25.70           C  
-ATOM   1466  C   GLY A 221       3.114  16.981  38.773  1.00 26.68           C  
-ATOM   1467  O   GLY A 221       2.270  17.805  39.118  1.00 26.28           O  
-ATOM   1468  N   GLU A 222       3.398  15.896  39.486  1.00 28.38           N  
-ATOM   1469  CA  GLU A 222       2.695  15.587  40.725  1.00 31.05           C  
-ATOM   1470  C   GLU A 222       2.923  16.557  41.881  1.00 31.56           C  
-ATOM   1471  O   GLU A 222       2.204  16.515  42.876  1.00 31.60           O  
-ATOM   1472  CB  GLU A 222       3.026  14.152  41.152  1.00 32.52           C  
-ATOM   1473  CG  GLU A 222       2.367  13.118  40.245  1.00 35.47           C  
-ATOM   1474  CD  GLU A 222       2.676  11.683  40.628  1.00 37.97           C  
-ATOM   1475  OE1 GLU A 222       2.587  11.347  41.832  1.00 38.47           O  
-ATOM   1476  OE2 GLU A 222       2.990  10.889  39.716  1.00 36.81           O  
-ATOM   1477  N   ASN A 223       3.907  17.439  41.741  1.00 32.66           N  
-ATOM   1478  CA  ASN A 223       4.208  18.419  42.778  1.00 31.84           C  
-ATOM   1479  C   ASN A 223       3.404  19.699  42.586  1.00 30.27           C  
-ATOM   1480  O   ASN A 223       3.480  20.617  43.396  1.00 29.68           O  
-ATOM   1481  CB  ASN A 223       5.701  18.732  42.775  1.00 36.31           C  
-ATOM   1482  CG  ASN A 223       6.539  17.543  43.195  1.00 41.40           C  
-ATOM   1483  OD1 ASN A 223       7.688  17.392  42.766  1.00 43.95           O  
-ATOM   1484  ND2 ASN A 223       5.972  16.693  44.049  1.00 40.80           N  
-ATOM   1485  N   PHE A 224       2.643  19.767  41.501  1.00 28.66           N  
-ATOM   1486  CA  PHE A 224       1.806  20.932  41.256  1.00 26.88           C  
-ATOM   1487  C   PHE A 224       0.456  20.629  41.891  1.00 26.02           C  
-ATOM   1488  O   PHE A 224       0.009  19.479  41.912  1.00 26.33           O  
-ATOM   1489  CB  PHE A 224       1.690  21.209  39.756  1.00 24.86           C  
-ATOM   1490  CG  PHE A 224       2.983  21.640  39.137  1.00 24.92           C  
-ATOM   1491  CD1 PHE A 224       3.846  20.706  38.570  1.00 24.82           C  
-ATOM   1492  CD2 PHE A 224       3.385  22.970  39.198  1.00 24.24           C  
-ATOM   1493  CE1 PHE A 224       5.088  21.092  38.080  1.00 21.87           C  
-ATOM   1494  CE2 PHE A 224       4.632  23.364  38.710  1.00 21.15           C  
-ATOM   1495  CZ  PHE A 224       5.481  22.425  38.153  1.00 22.68           C  
-ATOM   1496  N   VAL A 225      -0.185  21.668  42.408  1.00 27.22           N  
-ATOM   1497  CA  VAL A 225      -1.439  21.520  43.127  1.00 26.94           C  
-ATOM   1498  C   VAL A 225      -2.560  20.716  42.477  1.00 27.83           C  
-ATOM   1499  O   VAL A 225      -3.143  19.850  43.132  1.00 29.00           O  
-ATOM   1500  CB  VAL A 225      -1.967  22.908  43.582  1.00 28.41           C  
-ATOM   1501  CG1 VAL A 225      -2.672  23.616  42.445  1.00 28.66           C  
-ATOM   1502  CG2 VAL A 225      -2.874  22.742  44.794  1.00 28.76           C  
-ATOM   1503  N   THR A 226      -2.864  20.969  41.204  1.00 27.87           N  
-ATOM   1504  CA  THR A 226      -3.941  20.229  40.550  1.00 25.74           C  
-ATOM   1505  C   THR A 226      -3.659  18.726  40.487  1.00 27.03           C  
-ATOM   1506  O   THR A 226      -4.481  17.917  40.916  1.00 28.38           O  
-ATOM   1507  CB  THR A 226      -4.224  20.755  39.114  1.00 25.17           C  
-ATOM   1508  OG1 THR A 226      -3.076  20.551  38.279  1.00 27.03           O  
-ATOM   1509  CG2 THR A 226      -4.570  22.231  39.148  1.00 18.38           C  
-ATOM   1510  N   ARG A 227      -2.497  18.351  39.965  1.00 27.70           N  
-ATOM   1511  CA  ARG A 227      -2.143  16.940  39.855  1.00 29.52           C  
-ATOM   1512  C   ARG A 227      -1.959  16.322  41.240  1.00 31.09           C  
-ATOM   1513  O   ARG A 227      -2.280  15.157  41.460  1.00 31.55           O  
-ATOM   1514  CB  ARG A 227      -0.855  16.773  39.038  1.00 29.17           C  
-ATOM   1515  CG  ARG A 227      -0.496  15.328  38.739  1.00 27.80           C  
-ATOM   1516  CD  ARG A 227      -1.488  14.710  37.761  1.00 25.69           C  
-ATOM   1517  NE  ARG A 227      -1.396  13.254  37.725  1.00 25.64           N  
-ATOM   1518  CZ  ARG A 227      -0.356  12.566  37.256  1.00 29.43           C  
-ATOM   1519  NH1 ARG A 227       0.707  13.195  36.763  1.00 27.46           N  
-ATOM   1520  NH2 ARG A 227      -0.375  11.239  37.298  1.00 27.92           N  
-ATOM   1521  N   LYS A 228      -1.439  17.108  42.175  1.00 31.92           N  
-ATOM   1522  CA  LYS A 228      -1.232  16.619  43.529  1.00 31.48           C  
-ATOM   1523  C   LYS A 228      -2.580  16.185  44.085  1.00 30.86           C  
-ATOM   1524  O   LYS A 228      -2.706  15.107  44.660  1.00 32.19           O  
-ATOM   1525  CB  LYS A 228      -0.635  17.724  44.410  1.00 31.90           C  
-ATOM   1526  CG  LYS A 228      -0.359  17.297  45.851  1.00 33.16           C  
-ATOM   1527  CD  LYS A 228       0.249  18.429  46.661  1.00 33.73           C  
-ATOM   1528  CE  LYS A 228       0.542  18.014  48.092  1.00 34.69           C  
-ATOM   1529  NZ  LYS A 228       1.261  19.098  48.832  1.00 33.60           N  
-ATOM   1530  N   ILE A 229      -3.584  17.036  43.891  1.00 30.48           N  
-ATOM   1531  CA  ILE A 229      -4.938  16.777  44.366  1.00 29.50           C  
-ATOM   1532  C   ILE A 229      -5.599  15.570  43.699  1.00 30.87           C  
-ATOM   1533  O   ILE A 229      -6.129  14.697  44.380  1.00 32.34           O  
-ATOM   1534  CB  ILE A 229      -5.834  18.026  44.163  1.00 28.08           C  
-ATOM   1535  CG1 ILE A 229      -5.341  19.160  45.062  1.00 26.65           C  
-ATOM   1536  CG2 ILE A 229      -7.288  17.696  44.476  1.00 30.12           C  
-ATOM   1537  CD1 ILE A 229      -6.229  20.372  45.075  1.00 24.34           C  
-ATOM   1538  N   THR A 230      -5.567  15.510  42.373  1.00 30.58           N  
-ATOM   1539  CA  THR A 230      -6.197  14.396  41.677  1.00 30.91           C  
-ATOM   1540  C   THR A 230      -5.475  13.076  41.913  1.00 32.07           C  
-ATOM   1541  O   THR A 230      -6.103  12.017  41.960  1.00 32.68           O  
-ATOM   1542  CB  THR A 230      -6.279  14.649  40.166  1.00 29.06           C  
-ATOM   1543  OG1 THR A 230      -4.962  14.781  39.629  1.00 29.52           O  
-ATOM   1544  CG2 THR A 230      -7.066  15.906  39.885  1.00 28.87           C  
-ATOM   1545  N   ARG A 231      -4.157  13.137  42.060  1.00 32.26           N  
-ATOM   1546  CA  ARG A 231      -3.378  11.934  42.300  1.00 31.13           C  
-ATOM   1547  C   ARG A 231      -3.734  11.382  43.675  1.00 31.78           C  
-ATOM   1548  O   ARG A 231      -3.915  10.173  43.849  1.00 30.23           O  
-ATOM   1549  CB  ARG A 231      -1.885  12.249  42.259  1.00 30.88           C  
-ATOM   1550  CG  ARG A 231      -0.996  11.019  42.254  1.00 31.03           C  
-ATOM   1551  CD  ARG A 231      -1.000  10.356  40.884  1.00 34.92           C  
-ATOM   1552  NE  ARG A 231       0.063   9.366  40.760  1.00 35.21           N  
-ATOM   1553  CZ  ARG A 231      -0.003   8.125  41.229  1.00 37.27           C  
-ATOM   1554  NH1 ARG A 231      -1.093   7.698  41.855  1.00 38.15           N  
-ATOM   1555  NH2 ARG A 231       1.035   7.315  41.087  1.00 37.32           N  
-ATOM   1556  N   ALA A 232      -3.827  12.280  44.651  1.00 31.97           N  
-ATOM   1557  CA  ALA A 232      -4.158  11.896  46.019  1.00 32.33           C  
-ATOM   1558  C   ALA A 232      -5.591  11.383  46.076  1.00 33.79           C  
-ATOM   1559  O   ALA A 232      -5.859  10.328  46.652  1.00 34.43           O  
-ATOM   1560  CB  ALA A 232      -3.986  13.087  46.955  1.00 28.49           C  
-ATOM   1561  N   LEU A 233      -6.508  12.134  45.470  1.00 33.98           N  
-ATOM   1562  CA  LEU A 233      -7.916  11.754  45.444  1.00 34.82           C  
-ATOM   1563  C   LEU A 233      -8.096  10.316  44.968  1.00 35.66           C  
-ATOM   1564  O   LEU A 233      -8.840   9.541  45.571  1.00 36.20           O  
-ATOM   1565  CB  LEU A 233      -8.698  12.695  44.528  1.00 34.94           C  
-ATOM   1566  CG  LEU A 233     -10.157  12.320  44.270  1.00 35.45           C  
-ATOM   1567  CD1 LEU A 233     -10.924  12.243  45.589  1.00 34.13           C  
-ATOM   1568  CD2 LEU A 233     -10.774  13.349  43.343  1.00 35.40           C  
-ATOM   1569  N   GLY A 234      -7.417   9.967  43.882  1.00 34.40           N  
-ATOM   1570  CA  GLY A 234      -7.523   8.620  43.358  1.00 34.07           C  
-ATOM   1571  C   GLY A 234      -7.075   7.573  44.359  1.00 35.78           C  
-ATOM   1572  O   GLY A 234      -7.731   6.545  44.525  1.00 35.03           O  
-ATOM   1573  N   ARG A 235      -5.952   7.826  45.028  1.00 36.81           N  
-ATOM   1574  CA  ARG A 235      -5.432   6.885  46.017  1.00 38.47           C  
-ATOM   1575  C   ARG A 235      -6.332   6.805  47.244  1.00 38.52           C  
-ATOM   1576  O   ARG A 235      -6.434   5.763  47.889  1.00 40.00           O  
-ATOM   1577  CB  ARG A 235      -4.020   7.286  46.438  1.00 38.86           C  
-ATOM   1578  CG  ARG A 235      -2.963   6.990  45.394  1.00 40.13           C  
-ATOM   1579  CD  ARG A 235      -1.608   7.497  45.835  1.00 43.41           C  
-ATOM   1580  NE  ARG A 235      -0.557   7.028  44.942  1.00 48.78           N  
-ATOM   1581  CZ  ARG A 235       0.546   7.714  44.655  1.00 50.49           C  
-ATOM   1582  NH1 ARG A 235       0.748   8.913  45.191  1.00 51.26           N  
-ATOM   1583  NH2 ARG A 235       1.446   7.202  43.825  1.00 51.68           N  
-ATOM   1584  N   ILE A 236      -6.981   7.912  47.572  1.00 37.98           N  
-ATOM   1585  CA  ILE A 236      -7.877   7.933  48.712  1.00 38.37           C  
-ATOM   1586  C   ILE A 236      -9.096   7.082  48.377  1.00 39.46           C  
-ATOM   1587  O   ILE A 236      -9.559   6.286  49.193  1.00 40.41           O  
-ATOM   1588  CB  ILE A 236      -8.326   9.368  49.033  1.00 37.64           C  
-ATOM   1589  CG1 ILE A 236      -7.141  10.166  49.576  1.00 36.08           C  
-ATOM   1590  CG2 ILE A 236      -9.476   9.346  50.026  1.00 36.59           C  
-ATOM   1591  CD1 ILE A 236      -7.445  11.622  49.824  1.00 37.54           C  
-ATOM   1592  N   LYS A 237      -9.597   7.241  47.159  1.00 40.07           N  
-ATOM   1593  CA  LYS A 237     -10.765   6.499  46.714  1.00 40.17           C  
-ATOM   1594  C   LYS A 237     -10.566   4.981  46.774  1.00 40.14           C  
-ATOM   1595  O   LYS A 237     -11.470   4.251  47.181  1.00 39.34           O  
-ATOM   1596  CB  LYS A 237     -11.134   6.916  45.289  1.00 39.39           C  
-ATOM   1597  CG  LYS A 237     -12.443   6.335  44.790  1.00 40.44           C  
-ATOM   1598  CD  LYS A 237     -13.627   6.873  45.575  1.00 40.67           C  
-ATOM   1599  CE  LYS A 237     -14.938   6.351  45.010  1.00 41.09           C  
-ATOM   1600  NZ  LYS A 237     -16.114   6.939  45.714  1.00 43.15           N  
-ATOM   1601  N   VAL A 238      -9.390   4.508  46.372  1.00 40.47           N  
-ATOM   1602  CA  VAL A 238      -9.110   3.075  46.382  1.00 41.04           C  
-ATOM   1603  C   VAL A 238      -8.541   2.578  47.710  1.00 41.66           C  
-ATOM   1604  O   VAL A 238      -8.275   1.386  47.872  1.00 41.76           O  
-ATOM   1605  CB  VAL A 238      -8.136   2.690  45.249  1.00 41.68           C  
-ATOM   1606  CG1 VAL A 238      -8.738   3.066  43.905  1.00 42.64           C  
-ATOM   1607  CG2 VAL A 238      -6.802   3.382  45.449  1.00 42.52           C  
-ATOM   1608  N   GLY A 239      -8.343   3.494  48.652  1.00 42.11           N  
-ATOM   1609  CA  GLY A 239      -7.825   3.110  49.953  1.00 41.71           C  
-ATOM   1610  C   GLY A 239      -6.316   3.037  50.109  1.00 41.59           C  
-ATOM   1611  O   GLY A 239      -5.825   2.453  51.073  1.00 41.60           O  
-ATOM   1612  N   LEU A 240      -5.569   3.617  49.175  1.00 41.35           N  
-ATOM   1613  CA  LEU A 240      -4.115   3.600  49.275  1.00 39.56           C  
-ATOM   1614  C   LEU A 240      -3.592   4.796  50.069  1.00 39.13           C  
-ATOM   1615  O   LEU A 240      -2.443   4.801  50.505  1.00 39.13           O  
-ATOM   1616  CB  LEU A 240      -3.481   3.598  47.883  1.00 40.72           C  
-ATOM   1617  CG  LEU A 240      -3.634   2.323  47.054  1.00 40.57           C  
-ATOM   1618  CD1 LEU A 240      -3.004   2.523  45.687  1.00 39.26           C  
-ATOM   1619  CD2 LEU A 240      -2.976   1.165  47.780  1.00 39.16           C  
-ATOM   1620  N   GLN A 241      -4.436   5.806  50.260  1.00 38.19           N  
-ATOM   1621  CA  GLN A 241      -4.037   7.003  51.000  1.00 38.32           C  
-ATOM   1622  C   GLN A 241      -5.208   7.482  51.851  1.00 38.69           C  
-ATOM   1623  O   GLN A 241      -6.368   7.243  51.510  1.00 39.53           O  
-ATOM   1624  CB  GLN A 241      -3.619   8.104  50.021  1.00 38.50           C  
-ATOM   1625  CG  GLN A 241      -2.907   9.294  50.660  1.00 39.27           C  
-ATOM   1626  CD  GLN A 241      -2.427  10.301  49.629  1.00 38.14           C  
-ATOM   1627  OE1 GLN A 241      -1.917   9.926  48.576  1.00 37.81           O  
-ATOM   1628  NE2 GLN A 241      -2.577  11.583  49.932  1.00 38.51           N  
-ATOM   1629  N   THR A 242      -4.912   8.167  52.949  1.00 37.85           N  
-ATOM   1630  CA  THR A 242      -5.970   8.651  53.826  1.00 38.76           C  
-ATOM   1631  C   THR A 242      -5.973  10.162  54.029  1.00 38.68           C  
-ATOM   1632  O   THR A 242      -7.026  10.750  54.268  1.00 39.07           O  
-ATOM   1633  CB  THR A 242      -5.896   7.976  55.213  1.00 39.67           C  
-ATOM   1634  OG1 THR A 242      -4.738   8.440  55.915  1.00 41.90           O  
-ATOM   1635  CG2 THR A 242      -5.807   6.461  55.062  1.00 41.50           C  
-ATOM   1636  N   LYS A 243      -4.805  10.793  53.937  1.00 37.17           N  
-ATOM   1637  CA  LYS A 243      -4.721  12.240  54.128  1.00 36.36           C  
-ATOM   1638  C   LYS A 243      -4.051  12.979  52.964  1.00 36.34           C  
-ATOM   1639  O   LYS A 243      -3.181  12.437  52.281  1.00 35.19           O  
-ATOM   1640  CB  LYS A 243      -3.989  12.547  55.433  1.00 33.91           C  
-ATOM   1641  N   LEU A 244      -4.470  14.224  52.751  1.00 35.38           N  
-ATOM   1642  CA  LEU A 244      -3.927  15.064  51.691  1.00 35.67           C  
-ATOM   1643  C   LEU A 244      -3.531  16.420  52.274  1.00 35.91           C  
-ATOM   1644  O   LEU A 244      -4.393  17.196  52.686  1.00 37.73           O  
-ATOM   1645  CB  LEU A 244      -4.973  15.250  50.586  1.00 35.37           C  
-ATOM   1646  CG  LEU A 244      -4.770  16.384  49.578  1.00 35.21           C  
-ATOM   1647  CD1 LEU A 244      -3.420  16.247  48.874  1.00 35.03           C  
-ATOM   1648  CD2 LEU A 244      -5.907  16.361  48.580  1.00 34.30           C  
-ATOM   1649  N   PHE A 245      -2.229  16.700  52.307  1.00 36.01           N  
-ATOM   1650  CA  PHE A 245      -1.725  17.963  52.852  1.00 35.82           C  
-ATOM   1651  C   PHE A 245      -1.522  19.044  51.795  1.00 35.81           C  
-ATOM   1652  O   PHE A 245      -0.830  18.827  50.799  1.00 35.39           O  
-ATOM   1653  CB  PHE A 245      -0.405  17.732  53.592  1.00 36.66           C  
-ATOM   1654  CG  PHE A 245      -0.488  16.675  54.653  1.00 39.22           C  
-ATOM   1655  CD1 PHE A 245      -0.278  15.336  54.336  1.00 40.05           C  
-ATOM   1656  CD2 PHE A 245      -0.810  17.012  55.966  1.00 38.78           C  
-ATOM   1657  CE1 PHE A 245      -0.389  14.345  55.312  1.00 40.82           C  
-ATOM   1658  CE2 PHE A 245      -0.924  16.028  56.948  1.00 40.02           C  
-ATOM   1659  CZ  PHE A 245      -0.714  14.692  56.620  1.00 38.78           C  
-ATOM   1660  N   LEU A 246      -2.121  20.211  52.034  1.00 34.95           N  
-ATOM   1661  CA  LEU A 246      -2.027  21.345  51.119  1.00 34.71           C  
-ATOM   1662  C   LEU A 246      -1.653  22.632  51.854  1.00 35.24           C  
-ATOM   1663  O   LEU A 246      -1.489  22.643  53.077  1.00 35.15           O  
-ATOM   1664  CB  LEU A 246      -3.361  21.548  50.398  1.00 33.75           C  
-ATOM   1665  CG  LEU A 246      -3.849  20.361  49.570  1.00 33.93           C  
-ATOM   1666  CD1 LEU A 246      -5.274  20.609  49.090  1.00 32.06           C  
-ATOM   1667  CD2 LEU A 246      -2.900  20.148  48.396  1.00 33.00           C  
-ATOM   1668  N   GLY A 247      -1.518  23.717  51.097  1.00 34.75           N  
-ATOM   1669  CA  GLY A 247      -1.174  24.995  51.689  1.00 33.46           C  
-ATOM   1670  C   GLY A 247      -2.323  25.975  51.569  1.00 33.38           C  
-ATOM   1671  O   GLY A 247      -3.406  25.738  52.102  1.00 32.40           O  
-ATOM   1672  N   ASN A 248      -2.086  27.074  50.860  1.00 34.95           N  
-ATOM   1673  CA  ASN A 248      -3.096  28.109  50.655  1.00 35.60           C  
-ATOM   1674  C   ASN A 248      -4.172  27.654  49.672  1.00 37.14           C  
-ATOM   1675  O   ASN A 248      -3.898  27.441  48.490  1.00 36.83           O  
-ATOM   1676  CB  ASN A 248      -2.415  29.389  50.154  1.00 35.91           C  
-ATOM   1677  CG  ASN A 248      -3.397  30.420  49.640  1.00 35.49           C  
-ATOM   1678  OD1 ASN A 248      -4.500  30.569  50.168  1.00 38.20           O  
-ATOM   1679  ND2 ASN A 248      -2.990  31.158  48.613  1.00 37.83           N  
-ATOM   1680  N   LEU A 249      -5.398  27.507  50.169  1.00 38.26           N  
-ATOM   1681  CA  LEU A 249      -6.520  27.066  49.344  1.00 38.64           C  
-ATOM   1682  C   LEU A 249      -7.277  28.218  48.689  1.00 38.39           C  
-ATOM   1683  O   LEU A 249      -8.128  27.997  47.828  1.00 38.73           O  
-ATOM   1684  CB  LEU A 249      -7.512  26.256  50.187  1.00 38.30           C  
-ATOM   1685  CG  LEU A 249      -7.012  25.029  50.945  1.00 39.32           C  
-ATOM   1686  CD1 LEU A 249      -8.194  24.356  51.615  1.00 38.82           C  
-ATOM   1687  CD2 LEU A 249      -6.318  24.065  49.997  1.00 38.90           C  
-ATOM   1688  N   GLN A 250      -6.973  29.445  49.090  1.00 38.21           N  
-ATOM   1689  CA  GLN A 250      -7.674  30.594  48.538  1.00 38.49           C  
-ATOM   1690  C   GLN A 250      -7.022  31.218  47.314  1.00 36.71           C  
-ATOM   1691  O   GLN A 250      -7.591  32.116  46.696  1.00 35.83           O  
-ATOM   1692  CB  GLN A 250      -7.874  31.653  49.627  1.00 42.58           C  
-ATOM   1693  CG  GLN A 250      -8.740  31.163  50.784  1.00 46.41           C  
-ATOM   1694  CD  GLN A 250     -10.032  30.514  50.303  1.00 49.04           C  
-ATOM   1695  OE1 GLN A 250     -10.798  31.113  49.547  1.00 51.83           O  
-ATOM   1696  NE2 GLN A 250     -10.277  29.282  50.741  1.00 48.25           N  
-ATOM   1697  N   ALA A 251      -5.831  30.753  46.960  1.00 34.62           N  
-ATOM   1698  CA  ALA A 251      -5.160  31.278  45.779  1.00 33.33           C  
-ATOM   1699  C   ALA A 251      -6.089  31.002  44.603  1.00 32.49           C  
-ATOM   1700  O   ALA A 251      -6.658  29.914  44.503  1.00 31.26           O  
-ATOM   1701  CB  ALA A 251      -3.828  30.577  45.572  1.00 34.37           C  
-ATOM   1702  N   SER A 252      -6.258  31.986  43.727  1.00 31.52           N  
-ATOM   1703  CA  SER A 252      -7.133  31.817  42.574  1.00 32.18           C  
-ATOM   1704  C   SER A 252      -6.324  31.722  41.293  1.00 31.27           C  
-ATOM   1705  O   SER A 252      -5.406  32.513  41.064  1.00 28.90           O  
-ATOM   1706  CB  SER A 252      -8.119  32.982  42.471  1.00 33.31           C  
-ATOM   1707  OG  SER A 252      -9.053  32.746  41.434  1.00 33.27           O  
-ATOM   1708  N   ARG A 253      -6.680  30.751  40.457  1.00 31.68           N  
-ATOM   1709  CA  ARG A 253      -5.974  30.528  39.202  1.00 31.66           C  
-ATOM   1710  C   ARG A 253      -6.880  30.306  37.999  1.00 32.08           C  
-ATOM   1711  O   ARG A 253      -8.042  29.926  38.127  1.00 32.46           O  
-ATOM   1712  CB  ARG A 253      -5.029  29.327  39.340  1.00 30.70           C  
-ATOM   1713  CG  ARG A 253      -3.875  29.533  40.314  1.00 27.95           C  
-ATOM   1714  CD  ARG A 253      -2.879  30.566  39.789  1.00 28.17           C  
-ATOM   1715  NE  ARG A 253      -1.740  30.738  40.687  1.00 29.50           N  
-ATOM   1716  CZ  ARG A 253      -1.780  31.419  41.829  1.00 33.54           C  
-ATOM   1717  NH1 ARG A 253      -0.692  31.516  42.583  1.00 34.55           N  
-ATOM   1718  NH2 ARG A 253      -2.901  32.021  42.212  1.00 32.28           N  
-ATOM   1719  N   ASP A 254      -6.308  30.558  36.828  1.00 32.12           N  
-ATOM   1720  CA  ASP A 254      -6.962  30.392  35.539  1.00 30.25           C  
-ATOM   1721  C   ASP A 254      -6.343  29.102  34.994  1.00 29.23           C  
-ATOM   1722  O   ASP A 254      -5.199  29.104  34.540  1.00 29.01           O  
-ATOM   1723  CB  ASP A 254      -6.622  31.606  34.659  1.00 31.17           C  
-ATOM   1724  CG  ASP A 254      -7.215  31.526  33.264  1.00 29.73           C  
-ATOM   1725  OD1 ASP A 254      -7.538  32.595  32.708  1.00 29.05           O  
-ATOM   1726  OD2 ASP A 254      -7.338  30.416  32.711  1.00 31.94           O  
-ATOM   1727  N   TRP A 255      -7.098  28.007  35.063  1.00 27.61           N  
-ATOM   1728  CA  TRP A 255      -6.622  26.692  34.625  1.00 28.29           C  
-ATOM   1729  C   TRP A 255      -7.134  26.181  33.278  1.00 27.92           C  
-ATOM   1730  O   TRP A 255      -8.338  26.034  33.082  1.00 29.14           O  
-ATOM   1731  CB  TRP A 255      -6.966  25.636  35.682  1.00 28.37           C  
-ATOM   1732  CG  TRP A 255      -6.145  25.679  36.940  1.00 29.24           C  
-ATOM   1733  CD1 TRP A 255      -4.793  25.495  37.051  1.00 27.79           C  
-ATOM   1734  CD2 TRP A 255      -6.632  25.878  38.273  1.00 28.13           C  
-ATOM   1735  NE1 TRP A 255      -4.411  25.563  38.374  1.00 26.20           N  
-ATOM   1736  CE2 TRP A 255      -5.519  25.799  39.143  1.00 27.64           C  
-ATOM   1737  CE3 TRP A 255      -7.901  26.115  38.817  1.00 27.87           C  
-ATOM   1738  CZ2 TRP A 255      -5.639  25.952  40.527  1.00 26.33           C  
-ATOM   1739  CZ3 TRP A 255      -8.018  26.265  40.196  1.00 26.56           C  
-ATOM   1740  CH2 TRP A 255      -6.892  26.183  41.033  1.00 26.35           C  
-ATOM   1741  N   GLY A 256      -6.208  25.875  32.374  1.00 28.09           N  
-ATOM   1742  CA  GLY A 256      -6.567  25.348  31.066  1.00 27.05           C  
-ATOM   1743  C   GLY A 256      -5.909  23.992  30.838  1.00 27.67           C  
-ATOM   1744  O   GLY A 256      -5.152  23.525  31.685  1.00 25.45           O  
-ATOM   1745  N   PHE A 257      -6.195  23.359  29.699  1.00 28.62           N  
-ATOM   1746  CA  PHE A 257      -5.625  22.049  29.360  1.00 27.88           C  
-ATOM   1747  C   PHE A 257      -4.402  22.216  28.451  1.00 28.50           C  
-ATOM   1748  O   PHE A 257      -4.482  22.856  27.398  1.00 27.84           O  
-ATOM   1749  CB  PHE A 257      -6.691  21.186  28.668  1.00 28.03           C  
-ATOM   1750  CG  PHE A 257      -6.164  19.898  28.080  1.00 28.43           C  
-ATOM   1751  CD1 PHE A 257      -5.468  18.979  28.870  1.00 28.35           C  
-ATOM   1752  CD2 PHE A 257      -6.404  19.584  26.744  1.00 26.82           C  
-ATOM   1753  CE1 PHE A 257      -5.021  17.762  28.335  1.00 28.51           C  
-ATOM   1754  CE2 PHE A 257      -5.962  18.368  26.196  1.00 27.36           C  
-ATOM   1755  CZ  PHE A 257      -5.271  17.457  26.991  1.00 27.76           C  
-ATOM   1756  N   ALA A 258      -3.274  21.642  28.869  1.00 27.10           N  
-ATOM   1757  CA  ALA A 258      -2.022  21.732  28.117  1.00 27.52           C  
-ATOM   1758  C   ALA A 258      -2.180  21.331  26.654  1.00 28.31           C  
-ATOM   1759  O   ALA A 258      -1.554  21.921  25.770  1.00 28.16           O  
-ATOM   1760  CB  ALA A 258      -0.950  20.861  28.779  1.00 26.29           C  
-ATOM   1761  N   GLY A 259      -3.007  20.319  26.406  1.00 28.30           N  
-ATOM   1762  CA  GLY A 259      -3.229  19.863  25.049  1.00 28.65           C  
-ATOM   1763  C   GLY A 259      -3.724  20.996  24.171  1.00 29.81           C  
-ATOM   1764  O   GLY A 259      -3.325  21.112  23.013  1.00 30.76           O  
-ATOM   1765  N   ASP A 260      -4.596  21.835  24.722  1.00 28.49           N  
-ATOM   1766  CA  ASP A 260      -5.132  22.972  23.979  1.00 28.23           C  
-ATOM   1767  C   ASP A 260      -4.082  24.058  23.771  1.00 28.66           C  
-ATOM   1768  O   ASP A 260      -3.962  24.616  22.681  1.00 28.63           O  
-ATOM   1769  CB  ASP A 260      -6.306  23.608  24.729  1.00 28.45           C  
-ATOM   1770  CG  ASP A 260      -7.526  22.711  24.801  1.00 30.34           C  
-ATOM   1771  OD1 ASP A 260      -8.522  23.137  25.422  1.00 30.07           O  
-ATOM   1772  OD2 ASP A 260      -7.496  21.594  24.243  1.00 31.93           O  
-ATOM   1773  N   TYR A 261      -3.328  24.352  24.829  1.00 28.15           N  
-ATOM   1774  CA  TYR A 261      -2.323  25.412  24.802  1.00 27.78           C  
-ATOM   1775  C   TYR A 261      -1.140  25.253  23.862  1.00 26.83           C  
-ATOM   1776  O   TYR A 261      -0.717  26.230  23.254  1.00 28.99           O  
-ATOM   1777  CB  TYR A 261      -1.823  25.684  26.227  1.00 26.72           C  
-ATOM   1778  CG  TYR A 261      -2.848  26.381  27.096  1.00 26.30           C  
-ATOM   1779  CD1 TYR A 261      -4.208  26.098  26.961  1.00 28.01           C  
-ATOM   1780  CD2 TYR A 261      -2.462  27.315  28.058  1.00 25.82           C  
-ATOM   1781  CE1 TYR A 261      -5.159  26.723  27.758  1.00 26.44           C  
-ATOM   1782  CE2 TYR A 261      -3.408  27.947  28.866  1.00 25.62           C  
-ATOM   1783  CZ  TYR A 261      -4.757  27.643  28.709  1.00 26.64           C  
-ATOM   1784  OH  TYR A 261      -5.702  28.249  29.504  1.00 22.39           O  
-ATOM   1785  N   VAL A 262      -0.595  24.046  23.732  1.00 26.59           N  
-ATOM   1786  CA  VAL A 262       0.545  23.865  22.840  1.00 27.49           C  
-ATOM   1787  C   VAL A 262       0.190  24.274  21.414  1.00 28.69           C  
-ATOM   1788  O   VAL A 262       1.061  24.667  20.646  1.00 29.38           O  
-ATOM   1789  CB  VAL A 262       1.061  22.403  22.831  1.00 27.89           C  
-ATOM   1790  CG1 VAL A 262       1.565  22.027  24.217  1.00 26.94           C  
-ATOM   1791  CG2 VAL A 262      -0.039  21.453  22.363  1.00 26.77           C  
-ATOM   1792  N   GLU A 263      -1.091  24.189  21.068  1.00 27.91           N  
-ATOM   1793  CA  GLU A 263      -1.539  24.569  19.732  1.00 29.05           C  
-ATOM   1794  C   GLU A 263      -1.372  26.080  19.520  1.00 29.20           C  
-ATOM   1795  O   GLU A 263      -1.051  26.533  18.415  1.00 30.27           O  
-ATOM   1796  CB  GLU A 263      -2.998  24.163  19.534  1.00 26.78           C  
-ATOM   1797  N   ALA A 264      -1.584  26.857  20.580  1.00 26.48           N  
-ATOM   1798  CA  ALA A 264      -1.437  28.309  20.492  1.00 26.62           C  
-ATOM   1799  C   ALA A 264       0.023  28.653  20.228  1.00 25.29           C  
-ATOM   1800  O   ALA A 264       0.326  29.624  19.536  1.00 25.88           O  
-ATOM   1801  CB  ALA A 264      -1.910  28.978  21.787  1.00 21.36           C  
-ATOM   1802  N   MET A 265       0.921  27.848  20.788  1.00 24.28           N  
-ATOM   1803  CA  MET A 265       2.356  28.055  20.614  1.00 25.68           C  
-ATOM   1804  C   MET A 265       2.698  27.987  19.136  1.00 26.27           C  
-ATOM   1805  O   MET A 265       3.387  28.854  18.606  1.00 24.67           O  
-ATOM   1806  CB  MET A 265       3.156  26.972  21.356  1.00 24.96           C  
-ATOM   1807  CG  MET A 265       2.936  26.925  22.863  1.00 23.23           C  
-ATOM   1808  SD  MET A 265       3.861  25.588  23.630  1.00 25.99           S  
-ATOM   1809  CE  MET A 265       3.367  25.757  25.369  1.00 24.79           C  
-ATOM   1810  N   TRP A 266       2.222  26.932  18.486  1.00 27.95           N  
-ATOM   1811  CA  TRP A 266       2.463  26.717  17.068  1.00 29.54           C  
-ATOM   1812  C   TRP A 266       1.870  27.860  16.239  1.00 29.78           C  
-ATOM   1813  O   TRP A 266       2.530  28.403  15.352  1.00 30.95           O  
-ATOM   1814  CB  TRP A 266       1.851  25.381  16.648  1.00 31.39           C  
-ATOM   1815  CG  TRP A 266       1.971  25.082  15.188  1.00 34.34           C  
-ATOM   1816  CD1 TRP A 266       3.091  24.685  14.517  1.00 35.12           C  
-ATOM   1817  CD2 TRP A 266       0.925  25.159  14.216  1.00 33.44           C  
-ATOM   1818  NE1 TRP A 266       2.806  24.506  13.183  1.00 35.82           N  
-ATOM   1819  CE2 TRP A 266       1.482  24.790  12.971  1.00 35.51           C  
-ATOM   1820  CE3 TRP A 266      -0.431  25.506  14.275  1.00 33.52           C  
-ATOM   1821  CZ2 TRP A 266       0.728  24.756  11.792  1.00 35.75           C  
-ATOM   1822  CZ3 TRP A 266      -1.182  25.473  13.100  1.00 35.93           C  
-ATOM   1823  CH2 TRP A 266      -0.597  25.100  11.877  1.00 33.98           C  
-ATOM   1824  N   LEU A 267       0.633  28.234  16.548  1.00 30.99           N  
-ATOM   1825  CA  LEU A 267      -0.052  29.313  15.835  1.00 31.02           C  
-ATOM   1826  C   LEU A 267       0.725  30.627  15.822  1.00 31.90           C  
-ATOM   1827  O   LEU A 267       0.823  31.287  14.783  1.00 32.83           O  
-ATOM   1828  CB  LEU A 267      -1.442  29.550  16.441  1.00 30.12           C  
-ATOM   1829  CG  LEU A 267      -2.508  28.497  16.126  1.00 29.26           C  
-ATOM   1830  CD1 LEU A 267      -3.761  28.763  16.940  1.00 28.56           C  
-ATOM   1831  CD2 LEU A 267      -2.824  28.530  14.633  1.00 26.96           C  
-ATOM   1832  N   MET A 268       1.270  31.009  16.974  1.00 30.47           N  
-ATOM   1833  CA  MET A 268       2.031  32.249  17.079  1.00 30.03           C  
-ATOM   1834  C   MET A 268       3.126  32.323  16.032  1.00 30.30           C  
-ATOM   1835  O   MET A 268       3.364  33.381  15.452  1.00 30.31           O  
-ATOM   1836  CB  MET A 268       2.659  32.379  18.464  1.00 29.53           C  
-ATOM   1837  CG  MET A 268       1.661  32.612  19.575  1.00 31.71           C  
-ATOM   1838  SD  MET A 268       2.439  32.618  21.201  1.00 31.63           S  
-ATOM   1839  CE  MET A 268       1.120  31.907  22.175  1.00 29.50           C  
-ATOM   1840  N   LEU A 269       3.790  31.196  15.795  1.00 30.79           N  
-ATOM   1841  CA  LEU A 269       4.876  31.131  14.823  1.00 32.36           C  
-ATOM   1842  C   LEU A 269       4.397  30.993  13.386  1.00 35.19           C  
-ATOM   1843  O   LEU A 269       5.205  30.989  12.462  1.00 35.46           O  
-ATOM   1844  CB  LEU A 269       5.813  29.970  15.156  1.00 30.34           C  
-ATOM   1845  CG  LEU A 269       6.949  30.230  16.152  1.00 29.96           C  
-ATOM   1846  CD1 LEU A 269       6.434  30.944  17.379  1.00 29.93           C  
-ATOM   1847  CD2 LEU A 269       7.587  28.908  16.532  1.00 32.19           C  
-ATOM   1848  N   GLN A 270       3.087  30.875  13.192  1.00 36.51           N  
-ATOM   1849  CA  GLN A 270       2.553  30.742  11.842  1.00 38.85           C  
-ATOM   1850  C   GLN A 270       2.084  32.093  11.303  1.00 38.91           C  
-ATOM   1851  O   GLN A 270       1.688  32.207  10.141  1.00 38.85           O  
-ATOM   1852  CB  GLN A 270       1.406  29.726  11.816  1.00 38.78           C  
-ATOM   1853  CG  GLN A 270       1.765  28.367  12.423  1.00 41.59           C  
-ATOM   1854  CD  GLN A 270       3.133  27.853  11.978  1.00 44.00           C  
-ATOM   1855  OE1 GLN A 270       3.399  27.712  10.783  1.00 43.68           O  
-ATOM   1856  NE2 GLN A 270       4.005  27.566  12.946  1.00 40.29           N  
-ATOM   1857  N   GLN A 271       2.136  33.116  12.151  1.00 38.44           N  
-ATOM   1858  CA  GLN A 271       1.732  34.456  11.742  1.00 38.10           C  
-ATOM   1859  C   GLN A 271       2.836  35.064  10.886  1.00 39.24           C  
-ATOM   1860  O   GLN A 271       3.965  34.574  10.877  1.00 39.50           O  
-ATOM   1861  CB  GLN A 271       1.487  35.349  12.957  1.00 37.25           C  
-ATOM   1862  CG  GLN A 271       0.478  34.804  13.947  1.00 37.93           C  
-ATOM   1863  CD  GLN A 271      -0.778  34.283  13.277  1.00 39.54           C  
-ATOM   1864  OE1 GLN A 271      -0.956  33.074  13.122  1.00 40.90           O  
-ATOM   1865  NE2 GLN A 271      -1.654  35.194  12.868  1.00 38.69           N  
-ATOM   1866  N   GLU A 272       2.506  36.131  10.165  1.00 40.50           N  
-ATOM   1867  CA  GLU A 272       3.476  36.799   9.306  1.00 40.29           C  
-ATOM   1868  C   GLU A 272       4.470  37.571  10.166  1.00 39.77           C  
-ATOM   1869  O   GLU A 272       5.640  37.708   9.806  1.00 39.42           O  
-ATOM   1870  CB  GLU A 272       2.760  37.751   8.344  1.00 39.78           C  
-ATOM   1871  N   LYS A 273       3.995  38.067  11.305  1.00 38.75           N  
-ATOM   1872  CA  LYS A 273       4.838  38.831  12.214  1.00 38.68           C  
-ATOM   1873  C   LYS A 273       4.856  38.246  13.622  1.00 36.77           C  
-ATOM   1874  O   LYS A 273       3.876  37.661  14.075  1.00 35.74           O  
-ATOM   1875  CB  LYS A 273       4.365  40.286  12.273  1.00 40.09           C  
-ATOM   1876  CG  LYS A 273       4.486  41.026  10.946  1.00 43.37           C  
-ATOM   1877  CD  LYS A 273       3.990  42.455  11.059  1.00 45.76           C  
-ATOM   1878  CE  LYS A 273       4.122  43.187   9.731  1.00 48.16           C  
-ATOM   1879  NZ  LYS A 273       3.632  44.595   9.822  1.00 50.00           N  
-ATOM   1880  N   PRO A 274       5.984  38.399  14.330  1.00 35.46           N  
-ATOM   1881  CA  PRO A 274       6.139  37.891  15.694  1.00 35.63           C  
-ATOM   1882  C   PRO A 274       5.483  38.838  16.694  1.00 34.64           C  
-ATOM   1883  O   PRO A 274       5.441  40.044  16.473  1.00 35.58           O  
-ATOM   1884  CB  PRO A 274       7.650  37.846  15.860  1.00 34.97           C  
-ATOM   1885  CG  PRO A 274       8.071  39.077  15.129  1.00 35.52           C  
-ATOM   1886  CD  PRO A 274       7.248  38.988  13.852  1.00 35.69           C  
-ATOM   1887  N   ASP A 275       4.983  38.295  17.796  1.00 33.37           N  
-ATOM   1888  CA  ASP A 275       4.341  39.123  18.805  1.00 32.57           C  
-ATOM   1889  C   ASP A 275       4.197  38.338  20.106  1.00 31.00           C  
-ATOM   1890  O   ASP A 275       4.682  37.216  20.211  1.00 29.73           O  
-ATOM   1891  CB  ASP A 275       2.965  39.568  18.307  1.00 32.33           C  
-ATOM   1892  CG  ASP A 275       2.496  40.849  18.959  1.00 33.18           C  
-ATOM   1893  OD1 ASP A 275       1.372  41.292  18.651  1.00 35.91           O  
-ATOM   1894  OD2 ASP A 275       3.252  41.419  19.772  1.00 36.06           O  
-ATOM   1895  N   ASP A 276       3.535  38.936  21.091  1.00 31.21           N  
-ATOM   1896  CA  ASP A 276       3.320  38.289  22.380  1.00 30.87           C  
-ATOM   1897  C   ASP A 276       1.827  38.120  22.605  1.00 30.88           C  
-ATOM   1898  O   ASP A 276       1.049  39.049  22.389  1.00 31.18           O  
-ATOM   1899  CB  ASP A 276       3.916  39.132  23.508  1.00 31.31           C  
-ATOM   1900  CG  ASP A 276       5.319  39.595  23.201  1.00 31.52           C  
-ATOM   1901  OD1 ASP A 276       6.130  38.767  22.738  1.00 33.41           O  
-ATOM   1902  OD2 ASP A 276       5.615  40.785  23.423  1.00 32.77           O  
-ATOM   1903  N   TYR A 277       1.427  36.932  23.043  1.00 30.96           N  
-ATOM   1904  CA  TYR A 277       0.020  36.661  23.274  1.00 29.75           C  
-ATOM   1905  C   TYR A 277      -0.241  35.935  24.577  1.00 29.53           C  
-ATOM   1906  O   TYR A 277       0.506  35.035  24.973  1.00 30.54           O  
-ATOM   1907  CB  TYR A 277      -0.568  35.794  22.155  1.00 30.27           C  
-ATOM   1908  CG  TYR A 277      -0.174  36.168  20.748  1.00 31.30           C  
-ATOM   1909  CD1 TYR A 277       1.098  35.879  20.259  1.00 31.98           C  
-ATOM   1910  CD2 TYR A 277      -1.089  36.781  19.891  1.00 32.78           C  
-ATOM   1911  CE1 TYR A 277       1.451  36.185  18.948  1.00 34.05           C  
-ATOM   1912  CE2 TYR A 277      -0.749  37.093  18.580  1.00 32.02           C  
-ATOM   1913  CZ  TYR A 277       0.518  36.792  18.114  1.00 34.13           C  
-ATOM   1914  OH  TYR A 277       0.848  37.079  16.812  1.00 35.75           O  
-ATOM   1915  N   VAL A 278      -1.326  36.326  25.228  1.00 28.99           N  
-ATOM   1916  CA  VAL A 278      -1.761  35.684  26.452  1.00 29.36           C  
-ATOM   1917  C   VAL A 278      -2.623  34.504  26.006  1.00 28.99           C  
-ATOM   1918  O   VAL A 278      -3.443  34.632  25.100  1.00 29.67           O  
-ATOM   1919  CB  VAL A 278      -2.623  36.632  27.312  1.00 29.09           C  
-ATOM   1920  CG1 VAL A 278      -3.463  35.828  28.300  1.00 29.30           C  
-ATOM   1921  CG2 VAL A 278      -1.728  37.603  28.062  1.00 29.13           C  
-ATOM   1922  N   VAL A 279      -2.410  33.353  26.625  1.00 28.15           N  
-ATOM   1923  CA  VAL A 279      -3.174  32.158  26.321  1.00 26.58           C  
-ATOM   1924  C   VAL A 279      -3.772  31.763  27.662  1.00 27.98           C  
-ATOM   1925  O   VAL A 279      -3.044  31.432  28.601  1.00 27.81           O  
-ATOM   1926  CB  VAL A 279      -2.263  31.035  25.787  1.00 27.32           C  
-ATOM   1927  CG1 VAL A 279      -3.072  29.767  25.552  1.00 25.42           C  
-ATOM   1928  CG2 VAL A 279      -1.594  31.486  24.497  1.00 25.80           C  
-ATOM   1929  N   ALA A 280      -5.097  31.809  27.752  1.00 27.24           N  
-ATOM   1930  CA  ALA A 280      -5.787  31.510  28.996  1.00 27.22           C  
-ATOM   1931  C   ALA A 280      -7.244  31.171  28.723  1.00 27.41           C  
-ATOM   1932  O   ALA A 280      -7.685  31.234  27.581  1.00 27.74           O  
-ATOM   1933  CB  ALA A 280      -5.702  32.718  29.914  1.00 27.29           C  
-ATOM   1934  N   THR A 281      -7.988  30.821  29.772  1.00 28.15           N  
-ATOM   1935  CA  THR A 281      -9.409  30.487  29.635  1.00 28.93           C  
-ATOM   1936  C   THR A 281     -10.268  31.690  30.027  1.00 30.27           C  
-ATOM   1937  O   THR A 281     -11.451  31.766  29.688  1.00 29.50           O  
-ATOM   1938  CB  THR A 281      -9.804  29.282  30.528  1.00 28.13           C  
-ATOM   1939  OG1 THR A 281      -9.700  29.644  31.912  1.00 28.70           O  
-ATOM   1940  CG2 THR A 281      -8.890  28.098  30.254  1.00 27.55           C  
-ATOM   1941  N   GLU A 282      -9.647  32.623  30.744  1.00 32.12           N  
-ATOM   1942  CA  GLU A 282     -10.292  33.847  31.211  1.00 33.23           C  
-ATOM   1943  C   GLU A 282     -11.261  33.572  32.350  1.00 33.55           C  
-ATOM   1944  O   GLU A 282     -12.067  34.428  32.705  1.00 35.41           O  
-ATOM   1945  CB  GLU A 282     -11.031  34.542  30.059  1.00 32.76           C  
-ATOM   1946  CG  GLU A 282     -10.202  34.674  28.793  1.00 33.97           C  
-ATOM   1947  CD  GLU A 282     -10.877  35.524  27.739  1.00 33.07           C  
-ATOM   1948  OE1 GLU A 282     -12.088  35.337  27.508  1.00 36.89           O  
-ATOM   1949  OE2 GLU A 282     -10.197  36.371  27.132  1.00 33.92           O  
-ATOM   1950  N   GLU A 283     -11.178  32.379  32.923  1.00 33.23           N  
-ATOM   1951  CA  GLU A 283     -12.050  32.002  34.026  1.00 32.93           C  
-ATOM   1952  C   GLU A 283     -11.196  31.635  35.229  1.00 33.53           C  
-ATOM   1953  O   GLU A 283     -10.370  30.729  35.149  1.00 36.21           O  
-ATOM   1954  CB  GLU A 283     -12.924  30.818  33.621  1.00 33.88           C  
-ATOM   1955  N   GLY A 284     -11.396  32.331  36.344  1.00 32.45           N  
-ATOM   1956  CA  GLY A 284     -10.610  32.050  37.531  1.00 31.00           C  
-ATOM   1957  C   GLY A 284     -11.320  31.191  38.557  1.00 31.68           C  
-ATOM   1958  O   GLY A 284     -12.533  31.269  38.704  1.00 32.25           O  
-ATOM   1959  N   HIS A 285     -10.555  30.362  39.263  1.00 32.50           N  
-ATOM   1960  CA  HIS A 285     -11.099  29.488  40.298  1.00 32.36           C  
-ATOM   1961  C   HIS A 285     -10.068  29.330  41.416  1.00 32.28           C  
-ATOM   1962  O   HIS A 285      -8.868  29.439  41.179  1.00 30.66           O  
-ATOM   1963  CB  HIS A 285     -11.437  28.116  39.710  1.00 32.63           C  
-ATOM   1964  CG  HIS A 285     -12.530  28.148  38.690  1.00 34.37           C  
-ATOM   1965  ND1 HIS A 285     -13.855  28.334  39.023  1.00 35.93           N  
-ATOM   1966  CD2 HIS A 285     -12.494  28.025  37.342  1.00 32.77           C  
-ATOM   1967  CE1 HIS A 285     -14.587  28.325  37.923  1.00 35.92           C  
-ATOM   1968  NE2 HIS A 285     -13.785  28.139  36.889  1.00 33.00           N  
-ATOM   1969  N   THR A 286     -10.536  29.070  42.632  1.00 33.24           N  
-ATOM   1970  CA  THR A 286      -9.637  28.898  43.772  1.00 32.77           C  
-ATOM   1971  C   THR A 286      -9.260  27.435  43.950  1.00 33.12           C  
-ATOM   1972  O   THR A 286      -9.911  26.544  43.404  1.00 34.32           O  
-ATOM   1973  CB  THR A 286     -10.289  29.380  45.084  1.00 32.98           C  
-ATOM   1974  OG1 THR A 286     -11.460  28.601  45.344  1.00 32.80           O  
-ATOM   1975  CG2 THR A 286     -10.674  30.852  44.984  1.00 31.31           C  
-ATOM   1976  N   VAL A 287      -8.203  27.185  44.712  1.00 33.17           N  
-ATOM   1977  CA  VAL A 287      -7.774  25.818  44.952  1.00 33.11           C  
-ATOM   1978  C   VAL A 287      -8.901  25.069  45.663  1.00 35.02           C  
-ATOM   1979  O   VAL A 287      -9.066  23.861  45.483  1.00 34.06           O  
-ATOM   1980  CB  VAL A 287      -6.505  25.774  45.821  1.00 31.42           C  
-ATOM   1981  CG1 VAL A 287      -6.107  24.331  46.085  1.00 29.21           C  
-ATOM   1982  CG2 VAL A 287      -5.379  26.516  45.125  1.00 29.74           C  
-ATOM   1983  N   GLU A 288      -9.681  25.795  46.460  1.00 36.64           N  
-ATOM   1984  CA  GLU A 288     -10.796  25.196  47.189  1.00 38.46           C  
-ATOM   1985  C   GLU A 288     -11.852  24.719  46.197  1.00 37.41           C  
-ATOM   1986  O   GLU A 288     -12.361  23.604  46.311  1.00 37.97           O  
-ATOM   1987  CB  GLU A 288     -11.418  26.207  48.158  1.00 40.40           C  
-ATOM   1988  CG  GLU A 288     -12.339  25.568  49.191  1.00 44.85           C  
-ATOM   1989  CD  GLU A 288     -13.032  26.583  50.083  1.00 47.44           C  
-ATOM   1990  OE1 GLU A 288     -12.345  27.453  50.659  1.00 49.05           O  
-ATOM   1991  OE2 GLU A 288     -14.271  26.504  50.213  1.00 51.83           O  
-ATOM   1992  N   GLU A 289     -12.179  25.563  45.223  1.00 36.42           N  
-ATOM   1993  CA  GLU A 289     -13.162  25.189  44.213  1.00 36.62           C  
-ATOM   1994  C   GLU A 289     -12.667  23.942  43.484  1.00 35.65           C  
-ATOM   1995  O   GLU A 289     -13.454  23.073  43.115  1.00 36.87           O  
-ATOM   1996  CB  GLU A 289     -13.375  26.325  43.204  1.00 38.04           C  
-ATOM   1997  CG  GLU A 289     -13.963  27.604  43.791  1.00 42.43           C  
-ATOM   1998  CD  GLU A 289     -14.325  28.630  42.724  1.00 45.27           C  
-ATOM   1999  OE1 GLU A 289     -15.222  28.345  41.903  1.00 49.01           O  
-ATOM   2000  OE2 GLU A 289     -13.715  29.720  42.702  1.00 46.42           O  
-ATOM   2001  N   PHE A 290     -11.357  23.851  43.278  1.00 33.79           N  
-ATOM   2002  CA  PHE A 290     -10.797  22.689  42.599  1.00 32.56           C  
-ATOM   2003  C   PHE A 290     -11.068  21.451  43.446  1.00 33.16           C  
-ATOM   2004  O   PHE A 290     -11.369  20.377  42.924  1.00 33.44           O  
-ATOM   2005  CB  PHE A 290      -9.287  22.846  42.403  1.00 30.28           C  
-ATOM   2006  CG  PHE A 290      -8.692  21.817  41.486  1.00 29.35           C  
-ATOM   2007  CD1 PHE A 290      -8.519  22.091  40.135  1.00 28.49           C  
-ATOM   2008  CD2 PHE A 290      -8.343  20.560  41.965  1.00 28.04           C  
-ATOM   2009  CE1 PHE A 290      -8.009  21.130  39.272  1.00 28.24           C  
-ATOM   2010  CE2 PHE A 290      -7.833  19.590  41.111  1.00 29.47           C  
-ATOM   2011  CZ  PHE A 290      -7.666  19.877  39.758  1.00 28.32           C  
-ATOM   2012  N   LEU A 291     -10.955  21.613  44.760  1.00 34.10           N  
-ATOM   2013  CA  LEU A 291     -11.188  20.520  45.696  1.00 34.62           C  
-ATOM   2014  C   LEU A 291     -12.648  20.078  45.720  1.00 35.54           C  
-ATOM   2015  O   LEU A 291     -12.936  18.879  45.763  1.00 35.82           O  
-ATOM   2016  CB  LEU A 291     -10.752  20.940  47.100  1.00 34.35           C  
-ATOM   2017  CG  LEU A 291      -9.248  20.905  47.358  1.00 32.55           C  
-ATOM   2018  CD1 LEU A 291      -8.933  21.583  48.675  1.00 34.54           C  
-ATOM   2019  CD2 LEU A 291      -8.777  19.456  47.372  1.00 32.07           C  
-ATOM   2020  N   ASP A 292     -13.569  21.040  45.698  1.00 36.23           N  
-ATOM   2021  CA  ASP A 292     -14.995  20.715  45.714  1.00 37.02           C  
-ATOM   2022  C   ASP A 292     -15.355  19.898  44.479  1.00 36.89           C  
-ATOM   2023  O   ASP A 292     -15.986  18.840  44.572  1.00 37.59           O  
-ATOM   2024  CB  ASP A 292     -15.857  21.988  45.727  1.00 39.00           C  
-ATOM   2025  CG  ASP A 292     -15.640  22.837  46.968  1.00 42.26           C  
-ATOM   2026  OD1 ASP A 292     -15.416  22.264  48.053  1.00 43.25           O  
-ATOM   2027  OD2 ASP A 292     -15.710  24.082  46.862  1.00 43.49           O  
-ATOM   2028  N   VAL A 293     -14.939  20.402  43.321  1.00 35.36           N  
-ATOM   2029  CA  VAL A 293     -15.216  19.757  42.046  1.00 33.99           C  
-ATOM   2030  C   VAL A 293     -14.639  18.351  41.925  1.00 34.07           C  
-ATOM   2031  O   VAL A 293     -15.365  17.404  41.615  1.00 35.01           O  
-ATOM   2032  CB  VAL A 293     -14.684  20.611  40.874  1.00 33.50           C  
-ATOM   2033  CG1 VAL A 293     -15.024  19.947  39.547  1.00 30.31           C  
-ATOM   2034  CG2 VAL A 293     -15.274  22.017  40.949  1.00 30.16           C  
-ATOM   2035  N   SER A 294     -13.339  18.211  42.169  1.00 33.72           N  
-ATOM   2036  CA  SER A 294     -12.691  16.910  42.056  1.00 33.72           C  
-ATOM   2037  C   SER A 294     -13.201  15.870  43.054  1.00 35.16           C  
-ATOM   2038  O   SER A 294     -13.561  14.759  42.659  1.00 32.71           O  
-ATOM   2039  CB  SER A 294     -11.171  17.060  42.183  1.00 32.19           C  
-ATOM   2040  OG  SER A 294     -10.809  17.734  43.370  1.00 33.14           O  
-ATOM   2041  N   PHE A 295     -13.224  16.217  44.340  1.00 35.80           N  
-ATOM   2042  CA  PHE A 295     -13.710  15.281  45.353  1.00 35.84           C  
-ATOM   2043  C   PHE A 295     -15.214  15.044  45.206  1.00 35.52           C  
-ATOM   2044  O   PHE A 295     -15.683  13.911  45.298  1.00 36.57           O  
-ATOM   2045  CB  PHE A 295     -13.400  15.789  46.768  1.00 36.45           C  
-ATOM   2046  CG  PHE A 295     -12.012  15.448  47.251  1.00 38.59           C  
-ATOM   2047  CD1 PHE A 295     -10.901  16.152  46.793  1.00 37.40           C  
-ATOM   2048  CD2 PHE A 295     -11.817  14.409  48.161  1.00 37.90           C  
-ATOM   2049  CE1 PHE A 295      -9.617  15.827  47.236  1.00 38.55           C  
-ATOM   2050  CE2 PHE A 295     -10.539  14.076  48.609  1.00 37.75           C  
-ATOM   2051  CZ  PHE A 295      -9.436  14.786  48.146  1.00 38.68           C  
-ATOM   2052  N   GLY A 296     -15.969  16.111  44.972  1.00 36.04           N  
-ATOM   2053  CA  GLY A 296     -17.404  15.960  44.808  1.00 37.44           C  
-ATOM   2054  C   GLY A 296     -17.713  15.038  43.644  1.00 37.94           C  
-ATOM   2055  O   GLY A 296     -18.709  14.318  43.651  1.00 39.20           O  
-ATOM   2056  N   TYR A 297     -16.843  15.059  42.642  1.00 36.82           N  
-ATOM   2057  CA  TYR A 297     -17.010  14.230  41.462  1.00 38.11           C  
-ATOM   2058  C   TYR A 297     -16.971  12.747  41.826  1.00 39.04           C  
-ATOM   2059  O   TYR A 297     -17.593  11.922  41.158  1.00 39.37           O  
-ATOM   2060  CB  TYR A 297     -15.917  14.578  40.450  1.00 37.58           C  
-ATOM   2061  CG  TYR A 297     -15.881  13.738  39.194  1.00 38.03           C  
-ATOM   2062  CD1 TYR A 297     -16.985  13.653  38.342  1.00 37.37           C  
-ATOM   2063  CD2 TYR A 297     -14.713  13.073  38.824  1.00 36.44           C  
-ATOM   2064  CE1 TYR A 297     -16.916  12.927  37.143  1.00 35.96           C  
-ATOM   2065  CE2 TYR A 297     -14.635  12.353  37.639  1.00 36.97           C  
-ATOM   2066  CZ  TYR A 297     -15.733  12.284  36.801  1.00 35.83           C  
-ATOM   2067  OH  TYR A 297     -15.620  11.589  35.616  1.00 33.84           O  
-ATOM   2068  N   LEU A 298     -16.246  12.405  42.887  1.00 40.91           N  
-ATOM   2069  CA  LEU A 298     -16.171  11.009  43.317  1.00 42.59           C  
-ATOM   2070  C   LEU A 298     -17.037  10.752  44.554  1.00 43.65           C  
-ATOM   2071  O   LEU A 298     -16.951   9.692  45.181  1.00 43.78           O  
-ATOM   2072  CB  LEU A 298     -14.721  10.607  43.602  1.00 42.33           C  
-ATOM   2073  CG  LEU A 298     -13.791  10.517  42.390  1.00 41.32           C  
-ATOM   2074  CD1 LEU A 298     -12.451   9.964  42.824  1.00 42.22           C  
-ATOM   2075  CD2 LEU A 298     -14.402   9.609  41.334  1.00 44.48           C  
-ATOM   2076  N   GLY A 299     -17.870  11.732  44.895  1.00 44.40           N  
-ATOM   2077  CA  GLY A 299     -18.758  11.599  46.036  1.00 45.17           C  
-ATOM   2078  C   GLY A 299     -18.061  11.661  47.378  1.00 45.52           C  
-ATOM   2079  O   GLY A 299     -18.490  11.018  48.341  1.00 45.87           O  
-ATOM   2080  N   LEU A 300     -16.989  12.442  47.452  1.00 44.34           N  
-ATOM   2081  CA  LEU A 300     -16.242  12.568  48.691  1.00 42.86           C  
-ATOM   2082  C   LEU A 300     -16.176  14.012  49.157  1.00 42.40           C  
-ATOM   2083  O   LEU A 300     -16.295  14.943  48.359  1.00 43.01           O  
-ATOM   2084  CB  LEU A 300     -14.819  12.026  48.505  1.00 42.61           C  
-ATOM   2085  CG  LEU A 300     -14.671  10.574  48.036  1.00 42.75           C  
-ATOM   2086  CD1 LEU A 300     -13.197  10.234  47.877  1.00 41.55           C  
-ATOM   2087  CD2 LEU A 300     -15.325   9.634  49.039  1.00 42.34           C  
-ATOM   2088  N   ASN A 301     -15.999  14.193  50.460  1.00 42.35           N  
-ATOM   2089  CA  ASN A 301     -15.879  15.524  51.036  1.00 42.93           C  
-ATOM   2090  C   ASN A 301     -14.390  15.708  51.303  1.00 42.43           C  
-ATOM   2091  O   ASN A 301     -13.811  14.981  52.107  1.00 42.66           O  
-ATOM   2092  CB  ASN A 301     -16.653  15.616  52.353  1.00 44.49           C  
-ATOM   2093  CG  ASN A 301     -16.723  17.033  52.888  1.00 46.24           C  
-ATOM   2094  OD1 ASN A 301     -15.719  17.744  52.931  1.00 47.92           O  
-ATOM   2095  ND2 ASN A 301     -17.911  17.450  53.306  1.00 48.43           N  
-ATOM   2096  N   TRP A 302     -13.766  16.669  50.630  1.00 42.24           N  
-ATOM   2097  CA  TRP A 302     -12.338  16.885  50.817  1.00 42.63           C  
-ATOM   2098  C   TRP A 302     -11.986  17.348  52.225  1.00 44.17           C  
-ATOM   2099  O   TRP A 302     -10.857  17.153  52.688  1.00 43.96           O  
-ATOM   2100  CB  TRP A 302     -11.806  17.892  49.799  1.00 40.73           C  
-ATOM   2101  CG  TRP A 302     -12.399  19.256  49.904  1.00 39.14           C  
-ATOM   2102  CD1 TRP A 302     -13.467  19.746  49.205  1.00 36.85           C  
-ATOM   2103  CD2 TRP A 302     -11.923  20.332  50.720  1.00 37.85           C  
-ATOM   2104  NE1 TRP A 302     -13.679  21.064  49.530  1.00 35.68           N  
-ATOM   2105  CE2 TRP A 302     -12.747  21.450  50.457  1.00 37.11           C  
-ATOM   2106  CE3 TRP A 302     -10.879  20.462  51.646  1.00 37.82           C  
-ATOM   2107  CZ2 TRP A 302     -12.556  22.684  51.085  1.00 36.24           C  
-ATOM   2108  CZ3 TRP A 302     -10.690  21.690  52.271  1.00 37.61           C  
-ATOM   2109  CH2 TRP A 302     -11.527  22.785  51.986  1.00 37.07           C  
-ATOM   2110  N   LYS A 303     -12.953  17.955  52.907  1.00 44.72           N  
-ATOM   2111  CA  LYS A 303     -12.727  18.436  54.263  1.00 44.00           C  
-ATOM   2112  C   LYS A 303     -12.463  17.278  55.212  1.00 43.78           C  
-ATOM   2113  O   LYS A 303     -12.016  17.479  56.341  1.00 44.01           O  
-ATOM   2114  CB  LYS A 303     -13.926  19.261  54.737  1.00 44.45           C  
-ATOM   2115  CG  LYS A 303     -14.051  20.596  54.016  1.00 45.29           C  
-ATOM   2116  CD  LYS A 303     -15.238  21.403  54.497  1.00 46.32           C  
-ATOM   2117  CE  LYS A 303     -15.284  22.756  53.802  1.00 47.99           C  
-ATOM   2118  NZ  LYS A 303     -16.495  23.539  54.181  1.00 47.09           N  
-ATOM   2119  N   ASP A 304     -12.724  16.062  54.739  1.00 43.54           N  
-ATOM   2120  CA  ASP A 304     -12.502  14.868  55.542  1.00 43.88           C  
-ATOM   2121  C   ASP A 304     -11.137  14.235  55.291  1.00 43.44           C  
-ATOM   2122  O   ASP A 304     -10.814  13.212  55.893  1.00 44.65           O  
-ATOM   2123  CB  ASP A 304     -13.582  13.815  55.262  1.00 44.88           C  
-ATOM   2124  CG  ASP A 304     -14.942  14.206  55.805  1.00 47.28           C  
-ATOM   2125  OD1 ASP A 304     -15.036  14.555  57.002  1.00 49.23           O  
-ATOM   2126  OD2 ASP A 304     -15.923  14.155  55.036  1.00 49.31           O  
-ATOM   2127  N   TYR A 305     -10.336  14.826  54.406  1.00 43.38           N  
-ATOM   2128  CA  TYR A 305      -9.023  14.256  54.104  1.00 42.97           C  
-ATOM   2129  C   TYR A 305      -7.912  15.285  53.989  1.00 42.94           C  
-ATOM   2130  O   TYR A 305      -6.734  14.938  54.051  1.00 44.47           O  
-ATOM   2131  CB  TYR A 305      -9.064  13.464  52.793  1.00 42.36           C  
-ATOM   2132  CG  TYR A 305     -10.217  12.500  52.671  1.00 42.93           C  
-ATOM   2133  CD1 TYR A 305     -11.491  12.948  52.325  1.00 44.35           C  
-ATOM   2134  CD2 TYR A 305     -10.035  11.138  52.897  1.00 43.17           C  
-ATOM   2135  CE1 TYR A 305     -12.558  12.063  52.204  1.00 46.37           C  
-ATOM   2136  CE2 TYR A 305     -11.096  10.242  52.781  1.00 45.79           C  
-ATOM   2137  CZ  TYR A 305     -12.354  10.711  52.433  1.00 46.94           C  
-ATOM   2138  OH  TYR A 305     -13.402   9.828  52.305  1.00 51.14           O  
-ATOM   2139  N   VAL A 306      -8.287  16.544  53.807  1.00 42.33           N  
-ATOM   2140  CA  VAL A 306      -7.315  17.613  53.649  1.00 41.28           C  
-ATOM   2141  C   VAL A 306      -6.933  18.313  54.950  1.00 43.05           C  
-ATOM   2142  O   VAL A 306      -7.791  18.678  55.754  1.00 43.94           O  
-ATOM   2143  CB  VAL A 306      -7.840  18.671  52.650  1.00 39.61           C  
-ATOM   2144  CG1 VAL A 306      -6.917  19.875  52.625  1.00 38.31           C  
-ATOM   2145  CG2 VAL A 306      -7.952  18.060  51.266  1.00 39.08           C  
-ATOM   2146  N   GLU A 307      -5.630  18.492  55.141  1.00 43.67           N  
-ATOM   2147  CA  GLU A 307      -5.092  19.176  56.309  1.00 44.11           C  
-ATOM   2148  C   GLU A 307      -4.079  20.195  55.813  1.00 42.82           C  
-ATOM   2149  O   GLU A 307      -3.284  19.903  54.921  1.00 42.09           O  
-ATOM   2150  CB  GLU A 307      -4.414  18.184  57.256  1.00 47.84           C  
-ATOM   2151  CG  GLU A 307      -5.396  17.338  58.055  1.00 53.30           C  
-ATOM   2152  CD  GLU A 307      -4.706  16.329  58.951  1.00 56.47           C  
-ATOM   2153  OE1 GLU A 307      -3.909  16.749  59.820  1.00 58.67           O  
-ATOM   2154  OE2 GLU A 307      -4.964  15.115  58.787  1.00 59.25           O  
-ATOM   2155  N   ILE A 308      -4.115  21.393  56.383  1.00 42.77           N  
-ATOM   2156  CA  ILE A 308      -3.204  22.453  55.980  1.00 43.32           C  
-ATOM   2157  C   ILE A 308      -1.824  22.305  56.609  1.00 43.76           C  
-ATOM   2158  O   ILE A 308      -1.701  22.095  57.814  1.00 44.69           O  
-ATOM   2159  CB  ILE A 308      -3.777  23.830  56.346  1.00 44.08           C  
-ATOM   2160  CG1 ILE A 308      -5.150  24.001  55.694  1.00 44.97           C  
-ATOM   2161  CG2 ILE A 308      -2.834  24.930  55.887  1.00 44.42           C  
-ATOM   2162  CD1 ILE A 308      -5.142  23.818  54.188  1.00 45.17           C  
-ATOM   2163  N   ASP A 309      -0.789  22.411  55.778  1.00 43.60           N  
-ATOM   2164  CA  ASP A 309       0.594  22.295  56.234  1.00 42.08           C  
-ATOM   2165  C   ASP A 309       1.350  23.572  55.880  1.00 41.61           C  
-ATOM   2166  O   ASP A 309       1.593  23.857  54.708  1.00 42.57           O  
-ATOM   2167  CB  ASP A 309       1.261  21.075  55.584  1.00 42.19           C  
-ATOM   2168  CG  ASP A 309       2.718  20.895  56.008  1.00 43.56           C  
-ATOM   2169  OD1 ASP A 309       3.258  19.787  55.794  1.00 44.18           O  
-ATOM   2170  OD2 ASP A 309       3.330  21.848  56.541  1.00 44.90           O  
-ATOM   2171  N   GLN A 310       1.718  24.327  56.911  1.00 40.44           N  
-ATOM   2172  CA  GLN A 310       2.427  25.594  56.763  1.00 40.74           C  
-ATOM   2173  C   GLN A 310       3.610  25.559  55.800  1.00 40.80           C  
-ATOM   2174  O   GLN A 310       3.986  26.587  55.238  1.00 40.86           O  
-ATOM   2175  CB  GLN A 310       2.896  26.083  58.134  1.00 38.93           C  
-ATOM   2176  N   ARG A 311       4.193  24.383  55.603  1.00 40.45           N  
-ATOM   2177  CA  ARG A 311       5.342  24.253  54.716  1.00 41.62           C  
-ATOM   2178  C   ARG A 311       5.017  24.421  53.230  1.00 41.96           C  
-ATOM   2179  O   ARG A 311       5.912  24.693  52.428  1.00 42.66           O  
-ATOM   2180  CB  ARG A 311       6.021  22.903  54.942  1.00 43.67           C  
-ATOM   2181  CG  ARG A 311       6.495  22.695  56.376  1.00 47.54           C  
-ATOM   2182  CD  ARG A 311       7.033  21.292  56.575  1.00 48.27           C  
-ATOM   2183  NE  ARG A 311       6.056  20.284  56.175  1.00 50.21           N  
-ATOM   2184  CZ  ARG A 311       6.246  18.973  56.288  1.00 52.17           C  
-ATOM   2185  NH1 ARG A 311       7.383  18.508  56.795  1.00 52.26           N  
-ATOM   2186  NH2 ARG A 311       5.304  18.126  55.890  1.00 52.01           N  
-ATOM   2187  N   TYR A 312       3.747  24.272  52.859  1.00 40.42           N  
-ATOM   2188  CA  TYR A 312       3.359  24.402  51.461  1.00 38.42           C  
-ATOM   2189  C   TYR A 312       2.962  25.815  51.074  1.00 38.83           C  
-ATOM   2190  O   TYR A 312       2.485  26.053  49.966  1.00 38.67           O  
-ATOM   2191  CB  TYR A 312       2.234  23.419  51.134  1.00 37.55           C  
-ATOM   2192  CG  TYR A 312       2.684  21.983  51.231  1.00 37.24           C  
-ATOM   2193  CD1 TYR A 312       1.970  21.054  51.982  1.00 36.95           C  
-ATOM   2194  CD2 TYR A 312       3.867  21.565  50.620  1.00 39.20           C  
-ATOM   2195  CE1 TYR A 312       2.429  19.746  52.135  1.00 38.50           C  
-ATOM   2196  CE2 TYR A 312       4.332  20.258  50.765  1.00 39.86           C  
-ATOM   2197  CZ  TYR A 312       3.610  19.357  51.526  1.00 39.52           C  
-ATOM   2198  OH  TYR A 312       4.083  18.077  51.696  1.00 42.57           O  
-ATOM   2199  N   PHE A 313       3.163  26.752  51.994  1.00 38.05           N  
-ATOM   2200  CA  PHE A 313       2.860  28.152  51.738  1.00 37.60           C  
-ATOM   2201  C   PHE A 313       4.134  28.793  51.188  1.00 37.34           C  
-ATOM   2202  O   PHE A 313       5.226  28.514  51.674  1.00 36.51           O  
-ATOM   2203  CB  PHE A 313       2.445  28.849  53.034  1.00 38.80           C  
-ATOM   2204  CG  PHE A 313       1.056  28.504  53.495  1.00 42.05           C  
-ATOM   2205  CD1 PHE A 313      -0.034  29.270  53.098  1.00 43.36           C  
-ATOM   2206  CD2 PHE A 313       0.835  27.409  54.325  1.00 43.50           C  
-ATOM   2207  CE1 PHE A 313      -1.328  28.953  53.523  1.00 44.06           C  
-ATOM   2208  CE2 PHE A 313      -0.454  27.083  54.754  1.00 43.49           C  
-ATOM   2209  CZ  PHE A 313      -1.535  27.856  54.352  1.00 42.69           C  
-ATOM   2210  N   ARG A 314       3.998  29.639  50.172  1.00 36.05           N  
-ATOM   2211  CA  ARG A 314       5.156  30.303  49.582  1.00 36.12           C  
-ATOM   2212  C   ARG A 314       5.485  31.602  50.331  1.00 35.20           C  
-ATOM   2213  O   ARG A 314       4.587  32.294  50.816  1.00 35.31           O  
-ATOM   2214  CB  ARG A 314       4.905  30.613  48.092  1.00 35.40           C  
-ATOM   2215  CG  ARG A 314       4.915  29.397  47.144  1.00 36.25           C  
-ATOM   2216  CD  ARG A 314       3.618  28.586  47.204  1.00 35.03           C  
-ATOM   2217  NE  ARG A 314       3.678  27.337  46.433  1.00 33.19           N  
-ATOM   2218  CZ  ARG A 314       3.534  27.239  45.110  1.00 30.42           C  
-ATOM   2219  NH1 ARG A 314       3.609  26.049  44.526  1.00 27.79           N  
-ATOM   2220  NH2 ARG A 314       3.311  28.319  44.369  1.00 25.92           N  
-ATOM   2221  N   PRO A 315       6.782  31.943  50.438  1.00 33.65           N  
-ATOM   2222  CA  PRO A 315       7.221  33.162  51.127  1.00 32.36           C  
-ATOM   2223  C   PRO A 315       6.463  34.390  50.624  1.00 32.80           C  
-ATOM   2224  O   PRO A 315       6.155  35.300  51.386  1.00 33.70           O  
-ATOM   2225  CB  PRO A 315       8.707  33.223  50.796  1.00 32.13           C  
-ATOM   2226  CG  PRO A 315       9.087  31.776  50.749  1.00 33.04           C  
-ATOM   2227  CD  PRO A 315       7.941  31.162  49.966  1.00 33.84           C  
-ATOM   2228  N   ALA A 316       6.181  34.411  49.327  1.00 33.13           N  
-ATOM   2229  CA  ALA A 316       5.436  35.502  48.712  1.00 32.97           C  
-ATOM   2230  C   ALA A 316       4.433  34.808  47.794  1.00 33.54           C  
-ATOM   2231  O   ALA A 316       4.816  34.021  46.931  1.00 34.18           O  
-ATOM   2232  CB  ALA A 316       6.371  36.409  47.916  1.00 32.66           C  
-ATOM   2233  N   GLU A 317       3.151  35.095  47.989  1.00 33.31           N  
-ATOM   2234  CA  GLU A 317       2.095  34.451  47.217  1.00 33.37           C  
-ATOM   2235  C   GLU A 317       1.553  35.259  46.042  1.00 33.03           C  
-ATOM   2236  O   GLU A 317       1.671  36.487  45.993  1.00 34.64           O  
-ATOM   2237  CB  GLU A 317       0.943  34.079  48.165  1.00 33.89           C  
-ATOM   2238  CG  GLU A 317      -0.268  33.383  47.527  1.00 36.26           C  
-ATOM   2239  CD  GLU A 317       0.062  32.016  46.938  1.00 36.95           C  
-ATOM   2240  OE1 GLU A 317       0.678  31.966  45.851  1.00 38.10           O  
-ATOM   2241  OE2 GLU A 317      -0.291  30.993  47.565  1.00 36.21           O  
-ATOM   2242  N   VAL A 318       0.981  34.538  45.083  1.00 33.21           N  
-ATOM   2243  CA  VAL A 318       0.353  35.133  43.907  1.00 33.55           C  
-ATOM   2244  C   VAL A 318      -1.117  34.838  44.163  1.00 33.60           C  
-ATOM   2245  O   VAL A 318      -1.567  33.695  44.049  1.00 32.11           O  
-ATOM   2246  CB  VAL A 318       0.807  34.450  42.600  1.00 32.23           C  
-ATOM   2247  CG1 VAL A 318      -0.019  34.970  41.432  1.00 31.73           C  
-ATOM   2248  CG2 VAL A 318       2.280  34.723  42.364  1.00 30.14           C  
-ATOM   2249  N   ASP A 319      -1.852  35.881  44.521  1.00 35.04           N  
-ATOM   2250  CA  ASP A 319      -3.257  35.761  44.879  1.00 35.28           C  
-ATOM   2251  C   ASP A 319      -4.286  35.456  43.813  1.00 35.10           C  
-ATOM   2252  O   ASP A 319      -5.070  34.521  43.962  1.00 34.70           O  
-ATOM   2253  CB  ASP A 319      -3.694  37.025  45.627  1.00 36.11           C  
-ATOM   2254  CG  ASP A 319      -3.044  37.146  46.991  1.00 37.56           C  
-ATOM   2255  OD1 ASP A 319      -3.119  38.237  47.599  1.00 40.74           O  
-ATOM   2256  OD2 ASP A 319      -2.459  36.146  47.457  1.00 38.15           O  
-ATOM   2257  N   ASN A 320      -4.297  36.237  42.742  1.00 35.97           N  
-ATOM   2258  CA  ASN A 320      -5.320  36.047  41.730  1.00 37.38           C  
-ATOM   2259  C   ASN A 320      -4.876  36.254  40.292  1.00 36.42           C  
-ATOM   2260  O   ASN A 320      -4.391  37.321  39.917  1.00 36.75           O  
-ATOM   2261  CB  ASN A 320      -6.493  36.975  42.070  1.00 41.66           C  
-ATOM   2262  CG  ASN A 320      -7.657  36.826  41.124  1.00 44.23           C  
-ATOM   2263  OD1 ASN A 320      -7.975  35.724  40.677  1.00 45.86           O  
-ATOM   2264  ND2 ASN A 320      -8.321  37.938  40.831  1.00 46.78           N  
-ATOM   2265  N   LEU A 321      -5.057  35.216  39.486  1.00 35.71           N  
-ATOM   2266  CA  LEU A 321      -4.687  35.271  38.084  1.00 34.90           C  
-ATOM   2267  C   LEU A 321      -5.850  34.890  37.181  1.00 35.37           C  
-ATOM   2268  O   LEU A 321      -6.443  33.814  37.317  1.00 35.81           O  
-ATOM   2269  CB  LEU A 321      -3.499  34.346  37.808  1.00 34.19           C  
-ATOM   2270  CG  LEU A 321      -2.182  34.718  38.488  1.00 32.35           C  
-ATOM   2271  CD1 LEU A 321      -1.138  33.646  38.205  1.00 31.07           C  
-ATOM   2272  CD2 LEU A 321      -1.707  36.067  37.977  1.00 32.28           C  
-ATOM   2273  N   GLN A 322      -6.186  35.803  36.278  1.00 35.29           N  
-ATOM   2274  CA  GLN A 322      -7.248  35.593  35.301  1.00 35.10           C  
-ATOM   2275  C   GLN A 322      -6.801  36.358  34.077  1.00 32.67           C  
-ATOM   2276  O   GLN A 322      -6.651  37.573  34.119  1.00 32.18           O  
-ATOM   2277  CB  GLN A 322      -8.595  36.139  35.779  1.00 38.10           C  
-ATOM   2278  CG  GLN A 322      -9.700  35.898  34.754  1.00 41.51           C  
-ATOM   2279  CD  GLN A 322     -11.057  36.392  35.200  1.00 44.46           C  
-ATOM   2280  OE1 GLN A 322     -11.617  35.910  36.184  1.00 45.35           O  
-ATOM   2281  NE2 GLN A 322     -11.598  37.360  34.470  1.00 46.63           N  
-ATOM   2282  N   GLY A 323      -6.577  35.644  32.986  1.00 32.76           N  
-ATOM   2283  CA  GLY A 323      -6.108  36.307  31.788  1.00 33.95           C  
-ATOM   2284  C   GLY A 323      -7.157  36.840  30.838  1.00 33.86           C  
-ATOM   2285  O   GLY A 323      -8.348  36.526  30.920  1.00 33.90           O  
-ATOM   2286  N   ASP A 324      -6.686  37.687  29.938  1.00 33.81           N  
-ATOM   2287  CA  ASP A 324      -7.512  38.270  28.902  1.00 32.30           C  
-ATOM   2288  C   ASP A 324      -6.850  37.759  27.639  1.00 31.46           C  
-ATOM   2289  O   ASP A 324      -5.803  38.258  27.239  1.00 32.02           O  
-ATOM   2290  CB  ASP A 324      -7.445  39.793  28.949  1.00 33.80           C  
-ATOM   2291  CG  ASP A 324      -8.051  40.439  27.721  1.00 33.83           C  
-ATOM   2292  OD1 ASP A 324      -8.032  41.685  27.638  1.00 36.74           O  
-ATOM   2293  OD2 ASP A 324      -8.543  39.701  26.839  1.00 32.23           O  
-ATOM   2294  N   ALA A 325      -7.451  36.747  27.029  1.00 31.23           N  
-ATOM   2295  CA  ALA A 325      -6.902  36.147  25.821  1.00 31.39           C  
-ATOM   2296  C   ALA A 325      -7.607  36.631  24.557  1.00 32.74           C  
-ATOM   2297  O   ALA A 325      -7.783  35.864  23.610  1.00 31.74           O  
-ATOM   2298  CB  ALA A 325      -6.991  34.625  25.920  1.00 30.57           C  
-ATOM   2299  N   SER A 326      -8.005  37.901  24.545  1.00 33.09           N  
-ATOM   2300  CA  SER A 326      -8.688  38.477  23.389  1.00 34.16           C  
-ATOM   2301  C   SER A 326      -7.793  38.442  22.167  1.00 34.16           C  
-ATOM   2302  O   SER A 326      -8.173  37.926  21.118  1.00 34.63           O  
-ATOM   2303  CB  SER A 326      -9.085  39.930  23.662  1.00 33.32           C  
-ATOM   2304  OG  SER A 326     -10.072  40.001  24.668  1.00 36.56           O  
-ATOM   2305  N   LYS A 327      -6.598  38.999  22.322  1.00 34.31           N  
-ATOM   2306  CA  LYS A 327      -5.630  39.066  21.241  1.00 34.98           C  
-ATOM   2307  C   LYS A 327      -5.362  37.714  20.590  1.00 34.33           C  
-ATOM   2308  O   LYS A 327      -5.255  37.622  19.371  1.00 35.78           O  
-ATOM   2309  CB  LYS A 327      -4.323  39.674  21.759  1.00 35.64           C  
-ATOM   2310  CG  LYS A 327      -3.262  39.883  20.690  1.00 34.85           C  
-ATOM   2311  CD  LYS A 327      -2.041  40.565  21.275  1.00 33.60           C  
-ATOM   2312  CE  LYS A 327      -0.945  40.724  20.242  1.00 32.39           C  
-ATOM   2313  NZ  LYS A 327       0.225  41.414  20.846  1.00 35.85           N  
-ATOM   2314  N   ALA A 328      -5.250  36.663  21.392  1.00 34.99           N  
-ATOM   2315  CA  ALA A 328      -4.999  35.334  20.841  1.00 34.98           C  
-ATOM   2316  C   ALA A 328      -6.190  34.872  19.997  1.00 35.43           C  
-ATOM   2317  O   ALA A 328      -6.018  34.329  18.901  1.00 34.12           O  
-ATOM   2318  CB  ALA A 328      -4.738  34.338  21.963  1.00 35.27           C  
-ATOM   2319  N   LYS A 329      -7.396  35.090  20.510  1.00 34.98           N  
-ATOM   2320  CA  LYS A 329      -8.600  34.696  19.791  1.00 36.68           C  
-ATOM   2321  C   LYS A 329      -8.744  35.496  18.499  1.00 36.59           C  
-ATOM   2322  O   LYS A 329      -9.059  34.944  17.451  1.00 36.76           O  
-ATOM   2323  CB  LYS A 329      -9.840  34.914  20.661  1.00 38.15           C  
-ATOM   2324  CG  LYS A 329     -11.144  34.548  19.961  1.00 41.23           C  
-ATOM   2325  CD  LYS A 329     -12.366  34.829  20.832  1.00 42.52           C  
-ATOM   2326  CE  LYS A 329     -13.652  34.425  20.118  1.00 44.61           C  
-ATOM   2327  NZ  LYS A 329     -14.884  34.698  20.915  1.00 45.23           N  
-ATOM   2328  N   GLU A 330      -8.494  36.797  18.585  1.00 36.30           N  
-ATOM   2329  CA  GLU A 330      -8.613  37.690  17.441  1.00 36.58           C  
-ATOM   2330  C   GLU A 330      -7.542  37.510  16.367  1.00 36.32           C  
-ATOM   2331  O   GLU A 330      -7.850  37.511  15.176  1.00 36.91           O  
-ATOM   2332  CB  GLU A 330      -8.621  39.137  17.926  1.00 36.90           C  
-ATOM   2333  N   VAL A 331      -6.288  37.357  16.782  1.00 36.20           N  
-ATOM   2334  CA  VAL A 331      -5.187  37.198  15.834  1.00 34.54           C  
-ATOM   2335  C   VAL A 331      -4.831  35.753  15.486  1.00 34.31           C  
-ATOM   2336  O   VAL A 331      -4.509  35.452  14.339  1.00 34.07           O  
-ATOM   2337  CB  VAL A 331      -3.913  37.901  16.349  1.00 34.01           C  
-ATOM   2338  CG1 VAL A 331      -2.809  37.822  15.303  1.00 34.29           C  
-ATOM   2339  CG2 VAL A 331      -4.228  39.344  16.689  1.00 34.37           C  
-ATOM   2340  N   LEU A 332      -4.883  34.861  16.469  1.00 33.24           N  
-ATOM   2341  CA  LEU A 332      -4.546  33.460  16.229  1.00 32.80           C  
-ATOM   2342  C   LEU A 332      -5.777  32.592  15.973  1.00 32.78           C  
-ATOM   2343  O   LEU A 332      -5.659  31.461  15.506  1.00 33.98           O  
-ATOM   2344  CB  LEU A 332      -3.784  32.892  17.428  1.00 31.11           C  
-ATOM   2345  CG  LEU A 332      -2.567  33.675  17.914  1.00 30.04           C  
-ATOM   2346  CD1 LEU A 332      -1.993  32.987  19.142  1.00 30.97           C  
-ATOM   2347  CD2 LEU A 332      -1.533  33.767  16.810  1.00 27.73           C  
-ATOM   2348  N   GLY A 333      -6.955  33.120  16.282  1.00 33.53           N  
-ATOM   2349  CA  GLY A 333      -8.170  32.348  16.094  1.00 33.70           C  
-ATOM   2350  C   GLY A 333      -8.165  31.183  17.065  1.00 34.09           C  
-ATOM   2351  O   GLY A 333      -8.844  30.177  16.864  1.00 34.22           O  
-ATOM   2352  N   TRP A 334      -7.382  31.335  18.127  1.00 34.73           N  
-ATOM   2353  CA  TRP A 334      -7.244  30.318  19.159  1.00 34.98           C  
-ATOM   2354  C   TRP A 334      -8.258  30.491  20.277  1.00 35.14           C  
-ATOM   2355  O   TRP A 334      -8.563  31.608  20.690  1.00 36.33           O  
-ATOM   2356  CB  TRP A 334      -5.838  30.364  19.772  1.00 34.17           C  
-ATOM   2357  CG  TRP A 334      -5.639  29.326  20.838  1.00 32.22           C  
-ATOM   2358  CD1 TRP A 334      -5.201  28.045  20.664  1.00 30.41           C  
-ATOM   2359  CD2 TRP A 334      -5.967  29.452  22.225  1.00 29.78           C  
-ATOM   2360  NE1 TRP A 334      -5.242  27.363  21.854  1.00 29.24           N  
-ATOM   2361  CE2 TRP A 334      -5.708  28.203  22.830  1.00 29.53           C  
-ATOM   2362  CE3 TRP A 334      -6.459  30.499  23.015  1.00 28.81           C  
-ATOM   2363  CZ2 TRP A 334      -5.924  27.970  24.190  1.00 27.34           C  
-ATOM   2364  CZ3 TRP A 334      -6.674  30.270  24.367  1.00 28.78           C  
-ATOM   2365  CH2 TRP A 334      -6.405  29.013  24.941  1.00 29.26           C  
-ATOM   2366  N   LYS A 335      -8.753  29.369  20.780  1.00 36.30           N  
-ATOM   2367  CA  LYS A 335      -9.714  29.365  21.869  1.00 36.33           C  
-ATOM   2368  C   LYS A 335      -9.605  28.025  22.594  1.00 36.92           C  
-ATOM   2369  O   LYS A 335      -9.385  26.990  21.964  1.00 37.02           O  
-ATOM   2370  CB  LYS A 335     -11.123  29.557  21.326  1.00 37.50           C  
-ATOM   2371  N   PRO A 336      -9.737  28.029  23.931  1.00 36.44           N  
-ATOM   2372  CA  PRO A 336      -9.649  26.783  24.695  1.00 36.32           C  
-ATOM   2373  C   PRO A 336     -10.846  25.884  24.405  1.00 37.12           C  
-ATOM   2374  O   PRO A 336     -11.967  26.362  24.270  1.00 38.73           O  
-ATOM   2375  CB  PRO A 336      -9.616  27.269  26.143  1.00 36.68           C  
-ATOM   2376  CG  PRO A 336     -10.423  28.528  26.094  1.00 35.40           C  
-ATOM   2377  CD  PRO A 336      -9.924  29.185  24.828  1.00 35.21           C  
-ATOM   2378  N   GLN A 337     -10.605  24.584  24.305  1.00 37.20           N  
-ATOM   2379  CA  GLN A 337     -11.675  23.637  24.023  1.00 38.20           C  
-ATOM   2380  C   GLN A 337     -12.154  23.007  25.326  1.00 37.59           C  
-ATOM   2381  O   GLN A 337     -13.347  22.790  25.525  1.00 38.86           O  
-ATOM   2382  CB  GLN A 337     -11.169  22.540  23.086  1.00 39.34           C  
-ATOM   2383  CG  GLN A 337     -10.307  23.055  21.943  1.00 44.89           C  
-ATOM   2384  CD  GLN A 337      -9.458  21.963  21.299  1.00 48.81           C  
-ATOM   2385  OE1 GLN A 337      -8.446  22.250  20.649  1.00 49.01           O  
-ATOM   2386  NE2 GLN A 337      -9.869  20.707  21.471  1.00 49.37           N  
-ATOM   2387  N   VAL A 338     -11.212  22.726  26.217  1.00 35.56           N  
-ATOM   2388  CA  VAL A 338     -11.526  22.099  27.490  1.00 34.43           C  
-ATOM   2389  C   VAL A 338     -11.736  23.123  28.600  1.00 34.53           C  
-ATOM   2390  O   VAL A 338     -10.859  23.942  28.878  1.00 36.56           O  
-ATOM   2391  CB  VAL A 338     -10.401  21.123  27.894  1.00 34.14           C  
-ATOM   2392  CG1 VAL A 338     -10.718  20.472  29.233  1.00 35.84           C  
-ATOM   2393  CG2 VAL A 338     -10.228  20.070  26.809  1.00 31.08           C  
-ATOM   2394  N   GLY A 339     -12.908  23.069  29.229  1.00 34.33           N  
-ATOM   2395  CA  GLY A 339     -13.227  23.991  30.305  1.00 33.29           C  
-ATOM   2396  C   GLY A 339     -12.778  23.488  31.667  1.00 33.43           C  
-ATOM   2397  O   GLY A 339     -12.299  22.365  31.804  1.00 33.02           O  
-ATOM   2398  N   PHE A 340     -12.950  24.323  32.683  1.00 32.55           N  
-ATOM   2399  CA  PHE A 340     -12.544  23.986  34.037  1.00 33.33           C  
-ATOM   2400  C   PHE A 340     -12.986  22.605  34.526  1.00 34.83           C  
-ATOM   2401  O   PHE A 340     -12.154  21.715  34.696  1.00 37.35           O  
-ATOM   2402  CB  PHE A 340     -13.044  25.058  35.005  1.00 31.93           C  
-ATOM   2403  CG  PHE A 340     -12.620  24.835  36.422  1.00 31.58           C  
-ATOM   2404  CD1 PHE A 340     -13.568  24.719  37.434  1.00 32.18           C  
-ATOM   2405  CD2 PHE A 340     -11.273  24.726  36.748  1.00 31.35           C  
-ATOM   2406  CE1 PHE A 340     -13.182  24.496  38.754  1.00 33.11           C  
-ATOM   2407  CE2 PHE A 340     -10.875  24.501  38.065  1.00 32.91           C  
-ATOM   2408  CZ  PHE A 340     -11.831  24.385  39.069  1.00 32.78           C  
-ATOM   2409  N   GLU A 341     -14.283  22.423  34.761  1.00 35.84           N  
-ATOM   2410  CA  GLU A 341     -14.780  21.140  35.256  1.00 36.99           C  
-ATOM   2411  C   GLU A 341     -14.368  19.963  34.384  1.00 35.95           C  
-ATOM   2412  O   GLU A 341     -13.984  18.913  34.891  1.00 35.46           O  
-ATOM   2413  CB  GLU A 341     -16.305  21.170  35.406  1.00 39.31           C  
-ATOM   2414  CG  GLU A 341     -16.776  21.980  36.603  1.00 43.29           C  
-ATOM   2415  CD  GLU A 341     -18.251  21.786  36.902  1.00 45.27           C  
-ATOM   2416  OE1 GLU A 341     -18.689  20.618  37.007  1.00 45.70           O  
-ATOM   2417  OE2 GLU A 341     -18.969  22.802  37.039  1.00 46.61           O  
-ATOM   2418  N   LYS A 342     -14.445  20.136  33.072  1.00 35.17           N  
-ATOM   2419  CA  LYS A 342     -14.060  19.072  32.159  1.00 35.76           C  
-ATOM   2420  C   LYS A 342     -12.601  18.701  32.428  1.00 34.62           C  
-ATOM   2421  O   LYS A 342     -12.248  17.522  32.470  1.00 34.90           O  
-ATOM   2422  CB  LYS A 342     -14.233  19.539  30.711  1.00 37.98           C  
-ATOM   2423  CG  LYS A 342     -13.957  18.474  29.659  1.00 42.56           C  
-ATOM   2424  CD  LYS A 342     -14.087  19.065  28.265  1.00 46.58           C  
-ATOM   2425  CE  LYS A 342     -13.748  18.060  27.179  1.00 48.41           C  
-ATOM   2426  NZ  LYS A 342     -13.632  18.724  25.840  1.00 50.98           N  
-ATOM   2427  N   LEU A 343     -11.760  19.715  32.622  1.00 33.66           N  
-ATOM   2428  CA  LEU A 343     -10.341  19.493  32.890  1.00 32.91           C  
-ATOM   2429  C   LEU A 343     -10.166  18.707  34.184  1.00 33.73           C  
-ATOM   2430  O   LEU A 343      -9.409  17.736  34.236  1.00 32.57           O  
-ATOM   2431  CB  LEU A 343      -9.604  20.831  33.009  1.00 32.06           C  
-ATOM   2432  CG  LEU A 343      -8.128  20.757  33.418  1.00 30.72           C  
-ATOM   2433  CD1 LEU A 343      -7.290  20.187  32.275  1.00 28.56           C  
-ATOM   2434  CD2 LEU A 343      -7.644  22.144  33.797  1.00 28.24           C  
-ATOM   2435  N   VAL A 344     -10.875  19.131  35.226  1.00 33.55           N  
-ATOM   2436  CA  VAL A 344     -10.793  18.467  36.518  1.00 33.88           C  
-ATOM   2437  C   VAL A 344     -11.219  17.003  36.437  1.00 33.69           C  
-ATOM   2438  O   VAL A 344     -10.514  16.118  36.921  1.00 34.94           O  
-ATOM   2439  CB  VAL A 344     -11.670  19.183  37.573  1.00 33.28           C  
-ATOM   2440  CG1 VAL A 344     -11.583  18.456  38.907  1.00 31.96           C  
-ATOM   2441  CG2 VAL A 344     -11.213  20.622  37.737  1.00 35.87           C  
-ATOM   2442  N   LYS A 345     -12.370  16.749  35.823  1.00 34.54           N  
-ATOM   2443  CA  LYS A 345     -12.871  15.388  35.702  1.00 34.07           C  
-ATOM   2444  C   LYS A 345     -11.932  14.532  34.874  1.00 33.70           C  
-ATOM   2445  O   LYS A 345     -11.764  13.343  35.145  1.00 33.68           O  
-ATOM   2446  CB  LYS A 345     -14.282  15.396  35.105  1.00 35.58           C  
-ATOM   2447  CG  LYS A 345     -15.291  16.075  36.028  1.00 37.66           C  
-ATOM   2448  CD  LYS A 345     -16.695  16.134  35.447  1.00 40.56           C  
-ATOM   2449  CE  LYS A 345     -17.609  16.959  36.351  1.00 40.46           C  
-ATOM   2450  NZ  LYS A 345     -18.970  17.158  35.774  1.00 41.75           N  
-ATOM   2451  N   MET A 346     -11.306  15.146  33.876  1.00 34.03           N  
-ATOM   2452  CA  MET A 346     -10.358  14.441  33.021  1.00 34.24           C  
-ATOM   2453  C   MET A 346      -9.207  13.916  33.876  1.00 34.31           C  
-ATOM   2454  O   MET A 346      -8.861  12.731  33.821  1.00 34.88           O  
-ATOM   2455  CB  MET A 346      -9.795  15.387  31.957  1.00 33.99           C  
-ATOM   2456  CG  MET A 346      -8.729  14.756  31.071  1.00 35.30           C  
-ATOM   2457  SD  MET A 346      -7.802  15.979  30.109  1.00 38.01           S  
-ATOM   2458  CE  MET A 346      -9.039  16.453  28.884  1.00 35.71           C  
-ATOM   2459  N   MET A 347      -8.618  14.814  34.661  1.00 32.73           N  
-ATOM   2460  CA  MET A 347      -7.498  14.466  35.528  1.00 32.56           C  
-ATOM   2461  C   MET A 347      -7.892  13.451  36.593  1.00 30.31           C  
-ATOM   2462  O   MET A 347      -7.145  12.519  36.856  1.00 31.90           O  
-ATOM   2463  CB  MET A 347      -6.920  15.725  36.178  1.00 30.20           C  
-ATOM   2464  CG  MET A 347      -6.292  16.692  35.184  1.00 27.40           C  
-ATOM   2465  SD  MET A 347      -5.648  18.182  35.985  1.00 28.47           S  
-ATOM   2466  CE  MET A 347      -4.183  17.530  36.752  1.00 24.49           C  
-ATOM   2467  N   VAL A 348      -9.060  13.630  37.200  1.00 31.88           N  
-ATOM   2468  CA  VAL A 348      -9.539  12.695  38.217  1.00 31.53           C  
-ATOM   2469  C   VAL A 348      -9.725  11.295  37.629  1.00 32.78           C  
-ATOM   2470  O   VAL A 348      -9.331  10.305  38.247  1.00 33.59           O  
-ATOM   2471  CB  VAL A 348     -10.886  13.153  38.824  1.00 32.33           C  
-ATOM   2472  CG1 VAL A 348     -11.452  12.063  39.714  1.00 30.83           C  
-ATOM   2473  CG2 VAL A 348     -10.688  14.431  39.633  1.00 31.19           C  
-ATOM   2474  N   ASP A 349     -10.317  11.215  36.436  1.00 33.17           N  
-ATOM   2475  CA  ASP A 349     -10.549   9.926  35.780  1.00 34.01           C  
-ATOM   2476  C   ASP A 349      -9.254   9.144  35.581  1.00 33.23           C  
-ATOM   2477  O   ASP A 349      -9.175   7.967  35.930  1.00 32.65           O  
-ATOM   2478  CB  ASP A 349     -11.220  10.099  34.405  1.00 34.86           C  
-ATOM   2479  CG  ASP A 349     -12.665  10.552  34.499  1.00 36.74           C  
-ATOM   2480  OD1 ASP A 349     -13.304  10.331  35.546  1.00 37.55           O  
-ATOM   2481  OD2 ASP A 349     -13.170  11.119  33.508  1.00 39.24           O  
-ATOM   2482  N   GLU A 350      -8.246   9.791  35.003  1.00 33.25           N  
-ATOM   2483  CA  GLU A 350      -6.968   9.129  34.758  1.00 34.14           C  
-ATOM   2484  C   GLU A 350      -6.273   8.708  36.043  1.00 33.23           C  
-ATOM   2485  O   GLU A 350      -5.776   7.586  36.147  1.00 34.42           O  
-ATOM   2486  CB  GLU A 350      -6.032  10.037  33.953  1.00 36.42           C  
-ATOM   2487  CG  GLU A 350      -6.440  10.227  32.501  1.00 43.19           C  
-ATOM   2488  CD  GLU A 350      -6.600   8.907  31.758  1.00 45.90           C  
-ATOM   2489  OE1 GLU A 350      -5.636   8.111  31.725  1.00 46.66           O  
-ATOM   2490  OE2 GLU A 350      -7.693   8.667  31.203  1.00 49.28           O  
-ATOM   2491  N   ASP A 351      -6.236   9.605  37.022  1.00 32.38           N  
-ATOM   2492  CA  ASP A 351      -5.577   9.292  38.282  1.00 33.39           C  
-ATOM   2493  C   ASP A 351      -6.326   8.249  39.106  1.00 33.30           C  
-ATOM   2494  O   ASP A 351      -5.723   7.553  39.920  1.00 34.09           O  
-ATOM   2495  CB  ASP A 351      -5.337  10.576  39.092  1.00 31.50           C  
-ATOM   2496  CG  ASP A 351      -4.048  11.299  38.672  1.00 31.85           C  
-ATOM   2497  OD1 ASP A 351      -3.863  12.487  39.033  1.00 30.86           O  
-ATOM   2498  OD2 ASP A 351      -3.213  10.670  37.982  1.00 29.06           O  
-ATOM   2499  N   LEU A 352      -7.633   8.128  38.887  1.00 33.90           N  
-ATOM   2500  CA  LEU A 352      -8.421   7.134  39.608  1.00 34.27           C  
-ATOM   2501  C   LEU A 352      -8.077   5.761  39.040  1.00 35.05           C  
-ATOM   2502  O   LEU A 352      -7.860   4.793  39.779  1.00 34.65           O  
-ATOM   2503  CB  LEU A 352      -9.920   7.399  39.432  1.00 33.35           C  
-ATOM   2504  CG  LEU A 352     -10.839   6.335  40.037  1.00 32.31           C  
-ATOM   2505  CD1 LEU A 352     -10.574   6.224  41.529  1.00 33.49           C  
-ATOM   2506  CD2 LEU A 352     -12.289   6.697  39.783  1.00 32.59           C  
-ATOM   2507  N   GLU A 353      -8.025   5.689  37.716  1.00 34.78           N  
-ATOM   2508  CA  GLU A 353      -7.705   4.450  37.027  1.00 35.42           C  
-ATOM   2509  C   GLU A 353      -6.267   4.046  37.357  1.00 35.91           C  
-ATOM   2510  O   GLU A 353      -5.951   2.863  37.489  1.00 34.80           O  
-ATOM   2511  CB  GLU A 353      -7.881   4.646  35.521  1.00 36.90           C  
-ATOM   2512  CG  GLU A 353      -7.745   3.381  34.700  1.00 42.35           C  
-ATOM   2513  CD  GLU A 353      -8.638   2.261  35.199  1.00 43.46           C  
-ATOM   2514  OE1 GLU A 353      -9.842   2.510  35.444  1.00 43.84           O  
-ATOM   2515  OE2 GLU A 353      -8.126   1.127  35.339  1.00 45.25           O  
-ATOM   2516  N   LEU A 354      -5.398   5.042  37.495  1.00 34.63           N  
-ATOM   2517  CA  LEU A 354      -4.004   4.789  37.826  1.00 35.36           C  
-ATOM   2518  C   LEU A 354      -3.944   4.248  39.253  1.00 34.16           C  
-ATOM   2519  O   LEU A 354      -3.253   3.271  39.532  1.00 33.41           O  
-ATOM   2520  CB  LEU A 354      -3.194   6.089  37.706  1.00 35.83           C  
-ATOM   2521  CG  LEU A 354      -1.697   6.055  38.019  1.00 36.90           C  
-ATOM   2522  CD1 LEU A 354      -0.989   5.048  37.127  1.00 36.34           C  
-ATOM   2523  CD2 LEU A 354      -1.118   7.448  37.815  1.00 37.95           C  
-ATOM   2524  N   ALA A 355      -4.687   4.883  40.153  1.00 34.61           N  
-ATOM   2525  CA  ALA A 355      -4.717   4.454  41.545  1.00 35.40           C  
-ATOM   2526  C   ALA A 355      -5.237   3.016  41.653  1.00 36.53           C  
-ATOM   2527  O   ALA A 355      -4.658   2.193  42.361  1.00 38.03           O  
-ATOM   2528  CB  ALA A 355      -5.592   5.392  42.356  1.00 33.84           C  
-ATOM   2529  N   LYS A 356      -6.324   2.715  40.948  1.00 37.58           N  
-ATOM   2530  CA  LYS A 356      -6.894   1.372  40.979  1.00 37.72           C  
-ATOM   2531  C   LYS A 356      -5.862   0.362  40.514  1.00 38.77           C  
-ATOM   2532  O   LYS A 356      -5.694  -0.688  41.126  1.00 40.11           O  
-ATOM   2533  CB  LYS A 356      -8.137   1.286  40.087  1.00 36.58           C  
-ATOM   2534  CG  LYS A 356      -9.337   2.061  40.614  1.00 35.61           C  
-ATOM   2535  CD  LYS A 356     -10.524   1.986  39.663  1.00 36.42           C  
-ATOM   2536  CE  LYS A 356     -11.070   0.568  39.544  1.00 38.91           C  
-ATOM   2537  NZ  LYS A 356     -12.235   0.509  38.611  1.00 38.60           N  
-ATOM   2538  N   ARG A 357      -5.170   0.683  39.426  1.00 41.34           N  
-ATOM   2539  CA  ARG A 357      -4.148  -0.206  38.889  1.00 43.08           C  
-ATOM   2540  C   ARG A 357      -2.994  -0.402  39.875  1.00 43.21           C  
-ATOM   2541  O   ARG A 357      -2.359  -1.457  39.891  1.00 42.44           O  
-ATOM   2542  CB  ARG A 357      -3.632   0.339  37.551  1.00 44.15           C  
-ATOM   2543  CG  ARG A 357      -4.550   0.021  36.365  1.00 46.98           C  
-ATOM   2544  CD  ARG A 357      -4.412   1.049  35.253  1.00 48.24           C  
-ATOM   2545  NE  ARG A 357      -3.014   1.302  34.936  1.00 52.31           N  
-ATOM   2546  CZ  ARG A 357      -2.563   2.425  34.385  1.00 54.64           C  
-ATOM   2547  NH1 ARG A 357      -3.407   3.408  34.085  1.00 54.09           N  
-ATOM   2548  NH2 ARG A 357      -1.263   2.574  34.151  1.00 55.52           N  
-ATOM   2549  N   GLU A 358      -2.728   0.608  40.701  1.00 44.60           N  
-ATOM   2550  CA  GLU A 358      -1.660   0.512  41.694  1.00 45.44           C  
-ATOM   2551  C   GLU A 358      -2.082  -0.449  42.800  1.00 45.02           C  
-ATOM   2552  O   GLU A 358      -1.321  -1.325  43.202  1.00 44.29           O  
-ATOM   2553  CB  GLU A 358      -1.352   1.886  42.301  1.00 46.75           C  
-ATOM   2554  CG  GLU A 358      -0.560   2.812  41.394  1.00 49.33           C  
-ATOM   2555  CD  GLU A 358      -0.200   4.127  42.067  1.00 51.26           C  
-ATOM   2556  OE1 GLU A 358       0.610   4.881  41.490  1.00 53.10           O  
-ATOM   2557  OE2 GLU A 358      -0.724   4.410  43.168  1.00 52.14           O  
-ATOM   2558  N   LYS A 359      -3.301  -0.261  43.291  1.00 45.52           N  
-ATOM   2559  CA  LYS A 359      -3.867  -1.099  44.341  1.00 46.26           C  
-ATOM   2560  C   LYS A 359      -3.715  -2.567  43.948  1.00 46.62           C  
-ATOM   2561  O   LYS A 359      -3.324  -3.409  44.759  1.00 45.44           O  
-ATOM   2562  CB  LYS A 359      -5.347  -0.742  44.526  1.00 46.77           C  
-ATOM   2563  CG  LYS A 359      -6.147  -1.661  45.441  1.00 48.87           C  
-ATOM   2564  CD  LYS A 359      -5.622  -1.670  46.864  1.00 50.25           C  
-ATOM   2565  CE  LYS A 359      -6.668  -2.233  47.818  1.00 51.84           C  
-ATOM   2566  NZ  LYS A 359      -7.226  -3.538  47.357  1.00 52.12           N  
-ATOM   2567  N   VAL A 360      -4.014  -2.865  42.689  1.00 47.44           N  
-ATOM   2568  CA  VAL A 360      -3.905  -4.226  42.188  1.00 47.10           C  
-ATOM   2569  C   VAL A 360      -2.458  -4.705  42.237  1.00 47.52           C  
-ATOM   2570  O   VAL A 360      -2.183  -5.832  42.645  1.00 47.99           O  
-ATOM   2571  CB  VAL A 360      -4.418  -4.322  40.741  1.00 47.19           C  
-ATOM   2572  CG1 VAL A 360      -4.256  -5.744  40.224  1.00 47.49           C  
-ATOM   2573  CG2 VAL A 360      -5.876  -3.897  40.685  1.00 46.71           C  
-ATOM   2574  N   LEU A 361      -1.531  -3.845  41.830  1.00 48.26           N  
-ATOM   2575  CA  LEU A 361      -0.121  -4.210  41.833  1.00 49.13           C  
-ATOM   2576  C   LEU A 361       0.437  -4.303  43.252  1.00 50.34           C  
-ATOM   2577  O   LEU A 361       1.449  -4.964  43.490  1.00 50.45           O  
-ATOM   2578  CB  LEU A 361       0.684  -3.205  41.009  1.00 49.55           C  
-ATOM   2579  CG  LEU A 361       0.245  -3.070  39.546  1.00 50.55           C  
-ATOM   2580  CD1 LEU A 361       1.231  -2.187  38.807  1.00 51.13           C  
-ATOM   2581  CD2 LEU A 361       0.174  -4.439  38.884  1.00 50.96           C  
-ATOM   2582  N   VAL A 362      -0.228  -3.644  44.194  1.00 50.02           N  
-ATOM   2583  CA  VAL A 362       0.209  -3.677  45.580  1.00 51.20           C  
-ATOM   2584  C   VAL A 362      -0.200  -5.001  46.195  1.00 51.78           C  
-ATOM   2585  O   VAL A 362       0.612  -5.695  46.803  1.00 52.37           O  
-ATOM   2586  CB  VAL A 362      -0.425  -2.535  46.397  1.00 52.02           C  
-ATOM   2587  CG1 VAL A 362      -0.215  -2.778  47.887  1.00 51.13           C  
-ATOM   2588  CG2 VAL A 362       0.192  -1.207  45.986  1.00 51.11           C  
-ATOM   2589  N   ASP A 363      -1.470  -5.344  46.025  1.00 53.03           N  
-ATOM   2590  CA  ASP A 363      -2.010  -6.586  46.559  1.00 53.82           C  
-ATOM   2591  C   ASP A 363      -1.486  -7.797  45.789  1.00 54.04           C  
-ATOM   2592  O   ASP A 363      -1.970  -8.912  45.975  1.00 54.96           O  
-ATOM   2593  CB  ASP A 363      -3.540  -6.556  46.494  1.00 55.16           C  
-ATOM   2594  CG  ASP A 363      -4.134  -5.371  47.236  1.00 56.73           C  
-ATOM   2595  OD1 ASP A 363      -5.368  -5.180  47.164  1.00 56.51           O  
-ATOM   2596  OD2 ASP A 363      -3.368  -4.630  47.891  1.00 57.53           O  
-ATOM   2597  N   ALA A 364      -0.502  -7.576  44.922  1.00 52.72           N  
-ATOM   2598  CA  ALA A 364       0.073  -8.663  44.137  1.00 51.65           C  
-ATOM   2599  C   ALA A 364       1.561  -8.807  44.418  1.00 50.93           C  
-ATOM   2600  O   ALA A 364       2.184  -9.787  44.019  1.00 50.22           O  
-ATOM   2601  CB  ALA A 364      -0.155  -8.419  42.653  1.00 50.39           C  
-ATOM   2602  N   GLY A 365       2.129  -7.821  45.102  1.00 51.62           N  
-ATOM   2603  CA  GLY A 365       3.543  -7.869  45.426  1.00 53.49           C  
-ATOM   2604  C   GLY A 365       4.448  -7.218  44.397  1.00 54.55           C  
-ATOM   2605  O   GLY A 365       5.672  -7.229  44.547  1.00 54.68           O  
-ATOM   2606  N   TYR A 366       3.857  -6.647  43.352  1.00 55.29           N  
-ATOM   2607  CA  TYR A 366       4.635  -5.995  42.305  1.00 56.72           C  
-ATOM   2608  C   TYR A 366       5.265  -4.682  42.760  1.00 58.61           C  
-ATOM   2609  O   TYR A 366       6.286  -4.259  42.215  1.00 59.27           O  
-ATOM   2610  CB  TYR A 366       3.762  -5.761  41.070  1.00 55.43           C  
-ATOM   2611  CG  TYR A 366       3.671  -6.972  40.170  1.00 54.58           C  
-ATOM   2612  CD1 TYR A 366       3.375  -8.233  40.691  1.00 54.31           C  
-ATOM   2613  CD2 TYR A 366       3.894  -6.862  38.797  1.00 53.61           C  
-ATOM   2614  CE1 TYR A 366       3.309  -9.356  39.868  1.00 53.85           C  
-ATOM   2615  CE2 TYR A 366       3.828  -7.978  37.964  1.00 53.17           C  
-ATOM   2616  CZ  TYR A 366       3.537  -9.222  38.507  1.00 53.83           C  
-ATOM   2617  OH  TYR A 366       3.487 -10.331  37.693  1.00 52.82           O  
-ATOM   2618  N   MET A 367       4.659  -4.044  43.759  1.00 59.77           N  
-ATOM   2619  CA  MET A 367       5.170  -2.782  44.288  1.00 60.60           C  
-ATOM   2620  C   MET A 367       4.795  -2.587  45.757  1.00 61.61           C  
-ATOM   2621  O   MET A 367       4.103  -3.467  46.313  1.00 61.66           O  
-ATOM   2622  CB  MET A 367       4.645  -1.599  43.460  1.00 60.73           C  
-ATOM   2623  CG  MET A 367       3.129  -1.567  43.283  1.00 60.29           C  
-ATOM   2624  SD  MET A 367       2.523  -0.009  42.577  1.00 60.23           S  
-ATOM   2625  CE  MET A 367       3.032  -0.156  40.860  1.00 58.92           C  
-TER    2626      MET A 367                                                      
-ATOM   2627  N   ARG B  28      31.129  50.127  65.226  1.00 52.60           N  
-ATOM   2628  CA  ARG B  28      31.127  51.080  64.076  1.00 52.83           C  
-ATOM   2629  C   ARG B  28      30.490  50.441  62.835  1.00 51.62           C  
-ATOM   2630  O   ARG B  28      30.661  49.246  62.585  1.00 52.40           O  
-ATOM   2631  CB  ARG B  28      32.564  51.522  63.777  1.00 52.82           C  
-ATOM   2632  CG  ARG B  28      32.697  52.477  62.611  1.00 54.44           C  
-ATOM   2633  CD  ARG B  28      33.953  53.323  62.738  1.00 56.44           C  
-ATOM   2634  NE  ARG B  28      35.179  52.535  62.813  1.00 57.32           N  
-ATOM   2635  CZ  ARG B  28      36.394  53.069  62.911  1.00 58.70           C  
-ATOM   2636  NH1 ARG B  28      36.539  54.390  62.945  1.00 58.29           N  
-ATOM   2637  NH2 ARG B  28      37.464  52.288  62.976  1.00 58.89           N  
-ATOM   2638  N   LYS B  29      29.754  51.238  62.064  1.00 49.20           N  
-ATOM   2639  CA  LYS B  29      29.087  50.730  60.868  1.00 47.27           C  
-ATOM   2640  C   LYS B  29      30.037  50.171  59.812  1.00 44.89           C  
-ATOM   2641  O   LYS B  29      30.990  50.830  59.393  1.00 43.15           O  
-ATOM   2642  CB  LYS B  29      28.205  51.815  60.240  1.00 48.66           C  
-ATOM   2643  CG  LYS B  29      26.805  51.905  60.837  1.00 49.81           C  
-ATOM   2644  CD  LYS B  29      25.929  52.863  60.039  1.00 52.22           C  
-ATOM   2645  CE  LYS B  29      24.499  52.883  60.563  1.00 55.01           C  
-ATOM   2646  NZ  LYS B  29      23.613  53.779  59.762  1.00 55.84           N  
-ATOM   2647  N   ILE B  30      29.749  48.945  59.385  1.00 42.19           N  
-ATOM   2648  CA  ILE B  30      30.542  48.250  58.380  1.00 40.27           C  
-ATOM   2649  C   ILE B  30      29.780  48.161  57.058  1.00 39.32           C  
-ATOM   2650  O   ILE B  30      28.660  47.647  57.002  1.00 38.72           O  
-ATOM   2651  CB  ILE B  30      30.889  46.825  58.859  1.00 39.58           C  
-ATOM   2652  CG1 ILE B  30      31.726  46.909  60.140  1.00 38.26           C  
-ATOM   2653  CG2 ILE B  30      31.621  46.066  57.761  1.00 38.76           C  
-ATOM   2654  CD1 ILE B  30      32.166  45.570  60.692  1.00 37.72           C  
-ATOM   2655  N   ALA B  31      30.390  48.668  55.993  1.00 37.80           N  
-ATOM   2656  CA  ALA B  31      29.765  48.639  54.678  1.00 35.85           C  
-ATOM   2657  C   ALA B  31      30.530  47.756  53.690  1.00 35.39           C  
-ATOM   2658  O   ALA B  31      31.762  47.804  53.616  1.00 34.43           O  
-ATOM   2659  CB  ALA B  31      29.651  50.048  54.128  1.00 34.36           C  
-ATOM   2660  N   LEU B  32      29.789  46.939  52.948  1.00 33.31           N  
-ATOM   2661  CA  LEU B  32      30.380  46.070  51.936  1.00 32.82           C  
-ATOM   2662  C   LEU B  32      29.966  46.606  50.573  1.00 30.51           C  
-ATOM   2663  O   LEU B  32      28.778  46.765  50.294  1.00 31.27           O  
-ATOM   2664  CB  LEU B  32      29.883  44.630  52.090  1.00 31.91           C  
-ATOM   2665  CG  LEU B  32      30.321  43.673  50.976  1.00 31.18           C  
-ATOM   2666  CD1 LEU B  32      31.834  43.713  50.819  1.00 31.60           C  
-ATOM   2667  CD2 LEU B  32      29.855  42.266  51.301  1.00 32.46           C  
-ATOM   2668  N   ILE B  33      30.943  46.893  49.725  1.00 29.03           N  
-ATOM   2669  CA  ILE B  33      30.651  47.423  48.401  1.00 27.59           C  
-ATOM   2670  C   ILE B  33      31.156  46.497  47.298  1.00 27.68           C  
-ATOM   2671  O   ILE B  33      32.321  46.105  47.299  1.00 27.15           O  
-ATOM   2672  CB  ILE B  33      31.323  48.799  48.189  1.00 27.09           C  
-ATOM   2673  CG1 ILE B  33      30.988  49.745  49.346  1.00 25.44           C  
-ATOM   2674  CG2 ILE B  33      30.866  49.402  46.873  1.00 25.11           C  
-ATOM   2675  CD1 ILE B  33      31.684  51.093  49.238  1.00 23.13           C  
-ATOM   2676  N   THR B  34      30.273  46.128  46.374  1.00 28.58           N  
-ATOM   2677  CA  THR B  34      30.678  45.310  45.234  1.00 27.21           C  
-ATOM   2678  C   THR B  34      30.850  46.355  44.135  1.00 26.95           C  
-ATOM   2679  O   THR B  34      30.081  47.311  44.070  1.00 26.99           O  
-ATOM   2680  CB  THR B  34      29.587  44.286  44.799  1.00 25.60           C  
-ATOM   2681  OG1 THR B  34      28.435  44.981  44.309  1.00 26.08           O  
-ATOM   2682  CG2 THR B  34      29.182  43.403  45.963  1.00 18.82           C  
-ATOM   2683  N   GLY B  35      31.857  46.189  43.287  1.00 27.93           N  
-ATOM   2684  CA  GLY B  35      32.084  47.156  42.227  1.00 27.01           C  
-ATOM   2685  C   GLY B  35      32.681  48.430  42.795  1.00 27.55           C  
-ATOM   2686  O   GLY B  35      32.435  49.535  42.300  1.00 27.01           O  
-ATOM   2687  N   ILE B  36      33.481  48.267  43.841  1.00 27.76           N  
-ATOM   2688  CA  ILE B  36      34.109  49.393  44.510  1.00 27.23           C  
-ATOM   2689  C   ILE B  36      35.094  50.126  43.610  1.00 28.02           C  
-ATOM   2690  O   ILE B  36      35.291  51.333  43.759  1.00 28.56           O  
-ATOM   2691  CB  ILE B  36      34.834  48.929  45.804  1.00 25.33           C  
-ATOM   2692  CG1 ILE B  36      35.153  50.137  46.686  1.00 24.38           C  
-ATOM   2693  CG2 ILE B  36      36.112  48.175  45.449  1.00 23.32           C  
-ATOM   2694  CD1 ILE B  36      35.527  49.768  48.112  1.00 23.01           C  
-ATOM   2695  N   THR B  37      35.699  49.406  42.667  1.00 29.35           N  
-ATOM   2696  CA  THR B  37      36.675  50.010  41.760  1.00 27.42           C  
-ATOM   2697  C   THR B  37      36.047  50.900  40.702  1.00 26.84           C  
-ATOM   2698  O   THR B  37      36.755  51.619  39.996  1.00 27.52           O  
-ATOM   2699  CB  THR B  37      37.525  48.940  41.032  1.00 28.31           C  
-ATOM   2700  OG1 THR B  37      36.662  48.011  40.366  1.00 30.06           O  
-ATOM   2701  CG2 THR B  37      38.427  48.205  42.016  1.00 26.10           C  
-ATOM   2702  N   GLY B  38      34.723  50.853  40.592  1.00 26.76           N  
-ATOM   2703  CA  GLY B  38      34.032  51.660  39.604  1.00 25.95           C  
-ATOM   2704  C   GLY B  38      33.815  53.104  40.024  1.00 27.27           C  
-ATOM   2705  O   GLY B  38      34.132  53.485  41.153  1.00 27.90           O  
-ATOM   2706  N   GLN B  39      33.265  53.904  39.110  1.00 26.52           N  
-ATOM   2707  CA  GLN B  39      32.997  55.318  39.373  1.00 29.35           C  
-ATOM   2708  C   GLN B  39      32.245  55.547  40.680  1.00 30.94           C  
-ATOM   2709  O   GLN B  39      32.741  56.223  41.582  1.00 33.26           O  
-ATOM   2710  CB  GLN B  39      32.180  55.941  38.235  1.00 28.16           C  
-ATOM   2711  CG  GLN B  39      31.688  57.355  38.565  1.00 26.71           C  
-ATOM   2712  CD  GLN B  39      30.720  57.910  37.541  1.00 27.16           C  
-ATOM   2713  OE1 GLN B  39      31.036  58.855  36.832  1.00 27.57           O  
-ATOM   2714  NE2 GLN B  39      29.530  57.319  37.460  1.00 28.27           N  
-ATOM   2715  N   ASP B  40      31.041  54.990  40.767  1.00 30.24           N  
-ATOM   2716  CA  ASP B  40      30.205  55.144  41.946  1.00 28.62           C  
-ATOM   2717  C   ASP B  40      30.848  54.568  43.189  1.00 29.56           C  
-ATOM   2718  O   ASP B  40      30.752  55.151  44.266  1.00 30.64           O  
-ATOM   2719  CB  ASP B  40      28.847  54.479  41.718  1.00 29.55           C  
-ATOM   2720  CG  ASP B  40      28.030  55.175  40.646  1.00 28.76           C  
-ATOM   2721  OD1 ASP B  40      28.553  56.110  40.001  1.00 28.58           O  
-ATOM   2722  OD2 ASP B  40      26.864  54.786  40.451  1.00 30.12           O  
-ATOM   2723  N   GLY B  41      31.500  53.419  43.040  1.00 29.04           N  
-ATOM   2724  CA  GLY B  41      32.144  52.788  44.175  1.00 28.85           C  
-ATOM   2725  C   GLY B  41      33.225  53.656  44.800  1.00 29.79           C  
-ATOM   2726  O   GLY B  41      33.403  53.655  46.020  1.00 28.23           O  
-ATOM   2727  N   SER B  42      33.953  54.393  43.967  1.00 27.48           N  
-ATOM   2728  CA  SER B  42      35.011  55.255  44.468  1.00 29.30           C  
-ATOM   2729  C   SER B  42      34.416  56.419  45.254  1.00 30.42           C  
-ATOM   2730  O   SER B  42      34.926  56.773  46.316  1.00 32.95           O  
-ATOM   2731  CB  SER B  42      35.870  55.782  43.316  1.00 27.16           C  
-ATOM   2732  OG  SER B  42      35.114  56.594  42.446  1.00 24.78           O  
-ATOM   2733  N   TYR B  43      33.335  57.005  44.741  1.00 30.43           N  
-ATOM   2734  CA  TYR B  43      32.682  58.119  45.428  1.00 30.47           C  
-ATOM   2735  C   TYR B  43      31.955  57.674  46.692  1.00 31.27           C  
-ATOM   2736  O   TYR B  43      32.066  58.325  47.725  1.00 32.01           O  
-ATOM   2737  CB  TYR B  43      31.695  58.839  44.501  1.00 28.84           C  
-ATOM   2738  CG  TYR B  43      32.353  59.774  43.518  1.00 27.67           C  
-ATOM   2739  CD1 TYR B  43      32.408  59.468  42.160  1.00 29.87           C  
-ATOM   2740  CD2 TYR B  43      32.949  60.960  43.949  1.00 29.66           C  
-ATOM   2741  CE1 TYR B  43      33.043  60.320  41.251  1.00 27.87           C  
-ATOM   2742  CE2 TYR B  43      33.586  61.818  43.053  1.00 29.22           C  
-ATOM   2743  CZ  TYR B  43      33.629  61.490  41.707  1.00 29.44           C  
-ATOM   2744  OH  TYR B  43      34.257  62.334  40.822  1.00 29.79           O  
-ATOM   2745  N   LEU B  44      31.215  56.570  46.615  1.00 31.21           N  
-ATOM   2746  CA  LEU B  44      30.491  56.064  47.778  1.00 31.20           C  
-ATOM   2747  C   LEU B  44      31.478  55.747  48.892  1.00 32.84           C  
-ATOM   2748  O   LEU B  44      31.189  55.967  50.070  1.00 33.08           O  
-ATOM   2749  CB  LEU B  44      29.699  54.798  47.420  1.00 31.32           C  
-ATOM   2750  CG  LEU B  44      28.933  54.094  48.553  1.00 34.33           C  
-ATOM   2751  CD1 LEU B  44      27.882  55.035  49.140  1.00 33.48           C  
-ATOM   2752  CD2 LEU B  44      28.266  52.825  48.029  1.00 32.04           C  
-ATOM   2753  N   THR B  45      32.645  55.227  48.517  1.00 32.71           N  
-ATOM   2754  CA  THR B  45      33.672  54.882  49.496  1.00 32.70           C  
-ATOM   2755  C   THR B  45      34.099  56.132  50.264  1.00 33.39           C  
-ATOM   2756  O   THR B  45      34.139  56.129  51.492  1.00 32.17           O  
-ATOM   2757  CB  THR B  45      34.907  54.250  48.814  1.00 30.69           C  
-ATOM   2758  OG1 THR B  45      34.537  52.995  48.234  1.00 30.07           O  
-ATOM   2759  CG2 THR B  45      36.027  54.019  49.824  1.00 29.11           C  
-ATOM   2760  N   GLU B  46      34.407  57.201  49.536  1.00 34.75           N  
-ATOM   2761  CA  GLU B  46      34.817  58.449  50.172  1.00 36.81           C  
-ATOM   2762  C   GLU B  46      33.686  58.977  51.055  1.00 38.25           C  
-ATOM   2763  O   GLU B  46      33.925  59.452  52.166  1.00 39.50           O  
-ATOM   2764  CB  GLU B  46      35.190  59.492  49.108  1.00 35.80           C  
-ATOM   2765  CG  GLU B  46      36.400  59.098  48.264  1.00 37.74           C  
-ATOM   2766  CD  GLU B  46      36.612  60.005  47.067  1.00 38.63           C  
-ATOM   2767  OE1 GLU B  46      35.626  60.292  46.361  1.00 41.18           O  
-ATOM   2768  OE2 GLU B  46      37.762  60.422  46.816  1.00 39.90           O  
-ATOM   2769  N   PHE B  47      32.454  58.867  50.566  1.00 37.62           N  
-ATOM   2770  CA  PHE B  47      31.290  59.346  51.301  1.00 36.57           C  
-ATOM   2771  C   PHE B  47      31.049  58.588  52.600  1.00 37.37           C  
-ATOM   2772  O   PHE B  47      30.737  59.192  53.625  1.00 37.12           O  
-ATOM   2773  CB  PHE B  47      30.032  59.250  50.436  1.00 35.18           C  
-ATOM   2774  CG  PHE B  47      28.812  59.850  51.079  1.00 34.72           C  
-ATOM   2775  CD1 PHE B  47      28.632  61.232  51.107  1.00 33.66           C  
-ATOM   2776  CD2 PHE B  47      27.853  59.038  51.678  1.00 33.83           C  
-ATOM   2777  CE1 PHE B  47      27.514  61.795  51.721  1.00 33.97           C  
-ATOM   2778  CE2 PHE B  47      26.731  59.590  52.295  1.00 31.98           C  
-ATOM   2779  CZ  PHE B  47      26.562  60.971  52.316  1.00 33.55           C  
-ATOM   2780  N   LEU B  48      31.177  57.264  52.553  1.00 38.13           N  
-ATOM   2781  CA  LEU B  48      30.959  56.446  53.739  1.00 37.86           C  
-ATOM   2782  C   LEU B  48      32.082  56.622  54.751  1.00 38.06           C  
-ATOM   2783  O   LEU B  48      31.833  56.700  55.952  1.00 37.84           O  
-ATOM   2784  CB  LEU B  48      30.818  54.968  53.356  1.00 36.99           C  
-ATOM   2785  CG  LEU B  48      29.566  54.607  52.544  1.00 38.27           C  
-ATOM   2786  CD1 LEU B  48      29.485  53.104  52.364  1.00 37.25           C  
-ATOM   2787  CD2 LEU B  48      28.323  55.108  53.260  1.00 38.27           C  
-ATOM   2788  N   LEU B  49      33.318  56.674  54.267  1.00 39.01           N  
-ATOM   2789  CA  LEU B  49      34.454  56.863  55.155  1.00 40.06           C  
-ATOM   2790  C   LEU B  49      34.244  58.193  55.873  1.00 42.14           C  
-ATOM   2791  O   LEU B  49      34.559  58.328  57.054  1.00 42.35           O  
-ATOM   2792  CB  LEU B  49      35.765  56.877  54.360  1.00 38.10           C  
-ATOM   2793  CG  LEU B  49      36.265  55.517  53.853  1.00 34.97           C  
-ATOM   2794  CD1 LEU B  49      37.494  55.704  52.991  1.00 35.23           C  
-ATOM   2795  CD2 LEU B  49      36.586  54.616  55.030  1.00 32.20           C  
-ATOM   2796  N   GLY B  50      33.687  59.163  55.151  1.00 42.26           N  
-ATOM   2797  CA  GLY B  50      33.416  60.465  55.733  1.00 42.53           C  
-ATOM   2798  C   GLY B  50      32.374  60.387  56.838  1.00 42.98           C  
-ATOM   2799  O   GLY B  50      32.293  61.271  57.692  1.00 42.68           O  
-ATOM   2800  N   LYS B  51      31.569  59.328  56.819  1.00 42.54           N  
-ATOM   2801  CA  LYS B  51      30.537  59.130  57.831  1.00 41.26           C  
-ATOM   2802  C   LYS B  51      31.078  58.254  58.956  1.00 40.72           C  
-ATOM   2803  O   LYS B  51      30.338  57.860  59.853  1.00 41.32           O  
-ATOM   2804  CB  LYS B  51      29.301  58.456  57.221  1.00 42.20           C  
-ATOM   2805  CG  LYS B  51      28.551  59.292  56.186  1.00 43.16           C  
-ATOM   2806  CD  LYS B  51      27.838  60.472  56.826  1.00 45.12           C  
-ATOM   2807  CE  LYS B  51      27.033  61.252  55.798  1.00 45.77           C  
-ATOM   2808  NZ  LYS B  51      26.341  62.439  56.391  1.00 47.00           N  
-ATOM   2809  N   GLY B  52      32.365  57.931  58.894  1.00 39.75           N  
-ATOM   2810  CA  GLY B  52      32.962  57.107  59.930  1.00 39.38           C  
-ATOM   2811  C   GLY B  52      32.843  55.611  59.712  1.00 39.79           C  
-ATOM   2812  O   GLY B  52      33.257  54.827  60.563  1.00 41.11           O  
-ATOM   2813  N   TYR B  53      32.284  55.208  58.575  1.00 39.52           N  
-ATOM   2814  CA  TYR B  53      32.124  53.791  58.251  1.00 37.47           C  
-ATOM   2815  C   TYR B  53      33.438  53.044  58.073  1.00 37.48           C  
-ATOM   2816  O   TYR B  53      34.486  53.634  57.806  1.00 38.89           O  
-ATOM   2817  CB  TYR B  53      31.360  53.615  56.935  1.00 38.14           C  
-ATOM   2818  CG  TYR B  53      29.856  53.701  57.001  1.00 37.46           C  
-ATOM   2819  CD1 TYR B  53      29.216  54.894  57.325  1.00 37.59           C  
-ATOM   2820  CD2 TYR B  53      29.069  52.595  56.687  1.00 36.94           C  
-ATOM   2821  CE1 TYR B  53      27.827  54.984  57.330  1.00 38.49           C  
-ATOM   2822  CE2 TYR B  53      27.683  52.674  56.689  1.00 37.75           C  
-ATOM   2823  CZ  TYR B  53      27.069  53.871  57.010  1.00 37.72           C  
-ATOM   2824  OH  TYR B  53      25.698  53.957  57.008  1.00 40.03           O  
-ATOM   2825  N   GLU B  54      33.364  51.729  58.226  1.00 37.11           N  
-ATOM   2826  CA  GLU B  54      34.500  50.860  57.973  1.00 36.62           C  
-ATOM   2827  C   GLU B  54      34.041  50.285  56.629  1.00 36.36           C  
-ATOM   2828  O   GLU B  54      33.007  49.622  56.564  1.00 35.41           O  
-ATOM   2829  CB  GLU B  54      34.597  49.751  59.020  1.00 38.45           C  
-ATOM   2830  CG  GLU B  54      35.528  48.609  58.613  1.00 40.16           C  
-ATOM   2831  CD  GLU B  54      35.676  47.553  59.691  1.00 42.47           C  
-ATOM   2832  OE1 GLU B  54      36.136  46.436  59.368  1.00 42.58           O  
-ATOM   2833  OE2 GLU B  54      35.343  47.841  60.863  1.00 44.01           O  
-ATOM   2834  N   VAL B  55      34.786  50.562  55.564  1.00 35.65           N  
-ATOM   2835  CA  VAL B  55      34.410  50.108  54.227  1.00 35.41           C  
-ATOM   2836  C   VAL B  55      35.172  48.909  53.676  1.00 34.73           C  
-ATOM   2837  O   VAL B  55      36.400  48.883  53.665  1.00 33.95           O  
-ATOM   2838  CB  VAL B  55      34.545  51.267  53.202  1.00 36.72           C  
-ATOM   2839  CG1 VAL B  55      34.123  50.800  51.820  1.00 35.18           C  
-ATOM   2840  CG2 VAL B  55      33.703  52.453  53.644  1.00 35.02           C  
-ATOM   2841  N   HIS B  56      34.420  47.921  53.206  1.00 35.25           N  
-ATOM   2842  CA  HIS B  56      34.988  46.716  52.610  1.00 36.05           C  
-ATOM   2843  C   HIS B  56      34.522  46.637  51.162  1.00 35.75           C  
-ATOM   2844  O   HIS B  56      33.335  46.809  50.879  1.00 37.09           O  
-ATOM   2845  CB  HIS B  56      34.513  45.479  53.364  1.00 36.52           C  
-ATOM   2846  CG  HIS B  56      35.223  45.258  54.660  1.00 40.02           C  
-ATOM   2847  ND1 HIS B  56      36.441  44.618  54.738  1.00 38.91           N  
-ATOM   2848  CD2 HIS B  56      34.902  45.616  55.926  1.00 39.24           C  
-ATOM   2849  CE1 HIS B  56      36.838  44.587  55.998  1.00 41.72           C  
-ATOM   2850  NE2 HIS B  56      35.922  45.186  56.739  1.00 40.42           N  
-ATOM   2851  N   GLY B  57      35.455  46.386  50.250  1.00 34.39           N  
-ATOM   2852  CA  GLY B  57      35.103  46.293  48.844  1.00 32.74           C  
-ATOM   2853  C   GLY B  57      35.568  45.008  48.179  1.00 31.48           C  
-ATOM   2854  O   GLY B  57      36.630  44.477  48.510  1.00 30.92           O  
-ATOM   2855  N   LEU B  58      34.765  44.500  47.245  1.00 30.45           N  
-ATOM   2856  CA  LEU B  58      35.112  43.281  46.516  1.00 28.31           C  
-ATOM   2857  C   LEU B  58      35.673  43.676  45.153  1.00 28.07           C  
-ATOM   2858  O   LEU B  58      35.097  44.511  44.454  1.00 27.92           O  
-ATOM   2859  CB  LEU B  58      33.876  42.398  46.318  1.00 25.44           C  
-ATOM   2860  CG  LEU B  58      33.071  42.014  47.557  1.00 25.27           C  
-ATOM   2861  CD1 LEU B  58      31.995  41.018  47.160  1.00 24.06           C  
-ATOM   2862  CD2 LEU B  58      33.981  41.413  48.618  1.00 25.80           C  
-ATOM   2863  N   ILE B  59      36.800  43.082  44.778  1.00 28.00           N  
-ATOM   2864  CA  ILE B  59      37.415  43.386  43.492  1.00 27.93           C  
-ATOM   2865  C   ILE B  59      37.741  42.130  42.696  1.00 27.51           C  
-ATOM   2866  O   ILE B  59      37.839  41.027  43.242  1.00 26.79           O  
-ATOM   2867  CB  ILE B  59      38.727  44.183  43.650  1.00 27.63           C  
-ATOM   2868  CG1 ILE B  59      39.730  43.372  44.474  1.00 29.99           C  
-ATOM   2869  CG2 ILE B  59      38.448  45.526  44.290  1.00 29.02           C  
-ATOM   2870  CD1 ILE B  59      41.107  44.000  44.556  1.00 28.61           C  
-ATOM   2871  N   ARG B  60      37.914  42.319  41.395  1.00 27.22           N  
-ATOM   2872  CA  ARG B  60      38.254  41.232  40.497  1.00 27.01           C  
-ATOM   2873  C   ARG B  60      39.750  41.217  40.292  1.00 27.86           C  
-ATOM   2874  O   ARG B  60      40.397  42.270  40.266  1.00 28.99           O  
-ATOM   2875  CB  ARG B  60      37.606  41.422  39.125  1.00 27.10           C  
-ATOM   2876  CG  ARG B  60      36.097  41.419  39.109  1.00 25.74           C  
-ATOM   2877  CD  ARG B  60      35.600  41.232  37.685  1.00 24.99           C  
-ATOM   2878  NE  ARG B  60      35.931  42.362  36.819  1.00 24.38           N  
-ATOM   2879  CZ  ARG B  60      35.758  42.359  35.501  1.00 23.53           C  
-ATOM   2880  NH1 ARG B  60      35.266  41.283  34.902  1.00 21.54           N  
-ATOM   2881  NH2 ARG B  60      36.064  43.434  34.783  1.00 22.04           N  
-ATOM   2882  N   ARG B  61      40.304  40.021  40.152  1.00 27.84           N  
-ATOM   2883  CA  ARG B  61      41.718  39.901  39.884  1.00 29.03           C  
-ATOM   2884  C   ARG B  61      41.848  40.323  38.423  1.00 30.21           C  
-ATOM   2885  O   ARG B  61      41.018  39.952  37.588  1.00 26.76           O  
-ATOM   2886  CB  ARG B  61      42.176  38.452  40.064  1.00 31.47           C  
-ATOM   2887  CG  ARG B  61      43.668  38.245  39.852  1.00 32.72           C  
-ATOM   2888  CD  ARG B  61      44.015  38.063  38.376  1.00 35.61           C  
-ATOM   2889  NE  ARG B  61      45.454  38.175  38.163  1.00 36.78           N  
-ATOM   2890  CZ  ARG B  61      46.079  37.849  37.038  1.00 38.05           C  
-ATOM   2891  NH1 ARG B  61      45.396  37.377  36.000  1.00 37.05           N  
-ATOM   2892  NH2 ARG B  61      47.395  38.004  36.953  1.00 36.46           N  
-ATOM   2893  N   SER B  62      42.868  41.118  38.121  1.00 30.70           N  
-ATOM   2894  CA  SER B  62      43.095  41.572  36.753  1.00 32.37           C  
-ATOM   2895  C   SER B  62      44.582  41.482  36.455  1.00 31.70           C  
-ATOM   2896  O   SER B  62      45.399  41.620  37.364  1.00 29.33           O  
-ATOM   2897  CB  SER B  62      42.623  43.015  36.584  1.00 34.23           C  
-ATOM   2898  OG  SER B  62      42.836  43.451  35.252  1.00 38.25           O  
-ATOM   2899  N   SER B  63      44.934  41.248  35.191  1.00 31.69           N  
-ATOM   2900  CA  SER B  63      46.339  41.135  34.817  1.00 31.62           C  
-ATOM   2901  C   SER B  63      46.991  42.513  34.875  1.00 33.38           C  
-ATOM   2902  O   SER B  63      48.215  42.631  34.845  1.00 33.16           O  
-ATOM   2903  CB  SER B  63      46.485  40.542  33.406  1.00 30.99           C  
-ATOM   2904  OG  SER B  63      46.080  41.454  32.401  1.00 29.47           O  
-ATOM   2905  N   ASN B  64      46.157  43.547  34.963  1.00 34.15           N  
-ATOM   2906  CA  ASN B  64      46.620  44.927  35.032  1.00 36.75           C  
-ATOM   2907  C   ASN B  64      46.066  45.659  36.246  1.00 38.74           C  
-ATOM   2908  O   ASN B  64      45.142  45.191  36.913  1.00 39.75           O  
-ATOM   2909  CB  ASN B  64      46.206  45.702  33.772  1.00 37.51           C  
-ATOM   2910  CG  ASN B  64      47.208  45.568  32.639  1.00 36.96           C  
-ATOM   2911  OD1 ASN B  64      48.353  46.016  32.748  1.00 39.31           O  
-ATOM   2912  ND2 ASN B  64      46.783  44.956  31.544  1.00 34.37           N  
-ATOM   2913  N   PHE B  65      46.653  46.821  36.510  1.00 40.18           N  
-ATOM   2914  CA  PHE B  65      46.260  47.700  37.603  1.00 41.11           C  
-ATOM   2915  C   PHE B  65      44.769  47.983  37.394  1.00 39.94           C  
-ATOM   2916  O   PHE B  65      44.353  48.284  36.276  1.00 40.40           O  
-ATOM   2917  CB  PHE B  65      47.107  48.976  37.492  1.00 44.29           C  
-ATOM   2918  CG  PHE B  65      46.848  50.002  38.555  1.00 47.83           C  
-ATOM   2919  CD1 PHE B  65      46.634  49.632  39.877  1.00 49.39           C  
-ATOM   2920  CD2 PHE B  65      46.881  51.362  38.236  1.00 49.65           C  
-ATOM   2921  CE1 PHE B  65      46.457  50.604  40.868  1.00 49.76           C  
-ATOM   2922  CE2 PHE B  65      46.708  52.337  39.217  1.00 49.25           C  
-ATOM   2923  CZ  PHE B  65      46.496  51.957  40.535  1.00 49.50           C  
-ATOM   2924  N   ASN B  66      43.964  47.868  38.451  1.00 37.62           N  
-ATOM   2925  CA  ASN B  66      42.527  48.107  38.324  1.00 37.37           C  
-ATOM   2926  C   ASN B  66      41.902  48.916  39.464  1.00 35.93           C  
-ATOM   2927  O   ASN B  66      40.679  48.994  39.577  1.00 34.32           O  
-ATOM   2928  CB  ASN B  66      41.786  46.771  38.194  1.00 39.07           C  
-ATOM   2929  CG  ASN B  66      41.661  46.043  39.521  1.00 43.31           C  
-ATOM   2930  OD1 ASN B  66      42.620  45.962  40.292  1.00 46.18           O  
-ATOM   2931  ND2 ASN B  66      40.479  45.499  39.789  1.00 43.54           N  
-ATOM   2932  N   THR B  67      42.733  49.527  40.299  1.00 34.78           N  
-ATOM   2933  CA  THR B  67      42.229  50.310  41.417  1.00 34.71           C  
-ATOM   2934  C   THR B  67      42.579  51.792  41.279  1.00 33.97           C  
-ATOM   2935  O   THR B  67      42.730  52.502  42.270  1.00 33.74           O  
-ATOM   2936  CB  THR B  67      42.788  49.769  42.749  1.00 34.78           C  
-ATOM   2937  OG1 THR B  67      44.219  49.734  42.687  1.00 37.43           O  
-ATOM   2938  CG2 THR B  67      42.270  48.358  43.008  1.00 33.77           C  
-ATOM   2939  N   GLN B  68      42.689  52.253  40.038  1.00 33.82           N  
-ATOM   2940  CA  GLN B  68      43.035  53.642  39.753  1.00 34.14           C  
-ATOM   2941  C   GLN B  68      42.143  54.674  40.440  1.00 34.41           C  
-ATOM   2942  O   GLN B  68      42.619  55.737  40.844  1.00 35.13           O  
-ATOM   2943  CB  GLN B  68      43.019  53.898  38.239  1.00 32.67           C  
-ATOM   2944  CG  GLN B  68      44.069  53.120  37.458  1.00 35.91           C  
-ATOM   2945  CD  GLN B  68      43.589  51.759  36.975  1.00 36.82           C  
-ATOM   2946  OE1 GLN B  68      42.931  51.023  37.708  1.00 37.13           O  
-ATOM   2947  NE2 GLN B  68      43.932  51.415  35.735  1.00 36.95           N  
-ATOM   2948  N   ARG B  69      40.857  54.363  40.575  1.00 32.32           N  
-ATOM   2949  CA  ARG B  69      39.912  55.292  41.185  1.00 32.29           C  
-ATOM   2950  C   ARG B  69      39.937  55.356  42.709  1.00 33.64           C  
-ATOM   2951  O   ARG B  69      39.519  56.357  43.294  1.00 32.62           O  
-ATOM   2952  CB  ARG B  69      38.482  54.964  40.750  1.00 31.11           C  
-ATOM   2953  CG  ARG B  69      38.205  55.080  39.263  1.00 30.17           C  
-ATOM   2954  CD  ARG B  69      36.701  55.170  39.027  1.00 29.95           C  
-ATOM   2955  NE  ARG B  69      36.344  55.114  37.613  1.00 28.03           N  
-ATOM   2956  CZ  ARG B  69      36.301  53.996  36.895  1.00 28.41           C  
-ATOM   2957  NH1 ARG B  69      35.966  54.046  35.610  1.00 28.70           N  
-ATOM   2958  NH2 ARG B  69      36.578  52.828  37.463  1.00 27.25           N  
-ATOM   2959  N   ILE B  70      40.413  54.296  43.355  1.00 33.42           N  
-ATOM   2960  CA  ILE B  70      40.432  54.264  44.812  1.00 34.80           C  
-ATOM   2961  C   ILE B  70      41.814  54.128  45.431  1.00 36.35           C  
-ATOM   2962  O   ILE B  70      41.934  53.945  46.640  1.00 37.01           O  
-ATOM   2963  CB  ILE B  70      39.558  53.112  45.345  1.00 33.40           C  
-ATOM   2964  CG1 ILE B  70      40.113  51.772  44.857  1.00 32.34           C  
-ATOM   2965  CG2 ILE B  70      38.121  53.299  44.883  1.00 34.60           C  
-ATOM   2966  CD1 ILE B  70      39.369  50.562  45.393  1.00 32.63           C  
-ATOM   2967  N   ASN B  71      42.852  54.226  44.608  1.00 38.95           N  
-ATOM   2968  CA  ASN B  71      44.227  54.099  45.087  1.00 42.40           C  
-ATOM   2969  C   ASN B  71      44.565  55.129  46.167  1.00 42.71           C  
-ATOM   2970  O   ASN B  71      45.111  54.780  47.212  1.00 41.74           O  
-ATOM   2971  CB  ASN B  71      45.209  54.249  43.921  1.00 43.98           C  
-ATOM   2972  CG  ASN B  71      46.613  53.782  44.274  1.00 46.67           C  
-ATOM   2973  OD1 ASN B  71      47.602  54.445  43.948  1.00 47.76           O  
-ATOM   2974  ND2 ASN B  71      46.707  52.629  44.933  1.00 46.51           N  
-ATOM   2975  N   HIS B  72      44.234  56.393  45.909  1.00 43.29           N  
-ATOM   2976  CA  HIS B  72      44.514  57.473  46.854  1.00 43.83           C  
-ATOM   2977  C   HIS B  72      43.838  57.280  48.209  1.00 44.25           C  
-ATOM   2978  O   HIS B  72      44.272  57.841  49.212  1.00 45.36           O  
-ATOM   2979  CB  HIS B  72      44.082  58.820  46.265  1.00 42.88           C  
-ATOM   2980  CG  HIS B  72      42.610  58.927  46.009  1.00 43.61           C  
-ATOM   2981  ND1 HIS B  72      41.964  58.180  45.048  1.00 44.11           N  
-ATOM   2982  CD2 HIS B  72      41.658  59.698  46.588  1.00 43.31           C  
-ATOM   2983  CE1 HIS B  72      40.679  58.486  45.044  1.00 42.24           C  
-ATOM   2984  NE2 HIS B  72      40.467  59.404  45.969  1.00 42.41           N  
-ATOM   2985  N   ILE B  73      42.771  56.494  48.239  1.00 44.27           N  
-ATOM   2986  CA  ILE B  73      42.057  56.249  49.484  1.00 44.23           C  
-ATOM   2987  C   ILE B  73      42.709  55.084  50.225  1.00 45.73           C  
-ATOM   2988  O   ILE B  73      42.888  55.125  51.439  1.00 45.63           O  
-ATOM   2989  CB  ILE B  73      40.582  55.889  49.220  1.00 42.16           C  
-ATOM   2990  CG1 ILE B  73      39.932  56.947  48.333  1.00 39.63           C  
-ATOM   2991  CG2 ILE B  73      39.833  55.783  50.534  1.00 41.92           C  
-ATOM   2992  CD1 ILE B  73      38.542  56.563  47.867  1.00 38.24           C  
-ATOM   2993  N   TYR B  74      43.065  54.047  49.474  1.00 46.96           N  
-ATOM   2994  CA  TYR B  74      43.683  52.856  50.038  1.00 47.55           C  
-ATOM   2995  C   TYR B  74      45.064  53.147  50.616  1.00 48.41           C  
-ATOM   2996  O   TYR B  74      45.436  52.597  51.652  1.00 47.44           O  
-ATOM   2997  CB  TYR B  74      43.790  51.773  48.960  1.00 48.07           C  
-ATOM   2998  CG  TYR B  74      44.112  50.395  49.496  1.00 48.81           C  
-ATOM   2999  CD1 TYR B  74      45.331  49.781  49.211  1.00 49.96           C  
-ATOM   3000  CD2 TYR B  74      43.194  49.704  50.286  1.00 48.13           C  
-ATOM   3001  CE1 TYR B  74      45.626  48.505  49.702  1.00 51.58           C  
-ATOM   3002  CE2 TYR B  74      43.478  48.434  50.781  1.00 49.95           C  
-ATOM   3003  CZ  TYR B  74      44.694  47.841  50.487  1.00 51.07           C  
-ATOM   3004  OH  TYR B  74      44.980  46.588  50.983  1.00 51.60           O  
-ATOM   3005  N   ILE B  75      45.813  54.016  49.941  1.00 49.22           N  
-ATOM   3006  CA  ILE B  75      47.163  54.380  50.365  1.00 50.26           C  
-ATOM   3007  C   ILE B  75      47.202  55.403  51.503  1.00 51.64           C  
-ATOM   3008  O   ILE B  75      48.244  55.588  52.134  1.00 52.86           O  
-ATOM   3009  CB  ILE B  75      47.950  54.909  49.170  1.00 49.21           C  
-ATOM   3010  N   ASP B  76      46.078  56.067  51.762  1.00 51.91           N  
-ATOM   3011  CA  ASP B  76      46.010  57.065  52.827  1.00 51.74           C  
-ATOM   3012  C   ASP B  76      46.188  56.420  54.200  1.00 52.38           C  
-ATOM   3013  O   ASP B  76      46.768  57.016  55.111  1.00 54.09           O  
-ATOM   3014  CB  ASP B  76      44.675  57.806  52.764  1.00 51.38           C  
-ATOM   3015  N   LYS B  82      43.117  46.819  55.334  1.00 61.44           N  
-ATOM   3016  CA  LYS B  82      44.366  47.264  55.942  1.00 61.16           C  
-ATOM   3017  C   LYS B  82      44.111  48.211  57.119  1.00 60.62           C  
-ATOM   3018  O   LYS B  82      45.023  48.504  57.901  1.00 60.22           O  
-ATOM   3019  CB  LYS B  82      45.238  47.950  54.895  1.00 60.53           C  
-ATOM   3020  N   ALA B  83      42.870  48.679  57.240  1.00 59.29           N  
-ATOM   3021  CA  ALA B  83      42.477  49.589  58.314  1.00 58.38           C  
-ATOM   3022  C   ALA B  83      40.979  49.885  58.238  1.00 57.19           C  
-ATOM   3023  O   ALA B  83      40.163  49.111  58.738  1.00 57.37           O  
-ATOM   3024  CB  ALA B  83      43.272  50.890  58.219  1.00 59.49           C  
-ATOM   3025  N   LEU B  84      40.625  51.008  57.616  1.00 55.68           N  
-ATOM   3026  CA  LEU B  84      39.225  51.391  57.466  1.00 53.92           C  
-ATOM   3027  C   LEU B  84      38.695  51.051  56.074  1.00 52.33           C  
-ATOM   3028  O   LEU B  84      37.488  51.109  55.832  1.00 51.32           O  
-ATOM   3029  CB  LEU B  84      39.035  52.886  57.740  1.00 54.57           C  
-ATOM   3030  CG  LEU B  84      38.984  53.308  59.213  1.00 55.59           C  
-ATOM   3031  CD1 LEU B  84      38.713  54.803  59.304  1.00 54.97           C  
-ATOM   3032  CD2 LEU B  84      37.892  52.534  59.935  1.00 54.60           C  
-ATOM   3033  N   MET B  85      39.600  50.714  55.158  1.00 49.43           N  
-ATOM   3034  CA  MET B  85      39.207  50.332  53.807  1.00 46.56           C  
-ATOM   3035  C   MET B  85      39.970  49.089  53.372  1.00 44.42           C  
-ATOM   3036  O   MET B  85      41.169  49.156  53.092  1.00 44.54           O  
-ATOM   3037  CB  MET B  85      39.473  51.453  52.801  1.00 46.63           C  
-ATOM   3038  CG  MET B  85      38.959  51.098  51.409  1.00 47.97           C  
-ATOM   3039  SD  MET B  85      39.287  52.304  50.123  1.00 49.44           S  
-ATOM   3040  CE  MET B  85      40.379  51.394  49.055  1.00 47.52           C  
-ATOM   3041  N   LYS B  86      39.272  47.958  53.322  1.00 41.01           N  
-ATOM   3042  CA  LYS B  86      39.881  46.696  52.914  1.00 38.25           C  
-ATOM   3043  C   LYS B  86      39.314  46.235  51.568  1.00 36.87           C  
-ATOM   3044  O   LYS B  86      38.156  46.506  51.242  1.00 36.02           O  
-ATOM   3045  CB  LYS B  86      39.641  45.634  53.983  1.00 37.63           C  
-ATOM   3046  N   LEU B  87      40.142  45.545  50.790  1.00 34.46           N  
-ATOM   3047  CA  LEU B  87      39.742  45.050  49.478  1.00 32.56           C  
-ATOM   3048  C   LEU B  87      39.895  43.537  49.447  1.00 32.41           C  
-ATOM   3049  O   LEU B  87      40.900  43.002  49.908  1.00 33.52           O  
-ATOM   3050  CB  LEU B  87      40.612  45.689  48.392  1.00 30.76           C  
-ATOM   3051  CG  LEU B  87      40.548  47.221  48.323  1.00 28.34           C  
-ATOM   3052  CD1 LEU B  87      41.503  47.740  47.266  1.00 28.36           C  
-ATOM   3053  CD2 LEU B  87      39.125  47.664  48.018  1.00 28.07           C  
-ATOM   3054  N   HIS B  88      38.894  42.849  48.905  1.00 31.37           N  
-ATOM   3055  CA  HIS B  88      38.914  41.391  48.836  1.00 31.21           C  
-ATOM   3056  C   HIS B  88      38.572  40.896  47.435  1.00 30.49           C  
-ATOM   3057  O   HIS B  88      37.706  41.457  46.757  1.00 27.53           O  
-ATOM   3058  CB  HIS B  88      37.899  40.807  49.818  1.00 30.31           C  
-ATOM   3059  CG  HIS B  88      37.951  41.424  51.180  1.00 34.07           C  
-ATOM   3060  ND1 HIS B  88      38.888  41.068  52.125  1.00 34.12           N  
-ATOM   3061  CD2 HIS B  88      37.193  42.394  51.746  1.00 33.98           C  
-ATOM   3062  CE1 HIS B  88      38.704  41.790  53.216  1.00 35.15           C  
-ATOM   3063  NE2 HIS B  88      37.682  42.602  53.012  1.00 33.56           N  
-ATOM   3064  N   TYR B  89      39.243  39.827  47.019  1.00 29.72           N  
-ATOM   3065  CA  TYR B  89      39.008  39.241  45.709  1.00 29.18           C  
-ATOM   3066  C   TYR B  89      37.719  38.428  45.682  1.00 29.48           C  
-ATOM   3067  O   TYR B  89      37.477  37.582  46.548  1.00 29.41           O  
-ATOM   3068  CB  TYR B  89      40.177  38.346  45.305  1.00 27.65           C  
-ATOM   3069  CG  TYR B  89      41.421  39.104  44.915  1.00 29.18           C  
-ATOM   3070  CD1 TYR B  89      42.554  39.095  45.729  1.00 30.52           C  
-ATOM   3071  CD2 TYR B  89      41.475  39.814  43.719  1.00 29.39           C  
-ATOM   3072  CE1 TYR B  89      43.716  39.774  45.355  1.00 31.50           C  
-ATOM   3073  CE2 TYR B  89      42.622  40.495  43.336  1.00 31.41           C  
-ATOM   3074  CZ  TYR B  89      43.742  40.471  44.156  1.00 32.09           C  
-ATOM   3075  OH  TYR B  89      44.886  41.126  43.761  1.00 32.86           O  
-ATOM   3076  N   ALA B  90      36.898  38.697  44.673  1.00 27.36           N  
-ATOM   3077  CA  ALA B  90      35.633  38.007  44.492  1.00 25.47           C  
-ATOM   3078  C   ALA B  90      35.115  38.292  43.086  1.00 25.20           C  
-ATOM   3079  O   ALA B  90      35.720  39.048  42.327  1.00 25.59           O  
-ATOM   3080  CB  ALA B  90      34.621  38.483  45.527  1.00 24.61           C  
-ATOM   3081  N   ASP B  91      33.994  37.673  42.744  1.00 25.01           N  
-ATOM   3082  CA  ASP B  91      33.384  37.867  41.443  1.00 23.53           C  
-ATOM   3083  C   ASP B  91      31.905  37.569  41.587  1.00 22.31           C  
-ATOM   3084  O   ASP B  91      31.530  36.595  42.241  1.00 23.76           O  
-ATOM   3085  CB  ASP B  91      34.016  36.925  40.419  1.00 23.39           C  
-ATOM   3086  CG  ASP B  91      33.675  37.310  38.993  1.00 24.67           C  
-ATOM   3087  OD1 ASP B  91      32.507  37.138  38.591  1.00 25.61           O  
-ATOM   3088  OD2 ASP B  91      34.575  37.799  38.283  1.00 25.62           O  
-ATOM   3089  N   LEU B  92      31.060  38.408  40.994  1.00 22.71           N  
-ATOM   3090  CA  LEU B  92      29.623  38.193  41.092  1.00 22.57           C  
-ATOM   3091  C   LEU B  92      29.154  36.908  40.407  1.00 24.17           C  
-ATOM   3092  O   LEU B  92      27.993  36.527  40.538  1.00 25.53           O  
-ATOM   3093  CB  LEU B  92      28.856  39.394  40.535  1.00 23.85           C  
-ATOM   3094  CG  LEU B  92      28.255  40.290  41.627  1.00 25.06           C  
-ATOM   3095  CD1 LEU B  92      29.361  41.098  42.283  1.00 28.82           C  
-ATOM   3096  CD2 LEU B  92      27.212  41.209  41.037  1.00 28.40           C  
-ATOM   3097  N   THR B  93      30.041  36.235  39.680  1.00 23.17           N  
-ATOM   3098  CA  THR B  93      29.647  34.991  39.025  1.00 25.26           C  
-ATOM   3099  C   THR B  93      30.083  33.807  39.884  1.00 26.66           C  
-ATOM   3100  O   THR B  93      29.853  32.648  39.534  1.00 25.61           O  
-ATOM   3101  CB  THR B  93      30.271  34.846  37.610  1.00 24.06           C  
-ATOM   3102  OG1 THR B  93      31.700  34.793  37.706  1.00 25.63           O  
-ATOM   3103  CG2 THR B  93      29.859  36.016  36.730  1.00 24.40           C  
-ATOM   3104  N   ASP B  94      30.698  34.118  41.023  1.00 28.42           N  
-ATOM   3105  CA  ASP B  94      31.187  33.103  41.953  1.00 27.91           C  
-ATOM   3106  C   ASP B  94      30.480  33.288  43.295  1.00 28.73           C  
-ATOM   3107  O   ASP B  94      30.909  34.087  44.126  1.00 28.93           O  
-ATOM   3108  CB  ASP B  94      32.703  33.256  42.109  1.00 27.84           C  
-ATOM   3109  CG  ASP B  94      33.324  32.161  42.949  1.00 27.35           C  
-ATOM   3110  OD1 ASP B  94      34.566  32.013  42.902  1.00 28.12           O  
-ATOM   3111  OD2 ASP B  94      32.583  31.457  43.662  1.00 29.52           O  
-ATOM   3112  N   ALA B  95      29.397  32.540  43.496  1.00 28.19           N  
-ATOM   3113  CA  ALA B  95      28.599  32.625  44.717  1.00 27.10           C  
-ATOM   3114  C   ALA B  95      29.359  32.331  46.012  1.00 28.00           C  
-ATOM   3115  O   ALA B  95      29.040  32.890  47.063  1.00 28.44           O  
-ATOM   3116  CB  ALA B  95      27.382  31.703  44.603  1.00 25.13           C  
-ATOM   3117  N   SER B  96      30.354  31.454  45.946  1.00 28.93           N  
-ATOM   3118  CA  SER B  96      31.135  31.114  47.132  1.00 29.93           C  
-ATOM   3119  C   SER B  96      31.958  32.303  47.587  1.00 29.22           C  
-ATOM   3120  O   SER B  96      32.008  32.610  48.774  1.00 29.85           O  
-ATOM   3121  CB  SER B  96      32.078  29.955  46.843  1.00 31.99           C  
-ATOM   3122  OG  SER B  96      31.356  28.819  46.410  1.00 41.73           O  
-ATOM   3123  N   SER B  97      32.604  32.971  46.637  1.00 27.09           N  
-ATOM   3124  CA  SER B  97      33.432  34.120  46.963  1.00 27.90           C  
-ATOM   3125  C   SER B  97      32.603  35.205  47.636  1.00 28.19           C  
-ATOM   3126  O   SER B  97      33.106  35.936  48.486  1.00 29.17           O  
-ATOM   3127  CB  SER B  97      34.099  34.684  45.702  1.00 26.85           C  
-ATOM   3128  OG  SER B  97      33.181  35.423  44.914  1.00 27.74           O  
-ATOM   3129  N   LEU B  98      31.331  35.309  47.264  1.00 27.49           N  
-ATOM   3130  CA  LEU B  98      30.473  36.329  47.854  1.00 28.64           C  
-ATOM   3131  C   LEU B  98      30.107  35.980  49.293  1.00 29.87           C  
-ATOM   3132  O   LEU B  98      30.294  36.791  50.200  1.00 30.78           O  
-ATOM   3133  CB  LEU B  98      29.196  36.507  47.028  1.00 27.10           C  
-ATOM   3134  CG  LEU B  98      29.340  36.848  45.539  1.00 24.62           C  
-ATOM   3135  CD1 LEU B  98      27.955  36.987  44.939  1.00 22.22           C  
-ATOM   3136  CD2 LEU B  98      30.132  38.135  45.348  1.00 21.96           C  
-ATOM   3137  N   ARG B  99      29.587  34.774  49.500  1.00 30.63           N  
-ATOM   3138  CA  ARG B  99      29.193  34.335  50.835  1.00 33.40           C  
-ATOM   3139  C   ARG B  99      30.382  34.348  51.793  1.00 35.77           C  
-ATOM   3140  O   ARG B  99      30.251  34.755  52.948  1.00 37.01           O  
-ATOM   3141  CB  ARG B  99      28.579  32.931  50.778  1.00 31.76           C  
-ATOM   3142  CG  ARG B  99      28.204  32.343  52.144  1.00 31.59           C  
-ATOM   3143  CD  ARG B  99      27.226  33.240  52.905  1.00 31.88           C  
-ATOM   3144  NE  ARG B  99      26.967  32.746  54.255  1.00 31.13           N  
-ATOM   3145  CZ  ARG B  99      26.265  31.651  54.531  1.00 34.76           C  
-ATOM   3146  NH1 ARG B  99      25.744  30.931  53.547  1.00 34.73           N  
-ATOM   3147  NH2 ARG B  99      26.083  31.270  55.792  1.00 33.59           N  
-ATOM   3148  N   ARG B 100      31.539  33.908  51.305  1.00 36.88           N  
-ATOM   3149  CA  ARG B 100      32.756  33.866  52.108  1.00 39.46           C  
-ATOM   3150  C   ARG B 100      33.088  35.218  52.739  1.00 40.20           C  
-ATOM   3151  O   ARG B 100      33.324  35.300  53.941  1.00 40.15           O  
-ATOM   3152  CB  ARG B 100      33.936  33.392  51.249  1.00 42.02           C  
-ATOM   3153  CG  ARG B 100      35.312  33.601  51.871  1.00 43.29           C  
-ATOM   3154  CD  ARG B 100      36.395  32.929  51.033  1.00 46.33           C  
-ATOM   3155  NE  ARG B 100      37.741  33.211  51.526  1.00 48.53           N  
-ATOM   3156  CZ  ARG B 100      38.818  32.497  51.211  1.00 50.67           C  
-ATOM   3157  NH1 ARG B 100      40.003  32.829  51.706  1.00 51.60           N  
-ATOM   3158  NH2 ARG B 100      38.713  31.441  50.412  1.00 51.07           N  
-ATOM   3159  N   TRP B 101      33.108  36.274  51.931  1.00 38.47           N  
-ATOM   3160  CA  TRP B 101      33.425  37.593  52.452  1.00 38.08           C  
-ATOM   3161  C   TRP B 101      32.304  38.208  53.268  1.00 37.79           C  
-ATOM   3162  O   TRP B 101      32.548  39.080  54.100  1.00 38.80           O  
-ATOM   3163  CB  TRP B 101      33.848  38.522  51.315  1.00 36.65           C  
-ATOM   3164  CG  TRP B 101      35.181  38.117  50.802  1.00 37.30           C  
-ATOM   3165  CD1 TRP B 101      35.477  37.653  49.555  1.00 37.39           C  
-ATOM   3166  CD2 TRP B 101      36.390  38.021  51.564  1.00 37.07           C  
-ATOM   3167  NE1 TRP B 101      36.792  37.265  49.494  1.00 37.78           N  
-ATOM   3168  CE2 TRP B 101      37.377  37.480  50.714  1.00 37.30           C  
-ATOM   3169  CE3 TRP B 101      36.732  38.337  52.887  1.00 37.71           C  
-ATOM   3170  CZ2 TRP B 101      38.689  37.243  51.142  1.00 38.12           C  
-ATOM   3171  CZ3 TRP B 101      38.037  38.102  53.314  1.00 37.88           C  
-ATOM   3172  CH2 TRP B 101      38.998  37.559  52.441  1.00 38.42           C  
-ATOM   3173  N   ILE B 102      31.077  37.756  53.043  1.00 36.29           N  
-ATOM   3174  CA  ILE B 102      29.964  38.276  53.818  1.00 34.97           C  
-ATOM   3175  C   ILE B 102      30.097  37.711  55.226  1.00 34.59           C  
-ATOM   3176  O   ILE B 102      29.860  38.411  56.208  1.00 34.39           O  
-ATOM   3177  CB  ILE B 102      28.604  37.869  53.212  1.00 34.36           C  
-ATOM   3178  CG1 ILE B 102      28.406  38.602  51.881  1.00 33.40           C  
-ATOM   3179  CG2 ILE B 102      27.470  38.204  54.184  1.00 33.91           C  
-ATOM   3180  CD1 ILE B 102      27.044  38.416  51.264  1.00 33.53           C  
-ATOM   3181  N   ASP B 103      30.501  36.446  55.314  1.00 34.98           N  
-ATOM   3182  CA  ASP B 103      30.680  35.782  56.601  1.00 36.90           C  
-ATOM   3183  C   ASP B 103      31.842  36.389  57.371  1.00 36.94           C  
-ATOM   3184  O   ASP B 103      31.754  36.604  58.575  1.00 37.23           O  
-ATOM   3185  CB  ASP B 103      30.952  34.284  56.419  1.00 37.20           C  
-ATOM   3186  CG  ASP B 103      29.722  33.510  56.006  1.00 38.64           C  
-ATOM   3187  OD1 ASP B 103      28.601  34.006  56.246  1.00 40.34           O  
-ATOM   3188  OD2 ASP B 103      29.880  32.396  55.458  1.00 40.76           O  
-ATOM   3189  N   VAL B 104      32.932  36.657  56.664  1.00 36.81           N  
-ATOM   3190  CA  VAL B 104      34.121  37.225  57.274  1.00 37.23           C  
-ATOM   3191  C   VAL B 104      33.928  38.673  57.710  1.00 37.79           C  
-ATOM   3192  O   VAL B 104      34.350  39.061  58.800  1.00 38.09           O  
-ATOM   3193  CB  VAL B 104      35.315  37.164  56.299  1.00 35.79           C  
-ATOM   3194  CG1 VAL B 104      36.523  37.840  56.911  1.00 38.78           C  
-ATOM   3195  CG2 VAL B 104      35.632  35.724  55.960  1.00 37.03           C  
-ATOM   3196  N   ILE B 105      33.277  39.461  56.862  1.00 37.42           N  
-ATOM   3197  CA  ILE B 105      33.063  40.877  57.132  1.00 37.67           C  
-ATOM   3198  C   ILE B 105      31.905  41.229  58.065  1.00 38.53           C  
-ATOM   3199  O   ILE B 105      32.006  42.179  58.843  1.00 38.34           O  
-ATOM   3200  CB  ILE B 105      32.879  41.654  55.807  1.00 37.54           C  
-ATOM   3201  CG1 ILE B 105      34.102  41.437  54.908  1.00 38.06           C  
-ATOM   3202  CG2 ILE B 105      32.680  43.136  56.090  1.00 35.81           C  
-ATOM   3203  CD1 ILE B 105      33.969  42.031  53.520  1.00 36.64           C  
-ATOM   3204  N   LYS B 106      30.810  40.477  57.989  1.00 38.74           N  
-ATOM   3205  CA  LYS B 106      29.645  40.757  58.829  1.00 39.58           C  
-ATOM   3206  C   LYS B 106      29.243  42.213  58.623  1.00 38.90           C  
-ATOM   3207  O   LYS B 106      29.159  42.983  59.575  1.00 41.08           O  
-ATOM   3208  CB  LYS B 106      29.980  40.536  60.304  1.00 40.41           C  
-ATOM   3209  CG  LYS B 106      30.232  39.095  60.703  1.00 42.18           C  
-ATOM   3210  CD  LYS B 106      30.852  39.056  62.096  1.00 43.94           C  
-ATOM   3211  CE  LYS B 106      30.861  37.657  62.682  1.00 47.00           C  
-ATOM   3212  NZ  LYS B 106      29.485  37.191  63.024  1.00 49.03           N  
-ATOM   3213  N   PRO B 107      28.980  42.607  57.370  1.00 37.97           N  
-ATOM   3214  CA  PRO B 107      28.595  43.985  57.073  1.00 35.39           C  
-ATOM   3215  C   PRO B 107      27.214  44.368  57.570  1.00 34.39           C  
-ATOM   3216  O   PRO B 107      26.341  43.518  57.749  1.00 34.18           O  
-ATOM   3217  CB  PRO B 107      28.678  44.035  55.559  1.00 36.16           C  
-ATOM   3218  CG  PRO B 107      28.152  42.680  55.188  1.00 37.00           C  
-ATOM   3219  CD  PRO B 107      28.898  41.774  56.155  1.00 38.41           C  
-ATOM   3220  N   ASP B 108      27.032  45.667  57.777  1.00 31.97           N  
-ATOM   3221  CA  ASP B 108      25.768  46.214  58.230  1.00 33.26           C  
-ATOM   3222  C   ASP B 108      24.982  46.656  57.000  1.00 34.35           C  
-ATOM   3223  O   ASP B 108      23.758  46.538  56.943  1.00 33.87           O  
-ATOM   3224  CB  ASP B 108      26.023  47.409  59.157  1.00 33.22           C  
-ATOM   3225  CG  ASP B 108      26.802  47.018  60.404  1.00 33.84           C  
-ATOM   3226  OD1 ASP B 108      26.326  46.129  61.145  1.00 32.47           O  
-ATOM   3227  OD2 ASP B 108      27.888  47.591  60.641  1.00 31.65           O  
-ATOM   3228  N   GLU B 109      25.706  47.164  56.012  1.00 34.31           N  
-ATOM   3229  CA  GLU B 109      25.100  47.623  54.772  1.00 34.10           C  
-ATOM   3230  C   GLU B 109      25.831  47.017  53.581  1.00 32.98           C  
-ATOM   3231  O   GLU B 109      27.059  46.909  53.582  1.00 32.72           O  
-ATOM   3232  CB  GLU B 109      25.157  49.149  54.689  1.00 33.37           C  
-ATOM   3233  CG  GLU B 109      24.373  49.851  55.788  1.00 35.62           C  
-ATOM   3234  CD  GLU B 109      24.443  51.362  55.682  1.00 35.27           C  
-ATOM   3235  OE1 GLU B 109      23.712  52.043  56.432  1.00 37.44           O  
-ATOM   3236  OE2 GLU B 109      25.225  51.869  54.850  1.00 33.48           O  
-ATOM   3237  N   VAL B 110      25.067  46.611  52.573  1.00 31.56           N  
-ATOM   3238  CA  VAL B 110      25.640  46.027  51.367  1.00 29.76           C  
-ATOM   3239  C   VAL B 110      25.173  46.835  50.163  1.00 29.94           C  
-ATOM   3240  O   VAL B 110      23.977  47.051  49.972  1.00 30.45           O  
-ATOM   3241  CB  VAL B 110      25.214  44.543  51.195  1.00 28.72           C  
-ATOM   3242  CG1 VAL B 110      25.702  44.001  49.849  1.00 26.12           C  
-ATOM   3243  CG2 VAL B 110      25.779  43.710  52.336  1.00 26.05           C  
-ATOM   3244  N   TYR B 111      26.132  47.292  49.368  1.00 28.61           N  
-ATOM   3245  CA  TYR B 111      25.847  48.080  48.178  1.00 29.33           C  
-ATOM   3246  C   TYR B 111      26.311  47.290  46.960  1.00 29.32           C  
-ATOM   3247  O   TYR B 111      27.508  47.114  46.745  1.00 30.24           O  
-ATOM   3248  CB  TYR B 111      26.601  49.415  48.241  1.00 31.71           C  
-ATOM   3249  CG  TYR B 111      26.146  50.331  49.355  1.00 31.38           C  
-ATOM   3250  CD1 TYR B 111      25.202  51.330  49.121  1.00 31.44           C  
-ATOM   3251  CD2 TYR B 111      26.646  50.185  50.653  1.00 32.57           C  
-ATOM   3252  CE1 TYR B 111      24.765  52.166  50.153  1.00 32.87           C  
-ATOM   3253  CE2 TYR B 111      26.216  51.010  51.692  1.00 31.46           C  
-ATOM   3254  CZ  TYR B 111      25.277  52.000  51.435  1.00 33.31           C  
-ATOM   3255  OH  TYR B 111      24.853  52.821  52.455  1.00 32.14           O  
-ATOM   3256  N   ASN B 112      25.365  46.804  46.167  1.00 28.67           N  
-ATOM   3257  CA  ASN B 112      25.724  46.034  44.987  1.00 25.69           C  
-ATOM   3258  C   ASN B 112      25.822  46.942  43.777  1.00 25.55           C  
-ATOM   3259  O   ASN B 112      24.822  47.214  43.114  1.00 24.63           O  
-ATOM   3260  CB  ASN B 112      24.695  44.935  44.728  1.00 25.34           C  
-ATOM   3261  CG  ASN B 112      25.045  44.096  43.519  1.00 22.84           C  
-ATOM   3262  OD1 ASN B 112      26.157  43.584  43.408  1.00 22.63           O  
-ATOM   3263  ND2 ASN B 112      24.097  43.952  42.605  1.00 24.59           N  
-ATOM   3264  N   LEU B 113      27.034  47.408  43.492  1.00 23.91           N  
-ATOM   3265  CA  LEU B 113      27.262  48.295  42.362  1.00 24.06           C  
-ATOM   3266  C   LEU B 113      27.975  47.571  41.229  1.00 24.76           C  
-ATOM   3267  O   LEU B 113      28.115  48.113  40.132  1.00 26.26           O  
-ATOM   3268  CB  LEU B 113      28.108  49.494  42.798  1.00 23.42           C  
-ATOM   3269  CG  LEU B 113      27.738  50.149  44.131  1.00 25.20           C  
-ATOM   3270  CD1 LEU B 113      28.702  51.298  44.405  1.00 25.01           C  
-ATOM   3271  CD2 LEU B 113      26.295  50.643  44.100  1.00 24.60           C  
-ATOM   3272  N   ALA B 114      28.427  46.350  41.499  1.00 22.93           N  
-ATOM   3273  CA  ALA B 114      29.149  45.571  40.502  1.00 24.22           C  
-ATOM   3274  C   ALA B 114      28.298  45.259  39.277  1.00 23.87           C  
-ATOM   3275  O   ALA B 114      27.150  44.835  39.396  1.00 24.03           O  
-ATOM   3276  CB  ALA B 114      29.661  44.275  41.122  1.00 22.70           C  
-ATOM   3277  N   ALA B 115      28.867  45.476  38.098  1.00 24.18           N  
-ATOM   3278  CA  ALA B 115      28.151  45.188  36.865  1.00 23.73           C  
-ATOM   3279  C   ALA B 115      28.954  45.438  35.601  1.00 23.42           C  
-ATOM   3280  O   ALA B 115      29.897  46.226  35.589  1.00 23.48           O  
-ATOM   3281  CB  ALA B 115      26.868  46.007  36.808  1.00 22.33           C  
-ATOM   3282  N   GLN B 116      28.588  44.717  34.547  1.00 23.96           N  
-ATOM   3283  CA  GLN B 116      29.169  44.929  33.229  1.00 22.80           C  
-ATOM   3284  C   GLN B 116      28.183  46.049  32.888  1.00 22.96           C  
-ATOM   3285  O   GLN B 116      27.052  45.791  32.475  1.00 23.29           O  
-ATOM   3286  CB  GLN B 116      28.942  43.700  32.345  1.00 21.40           C  
-ATOM   3287  CG  GLN B 116      29.602  43.770  30.978  1.00 22.22           C  
-ATOM   3288  CD  GLN B 116      29.141  44.967  30.177  1.00 22.64           C  
-ATOM   3289  OE1 GLN B 116      29.678  46.069  30.313  1.00 23.86           O  
-ATOM   3290  NE2 GLN B 116      28.126  44.764  29.348  1.00 22.72           N  
-ATOM   3291  N   SER B 117      28.604  47.289  33.104  1.00 24.17           N  
-ATOM   3292  CA  SER B 117      27.724  48.438  32.923  1.00 26.42           C  
-ATOM   3293  C   SER B 117      27.601  49.122  31.568  1.00 27.13           C  
-ATOM   3294  O   SER B 117      26.817  50.063  31.440  1.00 27.53           O  
-ATOM   3295  CB  SER B 117      28.063  49.504  33.975  1.00 25.38           C  
-ATOM   3296  OG  SER B 117      29.335  50.083  33.734  1.00 27.17           O  
-ATOM   3297  N   HIS B 118      28.353  48.682  30.563  1.00 27.94           N  
-ATOM   3298  CA  HIS B 118      28.250  49.331  29.261  1.00 26.67           C  
-ATOM   3299  C   HIS B 118      27.161  48.699  28.403  1.00 24.97           C  
-ATOM   3300  O   HIS B 118      27.194  47.508  28.104  1.00 24.46           O  
-ATOM   3301  CB  HIS B 118      29.595  49.309  28.533  1.00 27.42           C  
-ATOM   3302  CG  HIS B 118      29.716  50.368  27.483  1.00 30.70           C  
-ATOM   3303  ND1 HIS B 118      29.055  50.298  26.275  1.00 33.17           N  
-ATOM   3304  CD2 HIS B 118      30.368  51.555  27.486  1.00 32.67           C  
-ATOM   3305  CE1 HIS B 118      29.295  51.396  25.579  1.00 34.00           C  
-ATOM   3306  NE2 HIS B 118      30.088  52.175  26.292  1.00 34.87           N  
-ATOM   3307  N   VAL B 119      26.189  49.518  28.015  1.00 25.49           N  
-ATOM   3308  CA  VAL B 119      25.062  49.061  27.219  1.00 24.76           C  
-ATOM   3309  C   VAL B 119      25.447  48.478  25.872  1.00 26.37           C  
-ATOM   3310  O   VAL B 119      24.959  47.415  25.495  1.00 26.82           O  
-ATOM   3311  CB  VAL B 119      24.040  50.207  27.003  1.00 26.33           C  
-ATOM   3312  CG1 VAL B 119      22.979  49.795  25.982  1.00 21.33           C  
-ATOM   3313  CG2 VAL B 119      23.381  50.558  28.327  1.00 24.54           C  
-ATOM   3314  N   ALA B 120      26.316  49.169  25.142  1.00 27.64           N  
-ATOM   3315  CA  ALA B 120      26.729  48.686  23.829  1.00 28.06           C  
-ATOM   3316  C   ALA B 120      27.431  47.344  23.955  1.00 28.29           C  
-ATOM   3317  O   ALA B 120      27.197  46.433  23.166  1.00 31.34           O  
-ATOM   3318  CB  ALA B 120      27.649  49.701  23.154  1.00 26.22           C  
-ATOM   3319  N   VAL B 121      28.291  47.222  24.957  1.00 29.55           N  
-ATOM   3320  CA  VAL B 121      29.025  45.985  25.174  1.00 27.77           C  
-ATOM   3321  C   VAL B 121      28.097  44.816  25.487  1.00 27.76           C  
-ATOM   3322  O   VAL B 121      28.379  43.677  25.106  1.00 29.00           O  
-ATOM   3323  CB  VAL B 121      30.046  46.153  26.319  1.00 28.32           C  
-ATOM   3324  CG1 VAL B 121      30.733  44.831  26.617  1.00 26.23           C  
-ATOM   3325  CG2 VAL B 121      31.077  47.203  25.927  1.00 27.60           C  
-ATOM   3326  N   SER B 122      26.984  45.093  26.159  1.00 26.53           N  
-ATOM   3327  CA  SER B 122      26.048  44.031  26.508  1.00 26.40           C  
-ATOM   3328  C   SER B 122      25.473  43.323  25.283  1.00 26.47           C  
-ATOM   3329  O   SER B 122      25.092  42.160  25.366  1.00 28.04           O  
-ATOM   3330  CB  SER B 122      24.910  44.565  27.387  1.00 25.96           C  
-ATOM   3331  OG  SER B 122      23.982  45.344  26.654  1.00 27.94           O  
-ATOM   3332  N   PHE B 123      25.401  44.010  24.147  1.00 27.31           N  
-ATOM   3333  CA  PHE B 123      24.880  43.367  22.943  1.00 27.26           C  
-ATOM   3334  C   PHE B 123      25.894  42.353  22.424  1.00 27.74           C  
-ATOM   3335  O   PHE B 123      25.527  41.370  21.791  1.00 28.89           O  
-ATOM   3336  CB  PHE B 123      24.584  44.391  21.843  1.00 24.65           C  
-ATOM   3337  CG  PHE B 123      23.368  45.227  22.100  1.00 25.91           C  
-ATOM   3338  CD1 PHE B 123      23.480  46.485  22.683  1.00 28.30           C  
-ATOM   3339  CD2 PHE B 123      22.106  44.760  21.754  1.00 25.36           C  
-ATOM   3340  CE1 PHE B 123      22.350  47.267  22.913  1.00 27.90           C  
-ATOM   3341  CE2 PHE B 123      20.970  45.532  21.979  1.00 24.89           C  
-ATOM   3342  CZ  PHE B 123      21.091  46.787  22.557  1.00 27.32           C  
-ATOM   3343  N   GLU B 124      27.169  42.589  22.709  1.00 29.27           N  
-ATOM   3344  CA  GLU B 124      28.225  41.687  22.259  1.00 32.48           C  
-ATOM   3345  C   GLU B 124      28.449  40.518  23.215  1.00 30.82           C  
-ATOM   3346  O   GLU B 124      28.815  39.426  22.786  1.00 29.92           O  
-ATOM   3347  CB  GLU B 124      29.529  42.459  22.080  1.00 34.25           C  
-ATOM   3348  CG  GLU B 124      29.333  43.801  21.409  1.00 43.00           C  
-ATOM   3349  CD  GLU B 124      30.465  44.149  20.477  1.00 46.70           C  
-ATOM   3350  OE1 GLU B 124      30.582  43.493  19.421  1.00 49.99           O  
-ATOM   3351  OE2 GLU B 124      31.238  45.073  20.803  1.00 51.66           O  
-ATOM   3352  N   ILE B 125      28.247  40.753  24.509  1.00 29.11           N  
-ATOM   3353  CA  ILE B 125      28.409  39.698  25.506  1.00 28.90           C  
-ATOM   3354  C   ILE B 125      27.181  39.667  26.411  1.00 28.98           C  
-ATOM   3355  O   ILE B 125      27.265  39.968  27.599  1.00 28.83           O  
-ATOM   3356  CB  ILE B 125      29.683  39.905  26.381  1.00 28.54           C  
-ATOM   3357  CG1 ILE B 125      29.688  41.310  26.986  1.00 27.59           C  
-ATOM   3358  CG2 ILE B 125      30.941  39.654  25.545  1.00 27.24           C  
-ATOM   3359  CD1 ILE B 125      30.834  41.569  27.933  1.00 25.77           C  
-ATOM   3360  N   PRO B 126      26.015  39.310  25.847  1.00 27.96           N  
-ATOM   3361  CA  PRO B 126      24.763  39.243  26.606  1.00 26.88           C  
-ATOM   3362  C   PRO B 126      24.770  38.215  27.734  1.00 26.23           C  
-ATOM   3363  O   PRO B 126      24.325  38.500  28.846  1.00 27.42           O  
-ATOM   3364  CB  PRO B 126      23.723  38.914  25.529  1.00 26.65           C  
-ATOM   3365  CG  PRO B 126      24.520  38.126  24.519  1.00 25.35           C  
-ATOM   3366  CD  PRO B 126      25.796  38.929  24.439  1.00 25.52           C  
-ATOM   3367  N   ASP B 127      25.273  37.022  27.444  1.00 27.60           N  
-ATOM   3368  CA  ASP B 127      25.314  35.956  28.436  1.00 28.49           C  
-ATOM   3369  C   ASP B 127      26.131  36.338  29.669  1.00 26.90           C  
-ATOM   3370  O   ASP B 127      25.656  36.212  30.795  1.00 24.80           O  
-ATOM   3371  CB  ASP B 127      25.867  34.682  27.805  1.00 32.99           C  
-ATOM   3372  CG  ASP B 127      25.057  34.237  26.600  1.00 40.87           C  
-ATOM   3373  OD1 ASP B 127      23.859  33.913  26.764  1.00 42.13           O  
-ATOM   3374  OD2 ASP B 127      25.614  34.220  25.482  1.00 47.06           O  
-ATOM   3375  N   TYR B 128      27.360  36.799  29.460  1.00 26.79           N  
-ATOM   3376  CA  TYR B 128      28.195  37.198  30.585  1.00 26.27           C  
-ATOM   3377  C   TYR B 128      27.526  38.338  31.347  1.00 25.93           C  
-ATOM   3378  O   TYR B 128      27.475  38.332  32.577  1.00 25.14           O  
-ATOM   3379  CB  TYR B 128      29.571  37.669  30.117  1.00 23.96           C  
-ATOM   3380  CG  TYR B 128      30.387  38.247  31.248  1.00 24.26           C  
-ATOM   3381  CD1 TYR B 128      31.089  37.417  32.126  1.00 24.36           C  
-ATOM   3382  CD2 TYR B 128      30.410  39.626  31.480  1.00 24.02           C  
-ATOM   3383  CE1 TYR B 128      31.791  37.947  33.206  1.00 22.13           C  
-ATOM   3384  CE2 TYR B 128      31.104  40.165  32.555  1.00 21.72           C  
-ATOM   3385  CZ  TYR B 128      31.793  39.323  33.415  1.00 23.76           C  
-ATOM   3386  OH  TYR B 128      32.471  39.860  34.487  1.00 25.88           O  
-ATOM   3387  N   THR B 129      27.023  39.318  30.604  1.00 24.31           N  
-ATOM   3388  CA  THR B 129      26.364  40.466  31.207  1.00 23.70           C  
-ATOM   3389  C   THR B 129      25.206  40.037  32.104  1.00 24.60           C  
-ATOM   3390  O   THR B 129      25.078  40.511  33.232  1.00 25.43           O  
-ATOM   3391  CB  THR B 129      25.824  41.431  30.131  1.00 24.36           C  
-ATOM   3392  OG1 THR B 129      26.919  41.970  29.378  1.00 25.63           O  
-ATOM   3393  CG2 THR B 129      25.049  42.572  30.779  1.00 23.77           C  
-ATOM   3394  N   ALA B 130      24.370  39.136  31.599  1.00 22.65           N  
-ATOM   3395  CA  ALA B 130      23.221  38.658  32.352  1.00 22.95           C  
-ATOM   3396  C   ALA B 130      23.651  37.923  33.613  1.00 24.59           C  
-ATOM   3397  O   ALA B 130      23.052  38.099  34.676  1.00 25.97           O  
-ATOM   3398  CB  ALA B 130      22.368  37.737  31.478  1.00 22.27           C  
-ATOM   3399  N   ASP B 131      24.684  37.093  33.489  1.00 22.69           N  
-ATOM   3400  CA  ASP B 131      25.184  36.323  34.617  1.00 22.34           C  
-ATOM   3401  C   ASP B 131      25.678  37.238  35.741  1.00 24.21           C  
-ATOM   3402  O   ASP B 131      25.553  36.909  36.917  1.00 24.21           O  
-ATOM   3403  CB  ASP B 131      26.313  35.394  34.155  1.00 24.78           C  
-ATOM   3404  CG  ASP B 131      26.640  34.316  35.172  1.00 21.58           C  
-ATOM   3405  OD1 ASP B 131      25.702  33.748  35.764  1.00 20.83           O  
-ATOM   3406  OD2 ASP B 131      27.837  34.022  35.366  1.00 26.58           O  
-ATOM   3407  N   VAL B 132      26.223  38.391  35.376  1.00 23.37           N  
-ATOM   3408  CA  VAL B 132      26.735  39.330  36.365  1.00 25.26           C  
-ATOM   3409  C   VAL B 132      25.696  40.340  36.870  1.00 26.73           C  
-ATOM   3410  O   VAL B 132      25.543  40.545  38.077  1.00 26.31           O  
-ATOM   3411  CB  VAL B 132      27.937  40.109  35.794  1.00 23.96           C  
-ATOM   3412  CG1 VAL B 132      28.404  41.156  36.784  1.00 23.60           C  
-ATOM   3413  CG2 VAL B 132      29.065  39.143  35.469  1.00 22.12           C  
-ATOM   3414  N   VAL B 133      24.978  40.955  35.941  1.00 25.81           N  
-ATOM   3415  CA  VAL B 133      23.994  41.968  36.286  1.00 25.62           C  
-ATOM   3416  C   VAL B 133      22.678  41.431  36.841  1.00 26.24           C  
-ATOM   3417  O   VAL B 133      22.078  42.042  37.724  1.00 25.89           O  
-ATOM   3418  CB  VAL B 133      23.709  42.864  35.066  1.00 24.38           C  
-ATOM   3419  CG1 VAL B 133      22.676  43.922  35.414  1.00 21.30           C  
-ATOM   3420  CG2 VAL B 133      25.004  43.512  34.603  1.00 22.48           C  
-ATOM   3421  N   ALA B 134      22.230  40.294  36.327  1.00 26.52           N  
-ATOM   3422  CA  ALA B 134      20.979  39.710  36.788  1.00 25.45           C  
-ATOM   3423  C   ALA B 134      21.213  38.630  37.843  1.00 25.42           C  
-ATOM   3424  O   ALA B 134      20.953  38.845  39.023  1.00 26.18           O  
-ATOM   3425  CB  ALA B 134      20.208  39.139  35.608  1.00 25.08           C  
-ATOM   3426  N   THR B 135      21.704  37.471  37.421  1.00 24.68           N  
-ATOM   3427  CA  THR B 135      21.947  36.375  38.350  1.00 23.27           C  
-ATOM   3428  C   THR B 135      22.964  36.760  39.429  1.00 24.48           C  
-ATOM   3429  O   THR B 135      22.859  36.320  40.571  1.00 23.49           O  
-ATOM   3430  CB  THR B 135      22.436  35.116  37.605  1.00 22.78           C  
-ATOM   3431  OG1 THR B 135      21.507  34.786  36.563  1.00 24.68           O  
-ATOM   3432  CG2 THR B 135      22.529  33.933  38.559  1.00 22.99           C  
-ATOM   3433  N   GLY B 136      23.939  37.586  39.062  1.00 23.44           N  
-ATOM   3434  CA  GLY B 136      24.948  38.018  40.016  1.00 25.06           C  
-ATOM   3435  C   GLY B 136      24.311  38.748  41.184  1.00 25.73           C  
-ATOM   3436  O   GLY B 136      24.702  38.560  42.335  1.00 25.57           O  
-ATOM   3437  N   ALA B 137      23.326  39.587  40.883  1.00 24.88           N  
-ATOM   3438  CA  ALA B 137      22.617  40.332  41.910  1.00 26.23           C  
-ATOM   3439  C   ALA B 137      21.834  39.347  42.779  1.00 26.64           C  
-ATOM   3440  O   ALA B 137      21.699  39.534  43.989  1.00 27.76           O  
-ATOM   3441  CB  ALA B 137      21.669  41.340  41.261  1.00 25.57           C  
-ATOM   3442  N   LEU B 138      21.318  38.293  42.155  1.00 24.66           N  
-ATOM   3443  CA  LEU B 138      20.566  37.286  42.889  1.00 24.28           C  
-ATOM   3444  C   LEU B 138      21.506  36.497  43.802  1.00 25.23           C  
-ATOM   3445  O   LEU B 138      21.146  36.169  44.935  1.00 25.50           O  
-ATOM   3446  CB  LEU B 138      19.846  36.341  41.922  1.00 22.86           C  
-ATOM   3447  CG  LEU B 138      18.986  35.241  42.553  1.00 22.94           C  
-ATOM   3448  CD1 LEU B 138      18.018  35.855  43.565  1.00 24.12           C  
-ATOM   3449  CD2 LEU B 138      18.216  34.500  41.462  1.00 23.22           C  
-ATOM   3450  N   ARG B 139      22.707  36.189  43.314  1.00 23.49           N  
-ATOM   3451  CA  ARG B 139      23.672  35.458  44.123  1.00 23.77           C  
-ATOM   3452  C   ARG B 139      23.988  36.238  45.397  1.00 26.13           C  
-ATOM   3453  O   ARG B 139      24.077  35.656  46.473  1.00 24.41           O  
-ATOM   3454  CB  ARG B 139      24.976  35.223  43.357  1.00 23.65           C  
-ATOM   3455  CG  ARG B 139      24.858  34.287  42.172  1.00 26.19           C  
-ATOM   3456  CD  ARG B 139      26.225  33.914  41.609  1.00 24.29           C  
-ATOM   3457  NE  ARG B 139      26.075  33.072  40.424  1.00 27.32           N  
-ATOM   3458  CZ  ARG B 139      26.002  33.528  39.177  1.00 25.05           C  
-ATOM   3459  NH1 ARG B 139      25.852  32.676  38.178  1.00 27.14           N  
-ATOM   3460  NH2 ARG B 139      26.109  34.822  38.922  1.00 23.37           N  
-ATOM   3461  N   LEU B 140      24.161  37.553  45.271  1.00 25.63           N  
-ATOM   3462  CA  LEU B 140      24.479  38.391  46.428  1.00 28.54           C  
-ATOM   3463  C   LEU B 140      23.296  38.406  47.390  1.00 28.81           C  
-ATOM   3464  O   LEU B 140      23.456  38.155  48.584  1.00 29.96           O  
-ATOM   3465  CB  LEU B 140      24.821  39.828  45.994  1.00 26.63           C  
-ATOM   3466  CG  LEU B 140      25.461  40.699  47.083  1.00 25.95           C  
-ATOM   3467  CD1 LEU B 140      26.747  40.032  47.565  1.00 27.11           C  
-ATOM   3468  CD2 LEU B 140      25.748  42.096  46.558  1.00 23.95           C  
-ATOM   3469  N   LEU B 141      22.113  38.697  46.862  1.00 28.47           N  
-ATOM   3470  CA  LEU B 141      20.901  38.719  47.672  1.00 27.86           C  
-ATOM   3471  C   LEU B 141      20.784  37.432  48.465  1.00 28.15           C  
-ATOM   3472  O   LEU B 141      20.574  37.462  49.677  1.00 30.14           O  
-ATOM   3473  CB  LEU B 141      19.657  38.864  46.793  1.00 25.65           C  
-ATOM   3474  CG  LEU B 141      19.341  40.226  46.166  1.00 27.56           C  
-ATOM   3475  CD1 LEU B 141      18.264  40.064  45.097  1.00 25.83           C  
-ATOM   3476  CD2 LEU B 141      18.876  41.188  47.248  1.00 27.77           C  
-ATOM   3477  N   GLU B 142      20.922  36.303  47.774  1.00 27.54           N  
-ATOM   3478  CA  GLU B 142      20.806  34.992  48.403  1.00 28.51           C  
-ATOM   3479  C   GLU B 142      21.925  34.718  49.402  1.00 28.33           C  
-ATOM   3480  O   GLU B 142      21.724  34.002  50.383  1.00 28.33           O  
-ATOM   3481  CB  GLU B 142      20.768  33.893  47.331  1.00 26.41           C  
-ATOM   3482  CG  GLU B 142      20.726  32.471  47.872  1.00 26.69           C  
-ATOM   3483  CD  GLU B 142      19.533  32.195  48.787  1.00 30.46           C  
-ATOM   3484  OE1 GLU B 142      18.598  33.021  48.847  1.00 30.59           O  
-ATOM   3485  OE2 GLU B 142      19.529  31.133  49.443  1.00 33.12           O  
-ATOM   3486  N   ALA B 143      23.102  35.277  49.149  1.00 28.17           N  
-ATOM   3487  CA  ALA B 143      24.230  35.098  50.054  1.00 28.21           C  
-ATOM   3488  C   ALA B 143      23.949  35.902  51.331  1.00 29.04           C  
-ATOM   3489  O   ALA B 143      24.257  35.459  52.433  1.00 28.18           O  
-ATOM   3490  CB  ALA B 143      25.514  35.587  49.397  1.00 26.61           C  
-ATOM   3491  N   VAL B 144      23.359  37.083  51.169  1.00 29.45           N  
-ATOM   3492  CA  VAL B 144      23.035  37.930  52.306  1.00 31.95           C  
-ATOM   3493  C   VAL B 144      21.897  37.327  53.121  1.00 33.62           C  
-ATOM   3494  O   VAL B 144      21.917  37.383  54.349  1.00 35.62           O  
-ATOM   3495  CB  VAL B 144      22.648  39.361  51.855  1.00 30.45           C  
-ATOM   3496  CG1 VAL B 144      22.024  40.125  53.009  1.00 30.58           C  
-ATOM   3497  CG2 VAL B 144      23.884  40.099  51.370  1.00 29.65           C  
-ATOM   3498  N   ARG B 145      20.909  36.743  52.447  1.00 35.24           N  
-ATOM   3499  CA  ARG B 145      19.786  36.136  53.153  1.00 35.45           C  
-ATOM   3500  C   ARG B 145      20.270  34.944  53.973  1.00 35.47           C  
-ATOM   3501  O   ARG B 145      19.948  34.821  55.154  1.00 35.25           O  
-ATOM   3502  CB  ARG B 145      18.709  35.661  52.174  1.00 35.42           C  
-ATOM   3503  CG  ARG B 145      17.429  35.183  52.866  1.00 36.48           C  
-ATOM   3504  CD  ARG B 145      16.566  34.325  51.950  1.00 41.32           C  
-ATOM   3505  NE  ARG B 145      17.247  33.088  51.571  1.00 45.58           N  
-ATOM   3506  CZ  ARG B 145      17.601  32.134  52.429  1.00 47.22           C  
-ATOM   3507  NH1 ARG B 145      17.332  32.269  53.720  1.00 49.36           N  
-ATOM   3508  NH2 ARG B 145      18.239  31.051  52.003  1.00 47.50           N  
-ATOM   3509  N   SER B 146      21.041  34.067  53.339  1.00 34.70           N  
-ATOM   3510  CA  SER B 146      21.565  32.882  54.006  1.00 37.19           C  
-ATOM   3511  C   SER B 146      22.415  33.256  55.210  1.00 38.35           C  
-ATOM   3512  O   SER B 146      22.389  32.572  56.233  1.00 39.69           O  
-ATOM   3513  CB  SER B 146      22.406  32.050  53.034  1.00 36.43           C  
-ATOM   3514  OG  SER B 146      21.619  31.576  51.959  1.00 39.30           O  
-ATOM   3515  N   HIS B 147      23.174  34.338  55.074  1.00 37.71           N  
-ATOM   3516  CA  HIS B 147      24.035  34.815  56.146  1.00 39.13           C  
-ATOM   3517  C   HIS B 147      23.227  35.284  57.350  1.00 39.53           C  
-ATOM   3518  O   HIS B 147      23.459  34.840  58.471  1.00 41.44           O  
-ATOM   3519  CB  HIS B 147      24.914  35.962  55.642  1.00 38.71           C  
-ATOM   3520  CG  HIS B 147      25.631  36.699  56.730  1.00 39.79           C  
-ATOM   3521  ND1 HIS B 147      26.600  36.113  57.516  1.00 39.30           N  
-ATOM   3522  CD2 HIS B 147      25.511  37.975  57.169  1.00 39.30           C  
-ATOM   3523  CE1 HIS B 147      27.047  36.996  58.392  1.00 39.92           C  
-ATOM   3524  NE2 HIS B 147      26.403  38.134  58.203  1.00 40.06           N  
-ATOM   3525  N   THR B 148      22.275  36.179  57.111  1.00 39.87           N  
-ATOM   3526  CA  THR B 148      21.452  36.712  58.185  1.00 41.63           C  
-ATOM   3527  C   THR B 148      20.680  35.632  58.932  1.00 43.29           C  
-ATOM   3528  O   THR B 148      20.466  35.741  60.136  1.00 44.19           O  
-ATOM   3529  CB  THR B 148      20.450  37.749  57.658  1.00 40.47           C  
-ATOM   3530  OG1 THR B 148      19.551  37.123  56.739  1.00 38.89           O  
-ATOM   3531  CG2 THR B 148      21.182  38.881  56.963  1.00 39.78           C  
-ATOM   3532  N   ILE B 149      20.261  34.592  58.221  1.00 45.09           N  
-ATOM   3533  CA  ILE B 149      19.510  33.511  58.845  1.00 47.01           C  
-ATOM   3534  C   ILE B 149      20.413  32.565  59.630  1.00 47.31           C  
-ATOM   3535  O   ILE B 149      20.089  32.169  60.748  1.00 47.21           O  
-ATOM   3536  CB  ILE B 149      18.720  32.696  57.792  1.00 47.51           C  
-ATOM   3537  CG1 ILE B 149      17.605  33.560  57.198  1.00 49.16           C  
-ATOM   3538  CG2 ILE B 149      18.132  31.443  58.423  1.00 47.98           C  
-ATOM   3539  CD1 ILE B 149      16.580  34.049  58.218  1.00 50.13           C  
-ATOM   3540  N   ASP B 150      21.548  32.211  59.040  1.00 46.77           N  
-ATOM   3541  CA  ASP B 150      22.488  31.304  59.679  1.00 47.04           C  
-ATOM   3542  C   ASP B 150      23.184  31.926  60.894  1.00 47.56           C  
-ATOM   3543  O   ASP B 150      23.547  31.218  61.834  1.00 47.25           O  
-ATOM   3544  CB  ASP B 150      23.537  30.849  58.659  1.00 47.01           C  
-ATOM   3545  CG  ASP B 150      24.502  29.826  59.227  1.00 46.51           C  
-ATOM   3546  OD1 ASP B 150      24.064  28.704  59.566  1.00 48.35           O  
-ATOM   3547  OD2 ASP B 150      25.701  30.144  59.336  1.00 47.36           O  
-ATOM   3548  N   SER B 151      23.362  33.245  60.878  1.00 47.47           N  
-ATOM   3549  CA  SER B 151      24.039  33.936  61.974  1.00 47.49           C  
-ATOM   3550  C   SER B 151      23.130  34.845  62.800  1.00 46.30           C  
-ATOM   3551  O   SER B 151      23.545  35.365  63.835  1.00 46.55           O  
-ATOM   3552  CB  SER B 151      25.199  34.770  61.428  1.00 47.64           C  
-ATOM   3553  OG  SER B 151      24.712  35.915  60.746  1.00 49.94           O  
-ATOM   3554  N   GLY B 152      21.904  35.052  62.335  1.00 45.08           N  
-ATOM   3555  CA  GLY B 152      20.974  35.899  63.060  1.00 43.73           C  
-ATOM   3556  C   GLY B 152      21.268  37.387  62.971  1.00 44.02           C  
-ATOM   3557  O   GLY B 152      20.660  38.180  63.689  1.00 45.43           O  
-ATOM   3558  N   ARG B 153      22.187  37.780  62.096  1.00 43.06           N  
-ATOM   3559  CA  ARG B 153      22.523  39.193  61.955  1.00 42.82           C  
-ATOM   3560  C   ARG B 153      21.540  39.920  61.050  1.00 42.20           C  
-ATOM   3561  O   ARG B 153      20.698  39.294  60.410  1.00 44.09           O  
-ATOM   3562  CB  ARG B 153      23.940  39.359  61.403  1.00 42.77           C  
-ATOM   3563  CG  ARG B 153      25.025  38.858  62.334  1.00 43.28           C  
-ATOM   3564  CD  ARG B 153      26.407  39.326  61.895  1.00 43.15           C  
-ATOM   3565  NE  ARG B 153      26.471  40.783  61.788  1.00 44.08           N  
-ATOM   3566  CZ  ARG B 153      26.235  41.467  60.673  1.00 44.33           C  
-ATOM   3567  NH1 ARG B 153      25.922  40.832  59.548  1.00 43.40           N  
-ATOM   3568  NH2 ARG B 153      26.303  42.791  60.685  1.00 42.37           N  
-ATOM   3569  N   THR B 154      21.653  41.243  61.000  1.00 40.58           N  
-ATOM   3570  CA  THR B 154      20.773  42.062  60.174  1.00 40.84           C  
-ATOM   3571  C   THR B 154      21.585  42.852  59.153  1.00 39.95           C  
-ATOM   3572  O   THR B 154      22.636  43.406  59.479  1.00 40.55           O  
-ATOM   3573  CB  THR B 154      19.964  43.040  61.041  1.00 40.91           C  
-ATOM   3574  OG1 THR B 154      19.130  42.293  61.932  1.00 46.90           O  
-ATOM   3575  CG2 THR B 154      19.090  43.933  60.179  1.00 43.41           C  
-ATOM   3576  N   VAL B 155      21.088  42.910  57.921  1.00 37.92           N  
-ATOM   3577  CA  VAL B 155      21.782  43.617  56.852  1.00 36.15           C  
-ATOM   3578  C   VAL B 155      20.848  44.466  55.999  1.00 36.27           C  
-ATOM   3579  O   VAL B 155      19.742  44.045  55.671  1.00 38.98           O  
-ATOM   3580  CB  VAL B 155      22.506  42.616  55.910  1.00 34.82           C  
-ATOM   3581  CG1 VAL B 155      23.208  43.363  54.788  1.00 35.39           C  
-ATOM   3582  CG2 VAL B 155      23.503  41.784  56.697  1.00 33.51           C  
-ATOM   3583  N   LYS B 156      21.291  45.668  55.650  1.00 35.13           N  
-ATOM   3584  CA  LYS B 156      20.506  46.544  54.794  1.00 36.71           C  
-ATOM   3585  C   LYS B 156      21.146  46.443  53.413  1.00 36.54           C  
-ATOM   3586  O   LYS B 156      22.368  46.540  53.275  1.00 36.76           O  
-ATOM   3587  CB  LYS B 156      20.527  47.978  55.318  1.00 39.24           C  
-ATOM   3588  CG  LYS B 156      19.732  48.149  56.604  1.00 40.88           C  
-ATOM   3589  CD  LYS B 156      19.599  49.611  56.978  1.00 45.73           C  
-ATOM   3590  CE  LYS B 156      18.715  49.792  58.201  1.00 48.81           C  
-ATOM   3591  NZ  LYS B 156      18.546  51.236  58.545  1.00 51.77           N  
-ATOM   3592  N   TYR B 157      20.314  46.251  52.394  1.00 34.82           N  
-ATOM   3593  CA  TYR B 157      20.802  46.043  51.035  1.00 31.48           C  
-ATOM   3594  C   TYR B 157      20.398  47.101  50.013  1.00 29.86           C  
-ATOM   3595  O   TYR B 157      19.251  47.547  49.981  1.00 29.44           O  
-ATOM   3596  CB  TYR B 157      20.309  44.669  50.575  1.00 31.46           C  
-ATOM   3597  CG  TYR B 157      20.887  44.139  49.285  1.00 30.38           C  
-ATOM   3598  CD1 TYR B 157      21.930  43.212  49.300  1.00 26.88           C  
-ATOM   3599  CD2 TYR B 157      20.340  44.500  48.049  1.00 29.02           C  
-ATOM   3600  CE1 TYR B 157      22.408  42.648  48.120  1.00 28.05           C  
-ATOM   3601  CE2 TYR B 157      20.812  43.943  46.860  1.00 28.44           C  
-ATOM   3602  CZ  TYR B 157      21.844  43.017  46.903  1.00 29.87           C  
-ATOM   3603  OH  TYR B 157      22.305  42.453  45.734  1.00 30.22           O  
-ATOM   3604  N   TYR B 158      21.357  47.492  49.177  1.00 28.93           N  
-ATOM   3605  CA  TYR B 158      21.124  48.464  48.114  1.00 27.33           C  
-ATOM   3606  C   TYR B 158      21.455  47.842  46.755  1.00 27.36           C  
-ATOM   3607  O   TYR B 158      22.526  47.262  46.576  1.00 27.29           O  
-ATOM   3608  CB  TYR B 158      22.005  49.703  48.289  1.00 26.89           C  
-ATOM   3609  CG  TYR B 158      21.873  50.671  47.129  1.00 24.55           C  
-ATOM   3610  CD1 TYR B 158      20.801  51.560  47.057  1.00 24.06           C  
-ATOM   3611  CD2 TYR B 158      22.785  50.653  46.072  1.00 25.95           C  
-ATOM   3612  CE1 TYR B 158      20.632  52.406  45.962  1.00 21.94           C  
-ATOM   3613  CE2 TYR B 158      22.628  51.497  44.964  1.00 22.36           C  
-ATOM   3614  CZ  TYR B 158      21.548  52.368  44.919  1.00 24.50           C  
-ATOM   3615  OH  TYR B 158      21.376  53.198  43.831  1.00 23.79           O  
-ATOM   3616  N   GLN B 159      20.538  47.980  45.801  1.00 28.70           N  
-ATOM   3617  CA  GLN B 159      20.732  47.461  44.448  1.00 26.82           C  
-ATOM   3618  C   GLN B 159      20.865  48.635  43.485  1.00 27.41           C  
-ATOM   3619  O   GLN B 159      20.007  49.519  43.451  1.00 27.48           O  
-ATOM   3620  CB  GLN B 159      19.546  46.576  44.049  1.00 27.97           C  
-ATOM   3621  CG  GLN B 159      19.450  46.228  42.559  1.00 28.79           C  
-ATOM   3622  CD  GLN B 159      20.735  45.643  41.979  1.00 27.19           C  
-ATOM   3623  OE1 GLN B 159      21.451  44.888  42.641  1.00 24.42           O  
-ATOM   3624  NE2 GLN B 159      21.020  45.983  40.727  1.00 27.31           N  
-ATOM   3625  N   ALA B 160      21.950  48.651  42.715  1.00 27.07           N  
-ATOM   3626  CA  ALA B 160      22.190  49.726  41.759  1.00 27.44           C  
-ATOM   3627  C   ALA B 160      21.281  49.626  40.530  1.00 29.37           C  
-ATOM   3628  O   ALA B 160      21.663  49.061  39.502  1.00 29.00           O  
-ATOM   3629  CB  ALA B 160      23.654  49.724  41.327  1.00 26.40           C  
-ATOM   3630  N   GLY B 161      20.079  50.181  40.647  1.00 28.34           N  
-ATOM   3631  CA  GLY B 161      19.141  50.170  39.540  1.00 28.43           C  
-ATOM   3632  C   GLY B 161      19.506  51.232  38.519  1.00 27.62           C  
-ATOM   3633  O   GLY B 161      20.322  52.115  38.790  1.00 26.92           O  
-ATOM   3634  N   SER B 162      18.890  51.163  37.345  1.00 28.41           N  
-ATOM   3635  CA  SER B 162      19.199  52.109  36.284  1.00 29.63           C  
-ATOM   3636  C   SER B 162      17.999  52.600  35.485  1.00 29.84           C  
-ATOM   3637  O   SER B 162      17.042  51.862  35.248  1.00 28.83           O  
-ATOM   3638  CB  SER B 162      20.206  51.473  35.324  1.00 31.98           C  
-ATOM   3639  OG  SER B 162      20.376  52.258  34.157  1.00 34.96           O  
-ATOM   3640  N   SER B 163      18.074  53.853  35.053  1.00 30.06           N  
-ATOM   3641  CA  SER B 163      17.020  54.452  34.250  1.00 30.15           C  
-ATOM   3642  C   SER B 163      16.909  53.682  32.938  1.00 30.35           C  
-ATOM   3643  O   SER B 163      15.896  53.743  32.237  1.00 31.12           O  
-ATOM   3644  CB  SER B 163      17.351  55.918  33.964  1.00 30.04           C  
-ATOM   3645  OG  SER B 163      18.618  56.054  33.338  1.00 30.57           O  
-ATOM   3646  N   GLU B 164      17.968  52.948  32.622  1.00 29.98           N  
-ATOM   3647  CA  GLU B 164      18.031  52.152  31.407  1.00 30.39           C  
-ATOM   3648  C   GLU B 164      16.908  51.112  31.394  1.00 29.89           C  
-ATOM   3649  O   GLU B 164      16.514  50.631  30.337  1.00 29.34           O  
-ATOM   3650  CB  GLU B 164      19.398  51.468  31.328  1.00 32.20           C  
-ATOM   3651  CG  GLU B 164      19.906  51.177  29.925  1.00 35.58           C  
-ATOM   3652  CD  GLU B 164      20.156  52.430  29.102  1.00 37.19           C  
-ATOM   3653  OE1 GLU B 164      20.465  53.491  29.685  1.00 37.49           O  
-ATOM   3654  OE2 GLU B 164      20.060  52.343  27.859  1.00 37.15           O  
-ATOM   3655  N   MET B 165      16.388  50.779  32.572  1.00 29.76           N  
-ATOM   3656  CA  MET B 165      15.311  49.800  32.679  1.00 30.50           C  
-ATOM   3657  C   MET B 165      14.030  50.309  32.014  1.00 30.83           C  
-ATOM   3658  O   MET B 165      13.250  49.522  31.474  1.00 31.44           O  
-ATOM   3659  CB  MET B 165      15.033  49.457  34.154  1.00 29.08           C  
-ATOM   3660  CG  MET B 165      16.259  48.973  34.923  1.00 30.00           C  
-ATOM   3661  SD  MET B 165      15.890  48.363  36.582  1.00 33.29           S  
-ATOM   3662  CE  MET B 165      15.520  49.897  37.449  1.00 32.78           C  
-ATOM   3663  N   PHE B 166      13.813  51.622  32.053  1.00 29.36           N  
-ATOM   3664  CA  PHE B 166      12.619  52.206  31.443  1.00 28.04           C  
-ATOM   3665  C   PHE B 166      12.650  52.030  29.933  1.00 28.22           C  
-ATOM   3666  O   PHE B 166      11.607  51.961  29.284  1.00 28.59           O  
-ATOM   3667  CB  PHE B 166      12.510  53.692  31.794  1.00 26.15           C  
-ATOM   3668  CG  PHE B 166      12.315  53.948  33.258  1.00 27.47           C  
-ATOM   3669  CD1 PHE B 166      13.271  54.645  33.990  1.00 26.60           C  
-ATOM   3670  CD2 PHE B 166      11.199  53.445  33.916  1.00 27.84           C  
-ATOM   3671  CE1 PHE B 166      13.123  54.834  35.360  1.00 26.35           C  
-ATOM   3672  CE2 PHE B 166      11.038  53.627  35.288  1.00 28.75           C  
-ATOM   3673  CZ  PHE B 166      12.003  54.323  36.013  1.00 28.34           C  
-ATOM   3674  N   GLY B 167      13.857  51.966  29.383  1.00 29.02           N  
-ATOM   3675  CA  GLY B 167      14.023  51.778  27.954  1.00 29.83           C  
-ATOM   3676  C   GLY B 167      13.319  52.795  27.077  1.00 32.00           C  
-ATOM   3677  O   GLY B 167      13.589  53.992  27.154  1.00 32.28           O  
-ATOM   3678  N   SER B 168      12.414  52.311  26.232  1.00 31.84           N  
-ATOM   3679  CA  SER B 168      11.683  53.177  25.322  1.00 32.53           C  
-ATOM   3680  C   SER B 168      10.451  53.829  25.940  1.00 33.35           C  
-ATOM   3681  O   SER B 168       9.809  54.658  25.306  1.00 33.50           O  
-ATOM   3682  CB  SER B 168      11.282  52.396  24.071  1.00 30.80           C  
-ATOM   3683  OG  SER B 168      10.645  51.182  24.417  1.00 31.15           O  
-ATOM   3684  N   THR B 169      10.112  53.463  27.171  1.00 34.84           N  
-ATOM   3685  CA  THR B 169       8.951  54.070  27.804  1.00 34.94           C  
-ATOM   3686  C   THR B 169       9.187  55.574  27.827  1.00 35.64           C  
-ATOM   3687  O   THR B 169      10.246  56.034  28.251  1.00 34.82           O  
-ATOM   3688  CB  THR B 169       8.755  53.568  29.236  1.00 35.07           C  
-ATOM   3689  OG1 THR B 169       8.622  52.141  29.223  1.00 32.83           O  
-ATOM   3690  CG2 THR B 169       7.496  54.176  29.838  1.00 32.61           C  
-ATOM   3691  N   PRO B 170       8.200  56.361  27.366  1.00 35.78           N  
-ATOM   3692  CA  PRO B 170       8.301  57.823  27.325  1.00 35.37           C  
-ATOM   3693  C   PRO B 170       8.496  58.527  28.665  1.00 35.35           C  
-ATOM   3694  O   PRO B 170       7.949  58.114  29.686  1.00 36.91           O  
-ATOM   3695  CB  PRO B 170       6.999  58.236  26.635  1.00 35.45           C  
-ATOM   3696  CG  PRO B 170       6.048  57.175  27.060  1.00 35.49           C  
-ATOM   3697  CD  PRO B 170       6.872  55.919  26.902  1.00 35.03           C  
-ATOM   3698  N   PRO B 171       9.287  59.610  28.670  1.00 34.57           N  
-ATOM   3699  CA  PRO B 171       9.574  60.403  29.867  1.00 35.02           C  
-ATOM   3700  C   PRO B 171       8.406  61.343  30.181  1.00 36.15           C  
-ATOM   3701  O   PRO B 171       7.528  61.554  29.344  1.00 36.53           O  
-ATOM   3702  CB  PRO B 171      10.826  61.169  29.466  1.00 34.13           C  
-ATOM   3703  CG  PRO B 171      10.554  61.459  28.025  1.00 33.35           C  
-ATOM   3704  CD  PRO B 171      10.040  60.129  27.512  1.00 33.52           C  
-ATOM   3705  N   PRO B 172       8.376  61.907  31.398  1.00 35.92           N  
-ATOM   3706  CA  PRO B 172       9.379  61.678  32.443  1.00 35.51           C  
-ATOM   3707  C   PRO B 172       9.099  60.348  33.122  1.00 33.76           C  
-ATOM   3708  O   PRO B 172       7.941  59.953  33.251  1.00 35.48           O  
-ATOM   3709  CB  PRO B 172       9.173  62.863  33.378  1.00 34.06           C  
-ATOM   3710  CG  PRO B 172       7.691  63.078  33.297  1.00 35.12           C  
-ATOM   3711  CD  PRO B 172       7.421  62.954  31.807  1.00 35.96           C  
-ATOM   3712  N   GLN B 173      10.151  59.657  33.551  1.00 32.02           N  
-ATOM   3713  CA  GLN B 173       9.982  58.362  34.204  1.00 31.99           C  
-ATOM   3714  C   GLN B 173      10.151  58.413  35.719  1.00 31.75           C  
-ATOM   3715  O   GLN B 173      11.121  58.973  36.227  1.00 31.26           O  
-ATOM   3716  CB  GLN B 173      10.962  57.336  33.621  1.00 29.95           C  
-ATOM   3717  CG  GLN B 173      10.756  57.034  32.148  1.00 28.06           C  
-ATOM   3718  CD  GLN B 173      11.682  57.828  31.248  1.00 29.97           C  
-ATOM   3719  OE1 GLN B 173      12.421  58.701  31.705  1.00 29.36           O  
-ATOM   3720  NE2 GLN B 173      11.644  57.529  29.956  1.00 28.66           N  
-ATOM   3721  N   SER B 174       9.196  57.817  36.431  1.00 33.06           N  
-ATOM   3722  CA  SER B 174       9.220  57.765  37.889  1.00 32.76           C  
-ATOM   3723  C   SER B 174       9.213  56.306  38.352  1.00 32.60           C  
-ATOM   3724  O   SER B 174       9.287  55.390  37.533  1.00 31.01           O  
-ATOM   3725  CB  SER B 174       8.004  58.495  38.467  1.00 33.80           C  
-ATOM   3726  OG  SER B 174       6.803  57.824  38.127  1.00 36.40           O  
-ATOM   3727  N   GLU B 175       9.120  56.099  39.663  1.00 32.25           N  
-ATOM   3728  CA  GLU B 175       9.114  54.753  40.238  1.00 34.28           C  
-ATOM   3729  C   GLU B 175       7.986  53.864  39.715  1.00 35.32           C  
-ATOM   3730  O   GLU B 175       8.081  52.641  39.774  1.00 36.58           O  
-ATOM   3731  CB  GLU B 175       8.989  54.811  41.770  1.00 34.12           C  
-ATOM   3732  CG  GLU B 175      10.111  55.515  42.529  1.00 32.71           C  
-ATOM   3733  CD  GLU B 175      10.064  57.029  42.399  1.00 33.19           C  
-ATOM   3734  OE1 GLU B 175       9.006  57.568  42.015  1.00 36.22           O  
-ATOM   3735  OE2 GLU B 175      11.086  57.684  42.692  1.00 32.93           O  
-ATOM   3736  N   THR B 176       6.916  54.476  39.220  1.00 37.01           N  
-ATOM   3737  CA  THR B 176       5.770  53.721  38.733  1.00 37.94           C  
-ATOM   3738  C   THR B 176       5.736  53.585  37.218  1.00 38.26           C  
-ATOM   3739  O   THR B 176       4.797  53.019  36.660  1.00 40.14           O  
-ATOM   3740  CB  THR B 176       4.445  54.367  39.197  1.00 38.30           C  
-ATOM   3741  OG1 THR B 176       4.289  55.650  38.578  1.00 40.97           O  
-ATOM   3742  CG2 THR B 176       4.445  54.544  40.710  1.00 38.92           C  
-ATOM   3743  N   THR B 177       6.757  54.104  36.552  1.00 37.13           N  
-ATOM   3744  CA  THR B 177       6.819  54.021  35.103  1.00 35.11           C  
-ATOM   3745  C   THR B 177       7.197  52.600  34.684  1.00 34.91           C  
-ATOM   3746  O   THR B 177       8.168  52.032  35.182  1.00 32.70           O  
-ATOM   3747  CB  THR B 177       7.849  55.014  34.535  1.00 33.95           C  
-ATOM   3748  OG1 THR B 177       7.507  56.343  34.948  1.00 36.00           O  
-ATOM   3749  CG2 THR B 177       7.857  54.961  33.020  1.00 35.18           C  
-ATOM   3750  N   PRO B 178       6.427  52.008  33.757  1.00 34.38           N  
-ATOM   3751  CA  PRO B 178       6.702  50.647  33.288  1.00 33.92           C  
-ATOM   3752  C   PRO B 178       8.049  50.491  32.588  1.00 33.37           C  
-ATOM   3753  O   PRO B 178       8.566  51.432  31.989  1.00 32.94           O  
-ATOM   3754  CB  PRO B 178       5.524  50.360  32.360  1.00 34.27           C  
-ATOM   3755  CG  PRO B 178       5.182  51.709  31.822  1.00 33.75           C  
-ATOM   3756  CD  PRO B 178       5.269  52.584  33.049  1.00 34.09           C  
-ATOM   3757  N   PHE B 179       8.623  49.296  32.674  1.00 33.31           N  
-ATOM   3758  CA  PHE B 179       9.898  49.035  32.024  1.00 32.38           C  
-ATOM   3759  C   PHE B 179       9.672  48.524  30.606  1.00 31.48           C  
-ATOM   3760  O   PHE B 179       8.654  47.904  30.314  1.00 33.89           O  
-ATOM   3761  CB  PHE B 179      10.703  47.955  32.760  1.00 31.21           C  
-ATOM   3762  CG  PHE B 179      11.034  48.277  34.189  1.00 31.69           C  
-ATOM   3763  CD1 PHE B 179      11.210  49.588  34.612  1.00 30.61           C  
-ATOM   3764  CD2 PHE B 179      11.229  47.245  35.105  1.00 32.22           C  
-ATOM   3765  CE1 PHE B 179      11.578  49.864  35.920  1.00 31.00           C  
-ATOM   3766  CE2 PHE B 179      11.599  47.512  36.418  1.00 31.22           C  
-ATOM   3767  CZ  PHE B 179      11.775  48.821  36.829  1.00 31.27           C  
-ATOM   3768  N   HIS B 180      10.633  48.798  29.734  1.00 30.41           N  
-ATOM   3769  CA  HIS B 180      10.626  48.301  28.364  1.00 30.40           C  
-ATOM   3770  C   HIS B 180      12.086  48.363  27.949  1.00 29.81           C  
-ATOM   3771  O   HIS B 180      12.468  49.161  27.095  1.00 30.26           O  
-ATOM   3772  CB  HIS B 180       9.776  49.154  27.421  1.00 29.53           C  
-ATOM   3773  CG  HIS B 180       9.547  48.506  26.087  1.00 31.56           C  
-ATOM   3774  ND1 HIS B 180       8.290  48.187  25.616  1.00 31.82           N  
-ATOM   3775  CD2 HIS B 180      10.421  48.065  25.150  1.00 31.08           C  
-ATOM   3776  CE1 HIS B 180       8.400  47.575  24.450  1.00 31.77           C  
-ATOM   3777  NE2 HIS B 180       9.683  47.487  24.145  1.00 33.64           N  
-ATOM   3778  N   PRO B 181      12.926  47.511  28.564  1.00 28.95           N  
-ATOM   3779  CA  PRO B 181      14.364  47.456  28.282  1.00 26.57           C  
-ATOM   3780  C   PRO B 181      14.689  47.311  26.805  1.00 25.42           C  
-ATOM   3781  O   PRO B 181      14.027  46.574  26.079  1.00 23.55           O  
-ATOM   3782  CB  PRO B 181      14.838  46.272  29.128  1.00 25.45           C  
-ATOM   3783  CG  PRO B 181      13.624  45.391  29.188  1.00 26.29           C  
-ATOM   3784  CD  PRO B 181      12.518  46.381  29.420  1.00 25.88           C  
-ATOM   3785  N   ARG B 182      15.725  48.023  26.376  1.00 25.54           N  
-ATOM   3786  CA  ARG B 182      16.144  48.016  24.981  1.00 25.89           C  
-ATOM   3787  C   ARG B 182      17.507  47.370  24.724  1.00 25.68           C  
-ATOM   3788  O   ARG B 182      18.067  47.518  23.640  1.00 28.33           O  
-ATOM   3789  CB  ARG B 182      16.143  49.455  24.468  1.00 24.95           C  
-ATOM   3790  CG  ARG B 182      14.762  50.083  24.466  1.00 27.45           C  
-ATOM   3791  CD  ARG B 182      13.992  49.657  23.225  1.00 27.66           C  
-ATOM   3792  NE  ARG B 182      14.496  50.369  22.057  1.00 30.59           N  
-ATOM   3793  CZ  ARG B 182      14.106  50.153  20.805  1.00 31.01           C  
-ATOM   3794  NH1 ARG B 182      13.196  49.227  20.533  1.00 31.02           N  
-ATOM   3795  NH2 ARG B 182      14.619  50.886  19.828  1.00 32.17           N  
-ATOM   3796  N   SER B 183      18.039  46.661  25.717  1.00 25.42           N  
-ATOM   3797  CA  SER B 183      19.332  45.980  25.581  1.00 25.43           C  
-ATOM   3798  C   SER B 183      19.417  44.842  26.589  1.00 25.98           C  
-ATOM   3799  O   SER B 183      18.613  44.773  27.515  1.00 26.94           O  
-ATOM   3800  CB  SER B 183      20.495  46.945  25.833  1.00 27.40           C  
-ATOM   3801  OG  SER B 183      20.516  47.379  27.183  1.00 23.40           O  
-ATOM   3802  N   PRO B 184      20.389  43.929  26.417  1.00 25.50           N  
-ATOM   3803  CA  PRO B 184      20.524  42.814  27.361  1.00 24.91           C  
-ATOM   3804  C   PRO B 184      20.845  43.339  28.759  1.00 24.98           C  
-ATOM   3805  O   PRO B 184      20.371  42.801  29.758  1.00 26.74           O  
-ATOM   3806  CB  PRO B 184      21.661  41.990  26.759  1.00 26.47           C  
-ATOM   3807  CG  PRO B 184      21.505  42.245  25.280  1.00 26.56           C  
-ATOM   3808  CD  PRO B 184      21.270  43.737  25.251  1.00 24.17           C  
-ATOM   3809  N   TYR B 185      21.651  44.393  28.818  1.00 23.61           N  
-ATOM   3810  CA  TYR B 185      22.009  45.019  30.085  1.00 24.84           C  
-ATOM   3811  C   TYR B 185      20.753  45.505  30.807  1.00 24.13           C  
-ATOM   3812  O   TYR B 185      20.527  45.185  31.973  1.00 25.56           O  
-ATOM   3813  CB  TYR B 185      22.929  46.226  29.855  1.00 24.34           C  
-ATOM   3814  CG  TYR B 185      23.046  47.143  31.062  1.00 22.67           C  
-ATOM   3815  CD1 TYR B 185      23.908  46.841  32.114  1.00 24.68           C  
-ATOM   3816  CD2 TYR B 185      22.274  48.302  31.159  1.00 23.31           C  
-ATOM   3817  CE1 TYR B 185      24.002  47.673  33.236  1.00 23.00           C  
-ATOM   3818  CE2 TYR B 185      22.357  49.138  32.273  1.00 22.08           C  
-ATOM   3819  CZ  TYR B 185      23.222  48.818  33.306  1.00 24.63           C  
-ATOM   3820  OH  TYR B 185      23.306  49.634  34.411  1.00 25.26           O  
-ATOM   3821  N   ALA B 186      19.946  46.290  30.108  1.00 24.04           N  
-ATOM   3822  CA  ALA B 186      18.728  46.831  30.700  1.00 26.40           C  
-ATOM   3823  C   ALA B 186      17.789  45.715  31.158  1.00 25.00           C  
-ATOM   3824  O   ALA B 186      17.246  45.766  32.259  1.00 26.52           O  
-ATOM   3825  CB  ALA B 186      18.023  47.761  29.701  1.00 24.35           C  
-ATOM   3826  N   ALA B 187      17.608  44.700  30.323  1.00 23.88           N  
-ATOM   3827  CA  ALA B 187      16.736  43.593  30.693  1.00 22.73           C  
-ATOM   3828  C   ALA B 187      17.308  42.877  31.922  1.00 21.75           C  
-ATOM   3829  O   ALA B 187      16.565  42.364  32.749  1.00 20.89           O  
-ATOM   3830  CB  ALA B 187      16.600  42.626  29.536  1.00 20.84           C  
-ATOM   3831  N   SER B 188      18.630  42.849  32.040  1.00 22.54           N  
-ATOM   3832  CA  SER B 188      19.263  42.208  33.185  1.00 22.99           C  
-ATOM   3833  C   SER B 188      19.103  43.077  34.440  1.00 23.51           C  
-ATOM   3834  O   SER B 188      19.000  42.552  35.553  1.00 21.22           O  
-ATOM   3835  CB  SER B 188      20.746  41.944  32.898  1.00 25.85           C  
-ATOM   3836  OG  SER B 188      20.909  40.952  31.895  1.00 23.77           O  
-ATOM   3837  N   LYS B 189      19.075  44.400  34.266  1.00 23.62           N  
-ATOM   3838  CA  LYS B 189      18.893  45.287  35.413  1.00 24.94           C  
-ATOM   3839  C   LYS B 189      17.470  45.134  35.938  1.00 26.27           C  
-ATOM   3840  O   LYS B 189      17.251  45.136  37.148  1.00 26.61           O  
-ATOM   3841  CB  LYS B 189      19.157  46.751  35.044  1.00 24.56           C  
-ATOM   3842  CG  LYS B 189      20.621  47.163  35.106  1.00 24.88           C  
-ATOM   3843  CD  LYS B 189      21.208  46.948  36.507  1.00 26.36           C  
-ATOM   3844  CE  LYS B 189      22.569  47.623  36.640  1.00 24.11           C  
-ATOM   3845  NZ  LYS B 189      23.197  47.362  37.959  1.00 24.90           N  
-ATOM   3846  N   CYS B 190      16.508  44.995  35.025  1.00 25.35           N  
-ATOM   3847  CA  CYS B 190      15.112  44.811  35.419  1.00 24.93           C  
-ATOM   3848  C   CYS B 190      14.989  43.534  36.246  1.00 24.39           C  
-ATOM   3849  O   CYS B 190      14.266  43.495  37.241  1.00 24.26           O  
-ATOM   3850  CB  CYS B 190      14.195  44.712  34.189  1.00 22.83           C  
-ATOM   3851  SG  CYS B 190      14.032  46.241  33.233  1.00 25.20           S  
-ATOM   3852  N   ALA B 191      15.698  42.493  35.824  1.00 25.27           N  
-ATOM   3853  CA  ALA B 191      15.677  41.216  36.529  1.00 25.54           C  
-ATOM   3854  C   ALA B 191      16.259  41.405  37.925  1.00 26.32           C  
-ATOM   3855  O   ALA B 191      15.712  40.910  38.917  1.00 27.04           O  
-ATOM   3856  CB  ALA B 191      16.489  40.180  35.759  1.00 26.06           C  
-ATOM   3857  N   ALA B 192      17.376  42.119  37.996  1.00 25.01           N  
-ATOM   3858  CA  ALA B 192      18.017  42.378  39.276  1.00 26.26           C  
-ATOM   3859  C   ALA B 192      17.053  43.195  40.138  1.00 26.88           C  
-ATOM   3860  O   ALA B 192      16.960  42.986  41.345  1.00 26.61           O  
-ATOM   3861  CB  ALA B 192      19.319  43.131  39.067  1.00 23.78           C  
-ATOM   3862  N   HIS B 193      16.329  44.113  39.501  1.00 25.70           N  
-ATOM   3863  CA  HIS B 193      15.363  44.950  40.196  1.00 26.93           C  
-ATOM   3864  C   HIS B 193      14.278  44.081  40.811  1.00 26.66           C  
-ATOM   3865  O   HIS B 193      13.896  44.270  41.969  1.00 25.75           O  
-ATOM   3866  CB  HIS B 193      14.718  45.947  39.230  1.00 28.48           C  
-ATOM   3867  CG  HIS B 193      13.713  46.848  39.878  1.00 30.51           C  
-ATOM   3868  ND1 HIS B 193      14.061  48.027  40.503  1.00 30.29           N  
-ATOM   3869  CD2 HIS B 193      12.372  46.722  40.030  1.00 30.03           C  
-ATOM   3870  CE1 HIS B 193      12.978  48.588  41.011  1.00 29.57           C  
-ATOM   3871  NE2 HIS B 193      11.941  47.816  40.740  1.00 29.30           N  
-ATOM   3872  N   TRP B 194      13.782  43.122  40.035  1.00 26.85           N  
-ATOM   3873  CA  TRP B 194      12.735  42.236  40.524  1.00 27.86           C  
-ATOM   3874  C   TRP B 194      13.196  41.213  41.551  1.00 25.65           C  
-ATOM   3875  O   TRP B 194      12.429  40.840  42.427  1.00 26.42           O  
-ATOM   3876  CB  TRP B 194      12.037  41.554  39.351  1.00 29.92           C  
-ATOM   3877  CG  TRP B 194      11.132  42.504  38.650  1.00 33.43           C  
-ATOM   3878  CD1 TRP B 194      11.153  42.837  37.330  1.00 35.00           C  
-ATOM   3879  CD2 TRP B 194      10.102  43.300  39.252  1.00 35.19           C  
-ATOM   3880  NE1 TRP B 194      10.206  43.798  37.070  1.00 35.32           N  
-ATOM   3881  CE2 TRP B 194       9.547  44.101  38.233  1.00 36.16           C  
-ATOM   3882  CE3 TRP B 194       9.595  43.414  40.558  1.00 37.06           C  
-ATOM   3883  CZ2 TRP B 194       8.504  45.015  38.475  1.00 39.48           C  
-ATOM   3884  CZ3 TRP B 194       8.555  44.322  40.803  1.00 36.34           C  
-ATOM   3885  CH2 TRP B 194       8.024  45.110  39.763  1.00 38.54           C  
-ATOM   3886  N   TYR B 195      14.441  40.760  41.456  1.00 24.81           N  
-ATOM   3887  CA  TYR B 195      14.956  39.806  42.433  1.00 25.29           C  
-ATOM   3888  C   TYR B 195      15.028  40.519  43.786  1.00 27.07           C  
-ATOM   3889  O   TYR B 195      14.666  39.959  44.825  1.00 27.37           O  
-ATOM   3890  CB  TYR B 195      16.359  39.326  42.036  1.00 24.08           C  
-ATOM   3891  CG  TYR B 195      16.394  38.405  40.834  1.00 23.21           C  
-ATOM   3892  CD1 TYR B 195      17.449  38.457  39.928  1.00 23.15           C  
-ATOM   3893  CD2 TYR B 195      15.377  37.478  40.605  1.00 22.81           C  
-ATOM   3894  CE1 TYR B 195      17.492  37.612  38.822  1.00 21.89           C  
-ATOM   3895  CE2 TYR B 195      15.412  36.630  39.505  1.00 22.11           C  
-ATOM   3896  CZ  TYR B 195      16.473  36.704  38.617  1.00 21.44           C  
-ATOM   3897  OH  TYR B 195      16.518  35.870  37.526  1.00 22.74           O  
-ATOM   3898  N   THR B 196      15.496  41.765  43.748  1.00 27.45           N  
-ATOM   3899  CA  THR B 196      15.643  42.595  44.939  1.00 27.30           C  
-ATOM   3900  C   THR B 196      14.279  42.866  45.573  1.00 27.48           C  
-ATOM   3901  O   THR B 196      14.085  42.641  46.764  1.00 28.45           O  
-ATOM   3902  CB  THR B 196      16.329  43.940  44.585  1.00 27.04           C  
-ATOM   3903  OG1 THR B 196      17.581  43.681  43.933  1.00 26.33           O  
-ATOM   3904  CG2 THR B 196      16.582  44.761  45.833  1.00 27.34           C  
-ATOM   3905  N   VAL B 197      13.333  43.347  44.777  1.00 28.43           N  
-ATOM   3906  CA  VAL B 197      11.999  43.615  45.291  1.00 28.93           C  
-ATOM   3907  C   VAL B 197      11.421  42.351  45.921  1.00 30.14           C  
-ATOM   3908  O   VAL B 197      10.782  42.407  46.975  1.00 30.80           O  
-ATOM   3909  CB  VAL B 197      11.053  44.094  44.170  1.00 27.74           C  
-ATOM   3910  CG1 VAL B 197       9.613  44.075  44.653  1.00 29.03           C  
-ATOM   3911  CG2 VAL B 197      11.437  45.500  43.740  1.00 27.72           C  
-ATOM   3912  N   ASN B 198      11.665  41.211  45.277  1.00 29.12           N  
-ATOM   3913  CA  ASN B 198      11.158  39.927  45.755  1.00 28.19           C  
-ATOM   3914  C   ASN B 198      11.735  39.516  47.111  1.00 27.39           C  
-ATOM   3915  O   ASN B 198      11.014  39.003  47.968  1.00 26.43           O  
-ATOM   3916  CB  ASN B 198      11.451  38.830  44.726  1.00 27.48           C  
-ATOM   3917  CG  ASN B 198      10.773  37.512  45.062  1.00 27.84           C  
-ATOM   3918  OD1 ASN B 198      11.299  36.442  44.767  1.00 27.99           O  
-ATOM   3919  ND2 ASN B 198       9.592  37.585  45.667  1.00 28.47           N  
-ATOM   3920  N   TYR B 199      13.035  39.720  47.304  1.00 27.78           N  
-ATOM   3921  CA  TYR B 199      13.646  39.344  48.572  1.00 28.86           C  
-ATOM   3922  C   TYR B 199      13.163  40.252  49.699  1.00 29.35           C  
-ATOM   3923  O   TYR B 199      13.178  39.868  50.866  1.00 29.18           O  
-ATOM   3924  CB  TYR B 199      15.174  39.368  48.462  1.00 27.43           C  
-ATOM   3925  CG  TYR B 199      15.755  38.023  48.085  1.00 30.22           C  
-ATOM   3926  CD1 TYR B 199      15.310  37.346  46.948  1.00 29.62           C  
-ATOM   3927  CD2 TYR B 199      16.723  37.408  48.883  1.00 28.34           C  
-ATOM   3928  CE1 TYR B 199      15.810  36.090  46.617  1.00 31.19           C  
-ATOM   3929  CE2 TYR B 199      17.228  36.152  48.557  1.00 30.33           C  
-ATOM   3930  CZ  TYR B 199      16.766  35.498  47.424  1.00 30.46           C  
-ATOM   3931  OH  TYR B 199      17.244  34.248  47.096  1.00 31.67           O  
-ATOM   3932  N   ARG B 200      12.727  41.454  49.335  1.00 29.50           N  
-ATOM   3933  CA  ARG B 200      12.213  42.409  50.306  1.00 30.50           C  
-ATOM   3934  C   ARG B 200      10.809  41.982  50.723  1.00 31.32           C  
-ATOM   3935  O   ARG B 200      10.499  41.899  51.911  1.00 30.75           O  
-ATOM   3936  CB  ARG B 200      12.151  43.809  49.695  1.00 29.92           C  
-ATOM   3937  CG  ARG B 200      11.482  44.843  50.594  1.00 30.33           C  
-ATOM   3938  CD  ARG B 200      11.613  46.237  50.022  1.00 28.49           C  
-ATOM   3939  NE  ARG B 200      10.720  46.476  48.895  1.00 29.00           N  
-ATOM   3940  CZ  ARG B 200      11.046  47.194  47.823  1.00 29.04           C  
-ATOM   3941  NH1 ARG B 200      12.252  47.738  47.717  1.00 28.17           N  
-ATOM   3942  NH2 ARG B 200      10.155  47.397  46.867  1.00 29.99           N  
-ATOM   3943  N   GLU B 201       9.974  41.703  49.724  1.00 30.95           N  
-ATOM   3944  CA  GLU B 201       8.591  41.298  49.944  1.00 31.17           C  
-ATOM   3945  C   GLU B 201       8.444  39.887  50.501  1.00 31.70           C  
-ATOM   3946  O   GLU B 201       7.574  39.632  51.329  1.00 33.62           O  
-ATOM   3947  CB  GLU B 201       7.794  41.420  48.634  1.00 28.61           C  
-ATOM   3948  CG  GLU B 201       7.612  42.858  48.155  1.00 28.54           C  
-ATOM   3949  CD  GLU B 201       6.795  42.981  46.875  1.00 27.98           C  
-ATOM   3950  OE1 GLU B 201       6.554  44.122  46.436  1.00 30.10           O  
-ATOM   3951  OE2 GLU B 201       6.393  41.950  46.301  1.00 29.44           O  
-ATOM   3952  N   ALA B 202       9.300  38.975  50.059  1.00 31.21           N  
-ATOM   3953  CA  ALA B 202       9.216  37.590  50.505  1.00 29.62           C  
-ATOM   3954  C   ALA B 202       9.893  37.271  51.833  1.00 29.76           C  
-ATOM   3955  O   ALA B 202       9.402  36.436  52.588  1.00 26.73           O  
-ATOM   3956  CB  ALA B 202       9.770  36.668  49.422  1.00 29.72           C  
-ATOM   3957  N   TYR B 203      11.017  37.921  52.116  1.00 30.72           N  
-ATOM   3958  CA  TYR B 203      11.749  37.635  53.344  1.00 31.83           C  
-ATOM   3959  C   TYR B 203      11.861  38.790  54.328  1.00 31.95           C  
-ATOM   3960  O   TYR B 203      12.399  38.622  55.422  1.00 31.90           O  
-ATOM   3961  CB  TYR B 203      13.151  37.133  52.997  1.00 31.95           C  
-ATOM   3962  CG  TYR B 203      13.154  35.900  52.124  1.00 33.40           C  
-ATOM   3963  CD1 TYR B 203      13.696  35.932  50.835  1.00 32.89           C  
-ATOM   3964  CD2 TYR B 203      12.614  34.701  52.580  1.00 33.49           C  
-ATOM   3965  CE1 TYR B 203      13.696  34.797  50.029  1.00 32.82           C  
-ATOM   3966  CE2 TYR B 203      12.611  33.564  51.784  1.00 32.92           C  
-ATOM   3967  CZ  TYR B 203      13.153  33.619  50.511  1.00 33.57           C  
-ATOM   3968  OH  TYR B 203      13.147  32.492  49.724  1.00 35.77           O  
-ATOM   3969  N   GLY B 204      11.355  39.954  53.943  1.00 32.19           N  
-ATOM   3970  CA  GLY B 204      11.426  41.107  54.821  1.00 32.52           C  
-ATOM   3971  C   GLY B 204      12.807  41.736  54.837  1.00 33.24           C  
-ATOM   3972  O   GLY B 204      13.129  42.519  55.729  1.00 33.79           O  
-ATOM   3973  N   LEU B 205      13.631  41.393  53.853  1.00 31.82           N  
-ATOM   3974  CA  LEU B 205      14.975  41.951  53.773  1.00 31.84           C  
-ATOM   3975  C   LEU B 205      14.893  43.448  53.505  1.00 31.93           C  
-ATOM   3976  O   LEU B 205      14.121  43.893  52.652  1.00 32.57           O  
-ATOM   3977  CB  LEU B 205      15.770  41.286  52.645  1.00 32.29           C  
-ATOM   3978  CG  LEU B 205      17.209  41.788  52.474  1.00 32.86           C  
-ATOM   3979  CD1 LEU B 205      18.024  41.428  53.707  1.00 32.66           C  
-ATOM   3980  CD2 LEU B 205      17.837  41.173  51.227  1.00 32.50           C  
-ATOM   3981  N   PHE B 206      15.676  44.229  54.242  1.00 31.17           N  
-ATOM   3982  CA  PHE B 206      15.680  45.669  54.038  1.00 31.05           C  
-ATOM   3983  C   PHE B 206      16.497  45.907  52.772  1.00 31.01           C  
-ATOM   3984  O   PHE B 206      17.703  46.158  52.826  1.00 30.79           O  
-ATOM   3985  CB  PHE B 206      16.312  46.393  55.236  1.00 30.82           C  
-ATOM   3986  CG  PHE B 206      16.136  47.888  55.200  1.00 32.17           C  
-ATOM   3987  CD1 PHE B 206      16.735  48.653  54.200  1.00 31.47           C  
-ATOM   3988  CD2 PHE B 206      15.350  48.532  56.152  1.00 31.76           C  
-ATOM   3989  CE1 PHE B 206      16.554  50.035  54.148  1.00 31.28           C  
-ATOM   3990  CE2 PHE B 206      15.161  49.918  56.109  1.00 30.00           C  
-ATOM   3991  CZ  PHE B 206      15.763  50.668  55.107  1.00 31.37           C  
-ATOM   3992  N   ALA B 207      15.827  45.807  51.630  1.00 31.70           N  
-ATOM   3993  CA  ALA B 207      16.479  45.985  50.344  1.00 30.88           C  
-ATOM   3994  C   ALA B 207      15.834  47.111  49.561  1.00 30.80           C  
-ATOM   3995  O   ALA B 207      14.613  47.156  49.406  1.00 32.54           O  
-ATOM   3996  CB  ALA B 207      16.415  44.680  49.545  1.00 29.45           C  
-ATOM   3997  N   CYS B 208      16.664  48.021  49.063  1.00 29.86           N  
-ATOM   3998  CA  CYS B 208      16.174  49.148  48.290  1.00 29.97           C  
-ATOM   3999  C   CYS B 208      16.728  49.111  46.882  1.00 29.50           C  
-ATOM   4000  O   CYS B 208      17.832  48.622  46.645  1.00 29.22           O  
-ATOM   4001  CB  CYS B 208      16.594  50.475  48.933  1.00 32.17           C  
-ATOM   4002  SG  CYS B 208      16.040  50.725  50.638  1.00 36.88           S  
-ATOM   4003  N   ASN B 209      15.948  49.629  45.945  1.00 28.82           N  
-ATOM   4004  CA  ASN B 209      16.382  49.709  44.563  1.00 28.41           C  
-ATOM   4005  C   ASN B 209      16.575  51.181  44.256  1.00 28.46           C  
-ATOM   4006  O   ASN B 209      15.635  51.974  44.349  1.00 28.60           O  
-ATOM   4007  CB  ASN B 209      15.334  49.129  43.610  1.00 27.80           C  
-ATOM   4008  CG  ASN B 209      15.381  47.617  43.540  1.00 28.97           C  
-ATOM   4009  OD1 ASN B 209      16.360  47.035  43.063  1.00 29.70           O  
-ATOM   4010  ND2 ASN B 209      14.323  46.972  44.014  1.00 26.75           N  
-ATOM   4011  N   GLY B 210      17.802  51.551  43.923  1.00 28.04           N  
-ATOM   4012  CA  GLY B 210      18.067  52.926  43.571  1.00 27.71           C  
-ATOM   4013  C   GLY B 210      17.945  52.989  42.066  1.00 27.79           C  
-ATOM   4014  O   GLY B 210      18.776  52.426  41.362  1.00 29.74           O  
-ATOM   4015  N   ILE B 211      16.904  53.639  41.562  1.00 28.08           N  
-ATOM   4016  CA  ILE B 211      16.717  53.751  40.118  1.00 28.43           C  
-ATOM   4017  C   ILE B 211      17.396  55.033  39.671  1.00 27.63           C  
-ATOM   4018  O   ILE B 211      16.743  56.055  39.458  1.00 28.90           O  
-ATOM   4019  CB  ILE B 211      15.226  53.815  39.745  1.00 29.40           C  
-ATOM   4020  CG1 ILE B 211      14.471  52.682  40.440  1.00 28.80           C  
-ATOM   4021  CG2 ILE B 211      15.065  53.698  38.234  1.00 26.27           C  
-ATOM   4022  CD1 ILE B 211      12.975  52.699  40.195  1.00 31.07           C  
-ATOM   4023  N   LEU B 212      18.714  54.972  39.533  1.00 27.21           N  
-ATOM   4024  CA  LEU B 212      19.485  56.141  39.147  1.00 27.31           C  
-ATOM   4025  C   LEU B 212      19.588  56.362  37.657  1.00 27.76           C  
-ATOM   4026  O   LEU B 212      19.704  55.421  36.879  1.00 28.84           O  
-ATOM   4027  CB  LEU B 212      20.895  56.069  39.741  1.00 27.81           C  
-ATOM   4028  CG  LEU B 212      21.036  56.428  41.224  1.00 27.90           C  
-ATOM   4029  CD1 LEU B 212      20.138  55.536  42.083  1.00 24.85           C  
-ATOM   4030  CD2 LEU B 212      22.492  56.277  41.631  1.00 25.45           C  
-ATOM   4031  N   PHE B 213      19.524  57.627  37.268  1.00 28.18           N  
-ATOM   4032  CA  PHE B 213      19.646  57.998  35.871  1.00 28.39           C  
-ATOM   4033  C   PHE B 213      21.122  58.295  35.663  1.00 26.24           C  
-ATOM   4034  O   PHE B 213      21.885  58.364  36.626  1.00 28.64           O  
-ATOM   4035  CB  PHE B 213      18.776  59.223  35.560  1.00 26.97           C  
-ATOM   4036  CG  PHE B 213      17.309  58.904  35.436  1.00 28.04           C  
-ATOM   4037  CD1 PHE B 213      16.619  58.324  36.492  1.00 28.22           C  
-ATOM   4038  CD2 PHE B 213      16.633  59.132  34.246  1.00 27.85           C  
-ATOM   4039  CE1 PHE B 213      15.279  57.973  36.362  1.00 29.81           C  
-ATOM   4040  CE2 PHE B 213      15.295  58.783  34.104  1.00 28.33           C  
-ATOM   4041  CZ  PHE B 213      14.616  58.201  35.164  1.00 28.32           C  
-ATOM   4042  N   ASN B 214      21.525  58.449  34.411  1.00 27.16           N  
-ATOM   4043  CA  ASN B 214      22.919  58.711  34.087  1.00 27.97           C  
-ATOM   4044  C   ASN B 214      23.584  59.716  35.024  1.00 27.72           C  
-ATOM   4045  O   ASN B 214      23.074  60.809  35.242  1.00 26.26           O  
-ATOM   4046  CB  ASN B 214      23.041  59.233  32.650  1.00 29.99           C  
-ATOM   4047  CG  ASN B 214      22.634  58.205  31.609  1.00 31.54           C  
-ATOM   4048  OD1 ASN B 214      21.540  57.648  31.659  1.00 32.48           O  
-ATOM   4049  ND2 ASN B 214      23.514  57.964  30.647  1.00 32.85           N  
-ATOM   4050  N   HIS B 215      24.711  59.326  35.603  1.00 28.21           N  
-ATOM   4051  CA  HIS B 215      25.465  60.240  36.440  1.00 27.90           C  
-ATOM   4052  C   HIS B 215      26.923  60.132  36.024  1.00 28.16           C  
-ATOM   4053  O   HIS B 215      27.465  59.033  35.886  1.00 26.66           O  
-ATOM   4054  CB  HIS B 215      25.283  59.962  37.940  1.00 27.46           C  
-ATOM   4055  CG  HIS B 215      25.260  58.515  38.308  1.00 27.40           C  
-ATOM   4056  ND1 HIS B 215      24.144  57.723  38.144  1.00 27.49           N  
-ATOM   4057  CD2 HIS B 215      26.192  57.734  38.901  1.00 27.36           C  
-ATOM   4058  CE1 HIS B 215      24.389  56.519  38.628  1.00 26.82           C  
-ATOM   4059  NE2 HIS B 215      25.624  56.499  39.092  1.00 27.87           N  
-ATOM   4060  N   GLU B 216      27.539  61.290  35.799  1.00 29.69           N  
-ATOM   4061  CA  GLU B 216      28.923  61.366  35.350  1.00 30.27           C  
-ATOM   4062  C   GLU B 216      29.842  62.021  36.372  1.00 29.21           C  
-ATOM   4063  O   GLU B 216      29.405  62.482  37.423  1.00 30.24           O  
-ATOM   4064  CB  GLU B 216      29.000  62.160  34.042  1.00 31.62           C  
-ATOM   4065  CG  GLU B 216      27.769  62.034  33.152  1.00 32.21           C  
-ATOM   4066  CD  GLU B 216      27.485  60.606  32.736  1.00 33.18           C  
-ATOM   4067  OE1 GLU B 216      26.514  60.013  33.253  1.00 34.65           O  
-ATOM   4068  OE2 GLU B 216      28.235  60.073  31.894  1.00 33.94           O  
-ATOM   4069  N   SER B 217      31.124  62.067  36.033  1.00 30.71           N  
-ATOM   4070  CA  SER B 217      32.142  62.651  36.890  1.00 29.98           C  
-ATOM   4071  C   SER B 217      33.487  62.573  36.168  1.00 30.89           C  
-ATOM   4072  O   SER B 217      33.583  62.030  35.070  1.00 31.01           O  
-ATOM   4073  CB  SER B 217      32.228  61.875  38.203  1.00 29.06           C  
-ATOM   4074  OG  SER B 217      32.816  60.604  37.994  1.00 29.33           O  
-ATOM   4075  N   PRO B 218      34.541  63.144  36.765  1.00 32.62           N  
-ATOM   4076  CA  PRO B 218      35.852  63.085  36.112  1.00 32.13           C  
-ATOM   4077  C   PRO B 218      36.421  61.667  36.155  1.00 31.51           C  
-ATOM   4078  O   PRO B 218      37.457  61.390  35.562  1.00 32.94           O  
-ATOM   4079  CB  PRO B 218      36.687  64.065  36.932  1.00 33.42           C  
-ATOM   4080  CG  PRO B 218      35.662  65.076  37.387  1.00 32.80           C  
-ATOM   4081  CD  PRO B 218      34.520  64.184  37.810  1.00 32.58           C  
-ATOM   4082  N   ARG B 219      35.727  60.774  36.854  1.00 31.57           N  
-ATOM   4083  CA  ARG B 219      36.151  59.380  36.993  1.00 31.20           C  
-ATOM   4084  C   ARG B 219      35.298  58.439  36.149  1.00 31.82           C  
-ATOM   4085  O   ARG B 219      35.437  57.220  36.233  1.00 33.51           O  
-ATOM   4086  CB  ARG B 219      36.047  58.941  38.450  1.00 29.89           C  
-ATOM   4087  CG  ARG B 219      36.742  59.853  39.428  1.00 29.41           C  
-ATOM   4088  CD  ARG B 219      36.509  59.374  40.842  1.00 31.77           C  
-ATOM   4089  NE  ARG B 219      36.985  60.335  41.830  1.00 30.14           N  
-ATOM   4090  CZ  ARG B 219      36.796  60.210  43.137  1.00 30.66           C  
-ATOM   4091  NH1 ARG B 219      37.266  61.132  43.960  1.00 32.06           N  
-ATOM   4092  NH2 ARG B 219      36.129  59.169  43.621  1.00 26.55           N  
-ATOM   4093  N   ARG B 220      34.411  59.008  35.346  1.00 30.90           N  
-ATOM   4094  CA  ARG B 220      33.532  58.221  34.494  1.00 30.75           C  
-ATOM   4095  C   ARG B 220      34.338  57.385  33.503  1.00 29.64           C  
-ATOM   4096  O   ARG B 220      35.375  57.825  33.013  1.00 30.47           O  
-ATOM   4097  CB  ARG B 220      32.592  59.164  33.742  1.00 30.67           C  
-ATOM   4098  CG  ARG B 220      31.592  58.492  32.839  1.00 30.60           C  
-ATOM   4099  CD  ARG B 220      30.575  57.701  33.630  1.00 30.63           C  
-ATOM   4100  NE  ARG B 220      29.285  57.655  32.943  1.00 29.39           N  
-ATOM   4101  CZ  ARG B 220      28.448  56.624  32.995  1.00 28.86           C  
-ATOM   4102  NH1 ARG B 220      28.771  55.547  33.695  1.00 28.35           N  
-ATOM   4103  NH2 ARG B 220      27.282  56.679  32.366  1.00 28.30           N  
-ATOM   4104  N   GLY B 221      33.865  56.175  33.219  1.00 29.76           N  
-ATOM   4105  CA  GLY B 221      34.557  55.322  32.270  1.00 29.41           C  
-ATOM   4106  C   GLY B 221      34.715  56.036  30.940  1.00 29.47           C  
-ATOM   4107  O   GLY B 221      33.770  56.633  30.432  1.00 30.17           O  
-ATOM   4108  N   GLU B 222      35.908  55.965  30.365  1.00 31.30           N  
-ATOM   4109  CA  GLU B 222      36.185  56.639  29.107  1.00 32.58           C  
-ATOM   4110  C   GLU B 222      35.398  56.160  27.899  1.00 32.52           C  
-ATOM   4111  O   GLU B 222      35.394  56.822  26.866  1.00 31.96           O  
-ATOM   4112  CB  GLU B 222      37.680  56.566  28.795  1.00 34.60           C  
-ATOM   4113  CG  GLU B 222      38.512  57.543  29.598  1.00 38.43           C  
-ATOM   4114  CD  GLU B 222      39.962  57.577  29.161  1.00 39.16           C  
-ATOM   4115  OE1 GLU B 222      40.217  57.622  27.937  1.00 41.81           O  
-ATOM   4116  OE2 GLU B 222      40.842  57.570  30.044  1.00 40.38           O  
-ATOM   4117  N   ASN B 223      34.729  55.021  28.020  1.00 34.41           N  
-ATOM   4118  CA  ASN B 223      33.956  54.482  26.904  1.00 34.18           C  
-ATOM   4119  C   ASN B 223      32.511  54.975  26.895  1.00 33.30           C  
-ATOM   4120  O   ASN B 223      31.743  54.655  25.990  1.00 34.34           O  
-ATOM   4121  CB  ASN B 223      34.014  52.952  26.924  1.00 36.45           C  
-ATOM   4122  CG  ASN B 223      35.423  52.426  26.691  1.00 39.85           C  
-ATOM   4123  OD1 ASN B 223      35.834  51.422  27.277  1.00 43.44           O  
-ATOM   4124  ND2 ASN B 223      36.170  53.102  25.825  1.00 40.39           N  
-ATOM   4125  N   PHE B 224      32.141  55.749  27.910  1.00 33.43           N  
-ATOM   4126  CA  PHE B 224      30.800  56.321  27.974  1.00 32.30           C  
-ATOM   4127  C   PHE B 224      30.902  57.678  27.281  1.00 31.50           C  
-ATOM   4128  O   PHE B 224      31.923  58.355  27.390  1.00 33.26           O  
-ATOM   4129  CB  PHE B 224      30.342  56.469  29.428  1.00 31.11           C  
-ATOM   4130  CG  PHE B 224      30.173  55.152  30.140  1.00 31.37           C  
-ATOM   4131  CD1 PHE B 224      31.188  54.643  30.948  1.00 30.97           C  
-ATOM   4132  CD2 PHE B 224      29.015  54.395  29.963  1.00 31.08           C  
-ATOM   4133  CE1 PHE B 224      31.054  53.400  31.566  1.00 29.82           C  
-ATOM   4134  CE2 PHE B 224      28.871  53.148  30.577  1.00 29.19           C  
-ATOM   4135  CZ  PHE B 224      29.893  52.652  31.379  1.00 29.47           C  
-ATOM   4136  N   VAL B 225      29.849  58.064  26.568  1.00 32.35           N  
-ATOM   4137  CA  VAL B 225      29.823  59.306  25.794  1.00 31.00           C  
-ATOM   4138  C   VAL B 225      30.321  60.595  26.457  1.00 31.45           C  
-ATOM   4139  O   VAL B 225      31.099  61.333  25.856  1.00 33.36           O  
-ATOM   4140  CB  VAL B 225      28.404  59.557  25.211  1.00 30.94           C  
-ATOM   4141  CG1 VAL B 225      27.514  60.239  26.243  1.00 29.77           C  
-ATOM   4142  CG2 VAL B 225      28.500  60.380  23.938  1.00 28.58           C  
-ATOM   4143  N   THR B 226      29.891  60.879  27.682  1.00 32.67           N  
-ATOM   4144  CA  THR B 226      30.320  62.109  28.338  1.00 31.72           C  
-ATOM   4145  C   THR B 226      31.825  62.157  28.565  1.00 33.05           C  
-ATOM   4146  O   THR B 226      32.474  63.155  28.244  1.00 35.03           O  
-ATOM   4147  CB  THR B 226      29.627  62.309  29.697  1.00 30.41           C  
-ATOM   4148  OG1 THR B 226      30.017  61.259  30.589  1.00 30.59           O  
-ATOM   4149  CG2 THR B 226      28.116  62.315  29.529  1.00 30.38           C  
-ATOM   4150  N   ARG B 227      32.377  61.082  29.118  1.00 32.59           N  
-ATOM   4151  CA  ARG B 227      33.807  61.030  29.389  1.00 32.34           C  
-ATOM   4152  C   ARG B 227      34.580  60.958  28.082  1.00 32.34           C  
-ATOM   4153  O   ARG B 227      35.612  61.605  27.921  1.00 32.71           O  
-ATOM   4154  CB  ARG B 227      34.145  59.813  30.252  1.00 31.97           C  
-ATOM   4155  CG  ARG B 227      35.574  59.813  30.751  1.00 31.18           C  
-ATOM   4156  CD  ARG B 227      35.790  60.947  31.732  1.00 29.82           C  
-ATOM   4157  NE  ARG B 227      37.203  61.229  31.958  1.00 32.11           N  
-ATOM   4158  CZ  ARG B 227      38.065  60.386  32.516  1.00 30.67           C  
-ATOM   4159  NH1 ARG B 227      37.662  59.190  32.920  1.00 31.79           N  
-ATOM   4160  NH2 ARG B 227      39.335  60.738  32.655  1.00 29.95           N  
-ATOM   4161  N   LYS B 228      34.076  60.166  27.146  1.00 31.97           N  
-ATOM   4162  CA  LYS B 228      34.726  60.029  25.858  1.00 32.38           C  
-ATOM   4163  C   LYS B 228      34.885  61.397  25.204  1.00 34.26           C  
-ATOM   4164  O   LYS B 228      35.895  61.672  24.558  1.00 35.12           O  
-ATOM   4165  CB  LYS B 228      33.905  59.122  24.946  1.00 31.60           C  
-ATOM   4166  CG  LYS B 228      34.520  58.931  23.576  1.00 30.78           C  
-ATOM   4167  CD  LYS B 228      33.669  58.018  22.713  1.00 31.86           C  
-ATOM   4168  CE  LYS B 228      34.282  57.834  21.340  1.00 31.43           C  
-ATOM   4169  NZ  LYS B 228      33.410  57.000  20.465  1.00 36.45           N  
-ATOM   4170  N   ILE B 229      33.886  62.256  25.381  1.00 35.02           N  
-ATOM   4171  CA  ILE B 229      33.925  63.587  24.794  1.00 34.18           C  
-ATOM   4172  C   ILE B 229      34.908  64.525  25.485  1.00 33.87           C  
-ATOM   4173  O   ILE B 229      35.786  65.084  24.832  1.00 33.67           O  
-ATOM   4174  CB  ILE B 229      32.521  64.225  24.789  1.00 34.82           C  
-ATOM   4175  CG1 ILE B 229      31.618  63.456  23.819  1.00 36.06           C  
-ATOM   4176  CG2 ILE B 229      32.605  65.690  24.382  1.00 33.52           C  
-ATOM   4177  CD1 ILE B 229      30.189  63.948  23.775  1.00 36.41           C  
-ATOM   4178  N   THR B 230      34.775  64.690  26.799  1.00 33.83           N  
-ATOM   4179  CA  THR B 230      35.660  65.591  27.533  1.00 33.49           C  
-ATOM   4180  C   THR B 230      37.116  65.141  27.485  1.00 34.54           C  
-ATOM   4181  O   THR B 230      38.030  65.969  27.541  1.00 35.39           O  
-ATOM   4182  CB  THR B 230      35.233  65.740  29.013  1.00 33.56           C  
-ATOM   4183  OG1 THR B 230      35.254  64.459  29.650  1.00 33.94           O  
-ATOM   4184  CG2 THR B 230      33.828  66.338  29.111  1.00 29.46           C  
-ATOM   4185  N   ARG B 231      37.334  63.834  27.385  1.00 33.32           N  
-ATOM   4186  CA  ARG B 231      38.687  63.301  27.315  1.00 34.61           C  
-ATOM   4187  C   ARG B 231      39.282  63.691  25.966  1.00 34.51           C  
-ATOM   4188  O   ARG B 231      40.411  64.181  25.889  1.00 32.50           O  
-ATOM   4189  CB  ARG B 231      38.672  61.776  27.440  1.00 37.46           C  
-ATOM   4190  CG  ARG B 231      40.050  61.150  27.623  1.00 39.03           C  
-ATOM   4191  CD  ARG B 231      40.582  61.381  29.031  1.00 41.00           C  
-ATOM   4192  NE  ARG B 231      41.757  60.554  29.296  1.00 44.54           N  
-ATOM   4193  CZ  ARG B 231      43.004  60.887  28.977  1.00 45.90           C  
-ATOM   4194  NH1 ARG B 231      43.260  62.045  28.382  1.00 46.40           N  
-ATOM   4195  NH2 ARG B 231      43.999  60.052  29.244  1.00 46.57           N  
-ATOM   4196  N   ALA B 232      38.506  63.472  24.907  1.00 34.79           N  
-ATOM   4197  CA  ALA B 232      38.938  63.799  23.554  1.00 36.27           C  
-ATOM   4198  C   ALA B 232      39.096  65.309  23.406  1.00 37.30           C  
-ATOM   4199  O   ALA B 232      40.048  65.780  22.786  1.00 39.32           O  
-ATOM   4200  CB  ALA B 232      37.931  63.273  22.540  1.00 34.70           C  
-ATOM   4201  N   LEU B 233      38.162  66.065  23.979  1.00 37.89           N  
-ATOM   4202  CA  LEU B 233      38.214  67.522  23.908  1.00 39.63           C  
-ATOM   4203  C   LEU B 233      39.524  68.026  24.496  1.00 39.86           C  
-ATOM   4204  O   LEU B 233      40.241  68.795  23.858  1.00 40.17           O  
-ATOM   4205  CB  LEU B 233      37.044  68.150  24.676  1.00 39.57           C  
-ATOM   4206  CG  LEU B 233      37.096  69.676  24.844  1.00 39.38           C  
-ATOM   4207  CD1 LEU B 233      37.067  70.345  23.481  1.00 38.13           C  
-ATOM   4208  CD2 LEU B 233      35.928  70.146  25.693  1.00 37.97           C  
-ATOM   4209  N   GLY B 234      39.820  67.584  25.716  1.00 40.34           N  
-ATOM   4210  CA  GLY B 234      41.040  67.985  26.389  1.00 40.01           C  
-ATOM   4211  C   GLY B 234      42.280  67.735  25.555  1.00 40.96           C  
-ATOM   4212  O   GLY B 234      43.185  68.566  25.532  1.00 40.96           O  
-ATOM   4213  N   ARG B 235      42.328  66.592  24.877  1.00 41.27           N  
-ATOM   4214  CA  ARG B 235      43.470  66.256  24.031  1.00 42.63           C  
-ATOM   4215  C   ARG B 235      43.545  67.192  22.831  1.00 42.29           C  
-ATOM   4216  O   ARG B 235      44.625  67.616  22.419  1.00 42.04           O  
-ATOM   4217  CB  ARG B 235      43.368  64.818  23.522  1.00 43.57           C  
-ATOM   4218  CG  ARG B 235      43.743  63.756  24.523  1.00 46.71           C  
-ATOM   4219  CD  ARG B 235      44.036  62.451  23.799  1.00 51.18           C  
-ATOM   4220  NE  ARG B 235      44.463  61.406  24.719  1.00 54.34           N  
-ATOM   4221  CZ  ARG B 235      43.708  60.938  25.706  1.00 55.63           C  
-ATOM   4222  NH1 ARG B 235      42.490  61.428  25.893  1.00 57.18           N  
-ATOM   4223  NH2 ARG B 235      44.168  59.983  26.505  1.00 55.99           N  
-ATOM   4224  N   ILE B 236      42.385  67.495  22.265  1.00 42.56           N  
-ATOM   4225  CA  ILE B 236      42.303  68.380  21.114  1.00 42.47           C  
-ATOM   4226  C   ILE B 236      42.788  69.780  21.479  1.00 41.96           C  
-ATOM   4227  O   ILE B 236      43.514  70.414  20.718  1.00 43.03           O  
-ATOM   4228  CB  ILE B 236      40.854  68.451  20.598  1.00 42.75           C  
-ATOM   4229  CG1 ILE B 236      40.457  67.090  20.018  1.00 41.66           C  
-ATOM   4230  CG2 ILE B 236      40.713  69.554  19.565  1.00 43.91           C  
-ATOM   4231  CD1 ILE B 236      39.004  66.970  19.662  1.00 42.22           C  
-ATOM   4232  N   LYS B 237      42.394  70.251  22.655  1.00 41.65           N  
-ATOM   4233  CA  LYS B 237      42.779  71.577  23.113  1.00 41.22           C  
-ATOM   4234  C   LYS B 237      44.294  71.717  23.227  1.00 43.04           C  
-ATOM   4235  O   LYS B 237      44.835  72.812  23.055  1.00 45.00           O  
-ATOM   4236  CB  LYS B 237      42.127  71.870  24.466  1.00 39.60           C  
-ATOM   4237  CG  LYS B 237      42.360  73.276  24.995  1.00 39.52           C  
-ATOM   4238  CD  LYS B 237      41.730  74.332  24.090  1.00 40.28           C  
-ATOM   4239  CE  LYS B 237      41.857  75.730  24.698  1.00 41.42           C  
-ATOM   4240  NZ  LYS B 237      41.284  76.797  23.821  1.00 43.38           N  
-ATOM   4241  N   VAL B 238      44.979  70.612  23.510  1.00 42.11           N  
-ATOM   4242  CA  VAL B 238      46.430  70.646  23.651  1.00 42.17           C  
-ATOM   4243  C   VAL B 238      47.157  70.090  22.429  1.00 42.39           C  
-ATOM   4244  O   VAL B 238      48.375  69.914  22.449  1.00 44.23           O  
-ATOM   4245  CB  VAL B 238      46.885  69.872  24.907  1.00 41.72           C  
-ATOM   4246  CG1 VAL B 238      46.187  70.431  26.137  1.00 40.22           C  
-ATOM   4247  CG2 VAL B 238      46.588  68.391  24.747  1.00 43.55           C  
-ATOM   4248  N   GLY B 239      46.406  69.804  21.371  1.00 41.78           N  
-ATOM   4249  CA  GLY B 239      47.011  69.303  20.149  1.00 41.40           C  
-ATOM   4250  C   GLY B 239      47.473  67.858  20.122  1.00 41.96           C  
-ATOM   4251  O   GLY B 239      48.348  67.509  19.331  1.00 43.19           O  
-ATOM   4252  N   LEU B 240      46.898  67.009  20.967  1.00 41.62           N  
-ATOM   4253  CA  LEU B 240      47.288  65.601  20.987  1.00 40.77           C  
-ATOM   4254  C   LEU B 240      46.327  64.734  20.178  1.00 41.11           C  
-ATOM   4255  O   LEU B 240      46.626  63.586  19.865  1.00 41.07           O  
-ATOM   4256  CB  LEU B 240      47.365  65.098  22.428  1.00 38.25           C  
-ATOM   4257  CG  LEU B 240      48.453  65.790  23.253  1.00 39.33           C  
-ATOM   4258  CD1 LEU B 240      48.395  65.327  24.702  1.00 35.84           C  
-ATOM   4259  CD2 LEU B 240      49.814  65.494  22.637  1.00 36.44           C  
-ATOM   4260  N   GLN B 241      45.175  65.298  19.833  1.00 42.76           N  
-ATOM   4261  CA  GLN B 241      44.165  64.586  19.056  1.00 42.88           C  
-ATOM   4262  C   GLN B 241      43.504  65.607  18.134  1.00 42.90           C  
-ATOM   4263  O   GLN B 241      43.517  66.801  18.426  1.00 45.09           O  
-ATOM   4264  CB  GLN B 241      43.128  63.975  19.999  1.00 43.32           C  
-ATOM   4265  CG  GLN B 241      42.271  62.876  19.392  1.00 44.45           C  
-ATOM   4266  CD  GLN B 241      41.313  62.281  20.406  1.00 44.98           C  
-ATOM   4267  OE1 GLN B 241      41.701  61.976  21.536  1.00 43.72           O  
-ATOM   4268  NE2 GLN B 241      40.057  62.106  20.007  1.00 46.53           N  
-ATOM   4269  N   THR B 242      42.926  65.152  17.027  1.00 42.40           N  
-ATOM   4270  CA  THR B 242      42.292  66.077  16.094  1.00 42.91           C  
-ATOM   4271  C   THR B 242      40.883  65.674  15.678  1.00 43.75           C  
-ATOM   4272  O   THR B 242      40.080  66.523  15.289  1.00 45.43           O  
-ATOM   4273  CB  THR B 242      43.131  66.229  14.815  1.00 43.38           C  
-ATOM   4274  OG1 THR B 242      43.248  64.953  14.173  1.00 42.81           O  
-ATOM   4275  CG2 THR B 242      44.521  66.758  15.145  1.00 43.63           C  
-ATOM   4276  N   LYS B 243      40.585  64.381  15.749  1.00 44.48           N  
-ATOM   4277  CA  LYS B 243      39.273  63.882  15.359  1.00 44.39           C  
-ATOM   4278  C   LYS B 243      38.605  63.069  16.467  1.00 44.98           C  
-ATOM   4279  O   LYS B 243      39.255  62.287  17.167  1.00 45.72           O  
-ATOM   4280  CB  LYS B 243      39.395  63.040  14.087  1.00 42.82           C  
-ATOM   4281  N   LEU B 244      37.299  63.266  16.617  1.00 44.54           N  
-ATOM   4282  CA  LEU B 244      36.507  62.568  17.623  1.00 43.77           C  
-ATOM   4283  C   LEU B 244      35.352  61.854  16.931  1.00 43.48           C  
-ATOM   4284  O   LEU B 244      34.573  62.475  16.206  1.00 43.56           O  
-ATOM   4285  CB  LEU B 244      35.971  63.568  18.653  1.00 41.98           C  
-ATOM   4286  CG  LEU B 244      34.817  63.159  19.576  1.00 42.21           C  
-ATOM   4287  CD1 LEU B 244      35.160  61.891  20.349  1.00 40.68           C  
-ATOM   4288  CD2 LEU B 244      34.519  64.310  20.529  1.00 39.72           C  
-ATOM   4289  N   PHE B 245      35.248  60.548  17.148  1.00 42.78           N  
-ATOM   4290  CA  PHE B 245      34.185  59.766  16.532  1.00 42.08           C  
-ATOM   4291  C   PHE B 245      33.074  59.428  17.517  1.00 40.84           C  
-ATOM   4292  O   PHE B 245      33.325  58.907  18.604  1.00 40.19           O  
-ATOM   4293  CB  PHE B 245      34.753  58.483  15.932  1.00 43.24           C  
-ATOM   4294  CG  PHE B 245      35.803  58.722  14.891  1.00 46.28           C  
-ATOM   4295  CD1 PHE B 245      37.099  59.066  15.260  1.00 46.91           C  
-ATOM   4296  CD2 PHE B 245      35.493  58.623  13.536  1.00 46.82           C  
-ATOM   4297  CE1 PHE B 245      38.074  59.310  14.294  1.00 48.62           C  
-ATOM   4298  CE2 PHE B 245      36.458  58.865  12.563  1.00 47.30           C  
-ATOM   4299  CZ  PHE B 245      37.752  59.209  12.942  1.00 48.48           C  
-ATOM   4300  N   LEU B 246      31.843  59.728  17.120  1.00 40.02           N  
-ATOM   4301  CA  LEU B 246      30.677  59.471  17.952  1.00 38.93           C  
-ATOM   4302  C   LEU B 246      29.573  58.816  17.133  1.00 39.10           C  
-ATOM   4303  O   LEU B 246      29.704  58.645  15.921  1.00 38.37           O  
-ATOM   4304  CB  LEU B 246      30.170  60.784  18.552  1.00 38.52           C  
-ATOM   4305  CG  LEU B 246      31.143  61.464  19.522  1.00 39.13           C  
-ATOM   4306  CD1 LEU B 246      30.680  62.879  19.812  1.00 39.88           C  
-ATOM   4307  CD2 LEU B 246      31.245  60.646  20.806  1.00 36.90           C  
-ATOM   4308  N   GLY B 247      28.487  58.450  17.804  1.00 38.93           N  
-ATOM   4309  CA  GLY B 247      27.377  57.820  17.116  1.00 38.72           C  
-ATOM   4310  C   GLY B 247      26.164  58.726  17.053  1.00 39.06           C  
-ATOM   4311  O   GLY B 247      26.168  59.731  16.342  1.00 38.62           O  
-ATOM   4312  N   ASN B 248      25.132  58.370  17.813  1.00 39.08           N  
-ATOM   4313  CA  ASN B 248      23.885  59.124  17.857  1.00 38.76           C  
-ATOM   4314  C   ASN B 248      23.947  60.344  18.779  1.00 39.89           C  
-ATOM   4315  O   ASN B 248      23.963  60.213  20.006  1.00 39.89           O  
-ATOM   4316  CB  ASN B 248      22.749  58.191  18.281  1.00 38.82           C  
-ATOM   4317  CG  ASN B 248      21.450  58.925  18.529  1.00 40.75           C  
-ATOM   4318  OD1 ASN B 248      21.112  59.875  17.820  1.00 39.83           O  
-ATOM   4319  ND2 ASN B 248      20.703  58.476  19.533  1.00 41.63           N  
-ATOM   4320  N   LEU B 249      23.963  61.530  18.175  1.00 39.55           N  
-ATOM   4321  CA  LEU B 249      24.038  62.785  18.919  1.00 39.94           C  
-ATOM   4322  C   LEU B 249      22.689  63.306  19.393  1.00 40.27           C  
-ATOM   4323  O   LEU B 249      22.628  64.180  20.259  1.00 39.63           O  
-ATOM   4324  CB  LEU B 249      24.699  63.863  18.058  1.00 40.00           C  
-ATOM   4325  CG  LEU B 249      26.110  63.578  17.547  1.00 41.10           C  
-ATOM   4326  CD1 LEU B 249      26.561  64.698  16.615  1.00 39.16           C  
-ATOM   4327  CD2 LEU B 249      27.054  63.444  18.734  1.00 41.75           C  
-ATOM   4328  N   GLN B 250      21.611  62.769  18.831  1.00 42.02           N  
-ATOM   4329  CA  GLN B 250      20.266  63.213  19.180  1.00 43.82           C  
-ATOM   4330  C   GLN B 250      19.680  62.567  20.434  1.00 43.58           C  
-ATOM   4331  O   GLN B 250      18.637  63.000  20.928  1.00 43.45           O  
-ATOM   4332  CB  GLN B 250      19.323  62.981  17.998  1.00 46.99           C  
-ATOM   4333  CG  GLN B 250      19.813  63.594  16.690  1.00 51.56           C  
-ATOM   4334  CD  GLN B 250      18.823  63.410  15.555  1.00 54.29           C  
-ATOM   4335  OE1 GLN B 250      17.723  63.966  15.579  1.00 55.92           O  
-ATOM   4336  NE2 GLN B 250      19.206  62.624  14.555  1.00 55.27           N  
-ATOM   4337  N   ALA B 251      20.340  61.534  20.950  1.00 42.30           N  
-ATOM   4338  CA  ALA B 251      19.851  60.870  22.154  1.00 39.99           C  
-ATOM   4339  C   ALA B 251      19.878  61.868  23.304  1.00 38.42           C  
-ATOM   4340  O   ALA B 251      20.823  62.642  23.435  1.00 38.59           O  
-ATOM   4341  CB  ALA B 251      20.724  59.671  22.482  1.00 40.87           C  
-ATOM   4342  N   SER B 252      18.838  61.857  24.130  1.00 36.36           N  
-ATOM   4343  CA  SER B 252      18.765  62.773  25.262  1.00 35.82           C  
-ATOM   4344  C   SER B 252      18.846  62.025  26.590  1.00 35.97           C  
-ATOM   4345  O   SER B 252      18.237  60.963  26.760  1.00 35.51           O  
-ATOM   4346  CB  SER B 252      17.471  63.586  25.204  1.00 35.86           C  
-ATOM   4347  OG  SER B 252      17.374  64.450  26.320  1.00 36.73           O  
-ATOM   4348  N   ARG B 253      19.591  62.591  27.536  1.00 34.03           N  
-ATOM   4349  CA  ARG B 253      19.768  61.962  28.838  1.00 32.95           C  
-ATOM   4350  C   ARG B 253      19.696  62.949  29.991  1.00 32.68           C  
-ATOM   4351  O   ARG B 253      19.918  64.147  29.826  1.00 34.83           O  
-ATOM   4352  CB  ARG B 253      21.123  61.241  28.891  1.00 33.14           C  
-ATOM   4353  CG  ARG B 253      21.249  60.038  27.960  1.00 34.71           C  
-ATOM   4354  CD  ARG B 253      20.456  58.831  28.477  1.00 32.76           C  
-ATOM   4355  NE  ARG B 253      20.656  57.635  27.657  1.00 32.70           N  
-ATOM   4356  CZ  ARG B 253      20.132  57.449  26.448  1.00 33.65           C  
-ATOM   4357  NH1 ARG B 253      20.375  56.329  25.782  1.00 33.51           N  
-ATOM   4358  NH2 ARG B 253      19.351  58.373  25.905  1.00 35.46           N  
-ATOM   4359  N   ASP B 254      19.378  62.422  31.162  1.00 32.01           N  
-ATOM   4360  CA  ASP B 254      19.300  63.199  32.385  1.00 30.71           C  
-ATOM   4361  C   ASP B 254      20.637  62.901  33.066  1.00 30.36           C  
-ATOM   4362  O   ASP B 254      20.841  61.812  33.602  1.00 29.31           O  
-ATOM   4363  CB  ASP B 254      18.112  62.705  33.213  1.00 30.78           C  
-ATOM   4364  CG  ASP B 254      18.024  63.358  34.575  1.00 32.06           C  
-ATOM   4365  OD1 ASP B 254      16.893  63.489  35.086  1.00 30.61           O  
-ATOM   4366  OD2 ASP B 254      19.073  63.721  35.145  1.00 34.91           O  
-ATOM   4367  N   TRP B 255      21.551  63.869  33.015  1.00 30.62           N  
-ATOM   4368  CA  TRP B 255      22.896  63.721  33.578  1.00 29.25           C  
-ATOM   4369  C   TRP B 255      23.149  64.414  34.911  1.00 29.99           C  
-ATOM   4370  O   TRP B 255      23.119  65.642  35.002  1.00 28.94           O  
-ATOM   4371  CB  TRP B 255      23.936  64.227  32.577  1.00 27.84           C  
-ATOM   4372  CG  TRP B 255      24.165  63.329  31.404  1.00 29.33           C  
-ATOM   4373  CD1 TRP B 255      24.599  62.032  31.433  1.00 28.04           C  
-ATOM   4374  CD2 TRP B 255      24.032  63.674  30.020  1.00 28.67           C  
-ATOM   4375  NE1 TRP B 255      24.749  61.553  30.154  1.00 28.96           N  
-ATOM   4376  CE2 TRP B 255      24.408  62.540  29.268  1.00 28.48           C  
-ATOM   4377  CE3 TRP B 255      23.633  64.834  29.343  1.00 28.80           C  
-ATOM   4378  CZ2 TRP B 255      24.396  62.531  27.872  1.00 30.11           C  
-ATOM   4379  CZ3 TRP B 255      23.621  64.825  27.953  1.00 27.60           C  
-ATOM   4380  CH2 TRP B 255      24.000  63.680  27.235  1.00 29.62           C  
-ATOM   4381  N   GLY B 256      23.426  63.615  35.936  1.00 30.48           N  
-ATOM   4382  CA  GLY B 256      23.711  64.159  37.250  1.00 30.68           C  
-ATOM   4383  C   GLY B 256      25.164  63.904  37.595  1.00 32.10           C  
-ATOM   4384  O   GLY B 256      25.911  63.368  36.775  1.00 31.73           O  
-ATOM   4385  N   PHE B 257      25.569  64.288  38.802  1.00 32.49           N  
-ATOM   4386  CA  PHE B 257      26.939  64.086  39.253  1.00 32.44           C  
-ATOM   4387  C   PHE B 257      27.002  62.916  40.227  1.00 33.14           C  
-ATOM   4388  O   PHE B 257      26.326  62.912  41.258  1.00 33.37           O  
-ATOM   4389  CB  PHE B 257      27.474  65.359  39.926  1.00 33.06           C  
-ATOM   4390  CG  PHE B 257      28.821  65.183  40.580  1.00 32.42           C  
-ATOM   4391  CD1 PHE B 257      29.897  64.664  39.862  1.00 31.64           C  
-ATOM   4392  CD2 PHE B 257      29.011  65.531  41.913  1.00 30.66           C  
-ATOM   4393  CE1 PHE B 257      31.141  64.493  40.463  1.00 29.97           C  
-ATOM   4394  CE2 PHE B 257      30.251  65.364  42.523  1.00 29.87           C  
-ATOM   4395  CZ  PHE B 257      31.319  64.844  41.796  1.00 30.46           C  
-ATOM   4396  N   ALA B 258      27.827  61.927  39.892  1.00 33.48           N  
-ATOM   4397  CA  ALA B 258      27.985  60.730  40.712  1.00 33.00           C  
-ATOM   4398  C   ALA B 258      28.239  61.042  42.185  1.00 32.49           C  
-ATOM   4399  O   ALA B 258      27.780  60.316  43.069  1.00 31.33           O  
-ATOM   4400  CB  ALA B 258      29.117  59.870  40.155  1.00 33.87           C  
-ATOM   4401  N   GLY B 259      28.976  62.116  42.447  1.00 31.75           N  
-ATOM   4402  CA  GLY B 259      29.261  62.484  43.821  1.00 31.51           C  
-ATOM   4403  C   GLY B 259      27.978  62.765  44.577  1.00 31.55           C  
-ATOM   4404  O   GLY B 259      27.851  62.433  45.753  1.00 31.55           O  
-ATOM   4405  N   ASP B 260      27.019  63.379  43.895  1.00 32.29           N  
-ATOM   4406  CA  ASP B 260      25.735  63.706  44.504  1.00 34.10           C  
-ATOM   4407  C   ASP B 260      24.890  62.455  44.722  1.00 35.20           C  
-ATOM   4408  O   ASP B 260      24.283  62.278  45.781  1.00 36.23           O  
-ATOM   4409  CB  ASP B 260      24.948  64.676  43.609  1.00 33.93           C  
-ATOM   4410  CG  ASP B 260      25.522  66.086  43.609  1.00 32.71           C  
-ATOM   4411  OD1 ASP B 260      25.063  66.902  42.783  1.00 32.30           O  
-ATOM   4412  OD2 ASP B 260      26.416  66.385  44.429  1.00 33.90           O  
-ATOM   4413  N   TYR B 261      24.864  61.592  43.710  1.00 33.51           N  
-ATOM   4414  CA  TYR B 261      24.069  60.369  43.732  1.00 32.04           C  
-ATOM   4415  C   TYR B 261      24.430  59.324  44.778  1.00 32.75           C  
-ATOM   4416  O   TYR B 261      23.536  58.692  45.346  1.00 33.18           O  
-ATOM   4417  CB  TYR B 261      24.083  59.744  42.338  1.00 30.45           C  
-ATOM   4418  CG  TYR B 261      23.290  60.546  41.329  1.00 29.59           C  
-ATOM   4419  CD1 TYR B 261      23.239  61.941  41.399  1.00 29.57           C  
-ATOM   4420  CD2 TYR B 261      22.582  59.914  40.310  1.00 29.09           C  
-ATOM   4421  CE1 TYR B 261      22.499  62.684  40.482  1.00 29.29           C  
-ATOM   4422  CE2 TYR B 261      21.840  60.646  39.386  1.00 30.05           C  
-ATOM   4423  CZ  TYR B 261      21.803  62.030  39.480  1.00 29.81           C  
-ATOM   4424  OH  TYR B 261      21.061  62.754  38.578  1.00 30.94           O  
-ATOM   4425  N   VAL B 262      25.720  59.134  45.042  1.00 32.79           N  
-ATOM   4426  CA  VAL B 262      26.125  58.148  46.037  1.00 33.17           C  
-ATOM   4427  C   VAL B 262      25.526  58.493  47.396  1.00 34.88           C  
-ATOM   4428  O   VAL B 262      25.282  57.608  48.216  1.00 37.12           O  
-ATOM   4429  CB  VAL B 262      27.669  58.046  46.159  1.00 33.29           C  
-ATOM   4430  CG1 VAL B 262      28.254  57.525  44.857  1.00 31.97           C  
-ATOM   4431  CG2 VAL B 262      28.269  59.405  46.500  1.00 31.33           C  
-ATOM   4432  N   GLU B 263      25.283  59.781  47.629  1.00 35.61           N  
-ATOM   4433  CA  GLU B 263      24.695  60.231  48.888  1.00 34.71           C  
-ATOM   4434  C   GLU B 263      23.266  59.696  49.003  1.00 34.39           C  
-ATOM   4435  O   GLU B 263      22.809  59.317  50.089  1.00 34.06           O  
-ATOM   4436  CB  GLU B 263      24.692  61.758  48.947  1.00 35.28           C  
-ATOM   4437  N   ALA B 264      22.573  59.666  47.867  1.00 32.65           N  
-ATOM   4438  CA  ALA B 264      21.199  59.184  47.801  1.00 31.86           C  
-ATOM   4439  C   ALA B 264      21.122  57.690  48.101  1.00 31.49           C  
-ATOM   4440  O   ALA B 264      20.158  57.222  48.704  1.00 33.25           O  
-ATOM   4441  CB  ALA B 264      20.609  59.476  46.422  1.00 30.45           C  
-ATOM   4442  N   MET B 265      22.136  56.943  47.678  1.00 31.08           N  
-ATOM   4443  CA  MET B 265      22.161  55.508  47.922  1.00 30.77           C  
-ATOM   4444  C   MET B 265      22.192  55.304  49.428  1.00 32.45           C  
-ATOM   4445  O   MET B 265      21.507  54.433  49.962  1.00 31.58           O  
-ATOM   4446  CB  MET B 265      23.412  54.873  47.313  1.00 30.59           C  
-ATOM   4447  CG  MET B 265      23.597  55.096  45.827  1.00 31.44           C  
-ATOM   4448  SD  MET B 265      25.180  54.406  45.297  1.00 33.14           S  
-ATOM   4449  CE  MET B 265      25.170  54.790  43.559  1.00 30.64           C  
-ATOM   4450  N   TRP B 266      23.014  56.113  50.097  1.00 33.52           N  
-ATOM   4451  CA  TRP B 266      23.173  56.060  51.545  1.00 33.84           C  
-ATOM   4452  C   TRP B 266      21.876  56.436  52.250  1.00 33.71           C  
-ATOM   4453  O   TRP B 266      21.439  55.744  53.166  1.00 35.08           O  
-ATOM   4454  CB  TRP B 266      24.289  57.012  51.989  1.00 34.85           C  
-ATOM   4455  CG  TRP B 266      24.447  57.105  53.481  1.00 34.51           C  
-ATOM   4456  CD1 TRP B 266      24.951  56.150  54.314  1.00 34.03           C  
-ATOM   4457  CD2 TRP B 266      24.046  58.197  54.319  1.00 35.24           C  
-ATOM   4458  NE1 TRP B 266      24.887  56.577  55.620  1.00 35.55           N  
-ATOM   4459  CE2 TRP B 266      24.335  57.830  55.652  1.00 34.86           C  
-ATOM   4460  CE3 TRP B 266      23.468  59.450  54.072  1.00 35.25           C  
-ATOM   4461  CZ2 TRP B 266      24.065  58.672  56.739  1.00 36.05           C  
-ATOM   4462  CZ3 TRP B 266      23.200  60.290  55.157  1.00 36.47           C  
-ATOM   4463  CH2 TRP B 266      23.499  59.893  56.472  1.00 33.33           C  
-ATOM   4464  N   LEU B 267      21.263  57.531  51.816  1.00 35.67           N  
-ATOM   4465  CA  LEU B 267      20.017  57.993  52.419  1.00 36.23           C  
-ATOM   4466  C   LEU B 267      18.960  56.903  52.415  1.00 36.73           C  
-ATOM   4467  O   LEU B 267      18.331  56.635  53.443  1.00 37.33           O  
-ATOM   4468  CB  LEU B 267      19.495  59.227  51.679  1.00 37.99           C  
-ATOM   4469  CG  LEU B 267      20.263  60.525  51.956  1.00 37.97           C  
-ATOM   4470  CD1 LEU B 267      19.822  61.615  50.995  1.00 37.89           C  
-ATOM   4471  CD2 LEU B 267      20.019  60.948  53.394  1.00 38.10           C  
-ATOM   4472  N   MET B 268      18.775  56.273  51.258  1.00 34.64           N  
-ATOM   4473  CA  MET B 268      17.797  55.200  51.111  1.00 32.68           C  
-ATOM   4474  C   MET B 268      17.884  54.172  52.230  1.00 30.74           C  
-ATOM   4475  O   MET B 268      16.865  53.745  52.764  1.00 29.76           O  
-ATOM   4476  CB  MET B 268      17.981  54.493  49.765  1.00 32.56           C  
-ATOM   4477  CG  MET B 268      17.544  55.317  48.573  1.00 33.55           C  
-ATOM   4478  SD  MET B 268      17.817  54.479  47.001  1.00 34.24           S  
-ATOM   4479  CE  MET B 268      18.404  55.854  46.007  1.00 32.87           C  
-ATOM   4480  N   LEU B 269      19.101  53.780  52.585  1.00 31.13           N  
-ATOM   4481  CA  LEU B 269      19.299  52.784  53.632  1.00 35.40           C  
-ATOM   4482  C   LEU B 269      19.135  53.314  55.057  1.00 37.49           C  
-ATOM   4483  O   LEU B 269      19.164  52.539  56.013  1.00 37.62           O  
-ATOM   4484  CB  LEU B 269      20.680  52.126  53.482  1.00 35.89           C  
-ATOM   4485  CG  LEU B 269      20.800  50.850  52.632  1.00 36.62           C  
-ATOM   4486  CD1 LEU B 269      20.110  51.023  51.293  1.00 35.65           C  
-ATOM   4487  CD2 LEU B 269      22.277  50.517  52.435  1.00 37.64           C  
-ATOM   4488  N   GLN B 270      18.960  54.623  55.209  1.00 39.53           N  
-ATOM   4489  CA  GLN B 270      18.799  55.187  56.546  1.00 40.86           C  
-ATOM   4490  C   GLN B 270      17.328  55.334  56.922  1.00 41.12           C  
-ATOM   4491  O   GLN B 270      16.998  55.529  58.092  1.00 42.99           O  
-ATOM   4492  CB  GLN B 270      19.504  56.548  56.649  1.00 39.87           C  
-ATOM   4493  CG  GLN B 270      20.962  56.524  56.205  1.00 40.61           C  
-ATOM   4494  CD  GLN B 270      21.728  55.324  56.748  1.00 41.65           C  
-ATOM   4495  OE1 GLN B 270      21.921  55.185  57.957  1.00 42.13           O  
-ATOM   4496  NE2 GLN B 270      22.166  54.447  55.847  1.00 41.31           N  
-ATOM   4497  N   GLN B 271      16.444  55.233  55.934  1.00 40.12           N  
-ATOM   4498  CA  GLN B 271      15.014  55.354  56.189  1.00 39.88           C  
-ATOM   4499  C   GLN B 271      14.508  54.231  57.092  1.00 38.83           C  
-ATOM   4500  O   GLN B 271      15.188  53.226  57.299  1.00 37.69           O  
-ATOM   4501  CB  GLN B 271      14.229  55.339  54.876  1.00 41.85           C  
-ATOM   4502  CG  GLN B 271      14.636  56.411  53.879  1.00 43.42           C  
-ATOM   4503  CD  GLN B 271      14.597  57.805  54.466  1.00 45.92           C  
-ATOM   4504  OE1 GLN B 271      15.459  58.182  55.257  1.00 48.64           O  
-ATOM   4505  NE2 GLN B 271      13.588  58.579  54.086  1.00 47.71           N  
-ATOM   4506  N   GLU B 272      13.304  54.414  57.624  1.00 39.35           N  
-ATOM   4507  CA  GLU B 272      12.687  53.438  58.514  1.00 40.49           C  
-ATOM   4508  C   GLU B 272      12.320  52.148  57.787  1.00 39.98           C  
-ATOM   4509  O   GLU B 272      12.488  51.054  58.323  1.00 40.46           O  
-ATOM   4510  CB  GLU B 272      11.441  54.045  59.159  1.00 41.19           C  
-ATOM   4511  N   LYS B 273      11.820  52.280  56.566  1.00 39.73           N  
-ATOM   4512  CA  LYS B 273      11.429  51.119  55.778  1.00 40.34           C  
-ATOM   4513  C   LYS B 273      12.052  51.139  54.379  1.00 38.71           C  
-ATOM   4514  O   LYS B 273      12.268  52.201  53.796  1.00 37.18           O  
-ATOM   4515  CB  LYS B 273       9.906  51.061  55.665  1.00 42.59           C  
-ATOM   4516  CG  LYS B 273       9.184  50.946  57.002  1.00 45.37           C  
-ATOM   4517  CD  LYS B 273       7.673  50.947  56.801  1.00 50.03           C  
-ATOM   4518  CE  LYS B 273       6.924  50.791  58.119  1.00 51.67           C  
-ATOM   4519  NZ  LYS B 273       5.451  50.696  57.907  1.00 53.41           N  
-ATOM   4520  N   PRO B 274      12.351  49.955  53.825  1.00 37.02           N  
-ATOM   4521  CA  PRO B 274      12.950  49.862  52.490  1.00 35.57           C  
-ATOM   4522  C   PRO B 274      11.986  50.317  51.400  1.00 35.16           C  
-ATOM   4523  O   PRO B 274      10.770  50.251  51.572  1.00 35.35           O  
-ATOM   4524  CB  PRO B 274      13.299  48.382  52.378  1.00 35.07           C  
-ATOM   4525  CG  PRO B 274      12.209  47.730  53.177  1.00 36.13           C  
-ATOM   4526  CD  PRO B 274      12.139  48.615  54.400  1.00 36.37           C  
-ATOM   4527  N   ASP B 275      12.525  50.784  50.280  1.00 34.11           N  
-ATOM   4528  CA  ASP B 275      11.682  51.238  49.179  1.00 32.36           C  
-ATOM   4529  C   ASP B 275      12.549  51.524  47.955  1.00 31.73           C  
-ATOM   4530  O   ASP B 275      13.775  51.435  48.021  1.00 30.64           O  
-ATOM   4531  CB  ASP B 275      10.920  52.499  49.596  1.00 31.74           C  
-ATOM   4532  CG  ASP B 275       9.620  52.685  48.827  1.00 32.88           C  
-ATOM   4533  OD1 ASP B 275       8.900  53.658  49.122  1.00 34.45           O  
-ATOM   4534  OD2 ASP B 275       9.313  51.869  47.932  1.00 32.02           O  
-ATOM   4535  N   ASP B 276      11.909  51.864  46.841  1.00 31.49           N  
-ATOM   4536  CA  ASP B 276      12.625  52.158  45.605  1.00 30.21           C  
-ATOM   4537  C   ASP B 276      12.490  53.638  45.273  1.00 30.39           C  
-ATOM   4538  O   ASP B 276      11.408  54.221  45.404  1.00 31.13           O  
-ATOM   4539  CB  ASP B 276      12.067  51.309  44.461  1.00 30.28           C  
-ATOM   4540  CG  ASP B 276      11.945  49.842  44.832  1.00 30.16           C  
-ATOM   4541  OD1 ASP B 276      12.914  49.280  45.384  1.00 31.18           O  
-ATOM   4542  OD2 ASP B 276      10.878  49.246  44.570  1.00 31.05           O  
-ATOM   4543  N   TYR B 277      13.586  54.249  44.839  1.00 30.10           N  
-ATOM   4544  CA  TYR B 277      13.566  55.668  44.523  1.00 29.01           C  
-ATOM   4545  C   TYR B 277      14.294  56.014  43.241  1.00 28.84           C  
-ATOM   4546  O   TYR B 277      15.338  55.444  42.937  1.00 29.23           O  
-ATOM   4547  CB  TYR B 277      14.220  56.478  45.641  1.00 28.70           C  
-ATOM   4548  CG  TYR B 277      13.777  56.134  47.040  1.00 30.68           C  
-ATOM   4549  CD1 TYR B 277      14.274  55.010  47.695  1.00 30.17           C  
-ATOM   4550  CD2 TYR B 277      12.889  56.961  47.725  1.00 31.19           C  
-ATOM   4551  CE1 TYR B 277      13.898  54.724  49.009  1.00 34.45           C  
-ATOM   4552  CE2 TYR B 277      12.508  56.685  49.029  1.00 31.95           C  
-ATOM   4553  CZ  TYR B 277      13.014  55.574  49.668  1.00 30.32           C  
-ATOM   4554  OH  TYR B 277      12.649  55.328  50.969  1.00 30.78           O  
-ATOM   4555  N   VAL B 278      13.738  56.962  42.499  1.00 29.59           N  
-ATOM   4556  CA  VAL B 278      14.367  57.440  41.280  1.00 30.10           C  
-ATOM   4557  C   VAL B 278      15.264  58.601  41.705  1.00 32.81           C  
-ATOM   4558  O   VAL B 278      14.844  59.465  42.478  1.00 33.12           O  
-ATOM   4559  CB  VAL B 278      13.338  57.983  40.276  1.00 30.13           C  
-ATOM   4560  CG1 VAL B 278      14.036  58.877  39.258  1.00 28.10           C  
-ATOM   4561  CG2 VAL B 278      12.626  56.828  39.571  1.00 33.04           C  
-ATOM   4562  N   VAL B 279      16.497  58.613  41.213  1.00 33.07           N  
-ATOM   4563  CA  VAL B 279      17.436  59.677  41.536  1.00 31.38           C  
-ATOM   4564  C   VAL B 279      17.862  60.303  40.216  1.00 32.49           C  
-ATOM   4565  O   VAL B 279      18.485  59.650  39.378  1.00 32.13           O  
-ATOM   4566  CB  VAL B 279      18.670  59.124  42.288  1.00 31.42           C  
-ATOM   4567  CG1 VAL B 279      19.681  60.231  42.530  1.00 30.76           C  
-ATOM   4568  CG2 VAL B 279      18.237  58.519  43.617  1.00 30.66           C  
-ATOM   4569  N   ALA B 280      17.504  61.569  40.028  1.00 31.72           N  
-ATOM   4570  CA  ALA B 280      17.828  62.275  38.799  1.00 32.68           C  
-ATOM   4571  C   ALA B 280      17.805  63.781  39.029  1.00 33.15           C  
-ATOM   4572  O   ALA B 280      17.484  64.241  40.125  1.00 33.77           O  
-ATOM   4573  CB  ALA B 280      16.829  61.898  37.714  1.00 29.62           C  
-ATOM   4574  N   THR B 281      18.150  64.537  37.990  1.00 33.49           N  
-ATOM   4575  CA  THR B 281      18.170  65.996  38.056  1.00 34.77           C  
-ATOM   4576  C   THR B 281      16.876  66.525  37.454  1.00 37.22           C  
-ATOM   4577  O   THR B 281      16.554  67.700  37.592  1.00 38.73           O  
-ATOM   4578  CB  THR B 281      19.337  66.592  37.241  1.00 32.92           C  
-ATOM   4579  OG1 THR B 281      19.072  66.428  35.841  1.00 30.59           O  
-ATOM   4580  CG2 THR B 281      20.648  65.897  37.592  1.00 31.95           C  
-ATOM   4581  N   GLU B 282      16.153  65.643  36.770  1.00 39.10           N  
-ATOM   4582  CA  GLU B 282      14.886  65.985  36.133  1.00 41.06           C  
-ATOM   4583  C   GLU B 282      15.107  66.944  34.977  1.00 41.59           C  
-ATOM   4584  O   GLU B 282      14.165  67.520  34.442  1.00 42.08           O  
-ATOM   4585  CB  GLU B 282      13.934  66.605  37.155  1.00 40.43           C  
-ATOM   4586  CG  GLU B 282      13.826  65.795  38.436  1.00 41.90           C  
-ATOM   4587  CD  GLU B 282      12.738  66.302  39.357  1.00 42.18           C  
-ATOM   4588  OE1 GLU B 282      12.782  67.491  39.735  1.00 43.10           O  
-ATOM   4589  OE2 GLU B 282      11.840  65.506  39.700  1.00 44.02           O  
-ATOM   4590  N   GLU B 283      16.368  67.099  34.594  1.00 42.49           N  
-ATOM   4591  CA  GLU B 283      16.743  67.979  33.497  1.00 42.56           C  
-ATOM   4592  C   GLU B 283      17.344  67.088  32.415  1.00 40.53           C  
-ATOM   4593  O   GLU B 283      18.219  66.271  32.698  1.00 41.37           O  
-ATOM   4594  CB  GLU B 283      17.780  68.998  33.987  1.00 46.13           C  
-ATOM   4595  CG  GLU B 283      18.000  70.199  33.076  1.00 51.42           C  
-ATOM   4596  CD  GLU B 283      19.062  71.158  33.617  1.00 53.88           C  
-ATOM   4597  OE1 GLU B 283      18.970  71.544  34.802  1.00 54.67           O  
-ATOM   4598  OE2 GLU B 283      19.984  71.527  32.858  1.00 53.79           O  
-ATOM   4599  N   GLY B 284      16.873  67.238  31.184  1.00 39.10           N  
-ATOM   4600  CA  GLY B 284      17.387  66.420  30.101  1.00 37.82           C  
-ATOM   4601  C   GLY B 284      18.148  67.204  29.053  1.00 37.16           C  
-ATOM   4602  O   GLY B 284      17.848  68.371  28.794  1.00 37.20           O  
-ATOM   4603  N   HIS B 285      19.142  66.560  28.449  1.00 37.09           N  
-ATOM   4604  CA  HIS B 285      19.958  67.188  27.416  1.00 35.33           C  
-ATOM   4605  C   HIS B 285      20.411  66.152  26.405  1.00 35.11           C  
-ATOM   4606  O   HIS B 285      20.583  64.982  26.737  1.00 36.15           O  
-ATOM   4607  CB  HIS B 285      21.192  67.853  28.033  1.00 34.84           C  
-ATOM   4608  CG  HIS B 285      20.878  69.025  28.908  1.00 34.23           C  
-ATOM   4609  ND1 HIS B 285      20.427  70.227  28.409  1.00 34.60           N  
-ATOM   4610  CD2 HIS B 285      20.961  69.181  30.251  1.00 35.95           C  
-ATOM   4611  CE1 HIS B 285      20.248  71.075  29.407  1.00 35.71           C  
-ATOM   4612  NE2 HIS B 285      20.565  70.465  30.535  1.00 35.35           N  
-ATOM   4613  N   THR B 286      20.602  66.590  25.168  1.00 35.52           N  
-ATOM   4614  CA  THR B 286      21.046  65.700  24.110  1.00 36.62           C  
-ATOM   4615  C   THR B 286      22.561  65.622  24.150  1.00 37.66           C  
-ATOM   4616  O   THR B 286      23.210  66.417  24.823  1.00 38.80           O  
-ATOM   4617  CB  THR B 286      20.648  66.227  22.718  1.00 37.58           C  
-ATOM   4618  OG1 THR B 286      21.313  67.474  22.474  1.00 36.55           O  
-ATOM   4619  CG2 THR B 286      19.144  66.423  22.628  1.00 36.94           C  
-ATOM   4620  N   VAL B 287      23.121  64.665  23.424  1.00 38.98           N  
-ATOM   4621  CA  VAL B 287      24.564  64.515  23.370  1.00 40.41           C  
-ATOM   4622  C   VAL B 287      25.135  65.735  22.644  1.00 42.02           C  
-ATOM   4623  O   VAL B 287      26.229  66.207  22.965  1.00 43.65           O  
-ATOM   4624  CB  VAL B 287      24.955  63.220  22.623  1.00 38.93           C  
-ATOM   4625  CG1 VAL B 287      26.463  63.137  22.465  1.00 38.90           C  
-ATOM   4626  CG2 VAL B 287      24.448  62.008  23.398  1.00 39.31           C  
-ATOM   4627  N   GLU B 288      24.376  66.252  21.679  1.00 42.57           N  
-ATOM   4628  CA  GLU B 288      24.806  67.417  20.910  1.00 43.48           C  
-ATOM   4629  C   GLU B 288      24.976  68.639  21.809  1.00 42.13           C  
-ATOM   4630  O   GLU B 288      25.925  69.407  21.653  1.00 42.24           O  
-ATOM   4631  CB  GLU B 288      23.799  67.734  19.799  1.00 45.27           C  
-ATOM   4632  CG  GLU B 288      24.348  68.702  18.760  1.00 51.36           C  
-ATOM   4633  CD  GLU B 288      23.340  69.073  17.682  1.00 53.86           C  
-ATOM   4634  OE1 GLU B 288      22.713  68.159  17.101  1.00 55.65           O  
-ATOM   4635  OE2 GLU B 288      23.189  70.284  17.407  1.00 53.79           O  
-ATOM   4636  N   GLU B 289      24.058  68.817  22.753  1.00 41.93           N  
-ATOM   4637  CA  GLU B 289      24.136  69.946  23.671  1.00 42.24           C  
-ATOM   4638  C   GLU B 289      25.351  69.787  24.578  1.00 42.15           C  
-ATOM   4639  O   GLU B 289      25.937  70.775  25.030  1.00 43.33           O  
-ATOM   4640  CB  GLU B 289      22.872  70.035  24.525  1.00 43.18           C  
-ATOM   4641  CG  GLU B 289      21.589  70.134  23.723  1.00 45.83           C  
-ATOM   4642  CD  GLU B 289      20.368  70.251  24.605  1.00 46.39           C  
-ATOM   4643  OE1 GLU B 289      20.137  71.341  25.166  1.00 46.55           O  
-ATOM   4644  OE2 GLU B 289      19.645  69.245  24.749  1.00 50.11           O  
-ATOM   4645  N   PHE B 290      25.716  68.535  24.850  1.00 39.80           N  
-ATOM   4646  CA  PHE B 290      26.870  68.246  25.687  1.00 37.22           C  
-ATOM   4647  C   PHE B 290      28.100  68.734  24.931  1.00 36.97           C  
-ATOM   4648  O   PHE B 290      29.025  69.296  25.516  1.00 36.60           O  
-ATOM   4649  CB  PHE B 290      26.996  66.743  25.941  1.00 34.70           C  
-ATOM   4650  CG  PHE B 290      27.964  66.404  27.033  1.00 32.05           C  
-ATOM   4651  CD1 PHE B 290      27.531  66.281  28.346  1.00 30.06           C  
-ATOM   4652  CD2 PHE B 290      29.319  66.275  26.760  1.00 30.26           C  
-ATOM   4653  CE1 PHE B 290      28.433  66.037  29.374  1.00 28.87           C  
-ATOM   4654  CE2 PHE B 290      30.227  66.032  27.780  1.00 29.42           C  
-ATOM   4655  CZ  PHE B 290      29.783  65.914  29.089  1.00 27.74           C  
-ATOM   4656  N   LEU B 291      28.092  68.507  23.620  1.00 37.12           N  
-ATOM   4657  CA  LEU B 291      29.178  68.928  22.752  1.00 36.80           C  
-ATOM   4658  C   LEU B 291      29.255  70.445  22.711  1.00 38.36           C  
-ATOM   4659  O   LEU B 291      30.336  71.020  22.829  1.00 37.53           O  
-ATOM   4660  CB  LEU B 291      28.963  68.391  21.336  1.00 35.88           C  
-ATOM   4661  CG  LEU B 291      29.155  66.884  21.128  1.00 37.16           C  
-ATOM   4662  CD1 LEU B 291      28.813  66.510  19.693  1.00 36.38           C  
-ATOM   4663  CD2 LEU B 291      30.596  66.506  21.441  1.00 35.32           C  
-ATOM   4664  N   ASP B 292      28.107  71.097  22.546  1.00 40.09           N  
-ATOM   4665  CA  ASP B 292      28.084  72.553  22.487  1.00 40.23           C  
-ATOM   4666  C   ASP B 292      28.697  73.148  23.743  1.00 39.43           C  
-ATOM   4667  O   ASP B 292      29.615  73.963  23.672  1.00 39.76           O  
-ATOM   4668  CB  ASP B 292      26.652  73.076  22.330  1.00 42.44           C  
-ATOM   4669  CG  ASP B 292      26.029  72.692  21.002  1.00 44.03           C  
-ATOM   4670  OD1 ASP B 292      26.740  72.730  19.975  1.00 46.45           O  
-ATOM   4671  OD2 ASP B 292      24.822  72.367  20.981  1.00 45.66           O  
-ATOM   4672  N   VAL B 293      28.189  72.726  24.894  1.00 38.42           N  
-ATOM   4673  CA  VAL B 293      28.670  73.226  26.173  1.00 37.30           C  
-ATOM   4674  C   VAL B 293      30.150  72.937  26.421  1.00 38.53           C  
-ATOM   4675  O   VAL B 293      30.923  73.850  26.715  1.00 39.14           O  
-ATOM   4676  CB  VAL B 293      27.844  72.631  27.330  1.00 37.57           C  
-ATOM   4677  CG1 VAL B 293      28.271  73.248  28.653  1.00 37.90           C  
-ATOM   4678  CG2 VAL B 293      26.362  72.882  27.084  1.00 39.67           C  
-ATOM   4679  N   SER B 294      30.547  71.672  26.300  1.00 38.26           N  
-ATOM   4680  CA  SER B 294      31.938  71.296  26.535  1.00 37.14           C  
-ATOM   4681  C   SER B 294      32.919  72.025  25.613  1.00 37.25           C  
-ATOM   4682  O   SER B 294      33.763  72.789  26.086  1.00 36.10           O  
-ATOM   4683  CB  SER B 294      32.109  69.776  26.406  1.00 36.28           C  
-ATOM   4684  OG  SER B 294      31.641  69.301  25.160  1.00 35.30           O  
-ATOM   4685  N   PHE B 295      32.812  71.800  24.306  1.00 36.02           N  
-ATOM   4686  CA  PHE B 295      33.708  72.463  23.369  1.00 37.86           C  
-ATOM   4687  C   PHE B 295      33.613  73.987  23.450  1.00 39.24           C  
-ATOM   4688  O   PHE B 295      34.635  74.676  23.502  1.00 38.53           O  
-ATOM   4689  CB  PHE B 295      33.433  71.998  21.941  1.00 37.87           C  
-ATOM   4690  CG  PHE B 295      34.163  70.742  21.569  1.00 40.40           C  
-ATOM   4691  CD1 PHE B 295      33.858  69.532  22.188  1.00 39.84           C  
-ATOM   4692  CD2 PHE B 295      35.184  70.771  20.621  1.00 39.85           C  
-ATOM   4693  CE1 PHE B 295      34.561  68.371  21.870  1.00 38.83           C  
-ATOM   4694  CE2 PHE B 295      35.892  69.613  20.297  1.00 39.69           C  
-ATOM   4695  CZ  PHE B 295      35.580  68.413  20.922  1.00 38.78           C  
-ATOM   4696  N   GLY B 296      32.390  74.508  23.470  1.00 39.54           N  
-ATOM   4697  CA  GLY B 296      32.205  75.946  23.554  1.00 39.72           C  
-ATOM   4698  C   GLY B 296      32.898  76.541  24.768  1.00 39.95           C  
-ATOM   4699  O   GLY B 296      33.398  77.662  24.720  1.00 40.22           O  
-ATOM   4700  N   TYR B 297      32.932  75.782  25.857  1.00 39.12           N  
-ATOM   4701  CA  TYR B 297      33.567  76.228  27.092  1.00 39.37           C  
-ATOM   4702  C   TYR B 297      35.059  76.506  26.897  1.00 40.47           C  
-ATOM   4703  O   TYR B 297      35.655  77.287  27.640  1.00 42.00           O  
-ATOM   4704  CB  TYR B 297      33.358  75.163  28.166  1.00 39.16           C  
-ATOM   4705  CG  TYR B 297      34.087  75.377  29.470  1.00 37.94           C  
-ATOM   4706  CD1 TYR B 297      33.915  76.543  30.214  1.00 39.17           C  
-ATOM   4707  CD2 TYR B 297      34.882  74.367  30.007  1.00 38.65           C  
-ATOM   4708  CE1 TYR B 297      34.513  76.691  31.471  1.00 38.16           C  
-ATOM   4709  CE2 TYR B 297      35.479  74.501  31.251  1.00 38.12           C  
-ATOM   4710  CZ  TYR B 297      35.291  75.662  31.982  1.00 39.29           C  
-ATOM   4711  OH  TYR B 297      35.866  75.770  33.232  1.00 39.55           O  
-ATOM   4712  N   LEU B 298      35.657  75.868  25.894  1.00 40.44           N  
-ATOM   4713  CA  LEU B 298      37.078  76.051  25.606  1.00 40.54           C  
-ATOM   4714  C   LEU B 298      37.302  76.851  24.321  1.00 41.31           C  
-ATOM   4715  O   LEU B 298      38.424  76.933  23.814  1.00 40.35           O  
-ATOM   4716  CB  LEU B 298      37.779  74.691  25.498  1.00 37.06           C  
-ATOM   4717  CG  LEU B 298      37.781  73.806  26.750  1.00 36.34           C  
-ATOM   4718  CD1 LEU B 298      38.539  72.523  26.466  1.00 35.63           C  
-ATOM   4719  CD2 LEU B 298      38.413  74.549  27.916  1.00 34.81           C  
-ATOM   4720  N   GLY B 299      36.227  77.431  23.796  1.00 42.52           N  
-ATOM   4721  CA  GLY B 299      36.325  78.232  22.590  1.00 43.24           C  
-ATOM   4722  C   GLY B 299      36.566  77.467  21.302  1.00 44.20           C  
-ATOM   4723  O   GLY B 299      37.322  77.920  20.446  1.00 46.31           O  
-ATOM   4724  N   LEU B 300      35.928  76.313  21.149  1.00 44.08           N  
-ATOM   4725  CA  LEU B 300      36.093  75.524  19.935  1.00 43.05           C  
-ATOM   4726  C   LEU B 300      34.734  75.116  19.383  1.00 43.03           C  
-ATOM   4727  O   LEU B 300      33.744  75.101  20.107  1.00 42.68           O  
-ATOM   4728  CB  LEU B 300      36.926  74.271  20.218  1.00 43.24           C  
-ATOM   4729  CG  LEU B 300      38.327  74.447  20.819  1.00 44.71           C  
-ATOM   4730  CD1 LEU B 300      38.929  73.072  21.082  1.00 44.60           C  
-ATOM   4731  CD2 LEU B 300      39.221  75.248  19.878  1.00 42.18           C  
-ATOM   4732  N   ASN B 301      34.698  74.800  18.093  1.00 44.79           N  
-ATOM   4733  CA  ASN B 301      33.473  74.373  17.424  1.00 46.38           C  
-ATOM   4734  C   ASN B 301      33.602  72.860  17.247  1.00 46.90           C  
-ATOM   4735  O   ASN B 301      34.373  72.393  16.404  1.00 46.72           O  
-ATOM   4736  CB  ASN B 301      33.360  75.051  16.053  1.00 48.43           C  
-ATOM   4737  CG  ASN B 301      31.964  74.941  15.449  1.00 50.78           C  
-ATOM   4738  OD1 ASN B 301      31.324  73.889  15.509  1.00 52.71           O  
-ATOM   4739  ND2 ASN B 301      31.494  76.030  14.849  1.00 49.85           N  
-ATOM   4740  N   TRP B 302      32.856  72.092  18.038  1.00 46.99           N  
-ATOM   4741  CA  TRP B 302      32.945  70.639  17.948  1.00 46.54           C  
-ATOM   4742  C   TRP B 302      32.718  70.124  16.538  1.00 45.94           C  
-ATOM   4743  O   TRP B 302      33.231  69.069  16.171  1.00 45.70           O  
-ATOM   4744  CB  TRP B 302      31.963  69.960  18.909  1.00 46.14           C  
-ATOM   4745  CG  TRP B 302      30.516  70.252  18.656  1.00 44.87           C  
-ATOM   4746  CD1 TRP B 302      29.776  71.263  19.198  1.00 44.34           C  
-ATOM   4747  CD2 TRP B 302      29.626  69.509  17.812  1.00 43.50           C  
-ATOM   4748  NE1 TRP B 302      28.479  71.193  18.746  1.00 45.15           N  
-ATOM   4749  CE2 TRP B 302      28.361  70.126  17.894  1.00 44.01           C  
-ATOM   4750  CE3 TRP B 302      29.776  68.382  16.994  1.00 42.57           C  
-ATOM   4751  CZ2 TRP B 302      27.250  69.653  17.188  1.00 43.70           C  
-ATOM   4752  CZ3 TRP B 302      28.671  67.911  16.293  1.00 42.20           C  
-ATOM   4753  CH2 TRP B 302      27.425  68.548  16.396  1.00 41.23           C  
-ATOM   4754  N   LYS B 303      31.959  70.872  15.743  1.00 45.93           N  
-ATOM   4755  CA  LYS B 303      31.684  70.464  14.371  1.00 46.54           C  
-ATOM   4756  C   LYS B 303      32.971  70.352  13.555  1.00 46.08           C  
-ATOM   4757  O   LYS B 303      32.981  69.749  12.483  1.00 46.23           O  
-ATOM   4758  CB  LYS B 303      30.730  71.450  13.715  1.00 48.33           C  
-ATOM   4759  N   ASP B 304      34.057  70.927  14.065  1.00 46.67           N  
-ATOM   4760  CA  ASP B 304      35.340  70.874  13.368  1.00 47.72           C  
-ATOM   4761  C   ASP B 304      36.108  69.587  13.652  1.00 48.14           C  
-ATOM   4762  O   ASP B 304      37.031  69.237  12.914  1.00 47.86           O  
-ATOM   4763  CB  ASP B 304      36.233  72.060  13.761  1.00 48.85           C  
-ATOM   4764  CG  ASP B 304      35.633  73.405  13.388  1.00 49.89           C  
-ATOM   4765  OD1 ASP B 304      35.143  73.548  12.247  1.00 48.78           O  
-ATOM   4766  OD2 ASP B 304      35.667  74.324  14.236  1.00 49.61           O  
-ATOM   4767  N   TYR B 305      35.729  68.876  14.711  1.00 47.55           N  
-ATOM   4768  CA  TYR B 305      36.442  67.655  15.069  1.00 46.75           C  
-ATOM   4769  C   TYR B 305      35.603  66.389  15.083  1.00 46.66           C  
-ATOM   4770  O   TYR B 305      36.107  65.301  14.794  1.00 45.88           O  
-ATOM   4771  CB  TYR B 305      37.100  67.830  16.435  1.00 46.14           C  
-ATOM   4772  CG  TYR B 305      37.755  69.175  16.613  1.00 46.43           C  
-ATOM   4773  CD1 TYR B 305      37.010  70.288  17.012  1.00 45.95           C  
-ATOM   4774  CD2 TYR B 305      39.116  69.345  16.367  1.00 44.66           C  
-ATOM   4775  CE1 TYR B 305      37.608  71.536  17.166  1.00 46.66           C  
-ATOM   4776  CE2 TYR B 305      39.723  70.587  16.514  1.00 46.25           C  
-ATOM   4777  CZ  TYR B 305      38.968  71.678  16.915  1.00 46.93           C  
-ATOM   4778  OH  TYR B 305      39.576  72.903  17.074  1.00 48.46           O  
-ATOM   4779  N   VAL B 306      34.327  66.525  15.421  1.00 46.06           N  
-ATOM   4780  CA  VAL B 306      33.445  65.368  15.488  1.00 45.60           C  
-ATOM   4781  C   VAL B 306      33.093  64.762  14.130  1.00 46.16           C  
-ATOM   4782  O   VAL B 306      32.894  65.471  13.147  1.00 46.64           O  
-ATOM   4783  CB  VAL B 306      32.134  65.717  16.229  1.00 44.54           C  
-ATOM   4784  CG1 VAL B 306      31.213  64.507  16.263  1.00 44.31           C  
-ATOM   4785  CG2 VAL B 306      32.447  66.181  17.643  1.00 42.15           C  
-ATOM   4786  N   GLU B 307      33.036  63.434  14.099  1.00 46.83           N  
-ATOM   4787  CA  GLU B 307      32.676  62.672  12.909  1.00 47.07           C  
-ATOM   4788  C   GLU B 307      31.798  61.516  13.380  1.00 46.75           C  
-ATOM   4789  O   GLU B 307      31.961  61.027  14.499  1.00 46.13           O  
-ATOM   4790  CB  GLU B 307      33.923  62.140  12.204  1.00 48.40           C  
-ATOM   4791  CG  GLU B 307      34.658  63.191  11.391  1.00 51.24           C  
-ATOM   4792  CD  GLU B 307      35.796  62.607  10.570  1.00 53.65           C  
-ATOM   4793  OE1 GLU B 307      35.605  61.526   9.966  1.00 53.85           O  
-ATOM   4794  OE2 GLU B 307      36.877  63.236  10.519  1.00 54.09           O  
-ATOM   4795  N   ILE B 308      30.871  61.081  12.535  1.00 46.58           N  
-ATOM   4796  CA  ILE B 308      29.960  60.005  12.909  1.00 46.28           C  
-ATOM   4797  C   ILE B 308      30.311  58.648  12.312  1.00 46.51           C  
-ATOM   4798  O   ILE B 308      30.599  58.536  11.121  1.00 47.01           O  
-ATOM   4799  CB  ILE B 308      28.505  60.354  12.513  1.00 45.59           C  
-ATOM   4800  CG1 ILE B 308      28.148  61.751  13.029  1.00 44.98           C  
-ATOM   4801  CG2 ILE B 308      27.540  59.323  13.087  1.00 45.13           C  
-ATOM   4802  CD1 ILE B 308      28.349  61.939  14.523  1.00 45.39           C  
-ATOM   4803  N   ASP B 309      30.276  57.619  13.156  1.00 46.92           N  
-ATOM   4804  CA  ASP B 309      30.575  56.252  12.735  1.00 46.61           C  
-ATOM   4805  C   ASP B 309      29.446  55.327  13.197  1.00 45.52           C  
-ATOM   4806  O   ASP B 309      29.142  55.251  14.387  1.00 44.76           O  
-ATOM   4807  CB  ASP B 309      31.916  55.800  13.331  1.00 47.43           C  
-ATOM   4808  CG  ASP B 309      32.338  54.415  12.858  1.00 48.32           C  
-ATOM   4809  OD1 ASP B 309      33.514  54.053  13.071  1.00 50.01           O  
-ATOM   4810  OD2 ASP B 309      31.505  53.683  12.283  1.00 47.76           O  
-ATOM   4811  N   GLN B 310      28.830  54.631  12.243  1.00 44.99           N  
-ATOM   4812  CA  GLN B 310      27.722  53.720  12.524  1.00 44.38           C  
-ATOM   4813  C   GLN B 310      28.050  52.669  13.583  1.00 44.10           C  
-ATOM   4814  O   GLN B 310      27.152  52.131  14.232  1.00 43.74           O  
-ATOM   4815  CB  GLN B 310      27.276  53.037  11.234  1.00 43.44           C  
-ATOM   4816  N   ARG B 311      29.339  52.390  13.758  1.00 44.01           N  
-ATOM   4817  CA  ARG B 311      29.796  51.403  14.731  1.00 43.57           C  
-ATOM   4818  C   ARG B 311      29.428  51.769  16.169  1.00 43.21           C  
-ATOM   4819  O   ARG B 311      29.452  50.915  17.056  1.00 44.61           O  
-ATOM   4820  CB  ARG B 311      31.309  51.223  14.616  1.00 43.82           C  
-ATOM   4821  N   TYR B 312      29.092  53.031  16.401  1.00 41.12           N  
-ATOM   4822  CA  TYR B 312      28.734  53.474  17.741  1.00 40.69           C  
-ATOM   4823  C   TYR B 312      27.229  53.500  17.960  1.00 40.53           C  
-ATOM   4824  O   TYR B 312      26.751  53.813  19.051  1.00 39.09           O  
-ATOM   4825  CB  TYR B 312      29.359  54.842  18.014  1.00 40.12           C  
-ATOM   4826  CG  TYR B 312      30.870  54.772  18.037  1.00 40.70           C  
-ATOM   4827  CD1 TYR B 312      31.648  55.718  17.372  1.00 40.44           C  
-ATOM   4828  CD2 TYR B 312      31.523  53.730  18.698  1.00 41.42           C  
-ATOM   4829  CE1 TYR B 312      33.039  55.625  17.360  1.00 40.40           C  
-ATOM   4830  CE2 TYR B 312      32.911  53.628  18.693  1.00 41.12           C  
-ATOM   4831  CZ  TYR B 312      33.662  54.577  18.021  1.00 41.16           C  
-ATOM   4832  OH  TYR B 312      35.033  54.464  17.999  1.00 41.84           O  
-ATOM   4833  N   PHE B 313      26.486  53.161  16.913  1.00 40.91           N  
-ATOM   4834  CA  PHE B 313      25.036  53.105  17.002  1.00 41.02           C  
-ATOM   4835  C   PHE B 313      24.715  51.734  17.568  1.00 40.58           C  
-ATOM   4836  O   PHE B 313      25.402  50.759  17.269  1.00 41.38           O  
-ATOM   4837  CB  PHE B 313      24.404  53.275  15.614  1.00 42.57           C  
-ATOM   4838  CG  PHE B 313      24.339  54.707  15.146  1.00 41.54           C  
-ATOM   4839  CD1 PHE B 313      23.184  55.463  15.331  1.00 43.66           C  
-ATOM   4840  CD2 PHE B 313      25.436  55.306  14.540  1.00 41.54           C  
-ATOM   4841  CE1 PHE B 313      23.124  56.797  14.917  1.00 43.48           C  
-ATOM   4842  CE2 PHE B 313      25.387  56.638  14.123  1.00 42.55           C  
-ATOM   4843  CZ  PHE B 313      24.230  57.384  14.313  1.00 41.85           C  
-ATOM   4844  N   ARG B 314      23.679  51.658  18.393  1.00 39.67           N  
-ATOM   4845  CA  ARG B 314      23.288  50.396  19.002  1.00 37.81           C  
-ATOM   4846  C   ARG B 314      22.099  49.740  18.296  1.00 36.68           C  
-ATOM   4847  O   ARG B 314      21.272  50.418  17.685  1.00 34.71           O  
-ATOM   4848  CB  ARG B 314      22.984  50.637  20.482  1.00 37.65           C  
-ATOM   4849  CG  ARG B 314      24.214  51.121  21.222  1.00 38.06           C  
-ATOM   4850  CD  ARG B 314      23.900  51.905  22.478  1.00 38.03           C  
-ATOM   4851  NE  ARG B 314      25.126  52.490  23.017  1.00 36.56           N  
-ATOM   4852  CZ  ARG B 314      25.206  53.159  24.160  1.00 36.11           C  
-ATOM   4853  NH1 ARG B 314      26.373  53.647  24.559  1.00 37.38           N  
-ATOM   4854  NH2 ARG B 314      24.124  53.339  24.903  1.00 37.24           N  
-ATOM   4855  N   PRO B 315      22.014  48.400  18.357  1.00 35.50           N  
-ATOM   4856  CA  PRO B 315      20.928  47.642  17.727  1.00 34.93           C  
-ATOM   4857  C   PRO B 315      19.546  48.186  18.085  1.00 35.06           C  
-ATOM   4858  O   PRO B 315      18.668  48.293  17.231  1.00 36.76           O  
-ATOM   4859  CB  PRO B 315      21.162  46.227  18.247  1.00 33.39           C  
-ATOM   4860  CG  PRO B 315      22.657  46.154  18.294  1.00 33.93           C  
-ATOM   4861  CD  PRO B 315      23.023  47.487  18.930  1.00 34.49           C  
-ATOM   4862  N   ALA B 316      19.363  48.512  19.358  1.00 35.02           N  
-ATOM   4863  CA  ALA B 316      18.113  49.068  19.858  1.00 35.06           C  
-ATOM   4864  C   ALA B 316      18.544  50.224  20.751  1.00 36.59           C  
-ATOM   4865  O   ALA B 316      19.302  50.033  21.704  1.00 37.90           O  
-ATOM   4866  CB  ALA B 316      17.348  48.023  20.657  1.00 35.35           C  
-ATOM   4867  N   GLU B 317      18.068  51.423  20.436  1.00 37.28           N  
-ATOM   4868  CA  GLU B 317      18.446  52.624  21.173  1.00 36.86           C  
-ATOM   4869  C   GLU B 317      17.431  53.101  22.202  1.00 36.86           C  
-ATOM   4870  O   GLU B 317      16.250  52.747  22.156  1.00 38.06           O  
-ATOM   4871  CB  GLU B 317      18.737  53.753  20.168  1.00 38.16           C  
-ATOM   4872  CG  GLU B 317      19.045  55.131  20.755  1.00 38.43           C  
-ATOM   4873  CD  GLU B 317      20.340  55.182  21.554  1.00 39.04           C  
-ATOM   4874  OE1 GLU B 317      20.361  54.683  22.700  1.00 39.32           O  
-ATOM   4875  OE2 GLU B 317      21.341  55.722  21.031  1.00 40.71           O  
-ATOM   4876  N   VAL B 318      17.927  53.899  23.141  1.00 36.03           N  
-ATOM   4877  CA  VAL B 318      17.121  54.500  24.192  1.00 36.18           C  
-ATOM   4878  C   VAL B 318      17.132  55.989  23.865  1.00 37.15           C  
-ATOM   4879  O   VAL B 318      18.118  56.684  24.108  1.00 36.94           O  
-ATOM   4880  CB  VAL B 318      17.747  54.270  25.579  1.00 35.76           C  
-ATOM   4881  CG1 VAL B 318      17.008  55.094  26.631  1.00 35.36           C  
-ATOM   4882  CG2 VAL B 318      17.690  52.780  25.928  1.00 34.31           C  
-ATOM   4883  N   ASP B 319      16.026  56.468  23.310  1.00 38.02           N  
-ATOM   4884  CA  ASP B 319      15.910  57.857  22.893  1.00 39.63           C  
-ATOM   4885  C   ASP B 319      15.874  58.972  23.937  1.00 38.53           C  
-ATOM   4886  O   ASP B 319      16.695  59.888  23.894  1.00 38.66           O  
-ATOM   4887  CB  ASP B 319      14.689  58.010  21.974  1.00 42.37           C  
-ATOM   4888  CG  ASP B 319      14.869  57.311  20.628  1.00 46.05           C  
-ATOM   4889  OD1 ASP B 319      13.901  57.291  19.831  1.00 45.95           O  
-ATOM   4890  OD2 ASP B 319      15.975  56.784  20.363  1.00 48.47           O  
-ATOM   4891  N   ASN B 320      14.944  58.905  24.882  1.00 37.57           N  
-ATOM   4892  CA  ASN B 320      14.814  59.998  25.838  1.00 36.33           C  
-ATOM   4893  C   ASN B 320      14.610  59.608  27.296  1.00 34.80           C  
-ATOM   4894  O   ASN B 320      13.557  59.100  27.672  1.00 35.46           O  
-ATOM   4895  CB  ASN B 320      13.644  60.879  25.393  1.00 37.33           C  
-ATOM   4896  CG  ASN B 320      13.638  62.232  26.060  1.00 38.70           C  
-ATOM   4897  OD1 ASN B 320      14.097  62.390  27.191  1.00 40.85           O  
-ATOM   4898  ND2 ASN B 320      13.094  63.220  25.365  1.00 38.21           N  
-ATOM   4899  N   LEU B 321      15.607  59.878  28.124  1.00 33.91           N  
-ATOM   4900  CA  LEU B 321      15.500  59.563  29.537  1.00 33.90           C  
-ATOM   4901  C   LEU B 321      15.525  60.835  30.379  1.00 35.15           C  
-ATOM   4902  O   LEU B 321      16.464  61.627  30.309  1.00 35.31           O  
-ATOM   4903  CB  LEU B 321      16.638  58.629  29.970  1.00 34.19           C  
-ATOM   4904  CG  LEU B 321      16.632  57.190  29.441  1.00 34.32           C  
-ATOM   4905  CD1 LEU B 321      17.880  56.468  29.925  1.00 32.01           C  
-ATOM   4906  CD2 LEU B 321      15.377  56.457  29.917  1.00 33.09           C  
-ATOM   4907  N   GLN B 322      14.472  61.029  31.162  1.00 34.67           N  
-ATOM   4908  CA  GLN B 322      14.366  62.180  32.042  1.00 36.07           C  
-ATOM   4909  C   GLN B 322      13.552  61.722  33.238  1.00 35.24           C  
-ATOM   4910  O   GLN B 322      12.382  61.383  33.105  1.00 36.52           O  
-ATOM   4911  CB  GLN B 322      13.659  63.346  31.346  1.00 38.72           C  
-ATOM   4912  CG  GLN B 322      13.689  64.626  32.174  1.00 42.87           C  
-ATOM   4913  CD  GLN B 322      12.749  65.691  31.654  1.00 45.11           C  
-ATOM   4914  OE1 GLN B 322      12.860  66.135  30.510  1.00 47.91           O  
-ATOM   4915  NE2 GLN B 322      11.813  66.108  32.496  1.00 43.93           N  
-ATOM   4916  N   GLY B 323      14.172  61.715  34.407  1.00 35.48           N  
-ATOM   4917  CA  GLY B 323      13.472  61.253  35.588  1.00 36.15           C  
-ATOM   4918  C   GLY B 323      12.685  62.258  36.401  1.00 37.43           C  
-ATOM   4919  O   GLY B 323      12.849  63.471  36.280  1.00 37.78           O  
-ATOM   4920  N   ASP B 324      11.808  61.716  37.233  1.00 37.62           N  
-ATOM   4921  CA  ASP B 324      10.976  62.485  38.136  1.00 37.28           C  
-ATOM   4922  C   ASP B 324      11.433  62.012  39.513  1.00 38.62           C  
-ATOM   4923  O   ASP B 324      11.102  60.902  39.940  1.00 37.76           O  
-ATOM   4924  CB  ASP B 324       9.503  62.146  37.902  1.00 37.08           C  
-ATOM   4925  CG  ASP B 324       8.586  62.770  38.936  1.00 39.15           C  
-ATOM   4926  OD1 ASP B 324       7.350  62.680  38.765  1.00 41.68           O  
-ATOM   4927  OD2 ASP B 324       9.094  63.342  39.923  1.00 40.55           O  
-ATOM   4928  N   ALA B 325      12.208  62.849  40.194  1.00 37.79           N  
-ATOM   4929  CA  ALA B 325      12.745  62.499  41.502  1.00 36.77           C  
-ATOM   4930  C   ALA B 325      11.953  63.067  42.672  1.00 37.71           C  
-ATOM   4931  O   ALA B 325      12.501  63.260  43.760  1.00 37.42           O  
-ATOM   4932  CB  ALA B 325      14.197  62.947  41.592  1.00 36.34           C  
-ATOM   4933  N   SER B 326      10.666  63.315  42.452  1.00 37.63           N  
-ATOM   4934  CA  SER B 326       9.792  63.858  43.487  1.00 38.22           C  
-ATOM   4935  C   SER B 326       9.850  63.053  44.778  1.00 38.48           C  
-ATOM   4936  O   SER B 326       9.954  63.615  45.866  1.00 39.69           O  
-ATOM   4937  CB  SER B 326       8.343  63.886  42.994  1.00 38.34           C  
-ATOM   4938  OG  SER B 326       8.208  64.701  41.848  1.00 40.31           O  
-ATOM   4939  N   LYS B 327       9.781  61.734  44.655  1.00 38.89           N  
-ATOM   4940  CA  LYS B 327       9.800  60.858  45.819  1.00 37.91           C  
-ATOM   4941  C   LYS B 327      11.099  60.932  46.620  1.00 38.14           C  
-ATOM   4942  O   LYS B 327      11.080  60.856  47.850  1.00 39.17           O  
-ATOM   4943  CB  LYS B 327       9.537  59.414  45.384  1.00 37.55           C  
-ATOM   4944  CG  LYS B 327       9.379  58.437  46.536  1.00 37.62           C  
-ATOM   4945  CD  LYS B 327       9.115  57.033  46.022  1.00 38.85           C  
-ATOM   4946  CE  LYS B 327       8.989  56.040  47.162  1.00 38.31           C  
-ATOM   4947  NZ  LYS B 327       8.771  54.657  46.658  1.00 39.42           N  
-ATOM   4948  N   ALA B 328      12.226  61.072  45.929  1.00 36.79           N  
-ATOM   4949  CA  ALA B 328      13.515  61.156  46.605  1.00 36.16           C  
-ATOM   4950  C   ALA B 328      13.594  62.480  47.354  1.00 35.57           C  
-ATOM   4951  O   ALA B 328      14.012  62.535  48.510  1.00 36.40           O  
-ATOM   4952  CB  ALA B 328      14.647  61.060  45.591  1.00 34.89           C  
-ATOM   4953  N   LYS B 329      13.183  63.547  46.681  1.00 35.35           N  
-ATOM   4954  CA  LYS B 329      13.196  64.873  47.275  1.00 37.22           C  
-ATOM   4955  C   LYS B 329      12.312  64.903  48.518  1.00 37.23           C  
-ATOM   4956  O   LYS B 329      12.747  65.316  49.586  1.00 37.54           O  
-ATOM   4957  CB  LYS B 329      12.707  65.901  46.261  1.00 37.44           C  
-ATOM   4958  N   GLU B 330      11.075  64.442  48.376  1.00 36.95           N  
-ATOM   4959  CA  GLU B 330      10.131  64.446  49.483  1.00 37.82           C  
-ATOM   4960  C   GLU B 330      10.443  63.468  50.609  1.00 37.78           C  
-ATOM   4961  O   GLU B 330      10.280  63.804  51.780  1.00 38.90           O  
-ATOM   4962  CB  GLU B 330       8.719  64.198  48.959  1.00 36.64           C  
-ATOM   4963  N   VAL B 331      10.894  62.264  50.272  1.00 38.65           N  
-ATOM   4964  CA  VAL B 331      11.181  61.261  51.301  1.00 37.95           C  
-ATOM   4965  C   VAL B 331      12.608  61.282  51.832  1.00 37.67           C  
-ATOM   4966  O   VAL B 331      12.826  61.184  53.041  1.00 37.67           O  
-ATOM   4967  CB  VAL B 331      10.871  59.823  50.791  1.00 39.31           C  
-ATOM   4968  CG1 VAL B 331      11.235  58.795  51.856  1.00 37.28           C  
-ATOM   4969  CG2 VAL B 331       9.399  59.704  50.435  1.00 38.24           C  
-ATOM   4970  N   LEU B 332      13.580  61.405  50.938  1.00 36.64           N  
-ATOM   4971  CA  LEU B 332      14.976  61.415  51.354  1.00 38.19           C  
-ATOM   4972  C   LEU B 332      15.485  62.838  51.535  1.00 38.74           C  
-ATOM   4973  O   LEU B 332      16.546  63.055  52.115  1.00 38.52           O  
-ATOM   4974  CB  LEU B 332      15.845  60.709  50.310  1.00 37.55           C  
-ATOM   4975  CG  LEU B 332      15.439  59.315  49.827  1.00 37.12           C  
-ATOM   4976  CD1 LEU B 332      16.334  58.917  48.668  1.00 34.19           C  
-ATOM   4977  CD2 LEU B 332      15.545  58.311  50.961  1.00 35.47           C  
-ATOM   4978  N   GLY B 333      14.723  63.804  51.036  1.00 40.44           N  
-ATOM   4979  CA  GLY B 333      15.145  65.187  51.132  1.00 41.06           C  
-ATOM   4980  C   GLY B 333      16.305  65.406  50.179  1.00 41.04           C  
-ATOM   4981  O   GLY B 333      16.926  66.467  50.159  1.00 41.33           O  
-ATOM   4982  N   TRP B 334      16.591  64.393  49.369  1.00 40.02           N  
-ATOM   4983  CA  TRP B 334      17.695  64.478  48.427  1.00 38.75           C  
-ATOM   4984  C   TRP B 334      17.433  65.411  47.257  1.00 39.70           C  
-ATOM   4985  O   TRP B 334      16.333  65.453  46.704  1.00 41.40           O  
-ATOM   4986  CB  TRP B 334      18.045  63.095  47.878  1.00 36.70           C  
-ATOM   4987  CG  TRP B 334      19.259  63.125  47.005  1.00 34.11           C  
-ATOM   4988  CD1 TRP B 334      20.563  63.064  47.411  1.00 32.21           C  
-ATOM   4989  CD2 TRP B 334      19.288  63.284  45.581  1.00 31.41           C  
-ATOM   4990  NE1 TRP B 334      21.401  63.176  46.328  1.00 33.44           N  
-ATOM   4991  CE2 TRP B 334      20.646  63.311  45.192  1.00 31.68           C  
-ATOM   4992  CE3 TRP B 334      18.299  63.404  44.597  1.00 30.90           C  
-ATOM   4993  CZ2 TRP B 334      21.041  63.453  43.860  1.00 31.49           C  
-ATOM   4994  CZ3 TRP B 334      18.691  63.547  43.270  1.00 32.19           C  
-ATOM   4995  CH2 TRP B 334      20.052  63.569  42.915  1.00 33.45           C  
-ATOM   4996  N   LYS B 335      18.469  66.148  46.880  1.00 39.81           N  
-ATOM   4997  CA  LYS B 335      18.404  67.073  45.765  1.00 39.56           C  
-ATOM   4998  C   LYS B 335      19.812  67.168  45.198  1.00 40.03           C  
-ATOM   4999  O   LYS B 335      20.784  67.235  45.947  1.00 40.92           O  
-ATOM   5000  CB  LYS B 335      17.935  68.445  46.239  1.00 39.97           C  
-ATOM   5001  N   PRO B 336      19.942  67.157  43.865  1.00 39.63           N  
-ATOM   5002  CA  PRO B 336      21.267  67.249  43.249  1.00 39.58           C  
-ATOM   5003  C   PRO B 336      21.842  68.643  43.475  1.00 39.77           C  
-ATOM   5004  O   PRO B 336      21.131  69.635  43.352  1.00 39.23           O  
-ATOM   5005  CB  PRO B 336      20.979  66.968  41.777  1.00 41.17           C  
-ATOM   5006  CG  PRO B 336      19.611  67.561  41.594  1.00 40.47           C  
-ATOM   5007  CD  PRO B 336      18.884  67.090  42.840  1.00 39.51           C  
-ATOM   5008  N   GLN B 337      23.123  68.715  43.816  1.00 39.49           N  
-ATOM   5009  CA  GLN B 337      23.766  69.995  44.062  1.00 38.93           C  
-ATOM   5010  C   GLN B 337      24.470  70.501  42.808  1.00 40.09           C  
-ATOM   5011  O   GLN B 337      24.559  71.706  42.582  1.00 40.24           O  
-ATOM   5012  CB  GLN B 337      24.759  69.870  45.215  1.00 39.40           C  
-ATOM   5013  N   VAL B 338      24.968  69.579  41.991  1.00 39.99           N  
-ATOM   5014  CA  VAL B 338      25.663  69.951  40.765  1.00 38.61           C  
-ATOM   5015  C   VAL B 338      24.718  69.908  39.573  1.00 37.98           C  
-ATOM   5016  O   VAL B 338      24.078  68.892  39.313  1.00 38.00           O  
-ATOM   5017  CB  VAL B 338      26.863  69.008  40.493  1.00 39.54           C  
-ATOM   5018  CG1 VAL B 338      27.542  69.379  39.182  1.00 36.88           C  
-ATOM   5019  CG2 VAL B 338      27.854  69.089  41.644  1.00 38.20           C  
-ATOM   5020  N   GLY B 339      24.633  71.024  38.857  1.00 38.04           N  
-ATOM   5021  CA  GLY B 339      23.769  71.099  37.694  1.00 36.87           C  
-ATOM   5022  C   GLY B 339      24.509  70.687  36.436  1.00 37.35           C  
-ATOM   5023  O   GLY B 339      25.720  70.475  36.461  1.00 38.24           O  
-ATOM   5024  N   PHE B 340      23.783  70.590  35.329  1.00 37.16           N  
-ATOM   5025  CA  PHE B 340      24.362  70.185  34.056  1.00 37.18           C  
-ATOM   5026  C   PHE B 340      25.604  70.968  33.616  1.00 39.09           C  
-ATOM   5027  O   PHE B 340      26.658  70.373  33.371  1.00 39.28           O  
-ATOM   5028  CB  PHE B 340      23.299  70.266  32.962  1.00 36.14           C  
-ATOM   5029  CG  PHE B 340      23.794  69.862  31.608  1.00 37.16           C  
-ATOM   5030  CD1 PHE B 340      23.833  70.778  30.568  1.00 36.74           C  
-ATOM   5031  CD2 PHE B 340      24.207  68.556  31.367  1.00 37.89           C  
-ATOM   5032  CE1 PHE B 340      24.271  70.399  29.302  1.00 37.39           C  
-ATOM   5033  CE2 PHE B 340      24.648  68.167  30.105  1.00 37.02           C  
-ATOM   5034  CZ  PHE B 340      24.679  69.089  29.071  1.00 35.91           C  
-ATOM   5035  N   GLU B 341      25.477  72.290  33.502  1.00 38.55           N  
-ATOM   5036  CA  GLU B 341      26.591  73.134  33.073  1.00 39.12           C  
-ATOM   5037  C   GLU B 341      27.819  72.966  33.964  1.00 39.44           C  
-ATOM   5038  O   GLU B 341      28.940  72.822  33.469  1.00 39.21           O  
-ATOM   5039  CB  GLU B 341      26.160  74.608  33.043  1.00 38.83           C  
-ATOM   5040  N   LYS B 342      27.608  72.984  35.278  1.00 39.40           N  
-ATOM   5041  CA  LYS B 342      28.707  72.827  36.218  1.00 39.65           C  
-ATOM   5042  C   LYS B 342      29.357  71.444  36.095  1.00 39.51           C  
-ATOM   5043  O   LYS B 342      30.573  71.308  36.246  1.00 39.53           O  
-ATOM   5044  CB  LYS B 342      28.216  73.057  37.650  1.00 42.06           C  
-ATOM   5045  CG  LYS B 342      29.333  73.038  38.683  1.00 45.36           C  
-ATOM   5046  CD  LYS B 342      28.901  73.636  40.010  1.00 47.10           C  
-ATOM   5047  CE  LYS B 342      30.070  73.651  40.988  1.00 49.47           C  
-ATOM   5048  NZ  LYS B 342      29.741  74.345  42.265  1.00 49.93           N  
-ATOM   5049  N   LEU B 343      28.547  70.421  35.822  1.00 38.71           N  
-ATOM   5050  CA  LEU B 343      29.058  69.061  35.662  1.00 36.28           C  
-ATOM   5051  C   LEU B 343      29.929  68.984  34.412  1.00 36.17           C  
-ATOM   5052  O   LEU B 343      31.043  68.465  34.452  1.00 34.87           O  
-ATOM   5053  CB  LEU B 343      27.907  68.058  35.536  1.00 36.54           C  
-ATOM   5054  CG  LEU B 343      28.306  66.604  35.248  1.00 34.76           C  
-ATOM   5055  CD1 LEU B 343      28.994  66.003  36.466  1.00 31.46           C  
-ATOM   5056  CD2 LEU B 343      27.068  65.798  34.877  1.00 34.45           C  
-ATOM   5057  N   VAL B 344      29.417  69.506  33.303  1.00 35.80           N  
-ATOM   5058  CA  VAL B 344      30.158  69.494  32.052  1.00 37.23           C  
-ATOM   5059  C   VAL B 344      31.486  70.232  32.199  1.00 38.74           C  
-ATOM   5060  O   VAL B 344      32.533  69.740  31.774  1.00 38.79           O  
-ATOM   5061  CB  VAL B 344      29.348  70.150  30.918  1.00 37.66           C  
-ATOM   5062  CG1 VAL B 344      30.152  70.136  29.622  1.00 37.16           C  
-ATOM   5063  CG2 VAL B 344      28.041  69.410  30.730  1.00 38.59           C  
-ATOM   5064  N   LYS B 345      31.442  71.412  32.806  1.00 39.81           N  
-ATOM   5065  CA  LYS B 345      32.646  72.207  32.998  1.00 41.12           C  
-ATOM   5066  C   LYS B 345      33.615  71.523  33.960  1.00 40.96           C  
-ATOM   5067  O   LYS B 345      34.830  71.654  33.822  1.00 40.47           O  
-ATOM   5068  CB  LYS B 345      32.271  73.601  33.511  1.00 43.00           C  
-ATOM   5069  CG  LYS B 345      31.452  74.401  32.511  1.00 46.03           C  
-ATOM   5070  CD  LYS B 345      30.894  75.681  33.116  1.00 49.16           C  
-ATOM   5071  CE  LYS B 345      30.026  76.425  32.106  1.00 49.84           C  
-ATOM   5072  NZ  LYS B 345      29.387  77.641  32.689  1.00 52.50           N  
-ATOM   5073  N   MET B 346      33.072  70.789  34.928  1.00 40.77           N  
-ATOM   5074  CA  MET B 346      33.892  70.076  35.904  1.00 39.31           C  
-ATOM   5075  C   MET B 346      34.687  68.980  35.203  1.00 38.91           C  
-ATOM   5076  O   MET B 346      35.874  68.781  35.470  1.00 38.28           O  
-ATOM   5077  CB  MET B 346      33.011  69.435  36.979  1.00 39.51           C  
-ATOM   5078  CG  MET B 346      33.796  68.678  38.041  1.00 40.47           C  
-ATOM   5079  SD  MET B 346      32.777  67.556  39.029  1.00 43.58           S  
-ATOM   5080  CE  MET B 346      31.719  68.738  39.888  1.00 43.32           C  
-ATOM   5081  N   MET B 347      34.018  68.266  34.307  1.00 36.80           N  
-ATOM   5082  CA  MET B 347      34.662  67.188  33.577  1.00 36.42           C  
-ATOM   5083  C   MET B 347      35.680  67.727  32.584  1.00 35.08           C  
-ATOM   5084  O   MET B 347      36.743  67.136  32.400  1.00 34.74           O  
-ATOM   5085  CB  MET B 347      33.614  66.335  32.856  1.00 35.19           C  
-ATOM   5086  CG  MET B 347      32.729  65.529  33.794  1.00 32.28           C  
-ATOM   5087  SD  MET B 347      31.548  64.499  32.900  1.00 33.01           S  
-ATOM   5088  CE  MET B 347      32.643  63.226  32.275  1.00 29.78           C  
-ATOM   5089  N   VAL B 348      35.362  68.849  31.950  1.00 35.62           N  
-ATOM   5090  CA  VAL B 348      36.281  69.447  30.988  1.00 36.41           C  
-ATOM   5091  C   VAL B 348      37.547  69.936  31.678  1.00 36.87           C  
-ATOM   5092  O   VAL B 348      38.650  69.720  31.183  1.00 37.76           O  
-ATOM   5093  CB  VAL B 348      35.636  70.630  30.245  1.00 35.60           C  
-ATOM   5094  CG1 VAL B 348      36.687  71.363  29.431  1.00 33.62           C  
-ATOM   5095  CG2 VAL B 348      34.538  70.125  29.332  1.00 35.26           C  
-ATOM   5096  N   ASP B 349      37.387  70.592  32.822  1.00 39.02           N  
-ATOM   5097  CA  ASP B 349      38.532  71.100  33.573  1.00 39.37           C  
-ATOM   5098  C   ASP B 349      39.476  69.967  33.972  1.00 40.04           C  
-ATOM   5099  O   ASP B 349      40.694  70.075  33.813  1.00 41.10           O  
-ATOM   5100  CB  ASP B 349      38.069  71.834  34.836  1.00 39.04           C  
-ATOM   5101  CG  ASP B 349      37.402  73.169  34.538  1.00 39.64           C  
-ATOM   5102  OD1 ASP B 349      37.416  73.620  33.372  1.00 37.14           O  
-ATOM   5103  OD2 ASP B 349      36.869  73.773  35.490  1.00 41.06           O  
-ATOM   5104  N   GLU B 350      38.908  68.884  34.496  1.00 40.43           N  
-ATOM   5105  CA  GLU B 350      39.692  67.733  34.926  1.00 40.02           C  
-ATOM   5106  C   GLU B 350      40.404  67.038  33.781  1.00 38.68           C  
-ATOM   5107  O   GLU B 350      41.586  66.729  33.883  1.00 39.00           O  
-ATOM   5108  CB  GLU B 350      38.801  66.730  35.653  1.00 41.42           C  
-ATOM   5109  CG  GLU B 350      38.318  67.239  36.986  1.00 46.42           C  
-ATOM   5110  CD  GLU B 350      39.461  67.780  37.814  1.00 49.63           C  
-ATOM   5111  OE1 GLU B 350      40.436  67.030  38.029  1.00 51.11           O  
-ATOM   5112  OE2 GLU B 350      39.389  68.952  38.243  1.00 51.61           O  
-ATOM   5113  N   ASP B 351      39.683  66.787  32.693  1.00 38.53           N  
-ATOM   5114  CA  ASP B 351      40.281  66.127  31.544  1.00 38.19           C  
-ATOM   5115  C   ASP B 351      41.248  67.035  30.800  1.00 38.12           C  
-ATOM   5116  O   ASP B 351      42.096  66.552  30.053  1.00 38.92           O  
-ATOM   5117  CB  ASP B 351      39.200  65.601  30.591  1.00 38.25           C  
-ATOM   5118  CG  ASP B 351      38.707  64.203  30.977  1.00 41.28           C  
-ATOM   5119  OD1 ASP B 351      37.888  63.620  30.229  1.00 39.95           O  
-ATOM   5120  OD2 ASP B 351      39.140  63.687  32.033  1.00 41.39           O  
-ATOM   5121  N   LEU B 352      41.122  68.347  30.991  1.00 38.56           N  
-ATOM   5122  CA  LEU B 352      42.032  69.284  30.340  1.00 38.00           C  
-ATOM   5123  C   LEU B 352      43.356  69.170  31.087  1.00 38.90           C  
-ATOM   5124  O   LEU B 352      44.427  69.104  30.486  1.00 38.63           O  
-ATOM   5125  CB  LEU B 352      41.498  70.721  30.423  1.00 37.76           C  
-ATOM   5126  CG  LEU B 352      42.386  71.807  29.791  1.00 37.57           C  
-ATOM   5127  CD1 LEU B 352      42.664  71.467  28.330  1.00 35.36           C  
-ATOM   5128  CD2 LEU B 352      41.705  73.171  29.898  1.00 36.68           C  
-ATOM   5129  N   GLU B 353      43.265  69.132  32.411  1.00 40.17           N  
-ATOM   5130  CA  GLU B 353      44.442  68.993  33.256  1.00 41.35           C  
-ATOM   5131  C   GLU B 353      45.136  67.679  32.904  1.00 41.46           C  
-ATOM   5132  O   GLU B 353      46.365  67.597  32.861  1.00 41.79           O  
-ATOM   5133  CB  GLU B 353      44.028  68.978  34.725  1.00 42.52           C  
-ATOM   5134  CG  GLU B 353      45.190  68.897  35.690  1.00 48.11           C  
-ATOM   5135  CD  GLU B 353      46.185  70.025  35.483  1.00 52.19           C  
-ATOM   5136  OE1 GLU B 353      45.743  71.192  35.369  1.00 54.23           O  
-ATOM   5137  OE2 GLU B 353      47.406  69.744  35.441  1.00 53.28           O  
-ATOM   5138  N   LEU B 354      44.332  66.651  32.650  1.00 40.41           N  
-ATOM   5139  CA  LEU B 354      44.853  65.339  32.300  1.00 38.98           C  
-ATOM   5140  C   LEU B 354      45.614  65.420  30.985  1.00 38.17           C  
-ATOM   5141  O   LEU B 354      46.736  64.924  30.868  1.00 37.12           O  
-ATOM   5142  CB  LEU B 354      43.707  64.337  32.168  1.00 38.02           C  
-ATOM   5143  CG  LEU B 354      44.121  62.902  31.864  1.00 38.82           C  
-ATOM   5144  CD1 LEU B 354      45.129  62.437  32.911  1.00 40.34           C  
-ATOM   5145  CD2 LEU B 354      42.892  62.001  31.861  1.00 40.53           C  
-ATOM   5146  N   ALA B 355      44.989  66.050  29.995  1.00 37.48           N  
-ATOM   5147  CA  ALA B 355      45.597  66.206  28.681  1.00 36.82           C  
-ATOM   5148  C   ALA B 355      46.906  66.985  28.797  1.00 36.49           C  
-ATOM   5149  O   ALA B 355      47.893  66.643  28.153  1.00 36.01           O  
-ATOM   5150  CB  ALA B 355      44.634  66.923  27.741  1.00 34.23           C  
-ATOM   5151  N   LYS B 356      46.914  68.025  29.624  1.00 36.06           N  
-ATOM   5152  CA  LYS B 356      48.117  68.821  29.808  1.00 37.71           C  
-ATOM   5153  C   LYS B 356      49.214  67.976  30.448  1.00 38.91           C  
-ATOM   5154  O   LYS B 356      50.387  68.114  30.122  1.00 38.69           O  
-ATOM   5155  CB  LYS B 356      47.827  70.044  30.681  1.00 37.50           C  
-ATOM   5156  CG  LYS B 356      46.995  71.117  29.993  1.00 39.42           C  
-ATOM   5157  CD  LYS B 356      46.833  72.353  30.872  1.00 38.60           C  
-ATOM   5158  CE  LYS B 356      46.058  73.437  30.144  1.00 40.64           C  
-ATOM   5159  NZ  LYS B 356      45.808  74.632  30.994  1.00 41.52           N  
-ATOM   5160  N   ARG B 357      48.823  67.099  31.365  1.00 42.05           N  
-ATOM   5161  CA  ARG B 357      49.780  66.231  32.034  1.00 43.42           C  
-ATOM   5162  C   ARG B 357      50.439  65.333  30.987  1.00 42.25           C  
-ATOM   5163  O   ARG B 357      51.642  65.081  31.032  1.00 42.66           O  
-ATOM   5164  CB  ARG B 357      49.068  65.370  33.083  1.00 46.65           C  
-ATOM   5165  CG  ARG B 357      49.997  64.473  33.888  1.00 51.23           C  
-ATOM   5166  CD  ARG B 357      49.220  63.439  34.694  1.00 54.06           C  
-ATOM   5167  NE  ARG B 357      48.669  62.381  33.849  1.00 57.74           N  
-ATOM   5168  CZ  ARG B 357      49.406  61.497  33.181  1.00 59.38           C  
-ATOM   5169  NH1 ARG B 357      50.728  61.541  33.259  1.00 61.23           N  
-ATOM   5170  NH2 ARG B 357      48.823  60.567  32.435  1.00 59.84           N  
-ATOM   5171  N   GLU B 358      49.637  64.856  30.041  1.00 41.72           N  
-ATOM   5172  CA  GLU B 358      50.140  63.988  28.985  1.00 41.12           C  
-ATOM   5173  C   GLU B 358      50.991  64.800  28.027  1.00 38.56           C  
-ATOM   5174  O   GLU B 358      51.958  64.296  27.461  1.00 39.42           O  
-ATOM   5175  CB  GLU B 358      48.973  63.345  28.235  1.00 41.30           C  
-ATOM   5176  CG  GLU B 358      48.008  62.609  29.155  1.00 45.06           C  
-ATOM   5177  CD  GLU B 358      46.897  61.902  28.404  1.00 45.74           C  
-ATOM   5178  OE1 GLU B 358      46.162  62.575  27.646  1.00 45.11           O  
-ATOM   5179  OE2 GLU B 358      46.760  60.672  28.576  1.00 46.25           O  
-ATOM   5180  N   LYS B 359      50.621  66.062  27.854  1.00 37.00           N  
-ATOM   5181  CA  LYS B 359      51.348  66.967  26.977  1.00 36.97           C  
-ATOM   5182  C   LYS B 359      52.763  67.156  27.518  1.00 36.19           C  
-ATOM   5183  O   LYS B 359      53.731  67.169  26.758  1.00 34.19           O  
-ATOM   5184  CB  LYS B 359      50.634  68.320  26.915  1.00 38.76           C  
-ATOM   5185  CG  LYS B 359      51.284  69.339  25.990  1.00 40.13           C  
-ATOM   5186  CD  LYS B 359      51.115  68.974  24.522  1.00 41.58           C  
-ATOM   5187  CE  LYS B 359      51.587  70.122  23.633  1.00 44.19           C  
-ATOM   5188  NZ  LYS B 359      51.385  69.859  22.180  1.00 47.32           N  
-ATOM   5189  N   VAL B 360      52.874  67.300  28.836  1.00 34.48           N  
-ATOM   5190  CA  VAL B 360      54.169  67.478  29.469  1.00 35.27           C  
-ATOM   5191  C   VAL B 360      55.050  66.259  29.220  1.00 36.85           C  
-ATOM   5192  O   VAL B 360      56.240  66.394  28.944  1.00 38.29           O  
-ATOM   5193  CB  VAL B 360      54.023  67.703  30.989  1.00 36.35           C  
-ATOM   5194  CG1 VAL B 360      55.386  67.669  31.662  1.00 32.90           C  
-ATOM   5195  CG2 VAL B 360      53.352  69.048  31.248  1.00 36.45           C  
-ATOM   5196  N   LEU B 361      54.466  65.067  29.306  1.00 36.91           N  
-ATOM   5197  CA  LEU B 361      55.226  63.846  29.081  1.00 36.08           C  
-ATOM   5198  C   LEU B 361      55.705  63.749  27.636  1.00 36.69           C  
-ATOM   5199  O   LEU B 361      56.819  63.297  27.374  1.00 38.03           O  
-ATOM   5200  CB  LEU B 361      54.385  62.624  29.447  1.00 36.60           C  
-ATOM   5201  CG  LEU B 361      54.084  62.530  30.944  1.00 38.45           C  
-ATOM   5202  CD1 LEU B 361      53.286  61.272  31.235  1.00 37.75           C  
-ATOM   5203  CD2 LEU B 361      55.394  62.523  31.724  1.00 37.02           C  
-ATOM   5204  N   VAL B 362      54.867  64.172  26.697  1.00 36.04           N  
-ATOM   5205  CA  VAL B 362      55.255  64.139  25.293  1.00 36.20           C  
-ATOM   5206  C   VAL B 362      56.381  65.152  25.070  1.00 36.79           C  
-ATOM   5207  O   VAL B 362      57.397  64.844  24.446  1.00 35.89           O  
-ATOM   5208  CB  VAL B 362      54.069  64.494  24.381  1.00 36.44           C  
-ATOM   5209  CG1 VAL B 362      54.518  64.517  22.933  1.00 36.91           C  
-ATOM   5210  CG2 VAL B 362      52.954  63.485  24.571  1.00 36.59           C  
-ATOM   5211  N   ASP B 363      56.192  66.358  25.598  1.00 35.99           N  
-ATOM   5212  CA  ASP B 363      57.181  67.420  25.479  1.00 37.53           C  
-ATOM   5213  C   ASP B 363      58.531  67.015  26.054  1.00 38.29           C  
-ATOM   5214  O   ASP B 363      59.574  67.298  25.466  1.00 38.14           O  
-ATOM   5215  CB  ASP B 363      56.692  68.676  26.202  1.00 38.54           C  
-ATOM   5216  CG  ASP B 363      55.629  69.422  25.423  1.00 39.40           C  
-ATOM   5217  OD1 ASP B 363      55.029  70.360  25.993  1.00 38.76           O  
-ATOM   5218  OD2 ASP B 363      55.401  69.077  24.240  1.00 39.17           O  
-ATOM   5219  N   ALA B 364      58.508  66.362  27.211  1.00 39.71           N  
-ATOM   5220  CA  ALA B 364      59.732  65.931  27.872  1.00 39.20           C  
-ATOM   5221  C   ALA B 364      60.306  64.682  27.219  1.00 41.08           C  
-ATOM   5222  O   ALA B 364      61.317  64.145  27.671  1.00 40.39           O  
-ATOM   5223  CB  ALA B 364      59.462  65.672  29.346  1.00 41.40           C  
-ATOM   5224  N   GLY B 365      59.648  64.221  26.160  1.00 42.16           N  
-ATOM   5225  CA  GLY B 365      60.109  63.044  25.450  1.00 43.60           C  
-ATOM   5226  C   GLY B 365      59.883  61.725  26.164  1.00 45.50           C  
-ATOM   5227  O   GLY B 365      60.434  60.709  25.753  1.00 46.31           O  
-ATOM   5228  N   TYR B 366      59.081  61.726  27.225  1.00 47.40           N  
-ATOM   5229  CA  TYR B 366      58.814  60.498  27.968  1.00 50.26           C  
-ATOM   5230  C   TYR B 366      57.659  59.692  27.381  1.00 52.24           C  
-ATOM   5231  O   TYR B 366      57.624  58.466  27.489  1.00 52.54           O  
-ATOM   5232  CB  TYR B 366      58.534  60.809  29.443  1.00 51.13           C  
-ATOM   5233  CG  TYR B 366      59.770  61.213  30.219  1.00 54.18           C  
-ATOM   5234  CD1 TYR B 366      60.263  62.514  30.156  1.00 56.13           C  
-ATOM   5235  CD2 TYR B 366      60.468  60.281  30.990  1.00 55.78           C  
-ATOM   5236  CE1 TYR B 366      61.423  62.881  30.842  1.00 57.38           C  
-ATOM   5237  CE2 TYR B 366      61.629  60.635  31.679  1.00 56.36           C  
-ATOM   5238  CZ  TYR B 366      62.101  61.937  31.602  1.00 58.36           C  
-ATOM   5239  OH  TYR B 366      63.249  62.298  32.280  1.00 58.62           O  
-ATOM   5240  N   MET B 367      56.718  60.382  26.752  1.00 54.33           N  
-ATOM   5241  CA  MET B 367      55.574  59.718  26.148  1.00 55.77           C  
-ATOM   5242  C   MET B 367      55.715  59.777  24.634  1.00 55.71           C  
-ATOM   5243  O   MET B 367      56.160  60.784  24.084  1.00 55.71           O  
-ATOM   5244  CB  MET B 367      54.280  60.408  26.583  1.00 56.25           C  
-ATOM   5245  CG  MET B 367      53.013  59.679  26.174  1.00 57.31           C  
-ATOM   5246  SD  MET B 367      51.537  60.531  26.769  1.00 61.12           S  
-ATOM   5247  CE  MET B 367      51.455  59.937  28.466  1.00 57.66           C  
-ATOM   5248  N   ASP B 368      55.346  58.692  23.962  1.00 56.73           N  
-ATOM   5249  CA  ASP B 368      55.437  58.639  22.509  1.00 58.48           C  
-ATOM   5250  C   ASP B 368      54.190  59.255  21.877  1.00 58.97           C  
-ATOM   5251  O   ASP B 368      53.278  59.654  22.636  1.00 58.28           O  
-ATOM   5252  CB  ASP B 368      55.607  57.192  22.047  1.00 58.58           C  
-TER    5253      ASP B 368                                                      
-ATOM   5254  N   ARG C  28      24.051  11.109  67.466  1.00 47.03           N  
-ATOM   5255  CA  ARG C  28      23.746  10.424  66.171  1.00 48.37           C  
-ATOM   5256  C   ARG C  28      24.425  11.146  65.003  1.00 46.46           C  
-ATOM   5257  O   ARG C  28      24.148  12.317  64.745  1.00 46.61           O  
-ATOM   5258  CB  ARG C  28      22.229  10.381  65.954  1.00 48.20           C  
-ATOM   5259  CG  ARG C  28      21.776   9.428  64.858  1.00 50.93           C  
-ATOM   5260  CD  ARG C  28      20.263   9.241  64.889  1.00 51.40           C  
-ATOM   5261  NE  ARG C  28      19.557  10.512  64.728  1.00 54.21           N  
-ATOM   5262  CZ  ARG C  28      18.235  10.652  64.801  1.00 53.90           C  
-ATOM   5263  NH1 ARG C  28      17.466   9.596  65.035  1.00 53.39           N  
-ATOM   5264  NH2 ARG C  28      17.680  11.848  64.639  1.00 52.47           N  
-ATOM   5265  N   LYS C  29      25.317  10.444  64.307  1.00 45.61           N  
-ATOM   5266  CA  LYS C  29      26.038  11.021  63.173  1.00 46.12           C  
-ATOM   5267  C   LYS C  29      25.113  11.478  62.051  1.00 45.13           C  
-ATOM   5268  O   LYS C  29      24.062  10.881  61.809  1.00 44.39           O  
-ATOM   5269  CB  LYS C  29      27.030  10.014  62.590  1.00 46.19           C  
-ATOM   5270  CG  LYS C  29      28.263   9.736  63.433  1.00 49.51           C  
-ATOM   5271  CD  LYS C  29      29.184   8.795  62.665  1.00 51.69           C  
-ATOM   5272  CE  LYS C  29      30.422   8.398  63.441  1.00 53.26           C  
-ATOM   5273  NZ  LYS C  29      31.248   7.448  62.638  1.00 53.12           N  
-ATOM   5274  N   ILE C  30      25.522  12.538  61.361  1.00 44.43           N  
-ATOM   5275  CA  ILE C  30      24.746  13.076  60.252  1.00 42.03           C  
-ATOM   5276  C   ILE C  30      25.579  13.060  58.978  1.00 40.51           C  
-ATOM   5277  O   ILE C  30      26.655  13.655  58.910  1.00 39.77           O  
-ATOM   5278  CB  ILE C  30      24.289  14.519  60.532  1.00 41.54           C  
-ATOM   5279  CG1 ILE C  30      23.536  14.574  61.864  1.00 41.95           C  
-ATOM   5280  CG2 ILE C  30      23.385  15.001  59.405  1.00 40.96           C  
-ATOM   5281  CD1 ILE C  30      23.021  15.943  62.229  1.00 39.86           C  
-ATOM   5282  N   ALA C  31      25.075  12.365  57.969  1.00 39.97           N  
-ATOM   5283  CA  ALA C  31      25.764  12.268  56.696  1.00 39.16           C  
-ATOM   5284  C   ALA C  31      24.977  12.986  55.605  1.00 39.07           C  
-ATOM   5285  O   ALA C  31      23.758  12.851  55.518  1.00 40.28           O  
-ATOM   5286  CB  ALA C  31      25.948  10.809  56.323  1.00 38.06           C  
-ATOM   5287  N   LEU C  32      25.679  13.767  54.790  1.00 37.48           N  
-ATOM   5288  CA  LEU C  32      25.053  14.466  53.676  1.00 35.23           C  
-ATOM   5289  C   LEU C  32      25.578  13.791  52.421  1.00 34.17           C  
-ATOM   5290  O   LEU C  32      26.788  13.757  52.186  1.00 32.78           O  
-ATOM   5291  CB  LEU C  32      25.434  15.947  53.657  1.00 36.24           C  
-ATOM   5292  CG  LEU C  32      24.922  16.738  52.444  1.00 37.47           C  
-ATOM   5293  CD1 LEU C  32      23.418  16.544  52.286  1.00 36.49           C  
-ATOM   5294  CD2 LEU C  32      25.251  18.208  52.616  1.00 35.33           C  
-ATOM   5295  N   ILE C  33      24.670  13.238  51.627  1.00 32.16           N  
-ATOM   5296  CA  ILE C  33      25.055  12.557  50.402  1.00 30.43           C  
-ATOM   5297  C   ILE C  33      24.575  13.291  49.150  1.00 30.66           C  
-ATOM   5298  O   ILE C  33      23.376  13.522  48.990  1.00 30.17           O  
-ATOM   5299  CB  ILE C  33      24.468  11.130  50.349  1.00 29.25           C  
-ATOM   5300  CG1 ILE C  33      24.858  10.348  51.606  1.00 28.76           C  
-ATOM   5301  CG2 ILE C  33      24.967  10.406  49.100  1.00 26.27           C  
-ATOM   5302  CD1 ILE C  33      24.224   8.976  51.684  1.00 30.78           C  
-ATOM   5303  N   THR C  34      25.509  13.671  48.281  1.00 28.71           N  
-ATOM   5304  CA  THR C  34      25.142  14.307  47.017  1.00 27.84           C  
-ATOM   5305  C   THR C  34      25.042  13.126  46.057  1.00 26.65           C  
-ATOM   5306  O   THR C  34      25.804  12.162  46.183  1.00 26.67           O  
-ATOM   5307  CB  THR C  34      26.224  15.279  46.477  1.00 24.43           C  
-ATOM   5308  OG1 THR C  34      27.358  14.534  46.025  1.00 26.78           O  
-ATOM   5309  CG2 THR C  34      26.655  16.254  47.543  1.00 26.38           C  
-ATOM   5310  N   GLY C  35      24.112  13.192  45.109  1.00 25.59           N  
-ATOM   5311  CA  GLY C  35      23.944  12.099  44.165  1.00 25.46           C  
-ATOM   5312  C   GLY C  35      23.330  10.892  44.852  1.00 25.12           C  
-ATOM   5313  O   GLY C  35      23.621   9.744  44.517  1.00 24.50           O  
-ATOM   5314  N   ILE C  36      22.462  11.163  45.819  1.00 27.64           N  
-ATOM   5315  CA  ILE C  36      21.811  10.116  46.588  1.00 27.97           C  
-ATOM   5316  C   ILE C  36      20.817   9.287  45.770  1.00 29.26           C  
-ATOM   5317  O   ILE C  36      20.554   8.136  46.107  1.00 30.43           O  
-ATOM   5318  CB  ILE C  36      21.099  10.720  47.828  1.00 27.76           C  
-ATOM   5319  CG1 ILE C  36      20.610   9.598  48.749  1.00 28.83           C  
-ATOM   5320  CG2 ILE C  36      19.944  11.610  47.390  1.00 26.69           C  
-ATOM   5321  CD1 ILE C  36      19.980  10.101  50.052  1.00 27.68           C  
-ATOM   5322  N   THR C  37      20.278   9.859  44.693  1.00 28.95           N  
-ATOM   5323  CA  THR C  37      19.319   9.136  43.852  1.00 26.54           C  
-ATOM   5324  C   THR C  37      20.005   8.119  42.939  1.00 27.42           C  
-ATOM   5325  O   THR C  37      19.352   7.229  42.387  1.00 27.06           O  
-ATOM   5326  CB  THR C  37      18.483  10.104  42.963  1.00 26.72           C  
-ATOM   5327  OG1 THR C  37      19.358  10.881  42.132  1.00 24.34           O  
-ATOM   5328  CG2 THR C  37      17.639  11.038  43.827  1.00 23.55           C  
-ATOM   5329  N   GLY C  38      21.320   8.248  42.782  1.00 26.45           N  
-ATOM   5330  CA  GLY C  38      22.053   7.328  41.927  1.00 24.81           C  
-ATOM   5331  C   GLY C  38      22.235   5.949  42.538  1.00 26.06           C  
-ATOM   5332  O   GLY C  38      21.811   5.701  43.668  1.00 25.99           O  
-ATOM   5333  N   GLN C  39      22.864   5.047  41.790  1.00 27.26           N  
-ATOM   5334  CA  GLN C  39      23.105   3.682  42.259  1.00 28.70           C  
-ATOM   5335  C   GLN C  39      23.761   3.667  43.640  1.00 31.04           C  
-ATOM   5336  O   GLN C  39      23.149   3.250  44.626  1.00 31.33           O  
-ATOM   5337  CB  GLN C  39      24.000   2.928  41.268  1.00 27.38           C  
-ATOM   5338  CG  GLN C  39      24.377   1.516  41.713  1.00 29.04           C  
-ATOM   5339  CD  GLN C  39      25.363   0.846  40.773  1.00 29.51           C  
-ATOM   5340  OE1 GLN C  39      25.062  -0.181  40.167  1.00 32.96           O  
-ATOM   5341  NE2 GLN C  39      26.550   1.430  40.645  1.00 29.27           N  
-ATOM   5342  N   ASP C  40      25.005   4.131  43.700  1.00 30.75           N  
-ATOM   5343  CA  ASP C  40      25.765   4.169  44.941  1.00 31.35           C  
-ATOM   5344  C   ASP C  40      25.035   4.900  46.063  1.00 31.61           C  
-ATOM   5345  O   ASP C  40      25.047   4.462  47.215  1.00 29.77           O  
-ATOM   5346  CB  ASP C  40      27.118   4.827  44.685  1.00 31.86           C  
-ATOM   5347  CG  ASP C  40      28.007   3.989  43.792  1.00 31.88           C  
-ATOM   5348  OD1 ASP C  40      27.493   3.043  43.159  1.00 31.52           O  
-ATOM   5349  OD2 ASP C  40      29.218   4.279  43.721  1.00 32.71           O  
-ATOM   5350  N   GLY C  41      24.396   6.013  45.721  1.00 31.60           N  
-ATOM   5351  CA  GLY C  41      23.672   6.777  46.719  1.00 31.49           C  
-ATOM   5352  C   GLY C  41      22.624   5.960  47.455  1.00 30.85           C  
-ATOM   5353  O   GLY C  41      22.486   6.083  48.669  1.00 29.44           O  
-ATOM   5354  N   SER C  42      21.884   5.131  46.722  1.00 31.32           N  
-ATOM   5355  CA  SER C  42      20.834   4.305  47.316  1.00 32.73           C  
-ATOM   5356  C   SER C  42      21.416   3.261  48.266  1.00 33.66           C  
-ATOM   5357  O   SER C  42      20.916   3.078  49.373  1.00 35.46           O  
-ATOM   5358  CB  SER C  42      20.012   3.612  46.226  1.00 30.22           C  
-ATOM   5359  OG  SER C  42      20.815   2.739  45.453  1.00 29.53           O  
-ATOM   5360  N   TYR C  43      22.466   2.573  47.835  1.00 33.89           N  
-ATOM   5361  CA  TYR C  43      23.098   1.580  48.692  1.00 33.54           C  
-ATOM   5362  C   TYR C  43      23.732   2.242  49.909  1.00 34.38           C  
-ATOM   5363  O   TYR C  43      23.468   1.834  51.041  1.00 34.97           O  
-ATOM   5364  CB  TYR C  43      24.153   0.788  47.923  1.00 31.50           C  
-ATOM   5365  CG  TYR C  43      23.561  -0.261  47.018  1.00 33.32           C  
-ATOM   5366  CD1 TYR C  43      23.547  -0.094  45.630  1.00 32.19           C  
-ATOM   5367  CD2 TYR C  43      22.989  -1.419  47.550  1.00 32.52           C  
-ATOM   5368  CE1 TYR C  43      22.980  -1.056  44.799  1.00 31.97           C  
-ATOM   5369  CE2 TYR C  43      22.418  -2.382  46.729  1.00 32.05           C  
-ATOM   5370  CZ  TYR C  43      22.416  -2.199  45.357  1.00 34.47           C  
-ATOM   5371  OH  TYR C  43      21.850  -3.164  44.547  1.00 35.74           O  
-ATOM   5372  N   LEU C  44      24.554   3.266  49.681  1.00 33.18           N  
-ATOM   5373  CA  LEU C  44      25.210   3.962  50.784  1.00 33.71           C  
-ATOM   5374  C   LEU C  44      24.205   4.451  51.828  1.00 34.63           C  
-ATOM   5375  O   LEU C  44      24.486   4.424  53.025  1.00 36.22           O  
-ATOM   5376  CB  LEU C  44      26.029   5.153  50.266  1.00 32.57           C  
-ATOM   5377  CG  LEU C  44      26.785   5.953  51.337  1.00 33.48           C  
-ATOM   5378  CD1 LEU C  44      27.809   5.050  52.008  1.00 31.64           C  
-ATOM   5379  CD2 LEU C  44      27.472   7.161  50.716  1.00 32.44           C  
-ATOM   5380  N   THR C  45      23.037   4.897  51.377  1.00 34.74           N  
-ATOM   5381  CA  THR C  45      22.013   5.383  52.295  1.00 35.60           C  
-ATOM   5382  C   THR C  45      21.529   4.260  53.211  1.00 37.43           C  
-ATOM   5383  O   THR C  45      21.370   4.456  54.418  1.00 35.52           O  
-ATOM   5384  CB  THR C  45      20.798   5.959  51.537  1.00 35.57           C  
-ATOM   5385  OG1 THR C  45      21.196   7.129  50.810  1.00 35.00           O  
-ATOM   5386  CG2 THR C  45      19.682   6.328  52.516  1.00 33.78           C  
-ATOM   5387  N   GLU C  46      21.282   3.090  52.627  1.00 37.38           N  
-ATOM   5388  CA  GLU C  46      20.826   1.939  53.397  1.00 39.26           C  
-ATOM   5389  C   GLU C  46      21.911   1.556  54.407  1.00 39.55           C  
-ATOM   5390  O   GLU C  46      21.637   1.388  55.594  1.00 38.36           O  
-ATOM   5391  CB  GLU C  46      20.525   0.761  52.461  1.00 38.55           C  
-ATOM   5392  CG  GLU C  46      19.401   1.042  51.466  1.00 38.74           C  
-ATOM   5393  CD  GLU C  46      19.188  -0.083  50.465  1.00 38.92           C  
-ATOM   5394  OE1 GLU C  46      20.145  -0.447  49.748  1.00 41.02           O  
-ATOM   5395  OE2 GLU C  46      18.057  -0.602  50.388  1.00 41.11           O  
-ATOM   5396  N   PHE C  47      23.146   1.444  53.925  1.00 40.27           N  
-ATOM   5397  CA  PHE C  47      24.281   1.087  54.768  1.00 40.51           C  
-ATOM   5398  C   PHE C  47      24.438   2.025  55.959  1.00 40.88           C  
-ATOM   5399  O   PHE C  47      24.629   1.576  57.091  1.00 43.26           O  
-ATOM   5400  CB  PHE C  47      25.574   1.105  53.951  1.00 40.75           C  
-ATOM   5401  CG  PHE C  47      26.777   0.637  54.719  1.00 41.33           C  
-ATOM   5402  CD1 PHE C  47      26.972  -0.717  54.973  1.00 40.99           C  
-ATOM   5403  CD2 PHE C  47      27.700   1.552  55.216  1.00 41.47           C  
-ATOM   5404  CE1 PHE C  47      28.070  -1.154  55.713  1.00 42.17           C  
-ATOM   5405  CE2 PHE C  47      28.803   1.125  55.958  1.00 41.31           C  
-ATOM   5406  CZ  PHE C  47      28.989  -0.229  56.207  1.00 41.23           C  
-ATOM   5407  N   LEU C  48      24.367   3.327  55.707  1.00 39.76           N  
-ATOM   5408  CA  LEU C  48      24.517   4.305  56.777  1.00 39.35           C  
-ATOM   5409  C   LEU C  48      23.350   4.286  57.760  1.00 39.33           C  
-ATOM   5410  O   LEU C  48      23.543   4.486  58.958  1.00 39.05           O  
-ATOM   5411  CB  LEU C  48      24.703   5.713  56.195  1.00 38.42           C  
-ATOM   5412  CG  LEU C  48      26.059   5.959  55.520  1.00 39.11           C  
-ATOM   5413  CD1 LEU C  48      26.107   7.357  54.913  1.00 38.19           C  
-ATOM   5414  CD2 LEU C  48      27.168   5.786  56.545  1.00 37.95           C  
-ATOM   5415  N   LEU C  49      22.140   4.061  57.261  1.00 40.06           N  
-ATOM   5416  CA  LEU C  49      20.978   4.000  58.143  1.00 41.18           C  
-ATOM   5417  C   LEU C  49      21.155   2.797  59.063  1.00 41.88           C  
-ATOM   5418  O   LEU C  49      20.839   2.857  60.250  1.00 41.76           O  
-ATOM   5419  CB  LEU C  49      19.683   3.857  57.334  1.00 40.11           C  
-ATOM   5420  CG  LEU C  49      19.167   5.127  56.647  1.00 39.30           C  
-ATOM   5421  CD1 LEU C  49      17.948   4.796  55.803  1.00 38.87           C  
-ATOM   5422  CD2 LEU C  49      18.823   6.173  57.695  1.00 36.30           C  
-ATOM   5423  N   GLY C  50      21.679   1.712  58.502  1.00 42.28           N  
-ATOM   5424  CA  GLY C  50      21.910   0.512  59.282  1.00 44.42           C  
-ATOM   5425  C   GLY C  50      22.921   0.757  60.387  1.00 45.26           C  
-ATOM   5426  O   GLY C  50      23.028  -0.035  61.320  1.00 46.93           O  
-ATOM   5427  N   LYS C  51      23.665   1.854  60.279  1.00 44.58           N  
-ATOM   5428  CA  LYS C  51      24.666   2.210  61.277  1.00 44.53           C  
-ATOM   5429  C   LYS C  51      24.111   3.281  62.207  1.00 43.75           C  
-ATOM   5430  O   LYS C  51      24.843   3.850  63.017  1.00 44.95           O  
-ATOM   5431  CB  LYS C  51      25.932   2.736  60.600  1.00 45.90           C  
-ATOM   5432  CG  LYS C  51      26.640   1.731  59.704  1.00 47.09           C  
-ATOM   5433  CD  LYS C  51      27.394   0.700  60.516  1.00 48.73           C  
-ATOM   5434  CE  LYS C  51      28.258  -0.172  59.623  1.00 49.23           C  
-ATOM   5435  NZ  LYS C  51      29.150  -1.058  60.416  1.00 49.17           N  
-ATOM   5436  N   GLY C  52      22.818   3.561  62.077  1.00 42.86           N  
-ATOM   5437  CA  GLY C  52      22.183   4.553  62.928  1.00 41.55           C  
-ATOM   5438  C   GLY C  52      22.407   6.000  62.527  1.00 41.01           C  
-ATOM   5439  O   GLY C  52      22.201   6.908  63.330  1.00 40.68           O  
-ATOM   5440  N   TYR C  53      22.827   6.224  61.288  1.00 40.71           N  
-ATOM   5441  CA  TYR C  53      23.059   7.582  60.806  1.00 40.01           C  
-ATOM   5442  C   TYR C  53      21.774   8.316  60.455  1.00 39.81           C  
-ATOM   5443  O   TYR C  53      20.739   7.706  60.189  1.00 39.54           O  
-ATOM   5444  CB  TYR C  53      23.913   7.577  59.537  1.00 40.44           C  
-ATOM   5445  CG  TYR C  53      25.406   7.500  59.725  1.00 39.46           C  
-ATOM   5446  CD1 TYR C  53      26.032   6.296  60.036  1.00 41.51           C  
-ATOM   5447  CD2 TYR C  53      26.203   8.623  59.516  1.00 39.52           C  
-ATOM   5448  CE1 TYR C  53      27.426   6.213  60.123  1.00 42.05           C  
-ATOM   5449  CE2 TYR C  53      27.585   8.553  59.602  1.00 40.74           C  
-ATOM   5450  CZ  TYR C  53      28.192   7.348  59.902  1.00 41.17           C  
-ATOM   5451  OH  TYR C  53      29.565   7.283  59.960  1.00 43.22           O  
-ATOM   5452  N   GLU C  54      21.859   9.640  60.466  1.00 40.00           N  
-ATOM   5453  CA  GLU C  54      20.754  10.493  60.056  1.00 39.93           C  
-ATOM   5454  C   GLU C  54      21.266  10.854  58.662  1.00 39.62           C  
-ATOM   5455  O   GLU C  54      22.308  11.499  58.527  1.00 39.14           O  
-ATOM   5456  CB  GLU C  54      20.660  11.746  60.935  1.00 40.81           C  
-ATOM   5457  CG  GLU C  54      19.645  12.779  60.450  1.00 42.39           C  
-ATOM   5458  CD  GLU C  54      19.542  13.989  61.372  1.00 44.58           C  
-ATOM   5459  OE1 GLU C  54      18.943  15.010  60.962  1.00 41.97           O  
-ATOM   5460  OE2 GLU C  54      20.055  13.918  62.511  1.00 48.02           O  
-ATOM   5461  N   VAL C  55      20.563  10.409  57.628  1.00 38.28           N  
-ATOM   5462  CA  VAL C  55      21.009  10.671  56.268  1.00 38.18           C  
-ATOM   5463  C   VAL C  55      20.235  11.751  55.526  1.00 37.10           C  
-ATOM   5464  O   VAL C  55      19.007  11.720  55.444  1.00 36.96           O  
-ATOM   5465  CB  VAL C  55      20.979   9.376  55.425  1.00 38.90           C  
-ATOM   5466  CG1 VAL C  55      21.530   9.640  54.035  1.00 37.76           C  
-ATOM   5467  CG2 VAL C  55      21.787   8.290  56.121  1.00 38.71           C  
-ATOM   5468  N   HIS C  56      20.980  12.711  54.994  1.00 36.53           N  
-ATOM   5469  CA  HIS C  56      20.417  13.805  54.217  1.00 35.73           C  
-ATOM   5470  C   HIS C  56      20.977  13.669  52.805  1.00 34.67           C  
-ATOM   5471  O   HIS C  56      22.167  13.398  52.620  1.00 32.85           O  
-ATOM   5472  CB  HIS C  56      20.831  15.155  54.806  1.00 35.50           C  
-ATOM   5473  CG  HIS C  56      20.093  15.525  56.054  1.00 38.45           C  
-ATOM   5474  ND1 HIS C  56      18.924  16.254  56.038  1.00 38.81           N  
-ATOM   5475  CD2 HIS C  56      20.355  15.262  57.357  1.00 37.29           C  
-ATOM   5476  CE1 HIS C  56      18.498  16.427  57.277  1.00 38.75           C  
-ATOM   5477  NE2 HIS C  56      19.349  15.834  58.096  1.00 37.86           N  
-ATOM   5478  N   GLY C  57      20.115  13.841  51.811  1.00 33.83           N  
-ATOM   5479  CA  GLY C  57      20.558  13.743  50.435  1.00 32.10           C  
-ATOM   5480  C   GLY C  57      20.166  14.972  49.644  1.00 30.99           C  
-ATOM   5481  O   GLY C  57      19.156  15.609  49.930  1.00 30.07           O  
-ATOM   5482  N   LEU C  58      20.977  15.328  48.658  1.00 30.03           N  
-ATOM   5483  CA  LEU C  58      20.667  16.480  47.829  1.00 29.36           C  
-ATOM   5484  C   LEU C  58      20.153  15.923  46.515  1.00 30.13           C  
-ATOM   5485  O   LEU C  58      20.804  15.076  45.903  1.00 32.70           O  
-ATOM   5486  CB  LEU C  58      21.920  17.326  47.587  1.00 29.03           C  
-ATOM   5487  CG  LEU C  58      22.684  17.814  48.821  1.00 26.94           C  
-ATOM   5488  CD1 LEU C  58      23.867  18.647  48.373  1.00 31.02           C  
-ATOM   5489  CD2 LEU C  58      21.773  18.629  49.724  1.00 27.33           C  
-ATOM   5490  N   ILE C  59      18.982  16.382  46.088  1.00 29.27           N  
-ATOM   5491  CA  ILE C  59      18.402  15.904  44.839  1.00 29.41           C  
-ATOM   5492  C   ILE C  59      18.082  17.036  43.863  1.00 28.65           C  
-ATOM   5493  O   ILE C  59      17.826  18.172  44.263  1.00 27.54           O  
-ATOM   5494  CB  ILE C  59      17.103  15.102  45.089  1.00 29.36           C  
-ATOM   5495  CG1 ILE C  59      16.009  16.020  45.634  1.00 29.56           C  
-ATOM   5496  CG2 ILE C  59      17.364  13.980  46.084  1.00 31.70           C  
-ATOM   5497  CD1 ILE C  59      14.649  15.349  45.717  1.00 31.28           C  
-ATOM   5498  N   ARG C  60      18.104  16.711  42.578  1.00 27.80           N  
-ATOM   5499  CA  ARG C  60      17.799  17.684  41.546  1.00 26.29           C  
-ATOM   5500  C   ARG C  60      16.300  17.729  41.314  1.00 26.18           C  
-ATOM   5501  O   ARG C  60      15.608  16.719  41.439  1.00 27.36           O  
-ATOM   5502  CB  ARG C  60      18.463  17.312  40.217  1.00 26.10           C  
-ATOM   5503  CG  ARG C  60      19.969  17.402  40.185  1.00 24.69           C  
-ATOM   5504  CD  ARG C  60      20.456  17.377  38.746  1.00 24.91           C  
-ATOM   5505  NE  ARG C  60      20.175  16.115  38.062  1.00 22.68           N  
-ATOM   5506  CZ  ARG C  60      20.420  15.904  36.771  1.00 21.43           C  
-ATOM   5507  NH1 ARG C  60      20.943  16.875  36.035  1.00 21.23           N  
-ATOM   5508  NH2 ARG C  60      20.156  14.723  36.215  1.00 19.18           N  
-ATOM   5509  N   ARG C  61      15.796  18.908  40.989  1.00 24.59           N  
-ATOM   5510  CA  ARG C  61      14.390  19.035  40.682  1.00 24.64           C  
-ATOM   5511  C   ARG C  61      14.264  18.464  39.263  1.00 24.30           C  
-ATOM   5512  O   ARG C  61      15.132  18.692  38.422  1.00 19.80           O  
-ATOM   5513  CB  ARG C  61      13.976  20.509  40.698  1.00 23.83           C  
-ATOM   5514  CG  ARG C  61      12.487  20.744  40.449  1.00 27.10           C  
-ATOM   5515  CD  ARG C  61      12.119  20.690  38.968  1.00 25.81           C  
-ATOM   5516  NE  ARG C  61      10.675  20.593  38.788  1.00 28.01           N  
-ATOM   5517  CZ  ARG C  61      10.043  20.787  37.634  1.00 29.22           C  
-ATOM   5518  NH1 ARG C  61      10.720  21.100  36.535  1.00 29.04           N  
-ATOM   5519  NH2 ARG C  61       8.728  20.652  37.577  1.00 28.92           N  
-ATOM   5520  N   SER C  62      13.204  17.708  39.003  1.00 25.99           N  
-ATOM   5521  CA  SER C  62      12.991  17.147  37.672  1.00 26.64           C  
-ATOM   5522  C   SER C  62      11.502  17.100  37.384  1.00 25.04           C  
-ATOM   5523  O   SER C  62      10.697  17.020  38.307  1.00 23.56           O  
-ATOM   5524  CB  SER C  62      13.591  15.743  37.568  1.00 30.50           C  
-ATOM   5525  OG  SER C  62      12.908  14.836  38.410  1.00 37.40           O  
-ATOM   5526  N   SER C  63      11.137  17.159  36.105  1.00 25.00           N  
-ATOM   5527  CA  SER C  63       9.732  17.136  35.716  1.00 26.23           C  
-ATOM   5528  C   SER C  63       9.116  15.753  35.951  1.00 27.44           C  
-ATOM   5529  O   SER C  63       7.894  15.594  35.925  1.00 27.35           O  
-ATOM   5530  CB  SER C  63       9.582  17.537  34.242  1.00 26.10           C  
-ATOM   5531  OG  SER C  63      10.095  16.534  33.382  1.00 24.69           O  
-ATOM   5532  N   ASN C  64       9.970  14.762  36.187  1.00 28.37           N  
-ATOM   5533  CA  ASN C  64       9.519  13.399  36.441  1.00 31.01           C  
-ATOM   5534  C   ASN C  64      10.043  12.839  37.748  1.00 32.34           C  
-ATOM   5535  O   ASN C  64      10.941  13.400  38.367  1.00 33.96           O  
-ATOM   5536  CB  ASN C  64       9.965  12.464  35.319  1.00 29.92           C  
-ATOM   5537  CG  ASN C  64       9.059  12.522  34.127  1.00 29.26           C  
-ATOM   5538  OD1 ASN C  64       7.858  12.260  34.237  1.00 31.84           O  
-ATOM   5539  ND2 ASN C  64       9.620  12.859  32.973  1.00 27.87           N  
-ATOM   5540  N   PHE C  65       9.460  11.717  38.148  1.00 34.66           N  
-ATOM   5541  CA  PHE C  65       9.841  10.987  39.353  1.00 36.83           C  
-ATOM   5542  C   PHE C  65      11.335  10.670  39.174  1.00 35.78           C  
-ATOM   5543  O   PHE C  65      11.743  10.237  38.094  1.00 36.64           O  
-ATOM   5544  CB  PHE C  65       8.991   9.703  39.400  1.00 39.98           C  
-ATOM   5545  CG  PHE C  65       9.184   8.858  40.629  1.00 45.07           C  
-ATOM   5546  CD1 PHE C  65       9.065   9.405  41.905  1.00 47.43           C  
-ATOM   5547  CD2 PHE C  65       9.429   7.488  40.506  1.00 46.07           C  
-ATOM   5548  CE1 PHE C  65       9.187   8.596  43.044  1.00 46.82           C  
-ATOM   5549  CE2 PHE C  65       9.551   6.675  41.632  1.00 46.09           C  
-ATOM   5550  CZ  PHE C  65       9.430   7.231  42.904  1.00 47.43           C  
-ATOM   5551  N   ASN C  66      12.155  10.905  40.197  1.00 34.63           N  
-ATOM   5552  CA  ASN C  66      13.586  10.616  40.074  1.00 35.18           C  
-ATOM   5553  C   ASN C  66      14.180   9.932  41.302  1.00 35.31           C  
-ATOM   5554  O   ASN C  66      15.401   9.845  41.445  1.00 35.52           O  
-ATOM   5555  CB  ASN C  66      14.363  11.899  39.780  1.00 36.77           C  
-ATOM   5556  CG  ASN C  66      14.435  12.823  40.976  1.00 40.43           C  
-ATOM   5557  OD1 ASN C  66      13.492  12.911  41.765  1.00 42.69           O  
-ATOM   5558  ND2 ASN C  66      15.550  13.531  41.109  1.00 40.18           N  
-ATOM   5559  N   THR C  67      13.313   9.438  42.179  1.00 34.20           N  
-ATOM   5560  CA  THR C  67      13.753   8.764  43.393  1.00 33.11           C  
-ATOM   5561  C   THR C  67      13.412   7.277  43.373  1.00 32.76           C  
-ATOM   5562  O   THR C  67      13.153   6.677  44.414  1.00 32.73           O  
-ATOM   5563  CB  THR C  67      13.105   9.398  44.634  1.00 33.61           C  
-ATOM   5564  OG1 THR C  67      11.684   9.466  44.448  1.00 34.84           O  
-ATOM   5565  CG2 THR C  67      13.653  10.797  44.868  1.00 33.75           C  
-ATOM   5566  N   GLN C  68      13.424   6.684  42.186  1.00 31.57           N  
-ATOM   5567  CA  GLN C  68      13.106   5.271  42.037  1.00 31.19           C  
-ATOM   5568  C   GLN C  68      13.940   4.342  42.909  1.00 31.94           C  
-ATOM   5569  O   GLN C  68      13.413   3.382  43.470  1.00 33.63           O  
-ATOM   5570  CB  GLN C  68      13.243   4.840  40.572  1.00 29.01           C  
-ATOM   5571  CG  GLN C  68      12.213   5.462  39.647  1.00 31.55           C  
-ATOM   5572  CD  GLN C  68      12.634   6.821  39.113  1.00 35.26           C  
-ATOM   5573  OE1 GLN C  68      13.293   7.599  39.802  1.00 32.55           O  
-ATOM   5574  NE2 GLN C  68      12.241   7.114  37.876  1.00 35.11           N  
-ATOM   5575  N   ARG C  69      15.236   4.622  43.027  1.00 31.72           N  
-ATOM   5576  CA  ARG C  69      16.130   3.776  43.819  1.00 31.73           C  
-ATOM   5577  C   ARG C  69      16.027   3.920  45.333  1.00 32.04           C  
-ATOM   5578  O   ARG C  69      16.442   3.021  46.067  1.00 32.79           O  
-ATOM   5579  CB  ARG C  69      17.591   4.018  43.429  1.00 31.05           C  
-ATOM   5580  CG  ARG C  69      17.946   3.674  41.997  1.00 30.64           C  
-ATOM   5581  CD  ARG C  69      19.452   3.708  41.789  1.00 28.43           C  
-ATOM   5582  NE  ARG C  69      19.795   3.572  40.378  1.00 31.53           N  
-ATOM   5583  CZ  ARG C  69      19.836   4.584  39.516  1.00 30.91           C  
-ATOM   5584  NH1 ARG C  69      20.149   4.361  38.248  1.00 28.79           N  
-ATOM   5585  NH2 ARG C  69      19.584   5.819  39.925  1.00 27.36           N  
-ATOM   5586  N   ILE C  70      15.481   5.031  45.813  1.00 32.16           N  
-ATOM   5587  CA  ILE C  70      15.407   5.240  47.253  1.00 34.74           C  
-ATOM   5588  C   ILE C  70      14.016   5.366  47.846  1.00 36.08           C  
-ATOM   5589  O   ILE C  70      13.868   5.465  49.064  1.00 36.23           O  
-ATOM   5590  CB  ILE C  70      16.205   6.488  47.660  1.00 33.74           C  
-ATOM   5591  CG1 ILE C  70      15.652   7.714  46.932  1.00 33.57           C  
-ATOM   5592  CG2 ILE C  70      17.672   6.288  47.335  1.00 34.32           C  
-ATOM   5593  CD1 ILE C  70      16.298   9.011  47.355  1.00 32.96           C  
-ATOM   5594  N   ASN C  71      12.999   5.356  46.995  1.00 37.55           N  
-ATOM   5595  CA  ASN C  71      11.632   5.487  47.469  1.00 41.26           C  
-ATOM   5596  C   ASN C  71      11.249   4.424  48.499  1.00 41.89           C  
-ATOM   5597  O   ASN C  71      10.492   4.703  49.428  1.00 41.57           O  
-ATOM   5598  CB  ASN C  71      10.663   5.447  46.285  1.00 44.43           C  
-ATOM   5599  CG  ASN C  71       9.237   5.736  46.697  1.00 48.13           C  
-ATOM   5600  OD1 ASN C  71       8.518   4.848  47.160  1.00 50.84           O  
-ATOM   5601  ND2 ASN C  71       8.823   6.989  46.550  1.00 49.98           N  
-ATOM   5602  N   HIS C  72      11.785   3.216  48.338  1.00 42.99           N  
-ATOM   5603  CA  HIS C  72      11.502   2.110  49.250  1.00 44.85           C  
-ATOM   5604  C   HIS C  72      12.138   2.302  50.626  1.00 46.60           C  
-ATOM   5605  O   HIS C  72      11.663   1.744  51.616  1.00 46.38           O  
-ATOM   5606  CB  HIS C  72      12.020   0.794  48.675  1.00 44.31           C  
-ATOM   5607  CG  HIS C  72      13.509   0.660  48.734  1.00 44.23           C  
-ATOM   5608  ND1 HIS C  72      14.354   1.351  47.892  1.00 45.20           N  
-ATOM   5609  CD2 HIS C  72      14.306  -0.066  49.554  1.00 45.07           C  
-ATOM   5610  CE1 HIS C  72      15.608   1.053  48.187  1.00 45.97           C  
-ATOM   5611  NE2 HIS C  72      15.606   0.195  49.193  1.00 46.02           N  
-ATOM   5612  N   ILE C  73      13.221   3.074  50.682  1.00 47.17           N  
-ATOM   5613  CA  ILE C  73      13.917   3.313  51.941  1.00 47.17           C  
-ATOM   5614  C   ILE C  73      12.986   3.921  52.985  1.00 49.29           C  
-ATOM   5615  O   ILE C  73      13.321   3.989  54.166  1.00 50.41           O  
-ATOM   5616  CB  ILE C  73      15.154   4.213  51.724  1.00 46.59           C  
-ATOM   5617  CG1 ILE C  73      16.178   3.463  50.863  1.00 46.44           C  
-ATOM   5618  CG2 ILE C  73      15.786   4.588  53.056  1.00 46.32           C  
-ATOM   5619  CD1 ILE C  73      17.408   4.276  50.490  1.00 45.91           C  
-ATOM   5620  N   TYR C  74      11.809   4.353  52.551  1.00 50.37           N  
-ATOM   5621  CA  TYR C  74      10.840   4.916  53.479  1.00 52.41           C  
-ATOM   5622  C   TYR C  74      10.132   3.790  54.245  1.00 53.68           C  
-ATOM   5623  O   TYR C  74      10.049   3.820  55.473  1.00 53.86           O  
-ATOM   5624  CB  TYR C  74       9.816   5.763  52.726  1.00 52.58           C  
-ATOM   5625  CG  TYR C  74      10.375   7.048  52.160  1.00 53.82           C  
-ATOM   5626  CD1 TYR C  74      10.923   8.022  52.996  1.00 54.18           C  
-ATOM   5627  CD2 TYR C  74      10.325   7.309  50.789  1.00 54.14           C  
-ATOM   5628  CE1 TYR C  74      11.403   9.230  52.480  1.00 54.65           C  
-ATOM   5629  CE2 TYR C  74      10.801   8.509  50.264  1.00 53.99           C  
-ATOM   5630  CZ  TYR C  74      11.335   9.465  51.113  1.00 55.03           C  
-ATOM   5631  OH  TYR C  74      11.779  10.661  50.598  1.00 54.91           O  
-ATOM   5632  N   ILE C  75       9.631   2.794  53.518  1.00 54.29           N  
-ATOM   5633  CA  ILE C  75       8.941   1.665  54.140  1.00 54.40           C  
-ATOM   5634  C   ILE C  75       9.927   0.730  54.841  1.00 54.21           C  
-ATOM   5635  O   ILE C  75      10.960   1.164  55.358  1.00 54.48           O  
-ATOM   5636  CB  ILE C  75       8.144   0.889  53.086  1.00 53.60           C  
-ATOM   5637  N   LYS C  82      10.876   6.860  60.413  1.00 51.57           N  
-ATOM   5638  CA  LYS C  82       9.999   7.996  60.150  1.00 51.57           C  
-ATOM   5639  C   LYS C  82      10.666   8.988  59.200  1.00 51.90           C  
-ATOM   5640  O   LYS C  82      10.088   9.374  58.180  1.00 52.19           O  
-ATOM   5641  CB  LYS C  82       9.638   8.687  61.460  1.00 49.68           C  
-ATOM   5642  N   ALA C  83      11.885   9.398  59.540  1.00 51.09           N  
-ATOM   5643  CA  ALA C  83      12.623  10.348  58.719  1.00 50.00           C  
-ATOM   5644  C   ALA C  83      14.112  10.446  59.078  1.00 49.06           C  
-ATOM   5645  O   ALA C  83      14.580  11.467  59.584  1.00 48.69           O  
-ATOM   5646  CB  ALA C  83      11.966  11.727  58.806  1.00 49.33           C  
-ATOM   5647  N   LEU C  84      14.848   9.367  58.829  1.00 47.19           N  
-ATOM   5648  CA  LEU C  84      16.283   9.353  59.074  1.00 44.58           C  
-ATOM   5649  C   LEU C  84      16.943   9.585  57.726  1.00 42.86           C  
-ATOM   5650  O   LEU C  84      18.163   9.534  57.593  1.00 41.77           O  
-ATOM   5651  CB  LEU C  84      16.727   8.015  59.657  1.00 46.66           C  
-ATOM   5652  CG  LEU C  84      16.539   7.892  61.167  1.00 48.48           C  
-ATOM   5653  CD1 LEU C  84      16.995   6.518  61.631  1.00 49.65           C  
-ATOM   5654  CD2 LEU C  84      17.335   8.990  61.862  1.00 48.31           C  
-ATOM   5655  N   MET C  85      16.104   9.819  56.722  1.00 40.53           N  
-ATOM   5656  CA  MET C  85      16.554  10.109  55.370  1.00 39.27           C  
-ATOM   5657  C   MET C  85      15.771  11.322  54.897  1.00 37.97           C  
-ATOM   5658  O   MET C  85      14.578  11.224  54.622  1.00 37.00           O  
-ATOM   5659  CB  MET C  85      16.287   8.941  54.419  1.00 39.35           C  
-ATOM   5660  CG  MET C  85      16.684   9.262  52.981  1.00 38.83           C  
-ATOM   5661  SD  MET C  85      16.365   7.953  51.794  1.00 40.57           S  
-ATOM   5662  CE  MET C  85      14.642   8.252  51.416  1.00 38.50           C  
-ATOM   5663  N   LYS C  86      16.442  12.465  54.827  1.00 37.31           N  
-ATOM   5664  CA  LYS C  86      15.813  13.704  54.386  1.00 36.94           C  
-ATOM   5665  C   LYS C  86      16.398  14.120  53.041  1.00 35.83           C  
-ATOM   5666  O   LYS C  86      17.614  14.090  52.849  1.00 36.04           O  
-ATOM   5667  CB  LYS C  86      16.059  14.817  55.406  1.00 39.56           C  
-ATOM   5668  CG  LYS C  86      15.436  14.598  56.773  1.00 42.20           C  
-ATOM   5669  CD  LYS C  86      13.919  14.521  56.698  1.00 45.68           C  
-ATOM   5670  CE  LYS C  86      13.297  14.736  58.069  1.00 47.52           C  
-ATOM   5671  NZ  LYS C  86      13.962  13.903  59.113  1.00 48.43           N  
-ATOM   5672  N   LEU C  87      15.531  14.507  52.113  1.00 33.59           N  
-ATOM   5673  CA  LEU C  87      15.965  14.928  50.788  1.00 29.89           C  
-ATOM   5674  C   LEU C  87      15.788  16.431  50.634  1.00 30.14           C  
-ATOM   5675  O   LEU C  87      14.791  16.995  51.082  1.00 30.55           O  
-ATOM   5676  CB  LEU C  87      15.159  14.195  49.716  1.00 27.25           C  
-ATOM   5677  CG  LEU C  87      15.272  12.668  49.711  1.00 25.98           C  
-ATOM   5678  CD1 LEU C  87      14.340  12.099  48.662  1.00 23.84           C  
-ATOM   5679  CD2 LEU C  87      16.701  12.242  49.438  1.00 22.60           C  
-ATOM   5680  N   HIS C  88      16.759  17.077  49.996  1.00 30.75           N  
-ATOM   5681  CA  HIS C  88      16.721  18.521  49.794  1.00 29.58           C  
-ATOM   5682  C   HIS C  88      17.093  18.895  48.358  1.00 29.98           C  
-ATOM   5683  O   HIS C  88      17.951  18.259  47.743  1.00 29.87           O  
-ATOM   5684  CB  HIS C  88      17.699  19.201  50.748  1.00 29.64           C  
-ATOM   5685  CG  HIS C  88      17.584  18.734  52.166  1.00 33.53           C  
-ATOM   5686  ND1 HIS C  88      16.533  19.087  52.985  1.00 34.27           N  
-ATOM   5687  CD2 HIS C  88      18.380  17.923  52.903  1.00 31.07           C  
-ATOM   5688  CE1 HIS C  88      16.687  18.515  54.165  1.00 34.02           C  
-ATOM   5689  NE2 HIS C  88      17.800  17.803  54.142  1.00 33.64           N  
-ATOM   5690  N   TYR C  89      16.446  19.935  47.838  1.00 28.59           N  
-ATOM   5691  CA  TYR C  89      16.708  20.417  46.489  1.00 25.89           C  
-ATOM   5692  C   TYR C  89      17.992  21.233  46.441  1.00 26.65           C  
-ATOM   5693  O   TYR C  89      18.170  22.182  47.208  1.00 25.19           O  
-ATOM   5694  CB  TYR C  89      15.544  21.281  45.989  1.00 25.65           C  
-ATOM   5695  CG  TYR C  89      14.319  20.491  45.595  1.00 25.00           C  
-ATOM   5696  CD1 TYR C  89      13.079  20.742  46.183  1.00 24.46           C  
-ATOM   5697  CD2 TYR C  89      14.401  19.481  44.634  1.00 24.44           C  
-ATOM   5698  CE1 TYR C  89      11.946  19.997  45.823  1.00 24.22           C  
-ATOM   5699  CE2 TYR C  89      13.285  18.739  44.266  1.00 23.31           C  
-ATOM   5700  CZ  TYR C  89      12.063  18.997  44.864  1.00 25.33           C  
-ATOM   5701  OH  TYR C  89      10.969  18.241  44.507  1.00 29.44           O  
-ATOM   5702  N   ALA C  90      18.875  20.848  45.524  1.00 25.84           N  
-ATOM   5703  CA  ALA C  90      20.153  21.517  45.320  1.00 25.30           C  
-ATOM   5704  C   ALA C  90      20.725  21.065  43.975  1.00 23.61           C  
-ATOM   5705  O   ALA C  90      20.113  20.253  43.274  1.00 24.24           O  
-ATOM   5706  CB  ALA C  90      21.118  21.159  46.451  1.00 24.18           C  
-ATOM   5707  N   ASP C  91      21.891  21.593  43.616  1.00 22.51           N  
-ATOM   5708  CA  ASP C  91      22.547  21.219  42.362  1.00 23.37           C  
-ATOM   5709  C   ASP C  91      24.030  21.553  42.448  1.00 24.15           C  
-ATOM   5710  O   ASP C  91      24.400  22.613  42.960  1.00 26.65           O  
-ATOM   5711  CB  ASP C  91      21.915  21.957  41.176  1.00 19.95           C  
-ATOM   5712  CG  ASP C  91      22.295  21.337  39.832  1.00 22.99           C  
-ATOM   5713  OD1 ASP C  91      23.469  21.436  39.422  1.00 22.75           O  
-ATOM   5714  OD2 ASP C  91      21.414  20.741  39.187  1.00 22.40           O  
-ATOM   5715  N   LEU C  92      24.877  20.657  41.948  1.00 24.20           N  
-ATOM   5716  CA  LEU C  92      26.315  20.882  41.997  1.00 24.80           C  
-ATOM   5717  C   LEU C  92      26.806  22.075  41.186  1.00 26.04           C  
-ATOM   5718  O   LEU C  92      27.970  22.466  41.297  1.00 25.66           O  
-ATOM   5719  CB  LEU C  92      27.071  19.617  41.582  1.00 26.46           C  
-ATOM   5720  CG  LEU C  92      27.661  18.870  42.787  1.00 30.13           C  
-ATOM   5721  CD1 LEU C  92      26.538  18.408  43.704  1.00 30.58           C  
-ATOM   5722  CD2 LEU C  92      28.489  17.691  42.319  1.00 32.42           C  
-ATOM   5723  N   THR C  93      25.931  22.657  40.371  1.00 23.21           N  
-ATOM   5724  CA  THR C  93      26.317  23.832  39.591  1.00 22.90           C  
-ATOM   5725  C   THR C  93      25.821  25.087  40.311  1.00 24.32           C  
-ATOM   5726  O   THR C  93      25.950  26.199  39.810  1.00 22.91           O  
-ATOM   5727  CB  THR C  93      25.707  23.809  38.173  1.00 22.63           C  
-ATOM   5728  OG1 THR C  93      24.277  23.870  38.260  1.00 19.57           O  
-ATOM   5729  CG2 THR C  93      26.119  22.549  37.441  1.00 22.81           C  
-ATOM   5730  N   ASP C  94      25.246  24.891  41.493  1.00 26.32           N  
-ATOM   5731  CA  ASP C  94      24.713  25.991  42.288  1.00 26.73           C  
-ATOM   5732  C   ASP C  94      25.385  26.000  43.668  1.00 26.77           C  
-ATOM   5733  O   ASP C  94      24.952  25.305  44.588  1.00 25.55           O  
-ATOM   5734  CB  ASP C  94      23.191  25.824  42.416  1.00 27.43           C  
-ATOM   5735  CG  ASP C  94      22.530  26.983  43.140  1.00 28.26           C  
-ATOM   5736  OD1 ASP C  94      21.278  27.048  43.151  1.00 26.12           O  
-ATOM   5737  OD2 ASP C  94      23.260  27.826  43.697  1.00 27.60           O  
-ATOM   5738  N   ALA C  95      26.448  26.790  43.796  1.00 27.09           N  
-ATOM   5739  CA  ALA C  95      27.207  26.895  45.039  1.00 27.68           C  
-ATOM   5740  C   ALA C  95      26.364  27.300  46.251  1.00 27.59           C  
-ATOM   5741  O   ALA C  95      26.546  26.759  47.341  1.00 28.56           O  
-ATOM   5742  CB  ALA C  95      28.374  27.873  44.858  1.00 27.41           C  
-ATOM   5743  N   SER C  96      25.450  28.246  46.069  1.00 28.57           N  
-ATOM   5744  CA  SER C  96      24.590  28.692  47.162  1.00 28.64           C  
-ATOM   5745  C   SER C  96      23.733  27.544  47.692  1.00 29.31           C  
-ATOM   5746  O   SER C  96      23.588  27.378  48.903  1.00 29.72           O  
-ATOM   5747  CB  SER C  96      23.668  29.815  46.694  1.00 30.60           C  
-ATOM   5748  OG  SER C  96      24.408  30.871  46.114  1.00 38.31           O  
-ATOM   5749  N   SER C  97      23.159  26.757  46.786  1.00 27.18           N  
-ATOM   5750  CA  SER C  97      22.318  25.639  47.200  1.00 27.83           C  
-ATOM   5751  C   SER C  97      23.097  24.621  48.042  1.00 26.61           C  
-ATOM   5752  O   SER C  97      22.532  23.981  48.928  1.00 27.88           O  
-ATOM   5753  CB  SER C  97      21.702  24.938  45.978  1.00 25.53           C  
-ATOM   5754  OG  SER C  97      22.654  24.150  45.283  1.00 27.57           O  
-ATOM   5755  N   LEU C  98      24.387  24.470  47.764  1.00 26.48           N  
-ATOM   5756  CA  LEU C  98      25.216  23.529  48.512  1.00 28.52           C  
-ATOM   5757  C   LEU C  98      25.488  24.032  49.936  1.00 30.92           C  
-ATOM   5758  O   LEU C  98      25.254  23.315  50.907  1.00 32.71           O  
-ATOM   5759  CB  LEU C  98      26.547  23.301  47.791  1.00 25.79           C  
-ATOM   5760  CG  LEU C  98      26.495  22.784  46.349  1.00 24.28           C  
-ATOM   5761  CD1 LEU C  98      27.912  22.460  45.879  1.00 19.33           C  
-ATOM   5762  CD2 LEU C  98      25.612  21.550  46.270  1.00 22.37           C  
-ATOM   5763  N   ARG C  99      25.987  25.261  50.052  1.00 31.75           N  
-ATOM   5764  CA  ARG C  99      26.288  25.847  51.354  1.00 34.98           C  
-ATOM   5765  C   ARG C  99      25.029  25.936  52.211  1.00 37.26           C  
-ATOM   5766  O   ARG C  99      25.072  25.710  53.420  1.00 38.42           O  
-ATOM   5767  CB  ARG C  99      26.897  27.247  51.178  1.00 34.08           C  
-ATOM   5768  CG  ARG C  99      27.208  27.985  52.482  1.00 35.58           C  
-ATOM   5769  CD  ARG C  99      28.210  27.224  53.366  1.00 35.60           C  
-ATOM   5770  NE  ARG C  99      28.388  27.873  54.666  1.00 34.20           N  
-ATOM   5771  CZ  ARG C  99      29.050  29.013  54.858  1.00 34.37           C  
-ATOM   5772  NH1 ARG C  99      29.614  29.643  53.834  1.00 33.35           N  
-ATOM   5773  NH2 ARG C  99      29.132  29.538  56.074  1.00 34.17           N  
-ATOM   5774  N   ARG C 100      23.910  26.262  51.569  1.00 38.06           N  
-ATOM   5775  CA  ARG C 100      22.625  26.399  52.243  1.00 37.87           C  
-ATOM   5776  C   ARG C 100      22.256  25.183  53.083  1.00 37.33           C  
-ATOM   5777  O   ARG C 100      21.944  25.305  54.261  1.00 36.41           O  
-ATOM   5778  CB  ARG C 100      21.530  26.664  51.205  1.00 40.20           C  
-ATOM   5779  CG  ARG C 100      20.109  26.741  51.752  1.00 41.66           C  
-ATOM   5780  CD  ARG C 100      19.165  27.323  50.699  1.00 41.85           C  
-ATOM   5781  NE  ARG C 100      17.789  27.449  51.174  1.00 44.34           N  
-ATOM   5782  CZ  ARG C 100      16.913  28.330  50.693  1.00 46.82           C  
-ATOM   5783  NH1 ARG C 100      15.676  28.382  51.175  1.00 45.56           N  
-ATOM   5784  NH2 ARG C 100      17.276  29.175  49.734  1.00 46.40           N  
-ATOM   5785  N   TRP C 101      22.290  24.005  52.479  1.00 37.01           N  
-ATOM   5786  CA  TRP C 101      21.930  22.802  53.205  1.00 37.48           C  
-ATOM   5787  C   TRP C 101      23.026  22.327  54.143  1.00 37.73           C  
-ATOM   5788  O   TRP C 101      22.760  21.619  55.108  1.00 38.28           O  
-ATOM   5789  CB  TRP C 101      21.546  21.704  52.220  1.00 38.05           C  
-ATOM   5790  CG  TRP C 101      20.349  22.084  51.433  1.00 39.02           C  
-ATOM   5791  CD1 TRP C 101      20.304  22.405  50.110  1.00 39.36           C  
-ATOM   5792  CD2 TRP C 101      19.016  22.242  51.932  1.00 39.96           C  
-ATOM   5793  NE1 TRP C 101      19.025  22.756  49.751  1.00 39.66           N  
-ATOM   5794  CE2 TRP C 101      18.214  22.664  50.851  1.00 38.96           C  
-ATOM   5795  CE3 TRP C 101      18.422  22.067  53.189  1.00 39.68           C  
-ATOM   5796  CZ2 TRP C 101      16.846  22.916  50.986  1.00 40.07           C  
-ATOM   5797  CZ3 TRP C 101      17.059  22.318  53.324  1.00 40.06           C  
-ATOM   5798  CH2 TRP C 101      16.288  22.738  52.227  1.00 39.45           C  
-ATOM   5799  N   ILE C 102      24.262  22.711  53.861  1.00 38.53           N  
-ATOM   5800  CA  ILE C 102      25.355  22.323  54.734  1.00 39.64           C  
-ATOM   5801  C   ILE C 102      25.200  23.068  56.062  1.00 39.80           C  
-ATOM   5802  O   ILE C 102      25.432  22.498  57.126  1.00 40.51           O  
-ATOM   5803  CB  ILE C 102      26.723  22.646  54.097  1.00 37.63           C  
-ATOM   5804  CG1 ILE C 102      27.014  21.645  52.979  1.00 35.52           C  
-ATOM   5805  CG2 ILE C 102      27.820  22.592  55.147  1.00 38.81           C  
-ATOM   5806  CD1 ILE C 102      28.336  21.870  52.285  1.00 33.85           C  
-ATOM   5807  N   ASP C 103      24.794  24.334  55.993  1.00 39.63           N  
-ATOM   5808  CA  ASP C 103      24.600  25.143  57.195  1.00 40.43           C  
-ATOM   5809  C   ASP C 103      23.418  24.644  58.021  1.00 39.90           C  
-ATOM   5810  O   ASP C 103      23.500  24.535  59.245  1.00 39.94           O  
-ATOM   5811  CB  ASP C 103      24.367  26.615  56.835  1.00 40.10           C  
-ATOM   5812  CG  ASP C 103      25.618  27.297  56.318  1.00 40.52           C  
-ATOM   5813  OD1 ASP C 103      26.729  26.842  56.665  1.00 41.06           O  
-ATOM   5814  OD2 ASP C 103      25.486  28.298  55.580  1.00 42.09           O  
-ATOM   5815  N   VAL C 104      22.316  24.351  57.342  1.00 38.43           N  
-ATOM   5816  CA  VAL C 104      21.117  23.862  58.002  1.00 36.74           C  
-ATOM   5817  C   VAL C 104      21.305  22.455  58.560  1.00 36.58           C  
-ATOM   5818  O   VAL C 104      20.856  22.152  59.666  1.00 37.24           O  
-ATOM   5819  CB  VAL C 104      19.919  23.850  57.027  1.00 36.36           C  
-ATOM   5820  CG1 VAL C 104      18.777  23.016  57.600  1.00 36.07           C  
-ATOM   5821  CG2 VAL C 104      19.453  25.272  56.769  1.00 35.28           C  
-ATOM   5822  N   ILE C 105      21.978  21.603  57.797  1.00 35.25           N  
-ATOM   5823  CA  ILE C 105      22.190  20.219  58.197  1.00 35.52           C  
-ATOM   5824  C   ILE C 105      23.344  19.998  59.172  1.00 36.63           C  
-ATOM   5825  O   ILE C 105      23.271  19.120  60.032  1.00 35.67           O  
-ATOM   5826  CB  ILE C 105      22.399  19.335  56.947  1.00 35.86           C  
-ATOM   5827  CG1 ILE C 105      21.144  19.401  56.065  1.00 37.54           C  
-ATOM   5828  CG2 ILE C 105      22.695  17.898  57.353  1.00 34.54           C  
-ATOM   5829  CD1 ILE C 105      21.273  18.687  54.730  1.00 36.43           C  
-ATOM   5830  N   LYS C 106      24.405  20.787  59.041  1.00 36.04           N  
-ATOM   5831  CA  LYS C 106      25.564  20.646  59.917  1.00 38.28           C  
-ATOM   5832  C   LYS C 106      25.953  19.174  59.975  1.00 38.46           C  
-ATOM   5833  O   LYS C 106      25.898  18.548  61.033  1.00 39.90           O  
-ATOM   5834  CB  LYS C 106      25.227  21.151  61.324  1.00 39.06           C  
-ATOM   5835  CG  LYS C 106      24.775  22.598  61.359  1.00 40.71           C  
-ATOM   5836  CD  LYS C 106      24.157  22.948  62.693  1.00 43.48           C  
-ATOM   5837  CE  LYS C 106      23.521  24.324  62.661  1.00 46.00           C  
-ATOM   5838  NZ  LYS C 106      22.805  24.626  63.938  1.00 50.67           N  
-ATOM   5839  N   PRO C 107      26.349  18.602  58.828  1.00 38.32           N  
-ATOM   5840  CA  PRO C 107      26.744  17.194  58.742  1.00 37.76           C  
-ATOM   5841  C   PRO C 107      28.113  16.880  59.331  1.00 36.93           C  
-ATOM   5842  O   PRO C 107      28.964  17.761  59.457  1.00 36.59           O  
-ATOM   5843  CB  PRO C 107      26.696  16.924  57.245  1.00 38.78           C  
-ATOM   5844  CG  PRO C 107      27.194  18.222  56.684  1.00 37.63           C  
-ATOM   5845  CD  PRO C 107      26.438  19.250  57.506  1.00 36.84           C  
-ATOM   5846  N   ASP C 108      28.310  15.610  59.677  1.00 36.33           N  
-ATOM   5847  CA  ASP C 108      29.570  15.134  60.235  1.00 37.19           C  
-ATOM   5848  C   ASP C 108      30.371  14.477  59.111  1.00 37.61           C  
-ATOM   5849  O   ASP C 108      31.603  14.457  59.132  1.00 37.72           O  
-ATOM   5850  CB  ASP C 108      29.304  14.118  61.351  1.00 37.21           C  
-ATOM   5851  CG  ASP C 108      28.385  14.664  62.431  1.00 38.34           C  
-ATOM   5852  OD1 ASP C 108      28.706  15.721  63.019  1.00 39.48           O  
-ATOM   5853  OD2 ASP C 108      27.338  14.037  62.689  1.00 38.46           O  
-ATOM   5854  N   GLU C 109      29.657  13.940  58.128  1.00 36.62           N  
-ATOM   5855  CA  GLU C 109      30.293  13.298  56.988  1.00 36.31           C  
-ATOM   5856  C   GLU C 109      29.625  13.730  55.683  1.00 34.84           C  
-ATOM   5857  O   GLU C 109      28.401  13.853  55.609  1.00 33.26           O  
-ATOM   5858  CB  GLU C 109      30.230  11.775  57.139  1.00 38.08           C  
-ATOM   5859  CG  GLU C 109      30.938  11.266  58.388  1.00 41.24           C  
-ATOM   5860  CD  GLU C 109      30.999   9.755  58.464  1.00 42.80           C  
-ATOM   5861  OE1 GLU C 109      31.697   9.244  59.365  1.00 47.20           O  
-ATOM   5862  OE2 GLU C 109      30.357   9.075  57.633  1.00 44.12           O  
-ATOM   5863  N   VAL C 110      30.442  13.980  54.663  1.00 32.96           N  
-ATOM   5864  CA  VAL C 110      29.941  14.393  53.357  1.00 30.08           C  
-ATOM   5865  C   VAL C 110      30.490  13.474  52.275  1.00 28.48           C  
-ATOM   5866  O   VAL C 110      31.697  13.284  52.158  1.00 28.23           O  
-ATOM   5867  CB  VAL C 110      30.329  15.861  53.031  1.00 29.72           C  
-ATOM   5868  CG1 VAL C 110      29.904  16.221  51.605  1.00 29.08           C  
-ATOM   5869  CG2 VAL C 110      29.650  16.798  54.011  1.00 28.44           C  
-ATOM   5870  N   TYR C 111      29.578  12.903  51.495  1.00 27.26           N  
-ATOM   5871  CA  TYR C 111      29.914  11.989  50.413  1.00 26.51           C  
-ATOM   5872  C   TYR C 111      29.491  12.611  49.085  1.00 28.43           C  
-ATOM   5873  O   TYR C 111      28.292  12.721  48.796  1.00 27.23           O  
-ATOM   5874  CB  TYR C 111      29.169  10.662  50.605  1.00 27.28           C  
-ATOM   5875  CG  TYR C 111      29.598   9.878  51.828  1.00 28.64           C  
-ATOM   5876  CD1 TYR C 111      30.596   8.913  51.741  1.00 29.59           C  
-ATOM   5877  CD2 TYR C 111      29.028  10.127  53.079  1.00 28.52           C  
-ATOM   5878  CE1 TYR C 111      31.023   8.211  52.866  1.00 32.18           C  
-ATOM   5879  CE2 TYR C 111      29.448   9.432  54.214  1.00 31.33           C  
-ATOM   5880  CZ  TYR C 111      30.449   8.474  54.097  1.00 32.44           C  
-ATOM   5881  OH  TYR C 111      30.880   7.782  55.208  1.00 33.76           O  
-ATOM   5882  N   ASN C 112      30.465  13.024  48.279  1.00 27.48           N  
-ATOM   5883  CA  ASN C 112      30.146  13.614  46.989  1.00 25.32           C  
-ATOM   5884  C   ASN C 112      30.095  12.533  45.920  1.00 24.12           C  
-ATOM   5885  O   ASN C 112      31.109  12.174  45.329  1.00 26.02           O  
-ATOM   5886  CB  ASN C 112      31.169  14.680  46.607  1.00 24.44           C  
-ATOM   5887  CG  ASN C 112      30.831  15.352  45.291  1.00 23.82           C  
-ATOM   5888  OD1 ASN C 112      29.697  15.781  45.079  1.00 23.17           O  
-ATOM   5889  ND2 ASN C 112      31.812  15.451  44.403  1.00 19.31           N  
-ATOM   5890  N   LEU C 113      28.896  12.019  45.681  1.00 23.01           N  
-ATOM   5891  CA  LEU C 113      28.689  10.976  44.696  1.00 22.52           C  
-ATOM   5892  C   LEU C 113      28.025  11.542  43.448  1.00 24.12           C  
-ATOM   5893  O   LEU C 113      27.939  10.863  42.428  1.00 25.17           O  
-ATOM   5894  CB  LEU C 113      27.791   9.886  45.280  1.00 23.45           C  
-ATOM   5895  CG  LEU C 113      28.223   9.255  46.604  1.00 25.22           C  
-ATOM   5896  CD1 LEU C 113      27.149   8.285  47.071  1.00 26.98           C  
-ATOM   5897  CD2 LEU C 113      29.555   8.542  46.430  1.00 27.29           C  
-ATOM   5898  N   ALA C 114      27.555  12.784  43.539  1.00 23.35           N  
-ATOM   5899  CA  ALA C 114      26.869  13.435  42.431  1.00 23.43           C  
-ATOM   5900  C   ALA C 114      27.741  13.624  41.198  1.00 23.32           C  
-ATOM   5901  O   ALA C 114      28.904  14.001  41.302  1.00 24.80           O  
-ATOM   5902  CB  ALA C 114      26.316  14.776  42.882  1.00 20.78           C  
-ATOM   5903  N   ALA C 115      27.165  13.367  40.027  1.00 23.59           N  
-ATOM   5904  CA  ALA C 115      27.896  13.529  38.779  1.00 23.90           C  
-ATOM   5905  C   ALA C 115      27.123  13.099  37.543  1.00 23.55           C  
-ATOM   5906  O   ALA C 115      26.142  12.354  37.627  1.00 23.31           O  
-ATOM   5907  CB  ALA C 115      29.203  12.742  38.837  1.00 22.90           C  
-ATOM   5908  N   GLN C 116      27.565  13.619  36.401  1.00 22.00           N  
-ATOM   5909  CA  GLN C 116      27.031  13.231  35.105  1.00 22.20           C  
-ATOM   5910  C   GLN C 116      28.026  12.084  34.916  1.00 22.90           C  
-ATOM   5911  O   GLN C 116      29.131  12.283  34.406  1.00 23.66           O  
-ATOM   5912  CB  GLN C 116      27.280  14.337  34.079  1.00 20.92           C  
-ATOM   5913  CG  GLN C 116      26.673  14.084  32.703  1.00 21.17           C  
-ATOM   5914  CD  GLN C 116      27.162  12.793  32.076  1.00 20.73           C  
-ATOM   5915  OE1 GLN C 116      26.647  11.712  32.364  1.00 20.48           O  
-ATOM   5916  NE2 GLN C 116      28.176  12.899  31.227  1.00 22.87           N  
-ATOM   5917  N   SER C 117      27.638  10.894  35.358  1.00 22.92           N  
-ATOM   5918  CA  SER C 117      28.533   9.734  35.341  1.00 26.59           C  
-ATOM   5919  C   SER C 117      28.722   8.894  34.079  1.00 26.72           C  
-ATOM   5920  O   SER C 117      29.550   7.983  34.072  1.00 27.97           O  
-ATOM   5921  CB  SER C 117      28.145   8.793  36.480  1.00 26.21           C  
-ATOM   5922  OG  SER C 117      26.911   8.165  36.198  1.00 29.29           O  
-ATOM   5923  N   HIS C 118      27.976   9.172  33.020  1.00 26.30           N  
-ATOM   5924  CA  HIS C 118      28.140   8.378  31.815  1.00 26.14           C  
-ATOM   5925  C   HIS C 118      29.253   8.917  30.919  1.00 25.08           C  
-ATOM   5926  O   HIS C 118      29.232  10.072  30.496  1.00 26.17           O  
-ATOM   5927  CB  HIS C 118      26.822   8.296  31.046  1.00 27.69           C  
-ATOM   5928  CG  HIS C 118      26.720   7.085  30.173  1.00 28.34           C  
-ATOM   5929  ND1 HIS C 118      27.321   7.007  28.935  1.00 27.90           N  
-ATOM   5930  CD2 HIS C 118      26.146   5.877  30.391  1.00 28.21           C  
-ATOM   5931  CE1 HIS C 118      27.124   5.803  28.428  1.00 29.84           C  
-ATOM   5932  NE2 HIS C 118      26.415   5.098  29.292  1.00 30.12           N  
-ATOM   5933  N   VAL C 119      30.229   8.060  30.641  1.00 26.07           N  
-ATOM   5934  CA  VAL C 119      31.371   8.418  29.816  1.00 24.55           C  
-ATOM   5935  C   VAL C 119      31.003   8.809  28.386  1.00 25.72           C  
-ATOM   5936  O   VAL C 119      31.441   9.845  27.890  1.00 26.01           O  
-ATOM   5937  CB  VAL C 119      32.405   7.255  29.792  1.00 25.61           C  
-ATOM   5938  CG1 VAL C 119      33.508   7.551  28.793  1.00 22.70           C  
-ATOM   5939  CG2 VAL C 119      33.001   7.058  31.194  1.00 22.29           C  
-ATOM   5940  N   ALA C 120      30.200   7.986  27.719  1.00 28.81           N  
-ATOM   5941  CA  ALA C 120      29.802   8.273  26.340  1.00 28.57           C  
-ATOM   5942  C   ALA C 120      29.101   9.628  26.258  1.00 27.82           C  
-ATOM   5943  O   ALA C 120      29.374  10.432  25.368  1.00 27.49           O  
-ATOM   5944  CB  ALA C 120      28.880   7.165  25.815  1.00 29.42           C  
-ATOM   5945  N   VAL C 121      28.198   9.879  27.196  1.00 26.82           N  
-ATOM   5946  CA  VAL C 121      27.473  11.138  27.215  1.00 26.56           C  
-ATOM   5947  C   VAL C 121      28.394  12.332  27.468  1.00 25.92           C  
-ATOM   5948  O   VAL C 121      28.125  13.436  26.990  1.00 26.52           O  
-ATOM   5949  CB  VAL C 121      26.365  11.123  28.283  1.00 26.29           C  
-ATOM   5950  CG1 VAL C 121      25.626  12.445  28.287  1.00 24.80           C  
-ATOM   5951  CG2 VAL C 121      25.392   9.988  27.996  1.00 26.65           C  
-ATOM   5952  N   SER C 122      29.490  12.115  28.193  1.00 25.12           N  
-ATOM   5953  CA  SER C 122      30.402  13.218  28.486  1.00 22.83           C  
-ATOM   5954  C   SER C 122      31.043  13.802  27.228  1.00 24.25           C  
-ATOM   5955  O   SER C 122      31.414  14.978  27.210  1.00 21.53           O  
-ATOM   5956  CB  SER C 122      31.480  12.791  29.498  1.00 20.44           C  
-ATOM   5957  OG  SER C 122      32.467  11.955  28.922  1.00 24.90           O  
-ATOM   5958  N   PHE C 123      31.172  13.000  26.171  1.00 25.15           N  
-ATOM   5959  CA  PHE C 123      31.753  13.519  24.937  1.00 26.77           C  
-ATOM   5960  C   PHE C 123      30.748  14.441  24.251  1.00 27.39           C  
-ATOM   5961  O   PHE C 123      31.132  15.307  23.472  1.00 29.14           O  
-ATOM   5962  CB  PHE C 123      32.125  12.396  23.964  1.00 26.31           C  
-ATOM   5963  CG  PHE C 123      33.289  11.558  24.406  1.00 24.16           C  
-ATOM   5964  CD1 PHE C 123      33.089  10.392  25.130  1.00 26.36           C  
-ATOM   5965  CD2 PHE C 123      34.585  11.917  24.059  1.00 23.53           C  
-ATOM   5966  CE1 PHE C 123      34.164   9.585  25.496  1.00 23.83           C  
-ATOM   5967  CE2 PHE C 123      35.667  11.123  24.417  1.00 22.93           C  
-ATOM   5968  CZ  PHE C 123      35.458   9.953  25.136  1.00 24.92           C  
-ATOM   5969  N   GLU C 124      29.463  14.252  24.550  1.00 29.32           N  
-ATOM   5970  CA  GLU C 124      28.396  15.060  23.951  1.00 30.69           C  
-ATOM   5971  C   GLU C 124      28.150  16.389  24.664  1.00 29.49           C  
-ATOM   5972  O   GLU C 124      27.882  17.407  24.022  1.00 28.88           O  
-ATOM   5973  CB  GLU C 124      27.092  14.272  23.933  1.00 33.92           C  
-ATOM   5974  CG  GLU C 124      27.200  12.900  23.321  1.00 36.66           C  
-ATOM   5975  CD  GLU C 124      26.053  12.620  22.387  1.00 39.50           C  
-ATOM   5976  OE1 GLU C 124      26.116  13.078  21.227  1.00 42.35           O  
-ATOM   5977  OE2 GLU C 124      25.084  11.963  22.819  1.00 40.22           O  
-ATOM   5978  N   ILE C 125      28.219  16.357  25.995  1.00 30.25           N  
-ATOM   5979  CA  ILE C 125      28.028  17.541  26.831  1.00 27.97           C  
-ATOM   5980  C   ILE C 125      29.236  17.715  27.754  1.00 27.84           C  
-ATOM   5981  O   ILE C 125      29.112  17.641  28.976  1.00 26.83           O  
-ATOM   5982  CB  ILE C 125      26.762  17.417  27.708  1.00 28.65           C  
-ATOM   5983  CG1 ILE C 125      26.719  16.035  28.364  1.00 27.78           C  
-ATOM   5984  CG2 ILE C 125      25.520  17.687  26.876  1.00 26.64           C  
-ATOM   5985  CD1 ILE C 125      25.580  15.852  29.330  1.00 27.33           C  
-ATOM   5986  N   PRO C 126      30.421  17.968  27.173  1.00 26.95           N  
-ATOM   5987  CA  PRO C 126      31.644  18.145  27.966  1.00 26.32           C  
-ATOM   5988  C   PRO C 126      31.610  19.316  28.950  1.00 27.22           C  
-ATOM   5989  O   PRO C 126      32.002  19.168  30.109  1.00 26.29           O  
-ATOM   5990  CB  PRO C 126      32.727  18.296  26.898  1.00 24.72           C  
-ATOM   5991  CG  PRO C 126      31.986  18.938  25.758  1.00 26.00           C  
-ATOM   5992  CD  PRO C 126      30.687  18.170  25.737  1.00 25.46           C  
-ATOM   5993  N   ASP C 127      31.144  20.472  28.486  1.00 25.88           N  
-ATOM   5994  CA  ASP C 127      31.061  21.657  29.328  1.00 26.28           C  
-ATOM   5995  C   ASP C 127      30.238  21.399  30.594  1.00 25.53           C  
-ATOM   5996  O   ASP C 127      30.708  21.640  31.705  1.00 24.34           O  
-ATOM   5997  CB  ASP C 127      30.468  22.828  28.532  1.00 30.18           C  
-ATOM   5998  CG  ASP C 127      31.379  23.285  27.386  1.00 35.49           C  
-ATOM   5999  OD1 ASP C 127      30.957  24.143  26.580  1.00 38.13           O  
-ATOM   6000  OD2 ASP C 127      32.524  22.794  27.289  1.00 34.80           O  
-ATOM   6001  N   TYR C 128      29.015  20.909  30.427  1.00 24.87           N  
-ATOM   6002  CA  TYR C 128      28.154  20.614  31.568  1.00 24.54           C  
-ATOM   6003  C   TYR C 128      28.789  19.559  32.480  1.00 24.72           C  
-ATOM   6004  O   TYR C 128      28.787  19.695  33.703  1.00 24.86           O  
-ATOM   6005  CB  TYR C 128      26.784  20.109  31.090  1.00 22.19           C  
-ATOM   6006  CG  TYR C 128      25.898  19.657  32.220  1.00 19.48           C  
-ATOM   6007  CD1 TYR C 128      25.141  20.573  32.954  1.00 19.19           C  
-ATOM   6008  CD2 TYR C 128      25.888  18.319  32.620  1.00 22.36           C  
-ATOM   6009  CE1 TYR C 128      24.398  20.167  34.069  1.00 17.88           C  
-ATOM   6010  CE2 TYR C 128      25.154  17.903  33.732  1.00 21.41           C  
-ATOM   6011  CZ  TYR C 128      24.414  18.831  34.452  1.00 19.46           C  
-ATOM   6012  OH  TYR C 128      23.722  18.414  35.562  1.00 20.64           O  
-ATOM   6013  N   THR C 129      29.326  18.503  31.877  1.00 25.15           N  
-ATOM   6014  CA  THR C 129      29.948  17.427  32.633  1.00 23.23           C  
-ATOM   6015  C   THR C 129      31.078  17.961  33.500  1.00 23.27           C  
-ATOM   6016  O   THR C 129      31.146  17.663  34.688  1.00 21.66           O  
-ATOM   6017  CB  THR C 129      30.506  16.328  31.691  1.00 25.36           C  
-ATOM   6018  OG1 THR C 129      29.429  15.745  30.947  1.00 23.58           O  
-ATOM   6019  CG2 THR C 129      31.218  15.237  32.486  1.00 19.60           C  
-ATOM   6020  N   ALA C 130      31.958  18.758  32.906  1.00 20.45           N  
-ATOM   6021  CA  ALA C 130      33.077  19.319  33.642  1.00 21.12           C  
-ATOM   6022  C   ALA C 130      32.591  20.203  34.786  1.00 22.02           C  
-ATOM   6023  O   ALA C 130      33.178  20.199  35.862  1.00 21.46           O  
-ATOM   6024  CB  ALA C 130      33.974  20.126  32.704  1.00 17.39           C  
-ATOM   6025  N   ASP C 131      31.513  20.949  34.551  1.00 20.98           N  
-ATOM   6026  CA  ASP C 131      30.976  21.844  35.568  1.00 22.53           C  
-ATOM   6027  C   ASP C 131      30.394  21.107  36.770  1.00 22.28           C  
-ATOM   6028  O   ASP C 131      30.419  21.618  37.888  1.00 23.85           O  
-ATOM   6029  CB  ASP C 131      29.913  22.767  34.962  1.00 23.48           C  
-ATOM   6030  CG  ASP C 131      29.641  23.985  35.823  1.00 21.44           C  
-ATOM   6031  OD1 ASP C 131      30.610  24.666  36.216  1.00 23.22           O  
-ATOM   6032  OD2 ASP C 131      28.462  24.271  36.102  1.00 27.86           O  
-ATOM   6033  N   VAL C 132      29.865  19.912  36.541  1.00 22.05           N  
-ATOM   6034  CA  VAL C 132      29.297  19.125  37.623  1.00 22.26           C  
-ATOM   6035  C   VAL C 132      30.346  18.236  38.294  1.00 24.35           C  
-ATOM   6036  O   VAL C 132      30.461  18.210  39.526  1.00 24.21           O  
-ATOM   6037  CB  VAL C 132      28.156  18.218  37.116  1.00 23.85           C  
-ATOM   6038  CG1 VAL C 132      27.603  17.380  38.268  1.00 22.20           C  
-ATOM   6039  CG2 VAL C 132      27.063  19.065  36.496  1.00 23.39           C  
-ATOM   6040  N   VAL C 133      31.110  17.522  37.474  1.00 20.97           N  
-ATOM   6041  CA  VAL C 133      32.126  16.594  37.959  1.00 23.25           C  
-ATOM   6042  C   VAL C 133      33.400  17.237  38.507  1.00 24.74           C  
-ATOM   6043  O   VAL C 133      33.936  16.786  39.517  1.00 25.77           O  
-ATOM   6044  CB  VAL C 133      32.517  15.592  36.846  1.00 22.24           C  
-ATOM   6045  CG1 VAL C 133      33.578  14.619  37.351  1.00 21.51           C  
-ATOM   6046  CG2 VAL C 133      31.289  14.832  36.383  1.00 22.43           C  
-ATOM   6047  N   ALA C 134      33.883  18.282  37.846  1.00 24.60           N  
-ATOM   6048  CA  ALA C 134      35.101  18.955  38.278  1.00 24.47           C  
-ATOM   6049  C   ALA C 134      34.846  20.161  39.191  1.00 25.20           C  
-ATOM   6050  O   ALA C 134      35.143  20.118  40.387  1.00 27.06           O  
-ATOM   6051  CB  ALA C 134      35.910  19.379  37.064  1.00 23.66           C  
-ATOM   6052  N   THR C 135      34.293  21.231  38.633  1.00 24.07           N  
-ATOM   6053  CA  THR C 135      34.030  22.431  39.416  1.00 23.52           C  
-ATOM   6054  C   THR C 135      32.976  22.174  40.490  1.00 25.01           C  
-ATOM   6055  O   THR C 135      33.031  22.761  41.570  1.00 25.64           O  
-ATOM   6056  CB  THR C 135      33.586  23.596  38.503  1.00 22.04           C  
-ATOM   6057  OG1 THR C 135      34.555  23.766  37.465  1.00 22.76           O  
-ATOM   6058  CG2 THR C 135      33.502  24.906  39.288  1.00 22.35           C  
-ATOM   6059  N   GLY C 136      32.026  21.291  40.193  1.00 22.53           N  
-ATOM   6060  CA  GLY C 136      30.994  20.964  41.155  1.00 22.36           C  
-ATOM   6061  C   GLY C 136      31.604  20.385  42.420  1.00 23.75           C  
-ATOM   6062  O   GLY C 136      31.193  20.725  43.529  1.00 24.80           O  
-ATOM   6063  N   ALA C 137      32.587  19.507  42.253  1.00 23.55           N  
-ATOM   6064  CA  ALA C 137      33.261  18.897  43.391  1.00 25.93           C  
-ATOM   6065  C   ALA C 137      33.985  19.984  44.178  1.00 26.40           C  
-ATOM   6066  O   ALA C 137      33.990  19.971  45.406  1.00 27.13           O  
-ATOM   6067  CB  ALA C 137      34.257  17.838  42.911  1.00 26.12           C  
-ATOM   6068  N   LEU C 138      34.591  20.927  43.463  1.00 25.90           N  
-ATOM   6069  CA  LEU C 138      35.308  22.018  44.108  1.00 23.30           C  
-ATOM   6070  C   LEU C 138      34.338  22.909  44.878  1.00 24.63           C  
-ATOM   6071  O   LEU C 138      34.658  23.372  45.975  1.00 25.44           O  
-ATOM   6072  CB  LEU C 138      36.074  22.838  43.064  1.00 23.68           C  
-ATOM   6073  CG  LEU C 138      36.820  24.088  43.533  1.00 22.99           C  
-ATOM   6074  CD1 LEU C 138      37.791  23.733  44.658  1.00 25.13           C  
-ATOM   6075  CD2 LEU C 138      37.568  24.698  42.358  1.00 24.02           C  
-ATOM   6076  N   ARG C 139      33.156  23.148  44.311  1.00 22.39           N  
-ATOM   6077  CA  ARG C 139      32.163  23.979  44.985  1.00 22.88           C  
-ATOM   6078  C   ARG C 139      31.788  23.357  46.325  1.00 23.34           C  
-ATOM   6079  O   ARG C 139      31.672  24.054  47.325  1.00 24.57           O  
-ATOM   6080  CB  ARG C 139      30.885  24.137  44.145  1.00 23.56           C  
-ATOM   6081  CG  ARG C 139      31.044  24.925  42.850  1.00 25.26           C  
-ATOM   6082  CD  ARG C 139      29.688  25.236  42.208  1.00 24.21           C  
-ATOM   6083  NE  ARG C 139      29.855  25.950  40.944  1.00 28.88           N  
-ATOM   6084  CZ  ARG C 139      29.998  25.364  39.757  1.00 28.01           C  
-ATOM   6085  NH1 ARG C 139      30.159  26.100  38.669  1.00 28.46           N  
-ATOM   6086  NH2 ARG C 139      29.946  24.047  39.647  1.00 28.94           N  
-ATOM   6087  N   LEU C 140      31.588  22.043  46.338  1.00 23.35           N  
-ATOM   6088  CA  LEU C 140      31.217  21.351  47.564  1.00 24.90           C  
-ATOM   6089  C   LEU C 140      32.350  21.478  48.585  1.00 26.17           C  
-ATOM   6090  O   LEU C 140      32.120  21.837  49.739  1.00 27.89           O  
-ATOM   6091  CB  LEU C 140      30.924  19.876  47.276  1.00 21.22           C  
-ATOM   6092  CG  LEU C 140      30.237  19.110  48.411  1.00 18.89           C  
-ATOM   6093  CD1 LEU C 140      28.912  19.779  48.745  1.00 19.01           C  
-ATOM   6094  CD2 LEU C 140      30.013  17.669  48.000  1.00 18.37           C  
-ATOM   6095  N   LEU C 141      33.568  21.189  48.141  1.00 26.45           N  
-ATOM   6096  CA  LEU C 141      34.755  21.282  48.984  1.00 27.61           C  
-ATOM   6097  C   LEU C 141      34.849  22.654  49.639  1.00 29.37           C  
-ATOM   6098  O   LEU C 141      35.008  22.765  50.858  1.00 29.88           O  
-ATOM   6099  CB  LEU C 141      36.008  21.050  48.145  1.00 26.03           C  
-ATOM   6100  CG  LEU C 141      36.354  19.625  47.721  1.00 25.97           C  
-ATOM   6101  CD1 LEU C 141      37.406  19.656  46.615  1.00 23.62           C  
-ATOM   6102  CD2 LEU C 141      36.862  18.851  48.934  1.00 26.55           C  
-ATOM   6103  N   GLU C 142      34.753  23.695  48.814  1.00 28.94           N  
-ATOM   6104  CA  GLU C 142      34.836  25.076  49.281  1.00 28.87           C  
-ATOM   6105  C   GLU C 142      33.686  25.453  50.209  1.00 29.42           C  
-ATOM   6106  O   GLU C 142      33.866  26.267  51.118  1.00 28.54           O  
-ATOM   6107  CB  GLU C 142      34.881  26.033  48.081  1.00 29.81           C  
-ATOM   6108  CG  GLU C 142      34.979  27.515  48.435  1.00 31.03           C  
-ATOM   6109  CD  GLU C 142      36.176  27.851  49.319  1.00 33.92           C  
-ATOM   6110  OE1 GLU C 142      37.076  26.999  49.479  1.00 33.85           O  
-ATOM   6111  OE2 GLU C 142      36.219  28.980  49.851  1.00 34.55           O  
-ATOM   6112  N   ALA C 143      32.509  24.874  49.978  1.00 28.54           N  
-ATOM   6113  CA  ALA C 143      31.344  25.151  50.819  1.00 28.20           C  
-ATOM   6114  C   ALA C 143      31.542  24.490  52.176  1.00 28.69           C  
-ATOM   6115  O   ALA C 143      31.160  25.044  53.202  1.00 30.02           O  
-ATOM   6116  CB  ALA C 143      30.074  24.628  50.170  1.00 26.13           C  
-ATOM   6117  N   VAL C 144      32.132  23.301  52.175  1.00 30.06           N  
-ATOM   6118  CA  VAL C 144      32.393  22.589  53.417  1.00 32.48           C  
-ATOM   6119  C   VAL C 144      33.441  23.355  54.220  1.00 34.32           C  
-ATOM   6120  O   VAL C 144      33.253  23.617  55.406  1.00 35.22           O  
-ATOM   6121  CB  VAL C 144      32.904  21.156  53.153  1.00 32.03           C  
-ATOM   6122  CG1 VAL C 144      33.417  20.541  54.447  1.00 32.82           C  
-ATOM   6123  CG2 VAL C 144      31.779  20.301  52.585  1.00 30.35           C  
-ATOM   6124  N   ARG C 145      34.537  23.726  53.562  1.00 36.29           N  
-ATOM   6125  CA  ARG C 145      35.610  24.472  54.216  1.00 36.46           C  
-ATOM   6126  C   ARG C 145      35.110  25.811  54.761  1.00 36.63           C  
-ATOM   6127  O   ARG C 145      35.480  26.223  55.858  1.00 37.62           O  
-ATOM   6128  CB  ARG C 145      36.755  24.729  53.234  1.00 35.73           C  
-ATOM   6129  CG  ARG C 145      37.948  25.437  53.857  1.00 37.23           C  
-ATOM   6130  CD  ARG C 145      38.722  26.238  52.829  1.00 39.60           C  
-ATOM   6131  NE  ARG C 145      37.940  27.370  52.338  1.00 43.44           N  
-ATOM   6132  CZ  ARG C 145      37.632  28.441  53.068  1.00 45.95           C  
-ATOM   6133  NH1 ARG C 145      38.048  28.529  54.326  1.00 47.48           N  
-ATOM   6134  NH2 ARG C 145      36.892  29.415  52.550  1.00 45.14           N  
-ATOM   6135  N   SER C 146      34.279  26.499  53.989  1.00 36.21           N  
-ATOM   6136  CA  SER C 146      33.747  27.783  54.427  1.00 37.36           C  
-ATOM   6137  C   SER C 146      32.857  27.586  55.644  1.00 38.07           C  
-ATOM   6138  O   SER C 146      32.822  28.427  56.543  1.00 38.11           O  
-ATOM   6139  CB  SER C 146      32.945  28.448  53.306  1.00 36.64           C  
-ATOM   6140  OG  SER C 146      33.805  28.872  52.268  1.00 41.53           O  
-ATOM   6141  N   HIS C 147      32.139  26.468  55.655  1.00 37.40           N  
-ATOM   6142  CA  HIS C 147      31.243  26.125  56.748  1.00 38.65           C  
-ATOM   6143  C   HIS C 147      32.014  25.845  58.034  1.00 38.55           C  
-ATOM   6144  O   HIS C 147      31.669  26.359  59.091  1.00 39.29           O  
-ATOM   6145  CB  HIS C 147      30.408  24.895  56.379  1.00 37.30           C  
-ATOM   6146  CG  HIS C 147      29.637  24.321  57.526  1.00 37.69           C  
-ATOM   6147  ND1 HIS C 147      28.642  25.017  58.177  1.00 37.24           N  
-ATOM   6148  CD2 HIS C 147      29.733  23.125  58.154  1.00 36.84           C  
-ATOM   6149  CE1 HIS C 147      28.158  24.275  59.157  1.00 36.98           C  
-ATOM   6150  NE2 HIS C 147      28.803  23.122  59.165  1.00 37.36           N  
-ATOM   6151  N   THR C 148      33.055  25.028  57.941  1.00 39.03           N  
-ATOM   6152  CA  THR C 148      33.850  24.687  59.114  1.00 41.43           C  
-ATOM   6153  C   THR C 148      34.546  25.907  59.709  1.00 42.61           C  
-ATOM   6154  O   THR C 148      34.671  26.022  60.925  1.00 42.81           O  
-ATOM   6155  CB  THR C 148      34.911  23.615  58.786  1.00 42.19           C  
-ATOM   6156  OG1 THR C 148      35.794  24.100  57.765  1.00 42.91           O  
-ATOM   6157  CG2 THR C 148      34.239  22.336  58.311  1.00 41.65           C  
-ATOM   6158  N   ILE C 149      34.994  26.819  58.855  1.00 43.02           N  
-ATOM   6159  CA  ILE C 149      35.666  28.020  59.327  1.00 43.64           C  
-ATOM   6160  C   ILE C 149      34.676  28.998  59.949  1.00 44.66           C  
-ATOM   6161  O   ILE C 149      35.019  29.751  60.860  1.00 44.67           O  
-ATOM   6162  CB  ILE C 149      36.412  28.735  58.177  1.00 44.67           C  
-ATOM   6163  CG1 ILE C 149      37.547  27.846  57.658  1.00 45.88           C  
-ATOM   6164  CG2 ILE C 149      36.964  30.074  58.661  1.00 44.28           C  
-ATOM   6165  CD1 ILE C 149      38.614  27.513  58.700  1.00 46.82           C  
-ATOM   6166  N   ASP C 150      33.443  28.980  59.460  1.00 45.02           N  
-ATOM   6167  CA  ASP C 150      32.424  29.883  59.967  1.00 46.14           C  
-ATOM   6168  C   ASP C 150      31.756  29.378  61.247  1.00 46.91           C  
-ATOM   6169  O   ASP C 150      31.361  30.171  62.101  1.00 46.33           O  
-ATOM   6170  CB  ASP C 150      31.361  30.121  58.891  1.00 46.11           C  
-ATOM   6171  CG  ASP C 150      30.340  31.166  59.299  1.00 47.58           C  
-ATOM   6172  OD1 ASP C 150      30.738  32.325  59.549  1.00 47.70           O  
-ATOM   6173  OD2 ASP C 150      29.140  30.830  59.370  1.00 48.77           O  
-ATOM   6174  N   SER C 151      31.638  28.061  61.383  1.00 46.50           N  
-ATOM   6175  CA  SER C 151      30.989  27.480  62.553  1.00 46.84           C  
-ATOM   6176  C   SER C 151      31.940  26.736  63.490  1.00 46.68           C  
-ATOM   6177  O   SER C 151      31.516  26.216  64.522  1.00 47.45           O  
-ATOM   6178  CB  SER C 151      29.881  26.526  62.106  1.00 45.76           C  
-ATOM   6179  OG  SER C 151      30.428  25.368  61.494  1.00 46.91           O  
-ATOM   6180  N   GLY C 152      33.218  26.678  63.130  1.00 45.59           N  
-ATOM   6181  CA  GLY C 152      34.183  25.985  63.964  1.00 43.54           C  
-ATOM   6182  C   GLY C 152      33.944  24.487  63.998  1.00 43.44           C  
-ATOM   6183  O   GLY C 152      34.654  23.751  64.694  1.00 43.76           O  
-ATOM   6184  N   ARG C 153      32.944  24.028  63.249  1.00 40.94           N  
-ATOM   6185  CA  ARG C 153      32.625  22.605  63.199  1.00 39.54           C  
-ATOM   6186  C   ARG C 153      33.679  21.834  62.423  1.00 38.83           C  
-ATOM   6187  O   ARG C 153      34.552  22.419  61.780  1.00 38.65           O  
-ATOM   6188  CB  ARG C 153      31.254  22.371  62.555  1.00 39.78           C  
-ATOM   6189  CG  ARG C 153      30.084  22.956  63.328  1.00 39.67           C  
-ATOM   6190  CD  ARG C 153      28.748  22.425  62.822  1.00 40.11           C  
-ATOM   6191  NE  ARG C 153      28.653  20.970  62.952  1.00 40.71           N  
-ATOM   6192  CZ  ARG C 153      28.974  20.097  62.001  1.00 40.76           C  
-ATOM   6193  NH1 ARG C 153      29.414  20.517  60.820  1.00 43.24           N  
-ATOM   6194  NH2 ARG C 153      28.865  18.796  62.234  1.00 39.81           N  
-ATOM   6195  N   THR C 154      33.587  20.511  62.492  1.00 38.96           N  
-ATOM   6196  CA  THR C 154      34.521  19.629  61.807  1.00 38.73           C  
-ATOM   6197  C   THR C 154      33.735  18.672  60.919  1.00 38.88           C  
-ATOM   6198  O   THR C 154      32.739  18.088  61.352  1.00 40.21           O  
-ATOM   6199  CB  THR C 154      35.349  18.819  62.822  1.00 38.69           C  
-ATOM   6200  OG1 THR C 154      36.156  19.719  63.590  1.00 41.65           O  
-ATOM   6201  CG2 THR C 154      36.249  17.815  62.114  1.00 38.92           C  
-ATOM   6202  N   VAL C 155      34.180  18.514  59.679  1.00 36.72           N  
-ATOM   6203  CA  VAL C 155      33.493  17.632  58.745  1.00 35.60           C  
-ATOM   6204  C   VAL C 155      34.463  16.716  58.017  1.00 34.21           C  
-ATOM   6205  O   VAL C 155      35.568  17.124  57.669  1.00 34.72           O  
-ATOM   6206  CB  VAL C 155      32.706  18.445  57.681  1.00 35.26           C  
-ATOM   6207  CG1 VAL C 155      31.986  17.503  56.731  1.00 35.23           C  
-ATOM   6208  CG2 VAL C 155      31.711  19.373  58.353  1.00 35.81           C  
-ATOM   6209  N   LYS C 156      34.053  15.470  57.811  1.00 33.04           N  
-ATOM   6210  CA  LYS C 156      34.868  14.516  57.080  1.00 34.01           C  
-ATOM   6211  C   LYS C 156      34.272  14.476  55.676  1.00 33.28           C  
-ATOM   6212  O   LYS C 156      33.049  14.537  55.508  1.00 30.89           O  
-ATOM   6213  CB  LYS C 156      34.840  13.144  57.757  1.00 37.14           C  
-ATOM   6214  CG  LYS C 156      35.597  13.136  59.087  1.00 41.35           C  
-ATOM   6215  CD  LYS C 156      35.890  11.726  59.593  1.00 43.52           C  
-ATOM   6216  CE  LYS C 156      36.839  11.765  60.790  1.00 45.73           C  
-ATOM   6217  NZ  LYS C 156      37.320  10.413  61.206  1.00 47.53           N  
-ATOM   6218  N   TYR C 157      35.135  14.368  54.671  1.00 32.60           N  
-ATOM   6219  CA  TYR C 157      34.692  14.419  53.279  1.00 32.29           C  
-ATOM   6220  C   TYR C 157      35.179  13.282  52.377  1.00 29.46           C  
-ATOM   6221  O   TYR C 157      36.357  12.930  52.383  1.00 29.50           O  
-ATOM   6222  CB  TYR C 157      35.144  15.772  52.708  1.00 32.00           C  
-ATOM   6223  CG  TYR C 157      34.675  16.126  51.313  1.00 32.74           C  
-ATOM   6224  CD1 TYR C 157      33.667  17.073  51.117  1.00 32.89           C  
-ATOM   6225  CD2 TYR C 157      35.300  15.589  50.188  1.00 33.25           C  
-ATOM   6226  CE1 TYR C 157      33.303  17.486  49.838  1.00 32.64           C  
-ATOM   6227  CE2 TYR C 157      34.940  15.993  48.902  1.00 33.18           C  
-ATOM   6228  CZ  TYR C 157      33.944  16.945  48.737  1.00 33.07           C  
-ATOM   6229  OH  TYR C 157      33.605  17.365  47.474  1.00 33.20           O  
-ATOM   6230  N   TYR C 158      34.256  12.727  51.595  1.00 27.77           N  
-ATOM   6231  CA  TYR C 158      34.564  11.650  50.656  1.00 27.16           C  
-ATOM   6232  C   TYR C 158      34.319  12.103  49.215  1.00 27.52           C  
-ATOM   6233  O   TYR C 158      33.288  12.705  48.913  1.00 28.36           O  
-ATOM   6234  CB  TYR C 158      33.684  10.426  50.922  1.00 26.60           C  
-ATOM   6235  CG  TYR C 158      33.892   9.311  49.915  1.00 26.61           C  
-ATOM   6236  CD1 TYR C 158      34.935   8.400  50.060  1.00 26.60           C  
-ATOM   6237  CD2 TYR C 158      33.085   9.209  48.780  1.00 27.93           C  
-ATOM   6238  CE1 TYR C 158      35.173   7.415  49.097  1.00 26.58           C  
-ATOM   6239  CE2 TYR C 158      33.318   8.228  47.807  1.00 25.98           C  
-ATOM   6240  CZ  TYR C 158      34.362   7.338  47.975  1.00 26.64           C  
-ATOM   6241  OH  TYR C 158      34.606   6.374  47.024  1.00 25.98           O  
-ATOM   6242  N   GLN C 159      35.264  11.806  48.330  1.00 27.58           N  
-ATOM   6243  CA  GLN C 159      35.126  12.147  46.917  1.00 27.73           C  
-ATOM   6244  C   GLN C 159      35.070  10.868  46.109  1.00 27.43           C  
-ATOM   6245  O   GLN C 159      35.944  10.014  46.232  1.00 27.17           O  
-ATOM   6246  CB  GLN C 159      36.308  12.991  46.429  1.00 28.60           C  
-ATOM   6247  CG  GLN C 159      36.454  13.073  44.898  1.00 26.36           C  
-ATOM   6248  CD  GLN C 159      35.218  13.626  44.182  1.00 24.66           C  
-ATOM   6249  OE1 GLN C 159      34.475  14.437  44.728  1.00 24.69           O  
-ATOM   6250  NE2 GLN C 159      35.018  13.204  42.942  1.00 21.64           N  
-ATOM   6251  N   ALA C 160      34.041  10.741  45.278  1.00 27.47           N  
-ATOM   6252  CA  ALA C 160      33.884   9.558  44.444  1.00 26.82           C  
-ATOM   6253  C   ALA C 160      34.808   9.587  43.229  1.00 26.60           C  
-ATOM   6254  O   ALA C 160      34.437  10.082  42.167  1.00 25.83           O  
-ATOM   6255  CB  ALA C 160      32.428   9.422  43.989  1.00 26.56           C  
-ATOM   6256  N   GLY C 161      36.012   9.054  43.400  1.00 28.11           N  
-ATOM   6257  CA  GLY C 161      36.969   8.990  42.313  1.00 27.78           C  
-ATOM   6258  C   GLY C 161      36.670   7.766  41.465  1.00 29.52           C  
-ATOM   6259  O   GLY C 161      35.919   6.883  41.884  1.00 29.16           O  
-ATOM   6260  N   SER C 162      37.264   7.694  40.281  1.00 30.53           N  
-ATOM   6261  CA  SER C 162      37.007   6.583  39.377  1.00 31.77           C  
-ATOM   6262  C   SER C 162      38.239   6.022  38.675  1.00 33.14           C  
-ATOM   6263  O   SER C 162      39.185   6.751  38.368  1.00 33.58           O  
-ATOM   6264  CB  SER C 162      35.994   7.023  38.319  1.00 32.58           C  
-ATOM   6265  OG  SER C 162      36.013   6.149  37.206  1.00 32.36           O  
-ATOM   6266  N   SER C 163      38.209   4.718  38.409  1.00 31.27           N  
-ATOM   6267  CA  SER C 163      39.305   4.050  37.722  1.00 32.43           C  
-ATOM   6268  C   SER C 163      39.444   4.613  36.309  1.00 31.24           C  
-ATOM   6269  O   SER C 163      40.451   4.407  35.632  1.00 31.16           O  
-ATOM   6270  CB  SER C 163      39.039   2.545  37.658  1.00 34.56           C  
-ATOM   6271  OG  SER C 163      37.757   2.271  37.112  1.00 34.93           O  
-ATOM   6272  N   GLU C 164      38.420   5.331  35.873  1.00 29.91           N  
-ATOM   6273  CA  GLU C 164      38.416   5.932  34.550  1.00 29.49           C  
-ATOM   6274  C   GLU C 164      39.533   6.974  34.469  1.00 29.01           C  
-ATOM   6275  O   GLU C 164      39.971   7.351  33.382  1.00 27.68           O  
-ATOM   6276  CB  GLU C 164      37.060   6.585  34.302  1.00 30.29           C  
-ATOM   6277  CG  GLU C 164      36.662   6.714  32.848  1.00 36.71           C  
-ATOM   6278  CD  GLU C 164      36.453   5.377  32.169  1.00 37.68           C  
-ATOM   6279  OE1 GLU C 164      36.003   4.418  32.830  1.00 40.43           O  
-ATOM   6280  OE2 GLU C 164      36.724   5.290  30.959  1.00 40.62           O  
-ATOM   6281  N   MET C 165      39.998   7.436  35.627  1.00 29.15           N  
-ATOM   6282  CA  MET C 165      41.068   8.428  35.665  1.00 28.99           C  
-ATOM   6283  C   MET C 165      42.372   7.864  35.110  1.00 29.41           C  
-ATOM   6284  O   MET C 165      43.157   8.594  34.512  1.00 32.25           O  
-ATOM   6285  CB  MET C 165      41.285   8.939  37.094  1.00 26.88           C  
-ATOM   6286  CG  MET C 165      40.054   9.599  37.691  1.00 26.26           C  
-ATOM   6287  SD  MET C 165      40.350  10.390  39.274  1.00 30.78           S  
-ATOM   6288  CE  MET C 165      40.902   8.982  40.267  1.00 27.93           C  
-ATOM   6289  N   PHE C 166      42.601   6.568  35.305  1.00 29.39           N  
-ATOM   6290  CA  PHE C 166      43.815   5.928  34.802  1.00 29.49           C  
-ATOM   6291  C   PHE C 166      43.759   5.860  33.283  1.00 29.57           C  
-ATOM   6292  O   PHE C 166      44.788   5.822  32.608  1.00 30.33           O  
-ATOM   6293  CB  PHE C 166      43.959   4.513  35.368  1.00 29.34           C  
-ATOM   6294  CG  PHE C 166      44.024   4.464  36.865  1.00 29.24           C  
-ATOM   6295  CD1 PHE C 166      43.078   3.748  37.590  1.00 28.66           C  
-ATOM   6296  CD2 PHE C 166      45.018   5.156  37.554  1.00 29.15           C  
-ATOM   6297  CE1 PHE C 166      43.116   3.721  38.982  1.00 29.46           C  
-ATOM   6298  CE2 PHE C 166      45.067   5.137  38.947  1.00 30.43           C  
-ATOM   6299  CZ  PHE C 166      44.113   4.418  39.663  1.00 30.61           C  
-ATOM   6300  N   GLY C 167      42.545   5.842  32.749  1.00 30.10           N  
-ATOM   6301  CA  GLY C 167      42.378   5.785  31.310  1.00 31.94           C  
-ATOM   6302  C   GLY C 167      43.194   4.701  30.628  1.00 32.52           C  
-ATOM   6303  O   GLY C 167      43.073   3.522  30.959  1.00 30.88           O  
-ATOM   6304  N   SER C 168      44.036   5.113  29.683  1.00 32.85           N  
-ATOM   6305  CA  SER C 168      44.866   4.194  28.909  1.00 32.65           C  
-ATOM   6306  C   SER C 168      46.079   3.615  29.624  1.00 34.26           C  
-ATOM   6307  O   SER C 168      46.794   2.791  29.052  1.00 33.58           O  
-ATOM   6308  CB  SER C 168      45.329   4.879  27.623  1.00 32.37           C  
-ATOM   6309  OG  SER C 168      45.992   6.102  27.900  1.00 29.77           O  
-ATOM   6310  N   THR C 169      46.328   4.043  30.859  1.00 35.57           N  
-ATOM   6311  CA  THR C 169      47.466   3.516  31.600  1.00 35.25           C  
-ATOM   6312  C   THR C 169      47.226   2.025  31.827  1.00 36.81           C  
-ATOM   6313  O   THR C 169      46.132   1.616  32.222  1.00 37.08           O  
-ATOM   6314  CB  THR C 169      47.643   4.222  32.964  1.00 36.86           C  
-ATOM   6315  OG1 THR C 169      47.848   5.627  32.757  1.00 36.44           O  
-ATOM   6316  CG2 THR C 169      48.844   3.646  33.706  1.00 32.58           C  
-ATOM   6317  N   PRO C 170      48.249   1.193  31.572  1.00 38.15           N  
-ATOM   6318  CA  PRO C 170      48.165  -0.263  31.738  1.00 37.79           C  
-ATOM   6319  C   PRO C 170      47.915  -0.753  33.162  1.00 37.81           C  
-ATOM   6320  O   PRO C 170      48.337  -0.123  34.130  1.00 38.60           O  
-ATOM   6321  CB  PRO C 170      49.503  -0.751  31.181  1.00 39.39           C  
-ATOM   6322  CG  PRO C 170      50.426   0.403  31.443  1.00 39.59           C  
-ATOM   6323  CD  PRO C 170      49.574   1.585  31.057  1.00 38.91           C  
-ATOM   6324  N   PRO C 171      47.207  -1.889  33.302  1.00 37.39           N  
-ATOM   6325  CA  PRO C 171      46.893  -2.482  34.605  1.00 36.05           C  
-ATOM   6326  C   PRO C 171      48.020  -3.386  35.089  1.00 36.97           C  
-ATOM   6327  O   PRO C 171      48.909  -3.744  34.319  1.00 37.44           O  
-ATOM   6328  CB  PRO C 171      45.623  -3.267  34.317  1.00 36.51           C  
-ATOM   6329  CG  PRO C 171      45.887  -3.774  32.934  1.00 36.47           C  
-ATOM   6330  CD  PRO C 171      46.450  -2.562  32.229  1.00 35.87           C  
-ATOM   6331  N   PRO C 172      47.999  -3.766  36.376  1.00 37.24           N  
-ATOM   6332  CA  PRO C 172      46.977  -3.374  37.349  1.00 37.50           C  
-ATOM   6333  C   PRO C 172      47.205  -1.938  37.811  1.00 37.19           C  
-ATOM   6334  O   PRO C 172      48.346  -1.513  37.983  1.00 39.52           O  
-ATOM   6335  CB  PRO C 172      47.169  -4.386  38.468  1.00 37.44           C  
-ATOM   6336  CG  PRO C 172      48.649  -4.603  38.449  1.00 39.06           C  
-ATOM   6337  CD  PRO C 172      48.939  -4.733  36.969  1.00 38.15           C  
-ATOM   6338  N   GLN C 173      46.120  -1.193  38.002  1.00 36.10           N  
-ATOM   6339  CA  GLN C 173      46.221   0.192  38.436  1.00 35.27           C  
-ATOM   6340  C   GLN C 173      46.035   0.305  39.945  1.00 34.87           C  
-ATOM   6341  O   GLN C 173      45.090  -0.253  40.501  1.00 35.71           O  
-ATOM   6342  CB  GLN C 173      45.167   1.056  37.727  1.00 33.42           C  
-ATOM   6343  CG  GLN C 173      45.317   1.166  36.210  1.00 31.50           C  
-ATOM   6344  CD  GLN C 173      44.563   0.083  35.444  1.00 32.89           C  
-ATOM   6345  OE1 GLN C 173      43.768  -0.670  36.014  1.00 33.00           O  
-ATOM   6346  NE2 GLN C 173      44.798   0.017  34.140  1.00 32.37           N  
-ATOM   6347  N   SER C 174      46.943   1.025  40.601  1.00 35.00           N  
-ATOM   6348  CA  SER C 174      46.880   1.234  42.046  1.00 35.59           C  
-ATOM   6349  C   SER C 174      46.879   2.737  42.343  1.00 35.95           C  
-ATOM   6350  O   SER C 174      46.834   3.550  41.424  1.00 36.18           O  
-ATOM   6351  CB  SER C 174      48.073   0.560  42.740  1.00 36.66           C  
-ATOM   6352  OG  SER C 174      49.307   1.139  42.348  1.00 38.04           O  
-ATOM   6353  N   GLU C 175      46.934   3.105  43.619  1.00 36.07           N  
-ATOM   6354  CA  GLU C 175      46.920   4.512  44.003  1.00 36.92           C  
-ATOM   6355  C   GLU C 175      48.088   5.313  43.444  1.00 36.93           C  
-ATOM   6356  O   GLU C 175      48.005   6.535  43.324  1.00 37.32           O  
-ATOM   6357  CB  GLU C 175      46.901   4.663  45.530  1.00 37.15           C  
-ATOM   6358  CG  GLU C 175      45.666   4.094  46.207  1.00 37.61           C  
-ATOM   6359  CD  GLU C 175      45.787   2.610  46.493  1.00 38.52           C  
-ATOM   6360  OE1 GLU C 175      46.688   1.963  45.919  1.00 38.30           O  
-ATOM   6361  OE2 GLU C 175      44.976   2.088  47.289  1.00 39.15           O  
-ATOM   6362  N   THR C 176      49.175   4.636  43.100  1.00 37.33           N  
-ATOM   6363  CA  THR C 176      50.346   5.327  42.572  1.00 38.10           C  
-ATOM   6364  C   THR C 176      50.389   5.320  41.049  1.00 36.79           C  
-ATOM   6365  O   THR C 176      51.256   5.949  40.442  1.00 37.34           O  
-ATOM   6366  CB  THR C 176      51.641   4.696  43.105  1.00 39.46           C  
-ATOM   6367  OG1 THR C 176      51.693   3.315  42.721  1.00 41.72           O  
-ATOM   6368  CG2 THR C 176      51.691   4.795  44.619  1.00 39.28           C  
-ATOM   6369  N   THR C 177      49.453   4.610  40.433  1.00 34.56           N  
-ATOM   6370  CA  THR C 177      49.403   4.540  38.979  1.00 34.61           C  
-ATOM   6371  C   THR C 177      49.046   5.905  38.380  1.00 33.16           C  
-ATOM   6372  O   THR C 177      48.123   6.575  38.839  1.00 34.64           O  
-ATOM   6373  CB  THR C 177      48.381   3.481  38.519  1.00 34.39           C  
-ATOM   6374  OG1 THR C 177      48.707   2.222  39.123  1.00 36.10           O  
-ATOM   6375  CG2 THR C 177      48.409   3.325  37.004  1.00 32.62           C  
-ATOM   6376  N   PRO C 178      49.791   6.339  37.354  1.00 31.55           N  
-ATOM   6377  CA  PRO C 178      49.552   7.628  36.698  1.00 31.08           C  
-ATOM   6378  C   PRO C 178      48.259   7.694  35.892  1.00 31.46           C  
-ATOM   6379  O   PRO C 178      47.814   6.693  35.324  1.00 32.93           O  
-ATOM   6380  CB  PRO C 178      50.794   7.809  35.830  1.00 30.25           C  
-ATOM   6381  CG  PRO C 178      51.167   6.398  35.481  1.00 32.44           C  
-ATOM   6382  CD  PRO C 178      50.980   5.673  36.794  1.00 30.80           C  
-ATOM   6383  N   PHE C 179      47.659   8.883  35.851  1.00 30.80           N  
-ATOM   6384  CA  PHE C 179      46.414   9.089  35.121  1.00 30.56           C  
-ATOM   6385  C   PHE C 179      46.666   9.462  33.665  1.00 31.72           C  
-ATOM   6386  O   PHE C 179      47.684  10.069  33.333  1.00 32.98           O  
-ATOM   6387  CB  PHE C 179      45.581  10.226  35.732  1.00 29.35           C  
-ATOM   6388  CG  PHE C 179      45.197  10.027  37.172  1.00 30.49           C  
-ATOM   6389  CD1 PHE C 179      44.916   8.761  37.676  1.00 29.98           C  
-ATOM   6390  CD2 PHE C 179      45.054  11.130  38.012  1.00 28.93           C  
-ATOM   6391  CE1 PHE C 179      44.498   8.597  38.995  1.00 31.91           C  
-ATOM   6392  CE2 PHE C 179      44.637  10.978  39.328  1.00 30.48           C  
-ATOM   6393  CZ  PHE C 179      44.357   9.707  39.823  1.00 30.02           C  
-ATOM   6394  N   HIS C 180      45.723   9.091  32.806  1.00 30.37           N  
-ATOM   6395  CA  HIS C 180      45.764   9.439  31.390  1.00 31.20           C  
-ATOM   6396  C   HIS C 180      44.319   9.319  30.915  1.00 31.15           C  
-ATOM   6397  O   HIS C 180      43.971   8.413  30.156  1.00 30.45           O  
-ATOM   6398  CB  HIS C 180      46.660   8.503  30.581  1.00 30.51           C  
-ATOM   6399  CG  HIS C 180      46.911   8.983  29.184  1.00 31.80           C  
-ATOM   6400  ND1 HIS C 180      48.147   9.414  28.754  1.00 33.18           N  
-ATOM   6401  CD2 HIS C 180      46.072   9.143  28.132  1.00 32.49           C  
-ATOM   6402  CE1 HIS C 180      48.060   9.819  27.499  1.00 32.08           C  
-ATOM   6403  NE2 HIS C 180      46.811   9.666  27.098  1.00 32.07           N  
-ATOM   6404  N   PRO C 181      43.459  10.246  31.368  1.00 29.46           N  
-ATOM   6405  CA  PRO C 181      42.034  10.281  31.024  1.00 28.63           C  
-ATOM   6406  C   PRO C 181      41.766  10.221  29.524  1.00 29.06           C  
-ATOM   6407  O   PRO C 181      42.468  10.844  28.725  1.00 27.01           O  
-ATOM   6408  CB  PRO C 181      41.558  11.582  31.668  1.00 28.15           C  
-ATOM   6409  CG  PRO C 181      42.772  12.449  31.614  1.00 28.13           C  
-ATOM   6410  CD  PRO C 181      43.868  11.498  32.027  1.00 28.51           C  
-ATOM   6411  N   ARG C 182      40.737   9.468  29.150  1.00 29.77           N  
-ATOM   6412  CA  ARG C 182      40.383   9.302  27.747  1.00 28.74           C  
-ATOM   6413  C   ARG C 182      39.030   9.921  27.393  1.00 28.45           C  
-ATOM   6414  O   ARG C 182      38.534   9.747  26.280  1.00 31.08           O  
-ATOM   6415  CB  ARG C 182      40.396   7.810  27.400  1.00 28.42           C  
-ATOM   6416  CG  ARG C 182      41.769   7.160  27.533  1.00 28.29           C  
-ATOM   6417  CD  ARG C 182      42.644   7.471  26.333  1.00 28.48           C  
-ATOM   6418  NE  ARG C 182      42.272   6.648  25.186  1.00 31.68           N  
-ATOM   6419  CZ  ARG C 182      42.676   6.860  23.936  1.00 31.81           C  
-ATOM   6420  NH1 ARG C 182      43.473   7.879  23.654  1.00 32.33           N  
-ATOM   6421  NH2 ARG C 182      42.273   6.051  22.961  1.00 34.40           N  
-ATOM   6422  N   SER C 183      38.439  10.651  28.336  1.00 28.62           N  
-ATOM   6423  CA  SER C 183      37.146  11.305  28.108  1.00 27.58           C  
-ATOM   6424  C   SER C 183      37.009  12.547  28.979  1.00 27.93           C  
-ATOM   6425  O   SER C 183      37.674  12.666  30.009  1.00 29.69           O  
-ATOM   6426  CB  SER C 183      36.005  10.358  28.448  1.00 27.37           C  
-ATOM   6427  OG  SER C 183      36.021  10.056  29.833  1.00 32.88           O  
-ATOM   6428  N   PRO C 184      36.143  13.494  28.576  1.00 27.54           N  
-ATOM   6429  CA  PRO C 184      35.951  14.712  29.366  1.00 26.58           C  
-ATOM   6430  C   PRO C 184      35.577  14.334  30.793  1.00 26.79           C  
-ATOM   6431  O   PRO C 184      36.033  14.958  31.747  1.00 26.26           O  
-ATOM   6432  CB  PRO C 184      34.823  15.420  28.629  1.00 26.07           C  
-ATOM   6433  CG  PRO C 184      35.110  15.054  27.195  1.00 27.00           C  
-ATOM   6434  CD  PRO C 184      35.394  13.570  27.308  1.00 27.19           C  
-ATOM   6435  N   TYR C 185      34.750  13.298  30.927  1.00 25.80           N  
-ATOM   6436  CA  TYR C 185      34.333  12.814  32.238  1.00 25.55           C  
-ATOM   6437  C   TYR C 185      35.567  12.432  33.062  1.00 26.64           C  
-ATOM   6438  O   TYR C 185      35.718  12.858  34.208  1.00 25.57           O  
-ATOM   6439  CB  TYR C 185      33.437  11.582  32.090  1.00 24.72           C  
-ATOM   6440  CG  TYR C 185      33.276  10.795  33.375  1.00 25.20           C  
-ATOM   6441  CD1 TYR C 185      32.352  11.180  34.343  1.00 24.65           C  
-ATOM   6442  CD2 TYR C 185      34.080   9.688  33.638  1.00 24.01           C  
-ATOM   6443  CE1 TYR C 185      32.233  10.480  35.545  1.00 24.38           C  
-ATOM   6444  CE2 TYR C 185      33.972   8.987  34.831  1.00 23.57           C  
-ATOM   6445  CZ  TYR C 185      33.049   9.384  35.778  1.00 23.36           C  
-ATOM   6446  OH  TYR C 185      32.933   8.679  36.954  1.00 25.08           O  
-ATOM   6447  N   ALA C 186      36.435  11.620  32.462  1.00 26.01           N  
-ATOM   6448  CA  ALA C 186      37.653  11.144  33.112  1.00 26.25           C  
-ATOM   6449  C   ALA C 186      38.553  12.295  33.536  1.00 25.37           C  
-ATOM   6450  O   ALA C 186      39.040  12.333  34.667  1.00 25.92           O  
-ATOM   6451  CB  ALA C 186      38.407  10.211  32.173  1.00 26.69           C  
-ATOM   6452  N   ALA C 187      38.778  13.222  32.613  1.00 24.35           N  
-ATOM   6453  CA  ALA C 187      39.604  14.386  32.882  1.00 22.24           C  
-ATOM   6454  C   ALA C 187      38.997  15.177  34.047  1.00 22.94           C  
-ATOM   6455  O   ALA C 187      39.717  15.668  34.916  1.00 20.60           O  
-ATOM   6456  CB  ALA C 187      39.689  15.261  31.633  1.00 20.96           C  
-ATOM   6457  N   SER C 188      37.671  15.284  34.065  1.00 21.48           N  
-ATOM   6458  CA  SER C 188      36.989  16.014  35.128  1.00 23.30           C  
-ATOM   6459  C   SER C 188      37.115  15.309  36.478  1.00 22.36           C  
-ATOM   6460  O   SER C 188      37.222  15.962  37.515  1.00 22.09           O  
-ATOM   6461  CB  SER C 188      35.518  16.230  34.768  1.00 23.89           C  
-ATOM   6462  OG  SER C 188      35.409  17.133  33.679  1.00 23.45           O  
-ATOM   6463  N   LYS C 189      37.098  13.981  36.472  1.00 22.84           N  
-ATOM   6464  CA  LYS C 189      37.267  13.245  37.716  1.00 24.02           C  
-ATOM   6465  C   LYS C 189      38.701  13.450  38.210  1.00 24.03           C  
-ATOM   6466  O   LYS C 189      38.939  13.512  39.412  1.00 26.94           O  
-ATOM   6467  CB  LYS C 189      36.976  11.758  37.520  1.00 24.07           C  
-ATOM   6468  CG  LYS C 189      35.502  11.416  37.568  1.00 23.86           C  
-ATOM   6469  CD  LYS C 189      34.914  11.683  38.952  1.00 24.78           C  
-ATOM   6470  CE  LYS C 189      33.463  11.246  39.011  1.00 24.06           C  
-ATOM   6471  NZ  LYS C 189      32.812  11.572  40.315  1.00 27.14           N  
-ATOM   6472  N   CYS C 190      39.652  13.568  37.287  1.00 23.78           N  
-ATOM   6473  CA  CYS C 190      41.043  13.801  37.677  1.00 26.21           C  
-ATOM   6474  C   CYS C 190      41.155  15.164  38.356  1.00 26.18           C  
-ATOM   6475  O   CYS C 190      41.915  15.329  39.311  1.00 24.93           O  
-ATOM   6476  CB  CYS C 190      41.982  13.762  36.462  1.00 25.06           C  
-ATOM   6477  SG  CYS C 190      42.138  12.132  35.669  1.00 25.72           S  
-ATOM   6478  N   ALA C 191      40.394  16.136  37.854  1.00 26.36           N  
-ATOM   6479  CA  ALA C 191      40.394  17.479  38.424  1.00 24.88           C  
-ATOM   6480  C   ALA C 191      39.831  17.431  39.841  1.00 25.96           C  
-ATOM   6481  O   ALA C 191      40.433  17.962  40.770  1.00 25.92           O  
-ATOM   6482  CB  ALA C 191      39.564  18.415  37.567  1.00 23.78           C  
-ATOM   6483  N   ALA C 192      38.679  16.787  40.001  1.00 25.07           N  
-ATOM   6484  CA  ALA C 192      38.046  16.675  41.309  1.00 26.45           C  
-ATOM   6485  C   ALA C 192      38.973  15.975  42.299  1.00 27.52           C  
-ATOM   6486  O   ALA C 192      39.026  16.329  43.478  1.00 27.87           O  
-ATOM   6487  CB  ALA C 192      36.734  15.907  41.194  1.00 25.15           C  
-ATOM   6488  N   HIS C 193      39.695  14.975  41.809  1.00 27.02           N  
-ATOM   6489  CA  HIS C 193      40.629  14.221  42.631  1.00 28.76           C  
-ATOM   6490  C   HIS C 193      41.669  15.173  43.212  1.00 28.76           C  
-ATOM   6491  O   HIS C 193      41.918  15.185  44.414  1.00 29.66           O  
-ATOM   6492  CB  HIS C 193      41.330  13.164  41.774  1.00 30.64           C  
-ATOM   6493  CG  HIS C 193      42.311  12.324  42.528  1.00 30.44           C  
-ATOM   6494  ND1 HIS C 193      41.947  11.177  43.200  1.00 32.92           N  
-ATOM   6495  CD2 HIS C 193      43.643  12.467  42.722  1.00 31.45           C  
-ATOM   6496  CE1 HIS C 193      43.014  10.648  43.773  1.00 31.90           C  
-ATOM   6497  NE2 HIS C 193      44.055  11.412  43.499  1.00 32.30           N  
-ATOM   6498  N   TRP C 194      42.273  15.971  42.342  1.00 27.35           N  
-ATOM   6499  CA  TRP C 194      43.289  16.923  42.752  1.00 28.81           C  
-ATOM   6500  C   TRP C 194      42.772  18.074  43.597  1.00 28.30           C  
-ATOM   6501  O   TRP C 194      43.473  18.550  44.490  1.00 28.08           O  
-ATOM   6502  CB  TRP C 194      44.026  17.440  41.524  1.00 30.69           C  
-ATOM   6503  CG  TRP C 194      44.978  16.421  41.038  1.00 34.74           C  
-ATOM   6504  CD1 TRP C 194      45.035  15.870  39.793  1.00 35.02           C  
-ATOM   6505  CD2 TRP C 194      45.989  15.770  41.817  1.00 36.78           C  
-ATOM   6506  NE1 TRP C 194      46.018  14.909  39.749  1.00 34.53           N  
-ATOM   6507  CE2 TRP C 194      46.618  14.827  40.979  1.00 36.41           C  
-ATOM   6508  CE3 TRP C 194      46.424  15.895  43.150  1.00 39.47           C  
-ATOM   6509  CZ2 TRP C 194      47.665  14.003  41.427  1.00 39.33           C  
-ATOM   6510  CZ3 TRP C 194      47.464  15.079  43.596  1.00 38.24           C  
-ATOM   6511  CH2 TRP C 194      48.071  14.144  42.733  1.00 40.17           C  
-ATOM   6512  N   TYR C 195      41.555  18.528  43.327  1.00 26.64           N  
-ATOM   6513  CA  TYR C 195      40.990  19.602  44.131  1.00 26.28           C  
-ATOM   6514  C   TYR C 195      40.864  19.051  45.549  1.00 27.10           C  
-ATOM   6515  O   TYR C 195      41.203  19.723  46.516  1.00 27.68           O  
-ATOM   6516  CB  TYR C 195      39.602  20.001  43.613  1.00 23.76           C  
-ATOM   6517  CG  TYR C 195      39.609  20.756  42.303  1.00 22.07           C  
-ATOM   6518  CD1 TYR C 195      38.576  20.591  41.378  1.00 22.58           C  
-ATOM   6519  CD2 TYR C 195      40.645  21.634  41.984  1.00 21.13           C  
-ATOM   6520  CE1 TYR C 195      38.576  21.276  40.162  1.00 22.39           C  
-ATOM   6521  CE2 TYR C 195      40.654  22.328  40.775  1.00 22.15           C  
-ATOM   6522  CZ  TYR C 195      39.618  22.142  39.867  1.00 24.71           C  
-ATOM   6523  OH  TYR C 195      39.633  22.806  38.659  1.00 27.65           O  
-ATOM   6524  N   THR C 196      40.382  17.813  45.648  1.00 27.13           N  
-ATOM   6525  CA  THR C 196      40.179  17.143  46.924  1.00 27.82           C  
-ATOM   6526  C   THR C 196      41.495  16.952  47.664  1.00 28.29           C  
-ATOM   6527  O   THR C 196      41.594  17.240  48.853  1.00 30.15           O  
-ATOM   6528  CB  THR C 196      39.512  15.767  46.726  1.00 25.60           C  
-ATOM   6529  OG1 THR C 196      38.302  15.932  45.980  1.00 27.15           O  
-ATOM   6530  CG2 THR C 196      39.173  15.138  48.070  1.00 23.94           C  
-ATOM   6531  N   VAL C 197      42.503  16.463  46.954  1.00 28.85           N  
-ATOM   6532  CA  VAL C 197      43.807  16.256  47.551  1.00 29.27           C  
-ATOM   6533  C   VAL C 197      44.377  17.594  47.991  1.00 29.75           C  
-ATOM   6534  O   VAL C 197      45.001  17.691  49.043  1.00 28.09           O  
-ATOM   6535  CB  VAL C 197      44.784  15.612  46.557  1.00 29.54           C  
-ATOM   6536  CG1 VAL C 197      46.182  15.560  47.165  1.00 30.79           C  
-ATOM   6537  CG2 VAL C 197      44.310  14.214  46.195  1.00 29.59           C  
-ATOM   6538  N   ASN C 198      44.153  18.628  47.183  1.00 30.58           N  
-ATOM   6539  CA  ASN C 198      44.670  19.953  47.493  1.00 31.43           C  
-ATOM   6540  C   ASN C 198      44.052  20.524  48.765  1.00 31.99           C  
-ATOM   6541  O   ASN C 198      44.740  21.182  49.541  1.00 34.23           O  
-ATOM   6542  CB  ASN C 198      44.432  20.911  46.322  1.00 31.45           C  
-ATOM   6543  CG  ASN C 198      45.121  22.253  46.512  1.00 32.76           C  
-ATOM   6544  OD1 ASN C 198      44.555  23.297  46.192  1.00 35.82           O  
-ATOM   6545  ND2 ASN C 198      46.352  22.232  47.019  1.00 31.34           N  
-ATOM   6546  N   TYR C 199      42.763  20.277  48.985  1.00 30.94           N  
-ATOM   6547  CA  TYR C 199      42.102  20.780  50.186  1.00 31.94           C  
-ATOM   6548  C   TYR C 199      42.579  20.053  51.435  1.00 31.32           C  
-ATOM   6549  O   TYR C 199      42.679  20.643  52.510  1.00 31.89           O  
-ATOM   6550  CB  TYR C 199      40.579  20.667  50.058  1.00 29.71           C  
-ATOM   6551  CG  TYR C 199      39.957  21.925  49.504  1.00 30.84           C  
-ATOM   6552  CD1 TYR C 199      40.393  22.462  48.291  1.00 29.91           C  
-ATOM   6553  CD2 TYR C 199      38.972  22.615  50.213  1.00 31.11           C  
-ATOM   6554  CE1 TYR C 199      39.873  23.653  47.803  1.00 30.74           C  
-ATOM   6555  CE2 TYR C 199      38.442  23.815  49.729  1.00 30.54           C  
-ATOM   6556  CZ  TYR C 199      38.901  24.325  48.526  1.00 30.74           C  
-ATOM   6557  OH  TYR C 199      38.412  25.516  48.046  1.00 33.52           O  
-ATOM   6558  N   ARG C 200      42.875  18.769  51.288  1.00 32.09           N  
-ATOM   6559  CA  ARG C 200      43.359  17.974  52.402  1.00 32.09           C  
-ATOM   6560  C   ARG C 200      44.733  18.490  52.812  1.00 33.63           C  
-ATOM   6561  O   ARG C 200      44.983  18.761  53.989  1.00 34.03           O  
-ATOM   6562  CB  ARG C 200      43.460  16.502  51.996  1.00 31.20           C  
-ATOM   6563  CG  ARG C 200      44.193  15.641  53.012  1.00 30.62           C  
-ATOM   6564  CD  ARG C 200      44.143  14.180  52.643  1.00 27.47           C  
-ATOM   6565  NE  ARG C 200      44.949  13.857  51.474  1.00 28.37           N  
-ATOM   6566  CZ  ARG C 200      44.546  13.041  50.507  1.00 29.20           C  
-ATOM   6567  NH1 ARG C 200      43.344  12.484  50.575  1.00 29.96           N  
-ATOM   6568  NH2 ARG C 200      45.343  12.763  49.484  1.00 30.56           N  
-ATOM   6569  N   GLU C 201      45.614  18.633  51.825  1.00 33.03           N  
-ATOM   6570  CA  GLU C 201      46.973  19.099  52.056  1.00 32.63           C  
-ATOM   6571  C   GLU C 201      47.088  20.578  52.410  1.00 32.46           C  
-ATOM   6572  O   GLU C 201      47.921  20.952  53.231  1.00 33.03           O  
-ATOM   6573  CB  GLU C 201      47.841  18.802  50.829  1.00 31.53           C  
-ATOM   6574  CG  GLU C 201      47.993  17.320  50.543  1.00 32.04           C  
-ATOM   6575  CD  GLU C 201      48.876  17.031  49.346  1.00 31.23           C  
-ATOM   6576  OE1 GLU C 201      49.130  15.839  49.085  1.00 32.75           O  
-ATOM   6577  OE2 GLU C 201      49.314  17.985  48.667  1.00 30.26           O  
-ATOM   6578  N   ALA C 202      46.251  21.414  51.802  1.00 33.62           N  
-ATOM   6579  CA  ALA C 202      46.295  22.855  52.052  1.00 32.34           C  
-ATOM   6580  C   ALA C 202      45.599  23.306  53.327  1.00 32.62           C  
-ATOM   6581  O   ALA C 202      46.136  24.132  54.065  1.00 32.33           O  
-ATOM   6582  CB  ALA C 202      45.713  23.609  50.863  1.00 33.06           C  
-ATOM   6583  N   TYR C 203      44.407  22.779  53.589  1.00 32.69           N  
-ATOM   6584  CA  TYR C 203      43.663  23.174  54.782  1.00 33.74           C  
-ATOM   6585  C   TYR C 203      43.557  22.085  55.841  1.00 32.74           C  
-ATOM   6586  O   TYR C 203      42.911  22.277  56.865  1.00 34.24           O  
-ATOM   6587  CB  TYR C 203      42.251  23.627  54.406  1.00 33.44           C  
-ATOM   6588  CG  TYR C 203      42.199  24.706  53.350  1.00 36.46           C  
-ATOM   6589  CD1 TYR C 203      41.884  24.400  52.026  1.00 37.38           C  
-ATOM   6590  CD2 TYR C 203      42.457  26.036  53.674  1.00 37.14           C  
-ATOM   6591  CE1 TYR C 203      41.825  25.390  51.053  1.00 37.10           C  
-ATOM   6592  CE2 TYR C 203      42.404  27.031  52.712  1.00 38.01           C  
-ATOM   6593  CZ  TYR C 203      42.086  26.702  51.403  1.00 37.40           C  
-ATOM   6594  OH  TYR C 203      42.030  27.690  50.449  1.00 38.11           O  
-ATOM   6595  N   GLY C 204      44.185  20.944  55.598  1.00 33.51           N  
-ATOM   6596  CA  GLY C 204      44.108  19.865  56.561  1.00 34.85           C  
-ATOM   6597  C   GLY C 204      42.717  19.261  56.664  1.00 36.86           C  
-ATOM   6598  O   GLY C 204      42.399  18.600  57.651  1.00 38.18           O  
-ATOM   6599  N   LEU C 205      41.878  19.485  55.655  1.00 36.29           N  
-ATOM   6600  CA  LEU C 205      40.527  18.926  55.659  1.00 34.50           C  
-ATOM   6601  C   LEU C 205      40.601  17.404  55.563  1.00 33.23           C  
-ATOM   6602  O   LEU C 205      41.430  16.860  54.832  1.00 31.88           O  
-ATOM   6603  CB  LEU C 205      39.721  19.461  54.471  1.00 36.61           C  
-ATOM   6604  CG  LEU C 205      38.304  18.912  54.266  1.00 35.11           C  
-ATOM   6605  CD1 LEU C 205      37.413  19.333  55.421  1.00 36.09           C  
-ATOM   6606  CD2 LEU C 205      37.740  19.432  52.950  1.00 37.52           C  
-ATOM   6607  N   PHE C 206      39.741  16.715  56.305  1.00 32.55           N  
-ATOM   6608  CA  PHE C 206      39.727  15.262  56.259  1.00 32.47           C  
-ATOM   6609  C   PHE C 206      38.963  14.874  54.999  1.00 31.96           C  
-ATOM   6610  O   PHE C 206      37.750  14.673  55.034  1.00 29.34           O  
-ATOM   6611  CB  PHE C 206      39.030  14.682  57.493  1.00 33.66           C  
-ATOM   6612  CG  PHE C 206      39.236  13.200  57.660  1.00 36.43           C  
-ATOM   6613  CD1 PHE C 206      38.748  12.304  56.714  1.00 36.11           C  
-ATOM   6614  CD2 PHE C 206      39.947  12.703  58.750  1.00 37.91           C  
-ATOM   6615  CE1 PHE C 206      38.966  10.935  56.846  1.00 39.12           C  
-ATOM   6616  CE2 PHE C 206      40.172  11.333  58.895  1.00 40.74           C  
-ATOM   6617  CZ  PHE C 206      39.681  10.447  57.939  1.00 41.06           C  
-ATOM   6618  N   ALA C 207      39.686  14.779  53.887  1.00 31.39           N  
-ATOM   6619  CA  ALA C 207      39.086  14.439  52.604  1.00 31.77           C  
-ATOM   6620  C   ALA C 207      39.761  13.230  51.979  1.00 30.79           C  
-ATOM   6621  O   ALA C 207      40.973  13.220  51.774  1.00 31.98           O  
-ATOM   6622  CB  ALA C 207      39.175  15.639  51.661  1.00 31.44           C  
-ATOM   6623  N   CYS C 208      38.969  12.210  51.670  1.00 30.37           N  
-ATOM   6624  CA  CYS C 208      39.500  10.997  51.067  1.00 31.64           C  
-ATOM   6625  C   CYS C 208      39.009  10.810  49.641  1.00 31.99           C  
-ATOM   6626  O   CYS C 208      37.884  11.183  49.299  1.00 29.72           O  
-ATOM   6627  CB  CYS C 208      39.086   9.767  51.880  1.00 33.87           C  
-ATOM   6628  SG  CYS C 208      39.452   9.871  53.643  1.00 36.02           S  
-ATOM   6629  N   ASN C 209      39.866  10.229  48.813  1.00 32.07           N  
-ATOM   6630  CA  ASN C 209      39.507   9.948  47.440  1.00 31.36           C  
-ATOM   6631  C   ASN C 209      39.308   8.451  47.296  1.00 31.34           C  
-ATOM   6632  O   ASN C 209      40.236   7.664  47.474  1.00 31.99           O  
-ATOM   6633  CB  ASN C 209      40.600  10.407  46.463  1.00 32.01           C  
-ATOM   6634  CG  ASN C 209      40.519  11.890  46.151  1.00 30.70           C  
-ATOM   6635  OD1 ASN C 209      39.491  12.379  45.688  1.00 32.07           O  
-ATOM   6636  ND2 ASN C 209      41.608  12.612  46.399  1.00 31.18           N  
-ATOM   6637  N   GLY C 210      38.080   8.058  47.002  1.00 30.77           N  
-ATOM   6638  CA  GLY C 210      37.808   6.660  46.788  1.00 30.62           C  
-ATOM   6639  C   GLY C 210      38.027   6.441  45.305  1.00 30.58           C  
-ATOM   6640  O   GLY C 210      37.294   6.982  44.481  1.00 31.54           O  
-ATOM   6641  N   ILE C 211      39.057   5.685  44.952  1.00 29.70           N  
-ATOM   6642  CA  ILE C 211      39.321   5.414  43.551  1.00 29.56           C  
-ATOM   6643  C   ILE C 211      38.646   4.088  43.256  1.00 30.10           C  
-ATOM   6644  O   ILE C 211      39.297   3.050  43.177  1.00 29.67           O  
-ATOM   6645  CB  ILE C 211      40.828   5.309  43.276  1.00 30.21           C  
-ATOM   6646  CG1 ILE C 211      41.530   6.577  43.770  1.00 31.29           C  
-ATOM   6647  CG2 ILE C 211      41.070   5.126  41.790  1.00 29.57           C  
-ATOM   6648  CD1 ILE C 211      43.031   6.585  43.548  1.00 32.64           C  
-ATOM   6649  N   LEU C 212      37.328   4.131  43.105  1.00 29.70           N  
-ATOM   6650  CA  LEU C 212      36.562   2.924  42.854  1.00 29.91           C  
-ATOM   6651  C   LEU C 212      36.525   2.487  41.404  1.00 30.92           C  
-ATOM   6652  O   LEU C 212      36.383   3.302  40.495  1.00 31.32           O  
-ATOM   6653  CB  LEU C 212      35.131   3.096  43.372  1.00 29.64           C  
-ATOM   6654  CG  LEU C 212      34.944   2.868  44.877  1.00 27.97           C  
-ATOM   6655  CD1 LEU C 212      35.891   3.765  45.666  1.00 26.26           C  
-ATOM   6656  CD2 LEU C 212      33.500   3.139  45.256  1.00 28.03           C  
-ATOM   6657  N   PHE C 213      36.673   1.184  41.195  1.00 30.66           N  
-ATOM   6658  CA  PHE C 213      36.617   0.634  39.853  1.00 31.75           C  
-ATOM   6659  C   PHE C 213      35.150   0.297  39.564  1.00 30.65           C  
-ATOM   6660  O   PHE C 213      34.316   0.330  40.472  1.00 28.74           O  
-ATOM   6661  CB  PHE C 213      37.520  -0.604  39.747  1.00 31.33           C  
-ATOM   6662  CG  PHE C 213      38.979  -0.267  39.569  1.00 32.34           C  
-ATOM   6663  CD1 PHE C 213      39.672   0.435  40.554  1.00 32.68           C  
-ATOM   6664  CD2 PHE C 213      39.643  -0.597  38.393  1.00 32.04           C  
-ATOM   6665  CE1 PHE C 213      41.001   0.808  40.369  1.00 32.67           C  
-ATOM   6666  CE2 PHE C 213      40.972  -0.228  38.198  1.00 33.60           C  
-ATOM   6667  CZ  PHE C 213      41.653   0.477  39.188  1.00 33.45           C  
-ATOM   6668  N   ASN C 214      34.837   0.002  38.305  1.00 30.53           N  
-ATOM   6669  CA  ASN C 214      33.469  -0.315  37.910  1.00 32.00           C  
-ATOM   6670  C   ASN C 214      32.729  -1.185  38.918  1.00 33.92           C  
-ATOM   6671  O   ASN C 214      33.199  -2.263  39.274  1.00 36.97           O  
-ATOM   6672  CB  ASN C 214      33.454  -1.045  36.569  1.00 31.16           C  
-ATOM   6673  CG  ASN C 214      33.886  -0.174  35.419  1.00 32.71           C  
-ATOM   6674  OD1 ASN C 214      35.010   0.327  35.387  1.00 34.20           O  
-ATOM   6675  ND2 ASN C 214      32.992   0.006  34.454  1.00 32.24           N  
-ATOM   6676  N   HIS C 215      31.581  -0.719  39.392  1.00 33.18           N  
-ATOM   6677  CA  HIS C 215      30.789  -1.530  40.304  1.00 33.72           C  
-ATOM   6678  C   HIS C 215      29.327  -1.483  39.896  1.00 34.86           C  
-ATOM   6679  O   HIS C 215      28.718  -0.416  39.814  1.00 35.56           O  
-ATOM   6680  CB  HIS C 215      30.970  -1.106  41.765  1.00 31.80           C  
-ATOM   6681  CG  HIS C 215      30.873   0.364  41.996  1.00 31.25           C  
-ATOM   6682  ND1 HIS C 215      31.830   1.250  41.555  1.00 32.59           N  
-ATOM   6683  CD2 HIS C 215      29.952   1.101  42.659  1.00 31.22           C  
-ATOM   6684  CE1 HIS C 215      31.505   2.470  41.940  1.00 32.66           C  
-ATOM   6685  NE2 HIS C 215      30.369   2.407  42.612  1.00 31.62           N  
-ATOM   6686  N   GLU C 216      28.779  -2.666  39.631  1.00 37.00           N  
-ATOM   6687  CA  GLU C 216      27.403  -2.819  39.183  1.00 36.32           C  
-ATOM   6688  C   GLU C 216      26.460  -3.349  40.263  1.00 36.26           C  
-ATOM   6689  O   GLU C 216      26.875  -3.666  41.382  1.00 34.82           O  
-ATOM   6690  CB  GLU C 216      27.371  -3.763  37.983  1.00 37.15           C  
-ATOM   6691  CG  GLU C 216      28.618  -3.707  37.104  1.00 36.89           C  
-ATOM   6692  CD  GLU C 216      28.891  -2.327  36.543  1.00 37.90           C  
-ATOM   6693  OE1 GLU C 216      29.839  -1.662  37.011  1.00 41.10           O  
-ATOM   6694  OE2 GLU C 216      28.153  -1.901  35.634  1.00 39.43           O  
-ATOM   6695  N   SER C 217      25.183  -3.444  39.904  1.00 34.96           N  
-ATOM   6696  CA  SER C 217      24.149  -3.932  40.805  1.00 34.19           C  
-ATOM   6697  C   SER C 217      22.835  -3.936  40.036  1.00 34.89           C  
-ATOM   6698  O   SER C 217      22.788  -3.521  38.878  1.00 36.26           O  
-ATOM   6699  CB  SER C 217      24.026  -3.017  42.030  1.00 32.78           C  
-ATOM   6700  OG  SER C 217      23.321  -1.831  41.714  1.00 30.95           O  
-ATOM   6701  N   PRO C 218      21.756  -4.432  40.657  1.00 34.95           N  
-ATOM   6702  CA  PRO C 218      20.459  -4.456  39.970  1.00 35.52           C  
-ATOM   6703  C   PRO C 218      19.869  -3.051  39.825  1.00 35.64           C  
-ATOM   6704  O   PRO C 218      18.863  -2.863  39.143  1.00 37.92           O  
-ATOM   6705  CB  PRO C 218      19.605  -5.346  40.873  1.00 35.77           C  
-ATOM   6706  CG  PRO C 218      20.620  -6.285  41.473  1.00 35.58           C  
-ATOM   6707  CD  PRO C 218      21.740  -5.328  41.826  1.00 35.68           C  
-ATOM   6708  N   ARG C 219      20.501  -2.072  40.467  1.00 34.98           N  
-ATOM   6709  CA  ARG C 219      20.035  -0.688  40.421  1.00 33.39           C  
-ATOM   6710  C   ARG C 219      20.868   0.149  39.458  1.00 33.43           C  
-ATOM   6711  O   ARG C 219      20.623   1.342  39.284  1.00 34.15           O  
-ATOM   6712  CB  ARG C 219      20.106  -0.066  41.815  1.00 32.07           C  
-ATOM   6713  CG  ARG C 219      19.436  -0.885  42.903  1.00 33.51           C  
-ATOM   6714  CD  ARG C 219      19.590  -0.209  44.254  1.00 34.61           C  
-ATOM   6715  NE  ARG C 219      19.128  -1.048  45.356  1.00 36.31           N  
-ATOM   6716  CZ  ARG C 219      19.251  -0.723  46.640  1.00 38.59           C  
-ATOM   6717  NH1 ARG C 219      18.805  -1.543  47.583  1.00 39.10           N  
-ATOM   6718  NH2 ARG C 219      19.824   0.423  46.983  1.00 35.41           N  
-ATOM   6719  N   ARG C 220      21.858  -0.485  38.842  1.00 32.54           N  
-ATOM   6720  CA  ARG C 220      22.741   0.177  37.891  1.00 32.00           C  
-ATOM   6721  C   ARG C 220      21.949   0.839  36.764  1.00 31.12           C  
-ATOM   6722  O   ARG C 220      20.919   0.319  36.334  1.00 29.61           O  
-ATOM   6723  CB  ARG C 220      23.715  -0.856  37.306  1.00 31.52           C  
-ATOM   6724  CG  ARG C 220      24.686  -0.329  36.259  1.00 27.79           C  
-ATOM   6725  CD  ARG C 220      25.589   0.755  36.818  1.00 29.73           C  
-ATOM   6726  NE  ARG C 220      26.979   0.575  36.403  1.00 29.00           N  
-ATOM   6727  CZ  ARG C 220      27.873   1.559  36.327  1.00 30.80           C  
-ATOM   6728  NH1 ARG C 220      27.523   2.801  36.630  1.00 30.66           N  
-ATOM   6729  NH2 ARG C 220      29.122   1.295  35.966  1.00 31.48           N  
-ATOM   6730  N   GLY C 221      22.432   1.985  36.293  1.00 31.17           N  
-ATOM   6731  CA  GLY C 221      21.762   2.676  35.204  1.00 32.06           C  
-ATOM   6732  C   GLY C 221      21.694   1.779  33.979  1.00 32.91           C  
-ATOM   6733  O   GLY C 221      22.685   1.163  33.600  1.00 33.68           O  
-ATOM   6734  N   GLU C 222      20.525   1.706  33.356  1.00 34.23           N  
-ATOM   6735  CA  GLU C 222      20.326   0.859  32.184  1.00 34.97           C  
-ATOM   6736  C   GLU C 222      21.122   1.243  30.939  1.00 34.21           C  
-ATOM   6737  O   GLU C 222      21.136   0.501  29.958  1.00 35.68           O  
-ATOM   6738  CB  GLU C 222      18.835   0.797  31.848  1.00 34.31           C  
-ATOM   6739  CG  GLU C 222      18.040  -0.084  32.805  1.00 37.48           C  
-ATOM   6740  CD  GLU C 222      16.539  -0.014  32.578  1.00 37.87           C  
-ATOM   6741  OE1 GLU C 222      16.111  -0.017  31.402  1.00 40.23           O  
-ATOM   6742  OE2 GLU C 222      15.789   0.031  33.577  1.00 36.72           O  
-ATOM   6743  N   ASN C 223      21.793   2.387  30.971  1.00 33.91           N  
-ATOM   6744  CA  ASN C 223      22.576   2.822  29.818  1.00 33.24           C  
-ATOM   6745  C   ASN C 223      24.038   2.397  29.906  1.00 32.90           C  
-ATOM   6746  O   ASN C 223      24.821   2.625  28.981  1.00 31.71           O  
-ATOM   6747  CB  ASN C 223      22.448   4.332  29.641  1.00 33.64           C  
-ATOM   6748  CG  ASN C 223      21.055   4.734  29.193  1.00 40.04           C  
-ATOM   6749  OD1 ASN C 223      20.660   5.896  29.294  1.00 42.32           O  
-ATOM   6750  ND2 ASN C 223      20.300   3.764  28.687  1.00 41.23           N  
-ATOM   6751  N   PHE C 224      24.405   1.779  31.023  1.00 31.13           N  
-ATOM   6752  CA  PHE C 224      25.760   1.278  31.184  1.00 32.16           C  
-ATOM   6753  C   PHE C 224      25.704  -0.150  30.634  1.00 32.48           C  
-ATOM   6754  O   PHE C 224      24.648  -0.784  30.649  1.00 32.29           O  
-ATOM   6755  CB  PHE C 224      26.180   1.315  32.657  1.00 31.78           C  
-ATOM   6756  CG  PHE C 224      26.294   2.713  33.215  1.00 32.73           C  
-ATOM   6757  CD1 PHE C 224      25.276   3.254  33.996  1.00 32.38           C  
-ATOM   6758  CD2 PHE C 224      27.409   3.503  32.929  1.00 32.33           C  
-ATOM   6759  CE1 PHE C 224      25.365   4.561  34.484  1.00 33.34           C  
-ATOM   6760  CE2 PHE C 224      27.509   4.811  33.412  1.00 29.99           C  
-ATOM   6761  CZ  PHE C 224      26.484   5.341  34.190  1.00 31.67           C  
-ATOM   6762  N   VAL C 225      26.831  -0.649  30.140  1.00 33.09           N  
-ATOM   6763  CA  VAL C 225      26.884  -1.968  29.518  1.00 32.43           C  
-ATOM   6764  C   VAL C 225      26.369  -3.179  30.291  1.00 33.58           C  
-ATOM   6765  O   VAL C 225      25.659  -4.009  29.725  1.00 33.52           O  
-ATOM   6766  CB  VAL C 225      28.306  -2.293  29.041  1.00 32.36           C  
-ATOM   6767  CG1 VAL C 225      29.172  -2.727  30.218  1.00 31.63           C  
-ATOM   6768  CG2 VAL C 225      28.247  -3.362  27.970  1.00 32.69           C  
-ATOM   6769  N   THR C 226      26.719  -3.292  31.568  1.00 32.48           N  
-ATOM   6770  CA  THR C 226      26.284  -4.437  32.351  1.00 32.47           C  
-ATOM   6771  C   THR C 226      24.770  -4.506  32.507  1.00 34.68           C  
-ATOM   6772  O   THR C 226      24.161  -5.540  32.231  1.00 33.93           O  
-ATOM   6773  CB  THR C 226      26.930  -4.443  33.747  1.00 33.10           C  
-ATOM   6774  OG1 THR C 226      26.465  -3.319  34.500  1.00 33.80           O  
-ATOM   6775  CG2 THR C 226      28.444  -4.376  33.624  1.00 31.89           C  
-ATOM   6776  N   ARG C 227      24.164  -3.405  32.938  1.00 34.18           N  
-ATOM   6777  CA  ARG C 227      22.723  -3.366  33.132  1.00 33.40           C  
-ATOM   6778  C   ARG C 227      22.005  -3.467  31.799  1.00 33.39           C  
-ATOM   6779  O   ARG C 227      20.951  -4.091  31.697  1.00 34.28           O  
-ATOM   6780  CB  ARG C 227      22.302  -2.071  33.826  1.00 31.35           C  
-ATOM   6781  CG  ARG C 227      20.848  -2.080  34.264  1.00 30.18           C  
-ATOM   6782  CD  ARG C 227      20.643  -3.041  35.419  1.00 29.05           C  
-ATOM   6783  NE  ARG C 227      19.233  -3.316  35.680  1.00 29.63           N  
-ATOM   6784  CZ  ARG C 227      18.333  -2.404  36.034  1.00 29.91           C  
-ATOM   6785  NH1 ARG C 227      18.684  -1.134  36.179  1.00 28.50           N  
-ATOM   6786  NH2 ARG C 227      17.074  -2.764  36.234  1.00 30.55           N  
-ATOM   6787  N   LYS C 228      22.573  -2.837  30.779  1.00 32.99           N  
-ATOM   6788  CA  LYS C 228      21.971  -2.869  29.458  1.00 32.83           C  
-ATOM   6789  C   LYS C 228      21.815  -4.319  29.021  1.00 32.93           C  
-ATOM   6790  O   LYS C 228      20.779  -4.716  28.489  1.00 32.52           O  
-ATOM   6791  CB  LYS C 228      22.853  -2.123  28.465  1.00 32.44           C  
-ATOM   6792  CG  LYS C 228      22.277  -2.048  27.072  1.00 31.81           C  
-ATOM   6793  CD  LYS C 228      23.188  -1.268  26.159  1.00 29.88           C  
-ATOM   6794  CE  LYS C 228      22.584  -1.136  24.782  1.00 30.78           C  
-ATOM   6795  NZ  LYS C 228      23.388  -0.212  23.939  1.00 32.61           N  
-ATOM   6796  N   ILE C 229      22.857  -5.104  29.269  1.00 34.12           N  
-ATOM   6797  CA  ILE C 229      22.888  -6.515  28.909  1.00 32.91           C  
-ATOM   6798  C   ILE C 229      21.865  -7.349  29.673  1.00 32.21           C  
-ATOM   6799  O   ILE C 229      20.996  -7.973  29.069  1.00 33.56           O  
-ATOM   6800  CB  ILE C 229      24.307  -7.092  29.132  1.00 31.54           C  
-ATOM   6801  CG1 ILE C 229      25.251  -6.546  28.060  1.00 31.06           C  
-ATOM   6802  CG2 ILE C 229      24.278  -8.610  29.104  1.00 33.63           C  
-ATOM   6803  CD1 ILE C 229      26.698  -6.958  28.234  1.00 33.83           C  
-ATOM   6804  N   THR C 230      21.958  -7.354  30.999  1.00 31.51           N  
-ATOM   6805  CA  THR C 230      21.037  -8.138  31.807  1.00 31.46           C  
-ATOM   6806  C   THR C 230      19.569  -7.747  31.604  1.00 33.89           C  
-ATOM   6807  O   THR C 230      18.689  -8.610  31.616  1.00 35.15           O  
-ATOM   6808  CB  THR C 230      21.381  -8.034  33.301  1.00 30.51           C  
-ATOM   6809  OG1 THR C 230      21.194  -6.689  33.745  1.00 32.25           O  
-ATOM   6810  CG2 THR C 230      22.822  -8.446  33.540  1.00 30.04           C  
-ATOM   6811  N   ARG C 231      19.305  -6.455  31.414  1.00 33.09           N  
-ATOM   6812  CA  ARG C 231      17.940  -5.978  31.203  1.00 32.83           C  
-ATOM   6813  C   ARG C 231      17.397  -6.542  29.898  1.00 33.09           C  
-ATOM   6814  O   ARG C 231      16.270  -7.041  29.842  1.00 32.23           O  
-ATOM   6815  CB  ARG C 231      17.910  -4.449  31.130  1.00 35.19           C  
-ATOM   6816  CG  ARG C 231      16.520  -3.841  31.243  1.00 35.64           C  
-ATOM   6817  CD  ARG C 231      15.996  -3.987  32.662  1.00 40.01           C  
-ATOM   6818  NE  ARG C 231      14.819  -3.161  32.916  1.00 41.29           N  
-ATOM   6819  CZ  ARG C 231      13.578  -3.488  32.575  1.00 42.38           C  
-ATOM   6820  NH1 ARG C 231      13.329  -4.639  31.961  1.00 42.42           N  
-ATOM   6821  NH2 ARG C 231      12.583  -2.658  32.851  1.00 39.74           N  
-ATOM   6822  N   ALA C 232      18.205  -6.442  28.847  1.00 34.50           N  
-ATOM   6823  CA  ALA C 232      17.832  -6.942  27.530  1.00 35.37           C  
-ATOM   6824  C   ALA C 232      17.727  -8.465  27.565  1.00 37.17           C  
-ATOM   6825  O   ALA C 232      16.844  -9.050  26.935  1.00 38.62           O  
-ATOM   6826  CB  ALA C 232      18.867  -6.510  26.497  1.00 33.85           C  
-ATOM   6827  N   LEU C 233      18.633  -9.104  28.303  1.00 37.90           N  
-ATOM   6828  CA  LEU C 233      18.634 -10.558  28.423  1.00 38.95           C  
-ATOM   6829  C   LEU C 233      17.306 -11.033  28.999  1.00 40.65           C  
-ATOM   6830  O   LEU C 233      16.593 -11.814  28.374  1.00 41.50           O  
-ATOM   6831  CB  LEU C 233      19.773 -11.022  29.335  1.00 37.95           C  
-ATOM   6832  CG  LEU C 233      19.797 -12.510  29.697  1.00 39.01           C  
-ATOM   6833  CD1 LEU C 233      19.780 -13.356  28.427  1.00 37.50           C  
-ATOM   6834  CD2 LEU C 233      21.038 -12.810  30.535  1.00 39.72           C  
-ATOM   6835  N   GLY C 234      16.987 -10.553  30.197  1.00 41.80           N  
-ATOM   6836  CA  GLY C 234      15.747 -10.935  30.842  1.00 41.69           C  
-ATOM   6837  C   GLY C 234      14.540 -10.761  29.943  1.00 42.18           C  
-ATOM   6838  O   GLY C 234      13.625 -11.585  29.960  1.00 42.74           O  
-ATOM   6839  N   ARG C 235      14.531  -9.691  29.155  1.00 41.95           N  
-ATOM   6840  CA  ARG C 235      13.414  -9.425  28.257  1.00 42.55           C  
-ATOM   6841  C   ARG C 235      13.432 -10.365  27.055  1.00 42.36           C  
-ATOM   6842  O   ARG C 235      12.388 -10.855  26.626  1.00 41.87           O  
-ATOM   6843  CB  ARG C 235      13.442  -7.962  27.799  1.00 41.97           C  
-ATOM   6844  CG  ARG C 235      13.218  -6.970  28.936  1.00 43.85           C  
-ATOM   6845  CD  ARG C 235      13.228  -5.534  28.441  1.00 44.69           C  
-ATOM   6846  NE  ARG C 235      12.243  -5.338  27.385  1.00 49.97           N  
-ATOM   6847  CZ  ARG C 235      12.062  -4.199  26.727  1.00 52.32           C  
-ATOM   6848  NH1 ARG C 235      12.803  -3.135  27.019  1.00 53.24           N  
-ATOM   6849  NH2 ARG C 235      11.143  -4.127  25.771  1.00 51.76           N  
-ATOM   6850  N   ILE C 236      14.619 -10.613  26.515  1.00 41.79           N  
-ATOM   6851  CA  ILE C 236      14.759 -11.514  25.380  1.00 41.08           C  
-ATOM   6852  C   ILE C 236      14.261 -12.901  25.792  1.00 41.04           C  
-ATOM   6853  O   ILE C 236      13.587 -13.589  25.021  1.00 40.83           O  
-ATOM   6854  CB  ILE C 236      16.241 -11.598  24.927  1.00 40.76           C  
-ATOM   6855  CG1 ILE C 236      16.643 -10.289  24.246  1.00 39.97           C  
-ATOM   6856  CG2 ILE C 236      16.449 -12.773  23.981  1.00 41.46           C  
-ATOM   6857  CD1 ILE C 236      18.074 -10.265  23.749  1.00 39.91           C  
-ATOM   6858  N   LYS C 237      14.580 -13.281  27.026  1.00 40.52           N  
-ATOM   6859  CA  LYS C 237      14.201 -14.571  27.592  1.00 40.54           C  
-ATOM   6860  C   LYS C 237      12.688 -14.760  27.724  1.00 42.78           C  
-ATOM   6861  O   LYS C 237      12.200 -15.894  27.720  1.00 43.61           O  
-ATOM   6862  CB  LYS C 237      14.854 -14.735  28.966  1.00 39.56           C  
-ATOM   6863  CG  LYS C 237      14.565 -16.052  29.670  1.00 39.18           C  
-ATOM   6864  CD  LYS C 237      15.227 -17.223  28.962  1.00 38.76           C  
-ATOM   6865  CE  LYS C 237      15.077 -18.507  29.764  1.00 38.34           C  
-ATOM   6866  NZ  LYS C 237      15.778 -19.640  29.099  1.00 40.39           N  
-ATOM   6867  N   VAL C 238      11.948 -13.660  27.848  1.00 42.14           N  
-ATOM   6868  CA  VAL C 238      10.497 -13.747  27.982  1.00 41.49           C  
-ATOM   6869  C   VAL C 238       9.770 -13.400  26.689  1.00 41.23           C  
-ATOM   6870  O   VAL C 238       8.542 -13.398  26.645  1.00 42.29           O  
-ATOM   6871  CB  VAL C 238       9.969 -12.829  29.111  1.00 42.66           C  
-ATOM   6872  CG1 VAL C 238      10.552 -13.264  30.448  1.00 41.80           C  
-ATOM   6873  CG2 VAL C 238      10.316 -11.374  28.814  1.00 41.48           C  
-ATOM   6874  N   GLY C 239      10.530 -13.105  25.639  1.00 41.44           N  
-ATOM   6875  CA  GLY C 239       9.923 -12.778  24.361  1.00 40.47           C  
-ATOM   6876  C   GLY C 239       9.589 -11.311  24.156  1.00 41.50           C  
-ATOM   6877  O   GLY C 239       8.956 -10.949  23.155  1.00 40.54           O  
-ATOM   6878  N   LEU C 240      10.011 -10.464  25.093  1.00 39.95           N  
-ATOM   6879  CA  LEU C 240       9.753  -9.031  24.999  1.00 40.28           C  
-ATOM   6880  C   LEU C 240      10.705  -8.321  24.045  1.00 40.33           C  
-ATOM   6881  O   LEU C 240      10.358  -7.291  23.468  1.00 41.56           O  
-ATOM   6882  CB  LEU C 240       9.850  -8.379  26.383  1.00 40.19           C  
-ATOM   6883  CG  LEU C 240       8.696  -8.638  27.353  1.00 39.74           C  
-ATOM   6884  CD1 LEU C 240       8.988  -7.986  28.697  1.00 38.51           C  
-ATOM   6885  CD2 LEU C 240       7.404  -8.086  26.760  1.00 40.44           C  
-ATOM   6886  N   GLN C 241      11.901  -8.877  23.876  1.00 40.47           N  
-ATOM   6887  CA  GLN C 241      12.916  -8.282  23.009  1.00 39.30           C  
-ATOM   6888  C   GLN C 241      13.565  -9.359  22.142  1.00 38.77           C  
-ATOM   6889  O   GLN C 241      13.584 -10.528  22.517  1.00 38.72           O  
-ATOM   6890  CB  GLN C 241      13.978  -7.601  23.875  1.00 38.94           C  
-ATOM   6891  CG  GLN C 241      14.776  -6.519  23.182  1.00 38.85           C  
-ATOM   6892  CD  GLN C 241      15.666  -5.764  24.150  1.00 38.48           C  
-ATOM   6893  OE1 GLN C 241      15.260  -5.464  25.277  1.00 36.70           O  
-ATOM   6894  NE2 GLN C 241      16.880  -5.441  23.715  1.00 37.60           N  
-ATOM   6895  N   THR C 242      14.103  -8.965  20.991  1.00 39.52           N  
-ATOM   6896  CA  THR C 242      14.737  -9.922  20.087  1.00 41.51           C  
-ATOM   6897  C   THR C 242      16.181  -9.574  19.718  1.00 42.79           C  
-ATOM   6898  O   THR C 242      16.998 -10.470  19.501  1.00 43.24           O  
-ATOM   6899  CB  THR C 242      13.940 -10.060  18.771  1.00 42.88           C  
-ATOM   6900  OG1 THR C 242      14.089  -8.864  17.991  1.00 45.17           O  
-ATOM   6901  CG2 THR C 242      12.458 -10.287  19.062  1.00 42.36           C  
-ATOM   6902  N   LYS C 243      16.493  -8.280  19.645  1.00 42.44           N  
-ATOM   6903  CA  LYS C 243      17.839  -7.839  19.286  1.00 42.73           C  
-ATOM   6904  C   LYS C 243      18.471  -6.873  20.290  1.00 43.74           C  
-ATOM   6905  O   LYS C 243      17.837  -5.911  20.734  1.00 43.95           O  
-ATOM   6906  CB  LYS C 243      17.817  -7.194  17.898  1.00 41.79           C  
-ATOM   6907  N   LEU C 244      19.730  -7.137  20.633  1.00 43.09           N  
-ATOM   6908  CA  LEU C 244      20.489  -6.305  21.563  1.00 41.52           C  
-ATOM   6909  C   LEU C 244      21.669  -5.697  20.819  1.00 41.54           C  
-ATOM   6910  O   LEU C 244      22.499  -6.423  20.279  1.00 42.19           O  
-ATOM   6911  CB  LEU C 244      21.010  -7.149  22.728  1.00 40.69           C  
-ATOM   6912  CG  LEU C 244      22.136  -6.540  23.569  1.00 40.83           C  
-ATOM   6913  CD1 LEU C 244      21.667  -5.245  24.219  1.00 39.72           C  
-ATOM   6914  CD2 LEU C 244      22.583  -7.545  24.619  1.00 39.71           C  
-ATOM   6915  N   PHE C 245      21.742  -4.370  20.794  1.00 42.02           N  
-ATOM   6916  CA  PHE C 245      22.827  -3.673  20.106  1.00 41.58           C  
-ATOM   6917  C   PHE C 245      23.909  -3.178  21.064  1.00 40.95           C  
-ATOM   6918  O   PHE C 245      23.633  -2.411  21.987  1.00 38.81           O  
-ATOM   6919  CB  PHE C 245      22.277  -2.484  19.315  1.00 42.90           C  
-ATOM   6920  CG  PHE C 245      21.299  -2.869  18.242  1.00 46.49           C  
-ATOM   6921  CD1 PHE C 245      19.996  -3.233  18.566  1.00 46.31           C  
-ATOM   6922  CD2 PHE C 245      21.688  -2.885  16.905  1.00 47.17           C  
-ATOM   6923  CE1 PHE C 245      19.092  -3.608  17.574  1.00 47.81           C  
-ATOM   6924  CE2 PHE C 245      20.793  -3.258  15.905  1.00 47.76           C  
-ATOM   6925  CZ  PHE C 245      19.490  -3.620  16.241  1.00 47.86           C  
-ATOM   6926  N   LEU C 246      25.144  -3.613  20.832  1.00 39.16           N  
-ATOM   6927  CA  LEU C 246      26.261  -3.206  21.673  1.00 38.65           C  
-ATOM   6928  C   LEU C 246      27.387  -2.574  20.868  1.00 39.07           C  
-ATOM   6929  O   LEU C 246      27.315  -2.474  19.643  1.00 38.99           O  
-ATOM   6930  CB  LEU C 246      26.792  -4.406  22.458  1.00 36.73           C  
-ATOM   6931  CG  LEU C 246      25.823  -4.925  23.522  1.00 35.46           C  
-ATOM   6932  CD1 LEU C 246      26.334  -6.231  24.120  1.00 33.85           C  
-ATOM   6933  CD2 LEU C 246      25.647  -3.856  24.598  1.00 32.03           C  
-ATOM   6934  N   GLY C 247      28.424  -2.135  21.571  1.00 39.54           N  
-ATOM   6935  CA  GLY C 247      29.555  -1.520  20.909  1.00 40.14           C  
-ATOM   6936  C   GLY C 247      30.787  -2.399  20.978  1.00 42.17           C  
-ATOM   6937  O   GLY C 247      30.849  -3.444  20.331  1.00 42.71           O  
-ATOM   6938  N   ASN C 248      31.760  -1.972  21.780  1.00 42.42           N  
-ATOM   6939  CA  ASN C 248      33.020  -2.682  21.954  1.00 41.71           C  
-ATOM   6940  C   ASN C 248      32.912  -3.822  22.960  1.00 42.01           C  
-ATOM   6941  O   ASN C 248      32.728  -3.591  24.154  1.00 41.77           O  
-ATOM   6942  CB  ASN C 248      34.096  -1.694  22.413  1.00 44.42           C  
-ATOM   6943  CG  ASN C 248      35.465  -2.329  22.524  1.00 46.13           C  
-ATOM   6944  OD1 ASN C 248      35.954  -2.939  21.574  1.00 48.78           O  
-ATOM   6945  ND2 ASN C 248      36.098  -2.181  23.682  1.00 48.07           N  
-ATOM   6946  N   LEU C 249      33.040  -5.054  22.481  1.00 41.05           N  
-ATOM   6947  CA  LEU C 249      32.952  -6.210  23.363  1.00 41.33           C  
-ATOM   6948  C   LEU C 249      34.325  -6.579  23.913  1.00 41.43           C  
-ATOM   6949  O   LEU C 249      34.437  -7.358  24.859  1.00 40.34           O  
-ATOM   6950  CB  LEU C 249      32.357  -7.402  22.609  1.00 41.18           C  
-ATOM   6951  CG  LEU C 249      31.012  -7.171  21.911  1.00 41.66           C  
-ATOM   6952  CD1 LEU C 249      30.556  -8.465  21.267  1.00 41.25           C  
-ATOM   6953  CD2 LEU C 249      29.974  -6.684  22.911  1.00 42.16           C  
-ATOM   6954  N   GLN C 250      35.366  -6.008  23.315  1.00 43.02           N  
-ATOM   6955  CA  GLN C 250      36.741  -6.270  23.734  1.00 44.01           C  
-ATOM   6956  C   GLN C 250      37.066  -5.614  25.068  1.00 43.26           C  
-ATOM   6957  O   GLN C 250      37.902  -6.109  25.826  1.00 43.49           O  
-ATOM   6958  CB  GLN C 250      37.723  -5.756  22.680  1.00 44.84           C  
-ATOM   6959  CG  GLN C 250      37.794  -6.588  21.409  1.00 47.17           C  
-ATOM   6960  CD  GLN C 250      36.438  -6.850  20.792  1.00 47.63           C  
-ATOM   6961  OE1 GLN C 250      35.805  -7.871  21.066  1.00 48.92           O  
-ATOM   6962  NE2 GLN C 250      35.977  -5.923  19.957  1.00 49.39           N  
-ATOM   6963  N   ALA C 251      36.404  -4.497  25.351  1.00 42.20           N  
-ATOM   6964  CA  ALA C 251      36.635  -3.764  26.588  1.00 39.74           C  
-ATOM   6965  C   ALA C 251      36.693  -4.693  27.791  1.00 38.19           C  
-ATOM   6966  O   ALA C 251      35.796  -5.512  27.997  1.00 37.22           O  
-ATOM   6967  CB  ALA C 251      35.543  -2.727  26.787  1.00 41.50           C  
-ATOM   6968  N   SER C 252      37.757  -4.566  28.578  1.00 35.54           N  
-ATOM   6969  CA  SER C 252      37.921  -5.381  29.773  1.00 34.82           C  
-ATOM   6970  C   SER C 252      37.785  -4.477  30.984  1.00 34.67           C  
-ATOM   6971  O   SER C 252      38.296  -3.361  30.988  1.00 36.71           O  
-ATOM   6972  CB  SER C 252      39.290  -6.064  29.788  1.00 33.97           C  
-ATOM   6973  OG  SER C 252      39.464  -6.805  30.985  1.00 27.73           O  
-ATOM   6974  N   ARG C 253      37.102  -4.965  32.012  1.00 34.21           N  
-ATOM   6975  CA  ARG C 253      36.880  -4.176  33.213  1.00 33.83           C  
-ATOM   6976  C   ARG C 253      36.910  -5.011  34.488  1.00 34.39           C  
-ATOM   6977  O   ARG C 253      36.760  -6.231  34.460  1.00 36.52           O  
-ATOM   6978  CB  ARG C 253      35.526  -3.458  33.116  1.00 33.13           C  
-ATOM   6979  CG  ARG C 253      35.414  -2.415  32.005  1.00 34.33           C  
-ATOM   6980  CD  ARG C 253      36.138  -1.121  32.373  1.00 33.74           C  
-ATOM   6981  NE  ARG C 253      35.932  -0.065  31.384  1.00 32.85           N  
-ATOM   6982  CZ  ARG C 253      36.531  -0.015  30.199  1.00 32.65           C  
-ATOM   6983  NH1 ARG C 253      36.275   0.985  29.370  1.00 30.85           N  
-ATOM   6984  NH2 ARG C 253      37.394  -0.958  29.844  1.00 33.08           N  
-ATOM   6985  N   ASP C 254      37.108  -4.326  35.606  1.00 35.08           N  
-ATOM   6986  CA  ASP C 254      37.144  -4.937  36.929  1.00 34.39           C  
-ATOM   6987  C   ASP C 254      35.788  -4.589  37.552  1.00 34.35           C  
-ATOM   6988  O   ASP C 254      35.596  -3.492  38.080  1.00 34.38           O  
-ATOM   6989  CB  ASP C 254      38.316  -4.329  37.718  1.00 34.02           C  
-ATOM   6990  CG  ASP C 254      38.402  -4.830  39.145  1.00 34.59           C  
-ATOM   6991  OD1 ASP C 254      39.527  -4.855  39.683  1.00 34.07           O  
-ATOM   6992  OD2 ASP C 254      37.361  -5.177  39.737  1.00 35.80           O  
-ATOM   6993  N   TRP C 255      34.847  -5.528  37.462  1.00 33.83           N  
-ATOM   6994  CA  TRP C 255      33.485  -5.343  37.966  1.00 32.26           C  
-ATOM   6995  C   TRP C 255      33.212  -5.876  39.368  1.00 31.75           C  
-ATOM   6996  O   TRP C 255      33.414  -7.055  39.649  1.00 34.15           O  
-ATOM   6997  CB  TRP C 255      32.487  -5.993  37.004  1.00 30.81           C  
-ATOM   6998  CG  TRP C 255      32.310  -5.279  35.699  1.00 30.83           C  
-ATOM   6999  CD1 TRP C 255      31.862  -4.003  35.518  1.00 29.35           C  
-ATOM   7000  CD2 TRP C 255      32.528  -5.814  34.388  1.00 29.96           C  
-ATOM   7001  NE1 TRP C 255      31.783  -3.710  34.178  1.00 26.88           N  
-ATOM   7002  CE2 TRP C 255      32.186  -4.804  33.461  1.00 28.55           C  
-ATOM   7003  CE3 TRP C 255      32.977  -7.051  33.905  1.00 30.21           C  
-ATOM   7004  CZ2 TRP C 255      32.278  -4.992  32.079  1.00 27.96           C  
-ATOM   7005  CZ3 TRP C 255      33.067  -7.236  32.525  1.00 29.12           C  
-ATOM   7006  CH2 TRP C 255      32.719  -6.211  31.632  1.00 29.51           C  
-ATOM   7007  N   GLY C 256      32.716  -5.003  40.234  1.00 32.54           N  
-ATOM   7008  CA  GLY C 256      32.396  -5.387  41.597  1.00 32.65           C  
-ATOM   7009  C   GLY C 256      30.941  -5.071  41.891  1.00 33.80           C  
-ATOM   7010  O   GLY C 256      30.222  -4.600  41.006  1.00 33.63           O  
-ATOM   7011  N   PHE C 257      30.504  -5.330  43.121  1.00 33.48           N  
-ATOM   7012  CA  PHE C 257      29.122  -5.073  43.516  1.00 33.61           C  
-ATOM   7013  C   PHE C 257      29.007  -3.804  44.350  1.00 34.36           C  
-ATOM   7014  O   PHE C 257      29.579  -3.704  45.436  1.00 35.82           O  
-ATOM   7015  CB  PHE C 257      28.557  -6.267  44.302  1.00 33.30           C  
-ATOM   7016  CG  PHE C 257      27.182  -6.023  44.867  1.00 33.19           C  
-ATOM   7017  CD1 PHE C 257      26.123  -5.674  44.031  1.00 33.32           C  
-ATOM   7018  CD2 PHE C 257      26.952  -6.112  46.237  1.00 32.60           C  
-ATOM   7019  CE1 PHE C 257      24.856  -5.413  44.552  1.00 32.03           C  
-ATOM   7020  CE2 PHE C 257      25.685  -5.853  46.770  1.00 33.91           C  
-ATOM   7021  CZ  PHE C 257      24.637  -5.501  45.923  1.00 32.71           C  
-ATOM   7022  N   ALA C 258      28.250  -2.843  43.831  1.00 34.32           N  
-ATOM   7023  CA  ALA C 258      28.045  -1.555  44.481  1.00 34.22           C  
-ATOM   7024  C   ALA C 258      27.757  -1.675  45.975  1.00 34.96           C  
-ATOM   7025  O   ALA C 258      28.220  -0.852  46.771  1.00 34.78           O  
-ATOM   7026  CB  ALA C 258      26.906  -0.797  43.782  1.00 33.75           C  
-ATOM   7027  N   GLY C 259      26.988  -2.694  46.351  1.00 33.62           N  
-ATOM   7028  CA  GLY C 259      26.657  -2.891  47.751  1.00 33.55           C  
-ATOM   7029  C   GLY C 259      27.882  -3.075  48.627  1.00 33.03           C  
-ATOM   7030  O   GLY C 259      27.896  -2.645  49.779  1.00 34.72           O  
-ATOM   7031  N   ASP C 260      28.909  -3.717  48.080  1.00 32.26           N  
-ATOM   7032  CA  ASP C 260      30.155  -3.955  48.804  1.00 33.87           C  
-ATOM   7033  C   ASP C 260      30.997  -2.683  48.879  1.00 34.51           C  
-ATOM   7034  O   ASP C 260      31.551  -2.346  49.929  1.00 36.23           O  
-ATOM   7035  CB  ASP C 260      30.974  -5.043  48.100  1.00 33.76           C  
-ATOM   7036  CG  ASP C 260      30.387  -6.440  48.277  1.00 35.20           C  
-ATOM   7037  OD1 ASP C 260      30.748  -7.330  47.482  1.00 34.64           O  
-ATOM   7038  OD2 ASP C 260      29.581  -6.656  49.211  1.00 34.65           O  
-ATOM   7039  N   TYR C 261      31.073  -1.984  47.751  1.00 33.68           N  
-ATOM   7040  CA  TYR C 261      31.858  -0.763  47.618  1.00 32.83           C  
-ATOM   7041  C   TYR C 261      31.448   0.413  48.493  1.00 32.60           C  
-ATOM   7042  O   TYR C 261      32.306   1.165  48.946  1.00 34.95           O  
-ATOM   7043  CB  TYR C 261      31.884  -0.343  46.146  1.00 31.07           C  
-ATOM   7044  CG  TYR C 261      32.699  -1.274  45.271  1.00 30.18           C  
-ATOM   7045  CD1 TYR C 261      32.683  -2.654  45.482  1.00 29.41           C  
-ATOM   7046  CD2 TYR C 261      33.494  -0.775  44.237  1.00 30.93           C  
-ATOM   7047  CE1 TYR C 261      33.441  -3.516  44.689  1.00 30.05           C  
-ATOM   7048  CE2 TYR C 261      34.255  -1.628  43.435  1.00 29.80           C  
-ATOM   7049  CZ  TYR C 261      34.223  -2.998  43.668  1.00 31.08           C  
-ATOM   7050  OH  TYR C 261      34.958  -3.850  42.873  1.00 32.42           O  
-ATOM   7051  N   VAL C 262      30.156   0.588  48.743  1.00 32.97           N  
-ATOM   7052  CA  VAL C 262      29.732   1.703  49.587  1.00 35.03           C  
-ATOM   7053  C   VAL C 262      30.289   1.569  51.002  1.00 34.90           C  
-ATOM   7054  O   VAL C 262      30.461   2.565  51.703  1.00 36.05           O  
-ATOM   7055  CB  VAL C 262      28.188   1.823  49.671  1.00 35.09           C  
-ATOM   7056  CG1 VAL C 262      27.631   2.274  48.336  1.00 36.10           C  
-ATOM   7057  CG2 VAL C 262      27.580   0.494  50.085  1.00 37.23           C  
-ATOM   7058  N   GLU C 263      30.570   0.337  51.418  1.00 34.76           N  
-ATOM   7059  CA  GLU C 263      31.113   0.093  52.752  1.00 35.47           C  
-ATOM   7060  C   GLU C 263      32.528   0.656  52.848  1.00 34.14           C  
-ATOM   7061  O   GLU C 263      32.918   1.211  53.875  1.00 34.09           O  
-ATOM   7062  CB  GLU C 263      31.119  -1.406  53.057  1.00 34.83           C  
-ATOM   7063  N   ALA C 264      33.290   0.515  51.769  1.00 33.51           N  
-ATOM   7064  CA  ALA C 264      34.658   1.016  51.731  1.00 34.79           C  
-ATOM   7065  C   ALA C 264      34.698   2.537  51.884  1.00 35.87           C  
-ATOM   7066  O   ALA C 264      35.607   3.080  52.516  1.00 37.69           O  
-ATOM   7067  CB  ALA C 264      35.325   0.601  50.424  1.00 35.01           C  
-ATOM   7068  N   MET C 265      33.709   3.219  51.307  1.00 35.73           N  
-ATOM   7069  CA  MET C 265      33.626   4.677  51.381  1.00 34.27           C  
-ATOM   7070  C   MET C 265      33.540   5.111  52.844  1.00 34.41           C  
-ATOM   7071  O   MET C 265      34.245   6.024  53.283  1.00 31.72           O  
-ATOM   7072  CB  MET C 265      32.379   5.189  50.633  1.00 34.95           C  
-ATOM   7073  CG  MET C 265      32.287   4.808  49.157  1.00 31.82           C  
-ATOM   7074  SD  MET C 265      30.704   5.303  48.412  1.00 32.47           S  
-ATOM   7075  CE  MET C 265      31.007   4.962  46.687  1.00 32.73           C  
-ATOM   7076  N   TRP C 266      32.657   4.447  53.585  1.00 34.20           N  
-ATOM   7077  CA  TRP C 266      32.441   4.732  54.999  1.00 35.26           C  
-ATOM   7078  C   TRP C 266      33.690   4.412  55.821  1.00 34.52           C  
-ATOM   7079  O   TRP C 266      34.090   5.194  56.684  1.00 35.22           O  
-ATOM   7080  CB  TRP C 266      31.252   3.911  55.520  1.00 35.85           C  
-ATOM   7081  CG  TRP C 266      31.043   4.008  57.000  1.00 35.32           C  
-ATOM   7082  CD1 TRP C 266      30.494   5.052  57.685  1.00 35.35           C  
-ATOM   7083  CD2 TRP C 266      31.411   3.030  57.982  1.00 35.17           C  
-ATOM   7084  NE1 TRP C 266      30.497   4.787  59.036  1.00 37.53           N  
-ATOM   7085  CE2 TRP C 266      31.055   3.553  59.246  1.00 36.54           C  
-ATOM   7086  CE3 TRP C 266      32.010   1.763  57.915  1.00 35.99           C  
-ATOM   7087  CZ2 TRP C 266      31.277   2.852  60.440  1.00 37.16           C  
-ATOM   7088  CZ3 TRP C 266      32.233   1.061  59.104  1.00 36.42           C  
-ATOM   7089  CH2 TRP C 266      31.865   1.611  60.350  1.00 37.14           C  
-ATOM   7090  N   LEU C 267      34.298   3.260  55.555  1.00 34.78           N  
-ATOM   7091  CA  LEU C 267      35.500   2.861  56.278  1.00 37.41           C  
-ATOM   7092  C   LEU C 267      36.584   3.920  56.116  1.00 38.84           C  
-ATOM   7093  O   LEU C 267      37.205   4.338  57.096  1.00 38.75           O  
-ATOM   7094  CB  LEU C 267      36.004   1.503  55.773  1.00 38.01           C  
-ATOM   7095  CG  LEU C 267      35.194   0.285  56.239  1.00 38.58           C  
-ATOM   7096  CD1 LEU C 267      35.701  -0.987  55.566  1.00 38.04           C  
-ATOM   7097  CD2 LEU C 267      35.298   0.164  57.752  1.00 37.55           C  
-ATOM   7098  N   MET C 268      36.795   4.363  54.878  1.00 37.42           N  
-ATOM   7099  CA  MET C 268      37.798   5.380  54.592  1.00 37.38           C  
-ATOM   7100  C   MET C 268      37.703   6.570  55.539  1.00 37.76           C  
-ATOM   7101  O   MET C 268      38.723   7.081  56.004  1.00 36.30           O  
-ATOM   7102  CB  MET C 268      37.655   5.884  53.153  1.00 37.02           C  
-ATOM   7103  CG  MET C 268      38.164   4.927  52.107  1.00 40.24           C  
-ATOM   7104  SD  MET C 268      37.981   5.600  50.451  1.00 39.35           S  
-ATOM   7105  CE  MET C 268      37.548   4.126  49.552  1.00 41.35           C  
-ATOM   7106  N   LEU C 269      36.478   7.009  55.819  1.00 37.03           N  
-ATOM   7107  CA  LEU C 269      36.255   8.156  56.692  1.00 39.41           C  
-ATOM   7108  C   LEU C 269      36.305   7.843  58.186  1.00 41.50           C  
-ATOM   7109  O   LEU C 269      36.269   8.751  59.018  1.00 40.80           O  
-ATOM   7110  CB  LEU C 269      34.915   8.820  56.352  1.00 39.08           C  
-ATOM   7111  CG  LEU C 269      34.932   9.958  55.320  1.00 38.84           C  
-ATOM   7112  CD1 LEU C 269      35.672   9.521  54.068  1.00 37.02           C  
-ATOM   7113  CD2 LEU C 269      33.497  10.368  54.995  1.00 38.21           C  
-ATOM   7114  N   GLN C 270      36.391   6.563  58.526  1.00 43.48           N  
-ATOM   7115  CA  GLN C 270      36.444   6.172  59.925  1.00 44.80           C  
-ATOM   7116  C   GLN C 270      37.887   6.041  60.401  1.00 45.48           C  
-ATOM   7117  O   GLN C 270      38.138   5.873  61.594  1.00 45.89           O  
-ATOM   7118  CB  GLN C 270      35.693   4.852  60.138  1.00 45.19           C  
-ATOM   7119  CG  GLN C 270      34.254   4.878  59.638  1.00 44.24           C  
-ATOM   7120  CD  GLN C 270      33.547   6.184  59.960  1.00 46.22           C  
-ATOM   7121  OE1 GLN C 270      33.447   6.581  61.123  1.00 44.90           O  
-ATOM   7122  NE2 GLN C 270      33.053   6.861  58.927  1.00 43.47           N  
-ATOM   7123  N   GLN C 271      38.832   6.129  59.466  1.00 45.62           N  
-ATOM   7124  CA  GLN C 271      40.249   6.021  59.800  1.00 44.59           C  
-ATOM   7125  C   GLN C 271      40.729   7.245  60.570  1.00 44.73           C  
-ATOM   7126  O   GLN C 271      40.009   8.239  60.694  1.00 43.16           O  
-ATOM   7127  CB  GLN C 271      41.090   5.863  58.535  1.00 44.90           C  
-ATOM   7128  CG  GLN C 271      40.673   4.716  57.640  1.00 47.22           C  
-ATOM   7129  CD  GLN C 271      40.553   3.404  58.384  1.00 47.75           C  
-ATOM   7130  OE1 GLN C 271      39.651   3.221  59.199  1.00 49.25           O  
-ATOM   7131  NE2 GLN C 271      41.466   2.481  58.108  1.00 48.53           N  
-ATOM   7132  N   GLU C 272      41.953   7.166  61.083  1.00 45.41           N  
-ATOM   7133  CA  GLU C 272      42.538   8.260  61.849  1.00 45.26           C  
-ATOM   7134  C   GLU C 272      42.974   9.385  60.923  1.00 45.40           C  
-ATOM   7135  O   GLU C 272      42.755  10.563  61.217  1.00 45.83           O  
-ATOM   7136  CB  GLU C 272      43.733   7.754  62.661  1.00 45.48           C  
-ATOM   7137  N   LYS C 273      43.588   9.016  59.802  1.00 44.57           N  
-ATOM   7138  CA  LYS C 273      44.062   9.996  58.833  1.00 43.72           C  
-ATOM   7139  C   LYS C 273      43.401   9.810  57.471  1.00 42.78           C  
-ATOM   7140  O   LYS C 273      43.089   8.688  57.067  1.00 42.12           O  
-ATOM   7141  CB  LYS C 273      45.579   9.898  58.692  1.00 44.01           C  
-ATOM   7142  N   PRO C 274      43.171  10.917  56.748  1.00 41.03           N  
-ATOM   7143  CA  PRO C 274      42.547  10.864  55.423  1.00 39.65           C  
-ATOM   7144  C   PRO C 274      43.557  10.387  54.390  1.00 38.38           C  
-ATOM   7145  O   PRO C 274      44.744  10.690  54.491  1.00 39.45           O  
-ATOM   7146  CB  PRO C 274      42.129  12.308  55.189  1.00 39.13           C  
-ATOM   7147  CG  PRO C 274      43.244  13.065  55.860  1.00 41.00           C  
-ATOM   7148  CD  PRO C 274      43.396  12.314  57.164  1.00 39.61           C  
-ATOM   7149  N   ASP C 275      43.089   9.650  53.394  1.00 36.43           N  
-ATOM   7150  CA  ASP C 275      43.979   9.145  52.360  1.00 36.35           C  
-ATOM   7151  C   ASP C 275      43.155   8.743  51.136  1.00 34.89           C  
-ATOM   7152  O   ASP C 275      41.936   8.908  51.123  1.00 34.68           O  
-ATOM   7153  CB  ASP C 275      44.756   7.942  52.905  1.00 36.55           C  
-ATOM   7154  CG  ASP C 275      46.097   7.742  52.216  1.00 38.57           C  
-ATOM   7155  OD1 ASP C 275      46.884   6.900  52.699  1.00 39.76           O  
-ATOM   7156  OD2 ASP C 275      46.368   8.416  51.198  1.00 38.29           O  
-ATOM   7157  N   ASP C 276      43.823   8.222  50.114  1.00 33.28           N  
-ATOM   7158  CA  ASP C 276      43.147   7.796  48.893  1.00 33.14           C  
-ATOM   7159  C   ASP C 276      43.320   6.289  48.737  1.00 32.68           C  
-ATOM   7160  O   ASP C 276      44.414   5.759  48.945  1.00 32.39           O  
-ATOM   7161  CB  ASP C 276      43.735   8.521  47.680  1.00 31.20           C  
-ATOM   7162  CG  ASP C 276      43.832  10.020  47.891  1.00 32.40           C  
-ATOM   7163  OD1 ASP C 276      42.838  10.617  48.351  1.00 31.98           O  
-ATOM   7164  OD2 ASP C 276      44.901  10.602  47.595  1.00 34.24           O  
-ATOM   7165  N   TYR C 277      42.242   5.603  48.369  1.00 32.66           N  
-ATOM   7166  CA  TYR C 277      42.296   4.159  48.214  1.00 33.30           C  
-ATOM   7167  C   TYR C 277      41.598   3.623  46.973  1.00 33.91           C  
-ATOM   7168  O   TYR C 277      40.522   4.089  46.592  1.00 34.91           O  
-ATOM   7169  CB  TYR C 277      41.662   3.462  49.416  1.00 33.28           C  
-ATOM   7170  CG  TYR C 277      42.019   4.017  50.774  1.00 35.37           C  
-ATOM   7171  CD1 TYR C 277      41.449   5.204  51.237  1.00 36.03           C  
-ATOM   7172  CD2 TYR C 277      42.875   3.318  51.626  1.00 35.17           C  
-ATOM   7173  CE1 TYR C 277      41.718   5.675  52.519  1.00 37.31           C  
-ATOM   7174  CE2 TYR C 277      43.149   3.775  52.901  1.00 34.86           C  
-ATOM   7175  CZ  TYR C 277      42.569   4.949  53.345  1.00 37.32           C  
-ATOM   7176  OH  TYR C 277      42.830   5.389  54.620  1.00 40.89           O  
-ATOM   7177  N   VAL C 278      42.217   2.622  46.363  1.00 33.91           N  
-ATOM   7178  CA  VAL C 278      41.651   1.956  45.205  1.00 33.29           C  
-ATOM   7179  C   VAL C 278      40.748   0.853  45.757  1.00 34.62           C  
-ATOM   7180  O   VAL C 278      41.169   0.063  46.600  1.00 34.78           O  
-ATOM   7181  CB  VAL C 278      42.749   1.306  44.332  1.00 31.93           C  
-ATOM   7182  CG1 VAL C 278      42.177   0.123  43.556  1.00 31.65           C  
-ATOM   7183  CG2 VAL C 278      43.311   2.325  43.363  1.00 30.49           C  
-ATOM   7184  N   VAL C 279      39.503   0.815  45.296  1.00 35.32           N  
-ATOM   7185  CA  VAL C 279      38.558  -0.206  45.731  1.00 34.99           C  
-ATOM   7186  C   VAL C 279      38.172  -0.984  44.478  1.00 34.59           C  
-ATOM   7187  O   VAL C 279      37.581  -0.432  43.553  1.00 34.91           O  
-ATOM   7188  CB  VAL C 279      37.314   0.433  46.385  1.00 33.86           C  
-ATOM   7189  CG1 VAL C 279      36.343  -0.645  46.847  1.00 35.77           C  
-ATOM   7190  CG2 VAL C 279      37.744   1.290  47.564  1.00 34.70           C  
-ATOM   7191  N   ALA C 280      38.546  -2.258  44.441  1.00 34.21           N  
-ATOM   7192  CA  ALA C 280      38.269  -3.111  43.289  1.00 35.41           C  
-ATOM   7193  C   ALA C 280      38.306  -4.583  43.690  1.00 34.11           C  
-ATOM   7194  O   ALA C 280      38.481  -4.901  44.864  1.00 34.33           O  
-ATOM   7195  CB  ALA C 280      39.300  -2.843  42.186  1.00 32.23           C  
-ATOM   7196  N   THR C 281      38.143  -5.470  42.711  1.00 33.97           N  
-ATOM   7197  CA  THR C 281      38.157  -6.906  42.968  1.00 35.23           C  
-ATOM   7198  C   THR C 281      39.449  -7.537  42.450  1.00 36.67           C  
-ATOM   7199  O   THR C 281      39.692  -8.726  42.645  1.00 36.67           O  
-ATOM   7200  CB  THR C 281      36.961  -7.619  42.293  1.00 35.03           C  
-ATOM   7201  OG1 THR C 281      37.082  -7.527  40.866  1.00 36.11           O  
-ATOM   7202  CG2 THR C 281      35.653  -6.987  42.730  1.00 34.26           C  
-ATOM   7203  N   GLU C 282      40.269  -6.736  41.781  1.00 39.04           N  
-ATOM   7204  CA  GLU C 282      41.541  -7.213  41.245  1.00 41.26           C  
-ATOM   7205  C   GLU C 282      41.347  -8.312  40.208  1.00 40.68           C  
-ATOM   7206  O   GLU C 282      42.224  -9.149  40.019  1.00 41.48           O  
-ATOM   7207  CB  GLU C 282      42.431  -7.739  42.378  1.00 41.34           C  
-ATOM   7208  CG  GLU C 282      42.445  -6.850  43.610  1.00 45.52           C  
-ATOM   7209  CD  GLU C 282      43.495  -7.259  44.623  1.00 47.30           C  
-ATOM   7210  OE1 GLU C 282      43.593  -8.465  44.932  1.00 50.27           O  
-ATOM   7211  OE2 GLU C 282      44.218  -6.370  45.120  1.00 47.87           O  
-ATOM   7212  N   GLU C 283      40.194  -8.309  39.546  1.00 41.42           N  
-ATOM   7213  CA  GLU C 283      39.887  -9.302  38.518  1.00 42.58           C  
-ATOM   7214  C   GLU C 283      39.197  -8.643  37.333  1.00 40.66           C  
-ATOM   7215  O   GLU C 283      38.168  -7.991  37.489  1.00 41.03           O  
-ATOM   7216  CB  GLU C 283      38.991 -10.405  39.088  1.00 46.22           C  
-ATOM   7217  CG  GLU C 283      39.716 -11.379  40.002  1.00 53.51           C  
-ATOM   7218  CD  GLU C 283      38.773 -12.345  40.697  1.00 58.08           C  
-ATOM   7219  OE1 GLU C 283      37.944 -12.975  40.003  1.00 60.47           O  
-ATOM   7220  OE2 GLU C 283      38.865 -12.478  41.940  1.00 60.38           O  
-ATOM   7221  N   GLY C 284      39.768  -8.817  36.148  1.00 39.65           N  
-ATOM   7222  CA  GLY C 284      39.190  -8.212  34.966  1.00 38.26           C  
-ATOM   7223  C   GLY C 284      38.539  -9.200  34.021  1.00 38.58           C  
-ATOM   7224  O   GLY C 284      39.040 -10.303  33.811  1.00 38.82           O  
-ATOM   7225  N   HIS C 285      37.409  -8.795  33.451  1.00 37.85           N  
-ATOM   7226  CA  HIS C 285      36.668  -9.621  32.504  1.00 38.19           C  
-ATOM   7227  C   HIS C 285      36.200  -8.707  31.388  1.00 38.30           C  
-ATOM   7228  O   HIS C 285      35.944  -7.525  31.619  1.00 41.01           O  
-ATOM   7229  CB  HIS C 285      35.453 -10.261  33.182  1.00 37.52           C  
-ATOM   7230  CG  HIS C 285      35.802 -11.188  34.304  1.00 38.21           C  
-ATOM   7231  ND1 HIS C 285      36.288 -12.461  34.096  1.00 38.57           N  
-ATOM   7232  CD2 HIS C 285      35.760 -11.016  35.647  1.00 37.06           C  
-ATOM   7233  CE1 HIS C 285      36.527 -13.033  35.263  1.00 38.02           C  
-ATOM   7234  NE2 HIS C 285      36.216 -12.177  36.220  1.00 38.45           N  
-ATOM   7235  N   THR C 286      36.097  -9.241  30.179  1.00 38.48           N  
-ATOM   7236  CA  THR C 286      35.648  -8.445  29.045  1.00 39.53           C  
-ATOM   7237  C   THR C 286      34.124  -8.453  28.973  1.00 40.50           C  
-ATOM   7238  O   THR C 286      33.466  -9.230  29.668  1.00 40.39           O  
-ATOM   7239  CB  THR C 286      36.193  -9.003  27.730  1.00 38.24           C  
-ATOM   7240  OG1 THR C 286      35.691 -10.332  27.539  1.00 40.32           O  
-ATOM   7241  CG2 THR C 286      37.711  -9.031  27.760  1.00 38.11           C  
-ATOM   7242  N   VAL C 287      33.564  -7.584  28.136  1.00 41.22           N  
-ATOM   7243  CA  VAL C 287      32.116  -7.517  27.985  1.00 42.03           C  
-ATOM   7244  C   VAL C 287      31.606  -8.826  27.380  1.00 41.97           C  
-ATOM   7245  O   VAL C 287      30.503  -9.276  27.687  1.00 41.77           O  
-ATOM   7246  CB  VAL C 287      31.698  -6.327  27.081  1.00 41.92           C  
-ATOM   7247  CG1 VAL C 287      30.182  -6.307  26.901  1.00 41.90           C  
-ATOM   7248  CG2 VAL C 287      32.168  -5.017  27.697  1.00 41.54           C  
-ATOM   7249  N   GLU C 288      32.414  -9.440  26.521  1.00 42.67           N  
-ATOM   7250  CA  GLU C 288      32.018 -10.698  25.905  1.00 42.90           C  
-ATOM   7251  C   GLU C 288      31.872 -11.746  26.992  1.00 41.66           C  
-ATOM   7252  O   GLU C 288      30.892 -12.486  27.026  1.00 41.02           O  
-ATOM   7253  CB  GLU C 288      33.056 -11.162  24.891  1.00 45.00           C  
-ATOM   7254  CG  GLU C 288      32.748 -12.537  24.327  1.00 48.45           C  
-ATOM   7255  CD  GLU C 288      33.729 -12.964  23.262  1.00 50.75           C  
-ATOM   7256  OE1 GLU C 288      33.759 -12.317  22.190  1.00 52.01           O  
-ATOM   7257  OE2 GLU C 288      34.471 -13.943  23.500  1.00 52.02           O  
-ATOM   7258  N   GLU C 289      32.859 -11.812  27.878  1.00 41.26           N  
-ATOM   7259  CA  GLU C 289      32.806 -12.760  28.977  1.00 41.20           C  
-ATOM   7260  C   GLU C 289      31.512 -12.507  29.737  1.00 41.28           C  
-ATOM   7261  O   GLU C 289      30.847 -13.443  30.180  1.00 43.32           O  
-ATOM   7262  CB  GLU C 289      34.006 -12.568  29.904  1.00 41.67           C  
-ATOM   7263  CG  GLU C 289      35.326 -13.025  29.308  1.00 44.18           C  
-ATOM   7264  CD  GLU C 289      36.513 -12.647  30.174  1.00 45.43           C  
-ATOM   7265  OE1 GLU C 289      36.456 -12.876  31.405  1.00 44.26           O  
-ATOM   7266  OE2 GLU C 289      37.504 -12.124  29.619  1.00 46.86           O  
-ATOM   7267  N   PHE C 290      31.158 -11.232  29.881  1.00 40.04           N  
-ATOM   7268  CA  PHE C 290      29.934 -10.860  30.576  1.00 38.00           C  
-ATOM   7269  C   PHE C 290      28.759 -11.445  29.794  1.00 37.54           C  
-ATOM   7270  O   PHE C 290      27.832 -12.002  30.375  1.00 36.15           O  
-ATOM   7271  CB  PHE C 290      29.792  -9.336  30.645  1.00 35.69           C  
-ATOM   7272  CG  PHE C 290      28.734  -8.877  31.603  1.00 34.61           C  
-ATOM   7273  CD1 PHE C 290      29.058  -8.578  32.923  1.00 33.69           C  
-ATOM   7274  CD2 PHE C 290      27.404  -8.801  31.204  1.00 34.87           C  
-ATOM   7275  CE1 PHE C 290      28.075  -8.211  33.838  1.00 33.78           C  
-ATOM   7276  CE2 PHE C 290      26.412  -8.437  32.109  1.00 36.65           C  
-ATOM   7277  CZ  PHE C 290      26.750  -8.141  33.433  1.00 35.85           C  
-ATOM   7278  N   LEU C 291      28.818 -11.309  28.470  1.00 37.39           N  
-ATOM   7279  CA  LEU C 291      27.789 -11.822  27.576  1.00 38.27           C  
-ATOM   7280  C   LEU C 291      27.705 -13.346  27.601  1.00 41.73           C  
-ATOM   7281  O   LEU C 291      26.619 -13.910  27.447  1.00 42.93           O  
-ATOM   7282  CB  LEU C 291      28.053 -11.356  26.143  1.00 35.74           C  
-ATOM   7283  CG  LEU C 291      27.689  -9.901  25.847  1.00 34.98           C  
-ATOM   7284  CD1 LEU C 291      28.129  -9.519  24.444  1.00 32.42           C  
-ATOM   7285  CD2 LEU C 291      26.181  -9.732  26.011  1.00 34.56           C  
-ATOM   7286  N   ASP C 292      28.845 -14.014  27.781  1.00 43.11           N  
-ATOM   7287  CA  ASP C 292      28.855 -15.473  27.829  1.00 44.69           C  
-ATOM   7288  C   ASP C 292      28.174 -15.932  29.110  1.00 44.13           C  
-ATOM   7289  O   ASP C 292      27.222 -16.710  29.077  1.00 45.44           O  
-ATOM   7290  CB  ASP C 292      30.286 -16.033  27.794  1.00 45.54           C  
-ATOM   7291  CG  ASP C 292      31.009 -15.750  26.478  1.00 48.33           C  
-ATOM   7292  OD1 ASP C 292      30.372 -15.801  25.401  1.00 47.32           O  
-ATOM   7293  OD2 ASP C 292      32.232 -15.494  26.525  1.00 49.36           O  
-ATOM   7294  N   VAL C 293      28.662 -15.436  30.241  1.00 43.14           N  
-ATOM   7295  CA  VAL C 293      28.112 -15.808  31.538  1.00 42.24           C  
-ATOM   7296  C   VAL C 293      26.619 -15.537  31.678  1.00 41.91           C  
-ATOM   7297  O   VAL C 293      25.850 -16.442  31.997  1.00 43.06           O  
-ATOM   7298  CB  VAL C 293      28.844 -15.077  32.678  1.00 41.95           C  
-ATOM   7299  CG1 VAL C 293      28.187 -15.397  34.012  1.00 44.17           C  
-ATOM   7300  CG2 VAL C 293      30.304 -15.492  32.701  1.00 43.91           C  
-ATOM   7301  N   SER C 294      26.210 -14.294  31.444  1.00 41.11           N  
-ATOM   7302  CA  SER C 294      24.808 -13.919  31.575  1.00 39.91           C  
-ATOM   7303  C   SER C 294      23.853 -14.772  30.730  1.00 40.78           C  
-ATOM   7304  O   SER C 294      23.027 -15.503  31.277  1.00 41.58           O  
-ATOM   7305  CB  SER C 294      24.628 -12.424  31.259  1.00 37.37           C  
-ATOM   7306  OG  SER C 294      25.214 -12.061  30.019  1.00 32.50           O  
-ATOM   7307  N   PHE C 295      23.962 -14.688  29.408  1.00 40.93           N  
-ATOM   7308  CA  PHE C 295      23.089 -15.466  28.535  1.00 43.02           C  
-ATOM   7309  C   PHE C 295      23.172 -16.973  28.796  1.00 44.01           C  
-ATOM   7310  O   PHE C 295      22.147 -17.646  28.927  1.00 43.77           O  
-ATOM   7311  CB  PHE C 295      23.410 -15.167  27.066  1.00 43.29           C  
-ATOM   7312  CG  PHE C 295      22.845 -13.861  26.576  1.00 44.45           C  
-ATOM   7313  CD1 PHE C 295      23.229 -12.655  27.156  1.00 44.37           C  
-ATOM   7314  CD2 PHE C 295      21.916 -13.838  25.539  1.00 45.73           C  
-ATOM   7315  CE1 PHE C 295      22.695 -11.444  26.709  1.00 44.37           C  
-ATOM   7316  CE2 PHE C 295      21.373 -12.630  25.084  1.00 45.33           C  
-ATOM   7317  CZ  PHE C 295      21.765 -11.434  25.671  1.00 44.82           C  
-ATOM   7318  N   GLY C 296      24.390 -17.499  28.875  1.00 44.93           N  
-ATOM   7319  CA  GLY C 296      24.567 -18.918  29.125  1.00 44.80           C  
-ATOM   7320  C   GLY C 296      23.829 -19.360  30.374  1.00 46.38           C  
-ATOM   7321  O   GLY C 296      23.283 -20.465  30.433  1.00 47.16           O  
-ATOM   7322  N   TYR C 297      23.809 -18.489  31.377  1.00 46.24           N  
-ATOM   7323  CA  TYR C 297      23.133 -18.776  32.636  1.00 45.93           C  
-ATOM   7324  C   TYR C 297      21.659 -19.088  32.375  1.00 46.71           C  
-ATOM   7325  O   TYR C 297      21.008 -19.771  33.166  1.00 47.07           O  
-ATOM   7326  CB  TYR C 297      23.266 -17.575  33.570  1.00 45.48           C  
-ATOM   7327  CG  TYR C 297      22.601 -17.731  34.919  1.00 44.72           C  
-ATOM   7328  CD1 TYR C 297      22.904 -18.804  35.752  1.00 44.49           C  
-ATOM   7329  CD2 TYR C 297      21.702 -16.773  35.384  1.00 44.16           C  
-ATOM   7330  CE1 TYR C 297      22.330 -18.917  37.022  1.00 43.65           C  
-ATOM   7331  CE2 TYR C 297      21.124 -16.877  36.648  1.00 43.36           C  
-ATOM   7332  CZ  TYR C 297      21.443 -17.949  37.461  1.00 42.21           C  
-ATOM   7333  OH  TYR C 297      20.878 -18.046  38.712  1.00 42.12           O  
-ATOM   7334  N   LEU C 298      21.138 -18.581  31.263  1.00 46.36           N  
-ATOM   7335  CA  LEU C 298      19.747 -18.822  30.894  1.00 47.07           C  
-ATOM   7336  C   LEU C 298      19.717 -19.716  29.658  1.00 47.84           C  
-ATOM   7337  O   LEU C 298      18.758 -19.710  28.886  1.00 48.95           O  
-ATOM   7338  CB  LEU C 298      19.026 -17.501  30.607  1.00 45.85           C  
-ATOM   7339  CG  LEU C 298      18.950 -16.474  31.742  1.00 45.46           C  
-ATOM   7340  CD1 LEU C 298      18.159 -15.264  31.268  1.00 46.31           C  
-ATOM   7341  CD2 LEU C 298      18.291 -17.084  32.967  1.00 43.87           C  
-ATOM   7342  N   GLY C 299      20.792 -20.477  29.480  1.00 47.99           N  
-ATOM   7343  CA  GLY C 299      20.892 -21.386  28.355  1.00 46.86           C  
-ATOM   7344  C   GLY C 299      20.719 -20.752  26.993  1.00 46.20           C  
-ATOM   7345  O   GLY C 299      20.197 -21.389  26.080  1.00 47.08           O  
-ATOM   7346  N   LEU C 300      21.151 -19.505  26.839  1.00 46.67           N  
-ATOM   7347  CA  LEU C 300      21.028 -18.829  25.551  1.00 46.58           C  
-ATOM   7348  C   LEU C 300      22.391 -18.514  24.950  1.00 46.96           C  
-ATOM   7349  O   LEU C 300      23.402 -18.514  25.649  1.00 48.08           O  
-ATOM   7350  CB  LEU C 300      20.219 -17.538  25.698  1.00 45.61           C  
-ATOM   7351  CG  LEU C 300      18.744 -17.677  26.088  1.00 46.69           C  
-ATOM   7352  CD1 LEU C 300      18.113 -16.289  26.176  1.00 45.68           C  
-ATOM   7353  CD2 LEU C 300      18.006 -18.531  25.061  1.00 44.57           C  
-ATOM   7354  N   ASN C 301      22.412 -18.254  23.648  1.00 48.11           N  
-ATOM   7355  CA  ASN C 301      23.649 -17.931  22.947  1.00 50.24           C  
-ATOM   7356  C   ASN C 301      23.603 -16.481  22.471  1.00 49.72           C  
-ATOM   7357  O   ASN C 301      23.039 -16.182  21.414  1.00 48.21           O  
-ATOM   7358  CB  ASN C 301      23.835 -18.873  21.754  1.00 52.55           C  
-ATOM   7359  CG  ASN C 301      25.052 -18.526  20.919  1.00 55.95           C  
-ATOM   7360  OD1 ASN C 301      26.158 -18.370  21.443  1.00 57.97           O  
-ATOM   7361  ND2 ASN C 301      24.856 -18.409  19.610  1.00 56.95           N  
-ATOM   7362  N   TRP C 302      24.208 -15.588  23.253  1.00 49.28           N  
-ATOM   7363  CA  TRP C 302      24.214 -14.164  22.935  1.00 47.14           C  
-ATOM   7364  C   TRP C 302      24.483 -13.848  21.473  1.00 47.53           C  
-ATOM   7365  O   TRP C 302      23.950 -12.873  20.942  1.00 48.12           O  
-ATOM   7366  CB  TRP C 302      25.221 -13.408  23.816  1.00 44.45           C  
-ATOM   7367  CG  TRP C 302      26.679 -13.688  23.551  1.00 41.78           C  
-ATOM   7368  CD1 TRP C 302      27.481 -14.582  24.211  1.00 40.96           C  
-ATOM   7369  CD2 TRP C 302      27.517 -13.034  22.589  1.00 39.21           C  
-ATOM   7370  NE1 TRP C 302      28.764 -14.517  23.720  1.00 39.44           N  
-ATOM   7371  CE2 TRP C 302      28.814 -13.577  22.725  1.00 38.13           C  
-ATOM   7372  CE3 TRP C 302      27.298 -12.039  21.627  1.00 37.55           C  
-ATOM   7373  CZ2 TRP C 302      29.888 -13.157  21.935  1.00 39.25           C  
-ATOM   7374  CZ3 TRP C 302      28.366 -11.621  20.841  1.00 37.99           C  
-ATOM   7375  CH2 TRP C 302      29.647 -12.180  21.002  1.00 37.76           C  
-ATOM   7376  N   LYS C 303      25.301 -14.666  20.819  1.00 48.30           N  
-ATOM   7377  CA  LYS C 303      25.617 -14.440  19.413  1.00 49.62           C  
-ATOM   7378  C   LYS C 303      24.372 -14.518  18.535  1.00 49.80           C  
-ATOM   7379  O   LYS C 303      24.398 -14.113  17.374  1.00 48.25           O  
-ATOM   7380  CB  LYS C 303      26.667 -15.448  18.936  1.00 51.43           C  
-ATOM   7381  CG  LYS C 303      28.058 -15.202  19.514  1.00 52.94           C  
-ATOM   7382  CD  LYS C 303      29.075 -16.200  18.982  1.00 52.83           C  
-ATOM   7383  CE  LYS C 303      30.470 -15.894  19.502  1.00 52.58           C  
-ATOM   7384  NZ  LYS C 303      31.469 -16.915  19.068  1.00 52.65           N  
-ATOM   7385  N   ASP C 304      23.283 -15.035  19.099  1.00 50.69           N  
-ATOM   7386  CA  ASP C 304      22.020 -15.153  18.375  1.00 51.64           C  
-ATOM   7387  C   ASP C 304      21.177 -13.881  18.455  1.00 51.98           C  
-ATOM   7388  O   ASP C 304      20.257 -13.697  17.654  1.00 52.65           O  
-ATOM   7389  CB  ASP C 304      21.185 -16.319  18.924  1.00 52.05           C  
-ATOM   7390  CG  ASP C 304      21.684 -17.671  18.457  1.00 52.71           C  
-ATOM   7391  OD1 ASP C 304      21.784 -17.871  17.227  1.00 53.44           O  
-ATOM   7392  OD2 ASP C 304      21.969 -18.534  19.316  1.00 52.26           O  
-ATOM   7393  N   TYR C 305      21.483 -13.005  19.410  1.00 50.57           N  
-ATOM   7394  CA  TYR C 305      20.703 -11.782  19.574  1.00 49.19           C  
-ATOM   7395  C   TYR C 305      21.499 -10.483  19.533  1.00 47.99           C  
-ATOM   7396  O   TYR C 305      20.918  -9.410  19.379  1.00 48.09           O  
-ATOM   7397  CB  TYR C 305      19.928 -11.828  20.893  1.00 49.64           C  
-ATOM   7398  CG  TYR C 305      19.435 -13.202  21.279  1.00 50.09           C  
-ATOM   7399  CD1 TYR C 305      20.281 -14.115  21.914  1.00 49.96           C  
-ATOM   7400  CD2 TYR C 305      18.122 -13.595  21.008  1.00 51.06           C  
-ATOM   7401  CE1 TYR C 305      19.832 -15.385  22.272  1.00 49.97           C  
-ATOM   7402  CE2 TYR C 305      17.662 -14.864  21.360  1.00 50.84           C  
-ATOM   7403  CZ  TYR C 305      18.521 -15.753  21.992  1.00 51.81           C  
-ATOM   7404  OH  TYR C 305      18.067 -17.006  22.344  1.00 53.30           O  
-ATOM   7405  N   VAL C 306      22.817 -10.569  19.668  1.00 47.28           N  
-ATOM   7406  CA  VAL C 306      23.646  -9.368  19.677  1.00 47.22           C  
-ATOM   7407  C   VAL C 306      24.095  -8.882  18.304  1.00 47.51           C  
-ATOM   7408  O   VAL C 306      24.311  -9.672  17.387  1.00 48.63           O  
-ATOM   7409  CB  VAL C 306      24.902  -9.571  20.564  1.00 47.56           C  
-ATOM   7410  CG1 VAL C 306      25.744  -8.304  20.586  1.00 46.94           C  
-ATOM   7411  CG2 VAL C 306      24.483  -9.943  21.979  1.00 46.00           C  
-ATOM   7412  N   GLU C 307      24.214  -7.565  18.177  1.00 46.77           N  
-ATOM   7413  CA  GLU C 307      24.664  -6.926  16.948  1.00 46.68           C  
-ATOM   7414  C   GLU C 307      25.507  -5.719  17.339  1.00 46.91           C  
-ATOM   7415  O   GLU C 307      25.316  -5.147  18.413  1.00 46.34           O  
-ATOM   7416  CB  GLU C 307      23.478  -6.493  16.090  1.00 47.59           C  
-ATOM   7417  CG  GLU C 307      22.836  -7.637  15.322  1.00 51.44           C  
-ATOM   7418  CD  GLU C 307      21.784  -7.159  14.344  1.00 52.29           C  
-ATOM   7419  OE1 GLU C 307      22.104  -6.280  13.514  1.00 54.05           O  
-ATOM   7420  OE2 GLU C 307      20.642  -7.664  14.403  1.00 52.29           O  
-ATOM   7421  N   ILE C 308      26.434  -5.330  16.468  1.00 45.68           N  
-ATOM   7422  CA  ILE C 308      27.321  -4.212  16.758  1.00 44.31           C  
-ATOM   7423  C   ILE C 308      26.983  -2.932  16.005  1.00 45.67           C  
-ATOM   7424  O   ILE C 308      26.899  -2.921  14.777  1.00 47.48           O  
-ATOM   7425  CB  ILE C 308      28.784  -4.594  16.458  1.00 42.06           C  
-ATOM   7426  CG1 ILE C 308      29.132  -5.901  17.178  1.00 40.89           C  
-ATOM   7427  CG2 ILE C 308      29.720  -3.471  16.886  1.00 40.80           C  
-ATOM   7428  CD1 ILE C 308      28.865  -5.886  18.668  1.00 41.62           C  
-ATOM   7429  N   ASP C 309      26.802  -1.849  16.753  1.00 45.76           N  
-ATOM   7430  CA  ASP C 309      26.481  -0.554  16.167  1.00 45.87           C  
-ATOM   7431  C   ASP C 309      27.586   0.436  16.523  1.00 45.05           C  
-ATOM   7432  O   ASP C 309      27.900   0.629  17.696  1.00 44.99           O  
-ATOM   7433  CB  ASP C 309      25.135  -0.065  16.704  1.00 47.83           C  
-ATOM   7434  CG  ASP C 309      24.664   1.214  16.037  1.00 50.28           C  
-ATOM   7435  OD1 ASP C 309      23.515   1.624  16.308  1.00 53.04           O  
-ATOM   7436  OD2 ASP C 309      25.432   1.809  15.249  1.00 50.11           O  
-ATOM   7437  N   GLN C 310      28.174   1.054  15.503  1.00 43.75           N  
-ATOM   7438  CA  GLN C 310      29.254   2.020  15.686  1.00 43.71           C  
-ATOM   7439  C   GLN C 310      28.903   3.142  16.670  1.00 43.89           C  
-ATOM   7440  O   GLN C 310      29.770   3.647  17.387  1.00 43.00           O  
-ATOM   7441  CB  GLN C 310      29.644   2.614  14.336  1.00 42.35           C  
-ATOM   7442  N   ARG C 311      27.631   3.527  16.700  1.00 43.49           N  
-ATOM   7443  CA  ARG C 311      27.171   4.590  17.584  1.00 44.17           C  
-ATOM   7444  C   ARG C 311      27.536   4.360  19.055  1.00 43.21           C  
-ATOM   7445  O   ARG C 311      27.619   5.313  19.831  1.00 43.62           O  
-ATOM   7446  CB  ARG C 311      25.658   4.763  17.443  1.00 43.01           C  
-ATOM   7447  N   TYR C 312      27.760   3.107  19.440  1.00 43.41           N  
-ATOM   7448  CA  TYR C 312      28.095   2.803  20.828  1.00 43.66           C  
-ATOM   7449  C   TYR C 312      29.582   2.771  21.132  1.00 43.07           C  
-ATOM   7450  O   TYR C 312      29.990   2.356  22.218  1.00 42.11           O  
-ATOM   7451  CB  TYR C 312      27.449   1.488  21.258  1.00 44.90           C  
-ATOM   7452  CG  TYR C 312      25.944   1.556  21.230  1.00 48.24           C  
-ATOM   7453  CD1 TYR C 312      25.223   1.043  20.152  1.00 47.74           C  
-ATOM   7454  CD2 TYR C 312      25.240   2.192  22.254  1.00 48.23           C  
-ATOM   7455  CE1 TYR C 312      23.839   1.165  20.093  1.00 48.91           C  
-ATOM   7456  CE2 TYR C 312      23.856   2.321  22.202  1.00 49.42           C  
-ATOM   7457  CZ  TYR C 312      23.165   1.806  21.119  1.00 48.87           C  
-ATOM   7458  OH  TYR C 312      21.801   1.946  21.057  1.00 51.68           O  
-ATOM   7459  N   PHE C 313      30.389   3.202  20.168  1.00 42.29           N  
-ATOM   7460  CA  PHE C 313      31.829   3.263  20.358  1.00 42.80           C  
-ATOM   7461  C   PHE C 313      32.138   4.671  20.844  1.00 41.26           C  
-ATOM   7462  O   PHE C 313      31.479   5.630  20.430  1.00 40.48           O  
-ATOM   7463  CB  PHE C 313      32.582   3.023  19.043  1.00 45.06           C  
-ATOM   7464  CG  PHE C 313      32.465   1.624  18.515  1.00 47.78           C  
-ATOM   7465  CD1 PHE C 313      32.524   0.530  19.374  1.00 48.18           C  
-ATOM   7466  CD2 PHE C 313      32.328   1.397  17.150  1.00 49.33           C  
-ATOM   7467  CE1 PHE C 313      32.447  -0.771  18.882  1.00 48.11           C  
-ATOM   7468  CE2 PHE C 313      32.250   0.099  16.648  1.00 49.56           C  
-ATOM   7469  CZ  PHE C 313      32.309  -0.987  17.520  1.00 49.43           C  
-ATOM   7470  N   ARG C 314      33.131   4.790  21.722  1.00 39.12           N  
-ATOM   7471  CA  ARG C 314      33.534   6.090  22.243  1.00 37.87           C  
-ATOM   7472  C   ARG C 314      34.643   6.648  21.355  1.00 36.33           C  
-ATOM   7473  O   ARG C 314      35.440   5.895  20.806  1.00 35.77           O  
-ATOM   7474  CB  ARG C 314      34.042   5.969  23.689  1.00 37.95           C  
-ATOM   7475  CG  ARG C 314      32.954   5.759  24.752  1.00 36.13           C  
-ATOM   7476  CD  ARG C 314      32.408   4.347  24.732  1.00 34.38           C  
-ATOM   7477  NE  ARG C 314      31.288   4.157  25.653  1.00 32.72           N  
-ATOM   7478  CZ  ARG C 314      31.393   4.086  26.977  1.00 30.38           C  
-ATOM   7479  NH1 ARG C 314      30.307   3.910  27.718  1.00 30.35           N  
-ATOM   7480  NH2 ARG C 314      32.575   4.189  27.564  1.00 30.06           N  
-ATOM   7481  N   PRO C 315      34.699   7.981  21.197  1.00 35.38           N  
-ATOM   7482  CA  PRO C 315      35.717   8.640  20.371  1.00 34.77           C  
-ATOM   7483  C   PRO C 315      37.132   8.223  20.773  1.00 34.59           C  
-ATOM   7484  O   PRO C 315      38.041   8.172  19.947  1.00 34.86           O  
-ATOM   7485  CB  PRO C 315      35.446  10.121  20.619  1.00 33.01           C  
-ATOM   7486  CG  PRO C 315      33.969  10.148  20.801  1.00 32.55           C  
-ATOM   7487  CD  PRO C 315      33.745   8.970  21.726  1.00 34.37           C  
-ATOM   7488  N   ALA C 316      37.302   7.936  22.058  1.00 35.47           N  
-ATOM   7489  CA  ALA C 316      38.573   7.495  22.615  1.00 34.83           C  
-ATOM   7490  C   ALA C 316      38.168   6.467  23.657  1.00 35.82           C  
-ATOM   7491  O   ALA C 316      37.383   6.767  24.559  1.00 35.68           O  
-ATOM   7492  CB  ALA C 316      39.307   8.659  23.267  1.00 36.72           C  
-ATOM   7493  N   GLU C 317      38.699   5.255  23.528  1.00 36.03           N  
-ATOM   7494  CA  GLU C 317      38.349   4.162  24.427  1.00 36.52           C  
-ATOM   7495  C   GLU C 317      39.355   3.866  25.528  1.00 36.01           C  
-ATOM   7496  O   GLU C 317      40.532   4.226  25.439  1.00 36.62           O  
-ATOM   7497  CB  GLU C 317      38.114   2.891  23.596  1.00 37.47           C  
-ATOM   7498  CG  GLU C 317      37.743   1.628  24.377  1.00 38.35           C  
-ATOM   7499  CD  GLU C 317      36.386   1.709  25.059  1.00 40.08           C  
-ATOM   7500  OE1 GLU C 317      36.310   2.224  26.198  1.00 39.43           O  
-ATOM   7501  OE2 GLU C 317      35.390   1.259  24.452  1.00 39.84           O  
-ATOM   7502  N   VAL C 318      38.850   3.214  26.571  1.00 35.22           N  
-ATOM   7503  CA  VAL C 318      39.628   2.776  27.724  1.00 34.96           C  
-ATOM   7504  C   VAL C 318      39.666   1.253  27.593  1.00 36.42           C  
-ATOM   7505  O   VAL C 318      38.674   0.574  27.860  1.00 35.37           O  
-ATOM   7506  CB  VAL C 318      38.932   3.159  29.047  1.00 35.06           C  
-ATOM   7507  CG1 VAL C 318      39.603   2.452  30.212  1.00 35.82           C  
-ATOM   7508  CG2 VAL C 318      38.991   4.669  29.244  1.00 32.92           C  
-ATOM   7509  N   ASP C 319      40.817   0.727  27.183  1.00 38.63           N  
-ATOM   7510  CA  ASP C 319      40.991  -0.706  26.951  1.00 39.89           C  
-ATOM   7511  C   ASP C 319      40.926  -1.691  28.112  1.00 38.89           C  
-ATOM   7512  O   ASP C 319      40.035  -2.535  28.165  1.00 37.90           O  
-ATOM   7513  CB  ASP C 319      42.301  -0.945  26.198  1.00 41.85           C  
-ATOM   7514  CG  ASP C 319      42.291  -0.346  24.804  1.00 45.77           C  
-ATOM   7515  OD1 ASP C 319      43.311  -0.486  24.092  1.00 46.96           O  
-ATOM   7516  OD2 ASP C 319      41.266   0.263  24.420  1.00 45.91           O  
-ATOM   7517  N   ASN C 320      41.870  -1.597  29.037  1.00 38.93           N  
-ATOM   7518  CA  ASN C 320      41.914  -2.549  30.133  1.00 40.09           C  
-ATOM   7519  C   ASN C 320      42.049  -1.938  31.524  1.00 38.72           C  
-ATOM   7520  O   ASN C 320      43.003  -1.219  31.811  1.00 38.53           O  
-ATOM   7521  CB  ASN C 320      43.063  -3.531  29.863  1.00 42.30           C  
-ATOM   7522  CG  ASN C 320      43.089  -4.700  30.830  1.00 44.41           C  
-ATOM   7523  OD1 ASN C 320      43.779  -5.690  30.591  1.00 48.59           O  
-ATOM   7524  ND2 ASN C 320      42.349  -4.592  31.927  1.00 45.83           N  
-ATOM   7525  N   LEU C 321      41.090  -2.242  32.390  1.00 38.24           N  
-ATOM   7526  CA  LEU C 321      41.113  -1.735  33.755  1.00 38.53           C  
-ATOM   7527  C   LEU C 321      41.009  -2.870  34.764  1.00 39.02           C  
-ATOM   7528  O   LEU C 321      40.060  -3.650  34.743  1.00 39.81           O  
-ATOM   7529  CB  LEU C 321      39.962  -0.750  33.992  1.00 37.55           C  
-ATOM   7530  CG  LEU C 321      39.969   0.577  33.230  1.00 37.79           C  
-ATOM   7531  CD1 LEU C 321      38.702   1.353  33.577  1.00 36.84           C  
-ATOM   7532  CD2 LEU C 321      41.210   1.385  33.587  1.00 35.44           C  
-ATOM   7533  N   GLN C 322      42.002  -2.955  35.641  1.00 40.12           N  
-ATOM   7534  CA  GLN C 322      42.037  -3.969  36.687  1.00 40.76           C  
-ATOM   7535  C   GLN C 322      42.772  -3.349  37.864  1.00 40.71           C  
-ATOM   7536  O   GLN C 322      43.919  -2.923  37.734  1.00 40.43           O  
-ATOM   7537  CB  GLN C 322      42.777  -5.222  36.216  1.00 42.22           C  
-ATOM   7538  CG  GLN C 322      42.754  -6.349  37.237  1.00 43.96           C  
-ATOM   7539  CD  GLN C 322      43.655  -7.507  36.859  1.00 46.20           C  
-ATOM   7540  OE1 GLN C 322      43.514  -8.096  35.786  1.00 46.86           O  
-ATOM   7541  NE2 GLN C 322      44.589  -7.841  37.743  1.00 47.12           N  
-ATOM   7542  N   GLY C 323      42.114  -3.304  39.014  1.00 40.80           N  
-ATOM   7543  CA  GLY C 323      42.722  -2.687  40.175  1.00 41.15           C  
-ATOM   7544  C   GLY C 323      43.608  -3.517  41.083  1.00 41.34           C  
-ATOM   7545  O   GLY C 323      43.641  -4.749  41.033  1.00 41.12           O  
-ATOM   7546  N   ASP C 324      44.340  -2.791  41.919  1.00 41.28           N  
-ATOM   7547  CA  ASP C 324      45.239  -3.354  42.913  1.00 40.45           C  
-ATOM   7548  C   ASP C 324      44.744  -2.724  44.212  1.00 39.48           C  
-ATOM   7549  O   ASP C 324      45.107  -1.589  44.536  1.00 37.60           O  
-ATOM   7550  CB  ASP C 324      46.679  -2.929  42.612  1.00 40.20           C  
-ATOM   7551  CG  ASP C 324      47.668  -3.410  43.658  1.00 40.23           C  
-ATOM   7552  OD1 ASP C 324      48.872  -3.110  43.513  1.00 41.78           O  
-ATOM   7553  OD2 ASP C 324      47.247  -4.079  44.624  1.00 41.12           O  
-ATOM   7554  N   ALA C 325      43.898  -3.457  44.936  1.00 39.04           N  
-ATOM   7555  CA  ALA C 325      43.308  -2.968  46.183  1.00 39.38           C  
-ATOM   7556  C   ALA C 325      44.030  -3.432  47.436  1.00 39.80           C  
-ATOM   7557  O   ALA C 325      43.421  -3.568  48.501  1.00 40.14           O  
-ATOM   7558  CB  ALA C 325      41.846  -3.381  46.255  1.00 39.68           C  
-ATOM   7559  N   SER C 326      45.330  -3.663  47.314  1.00 39.65           N  
-ATOM   7560  CA  SER C 326      46.123  -4.112  48.446  1.00 40.14           C  
-ATOM   7561  C   SER C 326      46.033  -3.127  49.604  1.00 40.26           C  
-ATOM   7562  O   SER C 326      45.917  -3.525  50.764  1.00 41.85           O  
-ATOM   7563  CB  SER C 326      47.578  -4.280  48.020  1.00 41.02           C  
-ATOM   7564  OG  SER C 326      47.661  -5.110  46.874  1.00 42.21           O  
-ATOM   7565  N   LYS C 327      46.069  -1.837  49.284  1.00 39.61           N  
-ATOM   7566  CA  LYS C 327      46.008  -0.801  50.308  1.00 39.06           C  
-ATOM   7567  C   LYS C 327      44.685  -0.801  51.071  1.00 38.42           C  
-ATOM   7568  O   LYS C 327      44.664  -0.584  52.281  1.00 38.76           O  
-ATOM   7569  CB  LYS C 327      46.259   0.574  49.674  1.00 38.31           C  
-ATOM   7570  CG  LYS C 327      46.446   1.706  50.681  1.00 36.98           C  
-ATOM   7571  CD  LYS C 327      46.702   3.038  49.978  1.00 36.05           C  
-ATOM   7572  CE  LYS C 327      46.730   4.191  50.971  1.00 37.27           C  
-ATOM   7573  NZ  LYS C 327      46.896   5.510  50.298  1.00 37.38           N  
-ATOM   7574  N   ALA C 328      43.582  -1.041  50.370  1.00 38.79           N  
-ATOM   7575  CA  ALA C 328      42.271  -1.072  51.017  1.00 38.92           C  
-ATOM   7576  C   ALA C 328      42.179  -2.247  51.992  1.00 38.32           C  
-ATOM   7577  O   ALA C 328      41.705  -2.099  53.122  1.00 39.27           O  
-ATOM   7578  CB  ALA C 328      41.168  -1.178  49.966  1.00 36.48           C  
-ATOM   7579  N   LYS C 329      42.634  -3.415  51.548  1.00 38.19           N  
-ATOM   7580  CA  LYS C 329      42.608  -4.613  52.377  1.00 39.08           C  
-ATOM   7581  C   LYS C 329      43.465  -4.444  53.630  1.00 40.45           C  
-ATOM   7582  O   LYS C 329      42.988  -4.633  54.751  1.00 40.12           O  
-ATOM   7583  CB  LYS C 329      43.093  -5.811  51.573  1.00 37.73           C  
-ATOM   7584  N   GLU C 330      44.725  -4.064  53.433  1.00 40.79           N  
-ATOM   7585  CA  GLU C 330      45.664  -3.882  54.535  1.00 41.77           C  
-ATOM   7586  C   GLU C 330      45.300  -2.781  55.526  1.00 43.11           C  
-ATOM   7587  O   GLU C 330      45.424  -2.972  56.738  1.00 44.70           O  
-ATOM   7588  CB  GLU C 330      47.065  -3.635  53.981  1.00 41.58           C  
-ATOM   7589  N   VAL C 331      44.853  -1.633  55.023  1.00 43.70           N  
-ATOM   7590  CA  VAL C 331      44.506  -0.506  55.891  1.00 41.68           C  
-ATOM   7591  C   VAL C 331      43.060  -0.474  56.375  1.00 42.46           C  
-ATOM   7592  O   VAL C 331      42.803  -0.348  57.573  1.00 43.17           O  
-ATOM   7593  CB  VAL C 331      44.799   0.846  55.195  1.00 41.67           C  
-ATOM   7594  CG1 VAL C 331      44.374   2.002  56.093  1.00 40.75           C  
-ATOM   7595  CG2 VAL C 331      46.281   0.953  54.866  1.00 40.85           C  
-ATOM   7596  N   LEU C 332      42.119  -0.579  55.444  1.00 42.33           N  
-ATOM   7597  CA  LEU C 332      40.703  -0.528  55.782  1.00 42.94           C  
-ATOM   7598  C   LEU C 332      40.146  -1.890  56.172  1.00 44.03           C  
-ATOM   7599  O   LEU C 332      39.109  -1.982  56.831  1.00 44.14           O  
-ATOM   7600  CB  LEU C 332      39.910   0.021  54.596  1.00 41.81           C  
-ATOM   7601  CG  LEU C 332      40.377   1.362  54.018  1.00 41.03           C  
-ATOM   7602  CD1 LEU C 332      39.525   1.700  52.803  1.00 39.45           C  
-ATOM   7603  CD2 LEU C 332      40.278   2.461  55.072  1.00 36.96           C  
-ATOM   7604  N   GLY C 333      40.842  -2.946  55.766  1.00 45.12           N  
-ATOM   7605  CA  GLY C 333      40.375  -4.282  56.072  1.00 44.89           C  
-ATOM   7606  C   GLY C 333      39.176  -4.575  55.200  1.00 44.74           C  
-ATOM   7607  O   GLY C 333      38.274  -5.310  55.590  1.00 45.17           O  
-ATOM   7608  N   TRP C 334      39.169  -3.985  54.008  1.00 44.93           N  
-ATOM   7609  CA  TRP C 334      38.073  -4.177  53.068  1.00 43.57           C  
-ATOM   7610  C   TRP C 334      38.368  -5.269  52.047  1.00 42.77           C  
-ATOM   7611  O   TRP C 334      39.470  -5.354  51.508  1.00 42.54           O  
-ATOM   7612  CB  TRP C 334      37.771  -2.877  52.318  1.00 42.31           C  
-ATOM   7613  CG  TRP C 334      36.620  -3.019  51.363  1.00 39.27           C  
-ATOM   7614  CD1 TRP C 334      35.292  -2.877  51.650  1.00 38.78           C  
-ATOM   7615  CD2 TRP C 334      36.694  -3.394  49.983  1.00 37.16           C  
-ATOM   7616  NE1 TRP C 334      34.535  -3.142  50.534  1.00 38.12           N  
-ATOM   7617  CE2 TRP C 334      35.370  -3.462  49.497  1.00 36.87           C  
-ATOM   7618  CE3 TRP C 334      37.752  -3.681  49.109  1.00 37.74           C  
-ATOM   7619  CZ2 TRP C 334      35.074  -3.805  48.175  1.00 36.12           C  
-ATOM   7620  CZ3 TRP C 334      37.457  -4.023  47.793  1.00 35.89           C  
-ATOM   7621  CH2 TRP C 334      36.127  -4.081  47.341  1.00 36.71           C  
-ATOM   7622  N   LYS C 335      37.363  -6.091  51.779  1.00 42.88           N  
-ATOM   7623  CA  LYS C 335      37.480  -7.177  50.817  1.00 43.83           C  
-ATOM   7624  C   LYS C 335      36.127  -7.347  50.140  1.00 44.24           C  
-ATOM   7625  O   LYS C 335      35.088  -7.316  50.800  1.00 46.78           O  
-ATOM   7626  CB  LYS C 335      37.878  -8.468  51.527  1.00 43.58           C  
-ATOM   7627  N   PRO C 336      36.115  -7.516  48.813  1.00 43.69           N  
-ATOM   7628  CA  PRO C 336      34.848  -7.689  48.099  1.00 43.99           C  
-ATOM   7629  C   PRO C 336      34.231  -9.053  48.395  1.00 45.33           C  
-ATOM   7630  O   PRO C 336      34.881 -10.082  48.211  1.00 47.93           O  
-ATOM   7631  CB  PRO C 336      35.261  -7.545  46.639  1.00 42.87           C  
-ATOM   7632  CG  PRO C 336      36.630  -8.136  46.629  1.00 42.30           C  
-ATOM   7633  CD  PRO C 336      37.255  -7.546  47.881  1.00 43.85           C  
-ATOM   7634  N   GLN C 337      32.980  -9.061  48.848  1.00 44.63           N  
-ATOM   7635  CA  GLN C 337      32.299 -10.313  49.165  1.00 44.40           C  
-ATOM   7636  C   GLN C 337      31.678 -10.984  47.935  1.00 44.16           C  
-ATOM   7637  O   GLN C 337      31.663 -12.209  47.833  1.00 46.04           O  
-ATOM   7638  CB  GLN C 337      31.224 -10.070  50.234  1.00 42.98           C  
-ATOM   7639  N   VAL C 338      31.174 -10.187  46.998  1.00 42.78           N  
-ATOM   7640  CA  VAL C 338      30.553 -10.738  45.798  1.00 41.21           C  
-ATOM   7641  C   VAL C 338      31.528 -10.849  44.633  1.00 41.78           C  
-ATOM   7642  O   VAL C 338      32.154  -9.868  44.241  1.00 41.30           O  
-ATOM   7643  CB  VAL C 338      29.350  -9.882  45.343  1.00 38.89           C  
-ATOM   7644  CG1 VAL C 338      28.696 -10.511  44.128  1.00 39.12           C  
-ATOM   7645  CG2 VAL C 338      28.351  -9.751  46.471  1.00 38.55           C  
-ATOM   7646  N   GLY C 339      31.640 -12.052  44.077  1.00 42.46           N  
-ATOM   7647  CA  GLY C 339      32.534 -12.271  42.954  1.00 41.04           C  
-ATOM   7648  C   GLY C 339      31.861 -11.989  41.627  1.00 40.66           C  
-ATOM   7649  O   GLY C 339      30.656 -11.758  41.577  1.00 42.19           O  
-ATOM   7650  N   PHE C 340      32.639 -12.014  40.549  1.00 40.71           N  
-ATOM   7651  CA  PHE C 340      32.122 -11.746  39.211  1.00 40.95           C  
-ATOM   7652  C   PHE C 340      30.897 -12.593  38.865  1.00 43.74           C  
-ATOM   7653  O   PHE C 340      29.804 -12.057  38.662  1.00 43.88           O  
-ATOM   7654  CB  PHE C 340      33.219 -11.988  38.181  1.00 39.08           C  
-ATOM   7655  CG  PHE C 340      32.794 -11.725  36.769  1.00 39.96           C  
-ATOM   7656  CD1 PHE C 340      32.866 -12.730  35.811  1.00 40.17           C  
-ATOM   7657  CD2 PHE C 340      32.354 -10.465  36.385  1.00 40.69           C  
-ATOM   7658  CE1 PHE C 340      32.511 -12.486  34.487  1.00 39.07           C  
-ATOM   7659  CE2 PHE C 340      31.996 -10.208  35.061  1.00 40.43           C  
-ATOM   7660  CZ  PHE C 340      32.076 -11.222  34.112  1.00 39.01           C  
-ATOM   7661  N   GLU C 341      31.085 -13.910  38.791  1.00 45.18           N  
-ATOM   7662  CA  GLU C 341      29.998 -14.834  38.467  1.00 45.76           C  
-ATOM   7663  C   GLU C 341      28.747 -14.503  39.272  1.00 44.95           C  
-ATOM   7664  O   GLU C 341      27.669 -14.319  38.706  1.00 44.69           O  
-ATOM   7665  CB  GLU C 341      30.404 -16.281  38.773  1.00 49.25           C  
-ATOM   7666  CG  GLU C 341      31.613 -16.812  38.006  1.00 54.43           C  
-ATOM   7667  CD  GLU C 341      31.314 -17.106  36.547  1.00 57.01           C  
-ATOM   7668  OE1 GLU C 341      30.992 -16.155  35.800  1.00 59.34           O  
-ATOM   7669  OE2 GLU C 341      31.404 -18.290  36.149  1.00 57.34           O  
-ATOM   7670  N   LYS C 342      28.897 -14.433  40.593  1.00 42.46           N  
-ATOM   7671  CA  LYS C 342      27.777 -14.136  41.476  1.00 42.41           C  
-ATOM   7672  C   LYS C 342      27.108 -12.807  41.134  1.00 42.35           C  
-ATOM   7673  O   LYS C 342      25.883 -12.687  41.198  1.00 41.05           O  
-ATOM   7674  CB  LYS C 342      28.238 -14.117  42.935  1.00 42.24           C  
-ATOM   7675  CG  LYS C 342      27.108 -13.863  43.924  1.00 46.38           C  
-ATOM   7676  CD  LYS C 342      27.576 -13.946  45.375  1.00 49.64           C  
-ATOM   7677  CE  LYS C 342      26.406 -13.759  46.343  1.00 50.42           C  
-ATOM   7678  NZ  LYS C 342      26.816 -13.910  47.771  1.00 51.62           N  
-ATOM   7679  N   LEU C 343      27.914 -11.808  40.785  1.00 41.87           N  
-ATOM   7680  CA  LEU C 343      27.388 -10.494  40.432  1.00 40.94           C  
-ATOM   7681  C   LEU C 343      26.530 -10.597  39.178  1.00 39.82           C  
-ATOM   7682  O   LEU C 343      25.378 -10.164  39.167  1.00 38.98           O  
-ATOM   7683  CB  LEU C 343      28.532  -9.504  40.184  1.00 40.80           C  
-ATOM   7684  CG  LEU C 343      28.152  -8.092  39.708  1.00 40.71           C  
-ATOM   7685  CD1 LEU C 343      27.313  -7.385  40.764  1.00 38.02           C  
-ATOM   7686  CD2 LEU C 343      29.419  -7.297  39.420  1.00 40.89           C  
-ATOM   7687  N   VAL C 344      27.101 -11.177  38.125  1.00 38.97           N  
-ATOM   7688  CA  VAL C 344      26.397 -11.331  36.859  1.00 39.67           C  
-ATOM   7689  C   VAL C 344      25.095 -12.098  37.027  1.00 40.84           C  
-ATOM   7690  O   VAL C 344      24.064 -11.722  36.469  1.00 41.39           O  
-ATOM   7691  CB  VAL C 344      27.255 -12.073  35.832  1.00 38.43           C  
-ATOM   7692  CG1 VAL C 344      26.500 -12.199  34.520  1.00 38.74           C  
-ATOM   7693  CG2 VAL C 344      28.558 -11.338  35.630  1.00 39.41           C  
-ATOM   7694  N   LYS C 345      25.147 -13.176  37.799  1.00 42.02           N  
-ATOM   7695  CA  LYS C 345      23.965 -13.991  38.030  1.00 42.81           C  
-ATOM   7696  C   LYS C 345      22.967 -13.275  38.936  1.00 42.39           C  
-ATOM   7697  O   LYS C 345      21.763 -13.506  38.846  1.00 41.73           O  
-ATOM   7698  CB  LYS C 345      24.376 -15.345  38.617  1.00 43.87           C  
-ATOM   7699  CG  LYS C 345      25.149 -16.198  37.616  1.00 44.25           C  
-ATOM   7700  CD  LYS C 345      25.614 -17.529  38.187  1.00 45.52           C  
-ATOM   7701  CE  LYS C 345      26.342 -18.337  37.111  1.00 46.22           C  
-ATOM   7702  NZ  LYS C 345      26.938 -19.602  37.628  1.00 47.84           N  
-ATOM   7703  N   MET C 346      23.471 -12.400  39.801  1.00 42.80           N  
-ATOM   7704  CA  MET C 346      22.610 -11.639  40.700  1.00 42.22           C  
-ATOM   7705  C   MET C 346      21.842 -10.611  39.872  1.00 42.45           C  
-ATOM   7706  O   MET C 346      20.651 -10.375  40.088  1.00 41.22           O  
-ATOM   7707  CB  MET C 346      23.446 -10.910  41.748  1.00 42.87           C  
-ATOM   7708  CG  MET C 346      22.637  -9.984  42.636  1.00 43.66           C  
-ATOM   7709  SD  MET C 346      23.599  -8.561  43.198  1.00 44.05           S  
-ATOM   7710  CE  MET C 346      24.501  -9.278  44.584  1.00 43.63           C  
-ATOM   7711  N   MET C 347      22.539 -10.000  38.922  1.00 41.28           N  
-ATOM   7712  CA  MET C 347      21.922  -9.007  38.060  1.00 40.42           C  
-ATOM   7713  C   MET C 347      20.941  -9.650  37.080  1.00 39.41           C  
-ATOM   7714  O   MET C 347      19.846  -9.133  36.865  1.00 37.26           O  
-ATOM   7715  CB  MET C 347      22.997  -8.219  37.297  1.00 37.80           C  
-ATOM   7716  CG  MET C 347      23.740  -7.198  38.159  1.00 36.16           C  
-ATOM   7717  SD  MET C 347      24.962  -6.240  37.230  1.00 36.33           S  
-ATOM   7718  CE  MET C 347      23.871  -5.222  36.211  1.00 36.57           C  
-ATOM   7719  N   VAL C 348      21.328 -10.777  36.491  1.00 40.70           N  
-ATOM   7720  CA  VAL C 348      20.453 -11.455  35.539  1.00 41.14           C  
-ATOM   7721  C   VAL C 348      19.165 -11.921  36.216  1.00 41.17           C  
-ATOM   7722  O   VAL C 348      18.078 -11.772  35.658  1.00 41.20           O  
-ATOM   7723  CB  VAL C 348      21.149 -12.665  34.884  1.00 41.25           C  
-ATOM   7724  CG1 VAL C 348      20.188 -13.365  33.940  1.00 42.33           C  
-ATOM   7725  CG2 VAL C 348      22.373 -12.206  34.119  1.00 40.50           C  
-ATOM   7726  N   ASP C 349      19.285 -12.471  37.419  1.00 40.42           N  
-ATOM   7727  CA  ASP C 349      18.111 -12.931  38.150  1.00 41.53           C  
-ATOM   7728  C   ASP C 349      17.104 -11.799  38.349  1.00 41.27           C  
-ATOM   7729  O   ASP C 349      15.910 -11.975  38.114  1.00 41.13           O  
-ATOM   7730  CB  ASP C 349      18.507 -13.487  39.522  1.00 42.24           C  
-ATOM   7731  CG  ASP C 349      19.108 -14.881  39.446  1.00 44.07           C  
-ATOM   7732  OD1 ASP C 349      19.178 -15.453  38.333  1.00 41.78           O  
-ATOM   7733  OD2 ASP C 349      19.506 -15.404  40.513  1.00 44.82           O  
-ATOM   7734  N   GLU C 350      17.592 -10.640  38.783  1.00 41.23           N  
-ATOM   7735  CA  GLU C 350      16.728  -9.486  39.031  1.00 41.80           C  
-ATOM   7736  C   GLU C 350      16.025  -9.003  37.775  1.00 40.28           C  
-ATOM   7737  O   GLU C 350      14.805  -8.854  37.755  1.00 39.24           O  
-ATOM   7738  CB  GLU C 350      17.533  -8.327  39.617  1.00 44.25           C  
-ATOM   7739  CG  GLU C 350      18.219  -8.656  40.916  1.00 49.41           C  
-ATOM   7740  CD  GLU C 350      17.246  -9.104  41.978  1.00 52.74           C  
-ATOM   7741  OE1 GLU C 350      16.390  -8.289  42.392  1.00 55.30           O  
-ATOM   7742  OE2 GLU C 350      17.337 -10.277  42.397  1.00 55.14           O  
-ATOM   7743  N   ASP C 351      16.803  -8.746  36.731  1.00 38.45           N  
-ATOM   7744  CA  ASP C 351      16.236  -8.270  35.486  1.00 39.50           C  
-ATOM   7745  C   ASP C 351      15.344  -9.301  34.816  1.00 40.18           C  
-ATOM   7746  O   ASP C 351      14.463  -8.937  34.041  1.00 40.80           O  
-ATOM   7747  CB  ASP C 351      17.344  -7.817  34.533  1.00 38.42           C  
-ATOM   7748  CG  ASP C 351      17.821  -6.400  34.832  1.00 39.45           C  
-ATOM   7749  OD1 ASP C 351      18.738  -5.912  34.131  1.00 39.72           O  
-ATOM   7750  OD2 ASP C 351      17.270  -5.774  35.766  1.00 37.90           O  
-ATOM   7751  N   LEU C 352      15.571 -10.583  35.107  1.00 40.34           N  
-ATOM   7752  CA  LEU C 352      14.742 -11.641  34.529  1.00 40.51           C  
-ATOM   7753  C   LEU C 352      13.384 -11.552  35.203  1.00 40.73           C  
-ATOM   7754  O   LEU C 352      12.345 -11.543  34.542  1.00 40.23           O  
-ATOM   7755  CB  LEU C 352      15.337 -13.027  34.786  1.00 40.60           C  
-ATOM   7756  CG  LEU C 352      14.479 -14.165  34.212  1.00 42.18           C  
-ATOM   7757  CD1 LEU C 352      14.429 -14.040  32.690  1.00 41.96           C  
-ATOM   7758  CD2 LEU C 352      15.049 -15.523  34.620  1.00 41.56           C  
-ATOM   7759  N   GLU C 353      13.406 -11.482  36.531  1.00 39.49           N  
-ATOM   7760  CA  GLU C 353      12.185 -11.369  37.307  1.00 40.31           C  
-ATOM   7761  C   GLU C 353      11.482 -10.068  36.941  1.00 39.80           C  
-ATOM   7762  O   GLU C 353      10.253  -9.988  36.954  1.00 40.56           O  
-ATOM   7763  CB  GLU C 353      12.505 -11.375  38.801  1.00 41.87           C  
-ATOM   7764  CG  GLU C 353      11.282 -11.271  39.692  1.00 45.79           C  
-ATOM   7765  CD  GLU C 353      10.268 -12.379  39.426  1.00 48.80           C  
-ATOM   7766  OE1 GLU C 353      10.670 -13.565  39.411  1.00 49.87           O  
-ATOM   7767  OE2 GLU C 353       9.072 -12.063  39.236  1.00 49.75           O  
-ATOM   7768  N   LEU C 354      12.271  -9.049  36.611  1.00 38.54           N  
-ATOM   7769  CA  LEU C 354      11.716  -7.755  36.244  1.00 37.29           C  
-ATOM   7770  C   LEU C 354      11.034  -7.885  34.893  1.00 36.90           C  
-ATOM   7771  O   LEU C 354       9.933  -7.378  34.691  1.00 35.69           O  
-ATOM   7772  CB  LEU C 354      12.820  -6.695  36.157  1.00 36.47           C  
-ATOM   7773  CG  LEU C 354      12.450  -5.273  36.598  1.00 37.60           C  
-ATOM   7774  CD1 LEU C 354      13.570  -4.322  36.194  1.00 37.35           C  
-ATOM   7775  CD2 LEU C 354      11.131  -4.831  35.966  1.00 37.19           C  
-ATOM   7776  N   ALA C 355      11.694  -8.570  33.966  1.00 36.31           N  
-ATOM   7777  CA  ALA C 355      11.140  -8.758  32.633  1.00 36.85           C  
-ATOM   7778  C   ALA C 355       9.860  -9.589  32.682  1.00 37.73           C  
-ATOM   7779  O   ALA C 355       8.918  -9.324  31.937  1.00 38.77           O  
-ATOM   7780  CB  ALA C 355      12.166  -9.427  31.732  1.00 35.22           C  
-ATOM   7781  N   LYS C 356       9.828 -10.587  33.563  1.00 38.80           N  
-ATOM   7782  CA  LYS C 356       8.661 -11.456  33.705  1.00 39.59           C  
-ATOM   7783  C   LYS C 356       7.456 -10.668  34.206  1.00 40.88           C  
-ATOM   7784  O   LYS C 356       6.351 -10.816  33.681  1.00 41.98           O  
-ATOM   7785  CB  LYS C 356       8.969 -12.609  34.664  1.00 37.96           C  
-ATOM   7786  N   ARG C 357       7.668  -9.837  35.224  1.00 41.69           N  
-ATOM   7787  CA  ARG C 357       6.586  -9.023  35.772  1.00 42.73           C  
-ATOM   7788  C   ARG C 357       6.064  -8.086  34.692  1.00 42.04           C  
-ATOM   7789  O   ARG C 357       4.865  -7.832  34.600  1.00 42.76           O  
-ATOM   7790  CB  ARG C 357       7.070  -8.205  36.969  1.00 42.35           C  
-ATOM   7791  CG  ARG C 357       7.511  -9.042  38.146  1.00 45.84           C  
-ATOM   7792  CD  ARG C 357       7.778  -8.171  39.360  1.00 50.18           C  
-ATOM   7793  NE  ARG C 357       8.309  -8.942  40.481  1.00 54.30           N  
-ATOM   7794  CZ  ARG C 357       8.513  -8.445  41.697  1.00 55.91           C  
-ATOM   7795  NH1 ARG C 357       8.226  -7.174  41.956  1.00 56.10           N  
-ATOM   7796  NH2 ARG C 357       9.013  -9.216  42.652  1.00 56.42           N  
-ATOM   7797  N   GLU C 358       6.974  -7.570  33.875  1.00 41.85           N  
-ATOM   7798  CA  GLU C 358       6.579  -6.682  32.797  1.00 41.80           C  
-ATOM   7799  C   GLU C 358       5.682  -7.449  31.846  1.00 40.90           C  
-ATOM   7800  O   GLU C 358       4.588  -6.993  31.512  1.00 41.42           O  
-ATOM   7801  CB  GLU C 358       7.801  -6.164  32.040  1.00 41.21           C  
-ATOM   7802  CG  GLU C 358       8.573  -5.097  32.787  1.00 45.59           C  
-ATOM   7803  CD  GLU C 358       9.738  -4.550  31.986  1.00 46.43           C  
-ATOM   7804  OE1 GLU C 358      10.360  -3.582  32.460  1.00 48.80           O  
-ATOM   7805  OE2 GLU C 358      10.032  -5.082  30.890  1.00 44.61           O  
-ATOM   7806  N   LYS C 359       6.150  -8.618  31.418  1.00 39.16           N  
-ATOM   7807  CA  LYS C 359       5.387  -9.451  30.502  1.00 38.47           C  
-ATOM   7808  C   LYS C 359       3.975  -9.654  31.040  1.00 37.10           C  
-ATOM   7809  O   LYS C 359       2.996  -9.552  30.295  1.00 35.88           O  
-ATOM   7810  CB  LYS C 359       6.068 -10.809  30.309  1.00 39.38           C  
-ATOM   7811  CG  LYS C 359       5.426 -11.646  29.212  1.00 39.61           C  
-ATOM   7812  CD  LYS C 359       6.075 -13.011  29.077  1.00 42.71           C  
-ATOM   7813  CE  LYS C 359       5.382 -13.842  27.999  1.00 42.59           C  
-ATOM   7814  NZ  LYS C 359       6.022 -15.181  27.821  1.00 43.96           N  
-ATOM   7815  N   VAL C 360       3.873  -9.938  32.336  1.00 35.51           N  
-ATOM   7816  CA  VAL C 360       2.575 -10.136  32.963  1.00 34.72           C  
-ATOM   7817  C   VAL C 360       1.718  -8.874  32.841  1.00 35.53           C  
-ATOM   7818  O   VAL C 360       0.544  -8.951  32.483  1.00 34.70           O  
-ATOM   7819  CB  VAL C 360       2.716 -10.510  34.462  1.00 35.13           C  
-ATOM   7820  CG1 VAL C 360       1.345 -10.480  35.145  1.00 35.43           C  
-ATOM   7821  CG2 VAL C 360       3.322 -11.903  34.595  1.00 34.97           C  
-ATOM   7822  N   LEU C 361       2.305  -7.714  33.129  1.00 35.69           N  
-ATOM   7823  CA  LEU C 361       1.564  -6.459  33.047  1.00 35.50           C  
-ATOM   7824  C   LEU C 361       1.187  -6.118  31.612  1.00 36.20           C  
-ATOM   7825  O   LEU C 361       0.125  -5.550  31.365  1.00 37.29           O  
-ATOM   7826  CB  LEU C 361       2.371  -5.314  33.660  1.00 34.14           C  
-ATOM   7827  CG  LEU C 361       2.677  -5.442  35.153  1.00 34.49           C  
-ATOM   7828  CD1 LEU C 361       3.411  -4.189  35.627  1.00 33.12           C  
-ATOM   7829  CD2 LEU C 361       1.382  -5.637  35.934  1.00 33.10           C  
-ATOM   7830  N   VAL C 362       2.056  -6.457  30.666  1.00 36.52           N  
-ATOM   7831  CA  VAL C 362       1.769  -6.193  29.263  1.00 36.86           C  
-ATOM   7832  C   VAL C 362       0.661  -7.138  28.799  1.00 38.42           C  
-ATOM   7833  O   VAL C 362      -0.287  -6.721  28.129  1.00 37.65           O  
-ATOM   7834  CB  VAL C 362       3.005  -6.432  28.381  1.00 38.08           C  
-ATOM   7835  CG1 VAL C 362       2.680  -6.092  26.930  1.00 38.07           C  
-ATOM   7836  CG2 VAL C 362       4.173  -5.598  28.886  1.00 38.07           C  
-ATOM   7837  N   ASP C 363       0.789  -8.413  29.164  1.00 37.37           N  
-ATOM   7838  CA  ASP C 363      -0.193  -9.424  28.788  1.00 36.99           C  
-ATOM   7839  C   ASP C 363      -1.564  -9.113  29.374  1.00 36.62           C  
-ATOM   7840  O   ASP C 363      -2.586  -9.363  28.742  1.00 37.25           O  
-ATOM   7841  CB  ASP C 363       0.269 -10.810  29.254  1.00 36.40           C  
-ATOM   7842  CG  ASP C 363       1.333 -11.411  28.349  1.00 37.21           C  
-ATOM   7843  OD1 ASP C 363       1.982 -12.398  28.760  1.00 35.12           O  
-ATOM   7844  OD2 ASP C 363       1.512 -10.905  27.221  1.00 38.21           O  
-ATOM   7845  N   ALA C 364      -1.580  -8.560  30.582  1.00 36.63           N  
-ATOM   7846  CA  ALA C 364      -2.827  -8.222  31.255  1.00 36.62           C  
-ATOM   7847  C   ALA C 364      -3.377  -6.852  30.851  1.00 37.19           C  
-ATOM   7848  O   ALA C 364      -4.404  -6.414  31.369  1.00 36.98           O  
-ATOM   7849  CB  ALA C 364      -2.626  -8.278  32.761  1.00 35.54           C  
-ATOM   7850  N   GLY C 365      -2.692  -6.176  29.935  1.00 38.04           N  
-ATOM   7851  CA  GLY C 365      -3.149  -4.870  29.488  1.00 38.34           C  
-ATOM   7852  C   GLY C 365      -2.889  -3.747  30.475  1.00 39.33           C  
-ATOM   7853  O   GLY C 365      -3.650  -2.783  30.538  1.00 37.90           O  
-ATOM   7854  N   TYR C 366      -1.814  -3.866  31.247  1.00 41.09           N  
-ATOM   7855  CA  TYR C 366      -1.458  -2.844  32.223  1.00 42.92           C  
-ATOM   7856  C   TYR C 366      -0.317  -1.960  31.737  1.00 45.97           C  
-ATOM   7857  O   TYR C 366      -0.103  -0.874  32.269  1.00 49.03           O  
-ATOM   7858  CB  TYR C 366      -1.079  -3.484  33.555  1.00 41.61           C  
-ATOM   7859  CG  TYR C 366      -2.263  -3.809  34.430  1.00 41.35           C  
-ATOM   7860  CD1 TYR C 366      -3.303  -4.608  33.962  1.00 41.49           C  
-ATOM   7861  CD2 TYR C 366      -2.339  -3.324  35.734  1.00 41.97           C  
-ATOM   7862  CE1 TYR C 366      -4.394  -4.920  34.772  1.00 42.18           C  
-ATOM   7863  CE2 TYR C 366      -3.423  -3.626  36.554  1.00 42.75           C  
-ATOM   7864  CZ  TYR C 366      -4.446  -4.426  36.068  1.00 42.73           C  
-ATOM   7865  OH  TYR C 366      -5.516  -4.738  36.879  1.00 43.37           O  
-ATOM   7866  N   MET C 367       0.421  -2.432  30.737  1.00 47.99           N  
-ATOM   7867  CA  MET C 367       1.526  -1.663  30.176  1.00 49.89           C  
-ATOM   7868  C   MET C 367       1.409  -1.670  28.661  1.00 50.52           C  
-ATOM   7869  O   MET C 367       0.657  -2.525  28.148  1.00 51.22           O  
-ATOM   7870  CB  MET C 367       2.879  -2.262  30.580  1.00 51.43           C  
-ATOM   7871  CG  MET C 367       3.209  -2.178  32.063  1.00 53.25           C  
-ATOM   7872  SD  MET C 367       4.925  -2.655  32.417  1.00 55.96           S  
-ATOM   7873  CE  MET C 367       5.674  -1.046  32.693  1.00 56.79           C  
-TER    7874      MET C 367                                                      
-ATOM   7875  N   ARG D  28      46.720  35.326   3.999  1.00 44.00           N  
-ATOM   7876  CA  ARG D  28      47.191  35.857   5.319  1.00 45.37           C  
-ATOM   7877  C   ARG D  28      46.650  35.032   6.487  1.00 43.73           C  
-ATOM   7878  O   ARG D  28      45.440  34.954   6.690  1.00 43.65           O  
-ATOM   7879  CB  ARG D  28      46.765  37.319   5.471  1.00 44.40           C  
-ATOM   7880  CG  ARG D  28      47.000  37.906   6.855  1.00 46.54           C  
-ATOM   7881  CD  ARG D  28      47.073  39.426   6.796  1.00 46.90           C  
-ATOM   7882  NE  ARG D  28      48.413  39.894   6.444  1.00 48.71           N  
-ATOM   7883  CZ  ARG D  28      48.710  41.146   6.104  1.00 48.68           C  
-ATOM   7884  NH1 ARG D  28      47.758  42.068   6.058  1.00 49.48           N  
-ATOM   7885  NH2 ARG D  28      49.963  41.481   5.824  1.00 47.50           N  
-ATOM   7886  N   LYS D  29      47.554  34.413   7.244  1.00 43.19           N  
-ATOM   7887  CA  LYS D  29      47.164  33.591   8.385  1.00 41.49           C  
-ATOM   7888  C   LYS D  29      46.495  34.409   9.481  1.00 39.32           C  
-ATOM   7889  O   LYS D  29      46.933  35.506   9.822  1.00 36.20           O  
-ATOM   7890  CB  LYS D  29      48.375  32.841   8.953  1.00 42.88           C  
-ATOM   7891  CG  LYS D  29      48.760  31.606   8.146  1.00 47.19           C  
-ATOM   7892  CD  LYS D  29      49.848  30.776   8.832  1.00 49.87           C  
-ATOM   7893  CE  LYS D  29      50.143  29.497   8.038  1.00 53.01           C  
-ATOM   7894  NZ  LYS D  29      51.159  28.604   8.678  1.00 51.72           N  
-ATOM   7895  N   ILE D  30      45.421  33.858  10.029  1.00 38.39           N  
-ATOM   7896  CA  ILE D  30      44.666  34.532  11.070  1.00 38.12           C  
-ATOM   7897  C   ILE D  30      44.834  33.831  12.409  1.00 37.05           C  
-ATOM   7898  O   ILE D  30      44.658  32.615  12.513  1.00 36.50           O  
-ATOM   7899  CB  ILE D  30      43.174  34.585  10.696  1.00 36.87           C  
-ATOM   7900  CG1 ILE D  30      43.020  35.304   9.351  1.00 37.52           C  
-ATOM   7901  CG2 ILE D  30      42.378  35.294  11.785  1.00 36.79           C  
-ATOM   7902  CD1 ILE D  30      41.593  35.405   8.862  1.00 35.67           C  
-ATOM   7903  N   ALA D  31      45.193  34.607  13.428  1.00 36.38           N  
-ATOM   7904  CA  ALA D  31      45.382  34.069  14.768  1.00 34.70           C  
-ATOM   7905  C   ALA D  31      44.419  34.722  15.756  1.00 34.28           C  
-ATOM   7906  O   ALA D  31      44.153  35.928  15.685  1.00 33.37           O  
-ATOM   7907  CB  ALA D  31      46.815  34.284  15.223  1.00 34.32           C  
-ATOM   7908  N   LEU D  32      43.893  33.907  16.667  1.00 32.59           N  
-ATOM   7909  CA  LEU D  32      42.973  34.376  17.697  1.00 31.12           C  
-ATOM   7910  C   LEU D  32      43.645  34.119  19.036  1.00 28.45           C  
-ATOM   7911  O   LEU D  32      44.034  32.994  19.341  1.00 28.65           O  
-ATOM   7912  CB  LEU D  32      41.640  33.621  17.620  1.00 30.73           C  
-ATOM   7913  CG  LEU D  32      40.618  33.892  18.730  1.00 31.29           C  
-ATOM   7914  CD1 LEU D  32      40.417  35.390  18.913  1.00 33.09           C  
-ATOM   7915  CD2 LEU D  32      39.305  33.212  18.379  1.00 32.03           C  
-ATOM   7916  N   ILE D  33      43.783  35.169  19.831  1.00 28.46           N  
-ATOM   7917  CA  ILE D  33      44.440  35.057  21.123  1.00 27.45           C  
-ATOM   7918  C   ILE D  33      43.538  35.411  22.292  1.00 27.41           C  
-ATOM   7919  O   ILE D  33      43.001  36.514  22.334  1.00 30.58           O  
-ATOM   7920  CB  ILE D  33      45.654  36.010  21.212  1.00 26.64           C  
-ATOM   7921  CG1 ILE D  33      46.621  35.759  20.056  1.00 23.04           C  
-ATOM   7922  CG2 ILE D  33      46.356  35.831  22.551  1.00 24.37           C  
-ATOM   7923  CD1 ILE D  33      47.780  36.731  20.038  1.00 21.15           C  
-ATOM   7924  N   THR D  34      43.362  34.484  23.234  1.00 28.36           N  
-ATOM   7925  CA  THR D  34      42.579  34.794  24.424  1.00 26.29           C  
-ATOM   7926  C   THR D  34      43.645  35.250  25.415  1.00 27.24           C  
-ATOM   7927  O   THR D  34      44.774  34.748  25.389  1.00 23.76           O  
-ATOM   7928  CB  THR D  34      41.828  33.573  25.025  1.00 26.64           C  
-ATOM   7929  OG1 THR D  34      42.773  32.621  25.523  1.00 26.45           O  
-ATOM   7930  CG2 THR D  34      40.920  32.926  23.985  1.00 26.81           C  
-ATOM   7931  N   GLY D  35      43.294  36.211  26.266  1.00 27.17           N  
-ATOM   7932  CA  GLY D  35      44.242  36.728  27.238  1.00 27.44           C  
-ATOM   7933  C   GLY D  35      45.314  37.557  26.558  1.00 28.79           C  
-ATOM   7934  O   GLY D  35      46.480  37.561  26.973  1.00 27.62           O  
-ATOM   7935  N   ILE D  36      44.914  38.270  25.510  1.00 28.55           N  
-ATOM   7936  CA  ILE D  36      45.840  39.096  24.749  1.00 28.68           C  
-ATOM   7937  C   ILE D  36      46.347  40.312  25.519  1.00 29.19           C  
-ATOM   7938  O   ILE D  36      47.415  40.834  25.211  1.00 31.28           O  
-ATOM   7939  CB  ILE D  36      45.196  39.565  23.407  1.00 28.08           C  
-ATOM   7940  CG1 ILE D  36      46.273  40.165  22.496  1.00 26.89           C  
-ATOM   7941  CG2 ILE D  36      44.085  40.579  23.676  1.00 25.40           C  
-ATOM   7942  CD1 ILE D  36      45.803  40.463  21.084  1.00 24.20           C  
-ATOM   7943  N   THR D  37      45.600  40.755  26.526  1.00 29.67           N  
-ATOM   7944  CA  THR D  37      46.007  41.923  27.307  1.00 29.27           C  
-ATOM   7945  C   THR D  37      47.046  41.598  28.382  1.00 29.21           C  
-ATOM   7946  O   THR D  37      47.576  42.500  29.042  1.00 28.26           O  
-ATOM   7947  CB  THR D  37      44.795  42.591  27.992  1.00 30.47           C  
-ATOM   7948  OG1 THR D  37      44.119  41.633  28.817  1.00 32.09           O  
-ATOM   7949  CG2 THR D  37      43.833  43.136  26.955  1.00 30.34           C  
-ATOM   7950  N   GLY D  38      47.332  40.311  28.555  1.00 28.84           N  
-ATOM   7951  CA  GLY D  38      48.303  39.891  29.550  1.00 26.36           C  
-ATOM   7952  C   GLY D  38      49.726  39.949  29.034  1.00 26.45           C  
-ATOM   7953  O   GLY D  38      49.956  40.355  27.898  1.00 27.87           O  
-ATOM   7954  N   GLN D  39      50.681  39.538  29.863  1.00 25.60           N  
-ATOM   7955  CA  GLN D  39      52.093  39.550  29.482  1.00 27.19           C  
-ATOM   7956  C   GLN D  39      52.373  38.785  28.188  1.00 27.78           C  
-ATOM   7957  O   GLN D  39      52.866  39.357  27.217  1.00 26.99           O  
-ATOM   7958  CB  GLN D  39      52.963  38.970  30.606  1.00 25.47           C  
-ATOM   7959  CG  GLN D  39      54.438  38.869  30.243  1.00 25.05           C  
-ATOM   7960  CD  GLN D  39      55.244  38.071  31.257  1.00 27.02           C  
-ATOM   7961  OE1 GLN D  39      56.184  38.584  31.860  1.00 30.46           O  
-ATOM   7962  NE2 GLN D  39      54.880  36.809  31.443  1.00 25.67           N  
-ATOM   7963  N   ASP D  40      52.070  37.490  28.184  1.00 27.36           N  
-ATOM   7964  CA  ASP D  40      52.308  36.664  27.005  1.00 28.82           C  
-ATOM   7965  C   ASP D  40      51.541  37.142  25.787  1.00 28.31           C  
-ATOM   7966  O   ASP D  40      52.088  37.196  24.685  1.00 29.26           O  
-ATOM   7967  CB  ASP D  40      51.961  35.207  27.307  1.00 28.68           C  
-ATOM   7968  CG  ASP D  40      52.953  34.569  28.244  1.00 29.88           C  
-ATOM   7969  OD1 ASP D  40      53.799  35.309  28.784  1.00 31.83           O  
-ATOM   7970  OD2 ASP D  40      52.891  33.338  28.447  1.00 32.92           O  
-ATOM   7971  N   GLY D  41      50.276  37.490  25.992  1.00 29.76           N  
-ATOM   7972  CA  GLY D  41      49.450  37.969  24.901  1.00 29.63           C  
-ATOM   7973  C   GLY D  41      50.076  39.160  24.197  1.00 31.62           C  
-ATOM   7974  O   GLY D  41      50.089  39.218  22.966  1.00 30.42           O  
-ATOM   7975  N   SER D  42      50.606  40.106  24.972  1.00 30.29           N  
-ATOM   7976  CA  SER D  42      51.225  41.297  24.399  1.00 29.44           C  
-ATOM   7977  C   SER D  42      52.420  40.954  23.508  1.00 29.15           C  
-ATOM   7978  O   SER D  42      52.555  41.500  22.415  1.00 30.20           O  
-ATOM   7979  CB  SER D  42      51.651  42.271  25.505  1.00 28.17           C  
-ATOM   7980  OG  SER D  42      52.686  41.739  26.307  1.00 29.00           O  
-ATOM   7981  N   TYR D  43      53.281  40.049  23.963  1.00 29.61           N  
-ATOM   7982  CA  TYR D  43      54.438  39.654  23.165  1.00 29.68           C  
-ATOM   7983  C   TYR D  43      54.065  38.764  21.977  1.00 30.51           C  
-ATOM   7984  O   TYR D  43      54.599  38.933  20.879  1.00 31.81           O  
-ATOM   7985  CB  TYR D  43      55.477  38.933  24.027  1.00 28.40           C  
-ATOM   7986  CG  TYR D  43      56.255  39.852  24.937  1.00 28.60           C  
-ATOM   7987  CD1 TYR D  43      55.920  39.978  26.285  1.00 28.22           C  
-ATOM   7988  CD2 TYR D  43      57.313  40.618  24.443  1.00 29.31           C  
-ATOM   7989  CE1 TYR D  43      56.618  40.847  27.122  1.00 30.14           C  
-ATOM   7990  CE2 TYR D  43      58.020  41.493  25.271  1.00 30.14           C  
-ATOM   7991  CZ  TYR D  43      57.665  41.601  26.609  1.00 32.24           C  
-ATOM   7992  OH  TYR D  43      58.344  42.470  27.429  1.00 33.13           O  
-ATOM   7993  N   LEU D  44      53.163  37.811  22.195  1.00 28.87           N  
-ATOM   7994  CA  LEU D  44      52.744  36.914  21.124  1.00 28.79           C  
-ATOM   7995  C   LEU D  44      52.114  37.718  19.994  1.00 29.68           C  
-ATOM   7996  O   LEU D  44      52.249  37.372  18.822  1.00 30.02           O  
-ATOM   7997  CB  LEU D  44      51.734  35.882  21.640  1.00 28.40           C  
-ATOM   7998  CG  LEU D  44      51.168  34.934  20.575  1.00 25.73           C  
-ATOM   7999  CD1 LEU D  44      52.306  34.165  19.937  1.00 27.66           C  
-ATOM   8000  CD2 LEU D  44      50.164  33.971  21.199  1.00 28.40           C  
-ATOM   8001  N   THR D  45      51.418  38.788  20.361  1.00 30.57           N  
-ATOM   8002  CA  THR D  45      50.773  39.657  19.391  1.00 31.06           C  
-ATOM   8003  C   THR D  45      51.833  40.282  18.489  1.00 31.46           C  
-ATOM   8004  O   THR D  45      51.734  40.216  17.267  1.00 31.21           O  
-ATOM   8005  CB  THR D  45      49.976  40.771  20.094  1.00 31.59           C  
-ATOM   8006  OG1 THR D  45      48.858  40.191  20.776  1.00 33.17           O  
-ATOM   8007  CG2 THR D  45      49.473  41.801  19.087  1.00 30.80           C  
-ATOM   8008  N   GLU D  46      52.850  40.882  19.097  1.00 31.62           N  
-ATOM   8009  CA  GLU D  46      53.925  41.501  18.332  1.00 33.13           C  
-ATOM   8010  C   GLU D  46      54.632  40.453  17.473  1.00 33.85           C  
-ATOM   8011  O   GLU D  46      54.910  40.691  16.301  1.00 35.97           O  
-ATOM   8012  CB  GLU D  46      54.931  42.176  19.272  1.00 32.81           C  
-ATOM   8013  CG  GLU D  46      54.313  43.257  20.151  1.00 37.79           C  
-ATOM   8014  CD  GLU D  46      55.297  43.867  21.134  1.00 38.75           C  
-ATOM   8015  OE1 GLU D  46      55.943  43.113  21.889  1.00 38.61           O  
-ATOM   8016  OE2 GLU D  46      55.420  45.110  21.155  1.00 43.58           O  
-ATOM   8017  N   PHE D  47      54.910  39.289  18.052  1.00 32.69           N  
-ATOM   8018  CA  PHE D  47      55.585  38.228  17.316  1.00 33.50           C  
-ATOM   8019  C   PHE D  47      54.825  37.829  16.054  1.00 35.21           C  
-ATOM   8020  O   PHE D  47      55.390  37.815  14.958  1.00 36.22           O  
-ATOM   8021  CB  PHE D  47      55.763  36.989  18.190  1.00 31.68           C  
-ATOM   8022  CG  PHE D  47      56.594  35.915  17.545  1.00 32.23           C  
-ATOM   8023  CD1 PHE D  47      57.973  36.059  17.429  1.00 31.33           C  
-ATOM   8024  CD2 PHE D  47      55.997  34.766  17.036  1.00 33.13           C  
-ATOM   8025  CE1 PHE D  47      58.744  35.076  16.819  1.00 32.24           C  
-ATOM   8026  CE2 PHE D  47      56.764  33.776  16.422  1.00 33.37           C  
-ATOM   8027  CZ  PHE D  47      58.140  33.933  16.315  1.00 31.66           C  
-ATOM   8028  N   LEU D  48      53.546  37.496  16.212  1.00 33.72           N  
-ATOM   8029  CA  LEU D  48      52.723  37.088  15.081  1.00 34.51           C  
-ATOM   8030  C   LEU D  48      52.590  38.184  14.022  1.00 35.15           C  
-ATOM   8031  O   LEU D  48      52.569  37.891  12.826  1.00 35.26           O  
-ATOM   8032  CB  LEU D  48      51.339  36.643  15.566  1.00 31.54           C  
-ATOM   8033  CG  LEU D  48      51.336  35.424  16.494  1.00 31.52           C  
-ATOM   8034  CD1 LEU D  48      49.905  35.090  16.880  1.00 33.33           C  
-ATOM   8035  CD2 LEU D  48      51.989  34.233  15.808  1.00 31.19           C  
-ATOM   8036  N   LEU D  49      52.500  39.439  14.453  1.00 36.22           N  
-ATOM   8037  CA  LEU D  49      52.397  40.549  13.510  1.00 38.08           C  
-ATOM   8038  C   LEU D  49      53.657  40.580  12.643  1.00 39.16           C  
-ATOM   8039  O   LEU D  49      53.580  40.702  11.419  1.00 39.27           O  
-ATOM   8040  CB  LEU D  49      52.241  41.879  14.252  1.00 36.53           C  
-ATOM   8041  CG  LEU D  49      50.876  42.123  14.897  1.00 37.22           C  
-ATOM   8042  CD1 LEU D  49      50.940  43.350  15.787  1.00 35.92           C  
-ATOM   8043  CD2 LEU D  49      49.816  42.287  13.812  1.00 35.18           C  
-ATOM   8044  N   GLY D  50      54.815  40.455  13.285  1.00 39.30           N  
-ATOM   8045  CA  GLY D  50      56.067  40.459  12.552  1.00 39.18           C  
-ATOM   8046  C   GLY D  50      56.111  39.308  11.565  1.00 40.45           C  
-ATOM   8047  O   GLY D  50      56.897  39.318  10.620  1.00 40.90           O  
-ATOM   8048  N   LYS D  51      55.261  38.311  11.792  1.00 40.11           N  
-ATOM   8049  CA  LYS D  51      55.178  37.139  10.929  1.00 40.20           C  
-ATOM   8050  C   LYS D  51      54.126  37.337   9.837  1.00 41.36           C  
-ATOM   8051  O   LYS D  51      53.817  36.409   9.086  1.00 40.69           O  
-ATOM   8052  CB  LYS D  51      54.815  35.905  11.754  1.00 40.90           C  
-ATOM   8053  CG  LYS D  51      55.917  35.403  12.666  1.00 40.42           C  
-ATOM   8054  CD  LYS D  51      56.954  34.639  11.880  1.00 40.36           C  
-ATOM   8055  CE  LYS D  51      58.030  34.078  12.783  1.00 39.22           C  
-ATOM   8056  NZ  LYS D  51      58.985  33.254  12.003  1.00 39.97           N  
-ATOM   8057  N   GLY D  52      53.565  38.542   9.768  1.00 41.70           N  
-ATOM   8058  CA  GLY D  52      52.562  38.843   8.760  1.00 41.88           C  
-ATOM   8059  C   GLY D  52      51.165  38.357   9.095  1.00 42.89           C  
-ATOM   8060  O   GLY D  52      50.252  38.455   8.267  1.00 43.06           O  
-ATOM   8061  N   TYR D  53      50.993  37.835  10.307  1.00 42.10           N  
-ATOM   8062  CA  TYR D  53      49.697  37.329  10.758  1.00 40.34           C  
-ATOM   8063  C   TYR D  53      48.661  38.420  10.955  1.00 39.40           C  
-ATOM   8064  O   TYR D  53      48.991  39.588  11.158  1.00 37.40           O  
-ATOM   8065  CB  TYR D  53      49.822  36.617  12.108  1.00 39.13           C  
-ATOM   8066  CG  TYR D  53      50.180  35.153  12.083  1.00 36.09           C  
-ATOM   8067  CD1 TYR D  53      51.471  34.731  11.782  1.00 36.14           C  
-ATOM   8068  CD2 TYR D  53      49.239  34.191  12.438  1.00 34.65           C  
-ATOM   8069  CE1 TYR D  53      51.819  33.382  11.844  1.00 36.25           C  
-ATOM   8070  CE2 TYR D  53      49.572  32.845  12.503  1.00 36.08           C  
-ATOM   8071  CZ  TYR D  53      50.863  32.446  12.208  1.00 35.54           C  
-ATOM   8072  OH  TYR D  53      51.192  31.114  12.292  1.00 35.46           O  
-ATOM   8073  N   GLU D  54      47.398  38.012  10.898  1.00 40.13           N  
-ATOM   8074  CA  GLU D  54      46.281  38.906  11.161  1.00 38.92           C  
-ATOM   8075  C   GLU D  54      45.929  38.461  12.576  1.00 37.52           C  
-ATOM   8076  O   GLU D  54      45.602  37.292  12.799  1.00 35.72           O  
-ATOM   8077  CB  GLU D  54      45.112  38.631  10.220  1.00 41.16           C  
-ATOM   8078  CG  GLU D  54      43.887  39.465  10.541  1.00 44.95           C  
-ATOM   8079  CD  GLU D  54      42.744  39.223   9.579  1.00 49.21           C  
-ATOM   8080  OE1 GLU D  54      41.626  39.705   9.862  1.00 49.43           O  
-ATOM   8081  OE2 GLU D  54      42.963  38.557   8.541  1.00 51.99           O  
-ATOM   8082  N   VAL D  55      46.013  39.377  13.533  1.00 36.26           N  
-ATOM   8083  CA  VAL D  55      45.759  39.019  14.921  1.00 34.31           C  
-ATOM   8084  C   VAL D  55      44.481  39.548  15.547  1.00 33.63           C  
-ATOM   8085  O   VAL D  55      44.213  40.746  15.543  1.00 31.70           O  
-ATOM   8086  CB  VAL D  55      46.945  39.446  15.809  1.00 34.67           C  
-ATOM   8087  CG1 VAL D  55      46.680  39.067  17.262  1.00 31.45           C  
-ATOM   8088  CG2 VAL D  55      48.225  38.794  15.301  1.00 33.28           C  
-ATOM   8089  N   HIS D  56      43.705  38.624  16.099  1.00 33.88           N  
-ATOM   8090  CA  HIS D  56      42.460  38.949  16.777  1.00 33.60           C  
-ATOM   8091  C   HIS D  56      42.599  38.506  18.223  1.00 33.07           C  
-ATOM   8092  O   HIS D  56      43.011  37.379  18.492  1.00 34.82           O  
-ATOM   8093  CB  HIS D  56      41.295  38.212  16.122  1.00 34.67           C  
-ATOM   8094  CG  HIS D  56      40.887  38.784  14.802  1.00 35.85           C  
-ATOM   8095  ND1 HIS D  56      39.890  39.727  14.677  1.00 36.32           N  
-ATOM   8096  CD2 HIS D  56      41.368  38.576  13.554  1.00 36.22           C  
-ATOM   8097  CE1 HIS D  56      39.773  40.076  13.408  1.00 36.92           C  
-ATOM   8098  NE2 HIS D  56      40.659  39.392  12.706  1.00 37.45           N  
-ATOM   8099  N   GLY D  57      42.273  39.399  19.150  1.00 32.29           N  
-ATOM   8100  CA  GLY D  57      42.362  39.061  20.559  1.00 30.29           C  
-ATOM   8101  C   GLY D  57      41.055  39.276  21.301  1.00 29.37           C  
-ATOM   8102  O   GLY D  57      40.295  40.201  21.003  1.00 28.96           O  
-ATOM   8103  N   LEU D  58      40.778  38.412  22.268  1.00 29.09           N  
-ATOM   8104  CA  LEU D  58      39.562  38.545  23.057  1.00 28.39           C  
-ATOM   8105  C   LEU D  58      39.905  39.283  24.345  1.00 28.13           C  
-ATOM   8106  O   LEU D  58      40.888  38.957  25.009  1.00 29.13           O  
-ATOM   8107  CB  LEU D  58      38.981  37.170  23.371  1.00 27.68           C  
-ATOM   8108  CG  LEU D  58      38.623  36.322  22.149  1.00 27.77           C  
-ATOM   8109  CD1 LEU D  58      37.901  35.067  22.612  1.00 28.00           C  
-ATOM   8110  CD2 LEU D  58      37.740  37.122  21.195  1.00 25.12           C  
-ATOM   8111  N   ILE D  59      39.109  40.286  24.690  1.00 27.80           N  
-ATOM   8112  CA  ILE D  59      39.367  41.057  25.899  1.00 29.09           C  
-ATOM   8113  C   ILE D  59      38.151  41.145  26.804  1.00 28.06           C  
-ATOM   8114  O   ILE D  59      37.014  41.046  26.353  1.00 28.35           O  
-ATOM   8115  CB  ILE D  59      39.819  42.506  25.576  1.00 28.95           C  
-ATOM   8116  CG1 ILE D  59      38.723  43.237  24.802  1.00 29.87           C  
-ATOM   8117  CG2 ILE D  59      41.103  42.494  24.768  1.00 29.84           C  
-ATOM   8118  CD1 ILE D  59      38.932  44.742  24.727  1.00 30.01           C  
-ATOM   8119  N   ARG D  60      38.404  41.323  28.093  1.00 27.87           N  
-ATOM   8120  CA  ARG D  60      37.332  41.453  29.063  1.00 27.09           C  
-ATOM   8121  C   ARG D  60      36.963  42.917  29.218  1.00 26.97           C  
-ATOM   8122  O   ARG D  60      37.830  43.786  29.171  1.00 26.83           O  
-ATOM   8123  CB  ARG D  60      37.770  40.953  30.434  1.00 27.77           C  
-ATOM   8124  CG  ARG D  60      37.820  39.471  30.609  1.00 27.56           C  
-ATOM   8125  CD  ARG D  60      37.793  39.158  32.092  1.00 28.18           C  
-ATOM   8126  NE  ARG D  60      38.924  39.755  32.794  1.00 28.14           N  
-ATOM   8127  CZ  ARG D  60      39.135  39.639  34.101  1.00 27.29           C  
-ATOM   8128  NH1 ARG D  60      38.282  38.953  34.851  1.00 26.54           N  
-ATOM   8129  NH2 ARG D  60      40.212  40.184  34.652  1.00 24.60           N  
-ATOM   8130  N   ARG D  61      35.680  43.196  29.400  1.00 26.94           N  
-ATOM   8131  CA  ARG D  61      35.268  44.571  29.625  1.00 26.89           C  
-ATOM   8132  C   ARG D  61      35.660  44.880  31.072  1.00 27.23           C  
-ATOM   8133  O   ARG D  61      35.604  44.003  31.933  1.00 26.20           O  
-ATOM   8134  CB  ARG D  61      33.755  44.714  29.466  1.00 26.69           C  
-ATOM   8135  CG  ARG D  61      33.259  46.146  29.604  1.00 26.94           C  
-ATOM   8136  CD  ARG D  61      33.042  46.554  31.052  1.00 26.17           C  
-ATOM   8137  NE  ARG D  61      32.837  47.993  31.156  1.00 28.90           N  
-ATOM   8138  CZ  ARG D  61      32.410  48.624  32.246  1.00 30.22           C  
-ATOM   8139  NH1 ARG D  61      32.128  47.944  33.352  1.00 28.71           N  
-ATOM   8140  NH2 ARG D  61      32.271  49.946  32.228  1.00 29.69           N  
-ATOM   8141  N   SER D  62      36.075  46.111  31.339  1.00 27.34           N  
-ATOM   8142  CA  SER D  62      36.440  46.494  32.698  1.00 29.29           C  
-ATOM   8143  C   SER D  62      36.128  47.969  32.887  1.00 28.80           C  
-ATOM   8144  O   SER D  62      36.052  48.714  31.906  1.00 26.73           O  
-ATOM   8145  CB  SER D  62      37.921  46.221  32.960  1.00 29.62           C  
-ATOM   8146  OG  SER D  62      38.731  46.976  32.091  1.00 33.12           O  
-ATOM   8147  N   SER D  63      35.945  48.390  34.137  1.00 28.03           N  
-ATOM   8148  CA  SER D  63      35.609  49.782  34.411  1.00 29.27           C  
-ATOM   8149  C   SER D  63      36.772  50.737  34.165  1.00 31.50           C  
-ATOM   8150  O   SER D  63      36.575  51.945  34.062  1.00 31.99           O  
-ATOM   8151  CB  SER D  63      35.082  49.942  35.844  1.00 26.81           C  
-ATOM   8152  OG  SER D  63      36.096  49.746  36.808  1.00 27.04           O  
-ATOM   8153  N   ASN D  64      37.980  50.192  34.057  1.00 34.41           N  
-ATOM   8154  CA  ASN D  64      39.170  51.003  33.801  1.00 36.05           C  
-ATOM   8155  C   ASN D  64      39.918  50.541  32.561  1.00 37.54           C  
-ATOM   8156  O   ASN D  64      39.649  49.472  32.014  1.00 38.92           O  
-ATOM   8157  CB  ASN D  64      40.139  50.946  34.990  1.00 34.95           C  
-ATOM   8158  CG  ASN D  64      39.744  51.876  36.111  1.00 34.69           C  
-ATOM   8159  OD1 ASN D  64      39.628  53.089  35.913  1.00 36.49           O  
-ATOM   8160  ND2 ASN D  64      39.541  51.318  37.300  1.00 32.33           N  
-ATOM   8161  N   PHE D  65      40.862  51.366  32.129  1.00 39.13           N  
-ATOM   8162  CA  PHE D  65      41.705  51.067  30.983  1.00 40.80           C  
-ATOM   8163  C   PHE D  65      42.300  49.697  31.303  1.00 40.89           C  
-ATOM   8164  O   PHE D  65      42.657  49.434  32.454  1.00 41.29           O  
-ATOM   8165  CB  PHE D  65      42.811  52.124  30.900  1.00 43.31           C  
-ATOM   8166  CG  PHE D  65      43.626  52.071  29.642  1.00 45.79           C  
-ATOM   8167  CD1 PHE D  65      45.018  52.104  29.703  1.00 46.43           C  
-ATOM   8168  CD2 PHE D  65      43.011  52.031  28.396  1.00 46.72           C  
-ATOM   8169  CE1 PHE D  65      45.784  52.098  28.544  1.00 47.16           C  
-ATOM   8170  CE2 PHE D  65      43.770  52.025  27.228  1.00 48.92           C  
-ATOM   8171  CZ  PHE D  65      45.160  52.059  27.304  1.00 48.00           C  
-ATOM   8172  N   ASN D  66      42.398  48.817  30.313  1.00 39.81           N  
-ATOM   8173  CA  ASN D  66      42.951  47.492  30.580  1.00 39.87           C  
-ATOM   8174  C   ASN D  66      43.806  46.958  29.440  1.00 39.01           C  
-ATOM   8175  O   ASN D  66      44.194  45.790  29.438  1.00 38.86           O  
-ATOM   8176  CB  ASN D  66      41.824  46.503  30.893  1.00 42.12           C  
-ATOM   8177  CG  ASN D  66      40.947  46.219  29.695  1.00 44.55           C  
-ATOM   8178  OD1 ASN D  66      40.500  47.136  29.005  1.00 47.50           O  
-ATOM   8179  ND2 ASN D  66      40.685  44.939  29.444  1.00 47.47           N  
-ATOM   8180  N   THR D  67      44.109  47.826  28.481  1.00 36.52           N  
-ATOM   8181  CA  THR D  67      44.921  47.451  27.334  1.00 34.78           C  
-ATOM   8182  C   THR D  67      46.296  48.109  27.394  1.00 32.85           C  
-ATOM   8183  O   THR D  67      46.889  48.425  26.362  1.00 31.27           O  
-ATOM   8184  CB  THR D  67      44.231  47.857  26.030  1.00 34.29           C  
-ATOM   8185  OG1 THR D  67      43.931  49.256  26.069  1.00 36.49           O  
-ATOM   8186  CG2 THR D  67      42.947  47.071  25.844  1.00 34.80           C  
-ATOM   8187  N   GLN D  68      46.800  48.300  28.610  1.00 32.21           N  
-ATOM   8188  CA  GLN D  68      48.103  48.927  28.821  1.00 31.61           C  
-ATOM   8189  C   GLN D  68      49.278  48.263  28.103  1.00 30.81           C  
-ATOM   8190  O   GLN D  68      50.190  48.951  27.656  1.00 31.07           O  
-ATOM   8191  CB  GLN D  68      48.429  49.003  30.317  1.00 30.76           C  
-ATOM   8192  CG  GLN D  68      47.502  49.904  31.119  1.00 33.64           C  
-ATOM   8193  CD  GLN D  68      46.274  49.183  31.628  1.00 32.93           C  
-ATOM   8194  OE1 GLN D  68      45.701  48.338  30.941  1.00 32.83           O  
-ATOM   8195  NE2 GLN D  68      45.856  49.522  32.838  1.00 33.85           N  
-ATOM   8196  N   ARG D  69      49.262  46.939  27.986  1.00 29.91           N  
-ATOM   8197  CA  ARG D  69      50.368  46.229  27.346  1.00 29.04           C  
-ATOM   8198  C   ARG D  69      50.358  46.222  25.820  1.00 29.92           C  
-ATOM   8199  O   ARG D  69      51.381  45.935  25.198  1.00 29.10           O  
-ATOM   8200  CB  ARG D  69      50.418  44.776  27.828  1.00 27.90           C  
-ATOM   8201  CG  ARG D  69      50.623  44.598  29.322  1.00 28.16           C  
-ATOM   8202  CD  ARG D  69      50.984  43.148  29.637  1.00 27.65           C  
-ATOM   8203  NE  ARG D  69      51.142  42.919  31.070  1.00 27.43           N  
-ATOM   8204  CZ  ARG D  69      50.136  42.781  31.927  1.00 26.68           C  
-ATOM   8205  NH1 ARG D  69      50.390  42.584  33.215  1.00 25.65           N  
-ATOM   8206  NH2 ARG D  69      48.880  42.820  31.498  1.00 21.02           N  
-ATOM   8207  N   ILE D  70      49.212  46.532  25.221  1.00 29.80           N  
-ATOM   8208  CA  ILE D  70      49.086  46.512  23.769  1.00 32.15           C  
-ATOM   8209  C   ILE D  70      48.595  47.825  23.167  1.00 35.55           C  
-ATOM   8210  O   ILE D  70      48.309  47.895  21.970  1.00 35.74           O  
-ATOM   8211  CB  ILE D  70      48.128  45.389  23.324  1.00 30.39           C  
-ATOM   8212  CG1 ILE D  70      46.727  45.649  23.882  1.00 29.01           C  
-ATOM   8213  CG2 ILE D  70      48.649  44.042  23.808  1.00 28.66           C  
-ATOM   8214  CD1 ILE D  70      45.709  44.592  23.505  1.00 31.03           C  
-ATOM   8215  N   ASN D  71      48.495  48.859  23.996  1.00 39.63           N  
-ATOM   8216  CA  ASN D  71      48.047  50.174  23.542  1.00 42.51           C  
-ATOM   8217  C   ASN D  71      48.922  50.650  22.379  1.00 44.61           C  
-ATOM   8218  O   ASN D  71      48.414  51.056  21.330  1.00 44.35           O  
-ATOM   8219  CB  ASN D  71      48.133  51.181  24.695  1.00 43.43           C  
-ATOM   8220  CG  ASN D  71      47.439  52.500  24.382  1.00 46.59           C  
-ATOM   8221  OD1 ASN D  71      47.684  53.515  25.042  1.00 48.02           O  
-ATOM   8222  ND2 ASN D  71      46.558  52.489  23.385  1.00 46.69           N  
-ATOM   8223  N   HIS D  72      50.239  50.581  22.570  1.00 45.49           N  
-ATOM   8224  CA  HIS D  72      51.194  51.011  21.551  1.00 46.40           C  
-ATOM   8225  C   HIS D  72      51.048  50.268  20.226  1.00 47.93           C  
-ATOM   8226  O   HIS D  72      51.499  50.749  19.187  1.00 48.30           O  
-ATOM   8227  CB  HIS D  72      52.631  50.852  22.064  1.00 46.89           C  
-ATOM   8228  CG  HIS D  72      53.082  49.428  22.205  1.00 47.16           C  
-ATOM   8229  ND1 HIS D  72      52.484  48.536  23.070  1.00 47.86           N  
-ATOM   8230  CD2 HIS D  72      54.099  48.755  21.616  1.00 47.21           C  
-ATOM   8231  CE1 HIS D  72      53.115  47.376  23.010  1.00 46.36           C  
-ATOM   8232  NE2 HIS D  72      54.100  47.483  22.136  1.00 48.06           N  
-ATOM   8233  N   ILE D  73      50.422  49.097  20.263  1.00 47.92           N  
-ATOM   8234  CA  ILE D  73      50.229  48.303  19.056  1.00 48.43           C  
-ATOM   8235  C   ILE D  73      48.942  48.720  18.348  1.00 51.07           C  
-ATOM   8236  O   ILE D  73      48.923  48.883  17.127  1.00 51.87           O  
-ATOM   8237  CB  ILE D  73      50.150  46.794  19.386  1.00 46.87           C  
-ATOM   8238  CG1 ILE D  73      51.421  46.350  20.106  1.00 45.07           C  
-ATOM   8239  CG2 ILE D  73      49.977  45.982  18.107  1.00 45.77           C  
-ATOM   8240  CD1 ILE D  73      51.362  44.933  20.606  1.00 45.18           C  
-ATOM   8241  N   TYR D  74      47.875  48.894  19.128  1.00 52.40           N  
-ATOM   8242  CA  TYR D  74      46.568  49.286  18.600  1.00 53.02           C  
-ATOM   8243  C   TYR D  74      46.668  50.577  17.806  1.00 52.94           C  
-ATOM   8244  O   TYR D  74      45.940  50.775  16.834  1.00 51.20           O  
-ATOM   8245  CB  TYR D  74      45.564  49.458  19.746  1.00 52.39           C  
-ATOM   8246  N   ILE D  75      47.576  51.450  18.232  1.00 54.22           N  
-ATOM   8247  CA  ILE D  75      47.784  52.735  17.578  1.00 54.86           C  
-ATOM   8248  C   ILE D  75      49.028  52.699  16.692  1.00 55.49           C  
-ATOM   8249  O   ILE D  75      49.615  51.639  16.466  1.00 55.79           O  
-ATOM   8250  CB  ILE D  75      47.914  53.834  18.629  1.00 54.21           C  
-ATOM   8251  N   LEU D  84      45.922  45.537  11.690  1.00 44.50           N  
-ATOM   8252  CA  LEU D  84      46.092  44.088  11.659  1.00 44.59           C  
-ATOM   8253  C   LEU D  84      45.844  43.441  13.019  1.00 43.53           C  
-ATOM   8254  O   LEU D  84      46.039  42.239  13.190  1.00 44.20           O  
-ATOM   8255  CB  LEU D  84      47.496  43.730  11.161  1.00 45.45           C  
-ATOM   8256  CG  LEU D  84      47.709  43.800   9.643  1.00 47.69           C  
-ATOM   8257  CD1 LEU D  84      49.184  43.616   9.309  1.00 46.50           C  
-ATOM   8258  CD2 LEU D  84      46.869  42.724   8.964  1.00 45.77           C  
-ATOM   8259  N   MET D  85      45.422  44.245  13.987  1.00 43.14           N  
-ATOM   8260  CA  MET D  85      45.123  43.742  15.322  1.00 42.25           C  
-ATOM   8261  C   MET D  85      43.723  44.201  15.715  1.00 42.18           C  
-ATOM   8262  O   MET D  85      43.485  45.395  15.912  1.00 42.33           O  
-ATOM   8263  CB  MET D  85      46.134  44.264  16.343  1.00 41.81           C  
-ATOM   8264  CG  MET D  85      45.834  43.815  17.764  1.00 42.44           C  
-ATOM   8265  SD  MET D  85      46.920  44.549  18.991  1.00 46.76           S  
-ATOM   8266  CE  MET D  85      46.024  46.040  19.388  1.00 44.10           C  
-ATOM   8267  N   LYS D  86      42.796  43.253  15.816  1.00 40.83           N  
-ATOM   8268  CA  LYS D  86      41.419  43.565  16.186  1.00 39.92           C  
-ATOM   8269  C   LYS D  86      41.135  43.055  17.592  1.00 37.24           C  
-ATOM   8270  O   LYS D  86      41.559  41.960  17.956  1.00 38.54           O  
-ATOM   8271  CB  LYS D  86      40.444  42.905  15.211  1.00 41.86           C  
-ATOM   8272  CG  LYS D  86      40.553  43.369  13.763  1.00 45.55           C  
-ATOM   8273  CD  LYS D  86      39.888  44.716  13.549  1.00 47.29           C  
-ATOM   8274  CE  LYS D  86      39.782  45.035  12.064  1.00 50.49           C  
-ATOM   8275  NZ  LYS D  86      38.999  46.282  11.806  1.00 52.11           N  
-ATOM   8276  N   LEU D  87      40.419  43.852  18.378  1.00 34.85           N  
-ATOM   8277  CA  LEU D  87      40.065  43.469  19.741  1.00 31.70           C  
-ATOM   8278  C   LEU D  87      38.558  43.239  19.819  1.00 31.15           C  
-ATOM   8279  O   LEU D  87      37.782  44.019  19.269  1.00 29.71           O  
-ATOM   8280  CB  LEU D  87      40.484  44.561  20.728  1.00 29.25           C  
-ATOM   8281  CG  LEU D  87      41.987  44.822  20.883  1.00 29.99           C  
-ATOM   8282  CD1 LEU D  87      42.188  45.871  21.964  1.00 29.54           C  
-ATOM   8283  CD2 LEU D  87      42.730  43.538  21.256  1.00 26.73           C  
-ATOM   8284  N   HIS D  88      38.150  42.163  20.493  1.00 31.45           N  
-ATOM   8285  CA  HIS D  88      36.732  41.817  20.624  1.00 30.46           C  
-ATOM   8286  C   HIS D  88      36.379  41.436  22.064  1.00 28.65           C  
-ATOM   8287  O   HIS D  88      37.130  40.722  22.723  1.00 27.90           O  
-ATOM   8288  CB  HIS D  88      36.394  40.629  19.719  1.00 28.94           C  
-ATOM   8289  CG  HIS D  88      37.025  40.692  18.364  1.00 32.48           C  
-ATOM   8290  ND1 HIS D  88      36.591  41.550  17.376  1.00 33.47           N  
-ATOM   8291  CD2 HIS D  88      38.056  39.993  17.829  1.00 32.38           C  
-ATOM   8292  CE1 HIS D  88      37.326  41.376  16.292  1.00 33.71           C  
-ATOM   8293  NE2 HIS D  88      38.223  40.437  16.541  1.00 31.97           N  
-ATOM   8294  N   TYR D  89      35.227  41.898  22.542  1.00 28.47           N  
-ATOM   8295  CA  TYR D  89      34.791  41.585  23.899  1.00 26.37           C  
-ATOM   8296  C   TYR D  89      34.339  40.139  24.023  1.00 25.94           C  
-ATOM   8297  O   TYR D  89      33.559  39.642  23.211  1.00 26.50           O  
-ATOM   8298  CB  TYR D  89      33.651  42.509  24.332  1.00 25.83           C  
-ATOM   8299  CG  TYR D  89      34.105  43.915  24.630  1.00 26.11           C  
-ATOM   8300  CD1 TYR D  89      33.652  44.989  23.868  1.00 24.18           C  
-ATOM   8301  CD2 TYR D  89      35.001  44.171  25.666  1.00 24.63           C  
-ATOM   8302  CE1 TYR D  89      34.077  46.279  24.127  1.00 26.73           C  
-ATOM   8303  CE2 TYR D  89      35.432  45.460  25.931  1.00 26.39           C  
-ATOM   8304  CZ  TYR D  89      34.966  46.509  25.158  1.00 26.88           C  
-ATOM   8305  OH  TYR D  89      35.388  47.791  25.417  1.00 31.45           O  
-ATOM   8306  N   ALA D  90      34.834  39.466  25.050  1.00 24.37           N  
-ATOM   8307  CA  ALA D  90      34.477  38.075  25.277  1.00 23.95           C  
-ATOM   8308  C   ALA D  90      34.913  37.672  26.679  1.00 22.74           C  
-ATOM   8309  O   ALA D  90      35.571  38.440  27.375  1.00 24.53           O  
-ATOM   8310  CB  ALA D  90      35.153  37.189  24.238  1.00 22.59           C  
-ATOM   8311  N   ASP D  91      34.536  36.470  27.091  1.00 21.97           N  
-ATOM   8312  CA  ASP D  91      34.907  35.977  28.406  1.00 20.69           C  
-ATOM   8313  C   ASP D  91      34.940  34.454  28.394  1.00 19.91           C  
-ATOM   8314  O   ASP D  91      34.065  33.808  27.821  1.00 21.51           O  
-ATOM   8315  CB  ASP D  91      33.926  36.489  29.465  1.00 20.39           C  
-ATOM   8316  CG  ASP D  91      34.469  36.335  30.866  1.00 23.49           C  
-ATOM   8317  OD1 ASP D  91      34.544  35.188  31.349  1.00 28.35           O  
-ATOM   8318  OD2 ASP D  91      34.840  37.359  31.478  1.00 26.92           O  
-ATOM   8319  N   LEU D  92      35.953  33.878  29.027  1.00 21.19           N  
-ATOM   8320  CA  LEU D  92      36.082  32.429  29.049  1.00 23.14           C  
-ATOM   8321  C   LEU D  92      34.978  31.728  29.819  1.00 21.68           C  
-ATOM   8322  O   LEU D  92      34.844  30.510  29.740  1.00 20.36           O  
-ATOM   8323  CB  LEU D  92      37.457  32.023  29.587  1.00 23.99           C  
-ATOM   8324  CG  LEU D  92      38.442  31.639  28.475  1.00 28.60           C  
-ATOM   8325  CD1 LEU D  92      38.539  32.769  27.452  1.00 30.58           C  
-ATOM   8326  CD2 LEU D  92      39.804  31.343  29.070  1.00 31.23           C  
-ATOM   8327  N   THR D  93      34.172  32.491  30.549  1.00 20.98           N  
-ATOM   8328  CA  THR D  93      33.072  31.889  31.290  1.00 23.27           C  
-ATOM   8329  C   THR D  93      31.790  31.985  30.470  1.00 23.28           C  
-ATOM   8330  O   THR D  93      30.729  31.550  30.906  1.00 23.78           O  
-ATOM   8331  CB  THR D  93      32.850  32.586  32.633  1.00 22.09           C  
-ATOM   8332  OG1 THR D  93      32.591  33.974  32.409  1.00 24.91           O  
-ATOM   8333  CG2 THR D  93      34.083  32.442  33.509  1.00 25.92           C  
-ATOM   8334  N   ASP D  94      31.913  32.546  29.271  1.00 24.53           N  
-ATOM   8335  CA  ASP D  94      30.783  32.738  28.369  1.00 25.29           C  
-ATOM   8336  C   ASP D  94      31.066  31.981  27.063  1.00 26.46           C  
-ATOM   8337  O   ASP D  94      31.716  32.502  26.153  1.00 26.52           O  
-ATOM   8338  CB  ASP D  94      30.613  34.245  28.123  1.00 25.70           C  
-ATOM   8339  CG  ASP D  94      29.427  34.586  27.228  1.00 27.85           C  
-ATOM   8340  OD1 ASP D  94      29.044  35.782  27.195  1.00 28.31           O  
-ATOM   8341  OD2 ASP D  94      28.886  33.685  26.555  1.00 27.12           O  
-ATOM   8342  N   ALA D  95      30.574  30.746  26.986  1.00 27.18           N  
-ATOM   8343  CA  ALA D  95      30.780  29.897  25.816  1.00 26.91           C  
-ATOM   8344  C   ALA D  95      30.273  30.545  24.535  1.00 28.16           C  
-ATOM   8345  O   ALA D  95      30.916  30.446  23.491  1.00 29.88           O  
-ATOM   8346  CB  ALA D  95      30.105  28.546  26.024  1.00 24.40           C  
-ATOM   8347  N   SER D  96      29.126  31.214  24.616  1.00 27.88           N  
-ATOM   8348  CA  SER D  96      28.556  31.872  23.448  1.00 29.27           C  
-ATOM   8349  C   SER D  96      29.532  32.896  22.873  1.00 29.15           C  
-ATOM   8350  O   SER D  96      29.775  32.917  21.662  1.00 28.92           O  
-ATOM   8351  CB  SER D  96      27.252  32.585  23.808  1.00 29.65           C  
-ATOM   8352  OG  SER D  96      26.358  31.725  24.487  1.00 38.76           O  
-ATOM   8353  N   SER D  97      30.087  33.741  23.740  1.00 26.53           N  
-ATOM   8354  CA  SER D  97      31.020  34.769  23.300  1.00 26.49           C  
-ATOM   8355  C   SER D  97      32.212  34.165  22.575  1.00 28.21           C  
-ATOM   8356  O   SER D  97      32.730  34.756  21.634  1.00 29.50           O  
-ATOM   8357  CB  SER D  97      31.517  35.606  24.485  1.00 27.79           C  
-ATOM   8358  OG  SER D  97      32.466  34.905  25.269  1.00 27.87           O  
-ATOM   8359  N   LEU D  98      32.641  32.985  23.009  1.00 28.75           N  
-ATOM   8360  CA  LEU D  98      33.780  32.324  22.387  1.00 29.78           C  
-ATOM   8361  C   LEU D  98      33.477  31.814  20.975  1.00 31.45           C  
-ATOM   8362  O   LEU D  98      34.258  32.031  20.049  1.00 32.00           O  
-ATOM   8363  CB  LEU D  98      34.253  31.162  23.262  1.00 27.29           C  
-ATOM   8364  CG  LEU D  98      34.698  31.511  24.685  1.00 26.17           C  
-ATOM   8365  CD1 LEU D  98      35.220  30.247  25.370  1.00 20.98           C  
-ATOM   8366  CD2 LEU D  98      35.781  32.585  24.644  1.00 24.16           C  
-ATOM   8367  N   ARG D  99      32.349  31.132  20.815  1.00 31.14           N  
-ATOM   8368  CA  ARG D  99      31.967  30.595  19.516  1.00 32.50           C  
-ATOM   8369  C   ARG D  99      31.640  31.716  18.530  1.00 34.15           C  
-ATOM   8370  O   ARG D  99      31.949  31.624  17.341  1.00 33.69           O  
-ATOM   8371  CB  ARG D  99      30.763  29.657  19.668  1.00 31.71           C  
-ATOM   8372  CG  ARG D  99      30.261  29.051  18.364  1.00 32.95           C  
-ATOM   8373  CD  ARG D  99      31.362  28.307  17.625  1.00 33.43           C  
-ATOM   8374  NE  ARG D  99      30.906  27.813  16.326  1.00 35.37           N  
-ATOM   8375  CZ  ARG D  99      30.038  26.820  16.160  1.00 33.17           C  
-ATOM   8376  NH1 ARG D  99      29.523  26.200  17.209  1.00 35.03           N  
-ATOM   8377  NH2 ARG D  99      29.683  26.447  14.941  1.00 34.62           N  
-ATOM   8378  N   ARG D 100      31.024  32.777  19.039  1.00 34.72           N  
-ATOM   8379  CA  ARG D 100      30.649  33.923  18.221  1.00 34.48           C  
-ATOM   8380  C   ARG D 100      31.846  34.476  17.454  1.00 35.65           C  
-ATOM   8381  O   ARG D 100      31.820  34.569  16.225  1.00 35.47           O  
-ATOM   8382  CB  ARG D 100      30.041  35.009  19.115  1.00 37.00           C  
-ATOM   8383  CG  ARG D 100      29.694  36.327  18.424  1.00 37.83           C  
-ATOM   8384  CD  ARG D 100      28.761  37.145  19.312  1.00 40.69           C  
-ATOM   8385  NE  ARG D 100      28.490  38.483  18.794  1.00 42.47           N  
-ATOM   8386  CZ  ARG D 100      27.545  39.290  19.273  1.00 43.63           C  
-ATOM   8387  NH1 ARG D 100      27.364  40.495  18.746  1.00 42.05           N  
-ATOM   8388  NH2 ARG D 100      26.770  38.888  20.276  1.00 42.90           N  
-ATOM   8389  N   TRP D 101      32.900  34.823  18.182  1.00 35.54           N  
-ATOM   8390  CA  TRP D 101      34.094  35.379  17.567  1.00 35.54           C  
-ATOM   8391  C   TRP D 101      34.876  34.407  16.699  1.00 35.80           C  
-ATOM   8392  O   TRP D 101      35.482  34.809  15.711  1.00 36.50           O  
-ATOM   8393  CB  TRP D 101      34.988  35.991  18.644  1.00 33.94           C  
-ATOM   8394  CG  TRP D 101      34.345  37.203  19.229  1.00 34.34           C  
-ATOM   8395  CD1 TRP D 101      33.920  37.372  20.513  1.00 34.39           C  
-ATOM   8396  CD2 TRP D 101      33.964  38.387  18.521  1.00 34.32           C  
-ATOM   8397  NE1 TRP D 101      33.292  38.583  20.649  1.00 33.42           N  
-ATOM   8398  CE2 TRP D 101      33.305  39.228  19.441  1.00 34.28           C  
-ATOM   8399  CE3 TRP D 101      34.113  38.816  17.196  1.00 33.47           C  
-ATOM   8400  CZ2 TRP D 101      32.794  40.479  19.080  1.00 37.86           C  
-ATOM   8401  CZ3 TRP D 101      33.606  40.057  16.836  1.00 36.67           C  
-ATOM   8402  CH2 TRP D 101      32.953  40.876  17.776  1.00 37.42           C  
-ATOM   8403  N   ILE D 102      34.871  33.132  17.061  1.00 35.82           N  
-ATOM   8404  CA  ILE D 102      35.570  32.146  16.256  1.00 35.73           C  
-ATOM   8405  C   ILE D 102      34.868  32.035  14.896  1.00 36.69           C  
-ATOM   8406  O   ILE D 102      35.519  31.859  13.868  1.00 36.82           O  
-ATOM   8407  CB  ILE D 102      35.581  30.766  16.944  1.00 33.70           C  
-ATOM   8408  CG1 ILE D 102      36.496  30.806  18.167  1.00 32.91           C  
-ATOM   8409  CG2 ILE D 102      36.066  29.693  15.973  1.00 33.89           C  
-ATOM   8410  CD1 ILE D 102      36.474  29.527  18.972  1.00 28.15           C  
-ATOM   8411  N   ASP D 103      33.540  32.145  14.896  1.00 36.82           N  
-ATOM   8412  CA  ASP D 103      32.764  32.062  13.658  1.00 37.55           C  
-ATOM   8413  C   ASP D 103      33.020  33.250  12.739  1.00 36.70           C  
-ATOM   8414  O   ASP D 103      33.187  33.082  11.536  1.00 36.93           O  
-ATOM   8415  CB  ASP D 103      31.261  31.988  13.955  1.00 37.39           C  
-ATOM   8416  CG  ASP D 103      30.841  30.651  14.524  1.00 36.24           C  
-ATOM   8417  OD1 ASP D 103      31.629  29.687  14.430  1.00 36.35           O  
-ATOM   8418  OD2 ASP D 103      29.714  30.563  15.053  1.00 38.32           O  
-ATOM   8419  N   VAL D 104      33.036  34.448  13.315  1.00 36.71           N  
-ATOM   8420  CA  VAL D 104      33.263  35.673  12.555  1.00 36.78           C  
-ATOM   8421  C   VAL D 104      34.715  35.810  12.099  1.00 37.23           C  
-ATOM   8422  O   VAL D 104      34.984  36.264  10.988  1.00 35.84           O  
-ATOM   8423  CB  VAL D 104      32.916  36.926  13.392  1.00 36.98           C  
-ATOM   8424  CG1 VAL D 104      33.137  38.185  12.565  1.00 36.01           C  
-ATOM   8425  CG2 VAL D 104      31.484  36.858  13.869  1.00 38.03           C  
-ATOM   8426  N   ILE D 105      35.646  35.425  12.965  1.00 36.95           N  
-ATOM   8427  CA  ILE D 105      37.067  35.531  12.656  1.00 36.52           C  
-ATOM   8428  C   ILE D 105      37.597  34.398  11.780  1.00 35.70           C  
-ATOM   8429  O   ILE D 105      38.447  34.624  10.921  1.00 36.91           O  
-ATOM   8430  CB  ILE D 105      37.903  35.589  13.958  1.00 37.45           C  
-ATOM   8431  CG1 ILE D 105      37.440  36.771  14.810  1.00 35.55           C  
-ATOM   8432  CG2 ILE D 105      39.394  35.710  13.631  1.00 36.28           C  
-ATOM   8433  CD1 ILE D 105      38.076  36.823  16.176  1.00 36.18           C  
-ATOM   8434  N   LYS D 106      37.092  33.188  11.989  1.00 35.88           N  
-ATOM   8435  CA  LYS D 106      37.547  32.029  11.224  1.00 37.00           C  
-ATOM   8436  C   LYS D 106      39.068  31.969  11.305  1.00 36.48           C  
-ATOM   8437  O   LYS D 106      39.762  32.064  10.293  1.00 36.48           O  
-ATOM   8438  CB  LYS D 106      37.105  32.136   9.762  1.00 38.85           C  
-ATOM   8439  CG  LYS D 106      35.602  32.061   9.570  1.00 43.13           C  
-ATOM   8440  CD  LYS D 106      35.216  32.103   8.097  1.00 46.95           C  
-ATOM   8441  CE  LYS D 106      33.703  31.975   7.918  1.00 49.22           C  
-ATOM   8442  NZ  LYS D 106      33.289  31.915   6.478  1.00 51.94           N  
-ATOM   8443  N   PRO D 107      39.605  31.807  12.526  1.00 35.10           N  
-ATOM   8444  CA  PRO D 107      41.046  31.736  12.778  1.00 32.02           C  
-ATOM   8445  C   PRO D 107      41.711  30.457  12.285  1.00 30.27           C  
-ATOM   8446  O   PRO D 107      41.067  29.418  12.154  1.00 30.16           O  
-ATOM   8447  CB  PRO D 107      41.123  31.863  14.293  1.00 33.84           C  
-ATOM   8448  CG  PRO D 107      39.910  31.086  14.728  1.00 33.04           C  
-ATOM   8449  CD  PRO D 107      38.849  31.608  13.779  1.00 33.76           C  
-ATOM   8450  N   ASP D 108      43.009  30.552  12.015  1.00 28.65           N  
-ATOM   8451  CA  ASP D 108      43.802  29.415  11.571  1.00 28.48           C  
-ATOM   8452  C   ASP D 108      44.476  28.837  12.813  1.00 27.66           C  
-ATOM   8453  O   ASP D 108      44.636  27.622  12.945  1.00 27.65           O  
-ATOM   8454  CB  ASP D 108      44.855  29.869  10.550  1.00 28.15           C  
-ATOM   8455  CG  ASP D 108      44.229  30.456   9.289  1.00 31.31           C  
-ATOM   8456  OD1 ASP D 108      43.534  29.707   8.565  1.00 33.26           O  
-ATOM   8457  OD2 ASP D 108      44.420  31.665   9.026  1.00 31.47           O  
-ATOM   8458  N   GLU D 109      44.856  29.723  13.726  1.00 26.74           N  
-ATOM   8459  CA  GLU D 109      45.496  29.319  14.973  1.00 29.02           C  
-ATOM   8460  C   GLU D 109      44.836  29.995  16.178  1.00 28.75           C  
-ATOM   8461  O   GLU D 109      44.564  31.195  16.159  1.00 28.48           O  
-ATOM   8462  CB  GLU D 109      46.988  29.657  14.932  1.00 27.63           C  
-ATOM   8463  CG  GLU D 109      47.727  28.951  13.810  1.00 32.12           C  
-ATOM   8464  CD  GLU D 109      49.207  29.281  13.760  1.00 33.48           C  
-ATOM   8465  OE1 GLU D 109      49.903  28.705  12.899  1.00 34.13           O  
-ATOM   8466  OE2 GLU D 109      49.675  30.109  14.574  1.00 33.81           O  
-ATOM   8467  N   VAL D 110      44.568  29.208  17.215  1.00 29.77           N  
-ATOM   8468  CA  VAL D 110      43.956  29.712  18.441  1.00 27.71           C  
-ATOM   8469  C   VAL D 110      44.909  29.492  19.609  1.00 27.96           C  
-ATOM   8470  O   VAL D 110      45.336  28.365  19.864  1.00 29.34           O  
-ATOM   8471  CB  VAL D 110      42.615  28.988  18.749  1.00 28.24           C  
-ATOM   8472  CG1 VAL D 110      42.064  29.449  20.096  1.00 26.71           C  
-ATOM   8473  CG2 VAL D 110      41.600  29.273  17.649  1.00 24.41           C  
-ATOM   8474  N   TYR D 111      45.248  30.575  20.302  1.00 27.60           N  
-ATOM   8475  CA  TYR D 111      46.140  30.528  21.460  1.00 26.36           C  
-ATOM   8476  C   TYR D 111      45.340  30.872  22.720  1.00 25.63           C  
-ATOM   8477  O   TYR D 111      44.921  32.019  22.909  1.00 25.17           O  
-ATOM   8478  CB  TYR D 111      47.282  31.538  21.288  1.00 27.27           C  
-ATOM   8479  CG  TYR D 111      48.235  31.218  20.156  1.00 26.33           C  
-ATOM   8480  CD1 TYR D 111      49.346  30.406  20.364  1.00 27.54           C  
-ATOM   8481  CD2 TYR D 111      48.013  31.712  18.869  1.00 28.13           C  
-ATOM   8482  CE1 TYR D 111      50.216  30.091  19.323  1.00 27.71           C  
-ATOM   8483  CE2 TYR D 111      48.873  31.402  17.820  1.00 26.76           C  
-ATOM   8484  CZ  TYR D 111      49.973  30.590  18.055  1.00 27.98           C  
-ATOM   8485  OH  TYR D 111      50.819  30.261  17.022  1.00 29.00           O  
-ATOM   8486  N   ASN D 112      45.120  29.879  23.573  1.00 25.97           N  
-ATOM   8487  CA  ASN D 112      44.364  30.090  24.809  1.00 25.31           C  
-ATOM   8488  C   ASN D 112      45.318  30.475  25.929  1.00 24.82           C  
-ATOM   8489  O   ASN D 112      45.829  29.610  26.634  1.00 25.91           O  
-ATOM   8490  CB  ASN D 112      43.619  28.813  25.209  1.00 24.24           C  
-ATOM   8491  CG  ASN D 112      42.761  29.003  26.446  1.00 24.05           C  
-ATOM   8492  OD1 ASN D 112      42.656  28.108  27.285  1.00 28.94           O  
-ATOM   8493  ND2 ASN D 112      42.135  30.166  26.561  1.00 18.90           N  
-ATOM   8494  N   LEU D 113      45.556  31.771  26.090  1.00 25.19           N  
-ATOM   8495  CA  LEU D 113      46.465  32.249  27.126  1.00 26.24           C  
-ATOM   8496  C   LEU D 113      45.698  32.845  28.298  1.00 27.14           C  
-ATOM   8497  O   LEU D 113      46.286  33.172  29.327  1.00 27.14           O  
-ATOM   8498  CB  LEU D 113      47.403  33.316  26.553  1.00 24.62           C  
-ATOM   8499  CG  LEU D 113      48.194  32.965  25.289  1.00 25.95           C  
-ATOM   8500  CD1 LEU D 113      49.149  34.105  24.977  1.00 24.25           C  
-ATOM   8501  CD2 LEU D 113      48.962  31.667  25.480  1.00 22.32           C  
-ATOM   8502  N   ALA D 114      44.384  32.976  28.136  1.00 26.88           N  
-ATOM   8503  CA  ALA D 114      43.541  33.564  29.166  1.00 26.85           C  
-ATOM   8504  C   ALA D 114      43.437  32.717  30.421  1.00 27.32           C  
-ATOM   8505  O   ALA D 114      43.295  31.492  30.355  1.00 29.70           O  
-ATOM   8506  CB  ALA D 114      42.153  33.829  28.614  1.00 25.67           C  
-ATOM   8507  N   ALA D 115      43.499  33.383  31.568  1.00 25.94           N  
-ATOM   8508  CA  ALA D 115      43.394  32.699  32.844  1.00 26.93           C  
-ATOM   8509  C   ALA D 115      43.519  33.642  34.016  1.00 26.45           C  
-ATOM   8510  O   ALA D 115      43.978  34.778  33.880  1.00 26.88           O  
-ATOM   8511  CB  ALA D 115      44.472  31.617  32.958  1.00 28.68           C  
-ATOM   8512  N   GLN D 116      43.067  33.158  35.166  1.00 27.55           N  
-ATOM   8513  CA  GLN D 116      43.192  33.884  36.418  1.00 26.47           C  
-ATOM   8514  C   GLN D 116      44.518  33.231  36.786  1.00 27.22           C  
-ATOM   8515  O   GLN D 116      44.549  32.119  37.310  1.00 27.90           O  
-ATOM   8516  CB  GLN D 116      42.071  33.475  37.373  1.00 24.25           C  
-ATOM   8517  CG  GLN D 116      42.061  34.217  38.695  1.00 24.45           C  
-ATOM   8518  CD  GLN D 116      43.345  34.013  39.478  1.00 24.47           C  
-ATOM   8519  OE1 GLN D 116      44.364  34.652  39.204  1.00 24.92           O  
-ATOM   8520  NE2 GLN D 116      43.307  33.108  40.449  1.00 23.45           N  
-ATOM   8521  N   SER D 117      45.614  33.912  36.474  1.00 28.92           N  
-ATOM   8522  CA  SER D 117      46.942  33.347  36.676  1.00 31.39           C  
-ATOM   8523  C   SER D 117      47.651  33.494  38.005  1.00 33.02           C  
-ATOM   8524  O   SER D 117      48.809  33.107  38.116  1.00 33.75           O  
-ATOM   8525  CB  SER D 117      47.871  33.852  35.573  1.00 30.94           C  
-ATOM   8526  OG  SER D 117      47.968  35.264  35.601  1.00 34.32           O  
-ATOM   8527  N   HIS D 118      46.991  34.036  39.019  1.00 34.98           N  
-ATOM   8528  CA  HIS D 118      47.676  34.181  40.295  1.00 36.24           C  
-ATOM   8529  C   HIS D 118      47.380  33.028  41.245  1.00 33.51           C  
-ATOM   8530  O   HIS D 118      46.249  32.838  41.686  1.00 32.86           O  
-ATOM   8531  CB  HIS D 118      47.324  35.517  40.951  1.00 41.70           C  
-ATOM   8532  CG  HIS D 118      48.422  36.063  41.811  1.00 47.52           C  
-ATOM   8533  ND1 HIS D 118      48.796  35.478  43.002  1.00 49.89           N  
-ATOM   8534  CD2 HIS D 118      49.272  37.099  41.618  1.00 49.44           C  
-ATOM   8535  CE1 HIS D 118      49.831  36.128  43.504  1.00 50.94           C  
-ATOM   8536  NE2 HIS D 118      50.140  37.116  42.683  1.00 51.62           N  
-ATOM   8537  N   VAL D 119      48.421  32.262  41.549  1.00 32.90           N  
-ATOM   8538  CA  VAL D 119      48.323  31.112  42.441  1.00 31.57           C  
-ATOM   8539  C   VAL D 119      47.717  31.457  43.797  1.00 31.68           C  
-ATOM   8540  O   VAL D 119      46.772  30.809  44.235  1.00 32.12           O  
-ATOM   8541  CB  VAL D 119      49.718  30.480  42.654  1.00 32.58           C  
-ATOM   8542  CG1 VAL D 119      49.651  29.370  43.698  1.00 30.55           C  
-ATOM   8543  CG2 VAL D 119      50.233  29.941  41.331  1.00 31.51           C  
-ATOM   8544  N   ALA D 120      48.262  32.479  44.456  1.00 32.19           N  
-ATOM   8545  CA  ALA D 120      47.775  32.895  45.771  1.00 32.44           C  
-ATOM   8546  C   ALA D 120      46.300  33.257  45.713  1.00 31.95           C  
-ATOM   8547  O   ALA D 120      45.514  32.868  46.576  1.00 33.08           O  
-ATOM   8548  CB  ALA D 120      48.584  34.093  46.282  1.00 30.91           C  
-ATOM   8549  N   VAL D 121      45.929  34.010  44.686  1.00 32.72           N  
-ATOM   8550  CA  VAL D 121      44.551  34.429  44.517  1.00 30.90           C  
-ATOM   8551  C   VAL D 121      43.618  33.243  44.292  1.00 31.20           C  
-ATOM   8552  O   VAL D 121      42.451  33.286  44.696  1.00 32.92           O  
-ATOM   8553  CB  VAL D 121      44.419  35.412  43.330  1.00 32.52           C  
-ATOM   8554  CG1 VAL D 121      42.959  35.799  43.120  1.00 30.84           C  
-ATOM   8555  CG2 VAL D 121      45.270  36.656  43.592  1.00 31.01           C  
-ATOM   8556  N   SER D 122      44.126  32.183  43.667  1.00 30.06           N  
-ATOM   8557  CA  SER D 122      43.297  31.012  43.383  1.00 30.30           C  
-ATOM   8558  C   SER D 122      42.718  30.374  44.643  1.00 31.07           C  
-ATOM   8559  O   SER D 122      41.655  29.758  44.590  1.00 30.94           O  
-ATOM   8560  CB  SER D 122      44.076  29.967  42.566  1.00 29.80           C  
-ATOM   8561  OG  SER D 122      44.993  29.243  43.362  1.00 33.11           O  
-ATOM   8562  N   PHE D 123      43.410  30.511  45.773  1.00 31.84           N  
-ATOM   8563  CA  PHE D 123      42.897  29.966  47.029  1.00 31.22           C  
-ATOM   8564  C   PHE D 123      41.729  30.821  47.502  1.00 32.85           C  
-ATOM   8565  O   PHE D 123      40.838  30.340  48.195  1.00 33.76           O  
-ATOM   8566  CB  PHE D 123      43.973  29.957  48.115  1.00 31.35           C  
-ATOM   8567  CG  PHE D 123      45.063  28.958  47.879  1.00 29.54           C  
-ATOM   8568  CD1 PHE D 123      46.232  29.324  47.224  1.00 27.46           C  
-ATOM   8569  CD2 PHE D 123      44.912  27.643  48.304  1.00 27.68           C  
-ATOM   8570  CE1 PHE D 123      47.237  28.395  46.996  1.00 28.27           C  
-ATOM   8571  CE2 PHE D 123      45.911  26.705  48.080  1.00 28.48           C  
-ATOM   8572  CZ  PHE D 123      47.076  27.079  47.426  1.00 28.34           C  
-ATOM   8573  N   GLU D 124      41.741  32.093  47.110  1.00 34.79           N  
-ATOM   8574  CA  GLU D 124      40.696  33.048  47.481  1.00 36.88           C  
-ATOM   8575  C   GLU D 124      39.426  32.890  46.639  1.00 36.20           C  
-ATOM   8576  O   GLU D 124      38.315  32.990  47.161  1.00 35.67           O  
-ATOM   8577  CB  GLU D 124      41.230  34.471  47.331  1.00 39.88           C  
-ATOM   8578  CG  GLU D 124      42.493  34.734  48.129  1.00 45.47           C  
-ATOM   8579  CD  GLU D 124      42.213  35.381  49.468  1.00 48.11           C  
-ATOM   8580  OE1 GLU D 124      41.399  34.835  50.245  1.00 50.60           O  
-ATOM   8581  OE2 GLU D 124      42.811  36.440  49.745  1.00 50.99           O  
-ATOM   8582  N   ILE D 125      39.595  32.667  45.336  1.00 34.24           N  
-ATOM   8583  CA  ILE D 125      38.461  32.482  44.431  1.00 31.94           C  
-ATOM   8584  C   ILE D 125      38.655  31.195  43.635  1.00 31.72           C  
-ATOM   8585  O   ILE D 125      38.848  31.217  42.416  1.00 29.94           O  
-ATOM   8586  CB  ILE D 125      38.312  33.672  43.449  1.00 31.78           C  
-ATOM   8587  CG1 ILE D 125      39.661  33.988  42.797  1.00 31.31           C  
-ATOM   8588  CG2 ILE D 125      37.763  34.889  44.181  1.00 31.57           C  
-ATOM   8589  CD1 ILE D 125      39.580  35.056  41.744  1.00 27.72           C  
-ATOM   8590  N   PRO D 126      38.594  30.046  44.323  1.00 30.74           N  
-ATOM   8591  CA  PRO D 126      38.769  28.740  43.688  1.00 30.13           C  
-ATOM   8592  C   PRO D 126      37.754  28.435  42.597  1.00 29.04           C  
-ATOM   8593  O   PRO D 126      38.133  28.032  41.500  1.00 28.32           O  
-ATOM   8594  CB  PRO D 126      38.674  27.771  44.864  1.00 29.97           C  
-ATOM   8595  CG  PRO D 126      37.737  28.474  45.793  1.00 31.09           C  
-ATOM   8596  CD  PRO D 126      38.244  29.891  45.745  1.00 31.33           C  
-ATOM   8597  N   ASP D 127      36.473  28.628  42.897  1.00 28.17           N  
-ATOM   8598  CA  ASP D 127      35.420  28.350  41.926  1.00 29.38           C  
-ATOM   8599  C   ASP D 127      35.616  29.138  40.642  1.00 29.01           C  
-ATOM   8600  O   ASP D 127      35.658  28.557  39.557  1.00 26.82           O  
-ATOM   8601  CB  ASP D 127      34.040  28.649  42.517  1.00 32.45           C  
-ATOM   8602  CG  ASP D 127      33.710  27.755  43.699  1.00 39.39           C  
-ATOM   8603  OD1 ASP D 127      34.221  26.613  43.743  1.00 41.10           O  
-ATOM   8604  OD2 ASP D 127      32.932  28.180  44.581  1.00 42.18           O  
-ATOM   8605  N   TYR D 128      35.745  30.456  40.767  1.00 26.84           N  
-ATOM   8606  CA  TYR D 128      35.950  31.307  39.603  1.00 27.60           C  
-ATOM   8607  C   TYR D 128      37.164  30.866  38.791  1.00 26.98           C  
-ATOM   8608  O   TYR D 128      37.107  30.782  37.566  1.00 28.72           O  
-ATOM   8609  CB  TYR D 128      36.161  32.766  40.021  1.00 26.25           C  
-ATOM   8610  CG  TYR D 128      36.501  33.667  38.857  1.00 24.48           C  
-ATOM   8611  CD1 TYR D 128      35.504  34.151  38.010  1.00 23.54           C  
-ATOM   8612  CD2 TYR D 128      37.833  33.981  38.558  1.00 25.42           C  
-ATOM   8613  CE1 TYR D 128      35.818  34.919  36.890  1.00 23.12           C  
-ATOM   8614  CE2 TYR D 128      38.157  34.746  37.442  1.00 24.03           C  
-ATOM   8615  CZ  TYR D 128      37.139  35.209  36.612  1.00 23.56           C  
-ATOM   8616  OH  TYR D 128      37.446  35.934  35.492  1.00 27.63           O  
-ATOM   8617  N   THR D 129      38.267  30.604  39.483  1.00 26.37           N  
-ATOM   8618  CA  THR D 129      39.501  30.200  38.824  1.00 26.29           C  
-ATOM   8619  C   THR D 129      39.336  28.901  38.050  1.00 24.52           C  
-ATOM   8620  O   THR D 129      39.814  28.783  36.925  1.00 25.12           O  
-ATOM   8621  CB  THR D 129      40.654  30.057  39.843  1.00 25.83           C  
-ATOM   8622  OG1 THR D 129      40.898  31.330  40.460  1.00 29.28           O  
-ATOM   8623  CG2 THR D 129      41.936  29.600  39.150  1.00 26.52           C  
-ATOM   8624  N   ALA D 130      38.658  27.932  38.651  1.00 23.71           N  
-ATOM   8625  CA  ALA D 130      38.441  26.653  37.991  1.00 25.26           C  
-ATOM   8626  C   ALA D 130      37.587  26.865  36.749  1.00 25.55           C  
-ATOM   8627  O   ALA D 130      37.861  26.310  35.688  1.00 26.27           O  
-ATOM   8628  CB  ALA D 130      37.748  25.677  38.937  1.00 21.75           C  
-ATOM   8629  N   ASP D 131      36.551  27.681  36.891  1.00 25.91           N  
-ATOM   8630  CA  ASP D 131      35.643  27.955  35.793  1.00 26.61           C  
-ATOM   8631  C   ASP D 131      36.358  28.587  34.604  1.00 26.70           C  
-ATOM   8632  O   ASP D 131      36.018  28.315  33.454  1.00 25.64           O  
-ATOM   8633  CB  ASP D 131      34.509  28.861  36.273  1.00 28.05           C  
-ATOM   8634  CG  ASP D 131      33.345  28.885  35.312  1.00 29.45           C  
-ATOM   8635  OD1 ASP D 131      32.990  27.808  34.789  1.00 29.36           O  
-ATOM   8636  OD2 ASP D 131      32.778  29.975  35.094  1.00 34.26           O  
-ATOM   8637  N   VAL D 132      37.359  29.414  34.891  1.00 25.73           N  
-ATOM   8638  CA  VAL D 132      38.126  30.094  33.856  1.00 24.64           C  
-ATOM   8639  C   VAL D 132      39.272  29.251  33.300  1.00 24.38           C  
-ATOM   8640  O   VAL D 132      39.390  29.061  32.094  1.00 25.87           O  
-ATOM   8641  CB  VAL D 132      38.729  31.424  34.398  1.00 25.58           C  
-ATOM   8642  CG1 VAL D 132      39.684  32.024  33.383  1.00 24.41           C  
-ATOM   8643  CG2 VAL D 132      37.621  32.411  34.710  1.00 24.58           C  
-ATOM   8644  N   VAL D 133      40.108  28.747  34.199  1.00 23.06           N  
-ATOM   8645  CA  VAL D 133      41.279  27.969  33.833  1.00 23.97           C  
-ATOM   8646  C   VAL D 133      40.993  26.544  33.358  1.00 24.76           C  
-ATOM   8647  O   VAL D 133      41.590  26.081  32.391  1.00 26.75           O  
-ATOM   8648  CB  VAL D 133      42.282  27.950  35.020  1.00 22.73           C  
-ATOM   8649  CG1 VAL D 133      43.525  27.152  34.672  1.00 18.69           C  
-ATOM   8650  CG2 VAL D 133      42.655  29.387  35.386  1.00 21.21           C  
-ATOM   8651  N   ALA D 134      40.078  25.854  34.027  1.00 26.51           N  
-ATOM   8652  CA  ALA D 134      39.749  24.488  33.645  1.00 25.41           C  
-ATOM   8653  C   ALA D 134      38.607  24.430  32.634  1.00 26.04           C  
-ATOM   8654  O   ALA D 134      38.819  24.133  31.461  1.00 24.72           O  
-ATOM   8655  CB  ALA D 134      39.394  23.671  34.884  1.00 24.92           C  
-ATOM   8656  N   THR D 135      37.395  24.724  33.089  1.00 25.35           N  
-ATOM   8657  CA  THR D 135      36.238  24.664  32.216  1.00 24.97           C  
-ATOM   8658  C   THR D 135      36.318  25.658  31.068  1.00 26.06           C  
-ATOM   8659  O   THR D 135      35.829  25.390  29.980  1.00 26.04           O  
-ATOM   8660  CB  THR D 135      34.938  24.907  32.994  1.00 25.23           C  
-ATOM   8661  OG1 THR D 135      34.878  24.017  34.119  1.00 25.55           O  
-ATOM   8662  CG2 THR D 135      33.735  24.644  32.085  1.00 25.54           C  
-ATOM   8663  N   GLY D 136      36.930  26.807  31.320  1.00 26.63           N  
-ATOM   8664  CA  GLY D 136      37.059  27.809  30.283  1.00 24.63           C  
-ATOM   8665  C   GLY D 136      37.820  27.241  29.106  1.00 24.67           C  
-ATOM   8666  O   GLY D 136      37.430  27.438  27.957  1.00 25.65           O  
-ATOM   8667  N   ALA D 137      38.909  26.534  29.397  1.00 24.18           N  
-ATOM   8668  CA  ALA D 137      39.729  25.922  28.359  1.00 24.68           C  
-ATOM   8669  C   ALA D 137      38.888  24.926  27.560  1.00 25.10           C  
-ATOM   8670  O   ALA D 137      38.950  24.888  26.329  1.00 25.84           O  
-ATOM   8671  CB  ALA D 137      40.930  25.219  28.989  1.00 22.84           C  
-ATOM   8672  N   LEU D 138      38.098  24.124  28.265  1.00 24.07           N  
-ATOM   8673  CA  LEU D 138      37.239  23.143  27.614  1.00 24.35           C  
-ATOM   8674  C   LEU D 138      36.218  23.847  26.713  1.00 24.90           C  
-ATOM   8675  O   LEU D 138      35.912  23.357  25.628  1.00 25.49           O  
-ATOM   8676  CB  LEU D 138      36.531  22.274  28.667  1.00 22.50           C  
-ATOM   8677  CG  LEU D 138      35.592  21.145  28.215  1.00 23.68           C  
-ATOM   8678  CD1 LEU D 138      36.282  20.225  27.192  1.00 22.33           C  
-ATOM   8679  CD2 LEU D 138      35.173  20.345  29.436  1.00 21.39           C  
-ATOM   8680  N   ARG D 139      35.699  24.995  27.153  1.00 24.13           N  
-ATOM   8681  CA  ARG D 139      34.732  25.741  26.351  1.00 23.73           C  
-ATOM   8682  C   ARG D 139      35.354  26.176  25.030  1.00 25.48           C  
-ATOM   8683  O   ARG D 139      34.729  26.075  23.973  1.00 23.59           O  
-ATOM   8684  CB  ARG D 139      34.249  26.997  27.077  1.00 24.34           C  
-ATOM   8685  CG  ARG D 139      33.413  26.763  28.308  1.00 23.34           C  
-ATOM   8686  CD  ARG D 139      32.775  28.067  28.763  1.00 24.00           C  
-ATOM   8687  NE  ARG D 139      31.975  27.857  29.960  1.00 26.29           N  
-ATOM   8688  CZ  ARG D 139      32.458  27.871  31.195  1.00 24.69           C  
-ATOM   8689  NH1 ARG D 139      31.648  27.652  32.217  1.00 25.49           N  
-ATOM   8690  NH2 ARG D 139      33.738  28.137  31.411  1.00 23.82           N  
-ATOM   8691  N   LEU D 140      36.583  26.679  25.094  1.00 23.69           N  
-ATOM   8692  CA  LEU D 140      37.260  27.124  23.888  1.00 26.16           C  
-ATOM   8693  C   LEU D 140      37.507  25.927  22.971  1.00 27.12           C  
-ATOM   8694  O   LEU D 140      37.266  26.005  21.773  1.00 29.47           O  
-ATOM   8695  CB  LEU D 140      38.579  27.821  24.240  1.00 26.04           C  
-ATOM   8696  CG  LEU D 140      39.249  28.642  23.132  1.00 26.97           C  
-ATOM   8697  CD1 LEU D 140      38.306  29.753  22.646  1.00 24.25           C  
-ATOM   8698  CD2 LEU D 140      40.546  29.234  23.668  1.00 24.57           C  
-ATOM   8699  N   LEU D 141      37.979  24.822  23.542  1.00 25.90           N  
-ATOM   8700  CA  LEU D 141      38.234  23.609  22.774  1.00 25.89           C  
-ATOM   8701  C   LEU D 141      36.972  23.129  22.080  1.00 26.28           C  
-ATOM   8702  O   LEU D 141      36.994  22.784  20.899  1.00 27.84           O  
-ATOM   8703  CB  LEU D 141      38.729  22.484  23.684  1.00 25.31           C  
-ATOM   8704  CG  LEU D 141      40.162  22.535  24.202  1.00 25.97           C  
-ATOM   8705  CD1 LEU D 141      40.300  21.616  25.406  1.00 23.85           C  
-ATOM   8706  CD2 LEU D 141      41.117  22.147  23.086  1.00 24.51           C  
-ATOM   8707  N   GLU D 142      35.875  23.091  22.825  1.00 24.78           N  
-ATOM   8708  CA  GLU D 142      34.608  22.631  22.280  1.00 25.92           C  
-ATOM   8709  C   GLU D 142      34.059  23.615  21.250  1.00 27.69           C  
-ATOM   8710  O   GLU D 142      33.409  23.213  20.289  1.00 27.66           O  
-ATOM   8711  CB  GLU D 142      33.603  22.418  23.412  1.00 27.13           C  
-ATOM   8712  CG  GLU D 142      32.233  21.890  22.984  1.00 28.08           C  
-ATOM   8713  CD  GLU D 142      32.296  20.610  22.147  1.00 29.42           C  
-ATOM   8714  OE1 GLU D 142      33.303  19.869  22.200  1.00 28.60           O  
-ATOM   8715  OE2 GLU D 142      31.311  20.333  21.439  1.00 32.90           O  
-ATOM   8716  N   ALA D 143      34.322  24.902  21.452  1.00 27.93           N  
-ATOM   8717  CA  ALA D 143      33.861  25.916  20.517  1.00 29.43           C  
-ATOM   8718  C   ALA D 143      34.620  25.753  19.197  1.00 30.42           C  
-ATOM   8719  O   ALA D 143      34.041  25.899  18.122  1.00 31.51           O  
-ATOM   8720  CB  ALA D 143      34.087  27.310  21.094  1.00 28.78           C  
-ATOM   8721  N   VAL D 144      35.912  25.446  19.290  1.00 30.62           N  
-ATOM   8722  CA  VAL D 144      36.752  25.243  18.110  1.00 31.47           C  
-ATOM   8723  C   VAL D 144      36.372  23.951  17.373  1.00 32.42           C  
-ATOM   8724  O   VAL D 144      36.221  23.952  16.153  1.00 32.82           O  
-ATOM   8725  CB  VAL D 144      38.256  25.176  18.487  1.00 30.21           C  
-ATOM   8726  CG1 VAL D 144      39.078  24.704  17.288  1.00 29.86           C  
-ATOM   8727  CG2 VAL D 144      38.742  26.548  18.935  1.00 28.37           C  
-ATOM   8728  N   ARG D 145      36.221  22.854  18.110  1.00 32.98           N  
-ATOM   8729  CA  ARG D 145      35.850  21.587  17.494  1.00 32.91           C  
-ATOM   8730  C   ARG D 145      34.502  21.722  16.796  1.00 34.16           C  
-ATOM   8731  O   ARG D 145      34.340  21.272  15.666  1.00 36.17           O  
-ATOM   8732  CB  ARG D 145      35.761  20.471  18.534  1.00 33.87           C  
-ATOM   8733  CG  ARG D 145      35.530  19.091  17.921  1.00 34.98           C  
-ATOM   8734  CD  ARG D 145      34.915  18.129  18.913  1.00 36.68           C  
-ATOM   8735  NE  ARG D 145      33.586  18.573  19.313  1.00 39.36           N  
-ATOM   8736  CZ  ARG D 145      32.550  18.673  18.487  1.00 40.71           C  
-ATOM   8737  NH1 ARG D 145      32.684  18.353  17.206  1.00 42.70           N  
-ATOM   8738  NH2 ARG D 145      31.381  19.109  18.935  1.00 38.50           N  
-ATOM   8739  N   SER D 146      33.535  22.334  17.475  1.00 33.69           N  
-ATOM   8740  CA  SER D 146      32.208  22.526  16.901  1.00 35.27           C  
-ATOM   8741  C   SER D 146      32.309  23.331  15.613  1.00 36.71           C  
-ATOM   8742  O   SER D 146      31.664  23.008  14.618  1.00 38.53           O  
-ATOM   8743  CB  SER D 146      31.286  23.270  17.880  1.00 35.68           C  
-ATOM   8744  OG  SER D 146      31.044  22.517  19.058  1.00 35.91           O  
-ATOM   8745  N   HIS D 147      33.124  24.381  15.644  1.00 36.79           N  
-ATOM   8746  CA  HIS D 147      33.319  25.260  14.494  1.00 35.51           C  
-ATOM   8747  C   HIS D 147      33.884  24.530  13.276  1.00 35.79           C  
-ATOM   8748  O   HIS D 147      33.365  24.663  12.170  1.00 34.12           O  
-ATOM   8749  CB  HIS D 147      34.253  26.410  14.882  1.00 34.33           C  
-ATOM   8750  CG  HIS D 147      34.749  27.215  13.720  1.00 32.16           C  
-ATOM   8751  ND1 HIS D 147      33.959  28.122  13.048  1.00 32.62           N  
-ATOM   8752  CD2 HIS D 147      35.962  27.254  13.118  1.00 32.57           C  
-ATOM   8753  CE1 HIS D 147      34.664  28.688  12.085  1.00 31.82           C  
-ATOM   8754  NE2 HIS D 147      35.883  28.178  12.106  1.00 31.11           N  
-ATOM   8755  N   THR D 148      34.946  23.762  13.483  1.00 36.71           N  
-ATOM   8756  CA  THR D 148      35.579  23.038  12.391  1.00 38.53           C  
-ATOM   8757  C   THR D 148      34.668  21.985  11.778  1.00 39.78           C  
-ATOM   8758  O   THR D 148      34.790  21.665  10.599  1.00 41.32           O  
-ATOM   8759  CB  THR D 148      36.880  22.359  12.852  1.00 37.65           C  
-ATOM   8760  OG1 THR D 148      36.578  21.341  13.814  1.00 36.12           O  
-ATOM   8761  CG2 THR D 148      37.814  23.386  13.473  1.00 35.63           C  
-ATOM   8762  N   ILE D 149      33.754  21.445  12.574  1.00 40.97           N  
-ATOM   8763  CA  ILE D 149      32.835  20.433  12.073  1.00 41.85           C  
-ATOM   8764  C   ILE D 149      31.677  21.078  11.314  1.00 42.26           C  
-ATOM   8765  O   ILE D 149      31.143  20.500  10.373  1.00 42.87           O  
-ATOM   8766  CB  ILE D 149      32.261  19.578  13.225  1.00 42.28           C  
-ATOM   8767  CG1 ILE D 149      33.386  18.809  13.922  1.00 43.87           C  
-ATOM   8768  CG2 ILE D 149      31.217  18.614  12.684  1.00 44.24           C  
-ATOM   8769  CD1 ILE D 149      34.098  17.793  13.035  1.00 44.44           C  
-ATOM   8770  N   ASP D 150      31.299  22.284  11.723  1.00 42.90           N  
-ATOM   8771  CA  ASP D 150      30.194  22.991  11.088  1.00 43.61           C  
-ATOM   8772  C   ASP D 150      30.627  23.713   9.816  1.00 44.34           C  
-ATOM   8773  O   ASP D 150      29.840  23.859   8.878  1.00 44.04           O  
-ATOM   8774  CB  ASP D 150      29.593  24.005  12.068  1.00 43.96           C  
-ATOM   8775  CG  ASP D 150      28.329  24.662  11.534  1.00 44.53           C  
-ATOM   8776  OD1 ASP D 150      27.305  23.960  11.375  1.00 44.30           O  
-ATOM   8777  OD2 ASP D 150      28.358  25.883  11.276  1.00 45.66           O  
-ATOM   8778  N   SER D 151      31.880  24.158   9.783  1.00 44.35           N  
-ATOM   8779  CA  SER D 151      32.393  24.884   8.629  1.00 44.37           C  
-ATOM   8780  C   SER D 151      33.379  24.067   7.799  1.00 44.63           C  
-ATOM   8781  O   SER D 151      33.845  24.523   6.753  1.00 45.22           O  
-ATOM   8782  CB  SER D 151      33.073  26.176   9.087  1.00 45.11           C  
-ATOM   8783  OG  SER D 151      34.303  25.897   9.734  1.00 45.15           O  
-ATOM   8784  N   GLY D 152      33.698  22.867   8.266  1.00 43.54           N  
-ATOM   8785  CA  GLY D 152      34.636  22.026   7.546  1.00 41.79           C  
-ATOM   8786  C   GLY D 152      36.052  22.574   7.552  1.00 41.67           C  
-ATOM   8787  O   GLY D 152      36.909  22.074   6.827  1.00 43.23           O  
-ATOM   8788  N   ARG D 153      36.306  23.592   8.372  1.00 40.68           N  
-ATOM   8789  CA  ARG D 153      37.633  24.204   8.456  1.00 39.05           C  
-ATOM   8790  C   ARG D 153      38.611  23.471   9.376  1.00 38.84           C  
-ATOM   8791  O   ARG D 153      38.244  22.538  10.093  1.00 38.88           O  
-ATOM   8792  CB  ARG D 153      37.528  25.654   8.933  1.00 39.03           C  
-ATOM   8793  CG  ARG D 153      36.715  26.571   8.050  1.00 38.42           C  
-ATOM   8794  CD  ARG D 153      36.926  28.021   8.464  1.00 38.08           C  
-ATOM   8795  NE  ARG D 153      38.346  28.364   8.444  1.00 40.48           N  
-ATOM   8796  CZ  ARG D 153      39.077  28.622   9.525  1.00 41.70           C  
-ATOM   8797  NH1 ARG D 153      38.529  28.590  10.734  1.00 41.48           N  
-ATOM   8798  NH2 ARG D 153      40.369  28.891   9.399  1.00 39.62           N  
-ATOM   8799  N   THR D 154      39.862  23.919   9.345  1.00 38.24           N  
-ATOM   8800  CA  THR D 154      40.928  23.353  10.167  1.00 38.86           C  
-ATOM   8801  C   THR D 154      41.498  24.434  11.088  1.00 37.51           C  
-ATOM   8802  O   THR D 154      41.664  25.587  10.679  1.00 34.93           O  
-ATOM   8803  CB  THR D 154      42.060  22.782   9.291  1.00 39.27           C  
-ATOM   8804  OG1 THR D 154      41.596  21.592   8.641  1.00 43.28           O  
-ATOM   8805  CG2 THR D 154      43.281  22.452  10.135  1.00 40.94           C  
-ATOM   8806  N   VAL D 155      41.797  24.055  12.329  1.00 35.96           N  
-ATOM   8807  CA  VAL D 155      42.325  24.997  13.308  1.00 34.32           C  
-ATOM   8808  C   VAL D 155      43.405  24.397  14.201  1.00 34.02           C  
-ATOM   8809  O   VAL D 155      43.245  23.303  14.734  1.00 33.57           O  
-ATOM   8810  CB  VAL D 155      41.192  25.531  14.223  1.00 35.87           C  
-ATOM   8811  CG1 VAL D 155      41.768  26.445  15.299  1.00 35.58           C  
-ATOM   8812  CG2 VAL D 155      40.165  26.283  13.395  1.00 35.45           C  
-ATOM   8813  N   LYS D 156      44.511  25.115  14.356  1.00 34.55           N  
-ATOM   8814  CA  LYS D 156      45.588  24.658  15.226  1.00 34.69           C  
-ATOM   8815  C   LYS D 156      45.347  25.324  16.580  1.00 33.12           C  
-ATOM   8816  O   LYS D 156      45.051  26.516  16.656  1.00 30.76           O  
-ATOM   8817  CB  LYS D 156      46.948  25.039  14.646  1.00 37.00           C  
-ATOM   8818  CG  LYS D 156      47.306  24.241  13.392  1.00 41.62           C  
-ATOM   8819  CD  LYS D 156      48.590  24.757  12.768  1.00 43.96           C  
-ATOM   8820  CE  LYS D 156      48.998  23.931  11.566  1.00 47.89           C  
-ATOM   8821  NZ  LYS D 156      50.217  24.505  10.923  1.00 49.38           N  
-ATOM   8822  N   TYR D 157      45.487  24.546  17.644  1.00 31.77           N  
-ATOM   8823  CA  TYR D 157      45.200  25.032  18.981  1.00 28.89           C  
-ATOM   8824  C   TYR D 157      46.365  24.948  19.962  1.00 28.76           C  
-ATOM   8825  O   TYR D 157      47.120  23.972  19.976  1.00 28.61           O  
-ATOM   8826  CB  TYR D 157      44.008  24.238  19.512  1.00 27.41           C  
-ATOM   8827  CG  TYR D 157      43.407  24.732  20.805  1.00 27.02           C  
-ATOM   8828  CD1 TYR D 157      42.252  25.511  20.805  1.00 25.33           C  
-ATOM   8829  CD2 TYR D 157      43.970  24.388  22.031  1.00 24.69           C  
-ATOM   8830  CE1 TYR D 157      41.670  25.929  21.991  1.00 27.14           C  
-ATOM   8831  CE2 TYR D 157      43.396  24.802  23.224  1.00 27.08           C  
-ATOM   8832  CZ  TYR D 157      42.249  25.570  23.197  1.00 26.83           C  
-ATOM   8833  OH  TYR D 157      41.684  25.980  24.378  1.00 30.65           O  
-ATOM   8834  N   TYR D 158      46.494  25.982  20.789  1.00 28.67           N  
-ATOM   8835  CA  TYR D 158      47.544  26.036  21.801  1.00 27.39           C  
-ATOM   8836  C   TYR D 158      46.961  26.273  23.196  1.00 27.77           C  
-ATOM   8837  O   TYR D 158      46.153  27.179  23.394  1.00 27.30           O  
-ATOM   8838  CB  TYR D 158      48.539  27.156  21.500  1.00 26.88           C  
-ATOM   8839  CG  TYR D 158      49.581  27.305  22.588  1.00 28.49           C  
-ATOM   8840  CD1 TYR D 158      50.710  26.487  22.615  1.00 28.19           C  
-ATOM   8841  CD2 TYR D 158      49.395  28.204  23.639  1.00 27.82           C  
-ATOM   8842  CE1 TYR D 158      51.624  26.556  23.661  1.00 28.33           C  
-ATOM   8843  CE2 TYR D 158      50.301  28.277  24.695  1.00 26.29           C  
-ATOM   8844  CZ  TYR D 158      51.411  27.449  24.700  1.00 27.46           C  
-ATOM   8845  OH  TYR D 158      52.296  27.497  25.751  1.00 26.03           O  
-ATOM   8846  N   GLN D 159      47.381  25.458  24.156  1.00 27.98           N  
-ATOM   8847  CA  GLN D 159      46.926  25.599  25.534  1.00 27.78           C  
-ATOM   8848  C   GLN D 159      48.106  26.010  26.398  1.00 27.13           C  
-ATOM   8849  O   GLN D 159      49.149  25.352  26.403  1.00 24.77           O  
-ATOM   8850  CB  GLN D 159      46.341  24.285  26.060  1.00 27.41           C  
-ATOM   8851  CG  GLN D 159      46.154  24.250  27.579  1.00 26.21           C  
-ATOM   8852  CD  GLN D 159      45.227  25.347  28.106  1.00 28.25           C  
-ATOM   8853  OE1 GLN D 159      45.207  25.632  29.306  1.00 25.97           O  
-ATOM   8854  NE2 GLN D 159      44.453  25.954  27.216  1.00 26.48           N  
-ATOM   8855  N   ALA D 160      47.937  27.102  27.133  1.00 27.15           N  
-ATOM   8856  CA  ALA D 160      49.002  27.596  27.986  1.00 26.89           C  
-ATOM   8857  C   ALA D 160      49.107  26.792  29.267  1.00 27.12           C  
-ATOM   8858  O   ALA D 160      48.416  27.079  30.244  1.00 27.75           O  
-ATOM   8859  CB  ALA D 160      48.777  29.073  28.309  1.00 27.46           C  
-ATOM   8860  N   GLY D 161      49.969  25.779  29.247  1.00 27.11           N  
-ATOM   8861  CA  GLY D 161      50.188  24.954  30.421  1.00 28.89           C  
-ATOM   8862  C   GLY D 161      51.187  25.623  31.349  1.00 30.02           C  
-ATOM   8863  O   GLY D 161      51.869  26.575  30.963  1.00 30.03           O  
-ATOM   8864  N   SER D 162      51.287  25.120  32.574  1.00 31.22           N  
-ATOM   8865  CA  SER D 162      52.189  25.705  33.557  1.00 31.02           C  
-ATOM   8866  C   SER D 162      52.953  24.668  34.368  1.00 30.28           C  
-ATOM   8867  O   SER D 162      52.403  23.637  34.753  1.00 29.83           O  
-ATOM   8868  CB  SER D 162      51.388  26.601  34.505  1.00 32.05           C  
-ATOM   8869  OG  SER D 162      52.210  27.141  35.519  1.00 36.69           O  
-ATOM   8870  N   SER D 163      54.201  24.988  34.684  1.00 29.95           N  
-ATOM   8871  CA  SER D 163      55.028  24.087  35.476  1.00 31.86           C  
-ATOM   8872  C   SER D 163      54.394  23.864  36.848  1.00 30.87           C  
-ATOM   8873  O   SER D 163      54.776  22.953  37.576  1.00 32.37           O  
-ATOM   8874  CB  SER D 163      56.445  24.658  35.630  1.00 31.11           C  
-ATOM   8875  OG  SER D 163      56.420  26.008  36.062  1.00 32.61           O  
-ATOM   8876  N   GLU D 164      53.424  24.704  37.192  1.00 31.23           N  
-ATOM   8877  CA  GLU D 164      52.725  24.588  38.464  1.00 30.72           C  
-ATOM   8878  C   GLU D 164      51.966  23.267  38.540  1.00 30.88           C  
-ATOM   8879  O   GLU D 164      51.647  22.792  39.628  1.00 29.17           O  
-ATOM   8880  CB  GLU D 164      51.740  25.748  38.633  1.00 34.42           C  
-ATOM   8881  CG  GLU D 164      52.396  27.083  38.880  1.00 37.71           C  
-ATOM   8882  CD  GLU D 164      53.107  27.121  40.208  1.00 38.78           C  
-ATOM   8883  OE1 GLU D 164      52.428  27.044  41.250  1.00 43.42           O  
-ATOM   8884  OE2 GLU D 164      54.350  27.215  40.217  1.00 41.27           O  
-ATOM   8885  N   MET D 165      51.702  22.692  37.342  1.00 28.95           N  
-ATOM   8886  CA  MET D 165      50.969  21.430  37.318  1.00 28.80           C  
-ATOM   8887  C   MET D 165      51.761  20.304  37.973  1.00 29.59           C  
-ATOM   8888  O   MET D 165      51.180  19.394  38.557  1.00 28.65           O  
-ATOM   8889  CB  MET D 165      50.614  21.031  35.875  1.00 27.06           C  
-ATOM   8890  CG  MET D 165      49.754  22.050  35.127  1.00 25.79           C  
-ATOM   8891  SD  MET D 165      49.361  21.562  33.425  1.00 27.80           S  
-ATOM   8892  CE  MET D 165      50.987  21.600  32.662  1.00 26.45           C  
-ATOM   8893  N   PHE D 166      53.086  20.366  37.879  1.00 29.62           N  
-ATOM   8894  CA  PHE D 166      53.925  19.332  38.472  1.00 30.15           C  
-ATOM   8895  C   PHE D 166      53.842  19.355  39.994  1.00 30.44           C  
-ATOM   8896  O   PHE D 166      53.934  18.316  40.648  1.00 30.88           O  
-ATOM   8897  CB  PHE D 166      55.377  19.504  38.023  1.00 29.48           C  
-ATOM   8898  CG  PHE D 166      55.574  19.322  36.548  1.00 27.28           C  
-ATOM   8899  CD1 PHE D 166      56.099  20.346  35.771  1.00 27.87           C  
-ATOM   8900  CD2 PHE D 166      55.227  18.128  35.933  1.00 26.48           C  
-ATOM   8901  CE1 PHE D 166      56.274  20.183  34.403  1.00 27.16           C  
-ATOM   8902  CE2 PHE D 166      55.397  17.954  34.568  1.00 26.51           C  
-ATOM   8903  CZ  PHE D 166      55.921  18.980  33.800  1.00 25.98           C  
-ATOM   8904  N   GLY D 167      53.665  20.545  40.553  1.00 30.13           N  
-ATOM   8905  CA  GLY D 167      53.566  20.665  41.993  1.00 32.36           C  
-ATOM   8906  C   GLY D 167      54.780  20.142  42.738  1.00 34.99           C  
-ATOM   8907  O   GLY D 167      55.913  20.550  42.472  1.00 32.74           O  
-ATOM   8908  N   SER D 168      54.535  19.218  43.662  1.00 36.61           N  
-ATOM   8909  CA  SER D 168      55.588  18.637  44.485  1.00 39.34           C  
-ATOM   8910  C   SER D 168      56.310  17.424  43.894  1.00 40.18           C  
-ATOM   8911  O   SER D 168      57.163  16.834  44.556  1.00 40.71           O  
-ATOM   8912  CB  SER D 168      55.008  18.264  45.848  1.00 39.81           C  
-ATOM   8913  OG  SER D 168      53.889  17.415  45.683  1.00 40.99           O  
-ATOM   8914  N   THR D 169      55.979  17.042  42.664  1.00 41.20           N  
-ATOM   8915  CA  THR D 169      56.648  15.903  42.047  1.00 41.35           C  
-ATOM   8916  C   THR D 169      58.129  16.241  41.949  1.00 43.35           C  
-ATOM   8917  O   THR D 169      58.494  17.343  41.538  1.00 44.20           O  
-ATOM   8918  CB  THR D 169      56.106  15.611  40.639  1.00 40.06           C  
-ATOM   8919  OG1 THR D 169      54.696  15.374  40.707  1.00 39.84           O  
-ATOM   8920  CG2 THR D 169      56.782  14.379  40.059  1.00 39.83           C  
-ATOM   8921  N   PRO D 170      59.003  15.302  42.340  1.00 44.03           N  
-ATOM   8922  CA  PRO D 170      60.453  15.515  42.294  1.00 45.39           C  
-ATOM   8923  C   PRO D 170      61.036  15.551  40.879  1.00 46.73           C  
-ATOM   8924  O   PRO D 170      60.578  14.833  39.985  1.00 46.03           O  
-ATOM   8925  CB  PRO D 170      60.992  14.347  43.111  1.00 45.59           C  
-ATOM   8926  CG  PRO D 170      60.016  13.252  42.791  1.00 45.14           C  
-ATOM   8927  CD  PRO D 170      58.684  13.971  42.887  1.00 44.75           C  
-ATOM   8928  N   PRO D 171      62.058  16.397  40.662  1.00 47.90           N  
-ATOM   8929  CA  PRO D 171      62.725  16.548  39.364  1.00 48.07           C  
-ATOM   8930  C   PRO D 171      63.391  15.274  38.843  1.00 46.76           C  
-ATOM   8931  O   PRO D 171      63.579  14.304  39.581  1.00 47.02           O  
-ATOM   8932  CB  PRO D 171      63.740  17.658  39.630  1.00 47.40           C  
-ATOM   8933  CG  PRO D 171      63.032  18.508  40.637  1.00 49.25           C  
-ATOM   8934  CD  PRO D 171      62.498  17.455  41.589  1.00 49.71           C  
-ATOM   8935  N   PRO D 172      63.736  15.260  37.548  1.00 46.53           N  
-ATOM   8936  CA  PRO D 172      63.506  16.383  36.631  1.00 44.55           C  
-ATOM   8937  C   PRO D 172      62.107  16.275  36.032  1.00 43.50           C  
-ATOM   8938  O   PRO D 172      61.647  15.172  35.721  1.00 42.89           O  
-ATOM   8939  CB  PRO D 172      64.596  16.191  35.588  1.00 44.90           C  
-ATOM   8940  CG  PRO D 172      64.630  14.689  35.455  1.00 46.44           C  
-ATOM   8941  CD  PRO D 172      64.559  14.216  36.906  1.00 45.31           C  
-ATOM   8942  N   GLN D 173      61.427  17.407  35.872  1.00 41.40           N  
-ATOM   8943  CA  GLN D 173      60.083  17.383  35.302  1.00 40.03           C  
-ATOM   8944  C   GLN D 173      60.094  17.559  33.790  1.00 38.66           C  
-ATOM   8945  O   GLN D 173      60.541  18.585  33.280  1.00 38.23           O  
-ATOM   8946  CB  GLN D 173      59.198  18.474  35.916  1.00 39.68           C  
-ATOM   8947  CG  GLN D 173      58.866  18.298  37.387  1.00 39.01           C  
-ATOM   8948  CD  GLN D 173      59.913  18.900  38.292  1.00 39.82           C  
-ATOM   8949  OE1 GLN D 173      60.416  19.994  38.034  1.00 38.91           O  
-ATOM   8950  NE2 GLN D 173      60.236  18.200  39.370  1.00 42.55           N  
-ATOM   8951  N   SER D 174      59.598  16.550  33.081  1.00 38.78           N  
-ATOM   8952  CA  SER D 174      59.524  16.588  31.621  1.00 37.95           C  
-ATOM   8953  C   SER D 174      58.054  16.523  31.205  1.00 36.92           C  
-ATOM   8954  O   SER D 174      57.161  16.621  32.051  1.00 36.30           O  
-ATOM   8955  CB  SER D 174      60.295  15.410  31.012  1.00 36.77           C  
-ATOM   8956  OG  SER D 174      59.757  14.170  31.438  1.00 38.77           O  
-ATOM   8957  N   GLU D 175      57.805  16.357  29.911  1.00 34.80           N  
-ATOM   8958  CA  GLU D 175      56.439  16.285  29.408  1.00 34.04           C  
-ATOM   8959  C   GLU D 175      55.608  15.179  30.058  1.00 34.60           C  
-ATOM   8960  O   GLU D 175      54.412  15.354  30.292  1.00 34.80           O  
-ATOM   8961  CB  GLU D 175      56.433  16.061  27.894  1.00 33.88           C  
-ATOM   8962  CG  GLU D 175      56.884  17.239  27.040  1.00 34.45           C  
-ATOM   8963  CD  GLU D 175      58.380  17.481  27.081  1.00 34.62           C  
-ATOM   8964  OE1 GLU D 175      59.137  16.551  27.425  1.00 36.64           O  
-ATOM   8965  OE2 GLU D 175      58.805  18.602  26.748  1.00 34.26           O  
-ATOM   8966  N   THR D 176      56.240  14.046  30.354  1.00 35.99           N  
-ATOM   8967  CA  THR D 176      55.534  12.901  30.932  1.00 35.99           C  
-ATOM   8968  C   THR D 176      55.484  12.826  32.455  1.00 34.83           C  
-ATOM   8969  O   THR D 176      54.820  11.951  33.004  1.00 35.41           O  
-ATOM   8970  CB  THR D 176      56.126  11.561  30.417  1.00 37.02           C  
-ATOM   8971  OG1 THR D 176      57.449  11.384  30.942  1.00 37.76           O  
-ATOM   8972  CG2 THR D 176      56.184  11.552  28.898  1.00 36.28           C  
-ATOM   8973  N   THR D 177      56.180  13.724  33.141  1.00 34.10           N  
-ATOM   8974  CA  THR D 177      56.176  13.702  34.600  1.00 33.05           C  
-ATOM   8975  C   THR D 177      54.760  13.832  35.159  1.00 33.79           C  
-ATOM   8976  O   THR D 177      53.976  14.667  34.705  1.00 33.75           O  
-ATOM   8977  CB  THR D 177      57.024  14.833  35.174  1.00 31.08           C  
-ATOM   8978  OG1 THR D 177      58.340  14.769  34.613  1.00 34.54           O  
-ATOM   8979  CG2 THR D 177      57.116  14.707  36.683  1.00 28.44           C  
-ATOM   8980  N   PRO D 178      54.411  12.999  36.152  1.00 34.53           N  
-ATOM   8981  CA  PRO D 178      53.068  13.068  36.737  1.00 33.44           C  
-ATOM   8982  C   PRO D 178      52.824  14.360  37.521  1.00 32.33           C  
-ATOM   8983  O   PRO D 178      53.740  14.928  38.113  1.00 28.28           O  
-ATOM   8984  CB  PRO D 178      53.008  11.817  37.614  1.00 34.81           C  
-ATOM   8985  CG  PRO D 178      54.438  11.623  38.030  1.00 35.64           C  
-ATOM   8986  CD  PRO D 178      55.189  11.894  36.744  1.00 35.59           C  
-ATOM   8987  N   PHE D 179      51.578  14.823  37.507  1.00 31.50           N  
-ATOM   8988  CA  PHE D 179      51.213  16.047  38.206  1.00 31.19           C  
-ATOM   8989  C   PHE D 179      50.803  15.800  39.660  1.00 31.54           C  
-ATOM   8990  O   PHE D 179      50.234  14.763  39.997  1.00 32.08           O  
-ATOM   8991  CB  PHE D 179      50.032  16.744  37.516  1.00 29.74           C  
-ATOM   8992  CG  PHE D 179      50.240  17.037  36.058  1.00 28.17           C  
-ATOM   8993  CD1 PHE D 179      51.484  17.420  35.571  1.00 29.60           C  
-ATOM   8994  CD2 PHE D 179      49.162  16.986  35.176  1.00 27.81           C  
-ATOM   8995  CE1 PHE D 179      51.653  17.751  34.228  1.00 27.98           C  
-ATOM   8996  CE2 PHE D 179      49.318  17.315  33.832  1.00 24.83           C  
-ATOM   8997  CZ  PHE D 179      50.563  17.698  33.356  1.00 27.78           C  
-ATOM   8998  N   HIS D 180      51.099  16.773  40.511  1.00 31.95           N  
-ATOM   8999  CA  HIS D 180      50.707  16.734  41.911  1.00 33.57           C  
-ATOM   9000  C   HIS D 180      50.496  18.203  42.265  1.00 32.22           C  
-ATOM   9001  O   HIS D 180      51.213  18.771  43.086  1.00 33.53           O  
-ATOM   9002  CB  HIS D 180      51.794  16.123  42.799  1.00 34.51           C  
-ATOM   9003  CG  HIS D 180      51.345  15.888  44.208  1.00 39.46           C  
-ATOM   9004  ND1 HIS D 180      51.082  14.630  44.708  1.00 42.01           N  
-ATOM   9005  CD2 HIS D 180      51.050  16.757  45.206  1.00 40.77           C  
-ATOM   9006  CE1 HIS D 180      50.643  14.735  45.950  1.00 41.79           C  
-ATOM   9007  NE2 HIS D 180      50.613  16.015  46.276  1.00 41.35           N  
-ATOM   9008  N   PRO D 181      49.499  18.838  41.627  1.00 31.19           N  
-ATOM   9009  CA  PRO D 181      49.183  20.251  41.854  1.00 29.38           C  
-ATOM   9010  C   PRO D 181      49.036  20.594  43.327  1.00 28.87           C  
-ATOM   9011  O   PRO D 181      48.537  19.791  44.111  1.00 29.05           O  
-ATOM   9012  CB  PRO D 181      47.898  20.449  41.048  1.00 27.70           C  
-ATOM   9013  CG  PRO D 181      47.266  19.095  41.082  1.00 26.63           C  
-ATOM   9014  CD  PRO D 181      48.436  18.186  40.841  1.00 27.41           C  
-ATOM   9015  N   ARG D 182      49.475  21.795  43.688  1.00 29.95           N  
-ATOM   9016  CA  ARG D 182      49.440  22.254  45.071  1.00 32.01           C  
-ATOM   9017  C   ARG D 182      48.476  23.409  45.310  1.00 31.07           C  
-ATOM   9018  O   ARG D 182      48.409  23.944  46.416  1.00 33.01           O  
-ATOM   9019  CB  ARG D 182      50.849  22.673  45.502  1.00 35.65           C  
-ATOM   9020  CG  ARG D 182      51.887  21.563  45.383  1.00 39.70           C  
-ATOM   9021  CD  ARG D 182      51.836  20.632  46.578  1.00 45.23           C  
-ATOM   9022  NE  ARG D 182      52.401  21.257  47.774  1.00 48.29           N  
-ATOM   9023  CZ  ARG D 182      52.274  20.768  49.006  1.00 52.49           C  
-ATOM   9024  NH1 ARG D 182      51.595  19.642  49.212  1.00 51.82           N  
-ATOM   9025  NH2 ARG D 182      52.825  21.403  50.035  1.00 53.49           N  
-ATOM   9026  N   SER D 183      47.744  23.810  44.277  1.00 29.65           N  
-ATOM   9027  CA  SER D 183      46.780  24.895  44.420  1.00 27.69           C  
-ATOM   9028  C   SER D 183      45.605  24.684  43.483  1.00 27.72           C  
-ATOM   9029  O   SER D 183      45.660  23.839  42.591  1.00 27.92           O  
-ATOM   9030  CB  SER D 183      47.432  26.247  44.112  1.00 26.84           C  
-ATOM   9031  OG  SER D 183      47.895  26.308  42.775  1.00 27.71           O  
-ATOM   9032  N   PRO D 184      44.512  25.434  43.692  1.00 27.34           N  
-ATOM   9033  CA  PRO D 184      43.340  25.297  42.824  1.00 26.05           C  
-ATOM   9034  C   PRO D 184      43.731  25.674  41.396  1.00 26.46           C  
-ATOM   9035  O   PRO D 184      43.300  25.038  40.435  1.00 26.25           O  
-ATOM   9036  CB  PRO D 184      42.349  26.278  43.435  1.00 27.03           C  
-ATOM   9037  CG  PRO D 184      42.689  26.209  44.901  1.00 28.06           C  
-ATOM   9038  CD  PRO D 184      44.198  26.267  44.869  1.00 27.40           C  
-ATOM   9039  N   TYR D 185      44.555  26.711  41.272  1.00 24.44           N  
-ATOM   9040  CA  TYR D 185      45.030  27.164  39.971  1.00 24.61           C  
-ATOM   9041  C   TYR D 185      45.764  26.038  39.241  1.00 24.91           C  
-ATOM   9042  O   TYR D 185      45.493  25.762  38.080  1.00 26.65           O  
-ATOM   9043  CB  TYR D 185      45.990  28.340  40.133  1.00 24.10           C  
-ATOM   9044  CG  TYR D 185      46.822  28.608  38.890  1.00 25.30           C  
-ATOM   9045  CD1 TYR D 185      46.294  29.318  37.813  1.00 24.84           C  
-ATOM   9046  CD2 TYR D 185      48.133  28.133  38.787  1.00 26.18           C  
-ATOM   9047  CE1 TYR D 185      47.047  29.553  36.665  1.00 24.99           C  
-ATOM   9048  CE2 TYR D 185      48.898  28.359  37.642  1.00 24.36           C  
-ATOM   9049  CZ  TYR D 185      48.347  29.070  36.583  1.00 26.30           C  
-ATOM   9050  OH  TYR D 185      49.081  29.280  35.434  1.00 24.84           O  
-ATOM   9051  N   ALA D 186      46.703  25.399  39.931  1.00 24.38           N  
-ATOM   9052  CA  ALA D 186      47.490  24.319  39.348  1.00 23.75           C  
-ATOM   9053  C   ALA D 186      46.624  23.126  38.971  1.00 24.21           C  
-ATOM   9054  O   ALA D 186      46.790  22.549  37.902  1.00 26.66           O  
-ATOM   9055  CB  ALA D 186      48.577  23.889  40.319  1.00 21.41           C  
-ATOM   9056  N   ALA D 187      45.703  22.760  39.853  1.00 23.26           N  
-ATOM   9057  CA  ALA D 187      44.813  21.638  39.602  1.00 23.52           C  
-ATOM   9058  C   ALA D 187      43.957  21.942  38.370  1.00 24.56           C  
-ATOM   9059  O   ALA D 187      43.705  21.068  37.538  1.00 25.84           O  
-ATOM   9060  CB  ALA D 187      43.932  21.400  40.814  1.00 22.59           C  
-ATOM   9061  N   SER D 188      43.523  23.190  38.255  1.00 23.65           N  
-ATOM   9062  CA  SER D 188      42.713  23.609  37.126  1.00 22.80           C  
-ATOM   9063  C   SER D 188      43.515  23.544  35.822  1.00 23.66           C  
-ATOM   9064  O   SER D 188      42.974  23.183  34.772  1.00 21.25           O  
-ATOM   9065  CB  SER D 188      42.180  25.023  37.367  1.00 22.03           C  
-ATOM   9066  OG  SER D 188      41.247  25.033  38.438  1.00 21.63           O  
-ATOM   9067  N   LYS D 189      44.798  23.896  35.881  1.00 22.79           N  
-ATOM   9068  CA  LYS D 189      45.632  23.828  34.687  1.00 23.31           C  
-ATOM   9069  C   LYS D 189      45.810  22.366  34.283  1.00 23.23           C  
-ATOM   9070  O   LYS D 189      45.856  22.041  33.094  1.00 25.48           O  
-ATOM   9071  CB  LYS D 189      47.000  24.474  34.927  1.00 23.32           C  
-ATOM   9072  CG  LYS D 189      47.023  25.991  34.784  1.00 23.96           C  
-ATOM   9073  CD  LYS D 189      46.786  26.429  33.345  1.00 24.40           C  
-ATOM   9074  CE  LYS D 189      46.840  27.949  33.215  1.00 25.71           C  
-ATOM   9075  NZ  LYS D 189      46.492  28.426  31.845  1.00 25.74           N  
-ATOM   9076  N   CYS D 190      45.901  21.485  35.274  1.00 22.61           N  
-ATOM   9077  CA  CYS D 190      46.054  20.058  35.005  1.00 25.08           C  
-ATOM   9078  C   CYS D 190      44.830  19.558  34.241  1.00 26.01           C  
-ATOM   9079  O   CYS D 190      44.947  18.770  33.305  1.00 28.01           O  
-ATOM   9080  CB  CYS D 190      46.202  19.269  36.314  1.00 24.01           C  
-ATOM   9081  SG  CYS D 190      47.770  19.543  37.186  1.00 26.01           S  
-ATOM   9082  N   ALA D 191      43.655  20.024  34.656  1.00 25.80           N  
-ATOM   9083  CA  ALA D 191      42.407  19.645  34.015  1.00 25.19           C  
-ATOM   9084  C   ALA D 191      42.412  20.143  32.570  1.00 23.47           C  
-ATOM   9085  O   ALA D 191      42.101  19.394  31.646  1.00 23.86           O  
-ATOM   9086  CB  ALA D 191      41.226  20.249  34.782  1.00 24.72           C  
-ATOM   9087  N   ALA D 192      42.768  21.412  32.388  1.00 23.00           N  
-ATOM   9088  CA  ALA D 192      42.816  22.013  31.062  1.00 23.89           C  
-ATOM   9089  C   ALA D 192      43.795  21.250  30.181  1.00 24.37           C  
-ATOM   9090  O   ALA D 192      43.539  21.024  28.998  1.00 23.08           O  
-ATOM   9091  CB  ALA D 192      43.227  23.472  31.163  1.00 24.99           C  
-ATOM   9092  N   HIS D 193      44.919  20.856  30.769  1.00 25.02           N  
-ATOM   9093  CA  HIS D 193      45.935  20.103  30.053  1.00 25.23           C  
-ATOM   9094  C   HIS D 193      45.321  18.804  29.529  1.00 27.00           C  
-ATOM   9095  O   HIS D 193      45.480  18.445  28.356  1.00 25.91           O  
-ATOM   9096  CB  HIS D 193      47.087  19.769  30.994  1.00 25.82           C  
-ATOM   9097  CG  HIS D 193      48.162  18.947  30.361  1.00 25.16           C  
-ATOM   9098  ND1 HIS D 193      49.224  19.506  29.684  1.00 23.95           N  
-ATOM   9099  CD2 HIS D 193      48.324  17.606  30.277  1.00 22.14           C  
-ATOM   9100  CE1 HIS D 193      49.995  18.544  29.210  1.00 23.29           C  
-ATOM   9101  NE2 HIS D 193      49.471  17.382  29.556  1.00 23.71           N  
-ATOM   9102  N   TRP D 194      44.613  18.101  30.407  1.00 26.62           N  
-ATOM   9103  CA  TRP D 194      43.990  16.846  30.022  1.00 28.44           C  
-ATOM   9104  C   TRP D 194      42.819  16.975  29.057  1.00 26.62           C  
-ATOM   9105  O   TRP D 194      42.635  16.106  28.211  1.00 25.16           O  
-ATOM   9106  CB  TRP D 194      43.587  16.057  31.261  1.00 28.32           C  
-ATOM   9107  CG  TRP D 194      44.767  15.381  31.870  1.00 32.32           C  
-ATOM   9108  CD1 TRP D 194      45.236  15.531  33.142  1.00 32.80           C  
-ATOM   9109  CD2 TRP D 194      45.650  14.458  31.222  1.00 33.63           C  
-ATOM   9110  NE1 TRP D 194      46.358  14.759  33.326  1.00 33.05           N  
-ATOM   9111  CE2 TRP D 194      46.634  14.090  32.163  1.00 33.18           C  
-ATOM   9112  CE3 TRP D 194      45.704  13.902  29.934  1.00 35.44           C  
-ATOM   9113  CZ2 TRP D 194      47.664  13.190  31.859  1.00 35.88           C  
-ATOM   9114  CZ3 TRP D 194      46.729  13.004  29.631  1.00 34.56           C  
-ATOM   9115  CH2 TRP D 194      47.693  12.660  30.592  1.00 35.69           C  
-ATOM   9116  N   TYR D 195      42.031  18.043  29.172  1.00 26.04           N  
-ATOM   9117  CA  TYR D 195      40.921  18.238  28.241  1.00 25.09           C  
-ATOM   9118  C   TYR D 195      41.522  18.398  26.842  1.00 25.75           C  
-ATOM   9119  O   TYR D 195      41.012  17.860  25.865  1.00 26.94           O  
-ATOM   9120  CB  TYR D 195      40.133  19.505  28.583  1.00 26.45           C  
-ATOM   9121  CG  TYR D 195      39.313  19.437  29.852  1.00 24.48           C  
-ATOM   9122  CD1 TYR D 195      39.181  20.559  30.669  1.00 25.72           C  
-ATOM   9123  CD2 TYR D 195      38.664  18.265  30.233  1.00 25.96           C  
-ATOM   9124  CE1 TYR D 195      38.426  20.516  31.839  1.00 23.62           C  
-ATOM   9125  CE2 TYR D 195      37.900  18.211  31.403  1.00 26.32           C  
-ATOM   9126  CZ  TYR D 195      37.792  19.345  32.199  1.00 25.33           C  
-ATOM   9127  OH  TYR D 195      37.059  19.310  33.357  1.00 25.82           O  
-ATOM   9128  N   THR D 196      42.617  19.150  26.769  1.00 25.69           N  
-ATOM   9129  CA  THR D 196      43.308  19.418  25.515  1.00 26.15           C  
-ATOM   9130  C   THR D 196      43.873  18.134  24.917  1.00 27.67           C  
-ATOM   9131  O   THR D 196      43.685  17.859  23.731  1.00 27.62           O  
-ATOM   9132  CB  THR D 196      44.451  20.428  25.727  1.00 26.23           C  
-ATOM   9133  OG1 THR D 196      43.925  21.611  26.342  1.00 25.07           O  
-ATOM   9134  CG2 THR D 196      45.098  20.801  24.395  1.00 24.10           C  
-ATOM   9135  N   VAL D 197      44.568  17.354  25.737  1.00 27.46           N  
-ATOM   9136  CA  VAL D 197      45.129  16.099  25.273  1.00 28.15           C  
-ATOM   9137  C   VAL D 197      43.988  15.224  24.768  1.00 29.57           C  
-ATOM   9138  O   VAL D 197      44.087  14.617  23.700  1.00 29.68           O  
-ATOM   9139  CB  VAL D 197      45.883  15.349  26.407  1.00 29.24           C  
-ATOM   9140  CG1 VAL D 197      46.212  13.923  25.967  1.00 27.16           C  
-ATOM   9141  CG2 VAL D 197      47.179  16.082  26.757  1.00 26.51           C  
-ATOM   9142  N   ASN D 198      42.899  15.181  25.531  1.00 28.65           N  
-ATOM   9143  CA  ASN D 198      41.749  14.369  25.164  1.00 28.53           C  
-ATOM   9144  C   ASN D 198      41.169  14.740  23.797  1.00 29.21           C  
-ATOM   9145  O   ASN D 198      40.826  13.864  23.008  1.00 27.75           O  
-ATOM   9146  CB  ASN D 198      40.653  14.479  26.223  1.00 28.75           C  
-ATOM   9147  CG  ASN D 198      39.529  13.479  25.999  1.00 30.28           C  
-ATOM   9148  OD1 ASN D 198      38.355  13.811  26.130  1.00 31.61           O  
-ATOM   9149  ND2 ASN D 198      39.889  12.243  25.665  1.00 29.40           N  
-ATOM   9150  N   TYR D 199      41.047  16.034  23.520  1.00 29.23           N  
-ATOM   9151  CA  TYR D 199      40.513  16.471  22.238  1.00 29.18           C  
-ATOM   9152  C   TYR D 199      41.452  16.103  21.097  1.00 29.75           C  
-ATOM   9153  O   TYR D 199      41.026  15.923  19.962  1.00 31.08           O  
-ATOM   9154  CB  TYR D 199      40.250  17.980  22.258  1.00 28.81           C  
-ATOM   9155  CG  TYR D 199      38.837  18.297  22.678  1.00 30.83           C  
-ATOM   9156  CD1 TYR D 199      38.315  17.778  23.865  1.00 29.66           C  
-ATOM   9157  CD2 TYR D 199      37.993  19.041  21.855  1.00 30.12           C  
-ATOM   9158  CE1 TYR D 199      36.990  17.979  24.216  1.00 30.82           C  
-ATOM   9159  CE2 TYR D 199      36.658  19.249  22.198  1.00 31.63           C  
-ATOM   9160  CZ  TYR D 199      36.167  18.709  23.381  1.00 31.31           C  
-ATOM   9161  OH  TYR D 199      34.850  18.878  23.725  1.00 30.12           O  
-ATOM   9162  N   ARG D 200      42.732  15.984  21.410  1.00 30.18           N  
-ATOM   9163  CA  ARG D 200      43.724  15.616  20.414  1.00 30.24           C  
-ATOM   9164  C   ARG D 200      43.551  14.133  20.079  1.00 29.43           C  
-ATOM   9165  O   ARG D 200      43.389  13.764  18.923  1.00 30.53           O  
-ATOM   9166  CB  ARG D 200      45.136  15.878  20.962  1.00 28.36           C  
-ATOM   9167  CG  ARG D 200      46.276  15.494  20.020  1.00 28.67           C  
-ATOM   9168  CD  ARG D 200      47.614  16.000  20.551  1.00 29.32           C  
-ATOM   9169  NE  ARG D 200      48.079  15.251  21.717  1.00 31.42           N  
-ATOM   9170  CZ  ARG D 200      48.744  15.788  22.738  1.00 29.29           C  
-ATOM   9171  NH1 ARG D 200      49.023  17.087  22.754  1.00 28.90           N  
-ATOM   9172  NH2 ARG D 200      49.145  15.022  23.738  1.00 29.35           N  
-ATOM   9173  N   GLU D 201      43.565  13.296  21.108  1.00 29.46           N  
-ATOM   9174  CA  GLU D 201      43.438  11.856  20.936  1.00 31.01           C  
-ATOM   9175  C   GLU D 201      42.053  11.384  20.501  1.00 31.73           C  
-ATOM   9176  O   GLU D 201      41.929  10.378  19.804  1.00 32.54           O  
-ATOM   9177  CB  GLU D 201      43.840  11.145  22.236  1.00 28.77           C  
-ATOM   9178  CG  GLU D 201      45.307  11.326  22.597  1.00 29.27           C  
-ATOM   9179  CD  GLU D 201      45.678  10.713  23.937  1.00 30.55           C  
-ATOM   9180  OE1 GLU D 201      46.866  10.791  24.320  1.00 33.21           O  
-ATOM   9181  OE2 GLU D 201      44.790  10.154  24.611  1.00 33.82           O  
-ATOM   9182  N   ALA D 202      41.015  12.112  20.897  1.00 31.66           N  
-ATOM   9183  CA  ALA D 202      39.654  11.727  20.555  1.00 30.95           C  
-ATOM   9184  C   ALA D 202      39.185  12.216  19.191  1.00 32.80           C  
-ATOM   9185  O   ALA D 202      38.547  11.473  18.450  1.00 33.37           O  
-ATOM   9186  CB  ALA D 202      38.693  12.213  21.635  1.00 28.90           C  
-ATOM   9187  N   TYR D 203      39.500  13.462  18.853  1.00 33.11           N  
-ATOM   9188  CA  TYR D 203      39.054  14.019  17.586  1.00 32.94           C  
-ATOM   9189  C   TYR D 203      40.170  14.326  16.605  1.00 33.12           C  
-ATOM   9190  O   TYR D 203      39.914  14.726  15.469  1.00 33.22           O  
-ATOM   9191  CB  TYR D 203      38.243  15.286  17.846  1.00 33.20           C  
-ATOM   9192  CG  TYR D 203      37.126  15.081  18.843  1.00 34.63           C  
-ATOM   9193  CD1 TYR D 203      37.237  15.549  20.154  1.00 34.24           C  
-ATOM   9194  CD2 TYR D 203      35.962  14.408  18.479  1.00 34.32           C  
-ATOM   9195  CE1 TYR D 203      36.211  15.354  21.077  1.00 34.78           C  
-ATOM   9196  CE2 TYR D 203      34.933  14.205  19.393  1.00 35.41           C  
-ATOM   9197  CZ  TYR D 203      35.062  14.680  20.688  1.00 36.03           C  
-ATOM   9198  OH  TYR D 203      34.040  14.474  21.585  1.00 37.96           O  
-ATOM   9199  N   GLY D 204      41.408  14.135  17.039  1.00 33.42           N  
-ATOM   9200  CA  GLY D 204      42.527  14.419  16.164  1.00 35.03           C  
-ATOM   9201  C   GLY D 204      42.703  15.910  15.962  1.00 34.59           C  
-ATOM   9202  O   GLY D 204      43.243  16.348  14.950  1.00 34.14           O  
-ATOM   9203  N   LEU D 205      42.229  16.702  16.918  1.00 34.94           N  
-ATOM   9204  CA  LEU D 205      42.378  18.149  16.816  1.00 33.61           C  
-ATOM   9205  C   LEU D 205      43.856  18.461  16.986  1.00 33.11           C  
-ATOM   9206  O   LEU D 205      44.547  17.811  17.772  1.00 31.91           O  
-ATOM   9207  CB  LEU D 205      41.581  18.859  17.912  1.00 32.57           C  
-ATOM   9208  CG  LEU D 205      41.763  20.380  17.971  1.00 34.69           C  
-ATOM   9209  CD1 LEU D 205      41.144  21.020  16.731  1.00 32.70           C  
-ATOM   9210  CD2 LEU D 205      41.115  20.938  19.239  1.00 35.38           C  
-ATOM   9211  N   PHE D 206      44.350  19.445  16.244  1.00 32.26           N  
-ATOM   9212  CA  PHE D 206      45.752  19.808  16.362  1.00 32.59           C  
-ATOM   9213  C   PHE D 206      45.900  20.683  17.611  1.00 32.59           C  
-ATOM   9214  O   PHE D 206      46.011  21.908  17.518  1.00 31.86           O  
-ATOM   9215  CB  PHE D 206      46.216  20.560  15.106  1.00 32.58           C  
-ATOM   9216  CG  PHE D 206      47.710  20.619  14.955  1.00 32.18           C  
-ATOM   9217  CD1 PHE D 206      48.486  21.372  15.831  1.00 33.91           C  
-ATOM   9218  CD2 PHE D 206      48.347  19.887  13.957  1.00 34.71           C  
-ATOM   9219  CE1 PHE D 206      49.878  21.395  15.720  1.00 32.85           C  
-ATOM   9220  CE2 PHE D 206      49.737  19.900  13.835  1.00 33.74           C  
-ATOM   9221  CZ  PHE D 206      50.504  20.656  14.721  1.00 34.39           C  
-ATOM   9222  N   ALA D 207      45.899  20.043  18.779  1.00 32.52           N  
-ATOM   9223  CA  ALA D 207      46.013  20.758  20.049  1.00 31.96           C  
-ATOM   9224  C   ALA D 207      47.325  20.477  20.765  1.00 31.64           C  
-ATOM   9225  O   ALA D 207      47.635  19.331  21.087  1.00 33.01           O  
-ATOM   9226  CB  ALA D 207      44.852  20.394  20.950  1.00 29.63           C  
-ATOM   9227  N   CYS D 208      48.085  21.536  21.026  1.00 32.80           N  
-ATOM   9228  CA  CYS D 208      49.368  21.415  21.707  1.00 32.65           C  
-ATOM   9229  C   CYS D 208      49.326  22.014  23.103  1.00 32.84           C  
-ATOM   9230  O   CYS D 208      48.718  23.062  23.318  1.00 34.09           O  
-ATOM   9231  CB  CYS D 208      50.465  22.133  20.919  1.00 33.55           C  
-ATOM   9232  SG  CYS D 208      50.767  21.516  19.257  1.00 35.94           S  
-ATOM   9233  N   ASN D 209      49.982  21.348  24.046  1.00 33.01           N  
-ATOM   9234  CA  ASN D 209      50.062  21.838  25.418  1.00 31.00           C  
-ATOM   9235  C   ASN D 209      51.471  22.360  25.674  1.00 29.30           C  
-ATOM   9236  O   ASN D 209      52.431  21.589  25.694  1.00 28.66           O  
-ATOM   9237  CB  ASN D 209      49.777  20.722  26.429  1.00 29.79           C  
-ATOM   9238  CG  ASN D 209      48.305  20.388  26.543  1.00 29.69           C  
-ATOM   9239  OD1 ASN D 209      47.501  21.197  27.014  1.00 31.27           O  
-ATOM   9240  ND2 ASN D 209      47.944  19.187  26.120  1.00 27.64           N  
-ATOM   9241  N   GLY D 210      51.594  23.669  25.856  1.00 28.66           N  
-ATOM   9242  CA  GLY D 210      52.889  24.244  26.162  1.00 27.26           C  
-ATOM   9243  C   GLY D 210      53.040  24.233  27.674  1.00 27.50           C  
-ATOM   9244  O   GLY D 210      52.335  24.951  28.372  1.00 28.20           O  
-ATOM   9245  N   ILE D 211      53.930  23.397  28.193  1.00 28.53           N  
-ATOM   9246  CA  ILE D 211      54.146  23.331  29.633  1.00 27.57           C  
-ATOM   9247  C   ILE D 211      55.265  24.313  29.938  1.00 29.45           C  
-ATOM   9248  O   ILE D 211      56.439  23.938  30.006  1.00 28.66           O  
-ATOM   9249  CB  ILE D 211      54.553  21.910  30.073  1.00 29.18           C  
-ATOM   9250  CG1 ILE D 211      53.476  20.911  29.628  1.00 28.65           C  
-ATOM   9251  CG2 ILE D 211      54.720  21.853  31.593  1.00 25.62           C  
-ATOM   9252  CD1 ILE D 211      53.882  19.458  29.752  1.00 28.77           C  
-ATOM   9253  N   LEU D 212      54.892  25.579  30.105  1.00 26.66           N  
-ATOM   9254  CA  LEU D 212      55.869  26.626  30.359  1.00 28.32           C  
-ATOM   9255  C   LEU D 212      56.188  26.922  31.817  1.00 28.30           C  
-ATOM   9256  O   LEU D 212      55.309  26.972  32.681  1.00 29.20           O  
-ATOM   9257  CB  LEU D 212      55.443  27.924  29.653  1.00 27.69           C  
-ATOM   9258  CG  LEU D 212      55.728  27.974  28.145  1.00 28.00           C  
-ATOM   9259  CD1 LEU D 212      55.021  26.822  27.451  1.00 28.23           C  
-ATOM   9260  CD2 LEU D 212      55.278  29.312  27.561  1.00 25.61           C  
-ATOM   9261  N   PHE D 213      57.476  27.103  32.078  1.00 28.86           N  
-ATOM   9262  CA  PHE D 213      57.941  27.435  33.406  1.00 28.12           C  
-ATOM   9263  C   PHE D 213      57.872  28.949  33.505  1.00 27.57           C  
-ATOM   9264  O   PHE D 213      57.563  29.621  32.526  1.00 28.38           O  
-ATOM   9265  CB  PHE D 213      59.366  26.916  33.615  1.00 28.18           C  
-ATOM   9266  CG  PHE D 213      59.422  25.456  33.955  1.00 28.16           C  
-ATOM   9267  CD1 PHE D 213      58.950  24.503  33.060  1.00 29.04           C  
-ATOM   9268  CD2 PHE D 213      59.895  25.036  35.194  1.00 29.26           C  
-ATOM   9269  CE1 PHE D 213      58.941  23.151  33.395  1.00 31.93           C  
-ATOM   9270  CE2 PHE D 213      59.891  23.684  35.539  1.00 29.11           C  
-ATOM   9271  CZ  PHE D 213      59.412  22.742  34.637  1.00 29.22           C  
-ATOM   9272  N   ASN D 214      58.143  29.487  34.683  1.00 28.50           N  
-ATOM   9273  CA  ASN D 214      58.072  30.927  34.896  1.00 29.49           C  
-ATOM   9274  C   ASN D 214      58.809  31.776  33.867  1.00 29.42           C  
-ATOM   9275  O   ASN D 214      59.982  31.545  33.586  1.00 29.23           O  
-ATOM   9276  CB  ASN D 214      58.610  31.273  36.286  1.00 29.66           C  
-ATOM   9277  CG  ASN D 214      57.846  30.583  37.399  1.00 32.57           C  
-ATOM   9278  OD1 ASN D 214      57.631  29.374  37.358  1.00 35.76           O  
-ATOM   9279  ND2 ASN D 214      57.445  31.346  38.408  1.00 32.57           N  
-ATOM   9280  N   HIS D 215      58.112  32.752  33.296  1.00 28.74           N  
-ATOM   9281  CA  HIS D 215      58.743  33.674  32.362  1.00 28.61           C  
-ATOM   9282  C   HIS D 215      58.335  35.085  32.748  1.00 27.40           C  
-ATOM   9283  O   HIS D 215      57.174  35.345  33.069  1.00 26.33           O  
-ATOM   9284  CB  HIS D 215      58.397  33.376  30.897  1.00 28.04           C  
-ATOM   9285  CG  HIS D 215      56.983  32.958  30.667  1.00 29.23           C  
-ATOM   9286  ND1 HIS D 215      56.494  31.737  31.076  1.00 27.76           N  
-ATOM   9287  CD2 HIS D 215      55.965  33.578  30.027  1.00 29.34           C  
-ATOM   9288  CE1 HIS D 215      55.235  31.621  30.694  1.00 29.40           C  
-ATOM   9289  NE2 HIS D 215      54.891  32.723  30.055  1.00 29.84           N  
-ATOM   9290  N   GLU D 216      59.315  35.982  32.733  1.00 27.65           N  
-ATOM   9291  CA  GLU D 216      59.122  37.365  33.135  1.00 27.91           C  
-ATOM   9292  C   GLU D 216      59.449  38.333  32.015  1.00 29.61           C  
-ATOM   9293  O   GLU D 216      59.911  37.935  30.942  1.00 32.25           O  
-ATOM   9294  CB  GLU D 216      60.018  37.665  34.339  1.00 28.86           C  
-ATOM   9295  CG  GLU D 216      60.245  36.458  35.248  1.00 28.76           C  
-ATOM   9296  CD  GLU D 216      58.960  35.943  35.867  1.00 28.32           C  
-ATOM   9297  OE1 GLU D 216      58.721  34.718  35.823  1.00 30.96           O  
-ATOM   9298  OE2 GLU D 216      58.190  36.762  36.407  1.00 31.00           O  
-ATOM   9299  N   SER D 217      59.226  39.612  32.283  1.00 28.81           N  
-ATOM   9300  CA  SER D 217      59.480  40.653  31.308  1.00 29.92           C  
-ATOM   9301  C   SER D 217      59.135  41.986  31.940  1.00 29.83           C  
-ATOM   9302  O   SER D 217      58.659  42.040  33.073  1.00 30.02           O  
-ATOM   9303  CB  SER D 217      58.587  40.458  30.088  1.00 29.27           C  
-ATOM   9304  OG  SER D 217      57.266  40.898  30.369  1.00 28.79           O  
-ATOM   9305  N   PRO D 218      59.390  43.086  31.218  1.00 30.56           N  
-ATOM   9306  CA  PRO D 218      59.079  44.419  31.736  1.00 29.25           C  
-ATOM   9307  C   PRO D 218      57.566  44.603  31.850  1.00 29.15           C  
-ATOM   9308  O   PRO D 218      57.103  45.557  32.469  1.00 29.50           O  
-ATOM   9309  CB  PRO D 218      59.683  45.345  30.684  1.00 29.32           C  
-ATOM   9310  CG  PRO D 218      60.866  44.574  30.208  1.00 29.81           C  
-ATOM   9311  CD  PRO D 218      60.291  43.179  30.054  1.00 29.40           C  
-ATOM   9312  N   ARG D 219      56.804  43.688  31.249  1.00 29.15           N  
-ATOM   9313  CA  ARG D 219      55.337  43.759  31.278  1.00 29.00           C  
-ATOM   9314  C   ARG D 219      54.719  42.758  32.256  1.00 27.35           C  
-ATOM   9315  O   ARG D 219      53.504  42.604  32.314  1.00 28.43           O  
-ATOM   9316  CB  ARG D 219      54.760  43.515  29.881  1.00 26.90           C  
-ATOM   9317  CG  ARG D 219      55.391  44.359  28.790  1.00 29.47           C  
-ATOM   9318  CD  ARG D 219      54.868  43.955  27.416  1.00 32.24           C  
-ATOM   9319  NE  ARG D 219      55.663  44.534  26.337  1.00 31.95           N  
-ATOM   9320  CZ  ARG D 219      55.530  44.212  25.053  1.00 33.79           C  
-ATOM   9321  NH1 ARG D 219      56.300  44.792  24.141  1.00 33.53           N  
-ATOM   9322  NH2 ARG D 219      54.631  43.308  24.679  1.00 31.24           N  
-ATOM   9323  N   ARG D 220      55.563  42.072  33.013  1.00 27.63           N  
-ATOM   9324  CA  ARG D 220      55.100  41.108  34.000  1.00 29.98           C  
-ATOM   9325  C   ARG D 220      54.238  41.832  35.042  1.00 30.36           C  
-ATOM   9326  O   ARG D 220      54.539  42.963  35.428  1.00 30.09           O  
-ATOM   9327  CB  ARG D 220      56.312  40.454  34.672  1.00 29.97           C  
-ATOM   9328  CG  ARG D 220      56.002  39.436  35.750  1.00 31.86           C  
-ATOM   9329  CD  ARG D 220      55.226  38.230  35.229  1.00 32.21           C  
-ATOM   9330  NE  ARG D 220      55.657  37.004  35.902  1.00 32.44           N  
-ATOM   9331  CZ  ARG D 220      54.934  35.889  35.984  1.00 32.86           C  
-ATOM   9332  NH1 ARG D 220      53.727  35.832  35.442  1.00 32.54           N  
-ATOM   9333  NH2 ARG D 220      55.427  34.825  36.602  1.00 34.49           N  
-ATOM   9334  N   GLY D 221      53.153  41.193  35.474  1.00 31.32           N  
-ATOM   9335  CA  GLY D 221      52.292  41.803  36.475  1.00 31.99           C  
-ATOM   9336  C   GLY D 221      53.100  42.203  37.696  1.00 31.96           C  
-ATOM   9337  O   GLY D 221      53.992  41.471  38.131  1.00 29.29           O  
-ATOM   9338  N   GLU D 222      52.800  43.368  38.255  1.00 34.56           N  
-ATOM   9339  CA  GLU D 222      53.532  43.846  39.421  1.00 39.66           C  
-ATOM   9340  C   GLU D 222      53.317  42.991  40.671  1.00 40.80           C  
-ATOM   9341  O   GLU D 222      54.022  43.151  41.667  1.00 42.01           O  
-ATOM   9342  CB  GLU D 222      53.178  45.315  39.694  1.00 39.92           C  
-ATOM   9343  CG  GLU D 222      53.814  46.270  38.679  1.00 42.12           C  
-ATOM   9344  CD  GLU D 222      53.423  47.729  38.876  1.00 43.78           C  
-ATOM   9345  OE1 GLU D 222      53.531  48.234  40.017  1.00 43.07           O  
-ATOM   9346  OE2 GLU D 222      53.019  48.372  37.880  1.00 43.21           O  
-ATOM   9347  N   ASN D 223      52.354  42.076  40.607  1.00 42.97           N  
-ATOM   9348  CA  ASN D 223      52.062  41.194  41.729  1.00 45.46           C  
-ATOM   9349  C   ASN D 223      52.971  39.971  41.727  1.00 45.43           C  
-ATOM   9350  O   ASN D 223      52.751  39.026  42.487  1.00 45.57           O  
-ATOM   9351  CB  ASN D 223      50.601  40.739  41.695  1.00 48.42           C  
-ATOM   9352  CG  ASN D 223      49.631  41.875  41.951  1.00 52.12           C  
-ATOM   9353  OD1 ASN D 223      49.694  42.539  42.987  1.00 54.38           O  
-ATOM   9354  ND2 ASN D 223      48.723  42.106  41.006  1.00 54.24           N  
-ATOM   9355  N   PHE D 224      53.983  39.981  40.865  1.00 44.26           N  
-ATOM   9356  CA  PHE D 224      54.927  38.874  40.805  1.00 42.84           C  
-ATOM   9357  C   PHE D 224      56.286  39.342  41.315  1.00 42.46           C  
-ATOM   9358  O   PHE D 224      56.699  40.476  41.075  1.00 41.11           O  
-ATOM   9359  CB  PHE D 224      55.031  38.323  39.380  1.00 41.39           C  
-ATOM   9360  CG  PHE D 224      53.751  37.719  38.877  1.00 40.11           C  
-ATOM   9361  CD1 PHE D 224      52.822  38.492  38.185  1.00 41.00           C  
-ATOM   9362  CD2 PHE D 224      53.449  36.387  39.139  1.00 40.30           C  
-ATOM   9363  CE1 PHE D 224      51.607  37.949  37.762  1.00 40.30           C  
-ATOM   9364  CE2 PHE D 224      52.235  35.831  38.722  1.00 40.31           C  
-ATOM   9365  CZ  PHE D 224      51.313  36.613  38.033  1.00 40.79           C  
-ATOM   9366  N   VAL D 225      56.972  38.461  42.032  1.00 43.84           N  
-ATOM   9367  CA  VAL D 225      58.265  38.785  42.623  1.00 44.71           C  
-ATOM   9368  C   VAL D 225      59.254  39.546  41.737  1.00 44.28           C  
-ATOM   9369  O   VAL D 225      59.761  40.597  42.132  1.00 45.63           O  
-ATOM   9370  CB  VAL D 225      58.946  37.508  43.158  1.00 46.91           C  
-ATOM   9371  CG1 VAL D 225      59.080  36.484  42.044  1.00 48.48           C  
-ATOM   9372  CG2 VAL D 225      60.302  37.850  43.751  1.00 47.16           C  
-ATOM   9373  N   THR D 226      59.532  39.028  40.547  1.00 43.61           N  
-ATOM   9374  CA  THR D 226      60.488  39.679  39.659  1.00 41.63           C  
-ATOM   9375  C   THR D 226      60.114  41.114  39.325  1.00 40.34           C  
-ATOM   9376  O   THR D 226      60.958  42.007  39.394  1.00 41.77           O  
-ATOM   9377  CB  THR D 226      60.663  38.897  38.339  1.00 41.74           C  
-ATOM   9378  OG1 THR D 226      59.413  38.849  37.639  1.00 41.13           O  
-ATOM   9379  CG2 THR D 226      61.139  37.480  38.620  1.00 39.76           C  
-ATOM   9380  N   ARG D 227      58.857  41.343  38.962  1.00 39.76           N  
-ATOM   9381  CA  ARG D 227      58.423  42.690  38.612  1.00 39.11           C  
-ATOM   9382  C   ARG D 227      58.296  43.575  39.848  1.00 40.30           C  
-ATOM   9383  O   ARG D 227      58.508  44.787  39.781  1.00 39.74           O  
-ATOM   9384  CB  ARG D 227      57.086  42.652  37.871  1.00 37.22           C  
-ATOM   9385  CG  ARG D 227      56.645  44.015  37.358  1.00 37.42           C  
-ATOM   9386  CD  ARG D 227      57.577  44.520  36.264  1.00 36.49           C  
-ATOM   9387  NE  ARG D 227      57.398  45.947  35.997  1.00 37.79           N  
-ATOM   9388  CZ  ARG D 227      56.283  46.502  35.531  1.00 36.58           C  
-ATOM   9389  NH1 ARG D 227      55.218  45.756  35.266  1.00 37.23           N  
-ATOM   9390  NH2 ARG D 227      56.233  47.812  35.332  1.00 36.70           N  
-ATOM   9391  N   LYS D 228      57.946  42.965  40.976  1.00 41.64           N  
-ATOM   9392  CA  LYS D 228      57.805  43.702  42.228  1.00 43.38           C  
-ATOM   9393  C   LYS D 228      59.137  44.357  42.588  1.00 42.93           C  
-ATOM   9394  O   LYS D 228      59.186  45.517  42.996  1.00 45.99           O  
-ATOM   9395  CB  LYS D 228      57.359  42.751  43.344  1.00 43.51           C  
-ATOM   9396  CG  LYS D 228      57.083  43.422  44.677  1.00 45.18           C  
-ATOM   9397  CD  LYS D 228      56.477  42.426  45.656  1.00 47.94           C  
-ATOM   9398  CE  LYS D 228      56.179  43.063  47.006  1.00 50.18           C  
-ATOM   9399  NZ  LYS D 228      55.615  42.074  47.975  1.00 51.35           N  
-ATOM   9400  N   ILE D 229      60.219  43.609  42.407  1.00 41.89           N  
-ATOM   9401  CA  ILE D 229      61.561  44.091  42.701  1.00 40.83           C  
-ATOM   9402  C   ILE D 229      62.024  45.219  41.767  1.00 42.75           C  
-ATOM   9403  O   ILE D 229      62.414  46.301  42.222  1.00 43.42           O  
-ATOM   9404  CB  ILE D 229      62.564  42.923  42.618  1.00 41.64           C  
-ATOM   9405  CG1 ILE D 229      62.239  41.895  43.709  1.00 41.68           C  
-ATOM   9406  CG2 ILE D 229      63.988  43.441  42.731  1.00 41.92           C  
-ATOM   9407  CD1 ILE D 229      63.121  40.678  43.696  1.00 43.52           C  
-ATOM   9408  N   THR D 230      61.980  44.970  40.464  1.00 41.16           N  
-ATOM   9409  CA  THR D 230      62.418  45.966  39.498  1.00 41.03           C  
-ATOM   9410  C   THR D 230      61.584  47.242  39.545  1.00 41.43           C  
-ATOM   9411  O   THR D 230      62.088  48.328  39.250  1.00 42.38           O  
-ATOM   9412  CB  THR D 230      62.395  45.397  38.062  1.00 41.29           C  
-ATOM   9413  OG1 THR D 230      61.051  45.070  37.692  1.00 39.84           O  
-ATOM   9414  CG2 THR D 230      63.261  44.140  37.980  1.00 40.41           C  
-ATOM   9415  N   ARG D 231      60.313  47.118  39.912  1.00 41.27           N  
-ATOM   9416  CA  ARG D 231      59.444  48.286  39.995  1.00 41.58           C  
-ATOM   9417  C   ARG D 231      59.944  49.196  41.121  1.00 42.26           C  
-ATOM   9418  O   ARG D 231      60.043  50.411  40.953  1.00 41.42           O  
-ATOM   9419  CB  ARG D 231      58.001  47.861  40.274  1.00 40.81           C  
-ATOM   9420  CG  ARG D 231      56.983  48.979  40.111  1.00 41.13           C  
-ATOM   9421  CD  ARG D 231      56.833  49.378  38.653  1.00 42.23           C  
-ATOM   9422  NE  ARG D 231      55.745  50.336  38.451  1.00 46.90           N  
-ATOM   9423  CZ  ARG D 231      55.854  51.655  38.600  1.00 47.49           C  
-ATOM   9424  NH1 ARG D 231      57.013  52.200  38.952  1.00 47.14           N  
-ATOM   9425  NH2 ARG D 231      54.796  52.433  38.403  1.00 46.93           N  
-ATOM   9426  N   ALA D 232      60.264  48.592  42.263  1.00 42.03           N  
-ATOM   9427  CA  ALA D 232      60.770  49.328  43.419  1.00 43.30           C  
-ATOM   9428  C   ALA D 232      62.094  50.020  43.085  1.00 44.02           C  
-ATOM   9429  O   ALA D 232      62.223  51.238  43.240  1.00 44.43           O  
-ATOM   9430  CB  ALA D 232      60.964  48.377  44.601  1.00 41.96           C  
-ATOM   9431  N   LEU D 233      63.071  49.237  42.631  1.00 43.44           N  
-ATOM   9432  CA  LEU D 233      64.381  49.766  42.275  1.00 43.44           C  
-ATOM   9433  C   LEU D 233      64.257  51.059  41.471  1.00 45.38           C  
-ATOM   9434  O   LEU D 233      64.860  52.073  41.817  1.00 44.86           O  
-ATOM   9435  CB  LEU D 233      65.166  48.725  41.469  1.00 44.01           C  
-ATOM   9436  CG  LEU D 233      66.525  49.140  40.886  1.00 45.30           C  
-ATOM   9437  CD1 LEU D 233      67.462  49.585  41.999  1.00 44.40           C  
-ATOM   9438  CD2 LEU D 233      67.130  47.973  40.116  1.00 44.76           C  
-ATOM   9439  N   GLY D 234      63.473  51.020  40.397  1.00 46.90           N  
-ATOM   9440  CA  GLY D 234      63.294  52.204  39.575  1.00 47.45           C  
-ATOM   9441  C   GLY D 234      62.784  53.364  40.407  1.00 48.91           C  
-ATOM   9442  O   GLY D 234      63.231  54.503  40.255  1.00 49.13           O  
-ATOM   9443  N   ARG D 235      61.842  53.065  41.295  1.00 49.82           N  
-ATOM   9444  CA  ARG D 235      61.258  54.068  42.170  1.00 49.13           C  
-ATOM   9445  C   ARG D 235      62.315  54.598  43.137  1.00 49.28           C  
-ATOM   9446  O   ARG D 235      62.432  55.808  43.338  1.00 49.04           O  
-ATOM   9447  CB  ARG D 235      60.088  53.465  42.938  1.00 49.16           C  
-ATOM   9448  N   ILE D 236      63.089  53.690  43.726  1.00 48.40           N  
-ATOM   9449  CA  ILE D 236      64.136  54.075  44.667  1.00 47.63           C  
-ATOM   9450  C   ILE D 236      65.164  54.982  43.996  1.00 47.80           C  
-ATOM   9451  O   ILE D 236      65.477  56.062  44.500  1.00 47.57           O  
-ATOM   9452  CB  ILE D 236      64.848  52.833  45.244  1.00 46.60           C  
-ATOM   9453  CG1 ILE D 236      63.835  51.976  46.009  1.00 46.21           C  
-ATOM   9454  CG2 ILE D 236      65.994  53.261  46.154  1.00 44.83           C  
-ATOM   9455  CD1 ILE D 236      64.416  50.728  46.634  1.00 46.83           C  
-ATOM   9456  N   LYS D 237      65.682  54.541  42.856  1.00 49.45           N  
-ATOM   9457  CA  LYS D 237      66.665  55.320  42.114  1.00 51.55           C  
-ATOM   9458  C   LYS D 237      66.145  56.737  41.866  1.00 53.17           C  
-ATOM   9459  O   LYS D 237      66.858  57.716  42.088  1.00 54.62           O  
-ATOM   9460  CB  LYS D 237      66.978  54.635  40.787  1.00 50.78           C  
-ATOM   9461  N   VAL D 238      64.901  56.842  41.409  1.00 54.16           N  
-ATOM   9462  CA  VAL D 238      64.295  58.141  41.135  1.00 54.60           C  
-ATOM   9463  C   VAL D 238      64.101  58.919  42.433  1.00 54.74           C  
-ATOM   9464  O   VAL D 238      63.896  60.135  42.415  1.00 54.67           O  
-ATOM   9465  CB  VAL D 238      62.950  57.958  40.427  1.00 53.87           C  
-ATOM   9466  N   GLY D 239      64.166  58.209  43.557  1.00 53.97           N  
-ATOM   9467  CA  GLY D 239      63.993  58.847  44.849  1.00 53.65           C  
-ATOM   9468  C   GLY D 239      62.534  58.986  45.246  1.00 54.11           C  
-ATOM   9469  O   GLY D 239      62.209  59.704  46.194  1.00 53.89           O  
-ATOM   9470  N   LEU D 240      61.657  58.292  44.523  1.00 54.04           N  
-ATOM   9471  CA  LEU D 240      60.221  58.333  44.791  1.00 52.87           C  
-ATOM   9472  C   LEU D 240      59.803  57.295  45.824  1.00 52.98           C  
-ATOM   9473  O   LEU D 240      58.709  57.382  46.385  1.00 53.68           O  
-ATOM   9474  CB  LEU D 240      59.439  58.119  43.498  1.00 51.32           C  
-ATOM   9475  N   GLN D 241      60.666  56.313  46.073  1.00 52.50           N  
-ATOM   9476  CA  GLN D 241      60.355  55.271  47.047  1.00 53.04           C  
-ATOM   9477  C   GLN D 241      61.486  55.092  48.048  1.00 53.81           C  
-ATOM   9478  O   GLN D 241      62.655  55.320  47.730  1.00 53.92           O  
-ATOM   9479  CB  GLN D 241      60.074  53.940  46.347  1.00 52.48           C  
-ATOM   9480  CG  GLN D 241      59.328  52.947  47.225  1.00 51.96           C  
-ATOM   9481  CD  GLN D 241      58.914  51.696  46.478  1.00 51.60           C  
-ATOM   9482  OE1 GLN D 241      58.512  51.758  45.315  1.00 49.87           O  
-ATOM   9483  NE2 GLN D 241      58.993  50.554  47.150  1.00 51.47           N  
-ATOM   9484  N   THR D 242      61.128  54.675  49.259  1.00 54.68           N  
-ATOM   9485  CA  THR D 242      62.104  54.484  50.323  1.00 55.96           C  
-ATOM   9486  C   THR D 242      62.519  53.032  50.525  1.00 55.78           C  
-ATOM   9487  O   THR D 242      63.689  52.694  50.360  1.00 56.37           O  
-ATOM   9488  CB  THR D 242      61.560  55.054  51.635  1.00 55.21           C  
-ATOM   9489  N   LYS D 243      61.565  52.178  50.883  1.00 55.47           N  
-ATOM   9490  CA  LYS D 243      61.870  50.773  51.129  1.00 56.18           C  
-ATOM   9491  C   LYS D 243      61.205  49.801  50.158  1.00 57.48           C  
-ATOM   9492  O   LYS D 243      60.217  50.133  49.496  1.00 58.61           O  
-ATOM   9493  CB  LYS D 243      61.490  50.409  52.560  1.00 54.97           C  
-ATOM   9494  N   LEU D 244      61.764  48.595  50.086  1.00 56.81           N  
-ATOM   9495  CA  LEU D 244      61.246  47.536  49.226  1.00 55.28           C  
-ATOM   9496  C   LEU D 244      60.945  46.303  50.080  1.00 54.25           C  
-ATOM   9497  O   LEU D 244      61.842  45.744  50.714  1.00 54.34           O  
-ATOM   9498  CB  LEU D 244      62.268  47.191  48.143  1.00 54.36           C  
-ATOM   9499  N   PHE D 245      59.683  45.888  50.104  1.00 52.68           N  
-ATOM   9500  CA  PHE D 245      59.287  44.717  50.880  1.00 51.60           C  
-ATOM   9501  C   PHE D 245      59.957  43.471  50.317  1.00 51.10           C  
-ATOM   9502  O   PHE D 245      60.160  42.487  51.027  1.00 51.49           O  
-ATOM   9503  CB  PHE D 245      57.771  44.556  50.850  1.00 51.10           C  
-ATOM   9504  N   ALA D 251      62.166  28.761  48.121  1.00 58.23           N  
-ATOM   9505  CA  ALA D 251      61.873  28.309  46.766  1.00 58.36           C  
-ATOM   9506  C   ALA D 251      62.639  29.133  45.733  1.00 58.77           C  
-ATOM   9507  O   ALA D 251      62.678  30.363  45.811  1.00 60.23           O  
-ATOM   9508  CB  ALA D 251      60.373  28.403  46.501  1.00 57.55           C  
-ATOM   9509  N   SER D 252      63.258  28.449  44.773  1.00 58.37           N  
-ATOM   9510  CA  SER D 252      64.012  29.116  43.712  1.00 56.13           C  
-ATOM   9511  C   SER D 252      63.258  28.856  42.420  1.00 54.87           C  
-ATOM   9512  O   SER D 252      62.375  27.992  42.381  1.00 54.90           O  
-ATOM   9513  CB  SER D 252      65.432  28.549  43.614  1.00 56.26           C  
-ATOM   9514  OG  SER D 252      66.196  29.260  42.656  1.00 54.93           O  
-ATOM   9515  N   ARG D 253      63.591  29.584  41.360  1.00 53.00           N  
-ATOM   9516  CA  ARG D 253      62.875  29.382  40.107  1.00 49.48           C  
-ATOM   9517  C   ARG D 253      63.664  29.474  38.808  1.00 45.37           C  
-ATOM   9518  O   ARG D 253      64.769  30.019  38.751  1.00 44.61           O  
-ATOM   9519  CB  ARG D 253      61.676  30.339  40.037  1.00 51.13           C  
-ATOM   9520  CG  ARG D 253      60.498  29.919  40.904  1.00 51.45           C  
-ATOM   9521  CD  ARG D 253      59.881  28.612  40.400  1.00 54.27           C  
-ATOM   9522  NE  ARG D 253      58.883  28.075  41.325  1.00 55.60           N  
-ATOM   9523  CZ  ARG D 253      57.729  28.668  41.621  1.00 56.72           C  
-ATOM   9524  NH1 ARG D 253      56.892  28.100  42.480  1.00 56.76           N  
-ATOM   9525  NH2 ARG D 253      57.405  29.823  41.056  1.00 57.40           N  
-ATOM   9526  N   ASP D 254      63.062  28.904  37.769  1.00 41.12           N  
-ATOM   9527  CA  ASP D 254      63.612  28.895  36.425  1.00 37.89           C  
-ATOM   9528  C   ASP D 254      62.901  30.039  35.716  1.00 35.89           C  
-ATOM   9529  O   ASP D 254      61.759  29.886  35.288  1.00 37.06           O  
-ATOM   9530  CB  ASP D 254      63.298  27.545  35.754  1.00 35.13           C  
-ATOM   9531  CG  ASP D 254      63.686  27.499  34.277  1.00 35.50           C  
-ATOM   9532  OD1 ASP D 254      63.892  26.379  33.756  1.00 33.55           O  
-ATOM   9533  OD2 ASP D 254      63.770  28.566  33.628  1.00 33.92           O  
-ATOM   9534  N   TRP D 255      63.565  31.189  35.621  1.00 35.36           N  
-ATOM   9535  CA  TRP D 255      62.978  32.360  34.968  1.00 34.78           C  
-ATOM   9536  C   TRP D 255      63.481  32.567  33.548  1.00 32.82           C  
-ATOM   9537  O   TRP D 255      64.682  32.634  33.314  1.00 31.39           O  
-ATOM   9538  CB  TRP D 255      63.266  33.638  35.763  1.00 37.13           C  
-ATOM   9539  CG  TRP D 255      62.541  33.747  37.070  1.00 41.09           C  
-ATOM   9540  CD1 TRP D 255      61.203  33.568  37.290  1.00 41.28           C  
-ATOM   9541  CD2 TRP D 255      63.114  34.082  38.339  1.00 41.80           C  
-ATOM   9542  NE1 TRP D 255      60.909  33.769  38.619  1.00 43.28           N  
-ATOM   9543  CE2 TRP D 255      62.064  34.085  39.285  1.00 42.65           C  
-ATOM   9544  CE3 TRP D 255      64.415  34.382  38.768  1.00 42.83           C  
-ATOM   9545  CZ2 TRP D 255      62.274  34.375  40.637  1.00 43.70           C  
-ATOM   9546  CZ3 TRP D 255      64.623  34.672  40.115  1.00 43.42           C  
-ATOM   9547  CH2 TRP D 255      63.557  34.665  41.032  1.00 43.06           C  
-ATOM   9548  N   GLY D 256      62.546  32.676  32.609  1.00 30.78           N  
-ATOM   9549  CA  GLY D 256      62.900  32.901  31.222  1.00 28.54           C  
-ATOM   9550  C   GLY D 256      62.247  34.193  30.774  1.00 29.67           C  
-ATOM   9551  O   GLY D 256      61.484  34.792  31.526  1.00 28.12           O  
-ATOM   9552  N   PHE D 257      62.547  34.626  29.554  1.00 30.41           N  
-ATOM   9553  CA  PHE D 257      61.980  35.851  29.007  1.00 29.41           C  
-ATOM   9554  C   PHE D 257      60.714  35.543  28.226  1.00 29.48           C  
-ATOM   9555  O   PHE D 257      60.725  34.706  27.324  1.00 31.74           O  
-ATOM   9556  CB  PHE D 257      62.993  36.531  28.087  1.00 29.06           C  
-ATOM   9557  CG  PHE D 257      62.442  37.717  27.343  1.00 29.17           C  
-ATOM   9558  CD1 PHE D 257      61.772  38.733  28.021  1.00 27.90           C  
-ATOM   9559  CD2 PHE D 257      62.624  37.835  25.970  1.00 27.03           C  
-ATOM   9560  CE1 PHE D 257      61.292  39.855  27.342  1.00 27.46           C  
-ATOM   9561  CE2 PHE D 257      62.150  38.951  25.281  1.00 27.45           C  
-ATOM   9562  CZ  PHE D 257      61.482  39.964  25.968  1.00 27.76           C  
-ATOM   9563  N   ALA D 258      59.626  36.224  28.571  1.00 29.73           N  
-ATOM   9564  CA  ALA D 258      58.344  36.018  27.902  1.00 30.15           C  
-ATOM   9565  C   ALA D 258      58.460  36.118  26.380  1.00 30.31           C  
-ATOM   9566  O   ALA D 258      57.751  35.422  25.655  1.00 30.06           O  
-ATOM   9567  CB  ALA D 258      57.318  37.031  28.417  1.00 31.07           C  
-ATOM   9568  N   GLY D 259      59.350  36.983  25.901  1.00 30.36           N  
-ATOM   9569  CA  GLY D 259      59.526  37.144  24.466  1.00 29.83           C  
-ATOM   9570  C   GLY D 259      59.983  35.868  23.782  1.00 29.88           C  
-ATOM   9571  O   GLY D 259      59.526  35.544  22.684  1.00 29.48           O  
-ATOM   9572  N   ASP D 260      60.888  35.146  24.440  1.00 28.68           N  
-ATOM   9573  CA  ASP D 260      61.426  33.891  23.928  1.00 30.07           C  
-ATOM   9574  C   ASP D 260      60.376  32.790  23.939  1.00 31.47           C  
-ATOM   9575  O   ASP D 260      60.240  32.038  22.970  1.00 33.35           O  
-ATOM   9576  CB  ASP D 260      62.611  33.423  24.784  1.00 27.96           C  
-ATOM   9577  CG  ASP D 260      63.857  34.263  24.582  1.00 33.21           C  
-ATOM   9578  OD1 ASP D 260      64.756  34.209  25.453  1.00 33.63           O  
-ATOM   9579  OD2 ASP D 260      63.947  34.968  23.554  1.00 35.13           O  
-ATOM   9580  N   TYR D 261      59.640  32.696  25.041  1.00 29.62           N  
-ATOM   9581  CA  TYR D 261      58.632  31.656  25.200  1.00 30.85           C  
-ATOM   9582  C   TYR D 261      57.450  31.688  24.241  1.00 30.40           C  
-ATOM   9583  O   TYR D 261      56.953  30.629  23.854  1.00 30.91           O  
-ATOM   9584  CB  TYR D 261      58.133  31.638  26.647  1.00 29.80           C  
-ATOM   9585  CG  TYR D 261      59.152  31.106  27.639  1.00 30.07           C  
-ATOM   9586  CD1 TYR D 261      60.516  31.344  27.468  1.00 30.36           C  
-ATOM   9587  CD2 TYR D 261      58.748  30.394  28.769  1.00 30.15           C  
-ATOM   9588  CE1 TYR D 261      61.451  30.887  28.396  1.00 30.61           C  
-ATOM   9589  CE2 TYR D 261      59.670  29.937  29.706  1.00 30.41           C  
-ATOM   9590  CZ  TYR D 261      61.020  30.186  29.515  1.00 31.47           C  
-ATOM   9591  OH  TYR D 261      61.936  29.743  30.446  1.00 31.15           O  
-ATOM   9592  N   VAL D 262      56.992  32.873  23.844  1.00 30.25           N  
-ATOM   9593  CA  VAL D 262      55.853  32.930  22.925  1.00 30.04           C  
-ATOM   9594  C   VAL D 262      56.254  32.418  21.552  1.00 30.77           C  
-ATOM   9595  O   VAL D 262      55.417  31.961  20.779  1.00 32.76           O  
-ATOM   9596  CB  VAL D 262      55.278  34.357  22.790  1.00 29.07           C  
-ATOM   9597  CG1 VAL D 262      54.755  34.820  24.132  1.00 29.49           C  
-ATOM   9598  CG2 VAL D 262      56.334  35.310  22.259  1.00 29.33           C  
-ATOM   9599  N   GLU D 263      57.546  32.491  21.259  1.00 32.59           N  
-ATOM   9600  CA  GLU D 263      58.067  32.017  19.983  1.00 34.12           C  
-ATOM   9601  C   GLU D 263      57.965  30.492  19.954  1.00 33.44           C  
-ATOM   9602  O   GLU D 263      57.685  29.891  18.916  1.00 31.43           O  
-ATOM   9603  CB  GLU D 263      59.518  32.465  19.827  1.00 37.42           C  
-ATOM   9604  CG  GLU D 263      60.215  31.932  18.587  1.00 44.23           C  
-ATOM   9605  CD  GLU D 263      61.543  32.620  18.339  1.00 46.33           C  
-ATOM   9606  OE1 GLU D 263      62.315  32.132  17.487  1.00 48.81           O  
-ATOM   9607  OE2 GLU D 263      61.809  33.655  18.994  1.00 47.23           O  
-ATOM   9608  N   ALA D 264      58.178  29.878  21.114  1.00 32.18           N  
-ATOM   9609  CA  ALA D 264      58.094  28.432  21.254  1.00 32.11           C  
-ATOM   9610  C   ALA D 264      56.643  27.993  21.085  1.00 32.46           C  
-ATOM   9611  O   ALA D 264      56.370  26.903  20.582  1.00 34.04           O  
-ATOM   9612  CB  ALA D 264      58.620  28.012  22.626  1.00 32.14           C  
-ATOM   9613  N   MET D 265      55.717  28.849  21.515  1.00 32.33           N  
-ATOM   9614  CA  MET D 265      54.289  28.568  21.398  1.00 32.02           C  
-ATOM   9615  C   MET D 265      53.960  28.446  19.919  1.00 31.99           C  
-ATOM   9616  O   MET D 265      53.297  27.511  19.482  1.00 31.93           O  
-ATOM   9617  CB  MET D 265      53.458  29.712  21.989  1.00 31.20           C  
-ATOM   9618  CG  MET D 265      53.661  29.972  23.472  1.00 32.68           C  
-ATOM   9619  SD  MET D 265      52.575  31.296  24.047  1.00 31.73           S  
-ATOM   9620  CE  MET D 265      52.910  31.278  25.805  1.00 33.78           C  
-ATOM   9621  N   TRP D 266      54.433  29.421  19.157  1.00 32.19           N  
-ATOM   9622  CA  TRP D 266      54.217  29.458  17.723  1.00 33.47           C  
-ATOM   9623  C   TRP D 266      54.891  28.277  17.024  1.00 33.39           C  
-ATOM   9624  O   TRP D 266      54.316  27.679  16.115  1.00 31.94           O  
-ATOM   9625  CB  TRP D 266      54.764  30.768  17.161  1.00 33.71           C  
-ATOM   9626  CG  TRP D 266      54.668  30.867  15.690  1.00 35.04           C  
-ATOM   9627  CD1 TRP D 266      53.542  31.084  14.954  1.00 35.28           C  
-ATOM   9628  CD2 TRP D 266      55.745  30.745  14.757  1.00 35.78           C  
-ATOM   9629  NE1 TRP D 266      53.851  31.109  13.614  1.00 38.07           N  
-ATOM   9630  CE2 TRP D 266      55.198  30.903  13.465  1.00 37.79           C  
-ATOM   9631  CE3 TRP D 266      57.120  30.516  14.886  1.00 36.66           C  
-ATOM   9632  CZ2 TRP D 266      55.980  30.839  12.307  1.00 37.58           C  
-ATOM   9633  CZ3 TRP D 266      57.896  30.452  13.737  1.00 36.94           C  
-ATOM   9634  CH2 TRP D 266      57.322  30.613  12.464  1.00 37.15           C  
-ATOM   9635  N   LEU D 267      56.111  27.948  17.443  1.00 33.94           N  
-ATOM   9636  CA  LEU D 267      56.839  26.838  16.836  1.00 33.68           C  
-ATOM   9637  C   LEU D 267      56.077  25.530  17.005  1.00 34.40           C  
-ATOM   9638  O   LEU D 267      56.070  24.685  16.112  1.00 34.10           O  
-ATOM   9639  CB  LEU D 267      58.232  26.705  17.453  1.00 33.28           C  
-ATOM   9640  CG  LEU D 267      59.267  27.761  17.064  1.00 34.96           C  
-ATOM   9641  CD1 LEU D 267      60.540  27.552  17.870  1.00 33.91           C  
-ATOM   9642  CD2 LEU D 267      59.558  27.666  15.575  1.00 34.51           C  
-ATOM   9643  N   MET D 268      55.439  25.366  18.159  1.00 33.98           N  
-ATOM   9644  CA  MET D 268      54.671  24.162  18.440  1.00 33.41           C  
-ATOM   9645  C   MET D 268      53.576  23.933  17.409  1.00 33.41           C  
-ATOM   9646  O   MET D 268      53.318  22.805  16.996  1.00 33.54           O  
-ATOM   9647  CB  MET D 268      54.035  24.254  19.827  1.00 33.58           C  
-ATOM   9648  CG  MET D 268      55.010  24.101  20.973  1.00 32.88           C  
-ATOM   9649  SD  MET D 268      54.163  24.196  22.550  1.00 32.98           S  
-ATOM   9650  CE  MET D 268      55.267  25.282  23.438  1.00 31.03           C  
-ATOM   9651  N   LEU D 269      52.931  25.012  16.993  1.00 33.58           N  
-ATOM   9652  CA  LEU D 269      51.849  24.916  16.027  1.00 34.94           C  
-ATOM   9653  C   LEU D 269      52.302  24.834  14.569  1.00 36.19           C  
-ATOM   9654  O   LEU D 269      51.465  24.745  13.667  1.00 34.44           O  
-ATOM   9655  CB  LEU D 269      50.887  26.094  16.219  1.00 31.49           C  
-ATOM   9656  CG  LEU D 269      49.706  25.841  17.166  1.00 31.23           C  
-ATOM   9657  CD1 LEU D 269      50.190  25.239  18.475  1.00 31.64           C  
-ATOM   9658  CD2 LEU D 269      48.958  27.142  17.403  1.00 27.71           C  
-ATOM   9659  N   GLN D 270      53.613  24.852  14.336  1.00 36.96           N  
-ATOM   9660  CA  GLN D 270      54.130  24.782  12.968  1.00 39.97           C  
-ATOM   9661  C   GLN D 270      54.647  23.389  12.624  1.00 39.84           C  
-ATOM   9662  O   GLN D 270      54.997  23.116  11.477  1.00 40.23           O  
-ATOM   9663  CB  GLN D 270      55.256  25.805  12.747  1.00 39.72           C  
-ATOM   9664  CG  GLN D 270      54.914  27.233  13.139  1.00 41.28           C  
-ATOM   9665  CD  GLN D 270      53.572  27.690  12.602  1.00 43.74           C  
-ATOM   9666  OE1 GLN D 270      53.338  27.692  11.391  1.00 43.58           O  
-ATOM   9667  NE2 GLN D 270      52.679  28.085  13.507  1.00 43.75           N  
-ATOM   9668  N   GLN D 271      54.697  22.511  13.618  1.00 40.27           N  
-ATOM   9669  CA  GLN D 271      55.171  21.151  13.396  1.00 40.50           C  
-ATOM   9670  C   GLN D 271      54.155  20.350  12.584  1.00 41.24           C  
-ATOM   9671  O   GLN D 271      53.032  20.805  12.356  1.00 40.67           O  
-ATOM   9672  CB  GLN D 271      55.429  20.465  14.738  1.00 39.15           C  
-ATOM   9673  CG  GLN D 271      56.396  21.224  15.628  1.00 40.10           C  
-ATOM   9674  CD  GLN D 271      57.685  21.573  14.913  1.00 41.46           C  
-ATOM   9675  OE1 GLN D 271      58.366  20.697  14.382  1.00 43.94           O  
-ATOM   9676  NE2 GLN D 271      58.028  22.858  14.893  1.00 41.01           N  
-ATOM   9677  N   GLU D 272      54.552  19.157  12.147  1.00 43.34           N  
-ATOM   9678  CA  GLU D 272      53.673  18.297  11.357  1.00 44.11           C  
-ATOM   9679  C   GLU D 272      52.568  17.696  12.218  1.00 43.05           C  
-ATOM   9680  O   GLU D 272      51.425  17.587  11.783  1.00 44.18           O  
-ATOM   9681  CB  GLU D 272      54.471  17.158  10.706  1.00 47.14           C  
-ATOM   9682  CG  GLU D 272      55.513  17.594   9.674  1.00 51.39           C  
-ATOM   9683  CD  GLU D 272      54.911  18.391   8.528  1.00 54.65           C  
-ATOM   9684  OE1 GLU D 272      53.872  17.958   7.981  1.00 56.14           O  
-ATOM   9685  OE2 GLU D 272      55.481  19.446   8.170  1.00 55.02           O  
-ATOM   9686  N   LYS D 273      52.917  17.302  13.438  1.00 41.26           N  
-ATOM   9687  CA  LYS D 273      51.953  16.696  14.354  1.00 40.73           C  
-ATOM   9688  C   LYS D 273      51.836  17.487  15.655  1.00 39.54           C  
-ATOM   9689  O   LYS D 273      52.781  18.148  16.079  1.00 38.46           O  
-ATOM   9690  CB  LYS D 273      52.375  15.263  14.696  1.00 42.47           C  
-ATOM   9691  CG  LYS D 273      52.450  14.301  13.523  1.00 43.58           C  
-ATOM   9692  CD  LYS D 273      52.921  12.929  13.999  1.00 45.67           C  
-ATOM   9693  CE  LYS D 273      52.930  11.901  12.875  1.00 46.38           C  
-ATOM   9694  NZ  LYS D 273      53.465  10.586  13.341  1.00 47.37           N  
-ATOM   9695  N   PRO D 274      50.665  17.427  16.305  1.00 38.52           N  
-ATOM   9696  CA  PRO D 274      50.460  18.145  17.565  1.00 36.69           C  
-ATOM   9697  C   PRO D 274      51.148  17.393  18.700  1.00 36.19           C  
-ATOM   9698  O   PRO D 274      51.206  16.167  18.684  1.00 36.37           O  
-ATOM   9699  CB  PRO D 274      48.942  18.151  17.709  1.00 36.24           C  
-ATOM   9700  CG  PRO D 274      48.551  16.848  17.094  1.00 37.42           C  
-ATOM   9701  CD  PRO D 274      49.410  16.802  15.846  1.00 38.95           C  
-ATOM   9702  N   ASP D 275      51.670  18.117  19.684  1.00 35.27           N  
-ATOM   9703  CA  ASP D 275      52.348  17.470  20.801  1.00 33.67           C  
-ATOM   9704  C   ASP D 275      52.422  18.408  22.007  1.00 33.40           C  
-ATOM   9705  O   ASP D 275      52.024  19.573  21.929  1.00 32.95           O  
-ATOM   9706  CB  ASP D 275      53.761  17.060  20.369  1.00 34.97           C  
-ATOM   9707  CG  ASP D 275      54.290  15.850  21.132  1.00 36.57           C  
-ATOM   9708  OD1 ASP D 275      55.357  15.339  20.742  1.00 38.02           O  
-ATOM   9709  OD2 ASP D 275      53.654  15.409  22.116  1.00 37.83           O  
-ATOM   9710  N   ASP D 276      52.931  17.887  23.119  1.00 31.43           N  
-ATOM   9711  CA  ASP D 276      53.081  18.664  24.340  1.00 31.64           C  
-ATOM   9712  C   ASP D 276      54.569  18.917  24.543  1.00 32.83           C  
-ATOM   9713  O   ASP D 276      55.391  18.031  24.294  1.00 32.73           O  
-ATOM   9714  CB  ASP D 276      52.502  17.892  25.522  1.00 30.31           C  
-ATOM   9715  CG  ASP D 276      51.094  17.412  25.252  1.00 30.76           C  
-ATOM   9716  OD1 ASP D 276      50.288  18.235  24.778  1.00 31.90           O  
-ATOM   9717  OD2 ASP D 276      50.793  16.224  25.504  1.00 31.63           O  
-ATOM   9718  N   TYR D 277      54.920  20.122  24.982  1.00 32.66           N  
-ATOM   9719  CA  TYR D 277      56.323  20.458  25.175  1.00 31.65           C  
-ATOM   9720  C   TYR D 277      56.612  21.300  26.407  1.00 32.40           C  
-ATOM   9721  O   TYR D 277      55.904  22.266  26.701  1.00 32.50           O  
-ATOM   9722  CB  TYR D 277      56.872  21.236  23.976  1.00 32.05           C  
-ATOM   9723  CG  TYR D 277      56.583  20.671  22.605  1.00 32.19           C  
-ATOM   9724  CD1 TYR D 277      55.345  20.861  21.998  1.00 32.19           C  
-ATOM   9725  CD2 TYR D 277      57.574  20.007  21.885  1.00 33.10           C  
-ATOM   9726  CE1 TYR D 277      55.103  20.413  20.701  1.00 33.29           C  
-ATOM   9727  CE2 TYR D 277      57.342  19.551  20.589  1.00 31.53           C  
-ATOM   9728  CZ  TYR D 277      56.109  19.760  20.002  1.00 34.18           C  
-ATOM   9729  OH  TYR D 277      55.890  19.345  18.709  1.00 34.15           O  
-ATOM   9730  N   VAL D 278      57.677  20.938  27.110  1.00 31.98           N  
-ATOM   9731  CA  VAL D 278      58.113  21.690  28.275  1.00 32.41           C  
-ATOM   9732  C   VAL D 278      59.027  22.798  27.752  1.00 32.52           C  
-ATOM   9733  O   VAL D 278      59.907  22.548  26.925  1.00 32.58           O  
-ATOM   9734  CB  VAL D 278      58.910  20.800  29.263  1.00 32.47           C  
-ATOM   9735  CG1 VAL D 278      59.676  21.671  30.257  1.00 32.55           C  
-ATOM   9736  CG2 VAL D 278      57.962  19.864  30.003  1.00 28.23           C  
-ATOM   9737  N   VAL D 279      58.793  24.023  28.210  1.00 32.02           N  
-ATOM   9738  CA  VAL D 279      59.606  25.163  27.806  1.00 30.73           C  
-ATOM   9739  C   VAL D 279      60.178  25.792  29.070  1.00 32.68           C  
-ATOM   9740  O   VAL D 279      59.431  26.274  29.930  1.00 32.88           O  
-ATOM   9741  CB  VAL D 279      58.773  26.206  27.045  1.00 30.53           C  
-ATOM   9742  CG1 VAL D 279      59.632  27.418  26.701  1.00 29.51           C  
-ATOM   9743  CG2 VAL D 279      58.210  25.583  25.781  1.00 30.27           C  
-ATOM   9744  N   ALA D 280      61.503  25.765  29.179  1.00 31.60           N  
-ATOM   9745  CA  ALA D 280      62.208  26.307  30.332  1.00 32.62           C  
-ATOM   9746  C   ALA D 280      63.659  26.601  29.965  1.00 32.71           C  
-ATOM   9747  O   ALA D 280      64.128  26.200  28.903  1.00 31.94           O  
-ATOM   9748  CB  ALA D 280      62.155  25.309  31.477  1.00 31.53           C  
-ATOM   9749  N   THR D 281      64.367  27.310  30.840  1.00 34.06           N  
-ATOM   9750  CA  THR D 281      65.773  27.624  30.587  1.00 34.22           C  
-ATOM   9751  C   THR D 281      66.649  26.509  31.166  1.00 35.74           C  
-ATOM   9752  O   THR D 281      67.813  26.357  30.790  1.00 35.42           O  
-ATOM   9753  CB  THR D 281      66.188  28.968  31.239  1.00 33.41           C  
-ATOM   9754  OG1 THR D 281      66.095  28.862  32.666  1.00 32.05           O  
-ATOM   9755  CG2 THR D 281      65.289  30.101  30.755  1.00 31.25           C  
-ATOM   9756  N   GLU D 282      66.065  25.737  32.080  1.00 36.93           N  
-ATOM   9757  CA  GLU D 282      66.735  24.623  32.748  1.00 38.78           C  
-ATOM   9758  C   GLU D 282      67.781  25.094  33.752  1.00 40.25           C  
-ATOM   9759  O   GLU D 282      68.554  24.297  34.279  1.00 41.18           O  
-ATOM   9760  CB  GLU D 282      67.378  23.691  31.719  1.00 37.91           C  
-ATOM   9761  CG  GLU D 282      66.399  23.159  30.684  1.00 38.21           C  
-ATOM   9762  CD  GLU D 282      67.039  22.178  29.717  1.00 37.21           C  
-ATOM   9763  OE1 GLU D 282      68.107  22.500  29.160  1.00 40.13           O  
-ATOM   9764  OE2 GLU D 282      66.471  21.088  29.505  1.00 35.18           O  
-ATOM   9765  N   GLU D 283      67.794  26.394  34.020  1.00 41.89           N  
-ATOM   9766  CA  GLU D 283      68.735  26.971  34.969  1.00 43.06           C  
-ATOM   9767  C   GLU D 283      67.980  27.605  36.130  1.00 44.70           C  
-ATOM   9768  O   GLU D 283      66.800  27.938  36.011  1.00 44.87           O  
-ATOM   9769  CB  GLU D 283      69.604  28.015  34.277  1.00 41.37           C  
-ATOM   9770  N   GLY D 284      68.664  27.773  37.255  1.00 46.25           N  
-ATOM   9771  CA  GLY D 284      68.030  28.371  38.414  1.00 46.61           C  
-ATOM   9772  C   GLY D 284      68.749  29.613  38.902  1.00 46.68           C  
-ATOM   9773  O   GLY D 284      69.922  29.832  38.599  1.00 46.76           O  
-ATOM   9774  N   HIS D 285      68.031  30.435  39.656  1.00 47.32           N  
-ATOM   9775  CA  HIS D 285      68.581  31.660  40.217  1.00 47.19           C  
-ATOM   9776  C   HIS D 285      67.734  32.036  41.425  1.00 47.35           C  
-ATOM   9777  O   HIS D 285      66.581  31.613  41.536  1.00 46.88           O  
-ATOM   9778  CB  HIS D 285      68.562  32.784  39.175  1.00 48.09           C  
-ATOM   9779  CG  HIS D 285      69.547  32.594  38.062  1.00 48.08           C  
-ATOM   9780  ND1 HIS D 285      70.903  32.775  38.230  1.00 48.54           N  
-ATOM   9781  CD2 HIS D 285      69.376  32.210  36.775  1.00 46.93           C  
-ATOM   9782  CE1 HIS D 285      71.525  32.512  37.094  1.00 46.72           C  
-ATOM   9783  NE2 HIS D 285      70.621  32.167  36.195  1.00 45.70           N  
-ATOM   9784  N   THR D 286      68.307  32.826  42.329  1.00 47.70           N  
-ATOM   9785  CA  THR D 286      67.600  33.237  43.538  1.00 47.04           C  
-ATOM   9786  C   THR D 286      67.179  34.701  43.507  1.00 46.27           C  
-ATOM   9787  O   THR D 286      67.735  35.511  42.764  1.00 45.59           O  
-ATOM   9788  CB  THR D 286      68.478  33.056  44.784  1.00 47.14           C  
-ATOM   9789  OG1 THR D 286      69.407  34.145  44.865  1.00 47.44           O  
-ATOM   9790  CG2 THR D 286      69.252  31.745  44.707  1.00 46.90           C  
-ATOM   9791  N   VAL D 287      66.200  35.034  44.340  1.00 46.70           N  
-ATOM   9792  CA  VAL D 287      65.711  36.397  44.432  1.00 47.86           C  
-ATOM   9793  C   VAL D 287      66.876  37.331  44.771  1.00 48.42           C  
-ATOM   9794  O   VAL D 287      66.956  38.452  44.259  1.00 46.65           O  
-ATOM   9795  CB  VAL D 287      64.632  36.512  45.516  1.00 48.16           C  
-ATOM   9796  CG1 VAL D 287      64.070  37.925  45.543  1.00 49.77           C  
-ATOM   9797  CG2 VAL D 287      63.528  35.500  45.252  1.00 49.07           C  
-ATOM   9798  N   GLU D 288      67.784  36.862  45.627  1.00 49.07           N  
-ATOM   9799  CA  GLU D 288      68.941  37.662  46.014  1.00 49.15           C  
-ATOM   9800  C   GLU D 288      69.849  37.873  44.809  1.00 48.65           C  
-ATOM   9801  O   GLU D 288      70.339  38.979  44.576  1.00 48.15           O  
-ATOM   9802  CB  GLU D 288      69.735  36.978  47.132  1.00 50.43           C  
-ATOM   9803  CG  GLU D 288      70.964  37.775  47.572  1.00 52.39           C  
-ATOM   9804  CD  GLU D 288      71.836  37.040  48.579  1.00 54.97           C  
-ATOM   9805  OE1 GLU D 288      72.838  37.632  49.036  1.00 56.27           O  
-ATOM   9806  OE2 GLU D 288      71.527  35.876  48.914  1.00 54.84           O  
-ATOM   9807  N   GLU D 289      70.080  36.803  44.052  1.00 48.54           N  
-ATOM   9808  CA  GLU D 289      70.923  36.891  42.866  1.00 49.22           C  
-ATOM   9809  C   GLU D 289      70.288  37.927  41.949  1.00 49.36           C  
-ATOM   9810  O   GLU D 289      70.979  38.688  41.272  1.00 48.27           O  
-ATOM   9811  CB  GLU D 289      70.995  35.539  42.170  1.00 49.16           C  
-ATOM   9812  N   PHE D 290      68.958  37.944  41.956  1.00 49.90           N  
-ATOM   9813  CA  PHE D 290      68.165  38.874  41.162  1.00 50.23           C  
-ATOM   9814  C   PHE D 290      68.392  40.289  41.710  1.00 50.00           C  
-ATOM   9815  O   PHE D 290      68.652  41.227  40.958  1.00 47.75           O  
-ATOM   9816  CB  PHE D 290      66.684  38.486  41.266  1.00 50.45           C  
-ATOM   9817  CG  PHE D 290      65.801  39.124  40.225  1.00 51.27           C  
-ATOM   9818  CD1 PHE D 290      65.591  40.502  40.211  1.00 51.90           C  
-ATOM   9819  CD2 PHE D 290      65.170  38.341  39.262  1.00 50.36           C  
-ATOM   9820  CE1 PHE D 290      64.764  41.091  39.252  1.00 51.58           C  
-ATOM   9821  CE2 PHE D 290      64.343  38.917  38.300  1.00 50.04           C  
-ATOM   9822  CZ  PHE D 290      64.139  40.295  38.294  1.00 50.77           C  
-ATOM   9823  N   LEU D 291      68.305  40.428  43.029  1.00 52.00           N  
-ATOM   9824  CA  LEU D 291      68.507  41.717  43.686  1.00 52.72           C  
-ATOM   9825  C   LEU D 291      69.894  42.288  43.378  1.00 52.99           C  
-ATOM   9826  O   LEU D 291      70.027  43.468  43.038  1.00 52.81           O  
-ATOM   9827  CB  LEU D 291      68.324  41.568  45.196  1.00 51.43           C  
-ATOM   9828  N   ASP D 292      70.919  41.444  43.498  1.00 52.87           N  
-ATOM   9829  CA  ASP D 292      72.298  41.853  43.237  1.00 52.04           C  
-ATOM   9830  C   ASP D 292      72.471  42.378  41.816  1.00 50.82           C  
-ATOM   9831  O   ASP D 292      73.038  43.454  41.606  1.00 49.77           O  
-ATOM   9832  CB  ASP D 292      73.253  40.674  43.456  1.00 54.04           C  
-ATOM   9833  CG  ASP D 292      73.311  40.225  44.907  1.00 56.52           C  
-ATOM   9834  OD1 ASP D 292      73.981  39.207  45.186  1.00 58.24           O  
-ATOM   9835  OD2 ASP D 292      72.694  40.886  45.769  1.00 57.60           O  
-ATOM   9836  N   VAL D 293      71.983  41.609  40.845  1.00 49.00           N  
-ATOM   9837  CA  VAL D 293      72.085  41.985  39.438  1.00 47.63           C  
-ATOM   9838  C   VAL D 293      71.293  43.257  39.160  1.00 46.98           C  
-ATOM   9839  O   VAL D 293      71.808  44.209  38.562  1.00 46.64           O  
-ATOM   9840  CB  VAL D 293      71.546  40.860  38.513  1.00 48.49           C  
-ATOM   9841  CG1 VAL D 293      71.728  41.254  37.047  1.00 47.36           C  
-ATOM   9842  CG2 VAL D 293      72.263  39.544  38.809  1.00 46.71           C  
-ATOM   9843  N   SER D 294      70.038  43.257  39.604  1.00 45.84           N  
-ATOM   9844  CA  SER D 294      69.129  44.381  39.418  1.00 45.17           C  
-ATOM   9845  C   SER D 294      69.671  45.673  40.023  1.00 46.56           C  
-ATOM   9846  O   SER D 294      69.938  46.644  39.308  1.00 47.66           O  
-ATOM   9847  CB  SER D 294      67.770  44.051  40.030  1.00 43.80           C  
-ATOM   9848  N   PHE D 295      69.833  45.687  41.341  1.00 45.13           N  
-ATOM   9849  CA  PHE D 295      70.331  46.874  42.021  1.00 44.77           C  
-ATOM   9850  C   PHE D 295      71.775  47.190  41.664  1.00 43.95           C  
-ATOM   9851  O   PHE D 295      72.164  48.356  41.615  1.00 42.70           O  
-ATOM   9852  CB  PHE D 295      70.163  46.711  43.534  1.00 45.76           C  
-ATOM   9853  CG  PHE D 295      68.738  46.855  43.991  1.00 46.78           C  
-ATOM   9854  CD1 PHE D 295      67.727  46.102  43.401  1.00 47.22           C  
-ATOM   9855  CD2 PHE D 295      68.398  47.777  44.973  1.00 47.45           C  
-ATOM   9856  CE1 PHE D 295      66.396  46.270  43.776  1.00 47.08           C  
-ATOM   9857  CE2 PHE D 295      67.069  47.951  45.356  1.00 47.92           C  
-ATOM   9858  CZ  PHE D 295      66.067  47.196  44.755  1.00 48.10           C  
-ATOM   9859  N   GLY D 296      72.558  46.150  41.397  1.00 44.00           N  
-ATOM   9860  CA  GLY D 296      73.949  46.349  41.041  1.00 44.48           C  
-ATOM   9861  C   GLY D 296      74.078  47.021  39.689  1.00 44.89           C  
-ATOM   9862  O   GLY D 296      75.036  47.746  39.429  1.00 46.42           O  
-ATOM   9863  N   TYR D 297      73.102  46.776  38.824  1.00 45.28           N  
-ATOM   9864  CA  TYR D 297      73.087  47.349  37.483  1.00 46.25           C  
-ATOM   9865  C   TYR D 297      72.966  48.877  37.532  1.00 46.95           C  
-ATOM   9866  O   TYR D 297      73.522  49.579  36.683  1.00 46.22           O  
-ATOM   9867  CB  TYR D 297      71.922  46.732  36.694  1.00 45.52           C  
-ATOM   9868  CG  TYR D 297      71.717  47.267  35.296  1.00 43.42           C  
-ATOM   9869  CD1 TYR D 297      72.754  47.268  34.366  1.00 44.29           C  
-ATOM   9870  CD2 TYR D 297      70.464  47.728  34.886  1.00 43.18           C  
-ATOM   9871  CE1 TYR D 297      72.546  47.713  33.059  1.00 42.43           C  
-ATOM   9872  CE2 TYR D 297      70.243  48.172  33.587  1.00 40.95           C  
-ATOM   9873  CZ  TYR D 297      71.288  48.160  32.679  1.00 42.84           C  
-ATOM   9874  OH  TYR D 297      71.072  48.582  31.388  1.00 42.34           O  
-ATOM   9875  N   LEU D 298      72.245  49.388  38.530  1.00 47.90           N  
-ATOM   9876  CA  LEU D 298      72.064  50.833  38.675  1.00 49.33           C  
-ATOM   9877  C   LEU D 298      73.037  51.445  39.683  1.00 49.90           C  
-ATOM   9878  O   LEU D 298      72.865  52.588  40.116  1.00 51.10           O  
-ATOM   9879  CB  LEU D 298      70.624  51.160  39.093  1.00 48.01           C  
-ATOM   9880  CG  LEU D 298      69.487  50.817  38.121  1.00 48.23           C  
-ATOM   9881  CD1 LEU D 298      68.211  51.517  38.576  1.00 46.02           C  
-ATOM   9882  CD2 LEU D 298      69.846  51.257  36.706  1.00 47.77           C  
-ATOM   9883  N   GLY D 299      74.055  50.678  40.057  1.00 50.26           N  
-ATOM   9884  CA  GLY D 299      75.044  51.171  40.997  1.00 50.94           C  
-ATOM   9885  C   GLY D 299      74.546  51.363  42.415  1.00 51.35           C  
-ATOM   9886  O   GLY D 299      75.042  52.232  43.137  1.00 52.02           O  
-ATOM   9887  N   LEU D 300      73.567  50.560  42.819  1.00 50.34           N  
-ATOM   9888  CA  LEU D 300      73.024  50.646  44.168  1.00 50.33           C  
-ATOM   9889  C   LEU D 300      73.233  49.321  44.898  1.00 51.59           C  
-ATOM   9890  O   LEU D 300      73.297  48.262  44.274  1.00 51.53           O  
-ATOM   9891  CB  LEU D 300      71.524  50.967  44.128  1.00 48.62           C  
-ATOM   9892  CG  LEU D 300      71.024  52.244  43.442  1.00 46.97           C  
-ATOM   9893  CD1 LEU D 300      69.502  52.281  43.519  1.00 44.24           C  
-ATOM   9894  CD2 LEU D 300      71.623  53.477  44.100  1.00 44.23           C  
-ATOM   9895  N   ASN D 301      73.351  49.384  46.219  1.00 52.65           N  
-ATOM   9896  CA  ASN D 301      73.522  48.179  47.019  1.00 54.16           C  
-ATOM   9897  C   ASN D 301      72.135  47.762  47.495  1.00 54.48           C  
-ATOM   9898  O   ASN D 301      71.375  48.586  48.006  1.00 55.16           O  
-ATOM   9899  CB  ASN D 301      74.432  48.457  48.213  1.00 54.68           C  
-ATOM   9900  N   TRP D 302      71.801  46.489  47.323  1.00 54.45           N  
-ATOM   9901  CA  TRP D 302      70.489  45.997  47.731  1.00 55.66           C  
-ATOM   9902  C   TRP D 302      70.306  45.992  49.253  1.00 55.67           C  
-ATOM   9903  O   TRP D 302      69.179  46.058  49.749  1.00 55.66           O  
-ATOM   9904  CB  TRP D 302      70.260  44.589  47.165  1.00 55.60           C  
-ATOM   9905  N   LYS D 303      71.411  45.925  49.989  1.00 54.95           N  
-ATOM   9906  CA  LYS D 303      71.354  45.898  51.449  1.00 55.24           C  
-ATOM   9907  C   LYS D 303      70.899  47.231  52.055  1.00 54.87           C  
-ATOM   9908  O   LYS D 303      70.578  47.305  53.244  1.00 53.25           O  
-ATOM   9909  CB  LYS D 303      72.721  45.499  52.012  1.00 55.01           C  
-ATOM   9910  N   ASP D 304      70.868  48.278  51.235  1.00 54.91           N  
-ATOM   9911  CA  ASP D 304      70.457  49.602  51.695  1.00 54.33           C  
-ATOM   9912  C   ASP D 304      68.964  49.882  51.509  1.00 53.88           C  
-ATOM   9913  O   ASP D 304      68.477  50.937  51.913  1.00 53.05           O  
-ATOM   9914  CB  ASP D 304      71.258  50.688  50.967  1.00 56.01           C  
-ATOM   9915  CG  ASP D 304      72.731  50.686  51.344  1.00 56.83           C  
-ATOM   9916  OD1 ASP D 304      73.409  49.660  51.124  1.00 58.68           O  
-ATOM   9917  OD2 ASP D 304      73.212  51.717  51.860  1.00 57.81           O  
-ATOM   9918  N   TYR D 305      68.237  48.950  50.901  1.00 52.47           N  
-ATOM   9919  CA  TYR D 305      66.811  49.158  50.680  1.00 51.31           C  
-ATOM   9920  C   TYR D 305      65.977  47.910  50.939  1.00 51.42           C  
-ATOM   9921  O   TYR D 305      64.776  48.004  51.186  1.00 51.73           O  
-ATOM   9922  CB  TYR D 305      66.577  49.660  49.259  1.00 51.55           C  
-ATOM   9923  N   VAL D 306      66.609  46.743  50.883  1.00 51.41           N  
-ATOM   9924  CA  VAL D 306      65.897  45.487  51.112  1.00 51.97           C  
-ATOM   9925  C   VAL D 306      65.236  45.482  52.489  1.00 52.28           C  
-ATOM   9926  O   VAL D 306      65.830  45.921  53.474  1.00 53.25           O  
-ATOM   9927  CB  VAL D 306      66.861  44.304  50.987  1.00 50.36           C  
-ATOM   9928  N   GLU D 307      64.003  44.985  52.550  1.00 51.96           N  
-ATOM   9929  CA  GLU D 307      63.267  44.920  53.806  1.00 50.99           C  
-ATOM   9930  C   GLU D 307      62.595  43.561  53.959  1.00 50.56           C  
-ATOM   9931  O   GLU D 307      61.441  43.381  53.573  1.00 50.92           O  
-ATOM   9932  CB  GLU D 307      62.226  46.027  53.855  1.00 51.35           C  
-ATOM   9933  N   ILE D 308      63.326  42.610  54.530  1.00 50.42           N  
-ATOM   9934  CA  ILE D 308      62.821  41.255  54.737  1.00 51.49           C  
-ATOM   9935  C   ILE D 308      61.442  41.238  55.405  1.00 51.22           C  
-ATOM   9936  O   ILE D 308      61.162  42.045  56.291  1.00 51.32           O  
-ATOM   9937  CB  ILE D 308      63.800  40.439  55.607  1.00 51.56           C  
-ATOM   9938  CG1 ILE D 308      65.226  40.595  55.071  1.00 52.39           C  
-ATOM   9939  CG2 ILE D 308      63.396  38.975  55.614  1.00 52.12           C  
-ATOM   9940  CD1 ILE D 308      65.398  40.161  53.630  1.00 53.22           C  
-ATOM   9941  N   ASP D 309      60.587  40.313  54.978  1.00 50.81           N  
-ATOM   9942  CA  ASP D 309      59.244  40.193  55.539  1.00 49.86           C  
-ATOM   9943  C   ASP D 309      59.032  38.819  56.166  1.00 49.29           C  
-ATOM   9944  O   ASP D 309      59.555  37.816  55.677  1.00 48.47           O  
-ATOM   9945  CB  ASP D 309      58.203  40.436  54.455  1.00 49.66           C  
-ATOM   9946  N   ASP D 319      58.401  26.589  44.414  1.00 56.99           N  
-ATOM   9947  CA  ASP D 319      58.861  25.458  45.215  1.00 57.53           C  
-ATOM   9948  C   ASP D 319      60.208  24.928  44.712  1.00 57.03           C  
-ATOM   9949  O   ASP D 319      61.255  25.530  44.966  1.00 56.66           O  
-ATOM   9950  CB  ASP D 319      57.808  24.345  45.198  1.00 56.90           C  
-ATOM   9951  N   ASN D 320      60.179  23.803  44.000  1.00 57.20           N  
-ATOM   9952  CA  ASN D 320      61.400  23.200  43.467  1.00 56.70           C  
-ATOM   9953  C   ASN D 320      61.151  22.613  42.076  1.00 56.69           C  
-ATOM   9954  O   ASN D 320      61.038  21.394  41.909  1.00 56.83           O  
-ATOM   9955  CB  ASN D 320      61.899  22.099  44.405  1.00 55.46           C  
-ATOM   9956  CG  ASN D 320      63.330  21.698  44.115  1.00 55.96           C  
-ATOM   9957  OD1 ASN D 320      64.247  22.511  44.232  1.00 56.27           O  
-ATOM   9958  ND2 ASN D 320      63.530  20.441  43.729  1.00 55.91           N  
-ATOM   9959  N   LEU D 321      61.081  23.493  41.082  1.00 55.49           N  
-ATOM   9960  CA  LEU D 321      60.829  23.090  39.705  1.00 53.77           C  
-ATOM   9961  C   LEU D 321      62.065  23.151  38.809  1.00 53.88           C  
-ATOM   9962  O   LEU D 321      62.566  24.237  38.499  1.00 53.74           O  
-ATOM   9963  CB  LEU D 321      59.740  23.981  39.104  1.00 53.31           C  
-ATOM   9964  CG  LEU D 321      58.381  24.004  39.804  1.00 51.18           C  
-ATOM   9965  CD1 LEU D 321      57.516  25.099  39.185  1.00 50.07           C  
-ATOM   9966  CD2 LEU D 321      57.712  22.640  39.681  1.00 49.68           C  
-ATOM   9967  N   GLN D 322      62.546  21.980  38.396  1.00 52.90           N  
-ATOM   9968  CA  GLN D 322      63.706  21.877  37.510  1.00 52.12           C  
-ATOM   9969  C   GLN D 322      63.253  21.148  36.242  1.00 49.46           C  
-ATOM   9970  O   GLN D 322      63.219  19.914  36.195  1.00 49.78           O  
-ATOM   9971  CB  GLN D 322      64.839  21.102  38.196  1.00 54.66           C  
-ATOM   9972  CG  GLN D 322      66.105  20.942  37.347  1.00 58.93           C  
-ATOM   9973  CD  GLN D 322      66.675  22.272  36.856  1.00 61.05           C  
-ATOM   9974  OE1 GLN D 322      67.112  23.114  37.647  1.00 62.01           O  
-ATOM   9975  NE2 GLN D 322      66.672  22.461  35.540  1.00 61.07           N  
-ATOM   9976  N   GLY D 323      62.910  21.922  35.217  1.00 46.29           N  
-ATOM   9977  CA  GLY D 323      62.421  21.346  33.977  1.00 43.52           C  
-ATOM   9978  C   GLY D 323      63.418  20.896  32.928  1.00 41.25           C  
-ATOM   9979  O   GLY D 323      64.500  21.461  32.779  1.00 40.69           O  
-ATOM   9980  N   ASP D 324      63.024  19.861  32.194  1.00 38.90           N  
-ATOM   9981  CA  ASP D 324      63.825  19.292  31.117  1.00 37.10           C  
-ATOM   9982  C   ASP D 324      63.160  19.707  29.802  1.00 35.72           C  
-ATOM   9983  O   ASP D 324      62.146  19.136  29.402  1.00 35.08           O  
-ATOM   9984  CB  ASP D 324      63.845  17.764  31.247  1.00 37.48           C  
-ATOM   9985  CG  ASP D 324      64.512  17.074  30.068  1.00 38.86           C  
-ATOM   9986  OD1 ASP D 324      64.503  15.825  30.036  1.00 39.67           O  
-ATOM   9987  OD2 ASP D 324      65.045  17.768  29.176  1.00 39.57           O  
-ATOM   9988  N   ALA D 325      63.731  20.705  29.138  1.00 33.63           N  
-ATOM   9989  CA  ALA D 325      63.188  21.200  27.879  1.00 32.46           C  
-ATOM   9990  C   ALA D 325      63.917  20.618  26.675  1.00 33.60           C  
-ATOM   9991  O   ALA D 325      64.008  21.259  25.629  1.00 33.44           O  
-ATOM   9992  CB  ALA D 325      63.267  22.724  27.847  1.00 32.97           C  
-ATOM   9993  N   SER D 326      64.431  19.402  26.822  1.00 34.21           N  
-ATOM   9994  CA  SER D 326      65.150  18.743  25.738  1.00 36.83           C  
-ATOM   9995  C   SER D 326      64.298  18.608  24.482  1.00 37.16           C  
-ATOM   9996  O   SER D 326      64.730  18.967  23.384  1.00 37.31           O  
-ATOM   9997  CB  SER D 326      65.615  17.352  26.175  1.00 37.19           C  
-ATOM   9998  OG  SER D 326      66.533  17.433  27.246  1.00 41.05           O  
-ATOM   9999  N   LYS D 327      63.091  18.078  24.650  1.00 37.37           N  
-ATOM  10000  CA  LYS D 327      62.181  17.879  23.529  1.00 37.38           C  
-ATOM  10001  C   LYS D 327      61.955  19.173  22.759  1.00 38.01           C  
-ATOM  10002  O   LYS D 327      61.938  19.174  21.524  1.00 40.22           O  
-ATOM  10003  CB  LYS D 327      60.847  17.329  24.034  1.00 37.22           C  
-ATOM  10004  CG  LYS D 327      59.872  16.924  22.942  1.00 36.50           C  
-ATOM  10005  CD  LYS D 327      58.611  16.355  23.562  1.00 38.02           C  
-ATOM  10006  CE  LYS D 327      57.572  15.991  22.519  1.00 37.67           C  
-ATOM  10007  NZ  LYS D 327      56.356  15.444  23.177  1.00 38.01           N  
-ATOM  10008  N   ALA D 328      61.788  20.274  23.487  1.00 36.56           N  
-ATOM  10009  CA  ALA D 328      61.566  21.569  22.858  1.00 36.59           C  
-ATOM  10010  C   ALA D 328      62.780  21.963  22.021  1.00 36.95           C  
-ATOM  10011  O   ALA D 328      62.641  22.474  20.905  1.00 37.33           O  
-ATOM  10012  CB  ALA D 328      61.294  22.629  23.921  1.00 36.99           C  
-ATOM  10013  N   LYS D 329      63.970  21.726  22.566  1.00 35.32           N  
-ATOM  10014  CA  LYS D 329      65.204  22.052  21.865  1.00 35.66           C  
-ATOM  10015  C   LYS D 329      65.381  21.165  20.636  1.00 35.90           C  
-ATOM  10016  O   LYS D 329      65.723  21.646  19.557  1.00 35.84           O  
-ATOM  10017  CB  LYS D 329      66.401  21.889  22.803  1.00 36.51           C  
-ATOM  10018  N   GLU D 330      65.129  19.872  20.801  1.00 36.75           N  
-ATOM  10019  CA  GLU D 330      65.285  18.916  19.710  1.00 37.58           C  
-ATOM  10020  C   GLU D 330      64.251  19.049  18.599  1.00 39.49           C  
-ATOM  10021  O   GLU D 330      64.605  19.284  17.444  1.00 40.55           O  
-ATOM  10022  CB  GLU D 330      65.267  17.492  20.260  1.00 38.09           C  
-ATOM  10023  N   VAL D 331      62.976  18.900  18.950  1.00 39.11           N  
-ATOM  10024  CA  VAL D 331      61.900  18.970  17.970  1.00 38.52           C  
-ATOM  10025  C   VAL D 331      61.575  20.364  17.436  1.00 39.45           C  
-ATOM  10026  O   VAL D 331      61.404  20.546  16.229  1.00 39.67           O  
-ATOM  10027  CB  VAL D 331      60.604  18.360  18.537  1.00 38.37           C  
-ATOM  10028  CG1 VAL D 331      59.513  18.378  17.476  1.00 37.52           C  
-ATOM  10029  CG2 VAL D 331      60.867  16.946  19.021  1.00 36.25           C  
-ATOM  10030  N   LEU D 332      61.480  21.349  18.322  1.00 38.72           N  
-ATOM  10031  CA  LEU D 332      61.156  22.704  17.886  1.00 38.07           C  
-ATOM  10032  C   LEU D 332      62.387  23.541  17.535  1.00 37.85           C  
-ATOM  10033  O   LEU D 332      62.268  24.594  16.905  1.00 38.74           O  
-ATOM  10034  CB  LEU D 332      60.352  23.429  18.972  1.00 36.95           C  
-ATOM  10035  CG  LEU D 332      59.082  22.743  19.486  1.00 36.75           C  
-ATOM  10036  CD1 LEU D 332      58.466  23.600  20.578  1.00 35.71           C  
-ATOM  10037  CD2 LEU D 332      58.095  22.529  18.346  1.00 33.48           C  
-ATOM  10038  N   GLY D 333      63.567  23.074  17.932  1.00 36.25           N  
-ATOM  10039  CA  GLY D 333      64.774  23.832  17.658  1.00 36.66           C  
-ATOM  10040  C   GLY D 333      64.735  25.145  18.428  1.00 36.46           C  
-ATOM  10041  O   GLY D 333      65.394  26.120  18.064  1.00 34.82           O  
-ATOM  10042  N   TRP D 334      63.949  25.165  19.501  1.00 36.73           N  
-ATOM  10043  CA  TRP D 334      63.803  26.355  20.332  1.00 36.28           C  
-ATOM  10044  C   TRP D 334      64.945  26.505  21.326  1.00 36.24           C  
-ATOM  10045  O   TRP D 334      65.389  25.535  21.934  1.00 36.98           O  
-ATOM  10046  CB  TRP D 334      62.480  26.310  21.106  1.00 34.08           C  
-ATOM  10047  CG  TRP D 334      62.314  27.471  22.040  1.00 33.34           C  
-ATOM  10048  CD1 TRP D 334      61.946  28.746  21.712  1.00 31.30           C  
-ATOM  10049  CD2 TRP D 334      62.577  27.480  23.449  1.00 31.55           C  
-ATOM  10050  NE1 TRP D 334      61.967  29.548  22.829  1.00 31.01           N  
-ATOM  10051  CE2 TRP D 334      62.350  28.796  23.909  1.00 30.80           C  
-ATOM  10052  CE3 TRP D 334      62.984  26.503  24.368  1.00 30.83           C  
-ATOM  10053  CZ2 TRP D 334      62.517  29.160  25.246  1.00 29.32           C  
-ATOM  10054  CZ3 TRP D 334      63.151  26.866  25.699  1.00 29.16           C  
-ATOM  10055  CH2 TRP D 334      62.917  28.185  26.124  1.00 29.62           C  
-ATOM  10056  N   LYS D 335      65.409  27.735  21.491  1.00 37.34           N  
-ATOM  10057  CA  LYS D 335      66.483  28.028  22.427  1.00 38.21           C  
-ATOM  10058  C   LYS D 335      66.301  29.450  22.934  1.00 38.86           C  
-ATOM  10059  O   LYS D 335      66.100  30.377  22.150  1.00 39.16           O  
-ATOM  10060  CB  LYS D 335      67.833  27.889  21.743  1.00 38.85           C  
-ATOM  10061  N   PRO D 336      66.338  29.639  24.260  1.00 38.84           N  
-ATOM  10062  CA  PRO D 336      66.174  30.998  24.780  1.00 40.06           C  
-ATOM  10063  C   PRO D 336      67.318  31.883  24.294  1.00 41.42           C  
-ATOM  10064  O   PRO D 336      68.487  31.546  24.470  1.00 42.59           O  
-ATOM  10065  CB  PRO D 336      66.173  30.793  26.297  1.00 39.77           C  
-ATOM  10066  CG  PRO D 336      66.922  29.507  26.486  1.00 38.84           C  
-ATOM  10067  CD  PRO D 336      66.426  28.658  25.352  1.00 38.33           C  
-ATOM  10068  N   GLN D 337      66.972  33.002  23.666  1.00 42.02           N  
-ATOM  10069  CA  GLN D 337      67.964  33.927  23.138  1.00 43.13           C  
-ATOM  10070  C   GLN D 337      68.151  35.112  24.075  1.00 45.64           C  
-ATOM  10071  O   GLN D 337      68.720  36.136  23.697  1.00 46.96           O  
-ATOM  10072  CB  GLN D 337      67.543  34.408  21.751  1.00 42.31           C  
-ATOM  10073  N   VAL D 338      67.659  34.966  25.301  1.00 46.35           N  
-ATOM  10074  CA  VAL D 338      67.780  36.006  26.318  1.00 45.44           C  
-ATOM  10075  C   VAL D 338      68.066  35.317  27.642  1.00 45.88           C  
-ATOM  10076  O   VAL D 338      67.237  34.561  28.154  1.00 46.23           O  
-ATOM  10077  CB  VAL D 338      66.482  36.838  26.459  1.00 45.19           C  
-ATOM  10078  CG1 VAL D 338      66.571  37.740  27.679  1.00 44.35           C  
-ATOM  10079  CG2 VAL D 338      66.261  37.678  25.210  1.00 44.41           C  
-ATOM  10080  N   GLY D 339      69.250  35.572  28.184  1.00 45.21           N  
-ATOM  10081  CA  GLY D 339      69.625  34.960  29.443  1.00 45.45           C  
-ATOM  10082  C   GLY D 339      69.110  35.711  30.658  1.00 45.30           C  
-ATOM  10083  O   GLY D 339      68.531  36.796  30.550  1.00 45.52           O  
-ATOM  10084  N   PHE D 340      69.327  35.120  31.824  1.00 44.96           N  
-ATOM  10085  CA  PHE D 340      68.893  35.705  33.082  1.00 46.57           C  
-ATOM  10086  C   PHE D 340      69.364  37.153  33.272  1.00 46.73           C  
-ATOM  10087  O   PHE D 340      68.559  38.038  33.571  1.00 47.21           O  
-ATOM  10088  CB  PHE D 340      69.383  34.822  34.230  1.00 46.68           C  
-ATOM  10089  CG  PHE D 340      69.082  35.364  35.592  1.00 48.44           C  
-ATOM  10090  CD1 PHE D 340      69.982  36.210  36.232  1.00 47.74           C  
-ATOM  10091  CD2 PHE D 340      67.905  35.012  36.248  1.00 49.40           C  
-ATOM  10092  CE1 PHE D 340      69.717  36.696  37.506  1.00 49.55           C  
-ATOM  10093  CE2 PHE D 340      67.627  35.491  37.524  1.00 50.16           C  
-ATOM  10094  CZ  PHE D 340      68.536  36.336  38.155  1.00 51.18           C  
-ATOM  10095  N   GLU D 341      70.661  37.386  33.087  1.00 45.55           N  
-ATOM  10096  CA  GLU D 341      71.240  38.713  33.254  1.00 45.18           C  
-ATOM  10097  C   GLU D 341      70.597  39.752  32.353  1.00 44.76           C  
-ATOM  10098  O   GLU D 341      70.216  40.828  32.809  1.00 44.60           O  
-ATOM  10099  CB  GLU D 341      72.745  38.667  32.990  1.00 46.67           C  
-ATOM  10100  N   LYS D 342      70.488  39.436  31.069  1.00 44.07           N  
-ATOM  10101  CA  LYS D 342      69.898  40.370  30.122  1.00 44.03           C  
-ATOM  10102  C   LYS D 342      68.422  40.609  30.444  1.00 43.25           C  
-ATOM  10103  O   LYS D 342      67.911  41.713  30.253  1.00 43.17           O  
-ATOM  10104  CB  LYS D 342      70.057  39.845  28.691  1.00 45.18           C  
-ATOM  10105  CG  LYS D 342      69.608  40.830  27.622  1.00 46.75           C  
-ATOM  10106  CD  LYS D 342      69.780  40.259  26.225  1.00 50.17           C  
-ATOM  10107  CE  LYS D 342      69.236  41.224  25.180  1.00 51.87           C  
-ATOM  10108  NZ  LYS D 342      69.374  40.694  23.796  1.00 53.50           N  
-ATOM  10109  N   LEU D 343      67.747  39.575  30.939  1.00 42.03           N  
-ATOM  10110  CA  LEU D 343      66.336  39.684  31.295  1.00 40.36           C  
-ATOM  10111  C   LEU D 343      66.168  40.659  32.448  1.00 40.32           C  
-ATOM  10112  O   LEU D 343      65.293  41.523  32.418  1.00 39.79           O  
-ATOM  10113  CB  LEU D 343      65.775  38.320  31.707  1.00 37.93           C  
-ATOM  10114  CG  LEU D 343      64.383  38.334  32.357  1.00 36.85           C  
-ATOM  10115  CD1 LEU D 343      63.383  39.054  31.453  1.00 35.06           C  
-ATOM  10116  CD2 LEU D 343      63.932  36.910  32.639  1.00 34.34           C  
-ATOM  10117  N   VAL D 344      67.009  40.510  33.467  1.00 40.36           N  
-ATOM  10118  CA  VAL D 344      66.955  41.384  34.632  1.00 40.02           C  
-ATOM  10119  C   VAL D 344      67.221  42.843  34.268  1.00 40.37           C  
-ATOM  10120  O   VAL D 344      66.408  43.716  34.563  1.00 41.49           O  
-ATOM  10121  CB  VAL D 344      67.970  40.946  35.703  1.00 37.81           C  
-ATOM  10122  CG1 VAL D 344      67.919  41.900  36.885  1.00 36.64           C  
-ATOM  10123  CG2 VAL D 344      67.661  39.524  36.157  1.00 37.04           C  
-ATOM  10124  N   LYS D 345      68.357  43.103  33.628  1.00 40.71           N  
-ATOM  10125  CA  LYS D 345      68.716  44.460  33.234  1.00 42.72           C  
-ATOM  10126  C   LYS D 345      67.654  45.047  32.312  1.00 43.61           C  
-ATOM  10127  O   LYS D 345      67.440  46.262  32.283  1.00 43.86           O  
-ATOM  10128  CB  LYS D 345      70.080  44.473  32.530  1.00 45.61           C  
-ATOM  10129  CG  LYS D 345      71.239  44.033  33.415  1.00 46.30           C  
-ATOM  10130  CD  LYS D 345      72.580  44.151  32.697  1.00 47.41           C  
-ATOM  10131  CE  LYS D 345      73.730  43.748  33.624  1.00 49.28           C  
-ATOM  10132  NZ  LYS D 345      75.075  43.874  32.982  1.00 48.84           N  
-ATOM  10133  N   MET D 346      66.990  44.179  31.556  1.00 42.87           N  
-ATOM  10134  CA  MET D 346      65.943  44.624  30.650  1.00 43.29           C  
-ATOM  10135  C   MET D 346      64.773  45.155  31.476  1.00 42.88           C  
-ATOM  10136  O   MET D 346      64.230  46.221  31.190  1.00 42.35           O  
-ATOM  10137  CB  MET D 346      65.463  43.466  29.780  1.00 44.12           C  
-ATOM  10138  CG  MET D 346      64.477  43.884  28.708  1.00 45.91           C  
-ATOM  10139  SD  MET D 346      63.508  42.496  28.103  1.00 48.14           S  
-ATOM  10140  CE  MET D 346      64.801  41.507  27.303  1.00 44.80           C  
-ATOM  10141  N   MET D 347      64.389  44.398  32.499  1.00 42.14           N  
-ATOM  10142  CA  MET D 347      63.293  44.793  33.371  1.00 42.83           C  
-ATOM  10143  C   MET D 347      63.653  46.068  34.136  1.00 42.76           C  
-ATOM  10144  O   MET D 347      62.822  46.960  34.302  1.00 43.34           O  
-ATOM  10145  CB  MET D 347      62.952  43.649  34.341  1.00 41.68           C  
-ATOM  10146  CG  MET D 347      62.170  42.503  33.681  1.00 40.48           C  
-ATOM  10147  SD  MET D 347      61.909  41.039  34.709  1.00 40.39           S  
-ATOM  10148  CE  MET D 347      60.638  41.616  35.857  1.00 37.54           C  
-ATOM  10149  N   VAL D 348      64.902  46.156  34.581  1.00 43.64           N  
-ATOM  10150  CA  VAL D 348      65.373  47.325  35.319  1.00 42.50           C  
-ATOM  10151  C   VAL D 348      65.344  48.596  34.466  1.00 42.95           C  
-ATOM  10152  O   VAL D 348      64.849  49.631  34.911  1.00 42.40           O  
-ATOM  10153  CB  VAL D 348      66.803  47.101  35.851  1.00 42.38           C  
-ATOM  10154  CG1 VAL D 348      67.326  48.373  36.501  1.00 42.95           C  
-ATOM  10155  CG2 VAL D 348      66.802  45.961  36.862  1.00 41.92           C  
-ATOM  10156  N   ASP D 349      65.872  48.524  33.246  1.00 43.20           N  
-ATOM  10157  CA  ASP D 349      65.882  49.691  32.367  1.00 45.44           C  
-ATOM  10158  C   ASP D 349      64.479  50.252  32.145  1.00 46.35           C  
-ATOM  10159  O   ASP D 349      64.261  51.459  32.258  1.00 45.15           O  
-ATOM  10160  CB  ASP D 349      66.501  49.354  31.001  1.00 46.96           C  
-ATOM  10161  CG  ASP D 349      68.020  49.279  31.043  1.00 49.42           C  
-ATOM  10162  OD1 ASP D 349      68.652  50.211  31.588  1.00 49.82           O  
-ATOM  10163  OD2 ASP D 349      68.583  48.295  30.519  1.00 49.52           O  
-ATOM  10164  N   GLU D 350      63.531  49.374  31.831  1.00 46.10           N  
-ATOM  10165  CA  GLU D 350      62.161  49.800  31.580  1.00 46.67           C  
-ATOM  10166  C   GLU D 350      61.459  50.380  32.801  1.00 45.90           C  
-ATOM  10167  O   GLU D 350      60.669  51.323  32.679  1.00 44.37           O  
-ATOM  10168  CB  GLU D 350      61.342  48.636  31.016  1.00 49.75           C  
-ATOM  10169  CG  GLU D 350      61.632  48.357  29.553  1.00 54.35           C  
-ATOM  10170  CD  GLU D 350      61.331  49.559  28.671  1.00 56.92           C  
-ATOM  10171  OE1 GLU D 350      60.142  49.934  28.558  1.00 57.00           O  
-ATOM  10172  OE2 GLU D 350      62.285  50.133  28.099  1.00 59.48           O  
-ATOM  10173  N   ASP D 351      61.743  49.819  33.973  1.00 43.34           N  
-ATOM  10174  CA  ASP D 351      61.121  50.290  35.200  1.00 42.97           C  
-ATOM  10175  C   ASP D 351      61.754  51.588  35.684  1.00 43.42           C  
-ATOM  10176  O   ASP D 351      61.168  52.312  36.490  1.00 43.98           O  
-ATOM  10177  CB  ASP D 351      61.189  49.199  36.278  1.00 42.23           C  
-ATOM  10178  CG  ASP D 351      59.964  48.289  36.262  1.00 39.57           C  
-ATOM  10179  OD1 ASP D 351      60.033  47.159  36.791  1.00 38.45           O  
-ATOM  10180  OD2 ASP D 351      58.921  48.714  35.725  1.00 38.51           O  
-ATOM  10181  N   LEU D 352      62.950  51.884  35.185  1.00 44.16           N  
-ATOM  10182  CA  LEU D 352      63.625  53.124  35.548  1.00 43.31           C  
-ATOM  10183  C   LEU D 352      62.991  54.217  34.686  1.00 44.07           C  
-ATOM  10184  O   LEU D 352      62.633  55.293  35.172  1.00 40.96           O  
-ATOM  10185  CB  LEU D 352      65.122  53.024  35.255  1.00 43.29           C  
-ATOM  10186  CG  LEU D 352      65.942  54.262  35.637  1.00 44.99           C  
-ATOM  10187  CD1 LEU D 352      65.789  54.536  37.131  1.00 43.94           C  
-ATOM  10188  CD2 LEU D 352      67.407  54.053  35.268  1.00 42.58           C  
-ATOM  10189  N   GLU D 353      62.850  53.916  33.401  1.00 44.78           N  
-ATOM  10190  CA  GLU D 353      62.244  54.833  32.444  1.00 47.19           C  
-ATOM  10191  C   GLU D 353      60.859  55.193  32.979  1.00 47.60           C  
-ATOM  10192  O   GLU D 353      60.385  56.324  32.825  1.00 46.53           O  
-ATOM  10193  CB  GLU D 353      62.095  54.136  31.089  1.00 49.94           C  
-ATOM  10194  CG  GLU D 353      62.217  55.036  29.874  1.00 53.89           C  
-ATOM  10195  CD  GLU D 353      63.657  55.425  29.588  1.00 57.81           C  
-ATOM  10196  OE1 GLU D 353      63.951  55.808  28.432  1.00 60.02           O  
-ATOM  10197  OE2 GLU D 353      64.492  55.354  30.517  1.00 58.05           O  
-ATOM  10198  N   LEU D 354      60.224  54.205  33.608  1.00 47.20           N  
-ATOM  10199  CA  LEU D 354      58.890  54.352  34.184  1.00 46.82           C  
-ATOM  10200  C   LEU D 354      58.919  55.240  35.427  1.00 46.47           C  
-ATOM  10201  O   LEU D 354      58.036  56.078  35.617  1.00 46.52           O  
-ATOM  10202  CB  LEU D 354      58.325  52.976  34.548  1.00 47.00           C  
-ATOM  10203  CG  LEU D 354      56.859  52.921  34.979  1.00 48.65           C  
-ATOM  10204  CD1 LEU D 354      55.972  53.356  33.818  1.00 49.28           C  
-ATOM  10205  CD2 LEU D 354      56.504  51.506  35.419  1.00 49.42           C  
-ATOM  10206  N   ALA D 355      59.924  55.046  36.275  1.00 45.35           N  
-ATOM  10207  CA  ALA D 355      60.056  55.855  37.483  1.00 46.59           C  
-ATOM  10208  C   ALA D 355      60.297  57.311  37.084  1.00 46.88           C  
-ATOM  10209  O   ALA D 355      59.692  58.226  37.641  1.00 46.62           O  
-ATOM  10210  CB  ALA D 355      61.214  55.347  38.334  1.00 45.55           C  
-ATOM  10211  N   LYS D 356      61.181  57.515  36.110  1.00 47.95           N  
-ATOM  10212  CA  LYS D 356      61.491  58.856  35.630  1.00 48.13           C  
-ATOM  10213  C   LYS D 356      60.237  59.559  35.123  1.00 48.83           C  
-ATOM  10214  O   LYS D 356      60.043  60.747  35.378  1.00 50.29           O  
-ATOM  10215  CB  LYS D 356      62.546  58.804  34.517  1.00 47.29           C  
-ATOM  10216  CG  LYS D 356      63.948  58.483  35.014  1.00 47.09           C  
-ATOM  10217  CD  LYS D 356      64.984  58.602  33.903  1.00 49.30           C  
-ATOM  10218  CE  LYS D 356      66.400  58.464  34.455  1.00 48.59           C  
-ATOM  10219  NZ  LYS D 356      67.440  58.534  33.386  1.00 49.91           N  
-ATOM  10220  N   ARG D 357      59.389  58.830  34.403  1.00 49.56           N  
-ATOM  10221  CA  ARG D 357      58.149  59.408  33.890  1.00 50.22           C  
-ATOM  10222  C   ARG D 357      57.342  59.923  35.078  1.00 50.90           C  
-ATOM  10223  O   ARG D 357      56.610  60.911  34.973  1.00 51.96           O  
-ATOM  10224  CB  ARG D 357      57.346  58.355  33.123  1.00 48.80           C  
-ATOM  10225  N   GLU D 358      57.494  59.246  36.213  1.00 51.18           N  
-ATOM  10226  CA  GLU D 358      56.789  59.614  37.434  1.00 51.70           C  
-ATOM  10227  C   GLU D 358      57.432  60.837  38.089  1.00 51.80           C  
-ATOM  10228  O   GLU D 358      56.735  61.742  38.555  1.00 51.35           O  
-ATOM  10229  CB  GLU D 358      56.782  58.434  38.405  1.00 50.85           C  
-ATOM  10230  N   LYS D 359      58.762  60.861  38.121  1.00 51.52           N  
-ATOM  10231  CA  LYS D 359      59.487  61.979  38.713  1.00 51.76           C  
-ATOM  10232  C   LYS D 359      59.165  63.258  37.952  1.00 52.15           C  
-ATOM  10233  O   LYS D 359      58.913  64.303  38.552  1.00 51.93           O  
-ATOM  10234  CB  LYS D 359      60.982  61.713  38.679  1.00 51.77           C  
-ATOM  10235  N   VAL D 360      59.173  63.167  36.625  1.00 53.31           N  
-ATOM  10236  CA  VAL D 360      58.873  64.313  35.776  1.00 54.20           C  
-ATOM  10237  C   VAL D 360      57.502  64.889  36.110  1.00 55.45           C  
-ATOM  10238  O   VAL D 360      57.349  66.104  36.237  1.00 55.27           O  
-ATOM  10239  CB  VAL D 360      58.895  63.926  34.281  1.00 54.09           C  
-ATOM  10240  CG1 VAL D 360      58.447  65.108  33.425  1.00 53.94           C  
-ATOM  10241  CG2 VAL D 360      60.294  63.491  33.884  1.00 53.26           C  
-ATOM  10242  N   LEU D 361      56.507  64.014  36.250  1.00 56.30           N  
-ATOM  10243  CA  LEU D 361      55.153  64.455  36.573  1.00 56.55           C  
-ATOM  10244  C   LEU D 361      55.123  65.160  37.922  1.00 56.35           C  
-ATOM  10245  O   LEU D 361      54.500  66.214  38.066  1.00 56.49           O  
-ATOM  10246  CB  LEU D 361      54.188  63.268  36.581  1.00 56.53           C  
-ATOM  10247  CG  LEU D 361      53.903  62.645  35.213  1.00 57.20           C  
-ATOM  10248  CD1 LEU D 361      52.878  61.535  35.361  1.00 57.04           C  
-ATOM  10249  CD2 LEU D 361      53.388  63.710  34.263  1.00 57.01           C  
-ATOM  10250  N   VAL D 362      55.801  64.577  38.906  1.00 56.34           N  
-ATOM  10251  CA  VAL D 362      55.862  65.160  40.241  1.00 56.05           C  
-ATOM  10252  C   VAL D 362      56.579  66.513  40.178  1.00 57.37           C  
-ATOM  10253  O   VAL D 362      55.992  67.519  40.638  1.00 57.66           O  
-ATOM  10254  CB  VAL D 362      56.609  64.223  41.223  1.00 54.81           C  
-ATOM  10255  CG1 VAL D 362      56.705  64.867  42.601  1.00 53.63           C  
-ATOM  10256  CG2 VAL D 362      55.883  62.895  41.318  1.00 51.88           C  
-TER   10257      VAL D 362                                                      
-HETATM10258  PA  NDP A 701       7.828  20.770  33.341  1.00 26.62           P  
-HETATM10259  O1A NDP A 701       8.493  21.108  34.624  1.00 25.90           O  
-HETATM10260  O2A NDP A 701       6.924  19.596  33.279  1.00 24.27           O  
-HETATM10261  O5B NDP A 701       8.936  20.527  32.233  1.00 25.81           O  
-HETATM10262  C5B NDP A 701      10.171  21.230  32.258  1.00 23.81           C  
-HETATM10263  C4B NDP A 701      11.070  20.686  31.183  1.00 22.76           C  
-HETATM10264  O4B NDP A 701      12.314  21.447  31.177  1.00 20.10           O  
-HETATM10265  C3B NDP A 701      11.488  19.231  31.395  1.00 23.95           C  
-HETATM10266  O3B NDP A 701      11.682  18.619  30.125  1.00 26.03           O  
-HETATM10267  C2B NDP A 701      12.820  19.405  32.116  1.00 21.60           C  
-HETATM10268  O2B NDP A 701      13.686  18.285  32.052  1.00 20.05           O  
-HETATM10269  C1B NDP A 701      13.398  20.552  31.298  1.00 22.28           C  
-HETATM10270  N9A NDP A 701      14.500  21.245  31.956  1.00 23.15           N  
-HETATM10271  C8A NDP A 701      14.548  21.766  33.223  1.00 22.88           C  
-HETATM10272  N7A NDP A 701      15.719  22.252  33.550  1.00 22.45           N  
-HETATM10273  C5A NDP A 701      16.495  22.034  32.420  1.00 23.76           C  
-HETATM10274  C6A NDP A 701      17.834  22.332  32.116  1.00 23.24           C  
-HETATM10275  N6A NDP A 701      18.677  22.921  32.970  1.00 21.16           N  
-HETATM10276  N1A NDP A 701      18.287  21.998  30.887  1.00 24.20           N  
-HETATM10277  C2A NDP A 701      17.447  21.402  30.036  1.00 20.78           C  
-HETATM10278  N3A NDP A 701      16.176  21.065  30.207  1.00 22.95           N  
-HETATM10279  C4A NDP A 701      15.756  21.414  31.432  1.00 22.51           C  
-HETATM10280  O3  NDP A 701       7.039  22.088  32.820  1.00 27.17           O  
-HETATM10281  PN  NDP A 701       5.745  22.373  31.881  1.00 24.26           P  
-HETATM10282  O1N NDP A 701       4.497  22.222  32.725  1.00 27.52           O  
-HETATM10283  O2N NDP A 701       5.748  21.365  30.749  1.00 25.33           O  
-HETATM10284  O5D NDP A 701       5.866  23.791  31.343  1.00 25.37           O  
-HETATM10285  C5D NDP A 701       6.533  24.044  30.113  1.00 23.68           C  
-HETATM10286  C4D NDP A 701       7.177  25.409  30.129  1.00 26.47           C  
-HETATM10287  O4D NDP A 701       6.162  26.442  30.215  1.00 26.73           O  
-HETATM10288  C3D NDP A 701       8.126  25.685  31.288  1.00 27.58           C  
-HETATM10289  O3D NDP A 701       9.075  26.656  30.868  1.00 24.45           O  
-HETATM10290  C2D NDP A 701       7.195  26.290  32.332  1.00 27.37           C  
-HETATM10291  O2D NDP A 701       7.880  27.126  33.244  1.00 27.46           O  
-HETATM10292  C1D NDP A 701       6.300  27.138  31.438  1.00 27.20           C  
-HETATM10293  N1N NDP A 701       4.957  27.445  31.939  1.00 29.14           N  
-HETATM10294  C2N NDP A 701       4.211  26.536  32.620  1.00 29.14           C  
-HETATM10295  C3N NDP A 701       2.935  26.741  32.936  1.00 29.33           C  
-HETATM10296  C7N NDP A 701       2.146  25.691  33.260  1.00 29.03           C  
-HETATM10297  O7N NDP A 701       1.024  25.796  33.756  1.00 29.05           O  
-HETATM10298  N7N NDP A 701       2.642  24.488  32.960  1.00 28.92           N  
-HETATM10299  C4N NDP A 701       2.358  27.921  32.612  1.00 30.14           C  
-HETATM10300  C5N NDP A 701       3.126  28.936  32.090  1.00 27.85           C  
-HETATM10301  C6N NDP A 701       4.424  28.702  31.746  1.00 29.64           C  
-HETATM10302  P2B NDP A 701      13.650  17.206  33.088  1.00 24.01           P  
-HETATM10303  O1X NDP A 701      15.026  16.570  33.150  1.00 20.89           O  
-HETATM10304  O2X NDP A 701      13.305  17.780  34.457  1.00 23.09           O  
-HETATM10305  O3X NDP A 701      12.630  16.142  32.734  1.00 20.80           O  
-HETATM10306  PB  GDR A 801       1.891  27.721  40.142  1.00 41.99           P  
-HETATM10307  O3A GDR A 801       1.355  26.197  40.344  1.00 38.92           O  
-HETATM10308  O1B GDR A 801       2.643  28.152  41.394  1.00 39.18           O  
-HETATM10309  O2B GDR A 801       0.696  28.638  39.895  1.00 39.02           O  
-HETATM10310  O3B GDR A 801       2.822  27.720  38.933  1.00 40.95           O  
-HETATM10311  PA  GDR A 801       0.964  25.246  41.609  1.00 38.11           P  
-HETATM10312  O1A GDR A 801      -0.037  24.259  41.132  1.00 35.67           O  
-HETATM10313  O2A GDR A 801       2.213  24.754  42.250  1.00 35.41           O  
-HETATM10314  O5D GDR A 801       0.263  26.219  42.661  1.00 38.29           O  
-HETATM10315  C5D GDR A 801      -0.937  26.916  42.331  1.00 35.78           C  
-HETATM10316  C4D GDR A 801      -1.467  27.658  43.537  1.00 36.89           C  
-HETATM10317  O4D GDR A 801      -1.966  26.698  44.519  1.00 37.12           O  
-HETATM10318  C1D GDR A 801      -1.264  26.869  45.733  1.00 37.08           C  
-HETATM10319  N9  GDR A 801      -1.190  25.582  46.425  1.00 38.72           N  
-HETATM10320  C4  GDR A 801      -0.229  24.602  46.260  1.00 39.40           C  
-HETATM10321  N3  GDR A 801       0.667  24.527  45.251  1.00 39.95           N  
-HETATM10322  C2  GDR A 801       1.446  23.460  45.361  1.00 40.55           C  
-HETATM10323  N2  GDR A 801       2.385  23.220  44.438  1.00 41.98           N  
-HETATM10324  N1  GDR A 801       1.362  22.548  46.383  1.00 39.05           N  
-HETATM10325  C6  GDR A 801       0.453  22.604  47.431  1.00 37.85           C  
-HETATM10326  O6  GDR A 801       0.467  21.726  48.304  1.00 39.31           O  
-HETATM10327  C5  GDR A 801      -0.399  23.737  47.324  1.00 39.09           C  
-HETATM10328  N7  GDR A 801      -1.441  24.157  48.138  1.00 37.74           N  
-HETATM10329  C8  GDR A 801      -1.881  25.247  47.566  1.00 38.48           C  
-HETATM10330  C2D GDR A 801       0.052  27.532  45.348  1.00 36.28           C  
-HETATM10331  O2D GDR A 801       0.593  28.202  46.468  1.00 36.12           O  
-HETATM10332  C3D GDR A 801      -0.442  28.507  44.286  1.00 36.12           C  
-HETATM10333  O3D GDR A 801      -1.095  29.600  44.915  1.00 36.27           O  
-HETATM10334  C1' GDR A 801       2.512  26.939  37.779  1.00 39.98           C  
-HETATM10335  C2' GDR A 801       3.799  26.358  37.174  1.00 38.45           C  
-HETATM10336  O2' GDR A 801       3.459  25.431  36.158  1.00 37.65           O  
-HETATM10337  C3' GDR A 801       4.657  27.474  36.575  1.00 38.50           C  
-HETATM10338  O3' GDR A 801       5.788  26.918  35.922  1.00 34.59           O  
-HETATM10339  C4' GDR A 801       3.832  28.270  35.572  1.00 38.72           C  
-HETATM10340  O4' GDR A 801       4.600  29.352  35.073  1.00 38.05           O  
-HETATM10341  C5' GDR A 801       2.556  28.796  36.244  1.00 39.96           C  
-HETATM10342  O5' GDR A 801       1.788  27.697  36.794  1.00 38.33           O  
-HETATM10343  C6' GDR A 801       1.656  29.519  35.259  1.00 39.33           C  
-HETATM10344  PB  GDR A 802      24.006  54.942  28.701  1.00 46.97           P  
-HETATM10345  O3A GDR A 802      25.402  55.771  28.529  1.00 45.61           O  
-HETATM10346  O1B GDR A 802      23.849  54.019  27.502  1.00 44.75           O  
-HETATM10347  O2B GDR A 802      22.837  55.915  28.778  1.00 44.19           O  
-HETATM10348  O3B GDR A 802      24.111  54.133  29.987  1.00 47.35           O  
-HETATM10349  PA  GDR A 802      26.382  56.180  27.292  1.00 43.61           P  
-HETATM10350  O1A GDR A 802      27.150  57.380  27.713  1.00 45.37           O  
-HETATM10351  O2A GDR A 802      27.123  54.968  26.842  1.00 42.43           O  
-HETATM10352  O5D GDR A 802      25.423  56.595  26.085  1.00 43.05           O  
-HETATM10353  C5D GDR A 802      24.433  57.608  26.249  1.00 41.58           C  
-HETATM10354  C4D GDR A 802      23.764  57.917  24.927  1.00 41.95           C  
-HETATM10355  O4D GDR A 802      24.723  58.572  24.038  1.00 43.08           O  
-HETATM10356  C1D GDR A 802      24.846  57.810  22.853  1.00 41.72           C  
-HETATM10357  N9  GDR A 802      26.189  57.988  22.305  1.00 41.75           N  
-HETATM10358  C4  GDR A 802      27.311  57.245  22.606  1.00 42.00           C  
-HETATM10359  N3  GDR A 802      27.454  56.407  23.656  1.00 41.43           N  
-HETATM10360  C2  GDR A 802      28.656  55.848  23.684  1.00 42.04           C  
-HETATM10361  N2  GDR A 802      28.977  54.994  24.669  1.00 40.12           N  
-HETATM10362  N1  GDR A 802      29.636  56.086  22.753  1.00 41.20           N  
-HETATM10363  C6  GDR A 802      29.514  56.944  21.665  1.00 42.00           C  
-HETATM10364  O6  GDR A 802      30.463  57.091  20.886  1.00 42.24           O  
-HETATM10365  C5  GDR A 802      28.231  57.556  21.624  1.00 42.49           C  
-HETATM10366  N7  GDR A 802      27.704  58.473  20.726  1.00 40.29           N  
-HETATM10367  C8  GDR A 802      26.498  58.704  21.171  1.00 41.45           C  
-HETATM10368  C2D GDR A 802      24.441  56.397  23.245  1.00 42.31           C  
-HETATM10369  O2D GDR A 802      24.051  55.690  22.088  1.00 41.03           O  
-HETATM10370  C3D GDR A 802      23.252  56.709  24.143  1.00 42.27           C  
-HETATM10371  O3D GDR A 802      22.164  57.106  23.319  1.00 45.21           O  
-HETATM10372  C1' GDR A 802      24.819  54.644  31.117  1.00 46.54           C  
-HETATM10373  C2' GDR A 802      25.627  53.512  31.775  1.00 46.14           C  
-HETATM10374  O2' GDR A 802      26.440  54.048  32.808  1.00 43.76           O  
-HETATM10375  C3' GDR A 802      24.683  52.465  32.372  1.00 47.04           C  
-HETATM10376  O3' GDR A 802      25.437  51.498  33.090  1.00 48.14           O  
-HETATM10377  C4' GDR A 802      23.688  53.148  33.315  1.00 47.84           C  
-HETATM10378  O4' GDR A 802      22.755  52.200  33.804  1.00 46.29           O  
-HETATM10379  C5' GDR A 802      22.959  54.281  32.575  1.00 48.90           C  
-HETATM10380  O5' GDR A 802      23.925  55.234  32.073  1.00 47.06           O  
-HETATM10381  C6' GDR A 802      21.978  55.047  33.446  1.00 48.29           C  
-HETATM10382  PB  GDR A 803      32.398   2.799  31.918  1.00 43.18           P  
-HETATM10383  O3A GDR A 803      31.125   1.784  31.820  1.00 42.20           O  
-HETATM10384  O1B GDR A 803      32.551   3.473  30.560  1.00 42.72           O  
-HETATM10385  O2B GDR A 803      33.655   2.006  32.268  1.00 40.19           O  
-HETATM10386  O3B GDR A 803      32.100   3.838  32.997  1.00 44.66           O  
-HETATM10387  PA  GDR A 803      30.109   1.294  30.644  1.00 40.06           P  
-HETATM10388  O1A GDR A 803      29.257   0.212  31.196  1.00 41.27           O  
-HETATM10389  O2A GDR A 803      29.462   2.478  30.021  1.00 38.16           O  
-HETATM10390  O5D GDR A 803      31.062   0.671  29.531  1.00 41.29           O  
-HETATM10391  C5D GDR A 803      32.052  -0.296  29.875  1.00 41.48           C  
-HETATM10392  C4D GDR A 803      32.841  -0.699  28.649  1.00 41.66           C  
-HETATM10393  O4D GDR A 803      31.965  -1.434  27.736  1.00 42.65           O  
-HETATM10394  C1D GDR A 803      31.896  -0.742  26.506  1.00 43.15           C  
-HETATM10395  N9  GDR A 803      30.586  -0.977  25.903  1.00 45.64           N  
-HETATM10396  C4  GDR A 803      29.430  -0.256  26.131  1.00 47.22           C  
-HETATM10397  N3  GDR A 803      29.222   0.616  27.141  1.00 46.53           N  
-HETATM10398  C2  GDR A 803      28.005   1.137  27.104  1.00 46.51           C  
-HETATM10399  N2  GDR A 803      27.622   2.011  28.045  1.00 46.02           N  
-HETATM10400  N1  GDR A 803      27.070   0.835  26.146  1.00 47.22           N  
-HETATM10401  C6  GDR A 803      27.258  -0.057  25.096  1.00 47.89           C  
-HETATM10402  O6  GDR A 803      26.343  -0.256  24.285  1.00 47.33           O  
-HETATM10403  C5  GDR A 803      28.559  -0.633  25.128  1.00 47.54           C  
-HETATM10404  N7  GDR A 803      29.148  -1.569  24.292  1.00 47.79           N  
-HETATM10405  C8  GDR A 803      30.342  -1.746  24.791  1.00 46.74           C  
-HETATM10406  C2D GDR A 803      32.257   0.700  26.839  1.00 42.53           C  
-HETATM10407  O2D GDR A 803      32.697   1.371  25.675  1.00 41.09           O  
-HETATM10408  C3D GDR A 803      33.394   0.460  27.822  1.00 41.57           C  
-HETATM10409  O3D GDR A 803      34.537   0.029  27.095  1.00 44.61           O  
-HETATM10410  C1' GDR A 803      31.438   3.469  34.208  1.00 43.70           C  
-HETATM10411  C2' GDR A 803      30.685   4.678  34.779  1.00 42.66           C  
-HETATM10412  O2' GDR A 803      29.907   4.261  35.891  1.00 42.59           O  
-HETATM10413  C3' GDR A 803      31.676   5.748  35.235  1.00 42.18           C  
-HETATM10414  O3' GDR A 803      30.974   6.809  35.862  1.00 42.49           O  
-HETATM10415  C4' GDR A 803      32.663   5.133  36.225  1.00 43.46           C  
-HETATM10416  O4' GDR A 803      33.627   6.096  36.609  1.00 41.71           O  
-HETATM10417  C5' GDR A 803      33.351   3.931  35.581  1.00 44.12           C  
-HETATM10418  O5' GDR A 803      32.359   2.953  35.182  1.00 45.12           O  
-HETATM10419  C6' GDR A 803      34.312   3.239  36.525  1.00 46.43           C  
-HETATM10420  PA  NDP B 702      31.494  50.982  36.355  1.00 25.49           P  
-HETATM10421  O1A NDP B 702      31.427  50.262  35.064  1.00 27.27           O  
-HETATM10422  O2A NDP B 702      32.401  52.155  36.488  1.00 26.93           O  
-HETATM10423  O5B NDP B 702      31.922  49.968  37.501  1.00 27.20           O  
-HETATM10424  C5B NDP B 702      31.486  48.608  37.504  1.00 24.88           C  
-HETATM10425  C4B NDP B 702      32.076  47.902  38.698  1.00 25.00           C  
-HETATM10426  O4B NDP B 702      31.621  46.512  38.723  1.00 23.02           O  
-HETATM10427  C3B NDP B 702      33.601  47.818  38.674  1.00 23.66           C  
-HETATM10428  O3B NDP B 702      34.085  47.796  40.011  1.00 27.49           O  
-HETATM10429  C2B NDP B 702      33.805  46.454  38.033  1.00 23.37           C  
-HETATM10430  O2B NDP B 702      35.096  45.909  38.214  1.00 24.99           O  
-HETATM10431  C1B NDP B 702      32.754  45.664  38.803  1.00 24.39           C  
-HETATM10432  N9A NDP B 702      32.418  44.367  38.214  1.00 24.22           N  
-HETATM10433  C8A NDP B 702      32.065  44.088  36.918  1.00 23.82           C  
-HETATM10434  N7A NDP B 702      31.884  42.811  36.683  1.00 25.10           N  
-HETATM10435  C5A NDP B 702      32.132  42.208  37.908  1.00 24.67           C  
-HETATM10436  C6A NDP B 702      32.089  40.864  38.332  1.00 25.32           C  
-HETATM10437  N6A NDP B 702      31.779  39.839  37.530  1.00 23.27           N  
-HETATM10438  N1A NDP B 702      32.379  40.606  39.627  1.00 26.49           N  
-HETATM10439  C2A NDP B 702      32.694  41.631  40.429  1.00 24.80           C  
-HETATM10440  N3A NDP B 702      32.769  42.931  40.146  1.00 25.59           N  
-HETATM10441  C4A NDP B 702      32.470  43.155  38.858  1.00 24.01           C  
-HETATM10442  O3  NDP B 702      30.003  51.459  36.779  1.00 28.85           O  
-HETATM10443  PN  NDP B 702      29.385  52.726  37.586  1.00 27.98           P  
-HETATM10444  O1N NDP B 702      29.342  53.916  36.642  1.00 26.43           O  
-HETATM10445  O2N NDP B 702      30.283  53.022  38.773  1.00 26.46           O  
-HETATM10446  O5D NDP B 702      27.990  52.358  38.056  1.00 28.89           O  
-HETATM10447  C5D NDP B 702      27.800  51.635  39.268  1.00 30.12           C  
-HETATM10448  C4D NDP B 702      26.609  50.714  39.150  1.00 30.27           C  
-HETATM10449  O4D NDP B 702      25.408  51.495  38.897  1.00 29.00           O  
-HETATM10450  C3D NDP B 702      26.691  49.704  38.011  1.00 31.10           C  
-HETATM10451  O3D NDP B 702      25.970  48.530  38.362  1.00 31.09           O  
-HETATM10452  C2D NDP B 702      26.002  50.438  36.868  1.00 30.92           C  
-HETATM10453  O2D NDP B 702      25.453  49.539  35.926  1.00 31.27           O  
-HETATM10454  C1D NDP B 702      24.891  51.159  37.626  1.00 32.54           C  
-HETATM10455  N1N NDP B 702      24.328  52.374  37.024  1.00 35.07           N  
-HETATM10456  C2N NDP B 702      25.086  53.261  36.330  1.00 36.53           C  
-HETATM10457  C3N NDP B 702      24.644  54.463  35.982  1.00 36.96           C  
-HETATM10458  C7N NDP B 702      25.527  55.426  35.647  1.00 37.45           C  
-HETATM10459  O7N NDP B 702      25.233  56.465  35.044  1.00 35.39           O  
-HETATM10460  N7N NDP B 702      26.779  55.209  36.046  1.00 35.47           N  
-HETATM10461  C4N NDP B 702      23.377  54.811  36.294  1.00 36.85           C  
-HETATM10462  C5N NDP B 702      22.504  53.848  36.730  1.00 33.53           C  
-HETATM10463  C6N NDP B 702      22.977  52.625  37.106  1.00 35.90           C  
-HETATM10464  P2B NDP B 702      36.204  46.178  37.245  1.00 26.12           P  
-HETATM10465  O1X NDP B 702      37.206  45.044  37.360  1.00 26.23           O  
-HETATM10466  O2X NDP B 702      35.681  46.235  35.822  1.00 24.55           O  
-HETATM10467  O3X NDP B 702      36.910  47.484  37.559  1.00 24.66           O  
-HETATM10468  PA  NDP C 703      24.689   7.544  38.892  1.00 27.85           P  
-HETATM10469  O1A NDP C 703      24.831   8.142  37.542  1.00 29.19           O  
-HETATM10470  O2A NDP C 703      23.758   6.403  39.086  1.00 29.80           O  
-HETATM10471  O5B NDP C 703      24.227   8.676  39.900  1.00 27.44           O  
-HETATM10472  C5B NDP C 703      24.635  10.025  39.725  1.00 25.85           C  
-HETATM10473  C4B NDP C 703      23.986  10.880  40.775  1.00 24.93           C  
-HETATM10474  O4B NDP C 703      24.458  12.249  40.616  1.00 23.06           O  
-HETATM10475  C3B NDP C 703      22.462  10.966  40.669  1.00 24.93           C  
-HETATM10476  O3B NDP C 703      21.915  11.118  41.972  1.00 23.46           O  
-HETATM10477  C2B NDP C 703      22.292  12.260  39.881  1.00 22.58           C  
-HETATM10478  O2B NDP C 703      21.018  12.870  39.983  1.00 26.52           O  
-HETATM10479  C1B NDP C 703      23.342  13.112  40.576  1.00 24.36           C  
-HETATM10480  N9A NDP C 703      23.705  14.317  39.838  1.00 25.46           N  
-HETATM10481  C8A NDP C 703      24.072  14.431  38.519  1.00 24.82           C  
-HETATM10482  N7A NDP C 703      24.231  15.668  38.122  1.00 24.07           N  
-HETATM10483  C5A NDP C 703      23.951  16.420  39.255  1.00 24.65           C  
-HETATM10484  C6A NDP C 703      23.954  17.805  39.499  1.00 22.68           C  
-HETATM10485  N6A NDP C 703      24.262  18.718  38.578  1.00 21.43           N  
-HETATM10486  N1A NDP C 703      23.628  18.223  40.744  1.00 24.62           N  
-HETATM10487  C2A NDP C 703      23.325  17.304  41.672  1.00 22.50           C  
-HETATM10488  N3A NDP C 703      23.293  15.979  41.563  1.00 22.51           N  
-HETATM10489  C4A NDP C 703      23.620  15.599  40.317  1.00 23.69           C  
-HETATM10490  O3  NDP C 703      26.164   7.130  39.431  1.00 29.68           O  
-HETATM10491  PN  NDP C 703      26.752   6.020  40.458  1.00 28.17           P  
-HETATM10492  O1N NDP C 703      26.842   4.695  39.726  1.00 32.90           O  
-HETATM10493  O2N NDP C 703      25.802   5.918  41.632  1.00 28.40           O  
-HETATM10494  O5D NDP C 703      28.132   6.470  40.926  1.00 29.75           O  
-HETATM10495  C5D NDP C 703      28.272   7.344  42.040  1.00 26.89           C  
-HETATM10496  C4D NDP C 703      29.462   8.256  41.853  1.00 29.66           C  
-HETATM10497  O4D NDP C 703      30.682   7.468  41.786  1.00 29.68           O  
-HETATM10498  C3D NDP C 703      29.459   9.101  40.585  1.00 28.61           C  
-HETATM10499  O3D NDP C 703      30.214  10.282  40.822  1.00 25.92           O  
-HETATM10500  C2D NDP C 703      30.187   8.205  39.592  1.00 30.63           C  
-HETATM10501  O2D NDP C 703      30.822   8.954  38.578  1.00 28.38           O  
-HETATM10502  C1D NDP C 703      31.247   7.582  40.497  1.00 30.73           C  
-HETATM10503  N1N NDP C 703      31.780   6.269  40.117  1.00 33.88           N  
-HETATM10504  C2N NDP C 703      31.014   5.327  39.523  1.00 36.02           C  
-HETATM10505  C3N NDP C 703      31.480   4.152  39.127  1.00 38.14           C  
-HETATM10506  C7N NDP C 703      30.621   3.127  38.942  1.00 37.00           C  
-HETATM10507  O7N NDP C 703      30.894   2.088  38.336  1.00 35.68           O  
-HETATM10508  N7N NDP C 703      29.423   3.286  39.501  1.00 35.50           N  
-HETATM10509  C4N NDP C 703      32.801   3.893  39.246  1.00 38.37           C  
-HETATM10510  C5N NDP C 703      33.604   4.768  39.934  1.00 35.58           C  
-HETATM10511  C6N NDP C 703      33.101   5.959  40.367  1.00 35.13           C  
-HETATM10512  P2B NDP C 703      19.908  12.532  39.036  1.00 27.29           P  
-HETATM10513  O1X NDP C 703      18.927  13.691  39.010  1.00 27.94           O  
-HETATM10514  O2X NDP C 703      20.438  12.300  37.634  1.00 26.55           O  
-HETATM10515  O3X NDP C 703      19.178  11.284  39.493  1.00 27.39           O  
-HETATM10516  PA  NDP D 704      48.482  37.441  32.804  1.00 31.22           P  
-HETATM10517  O1A NDP D 704      47.916  37.327  34.169  1.00 29.40           O  
-HETATM10518  O2A NDP D 704      49.449  38.536  32.510  1.00 30.78           O  
-HETATM10519  O5B NDP D 704      47.295  37.589  31.759  1.00 30.00           O  
-HETATM10520  C5B NDP D 704      46.111  36.809  31.867  1.00 28.23           C  
-HETATM10521  C4B NDP D 704      45.192  37.146  30.724  1.00 27.81           C  
-HETATM10522  O4B NDP D 704      43.958  36.374  30.841  1.00 25.03           O  
-HETATM10523  C3B NDP D 704      44.742  38.606  30.693  1.00 27.25           C  
-HETATM10524  O3B NDP D 704      44.562  38.990  29.337  1.00 30.45           O  
-HETATM10525  C2B NDP D 704      43.389  38.514  31.380  1.00 25.87           C  
-HETATM10526  O2B NDP D 704      42.534  39.620  31.155  1.00 27.94           O  
-HETATM10527  C1B NDP D 704      42.859  37.252  30.712  1.00 24.85           C  
-HETATM10528  N9A NDP D 704      41.708  36.660  31.384  1.00 23.74           N  
-HETATM10529  C8A NDP D 704      41.564  36.397  32.725  1.00 24.39           C  
-HETATM10530  N7A NDP D 704      40.369  35.976  33.055  1.00 23.84           N  
-HETATM10531  C5A NDP D 704      39.677  35.961  31.852  1.00 23.81           C  
-HETATM10532  C6A NDP D 704      38.359  35.607  31.529  1.00 25.48           C  
-HETATM10533  N6A NDP D 704      37.463  35.198  32.431  1.00 24.89           N  
-HETATM10534  N1A NDP D 704      37.985  35.692  30.230  1.00 26.51           N  
-HETATM10535  C2A NDP D 704      38.885  36.116  29.332  1.00 24.58           C  
-HETATM10536  N3A NDP D 704      40.153  36.486  29.519  1.00 23.96           N  
-HETATM10537  C4A NDP D 704      40.489  36.381  30.815  1.00 24.11           C  
-HETATM10538  O3  NDP D 704      49.172  36.028  32.394  1.00 30.09           O  
-HETATM10539  PN  NDP D 704      50.513  35.587  31.593  1.00 28.93           P  
-HETATM10540  O1N NDP D 704      51.722  35.848  32.476  1.00 31.47           O  
-HETATM10541  O2N NDP D 704      50.597  36.415  30.321  1.00 25.95           O  
-HETATM10542  O5D NDP D 704      50.410  34.108  31.262  1.00 30.89           O  
-HETATM10543  C5D NDP D 704      49.724  33.664  30.097  1.00 28.81           C  
-HETATM10544  C4D NDP D 704      49.135  32.297  30.333  1.00 29.73           C  
-HETATM10545  O4D NDP D 704      50.201  31.341  30.581  1.00 30.39           O  
-HETATM10546  C3D NDP D 704      48.211  32.201  31.539  1.00 31.10           C  
-HETATM10547  O3D NDP D 704      47.245  31.184  31.310  1.00 28.00           O  
-HETATM10548  C2D NDP D 704      49.166  31.801  32.660  1.00 32.30           C  
-HETATM10549  O2D NDP D 704      48.502  31.081  33.679  1.00 32.44           O  
-HETATM10550  C1D NDP D 704      50.113  30.868  31.911  1.00 31.16           C  
-HETATM10551  N1N NDP D 704      51.479  30.703  32.428  1.00 33.59           N  
-HETATM10552  C2N NDP D 704      52.182  31.729  32.970  1.00 34.05           C  
-HETATM10553  C3N NDP D 704      53.366  31.567  33.546  1.00 34.99           C  
-HETATM10554  C7N NDP D 704      54.207  32.616  33.632  1.00 34.94           C  
-HETATM10555  O7N NDP D 704      55.355  32.556  34.085  1.00 30.94           O  
-HETATM10556  N7N NDP D 704      53.724  33.768  33.166  1.00 35.08           N  
-HETATM10557  C4N NDP D 704      53.859  30.319  33.684  1.00 35.52           C  
-HETATM10558  C5N NDP D 704      53.321  29.303  32.938  1.00 35.14           C  
-HETATM10559  C6N NDP D 704      52.118  29.484  32.318  1.00 34.59           C  
-HETATM10560  P2B NDP D 704      42.527  40.795  32.080  1.00 28.86           P  
-HETATM10561  O1X NDP D 704      41.169  41.467  32.045  1.00 27.04           O  
-HETATM10562  O2X NDP D 704      42.814  40.333  33.497  1.00 27.16           O  
-HETATM10563  O3X NDP D 704      43.580  41.803  31.665  1.00 27.42           O  
-HETATM10564  O   HOH A 804      14.478  28.760  29.686  1.00 23.70           O  
-HETATM10565  O   HOH A 805       8.512  19.690  40.872  1.00 14.87           O  
-HETATM10566  O   HOH A 806      15.419  21.912  36.320  1.00 22.92           O  
-HETATM10567  O   HOH A 807      11.098  28.071  29.006  1.00 21.50           O  
-HETATM10568  O   HOH A 808       4.353  29.261  27.620  1.00 25.30           O  
-HETATM10569  O   HOH A 809      13.897  32.894  25.143  1.00 26.89           O  
-HETATM10570  O   HOH A 810       4.271  19.973  34.800  1.00 26.59           O  
-HETATM10571  O   HOH A 811       4.877  35.927  40.685  1.00 22.19           O  
-HETATM10572  O   HOH A 812      -4.971  29.041  31.833  1.00 27.32           O  
-HETATM10573  O   HOH A 813       8.289  44.324  20.258  1.00 38.72           O  
-HETATM10574  O   HOH A 814      23.093  33.041  35.133  1.00 22.14           O  
-HETATM10575  O   HOH A 815       5.088  33.087  44.493  1.00 22.45           O  
-HETATM10576  O   HOH A 816      22.663  18.227  31.821  1.00 26.50           O  
-HETATM10577  O   HOH A 817       5.502  33.393  41.879  1.00 25.28           O  
-HETATM10578  O   HOH A 818      -3.691   8.318  41.659  1.00 26.36           O  
-HETATM10579  O   HOH A 819      -1.535  17.652  15.188  1.00 33.21           O  
-HETATM10580  O   HOH A 820      13.287  20.161  35.673  1.00 18.60           O  
-HETATM10581  O   HOH A 821      12.497  30.411  30.474  1.00 22.64           O  
-HETATM10582  O   HOH A 822       4.520  25.956  40.969  1.00 29.26           O  
-HETATM10583  O   HOH A 823       2.085  30.661  42.073  1.00 31.39           O  
-HETATM10584  O   HOH A 824      13.853  45.998  23.365  1.00 24.47           O  
-HETATM10585  O   HOH A 825      13.664  17.597  27.998  1.00 27.34           O  
-HETATM10586  O   HOH A 826      23.068   7.684  31.508  1.00 20.17           O  
-HETATM10587  O   HOH A 827       7.562  35.332  28.013  1.00 22.76           O  
-HETATM10588  O   HOH A 828      -1.288  24.458  39.025  1.00 41.06           O  
-HETATM10589  O   HOH A 829      -8.129  24.356  27.827  1.00 32.64           O  
-HETATM10590  O   HOH A 830      20.598  21.079  34.897  1.00 24.32           O  
-HETATM10591  O   HOH A 831      -5.520  39.856  24.941  1.00 28.70           O  
-HETATM10592  O   HOH A 832       3.266  20.505  46.350  1.00 35.09           O  
-HETATM10593  O   HOH A 833      22.220  16.688  29.376  1.00 26.03           O  
-HETATM10594  O   HOH A 834      -4.304  37.135  24.142  1.00 30.04           O  
-HETATM10595  O   HOH A 835      19.557  36.452  33.452  1.00 23.53           O  
-HETATM10596  O   HOH A 836      22.034  16.317  33.536  1.00 23.12           O  
-HETATM10597  O   HOH A 837       4.178  26.924  28.671  1.00 26.30           O  
-HETATM10598  O   HOH A 838       7.286  20.853  28.621  1.00 27.15           O  
-HETATM10599  O   HOH A 839      15.643  20.601  27.348  1.00 20.91           O  
-HETATM10600  O   HOH A 840      29.271  20.837  26.220  1.00 23.30           O  
-HETATM10601  O   HOH A 841       1.126  30.643  49.618  1.00 35.40           O  
-HETATM10602  O   HOH A 842      19.860   9.689  30.612  1.00 29.00           O  
-HETATM10603  O   HOH A 843      27.942  36.317  22.569  1.00 31.15           O  
-HETATM10604  O   HOH A 844       2.961  35.887  16.052  1.00 34.63           O  
-HETATM10605  O   HOH A 845       9.253  34.126  29.854  1.00 21.64           O  
-HETATM10606  O   HOH A 846       9.090  12.631  30.225  1.00 27.11           O  
-HETATM10607  O   HOH A 847      15.201  16.368  30.331  1.00 27.31           O  
-HETATM10608  O   HOH A 848       3.638  24.848  47.679  1.00 38.69           O  
-HETATM10609  O   HOH A 849       5.819  14.232  38.669  1.00 38.36           O  
-HETATM10610  O   HOH A 850       1.787  14.451  44.778  1.00 29.59           O  
-HETATM10611  O   HOH A 851       6.272  18.496  35.581  1.00 40.65           O  
-HETATM10612  O   HOH A 852      -8.631  33.902  39.192  1.00 31.25           O  
-HETATM10613  O   HOH A 853      19.968  28.101  47.634  1.00 32.57           O  
-HETATM10614  O   HOH A 854      28.104   5.597  37.140  1.00 30.56           O  
-HETATM10615  O   HOH A 855      15.422   8.206  29.626  1.00 40.82           O  
-HETATM10616  O   HOH A 856     -11.772   6.478  36.075  1.00 32.64           O  
-HETATM10617  O   HOH A 857     -10.600  27.489  33.629  0.50 14.34           O  
-HETATM10618  O   HOH A 858      26.616  52.546  28.059  1.00 34.28           O  
-HETATM10619  O   HOH A 859      -0.625  13.587  45.545  1.00 36.19           O  
-HETATM10620  O   HOH A 860      26.658  30.084  19.752  1.00 34.27           O  
-HETATM10621  O   HOH A 861      22.120  12.543  19.535  1.00 35.36           O  
-HETATM10622  O   HOH A 862      28.201  52.841  34.133  1.00 31.84           O  
-HETATM10623  O   HOH A 863     -16.062  22.512  31.595  1.00 38.61           O  
-HETATM10624  O   HOH A 864       2.884  31.103  44.677  1.00 27.08           O  
-HETATM10625  O   HOH A 865      -0.295  14.761  50.783  1.00 36.19           O  
-HETATM10626  O   HOH A 866      -2.392  38.169  41.596  1.00 27.00           O  
-HETATM10627  O   HOH A 867       0.241  27.251  49.210  1.00 30.00           O  
-HETATM10628  O   HOH A 868      -1.032  17.429  21.588  1.00 29.92           O  
-HETATM10629  O   HOH A 869       3.555  43.430  30.081  1.00 44.76           O  
-HETATM10630  O   HOH A 870      -3.383  31.130  35.923  1.00 30.32           O  
-HETATM10631  O   HOH A 871       3.901  17.971  47.886  1.00 45.88           O  
-HETATM10632  O   HOH A 872       2.536  12.237  44.115  1.00 41.10           O  
-HETATM10633  O   HOH A 873     -12.787  29.567  47.876  1.00 44.88           O  
-HETATM10634  O   HOH A 874     -17.041   9.661  35.014  1.00 40.32           O  
-HETATM10635  O   HOH A 875      32.221  26.013  24.071  1.00 34.29           O  
-HETATM10636  O   HOH A 876      -0.479  13.732  48.550  1.00 30.39           O  
-HETATM10637  O   HOH A 877      22.863  40.741  22.158  1.00 30.63           O  
-HETATM10638  O   HOH A 878      -6.680  42.558  25.313  1.00 45.31           O  
-HETATM10639  O   HOH A 879      -7.976  42.952  29.962  1.00 42.83           O  
-HETATM10640  O   HOH A 880      24.702   2.515  26.061  1.00 30.84           O  
-HETATM10641  O   HOH A 881     -12.000   3.579  36.995  1.00 65.47           O  
-HETATM10642  O   HOH A 882      14.293  21.265  49.409  1.00 37.87           O  
-HETATM10643  O   HOH A 883     -11.196  37.420  39.707  1.00 50.39           O  
-HETATM10644  O   HOH A 884      -1.969   8.824  53.753  1.00 36.39           O  
-HETATM10645  O   HOH A 885      28.939  25.300  31.479  1.00 39.29           O  
-HETATM10646  O   HOH A 886       7.539  35.204   8.361  1.00 39.87           O  
-HETATM10647  O   HOH A 887      17.096  25.998   5.468  1.00 38.00           O  
-HETATM10648  O   HOH A 888      16.072  29.166   5.871  1.00 43.98           O  
-HETATM10649  O   HOH A 889      26.689  23.990  33.443  1.00 37.16           O  
-HETATM10650  O   HOH A 890      -2.825  10.942  35.478  1.00 38.89           O  
-HETATM10651  O   HOH A 891       7.936  20.173  43.640  1.00 37.58           O  
-HETATM10652  O   HOH A 892      -0.729  43.792  22.593  1.00 37.09           O  
-HETATM10653  O   HOH A 893       3.292  16.453  53.941  1.00 50.80           O  
-HETATM10654  O   HOH A 894      17.351  10.342  19.073  1.00 41.62           O  
-HETATM10655  O   HOH A 895       5.709  13.921  11.268  1.00 47.50           O  
-HETATM10656  O   HOH A 896      13.998  35.010  12.539  1.00 35.89           O  
-HETATM10657  O   HOH A 897      -0.670  38.247  44.727  1.00 34.66           O  
-HETATM10658  O   HOH A 898      -9.115  19.305  23.566  1.00 40.85           O  
-HETATM10659  O   HOH A 899      -7.372  24.635  21.537  1.00 38.70           O  
-HETATM10660  O   HOH A 900     -15.279   3.622  37.305  1.00 48.04           O  
-HETATM10661  O   HOH A 901      -0.915  10.977  46.051  1.00 34.55           O  
-HETATM10662  O   HOH A 902     -16.328  24.295  33.581  1.00 43.13           O  
-HETATM10663  O   HOH A 903      -2.700  43.564  24.586  1.00 37.06           O  
-HETATM10664  O   HOH A 904      19.978  10.002  23.757  1.00 50.86           O  
-HETATM10665  O   HOH A 905       6.355  17.496  49.520  1.00 40.09           O  
-HETATM10666  O   HOH A 906      -2.805  19.369  21.211  1.00 35.53           O  
-HETATM10667  O   HOH A 907       6.347  17.740  39.509  1.00 33.60           O  
-HETATM10668  O   HOH A 908       0.228  40.300  15.916  1.00 42.61           O  
-HETATM10669  O   HOH A 909     -18.090  17.638  40.613  1.00 40.83           O  
-HETATM10670  O   HOH A 910     -18.221  11.733  51.366  1.00 57.98           O  
-HETATM10671  O   HOH A 911       7.807  18.586  47.468  1.00 48.19           O  
-HETATM10672  O   HOH A 912     -11.705  11.353  30.954  1.00 41.90           O  
-HETATM10673  O   HOH A 913       1.774  45.744  40.755  1.00 38.93           O  
-HETATM10674  O   HOH A 914      -3.569  40.471  43.041  1.00 35.73           O  
-HETATM10675  O   HOH A 915     -14.655  28.252  34.282  1.00 34.86           O  
-HETATM10676  O   HOH A 916      30.021   5.088  31.016  1.00 37.83           O  
-HETATM10677  O   HOH A 917      -2.850  16.349  17.266  1.00 40.05           O  
-HETATM10678  O   HOH A 918      26.658  28.726  22.161  1.00 40.45           O  
-HETATM10679  O   HOH A 919      30.424  27.815  12.502  1.00 43.84           O  
-HETATM10680  O   HOH A 920     -18.155   7.786  42.954  1.00 49.57           O  
-HETATM10681  O   HOH A 921     -11.468  42.473  26.075  1.00 45.18           O  
-HETATM10682  O   HOH A 922       0.701  31.379  37.016  1.00 34.62           O  
-HETATM10683  O   HOH A 923       5.944  19.374   7.404  1.00 40.85           O  
-HETATM10684  O   HOH A 924       2.413  10.166  29.189  1.00 43.07           O  
-HETATM10685  O   HOH A 925      18.400  40.637  25.322  1.00 48.40           O  
-HETATM10686  O   HOH A 926      10.576  39.881  12.437  1.00 40.09           O  
-HETATM10687  O   HOH A 927      -4.480  13.147  36.008  1.00 39.21           O  
-HETATM10688  O   HOH A 928     -19.403  24.021  34.394  1.00 41.41           O  
-HETATM10689  O   HOH A 929      16.080  14.583  34.656  1.00 29.90           O  
-HETATM10690  O   HOH A 930       3.737  24.196   9.911  1.00 54.77           O  
-HETATM10691  O   HOH A 931       5.273  23.832  34.967  1.00 32.80           O  
-HETATM10692  O   HOH A 932      -8.405  10.593  40.902  1.00 39.62           O  
-HETATM10693  O   HOH A 933      -3.804  13.022  27.618  1.00 31.15           O  
-HETATM10694  O   HOH A 934      -9.973  28.161  36.081  1.00 36.47           O  
-HETATM10695  O   HOH A 935     -11.197  43.194  23.468  1.00 42.26           O  
-HETATM10696  O   HOH A 936       2.193  36.226  50.297  1.00 41.53           O  
-HETATM10697  O   HOH A 937      29.472  33.951  11.729  1.00 43.64           O  
-HETATM10698  O   HOH A 938       1.721  16.470  50.824  1.00 52.83           O  
-HETATM10699  O   HOH A 939      -0.462  38.615  49.008  1.00 57.70           O  
-HETATM10700  O   HOH A 940       2.068   3.574  39.369  1.00 53.13           O  
-HETATM10701  O   HOH A 941      -3.029  44.640  26.957  1.00 42.19           O  
-HETATM10702  O   HOH A 942     -12.923   6.772  33.379  1.00 39.20           O  
-HETATM10703  O   HOH A 943      -4.727   5.926  33.981  1.00 14.91           O  
-HETATM10704  O   HOH B 703      22.913  44.312  38.968  1.00 18.78           O  
-HETATM10705  O   HOH B 704      28.060  29.594  41.180  1.00 30.73           O  
-HETATM10706  O   HOH B 705      24.296  53.431  40.340  1.00 28.66           O  
-HETATM10707  O   HOH B 706      32.956  43.748  42.887  1.00 21.51           O  
-HETATM10708  O   HOH B 707      39.470  51.873  40.291  1.00 22.12           O  
-HETATM10709  O   HOH B 708      20.415  43.035  43.939  1.00 26.81           O  
-HETATM10710  O   HOH B 709      18.618  46.748  39.052  1.00 25.43           O  
-HETATM10711  O   HOH B 710       7.817  39.891  45.178  1.00 22.67           O  
-HETATM10712  O   HOH B 711      33.348  43.187  20.760  1.00 37.12           O  
-HETATM10713  O   HOH B 712      27.248  36.122  25.374  1.00 27.06           O  
-HETATM10714  O   HOH B 713      24.070  66.120  40.456  1.00 30.94           O  
-HETATM10715  O   HOH B 714      24.050  61.375  15.059  1.00 41.63           O  
-HETATM10716  O   HOH B 715      37.198  37.175  39.058  1.00 26.50           O  
-HETATM10717  O   HOH B 716      18.930  35.996  36.184  1.00 18.85           O  
-HETATM10718  O   HOH B 717      12.395  59.863  43.395  1.00 30.37           O  
-HETATM10719  O   HOH B 718      25.112  43.067  39.806  1.00 25.19           O  
-HETATM10720  O   HOH B 719      32.446  43.217  33.714  1.00 21.27           O  
-HETATM10721  O   HOH B 720      16.767  48.094  40.623  1.00 24.30           O  
-HETATM10722  O   HOH B 721      33.398  45.529  34.266  1.00 30.07           O  
-HETATM10723  O   HOH B 722      34.258  38.428  35.756  1.00 28.49           O  
-HETATM10724  O   HOH B 723      47.404  39.601  39.911  1.00 29.76           O  
-HETATM10725  O   HOH B 724      16.795  50.158  27.807  1.00 25.08           O  
-HETATM10726  O   HOH B 725      31.056  51.562  40.873  1.00 27.81           O  
-HETATM10727  O   HOH B 726      39.158  38.204  37.542  1.00 35.61           O  
-HETATM10728  O   HOH B 727      24.890  46.357  40.293  1.00 23.68           O  
-HETATM10729  O   HOH B 728      39.323  44.436  36.155  1.00 31.42           O  
-HETATM10730  O   HOH B 729      14.602  32.570  47.492  1.00 32.28           O  
-HETATM10731  O   HOH B 730      21.426  52.633  24.230  1.00 31.59           O  
-HETATM10732  O   HOH B 731      19.360  49.891  26.941  1.00 25.56           O  
-HETATM10733  O   HOH B 732      31.360  26.644  47.351  1.00 33.35           O  
-HETATM10734  O   HOH B 733      37.323  44.818  40.366  1.00 28.62           O  
-HETATM10735  O   HOH B 734      41.206  58.129  32.948  1.00 45.90           O  
-HETATM10736  O   HOH B 735      39.328  57.066  34.951  1.00 45.64           O  
-HETATM10737  O   HOH B 736      41.808  64.385  28.272  1.00 27.67           O  
-HETATM10738  O   HOH B 737      21.437  53.871  26.577  1.00 35.49           O  
-HETATM10739  O   HOH B 738      19.949  50.201  24.325  1.00 28.46           O  
-HETATM10740  O   HOH B 739       8.099  50.776  37.569  1.00 38.62           O  
-HETATM10741  O   HOH B 740       9.477  60.318  41.754  1.00 33.48           O  
-HETATM10742  O   HOH B 741      31.546  47.904  22.151  1.00 40.92           O  
-HETATM10743  O   HOH B 742      20.686  61.767  36.177  1.00 26.73           O  
-HETATM10744  O   HOH B 743      35.296  46.405  42.361  1.00 25.87           O  
-HETATM10745  O   HOH B 744      19.404  59.432  32.270  1.00 33.19           O  
-HETATM10746  O   HOH B 745      37.983  54.082  31.443  1.00 33.57           O  
-HETATM10747  O   HOH B 746      25.624  31.269  50.587  1.00 33.92           O  
-HETATM10748  O   HOH B 747      17.310  43.293  56.414  1.00 37.33           O  
-HETATM10749  O   HOH B 748      26.166  58.930  29.977  1.00 41.67           O  
-HETATM10750  O   HOH B 749       4.303  49.844  36.296  1.00 52.08           O  
-HETATM10751  O   HOH B 750      21.903  52.896  41.188  1.00 29.25           O  
-HETATM10752  O   HOH B 751      32.197  54.438  23.152  1.00 35.47           O  
-HETATM10753  O   HOH B 752      25.327  56.122  19.633  1.00 29.56           O  
-HETATM10754  O   HOH B 753      20.300  69.130  15.997  1.00 42.47           O  
-HETATM10755  O   HOH B 754      35.272  30.349  45.081  1.00 43.87           O  
-HETATM10756  O   HOH B 755       6.512  51.489  27.390  1.00 33.88           O  
-HETATM10757  O   HOH B 756      29.361  62.659  47.825  1.00 49.98           O  
-HETATM10758  O   HOH B 757       5.920  48.502  27.673  1.00 40.15           O  
-HETATM10759  O   HOH B 758       6.700  46.899  33.989  1.00 40.70           O  
-HETATM10760  O   HOH B 759      10.762  49.693  22.125  1.00 38.34           O  
-HETATM10761  O   HOH B 760      33.510  52.713  33.925  1.00 38.07           O  
-HETATM10762  O   HOH B 761       3.415  56.168  36.185  1.00 44.35           O  
-HETATM10763  O   HOH B 762       9.387  55.067  51.613  1.00 41.91           O  
-HETATM10764  O   HOH B 763      16.019  66.138  41.145  1.00 46.99           O  
-HETATM10765  O   HOH B 764       7.299  46.499  48.170  1.00 43.42           O  
-HETATM10766  O   HOH B 765      27.542  66.072  47.500  1.00 41.98           O  
-HETATM10767  O   HOH B 766      28.189  74.643  18.233  1.00 52.61           O  
-HETATM10768  O   HOH B 767      38.290  38.007  41.343  1.00 41.79           O  
-HETATM10769  O   HOH B 768      28.540  31.468  36.677  1.00 35.32           O  
-HETATM10770  O   HOH B 769      22.070  51.271  58.699  1.00 54.99           O  
-HETATM10771  O   HOH B 770      16.525  38.291  55.561  1.00 42.22           O  
-HETATM10772  O   HOH B 771      13.514  56.649  26.121  1.00 31.88           O  
-HETATM10773  O   HOH B 772      42.241  76.747  21.207  1.00 46.99           O  
-HETATM10774  O   HOH B 773      37.172  58.952  18.923  1.00 50.86           O  
-HETATM10775  O   HOH B 774      20.974  60.563  14.656  1.00 44.26           O  
-HETATM10776  O   HOH B 775       8.323  51.404  44.376  1.00 46.87           O  
-HETATM10777  O   HOH B 776      42.130  72.702  34.654  1.00 50.39           O  
-HETATM10778  O   HOH B 777      43.218  56.844  28.225  1.00 44.90           O  
-HETATM10779  O   HOH B 778      31.778  54.740  34.901  1.00 34.26           O  
-HETATM10780  O   HOH B 779      38.403  59.729  21.608  1.00 28.98           O  
-HETATM10781  O   HOH B 780      10.556  54.726  55.473  1.00 37.31           O  
-HETATM10782  O   HOH B 781      13.754  54.675  22.704  1.00 36.76           O  
-HETATM10783  O   HOH B 782      16.270  63.879  28.478  1.00 36.20           O  
-HETATM10784  O   HOH B 783      22.641  65.256  14.901  1.00 53.73           O  
-HETATM10785  O   HOH B 784      48.796  47.633  35.218  1.00 41.50           O  
-HETATM10786  O   HOH B 785       7.772  48.391  36.742  1.00 42.07           O  
-HETATM10787  O   HOH B 786      15.278  39.659  57.722  1.00 40.16           O  
-HETATM10788  O   HOH B 787      37.991  60.012  24.126  1.00 32.59           O  
-HETATM10789  O   HOH B 788      40.290  59.232  17.106  1.00 51.89           O  
-HETATM10790  O   HOH B 789      14.142  53.319  52.221  1.00 39.13           O  
-HETATM10791  O   HOH B 790      25.082  55.952  59.045  1.00 52.85           O  
-HETATM10792  O   HOH B 791      30.973  29.660  43.980  1.00 32.30           O  
-HETATM10793  O   HOH B 792      25.946  42.571  64.504  1.00 32.32           O  
-HETATM10794  O   HOH B 793      22.523  28.314  62.610  1.00 57.78           O  
-HETATM10795  O   HOH B 794       8.651  38.475  56.086  1.00 38.92           O  
-HETATM10796  O   HOH B 795      40.768  60.884  23.880  1.00 31.30           O  
-HETATM10797  O   HOH B 796      11.188  65.528  35.210  1.00 38.29           O  
-HETATM10798  O   HOH B 797      22.222  53.857  18.793  1.00 38.11           O  
-HETATM10799  O   HOH B 798      43.597  61.749  15.620  1.00 42.14           O  
-HETATM10800  O   HOH B 799      49.467  50.217  34.769  1.00 41.41           O  
-HETATM10801  O   HOH B 800      18.441  41.275  57.430  1.00 39.37           O  
-HETATM10802  O   HOH B 801      38.707  41.737  56.904  1.00 43.22           O  
-HETATM10803  O   HOH B 802      42.839  45.360  51.701  1.00 35.17           O  
-HETATM10804  O   HOH B 803      17.336  51.788  17.456  1.00 37.32           O  
-HETATM10805  O   HOH B 804      14.914  34.867  55.198  1.00 52.36           O  
-HETATM10806  O   HOH B 805      43.563  58.613  34.226  1.00 48.96           O  
-HETATM10807  O   HOH B 806      17.888  59.016  19.778  1.00 31.47           O  
-HETATM10808  O   HOH B 807      12.324  35.956  56.874  1.00 45.53           O  
-HETATM10809  O   HOH B 808       3.737  45.606  46.589  1.00 47.36           O  
-HETATM10810  O   HOH B 809      14.063  68.776  29.912  1.00 53.72           O  
-HETATM10811  O   HOH B 810      21.891  72.006  19.798  1.00 45.36           O  
-HETATM10812  O   HOH B 811      44.355  44.038  47.245  1.00 45.20           O  
-HETATM10813  O   HOH C 704      22.910  15.533  44.377  1.00 22.87           O  
-HETATM10814  O   HOH C 705      34.018   6.457  44.497  1.00 31.93           O  
-HETATM10815  O   HOH C 706      39.702   7.459  30.746  1.00 22.62           O  
-HETATM10816  O   HOH C 707      33.116  25.304  35.682  1.00 25.32           O  
-HETATM10817  O   HOH C 708      35.456  16.504  45.845  1.00 24.03           O  
-HETATM10818  O   HOH C 709      37.236  22.532  37.216  1.00 23.17           O  
-HETATM10819  O   HOH C 710      33.279  14.474  40.826  1.00 18.74           O  
-HETATM10820  O   HOH C 711      29.263  25.815  27.394  1.00 34.56           O  
-HETATM10821  O   HOH C 712      36.694   6.934  27.253  1.00 26.82           O  
-HETATM10822  O   HOH C 713      37.487  12.242  41.354  1.00 21.94           O  
-HETATM10823  O   HOH C 714      23.549  26.600  37.647  1.00 42.21           O  
-HETATM10824  O   HOH C 715      24.443  33.097  46.892  1.00 34.82           O  
-HETATM10825  O   HOH C 716      11.473  17.054  41.392  1.00 28.04           O  
-HETATM10826  O   HOH C 717      31.049  15.948  41.471  1.00 28.45           O  
-HETATM10827  O   HOH C 718      35.474  -3.119  40.686  1.00 28.04           O  
-HETATM10828  O   HOH C 719      25.181   7.542  43.545  1.00 29.99           O  
-HETATM10829  O   HOH C 720      18.811  21.389  39.612  1.00 24.68           O  
-HETATM10830  O   HOH C 721      36.993   7.577  29.890  1.00 24.31           O  
-HETATM10831  O   HOH C 722      29.995  -0.914  33.710  1.00 38.43           O  
-HETATM10832  O   HOH C 723      31.170  12.575  42.358  1.00 32.31           O  
-HETATM10833  O   HOH C 724      20.558  12.847  44.041  1.00 30.84           O  
-HETATM10834  O   HOH C 725      16.974  20.301  38.247  1.00 28.50           O  
-HETATM10835  O   HOH C 726      22.829  12.665  36.247  1.00 25.02           O  
-HETATM10836  O   HOH C 727      42.657  11.394  26.097  1.00 30.67           O  
-HETATM10837  O   HOH C 728      21.878  19.874  36.752  1.00 26.64           O  
-HETATM10838  O   HOH C 729      41.329   7.076  55.303  1.00 34.95           O  
-HETATM10839  O   HOH C 730      16.883  -5.333  38.475  1.00 34.12           O  
-HETATM10840  O   HOH C 731      16.541  14.166  37.561  1.00 31.10           O  
-HETATM10841  O   HOH C 732      17.706  21.016  42.215  1.00 30.31           O  
-HETATM10842  O   HOH C 733      28.115  28.238  58.333  1.00 39.41           O  
-HETATM10843  O   HOH C 734      39.071  11.059  43.310  1.00 33.94           O  
-HETATM10844  O   HOH C 735      31.822   0.650  23.076  1.00 42.10           O  
-HETATM10845  O   HOH C 736      42.765  -8.508  31.431  1.00 43.67           O  
-HETATM10846  O   HOH C 737      23.765  15.051  35.173  1.00 27.11           O  
-HETATM10847  O   HOH C 738      20.360  28.880  44.728  1.00 27.84           O  
-HETATM10848  O   HOH C 739      24.561   3.713  37.627  1.00 26.26           O  
-HETATM10849  O   HOH C 740      28.356  20.439  23.514  0.75 15.38           O  
-HETATM10850  O   HOH C 741      35.103   4.583  27.428  1.00 30.24           O  
-HETATM10851  O   HOH C 742      33.237  -5.307  19.449  1.00 36.18           O  
-HETATM10852  O   HOH C 743      33.433 -15.551  40.157  1.00 44.65           O  
-HETATM10853  O   HOH C 744      16.541   6.969  42.445  1.00 24.47           O  
-HETATM10854  O   HOH C 745      48.708   5.634  28.677  1.00 32.75           O  
-HETATM10855  O   HOH C 746      18.322   7.382  31.189  1.00 42.77           O  
-HETATM10856  O   HOH C 747      31.653   5.707  43.521  1.00 31.15           O  
-HETATM10857  O   HOH C 748      18.872  14.132  41.979  1.00 37.77           O  
-HETATM10858  O   HOH C 749      22.795   5.447  36.888  1.00 33.73           O  
-HETATM10859  O   HOH C 750      40.728  27.091  48.205  1.00 33.02           O  
-HETATM10860  O   HOH C 751      49.826   6.206  30.962  1.00 38.78           O  
-HETATM10861  O   HOH C 752      14.802  -7.120  32.033  1.00 35.21           O  
-HETATM10862  O   HOH C 753      31.931  -7.070  45.324  1.00 36.34           O  
-HETATM10863  O   HOH C 754      30.949 -17.223  22.017  1.00 60.97           O  
-HETATM10864  O   HOH C 755      33.825  31.080  55.726  1.00 46.58           O  
-HETATM10865  O   HOH C 756      42.958   2.394  26.471  1.00 30.03           O  
-HETATM10866  O   HOH C 757      26.630  -6.786  13.859  1.00 43.45           O  
-HETATM10867  O   HOH C 758      50.286   9.013  30.972  1.00 37.79           O  
-HETATM10868  O   HOH C 759      18.784  -3.198  27.565  1.00 28.73           O  
-HETATM10869  O   HOH C 760      24.044  29.426  39.759  1.00 38.37           O  
-HETATM10870  O   HOH C 761      14.008  20.040  52.392  1.00 31.89           O  
-HETATM10871  O   HOH C 762      28.498   3.504  24.811  1.00 36.69           O  
-HETATM10872  O   HOH C 763      49.005   5.415  48.684  1.00 47.82           O  
-HETATM10873  O   HOH C 764      22.646  12.940  22.265  1.00 48.49           O  
-HETATM10874  O   HOH C 765      46.284  10.690  45.077  1.00 33.24           O  
-HETATM10875  O   HOH C 766      21.800   4.880  33.025  1.00 38.56           O  
-HETATM10876  O   HOH C 767      47.872   8.269  40.898  1.00 40.99           O  
-HETATM10877  O   HOH C 768      18.515   3.797  34.149  1.00 32.14           O  
-HETATM10878  O   HOH C 769      19.183  -0.833  28.458  1.00 36.95           O  
-HETATM10879  O   HOH C 770      28.517  28.337  48.430  1.00 44.15           O  
-HETATM10880  O   HOH C 771      29.913  29.002  50.876  1.00 34.39           O  
-HETATM10881  O   HOH C 772      26.217   4.559  25.407  1.00 39.77           O  
-HETATM10882  O   HOH C 773      13.515  -6.189  19.807  1.00 47.73           O  
-HETATM10883  O   HOH C 774      16.153  -3.965  27.347  1.00 44.91           O  
-HETATM10884  O   HOH C 775      33.633  -7.934  18.520  1.00 44.79           O  
-HETATM10885  O   HOH C 776      32.589  -5.733  51.083  1.00 40.83           O  
-HETATM10886  O   HOH C 777      38.344   7.754  64.416  1.00 37.04           O  
-HETATM10887  O   HOH C 778      18.737 -18.283  41.684  1.00 53.00           O  
-HETATM10888  O   HOH C 779      34.565   2.057  22.231  1.00 34.04           O  
-HETATM10889  O   HOH C 780      38.053  18.243  58.452  1.00 40.83           O  
-HETATM10890  O   HOH C 781      21.183   4.478  24.182  1.00 49.36           O  
-HETATM10891  O   HOH C 782       9.927   5.265  36.548  1.00 43.77           O  
-HETATM10892  O   HOH C 783      43.728  -0.326  47.354  1.00 32.38           O  
-HETATM10893  O   HOH C 784      23.998   6.904  25.963  1.00 40.78           O  
-HETATM10894  O   HOH C 785      22.197   2.358  24.972  1.00 34.87           O  
-HETATM10895  O   HOH C 786      35.098   3.643  29.801  1.00 31.49           O  
-HETATM10896  O   HOH C 787      18.510  -3.000  24.654  1.00 33.52           O  
-HETATM10897  O   HOH C 788      25.198   8.804  24.055  1.00 48.91           O  
-HETATM10898  O   HOH C 789      31.544 -15.284  42.096  1.00 50.56           O  
-HETATM10899  O   HOH C 790      16.424  -3.638  20.960  1.00 55.52           O  
-HETATM10900  O   HOH C 791      39.313  -2.484  24.279  1.00 43.46           O  
-HETATM10901  O   HOH C 792      44.973   6.455  58.790  1.00 42.43           O  
-HETATM10902  O   HOH C 793      29.287   6.633  22.405  1.00 34.63           O  
-HETATM10903  O   HOH C 794      44.353  -2.752  22.880  1.00 51.04           O  
-HETATM10904  O   HOH C 795       9.025  -1.512  33.380  1.00 46.70           O  
-HETATM10905  O   HOH C 796      30.058   9.481  22.771  1.00 47.38           O  
-HETATM10906  O   HOH C 797       7.874  15.827  39.532  1.00 37.24           O  
-HETATM10907  O   HOH C 798      12.745   2.023  45.902  1.00 37.19           O  
-HETATM10908  O   HOH C 799      24.821  29.906  43.410  1.00 37.55           O  
-HETATM10909  O   HOH C 800      37.468  24.228  62.398  1.00 47.88           O  
-HETATM10910  O   HOH C 801      43.552   0.898  30.319  1.00 36.25           O  
-HETATM10911  O   HOH C 802      46.557  -0.619  46.512  1.00 36.73           O  
-HETATM10912  O   HOH C 803      48.990  11.509  37.445  1.00 43.00           O  
-HETATM10913  O   HOH C 804      47.822  22.141  56.780  1.00 43.57           O  
-HETATM10914  O   HOH C 805      37.026  -1.391  36.096  1.00 34.53           O  
-HETATM10915  O   HOH C 806      17.665 -11.066  33.148  1.00 48.04           O  
-HETATM10916  O   HOH C 807      10.238  -1.428  25.044  1.00 41.56           O  
-HETATM10917  O   HOH C 808       9.727  -8.317  20.635  1.00 46.05           O  
-HETATM10918  O   HOH C 809      43.719  -7.502  47.819  1.00 52.34           O  
-HETATM10919  O   HOH C 810      27.018 -19.014  18.030  1.00 40.95           O  
-HETATM10920  O   HOH C 811      29.904  11.013  20.631  1.00 50.32           O  
-HETATM10921  O   HOH C 812      35.240  -6.208  54.236  1.00 43.99           O  
-HETATM10922  O   HOH C 813      29.467 -19.031  38.516  1.00 44.92           O  
-HETATM10923  O   HOH C 814      20.071  16.866  64.197  1.00 52.18           O  
-HETATM10924  O   HOH C 815      23.985  -1.889  57.231  1.00 46.10           O  
-HETATM10925  O   HOH C 816      40.438  -5.909  33.202  1.00 52.43           O  
-HETATM10926  O   HOH C 817      25.721 -17.267  25.352  1.00 51.51           O  
-HETATM10927  O   HOH C 818      46.791  -7.129  45.357  1.00 38.89           O  
-HETATM10928  O   HOH C 819      42.710   5.907  20.054  1.00 51.16           O  
-HETATM10929  O   HOH C 820      31.099 -14.886  45.093  1.00 40.28           O  
-HETATM10930  O   HOH C 821       8.208   3.572  50.975  1.00 46.56           O  
-HETATM10931  O   HOH C 822      23.155   9.763  22.067  1.00 62.56           O  
-HETATM10932  O   HOH C 823      23.286   7.309  28.466  1.00 51.91           O  
-HETATM10933  O   HOH C 824      47.735  10.793  41.003  1.00 41.32           O  
-HETATM10934  O   HOH C 825      15.660   4.139  30.908  1.00 54.93           O  
-HETATM10935  O   HOH C 826      19.038  17.611  61.474  1.00 61.59           O  
-HETATM10936  O   HOH C 827      33.232  10.908  61.657  1.00 43.22           O  
-HETATM10937  O   HOH C 828      48.153  11.703  52.534  1.00 50.27           O  
-HETATM10938  O   HOH C 829      19.446 -13.074  43.064  1.00 50.07           O  
-HETATM10939  O   HOH C 830      36.483   2.862  34.753  1.00 45.97           O  
-HETATM10940  O   HOH C 831      -5.620  -1.986  28.949  1.00 40.79           O  
-HETATM10941  O   HOH C 832      27.542  26.675  36.519  1.00 14.91           O  
-HETATM10942  O   HOH C 833      38.495  23.324  57.307  1.00 14.91           O  
-HETATM10943  O   HOH D 705      33.318  50.104  29.278  1.00 15.34           O  
-HETATM10944  O   HOH D 706      43.880  27.361  31.090  1.00 21.84           O  
-HETATM10945  O   HOH D 707      41.749  28.992  30.068  1.00 27.27           O  
-HETATM10946  O   HOH D 708      40.756  36.664  26.875  1.00 22.11           O  
-HETATM10947  O   HOH D 709      48.781  36.682  28.262  1.00 29.94           O  
-HETATM10948  O   HOH D 710      35.618  37.320  33.895  1.00 19.40           O  
-HETATM10949  O   HOH D 711      60.748  20.102  26.054  1.00 25.82           O  
-HETATM10950  O   HOH D 712      42.608  39.737  27.051  1.00 22.17           O  
-HETATM10951  O   HOH D 713      36.572  47.885  28.468  1.00 32.85           O  
-HETATM10952  O   HOH D 714      32.488  31.671  37.395  1.00 33.89           O  
-HETATM10953  O   HOH D 715      50.309  25.910  42.744  1.00 22.43           O  
-HETATM10954  O   HOH D 716      36.740  21.759  34.552  1.00 21.07           O  
-HETATM10955  O   HOH D 717      47.173  45.310  28.644  1.00 36.28           O  
-HETATM10956  O   HOH D 718      45.277  29.588  29.316  1.00 22.20           O  
-HETATM10957  O   HOH D 719      41.001  41.161  29.075  1.00 39.59           O  
-HETATM10958  O   HOH D 720      40.798  36.447  35.844  1.00 26.41           O  
-HETATM10959  O   HOH D 721      42.876  38.174  35.032  1.00 28.97           O  
-HETATM10960  O   HOH D 722      34.251  41.647  32.356  1.00 26.08           O  
-HETATM10961  O   HOH D 723      33.665  39.636  30.610  1.00 24.65           O  
-HETATM10962  O   HOH D 724      61.819  17.426  27.315  1.00 24.78           O  
-HETATM10963  O   HOH D 725      64.407  33.203  28.015  1.00 26.35           O  
-HETATM10964  O   HOH D 726      42.671  24.258  26.232  1.00 30.08           O  
-HETATM10965  O   HOH D 727      50.388  14.443  28.646  1.00 45.31           O  
-HETATM10966  O   HOH D 728      59.366  27.774  37.204  1.00 34.60           O  
-HETATM10967  O   HOH D 729      53.589  20.105  17.874  1.00 35.76           O  
-HETATM10968  O   HOH D 730      51.376  49.616  25.093  1.00 33.42           O  
-HETATM10969  O   HOH D 731      52.232  38.329  33.962  1.00 32.51           O  
-HETATM10970  O   HOH D 732      61.166  29.177  32.830  1.00 30.76           O  
-HETATM10971  O   HOH D 733      48.754  22.210  29.377  1.00 26.63           O  
-HETATM10972  O   HOH D 734      36.716  51.599  30.779  1.00 36.14           O  
-HETATM10973  O   HOH D 735      47.050  23.741  31.111  1.00 21.45           O  
-HETATM10974  O   HOH D 736      52.041  28.112  28.434  1.00 25.64           O  
-HETATM10975  O   HOH D 737      51.456  14.345  32.171  1.00 45.55           O  
-HETATM10976  O   HOH D 738      58.864  48.063  33.214  1.00 37.76           O  
-HETATM10977  O   HOH D 739      28.262  29.014  29.291  1.00 27.58           O  
-HETATM10978  O   HOH D 740      50.296  44.768  37.555  1.00 37.58           O  
-HETATM10979  O   HOH D 741      29.986  26.165  20.026  1.00 40.81           O  
-HETATM10980  O   HOH D 742      24.463  30.819  23.059  1.00 36.02           O  
-HETATM10981  O   HOH D 743      72.714  35.272  32.055  1.00 36.83           O  
-HETATM10982  O   HOH D 744      27.508  31.467  26.865  1.00 31.94           O  
-HETATM10983  O   HOH D 745      51.279  23.441  42.255  1.00 24.38           O  
-HETATM10984  O   HOH D 746      33.895  15.904  23.992  1.00 30.17           O  
-HETATM10985  O   HOH D 747      28.750  23.857  20.136  1.00 37.47           O  
-HETATM10986  O   HOH D 748      63.766  50.291  37.345  1.00 42.21           O  
-HETATM10987  O   HOH D 749      49.354  13.284  35.469  1.00 37.15           O  
-HETATM10988  O   HOH D 750      48.491  12.416  22.676  1.00 36.88           O  
-HETATM10989  O   HOH D 751      59.278  13.117  29.163  1.00 40.04           O  
-HETATM10990  O   HOH D 752      63.223  14.795  27.890  1.00 36.57           O  
-HETATM10991  O   HOH D 753      31.917  29.231  39.410  1.00 51.64           O  
-HETATM10992  O   HOH D 754      27.580  32.654  20.169  1.00 46.27           O  
-HETATM10993  O   HOH D 755      64.618  30.004  18.954  1.00 46.28           O  
-HETATM10994  O   HOH D 756      29.470  34.004  32.588  1.00 29.99           O  
-HETATM10995  O   HOH D 757      48.693  12.571  20.109  1.00 39.85           O  
-HETATM10996  O   HOH D 758      26.149  27.584  12.118  1.00 51.06           O  
-HETATM10997  O   HOH D 759      50.557  35.010   6.992  1.00 39.01           O  
-HETATM10998  O   HOH D 760      57.439  39.113  20.897  1.00 42.40           O  
-HETATM10999  O   HOH D 761      59.271  37.022  20.473  1.00 45.15           O  
-HETATM11000  O   HOH D 762      30.136  30.205  33.907  1.00 38.32           O  
-HETATM11001  O   HOH D 763      38.170  16.287  27.257  1.00 33.19           O  
-HETATM11002  O   HOH D 764      51.785  12.649  23.096  1.00 56.04           O  
-HETATM11003  O   HOH D 765      63.652  32.233  21.617  1.00 49.20           O  
-HETATM11004  O   HOH D 766      66.383  53.057  30.574  1.00 44.43           O  
-HETATM11005  O   HOH D 767      48.555  43.555  38.835  1.00 48.41           O  
-HETATM11006  O   HOH D 768      54.662  46.240  42.820  1.00 43.26           O  
-HETATM11007  O   HOH D 769      50.231  39.959  34.721  1.00 46.83           O  
-HETATM11008  O   HOH D 770      29.869  27.765  35.635  1.00 41.45           O  
-HETATM11009  O   HOH D 771      51.126  33.056  41.455  1.00 43.65           O  
-HETATM11010  O   HOH D 772      51.727  12.444  42.373  1.00 43.77           O  
-HETATM11011  O   HOH D 773      39.282  17.770  14.323  1.00 47.11           O  
-HETATM11012  O   HOH D 774      34.760  16.442  16.423  1.00 47.53           O  
-HETATM11013  O   HOH D 775      52.457  14.382  26.830  1.00 45.49           O  
-HETATM11014  O   HOH D 776      32.971  34.650  35.130  1.00 46.58           O  
-HETATM11015  O   HOH D 777      34.587  43.683  18.021  1.00 37.08           O  
-HETATM11016  O   HOH D 778      59.108  14.030  26.616  1.00 35.75           O  
-HETATM11017  O   HOH D 779      44.399  44.146  32.196  1.00 47.01           O  
-HETATM11018  O   HOH D 780      39.962  43.647  33.566  1.00 47.59           O  
-HETATM11019  O   HOH D 781      34.113  40.823  28.095  1.00 36.16           O  
-HETATM11020  O   HOH D 782      28.756  22.106  15.826  1.00 51.49           O  
-HETATM11021  O   HOH D 783      42.931  20.688  13.965  1.00 43.38           O  
-HETATM11022  O   HOH D 784      43.333  27.091   8.601  1.00 34.87           O  
-HETATM11023  O   HOH D 785      56.913  13.383  25.091  1.00 50.38           O  
-HETATM11024  O   HOH D 786      66.796  25.413  27.524  1.00 50.19           O  
-HETATM11025  O   HOH D 787      69.396  28.657  29.675  1.00 51.63           O  
-HETATM11026  O   HOH D 788      29.290  21.598  21.669  1.00 48.38           O  
-HETATM11027  O   HOH D 789      54.266  13.546  44.975  1.00 43.28           O  
-HETATM11028  O   HOH D 790      62.000  12.994  34.081  1.00 54.18           O  
-HETATM11029  O   HOH D 791      58.905  53.999  50.517  1.00 45.03           O  
-HETATM11030  O   HOH D 792      65.198  25.643  40.041  1.00 47.09           O  
-HETATM11031  O   HOH D 793      63.841  24.291  35.626  1.00 58.11           O  
-HETATM11032  O   HOH D 794      71.266  55.411  40.053  1.00 46.44           O  
-HETATM11033  O   HOH D 795      50.954  34.617  34.865  1.00 35.31           O  
-HETATM11034  O   HOH D 796      47.634  39.894  42.604  1.00 44.25           O  
-HETATM11035  O   HOH D 797      41.168  38.449  48.803  1.00 35.77           O  
-HETATM11036  O   HOH D 798      29.208  27.992  22.169  1.00 38.54           O  
-HETATM11037  O   HOH D 799      41.016   9.052  16.309  1.00 45.24           O  
-HETATM11038  O   HOH D 800      52.137  30.836  28.916  1.00 32.55           O  
-CONECT1025810259102601026110280                                                 
-CONECT1025910258                                                                
-CONECT1026010258                                                                
-CONECT102611025810262                                                           
-CONECT102621026110263                                                           
-CONECT10263102621026410265                                                      
-CONECT102641026310269                                                           
-CONECT10265102631026610267                                                      
-CONECT1026610265                                                                
-CONECT10267102651026810269                                                      
-CONECT102681026710302                                                           
-CONECT10269102641026710270                                                      
-CONECT10270102691027110279                                                      
-CONECT102711027010272                                                           
-CONECT102721027110273                                                           
-CONECT10273102721027410279                                                      
-CONECT10274102731027510276                                                      
-CONECT1027510274                                                                
-CONECT102761027410277                                                           
-CONECT102771027610278                                                           
-CONECT102781027710279                                                           
-CONECT10279102701027310278                                                      
-CONECT102801025810281                                                           
-CONECT1028110280102821028310284                                                 
-CONECT1028210281                                                                
-CONECT1028310281                                                                
-CONECT102841028110285                                                           
-CONECT102851028410286                                                           
-CONECT10286102851028710288                                                      
-CONECT102871028610292                                                           
-CONECT10288102861028910290                                                      
-CONECT1028910288                                                                
-CONECT10290102881029110292                                                      
-CONECT1029110290                                                                
-CONECT10292102871029010293                                                      
-CONECT10293102921029410301                                                      
-CONECT102941029310295                                                           
-CONECT10295102941029610299                                                      
-CONECT10296102951029710298                                                      
-CONECT1029710296                                                                
-CONECT1029810296                                                                
-CONECT102991029510300                                                           
-CONECT103001029910301                                                           
-CONECT103011029310300                                                           
-CONECT1030210268103031030410305                                                 
-CONECT1030310302                                                                
-CONECT1030410302                                                                
-CONECT1030510302                                                                
-CONECT1030610307103081030910310                                                 
-CONECT103071030610311                                                           
-CONECT1030810306                                                                
-CONECT1030910306                                                                
-CONECT103101030610334                                                           
-CONECT1031110307103121031310314                                                 
-CONECT1031210311                                                                
-CONECT1031310311                                                                
-CONECT103141031110315                                                           
-CONECT103151031410316                                                           
-CONECT10316103151031710332                                                      
-CONECT103171031610318                                                           
-CONECT10318103171031910330                                                      
-CONECT10319103181032010329                                                      
-CONECT10320103191032110327                                                      
-CONECT103211032010322                                                           
-CONECT10322103211032310324                                                      
-CONECT1032310322                                                                
-CONECT103241032210325                                                           
-CONECT10325103241032610327                                                      
-CONECT1032610325                                                                
-CONECT10327103201032510328                                                      
-CONECT103281032710329                                                           
-CONECT103291031910328                                                           
-CONECT10330103181033110332                                                      
-CONECT1033110330                                                                
-CONECT10332103161033010333                                                      
-CONECT1033310332                                                                
-CONECT10334103101033510342                                                      
-CONECT10335103341033610337                                                      
-CONECT1033610335                                                                
-CONECT10337103351033810339                                                      
-CONECT1033810337                                                                
-CONECT10339103371034010341                                                      
-CONECT1034010339                                                                
-CONECT10341103391034210343                                                      
-CONECT103421033410341                                                           
-CONECT1034310341                                                                
-CONECT1034410345103461034710348                                                 
-CONECT103451034410349                                                           
-CONECT1034610344                                                                
-CONECT1034710344                                                                
-CONECT103481034410372                                                           
-CONECT1034910345103501035110352                                                 
-CONECT1035010349                                                                
-CONECT1035110349                                                                
-CONECT103521034910353                                                           
-CONECT103531035210354                                                           
-CONECT10354103531035510370                                                      
-CONECT103551035410356                                                           
-CONECT10356103551035710368                                                      
-CONECT10357103561035810367                                                      
-CONECT10358103571035910365                                                      
-CONECT103591035810360                                                           
-CONECT10360103591036110362                                                      
-CONECT1036110360                                                                
-CONECT103621036010363                                                           
-CONECT10363103621036410365                                                      
-CONECT1036410363                                                                
-CONECT10365103581036310366                                                      
-CONECT103661036510367                                                           
-CONECT103671035710366                                                           
-CONECT10368103561036910370                                                      
-CONECT1036910368                                                                
-CONECT10370103541036810371                                                      
-CONECT1037110370                                                                
-CONECT10372103481037310380                                                      
-CONECT10373103721037410375                                                      
-CONECT1037410373                                                                
-CONECT10375103731037610377                                                      
-CONECT1037610375                                                                
-CONECT10377103751037810379                                                      
-CONECT1037810377                                                                
-CONECT10379103771038010381                                                      
-CONECT103801037210379                                                           
-CONECT1038110379                                                                
-CONECT1038210383103841038510386                                                 
-CONECT103831038210387                                                           
-CONECT1038410382                                                                
-CONECT1038510382                                                                
-CONECT103861038210410                                                           
-CONECT1038710383103881038910390                                                 
-CONECT1038810387                                                                
-CONECT1038910387                                                                
-CONECT103901038710391                                                           
-CONECT103911039010392                                                           
-CONECT10392103911039310408                                                      
-CONECT103931039210394                                                           
-CONECT10394103931039510406                                                      
-CONECT10395103941039610405                                                      
-CONECT10396103951039710403                                                      
-CONECT103971039610398                                                           
-CONECT10398103971039910400                                                      
-CONECT1039910398                                                                
-CONECT104001039810401                                                           
-CONECT10401104001040210403                                                      
-CONECT1040210401                                                                
-CONECT10403103961040110404                                                      
-CONECT104041040310405                                                           
-CONECT104051039510404                                                           
-CONECT10406103941040710408                                                      
-CONECT1040710406                                                                
-CONECT10408103921040610409                                                      
-CONECT1040910408                                                                
-CONECT10410103861041110418                                                      
-CONECT10411104101041210413                                                      
-CONECT1041210411                                                                
-CONECT10413104111041410415                                                      
-CONECT1041410413                                                                
-CONECT10415104131041610417                                                      
-CONECT1041610415                                                                
-CONECT10417104151041810419                                                      
-CONECT104181041010417                                                           
-CONECT1041910417                                                                
-CONECT1042010421104221042310442                                                 
-CONECT1042110420                                                                
-CONECT1042210420                                                                
-CONECT104231042010424                                                           
-CONECT104241042310425                                                           
-CONECT10425104241042610427                                                      
-CONECT104261042510431                                                           
-CONECT10427104251042810429                                                      
-CONECT1042810427                                                                
-CONECT10429104271043010431                                                      
-CONECT104301042910464                                                           
-CONECT10431104261042910432                                                      
-CONECT10432104311043310441                                                      
-CONECT104331043210434                                                           
-CONECT104341043310435                                                           
-CONECT10435104341043610441                                                      
-CONECT10436104351043710438                                                      
-CONECT1043710436                                                                
-CONECT104381043610439                                                           
-CONECT104391043810440                                                           
-CONECT104401043910441                                                           
-CONECT10441104321043510440                                                      
-CONECT104421042010443                                                           
-CONECT1044310442104441044510446                                                 
-CONECT1044410443                                                                
-CONECT1044510443                                                                
-CONECT104461044310447                                                           
-CONECT104471044610448                                                           
-CONECT10448104471044910450                                                      
-CONECT104491044810454                                                           
-CONECT10450104481045110452                                                      
-CONECT1045110450                                                                
-CONECT10452104501045310454                                                      
-CONECT1045310452                                                                
-CONECT10454104491045210455                                                      
-CONECT10455104541045610463                                                      
-CONECT104561045510457                                                           
-CONECT10457104561045810461                                                      
-CONECT10458104571045910460                                                      
-CONECT1045910458                                                                
-CONECT1046010458                                                                
-CONECT104611045710462                                                           
-CONECT104621046110463                                                           
-CONECT104631045510462                                                           
-CONECT1046410430104651046610467                                                 
-CONECT1046510464                                                                
-CONECT1046610464                                                                
-CONECT1046710464                                                                
-CONECT1046810469104701047110490                                                 
-CONECT1046910468                                                                
-CONECT1047010468                                                                
-CONECT104711046810472                                                           
-CONECT104721047110473                                                           
-CONECT10473104721047410475                                                      
-CONECT104741047310479                                                           
-CONECT10475104731047610477                                                      
-CONECT1047610475                                                                
-CONECT10477104751047810479                                                      
-CONECT104781047710512                                                           
-CONECT10479104741047710480                                                      
-CONECT10480104791048110489                                                      
-CONECT104811048010482                                                           
-CONECT104821048110483                                                           
-CONECT10483104821048410489                                                      
-CONECT10484104831048510486                                                      
-CONECT1048510484                                                                
-CONECT104861048410487                                                           
-CONECT104871048610488                                                           
-CONECT104881048710489                                                           
-CONECT10489104801048310488                                                      
-CONECT104901046810491                                                           
-CONECT1049110490104921049310494                                                 
-CONECT1049210491                                                                
-CONECT1049310491                                                                
-CONECT104941049110495                                                           
-CONECT104951049410496                                                           
-CONECT10496104951049710498                                                      
-CONECT104971049610502                                                           
-CONECT10498104961049910500                                                      
-CONECT1049910498                                                                
-CONECT10500104981050110502                                                      
-CONECT1050110500                                                                
-CONECT10502104971050010503                                                      
-CONECT10503105021050410511                                                      
-CONECT105041050310505                                                           
-CONECT10505105041050610509                                                      
-CONECT10506105051050710508                                                      
-CONECT1050710506                                                                
-CONECT1050810506                                                                
-CONECT105091050510510                                                           
-CONECT105101050910511                                                           
-CONECT105111050310510                                                           
-CONECT1051210478105131051410515                                                 
-CONECT1051310512                                                                
-CONECT1051410512                                                                
-CONECT1051510512                                                                
-CONECT1051610517105181051910538                                                 
-CONECT1051710516                                                                
-CONECT1051810516                                                                
-CONECT105191051610520                                                           
-CONECT105201051910521                                                           
-CONECT10521105201052210523                                                      
-CONECT105221052110527                                                           
-CONECT10523105211052410525                                                      
-CONECT1052410523                                                                
-CONECT10525105231052610527                                                      
-CONECT105261052510560                                                           
-CONECT10527105221052510528                                                      
-CONECT10528105271052910537                                                      
-CONECT105291052810530                                                           
-CONECT105301052910531                                                           
-CONECT10531105301053210537                                                      
-CONECT10532105311053310534                                                      
-CONECT1053310532                                                                
-CONECT105341053210535                                                           
-CONECT105351053410536                                                           
-CONECT105361053510537                                                           
-CONECT10537105281053110536                                                      
-CONECT105381051610539                                                           
-CONECT1053910538105401054110542                                                 
-CONECT1054010539                                                                
-CONECT1054110539                                                                
-CONECT105421053910543                                                           
-CONECT105431054210544                                                           
-CONECT10544105431054510546                                                      
-CONECT105451054410550                                                           
-CONECT10546105441054710548                                                      
-CONECT1054710546                                                                
-CONECT10548105461054910550                                                      
-CONECT1054910548                                                                
-CONECT10550105451054810551                                                      
-CONECT10551105501055210559                                                      
-CONECT105521055110553                                                           
-CONECT10553105521055410557                                                      
-CONECT10554105531055510556                                                      
-CONECT1055510554                                                                
-CONECT1055610554                                                                
-CONECT105571055310558                                                           
-CONECT105581055710559                                                           
-CONECT105591055110558                                                           
-CONECT1056010526105611056210563                                                 
-CONECT1056110560                                                                
-CONECT1056210560                                                                
-CONECT1056310560                                                                
-MASTER      587    0    7   58   48    0   64    611034    4  306  120          
-END                                                                             
diff --git a/plip/test/pdb/1osn.pdb b/plip/test/pdb/1osn.pdb
deleted file mode 100644
index 5a22ab2..0000000
--- a/plip/test/pdb/1osn.pdb
+++ /dev/null
@@ -1,11018 +0,0 @@
-HEADER    TRANSFERASE                             20-MAR-03   1OSN              
-TITLE     CRYSTAL STRUCTURE OF VARICELLA ZOSTER VIRUS THYMIDINE                 
-TITLE    2 KINASE IN COMPLEX WITH BVDU-MP AND ADP                               
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
-COMPND   3 CHAIN: A, B, C, D;                                                   
-COMPND   4 SYNONYM: VZV-TK;                                                     
-COMPND   5 EC: 2.7.1.21;                                                        
-COMPND   6 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 3;                            
-SOURCE   3 ORGANISM_COMMON: VARICELLA-ZOSTER VIRUS;                             
-SOURCE   4 ORGANISM_TAXID: 10335;                                               
-SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
-SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
-SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX6P1VZV-TK                             
-KEYWDS    HUMAN HERPES VIRUS 3, CHICKENPOX, THYMIDINE KINASE, BVDU-MP,          
-KEYWDS   2 TRANSFERASE                                                          
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    L.E.BIRD,J.REN,A.WRIGHT,K.D.LESLIE,B.DEGREVE,J.BALZARINI,             
-AUTHOR   2 D.K.STAMMERS                                                         
-REVDAT   3   24-FEB-09 1OSN    1       VERSN                                    
-REVDAT   2   29-JUL-03 1OSN    1       JRNL                                     
-REVDAT   1   10-JUN-03 1OSN    0                                                
-JRNL        AUTH   L.E.BIRD,J.REN,A.WRIGHT,K.D.LESLIE,B.DEGREVE,                
-JRNL        AUTH 2 J.BALZARINI,D.K.STAMMERS                                     
-JRNL        TITL   CRYSTAL STRUCTURE OF VARICELLA ZOSTER VIRUS                  
-JRNL        TITL 2 THYMIDINE KINASE                                             
-JRNL        REF    J.BIOL.CHEM.                  V. 278 24680 2003              
-JRNL        REFN                   ISSN 0021-9258                               
-JRNL        PMID   12686543                                                     
-JRNL        DOI    10.1074/JBC.M302025200                                       
-REMARK   1                                                                      
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS 1.1                                              
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : NULL                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.78                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1354083.960                    
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
-REMARK   3   NUMBER OF REFLECTIONS             : 30027                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.235                           
-REMARK   3   FREE R VALUE                     : 0.268                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1490                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.60                        
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2760                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.3590                       
-REMARK   3   BIN FREE R VALUE                    : 0.3550                       
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 143                          
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 9855                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 181                                     
-REMARK   3   SOLVENT ATOMS            : 2                                       
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 77.20                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.20                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 30.72000                                             
-REMARK   3    B22 (A**2) : -15.18000                                            
-REMARK   3    B33 (A**2) : -15.54000                                            
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : -8.94000                                             
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.67                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.63                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.008                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.00                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.93                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : FLAT MODEL                                           
-REMARK   3   KSOL        : 0.27                                                 
-REMARK   3   BSOL        : 22.19                                                
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : CONSTR                                                  
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
-REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
-REMARK   3  PARAMETER FILE  3  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
-REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
-REMARK   3  TOPOLOGY FILE  3   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1OSN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-03.                  
-REMARK 100 THE RCSB ID CODE IS RCSB018628.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-01                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 5.0                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ESRF                               
-REMARK 200  BEAMLINE                       : ID14-2                             
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 167134                             
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.500                             
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
-REMARK 200  DATA REDUNDANCY                : 5.600                              
-REMARK 200  R MERGE                    (I) : 0.17100                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.5000                             
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.42800                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: CNS                                                   
-REMARK 200 STARTING MODEL: HSV-1 TK (1E2K)                                      
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 61.42                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, SODIUM ACETATE, ATP,          
-REMARK 280  BVDU, MGCL2, PH 5.0, VAPOR DIFFUSION, SITTING DROP,                 
-REMARK 280  TEMPERATURE 294K                                                    
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,Y+1/2,-Z                                             
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       27.10000            
-REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 300 REMARK: THERE ARE TWO BIOLOGICAL DIMERS IN THE                       
-REMARK 300 ASYMMETRIC UNIT                                                      
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 5870 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 26090 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 6170 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 25080 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 3                                                       
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 14530 ANGSTROM**2                         
-REMARK 350 SURFACE AREA OF THE COMPLEX: 48680 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL                       
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     SER A     2                                                      
-REMARK 465     THR A     3                                                      
-REMARK 465     ASP A     4                                                      
-REMARK 465     LYS A     5                                                      
-REMARK 465     THR A     6                                                      
-REMARK 465     ASP A     7                                                      
-REMARK 465     LYS A   186                                                      
-REMARK 465     ARG A   187                                                      
-REMARK 465     ALA A   188                                                      
-REMARK 465     ARG A   189                                                      
-REMARK 465     PRO A   190                                                      
-REMARK 465     GLY A   191                                                      
-REMARK 465     ASN A   339                                                      
-REMARK 465     THR A   340                                                      
-REMARK 465     SER A   341                                                      
-REMARK 465     MET B     1                                                      
-REMARK 465     SER B     2                                                      
-REMARK 465     THR B     3                                                      
-REMARK 465     ASP B     4                                                      
-REMARK 465     LYS B     5                                                      
-REMARK 465     THR B     6                                                      
-REMARK 465     ASP B     7                                                      
-REMARK 465     VAL B     8                                                      
-REMARK 465     LYS B     9                                                      
-REMARK 465     SER B   113                                                      
-REMARK 465     ASP B   114                                                      
-REMARK 465     LEU B   115                                                      
-REMARK 465     VAL B   116                                                      
-REMARK 465     GLN B   117                                                      
-REMARK 465     VAL B   118                                                      
-REMARK 465     ASN B   119                                                      
-REMARK 465     LYS B   120                                                      
-REMARK 465     LYS B   186                                                      
-REMARK 465     ARG B   187                                                      
-REMARK 465     ALA B   188                                                      
-REMARK 465     ARG B   189                                                      
-REMARK 465     PRO B   190                                                      
-REMARK 465     GLY B   191                                                      
-REMARK 465     ASN B   339                                                      
-REMARK 465     THR B   340                                                      
-REMARK 465     SER B   341                                                      
-REMARK 465     MET C     1                                                      
-REMARK 465     SER C     2                                                      
-REMARK 465     THR C     3                                                      
-REMARK 465     ASP C     4                                                      
-REMARK 465     LYS C     5                                                      
-REMARK 465     THR C     6                                                      
-REMARK 465     ASP C     7                                                      
-REMARK 465     VAL C     8                                                      
-REMARK 465     SER C   111                                                      
-REMARK 465     THR C   112                                                      
-REMARK 465     SER C   113                                                      
-REMARK 465     ASP C   114                                                      
-REMARK 465     LEU C   115                                                      
-REMARK 465     VAL C   116                                                      
-REMARK 465     GLN C   117                                                      
-REMARK 465     VAL C   118                                                      
-REMARK 465     ASN C   119                                                      
-REMARK 465     LYS C   120                                                      
-REMARK 465     GLU C   121                                                      
-REMARK 465     LYS C   186                                                      
-REMARK 465     ARG C   187                                                      
-REMARK 465     ALA C   188                                                      
-REMARK 465     ARG C   189                                                      
-REMARK 465     PRO C   190                                                      
-REMARK 465     GLY C   191                                                      
-REMARK 465     ASN C   339                                                      
-REMARK 465     THR C   340                                                      
-REMARK 465     SER C   341                                                      
-REMARK 465     MET D     1                                                      
-REMARK 465     SER D     2                                                      
-REMARK 465     THR D     3                                                      
-REMARK 465     ASP D     4                                                      
-REMARK 465     LYS D     5                                                      
-REMARK 465     THR D     6                                                      
-REMARK 465     ASP D     7                                                      
-REMARK 465     SER D   113                                                      
-REMARK 465     ASP D   114                                                      
-REMARK 465     LEU D   115                                                      
-REMARK 465     VAL D   116                                                      
-REMARK 465     GLN D   117                                                      
-REMARK 465     VAL D   118                                                      
-REMARK 465     ASN D   119                                                      
-REMARK 465     LYS D   120                                                      
-REMARK 465     SER D   185                                                      
-REMARK 465     LYS D   186                                                      
-REMARK 465     ARG D   187                                                      
-REMARK 465     ALA D   188                                                      
-REMARK 465     ARG D   189                                                      
-REMARK 465     PRO D   190                                                      
-REMARK 465     GLY D   191                                                      
-REMARK 465     GLU D   192                                                      
-REMARK 465     ASN D   339                                                      
-REMARK 465     THR D   340                                                      
-REMARK 465     SER D   341                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     SER A 185    OG                                                  
-REMARK 470     GLU A 192    CG   CD   OE1  OE2                                  
-REMARK 470     THR A 193    OG1  CG2                                            
-REMARK 470     VAL A 194    CG1  CG2                                            
-REMARK 470     SER B 185    OG                                                  
-REMARK 470     GLU B 192    CG   CD   OE1  OE2                                  
-REMARK 470     THR B 193    OG1  CG2                                            
-REMARK 470     VAL B 194    CG1  CG2                                            
-REMARK 470     SER C 185    OG                                                  
-REMARK 470     GLU C 192    CG   CD   OE1  OE2                                  
-REMARK 470     THR C 193    OG1  CG2                                            
-REMARK 470     VAL C 194    CG1  CG2                                            
-REMARK 470     THR D 193    OG1  CG2                                            
-REMARK 470     VAL D 194    CG1  CG2                                            
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    LYS A   9      158.80    -40.42                                   
-REMARK 500    ASP A  18     -163.37   -120.75                                   
-REMARK 500    HIS A  35       36.43    -99.26                                   
-REMARK 500    PHE A  36      -20.38   -164.93                                   
-REMARK 500    ALA A  37       32.07    -83.99                                   
-REMARK 500    ASN A  55       51.75   -167.40                                   
-REMARK 500    MET A 100      -70.86    -60.39                                   
-REMARK 500    THR A 110       58.55   -104.73                                   
-REMARK 500    ARG A 130      147.39     73.99                                   
-REMARK 500    PRO A 132      -35.42    -37.92                                   
-REMARK 500    ILE A 137      -46.24   -147.01                                   
-REMARK 500    VAL A 184      -77.94    -87.84                                   
-REMARK 500    PRO A 197      -57.52    -25.23                                   
-REMARK 500    HIS A 222       31.81    -79.27                                   
-REMARK 500    ALA A 223     -117.25    -67.86                                   
-REMARK 500    LYS A 241      -56.61   -120.55                                   
-REMARK 500    CYS A 244      -86.50    -59.57                                   
-REMARK 500    ILE A 245       97.80     -5.65                                   
-REMARK 500    PRO A 275      -71.42    -32.42                                   
-REMARK 500    GLN A 300     -176.36    170.35                                   
-REMARK 500    ASP B  18     -162.68   -121.97                                   
-REMARK 500    ALA B  37       33.27    -94.97                                   
-REMARK 500    ASN B  55       54.66   -165.96                                   
-REMARK 500    MET B 100      -73.01    -59.64                                   
-REMARK 500    THR B 110       54.51   -106.84                                   
-REMARK 500    ARG B 130      144.42     74.69                                   
-REMARK 500    PRO B 132      -35.51    -38.20                                   
-REMARK 500    ILE B 137      -46.77   -144.71                                   
-REMARK 500    VAL B 184      -75.49    -89.11                                   
-REMARK 500    PRO B 197      -59.10    -26.46                                   
-REMARK 500    HIS B 222       33.47    -78.93                                   
-REMARK 500    ALA B 223     -115.27    -70.58                                   
-REMARK 500    CYS B 244      -86.96    -59.85                                   
-REMARK 500    ILE B 245       99.72     -5.54                                   
-REMARK 500    PRO B 275      -73.49    -31.74                                   
-REMARK 500    GLN B 300     -176.93    172.30                                   
-REMARK 500    ASP C  18     -161.09   -122.01                                   
-REMARK 500    ASN C  55       54.09   -167.01                                   
-REMARK 500    MET C 100      -73.58    -58.51                                   
-REMARK 500    ARG C 130      144.52     73.12                                   
-REMARK 500    PRO C 132      -36.25    -35.60                                   
-REMARK 500    ILE C 137      -46.94   -145.33                                   
-REMARK 500    VAL C 184      -76.26    -89.24                                   
-REMARK 500    PRO C 197      -57.77    -27.34                                   
-REMARK 500    HIS C 222       32.99    -77.66                                   
-REMARK 500    ALA C 223     -115.11    -69.91                                   
-REMARK 500    CYS C 244      -86.72    -60.62                                   
-REMARK 500    ILE C 245       99.44     -5.25                                   
-REMARK 500    PRO C 275      -71.52    -33.70                                   
-REMARK 500    GLN C 300     -176.20    170.50                                   
-REMARK 500    GLN C 337       40.64   -104.30                                   
-REMARK 500    MET D  10      162.32    -43.63                                   
-REMARK 500    ASP D  18     -162.63   -121.99                                   
-REMARK 500    ASN D  55       51.14   -166.71                                   
-REMARK 500    MET D 100      -72.80    -60.67                                   
-REMARK 500    THR D 110       55.48   -105.39                                   
-REMARK 500    ARG D 130      144.58     71.64                                   
-REMARK 500    PRO D 132      -35.89    -37.72                                   
-REMARK 500    ILE D 137      -46.43   -144.87                                   
-REMARK 500    PRO D 197      -59.30    -25.35                                   
-REMARK 500    HIS D 222       31.14    -77.86                                   
-REMARK 500    ALA D 223     -116.65    -67.33                                   
-REMARK 500    LYS D 241      -53.09   -120.96                                   
-REMARK 500    CYS D 244      -86.63    -59.69                                   
-REMARK 500    ILE D 245       98.49     -5.83                                   
-REMARK 500    PRO D 275      -71.66    -32.22                                   
-REMARK 500    GLN D 300     -176.74    170.10                                   
-REMARK 500    GLN D 337       45.55   -100.35                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 610                                                                      
-REMARK 610 MISSING HETEROATOM                                                   
-REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 610 I=INSERTION CODE):                                                   
-REMARK 610   M RES C SSEQI                                                      
-REMARK 610     ADP A  400                                                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 400                 
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BVP A 500                 
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 1400                
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BVP B 1500                
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 2400                
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BVP C 2500                
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 3400                
-REMARK 800 SITE_IDENTIFIER: AC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BVP D 3500                
-DBREF  1OSN A    1   341  UNP    P0C0E6   KITH_VZVO        1    341             
-DBREF  1OSN B    1   341  UNP    P0C0E6   KITH_VZVO        1    341             
-DBREF  1OSN C    1   341  UNP    P0C0E6   KITH_VZVO        1    341             
-DBREF  1OSN D    1   341  UNP    P0C0E6   KITH_VZVO        1    341             
-SEQRES   1 A  341  MET SER THR ASP LYS THR ASP VAL LYS MET GLY VAL LEU          
-SEQRES   2 A  341  ARG ILE TYR LEU ASP GLY ALA TYR GLY ILE GLY LYS THR          
-SEQRES   3 A  341  THR ALA ALA GLU GLU PHE LEU HIS HIS PHE ALA ILE THR          
-SEQRES   4 A  341  PRO ASN ARG ILE LEU LEU ILE GLY GLU PRO LEU SER TYR          
-SEQRES   5 A  341  TRP ARG ASN LEU ALA GLY GLU ASP ALA ILE CYS GLY ILE          
-SEQRES   6 A  341  TYR GLY THR GLN THR ARG ARG LEU ASN GLY ASP VAL SER          
-SEQRES   7 A  341  PRO GLU ASP ALA GLN ARG LEU THR ALA HIS PHE GLN SER          
-SEQRES   8 A  341  LEU PHE CYS SER PRO HIS ALA ILE MET HIS ALA LYS ILE          
-SEQRES   9 A  341  SER ALA LEU MET ASP THR SER THR SER ASP LEU VAL GLN          
-SEQRES  10 A  341  VAL ASN LYS GLU PRO TYR LYS ILE MET LEU SER ASP ARG          
-SEQRES  11 A  341  HIS PRO ILE ALA SER THR ILE CYS PHE PRO LEU SER ARG          
-SEQRES  12 A  341  TYR LEU VAL GLY ASP MET SER PRO ALA ALA LEU PRO GLY          
-SEQRES  13 A  341  LEU LEU PHE THR LEU PRO ALA GLU PRO PRO GLY THR ASN          
-SEQRES  14 A  341  LEU VAL VAL CYS THR VAL SER LEU PRO SER HIS LEU SER          
-SEQRES  15 A  341  ARG VAL SER LYS ARG ALA ARG PRO GLY GLU THR VAL ASN          
-SEQRES  16 A  341  LEU PRO PHE VAL MET VAL LEU ARG ASN VAL TYR ILE MET          
-SEQRES  17 A  341  LEU ILE ASN THR ILE ILE PHE LEU LYS THR ASN ASN TRP          
-SEQRES  18 A  341  HIS ALA GLY TRP ASN THR LEU SER PHE CYS ASN ASP VAL          
-SEQRES  19 A  341  PHE LYS GLN LYS LEU GLN LYS SER GLU CYS ILE LYS LEU          
-SEQRES  20 A  341  ARG GLU VAL PRO GLY ILE GLU ASP THR LEU PHE ALA VAL          
-SEQRES  21 A  341  LEU LYS LEU PRO GLU LEU CYS GLY GLU PHE GLY ASN ILE          
-SEQRES  22 A  341  LEU PRO LEU TRP ALA TRP GLY MET GLU THR LEU SER ASN          
-SEQRES  23 A  341  CYS LEU ARG SER MET SER PRO PHE VAL LEU SER LEU GLU          
-SEQRES  24 A  341  GLN THR PRO GLN HIS ALA ALA GLN GLU LEU LYS THR LEU          
-SEQRES  25 A  341  LEU PRO GLN MET THR PRO ALA ASN MET SER SER GLY ALA          
-SEQRES  26 A  341  TRP ASN ILE LEU LYS GLU LEU VAL ASN ALA VAL GLN ASP          
-SEQRES  27 A  341  ASN THR SER                                                  
-SEQRES   1 B  341  MET SER THR ASP LYS THR ASP VAL LYS MET GLY VAL LEU          
-SEQRES   2 B  341  ARG ILE TYR LEU ASP GLY ALA TYR GLY ILE GLY LYS THR          
-SEQRES   3 B  341  THR ALA ALA GLU GLU PHE LEU HIS HIS PHE ALA ILE THR          
-SEQRES   4 B  341  PRO ASN ARG ILE LEU LEU ILE GLY GLU PRO LEU SER TYR          
-SEQRES   5 B  341  TRP ARG ASN LEU ALA GLY GLU ASP ALA ILE CYS GLY ILE          
-SEQRES   6 B  341  TYR GLY THR GLN THR ARG ARG LEU ASN GLY ASP VAL SER          
-SEQRES   7 B  341  PRO GLU ASP ALA GLN ARG LEU THR ALA HIS PHE GLN SER          
-SEQRES   8 B  341  LEU PHE CYS SER PRO HIS ALA ILE MET HIS ALA LYS ILE          
-SEQRES   9 B  341  SER ALA LEU MET ASP THR SER THR SER ASP LEU VAL GLN          
-SEQRES  10 B  341  VAL ASN LYS GLU PRO TYR LYS ILE MET LEU SER ASP ARG          
-SEQRES  11 B  341  HIS PRO ILE ALA SER THR ILE CYS PHE PRO LEU SER ARG          
-SEQRES  12 B  341  TYR LEU VAL GLY ASP MET SER PRO ALA ALA LEU PRO GLY          
-SEQRES  13 B  341  LEU LEU PHE THR LEU PRO ALA GLU PRO PRO GLY THR ASN          
-SEQRES  14 B  341  LEU VAL VAL CYS THR VAL SER LEU PRO SER HIS LEU SER          
-SEQRES  15 B  341  ARG VAL SER LYS ARG ALA ARG PRO GLY GLU THR VAL ASN          
-SEQRES  16 B  341  LEU PRO PHE VAL MET VAL LEU ARG ASN VAL TYR ILE MET          
-SEQRES  17 B  341  LEU ILE ASN THR ILE ILE PHE LEU LYS THR ASN ASN TRP          
-SEQRES  18 B  341  HIS ALA GLY TRP ASN THR LEU SER PHE CYS ASN ASP VAL          
-SEQRES  19 B  341  PHE LYS GLN LYS LEU GLN LYS SER GLU CYS ILE LYS LEU          
-SEQRES  20 B  341  ARG GLU VAL PRO GLY ILE GLU ASP THR LEU PHE ALA VAL          
-SEQRES  21 B  341  LEU LYS LEU PRO GLU LEU CYS GLY GLU PHE GLY ASN ILE          
-SEQRES  22 B  341  LEU PRO LEU TRP ALA TRP GLY MET GLU THR LEU SER ASN          
-SEQRES  23 B  341  CYS LEU ARG SER MET SER PRO PHE VAL LEU SER LEU GLU          
-SEQRES  24 B  341  GLN THR PRO GLN HIS ALA ALA GLN GLU LEU LYS THR LEU          
-SEQRES  25 B  341  LEU PRO GLN MET THR PRO ALA ASN MET SER SER GLY ALA          
-SEQRES  26 B  341  TRP ASN ILE LEU LYS GLU LEU VAL ASN ALA VAL GLN ASP          
-SEQRES  27 B  341  ASN THR SER                                                  
-SEQRES   1 C  341  MET SER THR ASP LYS THR ASP VAL LYS MET GLY VAL LEU          
-SEQRES   2 C  341  ARG ILE TYR LEU ASP GLY ALA TYR GLY ILE GLY LYS THR          
-SEQRES   3 C  341  THR ALA ALA GLU GLU PHE LEU HIS HIS PHE ALA ILE THR          
-SEQRES   4 C  341  PRO ASN ARG ILE LEU LEU ILE GLY GLU PRO LEU SER TYR          
-SEQRES   5 C  341  TRP ARG ASN LEU ALA GLY GLU ASP ALA ILE CYS GLY ILE          
-SEQRES   6 C  341  TYR GLY THR GLN THR ARG ARG LEU ASN GLY ASP VAL SER          
-SEQRES   7 C  341  PRO GLU ASP ALA GLN ARG LEU THR ALA HIS PHE GLN SER          
-SEQRES   8 C  341  LEU PHE CYS SER PRO HIS ALA ILE MET HIS ALA LYS ILE          
-SEQRES   9 C  341  SER ALA LEU MET ASP THR SER THR SER ASP LEU VAL GLN          
-SEQRES  10 C  341  VAL ASN LYS GLU PRO TYR LYS ILE MET LEU SER ASP ARG          
-SEQRES  11 C  341  HIS PRO ILE ALA SER THR ILE CYS PHE PRO LEU SER ARG          
-SEQRES  12 C  341  TYR LEU VAL GLY ASP MET SER PRO ALA ALA LEU PRO GLY          
-SEQRES  13 C  341  LEU LEU PHE THR LEU PRO ALA GLU PRO PRO GLY THR ASN          
-SEQRES  14 C  341  LEU VAL VAL CYS THR VAL SER LEU PRO SER HIS LEU SER          
-SEQRES  15 C  341  ARG VAL SER LYS ARG ALA ARG PRO GLY GLU THR VAL ASN          
-SEQRES  16 C  341  LEU PRO PHE VAL MET VAL LEU ARG ASN VAL TYR ILE MET          
-SEQRES  17 C  341  LEU ILE ASN THR ILE ILE PHE LEU LYS THR ASN ASN TRP          
-SEQRES  18 C  341  HIS ALA GLY TRP ASN THR LEU SER PHE CYS ASN ASP VAL          
-SEQRES  19 C  341  PHE LYS GLN LYS LEU GLN LYS SER GLU CYS ILE LYS LEU          
-SEQRES  20 C  341  ARG GLU VAL PRO GLY ILE GLU ASP THR LEU PHE ALA VAL          
-SEQRES  21 C  341  LEU LYS LEU PRO GLU LEU CYS GLY GLU PHE GLY ASN ILE          
-SEQRES  22 C  341  LEU PRO LEU TRP ALA TRP GLY MET GLU THR LEU SER ASN          
-SEQRES  23 C  341  CYS LEU ARG SER MET SER PRO PHE VAL LEU SER LEU GLU          
-SEQRES  24 C  341  GLN THR PRO GLN HIS ALA ALA GLN GLU LEU LYS THR LEU          
-SEQRES  25 C  341  LEU PRO GLN MET THR PRO ALA ASN MET SER SER GLY ALA          
-SEQRES  26 C  341  TRP ASN ILE LEU LYS GLU LEU VAL ASN ALA VAL GLN ASP          
-SEQRES  27 C  341  ASN THR SER                                                  
-SEQRES   1 D  341  MET SER THR ASP LYS THR ASP VAL LYS MET GLY VAL LEU          
-SEQRES   2 D  341  ARG ILE TYR LEU ASP GLY ALA TYR GLY ILE GLY LYS THR          
-SEQRES   3 D  341  THR ALA ALA GLU GLU PHE LEU HIS HIS PHE ALA ILE THR          
-SEQRES   4 D  341  PRO ASN ARG ILE LEU LEU ILE GLY GLU PRO LEU SER TYR          
-SEQRES   5 D  341  TRP ARG ASN LEU ALA GLY GLU ASP ALA ILE CYS GLY ILE          
-SEQRES   6 D  341  TYR GLY THR GLN THR ARG ARG LEU ASN GLY ASP VAL SER          
-SEQRES   7 D  341  PRO GLU ASP ALA GLN ARG LEU THR ALA HIS PHE GLN SER          
-SEQRES   8 D  341  LEU PHE CYS SER PRO HIS ALA ILE MET HIS ALA LYS ILE          
-SEQRES   9 D  341  SER ALA LEU MET ASP THR SER THR SER ASP LEU VAL GLN          
-SEQRES  10 D  341  VAL ASN LYS GLU PRO TYR LYS ILE MET LEU SER ASP ARG          
-SEQRES  11 D  341  HIS PRO ILE ALA SER THR ILE CYS PHE PRO LEU SER ARG          
-SEQRES  12 D  341  TYR LEU VAL GLY ASP MET SER PRO ALA ALA LEU PRO GLY          
-SEQRES  13 D  341  LEU LEU PHE THR LEU PRO ALA GLU PRO PRO GLY THR ASN          
-SEQRES  14 D  341  LEU VAL VAL CYS THR VAL SER LEU PRO SER HIS LEU SER          
-SEQRES  15 D  341  ARG VAL SER LYS ARG ALA ARG PRO GLY GLU THR VAL ASN          
-SEQRES  16 D  341  LEU PRO PHE VAL MET VAL LEU ARG ASN VAL TYR ILE MET          
-SEQRES  17 D  341  LEU ILE ASN THR ILE ILE PHE LEU LYS THR ASN ASN TRP          
-SEQRES  18 D  341  HIS ALA GLY TRP ASN THR LEU SER PHE CYS ASN ASP VAL          
-SEQRES  19 D  341  PHE LYS GLN LYS LEU GLN LYS SER GLU CYS ILE LYS LEU          
-SEQRES  20 D  341  ARG GLU VAL PRO GLY ILE GLU ASP THR LEU PHE ALA VAL          
-SEQRES  21 D  341  LEU LYS LEU PRO GLU LEU CYS GLY GLU PHE GLY ASN ILE          
-SEQRES  22 D  341  LEU PRO LEU TRP ALA TRP GLY MET GLU THR LEU SER ASN          
-SEQRES  23 D  341  CYS LEU ARG SER MET SER PRO PHE VAL LEU SER LEU GLU          
-SEQRES  24 D  341  GLN THR PRO GLN HIS ALA ALA GLN GLU LEU LYS THR LEU          
-SEQRES  25 D  341  LEU PRO GLN MET THR PRO ALA ASN MET SER SER GLY ALA          
-SEQRES  26 D  341  TRP ASN ILE LEU LYS GLU LEU VAL ASN ALA VAL GLN ASP          
-SEQRES  27 D  341  ASN THR SER                                                  
-HET    ADP  A 400       8                                                       
-HET    BVP  A 500      23                                                       
-HET    ADP  B1400      27                                                       
-HET    BVP  B1500      23                                                       
-HET    ADP  C2400      27                                                       
-HET    BVP  C2500      23                                                       
-HET    ADP  D3400      27                                                       
-HET    BVP  D3500      23                                                       
-HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
-HETNAM     BVP (E)-5-(2-BROMOVINYL)-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
-HETSYN     BVP BVDU-MP                                                          
-FORMUL   5  ADP    4(C10 H15 N5 O10 P2)                                         
-FORMUL   6  BVP    4(C11 H14 BR N2 O8 P)                                        
-FORMUL  13  HOH   *2(H2 O)                                                      
-HELIX    1   1 THR A   26  HIS A   35  1                                  10    
-HELIX    2   2 THR A   39  ASN A   41  5                                   3    
-HELIX    3   3 PRO A   49  ARG A   54  1                                   6    
-HELIX    4   4 ASP A   60  ASN A   74  1                                  15    
-HELIX    5   5 SER A   78  PHE A   93  1                                  16    
-HELIX    6   6 PHE A   93  LEU A  107  1                                  15    
-HELIX    7   7 PRO A  132  ILE A  137  1                                   6    
-HELIX    8   8 ILE A  137  VAL A  146  1                                  10    
-HELIX    9   9 SER A  150  ALA A  152  5                                   3    
-HELIX   10  10 ALA A  153  PHE A  159  1                                   7    
-HELIX   11  11 SER A  176  VAL A  184  1                                   9    
-HELIX   12  12 ASN A  195  ASN A  219  1                                  25    
-HELIX   13  13 ALA A  223  LEU A  228  5                                   6    
-HELIX   14  14 ASN A  232  GLN A  240  1                                   9    
-HELIX   15  15 GLY A  252  THR A  256  5                                   5    
-HELIX   16  16 LEU A  257  LYS A  262  1                                   6    
-HELIX   17  17 LEU A  263  CYS A  267  5                                   5    
-HELIX   18  18 LEU A  274  MET A  291  1                                  18    
-HELIX   19  19 THR A  301  LEU A  313  1                                  13    
-HELIX   20  20 PRO A  314  MET A  316  5                                   3    
-HELIX   21  21 SER A  322  GLN A  337  1                                  16    
-HELIX   22  22 THR B   26  GLU B   31  1                                   6    
-HELIX   23  23 PHE B   32  ALA B   37  1                                   6    
-HELIX   24  24 THR B   39  ASN B   41  5                                   3    
-HELIX   25  25 PRO B   49  ARG B   54  1                                   6    
-HELIX   26  26 ASP B   60  ASN B   74  1                                  15    
-HELIX   27  27 SER B   78  PHE B   93  1                                  16    
-HELIX   28  28 PHE B   93  LEU B  107  1                                  15    
-HELIX   29  29 PRO B  132  ILE B  137  1                                   6    
-HELIX   30  30 ILE B  137  VAL B  146  1                                  10    
-HELIX   31  31 SER B  150  ALA B  152  5                                   3    
-HELIX   32  32 ALA B  153  PHE B  159  1                                   7    
-HELIX   33  33 SER B  176  VAL B  184  1                                   9    
-HELIX   34  34 ASN B  195  ASN B  219  1                                  25    
-HELIX   35  35 ALA B  223  LEU B  228  5                                   6    
-HELIX   36  36 ASN B  232  SER B  242  1                                  11    
-HELIX   37  37 GLY B  252  THR B  256  5                                   5    
-HELIX   38  38 LEU B  257  LYS B  262  1                                   6    
-HELIX   39  39 LEU B  263  CYS B  267  5                                   5    
-HELIX   40  40 LEU B  274  MET B  291  1                                  18    
-HELIX   41  41 THR B  301  LEU B  313  1                                  13    
-HELIX   42  42 PRO B  314  MET B  316  5                                   3    
-HELIX   43  43 SER B  322  GLN B  337  1                                  16    
-HELIX   44  44 THR C   26  GLU C   31  1                                   6    
-HELIX   45  45 THR C   39  ASN C   41  5                                   3    
-HELIX   46  46 PRO C   49  ARG C   54  1                                   6    
-HELIX   47  47 ASP C   60  ASN C   74  1                                  15    
-HELIX   48  48 SER C   78  PHE C   93  1                                  16    
-HELIX   49  49 PHE C   93  LEU C  107  1                                  15    
-HELIX   50  50 PRO C  132  ILE C  137  1                                   6    
-HELIX   51  51 ILE C  137  VAL C  146  1                                  10    
-HELIX   52  52 SER C  150  ALA C  152  5                                   3    
-HELIX   53  53 ALA C  153  PHE C  159  1                                   7    
-HELIX   54  54 SER C  176  VAL C  184  1                                   9    
-HELIX   55  55 ASN C  195  ASN C  219  1                                  25    
-HELIX   56  56 ALA C  223  LEU C  228  5                                   6    
-HELIX   57  57 ASN C  232  SER C  242  1                                  11    
-HELIX   58  58 GLY C  252  THR C  256  5                                   5    
-HELIX   59  59 LEU C  257  LYS C  262  1                                   6    
-HELIX   60  60 LEU C  263  CYS C  267  5                                   5    
-HELIX   61  61 LEU C  274  MET C  291  1                                  18    
-HELIX   62  62 THR C  301  LEU C  313  1                                  13    
-HELIX   63  63 PRO C  314  MET C  316  5                                   3    
-HELIX   64  64 SER C  322  GLN C  337  1                                  16    
-HELIX   65  65 THR D   26  GLU D   31  1                                   6    
-HELIX   66  66 PHE D   32  ALA D   37  1                                   6    
-HELIX   67  67 THR D   39  ASN D   41  5                                   3    
-HELIX   68  68 PRO D   49  ARG D   54  1                                   6    
-HELIX   69  69 ASP D   60  ASN D   74  1                                  15    
-HELIX   70  70 SER D   78  PHE D   93  1                                  16    
-HELIX   71  71 PHE D   93  LEU D  107  1                                  15    
-HELIX   72  72 PRO D  132  ILE D  137  1                                   6    
-HELIX   73  73 ILE D  137  VAL D  146  1                                  10    
-HELIX   74  74 SER D  150  ALA D  152  5                                   3    
-HELIX   75  75 ALA D  153  PHE D  159  1                                   7    
-HELIX   76  76 SER D  176  VAL D  184  1                                   9    
-HELIX   77  77 ASN D  195  ASN D  219  1                                  25    
-HELIX   78  78 ALA D  223  LEU D  228  5                                   6    
-HELIX   79  79 ASN D  232  SER D  242  1                                  11    
-HELIX   80  80 GLY D  252  THR D  256  5                                   5    
-HELIX   81  81 LEU D  257  LYS D  262  1                                   6    
-HELIX   82  82 LEU D  263  CYS D  267  5                                   5    
-HELIX   83  83 LEU D  274  MET D  291  1                                  18    
-HELIX   84  84 THR D  301  LEU D  313  1                                  13    
-HELIX   85  85 PRO D  314  MET D  316  5                                   3    
-HELIX   86  86 SER D  322  GLN D  337  1                                  16    
-SHEET    1   A 5 SER A 292  SER A 297  0                                        
-SHEET    2   A 5 ASN A 169  THR A 174  1  N  VAL A 172   O  PHE A 294           
-SHEET    3   A 5 MET A  10  GLY A  19  1  N  TYR A  16   O  VAL A 171           
-SHEET    4   A 5 LYS A 124  ASP A 129  1  O  SER A 128   N  ILE A  15           
-SHEET    5   A 5 ILE A  43  ILE A  46  1  N  ILE A  46   O  ASP A 129           
-SHEET    1   B 4 SER A 292  SER A 297  0                                        
-SHEET    2   B 4 ASN A 169  THR A 174  1  N  VAL A 172   O  PHE A 294           
-SHEET    3   B 4 MET A  10  GLY A  19  1  N  TYR A  16   O  VAL A 171           
-SHEET    4   B 4 ALA A 319  MET A 321 -1  O  ALA A 319   N  VAL A  12           
-SHEET    1   C 5 SER B 292  SER B 297  0                                        
-SHEET    2   C 5 ASN B 169  THR B 174  1  N  LEU B 170   O  PHE B 294           
-SHEET    3   C 5 GLY B  11  GLY B  19  1  N  TYR B  16   O  VAL B 171           
-SHEET    4   C 5 LYS B 124  ASP B 129  1  O  SER B 128   N  ILE B  15           
-SHEET    5   C 5 ILE B  43  ILE B  46  1  N  ILE B  46   O  ASP B 129           
-SHEET    1   D 4 SER B 292  SER B 297  0                                        
-SHEET    2   D 4 ASN B 169  THR B 174  1  N  LEU B 170   O  PHE B 294           
-SHEET    3   D 4 GLY B  11  GLY B  19  1  N  TYR B  16   O  VAL B 171           
-SHEET    4   D 4 ALA B 319  ASN B 320 -1  O  ALA B 319   N  VAL B  12           
-SHEET    1   E 5 SER C 292  SER C 297  0                                        
-SHEET    2   E 5 ASN C 169  THR C 174  1  N  VAL C 172   O  PHE C 294           
-SHEET    3   E 5 MET C  10  GLY C  19  1  N  TYR C  16   O  VAL C 171           
-SHEET    4   E 5 LYS C 124  ASP C 129  1  O  SER C 128   N  ILE C  15           
-SHEET    5   E 5 ILE C  43  ILE C  46  1  N  ILE C  46   O  ASP C 129           
-SHEET    1   F 4 SER C 292  SER C 297  0                                        
-SHEET    2   F 4 ASN C 169  THR C 174  1  N  VAL C 172   O  PHE C 294           
-SHEET    3   F 4 MET C  10  GLY C  19  1  N  TYR C  16   O  VAL C 171           
-SHEET    4   F 4 ALA C 319  MET C 321 -1  O  ALA C 319   N  VAL C  12           
-SHEET    1   G 5 SER D 292  SER D 297  0                                        
-SHEET    2   G 5 ASN D 169  THR D 174  1  N  VAL D 172   O  PHE D 294           
-SHEET    3   G 5 GLY D  11  GLY D  19  1  N  TYR D  16   O  VAL D 171           
-SHEET    4   G 5 LYS D 124  ASP D 129  1  O  SER D 128   N  LEU D  17           
-SHEET    5   G 5 ILE D  43  ILE D  46  1  N  ILE D  46   O  ASP D 129           
-SHEET    1   H 4 SER D 292  SER D 297  0                                        
-SHEET    2   H 4 ASN D 169  THR D 174  1  N  VAL D 172   O  PHE D 294           
-SHEET    3   H 4 GLY D  11  GLY D  19  1  N  TYR D  16   O  VAL D 171           
-SHEET    4   H 4 ALA D 319  ASN D 320 -1  O  ALA D 319   N  VAL D  12           
-SITE     1 AC1  8 TYR A  21  GLY A  22  ILE A  23  GLY A  24                    
-SITE     2 AC1  8 LYS A  25  THR A  26  THR A  27  BVP A 500                    
-SITE     1 AC2 15 TYR A  21  GLY A  22  GLU A  48  TRP A  53                    
-SITE     2 AC2 15 ILE A  62  TYR A  66  GLN A  90  PHE A  93                    
-SITE     3 AC2 15 HIS A  97  ARG A 130  ALA A 134  SER A 135                    
-SITE     4 AC2 15 PHE A 139  ADP A 400  HOH A 600                               
-SITE     1 AC3 10 TYR B  21  GLY B  22  ILE B  23  GLY B  24                    
-SITE     2 AC3 10 LYS B  25  THR B  26  THR B  27  ARG B 183                    
-SITE     3 AC3 10 GLN B 300  BVP B1500                                          
-SITE     1 AC4 14 TYR B  21  GLY B  22  GLU B  48  TRP B  53                    
-SITE     2 AC4 14 ILE B  62  TYR B  66  GLN B  90  PHE B  93                    
-SITE     3 AC4 14 HIS B  97  ARG B 130  ALA B 134  SER B 135                    
-SITE     4 AC4 14 PHE B 139  ADP B1400                                          
-SITE     1 AC5 10 TYR C  21  GLY C  22  ILE C  23  GLY C  24                    
-SITE     2 AC5 10 LYS C  25  THR C  26  THR C  27  ARG C 183                    
-SITE     3 AC5 10 GLN C 300  BVP C2500                                          
-SITE     1 AC6 14 TYR C  21  GLY C  22  GLU C  48  TRP C  53                    
-SITE     2 AC6 14 ILE C  62  TYR C  66  GLN C  90  PHE C  93                    
-SITE     3 AC6 14 HIS C  97  ARG C 130  ALA C 134  SER C 135                    
-SITE     4 AC6 14 PHE C 139  ADP C2400                                          
-SITE     1 AC7 10 TYR D  21  GLY D  22  ILE D  23  GLY D  24                    
-SITE     2 AC7 10 LYS D  25  THR D  26  THR D  27  ARG D 183                    
-SITE     3 AC7 10 GLN D 300  BVP D3500                                          
-SITE     1 AC8 14 TYR D  21  GLY D  22  GLU D  48  TRP D  53                    
-SITE     2 AC8 14 ILE D  62  TYR D  66  GLN D  90  PHE D  93                    
-SITE     3 AC8 14 HIS D  97  ARG D 130  ALA D 134  SER D 135                    
-SITE     4 AC8 14 PHE D 139  ADP D3400                                          
-CRYST1   99.700   54.200  167.800  90.00  94.80  90.00 P 1 21 1      8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.010030  0.000000  0.000842        0.00000                         
-SCALE2      0.000000  0.018450  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.005980        0.00000                         
-ATOM      1  N   VAL A   8      80.585  -1.712  86.876  1.00 84.08           N  
-ATOM      2  CA  VAL A   8      81.081  -2.144  85.537  1.00 81.00           C  
-ATOM      3  C   VAL A   8      81.817  -0.989  84.849  1.00 78.04           C  
-ATOM      4  O   VAL A   8      82.548  -1.196  83.880  1.00 77.94           O  
-ATOM      5  CB  VAL A   8      79.899  -2.643  84.647  1.00 82.00           C  
-ATOM      6  CG1 VAL A   8      79.445  -4.028  85.102  1.00 71.97           C  
-ATOM      7  CG2 VAL A   8      78.726  -1.673  84.742  1.00 79.11           C  
-ATOM      8  N   LYS A   9      81.621   0.213  85.390  1.00 73.69           N  
-ATOM      9  CA  LYS A   9      82.197   1.488  84.926  1.00 69.93           C  
-ATOM     10  C   LYS A   9      83.671   1.508  84.455  1.00 67.02           C  
-ATOM     11  O   LYS A   9      84.467   0.642  84.820  1.00 75.34           O  
-ATOM     12  CB  LYS A   9      82.023   2.499  86.053  1.00 69.57           C  
-ATOM     13  CG  LYS A   9      81.417   3.827  85.689  1.00 72.41           C  
-ATOM     14  CD  LYS A   9      81.061   4.531  86.987  1.00 83.50           C  
-ATOM     15  CE  LYS A   9      80.914   6.038  86.841  1.00 87.01           C  
-ATOM     16  NZ  LYS A   9      80.626   6.690  88.160  1.00 83.26           N  
-ATOM     17  N   MET A  10      84.020   2.519  83.657  1.00 56.41           N  
-ATOM     18  CA  MET A  10      85.375   2.707  83.119  1.00 50.72           C  
-ATOM     19  C   MET A  10      85.458   4.115  82.544  1.00 49.31           C  
-ATOM     20  O   MET A  10      84.551   4.560  81.848  1.00 57.61           O  
-ATOM     21  CB  MET A  10      85.660   1.736  81.988  1.00 49.27           C  
-ATOM     22  CG  MET A  10      84.820   2.033  80.769  1.00 59.16           C  
-ATOM     23  SD  MET A  10      85.591   1.565  79.245  1.00 56.73           S  
-ATOM     24  CE  MET A  10      85.194  -0.177  79.217  1.00 70.61           C  
-ATOM     25  N   GLY A  11      86.557   4.806  82.794  1.00 44.74           N  
-ATOM     26  CA  GLY A  11      86.666   6.168  82.313  1.00 41.62           C  
-ATOM     27  C   GLY A  11      87.174   6.347  80.902  1.00 39.35           C  
-ATOM     28  O   GLY A  11      88.218   5.810  80.554  1.00 40.53           O  
-ATOM     29  N   VAL A  12      86.442   7.123  80.102  1.00 36.62           N  
-ATOM     30  CA  VAL A  12      86.801   7.401  78.710  1.00 26.16           C  
-ATOM     31  C   VAL A  12      87.385   8.794  78.565  1.00 18.43           C  
-ATOM     32  O   VAL A  12      87.386   9.588  79.510  1.00 12.94           O  
-ATOM     33  CB  VAL A  12      85.576   7.316  77.780  1.00 33.19           C  
-ATOM     34  CG1 VAL A  12      84.931   5.947  77.898  1.00 45.27           C  
-ATOM     35  CG2 VAL A  12      84.571   8.397  78.141  1.00 37.27           C  
-ATOM     36  N   LEU A  13      87.854   9.104  77.366  1.00 14.98           N  
-ATOM     37  CA  LEU A  13      88.456  10.409  77.113  1.00 16.99           C  
-ATOM     38  C   LEU A  13      87.887  11.048  75.856  1.00 16.60           C  
-ATOM     39  O   LEU A  13      88.353  10.764  74.756  1.00 17.01           O  
-ATOM     40  CB  LEU A  13      89.963  10.241  76.966  1.00 16.18           C  
-ATOM     41  CG  LEU A  13      90.831  11.289  77.645  1.00 13.50           C  
-ATOM     42  CD1 LEU A  13      90.406  11.404  79.102  1.00  9.56           C  
-ATOM     43  CD2 LEU A  13      92.298  10.907  77.529  1.00  7.70           C  
-ATOM     44  N   ARG A  14      86.882  11.910  76.016  1.00 17.62           N  
-ATOM     45  CA  ARG A  14      86.254  12.558  74.864  1.00 14.97           C  
-ATOM     46  C   ARG A  14      87.138  13.654  74.320  1.00 12.84           C  
-ATOM     47  O   ARG A  14      87.420  14.630  75.009  1.00 19.20           O  
-ATOM     48  CB  ARG A  14      84.865  13.117  75.228  1.00 11.91           C  
-ATOM     49  CG  ARG A  14      83.802  12.037  75.335  1.00 11.31           C  
-ATOM     50  CD  ARG A  14      82.383  12.538  75.192  1.00  7.16           C  
-ATOM     51  NE  ARG A  14      81.901  13.179  76.399  1.00 13.77           N  
-ATOM     52  CZ  ARG A  14      82.022  14.473  76.645  1.00 29.52           C  
-ATOM     53  NH1 ARG A  14      82.611  15.261  75.755  1.00 29.38           N  
-ATOM     54  NH2 ARG A  14      81.556  14.974  77.782  1.00 35.78           N  
-ATOM     55  N   ILE A  15      87.584  13.477  73.081  1.00  6.17           N  
-ATOM     56  CA  ILE A  15      88.453  14.449  72.438  1.00  7.14           C  
-ATOM     57  C   ILE A  15      87.930  14.875  71.074  1.00 14.73           C  
-ATOM     58  O   ILE A  15      87.883  14.082  70.139  1.00 20.59           O  
-ATOM     59  CB  ILE A  15      89.859  13.898  72.242  1.00  4.47           C  
-ATOM     60  CG1 ILE A  15      90.406  13.395  73.569  1.00  7.90           C  
-ATOM     61  CG2 ILE A  15      90.762  14.977  71.740  1.00  4.47           C  
-ATOM     62  CD1 ILE A  15      91.788  12.799  73.475  1.00  4.47           C  
-ATOM     63  N   TYR A  16      87.545  16.140  70.978  1.00 10.80           N  
-ATOM     64  CA  TYR A  16      87.034  16.717  69.755  1.00  4.47           C  
-ATOM     65  C   TYR A  16      88.147  17.545  69.123  1.00  4.47           C  
-ATOM     66  O   TYR A  16      88.689  18.454  69.732  1.00 21.43           O  
-ATOM     67  CB  TYR A  16      85.831  17.571  70.099  1.00  4.47           C  
-ATOM     68  CG  TYR A  16      84.670  16.761  70.602  1.00  4.47           C  
-ATOM     69  CD1 TYR A  16      83.879  16.053  69.724  1.00 14.28           C  
-ATOM     70  CD2 TYR A  16      84.359  16.709  71.940  1.00  4.47           C  
-ATOM     71  CE1 TYR A  16      82.795  15.306  70.166  1.00 30.52           C  
-ATOM     72  CE2 TYR A  16      83.277  15.971  72.396  1.00 10.04           C  
-ATOM     73  CZ  TYR A  16      82.494  15.269  71.502  1.00 21.14           C  
-ATOM     74  OH  TYR A  16      81.399  14.531  71.908  1.00 28.00           O  
-ATOM     75  N   LEU A  17      88.482  17.226  67.889  1.00  4.47           N  
-ATOM     76  CA  LEU A  17      89.567  17.885  67.188  1.00  7.88           C  
-ATOM     77  C   LEU A  17      89.025  18.879  66.172  1.00 16.91           C  
-ATOM     78  O   LEU A  17      88.445  18.478  65.160  1.00 24.13           O  
-ATOM     79  CB  LEU A  17      90.377  16.799  66.492  1.00 14.48           C  
-ATOM     80  CG  LEU A  17      91.805  17.036  66.053  1.00 20.90           C  
-ATOM     81  CD1 LEU A  17      92.607  17.510  67.245  1.00 35.99           C  
-ATOM     82  CD2 LEU A  17      92.377  15.746  65.498  1.00 12.66           C  
-ATOM     83  N   ASP A  18      89.222  20.171  66.419  1.00 18.46           N  
-ATOM     84  CA  ASP A  18      88.708  21.192  65.501  1.00 21.18           C  
-ATOM     85  C   ASP A  18      89.765  22.103  64.904  1.00 17.90           C  
-ATOM     86  O   ASP A  18      90.950  21.803  64.928  1.00 20.37           O  
-ATOM     87  CB  ASP A  18      87.648  22.056  66.203  1.00 23.96           C  
-ATOM     88  CG  ASP A  18      86.270  21.938  65.562  1.00 29.71           C  
-ATOM     89  OD1 ASP A  18      85.393  21.248  66.140  1.00 17.00           O  
-ATOM     90  OD2 ASP A  18      86.076  22.530  64.473  1.00 35.15           O  
-ATOM     91  N   GLY A  19      89.310  23.223  64.360  1.00 22.93           N  
-ATOM     92  CA  GLY A  19      90.215  24.183  63.764  1.00 30.02           C  
-ATOM     93  C   GLY A  19      89.714  24.552  62.389  1.00 33.28           C  
-ATOM     94  O   GLY A  19      88.578  24.214  62.039  1.00 27.00           O  
-ATOM     95  N   ALA A  20      90.557  25.243  61.620  1.00 35.35           N  
-ATOM     96  CA  ALA A  20      90.217  25.654  60.264  1.00 38.20           C  
-ATOM     97  C   ALA A  20      90.103  24.424  59.350  1.00 50.59           C  
-ATOM     98  O   ALA A  20      90.346  23.287  59.781  1.00 46.31           O  
-ATOM     99  CB  ALA A  20      91.268  26.605  59.734  1.00 26.44           C  
-ATOM    100  N   TYR A  21      89.734  24.654  58.089  1.00 61.10           N  
-ATOM    101  CA  TYR A  21      89.576  23.561  57.128  1.00 70.18           C  
-ATOM    102  C   TYR A  21      90.746  23.450  56.151  1.00 78.02           C  
-ATOM    103  O   TYR A  21      91.458  24.431  55.906  1.00 84.50           O  
-ATOM    104  CB  TYR A  21      88.250  23.711  56.356  1.00 70.62           C  
-ATOM    105  CG  TYR A  21      88.189  24.827  55.321  1.00 70.09           C  
-ATOM    106  CD1 TYR A  21      88.803  24.690  54.076  1.00 69.72           C  
-ATOM    107  CD2 TYR A  21      87.486  26.005  55.580  1.00 67.42           C  
-ATOM    108  CE1 TYR A  21      88.717  25.697  53.115  1.00 71.20           C  
-ATOM    109  CE2 TYR A  21      87.394  27.016  54.628  1.00 68.13           C  
-ATOM    110  CZ  TYR A  21      88.009  26.860  53.398  1.00 72.55           C  
-ATOM    111  OH  TYR A  21      87.907  27.869  52.457  1.00 72.37           O  
-ATOM    112  N   GLY A  22      90.938  22.250  55.598  1.00 79.10           N  
-ATOM    113  CA  GLY A  22      92.029  22.018  54.664  1.00 79.87           C  
-ATOM    114  C   GLY A  22      93.384  21.949  55.358  1.00 81.00           C  
-ATOM    115  O   GLY A  22      94.375  21.525  54.759  1.00 80.26           O  
-ATOM    116  N   ILE A  23      93.421  22.363  56.626  1.00 80.38           N  
-ATOM    117  CA  ILE A  23      94.649  22.362  57.421  1.00 78.62           C  
-ATOM    118  C   ILE A  23      95.286  20.975  57.550  1.00 80.45           C  
-ATOM    119  O   ILE A  23      96.505  20.861  57.700  1.00 86.07           O  
-ATOM    120  CB  ILE A  23      94.407  22.928  58.859  1.00 72.10           C  
-ATOM    121  CG1 ILE A  23      93.157  22.290  59.479  1.00 68.12           C  
-ATOM    122  CG2 ILE A  23      94.297  24.446  58.815  1.00 69.08           C  
-ATOM    123  CD1 ILE A  23      92.934  22.645  60.942  1.00 64.28           C  
-ATOM    124  N   GLY A  24      94.469  19.926  57.500  1.00 73.28           N  
-ATOM    125  CA  GLY A  24      95.005  18.581  57.614  1.00 66.42           C  
-ATOM    126  C   GLY A  24      94.713  17.897  58.937  1.00 61.50           C  
-ATOM    127  O   GLY A  24      95.411  16.955  59.329  1.00 58.31           O  
-ATOM    128  N   LYS A  25      93.673  18.361  59.623  1.00 57.89           N  
-ATOM    129  CA  LYS A  25      93.306  17.793  60.909  1.00 56.15           C  
-ATOM    130  C   LYS A  25      92.668  16.421  60.797  1.00 53.79           C  
-ATOM    131  O   LYS A  25      92.271  15.831  61.799  1.00 53.60           O  
-ATOM    132  CB  LYS A  25      92.378  18.746  61.676  1.00 52.69           C  
-ATOM    133  CG  LYS A  25      91.450  19.570  60.818  1.00 47.61           C  
-ATOM    134  CD  LYS A  25      90.308  20.125  61.640  1.00 43.90           C  
-ATOM    135  CE  LYS A  25      89.373  19.002  62.067  1.00 33.97           C  
-ATOM    136  NZ  LYS A  25      88.898  18.237  60.881  1.00 22.21           N  
-ATOM    137  N   THR A  26      92.568  15.905  59.582  1.00 56.70           N  
-ATOM    138  CA  THR A  26      91.984  14.583  59.398  1.00 69.38           C  
-ATOM    139  C   THR A  26      93.070  13.543  59.094  1.00 75.81           C  
-ATOM    140  O   THR A  26      93.064  12.454  59.674  1.00 77.98           O  
-ATOM    141  CB  THR A  26      90.916  14.576  58.266  1.00 70.19           C  
-ATOM    142  OG1 THR A  26      89.785  15.361  58.669  1.00 70.91           O  
-ATOM    143  CG2 THR A  26      90.444  13.156  57.981  1.00 71.19           C  
-ATOM    144  N   THR A  27      94.005  13.876  58.202  1.00 78.75           N  
-ATOM    145  CA  THR A  27      95.081  12.945  57.856  1.00 76.39           C  
-ATOM    146  C   THR A  27      96.073  12.884  59.014  1.00 72.28           C  
-ATOM    147  O   THR A  27      96.948  12.022  59.058  1.00 71.24           O  
-ATOM    148  CB  THR A  27      95.830  13.374  56.566  1.00 78.87           C  
-ATOM    149  OG1 THR A  27      94.935  14.075  55.692  1.00 79.55           O  
-ATOM    150  CG2 THR A  27      96.350  12.142  55.826  1.00 75.65           C  
-ATOM    151  N   ALA A  28      95.917  13.811  59.953  1.00 72.32           N  
-ATOM    152  CA  ALA A  28      96.770  13.870  61.134  1.00 76.56           C  
-ATOM    153  C   ALA A  28      96.036  13.270  62.340  1.00 77.41           C  
-ATOM    154  O   ALA A  28      96.654  12.958  63.366  1.00 73.20           O  
-ATOM    155  CB  ALA A  28      97.159  15.313  61.422  1.00 79.32           C  
-ATOM    156  N   ALA A  29      94.715  13.125  62.204  1.00 78.66           N  
-ATOM    157  CA  ALA A  29      93.867  12.555  63.252  1.00 73.92           C  
-ATOM    158  C   ALA A  29      93.781  11.055  63.030  1.00 73.34           C  
-ATOM    159  O   ALA A  29      93.449  10.298  63.940  1.00 71.37           O  
-ATOM    160  CB  ALA A  29      92.468  13.172  63.204  1.00 66.89           C  
-ATOM    161  N   GLU A  30      94.074  10.638  61.802  1.00 78.97           N  
-ATOM    162  CA  GLU A  30      94.055   9.230  61.438  1.00 80.90           C  
-ATOM    163  C   GLU A  30      95.418   8.625  61.764  1.00 80.36           C  
-ATOM    164  O   GLU A  30      95.501   7.537  62.330  1.00 81.00           O  
-ATOM    165  CB  GLU A  30      93.748   9.061  59.941  1.00 84.20           C  
-ATOM    166  CG  GLU A  30      92.309   9.412  59.540  1.00 93.48           C  
-ATOM    167  CD  GLU A  30      92.007   9.109  58.072  1.00103.45           C  
-ATOM    168  OE1 GLU A  30      92.159   7.939  57.652  1.00108.77           O  
-ATOM    169  OE2 GLU A  30      91.612  10.041  57.337  1.00104.06           O  
-ATOM    170  N   GLU A  31      96.485   9.341  61.419  1.00 78.67           N  
-ATOM    171  CA  GLU A  31      97.832   8.857  61.681  1.00 75.33           C  
-ATOM    172  C   GLU A  31      98.020   8.666  63.176  1.00 71.12           C  
-ATOM    173  O   GLU A  31      99.013   8.091  63.621  1.00 69.26           O  
-ATOM    174  CB  GLU A  31      98.869   9.845  61.150  1.00 81.32           C  
-ATOM    175  CG  GLU A  31     100.042   9.181  60.424  1.00 92.61           C  
-ATOM    176  CD  GLU A  31     100.775   8.137  61.271  1.00102.75           C  
-ATOM    177  OE1 GLU A  31     101.241   8.481  62.383  1.00107.29           O  
-ATOM    178  OE2 GLU A  31     100.894   6.971  60.820  1.00 99.13           O  
-ATOM    179  N   PHE A  32      97.063   9.160  63.951  1.00 69.83           N  
-ATOM    180  CA  PHE A  32      97.121   9.019  65.401  1.00 74.77           C  
-ATOM    181  C   PHE A  32      96.418   7.734  65.812  1.00 79.71           C  
-ATOM    182  O   PHE A  32      96.685   7.181  66.882  1.00 81.18           O  
-ATOM    183  CB  PHE A  32      96.436  10.198  66.089  1.00 69.54           C  
-ATOM    184  CG  PHE A  32      96.426  10.099  67.590  1.00 55.70           C  
-ATOM    185  CD1 PHE A  32      97.604  10.230  68.316  1.00 50.17           C  
-ATOM    186  CD2 PHE A  32      95.237   9.884  68.277  1.00 47.83           C  
-ATOM    187  CE1 PHE A  32      97.599  10.153  69.695  1.00 40.57           C  
-ATOM    188  CE2 PHE A  32      95.219   9.804  69.660  1.00 36.03           C  
-ATOM    189  CZ  PHE A  32      96.400   9.939  70.370  1.00 38.03           C  
-ATOM    190  N   LEU A  33      95.515   7.273  64.950  1.00 83.30           N  
-ATOM    191  CA  LEU A  33      94.749   6.057  65.198  1.00 83.41           C  
-ATOM    192  C   LEU A  33      95.584   4.813  64.868  1.00 87.17           C  
-ATOM    193  O   LEU A  33      95.500   3.811  65.566  1.00 89.07           O  
-ATOM    194  CB  LEU A  33      93.447   6.097  64.383  1.00 77.08           C  
-ATOM    195  CG  LEU A  33      92.424   4.969  64.531  1.00 70.43           C  
-ATOM    196  CD1 LEU A  33      92.070   4.759  65.995  1.00 66.47           C  
-ATOM    197  CD2 LEU A  33      91.183   5.325  63.728  1.00 64.61           C  
-ATOM    198  N   HIS A  34      96.428   4.897  63.840  1.00 92.68           N  
-ATOM    199  CA  HIS A  34      97.290   3.774  63.448  1.00 98.15           C  
-ATOM    200  C   HIS A  34      98.396   3.419  64.466  1.00101.75           C  
-ATOM    201  O   HIS A  34      98.692   2.240  64.677  1.00101.07           O  
-ATOM    202  CB  HIS A  34      97.965   4.065  62.096  1.00100.41           C  
-ATOM    203  CG  HIS A  34      97.318   3.393  60.922  1.00103.37           C  
-ATOM    204  ND1 HIS A  34      97.928   3.310  59.688  1.00101.37           N  
-ATOM    205  CD2 HIS A  34      96.115   2.784  60.788  1.00106.44           C  
-ATOM    206  CE1 HIS A  34      97.130   2.679  58.845  1.00102.13           C  
-ATOM    207  NE2 HIS A  34      96.024   2.350  59.487  1.00107.09           N  
-ATOM    208  N   HIS A  35      99.001   4.432  65.092  1.00105.02           N  
-ATOM    209  CA  HIS A  35     100.105   4.216  66.040  1.00107.10           C  
-ATOM    210  C   HIS A  35      99.779   4.231  67.541  1.00104.89           C  
-ATOM    211  O   HIS A  35     100.581   4.697  68.363  1.00101.95           O  
-ATOM    212  CB  HIS A  35     101.218   5.238  65.761  1.00112.00           C  
-ATOM    213  CG  HIS A  35     100.880   6.641  66.167  1.00109.18           C  
-ATOM    214  ND1 HIS A  35     101.660   7.721  65.813  1.00103.92           N  
-ATOM    215  CD2 HIS A  35      99.875   7.137  66.929  1.00104.15           C  
-ATOM    216  CE1 HIS A  35     101.152   8.818  66.341  1.00103.14           C  
-ATOM    217  NE2 HIS A  35     100.069   8.492  67.024  1.00102.71           N  
-ATOM    218  N   PHE A  36      98.616   3.707  67.901  1.00101.60           N  
-ATOM    219  CA  PHE A  36      98.216   3.682  69.299  1.00 97.47           C  
-ATOM    220  C   PHE A  36      97.059   2.719  69.456  1.00 93.93           C  
-ATOM    221  O   PHE A  36      96.774   2.239  70.557  1.00 85.77           O  
-ATOM    222  CB  PHE A  36      97.792   5.078  69.740  1.00100.00           C  
-ATOM    223  CG  PHE A  36      98.257   5.439  71.110  1.00 99.15           C  
-ATOM    224  CD1 PHE A  36      99.616   5.413  71.420  1.00101.29           C  
-ATOM    225  CD2 PHE A  36      97.345   5.809  72.091  1.00 92.10           C  
-ATOM    226  CE1 PHE A  36     100.062   5.749  72.692  1.00103.96           C  
-ATOM    227  CE2 PHE A  36      97.780   6.149  73.366  1.00101.10           C  
-ATOM    228  CZ  PHE A  36      99.143   6.119  73.671  1.00104.54           C  
-ATOM    229  N   ALA A  37      96.391   2.448  68.338  1.00 96.95           N  
-ATOM    230  CA  ALA A  37      95.267   1.522  68.341  1.00100.32           C  
-ATOM    231  C   ALA A  37      95.835   0.112  68.218  1.00103.14           C  
-ATOM    232  O   ALA A  37      95.217  -0.775  67.616  1.00102.71           O  
-ATOM    233  CB  ALA A  37      94.319   1.815  67.179  1.00 98.40           C  
-ATOM    234  N   ILE A  38      97.031  -0.074  68.782  1.00103.75           N  
-ATOM    235  CA  ILE A  38      97.719  -1.367  68.779  1.00 98.33           C  
-ATOM    236  C   ILE A  38      96.721  -2.363  69.382  1.00 94.64           C  
-ATOM    237  O   ILE A  38      96.594  -3.510  68.934  1.00 88.82           O  
-ATOM    238  CB  ILE A  38      99.011  -1.300  69.647  1.00 95.66           C  
-ATOM    239  CG1 ILE A  38      99.903  -0.140  69.173  1.00 90.19           C  
-ATOM    240  CG2 ILE A  38      99.772  -2.613  69.554  1.00 90.12           C  
-ATOM    241  CD1 ILE A  38     101.132   0.106  70.044  1.00 84.10           C  
-ATOM    242  N   THR A  39      96.017  -1.885  70.405  1.00 92.11           N  
-ATOM    243  CA  THR A  39      94.976  -2.641  71.085  1.00 88.30           C  
-ATOM    244  C   THR A  39      93.654  -2.045  70.566  1.00 85.84           C  
-ATOM    245  O   THR A  39      93.238  -0.954  70.970  1.00 80.92           O  
-ATOM    246  CB  THR A  39      95.098  -2.505  72.639  1.00 86.89           C  
-ATOM    247  OG1 THR A  39      93.792  -2.459  73.229  1.00 84.03           O  
-ATOM    248  CG2 THR A  39      95.900  -1.252  73.022  1.00 79.63           C  
-ATOM    249  N   PRO A  40      92.991  -2.763  69.641  1.00 85.48           N  
-ATOM    250  CA  PRO A  40      91.725  -2.393  68.998  1.00 79.55           C  
-ATOM    251  C   PRO A  40      90.677  -1.667  69.831  1.00 73.61           C  
-ATOM    252  O   PRO A  40      90.214  -0.598  69.440  1.00 73.08           O  
-ATOM    253  CB  PRO A  40      91.206  -3.730  68.470  1.00 82.32           C  
-ATOM    254  CG  PRO A  40      92.464  -4.425  68.076  1.00 85.86           C  
-ATOM    255  CD  PRO A  40      93.379  -4.137  69.257  1.00 88.84           C  
-ATOM    256  N   ASN A  41      90.301  -2.242  70.970  1.00 65.91           N  
-ATOM    257  CA  ASN A  41      89.268  -1.645  71.798  1.00 59.83           C  
-ATOM    258  C   ASN A  41      89.738  -0.514  72.697  1.00 56.95           C  
-ATOM    259  O   ASN A  41      89.080  -0.207  73.690  1.00 62.49           O  
-ATOM    260  CB  ASN A  41      88.578  -2.722  72.652  1.00 66.97           C  
-ATOM    261  CG  ASN A  41      87.064  -2.826  72.379  1.00 70.32           C  
-ATOM    262  OD1 ASN A  41      86.303  -3.349  73.204  1.00 66.90           O  
-ATOM    263  ND2 ASN A  41      86.632  -2.338  71.217  1.00 66.90           N  
-ATOM    264  N   ARG A  42      90.857   0.123  72.372  1.00 51.67           N  
-ATOM    265  CA  ARG A  42      91.301   1.216  73.231  1.00 48.88           C  
-ATOM    266  C   ARG A  42      90.992   2.570  72.636  1.00 45.76           C  
-ATOM    267  O   ARG A  42      91.129   3.579  73.315  1.00 53.98           O  
-ATOM    268  CB  ARG A  42      92.804   1.147  73.522  1.00 53.77           C  
-ATOM    269  CG  ARG A  42      93.199   1.996  74.735  1.00 54.73           C  
-ATOM    270  CD  ARG A  42      94.687   2.298  74.825  1.00 60.69           C  
-ATOM    271  NE  ARG A  42      94.956   3.308  75.853  1.00 66.58           N  
-ATOM    272  CZ  ARG A  42      96.096   3.993  75.969  1.00 71.86           C  
-ATOM    273  NH1 ARG A  42      97.092   3.776  75.120  1.00 84.00           N  
-ATOM    274  NH2 ARG A  42      96.238   4.916  76.917  1.00 54.92           N  
-ATOM    275  N   ILE A  43      90.558   2.603  71.380  1.00 41.96           N  
-ATOM    276  CA  ILE A  43      90.276   3.878  70.722  1.00 34.18           C  
-ATOM    277  C   ILE A  43      89.168   3.819  69.678  1.00 28.27           C  
-ATOM    278  O   ILE A  43      89.091   2.883  68.888  1.00 34.62           O  
-ATOM    279  CB  ILE A  43      91.553   4.410  70.065  1.00 33.26           C  
-ATOM    280  CG1 ILE A  43      91.319   5.798  69.503  1.00 26.92           C  
-ATOM    281  CG2 ILE A  43      92.009   3.462  68.972  1.00 38.79           C  
-ATOM    282  CD1 ILE A  43      92.584   6.401  68.960  1.00 35.77           C  
-ATOM    283  N   LEU A  44      88.321   4.841  69.671  1.00 22.64           N  
-ATOM    284  CA  LEU A  44      87.190   4.911  68.750  1.00 16.64           C  
-ATOM    285  C   LEU A  44      87.164   6.195  67.952  1.00 17.88           C  
-ATOM    286  O   LEU A  44      87.040   7.264  68.528  1.00 26.69           O  
-ATOM    287  CB  LEU A  44      85.886   4.813  69.532  1.00  8.07           C  
-ATOM    288  CG  LEU A  44      84.644   5.193  68.743  1.00  4.47           C  
-ATOM    289  CD1 LEU A  44      84.598   4.362  67.457  1.00 24.81           C  
-ATOM    290  CD2 LEU A  44      83.411   4.969  69.602  1.00  4.47           C  
-ATOM    291  N   LEU A  45      87.249   6.108  66.631  1.00 18.73           N  
-ATOM    292  CA  LEU A  45      87.232   7.327  65.836  1.00 19.37           C  
-ATOM    293  C   LEU A  45      85.889   7.603  65.169  1.00 15.86           C  
-ATOM    294  O   LEU A  45      85.194   6.686  64.748  1.00 26.78           O  
-ATOM    295  CB  LEU A  45      88.331   7.295  64.774  1.00 18.55           C  
-ATOM    296  CG  LEU A  45      88.303   8.570  63.912  1.00 42.86           C  
-ATOM    297  CD1 LEU A  45      88.559   9.806  64.790  1.00 41.89           C  
-ATOM    298  CD2 LEU A  45      89.339   8.471  62.796  1.00 51.21           C  
-ATOM    299  N   ILE A  46      85.533   8.875  65.076  1.00  4.47           N  
-ATOM    300  CA  ILE A  46      84.284   9.278  64.455  1.00 12.05           C  
-ATOM    301  C   ILE A  46      84.632  10.347  63.438  1.00 20.99           C  
-ATOM    302  O   ILE A  46      85.004  11.449  63.819  1.00 37.09           O  
-ATOM    303  CB  ILE A  46      83.327   9.895  65.485  1.00 10.43           C  
-ATOM    304  CG1 ILE A  46      82.978   8.869  66.554  1.00  9.32           C  
-ATOM    305  CG2 ILE A  46      82.074  10.382  64.799  1.00 24.55           C  
-ATOM    306  CD1 ILE A  46      82.052   9.392  67.627  1.00  4.91           C  
-ATOM    307  N   GLY A  47      84.506  10.042  62.153  1.00 19.81           N  
-ATOM    308  CA  GLY A  47      84.856  11.028  61.139  1.00 26.51           C  
-ATOM    309  C   GLY A  47      83.749  11.974  60.715  1.00 28.74           C  
-ATOM    310  O   GLY A  47      82.571  11.707  60.959  1.00 33.71           O  
-ATOM    311  N   GLU A  48      84.121  13.087  60.084  1.00 28.00           N  
-ATOM    312  CA  GLU A  48      83.129  14.051  59.622  1.00 26.69           C  
-ATOM    313  C   GLU A  48      82.147  13.307  58.735  1.00 19.43           C  
-ATOM    314  O   GLU A  48      82.556  12.478  57.932  1.00 24.33           O  
-ATOM    315  CB  GLU A  48      83.800  15.183  58.844  1.00 29.84           C  
-ATOM    316  CG  GLU A  48      84.480  16.211  59.747  1.00 46.20           C  
-ATOM    317  CD  GLU A  48      84.983  17.428  58.980  1.00 57.62           C  
-ATOM    318  OE1 GLU A  48      85.437  18.403  59.621  1.00 54.94           O  
-ATOM    319  OE2 GLU A  48      84.924  17.405  57.732  1.00 65.42           O  
-ATOM    320  N   PRO A  49      80.835  13.577  58.883  1.00 11.61           N  
-ATOM    321  CA  PRO A  49      79.790  12.926  58.097  1.00 10.31           C  
-ATOM    322  C   PRO A  49      79.536  13.534  56.703  1.00 16.18           C  
-ATOM    323  O   PRO A  49      78.416  13.943  56.395  1.00 22.39           O  
-ATOM    324  CB  PRO A  49      78.581  13.042  59.017  1.00  4.47           C  
-ATOM    325  CG  PRO A  49      78.749  14.386  59.556  1.00  4.47           C  
-ATOM    326  CD  PRO A  49      80.223  14.422  59.923  1.00  8.15           C  
-ATOM    327  N   LEU A  50      80.562  13.576  55.853  1.00 17.18           N  
-ATOM    328  CA  LEU A  50      80.415  14.144  54.515  1.00 13.45           C  
-ATOM    329  C   LEU A  50      79.229  13.532  53.806  1.00 16.75           C  
-ATOM    330  O   LEU A  50      78.469  14.238  53.154  1.00 27.99           O  
-ATOM    331  CB  LEU A  50      81.660  13.901  53.665  1.00  9.44           C  
-ATOM    332  CG  LEU A  50      83.024  14.195  54.281  1.00 25.88           C  
-ATOM    333  CD1 LEU A  50      84.076  14.054  53.190  1.00 35.73           C  
-ATOM    334  CD2 LEU A  50      83.062  15.589  54.885  1.00 30.57           C  
-ATOM    335  N   SER A  51      79.077  12.216  53.931  1.00 21.56           N  
-ATOM    336  CA  SER A  51      77.977  11.504  53.288  1.00 26.13           C  
-ATOM    337  C   SER A  51      76.615  12.157  53.518  1.00 28.75           C  
-ATOM    338  O   SER A  51      75.743  12.063  52.652  1.00 43.02           O  
-ATOM    339  CB  SER A  51      77.943  10.029  53.730  1.00 26.33           C  
-ATOM    340  OG  SER A  51      78.205   9.887  55.113  1.00 28.88           O  
-ATOM    341  N   TYR A  52      76.422  12.816  54.664  1.00 13.01           N  
-ATOM    342  CA  TYR A  52      75.152  13.495  54.929  1.00  6.22           C  
-ATOM    343  C   TYR A  52      75.190  14.955  54.457  1.00  8.31           C  
-ATOM    344  O   TYR A  52      74.198  15.515  53.985  1.00  5.47           O  
-ATOM    345  CB  TYR A  52      74.798  13.454  56.416  1.00  6.17           C  
-ATOM    346  CG  TYR A  52      74.311  12.101  56.929  1.00 12.27           C  
-ATOM    347  CD1 TYR A  52      75.210  11.074  57.202  1.00  6.57           C  
-ATOM    348  CD2 TYR A  52      72.950  11.853  57.138  1.00  4.47           C  
-ATOM    349  CE1 TYR A  52      74.778   9.839  57.668  1.00  6.64           C  
-ATOM    350  CE2 TYR A  52      72.512  10.619  57.596  1.00  8.89           C  
-ATOM    351  CZ  TYR A  52      73.435   9.613  57.861  1.00 12.76           C  
-ATOM    352  OH  TYR A  52      73.024   8.376  58.313  1.00 20.08           O  
-ATOM    353  N   TRP A  53      76.341  15.584  54.593  1.00 10.09           N  
-ATOM    354  CA  TRP A  53      76.451  16.950  54.150  1.00  4.47           C  
-ATOM    355  C   TRP A  53      76.266  16.991  52.651  1.00  7.01           C  
-ATOM    356  O   TRP A  53      75.605  17.885  52.139  1.00 11.80           O  
-ATOM    357  CB  TRP A  53      77.818  17.523  54.493  1.00  4.47           C  
-ATOM    358  CG  TRP A  53      78.053  17.689  55.933  1.00  4.47           C  
-ATOM    359  CD1 TRP A  53      77.117  17.731  56.925  1.00  4.47           C  
-ATOM    360  CD2 TRP A  53      79.316  17.867  56.562  1.00  4.57           C  
-ATOM    361  NE1 TRP A  53      77.725  17.924  58.142  1.00  4.47           N  
-ATOM    362  CE2 TRP A  53      79.077  18.009  57.946  1.00  5.81           C  
-ATOM    363  CE3 TRP A  53      80.630  17.923  56.093  1.00  4.47           C  
-ATOM    364  CZ2 TRP A  53      80.103  18.200  58.861  1.00 17.56           C  
-ATOM    365  CZ3 TRP A  53      81.651  18.118  57.006  1.00  9.14           C  
-ATOM    366  CH2 TRP A  53      81.384  18.254  58.374  1.00 19.42           C  
-ATOM    367  N   ARG A  54      76.850  16.026  51.947  1.00  4.47           N  
-ATOM    368  CA  ARG A  54      76.750  16.019  50.500  1.00 10.14           C  
-ATOM    369  C   ARG A  54      75.443  15.474  49.966  1.00  9.87           C  
-ATOM    370  O   ARG A  54      75.270  15.307  48.760  1.00 20.33           O  
-ATOM    371  CB  ARG A  54      77.944  15.293  49.873  1.00  9.17           C  
-ATOM    372  CG  ARG A  54      79.203  16.156  49.857  1.00 17.79           C  
-ATOM    373  CD  ARG A  54      80.243  15.621  48.897  1.00 36.01           C  
-ATOM    374  NE  ARG A  54      81.413  16.495  48.828  1.00 43.55           N  
-ATOM    375  CZ  ARG A  54      81.393  17.737  48.352  1.00 49.86           C  
-ATOM    376  NH1 ARG A  54      80.259  18.258  47.902  1.00 52.63           N  
-ATOM    377  NH2 ARG A  54      82.509  18.458  48.317  1.00 50.28           N  
-ATOM    378  N   ASN A  55      74.510  15.219  50.867  1.00  6.38           N  
-ATOM    379  CA  ASN A  55      73.201  14.743  50.466  1.00 10.27           C  
-ATOM    380  C   ASN A  55      72.261  14.835  51.644  1.00  7.73           C  
-ATOM    381  O   ASN A  55      71.589  13.862  52.018  1.00  4.47           O  
-ATOM    382  CB  ASN A  55      73.261  13.301  49.994  1.00 23.40           C  
-ATOM    383  CG  ASN A  55      71.888  12.755  49.683  1.00 38.99           C  
-ATOM    384  OD1 ASN A  55      71.176  13.289  48.822  1.00 43.73           O  
-ATOM    385  ND2 ASN A  55      71.492  11.702  50.396  1.00 38.90           N  
-ATOM    386  N   LEU A  56      72.218  16.013  52.245  1.00  9.27           N  
-ATOM    387  CA  LEU A  56      71.363  16.186  53.394  1.00 11.13           C  
-ATOM    388  C   LEU A  56      69.927  16.457  52.975  1.00 12.27           C  
-ATOM    389  O   LEU A  56      69.554  17.587  52.654  1.00  9.56           O  
-ATOM    390  CB  LEU A  56      71.890  17.301  54.288  1.00  4.47           C  
-ATOM    391  CG  LEU A  56      71.274  17.177  55.679  1.00  7.83           C  
-ATOM    392  CD1 LEU A  56      72.153  17.873  56.684  1.00 22.08           C  
-ATOM    393  CD2 LEU A  56      69.877  17.758  55.684  1.00 10.38           C  
-ATOM    394  N   ALA A  57      69.122  15.401  52.975  1.00 10.13           N  
-ATOM    395  CA  ALA A  57      67.726  15.531  52.604  1.00 13.87           C  
-ATOM    396  C   ALA A  57      67.544  16.227  51.256  1.00 18.81           C  
-ATOM    397  O   ALA A  57      66.600  16.993  51.056  1.00 20.17           O  
-ATOM    398  CB  ALA A  57      66.983  16.293  53.673  1.00 13.41           C  
-ATOM    399  N   GLY A  58      68.457  15.983  50.330  1.00 19.70           N  
-ATOM    400  CA  GLY A  58      68.290  16.584  49.027  1.00 19.10           C  
-ATOM    401  C   GLY A  58      69.310  17.594  48.573  1.00 23.49           C  
-ATOM    402  O   GLY A  58      69.641  17.638  47.388  1.00 39.47           O  
-ATOM    403  N   GLU A  59      69.826  18.410  49.478  1.00 13.11           N  
-ATOM    404  CA  GLU A  59      70.788  19.407  49.040  1.00 10.26           C  
-ATOM    405  C   GLU A  59      72.219  19.117  49.491  1.00  9.34           C  
-ATOM    406  O   GLU A  59      72.436  18.393  50.461  1.00  4.47           O  
-ATOM    407  CB  GLU A  59      70.312  20.786  49.507  1.00 10.13           C  
-ATOM    408  CG  GLU A  59      68.812  20.975  49.277  1.00 21.41           C  
-ATOM    409  CD  GLU A  59      68.337  22.420  49.392  1.00 27.18           C  
-ATOM    410  OE1 GLU A  59      68.634  23.081  50.406  1.00 16.39           O  
-ATOM    411  OE2 GLU A  59      67.646  22.891  48.464  1.00 40.48           O  
-ATOM    412  N   ASP A  60      73.191  19.657  48.755  1.00  9.47           N  
-ATOM    413  CA  ASP A  60      74.606  19.469  49.073  1.00 13.04           C  
-ATOM    414  C   ASP A  60      75.151  20.679  49.832  1.00 10.09           C  
-ATOM    415  O   ASP A  60      75.740  21.580  49.235  1.00  9.91           O  
-ATOM    416  CB  ASP A  60      75.418  19.275  47.790  1.00 18.58           C  
-ATOM    417  CG  ASP A  60      76.911  19.115  48.061  1.00 33.26           C  
-ATOM    418  OD1 ASP A  60      77.499  19.992  48.752  1.00 28.79           O  
-ATOM    419  OD2 ASP A  60      77.493  18.112  47.577  1.00 37.16           O  
-ATOM    420  N   ALA A  61      74.968  20.690  51.146  1.00  4.47           N  
-ATOM    421  CA  ALA A  61      75.426  21.803  51.952  1.00  4.47           C  
-ATOM    422  C   ALA A  61      76.706  22.429  51.429  1.00  9.86           C  
-ATOM    423  O   ALA A  61      76.763  23.639  51.207  1.00  8.82           O  
-ATOM    424  CB  ALA A  61      75.623  21.359  53.372  1.00  4.47           C  
-ATOM    425  N   ILE A  62      77.730  21.611  51.209  1.00 15.13           N  
-ATOM    426  CA  ILE A  62      78.998  22.158  50.746  1.00 15.60           C  
-ATOM    427  C   ILE A  62      78.915  22.938  49.452  1.00 12.25           C  
-ATOM    428  O   ILE A  62      79.214  24.135  49.433  1.00 14.83           O  
-ATOM    429  CB  ILE A  62      80.081  21.073  50.633  1.00 14.63           C  
-ATOM    430  CG1 ILE A  62      80.578  20.722  52.049  1.00 13.60           C  
-ATOM    431  CG2 ILE A  62      81.212  21.560  49.728  1.00 11.28           C  
-ATOM    432  CD1 ILE A  62      81.825  19.847  52.118  1.00 18.42           C  
-ATOM    433  N   CYS A  63      78.516  22.280  48.374  1.00  5.73           N  
-ATOM    434  CA  CYS A  63      78.409  22.982  47.106  1.00 11.93           C  
-ATOM    435  C   CYS A  63      77.581  24.262  47.271  1.00 11.62           C  
-ATOM    436  O   CYS A  63      77.994  25.342  46.827  1.00 12.61           O  
-ATOM    437  CB  CYS A  63      77.757  22.081  46.077  1.00 20.08           C  
-ATOM    438  SG  CYS A  63      77.647  22.784  44.439  1.00 48.20           S  
-ATOM    439  N   GLY A  64      76.426  24.130  47.928  1.00  8.12           N  
-ATOM    440  CA  GLY A  64      75.529  25.257  48.153  1.00  5.85           C  
-ATOM    441  C   GLY A  64      76.115  26.456  48.886  1.00  7.60           C  
-ATOM    442  O   GLY A  64      75.807  27.611  48.568  1.00  4.47           O  
-ATOM    443  N   ILE A  65      76.958  26.200  49.877  1.00  4.47           N  
-ATOM    444  CA  ILE A  65      77.546  27.308  50.593  1.00  7.56           C  
-ATOM    445  C   ILE A  65      78.569  28.009  49.714  1.00 14.15           C  
-ATOM    446  O   ILE A  65      78.716  29.219  49.783  1.00 24.70           O  
-ATOM    447  CB  ILE A  65      78.240  26.869  51.858  1.00  7.35           C  
-ATOM    448  CG1 ILE A  65      78.547  28.094  52.704  1.00  4.47           C  
-ATOM    449  CG2 ILE A  65      79.541  26.171  51.516  1.00 18.95           C  
-ATOM    450  CD1 ILE A  65      78.365  27.850  54.184  1.00 18.69           C  
-ATOM    451  N   TYR A  66      79.290  27.264  48.890  1.00 11.85           N  
-ATOM    452  CA  TYR A  66      80.253  27.917  48.038  1.00 11.03           C  
-ATOM    453  C   TYR A  66      79.562  28.457  46.800  1.00 14.28           C  
-ATOM    454  O   TYR A  66      79.660  29.644  46.500  1.00 23.24           O  
-ATOM    455  CB  TYR A  66      81.388  26.959  47.661  1.00 21.52           C  
-ATOM    456  CG  TYR A  66      82.291  26.649  48.829  1.00 25.42           C  
-ATOM    457  CD1 TYR A  66      82.292  25.391  49.416  1.00 27.65           C  
-ATOM    458  CD2 TYR A  66      83.090  27.641  49.399  1.00 33.55           C  
-ATOM    459  CE1 TYR A  66      83.062  25.121  50.557  1.00 34.27           C  
-ATOM    460  CE2 TYR A  66      83.865  27.388  50.542  1.00 39.29           C  
-ATOM    461  CZ  TYR A  66      83.842  26.120  51.122  1.00 37.22           C  
-ATOM    462  OH  TYR A  66      84.554  25.850  52.282  1.00 31.62           O  
-ATOM    463  N   GLY A  67      78.846  27.601  46.088  1.00 11.69           N  
-ATOM    464  CA  GLY A  67      78.181  28.054  44.884  1.00 23.11           C  
-ATOM    465  C   GLY A  67      77.445  29.363  45.080  1.00 20.31           C  
-ATOM    466  O   GLY A  67      77.432  30.229  44.195  1.00 24.25           O  
-ATOM    467  N   THR A  68      76.828  29.509  46.244  1.00  6.66           N  
-ATOM    468  CA  THR A  68      76.088  30.723  46.533  1.00  5.91           C  
-ATOM    469  C   THR A  68      76.962  31.969  46.475  1.00  4.47           C  
-ATOM    470  O   THR A  68      76.503  33.044  46.119  1.00  4.81           O  
-ATOM    471  CB  THR A  68      75.419  30.634  47.905  1.00 10.74           C  
-ATOM    472  OG1 THR A  68      74.267  29.791  47.809  1.00 26.94           O  
-ATOM    473  CG2 THR A  68      74.994  32.008  48.391  1.00  8.43           C  
-ATOM    474  N   GLN A  69      78.228  31.833  46.824  1.00  4.73           N  
-ATOM    475  CA  GLN A  69      79.103  32.981  46.780  1.00  6.46           C  
-ATOM    476  C   GLN A  69      79.472  33.238  45.336  1.00  8.94           C  
-ATOM    477  O   GLN A  69      79.489  34.378  44.891  1.00 22.73           O  
-ATOM    478  CB  GLN A  69      80.350  32.750  47.629  1.00 17.39           C  
-ATOM    479  CG  GLN A  69      80.048  32.446  49.098  1.00 24.46           C  
-ATOM    480  CD  GLN A  69      78.933  33.304  49.664  1.00 25.32           C  
-ATOM    481  OE1 GLN A  69      78.951  34.529  49.535  1.00 33.21           O  
-ATOM    482  NE2 GLN A  69      77.958  32.663  50.304  1.00 18.60           N  
-ATOM    483  N   THR A  70      79.767  32.189  44.589  1.00  6.76           N  
-ATOM    484  CA  THR A  70      80.084  32.380  43.181  1.00 18.04           C  
-ATOM    485  C   THR A  70      78.876  33.062  42.527  1.00 16.37           C  
-ATOM    486  O   THR A  70      79.024  34.013  41.767  1.00 21.08           O  
-ATOM    487  CB  THR A  70      80.327  31.043  42.462  1.00 24.98           C  
-ATOM    488  OG1 THR A  70      81.371  30.322  43.127  1.00 40.87           O  
-ATOM    489  CG2 THR A  70      80.731  31.290  41.017  1.00 25.67           C  
-ATOM    490  N   ARG A  71      77.681  32.570  42.836  1.00 11.44           N  
-ATOM    491  CA  ARG A  71      76.449  33.129  42.299  1.00  4.47           C  
-ATOM    492  C   ARG A  71      76.243  34.577  42.738  1.00  4.47           C  
-ATOM    493  O   ARG A  71      75.559  35.347  42.065  1.00  8.89           O  
-ATOM    494  CB  ARG A  71      75.264  32.280  42.741  1.00  4.47           C  
-ATOM    495  CG  ARG A  71      74.581  31.573  41.601  1.00  4.47           C  
-ATOM    496  CD  ARG A  71      73.799  30.377  42.081  1.00  4.47           C  
-ATOM    497  NE  ARG A  71      72.630  30.730  42.888  1.00 17.57           N  
-ATOM    498  CZ  ARG A  71      71.477  31.178  42.398  1.00 10.35           C  
-ATOM    499  NH1 ARG A  71      71.333  31.339  41.093  1.00 21.08           N  
-ATOM    500  NH2 ARG A  71      70.456  31.440  43.209  1.00  9.21           N  
-ATOM    501  N   ARG A  72      76.827  34.954  43.867  1.00  4.62           N  
-ATOM    502  CA  ARG A  72      76.701  36.328  44.340  1.00  6.61           C  
-ATOM    503  C   ARG A  72      77.612  37.251  43.534  1.00  7.61           C  
-ATOM    504  O   ARG A  72      77.193  38.332  43.133  1.00  4.47           O  
-ATOM    505  CB  ARG A  72      77.057  36.424  45.818  1.00  4.47           C  
-ATOM    506  CG  ARG A  72      77.272  37.824  46.297  1.00  4.47           C  
-ATOM    507  CD  ARG A  72      77.279  37.879  47.819  1.00 27.53           C  
-ATOM    508  NE  ARG A  72      77.562  39.223  48.333  1.00 46.86           N  
-ATOM    509  CZ  ARG A  72      77.570  39.549  49.625  1.00 47.37           C  
-ATOM    510  NH1 ARG A  72      77.304  38.631  50.548  1.00 46.76           N  
-ATOM    511  NH2 ARG A  72      77.863  40.791  49.997  1.00 45.97           N  
-ATOM    512  N   LEU A  73      78.847  36.817  43.289  1.00  4.47           N  
-ATOM    513  CA  LEU A  73      79.793  37.627  42.535  1.00 11.22           C  
-ATOM    514  C   LEU A  73      79.347  37.898  41.122  1.00 19.19           C  
-ATOM    515  O   LEU A  73      79.575  38.988  40.604  1.00 26.25           O  
-ATOM    516  CB  LEU A  73      81.165  36.966  42.501  1.00  9.34           C  
-ATOM    517  CG  LEU A  73      82.028  37.174  43.747  1.00 29.13           C  
-ATOM    518  CD1 LEU A  73      81.173  37.278  45.018  1.00 24.51           C  
-ATOM    519  CD2 LEU A  73      83.008  36.009  43.841  1.00 44.41           C  
-ATOM    520  N   ASN A  74      78.714  36.909  40.497  1.00 20.51           N  
-ATOM    521  CA  ASN A  74      78.258  37.044  39.118  1.00 19.41           C  
-ATOM    522  C   ASN A  74      76.985  37.846  39.063  1.00 18.53           C  
-ATOM    523  O   ASN A  74      76.505  38.212  37.993  1.00 20.22           O  
-ATOM    524  CB  ASN A  74      78.039  35.667  38.511  1.00 30.42           C  
-ATOM    525  CG  ASN A  74      79.314  34.845  38.465  1.00 38.87           C  
-ATOM    526  OD1 ASN A  74      79.278  33.620  38.315  1.00 50.01           O  
-ATOM    527  ND2 ASN A  74      80.451  35.519  38.586  1.00 30.90           N  
-ATOM    528  N   GLY A  75      76.441  38.132  40.232  1.00 20.87           N  
-ATOM    529  CA  GLY A  75      75.226  38.916  40.269  1.00 30.94           C  
-ATOM    530  C   GLY A  75      74.035  38.110  39.809  1.00 29.65           C  
-ATOM    531  O   GLY A  75      73.026  38.675  39.392  1.00 36.65           O  
-ATOM    532  N   ASP A  76      74.154  36.789  39.862  1.00 20.15           N  
-ATOM    533  CA  ASP A  76      73.044  35.940  39.474  1.00 15.95           C  
-ATOM    534  C   ASP A  76      71.976  36.065  40.563  1.00 11.56           C  
-ATOM    535  O   ASP A  76      70.827  35.673  40.365  1.00  9.80           O  
-ATOM    536  CB  ASP A  76      73.493  34.480  39.354  1.00 35.61           C  
-ATOM    537  CG  ASP A  76      74.290  34.198  38.077  1.00 56.07           C  
-ATOM    538  OD1 ASP A  76      74.747  33.041  37.893  1.00 62.53           O  
-ATOM    539  OD2 ASP A  76      74.456  35.124  37.253  1.00 65.65           O  
-ATOM    540  N   VAL A  77      72.360  36.621  41.712  1.00  4.75           N  
-ATOM    541  CA  VAL A  77      71.423  36.787  42.815  1.00  6.35           C  
-ATOM    542  C   VAL A  77      71.760  37.974  43.704  1.00 10.65           C  
-ATOM    543  O   VAL A  77      72.934  38.333  43.882  1.00 10.11           O  
-ATOM    544  CB  VAL A  77      71.368  35.543  43.704  1.00 11.76           C  
-ATOM    545  CG1 VAL A  77      72.597  35.486  44.607  1.00 15.79           C  
-ATOM    546  CG2 VAL A  77      70.111  35.575  44.527  1.00 18.27           C  
-ATOM    547  N   SER A  78      70.710  38.566  44.268  1.00 11.77           N  
-ATOM    548  CA  SER A  78      70.831  39.730  45.142  1.00 11.15           C  
-ATOM    549  C   SER A  78      71.739  39.452  46.326  1.00  8.93           C  
-ATOM    550  O   SER A  78      71.665  38.379  46.915  1.00 22.78           O  
-ATOM    551  CB  SER A  78      69.447  40.128  45.652  1.00  8.97           C  
-ATOM    552  OG  SER A  78      69.552  41.109  46.662  1.00 28.66           O  
-ATOM    553  N   PRO A  79      72.608  40.406  46.693  1.00  4.47           N  
-ATOM    554  CA  PRO A  79      73.500  40.182  47.832  1.00  9.33           C  
-ATOM    555  C   PRO A  79      72.685  39.986  49.105  1.00 13.16           C  
-ATOM    556  O   PRO A  79      73.121  39.306  50.026  1.00 16.53           O  
-ATOM    557  CB  PRO A  79      74.345  41.447  47.865  1.00  4.47           C  
-ATOM    558  CG  PRO A  79      73.370  42.469  47.442  1.00 14.59           C  
-ATOM    559  CD  PRO A  79      72.708  41.798  46.243  1.00 14.59           C  
-ATOM    560  N   GLU A  80      71.498  40.581  49.155  1.00 17.81           N  
-ATOM    561  CA  GLU A  80      70.635  40.417  50.318  1.00 14.10           C  
-ATOM    562  C   GLU A  80      70.168  38.953  50.375  1.00 13.09           C  
-ATOM    563  O   GLU A  80      70.148  38.347  51.446  1.00 10.29           O  
-ATOM    564  CB  GLU A  80      69.438  41.362  50.232  1.00 17.40           C  
-ATOM    565  CG  GLU A  80      68.548  41.331  51.459  1.00 38.01           C  
-ATOM    566  CD  GLU A  80      67.472  42.414  51.450  1.00 55.54           C  
-ATOM    567  OE1 GLU A  80      67.826  43.611  51.330  1.00 61.48           O  
-ATOM    568  OE2 GLU A  80      66.274  42.067  51.573  1.00 58.01           O  
-ATOM    569  N   ASP A  81      69.804  38.380  49.230  1.00  4.47           N  
-ATOM    570  CA  ASP A  81      69.379  36.991  49.223  1.00 10.24           C  
-ATOM    571  C   ASP A  81      70.576  36.068  49.439  1.00 12.74           C  
-ATOM    572  O   ASP A  81      70.517  35.103  50.205  1.00 15.32           O  
-ATOM    573  CB  ASP A  81      68.690  36.634  47.906  1.00  4.73           C  
-ATOM    574  CG  ASP A  81      67.392  37.397  47.697  1.00 23.28           C  
-ATOM    575  OD1 ASP A  81      66.600  37.544  48.660  1.00 24.77           O  
-ATOM    576  OD2 ASP A  81      67.158  37.842  46.553  1.00 37.88           O  
-ATOM    577  N   ALA A  82      71.672  36.373  48.765  1.00 16.88           N  
-ATOM    578  CA  ALA A  82      72.868  35.556  48.886  1.00 21.93           C  
-ATOM    579  C   ALA A  82      73.222  35.326  50.347  1.00 21.06           C  
-ATOM    580  O   ALA A  82      73.808  34.304  50.699  1.00 25.24           O  
-ATOM    581  CB  ALA A  82      74.034  36.221  48.162  1.00 22.71           C  
-ATOM    582  N   GLN A  83      72.863  36.272  51.203  1.00 18.83           N  
-ATOM    583  CA  GLN A  83      73.183  36.123  52.616  1.00 19.17           C  
-ATOM    584  C   GLN A  83      72.229  35.150  53.240  1.00 11.38           C  
-ATOM    585  O   GLN A  83      72.640  34.264  53.966  1.00 15.17           O  
-ATOM    586  CB  GLN A  83      73.095  37.462  53.356  1.00 25.81           C  
-ATOM    587  CG  GLN A  83      73.984  38.538  52.767  1.00 23.85           C  
-ATOM    588  CD  GLN A  83      74.197  39.688  53.704  1.00 21.87           C  
-ATOM    589  OE1 GLN A  83      73.242  40.304  54.198  1.00 20.66           O  
-ATOM    590  NE2 GLN A  83      75.461  39.993  53.961  1.00 25.33           N  
-ATOM    591  N   ARG A  84      70.947  35.322  52.951  1.00 11.42           N  
-ATOM    592  CA  ARG A  84      69.929  34.446  53.506  1.00 10.46           C  
-ATOM    593  C   ARG A  84      70.164  33.064  52.958  1.00 11.53           C  
-ATOM    594  O   ARG A  84      70.102  32.061  53.686  1.00 12.22           O  
-ATOM    595  CB  ARG A  84      68.543  34.956  53.125  1.00  4.47           C  
-ATOM    596  CG  ARG A  84      68.231  36.251  53.839  1.00 13.10           C  
-ATOM    597  CD  ARG A  84      67.134  37.048  53.186  1.00 12.93           C  
-ATOM    598  NE  ARG A  84      67.013  38.349  53.833  1.00 11.10           N  
-ATOM    599  CZ  ARG A  84      66.204  39.314  53.416  1.00 21.48           C  
-ATOM    600  NH1 ARG A  84      65.441  39.127  52.347  1.00 31.06           N  
-ATOM    601  NH2 ARG A  84      66.153  40.465  54.070  1.00 30.00           N  
-ATOM    602  N   LEU A  85      70.461  33.019  51.666  1.00  5.56           N  
-ATOM    603  CA  LEU A  85      70.716  31.758  51.010  1.00  4.47           C  
-ATOM    604  C   LEU A  85      71.866  31.058  51.716  1.00  8.33           C  
-ATOM    605  O   LEU A  85      71.826  29.852  51.937  1.00 12.91           O  
-ATOM    606  CB  LEU A  85      71.033  31.991  49.537  1.00  4.47           C  
-ATOM    607  CG  LEU A  85      70.147  31.176  48.593  1.00  4.91           C  
-ATOM    608  CD1 LEU A  85      68.696  31.216  49.033  1.00  4.47           C  
-ATOM    609  CD2 LEU A  85      70.267  31.736  47.208  1.00 15.48           C  
-ATOM    610  N   THR A  86      72.880  31.819  52.105  1.00  8.59           N  
-ATOM    611  CA  THR A  86      74.017  31.231  52.795  1.00  4.47           C  
-ATOM    612  C   THR A  86      73.566  30.621  54.111  1.00  4.47           C  
-ATOM    613  O   THR A  86      73.819  29.447  54.366  1.00  4.65           O  
-ATOM    614  CB  THR A  86      75.117  32.273  53.081  1.00  9.62           C  
-ATOM    615  OG1 THR A  86      75.578  32.853  51.851  1.00  5.78           O  
-ATOM    616  CG2 THR A  86      76.284  31.619  53.794  1.00  4.47           C  
-ATOM    617  N   ALA A  87      72.896  31.417  54.940  1.00  4.47           N  
-ATOM    618  CA  ALA A  87      72.414  30.947  56.242  1.00  8.21           C  
-ATOM    619  C   ALA A  87      71.771  29.591  56.085  1.00 13.97           C  
-ATOM    620  O   ALA A  87      72.011  28.683  56.883  1.00 14.80           O  
-ATOM    621  CB  ALA A  87      71.407  31.913  56.825  1.00 11.52           C  
-ATOM    622  N   HIS A  88      70.953  29.459  55.046  1.00 13.93           N  
-ATOM    623  CA  HIS A  88      70.279  28.198  54.786  1.00  8.94           C  
-ATOM    624  C   HIS A  88      71.259  27.045  54.737  1.00  6.03           C  
-ATOM    625  O   HIS A  88      71.167  26.121  55.541  1.00  4.64           O  
-ATOM    626  CB  HIS A  88      69.530  28.247  53.469  1.00  4.47           C  
-ATOM    627  CG  HIS A  88      68.946  26.930  53.073  1.00  7.11           C  
-ATOM    628  ND1 HIS A  88      67.938  26.315  53.789  1.00  5.63           N  
-ATOM    629  CD2 HIS A  88      69.239  26.102  52.041  1.00 12.22           C  
-ATOM    630  CE1 HIS A  88      67.635  25.164  53.211  1.00 11.52           C  
-ATOM    631  NE2 HIS A  88      68.409  25.011  52.150  1.00 19.09           N  
-ATOM    632  N   PHE A  89      72.190  27.097  53.784  1.00  7.78           N  
-ATOM    633  CA  PHE A  89      73.181  26.038  53.638  1.00  4.47           C  
-ATOM    634  C   PHE A  89      74.029  25.866  54.875  1.00  4.47           C  
-ATOM    635  O   PHE A  89      74.121  24.768  55.418  1.00 16.45           O  
-ATOM    636  CB  PHE A  89      74.065  26.295  52.432  1.00  4.47           C  
-ATOM    637  CG  PHE A  89      73.323  26.253  51.143  1.00  4.47           C  
-ATOM    638  CD1 PHE A  89      73.105  27.401  50.418  1.00  4.47           C  
-ATOM    639  CD2 PHE A  89      72.835  25.056  50.657  1.00  4.98           C  
-ATOM    640  CE1 PHE A  89      72.415  27.357  49.231  1.00  4.47           C  
-ATOM    641  CE2 PHE A  89      72.144  25.005  49.469  1.00  4.47           C  
-ATOM    642  CZ  PHE A  89      71.934  26.155  48.756  1.00  4.47           C  
-ATOM    643  N   GLN A  90      74.649  26.936  55.337  1.00  4.47           N  
-ATOM    644  CA  GLN A  90      75.459  26.810  56.531  1.00  5.72           C  
-ATOM    645  C   GLN A  90      74.762  25.953  57.595  1.00 10.33           C  
-ATOM    646  O   GLN A  90      75.371  25.065  58.181  1.00 11.49           O  
-ATOM    647  CB  GLN A  90      75.762  28.192  57.097  1.00  6.28           C  
-ATOM    648  CG  GLN A  90      76.400  28.188  58.478  1.00  7.27           C  
-ATOM    649  CD  GLN A  90      77.533  27.191  58.604  1.00 15.03           C  
-ATOM    650  OE1 GLN A  90      78.283  26.953  57.656  1.00 14.41           O  
-ATOM    651  NE2 GLN A  90      77.670  26.610  59.786  1.00 15.31           N  
-ATOM    652  N   SER A  91      73.479  26.219  57.825  1.00 12.56           N  
-ATOM    653  CA  SER A  91      72.695  25.491  58.821  1.00  5.96           C  
-ATOM    654  C   SER A  91      72.650  23.995  58.570  1.00  8.31           C  
-ATOM    655  O   SER A  91      72.542  23.222  59.514  1.00 12.85           O  
-ATOM    656  CB  SER A  91      71.254  26.002  58.851  1.00  7.17           C  
-ATOM    657  OG  SER A  91      70.448  25.298  57.912  1.00 29.25           O  
-ATOM    658  N   LEU A  92      72.711  23.585  57.304  1.00  8.43           N  
-ATOM    659  CA  LEU A  92      72.647  22.165  56.967  1.00  8.00           C  
-ATOM    660  C   LEU A  92      73.661  21.307  57.701  1.00  4.47           C  
-ATOM    661  O   LEU A  92      73.355  20.186  58.095  1.00  4.47           O  
-ATOM    662  CB  LEU A  92      72.799  21.961  55.462  1.00  6.62           C  
-ATOM    663  CG  LEU A  92      71.607  22.396  54.601  1.00  4.47           C  
-ATOM    664  CD1 LEU A  92      71.905  22.076  53.137  1.00  5.62           C  
-ATOM    665  CD2 LEU A  92      70.351  21.683  55.041  1.00  4.47           C  
-ATOM    666  N   PHE A  93      74.859  21.840  57.883  1.00  4.47           N  
-ATOM    667  CA  PHE A  93      75.922  21.132  58.585  1.00  7.08           C  
-ATOM    668  C   PHE A  93      75.586  20.727  60.021  1.00 10.32           C  
-ATOM    669  O   PHE A  93      76.181  19.789  60.546  1.00 19.14           O  
-ATOM    670  CB  PHE A  93      77.172  21.996  58.613  1.00 11.38           C  
-ATOM    671  CG  PHE A  93      77.795  22.201  57.273  1.00 18.20           C  
-ATOM    672  CD1 PHE A  93      78.637  21.237  56.742  1.00 23.74           C  
-ATOM    673  CD2 PHE A  93      77.554  23.359  56.541  1.00 12.66           C  
-ATOM    674  CE1 PHE A  93      79.240  21.420  55.498  1.00 18.81           C  
-ATOM    675  CE2 PHE A  93      78.152  23.547  55.297  1.00 16.75           C  
-ATOM    676  CZ  PHE A  93      78.998  22.574  54.776  1.00 11.01           C  
-ATOM    677  N   CYS A  94      74.641  21.424  60.650  1.00  7.25           N  
-ATOM    678  CA  CYS A  94      74.243  21.161  62.046  1.00 11.80           C  
-ATOM    679  C   CYS A  94      73.699  19.779  62.449  1.00 14.20           C  
-ATOM    680  O   CYS A  94      74.312  19.067  63.248  1.00 17.30           O  
-ATOM    681  CB  CYS A  94      73.238  22.226  62.497  1.00 11.09           C  
-ATOM    682  SG  CYS A  94      73.941  23.909  62.562  1.00 22.35           S  
-ATOM    683  N   SER A  95      72.544  19.407  61.914  1.00 19.24           N  
-ATOM    684  CA  SER A  95      71.913  18.130  62.243  1.00 12.19           C  
-ATOM    685  C   SER A  95      72.794  16.906  62.427  1.00  4.88           C  
-ATOM    686  O   SER A  95      72.857  16.365  63.516  1.00 10.37           O  
-ATOM    687  CB  SER A  95      70.812  17.807  61.231  1.00 12.35           C  
-ATOM    688  OG  SER A  95      71.179  18.222  59.925  1.00 38.19           O  
-ATOM    689  N   PRO A  96      73.502  16.459  61.383  1.00  4.47           N  
-ATOM    690  CA  PRO A  96      74.351  15.267  61.535  1.00  5.62           C  
-ATOM    691  C   PRO A  96      75.142  15.265  62.828  1.00  9.50           C  
-ATOM    692  O   PRO A  96      74.921  14.439  63.707  1.00 11.41           O  
-ATOM    693  CB  PRO A  96      75.272  15.328  60.328  1.00  4.47           C  
-ATOM    694  CG  PRO A  96      74.486  16.117  59.341  1.00 17.71           C  
-ATOM    695  CD  PRO A  96      73.880  17.202  60.177  1.00  7.05           C  
-ATOM    696  N   HIS A  97      76.073  16.200  62.935  1.00 11.00           N  
-ATOM    697  CA  HIS A  97      76.904  16.311  64.116  1.00  8.40           C  
-ATOM    698  C   HIS A  97      76.119  16.377  65.413  1.00  9.80           C  
-ATOM    699  O   HIS A  97      76.589  15.912  66.446  1.00 14.20           O  
-ATOM    700  CB  HIS A  97      77.784  17.541  64.003  1.00 12.17           C  
-ATOM    701  CG  HIS A  97      79.213  17.215  63.751  1.00 16.99           C  
-ATOM    702  ND1 HIS A  97      79.946  16.422  64.606  1.00 23.82           N  
-ATOM    703  CD2 HIS A  97      80.041  17.553  62.738  1.00  4.52           C  
-ATOM    704  CE1 HIS A  97      81.170  16.287  64.128  1.00 32.34           C  
-ATOM    705  NE2 HIS A  97      81.254  16.965  62.995  1.00 22.92           N  
-ATOM    706  N   ALA A  98      74.926  16.957  65.356  1.00  8.72           N  
-ATOM    707  CA  ALA A  98      74.089  17.099  66.538  1.00  4.47           C  
-ATOM    708  C   ALA A  98      73.375  15.814  66.932  1.00  4.47           C  
-ATOM    709  O   ALA A  98      73.332  15.481  68.106  1.00  4.47           O  
-ATOM    710  CB  ALA A  98      73.085  18.208  66.319  1.00  7.09           C  
-ATOM    711  N   ILE A  99      72.809  15.099  65.959  1.00 10.81           N  
-ATOM    712  CA  ILE A  99      72.097  13.843  66.235  1.00  8.66           C  
-ATOM    713  C   ILE A  99      73.042  12.953  67.016  1.00 10.25           C  
-ATOM    714  O   ILE A  99      72.670  12.354  68.023  1.00 11.48           O  
-ATOM    715  CB  ILE A  99      71.717  13.073  64.939  1.00  4.47           C  
-ATOM    716  CG1 ILE A  99      70.781  13.899  64.061  1.00  4.47           C  
-ATOM    717  CG2 ILE A  99      71.045  11.769  65.306  1.00  4.96           C  
-ATOM    718  CD1 ILE A  99      69.450  14.189  64.703  1.00  6.74           C  
-ATOM    719  N   MET A 100      74.272  12.885  66.514  1.00 12.17           N  
-ATOM    720  CA  MET A 100      75.354  12.095  67.083  1.00 10.86           C  
-ATOM    721  C   MET A 100      75.660  12.547  68.495  1.00 12.58           C  
-ATOM    722  O   MET A 100      75.379  11.846  69.453  1.00 15.64           O  
-ATOM    723  CB  MET A 100      76.602  12.268  66.223  1.00 26.47           C  
-ATOM    724  CG  MET A 100      77.804  11.460  66.659  1.00 38.28           C  
-ATOM    725  SD  MET A 100      77.827   9.807  65.964  1.00 45.50           S  
-ATOM    726  CE  MET A 100      77.471   8.860  67.370  1.00 47.83           C  
-ATOM    727  N   HIS A 101      76.246  13.729  68.618  1.00 17.23           N  
-ATOM    728  CA  HIS A 101      76.593  14.275  69.924  1.00 22.99           C  
-ATOM    729  C   HIS A 101      75.483  14.080  70.957  1.00 18.73           C  
-ATOM    730  O   HIS A 101      75.754  13.701  72.094  1.00 22.60           O  
-ATOM    731  CB  HIS A 101      76.909  15.768  69.807  1.00 30.17           C  
-ATOM    732  CG  HIS A 101      77.119  16.447  71.125  1.00 37.41           C  
-ATOM    733  ND1 HIS A 101      78.358  16.560  71.719  1.00 36.36           N  
-ATOM    734  CD2 HIS A 101      76.239  17.028  71.976  1.00 41.05           C  
-ATOM    735  CE1 HIS A 101      78.233  17.183  72.877  1.00 41.10           C  
-ATOM    736  NE2 HIS A 101      76.958  17.477  73.057  1.00 44.84           N  
-ATOM    737  N   ALA A 102      74.242  14.341  70.559  1.00 13.10           N  
-ATOM    738  CA  ALA A 102      73.109  14.218  71.463  1.00  7.64           C  
-ATOM    739  C   ALA A 102      72.903  12.797  71.936  1.00  4.47           C  
-ATOM    740  O   ALA A 102      72.496  12.576  73.072  1.00  4.47           O  
-ATOM    741  CB  ALA A 102      71.860  14.731  70.799  1.00 21.72           C  
-ATOM    742  N   LYS A 103      73.169  11.834  71.059  1.00 13.01           N  
-ATOM    743  CA  LYS A 103      73.038  10.413  71.404  1.00 16.75           C  
-ATOM    744  C   LYS A 103      74.127  10.066  72.420  1.00 13.11           C  
-ATOM    745  O   LYS A 103      73.858   9.510  73.483  1.00  4.92           O  
-ATOM    746  CB  LYS A 103      73.211   9.539  70.151  1.00 13.55           C  
-ATOM    747  CG  LYS A 103      73.600   8.099  70.448  1.00 20.47           C  
-ATOM    748  CD  LYS A 103      72.448   7.302  71.031  1.00 30.63           C  
-ATOM    749  CE  LYS A 103      71.429   6.970  69.955  1.00 36.99           C  
-ATOM    750  NZ  LYS A 103      70.306   6.166  70.502  1.00 48.80           N  
-ATOM    751  N   ILE A 104      75.361  10.403  72.066  1.00 14.75           N  
-ATOM    752  CA  ILE A 104      76.514  10.159  72.916  1.00 14.84           C  
-ATOM    753  C   ILE A 104      76.335  10.742  74.324  1.00 19.07           C  
-ATOM    754  O   ILE A 104      76.701  10.123  75.308  1.00 15.09           O  
-ATOM    755  CB  ILE A 104      77.776  10.746  72.263  1.00 13.89           C  
-ATOM    756  CG1 ILE A 104      78.255   9.801  71.164  1.00 18.87           C  
-ATOM    757  CG2 ILE A 104      78.845  11.001  73.306  1.00  7.75           C  
-ATOM    758  CD1 ILE A 104      79.303  10.388  70.241  1.00 22.50           C  
-ATOM    759  N   SER A 105      75.773  11.935  74.432  1.00 23.19           N  
-ATOM    760  CA  SER A 105      75.581  12.508  75.749  1.00 21.03           C  
-ATOM    761  C   SER A 105      74.669  11.618  76.564  1.00 19.95           C  
-ATOM    762  O   SER A 105      74.751  11.598  77.783  1.00 26.12           O  
-ATOM    763  CB  SER A 105      74.980  13.903  75.642  1.00 30.86           C  
-ATOM    764  OG  SER A 105      75.865  14.773  74.952  1.00 40.10           O  
-ATOM    765  N   ALA A 106      73.806  10.871  75.886  1.00 21.07           N  
-ATOM    766  CA  ALA A 106      72.870   9.984  76.565  1.00 21.22           C  
-ATOM    767  C   ALA A 106      73.549   8.734  77.098  1.00 18.32           C  
-ATOM    768  O   ALA A 106      73.127   8.178  78.107  1.00 18.53           O  
-ATOM    769  CB  ALA A 106      71.733   9.598  75.625  1.00 29.45           C  
-ATOM    770  N   LEU A 107      74.598   8.288  76.421  1.00 19.65           N  
-ATOM    771  CA  LEU A 107      75.313   7.100  76.863  1.00 23.11           C  
-ATOM    772  C   LEU A 107      76.401   7.476  77.846  1.00 25.76           C  
-ATOM    773  O   LEU A 107      77.240   6.653  78.183  1.00 29.11           O  
-ATOM    774  CB  LEU A 107      75.960   6.376  75.686  1.00 20.02           C  
-ATOM    775  CG  LEU A 107      75.095   6.095  74.469  1.00 35.41           C  
-ATOM    776  CD1 LEU A 107      75.896   5.266  73.472  1.00 35.66           C  
-ATOM    777  CD2 LEU A 107      73.829   5.373  74.896  1.00 40.82           C  
-ATOM    778  N   MET A 108      76.404   8.721  78.302  1.00 35.13           N  
-ATOM    779  CA  MET A 108      77.429   9.148  79.246  1.00 47.14           C  
-ATOM    780  C   MET A 108      76.912   9.078  80.679  1.00 60.07           C  
-ATOM    781  O   MET A 108      75.872   9.663  81.004  1.00 69.82           O  
-ATOM    782  CB  MET A 108      77.891  10.571  78.933  1.00 48.15           C  
-ATOM    783  CG  MET A 108      79.391  10.776  79.109  1.00 42.65           C  
-ATOM    784  SD  MET A 108      80.380  10.342  77.639  1.00 35.49           S  
-ATOM    785  CE  MET A 108      80.200   8.613  77.558  1.00 30.16           C  
-ATOM    786  N   ASP A 109      77.648   8.364  81.529  1.00 64.66           N  
-ATOM    787  CA  ASP A 109      77.279   8.192  82.932  1.00 70.11           C  
-ATOM    788  C   ASP A 109      77.561   9.441  83.760  1.00 69.50           C  
-ATOM    789  O   ASP A 109      78.715   9.815  83.962  1.00 63.14           O  
-ATOM    790  CB  ASP A 109      78.033   7.000  83.525  1.00 75.61           C  
-ATOM    791  CG  ASP A 109      77.617   6.695  84.950  1.00 78.60           C  
-ATOM    792  OD1 ASP A 109      76.425   6.403  85.186  1.00 81.76           O  
-ATOM    793  OD2 ASP A 109      78.487   6.746  85.837  1.00 79.82           O  
-ATOM    794  N   THR A 110      76.493  10.078  84.231  1.00 74.57           N  
-ATOM    795  CA  THR A 110      76.601  11.287  85.037  1.00 82.82           C  
-ATOM    796  C   THR A 110      76.317  10.916  86.487  1.00 86.57           C  
-ATOM    797  O   THR A 110      75.404  11.454  87.123  1.00 90.86           O  
-ATOM    798  CB  THR A 110      75.591  12.361  84.565  1.00 87.85           C  
-ATOM    799  OG1 THR A 110      75.718  12.542  83.149  1.00 90.10           O  
-ATOM    800  CG2 THR A 110      75.859  13.697  85.252  1.00 91.26           C  
-ATOM    801  N   SER A 111      77.129   9.990  86.996  1.00 85.13           N  
-ATOM    802  CA  SER A 111      77.002   9.485  88.358  1.00 81.78           C  
-ATOM    803  C   SER A 111      77.765  10.315  89.372  1.00 78.50           C  
-ATOM    804  O   SER A 111      78.981  10.474  89.284  1.00 79.30           O  
-ATOM    805  CB  SER A 111      77.486   8.030  88.430  1.00 86.12           C  
-ATOM    806  OG  SER A 111      77.313   7.481  89.726  1.00 86.80           O  
-ATOM    807  N   THR A 112      77.027  10.842  90.338  1.00 77.60           N  
-ATOM    808  CA  THR A 112      77.595  11.648  91.407  1.00 71.62           C  
-ATOM    809  C   THR A 112      77.822  10.679  92.562  1.00 69.71           C  
-ATOM    810  O   THR A 112      76.969  10.554  93.442  1.00 75.88           O  
-ATOM    811  CB  THR A 112      76.597  12.757  91.852  1.00 68.99           C  
-ATOM    812  OG1 THR A 112      75.416  12.159  92.414  1.00 66.09           O  
-ATOM    813  CG2 THR A 112      76.180  13.607  90.657  1.00 69.43           C  
-ATOM    814  N   SER A 113      78.951   9.975  92.560  1.00 63.45           N  
-ATOM    815  CA  SER A 113      79.206   9.017  93.633  1.00 65.94           C  
-ATOM    816  C   SER A 113      80.629   8.481  93.706  1.00 68.22           C  
-ATOM    817  O   SER A 113      81.459   8.748  92.829  1.00 66.96           O  
-ATOM    818  CB  SER A 113      78.236   7.829  93.527  1.00 65.32           C  
-ATOM    819  OG  SER A 113      77.296   7.825  94.592  1.00 64.24           O  
-ATOM    820  N   ASP A 114      80.886   7.718  94.772  1.00 68.52           N  
-ATOM    821  CA  ASP A 114      82.184   7.099  95.027  1.00 66.43           C  
-ATOM    822  C   ASP A 114      82.307   5.795  94.239  1.00 59.98           C  
-ATOM    823  O   ASP A 114      81.306   5.219  93.805  1.00 61.66           O  
-ATOM    824  CB  ASP A 114      82.356   6.804  96.526  1.00 76.05           C  
-ATOM    825  CG  ASP A 114      82.350   8.065  97.389  1.00 87.07           C  
-ATOM    826  OD1 ASP A 114      83.196   8.961  97.165  1.00 94.40           O  
-ATOM    827  OD2 ASP A 114      81.502   8.157  98.303  1.00 88.84           O  
-ATOM    828  N   LEU A 115      83.541   5.334  94.066  1.00 49.54           N  
-ATOM    829  CA  LEU A 115      83.814   4.108  93.329  1.00 40.37           C  
-ATOM    830  C   LEU A 115      83.900   2.870  94.201  1.00 48.36           C  
-ATOM    831  O   LEU A 115      84.647   2.833  95.180  1.00 52.08           O  
-ATOM    832  CB  LEU A 115      85.117   4.253  92.577  1.00 28.95           C  
-ATOM    833  CG  LEU A 115      84.979   5.030  91.292  1.00 23.60           C  
-ATOM    834  CD1 LEU A 115      86.328   5.521  90.861  1.00 16.18           C  
-ATOM    835  CD2 LEU A 115      84.332   4.129  90.250  1.00 33.98           C  
-ATOM    836  N   VAL A 116      83.151   1.841  93.833  1.00 51.88           N  
-ATOM    837  CA  VAL A 116      83.178   0.618  94.605  1.00 55.55           C  
-ATOM    838  C   VAL A 116      84.372  -0.219  94.145  1.00 59.56           C  
-ATOM    839  O   VAL A 116      84.969  -0.942  94.950  1.00 65.98           O  
-ATOM    840  CB  VAL A 116      81.862  -0.179  94.439  1.00 57.86           C  
-ATOM    841  CG1 VAL A 116      81.722  -1.197  95.567  1.00 64.76           C  
-ATOM    842  CG2 VAL A 116      80.670   0.770  94.447  1.00 56.99           C  
-ATOM    843  N   GLN A 117      84.732  -0.094  92.863  1.00 57.73           N  
-ATOM    844  CA  GLN A 117      85.862  -0.837  92.272  1.00 58.77           C  
-ATOM    845  C   GLN A 117      86.558  -0.063  91.154  1.00 53.62           C  
-ATOM    846  O   GLN A 117      85.980   0.869  90.597  1.00 61.72           O  
-ATOM    847  CB  GLN A 117      85.376  -2.174  91.703  1.00 66.74           C  
-ATOM    848  CG  GLN A 117      84.951  -3.191  92.758  1.00 75.23           C  
-ATOM    849  CD  GLN A 117      86.117  -4.001  93.309  1.00 70.13           C  
-ATOM    850  OE1 GLN A 117      87.274  -3.564  93.271  1.00 63.77           O  
-ATOM    851  NE2 GLN A 117      85.812  -5.185  93.837  1.00 69.30           N  
-ATOM    852  N   VAL A 118      87.793  -0.443  90.825  1.00 45.25           N  
-ATOM    853  CA  VAL A 118      88.524   0.233  89.746  1.00 46.19           C  
-ATOM    854  C   VAL A 118      88.686  -0.701  88.580  1.00 45.82           C  
-ATOM    855  O   VAL A 118      88.544  -1.911  88.730  1.00 44.65           O  
-ATOM    856  CB  VAL A 118      89.955   0.630  90.126  1.00 39.90           C  
-ATOM    857  CG1 VAL A 118      89.938   1.674  91.188  1.00 38.80           C  
-ATOM    858  CG2 VAL A 118      90.730  -0.606  90.565  1.00 40.91           C  
-ATOM    859  N   ASN A 119      88.994  -0.141  87.418  1.00 48.71           N  
-ATOM    860  CA  ASN A 119      89.223  -0.980  86.257  1.00 55.13           C  
-ATOM    861  C   ASN A 119      90.710  -0.992  85.967  1.00 54.51           C  
-ATOM    862  O   ASN A 119      91.343   0.060  85.877  1.00 54.14           O  
-ATOM    863  CB  ASN A 119      88.500  -0.469  85.018  1.00 61.33           C  
-ATOM    864  CG  ASN A 119      88.895  -1.246  83.772  1.00 61.92           C  
-ATOM    865  OD1 ASN A 119      88.684  -0.792  82.647  1.00 68.79           O  
-ATOM    866  ND2 ASN A 119      89.474  -2.430  83.973  1.00 56.06           N  
-ATOM    867  N   LYS A 120      91.254  -2.190  85.810  1.00 55.40           N  
-ATOM    868  CA  LYS A 120      92.668  -2.374  85.534  1.00 60.02           C  
-ATOM    869  C   LYS A 120      93.172  -1.620  84.300  1.00 69.38           C  
-ATOM    870  O   LYS A 120      94.181  -0.915  84.369  1.00 70.76           O  
-ATOM    871  CB  LYS A 120      92.951  -3.862  85.363  1.00 57.25           C  
-ATOM    872  CG  LYS A 120      94.400  -4.202  85.039  1.00 52.93           C  
-ATOM    873  CD  LYS A 120      94.532  -5.605  84.433  1.00 47.07           C  
-ATOM    874  CE  LYS A 120      93.876  -6.691  85.295  1.00 44.43           C  
-ATOM    875  NZ  LYS A 120      92.380  -6.632  85.308  1.00 41.64           N  
-ATOM    876  N   GLU A 121      92.465  -1.770  83.180  1.00 76.50           N  
-ATOM    877  CA  GLU A 121      92.850  -1.148  81.906  1.00 81.08           C  
-ATOM    878  C   GLU A 121      92.917   0.390  81.815  1.00 78.72           C  
-ATOM    879  O   GLU A 121      92.299   1.109  82.607  1.00 82.09           O  
-ATOM    880  CB  GLU A 121      91.945  -1.679  80.777  1.00 87.98           C  
-ATOM    881  CG  GLU A 121      92.172  -3.156  80.410  1.00 96.25           C  
-ATOM    882  CD  GLU A 121      91.570  -3.549  79.055  1.00 98.06           C  
-ATOM    883  OE1 GLU A 121      90.329  -3.485  78.888  1.00 92.29           O  
-ATOM    884  OE2 GLU A 121      92.350  -3.925  78.152  1.00 97.53           O  
-ATOM    885  N   PRO A 122      93.690   0.905  80.836  1.00 72.25           N  
-ATOM    886  CA  PRO A 122      93.889   2.332  80.570  1.00 68.11           C  
-ATOM    887  C   PRO A 122      92.599   2.968  80.070  1.00 64.40           C  
-ATOM    888  O   PRO A 122      91.686   2.259  79.658  1.00 61.71           O  
-ATOM    889  CB  PRO A 122      94.982   2.328  79.508  1.00 70.56           C  
-ATOM    890  CG  PRO A 122      94.717   1.067  78.769  1.00 72.00           C  
-ATOM    891  CD  PRO A 122      94.492   0.101  79.897  1.00 71.89           C  
-ATOM    892  N   TYR A 123      92.514   4.296  80.078  1.00 65.13           N  
-ATOM    893  CA  TYR A 123      91.264   4.897  79.645  1.00 58.65           C  
-ATOM    894  C   TYR A 123      91.058   4.885  78.147  1.00 54.37           C  
-ATOM    895  O   TYR A 123      91.941   5.248  77.380  1.00 54.94           O  
-ATOM    896  CB  TYR A 123      91.106   6.328  80.183  1.00 54.58           C  
-ATOM    897  CG  TYR A 123      92.363   7.155  80.162  1.00 46.89           C  
-ATOM    898  CD1 TYR A 123      93.175   7.196  79.030  1.00 42.00           C  
-ATOM    899  CD2 TYR A 123      92.752   7.883  81.285  1.00 55.68           C  
-ATOM    900  CE1 TYR A 123      94.345   7.929  79.007  1.00 43.52           C  
-ATOM    901  CE2 TYR A 123      93.928   8.631  81.280  1.00 65.15           C  
-ATOM    902  CZ  TYR A 123      94.724   8.645  80.133  1.00 61.60           C  
-ATOM    903  OH  TYR A 123      95.908   9.356  80.117  1.00 61.46           O  
-ATOM    904  N   LYS A 124      89.870   4.456  77.739  1.00 50.56           N  
-ATOM    905  CA  LYS A 124      89.518   4.398  76.332  1.00 44.25           C  
-ATOM    906  C   LYS A 124      89.233   5.796  75.791  1.00 36.81           C  
-ATOM    907  O   LYS A 124      88.369   6.516  76.293  1.00 37.76           O  
-ATOM    908  CB  LYS A 124      88.310   3.478  76.139  1.00 42.97           C  
-ATOM    909  CG  LYS A 124      88.633   2.007  76.388  1.00 48.03           C  
-ATOM    910  CD  LYS A 124      87.385   1.141  76.456  1.00 55.10           C  
-ATOM    911  CE  LYS A 124      87.730  -0.337  76.669  1.00 58.22           C  
-ATOM    912  NZ  LYS A 124      88.492  -0.610  77.919  1.00 60.31           N  
-ATOM    913  N   ILE A 125      89.990   6.170  74.768  1.00 26.93           N  
-ATOM    914  CA  ILE A 125      89.860   7.467  74.137  1.00 24.73           C  
-ATOM    915  C   ILE A 125      89.032   7.401  72.864  1.00 16.51           C  
-ATOM    916  O   ILE A 125      89.369   6.654  71.954  1.00 10.64           O  
-ATOM    917  CB  ILE A 125      91.261   8.055  73.785  1.00 28.05           C  
-ATOM    918  CG1 ILE A 125      91.212   8.745  72.422  1.00 36.99           C  
-ATOM    919  CG2 ILE A 125      92.309   6.972  73.748  1.00 26.35           C  
-ATOM    920  CD1 ILE A 125      92.571   9.161  71.892  1.00 54.82           C  
-ATOM    921  N   MET A 126      87.953   8.181  72.803  1.00 13.17           N  
-ATOM    922  CA  MET A 126      87.119   8.231  71.606  1.00 16.24           C  
-ATOM    923  C   MET A 126      87.312   9.588  70.918  1.00 16.19           C  
-ATOM    924  O   MET A 126      86.802  10.613  71.348  1.00 11.87           O  
-ATOM    925  CB  MET A 126      85.642   7.982  71.937  1.00 22.07           C  
-ATOM    926  CG  MET A 126      84.961   9.056  72.712  1.00 28.53           C  
-ATOM    927  SD  MET A 126      83.660   9.801  71.770  1.00 43.14           S  
-ATOM    928  CE  MET A 126      82.198   9.108  72.599  1.00 36.23           C  
-ATOM    929  N   LEU A 127      88.083   9.563  69.839  1.00 20.77           N  
-ATOM    930  CA  LEU A 127      88.429  10.738  69.060  1.00 17.25           C  
-ATOM    931  C   LEU A 127      87.330  11.100  68.077  1.00 19.35           C  
-ATOM    932  O   LEU A 127      86.773  10.226  67.435  1.00 25.99           O  
-ATOM    933  CB  LEU A 127      89.720  10.440  68.304  1.00 10.07           C  
-ATOM    934  CG  LEU A 127      90.526  11.596  67.733  1.00 19.77           C  
-ATOM    935  CD1 LEU A 127      90.925  12.591  68.825  1.00 14.42           C  
-ATOM    936  CD2 LEU A 127      91.751  11.008  67.086  1.00 21.29           C  
-ATOM    937  N   SER A 128      87.022  12.387  67.955  1.00 20.45           N  
-ATOM    938  CA  SER A 128      85.991  12.840  67.024  1.00 21.84           C  
-ATOM    939  C   SER A 128      86.491  13.972  66.140  1.00 23.42           C  
-ATOM    940  O   SER A 128      87.287  14.796  66.574  1.00 35.44           O  
-ATOM    941  CB  SER A 128      84.750  13.309  67.780  1.00 30.00           C  
-ATOM    942  OG  SER A 128      83.891  14.044  66.921  1.00 36.99           O  
-ATOM    943  N   ASP A 129      86.012  14.013  64.902  1.00 21.62           N  
-ATOM    944  CA  ASP A 129      86.415  15.036  63.946  1.00 17.58           C  
-ATOM    945  C   ASP A 129      85.438  16.205  64.000  1.00 20.35           C  
-ATOM    946  O   ASP A 129      84.316  16.122  63.490  1.00 10.88           O  
-ATOM    947  CB  ASP A 129      86.452  14.450  62.536  1.00 16.34           C  
-ATOM    948  CG  ASP A 129      87.154  15.345  61.555  1.00 28.24           C  
-ATOM    949  OD1 ASP A 129      87.256  14.955  60.374  1.00 39.74           O  
-ATOM    950  OD2 ASP A 129      87.606  16.435  61.962  1.00 36.16           O  
-ATOM    951  N   ARG A 130      85.889  17.291  64.625  1.00 22.56           N  
-ATOM    952  CA  ARG A 130      85.109  18.513  64.792  1.00 14.60           C  
-ATOM    953  C   ARG A 130      84.016  18.360  65.840  1.00 14.82           C  
-ATOM    954  O   ARG A 130      83.456  17.273  66.025  1.00 13.24           O  
-ATOM    955  CB  ARG A 130      84.501  18.958  63.457  1.00 13.16           C  
-ATOM    956  CG  ARG A 130      85.475  19.681  62.538  1.00 14.65           C  
-ATOM    957  CD  ARG A 130      84.747  20.524  61.479  1.00 12.81           C  
-ATOM    958  NE  ARG A 130      85.494  21.746  61.157  1.00 22.92           N  
-ATOM    959  CZ  ARG A 130      86.626  21.779  60.459  1.00 19.91           C  
-ATOM    960  NH1 ARG A 130      87.156  20.658  59.994  1.00 28.89           N  
-ATOM    961  NH2 ARG A 130      87.236  22.930  60.240  1.00 11.64           N  
-ATOM    962  N   HIS A 131      83.730  19.458  66.531  1.00  4.47           N  
-ATOM    963  CA  HIS A 131      82.712  19.470  67.566  1.00  4.47           C  
-ATOM    964  C   HIS A 131      81.570  20.324  67.070  1.00  4.47           C  
-ATOM    965  O   HIS A 131      81.796  21.299  66.380  1.00 12.33           O  
-ATOM    966  CB  HIS A 131      83.280  20.071  68.842  1.00  4.47           C  
-ATOM    967  CG  HIS A 131      82.310  20.098  69.975  1.00  5.45           C  
-ATOM    968  ND1 HIS A 131      81.190  20.897  69.974  1.00  5.77           N  
-ATOM    969  CD2 HIS A 131      82.268  19.390  71.128  1.00 18.58           C  
-ATOM    970  CE1 HIS A 131      80.497  20.681  71.078  1.00 16.35           C  
-ATOM    971  NE2 HIS A 131      81.129  19.770  71.795  1.00 20.75           N  
-ATOM    972  N   PRO A 132      80.327  19.974  67.418  1.00  4.47           N  
-ATOM    973  CA  PRO A 132      79.118  20.698  67.015  1.00  8.00           C  
-ATOM    974  C   PRO A 132      79.213  22.219  66.970  1.00  7.53           C  
-ATOM    975  O   PRO A 132      78.610  22.858  66.113  1.00 17.10           O  
-ATOM    976  CB  PRO A 132      78.095  20.219  68.026  1.00  7.43           C  
-ATOM    977  CG  PRO A 132      78.460  18.793  68.154  1.00  4.47           C  
-ATOM    978  CD  PRO A 132      79.969  18.841  68.281  1.00  4.47           C  
-ATOM    979  N   ILE A 133      79.968  22.805  67.885  1.00  4.47           N  
-ATOM    980  CA  ILE A 133      80.093  24.245  67.896  1.00  4.47           C  
-ATOM    981  C   ILE A 133      80.681  24.773  66.585  1.00  4.47           C  
-ATOM    982  O   ILE A 133      80.507  25.934  66.225  1.00  4.47           O  
-ATOM    983  CB  ILE A 133      80.934  24.712  69.103  1.00  7.74           C  
-ATOM    984  CG1 ILE A 133      82.406  24.372  68.900  1.00 11.47           C  
-ATOM    985  CG2 ILE A 133      80.431  24.035  70.372  1.00  4.47           C  
-ATOM    986  CD1 ILE A 133      83.290  24.897  70.024  1.00  8.55           C  
-ATOM    987  N   ALA A 134      81.368  23.918  65.851  1.00  4.47           N  
-ATOM    988  CA  ALA A 134      81.937  24.350  64.583  1.00  5.40           C  
-ATOM    989  C   ALA A 134      80.823  24.756  63.623  1.00  5.48           C  
-ATOM    990  O   ALA A 134      80.943  25.738  62.913  1.00 12.34           O  
-ATOM    991  CB  ALA A 134      82.766  23.243  63.967  1.00  9.82           C  
-ATOM    992  N   SER A 135      79.737  23.998  63.603  1.00  4.47           N  
-ATOM    993  CA  SER A 135      78.623  24.312  62.723  1.00  4.47           C  
-ATOM    994  C   SER A 135      77.702  25.350  63.324  1.00  8.84           C  
-ATOM    995  O   SER A 135      77.198  26.221  62.618  1.00 16.82           O  
-ATOM    996  CB  SER A 135      77.795  23.066  62.439  1.00  5.54           C  
-ATOM    997  OG  SER A 135      77.163  22.601  63.611  1.00  7.44           O  
-ATOM    998  N   THR A 136      77.479  25.257  64.631  1.00  7.87           N  
-ATOM    999  CA  THR A 136      76.577  26.182  65.311  1.00 12.07           C  
-ATOM   1000  C   THR A 136      77.194  27.472  65.813  1.00  8.17           C  
-ATOM   1001  O   THR A 136      76.469  28.352  66.274  1.00  4.89           O  
-ATOM   1002  CB  THR A 136      75.925  25.525  66.504  1.00 13.35           C  
-ATOM   1003  OG1 THR A 136      76.926  25.269  67.492  1.00 17.91           O  
-ATOM   1004  CG2 THR A 136      75.284  24.205  66.091  1.00 32.64           C  
-ATOM   1005  N   ILE A 137      78.515  27.597  65.756  1.00  4.75           N  
-ATOM   1006  CA  ILE A 137      79.105  28.825  66.236  1.00  6.98           C  
-ATOM   1007  C   ILE A 137      80.354  29.296  65.532  1.00  5.02           C  
-ATOM   1008  O   ILE A 137      80.433  30.465  65.189  1.00 19.63           O  
-ATOM   1009  CB  ILE A 137      79.327  28.803  67.800  1.00 10.76           C  
-ATOM   1010  CG1 ILE A 137      80.757  29.146  68.161  1.00  4.47           C  
-ATOM   1011  CG2 ILE A 137      78.985  27.458  68.390  1.00 17.16           C  
-ATOM   1012  CD1 ILE A 137      80.936  29.204  69.668  1.00 24.95           C  
-ATOM   1013  N   CYS A 138      81.325  28.433  65.282  1.00  4.47           N  
-ATOM   1014  CA  CYS A 138      82.513  28.935  64.612  1.00  4.47           C  
-ATOM   1015  C   CYS A 138      82.295  29.376  63.177  1.00  4.47           C  
-ATOM   1016  O   CYS A 138      82.543  30.528  62.854  1.00 10.60           O  
-ATOM   1017  CB  CYS A 138      83.633  27.925  64.697  1.00  4.47           C  
-ATOM   1018  SG  CYS A 138      84.201  27.798  66.392  1.00 21.48           S  
-ATOM   1019  N   PHE A 139      81.823  28.491  62.309  1.00  4.47           N  
-ATOM   1020  CA  PHE A 139      81.592  28.882  60.916  1.00  4.47           C  
-ATOM   1021  C   PHE A 139      80.523  29.946  60.756  1.00  4.63           C  
-ATOM   1022  O   PHE A 139      80.801  30.999  60.198  1.00 13.04           O  
-ATOM   1023  CB  PHE A 139      81.239  27.681  60.048  1.00  5.62           C  
-ATOM   1024  CG  PHE A 139      82.435  26.873  59.607  1.00 12.94           C  
-ATOM   1025  CD1 PHE A 139      83.144  26.081  60.503  1.00 13.25           C  
-ATOM   1026  CD2 PHE A 139      82.854  26.910  58.292  1.00 18.26           C  
-ATOM   1027  CE1 PHE A 139      84.246  25.348  60.087  1.00  4.47           C  
-ATOM   1028  CE2 PHE A 139      83.961  26.175  57.872  1.00 13.26           C  
-ATOM   1029  CZ  PHE A 139      84.652  25.398  58.771  1.00  4.47           C  
-ATOM   1030  N   PRO A 140      79.289  29.699  61.231  1.00  4.47           N  
-ATOM   1031  CA  PRO A 140      78.278  30.751  61.067  1.00  6.01           C  
-ATOM   1032  C   PRO A 140      78.793  32.147  61.462  1.00  7.12           C  
-ATOM   1033  O   PRO A 140      78.507  33.148  60.800  1.00  9.19           O  
-ATOM   1034  CB  PRO A 140      77.117  30.267  61.947  1.00  4.47           C  
-ATOM   1035  CG  PRO A 140      77.772  29.339  62.927  1.00  4.47           C  
-ATOM   1036  CD  PRO A 140      78.773  28.615  62.077  1.00  6.12           C  
-ATOM   1037  N   LEU A 141      79.577  32.209  62.527  1.00  4.47           N  
-ATOM   1038  CA  LEU A 141      80.114  33.482  62.970  1.00  4.47           C  
-ATOM   1039  C   LEU A 141      81.170  34.015  62.002  1.00  4.47           C  
-ATOM   1040  O   LEU A 141      81.292  35.224  61.812  1.00 10.09           O  
-ATOM   1041  CB  LEU A 141      80.704  33.335  64.377  1.00  4.67           C  
-ATOM   1042  CG  LEU A 141      80.170  34.256  65.470  1.00  4.47           C  
-ATOM   1043  CD1 LEU A 141      78.687  34.534  65.280  1.00  4.47           C  
-ATOM   1044  CD2 LEU A 141      80.428  33.595  66.798  1.00  4.47           C  
-ATOM   1045  N   SER A 142      81.947  33.133  61.396  1.00  4.47           N  
-ATOM   1046  CA  SER A 142      82.948  33.612  60.468  1.00  4.47           C  
-ATOM   1047  C   SER A 142      82.229  34.182  59.245  1.00 10.64           C  
-ATOM   1048  O   SER A 142      82.580  35.254  58.755  1.00 14.36           O  
-ATOM   1049  CB  SER A 142      83.895  32.486  60.077  1.00  4.47           C  
-ATOM   1050  OG  SER A 142      84.631  32.025  61.199  1.00  4.47           O  
-ATOM   1051  N   ARG A 143      81.210  33.482  58.759  1.00  4.47           N  
-ATOM   1052  CA  ARG A 143      80.461  33.981  57.618  1.00  4.47           C  
-ATOM   1053  C   ARG A 143      79.935  35.377  57.904  1.00  4.47           C  
-ATOM   1054  O   ARG A 143      79.996  36.245  57.054  1.00  8.33           O  
-ATOM   1055  CB  ARG A 143      79.284  33.073  57.296  1.00  4.47           C  
-ATOM   1056  CG  ARG A 143      79.683  31.723  56.762  1.00 11.67           C  
-ATOM   1057  CD  ARG A 143      80.361  31.808  55.410  1.00  4.47           C  
-ATOM   1058  NE  ARG A 143      80.854  30.499  55.016  1.00  4.47           N  
-ATOM   1059  CZ  ARG A 143      81.649  30.284  53.981  1.00  6.27           C  
-ATOM   1060  NH1 ARG A 143      82.034  31.310  53.237  1.00  4.47           N  
-ATOM   1061  NH2 ARG A 143      82.055  29.049  53.692  1.00 15.13           N  
-ATOM   1062  N   TYR A 144      79.402  35.596  59.095  1.00  4.47           N  
-ATOM   1063  CA  TYR A 144      78.893  36.916  59.423  1.00  8.65           C  
-ATOM   1064  C   TYR A 144      79.996  37.952  59.283  1.00  9.10           C  
-ATOM   1065  O   TYR A 144      79.884  38.897  58.504  1.00 14.57           O  
-ATOM   1066  CB  TYR A 144      78.340  36.955  60.853  1.00 14.62           C  
-ATOM   1067  CG  TYR A 144      78.072  38.356  61.353  1.00 16.44           C  
-ATOM   1068  CD1 TYR A 144      78.996  39.019  62.165  1.00 25.05           C  
-ATOM   1069  CD2 TYR A 144      76.916  39.041  60.977  1.00 21.98           C  
-ATOM   1070  CE1 TYR A 144      78.775  40.345  62.592  1.00 35.19           C  
-ATOM   1071  CE2 TYR A 144      76.685  40.363  61.392  1.00 34.77           C  
-ATOM   1072  CZ  TYR A 144      77.622  41.010  62.199  1.00 37.74           C  
-ATOM   1073  OH  TYR A 144      77.420  42.322  62.580  1.00 39.71           O  
-ATOM   1074  N   LEU A 145      81.064  37.761  60.042  1.00  8.85           N  
-ATOM   1075  CA  LEU A 145      82.185  38.684  60.032  1.00  7.28           C  
-ATOM   1076  C   LEU A 145      82.666  39.064  58.634  1.00  4.56           C  
-ATOM   1077  O   LEU A 145      82.979  40.223  58.384  1.00  4.47           O  
-ATOM   1078  CB  LEU A 145      83.339  38.098  60.850  1.00  7.57           C  
-ATOM   1079  CG  LEU A 145      83.020  37.874  62.325  1.00  4.47           C  
-ATOM   1080  CD1 LEU A 145      84.230  37.340  63.014  1.00  5.16           C  
-ATOM   1081  CD2 LEU A 145      82.608  39.166  62.972  1.00  4.97           C  
-ATOM   1082  N   VAL A 146      82.723  38.097  57.726  1.00  5.25           N  
-ATOM   1083  CA  VAL A 146      83.178  38.358  56.364  1.00  4.47           C  
-ATOM   1084  C   VAL A 146      82.095  39.002  55.513  1.00  4.47           C  
-ATOM   1085  O   VAL A 146      82.360  39.481  54.416  1.00  4.47           O  
-ATOM   1086  CB  VAL A 146      83.654  37.060  55.695  1.00  4.47           C  
-ATOM   1087  CG1 VAL A 146      83.405  37.103  54.209  1.00  9.80           C  
-ATOM   1088  CG2 VAL A 146      85.133  36.880  55.952  1.00  4.47           C  
-ATOM   1089  N   GLY A 147      80.869  39.000  56.021  1.00  7.13           N  
-ATOM   1090  CA  GLY A 147      79.770  39.610  55.302  1.00  4.47           C  
-ATOM   1091  C   GLY A 147      79.004  38.682  54.392  1.00  5.60           C  
-ATOM   1092  O   GLY A 147      78.153  39.138  53.629  1.00  9.59           O  
-ATOM   1093  N   ASP A 148      79.287  37.384  54.462  1.00 10.68           N  
-ATOM   1094  CA  ASP A 148      78.583  36.419  53.621  1.00 14.72           C  
-ATOM   1095  C   ASP A 148      77.237  35.929  54.185  1.00 13.28           C  
-ATOM   1096  O   ASP A 148      76.444  35.301  53.465  1.00  4.47           O  
-ATOM   1097  CB  ASP A 148      79.483  35.217  53.332  1.00 16.15           C  
-ATOM   1098  CG  ASP A 148      80.479  35.491  52.228  1.00 34.62           C  
-ATOM   1099  OD1 ASP A 148      80.128  36.225  51.281  1.00 43.67           O  
-ATOM   1100  OD2 ASP A 148      81.609  34.960  52.287  1.00 47.10           O  
-ATOM   1101  N   MET A 149      76.969  36.237  55.453  1.00 10.38           N  
-ATOM   1102  CA  MET A 149      75.736  35.798  56.095  1.00 11.19           C  
-ATOM   1103  C   MET A 149      75.132  36.875  56.982  1.00 16.79           C  
-ATOM   1104  O   MET A 149      75.851  37.680  57.559  1.00 16.38           O  
-ATOM   1105  CB  MET A 149      76.028  34.546  56.916  1.00 13.04           C  
-ATOM   1106  CG  MET A 149      74.878  34.070  57.773  1.00 14.48           C  
-ATOM   1107  SD  MET A 149      75.307  32.556  58.675  1.00  4.47           S  
-ATOM   1108  CE  MET A 149      75.363  31.427  57.338  1.00 13.97           C  
-ATOM   1109  N   SER A 150      73.805  36.884  57.086  1.00 26.12           N  
-ATOM   1110  CA  SER A 150      73.092  37.875  57.905  1.00 32.93           C  
-ATOM   1111  C   SER A 150      72.955  37.421  59.365  1.00 29.64           C  
-ATOM   1112  O   SER A 150      72.547  36.286  59.635  1.00 30.19           O  
-ATOM   1113  CB  SER A 150      71.699  38.142  57.313  1.00 44.47           C  
-ATOM   1114  OG  SER A 150      70.930  36.951  57.217  1.00 45.26           O  
-ATOM   1115  N   PRO A 151      73.256  38.317  60.324  1.00 21.54           N  
-ATOM   1116  CA  PRO A 151      73.183  38.019  61.761  1.00 14.60           C  
-ATOM   1117  C   PRO A 151      71.897  37.344  62.177  1.00 13.35           C  
-ATOM   1118  O   PRO A 151      71.857  36.600  63.155  1.00 20.47           O  
-ATOM   1119  CB  PRO A 151      73.337  39.386  62.410  1.00  4.47           C  
-ATOM   1120  CG  PRO A 151      72.705  40.265  61.433  1.00 14.47           C  
-ATOM   1121  CD  PRO A 151      73.275  39.771  60.118  1.00 17.13           C  
-ATOM   1122  N   ALA A 152      70.850  37.597  61.415  1.00  9.19           N  
-ATOM   1123  CA  ALA A 152      69.547  37.037  61.707  1.00  6.79           C  
-ATOM   1124  C   ALA A 152      69.550  35.559  62.073  1.00  7.08           C  
-ATOM   1125  O   ALA A 152      68.634  35.087  62.756  1.00  9.66           O  
-ATOM   1126  CB  ALA A 152      68.636  37.271  60.534  1.00 11.27           C  
-ATOM   1127  N   ALA A 153      70.575  34.827  61.645  1.00  4.47           N  
-ATOM   1128  CA  ALA A 153      70.612  33.397  61.933  1.00  8.17           C  
-ATOM   1129  C   ALA A 153      71.472  33.003  63.111  1.00 13.36           C  
-ATOM   1130  O   ALA A 153      71.644  31.812  63.373  1.00 20.60           O  
-ATOM   1131  CB  ALA A 153      71.071  32.636  60.706  1.00 11.78           C  
-ATOM   1132  N   LEU A 154      72.020  33.979  63.827  1.00 13.34           N  
-ATOM   1133  CA  LEU A 154      72.870  33.637  64.953  1.00  9.44           C  
-ATOM   1134  C   LEU A 154      72.109  33.108  66.161  1.00 10.59           C  
-ATOM   1135  O   LEU A 154      72.514  32.116  66.766  1.00 18.98           O  
-ATOM   1136  CB  LEU A 154      73.758  34.823  65.322  1.00  4.47           C  
-ATOM   1137  CG  LEU A 154      74.723  35.108  64.163  1.00  4.47           C  
-ATOM   1138  CD1 LEU A 154      75.553  36.308  64.453  1.00  5.06           C  
-ATOM   1139  CD2 LEU A 154      75.626  33.929  63.931  1.00  4.47           C  
-ATOM   1140  N   PRO A 155      70.975  33.725  66.508  1.00  4.47           N  
-ATOM   1141  CA  PRO A 155      70.217  33.250  67.664  1.00  4.47           C  
-ATOM   1142  C   PRO A 155      69.833  31.785  67.534  1.00  8.04           C  
-ATOM   1143  O   PRO A 155      69.965  30.997  68.470  1.00 16.76           O  
-ATOM   1144  CB  PRO A 155      69.002  34.161  67.674  1.00  4.47           C  
-ATOM   1145  CG  PRO A 155      69.522  35.421  67.060  1.00  9.39           C  
-ATOM   1146  CD  PRO A 155      70.318  34.887  65.899  1.00  5.03           C  
-ATOM   1147  N   GLY A 156      69.365  31.411  66.359  1.00  7.57           N  
-ATOM   1148  CA  GLY A 156      68.974  30.033  66.153  1.00 11.75           C  
-ATOM   1149  C   GLY A 156      70.091  29.032  66.343  1.00 13.83           C  
-ATOM   1150  O   GLY A 156      69.832  27.868  66.631  1.00 19.28           O  
-ATOM   1151  N   LEU A 157      71.336  29.469  66.191  1.00 18.12           N  
-ATOM   1152  CA  LEU A 157      72.457  28.551  66.348  1.00 21.30           C  
-ATOM   1153  C   LEU A 157      73.214  28.715  67.657  1.00 25.98           C  
-ATOM   1154  O   LEU A 157      73.587  27.714  68.274  1.00 36.10           O  
-ATOM   1155  CB  LEU A 157      73.441  28.715  65.196  1.00 22.31           C  
-ATOM   1156  CG  LEU A 157      72.885  28.888  63.777  1.00 19.45           C  
-ATOM   1157  CD1 LEU A 157      74.051  28.968  62.761  1.00  4.47           C  
-ATOM   1158  CD2 LEU A 157      71.947  27.730  63.459  1.00 13.47           C  
-ATOM   1159  N   LEU A 158      73.435  29.964  68.077  1.00 17.37           N  
-ATOM   1160  CA  LEU A 158      74.180  30.248  69.301  1.00  8.53           C  
-ATOM   1161  C   LEU A 158      73.406  30.104  70.586  1.00 12.58           C  
-ATOM   1162  O   LEU A 158      73.909  29.545  71.559  1.00 20.67           O  
-ATOM   1163  CB  LEU A 158      74.760  31.653  69.257  1.00  6.06           C  
-ATOM   1164  CG  LEU A 158      75.598  31.950  68.015  1.00 12.56           C  
-ATOM   1165  CD1 LEU A 158      76.224  33.335  68.117  1.00 16.04           C  
-ATOM   1166  CD2 LEU A 158      76.656  30.895  67.869  1.00  4.47           C  
-ATOM   1167  N   PHE A 159      72.177  30.595  70.593  1.00 13.46           N  
-ATOM   1168  CA  PHE A 159      71.379  30.547  71.805  1.00 15.54           C  
-ATOM   1169  C   PHE A 159      70.595  29.272  72.086  1.00 19.79           C  
-ATOM   1170  O   PHE A 159      70.069  29.101  73.178  1.00 34.12           O  
-ATOM   1171  CB  PHE A 159      70.444  31.746  71.829  1.00 11.01           C  
-ATOM   1172  CG  PHE A 159      71.138  33.056  71.588  1.00 15.73           C  
-ATOM   1173  CD1 PHE A 159      72.465  33.240  71.960  1.00 13.26           C  
-ATOM   1174  CD2 PHE A 159      70.448  34.129  71.045  1.00 11.99           C  
-ATOM   1175  CE1 PHE A 159      73.084  34.470  71.799  1.00  6.66           C  
-ATOM   1176  CE2 PHE A 159      71.068  35.365  70.883  1.00 13.33           C  
-ATOM   1177  CZ  PHE A 159      72.386  35.532  71.263  1.00  8.81           C  
-ATOM   1178  N   THR A 160      70.510  28.367  71.125  1.00 20.52           N  
-ATOM   1179  CA  THR A 160      69.779  27.128  71.367  1.00 25.08           C  
-ATOM   1180  C   THR A 160      70.694  25.936  71.668  1.00 22.60           C  
-ATOM   1181  O   THR A 160      70.304  24.782  71.473  1.00 27.73           O  
-ATOM   1182  CB  THR A 160      68.886  26.758  70.158  1.00 29.18           C  
-ATOM   1183  OG1 THR A 160      69.685  26.646  68.973  1.00 28.61           O  
-ATOM   1184  CG2 THR A 160      67.827  27.811  69.952  1.00 31.41           C  
-ATOM   1185  N   LEU A 161      71.904  26.200  72.143  1.00 11.64           N  
-ATOM   1186  CA  LEU A 161      72.816  25.105  72.423  1.00 12.13           C  
-ATOM   1187  C   LEU A 161      72.366  24.227  73.577  1.00 13.83           C  
-ATOM   1188  O   LEU A 161      71.857  24.714  74.577  1.00 26.84           O  
-ATOM   1189  CB  LEU A 161      74.211  25.645  72.695  1.00  7.20           C  
-ATOM   1190  CG  LEU A 161      74.893  26.182  71.447  1.00  4.47           C  
-ATOM   1191  CD1 LEU A 161      76.321  26.513  71.751  1.00  4.47           C  
-ATOM   1192  CD2 LEU A 161      74.832  25.137  70.371  1.00  4.47           C  
-ATOM   1193  N   PRO A 162      72.539  22.908  73.446  1.00 13.37           N  
-ATOM   1194  CA  PRO A 162      72.150  21.953  74.488  1.00 18.90           C  
-ATOM   1195  C   PRO A 162      73.245  21.782  75.544  1.00 23.27           C  
-ATOM   1196  O   PRO A 162      74.437  21.917  75.251  1.00 28.77           O  
-ATOM   1197  CB  PRO A 162      71.914  20.682  73.700  1.00 16.51           C  
-ATOM   1198  CG  PRO A 162      72.999  20.760  72.678  1.00 19.22           C  
-ATOM   1199  CD  PRO A 162      72.940  22.204  72.218  1.00 15.20           C  
-ATOM   1200  N   ALA A 163      72.834  21.482  76.769  1.00 19.85           N  
-ATOM   1201  CA  ALA A 163      73.777  21.307  77.864  1.00 20.03           C  
-ATOM   1202  C   ALA A 163      74.911  20.387  77.464  1.00 20.41           C  
-ATOM   1203  O   ALA A 163      74.693  19.251  77.025  1.00 25.28           O  
-ATOM   1204  CB  ALA A 163      73.064  20.744  79.076  1.00 33.33           C  
-ATOM   1205  N   GLU A 164      76.128  20.881  77.612  1.00 18.94           N  
-ATOM   1206  CA  GLU A 164      77.292  20.087  77.265  1.00 30.66           C  
-ATOM   1207  C   GLU A 164      77.689  19.251  78.475  1.00 41.83           C  
-ATOM   1208  O   GLU A 164      77.834  19.777  79.587  1.00 47.80           O  
-ATOM   1209  CB  GLU A 164      78.458  20.993  76.875  1.00 32.74           C  
-ATOM   1210  CG  GLU A 164      79.699  20.250  76.392  1.00 35.08           C  
-ATOM   1211  CD  GLU A 164      79.548  19.732  74.979  1.00 39.44           C  
-ATOM   1212  OE1 GLU A 164      78.418  19.803  74.448  1.00 48.92           O  
-ATOM   1213  OE2 GLU A 164      80.553  19.255  74.402  1.00 28.30           O  
-ATOM   1214  N   PRO A 165      77.848  17.931  78.281  1.00 41.50           N  
-ATOM   1215  CA  PRO A 165      78.236  17.030  79.370  1.00 41.76           C  
-ATOM   1216  C   PRO A 165      79.712  17.228  79.755  1.00 47.04           C  
-ATOM   1217  O   PRO A 165      80.564  17.489  78.898  1.00 51.28           O  
-ATOM   1218  CB  PRO A 165      77.955  15.654  78.784  1.00 37.96           C  
-ATOM   1219  CG  PRO A 165      78.212  15.860  77.330  1.00 32.40           C  
-ATOM   1220  CD  PRO A 165      77.542  17.173  77.056  1.00 31.26           C  
-ATOM   1221  N   PRO A 166      80.030  17.113  81.054  1.00 45.37           N  
-ATOM   1222  CA  PRO A 166      81.402  17.287  81.537  1.00 40.70           C  
-ATOM   1223  C   PRO A 166      82.411  16.404  80.818  1.00 34.30           C  
-ATOM   1224  O   PRO A 166      82.112  15.247  80.498  1.00 30.83           O  
-ATOM   1225  CB  PRO A 166      81.290  16.936  83.018  1.00 45.99           C  
-ATOM   1226  CG  PRO A 166      79.880  17.347  83.354  1.00 51.28           C  
-ATOM   1227  CD  PRO A 166      79.116  16.815  82.170  1.00 48.08           C  
-ATOM   1228  N   GLY A 167      83.593  16.965  80.554  1.00 28.84           N  
-ATOM   1229  CA  GLY A 167      84.651  16.204  79.909  1.00 25.10           C  
-ATOM   1230  C   GLY A 167      84.912  16.431  78.433  1.00 25.43           C  
-ATOM   1231  O   GLY A 167      85.505  15.573  77.767  1.00 22.77           O  
-ATOM   1232  N   THR A 168      84.480  17.570  77.903  1.00 22.37           N  
-ATOM   1233  CA  THR A 168      84.717  17.838  76.496  1.00 11.18           C  
-ATOM   1234  C   THR A 168      86.084  18.442  76.313  1.00 11.67           C  
-ATOM   1235  O   THR A 168      86.406  19.467  76.892  1.00 17.09           O  
-ATOM   1236  CB  THR A 168      83.718  18.799  75.931  1.00  4.70           C  
-ATOM   1237  OG1 THR A 168      82.402  18.253  76.069  1.00  9.97           O  
-ATOM   1238  CG2 THR A 168      84.027  19.045  74.473  1.00  4.47           C  
-ATOM   1239  N   ASN A 169      86.898  17.794  75.506  1.00 13.11           N  
-ATOM   1240  CA  ASN A 169      88.238  18.281  75.260  1.00 12.53           C  
-ATOM   1241  C   ASN A 169      88.311  18.794  73.829  1.00  7.50           C  
-ATOM   1242  O   ASN A 169      88.324  18.041  72.867  1.00  4.47           O  
-ATOM   1243  CB  ASN A 169      89.256  17.158  75.498  1.00 14.82           C  
-ATOM   1244  CG  ASN A 169      89.373  16.778  76.955  1.00  8.59           C  
-ATOM   1245  OD1 ASN A 169      89.963  17.503  77.742  1.00 16.40           O  
-ATOM   1246  ND2 ASN A 169      88.800  15.641  77.323  1.00  8.38           N  
-ATOM   1247  N   LEU A 170      88.350  20.102  73.703  1.00  9.61           N  
-ATOM   1248  CA  LEU A 170      88.411  20.739  72.406  1.00 12.15           C  
-ATOM   1249  C   LEU A 170      89.865  21.001  72.029  1.00 13.03           C  
-ATOM   1250  O   LEU A 170      90.562  21.756  72.695  1.00 22.11           O  
-ATOM   1251  CB  LEU A 170      87.639  22.038  72.480  1.00  6.21           C  
-ATOM   1252  CG  LEU A 170      86.958  22.487  71.219  1.00  6.08           C  
-ATOM   1253  CD1 LEU A 170      86.204  23.766  71.529  1.00 12.95           C  
-ATOM   1254  CD2 LEU A 170      87.999  22.679  70.129  1.00  6.31           C  
-ATOM   1255  N   VAL A 171      90.320  20.369  70.960  1.00  7.82           N  
-ATOM   1256  CA  VAL A 171      91.690  20.529  70.515  1.00  7.29           C  
-ATOM   1257  C   VAL A 171      91.700  21.315  69.225  1.00 16.26           C  
-ATOM   1258  O   VAL A 171      91.453  20.758  68.156  1.00 28.22           O  
-ATOM   1259  CB  VAL A 171      92.352  19.158  70.265  1.00  7.29           C  
-ATOM   1260  CG1 VAL A 171      93.788  19.331  69.820  1.00  4.47           C  
-ATOM   1261  CG2 VAL A 171      92.290  18.329  71.527  1.00 18.42           C  
-ATOM   1262  N   VAL A 172      91.973  22.612  69.325  1.00 12.22           N  
-ATOM   1263  CA  VAL A 172      92.028  23.469  68.147  1.00  4.47           C  
-ATOM   1264  C   VAL A 172      93.353  23.290  67.431  1.00  7.84           C  
-ATOM   1265  O   VAL A 172      94.396  23.546  68.010  1.00 16.46           O  
-ATOM   1266  CB  VAL A 172      91.916  24.934  68.526  1.00  4.47           C  
-ATOM   1267  CG1 VAL A 172      92.041  25.783  67.294  1.00  6.13           C  
-ATOM   1268  CG2 VAL A 172      90.604  25.189  69.215  1.00  4.47           C  
-ATOM   1269  N   CYS A 173      93.312  22.852  66.180  1.00 11.93           N  
-ATOM   1270  CA  CYS A 173      94.526  22.659  65.392  1.00 20.44           C  
-ATOM   1271  C   CYS A 173      94.932  23.982  64.787  1.00 20.91           C  
-ATOM   1272  O   CYS A 173      94.079  24.788  64.456  1.00 30.16           O  
-ATOM   1273  CB  CYS A 173      94.287  21.657  64.265  1.00 28.06           C  
-ATOM   1274  SG  CYS A 173      93.826  20.007  64.822  1.00 42.10           S  
-ATOM   1275  N   THR A 174      96.233  24.202  64.636  1.00 26.43           N  
-ATOM   1276  CA  THR A 174      96.737  25.452  64.069  1.00 32.10           C  
-ATOM   1277  C   THR A 174      97.882  25.191  63.106  1.00 37.37           C  
-ATOM   1278  O   THR A 174      98.673  24.271  63.308  1.00 44.23           O  
-ATOM   1279  CB  THR A 174      97.275  26.380  65.149  1.00 32.14           C  
-ATOM   1280  OG1 THR A 174      98.564  25.914  65.571  1.00 36.03           O  
-ATOM   1281  CG2 THR A 174      96.337  26.400  66.342  1.00 36.26           C  
-ATOM   1282  N   VAL A 175      97.969  26.011  62.065  1.00 42.17           N  
-ATOM   1283  CA  VAL A 175      99.023  25.877  61.066  1.00 49.75           C  
-ATOM   1284  C   VAL A 175      99.547  27.271  60.778  1.00 57.30           C  
-ATOM   1285  O   VAL A 175      98.839  28.246  61.007  1.00 56.83           O  
-ATOM   1286  CB  VAL A 175      98.481  25.293  59.746  1.00 47.73           C  
-ATOM   1287  CG1 VAL A 175      99.627  25.048  58.775  1.00 49.92           C  
-ATOM   1288  CG2 VAL A 175      97.732  24.007  60.011  1.00 49.40           C  
-ATOM   1289  N   SER A 176     100.782  27.377  60.296  1.00 65.94           N  
-ATOM   1290  CA  SER A 176     101.326  28.689  59.967  1.00 73.03           C  
-ATOM   1291  C   SER A 176     100.487  29.190  58.791  1.00 78.13           C  
-ATOM   1292  O   SER A 176      99.913  28.386  58.052  1.00 79.89           O  
-ATOM   1293  CB  SER A 176     102.811  28.590  59.583  1.00 76.59           C  
-ATOM   1294  OG  SER A 176     103.005  27.834  58.400  1.00 85.57           O  
-ATOM   1295  N   LEU A 177     100.407  30.506  58.618  1.00 83.31           N  
-ATOM   1296  CA  LEU A 177      99.600  31.092  57.547  1.00 88.53           C  
-ATOM   1297  C   LEU A 177      99.970  30.715  56.103  1.00 90.22           C  
-ATOM   1298  O   LEU A 177      99.120  30.223  55.361  1.00 91.01           O  
-ATOM   1299  CB  LEU A 177      99.564  32.617  57.698  1.00 91.00           C  
-ATOM   1300  CG  LEU A 177      98.757  33.401  56.661  1.00 95.28           C  
-ATOM   1301  CD1 LEU A 177      97.354  32.819  56.538  1.00 96.72           C  
-ATOM   1302  CD2 LEU A 177      98.703  34.867  57.071  1.00 95.55           C  
-ATOM   1303  N   PRO A 178     101.229  30.949  55.678  1.00 92.66           N  
-ATOM   1304  CA  PRO A 178     101.638  30.607  54.303  1.00 92.19           C  
-ATOM   1305  C   PRO A 178     101.512  29.116  53.947  1.00 90.83           C  
-ATOM   1306  O   PRO A 178     101.361  28.759  52.773  1.00 82.10           O  
-ATOM   1307  CB  PRO A 178     103.086  31.092  54.244  1.00 95.36           C  
-ATOM   1308  CG  PRO A 178     103.082  32.266  55.191  1.00 96.42           C  
-ATOM   1309  CD  PRO A 178     102.290  31.718  56.358  1.00 94.43           C  
-ATOM   1310  N   SER A 179     101.583  28.262  54.970  1.00 95.24           N  
-ATOM   1311  CA  SER A 179     101.476  26.806  54.816  1.00 96.22           C  
-ATOM   1312  C   SER A 179     100.008  26.387  54.663  1.00 98.59           C  
-ATOM   1313  O   SER A 179      99.686  25.455  53.919  1.00 97.94           O  
-ATOM   1314  CB  SER A 179     102.093  26.103  56.038  1.00 91.50           C  
-ATOM   1315  OG  SER A 179     101.969  24.692  55.961  1.00 86.75           O  
-ATOM   1316  N   HIS A 180      99.131  27.087  55.380  1.00 97.92           N  
-ATOM   1317  CA  HIS A 180      97.691  26.838  55.349  1.00 94.29           C  
-ATOM   1318  C   HIS A 180      97.153  27.126  53.942  1.00 93.02           C  
-ATOM   1319  O   HIS A 180      96.218  26.466  53.477  1.00 90.83           O  
-ATOM   1320  CB  HIS A 180      97.010  27.739  56.399  1.00 92.41           C  
-ATOM   1321  CG  HIS A 180      95.515  27.624  56.451  1.00 89.74           C  
-ATOM   1322  ND1 HIS A 180      94.768  28.206  57.453  1.00 83.64           N  
-ATOM   1323  CD2 HIS A 180      94.627  27.029  55.617  1.00 87.02           C  
-ATOM   1324  CE1 HIS A 180      93.486  27.975  57.234  1.00 84.03           C  
-ATOM   1325  NE2 HIS A 180      93.373  27.263  56.126  1.00 84.49           N  
-ATOM   1326  N   LEU A 181      97.768  28.095  53.266  1.00 92.03           N  
-ATOM   1327  CA  LEU A 181      97.357  28.491  51.923  1.00 90.80           C  
-ATOM   1328  C   LEU A 181      97.857  27.559  50.818  1.00 97.86           C  
-ATOM   1329  O   LEU A 181      97.687  27.849  49.630  1.00100.36           O  
-ATOM   1330  CB  LEU A 181      97.815  29.921  51.648  1.00 75.61           C  
-ATOM   1331  CG  LEU A 181      97.466  30.886  52.782  1.00 68.11           C  
-ATOM   1332  CD1 LEU A 181      97.856  32.299  52.372  1.00 68.84           C  
-ATOM   1333  CD2 LEU A 181      95.979  30.796  53.122  1.00 51.08           C  
-ATOM   1334  N   SER A 182      98.472  26.444  51.212  1.00101.48           N  
-ATOM   1335  CA  SER A 182      98.973  25.455  50.258  1.00101.02           C  
-ATOM   1336  C   SER A 182      98.264  24.118  50.500  1.00104.44           C  
-ATOM   1337  O   SER A 182      98.104  23.313  49.578  1.00108.15           O  
-ATOM   1338  CB  SER A 182     100.493  25.281  50.399  1.00 95.28           C  
-ATOM   1339  OG  SER A 182     100.842  24.721  51.654  1.00 87.73           O  
-ATOM   1340  N   ARG A 183      97.835  23.895  51.744  1.00103.80           N  
-ATOM   1341  CA  ARG A 183      97.127  22.669  52.135  1.00100.70           C  
-ATOM   1342  C   ARG A 183      95.773  22.591  51.422  1.00 98.03           C  
-ATOM   1343  O   ARG A 183      95.212  21.508  51.218  1.00 92.25           O  
-ATOM   1344  CB  ARG A 183      96.898  22.647  53.655  1.00 96.59           C  
-ATOM   1345  CG  ARG A 183      98.164  22.657  54.508  1.00 89.70           C  
-ATOM   1346  CD  ARG A 183      98.974  21.379  54.338  1.00 84.15           C  
-ATOM   1347  NE  ARG A 183     100.143  21.352  55.213  1.00 78.49           N  
-ATOM   1348  CZ  ARG A 183     100.089  21.337  56.542  1.00 73.70           C  
-ATOM   1349  NH1 ARG A 183      98.920  21.345  57.164  1.00 70.98           N  
-ATOM   1350  NH2 ARG A 183     101.207  21.311  57.253  1.00 76.95           N  
-ATOM   1351  N   VAL A 184      95.254  23.758  51.055  1.00 98.73           N  
-ATOM   1352  CA  VAL A 184      93.977  23.852  50.365  1.00100.46           C  
-ATOM   1353  C   VAL A 184      94.192  23.734  48.844  1.00104.32           C  
-ATOM   1354  O   VAL A 184      93.965  22.666  48.267  1.00104.26           O  
-ATOM   1355  CB  VAL A 184      93.267  25.196  50.704  1.00 96.98           C  
-ATOM   1356  CG1 VAL A 184      91.822  25.163  50.214  1.00 91.94           C  
-ATOM   1357  CG2 VAL A 184      93.318  25.451  52.217  1.00 90.67           C  
-ATOM   1358  N   SER A 185      94.645  24.814  48.203  1.00106.44           N  
-ATOM   1359  CA  SER A 185      94.881  24.827  46.750  1.00103.40           C  
-ATOM   1360  C   SER A 185      95.812  23.705  46.272  1.00101.47           C  
-ATOM   1361  O   SER A 185      95.494  22.966  45.333  1.00 96.65           O  
-ATOM   1362  CB  SER A 185      95.443  26.190  46.325  1.00 99.91           C  
-ATOM   1363  N   GLU A 192      84.963  24.047  46.759  1.00 90.95           N  
-ATOM   1364  CA  GLU A 192      85.829  24.752  47.703  1.00 96.55           C  
-ATOM   1365  C   GLU A 192      86.443  26.008  47.065  1.00 97.58           C  
-ATOM   1366  O   GLU A 192      86.446  26.140  45.839  1.00 98.08           O  
-ATOM   1367  CB  GLU A 192      86.931  23.807  48.197  1.00 94.29           C  
-ATOM   1368  N   THR A 193      86.958  26.925  47.892  1.00 98.06           N  
-ATOM   1369  CA  THR A 193      87.568  28.166  47.394  1.00 97.09           C  
-ATOM   1370  C   THR A 193      88.594  28.767  48.366  1.00 95.02           C  
-ATOM   1371  O   THR A 193      88.369  28.795  49.578  1.00 96.04           O  
-ATOM   1372  CB  THR A 193      86.477  29.193  47.092  1.00 96.52           C  
-ATOM   1373  N   VAL A 194      89.712  29.254  47.827  1.00 91.11           N  
-ATOM   1374  CA  VAL A 194      90.773  29.849  48.644  1.00 84.67           C  
-ATOM   1375  C   VAL A 194      90.771  31.380  48.613  1.00 79.39           C  
-ATOM   1376  O   VAL A 194      91.294  32.001  47.682  1.00 81.12           O  
-ATOM   1377  CB  VAL A 194      92.141  29.323  48.196  1.00 82.36           C  
-ATOM   1378  N   ASN A 195      90.171  31.979  49.634  1.00 69.77           N  
-ATOM   1379  CA  ASN A 195      90.117  33.428  49.745  1.00 65.92           C  
-ATOM   1380  C   ASN A 195      90.550  33.825  51.157  1.00 64.61           C  
-ATOM   1381  O   ASN A 195      89.929  33.441  52.155  1.00 62.98           O  
-ATOM   1382  CB  ASN A 195      88.701  33.966  49.456  1.00 66.30           C  
-ATOM   1383  CG  ASN A 195      87.678  33.554  50.514  1.00 67.58           C  
-ATOM   1384  OD1 ASN A 195      86.672  34.247  50.735  1.00 58.13           O  
-ATOM   1385  ND2 ASN A 195      87.925  32.418  51.164  1.00 70.44           N  
-ATOM   1386  N   LEU A 196      91.631  34.587  51.240  1.00 60.77           N  
-ATOM   1387  CA  LEU A 196      92.139  35.035  52.529  1.00 55.55           C  
-ATOM   1388  C   LEU A 196      91.014  35.452  53.479  1.00 44.84           C  
-ATOM   1389  O   LEU A 196      90.776  34.800  54.488  1.00 36.50           O  
-ATOM   1390  CB  LEU A 196      93.104  36.211  52.336  1.00 64.09           C  
-ATOM   1391  CG  LEU A 196      94.389  35.947  51.549  1.00 69.51           C  
-ATOM   1392  CD1 LEU A 196      95.070  37.273  51.214  1.00 74.35           C  
-ATOM   1393  CD2 LEU A 196      95.307  35.047  52.364  1.00 67.53           C  
-ATOM   1394  N   PRO A 197      90.286  36.525  53.137  1.00 39.19           N  
-ATOM   1395  CA  PRO A 197      89.194  37.029  53.967  1.00 37.82           C  
-ATOM   1396  C   PRO A 197      88.525  36.023  54.883  1.00 31.16           C  
-ATOM   1397  O   PRO A 197      88.495  36.217  56.092  1.00 29.19           O  
-ATOM   1398  CB  PRO A 197      88.234  37.606  52.938  1.00 48.18           C  
-ATOM   1399  CG  PRO A 197      89.172  38.201  51.955  1.00 46.96           C  
-ATOM   1400  CD  PRO A 197      90.188  37.094  51.779  1.00 37.92           C  
-ATOM   1401  N   PHE A 198      87.997  34.945  54.318  1.00 26.82           N  
-ATOM   1402  CA  PHE A 198      87.311  33.950  55.135  1.00 23.75           C  
-ATOM   1403  C   PHE A 198      88.250  33.169  56.024  1.00 24.11           C  
-ATOM   1404  O   PHE A 198      87.986  32.972  57.212  1.00 23.95           O  
-ATOM   1405  CB  PHE A 198      86.540  32.972  54.268  1.00 21.40           C  
-ATOM   1406  CG  PHE A 198      85.603  32.102  55.042  1.00  9.84           C  
-ATOM   1407  CD1 PHE A 198      84.510  32.654  55.699  1.00 11.73           C  
-ATOM   1408  CD2 PHE A 198      85.811  30.739  55.120  1.00 14.30           C  
-ATOM   1409  CE1 PHE A 198      83.644  31.863  56.419  1.00 13.10           C  
-ATOM   1410  CE2 PHE A 198      84.951  29.939  55.838  1.00 16.12           C  
-ATOM   1411  CZ  PHE A 198      83.865  30.501  56.488  1.00 17.17           C  
-ATOM   1412  N   VAL A 199      89.342  32.705  55.438  1.00 24.12           N  
-ATOM   1413  CA  VAL A 199      90.334  31.958  56.194  1.00 24.41           C  
-ATOM   1414  C   VAL A 199      90.863  32.803  57.364  1.00 20.95           C  
-ATOM   1415  O   VAL A 199      90.725  32.438  58.532  1.00  4.47           O  
-ATOM   1416  CB  VAL A 199      91.494  31.562  55.275  1.00 28.36           C  
-ATOM   1417  CG1 VAL A 199      92.707  31.167  56.095  1.00 38.81           C  
-ATOM   1418  CG2 VAL A 199      91.060  30.415  54.386  1.00 31.78           C  
-ATOM   1419  N   MET A 200      91.461  33.944  57.026  1.00 27.91           N  
-ATOM   1420  CA  MET A 200      92.010  34.871  58.008  1.00 22.61           C  
-ATOM   1421  C   MET A 200      91.044  35.026  59.176  1.00 16.05           C  
-ATOM   1422  O   MET A 200      91.457  35.061  60.325  1.00 20.79           O  
-ATOM   1423  CB  MET A 200      92.259  36.239  57.359  1.00 22.71           C  
-ATOM   1424  CG  MET A 200      93.514  36.939  57.869  1.00 34.90           C  
-ATOM   1425  SD  MET A 200      95.032  35.960  57.580  1.00 36.65           S  
-ATOM   1426  CE  MET A 200      95.355  36.419  55.813  1.00 31.20           C  
-ATOM   1427  N   VAL A 201      89.756  35.117  58.878  1.00  7.27           N  
-ATOM   1428  CA  VAL A 201      88.752  35.261  59.914  1.00  4.47           C  
-ATOM   1429  C   VAL A 201      88.568  33.962  60.672  1.00  4.47           C  
-ATOM   1430  O   VAL A 201      88.604  33.937  61.902  1.00  4.47           O  
-ATOM   1431  CB  VAL A 201      87.393  35.658  59.317  1.00  8.43           C  
-ATOM   1432  CG1 VAL A 201      86.308  35.529  60.351  1.00  9.69           C  
-ATOM   1433  CG2 VAL A 201      87.440  37.077  58.831  1.00 12.54           C  
-ATOM   1434  N   LEU A 202      88.370  32.877  59.935  1.00  4.47           N  
-ATOM   1435  CA  LEU A 202      88.153  31.585  60.567  1.00  7.63           C  
-ATOM   1436  C   LEU A 202      89.224  31.313  61.615  1.00  9.89           C  
-ATOM   1437  O   LEU A 202      88.924  30.988  62.760  1.00 10.95           O  
-ATOM   1438  CB  LEU A 202      88.135  30.480  59.510  1.00  4.47           C  
-ATOM   1439  CG  LEU A 202      87.561  29.136  59.976  1.00 15.83           C  
-ATOM   1440  CD1 LEU A 202      86.193  29.348  60.623  1.00 16.80           C  
-ATOM   1441  CD2 LEU A 202      87.440  28.188  58.789  1.00 29.92           C  
-ATOM   1442  N   ARG A 203      90.480  31.465  61.221  1.00 10.86           N  
-ATOM   1443  CA  ARG A 203      91.594  31.253  62.135  1.00  5.23           C  
-ATOM   1444  C   ARG A 203      91.353  32.106  63.380  1.00  6.20           C  
-ATOM   1445  O   ARG A 203      91.340  31.603  64.497  1.00  4.47           O  
-ATOM   1446  CB  ARG A 203      92.895  31.660  61.442  1.00  5.95           C  
-ATOM   1447  CG  ARG A 203      92.942  31.228  59.964  1.00 25.94           C  
-ATOM   1448  CD  ARG A 203      94.172  31.742  59.194  1.00 42.57           C  
-ATOM   1449  NE  ARG A 203      95.266  30.773  59.161  1.00 49.19           N  
-ATOM   1450  CZ  ARG A 203      96.157  30.605  60.135  1.00 62.02           C  
-ATOM   1451  NH1 ARG A 203      96.104  31.348  61.236  1.00 61.51           N  
-ATOM   1452  NH2 ARG A 203      97.091  29.670  60.019  1.00 70.51           N  
-ATOM   1453  N   ASN A 204      91.133  33.398  63.169  1.00 11.72           N  
-ATOM   1454  CA  ASN A 204      90.887  34.336  64.257  1.00 14.58           C  
-ATOM   1455  C   ASN A 204      89.761  33.875  65.168  1.00 15.67           C  
-ATOM   1456  O   ASN A 204      89.931  33.790  66.382  1.00 19.51           O  
-ATOM   1457  CB  ASN A 204      90.552  35.732  63.704  1.00 16.08           C  
-ATOM   1458  CG  ASN A 204      91.797  36.563  63.391  1.00 22.29           C  
-ATOM   1459  OD1 ASN A 204      91.904  37.190  62.328  1.00 30.37           O  
-ATOM   1460  ND2 ASN A 204      92.733  36.584  64.325  1.00 20.69           N  
-ATOM   1461  N   VAL A 205      88.610  33.571  64.587  1.00 10.13           N  
-ATOM   1462  CA  VAL A 205      87.490  33.154  65.401  1.00  7.50           C  
-ATOM   1463  C   VAL A 205      87.876  32.031  66.330  1.00  4.47           C  
-ATOM   1464  O   VAL A 205      87.711  32.148  67.532  1.00  6.63           O  
-ATOM   1465  CB  VAL A 205      86.309  32.713  64.538  1.00 10.45           C  
-ATOM   1466  CG1 VAL A 205      85.128  32.303  65.423  1.00  4.47           C  
-ATOM   1467  CG2 VAL A 205      85.907  33.843  63.632  1.00 11.39           C  
-ATOM   1468  N   TYR A 206      88.404  30.947  65.784  1.00  4.47           N  
-ATOM   1469  CA  TYR A 206      88.779  29.833  66.630  1.00  4.47           C  
-ATOM   1470  C   TYR A 206      89.661  30.272  67.765  1.00  6.56           C  
-ATOM   1471  O   TYR A 206      89.484  29.824  68.893  1.00 14.61           O  
-ATOM   1472  CB  TYR A 206      89.461  28.736  65.826  1.00 14.48           C  
-ATOM   1473  CG  TYR A 206      88.488  27.663  65.375  1.00 14.52           C  
-ATOM   1474  CD1 TYR A 206      87.854  26.843  66.307  1.00  6.28           C  
-ATOM   1475  CD2 TYR A 206      88.177  27.492  64.020  1.00 14.10           C  
-ATOM   1476  CE1 TYR A 206      86.933  25.879  65.904  1.00 18.25           C  
-ATOM   1477  CE2 TYR A 206      87.260  26.535  63.607  1.00 18.16           C  
-ATOM   1478  CZ  TYR A 206      86.641  25.729  64.551  1.00 26.30           C  
-ATOM   1479  OH  TYR A 206      85.739  24.768  64.141  1.00 31.64           O  
-ATOM   1480  N   ILE A 207      90.618  31.146  67.494  1.00  6.53           N  
-ATOM   1481  CA  ILE A 207      91.451  31.624  68.585  1.00  7.39           C  
-ATOM   1482  C   ILE A 207      90.555  32.253  69.651  1.00  8.22           C  
-ATOM   1483  O   ILE A 207      90.670  31.933  70.831  1.00 11.94           O  
-ATOM   1484  CB  ILE A 207      92.460  32.643  68.105  1.00  7.84           C  
-ATOM   1485  CG1 ILE A 207      93.624  31.908  67.451  1.00 14.94           C  
-ATOM   1486  CG2 ILE A 207      92.931  33.497  69.249  1.00  4.47           C  
-ATOM   1487  CD1 ILE A 207      94.257  30.879  68.350  1.00  6.28           C  
-ATOM   1488  N   MET A 208      89.653  33.138  69.239  1.00  7.02           N  
-ATOM   1489  CA  MET A 208      88.738  33.751  70.195  1.00  5.89           C  
-ATOM   1490  C   MET A 208      88.034  32.668  70.986  1.00  5.50           C  
-ATOM   1491  O   MET A 208      88.049  32.693  72.207  1.00  4.47           O  
-ATOM   1492  CB  MET A 208      87.694  34.608  69.488  1.00 14.09           C  
-ATOM   1493  CG  MET A 208      88.206  35.971  69.043  1.00 22.34           C  
-ATOM   1494  SD  MET A 208      86.949  36.880  68.116  1.00 27.89           S  
-ATOM   1495  CE  MET A 208      87.216  36.252  66.458  1.00 11.66           C  
-ATOM   1496  N   LEU A 209      87.430  31.707  70.289  1.00 17.50           N  
-ATOM   1497  CA  LEU A 209      86.720  30.606  70.954  1.00 17.81           C  
-ATOM   1498  C   LEU A 209      87.524  30.188  72.176  1.00 16.14           C  
-ATOM   1499  O   LEU A 209      87.044  30.271  73.307  1.00 19.61           O  
-ATOM   1500  CB  LEU A 209      86.557  29.394  70.026  1.00 10.49           C  
-ATOM   1501  CG  LEU A 209      85.399  28.416  70.312  1.00  6.48           C  
-ATOM   1502  CD1 LEU A 209      85.645  27.110  69.564  1.00  4.47           C  
-ATOM   1503  CD2 LEU A 209      85.275  28.130  71.789  1.00  4.55           C  
-ATOM   1504  N   ILE A 210      88.750  29.744  71.943  1.00  4.47           N  
-ATOM   1505  CA  ILE A 210      89.598  29.349  73.042  1.00  4.47           C  
-ATOM   1506  C   ILE A 210      89.630  30.434  74.122  1.00  4.47           C  
-ATOM   1507  O   ILE A 210      89.270  30.175  75.267  1.00  4.47           O  
-ATOM   1508  CB  ILE A 210      91.016  29.044  72.543  1.00  6.46           C  
-ATOM   1509  CG1 ILE A 210      90.978  27.812  71.642  1.00  5.15           C  
-ATOM   1510  CG2 ILE A 210      91.942  28.794  73.702  1.00  4.47           C  
-ATOM   1511  CD1 ILE A 210      92.331  27.366  71.164  1.00  6.31           C  
-ATOM   1512  N   ASN A 211      90.030  31.652  73.774  1.00  4.47           N  
-ATOM   1513  CA  ASN A 211      90.076  32.702  74.790  1.00  4.47           C  
-ATOM   1514  C   ASN A 211      88.740  32.790  75.527  1.00  4.47           C  
-ATOM   1515  O   ASN A 211      88.703  33.025  76.727  1.00  6.89           O  
-ATOM   1516  CB  ASN A 211      90.412  34.074  74.182  1.00  5.18           C  
-ATOM   1517  CG  ASN A 211      91.849  34.170  73.692  1.00 19.87           C  
-ATOM   1518  OD1 ASN A 211      92.756  33.576  74.269  1.00 29.97           O  
-ATOM   1519  ND2 ASN A 211      92.065  34.943  72.633  1.00 27.08           N  
-ATOM   1520  N   THR A 212      87.643  32.579  74.812  1.00  4.47           N  
-ATOM   1521  CA  THR A 212      86.319  32.661  75.414  1.00  4.47           C  
-ATOM   1522  C   THR A 212      86.096  31.584  76.456  1.00  6.15           C  
-ATOM   1523  O   THR A 212      85.506  31.821  77.503  1.00  4.47           O  
-ATOM   1524  CB  THR A 212      85.211  32.497  74.372  1.00  4.47           C  
-ATOM   1525  OG1 THR A 212      85.407  33.424  73.301  1.00 10.27           O  
-ATOM   1526  CG2 THR A 212      83.857  32.748  75.011  1.00  4.47           C  
-ATOM   1527  N   ILE A 213      86.543  30.379  76.148  1.00 14.00           N  
-ATOM   1528  CA  ILE A 213      86.366  29.277  77.072  1.00 10.55           C  
-ATOM   1529  C   ILE A 213      87.115  29.617  78.352  1.00 17.47           C  
-ATOM   1530  O   ILE A 213      86.529  29.607  79.428  1.00 20.98           O  
-ATOM   1531  CB  ILE A 213      86.899  27.955  76.479  1.00  4.96           C  
-ATOM   1532  CG1 ILE A 213      86.282  27.711  75.105  1.00  4.47           C  
-ATOM   1533  CG2 ILE A 213      86.529  26.808  77.365  1.00  4.47           C  
-ATOM   1534  CD1 ILE A 213      86.758  26.443  74.449  1.00 12.27           C  
-ATOM   1535  N   ILE A 214      88.405  29.936  78.236  1.00 17.28           N  
-ATOM   1536  CA  ILE A 214      89.213  30.275  79.405  1.00  7.42           C  
-ATOM   1537  C   ILE A 214      88.542  31.409  80.159  1.00 10.54           C  
-ATOM   1538  O   ILE A 214      88.266  31.296  81.351  1.00 10.98           O  
-ATOM   1539  CB  ILE A 214      90.595  30.742  79.002  1.00  4.76           C  
-ATOM   1540  CG1 ILE A 214      91.304  29.658  78.195  1.00  4.47           C  
-ATOM   1541  CG2 ILE A 214      91.386  31.065  80.222  1.00  6.77           C  
-ATOM   1542  CD1 ILE A 214      92.613  30.144  77.548  1.00 13.16           C  
-ATOM   1543  N   PHE A 215      88.289  32.505  79.448  1.00 12.78           N  
-ATOM   1544  CA  PHE A 215      87.622  33.682  80.014  1.00 12.75           C  
-ATOM   1545  C   PHE A 215      86.426  33.263  80.873  1.00  9.53           C  
-ATOM   1546  O   PHE A 215      86.327  33.600  82.049  1.00  6.17           O  
-ATOM   1547  CB  PHE A 215      87.149  34.604  78.871  1.00  5.75           C  
-ATOM   1548  CG  PHE A 215      86.419  35.836  79.335  1.00  9.43           C  
-ATOM   1549  CD1 PHE A 215      85.066  35.782  79.673  1.00  4.47           C  
-ATOM   1550  CD2 PHE A 215      87.093  37.050  79.454  1.00 22.07           C  
-ATOM   1551  CE1 PHE A 215      84.389  36.912  80.127  1.00  4.47           C  
-ATOM   1552  CE2 PHE A 215      86.430  38.187  79.907  1.00 31.78           C  
-ATOM   1553  CZ  PHE A 215      85.069  38.117  80.246  1.00 23.65           C  
-ATOM   1554  N   LEU A 216      85.526  32.514  80.257  1.00 11.20           N  
-ATOM   1555  CA  LEU A 216      84.316  32.032  80.902  1.00  8.54           C  
-ATOM   1556  C   LEU A 216      84.572  31.196  82.147  1.00 11.45           C  
-ATOM   1557  O   LEU A 216      83.682  31.052  82.979  1.00 11.88           O  
-ATOM   1558  CB  LEU A 216      83.519  31.208  79.895  1.00  8.08           C  
-ATOM   1559  CG  LEU A 216      82.210  31.717  79.297  1.00  6.14           C  
-ATOM   1560  CD1 LEU A 216      82.197  33.219  79.211  1.00 11.12           C  
-ATOM   1561  CD2 LEU A 216      82.052  31.096  77.908  1.00 14.51           C  
-ATOM   1562  N   LYS A 217      85.773  30.634  82.269  1.00 16.49           N  
-ATOM   1563  CA  LYS A 217      86.109  29.796  83.420  1.00 16.78           C  
-ATOM   1564  C   LYS A 217      86.063  30.587  84.707  1.00 21.84           C  
-ATOM   1565  O   LYS A 217      85.650  30.074  85.736  1.00 24.45           O  
-ATOM   1566  CB  LYS A 217      87.505  29.183  83.260  1.00 12.35           C  
-ATOM   1567  CG  LYS A 217      87.557  27.933  82.401  1.00 16.06           C  
-ATOM   1568  CD  LYS A 217      86.768  26.811  83.058  1.00 27.46           C  
-ATOM   1569  CE  LYS A 217      87.037  25.466  82.402  1.00 32.19           C  
-ATOM   1570  NZ  LYS A 217      86.742  25.505  80.953  1.00 33.56           N  
-ATOM   1571  N   THR A 218      86.475  31.848  84.633  1.00 30.78           N  
-ATOM   1572  CA  THR A 218      86.521  32.725  85.796  1.00 23.80           C  
-ATOM   1573  C   THR A 218      85.399  33.744  85.884  1.00 23.40           C  
-ATOM   1574  O   THR A 218      84.681  33.788  86.871  1.00 22.59           O  
-ATOM   1575  CB  THR A 218      87.815  33.508  85.820  1.00 25.97           C  
-ATOM   1576  OG1 THR A 218      88.894  32.671  85.381  1.00 25.73           O  
-ATOM   1577  CG2 THR A 218      88.074  34.009  87.226  1.00 42.10           C  
-ATOM   1578  N   ASN A 219      85.260  34.562  84.841  1.00 26.24           N  
-ATOM   1579  CA  ASN A 219      84.246  35.621  84.781  1.00 27.39           C  
-ATOM   1580  C   ASN A 219      82.967  35.271  84.017  1.00 30.56           C  
-ATOM   1581  O   ASN A 219      82.934  34.329  83.232  1.00 35.73           O  
-ATOM   1582  CB  ASN A 219      84.863  36.855  84.147  1.00 27.97           C  
-ATOM   1583  CG  ASN A 219      86.364  36.851  84.252  1.00 48.21           C  
-ATOM   1584  OD1 ASN A 219      86.919  36.873  85.356  1.00 60.50           O  
-ATOM   1585  ND2 ASN A 219      87.039  36.803  83.107  1.00 47.88           N  
-ATOM   1586  N   ASN A 220      81.918  36.053  84.252  1.00 33.21           N  
-ATOM   1587  CA  ASN A 220      80.621  35.876  83.598  1.00 33.70           C  
-ATOM   1588  C   ASN A 220      80.655  36.649  82.276  1.00 36.04           C  
-ATOM   1589  O   ASN A 220      81.459  37.563  82.125  1.00 47.22           O  
-ATOM   1590  CB  ASN A 220      79.529  36.450  84.496  1.00 47.61           C  
-ATOM   1591  CG  ASN A 220      78.155  36.299  83.907  1.00 62.83           C  
-ATOM   1592  OD1 ASN A 220      77.323  37.214  83.993  1.00 68.62           O  
-ATOM   1593  ND2 ASN A 220      77.893  35.135  83.315  1.00 65.61           N  
-ATOM   1594  N   TRP A 221      79.790  36.319  81.320  1.00 36.49           N  
-ATOM   1595  CA  TRP A 221      79.820  37.036  80.041  1.00 38.75           C  
-ATOM   1596  C   TRP A 221      79.539  38.521  80.206  1.00 45.84           C  
-ATOM   1597  O   TRP A 221      80.007  39.339  79.414  1.00 49.59           O  
-ATOM   1598  CB  TRP A 221      78.824  36.462  79.023  1.00 27.73           C  
-ATOM   1599  CG  TRP A 221      77.383  36.707  79.337  1.00 18.49           C  
-ATOM   1600  CD1 TRP A 221      76.580  35.947  80.131  1.00 25.06           C  
-ATOM   1601  CD2 TRP A 221      76.571  37.785  78.863  1.00 16.22           C  
-ATOM   1602  NE1 TRP A 221      75.315  36.479  80.182  1.00 20.80           N  
-ATOM   1603  CE2 TRP A 221      75.283  37.610  79.413  1.00 15.91           C  
-ATOM   1604  CE3 TRP A 221      76.806  38.884  78.027  1.00 21.66           C  
-ATOM   1605  CZ2 TRP A 221      74.230  38.494  79.156  1.00 18.65           C  
-ATOM   1606  CZ3 TRP A 221      75.755  39.767  77.769  1.00 16.24           C  
-ATOM   1607  CH2 TRP A 221      74.484  39.563  78.334  1.00 16.47           C  
-ATOM   1608  N   HIS A 222      78.786  38.873  81.241  1.00 50.24           N  
-ATOM   1609  CA  HIS A 222      78.452  40.270  81.474  1.00 55.22           C  
-ATOM   1610  C   HIS A 222      79.589  41.048  82.134  1.00 54.16           C  
-ATOM   1611  O   HIS A 222      79.339  41.973  82.903  1.00 63.11           O  
-ATOM   1612  CB  HIS A 222      77.199  40.372  82.345  1.00 66.40           C  
-ATOM   1613  CG  HIS A 222      76.328  41.538  82.000  1.00 81.84           C  
-ATOM   1614  ND1 HIS A 222      76.837  42.786  81.703  1.00 83.46           N  
-ATOM   1615  CD2 HIS A 222      74.982  41.646  81.891  1.00 90.05           C  
-ATOM   1616  CE1 HIS A 222      75.843  43.610  81.424  1.00 84.25           C  
-ATOM   1617  NE2 HIS A 222      74.706  42.944  81.531  1.00 90.53           N  
-ATOM   1618  N   ALA A 223      80.834  40.678  81.846  1.00 46.00           N  
-ATOM   1619  CA  ALA A 223      81.973  41.371  82.433  1.00 38.38           C  
-ATOM   1620  C   ALA A 223      82.037  42.786  81.871  1.00 41.20           C  
-ATOM   1621  O   ALA A 223      81.127  43.602  82.063  1.00 38.41           O  
-ATOM   1622  CB  ALA A 223      83.264  40.626  82.125  1.00 23.67           C  
-ATOM   1623  N   GLY A 224      83.121  43.076  81.170  1.00 44.93           N  
-ATOM   1624  CA  GLY A 224      83.272  44.393  80.592  1.00 45.57           C  
-ATOM   1625  C   GLY A 224      82.387  44.545  79.380  1.00 42.13           C  
-ATOM   1626  O   GLY A 224      82.792  45.151  78.390  1.00 47.05           O  
-ATOM   1627  N   TRP A 225      81.180  43.992  79.452  1.00 37.47           N  
-ATOM   1628  CA  TRP A 225      80.257  44.084  78.333  1.00 35.12           C  
-ATOM   1629  C   TRP A 225      80.014  45.543  77.995  1.00 38.13           C  
-ATOM   1630  O   TRP A 225      80.069  45.945  76.829  1.00 40.48           O  
-ATOM   1631  CB  TRP A 225      78.932  43.399  78.672  1.00 33.99           C  
-ATOM   1632  CG  TRP A 225      77.884  43.486  77.562  1.00 34.92           C  
-ATOM   1633  CD1 TRP A 225      76.807  44.330  77.511  1.00 36.44           C  
-ATOM   1634  CD2 TRP A 225      77.823  42.695  76.361  1.00 28.38           C  
-ATOM   1635  NE1 TRP A 225      76.084  44.113  76.362  1.00 30.80           N  
-ATOM   1636  CE2 TRP A 225      76.685  43.116  75.639  1.00 24.65           C  
-ATOM   1637  CE3 TRP A 225      78.619  41.670  75.829  1.00 26.42           C  
-ATOM   1638  CZ2 TRP A 225      76.326  42.551  74.414  1.00 23.10           C  
-ATOM   1639  CZ3 TRP A 225      78.261  41.108  74.612  1.00 25.80           C  
-ATOM   1640  CH2 TRP A 225      77.124  41.552  73.917  1.00 26.93           C  
-ATOM   1641  N   ASN A 226      79.764  46.343  79.022  1.00 36.14           N  
-ATOM   1642  CA  ASN A 226      79.503  47.750  78.805  1.00 31.82           C  
-ATOM   1643  C   ASN A 226      80.794  48.496  78.509  1.00 27.70           C  
-ATOM   1644  O   ASN A 226      80.820  49.723  78.484  1.00 36.96           O  
-ATOM   1645  CB  ASN A 226      78.788  48.336  80.025  1.00 39.43           C  
-ATOM   1646  CG  ASN A 226      77.411  47.728  80.237  1.00 50.47           C  
-ATOM   1647  OD1 ASN A 226      76.524  47.860  79.390  1.00 52.57           O  
-ATOM   1648  ND2 ASN A 226      77.228  47.049  81.367  1.00 60.73           N  
-ATOM   1649  N   THR A 227      81.865  47.751  78.273  1.00 18.05           N  
-ATOM   1650  CA  THR A 227      83.155  48.356  77.971  1.00 22.55           C  
-ATOM   1651  C   THR A 227      83.608  47.801  76.645  1.00 20.43           C  
-ATOM   1652  O   THR A 227      84.687  48.119  76.144  1.00 23.22           O  
-ATOM   1653  CB  THR A 227      84.211  48.008  79.027  1.00 30.27           C  
-ATOM   1654  OG1 THR A 227      84.690  46.674  78.811  1.00 31.72           O  
-ATOM   1655  CG2 THR A 227      83.614  48.119  80.423  1.00 34.99           C  
-ATOM   1656  N   LEU A 228      82.758  46.952  76.087  1.00 22.81           N  
-ATOM   1657  CA  LEU A 228      83.010  46.315  74.803  1.00 18.77           C  
-ATOM   1658  C   LEU A 228      82.440  47.179  73.696  1.00 16.57           C  
-ATOM   1659  O   LEU A 228      81.228  47.383  73.629  1.00 15.70           O  
-ATOM   1660  CB  LEU A 228      82.319  44.962  74.751  1.00 13.85           C  
-ATOM   1661  CG  LEU A 228      83.219  43.744  74.734  1.00 17.40           C  
-ATOM   1662  CD1 LEU A 228      82.343  42.514  74.647  1.00 27.51           C  
-ATOM   1663  CD2 LEU A 228      84.180  43.815  73.558  1.00 27.76           C  
-ATOM   1664  N   SER A 229      83.295  47.694  72.827  1.00 10.80           N  
-ATOM   1665  CA  SER A 229      82.780  48.512  71.747  1.00 20.52           C  
-ATOM   1666  C   SER A 229      81.962  47.588  70.872  1.00 19.00           C  
-ATOM   1667  O   SER A 229      82.288  46.407  70.739  1.00 20.91           O  
-ATOM   1668  CB  SER A 229      83.921  49.132  70.943  1.00 28.19           C  
-ATOM   1669  OG  SER A 229      84.835  48.138  70.522  1.00 33.90           O  
-ATOM   1670  N   PHE A 230      80.890  48.108  70.290  1.00 16.78           N  
-ATOM   1671  CA  PHE A 230      80.075  47.271  69.434  1.00 18.76           C  
-ATOM   1672  C   PHE A 230      80.923  46.734  68.295  1.00 20.35           C  
-ATOM   1673  O   PHE A 230      82.035  47.201  68.077  1.00 27.83           O  
-ATOM   1674  CB  PHE A 230      78.895  48.057  68.885  1.00 10.57           C  
-ATOM   1675  CG  PHE A 230      77.790  48.226  69.866  1.00  4.47           C  
-ATOM   1676  CD1 PHE A 230      77.711  49.346  70.646  1.00  4.47           C  
-ATOM   1677  CD2 PHE A 230      76.827  47.237  70.017  1.00 17.25           C  
-ATOM   1678  CE1 PHE A 230      76.689  49.491  71.564  1.00  4.75           C  
-ATOM   1679  CE2 PHE A 230      75.799  47.373  70.940  1.00 15.35           C  
-ATOM   1680  CZ  PHE A 230      75.732  48.505  71.713  1.00  4.47           C  
-ATOM   1681  N   CYS A 231      80.409  45.742  67.578  1.00 17.54           N  
-ATOM   1682  CA  CYS A 231      81.154  45.172  66.473  1.00 15.52           C  
-ATOM   1683  C   CYS A 231      80.946  46.057  65.258  1.00 21.56           C  
-ATOM   1684  O   CYS A 231      79.819  46.217  64.783  1.00 28.43           O  
-ATOM   1685  CB  CYS A 231      80.668  43.760  66.185  1.00 10.71           C  
-ATOM   1686  SG  CYS A 231      81.624  42.945  64.908  1.00 37.43           S  
-ATOM   1687  N   ASN A 232      82.035  46.630  64.756  1.00 19.51           N  
-ATOM   1688  CA  ASN A 232      81.962  47.524  63.606  1.00 28.60           C  
-ATOM   1689  C   ASN A 232      82.718  47.002  62.385  1.00 25.86           C  
-ATOM   1690  O   ASN A 232      83.444  46.022  62.471  1.00 29.31           O  
-ATOM   1691  CB  ASN A 232      82.523  48.874  64.005  1.00 38.89           C  
-ATOM   1692  CG  ASN A 232      83.945  48.770  64.455  1.00 45.08           C  
-ATOM   1693  OD1 ASN A 232      84.822  48.432  63.668  1.00 53.81           O  
-ATOM   1694  ND2 ASN A 232      84.187  49.035  65.731  1.00 53.33           N  
-ATOM   1695  N   ASP A 233      82.555  47.675  61.249  1.00 27.71           N  
-ATOM   1696  CA  ASP A 233      83.213  47.257  60.015  1.00 31.30           C  
-ATOM   1697  C   ASP A 233      84.709  47.376  60.120  1.00 25.12           C  
-ATOM   1698  O   ASP A 233      85.439  46.666  59.449  1.00 32.61           O  
-ATOM   1699  CB  ASP A 233      82.728  48.084  58.820  1.00 40.64           C  
-ATOM   1700  CG  ASP A 233      81.239  47.911  58.552  1.00 63.23           C  
-ATOM   1701  OD1 ASP A 233      80.425  48.308  59.421  1.00 71.81           O  
-ATOM   1702  OD2 ASP A 233      80.883  47.372  57.476  1.00 71.38           O  
-ATOM   1703  N   VAL A 234      85.169  48.286  60.959  1.00 24.69           N  
-ATOM   1704  CA  VAL A 234      86.595  48.473  61.129  1.00 28.98           C  
-ATOM   1705  C   VAL A 234      87.144  47.216  61.767  1.00 29.59           C  
-ATOM   1706  O   VAL A 234      88.182  46.701  61.372  1.00 42.28           O  
-ATOM   1707  CB  VAL A 234      86.896  49.649  62.057  1.00 30.29           C  
-ATOM   1708  CG1 VAL A 234      88.402  49.827  62.185  1.00 26.37           C  
-ATOM   1709  CG2 VAL A 234      86.202  50.911  61.541  1.00 33.62           C  
-ATOM   1710  N   PHE A 235      86.435  46.731  62.770  1.00 24.39           N  
-ATOM   1711  CA  PHE A 235      86.841  45.536  63.477  1.00 22.20           C  
-ATOM   1712  C   PHE A 235      86.890  44.388  62.479  1.00 23.65           C  
-ATOM   1713  O   PHE A 235      87.913  43.724  62.341  1.00 29.97           O  
-ATOM   1714  CB  PHE A 235      85.827  45.229  64.585  1.00 30.82           C  
-ATOM   1715  CG  PHE A 235      86.164  44.019  65.413  1.00 28.19           C  
-ATOM   1716  CD1 PHE A 235      85.157  43.290  66.036  1.00 30.61           C  
-ATOM   1717  CD2 PHE A 235      87.483  43.621  65.592  1.00 30.24           C  
-ATOM   1718  CE1 PHE A 235      85.462  42.185  66.824  1.00 28.44           C  
-ATOM   1719  CE2 PHE A 235      87.795  42.515  66.381  1.00 21.80           C  
-ATOM   1720  CZ  PHE A 235      86.786  41.800  66.995  1.00 24.00           C  
-ATOM   1721  N   LYS A 236      85.783  44.168  61.773  1.00 18.75           N  
-ATOM   1722  CA  LYS A 236      85.704  43.081  60.809  1.00 14.69           C  
-ATOM   1723  C   LYS A 236      86.837  43.140  59.808  1.00 17.22           C  
-ATOM   1724  O   LYS A 236      87.349  42.107  59.393  1.00 17.85           O  
-ATOM   1725  CB  LYS A 236      84.370  43.115  60.077  1.00 12.63           C  
-ATOM   1726  CG  LYS A 236      83.144  42.955  60.974  1.00 17.39           C  
-ATOM   1727  CD  LYS A 236      81.880  42.898  60.121  1.00 28.38           C  
-ATOM   1728  CE  LYS A 236      80.605  42.941  60.949  1.00 29.53           C  
-ATOM   1729  NZ  LYS A 236      79.412  42.994  60.048  1.00 37.17           N  
-ATOM   1730  N   GLN A 237      87.223  44.352  59.421  1.00 23.19           N  
-ATOM   1731  CA  GLN A 237      88.319  44.555  58.472  1.00 29.36           C  
-ATOM   1732  C   GLN A 237      89.629  43.963  58.981  1.00 31.56           C  
-ATOM   1733  O   GLN A 237      90.331  43.286  58.245  1.00 33.19           O  
-ATOM   1734  CB  GLN A 237      88.527  46.046  58.194  1.00 41.18           C  
-ATOM   1735  CG  GLN A 237      87.506  46.645  57.255  1.00 54.61           C  
-ATOM   1736  CD  GLN A 237      87.473  45.925  55.923  1.00 61.69           C  
-ATOM   1737  OE1 GLN A 237      88.496  45.795  55.244  1.00 62.15           O  
-ATOM   1738  NE2 GLN A 237      86.293  45.450  55.542  1.00 66.46           N  
-ATOM   1739  N   LYS A 238      89.972  44.225  60.236  1.00 33.35           N  
-ATOM   1740  CA  LYS A 238      91.204  43.682  60.786  1.00 34.51           C  
-ATOM   1741  C   LYS A 238      91.144  42.165  60.758  1.00 31.37           C  
-ATOM   1742  O   LYS A 238      92.092  41.503  60.341  1.00 38.50           O  
-ATOM   1743  CB  LYS A 238      91.415  44.150  62.231  1.00 44.23           C  
-ATOM   1744  CG  LYS A 238      91.735  45.637  62.397  1.00 60.82           C  
-ATOM   1745  CD  LYS A 238      91.974  45.986  63.872  1.00 69.57           C  
-ATOM   1746  CE  LYS A 238      92.148  47.492  64.101  1.00 68.48           C  
-ATOM   1747  NZ  LYS A 238      92.251  47.830  65.555  1.00 65.19           N  
-ATOM   1748  N   LEU A 239      90.015  41.620  61.193  1.00 22.76           N  
-ATOM   1749  CA  LEU A 239      89.833  40.180  61.240  1.00 16.16           C  
-ATOM   1750  C   LEU A 239      90.026  39.478  59.899  1.00 21.22           C  
-ATOM   1751  O   LEU A 239      90.297  38.280  59.861  1.00 24.11           O  
-ATOM   1752  CB  LEU A 239      88.450  39.858  61.807  1.00 11.71           C  
-ATOM   1753  CG  LEU A 239      88.237  40.259  63.270  1.00  9.43           C  
-ATOM   1754  CD1 LEU A 239      86.837  39.902  63.722  1.00 19.47           C  
-ATOM   1755  CD2 LEU A 239      89.237  39.552  64.134  1.00  4.47           C  
-ATOM   1756  N   GLN A 240      89.888  40.217  58.800  1.00 25.75           N  
-ATOM   1757  CA  GLN A 240      90.053  39.640  57.462  1.00 30.11           C  
-ATOM   1758  C   GLN A 240      91.458  39.839  56.918  1.00 38.63           C  
-ATOM   1759  O   GLN A 240      91.787  39.319  55.852  1.00 45.60           O  
-ATOM   1760  CB  GLN A 240      89.062  40.270  56.473  1.00 21.51           C  
-ATOM   1761  CG  GLN A 240      87.614  39.905  56.733  1.00 32.70           C  
-ATOM   1762  CD  GLN A 240      86.629  40.756  55.954  1.00 38.52           C  
-ATOM   1763  OE1 GLN A 240      86.663  40.819  54.714  1.00 39.90           O  
-ATOM   1764  NE2 GLN A 240      85.735  41.417  56.683  1.00 39.76           N  
-ATOM   1765  N   LYS A 241      92.291  40.575  57.651  1.00 42.78           N  
-ATOM   1766  CA  LYS A 241      93.630  40.869  57.171  1.00 42.54           C  
-ATOM   1767  C   LYS A 241      94.813  40.421  58.001  1.00 42.07           C  
-ATOM   1768  O   LYS A 241      95.669  39.691  57.517  1.00 38.52           O  
-ATOM   1769  CB  LYS A 241      93.766  42.383  56.917  1.00 44.75           C  
-ATOM   1770  CG  LYS A 241      92.921  42.920  55.750  1.00 60.26           C  
-ATOM   1771  CD  LYS A 241      93.077  44.434  55.571  1.00 66.27           C  
-ATOM   1772  CE  LYS A 241      92.243  44.958  54.402  1.00 66.62           C  
-ATOM   1773  NZ  LYS A 241      92.655  44.354  53.101  1.00 64.97           N  
-ATOM   1774  N   SER A 242      94.863  40.846  59.253  1.00 49.72           N  
-ATOM   1775  CA  SER A 242      96.022  40.544  60.082  1.00 57.83           C  
-ATOM   1776  C   SER A 242      96.080  39.331  60.997  1.00 56.87           C  
-ATOM   1777  O   SER A 242      97.139  39.058  61.558  1.00 63.12           O  
-ATOM   1778  CB  SER A 242      96.391  41.792  60.906  1.00 69.84           C  
-ATOM   1779  OG  SER A 242      95.312  42.241  61.715  1.00 80.29           O  
-ATOM   1780  N   GLU A 243      94.993  38.589  61.162  1.00 53.78           N  
-ATOM   1781  CA  GLU A 243      95.068  37.446  62.066  1.00 53.03           C  
-ATOM   1782  C   GLU A 243      95.519  38.007  63.407  1.00 45.60           C  
-ATOM   1783  O   GLU A 243      96.381  37.441  64.070  1.00 38.52           O  
-ATOM   1784  CB  GLU A 243      96.114  36.434  61.580  1.00 66.85           C  
-ATOM   1785  CG  GLU A 243      96.313  35.224  62.509  1.00 80.28           C  
-ATOM   1786  CD  GLU A 243      97.682  34.555  62.357  1.00 87.62           C  
-ATOM   1787  OE1 GLU A 243      98.054  34.177  61.222  1.00 92.21           O  
-ATOM   1788  OE2 GLU A 243      98.385  34.401  63.382  1.00 86.08           O  
-ATOM   1789  N   CYS A 244      94.949  39.144  63.782  1.00 43.92           N  
-ATOM   1790  CA  CYS A 244      95.289  39.791  65.040  1.00 47.80           C  
-ATOM   1791  C   CYS A 244      95.011  38.904  66.253  1.00 46.57           C  
-ATOM   1792  O   CYS A 244      95.907  38.204  66.715  1.00 53.00           O  
-ATOM   1793  CB  CYS A 244      94.528  41.110  65.156  1.00 56.79           C  
-ATOM   1794  SG  CYS A 244      92.865  41.049  64.472  1.00 62.17           S  
-ATOM   1795  N   ILE A 245      93.778  38.939  66.762  1.00 39.54           N  
-ATOM   1796  CA  ILE A 245      93.359  38.139  67.925  1.00 31.94           C  
-ATOM   1797  C   ILE A 245      94.415  37.153  68.430  1.00 27.12           C  
-ATOM   1798  O   ILE A 245      94.558  36.055  67.902  1.00 19.77           O  
-ATOM   1799  CB  ILE A 245      92.080  37.328  67.611  1.00 30.93           C  
-ATOM   1800  CG1 ILE A 245      90.999  38.252  67.071  1.00 32.67           C  
-ATOM   1801  CG2 ILE A 245      91.564  36.652  68.865  1.00 27.10           C  
-ATOM   1802  CD1 ILE A 245      90.620  39.356  68.024  1.00 32.04           C  
-ATOM   1803  N   LYS A 246      95.152  37.540  69.461  1.00 29.60           N  
-ATOM   1804  CA  LYS A 246      96.188  36.665  69.992  1.00 33.17           C  
-ATOM   1805  C   LYS A 246      95.778  35.875  71.226  1.00 29.21           C  
-ATOM   1806  O   LYS A 246      95.141  36.384  72.142  1.00 27.27           O  
-ATOM   1807  CB  LYS A 246      97.468  37.462  70.259  1.00 37.43           C  
-ATOM   1808  CG  LYS A 246      98.256  37.759  68.979  1.00 53.13           C  
-ATOM   1809  CD  LYS A 246      99.464  38.662  69.222  1.00 62.53           C  
-ATOM   1810  CE  LYS A 246     100.160  39.017  67.910  1.00 68.24           C  
-ATOM   1811  NZ  LYS A 246     101.191  40.092  68.076  1.00 65.54           N  
-ATOM   1812  N   LEU A 247      96.146  34.605  71.221  1.00 27.79           N  
-ATOM   1813  CA  LEU A 247      95.824  33.687  72.297  1.00 25.77           C  
-ATOM   1814  C   LEU A 247      96.594  34.143  73.509  1.00 27.13           C  
-ATOM   1815  O   LEU A 247      97.815  34.245  73.449  1.00 34.10           O  
-ATOM   1816  CB  LEU A 247      96.254  32.279  71.879  1.00 29.82           C  
-ATOM   1817  CG  LEU A 247      95.662  31.065  72.587  1.00 27.33           C  
-ATOM   1818  CD1 LEU A 247      96.088  29.794  71.876  1.00 17.54           C  
-ATOM   1819  CD2 LEU A 247      96.118  31.062  74.027  1.00 39.52           C  
-ATOM   1820  N   ARG A 248      95.904  34.410  74.612  1.00 27.13           N  
-ATOM   1821  CA  ARG A 248      96.610  34.886  75.799  1.00 36.76           C  
-ATOM   1822  C   ARG A 248      96.250  34.314  77.169  1.00 38.28           C  
-ATOM   1823  O   ARG A 248      95.084  34.087  77.479  1.00 31.75           O  
-ATOM   1824  CB  ARG A 248      96.545  36.413  75.856  1.00 42.46           C  
-ATOM   1825  CG  ARG A 248      95.186  37.000  75.562  1.00 48.76           C  
-ATOM   1826  CD  ARG A 248      95.258  38.520  75.557  1.00 53.31           C  
-ATOM   1827  NE  ARG A 248      96.240  39.016  74.596  1.00 59.52           N  
-ATOM   1828  CZ  ARG A 248      96.590  40.294  74.473  1.00 68.71           C  
-ATOM   1829  NH1 ARG A 248      96.036  41.214  75.255  1.00 69.42           N  
-ATOM   1830  NH2 ARG A 248      97.496  40.654  73.568  1.00 72.24           N  
-ATOM   1831  N   GLU A 249      97.296  34.125  77.980  1.00 42.98           N  
-ATOM   1832  CA  GLU A 249      97.243  33.568  79.331  1.00 40.61           C  
-ATOM   1833  C   GLU A 249      95.974  33.872  80.087  1.00 38.11           C  
-ATOM   1834  O   GLU A 249      95.247  32.970  80.476  1.00 30.30           O  
-ATOM   1835  CB  GLU A 249      98.442  34.059  80.127  1.00 55.50           C  
-ATOM   1836  CG  GLU A 249      99.783  33.626  79.547  1.00 77.27           C  
-ATOM   1837  CD  GLU A 249     100.102  32.152  79.793  1.00 88.61           C  
-ATOM   1838  OE1 GLU A 249      99.331  31.278  79.342  1.00 91.50           O  
-ATOM   1839  OE2 GLU A 249     101.136  31.864  80.437  1.00 96.26           O  
-ATOM   1840  N   VAL A 250      95.725  35.147  80.338  1.00 47.95           N  
-ATOM   1841  CA  VAL A 250      94.496  35.534  81.014  1.00 51.86           C  
-ATOM   1842  C   VAL A 250      93.746  36.445  80.073  1.00 51.67           C  
-ATOM   1843  O   VAL A 250      94.039  37.639  79.962  1.00 53.47           O  
-ATOM   1844  CB  VAL A 250      94.735  36.265  82.330  1.00 54.80           C  
-ATOM   1845  CG1 VAL A 250      93.448  36.953  82.773  1.00 56.87           C  
-ATOM   1846  CG2 VAL A 250      95.154  35.266  83.396  1.00 55.44           C  
-ATOM   1847  N   PRO A 251      92.761  35.876  79.375  1.00 44.92           N  
-ATOM   1848  CA  PRO A 251      91.916  36.558  78.409  1.00 41.13           C  
-ATOM   1849  C   PRO A 251      90.994  37.584  79.038  1.00 35.10           C  
-ATOM   1850  O   PRO A 251      90.562  37.442  80.181  1.00 30.83           O  
-ATOM   1851  CB  PRO A 251      91.157  35.407  77.775  1.00 44.58           C  
-ATOM   1852  CG  PRO A 251      90.953  34.500  78.928  1.00 42.82           C  
-ATOM   1853  CD  PRO A 251      92.319  34.484  79.549  1.00 46.17           C  
-ATOM   1854  N   GLY A 252      90.710  38.625  78.268  1.00 29.26           N  
-ATOM   1855  CA  GLY A 252      89.821  39.670  78.722  1.00 27.86           C  
-ATOM   1856  C   GLY A 252      88.653  39.702  77.761  1.00 25.36           C  
-ATOM   1857  O   GLY A 252      88.762  39.201  76.640  1.00 32.87           O  
-ATOM   1858  N   ILE A 253      87.547  40.305  78.178  1.00 15.06           N  
-ATOM   1859  CA  ILE A 253      86.359  40.363  77.342  1.00 12.32           C  
-ATOM   1860  C   ILE A 253      86.624  40.639  75.860  1.00 18.56           C  
-ATOM   1861  O   ILE A 253      86.011  40.012  75.001  1.00 26.11           O  
-ATOM   1862  CB  ILE A 253      85.364  41.401  77.885  1.00  7.02           C  
-ATOM   1863  CG1 ILE A 253      83.988  40.760  78.058  1.00  4.47           C  
-ATOM   1864  CG2 ILE A 253      85.283  42.591  76.953  1.00 10.93           C  
-ATOM   1865  CD1 ILE A 253      83.441  40.148  76.797  1.00  4.50           C  
-ATOM   1866  N   GLU A 254      87.539  41.550  75.549  1.00 14.99           N  
-ATOM   1867  CA  GLU A 254      87.815  41.869  74.150  1.00 21.80           C  
-ATOM   1868  C   GLU A 254      88.649  40.847  73.369  1.00 21.15           C  
-ATOM   1869  O   GLU A 254      88.901  41.020  72.171  1.00 18.98           O  
-ATOM   1870  CB  GLU A 254      88.483  43.245  74.038  1.00 32.71           C  
-ATOM   1871  CG  GLU A 254      89.731  43.428  74.881  1.00 44.06           C  
-ATOM   1872  CD  GLU A 254      89.415  43.872  76.294  1.00 60.58           C  
-ATOM   1873  OE1 GLU A 254      88.813  44.959  76.454  1.00 67.33           O  
-ATOM   1874  OE2 GLU A 254      89.768  43.141  77.244  1.00 69.87           O  
-ATOM   1875  N   ASP A 255      89.089  39.788  74.031  1.00 17.17           N  
-ATOM   1876  CA  ASP A 255      89.894  38.791  73.338  1.00 24.00           C  
-ATOM   1877  C   ASP A 255      89.045  37.571  73.053  1.00 22.04           C  
-ATOM   1878  O   ASP A 255      89.521  36.589  72.488  1.00 21.71           O  
-ATOM   1879  CB  ASP A 255      91.099  38.382  74.182  1.00 37.40           C  
-ATOM   1880  CG  ASP A 255      92.048  39.538  74.455  1.00 51.55           C  
-ATOM   1881  OD1 ASP A 255      92.555  40.138  73.473  1.00 53.90           O  
-ATOM   1882  OD2 ASP A 255      92.288  39.834  75.655  1.00 44.00           O  
-ATOM   1883  N   THR A 256      87.778  37.655  73.434  1.00 17.47           N  
-ATOM   1884  CA  THR A 256      86.836  36.568  73.241  1.00 18.49           C  
-ATOM   1885  C   THR A 256      85.926  36.685  72.005  1.00 25.64           C  
-ATOM   1886  O   THR A 256      86.201  37.425  71.056  1.00 24.19           O  
-ATOM   1887  CB  THR A 256      85.927  36.454  74.443  1.00 12.02           C  
-ATOM   1888  OG1 THR A 256      84.969  37.520  74.408  1.00 14.05           O  
-ATOM   1889  CG2 THR A 256      86.733  36.550  75.711  1.00 18.24           C  
-ATOM   1890  N   LEU A 257      84.833  35.925  72.046  1.00 27.86           N  
-ATOM   1891  CA  LEU A 257      83.837  35.896  70.984  1.00 17.81           C  
-ATOM   1892  C   LEU A 257      82.754  36.895  71.321  1.00 11.89           C  
-ATOM   1893  O   LEU A 257      81.936  37.254  70.474  1.00 12.81           O  
-ATOM   1894  CB  LEU A 257      83.199  34.513  70.882  1.00 12.74           C  
-ATOM   1895  CG  LEU A 257      84.025  33.378  70.303  1.00  6.78           C  
-ATOM   1896  CD1 LEU A 257      83.192  32.106  70.334  1.00  4.47           C  
-ATOM   1897  CD2 LEU A 257      84.437  33.725  68.885  1.00  7.92           C  
-ATOM   1898  N   PHE A 258      82.735  37.320  72.574  1.00  4.47           N  
-ATOM   1899  CA  PHE A 258      81.741  38.273  73.001  1.00  4.47           C  
-ATOM   1900  C   PHE A 258      82.040  39.589  72.330  1.00  4.47           C  
-ATOM   1901  O   PHE A 258      81.193  40.469  72.229  1.00  6.41           O  
-ATOM   1902  CB  PHE A 258      81.770  38.388  74.514  1.00  4.47           C  
-ATOM   1903  CG  PHE A 258      81.206  37.185  75.205  1.00 10.98           C  
-ATOM   1904  CD1 PHE A 258      79.842  36.919  75.151  1.00 17.03           C  
-ATOM   1905  CD2 PHE A 258      82.027  36.300  75.879  1.00  9.85           C  
-ATOM   1906  CE1 PHE A 258      79.309  35.788  75.761  1.00 11.81           C  
-ATOM   1907  CE2 PHE A 258      81.500  35.163  76.493  1.00 11.81           C  
-ATOM   1908  CZ  PHE A 258      80.144  34.908  76.434  1.00  9.85           C  
-ATOM   1909  N   ALA A 259      83.260  39.715  71.843  1.00  7.59           N  
-ATOM   1910  CA  ALA A 259      83.651  40.928  71.154  1.00 15.70           C  
-ATOM   1911  C   ALA A 259      82.894  40.982  69.837  1.00 15.25           C  
-ATOM   1912  O   ALA A 259      82.634  42.048  69.305  1.00 26.73           O  
-ATOM   1913  CB  ALA A 259      85.153  40.909  70.897  1.00 17.88           C  
-ATOM   1914  N   VAL A 260      82.544  39.805  69.331  1.00 18.17           N  
-ATOM   1915  CA  VAL A 260      81.846  39.650  68.061  1.00 18.81           C  
-ATOM   1916  C   VAL A 260      80.336  39.519  68.266  1.00 16.00           C  
-ATOM   1917  O   VAL A 260      79.559  39.645  67.328  1.00 22.97           O  
-ATOM   1918  CB  VAL A 260      82.394  38.391  67.288  1.00 15.51           C  
-ATOM   1919  CG1 VAL A 260      81.540  38.092  66.080  1.00 25.82           C  
-ATOM   1920  CG2 VAL A 260      83.822  38.630  66.829  1.00 11.87           C  
-ATOM   1921  N   LEU A 261      79.911  39.282  69.491  1.00  9.60           N  
-ATOM   1922  CA  LEU A 261      78.491  39.132  69.732  1.00 12.45           C  
-ATOM   1923  C   LEU A 261      77.784  40.415  70.138  1.00 20.11           C  
-ATOM   1924  O   LEU A 261      76.554  40.474  70.125  1.00 25.48           O  
-ATOM   1925  CB  LEU A 261      78.261  38.046  70.774  1.00 10.43           C  
-ATOM   1926  CG  LEU A 261      78.557  36.703  70.131  1.00 13.41           C  
-ATOM   1927  CD1 LEU A 261      78.497  35.598  71.166  1.00 22.15           C  
-ATOM   1928  CD2 LEU A 261      77.539  36.478  69.024  1.00 18.40           C  
-ATOM   1929  N   LYS A 262      78.555  41.437  70.504  1.00 16.65           N  
-ATOM   1930  CA  LYS A 262      77.986  42.722  70.892  1.00 10.70           C  
-ATOM   1931  C   LYS A 262      77.500  43.358  69.602  1.00 10.27           C  
-ATOM   1932  O   LYS A 262      78.209  44.131  68.972  1.00  8.49           O  
-ATOM   1933  CB  LYS A 262      79.063  43.601  71.529  1.00 24.01           C  
-ATOM   1934  CG  LYS A 262      78.648  45.047  71.793  1.00 27.20           C  
-ATOM   1935  CD  LYS A 262      77.755  45.164  73.018  1.00 36.27           C  
-ATOM   1936  CE  LYS A 262      78.516  45.691  74.239  1.00 35.75           C  
-ATOM   1937  NZ  LYS A 262      78.818  47.157  74.148  1.00 31.89           N  
-ATOM   1938  N   LEU A 263      76.285  43.015  69.196  1.00 18.95           N  
-ATOM   1939  CA  LEU A 263      75.723  43.545  67.955  1.00 14.60           C  
-ATOM   1940  C   LEU A 263      74.459  44.379  68.166  1.00 12.31           C  
-ATOM   1941  O   LEU A 263      73.552  44.010  68.914  1.00 14.44           O  
-ATOM   1942  CB  LEU A 263      75.402  42.400  66.986  1.00 14.05           C  
-ATOM   1943  CG  LEU A 263      76.533  41.426  66.658  1.00 16.93           C  
-ATOM   1944  CD1 LEU A 263      76.047  40.357  65.687  1.00  4.47           C  
-ATOM   1945  CD2 LEU A 263      77.694  42.201  66.066  1.00 20.91           C  
-ATOM   1946  N   PRO A 264      74.382  45.518  67.485  1.00  8.48           N  
-ATOM   1947  CA  PRO A 264      73.241  46.434  67.568  1.00 14.33           C  
-ATOM   1948  C   PRO A 264      71.929  45.708  67.294  1.00 15.16           C  
-ATOM   1949  O   PRO A 264      70.881  46.032  67.856  1.00 23.68           O  
-ATOM   1950  CB  PRO A 264      73.541  47.452  66.479  1.00  7.08           C  
-ATOM   1951  CG  PRO A 264      75.037  47.458  66.435  1.00 11.14           C  
-ATOM   1952  CD  PRO A 264      75.399  46.015  66.547  1.00  6.69           C  
-ATOM   1953  N   GLU A 265      72.002  44.725  66.413  1.00  9.38           N  
-ATOM   1954  CA  GLU A 265      70.836  43.955  66.039  1.00 14.93           C  
-ATOM   1955  C   GLU A 265      70.322  43.092  67.192  1.00 19.71           C  
-ATOM   1956  O   GLU A 265      69.225  42.536  67.117  1.00 29.61           O  
-ATOM   1957  CB  GLU A 265      71.162  43.065  64.827  1.00 16.21           C  
-ATOM   1958  CG  GLU A 265      71.679  43.821  63.595  1.00 25.80           C  
-ATOM   1959  CD  GLU A 265      73.202  43.975  63.558  1.00 39.18           C  
-ATOM   1960  OE1 GLU A 265      73.795  44.227  64.635  1.00 50.41           O  
-ATOM   1961  OE2 GLU A 265      73.801  43.862  62.452  1.00 31.91           O  
-ATOM   1962  N   LEU A 266      71.106  42.972  68.255  1.00 12.66           N  
-ATOM   1963  CA  LEU A 266      70.682  42.159  69.388  1.00 20.73           C  
-ATOM   1964  C   LEU A 266      70.338  43.028  70.591  1.00 29.97           C  
-ATOM   1965  O   LEU A 266      69.789  42.541  71.591  1.00 29.10           O  
-ATOM   1966  CB  LEU A 266      71.790  41.186  69.776  1.00 14.02           C  
-ATOM   1967  CG  LEU A 266      72.199  40.159  68.739  1.00  7.18           C  
-ATOM   1968  CD1 LEU A 266      73.448  39.451  69.217  1.00 18.91           C  
-ATOM   1969  CD2 LEU A 266      71.070  39.182  68.529  1.00 11.26           C  
-ATOM   1970  N   CYS A 267      70.672  44.313  70.490  1.00 29.76           N  
-ATOM   1971  CA  CYS A 267      70.420  45.251  71.571  1.00 29.38           C  
-ATOM   1972  C   CYS A 267      69.244  46.144  71.243  1.00 33.64           C  
-ATOM   1973  O   CYS A 267      68.827  46.244  70.083  1.00 32.04           O  
-ATOM   1974  CB  CYS A 267      71.654  46.115  71.820  1.00 33.49           C  
-ATOM   1975  SG  CYS A 267      73.170  45.204  72.180  1.00 40.72           S  
-ATOM   1976  N   GLY A 268      68.715  46.795  72.275  1.00 40.77           N  
-ATOM   1977  CA  GLY A 268      67.583  47.683  72.088  1.00 52.96           C  
-ATOM   1978  C   GLY A 268      67.973  49.141  71.916  1.00 60.55           C  
-ATOM   1979  O   GLY A 268      69.140  49.478  71.675  1.00 59.39           O  
-ATOM   1980  N   GLU A 269      66.974  50.007  72.041  1.00 68.71           N  
-ATOM   1981  CA  GLU A 269      67.155  51.450  71.908  1.00 74.62           C  
-ATOM   1982  C   GLU A 269      68.330  51.943  72.754  1.00 73.84           C  
-ATOM   1983  O   GLU A 269      69.325  52.454  72.230  1.00 73.45           O  
-ATOM   1984  CB  GLU A 269      65.868  52.164  72.347  1.00 79.20           C  
-ATOM   1985  CG  GLU A 269      65.859  53.682  72.171  1.00 83.40           C  
-ATOM   1986  CD  GLU A 269      64.639  54.329  72.815  1.00 87.00           C  
-ATOM   1987  OE1 GLU A 269      63.504  53.871  72.547  1.00 88.93           O  
-ATOM   1988  OE2 GLU A 269      64.817  55.297  73.588  1.00 86.08           O  
-ATOM   1989  N   PHE A 270      68.202  51.768  74.066  1.00 73.56           N  
-ATOM   1990  CA  PHE A 270      69.210  52.209  75.027  1.00 76.37           C  
-ATOM   1991  C   PHE A 270      70.557  51.521  74.856  1.00 69.82           C  
-ATOM   1992  O   PHE A 270      71.547  51.930  75.463  1.00 69.21           O  
-ATOM   1993  CB  PHE A 270      68.705  51.980  76.460  1.00 85.68           C  
-ATOM   1994  CG  PHE A 270      67.328  52.545  76.725  1.00 95.70           C  
-ATOM   1995  CD1 PHE A 270      66.579  52.089  77.808  1.00 97.67           C  
-ATOM   1996  CD2 PHE A 270      66.772  53.517  75.884  1.00 98.21           C  
-ATOM   1997  CE1 PHE A 270      65.296  52.585  78.048  1.00102.76           C  
-ATOM   1998  CE2 PHE A 270      65.489  54.021  76.116  1.00 99.87           C  
-ATOM   1999  CZ  PHE A 270      64.749  53.554  77.199  1.00102.67           C  
-ATOM   2000  N   GLY A 271      70.599  50.474  74.042  1.00 64.22           N  
-ATOM   2001  CA  GLY A 271      71.858  49.780  73.840  1.00 66.02           C  
-ATOM   2002  C   GLY A 271      72.103  48.623  74.801  1.00 65.77           C  
-ATOM   2003  O   GLY A 271      73.247  48.297  75.133  1.00 64.48           O  
-ATOM   2004  N   ASN A 272      71.022  48.005  75.260  1.00 62.57           N  
-ATOM   2005  CA  ASN A 272      71.120  46.863  76.154  1.00 53.51           C  
-ATOM   2006  C   ASN A 272      70.786  45.639  75.331  1.00 43.87           C  
-ATOM   2007  O   ASN A 272      69.938  45.707  74.443  1.00 41.35           O  
-ATOM   2008  CB  ASN A 272      70.114  46.984  77.296  1.00 65.15           C  
-ATOM   2009  CG  ASN A 272      70.606  47.873  78.409  1.00 77.61           C  
-ATOM   2010  OD1 ASN A 272      71.704  47.672  78.932  1.00 85.00           O  
-ATOM   2011  ND2 ASN A 272      69.795  48.857  78.791  1.00 85.49           N  
-ATOM   2012  N   ILE A 273      71.452  44.526  75.606  1.00 36.40           N  
-ATOM   2013  CA  ILE A 273      71.161  43.302  74.866  1.00 31.65           C  
-ATOM   2014  C   ILE A 273      69.764  42.798  75.293  1.00 27.50           C  
-ATOM   2015  O   ILE A 273      69.502  42.568  76.478  1.00 17.02           O  
-ATOM   2016  CB  ILE A 273      72.235  42.236  75.136  1.00 23.52           C  
-ATOM   2017  CG1 ILE A 273      71.851  40.929  74.450  1.00 19.76           C  
-ATOM   2018  CG2 ILE A 273      72.412  42.056  76.632  1.00 30.16           C  
-ATOM   2019  CD1 ILE A 273      72.801  39.786  74.726  1.00 20.24           C  
-ATOM   2020  N   LEU A 274      68.866  42.643  74.319  1.00 26.66           N  
-ATOM   2021  CA  LEU A 274      67.499  42.216  74.598  1.00 20.16           C  
-ATOM   2022  C   LEU A 274      67.391  40.969  75.465  1.00 20.56           C  
-ATOM   2023  O   LEU A 274      68.168  40.024  75.327  1.00 17.95           O  
-ATOM   2024  CB  LEU A 274      66.712  42.026  73.292  1.00 16.26           C  
-ATOM   2025  CG  LEU A 274      66.146  43.309  72.649  1.00 19.01           C  
-ATOM   2026  CD1 LEU A 274      67.237  44.030  71.897  1.00  4.47           C  
-ATOM   2027  CD2 LEU A 274      65.001  42.972  71.689  1.00 35.19           C  
-ATOM   2028  N   PRO A 275      66.408  40.960  76.379  1.00 21.65           N  
-ATOM   2029  CA  PRO A 275      66.119  39.877  77.316  1.00 18.02           C  
-ATOM   2030  C   PRO A 275      66.413  38.467  76.818  1.00 18.68           C  
-ATOM   2031  O   PRO A 275      67.360  37.827  77.276  1.00 25.90           O  
-ATOM   2032  CB  PRO A 275      64.644  40.090  77.623  1.00 10.91           C  
-ATOM   2033  CG  PRO A 275      64.575  41.558  77.703  1.00 12.05           C  
-ATOM   2034  CD  PRO A 275      65.376  42.008  76.487  1.00 19.79           C  
-ATOM   2035  N   LEU A 276      65.610  37.972  75.887  1.00 13.75           N  
-ATOM   2036  CA  LEU A 276      65.826  36.616  75.414  1.00 13.91           C  
-ATOM   2037  C   LEU A 276      67.268  36.390  75.040  1.00  8.76           C  
-ATOM   2038  O   LEU A 276      67.910  35.476  75.564  1.00 10.66           O  
-ATOM   2039  CB  LEU A 276      64.910  36.299  74.229  1.00 11.17           C  
-ATOM   2040  CG  LEU A 276      63.441  36.139  74.630  1.00  4.47           C  
-ATOM   2041  CD1 LEU A 276      62.609  35.786  73.423  1.00 10.36           C  
-ATOM   2042  CD2 LEU A 276      63.324  35.059  75.685  1.00  4.60           C  
-ATOM   2043  N   TRP A 277      67.780  37.242  74.159  1.00  4.47           N  
-ATOM   2044  CA  TRP A 277      69.154  37.117  73.703  1.00  4.47           C  
-ATOM   2045  C   TRP A 277      70.138  36.993  74.862  1.00  4.47           C  
-ATOM   2046  O   TRP A 277      71.194  36.380  74.732  1.00  4.47           O  
-ATOM   2047  CB  TRP A 277      69.511  38.308  72.825  1.00  7.51           C  
-ATOM   2048  CG  TRP A 277      68.657  38.466  71.577  1.00  5.23           C  
-ATOM   2049  CD1 TRP A 277      68.565  39.579  70.792  1.00  5.19           C  
-ATOM   2050  CD2 TRP A 277      67.825  37.474  70.955  1.00  5.73           C  
-ATOM   2051  NE1 TRP A 277      67.733  39.342  69.726  1.00 13.38           N  
-ATOM   2052  CE2 TRP A 277      67.266  38.057  69.802  1.00  4.47           C  
-ATOM   2053  CE3 TRP A 277      67.500  36.149  71.259  1.00 22.30           C  
-ATOM   2054  CZ2 TRP A 277      66.402  37.363  68.952  1.00  4.47           C  
-ATOM   2055  CZ3 TRP A 277      66.634  35.459  70.403  1.00 25.31           C  
-ATOM   2056  CH2 TRP A 277      66.099  36.073  69.266  1.00  4.47           C  
-ATOM   2057  N   ALA A 278      69.782  37.579  75.998  1.00 11.73           N  
-ATOM   2058  CA  ALA A 278      70.626  37.504  77.181  1.00  7.26           C  
-ATOM   2059  C   ALA A 278      70.583  36.074  77.646  1.00  9.52           C  
-ATOM   2060  O   ALA A 278      71.608  35.409  77.707  1.00 17.21           O  
-ATOM   2061  CB  ALA A 278      70.099  38.395  78.255  1.00  9.80           C  
-ATOM   2062  N   TRP A 279      69.384  35.599  77.969  1.00 13.17           N  
-ATOM   2063  CA  TRP A 279      69.209  34.219  78.410  1.00 14.40           C  
-ATOM   2064  C   TRP A 279      70.024  33.331  77.492  1.00 11.08           C  
-ATOM   2065  O   TRP A 279      70.667  32.392  77.935  1.00 15.58           O  
-ATOM   2066  CB  TRP A 279      67.741  33.811  78.339  1.00 16.10           C  
-ATOM   2067  CG  TRP A 279      66.870  34.537  79.305  1.00 25.00           C  
-ATOM   2068  CD1 TRP A 279      67.220  35.590  80.090  1.00 32.54           C  
-ATOM   2069  CD2 TRP A 279      65.484  34.293  79.558  1.00 30.03           C  
-ATOM   2070  NE1 TRP A 279      66.140  36.025  80.816  1.00 40.21           N  
-ATOM   2071  CE2 TRP A 279      65.059  35.243  80.507  1.00 37.09           C  
-ATOM   2072  CE3 TRP A 279      64.558  33.362  79.073  1.00 35.93           C  
-ATOM   2073  CZ2 TRP A 279      63.744  35.293  80.982  1.00 40.29           C  
-ATOM   2074  CZ3 TRP A 279      63.252  33.409  79.545  1.00 32.36           C  
-ATOM   2075  CH2 TRP A 279      62.857  34.369  80.490  1.00 38.07           C  
-ATOM   2076  N   GLY A 280      70.001  33.641  76.203  1.00  4.47           N  
-ATOM   2077  CA  GLY A 280      70.769  32.858  75.258  1.00  4.47           C  
-ATOM   2078  C   GLY A 280      72.253  32.891  75.579  1.00 10.22           C  
-ATOM   2079  O   GLY A 280      72.882  31.842  75.670  1.00 11.43           O  
-ATOM   2080  N   MET A 281      72.817  34.088  75.738  1.00  9.08           N  
-ATOM   2081  CA  MET A 281      74.229  34.225  76.060  1.00  5.85           C  
-ATOM   2082  C   MET A 281      74.536  33.290  77.220  1.00 11.20           C  
-ATOM   2083  O   MET A 281      75.571  32.624  77.245  1.00 20.44           O  
-ATOM   2084  CB  MET A 281      74.540  35.662  76.473  1.00  6.41           C  
-ATOM   2085  CG  MET A 281      74.198  36.697  75.421  1.00  7.02           C  
-ATOM   2086  SD  MET A 281      75.533  36.978  74.263  1.00  6.45           S  
-ATOM   2087  CE  MET A 281      75.618  35.460  73.473  1.00  9.61           C  
-ATOM   2088  N   GLU A 282      73.623  33.237  78.179  1.00  5.56           N  
-ATOM   2089  CA  GLU A 282      73.793  32.381  79.342  1.00 19.67           C  
-ATOM   2090  C   GLU A 282      74.100  30.925  78.930  1.00 20.16           C  
-ATOM   2091  O   GLU A 282      75.144  30.379  79.297  1.00 23.31           O  
-ATOM   2092  CB  GLU A 282      72.522  32.440  80.212  1.00 35.67           C  
-ATOM   2093  CG  GLU A 282      72.746  32.628  81.728  1.00 49.54           C  
-ATOM   2094  CD  GLU A 282      73.274  34.014  82.105  1.00 56.34           C  
-ATOM   2095  OE1 GLU A 282      72.588  35.022  81.813  1.00 59.12           O  
-ATOM   2096  OE2 GLU A 282      74.373  34.093  82.702  1.00 52.98           O  
-ATOM   2097  N   THR A 283      73.203  30.303  78.161  1.00 19.76           N  
-ATOM   2098  CA  THR A 283      73.384  28.911  77.724  1.00 11.68           C  
-ATOM   2099  C   THR A 283      74.627  28.748  76.855  1.00  7.60           C  
-ATOM   2100  O   THR A 283      75.342  27.757  76.965  1.00 13.62           O  
-ATOM   2101  CB  THR A 283      72.160  28.385  76.928  1.00  4.47           C  
-ATOM   2102  OG1 THR A 283      72.024  29.138  75.723  1.00 21.63           O  
-ATOM   2103  CG2 THR A 283      70.876  28.529  77.736  1.00  5.05           C  
-ATOM   2104  N   LEU A 284      74.880  29.712  75.981  1.00  4.96           N  
-ATOM   2105  CA  LEU A 284      76.062  29.649  75.138  1.00  4.47           C  
-ATOM   2106  C   LEU A 284      77.279  29.602  76.059  1.00 13.38           C  
-ATOM   2107  O   LEU A 284      78.227  28.864  75.802  1.00 14.71           O  
-ATOM   2108  CB  LEU A 284      76.138  30.875  74.218  1.00  4.47           C  
-ATOM   2109  CG  LEU A 284      77.453  31.071  73.451  1.00  4.47           C  
-ATOM   2110  CD1 LEU A 284      77.269  32.008  72.295  1.00  5.87           C  
-ATOM   2111  CD2 LEU A 284      78.488  31.641  74.371  1.00 14.33           C  
-ATOM   2112  N   SER A 285      77.251  30.398  77.128  1.00 15.51           N  
-ATOM   2113  CA  SER A 285      78.351  30.427  78.083  1.00 16.39           C  
-ATOM   2114  C   SER A 285      78.409  29.063  78.740  1.00 13.28           C  
-ATOM   2115  O   SER A 285      79.440  28.396  78.734  1.00 13.89           O  
-ATOM   2116  CB  SER A 285      78.121  31.502  79.152  1.00 22.50           C  
-ATOM   2117  OG  SER A 285      78.026  32.788  78.573  1.00 33.72           O  
-ATOM   2118  N   ASN A 286      77.280  28.654  79.302  1.00 17.61           N  
-ATOM   2119  CA  ASN A 286      77.167  27.364  79.966  1.00 22.36           C  
-ATOM   2120  C   ASN A 286      77.899  26.276  79.197  1.00 24.26           C  
-ATOM   2121  O   ASN A 286      78.641  25.491  79.784  1.00 26.81           O  
-ATOM   2122  CB  ASN A 286      75.692  26.977  80.113  1.00 23.15           C  
-ATOM   2123  CG  ASN A 286      75.062  27.536  81.373  1.00 33.96           C  
-ATOM   2124  OD1 ASN A 286      75.639  28.401  82.046  1.00 43.65           O  
-ATOM   2125  ND2 ASN A 286      73.866  27.046  81.702  1.00 30.37           N  
-ATOM   2126  N   CYS A 287      77.686  26.240  77.884  1.00 21.31           N  
-ATOM   2127  CA  CYS A 287      78.310  25.247  77.020  1.00 22.45           C  
-ATOM   2128  C   CYS A 287      79.834  25.394  76.932  1.00 29.82           C  
-ATOM   2129  O   CYS A 287      80.587  24.534  77.400  1.00 33.80           O  
-ATOM   2130  CB  CYS A 287      77.697  25.333  75.623  1.00 19.42           C  
-ATOM   2131  SG  CYS A 287      78.585  24.415  74.333  1.00 24.75           S  
-ATOM   2132  N   LEU A 288      80.281  26.488  76.328  1.00 29.60           N  
-ATOM   2133  CA  LEU A 288      81.703  26.768  76.154  1.00 21.82           C  
-ATOM   2134  C   LEU A 288      82.533  26.632  77.421  1.00 21.14           C  
-ATOM   2135  O   LEU A 288      83.671  26.179  77.372  1.00 28.02           O  
-ATOM   2136  CB  LEU A 288      81.867  28.176  75.598  1.00 16.88           C  
-ATOM   2137  CG  LEU A 288      82.272  28.334  74.133  1.00 22.32           C  
-ATOM   2138  CD1 LEU A 288      81.581  27.330  73.256  1.00 30.32           C  
-ATOM   2139  CD2 LEU A 288      81.933  29.740  73.692  1.00 19.52           C  
-ATOM   2140  N   ARG A 289      81.956  27.018  78.552  1.00 16.97           N  
-ATOM   2141  CA  ARG A 289      82.653  26.975  79.832  1.00 18.03           C  
-ATOM   2142  C   ARG A 289      83.027  25.591  80.310  1.00 22.96           C  
-ATOM   2143  O   ARG A 289      84.042  25.408  80.977  1.00 29.29           O  
-ATOM   2144  CB  ARG A 289      81.807  27.658  80.902  1.00 16.60           C  
-ATOM   2145  CG  ARG A 289      82.418  27.634  82.283  1.00 24.99           C  
-ATOM   2146  CD  ARG A 289      81.885  28.779  83.115  1.00 32.07           C  
-ATOM   2147  NE  ARG A 289      80.429  28.831  83.091  1.00 32.93           N  
-ATOM   2148  CZ  ARG A 289      79.733  29.958  82.980  1.00 43.66           C  
-ATOM   2149  NH1 ARG A 289      80.363  31.130  82.882  1.00 37.37           N  
-ATOM   2150  NH2 ARG A 289      78.406  29.911  82.961  1.00 48.34           N  
-ATOM   2151  N   SER A 290      82.201  24.613  79.978  1.00 25.72           N  
-ATOM   2152  CA  SER A 290      82.451  23.242  80.393  1.00 22.58           C  
-ATOM   2153  C   SER A 290      83.717  22.702  79.752  1.00 19.22           C  
-ATOM   2154  O   SER A 290      84.436  21.899  80.343  1.00 19.01           O  
-ATOM   2155  CB  SER A 290      81.276  22.352  79.984  1.00 30.15           C  
-ATOM   2156  OG  SER A 290      80.056  22.823  80.534  1.00 45.66           O  
-ATOM   2157  N   MET A 291      83.988  23.173  78.543  1.00 14.57           N  
-ATOM   2158  CA  MET A 291      85.122  22.716  77.760  1.00 10.19           C  
-ATOM   2159  C   MET A 291      86.551  22.907  78.246  1.00  4.47           C  
-ATOM   2160  O   MET A 291      86.885  23.875  78.889  1.00  4.47           O  
-ATOM   2161  CB  MET A 291      84.960  23.258  76.344  1.00 13.95           C  
-ATOM   2162  CG  MET A 291      83.776  22.607  75.645  1.00 13.55           C  
-ATOM   2163  SD  MET A 291      83.476  23.139  73.981  1.00 20.52           S  
-ATOM   2164  CE  MET A 291      81.847  23.879  74.195  1.00 24.52           C  
-ATOM   2165  N   SER A 292      87.390  21.939  77.918  1.00  4.47           N  
-ATOM   2166  CA  SER A 292      88.797  21.954  78.285  1.00 13.77           C  
-ATOM   2167  C   SER A 292      89.600  22.185  77.004  1.00  9.20           C  
-ATOM   2168  O   SER A 292      89.863  21.263  76.241  1.00  6.46           O  
-ATOM   2169  CB  SER A 292      89.176  20.613  78.914  1.00 29.72           C  
-ATOM   2170  OG  SER A 292      88.245  20.247  79.922  1.00 42.91           O  
-ATOM   2171  N   PRO A 293      90.012  23.431  76.768  1.00  7.94           N  
-ATOM   2172  CA  PRO A 293      90.775  23.881  75.603  1.00  6.41           C  
-ATOM   2173  C   PRO A 293      92.230  23.488  75.477  1.00  4.47           C  
-ATOM   2174  O   PRO A 293      93.018  23.644  76.403  1.00  6.38           O  
-ATOM   2175  CB  PRO A 293      90.616  25.384  75.671  1.00  9.36           C  
-ATOM   2176  CG  PRO A 293      90.701  25.616  77.143  1.00 13.29           C  
-ATOM   2177  CD  PRO A 293      89.788  24.547  77.701  1.00  7.46           C  
-ATOM   2178  N   PHE A 294      92.575  23.013  74.290  1.00  4.47           N  
-ATOM   2179  CA  PHE A 294      93.928  22.604  73.958  1.00  4.47           C  
-ATOM   2180  C   PHE A 294      94.261  23.018  72.521  1.00  9.91           C  
-ATOM   2181  O   PHE A 294      93.423  22.957  71.622  1.00 11.74           O  
-ATOM   2182  CB  PHE A 294      94.073  21.089  74.081  1.00  4.47           C  
-ATOM   2183  CG  PHE A 294      93.965  20.583  75.484  1.00  6.80           C  
-ATOM   2184  CD1 PHE A 294      92.914  19.773  75.857  1.00 13.64           C  
-ATOM   2185  CD2 PHE A 294      94.929  20.902  76.427  1.00 11.21           C  
-ATOM   2186  CE1 PHE A 294      92.823  19.282  77.139  1.00 23.40           C  
-ATOM   2187  CE2 PHE A 294      94.847  20.421  77.714  1.00 15.20           C  
-ATOM   2188  CZ  PHE A 294      93.792  19.607  78.073  1.00 27.65           C  
-ATOM   2189  N   VAL A 295      95.497  23.433  72.303  1.00 13.98           N  
-ATOM   2190  CA  VAL A 295      95.944  23.850  70.980  1.00  6.72           C  
-ATOM   2191  C   VAL A 295      97.002  22.874  70.480  1.00 15.17           C  
-ATOM   2192  O   VAL A 295      97.968  22.578  71.181  1.00 27.20           O  
-ATOM   2193  CB  VAL A 295      96.545  25.268  71.038  1.00  8.51           C  
-ATOM   2194  CG1 VAL A 295      97.517  25.488  69.883  1.00  9.66           C  
-ATOM   2195  CG2 VAL A 295      95.433  26.287  70.999  1.00  4.47           C  
-ATOM   2196  N   LEU A 296      96.823  22.385  69.260  1.00 16.35           N  
-ATOM   2197  CA  LEU A 296      97.752  21.427  68.671  1.00 18.50           C  
-ATOM   2198  C   LEU A 296      98.253  21.935  67.340  1.00 22.96           C  
-ATOM   2199  O   LEU A 296      97.468  22.210  66.446  1.00 27.15           O  
-ATOM   2200  CB  LEU A 296      97.040  20.093  68.471  1.00 19.82           C  
-ATOM   2201  CG  LEU A 296      97.812  18.890  67.942  1.00 17.36           C  
-ATOM   2202  CD1 LEU A 296      96.902  17.680  67.957  1.00 27.55           C  
-ATOM   2203  CD2 LEU A 296      98.290  19.150  66.546  1.00 21.01           C  
-ATOM   2204  N   SER A 297      99.567  22.040  67.201  1.00 31.99           N  
-ATOM   2205  CA  SER A 297     100.159  22.533  65.963  1.00 34.85           C  
-ATOM   2206  C   SER A 297     100.338  21.458  64.917  1.00 36.02           C  
-ATOM   2207  O   SER A 297     100.969  20.443  65.182  1.00 45.34           O  
-ATOM   2208  CB  SER A 297     101.519  23.151  66.245  1.00 39.55           C  
-ATOM   2209  OG  SER A 297     102.189  23.422  65.032  1.00 43.67           O  
-ATOM   2210  N   LEU A 298      99.798  21.683  63.725  1.00 37.43           N  
-ATOM   2211  CA  LEU A 298      99.936  20.715  62.646  1.00 45.16           C  
-ATOM   2212  C   LEU A 298     101.004  21.171  61.675  1.00 53.05           C  
-ATOM   2213  O   LEU A 298     100.980  20.810  60.500  1.00 57.63           O  
-ATOM   2214  CB  LEU A 298      98.621  20.540  61.893  1.00 41.90           C  
-ATOM   2215  CG  LEU A 298      97.466  19.936  62.685  1.00 45.87           C  
-ATOM   2216  CD1 LEU A 298      96.312  19.656  61.742  1.00 49.90           C  
-ATOM   2217  CD2 LEU A 298      97.910  18.649  63.354  1.00 49.22           C  
-ATOM   2218  N   GLU A 299     101.943  21.965  62.175  1.00 58.89           N  
-ATOM   2219  CA  GLU A 299     103.034  22.483  61.360  1.00 66.43           C  
-ATOM   2220  C   GLU A 299     104.231  21.535  61.424  1.00 66.58           C  
-ATOM   2221  O   GLU A 299     105.274  21.874  61.979  1.00 66.75           O  
-ATOM   2222  CB  GLU A 299     103.437  23.870  61.870  1.00 78.16           C  
-ATOM   2223  CG  GLU A 299     104.479  24.605  61.026  1.00 92.11           C  
-ATOM   2224  CD  GLU A 299     103.909  25.183  59.742  1.00 98.76           C  
-ATOM   2225  OE1 GLU A 299     104.673  25.839  58.999  1.00101.73           O  
-ATOM   2226  OE2 GLU A 299     102.703  24.984  59.478  1.00102.89           O  
-ATOM   2227  N   GLN A 300     104.070  20.347  60.852  1.00 68.94           N  
-ATOM   2228  CA  GLN A 300     105.123  19.335  60.840  1.00 71.48           C  
-ATOM   2229  C   GLN A 300     104.579  18.006  60.332  1.00 77.97           C  
-ATOM   2230  O   GLN A 300     103.415  17.914  59.940  1.00 83.95           O  
-ATOM   2231  CB  GLN A 300     105.689  19.143  62.245  1.00 67.38           C  
-ATOM   2232  CG  GLN A 300     104.634  18.886  63.305  1.00 64.59           C  
-ATOM   2233  CD  GLN A 300     105.222  18.824  64.704  1.00 67.75           C  
-ATOM   2234  OE1 GLN A 300     104.497  18.662  65.689  1.00 64.82           O  
-ATOM   2235  NE2 GLN A 300     106.546  18.948  64.798  1.00 63.55           N  
-ATOM   2236  N   THR A 301     105.424  16.977  60.343  1.00 80.47           N  
-ATOM   2237  CA  THR A 301     105.025  15.646  59.881  1.00 79.32           C  
-ATOM   2238  C   THR A 301     103.897  15.085  60.743  1.00 75.12           C  
-ATOM   2239  O   THR A 301     103.933  15.196  61.968  1.00 74.15           O  
-ATOM   2240  CB  THR A 301     106.210  14.663  59.929  1.00 80.02           C  
-ATOM   2241  OG1 THR A 301     106.709  14.583  61.270  1.00 78.46           O  
-ATOM   2242  CG2 THR A 301     107.328  15.132  59.003  1.00 80.44           C  
-ATOM   2243  N   PRO A 302     102.881  14.473  60.112  1.00 72.53           N  
-ATOM   2244  CA  PRO A 302     101.749  13.903  60.848  1.00 72.72           C  
-ATOM   2245  C   PRO A 302     102.207  13.101  62.056  1.00 74.94           C  
-ATOM   2246  O   PRO A 302     101.497  13.026  63.057  1.00 78.49           O  
-ATOM   2247  CB  PRO A 302     101.059  13.033  59.804  1.00 73.89           C  
-ATOM   2248  CG  PRO A 302     101.296  13.800  58.543  1.00 75.22           C  
-ATOM   2249  CD  PRO A 302     102.756  14.198  58.669  1.00 72.28           C  
-ATOM   2250  N   GLN A 303     103.396  12.506  61.955  1.00 76.34           N  
-ATOM   2251  CA  GLN A 303     103.951  11.716  63.052  1.00 79.59           C  
-ATOM   2252  C   GLN A 303     104.065  12.582  64.301  1.00 75.91           C  
-ATOM   2253  O   GLN A 303     103.561  12.228  65.367  1.00 75.03           O  
-ATOM   2254  CB  GLN A 303     105.336  11.154  62.686  1.00 88.48           C  
-ATOM   2255  CG  GLN A 303     105.331   9.832  61.896  1.00 97.19           C  
-ATOM   2256  CD  GLN A 303     104.901   9.992  60.439  1.00106.14           C  
-ATOM   2257  OE1 GLN A 303     105.518  10.736  59.670  1.00107.77           O  
-ATOM   2258  NE2 GLN A 303     103.842   9.284  60.053  1.00105.95           N  
-ATOM   2259  N   HIS A 304     104.725  13.725  64.169  1.00 73.80           N  
-ATOM   2260  CA  HIS A 304     104.880  14.627  65.302  1.00 72.58           C  
-ATOM   2261  C   HIS A 304     103.527  15.112  65.828  1.00 66.11           C  
-ATOM   2262  O   HIS A 304     103.229  14.972  67.017  1.00 62.42           O  
-ATOM   2263  CB  HIS A 304     105.749  15.824  64.908  1.00 80.00           C  
-ATOM   2264  CG  HIS A 304     107.205  15.500  64.769  1.00 84.97           C  
-ATOM   2265  ND1 HIS A 304     108.181  16.472  64.710  1.00 86.97           N  
-ATOM   2266  CD2 HIS A 304     107.852  14.312  64.697  1.00 85.14           C  
-ATOM   2267  CE1 HIS A 304     109.366  15.897  64.611  1.00 87.36           C  
-ATOM   2268  NE2 HIS A 304     109.195  14.588  64.601  1.00 87.42           N  
-ATOM   2269  N   ALA A 305     102.715  15.678  64.937  1.00 58.47           N  
-ATOM   2270  CA  ALA A 305     101.396  16.180  65.300  1.00 50.16           C  
-ATOM   2271  C   ALA A 305     100.705  15.209  66.247  1.00 50.92           C  
-ATOM   2272  O   ALA A 305     100.212  15.595  67.303  1.00 51.60           O  
-ATOM   2273  CB  ALA A 305     100.552  16.374  64.054  1.00 49.86           C  
-ATOM   2274  N   ALA A 306     100.681  13.940  65.865  1.00 50.62           N  
-ATOM   2275  CA  ALA A 306     100.044  12.920  66.680  1.00 52.35           C  
-ATOM   2276  C   ALA A 306     100.818  12.644  67.970  1.00 52.18           C  
-ATOM   2277  O   ALA A 306     100.230  12.441  69.034  1.00 51.83           O  
-ATOM   2278  CB  ALA A 306      99.893  11.640  65.872  1.00 49.99           C  
-ATOM   2279  N   GLN A 307     102.141  12.635  67.882  1.00 52.49           N  
-ATOM   2280  CA  GLN A 307     102.929  12.370  69.068  1.00 58.74           C  
-ATOM   2281  C   GLN A 307     102.637  13.457  70.079  1.00 55.10           C  
-ATOM   2282  O   GLN A 307     102.449  13.184  71.267  1.00 52.84           O  
-ATOM   2283  CB  GLN A 307     104.426  12.345  68.739  1.00 73.13           C  
-ATOM   2284  CG  GLN A 307     105.317  11.969  69.936  1.00 89.07           C  
-ATOM   2285  CD  GLN A 307     106.782  11.777  69.558  1.00 97.91           C  
-ATOM   2286  OE1 GLN A 307     107.118  10.920  68.734  1.00103.36           O  
-ATOM   2287  NE2 GLN A 307     107.661  12.573  70.164  1.00 94.62           N  
-ATOM   2288  N   GLU A 308     102.588  14.694  69.599  1.00 52.88           N  
-ATOM   2289  CA  GLU A 308     102.321  15.818  70.482  1.00 54.09           C  
-ATOM   2290  C   GLU A 308     100.979  15.590  71.157  1.00 47.55           C  
-ATOM   2291  O   GLU A 308     100.877  15.640  72.380  1.00 49.60           O  
-ATOM   2292  CB  GLU A 308     102.315  17.136  69.695  1.00 61.34           C  
-ATOM   2293  CG  GLU A 308     102.168  18.396  70.562  1.00 74.41           C  
-ATOM   2294  CD  GLU A 308     102.327  19.699  69.770  1.00 83.70           C  
-ATOM   2295  OE1 GLU A 308     102.107  20.789  70.352  1.00 84.35           O  
-ATOM   2296  OE2 GLU A 308     102.676  19.638  68.570  1.00 87.05           O  
-ATOM   2297  N   LEU A 309      99.954  15.315  70.359  1.00 38.69           N  
-ATOM   2298  CA  LEU A 309      98.628  15.077  70.905  1.00 33.26           C  
-ATOM   2299  C   LEU A 309      98.679  14.059  72.032  1.00 32.91           C  
-ATOM   2300  O   LEU A 309      97.923  14.153  72.996  1.00 36.14           O  
-ATOM   2301  CB  LEU A 309      97.677  14.590  69.808  1.00 25.01           C  
-ATOM   2302  CG  LEU A 309      96.285  14.103  70.232  1.00 13.21           C  
-ATOM   2303  CD1 LEU A 309      95.548  15.157  71.052  1.00 14.77           C  
-ATOM   2304  CD2 LEU A 309      95.505  13.759  68.983  1.00  9.99           C  
-ATOM   2305  N   LYS A 310      99.579  13.090  71.914  1.00 34.54           N  
-ATOM   2306  CA  LYS A 310      99.698  12.064  72.938  1.00 42.26           C  
-ATOM   2307  C   LYS A 310     100.140  12.648  74.276  1.00 38.72           C  
-ATOM   2308  O   LYS A 310      99.596  12.302  75.329  1.00 38.97           O  
-ATOM   2309  CB  LYS A 310     100.691  10.982  72.502  1.00 51.78           C  
-ATOM   2310  CG  LYS A 310     100.912   9.918  73.568  1.00 64.49           C  
-ATOM   2311  CD  LYS A 310     102.060   8.981  73.226  1.00 78.51           C  
-ATOM   2312  CE  LYS A 310     102.348   8.019  74.387  1.00 89.20           C  
-ATOM   2313  NZ  LYS A 310     103.486   7.080  74.112  1.00 89.92           N  
-ATOM   2314  N   THR A 311     101.125  13.538  74.228  1.00 33.55           N  
-ATOM   2315  CA  THR A 311     101.655  14.156  75.437  1.00 32.64           C  
-ATOM   2316  C   THR A 311     100.576  14.920  76.211  1.00 31.63           C  
-ATOM   2317  O   THR A 311     100.728  15.179  77.403  1.00 33.02           O  
-ATOM   2318  CB  THR A 311     102.816  15.118  75.096  1.00 31.36           C  
-ATOM   2319  OG1 THR A 311     102.299  16.425  74.822  1.00 41.77           O  
-ATOM   2320  CG2 THR A 311     103.555  14.637  73.858  1.00 30.70           C  
-ATOM   2321  N   LEU A 312      99.486  15.259  75.523  1.00 32.56           N  
-ATOM   2322  CA  LEU A 312      98.366  16.009  76.100  1.00 33.06           C  
-ATOM   2323  C   LEU A 312      97.325  15.147  76.798  1.00 34.86           C  
-ATOM   2324  O   LEU A 312      96.617  15.610  77.696  1.00 29.90           O  
-ATOM   2325  CB  LEU A 312      97.646  16.807  75.011  1.00 37.46           C  
-ATOM   2326  CG  LEU A 312      98.189  18.144  74.498  1.00 44.51           C  
-ATOM   2327  CD1 LEU A 312      99.598  17.993  73.951  1.00 51.14           C  
-ATOM   2328  CD2 LEU A 312      97.263  18.651  73.408  1.00 47.57           C  
-ATOM   2329  N   LEU A 313      97.219  13.898  76.364  1.00 39.33           N  
-ATOM   2330  CA  LEU A 313      96.251  12.970  76.931  1.00 40.42           C  
-ATOM   2331  C   LEU A 313      96.157  13.071  78.451  1.00 37.89           C  
-ATOM   2332  O   LEU A 313      95.058  13.091  79.007  1.00 35.00           O  
-ATOM   2333  CB  LEU A 313      96.608  11.544  76.517  1.00 41.47           C  
-ATOM   2334  CG  LEU A 313      96.696  11.337  75.010  1.00 35.86           C  
-ATOM   2335  CD1 LEU A 313      97.130   9.913  74.728  1.00 49.63           C  
-ATOM   2336  CD2 LEU A 313      95.348  11.641  74.372  1.00 35.71           C  
-ATOM   2337  N   PRO A 314      97.311  13.130  79.140  1.00 36.03           N  
-ATOM   2338  CA  PRO A 314      97.316  13.229  80.599  1.00 37.68           C  
-ATOM   2339  C   PRO A 314      96.765  14.529  81.171  1.00 36.89           C  
-ATOM   2340  O   PRO A 314      96.412  14.587  82.347  1.00 40.54           O  
-ATOM   2341  CB  PRO A 314      98.786  13.024  80.949  1.00 37.51           C  
-ATOM   2342  CG  PRO A 314      99.501  13.552  79.756  1.00 28.32           C  
-ATOM   2343  CD  PRO A 314      98.688  12.971  78.636  1.00 33.91           C  
-ATOM   2344  N   GLN A 315      96.681  15.565  80.343  1.00 38.21           N  
-ATOM   2345  CA  GLN A 315      96.179  16.864  80.792  1.00 37.22           C  
-ATOM   2346  C   GLN A 315      94.678  17.027  80.568  1.00 34.48           C  
-ATOM   2347  O   GLN A 315      94.047  17.903  81.156  1.00 40.70           O  
-ATOM   2348  CB  GLN A 315      96.901  18.005  80.069  1.00 37.20           C  
-ATOM   2349  CG  GLN A 315      98.417  17.940  80.116  1.00 49.89           C  
-ATOM   2350  CD  GLN A 315      99.081  19.170  79.512  1.00 56.26           C  
-ATOM   2351  OE1 GLN A 315      98.975  20.276  80.054  1.00 60.42           O  
-ATOM   2352  NE2 GLN A 315      99.769  18.983  78.385  1.00 52.78           N  
-ATOM   2353  N   MET A 316      94.106  16.184  79.720  1.00 24.12           N  
-ATOM   2354  CA  MET A 316      92.686  16.272  79.423  1.00 17.35           C  
-ATOM   2355  C   MET A 316      91.753  15.778  80.520  1.00 17.63           C  
-ATOM   2356  O   MET A 316      92.108  14.930  81.334  1.00 21.84           O  
-ATOM   2357  CB  MET A 316      92.411  15.529  78.131  1.00 14.21           C  
-ATOM   2358  CG  MET A 316      93.302  16.015  77.029  1.00 11.29           C  
-ATOM   2359  SD  MET A 316      93.045  15.125  75.530  1.00 36.64           S  
-ATOM   2360  CE  MET A 316      94.083  16.053  74.370  1.00 21.53           C  
-ATOM   2361  N   THR A 317      90.549  16.330  80.532  1.00 15.99           N  
-ATOM   2362  CA  THR A 317      89.544  15.963  81.511  1.00 19.44           C  
-ATOM   2363  C   THR A 317      88.841  14.704  81.050  1.00 22.51           C  
-ATOM   2364  O   THR A 317      88.362  14.640  79.928  1.00 34.66           O  
-ATOM   2365  CB  THR A 317      88.500  17.072  81.667  1.00 21.41           C  
-ATOM   2366  OG1 THR A 317      89.130  18.244  82.189  1.00 29.10           O  
-ATOM   2367  CG2 THR A 317      87.391  16.636  82.604  1.00 25.94           C  
-ATOM   2368  N   PRO A 318      88.783  13.681  81.908  1.00 23.31           N  
-ATOM   2369  CA  PRO A 318      88.129  12.412  81.575  1.00 27.82           C  
-ATOM   2370  C   PRO A 318      86.680  12.323  82.044  1.00 26.13           C  
-ATOM   2371  O   PRO A 318      86.281  13.018  82.984  1.00 26.42           O  
-ATOM   2372  CB  PRO A 318      89.011  11.402  82.284  1.00 35.64           C  
-ATOM   2373  CG  PRO A 318      89.343  12.131  83.558  1.00 24.09           C  
-ATOM   2374  CD  PRO A 318      89.687  13.514  83.062  1.00 18.28           C  
-ATOM   2375  N   ALA A 319      85.903  11.461  81.395  1.00 19.51           N  
-ATOM   2376  CA  ALA A 319      84.511  11.272  81.782  1.00 29.96           C  
-ATOM   2377  C   ALA A 319      84.250   9.792  82.026  1.00 32.93           C  
-ATOM   2378  O   ALA A 319      85.030   8.944  81.612  1.00 27.60           O  
-ATOM   2379  CB  ALA A 319      83.584  11.797  80.703  1.00 39.89           C  
-ATOM   2380  N   ASN A 320      83.148   9.483  82.693  1.00 40.65           N  
-ATOM   2381  CA  ASN A 320      82.825   8.098  82.988  1.00 46.19           C  
-ATOM   2382  C   ASN A 320      81.625   7.586  82.207  1.00 46.99           C  
-ATOM   2383  O   ASN A 320      80.632   8.300  82.027  1.00 48.50           O  
-ATOM   2384  CB  ASN A 320      82.550   7.940  84.479  1.00 57.34           C  
-ATOM   2385  CG  ASN A 320      83.626   8.559  85.328  1.00 64.75           C  
-ATOM   2386  OD1 ASN A 320      84.811   8.288  85.132  1.00 61.86           O  
-ATOM   2387  ND2 ASN A 320      83.224   9.399  86.282  1.00 74.68           N  
-ATOM   2388  N   MET A 321      81.722   6.340  81.751  1.00 45.02           N  
-ATOM   2389  CA  MET A 321      80.635   5.716  81.014  1.00 41.39           C  
-ATOM   2390  C   MET A 321      80.601   4.207  81.184  1.00 41.20           C  
-ATOM   2391  O   MET A 321      81.629   3.566  81.377  1.00 34.17           O  
-ATOM   2392  CB  MET A 321      80.725   6.054  79.529  1.00 37.28           C  
-ATOM   2393  CG  MET A 321      81.694   5.229  78.726  1.00 20.84           C  
-ATOM   2394  SD  MET A 321      81.500   5.597  76.960  1.00 22.83           S  
-ATOM   2395  CE  MET A 321      80.029   4.806  76.605  1.00 25.54           C  
-ATOM   2396  N   SER A 322      79.398   3.651  81.115  1.00 45.98           N  
-ATOM   2397  CA  SER A 322      79.189   2.213  81.242  1.00 50.25           C  
-ATOM   2398  C   SER A 322      80.078   1.430  80.274  1.00 51.35           C  
-ATOM   2399  O   SER A 322      80.164   1.751  79.089  1.00 61.78           O  
-ATOM   2400  CB  SER A 322      77.714   1.882  80.962  1.00 56.05           C  
-ATOM   2401  OG  SER A 322      77.479   0.481  80.922  1.00 57.58           O  
-ATOM   2402  N   SER A 323      80.748   0.403  80.774  1.00 44.92           N  
-ATOM   2403  CA  SER A 323      81.589  -0.403  79.913  1.00 39.68           C  
-ATOM   2404  C   SER A 323      80.692  -0.902  78.794  1.00 41.03           C  
-ATOM   2405  O   SER A 323      81.068  -0.890  77.628  1.00 48.26           O  
-ATOM   2406  CB  SER A 323      82.158  -1.587  80.682  1.00 38.90           C  
-ATOM   2407  OG  SER A 323      83.004  -2.354  79.850  1.00 39.33           O  
-ATOM   2408  N   GLY A 324      79.487  -1.321  79.159  1.00 38.59           N  
-ATOM   2409  CA  GLY A 324      78.547  -1.817  78.172  1.00 32.89           C  
-ATOM   2410  C   GLY A 324      78.271  -0.819  77.073  1.00 25.84           C  
-ATOM   2411  O   GLY A 324      78.320  -1.159  75.892  1.00 18.37           O  
-ATOM   2412  N   ALA A 325      77.987   0.416  77.477  1.00 26.79           N  
-ATOM   2413  CA  ALA A 325      77.691   1.509  76.552  1.00 19.99           C  
-ATOM   2414  C   ALA A 325      78.808   1.741  75.543  1.00 14.95           C  
-ATOM   2415  O   ALA A 325      78.552   1.923  74.354  1.00 12.33           O  
-ATOM   2416  CB  ALA A 325      77.426   2.773  77.321  1.00 21.18           C  
-ATOM   2417  N   TRP A 326      80.049   1.752  76.009  1.00  9.52           N  
-ATOM   2418  CA  TRP A 326      81.165   1.930  75.095  1.00 13.06           C  
-ATOM   2419  C   TRP A 326      81.059   0.936  73.932  1.00 17.91           C  
-ATOM   2420  O   TRP A 326      81.272   1.298  72.774  1.00 10.70           O  
-ATOM   2421  CB  TRP A 326      82.487   1.738  75.833  1.00 11.34           C  
-ATOM   2422  CG  TRP A 326      83.660   1.590  74.923  1.00  8.76           C  
-ATOM   2423  CD1 TRP A 326      84.131   0.440  74.394  1.00 11.99           C  
-ATOM   2424  CD2 TRP A 326      84.505   2.636  74.421  1.00 15.14           C  
-ATOM   2425  NE1 TRP A 326      85.218   0.689  73.592  1.00 10.69           N  
-ATOM   2426  CE2 TRP A 326      85.470   2.030  73.590  1.00 10.29           C  
-ATOM   2427  CE3 TRP A 326      84.542   4.028  74.595  1.00 15.04           C  
-ATOM   2428  CZ2 TRP A 326      86.465   2.760  72.934  1.00 13.11           C  
-ATOM   2429  CZ3 TRP A 326      85.538   4.758  73.941  1.00 14.84           C  
-ATOM   2430  CH2 TRP A 326      86.484   4.120  73.122  1.00 10.44           C  
-ATOM   2431  N   ASN A 327      80.723  -0.316  74.241  1.00 25.58           N  
-ATOM   2432  CA  ASN A 327      80.586  -1.344  73.211  1.00 28.09           C  
-ATOM   2433  C   ASN A 327      79.432  -1.029  72.268  1.00 20.64           C  
-ATOM   2434  O   ASN A 327      79.504  -1.288  71.076  1.00 12.90           O  
-ATOM   2435  CB  ASN A 327      80.387  -2.714  73.854  1.00 38.66           C  
-ATOM   2436  CG  ASN A 327      81.641  -3.214  74.565  1.00 43.94           C  
-ATOM   2437  OD1 ASN A 327      82.742  -3.241  73.996  1.00 26.94           O  
-ATOM   2438  ND2 ASN A 327      81.477  -3.622  75.816  1.00 53.57           N  
-ATOM   2439  N   ILE A 328      78.364  -0.475  72.822  1.00 21.77           N  
-ATOM   2440  CA  ILE A 328      77.210  -0.075  72.034  1.00 19.54           C  
-ATOM   2441  C   ILE A 328      77.650   1.091  71.159  1.00 22.20           C  
-ATOM   2442  O   ILE A 328      77.618   1.007  69.938  1.00 24.21           O  
-ATOM   2443  CB  ILE A 328      76.073   0.391  72.944  1.00 24.17           C  
-ATOM   2444  CG1 ILE A 328      75.388  -0.823  73.570  1.00 20.36           C  
-ATOM   2445  CG2 ILE A 328      75.113   1.278  72.173  1.00 17.11           C  
-ATOM   2446  CD1 ILE A 328      74.393  -0.472  74.659  1.00 31.18           C  
-ATOM   2447  N   LEU A 329      78.064   2.180  71.795  1.00 20.92           N  
-ATOM   2448  CA  LEU A 329      78.523   3.352  71.067  1.00 24.97           C  
-ATOM   2449  C   LEU A 329      79.328   2.923  69.850  1.00 25.21           C  
-ATOM   2450  O   LEU A 329      79.029   3.329  68.731  1.00 27.71           O  
-ATOM   2451  CB  LEU A 329      79.388   4.235  71.972  1.00 21.36           C  
-ATOM   2452  CG  LEU A 329      80.121   5.408  71.320  1.00  4.47           C  
-ATOM   2453  CD1 LEU A 329      79.117   6.346  70.717  1.00  4.47           C  
-ATOM   2454  CD2 LEU A 329      80.970   6.121  72.358  1.00 10.94           C  
-ATOM   2455  N   LYS A 330      80.337   2.085  70.079  1.00 27.10           N  
-ATOM   2456  CA  LYS A 330      81.202   1.595  69.011  1.00 32.30           C  
-ATOM   2457  C   LYS A 330      80.413   1.047  67.836  1.00 38.91           C  
-ATOM   2458  O   LYS A 330      80.720   1.352  66.684  1.00 37.82           O  
-ATOM   2459  CB  LYS A 330      82.128   0.495  69.523  1.00 36.68           C  
-ATOM   2460  CG  LYS A 330      83.224   0.960  70.448  1.00 44.12           C  
-ATOM   2461  CD  LYS A 330      84.300  -0.102  70.601  1.00 54.36           C  
-ATOM   2462  CE  LYS A 330      84.896  -0.497  69.257  1.00 63.62           C  
-ATOM   2463  NZ  LYS A 330      85.425   0.665  68.489  1.00 62.90           N  
-ATOM   2464  N   GLU A 331      79.409   0.222  68.137  1.00 43.36           N  
-ATOM   2465  CA  GLU A 331      78.567  -0.386  67.110  1.00 40.79           C  
-ATOM   2466  C   GLU A 331      77.825   0.703  66.338  1.00 37.45           C  
-ATOM   2467  O   GLU A 331      77.795   0.691  65.108  1.00 40.89           O  
-ATOM   2468  CB  GLU A 331      77.554  -1.348  67.742  1.00 39.51           C  
-ATOM   2469  CG  GLU A 331      76.733  -2.140  66.730  1.00 55.83           C  
-ATOM   2470  CD  GLU A 331      75.249  -2.237  67.097  1.00 71.49           C  
-ATOM   2471  OE1 GLU A 331      74.928  -2.679  68.223  1.00 75.61           O  
-ATOM   2472  OE2 GLU A 331      74.397  -1.877  66.252  1.00 74.07           O  
-ATOM   2473  N   LEU A 332      77.233   1.650  67.058  1.00 26.80           N  
-ATOM   2474  CA  LEU A 332      76.499   2.726  66.415  1.00 18.39           C  
-ATOM   2475  C   LEU A 332      77.433   3.504  65.521  1.00 12.92           C  
-ATOM   2476  O   LEU A 332      77.156   3.714  64.347  1.00  9.62           O  
-ATOM   2477  CB  LEU A 332      75.888   3.644  67.461  1.00 12.76           C  
-ATOM   2478  CG  LEU A 332      75.066   2.857  68.476  1.00 22.61           C  
-ATOM   2479  CD1 LEU A 332      74.471   3.799  69.490  1.00 30.62           C  
-ATOM   2480  CD2 LEU A 332      73.977   2.076  67.770  1.00 19.84           C  
-ATOM   2481  N   VAL A 333      78.553   3.922  66.083  1.00 15.58           N  
-ATOM   2482  CA  VAL A 333      79.526   4.677  65.326  1.00 17.37           C  
-ATOM   2483  C   VAL A 333      79.915   3.915  64.087  1.00 22.84           C  
-ATOM   2484  O   VAL A 333      80.080   4.497  63.024  1.00 30.92           O  
-ATOM   2485  CB  VAL A 333      80.787   4.922  66.126  1.00 18.41           C  
-ATOM   2486  CG1 VAL A 333      81.746   5.753  65.311  1.00 21.99           C  
-ATOM   2487  CG2 VAL A 333      80.442   5.609  67.435  1.00 33.13           C  
-ATOM   2488  N   ASN A 334      80.073   2.607  64.218  1.00 31.86           N  
-ATOM   2489  CA  ASN A 334      80.454   1.799  63.073  1.00 41.10           C  
-ATOM   2490  C   ASN A 334      79.279   1.631  62.139  1.00 41.63           C  
-ATOM   2491  O   ASN A 334      79.455   1.459  60.934  1.00 44.56           O  
-ATOM   2492  CB  ASN A 334      80.935   0.425  63.518  1.00 51.33           C  
-ATOM   2493  CG  ASN A 334      81.414  -0.416  62.359  1.00 62.79           C  
-ATOM   2494  OD1 ASN A 334      82.431  -0.102  61.734  1.00 66.76           O  
-ATOM   2495  ND2 ASN A 334      80.676  -1.485  62.052  1.00 64.89           N  
-ATOM   2496  N   ALA A 335      78.076   1.683  62.696  1.00 43.76           N  
-ATOM   2497  CA  ALA A 335      76.863   1.528  61.904  1.00 42.53           C  
-ATOM   2498  C   ALA A 335      76.600   2.693  60.987  1.00 44.65           C  
-ATOM   2499  O   ALA A 335      75.964   2.515  59.950  1.00 48.94           O  
-ATOM   2500  CB  ALA A 335      75.668   1.330  62.815  1.00 42.77           C  
-ATOM   2501  N   VAL A 336      77.081   3.883  61.357  1.00 46.66           N  
-ATOM   2502  CA  VAL A 336      76.872   5.094  60.538  1.00 45.66           C  
-ATOM   2503  C   VAL A 336      78.083   5.590  59.755  1.00 53.77           C  
-ATOM   2504  O   VAL A 336      77.926   6.284  58.768  1.00 53.92           O  
-ATOM   2505  CB  VAL A 336      76.357   6.250  61.389  1.00 40.85           C  
-ATOM   2506  CG1 VAL A 336      75.213   5.789  62.270  1.00 43.86           C  
-ATOM   2507  CG2 VAL A 336      77.478   6.840  62.216  1.00 44.11           C  
-ATOM   2508  N   GLN A 337      79.297   5.283  60.200  1.00 63.51           N  
-ATOM   2509  CA  GLN A 337      80.455   5.733  59.415  1.00 73.90           C  
-ATOM   2510  C   GLN A 337      80.556   4.739  58.256  1.00 79.42           C  
-ATOM   2511  O   GLN A 337      81.481   4.805  57.461  1.00 81.96           O  
-ATOM   2512  CB  GLN A 337      81.739   5.724  60.247  1.00 77.00           C  
-ATOM   2513  CG  GLN A 337      81.742   6.712  61.428  1.00 80.55           C  
-ATOM   2514  CD  GLN A 337      81.518   8.154  61.016  1.00 86.23           C  
-ATOM   2515  OE1 GLN A 337      82.374   8.767  60.374  1.00 94.18           O  
-ATOM   2516  NE2 GLN A 337      80.371   8.708  61.395  1.00 81.68           N  
-ATOM   2517  N   ASP A 338      79.614   3.796  58.219  1.00 89.38           N  
-ATOM   2518  CA  ASP A 338      79.540   2.741  57.216  1.00 96.81           C  
-ATOM   2519  C   ASP A 338      79.328   3.241  55.755  1.00101.10           C  
-ATOM   2520  O   ASP A 338      80.279   3.079  54.955  1.00101.65           O  
-ATOM   2521  CB  ASP A 338      78.383   1.776  57.550  1.00100.55           C  
-ATOM   2522  CG  ASP A 338      78.388   0.542  56.664  1.00101.59           C  
-ATOM   2523  OD1 ASP A 338      79.236  -0.351  56.880  1.00 98.65           O  
-ATOM   2524  OD2 ASP A 338      77.545   0.485  55.744  1.00102.71           O  
-TER    2525      ASP A 338                                                      
-ATOM   2526  N   MET B  10      55.449  22.953  95.393  1.00 66.81           N  
-ATOM   2527  CA  MET B  10      54.020  22.949  94.945  1.00 70.09           C  
-ATOM   2528  C   MET B  10      53.893  22.486  93.487  1.00 69.12           C  
-ATOM   2529  O   MET B  10      54.895  22.433  92.768  1.00 67.61           O  
-ATOM   2530  CB  MET B  10      53.396  24.350  95.113  1.00 71.35           C  
-ATOM   2531  CG  MET B  10      54.125  25.499  94.405  1.00 73.63           C  
-ATOM   2532  SD  MET B  10      53.108  27.011  94.274  1.00 82.80           S  
-ATOM   2533  CE  MET B  10      53.873  28.109  95.470  1.00 73.84           C  
-ATOM   2534  N   GLY B  11      52.668  22.162  93.056  1.00 61.35           N  
-ATOM   2535  CA  GLY B  11      52.446  21.686  91.695  1.00 50.96           C  
-ATOM   2536  C   GLY B  11      51.807  22.666  90.727  1.00 48.03           C  
-ATOM   2537  O   GLY B  11      50.747  23.224  91.010  1.00 51.68           O  
-ATOM   2538  N   VAL B  12      52.451  22.860  89.576  1.00 43.92           N  
-ATOM   2539  CA  VAL B  12      51.965  23.777  88.541  1.00 39.84           C  
-ATOM   2540  C   VAL B  12      51.265  23.048  87.398  1.00 34.87           C  
-ATOM   2541  O   VAL B  12      51.235  21.818  87.353  1.00 38.84           O  
-ATOM   2542  CB  VAL B  12      53.118  24.591  87.940  1.00 39.20           C  
-ATOM   2543  CG1 VAL B  12      53.829  25.362  89.031  1.00 41.39           C  
-ATOM   2544  CG2 VAL B  12      54.085  23.663  87.236  1.00 39.23           C  
-ATOM   2545  N   LEU B  13      50.716  23.809  86.461  1.00 23.88           N  
-ATOM   2546  CA  LEU B  13      50.020  23.198  85.345  1.00 25.61           C  
-ATOM   2547  C   LEU B  13      50.458  23.826  84.027  1.00 30.03           C  
-ATOM   2548  O   LEU B  13      49.930  24.868  83.617  1.00 25.78           O  
-ATOM   2549  CB  LEU B  13      48.516  23.367  85.544  1.00 20.77           C  
-ATOM   2550  CG  LEU B  13      47.652  22.153  85.226  1.00 20.27           C  
-ATOM   2551  CD1 LEU B  13      48.196  20.951  85.984  1.00 10.67           C  
-ATOM   2552  CD2 LEU B  13      46.187  22.448  85.603  1.00 17.17           C  
-ATOM   2553  N   ARG B  14      51.428  23.195  83.364  1.00 33.89           N  
-ATOM   2554  CA  ARG B  14      51.928  23.714  82.090  1.00 33.21           C  
-ATOM   2555  C   ARG B  14      50.964  23.442  80.947  1.00 31.29           C  
-ATOM   2556  O   ARG B  14      50.718  22.289  80.578  1.00 37.47           O  
-ATOM   2557  CB  ARG B  14      53.306  23.128  81.768  1.00 34.48           C  
-ATOM   2558  CG  ARG B  14      54.418  23.739  82.613  1.00 33.89           C  
-ATOM   2559  CD  ARG B  14      55.803  23.578  81.985  1.00 35.40           C  
-ATOM   2560  NE  ARG B  14      56.330  22.226  82.136  1.00 37.52           N  
-ATOM   2561  CZ  ARG B  14      56.166  21.253  81.250  1.00 37.31           C  
-ATOM   2562  NH1 ARG B  14      55.490  21.479  80.131  1.00 34.16           N  
-ATOM   2563  NH2 ARG B  14      56.673  20.051  81.492  1.00 40.06           N  
-ATOM   2564  N   ILE B  15      50.417  24.516  80.390  1.00 22.01           N  
-ATOM   2565  CA  ILE B  15      49.462  24.386  79.309  1.00 17.35           C  
-ATOM   2566  C   ILE B  15      49.849  25.222  78.108  1.00 23.69           C  
-ATOM   2567  O   ILE B  15      49.877  26.457  78.172  1.00 27.96           O  
-ATOM   2568  CB  ILE B  15      48.064  24.820  79.747  1.00  9.20           C  
-ATOM   2569  CG1 ILE B  15      47.653  24.063  81.004  1.00 10.67           C  
-ATOM   2570  CG2 ILE B  15      47.076  24.524  78.645  1.00  7.90           C  
-ATOM   2571  CD1 ILE B  15      46.318  24.486  81.545  1.00 13.93           C  
-ATOM   2572  N   TYR B  16      50.146  24.530  77.014  1.00 21.83           N  
-ATOM   2573  CA  TYR B  16      50.517  25.170  75.766  1.00 16.11           C  
-ATOM   2574  C   TYR B  16      49.312  25.123  74.826  1.00 18.19           C  
-ATOM   2575  O   TYR B  16      48.750  24.058  74.535  1.00 16.93           O  
-ATOM   2576  CB  TYR B  16      51.722  24.453  75.172  1.00  8.42           C  
-ATOM   2577  CG  TYR B  16      52.955  24.584  76.025  1.00  7.52           C  
-ATOM   2578  CD1 TYR B  16      53.729  25.740  75.981  1.00 13.44           C  
-ATOM   2579  CD2 TYR B  16      53.352  23.556  76.880  1.00 12.89           C  
-ATOM   2580  CE1 TYR B  16      54.881  25.874  76.764  1.00 24.40           C  
-ATOM   2581  CE2 TYR B  16      54.506  23.678  77.674  1.00 23.08           C  
-ATOM   2582  CZ  TYR B  16      55.268  24.842  77.606  1.00 25.49           C  
-ATOM   2583  OH  TYR B  16      56.431  24.974  78.341  1.00 25.89           O  
-ATOM   2584  N   LEU B  17      48.917  26.297  74.361  1.00 22.16           N  
-ATOM   2585  CA  LEU B  17      47.764  26.442  73.490  1.00 25.91           C  
-ATOM   2586  C   LEU B  17      48.190  26.662  72.033  1.00 26.51           C  
-ATOM   2587  O   LEU B  17      48.726  27.716  71.688  1.00 30.56           O  
-ATOM   2588  CB  LEU B  17      46.944  27.627  73.998  1.00 27.21           C  
-ATOM   2589  CG  LEU B  17      45.470  27.760  73.642  1.00 31.71           C  
-ATOM   2590  CD1 LEU B  17      44.719  26.492  74.037  1.00 37.67           C  
-ATOM   2591  CD2 LEU B  17      44.910  28.966  74.378  1.00 28.88           C  
-ATOM   2592  N   ASP B  18      47.943  25.672  71.182  1.00 24.95           N  
-ATOM   2593  CA  ASP B  18      48.317  25.768  69.775  1.00 26.60           C  
-ATOM   2594  C   ASP B  18      47.169  25.615  68.784  1.00 27.29           C  
-ATOM   2595  O   ASP B  18      46.002  25.730  69.143  1.00 30.95           O  
-ATOM   2596  CB  ASP B  18      49.382  24.728  69.441  1.00 31.94           C  
-ATOM   2597  CG  ASP B  18      50.697  25.356  69.049  1.00 42.56           C  
-ATOM   2598  OD1 ASP B  18      51.631  25.326  69.887  1.00 36.73           O  
-ATOM   2599  OD2 ASP B  18      50.784  25.887  67.911  1.00 47.58           O  
-ATOM   2600  N   GLY B  19      47.524  25.342  67.530  1.00 27.12           N  
-ATOM   2601  CA  GLY B  19      46.536  25.184  66.479  1.00 27.12           C  
-ATOM   2602  C   GLY B  19      46.896  26.094  65.322  1.00 33.04           C  
-ATOM   2603  O   GLY B  19      48.007  26.622  65.288  1.00 39.50           O  
-ATOM   2604  N   ALA B  20      45.968  26.287  64.385  1.00 31.46           N  
-ATOM   2605  CA  ALA B  20      46.193  27.145  63.219  1.00 32.25           C  
-ATOM   2606  C   ALA B  20      46.307  28.619  63.603  1.00 40.96           C  
-ATOM   2607  O   ALA B  20      46.177  28.970  64.774  1.00 44.77           O  
-ATOM   2608  CB  ALA B  20      45.069  26.962  62.234  1.00 31.54           C  
-ATOM   2609  N   TYR B  21      46.539  29.486  62.620  1.00 49.28           N  
-ATOM   2610  CA  TYR B  21      46.672  30.913  62.902  1.00 61.47           C  
-ATOM   2611  C   TYR B  21      45.445  31.720  62.507  1.00 67.35           C  
-ATOM   2612  O   TYR B  21      44.677  31.303  61.648  1.00 74.24           O  
-ATOM   2613  CB  TYR B  21      47.917  31.481  62.209  1.00 66.04           C  
-ATOM   2614  CG  TYR B  21      47.834  31.625  60.705  1.00 65.26           C  
-ATOM   2615  CD1 TYR B  21      47.135  32.677  60.119  1.00 65.19           C  
-ATOM   2616  CD2 TYR B  21      48.495  30.731  59.868  1.00 69.96           C  
-ATOM   2617  CE1 TYR B  21      47.102  32.837  58.737  1.00 67.76           C  
-ATOM   2618  CE2 TYR B  21      48.468  30.880  58.486  1.00 71.11           C  
-ATOM   2619  CZ  TYR B  21      47.772  31.935  57.926  1.00 68.29           C  
-ATOM   2620  OH  TYR B  21      47.749  32.087  56.559  1.00 64.83           O  
-ATOM   2621  N   GLY B  22      45.269  32.876  63.143  1.00 69.64           N  
-ATOM   2622  CA  GLY B  22      44.128  33.724  62.853  1.00 69.45           C  
-ATOM   2623  C   GLY B  22      42.842  33.179  63.445  1.00 69.38           C  
-ATOM   2624  O   GLY B  22      41.833  33.880  63.504  1.00 70.26           O  
-ATOM   2625  N   ILE B  23      42.880  31.926  63.889  1.00 70.20           N  
-ATOM   2626  CA  ILE B  23      41.711  31.275  64.477  1.00 71.73           C  
-ATOM   2627  C   ILE B  23      41.157  32.006  65.706  1.00 72.53           C  
-ATOM   2628  O   ILE B  23      39.959  31.930  65.985  1.00 75.52           O  
-ATOM   2629  CB  ILE B  23      42.014  29.796  64.875  1.00 68.86           C  
-ATOM   2630  CG1 ILE B  23      43.333  29.719  65.646  1.00 71.83           C  
-ATOM   2631  CG2 ILE B  23      42.051  28.913  63.642  1.00 61.65           C  
-ATOM   2632  CD1 ILE B  23      43.617  28.356  66.251  1.00 70.31           C  
-ATOM   2633  N   GLY B  24      42.021  32.704  66.440  1.00 65.91           N  
-ATOM   2634  CA  GLY B  24      41.567  33.422  67.618  1.00 58.40           C  
-ATOM   2635  C   GLY B  24      41.974  32.798  68.937  1.00 55.06           C  
-ATOM   2636  O   GLY B  24      41.341  33.028  69.963  1.00 52.67           O  
-ATOM   2637  N   LYS B  25      43.043  32.012  68.913  1.00 58.49           N  
-ATOM   2638  CA  LYS B  25      43.533  31.347  70.117  1.00 55.42           C  
-ATOM   2639  C   LYS B  25      44.236  32.294  71.077  1.00 48.26           C  
-ATOM   2640  O   LYS B  25      44.742  31.877  72.107  1.00 46.31           O  
-ATOM   2641  CB  LYS B  25      44.474  30.178  69.757  1.00 58.19           C  
-ATOM   2642  CG  LYS B  25      45.309  30.369  68.488  1.00 58.76           C  
-ATOM   2643  CD  LYS B  25      46.482  29.403  68.434  1.00 47.77           C  
-ATOM   2644  CE  LYS B  25      47.514  29.782  69.482  1.00 46.81           C  
-ATOM   2645  NZ  LYS B  25      47.912  31.220  69.324  1.00 41.21           N  
-ATOM   2646  N   THR B  26      44.268  33.573  70.743  1.00 53.36           N  
-ATOM   2647  CA  THR B  26      44.910  34.537  71.619  1.00 62.59           C  
-ATOM   2648  C   THR B  26      43.851  35.361  72.342  1.00 67.71           C  
-ATOM   2649  O   THR B  26      43.931  35.544  73.555  1.00 70.96           O  
-ATOM   2650  CB  THR B  26      45.876  35.473  70.835  1.00 64.71           C  
-ATOM   2651  OG1 THR B  26      46.997  34.717  70.357  1.00 66.93           O  
-ATOM   2652  CG2 THR B  26      46.393  36.581  71.729  1.00 65.16           C  
-ATOM   2653  N   THR B  27      42.849  35.844  71.609  1.00 72.77           N  
-ATOM   2654  CA  THR B  27      41.797  36.644  72.232  1.00 76.29           C  
-ATOM   2655  C   THR B  27      40.913  35.732  73.074  1.00 73.68           C  
-ATOM   2656  O   THR B  27      40.082  36.199  73.856  1.00 74.30           O  
-ATOM   2657  CB  THR B  27      40.914  37.370  71.187  1.00 74.80           C  
-ATOM   2658  OG1 THR B  27      41.679  37.628  70.005  1.00 73.54           O  
-ATOM   2659  CG2 THR B  27      40.432  38.712  71.748  1.00 73.18           C  
-ATOM   2660  N   ALA B  28      41.107  34.428  72.908  1.00 68.93           N  
-ATOM   2661  CA  ALA B  28      40.344  33.438  73.652  1.00 66.91           C  
-ATOM   2662  C   ALA B  28      41.206  32.879  74.771  1.00 63.99           C  
-ATOM   2663  O   ALA B  28      40.710  32.236  75.689  1.00 63.44           O  
-ATOM   2664  CB  ALA B  28      39.892  32.321  72.727  1.00 71.77           C  
-ATOM   2665  N   ALA B  29      42.507  33.125  74.686  1.00 65.08           N  
-ATOM   2666  CA  ALA B  29      43.437  32.656  75.703  1.00 64.90           C  
-ATOM   2667  C   ALA B  29      43.575  33.749  76.742  1.00 67.78           C  
-ATOM   2668  O   ALA B  29      44.009  33.505  77.862  1.00 68.37           O  
-ATOM   2669  CB  ALA B  29      44.787  32.355  75.084  1.00 61.13           C  
-ATOM   2670  N   GLU B  30      43.214  34.964  76.349  1.00 72.98           N  
-ATOM   2671  CA  GLU B  30      43.276  36.105  77.245  1.00 75.69           C  
-ATOM   2672  C   GLU B  30      41.979  36.163  78.050  1.00 76.77           C  
-ATOM   2673  O   GLU B  30      42.001  36.353  79.266  1.00 79.13           O  
-ATOM   2674  CB  GLU B  30      43.466  37.403  76.447  1.00 79.65           C  
-ATOM   2675  CG  GLU B  30      44.845  37.564  75.808  1.00 88.31           C  
-ATOM   2676  CD  GLU B  30      45.033  38.924  75.135  1.00 99.03           C  
-ATOM   2677  OE1 GLU B  30      44.913  39.961  75.825  1.00104.29           O  
-ATOM   2678  OE2 GLU B  30      45.305  38.961  73.916  1.00103.06           O  
-ATOM   2679  N   GLU B  31      40.849  35.980  77.372  1.00 74.90           N  
-ATOM   2680  CA  GLU B  31      39.552  36.023  78.041  1.00 71.76           C  
-ATOM   2681  C   GLU B  31      39.499  34.945  79.106  1.00 67.04           C  
-ATOM   2682  O   GLU B  31      38.575  34.897  79.909  1.00 69.17           O  
-ATOM   2683  CB  GLU B  31      38.415  35.810  77.038  1.00 78.21           C  
-ATOM   2684  CG  GLU B  31      37.232  36.766  77.203  1.00 85.78           C  
-ATOM   2685  CD  GLU B  31      36.599  36.706  78.579  1.00 92.48           C  
-ATOM   2686  OE1 GLU B  31      36.201  35.598  78.996  1.00100.47           O  
-ATOM   2687  OE2 GLU B  31      36.492  37.766  79.240  1.00 89.30           O  
-ATOM   2688  N   PHE B  32      40.496  34.074  79.107  1.00 63.63           N  
-ATOM   2689  CA  PHE B  32      40.551  33.010  80.089  1.00 65.96           C  
-ATOM   2690  C   PHE B  32      41.352  33.488  81.278  1.00 68.73           C  
-ATOM   2691  O   PHE B  32      41.211  32.977  82.381  1.00 75.19           O  
-ATOM   2692  CB  PHE B  32      41.220  31.772  79.501  1.00 65.77           C  
-ATOM   2693  CG  PHE B  32      41.347  30.631  80.474  1.00 60.86           C  
-ATOM   2694  CD1 PHE B  32      40.226  29.923  80.892  1.00 55.91           C  
-ATOM   2695  CD2 PHE B  32      42.590  30.264  80.976  1.00 54.94           C  
-ATOM   2696  CE1 PHE B  32      40.345  28.870  81.791  1.00 44.74           C  
-ATOM   2697  CE2 PHE B  32      42.715  29.211  81.878  1.00 40.56           C  
-ATOM   2698  CZ  PHE B  32      41.592  28.515  82.284  1.00 38.34           C  
-ATOM   2699  N   LEU B  33      42.202  34.476  81.042  1.00 72.27           N  
-ATOM   2700  CA  LEU B  33      43.042  35.026  82.091  1.00 76.39           C  
-ATOM   2701  C   LEU B  33      42.265  36.048  82.920  1.00 83.81           C  
-ATOM   2702  O   LEU B  33      42.382  36.082  84.145  1.00 85.43           O  
-ATOM   2703  CB  LEU B  33      44.282  35.666  81.460  1.00 71.43           C  
-ATOM   2704  CG  LEU B  33      45.348  36.293  82.359  1.00 64.00           C  
-ATOM   2705  CD1 LEU B  33      45.831  35.294  83.384  1.00 55.54           C  
-ATOM   2706  CD2 LEU B  33      46.502  36.774  81.494  1.00 60.27           C  
-ATOM   2707  N   HIS B  34      41.447  36.852  82.245  1.00 88.25           N  
-ATOM   2708  CA  HIS B  34      40.648  37.884  82.906  1.00 93.62           C  
-ATOM   2709  C   HIS B  34      39.579  37.344  83.849  1.00 95.08           C  
-ATOM   2710  O   HIS B  34      39.208  38.021  84.807  1.00 98.81           O  
-ATOM   2711  CB  HIS B  34      39.969  38.782  81.865  1.00 95.83           C  
-ATOM   2712  CG  HIS B  34      40.888  39.769  81.214  1.00 96.88           C  
-ATOM   2713  ND1 HIS B  34      42.167  39.447  80.810  1.00 96.01           N  
-ATOM   2714  CD2 HIS B  34      40.695  41.059  80.850  1.00 97.08           C  
-ATOM   2715  CE1 HIS B  34      42.721  40.494  80.225  1.00 93.45           C  
-ATOM   2716  NE2 HIS B  34      41.848  41.485  80.235  1.00 97.11           N  
-ATOM   2717  N   HIS B  35      39.082  36.138  83.583  1.00 93.31           N  
-ATOM   2718  CA  HIS B  35      38.033  35.550  84.415  1.00 93.70           C  
-ATOM   2719  C   HIS B  35      38.476  34.677  85.583  1.00 93.73           C  
-ATOM   2720  O   HIS B  35      37.785  34.613  86.596  1.00 99.83           O  
-ATOM   2721  CB  HIS B  35      37.060  34.731  83.558  1.00 97.73           C  
-ATOM   2722  CG  HIS B  35      35.832  35.481  83.141  1.00107.60           C  
-ATOM   2723  ND1 HIS B  35      34.761  34.867  82.528  1.00110.02           N  
-ATOM   2724  CD2 HIS B  35      35.510  36.793  83.236  1.00111.63           C  
-ATOM   2725  CE1 HIS B  35      33.831  35.768  82.262  1.00112.83           C  
-ATOM   2726  NE2 HIS B  35      34.261  36.945  82.681  1.00113.73           N  
-ATOM   2727  N   PHE B  36      39.614  34.005  85.466  1.00 88.88           N  
-ATOM   2728  CA  PHE B  36      40.039  33.125  86.545  1.00 84.65           C  
-ATOM   2729  C   PHE B  36      41.281  33.570  87.291  1.00 83.79           C  
-ATOM   2730  O   PHE B  36      41.771  32.866  88.170  1.00 81.86           O  
-ATOM   2731  CB  PHE B  36      40.198  31.713  85.987  1.00 83.51           C  
-ATOM   2732  CG  PHE B  36      38.936  31.182  85.352  1.00 87.88           C  
-ATOM   2733  CD1 PHE B  36      38.990  30.326  84.260  1.00 87.73           C  
-ATOM   2734  CD2 PHE B  36      37.685  31.565  85.834  1.00 92.93           C  
-ATOM   2735  CE1 PHE B  36      37.816  29.860  83.652  1.00 85.42           C  
-ATOM   2736  CE2 PHE B  36      36.508  31.104  85.234  1.00 92.11           C  
-ATOM   2737  CZ  PHE B  36      36.577  30.251  84.140  1.00 87.94           C  
-ATOM   2738  N   ALA B  37      41.776  34.753  86.946  1.00 89.19           N  
-ATOM   2739  CA  ALA B  37      42.947  35.316  87.608  1.00 94.39           C  
-ATOM   2740  C   ALA B  37      42.455  36.242  88.720  1.00 94.60           C  
-ATOM   2741  O   ALA B  37      43.073  37.267  89.018  1.00 96.39           O  
-ATOM   2742  CB  ALA B  37      43.803  36.095  86.609  1.00 94.77           C  
-ATOM   2743  N   ILE B  38      41.324  35.873  89.316  1.00 91.51           N  
-ATOM   2744  CA  ILE B  38      40.721  36.637  90.399  1.00 85.90           C  
-ATOM   2745  C   ILE B  38      41.812  36.806  91.448  1.00 83.74           C  
-ATOM   2746  O   ILE B  38      41.981  37.865  92.043  1.00 83.61           O  
-ATOM   2747  CB  ILE B  38      39.522  35.865  90.988  1.00 85.28           C  
-ATOM   2748  CG1 ILE B  38      38.547  35.494  89.868  1.00 84.21           C  
-ATOM   2749  CG2 ILE B  38      38.808  36.711  92.016  1.00 86.58           C  
-ATOM   2750  CD1 ILE B  38      37.398  34.617  90.311  1.00 82.68           C  
-ATOM   2751  N   THR B  39      42.555  35.731  91.659  1.00 85.21           N  
-ATOM   2752  CA  THR B  39      43.673  35.714  92.588  1.00 85.04           C  
-ATOM   2753  C   THR B  39      44.928  35.800  91.699  1.00 87.92           C  
-ATOM   2754  O   THR B  39      45.316  34.820  91.060  1.00 96.67           O  
-ATOM   2755  CB  THR B  39      43.663  34.399  93.434  1.00 84.91           C  
-ATOM   2756  OG1 THR B  39      45.005  33.946  93.639  1.00 88.33           O  
-ATOM   2757  CG2 THR B  39      42.838  33.292  92.741  1.00 75.50           C  
-ATOM   2758  N   PRO B  40      45.568  36.984  91.644  1.00 82.94           N  
-ATOM   2759  CA  PRO B  40      46.774  37.308  90.858  1.00 78.58           C  
-ATOM   2760  C   PRO B  40      47.853  36.240  90.674  1.00 73.44           C  
-ATOM   2761  O   PRO B  40      48.231  35.915  89.541  1.00 69.65           O  
-ATOM   2762  CB  PRO B  40      47.318  38.543  91.565  1.00 76.64           C  
-ATOM   2763  CG  PRO B  40      46.071  39.234  91.976  1.00 82.33           C  
-ATOM   2764  CD  PRO B  40      45.226  38.105  92.537  1.00 81.50           C  
-ATOM   2765  N   ASN B  41      48.354  35.710  91.785  1.00 65.43           N  
-ATOM   2766  CA  ASN B  41      49.404  34.703  91.734  1.00 60.30           C  
-ATOM   2767  C   ASN B  41      48.940  33.282  91.440  1.00 55.26           C  
-ATOM   2768  O   ASN B  41      49.625  32.330  91.805  1.00 50.54           O  
-ATOM   2769  CB  ASN B  41      50.193  34.693  93.046  1.00 67.25           C  
-ATOM   2770  CG  ASN B  41      51.670  35.016  92.848  1.00 72.97           C  
-ATOM   2771  OD1 ASN B  41      52.512  34.672  93.688  1.00 64.42           O  
-ATOM   2772  ND2 ASN B  41      51.990  35.688  91.741  1.00 76.70           N  
-ATOM   2773  N   ARG B  42      47.791  33.118  90.792  1.00 55.73           N  
-ATOM   2774  CA  ARG B  42      47.334  31.766  90.493  1.00 58.89           C  
-ATOM   2775  C   ARG B  42      47.525  31.415  89.028  1.00 53.61           C  
-ATOM   2776  O   ARG B  42      47.397  30.252  88.641  1.00 60.69           O  
-ATOM   2777  CB  ARG B  42      45.853  31.557  90.864  1.00 63.98           C  
-ATOM   2778  CG  ARG B  42      45.497  30.059  90.966  1.00 75.91           C  
-ATOM   2779  CD  ARG B  42      44.004  29.755  90.879  1.00 81.47           C  
-ATOM   2780  NE  ARG B  42      43.774  28.316  90.700  1.00 87.00           N  
-ATOM   2781  CZ  ARG B  42      42.619  27.771  90.314  1.00 86.85           C  
-ATOM   2782  NH1 ARG B  42      41.566  28.541  90.058  1.00 89.30           N  
-ATOM   2783  NH2 ARG B  42      42.518  26.452  90.173  1.00 77.83           N  
-ATOM   2784  N   ILE B  43      47.857  32.406  88.212  1.00 44.54           N  
-ATOM   2785  CA  ILE B  43      48.021  32.144  86.793  1.00 38.18           C  
-ATOM   2786  C   ILE B  43      49.042  33.053  86.117  1.00 37.33           C  
-ATOM   2787  O   ILE B  43      49.111  34.261  86.384  1.00 41.94           O  
-ATOM   2788  CB  ILE B  43      46.671  32.276  86.098  1.00 30.01           C  
-ATOM   2789  CG1 ILE B  43      46.789  31.890  84.641  1.00 21.90           C  
-ATOM   2790  CG2 ILE B  43      46.170  33.699  86.225  1.00 48.80           C  
-ATOM   2791  CD1 ILE B  43      45.463  31.909  83.946  1.00 36.50           C  
-ATOM   2792  N   LEU B  44      49.832  32.460  85.230  1.00 31.79           N  
-ATOM   2793  CA  LEU B  44      50.867  33.195  84.518  1.00 32.16           C  
-ATOM   2794  C   LEU B  44      50.753  33.019  83.010  1.00 32.76           C  
-ATOM   2795  O   LEU B  44      50.787  31.892  82.520  1.00 38.43           O  
-ATOM   2796  CB  LEU B  44      52.245  32.713  84.978  1.00 26.65           C  
-ATOM   2797  CG  LEU B  44      53.417  33.185  84.115  1.00 23.32           C  
-ATOM   2798  CD1 LEU B  44      53.381  34.688  84.022  1.00 24.77           C  
-ATOM   2799  CD2 LEU B  44      54.743  32.710  84.700  1.00 27.22           C  
-ATOM   2800  N   LEU B  45      50.631  34.119  82.269  1.00 29.66           N  
-ATOM   2801  CA  LEU B  45      50.521  34.016  80.814  1.00 25.53           C  
-ATOM   2802  C   LEU B  45      51.779  34.431  80.062  1.00 24.65           C  
-ATOM   2803  O   LEU B  45      52.469  35.384  80.421  1.00 30.37           O  
-ATOM   2804  CB  LEU B  45      49.352  34.846  80.290  1.00 24.90           C  
-ATOM   2805  CG  LEU B  45      49.234  34.758  78.769  1.00 31.58           C  
-ATOM   2806  CD1 LEU B  45      48.977  33.307  78.375  1.00 40.35           C  
-ATOM   2807  CD2 LEU B  45      48.118  35.651  78.269  1.00 41.25           C  
-ATOM   2808  N   ILE B  46      52.061  33.705  78.997  1.00 17.96           N  
-ATOM   2809  CA  ILE B  46      53.220  33.981  78.179  1.00 19.83           C  
-ATOM   2810  C   ILE B  46      52.743  34.124  76.747  1.00 26.95           C  
-ATOM   2811  O   ILE B  46      52.362  33.135  76.120  1.00 35.98           O  
-ATOM   2812  CB  ILE B  46      54.206  32.817  78.244  1.00 17.80           C  
-ATOM   2813  CG1 ILE B  46      54.690  32.628  79.676  1.00 14.10           C  
-ATOM   2814  CG2 ILE B  46      55.379  33.085  77.319  1.00 33.02           C  
-ATOM   2815  CD1 ILE B  46      55.666  31.482  79.831  1.00 19.04           C  
-ATOM   2816  N   GLY B  47      52.767  35.341  76.218  1.00 29.61           N  
-ATOM   2817  CA  GLY B  47      52.302  35.543  74.851  1.00 36.58           C  
-ATOM   2818  C   GLY B  47      53.344  35.357  73.757  1.00 39.59           C  
-ATOM   2819  O   GLY B  47      54.556  35.402  74.024  1.00 39.84           O  
-ATOM   2820  N   GLU B  48      52.873  35.148  72.523  1.00 37.61           N  
-ATOM   2821  CA  GLU B  48      53.772  34.968  71.382  1.00 35.80           C  
-ATOM   2822  C   GLU B  48      54.730  36.150  71.337  1.00 31.45           C  
-ATOM   2823  O   GLU B  48      54.322  37.296  71.514  1.00 38.39           O  
-ATOM   2824  CB  GLU B  48      52.982  34.867  70.076  1.00 36.69           C  
-ATOM   2825  CG  GLU B  48      52.304  33.517  69.875  1.00 43.80           C  
-ATOM   2826  CD  GLU B  48      51.696  33.370  68.496  1.00 52.62           C  
-ATOM   2827  OE1 GLU B  48      51.244  32.255  68.166  1.00 60.50           O  
-ATOM   2828  OE2 GLU B  48      51.668  34.367  67.742  1.00 50.24           O  
-ATOM   2829  N   PRO B  49      56.022  35.884  71.113  1.00 24.45           N  
-ATOM   2830  CA  PRO B  49      57.025  36.950  71.066  1.00 23.79           C  
-ATOM   2831  C   PRO B  49      57.143  37.681  69.732  1.00 26.08           C  
-ATOM   2832  O   PRO B  49      58.213  37.692  69.118  1.00 29.93           O  
-ATOM   2833  CB  PRO B  49      58.299  36.207  71.442  1.00 17.60           C  
-ATOM   2834  CG  PRO B  49      58.101  34.900  70.730  1.00 16.96           C  
-ATOM   2835  CD  PRO B  49      56.659  34.556  71.038  1.00 11.76           C  
-ATOM   2836  N   LEU B  50      56.054  38.306  69.292  1.00 27.29           N  
-ATOM   2837  CA  LEU B  50      56.065  39.032  68.022  1.00 28.04           C  
-ATOM   2838  C   LEU B  50      57.226  40.009  67.950  1.00 22.89           C  
-ATOM   2839  O   LEU B  50      57.900  40.106  66.926  1.00 23.84           O  
-ATOM   2840  CB  LEU B  50      54.772  39.817  67.828  1.00 26.30           C  
-ATOM   2841  CG  LEU B  50      53.449  39.097  68.054  1.00 34.75           C  
-ATOM   2842  CD1 LEU B  50      52.327  40.022  67.613  1.00 39.77           C  
-ATOM   2843  CD2 LEU B  50      53.406  37.785  67.273  1.00 36.17           C  
-ATOM   2844  N   SER B  51      57.446  40.734  69.042  1.00 18.82           N  
-ATOM   2845  CA  SER B  51      58.517  41.711  69.103  1.00 19.03           C  
-ATOM   2846  C   SER B  51      59.857  41.163  68.613  1.00 25.34           C  
-ATOM   2847  O   SER B  51      60.666  41.923  68.089  1.00 34.72           O  
-ATOM   2848  CB  SER B  51      58.652  42.254  70.523  1.00 28.38           C  
-ATOM   2849  OG  SER B  51      58.579  41.207  71.479  1.00 52.81           O  
-ATOM   2850  N   TYR B  52      60.110  39.863  68.777  1.00 19.95           N  
-ATOM   2851  CA  TYR B  52      61.372  39.303  68.290  1.00 11.42           C  
-ATOM   2852  C   TYR B  52      61.221  38.795  66.860  1.00 11.47           C  
-ATOM   2853  O   TYR B  52      62.150  38.885  66.059  1.00 10.70           O  
-ATOM   2854  CB  TYR B  52      61.862  38.168  69.182  1.00  5.64           C  
-ATOM   2855  CG  TYR B  52      62.448  38.622  70.503  1.00 15.28           C  
-ATOM   2856  CD1 TYR B  52      61.618  38.996  71.563  1.00 18.39           C  
-ATOM   2857  CD2 TYR B  52      63.835  38.655  70.708  1.00 10.08           C  
-ATOM   2858  CE1 TYR B  52      62.148  39.388  72.798  1.00 18.44           C  
-ATOM   2859  CE2 TYR B  52      64.374  39.046  71.939  1.00 11.26           C  
-ATOM   2860  CZ  TYR B  52      63.520  39.410  72.981  1.00 18.50           C  
-ATOM   2861  OH  TYR B  52      64.016  39.791  74.210  1.00 21.97           O  
-ATOM   2862  N   TRP B  53      60.048  38.261  66.538  1.00  9.10           N  
-ATOM   2863  CA  TRP B  53      59.816  37.762  65.198  1.00  4.47           C  
-ATOM   2864  C   TRP B  53      59.863  38.909  64.222  1.00 11.60           C  
-ATOM   2865  O   TRP B  53      60.403  38.782  63.132  1.00 23.42           O  
-ATOM   2866  CB  TRP B  53      58.455  37.085  65.082  1.00  8.40           C  
-ATOM   2867  CG  TRP B  53      58.322  35.804  65.851  1.00 15.29           C  
-ATOM   2868  CD1 TRP B  53      59.327  35.026  66.352  1.00 16.70           C  
-ATOM   2869  CD2 TRP B  53      57.104  35.147  66.191  1.00 12.16           C  
-ATOM   2870  NE1 TRP B  53      58.806  33.926  66.989  1.00  4.47           N  
-ATOM   2871  CE2 TRP B  53      57.443  33.978  66.905  1.00  8.33           C  
-ATOM   2872  CE3 TRP B  53      55.753  35.433  65.961  1.00 14.44           C  
-ATOM   2873  CZ2 TRP B  53      56.482  33.100  67.394  1.00 18.52           C  
-ATOM   2874  CZ3 TRP B  53      54.793  34.556  66.445  1.00 11.47           C  
-ATOM   2875  CH2 TRP B  53      55.162  33.404  67.155  1.00 19.03           C  
-ATOM   2876  N   ARG B  54      59.300  40.044  64.605  1.00 12.09           N  
-ATOM   2877  CA  ARG B  54      59.298  41.178  63.701  1.00  5.87           C  
-ATOM   2878  C   ARG B  54      60.594  41.940  63.681  1.00 10.22           C  
-ATOM   2879  O   ARG B  54      60.686  42.978  63.048  1.00 22.21           O  
-ATOM   2880  CB  ARG B  54      58.135  42.113  64.012  1.00  4.86           C  
-ATOM   2881  CG  ARG B  54      56.822  41.566  63.475  1.00 26.42           C  
-ATOM   2882  CD  ARG B  54      55.729  42.625  63.397  1.00 40.08           C  
-ATOM   2883  NE  ARG B  54      54.515  42.105  62.766  1.00 44.76           N  
-ATOM   2884  CZ  ARG B  54      54.444  41.693  61.502  1.00 49.99           C  
-ATOM   2885  NH1 ARG B  54      55.515  41.738  60.720  1.00 50.27           N  
-ATOM   2886  NH2 ARG B  54      53.298  41.235  61.016  1.00 53.63           N  
-ATOM   2887  N   ASN B  55      61.599  41.426  64.376  1.00 10.89           N  
-ATOM   2888  CA  ASN B  55      62.913  42.061  64.399  1.00 14.96           C  
-ATOM   2889  C   ASN B  55      63.912  41.081  64.971  1.00 10.14           C  
-ATOM   2890  O   ASN B  55      64.624  41.363  65.940  1.00 14.70           O  
-ATOM   2891  CB  ASN B  55      62.902  43.334  65.244  1.00 30.72           C  
-ATOM   2892  CG  ASN B  55      64.282  43.974  65.347  1.00 36.46           C  
-ATOM   2893  OD1 ASN B  55      64.872  44.358  64.331  1.00 17.97           O  
-ATOM   2894  ND2 ASN B  55      64.807  44.082  66.579  1.00 45.95           N  
-ATOM   2895  N   LEU B  56      63.965  39.908  64.369  1.00  4.47           N  
-ATOM   2896  CA  LEU B  56      64.874  38.936  64.873  1.00  4.47           C  
-ATOM   2897  C   LEU B  56      66.235  39.168  64.294  1.00  4.47           C  
-ATOM   2898  O   LEU B  56      66.502  38.780  63.169  1.00  5.95           O  
-ATOM   2899  CB  LEU B  56      64.387  37.539  64.556  1.00  4.47           C  
-ATOM   2900  CG  LEU B  56      65.112  36.553  65.480  1.00 14.50           C  
-ATOM   2901  CD1 LEU B  56      64.271  35.299  65.717  1.00 17.60           C  
-ATOM   2902  CD2 LEU B  56      66.482  36.232  64.879  1.00 11.46           C  
-ATOM   2903  N   ALA B  57      67.093  39.807  65.081  1.00  8.73           N  
-ATOM   2904  CA  ALA B  57      68.456  40.088  64.663  1.00 13.52           C  
-ATOM   2905  C   ALA B  57      68.509  40.759  63.300  1.00 11.46           C  
-ATOM   2906  O   ALA B  57      69.419  40.494  62.508  1.00 18.06           O  
-ATOM   2907  CB  ALA B  57      69.276  38.797  64.649  1.00 12.14           C  
-ATOM   2908  N   GLY B  58      67.523  41.605  63.016  1.00  5.76           N  
-ATOM   2909  CA  GLY B  58      67.533  42.322  61.756  1.00 14.85           C  
-ATOM   2910  C   GLY B  58      66.446  42.046  60.737  1.00 22.51           C  
-ATOM   2911  O   GLY B  58      66.036  42.959  60.018  1.00 30.85           O  
-ATOM   2912  N   GLU B  59      65.971  40.809  60.645  1.00 19.54           N  
-ATOM   2913  CA  GLU B  59      64.946  40.509  59.661  1.00 10.22           C  
-ATOM   2914  C   GLU B  59      63.581  40.255  60.309  1.00 11.09           C  
-ATOM   2915  O   GLU B  59      63.487  39.895  61.485  1.00 12.49           O  
-ATOM   2916  CB  GLU B  59      65.407  39.324  58.798  1.00  9.11           C  
-ATOM   2917  CG  GLU B  59      66.865  39.471  58.338  1.00 11.60           C  
-ATOM   2918  CD  GLU B  59      67.288  38.479  57.261  1.00 21.99           C  
-ATOM   2919  OE1 GLU B  59      67.054  37.254  57.412  1.00 14.41           O  
-ATOM   2920  OE2 GLU B  59      67.875  38.939  56.259  1.00 28.42           O  
-ATOM   2921  N   ASP B  60      62.524  40.480  59.540  1.00 12.93           N  
-ATOM   2922  CA  ASP B  60      61.161  40.280  60.016  1.00 13.77           C  
-ATOM   2923  C   ASP B  60      60.637  38.928  59.548  1.00  6.49           C  
-ATOM   2924  O   ASP B  60      60.006  38.839  58.512  1.00  8.92           O  
-ATOM   2925  CB  ASP B  60      60.256  41.376  59.464  1.00 21.83           C  
-ATOM   2926  CG  ASP B  60      58.804  41.195  59.868  1.00 28.46           C  
-ATOM   2927  OD1 ASP B  60      58.246  40.092  59.674  1.00 24.51           O  
-ATOM   2928  OD2 ASP B  60      58.215  42.167  60.377  1.00 34.25           O  
-ATOM   2929  N   ALA B  61      60.885  37.881  60.316  1.00  4.47           N  
-ATOM   2930  CA  ALA B  61      60.439  36.556  59.934  1.00  4.47           C  
-ATOM   2931  C   ALA B  61      59.088  36.561  59.234  1.00 12.10           C  
-ATOM   2932  O   ALA B  61      58.961  36.036  58.128  1.00 20.51           O  
-ATOM   2933  CB  ALA B  61      60.383  35.639  61.150  1.00  4.47           C  
-ATOM   2934  N   ILE B  62      58.076  37.163  59.847  1.00 10.21           N  
-ATOM   2935  CA  ILE B  62      56.760  37.147  59.231  1.00  5.47           C  
-ATOM   2936  C   ILE B  62      56.694  37.694  57.813  1.00  5.64           C  
-ATOM   2937  O   ILE B  62      56.324  36.979  56.886  1.00  4.47           O  
-ATOM   2938  CB  ILE B  62      55.736  37.863  60.103  1.00 11.04           C  
-ATOM   2939  CG1 ILE B  62      55.393  36.965  61.304  1.00 18.01           C  
-ATOM   2940  CG2 ILE B  62      54.502  38.191  59.283  1.00  6.42           C  
-ATOM   2941  CD1 ILE B  62      54.201  37.408  62.129  1.00 16.01           C  
-ATOM   2942  N   CYS B  63      57.041  38.960  57.636  1.00 16.14           N  
-ATOM   2943  CA  CYS B  63      57.022  39.557  56.305  1.00 16.22           C  
-ATOM   2944  C   CYS B  63      57.812  38.669  55.329  1.00 14.15           C  
-ATOM   2945  O   CYS B  63      57.323  38.324  54.258  1.00 16.84           O  
-ATOM   2946  CB  CYS B  63      57.628  40.967  56.358  1.00 29.13           C  
-ATOM   2947  SG  CYS B  63      57.481  41.948  54.837  1.00 56.70           S  
-ATOM   2948  N   GLY B  64      59.024  38.285  55.724  1.00 17.13           N  
-ATOM   2949  CA  GLY B  64      59.872  37.447  54.893  1.00  9.48           C  
-ATOM   2950  C   GLY B  64      59.276  36.121  54.465  1.00  5.29           C  
-ATOM   2951  O   GLY B  64      59.483  35.672  53.343  1.00  6.47           O  
-ATOM   2952  N   ILE B  65      58.529  35.476  55.342  1.00  7.00           N  
-ATOM   2953  CA  ILE B  65      57.960  34.210  54.950  1.00  4.47           C  
-ATOM   2954  C   ILE B  65      56.870  34.464  53.946  1.00  4.47           C  
-ATOM   2955  O   ILE B  65      56.715  33.703  53.005  1.00 14.71           O  
-ATOM   2956  CB  ILE B  65      57.381  33.433  56.135  1.00  4.47           C  
-ATOM   2957  CG1 ILE B  65      57.058  32.004  55.696  1.00 12.78           C  
-ATOM   2958  CG2 ILE B  65      56.115  34.097  56.621  1.00 11.68           C  
-ATOM   2959  CD1 ILE B  65      57.320  30.941  56.760  1.00 21.85           C  
-ATOM   2960  N   TYR B  66      56.113  35.536  54.117  1.00  4.47           N  
-ATOM   2961  CA  TYR B  66      55.053  35.784  53.156  1.00 13.97           C  
-ATOM   2962  C   TYR B  66      55.578  36.441  51.890  1.00 19.31           C  
-ATOM   2963  O   TYR B  66      55.380  35.925  50.784  1.00 19.92           O  
-ATOM   2964  CB  TYR B  66      53.930  36.620  53.783  1.00 26.89           C  
-ATOM   2965  CG  TYR B  66      53.131  35.845  54.822  1.00 36.84           C  
-ATOM   2966  CD1 TYR B  66      53.233  36.149  56.184  1.00 34.98           C  
-ATOM   2967  CD2 TYR B  66      52.323  34.760  54.448  1.00 41.16           C  
-ATOM   2968  CE1 TYR B  66      52.558  35.390  57.150  1.00 36.01           C  
-ATOM   2969  CE2 TYR B  66      51.644  33.993  55.408  1.00 40.43           C  
-ATOM   2970  CZ  TYR B  66      51.771  34.313  56.757  1.00 39.46           C  
-ATOM   2971  OH  TYR B  66      51.145  33.543  57.719  1.00 40.10           O  
-ATOM   2972  N   GLY B  67      56.255  37.571  52.046  1.00 20.14           N  
-ATOM   2973  CA  GLY B  67      56.801  38.256  50.889  1.00 20.33           C  
-ATOM   2974  C   GLY B  67      57.513  37.307  49.934  1.00 20.94           C  
-ATOM   2975  O   GLY B  67      57.406  37.448  48.717  1.00 18.67           O  
-ATOM   2976  N   THR B  68      58.236  36.333  50.482  1.00 18.01           N  
-ATOM   2977  CA  THR B  68      58.956  35.389  49.659  1.00  4.47           C  
-ATOM   2978  C   THR B  68      58.007  34.662  48.745  1.00 11.15           C  
-ATOM   2979  O   THR B  68      58.364  34.339  47.611  1.00 18.13           O  
-ATOM   2980  CB  THR B  68      59.715  34.394  50.506  1.00  4.47           C  
-ATOM   2981  OG1 THR B  68      60.925  35.009  50.954  1.00  4.47           O  
-ATOM   2982  CG2 THR B  68      60.055  33.151  49.705  1.00  8.23           C  
-ATOM   2983  N   GLN B  69      56.790  34.405  49.210  1.00 13.27           N  
-ATOM   2984  CA  GLN B  69      55.841  33.715  48.347  1.00 20.18           C  
-ATOM   2985  C   GLN B  69      55.357  34.669  47.255  1.00 22.79           C  
-ATOM   2986  O   GLN B  69      55.271  34.295  46.075  1.00 27.14           O  
-ATOM   2987  CB  GLN B  69      54.668  33.163  49.159  1.00 12.36           C  
-ATOM   2988  CG  GLN B  69      55.090  32.167  50.229  1.00 21.51           C  
-ATOM   2989  CD  GLN B  69      56.216  31.240  49.779  1.00 32.02           C  
-ATOM   2990  OE1 GLN B  69      56.135  30.599  48.722  1.00 39.83           O  
-ATOM   2991  NE2 GLN B  69      57.275  31.162  50.587  1.00 26.53           N  
-ATOM   2992  N   THR B  70      55.057  35.906  47.638  1.00 18.39           N  
-ATOM   2993  CA  THR B  70      54.617  36.885  46.653  1.00 19.77           C  
-ATOM   2994  C   THR B  70      55.741  37.033  45.625  1.00 14.61           C  
-ATOM   2995  O   THR B  70      55.501  37.087  44.420  1.00 12.15           O  
-ATOM   2996  CB  THR B  70      54.351  38.253  47.297  1.00 27.07           C  
-ATOM   2997  OG1 THR B  70      53.380  38.117  48.341  1.00 37.41           O  
-ATOM   2998  CG2 THR B  70      53.831  39.220  46.261  1.00 26.50           C  
-ATOM   2999  N   ARG B  71      56.975  37.073  46.115  1.00  7.13           N  
-ATOM   3000  CA  ARG B  71      58.135  37.212  45.251  1.00  4.47           C  
-ATOM   3001  C   ARG B  71      58.305  36.006  44.360  1.00  4.47           C  
-ATOM   3002  O   ARG B  71      58.935  36.096  43.309  1.00  8.64           O  
-ATOM   3003  CB  ARG B  71      59.391  37.417  46.089  1.00  4.47           C  
-ATOM   3004  CG  ARG B  71      60.036  38.772  45.887  1.00 11.22           C  
-ATOM   3005  CD  ARG B  71      60.908  39.163  47.062  1.00  4.47           C  
-ATOM   3006  NE  ARG B  71      62.120  38.351  47.179  1.00 12.98           N  
-ATOM   3007  CZ  ARG B  71      63.200  38.497  46.419  1.00  5.35           C  
-ATOM   3008  NH1 ARG B  71      63.214  39.425  45.476  1.00 24.72           N  
-ATOM   3009  NH2 ARG B  71      64.270  37.740  46.618  1.00  4.47           N  
-ATOM   3010  N   ARG B  72      57.753  34.873  44.780  1.00  4.47           N  
-ATOM   3011  CA  ARG B  72      57.843  33.664  43.978  1.00  4.47           C  
-ATOM   3012  C   ARG B  72      56.834  33.695  42.847  1.00 10.53           C  
-ATOM   3013  O   ARG B  72      57.158  33.316  41.726  1.00 23.64           O  
-ATOM   3014  CB  ARG B  72      57.597  32.426  44.818  1.00  8.29           C  
-ATOM   3015  CG  ARG B  72      57.395  31.167  44.000  1.00  8.77           C  
-ATOM   3016  CD  ARG B  72      57.489  29.947  44.893  1.00 23.87           C  
-ATOM   3017  NE  ARG B  72      57.186  28.718  44.172  1.00 44.37           N  
-ATOM   3018  CZ  ARG B  72      57.273  27.502  44.706  1.00 50.31           C  
-ATOM   3019  NH1 ARG B  72      57.661  27.365  45.969  1.00 53.67           N  
-ATOM   3020  NH2 ARG B  72      56.954  26.426  43.989  1.00 46.48           N  
-ATOM   3021  N   LEU B  73      55.614  34.148  43.132  1.00  9.64           N  
-ATOM   3022  CA  LEU B  73      54.571  34.218  42.102  1.00 12.92           C  
-ATOM   3023  C   LEU B  73      54.894  35.193  40.985  1.00 17.86           C  
-ATOM   3024  O   LEU B  73      54.555  34.956  39.824  1.00 15.51           O  
-ATOM   3025  CB  LEU B  73      53.234  34.608  42.721  1.00 14.40           C  
-ATOM   3026  CG  LEU B  73      52.474  33.477  43.409  1.00 33.43           C  
-ATOM   3027  CD1 LEU B  73      53.438  32.452  44.028  1.00 35.13           C  
-ATOM   3028  CD2 LEU B  73      51.560  34.088  44.462  1.00 41.06           C  
-ATOM   3029  N   ASN B  74      55.542  36.297  41.341  1.00 20.35           N  
-ATOM   3030  CA  ASN B  74      55.911  37.312  40.364  1.00 21.29           C  
-ATOM   3031  C   ASN B  74      57.152  36.909  39.598  1.00 18.60           C  
-ATOM   3032  O   ASN B  74      57.572  37.606  38.676  1.00 23.66           O  
-ATOM   3033  CB  ASN B  74      56.152  38.636  41.065  1.00 27.59           C  
-ATOM   3034  CG  ASN B  74      54.935  39.104  41.821  1.00 46.43           C  
-ATOM   3035  OD1 ASN B  74      55.030  39.955  42.715  1.00 60.90           O  
-ATOM   3036  ND2 ASN B  74      53.769  38.554  41.465  1.00 42.99           N  
-ATOM   3037  N   GLY B  75      57.734  35.779  39.978  1.00 10.44           N  
-ATOM   3038  CA  GLY B  75      58.923  35.308  39.302  1.00 14.92           C  
-ATOM   3039  C   GLY B  75      60.117  36.200  39.573  1.00 17.29           C  
-ATOM   3040  O   GLY B  75      61.089  36.219  38.809  1.00 11.80           O  
-ATOM   3041  N   ASP B  76      60.048  36.956  40.663  1.00 21.97           N  
-ATOM   3042  CA  ASP B  76      61.155  37.832  41.018  1.00 28.45           C  
-ATOM   3043  C   ASP B  76      62.310  36.942  41.458  1.00 21.48           C  
-ATOM   3044  O   ASP B  76      63.461  37.370  41.502  1.00 22.91           O  
-ATOM   3045  CB  ASP B  76      60.759  38.794  42.153  1.00 35.54           C  
-ATOM   3046  CG  ASP B  76      59.871  39.950  41.677  1.00 52.16           C  
-ATOM   3047  OD1 ASP B  76      59.456  40.766  42.532  1.00 53.04           O  
-ATOM   3048  OD2 ASP B  76      59.590  40.048  40.457  1.00 63.35           O  
-ATOM   3049  N   VAL B  77      61.994  35.689  41.768  1.00 20.45           N  
-ATOM   3050  CA  VAL B  77      63.014  34.745  42.217  1.00 16.59           C  
-ATOM   3051  C   VAL B  77      62.699  33.289  41.857  1.00 15.43           C  
-ATOM   3052  O   VAL B  77      61.539  32.869  41.831  1.00 21.04           O  
-ATOM   3053  CB  VAL B  77      63.204  34.824  43.732  1.00  8.27           C  
-ATOM   3054  CG1 VAL B  77      62.049  34.123  44.441  1.00  7.89           C  
-ATOM   3055  CG2 VAL B  77      64.526  34.220  44.100  1.00 10.75           C  
-ATOM   3056  N   SER B  78      63.750  32.525  41.590  1.00  9.65           N  
-ATOM   3057  CA  SER B  78      63.621  31.120  41.225  1.00 11.24           C  
-ATOM   3058  C   SER B  78      62.806  30.346  42.259  1.00 11.99           C  
-ATOM   3059  O   SER B  78      62.955  30.571  43.454  1.00 26.05           O  
-ATOM   3060  CB  SER B  78      65.024  30.508  41.098  1.00 17.06           C  
-ATOM   3061  OG  SER B  78      64.975  29.102  40.919  1.00 33.20           O  
-ATOM   3062  N   PRO B  79      61.935  29.420  41.819  1.00 11.02           N  
-ATOM   3063  CA  PRO B  79      61.127  28.640  42.767  1.00 15.64           C  
-ATOM   3064  C   PRO B  79      62.047  27.781  43.634  1.00 19.70           C  
-ATOM   3065  O   PRO B  79      61.708  27.434  44.770  1.00 15.55           O  
-ATOM   3066  CB  PRO B  79      60.240  27.804  41.857  1.00  4.47           C  
-ATOM   3067  CG  PRO B  79      61.145  27.536  40.723  1.00 15.56           C  
-ATOM   3068  CD  PRO B  79      61.770  28.894  40.458  1.00 18.37           C  
-ATOM   3069  N   GLU B  80      63.218  27.446  43.094  1.00 20.16           N  
-ATOM   3070  CA  GLU B  80      64.187  26.660  43.842  1.00 20.01           C  
-ATOM   3071  C   GLU B  80      64.730  27.522  44.993  1.00 15.68           C  
-ATOM   3072  O   GLU B  80      64.861  27.047  46.120  1.00 18.82           O  
-ATOM   3073  CB  GLU B  80      65.330  26.192  42.929  1.00 24.36           C  
-ATOM   3074  CG  GLU B  80      66.275  25.194  43.595  1.00 43.47           C  
-ATOM   3075  CD  GLU B  80      67.295  24.578  42.631  1.00 58.55           C  
-ATOM   3076  OE1 GLU B  80      66.881  23.938  41.638  1.00 59.36           O  
-ATOM   3077  OE2 GLU B  80      68.516  24.724  42.873  1.00 67.08           O  
-ATOM   3078  N   ASP B  81      65.033  28.789  44.728  1.00  4.47           N  
-ATOM   3079  CA  ASP B  81      65.533  29.645  45.791  1.00  4.47           C  
-ATOM   3080  C   ASP B  81      64.404  30.020  46.730  1.00  4.47           C  
-ATOM   3081  O   ASP B  81      64.578  30.071  47.942  1.00 13.66           O  
-ATOM   3082  CB  ASP B  81      66.159  30.921  45.239  1.00  4.47           C  
-ATOM   3083  CG  ASP B  81      67.364  30.657  44.358  1.00 11.99           C  
-ATOM   3084  OD1 ASP B  81      68.228  29.834  44.721  1.00 22.92           O  
-ATOM   3085  OD2 ASP B  81      67.462  31.291  43.292  1.00 23.21           O  
-ATOM   3086  N   ALA B  82      63.233  30.283  46.175  1.00  6.26           N  
-ATOM   3087  CA  ALA B  82      62.090  30.659  46.996  1.00 13.82           C  
-ATOM   3088  C   ALA B  82      61.870  29.639  48.105  1.00 17.43           C  
-ATOM   3089  O   ALA B  82      61.393  29.987  49.185  1.00 11.41           O  
-ATOM   3090  CB  ALA B  82      60.836  30.773  46.133  1.00 16.63           C  
-ATOM   3091  N   GLN B  83      62.212  28.379  47.834  1.00 21.36           N  
-ATOM   3092  CA  GLN B  83      62.042  27.319  48.829  1.00 20.64           C  
-ATOM   3093  C   GLN B  83      63.095  27.446  49.899  1.00 12.99           C  
-ATOM   3094  O   GLN B  83      62.783  27.420  51.080  1.00 18.04           O  
-ATOM   3095  CB  GLN B  83      62.142  25.934  48.191  1.00 21.61           C  
-ATOM   3096  CG  GLN B  83      61.150  25.722  47.070  1.00 22.47           C  
-ATOM   3097  CD  GLN B  83      60.944  24.264  46.743  1.00 18.72           C  
-ATOM   3098  OE1 GLN B  83      61.895  23.544  46.435  1.00 14.64           O  
-ATOM   3099  NE2 GLN B  83      59.693  23.818  46.805  1.00 19.96           N  
-ATOM   3100  N   ARG B  84      64.345  27.576  49.479  1.00  4.56           N  
-ATOM   3101  CA  ARG B  84      65.435  27.729  50.417  1.00  4.47           C  
-ATOM   3102  C   ARG B  84      65.219  28.992  51.202  1.00  4.47           C  
-ATOM   3103  O   ARG B  84      65.350  29.006  52.426  1.00  4.47           O  
-ATOM   3104  CB  ARG B  84      66.748  27.795  49.667  1.00  4.47           C  
-ATOM   3105  CG  ARG B  84      67.065  26.472  49.044  1.00  8.36           C  
-ATOM   3106  CD  ARG B  84      68.076  26.554  47.937  1.00  5.98           C  
-ATOM   3107  NE  ARG B  84      68.183  25.251  47.300  1.00  9.89           N  
-ATOM   3108  CZ  ARG B  84      68.873  25.017  46.196  1.00 20.08           C  
-ATOM   3109  NH1 ARG B  84      69.521  26.014  45.611  1.00 31.35           N  
-ATOM   3110  NH2 ARG B  84      68.909  23.792  45.678  1.00 27.14           N  
-ATOM   3111  N   LEU B  85      64.870  30.055  50.485  1.00  8.52           N  
-ATOM   3112  CA  LEU B  85      64.621  31.347  51.101  1.00  6.83           C  
-ATOM   3113  C   LEU B  85      63.549  31.213  52.186  1.00 14.42           C  
-ATOM   3114  O   LEU B  85      63.646  31.832  53.243  1.00 12.20           O  
-ATOM   3115  CB  LEU B  85      64.192  32.339  50.028  1.00  4.47           C  
-ATOM   3116  CG  LEU B  85      65.019  33.620  50.041  1.00 10.82           C  
-ATOM   3117  CD1 LEU B  85      66.483  33.270  50.185  1.00  4.47           C  
-ATOM   3118  CD2 LEU B  85      64.759  34.422  48.770  1.00 10.52           C  
-ATOM   3119  N   THR B  86      62.537  30.386  51.929  1.00 18.36           N  
-ATOM   3120  CA  THR B  86      61.472  30.169  52.901  1.00 10.89           C  
-ATOM   3121  C   THR B  86      62.053  29.513  54.149  1.00  4.47           C  
-ATOM   3122  O   THR B  86      61.904  30.020  55.259  1.00  4.47           O  
-ATOM   3123  CB  THR B  86      60.357  29.259  52.331  1.00 15.67           C  
-ATOM   3124  OG1 THR B  86      59.788  29.867  51.158  1.00 16.42           O  
-ATOM   3125  CG2 THR B  86      59.257  29.044  53.377  1.00 13.61           C  
-ATOM   3126  N   ALA B  87      62.725  28.387  53.958  1.00  4.47           N  
-ATOM   3127  CA  ALA B  87      63.322  27.672  55.070  1.00  4.47           C  
-ATOM   3128  C   ALA B  87      63.999  28.660  55.978  1.00  4.47           C  
-ATOM   3129  O   ALA B  87      63.837  28.615  57.187  1.00  4.93           O  
-ATOM   3130  CB  ALA B  87      64.334  26.665  54.565  1.00 14.20           C  
-ATOM   3131  N   HIS B  88      64.758  29.567  55.385  1.00  7.94           N  
-ATOM   3132  CA  HIS B  88      65.469  30.563  56.165  1.00  8.64           C  
-ATOM   3133  C   HIS B  88      64.561  31.285  57.139  1.00 13.46           C  
-ATOM   3134  O   HIS B  88      64.766  31.213  58.351  1.00 22.08           O  
-ATOM   3135  CB  HIS B  88      66.108  31.587  55.259  1.00  4.47           C  
-ATOM   3136  CG  HIS B  88      66.703  32.728  56.003  1.00  4.47           C  
-ATOM   3137  ND1 HIS B  88      67.808  32.586  56.813  1.00 12.65           N  
-ATOM   3138  CD2 HIS B  88      66.331  34.025  56.087  1.00  4.47           C  
-ATOM   3139  CE1 HIS B  88      68.093  33.753  57.361  1.00 18.31           C  
-ATOM   3140  NE2 HIS B  88      67.212  34.643  56.936  1.00  8.71           N  
-ATOM   3141  N   PHE B  89      63.566  31.994  56.608  1.00 10.73           N  
-ATOM   3142  CA  PHE B  89      62.624  32.731  57.446  1.00  4.47           C  
-ATOM   3143  C   PHE B  89      61.885  31.841  58.415  1.00  4.47           C  
-ATOM   3144  O   PHE B  89      61.880  32.096  59.607  1.00  4.47           O  
-ATOM   3145  CB  PHE B  89      61.622  33.474  56.592  1.00  4.47           C  
-ATOM   3146  CG  PHE B  89      62.234  34.548  55.768  1.00  4.47           C  
-ATOM   3147  CD1 PHE B  89      62.371  34.403  54.398  1.00  7.74           C  
-ATOM   3148  CD2 PHE B  89      62.691  35.707  56.363  1.00  4.47           C  
-ATOM   3149  CE1 PHE B  89      62.958  35.407  53.642  1.00  4.47           C  
-ATOM   3150  CE2 PHE B  89      63.274  36.708  55.616  1.00  4.47           C  
-ATOM   3151  CZ  PHE B  89      63.410  36.561  54.257  1.00  4.47           C  
-ATOM   3152  N   GLN B  90      61.260  30.788  57.911  1.00  4.53           N  
-ATOM   3153  CA  GLN B  90      60.543  29.881  58.794  1.00 13.90           C  
-ATOM   3154  C   GLN B  90      61.368  29.569  60.050  1.00 13.93           C  
-ATOM   3155  O   GLN B  90      60.861  29.609  61.169  1.00 15.21           O  
-ATOM   3156  CB  GLN B  90      60.210  28.589  58.055  1.00 10.76           C  
-ATOM   3157  CG  GLN B  90      59.696  27.475  58.947  1.00 14.96           C  
-ATOM   3158  CD  GLN B  90      58.610  27.933  59.907  1.00 13.46           C  
-ATOM   3159  OE1 GLN B  90      57.780  28.791  59.583  1.00  4.47           O  
-ATOM   3160  NE2 GLN B  90      58.603  27.339  61.097  1.00 17.77           N  
-ATOM   3161  N   SER B  91      62.647  29.279  59.849  1.00 17.49           N  
-ATOM   3162  CA  SER B  91      63.551  28.959  60.944  1.00 14.03           C  
-ATOM   3163  C   SER B  91      63.640  30.065  61.974  1.00  8.60           C  
-ATOM   3164  O   SER B  91      63.839  29.783  63.154  1.00 15.67           O  
-ATOM   3165  CB  SER B  91      64.965  28.704  60.426  1.00 20.69           C  
-ATOM   3166  OG  SER B  91      65.723  29.911  60.400  1.00 18.31           O  
-ATOM   3167  N   LEU B  92      63.527  31.318  61.536  1.00  4.47           N  
-ATOM   3168  CA  LEU B  92      63.621  32.443  62.468  1.00  5.70           C  
-ATOM   3169  C   LEU B  92      62.695  32.350  63.673  1.00 13.21           C  
-ATOM   3170  O   LEU B  92      63.066  32.771  64.770  1.00 17.64           O  
-ATOM   3171  CB  LEU B  92      63.352  33.758  61.766  1.00  4.47           C  
-ATOM   3172  CG  LEU B  92      64.456  34.195  60.823  1.00  6.33           C  
-ATOM   3173  CD1 LEU B  92      64.061  35.502  60.153  1.00 19.01           C  
-ATOM   3174  CD2 LEU B  92      65.735  34.373  61.592  1.00  4.47           C  
-ATOM   3175  N   PHE B  93      61.501  31.796  63.467  1.00  8.53           N  
-ATOM   3176  CA  PHE B  93      60.508  31.642  64.525  1.00  8.29           C  
-ATOM   3177  C   PHE B  93      60.971  30.774  65.698  1.00 14.26           C  
-ATOM   3178  O   PHE B  93      60.468  30.911  66.819  1.00 28.28           O  
-ATOM   3179  CB  PHE B  93      59.231  31.041  63.943  1.00 11.09           C  
-ATOM   3180  CG  PHE B  93      58.469  31.975  63.046  1.00 17.93           C  
-ATOM   3181  CD1 PHE B  93      57.675  32.992  63.580  1.00 23.87           C  
-ATOM   3182  CD2 PHE B  93      58.552  31.851  61.667  1.00  5.50           C  
-ATOM   3183  CE1 PHE B  93      56.974  33.869  62.743  1.00 20.09           C  
-ATOM   3184  CE2 PHE B  93      57.857  32.727  60.830  1.00 10.70           C  
-ATOM   3185  CZ  PHE B  93      57.069  33.733  61.366  1.00  6.01           C  
-ATOM   3186  N   CYS B  94      61.933  29.893  65.445  1.00 11.39           N  
-ATOM   3187  CA  CYS B  94      62.438  28.976  66.467  1.00 16.69           C  
-ATOM   3188  C   CYS B  94      63.074  29.543  67.749  1.00 13.41           C  
-ATOM   3189  O   CYS B  94      62.546  29.373  68.846  1.00 15.43           O  
-ATOM   3190  CB  CYS B  94      63.401  27.983  65.804  1.00 16.96           C  
-ATOM   3191  SG  CYS B  94      62.586  26.892  64.588  1.00  7.82           S  
-ATOM   3192  N   SER B  95      64.205  30.215  67.611  1.00 20.14           N  
-ATOM   3193  CA  SER B  95      64.925  30.756  68.764  1.00 18.62           C  
-ATOM   3194  C   SER B  95      64.143  31.323  69.945  1.00 15.56           C  
-ATOM   3195  O   SER B  95      64.234  30.793  71.050  1.00 18.92           O  
-ATOM   3196  CB  SER B  95      65.956  31.796  68.299  1.00 18.12           C  
-ATOM   3197  OG  SER B  95      65.451  32.571  67.222  1.00 31.09           O  
-ATOM   3198  N   PRO B  96      63.353  32.388  69.734  1.00 18.18           N  
-ATOM   3199  CA  PRO B  96      62.592  32.987  70.840  1.00  9.27           C  
-ATOM   3200  C   PRO B  96      61.908  31.940  71.675  1.00 13.42           C  
-ATOM   3201  O   PRO B  96      62.237  31.752  72.842  1.00 18.76           O  
-ATOM   3202  CB  PRO B  96      61.582  33.884  70.138  1.00  4.77           C  
-ATOM   3203  CG  PRO B  96      62.252  34.206  68.849  1.00 22.49           C  
-ATOM   3204  CD  PRO B  96      62.850  32.878  68.445  1.00 17.93           C  
-ATOM   3205  N   HIS B  97      60.963  31.245  71.061  1.00  8.37           N  
-ATOM   3206  CA  HIS B  97      60.223  30.226  71.769  1.00 12.27           C  
-ATOM   3207  C   HIS B  97      61.089  29.196  72.447  1.00 16.86           C  
-ATOM   3208  O   HIS B  97      60.719  28.680  73.499  1.00 25.79           O  
-ATOM   3209  CB  HIS B  97      59.268  29.522  70.827  1.00 25.36           C  
-ATOM   3210  CG  HIS B  97      57.835  29.861  71.075  1.00 32.90           C  
-ATOM   3211  ND1 HIS B  97      57.230  29.677  72.301  1.00 28.22           N  
-ATOM   3212  CD2 HIS B  97      56.889  30.379  70.258  1.00 28.80           C  
-ATOM   3213  CE1 HIS B  97      55.971  30.067  72.225  1.00 40.06           C  
-ATOM   3214  NE2 HIS B  97      55.738  30.497  70.996  1.00 39.15           N  
-ATOM   3215  N   ALA B  98      62.239  28.900  71.847  1.00 17.61           N  
-ATOM   3216  CA  ALA B  98      63.166  27.906  72.387  1.00  6.85           C  
-ATOM   3217  C   ALA B  98      63.964  28.407  73.575  1.00  7.22           C  
-ATOM   3218  O   ALA B  98      64.085  27.692  74.567  1.00 13.44           O  
-ATOM   3219  CB  ALA B  98      64.099  27.440  71.306  1.00 17.02           C  
-ATOM   3220  N   ILE B  99      64.514  29.621  73.476  1.00  4.96           N  
-ATOM   3221  CA  ILE B  99      65.290  30.196  74.576  1.00  4.47           C  
-ATOM   3222  C   ILE B  99      64.437  30.091  75.825  1.00  8.84           C  
-ATOM   3223  O   ILE B  99      64.906  29.657  76.873  1.00 16.75           O  
-ATOM   3224  CB  ILE B  99      65.585  31.685  74.371  1.00  4.47           C  
-ATOM   3225  CG1 ILE B  99      66.390  31.908  73.094  1.00  5.56           C  
-ATOM   3226  CG2 ILE B  99      66.340  32.218  75.571  1.00 11.87           C  
-ATOM   3227  CD1 ILE B  99      67.725  31.228  73.081  1.00 10.30           C  
-ATOM   3228  N   MET B 100      63.177  30.492  75.677  1.00  8.80           N  
-ATOM   3229  CA  MET B 100      62.186  30.476  76.740  1.00 12.35           C  
-ATOM   3230  C   MET B 100      61.980  29.068  77.270  1.00 12.32           C  
-ATOM   3231  O   MET B 100      62.400  28.738  78.373  1.00 22.81           O  
-ATOM   3232  CB  MET B 100      60.868  30.999  76.196  1.00 23.17           C  
-ATOM   3233  CG  MET B 100      59.781  31.142  77.218  1.00 47.66           C  
-ATOM   3234  SD  MET B 100      59.837  32.745  78.030  1.00 64.23           S  
-ATOM   3235  CE  MET B 100      60.245  32.218  79.744  1.00 48.87           C  
-ATOM   3236  N   HIS B 101      61.318  28.239  76.485  1.00 12.70           N  
-ATOM   3237  CA  HIS B 101      61.064  26.862  76.887  1.00 23.48           C  
-ATOM   3238  C   HIS B 101      62.265  26.186  77.554  1.00 22.40           C  
-ATOM   3239  O   HIS B 101      62.109  25.477  78.548  1.00 27.17           O  
-ATOM   3240  CB  HIS B 101      60.651  26.036  75.679  1.00 26.57           C  
-ATOM   3241  CG  HIS B 101      60.519  24.578  75.968  1.00 30.90           C  
-ATOM   3242  ND1 HIS B 101      59.327  24.001  76.350  1.00 38.39           N  
-ATOM   3243  CD2 HIS B 101      61.431  23.579  75.933  1.00 36.13           C  
-ATOM   3244  CE1 HIS B 101      59.510  22.705  76.533  1.00 42.83           C  
-ATOM   3245  NE2 HIS B 101      60.778  22.423  76.287  1.00 43.27           N  
-ATOM   3246  N   ALA B 102      63.458  26.396  77.011  1.00 14.15           N  
-ATOM   3247  CA  ALA B 102      64.654  25.779  77.576  1.00 12.52           C  
-ATOM   3248  C   ALA B 102      64.952  26.295  78.984  1.00 12.40           C  
-ATOM   3249  O   ALA B 102      65.420  25.551  79.846  1.00  9.72           O  
-ATOM   3250  CB  ALA B 102      65.837  26.022  76.670  1.00 22.59           C  
-ATOM   3251  N   LYS B 103      64.689  27.574  79.213  1.00 11.14           N  
-ATOM   3252  CA  LYS B 103      64.904  28.171  80.528  1.00 13.25           C  
-ATOM   3253  C   LYS B 103      63.918  27.543  81.499  1.00 20.34           C  
-ATOM   3254  O   LYS B 103      64.286  27.052  82.570  1.00 25.93           O  
-ATOM   3255  CB  LYS B 103      64.652  29.675  80.479  1.00 10.07           C  
-ATOM   3256  CG  LYS B 103      64.384  30.297  81.839  1.00 26.12           C  
-ATOM   3257  CD  LYS B 103      65.637  30.352  82.714  1.00 35.91           C  
-ATOM   3258  CE  LYS B 103      66.581  31.464  82.251  1.00 44.37           C  
-ATOM   3259  NZ  LYS B 103      67.791  31.562  83.118  1.00 50.37           N  
-ATOM   3260  N   ILE B 104      62.651  27.580  81.113  1.00 18.34           N  
-ATOM   3261  CA  ILE B 104      61.581  27.012  81.915  1.00 22.35           C  
-ATOM   3262  C   ILE B 104      61.841  25.549  82.299  1.00 26.02           C  
-ATOM   3263  O   ILE B 104      61.569  25.133  83.425  1.00 30.52           O  
-ATOM   3264  CB  ILE B 104      60.244  27.139  81.154  1.00 19.56           C  
-ATOM   3265  CG1 ILE B 104      59.723  28.571  81.318  1.00 22.64           C  
-ATOM   3266  CG2 ILE B 104      59.239  26.081  81.624  1.00 12.15           C  
-ATOM   3267  CD1 ILE B 104      58.568  28.921  80.403  1.00 27.08           C  
-ATOM   3268  N   SER B 105      62.373  24.759  81.379  1.00 26.22           N  
-ATOM   3269  CA  SER B 105      62.635  23.367  81.713  1.00 33.41           C  
-ATOM   3270  C   SER B 105      63.650  23.294  82.840  1.00 33.60           C  
-ATOM   3271  O   SER B 105      63.666  22.330  83.607  1.00 42.22           O  
-ATOM   3272  CB  SER B 105      63.166  22.610  80.499  1.00 40.46           C  
-ATOM   3273  OG  SER B 105      62.203  22.585  79.461  1.00 55.73           O  
-ATOM   3274  N   ALA B 106      64.492  24.318  82.941  1.00 26.06           N  
-ATOM   3275  CA  ALA B 106      65.511  24.355  83.979  1.00 28.37           C  
-ATOM   3276  C   ALA B 106      64.926  24.670  85.353  1.00 27.42           C  
-ATOM   3277  O   ALA B 106      65.436  24.215  86.382  1.00 28.41           O  
-ATOM   3278  CB  ALA B 106      66.580  25.369  83.620  1.00 33.92           C  
-ATOM   3279  N   LEU B 107      63.855  25.450  85.373  1.00 28.10           N  
-ATOM   3280  CA  LEU B 107      63.228  25.795  86.639  1.00 37.69           C  
-ATOM   3281  C   LEU B 107      62.210  24.737  87.028  1.00 37.91           C  
-ATOM   3282  O   LEU B 107      61.429  24.943  87.952  1.00 48.77           O  
-ATOM   3283  CB  LEU B 107      62.527  27.153  86.549  1.00 31.77           C  
-ATOM   3284  CG  LEU B 107      63.328  28.301  85.939  1.00 40.45           C  
-ATOM   3285  CD1 LEU B 107      62.509  29.594  86.030  1.00 43.56           C  
-ATOM   3286  CD2 LEU B 107      64.662  28.440  86.668  1.00 43.45           C  
-ATOM   3287  N   MET B 108      62.208  23.609  86.329  1.00 39.57           N  
-ATOM   3288  CA  MET B 108      61.249  22.560  86.644  1.00 54.54           C  
-ATOM   3289  C   MET B 108      61.875  21.485  87.527  1.00 62.65           C  
-ATOM   3290  O   MET B 108      62.891  20.884  87.169  1.00 64.22           O  
-ATOM   3291  CB  MET B 108      60.696  21.926  85.362  1.00 51.43           C  
-ATOM   3292  CG  MET B 108      59.207  21.614  85.431  1.00 48.17           C  
-ATOM   3293  SD  MET B 108      58.173  23.022  84.952  1.00 57.64           S  
-ATOM   3294  CE  MET B 108      58.378  24.177  86.303  1.00 35.96           C  
-ATOM   3295  N   ASP B 109      61.255  21.254  88.683  1.00 70.90           N  
-ATOM   3296  CA  ASP B 109      61.728  20.265  89.646  1.00 76.72           C  
-ATOM   3297  C   ASP B 109      61.435  18.840  89.183  1.00 81.99           C  
-ATOM   3298  O   ASP B 109      60.276  18.418  89.105  1.00 80.41           O  
-ATOM   3299  CB  ASP B 109      61.074  20.511  91.011  1.00 79.83           C  
-ATOM   3300  CG  ASP B 109      61.598  19.576  92.089  1.00 88.03           C  
-ATOM   3301  OD1 ASP B 109      62.817  19.610  92.368  1.00 89.22           O  
-ATOM   3302  OD2 ASP B 109      60.787  18.811  92.660  1.00 93.74           O  
-ATOM   3303  N   THR B 110      62.501  18.107  88.876  1.00 88.82           N  
-ATOM   3304  CA  THR B 110      62.400  16.722  88.425  1.00 91.92           C  
-ATOM   3305  C   THR B 110      62.867  15.801  89.563  1.00 92.27           C  
-ATOM   3306  O   THR B 110      63.768  14.977  89.393  1.00 91.09           O  
-ATOM   3307  CB  THR B 110      63.287  16.485  87.170  1.00 94.73           C  
-ATOM   3308  OG1 THR B 110      63.014  17.496  86.189  1.00 92.80           O  
-ATOM   3309  CG2 THR B 110      63.004  15.113  86.561  1.00 95.56           C  
-ATOM   3310  N   SER B 111      62.260  15.956  90.734  1.00 93.72           N  
-ATOM   3311  CA  SER B 111      62.627  15.141  91.889  1.00 95.60           C  
-ATOM   3312  C   SER B 111      61.655  13.972  92.032  1.00 95.20           C  
-ATOM   3313  O   SER B 111      60.442  14.143  91.871  1.00 96.95           O  
-ATOM   3314  CB  SER B 111      62.620  15.997  93.167  1.00 95.36           C  
-ATOM   3315  OG  SER B 111      63.056  15.259  94.298  1.00 93.15           O  
-ATOM   3316  N   THR B 112      62.195  12.787  92.319  1.00 92.40           N  
-ATOM   3317  CA  THR B 112      61.383  11.580  92.493  1.00 86.36           C  
-ATOM   3318  C   THR B 112      60.920  11.437  93.945  1.00 87.92           C  
-ATOM   3319  O   THR B 112      59.744  11.646  94.264  1.00 86.82           O  
-ATOM   3320  CB  THR B 112      62.169  10.298  92.099  1.00 79.77           C  
-ATOM   3321  OG1 THR B 112      63.505  10.372  92.624  1.00 74.94           O  
-ATOM   3322  CG2 THR B 112      62.201  10.125  90.577  1.00 71.96           C  
-ATOM   3323  N   GLU B 121      44.081  20.890  96.450  1.00 85.01           N  
-ATOM   3324  CA  GLU B 121      44.352  22.322  96.541  1.00 90.49           C  
-ATOM   3325  C   GLU B 121      44.679  22.899  95.153  1.00 91.00           C  
-ATOM   3326  O   GLU B 121      45.254  22.207  94.305  1.00 91.45           O  
-ATOM   3327  CB  GLU B 121      45.524  22.569  97.507  1.00 92.55           C  
-ATOM   3328  CG  GLU B 121      45.209  23.473  98.709  1.00 88.87           C  
-ATOM   3329  CD  GLU B 121      45.107  24.952  98.353  1.00 81.37           C  
-ATOM   3330  OE1 GLU B 121      46.126  25.549  97.940  1.00 79.39           O  
-ATOM   3331  OE2 GLU B 121      44.004  25.519  98.491  1.00 71.71           O  
-ATOM   3332  N   PRO B 122      44.294  24.170  94.905  1.00 87.22           N  
-ATOM   3333  CA  PRO B 122      44.508  24.909  93.653  1.00 77.14           C  
-ATOM   3334  C   PRO B 122      45.955  25.118  93.199  1.00 74.09           C  
-ATOM   3335  O   PRO B 122      46.697  25.927  93.775  1.00 68.92           O  
-ATOM   3336  CB  PRO B 122      43.804  26.235  93.916  1.00 75.44           C  
-ATOM   3337  CG  PRO B 122      42.653  25.818  94.753  1.00 83.59           C  
-ATOM   3338  CD  PRO B 122      43.314  24.885  95.747  1.00 87.47           C  
-ATOM   3339  N   TYR B 123      46.318  24.381  92.147  1.00 69.72           N  
-ATOM   3340  CA  TYR B 123      47.630  24.414  91.491  1.00 60.11           C  
-ATOM   3341  C   TYR B 123      47.756  25.619  90.543  1.00 52.30           C  
-ATOM   3342  O   TYR B 123      46.818  25.954  89.813  1.00 43.57           O  
-ATOM   3343  CB  TYR B 123      47.829  23.118  90.697  1.00 56.44           C  
-ATOM   3344  CG  TYR B 123      46.535  22.579  90.135  1.00 63.46           C  
-ATOM   3345  CD1 TYR B 123      45.615  23.436  89.509  1.00 70.08           C  
-ATOM   3346  CD2 TYR B 123      46.202  21.227  90.257  1.00 58.39           C  
-ATOM   3347  CE1 TYR B 123      44.388  22.965  89.021  1.00 72.49           C  
-ATOM   3348  CE2 TYR B 123      44.974  20.741  89.769  1.00 66.38           C  
-ATOM   3349  CZ  TYR B 123      44.072  21.619  89.155  1.00 70.93           C  
-ATOM   3350  OH  TYR B 123      42.852  21.169  88.689  1.00 68.04           O  
-ATOM   3351  N   LYS B 124      48.920  26.262  90.559  1.00 49.46           N  
-ATOM   3352  CA  LYS B 124      49.163  27.422  89.711  1.00 48.85           C  
-ATOM   3353  C   LYS B 124      49.346  27.009  88.251  1.00 46.39           C  
-ATOM   3354  O   LYS B 124      50.227  26.216  87.910  1.00 48.33           O  
-ATOM   3355  CB  LYS B 124      50.391  28.189  90.213  1.00 46.56           C  
-ATOM   3356  CG  LYS B 124      50.177  28.846  91.565  1.00 47.43           C  
-ATOM   3357  CD  LYS B 124      51.478  29.351  92.171  1.00 56.77           C  
-ATOM   3358  CE  LYS B 124      51.234  30.061  93.512  1.00 67.56           C  
-ATOM   3359  NZ  LYS B 124      50.573  29.197  94.541  1.00 63.97           N  
-ATOM   3360  N   ILE B 125      48.494  27.556  87.393  1.00 40.31           N  
-ATOM   3361  CA  ILE B 125      48.522  27.256  85.970  1.00 34.78           C  
-ATOM   3362  C   ILE B 125      49.256  28.337  85.189  1.00 32.57           C  
-ATOM   3363  O   ILE B 125      48.908  29.509  85.285  1.00 40.06           O  
-ATOM   3364  CB  ILE B 125      47.075  27.128  85.406  1.00 31.67           C  
-ATOM   3365  CG1 ILE B 125      46.994  27.770  84.022  1.00 38.95           C  
-ATOM   3366  CG2 ILE B 125      46.078  27.808  86.330  1.00 35.45           C  
-ATOM   3367  CD1 ILE B 125      45.584  27.913  83.493  1.00 57.65           C  
-ATOM   3368  N   MET B 126      50.277  27.952  84.427  1.00 29.12           N  
-ATOM   3369  CA  MET B 126      51.005  28.921  83.607  1.00 29.36           C  
-ATOM   3370  C   MET B 126      50.691  28.612  82.142  1.00 28.95           C  
-ATOM   3371  O   MET B 126      51.172  27.641  81.553  1.00 29.03           O  
-ATOM   3372  CB  MET B 126      52.523  28.871  83.862  1.00 36.83           C  
-ATOM   3373  CG  MET B 126      53.213  27.617  83.363  1.00 51.08           C  
-ATOM   3374  SD  MET B 126      54.407  27.957  82.051  1.00 57.09           S  
-ATOM   3375  CE  MET B 126      55.959  27.764  82.990  1.00 59.05           C  
-ATOM   3376  N   LEU B 127      49.852  29.457  81.568  1.00 31.59           N  
-ATOM   3377  CA  LEU B 127      49.406  29.319  80.186  1.00 30.95           C  
-ATOM   3378  C   LEU B 127      50.415  29.906  79.192  1.00 27.37           C  
-ATOM   3379  O   LEU B 127      51.001  30.965  79.431  1.00 29.81           O  
-ATOM   3380  CB  LEU B 127      48.060  30.030  80.059  1.00 27.04           C  
-ATOM   3381  CG  LEU B 127      47.148  29.764  78.878  1.00 22.63           C  
-ATOM   3382  CD1 LEU B 127      46.794  28.290  78.812  1.00 25.72           C  
-ATOM   3383  CD2 LEU B 127      45.899  30.602  79.058  1.00 24.28           C  
-ATOM   3384  N   SER B 128      50.619  29.223  78.075  1.00 21.30           N  
-ATOM   3385  CA  SER B 128      51.549  29.715  77.067  1.00 28.43           C  
-ATOM   3386  C   SER B 128      50.922  29.721  75.688  1.00 27.84           C  
-ATOM   3387  O   SER B 128      50.130  28.846  75.358  1.00 33.81           O  
-ATOM   3388  CB  SER B 128      52.814  28.856  77.027  1.00 38.32           C  
-ATOM   3389  OG  SER B 128      53.575  29.117  75.849  1.00 36.30           O  
-ATOM   3390  N   ASP B 129      51.296  30.703  74.877  1.00 26.86           N  
-ATOM   3391  CA  ASP B 129      50.765  30.818  73.526  1.00 26.25           C  
-ATOM   3392  C   ASP B 129      51.664  30.077  72.535  1.00 23.45           C  
-ATOM   3393  O   ASP B 129      52.732  30.557  72.167  1.00 21.90           O  
-ATOM   3394  CB  ASP B 129      50.652  32.293  73.136  1.00 29.99           C  
-ATOM   3395  CG  ASP B 129      49.848  32.498  71.869  1.00 37.80           C  
-ATOM   3396  OD1 ASP B 129      49.678  33.665  71.445  1.00 48.74           O  
-ATOM   3397  OD2 ASP B 129      49.385  31.486  71.304  1.00 31.77           O  
-ATOM   3398  N   ARG B 130      51.214  28.904  72.107  1.00 19.69           N  
-ATOM   3399  CA  ARG B 130      51.960  28.076  71.170  1.00 13.72           C  
-ATOM   3400  C   ARG B 130      53.144  27.386  71.822  1.00 17.80           C  
-ATOM   3401  O   ARG B 130      53.785  27.943  72.711  1.00 23.11           O  
-ATOM   3402  CB  ARG B 130      52.440  28.899  69.970  1.00  6.64           C  
-ATOM   3403  CG  ARG B 130      51.373  29.073  68.904  1.00  8.65           C  
-ATOM   3404  CD  ARG B 130      51.974  29.434  67.565  1.00  7.11           C  
-ATOM   3405  NE  ARG B 130      51.148  28.941  66.471  1.00 13.42           N  
-ATOM   3406  CZ  ARG B 130      49.980  29.463  66.113  1.00 20.08           C  
-ATOM   3407  NH1 ARG B 130      49.481  30.509  66.757  1.00 22.40           N  
-ATOM   3408  NH2 ARG B 130      49.303  28.932  65.105  1.00 24.09           N  
-ATOM   3409  N   HIS B 131      53.415  26.162  71.377  1.00 12.68           N  
-ATOM   3410  CA  HIS B 131      54.518  25.369  71.889  1.00  4.47           C  
-ATOM   3411  C   HIS B 131      55.570  25.279  70.801  1.00  6.79           C  
-ATOM   3412  O   HIS B 131      55.237  25.231  69.619  1.00 13.64           O  
-ATOM   3413  CB  HIS B 131      54.028  23.978  72.239  1.00  4.47           C  
-ATOM   3414  CG  HIS B 131      55.084  23.111  72.834  1.00 12.12           C  
-ATOM   3415  ND1 HIS B 131      56.159  22.653  72.108  1.00 17.71           N  
-ATOM   3416  CD2 HIS B 131      55.259  22.659  74.098  1.00 16.70           C  
-ATOM   3417  CE1 HIS B 131      56.953  21.954  72.901  1.00 28.93           C  
-ATOM   3418  NE2 HIS B 131      56.431  21.944  74.114  1.00 21.52           N  
-ATOM   3419  N   PRO B 132      56.857  25.257  71.178  1.00  6.65           N  
-ATOM   3420  CA  PRO B 132      58.001  25.175  70.257  1.00 13.44           C  
-ATOM   3421  C   PRO B 132      57.837  24.274  69.033  1.00 10.86           C  
-ATOM   3422  O   PRO B 132      58.344  24.582  67.953  1.00 11.08           O  
-ATOM   3423  CB  PRO B 132      59.130  24.715  71.165  1.00 17.03           C  
-ATOM   3424  CG  PRO B 132      58.841  25.488  72.394  1.00 12.87           C  
-ATOM   3425  CD  PRO B 132      57.330  25.306  72.567  1.00  6.69           C  
-ATOM   3426  N   ILE B 133      57.132  23.164  69.196  1.00  4.98           N  
-ATOM   3427  CA  ILE B 133      56.924  22.269  68.075  1.00  8.75           C  
-ATOM   3428  C   ILE B 133      56.186  22.966  66.921  1.00 10.73           C  
-ATOM   3429  O   ILE B 133      56.210  22.501  65.776  1.00 11.30           O  
-ATOM   3430  CB  ILE B 133      56.149  21.000  68.510  1.00 15.52           C  
-ATOM   3431  CG1 ILE B 133      54.673  21.312  68.758  1.00 16.21           C  
-ATOM   3432  CG2 ILE B 133      56.771  20.432  69.784  1.00 16.29           C  
-ATOM   3433  CD1 ILE B 133      53.858  20.056  69.112  1.00  6.66           C  
-ATOM   3434  N   ALA B 134      55.539  24.089  67.219  1.00 10.39           N  
-ATOM   3435  CA  ALA B 134      54.829  24.824  66.190  1.00  6.54           C  
-ATOM   3436  C   ALA B 134      55.829  25.326  65.174  1.00 11.70           C  
-ATOM   3437  O   ALA B 134      55.582  25.244  63.975  1.00 18.25           O  
-ATOM   3438  CB  ALA B 134      54.098  25.983  66.789  1.00  4.47           C  
-ATOM   3439  N   SER B 135      56.963  25.836  65.652  1.00 10.40           N  
-ATOM   3440  CA  SER B 135      57.999  26.364  64.758  1.00  7.81           C  
-ATOM   3441  C   SER B 135      58.922  25.297  64.217  1.00  4.47           C  
-ATOM   3442  O   SER B 135      59.355  25.355  63.068  1.00  4.47           O  
-ATOM   3443  CB  SER B 135      58.860  27.391  65.481  1.00  9.79           C  
-ATOM   3444  OG  SER B 135      59.621  26.763  66.493  1.00 27.05           O  
-ATOM   3445  N   THR B 136      59.217  24.321  65.058  1.00  4.47           N  
-ATOM   3446  CA  THR B 136      60.121  23.258  64.678  1.00 10.67           C  
-ATOM   3447  C   THR B 136      59.486  22.063  64.001  1.00  9.98           C  
-ATOM   3448  O   THR B 136      60.201  21.210  63.487  1.00  8.50           O  
-ATOM   3449  CB  THR B 136      60.875  22.731  65.891  1.00 22.20           C  
-ATOM   3450  OG1 THR B 136      59.953  22.092  66.782  1.00 18.00           O  
-ATOM   3451  CG2 THR B 136      61.562  23.882  66.625  1.00 42.85           C  
-ATOM   3452  N   ILE B 137      58.161  21.968  64.008  1.00 10.09           N  
-ATOM   3453  CA  ILE B 137      57.547  20.814  63.369  1.00  9.36           C  
-ATOM   3454  C   ILE B 137      56.231  21.030  62.660  1.00  4.91           C  
-ATOM   3455  O   ILE B 137      56.074  20.587  61.532  1.00 10.19           O  
-ATOM   3456  CB  ILE B 137      57.439  19.593  64.364  1.00 17.80           C  
-ATOM   3457  CG1 ILE B 137      56.022  19.039  64.427  1.00 13.38           C  
-ATOM   3458  CG2 ILE B 137      57.907  19.981  65.750  1.00 21.58           C  
-ATOM   3459  CD1 ILE B 137      55.946  17.787  65.301  1.00 16.02           C  
-ATOM   3460  N   CYS B 138      55.283  21.713  63.276  1.00  4.47           N  
-ATOM   3461  CA  CYS B 138      54.022  21.906  62.575  1.00  8.57           C  
-ATOM   3462  C   CYS B 138      54.130  22.778  61.325  1.00  7.23           C  
-ATOM   3463  O   CYS B 138      53.854  22.305  60.229  1.00  4.47           O  
-ATOM   3464  CB  CYS B 138      52.961  22.454  63.527  1.00 14.45           C  
-ATOM   3465  SG  CYS B 138      52.528  21.239  64.779  1.00 41.78           S  
-ATOM   3466  N   PHE B 139      54.539  24.038  61.469  1.00 12.26           N  
-ATOM   3467  CA  PHE B 139      54.645  24.918  60.306  1.00  9.16           C  
-ATOM   3468  C   PHE B 139      55.646  24.428  59.274  1.00 15.83           C  
-ATOM   3469  O   PHE B 139      55.280  24.190  58.124  1.00 25.18           O  
-ATOM   3470  CB  PHE B 139      54.999  26.347  60.714  1.00  4.47           C  
-ATOM   3471  CG  PHE B 139      53.821  27.150  61.168  1.00 11.26           C  
-ATOM   3472  CD1 PHE B 139      53.199  26.880  62.379  1.00 17.53           C  
-ATOM   3473  CD2 PHE B 139      53.327  28.178  60.385  1.00 18.09           C  
-ATOM   3474  CE1 PHE B 139      52.102  27.627  62.798  1.00 13.83           C  
-ATOM   3475  CE2 PHE B 139      52.232  28.927  60.797  1.00 13.52           C  
-ATOM   3476  CZ  PHE B 139      51.621  28.651  62.002  1.00 10.06           C  
-ATOM   3477  N   PRO B 140      56.924  24.263  59.658  1.00 16.47           N  
-ATOM   3478  CA  PRO B 140      57.855  23.788  58.625  1.00 15.51           C  
-ATOM   3479  C   PRO B 140      57.285  22.616  57.802  1.00 13.74           C  
-ATOM   3480  O   PRO B 140      57.414  22.571  56.579  1.00  9.94           O  
-ATOM   3481  CB  PRO B 140      59.112  23.422  59.431  1.00 20.58           C  
-ATOM   3482  CG  PRO B 140      58.598  23.219  60.862  1.00 13.66           C  
-ATOM   3483  CD  PRO B 140      57.566  24.295  60.986  1.00 12.33           C  
-ATOM   3484  N   LEU B 141      56.610  21.692  58.471  1.00 10.65           N  
-ATOM   3485  CA  LEU B 141      56.049  20.545  57.777  1.00  9.79           C  
-ATOM   3486  C   LEU B 141      54.910  20.948  56.864  1.00  4.47           C  
-ATOM   3487  O   LEU B 141      54.712  20.369  55.807  1.00  4.47           O  
-ATOM   3488  CB  LEU B 141      55.572  19.508  58.795  1.00  4.47           C  
-ATOM   3489  CG  LEU B 141      56.135  18.091  58.660  1.00  4.47           C  
-ATOM   3490  CD1 LEU B 141      57.587  18.113  58.181  1.00  4.93           C  
-ATOM   3491  CD2 LEU B 141      56.023  17.408  60.020  1.00 11.04           C  
-ATOM   3492  N   SER B 142      54.146  21.937  57.273  1.00  4.47           N  
-ATOM   3493  CA  SER B 142      53.049  22.346  56.437  1.00  5.69           C  
-ATOM   3494  C   SER B 142      53.636  22.991  55.186  1.00  7.74           C  
-ATOM   3495  O   SER B 142      53.166  22.739  54.083  1.00 12.93           O  
-ATOM   3496  CB  SER B 142      52.128  23.321  57.188  1.00 12.20           C  
-ATOM   3497  OG  SER B 142      51.478  22.712  58.304  1.00  4.47           O  
-ATOM   3498  N   ARG B 143      54.676  23.804  55.347  1.00  6.45           N  
-ATOM   3499  CA  ARG B 143      55.297  24.455  54.196  1.00  4.47           C  
-ATOM   3500  C   ARG B 143      55.775  23.403  53.201  1.00  9.46           C  
-ATOM   3501  O   ARG B 143      55.634  23.563  51.985  1.00  8.89           O  
-ATOM   3502  CB  ARG B 143      56.491  25.308  54.624  1.00  4.47           C  
-ATOM   3503  CG  ARG B 143      56.125  26.535  55.415  1.00  4.47           C  
-ATOM   3504  CD  ARG B 143      55.321  27.540  54.606  1.00  4.47           C  
-ATOM   3505  NE  ARG B 143      54.889  28.672  55.431  1.00  9.48           N  
-ATOM   3506  CZ  ARG B 143      54.021  29.605  55.039  1.00 18.35           C  
-ATOM   3507  NH1 ARG B 143      53.481  29.553  53.823  1.00 18.90           N  
-ATOM   3508  NH2 ARG B 143      53.683  30.589  55.869  1.00 11.00           N  
-ATOM   3509  N   TYR B 144      56.352  22.324  53.713  1.00 10.77           N  
-ATOM   3510  CA  TYR B 144      56.827  21.279  52.821  1.00 14.96           C  
-ATOM   3511  C   TYR B 144      55.668  20.740  52.003  1.00 13.55           C  
-ATOM   3512  O   TYR B 144      55.659  20.836  50.783  1.00 15.91           O  
-ATOM   3513  CB  TYR B 144      57.476  20.131  53.606  1.00 18.42           C  
-ATOM   3514  CG  TYR B 144      57.726  18.888  52.768  1.00 15.37           C  
-ATOM   3515  CD1 TYR B 144      56.825  17.837  52.770  1.00 17.41           C  
-ATOM   3516  CD2 TYR B 144      58.833  18.796  51.925  1.00 24.81           C  
-ATOM   3517  CE1 TYR B 144      57.011  16.727  51.952  1.00 31.05           C  
-ATOM   3518  CE2 TYR B 144      59.029  17.688  51.097  1.00 28.91           C  
-ATOM   3519  CZ  TYR B 144      58.112  16.658  51.112  1.00 33.26           C  
-ATOM   3520  OH  TYR B 144      58.274  15.575  50.266  1.00 39.51           O  
-ATOM   3521  N   LEU B 145      54.690  20.177  52.696  1.00 15.44           N  
-ATOM   3522  CA  LEU B 145      53.513  19.601  52.063  1.00 11.05           C  
-ATOM   3523  C   LEU B 145      52.912  20.467  50.958  1.00  7.33           C  
-ATOM   3524  O   LEU B 145      52.518  19.961  49.918  1.00  4.47           O  
-ATOM   3525  CB  LEU B 145      52.462  19.316  53.134  1.00  9.29           C  
-ATOM   3526  CG  LEU B 145      52.922  18.309  54.190  1.00 12.13           C  
-ATOM   3527  CD1 LEU B 145      51.808  18.071  55.181  1.00 15.42           C  
-ATOM   3528  CD2 LEU B 145      53.301  16.995  53.514  1.00 17.98           C  
-ATOM   3529  N   VAL B 146      52.840  21.772  51.187  1.00  5.16           N  
-ATOM   3530  CA  VAL B 146      52.278  22.690  50.208  1.00  4.47           C  
-ATOM   3531  C   VAL B 146      53.271  22.979  49.099  1.00 10.77           C  
-ATOM   3532  O   VAL B 146      52.905  23.517  48.056  1.00 23.71           O  
-ATOM   3533  CB  VAL B 146      51.853  24.020  50.880  1.00  5.30           C  
-ATOM   3534  CG1 VAL B 146      51.975  25.175  49.915  1.00  9.83           C  
-ATOM   3535  CG2 VAL B 146      50.418  23.910  51.351  1.00 19.62           C  
-ATOM   3536  N   GLY B 147      54.533  22.632  49.328  1.00 11.92           N  
-ATOM   3537  CA  GLY B 147      55.547  22.853  48.315  1.00 10.88           C  
-ATOM   3538  C   GLY B 147      56.260  24.184  48.425  1.00 12.69           C  
-ATOM   3539  O   GLY B 147      57.002  24.562  47.520  1.00 20.27           O  
-ATOM   3540  N   ASP B 148      56.053  24.904  49.519  1.00  4.80           N  
-ATOM   3541  CA  ASP B 148      56.716  26.184  49.675  1.00 10.45           C  
-ATOM   3542  C   ASP B 148      58.106  26.065  50.288  1.00 12.88           C  
-ATOM   3543  O   ASP B 148      58.866  27.032  50.285  1.00 16.50           O  
-ATOM   3544  CB  ASP B 148      55.868  27.135  50.526  1.00 28.41           C  
-ATOM   3545  CG  ASP B 148      54.763  27.831  49.722  1.00 51.53           C  
-ATOM   3546  OD1 ASP B 148      54.996  28.126  48.528  1.00 62.71           O  
-ATOM   3547  OD2 ASP B 148      53.671  28.108  50.283  1.00 56.54           O  
-ATOM   3548  N   MET B 149      58.449  24.885  50.796  1.00  8.69           N  
-ATOM   3549  CA  MET B 149      59.750  24.693  51.431  1.00 13.88           C  
-ATOM   3550  C   MET B 149      60.371  23.349  51.075  1.00 27.25           C  
-ATOM   3551  O   MET B 149      59.655  22.363  50.918  1.00 27.52           O  
-ATOM   3552  CB  MET B 149      59.584  24.799  52.944  1.00  8.91           C  
-ATOM   3553  CG  MET B 149      60.814  24.450  53.750  1.00  9.29           C  
-ATOM   3554  SD  MET B 149      60.490  24.698  55.524  1.00 18.84           S  
-ATOM   3555  CE  MET B 149      60.389  26.428  55.579  1.00  4.47           C  
-ATOM   3556  N   SER B 150      61.702  23.310  50.956  1.00 37.28           N  
-ATOM   3557  CA  SER B 150      62.432  22.074  50.615  1.00 34.73           C  
-ATOM   3558  C   SER B 150      62.687  21.218  51.859  1.00 29.19           C  
-ATOM   3559  O   SER B 150      63.139  21.731  52.884  1.00 38.63           O  
-ATOM   3560  CB  SER B 150      63.769  22.417  49.936  1.00 41.11           C  
-ATOM   3561  OG  SER B 150      64.571  23.254  50.756  1.00 50.56           O  
-ATOM   3562  N   PRO B 151      62.430  19.897  51.773  1.00 20.29           N  
-ATOM   3563  CA  PRO B 151      62.613  18.944  52.884  1.00 16.89           C  
-ATOM   3564  C   PRO B 151      63.963  19.054  53.592  1.00 15.54           C  
-ATOM   3565  O   PRO B 151      64.090  18.745  54.781  1.00 14.57           O  
-ATOM   3566  CB  PRO B 151      62.416  17.585  52.212  1.00  4.47           C  
-ATOM   3567  CG  PRO B 151      62.939  17.823  50.851  1.00 12.47           C  
-ATOM   3568  CD  PRO B 151      62.321  19.170  50.500  1.00 18.88           C  
-ATOM   3569  N   ALA B 152      64.956  19.520  52.848  1.00 11.25           N  
-ATOM   3570  CA  ALA B 152      66.305  19.677  53.349  1.00  4.47           C  
-ATOM   3571  C   ALA B 152      66.390  20.289  54.739  1.00  4.47           C  
-ATOM   3572  O   ALA B 152      67.349  20.043  55.464  1.00 11.90           O  
-ATOM   3573  CB  ALA B 152      67.107  20.514  52.364  1.00 14.52           C  
-ATOM   3574  N   ALA B 153      65.391  21.067  55.135  1.00  6.28           N  
-ATOM   3575  CA  ALA B 153      65.449  21.720  56.443  1.00 10.03           C  
-ATOM   3576  C   ALA B 153      64.691  21.018  57.524  1.00 11.03           C  
-ATOM   3577  O   ALA B 153      64.579  21.545  58.621  1.00 16.11           O  
-ATOM   3578  CB  ALA B 153      64.952  23.154  56.349  1.00  4.47           C  
-ATOM   3579  N   LEU B 154      64.158  19.843  57.233  1.00  9.87           N  
-ATOM   3580  CA  LEU B 154      63.413  19.138  58.257  1.00 11.41           C  
-ATOM   3581  C   LEU B 154      64.286  18.515  59.342  1.00 11.23           C  
-ATOM   3582  O   LEU B 154      63.972  18.624  60.526  1.00  9.95           O  
-ATOM   3583  CB  LEU B 154      62.512  18.088  57.618  1.00  6.41           C  
-ATOM   3584  CG  LEU B 154      61.457  18.792  56.766  1.00  7.87           C  
-ATOM   3585  CD1 LEU B 154      60.612  17.773  56.068  1.00 16.09           C  
-ATOM   3586  CD2 LEU B 154      60.592  19.685  57.633  1.00  4.47           C  
-ATOM   3587  N   PRO B 155      65.413  17.890  58.964  1.00  8.48           N  
-ATOM   3588  CA  PRO B 155      66.282  17.269  59.975  1.00  9.23           C  
-ATOM   3589  C   PRO B 155      66.743  18.268  61.033  1.00  6.54           C  
-ATOM   3590  O   PRO B 155      66.779  17.990  62.233  1.00  4.47           O  
-ATOM   3591  CB  PRO B 155      67.445  16.734  59.143  1.00 12.32           C  
-ATOM   3592  CG  PRO B 155      66.824  16.485  57.806  1.00  5.88           C  
-ATOM   3593  CD  PRO B 155      65.975  17.715  57.618  1.00  4.47           C  
-ATOM   3594  N   GLY B 156      67.092  19.451  60.566  1.00 17.20           N  
-ATOM   3595  CA  GLY B 156      67.546  20.477  61.480  1.00 28.34           C  
-ATOM   3596  C   GLY B 156      66.498  20.896  62.490  1.00 26.74           C  
-ATOM   3597  O   GLY B 156      66.838  21.392  63.560  1.00 31.88           O  
-ATOM   3598  N   LEU B 157      65.224  20.700  62.170  1.00 23.60           N  
-ATOM   3599  CA  LEU B 157      64.181  21.099  63.102  1.00 19.37           C  
-ATOM   3600  C   LEU B 157      63.527  19.925  63.817  1.00 22.93           C  
-ATOM   3601  O   LEU B 157      63.253  20.006  65.012  1.00 33.95           O  
-ATOM   3602  CB  LEU B 157      63.099  21.901  62.388  1.00 11.47           C  
-ATOM   3603  CG  LEU B 157      63.528  22.917  61.335  1.00 14.13           C  
-ATOM   3604  CD1 LEU B 157      62.273  23.609  60.793  1.00  4.47           C  
-ATOM   3605  CD2 LEU B 157      64.524  23.913  61.926  1.00  9.64           C  
-ATOM   3606  N   LEU B 158      63.286  18.832  63.100  1.00 14.79           N  
-ATOM   3607  CA  LEU B 158      62.619  17.679  63.694  1.00 10.13           C  
-ATOM   3608  C   LEU B 158      63.484  16.771  64.527  1.00 16.46           C  
-ATOM   3609  O   LEU B 158      63.072  16.336  65.602  1.00 24.06           O  
-ATOM   3610  CB  LEU B 158      61.961  16.829  62.615  1.00 10.42           C  
-ATOM   3611  CG  LEU B 158      61.048  17.596  61.661  1.00 21.10           C  
-ATOM   3612  CD1 LEU B 158      60.376  16.628  60.677  1.00 23.60           C  
-ATOM   3613  CD2 LEU B 158      60.020  18.358  62.476  1.00 15.62           C  
-ATOM   3614  N   PHE B 159      64.684  16.484  64.039  1.00 16.59           N  
-ATOM   3615  CA  PHE B 159      65.576  15.573  64.743  1.00 13.60           C  
-ATOM   3616  C   PHE B 159      66.449  16.145  65.871  1.00 15.19           C  
-ATOM   3617  O   PHE B 159      67.048  15.391  66.627  1.00 15.28           O  
-ATOM   3618  CB  PHE B 159      66.454  14.860  63.723  1.00 12.24           C  
-ATOM   3619  CG  PHE B 159      65.686  14.235  62.586  1.00 15.01           C  
-ATOM   3620  CD1 PHE B 159      64.390  13.765  62.782  1.00 10.65           C  
-ATOM   3621  CD2 PHE B 159      66.285  14.056  61.331  1.00  7.96           C  
-ATOM   3622  CE1 PHE B 159      63.701  13.122  61.749  1.00  4.47           C  
-ATOM   3623  CE2 PHE B 159      65.601  13.412  60.295  1.00  4.47           C  
-ATOM   3624  CZ  PHE B 159      64.308  12.944  60.506  1.00  4.47           C  
-ATOM   3625  N   THR B 160      66.526  17.464  65.996  1.00 19.83           N  
-ATOM   3626  CA  THR B 160      67.341  18.056  67.054  1.00 18.98           C  
-ATOM   3627  C   THR B 160      66.513  18.533  68.244  1.00 20.36           C  
-ATOM   3628  O   THR B 160      66.954  19.400  68.999  1.00 19.30           O  
-ATOM   3629  CB  THR B 160      68.151  19.258  66.538  1.00 22.10           C  
-ATOM   3630  OG1 THR B 160      67.264  20.215  65.939  1.00 30.43           O  
-ATOM   3631  CG2 THR B 160      69.175  18.806  65.529  1.00 20.23           C  
-ATOM   3632  N   LEU B 161      65.320  17.976  68.421  1.00 18.04           N  
-ATOM   3633  CA  LEU B 161      64.477  18.397  69.534  1.00 15.90           C  
-ATOM   3634  C   LEU B 161      65.062  18.034  70.884  1.00 16.99           C  
-ATOM   3635  O   LEU B 161      65.643  16.971  71.064  1.00 23.82           O  
-ATOM   3636  CB  LEU B 161      63.084  17.795  69.413  1.00 11.08           C  
-ATOM   3637  CG  LEU B 161      62.252  18.439  68.319  1.00  8.90           C  
-ATOM   3638  CD1 LEU B 161      60.843  17.916  68.397  1.00  7.33           C  
-ATOM   3639  CD2 LEU B 161      62.268  19.948  68.503  1.00  5.84           C  
-ATOM   3640  N   PRO B 162      64.920  18.927  71.861  1.00 17.03           N  
-ATOM   3641  CA  PRO B 162      65.443  18.695  73.206  1.00 20.15           C  
-ATOM   3642  C   PRO B 162      64.442  17.931  74.063  1.00 20.88           C  
-ATOM   3643  O   PRO B 162      63.231  18.038  73.853  1.00 22.39           O  
-ATOM   3644  CB  PRO B 162      65.688  20.110  73.713  1.00 20.08           C  
-ATOM   3645  CG  PRO B 162      64.518  20.835  73.149  1.00 20.54           C  
-ATOM   3646  CD  PRO B 162      64.437  20.308  71.718  1.00 19.57           C  
-ATOM   3647  N   ALA B 163      64.961  17.170  75.026  1.00 22.03           N  
-ATOM   3648  CA  ALA B 163      64.146  16.373  75.942  1.00 19.82           C  
-ATOM   3649  C   ALA B 163      63.031  17.206  76.542  1.00 25.39           C  
-ATOM   3650  O   ALA B 163      63.280  18.222  77.198  1.00 23.11           O  
-ATOM   3651  CB  ALA B 163      65.006  15.815  77.050  1.00 17.64           C  
-ATOM   3652  N   GLU B 164      61.799  16.765  76.317  1.00 29.82           N  
-ATOM   3653  CA  GLU B 164      60.636  17.474  76.829  1.00 34.70           C  
-ATOM   3654  C   GLU B 164      60.380  17.014  78.246  1.00 36.41           C  
-ATOM   3655  O   GLU B 164      60.302  15.816  78.507  1.00 41.78           O  
-ATOM   3656  CB  GLU B 164      59.399  17.174  75.973  1.00 39.85           C  
-ATOM   3657  CG  GLU B 164      58.157  17.979  76.346  1.00 39.71           C  
-ATOM   3658  CD  GLU B 164      58.229  19.417  75.858  1.00 50.43           C  
-ATOM   3659  OE1 GLU B 164      59.307  19.833  75.372  1.00 56.50           O  
-ATOM   3660  OE2 GLU B 164      57.208  20.132  75.962  1.00 50.10           O  
-ATOM   3661  N   PRO B 165      60.269  17.960  79.186  1.00 39.11           N  
-ATOM   3662  CA  PRO B 165      60.015  17.637  80.594  1.00 42.34           C  
-ATOM   3663  C   PRO B 165      58.566  17.179  80.791  1.00 45.01           C  
-ATOM   3664  O   PRO B 165      57.645  17.674  80.133  1.00 46.99           O  
-ATOM   3665  CB  PRO B 165      60.340  18.946  81.313  1.00 45.63           C  
-ATOM   3666  CG  PRO B 165      59.969  19.981  80.299  1.00 46.51           C  
-ATOM   3667  CD  PRO B 165      60.529  19.399  79.016  1.00 44.15           C  
-ATOM   3668  N   PRO B 166      58.350  16.222  81.701  1.00 44.16           N  
-ATOM   3669  CA  PRO B 166      57.016  15.685  81.980  1.00 40.53           C  
-ATOM   3670  C   PRO B 166      56.003  16.741  82.336  1.00 30.08           C  
-ATOM   3671  O   PRO B 166      56.319  17.678  83.063  1.00 25.51           O  
-ATOM   3672  CB  PRO B 166      57.268  14.734  83.145  1.00 48.12           C  
-ATOM   3673  CG  PRO B 166      58.675  14.271  82.899  1.00 51.35           C  
-ATOM   3674  CD  PRO B 166      59.359  15.571  82.550  1.00 46.53           C  
-ATOM   3675  N   GLY B 167      54.790  16.591  81.814  1.00 23.85           N  
-ATOM   3676  CA  GLY B 167      53.741  17.537  82.139  1.00 27.85           C  
-ATOM   3677  C   GLY B 167      53.357  18.563  81.092  1.00 30.82           C  
-ATOM   3678  O   GLY B 167      52.784  19.614  81.426  1.00 29.68           O  
-ATOM   3679  N   THR B 168      53.659  18.281  79.829  1.00 27.47           N  
-ATOM   3680  CA  THR B 168      53.301  19.219  78.772  1.00 19.83           C  
-ATOM   3681  C   THR B 168      51.882  18.944  78.294  1.00 22.77           C  
-ATOM   3682  O   THR B 168      51.556  17.842  77.837  1.00 21.06           O  
-ATOM   3683  CB  THR B 168      54.247  19.121  77.562  1.00 13.18           C  
-ATOM   3684  OG1 THR B 168      55.588  19.405  77.976  1.00 12.87           O  
-ATOM   3685  CG2 THR B 168      53.831  20.110  76.485  1.00  4.47           C  
-ATOM   3686  N   ASN B 169      51.033  19.953  78.417  1.00 22.79           N  
-ATOM   3687  CA  ASN B 169      49.657  19.833  77.981  1.00 16.30           C  
-ATOM   3688  C   ASN B 169      49.476  20.659  76.707  1.00 16.62           C  
-ATOM   3689  O   ASN B 169      49.492  21.891  76.705  1.00  4.47           O  
-ATOM   3690  CB  ASN B 169      48.727  20.295  79.098  1.00 13.55           C  
-ATOM   3691  CG  ASN B 169      48.741  19.343  80.279  1.00 21.80           C  
-ATOM   3692  OD1 ASN B 169      48.208  18.234  80.191  1.00 18.48           O  
-ATOM   3693  ND2 ASN B 169      49.368  19.761  81.389  1.00 17.16           N  
-ATOM   3694  N   LEU B 170      49.342  19.950  75.603  1.00 17.36           N  
-ATOM   3695  CA  LEU B 170      49.170  20.591  74.328  1.00 17.15           C  
-ATOM   3696  C   LEU B 170      47.673  20.690  74.055  1.00 16.77           C  
-ATOM   3697  O   LEU B 170      46.968  19.675  73.994  1.00 21.66           O  
-ATOM   3698  CB  LEU B 170      49.869  19.751  73.253  1.00 17.00           C  
-ATOM   3699  CG  LEU B 170      50.473  20.484  72.053  1.00 17.25           C  
-ATOM   3700  CD1 LEU B 170      51.149  19.469  71.164  1.00 19.40           C  
-ATOM   3701  CD2 LEU B 170      49.398  21.232  71.277  1.00 16.93           C  
-ATOM   3702  N   VAL B 171      47.186  21.915  73.909  1.00  9.80           N  
-ATOM   3703  CA  VAL B 171      45.775  22.126  73.625  1.00 16.68           C  
-ATOM   3704  C   VAL B 171      45.614  22.680  72.214  1.00 13.03           C  
-ATOM   3705  O   VAL B 171      45.784  23.871  71.994  1.00 24.58           O  
-ATOM   3706  CB  VAL B 171      45.149  23.123  74.630  1.00 25.54           C  
-ATOM   3707  CG1 VAL B 171      43.654  23.295  74.348  1.00 24.65           C  
-ATOM   3708  CG2 VAL B 171      45.365  22.624  76.052  1.00 22.85           C  
-ATOM   3709  N   VAL B 172      45.296  21.810  71.263  1.00 11.48           N  
-ATOM   3710  CA  VAL B 172      45.106  22.208  69.865  1.00 12.35           C  
-ATOM   3711  C   VAL B 172      43.732  22.824  69.692  1.00 20.49           C  
-ATOM   3712  O   VAL B 172      42.715  22.150  69.891  1.00 21.81           O  
-ATOM   3713  CB  VAL B 172      45.153  20.993  68.900  1.00  7.95           C  
-ATOM   3714  CG1 VAL B 172      44.848  21.443  67.492  1.00  4.47           C  
-ATOM   3715  CG2 VAL B 172      46.499  20.307  68.967  1.00  7.67           C  
-ATOM   3716  N   CYS B 173      43.695  24.096  69.311  1.00 23.40           N  
-ATOM   3717  CA  CYS B 173      42.424  24.777  69.091  1.00 31.54           C  
-ATOM   3718  C   CYS B 173      41.913  24.438  67.693  1.00 38.95           C  
-ATOM   3719  O   CYS B 173      42.704  24.228  66.762  1.00 43.02           O  
-ATOM   3720  CB  CYS B 173      42.603  26.284  69.227  1.00 34.86           C  
-ATOM   3721  SG  CYS B 173      43.123  26.787  70.879  1.00 55.49           S  
-ATOM   3722  N   THR B 174      40.593  24.380  67.546  1.00 39.66           N  
-ATOM   3723  CA  THR B 174      39.986  24.054  66.258  1.00 40.65           C  
-ATOM   3724  C   THR B 174      38.784  24.942  65.986  1.00 43.13           C  
-ATOM   3725  O   THR B 174      38.060  25.315  66.905  1.00 47.74           O  
-ATOM   3726  CB  THR B 174      39.491  22.608  66.230  1.00 40.65           C  
-ATOM   3727  OG1 THR B 174      38.260  22.518  66.959  1.00 41.14           O  
-ATOM   3728  CG2 THR B 174      40.523  21.677  66.866  1.00 40.08           C  
-ATOM   3729  N   VAL B 175      38.565  25.264  64.718  1.00 44.16           N  
-ATOM   3730  CA  VAL B 175      37.443  26.102  64.326  1.00 47.08           C  
-ATOM   3731  C   VAL B 175      36.825  25.473  63.099  1.00 55.59           C  
-ATOM   3732  O   VAL B 175      37.492  24.715  62.409  1.00 62.28           O  
-ATOM   3733  CB  VAL B 175      37.914  27.502  63.940  1.00 42.91           C  
-ATOM   3734  CG1 VAL B 175      36.724  28.377  63.643  1.00 50.21           C  
-ATOM   3735  CG2 VAL B 175      38.756  28.088  65.041  1.00 43.05           C  
-ATOM   3736  N   SER B 176      35.560  25.770  62.821  1.00 62.82           N  
-ATOM   3737  CA  SER B 176      34.933  25.219  61.624  1.00 71.60           C  
-ATOM   3738  C   SER B 176      35.659  25.861  60.432  1.00 76.56           C  
-ATOM   3739  O   SER B 176      36.202  26.957  60.561  1.00 76.35           O  
-ATOM   3740  CB  SER B 176      33.437  25.553  61.597  1.00 70.20           C  
-ATOM   3741  OG  SER B 176      33.209  26.950  61.516  1.00 63.44           O  
-ATOM   3742  N   LEU B 177      35.676  25.186  59.283  1.00 80.73           N  
-ATOM   3743  CA  LEU B 177      36.367  25.704  58.100  1.00 84.24           C  
-ATOM   3744  C   LEU B 177      35.890  27.061  57.556  1.00 84.82           C  
-ATOM   3745  O   LEU B 177      36.687  27.985  57.427  1.00 85.16           O  
-ATOM   3746  CB  LEU B 177      36.343  24.656  56.980  1.00 91.00           C  
-ATOM   3747  CG  LEU B 177      37.013  25.026  55.650  1.00 95.33           C  
-ATOM   3748  CD1 LEU B 177      38.427  25.524  55.902  1.00 94.86           C  
-ATOM   3749  CD2 LEU B 177      37.024  23.808  54.722  1.00 98.64           C  
-ATOM   3750  N   PRO B 178      34.595  27.198  57.216  1.00 86.94           N  
-ATOM   3751  CA  PRO B 178      34.102  28.480  56.693  1.00 86.41           C  
-ATOM   3752  C   PRO B 178      34.284  29.665  57.649  1.00 84.42           C  
-ATOM   3753  O   PRO B 178      34.374  30.815  57.214  1.00 81.18           O  
-ATOM   3754  CB  PRO B 178      32.631  28.187  56.407  1.00 90.79           C  
-ATOM   3755  CG  PRO B 178      32.647  26.727  56.036  1.00 89.44           C  
-ATOM   3756  CD  PRO B 178      33.556  26.157  57.098  1.00 90.60           C  
-ATOM   3757  N   SER B 179      34.333  29.372  58.946  1.00 86.68           N  
-ATOM   3758  CA  SER B 179      34.503  30.392  59.985  1.00 89.50           C  
-ATOM   3759  C   SER B 179      35.969  30.817  60.096  1.00 91.46           C  
-ATOM   3760  O   SER B 179      36.278  31.980  60.357  1.00 92.16           O  
-ATOM   3761  CB  SER B 179      34.019  29.845  61.336  1.00 86.30           C  
-ATOM   3762  OG  SER B 179      34.189  30.794  62.376  1.00 80.78           O  
-ATOM   3763  N   HIS B 180      36.864  29.857  59.898  1.00 91.33           N  
-ATOM   3764  CA  HIS B 180      38.304  30.083  59.958  1.00 86.26           C  
-ATOM   3765  C   HIS B 180      38.706  31.034  58.832  1.00 85.30           C  
-ATOM   3766  O   HIS B 180      39.625  31.837  58.981  1.00 84.27           O  
-ATOM   3767  CB  HIS B 180      39.015  28.724  59.825  1.00 85.32           C  
-ATOM   3768  CG  HIS B 180      40.514  28.791  59.803  1.00 79.21           C  
-ATOM   3769  ND1 HIS B 180      41.302  27.660  59.861  1.00 73.46           N  
-ATOM   3770  CD2 HIS B 180      41.368  29.835  59.693  1.00 80.11           C  
-ATOM   3771  CE1 HIS B 180      42.574  28.005  59.787  1.00 72.83           C  
-ATOM   3772  NE2 HIS B 180      42.643  29.320  59.684  1.00 75.95           N  
-ATOM   3773  N   LEU B 181      37.991  30.958  57.715  1.00 86.92           N  
-ATOM   3774  CA  LEU B 181      38.289  31.794  56.558  1.00 90.60           C  
-ATOM   3775  C   LEU B 181      37.755  33.226  56.669  1.00 95.88           C  
-ATOM   3776  O   LEU B 181      37.811  33.999  55.707  1.00 98.60           O  
-ATOM   3777  CB  LEU B 181      37.755  31.120  55.291  1.00 80.37           C  
-ATOM   3778  CG  LEU B 181      38.145  29.642  55.169  1.00 68.83           C  
-ATOM   3779  CD1 LEU B 181      37.646  29.092  53.844  1.00 71.01           C  
-ATOM   3780  CD2 LEU B 181      39.657  29.480  55.285  1.00 51.13           C  
-ATOM   3781  N   SER B 182      37.244  33.576  57.844  1.00 96.18           N  
-ATOM   3782  CA  SER B 182      36.725  34.916  58.072  1.00 97.12           C  
-ATOM   3783  C   SER B 182      37.510  35.560  59.208  1.00 98.93           C  
-ATOM   3784  O   SER B 182      37.645  36.784  59.263  1.00105.24           O  
-ATOM   3785  CB  SER B 182      35.233  34.868  58.422  1.00 95.41           C  
-ATOM   3786  OG  SER B 182      35.010  34.204  59.652  1.00 92.98           O  
-ATOM   3787  N   ARG B 183      38.032  34.724  60.106  1.00 96.57           N  
-ATOM   3788  CA  ARG B 183      38.815  35.193  61.251  1.00 93.67           C  
-ATOM   3789  C   ARG B 183      40.107  35.834  60.763  1.00 93.32           C  
-ATOM   3790  O   ARG B 183      40.700  36.672  61.446  1.00 91.19           O  
-ATOM   3791  CB  ARG B 183      39.161  34.027  62.183  1.00 92.70           C  
-ATOM   3792  CG  ARG B 183      37.970  33.310  62.798  1.00 88.40           C  
-ATOM   3793  CD  ARG B 183      37.237  34.188  63.793  1.00 82.41           C  
-ATOM   3794  NE  ARG B 183      36.136  33.474  64.436  1.00 81.26           N  
-ATOM   3795  CZ  ARG B 183      36.291  32.433  65.249  1.00 76.55           C  
-ATOM   3796  NH1 ARG B 183      37.504  31.978  65.526  1.00 67.63           N  
-ATOM   3797  NH2 ARG B 183      35.230  31.845  65.786  1.00 78.75           N  
-ATOM   3798  N   VAL B 184      40.542  35.419  59.578  1.00 94.84           N  
-ATOM   3799  CA  VAL B 184      41.759  35.945  58.980  1.00 96.36           C  
-ATOM   3800  C   VAL B 184      41.381  37.174  58.156  1.00100.22           C  
-ATOM   3801  O   VAL B 184      41.604  38.315  58.580  1.00102.47           O  
-ATOM   3802  CB  VAL B 184      42.429  34.886  58.068  1.00 89.87           C  
-ATOM   3803  CG1 VAL B 184      43.825  35.341  57.676  1.00 88.74           C  
-ATOM   3804  CG2 VAL B 184      42.491  33.546  58.782  1.00 79.22           C  
-ATOM   3805  N   SER B 185      40.784  36.926  56.991  1.00 99.98           N  
-ATOM   3806  CA  SER B 185      40.358  37.994  56.095  1.00 98.47           C  
-ATOM   3807  C   SER B 185      39.350  38.901  56.792  1.00 98.79           C  
-ATOM   3808  O   SER B 185      39.724  39.892  57.421  1.00 98.17           O  
-ATOM   3809  CB  SER B 185      39.744  37.401  54.837  1.00 94.62           C  
-ATOM   3810  N   GLU B 192      50.477  38.779  56.103  1.00 91.80           N  
-ATOM   3811  CA  GLU B 192      49.682  37.556  56.039  1.00 97.23           C  
-ATOM   3812  C   GLU B 192      49.007  37.381  54.668  1.00100.91           C  
-ATOM   3813  O   GLU B 192      49.059  38.277  53.823  1.00103.18           O  
-ATOM   3814  CB  GLU B 192      48.633  37.562  57.154  1.00 92.75           C  
-ATOM   3815  N   THR B 193      48.386  36.219  54.455  1.00102.56           N  
-ATOM   3816  CA  THR B 193      47.695  35.894  53.200  1.00 98.85           C  
-ATOM   3817  C   THR B 193      46.720  34.722  53.393  1.00 97.30           C  
-ATOM   3818  O   THR B 193      47.040  33.741  54.071  1.00 97.60           O  
-ATOM   3819  CB  THR B 193      48.715  35.548  52.116  1.00 96.55           C  
-ATOM   3820  N   VAL B 194      45.537  34.825  52.786  1.00 93.56           N  
-ATOM   3821  CA  VAL B 194      44.515  33.782  52.899  1.00 84.68           C  
-ATOM   3822  C   VAL B 194      44.445  32.875  51.671  1.00 79.04           C  
-ATOM   3823  O   VAL B 194      43.818  33.225  50.667  1.00 78.16           O  
-ATOM   3824  CB  VAL B 194      43.144  34.418  53.151  1.00 80.20           C  
-ATOM   3825  N   ASN B 195      45.098  31.717  51.759  1.00 71.77           N  
-ATOM   3826  CA  ASN B 195      45.098  30.738  50.672  1.00 65.88           C  
-ATOM   3827  C   ASN B 195      44.757  29.364  51.226  1.00 59.87           C  
-ATOM   3828  O   ASN B 195      45.484  28.823  52.055  1.00 60.82           O  
-ATOM   3829  CB  ASN B 195      46.464  30.675  49.967  1.00 65.00           C  
-ATOM   3830  CG  ASN B 195      47.570  30.119  50.855  1.00 60.35           C  
-ATOM   3831  OD1 ASN B 195      48.553  29.550  50.366  1.00 53.01           O  
-ATOM   3832  ND2 ASN B 195      47.423  30.296  52.163  1.00 60.98           N  
-ATOM   3833  N   LEU B 196      43.647  28.801  50.768  1.00 54.57           N  
-ATOM   3834  CA  LEU B 196      43.219  27.492  51.242  1.00 55.72           C  
-ATOM   3835  C   LEU B 196      44.379  26.504  51.406  1.00 52.06           C  
-ATOM   3836  O   LEU B 196      44.695  26.085  52.529  1.00 50.59           O  
-ATOM   3837  CB  LEU B 196      42.175  26.901  50.292  1.00 60.96           C  
-ATOM   3838  CG  LEU B 196      40.842  27.633  50.161  1.00 65.60           C  
-ATOM   3839  CD1 LEU B 196      40.081  27.061  48.968  1.00 72.42           C  
-ATOM   3840  CD2 LEU B 196      40.036  27.498  51.451  1.00 59.35           C  
-ATOM   3841  N   PRO B 197      45.044  26.141  50.291  1.00 42.29           N  
-ATOM   3842  CA  PRO B 197      46.164  25.198  50.300  1.00 35.01           C  
-ATOM   3843  C   PRO B 197      46.949  25.116  51.605  1.00 33.14           C  
-ATOM   3844  O   PRO B 197      47.028  24.049  52.218  1.00 36.84           O  
-ATOM   3845  CB  PRO B 197      47.009  25.678  49.136  1.00 34.81           C  
-ATOM   3846  CG  PRO B 197      45.962  26.063  48.156  1.00 37.81           C  
-ATOM   3847  CD  PRO B 197      44.994  26.855  49.003  1.00 35.54           C  
-ATOM   3848  N   PHE B 198      47.516  26.234  52.043  1.00 25.33           N  
-ATOM   3849  CA  PHE B 198      48.294  26.225  53.275  1.00 21.03           C  
-ATOM   3850  C   PHE B 198      47.439  25.956  54.503  1.00 22.11           C  
-ATOM   3851  O   PHE B 198      47.787  25.122  55.338  1.00 24.49           O  
-ATOM   3852  CB  PHE B 198      49.037  27.549  53.455  1.00 19.95           C  
-ATOM   3853  CG  PHE B 198      50.071  27.512  54.537  1.00  9.59           C  
-ATOM   3854  CD1 PHE B 198      51.175  26.690  54.419  1.00 18.53           C  
-ATOM   3855  CD2 PHE B 198      49.928  28.270  55.679  1.00 14.16           C  
-ATOM   3856  CE1 PHE B 198      52.120  26.618  55.421  1.00 14.14           C  
-ATOM   3857  CE2 PHE B 198      50.865  28.207  56.688  1.00 19.35           C  
-ATOM   3858  CZ  PHE B 198      51.964  27.378  56.558  1.00 20.58           C  
-ATOM   3859  N   VAL B 199      46.322  26.669  54.611  1.00 22.25           N  
-ATOM   3860  CA  VAL B 199      45.416  26.509  55.740  1.00 23.68           C  
-ATOM   3861  C   VAL B 199      44.943  25.067  55.824  1.00 21.19           C  
-ATOM   3862  O   VAL B 199      45.189  24.365  56.813  1.00 19.47           O  
-ATOM   3863  CB  VAL B 199      44.197  27.452  55.607  1.00 20.37           C  
-ATOM   3864  CG1 VAL B 199      43.081  27.007  56.529  1.00 28.94           C  
-ATOM   3865  CG2 VAL B 199      44.613  28.873  55.958  1.00 20.07           C  
-ATOM   3866  N   MET B 200      44.273  24.631  54.768  1.00 19.41           N  
-ATOM   3867  CA  MET B 200      43.760  23.271  54.694  1.00 23.85           C  
-ATOM   3868  C   MET B 200      44.803  22.291  55.234  1.00 21.05           C  
-ATOM   3869  O   MET B 200      44.486  21.379  56.011  1.00 20.68           O  
-ATOM   3870  CB  MET B 200      43.422  22.932  53.238  1.00 23.98           C  
-ATOM   3871  CG  MET B 200      42.173  22.076  53.073  1.00 37.74           C  
-ATOM   3872  SD  MET B 200      40.678  22.849  53.740  1.00 43.93           S  
-ATOM   3873  CE  MET B 200      40.211  23.886  52.360  1.00 33.63           C  
-ATOM   3874  N   VAL B 201      46.052  22.500  54.831  1.00 14.56           N  
-ATOM   3875  CA  VAL B 201      47.140  21.647  55.267  1.00  8.85           C  
-ATOM   3876  C   VAL B 201      47.437  21.823  56.740  1.00  4.47           C  
-ATOM   3877  O   VAL B 201      47.451  20.859  57.500  1.00  5.23           O  
-ATOM   3878  CB  VAL B 201      48.415  21.933  54.466  1.00  8.68           C  
-ATOM   3879  CG1 VAL B 201      49.605  21.238  55.111  1.00 13.86           C  
-ATOM   3880  CG2 VAL B 201      48.238  21.440  53.038  1.00  4.47           C  
-ATOM   3881  N   LEU B 202      47.668  23.061  57.140  1.00  4.47           N  
-ATOM   3882  CA  LEU B 202      47.983  23.361  58.530  1.00 13.05           C  
-ATOM   3883  C   LEU B 202      46.999  22.681  59.469  1.00 14.68           C  
-ATOM   3884  O   LEU B 202      47.392  22.036  60.439  1.00 16.28           O  
-ATOM   3885  CB  LEU B 202      47.960  24.878  58.763  1.00 18.11           C  
-ATOM   3886  CG  LEU B 202      48.638  25.381  60.044  1.00 26.28           C  
-ATOM   3887  CD1 LEU B 202      50.047  24.789  60.139  1.00 32.42           C  
-ATOM   3888  CD2 LEU B 202      48.712  26.903  60.036  1.00 25.52           C  
-ATOM   3889  N   ARG B 203      45.715  22.825  59.175  1.00 16.31           N  
-ATOM   3890  CA  ARG B 203      44.687  22.216  59.996  1.00 17.43           C  
-ATOM   3891  C   ARG B 203      44.979  20.717  60.071  1.00 25.98           C  
-ATOM   3892  O   ARG B 203      45.085  20.138  61.170  1.00 28.61           O  
-ATOM   3893  CB  ARG B 203      43.330  22.473  59.353  1.00 19.04           C  
-ATOM   3894  CG  ARG B 203      43.181  23.915  58.889  1.00 34.19           C  
-ATOM   3895  CD  ARG B 203      41.883  24.176  58.146  1.00 49.33           C  
-ATOM   3896  NE  ARG B 203      40.854  24.747  59.012  1.00 52.37           N  
-ATOM   3897  CZ  ARG B 203      40.046  24.043  59.801  1.00 58.01           C  
-ATOM   3898  NH1 ARG B 203      40.126  22.716  59.854  1.00 54.41           N  
-ATOM   3899  NH2 ARG B 203      39.146  24.676  60.537  1.00 62.81           N  
-ATOM   3900  N   ASN B 204      45.131  20.103  58.894  1.00 22.46           N  
-ATOM   3901  CA  ASN B 204      45.418  18.675  58.793  1.00 17.10           C  
-ATOM   3902  C   ASN B 204      46.606  18.247  59.630  1.00 19.44           C  
-ATOM   3903  O   ASN B 204      46.495  17.353  60.476  1.00 25.77           O  
-ATOM   3904  CB  ASN B 204      45.649  18.290  57.337  1.00  8.20           C  
-ATOM   3905  CG  ASN B 204      44.353  18.014  56.606  1.00 23.92           C  
-ATOM   3906  OD1 ASN B 204      44.153  18.467  55.479  1.00 34.21           O  
-ATOM   3907  ND2 ASN B 204      43.464  17.251  57.242  1.00 26.94           N  
-ATOM   3908  N   VAL B 205      47.746  18.884  59.399  1.00 17.87           N  
-ATOM   3909  CA  VAL B 205      48.942  18.552  60.154  1.00 15.46           C  
-ATOM   3910  C   VAL B 205      48.672  18.507  61.657  1.00 15.06           C  
-ATOM   3911  O   VAL B 205      48.921  17.482  62.295  1.00 19.32           O  
-ATOM   3912  CB  VAL B 205      50.060  19.550  59.875  1.00  9.29           C  
-ATOM   3913  CG1 VAL B 205      51.302  19.182  60.666  1.00  5.80           C  
-ATOM   3914  CG2 VAL B 205      50.356  19.556  58.397  1.00 13.01           C  
-ATOM   3915  N   TYR B 206      48.153  19.596  62.222  1.00  6.94           N  
-ATOM   3916  CA  TYR B 206      47.876  19.611  63.655  1.00 13.04           C  
-ATOM   3917  C   TYR B 206      47.062  18.395  64.062  1.00 13.07           C  
-ATOM   3918  O   TYR B 206      47.349  17.746  65.075  1.00 19.33           O  
-ATOM   3919  CB  TYR B 206      47.172  20.906  64.082  1.00  7.76           C  
-ATOM   3920  CG  TYR B 206      48.154  21.940  64.584  1.00  4.47           C  
-ATOM   3921  CD1 TYR B 206      48.901  21.715  65.729  1.00  6.99           C  
-ATOM   3922  CD2 TYR B 206      48.371  23.122  63.888  1.00 12.15           C  
-ATOM   3923  CE1 TYR B 206      49.848  22.650  66.170  1.00 21.73           C  
-ATOM   3924  CE2 TYR B 206      49.309  24.053  64.318  1.00 16.23           C  
-ATOM   3925  CZ  TYR B 206      50.042  23.814  65.458  1.00 19.41           C  
-ATOM   3926  OH  TYR B 206      50.962  24.745  65.883  1.00 26.32           O  
-ATOM   3927  N   ILE B 207      46.052  18.063  63.278  1.00  6.79           N  
-ATOM   3928  CA  ILE B 207      45.285  16.895  63.625  1.00 11.23           C  
-ATOM   3929  C   ILE B 207      46.244  15.716  63.732  1.00 17.77           C  
-ATOM   3930  O   ILE B 207      46.257  15.009  64.749  1.00 21.10           O  
-ATOM   3931  CB  ILE B 207      44.216  16.620  62.583  1.00 10.63           C  
-ATOM   3932  CG1 ILE B 207      43.032  17.547  62.842  1.00 10.85           C  
-ATOM   3933  CG2 ILE B 207      43.791  15.169  62.641  1.00 15.69           C  
-ATOM   3934  CD1 ILE B 207      42.518  17.459  64.282  1.00 11.72           C  
-ATOM   3935  N   MET B 208      47.054  15.514  62.693  1.00 15.16           N  
-ATOM   3936  CA  MET B 208      48.030  14.431  62.705  1.00 16.77           C  
-ATOM   3937  C   MET B 208      48.858  14.478  63.984  1.00 15.19           C  
-ATOM   3938  O   MET B 208      48.958  13.485  64.708  1.00 16.68           O  
-ATOM   3939  CB  MET B 208      48.958  14.531  61.504  1.00 12.03           C  
-ATOM   3940  CG  MET B 208      48.341  14.040  60.229  1.00 21.14           C  
-ATOM   3941  SD  MET B 208      49.454  14.277  58.853  1.00 20.32           S  
-ATOM   3942  CE  MET B 208      49.064  15.929  58.391  1.00 13.32           C  
-ATOM   3943  N   LEU B 209      49.442  15.634  64.267  1.00  9.58           N  
-ATOM   3944  CA  LEU B 209      50.254  15.778  65.465  1.00 15.89           C  
-ATOM   3945  C   LEU B 209      49.574  15.018  66.589  1.00 25.15           C  
-ATOM   3946  O   LEU B 209      50.137  14.061  67.146  1.00 26.93           O  
-ATOM   3947  CB  LEU B 209      50.382  17.245  65.870  1.00 12.03           C  
-ATOM   3948  CG  LEU B 209      51.605  17.648  66.708  1.00  8.17           C  
-ATOM   3949  CD1 LEU B 209      51.364  19.027  67.299  1.00 19.23           C  
-ATOM   3950  CD2 LEU B 209      51.855  16.671  67.816  1.00  4.47           C  
-ATOM   3951  N   ILE B 210      48.354  15.438  66.912  1.00 22.41           N  
-ATOM   3952  CA  ILE B 210      47.607  14.790  67.975  1.00 19.58           C  
-ATOM   3953  C   ILE B 210      47.612  13.272  67.779  1.00 20.14           C  
-ATOM   3954  O   ILE B 210      48.092  12.533  68.658  1.00 19.48           O  
-ATOM   3955  CB  ILE B 210      46.162  15.337  68.045  1.00 17.56           C  
-ATOM   3956  CG1 ILE B 210      46.203  16.803  68.489  1.00 17.49           C  
-ATOM   3957  CG2 ILE B 210      45.337  14.540  69.034  1.00 13.26           C  
-ATOM   3958  CD1 ILE B 210      44.850  17.448  68.640  1.00 14.91           C  
-ATOM   3959  N   ASN B 211      47.113  12.802  66.634  1.00  4.47           N  
-ATOM   3960  CA  ASN B 211      47.094  11.367  66.400  1.00  7.08           C  
-ATOM   3961  C   ASN B 211      48.456  10.753  66.638  1.00  8.73           C  
-ATOM   3962  O   ASN B 211      48.549   9.627  67.116  1.00 14.07           O  
-ATOM   3963  CB  ASN B 211      46.642  11.031  64.983  1.00 12.25           C  
-ATOM   3964  CG  ASN B 211      45.169  11.318  64.757  1.00 24.09           C  
-ATOM   3965  OD1 ASN B 211      44.355  11.193  65.671  1.00 38.81           O  
-ATOM   3966  ND2 ASN B 211      44.816  11.681  63.529  1.00 21.19           N  
-ATOM   3967  N   THR B 212      49.512  11.498  66.319  1.00  9.15           N  
-ATOM   3968  CA  THR B 212      50.876  11.008  66.504  1.00  9.73           C  
-ATOM   3969  C   THR B 212      51.246  10.853  67.972  1.00 10.05           C  
-ATOM   3970  O   THR B 212      51.929   9.893  68.365  1.00  4.47           O  
-ATOM   3971  CB  THR B 212      51.897  11.951  65.906  1.00 10.20           C  
-ATOM   3972  OG1 THR B 212      51.576  12.203  64.531  1.00 14.80           O  
-ATOM   3973  CG2 THR B 212      53.286  11.324  66.014  1.00  8.99           C  
-ATOM   3974  N   ILE B 213      50.811  11.816  68.778  1.00 12.76           N  
-ATOM   3975  CA  ILE B 213      51.103  11.772  70.199  1.00 14.60           C  
-ATOM   3976  C   ILE B 213      50.458  10.527  70.775  1.00 15.88           C  
-ATOM   3977  O   ILE B 213      51.129   9.710  71.395  1.00 16.97           O  
-ATOM   3978  CB  ILE B 213      50.560  13.006  70.923  1.00  6.68           C  
-ATOM   3979  CG1 ILE B 213      51.013  14.267  70.197  1.00  9.08           C  
-ATOM   3980  CG2 ILE B 213      51.092  13.037  72.342  1.00  6.35           C  
-ATOM   3981  CD1 ILE B 213      50.622  15.550  70.881  1.00 15.06           C  
-ATOM   3982  N   ILE B 214      49.153  10.384  70.559  1.00 17.98           N  
-ATOM   3983  CA  ILE B 214      48.423   9.219  71.052  1.00 16.27           C  
-ATOM   3984  C   ILE B 214      49.104   7.950  70.554  1.00 18.02           C  
-ATOM   3985  O   ILE B 214      49.487   7.091  71.351  1.00 21.53           O  
-ATOM   3986  CB  ILE B 214      46.980   9.206  70.539  1.00 14.13           C  
-ATOM   3987  CG1 ILE B 214      46.300  10.527  70.885  1.00 14.20           C  
-ATOM   3988  CG2 ILE B 214      46.223   8.032  71.141  1.00  4.47           C  
-ATOM   3989  CD1 ILE B 214      44.943  10.683  70.224  1.00 22.43           C  
-ATOM   3990  N   PHE B 215      49.237   7.841  69.233  1.00  8.56           N  
-ATOM   3991  CA  PHE B 215      49.877   6.697  68.594  1.00 10.31           C  
-ATOM   3992  C   PHE B 215      51.164   6.328  69.331  1.00 23.49           C  
-ATOM   3993  O   PHE B 215      51.354   5.171  69.738  1.00 29.98           O  
-ATOM   3994  CB  PHE B 215      50.193   7.039  67.133  1.00  7.98           C  
-ATOM   3995  CG  PHE B 215      50.890   5.942  66.387  1.00 12.55           C  
-ATOM   3996  CD1 PHE B 215      52.255   5.742  66.531  1.00 20.10           C  
-ATOM   3997  CD2 PHE B 215      50.175   5.087  65.557  1.00 20.92           C  
-ATOM   3998  CE1 PHE B 215      52.899   4.699  65.859  1.00 27.29           C  
-ATOM   3999  CE2 PHE B 215      50.805   4.045  64.883  1.00 25.30           C  
-ATOM   4000  CZ  PHE B 215      52.170   3.849  65.034  1.00 26.28           C  
-ATOM   4001  N   LEU B 216      52.037   7.320  69.498  1.00 15.06           N  
-ATOM   4002  CA  LEU B 216      53.319   7.150  70.168  1.00 10.94           C  
-ATOM   4003  C   LEU B 216      53.216   6.645  71.615  1.00 18.96           C  
-ATOM   4004  O   LEU B 216      54.171   6.085  72.153  1.00 28.81           O  
-ATOM   4005  CB  LEU B 216      54.057   8.485  70.141  1.00 13.16           C  
-ATOM   4006  CG  LEU B 216      55.287   8.666  69.252  1.00 18.55           C  
-ATOM   4007  CD1 LEU B 216      55.199   7.801  68.012  1.00 18.06           C  
-ATOM   4008  CD2 LEU B 216      55.404  10.136  68.887  1.00 15.83           C  
-ATOM   4009  N   LYS B 217      52.067   6.852  72.249  1.00 21.05           N  
-ATOM   4010  CA  LYS B 217      51.865   6.428  73.629  1.00 21.12           C  
-ATOM   4011  C   LYS B 217      51.970   4.922  73.787  1.00 31.70           C  
-ATOM   4012  O   LYS B 217      52.493   4.432  74.791  1.00 34.76           O  
-ATOM   4013  CB  LYS B 217      50.496   6.893  74.124  1.00 16.38           C  
-ATOM   4014  CG  LYS B 217      50.450   8.330  74.591  1.00 14.68           C  
-ATOM   4015  CD  LYS B 217      51.343   8.510  75.812  1.00 27.74           C  
-ATOM   4016  CE  LYS B 217      51.088   9.842  76.509  1.00 33.34           C  
-ATOM   4017  NZ  LYS B 217      51.224  10.997  75.589  1.00 29.96           N  
-ATOM   4018  N   THR B 218      51.482   4.195  72.783  1.00 38.52           N  
-ATOM   4019  CA  THR B 218      51.480   2.730  72.794  1.00 39.51           C  
-ATOM   4020  C   THR B 218      52.561   2.077  71.926  1.00 36.17           C  
-ATOM   4021  O   THR B 218      53.357   1.270  72.419  1.00 39.29           O  
-ATOM   4022  CB  THR B 218      50.113   2.176  72.316  1.00 37.77           C  
-ATOM   4023  OG1 THR B 218      49.052   2.950  72.886  1.00 38.00           O  
-ATOM   4024  CG2 THR B 218      49.949   0.731  72.743  1.00 39.07           C  
-ATOM   4025  N   ASN B 219      52.582   2.434  70.642  1.00 30.26           N  
-ATOM   4026  CA  ASN B 219      53.529   1.860  69.690  1.00 33.70           C  
-ATOM   4027  C   ASN B 219      54.763   2.711  69.397  1.00 34.05           C  
-ATOM   4028  O   ASN B 219      54.796   3.911  69.669  1.00 27.36           O  
-ATOM   4029  CB  ASN B 219      52.810   1.583  68.371  1.00 39.46           C  
-ATOM   4030  CG  ASN B 219      51.317   1.437  68.546  1.00 53.86           C  
-ATOM   4031  OD1 ASN B 219      50.844   0.494  69.188  1.00 69.98           O  
-ATOM   4032  ND2 ASN B 219      50.559   2.377  67.984  1.00 49.86           N  
-ATOM   4033  N   ASN B 220      55.772   2.064  68.820  1.00 38.28           N  
-ATOM   4034  CA  ASN B 220      57.018   2.715  68.436  1.00 42.57           C  
-ATOM   4035  C   ASN B 220      56.841   3.281  67.016  1.00 40.38           C  
-ATOM   4036  O   ASN B 220      56.004   2.797  66.265  1.00 40.69           O  
-ATOM   4037  CB  ASN B 220      58.145   1.685  68.447  1.00 47.15           C  
-ATOM   4038  CG  ASN B 220      59.493   2.287  68.102  1.00 64.92           C  
-ATOM   4039  OD1 ASN B 220      60.281   1.683  67.366  1.00 76.91           O  
-ATOM   4040  ND2 ASN B 220      59.774   3.481  68.636  1.00 67.57           N  
-ATOM   4041  N   TRP B 221      57.617   4.295  66.634  1.00 43.91           N  
-ATOM   4042  CA  TRP B 221      57.477   4.860  65.291  1.00 35.14           C  
-ATOM   4043  C   TRP B 221      57.699   3.822  64.209  1.00 40.93           C  
-ATOM   4044  O   TRP B 221      57.132   3.927  63.130  1.00 45.77           O  
-ATOM   4045  CB  TRP B 221      58.445   6.020  65.053  1.00 23.35           C  
-ATOM   4046  CG  TRP B 221      59.897   5.642  64.936  1.00 14.24           C  
-ATOM   4047  CD1 TRP B 221      60.799   5.519  65.954  1.00 23.24           C  
-ATOM   4048  CD2 TRP B 221      60.623   5.388  63.729  1.00  9.75           C  
-ATOM   4049  NE1 TRP B 221      62.047   5.210  65.454  1.00 20.89           N  
-ATOM   4050  CE2 TRP B 221      61.965   5.123  64.092  1.00 11.74           C  
-ATOM   4051  CE3 TRP B 221      60.273   5.363  62.376  1.00 21.12           C  
-ATOM   4052  CZ2 TRP B 221      62.957   4.837  63.152  1.00 15.20           C  
-ATOM   4053  CZ3 TRP B 221      61.264   5.078  61.433  1.00 22.74           C  
-ATOM   4054  CH2 TRP B 221      62.591   4.818  61.830  1.00 18.08           C  
-ATOM   4055  N   HIS B 222      58.516   2.816  64.500  1.00 47.40           N  
-ATOM   4056  CA  HIS B 222      58.809   1.777  63.524  1.00 50.89           C  
-ATOM   4057  C   HIS B 222      57.689   0.750  63.422  1.00 48.00           C  
-ATOM   4058  O   HIS B 222      57.950  -0.423  63.182  1.00 58.60           O  
-ATOM   4059  CB  HIS B 222      60.127   1.058  63.869  1.00 60.91           C  
-ATOM   4060  CG  HIS B 222      60.924   0.648  62.664  1.00 81.69           C  
-ATOM   4061  ND1 HIS B 222      60.343   0.110  61.533  1.00 87.07           N  
-ATOM   4062  CD2 HIS B 222      62.253   0.721  62.402  1.00 87.81           C  
-ATOM   4063  CE1 HIS B 222      61.277  -0.127  60.627  1.00 86.42           C  
-ATOM   4064  NE2 HIS B 222      62.445   0.235  61.129  1.00 88.92           N  
-ATOM   4065  N   ALA B 223      56.446   1.178  63.602  1.00 42.18           N  
-ATOM   4066  CA  ALA B 223      55.322   0.251  63.510  1.00 38.83           C  
-ATOM   4067  C   ALA B 223      55.128  -0.173  62.063  1.00 44.27           C  
-ATOM   4068  O   ALA B 223      55.987  -0.829  61.464  1.00 45.46           O  
-ATOM   4069  CB  ALA B 223      54.049   0.901  64.023  1.00 32.14           C  
-ATOM   4070  N   GLY B 224      53.989   0.202  61.495  1.00 43.77           N  
-ATOM   4071  CA  GLY B 224      53.726  -0.159  60.119  1.00 44.22           C  
-ATOM   4072  C   GLY B 224      54.516   0.729  59.182  1.00 46.35           C  
-ATOM   4073  O   GLY B 224      54.009   1.146  58.141  1.00 48.79           O  
-ATOM   4074  N   TRP B 225      55.757   1.033  59.551  1.00 45.35           N  
-ATOM   4075  CA  TRP B 225      56.595   1.891  58.721  1.00 38.82           C  
-ATOM   4076  C   TRP B 225      56.743   1.266  57.346  1.00 35.03           C  
-ATOM   4077  O   TRP B 225      56.576   1.930  56.324  1.00 41.37           O  
-ATOM   4078  CB  TRP B 225      57.968   2.097  59.375  1.00 32.84           C  
-ATOM   4079  CG  TRP B 225      58.923   2.957  58.577  1.00 32.73           C  
-ATOM   4080  CD1 TRP B 225      59.943   2.520  57.774  1.00 40.54           C  
-ATOM   4081  CD2 TRP B 225      58.931   4.395  58.485  1.00 25.55           C  
-ATOM   4082  NE1 TRP B 225      60.584   3.593  57.189  1.00 39.74           N  
-ATOM   4083  CE2 TRP B 225      59.983   4.752  57.607  1.00 31.13           C  
-ATOM   4084  CE3 TRP B 225      58.151   5.411  59.053  1.00  8.96           C  
-ATOM   4085  CZ2 TRP B 225      60.271   6.080  57.287  1.00 23.73           C  
-ATOM   4086  CZ3 TRP B 225      58.436   6.724  58.730  1.00 16.86           C  
-ATOM   4087  CH2 TRP B 225      59.489   7.047  57.855  1.00 23.91           C  
-ATOM   4088  N   ASN B 226      57.031  -0.025  57.316  1.00 36.25           N  
-ATOM   4089  CA  ASN B 226      57.195  -0.713  56.046  1.00 39.46           C  
-ATOM   4090  C   ASN B 226      55.851  -1.001  55.379  1.00 38.78           C  
-ATOM   4091  O   ASN B 226      55.765  -1.757  54.418  1.00 36.00           O  
-ATOM   4092  CB  ASN B 226      57.990  -1.998  56.259  1.00 44.53           C  
-ATOM   4093  CG  ASN B 226      59.401  -1.726  56.763  1.00 56.49           C  
-ATOM   4094  OD1 ASN B 226      60.196  -1.068  56.089  1.00 58.51           O  
-ATOM   4095  ND2 ASN B 226      59.714  -2.222  57.956  1.00 61.39           N  
-ATOM   4096  N   THR B 227      54.799  -0.380  55.895  1.00 43.42           N  
-ATOM   4097  CA  THR B 227      53.457  -0.546  55.339  1.00 42.14           C  
-ATOM   4098  C   THR B 227      52.943   0.857  55.022  1.00 43.04           C  
-ATOM   4099  O   THR B 227      51.820   1.030  54.538  1.00 48.33           O  
-ATOM   4100  CB  THR B 227      52.488  -1.218  56.355  1.00 48.74           C  
-ATOM   4101  OG1 THR B 227      52.051  -0.254  57.336  1.00 54.19           O  
-ATOM   4102  CG2 THR B 227      53.194  -2.388  57.060  1.00 47.02           C  
-ATOM   4103  N   LEU B 228      53.777   1.851  55.318  1.00 32.52           N  
-ATOM   4104  CA  LEU B 228      53.448   3.244  55.077  1.00 24.96           C  
-ATOM   4105  C   LEU B 228      53.889   3.584  53.681  1.00 24.62           C  
-ATOM   4106  O   LEU B 228      55.073   3.487  53.373  1.00 27.75           O  
-ATOM   4107  CB  LEU B 228      54.210   4.135  56.040  1.00 21.10           C  
-ATOM   4108  CG  LEU B 228      53.382   4.863  57.077  1.00 27.23           C  
-ATOM   4109  CD1 LEU B 228      54.314   5.700  57.942  1.00 30.87           C  
-ATOM   4110  CD2 LEU B 228      52.333   5.720  56.379  1.00 29.24           C  
-ATOM   4111  N   SER B 229      52.957   3.968  52.823  1.00 22.79           N  
-ATOM   4112  CA  SER B 229      53.367   4.327  51.475  1.00 29.56           C  
-ATOM   4113  C   SER B 229      54.154   5.622  51.624  1.00 25.33           C  
-ATOM   4114  O   SER B 229      53.876   6.440  52.518  1.00 18.45           O  
-ATOM   4115  CB  SER B 229      52.152   4.528  50.558  1.00 37.19           C  
-ATOM   4116  OG  SER B 229      51.249   5.459  51.125  1.00 58.37           O  
-ATOM   4117  N   PHE B 230      55.160   5.800  50.782  1.00 19.54           N  
-ATOM   4118  CA  PHE B 230      55.936   7.016  50.869  1.00 17.91           C  
-ATOM   4119  C   PHE B 230      55.018   8.208  50.659  1.00 22.77           C  
-ATOM   4120  O   PHE B 230      53.871   8.047  50.252  1.00 32.68           O  
-ATOM   4121  CB  PHE B 230      57.029   7.016  49.816  1.00 18.25           C  
-ATOM   4122  CG  PHE B 230      58.196   6.164  50.173  1.00  9.08           C  
-ATOM   4123  CD1 PHE B 230      58.291   4.873  49.707  1.00 15.42           C  
-ATOM   4124  CD2 PHE B 230      59.211   6.663  50.981  1.00  5.32           C  
-ATOM   4125  CE1 PHE B 230      59.391   4.090  50.042  1.00 24.70           C  
-ATOM   4126  CE2 PHE B 230      60.307   5.894  51.321  1.00  4.47           C  
-ATOM   4127  CZ  PHE B 230      60.403   4.611  50.854  1.00  6.98           C  
-ATOM   4128  N   CYS B 231      55.518   9.405  50.940  1.00 22.00           N  
-ATOM   4129  CA  CYS B 231      54.729  10.616  50.765  1.00 20.99           C  
-ATOM   4130  C   CYS B 231      54.818  11.039  49.294  1.00 25.77           C  
-ATOM   4131  O   CYS B 231      55.901  11.324  48.784  1.00 26.83           O  
-ATOM   4132  CB  CYS B 231      55.260  11.718  51.677  1.00 16.45           C  
-ATOM   4133  SG  CYS B 231      54.314  13.233  51.619  1.00 33.84           S  
-ATOM   4134  N   ASN B 232      53.673  11.066  48.616  1.00 28.14           N  
-ATOM   4135  CA  ASN B 232      53.613  11.421  47.202  1.00 23.30           C  
-ATOM   4136  C   ASN B 232      52.789  12.680  46.968  1.00 28.08           C  
-ATOM   4137  O   ASN B 232      52.122  13.187  47.877  1.00 30.80           O  
-ATOM   4138  CB  ASN B 232      53.011  10.257  46.416  1.00 26.41           C  
-ATOM   4139  CG  ASN B 232      51.625   9.889  46.902  1.00 38.60           C  
-ATOM   4140  OD1 ASN B 232      50.691  10.671  46.765  1.00 58.94           O  
-ATOM   4141  ND2 ASN B 232      51.485   8.704  47.484  1.00 43.79           N  
-ATOM   4142  N   ASP B 233      52.826  13.178  45.738  1.00 31.84           N  
-ATOM   4143  CA  ASP B 233      52.086  14.384  45.387  1.00 33.77           C  
-ATOM   4144  C   ASP B 233      50.585  14.192  45.517  1.00 27.23           C  
-ATOM   4145  O   ASP B 233      49.856  15.131  45.831  1.00 28.11           O  
-ATOM   4146  CB  ASP B 233      52.439  14.825  43.966  1.00 40.74           C  
-ATOM   4147  CG  ASP B 233      53.906  15.186  43.820  1.00 51.99           C  
-ATOM   4148  OD1 ASP B 233      54.759  14.285  43.985  1.00 58.54           O  
-ATOM   4149  OD2 ASP B 233      54.204  16.370  43.551  1.00 56.27           O  
-ATOM   4150  N   VAL B 234      50.129  12.972  45.267  1.00 23.58           N  
-ATOM   4151  CA  VAL B 234      48.711  12.663  45.376  1.00 31.34           C  
-ATOM   4152  C   VAL B 234      48.273  12.916  46.819  1.00 35.22           C  
-ATOM   4153  O   VAL B 234      47.231  13.525  47.075  1.00 41.05           O  
-ATOM   4154  CB  VAL B 234      48.433  11.184  45.041  1.00 32.07           C  
-ATOM   4155  CG1 VAL B 234      46.935  10.916  45.093  1.00 35.54           C  
-ATOM   4156  CG2 VAL B 234      49.015  10.838  43.683  1.00 34.92           C  
-ATOM   4157  N   PHE B 235      49.084  12.433  47.755  1.00 32.74           N  
-ATOM   4158  CA  PHE B 235      48.818  12.579  49.173  1.00 19.64           C  
-ATOM   4159  C   PHE B 235      48.757  14.055  49.482  1.00 18.52           C  
-ATOM   4160  O   PHE B 235      47.769  14.538  50.029  1.00 20.05           O  
-ATOM   4161  CB  PHE B 235      49.941  11.933  49.978  1.00 23.07           C  
-ATOM   4162  CG  PHE B 235      49.726  11.966  51.462  1.00 32.14           C  
-ATOM   4163  CD1 PHE B 235      50.811  11.936  52.331  1.00 34.65           C  
-ATOM   4164  CD2 PHE B 235      48.446  12.015  51.997  1.00 39.57           C  
-ATOM   4165  CE1 PHE B 235      50.622  11.956  53.709  1.00 32.06           C  
-ATOM   4166  CE2 PHE B 235      48.245  12.034  53.379  1.00 30.93           C  
-ATOM   4167  CZ  PHE B 235      49.333  12.005  54.231  1.00 32.75           C  
-ATOM   4168  N   LYS B 236      49.815  14.774  49.119  1.00 15.28           N  
-ATOM   4169  CA  LYS B 236      49.867  16.208  49.371  1.00 17.66           C  
-ATOM   4170  C   LYS B 236      48.631  16.916  48.820  1.00 25.76           C  
-ATOM   4171  O   LYS B 236      48.092  17.826  49.458  1.00 22.88           O  
-ATOM   4172  CB  LYS B 236      51.125  16.813  48.755  1.00  8.12           C  
-ATOM   4173  CG  LYS B 236      52.420  16.300  49.352  1.00 19.58           C  
-ATOM   4174  CD  LYS B 236      53.617  17.049  48.781  1.00 26.70           C  
-ATOM   4175  CE  LYS B 236      54.946  16.394  49.143  1.00 32.78           C  
-ATOM   4176  NZ  LYS B 236      56.082  17.067  48.451  1.00 32.00           N  
-ATOM   4177  N   GLN B 237      48.182  16.491  47.638  1.00 31.32           N  
-ATOM   4178  CA  GLN B 237      46.999  17.074  47.007  1.00 31.95           C  
-ATOM   4179  C   GLN B 237      45.767  16.999  47.904  1.00 34.64           C  
-ATOM   4180  O   GLN B 237      45.062  17.990  48.077  1.00 39.16           O  
-ATOM   4181  CB  GLN B 237      46.699  16.376  45.683  1.00 37.64           C  
-ATOM   4182  CG  GLN B 237      47.612  16.795  44.559  1.00 45.52           C  
-ATOM   4183  CD  GLN B 237      47.568  18.283  44.334  1.00 56.19           C  
-ATOM   4184  OE1 GLN B 237      46.497  18.858  44.114  1.00 60.85           O  
-ATOM   4185  NE2 GLN B 237      48.731  18.925  44.391  1.00 64.59           N  
-ATOM   4186  N   LYS B 238      45.495  15.827  48.466  1.00 35.05           N  
-ATOM   4187  CA  LYS B 238      44.341  15.700  49.342  1.00 40.28           C  
-ATOM   4188  C   LYS B 238      44.490  16.661  50.520  1.00 41.27           C  
-ATOM   4189  O   LYS B 238      43.544  17.368  50.868  1.00 50.10           O  
-ATOM   4190  CB  LYS B 238      44.206  14.268  49.879  1.00 46.78           C  
-ATOM   4191  CG  LYS B 238      43.842  13.214  48.844  1.00 60.43           C  
-ATOM   4192  CD  LYS B 238      43.700  11.835  49.499  1.00 65.47           C  
-ATOM   4193  CE  LYS B 238      43.489  10.731  48.468  1.00 67.39           C  
-ATOM   4194  NZ  LYS B 238      43.497   9.380  49.103  1.00 71.13           N  
-ATOM   4195  N   LEU B 239      45.684  16.696  51.115  1.00 29.76           N  
-ATOM   4196  CA  LEU B 239      45.942  17.539  52.274  1.00 19.42           C  
-ATOM   4197  C   LEU B 239      45.695  19.025  52.045  1.00 30.12           C  
-ATOM   4198  O   LEU B 239      45.510  19.785  53.000  1.00 34.30           O  
-ATOM   4199  CB  LEU B 239      47.369  17.317  52.762  1.00 11.32           C  
-ATOM   4200  CG  LEU B 239      47.669  15.916  53.307  1.00 13.35           C  
-ATOM   4201  CD1 LEU B 239      49.129  15.811  53.727  1.00 13.49           C  
-ATOM   4202  CD2 LEU B 239      46.769  15.631  54.493  1.00  9.37           C  
-ATOM   4203  N   GLN B 240      45.688  19.441  50.782  1.00 33.30           N  
-ATOM   4204  CA  GLN B 240      45.451  20.845  50.437  1.00 34.20           C  
-ATOM   4205  C   GLN B 240      43.992  21.107  50.062  1.00 40.54           C  
-ATOM   4206  O   GLN B 240      43.594  22.260  49.875  1.00 43.84           O  
-ATOM   4207  CB  GLN B 240      46.335  21.258  49.258  1.00 28.83           C  
-ATOM   4208  CG  GLN B 240      47.817  21.323  49.572  1.00 33.33           C  
-ATOM   4209  CD  GLN B 240      48.692  21.451  48.329  1.00 28.89           C  
-ATOM   4210  OE1 GLN B 240      48.564  22.395  47.548  1.00 32.47           O  
-ATOM   4211  NE2 GLN B 240      49.592  20.499  48.149  1.00 20.41           N  
-ATOM   4212  N   LYS B 241      43.194  20.045  49.963  1.00 42.21           N  
-ATOM   4213  CA  LYS B 241      41.802  20.198  49.574  1.00 44.78           C  
-ATOM   4214  C   LYS B 241      40.703  19.772  50.548  1.00 50.77           C  
-ATOM   4215  O   LYS B 241      39.850  20.581  50.916  1.00 55.87           O  
-ATOM   4216  CB  LYS B 241      41.572  19.481  48.247  1.00 41.38           C  
-ATOM   4217  CG  LYS B 241      42.313  20.091  47.066  1.00 57.00           C  
-ATOM   4218  CD  LYS B 241      42.058  19.300  45.777  1.00 65.76           C  
-ATOM   4219  CE  LYS B 241      42.757  19.925  44.574  1.00 68.06           C  
-ATOM   4220  NZ  LYS B 241      42.254  21.305  44.290  1.00 74.78           N  
-ATOM   4221  N   SER B 242      40.725  18.520  50.981  1.00 50.41           N  
-ATOM   4222  CA  SER B 242      39.652  18.021  51.830  1.00 56.04           C  
-ATOM   4223  C   SER B 242      39.720  18.039  53.346  1.00 57.51           C  
-ATOM   4224  O   SER B 242      38.719  17.725  53.991  1.00 66.07           O  
-ATOM   4225  CB  SER B 242      39.290  16.598  51.391  1.00 67.26           C  
-ATOM   4226  OG  SER B 242      40.413  15.731  51.441  1.00 77.22           O  
-ATOM   4227  N   GLU B 243      40.847  18.401  53.942  1.00 53.96           N  
-ATOM   4228  CA  GLU B 243      40.887  18.374  55.405  1.00 59.81           C  
-ATOM   4229  C   GLU B 243      40.515  16.948  55.824  1.00 53.45           C  
-ATOM   4230  O   GLU B 243      39.732  16.739  56.757  1.00 44.41           O  
-ATOM   4231  CB  GLU B 243      39.858  19.350  56.001  1.00 69.74           C  
-ATOM   4232  CG  GLU B 243      39.804  19.356  57.536  1.00 82.28           C  
-ATOM   4233  CD  GLU B 243      38.461  19.820  58.091  1.00 88.66           C  
-ATOM   4234  OE1 GLU B 243      38.011  20.934  57.737  1.00 91.33           O  
-ATOM   4235  OE2 GLU B 243      37.859  19.065  58.888  1.00 87.48           O  
-ATOM   4236  N   CYS B 244      41.063  15.973  55.105  1.00 49.40           N  
-ATOM   4237  CA  CYS B 244      40.798  14.571  55.382  1.00 50.24           C  
-ATOM   4238  C   CYS B 244      41.218  14.173  56.788  1.00 51.59           C  
-ATOM   4239  O   CYS B 244      40.402  14.213  57.710  1.00 62.97           O  
-ATOM   4240  CB  CYS B 244      41.508  13.699  54.354  1.00 54.94           C  
-ATOM   4241  SG  CYS B 244      43.112  14.334  53.843  1.00 65.72           S  
-ATOM   4242  N   ILE B 245      42.484  13.792  56.945  1.00 42.37           N  
-ATOM   4243  CA  ILE B 245      43.035  13.383  58.241  1.00 38.69           C  
-ATOM   4244  C   ILE B 245      42.056  13.566  59.407  1.00 37.76           C  
-ATOM   4245  O   ILE B 245      41.885  14.671  59.930  1.00 34.48           O  
-ATOM   4246  CB  ILE B 245      44.319  14.176  58.569  1.00 33.36           C  
-ATOM   4247  CG1 ILE B 245      45.303  14.080  57.409  1.00 19.27           C  
-ATOM   4248  CG2 ILE B 245      44.962  13.626  59.841  1.00 38.77           C  
-ATOM   4249  CD1 ILE B 245      45.715  12.661  57.103  1.00 31.05           C  
-ATOM   4250  N   LYS B 246      41.409  12.484  59.817  1.00 37.73           N  
-ATOM   4251  CA  LYS B 246      40.456  12.579  60.908  1.00 40.24           C  
-ATOM   4252  C   LYS B 246      41.005  12.098  62.246  1.00 38.41           C  
-ATOM   4253  O   LYS B 246      41.694  11.079  62.337  1.00 45.94           O  
-ATOM   4254  CB  LYS B 246      39.164  11.835  60.540  1.00 43.13           C  
-ATOM   4255  CG  LYS B 246      38.277  12.629  59.589  1.00 47.01           C  
-ATOM   4256  CD  LYS B 246      37.072  11.836  59.123  1.00 62.91           C  
-ATOM   4257  CE  LYS B 246      36.253  12.647  58.133  1.00 71.62           C  
-ATOM   4258  NZ  LYS B 246      35.194  11.823  57.471  1.00 77.44           N  
-ATOM   4259  N   LEU B 247      40.703  12.872  63.280  1.00 31.33           N  
-ATOM   4260  CA  LEU B 247      41.131  12.581  64.636  1.00 32.41           C  
-ATOM   4261  C   LEU B 247      40.429  11.301  65.088  1.00 36.54           C  
-ATOM   4262  O   LEU B 247      39.198  11.246  65.088  1.00 39.83           O  
-ATOM   4263  CB  LEU B 247      40.738  13.758  65.524  1.00 26.82           C  
-ATOM   4264  CG  LEU B 247      41.439  13.928  66.867  1.00 38.08           C  
-ATOM   4265  CD1 LEU B 247      41.029  15.277  67.448  1.00 31.35           C  
-ATOM   4266  CD2 LEU B 247      41.094  12.763  67.820  1.00 46.35           C  
-ATOM   4267  N   ARG B 248      41.189  10.278  65.476  1.00 36.02           N  
-ATOM   4268  CA  ARG B 248      40.557   9.030  65.883  1.00 44.83           C  
-ATOM   4269  C   ARG B 248      41.051   8.313  67.146  1.00 51.18           C  
-ATOM   4270  O   ARG B 248      42.250   8.256  67.427  1.00 48.07           O  
-ATOM   4271  CB  ARG B 248      40.553   8.060  64.697  1.00 45.73           C  
-ATOM   4272  CG  ARG B 248      41.842   8.022  63.912  1.00 47.93           C  
-ATOM   4273  CD  ARG B 248      41.699   7.098  62.718  1.00 57.34           C  
-ATOM   4274  NE  ARG B 248      40.620   7.521  61.829  1.00 61.68           N  
-ATOM   4275  CZ  ARG B 248      40.187   6.813  60.787  1.00 70.23           C  
-ATOM   4276  NH1 ARG B 248      40.740   5.639  60.499  1.00 73.10           N  
-ATOM   4277  NH2 ARG B 248      39.198   7.274  60.033  1.00 66.40           N  
-ATOM   4278  N   GLU B 249      40.079   7.764  67.882  1.00 57.96           N  
-ATOM   4279  CA  GLU B 249      40.260   7.030  69.138  1.00 58.19           C  
-ATOM   4280  C   GLU B 249      41.576   6.284  69.222  1.00 56.73           C  
-ATOM   4281  O   GLU B 249      42.397   6.572  70.088  1.00 58.69           O  
-ATOM   4282  CB  GLU B 249      39.103   6.045  69.331  1.00 68.62           C  
-ATOM   4283  CG  GLU B 249      37.729   6.705  69.431  1.00 84.08           C  
-ATOM   4284  CD  GLU B 249      37.504   7.411  70.759  1.00 91.47           C  
-ATOM   4285  OE1 GLU B 249      38.277   8.339  71.095  1.00 91.98           O  
-ATOM   4286  OE2 GLU B 249      36.545   7.031  71.467  1.00 97.60           O  
-ATOM   4287  N   VAL B 250      41.762   5.298  68.352  1.00 57.47           N  
-ATOM   4288  CA  VAL B 250      43.016   4.561  68.329  1.00 59.60           C  
-ATOM   4289  C   VAL B 250      43.640   4.788  66.965  1.00 59.61           C  
-ATOM   4290  O   VAL B 250      43.272   4.153  65.973  1.00 60.84           O  
-ATOM   4291  CB  VAL B 250      42.838   3.056  68.573  1.00 55.42           C  
-ATOM   4292  CG1 VAL B 250      44.120   2.311  68.180  1.00 54.08           C  
-ATOM   4293  CG2 VAL B 250      42.543   2.816  70.044  1.00 54.59           C  
-ATOM   4294  N   PRO B 251      44.597   5.721  66.907  1.00 54.51           N  
-ATOM   4295  CA  PRO B 251      45.321   6.102  65.701  1.00 45.28           C  
-ATOM   4296  C   PRO B 251      46.230   5.001  65.187  1.00 42.92           C  
-ATOM   4297  O   PRO B 251      46.754   4.182  65.963  1.00 46.69           O  
-ATOM   4298  CB  PRO B 251      46.102   7.324  66.158  1.00 51.03           C  
-ATOM   4299  CG  PRO B 251      46.450   6.965  67.574  1.00 56.96           C  
-ATOM   4300  CD  PRO B 251      45.137   6.428  68.085  1.00 58.25           C  
-ATOM   4301  N   GLY B 252      46.402   4.988  63.871  1.00 31.85           N  
-ATOM   4302  CA  GLY B 252      47.266   4.011  63.240  1.00 31.99           C  
-ATOM   4303  C   GLY B 252      48.374   4.779  62.556  1.00 31.96           C  
-ATOM   4304  O   GLY B 252      48.212   5.977  62.300  1.00 36.95           O  
-ATOM   4305  N   ILE B 253      49.483   4.111  62.249  1.00 23.89           N  
-ATOM   4306  CA  ILE B 253      50.617   4.777  61.611  1.00 20.59           C  
-ATOM   4307  C   ILE B 253      50.229   5.780  60.521  1.00 23.89           C  
-ATOM   4308  O   ILE B 253      50.798   6.867  60.467  1.00 28.62           O  
-ATOM   4309  CB  ILE B 253      51.618   3.749  61.016  1.00 14.74           C  
-ATOM   4310  CG1 ILE B 253      53.041   4.063  61.478  1.00  7.03           C  
-ATOM   4311  CG2 ILE B 253      51.584   3.784  59.512  1.00 13.69           C  
-ATOM   4312  CD1 ILE B 253      53.486   5.451  61.173  1.00  4.47           C  
-ATOM   4313  N   GLU B 254      49.259   5.436  59.674  1.00 21.54           N  
-ATOM   4314  CA  GLU B 254      48.854   6.331  58.588  1.00 25.00           C  
-ATOM   4315  C   GLU B 254      48.001   7.534  58.988  1.00 28.49           C  
-ATOM   4316  O   GLU B 254      47.641   8.351  58.132  1.00 33.00           O  
-ATOM   4317  CB  GLU B 254      48.121   5.555  57.489  1.00 32.79           C  
-ATOM   4318  CG  GLU B 254      46.933   4.735  57.964  1.00 47.39           C  
-ATOM   4319  CD  GLU B 254      47.335   3.359  58.460  1.00 60.28           C  
-ATOM   4320  OE1 GLU B 254      47.898   2.581  57.658  1.00 67.21           O  
-ATOM   4321  OE2 GLU B 254      47.088   3.052  59.645  1.00 66.08           O  
-ATOM   4322  N   ASP B 255      47.672   7.656  60.271  1.00 23.87           N  
-ATOM   4323  CA  ASP B 255      46.864   8.783  60.714  1.00 24.20           C  
-ATOM   4324  C   ASP B 255      47.743   9.786  61.418  1.00 20.79           C  
-ATOM   4325  O   ASP B 255      47.266  10.825  61.864  1.00 17.30           O  
-ATOM   4326  CB  ASP B 255      45.768   8.321  61.667  1.00 38.90           C  
-ATOM   4327  CG  ASP B 255      44.779   7.371  61.009  1.00 55.23           C  
-ATOM   4328  OD1 ASP B 255      44.138   7.781  60.007  1.00 60.83           O  
-ATOM   4329  OD2 ASP B 255      44.646   6.219  61.501  1.00 49.58           O  
-ATOM   4330  N   THR B 256      49.034   9.471  61.490  1.00 18.30           N  
-ATOM   4331  CA  THR B 256      50.014  10.318  62.161  1.00 18.61           C  
-ATOM   4332  C   THR B 256      50.816  11.236  61.255  1.00 20.76           C  
-ATOM   4333  O   THR B 256      50.447  11.496  60.112  1.00 22.31           O  
-ATOM   4334  CB  THR B 256      51.027   9.474  62.895  1.00 16.24           C  
-ATOM   4335  OG1 THR B 256      51.912   8.877  61.938  1.00 14.70           O  
-ATOM   4336  CG2 THR B 256      50.323   8.385  63.675  1.00 29.65           C  
-ATOM   4337  N   LEU B 257      51.930  11.721  61.802  1.00 25.39           N  
-ATOM   4338  CA  LEU B 257      52.851  12.603  61.093  1.00 21.10           C  
-ATOM   4339  C   LEU B 257      53.903  11.757  60.391  1.00 16.84           C  
-ATOM   4340  O   LEU B 257      54.602  12.218  59.489  1.00 18.73           O  
-ATOM   4341  CB  LEU B 257      53.545  13.548  62.073  1.00 15.10           C  
-ATOM   4342  CG  LEU B 257      52.733  14.711  62.647  1.00 17.12           C  
-ATOM   4343  CD1 LEU B 257      53.620  15.502  63.608  1.00 12.41           C  
-ATOM   4344  CD2 LEU B 257      52.228  15.617  61.512  1.00 10.04           C  
-ATOM   4345  N   PHE B 258      54.015  10.509  60.818  1.00 13.43           N  
-ATOM   4346  CA  PHE B 258      54.979   9.613  60.226  1.00  8.87           C  
-ATOM   4347  C   PHE B 258      54.583   9.342  58.786  1.00  8.97           C  
-ATOM   4348  O   PHE B 258      55.404   8.933  57.956  1.00  4.47           O  
-ATOM   4349  CB  PHE B 258      55.048   8.344  61.060  1.00  4.47           C  
-ATOM   4350  CG  PHE B 258      55.726   8.548  62.380  1.00  8.84           C  
-ATOM   4351  CD1 PHE B 258      57.090   8.852  62.433  1.00 11.15           C  
-ATOM   4352  CD2 PHE B 258      55.010   8.483  63.563  1.00  9.42           C  
-ATOM   4353  CE1 PHE B 258      57.727   9.089  63.642  1.00  5.46           C  
-ATOM   4354  CE2 PHE B 258      55.641   8.721  64.790  1.00 14.68           C  
-ATOM   4355  CZ  PHE B 258      57.000   9.024  64.828  1.00 12.71           C  
-ATOM   4356  N   ALA B 259      53.318   9.612  58.491  1.00 11.49           N  
-ATOM   4357  CA  ALA B 259      52.797   9.425  57.142  1.00 17.82           C  
-ATOM   4358  C   ALA B 259      53.426  10.467  56.237  1.00 17.79           C  
-ATOM   4359  O   ALA B 259      53.545  10.267  55.032  1.00 24.14           O  
-ATOM   4360  CB  ALA B 259      51.274   9.587  57.133  1.00 16.10           C  
-ATOM   4361  N   VAL B 260      53.818  11.583  56.843  1.00 15.37           N  
-ATOM   4362  CA  VAL B 260      54.421  12.697  56.137  1.00 12.24           C  
-ATOM   4363  C   VAL B 260      55.932  12.661  56.265  1.00 15.20           C  
-ATOM   4364  O   VAL B 260      56.624  13.374  55.545  1.00 25.38           O  
-ATOM   4365  CB  VAL B 260      53.888  14.043  56.695  1.00 12.11           C  
-ATOM   4366  CG1 VAL B 260      54.699  15.210  56.170  1.00 15.63           C  
-ATOM   4367  CG2 VAL B 260      52.441  14.215  56.301  1.00 15.95           C  
-ATOM   4368  N   LEU B 261      56.454  11.831  57.164  1.00 10.21           N  
-ATOM   4369  CA  LEU B 261      57.898  11.767  57.331  1.00 11.33           C  
-ATOM   4370  C   LEU B 261      58.579  10.688  56.518  1.00 20.04           C  
-ATOM   4371  O   LEU B 261      59.803  10.707  56.357  1.00 27.05           O  
-ATOM   4372  CB  LEU B 261      58.254  11.639  58.801  1.00  4.47           C  
-ATOM   4373  CG  LEU B 261      58.011  12.998  59.478  1.00  8.98           C  
-ATOM   4374  CD1 LEU B 261      58.198  12.891  60.968  1.00  7.67           C  
-ATOM   4375  CD2 LEU B 261      58.959  14.045  58.902  1.00  7.39           C  
-ATOM   4376  N   LYS B 262      57.790   9.752  56.000  1.00 18.83           N  
-ATOM   4377  CA  LYS B 262      58.332   8.693  55.157  1.00 20.35           C  
-ATOM   4378  C   LYS B 262      58.706   9.366  53.820  1.00 16.43           C  
-ATOM   4379  O   LYS B 262      57.918   9.375  52.880  1.00 24.16           O  
-ATOM   4380  CB  LYS B 262      57.270   7.600  54.946  1.00 25.95           C  
-ATOM   4381  CG  LYS B 262      57.626   6.533  53.911  1.00 28.40           C  
-ATOM   4382  CD  LYS B 262      58.622   5.530  54.455  1.00 29.89           C  
-ATOM   4383  CE  LYS B 262      57.951   4.210  54.833  1.00 35.12           C  
-ATOM   4384  NZ  LYS B 262      57.588   3.331  53.671  1.00 33.60           N  
-ATOM   4385  N   LEU B 263      59.904   9.938  53.744  1.00  6.14           N  
-ATOM   4386  CA  LEU B 263      60.337  10.611  52.537  1.00  4.47           C  
-ATOM   4387  C   LEU B 263      61.540   9.960  51.880  1.00  4.47           C  
-ATOM   4388  O   LEU B 263      62.495   9.630  52.554  1.00 11.46           O  
-ATOM   4389  CB  LEU B 263      60.669  12.055  52.864  1.00  4.47           C  
-ATOM   4390  CG  LEU B 263      59.532  12.843  53.502  1.00  5.50           C  
-ATOM   4391  CD1 LEU B 263      59.990  14.276  53.717  1.00  4.47           C  
-ATOM   4392  CD2 LEU B 263      58.294  12.805  52.609  1.00 13.91           C  
-ATOM   4393  N   PRO B 264      61.513   9.787  50.548  1.00  4.47           N  
-ATOM   4394  CA  PRO B 264      62.616   9.174  49.792  1.00  6.25           C  
-ATOM   4395  C   PRO B 264      63.941   9.892  50.062  1.00  8.60           C  
-ATOM   4396  O   PRO B 264      65.015   9.295  50.032  1.00 12.25           O  
-ATOM   4397  CB  PRO B 264      62.178   9.346  48.342  1.00  5.81           C  
-ATOM   4398  CG  PRO B 264      60.682   9.361  48.433  1.00  5.33           C  
-ATOM   4399  CD  PRO B 264      60.425  10.202  49.645  1.00  4.47           C  
-ATOM   4400  N   GLU B 265      63.845  11.189  50.321  1.00  9.50           N  
-ATOM   4401  CA  GLU B 265      65.009  12.007  50.584  1.00 11.83           C  
-ATOM   4402  C   GLU B 265      65.667  11.636  51.902  1.00 18.73           C  
-ATOM   4403  O   GLU B 265      66.776  12.076  52.181  1.00 33.97           O  
-ATOM   4404  CB  GLU B 265      64.615  13.492  50.607  1.00 10.90           C  
-ATOM   4405  CG  GLU B 265      63.976  14.001  49.317  1.00 25.97           C  
-ATOM   4406  CD  GLU B 265      62.458  13.886  49.299  1.00 32.38           C  
-ATOM   4407  OE1 GLU B 265      61.918  12.865  49.775  1.00 28.26           O  
-ATOM   4408  OE2 GLU B 265      61.805  14.823  48.789  1.00 39.73           O  
-ATOM   4409  N   LEU B 266      64.986  10.838  52.719  1.00 17.51           N  
-ATOM   4410  CA  LEU B 266      65.529  10.443  54.018  1.00 16.32           C  
-ATOM   4411  C   LEU B 266      65.909   8.978  54.028  1.00 21.45           C  
-ATOM   4412  O   LEU B 266      66.527   8.505  54.979  1.00 27.03           O  
-ATOM   4413  CB  LEU B 266      64.515  10.692  55.139  1.00  6.48           C  
-ATOM   4414  CG  LEU B 266      64.069  12.129  55.374  1.00  8.41           C  
-ATOM   4415  CD1 LEU B 266      62.903  12.156  56.335  1.00 12.40           C  
-ATOM   4416  CD2 LEU B 266      65.214  12.925  55.911  1.00  4.47           C  
-ATOM   4417  N   CYS B 267      65.534   8.264  52.969  1.00 22.54           N  
-ATOM   4418  CA  CYS B 267      65.820   6.838  52.860  1.00 21.13           C  
-ATOM   4419  C   CYS B 267      66.921   6.584  51.850  1.00 23.41           C  
-ATOM   4420  O   CYS B 267      67.231   7.444  51.036  1.00 29.44           O  
-ATOM   4421  CB  CYS B 267      64.576   6.074  52.421  1.00 27.71           C  
-ATOM   4422  SG  CYS B 267      63.130   6.249  53.472  1.00 44.98           S  
-ATOM   4423  N   GLY B 268      67.501   5.392  51.900  1.00 25.94           N  
-ATOM   4424  CA  GLY B 268      68.569   5.056  50.986  1.00 30.97           C  
-ATOM   4425  C   GLY B 268      68.097   4.286  49.779  1.00 41.96           C  
-ATOM   4426  O   GLY B 268      66.908   4.228  49.483  1.00 47.78           O  
-ATOM   4427  N   GLU B 269      69.051   3.694  49.077  1.00 48.21           N  
-ATOM   4428  CA  GLU B 269      68.784   2.911  47.882  1.00 51.53           C  
-ATOM   4429  C   GLU B 269      67.654   1.919  48.101  1.00 56.54           C  
-ATOM   4430  O   GLU B 269      66.603   2.006  47.474  1.00 57.50           O  
-ATOM   4431  CB  GLU B 269      70.055   2.161  47.484  1.00 57.52           C  
-ATOM   4432  CG  GLU B 269      69.979   1.384  46.190  1.00 70.06           C  
-ATOM   4433  CD  GLU B 269      71.209   0.524  45.962  1.00 76.32           C  
-ATOM   4434  OE1 GLU B 269      72.337   1.046  46.066  1.00 78.02           O  
-ATOM   4435  OE2 GLU B 269      71.050  -0.678  45.674  1.00 82.52           O  
-ATOM   4436  N   PHE B 270      67.886   0.981  49.011  1.00 64.20           N  
-ATOM   4437  CA  PHE B 270      66.932  -0.074  49.321  1.00 61.54           C  
-ATOM   4438  C   PHE B 270      65.611   0.446  49.861  1.00 53.87           C  
-ATOM   4439  O   PHE B 270      64.641  -0.294  49.946  1.00 57.04           O  
-ATOM   4440  CB  PHE B 270      67.553  -1.046  50.325  1.00 75.19           C  
-ATOM   4441  CG  PHE B 270      68.911  -1.558  49.925  1.00 86.77           C  
-ATOM   4442  CD1 PHE B 270      69.764  -2.112  50.882  1.00 96.63           C  
-ATOM   4443  CD2 PHE B 270      69.349  -1.476  48.604  1.00 86.68           C  
-ATOM   4444  CE1 PHE B 270      71.036  -2.572  50.529  1.00102.13           C  
-ATOM   4445  CE2 PHE B 270      70.614  -1.931  48.239  1.00 92.37           C  
-ATOM   4446  CZ  PHE B 270      71.462  -2.480  49.202  1.00 99.92           C  
-ATOM   4447  N   GLY B 271      65.566   1.715  50.231  1.00 50.23           N  
-ATOM   4448  CA  GLY B 271      64.328   2.259  50.752  1.00 52.48           C  
-ATOM   4449  C   GLY B 271      64.224   2.203  52.265  1.00 56.19           C  
-ATOM   4450  O   GLY B 271      63.119   2.109  52.814  1.00 59.63           O  
-ATOM   4451  N   ASN B 272      65.372   2.246  52.939  1.00 51.84           N  
-ATOM   4452  CA  ASN B 272      65.410   2.224  54.395  1.00 51.18           C  
-ATOM   4453  C   ASN B 272      65.746   3.625  54.852  1.00 46.58           C  
-ATOM   4454  O   ASN B 272      66.528   4.305  54.197  1.00 44.77           O  
-ATOM   4455  CB  ASN B 272      66.487   1.264  54.904  1.00 64.69           C  
-ATOM   4456  CG  ASN B 272      66.015  -0.183  54.953  1.00 79.48           C  
-ATOM   4457  OD1 ASN B 272      64.973  -0.493  55.539  1.00 85.13           O  
-ATOM   4458  ND2 ASN B 272      66.792  -1.080  54.349  1.00 85.25           N  
-ATOM   4459  N   ILE B 273      65.158   4.063  55.962  1.00 39.19           N  
-ATOM   4460  CA  ILE B 273      65.442   5.398  56.469  1.00 25.46           C  
-ATOM   4461  C   ILE B 273      66.882   5.408  56.987  1.00 17.83           C  
-ATOM   4462  O   ILE B 273      67.243   4.603  57.830  1.00 10.98           O  
-ATOM   4463  CB  ILE B 273      64.451   5.783  57.583  1.00 21.31           C  
-ATOM   4464  CG1 ILE B 273      64.839   7.131  58.172  1.00 21.69           C  
-ATOM   4465  CG2 ILE B 273      64.402   4.697  58.637  1.00 19.77           C  
-ATOM   4466  CD1 ILE B 273      63.924   7.593  59.265  1.00 27.51           C  
-ATOM   4467  N   LEU B 274      67.707   6.308  56.454  1.00 20.32           N  
-ATOM   4468  CA  LEU B 274      69.116   6.393  56.841  1.00 12.30           C  
-ATOM   4469  C   LEU B 274      69.341   6.477  58.340  1.00 12.30           C  
-ATOM   4470  O   LEU B 274      68.602   7.152  59.057  1.00 11.58           O  
-ATOM   4471  CB  LEU B 274      69.814   7.574  56.141  1.00 12.63           C  
-ATOM   4472  CG  LEU B 274      70.269   7.338  54.683  1.00 22.45           C  
-ATOM   4473  CD1 LEU B 274      69.085   7.460  53.760  1.00 20.19           C  
-ATOM   4474  CD2 LEU B 274      71.332   8.347  54.252  1.00 29.25           C  
-ATOM   4475  N   PRO B 275      70.386   5.788  58.830  1.00 16.73           N  
-ATOM   4476  CA  PRO B 275      70.799   5.713  60.232  1.00  5.07           C  
-ATOM   4477  C   PRO B 275      70.525   6.952  61.065  1.00 10.85           C  
-ATOM   4478  O   PRO B 275      69.616   6.956  61.902  1.00 10.15           O  
-ATOM   4479  CB  PRO B 275      72.281   5.399  60.127  1.00  4.47           C  
-ATOM   4480  CG  PRO B 275      72.303   4.457  59.001  1.00  7.64           C  
-ATOM   4481  CD  PRO B 275      71.383   5.114  57.977  1.00 20.24           C  
-ATOM   4482  N   LEU B 276      71.302   8.007  60.848  1.00  5.10           N  
-ATOM   4483  CA  LEU B 276      71.105   9.203  61.644  1.00  4.47           C  
-ATOM   4484  C   LEU B 276      69.649   9.598  61.703  1.00  4.47           C  
-ATOM   4485  O   LEU B 276      69.101   9.737  62.784  1.00  9.30           O  
-ATOM   4486  CB  LEU B 276      71.936  10.352  61.107  1.00  4.81           C  
-ATOM   4487  CG  LEU B 276      73.421  10.147  61.339  1.00  4.47           C  
-ATOM   4488  CD1 LEU B 276      74.199  11.320  60.759  1.00 22.75           C  
-ATOM   4489  CD2 LEU B 276      73.666  10.015  62.815  1.00  4.47           C  
-ATOM   4490  N   TRP B 277      69.020   9.756  60.545  1.00  4.47           N  
-ATOM   4491  CA  TRP B 277      67.625  10.147  60.494  1.00  4.47           C  
-ATOM   4492  C   TRP B 277      66.769   9.244  61.386  1.00  4.47           C  
-ATOM   4493  O   TRP B 277      65.754   9.667  61.948  1.00  4.47           O  
-ATOM   4494  CB  TRP B 277      67.136  10.111  59.049  1.00  8.46           C  
-ATOM   4495  CG  TRP B 277      67.884  11.031  58.109  1.00 11.17           C  
-ATOM   4496  CD1 TRP B 277      67.884  10.970  56.740  1.00 13.72           C  
-ATOM   4497  CD2 TRP B 277      68.720  12.148  58.458  1.00  4.47           C  
-ATOM   4498  NE1 TRP B 277      68.665  11.972  56.220  1.00  7.80           N  
-ATOM   4499  CE2 TRP B 277      69.189  12.710  57.249  1.00  8.19           C  
-ATOM   4500  CE3 TRP B 277      69.115  12.731  59.669  1.00  4.47           C  
-ATOM   4501  CZ2 TRP B 277      70.032  13.828  57.218  1.00 14.73           C  
-ATOM   4502  CZ3 TRP B 277      69.952  13.842  59.634  1.00 13.84           C  
-ATOM   4503  CH2 TRP B 277      70.401  14.378  58.416  1.00 10.72           C  
-ATOM   4504  N   ALA B 278      67.181   7.998  61.534  1.00  4.47           N  
-ATOM   4505  CA  ALA B 278      66.428   7.106  62.388  1.00  5.17           C  
-ATOM   4506  C   ALA B 278      66.570   7.641  63.797  1.00 15.65           C  
-ATOM   4507  O   ALA B 278      65.587   8.038  64.424  1.00 18.08           O  
-ATOM   4508  CB  ALA B 278      66.979   5.720  62.314  1.00  4.47           C  
-ATOM   4509  N   TRP B 279      67.804   7.658  64.292  1.00 17.15           N  
-ATOM   4510  CA  TRP B 279      68.065   8.162  65.634  1.00 12.61           C  
-ATOM   4511  C   TRP B 279      67.213   9.403  65.837  1.00 12.49           C  
-ATOM   4512  O   TRP B 279      66.654   9.592  66.906  1.00 21.01           O  
-ATOM   4513  CB  TRP B 279      69.547   8.518  65.809  1.00 14.10           C  
-ATOM   4514  CG  TRP B 279      70.464   7.346  65.731  1.00 14.99           C  
-ATOM   4515  CD1 TRP B 279      70.133   6.078  65.385  1.00 17.39           C  
-ATOM   4516  CD2 TRP B 279      71.880   7.344  65.951  1.00 19.99           C  
-ATOM   4517  NE1 TRP B 279      71.249   5.281  65.369  1.00 21.18           N  
-ATOM   4518  CE2 TRP B 279      72.336   6.036  65.714  1.00 19.68           C  
-ATOM   4519  CE3 TRP B 279      72.806   8.322  66.323  1.00 27.03           C  
-ATOM   4520  CZ2 TRP B 279      73.673   5.680  65.835  1.00 21.01           C  
-ATOM   4521  CZ3 TRP B 279      74.138   7.966  66.442  1.00 13.19           C  
-ATOM   4522  CH2 TRP B 279      74.555   6.659  66.199  1.00 18.43           C  
-ATOM   4523  N   GLY B 280      67.112  10.233  64.800  1.00  4.98           N  
-ATOM   4524  CA  GLY B 280      66.322  11.445  64.889  1.00  6.25           C  
-ATOM   4525  C   GLY B 280      64.870  11.134  65.201  1.00 16.09           C  
-ATOM   4526  O   GLY B 280      64.287  11.689  66.151  1.00 18.30           O  
-ATOM   4527  N   MET B 281      64.272  10.248  64.408  1.00  8.84           N  
-ATOM   4528  CA  MET B 281      62.880   9.880  64.632  1.00  5.51           C  
-ATOM   4529  C   MET B 281      62.707   9.568  66.107  1.00 10.64           C  
-ATOM   4530  O   MET B 281      61.742   9.993  66.738  1.00 12.58           O  
-ATOM   4531  CB  MET B 281      62.514   8.657  63.800  1.00  4.47           C  
-ATOM   4532  CG  MET B 281      62.713   8.844  62.309  1.00  8.49           C  
-ATOM   4533  SD  MET B 281      61.272   9.510  61.459  1.00  5.49           S  
-ATOM   4534  CE  MET B 281      61.255  11.146  62.121  1.00 28.47           C  
-ATOM   4535  N   GLU B 282      63.675   8.841  66.652  1.00 16.55           N  
-ATOM   4536  CA  GLU B 282      63.660   8.446  68.053  1.00 20.00           C  
-ATOM   4537  C   GLU B 282      63.418   9.646  68.970  1.00 18.78           C  
-ATOM   4538  O   GLU B 282      62.446   9.664  69.717  1.00 25.31           O  
-ATOM   4539  CB  GLU B 282      64.987   7.766  68.418  1.00 36.04           C  
-ATOM   4540  CG  GLU B 282      64.867   6.439  69.202  1.00 51.75           C  
-ATOM   4541  CD  GLU B 282      64.307   5.273  68.371  1.00 60.87           C  
-ATOM   4542  OE1 GLU B 282      64.914   4.904  67.334  1.00 62.52           O  
-ATOM   4543  OE2 GLU B 282      63.256   4.720  68.766  1.00 58.73           O  
-ATOM   4544  N   THR B 283      64.291  10.647  68.909  1.00 14.82           N  
-ATOM   4545  CA  THR B 283      64.155  11.829  69.755  1.00 10.66           C  
-ATOM   4546  C   THR B 283      62.855  12.568  69.469  1.00 10.87           C  
-ATOM   4547  O   THR B 283      62.211  13.082  70.395  1.00  4.78           O  
-ATOM   4548  CB  THR B 283      65.322  12.810  69.556  1.00  6.13           C  
-ATOM   4549  OG1 THR B 283      65.291  13.323  68.222  1.00 23.46           O  
-ATOM   4550  CG2 THR B 283      66.643  12.118  69.774  1.00  7.27           C  
-ATOM   4551  N   LEU B 284      62.472  12.628  68.193  1.00  6.26           N  
-ATOM   4552  CA  LEU B 284      61.232  13.304  67.826  1.00 15.61           C  
-ATOM   4553  C   LEU B 284      60.065  12.588  68.495  1.00 19.28           C  
-ATOM   4554  O   LEU B 284      59.097  13.218  68.934  1.00 23.66           O  
-ATOM   4555  CB  LEU B 284      61.033  13.310  66.309  1.00 16.29           C  
-ATOM   4556  CG  LEU B 284      59.655  13.790  65.830  1.00 14.18           C  
-ATOM   4557  CD1 LEU B 284      59.723  14.182  64.374  1.00 13.58           C  
-ATOM   4558  CD2 LEU B 284      58.627  12.689  66.027  1.00 14.07           C  
-ATOM   4559  N   SER B 285      60.145  11.264  68.540  1.00 14.60           N  
-ATOM   4560  CA  SER B 285      59.115  10.475  69.188  1.00 16.11           C  
-ATOM   4561  C   SER B 285      59.180  10.765  70.686  1.00 22.03           C  
-ATOM   4562  O   SER B 285      58.171  11.092  71.306  1.00 23.72           O  
-ATOM   4563  CB  SER B 285      59.369   9.002  68.945  1.00 23.95           C  
-ATOM   4564  OG  SER B 285      59.384   8.740  67.561  1.00 30.96           O  
-ATOM   4565  N   ASN B 286      60.378  10.640  71.256  1.00 25.22           N  
-ATOM   4566  CA  ASN B 286      60.615  10.907  72.675  1.00 26.28           C  
-ATOM   4567  C   ASN B 286      59.891  12.163  73.150  1.00 30.01           C  
-ATOM   4568  O   ASN B 286      59.256  12.162  74.206  1.00 31.47           O  
-ATOM   4569  CB  ASN B 286      62.115  11.068  72.933  1.00 32.70           C  
-ATOM   4570  CG  ASN B 286      62.809   9.746  73.199  1.00 37.36           C  
-ATOM   4571  OD1 ASN B 286      62.244   8.675  72.960  1.00 39.68           O  
-ATOM   4572  ND2 ASN B 286      64.045   9.814  73.695  1.00 38.17           N  
-ATOM   4573  N   CYS B 287      60.003  13.231  72.367  1.00 28.38           N  
-ATOM   4574  CA  CYS B 287      59.359  14.502  72.678  1.00 30.77           C  
-ATOM   4575  C   CYS B 287      57.824  14.413  72.640  1.00 31.57           C  
-ATOM   4576  O   CYS B 287      57.149  14.497  73.672  1.00 38.00           O  
-ATOM   4577  CB  CYS B 287      59.835  15.568  71.691  1.00 28.46           C  
-ATOM   4578  SG  CYS B 287      58.959  17.132  71.820  1.00 41.18           S  
-ATOM   4579  N   LEU B 288      57.284  14.247  71.440  1.00 29.00           N  
-ATOM   4580  CA  LEU B 288      55.845  14.143  71.227  1.00 27.01           C  
-ATOM   4581  C   LEU B 288      55.121  13.188  72.183  1.00 30.65           C  
-ATOM   4582  O   LEU B 288      54.015  13.469  72.636  1.00 41.55           O  
-ATOM   4583  CB  LEU B 288      55.589  13.708  69.785  1.00 14.63           C  
-ATOM   4584  CG  LEU B 288      55.059  14.746  68.806  1.00 11.41           C  
-ATOM   4585  CD1 LEU B 288      55.742  16.082  69.003  1.00 31.35           C  
-ATOM   4586  CD2 LEU B 288      55.264  14.229  67.411  1.00  4.65           C  
-ATOM   4587  N   ARG B 289      55.745  12.061  72.490  1.00 27.11           N  
-ATOM   4588  CA  ARG B 289      55.139  11.070  73.369  1.00 25.27           C  
-ATOM   4589  C   ARG B 289      54.904  11.548  74.796  1.00 24.37           C  
-ATOM   4590  O   ARG B 289      53.971  11.101  75.460  1.00 28.65           O  
-ATOM   4591  CB  ARG B 289      56.004   9.810  73.384  1.00 25.13           C  
-ATOM   4592  CG  ARG B 289      55.489   8.710  74.281  1.00 24.83           C  
-ATOM   4593  CD  ARG B 289      56.038   7.370  73.830  1.00 25.93           C  
-ATOM   4594  NE  ARG B 289      57.483   7.415  73.653  1.00 33.07           N  
-ATOM   4595  CZ  ARG B 289      58.124   6.840  72.643  1.00 36.24           C  
-ATOM   4596  NH1 ARG B 289      57.440   6.180  71.721  1.00 26.32           N  
-ATOM   4597  NH2 ARG B 289      59.448   6.926  72.555  1.00 47.98           N  
-ATOM   4598  N   SER B 290      55.748  12.455  75.269  1.00 19.82           N  
-ATOM   4599  CA  SER B 290      55.618  12.968  76.622  1.00 18.51           C  
-ATOM   4600  C   SER B 290      54.349  13.758  76.781  1.00 19.64           C  
-ATOM   4601  O   SER B 290      53.747  13.775  77.851  1.00 31.49           O  
-ATOM   4602  CB  SER B 290      56.783  13.883  76.951  1.00 15.22           C  
-ATOM   4603  OG  SER B 290      58.002  13.191  76.799  1.00 38.13           O  
-ATOM   4604  N   MET B 291      53.944  14.405  75.699  1.00 14.71           N  
-ATOM   4605  CA  MET B 291      52.767  15.263  75.697  1.00 17.79           C  
-ATOM   4606  C   MET B 291      51.367  14.698  75.958  1.00 17.78           C  
-ATOM   4607  O   MET B 291      51.036  13.570  75.599  1.00 15.03           O  
-ATOM   4608  CB  MET B 291      52.774  16.076  74.408  1.00 22.28           C  
-ATOM   4609  CG  MET B 291      53.918  17.078  74.403  1.00 32.08           C  
-ATOM   4610  SD  MET B 291      54.080  18.045  72.906  1.00 44.26           S  
-ATOM   4611  CE  MET B 291      55.666  17.480  72.328  1.00 38.83           C  
-ATOM   4612  N   SER B 292      50.553  15.519  76.613  1.00 19.36           N  
-ATOM   4613  CA  SER B 292      49.182  15.167  76.949  1.00 21.74           C  
-ATOM   4614  C   SER B 292      48.301  16.031  76.059  1.00 19.34           C  
-ATOM   4615  O   SER B 292      48.083  17.213  76.324  1.00 25.97           O  
-ATOM   4616  CB  SER B 292      48.921  15.471  78.421  1.00 33.64           C  
-ATOM   4617  OG  SER B 292      49.955  14.926  79.226  1.00 42.24           O  
-ATOM   4618  N   PRO B 293      47.785  15.442  74.987  1.00 10.05           N  
-ATOM   4619  CA  PRO B 293      46.926  16.078  73.990  1.00 13.79           C  
-ATOM   4620  C   PRO B 293      45.477  16.382  74.366  1.00 13.36           C  
-ATOM   4621  O   PRO B 293      44.763  15.530  74.895  1.00 19.69           O  
-ATOM   4622  CB  PRO B 293      47.005  15.100  72.824  1.00 26.65           C  
-ATOM   4623  CG  PRO B 293      47.018  13.782  73.538  1.00 23.07           C  
-ATOM   4624  CD  PRO B 293      48.012  14.024  74.662  1.00 11.00           C  
-ATOM   4625  N   PHE B 294      45.048  17.596  74.041  1.00  4.47           N  
-ATOM   4626  CA  PHE B 294      43.692  18.032  74.288  1.00  4.47           C  
-ATOM   4627  C   PHE B 294      43.230  18.904  73.146  1.00 11.60           C  
-ATOM   4628  O   PHE B 294      43.998  19.708  72.625  1.00 14.59           O  
-ATOM   4629  CB  PHE B 294      43.637  18.852  75.542  1.00  4.47           C  
-ATOM   4630  CG  PHE B 294      43.879  18.070  76.786  1.00 20.46           C  
-ATOM   4631  CD1 PHE B 294      44.986  18.344  77.593  1.00 24.50           C  
-ATOM   4632  CD2 PHE B 294      42.984  17.080  77.180  1.00 23.56           C  
-ATOM   4633  CE1 PHE B 294      45.198  17.649  78.774  1.00 21.10           C  
-ATOM   4634  CE2 PHE B 294      43.185  16.372  78.362  1.00 25.29           C  
-ATOM   4635  CZ  PHE B 294      44.296  16.660  79.161  1.00 29.87           C  
-ATOM   4636  N   VAL B 295      41.964  18.760  72.773  1.00 19.61           N  
-ATOM   4637  CA  VAL B 295      41.379  19.551  71.692  1.00 17.48           C  
-ATOM   4638  C   VAL B 295      40.335  20.509  72.242  1.00 24.67           C  
-ATOM   4639  O   VAL B 295      39.428  20.104  72.971  1.00 25.55           O  
-ATOM   4640  CB  VAL B 295      40.717  18.648  70.655  1.00  9.42           C  
-ATOM   4641  CG1 VAL B 295      39.664  19.427  69.874  1.00 12.90           C  
-ATOM   4642  CG2 VAL B 295      41.778  18.089  69.727  1.00 12.22           C  
-ATOM   4643  N   LEU B 296      40.463  21.781  71.880  1.00 32.56           N  
-ATOM   4644  CA  LEU B 296      39.542  22.817  72.342  1.00 36.45           C  
-ATOM   4645  C   LEU B 296      38.929  23.556  71.151  1.00 42.84           C  
-ATOM   4646  O   LEU B 296      39.648  24.119  70.310  1.00 42.23           O  
-ATOM   4647  CB  LEU B 296      40.294  23.798  73.244  1.00 29.91           C  
-ATOM   4648  CG  LEU B 296      39.559  24.947  73.922  1.00 22.24           C  
-ATOM   4649  CD1 LEU B 296      40.561  25.685  74.793  1.00 27.86           C  
-ATOM   4650  CD2 LEU B 296      38.954  25.895  72.900  1.00 21.68           C  
-ATOM   4651  N   SER B 297      37.598  23.560  71.091  1.00 46.72           N  
-ATOM   4652  CA  SER B 297      36.882  24.222  70.002  1.00 50.50           C  
-ATOM   4653  C   SER B 297      36.677  25.710  70.251  1.00 48.51           C  
-ATOM   4654  O   SER B 297      36.143  26.100  71.288  1.00 51.98           O  
-ATOM   4655  CB  SER B 297      35.516  23.564  69.790  1.00 54.05           C  
-ATOM   4656  OG  SER B 297      34.755  24.291  68.838  1.00 54.58           O  
-ATOM   4657  N   LEU B 298      37.097  26.537  69.300  1.00 45.23           N  
-ATOM   4658  CA  LEU B 298      36.931  27.977  69.434  1.00 49.97           C  
-ATOM   4659  C   LEU B 298      35.761  28.443  68.581  1.00 55.20           C  
-ATOM   4660  O   LEU B 298      35.692  29.605  68.182  1.00 58.85           O  
-ATOM   4661  CB  LEU B 298      38.206  28.714  69.010  1.00 46.87           C  
-ATOM   4662  CG  LEU B 298      39.464  28.474  69.844  1.00 36.82           C  
-ATOM   4663  CD1 LEU B 298      40.546  29.432  69.407  1.00 31.19           C  
-ATOM   4664  CD2 LEU B 298      39.153  28.685  71.304  1.00 44.91           C  
-ATOM   4665  N   GLU B 299      34.841  27.524  68.312  1.00 61.50           N  
-ATOM   4666  CA  GLU B 299      33.663  27.816  67.500  1.00 70.12           C  
-ATOM   4667  C   GLU B 299      32.529  28.311  68.391  1.00 69.53           C  
-ATOM   4668  O   GLU B 299      31.505  27.644  68.538  1.00 71.45           O  
-ATOM   4669  CB  GLU B 299      33.226  26.552  66.749  1.00 78.28           C  
-ATOM   4670  CG  GLU B 299      32.093  26.749  65.746  1.00 89.29           C  
-ATOM   4671  CD  GLU B 299      32.545  27.416  64.453  1.00100.56           C  
-ATOM   4672  OE1 GLU B 299      31.703  27.594  63.542  1.00104.83           O  
-ATOM   4673  OE2 GLU B 299      33.741  27.760  64.341  1.00104.71           O  
-ATOM   4674  N   GLN B 300      32.728  29.482  68.988  1.00 71.43           N  
-ATOM   4675  CA  GLN B 300      31.735  30.087  69.870  1.00 74.66           C  
-ATOM   4676  C   GLN B 300      32.303  31.325  70.558  1.00 75.68           C  
-ATOM   4677  O   GLN B 300      33.436  31.731  70.291  1.00 73.84           O  
-ATOM   4678  CB  GLN B 300      31.277  29.077  70.924  1.00 70.65           C  
-ATOM   4679  CG  GLN B 300      32.416  28.425  71.685  1.00 66.74           C  
-ATOM   4680  CD  GLN B 300      31.937  27.342  72.639  1.00 72.25           C  
-ATOM   4681  OE1 GLN B 300      32.737  26.695  73.318  1.00 67.57           O  
-ATOM   4682  NE2 GLN B 300      30.622  27.142  72.698  1.00 73.46           N  
-ATOM   4683  N   THR B 301      31.505  31.925  71.437  1.00 78.81           N  
-ATOM   4684  CA  THR B 301      31.924  33.118  72.171  1.00 77.41           C  
-ATOM   4685  C   THR B 301      33.133  32.800  73.040  1.00 72.80           C  
-ATOM   4686  O   THR B 301      33.192  31.749  73.683  1.00 74.58           O  
-ATOM   4687  CB  THR B 301      30.791  33.654  73.084  1.00 82.03           C  
-ATOM   4688  OG1 THR B 301      30.402  32.636  74.020  1.00 85.93           O  
-ATOM   4689  CG2 THR B 301      29.581  34.075  72.250  1.00 80.40           C  
-ATOM   4690  N   PRO B 302      34.115  33.711  73.073  1.00 67.68           N  
-ATOM   4691  CA  PRO B 302      35.326  33.513  73.872  1.00 70.25           C  
-ATOM   4692  C   PRO B 302      35.002  33.018  75.274  1.00 75.34           C  
-ATOM   4693  O   PRO B 302      35.772  32.266  75.871  1.00 80.18           O  
-ATOM   4694  CB  PRO B 302      35.962  34.896  73.873  1.00 67.40           C  
-ATOM   4695  CG  PRO B 302      35.587  35.422  72.530  1.00 70.18           C  
-ATOM   4696  CD  PRO B 302      34.130  35.029  72.420  1.00 66.88           C  
-ATOM   4697  N   GLN B 303      33.856  33.441  75.796  1.00 77.84           N  
-ATOM   4698  CA  GLN B 303      33.431  33.024  77.126  1.00 80.17           C  
-ATOM   4699  C   GLN B 303      33.380  31.496  77.196  1.00 75.99           C  
-ATOM   4700  O   GLN B 303      33.994  30.877  78.068  1.00 70.59           O  
-ATOM   4701  CB  GLN B 303      32.047  33.608  77.460  1.00 88.55           C  
-ATOM   4702  CG  GLN B 303      32.049  35.032  78.026  1.00 96.12           C  
-ATOM   4703  CD  GLN B 303      32.354  36.099  76.988  1.00103.66           C  
-ATOM   4704  OE1 GLN B 303      31.639  36.237  75.993  1.00108.22           O  
-ATOM   4705  NE2 GLN B 303      33.416  36.868  77.221  1.00104.98           N  
-ATOM   4706  N   HIS B 304      32.648  30.891  76.268  1.00 73.68           N  
-ATOM   4707  CA  HIS B 304      32.530  29.444  76.248  1.00 76.27           C  
-ATOM   4708  C   HIS B 304      33.887  28.776  76.071  1.00 73.11           C  
-ATOM   4709  O   HIS B 304      34.273  27.910  76.863  1.00 73.62           O  
-ATOM   4710  CB  HIS B 304      31.576  29.003  75.134  1.00 79.73           C  
-ATOM   4711  CG  HIS B 304      30.133  29.255  75.441  1.00 89.14           C  
-ATOM   4712  ND1 HIS B 304      29.107  28.668  74.730  1.00 93.89           N  
-ATOM   4713  CD2 HIS B 304      29.542  30.017  76.393  1.00 90.49           C  
-ATOM   4714  CE1 HIS B 304      27.948  29.056  75.233  1.00 96.09           C  
-ATOM   4715  NE2 HIS B 304      28.184  29.874  76.243  1.00 94.91           N  
-ATOM   4716  N   ALA B 305      34.608  29.186  75.032  1.00 67.00           N  
-ATOM   4717  CA  ALA B 305      35.923  28.629  74.743  1.00 58.73           C  
-ATOM   4718  C   ALA B 305      36.727  28.474  76.019  1.00 54.10           C  
-ATOM   4719  O   ALA B 305      37.270  27.410  76.295  1.00 55.58           O  
-ATOM   4720  CB  ALA B 305      36.668  29.529  73.769  1.00 54.95           C  
-ATOM   4721  N   ALA B 306      36.784  29.544  76.803  1.00 51.45           N  
-ATOM   4722  CA  ALA B 306      37.536  29.540  78.049  1.00 49.64           C  
-ATOM   4723  C   ALA B 306      36.891  28.663  79.109  1.00 51.03           C  
-ATOM   4724  O   ALA B 306      37.582  27.959  79.846  1.00 46.38           O  
-ATOM   4725  CB  ALA B 306      37.681  30.960  78.566  1.00 47.21           C  
-ATOM   4726  N   GLN B 307      35.567  28.707  79.194  1.00 56.00           N  
-ATOM   4727  CA  GLN B 307      34.876  27.894  80.183  1.00 64.50           C  
-ATOM   4728  C   GLN B 307      35.178  26.424  79.907  1.00 62.19           C  
-ATOM   4729  O   GLN B 307      35.456  25.648  80.831  1.00 56.50           O  
-ATOM   4730  CB  GLN B 307      33.362  28.141  80.135  1.00 77.04           C  
-ATOM   4731  CG  GLN B 307      32.588  27.392  81.231  1.00 92.81           C  
-ATOM   4732  CD  GLN B 307      31.111  27.762  81.285  1.00101.36           C  
-ATOM   4733  OE1 GLN B 307      30.758  28.924  81.501  1.00104.21           O  
-ATOM   4734  NE2 GLN B 307      30.242  26.771  81.094  1.00102.23           N  
-ATOM   4735  N   GLU B 308      35.125  26.046  78.631  1.00 61.02           N  
-ATOM   4736  CA  GLU B 308      35.403  24.668  78.247  1.00 59.07           C  
-ATOM   4737  C   GLU B 308      36.814  24.314  78.729  1.00 54.31           C  
-ATOM   4738  O   GLU B 308      37.001  23.326  79.445  1.00 53.48           O  
-ATOM   4739  CB  GLU B 308      35.284  24.496  76.725  1.00 59.12           C  
-ATOM   4740  CG  GLU B 308      35.433  23.051  76.242  1.00 69.20           C  
-ATOM   4741  CD  GLU B 308      35.153  22.886  74.748  1.00 84.27           C  
-ATOM   4742  OE1 GLU B 308      35.365  21.772  74.215  1.00 86.84           O  
-ATOM   4743  OE2 GLU B 308      34.716  23.866  74.104  1.00 90.08           O  
-ATOM   4744  N   LEU B 309      37.797  25.136  78.363  1.00 43.44           N  
-ATOM   4745  CA  LEU B 309      39.176  24.900  78.770  1.00 33.41           C  
-ATOM   4746  C   LEU B 309      39.266  24.638  80.267  1.00 39.41           C  
-ATOM   4747  O   LEU B 309      40.099  23.851  80.716  1.00 39.95           O  
-ATOM   4748  CB  LEU B 309      40.052  26.099  78.413  1.00 26.89           C  
-ATOM   4749  CG  LEU B 309      41.489  26.108  78.951  1.00 22.47           C  
-ATOM   4750  CD1 LEU B 309      42.219  24.844  78.540  1.00 23.83           C  
-ATOM   4751  CD2 LEU B 309      42.219  27.332  78.426  1.00 21.65           C  
-ATOM   4752  N   LYS B 310      38.408  25.294  81.043  1.00 42.79           N  
-ATOM   4753  CA  LYS B 310      38.419  25.103  82.491  1.00 44.19           C  
-ATOM   4754  C   LYS B 310      38.033  23.680  82.867  1.00 41.94           C  
-ATOM   4755  O   LYS B 310      38.640  23.067  83.744  1.00 42.67           O  
-ATOM   4756  CB  LYS B 310      37.448  26.065  83.176  1.00 53.05           C  
-ATOM   4757  CG  LYS B 310      37.348  25.837  84.684  1.00 60.22           C  
-ATOM   4758  CD  LYS B 310      36.225  26.641  85.320  1.00 72.52           C  
-ATOM   4759  CE  LYS B 310      36.089  26.296  86.799  1.00 77.56           C  
-ATOM   4760  NZ  LYS B 310      34.980  27.039  87.457  1.00 83.97           N  
-ATOM   4761  N   THR B 311      37.015  23.158  82.199  1.00 36.76           N  
-ATOM   4762  CA  THR B 311      36.546  21.816  82.485  1.00 43.13           C  
-ATOM   4763  C   THR B 311      37.645  20.771  82.275  1.00 44.95           C  
-ATOM   4764  O   THR B 311      37.583  19.668  82.835  1.00 46.84           O  
-ATOM   4765  CB  THR B 311      35.342  21.473  81.595  1.00 47.79           C  
-ATOM   4766  OG1 THR B 311      35.797  20.878  80.372  1.00 53.08           O  
-ATOM   4767  CG2 THR B 311      34.552  22.749  81.271  1.00 36.05           C  
-ATOM   4768  N   LEU B 312      38.649  21.136  81.476  1.00 46.45           N  
-ATOM   4769  CA  LEU B 312      39.781  20.257  81.148  1.00 45.58           C  
-ATOM   4770  C   LEU B 312      40.910  20.256  82.172  1.00 42.42           C  
-ATOM   4771  O   LEU B 312      41.649  19.274  82.276  1.00 37.14           O  
-ATOM   4772  CB  LEU B 312      40.385  20.641  79.791  1.00 38.20           C  
-ATOM   4773  CG  LEU B 312      39.726  20.198  78.488  1.00 39.98           C  
-ATOM   4774  CD1 LEU B 312      38.281  20.651  78.397  1.00 48.28           C  
-ATOM   4775  CD2 LEU B 312      40.527  20.789  77.360  1.00 49.86           C  
-ATOM   4776  N   LEU B 313      41.047  21.360  82.907  1.00 41.92           N  
-ATOM   4777  CA  LEU B 313      42.105  21.511  83.909  1.00 42.76           C  
-ATOM   4778  C   LEU B 313      42.316  20.267  84.758  1.00 46.14           C  
-ATOM   4779  O   LEU B 313      43.454  19.871  85.015  1.00 45.45           O  
-ATOM   4780  CB  LEU B 313      41.811  22.707  84.815  1.00 42.91           C  
-ATOM   4781  CG  LEU B 313      41.605  24.033  84.079  1.00 48.80           C  
-ATOM   4782  CD1 LEU B 313      41.219  25.122  85.068  1.00 54.95           C  
-ATOM   4783  CD2 LEU B 313      42.872  24.408  83.343  1.00 48.76           C  
-ATOM   4784  N   PRO B 314      41.220  19.637  85.218  1.00 52.30           N  
-ATOM   4785  CA  PRO B 314      41.337  18.426  86.043  1.00 52.33           C  
-ATOM   4786  C   PRO B 314      41.861  17.176  85.294  1.00 55.71           C  
-ATOM   4787  O   PRO B 314      42.308  16.217  85.927  1.00 58.18           O  
-ATOM   4788  CB  PRO B 314      39.912  18.240  86.579  1.00 49.20           C  
-ATOM   4789  CG  PRO B 314      39.053  18.805  85.462  1.00 50.59           C  
-ATOM   4790  CD  PRO B 314      39.810  20.073  85.121  1.00 50.54           C  
-ATOM   4791  N   GLN B 315      41.812  17.192  83.959  1.00 53.64           N  
-ATOM   4792  CA  GLN B 315      42.273  16.057  83.153  1.00 45.85           C  
-ATOM   4793  C   GLN B 315      43.753  16.167  82.769  1.00 39.41           C  
-ATOM   4794  O   GLN B 315      44.393  15.178  82.410  1.00 41.33           O  
-ATOM   4795  CB  GLN B 315      41.433  15.941  81.869  1.00 45.18           C  
-ATOM   4796  CG  GLN B 315      39.921  15.902  82.083  1.00 51.47           C  
-ATOM   4797  CD  GLN B 315      39.151  15.594  80.801  1.00 59.48           C  
-ATOM   4798  OE1 GLN B 315      39.230  14.486  80.264  1.00 64.77           O  
-ATOM   4799  NE2 GLN B 315      38.405  16.579  80.305  1.00 58.51           N  
-ATOM   4800  N   MET B 316      44.293  17.375  82.857  1.00 33.72           N  
-ATOM   4801  CA  MET B 316      45.674  17.625  82.481  1.00 29.35           C  
-ATOM   4802  C   MET B 316      46.701  17.083  83.447  1.00 29.95           C  
-ATOM   4803  O   MET B 316      46.436  16.929  84.637  1.00 29.78           O  
-ATOM   4804  CB  MET B 316      45.877  19.123  82.296  1.00 26.10           C  
-ATOM   4805  CG  MET B 316      44.892  19.708  81.294  1.00 28.55           C  
-ATOM   4806  SD  MET B 316      45.077  21.483  81.027  1.00 33.76           S  
-ATOM   4807  CE  MET B 316      43.901  21.730  79.662  1.00 21.82           C  
-ATOM   4808  N   THR B 317      47.881  16.789  82.915  1.00 30.91           N  
-ATOM   4809  CA  THR B 317      48.977  16.270  83.720  1.00 32.66           C  
-ATOM   4810  C   THR B 317      49.729  17.423  84.368  1.00 31.65           C  
-ATOM   4811  O   THR B 317      50.152  18.360  83.684  1.00 37.17           O  
-ATOM   4812  CB  THR B 317      49.958  15.466  82.860  1.00 35.67           C  
-ATOM   4813  OG1 THR B 317      49.279  14.325  82.317  1.00 43.77           O  
-ATOM   4814  CG2 THR B 317      51.163  15.014  83.695  1.00 26.63           C  
-ATOM   4815  N   PRO B 318      49.885  17.381  85.703  1.00 29.65           N  
-ATOM   4816  CA  PRO B 318      50.587  18.420  86.470  1.00 32.57           C  
-ATOM   4817  C   PRO B 318      52.072  18.131  86.698  1.00 37.49           C  
-ATOM   4818  O   PRO B 318      52.498  16.976  86.716  1.00 42.43           O  
-ATOM   4819  CB  PRO B 318      49.824  18.436  87.782  1.00 29.66           C  
-ATOM   4820  CG  PRO B 318      49.561  16.980  87.995  1.00 22.65           C  
-ATOM   4821  CD  PRO B 318      49.106  16.514  86.608  1.00 23.36           C  
-ATOM   4822  N   ALA B 319      52.856  19.186  86.883  1.00 37.60           N  
-ATOM   4823  CA  ALA B 319      54.287  19.037  87.128  1.00 37.63           C  
-ATOM   4824  C   ALA B 319      54.627  19.753  88.418  1.00 40.06           C  
-ATOM   4825  O   ALA B 319      53.859  20.589  88.896  1.00 41.84           O  
-ATOM   4826  CB  ALA B 319      55.093  19.622  85.978  1.00 41.41           C  
-ATOM   4827  N   ASN B 320      55.787  19.438  88.975  1.00 44.00           N  
-ATOM   4828  CA  ASN B 320      56.196  20.055  90.228  1.00 53.14           C  
-ATOM   4829  C   ASN B 320      57.347  21.038  90.060  1.00 53.76           C  
-ATOM   4830  O   ASN B 320      58.282  20.783  89.296  1.00 51.25           O  
-ATOM   4831  CB  ASN B 320      56.604  18.975  91.233  1.00 63.06           C  
-ATOM   4832  CG  ASN B 320      55.558  17.880  91.377  1.00 72.58           C  
-ATOM   4833  OD1 ASN B 320      54.377  18.154  91.604  1.00 77.45           O  
-ATOM   4834  ND2 ASN B 320      55.993  16.626  91.255  1.00 77.32           N  
-ATOM   4835  N   MET B 321      57.271  22.161  90.777  1.00 56.31           N  
-ATOM   4836  CA  MET B 321      58.322  23.174  90.729  1.00 53.99           C  
-ATOM   4837  C   MET B 321      58.442  23.963  92.031  1.00 56.28           C  
-ATOM   4838  O   MET B 321      57.462  24.136  92.773  1.00 50.61           O  
-ATOM   4839  CB  MET B 321      58.105  24.139  89.559  1.00 44.38           C  
-ATOM   4840  CG  MET B 321      57.116  25.251  89.795  1.00 37.32           C  
-ATOM   4841  SD  MET B 321      57.136  26.364  88.373  1.00 53.36           S  
-ATOM   4842  CE  MET B 321      58.660  27.262  88.666  1.00 41.01           C  
-ATOM   4843  N   SER B 322      59.663  24.426  92.296  1.00 60.74           N  
-ATOM   4844  CA  SER B 322      59.971  25.202  93.493  1.00 64.70           C  
-ATOM   4845  C   SER B 322      59.048  26.413  93.604  1.00 67.58           C  
-ATOM   4846  O   SER B 322      58.857  27.150  92.629  1.00 69.26           O  
-ATOM   4847  CB  SER B 322      61.435  25.673  93.454  1.00 61.78           C  
-ATOM   4848  OG  SER B 322      61.740  26.542  94.537  1.00 57.64           O  
-ATOM   4849  N   SER B 323      58.461  26.608  94.784  1.00 65.85           N  
-ATOM   4850  CA  SER B 323      57.590  27.754  94.992  1.00 61.22           C  
-ATOM   4851  C   SER B 323      58.424  28.981  94.625  1.00 62.41           C  
-ATOM   4852  O   SER B 323      57.947  29.886  93.927  1.00 63.88           O  
-ATOM   4853  CB  SER B 323      57.144  27.842  96.453  1.00 56.71           C  
-ATOM   4854  OG  SER B 323      56.319  28.979  96.653  1.00 60.35           O  
-ATOM   4855  N   GLY B 324      59.678  28.989  95.086  1.00 58.95           N  
-ATOM   4856  CA  GLY B 324      60.574  30.094  94.793  1.00 55.50           C  
-ATOM   4857  C   GLY B 324      60.708  30.336  93.295  1.00 53.00           C  
-ATOM   4858  O   GLY B 324      60.549  31.472  92.815  1.00 54.30           O  
-ATOM   4859  N   ALA B 325      60.993  29.267  92.552  1.00 42.26           N  
-ATOM   4860  CA  ALA B 325      61.152  29.358  91.102  1.00 38.85           C  
-ATOM   4861  C   ALA B 325      59.950  30.028  90.414  1.00 34.70           C  
-ATOM   4862  O   ALA B 325      60.115  30.918  89.569  1.00 23.24           O  
-ATOM   4863  CB  ALA B 325      61.390  27.959  90.519  1.00 31.03           C  
-ATOM   4864  N   TRP B 326      58.743  29.602  90.780  1.00 32.64           N  
-ATOM   4865  CA  TRP B 326      57.547  30.174  90.186  1.00 32.62           C  
-ATOM   4866  C   TRP B 326      57.618  31.702  90.255  1.00 32.04           C  
-ATOM   4867  O   TRP B 326      57.331  32.391  89.266  1.00 22.18           O  
-ATOM   4868  CB  TRP B 326      56.291  29.637  90.900  1.00 34.05           C  
-ATOM   4869  CG  TRP B 326      55.027  30.409  90.584  1.00 39.49           C  
-ATOM   4870  CD1 TRP B 326      54.582  31.548  91.207  1.00 40.17           C  
-ATOM   4871  CD2 TRP B 326      54.087  30.137  89.532  1.00 37.70           C  
-ATOM   4872  NE1 TRP B 326      53.430  32.003  90.606  1.00 36.28           N  
-ATOM   4873  CE2 TRP B 326      53.101  31.159  89.577  1.00 37.55           C  
-ATOM   4874  CE3 TRP B 326      53.983  29.136  88.554  1.00 38.33           C  
-ATOM   4875  CZ2 TRP B 326      52.018  31.206  88.679  1.00 35.92           C  
-ATOM   4876  CZ3 TRP B 326      52.902  29.182  87.655  1.00 41.74           C  
-ATOM   4877  CH2 TRP B 326      51.936  30.214  87.729  1.00 39.21           C  
-ATOM   4878  N   ASN B 327      58.024  32.227  91.412  1.00 31.98           N  
-ATOM   4879  CA  ASN B 327      58.129  33.679  91.592  1.00 46.14           C  
-ATOM   4880  C   ASN B 327      59.184  34.250  90.660  1.00 46.65           C  
-ATOM   4881  O   ASN B 327      59.050  35.372  90.143  1.00 47.23           O  
-ATOM   4882  CB  ASN B 327      58.472  34.038  93.046  1.00 50.90           C  
-ATOM   4883  CG  ASN B 327      57.315  33.778  93.998  1.00 60.46           C  
-ATOM   4884  OD1 ASN B 327      56.191  34.259  93.783  1.00 58.44           O  
-ATOM   4885  ND2 ASN B 327      57.580  33.015  95.059  1.00 62.07           N  
-ATOM   4886  N   ILE B 328      60.239  33.470  90.455  1.00 42.70           N  
-ATOM   4887  CA  ILE B 328      61.312  33.869  89.558  1.00 45.37           C  
-ATOM   4888  C   ILE B 328      60.746  33.871  88.136  1.00 42.44           C  
-ATOM   4889  O   ILE B 328      60.673  34.913  87.473  1.00 42.08           O  
-ATOM   4890  CB  ILE B 328      62.490  32.877  89.648  1.00 41.54           C  
-ATOM   4891  CG1 ILE B 328      63.279  33.147  90.935  1.00 42.47           C  
-ATOM   4892  CG2 ILE B 328      63.363  32.975  88.390  1.00 32.36           C  
-ATOM   4893  CD1 ILE B 328      64.362  32.125  91.225  1.00 38.88           C  
-ATOM   4894  N   LEU B 329      60.344  32.690  87.684  1.00 33.61           N  
-ATOM   4895  CA  LEU B 329      59.762  32.530  86.367  1.00 30.38           C  
-ATOM   4896  C   LEU B 329      58.890  33.732  86.033  1.00 33.76           C  
-ATOM   4897  O   LEU B 329      59.061  34.359  84.991  1.00 31.45           O  
-ATOM   4898  CB  LEU B 329      58.912  31.267  86.348  1.00 30.44           C  
-ATOM   4899  CG  LEU B 329      58.066  31.036  85.104  1.00 27.28           C  
-ATOM   4900  CD1 LEU B 329      58.990  30.958  83.898  1.00 33.19           C  
-ATOM   4901  CD2 LEU B 329      57.241  29.744  85.267  1.00 19.64           C  
-ATOM   4902  N   LYS B 330      57.961  34.045  86.936  1.00 41.55           N  
-ATOM   4903  CA  LYS B 330      57.042  35.173  86.765  1.00 46.64           C  
-ATOM   4904  C   LYS B 330      57.765  36.449  86.410  1.00 46.08           C  
-ATOM   4905  O   LYS B 330      57.364  37.159  85.484  1.00 43.63           O  
-ATOM   4906  CB  LYS B 330      56.244  35.428  88.043  1.00 52.29           C  
-ATOM   4907  CG  LYS B 330      55.204  34.367  88.364  1.00 68.73           C  
-ATOM   4908  CD  LYS B 330      54.182  34.876  89.384  1.00 74.16           C  
-ATOM   4909  CE  LYS B 330      53.491  36.168  88.898  1.00 85.76           C  
-ATOM   4910  NZ  LYS B 330      52.832  36.047  87.546  1.00 86.94           N  
-ATOM   4911  N   GLU B 331      58.822  36.739  87.168  1.00 48.57           N  
-ATOM   4912  CA  GLU B 331      59.625  37.942  86.954  1.00 55.78           C  
-ATOM   4913  C   GLU B 331      60.249  37.940  85.558  1.00 47.74           C  
-ATOM   4914  O   GLU B 331      60.201  38.939  84.831  1.00 48.26           O  
-ATOM   4915  CB  GLU B 331      60.737  38.048  88.009  1.00 59.38           C  
-ATOM   4916  CG  GLU B 331      61.515  39.371  87.951  1.00 73.95           C  
-ATOM   4917  CD  GLU B 331      63.017  39.183  88.119  1.00 83.79           C  
-ATOM   4918  OE1 GLU B 331      63.433  38.592  89.140  1.00 88.84           O  
-ATOM   4919  OE2 GLU B 331      63.781  39.627  87.230  1.00 83.19           O  
-ATOM   4920  N   LEU B 332      60.839  36.812  85.191  1.00 35.27           N  
-ATOM   4921  CA  LEU B 332      61.464  36.689  83.889  1.00 32.34           C  
-ATOM   4922  C   LEU B 332      60.421  36.885  82.813  1.00 30.82           C  
-ATOM   4923  O   LEU B 332      60.606  37.675  81.891  1.00 30.13           O  
-ATOM   4924  CB  LEU B 332      62.096  35.313  83.750  1.00 34.74           C  
-ATOM   4925  CG  LEU B 332      63.012  34.995  84.933  1.00 50.42           C  
-ATOM   4926  CD1 LEU B 332      63.601  33.583  84.754  1.00 40.12           C  
-ATOM   4927  CD2 LEU B 332      64.109  36.095  85.058  1.00 44.22           C  
-ATOM   4928  N   VAL B 333      59.315  36.166  82.938  1.00 30.92           N  
-ATOM   4929  CA  VAL B 333      58.246  36.274  81.960  1.00 35.52           C  
-ATOM   4930  C   VAL B 333      57.798  37.713  81.826  1.00 33.92           C  
-ATOM   4931  O   VAL B 333      57.529  38.200  80.727  1.00 29.29           O  
-ATOM   4932  CB  VAL B 333      57.029  35.456  82.368  1.00 42.17           C  
-ATOM   4933  CG1 VAL B 333      55.955  35.565  81.273  1.00 40.02           C  
-ATOM   4934  CG2 VAL B 333      57.437  34.006  82.623  1.00 46.23           C  
-ATOM   4935  N   ASN B 334      57.703  38.389  82.960  1.00 37.37           N  
-ATOM   4936  CA  ASN B 334      57.286  39.776  82.950  1.00 50.61           C  
-ATOM   4937  C   ASN B 334      58.406  40.653  82.384  1.00 52.84           C  
-ATOM   4938  O   ASN B 334      58.151  41.685  81.755  1.00 53.47           O  
-ATOM   4939  CB  ASN B 334      56.927  40.232  84.367  1.00 57.86           C  
-ATOM   4940  CG  ASN B 334      56.385  41.647  84.397  1.00 71.74           C  
-ATOM   4941  OD1 ASN B 334      55.289  41.912  83.894  1.00 74.47           O  
-ATOM   4942  ND2 ASN B 334      57.156  42.570  84.973  1.00 76.44           N  
-ATOM   4943  N   ALA B 335      59.647  40.228  82.605  1.00 54.24           N  
-ATOM   4944  CA  ALA B 335      60.809  40.975  82.139  1.00 52.35           C  
-ATOM   4945  C   ALA B 335      60.929  41.011  80.623  1.00 50.88           C  
-ATOM   4946  O   ALA B 335      61.466  41.965  80.073  1.00 54.14           O  
-ATOM   4947  CB  ALA B 335      62.095  40.399  82.753  1.00 44.29           C  
-ATOM   4948  N   VAL B 336      60.429  39.980  79.946  1.00 53.23           N  
-ATOM   4949  CA  VAL B 336      60.521  39.897  78.487  1.00 55.88           C  
-ATOM   4950  C   VAL B 336      59.200  40.151  77.785  1.00 60.03           C  
-ATOM   4951  O   VAL B 336      59.191  40.453  76.588  1.00 56.51           O  
-ATOM   4952  CB  VAL B 336      61.035  38.525  78.031  1.00 54.08           C  
-ATOM   4953  CG1 VAL B 336      62.277  38.142  78.812  1.00 58.96           C  
-ATOM   4954  CG2 VAL B 336      59.941  37.476  78.211  1.00 48.93           C  
-ATOM   4955  N   GLN B 337      58.093  39.980  78.502  1.00 69.40           N  
-ATOM   4956  CA  GLN B 337      56.795  40.217  77.915  1.00 80.89           C  
-ATOM   4957  C   GLN B 337      56.366  41.670  78.046  1.00 85.39           C  
-ATOM   4958  O   GLN B 337      55.178  41.980  77.924  1.00 84.59           O  
-ATOM   4959  CB  GLN B 337      55.726  39.303  78.544  1.00 83.44           C  
-ATOM   4960  CG  GLN B 337      55.776  37.844  78.055  1.00 91.12           C  
-ATOM   4961  CD  GLN B 337      55.726  37.690  76.517  1.00 90.32           C  
-ATOM   4962  OE1 GLN B 337      54.764  38.100  75.861  1.00 93.45           O  
-ATOM   4963  NE2 GLN B 337      56.778  37.096  75.948  1.00 80.01           N  
-ATOM   4964  N   ASP B 338      57.353  42.539  78.265  1.00 92.71           N  
-ATOM   4965  CA  ASP B 338      57.109  43.976  78.331  1.00 99.58           C  
-ATOM   4966  C   ASP B 338      57.328  44.554  76.916  1.00101.45           C  
-ATOM   4967  O   ASP B 338      56.305  44.779  76.217  1.00 99.54           O  
-ATOM   4968  CB  ASP B 338      58.064  44.678  79.292  1.00101.68           C  
-ATOM   4969  CG  ASP B 338      57.819  46.176  79.362  1.00102.17           C  
-ATOM   4970  OD1 ASP B 338      56.901  46.624  80.084  1.00 99.02           O  
-ATOM   4971  OD2 ASP B 338      58.549  46.907  78.658  1.00100.23           O  
-TER    4972      ASP B 338                                                      
-ATOM   4973  N   LYS C   9      67.088  19.656 -11.300  1.00 91.39           N  
-ATOM   4974  CA  LYS C   9      66.628  20.570 -10.214  1.00 86.27           C  
-ATOM   4975  C   LYS C   9      65.111  20.492 -10.037  1.00 82.65           C  
-ATOM   4976  O   LYS C   9      64.374  21.409 -10.418  1.00 78.73           O  
-ATOM   4977  CB  LYS C   9      67.055  22.011 -10.524  1.00 87.52           C  
-ATOM   4978  CG  LYS C   9      66.499  23.066  -9.577  1.00 85.66           C  
-ATOM   4979  CD  LYS C   9      66.957  24.452  -9.986  1.00 89.13           C  
-ATOM   4980  CE  LYS C   9      66.116  25.542  -9.339  1.00 91.12           C  
-ATOM   4981  NZ  LYS C   9      66.532  26.900  -9.798  1.00 87.49           N  
-ATOM   4982  N   MET C  10      64.661  19.382  -9.453  1.00 79.48           N  
-ATOM   4983  CA  MET C  10      63.240  19.135  -9.197  1.00 74.00           C  
-ATOM   4984  C   MET C  10      62.835  19.635  -7.808  1.00 65.89           C  
-ATOM   4985  O   MET C  10      63.624  19.567  -6.857  1.00 57.62           O  
-ATOM   4986  CB  MET C  10      62.922  17.630  -9.306  1.00 74.59           C  
-ATOM   4987  CG  MET C  10      63.809  16.723  -8.441  1.00 70.85           C  
-ATOM   4988  SD  MET C  10      63.099  15.084  -8.129  1.00 76.71           S  
-ATOM   4989  CE  MET C  10      63.390  14.264  -9.670  1.00 73.49           C  
-ATOM   4990  N   GLY C  11      61.600  20.123  -7.697  1.00 57.46           N  
-ATOM   4991  CA  GLY C  11      61.120  20.619  -6.421  1.00 50.52           C  
-ATOM   4992  C   GLY C  11      60.362  19.600  -5.585  1.00 51.21           C  
-ATOM   4993  O   GLY C  11      59.394  19.000  -6.058  1.00 54.00           O  
-ATOM   4994  N   VAL C  12      60.807  19.408  -4.339  1.00 46.87           N  
-ATOM   4995  CA  VAL C  12      60.176  18.478  -3.402  1.00 37.91           C  
-ATOM   4996  C   VAL C  12      59.286  19.217  -2.393  1.00 32.25           C  
-ATOM   4997  O   VAL C  12      59.260  20.454  -2.342  1.00 30.25           O  
-ATOM   4998  CB  VAL C  12      61.231  17.683  -2.617  1.00 35.33           C  
-ATOM   4999  CG1 VAL C  12      62.120  16.927  -3.568  1.00 37.70           C  
-ATOM   5000  CG2 VAL C  12      62.061  18.623  -1.776  1.00 38.24           C  
-ATOM   5001  N   LEU C  13      58.564  18.457  -1.580  1.00 23.49           N  
-ATOM   5002  CA  LEU C  13      57.679  19.057  -0.597  1.00 26.42           C  
-ATOM   5003  C   LEU C  13      57.893  18.427   0.783  1.00 33.20           C  
-ATOM   5004  O   LEU C  13      57.316  17.377   1.097  1.00 31.74           O  
-ATOM   5005  CB  LEU C  13      56.235  18.873  -1.052  1.00 16.56           C  
-ATOM   5006  CG  LEU C  13      55.318  20.074  -0.870  1.00 21.14           C  
-ATOM   5007  CD1 LEU C  13      55.958  21.312  -1.498  1.00 15.46           C  
-ATOM   5008  CD2 LEU C  13      53.962  19.761  -1.510  1.00 17.98           C  
-ATOM   5009  N   ARG C  14      58.731  19.063   1.604  1.00 33.81           N  
-ATOM   5010  CA  ARG C  14      59.011  18.536   2.934  1.00 28.99           C  
-ATOM   5011  C   ARG C  14      57.850  18.804   3.879  1.00 28.00           C  
-ATOM   5012  O   ARG C  14      57.516  19.954   4.169  1.00 36.85           O  
-ATOM   5013  CB  ARG C  14      60.315  19.125   3.494  1.00 26.31           C  
-ATOM   5014  CG  ARG C  14      61.566  18.535   2.859  1.00 22.45           C  
-ATOM   5015  CD  ARG C  14      62.817  18.699   3.716  1.00 30.07           C  
-ATOM   5016  NE  ARG C  14      63.364  20.053   3.662  1.00 40.59           N  
-ATOM   5017  CZ  ARG C  14      63.036  21.035   4.499  1.00 45.05           C  
-ATOM   5018  NH1 ARG C  14      62.158  20.823   5.474  1.00 43.70           N  
-ATOM   5019  NH2 ARG C  14      63.582  22.238   4.357  1.00 45.77           N  
-ATOM   5020  N   ILE C  15      57.230  17.727   4.347  1.00 21.22           N  
-ATOM   5021  CA  ILE C  15      56.101  17.842   5.249  1.00 17.49           C  
-ATOM   5022  C   ILE C  15      56.289  17.003   6.497  1.00 25.15           C  
-ATOM   5023  O   ILE C  15      56.342  15.764   6.435  1.00 27.85           O  
-ATOM   5024  CB  ILE C  15      54.802  17.390   4.581  1.00 18.31           C  
-ATOM   5025  CG1 ILE C  15      54.603  18.141   3.256  1.00 16.29           C  
-ATOM   5026  CG2 ILE C  15      53.635  17.632   5.536  1.00 13.10           C  
-ATOM   5027  CD1 ILE C  15      53.370  17.712   2.496  1.00  6.67           C  
-ATOM   5028  N   TYR C  16      56.385  17.696   7.627  1.00 25.23           N  
-ATOM   5029  CA  TYR C  16      56.543  17.065   8.926  1.00 17.76           C  
-ATOM   5030  C   TYR C  16      55.190  17.101   9.651  1.00 17.18           C  
-ATOM   5031  O   TYR C  16      54.570  18.159   9.829  1.00 14.14           O  
-ATOM   5032  CB  TYR C  16      57.620  17.808   9.701  1.00 16.47           C  
-ATOM   5033  CG  TYR C  16      58.981  17.690   9.064  1.00 10.52           C  
-ATOM   5034  CD1 TYR C  16      59.737  16.537   9.220  1.00 13.47           C  
-ATOM   5035  CD2 TYR C  16      59.524  18.737   8.322  1.00  9.09           C  
-ATOM   5036  CE1 TYR C  16      61.011  16.424   8.663  1.00 20.67           C  
-ATOM   5037  CE2 TYR C  16      60.800  18.636   7.756  1.00 12.25           C  
-ATOM   5038  CZ  TYR C  16      61.541  17.477   7.933  1.00 18.58           C  
-ATOM   5039  OH  TYR C  16      62.815  17.370   7.401  1.00 21.69           O  
-ATOM   5040  N   LEU C  17      54.740  15.926  10.061  1.00 17.58           N  
-ATOM   5041  CA  LEU C  17      53.452  15.774  10.714  1.00 21.93           C  
-ATOM   5042  C   LEU C  17      53.624  15.550  12.206  1.00 19.90           C  
-ATOM   5043  O   LEU C  17      54.109  14.501  12.630  1.00 16.98           O  
-ATOM   5044  CB  LEU C  17      52.740  14.582  10.079  1.00 26.92           C  
-ATOM   5045  CG  LEU C  17      51.230  14.432  10.152  1.00 29.02           C  
-ATOM   5046  CD1 LEU C  17      50.551  15.694   9.649  1.00 38.61           C  
-ATOM   5047  CD2 LEU C  17      50.836  13.233   9.292  1.00 28.13           C  
-ATOM   5048  N   ASP C  18      53.216  16.534  13.000  1.00 23.22           N  
-ATOM   5049  CA  ASP C  18      53.343  16.438  14.452  1.00 31.36           C  
-ATOM   5050  C   ASP C  18      52.034  16.570  15.221  1.00 34.11           C  
-ATOM   5051  O   ASP C  18      50.951  16.407  14.659  1.00 37.13           O  
-ATOM   5052  CB  ASP C  18      54.322  17.492  14.981  1.00 35.26           C  
-ATOM   5053  CG  ASP C  18      55.565  16.875  15.597  1.00 40.34           C  
-ATOM   5054  OD1 ASP C  18      56.633  16.914  14.943  1.00 32.28           O  
-ATOM   5055  OD2 ASP C  18      55.465  16.341  16.728  1.00 41.89           O  
-ATOM   5056  N   GLY C  19      52.162  16.878  16.514  1.00 35.92           N  
-ATOM   5057  CA  GLY C  19      51.012  17.027  17.393  1.00 36.31           C  
-ATOM   5058  C   GLY C  19      51.166  16.113  18.600  1.00 39.59           C  
-ATOM   5059  O   GLY C  19      52.257  15.588  18.843  1.00 40.56           O  
-ATOM   5060  N   ALA C  20      50.084  15.913  19.351  1.00 36.89           N  
-ATOM   5061  CA  ALA C  20      50.105  15.052  20.534  1.00 33.03           C  
-ATOM   5062  C   ALA C  20      50.310  13.581  20.172  1.00 38.88           C  
-ATOM   5063  O   ALA C  20      50.402  13.233  19.000  1.00 42.80           O  
-ATOM   5064  CB  ALA C  20      48.815  15.220  21.299  1.00 30.22           C  
-ATOM   5065  N   TYR C  21      50.375  12.713  21.177  1.00 48.24           N  
-ATOM   5066  CA  TYR C  21      50.571  11.287  20.920  1.00 60.53           C  
-ATOM   5067  C   TYR C  21      49.293  10.472  21.097  1.00 66.23           C  
-ATOM   5068  O   TYR C  21      48.374  10.889  21.798  1.00 71.58           O  
-ATOM   5069  CB  TYR C  21      51.687  10.730  21.821  1.00 65.23           C  
-ATOM   5070  CG  TYR C  21      51.352  10.580  23.298  1.00 68.43           C  
-ATOM   5071  CD1 TYR C  21      50.573   9.515  23.760  1.00 70.19           C  
-ATOM   5072  CD2 TYR C  21      51.839  11.487  24.237  1.00 71.92           C  
-ATOM   5073  CE1 TYR C  21      50.293   9.357  25.122  1.00 67.80           C  
-ATOM   5074  CE2 TYR C  21      51.562  11.338  25.598  1.00 72.83           C  
-ATOM   5075  CZ  TYR C  21      50.791  10.272  26.031  1.00 68.53           C  
-ATOM   5076  OH  TYR C  21      50.519  10.126  27.370  1.00 68.69           O  
-ATOM   5077  N   GLY C  22      49.239   9.309  20.454  1.00 69.01           N  
-ATOM   5078  CA  GLY C  22      48.065   8.460  20.554  1.00 68.84           C  
-ATOM   5079  C   GLY C  22      46.896   8.994  19.749  1.00 69.07           C  
-ATOM   5080  O   GLY C  22      45.919   8.284  19.519  1.00 67.93           O  
-ATOM   5081  N   ILE C  23      47.001  10.247  19.313  1.00 72.05           N  
-ATOM   5082  CA  ILE C  23      45.952  10.891  18.522  1.00 73.73           C  
-ATOM   5083  C   ILE C  23      45.622  10.154  17.215  1.00 75.99           C  
-ATOM   5084  O   ILE C  23      44.491  10.216  16.732  1.00 80.45           O  
-ATOM   5085  CB  ILE C  23      46.317  12.370  18.172  1.00 68.75           C  
-ATOM   5086  CG1 ILE C  23      47.748  12.453  17.637  1.00 66.45           C  
-ATOM   5087  CG2 ILE C  23      46.140  13.256  19.389  1.00 67.04           C  
-ATOM   5088  CD1 ILE C  23      48.123  13.824  17.106  1.00 64.51           C  
-ATOM   5089  N   GLY C  24      46.604   9.467  16.639  1.00 71.07           N  
-ATOM   5090  CA  GLY C  24      46.360   8.745  15.404  1.00 61.72           C  
-ATOM   5091  C   GLY C  24      47.001   9.376  14.185  1.00 57.00           C  
-ATOM   5092  O   GLY C  24      46.571   9.137  13.057  1.00 59.77           O  
-ATOM   5093  N   LYS C  25      48.039  10.175  14.405  1.00 54.65           N  
-ATOM   5094  CA  LYS C  25      48.724  10.838  13.306  1.00 53.87           C  
-ATOM   5095  C   LYS C  25      49.579   9.904  12.474  1.00 49.38           C  
-ATOM   5096  O   LYS C  25      50.236  10.338  11.540  1.00 50.65           O  
-ATOM   5097  CB  LYS C  25      49.587  12.006  13.818  1.00 58.22           C  
-ATOM   5098  CG  LYS C  25      50.195  11.817  15.203  1.00 57.45           C  
-ATOM   5099  CD  LYS C  25      51.326  12.809  15.448  1.00 48.76           C  
-ATOM   5100  CE  LYS C  25      52.530  12.453  14.591  1.00 46.67           C  
-ATOM   5101  NZ  LYS C  25      52.918  11.024  14.804  1.00 41.61           N  
-ATOM   5102  N   THR C  26      49.573   8.620  12.803  1.00 53.84           N  
-ATOM   5103  CA  THR C  26      50.362   7.663  12.041  1.00 62.72           C  
-ATOM   5104  C   THR C  26      49.451   6.822  11.147  1.00 65.65           C  
-ATOM   5105  O   THR C  26      49.736   6.641   9.965  1.00 70.85           O  
-ATOM   5106  CB  THR C  26      51.213   6.741  12.971  1.00 65.19           C  
-ATOM   5107  OG1 THR C  26      52.236   7.512  13.615  1.00 64.28           O  
-ATOM   5108  CG2 THR C  26      51.884   5.642  12.171  1.00 67.65           C  
-ATOM   5109  N   THR C  27      48.347   6.324  11.695  1.00 67.63           N  
-ATOM   5110  CA  THR C  27      47.440   5.515  10.893  1.00 71.28           C  
-ATOM   5111  C   THR C  27      46.716   6.434   9.915  1.00 70.31           C  
-ATOM   5112  O   THR C  27      46.055   5.974   8.986  1.00 72.02           O  
-ATOM   5113  CB  THR C  27      46.400   4.774  11.765  1.00 73.26           C  
-ATOM   5114  OG1 THR C  27      46.948   4.524  13.061  1.00 76.17           O  
-ATOM   5115  CG2 THR C  27      46.047   3.424  11.135  1.00 70.12           C  
-ATOM   5116  N   ALA C  28      46.851   7.737  10.132  1.00 65.93           N  
-ATOM   5117  CA  ALA C  28      46.222   8.723   9.269  1.00 64.33           C  
-ATOM   5118  C   ALA C  28      47.263   9.301   8.321  1.00 64.68           C  
-ATOM   5119  O   ALA C  28      46.929   9.969   7.348  1.00 65.88           O  
-ATOM   5120  CB  ALA C  28      45.600   9.822  10.099  1.00 65.54           C  
-ATOM   5121  N   ALA C  29      48.532   9.044   8.613  1.00 66.10           N  
-ATOM   5122  CA  ALA C  29      49.619   9.526   7.768  1.00 65.41           C  
-ATOM   5123  C   ALA C  29      49.948   8.433   6.780  1.00 66.07           C  
-ATOM   5124  O   ALA C  29      50.578   8.677   5.760  1.00 69.30           O  
-ATOM   5125  CB  ALA C  29      50.837   9.845   8.596  1.00 61.11           C  
-ATOM   5126  N   GLU C  30      49.527   7.218   7.102  1.00 68.68           N  
-ATOM   5127  CA  GLU C  30      49.760   6.085   6.228  1.00 73.13           C  
-ATOM   5128  C   GLU C  30      48.623   6.016   5.216  1.00 71.69           C  
-ATOM   5129  O   GLU C  30      48.855   5.825   4.023  1.00 72.78           O  
-ATOM   5130  CB  GLU C  30      49.831   4.782   7.038  1.00 80.88           C  
-ATOM   5131  CG  GLU C  30      51.087   4.631   7.905  1.00 87.58           C  
-ATOM   5132  CD  GLU C  30      51.172   3.274   8.601  1.00 95.72           C  
-ATOM   5133  OE1 GLU C  30      51.176   2.237   7.901  1.00100.38           O  
-ATOM   5134  OE2 GLU C  30      51.239   3.243   9.850  1.00 97.89           O  
-ATOM   5135  N   GLU C  31      47.394   6.193   5.692  1.00 69.32           N  
-ATOM   5136  CA  GLU C  31      46.231   6.141   4.813  1.00 70.67           C  
-ATOM   5137  C   GLU C  31      46.345   7.219   3.754  1.00 66.95           C  
-ATOM   5138  O   GLU C  31      45.549   7.270   2.822  1.00 68.86           O  
-ATOM   5139  CB  GLU C  31      44.933   6.340   5.603  1.00 78.31           C  
-ATOM   5140  CG  GLU C  31      43.794   5.375   5.229  1.00 88.50           C  
-ATOM   5141  CD  GLU C  31      43.406   5.430   3.760  1.00 95.78           C  
-ATOM   5142  OE1 GLU C  31      43.080   6.536   3.274  1.00 98.98           O  
-ATOM   5143  OE2 GLU C  31      43.421   4.364   3.095  1.00 97.39           O  
-ATOM   5144  N   PHE C  32      47.336   8.086   3.905  1.00 64.43           N  
-ATOM   5145  CA  PHE C  32      47.552   9.152   2.942  1.00 67.15           C  
-ATOM   5146  C   PHE C  32      48.569   8.690   1.911  1.00 70.96           C  
-ATOM   5147  O   PHE C  32      48.638   9.214   0.803  1.00 74.58           O  
-ATOM   5148  CB  PHE C  32      48.084  10.395   3.638  1.00 65.88           C  
-ATOM   5149  CG  PHE C  32      48.368  11.536   2.703  1.00 62.23           C  
-ATOM   5150  CD1 PHE C  32      47.326  12.234   2.097  1.00 56.02           C  
-ATOM   5151  CD2 PHE C  32      49.680  11.925   2.440  1.00 54.64           C  
-ATOM   5152  CE1 PHE C  32      47.590  13.304   1.248  1.00 47.12           C  
-ATOM   5153  CE2 PHE C  32      49.953  12.994   1.591  1.00 39.49           C  
-ATOM   5154  CZ  PHE C  32      48.908  13.683   0.997  1.00 40.56           C  
-ATOM   5155  N   LEU C  33      49.358   7.697   2.292  1.00 72.81           N  
-ATOM   5156  CA  LEU C  33      50.384   7.154   1.422  1.00 74.79           C  
-ATOM   5157  C   LEU C  33      49.838   6.072   0.502  1.00 82.48           C  
-ATOM   5158  O   LEU C  33      50.022   6.118  -0.718  1.00 85.10           O  
-ATOM   5159  CB  LEU C  33      51.501   6.571   2.277  1.00 65.98           C  
-ATOM   5160  CG  LEU C  33      52.682   5.921   1.568  1.00 59.70           C  
-ATOM   5161  CD1 LEU C  33      53.333   6.911   0.635  1.00 56.40           C  
-ATOM   5162  CD2 LEU C  33      53.671   5.437   2.604  1.00 55.40           C  
-ATOM   5163  N   HIS C  34      49.201   5.077   1.115  1.00 87.28           N  
-ATOM   5164  CA  HIS C  34      48.631   3.950   0.382  1.00 94.89           C  
-ATOM   5165  C   HIS C  34      47.476   4.411  -0.501  1.00 94.29           C  
-ATOM   5166  O   HIS C  34      46.943   3.631  -1.290  1.00 92.58           O  
-ATOM   5167  CB  HIS C  34      48.106   2.869   1.352  1.00 96.94           C  
-ATOM   5168  CG  HIS C  34      49.126   2.356   2.329  1.00 94.45           C  
-ATOM   5169  ND1 HIS C  34      50.457   2.189   2.009  1.00 91.62           N  
-ATOM   5170  CD2 HIS C  34      48.991   1.919   3.604  1.00 93.07           C  
-ATOM   5171  CE1 HIS C  34      51.097   1.673   3.044  1.00 88.84           C  
-ATOM   5172  NE2 HIS C  34      50.230   1.499   4.025  1.00 89.99           N  
-ATOM   5173  N   HIS C  35      47.108   5.683  -0.369  1.00 94.08           N  
-ATOM   5174  CA  HIS C  35      45.988   6.250  -1.114  1.00 95.05           C  
-ATOM   5175  C   HIS C  35      46.373   7.287  -2.173  1.00 92.90           C  
-ATOM   5176  O   HIS C  35      45.541   7.644  -3.002  1.00 98.57           O  
-ATOM   5177  CB  HIS C  35      44.996   6.884  -0.124  1.00101.11           C  
-ATOM   5178  CG  HIS C  35      43.627   7.126  -0.685  1.00104.54           C  
-ATOM   5179  ND1 HIS C  35      42.744   8.024  -0.122  1.00105.03           N  
-ATOM   5180  CD2 HIS C  35      42.972   6.557  -1.724  1.00107.44           C  
-ATOM   5181  CE1 HIS C  35      41.605   7.997  -0.790  1.00108.65           C  
-ATOM   5182  NE2 HIS C  35      41.717   7.114  -1.766  1.00111.09           N  
-ATOM   5183  N   PHE C  36      47.611   7.774  -2.162  1.00 86.27           N  
-ATOM   5184  CA  PHE C  36      48.009   8.780  -3.145  1.00 84.34           C  
-ATOM   5185  C   PHE C  36      49.388   8.526  -3.759  1.00 84.49           C  
-ATOM   5186  O   PHE C  36      49.951   9.383  -4.435  1.00 85.10           O  
-ATOM   5187  CB  PHE C  36      47.943  10.179  -2.508  1.00 85.31           C  
-ATOM   5188  CG  PHE C  36      46.526  10.663  -2.216  1.00 88.44           C  
-ATOM   5189  CD1 PHE C  36      46.216  11.272  -1.002  1.00 88.56           C  
-ATOM   5190  CD2 PHE C  36      45.509  10.524  -3.160  1.00 93.12           C  
-ATOM   5191  CE1 PHE C  36      44.917  11.732  -0.733  1.00 87.38           C  
-ATOM   5192  CE2 PHE C  36      44.205  10.983  -2.897  1.00 88.71           C  
-ATOM   5193  CZ  PHE C  36      43.913  11.586  -1.685  1.00 85.84           C  
-ATOM   5194  N   ALA C  37      49.908   7.329  -3.521  1.00 87.21           N  
-ATOM   5195  CA  ALA C  37      51.202   6.882  -4.023  1.00 88.83           C  
-ATOM   5196  C   ALA C  37      50.935   5.961  -5.207  1.00 90.28           C  
-ATOM   5197  O   ALA C  37      51.613   4.950  -5.391  1.00 93.11           O  
-ATOM   5198  CB  ALA C  37      51.944   6.124  -2.929  1.00 88.16           C  
-ATOM   5199  N   ILE C  38      49.920   6.311  -5.991  1.00 87.97           N  
-ATOM   5200  CA  ILE C  38      49.536   5.544  -7.169  1.00 83.87           C  
-ATOM   5201  C   ILE C  38      50.791   5.377  -8.025  1.00 83.80           C  
-ATOM   5202  O   ILE C  38      51.066   4.314  -8.581  1.00 77.18           O  
-ATOM   5203  CB  ILE C  38      48.446   6.297  -7.952  1.00 82.82           C  
-ATOM   5204  CG1 ILE C  38      47.292   6.656  -7.014  1.00 81.01           C  
-ATOM   5205  CG2 ILE C  38      47.925   5.433  -9.076  1.00 90.82           C  
-ATOM   5206  CD1 ILE C  38      46.210   7.506  -7.647  1.00 80.98           C  
-ATOM   5207  N   THR C  39      51.555   6.456  -8.107  1.00 88.89           N  
-ATOM   5208  CA  THR C  39      52.815   6.478  -8.836  1.00 86.73           C  
-ATOM   5209  C   THR C  39      53.906   6.401  -7.738  1.00 87.77           C  
-ATOM   5210  O   THR C  39      54.179   7.389  -7.037  1.00 92.17           O  
-ATOM   5211  CB  THR C  39      52.950   7.787  -9.674  1.00 84.15           C  
-ATOM   5212  OG1 THR C  39      54.258   8.329  -9.494  1.00 92.73           O  
-ATOM   5213  CG2 THR C  39      51.898   8.832  -9.257  1.00 74.87           C  
-ATOM   5214  N   PRO C  40      54.536   5.219  -7.573  1.00 82.84           N  
-ATOM   5215  CA  PRO C  40      55.589   4.906  -6.593  1.00 79.07           C  
-ATOM   5216  C   PRO C  40      56.606   5.984  -6.233  1.00 74.70           C  
-ATOM   5217  O   PRO C  40      56.790   6.303  -5.048  1.00 74.74           O  
-ATOM   5218  CB  PRO C  40      56.253   3.672  -7.192  1.00 73.82           C  
-ATOM   5219  CG  PRO C  40      55.105   2.965  -7.782  1.00 79.11           C  
-ATOM   5220  CD  PRO C  40      54.355   4.082  -8.492  1.00 81.99           C  
-ATOM   5221  N   ASN C  41      57.268   6.535  -7.245  1.00 64.45           N  
-ATOM   5222  CA  ASN C  41      58.281   7.553  -7.009  1.00 57.47           C  
-ATOM   5223  C   ASN C  41      57.761   8.963  -6.801  1.00 51.28           C  
-ATOM   5224  O   ASN C  41      58.492   9.915  -7.042  1.00 48.64           O  
-ATOM   5225  CB  ASN C  41      59.298   7.573  -8.151  1.00 60.14           C  
-ATOM   5226  CG  ASN C  41      60.713   7.240  -7.685  1.00 70.23           C  
-ATOM   5227  OD1 ASN C  41      61.690   7.563  -8.364  1.00 69.55           O  
-ATOM   5228  ND2 ASN C  41      60.827   6.582  -6.531  1.00 76.25           N  
-ATOM   5229  N   ARG C  42      56.517   9.117  -6.354  1.00 51.04           N  
-ATOM   5230  CA  ARG C  42      56.004  10.463  -6.128  1.00 56.10           C  
-ATOM   5231  C   ARG C  42      55.935  10.817  -4.648  1.00 53.77           C  
-ATOM   5232  O   ARG C  42      55.727  11.974  -4.292  1.00 61.62           O  
-ATOM   5233  CB  ARG C  42      54.612  10.654  -6.747  1.00 62.47           C  
-ATOM   5234  CG  ARG C  42      54.268  12.142  -6.936  1.00 76.42           C  
-ATOM   5235  CD  ARG C  42      52.774  12.430  -7.110  1.00 81.56           C  
-ATOM   5236  NE  ARG C  42      52.498  13.866  -6.983  1.00 87.37           N  
-ATOM   5237  CZ  ARG C  42      51.290  14.395  -6.792  1.00 85.39           C  
-ATOM   5238  NH1 ARG C  42      50.226  13.608  -6.703  1.00 83.18           N  
-ATOM   5239  NH2 ARG C  42      51.143  15.713  -6.681  1.00 80.51           N  
-ATOM   5240  N   ILE C  43      56.135   9.836  -3.780  1.00 48.20           N  
-ATOM   5241  CA  ILE C  43      56.050  10.102  -2.354  1.00 38.16           C  
-ATOM   5242  C   ILE C  43      56.947   9.198  -1.507  1.00 36.46           C  
-ATOM   5243  O   ILE C  43      57.058   7.991  -1.749  1.00 42.51           O  
-ATOM   5244  CB  ILE C  43      54.601   9.949  -1.911  1.00 33.97           C  
-ATOM   5245  CG1 ILE C  43      54.454  10.315  -0.447  1.00 30.13           C  
-ATOM   5246  CG2 ILE C  43      54.143   8.518  -2.152  1.00 51.14           C  
-ATOM   5247  CD1 ILE C  43      53.013  10.258   0.025  1.00 37.75           C  
-ATOM   5248  N   LEU C  44      57.580   9.791  -0.503  1.00 30.81           N  
-ATOM   5249  CA  LEU C  44      58.480   9.053   0.377  1.00 25.64           C  
-ATOM   5250  C   LEU C  44      58.123   9.235   1.842  1.00 23.00           C  
-ATOM   5251  O   LEU C  44      58.088  10.363   2.330  1.00 28.19           O  
-ATOM   5252  CB  LEU C  44      59.909   9.526   0.150  1.00 23.07           C  
-ATOM   5253  CG  LEU C  44      60.908   9.072   1.204  1.00 22.31           C  
-ATOM   5254  CD1 LEU C  44      60.875   7.576   1.289  1.00 24.31           C  
-ATOM   5255  CD2 LEU C  44      62.306   9.567   0.852  1.00 26.55           C  
-ATOM   5256  N   LEU C  45      57.867   8.137   2.549  1.00 22.36           N  
-ATOM   5257  CA  LEU C  45      57.510   8.238   3.968  1.00 26.71           C  
-ATOM   5258  C   LEU C  45      58.620   7.840   4.933  1.00 26.63           C  
-ATOM   5259  O   LEU C  45      59.384   6.907   4.697  1.00 34.07           O  
-ATOM   5260  CB  LEU C  45      56.269   7.404   4.296  1.00 26.72           C  
-ATOM   5261  CG  LEU C  45      55.884   7.500   5.774  1.00 29.17           C  
-ATOM   5262  CD1 LEU C  45      55.526   8.944   6.110  1.00 33.66           C  
-ATOM   5263  CD2 LEU C  45      54.715   6.586   6.068  1.00 40.39           C  
-ATOM   5264  N   ILE C  46      58.691   8.556   6.039  1.00 17.63           N  
-ATOM   5265  CA  ILE C  46      59.698   8.283   7.029  1.00 19.65           C  
-ATOM   5266  C   ILE C  46      58.977   8.150   8.343  1.00 29.66           C  
-ATOM   5267  O   ILE C  46      58.476   9.144   8.863  1.00 38.76           O  
-ATOM   5268  CB  ILE C  46      60.671   9.442   7.138  1.00 14.23           C  
-ATOM   5269  CG1 ILE C  46      61.387   9.640   5.813  1.00 12.11           C  
-ATOM   5270  CG2 ILE C  46      61.678   9.164   8.231  1.00 28.32           C  
-ATOM   5271  CD1 ILE C  46      62.352  10.800   5.832  1.00 17.91           C  
-ATOM   5272  N   GLY C  47      58.928   6.935   8.886  1.00 33.29           N  
-ATOM   5273  CA  GLY C  47      58.237   6.723  10.153  1.00 38.58           C  
-ATOM   5274  C   GLY C  47      59.066   6.916  11.416  1.00 38.96           C  
-ATOM   5275  O   GLY C  47      60.304   6.868  11.372  1.00 36.46           O  
-ATOM   5276  N   GLU C  48      58.385   7.141  12.544  1.00 38.61           N  
-ATOM   5277  CA  GLU C  48      59.071   7.322  13.824  1.00 35.48           C  
-ATOM   5278  C   GLU C  48      60.016   6.141  14.015  1.00 31.85           C  
-ATOM   5279  O   GLU C  48      59.652   5.002  13.744  1.00 39.48           O  
-ATOM   5280  CB  GLU C  48      58.060   7.396  14.973  1.00 32.47           C  
-ATOM   5281  CG  GLU C  48      57.324   8.732  15.043  1.00 45.16           C  
-ATOM   5282  CD  GLU C  48      56.481   8.881  16.297  1.00 50.00           C  
-ATOM   5283  OE1 GLU C  48      55.991   9.999  16.566  1.00 50.87           O  
-ATOM   5284  OE2 GLU C  48      56.306   7.877  17.014  1.00 52.21           O  
-ATOM   5285  N   PRO C  49      61.252   6.399  14.463  1.00 26.68           N  
-ATOM   5286  CA  PRO C  49      62.245   5.338  14.674  1.00 23.36           C  
-ATOM   5287  C   PRO C  49      62.133   4.603  16.011  1.00 28.58           C  
-ATOM   5288  O   PRO C  49      63.088   4.602  16.790  1.00 32.05           O  
-ATOM   5289  CB  PRO C  49      63.555   6.095  14.555  1.00 17.68           C  
-ATOM   5290  CG  PRO C  49      63.218   7.388  15.266  1.00 17.58           C  
-ATOM   5291  CD  PRO C  49      61.848   7.730  14.690  1.00 19.59           C  
-ATOM   5292  N   LEU C  50      60.985   3.974  16.270  1.00 30.24           N  
-ATOM   5293  CA  LEU C  50      60.772   3.257  17.530  1.00 28.20           C  
-ATOM   5294  C   LEU C  50      61.905   2.289  17.795  1.00 28.71           C  
-ATOM   5295  O   LEU C  50      62.391   2.186  18.921  1.00 36.02           O  
-ATOM   5296  CB  LEU C  50      59.470   2.466  17.506  1.00 24.76           C  
-ATOM   5297  CG  LEU C  50      58.201   3.179  17.054  1.00 34.13           C  
-ATOM   5298  CD1 LEU C  50      57.026   2.245  17.303  1.00 42.86           C  
-ATOM   5299  CD2 LEU C  50      58.016   4.492  17.803  1.00 34.09           C  
-ATOM   5300  N   SER C  51      62.321   1.578  16.754  1.00 24.57           N  
-ATOM   5301  CA  SER C  51      63.400   0.614  16.889  1.00 25.05           C  
-ATOM   5302  C   SER C  51      64.621   1.180  17.615  1.00 27.63           C  
-ATOM   5303  O   SER C  51      65.314   0.438  18.303  1.00 41.45           O  
-ATOM   5304  CB  SER C  51      63.800   0.070  15.514  1.00 34.68           C  
-ATOM   5305  OG  SER C  51      63.861   1.111  14.552  1.00 56.48           O  
-ATOM   5306  N   TYR C  52      64.897   2.478  17.476  1.00 21.53           N  
-ATOM   5307  CA  TYR C  52      66.046   3.057  18.180  1.00 12.84           C  
-ATOM   5308  C   TYR C  52      65.652   3.555  19.560  1.00  7.39           C  
-ATOM   5309  O   TYR C  52      66.425   3.453  20.500  1.00 10.78           O  
-ATOM   5310  CB  TYR C  52      66.673   4.205  17.387  1.00 12.06           C  
-ATOM   5311  CG  TYR C  52      67.485   3.765  16.185  1.00 13.17           C  
-ATOM   5312  CD1 TYR C  52      66.860   3.412  14.993  1.00 14.76           C  
-ATOM   5313  CD2 TYR C  52      68.884   3.719  16.236  1.00 12.20           C  
-ATOM   5314  CE1 TYR C  52      67.602   3.029  13.867  1.00 24.75           C  
-ATOM   5315  CE2 TYR C  52      69.642   3.333  15.117  1.00 15.68           C  
-ATOM   5316  CZ  TYR C  52      68.993   2.992  13.929  1.00 25.35           C  
-ATOM   5317  OH  TYR C  52      69.714   2.640  12.792  1.00 24.53           O  
-ATOM   5318  N   TRP C  53      64.451   4.103  19.678  1.00  4.47           N  
-ATOM   5319  CA  TRP C  53      63.988   4.584  20.961  1.00  5.95           C  
-ATOM   5320  C   TRP C  53      63.882   3.427  21.936  1.00 17.20           C  
-ATOM   5321  O   TRP C  53      64.254   3.562  23.102  1.00 24.82           O  
-ATOM   5322  CB  TRP C  53      62.619   5.243  20.839  1.00  7.19           C  
-ATOM   5323  CG  TRP C  53      62.615   6.497  20.042  1.00 12.26           C  
-ATOM   5324  CD1 TRP C  53      63.688   7.272  19.714  1.00 13.52           C  
-ATOM   5325  CD2 TRP C  53      61.471   7.149  19.502  1.00 13.06           C  
-ATOM   5326  NE1 TRP C  53      63.279   8.372  18.998  1.00  7.03           N  
-ATOM   5327  CE2 TRP C  53      61.920   8.319  18.855  1.00  9.62           C  
-ATOM   5328  CE3 TRP C  53      60.102   6.858  19.501  1.00 19.77           C  
-ATOM   5329  CZ2 TRP C  53      61.053   9.195  18.217  1.00 18.04           C  
-ATOM   5330  CZ3 TRP C  53      59.236   7.731  18.865  1.00 16.90           C  
-ATOM   5331  CH2 TRP C  53      59.715   8.886  18.232  1.00 22.36           C  
-ATOM   5332  N   ARG C  54      63.382   2.284  21.464  1.00 19.15           N  
-ATOM   5333  CA  ARG C  54      63.226   1.129  22.340  1.00 12.01           C  
-ATOM   5334  C   ARG C  54      64.498   0.358  22.564  1.00 16.65           C  
-ATOM   5335  O   ARG C  54      64.481  -0.706  23.167  1.00 30.11           O  
-ATOM   5336  CB  ARG C  54      62.126   0.199  21.838  1.00  4.47           C  
-ATOM   5337  CG  ARG C  54      60.748   0.746  22.156  1.00 17.73           C  
-ATOM   5338  CD  ARG C  54      59.669  -0.312  22.032  1.00 37.46           C  
-ATOM   5339  NE  ARG C  54      58.360   0.191  22.444  1.00 42.78           N  
-ATOM   5340  CZ  ARG C  54      58.062   0.583  23.680  1.00 49.45           C  
-ATOM   5341  NH1 ARG C  54      58.979   0.534  24.636  1.00 52.60           N  
-ATOM   5342  NH2 ARG C  54      56.844   1.023  23.964  1.00 55.37           N  
-ATOM   5343  N   ASN C  55      65.605   0.896  22.074  1.00 13.49           N  
-ATOM   5344  CA  ASN C  55      66.900   0.269  22.279  1.00 15.08           C  
-ATOM   5345  C   ASN C  55      67.979   1.252  21.898  1.00 17.21           C  
-ATOM   5346  O   ASN C  55      68.860   0.953  21.076  1.00 23.28           O  
-ATOM   5347  CB  ASN C  55      67.055  -0.998  21.448  1.00 26.28           C  
-ATOM   5348  CG  ASN C  55      68.448  -1.598  21.572  1.00 33.22           C  
-ATOM   5349  OD1 ASN C  55      68.870  -1.990  22.666  1.00 23.08           O  
-ATOM   5350  ND2 ASN C  55      69.176  -1.657  20.450  1.00 39.87           N  
-ATOM   5351  N   LEU C  56      67.919   2.435  22.497  1.00 11.43           N  
-ATOM   5352  CA  LEU C  56      68.907   3.429  22.169  1.00  9.19           C  
-ATOM   5353  C   LEU C  56      70.161   3.206  22.972  1.00  7.71           C  
-ATOM   5354  O   LEU C  56      70.235   3.580  24.134  1.00 10.09           O  
-ATOM   5355  CB  LEU C  56      68.361   4.828  22.406  1.00  5.27           C  
-ATOM   5356  CG  LEU C  56      69.213   5.829  21.624  1.00 15.22           C  
-ATOM   5357  CD1 LEU C  56      68.388   7.071  21.283  1.00 14.04           C  
-ATOM   5358  CD2 LEU C  56      70.481   6.149  22.425  1.00  6.73           C  
-ATOM   5359  N   ALA C  57      71.144   2.578  22.338  1.00 10.47           N  
-ATOM   5360  CA  ALA C  57      72.408   2.306  22.988  1.00 14.99           C  
-ATOM   5361  C   ALA C  57      72.213   1.631  24.350  1.00 16.11           C  
-ATOM   5362  O   ALA C  57      72.946   1.907  25.305  1.00 27.46           O  
-ATOM   5363  CB  ALA C  57      73.192   3.611  23.142  1.00 15.85           C  
-ATOM   5364  N   GLY C  58      71.213   0.762  24.449  1.00 10.48           N  
-ATOM   5365  CA  GLY C  58      71.002   0.057  25.699  1.00 18.96           C  
-ATOM   5366  C   GLY C  58      69.750   0.343  26.508  1.00 23.94           C  
-ATOM   5367  O   GLY C  58      69.221  -0.567  27.148  1.00 28.56           O  
-ATOM   5368  N   GLU C  59      69.264   1.581  26.503  1.00 19.80           N  
-ATOM   5369  CA  GLU C  59      68.075   1.888  27.288  1.00 12.04           C  
-ATOM   5370  C   GLU C  59      66.840   2.133  26.417  1.00 11.45           C  
-ATOM   5371  O   GLU C  59      66.946   2.521  25.246  1.00  8.90           O  
-ATOM   5372  CB  GLU C  59      68.365   3.086  28.206  1.00 12.90           C  
-ATOM   5373  CG  GLU C  59      69.724   2.965  28.919  1.00 27.71           C  
-ATOM   5374  CD  GLU C  59      69.927   3.950  30.083  1.00 37.20           C  
-ATOM   5375  OE1 GLU C  59      69.714   5.179  29.901  1.00 24.35           O  
-ATOM   5376  OE2 GLU C  59      70.322   3.481  31.184  1.00 40.43           O  
-ATOM   5377  N   ASP C  60      65.669   1.878  26.993  1.00  9.11           N  
-ATOM   5378  CA  ASP C  60      64.399   2.057  26.294  1.00  7.75           C  
-ATOM   5379  C   ASP C  60      63.771   3.400  26.666  1.00  7.87           C  
-ATOM   5380  O   ASP C  60      62.939   3.481  27.557  1.00  5.07           O  
-ATOM   5381  CB  ASP C  60      63.443   0.936  26.675  1.00 14.48           C  
-ATOM   5382  CG  ASP C  60      62.080   1.098  26.057  1.00 24.48           C  
-ATOM   5383  OD1 ASP C  60      61.478   2.188  26.187  1.00 28.94           O  
-ATOM   5384  OD2 ASP C  60      61.607   0.123  25.446  1.00 31.06           O  
-ATOM   5385  N   ALA C  61      64.162   4.451  25.966  1.00  8.94           N  
-ATOM   5386  CA  ALA C  61      63.648   5.773  26.259  1.00  7.70           C  
-ATOM   5387  C   ALA C  61      62.202   5.750  26.703  1.00  6.57           C  
-ATOM   5388  O   ALA C  61      61.881   6.276  27.757  1.00 19.50           O  
-ATOM   5389  CB  ALA C  61      63.806   6.689  25.044  1.00 12.80           C  
-ATOM   5390  N   ILE C  62      61.326   5.126  25.930  1.00  4.47           N  
-ATOM   5391  CA  ILE C  62      59.921   5.133  26.307  1.00  8.65           C  
-ATOM   5392  C   ILE C  62      59.606   4.582  27.693  1.00 13.86           C  
-ATOM   5393  O   ILE C  62      59.036   5.283  28.532  1.00 10.26           O  
-ATOM   5394  CB  ILE C  62      59.053   4.414  25.263  1.00 13.56           C  
-ATOM   5395  CG1 ILE C  62      58.937   5.300  24.010  1.00 19.59           C  
-ATOM   5396  CG2 ILE C  62      57.679   4.100  25.857  1.00  4.47           C  
-ATOM   5397  CD1 ILE C  62      57.901   4.862  22.996  1.00 13.51           C  
-ATOM   5398  N   CYS C  63      59.962   3.328  27.942  1.00 19.92           N  
-ATOM   5399  CA  CYS C  63      59.702   2.730  29.250  1.00 18.49           C  
-ATOM   5400  C   CYS C  63      60.281   3.627  30.345  1.00  9.36           C  
-ATOM   5401  O   CYS C  63      59.600   3.967  31.310  1.00  5.02           O  
-ATOM   5402  CB  CYS C  63      60.329   1.331  29.325  1.00 30.81           C  
-ATOM   5403  SG  CYS C  63      59.877   0.350  30.800  1.00 51.60           S  
-ATOM   5404  N   GLY C  64      61.538   4.018  30.159  1.00  9.04           N  
-ATOM   5405  CA  GLY C  64      62.236   4.869  31.105  1.00  5.66           C  
-ATOM   5406  C   GLY C  64      61.574   6.182  31.436  1.00  4.47           C  
-ATOM   5407  O   GLY C  64      61.626   6.630  32.573  1.00  4.47           O  
-ATOM   5408  N   ILE C  65      60.954   6.812  30.453  1.00  4.47           N  
-ATOM   5409  CA  ILE C  65      60.303   8.078  30.729  1.00  6.64           C  
-ATOM   5410  C   ILE C  65      59.039   7.821  31.522  1.00  7.62           C  
-ATOM   5411  O   ILE C  65      58.685   8.593  32.400  1.00 24.19           O  
-ATOM   5412  CB  ILE C  65      59.940   8.858  29.448  1.00  5.17           C  
-ATOM   5413  CG1 ILE C  65      59.531  10.286  29.815  1.00 10.88           C  
-ATOM   5414  CG2 ILE C  65      58.786   8.196  28.749  1.00  5.71           C  
-ATOM   5415  CD1 ILE C  65      59.977  11.344  28.813  1.00 19.75           C  
-ATOM   5416  N   TYR C  66      58.348   6.733  31.240  1.00  8.07           N  
-ATOM   5417  CA  TYR C  66      57.140   6.487  31.997  1.00 15.48           C  
-ATOM   5418  C   TYR C  66      57.469   5.843  33.330  1.00 20.07           C  
-ATOM   5419  O   TYR C  66      57.093   6.365  34.386  1.00 21.11           O  
-ATOM   5420  CB  TYR C  66      56.155   5.630  31.187  1.00 26.30           C  
-ATOM   5421  CG  TYR C  66      55.547   6.396  30.023  1.00 35.82           C  
-ATOM   5422  CD1 TYR C  66      55.911   6.110  28.702  1.00 34.41           C  
-ATOM   5423  CD2 TYR C  66      54.668   7.468  30.248  1.00 40.90           C  
-ATOM   5424  CE1 TYR C  66      55.423   6.878  27.631  1.00 35.48           C  
-ATOM   5425  CE2 TYR C  66      54.173   8.243  29.183  1.00 39.64           C  
-ATOM   5426  CZ  TYR C  66      54.560   7.945  27.878  1.00 37.24           C  
-ATOM   5427  OH  TYR C  66      54.130   8.733  26.827  1.00 34.70           O  
-ATOM   5428  N   GLY C  67      58.185   4.721  33.290  1.00 21.65           N  
-ATOM   5429  CA  GLY C  67      58.540   4.040  34.524  1.00 23.96           C  
-ATOM   5430  C   GLY C  67      59.033   4.998  35.601  1.00 26.52           C  
-ATOM   5431  O   GLY C  67      58.689   4.875  36.782  1.00 18.04           O  
-ATOM   5432  N   THR C  68      59.842   5.968  35.185  1.00 24.26           N  
-ATOM   5433  CA  THR C  68      60.384   6.941  36.109  1.00 11.99           C  
-ATOM   5434  C   THR C  68      59.282   7.663  36.841  1.00  7.87           C  
-ATOM   5435  O   THR C  68      59.434   8.014  38.004  1.00 17.19           O  
-ATOM   5436  CB  THR C  68      61.265   7.953  35.387  1.00  4.55           C  
-ATOM   5437  OG1 THR C  68      62.533   7.351  35.116  1.00 10.41           O  
-ATOM   5438  CG2 THR C  68      61.469   9.182  36.231  1.00  9.38           C  
-ATOM   5439  N   GLN C  69      58.165   7.892  36.178  1.00  4.47           N  
-ATOM   5440  CA  GLN C  69      57.091   8.571  36.872  1.00 13.97           C  
-ATOM   5441  C   GLN C  69      56.427   7.617  37.849  1.00 15.70           C  
-ATOM   5442  O   GLN C  69      56.108   7.999  38.981  1.00 14.29           O  
-ATOM   5443  CB  GLN C  69      56.077   9.127  35.883  1.00 23.23           C  
-ATOM   5444  CG  GLN C  69      56.684  10.120  34.892  1.00 28.27           C  
-ATOM   5445  CD  GLN C  69      57.687  11.071  35.533  1.00 31.01           C  
-ATOM   5446  OE1 GLN C  69      57.403  11.724  36.547  1.00 32.97           O  
-ATOM   5447  NE2 GLN C  69      58.869  11.158  34.937  1.00 30.74           N  
-ATOM   5448  N   THR C  70      56.226   6.374  37.419  1.00 17.06           N  
-ATOM   5449  CA  THR C  70      55.626   5.387  38.307  1.00 23.64           C  
-ATOM   5450  C   THR C  70      56.547   5.237  39.519  1.00 21.52           C  
-ATOM   5451  O   THR C  70      56.090   5.165  40.664  1.00 20.84           O  
-ATOM   5452  CB  THR C  70      55.496   4.024  37.638  1.00 25.25           C  
-ATOM   5453  OG1 THR C  70      54.737   4.156  36.433  1.00 38.02           O  
-ATOM   5454  CG2 THR C  70      54.798   3.053  38.573  1.00 24.73           C  
-ATOM   5455  N   ARG C  71      57.852   5.206  39.253  1.00 13.70           N  
-ATOM   5456  CA  ARG C  71      58.840   5.075  40.310  1.00  6.07           C  
-ATOM   5457  C   ARG C  71      58.839   6.297  41.221  1.00  5.11           C  
-ATOM   5458  O   ARG C  71      59.270   6.226  42.367  1.00 12.16           O  
-ATOM   5459  CB  ARG C  71      60.220   4.865  39.706  1.00  4.47           C  
-ATOM   5460  CG  ARG C  71      60.807   3.524  40.044  1.00  4.47           C  
-ATOM   5461  CD  ARG C  71      61.870   3.138  39.055  1.00  9.35           C  
-ATOM   5462  NE  ARG C  71      63.061   3.980  39.137  1.00 16.80           N  
-ATOM   5463  CZ  ARG C  71      63.998   3.853  40.068  1.00 11.73           C  
-ATOM   5464  NH1 ARG C  71      63.872   2.911  40.999  1.00 25.57           N  
-ATOM   5465  NH2 ARG C  71      65.061   4.653  40.057  1.00  4.47           N  
-ATOM   5466  N   ARG C  72      58.354   7.422  40.714  1.00  4.47           N  
-ATOM   5467  CA  ARG C  72      58.296   8.624  41.523  1.00  5.02           C  
-ATOM   5468  C   ARG C  72      57.102   8.577  42.466  1.00 11.37           C  
-ATOM   5469  O   ARG C  72      57.216   8.951  43.629  1.00 18.69           O  
-ATOM   5470  CB  ARG C  72      58.193   9.860  40.645  1.00  9.45           C  
-ATOM   5471  CG  ARG C  72      57.824  11.125  41.410  1.00 14.12           C  
-ATOM   5472  CD  ARG C  72      58.073  12.356  40.556  1.00 26.19           C  
-ATOM   5473  NE  ARG C  72      57.628  13.582  41.208  1.00 41.14           N  
-ATOM   5474  CZ  ARG C  72      57.800  14.799  40.700  1.00 46.06           C  
-ATOM   5475  NH1 ARG C  72      58.416  14.951  39.532  1.00 53.73           N  
-ATOM   5476  NH2 ARG C  72      57.332  15.861  41.344  1.00 41.74           N  
-ATOM   5477  N   LEU C  73      55.957   8.115  41.972  1.00 10.25           N  
-ATOM   5478  CA  LEU C  73      54.754   8.034  42.803  1.00 14.57           C  
-ATOM   5479  C   LEU C  73      54.887   7.068  43.966  1.00 18.07           C  
-ATOM   5480  O   LEU C  73      54.376   7.311  45.061  1.00 18.58           O  
-ATOM   5481  CB  LEU C  73      53.557   7.628  41.955  1.00 13.29           C  
-ATOM   5482  CG  LEU C  73      52.920   8.759  41.146  1.00 38.42           C  
-ATOM   5483  CD1 LEU C  73      53.966   9.820  40.705  1.00 38.19           C  
-ATOM   5484  CD2 LEU C  73      52.209   8.124  39.950  1.00 47.28           C  
-ATOM   5485  N   ASN C  74      55.575   5.964  43.724  1.00 19.25           N  
-ATOM   5486  CA  ASN C  74      55.774   4.961  44.757  1.00 23.55           C  
-ATOM   5487  C   ASN C  74      56.847   5.396  45.733  1.00 20.63           C  
-ATOM   5488  O   ASN C  74      57.085   4.736  46.738  1.00 28.67           O  
-ATOM   5489  CB  ASN C  74      56.161   3.636  44.112  1.00 31.30           C  
-ATOM   5490  CG  ASN C  74      55.106   3.149  43.148  1.00 51.15           C  
-ATOM   5491  OD1 ASN C  74      55.363   2.283  42.300  1.00 61.82           O  
-ATOM   5492  ND2 ASN C  74      53.893   3.704  43.275  1.00 50.68           N  
-ATOM   5493  N   GLY C  75      57.494   6.511  45.434  1.00 10.82           N  
-ATOM   5494  CA  GLY C  75      58.535   6.992  46.309  1.00 10.93           C  
-ATOM   5495  C   GLY C  75      59.767   6.122  46.240  1.00 11.69           C  
-ATOM   5496  O   GLY C  75      60.591   6.133  47.159  1.00 11.95           O  
-ATOM   5497  N   ASP C  76      59.896   5.355  45.163  1.00 11.93           N  
-ATOM   5498  CA  ASP C  76      61.063   4.497  45.011  1.00 21.65           C  
-ATOM   5499  C   ASP C  76      62.269   5.394  44.780  1.00 18.80           C  
-ATOM   5500  O   ASP C  76      63.414   4.969  44.954  1.00 21.05           O  
-ATOM   5501  CB  ASP C  76      60.896   3.523  43.833  1.00 30.54           C  
-ATOM   5502  CG  ASP C  76      59.965   2.358  44.153  1.00 49.60           C  
-ATOM   5503  OD1 ASP C  76      59.734   1.525  43.249  1.00 56.77           O  
-ATOM   5504  OD2 ASP C  76      59.470   2.272  45.301  1.00 58.24           O  
-ATOM   5505  N   VAL C  77      62.002   6.645  44.411  1.00 15.55           N  
-ATOM   5506  CA  VAL C  77      63.070   7.606  44.139  1.00 12.35           C  
-ATOM   5507  C   VAL C  77      62.695   9.056  44.433  1.00 11.65           C  
-ATOM   5508  O   VAL C  77      61.560   9.484  44.228  1.00 13.61           O  
-ATOM   5509  CB  VAL C  77      63.513   7.541  42.674  1.00  4.55           C  
-ATOM   5510  CG1 VAL C  77      62.498   8.242  41.801  1.00  4.47           C  
-ATOM   5511  CG2 VAL C  77      64.877   8.155  42.530  1.00  9.06           C  
-ATOM   5512  N   SER C  78      63.675   9.814  44.900  1.00 11.44           N  
-ATOM   5513  CA  SER C  78      63.477  11.217  45.226  1.00 15.72           C  
-ATOM   5514  C   SER C  78      62.864  11.993  44.066  1.00 18.79           C  
-ATOM   5515  O   SER C  78      63.248  11.802  42.906  1.00 28.65           O  
-ATOM   5516  CB  SER C  78      64.823  11.850  45.595  1.00 23.27           C  
-ATOM   5517  OG  SER C  78      64.729  13.266  45.700  1.00 40.52           O  
-ATOM   5518  N   PRO C  79      61.907  12.890  44.359  1.00 16.53           N  
-ATOM   5519  CA  PRO C  79      61.285  13.674  43.288  1.00 18.82           C  
-ATOM   5520  C   PRO C  79      62.345  14.526  42.592  1.00 15.14           C  
-ATOM   5521  O   PRO C  79      62.227  14.843  41.413  1.00 13.43           O  
-ATOM   5522  CB  PRO C  79      60.257  14.517  44.032  1.00  8.68           C  
-ATOM   5523  CG  PRO C  79      60.944  14.767  45.316  1.00 19.71           C  
-ATOM   5524  CD  PRO C  79      61.483  13.393  45.672  1.00 17.64           C  
-ATOM   5525  N   GLU C  80      63.385  14.885  43.332  1.00 16.96           N  
-ATOM   5526  CA  GLU C  80      64.456  15.675  42.759  1.00 20.13           C  
-ATOM   5527  C   GLU C  80      65.201  14.824  41.723  1.00 10.87           C  
-ATOM   5528  O   GLU C  80      65.564  15.318  40.656  1.00  8.73           O  
-ATOM   5529  CB  GLU C  80      65.419  16.161  43.858  1.00 28.59           C  
-ATOM   5530  CG  GLU C  80      66.470  17.160  43.350  1.00 45.34           C  
-ATOM   5531  CD  GLU C  80      67.309  17.798  44.465  1.00 61.31           C  
-ATOM   5532  OE1 GLU C  80      66.730  18.446  45.368  1.00 64.98           O  
-ATOM   5533  OE2 GLU C  80      68.555  17.662  44.432  1.00 67.02           O  
-ATOM   5534  N   ASP C  81      65.424  13.549  42.018  1.00  4.47           N  
-ATOM   5535  CA  ASP C  81      66.130  12.718  41.058  1.00  4.47           C  
-ATOM   5536  C   ASP C  81      65.193  12.332  39.945  1.00 10.71           C  
-ATOM   5537  O   ASP C  81      65.581  12.280  38.776  1.00 15.55           O  
-ATOM   5538  CB  ASP C  81      66.670  11.446  41.696  1.00  5.63           C  
-ATOM   5539  CG  ASP C  81      67.687  11.721  42.771  1.00 21.99           C  
-ATOM   5540  OD1 ASP C  81      68.615  12.531  42.543  1.00 29.21           O  
-ATOM   5541  OD2 ASP C  81      67.564  11.109  43.850  1.00 39.59           O  
-ATOM   5542  N   ALA C  82      63.949  12.054  40.306  1.00  4.47           N  
-ATOM   5543  CA  ALA C  82      62.976  11.672  39.304  1.00  8.57           C  
-ATOM   5544  C   ALA C  82      62.937  12.692  38.171  1.00 15.04           C  
-ATOM   5545  O   ALA C  82      62.658  12.342  37.029  1.00 17.49           O  
-ATOM   5546  CB  ALA C  82      61.615  11.547  39.932  1.00 10.50           C  
-ATOM   5547  N   GLN C  83      63.214  13.955  38.487  1.00 17.56           N  
-ATOM   5548  CA  GLN C  83      63.199  15.000  37.472  1.00 14.57           C  
-ATOM   5549  C   GLN C  83      64.419  14.886  36.594  1.00 14.44           C  
-ATOM   5550  O   GLN C  83      64.320  14.922  35.371  1.00 22.25           O  
-ATOM   5551  CB  GLN C  83      63.170  16.382  38.108  1.00 15.21           C  
-ATOM   5552  CG  GLN C  83      61.982  16.598  39.010  1.00 17.69           C  
-ATOM   5553  CD  GLN C  83      61.726  18.064  39.290  1.00 20.76           C  
-ATOM   5554  OE1 GLN C  83      62.601  18.795  39.776  1.00 14.70           O  
-ATOM   5555  NE2 GLN C  83      60.515  18.506  38.985  1.00 21.77           N  
-ATOM   5556  N   ARG C  84      65.576  14.751  37.223  1.00 10.91           N  
-ATOM   5557  CA  ARG C  84      66.818  14.626  36.482  1.00 10.18           C  
-ATOM   5558  C   ARG C  84      66.753  13.360  35.666  1.00  4.47           C  
-ATOM   5559  O   ARG C  84      67.099  13.349  34.484  1.00  4.47           O  
-ATOM   5560  CB  ARG C  84      67.993  14.585  37.458  1.00 11.72           C  
-ATOM   5561  CG  ARG C  84      68.220  15.928  38.110  1.00 12.61           C  
-ATOM   5562  CD  ARG C  84      69.016  15.855  39.381  1.00  7.77           C  
-ATOM   5563  NE  ARG C  84      68.992  17.161  40.025  1.00 10.64           N  
-ATOM   5564  CZ  ARG C  84      69.464  17.404  41.238  1.00 19.45           C  
-ATOM   5565  NH1 ARG C  84      70.008  16.422  41.948  1.00 26.58           N  
-ATOM   5566  NH2 ARG C  84      69.383  18.629  41.740  1.00 27.86           N  
-ATOM   5567  N   LEU C  85      66.281  12.299  36.311  1.00  4.61           N  
-ATOM   5568  CA  LEU C  85      66.160  11.009  35.669  1.00  5.38           C  
-ATOM   5569  C   LEU C  85      65.293  11.127  34.412  1.00 11.78           C  
-ATOM   5570  O   LEU C  85      65.579  10.514  33.386  1.00 14.65           O  
-ATOM   5571  CB  LEU C  85      65.577  10.014  36.662  1.00  4.47           C  
-ATOM   5572  CG  LEU C  85      66.414   8.741  36.774  1.00  4.47           C  
-ATOM   5573  CD1 LEU C  85      67.894   9.063  36.838  1.00  4.47           C  
-ATOM   5574  CD2 LEU C  85      65.965   7.976  37.993  1.00 13.95           C  
-ATOM   5575  N   THR C  86      64.241  11.934  34.486  1.00 15.44           N  
-ATOM   5576  CA  THR C  86      63.365  12.145  33.335  1.00 10.88           C  
-ATOM   5577  C   THR C  86      64.162  12.811  32.207  1.00  8.36           C  
-ATOM   5578  O   THR C  86      64.213  12.311  31.084  1.00  4.47           O  
-ATOM   5579  CB  THR C  86      62.165  13.055  33.700  1.00 14.98           C  
-ATOM   5580  OG1 THR C  86      61.399  12.444  34.749  1.00 18.82           O  
-ATOM   5581  CG2 THR C  86      61.269  13.267  32.492  1.00  9.73           C  
-ATOM   5582  N   ALA C  87      64.787  13.940  32.520  1.00  4.47           N  
-ATOM   5583  CA  ALA C  87      65.582  14.660  31.541  1.00  4.47           C  
-ATOM   5584  C   ALA C  87      66.400  13.676  30.765  1.00  4.47           C  
-ATOM   5585  O   ALA C  87      66.410  13.692  29.550  1.00 13.19           O  
-ATOM   5586  CB  ALA C  87      66.502  15.645  32.227  1.00 14.72           C  
-ATOM   5587  N   HIS C  88      67.091  12.807  31.478  1.00  4.47           N  
-ATOM   5588  CA  HIS C  88      67.915  11.810  30.829  1.00  4.47           C  
-ATOM   5589  C   HIS C  88      67.172  11.101  29.726  1.00 12.41           C  
-ATOM   5590  O   HIS C  88      67.550  11.200  28.559  1.00 21.94           O  
-ATOM   5591  CB  HIS C  88      68.369  10.769  31.821  1.00  4.47           C  
-ATOM   5592  CG  HIS C  88      69.101   9.632  31.190  1.00  4.47           C  
-ATOM   5593  ND1 HIS C  88      70.339   9.781  30.599  1.00  4.47           N  
-ATOM   5594  CD2 HIS C  88      68.769   8.326  31.058  1.00  4.47           C  
-ATOM   5595  CE1 HIS C  88      70.739   8.611  30.135  1.00 11.96           C  
-ATOM   5596  NE2 HIS C  88      69.805   7.712  30.401  1.00  7.11           N  
-ATOM   5597  N   PHE C  89      66.121  10.371  30.094  1.00 11.27           N  
-ATOM   5598  CA  PHE C  89      65.331   9.636  29.105  1.00 10.98           C  
-ATOM   5599  C   PHE C  89      64.766  10.519  28.001  1.00  8.59           C  
-ATOM   5600  O   PHE C  89      64.983  10.265  26.822  1.00  6.85           O  
-ATOM   5601  CB  PHE C  89      64.200   8.889  29.789  1.00  9.09           C  
-ATOM   5602  CG  PHE C  89      64.673   7.805  30.697  1.00 12.33           C  
-ATOM   5603  CD1 PHE C  89      64.572   7.938  32.068  1.00  4.47           C  
-ATOM   5604  CD2 PHE C  89      65.245   6.654  30.177  1.00 12.77           C  
-ATOM   5605  CE1 PHE C  89      65.032   6.946  32.900  1.00  4.47           C  
-ATOM   5606  CE2 PHE C  89      65.709   5.656  31.014  1.00  4.47           C  
-ATOM   5607  CZ  PHE C  89      65.602   5.805  32.373  1.00  4.47           C  
-ATOM   5608  N   GLN C  90      64.039  11.558  28.379  1.00  5.69           N  
-ATOM   5609  CA  GLN C  90      63.486  12.456  27.382  1.00  6.29           C  
-ATOM   5610  C   GLN C  90      64.521  12.775  26.308  1.00  7.39           C  
-ATOM   5611  O   GLN C  90      64.217  12.757  25.125  1.00 11.35           O  
-ATOM   5612  CB  GLN C  90      63.024  13.743  28.048  1.00  7.99           C  
-ATOM   5613  CG  GLN C  90      62.663  14.845  27.088  1.00  8.97           C  
-ATOM   5614  CD  GLN C  90      61.755  14.384  25.974  1.00 10.74           C  
-ATOM   5615  OE1 GLN C  90      60.898  13.513  26.156  1.00  4.47           O  
-ATOM   5616  NE2 GLN C  90      61.925  14.988  24.807  1.00 19.69           N  
-ATOM   5617  N   SER C  91      65.749  13.050  26.731  1.00  9.93           N  
-ATOM   5618  CA  SER C  91      66.822  13.388  25.809  1.00  8.51           C  
-ATOM   5619  C   SER C  91      67.100  12.291  24.810  1.00  8.63           C  
-ATOM   5620  O   SER C  91      67.482  12.570  23.677  1.00 17.99           O  
-ATOM   5621  CB  SER C  91      68.117  13.650  26.551  1.00 11.33           C  
-ATOM   5622  OG  SER C  91      68.842  12.435  26.667  1.00 13.73           O  
-ATOM   5623  N   LEU C  92      66.942  11.042  25.228  1.00  8.16           N  
-ATOM   5624  CA  LEU C  92      67.197   9.913  24.322  1.00 16.04           C  
-ATOM   5625  C   LEU C  92      66.506  10.005  22.949  1.00 16.05           C  
-ATOM   5626  O   LEU C  92      67.090   9.616  21.927  1.00  7.01           O  
-ATOM   5627  CB  LEU C  92      66.807   8.589  24.993  1.00 12.96           C  
-ATOM   5628  CG  LEU C  92      67.722   8.140  26.134  1.00  6.09           C  
-ATOM   5629  CD1 LEU C  92      67.205   6.835  26.687  1.00  5.34           C  
-ATOM   5630  CD2 LEU C  92      69.159   7.983  25.638  1.00  4.47           C  
-ATOM   5631  N   PHE C  93      65.275  10.520  22.941  1.00 16.24           N  
-ATOM   5632  CA  PHE C  93      64.481  10.683  21.722  1.00 16.57           C  
-ATOM   5633  C   PHE C  93      65.150  11.553  20.643  1.00 17.50           C  
-ATOM   5634  O   PHE C  93      64.890  11.386  19.446  1.00 25.95           O  
-ATOM   5635  CB  PHE C  93      63.109  11.286  22.075  1.00 13.87           C  
-ATOM   5636  CG  PHE C  93      62.204  10.346  22.826  1.00 18.91           C  
-ATOM   5637  CD1 PHE C  93      61.521   9.327  22.162  1.00 25.24           C  
-ATOM   5638  CD2 PHE C  93      62.050  10.464  24.201  1.00 16.95           C  
-ATOM   5639  CE1 PHE C  93      60.695   8.437  22.867  1.00 25.98           C  
-ATOM   5640  CE2 PHE C  93      61.229   9.580  24.913  1.00 22.26           C  
-ATOM   5641  CZ  PHE C  93      60.552   8.568  24.249  1.00 18.86           C  
-ATOM   5642  N   CYS C  94      66.014  12.466  21.067  1.00 13.49           N  
-ATOM   5643  CA  CYS C  94      66.695  13.388  20.158  1.00 14.50           C  
-ATOM   5644  C   CYS C  94      67.546  12.831  19.016  1.00 13.05           C  
-ATOM   5645  O   CYS C  94      67.233  13.034  17.856  1.00 15.78           O  
-ATOM   5646  CB  CYS C  94      67.550  14.359  20.978  1.00 17.17           C  
-ATOM   5647  SG  CYS C  94      66.583  15.394  22.111  1.00 30.17           S  
-ATOM   5648  N   SER C  95      68.630  12.145  19.349  1.00 19.99           N  
-ATOM   5649  CA  SER C  95      69.547  11.611  18.347  1.00 18.83           C  
-ATOM   5650  C   SER C  95      68.988  11.040  17.050  1.00 16.50           C  
-ATOM   5651  O   SER C  95      69.268  11.567  15.972  1.00 22.49           O  
-ATOM   5652  CB  SER C  95      70.483  10.581  18.991  1.00 23.72           C  
-ATOM   5653  OG  SER C  95      69.811   9.848  19.999  1.00 33.22           O  
-ATOM   5654  N   PRO C  96      68.185   9.970  17.125  1.00 13.39           N  
-ATOM   5655  CA  PRO C  96      67.628   9.370  15.903  1.00 15.01           C  
-ATOM   5656  C   PRO C  96      67.100  10.418  14.943  1.00 18.90           C  
-ATOM   5657  O   PRO C  96      67.654  10.634  13.863  1.00 24.32           O  
-ATOM   5658  CB  PRO C  96      66.509   8.470  16.422  1.00  9.73           C  
-ATOM   5659  CG  PRO C  96      66.957   8.140  17.797  1.00 26.83           C  
-ATOM   5660  CD  PRO C  96      67.479   9.469  18.308  1.00 17.87           C  
-ATOM   5661  N   HIS C  97      66.025  11.074  15.350  1.00 14.80           N  
-ATOM   5662  CA  HIS C  97      65.427  12.098  14.525  1.00 12.38           C  
-ATOM   5663  C   HIS C  97      66.407  13.131  14.009  1.00 11.61           C  
-ATOM   5664  O   HIS C  97      66.237  13.635  12.903  1.00 18.47           O  
-ATOM   5665  CB  HIS C  97      64.335  12.800  15.300  1.00 23.74           C  
-ATOM   5666  CG  HIS C  97      62.972  12.445  14.832  1.00 31.85           C  
-ATOM   5667  ND1 HIS C  97      62.581  12.614  13.522  1.00 34.59           N  
-ATOM   5668  CD2 HIS C  97      61.916  11.903  15.480  1.00 32.81           C  
-ATOM   5669  CE1 HIS C  97      61.337  12.191  13.385  1.00 46.78           C  
-ATOM   5670  NE2 HIS C  97      60.911  11.755  14.558  1.00 45.36           N  
-ATOM   5671  N   ALA C  98      67.425  13.439  14.811  1.00  8.03           N  
-ATOM   5672  CA  ALA C  98      68.427  14.437  14.458  1.00  8.13           C  
-ATOM   5673  C   ALA C  98      69.449  13.944  13.437  1.00 14.63           C  
-ATOM   5674  O   ALA C  98      69.774  14.671  12.495  1.00 24.17           O  
-ATOM   5675  CB  ALA C  98      69.126  14.926  15.703  1.00  7.76           C  
-ATOM   5676  N   ILE C  99      69.966  12.730  13.617  1.00 10.40           N  
-ATOM   5677  CA  ILE C  99      70.931  12.183  12.658  1.00 12.10           C  
-ATOM   5678  C   ILE C  99      70.305  12.274  11.270  1.00 14.39           C  
-ATOM   5679  O   ILE C  99      70.940  12.711  10.308  1.00 14.39           O  
-ATOM   5680  CB  ILE C  99      71.214  10.699  12.911  1.00 14.40           C  
-ATOM   5681  CG1 ILE C  99      71.769  10.502  14.323  1.00 10.86           C  
-ATOM   5682  CG2 ILE C  99      72.178  10.178  11.837  1.00 10.70           C  
-ATOM   5683  CD1 ILE C  99      73.091  11.173  14.544  1.00 14.76           C  
-ATOM   5684  N   MET C 100      69.050  11.842  11.202  1.00 14.97           N  
-ATOM   5685  CA  MET C 100      68.248  11.845   9.994  1.00 17.88           C  
-ATOM   5686  C   MET C 100      68.125  13.270   9.437  1.00 21.21           C  
-ATOM   5687  O   MET C 100      68.739  13.608   8.424  1.00 27.97           O  
-ATOM   5688  CB  MET C 100      66.863  11.298  10.329  1.00 25.11           C  
-ATOM   5689  CG  MET C 100      65.929  11.161   9.159  1.00 47.88           C  
-ATOM   5690  SD  MET C 100      66.186   9.613   8.304  1.00 70.90           S  
-ATOM   5691  CE  MET C 100      66.876  10.180   6.736  1.00 56.90           C  
-ATOM   5692  N   HIS C 101      67.325  14.102  10.099  1.00 19.28           N  
-ATOM   5693  CA  HIS C 101      67.122  15.481   9.662  1.00 20.22           C  
-ATOM   5694  C   HIS C 101      68.415  16.167   9.216  1.00 21.97           C  
-ATOM   5695  O   HIS C 101      68.433  16.865   8.205  1.00 26.25           O  
-ATOM   5696  CB  HIS C 101      66.494  16.296  10.779  1.00 17.50           C  
-ATOM   5697  CG  HIS C 101      66.406  17.757  10.481  1.00 32.74           C  
-ATOM   5698  ND1 HIS C 101      65.300  18.331   9.893  1.00 39.75           N  
-ATOM   5699  CD2 HIS C 101      67.290  18.764  10.682  1.00 42.61           C  
-ATOM   5700  CE1 HIS C 101      65.502  19.629   9.751  1.00 38.52           C  
-ATOM   5701  NE2 HIS C 101      66.702  19.919  10.221  1.00 42.66           N  
-ATOM   5702  N   ALA C 102      69.495  15.977   9.966  1.00 18.98           N  
-ATOM   5703  CA  ALA C 102      70.771  16.597   9.620  1.00 21.16           C  
-ATOM   5704  C   ALA C 102      71.326  16.075   8.287  1.00 20.51           C  
-ATOM   5705  O   ALA C 102      71.957  16.824   7.532  1.00 15.91           O  
-ATOM   5706  CB  ALA C 102      71.773  16.364  10.732  1.00 29.86           C  
-ATOM   5707  N   LYS C 103      71.108  14.790   8.010  1.00 18.32           N  
-ATOM   5708  CA  LYS C 103      71.556  14.193   6.751  1.00 17.61           C  
-ATOM   5709  C   LYS C 103      70.749  14.815   5.620  1.00 19.41           C  
-ATOM   5710  O   LYS C 103      71.299  15.313   4.637  1.00 22.61           O  
-ATOM   5711  CB  LYS C 103      71.317  12.686   6.754  1.00 11.57           C  
-ATOM   5712  CG  LYS C 103      71.291  12.066   5.361  1.00 28.21           C  
-ATOM   5713  CD  LYS C 103      72.673  12.017   4.711  1.00 37.63           C  
-ATOM   5714  CE  LYS C 103      73.530  10.911   5.323  1.00 42.82           C  
-ATOM   5715  NZ  LYS C 103      74.856  10.825   4.651  1.00 45.72           N  
-ATOM   5716  N   ILE C 104      69.433  14.767   5.774  1.00 18.98           N  
-ATOM   5717  CA  ILE C 104      68.514  15.327   4.801  1.00 23.09           C  
-ATOM   5718  C   ILE C 104      68.820  16.787   4.456  1.00 24.97           C  
-ATOM   5719  O   ILE C 104      68.735  17.188   3.299  1.00 31.67           O  
-ATOM   5720  CB  ILE C 104      67.078  15.190   5.323  1.00 21.75           C  
-ATOM   5721  CG1 ILE C 104      66.625  13.750   5.090  1.00 26.08           C  
-ATOM   5722  CG2 ILE C 104      66.150  16.226   4.677  1.00 14.95           C  
-ATOM   5723  CD1 ILE C 104      65.342  13.404   5.793  1.00 36.09           C  
-ATOM   5724  N   SER C 105      69.179  17.588   5.446  1.00 26.59           N  
-ATOM   5725  CA  SER C 105      69.484  18.985   5.159  1.00 34.38           C  
-ATOM   5726  C   SER C 105      70.683  19.074   4.228  1.00 31.18           C  
-ATOM   5727  O   SER C 105      70.817  20.036   3.476  1.00 37.14           O  
-ATOM   5728  CB  SER C 105      69.782  19.757   6.448  1.00 44.09           C  
-ATOM   5729  OG  SER C 105      68.651  19.779   7.303  1.00 55.36           O  
-ATOM   5730  N   ALA C 106      71.551  18.066   4.278  1.00 27.81           N  
-ATOM   5731  CA  ALA C 106      72.745  18.042   3.436  1.00 30.15           C  
-ATOM   5732  C   ALA C 106      72.407  17.713   1.982  1.00 33.32           C  
-ATOM   5733  O   ALA C 106      73.084  18.167   1.055  1.00 31.50           O  
-ATOM   5734  CB  ALA C 106      73.751  17.033   3.980  1.00 34.38           C  
-ATOM   5735  N   LEU C 107      71.357  16.923   1.783  1.00 38.35           N  
-ATOM   5736  CA  LEU C 107      70.940  16.554   0.437  1.00 39.19           C  
-ATOM   5737  C   LEU C 107      70.003  17.611  -0.128  1.00 41.10           C  
-ATOM   5738  O   LEU C 107      69.407  17.406  -1.176  1.00 52.30           O  
-ATOM   5739  CB  LEU C 107      70.223  15.198   0.441  1.00 27.99           C  
-ATOM   5740  CG  LEU C 107      70.926  14.049   1.163  1.00 37.58           C  
-ATOM   5741  CD1 LEU C 107      70.149  12.752   0.926  1.00 40.70           C  
-ATOM   5742  CD2 LEU C 107      72.372  13.927   0.669  1.00 43.55           C  
-ATOM   5743  N   MET C 108      69.868  18.739   0.558  1.00 43.58           N  
-ATOM   5744  CA  MET C 108      68.973  19.784   0.078  1.00 55.11           C  
-ATOM   5745  C   MET C 108      69.738  20.865  -0.681  1.00 64.58           C  
-ATOM   5746  O   MET C 108      70.664  21.484  -0.146  1.00 63.64           O  
-ATOM   5747  CB  MET C 108      68.197  20.412   1.245  1.00 54.81           C  
-ATOM   5748  CG  MET C 108      66.718  20.697   0.940  1.00 52.25           C  
-ATOM   5749  SD  MET C 108      65.599  19.292   1.278  1.00 57.34           S  
-ATOM   5750  CE  MET C 108      66.059  18.127  -0.043  1.00 42.78           C  
-ATOM   5751  N   ASP C 109      69.338  21.078  -1.934  1.00 72.77           N  
-ATOM   5752  CA  ASP C 109      69.963  22.070  -2.802  1.00 78.71           C  
-ATOM   5753  C   ASP C 109      69.587  23.491  -2.391  1.00 81.53           C  
-ATOM   5754  O   ASP C 109      68.425  23.902  -2.501  1.00 78.52           O  
-ATOM   5755  CB  ASP C 109      69.553  21.825  -4.261  1.00 82.77           C  
-ATOM   5756  CG  ASP C 109      70.247  22.774  -5.233  1.00 91.82           C  
-ATOM   5757  OD1 ASP C 109      71.498  22.759  -5.288  1.00 92.95           O  
-ATOM   5758  OD2 ASP C 109      69.545  23.533  -5.943  1.00 96.87           O  
-ATOM   5759  N   THR C 110      70.583  24.232  -1.915  1.00 87.25           N  
-ATOM   5760  CA  THR C 110      70.387  25.614  -1.488  1.00 95.59           C  
-ATOM   5761  C   THR C 110      70.998  26.560  -2.535  1.00 94.58           C  
-ATOM   5762  O   THR C 110      71.883  27.370  -2.243  1.00 93.27           O  
-ATOM   5763  CB  THR C 110      71.038  25.868  -0.087  1.00 99.32           C  
-ATOM   5764  OG1 THR C 110      70.606  24.855   0.838  1.00 99.20           O  
-ATOM   5765  CG2 THR C 110      70.632  27.246   0.461  1.00 97.83           C  
-ATOM   5766  N   PRO C 122      53.654  17.738 -11.185  1.00 89.09           N  
-ATOM   5767  CA  PRO C 122      53.627  17.682  -9.720  1.00 79.95           C  
-ATOM   5768  C   PRO C 122      54.954  17.263  -9.054  1.00 76.51           C  
-ATOM   5769  O   PRO C 122      55.673  16.370  -9.530  1.00 75.25           O  
-ATOM   5770  CB  PRO C 122      52.469  16.718  -9.432  1.00 75.50           C  
-ATOM   5771  CG  PRO C 122      52.471  15.816 -10.630  1.00 83.58           C  
-ATOM   5772  CD  PRO C 122      52.681  16.796 -11.766  1.00 90.83           C  
-ATOM   5773  N   TYR C 123      55.233  17.945  -7.944  1.00 67.63           N  
-ATOM   5774  CA  TYR C 123      56.406  17.828  -7.064  1.00 59.26           C  
-ATOM   5775  C   TYR C 123      56.392  16.612  -6.109  1.00 56.00           C  
-ATOM   5776  O   TYR C 123      55.349  16.254  -5.552  1.00 48.93           O  
-ATOM   5777  CB  TYR C 123      56.487  19.119  -6.245  1.00 57.81           C  
-ATOM   5778  CG  TYR C 123      55.109  19.657  -5.911  1.00 64.08           C  
-ATOM   5779  CD1 TYR C 123      54.097  18.795  -5.457  1.00 71.44           C  
-ATOM   5780  CD2 TYR C 123      54.794  21.007  -6.084  1.00 58.70           C  
-ATOM   5781  CE1 TYR C 123      52.800  19.254  -5.190  1.00 72.64           C  
-ATOM   5782  CE2 TYR C 123      53.492  21.482  -5.816  1.00 69.55           C  
-ATOM   5783  CZ  TYR C 123      52.501  20.593  -5.371  1.00 71.17           C  
-ATOM   5784  OH  TYR C 123      51.212  21.024  -5.122  1.00 64.16           O  
-ATOM   5785  N   LYS C 124      57.557  15.995  -5.905  1.00 54.27           N  
-ATOM   5786  CA  LYS C 124      57.656  14.828  -5.030  1.00 48.87           C  
-ATOM   5787  C   LYS C 124      57.568  15.239  -3.570  1.00 44.33           C  
-ATOM   5788  O   LYS C 124      58.355  16.054  -3.089  1.00 49.28           O  
-ATOM   5789  CB  LYS C 124      58.959  14.066  -5.303  1.00 46.96           C  
-ATOM   5790  CG  LYS C 124      58.992  13.404  -6.671  1.00 50.79           C  
-ATOM   5791  CD  LYS C 124      60.382  12.916  -7.044  1.00 56.82           C  
-ATOM   5792  CE  LYS C 124      60.369  12.211  -8.411  1.00 68.76           C  
-ATOM   5793  NZ  LYS C 124      59.870  13.065  -9.534  1.00 59.72           N  
-ATOM   5794  N   ILE C 125      56.591  14.669  -2.875  1.00 38.71           N  
-ATOM   5795  CA  ILE C 125      56.361  14.963  -1.469  1.00 34.41           C  
-ATOM   5796  C   ILE C 125      56.958  13.893  -0.567  1.00 30.18           C  
-ATOM   5797  O   ILE C 125      56.654  12.712  -0.719  1.00 33.35           O  
-ATOM   5798  CB  ILE C 125      54.833  15.086  -1.170  1.00 34.55           C  
-ATOM   5799  CG1 ILE C 125      54.508  14.443   0.177  1.00 42.11           C  
-ATOM   5800  CG2 ILE C 125      54.016  14.420  -2.259  1.00 34.20           C  
-ATOM   5801  CD1 ILE C 125      53.025  14.303   0.442  1.00 55.13           C  
-ATOM   5802  N   MET C 126      57.821  14.300   0.360  1.00 27.29           N  
-ATOM   5803  CA  MET C 126      58.412  13.345   1.299  1.00 32.42           C  
-ATOM   5804  C   MET C 126      57.841  13.633   2.701  1.00 30.99           C  
-ATOM   5805  O   MET C 126      58.186  14.603   3.381  1.00 32.68           O  
-ATOM   5806  CB  MET C 126      59.954  13.414   1.275  1.00 39.56           C  
-ATOM   5807  CG  MET C 126      60.553  14.645   1.901  1.00 53.11           C  
-ATOM   5808  SD  MET C 126      61.468  14.285   3.411  1.00 60.84           S  
-ATOM   5809  CE  MET C 126      63.166  14.588   2.757  1.00 60.50           C  
-ATOM   5810  N   LEU C 127      56.928  12.772   3.110  1.00 27.38           N  
-ATOM   5811  CA  LEU C 127      56.248  12.915   4.381  1.00 26.90           C  
-ATOM   5812  C   LEU C 127      57.067  12.343   5.526  1.00 28.62           C  
-ATOM   5813  O   LEU C 127      57.683  11.290   5.388  1.00 33.73           O  
-ATOM   5814  CB  LEU C 127      54.912  12.188   4.276  1.00 29.00           C  
-ATOM   5815  CG  LEU C 127      53.822  12.451   5.303  1.00 27.40           C  
-ATOM   5816  CD1 LEU C 127      53.460  13.936   5.326  1.00 23.29           C  
-ATOM   5817  CD2 LEU C 127      52.623  11.588   4.932  1.00 26.15           C  
-ATOM   5818  N   SER C 128      57.072  13.026   6.663  1.00 29.69           N  
-ATOM   5819  CA  SER C 128      57.817  12.534   7.826  1.00 32.45           C  
-ATOM   5820  C   SER C 128      56.959  12.530   9.086  1.00 30.68           C  
-ATOM   5821  O   SER C 128      56.116  13.406   9.278  1.00 33.97           O  
-ATOM   5822  CB  SER C 128      59.061  13.387   8.076  1.00 37.69           C  
-ATOM   5823  OG  SER C 128      59.608  13.115   9.360  1.00 35.44           O  
-ATOM   5824  N   ASP C 129      57.187  11.547   9.949  1.00 27.81           N  
-ATOM   5825  CA  ASP C 129      56.429  11.424  11.189  1.00 23.91           C  
-ATOM   5826  C   ASP C 129      57.139  12.169  12.308  1.00 18.88           C  
-ATOM   5827  O   ASP C 129      58.139  11.697  12.828  1.00 14.54           O  
-ATOM   5828  CB  ASP C 129      56.280   9.951  11.566  1.00 30.72           C  
-ATOM   5829  CG  ASP C 129      55.246   9.729  12.643  1.00 38.81           C  
-ATOM   5830  OD1 ASP C 129      55.004   8.551  13.003  1.00 44.93           O  
-ATOM   5831  OD2 ASP C 129      54.678  10.736  13.119  1.00 35.84           O  
-ATOM   5832  N   ARG C 130      56.601  13.328  12.672  1.00 17.20           N  
-ATOM   5833  CA  ARG C 130      57.169  14.173  13.718  1.00 13.18           C  
-ATOM   5834  C   ARG C 130      58.442  14.877  13.279  1.00 14.14           C  
-ATOM   5835  O   ARG C 130      59.228  14.325  12.513  1.00 14.59           O  
-ATOM   5836  CB  ARG C 130      57.444  13.366  14.986  1.00  8.60           C  
-ATOM   5837  CG  ARG C 130      56.210  13.158  15.839  1.00 15.25           C  
-ATOM   5838  CD  ARG C 130      56.570  12.787  17.262  1.00  8.10           C  
-ATOM   5839  NE  ARG C 130      55.561  13.292  18.183  1.00 16.13           N  
-ATOM   5840  CZ  ARG C 130      54.350  12.766  18.331  1.00 18.68           C  
-ATOM   5841  NH1 ARG C 130      53.993  11.711  17.621  1.00 22.68           N  
-ATOM   5842  NH2 ARG C 130      53.491  13.295  19.189  1.00 22.53           N  
-ATOM   5843  N   HIS C 131      58.622  16.108  13.758  1.00 11.35           N  
-ATOM   5844  CA  HIS C 131      59.791  16.919  13.441  1.00  8.64           C  
-ATOM   5845  C   HIS C 131      60.663  17.029  14.691  1.00 14.15           C  
-ATOM   5846  O   HIS C 131      60.141  17.128  15.804  1.00 21.72           O  
-ATOM   5847  CB  HIS C 131      59.353  18.311  12.993  1.00  6.50           C  
-ATOM   5848  CG  HIS C 131      60.493  19.196  12.606  1.00 11.14           C  
-ATOM   5849  ND1 HIS C 131      61.429  19.640  13.512  1.00 10.32           N  
-ATOM   5850  CD2 HIS C 131      60.875  19.679  11.402  1.00 15.75           C  
-ATOM   5851  CE1 HIS C 131      62.340  20.359  12.882  1.00 20.30           C  
-ATOM   5852  NE2 HIS C 131      62.028  20.397  11.600  1.00 18.08           N  
-ATOM   5853  N   PRO C 132      61.999  17.024  14.528  1.00 12.89           N  
-ATOM   5854  CA  PRO C 132      62.956  17.118  15.640  1.00 16.37           C  
-ATOM   5855  C   PRO C 132      62.558  18.006  16.819  1.00  9.86           C  
-ATOM   5856  O   PRO C 132      62.858  17.678  17.965  1.00  5.73           O  
-ATOM   5857  CB  PRO C 132      64.225  17.602  14.949  1.00 14.46           C  
-ATOM   5858  CG  PRO C 132      64.160  16.851  13.673  1.00  7.37           C  
-ATOM   5859  CD  PRO C 132      62.714  17.032  13.243  1.00  4.47           C  
-ATOM   5860  N   ILE C 133      61.884  19.119  16.543  1.00  4.47           N  
-ATOM   5861  CA  ILE C 133      61.471  20.021  17.606  1.00  6.29           C  
-ATOM   5862  C   ILE C 133      60.536  19.336  18.605  1.00  8.30           C  
-ATOM   5863  O   ILE C 133      60.330  19.826  19.722  1.00 12.56           O  
-ATOM   5864  CB  ILE C 133      60.783  21.294  17.045  1.00 12.49           C  
-ATOM   5865  CG1 ILE C 133      59.379  20.972  16.531  1.00 18.94           C  
-ATOM   5866  CG2 ILE C 133      61.626  21.886  15.925  1.00 10.33           C  
-ATOM   5867  CD1 ILE C 133      58.615  22.214  16.051  1.00  4.47           C  
-ATOM   5868  N   ALA C 134      59.971  18.201  18.212  1.00  4.47           N  
-ATOM   5869  CA  ALA C 134      59.098  17.477  19.120  1.00  5.36           C  
-ATOM   5870  C   ALA C 134      59.921  16.967  20.307  1.00 10.24           C  
-ATOM   5871  O   ALA C 134      59.480  17.053  21.453  1.00 10.60           O  
-ATOM   5872  CB  ALA C 134      58.438  16.323  18.410  1.00  4.47           C  
-ATOM   5873  N   SER C 135      61.119  16.449  20.032  1.00 13.31           N  
-ATOM   5874  CA  SER C 135      62.002  15.931  21.091  1.00  9.93           C  
-ATOM   5875  C   SER C 135      62.805  17.032  21.776  1.00  7.10           C  
-ATOM   5876  O   SER C 135      63.017  17.010  22.991  1.00  6.91           O  
-ATOM   5877  CB  SER C 135      63.003  14.919  20.528  1.00  6.62           C  
-ATOM   5878  OG  SER C 135      63.949  15.566  19.678  1.00 16.88           O  
-ATOM   5879  N   THR C 136      63.257  17.994  20.987  1.00  4.47           N  
-ATOM   5880  CA  THR C 136      64.067  19.076  21.519  1.00 11.69           C  
-ATOM   5881  C   THR C 136      63.301  20.268  22.059  1.00  8.95           C  
-ATOM   5882  O   THR C 136      63.900  21.146  22.680  1.00  6.08           O  
-ATOM   5883  CB  THR C 136      65.053  19.610  20.462  1.00 19.04           C  
-ATOM   5884  OG1 THR C 136      64.324  20.282  19.428  1.00 20.67           O  
-ATOM   5885  CG2 THR C 136      65.863  18.462  19.853  1.00 30.45           C  
-ATOM   5886  N   ILE C 137      61.995  20.334  21.820  1.00 10.95           N  
-ATOM   5887  CA  ILE C 137      61.257  21.478  22.329  1.00 11.48           C  
-ATOM   5888  C   ILE C 137      59.840  21.246  22.787  1.00  9.84           C  
-ATOM   5889  O   ILE C 137      59.479  21.689  23.870  1.00 23.62           O  
-ATOM   5890  CB  ILE C 137      61.307  22.691  21.344  1.00  8.72           C  
-ATOM   5891  CG1 ILE C 137      59.918  23.220  21.047  1.00  4.47           C  
-ATOM   5892  CG2 ILE C 137      62.019  22.321  20.074  1.00 19.53           C  
-ATOM   5893  CD1 ILE C 137      59.989  24.501  20.227  1.00 18.71           C  
-ATOM   5894  N   CYS C 138      59.024  20.552  22.019  1.00  5.10           N  
-ATOM   5895  CA  CYS C 138      57.664  20.359  22.497  1.00  9.43           C  
-ATOM   5896  C   CYS C 138      57.547  19.484  23.739  1.00  9.56           C  
-ATOM   5897  O   CYS C 138      57.052  19.953  24.756  1.00 11.55           O  
-ATOM   5898  CB  CYS C 138      56.786  19.837  21.376  1.00 14.22           C  
-ATOM   5899  SG  CYS C 138      56.587  21.101  20.122  1.00 33.62           S  
-ATOM   5900  N   PHE C 139      57.995  18.229  23.679  1.00 11.62           N  
-ATOM   5901  CA  PHE C 139      57.913  17.359  24.859  1.00 12.00           C  
-ATOM   5902  C   PHE C 139      58.726  17.868  26.060  1.00 13.90           C  
-ATOM   5903  O   PHE C 139      58.161  18.099  27.128  1.00 12.74           O  
-ATOM   5904  CB  PHE C 139      58.352  15.931  24.531  1.00 10.84           C  
-ATOM   5905  CG  PHE C 139      57.287  15.109  23.886  1.00 16.62           C  
-ATOM   5906  CD1 PHE C 139      56.883  15.370  22.590  1.00 18.41           C  
-ATOM   5907  CD2 PHE C 139      56.686  14.061  24.576  1.00 22.15           C  
-ATOM   5908  CE1 PHE C 139      55.898  14.598  21.989  1.00 19.71           C  
-ATOM   5909  CE2 PHE C 139      55.700  13.286  23.983  1.00 11.78           C  
-ATOM   5910  CZ  PHE C 139      55.307  13.552  22.693  1.00 12.67           C  
-ATOM   5911  N   PRO C 140      60.058  18.049  25.909  1.00 14.91           N  
-ATOM   5912  CA  PRO C 140      60.796  18.537  27.079  1.00  9.20           C  
-ATOM   5913  C   PRO C 140      60.084  19.692  27.781  1.00 11.46           C  
-ATOM   5914  O   PRO C 140      60.031  19.740  29.009  1.00 15.25           O  
-ATOM   5915  CB  PRO C 140      62.163  18.931  26.502  1.00  4.80           C  
-ATOM   5916  CG  PRO C 140      61.907  19.118  25.031  1.00  6.25           C  
-ATOM   5917  CD  PRO C 140      60.929  18.023  24.720  1.00 12.89           C  
-ATOM   5918  N   LEU C 141      59.506  20.603  27.006  1.00  7.34           N  
-ATOM   5919  CA  LEU C 141      58.804  21.747  27.584  1.00  7.44           C  
-ATOM   5920  C   LEU C 141      57.504  21.349  28.282  1.00  4.47           C  
-ATOM   5921  O   LEU C 141      57.087  21.957  29.263  1.00  6.02           O  
-ATOM   5922  CB  LEU C 141      58.511  22.771  26.500  1.00  4.47           C  
-ATOM   5923  CG  LEU C 141      59.053  24.167  26.731  1.00  4.47           C  
-ATOM   5924  CD1 LEU C 141      60.395  24.101  27.436  1.00  4.47           C  
-ATOM   5925  CD2 LEU C 141      59.170  24.868  25.384  1.00  5.43           C  
-ATOM   5926  N   SER C 142      56.843  20.331  27.775  1.00  4.47           N  
-ATOM   5927  CA  SER C 142      55.616  19.921  28.418  1.00  7.33           C  
-ATOM   5928  C   SER C 142      55.999  19.287  29.752  1.00  9.74           C  
-ATOM   5929  O   SER C 142      55.343  19.533  30.756  1.00 15.64           O  
-ATOM   5930  CB  SER C 142      54.851  18.917  27.544  1.00 11.71           C  
-ATOM   5931  OG  SER C 142      54.403  19.495  26.321  1.00  5.34           O  
-ATOM   5932  N   ARG C 143      57.064  18.484  29.766  1.00  6.56           N  
-ATOM   5933  CA  ARG C 143      57.499  17.835  31.001  1.00  7.31           C  
-ATOM   5934  C   ARG C 143      57.778  18.876  32.071  1.00 12.24           C  
-ATOM   5935  O   ARG C 143      57.418  18.707  33.243  1.00 10.43           O  
-ATOM   5936  CB  ARG C 143      58.761  16.999  30.779  1.00  4.47           C  
-ATOM   5937  CG  ARG C 143      58.538  15.757  29.950  1.00  4.47           C  
-ATOM   5938  CD  ARG C 143      57.621  14.747  30.625  1.00  4.54           C  
-ATOM   5939  NE  ARG C 143      57.313  13.640  29.724  1.00 16.36           N  
-ATOM   5940  CZ  ARG C 143      56.412  12.693  29.972  1.00 25.93           C  
-ATOM   5941  NH1 ARG C 143      55.719  12.707  31.110  1.00 22.26           N  
-ATOM   5942  NH2 ARG C 143      56.190  11.743  29.066  1.00 27.88           N  
-ATOM   5943  N   TYR C 144      58.433  19.957  31.670  1.00 14.63           N  
-ATOM   5944  CA  TYR C 144      58.732  21.016  32.619  1.00 19.67           C  
-ATOM   5945  C   TYR C 144      57.432  21.545  33.208  1.00 18.96           C  
-ATOM   5946  O   TYR C 144      57.195  21.465  34.416  1.00 23.91           O  
-ATOM   5947  CB  TYR C 144      59.494  22.168  31.946  1.00 18.39           C  
-ATOM   5948  CG  TYR C 144      59.584  23.411  32.812  1.00 16.27           C  
-ATOM   5949  CD1 TYR C 144      58.694  24.459  32.644  1.00 17.76           C  
-ATOM   5950  CD2 TYR C 144      60.522  23.508  33.842  1.00 22.43           C  
-ATOM   5951  CE1 TYR C 144      58.727  25.571  33.478  1.00 25.84           C  
-ATOM   5952  CE2 TYR C 144      60.562  24.619  34.683  1.00 24.57           C  
-ATOM   5953  CZ  TYR C 144      59.658  25.644  34.494  1.00 26.95           C  
-ATOM   5954  OH  TYR C 144      59.664  26.736  35.332  1.00 40.62           O  
-ATOM   5955  N   LEU C 145      56.587  22.081  32.339  1.00 15.29           N  
-ATOM   5956  CA  LEU C 145      55.314  22.638  32.761  1.00 15.70           C  
-ATOM   5957  C   LEU C 145      54.533  21.766  33.754  1.00 10.36           C  
-ATOM   5958  O   LEU C 145      53.957  22.275  34.711  1.00  8.66           O  
-ATOM   5959  CB  LEU C 145      54.465  22.935  31.524  1.00 10.61           C  
-ATOM   5960  CG  LEU C 145      55.113  23.944  30.574  1.00  9.98           C  
-ATOM   5961  CD1 LEU C 145      54.185  24.188  29.423  1.00 20.94           C  
-ATOM   5962  CD2 LEU C 145      55.389  25.251  31.288  1.00  8.09           C  
-ATOM   5963  N   VAL C 146      54.518  20.459  33.529  1.00  4.47           N  
-ATOM   5964  CA  VAL C 146      53.798  19.549  34.406  1.00  4.47           C  
-ATOM   5965  C   VAL C 146      54.571  19.280  35.679  1.00 10.71           C  
-ATOM   5966  O   VAL C 146      54.015  18.770  36.655  1.00 17.86           O  
-ATOM   5967  CB  VAL C 146      53.499  18.213  33.686  1.00  9.92           C  
-ATOM   5968  CG1 VAL C 146      53.429  17.068  34.673  1.00  6.24           C  
-ATOM   5969  CG2 VAL C 146      52.172  18.320  32.965  1.00 23.28           C  
-ATOM   5970  N   GLY C 147      55.858  19.617  35.669  1.00 10.85           N  
-ATOM   5971  CA  GLY C 147      56.679  19.413  36.848  1.00  8.24           C  
-ATOM   5972  C   GLY C 147      57.417  18.094  36.868  1.00 10.74           C  
-ATOM   5973  O   GLY C 147      57.984  17.727  37.892  1.00 16.56           O  
-ATOM   5974  N   ASP C 148      57.421  17.377  35.750  1.00  8.53           N  
-ATOM   5975  CA  ASP C 148      58.116  16.098  35.696  1.00 14.37           C  
-ATOM   5976  C   ASP C 148      59.590  16.226  35.323  1.00 14.39           C  
-ATOM   5977  O   ASP C 148      60.351  15.265  35.441  1.00 14.02           O  
-ATOM   5978  CB  ASP C 148      57.430  15.152  34.704  1.00 31.18           C  
-ATOM   5979  CG  ASP C 148      56.210  14.448  35.301  1.00 51.87           C  
-ATOM   5980  OD1 ASP C 148      56.236  14.141  36.517  1.00 63.48           O  
-ATOM   5981  OD2 ASP C 148      55.236  14.177  34.554  1.00 51.75           O  
-ATOM   5982  N   MET C 149      59.999  17.411  34.887  1.00 10.64           N  
-ATOM   5983  CA  MET C 149      61.383  17.620  34.488  1.00 16.10           C  
-ATOM   5984  C   MET C 149      61.935  18.972  34.953  1.00 28.30           C  
-ATOM   5985  O   MET C 149      61.198  19.956  34.999  1.00 33.53           O  
-ATOM   5986  CB  MET C 149      61.475  17.520  32.972  1.00 13.18           C  
-ATOM   5987  CG  MET C 149      62.837  17.855  32.423  1.00 13.30           C  
-ATOM   5988  SD  MET C 149      62.919  17.627  30.651  1.00 19.89           S  
-ATOM   5989  CE  MET C 149      62.804  15.866  30.542  1.00  8.18           C  
-ATOM   5990  N   SER C 150      63.228  19.023  35.285  1.00 33.75           N  
-ATOM   5991  CA  SER C 150      63.871  20.263  35.750  1.00 32.05           C  
-ATOM   5992  C   SER C 150      64.332  21.120  34.574  1.00 26.19           C  
-ATOM   5993  O   SER C 150      64.965  20.613  33.653  1.00 34.82           O  
-ATOM   5994  CB  SER C 150      65.077  19.936  36.645  1.00 41.90           C  
-ATOM   5995  OG  SER C 150      66.031  19.131  35.965  1.00 45.78           O  
-ATOM   5996  N   PRO C 151      64.051  22.436  34.610  1.00 18.84           N  
-ATOM   5997  CA  PRO C 151      64.423  23.391  33.550  1.00 15.80           C  
-ATOM   5998  C   PRO C 151      65.879  23.280  33.104  1.00 16.00           C  
-ATOM   5999  O   PRO C 151      66.223  23.568  31.954  1.00 17.05           O  
-ATOM   6000  CB  PRO C 151      64.117  24.749  34.180  1.00  4.47           C  
-ATOM   6001  CG  PRO C 151      64.390  24.504  35.614  1.00 19.84           C  
-ATOM   6002  CD  PRO C 151      63.719  23.159  35.847  1.00 22.80           C  
-ATOM   6003  N   ALA C 152      66.727  22.842  34.023  1.00 16.61           N  
-ATOM   6004  CA  ALA C 152      68.148  22.675  33.756  1.00 13.78           C  
-ATOM   6005  C   ALA C 152      68.482  22.054  32.386  1.00  7.94           C  
-ATOM   6006  O   ALA C 152      69.546  22.291  31.825  1.00 13.37           O  
-ATOM   6007  CB  ALA C 152      68.768  21.836  34.875  1.00 11.09           C  
-ATOM   6008  N   ALA C 153      67.580  21.272  31.829  1.00  4.47           N  
-ATOM   6009  CA  ALA C 153      67.886  20.639  30.564  1.00  8.34           C  
-ATOM   6010  C   ALA C 153      67.314  21.357  29.371  1.00 15.60           C  
-ATOM   6011  O   ALA C 153      67.420  20.855  28.258  1.00 27.14           O  
-ATOM   6012  CB  ALA C 153      67.402  19.199  30.570  1.00  7.50           C  
-ATOM   6013  N   LEU C 154      66.708  22.518  29.570  1.00 10.94           N  
-ATOM   6014  CA  LEU C 154      66.144  23.206  28.420  1.00 10.37           C  
-ATOM   6015  C   LEU C 154      67.185  23.841  27.499  1.00 13.99           C  
-ATOM   6016  O   LEU C 154      67.062  23.755  26.280  1.00 16.19           O  
-ATOM   6017  CB  LEU C 154      65.114  24.236  28.872  1.00  5.26           C  
-ATOM   6018  CG  LEU C 154      63.930  23.525  29.531  1.00  4.47           C  
-ATOM   6019  CD1 LEU C 154      62.948  24.533  30.079  1.00  9.96           C  
-ATOM   6020  CD2 LEU C 154      63.260  22.634  28.532  1.00  4.47           C  
-ATOM   6021  N   PRO C 155      68.243  24.454  28.061  1.00 14.59           N  
-ATOM   6022  CA  PRO C 155      69.273  25.085  27.223  1.00  6.95           C  
-ATOM   6023  C   PRO C 155      69.921  24.091  26.275  1.00  4.47           C  
-ATOM   6024  O   PRO C 155      70.161  24.365  25.101  1.00  4.47           O  
-ATOM   6025  CB  PRO C 155      70.264  25.620  28.243  1.00 10.68           C  
-ATOM   6026  CG  PRO C 155      69.397  25.897  29.437  1.00 16.06           C  
-ATOM   6027  CD  PRO C 155      68.542  24.654  29.487  1.00 12.19           C  
-ATOM   6028  N   GLY C 156      70.205  22.919  26.797  1.00  4.88           N  
-ATOM   6029  CA  GLY C 156      70.811  21.911  25.957  1.00 22.76           C  
-ATOM   6030  C   GLY C 156      69.953  21.481  24.780  1.00 24.27           C  
-ATOM   6031  O   GLY C 156      70.471  20.968  23.784  1.00 29.56           O  
-ATOM   6032  N   LEU C 157      68.643  21.682  24.875  1.00 25.35           N  
-ATOM   6033  CA  LEU C 157      67.764  21.274  23.784  1.00 27.66           C  
-ATOM   6034  C   LEU C 157      67.246  22.444  22.939  1.00 25.48           C  
-ATOM   6035  O   LEU C 157      67.232  22.373  21.711  1.00 29.95           O  
-ATOM   6036  CB  LEU C 157      66.565  20.482  24.327  1.00 20.92           C  
-ATOM   6037  CG  LEU C 157      66.798  19.422  25.393  1.00  9.82           C  
-ATOM   6038  CD1 LEU C 157      65.474  18.730  25.681  1.00  4.47           C  
-ATOM   6039  CD2 LEU C 157      67.876  18.442  24.929  1.00 11.26           C  
-ATOM   6040  N   LEU C 158      66.828  23.516  23.601  1.00 17.42           N  
-ATOM   6041  CA  LEU C 158      66.278  24.667  22.911  1.00 13.06           C  
-ATOM   6042  C   LEU C 158      67.281  25.576  22.253  1.00 21.18           C  
-ATOM   6043  O   LEU C 158      67.058  26.019  21.129  1.00 32.15           O  
-ATOM   6044  CB  LEU C 158      65.456  25.508  23.871  1.00 13.60           C  
-ATOM   6045  CG  LEU C 158      64.405  24.722  24.638  1.00 22.34           C  
-ATOM   6046  CD1 LEU C 158      63.559  25.675  25.500  1.00 26.82           C  
-ATOM   6047  CD2 LEU C 158      63.556  23.958  23.640  1.00  9.69           C  
-ATOM   6048  N   PHE C 159      68.382  25.862  22.942  1.00 19.02           N  
-ATOM   6049  CA  PHE C 159      69.383  26.778  22.406  1.00 13.12           C  
-ATOM   6050  C   PHE C 159      70.446  26.216  21.464  1.00 15.35           C  
-ATOM   6051  O   PHE C 159      71.178  26.975  20.844  1.00 16.29           O  
-ATOM   6052  CB  PHE C 159      70.058  27.512  23.554  1.00 10.13           C  
-ATOM   6053  CG  PHE C 159      69.090  28.138  24.526  1.00 15.79           C  
-ATOM   6054  CD1 PHE C 159      67.831  28.560  24.108  1.00 14.17           C  
-ATOM   6055  CD2 PHE C 159      69.457  28.350  25.855  1.00  8.18           C  
-ATOM   6056  CE1 PHE C 159      66.957  29.184  25.000  1.00  6.45           C  
-ATOM   6057  CE2 PHE C 159      68.590  28.974  26.746  1.00  4.47           C  
-ATOM   6058  CZ  PHE C 159      67.340  29.390  26.318  1.00  4.47           C  
-ATOM   6059  N   THR C 160      70.534  24.899  21.335  1.00 20.18           N  
-ATOM   6060  CA  THR C 160      71.526  24.313  20.437  1.00 19.70           C  
-ATOM   6061  C   THR C 160      70.932  23.843  19.113  1.00 22.74           C  
-ATOM   6062  O   THR C 160      71.531  23.025  18.420  1.00 26.01           O  
-ATOM   6063  CB  THR C 160      72.229  23.114  21.081  1.00 23.43           C  
-ATOM   6064  OG1 THR C 160      71.252  22.146  21.497  1.00 29.36           O  
-ATOM   6065  CG2 THR C 160      73.038  23.562  22.267  1.00 29.40           C  
-ATOM   6066  N   LEU C 161      69.763  24.357  18.750  1.00 20.65           N  
-ATOM   6067  CA  LEU C 161      69.141  23.945  17.498  1.00 15.15           C  
-ATOM   6068  C   LEU C 161      69.952  24.317  16.269  1.00 20.06           C  
-ATOM   6069  O   LEU C 161      70.534  25.400  16.186  1.00 30.47           O  
-ATOM   6070  CB  LEU C 161      67.746  24.546  17.371  1.00  7.28           C  
-ATOM   6071  CG  LEU C 161      66.738  23.915  18.314  1.00  6.95           C  
-ATOM   6072  CD1 LEU C 161      65.347  24.435  18.011  1.00  4.47           C  
-ATOM   6073  CD2 LEU C 161      66.800  22.398  18.143  1.00 13.43           C  
-ATOM   6074  N   PRO C 162      70.001  23.417  15.290  1.00 18.87           N  
-ATOM   6075  CA  PRO C 162      70.743  23.650  14.050  1.00 23.25           C  
-ATOM   6076  C   PRO C 162      69.909  24.415  13.020  1.00 20.99           C  
-ATOM   6077  O   PRO C 162      68.673  24.319  13.006  1.00 20.01           O  
-ATOM   6078  CB  PRO C 162      71.070  22.240  13.595  1.00 27.81           C  
-ATOM   6079  CG  PRO C 162      69.818  21.505  13.974  1.00 20.60           C  
-ATOM   6080  CD  PRO C 162      69.532  22.025  15.368  1.00 12.92           C  
-ATOM   6081  N   ALA C 163      70.594  25.160  12.157  1.00 18.46           N  
-ATOM   6082  CA  ALA C 163      69.935  25.950  11.122  1.00 24.28           C  
-ATOM   6083  C   ALA C 163      68.927  25.124  10.341  1.00 29.05           C  
-ATOM   6084  O   ALA C 163      69.285  24.110   9.729  1.00 28.04           O  
-ATOM   6085  CB  ALA C 163      70.968  26.523  10.174  1.00 26.09           C  
-ATOM   6086  N   GLU C 164      67.672  25.565  10.360  1.00 29.63           N  
-ATOM   6087  CA  GLU C 164      66.611  24.862   9.650  1.00 36.26           C  
-ATOM   6088  C   GLU C 164      66.607  25.311   8.196  1.00 43.16           C  
-ATOM   6089  O   GLU C 164      66.556  26.510   7.921  1.00 54.00           O  
-ATOM   6090  CB  GLU C 164      65.242  25.176  10.277  1.00 36.34           C  
-ATOM   6091  CG  GLU C 164      64.075  24.361   9.716  1.00 34.95           C  
-ATOM   6092  CD  GLU C 164      64.072  22.921  10.204  1.00 45.07           C  
-ATOM   6093  OE1 GLU C 164      65.063  22.490  10.837  1.00 54.29           O  
-ATOM   6094  OE2 GLU C 164      63.076  22.215   9.950  1.00 41.80           O  
-ATOM   6095  N   PRO C 165      66.682  24.361   7.245  1.00 44.96           N  
-ATOM   6096  CA  PRO C 165      66.676  24.684   5.811  1.00 44.82           C  
-ATOM   6097  C   PRO C 165      65.277  25.125   5.363  1.00 46.98           C  
-ATOM   6098  O   PRO C 165      64.264  24.606   5.844  1.00 46.23           O  
-ATOM   6099  CB  PRO C 165      67.122  23.377   5.160  1.00 43.93           C  
-ATOM   6100  CG  PRO C 165      66.583  22.346   6.089  1.00 45.93           C  
-ATOM   6101  CD  PRO C 165      66.926  22.924   7.451  1.00 46.74           C  
-ATOM   6102  N   PRO C 166      65.207  26.096   4.434  1.00 51.44           N  
-ATOM   6103  CA  PRO C 166      63.931  26.620   3.924  1.00 46.98           C  
-ATOM   6104  C   PRO C 166      62.997  25.545   3.397  1.00 37.36           C  
-ATOM   6105  O   PRO C 166      63.437  24.596   2.737  1.00 31.51           O  
-ATOM   6106  CB  PRO C 166      64.367  27.588   2.820  1.00 50.19           C  
-ATOM   6107  CG  PRO C 166      65.714  28.061   3.295  1.00 56.10           C  
-ATOM   6108  CD  PRO C 166      66.344  26.761   3.770  1.00 55.31           C  
-ATOM   6109  N   GLY C 167      61.711  25.690   3.700  1.00 29.54           N  
-ATOM   6110  CA  GLY C 167      60.751  24.723   3.205  1.00 29.20           C  
-ATOM   6111  C   GLY C 167      60.211  23.697   4.180  1.00 27.75           C  
-ATOM   6112  O   GLY C 167      59.727  22.644   3.764  1.00 23.29           O  
-ATOM   6113  N   THR C 168      60.285  23.984   5.473  1.00 26.63           N  
-ATOM   6114  CA  THR C 168      59.752  23.045   6.443  1.00 16.81           C  
-ATOM   6115  C   THR C 168      58.272  23.313   6.674  1.00 18.89           C  
-ATOM   6116  O   THR C 168      57.868  24.408   7.084  1.00 15.67           O  
-ATOM   6117  CB  THR C 168      60.457  23.153   7.777  1.00 13.23           C  
-ATOM   6118  OG1 THR C 168      61.855  22.898   7.598  1.00 13.69           O  
-ATOM   6119  CG2 THR C 168      59.865  22.142   8.749  1.00  7.15           C  
-ATOM   6120  N   ASN C 169      57.463  22.304   6.401  1.00 17.86           N  
-ATOM   6121  CA  ASN C 169      56.029  22.419   6.590  1.00 16.74           C  
-ATOM   6122  C   ASN C 169      55.622  21.600   7.808  1.00 17.45           C  
-ATOM   6123  O   ASN C 169      55.640  20.367   7.817  1.00  8.12           O  
-ATOM   6124  CB  ASN C 169      55.302  21.942   5.339  1.00 18.00           C  
-ATOM   6125  CG  ASN C 169      55.516  22.868   4.161  1.00 21.95           C  
-ATOM   6126  OD1 ASN C 169      54.957  23.967   4.117  1.00 28.51           O  
-ATOM   6127  ND2 ASN C 169      56.335  22.438   3.201  1.00 19.48           N  
-ATOM   6128  N   LEU C 170      55.273  22.314   8.858  1.00 19.35           N  
-ATOM   6129  CA  LEU C 170      54.884  21.665  10.082  1.00 23.74           C  
-ATOM   6130  C   LEU C 170      53.359  21.560  10.111  1.00 21.39           C  
-ATOM   6131  O   LEU C 170      52.637  22.569  10.078  1.00 19.03           O  
-ATOM   6132  CB  LEU C 170      55.414  22.479  11.271  1.00 21.93           C  
-ATOM   6133  CG  LEU C 170      55.816  21.734  12.545  1.00 18.84           C  
-ATOM   6134  CD1 LEU C 170      56.352  22.754  13.532  1.00 27.67           C  
-ATOM   6135  CD2 LEU C 170      54.623  20.988  13.140  1.00 14.99           C  
-ATOM   6136  N   VAL C 171      52.873  20.328  10.158  1.00 12.26           N  
-ATOM   6137  CA  VAL C 171      51.444  20.102  10.205  1.00 16.29           C  
-ATOM   6138  C   VAL C 171      51.060  19.547  11.565  1.00 15.30           C  
-ATOM   6139  O   VAL C 171      51.217  18.353  11.829  1.00 20.90           O  
-ATOM   6140  CB  VAL C 171      51.005  19.103   9.112  1.00 25.49           C  
-ATOM   6141  CG1 VAL C 171      49.475  18.929   9.126  1.00 13.94           C  
-ATOM   6142  CG2 VAL C 171      51.487  19.593   7.755  1.00 24.37           C  
-ATOM   6143  N   VAL C 172      50.563  20.422  12.430  1.00 10.71           N  
-ATOM   6144  CA  VAL C 172      50.141  20.012  13.764  1.00 13.73           C  
-ATOM   6145  C   VAL C 172      48.762  19.370  13.700  1.00 16.56           C  
-ATOM   6146  O   VAL C 172      47.795  20.024  13.316  1.00 19.05           O  
-ATOM   6147  CB  VAL C 172      50.035  21.216  14.724  1.00 13.50           C  
-ATOM   6148  CG1 VAL C 172      49.519  20.759  16.082  1.00  4.47           C  
-ATOM   6149  CG2 VAL C 172      51.384  21.897  14.854  1.00 12.17           C  
-ATOM   6150  N   CYS C 173      48.674  18.100  14.078  1.00 16.65           N  
-ATOM   6151  CA  CYS C 173      47.402  17.392  14.090  1.00 24.28           C  
-ATOM   6152  C   CYS C 173      46.648  17.723  15.381  1.00 30.69           C  
-ATOM   6153  O   CYS C 173      47.261  17.913  16.437  1.00 38.81           O  
-ATOM   6154  CB  CYS C 173      47.643  15.884  14.004  1.00 32.82           C  
-ATOM   6155  SG  CYS C 173      48.496  15.346  12.488  1.00 47.03           S  
-ATOM   6156  N   THR C 174      45.322  17.791  15.297  1.00 30.46           N  
-ATOM   6157  CA  THR C 174      44.497  18.110  16.459  1.00 32.58           C  
-ATOM   6158  C   THR C 174      43.272  17.222  16.512  1.00 36.60           C  
-ATOM   6159  O   THR C 174      42.720  16.859  15.482  1.00 41.10           O  
-ATOM   6160  CB  THR C 174      43.984  19.537  16.405  1.00 34.42           C  
-ATOM   6161  OG1 THR C 174      42.891  19.605  15.483  1.00 40.76           O  
-ATOM   6162  CG2 THR C 174      45.085  20.483  15.949  1.00 40.83           C  
-ATOM   6163  N   VAL C 175      42.835  16.897  17.720  1.00 41.96           N  
-ATOM   6164  CA  VAL C 175      41.669  16.047  17.914  1.00 47.98           C  
-ATOM   6165  C   VAL C 175      40.848  16.673  19.021  1.00 56.97           C  
-ATOM   6166  O   VAL C 175      41.379  17.448  19.808  1.00 63.48           O  
-ATOM   6167  CB  VAL C 175      42.078  14.637  18.378  1.00 47.19           C  
-ATOM   6168  CG1 VAL C 175      40.856  13.749  18.465  1.00 48.74           C  
-ATOM   6169  CG2 VAL C 175      43.102  14.049  17.432  1.00 48.00           C  
-ATOM   6170  N   SER C 176      39.559  16.356  19.088  1.00 64.58           N  
-ATOM   6171  CA  SER C 176      38.733  16.898  20.161  1.00 72.84           C  
-ATOM   6172  C   SER C 176      39.242  16.253  21.456  1.00 77.70           C  
-ATOM   6173  O   SER C 176      39.818  15.163  21.426  1.00 74.74           O  
-ATOM   6174  CB  SER C 176      37.253  16.566  19.937  1.00 71.35           C  
-ATOM   6175  OG  SER C 176      37.011  15.174  20.005  1.00 70.54           O  
-ATOM   6176  N   LEU C 177      39.035  16.923  22.586  1.00 84.03           N  
-ATOM   6177  CA  LEU C 177      39.518  16.415  23.869  1.00 89.73           C  
-ATOM   6178  C   LEU C 177      38.978  15.052  24.316  1.00 90.04           C  
-ATOM   6179  O   LEU C 177      39.755  14.133  24.570  1.00 91.72           O  
-ATOM   6180  CB  LEU C 177      39.283  17.460  24.973  1.00 93.13           C  
-ATOM   6181  CG  LEU C 177      39.727  17.100  26.397  1.00 93.78           C  
-ATOM   6182  CD1 LEU C 177      41.173  16.610  26.397  1.00 93.41           C  
-ATOM   6183  CD2 LEU C 177      39.567  18.324  27.293  1.00 96.23           C  
-ATOM   6184  N   PRO C 178      37.646  14.901  24.428  1.00 90.81           N  
-ATOM   6185  CA  PRO C 178      37.080  13.613  24.856  1.00 88.79           C  
-ATOM   6186  C   PRO C 178      37.440  12.429  23.951  1.00 85.18           C  
-ATOM   6187  O   PRO C 178      37.465  11.277  24.396  1.00 80.11           O  
-ATOM   6188  CB  PRO C 178      35.578  13.892  24.876  1.00 91.83           C  
-ATOM   6189  CG  PRO C 178      35.516  15.357  25.229  1.00 93.89           C  
-ATOM   6190  CD  PRO C 178      36.595  15.932  24.343  1.00 92.36           C  
-ATOM   6191  N   SER C 179      37.715  12.726  22.685  1.00 87.02           N  
-ATOM   6192  CA  SER C 179      38.069  11.712  21.694  1.00 87.85           C  
-ATOM   6193  C   SER C 179      39.530  11.303  21.845  1.00 88.83           C  
-ATOM   6194  O   SER C 179      39.890  10.143  21.647  1.00 89.52           O  
-ATOM   6195  CB  SER C 179      37.822  12.260  20.283  1.00 85.08           C  
-ATOM   6196  OG  SER C 179      38.184  11.324  19.285  1.00 81.90           O  
-ATOM   6197  N   HIS C 180      40.364  12.276  22.195  1.00 89.34           N  
-ATOM   6198  CA  HIS C 180      41.793  12.062  22.391  1.00 87.33           C  
-ATOM   6199  C   HIS C 180      42.010  11.108  23.569  1.00 86.75           C  
-ATOM   6200  O   HIS C 180      42.955  10.318  23.580  1.00 84.78           O  
-ATOM   6201  CB  HIS C 180      42.463  13.427  22.646  1.00 84.51           C  
-ATOM   6202  CG  HIS C 180      43.936  13.364  22.931  1.00 82.42           C  
-ATOM   6203  ND1 HIS C 180      44.720  14.496  23.003  1.00 76.91           N  
-ATOM   6204  CD2 HIS C 180      44.763  12.321  23.191  1.00 82.90           C  
-ATOM   6205  CE1 HIS C 180      45.963  14.154  23.294  1.00 74.32           C  
-ATOM   6206  NE2 HIS C 180      46.016  12.840  23.415  1.00 75.66           N  
-ATOM   6207  N   LEU C 181      41.110  11.168  24.545  1.00 87.63           N  
-ATOM   6208  CA  LEU C 181      41.212  10.331  25.736  1.00 87.22           C  
-ATOM   6209  C   LEU C 181      40.711   8.902  25.536  1.00 91.31           C  
-ATOM   6210  O   LEU C 181      40.599   8.133  26.493  1.00 92.48           O  
-ATOM   6211  CB  LEU C 181      40.466  10.996  26.896  1.00 76.47           C  
-ATOM   6212  CG  LEU C 181      40.806  12.480  27.070  1.00 65.09           C  
-ATOM   6213  CD1 LEU C 181      40.084  13.021  28.284  1.00 66.61           C  
-ATOM   6214  CD2 LEU C 181      42.310  12.669  27.202  1.00 49.37           C  
-ATOM   6215  N   SER C 182      40.414   8.550  24.290  1.00 93.06           N  
-ATOM   6216  CA  SER C 182      39.954   7.207  23.970  1.00 95.06           C  
-ATOM   6217  C   SER C 182      40.933   6.569  22.984  1.00 98.30           C  
-ATOM   6218  O   SER C 182      41.090   5.346  22.956  1.00103.30           O  
-ATOM   6219  CB  SER C 182      38.545   7.249  23.370  1.00 92.08           C  
-ATOM   6220  OG  SER C 182      38.537   7.922  22.126  1.00 90.92           O  
-ATOM   6221  N   ARG C 183      41.596   7.407  22.187  1.00 96.55           N  
-ATOM   6222  CA  ARG C 183      42.574   6.948  21.197  1.00 93.42           C  
-ATOM   6223  C   ARG C 183      43.770   6.311  21.898  1.00 92.54           C  
-ATOM   6224  O   ARG C 183      44.483   5.483  21.325  1.00 89.03           O  
-ATOM   6225  CB  ARG C 183      43.067   8.124  20.344  1.00 92.46           C  
-ATOM   6226  CG  ARG C 183      41.992   8.838  19.535  1.00 86.41           C  
-ATOM   6227  CD  ARG C 183      41.444   7.957  18.428  1.00 84.23           C  
-ATOM   6228  NE  ARG C 183      40.466   8.655  17.597  1.00 80.51           N  
-ATOM   6229  CZ  ARG C 183      40.751   9.682  16.803  1.00 73.90           C  
-ATOM   6230  NH1 ARG C 183      41.990  10.140  16.725  1.00 69.33           N  
-ATOM   6231  NH2 ARG C 183      39.795  10.251  16.083  1.00 74.94           N  
-ATOM   6232  N   VAL C 184      43.986   6.718  23.143  1.00 95.60           N  
-ATOM   6233  CA  VAL C 184      45.085   6.200  23.944  1.00 98.14           C  
-ATOM   6234  C   VAL C 184      44.610   4.950  24.702  1.00100.90           C  
-ATOM   6235  O   VAL C 184      44.926   3.818  24.316  1.00101.52           O  
-ATOM   6236  CB  VAL C 184      45.586   7.277  24.950  1.00 93.58           C  
-ATOM   6237  CG1 VAL C 184      46.906   6.839  25.581  1.00 92.66           C  
-ATOM   6238  CG2 VAL C 184      45.747   8.622  24.240  1.00 81.09           C  
-ATOM   6239  N   SER C 185      43.836   5.165  25.766  1.00 98.80           N  
-ATOM   6240  CA  SER C 185      43.305   4.079  26.583  1.00 96.98           C  
-ATOM   6241  C   SER C 185      42.469   3.124  25.736  1.00 98.81           C  
-ATOM   6242  O   SER C 185      42.926   2.044  25.361  1.00 97.66           O  
-ATOM   6243  CB  SER C 185      42.459   4.648  27.717  1.00 93.69           C  
-ATOM   6244  N   GLU C 192      53.113   3.428  28.346  1.00 92.33           N  
-ATOM   6245  CA  GLU C 192      52.376   4.684  28.259  1.00 96.74           C  
-ATOM   6246  C   GLU C 192      51.472   4.854  29.479  1.00100.61           C  
-ATOM   6247  O   GLU C 192      51.381   3.959  30.325  1.00102.69           O  
-ATOM   6248  CB  GLU C 192      51.547   4.725  26.968  1.00 90.39           C  
-ATOM   6249  N   THR C 193      50.813   6.008  29.564  1.00101.31           N  
-ATOM   6250  CA  THR C 193      49.912   6.323  30.674  1.00 98.37           C  
-ATOM   6251  C   THR C 193      48.979   7.480  30.303  1.00 96.58           C  
-ATOM   6252  O   THR C 193      49.401   8.449  29.668  1.00 98.11           O  
-ATOM   6253  CB  THR C 193      50.724   6.684  31.920  1.00 96.52           C  
-ATOM   6254  N   VAL C 194      47.714   7.378  30.706  1.00 92.50           N  
-ATOM   6255  CA  VAL C 194      46.729   8.415  30.406  1.00 83.98           C  
-ATOM   6256  C   VAL C 194      46.444   9.312  31.604  1.00 78.88           C  
-ATOM   6257  O   VAL C 194      45.670   8.946  32.495  1.00 78.77           O  
-ATOM   6258  CB  VAL C 194      45.428   7.777  29.918  1.00 79.47           C  
-ATOM   6259  N   ASN C 195      47.082  10.482  31.622  1.00 70.29           N  
-ATOM   6260  CA  ASN C 195      46.887  11.453  32.697  1.00 64.65           C  
-ATOM   6261  C   ASN C 195      46.637  12.817  32.094  1.00 57.58           C  
-ATOM   6262  O   ASN C 195      47.492  13.360  31.402  1.00 57.40           O  
-ATOM   6263  CB  ASN C 195      48.111  11.533  33.622  1.00 67.38           C  
-ATOM   6264  CG  ASN C 195      49.342  12.109  32.934  1.00 60.25           C  
-ATOM   6265  OD1 ASN C 195      50.233  12.664  33.589  1.00 48.99           O  
-ATOM   6266  ND2 ASN C 195      49.407  11.964  31.616  1.00 57.58           N  
-ATOM   6267  N   LEU C 196      45.462  13.370  32.363  1.00 53.05           N  
-ATOM   6268  CA  LEU C 196      45.104  14.672  31.824  1.00 54.70           C  
-ATOM   6269  C   LEU C 196      46.262  15.676  31.855  1.00 51.31           C  
-ATOM   6270  O   LEU C 196      46.757  16.101  30.802  1.00 51.60           O  
-ATOM   6271  CB  LEU C 196      43.908  15.245  32.585  1.00 59.18           C  
-ATOM   6272  CG  LEU C 196      42.577  14.504  32.476  1.00 63.82           C  
-ATOM   6273  CD1 LEU C 196      41.615  15.054  33.512  1.00 72.48           C  
-ATOM   6274  CD2 LEU C 196      42.005  14.665  31.076  1.00 63.46           C  
-ATOM   6275  N   PRO C 197      46.725  16.043  33.062  1.00 40.65           N  
-ATOM   6276  CA  PRO C 197      47.819  17.002  33.242  1.00 34.13           C  
-ATOM   6277  C   PRO C 197      48.826  17.088  32.097  1.00 31.26           C  
-ATOM   6278  O   PRO C 197      49.018  18.159  31.517  1.00 29.02           O  
-ATOM   6279  CB  PRO C 197      48.448  16.546  34.545  1.00 35.92           C  
-ATOM   6280  CG  PRO C 197      47.252  16.139  35.322  1.00 39.28           C  
-ATOM   6281  CD  PRO C 197      46.468  15.322  34.319  1.00 35.78           C  
-ATOM   6282  N   PHE C 198      49.458  15.969  31.759  1.00 25.21           N  
-ATOM   6283  CA  PHE C 198      50.445  15.980  30.687  1.00 23.80           C  
-ATOM   6284  C   PHE C 198      49.829  16.234  29.318  1.00 29.04           C  
-ATOM   6285  O   PHE C 198      50.326  17.056  28.556  1.00 36.19           O  
-ATOM   6286  CB  PHE C 198      51.220  14.669  30.649  1.00 19.82           C  
-ATOM   6287  CG  PHE C 198      52.418  14.719  29.764  1.00  9.18           C  
-ATOM   6288  CD1 PHE C 198      53.471  15.560  30.066  1.00 18.41           C  
-ATOM   6289  CD2 PHE C 198      52.484  13.958  28.619  1.00 18.56           C  
-ATOM   6290  CE1 PHE C 198      54.580  15.646  29.236  1.00 21.25           C  
-ATOM   6291  CE2 PHE C 198      53.588  14.034  27.781  1.00 28.47           C  
-ATOM   6292  CZ  PHE C 198      54.639  14.882  28.092  1.00 26.16           C  
-ATOM   6293  N   VAL C 199      48.758  15.513  29.002  1.00 27.72           N  
-ATOM   6294  CA  VAL C 199      48.067  15.675  27.730  1.00 20.08           C  
-ATOM   6295  C   VAL C 199      47.592  17.112  27.585  1.00 19.91           C  
-ATOM   6296  O   VAL C 199      47.996  17.821  26.664  1.00 19.70           O  
-ATOM   6297  CB  VAL C 199      46.868  14.738  27.661  1.00 19.18           C  
-ATOM   6298  CG1 VAL C 199      45.907  15.174  26.580  1.00 28.50           C  
-ATOM   6299  CG2 VAL C 199      47.357  13.336  27.391  1.00 28.58           C  
-ATOM   6300  N   MET C 200      46.744  17.542  28.511  1.00 17.78           N  
-ATOM   6301  CA  MET C 200      46.215  18.899  28.492  1.00 20.11           C  
-ATOM   6302  C   MET C 200      47.320  19.892  28.156  1.00 13.41           C  
-ATOM   6303  O   MET C 200      47.123  20.817  27.372  1.00 17.06           O  
-ATOM   6304  CB  MET C 200      45.612  19.244  29.857  1.00 25.00           C  
-ATOM   6305  CG  MET C 200      44.362  20.109  29.790  1.00 33.46           C  
-ATOM   6306  SD  MET C 200      43.031  19.307  28.885  1.00 38.50           S  
-ATOM   6307  CE  MET C 200      42.321  18.244  30.179  1.00 30.44           C  
-ATOM   6308  N   VAL C 201      48.488  19.685  28.748  1.00  7.86           N  
-ATOM   6309  CA  VAL C 201      49.621  20.564  28.512  1.00  8.18           C  
-ATOM   6310  C   VAL C 201      50.181  20.396  27.116  1.00  4.47           C  
-ATOM   6311  O   VAL C 201      50.334  21.359  26.378  1.00  4.47           O  
-ATOM   6312  CB  VAL C 201      50.742  20.301  29.527  1.00 10.34           C  
-ATOM   6313  CG1 VAL C 201      52.027  20.999  29.087  1.00 11.21           C  
-ATOM   6314  CG2 VAL C 201      50.310  20.797  30.901  1.00  4.47           C  
-ATOM   6315  N   LEU C 202      50.483  19.162  26.760  1.00  4.47           N  
-ATOM   6316  CA  LEU C 202      51.039  18.858  25.450  1.00 10.08           C  
-ATOM   6317  C   LEU C 202      50.227  19.548  24.360  1.00 18.94           C  
-ATOM   6318  O   LEU C 202      50.774  20.222  23.481  1.00 23.27           O  
-ATOM   6319  CB  LEU C 202      51.047  17.338  25.222  1.00 12.03           C  
-ATOM   6320  CG  LEU C 202      51.959  16.829  24.098  1.00 22.13           C  
-ATOM   6321  CD1 LEU C 202      53.361  17.444  24.242  1.00 24.81           C  
-ATOM   6322  CD2 LEU C 202      52.034  15.307  24.147  1.00 17.12           C  
-ATOM   6323  N   ARG C 203      48.914  19.377  24.425  1.00 20.24           N  
-ATOM   6324  CA  ARG C 203      48.025  19.985  23.456  1.00 17.49           C  
-ATOM   6325  C   ARG C 203      48.325  21.479  23.423  1.00 24.62           C  
-ATOM   6326  O   ARG C 203      48.630  22.040  22.361  1.00 30.32           O  
-ATOM   6327  CB  ARG C 203      46.581  19.733  23.880  1.00 12.71           C  
-ATOM   6328  CG  ARG C 203      46.340  18.287  24.277  1.00 33.22           C  
-ATOM   6329  CD  ARG C 203      44.925  18.027  24.789  1.00 47.26           C  
-ATOM   6330  NE  ARG C 203      44.059  17.424  23.777  1.00 47.22           N  
-ATOM   6331  CZ  ARG C 203      43.388  18.105  22.857  1.00 50.92           C  
-ATOM   6332  NH1 ARG C 203      43.466  19.427  22.809  1.00 55.94           N  
-ATOM   6333  NH2 ARG C 203      42.642  17.460  21.980  1.00 56.24           N  
-ATOM   6334  N   ASN C 204      48.254  22.108  24.600  1.00 24.85           N  
-ATOM   6335  CA  ASN C 204      48.505  23.545  24.749  1.00 21.08           C  
-ATOM   6336  C   ASN C 204      49.822  23.988  24.138  1.00 23.11           C  
-ATOM   6337  O   ASN C 204      49.853  24.907  23.308  1.00 22.32           O  
-ATOM   6338  CB  ASN C 204      48.466  23.942  26.225  1.00 12.68           C  
-ATOM   6339  CG  ASN C 204      47.058  24.185  26.716  1.00 20.17           C  
-ATOM   6340  OD1 ASN C 204      46.667  23.731  27.791  1.00 21.04           O  
-ATOM   6341  ND2 ASN C 204      46.284  24.918  25.927  1.00 28.82           N  
-ATOM   6342  N   VAL C 205      50.909  23.335  24.541  1.00 21.96           N  
-ATOM   6343  CA  VAL C 205      52.222  23.675  24.009  1.00 19.74           C  
-ATOM   6344  C   VAL C 205      52.216  23.703  22.482  1.00 20.13           C  
-ATOM   6345  O   VAL C 205      52.547  24.729  21.885  1.00 25.63           O  
-ATOM   6346  CB  VAL C 205      53.280  22.696  24.481  1.00 12.45           C  
-ATOM   6347  CG1 VAL C 205      54.636  23.072  23.904  1.00  6.28           C  
-ATOM   6348  CG2 VAL C 205      53.312  22.706  25.989  1.00 17.68           C  
-ATOM   6349  N   TYR C 206      51.837  22.598  21.846  1.00  6.72           N  
-ATOM   6350  CA  TYR C 206      51.802  22.587  20.393  1.00  9.31           C  
-ATOM   6351  C   TYR C 206      51.052  23.802  19.853  1.00 16.42           C  
-ATOM   6352  O   TYR C 206      51.508  24.451  18.905  1.00 27.02           O  
-ATOM   6353  CB  TYR C 206      51.181  21.293  19.874  1.00  4.47           C  
-ATOM   6354  CG  TYR C 206      52.228  20.267  19.548  1.00 10.15           C  
-ATOM   6355  CD1 TYR C 206      53.166  20.504  18.533  1.00 19.56           C  
-ATOM   6356  CD2 TYR C 206      52.327  19.080  20.277  1.00  9.24           C  
-ATOM   6357  CE1 TYR C 206      54.189  19.578  18.249  1.00 26.65           C  
-ATOM   6358  CE2 TYR C 206      53.340  18.152  20.008  1.00 17.12           C  
-ATOM   6359  CZ  TYR C 206      54.268  18.408  18.992  1.00 28.16           C  
-ATOM   6360  OH  TYR C 206      55.277  17.509  18.727  1.00 33.42           O  
-ATOM   6361  N   ILE C 207      49.913  24.132  20.447  1.00  7.42           N  
-ATOM   6362  CA  ILE C 207      49.206  25.295  19.974  1.00  7.08           C  
-ATOM   6363  C   ILE C 207      50.162  26.480  20.040  1.00 16.89           C  
-ATOM   6364  O   ILE C 207      50.351  27.188  19.040  1.00 22.00           O  
-ATOM   6365  CB  ILE C 207      47.970  25.561  20.815  1.00  7.38           C  
-ATOM   6366  CG1 ILE C 207      46.865  24.616  20.363  1.00  7.54           C  
-ATOM   6367  CG2 ILE C 207      47.536  27.019  20.678  1.00 11.37           C  
-ATOM   6368  CD1 ILE C 207      46.595  24.704  18.877  1.00 17.99           C  
-ATOM   6369  N   MET C 208      50.781  26.689  21.201  1.00  9.85           N  
-ATOM   6370  CA  MET C 208      51.727  27.789  21.340  1.00 11.77           C  
-ATOM   6371  C   MET C 208      52.751  27.752  20.217  1.00 13.09           C  
-ATOM   6372  O   MET C 208      52.949  28.744  19.512  1.00 14.01           O  
-ATOM   6373  CB  MET C 208      52.452  27.723  22.678  1.00 14.97           C  
-ATOM   6374  CG  MET C 208      51.630  28.243  23.833  1.00 30.63           C  
-ATOM   6375  SD  MET C 208      52.463  28.041  25.408  1.00 26.28           S  
-ATOM   6376  CE  MET C 208      51.971  26.340  25.813  1.00 20.63           C  
-ATOM   6377  N   LEU C 209      53.388  26.600  20.039  1.00 12.44           N  
-ATOM   6378  CA  LEU C 209      54.396  26.451  18.995  1.00 16.99           C  
-ATOM   6379  C   LEU C 209      53.919  27.198  17.771  1.00 23.36           C  
-ATOM   6380  O   LEU C 209      54.559  28.145  17.306  1.00 32.54           O  
-ATOM   6381  CB  LEU C 209      54.596  24.986  18.618  1.00 13.39           C  
-ATOM   6382  CG  LEU C 209      55.959  24.590  18.023  1.00 16.61           C  
-ATOM   6383  CD1 LEU C 209      55.841  23.186  17.402  1.00 15.00           C  
-ATOM   6384  CD2 LEU C 209      56.415  25.598  16.977  1.00 12.55           C  
-ATOM   6385  N   ILE C 210      52.782  26.771  17.249  1.00 17.78           N  
-ATOM   6386  CA  ILE C 210      52.238  27.429  16.080  1.00 19.76           C  
-ATOM   6387  C   ILE C 210      52.195  28.956  16.283  1.00 16.25           C  
-ATOM   6388  O   ILE C 210      52.813  29.717  15.516  1.00 12.69           O  
-ATOM   6389  CB  ILE C 210      50.831  26.871  15.761  1.00 16.66           C  
-ATOM   6390  CG1 ILE C 210      50.957  25.395  15.374  1.00 12.49           C  
-ATOM   6391  CG2 ILE C 210      50.179  27.665  14.633  1.00  7.33           C  
-ATOM   6392  CD1 ILE C 210      49.647  24.743  15.012  1.00 17.42           C  
-ATOM   6393  N   ASN C 211      51.501  29.412  17.321  1.00  4.47           N  
-ATOM   6394  CA  ASN C 211      51.421  30.844  17.528  1.00  6.47           C  
-ATOM   6395  C   ASN C 211      52.803  31.458  17.515  1.00  8.63           C  
-ATOM   6396  O   ASN C 211      52.981  32.571  17.038  1.00 15.54           O  
-ATOM   6397  CB  ASN C 211      50.722  31.184  18.845  1.00  5.18           C  
-ATOM   6398  CG  ASN C 211      49.240  30.870  18.817  1.00 16.18           C  
-ATOM   6399  OD1 ASN C 211      48.592  30.985  17.776  1.00 32.88           O  
-ATOM   6400  ND2 ASN C 211      48.689  30.490  19.967  1.00 18.32           N  
-ATOM   6401  N   THR C 212      53.786  30.722  18.021  1.00  8.62           N  
-ATOM   6402  CA  THR C 212      55.162  31.224  18.081  1.00 13.82           C  
-ATOM   6403  C   THR C 212      55.784  31.395  16.706  1.00 15.21           C  
-ATOM   6404  O   THR C 212      56.527  32.359  16.452  1.00  4.47           O  
-ATOM   6405  CB  THR C 212      56.084  30.278  18.858  1.00 10.78           C  
-ATOM   6406  OG1 THR C 212      55.540  30.036  20.162  1.00 19.46           O  
-ATOM   6407  CG2 THR C 212      57.472  30.894  18.976  1.00  4.47           C  
-ATOM   6408  N   ILE C 213      55.497  30.437  15.828  1.00 17.23           N  
-ATOM   6409  CA  ILE C 213      56.037  30.479  14.484  1.00 14.81           C  
-ATOM   6410  C   ILE C 213      55.481  31.706  13.792  1.00 12.81           C  
-ATOM   6411  O   ILE C 213      56.232  32.522  13.260  1.00 11.24           O  
-ATOM   6412  CB  ILE C 213      55.665  29.231  13.700  1.00 10.59           C  
-ATOM   6413  CG1 ILE C 213      56.002  27.984  14.527  1.00  4.47           C  
-ATOM   6414  CG2 ILE C 213      56.435  29.221  12.396  1.00 13.04           C  
-ATOM   6415  CD1 ILE C 213      55.720  26.690  13.833  1.00  7.65           C  
-ATOM   6416  N   ILE C 214      54.161  31.844  13.816  1.00 13.80           N  
-ATOM   6417  CA  ILE C 214      53.517  33.006  13.203  1.00 19.80           C  
-ATOM   6418  C   ILE C 214      54.096  34.293  13.796  1.00 19.11           C  
-ATOM   6419  O   ILE C 214      54.606  35.150  13.075  1.00 23.50           O  
-ATOM   6420  CB  ILE C 214      52.004  33.012  13.467  1.00 17.74           C  
-ATOM   6421  CG1 ILE C 214      51.390  31.696  12.984  1.00 14.47           C  
-ATOM   6422  CG2 ILE C 214      51.363  34.214  12.781  1.00  4.47           C  
-ATOM   6423  CD1 ILE C 214      49.943  31.521  13.410  1.00 17.91           C  
-ATOM   6424  N   PHE C 215      53.993  34.414  15.115  1.00 13.53           N  
-ATOM   6425  CA  PHE C 215      54.504  35.567  15.844  1.00 12.41           C  
-ATOM   6426  C   PHE C 215      55.898  35.944  15.345  1.00 19.99           C  
-ATOM   6427  O   PHE C 215      56.159  37.106  14.984  1.00 22.96           O  
-ATOM   6428  CB  PHE C 215      54.558  35.238  17.338  1.00  7.95           C  
-ATOM   6429  CG  PHE C 215      55.110  36.344  18.188  1.00 11.43           C  
-ATOM   6430  CD1 PHE C 215      56.484  36.542  18.296  1.00 17.12           C  
-ATOM   6431  CD2 PHE C 215      54.254  37.187  18.890  1.00 12.67           C  
-ATOM   6432  CE1 PHE C 215      56.996  37.566  19.096  1.00 22.50           C  
-ATOM   6433  CE2 PHE C 215      54.752  38.211  19.689  1.00 17.27           C  
-ATOM   6434  CZ  PHE C 215      56.125  38.402  19.794  1.00 24.81           C  
-ATOM   6435  N   LEU C 216      56.782  34.948  15.330  1.00 17.88           N  
-ATOM   6436  CA  LEU C 216      58.166  35.114  14.896  1.00 20.31           C  
-ATOM   6437  C   LEU C 216      58.316  35.628  13.457  1.00 25.24           C  
-ATOM   6438  O   LEU C 216      59.347  36.207  13.101  1.00 29.54           O  
-ATOM   6439  CB  LEU C 216      58.894  33.779  15.043  1.00 14.90           C  
-ATOM   6440  CG  LEU C 216      59.952  33.602  16.128  1.00 20.27           C  
-ATOM   6441  CD1 LEU C 216      59.660  34.475  17.337  1.00 21.38           C  
-ATOM   6442  CD2 LEU C 216      59.989  32.121  16.504  1.00 16.43           C  
-ATOM   6443  N   LYS C 217      57.292  35.408  12.635  1.00 25.10           N  
-ATOM   6444  CA  LYS C 217      57.316  35.837  11.240  1.00 22.60           C  
-ATOM   6445  C   LYS C 217      57.416  37.343  11.097  1.00 25.26           C  
-ATOM   6446  O   LYS C 217      58.057  37.848  10.171  1.00 21.97           O  
-ATOM   6447  CB  LYS C 217      56.059  35.354  10.520  1.00 17.53           C  
-ATOM   6448  CG  LYS C 217      56.122  33.918  10.039  1.00 17.30           C  
-ATOM   6449  CD  LYS C 217      57.214  33.755   8.985  1.00 25.55           C  
-ATOM   6450  CE  LYS C 217      57.103  32.425   8.265  1.00 31.74           C  
-ATOM   6451  NZ  LYS C 217      57.104  31.279   9.207  1.00 32.89           N  
-ATOM   6452  N   THR C 218      56.783  38.051  12.026  1.00 33.55           N  
-ATOM   6453  CA  THR C 218      56.768  39.508  12.008  1.00 39.64           C  
-ATOM   6454  C   THR C 218      57.671  40.169  13.051  1.00 40.53           C  
-ATOM   6455  O   THR C 218      58.533  40.990  12.701  1.00 43.22           O  
-ATOM   6456  CB  THR C 218      55.344  40.045  12.235  1.00 40.26           C  
-ATOM   6457  OG1 THR C 218      54.407  39.235  11.516  1.00 41.33           O  
-ATOM   6458  CG2 THR C 218      55.241  41.492  11.752  1.00 40.76           C  
-ATOM   6459  N   ASN C 219      57.471  39.809  14.320  1.00 33.21           N  
-ATOM   6460  CA  ASN C 219      58.235  40.405  15.413  1.00 32.64           C  
-ATOM   6461  C   ASN C 219      59.411  39.574  15.911  1.00 30.66           C  
-ATOM   6462  O   ASN C 219      59.510  38.384  15.628  1.00 25.64           O  
-ATOM   6463  CB  ASN C 219      57.301  40.683  16.587  1.00 38.08           C  
-ATOM   6464  CG  ASN C 219      55.863  40.823  16.158  1.00 48.73           C  
-ATOM   6465  OD1 ASN C 219      55.506  41.770  15.464  1.00 64.26           O  
-ATOM   6466  ND2 ASN C 219      55.026  39.873  16.563  1.00 47.97           N  
-ATOM   6467  N   ASN C 220      60.296  40.227  16.662  1.00 36.34           N  
-ATOM   6468  CA  ASN C 220      61.470  39.588  17.257  1.00 43.28           C  
-ATOM   6469  C   ASN C 220      61.060  39.011  18.625  1.00 43.38           C  
-ATOM   6470  O   ASN C 220      60.095  39.484  19.223  1.00 45.90           O  
-ATOM   6471  CB  ASN C 220      62.572  40.628  17.455  1.00 49.52           C  
-ATOM   6472  CG  ASN C 220      63.839  40.031  18.039  1.00 68.56           C  
-ATOM   6473  OD1 ASN C 220      64.483  40.641  18.905  1.00 78.61           O  
-ATOM   6474  ND2 ASN C 220      64.213  38.834  17.564  1.00 72.55           N  
-ATOM   6475  N   TRP C 221      61.776  38.006  19.132  1.00 41.48           N  
-ATOM   6476  CA  TRP C 221      61.399  37.433  20.427  1.00 37.49           C  
-ATOM   6477  C   TRP C 221      61.407  38.470  21.535  1.00 44.99           C  
-ATOM   6478  O   TRP C 221      60.634  38.365  22.482  1.00 47.89           O  
-ATOM   6479  CB  TRP C 221      62.316  36.277  20.834  1.00 26.50           C  
-ATOM   6480  CG  TRP C 221      63.726  36.669  21.205  1.00 21.39           C  
-ATOM   6481  CD1 TRP C 221      64.786  36.830  20.358  1.00 23.99           C  
-ATOM   6482  CD2 TRP C 221      64.230  36.913  22.523  1.00 14.34           C  
-ATOM   6483  NE1 TRP C 221      65.920  37.156  21.068  1.00 16.56           N  
-ATOM   6484  CE2 TRP C 221      65.607  37.214  22.398  1.00 11.24           C  
-ATOM   6485  CE3 TRP C 221      63.653  36.905  23.799  1.00 22.17           C  
-ATOM   6486  CZ2 TRP C 221      66.417  37.506  23.497  1.00 13.56           C  
-ATOM   6487  CZ3 TRP C 221      64.458  37.197  24.899  1.00 25.61           C  
-ATOM   6488  CH2 TRP C 221      65.830  37.494  24.736  1.00 21.15           C  
-ATOM   6489  N   HIS C 222      62.270  39.477  21.410  1.00 51.10           N  
-ATOM   6490  CA  HIS C 222      62.371  40.522  22.422  1.00 51.98           C  
-ATOM   6491  C   HIS C 222      61.241  41.546  22.328  1.00 50.79           C  
-ATOM   6492  O   HIS C 222      61.446  42.722  22.621  1.00 59.13           O  
-ATOM   6493  CB  HIS C 222      63.724  41.244  22.313  1.00 61.12           C  
-ATOM   6494  CG  HIS C 222      64.293  41.660  23.641  1.00 83.03           C  
-ATOM   6495  ND1 HIS C 222      63.520  42.204  24.648  1.00 86.88           N  
-ATOM   6496  CD2 HIS C 222      65.554  41.594  24.134  1.00 86.83           C  
-ATOM   6497  CE1 HIS C 222      64.278  42.450  25.702  1.00 83.73           C  
-ATOM   6498  NE2 HIS C 222      65.517  42.090  25.417  1.00 84.59           N  
-ATOM   6499  N   ALA C 223      60.050  41.111  21.921  1.00 47.18           N  
-ATOM   6500  CA  ALA C 223      58.914  42.029  21.805  1.00 41.86           C  
-ATOM   6501  C   ALA C 223      58.467  42.456  23.191  1.00 44.13           C  
-ATOM   6502  O   ALA C 223      59.204  43.129  23.920  1.00 44.74           O  
-ATOM   6503  CB  ALA C 223      57.756  41.361  21.079  1.00 28.69           C  
-ATOM   6504  N   GLY C 224      57.251  42.067  23.553  1.00 43.69           N  
-ATOM   6505  CA  GLY C 224      56.743  42.409  24.867  1.00 47.42           C  
-ATOM   6506  C   GLY C 224      57.365  41.525  25.937  1.00 49.58           C  
-ATOM   6507  O   GLY C 224      56.691  41.121  26.888  1.00 47.93           O  
-ATOM   6508  N   TRP C 225      58.651  41.210  25.780  1.00 49.61           N  
-ATOM   6509  CA  TRP C 225      59.351  40.366  26.745  1.00 40.25           C  
-ATOM   6510  C   TRP C 225      59.260  41.002  28.121  1.00 39.48           C  
-ATOM   6511  O   TRP C 225      58.928  40.336  29.097  1.00 43.85           O  
-ATOM   6512  CB  TRP C 225      60.818  40.185  26.337  1.00 33.40           C  
-ATOM   6513  CG  TRP C 225      61.621  39.355  27.288  1.00 28.78           C  
-ATOM   6514  CD1 TRP C 225      62.486  39.810  28.244  1.00 41.79           C  
-ATOM   6515  CD2 TRP C 225      61.626  37.927  27.391  1.00 22.94           C  
-ATOM   6516  NE1 TRP C 225      63.031  38.749  28.938  1.00 43.09           N  
-ATOM   6517  CE2 TRP C 225      62.520  37.583  28.435  1.00 32.06           C  
-ATOM   6518  CE3 TRP C 225      60.961  36.905  26.708  1.00 13.28           C  
-ATOM   6519  CZ2 TRP C 225      62.764  36.260  28.810  1.00 25.72           C  
-ATOM   6520  CZ3 TRP C 225      61.203  35.591  27.080  1.00 26.39           C  
-ATOM   6521  CH2 TRP C 225      62.099  35.281  28.125  1.00 29.54           C  
-ATOM   6522  N   ASN C 226      59.533  42.299  28.197  1.00 37.96           N  
-ATOM   6523  CA  ASN C 226      59.467  42.995  29.470  1.00 38.49           C  
-ATOM   6524  C   ASN C 226      58.021  43.272  29.893  1.00 36.99           C  
-ATOM   6525  O   ASN C 226      57.762  44.025  30.829  1.00 35.38           O  
-ATOM   6526  CB  ASN C 226      60.276  44.285  29.385  1.00 44.35           C  
-ATOM   6527  CG  ASN C 226      61.750  44.021  29.122  1.00 53.30           C  
-ATOM   6528  OD1 ASN C 226      62.433  43.376  29.922  1.00 59.96           O  
-ATOM   6529  ND2 ASN C 226      62.246  44.513  27.994  1.00 54.96           N  
-ATOM   6530  N   THR C 227      57.082  42.640  29.201  1.00 37.35           N  
-ATOM   6531  CA  THR C 227      55.663  42.791  29.508  1.00 38.32           C  
-ATOM   6532  C   THR C 227      55.111  41.385  29.748  1.00 36.00           C  
-ATOM   6533  O   THR C 227      53.926  41.187  30.045  1.00 38.03           O  
-ATOM   6534  CB  THR C 227      54.906  43.441  28.329  1.00 49.38           C  
-ATOM   6535  OG1 THR C 227      54.681  42.466  27.290  1.00 51.12           O  
-ATOM   6536  CG2 THR C 227      55.721  44.618  27.767  1.00 46.70           C  
-ATOM   6537  N   LEU C 228      55.996  40.409  29.600  1.00 27.15           N  
-ATOM   6538  CA  LEU C 228      55.651  39.019  29.796  1.00 24.08           C  
-ATOM   6539  C   LEU C 228      55.853  38.679  31.255  1.00 24.53           C  
-ATOM   6540  O   LEU C 228      56.970  38.750  31.767  1.00 16.31           O  
-ATOM   6541  CB  LEU C 228      56.569  38.133  28.968  1.00 22.61           C  
-ATOM   6542  CG  LEU C 228      55.953  37.367  27.813  1.00 23.51           C  
-ATOM   6543  CD1 LEU C 228      57.031  36.554  27.109  1.00 20.04           C  
-ATOM   6544  CD2 LEU C 228      54.843  36.481  28.343  1.00 22.69           C  
-ATOM   6545  N   SER C 229      54.781  38.323  31.943  1.00 26.70           N  
-ATOM   6546  CA  SER C 229      54.949  37.953  33.333  1.00 27.73           C  
-ATOM   6547  C   SER C 229      55.757  36.653  33.305  1.00 24.63           C  
-ATOM   6548  O   SER C 229      55.638  35.839  32.372  1.00 13.89           O  
-ATOM   6549  CB  SER C 229      53.588  37.745  34.014  1.00 33.33           C  
-ATOM   6550  OG  SER C 229      52.795  36.819  33.296  1.00 54.60           O  
-ATOM   6551  N   PHE C 230      56.603  36.470  34.308  1.00 24.30           N  
-ATOM   6552  CA  PHE C 230      57.400  35.261  34.368  1.00 20.52           C  
-ATOM   6553  C   PHE C 230      56.482  34.054  34.425  1.00 23.73           C  
-ATOM   6554  O   PHE C 230      55.281  34.193  34.641  1.00 37.36           O  
-ATOM   6555  CB  PHE C 230      58.290  35.282  35.600  1.00 19.35           C  
-ATOM   6556  CG  PHE C 230      59.495  36.148  35.453  1.00  7.90           C  
-ATOM   6557  CD1 PHE C 230      59.484  37.450  35.896  1.00 11.22           C  
-ATOM   6558  CD2 PHE C 230      60.642  35.653  34.852  1.00  4.47           C  
-ATOM   6559  CE1 PHE C 230      60.604  38.247  35.741  1.00 18.79           C  
-ATOM   6560  CE2 PHE C 230      61.760  36.439  34.694  1.00  4.47           C  
-ATOM   6561  CZ  PHE C 230      61.748  37.734  35.135  1.00  4.64           C  
-ATOM   6562  N   CYS C 231      57.039  32.867  34.234  1.00 18.86           N  
-ATOM   6563  CA  CYS C 231      56.228  31.662  34.285  1.00 19.40           C  
-ATOM   6564  C   CYS C 231      56.041  31.230  35.737  1.00 17.84           C  
-ATOM   6565  O   CYS C 231      57.002  30.914  36.425  1.00 24.75           O  
-ATOM   6566  CB  CYS C 231      56.898  30.551  33.490  1.00 21.33           C  
-ATOM   6567  SG  CYS C 231      55.924  29.055  33.451  1.00 39.13           S  
-ATOM   6568  N   ASN C 232      54.798  31.217  36.199  1.00 17.86           N  
-ATOM   6569  CA  ASN C 232      54.499  30.846  37.574  1.00 18.30           C  
-ATOM   6570  C   ASN C 232      53.665  29.576  37.661  1.00 26.07           C  
-ATOM   6571  O   ASN C 232      53.180  29.061  36.651  1.00 35.56           O  
-ATOM   6572  CB  ASN C 232      53.752  31.986  38.242  1.00 26.66           C  
-ATOM   6573  CG  ASN C 232      52.465  32.328  37.523  1.00 40.82           C  
-ATOM   6574  OD1 ASN C 232      51.533  31.530  37.501  1.00 50.03           O  
-ATOM   6575  ND2 ASN C 232      52.409  33.515  36.922  1.00 50.76           N  
-ATOM   6576  N   ASP C 233      53.489  29.078  38.878  1.00 29.28           N  
-ATOM   6577  CA  ASP C 233      52.715  27.861  39.103  1.00 33.61           C  
-ATOM   6578  C   ASP C 233      51.250  28.051  38.737  1.00 29.31           C  
-ATOM   6579  O   ASP C 233      50.571  27.098  38.353  1.00 34.94           O  
-ATOM   6580  CB  ASP C 233      52.823  27.418  40.568  1.00 48.61           C  
-ATOM   6581  CG  ASP C 233      54.249  27.087  40.982  1.00 56.00           C  
-ATOM   6582  OD1 ASP C 233      55.105  28.001  40.983  1.00 58.67           O  
-ATOM   6583  OD2 ASP C 233      54.511  25.908  41.307  1.00 62.44           O  
-ATOM   6584  N   VAL C 234      50.760  29.278  38.870  1.00 24.65           N  
-ATOM   6585  CA  VAL C 234      49.375  29.575  38.527  1.00 32.41           C  
-ATOM   6586  C   VAL C 234      49.199  29.313  37.036  1.00 36.21           C  
-ATOM   6587  O   VAL C 234      48.228  28.685  36.604  1.00 44.16           O  
-ATOM   6588  CB  VAL C 234      49.034  31.048  38.794  1.00 32.69           C  
-ATOM   6589  CG1 VAL C 234      47.567  31.311  38.463  1.00 33.63           C  
-ATOM   6590  CG2 VAL C 234      49.346  31.395  40.234  1.00 38.15           C  
-ATOM   6591  N   PHE C 235      50.153  29.809  36.257  1.00 31.27           N  
-ATOM   6592  CA  PHE C 235      50.138  29.645  34.819  1.00 21.14           C  
-ATOM   6593  C   PHE C 235      50.127  28.159  34.519  1.00 21.81           C  
-ATOM   6594  O   PHE C 235      49.225  27.657  33.840  1.00 25.85           O  
-ATOM   6595  CB  PHE C 235      51.384  30.287  34.213  1.00 22.96           C  
-ATOM   6596  CG  PHE C 235      51.416  30.265  32.708  1.00 34.64           C  
-ATOM   6597  CD1 PHE C 235      52.632  30.303  32.033  1.00 37.02           C  
-ATOM   6598  CD2 PHE C 235      50.240  30.216  31.961  1.00 38.98           C  
-ATOM   6599  CE1 PHE C 235      52.679  30.290  30.645  1.00 31.79           C  
-ATOM   6600  CE2 PHE C 235      50.277  30.203  30.566  1.00 28.97           C  
-ATOM   6601  CZ  PHE C 235      51.497  30.239  29.913  1.00 31.28           C  
-ATOM   6602  N   LYS C 236      51.123  27.450  35.042  1.00 16.63           N  
-ATOM   6603  CA  LYS C 236      51.219  26.014  34.806  1.00 21.05           C  
-ATOM   6604  C   LYS C 236      49.922  25.289  35.160  1.00 21.84           C  
-ATOM   6605  O   LYS C 236      49.522  24.343  34.483  1.00 21.70           O  
-ATOM   6606  CB  LYS C 236      52.376  25.416  35.603  1.00 14.99           C  
-ATOM   6607  CG  LYS C 236      53.747  25.959  35.247  1.00 18.60           C  
-ATOM   6608  CD  LYS C 236      54.829  25.197  36.003  1.00 26.96           C  
-ATOM   6609  CE  LYS C 236      56.196  25.854  35.884  1.00 35.49           C  
-ATOM   6610  NZ  LYS C 236      57.187  25.158  36.753  1.00 38.10           N  
-ATOM   6611  N   GLN C 237      49.268  25.735  36.226  1.00 22.85           N  
-ATOM   6612  CA  GLN C 237      48.014  25.130  36.642  1.00 31.22           C  
-ATOM   6613  C   GLN C 237      46.974  25.196  35.531  1.00 36.13           C  
-ATOM   6614  O   GLN C 237      46.340  24.191  35.225  1.00 44.78           O  
-ATOM   6615  CB  GLN C 237      47.465  25.824  37.891  1.00 37.42           C  
-ATOM   6616  CG  GLN C 237      48.161  25.421  39.166  1.00 44.16           C  
-ATOM   6617  CD  GLN C 237      48.103  23.931  39.377  1.00 54.47           C  
-ATOM   6618  OE1 GLN C 237      47.022  23.341  39.400  1.00 57.31           O  
-ATOM   6619  NE2 GLN C 237      49.265  23.308  39.526  1.00 62.24           N  
-ATOM   6620  N   LYS C 238      46.791  26.367  34.927  1.00 35.35           N  
-ATOM   6621  CA  LYS C 238      45.806  26.488  33.857  1.00 39.96           C  
-ATOM   6622  C   LYS C 238      46.155  25.536  32.716  1.00 38.68           C  
-ATOM   6623  O   LYS C 238      45.286  24.840  32.184  1.00 45.54           O  
-ATOM   6624  CB  LYS C 238      45.743  27.922  33.313  1.00 45.77           C  
-ATOM   6625  CG  LYS C 238      45.160  28.960  34.258  1.00 56.86           C  
-ATOM   6626  CD  LYS C 238      45.132  30.341  33.592  1.00 65.30           C  
-ATOM   6627  CE  LYS C 238      44.749  31.447  34.574  1.00 70.19           C  
-ATOM   6628  NZ  LYS C 238      44.863  32.809  33.973  1.00 65.92           N  
-ATOM   6629  N   LEU C 239      47.432  25.498  32.353  1.00 26.63           N  
-ATOM   6630  CA  LEU C 239      47.884  24.654  31.258  1.00 22.23           C  
-ATOM   6631  C   LEU C 239      47.606  23.162  31.446  1.00 28.48           C  
-ATOM   6632  O   LEU C 239      47.599  22.398  30.478  1.00 32.28           O  
-ATOM   6633  CB  LEU C 239      49.375  24.885  31.023  1.00 15.08           C  
-ATOM   6634  CG  LEU C 239      49.753  26.290  30.548  1.00 12.95           C  
-ATOM   6635  CD1 LEU C 239      51.263  26.407  30.393  1.00 14.26           C  
-ATOM   6636  CD2 LEU C 239      49.073  26.564  29.224  1.00 14.33           C  
-ATOM   6637  N   GLN C 240      47.375  22.748  32.688  1.00 27.61           N  
-ATOM   6638  CA  GLN C 240      47.098  21.348  32.988  1.00 27.19           C  
-ATOM   6639  C   GLN C 240      45.611  21.076  33.103  1.00 34.54           C  
-ATOM   6640  O   GLN C 240      45.204  19.926  33.228  1.00 39.21           O  
-ATOM   6641  CB  GLN C 240      47.758  20.949  34.306  1.00 26.01           C  
-ATOM   6642  CG  GLN C 240      49.268  20.890  34.248  1.00 36.51           C  
-ATOM   6643  CD  GLN C 240      49.925  20.788  35.619  1.00 34.15           C  
-ATOM   6644  OE1 GLN C 240      49.675  19.853  36.389  1.00 41.35           O  
-ATOM   6645  NE2 GLN C 240      50.781  21.751  35.922  1.00 25.13           N  
-ATOM   6646  N   LYS C 241      44.797  22.126  33.056  1.00 43.53           N  
-ATOM   6647  CA  LYS C 241      43.350  21.964  33.199  1.00 50.20           C  
-ATOM   6648  C   LYS C 241      42.424  22.385  32.048  1.00 54.30           C  
-ATOM   6649  O   LYS C 241      41.640  21.574  31.543  1.00 57.29           O  
-ATOM   6650  CB  LYS C 241      42.876  22.678  34.471  1.00 43.61           C  
-ATOM   6651  CG  LYS C 241      43.396  22.070  35.764  1.00 58.95           C  
-ATOM   6652  CD  LYS C 241      42.916  22.860  36.987  1.00 65.72           C  
-ATOM   6653  CE  LYS C 241      43.413  22.242  38.297  1.00 69.01           C  
-ATOM   6654  NZ  LYS C 241      42.895  20.853  38.507  1.00 72.34           N  
-ATOM   6655  N   SER C 242      42.514  23.640  31.625  1.00 52.71           N  
-ATOM   6656  CA  SER C 242      41.602  24.133  30.607  1.00 57.11           C  
-ATOM   6657  C   SER C 242      41.940  24.109  29.122  1.00 61.23           C  
-ATOM   6658  O   SER C 242      41.063  24.410  28.308  1.00 68.71           O  
-ATOM   6659  CB  SER C 242      41.154  25.555  30.984  1.00 63.36           C  
-ATOM   6660  OG  SER C 242      42.256  26.434  31.148  1.00 68.60           O  
-ATOM   6661  N   GLU C 243      43.160  23.753  28.734  1.00 58.23           N  
-ATOM   6662  CA  GLU C 243      43.466  23.777  27.300  1.00 60.84           C  
-ATOM   6663  C   GLU C 243      43.153  25.205  26.827  1.00 55.76           C  
-ATOM   6664  O   GLU C 243      42.531  25.413  25.783  1.00 51.31           O  
-ATOM   6665  CB  GLU C 243      42.568  22.789  26.533  1.00 70.26           C  
-ATOM   6666  CG  GLU C 243      42.775  22.779  25.010  1.00 80.27           C  
-ATOM   6667  CD  GLU C 243      41.548  22.303  24.240  1.00 84.14           C  
-ATOM   6668  OE1 GLU C 243      41.051  21.190  24.520  1.00 84.31           O  
-ATOM   6669  OE2 GLU C 243      41.084  23.047  23.349  1.00 85.56           O  
-ATOM   6670  N   CYS C 244      43.563  26.184  27.625  1.00 51.40           N  
-ATOM   6671  CA  CYS C 244      43.324  27.579  27.303  1.00 49.43           C  
-ATOM   6672  C   CYS C 244      43.982  27.973  25.989  1.00 49.33           C  
-ATOM   6673  O   CYS C 244      43.342  27.911  24.938  1.00 57.53           O  
-ATOM   6674  CB  CYS C 244      43.830  28.463  28.440  1.00 55.84           C  
-ATOM   6675  SG  CYS C 244      45.336  27.843  29.219  1.00 65.89           S  
-ATOM   6676  N   ILE C 245      45.252  28.369  26.051  1.00 41.96           N  
-ATOM   6677  CA  ILE C 245      46.013  28.784  24.869  1.00 39.00           C  
-ATOM   6678  C   ILE C 245      45.251  28.597  23.549  1.00 39.72           C  
-ATOM   6679  O   ILE C 245      45.187  27.491  22.999  1.00 34.65           O  
-ATOM   6680  CB  ILE C 245      47.346  28.009  24.768  1.00 35.12           C  
-ATOM   6681  CG1 ILE C 245      48.111  28.120  26.080  1.00 21.35           C  
-ATOM   6682  CG2 ILE C 245      48.190  28.568  23.617  1.00 41.76           C  
-ATOM   6683  CD1 ILE C 245      48.419  29.544  26.469  1.00 28.82           C  
-ATOM   6684  N   LYS C 246      44.673  29.679  23.041  1.00 38.77           N  
-ATOM   6685  CA  LYS C 246      43.930  29.589  21.801  1.00 40.98           C  
-ATOM   6686  C   LYS C 246      44.701  30.074  20.584  1.00 40.45           C  
-ATOM   6687  O   LYS C 246      45.372  31.106  20.616  1.00 43.56           O  
-ATOM   6688  CB  LYS C 246      42.600  30.333  21.936  1.00 41.45           C  
-ATOM   6689  CG  LYS C 246      41.565  29.531  22.714  1.00 52.02           C  
-ATOM   6690  CD  LYS C 246      40.273  30.304  22.935  1.00 66.36           C  
-ATOM   6691  CE  LYS C 246      39.302  29.495  23.788  1.00 76.68           C  
-ATOM   6692  NZ  LYS C 246      38.121  30.301  24.227  1.00 79.74           N  
-ATOM   6693  N   LEU C 247      44.605  29.292  19.514  1.00 37.79           N  
-ATOM   6694  CA  LEU C 247      45.261  29.586  18.251  1.00 33.15           C  
-ATOM   6695  C   LEU C 247      44.625  30.853  17.687  1.00 34.66           C  
-ATOM   6696  O   LEU C 247      43.406  30.901  17.494  1.00 35.81           O  
-ATOM   6697  CB  LEU C 247      45.044  28.404  17.313  1.00 26.53           C  
-ATOM   6698  CG  LEU C 247      45.984  28.237  16.127  1.00 35.07           C  
-ATOM   6699  CD1 LEU C 247      45.706  26.881  15.486  1.00 28.71           C  
-ATOM   6700  CD2 LEU C 247      45.803  29.394  15.126  1.00 50.66           C  
-ATOM   6701  N   ARG C 248      45.433  31.877  17.418  1.00 34.99           N  
-ATOM   6702  CA  ARG C 248      44.867  33.118  16.912  1.00 44.80           C  
-ATOM   6703  C   ARG C 248      45.568  33.834  15.757  1.00 49.89           C  
-ATOM   6704  O   ARG C 248      46.798  33.883  15.683  1.00 46.66           O  
-ATOM   6705  CB  ARG C 248      44.657  34.089  18.077  1.00 52.30           C  
-ATOM   6706  CG  ARG C 248      45.807  34.161  19.066  1.00 53.15           C  
-ATOM   6707  CD  ARG C 248      45.445  35.087  20.219  1.00 61.60           C  
-ATOM   6708  NE  ARG C 248      44.229  34.649  20.901  1.00 64.37           N  
-ATOM   6709  CZ  ARG C 248      43.613  35.349  21.848  1.00 71.68           C  
-ATOM   6710  NH1 ARG C 248      44.099  36.528  22.229  1.00 72.45           N  
-ATOM   6711  NH2 ARG C 248      42.507  34.871  22.411  1.00 69.46           N  
-ATOM   6712  N   GLU C 249      44.734  34.395  14.874  1.00 56.03           N  
-ATOM   6713  CA  GLU C 249      45.129  35.130  13.669  1.00 56.76           C  
-ATOM   6714  C   GLU C 249      46.441  35.895  13.801  1.00 53.25           C  
-ATOM   6715  O   GLU C 249      47.403  35.626  13.082  1.00 53.97           O  
-ATOM   6716  CB  GLU C 249      44.004  36.091  13.274  1.00 67.81           C  
-ATOM   6717  CG  GLU C 249      42.670  35.408  12.950  1.00 80.55           C  
-ATOM   6718  CD  GLU C 249      42.671  34.698  11.606  1.00 90.14           C  
-ATOM   6719  OE1 GLU C 249      43.494  33.776  11.410  1.00 93.05           O  
-ATOM   6720  OE2 GLU C 249      41.843  35.069  10.744  1.00 98.14           O  
-ATOM   6721  N   VAL C 250      46.468  36.879  14.688  1.00 52.79           N  
-ATOM   6722  CA  VAL C 250      47.695  37.626  14.915  1.00 58.11           C  
-ATOM   6723  C   VAL C 250      48.082  37.400  16.362  1.00 58.95           C  
-ATOM   6724  O   VAL C 250      47.555  38.032  17.285  1.00 62.27           O  
-ATOM   6725  CB  VAL C 250      47.546  39.129  14.645  1.00 58.03           C  
-ATOM   6726  CG1 VAL C 250      48.737  39.879  15.246  1.00 57.60           C  
-ATOM   6727  CG2 VAL C 250      47.506  39.375  13.145  1.00 57.20           C  
-ATOM   6728  N   PRO C 251      49.017  36.473  16.572  1.00 53.63           N  
-ATOM   6729  CA  PRO C 251      49.520  36.104  17.889  1.00 47.45           C  
-ATOM   6730  C   PRO C 251      50.298  37.220  18.566  1.00 44.01           C  
-ATOM   6731  O   PRO C 251      50.913  38.065  17.900  1.00 47.26           O  
-ATOM   6732  CB  PRO C 251      50.385  34.889  17.578  1.00 53.51           C  
-ATOM   6733  CG  PRO C 251      50.954  35.239  16.223  1.00 50.82           C  
-ATOM   6734  CD  PRO C 251      49.749  35.764  15.504  1.00 50.15           C  
-ATOM   6735  N   GLY C 252      50.252  37.217  19.894  1.00 35.42           N  
-ATOM   6736  CA  GLY C 252      50.970  38.205  20.677  1.00 34.63           C  
-ATOM   6737  C   GLY C 252      51.952  37.450  21.540  1.00 30.67           C  
-ATOM   6738  O   GLY C 252      51.762  36.248  21.757  1.00 33.19           O  
-ATOM   6739  N   ILE C 253      52.983  38.130  22.040  1.00 24.05           N  
-ATOM   6740  CA  ILE C 253      53.996  37.465  22.862  1.00 23.65           C  
-ATOM   6741  C   ILE C 253      53.432  36.450  23.871  1.00 25.33           C  
-ATOM   6742  O   ILE C 253      53.982  35.358  24.019  1.00 25.83           O  
-ATOM   6743  CB  ILE C 253      54.876  38.497  23.616  1.00 15.09           C  
-ATOM   6744  CG1 ILE C 253      56.364  38.196  23.396  1.00  4.47           C  
-ATOM   6745  CG2 ILE C 253      54.559  38.474  25.086  1.00 11.15           C  
-ATOM   6746  CD1 ILE C 253      56.781  36.819  23.802  1.00  4.47           C  
-ATOM   6747  N   GLU C 254      52.330  36.792  24.540  1.00 23.98           N  
-ATOM   6748  CA  GLU C 254      51.740  35.893  25.535  1.00 27.43           C  
-ATOM   6749  C   GLU C 254      50.990  34.677  25.009  1.00 29.60           C  
-ATOM   6750  O   GLU C 254      50.503  33.865  25.804  1.00 30.00           O  
-ATOM   6751  CB  GLU C 254      50.804  36.659  26.479  1.00 35.32           C  
-ATOM   6752  CG  GLU C 254      49.718  37.475  25.799  1.00 47.78           C  
-ATOM   6753  CD  GLU C 254      50.198  38.857  25.385  1.00 60.19           C  
-ATOM   6754  OE1 GLU C 254      50.600  39.640  26.277  1.00 62.83           O  
-ATOM   6755  OE2 GLU C 254      50.172  39.163  24.173  1.00 65.13           O  
-ATOM   6756  N   ASP C 255      50.882  34.543  23.691  1.00 29.64           N  
-ATOM   6757  CA  ASP C 255      50.172  33.404  23.122  1.00 26.99           C  
-ATOM   6758  C   ASP C 255      51.170  32.402  22.593  1.00 22.50           C  
-ATOM   6759  O   ASP C 255      50.783  31.346  22.106  1.00 19.13           O  
-ATOM   6760  CB  ASP C 255      49.252  33.856  21.987  1.00 40.22           C  
-ATOM   6761  CG  ASP C 255      48.158  34.809  22.458  1.00 54.73           C  
-ATOM   6762  OD1 ASP C 255      47.358  34.397  23.335  1.00 57.15           O  
-ATOM   6763  OD2 ASP C 255      48.098  35.960  21.947  1.00 49.39           O  
-ATOM   6764  N   THR C 256      52.453  32.736  22.721  1.00 19.35           N  
-ATOM   6765  CA  THR C 256      53.542  31.897  22.227  1.00 17.59           C  
-ATOM   6766  C   THR C 256      54.179  30.972  23.249  1.00 19.71           C  
-ATOM   6767  O   THR C 256      53.601  30.672  24.289  1.00 22.93           O  
-ATOM   6768  CB  THR C 256      54.657  32.756  21.675  1.00 12.45           C  
-ATOM   6769  OG1 THR C 256      55.362  33.372  22.760  1.00 13.91           O  
-ATOM   6770  CG2 THR C 256      54.082  33.833  20.794  1.00 27.60           C  
-ATOM   6771  N   LEU C 257      55.389  30.525  22.922  1.00 21.20           N  
-ATOM   6772  CA  LEU C 257      56.173  29.650  23.785  1.00 16.55           C  
-ATOM   6773  C   LEU C 257      57.064  30.514  24.656  1.00 11.86           C  
-ATOM   6774  O   LEU C 257      57.560  30.087  25.694  1.00 15.02           O  
-ATOM   6775  CB  LEU C 257      57.052  28.716  22.956  1.00 10.13           C  
-ATOM   6776  CG  LEU C 257      56.360  27.549  22.258  1.00 16.47           C  
-ATOM   6777  CD1 LEU C 257      57.406  26.756  21.480  1.00 13.81           C  
-ATOM   6778  CD2 LEU C 257      55.656  26.659  23.286  1.00  6.83           C  
-ATOM   6779  N   PHE C 258      57.274  31.741  24.221  1.00  6.29           N  
-ATOM   6780  CA  PHE C 258      58.100  32.640  24.979  1.00  7.28           C  
-ATOM   6781  C   PHE C 258      57.453  32.908  26.327  1.00  7.45           C  
-ATOM   6782  O   PHE C 258      58.103  33.338  27.277  1.00  4.58           O  
-ATOM   6783  CB  PHE C 258      58.296  33.909  24.174  1.00  7.39           C  
-ATOM   6784  CG  PHE C 258      59.193  33.718  22.996  1.00 10.13           C  
-ATOM   6785  CD1 PHE C 258      60.541  33.419  23.182  1.00 18.44           C  
-ATOM   6786  CD2 PHE C 258      58.702  33.808  21.710  1.00  4.47           C  
-ATOM   6787  CE1 PHE C 258      61.385  33.214  22.095  1.00 17.90           C  
-ATOM   6788  CE2 PHE C 258      59.539  33.603  20.617  1.00  8.61           C  
-ATOM   6789  CZ  PHE C 258      60.879  33.307  20.806  1.00  8.98           C  
-ATOM   6790  N   ALA C 259      56.163  32.617  26.409  1.00 13.83           N  
-ATOM   6791  CA  ALA C 259      55.417  32.815  27.645  1.00 20.03           C  
-ATOM   6792  C   ALA C 259      55.868  31.775  28.642  1.00 18.47           C  
-ATOM   6793  O   ALA C 259      55.746  31.969  29.852  1.00 26.37           O  
-ATOM   6794  CB  ALA C 259      53.927  32.663  27.392  1.00 26.52           C  
-ATOM   6795  N   VAL C 260      56.377  30.670  28.110  1.00  8.96           N  
-ATOM   6796  CA  VAL C 260      56.854  29.565  28.916  1.00 11.54           C  
-ATOM   6797  C   VAL C 260      58.366  29.608  29.060  1.00 11.96           C  
-ATOM   6798  O   VAL C 260      58.930  28.885  29.869  1.00 17.62           O  
-ATOM   6799  CB  VAL C 260      56.438  28.218  28.282  1.00 17.74           C  
-ATOM   6800  CG1 VAL C 260      57.136  27.053  28.962  1.00 20.88           C  
-ATOM   6801  CG2 VAL C 260      54.947  28.046  28.407  1.00 21.87           C  
-ATOM   6802  N   LEU C 261      59.034  30.457  28.291  1.00  9.11           N  
-ATOM   6803  CA  LEU C 261      60.486  30.519  28.389  1.00 10.70           C  
-ATOM   6804  C   LEU C 261      61.012  31.601  29.310  1.00 14.42           C  
-ATOM   6805  O   LEU C 261      62.190  31.575  29.690  1.00 19.06           O  
-ATOM   6806  CB  LEU C 261      61.103  30.648  27.002  1.00 10.37           C  
-ATOM   6807  CG  LEU C 261      60.994  29.301  26.273  1.00 10.85           C  
-ATOM   6808  CD1 LEU C 261      61.428  29.440  24.833  1.00 11.31           C  
-ATOM   6809  CD2 LEU C 261      61.840  28.259  26.996  1.00  5.99           C  
-ATOM   6810  N   LYS C 262      60.145  32.544  29.675  1.00 13.44           N  
-ATOM   6811  CA  LYS C 262      60.519  33.620  30.597  1.00 15.03           C  
-ATOM   6812  C   LYS C 262      60.644  32.967  31.981  1.00 17.18           C  
-ATOM   6813  O   LYS C 262      59.699  32.970  32.777  1.00 16.28           O  
-ATOM   6814  CB  LYS C 262      59.432  34.696  30.618  1.00 21.76           C  
-ATOM   6815  CG  LYS C 262      59.590  35.756  31.691  1.00 21.28           C  
-ATOM   6816  CD  LYS C 262      60.636  36.764  31.303  1.00 28.49           C  
-ATOM   6817  CE  LYS C 262      60.009  38.070  30.821  1.00 35.45           C  
-ATOM   6818  NZ  LYS C 262      59.425  38.907  31.919  1.00 35.05           N  
-ATOM   6819  N   LEU C 263      61.813  32.399  32.261  1.00  9.01           N  
-ATOM   6820  CA  LEU C 263      62.024  31.726  33.524  1.00  4.47           C  
-ATOM   6821  C   LEU C 263      63.105  32.371  34.364  1.00  6.80           C  
-ATOM   6822  O   LEU C 263      64.181  32.668  33.870  1.00 18.06           O  
-ATOM   6823  CB  LEU C 263      62.396  30.273  33.264  1.00  9.06           C  
-ATOM   6824  CG  LEU C 263      61.417  29.456  32.424  1.00  4.61           C  
-ATOM   6825  CD1 LEU C 263      61.933  28.024  32.265  1.00  4.47           C  
-ATOM   6826  CD2 LEU C 263      60.049  29.471  33.094  1.00  8.39           C  
-ATOM   6827  N   PRO C 264      62.841  32.569  35.659  1.00  4.47           N  
-ATOM   6828  CA  PRO C 264      63.787  33.180  36.595  1.00  4.47           C  
-ATOM   6829  C   PRO C 264      65.131  32.476  36.550  1.00  4.47           C  
-ATOM   6830  O   PRO C 264      66.164  33.094  36.762  1.00  5.70           O  
-ATOM   6831  CB  PRO C 264      63.112  32.985  37.944  1.00  4.47           C  
-ATOM   6832  CG  PRO C 264      61.654  32.953  37.606  1.00  4.47           C  
-ATOM   6833  CD  PRO C 264      61.618  32.132  36.353  1.00  5.27           C  
-ATOM   6834  N   GLU C 265      65.098  31.174  36.277  1.00  5.91           N  
-ATOM   6835  CA  GLU C 265      66.303  30.363  36.226  1.00 11.02           C  
-ATOM   6836  C   GLU C 265      67.171  30.725  35.040  1.00 16.45           C  
-ATOM   6837  O   GLU C 265      68.313  30.281  34.952  1.00 31.92           O  
-ATOM   6838  CB  GLU C 265      65.947  28.869  36.165  1.00 11.14           C  
-ATOM   6839  CG  GLU C 265      65.110  28.370  37.341  1.00 19.55           C  
-ATOM   6840  CD  GLU C 265      63.612  28.463  37.086  1.00 31.15           C  
-ATOM   6841  OE1 GLU C 265      63.147  29.478  36.520  1.00 24.21           O  
-ATOM   6842  OE2 GLU C 265      62.894  27.514  37.466  1.00 45.56           O  
-ATOM   6843  N   LEU C 266      66.634  31.523  34.123  1.00  7.95           N  
-ATOM   6844  CA  LEU C 266      67.390  31.923  32.943  1.00 16.01           C  
-ATOM   6845  C   LEU C 266      67.772  33.393  33.007  1.00 24.07           C  
-ATOM   6846  O   LEU C 266      68.570  33.872  32.199  1.00 33.22           O  
-ATOM   6847  CB  LEU C 266      66.579  31.672  31.669  1.00  8.16           C  
-ATOM   6848  CG  LEU C 266      66.218  30.222  31.357  1.00 15.17           C  
-ATOM   6849  CD1 LEU C 266      65.212  30.200  30.216  1.00 10.28           C  
-ATOM   6850  CD2 LEU C 266      67.479  29.424  31.019  1.00  4.47           C  
-ATOM   6851  N   CYS C 267      67.200  34.107  33.969  1.00 22.73           N  
-ATOM   6852  CA  CYS C 267      67.458  35.533  34.122  1.00 19.76           C  
-ATOM   6853  C   CYS C 267      68.366  35.790  35.312  1.00 26.28           C  
-ATOM   6854  O   CYS C 267      68.531  34.929  36.163  1.00 38.63           O  
-ATOM   6855  CB  CYS C 267      66.147  36.284  34.328  1.00 25.77           C  
-ATOM   6856  SG  CYS C 267      64.901  36.049  33.045  1.00 42.19           S  
-ATOM   6857  N   GLY C 268      68.948  36.980  35.375  1.00 28.01           N  
-ATOM   6858  CA  GLY C 268      69.835  37.307  36.470  1.00 28.27           C  
-ATOM   6859  C   GLY C 268      69.145  38.081  37.571  1.00 41.14           C  
-ATOM   6860  O   GLY C 268      67.922  38.129  37.654  1.00 45.73           O  
-ATOM   6861  N   GLU C 269      69.954  38.693  38.423  1.00 50.22           N  
-ATOM   6862  CA  GLU C 269      69.477  39.480  39.549  1.00 52.32           C  
-ATOM   6863  C   GLU C 269      68.398  40.468  39.134  1.00 57.30           C  
-ATOM   6864  O   GLU C 269      67.253  40.378  39.570  1.00 55.31           O  
-ATOM   6865  CB  GLU C 269      70.659  40.235  40.160  1.00 56.99           C  
-ATOM   6866  CG  GLU C 269      70.361  41.008  41.417  1.00 67.27           C  
-ATOM   6867  CD  GLU C 269      71.535  41.868  41.851  1.00 77.16           C  
-ATOM   6868  OE1 GLU C 269      72.666  41.344  41.932  1.00 75.88           O  
-ATOM   6869  OE2 GLU C 269      71.327  43.069  42.119  1.00 86.27           O  
-ATOM   6870  N   PHE C 270      68.780  41.404  38.273  1.00 63.64           N  
-ATOM   6871  CA  PHE C 270      67.887  42.452  37.807  1.00 62.73           C  
-ATOM   6872  C   PHE C 270      66.685  41.924  37.051  1.00 56.06           C  
-ATOM   6873  O   PHE C 270      65.735  42.660  36.820  1.00 58.88           O  
-ATOM   6874  CB  PHE C 270      68.663  43.429  36.922  1.00 77.48           C  
-ATOM   6875  CG  PHE C 270      69.931  43.945  37.549  1.00 87.02           C  
-ATOM   6876  CD1 PHE C 270      70.938  44.489  36.754  1.00 95.72           C  
-ATOM   6877  CD2 PHE C 270      70.131  43.869  38.923  1.00 83.32           C  
-ATOM   6878  CE1 PHE C 270      72.128  44.943  37.319  1.00 98.78           C  
-ATOM   6879  CE2 PHE C 270      71.313  44.319  39.494  1.00 89.07           C  
-ATOM   6880  CZ  PHE C 270      72.316  44.856  38.692  1.00 96.20           C  
-ATOM   6881  N   GLY C 271      66.722  40.657  36.660  1.00 50.63           N  
-ATOM   6882  CA  GLY C 271      65.600  40.093  35.930  1.00 49.91           C  
-ATOM   6883  C   GLY C 271      65.755  40.136  34.419  1.00 50.59           C  
-ATOM   6884  O   GLY C 271      64.764  40.192  33.690  1.00 52.82           O  
-ATOM   6885  N   ASN C 272      67.000  40.123  33.949  1.00 47.53           N  
-ATOM   6886  CA  ASN C 272      67.291  40.141  32.521  1.00 44.51           C  
-ATOM   6887  C   ASN C 272      67.712  38.749  32.120  1.00 40.71           C  
-ATOM   6888  O   ASN C 272      68.401  38.077  32.871  1.00 47.12           O  
-ATOM   6889  CB  ASN C 272      68.434  41.104  32.213  1.00 58.62           C  
-ATOM   6890  CG  ASN C 272      67.973  42.545  32.092  1.00 76.58           C  
-ATOM   6891  OD1 ASN C 272      67.055  42.857  31.324  1.00 86.21           O  
-ATOM   6892  ND2 ASN C 272      68.618  43.437  32.840  1.00 80.58           N  
-ATOM   6893  N   ILE C 273      67.307  38.301  30.942  1.00 30.94           N  
-ATOM   6894  CA  ILE C 273      67.700  36.969  30.516  1.00 21.51           C  
-ATOM   6895  C   ILE C 273      69.214  36.972  30.273  1.00 15.13           C  
-ATOM   6896  O   ILE C 273      69.729  37.784  29.510  1.00 16.00           O  
-ATOM   6897  CB  ILE C 273      66.919  36.551  29.242  1.00 17.68           C  
-ATOM   6898  CG1 ILE C 273      67.448  35.219  28.708  1.00 18.76           C  
-ATOM   6899  CG2 ILE C 273      67.007  37.637  28.206  1.00 23.40           C  
-ATOM   6900  CD1 ILE C 273      66.725  34.706  27.482  1.00 17.02           C  
-ATOM   6901  N   LEU C 274      69.931  36.082  30.949  1.00 11.81           N  
-ATOM   6902  CA  LEU C 274      71.383  36.008  30.801  1.00 15.62           C  
-ATOM   6903  C   LEU C 274      71.869  35.938  29.347  1.00 19.98           C  
-ATOM   6904  O   LEU C 274      71.251  35.288  28.490  1.00 20.02           O  
-ATOM   6905  CB  LEU C 274      71.953  34.818  31.595  1.00 12.82           C  
-ATOM   6906  CG  LEU C 274      72.172  35.053  33.099  1.00 23.45           C  
-ATOM   6907  CD1 LEU C 274      70.850  34.923  33.805  1.00 25.30           C  
-ATOM   6908  CD2 LEU C 274      73.170  34.049  33.692  1.00 29.38           C  
-ATOM   6909  N   PRO C 275      72.999  36.611  29.057  1.00 16.81           N  
-ATOM   6910  CA  PRO C 275      73.647  36.693  27.750  1.00 10.22           C  
-ATOM   6911  C   PRO C 275      73.539  35.455  26.873  1.00 16.07           C  
-ATOM   6912  O   PRO C 275      72.814  35.466  25.877  1.00 23.30           O  
-ATOM   6913  CB  PRO C 275      75.084  37.025  28.112  1.00  4.47           C  
-ATOM   6914  CG  PRO C 275      74.894  37.968  29.211  1.00  7.52           C  
-ATOM   6915  CD  PRO C 275      73.821  37.301  30.065  1.00 15.69           C  
-ATOM   6916  N   LEU C 276      74.245  34.386  27.231  1.00 11.00           N  
-ATOM   6917  CA  LEU C 276      74.213  33.189  26.406  1.00  4.47           C  
-ATOM   6918  C   LEU C 276      72.801  32.778  26.088  1.00  4.73           C  
-ATOM   6919  O   LEU C 276      72.452  32.626  24.919  1.00  6.24           O  
-ATOM   6920  CB  LEU C 276      74.953  32.045  27.075  1.00  4.47           C  
-ATOM   6921  CG  LEU C 276      76.465  32.256  27.099  1.00  4.47           C  
-ATOM   6922  CD1 LEU C 276      77.158  31.084  27.782  1.00 15.15           C  
-ATOM   6923  CD2 LEU C 276      76.953  32.408  25.691  1.00  4.47           C  
-ATOM   6924  N   TRP C 277      71.983  32.627  27.124  1.00  6.37           N  
-ATOM   6925  CA  TRP C 277      70.592  32.220  26.939  1.00  9.93           C  
-ATOM   6926  C   TRP C 277      69.900  33.123  25.931  1.00  8.47           C  
-ATOM   6927  O   TRP C 277      68.983  32.698  25.228  1.00 18.31           O  
-ATOM   6928  CB  TRP C 277      69.837  32.236  28.272  1.00 12.78           C  
-ATOM   6929  CG  TRP C 277      70.403  31.315  29.324  1.00  5.67           C  
-ATOM   6930  CD1 TRP C 277      70.142  31.362  30.653  1.00  5.06           C  
-ATOM   6931  CD2 TRP C 277      71.317  30.217  29.131  1.00  4.47           C  
-ATOM   6932  NE1 TRP C 277      70.830  30.372  31.306  1.00 16.14           N  
-ATOM   6933  CE2 TRP C 277      71.558  29.653  30.396  1.00  7.00           C  
-ATOM   6934  CE3 TRP C 277      71.951  29.655  28.012  1.00  4.47           C  
-ATOM   6935  CZ2 TRP C 277      72.406  28.550  30.581  1.00  8.42           C  
-ATOM   6936  CZ3 TRP C 277      72.791  28.556  28.196  1.00  7.44           C  
-ATOM   6937  CH2 TRP C 277      73.008  28.017  29.473  1.00  4.47           C  
-ATOM   6938  N   ALA C 278      70.330  34.371  25.851  1.00  4.47           N  
-ATOM   6939  CA  ALA C 278      69.734  35.256  24.870  1.00 10.71           C  
-ATOM   6940  C   ALA C 278      70.124  34.733  23.483  1.00 11.82           C  
-ATOM   6941  O   ALA C 278      69.264  34.361  22.679  1.00 14.08           O  
-ATOM   6942  CB  ALA C 278      70.237  36.659  25.064  1.00 10.43           C  
-ATOM   6943  N   TRP C 279      71.424  34.698  23.214  1.00  8.77           N  
-ATOM   6944  CA  TRP C 279      71.915  34.209  21.938  1.00  7.53           C  
-ATOM   6945  C   TRP C 279      71.139  32.959  21.586  1.00  9.82           C  
-ATOM   6946  O   TRP C 279      70.802  32.734  20.428  1.00 18.72           O  
-ATOM   6947  CB  TRP C 279      73.399  33.870  22.029  1.00 12.35           C  
-ATOM   6948  CG  TRP C 279      74.275  35.046  22.283  1.00 17.52           C  
-ATOM   6949  CD1 TRP C 279      73.875  36.320  22.550  1.00 23.33           C  
-ATOM   6950  CD2 TRP C 279      75.707  35.059  22.311  1.00 21.90           C  
-ATOM   6951  NE1 TRP C 279      74.968  37.131  22.743  1.00 32.07           N  
-ATOM   6952  CE2 TRP C 279      76.106  36.380  22.600  1.00 32.37           C  
-ATOM   6953  CE3 TRP C 279      76.693  34.081  22.122  1.00 25.19           C  
-ATOM   6954  CZ2 TRP C 279      77.453  36.750  22.704  1.00 35.30           C  
-ATOM   6955  CZ3 TRP C 279      78.030  34.448  22.228  1.00 20.36           C  
-ATOM   6956  CH2 TRP C 279      78.396  35.769  22.515  1.00 28.30           C  
-ATOM   6957  N   GLY C 280      70.859  32.143  22.594  1.00  5.45           N  
-ATOM   6958  CA  GLY C 280      70.108  30.928  22.358  1.00 10.72           C  
-ATOM   6959  C   GLY C 280      68.727  31.239  21.798  1.00 15.14           C  
-ATOM   6960  O   GLY C 280      68.334  30.702  20.755  1.00 18.31           O  
-ATOM   6961  N   MET C 281      67.985  32.108  22.483  1.00  6.02           N  
-ATOM   6962  CA  MET C 281      66.650  32.471  22.027  1.00  8.73           C  
-ATOM   6963  C   MET C 281      66.730  32.802  20.545  1.00 15.96           C  
-ATOM   6964  O   MET C 281      65.868  32.420  19.755  1.00 20.74           O  
-ATOM   6965  CB  MET C 281      66.142  33.689  22.792  1.00  4.47           C  
-ATOM   6966  CG  MET C 281      66.063  33.500  24.298  1.00 12.97           C  
-ATOM   6967  SD  MET C 281      64.475  32.850  24.840  1.00 20.15           S  
-ATOM   6968  CE  MET C 281      64.591  31.185  24.154  1.00 22.96           C  
-ATOM   6969  N   GLU C 282      67.793  33.507  20.180  1.00 18.47           N  
-ATOM   6970  CA  GLU C 282      68.013  33.911  18.804  1.00 21.91           C  
-ATOM   6971  C   GLU C 282      67.937  32.711  17.863  1.00 19.80           C  
-ATOM   6972  O   GLU C 282      67.109  32.688  16.958  1.00 28.45           O  
-ATOM   6973  CB  GLU C 282      69.383  34.597  18.676  1.00 36.20           C  
-ATOM   6974  CG  GLU C 282      69.397  35.915  17.875  1.00 53.33           C  
-ATOM   6975  CD  GLU C 282      68.700  37.078  18.591  1.00 64.29           C  
-ATOM   6976  OE1 GLU C 282      69.123  37.444  19.721  1.00 61.75           O  
-ATOM   6977  OE2 GLU C 282      67.732  37.628  18.010  1.00 64.17           O  
-ATOM   6978  N   THR C 283      68.788  31.710  18.079  1.00 16.13           N  
-ATOM   6979  CA  THR C 283      68.801  30.532  17.213  1.00 14.22           C  
-ATOM   6980  C   THR C 283      67.469  29.787  17.250  1.00 12.96           C  
-ATOM   6981  O   THR C 283      66.983  29.316  16.207  1.00  7.67           O  
-ATOM   6982  CB  THR C 283      69.935  29.552  17.599  1.00 10.78           C  
-ATOM   6983  OG1 THR C 283      69.681  29.014  18.898  1.00 26.41           O  
-ATOM   6984  CG2 THR C 283      71.273  30.263  17.615  1.00  4.47           C  
-ATOM   6985  N   LEU C 284      66.882  29.680  18.442  1.00  8.32           N  
-ATOM   6986  CA  LEU C 284      65.596  29.003  18.583  1.00 11.80           C  
-ATOM   6987  C   LEU C 284      64.564  29.710  17.728  1.00 11.69           C  
-ATOM   6988  O   LEU C 284      63.699  29.073  17.135  1.00 13.78           O  
-ATOM   6989  CB  LEU C 284      65.137  28.999  20.035  1.00 15.91           C  
-ATOM   6990  CG  LEU C 284      63.701  28.517  20.250  1.00 12.61           C  
-ATOM   6991  CD1 LEU C 284      63.525  28.107  21.701  1.00 21.32           C  
-ATOM   6992  CD2 LEU C 284      62.726  29.619  19.883  1.00  7.07           C  
-ATOM   6993  N   SER C 285      64.642  31.036  17.696  1.00 12.64           N  
-ATOM   6994  CA  SER C 285      63.740  31.833  16.874  1.00 18.71           C  
-ATOM   6995  C   SER C 285      64.061  31.537  15.403  1.00 22.38           C  
-ATOM   6996  O   SER C 285      63.182  31.176  14.615  1.00 19.08           O  
-ATOM   6997  CB  SER C 285      63.949  33.318  17.155  1.00 22.72           C  
-ATOM   6998  OG  SER C 285      63.731  33.602  18.522  1.00 32.59           O  
-ATOM   6999  N   ASN C 286      65.336  31.687  15.052  1.00 27.41           N  
-ATOM   7000  CA  ASN C 286      65.818  31.423  13.703  1.00 28.70           C  
-ATOM   7001  C   ASN C 286      65.193  30.166  13.128  1.00 28.00           C  
-ATOM   7002  O   ASN C 286      64.733  30.162  11.995  1.00 32.84           O  
-ATOM   7003  CB  ASN C 286      67.337  31.266  13.713  1.00 28.65           C  
-ATOM   7004  CG  ASN C 286      68.052  32.588  13.580  1.00 36.91           C  
-ATOM   7005  OD1 ASN C 286      67.437  33.653  13.682  1.00 36.37           O  
-ATOM   7006  ND2 ASN C 286      69.363  32.533  13.348  1.00 41.93           N  
-ATOM   7007  N   CYS C 287      65.185  29.103  13.922  1.00 25.46           N  
-ATOM   7008  CA  CYS C 287      64.623  27.826  13.509  1.00 30.09           C  
-ATOM   7009  C   CYS C 287      63.114  27.892  13.272  1.00 29.75           C  
-ATOM   7010  O   CYS C 287      62.636  27.761  12.139  1.00 34.24           O  
-ATOM   7011  CB  CYS C 287      64.932  26.772  14.581  1.00 31.19           C  
-ATOM   7012  SG  CYS C 287      64.080  25.187  14.388  1.00 36.75           S  
-ATOM   7013  N   LEU C 288      62.375  28.086  14.356  1.00 26.41           N  
-ATOM   7014  CA  LEU C 288      60.921  28.157  14.319  1.00 29.24           C  
-ATOM   7015  C   LEU C 288      60.345  29.101  13.247  1.00 36.37           C  
-ATOM   7016  O   LEU C 288      59.317  28.803  12.618  1.00 37.47           O  
-ATOM   7017  CB  LEU C 288      60.420  28.563  15.705  1.00 16.49           C  
-ATOM   7018  CG  LEU C 288      59.693  27.509  16.543  1.00 13.83           C  
-ATOM   7019  CD1 LEU C 288      60.377  26.167  16.485  1.00 24.49           C  
-ATOM   7020  CD2 LEU C 288      59.630  28.014  17.955  1.00 22.82           C  
-ATOM   7021  N   ARG C 289      61.013  30.232  13.039  1.00 34.56           N  
-ATOM   7022  CA  ARG C 289      60.568  31.229  12.067  1.00 27.66           C  
-ATOM   7023  C   ARG C 289      60.578  30.763  10.611  1.00 25.09           C  
-ATOM   7024  O   ARG C 289      59.773  31.222   9.800  1.00 25.32           O  
-ATOM   7025  CB  ARG C 289      61.417  32.489  12.204  1.00 19.61           C  
-ATOM   7026  CG  ARG C 289      61.052  33.575  11.232  1.00 19.74           C  
-ATOM   7027  CD  ARG C 289      61.498  34.918  11.758  1.00 23.26           C  
-ATOM   7028  NE  ARG C 289      62.892  34.903  12.173  1.00 31.02           N  
-ATOM   7029  CZ  ARG C 289      63.338  35.488  13.279  1.00 40.56           C  
-ATOM   7030  NH1 ARG C 289      62.494  36.133  14.077  1.00 34.32           N  
-ATOM   7031  NH2 ARG C 289      64.625  35.416  13.596  1.00 51.39           N  
-ATOM   7032  N   SER C 290      61.490  29.857  10.283  1.00 21.88           N  
-ATOM   7033  CA  SER C 290      61.601  29.335   8.927  1.00 21.49           C  
-ATOM   7034  C   SER C 290      60.375  28.531   8.547  1.00 24.10           C  
-ATOM   7035  O   SER C 290      59.950  28.514   7.390  1.00 29.29           O  
-ATOM   7036  CB  SER C 290      62.818  28.423   8.813  1.00 19.39           C  
-ATOM   7037  OG  SER C 290      64.004  29.135   9.098  1.00 44.99           O  
-ATOM   7038  N   MET C 291      59.806  27.868   9.544  1.00 24.91           N  
-ATOM   7039  CA  MET C 291      58.651  26.999   9.357  1.00 22.24           C  
-ATOM   7040  C   MET C 291      57.313  27.546   8.848  1.00 18.56           C  
-ATOM   7041  O   MET C 291      56.909  28.667   9.142  1.00 18.84           O  
-ATOM   7042  CB  MET C 291      58.445  26.216  10.652  1.00 26.25           C  
-ATOM   7043  CG  MET C 291      59.568  25.202  10.865  1.00 36.18           C  
-ATOM   7044  SD  MET C 291      59.466  24.185  12.337  1.00 30.05           S  
-ATOM   7045  CE  MET C 291      60.944  24.770  13.171  1.00 43.46           C  
-ATOM   7046  N   SER C 292      56.635  26.722   8.060  1.00 15.68           N  
-ATOM   7047  CA  SER C 292      55.339  27.068   7.505  1.00 14.64           C  
-ATOM   7048  C   SER C 292      54.327  26.187   8.234  1.00 16.12           C  
-ATOM   7049  O   SER C 292      54.181  24.996   7.942  1.00 14.14           O  
-ATOM   7050  CB  SER C 292      55.351  26.775   6.023  1.00 23.30           C  
-ATOM   7051  OG  SER C 292      56.528  27.323   5.459  1.00 30.56           O  
-ATOM   7052  N   PRO C 293      53.623  26.771   9.207  1.00 10.41           N  
-ATOM   7053  CA  PRO C 293      52.615  26.134  10.054  1.00 14.70           C  
-ATOM   7054  C   PRO C 293      51.266  25.815   9.448  1.00 12.94           C  
-ATOM   7055  O   PRO C 293      50.650  26.657   8.792  1.00 16.38           O  
-ATOM   7056  CB  PRO C 293      52.488  27.115  11.209  1.00 24.07           C  
-ATOM   7057  CG  PRO C 293      52.606  28.424  10.506  1.00 22.52           C  
-ATOM   7058  CD  PRO C 293      53.779  28.190   9.563  1.00 10.89           C  
-ATOM   7059  N   PHE C 294      50.803  24.597   9.710  1.00  8.00           N  
-ATOM   7060  CA  PHE C 294      49.514  24.144   9.221  1.00  8.07           C  
-ATOM   7061  C   PHE C 294      48.873  23.279  10.283  1.00 15.96           C  
-ATOM   7062  O   PHE C 294      49.563  22.536  10.992  1.00 14.65           O  
-ATOM   7063  CB  PHE C 294      49.677  23.317   7.953  1.00  7.87           C  
-ATOM   7064  CG  PHE C 294      50.120  24.106   6.756  1.00 12.75           C  
-ATOM   7065  CD1 PHE C 294      51.351  23.855   6.162  1.00 16.64           C  
-ATOM   7066  CD2 PHE C 294      49.301  25.091   6.215  1.00 20.76           C  
-ATOM   7067  CE1 PHE C 294      51.764  24.569   5.048  1.00 14.09           C  
-ATOM   7068  CE2 PHE C 294      49.700  25.814   5.102  1.00 22.04           C  
-ATOM   7069  CZ  PHE C 294      50.938  25.550   4.517  1.00 26.70           C  
-ATOM   7070  N   VAL C 295      47.551  23.377  10.386  1.00 20.78           N  
-ATOM   7071  CA  VAL C 295      46.792  22.595  11.357  1.00 22.74           C  
-ATOM   7072  C   VAL C 295      45.865  21.636  10.630  1.00 27.63           C  
-ATOM   7073  O   VAL C 295      45.100  22.045   9.762  1.00 33.33           O  
-ATOM   7074  CB  VAL C 295      45.953  23.505  12.273  1.00 19.99           C  
-ATOM   7075  CG1 VAL C 295      44.764  22.728  12.864  1.00 19.34           C  
-ATOM   7076  CG2 VAL C 295      46.842  24.055  13.382  1.00 16.79           C  
-ATOM   7077  N   LEU C 296      45.934  20.363  11.003  1.00 31.23           N  
-ATOM   7078  CA  LEU C 296      45.124  19.321  10.387  1.00 27.36           C  
-ATOM   7079  C   LEU C 296      44.320  18.590  11.454  1.00 33.73           C  
-ATOM   7080  O   LEU C 296      44.883  18.046  12.400  1.00 36.56           O  
-ATOM   7081  CB  LEU C 296      46.044  18.346   9.659  1.00 18.72           C  
-ATOM   7082  CG  LEU C 296      45.444  17.203   8.856  1.00 21.08           C  
-ATOM   7083  CD1 LEU C 296      46.570  16.473   8.151  1.00 20.57           C  
-ATOM   7084  CD2 LEU C 296      44.680  16.261   9.756  1.00 25.28           C  
-ATOM   7085  N   SER C 297      43.002  18.570  11.293  1.00 42.84           N  
-ATOM   7086  CA  SER C 297      42.123  17.903  12.254  1.00 46.87           C  
-ATOM   7087  C   SER C 297      41.964  16.418  11.958  1.00 45.03           C  
-ATOM   7088  O   SER C 297      41.619  16.035  10.841  1.00 50.07           O  
-ATOM   7089  CB  SER C 297      40.739  18.556  12.254  1.00 52.51           C  
-ATOM   7090  OG  SER C 297      39.839  17.821  13.063  1.00 53.60           O  
-ATOM   7091  N   LEU C 298      42.215  15.586  12.962  1.00 44.48           N  
-ATOM   7092  CA  LEU C 298      42.079  14.144  12.800  1.00 49.76           C  
-ATOM   7093  C   LEU C 298      40.782  13.682  13.443  1.00 56.05           C  
-ATOM   7094  O   LEU C 298      40.661  12.524  13.844  1.00 64.06           O  
-ATOM   7095  CB  LEU C 298      43.258  13.404  13.443  1.00 42.56           C  
-ATOM   7096  CG  LEU C 298      44.637  13.662  12.846  1.00 35.89           C  
-ATOM   7097  CD1 LEU C 298      45.628  12.723  13.479  1.00 34.86           C  
-ATOM   7098  CD2 LEU C 298      44.602  13.450  11.352  1.00 42.73           C  
-ATOM   7099  N   GLU C 299      39.820  14.595  13.540  1.00 57.53           N  
-ATOM   7100  CA  GLU C 299      38.523  14.299  14.136  1.00 66.64           C  
-ATOM   7101  C   GLU C 299      37.565  13.796  13.057  1.00 70.14           C  
-ATOM   7102  O   GLU C 299      36.591  14.469  12.712  1.00 71.19           O  
-ATOM   7103  CB  GLU C 299      37.955  15.561  14.799  1.00 73.61           C  
-ATOM   7104  CG  GLU C 299      36.659  15.365  15.585  1.00 85.30           C  
-ATOM   7105  CD  GLU C 299      36.873  14.687  16.927  1.00 98.00           C  
-ATOM   7106  OE1 GLU C 299      35.880  14.498  17.664  1.00101.69           O  
-ATOM   7107  OE2 GLU C 299      38.033  14.345  17.246  1.00106.35           O  
-ATOM   7108  N   GLN C 300      37.853  12.610  12.527  1.00 74.06           N  
-ATOM   7109  CA  GLN C 300      37.034  11.999  11.483  1.00 76.41           C  
-ATOM   7110  C   GLN C 300      37.726  10.765  10.907  1.00 77.23           C  
-ATOM   7111  O   GLN C 300      38.793  10.367  11.375  1.00 79.09           O  
-ATOM   7112  CB  GLN C 300      36.762  13.013  10.365  1.00 73.62           C  
-ATOM   7113  CG  GLN C 300      38.017  13.686   9.823  1.00 70.83           C  
-ATOM   7114  CD  GLN C 300      37.709  14.759   8.791  1.00 73.58           C  
-ATOM   7115  OE1 GLN C 300      38.617  15.410   8.266  1.00 69.12           O  
-ATOM   7116  NE2 GLN C 300      36.423  14.946   8.491  1.00 73.46           N  
-ATOM   7117  N   THR C 301      37.112  10.165   9.891  1.00 78.72           N  
-ATOM   7118  CA  THR C 301      37.667   8.977   9.241  1.00 77.48           C  
-ATOM   7119  C   THR C 301      39.014   9.299   8.595  1.00 73.02           C  
-ATOM   7120  O   THR C 301      39.174  10.346   7.966  1.00 73.81           O  
-ATOM   7121  CB  THR C 301      36.712   8.442   8.150  1.00 81.70           C  
-ATOM   7122  OG1 THR C 301      36.474   9.471   7.177  1.00 83.83           O  
-ATOM   7123  CG2 THR C 301      35.379   8.004   8.766  1.00 82.42           C  
-ATOM   7124  N   PRO C 302      40.000   8.397   8.742  1.00 68.96           N  
-ATOM   7125  CA  PRO C 302      41.331   8.605   8.166  1.00 69.40           C  
-ATOM   7126  C   PRO C 302      41.249   9.093   6.726  1.00 74.41           C  
-ATOM   7127  O   PRO C 302      42.108   9.845   6.269  1.00 78.21           O  
-ATOM   7128  CB  PRO C 302      41.973   7.229   8.281  1.00 64.48           C  
-ATOM   7129  CG  PRO C 302      41.379   6.700   9.537  1.00 67.19           C  
-ATOM   7130  CD  PRO C 302      39.920   7.082   9.403  1.00 68.03           C  
-ATOM   7131  N   GLN C 303      40.210   8.663   6.016  1.00 77.35           N  
-ATOM   7132  CA  GLN C 303      40.017   9.073   4.631  1.00 78.98           C  
-ATOM   7133  C   GLN C 303      39.967  10.599   4.554  1.00 76.55           C  
-ATOM   7134  O   GLN C 303      40.731  11.215   3.812  1.00 73.91           O  
-ATOM   7135  CB  GLN C 303      38.718   8.480   4.060  1.00 85.69           C  
-ATOM   7136  CG  GLN C 303      38.835   7.054   3.506  1.00 95.73           C  
-ATOM   7137  CD  GLN C 303      38.968   5.987   4.583  1.00100.65           C  
-ATOM   7138  OE1 GLN C 303      38.095   5.840   5.438  1.00104.38           O  
-ATOM   7139  NE2 GLN C 303      40.060   5.230   4.539  1.00100.40           N  
-ATOM   7140  N   HIS C 304      39.075  11.205   5.332  1.00 75.22           N  
-ATOM   7141  CA  HIS C 304      38.938  12.656   5.335  1.00 74.47           C  
-ATOM   7142  C   HIS C 304      40.232  13.338   5.747  1.00 71.14           C  
-ATOM   7143  O   HIS C 304      40.730  14.218   5.039  1.00 74.02           O  
-ATOM   7144  CB  HIS C 304      37.800  13.090   6.265  1.00 78.19           C  
-ATOM   7145  CG  HIS C 304      36.431  12.820   5.718  1.00 90.23           C  
-ATOM   7146  ND1 HIS C 304      35.291  13.382   6.255  1.00 91.78           N  
-ATOM   7147  CD2 HIS C 304      36.020  12.059   4.673  1.00 91.66           C  
-ATOM   7148  CE1 HIS C 304      34.239  12.980   5.564  1.00 93.13           C  
-ATOM   7149  NE2 HIS C 304      34.653  12.177   4.599  1.00 92.66           N  
-ATOM   7150  N   ALA C 305      40.770  12.927   6.891  1.00 65.78           N  
-ATOM   7151  CA  ALA C 305      42.013  13.493   7.406  1.00 60.19           C  
-ATOM   7152  C   ALA C 305      43.042  13.645   6.292  1.00 57.76           C  
-ATOM   7153  O   ALA C 305      43.636  14.712   6.126  1.00 62.44           O  
-ATOM   7154  CB  ALA C 305      42.572  12.606   8.506  1.00 53.82           C  
-ATOM   7155  N   ALA C 306      43.239  12.579   5.523  1.00 49.17           N  
-ATOM   7156  CA  ALA C 306      44.201  12.595   4.433  1.00 45.04           C  
-ATOM   7157  C   ALA C 306      43.741  13.463   3.276  1.00 51.36           C  
-ATOM   7158  O   ALA C 306      44.548  14.160   2.663  1.00 51.14           O  
-ATOM   7159  CB  ALA C 306      44.453  11.195   3.952  1.00 44.94           C  
-ATOM   7160  N   GLN C 307      42.448  13.419   2.966  1.00 57.93           N  
-ATOM   7161  CA  GLN C 307      41.924  14.227   1.870  1.00 62.12           C  
-ATOM   7162  C   GLN C 307      42.159  15.691   2.204  1.00 57.95           C  
-ATOM   7163  O   GLN C 307      42.586  16.471   1.349  1.00 56.75           O  
-ATOM   7164  CB  GLN C 307      40.425  13.972   1.655  1.00 74.15           C  
-ATOM   7165  CG  GLN C 307      39.842  14.713   0.445  1.00 90.04           C  
-ATOM   7166  CD  GLN C 307      38.401  14.327   0.137  1.00 99.47           C  
-ATOM   7167  OE1 GLN C 307      38.101  13.161  -0.134  1.00104.10           O  
-ATOM   7168  NE2 GLN C 307      37.503  15.310   0.170  1.00 98.63           N  
-ATOM   7169  N   GLU C 308      41.890  16.059   3.453  1.00 52.79           N  
-ATOM   7170  CA  GLU C 308      42.090  17.434   3.878  1.00 54.91           C  
-ATOM   7171  C   GLU C 308      43.555  17.802   3.652  1.00 49.37           C  
-ATOM   7172  O   GLU C 308      43.863  18.802   3.001  1.00 54.48           O  
-ATOM   7173  CB  GLU C 308      41.712  17.606   5.354  1.00 59.37           C  
-ATOM   7174  CG  GLU C 308      41.757  19.057   5.841  1.00 71.49           C  
-ATOM   7175  CD  GLU C 308      41.218  19.227   7.251  1.00 80.66           C  
-ATOM   7176  OE1 GLU C 308      41.318  20.349   7.797  1.00 81.55           O  
-ATOM   7177  OE2 GLU C 308      40.690  18.240   7.811  1.00 85.34           O  
-ATOM   7178  N   LEU C 309      44.460  16.983   4.170  1.00 38.66           N  
-ATOM   7179  CA  LEU C 309      45.882  17.242   3.996  1.00 35.97           C  
-ATOM   7180  C   LEU C 309      46.216  17.519   2.530  1.00 37.09           C  
-ATOM   7181  O   LEU C 309      47.075  18.343   2.225  1.00 37.70           O  
-ATOM   7182  CB  LEU C 309      46.706  16.050   4.500  1.00 33.43           C  
-ATOM   7183  CG  LEU C 309      48.221  16.049   4.229  1.00 26.39           C  
-ATOM   7184  CD1 LEU C 309      48.851  17.319   4.774  1.00 28.22           C  
-ATOM   7185  CD2 LEU C 309      48.857  14.835   4.871  1.00 17.45           C  
-ATOM   7186  N   LYS C 310      45.536  16.834   1.619  1.00 37.14           N  
-ATOM   7187  CA  LYS C 310      45.791  17.035   0.200  1.00 40.50           C  
-ATOM   7188  C   LYS C 310      45.463  18.458  -0.244  1.00 42.11           C  
-ATOM   7189  O   LYS C 310      46.204  19.071  -1.014  1.00 45.86           O  
-ATOM   7190  CB  LYS C 310      44.969  16.057  -0.636  1.00 46.85           C  
-ATOM   7191  CG  LYS C 310      45.139  16.271  -2.134  1.00 60.18           C  
-ATOM   7192  CD  LYS C 310      44.137  15.469  -2.952  1.00 71.90           C  
-ATOM   7193  CE  LYS C 310      44.256  15.811  -4.436  1.00 77.15           C  
-ATOM   7194  NZ  LYS C 310      43.274  15.074  -5.276  1.00 81.76           N  
-ATOM   7195  N   THR C 311      44.345  18.980   0.238  1.00 40.28           N  
-ATOM   7196  CA  THR C 311      43.914  20.325  -0.124  1.00 42.75           C  
-ATOM   7197  C   THR C 311      44.950  21.383   0.272  1.00 43.44           C  
-ATOM   7198  O   THR C 311      44.974  22.489  -0.288  1.00 36.74           O  
-ATOM   7199  CB  THR C 311      42.554  20.660   0.548  1.00 44.64           C  
-ATOM   7200  OG1 THR C 311      42.771  21.252   1.837  1.00 43.40           O  
-ATOM   7201  CG2 THR C 311      41.723  19.383   0.725  1.00 30.01           C  
-ATOM   7202  N   LEU C 312      45.805  21.022   1.231  1.00 46.67           N  
-ATOM   7203  CA  LEU C 312      46.857  21.904   1.753  1.00 47.58           C  
-ATOM   7204  C   LEU C 312      48.147  21.902   0.939  1.00 46.67           C  
-ATOM   7205  O   LEU C 312      48.885  22.888   0.948  1.00 51.02           O  
-ATOM   7206  CB  LEU C 312      47.220  21.524   3.195  1.00 41.56           C  
-ATOM   7207  CG  LEU C 312      46.352  21.961   4.368  1.00 39.47           C  
-ATOM   7208  CD1 LEU C 312      44.910  21.494   4.223  1.00 47.63           C  
-ATOM   7209  CD2 LEU C 312      46.971  21.371   5.600  1.00 45.22           C  
-ATOM   7210  N   LEU C 313      48.423  20.793   0.259  1.00 39.98           N  
-ATOM   7211  CA  LEU C 313      49.636  20.661  -0.540  1.00 41.17           C  
-ATOM   7212  C   LEU C 313      49.976  21.912  -1.340  1.00 46.78           C  
-ATOM   7213  O   LEU C 313      51.139  22.327  -1.390  1.00 52.35           O  
-ATOM   7214  CB  LEU C 313      49.507  19.476  -1.490  1.00 44.67           C  
-ATOM   7215  CG  LEU C 313      49.193  18.148  -0.808  1.00 50.00           C  
-ATOM   7216  CD1 LEU C 313      48.987  17.067  -1.867  1.00 56.35           C  
-ATOM   7217  CD2 LEU C 313      50.325  17.787   0.135  1.00 47.79           C  
-ATOM   7218  N   PRO C 314      48.969  22.529  -1.986  1.00 47.33           N  
-ATOM   7219  CA  PRO C 314      49.217  23.742  -2.777  1.00 48.15           C  
-ATOM   7220  C   PRO C 314      49.609  24.986  -1.957  1.00 52.45           C  
-ATOM   7221  O   PRO C 314      50.184  25.935  -2.508  1.00 55.95           O  
-ATOM   7222  CB  PRO C 314      47.900  23.927  -3.538  1.00 44.49           C  
-ATOM   7223  CG  PRO C 314      46.878  23.350  -2.590  1.00 46.28           C  
-ATOM   7224  CD  PRO C 314      47.567  22.088  -2.128  1.00 44.46           C  
-ATOM   7225  N   GLN C 315      49.310  24.974  -0.654  1.00 48.08           N  
-ATOM   7226  CA  GLN C 315      49.616  26.100   0.233  1.00 39.68           C  
-ATOM   7227  C   GLN C 315      50.998  26.007   0.869  1.00 33.89           C  
-ATOM   7228  O   GLN C 315      51.533  27.000   1.371  1.00 36.04           O  
-ATOM   7229  CB  GLN C 315      48.568  26.198   1.347  1.00 36.06           C  
-ATOM   7230  CG  GLN C 315      47.131  26.247   0.862  1.00 48.79           C  
-ATOM   7231  CD  GLN C 315      46.149  26.560   1.981  1.00 61.72           C  
-ATOM   7232  OE1 GLN C 315      46.116  27.680   2.503  1.00 64.86           O  
-ATOM   7233  NE2 GLN C 315      45.344  25.568   2.360  1.00 63.22           N  
-ATOM   7234  N   MET C 316      51.572  24.811   0.837  1.00 30.92           N  
-ATOM   7235  CA  MET C 316      52.876  24.560   1.439  1.00 30.30           C  
-ATOM   7236  C   MET C 316      54.064  25.108   0.673  1.00 29.29           C  
-ATOM   7237  O   MET C 316      54.024  25.236  -0.550  1.00 29.36           O  
-ATOM   7238  CB  MET C 316      53.051  23.064   1.643  1.00 20.34           C  
-ATOM   7239  CG  MET C 316      51.922  22.483   2.430  1.00 21.36           C  
-ATOM   7240  SD  MET C 316      52.118  20.751   2.711  1.00 26.45           S  
-ATOM   7241  CE  MET C 316      50.711  20.491   3.911  1.00 29.41           C  
-ATOM   7242  N   THR C 317      55.121  25.429   1.413  1.00 25.45           N  
-ATOM   7243  CA  THR C 317      56.336  25.958   0.819  1.00 27.13           C  
-ATOM   7244  C   THR C 317      57.189  24.813   0.311  1.00 27.19           C  
-ATOM   7245  O   THR C 317      57.489  23.877   1.044  1.00 33.69           O  
-ATOM   7246  CB  THR C 317      57.157  26.763   1.839  1.00 31.62           C  
-ATOM   7247  OG1 THR C 317      56.401  27.905   2.265  1.00 41.30           O  
-ATOM   7248  CG2 THR C 317      58.473  27.228   1.218  1.00 26.92           C  
-ATOM   7249  N   PRO C 318      57.578  24.866  -0.965  1.00 29.76           N  
-ATOM   7250  CA  PRO C 318      58.407  23.825  -1.586  1.00 32.86           C  
-ATOM   7251  C   PRO C 318      59.910  24.129  -1.559  1.00 31.11           C  
-ATOM   7252  O   PRO C 318      60.325  25.288  -1.505  1.00 29.65           O  
-ATOM   7253  CB  PRO C 318      57.869  23.781  -3.007  1.00 37.82           C  
-ATOM   7254  CG  PRO C 318      57.618  25.251  -3.283  1.00 34.20           C  
-ATOM   7255  CD  PRO C 318      56.955  25.726  -1.990  1.00 30.13           C  
-ATOM   7256  N   ALA C 319      60.721  23.081  -1.608  1.00 28.74           N  
-ATOM   7257  CA  ALA C 319      62.170  23.243  -1.601  1.00 34.02           C  
-ATOM   7258  C   ALA C 319      62.751  22.529  -2.801  1.00 38.59           C  
-ATOM   7259  O   ALA C 319      62.102  21.662  -3.382  1.00 44.87           O  
-ATOM   7260  CB  ALA C 319      62.758  22.669  -0.328  1.00 44.01           C  
-ATOM   7261  N   ASN C 320      63.981  22.873  -3.161  1.00 41.29           N  
-ATOM   7262  CA  ASN C 320      64.612  22.257  -4.320  1.00 51.08           C  
-ATOM   7263  C   ASN C 320      65.714  21.274  -3.965  1.00 50.73           C  
-ATOM   7264  O   ASN C 320      66.498  21.522  -3.055  1.00 51.56           O  
-ATOM   7265  CB  ASN C 320      65.185  23.338  -5.237  1.00 59.84           C  
-ATOM   7266  CG  ASN C 320      64.169  24.412  -5.581  1.00 71.01           C  
-ATOM   7267  OD1 ASN C 320      63.064  24.121  -6.049  1.00 75.96           O  
-ATOM   7268  ND2 ASN C 320      64.544  25.666  -5.356  1.00 76.87           N  
-ATOM   7269  N   MET C 321      65.772  20.160  -4.691  1.00 52.62           N  
-ATOM   7270  CA  MET C 321      66.802  19.159  -4.454  1.00 54.56           C  
-ATOM   7271  C   MET C 321      67.158  18.369  -5.712  1.00 58.63           C  
-ATOM   7272  O   MET C 321      66.323  18.184  -6.611  1.00 53.45           O  
-ATOM   7273  CB  MET C 321      66.375  18.195  -3.337  1.00 49.79           C  
-ATOM   7274  CG  MET C 321      65.435  17.080  -3.741  1.00 38.32           C  
-ATOM   7275  SD  MET C 321      65.196  15.963  -2.357  1.00 41.47           S  
-ATOM   7276  CE  MET C 321      66.762  15.065  -2.384  1.00 40.94           C  
-ATOM   7277  N   SER C 322      68.410  17.913  -5.758  1.00 63.67           N  
-ATOM   7278  CA  SER C 322      68.933  17.136  -6.881  1.00 64.93           C  
-ATOM   7279  C   SER C 322      68.054  15.922  -7.149  1.00 65.24           C  
-ATOM   7280  O   SER C 322      67.708  15.183  -6.221  1.00 66.23           O  
-ATOM   7281  CB  SER C 322      70.372  16.673  -6.579  1.00 61.18           C  
-ATOM   7282  OG  SER C 322      70.891  15.843  -7.608  1.00 56.74           O  
-ATOM   7283  N   SER C 323      67.678  15.724  -8.411  1.00 64.12           N  
-ATOM   7284  CA  SER C 323      66.868  14.566  -8.764  1.00 63.44           C  
-ATOM   7285  C   SER C 323      67.637  13.335  -8.268  1.00 62.51           C  
-ATOM   7286  O   SER C 323      67.052  12.417  -7.686  1.00 65.30           O  
-ATOM   7287  CB  SER C 323      66.669  14.480 -10.284  1.00 61.33           C  
-ATOM   7288  OG  SER C 323      65.903  13.334 -10.630  1.00 63.00           O  
-ATOM   7289  N   GLY C 324      68.952  13.336  -8.490  1.00 57.13           N  
-ATOM   7290  CA  GLY C 324      69.781  12.227  -8.057  1.00 50.38           C  
-ATOM   7291  C   GLY C 324      69.666  11.996  -6.561  1.00 49.37           C  
-ATOM   7292  O   GLY C 324      69.454  10.863  -6.111  1.00 51.60           O  
-ATOM   7293  N   ALA C 325      69.800  13.072  -5.787  1.00 42.80           N  
-ATOM   7294  CA  ALA C 325      69.718  12.997  -4.330  1.00 40.31           C  
-ATOM   7295  C   ALA C 325      68.417  12.321  -3.853  1.00 40.10           C  
-ATOM   7296  O   ALA C 325      68.446  11.439  -2.980  1.00 34.41           O  
-ATOM   7297  CB  ALA C 325      69.844  14.405  -3.734  1.00 29.01           C  
-ATOM   7298  N   TRP C 326      67.282  12.733  -4.421  1.00 37.59           N  
-ATOM   7299  CA  TRP C 326      66.000  12.144  -4.045  1.00 34.85           C  
-ATOM   7300  C   TRP C 326      66.094  10.609  -4.100  1.00 34.95           C  
-ATOM   7301  O   TRP C 326      65.659   9.919  -3.172  1.00 31.82           O  
-ATOM   7302  CB  TRP C 326      64.880  12.671  -4.964  1.00 30.27           C  
-ATOM   7303  CG  TRP C 326      63.593  11.892  -4.877  1.00 34.69           C  
-ATOM   7304  CD1 TRP C 326      63.271  10.763  -5.579  1.00 36.22           C  
-ATOM   7305  CD2 TRP C 326      62.483  12.150  -4.005  1.00 35.65           C  
-ATOM   7306  NE1 TRP C 326      62.033  10.301  -5.197  1.00 36.16           N  
-ATOM   7307  CE2 TRP C 326      61.525  11.132  -4.234  1.00 36.13           C  
-ATOM   7308  CE3 TRP C 326      62.204  13.138  -3.052  1.00 35.63           C  
-ATOM   7309  CZ2 TRP C 326      60.302  11.074  -3.542  1.00 31.46           C  
-ATOM   7310  CZ3 TRP C 326      60.984  13.081  -2.361  1.00 35.54           C  
-ATOM   7311  CH2 TRP C 326      60.051  12.053  -2.615  1.00 31.36           C  
-ATOM   7312  N   ASN C 327      66.686  10.079  -5.171  1.00 34.70           N  
-ATOM   7313  CA  ASN C 327      66.829   8.630  -5.319  1.00 43.15           C  
-ATOM   7314  C   ASN C 327      67.713   8.079  -4.212  1.00 43.52           C  
-ATOM   7315  O   ASN C 327      67.485   6.970  -3.707  1.00 43.25           O  
-ATOM   7316  CB  ASN C 327      67.425   8.272  -6.689  1.00 49.77           C  
-ATOM   7317  CG  ASN C 327      66.454   8.517  -7.830  1.00 56.44           C  
-ATOM   7318  OD1 ASN C 327      65.320   8.020  -7.818  1.00 49.55           O  
-ATOM   7319  ND2 ASN C 327      66.896   9.283  -8.828  1.00 61.62           N  
-ATOM   7320  N   ILE C 328      68.726   8.860  -3.846  1.00 42.71           N  
-ATOM   7321  CA  ILE C 328      69.641   8.481  -2.773  1.00 45.89           C  
-ATOM   7322  C   ILE C 328      68.844   8.477  -1.466  1.00 43.16           C  
-ATOM   7323  O   ILE C 328      68.682   7.434  -0.819  1.00 44.49           O  
-ATOM   7324  CB  ILE C 328      70.809   9.492  -2.661  1.00 41.72           C  
-ATOM   7325  CG1 ILE C 328      71.813   9.241  -3.791  1.00 38.90           C  
-ATOM   7326  CG2 ILE C 328      71.453   9.404  -1.277  1.00 32.52           C  
-ATOM   7327  CD1 ILE C 328      72.895  10.289  -3.881  1.00 33.56           C  
-ATOM   7328  N   LEU C 329      68.354   9.653  -1.092  1.00 33.54           N  
-ATOM   7329  CA  LEU C 329      67.554   9.807   0.106  1.00 30.39           C  
-ATOM   7330  C   LEU C 329      66.644   8.591   0.279  1.00 34.23           C  
-ATOM   7331  O   LEU C 329      66.637   7.956   1.339  1.00 30.39           O  
-ATOM   7332  CB  LEU C 329      66.704  11.067  -0.016  1.00 29.18           C  
-ATOM   7333  CG  LEU C 329      65.653  11.300   1.067  1.00 24.33           C  
-ATOM   7334  CD1 LEU C 329      66.351  11.418   2.403  1.00 27.39           C  
-ATOM   7335  CD2 LEU C 329      64.846  12.563   0.755  1.00 14.58           C  
-ATOM   7336  N   LYS C 330      65.890   8.271  -0.776  1.00 39.29           N  
-ATOM   7337  CA  LYS C 330      64.963   7.137  -0.765  1.00 46.50           C  
-ATOM   7338  C   LYS C 330      65.623   5.863  -0.281  1.00 50.79           C  
-ATOM   7339  O   LYS C 330      65.071   5.156   0.572  1.00 52.04           O  
-ATOM   7340  CB  LYS C 330      64.392   6.878  -2.160  1.00 48.16           C  
-ATOM   7341  CG  LYS C 330      63.395   7.922  -2.630  1.00 64.32           C  
-ATOM   7342  CD  LYS C 330      62.581   7.418  -3.815  1.00 70.05           C  
-ATOM   7343  CE  LYS C 330      61.834   6.125  -3.466  1.00 82.28           C  
-ATOM   7344  NZ  LYS C 330      60.970   6.251  -2.243  1.00 83.38           N  
-ATOM   7345  N   GLU C 331      66.800   5.575  -0.837  1.00 52.56           N  
-ATOM   7346  CA  GLU C 331      67.560   4.376  -0.481  1.00 54.19           C  
-ATOM   7347  C   GLU C 331      67.930   4.382   0.997  1.00 43.71           C  
-ATOM   7348  O   GLU C 331      67.757   3.384   1.707  1.00 42.93           O  
-ATOM   7349  CB  GLU C 331      68.841   4.282  -1.318  1.00 64.25           C  
-ATOM   7350  CG  GLU C 331      69.616   2.974  -1.116  1.00 76.80           C  
-ATOM   7351  CD  GLU C 331      71.125   3.186  -1.031  1.00 85.01           C  
-ATOM   7352  OE1 GLU C 331      71.703   3.770  -1.978  1.00 91.09           O  
-ATOM   7353  OE2 GLU C 331      71.731   2.765  -0.017  1.00 81.80           O  
-ATOM   7354  N   LEU C 332      68.448   5.513   1.448  1.00 31.33           N  
-ATOM   7355  CA  LEU C 332      68.831   5.653   2.835  1.00 30.38           C  
-ATOM   7356  C   LEU C 332      67.617   5.438   3.709  1.00 30.20           C  
-ATOM   7357  O   LEU C 332      67.645   4.625   4.636  1.00 28.34           O  
-ATOM   7358  CB  LEU C 332      69.399   7.042   3.071  1.00 33.42           C  
-ATOM   7359  CG  LEU C 332      70.515   7.354   2.067  1.00 49.11           C  
-ATOM   7360  CD1 LEU C 332      71.053   8.771   2.350  1.00 47.03           C  
-ATOM   7361  CD2 LEU C 332      71.630   6.270   2.139  1.00 38.18           C  
-ATOM   7362  N   VAL C 333      66.547   6.165   3.402  1.00 30.56           N  
-ATOM   7363  CA  VAL C 333      65.315   6.050   4.169  1.00 34.42           C  
-ATOM   7364  C   VAL C 333      64.866   4.606   4.233  1.00 35.45           C  
-ATOM   7365  O   VAL C 333      64.421   4.126   5.279  1.00 29.72           O  
-ATOM   7366  CB  VAL C 333      64.178   6.850   3.544  1.00 34.01           C  
-ATOM   7367  CG1 VAL C 333      62.934   6.736   4.424  1.00 35.86           C  
-ATOM   7368  CG2 VAL C 333      64.598   8.292   3.373  1.00 40.88           C  
-ATOM   7369  N   ASN C 334      64.975   3.921   3.101  1.00 41.43           N  
-ATOM   7370  CA  ASN C 334      64.582   2.524   3.032  1.00 50.94           C  
-ATOM   7371  C   ASN C 334      65.599   1.654   3.771  1.00 54.57           C  
-ATOM   7372  O   ASN C 334      65.246   0.604   4.327  1.00 53.74           O  
-ATOM   7373  CB  ASN C 334      64.473   2.069   1.577  1.00 54.98           C  
-ATOM   7374  CG  ASN C 334      63.953   0.652   1.456  1.00 70.82           C  
-ATOM   7375  OD1 ASN C 334      62.793   0.376   1.773  1.00 75.48           O  
-ATOM   7376  ND2 ASN C 334      64.812  -0.262   1.010  1.00 76.89           N  
-ATOM   7377  N   ALA C 335      66.856   2.102   3.779  1.00 54.58           N  
-ATOM   7378  CA  ALA C 335      67.937   1.377   4.448  1.00 54.36           C  
-ATOM   7379  C   ALA C 335      67.800   1.345   5.972  1.00 56.34           C  
-ATOM   7380  O   ALA C 335      68.261   0.396   6.611  1.00 59.34           O  
-ATOM   7381  CB  ALA C 335      69.292   1.979   4.072  1.00 40.52           C  
-ATOM   7382  N   VAL C 336      67.168   2.369   6.549  1.00 55.87           N  
-ATOM   7383  CA  VAL C 336      67.004   2.450   8.002  1.00 55.97           C  
-ATOM   7384  C   VAL C 336      65.588   2.160   8.481  1.00 61.57           C  
-ATOM   7385  O   VAL C 336      65.363   1.912   9.673  1.00 60.33           O  
-ATOM   7386  CB  VAL C 336      67.409   3.836   8.524  1.00 51.70           C  
-ATOM   7387  CG1 VAL C 336      68.757   4.236   7.940  1.00 53.01           C  
-ATOM   7388  CG2 VAL C 336      66.348   4.850   8.169  1.00 46.59           C  
-ATOM   7389  N   GLN C 337      64.637   2.204   7.551  1.00 69.90           N  
-ATOM   7390  CA  GLN C 337      63.239   1.931   7.872  1.00 81.84           C  
-ATOM   7391  C   GLN C 337      62.859   0.537   7.375  1.00 86.24           C  
-ATOM   7392  O   GLN C 337      61.763   0.319   6.843  1.00 79.38           O  
-ATOM   7393  CB  GLN C 337      62.326   2.986   7.238  1.00 88.10           C  
-ATOM   7394  CG  GLN C 337      62.454   4.405   7.826  1.00 93.35           C  
-ATOM   7395  CD  GLN C 337      62.023   4.505   9.295  1.00 95.64           C  
-ATOM   7396  OE1 GLN C 337      60.928   4.068   9.669  1.00 97.26           O  
-ATOM   7397  NE2 GLN C 337      62.883   5.097  10.127  1.00 88.66           N  
-ATOM   7398  N   ASP C 338      63.790  -0.396   7.564  1.00 95.82           N  
-ATOM   7399  CA  ASP C 338      63.633  -1.795   7.170  1.00101.53           C  
-ATOM   7400  C   ASP C 338      64.732  -2.599   7.883  1.00 99.70           C  
-ATOM   7401  O   ASP C 338      65.652  -3.109   7.209  1.00 98.24           O  
-ATOM   7402  CB  ASP C 338      63.745  -1.923   5.636  1.00105.04           C  
-ATOM   7403  CG  ASP C 338      63.316  -3.297   5.116  1.00105.86           C  
-ATOM   7404  OD1 ASP C 338      62.385  -3.905   5.698  1.00104.56           O  
-ATOM   7405  OD2 ASP C 338      63.901  -3.755   4.107  1.00101.30           O  
-TER    7406      ASP C 338                                                      
-ATOM   7407  N   VAL D   8      89.289  43.271   2.685  1.00 90.53           N  
-ATOM   7408  CA  VAL D   8      89.094  43.577   4.135  1.00 91.91           C  
-ATOM   7409  C   VAL D   8      88.660  42.319   4.893  1.00 92.02           C  
-ATOM   7410  O   VAL D   8      87.599  42.298   5.518  1.00 92.96           O  
-ATOM   7411  CB  VAL D   8      88.013  44.685   4.338  1.00 90.58           C  
-ATOM   7412  CG1 VAL D   8      87.972  45.122   5.805  1.00 87.21           C  
-ATOM   7413  CG2 VAL D   8      88.304  45.879   3.431  1.00 87.19           C  
-ATOM   7414  N   LYS D   9      89.482  41.272   4.829  1.00 90.43           N  
-ATOM   7415  CA  LYS D   9      89.180  40.008   5.509  1.00 85.90           C  
-ATOM   7416  C   LYS D   9      90.436  39.399   6.148  1.00 82.87           C  
-ATOM   7417  O   LYS D   9      90.787  38.255   5.847  1.00 86.29           O  
-ATOM   7418  CB  LYS D   9      88.597  38.984   4.522  1.00 85.22           C  
-ATOM   7419  CG  LYS D   9      87.533  39.508   3.571  1.00 84.70           C  
-ATOM   7420  CD  LYS D   9      86.250  39.868   4.280  1.00 87.31           C  
-ATOM   7421  CE  LYS D   9      85.188  40.266   3.276  1.00 88.74           C  
-ATOM   7422  NZ  LYS D   9      83.895  40.579   3.938  1.00 85.79           N  
-ATOM   7423  N   MET D  10      91.102  40.153   7.023  1.00 75.22           N  
-ATOM   7424  CA  MET D  10      92.317  39.681   7.698  1.00 67.29           C  
-ATOM   7425  C   MET D  10      92.206  38.238   8.203  1.00 63.09           C  
-ATOM   7426  O   MET D  10      91.106  37.696   8.348  1.00 64.14           O  
-ATOM   7427  CB  MET D  10      92.649  40.588   8.879  1.00 66.72           C  
-ATOM   7428  CG  MET D  10      91.563  40.615   9.933  1.00 71.76           C  
-ATOM   7429  SD  MET D  10      92.109  41.442  11.411  1.00 82.14           S  
-ATOM   7430  CE  MET D  10      91.452  43.104  11.163  1.00 76.82           C  
-ATOM   7431  N   GLY D  11      93.355  37.630   8.487  1.00 54.84           N  
-ATOM   7432  CA  GLY D  11      93.375  36.256   8.958  1.00 47.42           C  
-ATOM   7433  C   GLY D  11      93.628  36.075  10.445  1.00 46.50           C  
-ATOM   7434  O   GLY D  11      94.603  36.598  10.993  1.00 44.47           O  
-ATOM   7435  N   VAL D  12      92.745  35.315  11.094  1.00 46.32           N  
-ATOM   7436  CA  VAL D  12      92.830  35.037  12.532  1.00 37.32           C  
-ATOM   7437  C   VAL D  12      93.385  33.643  12.796  1.00 30.18           C  
-ATOM   7438  O   VAL D  12      93.561  32.841  11.874  1.00 28.47           O  
-ATOM   7439  CB  VAL D  12      91.440  35.125  13.215  1.00 37.46           C  
-ATOM   7440  CG1 VAL D  12      90.823  36.497  12.977  1.00 41.27           C  
-ATOM   7441  CG2 VAL D  12      90.523  34.035  12.678  1.00 38.30           C  
-ATOM   7442  N   LEU D  13      93.633  33.345  14.064  1.00 23.29           N  
-ATOM   7443  CA  LEU D  13      94.184  32.044  14.429  1.00 25.19           C  
-ATOM   7444  C   LEU D  13      93.391  31.407  15.561  1.00 28.32           C  
-ATOM   7445  O   LEU D  13      93.644  31.691  16.734  1.00 29.28           O  
-ATOM   7446  CB  LEU D  13      95.643  32.209  14.857  1.00 19.55           C  
-ATOM   7447  CG  LEU D  13      96.636  31.170  14.351  1.00 12.35           C  
-ATOM   7448  CD1 LEU D  13      96.508  31.023  12.833  1.00 13.57           C  
-ATOM   7449  CD2 LEU D  13      98.038  31.595  14.732  1.00  9.64           C  
-ATOM   7450  N   ARG D  14      92.433  30.548  15.214  1.00 28.30           N  
-ATOM   7451  CA  ARG D  14      91.613  29.889  16.227  1.00 25.20           C  
-ATOM   7452  C   ARG D  14      92.391  28.785  16.920  1.00 22.99           C  
-ATOM   7453  O   ARG D  14      92.793  27.807  16.298  1.00 28.87           O  
-ATOM   7454  CB  ARG D  14      90.324  29.326  15.613  1.00 21.63           C  
-ATOM   7455  CG  ARG D  14      89.297  30.403  15.330  1.00 22.74           C  
-ATOM   7456  CD  ARG D  14      87.876  29.885  15.212  1.00 19.48           C  
-ATOM   7457  NE  ARG D  14      87.627  29.226  13.938  1.00 32.81           N  
-ATOM   7458  CZ  ARG D  14      87.804  27.927  13.726  1.00 44.27           C  
-ATOM   7459  NH1 ARG D  14      88.230  27.151  14.717  1.00 43.39           N  
-ATOM   7460  NH2 ARG D  14      87.558  27.401  12.528  1.00 42.88           N  
-ATOM   7461  N   ILE D  15      92.607  28.955  18.216  1.00 16.18           N  
-ATOM   7462  CA  ILE D  15      93.352  27.981  18.995  1.00 15.24           C  
-ATOM   7463  C   ILE D  15      92.584  27.563  20.248  1.00 24.46           C  
-ATOM   7464  O   ILE D  15      92.357  28.363  21.164  1.00 32.08           O  
-ATOM   7465  CB  ILE D  15      94.715  28.545  19.445  1.00 11.71           C  
-ATOM   7466  CG1 ILE D  15      95.486  29.071  18.244  1.00 18.35           C  
-ATOM   7467  CG2 ILE D  15      95.529  27.466  20.130  1.00  4.47           C  
-ATOM   7468  CD1 ILE D  15      96.802  29.715  18.616  1.00 15.05           C  
-ATOM   7469  N   TYR D  16      92.194  26.297  20.281  1.00 16.35           N  
-ATOM   7470  CA  TYR D  16      91.472  25.746  21.406  1.00  6.73           C  
-ATOM   7471  C   TYR D  16      92.457  24.933  22.230  1.00 10.14           C  
-ATOM   7472  O   TYR D  16      93.127  24.036  21.726  1.00 17.05           O  
-ATOM   7473  CB  TYR D  16      90.341  24.888  20.879  1.00  6.91           C  
-ATOM   7474  CG  TYR D  16      89.291  25.694  20.154  1.00  4.47           C  
-ATOM   7475  CD1 TYR D  16      88.343  26.418  20.864  1.00 12.89           C  
-ATOM   7476  CD2 TYR D  16      89.239  25.726  18.765  1.00  4.47           C  
-ATOM   7477  CE1 TYR D  16      87.355  27.158  20.213  1.00 26.41           C  
-ATOM   7478  CE2 TYR D  16      88.254  26.463  18.096  1.00 16.15           C  
-ATOM   7479  CZ  TYR D  16      87.309  27.178  18.828  1.00 25.67           C  
-ATOM   7480  OH  TYR D  16      86.306  27.902  18.197  1.00 25.16           O  
-ATOM   7481  N   LEU D  17      92.544  25.261  23.505  1.00  9.66           N  
-ATOM   7482  CA  LEU D  17      93.479  24.610  24.402  1.00 16.57           C  
-ATOM   7483  C   LEU D  17      92.754  23.602  25.285  1.00 24.53           C  
-ATOM   7484  O   LEU D  17      91.954  23.990  26.140  1.00 32.14           O  
-ATOM   7485  CB  LEU D  17      94.137  25.698  25.252  1.00 22.17           C  
-ATOM   7486  CG  LEU D  17      95.475  25.483  25.940  1.00 22.52           C  
-ATOM   7487  CD1 LEU D  17      96.494  24.998  24.924  1.00 33.49           C  
-ATOM   7488  CD2 LEU D  17      95.914  26.789  26.574  1.00  6.89           C  
-ATOM   7489  N   ASP D  18      93.024  22.312  25.092  1.00 23.21           N  
-ATOM   7490  CA  ASP D  18      92.359  21.296  25.906  1.00 26.71           C  
-ATOM   7491  C   ASP D  18      93.296  20.394  26.688  1.00 27.98           C  
-ATOM   7492  O   ASP D  18      94.465  20.709  26.888  1.00 31.33           O  
-ATOM   7493  CB  ASP D  18      91.443  20.427  25.045  1.00 29.11           C  
-ATOM   7494  CG  ASP D  18      89.977  20.559  25.440  1.00 40.25           C  
-ATOM   7495  OD1 ASP D  18      89.222  21.253  24.712  1.00 39.14           O  
-ATOM   7496  OD2 ASP D  18      89.589  19.977  26.484  1.00 38.03           O  
-ATOM   7497  N   GLY D  19      92.760  19.265  27.136  1.00 33.24           N  
-ATOM   7498  CA  GLY D  19      93.542  18.311  27.901  1.00 35.63           C  
-ATOM   7499  C   GLY D  19      92.802  17.946  29.173  1.00 38.76           C  
-ATOM   7500  O   GLY D  19      91.622  18.298  29.322  1.00 42.05           O  
-ATOM   7501  N   ALA D  20      93.484  17.247  30.080  1.00 33.72           N  
-ATOM   7502  CA  ALA D  20      92.893  16.843  31.349  1.00 36.24           C  
-ATOM   7503  C   ALA D  20      92.587  18.067  32.223  1.00 48.91           C  
-ATOM   7504  O   ALA D  20      92.873  19.211  31.836  1.00 49.87           O  
-ATOM   7505  CB  ALA D  20      93.833  15.911  32.069  1.00 26.86           C  
-ATOM   7506  N   TYR D  21      92.004  17.834  33.398  1.00 56.81           N  
-ATOM   7507  CA  TYR D  21      91.668  18.938  34.298  1.00 66.71           C  
-ATOM   7508  C   TYR D  21      92.636  19.063  35.469  1.00 74.44           C  
-ATOM   7509  O   TYR D  21      93.291  18.088  35.853  1.00 80.96           O  
-ATOM   7510  CB  TYR D  21      90.231  18.792  34.821  1.00 66.77           C  
-ATOM   7511  CG  TYR D  21      89.999  17.680  35.830  1.00 68.20           C  
-ATOM   7512  CD1 TYR D  21      90.369  17.828  37.168  1.00 64.20           C  
-ATOM   7513  CD2 TYR D  21      89.364  16.496  35.452  1.00 73.92           C  
-ATOM   7514  CE1 TYR D  21      90.107  16.829  38.103  1.00 66.82           C  
-ATOM   7515  CE2 TYR D  21      89.096  15.490  36.380  1.00 73.64           C  
-ATOM   7516  CZ  TYR D  21      89.467  15.663  37.702  1.00 71.53           C  
-ATOM   7517  OH  TYR D  21      89.177  14.676  38.618  1.00 70.75           O  
-ATOM   7518  N   GLY D  22      92.717  20.269  36.030  1.00 75.96           N  
-ATOM   7519  CA  GLY D  22      93.605  20.515  37.153  1.00 77.58           C  
-ATOM   7520  C   GLY D  22      95.060  20.585  36.728  1.00 78.16           C  
-ATOM   7521  O   GLY D  22      95.915  21.009  37.507  1.00 81.13           O  
-ATOM   7522  N   ILE D  23      95.339  20.171  35.492  1.00 75.61           N  
-ATOM   7523  CA  ILE D  23      96.697  20.174  34.951  1.00 72.60           C  
-ATOM   7524  C   ILE D  23      97.343  21.559  34.934  1.00 72.74           C  
-ATOM   7525  O   ILE D  23      98.566  21.680  35.012  1.00 77.77           O  
-ATOM   7526  CB  ILE D  23      96.733  19.603  33.507  1.00 71.15           C  
-ATOM   7527  CG1 ILE D  23      95.622  20.235  32.659  1.00 72.13           C  
-ATOM   7528  CG2 ILE D  23      96.606  18.090  33.541  1.00 70.31           C  
-ATOM   7529  CD1 ILE D  23      95.690  19.883  31.172  1.00 67.81           C  
-ATOM   7530  N   GLY D  24      96.529  22.602  34.822  1.00 67.33           N  
-ATOM   7531  CA  GLY D  24      97.080  23.944  34.808  1.00 63.58           C  
-ATOM   7532  C   GLY D  24      97.046  24.614  33.452  1.00 61.02           C  
-ATOM   7533  O   GLY D  24      97.819  25.539  33.194  1.00 62.38           O  
-ATOM   7534  N   LYS D  25      96.147  24.154  32.586  1.00 58.48           N  
-ATOM   7535  CA  LYS D  25      96.020  24.718  31.250  1.00 56.49           C  
-ATOM   7536  C   LYS D  25      95.355  26.092  31.228  1.00 57.95           C  
-ATOM   7537  O   LYS D  25      95.139  26.662  30.156  1.00 55.84           O  
-ATOM   7538  CB  LYS D  25      95.255  23.758  30.331  1.00 53.71           C  
-ATOM   7539  CG  LYS D  25      94.185  22.932  31.011  1.00 51.42           C  
-ATOM   7540  CD  LYS D  25      93.211  22.369  29.999  1.00 48.97           C  
-ATOM   7541  CE  LYS D  25      92.370  23.494  29.410  1.00 44.99           C  
-ATOM   7542  NZ  LYS D  25      91.689  24.279  30.490  1.00 34.95           N  
-ATOM   7543  N   THR D  26      95.026  26.622  32.404  1.00 63.40           N  
-ATOM   7544  CA  THR D  26      94.406  27.943  32.481  1.00 67.90           C  
-ATOM   7545  C   THR D  26      95.415  28.985  32.975  1.00 70.84           C  
-ATOM   7546  O   THR D  26      95.530  30.060  32.385  1.00 70.86           O  
-ATOM   7547  CB  THR D  26      93.149  27.944  33.401  1.00 64.95           C  
-ATOM   7548  OG1 THR D  26      92.114  27.147  32.809  1.00 64.50           O  
-ATOM   7549  CG2 THR D  26      92.625  29.357  33.580  1.00 65.52           C  
-ATOM   7550  N   THR D  27      96.158  28.666  34.036  1.00 73.49           N  
-ATOM   7551  CA  THR D  27      97.149  29.603  34.568  1.00 73.77           C  
-ATOM   7552  C   THR D  27      98.339  29.676  33.608  1.00 71.01           C  
-ATOM   7553  O   THR D  27      99.201  30.550  33.720  1.00 68.38           O  
-ATOM   7554  CB  THR D  27      97.657  29.177  35.972  1.00 76.16           C  
-ATOM   7555  OG1 THR D  27      96.642  28.429  36.655  1.00 75.28           O  
-ATOM   7556  CG2 THR D  27      97.979  30.416  36.808  1.00 75.49           C  
-ATOM   7557  N   ALA D  28      98.369  28.748  32.660  1.00 70.55           N  
-ATOM   7558  CA  ALA D  28      99.429  28.692  31.665  1.00 71.06           C  
-ATOM   7559  C   ALA D  28      98.916  29.281  30.352  1.00 71.44           C  
-ATOM   7560  O   ALA D  28      99.699  29.592  29.449  1.00 68.93           O  
-ATOM   7561  CB  ALA D  28      99.878  27.243  31.459  1.00 71.76           C  
-ATOM   7562  N   ALA D  29      97.594  29.423  30.254  1.00 73.61           N  
-ATOM   7563  CA  ALA D  29      96.955  29.981  29.062  1.00 72.98           C  
-ATOM   7564  C   ALA D  29      96.808  31.478  29.265  1.00 72.27           C  
-ATOM   7565  O   ALA D  29      96.633  32.234  28.310  1.00 73.15           O  
-ATOM   7566  CB  ALA D  29      95.579  29.342  28.833  1.00 70.58           C  
-ATOM   7567  N   GLU D  30      96.869  31.896  30.524  1.00 75.17           N  
-ATOM   7568  CA  GLU D  30      96.773  33.309  30.867  1.00 77.86           C  
-ATOM   7569  C   GLU D  30      98.170  33.924  30.801  1.00 78.79           C  
-ATOM   7570  O   GLU D  30      98.348  35.015  30.263  1.00 77.90           O  
-ATOM   7571  CB  GLU D  30      96.193  33.488  32.272  1.00 80.67           C  
-ATOM   7572  CG  GLU D  30      94.716  33.125  32.397  1.00 90.25           C  
-ATOM   7573  CD  GLU D  30      94.149  33.427  33.781  1.00 98.00           C  
-ATOM   7574  OE1 GLU D  30      94.212  34.600  34.208  1.00103.84           O  
-ATOM   7575  OE2 GLU D  30      93.636  32.498  34.442  1.00 98.15           O  
-ATOM   7576  N   GLU D  31      99.161  33.215  31.338  1.00 79.40           N  
-ATOM   7577  CA  GLU D  31     100.537  33.702  31.322  1.00 76.91           C  
-ATOM   7578  C   GLU D  31     101.000  33.884  29.873  1.00 72.83           C  
-ATOM   7579  O   GLU D  31     102.062  34.448  29.615  1.00 70.96           O  
-ATOM   7580  CB  GLU D  31     101.464  32.717  32.047  1.00 80.83           C  
-ATOM   7581  CG  GLU D  31     102.481  33.373  32.982  1.00 85.93           C  
-ATOM   7582  CD  GLU D  31     103.355  34.407  32.288  1.00 94.87           C  
-ATOM   7583  OE1 GLU D  31     104.026  34.054  31.293  1.00101.30           O  
-ATOM   7584  OE2 GLU D  31     103.375  35.574  32.740  1.00 92.77           O  
-ATOM   7585  N   PHE D  32     100.201  33.395  28.929  1.00 68.99           N  
-ATOM   7586  CA  PHE D  32     100.528  33.529  27.517  1.00 69.17           C  
-ATOM   7587  C   PHE D  32      99.891  34.802  26.978  1.00 73.51           C  
-ATOM   7588  O   PHE D  32     100.335  35.358  25.974  1.00 76.35           O  
-ATOM   7589  CB  PHE D  32      99.999  32.338  26.731  1.00 65.39           C  
-ATOM   7590  CG  PHE D  32     100.263  32.424  25.252  1.00 59.03           C  
-ATOM   7591  CD1 PHE D  32     101.557  32.300  24.756  1.00 52.44           C  
-ATOM   7592  CD2 PHE D  32      99.214  32.616  24.353  1.00 50.42           C  
-ATOM   7593  CE1 PHE D  32     101.803  32.362  23.394  1.00 43.94           C  
-ATOM   7594  CE2 PHE D  32      99.450  32.678  22.990  1.00 36.69           C  
-ATOM   7595  CZ  PHE D  32     100.746  32.550  22.508  1.00 40.88           C  
-ATOM   7596  N   LEU D  33      98.844  35.254  27.659  1.00 76.95           N  
-ATOM   7597  CA  LEU D  33      98.119  36.459  27.270  1.00 80.52           C  
-ATOM   7598  C   LEU D  33      98.800  37.742  27.765  1.00 87.19           C  
-ATOM   7599  O   LEU D  33      98.999  38.672  26.990  1.00 86.55           O  
-ATOM   7600  CB  LEU D  33      96.682  36.387  27.797  1.00 73.58           C  
-ATOM   7601  CG  LEU D  33      95.724  37.541  27.496  1.00 63.42           C  
-ATOM   7602  CD1 LEU D  33      95.632  37.772  26.004  1.00 62.40           C  
-ATOM   7603  CD2 LEU D  33      94.360  37.210  28.062  1.00 58.41           C  
-ATOM   7604  N   HIS D  34      99.133  37.807  29.053  1.00 96.29           N  
-ATOM   7605  CA  HIS D  34      99.813  38.985  29.607  1.00 98.85           C  
-ATOM   7606  C   HIS D  34     101.148  39.140  28.870  1.00101.29           C  
-ATOM   7607  O   HIS D  34     101.676  40.248  28.729  1.00101.21           O  
-ATOM   7608  CB  HIS D  34     100.097  38.796  31.107  1.00 96.36           C  
-ATOM   7609  CG  HIS D  34      98.867  38.725  31.958  1.00 98.49           C  
-ATOM   7610  ND1 HIS D  34      97.787  37.928  31.644  1.00 98.40           N  
-ATOM   7611  CD2 HIS D  34      98.555  39.339  33.123  1.00100.00           C  
-ATOM   7612  CE1 HIS D  34      96.862  38.054  32.578  1.00 95.93           C  
-ATOM   7613  NE2 HIS D  34      97.303  38.904  33.488  1.00 99.65           N  
-ATOM   7614  N   HIS D  35     101.663  38.007  28.392  1.00102.50           N  
-ATOM   7615  CA  HIS D  35     102.945  37.913  27.693  1.00100.76           C  
-ATOM   7616  C   HIS D  35     103.007  38.514  26.299  1.00 97.69           C  
-ATOM   7617  O   HIS D  35     103.846  39.378  26.028  1.00100.77           O  
-ATOM   7618  CB  HIS D  35     103.378  36.443  27.601  1.00104.65           C  
-ATOM   7619  CG  HIS D  35     104.741  36.176  28.162  1.00111.34           C  
-ATOM   7620  ND1 HIS D  35     105.298  34.915  28.190  1.00109.10           N  
-ATOM   7621  CD2 HIS D  35     105.648  37.002  28.738  1.00114.51           C  
-ATOM   7622  CE1 HIS D  35     106.488  34.975  28.762  1.00113.63           C  
-ATOM   7623  NE2 HIS D  35     106.724  36.230  29.103  1.00115.80           N  
-ATOM   7624  N   PHE D  36     102.135  38.052  25.410  1.00 94.09           N  
-ATOM   7625  CA  PHE D  36     102.163  38.552  24.046  1.00 94.88           C  
-ATOM   7626  C   PHE D  36     100.914  39.311  23.589  1.00 95.65           C  
-ATOM   7627  O   PHE D  36     100.466  39.190  22.439  1.00 92.32           O  
-ATOM   7628  CB  PHE D  36     102.527  37.395  23.106  1.00 92.00           C  
-ATOM   7629  CG  PHE D  36     103.745  36.621  23.567  1.00 95.15           C  
-ATOM   7630  CD1 PHE D  36     103.608  35.391  24.217  1.00 96.38           C  
-ATOM   7631  CD2 PHE D  36     105.027  37.159  23.422  1.00 93.64           C  
-ATOM   7632  CE1 PHE D  36     104.729  34.710  24.721  1.00 94.36           C  
-ATOM   7633  CE2 PHE D  36     106.154  36.488  23.923  1.00 93.54           C  
-ATOM   7634  CZ  PHE D  36     106.004  35.263  24.573  1.00 93.13           C  
-ATOM   7635  N   ALA D  37     100.369  40.097  24.523  1.00 96.86           N  
-ATOM   7636  CA  ALA D  37      99.218  40.969  24.281  1.00 98.36           C  
-ATOM   7637  C   ALA D  37      99.737  42.395  24.494  1.00 99.40           C  
-ATOM   7638  O   ALA D  37      99.008  43.278  24.964  1.00 98.89           O  
-ATOM   7639  CB  ALA D  37      98.079  40.675  25.262  1.00 95.57           C  
-ATOM   7640  N   ILE D  38     101.016  42.592  24.163  1.00 99.21           N  
-ATOM   7641  CA  ILE D  38     101.684  43.891  24.284  1.00 95.01           C  
-ATOM   7642  C   ILE D  38     100.811  44.879  23.511  1.00 90.68           C  
-ATOM   7643  O   ILE D  38     100.595  46.021  23.930  1.00 84.79           O  
-ATOM   7644  CB  ILE D  38     103.117  43.834  23.664  1.00 93.63           C  
-ATOM   7645  CG1 ILE D  38     103.916  42.679  24.295  1.00 87.23           C  
-ATOM   7646  CG2 ILE D  38     103.840  45.160  23.884  1.00 89.09           C  
-ATOM   7647  CD1 ILE D  38     105.290  42.446  23.678  1.00 79.68           C  
-ATOM   7648  N   THR D  39     100.315  44.400  22.374  1.00 89.50           N  
-ATOM   7649  CA  THR D  39      99.415  45.150  21.513  1.00 86.85           C  
-ATOM   7650  C   THR D  39      98.020  44.550  21.781  1.00 84.82           C  
-ATOM   7651  O   THR D  39      97.697  43.456  21.313  1.00 84.09           O  
-ATOM   7652  CB  THR D  39      99.833  45.012  20.004  1.00 84.32           C  
-ATOM   7653  OG1 THR D  39      98.666  44.961  19.174  1.00 83.27           O  
-ATOM   7654  CG2 THR D  39     100.692  43.764  19.778  1.00 75.36           C  
-ATOM   7655  N   PRO D  40      97.189  45.265  22.564  1.00 82.11           N  
-ATOM   7656  CA  PRO D  40      95.826  44.892  22.963  1.00 75.97           C  
-ATOM   7657  C   PRO D  40      94.951  44.157  21.954  1.00 72.33           C  
-ATOM   7658  O   PRO D  40      94.432  43.083  22.256  1.00 71.30           O  
-ATOM   7659  CB  PRO D  40      95.214  46.226  23.375  1.00 79.24           C  
-ATOM   7660  CG  PRO D  40      96.370  46.924  23.997  1.00 84.90           C  
-ATOM   7661  CD  PRO D  40      97.489  46.643  23.006  1.00 86.16           C  
-ATOM   7662  N   ASN D  41      94.781  44.731  20.766  1.00 67.10           N  
-ATOM   7663  CA  ASN D  41      93.927  44.122  19.751  1.00 61.11           C  
-ATOM   7664  C   ASN D  41      94.560  42.987  18.954  1.00 56.17           C  
-ATOM   7665  O   ASN D  41      94.100  42.672  17.855  1.00 55.84           O  
-ATOM   7666  CB  ASN D  41      93.413  45.193  18.776  1.00 66.94           C  
-ATOM   7667  CG  ASN D  41      91.884  45.291  18.753  1.00 66.43           C  
-ATOM   7668  OD1 ASN D  41      91.295  45.803  17.797  1.00 62.26           O  
-ATOM   7669  ND2 ASN D  41      91.241  44.811  19.811  1.00 68.37           N  
-ATOM   7670  N   ARG D  42      95.601  42.357  19.484  1.00 53.99           N  
-ATOM   7671  CA  ARG D  42      96.210  41.269  18.729  1.00 57.43           C  
-ATOM   7672  C   ARG D  42      95.811  39.910  19.263  1.00 54.04           C  
-ATOM   7673  O   ARG D  42      96.079  38.897  18.627  1.00 60.57           O  
-ATOM   7674  CB  ARG D  42      97.742  41.360  18.723  1.00 64.57           C  
-ATOM   7675  CG  ARG D  42      98.365  40.514  17.604  1.00 71.07           C  
-ATOM   7676  CD  ARG D  42      99.841  40.194  17.819  1.00 78.69           C  
-ATOM   7677  NE  ARG D  42     100.303  39.187  16.860  1.00 82.29           N  
-ATOM   7678  CZ  ARG D  42     101.444  38.506  16.966  1.00 85.94           C  
-ATOM   7679  NH1 ARG D  42     102.261  38.718  17.995  1.00 89.68           N  
-ATOM   7680  NH2 ARG D  42     101.761  37.596  16.049  1.00 81.72           N  
-ATOM   7681  N   ILE D  43      95.154  39.879  20.417  1.00 48.42           N  
-ATOM   7682  CA  ILE D  43      94.767  38.604  21.010  1.00 40.92           C  
-ATOM   7683  C   ILE D  43      93.478  38.660  21.829  1.00 35.43           C  
-ATOM   7684  O   ILE D  43      93.237  39.605  22.580  1.00 43.69           O  
-ATOM   7685  CB  ILE D  43      95.911  38.082  21.893  1.00 40.14           C  
-ATOM   7686  CG1 ILE D  43      95.582  36.691  22.417  1.00 30.19           C  
-ATOM   7687  CG2 ILE D  43      96.169  39.058  23.038  1.00 42.71           C  
-ATOM   7688  CD1 ILE D  43      96.724  36.091  23.200  1.00 34.44           C  
-ATOM   7689  N   LEU D  44      92.657  37.629  21.691  1.00 25.47           N  
-ATOM   7690  CA  LEU D  44      91.388  37.572  22.395  1.00 21.24           C  
-ATOM   7691  C   LEU D  44      91.237  36.284  23.169  1.00 23.22           C  
-ATOM   7692  O   LEU D  44      91.264  35.214  22.573  1.00 34.37           O  
-ATOM   7693  CB  LEU D  44      90.242  37.667  21.392  1.00 16.82           C  
-ATOM   7694  CG  LEU D  44      88.863  37.311  21.947  1.00 16.05           C  
-ATOM   7695  CD1 LEU D  44      88.565  38.177  23.183  1.00 25.96           C  
-ATOM   7696  CD2 LEU D  44      87.810  37.509  20.859  1.00 15.99           C  
-ATOM   7697  N   LEU D  45      91.060  36.367  24.484  1.00 16.80           N  
-ATOM   7698  CA  LEU D  45      90.897  35.145  25.256  1.00 15.41           C  
-ATOM   7699  C   LEU D  45      89.450  34.855  25.655  1.00 19.04           C  
-ATOM   7700  O   LEU D  45      88.665  35.764  25.925  1.00 24.21           O  
-ATOM   7701  CB  LEU D  45      91.781  35.161  26.505  1.00 11.16           C  
-ATOM   7702  CG  LEU D  45      91.592  33.894  27.360  1.00 31.90           C  
-ATOM   7703  CD1 LEU D  45      92.010  32.657  26.575  1.00 33.03           C  
-ATOM   7704  CD2 LEU D  45      92.394  33.998  28.642  1.00 44.07           C  
-ATOM   7705  N   ILE D  46      89.104  33.573  25.680  1.00 17.85           N  
-ATOM   7706  CA  ILE D  46      87.768  33.141  26.061  1.00 20.26           C  
-ATOM   7707  C   ILE D  46      87.941  32.073  27.125  1.00 23.24           C  
-ATOM   7708  O   ILE D  46      88.413  30.986  26.821  1.00 29.54           O  
-ATOM   7709  CB  ILE D  46      87.025  32.517  24.877  1.00 17.62           C  
-ATOM   7710  CG1 ILE D  46      86.878  33.542  23.755  1.00 21.63           C  
-ATOM   7711  CG2 ILE D  46      85.659  32.039  25.321  1.00 28.07           C  
-ATOM   7712  CD1 ILE D  46      86.125  33.013  22.555  1.00 15.30           C  
-ATOM   7713  N   GLY D  47      87.560  32.375  28.362  1.00 25.21           N  
-ATOM   7714  CA  GLY D  47      87.714  31.404  29.437  1.00 29.01           C  
-ATOM   7715  C   GLY D  47      86.539  30.467  29.659  1.00 27.95           C  
-ATOM   7716  O   GLY D  47      85.419  30.735  29.221  1.00 31.88           O  
-ATOM   7717  N   GLU D  48      86.795  29.355  30.338  1.00 24.33           N  
-ATOM   7718  CA  GLU D  48      85.739  28.397  30.613  1.00 25.27           C  
-ATOM   7719  C   GLU D  48      84.604  29.130  31.301  1.00 21.53           C  
-ATOM   7720  O   GLU D  48      84.843  29.959  32.165  1.00 32.18           O  
-ATOM   7721  CB  GLU D  48      86.263  27.277  31.501  1.00 34.25           C  
-ATOM   7722  CG  GLU D  48      87.118  26.252  30.751  1.00 47.78           C  
-ATOM   7723  CD  GLU D  48      87.479  25.040  31.611  1.00 58.04           C  
-ATOM   7724  OE1 GLU D  48      88.031  24.054  31.069  1.00 48.01           O  
-ATOM   7725  OE2 GLU D  48      87.210  25.080  32.835  1.00 65.97           O  
-ATOM   7726  N   PRO D  49      83.352  28.843  30.921  1.00 14.04           N  
-ATOM   7727  CA  PRO D  49      82.179  29.490  31.507  1.00 17.74           C  
-ATOM   7728  C   PRO D  49      81.669  28.872  32.818  1.00 23.14           C  
-ATOM   7729  O   PRO D  49      80.517  28.435  32.897  1.00 23.76           O  
-ATOM   7730  CB  PRO D  49      81.161  29.381  30.390  1.00  4.47           C  
-ATOM   7731  CG  PRO D  49      81.443  28.018  29.895  1.00  5.35           C  
-ATOM   7732  CD  PRO D  49      82.950  28.010  29.782  1.00  8.90           C  
-ATOM   7733  N   LEU D  50      82.516  28.855  33.848  1.00 23.99           N  
-ATOM   7734  CA  LEU D  50      82.132  28.293  35.140  1.00 19.14           C  
-ATOM   7735  C   LEU D  50      80.828  28.895  35.606  1.00 23.02           C  
-ATOM   7736  O   LEU D  50      79.955  28.174  36.081  1.00 29.65           O  
-ATOM   7737  CB  LEU D  50      83.191  28.561  36.203  1.00 13.14           C  
-ATOM   7738  CG  LEU D  50      84.652  28.303  35.838  1.00 25.46           C  
-ATOM   7739  CD1 LEU D  50      85.488  28.485  37.096  1.00 33.85           C  
-ATOM   7740  CD2 LEU D  50      84.835  26.905  35.254  1.00 30.54           C  
-ATOM   7741  N   SER D  51      80.697  30.215  35.463  1.00 27.03           N  
-ATOM   7742  CA  SER D  51      79.487  30.927  35.888  1.00 30.69           C  
-ATOM   7743  C   SER D  51      78.184  30.269  35.420  1.00 32.99           C  
-ATOM   7744  O   SER D  51      77.154  30.374  36.102  1.00 41.37           O  
-ATOM   7745  CB  SER D  51      79.533  32.397  35.437  1.00 28.27           C  
-ATOM   7746  OG  SER D  51      80.039  32.532  34.123  1.00 30.61           O  
-ATOM   7747  N   TYR D  52      78.220  29.587  34.273  1.00 23.10           N  
-ATOM   7748  CA  TYR D  52      77.023  28.914  33.773  1.00 14.85           C  
-ATOM   7749  C   TYR D  52      76.989  27.471  34.258  1.00  8.74           C  
-ATOM   7750  O   TYR D  52      75.929  26.916  34.562  1.00  7.07           O  
-ATOM   7751  CB  TYR D  52      76.954  28.941  32.233  1.00 11.38           C  
-ATOM   7752  CG  TYR D  52      76.563  30.283  31.615  1.00 10.34           C  
-ATOM   7753  CD1 TYR D  52      77.503  31.295  31.455  1.00 12.96           C  
-ATOM   7754  CD2 TYR D  52      75.246  30.544  31.224  1.00  4.47           C  
-ATOM   7755  CE1 TYR D  52      77.152  32.528  30.928  1.00 16.44           C  
-ATOM   7756  CE2 TYR D  52      74.883  31.775  30.701  1.00 11.48           C  
-ATOM   7757  CZ  TYR D  52      75.846  32.771  30.555  1.00 23.31           C  
-ATOM   7758  OH  TYR D  52      75.517  34.021  30.047  1.00 38.07           O  
-ATOM   7759  N   TRP D  53      78.152  26.853  34.332  1.00  4.47           N  
-ATOM   7760  CA  TRP D  53      78.168  25.488  34.788  1.00  4.70           C  
-ATOM   7761  C   TRP D  53      77.702  25.443  36.235  1.00 12.02           C  
-ATOM   7762  O   TRP D  53      76.950  24.552  36.623  1.00 18.01           O  
-ATOM   7763  CB  TRP D  53      79.573  24.885  34.692  1.00  5.15           C  
-ATOM   7764  CG  TRP D  53      80.087  24.721  33.309  1.00  7.44           C  
-ATOM   7765  CD1 TRP D  53      79.357  24.690  32.154  1.00 12.67           C  
-ATOM   7766  CD2 TRP D  53      81.449  24.546  32.925  1.00  5.30           C  
-ATOM   7767  NE1 TRP D  53      80.186  24.510  31.072  1.00  6.94           N  
-ATOM   7768  CE2 TRP D  53      81.476  24.421  31.521  1.00  4.47           C  
-ATOM   7769  CE3 TRP D  53      82.651  24.484  33.633  1.00 10.03           C  
-ATOM   7770  CZ2 TRP D  53      82.657  24.239  30.813  1.00 11.63           C  
-ATOM   7771  CZ3 TRP D  53      83.825  24.301  32.927  1.00 16.64           C  
-ATOM   7772  CH2 TRP D  53      83.820  24.181  31.528  1.00 15.71           C  
-ATOM   7773  N   ARG D  54      78.136  26.404  37.041  1.00  8.92           N  
-ATOM   7774  CA  ARG D  54      77.768  26.375  38.447  1.00  8.18           C  
-ATOM   7775  C   ARG D  54      76.392  26.915  38.720  1.00 11.22           C  
-ATOM   7776  O   ARG D  54      75.997  27.100  39.873  1.00 18.22           O  
-ATOM   7777  CB  ARG D  54      78.807  27.103  39.297  1.00  9.47           C  
-ATOM   7778  CG  ARG D  54      80.052  26.268  39.531  1.00 20.33           C  
-ATOM   7779  CD  ARG D  54      80.898  26.816  40.679  1.00 44.94           C  
-ATOM   7780  NE  ARG D  54      82.051  25.959  40.961  1.00 47.90           N  
-ATOM   7781  CZ  ARG D  54      81.960  24.706  41.390  1.00 49.27           C  
-ATOM   7782  NH1 ARG D  54      80.771  24.161  41.591  1.00 47.33           N  
-ATOM   7783  NH2 ARG D  54      83.057  23.995  41.614  1.00 57.21           N  
-ATOM   7784  N   ASN D  55      75.661  27.176  37.651  1.00 12.70           N  
-ATOM   7785  CA  ASN D  55      74.300  27.658  37.784  1.00 16.67           C  
-ATOM   7786  C   ASN D  55      73.606  27.559  36.449  1.00 10.99           C  
-ATOM   7787  O   ASN D  55      73.018  28.526  35.964  1.00  6.92           O  
-ATOM   7788  CB  ASN D  55      74.254  29.103  38.261  1.00 22.87           C  
-ATOM   7789  CG  ASN D  55      72.841  29.641  38.289  1.00 33.36           C  
-ATOM   7790  OD1 ASN D  55      71.966  29.090  38.961  1.00 35.78           O  
-ATOM   7791  ND2 ASN D  55      72.603  30.707  37.542  1.00 39.33           N  
-ATOM   7792  N   LEU D  56      73.679  26.386  35.845  1.00  4.47           N  
-ATOM   7793  CA  LEU D  56      73.049  26.229  34.562  1.00  5.93           C  
-ATOM   7794  C   LEU D  56      71.554  25.944  34.711  1.00 14.09           C  
-ATOM   7795  O   LEU D  56      71.131  24.817  34.967  1.00 10.78           O  
-ATOM   7796  CB  LEU D  56      73.741  25.131  33.781  1.00  4.47           C  
-ATOM   7797  CG  LEU D  56      73.389  25.240  32.308  1.00 10.71           C  
-ATOM   7798  CD1 LEU D  56      74.447  24.531  31.497  1.00 21.35           C  
-ATOM   7799  CD2 LEU D  56      72.006  24.664  32.059  1.00 12.55           C  
-ATOM   7800  N   ALA D  57      70.751  26.990  34.560  1.00 18.71           N  
-ATOM   7801  CA  ALA D  57      69.310  26.852  34.670  1.00 13.94           C  
-ATOM   7802  C   ALA D  57      68.893  26.160  35.957  1.00 15.92           C  
-ATOM   7803  O   ALA D  57      67.937  25.388  35.972  1.00 17.24           O  
-ATOM   7804  CB  ALA D  57      68.786  26.082  33.497  1.00 14.89           C  
-ATOM   7805  N   GLY D  58      69.619  26.408  37.038  1.00 19.89           N  
-ATOM   7806  CA  GLY D  58      69.218  25.804  38.293  1.00 22.47           C  
-ATOM   7807  C   GLY D  58      70.136  24.793  38.941  1.00 20.10           C  
-ATOM   7808  O   GLY D  58      70.225  24.735  40.165  1.00 31.67           O  
-ATOM   7809  N   GLU D  59      70.831  23.994  38.152  1.00 10.35           N  
-ATOM   7810  CA  GLU D  59      71.700  22.997  38.750  1.00  8.36           C  
-ATOM   7811  C   GLU D  59      73.185  23.294  38.549  1.00  8.12           C  
-ATOM   7812  O   GLU D  59      73.568  24.005  37.626  1.00  4.47           O  
-ATOM   7813  CB  GLU D  59      71.319  21.616  38.211  1.00  9.53           C  
-ATOM   7814  CG  GLU D  59      69.797  21.411  38.200  1.00 20.80           C  
-ATOM   7815  CD  GLU D  59      69.362  19.970  38.003  1.00 20.24           C  
-ATOM   7816  OE1 GLU D  59      69.814  19.323  37.040  1.00 17.37           O  
-ATOM   7817  OE2 GLU D  59      68.550  19.489  38.815  1.00 25.05           O  
-ATOM   7818  N   ASP D  60      74.012  22.767  39.445  1.00 11.46           N  
-ATOM   7819  CA  ASP D  60      75.452  22.978  39.387  1.00 11.71           C  
-ATOM   7820  C   ASP D  60      76.124  21.773  38.769  1.00  9.03           C  
-ATOM   7821  O   ASP D  60      76.580  20.887  39.476  1.00 16.31           O  
-ATOM   7822  CB  ASP D  60      76.008  23.181  40.793  1.00 24.67           C  
-ATOM   7823  CG  ASP D  60      77.516  23.343  40.804  1.00 36.59           C  
-ATOM   7824  OD1 ASP D  60      78.217  22.468  40.236  1.00 29.81           O  
-ATOM   7825  OD2 ASP D  60      77.994  24.348  41.387  1.00 44.44           O  
-ATOM   7826  N   ALA D  61      76.194  21.743  37.448  1.00  9.79           N  
-ATOM   7827  CA  ALA D  61      76.811  20.623  36.750  1.00  8.04           C  
-ATOM   7828  C   ALA D  61      77.981  20.019  37.499  1.00  6.16           C  
-ATOM   7829  O   ALA D  61      78.011  18.813  37.719  1.00 10.55           O  
-ATOM   7830  CB  ALA D  61      77.263  21.047  35.370  1.00  4.47           C  
-ATOM   7831  N   ILE D  62      78.944  20.843  37.899  1.00  6.84           N  
-ATOM   7832  CA  ILE D  62      80.101  20.298  38.597  1.00 13.16           C  
-ATOM   7833  C   ILE D  62      79.782  19.523  39.871  1.00 18.45           C  
-ATOM   7834  O   ILE D  62      80.097  18.328  39.970  1.00 19.82           O  
-ATOM   7835  CB  ILE D  62      81.127  21.374  38.907  1.00 12.16           C  
-ATOM   7836  CG1 ILE D  62      81.840  21.764  37.609  1.00 10.20           C  
-ATOM   7837  CG2 ILE D  62      82.100  20.865  39.966  1.00  7.30           C  
-ATOM   7838  CD1 ILE D  62      83.068  22.628  37.802  1.00 21.23           C  
-ATOM   7839  N   CYS D  63      79.170  20.182  40.847  1.00  4.47           N  
-ATOM   7840  CA  CYS D  63      78.817  19.487  42.073  1.00 14.34           C  
-ATOM   7841  C   CYS D  63      78.053  18.196  41.752  1.00 10.54           C  
-ATOM   7842  O   CYS D  63      78.386  17.123  42.250  1.00 16.85           O  
-ATOM   7843  CB  CYS D  63      77.951  20.378  42.947  1.00 23.21           C  
-ATOM   7844  SG  CYS D  63      77.616  19.714  44.585  1.00 51.78           S  
-ATOM   7845  N   GLY D  64      77.039  18.313  40.904  1.00 10.02           N  
-ATOM   7846  CA  GLY D  64      76.224  17.169  40.522  1.00 12.14           C  
-ATOM   7847  C   GLY D  64      76.949  15.987  39.886  1.00 15.28           C  
-ATOM   7848  O   GLY D  64      76.591  14.824  40.102  1.00 15.37           O  
-ATOM   7849  N   ILE D  65      77.970  16.256  39.091  1.00  6.84           N  
-ATOM   7850  CA  ILE D  65      78.665  15.151  38.491  1.00  4.47           C  
-ATOM   7851  C   ILE D  65      79.484  14.451  39.556  1.00  7.60           C  
-ATOM   7852  O   ILE D  65      79.596  13.234  39.541  1.00 15.66           O  
-ATOM   7853  CB  ILE D  65      79.581  15.602  37.374  1.00  4.47           C  
-ATOM   7854  CG1 ILE D  65      80.070  14.388  36.608  1.00  6.56           C  
-ATOM   7855  CG2 ILE D  65      80.765  16.320  37.940  1.00  8.07           C  
-ATOM   7856  CD1 ILE D  65      80.179  14.614  35.119  1.00 16.00           C  
-ATOM   7857  N   TYR D  66      80.054  15.201  40.491  1.00  4.47           N  
-ATOM   7858  CA  TYR D  66      80.846  14.552  41.523  1.00  7.64           C  
-ATOM   7859  C   TYR D  66      79.965  13.990  42.623  1.00 12.42           C  
-ATOM   7860  O   TYR D  66      80.048  12.806  42.942  1.00 15.95           O  
-ATOM   7861  CB  TYR D  66      81.884  15.515  42.095  1.00 17.54           C  
-ATOM   7862  CG  TYR D  66      82.988  15.822  41.119  1.00 21.84           C  
-ATOM   7863  CD1 TYR D  66      83.110  17.086  40.550  1.00 24.69           C  
-ATOM   7864  CD2 TYR D  66      83.864  14.821  40.700  1.00 31.30           C  
-ATOM   7865  CE1 TYR D  66      84.074  17.347  39.574  1.00 34.69           C  
-ATOM   7866  CE2 TYR D  66      84.834  15.066  39.719  1.00 38.90           C  
-ATOM   7867  CZ  TYR D  66      84.933  16.328  39.154  1.00 39.44           C  
-ATOM   7868  OH  TYR D  66      85.856  16.550  38.147  1.00 33.89           O  
-ATOM   7869  N   GLY D  67      79.111  14.830  43.197  1.00 20.59           N  
-ATOM   7870  CA  GLY D  67      78.228  14.374  44.261  1.00 26.05           C  
-ATOM   7871  C   GLY D  67      77.541  13.055  43.934  1.00 23.30           C  
-ATOM   7872  O   GLY D  67      77.378  12.180  44.795  1.00 17.79           O  
-ATOM   7873  N   THR D  68      77.134  12.910  42.679  1.00 15.65           N  
-ATOM   7874  CA  THR D  68      76.464  11.697  42.253  1.00  8.22           C  
-ATOM   7875  C   THR D  68      77.334  10.478  42.478  1.00  4.47           C  
-ATOM   7876  O   THR D  68      76.836   9.413  42.767  1.00  4.47           O  
-ATOM   7877  CB  THR D  68      76.064  11.782  40.774  1.00  4.47           C  
-ATOM   7878  OG1 THR D  68      74.888  12.584  40.654  1.00 14.07           O  
-ATOM   7879  CG2 THR D  68      75.765  10.429  40.220  1.00  4.47           C  
-ATOM   7880  N   GLN D  69      78.640  10.626  42.359  1.00  4.47           N  
-ATOM   7881  CA  GLN D  69      79.498   9.481  42.556  1.00  4.47           C  
-ATOM   7882  C   GLN D  69      79.593   9.198  44.037  1.00 15.99           C  
-ATOM   7883  O   GLN D  69      79.521   8.046  44.459  1.00 25.35           O  
-ATOM   7884  CB  GLN D  69      80.876   9.726  41.949  1.00 12.69           C  
-ATOM   7885  CG  GLN D  69      80.859  10.049  40.437  1.00 23.28           C  
-ATOM   7886  CD  GLN D  69      79.894   9.182  39.632  1.00 28.35           C  
-ATOM   7887  OE1 GLN D  69      79.871   7.953  39.767  1.00 41.75           O  
-ATOM   7888  NE2 GLN D  69      79.101   9.822  38.782  1.00 11.90           N  
-ATOM   7889  N   THR D  70      79.743  10.246  44.838  1.00 23.67           N  
-ATOM   7890  CA  THR D  70      79.796  10.067  46.291  1.00 25.01           C  
-ATOM   7891  C   THR D  70      78.482   9.402  46.723  1.00 18.29           C  
-ATOM   7892  O   THR D  70      78.470   8.500  47.551  1.00 13.79           O  
-ATOM   7893  CB  THR D  70      79.897  11.412  47.032  1.00 28.80           C  
-ATOM   7894  OG1 THR D  70      81.030  12.148  46.549  1.00 43.47           O  
-ATOM   7895  CG2 THR D  70      80.033  11.171  48.531  1.00 26.23           C  
-ATOM   7896  N   ARG D  71      77.376   9.868  46.150  1.00 15.80           N  
-ATOM   7897  CA  ARG D  71      76.065   9.324  46.449  1.00  6.00           C  
-ATOM   7898  C   ARG D  71      75.949   7.880  45.981  1.00  4.47           C  
-ATOM   7899  O   ARG D  71      75.127   7.119  46.485  1.00  5.87           O  
-ATOM   7900  CB  ARG D  71      74.990  10.177  45.782  1.00  4.47           C  
-ATOM   7901  CG  ARG D  71      74.107  10.878  46.771  1.00  4.76           C  
-ATOM   7902  CD  ARG D  71      73.444  12.065  46.155  1.00  5.13           C  
-ATOM   7903  NE  ARG D  71      72.448  11.694  45.158  1.00 17.73           N  
-ATOM   7904  CZ  ARG D  71      71.235  11.231  45.442  1.00 15.01           C  
-ATOM   7905  NH1 ARG D  71      70.852  11.073  46.701  1.00 24.54           N  
-ATOM   7906  NH2 ARG D  71      70.394  10.949  44.460  1.00 20.50           N  
-ATOM   7907  N   ARG D  72      76.769   7.502  45.009  1.00  4.47           N  
-ATOM   7908  CA  ARG D  72      76.737   6.138  44.516  1.00  7.34           C  
-ATOM   7909  C   ARG D  72      77.479   5.223  45.480  1.00 13.22           C  
-ATOM   7910  O   ARG D  72      76.985   4.143  45.801  1.00 18.14           O  
-ATOM   7911  CB  ARG D  72      77.373   6.044  43.135  1.00  7.89           C  
-ATOM   7912  CG  ARG D  72      77.665   4.625  42.695  1.00  9.33           C  
-ATOM   7913  CD  ARG D  72      78.001   4.570  41.220  1.00 23.17           C  
-ATOM   7914  NE  ARG D  72      78.355   3.223  40.770  1.00 40.80           N  
-ATOM   7915  CZ  ARG D  72      78.590   2.895  39.499  1.00 49.02           C  
-ATOM   7916  NH1 ARG D  72      78.505   3.814  38.540  1.00 53.26           N  
-ATOM   7917  NH2 ARG D  72      78.928   1.651  39.182  1.00 45.69           N  
-ATOM   7918  N   LEU D  73      78.653   5.647  45.945  1.00  4.47           N  
-ATOM   7919  CA  LEU D  73      79.435   4.829  46.875  1.00 13.49           C  
-ATOM   7920  C   LEU D  73      78.738   4.558  48.199  1.00 17.20           C  
-ATOM   7921  O   LEU D  73      78.889   3.481  48.781  1.00 17.05           O  
-ATOM   7922  CB  LEU D  73      80.780   5.483  47.168  1.00 14.41           C  
-ATOM   7923  CG  LEU D  73      81.847   5.306  46.096  1.00 33.74           C  
-ATOM   7924  CD1 LEU D  73      81.219   5.218  44.690  1.00 32.57           C  
-ATOM   7925  CD2 LEU D  73      82.816   6.485  46.203  1.00 46.20           C  
-ATOM   7926  N   ASN D  74      77.988   5.543  48.679  1.00 18.94           N  
-ATOM   7927  CA  ASN D  74      77.279   5.422  49.944  1.00 20.53           C  
-ATOM   7928  C   ASN D  74      76.008   4.614  49.760  1.00 16.66           C  
-ATOM   7929  O   ASN D  74      75.313   4.277  50.723  1.00 15.99           O  
-ATOM   7930  CB  ASN D  74      76.949   6.812  50.480  1.00 33.52           C  
-ATOM   7931  CG  ASN D  74      78.194   7.642  50.758  1.00 40.14           C  
-ATOM   7932  OD1 ASN D  74      78.121   8.864  50.878  1.00 54.69           O  
-ATOM   7933  ND2 ASN D  74      79.338   6.980  50.871  1.00 33.42           N  
-ATOM   7934  N   GLY D  75      75.710   4.295  48.512  1.00 12.39           N  
-ATOM   7935  CA  GLY D  75      74.527   3.513  48.253  1.00 19.35           C  
-ATOM   7936  C   GLY D  75      73.272   4.317  48.500  1.00 25.75           C  
-ATOM   7937  O   GLY D  75      72.212   3.752  48.779  1.00 30.70           O  
-ATOM   7938  N   ASP D  76      73.385   5.640  48.418  1.00 26.54           N  
-ATOM   7939  CA  ASP D  76      72.214   6.493  48.605  1.00 23.87           C  
-ATOM   7940  C   ASP D  76      71.366   6.371  47.339  1.00 17.86           C  
-ATOM   7941  O   ASP D  76      70.199   6.764  47.322  1.00 15.45           O  
-ATOM   7942  CB  ASP D  76      72.622   7.959  48.814  1.00 38.00           C  
-ATOM   7943  CG  ASP D  76      73.151   8.246  50.230  1.00 54.67           C  
-ATOM   7944  OD1 ASP D  76      73.551   9.406  50.489  1.00 62.80           O  
-ATOM   7945  OD2 ASP D  76      73.166   7.332  51.086  1.00 59.57           O  
-ATOM   7946  N   VAL D  77      71.966   5.821  46.282  1.00 10.84           N  
-ATOM   7947  CA  VAL D  77      71.272   5.646  45.014  1.00 11.86           C  
-ATOM   7948  C   VAL D  77      71.775   4.456  44.204  1.00 17.32           C  
-ATOM   7949  O   VAL D  77      72.972   4.131  44.211  1.00 15.36           O  
-ATOM   7950  CB  VAL D  77      71.394   6.887  44.122  1.00 12.55           C  
-ATOM   7951  CG1 VAL D  77      72.757   6.925  43.457  1.00  4.82           C  
-ATOM   7952  CG2 VAL D  77      70.306   6.862  43.083  1.00 19.45           C  
-ATOM   7953  N   SER D  78      70.841   3.830  43.490  1.00 15.07           N  
-ATOM   7954  CA  SER D  78      71.123   2.665  42.664  1.00  9.91           C  
-ATOM   7955  C   SER D  78      72.229   2.969  41.683  1.00  7.41           C  
-ATOM   7956  O   SER D  78      72.269   4.059  41.131  1.00 17.86           O  
-ATOM   7957  CB  SER D  78      69.868   2.274  41.895  1.00 17.66           C  
-ATOM   7958  OG  SER D  78      70.166   1.294  40.918  1.00 39.28           O  
-ATOM   7959  N   PRO D  79      73.144   2.015  41.453  1.00  6.07           N  
-ATOM   7960  CA  PRO D  79      74.242   2.243  40.507  1.00 13.32           C  
-ATOM   7961  C   PRO D  79      73.680   2.430  39.100  1.00 22.35           C  
-ATOM   7962  O   PRO D  79      74.292   3.090  38.255  1.00 28.45           O  
-ATOM   7963  CB  PRO D  79      75.082   0.977  40.639  1.00  5.37           C  
-ATOM   7964  CG  PRO D  79      74.053  -0.049  40.884  1.00 15.89           C  
-ATOM   7965  CD  PRO D  79      73.166   0.625  41.926  1.00 16.37           C  
-ATOM   7966  N   GLU D  80      72.507   1.851  38.847  1.00 25.54           N  
-ATOM   7967  CA  GLU D  80      71.871   2.003  37.544  1.00 21.46           C  
-ATOM   7968  C   GLU D  80      71.444   3.468  37.391  1.00 17.18           C  
-ATOM   7969  O   GLU D  80      71.685   4.080  36.351  1.00 17.75           O  
-ATOM   7970  CB  GLU D  80      70.661   1.073  37.417  1.00 22.27           C  
-ATOM   7971  CG  GLU D  80      70.049   1.059  36.027  1.00 36.76           C  
-ATOM   7972  CD  GLU D  80      69.008  -0.039  35.839  1.00 55.82           C  
-ATOM   7973  OE1 GLU D  80      69.346  -1.239  36.004  1.00 61.15           O  
-ATOM   7974  OE2 GLU D  80      67.849   0.304  35.519  1.00 59.27           O  
-ATOM   7975  N   ASP D  81      70.833   4.040  38.429  1.00  7.24           N  
-ATOM   7976  CA  ASP D  81      70.416   5.435  38.350  1.00  8.37           C  
-ATOM   7977  C   ASP D  81      71.628   6.361  38.351  1.00 10.85           C  
-ATOM   7978  O   ASP D  81      71.700   7.320  37.582  1.00 11.84           O  
-ATOM   7979  CB  ASP D  81      69.488   5.802  39.508  1.00  4.47           C  
-ATOM   7980  CG  ASP D  81      68.213   5.000  39.504  1.00 10.87           C  
-ATOM   7981  OD1 ASP D  81      67.591   4.828  38.434  1.00 14.73           O  
-ATOM   7982  OD2 ASP D  81      67.821   4.540  40.588  1.00 32.38           O  
-ATOM   7983  N   ALA D  82      72.587   6.064  39.215  1.00 16.75           N  
-ATOM   7984  CA  ALA D  82      73.787   6.881  39.312  1.00 17.89           C  
-ATOM   7985  C   ALA D  82      74.402   7.086  37.945  1.00 15.79           C  
-ATOM   7986  O   ALA D  82      75.028   8.109  37.690  1.00 21.23           O  
-ATOM   7987  CB  ALA D  82      74.801   6.230  40.244  1.00 22.49           C  
-ATOM   7988  N   GLN D  83      74.220   6.121  37.055  1.00 11.42           N  
-ATOM   7989  CA  GLN D  83      74.796   6.262  35.731  1.00 15.45           C  
-ATOM   7990  C   GLN D  83      73.978   7.235  34.929  1.00 12.63           C  
-ATOM   7991  O   GLN D  83      74.513   8.114  34.257  1.00 14.12           O  
-ATOM   7992  CB  GLN D  83      74.833   4.921  35.010  1.00 16.66           C  
-ATOM   7993  CG  GLN D  83      75.613   3.873  35.754  1.00 23.12           C  
-ATOM   7994  CD  GLN D  83      76.029   2.726  34.872  1.00 26.34           C  
-ATOM   7995  OE1 GLN D  83      75.193   2.076  34.235  1.00 26.77           O  
-ATOM   7996  NE2 GLN D  83      77.335   2.466  34.825  1.00 25.85           N  
-ATOM   7997  N   ARG D  84      72.667   7.063  35.004  1.00 10.33           N  
-ATOM   7998  CA  ARG D  84      71.758   7.920  34.279  1.00  8.50           C  
-ATOM   7999  C   ARG D  84      71.883   9.304  34.852  1.00 10.27           C  
-ATOM   8000  O   ARG D  84      71.976  10.300  34.120  1.00 14.08           O  
-ATOM   8001  CB  ARG D  84      70.340   7.389  34.421  1.00  4.47           C  
-ATOM   8002  CG  ARG D  84      70.161   6.115  33.633  1.00  5.99           C  
-ATOM   8003  CD  ARG D  84      68.975   5.316  34.083  1.00  4.47           C  
-ATOM   8004  NE  ARG D  84      68.988   4.022  33.410  1.00 17.70           N  
-ATOM   8005  CZ  ARG D  84      68.125   3.045  33.652  1.00 24.09           C  
-ATOM   8006  NH1 ARG D  84      67.171   3.212  34.560  1.00 35.70           N  
-ATOM   8007  NH2 ARG D  84      68.217   1.902  32.985  1.00 22.12           N  
-ATOM   8008  N   LEU D  85      71.909   9.359  36.174  1.00  4.47           N  
-ATOM   8009  CA  LEU D  85      72.040  10.625  36.854  1.00  4.47           C  
-ATOM   8010  C   LEU D  85      73.302  11.332  36.378  1.00  9.72           C  
-ATOM   8011  O   LEU D  85      73.298  12.547  36.181  1.00 17.61           O  
-ATOM   8012  CB  LEU D  85      72.077  10.395  38.356  1.00  4.47           C  
-ATOM   8013  CG  LEU D  85      71.029  11.223  39.109  1.00 13.10           C  
-ATOM   8014  CD1 LEU D  85      69.695  11.222  38.389  1.00  8.30           C  
-ATOM   8015  CD2 LEU D  85      70.858  10.650  40.497  1.00 20.71           C  
-ATOM   8016  N   THR D  86      74.377  10.577  36.173  1.00  7.58           N  
-ATOM   8017  CA  THR D  86      75.616  11.174  35.698  1.00  4.47           C  
-ATOM   8018  C   THR D  86      75.402  11.780  34.316  1.00  4.47           C  
-ATOM   8019  O   THR D  86      75.647  12.969  34.114  1.00 14.32           O  
-ATOM   8020  CB  THR D  86      76.753  10.145  35.622  1.00  7.87           C  
-ATOM   8021  OG1 THR D  86      76.982   9.593  36.920  1.00  7.83           O  
-ATOM   8022  CG2 THR D  86      78.040  10.801  35.143  1.00  4.47           C  
-ATOM   8023  N   ALA D  87      74.942  10.969  33.367  1.00  4.47           N  
-ATOM   8024  CA  ALA D  87      74.705  11.456  32.009  1.00  5.61           C  
-ATOM   8025  C   ALA D  87      74.048  12.826  32.053  1.00 12.17           C  
-ATOM   8026  O   ALA D  87      74.484  13.757  31.371  1.00 11.04           O  
-ATOM   8027  CB  ALA D  87      73.823  10.494  31.252  1.00 13.56           C  
-ATOM   8028  N   HIS D  88      73.004  12.946  32.869  1.00  8.17           N  
-ATOM   8029  CA  HIS D  88      72.299  14.205  32.998  1.00  4.47           C  
-ATOM   8030  C   HIS D  88      73.260  15.358  33.243  1.00  4.47           C  
-ATOM   8031  O   HIS D  88      73.342  16.277  32.437  1.00  5.82           O  
-ATOM   8032  CB  HIS D  88      71.306  14.140  34.143  1.00  5.88           C  
-ATOM   8033  CG  HIS D  88      70.675  15.458  34.458  1.00  8.91           C  
-ATOM   8034  ND1 HIS D  88      69.815  16.088  33.588  1.00  6.84           N  
-ATOM   8035  CD2 HIS D  88      70.788  16.270  35.539  1.00  4.90           C  
-ATOM   8036  CE1 HIS D  88      69.419  17.231  34.121  1.00 15.27           C  
-ATOM   8037  NE2 HIS D  88      69.994  17.365  35.304  1.00  8.16           N  
-ATOM   8038  N   PHE D  89      73.978  15.310  34.361  1.00  5.57           N  
-ATOM   8039  CA  PHE D  89      74.919  16.369  34.699  1.00  7.49           C  
-ATOM   8040  C   PHE D  89      75.978  16.562  33.637  1.00  4.47           C  
-ATOM   8041  O   PHE D  89      76.159  17.669  33.137  1.00 12.19           O  
-ATOM   8042  CB  PHE D  89      75.568  16.086  36.045  1.00  4.47           C  
-ATOM   8043  CG  PHE D  89      74.605  16.130  37.171  1.00  4.47           C  
-ATOM   8044  CD1 PHE D  89      74.245  14.984  37.831  1.00  4.47           C  
-ATOM   8045  CD2 PHE D  89      74.032  17.330  37.562  1.00 11.64           C  
-ATOM   8046  CE1 PHE D  89      73.318  15.029  38.876  1.00  9.75           C  
-ATOM   8047  CE2 PHE D  89      73.111  17.383  38.602  1.00  4.47           C  
-ATOM   8048  CZ  PHE D  89      72.755  16.233  39.257  1.00  4.47           C  
-ATOM   8049  N   GLN D  90      76.677  15.497  33.285  1.00  4.47           N  
-ATOM   8050  CA  GLN D  90      77.698  15.608  32.262  1.00  6.39           C  
-ATOM   8051  C   GLN D  90      77.204  16.445  31.094  1.00 16.85           C  
-ATOM   8052  O   GLN D  90      77.915  17.328  30.614  1.00 22.35           O  
-ATOM   8053  CB  GLN D  90      78.095  14.227  31.752  1.00 12.90           C  
-ATOM   8054  CG  GLN D  90      78.997  14.225  30.518  1.00  6.65           C  
-ATOM   8055  CD  GLN D  90      80.116  15.246  30.602  1.00  9.12           C  
-ATOM   8056  OE1 GLN D  90      80.665  15.506  31.668  1.00 11.38           O  
-ATOM   8057  NE2 GLN D  90      80.464  15.821  29.470  1.00  7.87           N  
-ATOM   8058  N   SER D  91      75.983  16.167  30.646  1.00 15.79           N  
-ATOM   8059  CA  SER D  91      75.391  16.890  29.524  1.00  8.20           C  
-ATOM   8060  C   SER D  91      75.295  18.388  29.759  1.00  9.20           C  
-ATOM   8061  O   SER D  91      75.369  19.154  28.802  1.00 21.26           O  
-ATOM   8062  CB  SER D  91      73.987  16.381  29.232  1.00 12.98           C  
-ATOM   8063  OG  SER D  91      73.041  17.069  30.036  1.00 21.74           O  
-ATOM   8064  N   LEU D  92      75.110  18.810  31.012  1.00  5.40           N  
-ATOM   8065  CA  LEU D  92      74.991  20.240  31.323  1.00  9.20           C  
-ATOM   8066  C   LEU D  92      76.120  21.109  30.785  1.00  9.37           C  
-ATOM   8067  O   LEU D  92      75.885  22.238  30.358  1.00  8.46           O  
-ATOM   8068  CB  LEU D  92      74.874  20.458  32.824  1.00  4.71           C  
-ATOM   8069  CG  LEU D  92      73.543  20.018  33.429  1.00  7.52           C  
-ATOM   8070  CD1 LEU D  92      73.561  20.302  34.925  1.00 13.18           C  
-ATOM   8071  CD2 LEU D  92      72.396  20.755  32.757  1.00  5.95           C  
-ATOM   8072  N   PHE D  93      77.337  20.573  30.806  1.00  9.87           N  
-ATOM   8073  CA  PHE D  93      78.525  21.273  30.314  1.00 10.66           C  
-ATOM   8074  C   PHE D  93      78.473  21.677  28.838  1.00 16.54           C  
-ATOM   8075  O   PHE D  93      79.180  22.602  28.424  1.00 25.11           O  
-ATOM   8076  CB  PHE D  93      79.756  20.399  30.524  1.00 10.14           C  
-ATOM   8077  CG  PHE D  93      80.136  20.218  31.965  1.00 17.12           C  
-ATOM   8078  CD1 PHE D  93      80.850  21.204  32.642  1.00 27.15           C  
-ATOM   8079  CD2 PHE D  93      79.792  19.069  32.645  1.00  8.94           C  
-ATOM   8080  CE1 PHE D  93      81.222  21.041  33.981  1.00 15.72           C  
-ATOM   8081  CE2 PHE D  93      80.159  18.904  33.981  1.00 17.86           C  
-ATOM   8082  CZ  PHE D  93      80.875  19.891  34.646  1.00  7.40           C  
-ATOM   8083  N   CYS D  94      77.641  20.996  28.054  1.00 10.24           N  
-ATOM   8084  CA  CYS D  94      77.520  21.258  26.622  1.00  7.36           C  
-ATOM   8085  C   CYS D  94      77.038  22.625  26.136  1.00 14.05           C  
-ATOM   8086  O   CYS D  94      77.784  23.353  25.473  1.00 10.21           O  
-ATOM   8087  CB  CYS D  94      76.651  20.176  25.996  1.00 12.72           C  
-ATOM   8088  SG  CYS D  94      77.431  18.533  26.119  1.00 39.89           S  
-ATOM   8089  N   SER D  95      75.797  22.978  26.455  1.00 16.78           N  
-ATOM   8090  CA  SER D  95      75.218  24.247  26.000  1.00 14.12           C  
-ATOM   8091  C   SER D  95      76.110  25.479  25.970  1.00  8.29           C  
-ATOM   8092  O   SER D  95      76.373  26.015  24.910  1.00 11.21           O  
-ATOM   8093  CB  SER D  95      73.943  24.565  26.782  1.00 13.56           C  
-ATOM   8094  OG  SER D  95      74.066  24.145  28.125  1.00 36.19           O  
-ATOM   8095  N   PRO D  96      76.603  25.934  27.123  1.00  6.51           N  
-ATOM   8096  CA  PRO D  96      77.459  27.125  27.126  1.00 15.49           C  
-ATOM   8097  C   PRO D  96      78.487  27.131  25.994  1.00 20.63           C  
-ATOM   8098  O   PRO D  96      78.430  27.953  25.086  1.00 23.59           O  
-ATOM   8099  CB  PRO D  96      78.140  27.061  28.485  1.00 11.35           C  
-ATOM   8100  CG  PRO D  96      77.183  26.278  29.309  1.00 19.19           C  
-ATOM   8101  CD  PRO D  96      76.753  25.196  28.382  1.00 12.03           C  
-ATOM   8102  N   HIS D  97      79.433  26.205  26.059  1.00 21.06           N  
-ATOM   8103  CA  HIS D  97      80.475  26.113  25.052  1.00 15.96           C  
-ATOM   8104  C   HIS D  97      79.942  26.047  23.629  1.00 13.40           C  
-ATOM   8105  O   HIS D  97      80.589  26.504  22.678  1.00 12.16           O  
-ATOM   8106  CB  HIS D  97      81.326  24.883  25.322  1.00 21.81           C  
-ATOM   8107  CG  HIS D  97      82.692  25.208  25.809  1.00 18.77           C  
-ATOM   8108  ND1 HIS D  97      83.552  26.021  25.107  1.00 22.23           N  
-ATOM   8109  CD2 HIS D  97      83.345  24.846  26.933  1.00 18.93           C  
-ATOM   8110  CE1 HIS D  97      84.680  26.146  25.781  1.00 32.73           C  
-ATOM   8111  NE2 HIS D  97      84.580  25.442  26.892  1.00 32.73           N  
-ATOM   8112  N   ALA D  98      78.758  25.466  23.488  1.00 15.12           N  
-ATOM   8113  CA  ALA D  98      78.139  25.304  22.178  1.00 20.88           C  
-ATOM   8114  C   ALA D  98      77.516  26.589  21.626  1.00 13.56           C  
-ATOM   8115  O   ALA D  98      77.729  26.928  20.463  1.00 12.54           O  
-ATOM   8116  CB  ALA D  98      77.090  24.181  22.244  1.00 15.64           C  
-ATOM   8117  N   ILE D  99      76.739  27.283  22.457  1.00 10.28           N  
-ATOM   8118  CA  ILE D  99      76.099  28.534  22.060  1.00  4.47           C  
-ATOM   8119  C   ILE D  99      77.187  29.426  21.489  1.00  9.34           C  
-ATOM   8120  O   ILE D  99      77.024  30.026  20.436  1.00 14.00           O  
-ATOM   8121  CB  ILE D  99      75.492  29.291  23.270  1.00  4.47           C  
-ATOM   8122  CG1 ILE D  99      74.424  28.448  23.967  1.00  4.47           C  
-ATOM   8123  CG2 ILE D  99      74.918  30.614  22.806  1.00  8.74           C  
-ATOM   8124  CD1 ILE D  99      73.224  28.134  23.114  1.00  7.09           C  
-ATOM   8125  N   MET D 100      78.294  29.500  22.218  1.00  9.73           N  
-ATOM   8126  CA  MET D 100      79.454  30.292  21.852  1.00 13.49           C  
-ATOM   8127  C   MET D 100      80.018  29.811  20.517  1.00 18.83           C  
-ATOM   8128  O   MET D 100      79.879  30.481  19.494  1.00 23.91           O  
-ATOM   8129  CB  MET D 100      80.520  30.152  22.941  1.00 30.20           C  
-ATOM   8130  CG  MET D 100      81.784  30.975  22.739  1.00 44.86           C  
-ATOM   8131  SD  MET D 100      81.636  32.629  23.418  1.00 45.79           S  
-ATOM   8132  CE  MET D 100      81.601  33.592  21.966  1.00 43.63           C  
-ATOM   8133  N   HIS D 101      80.658  28.649  20.525  1.00 17.79           N  
-ATOM   8134  CA  HIS D 101      81.234  28.107  19.302  1.00 25.50           C  
-ATOM   8135  C   HIS D 101      80.336  28.299  18.071  1.00 23.62           C  
-ATOM   8136  O   HIS D 101      80.809  28.671  16.994  1.00 25.19           O  
-ATOM   8137  CB  HIS D 101      81.517  26.614  19.473  1.00 34.87           C  
-ATOM   8138  CG  HIS D 101      81.967  25.939  18.212  1.00 35.59           C  
-ATOM   8139  ND1 HIS D 101      83.295  25.819  17.862  1.00 38.54           N  
-ATOM   8140  CD2 HIS D 101      81.260  25.369  17.208  1.00 30.75           C  
-ATOM   8141  CE1 HIS D 101      83.387  25.202  16.698  1.00 39.16           C  
-ATOM   8142  NE2 HIS D 101      82.166  24.919  16.280  1.00 36.75           N  
-ATOM   8143  N   ALA D 102      79.043  28.038  18.230  1.00 23.07           N  
-ATOM   8144  CA  ALA D 102      78.105  28.164  17.119  1.00 18.52           C  
-ATOM   8145  C   ALA D 102      77.971  29.593  16.619  1.00  7.91           C  
-ATOM   8146  O   ALA D 102      77.760  29.816  15.431  1.00  6.51           O  
-ATOM   8147  CB  ALA D 102      76.750  27.620  17.523  1.00 29.76           C  
-ATOM   8148  N   LYS D 103      78.077  30.556  17.530  1.00 11.68           N  
-ATOM   8149  CA  LYS D 103      77.987  31.974  17.175  1.00 14.50           C  
-ATOM   8150  C   LYS D 103      79.236  32.328  16.388  1.00 12.80           C  
-ATOM   8151  O   LYS D 103      79.166  32.891  15.299  1.00 10.31           O  
-ATOM   8152  CB  LYS D 103      77.922  32.840  18.435  1.00  6.66           C  
-ATOM   8153  CG  LYS D 103      78.347  34.270  18.221  1.00 12.26           C  
-ATOM   8154  CD  LYS D 103      77.310  35.048  17.443  1.00 34.46           C  
-ATOM   8155  CE  LYS D 103      76.104  35.392  18.308  1.00 38.36           C  
-ATOM   8156  NZ  LYS D 103      75.083  36.179  17.559  1.00 43.48           N  
-ATOM   8157  N   ILE D 104      80.382  31.985  16.962  1.00 15.61           N  
-ATOM   8158  CA  ILE D 104      81.669  32.240  16.340  1.00 17.83           C  
-ATOM   8159  C   ILE D 104      81.767  31.657  14.935  1.00 23.92           C  
-ATOM   8160  O   ILE D 104      82.337  32.280  14.045  1.00 25.14           O  
-ATOM   8161  CB  ILE D 104      82.798  31.677  17.207  1.00 19.12           C  
-ATOM   8162  CG1 ILE D 104      83.064  32.643  18.360  1.00 18.50           C  
-ATOM   8163  CG2 ILE D 104      84.041  31.418  16.364  1.00 16.78           C  
-ATOM   8164  CD1 ILE D 104      83.904  32.061  19.470  1.00 31.27           C  
-ATOM   8165  N   SER D 105      81.223  30.466  14.721  1.00 25.91           N  
-ATOM   8166  CA  SER D 105      81.285  29.889  13.389  1.00 30.86           C  
-ATOM   8167  C   SER D 105      80.525  30.777  12.402  1.00 27.69           C  
-ATOM   8168  O   SER D 105      80.834  30.807  11.213  1.00 35.57           O  
-ATOM   8169  CB  SER D 105      80.694  28.482  13.391  1.00 42.01           C  
-ATOM   8170  OG  SER D 105      81.433  27.624  14.248  1.00 55.44           O  
-ATOM   8171  N   ALA D 106      79.544  31.515  12.905  1.00 22.33           N  
-ATOM   8172  CA  ALA D 106      78.748  32.392  12.063  1.00 22.96           C  
-ATOM   8173  C   ALA D 106      79.510  33.647  11.663  1.00 26.76           C  
-ATOM   8174  O   ALA D 106      79.271  34.207  10.600  1.00 28.69           O  
-ATOM   8175  CB  ALA D 106      77.463  32.770  12.776  1.00 27.56           C  
-ATOM   8176  N   LEU D 107      80.422  34.097  12.517  1.00 32.78           N  
-ATOM   8177  CA  LEU D 107      81.208  35.291  12.215  1.00 30.18           C  
-ATOM   8178  C   LEU D 107      82.469  34.913  11.461  1.00 37.62           C  
-ATOM   8179  O   LEU D 107      83.362  35.740  11.308  1.00 40.30           O  
-ATOM   8180  CB  LEU D 107      81.622  36.021  13.492  1.00 27.40           C  
-ATOM   8181  CG  LEU D 107      80.540  36.284  14.537  1.00 37.55           C  
-ATOM   8182  CD1 LEU D 107      81.128  37.117  15.679  1.00 36.08           C  
-ATOM   8183  CD2 LEU D 107      79.363  36.989  13.884  1.00 40.06           C  
-ATOM   8184  N   MET D 108      82.555  33.665  11.005  1.00 42.20           N  
-ATOM   8185  CA  MET D 108      83.733  33.225  10.272  1.00 48.93           C  
-ATOM   8186  C   MET D 108      83.489  33.293   8.767  1.00 62.56           C  
-ATOM   8187  O   MET D 108      82.541  32.690   8.251  1.00 67.94           O  
-ATOM   8188  CB  MET D 108      84.117  31.799  10.670  1.00 49.88           C  
-ATOM   8189  CG  MET D 108      85.622  31.589  10.801  1.00 53.68           C  
-ATOM   8190  SD  MET D 108      86.291  32.036  12.441  1.00 56.44           S  
-ATOM   8191  CE  MET D 108      86.126  33.794  12.459  1.00 38.43           C  
-ATOM   8192  N   ASP D 109      84.351  34.035   8.073  1.00 69.67           N  
-ATOM   8193  CA  ASP D 109      84.254  34.210   6.627  1.00 76.44           C  
-ATOM   8194  C   ASP D 109      84.690  32.953   5.875  1.00 82.36           C  
-ATOM   8195  O   ASP D 109      85.870  32.573   5.903  1.00 81.86           O  
-ATOM   8196  CB  ASP D 109      85.111  35.406   6.186  1.00 78.40           C  
-ATOM   8197  CG  ASP D 109      84.985  35.707   4.693  1.00 87.12           C  
-ATOM   8198  OD1 ASP D 109      83.856  35.973   4.222  1.00 90.13           O  
-ATOM   8199  OD2 ASP D 109      86.019  35.683   3.989  1.00 91.29           O  
-ATOM   8200  N   THR D 110      83.727  32.312   5.211  1.00 87.04           N  
-ATOM   8201  CA  THR D 110      83.984  31.101   4.430  1.00 94.22           C  
-ATOM   8202  C   THR D 110      83.953  31.475   2.938  1.00 95.03           C  
-ATOM   8203  O   THR D 110      83.196  30.903   2.141  1.00 92.96           O  
-ATOM   8204  CB  THR D 110      82.919  30.006   4.734  1.00 95.79           C  
-ATOM   8205  OG1 THR D 110      82.798  29.835   6.153  1.00 93.61           O  
-ATOM   8206  CG2 THR D 110      83.327  28.667   4.114  1.00 96.93           C  
-ATOM   8207  N   SER D 111      84.789  32.454   2.587  1.00 95.92           N  
-ATOM   8208  CA  SER D 111      84.902  32.972   1.226  1.00 95.08           C  
-ATOM   8209  C   SER D 111      86.028  32.284   0.453  1.00 94.62           C  
-ATOM   8210  O   SER D 111      87.117  32.044   0.992  1.00 94.31           O  
-ATOM   8211  CB  SER D 111      85.146  34.491   1.272  1.00 94.44           C  
-ATOM   8212  OG  SER D 111      85.205  35.060  -0.025  1.00 95.53           O  
-ATOM   8213  N   THR D 112      85.747  31.977  -0.814  1.00 92.91           N  
-ATOM   8214  CA  THR D 112      86.691  31.312  -1.709  1.00 84.60           C  
-ATOM   8215  C   THR D 112      87.386  32.293  -2.657  1.00 80.82           C  
-ATOM   8216  O   THR D 112      88.612  32.429  -2.639  1.00 73.73           O  
-ATOM   8217  CB  THR D 112      85.970  30.228  -2.545  1.00 78.03           C  
-ATOM   8218  OG1 THR D 112      84.686  30.717  -2.965  1.00 71.24           O  
-ATOM   8219  CG2 THR D 112      85.795  28.957  -1.728  1.00 69.04           C  
-ATOM   8220  N   GLU D 121     102.773  42.323   8.773  1.00 86.30           N  
-ATOM   8221  CA  GLU D 121     101.397  42.282   9.273  1.00 91.46           C  
-ATOM   8222  C   GLU D 121     100.998  40.919   9.863  1.00 91.05           C  
-ATOM   8223  O   GLU D 121     100.635  39.992   9.126  1.00 92.23           O  
-ATOM   8224  CB  GLU D 121     100.417  42.656   8.150  1.00 93.79           C  
-ATOM   8225  CG  GLU D 121     100.331  44.152   7.837  1.00 93.44           C  
-ATOM   8226  CD  GLU D 121      99.662  44.946   8.948  1.00 89.91           C  
-ATOM   8227  OE1 GLU D 121      98.519  44.601   9.318  1.00 89.21           O  
-ATOM   8228  OE2 GLU D 121     100.275  45.914   9.448  1.00 85.71           O  
-ATOM   8229  N   PRO D 122     101.058  40.781  11.203  1.00 86.74           N  
-ATOM   8230  CA  PRO D 122     100.689  39.508  11.833  1.00 81.46           C  
-ATOM   8231  C   PRO D 122      99.176  39.235  11.844  1.00 79.38           C  
-ATOM   8232  O   PRO D 122      98.368  40.073  11.421  1.00 77.70           O  
-ATOM   8233  CB  PRO D 122     101.285  39.632  13.237  1.00 76.62           C  
-ATOM   8234  CG  PRO D 122     101.181  41.096  13.512  1.00 82.34           C  
-ATOM   8235  CD  PRO D 122     101.612  41.719  12.198  1.00 84.65           C  
-ATOM   8236  N   TYR D 123      98.816  38.044  12.323  1.00 74.75           N  
-ATOM   8237  CA  TYR D 123      97.426  37.582  12.417  1.00 64.89           C  
-ATOM   8238  C   TYR D 123      96.922  37.603  13.867  1.00 58.77           C  
-ATOM   8239  O   TYR D 123      97.654  37.254  14.805  1.00 50.12           O  
-ATOM   8240  CB  TYR D 123      97.315  36.153  11.846  1.00 57.91           C  
-ATOM   8241  CG  TYR D 123      98.558  35.323  12.090  1.00 61.89           C  
-ATOM   8242  CD1 TYR D 123      99.172  35.311  13.354  1.00 69.50           C  
-ATOM   8243  CD2 TYR D 123      99.154  34.589  11.059  1.00 60.82           C  
-ATOM   8244  CE1 TYR D 123     100.352  34.597  13.592  1.00 72.68           C  
-ATOM   8245  CE2 TYR D 123     100.343  33.862  11.285  1.00 70.84           C  
-ATOM   8246  CZ  TYR D 123     100.935  33.876  12.559  1.00 74.89           C  
-ATOM   8247  OH  TYR D 123     102.105  33.187  12.814  1.00 72.08           O  
-ATOM   8248  N   LYS D 124      95.670  38.020  14.043  1.00 54.22           N  
-ATOM   8249  CA  LYS D 124      95.067  38.079  15.369  1.00 47.72           C  
-ATOM   8250  C   LYS D 124      94.683  36.684  15.856  1.00 44.66           C  
-ATOM   8251  O   LYS D 124      93.901  35.971  15.223  1.00 45.43           O  
-ATOM   8252  CB  LYS D 124      93.841  38.993  15.353  1.00 45.52           C  
-ATOM   8253  CG  LYS D 124      94.192  40.462  15.177  1.00 51.87           C  
-ATOM   8254  CD  LYS D 124      92.964  41.310  14.882  1.00 58.36           C  
-ATOM   8255  CE  LYS D 124      93.328  42.783  14.694  1.00 64.65           C  
-ATOM   8256  NZ  LYS D 124      94.304  43.042  13.590  1.00 65.18           N  
-ATOM   8257  N   ILE D 125      95.260  36.302  16.988  1.00 39.58           N  
-ATOM   8258  CA  ILE D 125      95.016  35.003  17.592  1.00 33.47           C  
-ATOM   8259  C   ILE D 125      93.953  35.065  18.690  1.00 28.42           C  
-ATOM   8260  O   ILE D 125      94.096  35.818  19.652  1.00 27.52           O  
-ATOM   8261  CB  ILE D 125      96.340  34.413  18.196  1.00 32.01           C  
-ATOM   8262  CG1 ILE D 125      96.046  33.709  19.517  1.00 44.10           C  
-ATOM   8263  CG2 ILE D 125      97.360  35.501  18.446  1.00 27.64           C  
-ATOM   8264  CD1 ILE D 125      97.286  33.314  20.288  1.00 58.10           C  
-ATOM   8265  N   MET D 126      92.885  34.284  18.544  1.00 24.12           N  
-ATOM   8266  CA  MET D 126      91.852  34.242  19.570  1.00 27.68           C  
-ATOM   8267  C   MET D 126      91.939  32.885  20.274  1.00 24.69           C  
-ATOM   8268  O   MET D 126      91.550  31.851  19.740  1.00 20.14           O  
-ATOM   8269  CB  MET D 126      90.457  34.472  18.972  1.00 32.70           C  
-ATOM   8270  CG  MET D 126      89.948  33.366  18.098  1.00 39.46           C  
-ATOM   8271  SD  MET D 126      88.494  32.583  18.795  1.00 54.98           S  
-ATOM   8272  CE  MET D 126      87.160  33.288  17.750  1.00 49.76           C  
-ATOM   8273  N   LEU D 127      92.483  32.920  21.483  1.00 24.00           N  
-ATOM   8274  CA  LEU D 127      92.685  31.745  22.311  1.00 22.72           C  
-ATOM   8275  C   LEU D 127      91.408  31.372  23.065  1.00 25.64           C  
-ATOM   8276  O   LEU D 127      90.691  32.242  23.543  1.00 30.11           O  
-ATOM   8277  CB  LEU D 127      93.812  32.056  23.291  1.00 11.60           C  
-ATOM   8278  CG  LEU D 127      94.525  30.923  23.997  1.00 17.35           C  
-ATOM   8279  CD1 LEU D 127      95.122  29.949  22.995  1.00 23.28           C  
-ATOM   8280  CD2 LEU D 127      95.604  31.529  24.842  1.00 17.78           C  
-ATOM   8281  N   SER D 128      91.119  30.081  23.169  1.00 26.63           N  
-ATOM   8282  CA  SER D 128      89.926  29.628  23.881  1.00 30.30           C  
-ATOM   8283  C   SER D 128      90.265  28.507  24.852  1.00 31.68           C  
-ATOM   8284  O   SER D 128      91.144  27.689  24.575  1.00 40.78           O  
-ATOM   8285  CB  SER D 128      88.863  29.132  22.895  1.00 36.19           C  
-ATOM   8286  OG  SER D 128      87.860  28.381  23.563  1.00 43.79           O  
-ATOM   8287  N   ASP D 129      89.559  28.469  25.982  1.00 27.92           N  
-ATOM   8288  CA  ASP D 129      89.777  27.441  27.001  1.00 25.07           C  
-ATOM   8289  C   ASP D 129      88.841  26.255  26.764  1.00 25.83           C  
-ATOM   8290  O   ASP D 129      87.644  26.336  27.044  1.00 23.87           O  
-ATOM   8291  CB  ASP D 129      89.528  28.016  28.392  1.00 24.32           C  
-ATOM   8292  CG  ASP D 129      90.057  27.126  29.491  1.00 35.17           C  
-ATOM   8293  OD1 ASP D 129      89.939  27.512  30.674  1.00 50.22           O  
-ATOM   8294  OD2 ASP D 129      90.595  26.045  29.177  1.00 36.79           O  
-ATOM   8295  N   ARG D 130      89.408  25.162  26.250  1.00 24.86           N  
-ATOM   8296  CA  ARG D 130      88.674  23.939  25.933  1.00 16.19           C  
-ATOM   8297  C   ARG D 130      87.768  24.090  24.713  1.00 19.21           C  
-ATOM   8298  O   ARG D 130      87.182  25.159  24.466  1.00  9.45           O  
-ATOM   8299  CB  ARG D 130      87.839  23.474  27.123  1.00 13.05           C  
-ATOM   8300  CG  ARG D 130      88.633  22.759  28.183  1.00 13.92           C  
-ATOM   8301  CD  ARG D 130      87.733  21.936  29.096  1.00 16.40           C  
-ATOM   8302  NE  ARG D 130      88.420  20.720  29.536  1.00 22.04           N  
-ATOM   8303  CZ  ARG D 130      89.393  20.691  30.439  1.00 20.05           C  
-ATOM   8304  NH1 ARG D 130      89.806  21.811  31.024  1.00 29.73           N  
-ATOM   8305  NH2 ARG D 130      89.967  19.543  30.739  1.00 12.95           N  
-ATOM   8306  N   HIS D 131      87.670  23.003  23.951  1.00 15.47           N  
-ATOM   8307  CA  HIS D 131      86.847  22.963  22.752  1.00 10.66           C  
-ATOM   8308  C   HIS D 131      85.627  22.101  23.037  1.00 11.26           C  
-ATOM   8309  O   HIS D 131      85.720  21.120  23.764  1.00 21.55           O  
-ATOM   8310  CB  HIS D 131      87.638  22.364  21.597  1.00 10.15           C  
-ATOM   8311  CG  HIS D 131      86.884  22.340  20.301  1.00 16.56           C  
-ATOM   8312  ND1 HIS D 131      85.776  21.545  20.099  1.00 19.95           N  
-ATOM   8313  CD2 HIS D 131      87.063  23.034  19.151  1.00 21.00           C  
-ATOM   8314  CE1 HIS D 131      85.305  21.750  18.881  1.00 27.32           C  
-ATOM   8315  NE2 HIS D 131      86.068  22.650  18.284  1.00 23.55           N  
-ATOM   8316  N   PRO D 132      84.467  22.453  22.465  1.00  6.20           N  
-ATOM   8317  CA  PRO D 132      83.207  21.727  22.648  1.00 10.35           C  
-ATOM   8318  C   PRO D 132      83.297  20.210  22.721  1.00 13.50           C  
-ATOM   8319  O   PRO D 132      82.551  19.577  23.467  1.00 22.45           O  
-ATOM   8320  CB  PRO D 132      82.381  22.202  21.471  1.00 15.60           C  
-ATOM   8321  CG  PRO D 132      82.763  23.654  21.415  1.00 10.02           C  
-ATOM   8322  CD  PRO D 132      84.269  23.602  21.566  1.00  5.47           C  
-ATOM   8323  N   ILE D 133      84.203  19.622  21.953  1.00  4.84           N  
-ATOM   8324  CA  ILE D 133      84.346  18.180  21.969  1.00  5.18           C  
-ATOM   8325  C   ILE D 133      84.689  17.659  23.376  1.00  5.43           C  
-ATOM   8326  O   ILE D 133      84.463  16.491  23.696  1.00  4.47           O  
-ATOM   8327  CB  ILE D 133      85.419  17.721  20.942  1.00 15.40           C  
-ATOM   8328  CG1 ILE D 133      86.825  18.073  21.427  1.00 11.75           C  
-ATOM   8329  CG2 ILE D 133      85.166  18.395  19.591  1.00 15.23           C  
-ATOM   8330  CD1 ILE D 133      87.903  17.571  20.494  1.00  9.77           C  
-ATOM   8331  N   ALA D 134      85.224  18.526  24.224  1.00  5.99           N  
-ATOM   8332  CA  ALA D 134      85.563  18.118  25.579  1.00  4.47           C  
-ATOM   8333  C   ALA D 134      84.300  17.687  26.294  1.00  9.00           C  
-ATOM   8334  O   ALA D 134      84.317  16.689  27.002  1.00 16.86           O  
-ATOM   8335  CB  ALA D 134      86.208  19.254  26.334  1.00  4.47           C  
-ATOM   8336  N   SER D 135      83.207  18.433  26.107  1.00  7.46           N  
-ATOM   8337  CA  SER D 135      81.926  18.113  26.757  1.00  4.82           C  
-ATOM   8338  C   SER D 135      81.117  17.077  26.010  1.00  7.10           C  
-ATOM   8339  O   SER D 135      80.448  16.239  26.609  1.00 14.27           O  
-ATOM   8340  CB  SER D 135      81.049  19.354  26.893  1.00  4.47           C  
-ATOM   8341  OG  SER D 135      80.633  19.823  25.625  1.00  9.43           O  
-ATOM   8342  N   THR D 136      81.177  17.141  24.691  1.00 10.30           N  
-ATOM   8343  CA  THR D 136      80.417  16.225  23.860  1.00 16.58           C  
-ATOM   8344  C   THR D 136      81.120  14.925  23.509  1.00 15.24           C  
-ATOM   8345  O   THR D 136      80.490  14.016  22.974  1.00 11.88           O  
-ATOM   8346  CB  THR D 136      80.018  16.902  22.546  1.00 19.73           C  
-ATOM   8347  OG1 THR D 136      81.199  17.207  21.791  1.00 14.01           O  
-ATOM   8348  CG2 THR D 136      79.284  18.200  22.830  1.00 37.43           C  
-ATOM   8349  N   ILE D 137      82.418  14.826  23.772  1.00 11.59           N  
-ATOM   8350  CA  ILE D 137      83.092  13.597  23.415  1.00 10.86           C  
-ATOM   8351  C   ILE D 137      84.193  13.133  24.341  1.00 16.91           C  
-ATOM   8352  O   ILE D 137      84.215  11.963  24.704  1.00 35.48           O  
-ATOM   8353  CB  ILE D 137      83.604  13.622  21.926  1.00  6.15           C  
-ATOM   8354  CG1 ILE D 137      85.084  13.284  21.846  1.00  7.39           C  
-ATOM   8355  CG2 ILE D 137      83.355  14.964  21.284  1.00 12.24           C  
-ATOM   8356  CD1 ILE D 137      85.575  13.218  20.413  1.00 24.63           C  
-ATOM   8357  N   CYS D 138      85.100  14.002  24.758  1.00 10.26           N  
-ATOM   8358  CA  CYS D 138      86.148  13.501  25.633  1.00 10.77           C  
-ATOM   8359  C   CYS D 138      85.646  13.057  27.003  1.00 10.46           C  
-ATOM   8360  O   CYS D 138      85.786  11.879  27.354  1.00 16.00           O  
-ATOM   8361  CB  CYS D 138      87.272  14.524  25.754  1.00 16.01           C  
-ATOM   8362  SG  CYS D 138      88.170  14.655  24.196  1.00 27.11           S  
-ATOM   8363  N   PHE D 139      85.048  13.966  27.771  1.00  5.91           N  
-ATOM   8364  CA  PHE D 139      84.553  13.597  29.095  1.00  9.50           C  
-ATOM   8365  C   PHE D 139      83.484  12.495  29.061  1.00 18.12           C  
-ATOM   8366  O   PHE D 139      83.683  11.420  29.648  1.00 26.60           O  
-ATOM   8367  CB  PHE D 139      84.023  14.823  29.852  1.00  4.47           C  
-ATOM   8368  CG  PHE D 139      85.095  15.631  30.526  1.00  6.78           C  
-ATOM   8369  CD1 PHE D 139      85.960  16.419  29.790  1.00 12.94           C  
-ATOM   8370  CD2 PHE D 139      85.252  15.592  31.906  1.00 18.87           C  
-ATOM   8371  CE1 PHE D 139      86.968  17.157  30.419  1.00  6.22           C  
-ATOM   8372  CE2 PHE D 139      86.262  16.328  32.543  1.00  8.12           C  
-ATOM   8373  CZ  PHE D 139      87.114  17.106  31.796  1.00  4.47           C  
-ATOM   8374  N   PRO D 140      82.348  12.725  28.368  1.00 17.07           N  
-ATOM   8375  CA  PRO D 140      81.330  11.664  28.343  1.00 17.33           C  
-ATOM   8376  C   PRO D 140      81.921  10.268  28.077  1.00 12.63           C  
-ATOM   8377  O   PRO D 140      81.533   9.264  28.699  1.00  4.47           O  
-ATOM   8378  CB  PRO D 140      80.355  12.136  27.247  1.00 14.54           C  
-ATOM   8379  CG  PRO D 140      81.177  13.063  26.389  1.00  4.47           C  
-ATOM   8380  CD  PRO D 140      82.006  13.797  27.418  1.00 18.23           C  
-ATOM   8381  N   LEU D 141      82.892  10.220  27.175  1.00  8.81           N  
-ATOM   8382  CA  LEU D 141      83.529   8.960  26.843  1.00 12.93           C  
-ATOM   8383  C   LEU D 141      84.403   8.448  27.989  1.00  7.53           C  
-ATOM   8384  O   LEU D 141      84.518   7.236  28.205  1.00 12.41           O  
-ATOM   8385  CB  LEU D 141      84.353   9.112  25.561  1.00 10.49           C  
-ATOM   8386  CG  LEU D 141      84.006   8.173  24.397  1.00  5.49           C  
-ATOM   8387  CD1 LEU D 141      82.501   7.884  24.306  1.00  4.47           C  
-ATOM   8388  CD2 LEU D 141      84.533   8.817  23.123  1.00  7.53           C  
-ATOM   8389  N   SER D 142      85.029   9.349  28.728  1.00  4.47           N  
-ATOM   8390  CA  SER D 142      85.833   8.866  29.822  1.00  4.47           C  
-ATOM   8391  C   SER D 142      84.915   8.281  30.880  1.00 14.24           C  
-ATOM   8392  O   SER D 142      85.197   7.207  31.433  1.00 21.13           O  
-ATOM   8393  CB  SER D 142      86.668   9.982  30.402  1.00  6.06           C  
-ATOM   8394  OG  SER D 142      87.597  10.415  29.433  1.00 14.23           O  
-ATOM   8395  N   ARG D 143      83.807   8.969  31.152  1.00 14.09           N  
-ATOM   8396  CA  ARG D 143      82.846   8.477  32.141  1.00 11.84           C  
-ATOM   8397  C   ARG D 143      82.384   7.065  31.802  1.00  8.60           C  
-ATOM   8398  O   ARG D 143      82.304   6.205  32.686  1.00  4.47           O  
-ATOM   8399  CB  ARG D 143      81.634   9.395  32.225  1.00  8.13           C  
-ATOM   8400  CG  ARG D 143      81.935  10.747  32.836  1.00 10.87           C  
-ATOM   8401  CD  ARG D 143      82.385  10.659  34.291  1.00  4.47           C  
-ATOM   8402  NE  ARG D 143      82.782  11.980  34.782  1.00 13.66           N  
-ATOM   8403  CZ  ARG D 143      83.337  12.207  35.972  1.00 16.33           C  
-ATOM   8404  NH1 ARG D 143      83.564  11.195  36.798  1.00  5.36           N  
-ATOM   8405  NH2 ARG D 143      83.657  13.450  36.337  1.00 14.99           N  
-ATOM   8406  N   TYR D 144      82.072   6.832  30.529  1.00  4.54           N  
-ATOM   8407  CA  TYR D 144      81.650   5.505  30.107  1.00 11.20           C  
-ATOM   8408  C   TYR D 144      82.729   4.478  30.453  1.00 11.20           C  
-ATOM   8409  O   TYR D 144      82.485   3.532  31.204  1.00  6.47           O  
-ATOM   8410  CB  TYR D 144      81.379   5.470  28.598  1.00 11.87           C  
-ATOM   8411  CG  TYR D 144      81.215   4.071  28.055  1.00 13.61           C  
-ATOM   8412  CD1 TYR D 144      82.269   3.422  27.408  1.00 20.67           C  
-ATOM   8413  CD2 TYR D 144      80.023   3.369  28.242  1.00 22.20           C  
-ATOM   8414  CE1 TYR D 144      82.142   2.100  26.960  1.00 31.76           C  
-ATOM   8415  CE2 TYR D 144      79.884   2.046  27.802  1.00 32.26           C  
-ATOM   8416  CZ  TYR D 144      80.949   1.417  27.162  1.00 34.31           C  
-ATOM   8417  OH  TYR D 144      80.824   0.110  26.740  1.00 38.81           O  
-ATOM   8418  N   LEU D 145      83.921   4.684  29.902  1.00 13.73           N  
-ATOM   8419  CA  LEU D 145      85.044   3.786  30.121  1.00 14.92           C  
-ATOM   8420  C   LEU D 145      85.263   3.435  31.583  1.00 13.57           C  
-ATOM   8421  O   LEU D 145      85.545   2.283  31.907  1.00 22.35           O  
-ATOM   8422  CB  LEU D 145      86.319   4.387  29.528  1.00 16.20           C  
-ATOM   8423  CG  LEU D 145      86.254   4.598  28.012  1.00 11.01           C  
-ATOM   8424  CD1 LEU D 145      87.557   5.182  27.536  1.00 11.17           C  
-ATOM   8425  CD2 LEU D 145      85.982   3.279  27.313  1.00  4.47           C  
-ATOM   8426  N   VAL D 146      85.136   4.412  32.469  1.00  4.47           N  
-ATOM   8427  CA  VAL D 146      85.316   4.140  33.887  1.00  5.97           C  
-ATOM   8428  C   VAL D 146      84.097   3.463  34.519  1.00  6.22           C  
-ATOM   8429  O   VAL D 146      84.176   2.933  35.624  1.00  8.09           O  
-ATOM   8430  CB  VAL D 146      85.646   5.427  34.632  1.00  9.19           C  
-ATOM   8431  CG1 VAL D 146      85.130   5.380  36.054  1.00 19.79           C  
-ATOM   8432  CG2 VAL D 146      87.143   5.601  34.645  1.00 14.73           C  
-ATOM   8433  N   GLY D 147      82.974   3.477  33.813  1.00  6.00           N  
-ATOM   8434  CA  GLY D 147      81.781   2.834  34.331  1.00  7.56           C  
-ATOM   8435  C   GLY D 147      80.842   3.750  35.091  1.00 14.57           C  
-ATOM   8436  O   GLY D 147      79.866   3.290  35.704  1.00  9.64           O  
-ATOM   8437  N   ASP D 148      81.120   5.051  35.049  1.00 18.45           N  
-ATOM   8438  CA  ASP D 148      80.278   6.012  35.746  1.00 19.94           C  
-ATOM   8439  C   ASP D 148      79.061   6.482  34.940  1.00 13.49           C  
-ATOM   8440  O   ASP D 148      78.136   7.075  35.493  1.00 10.13           O  
-ATOM   8441  CB  ASP D 148      81.114   7.224  36.182  1.00 32.66           C  
-ATOM   8442  CG  ASP D 148      81.909   6.964  37.458  1.00 43.67           C  
-ATOM   8443  OD1 ASP D 148      81.393   6.239  38.339  1.00 52.15           O  
-ATOM   8444  OD2 ASP D 148      83.035   7.500  37.590  1.00 44.28           O  
-ATOM   8445  N   MET D 149      79.048   6.195  33.644  1.00 14.28           N  
-ATOM   8446  CA  MET D 149      77.957   6.629  32.777  1.00 13.18           C  
-ATOM   8447  C   MET D 149      77.529   5.553  31.789  1.00 19.49           C  
-ATOM   8448  O   MET D 149      78.354   4.770  31.319  1.00 22.36           O  
-ATOM   8449  CB  MET D 149      78.400   7.880  32.021  1.00  4.94           C  
-ATOM   8450  CG  MET D 149      77.459   8.343  30.939  1.00 10.56           C  
-ATOM   8451  SD  MET D 149      78.043   9.876  30.106  1.00 17.29           S  
-ATOM   8452  CE  MET D 149      77.834  11.024  31.444  1.00 14.99           C  
-ATOM   8453  N   SER D 150      76.237   5.521  31.471  1.00 27.54           N  
-ATOM   8454  CA  SER D 150      75.688   4.532  30.531  1.00 32.80           C  
-ATOM   8455  C   SER D 150      75.840   4.965  29.070  1.00 27.40           C  
-ATOM   8456  O   SER D 150      75.505   6.094  28.714  1.00 37.69           O  
-ATOM   8457  CB  SER D 150      74.200   4.284  30.835  1.00 41.75           C  
-ATOM   8458  OG  SER D 150      73.433   5.486  30.796  1.00 34.39           O  
-ATOM   8459  N   PRO D 151      76.316   4.064  28.198  1.00 14.78           N  
-ATOM   8460  CA  PRO D 151      76.509   4.369  26.772  1.00 16.88           C  
-ATOM   8461  C   PRO D 151      75.316   5.046  26.103  1.00 15.75           C  
-ATOM   8462  O   PRO D 151      75.465   5.774  25.115  1.00 18.27           O  
-ATOM   8463  CB  PRO D 151      76.794   2.999  26.162  1.00  8.61           C  
-ATOM   8464  CG  PRO D 151      76.005   2.096  27.029  1.00 11.33           C  
-ATOM   8465  CD  PRO D 151      76.346   2.612  28.412  1.00 10.90           C  
-ATOM   8466  N   ALA D 152      74.134   4.799  26.654  1.00 11.48           N  
-ATOM   8467  CA  ALA D 152      72.892   5.348  26.127  1.00  7.69           C  
-ATOM   8468  C   ALA D 152      72.938   6.831  25.781  1.00 12.78           C  
-ATOM   8469  O   ALA D 152      72.128   7.312  24.980  1.00 16.24           O  
-ATOM   8470  CB  ALA D 152      71.775   5.094  27.106  1.00  4.47           C  
-ATOM   8471  N   ALA D 153      73.878   7.564  26.365  1.00 11.62           N  
-ATOM   8472  CA  ALA D 153      73.951   8.991  26.086  1.00 13.56           C  
-ATOM   8473  C   ALA D 153      75.021   9.383  25.085  1.00 15.31           C  
-ATOM   8474  O   ALA D 153      75.225  10.572  24.850  1.00 25.61           O  
-ATOM   8475  CB  ALA D 153      74.160   9.764  27.386  1.00 16.92           C  
-ATOM   8476  N   LEU D 154      75.703   8.411  24.488  1.00 10.80           N  
-ATOM   8477  CA  LEU D 154      76.757   8.754  23.545  1.00 11.32           C  
-ATOM   8478  C   LEU D 154      76.244   9.270  22.208  1.00 17.23           C  
-ATOM   8479  O   LEU D 154      76.766  10.256  21.673  1.00 22.95           O  
-ATOM   8480  CB  LEU D 154      77.715   7.572  23.360  1.00  4.47           C  
-ATOM   8481  CG  LEU D 154      78.456   7.287  24.688  1.00  6.14           C  
-ATOM   8482  CD1 LEU D 154      79.327   6.066  24.555  1.00  4.47           C  
-ATOM   8483  CD2 LEU D 154      79.302   8.488  25.104  1.00  4.47           C  
-ATOM   8484  N   PRO D 155      75.191   8.646  21.662  1.00 19.87           N  
-ATOM   8485  CA  PRO D 155      74.662   9.109  20.369  1.00 18.29           C  
-ATOM   8486  C   PRO D 155      74.241  10.573  20.415  1.00 15.28           C  
-ATOM   8487  O   PRO D 155      74.504  11.341  19.485  1.00 14.22           O  
-ATOM   8488  CB  PRO D 155      73.477   8.178  20.124  1.00 17.76           C  
-ATOM   8489  CG  PRO D 155      73.866   6.916  20.861  1.00 19.80           C  
-ATOM   8490  CD  PRO D 155      74.442   7.476  22.151  1.00 19.53           C  
-ATOM   8491  N   GLY D 156      73.593  10.947  21.514  1.00 17.39           N  
-ATOM   8492  CA  GLY D 156      73.138  12.312  21.684  1.00 22.71           C  
-ATOM   8493  C   GLY D 156      74.259  13.332  21.699  1.00 23.92           C  
-ATOM   8494  O   GLY D 156      74.027  14.508  21.412  1.00 33.14           O  
-ATOM   8495  N   LEU D 157      75.477  12.902  22.017  1.00 20.08           N  
-ATOM   8496  CA  LEU D 157      76.595  13.843  22.063  1.00 23.80           C  
-ATOM   8497  C   LEU D 157      77.589  13.680  20.916  1.00 24.84           C  
-ATOM   8498  O   LEU D 157      78.069  14.680  20.367  1.00 29.54           O  
-ATOM   8499  CB  LEU D 157      77.353  13.717  23.389  1.00 26.44           C  
-ATOM   8500  CG  LEU D 157      76.560  13.531  24.690  1.00 22.99           C  
-ATOM   8501  CD1 LEU D 157      77.524  13.429  25.889  1.00  4.47           C  
-ATOM   8502  CD2 LEU D 157      75.583  14.682  24.849  1.00 16.41           C  
-ATOM   8503  N   LEU D 158      77.885  12.429  20.554  1.00 13.71           N  
-ATOM   8504  CA  LEU D 158      78.847  12.137  19.498  1.00  8.44           C  
-ATOM   8505  C   LEU D 158      78.336  12.277  18.087  1.00 13.73           C  
-ATOM   8506  O   LEU D 158      79.024  12.824  17.218  1.00 18.52           O  
-ATOM   8507  CB  LEU D 158      79.385  10.724  19.655  1.00  5.73           C  
-ATOM   8508  CG  LEU D 158      79.958  10.415  21.032  1.00 15.36           C  
-ATOM   8509  CD1 LEU D 158      80.590   9.024  21.048  1.00 13.67           C  
-ATOM   8510  CD2 LEU D 158      80.974  11.490  21.385  1.00 18.27           C  
-ATOM   8511  N   PHE D 159      77.128  11.783  17.856  1.00 12.32           N  
-ATOM   8512  CA  PHE D 159      76.560  11.818  16.524  1.00 10.58           C  
-ATOM   8513  C   PHE D 159      75.838  13.080  16.077  1.00 14.19           C  
-ATOM   8514  O   PHE D 159      75.538  13.226  14.898  1.00 25.90           O  
-ATOM   8515  CB  PHE D 159      75.648  10.619  16.359  1.00 11.76           C  
-ATOM   8516  CG  PHE D 159      76.293   9.314  16.738  1.00 17.80           C  
-ATOM   8517  CD1 PHE D 159      77.669   9.133  16.608  1.00 16.38           C  
-ATOM   8518  CD2 PHE D 159      75.519   8.242  17.166  1.00 18.42           C  
-ATOM   8519  CE1 PHE D 159      78.265   7.902  16.891  1.00  9.07           C  
-ATOM   8520  CE2 PHE D 159      76.106   7.007  17.452  1.00 20.71           C  
-ATOM   8521  CZ  PHE D 159      77.486   6.840  17.311  1.00 15.81           C  
-ATOM   8522  N   THR D 160      75.564  13.999  16.991  1.00 16.29           N  
-ATOM   8523  CA  THR D 160      74.873  15.228  16.615  1.00 17.72           C  
-ATOM   8524  C   THR D 160      75.811  16.425  16.474  1.00 22.00           C  
-ATOM   8525  O   THR D 160      75.371  17.578  16.540  1.00 27.31           O  
-ATOM   8526  CB  THR D 160      73.773  15.591  17.648  1.00 22.98           C  
-ATOM   8527  OG1 THR D 160      74.347  15.715  18.957  1.00 25.70           O  
-ATOM   8528  CG2 THR D 160      72.712  14.526  17.673  1.00 22.66           C  
-ATOM   8529  N   LEU D 161      77.099  16.165  16.273  1.00 20.47           N  
-ATOM   8530  CA  LEU D 161      78.055  17.260  16.149  1.00 19.31           C  
-ATOM   8531  C   LEU D 161      77.821  18.142  14.937  1.00 18.75           C  
-ATOM   8532  O   LEU D 161      77.510  17.655  13.855  1.00 30.07           O  
-ATOM   8533  CB  LEU D 161      79.483  16.723  16.126  1.00 10.05           C  
-ATOM   8534  CG  LEU D 161      79.925  16.193  17.485  1.00  4.47           C  
-ATOM   8535  CD1 LEU D 161      81.396  15.898  17.454  1.00  4.47           C  
-ATOM   8536  CD2 LEU D 161      79.624  17.228  18.556  1.00  6.03           C  
-ATOM   8537  N   PRO D 162      77.960  19.463  15.107  1.00 17.44           N  
-ATOM   8538  CA  PRO D 162      77.760  20.415  14.011  1.00 24.77           C  
-ATOM   8539  C   PRO D 162      79.026  20.591  13.181  1.00 26.73           C  
-ATOM   8540  O   PRO D 162      80.144  20.448  13.699  1.00 27.45           O  
-ATOM   8541  CB  PRO D 162      77.382  21.687  14.741  1.00 22.80           C  
-ATOM   8542  CG  PRO D 162      78.278  21.609  15.946  1.00 19.03           C  
-ATOM   8543  CD  PRO D 162      78.148  20.170  16.384  1.00 14.27           C  
-ATOM   8544  N   ALA D 163      78.840  20.905  11.902  1.00 20.66           N  
-ATOM   8545  CA  ALA D 163      79.958  21.096  10.992  1.00 22.44           C  
-ATOM   8546  C   ALA D 163      81.003  22.030  11.589  1.00 26.28           C  
-ATOM   8547  O   ALA D 163      80.709  23.171  11.961  1.00 23.99           O  
-ATOM   8548  CB  ALA D 163      79.463  21.654   9.675  1.00 30.97           C  
-ATOM   8549  N   GLU D 164      82.229  21.533  11.682  1.00 33.04           N  
-ATOM   8550  CA  GLU D 164      83.327  22.317  12.226  1.00 36.08           C  
-ATOM   8551  C   GLU D 164      83.933  23.144  11.096  1.00 43.13           C  
-ATOM   8552  O   GLU D 164      84.276  22.611  10.034  1.00 42.99           O  
-ATOM   8553  CB  GLU D 164      84.406  21.400  12.819  1.00 31.15           C  
-ATOM   8554  CG  GLU D 164      85.530  22.133  13.535  1.00 36.09           C  
-ATOM   8555  CD  GLU D 164      85.115  22.633  14.911  1.00 45.49           C  
-ATOM   8556  OE1 GLU D 164      83.910  22.562  15.225  1.00 54.71           O  
-ATOM   8557  OE2 GLU D 164      85.988  23.098  15.680  1.00 40.08           O  
-ATOM   8558  N   PRO D 165      84.039  24.467  11.298  1.00 46.12           N  
-ATOM   8559  CA  PRO D 165      84.613  25.371  10.296  1.00 42.29           C  
-ATOM   8560  C   PRO D 165      86.135  25.181  10.218  1.00 46.98           C  
-ATOM   8561  O   PRO D 165      86.805  24.938  11.232  1.00 46.97           O  
-ATOM   8562  CB  PRO D 165      84.218  26.748  10.814  1.00 46.22           C  
-ATOM   8563  CG  PRO D 165      84.198  26.551  12.304  1.00 44.51           C  
-ATOM   8564  CD  PRO D 165      83.489  25.225  12.437  1.00 43.47           C  
-ATOM   8565  N   PRO D 166      86.701  25.287   9.008  1.00 48.36           N  
-ATOM   8566  CA  PRO D 166      88.142  25.120   8.784  1.00 44.94           C  
-ATOM   8567  C   PRO D 166      89.012  26.006   9.660  1.00 35.32           C  
-ATOM   8568  O   PRO D 166      88.679  27.165   9.895  1.00 34.41           O  
-ATOM   8569  CB  PRO D 166      88.301  25.456   7.302  1.00 50.64           C  
-ATOM   8570  CG  PRO D 166      86.977  25.038   6.719  1.00 54.48           C  
-ATOM   8571  CD  PRO D 166      86.007  25.588   7.743  1.00 51.79           C  
-ATOM   8572  N   GLY D 167      90.119  25.453  10.148  1.00 28.19           N  
-ATOM   8573  CA  GLY D 167      91.028  26.240  10.962  1.00 27.79           C  
-ATOM   8574  C   GLY D 167      91.011  26.020  12.462  1.00 29.33           C  
-ATOM   8575  O   GLY D 167      91.464  26.889  13.227  1.00 24.51           O  
-ATOM   8576  N   THR D 168      90.499  24.875  12.902  1.00 23.93           N  
-ATOM   8577  CA  THR D 168      90.464  24.613  14.329  1.00 17.76           C  
-ATOM   8578  C   THR D 168      91.790  24.014  14.748  1.00 22.25           C  
-ATOM   8579  O   THR D 168      92.220  22.995  14.214  1.00 27.73           O  
-ATOM   8580  CB  THR D 168      89.334  23.644  14.710  1.00 10.12           C  
-ATOM   8581  OG1 THR D 168      88.078  24.219  14.344  1.00 10.21           O  
-ATOM   8582  CG2 THR D 168      89.337  23.380  16.212  1.00  4.47           C  
-ATOM   8583  N   ASN D 169      92.446  24.667  15.695  1.00 21.77           N  
-ATOM   8584  CA  ASN D 169      93.724  24.198  16.204  1.00 16.18           C  
-ATOM   8585  C   ASN D 169      93.532  23.686  17.626  1.00 16.18           C  
-ATOM   8586  O   ASN D 169      93.364  24.456  18.572  1.00 15.96           O  
-ATOM   8587  CB  ASN D 169      94.746  25.333  16.163  1.00 16.35           C  
-ATOM   8588  CG  ASN D 169      95.123  25.712  14.751  1.00  9.79           C  
-ATOM   8589  OD1 ASN D 169      95.832  24.980  14.087  1.00 23.47           O  
-ATOM   8590  ND2 ASN D 169      94.634  26.848  14.282  1.00  6.51           N  
-ATOM   8591  N   LEU D 170      93.541  22.370  17.761  1.00 18.01           N  
-ATOM   8592  CA  LEU D 170      93.355  21.738  19.051  1.00 17.97           C  
-ATOM   8593  C   LEU D 170      94.714  21.498  19.679  1.00 19.05           C  
-ATOM   8594  O   LEU D 170      95.536  20.763  19.133  1.00 22.95           O  
-ATOM   8595  CB  LEU D 170      92.622  20.418  18.860  1.00 12.07           C  
-ATOM   8596  CG  LEU D 170      91.689  19.980  19.976  1.00 12.43           C  
-ATOM   8597  CD1 LEU D 170      90.998  18.701  19.543  1.00 23.41           C  
-ATOM   8598  CD2 LEU D 170      92.471  19.774  21.258  1.00 13.06           C  
-ATOM   8599  N   VAL D 171      94.950  22.134  20.820  1.00 15.36           N  
-ATOM   8600  CA  VAL D 171      96.211  21.983  21.527  1.00 17.31           C  
-ATOM   8601  C   VAL D 171      95.988  21.200  22.816  1.00 20.40           C  
-ATOM   8602  O   VAL D 171      95.540  21.756  23.828  1.00 23.96           O  
-ATOM   8603  CB  VAL D 171      96.820  23.355  21.874  1.00 18.48           C  
-ATOM   8604  CG1 VAL D 171      98.163  23.179  22.561  1.00 13.63           C  
-ATOM   8605  CG2 VAL D 171      96.971  24.175  20.614  1.00 22.59           C  
-ATOM   8606  N   VAL D 172      96.291  19.906  22.767  1.00 16.28           N  
-ATOM   8607  CA  VAL D 172      96.141  19.042  23.926  1.00 16.88           C  
-ATOM   8608  C   VAL D 172      97.318  19.229  24.870  1.00 20.01           C  
-ATOM   8609  O   VAL D 172      98.463  18.983  24.497  1.00 22.91           O  
-ATOM   8610  CB  VAL D 172      96.104  17.557  23.528  1.00 15.62           C  
-ATOM   8611  CG1 VAL D 172      96.012  16.692  24.786  1.00 14.66           C  
-ATOM   8612  CG2 VAL D 172      94.928  17.292  22.593  1.00  9.79           C  
-ATOM   8613  N   CYS D 173      97.033  19.664  26.089  1.00 22.34           N  
-ATOM   8614  CA  CYS D 173      98.075  19.864  27.082  1.00 31.51           C  
-ATOM   8615  C   CYS D 173      98.366  18.534  27.752  1.00 34.13           C  
-ATOM   8616  O   CYS D 173      97.465  17.704  27.903  1.00 36.36           O  
-ATOM   8617  CB  CYS D 173      97.618  20.879  28.132  1.00 38.27           C  
-ATOM   8618  SG  CYS D 173      97.286  22.515  27.454  1.00 57.81           S  
-ATOM   8619  N   THR D 174      99.621  18.330  28.150  1.00 35.60           N  
-ATOM   8620  CA  THR D 174     100.019  17.087  28.811  1.00 39.50           C  
-ATOM   8621  C   THR D 174     100.962  17.361  29.969  1.00 39.23           C  
-ATOM   8622  O   THR D 174     101.763  18.287  29.912  1.00 41.95           O  
-ATOM   8623  CB  THR D 174     100.755  16.164  27.856  1.00 41.47           C  
-ATOM   8624  OG1 THR D 174     102.096  16.641  27.690  1.00 42.90           O  
-ATOM   8625  CG2 THR D 174     100.060  16.143  26.497  1.00 48.28           C  
-ATOM   8626  N   VAL D 175     100.872  16.544  31.010  1.00 41.71           N  
-ATOM   8627  CA  VAL D 175     101.726  16.697  32.179  1.00 47.89           C  
-ATOM   8628  C   VAL D 175     102.190  15.315  32.567  1.00 57.42           C  
-ATOM   8629  O   VAL D 175     101.547  14.338  32.202  1.00 62.46           O  
-ATOM   8630  CB  VAL D 175     100.947  17.270  33.367  1.00 50.54           C  
-ATOM   8631  CG1 VAL D 175     101.885  17.497  34.552  1.00 51.31           C  
-ATOM   8632  CG2 VAL D 175     100.256  18.560  32.957  1.00 50.57           C  
-ATOM   8633  N   SER D 176     103.302  15.216  33.290  1.00 65.13           N  
-ATOM   8634  CA  SER D 176     103.772  13.902  33.722  1.00 73.99           C  
-ATOM   8635  C   SER D 176     102.732  13.400  34.730  1.00 78.47           C  
-ATOM   8636  O   SER D 176     102.035  14.206  35.357  1.00 76.55           O  
-ATOM   8637  CB  SER D 176     105.158  13.999  34.373  1.00 75.63           C  
-ATOM   8638  OG  SER D 176     105.114  14.747  35.576  1.00 85.19           O  
-ATOM   8639  N   LEU D 177     102.623  12.081  34.882  1.00 84.52           N  
-ATOM   8640  CA  LEU D 177     101.632  11.487  35.783  1.00 86.89           C  
-ATOM   8641  C   LEU D 177     101.730  11.870  37.263  1.00 86.52           C  
-ATOM   8642  O   LEU D 177     100.759  12.361  37.836  1.00 84.59           O  
-ATOM   8643  CB  LEU D 177     101.636   9.958  35.634  1.00 90.04           C  
-ATOM   8644  CG  LEU D 177     100.657   9.162  36.501  1.00 91.55           C  
-ATOM   8645  CD1 LEU D 177      99.257   9.731  36.358  1.00 92.50           C  
-ATOM   8646  CD2 LEU D 177     100.692   7.695  36.092  1.00 92.77           C  
-ATOM   8647  N   PRO D 178     102.892  11.646  37.904  1.00 89.51           N  
-ATOM   8648  CA  PRO D 178     103.039  11.994  39.326  1.00 89.54           C  
-ATOM   8649  C   PRO D 178     102.831  13.479  39.639  1.00 86.36           C  
-ATOM   8650  O   PRO D 178     102.443  13.841  40.754  1.00 79.74           O  
-ATOM   8651  CB  PRO D 178     104.459  11.530  39.647  1.00 93.67           C  
-ATOM   8652  CG  PRO D 178     104.637  10.350  38.724  1.00 96.67           C  
-ATOM   8653  CD  PRO D 178     104.065  10.887  37.431  1.00 93.09           C  
-ATOM   8654  N   SER D 179     103.096  14.325  38.645  1.00 88.75           N  
-ATOM   8655  CA  SER D 179     102.950  15.774  38.773  1.00 90.65           C  
-ATOM   8656  C   SER D 179     101.485  16.180  38.647  1.00 92.89           C  
-ATOM   8657  O   SER D 179     101.027  17.113  39.303  1.00 94.78           O  
-ATOM   8658  CB  SER D 179     103.772  16.477  37.690  1.00 86.80           C  
-ATOM   8659  OG  SER D 179     103.610  17.882  37.745  1.00 84.61           O  
-ATOM   8660  N   HIS D 180     100.761  15.473  37.787  1.00 94.25           N  
-ATOM   8661  CA  HIS D 180      99.339  15.720  37.558  1.00 93.19           C  
-ATOM   8662  C   HIS D 180      98.556  15.434  38.848  1.00 92.92           C  
-ATOM   8663  O   HIS D 180      97.547  16.089  39.134  1.00 91.00           O  
-ATOM   8664  CB  HIS D 180      98.861  14.813  36.405  1.00 90.03           C  
-ATOM   8665  CG  HIS D 180      97.397  14.914  36.086  1.00 82.99           C  
-ATOM   8666  ND1 HIS D 180      96.843  14.307  34.979  1.00 77.02           N  
-ATOM   8667  CD2 HIS D 180      96.371  15.519  36.733  1.00 78.57           C  
-ATOM   8668  CE1 HIS D 180      95.542  14.533  34.959  1.00 75.75           C  
-ATOM   8669  NE2 HIS D 180      95.229  15.265  36.012  1.00 72.44           N  
-ATOM   8670  N   LEU D 181      99.043  14.473  39.634  1.00 91.55           N  
-ATOM   8671  CA  LEU D 181      98.390  14.081  40.883  1.00 91.27           C  
-ATOM   8672  C   LEU D 181      98.667  15.011  42.067  1.00 95.22           C  
-ATOM   8673  O   LEU D 181      98.295  14.714  43.205  1.00 93.43           O  
-ATOM   8674  CB  LEU D 181      98.790  12.650  41.240  1.00 80.87           C  
-ATOM   8675  CG  LEU D 181      98.668  11.680  40.061  1.00 71.96           C  
-ATOM   8676  CD1 LEU D 181      98.980  10.269  40.537  1.00 72.65           C  
-ATOM   8677  CD2 LEU D 181      97.269  11.754  39.457  1.00 60.09           C  
-ATOM   8678  N   SER D 182      99.322  16.135  41.790  1.00 99.13           N  
-ATOM   8679  CA  SER D 182      99.628  17.125  42.820  1.00 99.65           C  
-ATOM   8680  C   SER D 182      98.967  18.456  42.449  1.00101.42           C  
-ATOM   8681  O   SER D 182      98.633  19.257  43.325  1.00101.46           O  
-ATOM   8682  CB  SER D 182     101.146  17.313  42.961  1.00 96.82           C  
-ATOM   8683  OG  SER D 182     101.719  17.881  41.794  1.00 93.79           O  
-ATOM   8684  N   ARG D 183      98.778  18.673  41.144  1.00101.72           N  
-ATOM   8685  CA  ARG D 183      98.151  19.890  40.615  1.00 97.68           C  
-ATOM   8686  C   ARG D 183      96.686  19.956  41.046  1.00 95.25           C  
-ATOM   8687  O   ARG D 183      96.086  21.033  41.117  1.00 91.19           O  
-ATOM   8688  CB  ARG D 183      98.219  19.903  39.080  1.00 95.90           C  
-ATOM   8689  CG  ARG D 183      99.627  19.898  38.480  1.00 91.15           C  
-ATOM   8690  CD  ARG D 183     100.383  21.191  38.782  1.00 86.17           C  
-ATOM   8691  NE  ARG D 183     101.697  21.224  38.140  1.00 82.21           N  
-ATOM   8692  CZ  ARG D 183     101.894  21.247  36.823  1.00 79.88           C  
-ATOM   8693  NH1 ARG D 183     100.862  21.241  35.988  1.00 77.50           N  
-ATOM   8694  NH2 ARG D 183     103.127  21.276  36.338  1.00 80.47           N  
-ATOM   8695  N   VAL D 184      96.116  18.789  41.321  1.00 95.84           N  
-ATOM   8696  CA  VAL D 184      94.730  18.695  41.749  1.00 97.40           C  
-ATOM   8697  C   VAL D 184      94.662  18.787  43.277  1.00101.59           C  
-ATOM   8698  O   VAL D 184      94.373  19.849  43.839  1.00103.92           O  
-ATOM   8699  CB  VAL D 184      94.102  17.360  41.285  1.00 92.38           C  
-ATOM   8700  CG1 VAL D 184      92.599  17.389  41.502  1.00 89.73           C  
-ATOM   8701  CG2 VAL D 184      94.428  17.110  39.819  1.00 85.07           C  
-ATOM   8702  N   THR D 193      87.432  15.556  42.913  1.00 99.33           N  
-ATOM   8703  CA  THR D 193      87.915  14.326  43.539  1.00 97.25           C  
-ATOM   8704  C   THR D 193      89.102  13.736  42.775  1.00 95.53           C  
-ATOM   8705  O   THR D 193      89.110  13.710  41.543  1.00 97.13           O  
-ATOM   8706  CB  THR D 193      86.783  13.302  43.622  1.00 94.17           C  
-ATOM   8707  N   VAL D 194      90.100  13.257  43.512  1.00 90.41           N  
-ATOM   8708  CA  VAL D 194      91.289  12.675  42.897  1.00 85.20           C  
-ATOM   8709  C   VAL D 194      91.285  11.145  42.925  1.00 81.61           C  
-ATOM   8710  O   VAL D 194      91.620  10.524  43.941  1.00 83.36           O  
-ATOM   8711  CB  VAL D 194      92.549  13.207  43.587  1.00 84.39           C  
-ATOM   8712  N   ASN D 195      90.894  10.545  41.804  1.00 71.97           N  
-ATOM   8713  CA  ASN D 195      90.868   9.096  41.681  1.00 65.32           C  
-ATOM   8714  C   ASN D 195      91.566   8.698  40.378  1.00 62.97           C  
-ATOM   8715  O   ASN D 195      91.140   9.066  39.280  1.00 58.45           O  
-ATOM   8716  CB  ASN D 195      89.426   8.559  41.694  1.00 63.87           C  
-ATOM   8717  CG  ASN D 195      88.636   8.957  40.452  1.00 63.65           C  
-ATOM   8718  OD1 ASN D 195      87.699   8.261  40.032  1.00 57.21           O  
-ATOM   8719  ND2 ASN D 195      89.003  10.086  39.864  1.00 64.30           N  
-ATOM   8720  N   LEU D 196      92.656   7.955  40.509  1.00 60.22           N  
-ATOM   8721  CA  LEU D 196      93.401   7.508  39.347  1.00 55.45           C  
-ATOM   8722  C   LEU D 196      92.477   7.083  38.205  1.00 48.59           C  
-ATOM   8723  O   LEU D 196      92.441   7.736  37.166  1.00 44.39           O  
-ATOM   8724  CB  LEU D 196      94.312   6.340  39.728  1.00 63.17           C  
-ATOM   8725  CG  LEU D 196      95.423   6.614  40.737  1.00 63.26           C  
-ATOM   8726  CD1 LEU D 196      96.032   5.291  41.197  1.00 71.30           C  
-ATOM   8727  CD2 LEU D 196      96.469   7.508  40.099  1.00 59.27           C  
-ATOM   8728  N   PRO D 197      91.689   6.007  38.406  1.00 45.34           N  
-ATOM   8729  CA  PRO D 197      90.771   5.491  37.385  1.00 44.83           C  
-ATOM   8730  C   PRO D 197      90.288   6.500  36.347  1.00 41.45           C  
-ATOM   8731  O   PRO D 197      90.520   6.329  35.139  1.00 36.15           O  
-ATOM   8732  CB  PRO D 197      89.631   4.913  38.219  1.00 44.32           C  
-ATOM   8733  CG  PRO D 197      90.368   4.327  39.361  1.00 43.68           C  
-ATOM   8734  CD  PRO D 197      91.338   5.437  39.723  1.00 41.02           C  
-ATOM   8735  N   PHE D 198      89.633   7.560  36.811  1.00 34.00           N  
-ATOM   8736  CA  PHE D 198      89.113   8.549  35.884  1.00 26.39           C  
-ATOM   8737  C   PHE D 198      90.204   9.334  35.184  1.00 24.12           C  
-ATOM   8738  O   PHE D 198      90.168   9.524  33.964  1.00 25.60           O  
-ATOM   8739  CB  PHE D 198      88.177   9.509  36.596  1.00 21.67           C  
-ATOM   8740  CG  PHE D 198      87.398  10.379  35.658  1.00 19.37           C  
-ATOM   8741  CD1 PHE D 198      86.462   9.819  34.796  1.00 19.58           C  
-ATOM   8742  CD2 PHE D 198      87.618  11.746  35.611  1.00 20.98           C  
-ATOM   8743  CE1 PHE D 198      85.761  10.604  33.905  1.00 15.89           C  
-ATOM   8744  CE2 PHE D 198      86.923  12.538  34.726  1.00 18.16           C  
-ATOM   8745  CZ  PHE D 198      85.993  11.965  33.870  1.00 21.58           C  
-ATOM   8746  N   VAL D 199      91.165   9.805  35.964  1.00 20.95           N  
-ATOM   8747  CA  VAL D 199      92.275  10.550  35.402  1.00 24.09           C  
-ATOM   8748  C   VAL D 199      92.999   9.698  34.356  1.00 22.85           C  
-ATOM   8749  O   VAL D 199      93.043  10.045  33.172  1.00 10.06           O  
-ATOM   8750  CB  VAL D 199      93.255  10.953  36.510  1.00 29.64           C  
-ATOM   8751  CG1 VAL D 199      94.594  11.371  35.908  1.00 34.00           C  
-ATOM   8752  CG2 VAL D 199      92.660  12.094  37.316  1.00 28.69           C  
-ATOM   8753  N   MET D 200      93.549   8.573  34.808  1.00 28.16           N  
-ATOM   8754  CA  MET D 200      94.273   7.649  33.941  1.00 27.65           C  
-ATOM   8755  C   MET D 200      93.548   7.487  32.606  1.00 21.46           C  
-ATOM   8756  O   MET D 200      94.174   7.449  31.542  1.00 23.73           O  
-ATOM   8757  CB  MET D 200      94.408   6.284  34.625  1.00 28.07           C  
-ATOM   8758  CG  MET D 200      95.740   5.604  34.358  1.00 35.13           C  
-ATOM   8759  SD  MET D 200      97.141   6.594  34.960  1.00 38.44           S  
-ATOM   8760  CE  MET D 200      97.186   6.099  36.732  1.00 24.59           C  
-ATOM   8761  N   VAL D 201      92.226   7.393  32.668  1.00 10.25           N  
-ATOM   8762  CA  VAL D 201      91.432   7.240  31.465  1.00  8.23           C  
-ATOM   8763  C   VAL D 201      91.405   8.532  30.667  1.00  5.20           C  
-ATOM   8764  O   VAL D 201      91.716   8.550  29.471  1.00  4.47           O  
-ATOM   8765  CB  VAL D 201      89.985   6.851  31.807  1.00 13.04           C  
-ATOM   8766  CG1 VAL D 201      89.104   6.993  30.585  1.00 11.97           C  
-ATOM   8767  CG2 VAL D 201      89.939   5.422  32.306  1.00 15.11           C  
-ATOM   8768  N   LEU D 202      91.032   9.613  31.340  1.00 10.17           N  
-ATOM   8769  CA  LEU D 202      90.940  10.909  30.686  1.00 16.24           C  
-ATOM   8770  C   LEU D 202      92.191  11.196  29.861  1.00 18.39           C  
-ATOM   8771  O   LEU D 202      92.098  11.563  28.685  1.00 20.34           O  
-ATOM   8772  CB  LEU D 202      90.708  12.014  31.724  1.00 15.50           C  
-ATOM   8773  CG  LEU D 202      90.237  13.364  31.167  1.00 19.98           C  
-ATOM   8774  CD1 LEU D 202      89.018  13.170  30.269  1.00 14.59           C  
-ATOM   8775  CD2 LEU D 202      89.903  14.302  32.324  1.00 26.02           C  
-ATOM   8776  N   ARG D 203      93.358  11.014  30.474  1.00 16.50           N  
-ATOM   8777  CA  ARG D 203      94.625  11.242  29.788  1.00 11.71           C  
-ATOM   8778  C   ARG D 203      94.633  10.382  28.530  1.00 20.36           C  
-ATOM   8779  O   ARG D 203      94.861  10.884  27.426  1.00 26.39           O  
-ATOM   8780  CB  ARG D 203      95.781  10.850  30.699  1.00  9.26           C  
-ATOM   8781  CG  ARG D 203      95.563  11.305  32.137  1.00 35.20           C  
-ATOM   8782  CD  ARG D 203      96.621  10.792  33.119  1.00 49.94           C  
-ATOM   8783  NE  ARG D 203      97.678  11.770  33.346  1.00 55.76           N  
-ATOM   8784  CZ  ARG D 203      98.735  11.928  32.559  1.00 62.23           C  
-ATOM   8785  NH1 ARG D 203      98.896  11.162  31.486  1.00 58.25           N  
-ATOM   8786  NH2 ARG D 203      99.622  12.874  32.836  1.00 72.47           N  
-ATOM   8787  N   ASN D 204      94.360   9.088  28.701  1.00 19.63           N  
-ATOM   8788  CA  ASN D 204      94.332   8.144  27.587  1.00 19.66           C  
-ATOM   8789  C   ASN D 204      93.401   8.594  26.474  1.00 21.47           C  
-ATOM   8790  O   ASN D 204      93.810   8.677  25.309  1.00 22.36           O  
-ATOM   8791  CB  ASN D 204      93.910   6.750  28.068  1.00 20.10           C  
-ATOM   8792  CG  ASN D 204      95.075   5.940  28.613  1.00 23.95           C  
-ATOM   8793  OD1 ASN D 204      94.985   5.316  29.680  1.00 25.55           O  
-ATOM   8794  ND2 ASN D 204      96.175   5.936  27.873  1.00 22.47           N  
-ATOM   8795  N   VAL D 205      92.153   8.891  26.824  1.00 16.51           N  
-ATOM   8796  CA  VAL D 205      91.198   9.314  25.808  1.00 17.81           C  
-ATOM   8797  C   VAL D 205      91.752  10.461  24.975  1.00 16.85           C  
-ATOM   8798  O   VAL D 205      91.815  10.358  23.749  1.00 22.69           O  
-ATOM   8799  CB  VAL D 205      89.845   9.730  26.428  1.00 14.80           C  
-ATOM   8800  CG1 VAL D 205      88.842  10.153  25.333  1.00  4.47           C  
-ATOM   8801  CG2 VAL D 205      89.288   8.571  27.216  1.00 13.43           C  
-ATOM   8802  N   TYR D 206      92.171  11.542  25.623  1.00  4.47           N  
-ATOM   8803  CA  TYR D 206      92.698  12.660  24.864  1.00 12.60           C  
-ATOM   8804  C   TYR D 206      93.766  12.221  23.888  1.00 16.46           C  
-ATOM   8805  O   TYR D 206      93.771  12.653  22.729  1.00 21.62           O  
-ATOM   8806  CB  TYR D 206      93.228  13.753  25.790  1.00 16.77           C  
-ATOM   8807  CG  TYR D 206      92.184  14.820  26.047  1.00 15.02           C  
-ATOM   8808  CD1 TYR D 206      91.720  15.626  25.008  1.00  9.53           C  
-ATOM   8809  CD2 TYR D 206      91.615  14.984  27.310  1.00 16.89           C  
-ATOM   8810  CE1 TYR D 206      90.710  16.573  25.222  1.00 22.35           C  
-ATOM   8811  CE2 TYR D 206      90.603  15.928  27.532  1.00 24.10           C  
-ATOM   8812  CZ  TYR D 206      90.155  16.723  26.486  1.00 23.63           C  
-ATOM   8813  OH  TYR D 206      89.176  17.673  26.709  1.00 22.24           O  
-ATOM   8814  N   ILE D 207      94.670  11.359  24.336  1.00 15.86           N  
-ATOM   8815  CA  ILE D 207      95.691  10.866  23.425  1.00 19.35           C  
-ATOM   8816  C   ILE D 207      95.017  10.237  22.195  1.00 22.02           C  
-ATOM   8817  O   ILE D 207      95.344  10.581  21.047  1.00 21.57           O  
-ATOM   8818  CB  ILE D 207      96.583   9.837  24.106  1.00 17.39           C  
-ATOM   8819  CG1 ILE D 207      97.585  10.571  24.995  1.00 18.77           C  
-ATOM   8820  CG2 ILE D 207      97.278   8.977  23.056  1.00 16.10           C  
-ATOM   8821  CD1 ILE D 207      98.382  11.643  24.234  1.00 18.36           C  
-ATOM   8822  N   MET D 208      94.080   9.320  22.436  1.00 15.11           N  
-ATOM   8823  CA  MET D 208      93.355   8.706  21.336  1.00 12.99           C  
-ATOM   8824  C   MET D 208      92.800   9.794  20.432  1.00 15.82           C  
-ATOM   8825  O   MET D 208      93.043   9.769  19.229  1.00 13.80           O  
-ATOM   8826  CB  MET D 208      92.196   7.853  21.843  1.00 18.92           C  
-ATOM   8827  CG  MET D 208      92.616   6.488  22.347  1.00 27.16           C  
-ATOM   8828  SD  MET D 208      91.231   5.523  22.990  1.00 22.56           S  
-ATOM   8829  CE  MET D 208      91.180   6.165  24.724  1.00 23.01           C  
-ATOM   8830  N   LEU D 209      92.068  10.749  21.016  1.00 21.42           N  
-ATOM   8831  CA  LEU D 209      91.470  11.836  20.238  1.00 25.58           C  
-ATOM   8832  C   LEU D 209      92.479  12.248  19.180  1.00 27.46           C  
-ATOM   8833  O   LEU D 209      92.205  12.161  17.970  1.00 26.78           O  
-ATOM   8834  CB  LEU D 209      91.133  13.051  21.117  1.00 18.15           C  
-ATOM   8835  CG  LEU D 209      90.041  14.020  20.610  1.00 16.18           C  
-ATOM   8836  CD1 LEU D 209      90.139  15.323  21.401  1.00 14.87           C  
-ATOM   8837  CD2 LEU D 209      90.192  14.318  19.118  1.00  5.57           C  
-ATOM   8838  N   ILE D 210      93.653  12.674  19.638  1.00 18.91           N  
-ATOM   8839  CA  ILE D 210      94.686  13.086  18.706  1.00 24.12           C  
-ATOM   8840  C   ILE D 210      94.934  11.998  17.647  1.00 20.69           C  
-ATOM   8841  O   ILE D 210      94.806  12.259  16.438  1.00 19.37           O  
-ATOM   8842  CB  ILE D 210      95.994  13.444  19.449  1.00 20.84           C  
-ATOM   8843  CG1 ILE D 210      95.764  14.692  20.308  1.00 16.49           C  
-ATOM   8844  CG2 ILE D 210      97.111  13.725  18.450  1.00 13.45           C  
-ATOM   8845  CD1 ILE D 210      96.995  15.166  21.041  1.00 17.22           C  
-ATOM   8846  N   ASN D 211      95.262  10.779  18.075  1.00 10.89           N  
-ATOM   8847  CA  ASN D 211      95.497   9.731  17.086  1.00 10.08           C  
-ATOM   8848  C   ASN D 211      94.334   9.631  16.115  1.00 13.06           C  
-ATOM   8849  O   ASN D 211      94.537   9.380  14.934  1.00 15.52           O  
-ATOM   8850  CB  ASN D 211      95.720   8.374  17.744  1.00  8.23           C  
-ATOM   8851  CG  ASN D 211      97.036   8.307  18.500  1.00 31.21           C  
-ATOM   8852  OD1 ASN D 211      98.025   8.919  18.096  1.00 44.87           O  
-ATOM   8853  ND2 ASN D 211      97.061   7.548  19.593  1.00 33.64           N  
-ATOM   8854  N   THR D 212      93.117   9.854  16.607  1.00 12.86           N  
-ATOM   8855  CA  THR D 212      91.919   9.776  15.767  1.00 12.69           C  
-ATOM   8856  C   THR D 212      91.889  10.852  14.687  1.00 15.73           C  
-ATOM   8857  O   THR D 212      91.521  10.597  13.531  1.00  7.05           O  
-ATOM   8858  CB  THR D 212      90.625   9.945  16.589  1.00  9.63           C  
-ATOM   8859  OG1 THR D 212      90.629   9.043  17.700  1.00 12.44           O  
-ATOM   8860  CG2 THR D 212      89.401   9.668  15.703  1.00  4.47           C  
-ATOM   8861  N   ILE D 213      92.250  12.069  15.075  1.00 15.12           N  
-ATOM   8862  CA  ILE D 213      92.242  13.167  14.126  1.00 17.11           C  
-ATOM   8863  C   ILE D 213      93.210  12.805  13.002  1.00 23.30           C  
-ATOM   8864  O   ILE D 213      92.815  12.772  11.834  1.00 19.82           O  
-ATOM   8865  CB  ILE D 213      92.665  14.509  14.794  1.00 16.34           C  
-ATOM   8866  CG1 ILE D 213      91.831  14.755  16.061  1.00 14.73           C  
-ATOM   8867  CG2 ILE D 213      92.466  15.658  13.815  1.00  4.47           C  
-ATOM   8868  CD1 ILE D 213      92.171  16.041  16.803  1.00  5.11           C  
-ATOM   8869  N   ILE D 214      94.462  12.505  13.360  1.00 20.50           N  
-ATOM   8870  CA  ILE D 214      95.476  12.149  12.367  1.00 14.91           C  
-ATOM   8871  C   ILE D 214      94.959  11.022  11.489  1.00  7.09           C  
-ATOM   8872  O   ILE D 214      94.910  11.125  10.271  1.00  4.47           O  
-ATOM   8873  CB  ILE D 214      96.768  11.664  13.028  1.00 13.32           C  
-ATOM   8874  CG1 ILE D 214      97.267  12.703  14.026  1.00 18.94           C  
-ATOM   8875  CG2 ILE D 214      97.826  11.417  11.959  1.00  5.37           C  
-ATOM   8876  CD1 ILE D 214      98.425  12.201  14.885  1.00 22.98           C  
-ATOM   8877  N   PHE D 215      94.580   9.938  12.142  1.00 13.23           N  
-ATOM   8878  CA  PHE D 215      94.053   8.765  11.468  1.00 14.88           C  
-ATOM   8879  C   PHE D 215      93.043   9.185  10.419  1.00 11.07           C  
-ATOM   8880  O   PHE D 215      93.168   8.855   9.243  1.00 12.17           O  
-ATOM   8881  CB  PHE D 215      93.387   7.845  12.504  1.00 14.12           C  
-ATOM   8882  CG  PHE D 215      92.771   6.603  11.919  1.00 22.02           C  
-ATOM   8883  CD1 PHE D 215      91.501   6.644  11.341  1.00 22.93           C  
-ATOM   8884  CD2 PHE D 215      93.473   5.394  11.918  1.00 25.80           C  
-ATOM   8885  CE1 PHE D 215      90.932   5.496  10.763  1.00 24.42           C  
-ATOM   8886  CE2 PHE D 215      92.917   4.243  11.345  1.00 32.37           C  
-ATOM   8887  CZ  PHE D 215      91.642   4.294  10.764  1.00 28.53           C  
-ATOM   8888  N   LEU D 216      92.043   9.927  10.871  1.00 15.96           N  
-ATOM   8889  CA  LEU D 216      90.964  10.408  10.018  1.00 22.00           C  
-ATOM   8890  C   LEU D 216      91.442  11.222   8.815  1.00 22.26           C  
-ATOM   8891  O   LEU D 216      90.737  11.325   7.810  1.00 16.72           O  
-ATOM   8892  CB  LEU D 216      90.001  11.254  10.864  1.00 19.97           C  
-ATOM   8893  CG  LEU D 216      88.602  10.732  11.196  1.00 15.09           C  
-ATOM   8894  CD1 LEU D 216      88.599   9.216  11.316  1.00 17.97           C  
-ATOM   8895  CD2 LEU D 216      88.143  11.384  12.492  1.00 12.76           C  
-ATOM   8896  N   LYS D 217      92.634  11.807   8.926  1.00 29.33           N  
-ATOM   8897  CA  LYS D 217      93.188  12.633   7.855  1.00 26.31           C  
-ATOM   8898  C   LYS D 217      93.404  11.849   6.591  1.00 27.75           C  
-ATOM   8899  O   LYS D 217      93.220  12.380   5.505  1.00 37.81           O  
-ATOM   8900  CB  LYS D 217      94.524  13.253   8.277  1.00 26.72           C  
-ATOM   8901  CG  LYS D 217      94.413  14.528   9.116  1.00 22.84           C  
-ATOM   8902  CD  LYS D 217      93.764  15.645   8.313  1.00 30.44           C  
-ATOM   8903  CE  LYS D 217      93.896  16.980   9.026  1.00 37.16           C  
-ATOM   8904  NZ  LYS D 217      93.356  16.927  10.419  1.00 39.53           N  
-ATOM   8905  N   THR D 218      93.785  10.583   6.739  1.00 36.29           N  
-ATOM   8906  CA  THR D 218      94.058   9.710   5.598  1.00 36.12           C  
-ATOM   8907  C   THR D 218      92.971   8.671   5.300  1.00 37.21           C  
-ATOM   8908  O   THR D 218      92.446   8.621   4.175  1.00 32.43           O  
-ATOM   8909  CB  THR D 218      95.377   8.957   5.805  1.00 36.94           C  
-ATOM   8910  OG1 THR D 218      96.357   9.857   6.340  1.00 33.41           O  
-ATOM   8911  CG2 THR D 218      95.876   8.392   4.483  1.00 42.45           C  
-ATOM   8912  N   ASN D 219      92.643   7.854   6.309  1.00 32.07           N  
-ATOM   8913  CA  ASN D 219      91.641   6.787   6.183  1.00 29.51           C  
-ATOM   8914  C   ASN D 219      90.241   7.123   6.705  1.00 32.53           C  
-ATOM   8915  O   ASN D 219      90.057   8.055   7.487  1.00 37.47           O  
-ATOM   8916  CB  ASN D 219      92.140   5.555   6.912  1.00 33.04           C  
-ATOM   8917  CG  ASN D 219      93.637   5.565   7.079  1.00 52.01           C  
-ATOM   8918  OD1 ASN D 219      94.383   5.513   6.099  1.00 60.90           O  
-ATOM   8919  ND2 ASN D 219      94.093   5.648   8.326  1.00 55.28           N  
-ATOM   8920  N   ASN D 220      89.258   6.344   6.267  1.00 34.56           N  
-ATOM   8921  CA  ASN D 220      87.862   6.515   6.670  1.00 40.27           C  
-ATOM   8922  C   ASN D 220      87.660   5.749   7.979  1.00 42.74           C  
-ATOM   8923  O   ASN D 220      88.432   4.840   8.278  1.00 52.89           O  
-ATOM   8924  CB  ASN D 220      86.954   5.939   5.582  1.00 53.59           C  
-ATOM   8925  CG  ASN D 220      85.479   6.095   5.902  1.00 66.01           C  
-ATOM   8926  OD1 ASN D 220      84.682   5.180   5.655  1.00 72.31           O  
-ATOM   8927  ND2 ASN D 220      85.102   7.260   6.438  1.00 65.30           N  
-ATOM   8928  N   TRP D 221      86.636   6.086   8.760  1.00 38.38           N  
-ATOM   8929  CA  TRP D 221      86.430   5.371  10.024  1.00 41.83           C  
-ATOM   8930  C   TRP D 221      86.202   3.879   9.807  1.00 45.74           C  
-ATOM   8931  O   TRP D 221      86.548   3.066  10.664  1.00 45.87           O  
-ATOM   8932  CB  TRP D 221      85.249   5.943  10.829  1.00 34.60           C  
-ATOM   8933  CG  TRP D 221      83.871   5.682  10.248  1.00 30.55           C  
-ATOM   8934  CD1 TRP D 221      83.218   6.438   9.315  1.00 35.41           C  
-ATOM   8935  CD2 TRP D 221      82.981   4.602  10.578  1.00 22.12           C  
-ATOM   8936  NE1 TRP D 221      81.977   5.900   9.047  1.00 29.34           N  
-ATOM   8937  CE2 TRP D 221      81.809   4.775   9.808  1.00 19.89           C  
-ATOM   8938  CE3 TRP D 221      83.061   3.509  11.450  1.00 23.13           C  
-ATOM   8939  CZ2 TRP D 221      80.728   3.898   9.883  1.00 22.53           C  
-ATOM   8940  CZ3 TRP D 221      81.980   2.633  11.525  1.00 16.79           C  
-ATOM   8941  CH2 TRP D 221      80.831   2.836  10.745  1.00 20.86           C  
-ATOM   8942  N   HIS D 222      85.632   3.522   8.659  1.00 49.74           N  
-ATOM   8943  CA  HIS D 222      85.353   2.122   8.357  1.00 57.65           C  
-ATOM   8944  C   HIS D 222      86.597   1.344   7.915  1.00 55.15           C  
-ATOM   8945  O   HIS D 222      86.496   0.407   7.117  1.00 58.75           O  
-ATOM   8946  CB  HIS D 222      84.273   2.016   7.267  1.00 66.96           C  
-ATOM   8947  CG  HIS D 222      83.358   0.842   7.440  1.00 79.98           C  
-ATOM   8948  ND1 HIS D 222      83.808  -0.404   7.829  1.00 82.88           N  
-ATOM   8949  CD2 HIS D 222      82.016   0.729   7.300  1.00 86.81           C  
-ATOM   8950  CE1 HIS D 222      82.781  -1.231   7.926  1.00 84.26           C  
-ATOM   8951  NE2 HIS D 222      81.682  -0.568   7.610  1.00 90.00           N  
-ATOM   8952  N   ALA D 223      87.764   1.727   8.428  1.00 47.75           N  
-ATOM   8953  CA  ALA D 223      89.001   1.039   8.070  1.00 44.61           C  
-ATOM   8954  C   ALA D 223      88.975  -0.383   8.632  1.00 47.65           C  
-ATOM   8955  O   ALA D 223      88.132  -1.208   8.250  1.00 46.43           O  
-ATOM   8956  CB  ALA D 223      90.204   1.798   8.618  1.00 34.86           C  
-ATOM   8957  N   GLY D 224      89.904  -0.668   9.538  1.00 49.55           N  
-ATOM   8958  CA  GLY D 224      89.956  -1.984  10.145  1.00 48.77           C  
-ATOM   8959  C   GLY D 224      88.860  -2.137  11.187  1.00 50.12           C  
-ATOM   8960  O   GLY D 224      89.080  -2.735  12.245  1.00 49.88           O  
-ATOM   8961  N   TRP D 225      87.679  -1.591  10.899  1.00 46.29           N  
-ATOM   8962  CA  TRP D 225      86.557  -1.683  11.824  1.00 36.76           C  
-ATOM   8963  C   TRP D 225      86.249  -3.145  12.094  1.00 40.20           C  
-ATOM   8964  O   TRP D 225      86.064  -3.551  13.234  1.00 46.79           O  
-ATOM   8965  CB  TRP D 225      85.325  -0.997  11.245  1.00 30.37           C  
-ATOM   8966  CG  TRP D 225      84.105  -1.094  12.125  1.00 31.93           C  
-ATOM   8967  CD1 TRP D 225      83.039  -1.935  11.963  1.00 40.88           C  
-ATOM   8968  CD2 TRP D 225      83.816  -0.305  13.288  1.00 27.57           C  
-ATOM   8969  NE1 TRP D 225      82.103  -1.716  12.950  1.00 38.81           N  
-ATOM   8970  CE2 TRP D 225      82.555  -0.722  13.777  1.00 29.60           C  
-ATOM   8971  CE3 TRP D 225      84.499   0.714  13.964  1.00 25.60           C  
-ATOM   8972  CZ2 TRP D 225      81.961  -0.153  14.912  1.00 26.42           C  
-ATOM   8973  CZ3 TRP D 225      83.908   1.282  15.096  1.00 29.42           C  
-ATOM   8974  CH2 TRP D 225      82.651   0.843  15.556  1.00 29.96           C  
-ATOM   8975  N   ASN D 226      86.212  -3.947  11.042  1.00 39.88           N  
-ATOM   8976  CA  ASN D 226      85.921  -5.359  11.211  1.00 39.77           C  
-ATOM   8977  C   ASN D 226      87.145  -6.103  11.732  1.00 37.12           C  
-ATOM   8978  O   ASN D 226      87.171  -7.334  11.753  1.00 41.46           O  
-ATOM   8979  CB  ASN D 226      85.437  -5.954   9.880  1.00 51.43           C  
-ATOM   8980  CG  ASN D 226      84.107  -5.343   9.412  1.00 61.90           C  
-ATOM   8981  OD1 ASN D 226      83.073  -5.473  10.083  1.00 61.04           O  
-ATOM   8982  ND2 ASN D 226      84.134  -4.669   8.259  1.00 62.81           N  
-ATOM   8983  N   THR D 227      88.158  -5.350  12.153  1.00 31.35           N  
-ATOM   8984  CA  THR D 227      89.379  -5.942  12.695  1.00 37.28           C  
-ATOM   8985  C   THR D 227      89.575  -5.371  14.092  1.00 33.71           C  
-ATOM   8986  O   THR D 227      90.541  -5.680  14.793  1.00 35.80           O  
-ATOM   8987  CB  THR D 227      90.607  -5.598  11.843  1.00 40.29           C  
-ATOM   8988  OG1 THR D 227      91.037  -4.264  12.138  1.00 46.39           O  
-ATOM   8989  CG2 THR D 227      90.264  -5.697  10.369  1.00 40.49           C  
-ATOM   8990  N   LEU D 228      88.631  -4.526  14.480  1.00 31.63           N  
-ATOM   8991  CA  LEU D 228      88.634  -3.886  15.789  1.00 27.29           C  
-ATOM   8992  C   LEU D 228      87.868  -4.737  16.774  1.00 22.02           C  
-ATOM   8993  O   LEU D 228      86.656  -4.904  16.638  1.00 22.62           O  
-ATOM   8994  CB  LEU D 228      87.943  -2.531  15.709  1.00 28.70           C  
-ATOM   8995  CG  LEU D 228      88.815  -1.296  15.866  1.00 31.59           C  
-ATOM   8996  CD1 LEU D 228      87.937  -0.059  15.728  1.00 35.71           C  
-ATOM   8997  CD2 LEU D 228      89.521  -1.337  17.228  1.00 33.97           C  
-ATOM   8998  N   SER D 229      88.550  -5.274  17.772  1.00 18.53           N  
-ATOM   8999  CA  SER D 229      87.835  -6.085  18.743  1.00 27.56           C  
-ATOM   9000  C   SER D 229      86.866  -5.154  19.446  1.00 25.03           C  
-ATOM   9001  O   SER D 229      87.159  -3.974  19.629  1.00 27.07           O  
-ATOM   9002  CB  SER D 229      88.801  -6.706  19.752  1.00 34.87           C  
-ATOM   9003  OG  SER D 229      89.599  -5.708  20.362  1.00 43.54           O  
-ATOM   9004  N   PHE D 230      85.701  -5.665  19.819  1.00 21.91           N  
-ATOM   9005  CA  PHE D 230      84.745  -4.818  20.504  1.00 20.76           C  
-ATOM   9006  C   PHE D 230      85.374  -4.276  21.773  1.00 20.36           C  
-ATOM   9007  O   PHE D 230      86.441  -4.720  22.183  1.00 26.46           O  
-ATOM   9008  CB  PHE D 230      83.485  -5.600  20.853  1.00 18.41           C  
-ATOM   9009  CG  PHE D 230      82.574  -5.800  19.698  1.00  8.36           C  
-ATOM   9010  CD1 PHE D 230      82.670  -6.931  18.908  1.00  8.04           C  
-ATOM   9011  CD2 PHE D 230      81.638  -4.833  19.378  1.00 15.64           C  
-ATOM   9012  CE1 PHE D 230      81.840  -7.101  17.808  1.00 14.96           C  
-ATOM   9013  CE2 PHE D 230      80.803  -4.988  18.278  1.00 24.83           C  
-ATOM   9014  CZ  PHE D 230      80.905  -6.129  17.490  1.00 15.21           C  
-ATOM   9015  N   CYS D 231      84.721  -3.305  22.391  1.00 19.39           N  
-ATOM   9016  CA  CYS D 231      85.246  -2.742  23.622  1.00 22.18           C  
-ATOM   9017  C   CYS D 231      84.801  -3.638  24.777  1.00 24.07           C  
-ATOM   9018  O   CYS D 231      83.605  -3.806  25.022  1.00 25.65           O  
-ATOM   9019  CB  CYS D 231      84.727  -1.318  23.816  1.00 22.02           C  
-ATOM   9020  SG  CYS D 231      85.412  -0.484  25.257  1.00 38.63           S  
-ATOM   9021  N   ASN D 232      85.771  -4.216  25.477  1.00 24.07           N  
-ATOM   9022  CA  ASN D 232      85.495  -5.110  26.596  1.00 29.57           C  
-ATOM   9023  C   ASN D 232      86.014  -4.564  27.935  1.00 32.04           C  
-ATOM   9024  O   ASN D 232      86.743  -3.575  27.977  1.00 40.73           O  
-ATOM   9025  CB  ASN D 232      86.149  -6.446  26.316  1.00 37.75           C  
-ATOM   9026  CG  ASN D 232      87.638  -6.307  26.123  1.00 47.09           C  
-ATOM   9027  OD1 ASN D 232      88.357  -5.933  27.049  1.00 53.27           O  
-ATOM   9028  ND2 ASN D 232      88.111  -6.584  24.914  1.00 51.62           N  
-ATOM   9029  N   ASP D 233      85.650  -5.225  29.028  1.00 31.03           N  
-ATOM   9030  CA  ASP D 233      86.074  -4.785  30.355  1.00 33.36           C  
-ATOM   9031  C   ASP D 233      87.570  -4.895  30.537  1.00 25.45           C  
-ATOM   9032  O   ASP D 233      88.155  -4.172  31.330  1.00 27.40           O  
-ATOM   9033  CB  ASP D 233      85.377  -5.599  31.447  1.00 47.31           C  
-ATOM   9034  CG  ASP D 233      83.867  -5.430  31.425  1.00 60.28           C  
-ATOM   9035  OD1 ASP D 233      83.229  -5.825  30.424  1.00 67.95           O  
-ATOM   9036  OD2 ASP D 233      83.318  -4.898  32.412  1.00 66.77           O  
-ATOM   9037  N   VAL D 234      88.188  -5.811  29.808  1.00 23.50           N  
-ATOM   9038  CA  VAL D 234      89.627  -5.986  29.906  1.00 30.84           C  
-ATOM   9039  C   VAL D 234      90.279  -4.731  29.374  1.00 29.91           C  
-ATOM   9040  O   VAL D 234      91.222  -4.205  29.963  1.00 35.54           O  
-ATOM   9041  CB  VAL D 234      90.116  -7.171  29.057  1.00 38.73           C  
-ATOM   9042  CG1 VAL D 234      91.636  -7.341  29.218  1.00 32.38           C  
-ATOM   9043  CG2 VAL D 234      89.351  -8.443  29.451  1.00 44.44           C  
-ATOM   9044  N   PHE D 235      89.767  -4.264  28.244  1.00 23.46           N  
-ATOM   9045  CA  PHE D 235      90.281  -3.066  27.614  1.00 23.78           C  
-ATOM   9046  C   PHE D 235      90.142  -1.912  28.606  1.00 27.27           C  
-ATOM   9047  O   PHE D 235      91.123  -1.244  28.939  1.00 31.14           O  
-ATOM   9048  CB  PHE D 235      89.478  -2.769  26.343  1.00 30.64           C  
-ATOM   9049  CG  PHE D 235      89.957  -1.560  25.579  1.00 35.41           C  
-ATOM   9050  CD1 PHE D 235      89.080  -0.846  24.764  1.00 35.04           C  
-ATOM   9051  CD2 PHE D 235      91.286  -1.145  25.656  1.00 37.34           C  
-ATOM   9052  CE1 PHE D 235      89.519   0.258  24.042  1.00 35.61           C  
-ATOM   9053  CE2 PHE D 235      91.736  -0.042  24.936  1.00 29.47           C  
-ATOM   9054  CZ  PHE D 235      90.851   0.659  24.129  1.00 35.53           C  
-ATOM   9055  N   LYS D 236      88.921  -1.692  29.086  1.00 24.62           N  
-ATOM   9056  CA  LYS D 236      88.652  -0.612  30.028  1.00 21.26           C  
-ATOM   9057  C   LYS D 236      89.591  -0.664  31.221  1.00 20.28           C  
-ATOM   9058  O   LYS D 236      90.022   0.373  31.724  1.00 15.92           O  
-ATOM   9059  CB  LYS D 236      87.206  -0.682  30.510  1.00 18.96           C  
-ATOM   9060  CG  LYS D 236      86.165  -0.525  29.404  1.00 23.91           C  
-ATOM   9061  CD  LYS D 236      84.766  -0.467  30.014  1.00 35.18           C  
-ATOM   9062  CE  LYS D 236      83.658  -0.493  28.965  1.00 38.99           C  
-ATOM   9063  NZ  LYS D 236      82.309  -0.540  29.627  1.00 37.47           N  
-ATOM   9064  N   GLN D 237      89.903  -1.877  31.664  1.00 24.31           N  
-ATOM   9065  CA  GLN D 237      90.801  -2.072  32.792  1.00 32.94           C  
-ATOM   9066  C   GLN D 237      92.172  -1.460  32.535  1.00 33.02           C  
-ATOM   9067  O   GLN D 237      92.703  -0.754  33.388  1.00 38.32           O  
-ATOM   9068  CB  GLN D 237      90.962  -3.563  33.109  1.00 44.56           C  
-ATOM   9069  CG  GLN D 237      89.790  -4.173  33.857  1.00 52.06           C  
-ATOM   9070  CD  GLN D 237      89.508  -3.453  35.156  1.00 58.48           C  
-ATOM   9071  OE1 GLN D 237      90.385  -3.330  36.017  1.00 57.03           O  
-ATOM   9072  NE2 GLN D 237      88.278  -2.966  35.305  1.00 65.37           N  
-ATOM   9073  N   LYS D 238      92.753  -1.731  31.373  1.00 30.97           N  
-ATOM   9074  CA  LYS D 238      94.062  -1.173  31.064  1.00 36.47           C  
-ATOM   9075  C   LYS D 238      93.987   0.349  31.068  1.00 37.29           C  
-ATOM   9076  O   LYS D 238      94.852   1.028  31.627  1.00 44.35           O  
-ATOM   9077  CB  LYS D 238      94.553  -1.645  29.692  1.00 45.60           C  
-ATOM   9078  CG  LYS D 238      94.890  -3.130  29.594  1.00 59.80           C  
-ATOM   9079  CD  LYS D 238      95.401  -3.476  28.192  1.00 70.30           C  
-ATOM   9080  CE  LYS D 238      95.592  -4.984  27.989  1.00 73.90           C  
-ATOM   9081  NZ  LYS D 238      95.991  -5.332  26.582  1.00 70.23           N  
-ATOM   9082  N   LEU D 239      92.943   0.883  30.446  1.00 29.84           N  
-ATOM   9083  CA  LEU D 239      92.768   2.322  30.364  1.00 22.68           C  
-ATOM   9084  C   LEU D 239      92.706   3.028  31.718  1.00 27.46           C  
-ATOM   9085  O   LEU D 239      92.964   4.228  31.795  1.00 33.25           O  
-ATOM   9086  CB  LEU D 239      91.517   2.639  29.550  1.00 15.27           C  
-ATOM   9087  CG  LEU D 239      91.598   2.240  28.075  1.00 13.89           C  
-ATOM   9088  CD1 LEU D 239      90.299   2.579  27.360  1.00 22.33           C  
-ATOM   9089  CD2 LEU D 239      92.743   2.972  27.426  1.00  6.46           C  
-ATOM   9090  N   GLN D 240      92.372   2.293  32.778  1.00 25.66           N  
-ATOM   9091  CA  GLN D 240      92.283   2.866  34.123  1.00 26.22           C  
-ATOM   9092  C   GLN D 240      93.560   2.676  34.925  1.00 32.64           C  
-ATOM   9093  O   GLN D 240      93.689   3.208  36.025  1.00 35.78           O  
-ATOM   9094  CB  GLN D 240      91.134   2.226  34.905  1.00 21.97           C  
-ATOM   9095  CG  GLN D 240      89.751   2.580  34.388  1.00 38.34           C  
-ATOM   9096  CD  GLN D 240      88.635   1.718  34.985  1.00 43.57           C  
-ATOM   9097  OE1 GLN D 240      88.446   1.658  36.212  1.00 40.04           O  
-ATOM   9098  NE2 GLN D 240      87.885   1.047  34.109  1.00 38.89           N  
-ATOM   9099  N   LYS D 241      94.510   1.932  34.372  1.00 39.86           N  
-ATOM   9100  CA  LYS D 241      95.746   1.649  35.091  1.00 44.01           C  
-ATOM   9101  C   LYS D 241      97.080   2.074  34.481  1.00 48.89           C  
-ATOM   9102  O   LYS D 241      97.867   2.751  35.138  1.00 50.91           O  
-ATOM   9103  CB  LYS D 241      95.831   0.149  35.390  1.00 46.33           C  
-ATOM   9104  CG  LYS D 241      94.763  -0.387  36.332  1.00 56.46           C  
-ATOM   9105  CD  LYS D 241      94.911  -1.901  36.533  1.00 65.96           C  
-ATOM   9106  CE  LYS D 241      93.898  -2.448  37.541  1.00 68.53           C  
-ATOM   9107  NZ  LYS D 241      94.073  -1.868  38.906  1.00 68.44           N  
-ATOM   9108  N   SER D 242      97.343   1.683  33.238  1.00 51.32           N  
-ATOM   9109  CA  SER D 242      98.637   1.980  32.637  1.00 58.96           C  
-ATOM   9110  C   SER D 242      98.859   3.191  31.737  1.00 62.12           C  
-ATOM   9111  O   SER D 242     100.007   3.462  31.372  1.00 69.70           O  
-ATOM   9112  CB  SER D 242      99.152   0.733  31.903  1.00 66.39           C  
-ATOM   9113  OG  SER D 242      98.239   0.292  30.911  1.00 70.81           O  
-ATOM   9114  N   GLU D 243      97.821   3.935  31.376  1.00 59.97           N  
-ATOM   9115  CA  GLU D 243      98.062   5.082  30.495  1.00 61.46           C  
-ATOM   9116  C   GLU D 243      98.769   4.517  29.262  1.00 52.19           C  
-ATOM   9117  O   GLU D 243      99.749   5.079  28.768  1.00 43.09           O  
-ATOM   9118  CB  GLU D 243      98.983   6.114  31.175  1.00 71.65           C  
-ATOM   9119  CG  GLU D 243      99.336   7.334  30.306  1.00 81.78           C  
-ATOM   9120  CD  GLU D 243     100.653   7.997  30.705  1.00 89.02           C  
-ATOM   9121  OE1 GLU D 243     100.809   8.374  31.891  1.00 91.15           O  
-ATOM   9122  OE2 GLU D 243     101.532   8.146  29.825  1.00 88.14           O  
-ATOM   9123  N   CYS D 244      98.281   3.376  28.796  1.00 49.48           N  
-ATOM   9124  CA  CYS D 244      98.852   2.725  27.630  1.00 52.07           C  
-ATOM   9125  C   CYS D 244      98.792   3.616  26.395  1.00 52.25           C  
-ATOM   9126  O   CYS D 244      99.751   4.334  26.111  1.00 61.73           O  
-ATOM   9127  CB  CYS D 244      98.129   1.405  27.366  1.00 57.14           C  
-ATOM   9128  SG  CYS D 244      96.363   1.449  27.728  1.00 69.48           S  
-ATOM   9129  N   ILE D 245      97.671   3.569  25.674  1.00 44.73           N  
-ATOM   9130  CA  ILE D 245      97.463   4.363  24.456  1.00 38.35           C  
-ATOM   9131  C   ILE D 245      98.583   5.349  24.165  1.00 35.47           C  
-ATOM   9132  O   ILE D 245      98.618   6.440  24.735  1.00 33.86           O  
-ATOM   9133  CB  ILE D 245      96.154   5.162  24.531  1.00 37.77           C  
-ATOM   9134  CG1 ILE D 245      94.995   4.228  24.873  1.00 36.07           C  
-ATOM   9135  CG2 ILE D 245      95.885   5.847  23.191  1.00 42.83           C  
-ATOM   9136  CD1 ILE D 245      94.793   3.116  23.866  1.00 29.48           C  
-ATOM   9137  N   LYS D 246      99.498   4.974  23.278  1.00 36.30           N  
-ATOM   9138  CA  LYS D 246     100.610   5.860  22.962  1.00 43.81           C  
-ATOM   9139  C   LYS D 246     100.430   6.637  21.667  1.00 44.79           C  
-ATOM   9140  O   LYS D 246      99.975   6.106  20.646  1.00 48.62           O  
-ATOM   9141  CB  LYS D 246     101.927   5.079  22.942  1.00 46.97           C  
-ATOM   9142  CG  LYS D 246     102.477   4.801  24.337  1.00 50.30           C  
-ATOM   9143  CD  LYS D 246     103.707   3.905  24.304  1.00 60.49           C  
-ATOM   9144  CE  LYS D 246     104.161   3.569  25.711  1.00 69.53           C  
-ATOM   9145  NZ  LYS D 246     105.190   2.488  25.722  1.00 74.71           N  
-ATOM   9146  N   LEU D 247     100.774   7.917  21.738  1.00 38.75           N  
-ATOM   9147  CA  LEU D 247     100.664   8.815  20.604  1.00 38.36           C  
-ATOM   9148  C   LEU D 247     101.666   8.341  19.550  1.00 38.14           C  
-ATOM   9149  O   LEU D 247     102.858   8.184  19.842  1.00 38.92           O  
-ATOM   9150  CB  LEU D 247     100.983  10.235  21.081  1.00 41.72           C  
-ATOM   9151  CG  LEU D 247     100.539  11.440  20.248  1.00 45.63           C  
-ATOM   9152  CD1 LEU D 247     100.807  12.708  21.060  1.00 42.17           C  
-ATOM   9153  CD2 LEU D 247     101.273  11.471  18.898  1.00 43.34           C  
-ATOM   9154  N   ARG D 248     101.199   8.101  18.328  1.00 36.70           N  
-ATOM   9155  CA  ARG D 248     102.118   7.624  17.305  1.00 46.14           C  
-ATOM   9156  C   ARG D 248     102.022   8.199  15.893  1.00 50.02           C  
-ATOM   9157  O   ARG D 248     100.933   8.439  15.367  1.00 47.60           O  
-ATOM   9158  CB  ARG D 248     102.056   6.099  17.241  1.00 50.67           C  
-ATOM   9159  CG  ARG D 248     100.661   5.519  17.290  1.00 49.45           C  
-ATOM   9160  CD  ARG D 248     100.744   4.002  17.320  1.00 58.81           C  
-ATOM   9161  NE  ARG D 248     101.539   3.517  18.451  1.00 63.74           N  
-ATOM   9162  CZ  ARG D 248     101.877   2.243  18.639  1.00 72.22           C  
-ATOM   9163  NH1 ARG D 248     101.492   1.312  17.767  1.00 75.75           N  
-ATOM   9164  NH2 ARG D 248     102.601   1.896  19.698  1.00 70.99           N  
-ATOM   9165  N   GLU D 249     103.204   8.385  15.299  1.00 53.41           N  
-ATOM   9166  CA  GLU D 249     103.402   8.936  13.955  1.00 56.06           C  
-ATOM   9167  C   GLU D 249     102.283   8.625  12.982  1.00 54.84           C  
-ATOM   9168  O   GLU D 249     101.618   9.533  12.481  1.00 56.17           O  
-ATOM   9169  CB  GLU D 249     104.732   8.435  13.389  1.00 66.14           C  
-ATOM   9170  CG  GLU D 249     105.958   8.869  14.200  1.00 83.00           C  
-ATOM   9171  CD  GLU D 249     106.313  10.348  14.020  1.00 93.96           C  
-ATOM   9172  OE1 GLU D 249     105.469  11.223  14.331  1.00 98.88           O  
-ATOM   9173  OE2 GLU D 249     107.447  10.633  13.567  1.00 93.91           O  
-ATOM   9174  N   VAL D 250     102.103   7.346  12.681  1.00 57.53           N  
-ATOM   9175  CA  VAL D 250     101.022   6.939  11.798  1.00 59.04           C  
-ATOM   9176  C   VAL D 250     100.117   6.030  12.601  1.00 57.21           C  
-ATOM   9177  O   VAL D 250     100.403   4.845  12.806  1.00 58.12           O  
-ATOM   9178  CB  VAL D 250     101.516   6.207  10.545  1.00 59.39           C  
-ATOM   9179  CG1 VAL D 250     100.343   5.506   9.863  1.00 60.17           C  
-ATOM   9180  CG2 VAL D 250     102.129   7.211   9.579  1.00 60.19           C  
-ATOM   9181  N   PRO D 251      99.007   6.595  13.085  1.00 53.32           N  
-ATOM   9182  CA  PRO D 251      98.004   5.910  13.886  1.00 48.95           C  
-ATOM   9183  C   PRO D 251      97.210   4.872  13.096  1.00 44.12           C  
-ATOM   9184  O   PRO D 251      96.976   5.024  11.889  1.00 34.88           O  
-ATOM   9185  CB  PRO D 251      97.138   7.061  14.383  1.00 52.98           C  
-ATOM   9186  CG  PRO D 251      97.138   7.976  13.204  1.00 54.69           C  
-ATOM   9187  CD  PRO D 251      98.595   7.986  12.821  1.00 55.41           C  
-ATOM   9188  N   GLY D 252      96.817   3.814  13.803  1.00 39.74           N  
-ATOM   9189  CA  GLY D 252      96.033   2.744  13.217  1.00 37.01           C  
-ATOM   9190  C   GLY D 252      94.700   2.717  13.935  1.00 32.81           C  
-ATOM   9191  O   GLY D 252      94.598   3.205  15.061  1.00 36.78           O  
-ATOM   9192  N   ILE D 253      93.683   2.141  13.306  1.00 22.45           N  
-ATOM   9193  CA  ILE D 253      92.356   2.100  13.900  1.00 16.56           C  
-ATOM   9194  C   ILE D 253      92.334   1.837  15.411  1.00 23.59           C  
-ATOM   9195  O   ILE D 253      91.561   2.461  16.135  1.00 27.45           O  
-ATOM   9196  CB  ILE D 253      91.470   1.054  13.179  1.00 16.32           C  
-ATOM   9197  CG1 ILE D 253      90.143   1.695  12.765  1.00 15.69           C  
-ATOM   9198  CG2 ILE D 253      91.212  -0.148  14.079  1.00 18.79           C  
-ATOM   9199  CD1 ILE D 253      89.366   2.309  13.914  1.00 11.50           C  
-ATOM   9200  N   GLU D 254      93.188   0.937  15.893  1.00 25.44           N  
-ATOM   9201  CA  GLU D 254      93.208   0.602  17.319  1.00 29.63           C  
-ATOM   9202  C   GLU D 254      93.873   1.617  18.248  1.00 27.08           C  
-ATOM   9203  O   GLU D 254      93.888   1.441  19.476  1.00 21.83           O  
-ATOM   9204  CB  GLU D 254      93.860  -0.772  17.542  1.00 38.58           C  
-ATOM   9205  CG  GLU D 254      95.253  -0.936  16.941  1.00 47.38           C  
-ATOM   9206  CD  GLU D 254      95.217  -1.390  15.491  1.00 59.74           C  
-ATOM   9207  OE1 GLU D 254      94.668  -2.486  15.218  1.00 65.50           O  
-ATOM   9208  OE2 GLU D 254      95.741  -0.652  14.628  1.00 62.99           O  
-ATOM   9209  N   ASP D 255      94.426   2.677  17.680  1.00 23.92           N  
-ATOM   9210  CA  ASP D 255      95.081   3.678  18.510  1.00 29.16           C  
-ATOM   9211  C   ASP D 255      94.184   4.885  18.636  1.00 27.57           C  
-ATOM   9212  O   ASP D 255      94.543   5.863  19.291  1.00 28.66           O  
-ATOM   9213  CB  ASP D 255      96.418   4.094  17.894  1.00 43.29           C  
-ATOM   9214  CG  ASP D 255      97.398   2.934  17.784  1.00 56.91           C  
-ATOM   9215  OD1 ASP D 255      97.746   2.358  18.845  1.00 57.71           O  
-ATOM   9216  OD2 ASP D 255      97.817   2.602  16.643  1.00 52.83           O  
-ATOM   9217  N   THR D 256      93.007   4.793  18.019  1.00 25.14           N  
-ATOM   9218  CA  THR D 256      92.030   5.878  18.019  1.00 23.48           C  
-ATOM   9219  C   THR D 256      90.916   5.775  19.053  1.00 22.59           C  
-ATOM   9220  O   THR D 256      91.016   5.067  20.051  1.00 24.89           O  
-ATOM   9221  CB  THR D 256      91.335   5.979  16.673  1.00 21.73           C  
-ATOM   9222  OG1 THR D 256      90.379   4.917  16.566  1.00 14.83           O  
-ATOM   9223  CG2 THR D 256      92.353   5.889  15.542  1.00 30.55           C  
-ATOM   9224  N   LEU D 257      89.847   6.515  18.783  1.00 29.16           N  
-ATOM   9225  CA  LEU D 257      88.670   6.552  19.641  1.00 26.00           C  
-ATOM   9226  C   LEU D 257      87.683   5.541  19.111  1.00 14.68           C  
-ATOM   9227  O   LEU D 257      86.752   5.137  19.807  1.00 17.75           O  
-ATOM   9228  CB  LEU D 257      88.022   7.943  19.623  1.00 23.57           C  
-ATOM   9229  CG  LEU D 257      88.724   9.084  20.360  1.00 18.65           C  
-ATOM   9230  CD1 LEU D 257      87.928  10.368  20.157  1.00 13.43           C  
-ATOM   9231  CD2 LEU D 257      88.846   8.740  21.850  1.00 14.86           C  
-ATOM   9232  N   PHE D 258      87.876   5.147  17.864  1.00  4.47           N  
-ATOM   9233  CA  PHE D 258      86.989   4.169  17.285  1.00  7.46           C  
-ATOM   9234  C   PHE D 258      87.150   2.844  18.029  1.00 12.81           C  
-ATOM   9235  O   PHE D 258      86.275   1.975  18.003  1.00  9.36           O  
-ATOM   9236  CB  PHE D 258      87.299   4.030  15.803  1.00 12.70           C  
-ATOM   9237  CG  PHE D 258      86.860   5.213  15.001  1.00 20.32           C  
-ATOM   9238  CD1 PHE D 258      85.500   5.470  14.805  1.00 20.24           C  
-ATOM   9239  CD2 PHE D 258      87.793   6.105  14.485  1.00 28.83           C  
-ATOM   9240  CE1 PHE D 258      85.072   6.601  14.110  1.00 14.65           C  
-ATOM   9241  CE2 PHE D 258      87.378   7.250  13.783  1.00 30.47           C  
-ATOM   9242  CZ  PHE D 258      86.016   7.498  13.597  1.00 21.92           C  
-ATOM   9243  N   ALA D 259      88.277   2.703  18.711  1.00 19.16           N  
-ATOM   9244  CA  ALA D 259      88.547   1.500  19.485  1.00 22.22           C  
-ATOM   9245  C   ALA D 259      87.566   1.460  20.650  1.00 21.97           C  
-ATOM   9246  O   ALA D 259      87.226   0.395  21.159  1.00 30.47           O  
-ATOM   9247  CB  ALA D 259      89.984   1.533  20.015  1.00 24.33           C  
-ATOM   9248  N   VAL D 260      87.124   2.641  21.064  1.00 20.22           N  
-ATOM   9249  CA  VAL D 260      86.198   2.788  22.178  1.00 23.85           C  
-ATOM   9250  C   VAL D 260      84.744   2.912  21.692  1.00 22.98           C  
-ATOM   9251  O   VAL D 260      83.798   2.773  22.466  1.00 26.66           O  
-ATOM   9252  CB  VAL D 260      86.589   4.038  23.038  1.00 21.47           C  
-ATOM   9253  CG1 VAL D 260      85.522   4.330  24.077  1.00 29.03           C  
-ATOM   9254  CG2 VAL D 260      87.906   3.793  23.741  1.00 17.69           C  
-ATOM   9255  N   LEU D 261      84.556   3.152  20.407  1.00 19.30           N  
-ATOM   9256  CA  LEU D 261      83.204   3.292  19.899  1.00 22.61           C  
-ATOM   9257  C   LEU D 261      82.591   1.999  19.372  1.00 31.57           C  
-ATOM   9258  O   LEU D 261      81.378   1.930  19.163  1.00 38.09           O  
-ATOM   9259  CB  LEU D 261      83.167   4.382  18.829  1.00 14.97           C  
-ATOM   9260  CG  LEU D 261      83.304   5.730  19.533  1.00 12.84           C  
-ATOM   9261  CD1 LEU D 261      83.417   6.855  18.522  1.00 17.49           C  
-ATOM   9262  CD2 LEU D 261      82.096   5.929  20.436  1.00  8.87           C  
-ATOM   9263  N   LYS D 262      83.424   0.982  19.153  1.00 28.79           N  
-ATOM   9264  CA  LYS D 262      82.953  -0.315  18.667  1.00 19.83           C  
-ATOM   9265  C   LYS D 262      82.227  -0.964  19.842  1.00 16.19           C  
-ATOM   9266  O   LYS D 262      82.798  -1.762  20.582  1.00 17.31           O  
-ATOM   9267  CB  LYS D 262      84.150  -1.174  18.232  1.00 27.39           C  
-ATOM   9268  CG  LYS D 262      83.824  -2.628  17.905  1.00 32.06           C  
-ATOM   9269  CD  LYS D 262      83.140  -2.752  16.559  1.00 38.58           C  
-ATOM   9270  CE  LYS D 262      84.094  -3.283  15.506  1.00 38.40           C  
-ATOM   9271  NZ  LYS D 262      84.385  -4.737  15.694  1.00 39.69           N  
-ATOM   9272  N   LEU D 263      80.962  -0.615  20.016  1.00 17.97           N  
-ATOM   9273  CA  LEU D 263      80.185  -1.145  21.128  1.00 17.72           C  
-ATOM   9274  C   LEU D 263      78.987  -1.985  20.695  1.00 13.66           C  
-ATOM   9275  O   LEU D 263      78.236  -1.615  19.794  1.00 17.73           O  
-ATOM   9276  CB  LEU D 263      79.696   0.010  22.010  1.00 17.97           C  
-ATOM   9277  CG  LEU D 263      80.749   0.982  22.545  1.00 14.43           C  
-ATOM   9278  CD1 LEU D 263      80.074   2.033  23.406  1.00 13.59           C  
-ATOM   9279  CD2 LEU D 263      81.776   0.222  23.364  1.00 17.49           C  
-ATOM   9280  N   PRO D 264      78.788  -3.128  21.350  1.00  6.22           N  
-ATOM   9281  CA  PRO D 264      77.683  -4.054  21.072  1.00  7.72           C  
-ATOM   9282  C   PRO D 264      76.336  -3.337  21.100  1.00 11.36           C  
-ATOM   9283  O   PRO D 264      75.410  -3.673  20.365  1.00 14.94           O  
-ATOM   9284  CB  PRO D 264      77.784  -5.052  22.208  1.00  7.62           C  
-ATOM   9285  CG  PRO D 264      79.253  -5.053  22.508  1.00 16.03           C  
-ATOM   9286  CD  PRO D 264      79.621  -3.609  22.458  1.00  6.01           C  
-ATOM   9287  N   GLU D 265      76.239  -2.349  21.974  1.00 10.95           N  
-ATOM   9288  CA  GLU D 265      75.022  -1.574  22.125  1.00 19.30           C  
-ATOM   9289  C   GLU D 265      74.730  -0.714  20.892  1.00 22.88           C  
-ATOM   9290  O   GLU D 265      73.640  -0.148  20.760  1.00 35.53           O  
-ATOM   9291  CB  GLU D 265      75.120  -0.678  23.371  1.00 14.57           C  
-ATOM   9292  CG  GLU D 265      75.406  -1.436  24.667  1.00 27.63           C  
-ATOM   9293  CD  GLU D 265      76.904  -1.588  24.978  1.00 43.99           C  
-ATOM   9294  OE1 GLU D 265      77.694  -1.856  24.041  1.00 46.53           O  
-ATOM   9295  OE2 GLU D 265      77.293  -1.455  26.169  1.00 50.29           O  
-ATOM   9296  N   LEU D 266      75.695  -0.605  19.988  1.00 14.00           N  
-ATOM   9297  CA  LEU D 266      75.487   0.206  18.790  1.00 24.61           C  
-ATOM   9298  C   LEU D 266      75.392  -0.665  17.548  1.00 30.94           C  
-ATOM   9299  O   LEU D 266      75.062  -0.175  16.461  1.00 31.50           O  
-ATOM   9300  CB  LEU D 266      76.635   1.199  18.602  1.00 21.16           C  
-ATOM   9301  CG  LEU D 266      76.848   2.230  19.703  1.00 18.36           C  
-ATOM   9302  CD1 LEU D 266      78.170   2.940  19.484  1.00 13.31           C  
-ATOM   9303  CD2 LEU D 266      75.688   3.203  19.703  1.00 15.21           C  
-ATOM   9304  N   CYS D 267      75.695  -1.952  17.711  1.00 28.01           N  
-ATOM   9305  CA  CYS D 267      75.656  -2.889  16.601  1.00 25.38           C  
-ATOM   9306  C   CYS D 267      74.440  -3.784  16.708  1.00 29.71           C  
-ATOM   9307  O   CYS D 267      73.806  -3.873  17.767  1.00 28.07           O  
-ATOM   9308  CB  CYS D 267      76.914  -3.752  16.588  1.00 26.78           C  
-ATOM   9309  SG  CYS D 267      78.456  -2.835  16.547  1.00 27.72           S  
-ATOM   9310  N   GLY D 268      74.122  -4.448  15.601  1.00 40.31           N  
-ATOM   9311  CA  GLY D 268      72.977  -5.339  15.570  1.00 51.93           C  
-ATOM   9312  C   GLY D 268      73.327  -6.792  15.826  1.00 53.45           C  
-ATOM   9313  O   GLY D 268      74.429  -7.120  16.282  1.00 49.60           O  
-ATOM   9314  N   GLU D 269      72.366  -7.662  15.531  1.00 61.52           N  
-ATOM   9315  CA  GLU D 269      72.521  -9.101  15.710  1.00 70.34           C  
-ATOM   9316  C   GLU D 269      73.837  -9.598  15.100  1.00 72.92           C  
-ATOM   9317  O   GLU D 269      74.717 -10.110  15.809  1.00 72.98           O  
-ATOM   9318  CB  GLU D 269      71.339  -9.822  15.047  1.00 73.13           C  
-ATOM   9319  CG  GLU D 269      71.306 -11.337  15.225  1.00 79.66           C  
-ATOM   9320  CD  GLU D 269      70.224 -11.997  14.376  1.00 85.14           C  
-ATOM   9321  OE1 GLU D 269      69.054 -11.547  14.436  1.00 83.11           O  
-ATOM   9322  OE2 GLU D 269      70.544 -12.969  13.654  1.00 88.73           O  
-ATOM   9323  N   PHE D 270      73.961  -9.426  13.783  1.00 72.36           N  
-ATOM   9324  CA  PHE D 270      75.135  -9.865  13.027  1.00 72.65           C  
-ATOM   9325  C   PHE D 270      76.427  -9.167  13.446  1.00 66.30           C  
-ATOM   9326  O   PHE D 270      77.519  -9.580  13.054  1.00 64.91           O  
-ATOM   9327  CB  PHE D 270      74.905  -9.644  11.523  1.00 82.88           C  
-ATOM   9328  CG  PHE D 270      73.606 -10.220  11.006  1.00 94.56           C  
-ATOM   9329  CD1 PHE D 270      73.067  -9.768   9.800  1.00 98.50           C  
-ATOM   9330  CD2 PHE D 270      72.910 -11.194  11.730  1.00 96.16           C  
-ATOM   9331  CE1 PHE D 270      71.852 -10.269   9.324  1.00101.94           C  
-ATOM   9332  CE2 PHE D 270      71.695 -11.702  11.262  1.00 98.26           C  
-ATOM   9333  CZ  PHE D 270      71.164 -11.238  10.058  1.00101.35           C  
-ATOM   9334  N   GLY D 271      76.308  -8.105  14.232  1.00 58.81           N  
-ATOM   9335  CA  GLY D 271      77.503  -7.414  14.667  1.00 59.90           C  
-ATOM   9336  C   GLY D 271      77.911  -6.265  13.763  1.00 61.35           C  
-ATOM   9337  O   GLY D 271      79.099  -5.942  13.626  1.00 61.33           O  
-ATOM   9338  N   ASN D 272      76.919  -5.654  13.128  1.00 63.89           N  
-ATOM   9339  CA  ASN D 272      77.160  -4.508  12.261  1.00 60.08           C  
-ATOM   9340  C   ASN D 272      76.667  -3.271  12.995  1.00 48.48           C  
-ATOM   9341  O   ASN D 272      75.644  -3.319  13.685  1.00 43.24           O  
-ATOM   9342  CB  ASN D 272      76.394  -4.644  10.940  1.00 68.03           C  
-ATOM   9343  CG  ASN D 272      77.112  -5.521   9.933  1.00 80.65           C  
-ATOM   9344  OD1 ASN D 272      78.289  -5.299   9.618  1.00 85.43           O  
-ATOM   9345  ND2 ASN D 272      76.404  -6.520   9.410  1.00 88.23           N  
-ATOM   9346  N   ILE D 273      77.392  -2.168  12.860  1.00 40.55           N  
-ATOM   9347  CA  ILE D 273      76.970  -0.938  13.518  1.00 36.67           C  
-ATOM   9348  C   ILE D 273      75.673  -0.447  12.848  1.00 27.84           C  
-ATOM   9349  O   ILE D 273      75.636  -0.218  11.638  1.00 23.86           O  
-ATOM   9350  CB  ILE D 273      78.068   0.140  13.425  1.00 31.07           C  
-ATOM   9351  CG1 ILE D 273      77.543   1.451  14.015  1.00 30.95           C  
-ATOM   9352  CG2 ILE D 273      78.530   0.293  11.973  1.00 26.13           C  
-ATOM   9353  CD1 ILE D 273      78.529   2.597  13.954  1.00 32.35           C  
-ATOM   9354  N   LEU D 274      74.613  -0.298  13.641  1.00 20.84           N  
-ATOM   9355  CA  LEU D 274      73.318   0.127  13.115  1.00 22.03           C  
-ATOM   9356  C   LEU D 274      73.364   1.372  12.239  1.00 22.15           C  
-ATOM   9357  O   LEU D 274      74.105   2.321  12.519  1.00 13.85           O  
-ATOM   9358  CB  LEU D 274      72.293   0.324  14.250  1.00 19.63           C  
-ATOM   9359  CG  LEU D 274      71.605  -0.959  14.762  1.00 23.75           C  
-ATOM   9360  CD1 LEU D 274      72.540  -1.711  15.687  1.00 16.71           C  
-ATOM   9361  CD2 LEU D 274      70.314  -0.615  15.501  1.00 31.42           C  
-ATOM   9362  N   PRO D 275      72.555   1.373  11.158  1.00 22.69           N  
-ATOM   9363  CA  PRO D 275      72.431   2.449  10.176  1.00 20.73           C  
-ATOM   9364  C   PRO D 275      72.630   3.858  10.709  1.00 16.09           C  
-ATOM   9365  O   PRO D 275      73.652   4.494  10.423  1.00 20.39           O  
-ATOM   9366  CB  PRO D 275      71.035   2.228   9.624  1.00 17.41           C  
-ATOM   9367  CG  PRO D 275      70.989   0.743   9.535  1.00 14.53           C  
-ATOM   9368  CD  PRO D 275      71.565   0.313  10.871  1.00 15.37           C  
-ATOM   9369  N   LEU D 276      71.667   4.351  11.480  1.00  8.06           N  
-ATOM   9370  CA  LEU D 276      71.791   5.715  11.984  1.00 13.50           C  
-ATOM   9371  C   LEU D 276      73.138   5.953  12.622  1.00  8.17           C  
-ATOM   9372  O   LEU D 276      73.859   6.873  12.228  1.00 14.24           O  
-ATOM   9373  CB  LEU D 276      70.675   6.042  12.974  1.00  4.55           C  
-ATOM   9374  CG  LEU D 276      69.315   6.209  12.310  1.00  4.47           C  
-ATOM   9375  CD1 LEU D 276      68.244   6.507  13.329  1.00  8.03           C  
-ATOM   9376  CD2 LEU D 276      69.414   7.337  11.320  1.00  4.47           C  
-ATOM   9377  N   TRP D 277      73.487   5.111  13.586  1.00  4.47           N  
-ATOM   9378  CA  TRP D 277      74.761   5.251  14.278  1.00  8.27           C  
-ATOM   9379  C   TRP D 277      75.931   5.372  13.290  1.00 15.22           C  
-ATOM   9380  O   TRP D 277      76.941   6.018  13.580  1.00 10.85           O  
-ATOM   9381  CB  TRP D 277      74.974   4.061  15.219  1.00 10.97           C  
-ATOM   9382  CG  TRP D 277      73.900   3.893  16.287  1.00  9.95           C  
-ATOM   9383  CD1 TRP D 277      73.654   2.768  17.030  1.00 11.41           C  
-ATOM   9384  CD2 TRP D 277      72.955   4.875  16.730  1.00  6.38           C  
-ATOM   9385  NE1 TRP D 277      72.617   2.991  17.900  1.00 12.45           N  
-ATOM   9386  CE2 TRP D 277      72.169   4.275  17.740  1.00  4.47           C  
-ATOM   9387  CE3 TRP D 277      72.697   6.204  16.375  1.00 20.69           C  
-ATOM   9388  CZ2 TRP D 277      71.141   4.958  18.400  1.00  4.47           C  
-ATOM   9389  CZ3 TRP D 277      71.666   6.887  17.040  1.00 26.55           C  
-ATOM   9390  CH2 TRP D 277      70.904   6.256  18.041  1.00  7.20           C  
-ATOM   9391  N   ALA D 278      75.794   4.757  12.119  1.00 13.82           N  
-ATOM   9392  CA  ALA D 278      76.846   4.838  11.122  1.00  8.09           C  
-ATOM   9393  C   ALA D 278      76.888   6.268  10.676  1.00  4.85           C  
-ATOM   9394  O   ALA D 278      77.897   6.939  10.838  1.00  8.92           O  
-ATOM   9395  CB  ALA D 278      76.538   3.951   9.955  1.00  7.42           C  
-ATOM   9396  N   TRP D 279      75.776   6.734  10.120  1.00 10.31           N  
-ATOM   9397  CA  TRP D 279      75.687   8.112   9.651  1.00 18.77           C  
-ATOM   9398  C   TRP D 279      76.311   9.004  10.698  1.00 11.52           C  
-ATOM   9399  O   TRP D 279      77.015   9.958  10.381  1.00 13.04           O  
-ATOM   9400  CB  TRP D 279      74.229   8.525   9.436  1.00 21.17           C  
-ATOM   9401  CG  TRP D 279      73.551   7.798   8.307  1.00 23.84           C  
-ATOM   9402  CD1 TRP D 279      74.038   6.739   7.613  1.00 25.45           C  
-ATOM   9403  CD2 TRP D 279      72.231   8.033   7.808  1.00 21.74           C  
-ATOM   9404  NE1 TRP D 279      73.105   6.292   6.719  1.00 33.61           N  
-ATOM   9405  CE2 TRP D 279      71.984   7.070   6.820  1.00 28.12           C  
-ATOM   9406  CE3 TRP D 279      71.230   8.965   8.107  1.00 32.75           C  
-ATOM   9407  CZ2 TRP D 279      70.774   7.004   6.124  1.00 39.56           C  
-ATOM   9408  CZ3 TRP D 279      70.026   8.904   7.417  1.00 27.54           C  
-ATOM   9409  CH2 TRP D 279      69.808   7.929   6.436  1.00 34.96           C  
-ATOM   9410  N   GLY D 280      76.054   8.674  11.954  1.00  8.45           N  
-ATOM   9411  CA  GLY D 280      76.609   9.457  13.034  1.00 13.17           C  
-ATOM   9412  C   GLY D 280      78.125   9.452  12.986  1.00 16.33           C  
-ATOM   9413  O   GLY D 280      78.748  10.514  13.012  1.00 18.40           O  
-ATOM   9414  N   MET D 281      78.721   8.262  12.929  1.00 16.74           N  
-ATOM   9415  CA  MET D 281      80.177   8.142  12.869  1.00 15.84           C  
-ATOM   9416  C   MET D 281      80.690   9.087  11.785  1.00 21.01           C  
-ATOM   9417  O   MET D 281      81.704   9.764  11.959  1.00 25.48           O  
-ATOM   9418  CB  MET D 281      80.578   6.704  12.523  1.00 12.84           C  
-ATOM   9419  CG  MET D 281      80.068   5.668  13.518  1.00 19.77           C  
-ATOM   9420  SD  MET D 281      81.140   5.436  14.968  1.00 30.21           S  
-ATOM   9421  CE  MET D 281      81.016   6.939  15.726  1.00 17.67           C  
-ATOM   9422  N   GLU D 282      79.972   9.134  10.668  1.00 20.59           N  
-ATOM   9423  CA  GLU D 282      80.341   9.994   9.549  1.00 25.52           C  
-ATOM   9424  C   GLU D 282      80.559  11.449  10.011  1.00 20.92           C  
-ATOM   9425  O   GLU D 282      81.655  11.993   9.860  1.00 19.96           O  
-ATOM   9426  CB  GLU D 282      79.243   9.936   8.469  1.00 38.02           C  
-ATOM   9427  CG  GLU D 282      79.741   9.738   7.028  1.00 49.84           C  
-ATOM   9428  CD  GLU D 282      80.341   8.358   6.776  1.00 57.66           C  
-ATOM   9429  OE1 GLU D 282      79.617   7.349   6.954  1.00 58.50           O  
-ATOM   9430  OE2 GLU D 282      81.535   8.288   6.394  1.00 56.63           O  
-ATOM   9431  N   THR D 283      79.522  12.066  10.580  1.00 20.26           N  
-ATOM   9432  CA  THR D 283      79.606  13.455  11.052  1.00 15.71           C  
-ATOM   9433  C   THR D 283      80.682  13.625  12.129  1.00 12.50           C  
-ATOM   9434  O   THR D 283      81.419  14.605  12.123  1.00 14.13           O  
-ATOM   9435  CB  THR D 283      78.245  13.954  11.625  1.00 11.61           C  
-ATOM   9436  OG1 THR D 283      77.898  13.186  12.783  1.00 27.49           O  
-ATOM   9437  CG2 THR D 283      77.139  13.794  10.611  1.00  8.98           C  
-ATOM   9438  N   LEU D 284      80.762  12.681  13.063  1.00 12.90           N  
-ATOM   9439  CA  LEU D 284      81.775  12.752  14.111  1.00 14.43           C  
-ATOM   9440  C   LEU D 284      83.151  12.780  13.442  1.00 16.53           C  
-ATOM   9441  O   LEU D 284      84.052  13.490  13.878  1.00 16.24           O  
-ATOM   9442  CB  LEU D 284      81.666  11.543  15.058  1.00 15.36           C  
-ATOM   9443  CG  LEU D 284      82.818  11.354  16.060  1.00 12.82           C  
-ATOM   9444  CD1 LEU D 284      82.404  10.430  17.181  1.00 10.48           C  
-ATOM   9445  CD2 LEU D 284      84.027  10.773  15.352  1.00 20.15           C  
-ATOM   9446  N   SER D 285      83.312  11.988  12.388  1.00 14.95           N  
-ATOM   9447  CA  SER D 285      84.566  11.953  11.669  1.00 16.62           C  
-ATOM   9448  C   SER D 285      84.728  13.323  11.037  1.00 18.94           C  
-ATOM   9449  O   SER D 285      85.730  13.997  11.247  1.00 22.95           O  
-ATOM   9450  CB  SER D 285      84.522  10.881  10.583  1.00 23.95           C  
-ATOM   9451  OG  SER D 285      84.337   9.596  11.143  1.00 30.84           O  
-ATOM   9452  N   ASN D 286      83.722  13.733  10.271  1.00 23.85           N  
-ATOM   9453  CA  ASN D 286      83.731  15.029   9.592  1.00 30.88           C  
-ATOM   9454  C   ASN D 286      84.307  16.139  10.461  1.00 25.63           C  
-ATOM   9455  O   ASN D 286      85.132  16.934  10.010  1.00 22.72           O  
-ATOM   9456  CB  ASN D 286      82.308  15.402   9.151  1.00 28.54           C  
-ATOM   9457  CG  ASN D 286      81.951  14.844   7.773  1.00 40.40           C  
-ATOM   9458  OD1 ASN D 286      82.656  13.983   7.227  1.00 45.25           O  
-ATOM   9459  ND2 ASN D 286      80.850  15.335   7.204  1.00 41.72           N  
-ATOM   9460  N   CYS D 287      83.865  16.175  11.714  1.00 29.09           N  
-ATOM   9461  CA  CYS D 287      84.308  17.183  12.676  1.00 30.87           C  
-ATOM   9462  C   CYS D 287      85.798  17.054  13.041  1.00 35.05           C  
-ATOM   9463  O   CYS D 287      86.612  17.926  12.712  1.00 31.20           O  
-ATOM   9464  CB  CYS D 287      83.434  17.092  13.941  1.00 23.17           C  
-ATOM   9465  SG  CYS D 287      84.047  18.005  15.399  1.00 26.68           S  
-ATOM   9466  N   LEU D 288      86.138  15.960  13.722  1.00 36.67           N  
-ATOM   9467  CA  LEU D 288      87.502  15.668  14.163  1.00 25.16           C  
-ATOM   9468  C   LEU D 288      88.558  15.797  13.073  1.00 28.48           C  
-ATOM   9469  O   LEU D 288      89.659  16.267  13.321  1.00 29.17           O  
-ATOM   9470  CB  LEU D 288      87.547  14.257  14.734  1.00 17.39           C  
-ATOM   9471  CG  LEU D 288      87.659  14.091  16.251  1.00 21.17           C  
-ATOM   9472  CD1 LEU D 288      86.782  15.078  16.965  1.00 31.60           C  
-ATOM   9473  CD2 LEU D 288      87.261  12.669  16.635  1.00 21.10           C  
-ATOM   9474  N   ARG D 289      88.217  15.370  11.865  1.00 33.62           N  
-ATOM   9475  CA  ARG D 289      89.140  15.420  10.736  1.00 31.51           C  
-ATOM   9476  C   ARG D 289      89.558  16.830  10.345  1.00 31.56           C  
-ATOM   9477  O   ARG D 289      90.680  17.051   9.901  1.00 38.02           O  
-ATOM   9478  CB  ARG D 289      88.513  14.721   9.523  1.00 31.49           C  
-ATOM   9479  CG  ARG D 289      89.354  14.763   8.251  1.00 30.16           C  
-ATOM   9480  CD  ARG D 289      88.965  13.625   7.327  1.00 30.34           C  
-ATOM   9481  NE  ARG D 289      87.523  13.571   7.108  1.00 27.02           N  
-ATOM   9482  CZ  ARG D 289      86.816  12.444   7.107  1.00 37.62           C  
-ATOM   9483  NH1 ARG D 289      87.419  11.275   7.319  1.00 35.40           N  
-ATOM   9484  NH2 ARG D 289      85.506  12.485   6.889  1.00 37.75           N  
-ATOM   9485  N   SER D 290      88.654  17.785  10.501  1.00 27.41           N  
-ATOM   9486  CA  SER D 290      88.960  19.153  10.139  1.00 24.10           C  
-ATOM   9487  C   SER D 290      90.092  19.694  10.986  1.00 24.65           C  
-ATOM   9488  O   SER D 290      90.920  20.471  10.514  1.00 31.90           O  
-ATOM   9489  CB  SER D 290      87.724  20.023  10.341  1.00 28.42           C  
-ATOM   9490  OG  SER D 290      86.642  19.534   9.570  1.00 44.54           O  
-ATOM   9491  N   MET D 291      90.132  19.250  12.236  1.00 22.22           N  
-ATOM   9492  CA  MET D 291      91.111  19.726  13.206  1.00 19.32           C  
-ATOM   9493  C   MET D 291      92.612  19.520  12.984  1.00 12.61           C  
-ATOM   9494  O   MET D 291      93.053  18.530  12.412  1.00 13.07           O  
-ATOM   9495  CB  MET D 291      90.693  19.218  14.587  1.00 23.61           C  
-ATOM   9496  CG  MET D 291      89.384  19.860  15.044  1.00 26.14           C  
-ATOM   9497  SD  MET D 291      88.736  19.336  16.643  1.00 37.72           S  
-ATOM   9498  CE  MET D 291      87.207  18.586  16.104  1.00 33.41           C  
-ATOM   9499  N   SER D 292      93.381  20.501  13.446  1.00 10.18           N  
-ATOM   9500  CA  SER D 292      94.835  20.501  13.341  1.00 15.44           C  
-ATOM   9501  C   SER D 292      95.353  20.277  14.751  1.00 14.33           C  
-ATOM   9502  O   SER D 292      95.419  21.191  15.566  1.00 23.46           O  
-ATOM   9503  CB  SER D 292      95.321  21.850  12.807  1.00 27.06           C  
-ATOM   9504  OG  SER D 292      94.599  22.231  11.646  1.00 40.58           O  
-ATOM   9505  N   PRO D 293      95.736  19.046  15.052  1.00 10.09           N  
-ATOM   9506  CA  PRO D 293      96.248  18.610  16.350  1.00 16.08           C  
-ATOM   9507  C   PRO D 293      97.664  19.030  16.745  1.00 19.35           C  
-ATOM   9508  O   PRO D 293      98.609  18.898  15.955  1.00 22.53           O  
-ATOM   9509  CB  PRO D 293      96.116  17.096  16.256  1.00 23.28           C  
-ATOM   9510  CG  PRO D 293      96.496  16.861  14.817  1.00 19.88           C  
-ATOM   9511  CD  PRO D 293      95.723  17.937  14.086  1.00 10.34           C  
-ATOM   9512  N   PHE D 294      97.793  19.499  17.989  1.00 12.44           N  
-ATOM   9513  CA  PHE D 294      99.068  19.924  18.567  1.00  8.62           C  
-ATOM   9514  C   PHE D 294      99.142  19.516  20.029  1.00 12.44           C  
-ATOM   9515  O   PHE D 294      98.150  19.577  20.754  1.00 15.45           O  
-ATOM   9516  CB  PHE D 294      99.229  21.439  18.489  1.00 10.85           C  
-ATOM   9517  CG  PHE D 294      99.384  21.958  17.097  1.00 16.48           C  
-ATOM   9518  CD1 PHE D 294      98.403  22.760  16.532  1.00 19.43           C  
-ATOM   9519  CD2 PHE D 294     100.512  21.638  16.346  1.00 25.74           C  
-ATOM   9520  CE1 PHE D 294      98.538  23.238  15.240  1.00 28.33           C  
-ATOM   9521  CE2 PHE D 294     100.662  22.109  15.049  1.00 33.46           C  
-ATOM   9522  CZ  PHE D 294      99.671  22.912  14.493  1.00 37.47           C  
-ATOM   9523  N   VAL D 295     100.327  19.113  20.465  1.00 17.36           N  
-ATOM   9524  CA  VAL D 295     100.520  18.690  21.849  1.00 23.20           C  
-ATOM   9525  C   VAL D 295     101.462  19.660  22.528  1.00 30.99           C  
-ATOM   9526  O   VAL D 295     102.539  19.952  22.003  1.00 40.06           O  
-ATOM   9527  CB  VAL D 295     101.113  17.255  21.930  1.00 21.65           C  
-ATOM   9528  CG1 VAL D 295     101.867  17.055  23.252  1.00 19.25           C  
-ATOM   9529  CG2 VAL D 295      99.985  16.231  21.811  1.00 12.49           C  
-ATOM   9530  N   LEU D 296     101.052  20.148  23.697  1.00 30.42           N  
-ATOM   9531  CA  LEU D 296     101.843  21.108  24.452  1.00 28.44           C  
-ATOM   9532  C   LEU D 296     102.081  20.589  25.855  1.00 33.72           C  
-ATOM   9533  O   LEU D 296     101.134  20.258  26.574  1.00 35.22           O  
-ATOM   9534  CB  LEU D 296     101.096  22.438  24.503  1.00 26.90           C  
-ATOM   9535  CG  LEU D 296     101.743  23.651  25.166  1.00 32.22           C  
-ATOM   9536  CD1 LEU D 296     100.840  24.864  24.966  1.00 34.47           C  
-ATOM   9537  CD2 LEU D 296     101.954  23.395  26.653  1.00 36.55           C  
-ATOM   9538  N   SER D 297     103.347  20.530  26.249  1.00 36.76           N  
-ATOM   9539  CA  SER D 297     103.698  20.037  27.574  1.00 42.04           C  
-ATOM   9540  C   SER D 297     103.669  21.121  28.624  1.00 39.16           C  
-ATOM   9541  O   SER D 297     104.318  22.144  28.463  1.00 45.60           O  
-ATOM   9542  CB  SER D 297     105.094  19.420  27.557  1.00 51.51           C  
-ATOM   9543  OG  SER D 297     105.519  19.114  28.876  1.00 58.33           O  
-ATOM   9544  N   LEU D 298     102.924  20.897  29.701  1.00 40.12           N  
-ATOM   9545  CA  LEU D 298     102.851  21.873  30.785  1.00 48.80           C  
-ATOM   9546  C   LEU D 298     103.732  21.435  31.946  1.00 57.84           C  
-ATOM   9547  O   LEU D 298     103.504  21.827  33.094  1.00 58.78           O  
-ATOM   9548  CB  LEU D 298     101.413  22.038  31.279  1.00 44.17           C  
-ATOM   9549  CG  LEU D 298     100.412  22.620  30.282  1.00 42.21           C  
-ATOM   9550  CD1 LEU D 298      99.106  22.905  30.993  1.00 40.83           C  
-ATOM   9551  CD2 LEU D 298     100.958  23.899  29.689  1.00 46.08           C  
-ATOM   9552  N   GLU D 299     104.738  20.621  31.632  1.00 66.80           N  
-ATOM   9553  CA  GLU D 299     105.671  20.103  32.633  1.00 75.70           C  
-ATOM   9554  C   GLU D 299     106.853  21.058  32.793  1.00 75.41           C  
-ATOM   9555  O   GLU D 299     107.989  20.730  32.437  1.00 77.43           O  
-ATOM   9556  CB  GLU D 299     106.172  18.713  32.208  1.00 82.99           C  
-ATOM   9557  CG  GLU D 299     107.044  17.988  33.239  1.00 93.75           C  
-ATOM   9558  CD  GLU D 299     106.246  17.413  34.401  1.00100.80           C  
-ATOM   9559  OE1 GLU D 299     106.867  16.782  35.287  1.00103.50           O  
-ATOM   9560  OE2 GLU D 299     105.006  17.587  34.426  1.00103.81           O  
-ATOM   9561  N   GLN D 300     106.574  22.242  33.331  1.00 73.56           N  
-ATOM   9562  CA  GLN D 300     107.597  23.257  33.539  1.00 75.12           C  
-ATOM   9563  C   GLN D 300     106.951  24.580  33.937  1.00 80.85           C  
-ATOM   9564  O   GLN D 300     105.731  24.662  34.100  1.00 82.91           O  
-ATOM   9565  CB  GLN D 300     108.414  23.445  32.259  1.00 71.05           C  
-ATOM   9566  CG  GLN D 300     107.569  23.679  31.017  1.00 65.02           C  
-ATOM   9567  CD  GLN D 300     108.402  23.767  29.759  1.00 67.61           C  
-ATOM   9568  OE1 GLN D 300     107.868  23.950  28.667  1.00 67.36           O  
-ATOM   9569  NE2 GLN D 300     109.721  23.642  29.905  1.00 66.62           N  
-ATOM   9570  N   THR D 301     107.776  25.613  34.092  1.00 84.76           N  
-ATOM   9571  CA  THR D 301     107.294  26.944  34.458  1.00 81.73           C  
-ATOM   9572  C   THR D 301     106.342  27.496  33.387  1.00 77.95           C  
-ATOM   9573  O   THR D 301     106.603  27.373  32.187  1.00 76.16           O  
-ATOM   9574  CB  THR D 301     108.476  27.939  34.632  1.00 82.78           C  
-ATOM   9575  OG1 THR D 301     109.216  28.034  33.404  1.00 79.97           O  
-ATOM   9576  CG2 THR D 301     109.403  27.475  35.755  1.00 80.82           C  
-ATOM   9577  N   PRO D 302     105.222  28.109  33.812  1.00 74.31           N  
-ATOM   9578  CA  PRO D 302     104.243  28.676  32.879  1.00 74.05           C  
-ATOM   9579  C   PRO D 302     104.920  29.480  31.774  1.00 77.41           C  
-ATOM   9580  O   PRO D 302     104.412  29.544  30.654  1.00 80.05           O  
-ATOM   9581  CB  PRO D 302     103.377  29.549  33.778  1.00 72.80           C  
-ATOM   9582  CG  PRO D 302     103.374  28.781  35.059  1.00 74.21           C  
-ATOM   9583  CD  PRO D 302     104.827  28.375  35.207  1.00 73.38           C  
-ATOM   9584  N   GLN D 303     106.060  30.094  32.098  1.00 79.26           N  
-ATOM   9585  CA  GLN D 303     106.817  30.878  31.122  1.00 81.42           C  
-ATOM   9586  C   GLN D 303     107.166  30.006  29.913  1.00 79.67           C  
-ATOM   9587  O   GLN D 303     106.863  30.363  28.771  1.00 79.37           O  
-ATOM   9588  CB  GLN D 303     108.111  31.438  31.741  1.00 86.35           C  
-ATOM   9589  CG  GLN D 303     107.956  32.755  32.509  1.00 94.18           C  
-ATOM   9590  CD  GLN D 303     107.256  32.593  33.848  1.00101.18           C  
-ATOM   9591  OE1 GLN D 303     107.728  31.869  34.725  1.00103.64           O  
-ATOM   9592  NE2 GLN D 303     106.127  33.274  34.014  1.00103.57           N  
-ATOM   9593  N   HIS D 304     107.799  28.862  30.165  1.00 76.43           N  
-ATOM   9594  CA  HIS D 304     108.169  27.954  29.085  1.00 73.45           C  
-ATOM   9595  C   HIS D 304     106.945  27.454  28.321  1.00 71.18           C  
-ATOM   9596  O   HIS D 304     106.886  27.563  27.094  1.00 71.47           O  
-ATOM   9597  CB  HIS D 304     108.954  26.765  29.635  1.00 77.91           C  
-ATOM   9598  CG  HIS D 304     110.355  27.099  30.037  1.00 88.26           C  
-ATOM   9599  ND1 HIS D 304     111.304  26.133  30.294  1.00 91.99           N  
-ATOM   9600  CD2 HIS D 304     110.972  28.291  30.217  1.00 91.62           C  
-ATOM   9601  CE1 HIS D 304     112.447  26.715  30.612  1.00 94.36           C  
-ATOM   9602  NE2 HIS D 304     112.272  28.025  30.572  1.00 96.68           N  
-ATOM   9603  N   ALA D 305     105.972  26.908  29.050  1.00 66.71           N  
-ATOM   9604  CA  ALA D 305     104.742  26.395  28.446  1.00 58.97           C  
-ATOM   9605  C   ALA D 305     104.231  27.353  27.380  1.00 55.85           C  
-ATOM   9606  O   ALA D 305     103.947  26.950  26.253  1.00 54.47           O  
-ATOM   9607  CB  ALA D 305     103.677  26.201  29.515  1.00 57.82           C  
-ATOM   9608  N   ALA D 306     104.125  28.627  27.745  1.00 52.97           N  
-ATOM   9609  CA  ALA D 306     103.650  29.651  26.824  1.00 54.01           C  
-ATOM   9610  C   ALA D 306     104.644  29.921  25.696  1.00 54.97           C  
-ATOM   9611  O   ALA D 306     104.250  30.104  24.544  1.00 56.10           O  
-ATOM   9612  CB  ALA D 306     103.361  30.937  27.581  1.00 51.85           C  
-ATOM   9613  N   GLN D 307     105.931  29.953  26.021  1.00 57.34           N  
-ATOM   9614  CA  GLN D 307     106.939  30.203  24.999  1.00 62.99           C  
-ATOM   9615  C   GLN D 307     106.862  29.107  23.947  1.00 57.95           C  
-ATOM   9616  O   GLN D 307     106.920  29.374  22.745  1.00 51.49           O  
-ATOM   9617  CB  GLN D 307     108.345  30.240  25.613  1.00 75.32           C  
-ATOM   9618  CG  GLN D 307     109.446  30.608  24.608  1.00 92.60           C  
-ATOM   9619  CD  GLN D 307     110.813  30.820  25.256  1.00101.64           C  
-ATOM   9620  OE1 GLN D 307     110.981  31.688  26.122  1.00106.03           O  
-ATOM   9621  NE2 GLN D 307     111.799  30.030  24.832  1.00 98.89           N  
-ATOM   9622  N   GLU D 308     106.726  27.870  24.411  1.00 56.32           N  
-ATOM   9623  CA  GLU D 308     106.635  26.742  23.503  1.00 54.63           C  
-ATOM   9624  C   GLU D 308     105.431  26.966  22.594  1.00 46.97           C  
-ATOM   9625  O   GLU D 308     105.551  26.926  21.375  1.00 44.20           O  
-ATOM   9626  CB  GLU D 308     106.490  25.430  24.290  1.00 59.13           C  
-ATOM   9627  CG  GLU D 308     106.527  24.171  23.420  1.00 72.30           C  
-ATOM   9628  CD  GLU D 308     106.529  22.879  24.228  1.00 82.13           C  
-ATOM   9629  OE1 GLU D 308     106.415  21.788  23.624  1.00 84.19           O  
-ATOM   9630  OE2 GLU D 308     106.648  22.955  25.467  1.00 88.23           O  
-ATOM   9631  N   LEU D 309     104.274  27.227  23.189  1.00 39.14           N  
-ATOM   9632  CA  LEU D 309     103.068  27.454  22.408  1.00 36.19           C  
-ATOM   9633  C   LEU D 309     103.317  28.468  21.300  1.00 39.52           C  
-ATOM   9634  O   LEU D 309     102.757  28.355  20.207  1.00 41.45           O  
-ATOM   9635  CB  LEU D 309     101.933  27.948  23.312  1.00 32.99           C  
-ATOM   9636  CG  LEU D 309     100.643  28.438  22.632  1.00 24.56           C  
-ATOM   9637  CD1 LEU D 309     100.087  27.362  21.703  1.00 24.40           C  
-ATOM   9638  CD2 LEU D 309      99.619  28.802  23.692  1.00 18.40           C  
-ATOM   9639  N   LYS D 310     104.160  29.456  21.580  1.00 41.33           N  
-ATOM   9640  CA  LYS D 310     104.462  30.486  20.594  1.00 45.50           C  
-ATOM   9641  C   LYS D 310     105.156  29.909  19.364  1.00 45.28           C  
-ATOM   9642  O   LYS D 310     104.838  30.266  18.227  1.00 44.79           O  
-ATOM   9643  CB  LYS D 310     105.355  31.568  21.205  1.00 53.02           C  
-ATOM   9644  CG  LYS D 310     105.787  32.616  20.188  1.00 66.87           C  
-ATOM   9645  CD  LYS D 310     106.845  33.562  20.741  1.00 79.52           C  
-ATOM   9646  CE  LYS D 310     107.340  34.519  19.653  1.00 87.80           C  
-ATOM   9647  NZ  LYS D 310     108.400  35.458  20.141  1.00 92.26           N  
-ATOM   9648  N   THR D 311     106.108  29.016  19.601  1.00 43.86           N  
-ATOM   9649  CA  THR D 311     106.864  28.403  18.517  1.00 41.80           C  
-ATOM   9650  C   THR D 311     105.947  27.647  17.553  1.00 38.15           C  
-ATOM   9651  O   THR D 311     106.302  27.422  16.393  1.00 36.52           O  
-ATOM   9652  CB  THR D 311     107.935  27.430  19.083  1.00 47.18           C  
-ATOM   9653  OG1 THR D 311     107.368  26.121  19.229  1.00 53.84           O  
-ATOM   9654  CG2 THR D 311     108.424  27.911  20.468  1.00 41.77           C  
-ATOM   9655  N   LEU D 312     104.763  27.280  18.045  1.00 38.60           N  
-ATOM   9656  CA  LEU D 312     103.770  26.526  17.278  1.00 39.21           C  
-ATOM   9657  C   LEU D 312     102.887  27.374  16.393  1.00 38.12           C  
-ATOM   9658  O   LEU D 312     102.374  26.893  15.384  1.00 32.34           O  
-ATOM   9659  CB  LEU D 312     102.860  25.732  18.218  1.00 41.32           C  
-ATOM   9660  CG  LEU D 312     103.319  24.399  18.819  1.00 47.81           C  
-ATOM   9661  CD1 LEU D 312     104.610  24.545  19.609  1.00 47.63           C  
-ATOM   9662  CD2 LEU D 312     102.215  23.894  19.720  1.00 50.56           C  
-ATOM   9663  N   LEU D 313     102.692  28.627  16.790  1.00 43.13           N  
-ATOM   9664  CA  LEU D 313     101.844  29.558  16.044  1.00 46.12           C  
-ATOM   9665  C   LEU D 313     102.032  29.474  14.533  1.00 44.74           C  
-ATOM   9666  O   LEU D 313     101.055  29.478  13.783  1.00 43.72           O  
-ATOM   9667  CB  LEU D 313     102.097  30.992  16.515  1.00 46.28           C  
-ATOM   9668  CG  LEU D 313     101.914  31.203  18.021  1.00 49.09           C  
-ATOM   9669  CD1 LEU D 313     102.288  32.626  18.392  1.00 55.18           C  
-ATOM   9670  CD2 LEU D 313     100.476  30.904  18.407  1.00 47.16           C  
-ATOM   9671  N   PRO D 314     103.291  29.403  14.066  1.00 46.58           N  
-ATOM   9672  CA  PRO D 314     103.565  29.317  12.626  1.00 48.61           C  
-ATOM   9673  C   PRO D 314     103.133  28.002  11.952  1.00 50.94           C  
-ATOM   9674  O   PRO D 314     102.989  27.943  10.722  1.00 47.09           O  
-ATOM   9675  CB  PRO D 314     105.076  29.543  12.553  1.00 46.58           C  
-ATOM   9676  CG  PRO D 314     105.566  28.985  13.864  1.00 47.19           C  
-ATOM   9677  CD  PRO D 314     104.549  29.537  14.828  1.00 45.99           C  
-ATOM   9678  N   GLN D 315     102.919  26.959  12.756  1.00 52.99           N  
-ATOM   9679  CA  GLN D 315     102.517  25.648  12.233  1.00 50.21           C  
-ATOM   9680  C   GLN D 315     100.994  25.483  12.162  1.00 45.78           C  
-ATOM   9681  O   GLN D 315     100.485  24.607  11.450  1.00 46.90           O  
-ATOM   9682  CB  GLN D 315     103.099  24.514  13.104  1.00 47.29           C  
-ATOM   9683  CG  GLN D 315     104.605  24.574  13.327  1.00 51.54           C  
-ATOM   9684  CD  GLN D 315     105.136  23.339  14.036  1.00 59.31           C  
-ATOM   9685  OE1 GLN D 315     105.141  22.242  13.476  1.00 63.52           O  
-ATOM   9686  NE2 GLN D 315     105.579  23.512  15.277  1.00 63.75           N  
-ATOM   9687  N   MET D 316     100.270  26.325  12.896  1.00 35.80           N  
-ATOM   9688  CA  MET D 316      98.820  26.235  12.938  1.00 27.14           C  
-ATOM   9689  C   MET D 316      98.113  26.720  11.684  1.00 29.57           C  
-ATOM   9690  O   MET D 316      98.616  27.570  10.953  1.00 33.79           O  
-ATOM   9691  CB  MET D 316      98.306  26.985  14.160  1.00 14.36           C  
-ATOM   9692  CG  MET D 316      98.969  26.508  15.416  1.00 13.05           C  
-ATOM   9693  SD  MET D 316      98.439  27.398  16.849  1.00 33.18           S  
-ATOM   9694  CE  MET D 316      99.251  26.451  18.170  1.00 24.44           C  
-ATOM   9695  N   THR D 317      96.941  26.150  11.438  1.00 29.58           N  
-ATOM   9696  CA  THR D 317      96.132  26.510  10.288  1.00 31.50           C  
-ATOM   9697  C   THR D 317      95.332  27.762  10.616  1.00 35.93           C  
-ATOM   9698  O   THR D 317      94.624  27.804  11.626  1.00 44.27           O  
-ATOM   9699  CB  THR D 317      95.148  25.395   9.946  1.00 35.82           C  
-ATOM   9700  OG1 THR D 317      95.880  24.216   9.588  1.00 40.25           O  
-ATOM   9701  CG2 THR D 317      94.232  25.825   8.797  1.00 34.00           C  
-ATOM   9702  N   PRO D 318      95.448  28.805   9.776  1.00 36.88           N  
-ATOM   9703  CA  PRO D 318      94.736  30.078   9.959  1.00 37.05           C  
-ATOM   9704  C   PRO D 318      93.389  30.154   9.223  1.00 36.42           C  
-ATOM   9705  O   PRO D 318      93.175  29.459   8.222  1.00 35.37           O  
-ATOM   9706  CB  PRO D 318      95.734  31.091   9.420  1.00 34.02           C  
-ATOM   9707  CG  PRO D 318      96.304  30.363   8.246  1.00 28.43           C  
-ATOM   9708  CD  PRO D 318      96.549  28.966   8.805  1.00 32.97           C  
-ATOM   9709  N   ALA D 319      92.488  30.998   9.727  1.00 33.92           N  
-ATOM   9710  CA  ALA D 319      91.170  31.175   9.115  1.00 39.96           C  
-ATOM   9711  C   ALA D 319      90.946  32.645   8.826  1.00 40.90           C  
-ATOM   9712  O   ALA D 319      91.610  33.503   9.399  1.00 34.30           O  
-ATOM   9713  CB  ALA D 319      90.070  30.658  10.031  1.00 44.76           C  
-ATOM   9714  N   ASN D 320      89.999  32.936   7.946  1.00 47.02           N  
-ATOM   9715  CA  ASN D 320      89.734  34.314   7.577  1.00 52.96           C  
-ATOM   9716  C   ASN D 320      88.417  34.816   8.134  1.00 52.05           C  
-ATOM   9717  O   ASN D 320      87.420  34.090   8.145  1.00 49.21           O  
-ATOM   9718  CB  ASN D 320      89.718  34.462   6.048  1.00 65.48           C  
-ATOM   9719  CG  ASN D 320      90.951  33.868   5.384  1.00 74.97           C  
-ATOM   9720  OD1 ASN D 320      92.084  34.173   5.765  1.00 78.22           O  
-ATOM   9721  ND2 ASN D 320      90.733  33.021   4.375  1.00 77.35           N  
-ATOM   9722  N   MET D 321      88.423  36.067   8.589  1.00 52.84           N  
-ATOM   9723  CA  MET D 321      87.220  36.688   9.124  1.00 51.67           C  
-ATOM   9724  C   MET D 321      87.217  38.199   8.955  1.00 52.28           C  
-ATOM   9725  O   MET D 321      88.271  38.845   8.953  1.00 42.45           O  
-ATOM   9726  CB  MET D 321      87.037  36.348  10.605  1.00 50.18           C  
-ATOM   9727  CG  MET D 321      87.828  37.198  11.586  1.00 37.51           C  
-ATOM   9728  SD  MET D 321      87.346  36.798  13.292  1.00 37.00           S  
-ATOM   9729  CE  MET D 321      85.768  37.550  13.387  1.00 34.14           C  
-ATOM   9730  N   SER D 322      86.011  38.746   8.817  1.00 58.48           N  
-ATOM   9731  CA  SER D 322      85.812  40.181   8.646  1.00 61.24           C  
-ATOM   9732  C   SER D 322      86.505  40.969   9.757  1.00 57.44           C  
-ATOM   9733  O   SER D 322      86.385  40.642  10.936  1.00 59.13           O  
-ATOM   9734  CB  SER D 322      84.307  40.500   8.634  1.00 63.73           C  
-ATOM   9735  OG  SER D 322      84.065  41.900   8.581  1.00 67.49           O  
-ATOM   9736  N   SER D 323      87.249  41.998   9.378  1.00 55.53           N  
-ATOM   9737  CA  SER D 323      87.917  42.812  10.373  1.00 54.54           C  
-ATOM   9738  C   SER D 323      86.824  43.318  11.302  1.00 55.64           C  
-ATOM   9739  O   SER D 323      86.983  43.328  12.521  1.00 59.25           O  
-ATOM   9740  CB  SER D 323      88.621  43.998   9.718  1.00 55.39           C  
-ATOM   9741  OG  SER D 323      89.246  44.806  10.704  1.00 54.16           O  
-ATOM   9742  N   GLY D 324      85.705  43.728  10.712  1.00 52.53           N  
-ATOM   9743  CA  GLY D 324      84.595  44.224  11.506  1.00 48.71           C  
-ATOM   9744  C   GLY D 324      84.125  43.215  12.536  1.00 43.01           C  
-ATOM   9745  O   GLY D 324      83.964  43.544  13.718  1.00 36.57           O  
-ATOM   9746  N   ALA D 325      83.916  41.981  12.082  1.00 41.45           N  
-ATOM   9747  CA  ALA D 325      83.454  40.894  12.939  1.00 32.36           C  
-ATOM   9748  C   ALA D 325      84.366  40.691  14.145  1.00 29.40           C  
-ATOM   9749  O   ALA D 325      83.883  40.554  15.272  1.00 33.05           O  
-ATOM   9750  CB  ALA D 325      83.349  39.614  12.141  1.00 25.96           C  
-ATOM   9751  N   TRP D 326      85.676  40.673  13.919  1.00 21.34           N  
-ATOM   9752  CA  TRP D 326      86.610  40.504  15.026  1.00 24.00           C  
-ATOM   9753  C   TRP D 326      86.279  41.490  16.153  1.00 25.63           C  
-ATOM   9754  O   TRP D 326      86.244  41.119  17.330  1.00 16.93           O  
-ATOM   9755  CB  TRP D 326      88.047  40.704  14.534  1.00 26.99           C  
-ATOM   9756  CG  TRP D 326      89.064  40.867  15.629  1.00 25.59           C  
-ATOM   9757  CD1 TRP D 326      89.445  42.031  16.217  1.00 20.24           C  
-ATOM   9758  CD2 TRP D 326      89.805  39.826  16.283  1.00 28.07           C  
-ATOM   9759  NE1 TRP D 326      90.374  41.787  17.199  1.00 19.15           N  
-ATOM   9760  CE2 TRP D 326      90.613  40.442  17.262  1.00 23.14           C  
-ATOM   9761  CE3 TRP D 326      89.865  38.434  16.137  1.00 25.66           C  
-ATOM   9762  CZ2 TRP D 326      91.470  39.717  18.093  1.00 27.61           C  
-ATOM   9763  CZ3 TRP D 326      90.722  37.710  16.968  1.00 30.08           C  
-ATOM   9764  CH2 TRP D 326      91.511  38.355  17.932  1.00 28.32           C  
-ATOM   9765  N   ASN D 327      86.019  42.742  15.787  1.00 31.16           N  
-ATOM   9766  CA  ASN D 327      85.682  43.763  16.770  1.00 36.50           C  
-ATOM   9767  C   ASN D 327      84.375  43.426  17.464  1.00 32.34           C  
-ATOM   9768  O   ASN D 327      84.216  43.674  18.652  1.00 31.73           O  
-ATOM   9769  CB  ASN D 327      85.585  45.129  16.100  1.00 48.84           C  
-ATOM   9770  CG  ASN D 327      86.934  45.640  15.631  1.00 54.67           C  
-ATOM   9771  OD1 ASN D 327      87.897  45.699  16.407  1.00 44.16           O  
-ATOM   9772  ND2 ASN D 327      87.013  46.015  14.358  1.00 62.13           N  
-ATOM   9773  N   ILE D 328      83.435  42.874  16.710  1.00 27.67           N  
-ATOM   9774  CA  ILE D 328      82.160  42.467  17.267  1.00 29.08           C  
-ATOM   9775  C   ILE D 328      82.435  41.309  18.227  1.00 33.44           C  
-ATOM   9776  O   ILE D 328      82.164  41.399  19.423  1.00 38.42           O  
-ATOM   9777  CB  ILE D 328      81.217  41.987  16.155  1.00 33.85           C  
-ATOM   9778  CG1 ILE D 328      80.655  43.187  15.404  1.00 32.07           C  
-ATOM   9779  CG2 ILE D 328      80.102  41.122  16.730  1.00 38.67           C  
-ATOM   9780  CD1 ILE D 328      79.837  42.804  14.187  1.00 34.71           C  
-ATOM   9781  N   LEU D 329      82.975  40.220  17.691  1.00 27.65           N  
-ATOM   9782  CA  LEU D 329      83.288  39.052  18.495  1.00 25.32           C  
-ATOM   9783  C   LEU D 329      83.842  39.487  19.830  1.00 23.61           C  
-ATOM   9784  O   LEU D 329      83.340  39.084  20.872  1.00 26.71           O  
-ATOM   9785  CB  LEU D 329      84.315  38.183  17.782  1.00 30.06           C  
-ATOM   9786  CG  LEU D 329      84.915  37.015  18.569  1.00 22.34           C  
-ATOM   9787  CD1 LEU D 329      83.815  36.064  18.968  1.00 20.02           C  
-ATOM   9788  CD2 LEU D 329      85.956  36.298  17.711  1.00 27.50           C  
-ATOM   9789  N   LYS D 330      84.872  40.324  19.790  1.00 28.10           N  
-ATOM   9790  CA  LYS D 330      85.509  40.823  21.006  1.00 39.87           C  
-ATOM   9791  C   LYS D 330      84.513  41.373  22.014  1.00 42.99           C  
-ATOM   9792  O   LYS D 330      84.599  41.069  23.204  1.00 45.67           O  
-ATOM   9793  CB  LYS D 330      86.515  41.927  20.681  1.00 51.04           C  
-ATOM   9794  CG  LYS D 330      87.776  41.462  19.985  1.00 59.54           C  
-ATOM   9795  CD  LYS D 330      88.854  42.539  20.036  1.00 67.99           C  
-ATOM   9796  CE  LYS D 330      89.174  42.942  21.472  1.00 73.83           C  
-ATOM   9797  NZ  LYS D 330      89.564  41.782  22.325  1.00 71.76           N  
-ATOM   9798  N   GLU D 331      83.586  42.199  21.533  1.00 45.23           N  
-ATOM   9799  CA  GLU D 331      82.570  42.804  22.386  1.00 45.23           C  
-ATOM   9800  C   GLU D 331      81.706  41.710  23.007  1.00 44.31           C  
-ATOM   9801  O   GLU D 331      81.457  41.718  24.211  1.00 48.22           O  
-ATOM   9802  CB  GLU D 331      81.684  43.756  21.578  1.00 49.69           C  
-ATOM   9803  CG  GLU D 331      80.670  44.532  22.417  1.00 64.51           C  
-ATOM   9804  CD  GLU D 331      79.280  44.616  21.769  1.00 82.37           C  
-ATOM   9805  OE1 GLU D 331      79.173  45.066  20.600  1.00 87.91           O  
-ATOM   9806  OE2 GLU D 331      78.288  44.235  22.438  1.00 81.61           O  
-ATOM   9807  N   LEU D 332      81.256  40.765  22.187  1.00 36.63           N  
-ATOM   9808  CA  LEU D 332      80.420  39.680  22.681  1.00 26.17           C  
-ATOM   9809  C   LEU D 332      81.170  38.891  23.728  1.00 20.25           C  
-ATOM   9810  O   LEU D 332      80.660  38.643  24.818  1.00 14.90           O  
-ATOM   9811  CB  LEU D 332      80.018  38.778  21.532  1.00 22.65           C  
-ATOM   9812  CG  LEU D 332      79.428  39.585  20.376  1.00 27.01           C  
-ATOM   9813  CD1 LEU D 332      79.058  38.651  19.245  1.00 34.76           C  
-ATOM   9814  CD2 LEU D 332      78.211  40.366  20.853  1.00 31.43           C  
-ATOM   9815  N   VAL D 333      82.394  38.509  23.395  1.00 20.17           N  
-ATOM   9816  CA  VAL D 333      83.220  37.758  24.319  1.00 25.12           C  
-ATOM   9817  C   VAL D 333      83.380  38.522  25.607  1.00 28.01           C  
-ATOM   9818  O   VAL D 333      83.372  37.939  26.677  1.00 31.60           O  
-ATOM   9819  CB  VAL D 333      84.608  37.511  23.767  1.00 30.21           C  
-ATOM   9820  CG1 VAL D 333      85.418  36.712  24.772  1.00 32.57           C  
-ATOM   9821  CG2 VAL D 333      84.510  36.785  22.431  1.00 38.55           C  
-ATOM   9822  N   ASN D 334      83.540  39.832  25.503  1.00 34.33           N  
-ATOM   9823  CA  ASN D 334      83.691  40.649  26.695  1.00 45.34           C  
-ATOM   9824  C   ASN D 334      82.347  40.826  27.393  1.00 47.29           C  
-ATOM   9825  O   ASN D 334      82.292  41.019  28.603  1.00 54.09           O  
-ATOM   9826  CB  ASN D 334      84.256  42.023  26.343  1.00 55.38           C  
-ATOM   9827  CG  ASN D 334      84.499  42.878  27.571  1.00 64.43           C  
-ATOM   9828  OD1 ASN D 334      85.382  42.582  28.378  1.00 67.04           O  
-ATOM   9829  ND2 ASN D 334      83.708  43.938  27.725  1.00 66.86           N  
-ATOM   9830  N   ALA D 335      81.264  40.757  26.629  1.00 45.69           N  
-ATOM   9831  CA  ALA D 335      79.927  40.915  27.189  1.00 44.61           C  
-ATOM   9832  C   ALA D 335      79.499  39.743  28.058  1.00 50.70           C  
-ATOM   9833  O   ALA D 335      78.683  39.925  28.960  1.00 54.35           O  
-ATOM   9834  CB  ALA D 335      78.920  41.105  26.083  1.00 42.53           C  
-ATOM   9835  N   VAL D 336      80.031  38.548  27.783  1.00 52.45           N  
-ATOM   9836  CA  VAL D 336      79.675  37.351  28.549  1.00 51.42           C  
-ATOM   9837  C   VAL D 336      80.762  36.926  29.529  1.00 56.94           C  
-ATOM   9838  O   VAL D 336      80.493  36.170  30.454  1.00 58.82           O  
-ATOM   9839  CB  VAL D 336      79.351  36.151  27.624  1.00 47.78           C  
-ATOM   9840  CG1 VAL D 336      78.386  36.582  26.543  1.00 52.88           C  
-ATOM   9841  CG2 VAL D 336      80.617  35.586  27.023  1.00 43.81           C  
-ATOM   9842  N   GLN D 337      81.983  37.416  29.322  1.00 66.07           N  
-ATOM   9843  CA  GLN D 337      83.119  37.101  30.194  1.00 75.45           C  
-ATOM   9844  C   GLN D 337      83.330  38.273  31.146  1.00 83.57           C  
-ATOM   9845  O   GLN D 337      84.466  38.722  31.342  1.00 84.84           O  
-ATOM   9846  CB  GLN D 337      84.410  36.891  29.380  1.00 79.31           C  
-ATOM   9847  CG  GLN D 337      84.412  35.710  28.398  1.00 85.01           C  
-ATOM   9848  CD  GLN D 337      84.409  34.356  29.085  1.00 88.21           C  
-ATOM   9849  OE1 GLN D 337      85.268  34.074  29.918  1.00 96.22           O  
-ATOM   9850  NE2 GLN D 337      83.445  33.507  28.732  1.00 82.06           N  
-ATOM   9851  N   ASP D 338      82.229  38.762  31.721  1.00 93.63           N  
-ATOM   9852  CA  ASP D 338      82.241  39.900  32.653  1.00100.39           C  
-ATOM   9853  C   ASP D 338      80.843  40.148  33.253  1.00 98.49           C  
-ATOM   9854  O   ASP D 338      80.141  41.073  32.784  1.00 94.53           O  
-ATOM   9855  CB  ASP D 338      82.745  41.168  31.929  1.00105.23           C  
-ATOM   9856  CG  ASP D 338      82.811  42.394  32.840  1.00102.25           C  
-ATOM   9857  OD1 ASP D 338      83.523  42.350  33.870  1.00 96.17           O  
-ATOM   9858  OD2 ASP D 338      82.153  43.406  32.511  1.00 99.04           O  
-TER    9859      ASP D 338                                                      
-HETATM 9860  PB  ADP A 400      91.067  18.664  57.148  1.00 97.61           P  
-HETATM 9861  O1B ADP A 400      90.990  20.091  57.514  1.00 94.96           O  
-HETATM 9862  O2B ADP A 400      91.047  17.809  58.350  1.00 94.51           O  
-HETATM 9863  O3B ADP A 400      89.934  18.331  56.264  1.00 97.57           O  
-HETATM 9864  PA  ADP A 400      92.899  17.367  55.417  1.00107.82           P  
-HETATM 9865  O1A ADP A 400      93.483  16.236  56.183  1.00102.73           O  
-HETATM 9866  O2A ADP A 400      91.930  16.893  54.384  1.00105.52           O  
-HETATM 9867  O3A ADP A 400      92.288  18.418  56.320  1.00101.25           O  
-HETATM 9868  O3' BVP A 500      84.775  22.905  52.971  1.00 19.86           O  
-HETATM 9869  C3' BVP A 500      84.840  22.493  54.336  1.00 20.59           C  
-HETATM 9870  C2' BVP A 500      84.298  23.528  55.308  1.00 17.71           C  
-HETATM 9871  C1' BVP A 500      82.802  23.279  55.231  1.00 15.39           C  
-HETATM 9872  O4' BVP A 500      82.642  21.899  54.864  1.00 20.31           O  
-HETATM 9873  C4' BVP A 500      83.919  21.324  54.502  1.00 21.22           C  
-HETATM 9874  C5' BVP A 500      84.304  20.323  55.603  1.00 29.81           C  
-HETATM 9875  O5' BVP A 500      85.635  19.808  55.408  1.00 45.31           O  
-HETATM 9876  P   BVP A 500      86.816  19.964  56.535  1.00 58.82           P  
-HETATM 9877  O1P BVP A 500      86.394  20.980  57.539  1.00 49.57           O  
-HETATM 9878  O2P BVP A 500      88.081  20.412  55.861  1.00 64.54           O  
-HETATM 9879  O3P BVP A 500      87.057  18.680  57.202  1.00 53.05           O  
-HETATM 9880  N1  BVP A 500      81.985  23.534  56.504  1.00 20.45           N  
-HETATM 9881  C6  BVP A 500      82.142  22.736  57.644  1.00 30.32           C  
-HETATM 9882  C5  BVP A 500      81.364  22.995  58.842  1.00 32.23           C  
-HETATM 9883  C5A BVP A 500      81.349  22.479  59.863  1.00 43.70           C  
-HETATM 9884  C5B BVP A 500      80.719  21.296  60.218  1.00 56.93           C  
-HETATM 9885 BR   BVP A 500      80.435  20.721  62.090  1.00 77.35          BR  
-HETATM 9886  C4  BVP A 500      80.417  24.120  58.791  1.00 27.44           C  
-HETATM 9887  O4  BVP A 500      79.675  24.474  59.745  1.00 39.61           O  
-HETATM 9888  N3  BVP A 500      80.337  24.847  57.617  1.00 13.82           N  
-HETATM 9889  C2  BVP A 500      81.078  24.592  56.498  1.00 22.72           C  
-HETATM 9890  O2  BVP A 500      80.921  25.311  55.522  1.00 28.34           O  
-HETATM 9891  PB  ADP B1400      45.454  33.868  66.912  1.00 95.36           P  
-HETATM 9892  O1B ADP B1400      45.502  32.707  66.003  1.00 88.63           O  
-HETATM 9893  O2B ADP B1400      45.617  33.444  68.311  1.00 99.03           O  
-HETATM 9894  O3B ADP B1400      46.521  34.817  66.550  1.00 97.27           O  
-HETATM 9895  PA  ADP B1400      43.549  35.935  67.083  1.00 85.79           P  
-HETATM 9896  O1A ADP B1400      43.085  35.973  68.483  1.00 87.96           O  
-HETATM 9897  O2A ADP B1400      44.457  37.069  66.763  1.00 90.94           O  
-HETATM 9898  O3A ADP B1400      44.175  34.618  66.723  1.00 91.19           O  
-HETATM 9899  O5' ADP B1400      42.235  36.091  66.140  1.00 95.07           O  
-HETATM 9900  C5' ADP B1400      42.207  36.919  64.939  1.00105.60           C  
-HETATM 9901  C4' ADP B1400      41.043  37.943  64.963  1.00109.11           C  
-HETATM 9902  O4' ADP B1400      39.738  37.250  64.883  1.00107.51           O  
-HETATM 9903  C3' ADP B1400      41.018  38.739  66.251  1.00112.99           C  
-HETATM 9904  O3' ADP B1400      41.655  40.005  66.009  1.00112.63           O  
-HETATM 9905  C2' ADP B1400      39.562  38.896  66.622  1.00116.65           C  
-HETATM 9906  O2' ADP B1400      39.061  40.203  66.333  1.00123.38           O  
-HETATM 9907  C1' ADP B1400      38.789  37.794  65.872  1.00113.09           C  
-HETATM 9908  N9  ADP B1400      38.283  36.710  66.791  1.00113.19           N  
-HETATM 9909  C8  ADP B1400      39.003  35.874  67.632  1.00115.68           C  
-HETATM 9910  N7  ADP B1400      38.258  35.030  68.300  1.00114.12           N  
-HETATM 9911  C5  ADP B1400      36.957  35.255  67.938  1.00112.44           C  
-HETATM 9912  C6  ADP B1400      35.702  34.669  68.305  1.00111.74           C  
-HETATM 9913  N6  ADP B1400      35.611  33.660  69.197  1.00108.08           N  
-HETATM 9914  N1  ADP B1400      34.560  35.174  67.711  1.00114.82           N  
-HETATM 9915  C2  ADP B1400      34.655  36.184  66.815  1.00116.81           C  
-HETATM 9916  N3  ADP B1400      35.775  36.815  66.387  1.00117.43           N  
-HETATM 9917  C4  ADP B1400      36.939  36.322  66.973  1.00114.10           C  
-HETATM 9918  O3' BVP B1500      51.241  34.771  60.499  1.00 34.04           O  
-HETATM 9919  C3' BVP B1500      51.251  33.940  61.655  1.00 27.78           C  
-HETATM 9920  C2' BVP B1500      51.798  32.546  61.395  1.00 24.46           C  
-HETATM 9921  C1' BVP B1500      53.301  32.807  61.415  1.00 26.46           C  
-HETATM 9922  O4' BVP B1500      53.507  33.949  62.274  1.00 28.98           O  
-HETATM 9923  C4' BVP B1500      52.227  34.542  62.619  1.00 26.62           C  
-HETATM 9924  C5' BVP B1500      51.949  34.256  64.114  1.00 36.70           C  
-HETATM 9925  O5' BVP B1500      50.614  34.685  64.504  1.00 44.26           O  
-HETATM 9926  P   BVP B1500      49.502  33.689  65.185  1.00 40.02           P  
-HETATM 9927  O1P BVP B1500      49.926  32.285  64.964  1.00 42.20           O  
-HETATM 9928  O2P BVP B1500      48.188  33.915  64.538  1.00 50.99           O  
-HETATM 9929  O3P BVP B1500      49.386  33.959  66.617  1.00 39.83           O  
-HETATM 9930  N1  BVP B1500      54.197  31.669  61.910  1.00 26.69           N  
-HETATM 9931  C6  BVP B1500      54.165  31.247  63.244  1.00 30.59           C  
-HETATM 9932  C5  BVP B1500      55.020  30.163  63.696  1.00 35.26           C  
-HETATM 9933  C5A BVP B1500      55.143  29.666  64.719  1.00 39.19           C  
-HETATM 9934  C5B BVP B1500      55.864  30.122  65.801  1.00 54.37           C  
-HETATM 9935 BR   BVP B1500      56.354  28.990  67.321  1.00 74.72          BR  
-HETATM 9936  C4  BVP B1500      55.901  29.549  62.692  1.00 37.72           C  
-HETATM 9937  O4  BVP B1500      56.694  28.602  62.928  1.00 53.69           O  
-HETATM 9938  N3  BVP B1500      55.855  30.039  61.397  1.00 30.80           N  
-HETATM 9939  C2  BVP B1500      55.044  31.060  60.987  1.00 32.90           C  
-HETATM 9940  O2  BVP B1500      55.089  31.405  59.811  1.00 41.44           O  
-HETATM 9941  PB  ADP C2400      50.084   8.345  16.792  1.00 99.52           P  
-HETATM 9942  O1B ADP C2400      49.972   9.511  17.693  1.00 91.16           O  
-HETATM 9943  O2B ADP C2400      50.481   8.772  15.437  1.00 99.07           O  
-HETATM 9944  O3B ADP C2400      51.075   7.405  17.342  1.00100.23           O  
-HETATM 9945  PA  ADP C2400      48.240   6.252  16.302  1.00 84.52           P  
-HETATM 9946  O1A ADP C2400      48.019   6.209  14.841  1.00 90.64           O  
-HETATM 9947  O2A ADP C2400      49.086   5.122  16.772  1.00 91.53           O  
-HETATM 9948  O3A ADP C2400      48.795   7.575  16.761  1.00 95.32           O  
-HETATM 9949  O5' ADP C2400      46.788   6.091  17.005  1.00 92.46           O  
-HETATM 9950  C5' ADP C2400      46.565   5.251  18.175  1.00104.71           C  
-HETATM 9951  C4' ADP C2400      45.432   4.213  17.941  1.00109.78           C  
-HETATM 9952  O4' ADP C2400      44.129   4.892  17.786  1.00110.90           O  
-HETATM 9953  C3' ADP C2400      45.637   3.419  16.667  1.00113.22           C  
-HETATM 9954  O3' ADP C2400      46.231   2.161  17.019  1.00110.76           O  
-HETATM 9955  C2' ADP C2400      44.268   3.252  16.045  1.00116.03           C  
-HETATM 9956  O2' ADP C2400      43.726   1.945  16.244  1.00122.03           O  
-HETATM 9957  C1' ADP C2400      43.371   4.345  16.644  1.00113.75           C  
-HETATM 9958  N9  ADP C2400      43.035   5.430  15.651  1.00113.88           N  
-HETATM 9959  C8  ADP C2400      43.887   6.274  14.943  1.00113.52           C  
-HETATM 9960  N7  ADP C2400      43.265   7.114  14.159  1.00110.73           N  
-HETATM 9961  C5  ADP C2400      41.920   6.884  14.292  1.00112.23           C  
-HETATM 9962  C6  ADP C2400      40.747   7.461  13.717  1.00113.12           C  
-HETATM 9963  N6  ADP C2400      40.809   8.469  12.823  1.00111.60           N  
-HETATM 9964  N1  ADP C2400      39.519   6.950  14.106  1.00116.73           N  
-HETATM 9965  C2  ADP C2400      39.462   5.938  15.006  1.00117.86           C  
-HETATM 9966  N3  ADP C2400      40.495   5.310  15.621  1.00117.13           N  
-HETATM 9967  C4  ADP C2400      41.742   5.814  15.239  1.00114.32           C  
-HETATM 9968  O3' BVP C2500      54.657   7.483  24.088  1.00 33.81           O  
-HETATM 9969  C3' BVP C2500      54.877   8.317  22.954  1.00 28.55           C  
-HETATM 9970  C2' BVP C2500      55.359   9.710  23.311  1.00 25.63           C  
-HETATM 9971  C1' BVP C2500      56.846   9.466  23.551  1.00 23.42           C  
-HETATM 9972  O4' BVP C2500      57.212   8.332  22.738  1.00 25.54           O  
-HETATM 9973  C4' BVP C2500      56.022   7.725  22.176  1.00 27.79           C  
-HETATM 9974  C5' BVP C2500      56.015   8.008  20.653  1.00 30.42           C  
-HETATM 9975  O5' BVP C2500      54.774   7.569  20.032  1.00 44.08           O  
-HETATM 9976  P   BVP C2500      53.784   8.555  19.171  1.00 42.06           P  
-HETATM 9977  O1P BVP C2500      54.146   9.964  19.458  1.00 43.73           O  
-HETATM 9978  O2P BVP C2500      52.366   8.318  19.577  1.00 48.12           O  
-HETATM 9979  O3P BVP C2500      53.940   8.284  17.745  1.00 40.36           O  
-HETATM 9980  N1  BVP C2500      57.803  10.614  23.218  1.00 23.56           N  
-HETATM 9981  C6  BVP C2500      57.992  11.043  21.904  1.00 25.19           C  
-HETATM 9982  C5  BVP C2500      58.903  12.131  21.608  1.00 31.65           C  
-HETATM 9983  C5A BVP C2500      59.195  12.629  20.625  1.00 42.31           C  
-HETATM 9984  C5B BVP C2500      60.118  12.165  19.700  1.00 62.40           C  
-HETATM 9985 BR   BVP C2500      60.878  13.261  18.262  1.00 86.49          BR  
-HETATM 9986  C4  BVP C2500      59.600  12.741  22.738  1.00 35.83           C  
-HETATM 9987  O4  BVP C2500      60.417  13.693  22.632  1.00 50.13           O  
-HETATM 9988  N3  BVP C2500      59.344  12.244  24.007  1.00 26.37           N  
-HETATM 9989  C2  BVP C2500      58.483  11.218  24.270  1.00 27.95           C  
-HETATM 9990  O2  BVP C2500      58.336  10.865  25.429  1.00 36.33           O  
-HETATM 9991  PB  ADP D3400      93.096  23.841  34.570  1.00 94.78           P  
-HETATM 9992  O1B ADP D3400      93.089  22.410  34.195  1.00 90.99           O  
-HETATM 9993  O2B ADP D3400      93.285  24.699  33.387  1.00 95.64           O  
-HETATM 9994  O3B ADP D3400      91.830  24.174  35.237  1.00 97.60           O  
-HETATM 9995  PA  ADP D3400      94.574  25.161  36.566  1.00 97.77           P  
-HETATM 9996  O1A ADP D3400      95.285  26.283  35.905  1.00 96.59           O  
-HETATM 9997  O2A ADP D3400      93.428  25.630  37.392  1.00101.90           O  
-HETATM 9998  O3A ADP D3400      94.145  24.098  35.593  1.00 94.90           O  
-HETATM 9999  O5' ADP D3400      95.631  24.455  37.580  1.00100.92           O  
-HETATM10000  C5' ADP D3400      95.273  24.014  38.923  1.00108.85           C  
-HETATM10001  C4' ADP D3400      96.218  24.613  39.997  1.00115.18           C  
-HETATM10002  O4' ADP D3400      97.587  24.072  39.845  1.00117.41           O  
-HETATM10003  C3' ADP D3400      96.349  26.120  39.871  1.00116.26           C  
-HETATM10004  O3' ADP D3400      95.463  26.721  40.831  1.00115.11           O  
-HETATM10005  C2' ADP D3400      97.798  26.447  40.153  1.00118.51           C  
-HETATM10006  O2' ADP D3400      97.992  26.992  41.464  1.00118.10           O  
-HETATM10007  C1' ADP D3400      98.600  25.145  39.937  1.00119.05           C  
-HETATM10008  N9  ADP D3400      99.463  25.177  38.697  1.00118.05           N  
-HETATM10009  C8  ADP D3400      99.084  25.360  37.368  1.00116.87           C  
-HETATM10010  N7  ADP D3400     100.084  25.332  36.526  1.00116.44           N  
-HETATM10011  C5  ADP D3400     101.235  25.121  37.256  1.00116.75           C  
-HETATM10012  C6  ADP D3400     102.622  24.996  36.925  1.00115.23           C  
-HETATM10013  N6  ADP D3400     103.062  25.076  35.648  1.00115.39           N  
-HETATM10014  N1  ADP D3400     103.521  24.784  37.963  1.00112.82           N  
-HETATM10015  C2  ADP D3400     103.074  24.703  39.237  1.00111.52           C  
-HETATM10016  N3  ADP D3400     101.798  24.804  39.680  1.00113.46           N  
-HETATM10017  C4  ADP D3400     100.874  25.020  38.646  1.00116.76           C  
-HETATM10018  O3' BVP D3500      86.130  19.601  37.457  1.00 15.44           O  
-HETATM10019  C3' BVP D3500      86.469  20.018  36.144  1.00 13.53           C  
-HETATM10020  C2' BVP D3500      86.146  18.996  35.080  1.00 15.92           C  
-HETATM10021  C1' BVP D3500      84.656  19.222  34.887  1.00 17.46           C  
-HETATM10022  O4' BVP D3500      84.417  20.602  35.202  1.00 13.67           O  
-HETATM10023  C4' BVP D3500      85.593  21.176  35.810  1.00 14.56           C  
-HETATM10024  C5' BVP D3500      86.185  22.182  34.816  1.00 33.34           C  
-HETATM10025  O5' BVP D3500      87.480  22.665  35.253  1.00 51.89           O  
-HETATM10026  P   BVP D3500      88.856  22.500  34.359  1.00 58.07           P  
-HETATM10027  O1P BVP D3500      88.631  21.472  33.316  1.00 45.87           O  
-HETATM10028  O2P BVP D3500      89.972  22.074  35.257  1.00 59.17           O  
-HETATM10029  O3P BVP D3500      89.206  23.777  33.720  1.00 54.07           O  
-HETATM10030  N1  BVP D3500      84.089  18.942  33.496  1.00 21.08           N  
-HETATM10031  C6  BVP D3500      84.439  19.727  32.410  1.00 29.66           C  
-HETATM10032  C5  BVP D3500      83.896  19.447  31.094  1.00 35.68           C  
-HETATM10033  C5A BVP D3500      84.060  19.957  30.089  1.00 48.86           C  
-HETATM10034  C5B BVP D3500      83.504  21.135  29.638  1.00 58.77           C  
-HETATM10035 BR   BVP D3500      83.582  21.685  27.765  1.00 98.98          BR  
-HETATM10036  C4  BVP D3500      82.978  18.309  30.975  1.00 28.94           C  
-HETATM10037  O4  BVP D3500      82.428  17.937  29.913  1.00 43.27           O  
-HETATM10038  N3  BVP D3500      82.696  17.595  32.107  1.00 22.06           N  
-HETATM10039  C2  BVP D3500      83.214  17.867  33.342  1.00 30.06           C  
-HETATM10040  O2  BVP D3500      82.885  17.146  34.280  1.00 42.26           O  
-HETATM10041  O   HOH A 600      80.536  28.154  56.202  1.00 10.17           O  
-HETATM10042  O   HOH A 601      77.235  17.419  60.464  1.00 12.05           O  
-CONECT 9860 9861 9862 9863 9867                                                 
-CONECT 9861 9860                                                                
-CONECT 9862 9860                                                                
-CONECT 9863 9860                                                                
-CONECT 9864 9865 9866 9867                                                      
-CONECT 9865 9864                                                                
-CONECT 9866 9864                                                                
-CONECT 9867 9860 9864                                                           
-CONECT 9868 9869                                                                
-CONECT 9869 9868 9870 9873                                                      
-CONECT 9870 9869 9871                                                           
-CONECT 9871 9870 9872 9880                                                      
-CONECT 9872 9871 9873                                                           
-CONECT 9873 9869 9872 9874                                                      
-CONECT 9874 9873 9875                                                           
-CONECT 9875 9874 9876                                                           
-CONECT 9876 9875 9877 9878 9879                                                 
-CONECT 9877 9876                                                                
-CONECT 9878 9876                                                                
-CONECT 9879 9876                                                                
-CONECT 9880 9871 9881 9889                                                      
-CONECT 9881 9880 9882                                                           
-CONECT 9882 9881 9883 9886                                                      
-CONECT 9883 9882 9884                                                           
-CONECT 9884 9883 9885                                                           
-CONECT 9885 9884                                                                
-CONECT 9886 9882 9887 9888                                                      
-CONECT 9887 9886                                                                
-CONECT 9888 9886 9889                                                           
-CONECT 9889 9880 9888 9890                                                      
-CONECT 9890 9889                                                                
-CONECT 9891 9892 9893 9894 9898                                                 
-CONECT 9892 9891                                                                
-CONECT 9893 9891                                                                
-CONECT 9894 9891                                                                
-CONECT 9895 9896 9897 9898 9899                                                 
-CONECT 9896 9895                                                                
-CONECT 9897 9895                                                                
-CONECT 9898 9891 9895                                                           
-CONECT 9899 9895 9900                                                           
-CONECT 9900 9899 9901                                                           
-CONECT 9901 9900 9902 9903                                                      
-CONECT 9902 9901 9907                                                           
-CONECT 9903 9901 9904 9905                                                      
-CONECT 9904 9903                                                                
-CONECT 9905 9903 9906 9907                                                      
-CONECT 9906 9905                                                                
-CONECT 9907 9902 9905 9908                                                      
-CONECT 9908 9907 9909 9917                                                      
-CONECT 9909 9908 9910                                                           
-CONECT 9910 9909 9911                                                           
-CONECT 9911 9910 9912 9917                                                      
-CONECT 9912 9911 9913 9914                                                      
-CONECT 9913 9912                                                                
-CONECT 9914 9912 9915                                                           
-CONECT 9915 9914 9916                                                           
-CONECT 9916 9915 9917                                                           
-CONECT 9917 9908 9911 9916                                                      
-CONECT 9918 9919                                                                
-CONECT 9919 9918 9920 9923                                                      
-CONECT 9920 9919 9921                                                           
-CONECT 9921 9920 9922 9930                                                      
-CONECT 9922 9921 9923                                                           
-CONECT 9923 9919 9922 9924                                                      
-CONECT 9924 9923 9925                                                           
-CONECT 9925 9924 9926                                                           
-CONECT 9926 9925 9927 9928 9929                                                 
-CONECT 9927 9926                                                                
-CONECT 9928 9926                                                                
-CONECT 9929 9926                                                                
-CONECT 9930 9921 9931 9939                                                      
-CONECT 9931 9930 9932                                                           
-CONECT 9932 9931 9933 9936                                                      
-CONECT 9933 9932 9934                                                           
-CONECT 9934 9933 9935                                                           
-CONECT 9935 9934                                                                
-CONECT 9936 9932 9937 9938                                                      
-CONECT 9937 9936                                                                
-CONECT 9938 9936 9939                                                           
-CONECT 9939 9930 9938 9940                                                      
-CONECT 9940 9939                                                                
-CONECT 9941 9942 9943 9944 9948                                                 
-CONECT 9942 9941                                                                
-CONECT 9943 9941                                                                
-CONECT 9944 9941                                                                
-CONECT 9945 9946 9947 9948 9949                                                 
-CONECT 9946 9945                                                                
-CONECT 9947 9945                                                                
-CONECT 9948 9941 9945                                                           
-CONECT 9949 9945 9950                                                           
-CONECT 9950 9949 9951                                                           
-CONECT 9951 9950 9952 9953                                                      
-CONECT 9952 9951 9957                                                           
-CONECT 9953 9951 9954 9955                                                      
-CONECT 9954 9953                                                                
-CONECT 9955 9953 9956 9957                                                      
-CONECT 9956 9955                                                                
-CONECT 9957 9952 9955 9958                                                      
-CONECT 9958 9957 9959 9967                                                      
-CONECT 9959 9958 9960                                                           
-CONECT 9960 9959 9961                                                           
-CONECT 9961 9960 9962 9967                                                      
-CONECT 9962 9961 9963 9964                                                      
-CONECT 9963 9962                                                                
-CONECT 9964 9962 9965                                                           
-CONECT 9965 9964 9966                                                           
-CONECT 9966 9965 9967                                                           
-CONECT 9967 9958 9961 9966                                                      
-CONECT 9968 9969                                                                
-CONECT 9969 9968 9970 9973                                                      
-CONECT 9970 9969 9971                                                           
-CONECT 9971 9970 9972 9980                                                      
-CONECT 9972 9971 9973                                                           
-CONECT 9973 9969 9972 9974                                                      
-CONECT 9974 9973 9975                                                           
-CONECT 9975 9974 9976                                                           
-CONECT 9976 9975 9977 9978 9979                                                 
-CONECT 9977 9976                                                                
-CONECT 9978 9976                                                                
-CONECT 9979 9976                                                                
-CONECT 9980 9971 9981 9989                                                      
-CONECT 9981 9980 9982                                                           
-CONECT 9982 9981 9983 9986                                                      
-CONECT 9983 9982 9984                                                           
-CONECT 9984 9983 9985                                                           
-CONECT 9985 9984                                                                
-CONECT 9986 9982 9987 9988                                                      
-CONECT 9987 9986                                                                
-CONECT 9988 9986 9989                                                           
-CONECT 9989 9980 9988 9990                                                      
-CONECT 9990 9989                                                                
-CONECT 9991 9992 9993 9994 9998                                                 
-CONECT 9992 9991                                                                
-CONECT 9993 9991                                                                
-CONECT 9994 9991                                                                
-CONECT 9995 9996 9997 9998 9999                                                 
-CONECT 9996 9995                                                                
-CONECT 9997 9995                                                                
-CONECT 9998 9991 9995                                                           
-CONECT 9999 999510000                                                           
-CONECT10000 999910001                                                           
-CONECT10001100001000210003                                                      
-CONECT100021000110007                                                           
-CONECT10003100011000410005                                                      
-CONECT1000410003                                                                
-CONECT10005100031000610007                                                      
-CONECT1000610005                                                                
-CONECT10007100021000510008                                                      
-CONECT10008100071000910017                                                      
-CONECT100091000810010                                                           
-CONECT100101000910011                                                           
-CONECT10011100101001210017                                                      
-CONECT10012100111001310014                                                      
-CONECT1001310012                                                                
-CONECT100141001210015                                                           
-CONECT100151001410016                                                           
-CONECT100161001510017                                                           
-CONECT10017100081001110016                                                      
-CONECT1001810019                                                                
-CONECT10019100181002010023                                                      
-CONECT100201001910021                                                           
-CONECT10021100201002210030                                                      
-CONECT100221002110023                                                           
-CONECT10023100191002210024                                                      
-CONECT100241002310025                                                           
-CONECT100251002410026                                                           
-CONECT1002610025100271002810029                                                 
-CONECT1002710026                                                                
-CONECT1002810026                                                                
-CONECT1002910026                                                                
-CONECT10030100211003110039                                                      
-CONECT100311003010032                                                           
-CONECT10032100311003310036                                                      
-CONECT100331003210034                                                           
-CONECT100341003310035                                                           
-CONECT1003510034                                                                
-CONECT10036100321003710038                                                      
-CONECT1003710036                                                                
-CONECT100381003610039                                                           
-CONECT10039100301003810040                                                      
-CONECT1004010039                                                                
-MASTER      477    0    8   86   36    0   27    610038    4  181  108          
-END                                                                             
diff --git a/plip/test/pdb/1p5e.pdb b/plip/test/pdb/1p5e.pdb
deleted file mode 100644
index ea484a7..0000000
--- a/plip/test/pdb/1p5e.pdb
+++ /dev/null
@@ -1,9844 +0,0 @@
-HEADER    CELL CYCLE                              26-APR-03   1P5E              
-TITLE     THE STRUCURE OF PHOSPHO-CDK2/CYCLIN A IN COMPLEX WITH THE             
-TITLE    2 INHIBITOR 4,5,6,7-TETRABROMOBENZOTRIAZOLE (TBS)                      
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
-COMPND   3 CHAIN: A, C;                                                         
-COMPND   4 SYNONYM: P33 PROTEIN KINASE;                                         
-COMPND   5 EC: 2.7.1.-;                                                         
-COMPND   6 ENGINEERED: YES;                                                     
-COMPND   7 MOL_ID: 2;                                                           
-COMPND   8 MOLECULE: CYCLIN A2;                                                 
-COMPND   9 CHAIN: B, D;                                                         
-COMPND  10 FRAGMENT: RESIDUES 175-432;                                          
-COMPND  11 SYNONYM: CYCLIN A;                                                   
-COMPND  12 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: CDK2;                                                          
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834 (DE3) PLYSS;                          
-SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX 3C;                                  
-SOURCE  11 MOL_ID: 2;                                                           
-SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
-SOURCE  14 ORGANISM_TAXID: 9606;                                                
-SOURCE  15 GENE: CCNA2 OR CCNA OR CCN1;                                         
-SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE  18 EXPRESSION_SYSTEM_STRAIN: B834 (DE3) PLYSS;                          
-SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET21D                                    
-KEYWDS    KINASE INHIBITOR, CDK2, TBS, CELL CYCLE                               
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    E.DE MOLINER,N.R.BROWN,L.N.JOHNSON                                    
-REVDAT   2   24-FEB-09 1P5E    1       VERSN                                    
-REVDAT   1   01-JUL-03 1P5E    0                                                
-JRNL        AUTH   E.DE MOLINER,N.R.BROWN,L.N.JOHNSON                           
-JRNL        TITL   ALTERNATIVE BINDING MODES OF AN INHIBITOR TO TWO             
-JRNL        TITL 2 DIFFERENT KINASES                                            
-JRNL        REF    EUR.J.BIOCHEM.                V. 270     1 2003              
-JRNL        REFN                   ISSN 0014-2956                               
-JRNL        PMID   12869192                                                     
-JRNL        DOI    10.1046/J.1432-1033.2003.03697.X                             
-REMARK   1                                                                      
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.22 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS 1.0                                              
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.97                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.8                           
-REMARK   3   NUMBER OF REFLECTIONS             : 62398                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.219                           
-REMARK   3   FREE R VALUE                     : 0.257                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.200                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 5557                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.22                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.80                        
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8571                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
-REMARK   3   BIN FREE R VALUE                    : 0.2940                       
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.30                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 778                          
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 8946                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 26                                      
-REMARK   3   SOLVENT ATOMS            : 242                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 30.80                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.20                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -0.53000                                             
-REMARK   3    B22 (A**2) : 0.03000                                              
-REMARK   3    B33 (A**2) : 0.50000                                              
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.22                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.32                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.006                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.40                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.98                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.370 ; 1.500                
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.250 ; 2.000                
-REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.190 ; 2.000                
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.200 ; 2.500                
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : FLAT MODEL                                           
-REMARK   3   KSOL        : 0.39                                                 
-REMARK   3   BSOL        : 34.74                                                
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
-REMARK   3  PARAMETER FILE  2  : TBB.PARAM                                      
-REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
-REMARK   3  PARAMETER FILE  4  : TPO.PARAM                                      
-REMARK   3  PARAMETER FILE  5  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
-REMARK   3  TOPOLOGY FILE  2   : TBB.TOP                                        
-REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
-REMARK   3  TOPOLOGY FILE  4   : NULL                                           
-REMARK   3  TOPOLOGY FILE  5   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1P5E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-03.                  
-REMARK 100 THE RCSB ID CODE IS RCSB019028.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 29-APR-01                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 7                                  
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ESRF                               
-REMARK 200  BEAMLINE                       : ID14-1                             
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
-REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
-REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72014                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 46.970                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
-REMARK 200  DATA REDUNDANCY                : 2.800                              
-REMARK 200  R MERGE                    (I) : 0.07400                            
-REMARK 200  R SYM                      (I) : 0.05400                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 2.22                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.33400                            
-REMARK 200  R SYM FOR SHELL            (I) : 0.23200                            
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: CNS                                                   
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 57.06                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML PCDK2/CYCLIN A, 0.5 MM          
-REMARK 280  TBS, 1.25 M AMMONIUM SULPHATE, 0.85 M KCL, HEPES 100MM, PH 7,       
-REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.76800            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.21200            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.97350            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.21200            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.76800            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.97350            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2                                                    
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 3780 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 22980 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 3840 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 23430 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     ARG A   297                                                      
-REMARK 465     LEU A   298                                                      
-REMARK 465     ARG C   297                                                      
-REMARK 465     LEU C   298                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   O    SER A    94     O    THR A    97              2.12            
-REMARK 500   OG   SER B   245     O    HOH B   502              2.14            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASP A  38      119.74     52.28                                   
-REMARK 500    GLU A  40     -145.98    -92.80                                   
-REMARK 500    THR A  41     -103.29     56.81                                   
-REMARK 500    GLU A  73       75.65     33.54                                   
-REMARK 500    LEU A  96      -93.03    -59.43                                   
-REMARK 500    ASP A 127       45.49   -158.40                                   
-REMARK 500    ASP A 145       86.25     61.34                                   
-REMARK 500    VAL A 164      127.96     83.55                                   
-REMARK 500    SER A 181     -147.70   -140.18                                   
-REMARK 500    LYS A 291       74.84   -118.48                                   
-REMARK 500    TRP B 372      112.41    -33.63                                   
-REMARK 500    GLU C  12     -104.99   -167.09                                   
-REMARK 500    TYR C  15      -36.20     59.39                                   
-REMARK 500    THR C  41     -103.69    119.30                                   
-REMARK 500    ASP C 127       46.37   -144.94                                   
-REMARK 500    ASP C 145       79.27     54.43                                   
-REMARK 500    VAL C 164      126.73     70.48                                   
-REMARK 500    SER C 181     -147.06   -153.74                                   
-REMARK 500    PRO C 222       99.55    -55.53                                   
-REMARK 500    PRO C 238       35.08    -78.32                                   
-REMARK 500    PHE C 240      -62.10   -148.20                                   
-REMARK 500    PRO C 241      179.92    -57.98                                   
-REMARK 500    LYS C 242     -142.20     92.57                                   
-REMARK 500    TRP C 243     -142.60     41.15                                   
-REMARK 500    ALA C 244     -165.64     77.80                                   
-REMARK 500    ARG C 245     -162.01   -166.05                                   
-REMARK 500    GLN C 246      105.16     45.62                                   
-REMARK 500    PHE C 248       91.93    -57.92                                   
-REMARK 500    SER C 249      -46.77   -165.04                                   
-REMARK 500    ASP D 283     -111.17     64.98                                   
-REMARK 500    HIS D 321       30.77    -99.47                                   
-REMARK 500    TRP D 372      106.91    -37.39                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBS A 301                 
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBS C 302                 
-DBREF  1P5E A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
-DBREF  1P5E B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
-DBREF  1P5E C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
-DBREF  1P5E D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
-SEQADV 1P5E SER A    0  UNP  P24941              CLONING ARTIFACT               
-SEQADV 1P5E TPO A  160  UNP  P24941    THR   160 MODIFIED RESIDUE               
-SEQADV 1P5E SER C    0  UNP  P24941              CLONING ARTIFACT               
-SEQADV 1P5E TPO C  160  UNP  P24941    THR   160 MODIFIED RESIDUE               
-SEQRES   1 A  299  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
-SEQRES   2 A  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
-SEQRES   3 A  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
-SEQRES   4 A  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
-SEQRES   5 A  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
-SEQRES   6 A  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
-SEQRES   7 A  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
-SEQRES   8 A  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
-SEQRES   9 A  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
-SEQRES  10 A  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
-SEQRES  11 A  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
-SEQRES  12 A  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
-SEQRES  13 A  299  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
-SEQRES  14 A  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
-SEQRES  15 A  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
-SEQRES  16 A  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
-SEQRES  17 A  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
-SEQRES  18 A  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
-SEQRES  19 A  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
-SEQRES  20 A  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
-SEQRES  21 A  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
-SEQRES  22 A  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
-SEQRES  23 A  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
-SEQRES   1 B  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
-SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
-SEQRES   3 B  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
-SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
-SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
-SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
-SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
-SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
-SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
-SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
-SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
-SEQRES  12 B  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
-SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
-SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
-SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
-SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
-SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
-SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
-SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
-SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
-SEQRES   1 C  299  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
-SEQRES   2 C  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
-SEQRES   3 C  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
-SEQRES   4 C  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
-SEQRES   5 C  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
-SEQRES   6 C  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
-SEQRES   7 C  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
-SEQRES   8 C  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
-SEQRES   9 C  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
-SEQRES  10 C  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
-SEQRES  11 C  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
-SEQRES  12 C  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
-SEQRES  13 C  299  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
-SEQRES  14 C  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
-SEQRES  15 C  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
-SEQRES  16 C  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
-SEQRES  17 C  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
-SEQRES  18 C  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
-SEQRES  19 C  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
-SEQRES  20 C  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
-SEQRES  21 C  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
-SEQRES  22 C  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
-SEQRES  23 C  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
-SEQRES   1 D  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
-SEQRES   2 D  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
-SEQRES   3 D  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
-SEQRES   4 D  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
-SEQRES   5 D  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
-SEQRES   6 D  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
-SEQRES   7 D  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
-SEQRES   8 D  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
-SEQRES   9 D  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
-SEQRES  10 D  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
-SEQRES  11 D  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
-SEQRES  12 D  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
-SEQRES  13 D  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
-SEQRES  14 D  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
-SEQRES  15 D  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
-SEQRES  16 D  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
-SEQRES  17 D  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
-SEQRES  18 D  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
-SEQRES  19 D  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
-SEQRES  20 D  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
-MODRES 1P5E TPO A  160  THR  PHOSPHOTHREONINE                                   
-MODRES 1P5E TPO C  160  THR  PHOSPHOTHREONINE                                   
-HET    TPO  A 160      11                                                       
-HET    TPO  C 160      11                                                       
-HET    TBS  A 301      13                                                       
-HET    TBS  C 302      13                                                       
-HETNAM     TPO PHOSPHOTHREONINE                                                 
-HETNAM     TBS 4,5,6,7-TETRABROMOBENZOTRIAZOLE                                  
-HETSYN     TPO PHOSPHONOTHREONINE                                               
-HETSYN     TBS TETRABROMO-2-BENZOTRIAZOLE                                       
-FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
-FORMUL   5  TBS    2(C6 H BR4 N3)                                               
-FORMUL   7  HOH   *242(H2 O)                                                    
-HELIX    1   1 SER A    0  GLU A    2  5                                   3    
-HELIX    2   2 PRO A   45  LYS A   56  1                                  12    
-HELIX    3   3 LEU A   87  SER A   94  1                                   8    
-HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
-HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
-HELIX    6   6 THR A  165  ARG A  169  5                                   5    
-HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
-HELIX    8   8 THR A  182  ARG A  199  1                                  18    
-HELIX    9   9 SER A  207  GLY A  220  1                                  14    
-HELIX   10  10 GLY A  229  MET A  233  5                                   5    
-HELIX   11  11 ASP A  247  VAL A  251  5                                   5    
-HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
-HELIX   13  13 SER A  276  LEU A  281  1                                   6    
-HELIX   14  14 ALA A  282  GLN A  287  5                                   6    
-HELIX   15  15 VAL B  175  ASP B  177  5                                   3    
-HELIX   16  16 TYR B  178  CYS B  193  1                                  16    
-HELIX   17  17 GLY B  198  GLN B  203  5                                   6    
-HELIX   18  18 THR B  207  TYR B  225  1                                  19    
-HELIX   19  19 GLN B  228  MET B  246  1                                  19    
-HELIX   20  20 LEU B  249  GLY B  251  5                                   3    
-HELIX   21  21 LYS B  252  GLU B  269  1                                  18    
-HELIX   22  22 GLU B  274  THR B  282  1                                   9    
-HELIX   23  23 THR B  287  LEU B  302  1                                  16    
-HELIX   24  24 THR B  310  PHE B  319  1                                  10    
-HELIX   25  25 LEU B  320  GLN B  322  5                                   3    
-HELIX   26  26 ASN B  326  SER B  340  1                                  15    
-HELIX   27  27 ASP B  343  LEU B  348  1                                   6    
-HELIX   28  28 LEU B  351  GLY B  369  1                                  19    
-HELIX   29  29 PRO B  373  GLY B  381  1                                   9    
-HELIX   30  30 THR B  383  ALA B  401  1                                  19    
-HELIX   31  31 PRO B  402  HIS B  404  5                                   3    
-HELIX   32  32 GLN B  407  TYR B  413  1                                   7    
-HELIX   33  33 LYS B  414  HIS B  419  5                                   6    
-HELIX   34  34 GLY B  420  LEU B  424  5                                   5    
-HELIX   35  35 PRO C   45  LEU C   58  1                                  14    
-HELIX   36  36 LEU C   87  SER C   94  1                                   8    
-HELIX   37  37 PRO C  100  HIS C  121  1                                  22    
-HELIX   38  38 LYS C  129  GLN C  131  5                                   3    
-HELIX   39  39 THR C  165  ARG C  169  5                                   5    
-HELIX   40  40 ALA C  170  LEU C  175  1                                   6    
-HELIX   41  41 THR C  182  ARG C  199  1                                  18    
-HELIX   42  42 SER C  207  GLY C  220  1                                  14    
-HELIX   43  43 ASP C  256  LEU C  267  1                                  12    
-HELIX   44  44 SER C  276  LEU C  281  1                                   6    
-HELIX   45  45 ALA C  282  GLN C  287  5                                   6    
-HELIX   46  46 VAL D  175  ASP D  177  5                                   3    
-HELIX   47  47 TYR D  178  CYS D  193  1                                  16    
-HELIX   48  48 TYR D  199  GLN D  203  5                                   5    
-HELIX   49  49 THR D  207  TYR D  225  1                                  19    
-HELIX   50  50 GLN D  228  SER D  244  1                                  17    
-HELIX   51  51 LEU D  249  GLU D  269  1                                  21    
-HELIX   52  52 GLU D  274  THR D  282  1                                   9    
-HELIX   53  53 THR D  287  LEU D  302  1                                  16    
-HELIX   54  54 THR D  310  PHE D  319  1                                  10    
-HELIX   55  55 LEU D  320  GLN D  322  5                                   3    
-HELIX   56  56 ASN D  326  ASP D  343  1                                  18    
-HELIX   57  57 ASP D  343  LEU D  348  1                                   6    
-HELIX   58  58 LEU D  351  THR D  368  1                                  18    
-HELIX   59  59 PRO D  373  GLY D  381  1                                   9    
-HELIX   60  60 LEU D  387  ALA D  401  1                                  15    
-HELIX   61  61 GLN D  407  TYR D  413  1                                   7    
-HELIX   62  62 LYS D  414  HIS D  419  5                                   6    
-HELIX   63  63 GLY D  420  LEU D  424  5                                   5    
-SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
-SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  GLY A  11           
-SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
-SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
-SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  ILE A  70   O  TYR A  77           
-SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
-SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
-SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
-SHEET    1   C 2 VAL A 123  LEU A 124  0                                        
-SHEET    2   C 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
-SHEET    1   D 5 PHE C   4  GLY C  11  0                                        
-SHEET    2   D 5 VAL C  18  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
-SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
-SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
-SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  ILE C  70   O  TYR C  77           
-SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
-SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
-SHEET    3   E 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
-SHEET    1   F 2 VAL C 123  LEU C 124  0                                        
-SHEET    2   F 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
-LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
-LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
-LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.33  
-LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
-CISPEP   1 VAL A  154    PRO A  155          0        -9.23                     
-CISPEP   2 GLN B  323    PRO B  324          0        -1.44                     
-CISPEP   3 ASP B  345    PRO B  346          0         2.69                     
-CISPEP   4 VAL C  154    PRO C  155          0        -2.34                     
-CISPEP   5 GLN D  323    PRO D  324          0        -6.99                     
-CISPEP   6 ASP D  345    PRO D  346          0         5.50                     
-SITE     1 AC1 10 ILE A  10  VAL A  18  ALA A  31  PHE A  80                    
-SITE     2 AC1 10 GLU A  81  LEU A  83  LEU A 134  HOH A 302                    
-SITE     3 AC1 10 HOH A 325  HOH A 399                                          
-SITE     1 AC2  9 VAL C  18  ALA C  31  PHE C  80  GLU C  81                    
-SITE     2 AC2  9 LEU C  83  LEU C 134  HOH C 303  HOH C 305                    
-SITE     3 AC2  9 HOH C 338                                                     
-CRYST1   73.536  133.947  148.424  90.00  90.00  90.00 P 21 21 21    8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.013599  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.007466  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.006737        0.00000                         
-ATOM      1  N   SER A   0      17.555  59.442  42.891  1.00 44.14           N  
-ATOM      2  CA  SER A   0      16.571  60.209  42.057  1.00 44.20           C  
-ATOM      3  C   SER A   0      15.440  59.313  41.582  1.00 43.90           C  
-ATOM      4  O   SER A   0      15.675  58.158  41.208  1.00 44.06           O  
-ATOM      5  CB  SER A   0      17.254  60.833  40.838  1.00 44.15           C  
-ATOM      6  OG  SER A   0      18.592  61.198  41.123  1.00 45.78           O  
-ATOM      7  N   MET A   1      14.223  59.854  41.580  1.00 43.33           N  
-ATOM      8  CA  MET A   1      13.051  59.131  41.094  1.00 43.03           C  
-ATOM      9  C   MET A   1      13.190  58.723  39.627  1.00 42.34           C  
-ATOM     10  O   MET A   1      12.684  57.675  39.220  1.00 42.21           O  
-ATOM     11  CB  MET A   1      11.789  59.965  41.289  1.00 43.37           C  
-ATOM     12  CG  MET A   1      10.726  59.332  42.173  1.00 45.22           C  
-ATOM     13  SD  MET A   1      11.340  58.128  43.378  1.00 49.84           S  
-ATOM     14  CE  MET A   1      10.580  56.681  42.730  1.00 49.04           C  
-ATOM     15  N   GLU A   2      13.899  59.545  38.856  1.00 41.41           N  
-ATOM     16  CA  GLU A   2      14.131  59.305  37.435  1.00 40.88           C  
-ATOM     17  C   GLU A   2      14.713  57.923  37.125  1.00 39.90           C  
-ATOM     18  O   GLU A   2      14.348  57.315  36.121  1.00 39.78           O  
-ATOM     19  CB  GLU A   2      15.031  60.400  36.847  1.00 41.12           C  
-ATOM     20  CG  GLU A   2      15.296  60.276  35.343  1.00 43.26           C  
-ATOM     21  CD  GLU A   2      14.029  60.150  34.510  1.00 44.93           C  
-ATOM     22  OE1 GLU A   2      13.212  61.096  34.524  1.00 46.52           O  
-ATOM     23  OE2 GLU A   2      13.849  59.104  33.843  1.00 45.62           O  
-ATOM     24  N   ASN A   3      15.602  57.431  37.989  1.00 38.50           N  
-ATOM     25  CA  ASN A   3      16.263  56.150  37.764  1.00 37.37           C  
-ATOM     26  C   ASN A   3      15.392  54.929  38.047  1.00 36.42           C  
-ATOM     27  O   ASN A   3      15.822  53.796  37.825  1.00 36.28           O  
-ATOM     28  CB  ASN A   3      17.565  56.068  38.564  1.00 37.41           C  
-ATOM     29  CG  ASN A   3      18.656  56.954  37.995  1.00 38.11           C  
-ATOM     30  OD1 ASN A   3      19.564  57.390  38.716  1.00 37.41           O  
-ATOM     31  ND2 ASN A   3      18.582  57.221  36.690  1.00 38.58           N  
-ATOM     32  N   PHE A   4      14.172  55.160  38.521  1.00 35.28           N  
-ATOM     33  CA  PHE A   4      13.299  54.069  38.920  1.00 34.68           C  
-ATOM     34  C   PHE A   4      12.101  53.911  37.995  1.00 34.97           C  
-ATOM     35  O   PHE A   4      11.458  54.889  37.620  1.00 34.85           O  
-ATOM     36  CB  PHE A   4      12.840  54.243  40.371  1.00 33.98           C  
-ATOM     37  CG  PHE A   4      13.934  54.038  41.381  1.00 32.32           C  
-ATOM     38  CD1 PHE A   4      14.475  52.772  41.597  1.00 29.91           C  
-ATOM     39  CD2 PHE A   4      14.424  55.110  42.118  1.00 30.23           C  
-ATOM     40  CE1 PHE A   4      15.482  52.581  42.530  1.00 29.15           C  
-ATOM     41  CE2 PHE A   4      15.431  54.932  43.055  1.00 28.56           C  
-ATOM     42  CZ  PHE A   4      15.965  53.669  43.263  1.00 29.02           C  
-ATOM     43  N   GLN A   5      11.823  52.665  37.630  1.00 34.90           N  
-ATOM     44  CA  GLN A   5      10.661  52.331  36.830  1.00 35.21           C  
-ATOM     45  C   GLN A   5       9.700  51.508  37.679  1.00 35.08           C  
-ATOM     46  O   GLN A   5      10.023  50.388  38.077  1.00 34.55           O  
-ATOM     47  CB  GLN A   5      11.086  51.554  35.577  1.00 35.32           C  
-ATOM     48  CG  GLN A   5       9.948  50.950  34.771  1.00 37.25           C  
-ATOM     49  CD  GLN A   5       9.075  51.995  34.114  1.00 39.86           C  
-ATOM     50  OE1 GLN A   5       9.559  52.800  33.317  1.00 42.50           O  
-ATOM     51  NE2 GLN A   5       7.785  51.993  34.448  1.00 41.03           N  
-ATOM     52  N   LYS A   6       8.529  52.083  37.958  1.00 35.25           N  
-ATOM     53  CA  LYS A   6       7.484  51.411  38.725  1.00 35.72           C  
-ATOM     54  C   LYS A   6       6.908  50.245  37.933  1.00 35.74           C  
-ATOM     55  O   LYS A   6       6.710  50.338  36.718  1.00 35.89           O  
-ATOM     56  CB  LYS A   6       6.368  52.384  39.099  1.00 35.82           C  
-ATOM     57  CG  LYS A   6       6.733  53.356  40.200  1.00 37.05           C  
-ATOM     58  CD  LYS A   6       5.499  54.020  40.777  1.00 39.19           C  
-ATOM     59  CE  LYS A   6       5.812  55.436  41.216  1.00 41.52           C  
-ATOM     60  NZ  LYS A   6       4.571  56.168  41.622  1.00 44.66           N  
-ATOM     61  N   VAL A   7       6.640  49.150  38.639  1.00 35.63           N  
-ATOM     62  CA  VAL A   7       6.216  47.911  38.018  1.00 35.38           C  
-ATOM     63  C   VAL A   7       4.751  47.646  38.349  1.00 35.44           C  
-ATOM     64  O   VAL A   7       3.934  47.468  37.449  1.00 35.48           O  
-ATOM     65  CB  VAL A   7       7.116  46.726  38.462  1.00 35.56           C  
-ATOM     66  CG1 VAL A   7       6.659  45.425  37.830  1.00 35.48           C  
-ATOM     67  CG2 VAL A   7       8.584  46.999  38.122  1.00 35.47           C  
-ATOM     68  N   GLU A   8       4.430  47.628  39.641  1.00 35.31           N  
-ATOM     69  CA  GLU A   8       3.074  47.379  40.118  1.00 34.99           C  
-ATOM     70  C   GLU A   8       2.989  47.674  41.612  1.00 34.79           C  
-ATOM     71  O   GLU A   8       4.022  47.830  42.276  1.00 34.87           O  
-ATOM     72  CB  GLU A   8       2.663  45.925  39.845  1.00 35.23           C  
-ATOM     73  CG  GLU A   8       3.302  44.895  40.772  1.00 35.73           C  
-ATOM     74  CD  GLU A   8       3.205  43.472  40.254  1.00 38.13           C  
-ATOM     75  OE1 GLU A   8       3.049  43.267  39.022  1.00 39.80           O  
-ATOM     76  OE2 GLU A   8       3.293  42.546  41.085  1.00 39.28           O  
-ATOM     77  N   LYS A   9       1.767  47.726  42.136  1.00 34.22           N  
-ATOM     78  CA  LYS A   9       1.538  47.901  43.570  1.00 34.11           C  
-ATOM     79  C   LYS A   9       1.674  46.566  44.279  1.00 33.47           C  
-ATOM     80  O   LYS A   9       1.197  45.541  43.768  1.00 33.37           O  
-ATOM     81  CB  LYS A   9       0.152  48.499  43.819  1.00 34.24           C  
-ATOM     82  CG  LYS A   9      -0.175  48.758  45.276  1.00 35.21           C  
-ATOM     83  CD  LYS A   9      -1.660  48.580  45.548  1.00 37.07           C  
-ATOM     84  CE  LYS A   9      -2.021  49.056  46.951  1.00 38.53           C  
-ATOM     85  NZ  LYS A   9      -3.283  48.429  47.470  1.00 39.79           N  
-ATOM     86  N   ILE A  10       2.326  46.573  45.446  1.00 32.80           N  
-ATOM     87  CA  ILE A  10       2.563  45.335  46.210  1.00 32.49           C  
-ATOM     88  C   ILE A  10       2.109  45.375  47.675  1.00 33.20           C  
-ATOM     89  O   ILE A  10       2.094  44.347  48.363  1.00 33.16           O  
-ATOM     90  CB  ILE A  10       4.050  44.880  46.124  1.00 32.26           C  
-ATOM     91  CG1 ILE A  10       5.002  46.002  46.547  1.00 31.20           C  
-ATOM     92  CG2 ILE A  10       4.390  44.358  44.718  1.00 31.69           C  
-ATOM     93  CD1 ILE A  10       6.421  45.511  46.868  1.00 30.34           C  
-ATOM     94  N   GLY A  11       1.751  46.559  48.151  1.00 33.88           N  
-ATOM     95  CA  GLY A  11       1.241  46.719  49.498  1.00 34.97           C  
-ATOM     96  C   GLY A  11       0.821  48.148  49.734  1.00 36.08           C  
-ATOM     97  O   GLY A  11       0.820  48.962  48.807  1.00 36.20           O  
-ATOM     98  N   GLU A  12       0.470  48.453  50.978  1.00 37.19           N  
-ATOM     99  CA  GLU A  12       0.074  49.798  51.375  1.00 38.82           C  
-ATOM    100  C   GLU A  12       0.146  49.967  52.891  1.00 39.35           C  
-ATOM    101  O   GLU A  12      -0.002  49.001  53.644  1.00 39.43           O  
-ATOM    102  CB  GLU A  12      -1.329  50.155  50.844  1.00 38.95           C  
-ATOM    103  CG  GLU A  12      -2.451  49.256  51.340  1.00 41.27           C  
-ATOM    104  CD  GLU A  12      -3.791  49.544  50.677  1.00 44.62           C  
-ATOM    105  OE1 GLU A  12      -4.144  50.741  50.488  1.00 45.55           O  
-ATOM    106  OE2 GLU A  12      -4.502  48.565  50.356  1.00 45.80           O  
-ATOM    107  N   GLY A  13       0.394  51.201  53.322  1.00 40.03           N  
-ATOM    108  CA  GLY A  13       0.448  51.542  54.731  1.00 40.89           C  
-ATOM    109  C   GLY A  13      -0.498  52.691  55.018  1.00 41.50           C  
-ATOM    110  O   GLY A  13      -1.439  52.931  54.262  1.00 41.87           O  
-ATOM    111  N   THR A  14      -0.243  53.408  56.105  1.00 41.73           N  
-ATOM    112  CA  THR A  14      -1.082  54.533  56.495  1.00 42.22           C  
-ATOM    113  C   THR A  14      -0.894  55.750  55.586  1.00 42.33           C  
-ATOM    114  O   THR A  14      -1.860  56.451  55.284  1.00 42.63           O  
-ATOM    115  CB  THR A  14      -0.813  54.895  57.967  1.00 42.29           C  
-ATOM    116  OG1 THR A  14      -1.033  53.734  58.781  1.00 42.99           O  
-ATOM    117  CG2 THR A  14      -1.848  55.879  58.488  1.00 42.59           C  
-ATOM    118  N   TYR A  15       0.340  55.979  55.134  1.00 42.25           N  
-ATOM    119  CA  TYR A  15       0.692  57.217  54.433  1.00 42.21           C  
-ATOM    120  C   TYR A  15       1.002  57.041  52.945  1.00 41.72           C  
-ATOM    121  O   TYR A  15       1.572  57.931  52.309  1.00 41.74           O  
-ATOM    122  CB  TYR A  15       1.861  57.908  55.142  1.00 42.46           C  
-ATOM    123  CG  TYR A  15       1.510  58.381  56.532  1.00 43.45           C  
-ATOM    124  CD1 TYR A  15       0.822  59.573  56.726  1.00 44.66           C  
-ATOM    125  CD2 TYR A  15       1.855  57.629  57.653  1.00 44.83           C  
-ATOM    126  CE1 TYR A  15       0.490  60.011  58.002  1.00 45.32           C  
-ATOM    127  CE2 TYR A  15       1.524  58.056  58.938  1.00 45.07           C  
-ATOM    128  CZ  TYR A  15       0.842  59.250  59.101  1.00 45.44           C  
-ATOM    129  OH  TYR A  15       0.509  59.691  60.362  1.00 45.66           O  
-ATOM    130  N   GLY A  16       0.610  55.902  52.390  1.00 40.96           N  
-ATOM    131  CA  GLY A  16       0.857  55.636  50.990  1.00 39.91           C  
-ATOM    132  C   GLY A  16       0.952  54.160  50.673  1.00 39.06           C  
-ATOM    133  O   GLY A  16       0.956  53.302  51.554  1.00 38.95           O  
-ATOM    134  N   VAL A  17       1.018  53.867  49.386  1.00 38.24           N  
-ATOM    135  CA  VAL A  17       1.127  52.492  48.937  1.00 37.34           C  
-ATOM    136  C   VAL A  17       2.602  52.130  48.777  1.00 36.22           C  
-ATOM    137  O   VAL A  17       3.478  52.988  48.879  1.00 36.39           O  
-ATOM    138  CB  VAL A  17       0.338  52.265  47.628  1.00 37.51           C  
-ATOM    139  CG1 VAL A  17      -1.137  52.599  47.837  1.00 37.98           C  
-ATOM    140  CG2 VAL A  17       0.917  53.083  46.493  1.00 37.29           C  
-ATOM    141  N   VAL A  18       2.870  50.856  48.550  1.00 34.78           N  
-ATOM    142  CA  VAL A  18       4.220  50.399  48.276  1.00 33.42           C  
-ATOM    143  C   VAL A  18       4.216  49.836  46.862  1.00 32.71           C  
-ATOM    144  O   VAL A  18       3.342  49.044  46.517  1.00 31.96           O  
-ATOM    145  CB  VAL A  18       4.679  49.338  49.322  1.00 33.40           C  
-ATOM    146  CG1 VAL A  18       6.021  48.718  48.951  1.00 32.20           C  
-ATOM    147  CG2 VAL A  18       4.743  49.959  50.722  1.00 33.22           C  
-ATOM    148  N   TYR A  19       5.176  50.274  46.048  1.00 32.27           N  
-ATOM    149  CA  TYR A  19       5.356  49.755  44.691  1.00 32.07           C  
-ATOM    150  C   TYR A  19       6.593  48.889  44.529  1.00 30.81           C  
-ATOM    151  O   TYR A  19       7.670  49.211  45.046  1.00 30.41           O  
-ATOM    152  CB  TYR A  19       5.473  50.901  43.681  1.00 32.83           C  
-ATOM    153  CG  TYR A  19       4.199  51.662  43.473  1.00 36.66           C  
-ATOM    154  CD1 TYR A  19       3.158  51.121  42.725  1.00 39.79           C  
-ATOM    155  CD2 TYR A  19       4.028  52.925  44.030  1.00 40.25           C  
-ATOM    156  CE1 TYR A  19       1.976  51.820  42.532  1.00 42.39           C  
-ATOM    157  CE2 TYR A  19       2.849  53.634  43.837  1.00 42.77           C  
-ATOM    158  CZ  TYR A  19       1.831  53.072  43.092  1.00 43.23           C  
-ATOM    159  OH  TYR A  19       0.658  53.768  42.906  1.00 46.79           O  
-ATOM    160  N   LYS A  20       6.445  47.811  43.766  1.00 29.32           N  
-ATOM    161  CA  LYS A  20       7.600  47.162  43.171  1.00 28.25           C  
-ATOM    162  C   LYS A  20       8.136  48.088  42.083  1.00 27.81           C  
-ATOM    163  O   LYS A  20       7.370  48.590  41.263  1.00 27.68           O  
-ATOM    164  CB  LYS A  20       7.215  45.810  42.569  1.00 28.23           C  
-ATOM    165  CG  LYS A  20       8.383  45.028  41.964  1.00 27.53           C  
-ATOM    166  CD  LYS A  20       7.909  43.658  41.499  1.00 28.60           C  
-ATOM    167  CE  LYS A  20       9.056  42.774  41.057  1.00 29.53           C  
-ATOM    168  NZ  LYS A  20       8.549  41.426  40.637  1.00 33.31           N  
-ATOM    169  N   ALA A  21       9.443  48.332  42.094  1.00 27.14           N  
-ATOM    170  CA  ALA A  21      10.086  49.118  41.047  1.00 26.67           C  
-ATOM    171  C   ALA A  21      11.442  48.532  40.722  1.00 26.64           C  
-ATOM    172  O   ALA A  21      11.937  47.673  41.436  1.00 26.04           O  
-ATOM    173  CB  ALA A  21      10.238  50.550  41.464  1.00 26.40           C  
-ATOM    174  N   ARG A  22      12.034  48.994  39.629  1.00 27.00           N  
-ATOM    175  CA  ARG A  22      13.366  48.552  39.274  1.00 27.86           C  
-ATOM    176  C   ARG A  22      14.246  49.729  38.895  1.00 27.67           C  
-ATOM    177  O   ARG A  22      13.812  50.663  38.215  1.00 27.46           O  
-ATOM    178  CB  ARG A  22      13.342  47.469  38.184  1.00 28.06           C  
-ATOM    179  CG  ARG A  22      12.813  47.942  36.868  1.00 31.40           C  
-ATOM    180  CD  ARG A  22      13.164  47.074  35.675  1.00 36.86           C  
-ATOM    181  NE  ARG A  22      12.438  47.556  34.497  1.00 40.39           N  
-ATOM    182  CZ  ARG A  22      12.938  48.394  33.598  1.00 42.26           C  
-ATOM    183  NH1 ARG A  22      14.183  48.841  33.710  1.00 44.18           N  
-ATOM    184  NH2 ARG A  22      12.195  48.777  32.571  1.00 44.37           N  
-ATOM    185  N   ASN A  23      15.477  49.671  39.388  1.00 27.84           N  
-ATOM    186  CA  ASN A  23      16.515  50.635  39.082  1.00 28.00           C  
-ATOM    187  C   ASN A  23      16.891  50.415  37.620  1.00 27.97           C  
-ATOM    188  O   ASN A  23      17.325  49.332  37.247  1.00 27.35           O  
-ATOM    189  CB  ASN A  23      17.709  50.403  40.028  1.00 27.80           C  
-ATOM    190  CG  ASN A  23      18.813  51.437  39.871  1.00 28.43           C  
-ATOM    191  OD1 ASN A  23      19.168  51.824  38.755  1.00 29.14           O  
-ATOM    192  ND2 ASN A  23      19.394  51.859  40.999  1.00 27.03           N  
-ATOM    193  N   LYS A  24      16.702  51.444  36.795  1.00 28.16           N  
-ATOM    194  CA  LYS A  24      16.921  51.323  35.351  1.00 28.19           C  
-ATOM    195  C   LYS A  24      18.388  51.155  34.980  1.00 27.84           C  
-ATOM    196  O   LYS A  24      18.699  50.642  33.913  1.00 28.33           O  
-ATOM    197  CB  LYS A  24      16.319  52.519  34.615  1.00 28.81           C  
-ATOM    198  CG  LYS A  24      14.814  52.678  34.846  1.00 30.09           C  
-ATOM    199  CD  LYS A  24      14.157  53.461  33.736  1.00 34.71           C  
-ATOM    200  CE  LYS A  24      14.098  54.934  34.071  1.00 36.60           C  
-ATOM    201  NZ  LYS A  24      13.245  55.675  33.103  1.00 39.91           N  
-ATOM    202  N   LEU A  25      19.282  51.570  35.876  1.00 27.22           N  
-ATOM    203  CA  LEU A  25      20.712  51.573  35.609  1.00 26.40           C  
-ATOM    204  C   LEU A  25      21.441  50.333  36.133  1.00 25.95           C  
-ATOM    205  O   LEU A  25      22.298  49.791  35.441  1.00 25.88           O  
-ATOM    206  CB  LEU A  25      21.356  52.839  36.185  1.00 26.45           C  
-ATOM    207  CG  LEU A  25      21.457  54.107  35.318  1.00 26.77           C  
-ATOM    208  CD1 LEU A  25      20.481  54.126  34.156  1.00 26.58           C  
-ATOM    209  CD2 LEU A  25      21.289  55.351  36.180  1.00 25.65           C  
-ATOM    210  N   THR A  26      21.114  49.904  37.353  1.00 25.03           N  
-ATOM    211  CA  THR A  26      21.778  48.749  37.959  1.00 24.08           C  
-ATOM    212  C   THR A  26      21.007  47.457  37.751  1.00 23.96           C  
-ATOM    213  O   THR A  26      21.557  46.368  37.948  1.00 24.27           O  
-ATOM    214  CB  THR A  26      21.980  48.946  39.488  1.00 23.79           C  
-ATOM    215  OG1 THR A  26      20.703  49.106  40.127  1.00 22.38           O  
-ATOM    216  CG2 THR A  26      22.721  50.229  39.781  1.00 22.97           C  
-ATOM    217  N   GLY A  27      19.735  47.584  37.388  1.00 23.67           N  
-ATOM    218  CA  GLY A  27      18.827  46.452  37.312  1.00 23.63           C  
-ATOM    219  C   GLY A  27      18.157  46.062  38.630  1.00 23.58           C  
-ATOM    220  O   GLY A  27      17.250  45.234  38.644  1.00 23.04           O  
-ATOM    221  N   GLU A  28      18.597  46.649  39.738  1.00 23.67           N  
-ATOM    222  CA  GLU A  28      18.112  46.219  41.053  1.00 24.30           C  
-ATOM    223  C   GLU A  28      16.610  46.412  41.197  1.00 24.28           C  
-ATOM    224  O   GLU A  28      16.083  47.500  40.932  1.00 24.80           O  
-ATOM    225  CB  GLU A  28      18.857  46.933  42.185  1.00 24.11           C  
-ATOM    226  CG  GLU A  28      18.361  46.580  43.587  1.00 25.66           C  
-ATOM    227  CD  GLU A  28      19.158  47.272  44.686  1.00 26.93           C  
-ATOM    228  OE1 GLU A  28      19.589  48.421  44.491  1.00 29.32           O  
-ATOM    229  OE2 GLU A  28      19.370  46.668  45.748  1.00 29.27           O  
-ATOM    230  N   VAL A  29      15.926  45.342  41.597  1.00 24.14           N  
-ATOM    231  CA  VAL A  29      14.501  45.399  41.910  1.00 24.02           C  
-ATOM    232  C   VAL A  29      14.353  45.895  43.342  1.00 23.63           C  
-ATOM    233  O   VAL A  29      15.038  45.416  44.241  1.00 23.55           O  
-ATOM    234  CB  VAL A  29      13.827  44.020  41.754  1.00 23.96           C  
-ATOM    235  CG1 VAL A  29      12.344  44.114  42.049  1.00 24.18           C  
-ATOM    236  CG2 VAL A  29      14.051  43.469  40.345  1.00 24.89           C  
-ATOM    237  N   VAL A  30      13.465  46.862  43.538  1.00 23.21           N  
-ATOM    238  CA  VAL A  30      13.273  47.514  44.831  1.00 22.68           C  
-ATOM    239  C   VAL A  30      11.787  47.651  45.190  1.00 23.16           C  
-ATOM    240  O   VAL A  30      10.906  47.514  44.330  1.00 23.12           O  
-ATOM    241  CB  VAL A  30      13.928  48.926  44.855  1.00 22.79           C  
-ATOM    242  CG1 VAL A  30      15.446  48.848  44.597  1.00 21.31           C  
-ATOM    243  CG2 VAL A  30      13.256  49.850  43.859  1.00 21.39           C  
-ATOM    244  N   ALA A  31      11.526  47.915  46.463  1.00 23.33           N  
-ATOM    245  CA  ALA A  31      10.206  48.309  46.926  1.00 24.38           C  
-ATOM    246  C   ALA A  31      10.240  49.792  47.274  1.00 25.18           C  
-ATOM    247  O   ALA A  31      11.164  50.258  47.943  1.00 25.22           O  
-ATOM    248  CB  ALA A  31       9.787  47.484  48.126  1.00 23.84           C  
-ATOM    249  N   LEU A  32       9.251  50.538  46.797  1.00 26.42           N  
-ATOM    250  CA  LEU A  32       9.179  51.967  47.085  1.00 27.75           C  
-ATOM    251  C   LEU A  32       8.000  52.242  47.990  1.00 28.70           C  
-ATOM    252  O   LEU A  32       6.842  52.025  47.612  1.00 28.96           O  
-ATOM    253  CB  LEU A  32       9.085  52.804  45.809  1.00 27.79           C  
-ATOM    254  CG  LEU A  32      10.096  52.581  44.680  1.00 27.93           C  
-ATOM    255  CD1 LEU A  32       9.676  53.397  43.459  1.00 27.46           C  
-ATOM    256  CD2 LEU A  32      11.498  52.959  45.114  1.00 29.28           C  
-ATOM    257  N   LYS A  33       8.308  52.683  49.201  1.00 30.08           N  
-ATOM    258  CA  LYS A  33       7.295  52.987  50.195  1.00 31.82           C  
-ATOM    259  C   LYS A  33       7.036  54.481  50.147  1.00 33.28           C  
-ATOM    260  O   LYS A  33       7.884  55.289  50.538  1.00 33.35           O  
-ATOM    261  CB  LYS A  33       7.759  52.555  51.588  1.00 31.64           C  
-ATOM    262  CG  LYS A  33       6.696  52.644  52.658  1.00 31.79           C  
-ATOM    263  CD  LYS A  33       7.087  51.837  53.868  1.00 33.42           C  
-ATOM    264  CE  LYS A  33       6.046  51.968  54.965  1.00 35.29           C  
-ATOM    265  NZ  LYS A  33       6.435  51.156  56.151  1.00 36.22           N  
-ATOM    266  N   LYS A  34       5.866  54.837  49.639  1.00 35.20           N  
-ATOM    267  CA  LYS A  34       5.484  56.228  49.496  1.00 37.53           C  
-ATOM    268  C   LYS A  34       4.966  56.758  50.826  1.00 38.84           C  
-ATOM    269  O   LYS A  34       4.140  56.121  51.477  1.00 38.79           O  
-ATOM    270  CB  LYS A  34       4.419  56.363  48.411  1.00 37.60           C  
-ATOM    271  CG  LYS A  34       4.258  57.767  47.856  1.00 39.36           C  
-ATOM    272  CD  LYS A  34       3.505  57.741  46.521  1.00 42.15           C  
-ATOM    273  CE  LYS A  34       2.022  57.485  46.725  1.00 43.79           C  
-ATOM    274  NZ  LYS A  34       1.309  57.343  45.431  1.00 45.91           N  
-ATOM    275  N   ILE A  35       5.488  57.909  51.236  1.00 40.87           N  
-ATOM    276  CA  ILE A  35       5.008  58.602  52.423  1.00 42.90           C  
-ATOM    277  C   ILE A  35       4.559  60.002  52.004  1.00 44.85           C  
-ATOM    278  O   ILE A  35       5.385  60.842  51.636  1.00 44.85           O  
-ATOM    279  CB  ILE A  35       6.104  58.671  53.540  1.00 42.67           C  
-ATOM    280  CG1 ILE A  35       6.779  57.302  53.775  1.00 42.21           C  
-ATOM    281  CG2 ILE A  35       5.537  59.301  54.824  1.00 41.74           C  
-ATOM    282  CD1 ILE A  35       6.048  56.343  54.717  1.00 41.17           C  
-ATOM    283  N   ARG A  36       3.246  60.228  52.036  1.00 47.59           N  
-ATOM    284  CA  ARG A  36       2.658  61.533  51.717  1.00 50.44           C  
-ATOM    285  C   ARG A  36       2.955  62.528  52.837  1.00 51.80           C  
-ATOM    286  O   ARG A  36       2.793  62.207  54.015  1.00 51.96           O  
-ATOM    287  CB  ARG A  36       1.148  61.408  51.498  1.00 50.74           C  
-ATOM    288  CG  ARG A  36       0.758  60.530  50.312  1.00 53.01           C  
-ATOM    289  CD  ARG A  36      -0.466  61.018  49.532  1.00 57.02           C  
-ATOM    290  NE  ARG A  36      -0.200  61.045  48.093  1.00 60.26           N  
-ATOM    291  CZ  ARG A  36      -0.409  60.022  47.266  1.00 61.92           C  
-ATOM    292  NH1 ARG A  36      -0.902  58.876  47.723  1.00 62.85           N  
-ATOM    293  NH2 ARG A  36      -0.126  60.143  45.974  1.00 62.90           N  
-ATOM    294  N   LEU A  37       3.388  63.731  52.465  1.00 53.97           N  
-ATOM    295  CA  LEU A  37       3.949  64.678  53.431  1.00 56.17           C  
-ATOM    296  C   LEU A  37       3.044  65.839  53.859  1.00 57.90           C  
-ATOM    297  O   LEU A  37       3.005  66.178  55.047  1.00 58.18           O  
-ATOM    298  CB  LEU A  37       5.293  65.217  52.933  1.00 55.87           C  
-ATOM    299  CG  LEU A  37       6.502  64.283  52.999  1.00 55.88           C  
-ATOM    300  CD1 LEU A  37       7.729  64.988  52.452  1.00 55.28           C  
-ATOM    301  CD2 LEU A  37       6.756  63.786  54.414  1.00 55.81           C  
-ATOM    302  N   ASP A  38       2.327  66.430  52.899  1.00 59.95           N  
-ATOM    303  CA  ASP A  38       1.523  67.665  53.087  1.00 62.07           C  
-ATOM    304  C   ASP A  38       2.249  68.880  53.712  1.00 62.84           C  
-ATOM    305  O   ASP A  38       2.738  68.824  54.850  1.00 63.07           O  
-ATOM    306  CB  ASP A  38       0.164  67.414  53.778  1.00 62.36           C  
-ATOM    307  CG  ASP A  38       0.121  66.118  54.563  1.00 63.84           C  
-ATOM    308  OD1 ASP A  38       0.507  66.138  55.753  1.00 65.42           O  
-ATOM    309  OD2 ASP A  38      -0.289  65.037  54.079  1.00 65.36           O  
-ATOM    310  N   THR A  39       2.290  69.974  52.950  1.00 63.72           N  
-ATOM    311  CA  THR A  39       3.001  71.200  53.333  1.00 64.49           C  
-ATOM    312  C   THR A  39       2.441  71.838  54.608  1.00 64.43           C  
-ATOM    313  O   THR A  39       3.185  72.444  55.383  1.00 64.73           O  
-ATOM    314  CB  THR A  39       3.012  72.211  52.147  1.00 64.69           C  
-ATOM    315  OG1 THR A  39       4.246  72.088  51.428  1.00 65.54           O  
-ATOM    316  CG2 THR A  39       3.041  73.668  52.629  1.00 65.25           C  
-ATOM    317  N   GLU A  40       1.133  71.700  54.807  1.00 64.23           N  
-ATOM    318  CA  GLU A  40       0.476  72.144  56.031  1.00 63.85           C  
-ATOM    319  C   GLU A  40       0.409  70.984  57.028  1.00 62.61           C  
-ATOM    320  O   GLU A  40       1.315  70.141  57.078  1.00 62.77           O  
-ATOM    321  CB  GLU A  40      -0.930  72.664  55.714  1.00 64.47           C  
-ATOM    322  CG  GLU A  40      -0.986  74.132  55.311  1.00 67.00           C  
-ATOM    323  CD  GLU A  40      -0.562  74.375  53.872  1.00 70.20           C  
-ATOM    324  OE1 GLU A  40      -0.833  73.510  53.006  1.00 71.64           O  
-ATOM    325  OE2 GLU A  40       0.044  75.438  53.604  1.00 71.45           O  
-ATOM    326  N   THR A  41      -0.672  70.949  57.811  1.00 60.85           N  
-ATOM    327  CA  THR A  41      -0.967  69.866  58.758  1.00 58.73           C  
-ATOM    328  C   THR A  41       0.142  69.619  59.791  1.00 56.91           C  
-ATOM    329  O   THR A  41       0.280  70.387  60.742  1.00 57.02           O  
-ATOM    330  CB  THR A  41      -1.395  68.546  58.030  1.00 58.96           C  
-ATOM    331  OG1 THR A  41      -0.571  68.321  56.879  1.00 58.70           O  
-ATOM    332  CG2 THR A  41      -2.792  68.685  57.440  1.00 59.43           C  
-ATOM    333  N   GLU A  42       0.933  68.565  59.605  1.00 54.17           N  
-ATOM    334  CA  GLU A  42       1.843  68.135  60.659  1.00 51.40           C  
-ATOM    335  C   GLU A  42       3.286  67.881  60.235  1.00 48.69           C  
-ATOM    336  O   GLU A  42       4.136  67.601  61.079  1.00 48.73           O  
-ATOM    337  CB  GLU A  42       1.272  66.906  61.370  1.00 52.10           C  
-ATOM    338  CG  GLU A  42       0.263  67.237  62.463  1.00 53.71           C  
-ATOM    339  CD  GLU A  42       0.913  67.834  63.702  1.00 56.17           C  
-ATOM    340  OE1 GLU A  42       2.011  67.367  64.093  1.00 57.39           O  
-ATOM    341  OE2 GLU A  42       0.326  68.771  64.283  1.00 56.47           O  
-ATOM    342  N   GLY A  43       3.570  68.002  58.943  1.00 45.41           N  
-ATOM    343  CA  GLY A  43       4.910  67.755  58.437  1.00 41.57           C  
-ATOM    344  C   GLY A  43       5.206  66.269  58.353  1.00 38.86           C  
-ATOM    345  O   GLY A  43       4.284  65.472  58.149  1.00 38.45           O  
-ATOM    346  N   VAL A  44       6.478  65.894  58.509  1.00 35.81           N  
-ATOM    347  CA  VAL A  44       6.868  64.485  58.428  1.00 32.99           C  
-ATOM    348  C   VAL A  44       6.251  63.681  59.587  1.00 31.36           C  
-ATOM    349  O   VAL A  44       6.489  63.983  60.753  1.00 30.82           O  
-ATOM    350  CB  VAL A  44       8.413  64.281  58.364  1.00 33.03           C  
-ATOM    351  CG1 VAL A  44       8.754  62.818  58.125  1.00 31.77           C  
-ATOM    352  CG2 VAL A  44       9.042  65.151  57.273  1.00 32.47           C  
-ATOM    353  N   PRO A  45       5.447  62.669  59.259  1.00 29.82           N  
-ATOM    354  CA  PRO A  45       4.816  61.825  60.283  1.00 28.75           C  
-ATOM    355  C   PRO A  45       5.861  61.130  61.158  1.00 27.82           C  
-ATOM    356  O   PRO A  45       6.875  60.655  60.624  1.00 27.38           O  
-ATOM    357  CB  PRO A  45       4.030  60.798  59.464  1.00 28.70           C  
-ATOM    358  CG  PRO A  45       4.561  60.886  58.090  1.00 29.04           C  
-ATOM    359  CD  PRO A  45       5.071  62.263  57.891  1.00 29.52           C  
-ATOM    360  N   SER A  46       5.618  61.099  62.470  1.00 26.44           N  
-ATOM    361  CA  SER A  46       6.545  60.513  63.442  1.00 25.76           C  
-ATOM    362  C   SER A  46       6.847  59.047  63.140  1.00 25.17           C  
-ATOM    363  O   SER A  46       7.940  58.565  63.419  1.00 25.13           O  
-ATOM    364  CB  SER A  46       5.987  60.635  64.867  1.00 25.97           C  
-ATOM    365  OG  SER A  46       4.730  59.982  64.981  1.00 26.14           O  
-ATOM    366  N   THR A  47       5.873  58.346  62.568  1.00 24.21           N  
-ATOM    367  CA  THR A  47       6.045  56.947  62.196  1.00 24.00           C  
-ATOM    368  C   THR A  47       7.140  56.830  61.136  1.00 23.12           C  
-ATOM    369  O   THR A  47       7.954  55.905  61.178  1.00 22.28           O  
-ATOM    370  CB  THR A  47       4.735  56.368  61.641  1.00 24.17           C  
-ATOM    371  OG1 THR A  47       4.190  57.293  60.694  1.00 25.32           O  
-ATOM    372  CG2 THR A  47       3.673  56.296  62.726  1.00 24.69           C  
-ATOM    373  N   ALA A  48       7.158  57.778  60.199  1.00 22.48           N  
-ATOM    374  CA  ALA A  48       8.208  57.824  59.179  1.00 22.36           C  
-ATOM    375  C   ALA A  48       9.536  58.265  59.787  1.00 22.45           C  
-ATOM    376  O   ALA A  48      10.606  57.751  59.431  1.00 22.30           O  
-ATOM    377  CB  ALA A  48       7.810  58.734  58.031  1.00 21.93           C  
-ATOM    378  N   ILE A  49       9.469  59.212  60.715  1.00 22.25           N  
-ATOM    379  CA  ILE A  49      10.681  59.677  61.377  1.00 22.37           C  
-ATOM    380  C   ILE A  49      11.364  58.520  62.122  1.00 22.05           C  
-ATOM    381  O   ILE A  49      12.581  58.309  61.988  1.00 21.91           O  
-ATOM    382  CB  ILE A  49      10.371  60.911  62.261  1.00 22.40           C  
-ATOM    383  CG1 ILE A  49      10.444  62.178  61.386  1.00 22.61           C  
-ATOM    384  CG2 ILE A  49      11.304  61.001  63.462  1.00 22.39           C  
-ATOM    385  CD1 ILE A  49       9.614  63.326  61.905  1.00 23.46           C  
-ATOM    386  N   ARG A  50      10.564  57.745  62.850  1.00 21.44           N  
-ATOM    387  CA  ARG A  50      11.053  56.568  63.564  1.00 21.21           C  
-ATOM    388  C   ARG A  50      11.507  55.434  62.636  1.00 21.09           C  
-ATOM    389  O   ARG A  50      12.565  54.856  62.854  1.00 20.34           O  
-ATOM    390  CB  ARG A  50       9.981  56.044  64.520  1.00 21.39           C  
-ATOM    391  CG  ARG A  50       9.911  56.777  65.850  1.00 21.56           C  
-ATOM    392  CD  ARG A  50       8.715  56.371  66.680  1.00 21.08           C  
-ATOM    393  NE  ARG A  50       8.632  57.076  67.955  1.00 21.89           N  
-ATOM    394  CZ  ARG A  50       7.609  56.963  68.800  1.00 21.65           C  
-ATOM    395  NH1 ARG A  50       6.588  56.173  68.505  1.00 19.65           N  
-ATOM    396  NH2 ARG A  50       7.608  57.637  69.950  1.00 21.10           N  
-ATOM    397  N   GLU A  51      10.702  55.102  61.625  1.00 21.11           N  
-ATOM    398  CA  GLU A  51      11.049  54.004  60.705  1.00 21.68           C  
-ATOM    399  C   GLU A  51      12.400  54.257  60.020  1.00 21.10           C  
-ATOM    400  O   GLU A  51      13.250  53.366  59.972  1.00 21.02           O  
-ATOM    401  CB  GLU A  51       9.938  53.751  59.660  1.00 21.79           C  
-ATOM    402  CG  GLU A  51      10.374  52.909  58.458  1.00 24.48           C  
-ATOM    403  CD  GLU A  51       9.248  52.061  57.870  1.00 29.02           C  
-ATOM    404  OE1 GLU A  51       8.266  52.663  57.386  1.00 29.46           O  
-ATOM    405  OE2 GLU A  51       9.348  50.798  57.887  1.00 29.27           O  
-ATOM    406  N   ILE A  52      12.599  55.473  59.512  1.00 20.26           N  
-ATOM    407  CA  ILE A  52      13.824  55.789  58.787  1.00 19.35           C  
-ATOM    408  C   ILE A  52      15.048  55.794  59.691  1.00 19.40           C  
-ATOM    409  O   ILE A  52      16.039  55.120  59.385  1.00 18.94           O  
-ATOM    410  CB  ILE A  52      13.715  57.121  58.016  1.00 19.12           C  
-ATOM    411  CG1 ILE A  52      12.619  57.043  56.940  1.00 19.82           C  
-ATOM    412  CG2 ILE A  52      15.061  57.471  57.367  1.00 19.07           C  
-ATOM    413  CD1 ILE A  52      12.184  58.427  56.410  1.00 19.55           C  
-ATOM    414  N   SER A  53      14.989  56.553  60.786  1.00 19.23           N  
-ATOM    415  CA  SER A  53      16.147  56.683  61.678  1.00 20.21           C  
-ATOM    416  C   SER A  53      16.534  55.369  62.339  1.00 20.03           C  
-ATOM    417  O   SER A  53      17.709  55.111  62.557  1.00 19.86           O  
-ATOM    418  CB  SER A  53      15.961  57.778  62.743  1.00 20.25           C  
-ATOM    419  OG  SER A  53      14.839  57.528  63.565  1.00 21.76           O  
-ATOM    420  N   LEU A  54      15.557  54.525  62.646  1.00 20.47           N  
-ATOM    421  CA  LEU A  54      15.900  53.246  63.255  1.00 20.82           C  
-ATOM    422  C   LEU A  54      16.432  52.273  62.227  1.00 21.38           C  
-ATOM    423  O   LEU A  54      17.355  51.526  62.505  1.00 21.36           O  
-ATOM    424  CB  LEU A  54      14.729  52.667  64.046  1.00 21.01           C  
-ATOM    425  CG  LEU A  54      14.274  53.558  65.205  1.00 20.76           C  
-ATOM    426  CD1 LEU A  54      12.964  53.049  65.804  1.00 20.89           C  
-ATOM    427  CD2 LEU A  54      15.344  53.675  66.258  1.00 21.40           C  
-ATOM    428  N   LEU A  55      15.871  52.306  61.022  1.00 22.17           N  
-ATOM    429  CA  LEU A  55      16.286  51.385  59.979  1.00 23.15           C  
-ATOM    430  C   LEU A  55      17.689  51.687  59.462  1.00 24.20           C  
-ATOM    431  O   LEU A  55      18.384  50.790  58.991  1.00 24.83           O  
-ATOM    432  CB  LEU A  55      15.285  51.403  58.833  1.00 22.62           C  
-ATOM    433  CG  LEU A  55      14.597  50.099  58.435  1.00 23.27           C  
-ATOM    434  CD1 LEU A  55      14.673  48.994  59.489  1.00 21.47           C  
-ATOM    435  CD2 LEU A  55      13.164  50.388  58.053  1.00 23.09           C  
-ATOM    436  N   LYS A  56      18.093  52.951  59.559  1.00 25.13           N  
-ATOM    437  CA  LYS A  56      19.427  53.388  59.165  1.00 26.51           C  
-ATOM    438  C   LYS A  56      20.523  52.799  60.053  1.00 26.96           C  
-ATOM    439  O   LYS A  56      21.679  52.704  59.643  1.00 27.34           O  
-ATOM    440  CB  LYS A  56      19.502  54.916  59.165  1.00 26.30           C  
-ATOM    441  CG  LYS A  56      18.901  55.531  57.904  1.00 27.78           C  
-ATOM    442  CD  LYS A  56      19.358  56.962  57.702  1.00 30.91           C  
-ATOM    443  CE  LYS A  56      20.644  57.002  56.885  1.00 32.12           C  
-ATOM    444  NZ  LYS A  56      21.278  58.349  56.916  1.00 34.31           N  
-ATOM    445  N   GLU A  57      20.157  52.399  61.265  1.00 27.62           N  
-ATOM    446  CA  GLU A  57      21.113  51.771  62.172  1.00 28.09           C  
-ATOM    447  C   GLU A  57      21.112  50.246  62.044  1.00 27.99           C  
-ATOM    448  O   GLU A  57      22.088  49.572  62.403  1.00 29.21           O  
-ATOM    449  CB  GLU A  57      20.813  52.194  63.609  1.00 28.26           C  
-ATOM    450  CG  GLU A  57      21.246  53.627  63.901  1.00 30.24           C  
-ATOM    451  CD  GLU A  57      20.955  54.086  65.318  1.00 32.55           C  
-ATOM    452  OE1 GLU A  57      20.893  53.256  66.252  1.00 33.73           O  
-ATOM    453  OE2 GLU A  57      20.810  55.305  65.498  1.00 34.37           O  
-ATOM    454  N   LEU A  58      20.028  49.706  61.510  1.00 26.93           N  
-ATOM    455  CA  LEU A  58      19.783  48.275  61.576  1.00 26.41           C  
-ATOM    456  C   LEU A  58      20.149  47.558  60.288  1.00 25.88           C  
-ATOM    457  O   LEU A  58      19.282  47.215  59.484  1.00 27.04           O  
-ATOM    458  CB  LEU A  58      18.321  47.993  61.975  1.00 25.60           C  
-ATOM    459  CG  LEU A  58      17.914  48.431  63.387  1.00 25.50           C  
-ATOM    460  CD1 LEU A  58      16.422  48.259  63.612  1.00 25.37           C  
-ATOM    461  CD2 LEU A  58      18.692  47.703  64.480  1.00 24.58           C  
-ATOM    462  N   ASN A  59      21.436  47.327  60.100  1.00 25.22           N  
-ATOM    463  CA  ASN A  59      21.908  46.553  58.968  1.00 24.82           C  
-ATOM    464  C   ASN A  59      22.124  45.108  59.374  1.00 23.18           C  
-ATOM    465  O   ASN A  59      23.048  44.790  60.124  1.00 23.10           O  
-ATOM    466  CB  ASN A  59      23.197  47.139  58.390  1.00 25.86           C  
-ATOM    467  CG  ASN A  59      23.437  46.699  56.969  1.00 30.63           C  
-ATOM    468  OD1 ASN A  59      22.770  47.176  56.040  1.00 36.23           O  
-ATOM    469  ND2 ASN A  59      24.375  45.765  56.780  1.00 35.64           N  
-ATOM    470  N   HIS A  60      21.269  44.229  58.865  1.00 21.17           N  
-ATOM    471  CA  HIS A  60      21.293  42.833  59.266  1.00 19.87           C  
-ATOM    472  C   HIS A  60      20.601  41.993  58.186  1.00 19.20           C  
-ATOM    473  O   HIS A  60      19.585  42.428  57.632  1.00 19.04           O  
-ATOM    474  CB  HIS A  60      20.598  42.672  60.632  1.00 19.44           C  
-ATOM    475  CG  HIS A  60      20.672  41.281  61.180  1.00 19.57           C  
-ATOM    476  ND1 HIS A  60      21.647  40.879  62.071  1.00 19.82           N  
-ATOM    477  CD2 HIS A  60      19.911  40.191  60.938  1.00 16.78           C  
-ATOM    478  CE1 HIS A  60      21.482  39.599  62.350  1.00 18.05           C  
-ATOM    479  NE2 HIS A  60      20.433  39.160  61.680  1.00 19.62           N  
-ATOM    480  N   PRO A  61      21.140  40.812  57.867  1.00 18.18           N  
-ATOM    481  CA  PRO A  61      20.534  39.963  56.823  1.00 17.60           C  
-ATOM    482  C   PRO A  61      19.057  39.611  57.069  1.00 17.43           C  
-ATOM    483  O   PRO A  61      18.384  39.259  56.109  1.00 17.22           O  
-ATOM    484  CB  PRO A  61      21.406  38.702  56.827  1.00 17.96           C  
-ATOM    485  CG  PRO A  61      22.185  38.756  58.149  1.00 17.69           C  
-ATOM    486  CD  PRO A  61      22.369  40.216  58.427  1.00 17.55           C  
-ATOM    487  N   ASN A  62      18.566  39.729  58.303  1.00 16.83           N  
-ATOM    488  CA  ASN A  62      17.172  39.408  58.621  1.00 16.57           C  
-ATOM    489  C   ASN A  62      16.303  40.621  58.990  1.00 17.25           C  
-ATOM    490  O   ASN A  62      15.256  40.509  59.632  1.00 17.68           O  
-ATOM    491  CB  ASN A  62      17.107  38.303  59.672  1.00 16.16           C  
-ATOM    492  CG  ASN A  62      17.807  37.027  59.214  1.00 15.97           C  
-ATOM    493  OD1 ASN A  62      18.833  36.637  59.767  1.00 16.77           O  
-ATOM    494  ND2 ASN A  62      17.269  36.390  58.187  1.00 13.71           N  
-ATOM    495  N   ILE A  63      16.752  41.792  58.561  1.00 17.80           N  
-ATOM    496  CA  ILE A  63      15.992  43.009  58.707  1.00 17.60           C  
-ATOM    497  C   ILE A  63      15.955  43.604  57.303  1.00 18.63           C  
-ATOM    498  O   ILE A  63      16.996  43.713  56.642  1.00 18.25           O  
-ATOM    499  CB  ILE A  63      16.666  43.958  59.737  1.00 17.67           C  
-ATOM    500  CG1 ILE A  63      16.716  43.303  61.133  1.00 16.72           C  
-ATOM    501  CG2 ILE A  63      15.926  45.289  59.811  1.00 17.48           C  
-ATOM    502  CD1 ILE A  63      17.498  44.087  62.179  1.00 17.58           C  
-ATOM    503  N   VAL A  64      14.752  43.941  56.835  1.00 18.86           N  
-ATOM    504  CA  VAL A  64      14.583  44.591  55.537  1.00 19.63           C  
-ATOM    505  C   VAL A  64      15.521  45.791  55.427  1.00 19.50           C  
-ATOM    506  O   VAL A  64      15.568  46.633  56.325  1.00 19.96           O  
-ATOM    507  CB  VAL A  64      13.099  45.000  55.267  1.00 19.39           C  
-ATOM    508  CG1 VAL A  64      12.672  46.193  56.140  1.00 19.53           C  
-ATOM    509  CG2 VAL A  64      12.887  45.318  53.771  1.00 21.30           C  
-ATOM    510  N   LYS A  65      16.295  45.838  54.350  1.00 19.34           N  
-ATOM    511  CA  LYS A  65      17.276  46.901  54.160  1.00 19.59           C  
-ATOM    512  C   LYS A  65      16.692  48.152  53.509  1.00 19.27           C  
-ATOM    513  O   LYS A  65      16.185  48.100  52.384  1.00 18.61           O  
-ATOM    514  CB  LYS A  65      18.455  46.404  53.330  1.00 20.04           C  
-ATOM    515  CG  LYS A  65      19.661  47.331  53.372  1.00 22.60           C  
-ATOM    516  CD  LYS A  65      20.831  46.781  52.556  1.00 27.53           C  
-ATOM    517  CE  LYS A  65      22.058  47.684  52.688  1.00 30.46           C  
-ATOM    518  NZ  LYS A  65      23.124  47.325  51.697  1.00 33.67           N  
-ATOM    519  N   LEU A  66      16.758  49.264  54.236  1.00 18.96           N  
-ATOM    520  CA  LEU A  66      16.468  50.573  53.679  1.00 19.08           C  
-ATOM    521  C   LEU A  66      17.670  50.998  52.842  1.00 19.39           C  
-ATOM    522  O   LEU A  66      18.774  51.165  53.371  1.00 19.30           O  
-ATOM    523  CB  LEU A  66      16.196  51.595  54.788  1.00 18.84           C  
-ATOM    524  CG  LEU A  66      15.913  53.038  54.343  1.00 19.14           C  
-ATOM    525  CD1 LEU A  66      14.590  53.119  53.555  1.00 17.32           C  
-ATOM    526  CD2 LEU A  66      15.877  53.991  55.544  1.00 19.74           C  
-ATOM    527  N   LEU A  67      17.452  51.152  51.541  1.00 19.40           N  
-ATOM    528  CA  LEU A  67      18.524  51.463  50.597  1.00 20.73           C  
-ATOM    529  C   LEU A  67      18.767  52.953  50.457  1.00 21.64           C  
-ATOM    530  O   LEU A  67      19.899  53.376  50.288  1.00 21.98           O  
-ATOM    531  CB  LEU A  67      18.235  50.854  49.212  1.00 20.47           C  
-ATOM    532  CG  LEU A  67      18.097  49.327  49.119  1.00 20.00           C  
-ATOM    533  CD1 LEU A  67      17.701  48.907  47.709  1.00 20.37           C  
-ATOM    534  CD2 LEU A  67      19.405  48.641  49.526  1.00 19.69           C  
-ATOM    535  N   ASP A  68      17.701  53.746  50.559  1.00 23.46           N  
-ATOM    536  CA  ASP A  68      17.764  55.170  50.268  1.00 24.86           C  
-ATOM    537  C   ASP A  68      16.460  55.834  50.664  1.00 25.97           C  
-ATOM    538  O   ASP A  68      15.431  55.166  50.796  1.00 25.65           O  
-ATOM    539  CB  ASP A  68      17.991  55.378  48.759  1.00 25.23           C  
-ATOM    540  CG  ASP A  68      18.667  56.716  48.432  1.00 26.58           C  
-ATOM    541  OD1 ASP A  68      18.762  57.613  49.307  1.00 27.51           O  
-ATOM    542  OD2 ASP A  68      19.135  56.951  47.307  1.00 26.94           O  
-ATOM    543  N   VAL A  69      16.508  57.150  50.848  1.00 27.42           N  
-ATOM    544  CA  VAL A  69      15.312  57.947  51.090  1.00 29.64           C  
-ATOM    545  C   VAL A  69      15.269  59.057  50.041  1.00 31.81           C  
-ATOM    546  O   VAL A  69      16.200  59.846  49.942  1.00 32.11           O  
-ATOM    547  CB  VAL A  69      15.301  58.539  52.531  1.00 29.55           C  
-ATOM    548  CG1 VAL A  69      14.174  59.565  52.706  1.00 28.95           C  
-ATOM    549  CG2 VAL A  69      15.184  57.423  53.579  1.00 28.17           C  
-ATOM    550  N   ILE A  70      14.205  59.097  49.243  1.00 34.66           N  
-ATOM    551  CA  ILE A  70      14.076  60.111  48.198  1.00 37.43           C  
-ATOM    552  C   ILE A  70      12.985  61.106  48.565  1.00 39.62           C  
-ATOM    553  O   ILE A  70      11.834  60.721  48.783  1.00 40.01           O  
-ATOM    554  CB  ILE A  70      13.746  59.478  46.806  1.00 37.34           C  
-ATOM    555  CG1 ILE A  70      14.649  58.271  46.469  1.00 37.38           C  
-ATOM    556  CG2 ILE A  70      13.751  60.544  45.701  1.00 37.63           C  
-ATOM    557  CD1 ILE A  70      16.105  58.592  46.136  1.00 37.57           C  
-ATOM    558  N   HIS A  71      13.350  62.380  48.644  1.00 42.36           N  
-ATOM    559  CA  HIS A  71      12.354  63.442  48.700  1.00 45.33           C  
-ATOM    560  C   HIS A  71      12.149  64.026  47.305  1.00 47.14           C  
-ATOM    561  O   HIS A  71      13.004  64.748  46.790  1.00 47.44           O  
-ATOM    562  CB  HIS A  71      12.744  64.544  49.691  1.00 45.24           C  
-ATOM    563  CG  HIS A  71      11.723  65.636  49.807  1.00 46.30           C  
-ATOM    564  ND1 HIS A  71      12.062  66.961  49.974  1.00 47.44           N  
-ATOM    565  CD2 HIS A  71      10.368  65.597  49.774  1.00 47.47           C  
-ATOM    566  CE1 HIS A  71      10.963  67.691  50.040  1.00 47.55           C  
-ATOM    567  NE2 HIS A  71       9.921  66.888  49.921  1.00 46.88           N  
-ATOM    568  N   THR A  72      11.020  63.692  46.692  1.00 49.51           N  
-ATOM    569  CA  THR A  72      10.666  64.262  45.399  1.00 51.73           C  
-ATOM    570  C   THR A  72       9.434  65.149  45.550  1.00 53.03           C  
-ATOM    571  O   THR A  72       8.303  64.669  45.681  1.00 53.27           O  
-ATOM    572  CB  THR A  72      10.518  63.172  44.287  1.00 51.71           C  
-ATOM    573  OG1 THR A  72      10.179  63.794  43.039  1.00 52.67           O  
-ATOM    574  CG2 THR A  72       9.339  62.241  44.550  1.00 52.64           C  
-ATOM    575  N   GLU A  73       9.702  66.453  45.582  1.00 54.81           N  
-ATOM    576  CA  GLU A  73       8.692  67.515  45.644  1.00 56.02           C  
-ATOM    577  C   GLU A  73       7.435  67.145  46.443  1.00 55.97           C  
-ATOM    578  O   GLU A  73       6.379  66.834  45.877  1.00 56.13           O  
-ATOM    579  CB  GLU A  73       8.358  68.029  44.236  1.00 56.62           C  
-ATOM    580  CG  GLU A  73       9.554  68.514  43.413  1.00 59.52           C  
-ATOM    581  CD  GLU A  73      10.749  68.939  44.257  1.00 63.16           C  
-ATOM    582  OE1 GLU A  73      10.744  70.079  44.780  1.00 64.99           O  
-ATOM    583  OE2 GLU A  73      11.695  68.129  44.398  1.00 64.58           O  
-ATOM    584  N   ASN A  74       7.602  67.159  47.766  1.00 55.79           N  
-ATOM    585  CA  ASN A  74       6.541  66.945  48.760  1.00 55.29           C  
-ATOM    586  C   ASN A  74       5.939  65.542  48.881  1.00 54.09           C  
-ATOM    587  O   ASN A  74       4.727  65.371  49.033  1.00 54.17           O  
-ATOM    588  CB  ASN A  74       5.472  68.043  48.671  1.00 56.13           C  
-ATOM    589  CG  ASN A  74       6.063  69.432  48.845  1.00 57.97           C  
-ATOM    590  OD1 ASN A  74       6.590  69.770  49.916  1.00 60.49           O  
-ATOM    591  ND2 ASN A  74       6.005  70.238  47.783  1.00 59.77           N  
-ATOM    592  N   LYS A  75       6.817  64.544  48.814  1.00 52.39           N  
-ATOM    593  CA  LYS A  75       6.550  63.196  49.329  1.00 50.56           C  
-ATOM    594  C   LYS A  75       7.867  62.504  49.657  1.00 48.62           C  
-ATOM    595  O   LYS A  75       8.921  62.880  49.143  1.00 48.44           O  
-ATOM    596  CB  LYS A  75       5.704  62.332  48.377  1.00 51.06           C  
-ATOM    597  CG  LYS A  75       5.914  62.562  46.887  1.00 52.54           C  
-ATOM    598  CD  LYS A  75       5.223  61.477  46.059  1.00 54.99           C  
-ATOM    599  CE  LYS A  75       3.705  61.609  46.079  1.00 56.67           C  
-ATOM    600  NZ  LYS A  75       3.070  60.818  44.981  1.00 58.10           N  
-ATOM    601  N   LEU A  76       7.802  61.510  50.535  1.00 46.10           N  
-ATOM    602  CA  LEU A  76       8.959  60.694  50.854  1.00 43.69           C  
-ATOM    603  C   LEU A  76       8.805  59.333  50.193  1.00 41.77           C  
-ATOM    604  O   LEU A  76       7.758  58.697  50.301  1.00 41.24           O  
-ATOM    605  CB  LEU A  76       9.094  60.535  52.373  1.00 43.91           C  
-ATOM    606  CG  LEU A  76      10.293  61.115  53.129  1.00 44.20           C  
-ATOM    607  CD1 LEU A  76      10.669  62.519  52.657  1.00 44.63           C  
-ATOM    608  CD2 LEU A  76       9.999  61.111  54.623  1.00 43.66           C  
-ATOM    609  N   TYR A  77       9.849  58.907  49.489  1.00 39.49           N  
-ATOM    610  CA  TYR A  77       9.933  57.555  48.965  1.00 37.34           C  
-ATOM    611  C   TYR A  77      11.021  56.806  49.714  1.00 35.43           C  
-ATOM    612  O   TYR A  77      12.197  57.180  49.668  1.00 35.08           O  
-ATOM    613  CB  TYR A  77      10.261  57.567  47.473  1.00 37.84           C  
-ATOM    614  CG  TYR A  77       9.067  57.754  46.566  1.00 39.16           C  
-ATOM    615  CD1 TYR A  77       8.225  56.686  46.261  1.00 40.49           C  
-ATOM    616  CD2 TYR A  77       8.794  58.994  45.995  1.00 40.65           C  
-ATOM    617  CE1 TYR A  77       7.135  56.848  45.417  1.00 41.56           C  
-ATOM    618  CE2 TYR A  77       7.705  59.166  45.146  1.00 41.78           C  
-ATOM    619  CZ  TYR A  77       6.881  58.089  44.865  1.00 42.05           C  
-ATOM    620  OH  TYR A  77       5.804  58.250  44.031  1.00 43.56           O  
-ATOM    621  N   LEU A  78      10.623  55.756  50.417  1.00 32.94           N  
-ATOM    622  CA  LEU A  78      11.588  54.881  51.063  1.00 30.67           C  
-ATOM    623  C   LEU A  78      11.940  53.752  50.103  1.00 28.97           C  
-ATOM    624  O   LEU A  78      11.066  52.963  49.713  1.00 28.31           O  
-ATOM    625  CB  LEU A  78      11.040  54.326  52.385  1.00 30.55           C  
-ATOM    626  CG  LEU A  78      10.599  55.287  53.499  1.00 30.23           C  
-ATOM    627  CD1 LEU A  78      10.791  54.621  54.846  1.00 30.15           C  
-ATOM    628  CD2 LEU A  78      11.338  56.611  53.447  1.00 31.12           C  
-ATOM    629  N   VAL A  79      13.210  53.701  49.710  1.00 26.64           N  
-ATOM    630  CA  VAL A  79      13.695  52.671  48.797  1.00 25.43           C  
-ATOM    631  C   VAL A  79      14.218  51.471  49.581  1.00 24.68           C  
-ATOM    632  O   VAL A  79      15.242  51.554  50.247  1.00 23.89           O  
-ATOM    633  CB  VAL A  79      14.774  53.207  47.832  1.00 25.39           C  
-ATOM    634  CG1 VAL A  79      15.218  52.125  46.843  1.00 24.03           C  
-ATOM    635  CG2 VAL A  79      14.267  54.462  47.098  1.00 25.51           C  
-ATOM    636  N   PHE A  80      13.488  50.363  49.494  1.00 24.08           N  
-ATOM    637  CA  PHE A  80      13.809  49.140  50.220  1.00 24.01           C  
-ATOM    638  C   PHE A  80      14.267  48.047  49.250  1.00 23.68           C  
-ATOM    639  O   PHE A  80      13.882  48.053  48.089  1.00 23.69           O  
-ATOM    640  CB  PHE A  80      12.557  48.627  50.928  1.00 23.65           C  
-ATOM    641  CG  PHE A  80      12.152  49.419  52.130  1.00 24.02           C  
-ATOM    642  CD1 PHE A  80      12.859  49.318  53.330  1.00 23.88           C  
-ATOM    643  CD2 PHE A  80      11.012  50.212  52.096  1.00 24.29           C  
-ATOM    644  CE1 PHE A  80      12.452  50.031  54.453  1.00 23.67           C  
-ATOM    645  CE2 PHE A  80      10.601  50.921  53.221  1.00 24.01           C  
-ATOM    646  CZ  PHE A  80      11.323  50.837  54.394  1.00 22.98           C  
-ATOM    647  N   GLU A  81      15.073  47.109  49.733  1.00 23.74           N  
-ATOM    648  CA  GLU A  81      15.340  45.860  49.016  1.00 23.55           C  
-ATOM    649  C   GLU A  81      14.023  45.129  48.757  1.00 23.77           C  
-ATOM    650  O   GLU A  81      13.156  45.064  49.643  1.00 23.51           O  
-ATOM    651  CB  GLU A  81      16.260  44.960  49.845  1.00 24.00           C  
-ATOM    652  CG  GLU A  81      15.595  44.309  51.067  1.00 23.73           C  
-ATOM    653  CD  GLU A  81      16.439  43.209  51.688  1.00 25.84           C  
-ATOM    654  OE1 GLU A  81      16.812  42.251  50.978  1.00 27.27           O  
-ATOM    655  OE2 GLU A  81      16.748  43.304  52.892  1.00 27.80           O  
-ATOM    656  N   PHE A  82      13.857  44.597  47.550  1.00 23.88           N  
-ATOM    657  CA  PHE A  82      12.626  43.894  47.214  1.00 23.97           C  
-ATOM    658  C   PHE A  82      12.604  42.481  47.762  1.00 24.22           C  
-ATOM    659  O   PHE A  82      13.539  41.703  47.555  1.00 24.48           O  
-ATOM    660  CB  PHE A  82      12.394  43.849  45.708  1.00 24.09           C  
-ATOM    661  CG  PHE A  82      11.183  43.046  45.311  1.00 24.49           C  
-ATOM    662  CD1 PHE A  82       9.909  43.578  45.441  1.00 24.53           C  
-ATOM    663  CD2 PHE A  82      11.318  41.750  44.820  1.00 25.10           C  
-ATOM    664  CE1 PHE A  82       8.785  42.839  45.083  1.00 24.77           C  
-ATOM    665  CE2 PHE A  82      10.196  41.009  44.457  1.00 26.04           C  
-ATOM    666  CZ  PHE A  82       8.928  41.558  44.595  1.00 23.38           C  
-ATOM    667  N   LEU A  83      11.506  42.160  48.437  1.00 24.36           N  
-ATOM    668  CA  LEU A  83      11.239  40.826  48.952  1.00 24.96           C  
-ATOM    669  C   LEU A  83       9.936  40.349  48.324  1.00 25.48           C  
-ATOM    670  O   LEU A  83       9.087  41.163  47.997  1.00 25.62           O  
-ATOM    671  CB  LEU A  83      11.149  40.878  50.484  1.00 25.06           C  
-ATOM    672  CG  LEU A  83      12.507  41.249  51.109  1.00 24.82           C  
-ATOM    673  CD1 LEU A  83      12.379  41.846  52.490  1.00 25.42           C  
-ATOM    674  CD2 LEU A  83      13.339  40.003  51.165  1.00 26.59           C  
-ATOM    675  N   HIS A  84       9.778  39.042  48.163  1.00 26.12           N  
-ATOM    676  CA  HIS A  84       8.784  38.504  47.233  1.00 26.99           C  
-ATOM    677  C   HIS A  84       7.377  38.363  47.788  1.00 27.47           C  
-ATOM    678  O   HIS A  84       6.399  38.596  47.076  1.00 27.57           O  
-ATOM    679  CB  HIS A  84       9.274  37.191  46.637  1.00 27.33           C  
-ATOM    680  CG  HIS A  84      10.543  37.336  45.854  1.00 28.97           C  
-ATOM    681  ND1 HIS A  84      10.561  37.421  44.476  1.00 29.44           N  
-ATOM    682  CD2 HIS A  84      11.834  37.444  46.258  1.00 28.59           C  
-ATOM    683  CE1 HIS A  84      11.811  37.554  44.065  1.00 29.94           C  
-ATOM    684  NE2 HIS A  84      12.602  37.569  45.124  1.00 29.91           N  
-ATOM    685  N   GLN A  85       7.265  37.959  49.047  1.00 27.75           N  
-ATOM    686  CA  GLN A  85       5.965  37.933  49.694  1.00 28.11           C  
-ATOM    687  C   GLN A  85       6.075  37.965  51.208  1.00 27.27           C  
-ATOM    688  O   GLN A  85       7.179  37.921  51.745  1.00 26.89           O  
-ATOM    689  CB  GLN A  85       5.102  36.773  49.177  1.00 29.04           C  
-ATOM    690  CG  GLN A  85       5.443  35.370  49.627  1.00 31.91           C  
-ATOM    691  CD  GLN A  85       4.318  34.397  49.296  1.00 36.11           C  
-ATOM    692  OE1 GLN A  85       3.199  34.818  49.014  1.00 41.00           O  
-ATOM    693  NE2 GLN A  85       4.614  33.105  49.309  1.00 38.47           N  
-ATOM    694  N   ASP A  86       4.935  38.101  51.877  1.00 26.52           N  
-ATOM    695  CA  ASP A  86       4.890  38.131  53.331  1.00 26.23           C  
-ATOM    696  C   ASP A  86       4.502  36.763  53.865  1.00 26.02           C  
-ATOM    697  O   ASP A  86       3.970  35.929  53.121  1.00 26.42           O  
-ATOM    698  CB  ASP A  86       3.969  39.243  53.847  1.00 26.59           C  
-ATOM    699  CG  ASP A  86       2.500  38.977  53.577  1.00 27.43           C  
-ATOM    700  OD1 ASP A  86       1.950  37.979  54.087  1.00 27.65           O  
-ATOM    701  OD2 ASP A  86       1.808  39.733  52.872  1.00 31.37           O  
-ATOM    702  N   LEU A  87       4.775  36.527  55.140  1.00 25.51           N  
-ATOM    703  CA  LEU A  87       4.589  35.204  55.729  1.00 25.98           C  
-ATOM    704  C   LEU A  87       3.122  34.753  55.775  1.00 26.74           C  
-ATOM    705  O   LEU A  87       2.843  33.558  55.698  1.00 26.96           O  
-ATOM    706  CB  LEU A  87       5.212  35.137  57.130  1.00 24.76           C  
-ATOM    707  CG  LEU A  87       5.142  33.807  57.886  1.00 24.41           C  
-ATOM    708  CD1 LEU A  87       5.833  32.669  57.110  1.00 23.19           C  
-ATOM    709  CD2 LEU A  87       5.727  33.941  59.296  1.00 22.92           C  
-ATOM    710  N   LYS A  88       2.207  35.704  55.936  1.00 28.18           N  
-ATOM    711  CA  LYS A  88       0.779  35.406  55.959  1.00 29.84           C  
-ATOM    712  C   LYS A  88       0.338  34.798  54.632  1.00 30.66           C  
-ATOM    713  O   LYS A  88      -0.361  33.787  54.615  1.00 31.04           O  
-ATOM    714  CB  LYS A  88      -0.031  36.668  56.265  1.00 30.03           C  
-ATOM    715  CG  LYS A  88      -1.538  36.444  56.362  1.00 31.70           C  
-ATOM    716  CD  LYS A  88      -2.251  37.703  56.824  1.00 34.78           C  
-ATOM    717  CE  LYS A  88      -3.188  38.276  55.753  1.00 36.50           C  
-ATOM    718  NZ  LYS A  88      -4.195  39.226  56.353  1.00 37.07           N  
-ATOM    719  N   LYS A  89       0.754  35.418  53.527  1.00 31.63           N  
-ATOM    720  CA  LYS A  89       0.443  34.915  52.190  1.00 32.55           C  
-ATOM    721  C   LYS A  89       1.018  33.523  51.980  1.00 32.51           C  
-ATOM    722  O   LYS A  89       0.369  32.657  51.399  1.00 32.73           O  
-ATOM    723  CB  LYS A  89       0.971  35.867  51.119  1.00 32.83           C  
-ATOM    724  CG  LYS A  89      -0.018  36.950  50.732  1.00 35.70           C  
-ATOM    725  CD  LYS A  89       0.642  38.324  50.587  1.00 39.75           C  
-ATOM    726  CE  LYS A  89       1.428  38.447  49.279  1.00 42.35           C  
-ATOM    727  NZ  LYS A  89       2.415  39.579  49.331  1.00 44.30           N  
-ATOM    728  N   PHE A  90       2.232  33.303  52.477  1.00 32.45           N  
-ATOM    729  CA  PHE A  90       2.895  32.013  52.333  1.00 32.11           C  
-ATOM    730  C   PHE A  90       2.180  30.917  53.121  1.00 32.75           C  
-ATOM    731  O   PHE A  90       2.073  29.782  52.656  1.00 32.53           O  
-ATOM    732  CB  PHE A  90       4.349  32.110  52.774  1.00 31.79           C  
-ATOM    733  CG  PHE A  90       5.138  30.856  52.545  1.00 30.04           C  
-ATOM    734  CD1 PHE A  90       5.466  30.454  51.256  1.00 28.98           C  
-ATOM    735  CD2 PHE A  90       5.558  30.084  53.618  1.00 29.44           C  
-ATOM    736  CE1 PHE A  90       6.205  29.308  51.036  1.00 28.83           C  
-ATOM    737  CE2 PHE A  90       6.302  28.925  53.416  1.00 28.94           C  
-ATOM    738  CZ  PHE A  90       6.629  28.541  52.115  1.00 29.00           C  
-ATOM    739  N   MET A  91       1.691  31.254  54.310  1.00 33.53           N  
-ATOM    740  CA  MET A  91       0.938  30.284  55.099  1.00 34.60           C  
-ATOM    741  C   MET A  91      -0.377  29.922  54.408  1.00 35.36           C  
-ATOM    742  O   MET A  91      -0.739  28.751  54.363  1.00 35.51           O  
-ATOM    743  CB  MET A  91       0.708  30.781  56.518  1.00 34.61           C  
-ATOM    744  CG  MET A  91       1.970  30.763  57.370  1.00 34.96           C  
-ATOM    745  SD  MET A  91       1.729  31.479  58.996  1.00 36.79           S  
-ATOM    746  CE  MET A  91       1.243  33.081  58.633  1.00 32.23           C  
-ATOM    747  N   ASP A  92      -1.060  30.920  53.844  1.00 36.69           N  
-ATOM    748  CA  ASP A  92      -2.257  30.690  53.030  1.00 38.02           C  
-ATOM    749  C   ASP A  92      -1.961  29.756  51.860  1.00 38.68           C  
-ATOM    750  O   ASP A  92      -2.678  28.785  51.642  1.00 38.86           O  
-ATOM    751  CB  ASP A  92      -2.820  32.007  52.489  1.00 37.89           C  
-ATOM    752  CG  ASP A  92      -3.315  32.936  53.580  1.00 39.17           C  
-ATOM    753  OD1 ASP A  92      -3.595  32.469  54.705  1.00 40.28           O  
-ATOM    754  OD2 ASP A  92      -3.466  34.168  53.390  1.00 41.32           O  
-ATOM    755  N   ALA A  93      -0.895  30.057  51.122  1.00 39.99           N  
-ATOM    756  CA  ALA A  93      -0.447  29.247  49.989  1.00 41.39           C  
-ATOM    757  C   ALA A  93      -0.079  27.814  50.399  1.00 42.50           C  
-ATOM    758  O   ALA A  93      -0.131  26.894  49.576  1.00 42.33           O  
-ATOM    759  CB  ALA A  93       0.728  29.922  49.292  1.00 41.14           C  
-ATOM    760  N   SER A  94       0.284  27.644  51.672  1.00 43.91           N  
-ATOM    761  CA  SER A  94       0.607  26.341  52.249  1.00 45.49           C  
-ATOM    762  C   SER A  94      -0.583  25.710  52.987  1.00 46.78           C  
-ATOM    763  O   SER A  94      -0.402  24.770  53.758  1.00 46.76           O  
-ATOM    764  CB  SER A  94       1.794  26.464  53.211  1.00 45.25           C  
-ATOM    765  OG  SER A  94       3.020  26.562  52.510  1.00 45.59           O  
-ATOM    766  N   ALA A  95      -1.793  26.222  52.758  1.00 48.14           N  
-ATOM    767  CA  ALA A  95      -2.998  25.677  53.398  1.00 49.42           C  
-ATOM    768  C   ALA A  95      -3.217  24.202  53.068  1.00 50.11           C  
-ATOM    769  O   ALA A  95      -3.873  23.480  53.822  1.00 50.37           O  
-ATOM    770  CB  ALA A  95      -4.231  26.489  53.019  1.00 49.64           C  
-ATOM    771  N   LEU A  96      -2.662  23.776  51.935  1.00 50.78           N  
-ATOM    772  CA  LEU A  96      -2.740  22.400  51.468  1.00 51.24           C  
-ATOM    773  C   LEU A  96      -2.119  21.473  52.501  1.00 50.85           C  
-ATOM    774  O   LEU A  96      -2.793  21.001  53.423  1.00 51.14           O  
-ATOM    775  CB  LEU A  96      -1.992  22.273  50.135  1.00 51.75           C  
-ATOM    776  CG  LEU A  96      -2.536  21.293  49.094  1.00 53.10           C  
-ATOM    777  CD1 LEU A  96      -2.090  21.711  47.698  1.00 54.52           C  
-ATOM    778  CD2 LEU A  96      -2.108  19.858  49.404  1.00 54.46           C  
-ATOM    779  N   THR A  97      -0.833  21.202  52.310  1.00 50.06           N  
-ATOM    780  CA  THR A  97       0.015  20.610  53.330  1.00 49.13           C  
-ATOM    781  C   THR A  97       0.622  21.769  54.113  1.00 47.65           C  
-ATOM    782  O   THR A  97       0.602  22.906  53.655  1.00 47.81           O  
-ATOM    783  CB  THR A  97       1.134  19.806  52.672  1.00 49.40           C  
-ATOM    784  OG1 THR A  97       2.265  19.757  53.554  1.00 50.57           O  
-ATOM    785  CG2 THR A  97       1.671  20.555  51.461  1.00 49.55           C  
-ATOM    786  N   GLY A  98       1.192  21.480  55.274  1.00 45.85           N  
-ATOM    787  CA  GLY A  98       1.796  22.523  56.075  1.00 43.22           C  
-ATOM    788  C   GLY A  98       3.051  23.109  55.468  1.00 41.23           C  
-ATOM    789  O   GLY A  98       3.351  22.910  54.287  1.00 41.24           O  
-ATOM    790  N   ILE A  99       3.780  23.859  56.285  1.00 39.19           N  
-ATOM    791  CA  ILE A  99       5.116  24.294  55.918  1.00 36.51           C  
-ATOM    792  C   ILE A  99       6.064  23.205  56.406  1.00 35.04           C  
-ATOM    793  O   ILE A  99       5.980  22.792  57.560  1.00 34.74           O  
-ATOM    794  CB  ILE A  99       5.451  25.653  56.582  1.00 36.60           C  
-ATOM    795  CG1 ILE A  99       4.331  26.674  56.344  1.00 35.96           C  
-ATOM    796  CG2 ILE A  99       6.812  26.171  56.107  1.00 35.28           C  
-ATOM    797  CD1 ILE A  99       4.489  27.950  57.154  1.00 35.66           C  
-ATOM    798  N   PRO A 100       6.956  22.728  55.543  1.00 33.55           N  
-ATOM    799  CA  PRO A 100       7.968  21.759  55.968  1.00 32.79           C  
-ATOM    800  C   PRO A 100       8.662  22.250  57.238  1.00 32.03           C  
-ATOM    801  O   PRO A 100       9.028  23.429  57.336  1.00 31.73           O  
-ATOM    802  CB  PRO A 100       8.957  21.741  54.798  1.00 32.76           C  
-ATOM    803  CG  PRO A 100       8.159  22.176  53.619  1.00 33.03           C  
-ATOM    804  CD  PRO A 100       7.069  23.067  54.113  1.00 33.55           C  
-ATOM    805  N   LEU A 101       8.820  21.350  58.199  1.00 31.00           N  
-ATOM    806  CA  LEU A 101       9.422  21.677  59.484  1.00 30.62           C  
-ATOM    807  C   LEU A 101      10.810  22.323  59.367  1.00 29.65           C  
-ATOM    808  O   LEU A 101      11.086  23.272  60.101  1.00 29.70           O  
-ATOM    809  CB  LEU A 101       9.479  20.448  60.404  1.00 30.75           C  
-ATOM    810  CG  LEU A 101       9.100  20.607  61.883  1.00 32.39           C  
-ATOM    811  CD1 LEU A 101       9.964  21.609  62.614  1.00 33.14           C  
-ATOM    812  CD2 LEU A 101       7.631  20.981  62.048  1.00 35.34           C  
-ATOM    813  N   PRO A 102      11.679  21.833  58.473  1.00 28.67           N  
-ATOM    814  CA  PRO A 102      12.984  22.477  58.266  1.00 27.60           C  
-ATOM    815  C   PRO A 102      12.833  23.962  57.957  1.00 26.50           C  
-ATOM    816  O   PRO A 102      13.658  24.760  58.403  1.00 26.55           O  
-ATOM    817  CB  PRO A 102      13.546  21.734  57.054  1.00 27.99           C  
-ATOM    818  CG  PRO A 102      12.923  20.354  57.157  1.00 28.57           C  
-ATOM    819  CD  PRO A 102      11.528  20.637  57.616  1.00 28.51           C  
-ATOM    820  N   LEU A 103      11.764  24.321  57.250  1.00 24.93           N  
-ATOM    821  CA  LEU A 103      11.522  25.703  56.855  1.00 23.77           C  
-ATOM    822  C   LEU A 103      10.989  26.544  58.013  1.00 22.63           C  
-ATOM    823  O   LEU A 103      11.413  27.680  58.187  1.00 22.22           O  
-ATOM    824  CB  LEU A 103      10.582  25.772  55.640  1.00 23.60           C  
-ATOM    825  CG  LEU A 103      10.559  27.092  54.862  1.00 24.80           C  
-ATOM    826  CD1 LEU A 103      11.909  27.387  54.165  1.00 23.80           C  
-ATOM    827  CD2 LEU A 103       9.430  27.089  53.837  1.00 26.03           C  
-ATOM    828  N   ILE A 104      10.067  25.983  58.796  1.00 21.38           N  
-ATOM    829  CA  ILE A 104       9.571  26.632  60.008  1.00 20.54           C  
-ATOM    830  C   ILE A 104      10.722  26.931  60.973  1.00 20.16           C  
-ATOM    831  O   ILE A 104      10.794  28.012  61.561  1.00 19.39           O  
-ATOM    832  CB  ILE A 104       8.517  25.740  60.709  1.00 20.45           C  
-ATOM    833  CG1 ILE A 104       7.228  25.667  59.882  1.00 20.83           C  
-ATOM    834  CG2 ILE A 104       8.224  26.235  62.133  1.00 19.87           C  
-ATOM    835  CD1 ILE A 104       6.241  24.608  60.374  1.00 19.79           C  
-ATOM    836  N   LYS A 105      11.598  25.944  61.136  1.00 19.93           N  
-ATOM    837  CA  LYS A 105      12.755  26.034  62.016  1.00 20.14           C  
-ATOM    838  C   LYS A 105      13.727  27.101  61.504  1.00 19.59           C  
-ATOM    839  O   LYS A 105      14.226  27.905  62.283  1.00 19.22           O  
-ATOM    840  CB  LYS A 105      13.426  24.661  62.100  1.00 20.19           C  
-ATOM    841  CG  LYS A 105      14.441  24.492  63.209  1.00 22.53           C  
-ATOM    842  CD  LYS A 105      14.979  23.048  63.235  1.00 25.33           C  
-ATOM    843  CE  LYS A 105      13.965  22.090  63.857  1.00 26.75           C  
-ATOM    844  NZ  LYS A 105      14.480  20.692  63.860  1.00 30.36           N  
-ATOM    845  N   SER A 106      13.955  27.104  60.187  1.00 19.40           N  
-ATOM    846  CA  SER A 106      14.810  28.089  59.515  1.00 19.19           C  
-ATOM    847  C   SER A 106      14.257  29.504  59.686  1.00 18.97           C  
-ATOM    848  O   SER A 106      15.009  30.451  59.959  1.00 18.70           O  
-ATOM    849  CB  SER A 106      14.912  27.773  58.022  1.00 19.29           C  
-ATOM    850  OG  SER A 106      15.564  28.816  57.319  1.00 19.83           O  
-ATOM    851  N   TYR A 107      12.941  29.633  59.534  1.00 18.19           N  
-ATOM    852  CA  TYR A 107      12.283  30.926  59.629  1.00 18.21           C  
-ATOM    853  C   TYR A 107      12.310  31.430  61.062  1.00 17.62           C  
-ATOM    854  O   TYR A 107      12.651  32.585  61.293  1.00 17.81           O  
-ATOM    855  CB  TYR A 107      10.844  30.861  59.098  1.00 18.28           C  
-ATOM    856  CG  TYR A 107      10.733  30.921  57.597  1.00 18.63           C  
-ATOM    857  CD1 TYR A 107      11.865  31.102  56.797  1.00 18.74           C  
-ATOM    858  CD2 TYR A 107       9.486  30.819  56.965  1.00 19.02           C  
-ATOM    859  CE1 TYR A 107      11.765  31.165  55.413  1.00 17.92           C  
-ATOM    860  CE2 TYR A 107       9.377  30.897  55.572  1.00 19.16           C  
-ATOM    861  CZ  TYR A 107      10.523  31.062  54.807  1.00 19.52           C  
-ATOM    862  OH  TYR A 107      10.437  31.129  53.428  1.00 19.48           O  
-ATOM    863  N   LEU A 108      11.980  30.567  62.023  1.00 17.12           N  
-ATOM    864  CA  LEU A 108      12.028  30.967  63.433  1.00 16.74           C  
-ATOM    865  C   LEU A 108      13.440  31.416  63.852  1.00 17.02           C  
-ATOM    866  O   LEU A 108      13.605  32.436  64.526  1.00 17.09           O  
-ATOM    867  CB  LEU A 108      11.528  29.853  64.362  1.00 16.01           C  
-ATOM    868  CG  LEU A 108      11.438  30.282  65.836  1.00 14.89           C  
-ATOM    869  CD1 LEU A 108      10.658  31.609  65.981  1.00 13.79           C  
-ATOM    870  CD2 LEU A 108      10.838  29.205  66.728  1.00 11.93           C  
-ATOM    871  N   PHE A 109      14.442  30.634  63.457  1.00 17.47           N  
-ATOM    872  CA  PHE A 109      15.845  30.923  63.763  1.00 17.81           C  
-ATOM    873  C   PHE A 109      16.278  32.281  63.196  1.00 17.55           C  
-ATOM    874  O   PHE A 109      16.891  33.100  63.896  1.00 17.54           O  
-ATOM    875  CB  PHE A 109      16.734  29.792  63.213  1.00 18.27           C  
-ATOM    876  CG  PHE A 109      18.150  29.843  63.690  1.00 18.39           C  
-ATOM    877  CD1 PHE A 109      18.466  29.507  64.996  1.00 18.47           C  
-ATOM    878  CD2 PHE A 109      19.169  30.216  62.823  1.00 19.66           C  
-ATOM    879  CE1 PHE A 109      19.791  29.545  65.445  1.00 20.65           C  
-ATOM    880  CE2 PHE A 109      20.494  30.267  63.265  1.00 21.70           C  
-ATOM    881  CZ  PHE A 109      20.800  29.928  64.586  1.00 20.52           C  
-ATOM    882  N   GLN A 110      15.939  32.521  61.935  1.00 17.36           N  
-ATOM    883  CA  GLN A 110      16.220  33.800  61.287  1.00 16.83           C  
-ATOM    884  C   GLN A 110      15.456  34.964  61.922  1.00 16.91           C  
-ATOM    885  O   GLN A 110      16.022  36.046  62.120  1.00 16.53           O  
-ATOM    886  CB  GLN A 110      15.875  33.726  59.820  1.00 16.99           C  
-ATOM    887  CG  GLN A 110      16.840  32.907  58.992  1.00 17.84           C  
-ATOM    888  CD  GLN A 110      16.416  32.869  57.552  1.00 18.33           C  
-ATOM    889  OE1 GLN A 110      16.618  33.838  56.827  1.00 18.10           O  
-ATOM    890  NE2 GLN A 110      15.816  31.756  57.131  1.00 18.52           N  
-ATOM    891  N   LEU A 111      14.174  34.755  62.229  1.00 16.41           N  
-ATOM    892  CA  LEU A 111      13.405  35.789  62.932  1.00 16.77           C  
-ATOM    893  C   LEU A 111      14.068  36.155  64.264  1.00 16.32           C  
-ATOM    894  O   LEU A 111      14.224  37.327  64.580  1.00 16.48           O  
-ATOM    895  CB  LEU A 111      11.964  35.355  63.165  1.00 16.58           C  
-ATOM    896  CG  LEU A 111      11.121  35.204  61.890  1.00 17.10           C  
-ATOM    897  CD1 LEU A 111       9.829  34.461  62.210  1.00 17.49           C  
-ATOM    898  CD2 LEU A 111      10.849  36.557  61.237  1.00 16.82           C  
-ATOM    899  N   LEU A 112      14.484  35.140  65.009  1.00 16.30           N  
-ATOM    900  CA  LEU A 112      15.137  35.337  66.298  1.00 16.65           C  
-ATOM    901  C   LEU A 112      16.459  36.078  66.171  1.00 16.89           C  
-ATOM    902  O   LEU A 112      16.790  36.879  67.031  1.00 17.86           O  
-ATOM    903  CB  LEU A 112      15.344  34.000  67.012  1.00 15.66           C  
-ATOM    904  CG  LEU A 112      14.088  33.395  67.644  1.00 15.41           C  
-ATOM    905  CD1 LEU A 112      14.282  31.896  67.882  1.00 12.21           C  
-ATOM    906  CD2 LEU A 112      13.655  34.133  68.942  1.00 11.87           C  
-ATOM    907  N   GLN A 113      17.188  35.832  65.087  1.00 17.65           N  
-ATOM    908  CA  GLN A 113      18.454  36.516  64.830  1.00 18.02           C  
-ATOM    909  C   GLN A 113      18.216  38.002  64.586  1.00 17.56           C  
-ATOM    910  O   GLN A 113      18.933  38.843  65.103  1.00 17.38           O  
-ATOM    911  CB  GLN A 113      19.100  35.953  63.576  1.00 18.18           C  
-ATOM    912  CG  GLN A 113      20.053  34.789  63.769  1.00 19.60           C  
-ATOM    913  CD  GLN A 113      20.663  34.399  62.438  1.00 19.52           C  
-ATOM    914  OE1 GLN A 113      21.433  35.153  61.872  1.00 21.13           O  
-ATOM    915  NE2 GLN A 113      20.268  33.261  61.915  1.00 20.62           N  
-ATOM    916  N   GLY A 114      17.215  38.297  63.757  1.00 17.61           N  
-ATOM    917  CA  GLY A 114      16.862  39.657  63.398  1.00 16.78           C  
-ATOM    918  C   GLY A 114      16.422  40.393  64.638  1.00 16.55           C  
-ATOM    919  O   GLY A 114      16.835  41.530  64.866  1.00 16.66           O  
-ATOM    920  N   LEU A 115      15.619  39.717  65.465  1.00 16.31           N  
-ATOM    921  CA  LEU A 115      15.054  40.337  66.665  1.00 15.72           C  
-ATOM    922  C   LEU A 115      16.113  40.626  67.715  1.00 15.59           C  
-ATOM    923  O   LEU A 115      16.113  41.707  68.324  1.00 15.77           O  
-ATOM    924  CB  LEU A 115      13.933  39.479  67.259  1.00 15.83           C  
-ATOM    925  CG  LEU A 115      13.134  40.157  68.379  1.00 17.22           C  
-ATOM    926  CD1 LEU A 115      12.587  41.546  67.926  1.00 15.71           C  
-ATOM    927  CD2 LEU A 115      12.019  39.243  68.881  1.00 17.26           C  
-ATOM    928  N   ALA A 116      16.998  39.650  67.932  1.00 15.03           N  
-ATOM    929  CA  ALA A 116      18.129  39.807  68.844  1.00 15.19           C  
-ATOM    930  C   ALA A 116      19.004  40.984  68.402  1.00 14.77           C  
-ATOM    931  O   ALA A 116      19.506  41.744  69.232  1.00 15.16           O  
-ATOM    932  CB  ALA A 116      18.954  38.510  68.902  1.00 14.77           C  
-ATOM    933  N   PHE A 117      19.180  41.137  67.093  1.00 14.48           N  
-ATOM    934  CA  PHE A 117      19.913  42.284  66.574  1.00 14.35           C  
-ATOM    935  C   PHE A 117      19.176  43.576  66.911  1.00 14.08           C  
-ATOM    936  O   PHE A 117      19.801  44.527  67.392  1.00 13.80           O  
-ATOM    937  CB  PHE A 117      20.135  42.175  65.060  1.00 14.32           C  
-ATOM    938  CG  PHE A 117      21.150  43.163  64.522  1.00 15.13           C  
-ATOM    939  CD1 PHE A 117      22.518  42.853  64.523  1.00 14.41           C  
-ATOM    940  CD2 PHE A 117      20.749  44.398  64.039  1.00 12.63           C  
-ATOM    941  CE1 PHE A 117      23.458  43.747  64.018  1.00 14.32           C  
-ATOM    942  CE2 PHE A 117      21.689  45.310  63.530  1.00 12.63           C  
-ATOM    943  CZ  PHE A 117      23.045  44.985  63.526  1.00 12.82           C  
-ATOM    944  N   CYS A 118      17.860  43.625  66.663  1.00 14.29           N  
-ATOM    945  CA  CYS A 118      17.058  44.804  67.069  1.00 15.14           C  
-ATOM    946  C   CYS A 118      17.244  45.157  68.535  1.00 14.61           C  
-ATOM    947  O   CYS A 118      17.526  46.311  68.878  1.00 14.78           O  
-ATOM    948  CB  CYS A 118      15.555  44.611  66.804  1.00 15.14           C  
-ATOM    949  SG  CYS A 118      15.129  44.620  65.054  1.00 19.78           S  
-ATOM    950  N   HIS A 119      17.064  44.162  69.394  1.00 14.50           N  
-ATOM    951  CA  HIS A 119      17.102  44.368  70.838  1.00 15.08           C  
-ATOM    952  C   HIS A 119      18.510  44.770  71.329  1.00 15.58           C  
-ATOM    953  O   HIS A 119      18.643  45.595  72.237  1.00 15.62           O  
-ATOM    954  CB  HIS A 119      16.600  43.103  71.547  1.00 14.93           C  
-ATOM    955  CG  HIS A 119      15.137  42.843  71.351  1.00 15.17           C  
-ATOM    956  ND1 HIS A 119      14.533  41.664  71.732  1.00 15.72           N  
-ATOM    957  CD2 HIS A 119      14.156  43.617  70.823  1.00 14.06           C  
-ATOM    958  CE1 HIS A 119      13.242  41.725  71.453  1.00 15.79           C  
-ATOM    959  NE2 HIS A 119      12.988  42.897  70.899  1.00 15.00           N  
-ATOM    960  N   SER A 120      19.548  44.205  70.708  1.00 15.59           N  
-ATOM    961  CA  SER A 120      20.931  44.588  71.024  1.00 16.75           C  
-ATOM    962  C   SER A 120      21.208  46.029  70.628  1.00 16.75           C  
-ATOM    963  O   SER A 120      22.147  46.635  71.108  1.00 17.43           O  
-ATOM    964  CB  SER A 120      21.917  43.664  70.317  1.00 16.59           C  
-ATOM    965  OG  SER A 120      21.818  42.375  70.882  1.00 18.65           O  
-ATOM    966  N   HIS A 121      20.368  46.577  69.760  1.00 16.91           N  
-ATOM    967  CA  HIS A 121      20.524  47.953  69.302  1.00 17.29           C  
-ATOM    968  C   HIS A 121      19.411  48.838  69.837  1.00 16.95           C  
-ATOM    969  O   HIS A 121      19.012  49.811  69.199  1.00 17.60           O  
-ATOM    970  CB  HIS A 121      20.630  47.988  67.778  1.00 17.24           C  
-ATOM    971  CG  HIS A 121      21.885  47.355  67.282  1.00 19.39           C  
-ATOM    972  ND1 HIS A 121      22.075  45.989  67.282  1.00 22.23           N  
-ATOM    973  CD2 HIS A 121      23.045  47.898  66.850  1.00 20.41           C  
-ATOM    974  CE1 HIS A 121      23.288  45.720  66.831  1.00 22.72           C  
-ATOM    975  NE2 HIS A 121      23.897  46.863  66.565  1.00 22.05           N  
-ATOM    976  N   ARG A 122      18.946  48.485  71.036  1.00 16.19           N  
-ATOM    977  CA  ARG A 122      17.890  49.194  71.754  1.00 15.62           C  
-ATOM    978  C   ARG A 122      16.651  49.554  70.902  1.00 15.34           C  
-ATOM    979  O   ARG A 122      16.102  50.633  71.035  1.00 15.48           O  
-ATOM    980  CB  ARG A 122      18.456  50.406  72.556  1.00 15.66           C  
-ATOM    981  CG  ARG A 122      19.291  51.433  71.752  1.00 16.11           C  
-ATOM    982  CD  ARG A 122      18.468  52.543  71.110  1.00 18.04           C  
-ATOM    983  NE  ARG A 122      19.277  53.610  70.511  1.00 20.69           N  
-ATOM    984  CZ  ARG A 122      19.771  53.586  69.271  1.00 20.89           C  
-ATOM    985  NH1 ARG A 122      19.556  52.545  68.466  1.00 21.28           N  
-ATOM    986  NH2 ARG A 122      20.477  54.615  68.834  1.00 21.65           N  
-ATOM    987  N   VAL A 123      16.210  48.638  70.040  1.00 15.33           N  
-ATOM    988  CA  VAL A 123      14.979  48.855  69.254  1.00 14.90           C  
-ATOM    989  C   VAL A 123      13.944  47.779  69.566  1.00 14.84           C  
-ATOM    990  O   VAL A 123      14.240  46.579  69.495  1.00 14.45           O  
-ATOM    991  CB  VAL A 123      15.244  48.897  67.720  1.00 15.08           C  
-ATOM    992  CG1 VAL A 123      13.932  48.926  66.929  1.00 14.98           C  
-ATOM    993  CG2 VAL A 123      16.118  50.117  67.355  1.00 15.47           C  
-ATOM    994  N   LEU A 124      12.741  48.227  69.922  1.00 14.86           N  
-ATOM    995  CA  LEU A 124      11.571  47.361  70.038  1.00 14.97           C  
-ATOM    996  C   LEU A 124      10.805  47.459  68.728  1.00 15.30           C  
-ATOM    997  O   LEU A 124      10.598  48.564  68.219  1.00 15.31           O  
-ATOM    998  CB  LEU A 124      10.665  47.792  71.214  1.00 14.34           C  
-ATOM    999  CG  LEU A 124      11.217  47.867  72.650  1.00 14.24           C  
-ATOM   1000  CD1 LEU A 124      10.160  48.434  73.644  1.00 14.04           C  
-ATOM   1001  CD2 LEU A 124      11.727  46.544  73.150  1.00 14.59           C  
-ATOM   1002  N   HIS A 125      10.387  46.319  68.179  1.00 15.59           N  
-ATOM   1003  CA  HIS A 125       9.607  46.335  66.936  1.00 16.36           C  
-ATOM   1004  C   HIS A 125       8.128  46.728  67.135  1.00 16.67           C  
-ATOM   1005  O   HIS A 125       7.623  47.623  66.462  1.00 16.54           O  
-ATOM   1006  CB  HIS A 125       9.708  45.004  66.182  1.00 15.61           C  
-ATOM   1007  CG  HIS A 125       9.063  45.037  64.829  1.00 17.09           C  
-ATOM   1008  ND1 HIS A 125       7.702  44.891  64.648  1.00 17.39           N  
-ATOM   1009  CD2 HIS A 125       9.590  45.197  63.590  1.00 17.87           C  
-ATOM   1010  CE1 HIS A 125       7.420  44.961  63.358  1.00 15.69           C  
-ATOM   1011  NE2 HIS A 125       8.546  45.142  62.693  1.00 15.86           N  
-ATOM   1012  N   ARG A 126       7.445  45.988  68.008  1.00 17.31           N  
-ATOM   1013  CA  ARG A 126       6.099  46.303  68.499  1.00 17.96           C  
-ATOM   1014  C   ARG A 126       4.949  46.022  67.527  1.00 18.24           C  
-ATOM   1015  O   ARG A 126       3.813  46.423  67.775  1.00 18.80           O  
-ATOM   1016  CB  ARG A 126       6.021  47.742  69.054  1.00 18.12           C  
-ATOM   1017  CG  ARG A 126       7.097  48.063  70.108  1.00 17.74           C  
-ATOM   1018  CD  ARG A 126       6.884  49.358  70.873  1.00 15.31           C  
-ATOM   1019  NE  ARG A 126       6.730  50.516  69.992  1.00 15.08           N  
-ATOM   1020  CZ  ARG A 126       6.312  51.711  70.400  1.00 15.67           C  
-ATOM   1021  NH1 ARG A 126       6.014  51.913  71.679  1.00 15.10           N  
-ATOM   1022  NH2 ARG A 126       6.194  52.708  69.535  1.00 16.27           N  
-ATOM   1023  N   ASP A 127       5.225  45.302  66.450  1.00 18.24           N  
-ATOM   1024  CA  ASP A 127       4.173  44.895  65.525  1.00 18.72           C  
-ATOM   1025  C   ASP A 127       4.621  43.686  64.713  1.00 18.91           C  
-ATOM   1026  O   ASP A 127       4.431  43.627  63.494  1.00 18.68           O  
-ATOM   1027  CB  ASP A 127       3.725  46.057  64.620  1.00 18.93           C  
-ATOM   1028  CG  ASP A 127       2.292  45.885  64.086  1.00 20.98           C  
-ATOM   1029  OD1 ASP A 127       1.442  45.230  64.731  1.00 22.81           O  
-ATOM   1030  OD2 ASP A 127       1.919  46.374  63.008  1.00 24.57           O  
-ATOM   1031  N   LEU A 128       5.205  42.712  65.406  1.00 19.12           N  
-ATOM   1032  CA  LEU A 128       5.556  41.451  64.772  1.00 19.66           C  
-ATOM   1033  C   LEU A 128       4.307  40.605  64.548  1.00 20.22           C  
-ATOM   1034  O   LEU A 128       3.676  40.110  65.493  1.00 20.62           O  
-ATOM   1035  CB  LEU A 128       6.608  40.690  65.578  1.00 19.32           C  
-ATOM   1036  CG  LEU A 128       7.997  41.334  65.687  1.00 18.33           C  
-ATOM   1037  CD1 LEU A 128       8.850  40.533  66.669  1.00 17.60           C  
-ATOM   1038  CD2 LEU A 128       8.687  41.463  64.333  1.00 17.04           C  
-ATOM   1039  N   LYS A 129       3.938  40.499  63.284  1.00 20.45           N  
-ATOM   1040  CA  LYS A 129       2.823  39.676  62.834  1.00 21.07           C  
-ATOM   1041  C   LYS A 129       3.250  39.197  61.456  1.00 20.83           C  
-ATOM   1042  O   LYS A 129       4.073  39.848  60.833  1.00 21.11           O  
-ATOM   1043  CB  LYS A 129       1.536  40.505  62.747  1.00 20.73           C  
-ATOM   1044  CG  LYS A 129       1.643  41.773  61.905  1.00 21.88           C  
-ATOM   1045  CD  LYS A 129       0.292  42.466  61.814  1.00 24.71           C  
-ATOM   1046  CE  LYS A 129       0.388  43.768  61.051  1.00 26.11           C  
-ATOM   1047  NZ  LYS A 129      -0.767  44.665  61.410  1.00 29.39           N  
-ATOM   1048  N   PRO A 130       2.683  38.094  60.974  1.00 21.30           N  
-ATOM   1049  CA  PRO A 130       3.100  37.469  59.711  1.00 21.48           C  
-ATOM   1050  C   PRO A 130       3.120  38.406  58.508  1.00 21.69           C  
-ATOM   1051  O   PRO A 130       3.972  38.224  57.622  1.00 22.19           O  
-ATOM   1052  CB  PRO A 130       2.039  36.385  59.500  1.00 21.98           C  
-ATOM   1053  CG  PRO A 130       1.599  36.045  60.875  1.00 21.76           C  
-ATOM   1054  CD  PRO A 130       1.571  37.355  61.604  1.00 21.43           C  
-ATOM   1055  N   GLN A 131       2.212  39.379  58.474  1.00 21.37           N  
-ATOM   1056  CA  GLN A 131       2.148  40.354  57.386  1.00 21.48           C  
-ATOM   1057  C   GLN A 131       3.372  41.270  57.321  1.00 20.79           C  
-ATOM   1058  O   GLN A 131       3.655  41.844  56.268  1.00 20.49           O  
-ATOM   1059  CB  GLN A 131       0.882  41.211  57.490  1.00 22.49           C  
-ATOM   1060  CG  GLN A 131      -0.428  40.431  57.457  1.00 25.26           C  
-ATOM   1061  CD  GLN A 131      -1.006  40.201  58.845  1.00 28.92           C  
-ATOM   1062  OE1 GLN A 131      -0.380  39.570  59.705  1.00 27.81           O  
-ATOM   1063  NE2 GLN A 131      -2.203  40.728  59.070  1.00 32.54           N  
-ATOM   1064  N   ASN A 132       4.090  41.411  58.438  1.00 20.42           N  
-ATOM   1065  CA  ASN A 132       5.308  42.238  58.485  1.00 19.48           C  
-ATOM   1066  C   ASN A 132       6.607  41.441  58.404  1.00 19.41           C  
-ATOM   1067  O   ASN A 132       7.685  41.952  58.697  1.00 19.78           O  
-ATOM   1068  CB  ASN A 132       5.310  43.122  59.733  1.00 19.15           C  
-ATOM   1069  CG  ASN A 132       4.222  44.190  59.696  1.00 18.17           C  
-ATOM   1070  OD1 ASN A 132       3.763  44.568  58.633  1.00 19.83           O  
-ATOM   1071  ND2 ASN A 132       3.808  44.665  60.862  1.00 14.16           N  
-ATOM   1072  N   LEU A 133       6.504  40.179  58.011  1.00 19.66           N  
-ATOM   1073  CA  LEU A 133       7.672  39.308  57.900  1.00 18.93           C  
-ATOM   1074  C   LEU A 133       7.790  38.917  56.452  1.00 19.20           C  
-ATOM   1075  O   LEU A 133       6.886  38.293  55.902  1.00 20.25           O  
-ATOM   1076  CB  LEU A 133       7.504  38.076  58.786  1.00 18.48           C  
-ATOM   1077  CG  LEU A 133       7.303  38.359  60.278  1.00 19.24           C  
-ATOM   1078  CD1 LEU A 133       7.141  37.062  61.073  1.00 18.24           C  
-ATOM   1079  CD2 LEU A 133       8.452  39.219  60.842  1.00 19.05           C  
-ATOM   1080  N   LEU A 134       8.881  39.313  55.812  1.00 18.59           N  
-ATOM   1081  CA  LEU A 134       8.984  39.163  54.366  1.00 18.48           C  
-ATOM   1082  C   LEU A 134       9.963  38.057  53.976  1.00 18.55           C  
-ATOM   1083  O   LEU A 134      11.050  37.923  54.572  1.00 18.03           O  
-ATOM   1084  CB  LEU A 134       9.359  40.496  53.706  1.00 17.92           C  
-ATOM   1085  CG  LEU A 134       8.416  41.688  53.953  1.00 19.52           C  
-ATOM   1086  CD1 LEU A 134       8.918  42.950  53.265  1.00 20.02           C  
-ATOM   1087  CD2 LEU A 134       6.993  41.393  53.507  1.00 19.24           C  
-ATOM   1088  N   ILE A 135       9.565  37.264  52.985  1.00 18.18           N  
-ATOM   1089  CA  ILE A 135      10.392  36.167  52.512  1.00 19.27           C  
-ATOM   1090  C   ILE A 135      10.840  36.354  51.070  1.00 19.62           C  
-ATOM   1091  O   ILE A 135      10.176  37.026  50.282  1.00 19.12           O  
-ATOM   1092  CB  ILE A 135       9.688  34.786  52.723  1.00 19.34           C  
-ATOM   1093  CG1 ILE A 135       8.371  34.677  51.932  1.00 20.04           C  
-ATOM   1094  CG2 ILE A 135       9.439  34.542  54.188  1.00 19.07           C  
-ATOM   1095  CD1 ILE A 135       7.888  33.219  51.751  1.00 21.05           C  
-ATOM   1096  N   ASN A 136      11.992  35.780  50.741  1.00 20.37           N  
-ATOM   1097  CA  ASN A 136      12.466  35.788  49.370  1.00 21.10           C  
-ATOM   1098  C   ASN A 136      12.603  34.365  48.843  1.00 22.09           C  
-ATOM   1099  O   ASN A 136      12.294  33.405  49.556  1.00 22.45           O  
-ATOM   1100  CB  ASN A 136      13.759  36.612  49.214  1.00 20.65           C  
-ATOM   1101  CG  ASN A 136      14.989  35.937  49.825  1.00 21.21           C  
-ATOM   1102  OD1 ASN A 136      14.983  34.748  50.164  1.00 20.09           O  
-ATOM   1103  ND2 ASN A 136      16.062  36.712  49.969  1.00 21.82           N  
-ATOM   1104  N   THR A 137      13.063  34.232  47.604  1.00 23.03           N  
-ATOM   1105  CA  THR A 137      13.154  32.929  46.960  1.00 24.15           C  
-ATOM   1106  C   THR A 137      14.364  32.133  47.416  1.00 25.04           C  
-ATOM   1107  O   THR A 137      14.439  30.938  47.144  1.00 25.59           O  
-ATOM   1108  CB  THR A 137      13.176  33.072  45.420  1.00 24.39           C  
-ATOM   1109  OG1 THR A 137      14.293  33.891  45.023  1.00 25.34           O  
-ATOM   1110  CG2 THR A 137      11.941  33.829  44.924  1.00 23.26           C  
-ATOM   1111  N   GLU A 138      15.301  32.773  48.118  1.00 25.64           N  
-ATOM   1112  CA  GLU A 138      16.506  32.077  48.573  1.00 26.19           C  
-ATOM   1113  C   GLU A 138      16.405  31.457  49.981  1.00 25.35           C  
-ATOM   1114  O   GLU A 138      17.355  30.823  50.460  1.00 25.58           O  
-ATOM   1115  CB  GLU A 138      17.735  32.986  48.460  1.00 26.76           C  
-ATOM   1116  CG  GLU A 138      18.246  33.146  47.033  1.00 30.58           C  
-ATOM   1117  CD  GLU A 138      18.704  31.831  46.416  1.00 36.06           C  
-ATOM   1118  OE1 GLU A 138      19.614  31.173  46.978  1.00 38.33           O  
-ATOM   1119  OE2 GLU A 138      18.156  31.449  45.358  1.00 38.66           O  
-ATOM   1120  N   GLY A 139      15.262  31.626  50.637  1.00 23.95           N  
-ATOM   1121  CA  GLY A 139      15.073  31.055  51.958  1.00 22.30           C  
-ATOM   1122  C   GLY A 139      15.219  32.038  53.099  1.00 21.32           C  
-ATOM   1123  O   GLY A 139      15.062  31.667  54.274  1.00 21.29           O  
-ATOM   1124  N   ALA A 140      15.524  33.292  52.772  1.00 19.83           N  
-ATOM   1125  CA  ALA A 140      15.599  34.325  53.798  1.00 19.06           C  
-ATOM   1126  C   ALA A 140      14.215  34.739  54.289  1.00 18.61           C  
-ATOM   1127  O   ALA A 140      13.235  34.651  53.549  1.00 18.98           O  
-ATOM   1128  CB  ALA A 140      16.375  35.527  53.293  1.00 18.98           C  
-ATOM   1129  N   ILE A 141      14.137  35.136  55.558  1.00 18.24           N  
-ATOM   1130  CA  ILE A 141      12.983  35.842  56.093  1.00 17.99           C  
-ATOM   1131  C   ILE A 141      13.497  37.072  56.849  1.00 17.71           C  
-ATOM   1132  O   ILE A 141      14.545  37.008  57.496  1.00 17.12           O  
-ATOM   1133  CB  ILE A 141      12.066  34.917  56.981  1.00 18.16           C  
-ATOM   1134  CG1 ILE A 141      10.749  35.636  57.331  1.00 18.13           C  
-ATOM   1135  CG2 ILE A 141      12.761  34.478  58.239  1.00 17.75           C  
-ATOM   1136  CD1 ILE A 141       9.668  34.725  57.944  1.00 15.96           C  
-ATOM   1137  N   LYS A 142      12.775  38.187  56.739  1.00 17.62           N  
-ATOM   1138  CA  LYS A 142      13.228  39.464  57.294  1.00 18.41           C  
-ATOM   1139  C   LYS A 142      12.114  40.223  57.992  1.00 18.85           C  
-ATOM   1140  O   LYS A 142      10.973  40.254  57.498  1.00 19.25           O  
-ATOM   1141  CB  LYS A 142      13.846  40.349  56.199  1.00 18.34           C  
-ATOM   1142  CG  LYS A 142      14.727  39.580  55.206  1.00 17.71           C  
-ATOM   1143  CD  LYS A 142      15.714  40.478  54.446  1.00 18.72           C  
-ATOM   1144  CE  LYS A 142      16.605  39.616  53.526  1.00 17.29           C  
-ATOM   1145  NZ  LYS A 142      17.700  40.380  52.907  1.00 17.91           N  
-ATOM   1146  N   LEU A 143      12.453  40.836  59.129  1.00 18.43           N  
-ATOM   1147  CA  LEU A 143      11.545  41.762  59.801  1.00 18.62           C  
-ATOM   1148  C   LEU A 143      11.366  43.004  58.959  1.00 18.45           C  
-ATOM   1149  O   LEU A 143      12.342  43.588  58.478  1.00 18.00           O  
-ATOM   1150  CB  LEU A 143      12.029  42.157  61.208  1.00 18.51           C  
-ATOM   1151  CG  LEU A 143      12.603  41.148  62.212  1.00 19.87           C  
-ATOM   1152  CD1 LEU A 143      12.658  41.745  63.626  1.00 21.31           C  
-ATOM   1153  CD2 LEU A 143      11.856  39.858  62.232  1.00 20.35           C  
-ATOM   1154  N   ALA A 144      10.110  43.411  58.780  1.00 18.37           N  
-ATOM   1155  CA  ALA A 144       9.831  44.637  58.052  1.00 18.31           C  
-ATOM   1156  C   ALA A 144       8.804  45.493  58.781  1.00 18.64           C  
-ATOM   1157  O   ALA A 144       8.253  45.071  59.803  1.00 18.54           O  
-ATOM   1158  CB  ALA A 144       9.390  44.331  56.615  1.00 17.79           C  
-ATOM   1159  N   ASP A 145       8.568  46.696  58.247  1.00 18.71           N  
-ATOM   1160  CA  ASP A 145       7.631  47.674  58.804  1.00 19.04           C  
-ATOM   1161  C   ASP A 145       8.002  48.131  60.214  1.00 18.69           C  
-ATOM   1162  O   ASP A 145       7.503  47.604  61.199  1.00 18.93           O  
-ATOM   1163  CB  ASP A 145       6.177  47.184  58.761  1.00 18.99           C  
-ATOM   1164  CG  ASP A 145       5.172  48.335  58.824  1.00 20.68           C  
-ATOM   1165  OD1 ASP A 145       5.568  49.478  59.203  1.00 20.63           O  
-ATOM   1166  OD2 ASP A 145       3.967  48.194  58.499  1.00 21.64           O  
-ATOM   1167  N   PHE A 146       8.856  49.142  60.287  1.00 18.72           N  
-ATOM   1168  CA  PHE A 146       9.359  49.646  61.556  1.00 18.91           C  
-ATOM   1169  C   PHE A 146       8.672  50.957  61.942  1.00 19.62           C  
-ATOM   1170  O   PHE A 146       9.166  51.687  62.799  1.00 20.43           O  
-ATOM   1171  CB  PHE A 146      10.893  49.794  61.499  1.00 18.17           C  
-ATOM   1172  CG  PHE A 146      11.632  48.501  61.757  1.00 17.36           C  
-ATOM   1173  CD1 PHE A 146      11.678  47.498  60.785  1.00 16.33           C  
-ATOM   1174  CD2 PHE A 146      12.247  48.268  62.984  1.00 16.62           C  
-ATOM   1175  CE1 PHE A 146      12.349  46.290  61.020  1.00 14.90           C  
-ATOM   1176  CE2 PHE A 146      12.924  47.062  63.233  1.00 15.67           C  
-ATOM   1177  CZ  PHE A 146      12.970  46.073  62.247  1.00 14.95           C  
-ATOM   1178  N   GLY A 147       7.527  51.241  61.315  1.00 19.70           N  
-ATOM   1179  CA  GLY A 147       6.727  52.422  61.624  1.00 19.83           C  
-ATOM   1180  C   GLY A 147       6.249  52.488  63.072  1.00 20.57           C  
-ATOM   1181  O   GLY A 147       6.149  53.581  63.651  1.00 20.85           O  
-ATOM   1182  N   LEU A 148       5.975  51.324  63.656  1.00 19.85           N  
-ATOM   1183  CA  LEU A 148       5.500  51.223  65.035  1.00 20.03           C  
-ATOM   1184  C   LEU A 148       6.615  50.959  66.063  1.00 19.68           C  
-ATOM   1185  O   LEU A 148       6.349  50.883  67.250  1.00 19.78           O  
-ATOM   1186  CB  LEU A 148       4.397  50.157  65.127  1.00 20.21           C  
-ATOM   1187  CG  LEU A 148       2.995  50.590  64.645  1.00 22.01           C  
-ATOM   1188  CD1 LEU A 148       3.007  51.065  63.225  1.00 24.25           C  
-ATOM   1189  CD2 LEU A 148       1.992  49.465  64.758  1.00 23.61           C  
-ATOM   1190  N   ALA A 149       7.860  50.872  65.598  1.00 19.52           N  
-ATOM   1191  CA  ALA A 149       9.012  50.615  66.443  1.00 19.42           C  
-ATOM   1192  C   ALA A 149       9.399  51.839  67.280  1.00 19.80           C  
-ATOM   1193  O   ALA A 149       8.909  52.941  67.041  1.00 19.72           O  
-ATOM   1194  CB  ALA A 149      10.184  50.175  65.580  1.00 19.62           C  
-ATOM   1195  N   ARG A 150      10.257  51.633  68.274  1.00 19.92           N  
-ATOM   1196  CA  ARG A 150      10.890  52.742  68.982  1.00 20.30           C  
-ATOM   1197  C   ARG A 150      12.221  52.378  69.646  1.00 19.77           C  
-ATOM   1198  O   ARG A 150      12.462  51.212  69.981  1.00 19.50           O  
-ATOM   1199  CB  ARG A 150       9.923  53.440  69.961  1.00 21.16           C  
-ATOM   1200  CG  ARG A 150       9.749  52.816  71.321  1.00 21.71           C  
-ATOM   1201  CD  ARG A 150       9.815  53.836  72.459  1.00 23.85           C  
-ATOM   1202  NE  ARG A 150       8.639  54.705  72.584  1.00 22.57           N  
-ATOM   1203  CZ  ARG A 150       8.703  56.009  72.889  1.00 23.13           C  
-ATOM   1204  NH1 ARG A 150       9.884  56.601  73.085  1.00 22.19           N  
-ATOM   1205  NH2 ARG A 150       7.592  56.729  73.010  1.00 22.30           N  
-ATOM   1206  N   ALA A 151      13.085  53.381  69.792  1.00 18.50           N  
-ATOM   1207  CA  ALA A 151      14.342  53.202  70.493  1.00 18.75           C  
-ATOM   1208  C   ALA A 151      14.042  53.270  71.980  1.00 18.91           C  
-ATOM   1209  O   ALA A 151      13.493  54.263  72.458  1.00 19.44           O  
-ATOM   1210  CB  ALA A 151      15.345  54.295  70.109  1.00 17.89           C  
-ATOM   1211  N   PHE A 152      14.408  52.233  72.714  1.00 18.82           N  
-ATOM   1212  CA  PHE A 152      14.142  52.229  74.147  1.00 19.12           C  
-ATOM   1213  C   PHE A 152      15.374  52.603  74.953  1.00 19.73           C  
-ATOM   1214  O   PHE A 152      16.496  52.626  74.425  1.00 19.83           O  
-ATOM   1215  CB  PHE A 152      13.485  50.910  74.611  1.00 18.63           C  
-ATOM   1216  CG  PHE A 152      14.347  49.679  74.463  1.00 17.63           C  
-ATOM   1217  CD1 PHE A 152      14.370  48.966  73.273  1.00 16.64           C  
-ATOM   1218  CD2 PHE A 152      15.096  49.206  75.537  1.00 16.89           C  
-ATOM   1219  CE1 PHE A 152      15.129  47.808  73.145  1.00 15.91           C  
-ATOM   1220  CE2 PHE A 152      15.879  48.050  75.419  1.00 15.87           C  
-ATOM   1221  CZ  PHE A 152      15.900  47.361  74.214  1.00 16.69           C  
-ATOM   1222  N   GLY A 153      15.148  52.958  76.214  1.00 20.47           N  
-ATOM   1223  CA  GLY A 153      16.228  53.253  77.141  1.00 20.38           C  
-ATOM   1224  C   GLY A 153      16.368  52.124  78.134  1.00 20.85           C  
-ATOM   1225  O   GLY A 153      15.496  51.249  78.236  1.00 20.76           O  
-ATOM   1226  N   VAL A 154      17.472  52.135  78.870  1.00 21.32           N  
-ATOM   1227  CA  VAL A 154      17.734  51.127  79.883  1.00 21.74           C  
-ATOM   1228  C   VAL A 154      17.897  51.830  81.240  1.00 21.91           C  
-ATOM   1229  O   VAL A 154      18.763  52.704  81.382  1.00 21.74           O  
-ATOM   1230  CB  VAL A 154      18.995  50.285  79.536  1.00 21.84           C  
-ATOM   1231  CG1 VAL A 154      19.308  49.276  80.647  1.00 21.99           C  
-ATOM   1232  CG2 VAL A 154      18.819  49.539  78.215  1.00 23.01           C  
-ATOM   1233  N   PRO A 155      17.046  51.508  82.222  1.00 22.31           N  
-ATOM   1234  CA  PRO A 155      15.853  50.677  82.037  1.00 22.27           C  
-ATOM   1235  C   PRO A 155      14.771  51.458  81.287  1.00 22.34           C  
-ATOM   1236  O   PRO A 155      14.874  52.670  81.151  1.00 21.65           O  
-ATOM   1237  CB  PRO A 155      15.396  50.412  83.477  1.00 22.11           C  
-ATOM   1238  CG  PRO A 155      15.825  51.613  84.217  1.00 22.81           C  
-ATOM   1239  CD  PRO A 155      17.174  51.968  83.620  1.00 22.25           C  
-ATOM   1240  N   VAL A 156      13.754  50.763  80.791  1.00 23.05           N  
-ATOM   1241  CA  VAL A 156      12.715  51.415  79.994  1.00 23.67           C  
-ATOM   1242  C   VAL A 156      11.836  52.330  80.850  1.00 23.85           C  
-ATOM   1243  O   VAL A 156      11.762  52.182  82.065  1.00 23.96           O  
-ATOM   1244  CB  VAL A 156      11.852  50.382  79.226  1.00 23.92           C  
-ATOM   1245  CG1 VAL A 156      12.745  49.473  78.383  1.00 23.64           C  
-ATOM   1246  CG2 VAL A 156      10.964  49.551  80.186  1.00 23.65           C  
-ATOM   1247  N   ARG A 157      11.201  53.303  80.218  1.00 24.62           N  
-ATOM   1248  CA  ARG A 157      10.117  54.024  80.883  1.00 24.72           C  
-ATOM   1249  C   ARG A 157       8.805  53.661  80.201  1.00 24.27           C  
-ATOM   1250  O   ARG A 157       8.769  52.794  79.312  1.00 23.74           O  
-ATOM   1251  CB  ARG A 157      10.362  55.547  80.902  1.00 25.45           C  
-ATOM   1252  CG  ARG A 157      10.568  56.180  79.546  1.00 26.43           C  
-ATOM   1253  CD  ARG A 157      10.726  57.696  79.563  1.00 29.49           C  
-ATOM   1254  NE  ARG A 157      10.131  58.257  78.349  1.00 32.10           N  
-ATOM   1255  CZ  ARG A 157      10.806  58.529  77.241  1.00 32.63           C  
-ATOM   1256  NH1 ARG A 157      12.119  58.336  77.190  1.00 33.79           N  
-ATOM   1257  NH2 ARG A 157      10.169  59.013  76.186  1.00 33.26           N  
-ATOM   1258  N   THR A 158       7.724  54.305  80.632  1.00 24.34           N  
-ATOM   1259  CA  THR A 158       6.411  54.055  80.060  1.00 23.99           C  
-ATOM   1260  C   THR A 158       6.389  54.567  78.630  1.00 23.50           C  
-ATOM   1261  O   THR A 158       6.797  55.694  78.369  1.00 23.35           O  
-ATOM   1262  CB  THR A 158       5.323  54.710  80.924  1.00 24.10           C  
-ATOM   1263  OG1 THR A 158       5.296  54.046  82.193  1.00 25.79           O  
-ATOM   1264  CG2 THR A 158       3.918  54.430  80.366  1.00 23.68           C  
-ATOM   1265  N   TYR A 159       5.946  53.712  77.712  1.00 23.14           N  
-ATOM   1266  CA  TYR A 159       5.806  54.068  76.301  1.00 23.03           C  
-ATOM   1267  C   TYR A 159       4.337  53.886  75.905  1.00 23.12           C  
-ATOM   1268  O   TYR A 159       3.485  53.640  76.773  1.00 22.68           O  
-ATOM   1269  CB  TYR A 159       6.730  53.200  75.425  1.00 23.15           C  
-ATOM   1270  CG  TYR A 159       8.199  53.182  75.842  1.00 23.37           C  
-ATOM   1271  CD1 TYR A 159       8.911  54.367  76.055  1.00 23.27           C  
-ATOM   1272  CD2 TYR A 159       8.874  51.976  76.009  1.00 23.74           C  
-ATOM   1273  CE1 TYR A 159      10.253  54.338  76.434  1.00 23.93           C  
-ATOM   1274  CE2 TYR A 159      10.207  51.939  76.383  1.00 23.13           C  
-ATOM   1275  CZ  TYR A 159      10.886  53.117  76.601  1.00 24.06           C  
-ATOM   1276  OH  TYR A 159      12.204  53.064  76.975  1.00 25.68           O  
-HETATM 1277  N   TPO A 160       4.043  54.009  74.610  1.00 23.07           N  
-HETATM 1278  CA  TPO A 160       2.671  53.953  74.129  1.00 23.78           C  
-HETATM 1279  CB  TPO A 160       2.630  54.159  72.618  1.00 23.89           C  
-HETATM 1280  CG2 TPO A 160       1.197  54.241  72.093  1.00 22.31           C  
-HETATM 1281  OG1 TPO A 160       3.310  55.383  72.314  1.00 24.64           O  
-HETATM 1282  P   TPO A 160       4.763  55.367  71.608  1.00 24.78           P  
-HETATM 1283  O1P TPO A 160       5.358  56.838  71.553  1.00 25.13           O  
-HETATM 1284  O2P TPO A 160       5.748  54.447  72.434  1.00 23.01           O  
-HETATM 1285  O3P TPO A 160       4.612  54.802  70.130  1.00 24.38           O  
-HETATM 1286  C   TPO A 160       1.993  52.670  74.557  1.00 24.31           C  
-HETATM 1287  O   TPO A 160       2.559  51.583  74.459  1.00 23.47           O  
-ATOM   1288  N   HIS A 161       0.770  52.813  75.064  1.00 25.13           N  
-ATOM   1289  CA  HIS A 161      -0.028  51.672  75.497  1.00 26.49           C  
-ATOM   1290  C   HIS A 161      -0.752  51.009  74.341  1.00 26.70           C  
-ATOM   1291  O   HIS A 161      -0.844  51.574  73.247  1.00 26.69           O  
-ATOM   1292  CB  HIS A 161      -1.019  52.074  76.605  1.00 27.41           C  
-ATOM   1293  CG  HIS A 161      -2.018  53.116  76.199  1.00 29.95           C  
-ATOM   1294  ND1 HIS A 161      -2.692  53.889  77.119  1.00 33.66           N  
-ATOM   1295  CD2 HIS A 161      -2.468  53.506  74.981  1.00 33.15           C  
-ATOM   1296  CE1 HIS A 161      -3.510  54.711  76.489  1.00 35.12           C  
-ATOM   1297  NE2 HIS A 161      -3.393  54.502  75.190  1.00 35.29           N  
-ATOM   1298  N   GLU A 162      -1.252  49.800  74.592  1.00 27.30           N  
-ATOM   1299  CA  GLU A 162      -2.088  49.060  73.644  1.00 27.69           C  
-ATOM   1300  C   GLU A 162      -1.387  48.808  72.312  1.00 27.41           C  
-ATOM   1301  O   GLU A 162      -2.048  48.675  71.273  1.00 27.87           O  
-ATOM   1302  CB  GLU A 162      -3.427  49.782  73.394  1.00 28.41           C  
-ATOM   1303  CG  GLU A 162      -4.274  50.022  74.636  1.00 31.15           C  
-ATOM   1304  CD  GLU A 162      -5.548  50.798  74.347  1.00 35.03           C  
-ATOM   1305  OE1 GLU A 162      -6.027  50.793  73.187  1.00 38.26           O  
-ATOM   1306  OE2 GLU A 162      -6.083  51.411  75.291  1.00 36.97           O  
-ATOM   1307  N   VAL A 163      -0.056  48.747  72.342  1.00 26.01           N  
-ATOM   1308  CA  VAL A 163       0.718  48.493  71.135  1.00 24.81           C  
-ATOM   1309  C   VAL A 163       0.630  47.025  70.745  1.00 23.95           C  
-ATOM   1310  O   VAL A 163       0.267  46.176  71.567  1.00 23.99           O  
-ATOM   1311  CB  VAL A 163       2.219  48.892  71.291  1.00 24.85           C  
-ATOM   1312  CG1 VAL A 163       2.375  50.407  71.340  1.00 24.39           C  
-ATOM   1313  CG2 VAL A 163       2.843  48.236  72.517  1.00 24.96           C  
-ATOM   1314  N   VAL A 164       0.985  46.749  69.490  1.00 22.28           N  
-ATOM   1315  CA  VAL A 164       1.012  45.416  68.910  1.00 21.00           C  
-ATOM   1316  C   VAL A 164      -0.370  45.030  68.428  1.00 20.60           C  
-ATOM   1317  O   VAL A 164      -1.334  45.137  69.162  1.00 21.04           O  
-ATOM   1318  CB  VAL A 164       1.613  44.315  69.853  1.00 20.99           C  
-ATOM   1319  CG1 VAL A 164       1.766  43.013  69.102  1.00 19.08           C  
-ATOM   1320  CG2 VAL A 164       2.982  44.758  70.443  1.00 20.46           C  
-ATOM   1321  N   THR A 165      -0.457  44.604  67.175  1.00 20.25           N  
-ATOM   1322  CA  THR A 165      -1.696  44.049  66.643  1.00 19.61           C  
-ATOM   1323  C   THR A 165      -2.226  43.014  67.620  1.00 19.29           C  
-ATOM   1324  O   THR A 165      -1.492  42.121  68.048  1.00 18.96           O  
-ATOM   1325  CB  THR A 165      -1.438  43.411  65.287  1.00 19.45           C  
-ATOM   1326  OG1 THR A 165      -1.037  44.438  64.373  1.00 18.64           O  
-ATOM   1327  CG2 THR A 165      -2.749  42.856  64.686  1.00 18.98           C  
-ATOM   1328  N   LEU A 166      -3.508  43.153  67.955  1.00 19.05           N  
-ATOM   1329  CA  LEU A 166      -4.135  42.458  69.076  1.00 18.42           C  
-ATOM   1330  C   LEU A 166      -3.795  40.969  69.222  1.00 18.10           C  
-ATOM   1331  O   LEU A 166      -3.486  40.515  70.325  1.00 17.50           O  
-ATOM   1332  CB  LEU A 166      -5.667  42.652  69.033  1.00 18.89           C  
-ATOM   1333  CG  LEU A 166      -6.451  42.047  70.201  1.00 18.75           C  
-ATOM   1334  CD1 LEU A 166      -6.007  42.637  71.543  1.00 17.31           C  
-ATOM   1335  CD2 LEU A 166      -7.967  42.246  69.986  1.00 20.94           C  
-ATOM   1336  N   TRP A 167      -3.860  40.217  68.125  1.00 17.60           N  
-ATOM   1337  CA  TRP A 167      -3.660  38.759  68.182  1.00 17.98           C  
-ATOM   1338  C   TRP A 167      -2.273  38.378  68.717  1.00 17.79           C  
-ATOM   1339  O   TRP A 167      -2.093  37.277  69.263  1.00 17.24           O  
-ATOM   1340  CB  TRP A 167      -3.834  38.129  66.797  1.00 17.72           C  
-ATOM   1341  CG  TRP A 167      -5.238  38.133  66.243  1.00 19.74           C  
-ATOM   1342  CD1 TRP A 167      -6.382  38.634  66.840  1.00 20.12           C  
-ATOM   1343  CD2 TRP A 167      -5.652  37.609  64.979  1.00 19.65           C  
-ATOM   1344  NE1 TRP A 167      -7.464  38.453  66.010  1.00 19.75           N  
-ATOM   1345  CE2 TRP A 167      -7.049  37.825  64.866  1.00 20.20           C  
-ATOM   1346  CE3 TRP A 167      -4.987  36.980  63.925  1.00 18.99           C  
-ATOM   1347  CZ2 TRP A 167      -7.784  37.424  63.744  1.00 20.62           C  
-ATOM   1348  CZ3 TRP A 167      -5.721  36.579  62.812  1.00 20.46           C  
-ATOM   1349  CH2 TRP A 167      -7.106  36.805  62.732  1.00 20.04           C  
-ATOM   1350  N   TYR A 168      -1.320  39.304  68.558  1.00 17.17           N  
-ATOM   1351  CA  TYR A 168       0.102  39.078  68.859  1.00 17.10           C  
-ATOM   1352  C   TYR A 168       0.543  39.867  70.078  1.00 17.30           C  
-ATOM   1353  O   TYR A 168       1.746  39.931  70.393  1.00 17.38           O  
-ATOM   1354  CB  TYR A 168       0.969  39.433  67.623  1.00 16.65           C  
-ATOM   1355  CG  TYR A 168       0.483  38.684  66.404  1.00 16.41           C  
-ATOM   1356  CD1 TYR A 168       0.837  37.354  66.215  1.00 16.87           C  
-ATOM   1357  CD2 TYR A 168      -0.399  39.279  65.486  1.00 14.62           C  
-ATOM   1358  CE1 TYR A 168       0.355  36.626  65.140  1.00 18.61           C  
-ATOM   1359  CE2 TYR A 168      -0.890  38.561  64.391  1.00 16.82           C  
-ATOM   1360  CZ  TYR A 168      -0.513  37.233  64.227  1.00 19.23           C  
-ATOM   1361  OH  TYR A 168      -0.967  36.482  63.162  1.00 17.74           O  
-ATOM   1362  N   ARG A 169      -0.432  40.486  70.743  1.00 17.20           N  
-ATOM   1363  CA  ARG A 169      -0.174  41.372  71.881  1.00 17.61           C  
-ATOM   1364  C   ARG A 169       0.069  40.585  73.163  1.00 17.82           C  
-ATOM   1365  O   ARG A 169      -0.681  39.658  73.472  1.00 17.72           O  
-ATOM   1366  CB  ARG A 169      -1.342  42.348  72.079  1.00 17.21           C  
-ATOM   1367  CG  ARG A 169      -1.116  43.398  73.145  1.00 17.00           C  
-ATOM   1368  CD  ARG A 169      -2.223  44.421  73.225  1.00 17.31           C  
-ATOM   1369  NE  ARG A 169      -2.528  44.994  71.915  1.00 17.88           N  
-ATOM   1370  CZ  ARG A 169      -3.593  45.750  71.654  1.00 18.46           C  
-ATOM   1371  NH1 ARG A 169      -4.478  46.027  72.615  1.00 15.82           N  
-ATOM   1372  NH2 ARG A 169      -3.782  46.208  70.423  1.00 16.81           N  
-ATOM   1373  N   ALA A 170       1.102  40.993  73.905  1.00 17.99           N  
-ATOM   1374  CA  ALA A 170       1.538  40.311  75.118  1.00 18.34           C  
-ATOM   1375  C   ALA A 170       0.639  40.599  76.313  1.00 18.88           C  
-ATOM   1376  O   ALA A 170       0.075  41.686  76.404  1.00 19.25           O  
-ATOM   1377  CB  ALA A 170       2.994  40.687  75.441  1.00 18.34           C  
-ATOM   1378  N   PRO A 171       0.518  39.643  77.243  1.00 19.34           N  
-ATOM   1379  CA  PRO A 171      -0.351  39.823  78.419  1.00 19.53           C  
-ATOM   1380  C   PRO A 171      -0.029  41.054  79.237  1.00 19.43           C  
-ATOM   1381  O   PRO A 171      -0.964  41.688  79.710  1.00 19.08           O  
-ATOM   1382  CB  PRO A 171      -0.151  38.537  79.243  1.00 19.54           C  
-ATOM   1383  CG  PRO A 171       1.063  37.872  78.666  1.00 20.04           C  
-ATOM   1384  CD  PRO A 171       1.143  38.310  77.223  1.00 19.03           C  
-ATOM   1385  N   GLU A 172       1.247  41.411  79.366  1.00 19.57           N  
-ATOM   1386  CA  GLU A 172       1.635  42.605  80.127  1.00 19.42           C  
-ATOM   1387  C   GLU A 172       1.124  43.903  79.488  1.00 19.73           C  
-ATOM   1388  O   GLU A 172       0.836  44.862  80.211  1.00 20.34           O  
-ATOM   1389  CB  GLU A 172       3.165  42.655  80.374  1.00 19.35           C  
-ATOM   1390  CG  GLU A 172       4.014  42.770  79.107  1.00 18.47           C  
-ATOM   1391  CD  GLU A 172       4.453  41.427  78.550  1.00 19.35           C  
-ATOM   1392  OE1 GLU A 172       3.679  40.441  78.626  1.00 18.72           O  
-ATOM   1393  OE2 GLU A 172       5.578  41.362  78.018  1.00 18.52           O  
-ATOM   1394  N   ILE A 173       1.004  43.936  78.158  1.00 19.69           N  
-ATOM   1395  CA  ILE A 173       0.362  45.075  77.480  1.00 20.34           C  
-ATOM   1396  C   ILE A 173      -1.142  45.060  77.789  1.00 20.73           C  
-ATOM   1397  O   ILE A 173      -1.725  46.082  78.177  1.00 20.46           O  
-ATOM   1398  CB  ILE A 173       0.527  45.050  75.931  1.00 20.41           C  
-ATOM   1399  CG1 ILE A 173       1.966  44.741  75.466  1.00 20.92           C  
-ATOM   1400  CG2 ILE A 173       0.032  46.365  75.338  1.00 19.39           C  
-ATOM   1401  CD1 ILE A 173       2.977  45.671  75.982  1.00 24.72           C  
-ATOM   1402  N   LEU A 174      -1.740  43.884  77.605  1.00 20.26           N  
-ATOM   1403  CA  LEU A 174      -3.160  43.670  77.836  1.00 21.03           C  
-ATOM   1404  C   LEU A 174      -3.587  44.028  79.250  1.00 21.40           C  
-ATOM   1405  O   LEU A 174      -4.696  44.507  79.453  1.00 21.64           O  
-ATOM   1406  CB  LEU A 174      -3.530  42.217  77.536  1.00 20.14           C  
-ATOM   1407  CG  LEU A 174      -3.519  41.883  76.050  1.00 19.83           C  
-ATOM   1408  CD1 LEU A 174      -3.477  40.392  75.854  1.00 17.97           C  
-ATOM   1409  CD2 LEU A 174      -4.745  42.521  75.357  1.00 19.13           C  
-ATOM   1410  N   LEU A 175      -2.691  43.808  80.207  1.00 22.02           N  
-ATOM   1411  CA  LEU A 175      -2.970  44.062  81.612  1.00 23.08           C  
-ATOM   1412  C   LEU A 175      -2.515  45.451  82.063  1.00 23.95           C  
-ATOM   1413  O   LEU A 175      -2.511  45.751  83.261  1.00 24.30           O  
-ATOM   1414  CB  LEU A 175      -2.353  42.963  82.485  1.00 22.67           C  
-ATOM   1415  CG  LEU A 175      -3.007  41.579  82.377  1.00 23.03           C  
-ATOM   1416  CD1 LEU A 175      -2.099  40.510  82.951  1.00 23.40           C  
-ATOM   1417  CD2 LEU A 175      -4.392  41.536  83.053  1.00 23.60           C  
-ATOM   1418  N   GLY A 176      -2.130  46.290  81.099  1.00 25.08           N  
-ATOM   1419  CA  GLY A 176      -1.841  47.694  81.349  1.00 25.83           C  
-ATOM   1420  C   GLY A 176      -0.625  47.999  82.201  1.00 27.02           C  
-ATOM   1421  O   GLY A 176      -0.588  49.036  82.869  1.00 27.22           O  
-ATOM   1422  N   CYS A 177       0.376  47.125  82.186  1.00 27.94           N  
-ATOM   1423  CA  CYS A 177       1.611  47.393  82.933  1.00 29.37           C  
-ATOM   1424  C   CYS A 177       2.250  48.721  82.545  1.00 28.46           C  
-ATOM   1425  O   CYS A 177       2.242  49.126  81.376  1.00 28.26           O  
-ATOM   1426  CB  CYS A 177       2.639  46.275  82.770  1.00 29.63           C  
-ATOM   1427  SG  CYS A 177       4.139  46.518  83.769  1.00 38.96           S  
-ATOM   1428  N   LYS A 178       2.787  49.390  83.555  1.00 28.01           N  
-ATOM   1429  CA  LYS A 178       3.507  50.641  83.400  1.00 27.94           C  
-ATOM   1430  C   LYS A 178       4.683  50.469  82.436  1.00 27.11           C  
-ATOM   1431  O   LYS A 178       4.943  51.327  81.595  1.00 26.62           O  
-ATOM   1432  CB  LYS A 178       4.033  51.062  84.765  1.00 28.31           C  
-ATOM   1433  CG  LYS A 178       4.267  52.535  84.928  1.00 30.69           C  
-ATOM   1434  CD  LYS A 178       4.968  52.806  86.263  1.00 34.43           C  
-ATOM   1435  CE  LYS A 178       4.872  54.273  86.654  1.00 36.21           C  
-ATOM   1436  NZ  LYS A 178       5.325  55.167  85.559  1.00 39.71           N  
-ATOM   1437  N   TYR A 179       5.371  49.339  82.563  1.00 26.35           N  
-ATOM   1438  CA  TYR A 179       6.581  49.085  81.800  1.00 25.82           C  
-ATOM   1439  C   TYR A 179       6.458  47.836  80.958  1.00 24.74           C  
-ATOM   1440  O   TYR A 179       5.984  46.806  81.421  1.00 25.42           O  
-ATOM   1441  CB  TYR A 179       7.772  48.945  82.743  1.00 26.24           C  
-ATOM   1442  CG  TYR A 179       7.996  50.139  83.654  1.00 27.90           C  
-ATOM   1443  CD1 TYR A 179       8.251  51.405  83.132  1.00 28.65           C  
-ATOM   1444  CD2 TYR A 179       7.961  49.992  85.041  1.00 30.70           C  
-ATOM   1445  CE1 TYR A 179       8.467  52.498  83.969  1.00 31.47           C  
-ATOM   1446  CE2 TYR A 179       8.177  51.084  85.892  1.00 32.18           C  
-ATOM   1447  CZ  TYR A 179       8.431  52.330  85.347  1.00 32.79           C  
-ATOM   1448  OH  TYR A 179       8.647  53.410  86.180  1.00 34.91           O  
-ATOM   1449  N   TYR A 180       6.879  47.946  79.710  1.00 23.37           N  
-ATOM   1450  CA  TYR A 180       7.051  46.787  78.855  1.00 21.90           C  
-ATOM   1451  C   TYR A 180       8.354  46.926  78.082  1.00 21.48           C  
-ATOM   1452  O   TYR A 180       8.806  48.045  77.815  1.00 21.56           O  
-ATOM   1453  CB  TYR A 180       5.841  46.591  77.931  1.00 21.66           C  
-ATOM   1454  CG  TYR A 180       5.619  47.654  76.870  1.00 20.09           C  
-ATOM   1455  CD1 TYR A 180       6.424  47.713  75.730  1.00 19.93           C  
-ATOM   1456  CD2 TYR A 180       4.558  48.557  76.972  1.00 21.17           C  
-ATOM   1457  CE1 TYR A 180       6.209  48.671  74.737  1.00 18.01           C  
-ATOM   1458  CE2 TYR A 180       4.335  49.536  75.979  1.00 20.50           C  
-ATOM   1459  CZ  TYR A 180       5.174  49.576  74.867  1.00 19.13           C  
-ATOM   1460  OH  TYR A 180       4.970  50.505  73.877  1.00 19.72           O  
-ATOM   1461  N   SER A 181       8.950  45.794  77.723  1.00 20.32           N  
-ATOM   1462  CA  SER A 181      10.252  45.808  77.096  1.00 20.22           C  
-ATOM   1463  C   SER A 181      10.367  44.785  75.973  1.00 18.81           C  
-ATOM   1464  O   SER A 181       9.377  44.481  75.318  1.00 18.57           O  
-ATOM   1465  CB  SER A 181      11.342  45.560  78.141  1.00 19.97           C  
-ATOM   1466  OG  SER A 181      12.560  46.068  77.638  1.00 25.48           O  
-ATOM   1467  N   THR A 182      11.578  44.242  75.791  1.00 17.08           N  
-ATOM   1468  CA  THR A 182      11.900  43.356  74.679  1.00 15.92           C  
-ATOM   1469  C   THR A 182      11.030  42.113  74.645  1.00 15.57           C  
-ATOM   1470  O   THR A 182      10.797  41.550  73.567  1.00 14.51           O  
-ATOM   1471  CB  THR A 182      13.377  42.916  74.734  1.00 16.05           C  
-ATOM   1472  OG1 THR A 182      13.632  42.304  76.007  1.00 16.70           O  
-ATOM   1473  CG2 THR A 182      14.330  44.123  74.704  1.00 14.84           C  
-ATOM   1474  N   ALA A 183      10.594  41.665  75.826  1.00 14.86           N  
-ATOM   1475  CA  ALA A 183       9.804  40.443  75.936  1.00 14.58           C  
-ATOM   1476  C   ALA A 183       8.487  40.523  75.145  1.00 14.70           C  
-ATOM   1477  O   ALA A 183       7.942  39.476  74.769  1.00 14.66           O  
-ATOM   1478  CB  ALA A 183       9.536  40.084  77.419  1.00 14.30           C  
-ATOM   1479  N   VAL A 184       7.987  41.735  74.858  1.00 14.85           N  
-ATOM   1480  CA  VAL A 184       6.753  41.827  74.046  1.00 14.89           C  
-ATOM   1481  C   VAL A 184       6.964  41.296  72.631  1.00 15.28           C  
-ATOM   1482  O   VAL A 184       6.058  40.682  72.066  1.00 15.20           O  
-ATOM   1483  CB  VAL A 184       6.047  43.228  74.039  1.00 15.19           C  
-ATOM   1484  CG1 VAL A 184       5.902  43.781  75.460  1.00 14.16           C  
-ATOM   1485  CG2 VAL A 184       6.740  44.230  73.087  1.00 14.83           C  
-ATOM   1486  N   ASP A 185       8.171  41.485  72.079  1.00 15.15           N  
-ATOM   1487  CA  ASP A 185       8.443  41.043  70.705  1.00 14.98           C  
-ATOM   1488  C   ASP A 185       8.582  39.520  70.669  1.00 15.08           C  
-ATOM   1489  O   ASP A 185       8.174  38.868  69.697  1.00 15.49           O  
-ATOM   1490  CB  ASP A 185       9.714  41.689  70.145  1.00 14.44           C  
-ATOM   1491  CG  ASP A 185       9.533  43.150  69.779  1.00 16.38           C  
-ATOM   1492  OD1 ASP A 185       8.389  43.589  69.460  1.00 15.44           O  
-ATOM   1493  OD2 ASP A 185      10.505  43.944  69.783  1.00 17.18           O  
-ATOM   1494  N   ILE A 186       9.163  38.960  71.728  1.00 14.68           N  
-ATOM   1495  CA  ILE A 186       9.269  37.509  71.871  1.00 14.59           C  
-ATOM   1496  C   ILE A 186       7.881  36.837  71.943  1.00 14.65           C  
-ATOM   1497  O   ILE A 186       7.680  35.760  71.365  1.00 14.53           O  
-ATOM   1498  CB  ILE A 186      10.126  37.137  73.122  1.00 14.70           C  
-ATOM   1499  CG1 ILE A 186      11.605  37.525  72.909  1.00 16.01           C  
-ATOM   1500  CG2 ILE A 186      10.022  35.620  73.412  1.00 13.71           C  
-ATOM   1501  CD1 ILE A 186      12.275  36.801  71.727  1.00 17.13           C  
-ATOM   1502  N   TRP A 187       6.940  37.467  72.658  1.00 14.81           N  
-ATOM   1503  CA  TRP A 187       5.577  36.937  72.760  1.00 15.19           C  
-ATOM   1504  C   TRP A 187       5.015  36.857  71.351  1.00 15.10           C  
-ATOM   1505  O   TRP A 187       4.513  35.814  70.931  1.00 15.32           O  
-ATOM   1506  CB  TRP A 187       4.687  37.801  73.674  1.00 15.67           C  
-ATOM   1507  CG  TRP A 187       3.253  37.290  73.774  1.00 17.37           C  
-ATOM   1508  CD1 TRP A 187       2.221  37.560  72.917  1.00 16.46           C  
-ATOM   1509  CD2 TRP A 187       2.722  36.410  74.772  1.00 17.22           C  
-ATOM   1510  NE1 TRP A 187       1.083  36.908  73.326  1.00 18.00           N  
-ATOM   1511  CE2 TRP A 187       1.360  36.191  74.459  1.00 18.74           C  
-ATOM   1512  CE3 TRP A 187       3.259  35.779  75.905  1.00 17.55           C  
-ATOM   1513  CZ2 TRP A 187       0.527  35.361  75.237  1.00 18.98           C  
-ATOM   1514  CZ3 TRP A 187       2.422  34.957  76.690  1.00 17.93           C  
-ATOM   1515  CH2 TRP A 187       1.077  34.765  76.351  1.00 17.98           C  
-ATOM   1516  N   SER A 188       5.149  37.947  70.600  1.00 15.10           N  
-ATOM   1517  CA  SER A 188       4.695  37.958  69.209  1.00 15.45           C  
-ATOM   1518  C   SER A 188       5.315  36.824  68.392  1.00 15.19           C  
-ATOM   1519  O   SER A 188       4.605  36.097  67.727  1.00 14.95           O  
-ATOM   1520  CB  SER A 188       4.949  39.311  68.558  1.00 14.81           C  
-ATOM   1521  OG  SER A 188       4.320  40.329  69.307  1.00 16.31           O  
-ATOM   1522  N   LEU A 189       6.629  36.644  68.476  1.00 15.62           N  
-ATOM   1523  CA  LEU A 189       7.285  35.561  67.724  1.00 15.83           C  
-ATOM   1524  C   LEU A 189       6.810  34.177  68.169  1.00 15.35           C  
-ATOM   1525  O   LEU A 189       6.789  33.246  67.369  1.00 15.13           O  
-ATOM   1526  CB  LEU A 189       8.808  35.637  67.870  1.00 16.40           C  
-ATOM   1527  CG  LEU A 189       9.581  36.679  67.059  1.00 19.06           C  
-ATOM   1528  CD1 LEU A 189      11.061  36.235  66.961  1.00 20.30           C  
-ATOM   1529  CD2 LEU A 189       8.980  36.922  65.653  1.00 19.56           C  
-ATOM   1530  N   GLY A 190       6.467  34.049  69.451  1.00 15.27           N  
-ATOM   1531  CA  GLY A 190       5.896  32.825  69.986  1.00 15.79           C  
-ATOM   1532  C   GLY A 190       4.575  32.494  69.311  1.00 16.67           C  
-ATOM   1533  O   GLY A 190       4.349  31.347  68.909  1.00 16.28           O  
-ATOM   1534  N   CYS A 191       3.715  33.509  69.173  1.00 17.02           N  
-ATOM   1535  CA  CYS A 191       2.455  33.371  68.440  1.00 17.59           C  
-ATOM   1536  C   CYS A 191       2.677  33.042  66.978  1.00 17.99           C  
-ATOM   1537  O   CYS A 191       1.925  32.260  66.406  1.00 18.58           O  
-ATOM   1538  CB  CYS A 191       1.625  34.643  68.555  1.00 17.43           C  
-ATOM   1539  SG  CYS A 191       1.163  34.973  70.260  1.00 17.94           S  
-ATOM   1540  N   ILE A 192       3.706  33.632  66.373  1.00 18.42           N  
-ATOM   1541  CA  ILE A 192       4.036  33.324  64.981  1.00 18.85           C  
-ATOM   1542  C   ILE A 192       4.556  31.889  64.818  1.00 18.60           C  
-ATOM   1543  O   ILE A 192       4.259  31.223  63.813  1.00 18.55           O  
-ATOM   1544  CB  ILE A 192       5.033  34.341  64.409  1.00 19.03           C  
-ATOM   1545  CG1 ILE A 192       4.385  35.735  64.361  1.00 20.90           C  
-ATOM   1546  CG2 ILE A 192       5.505  33.905  63.000  1.00 19.16           C  
-ATOM   1547  CD1 ILE A 192       5.392  36.878  64.269  1.00 22.61           C  
-ATOM   1548  N   PHE A 193       5.338  31.426  65.796  1.00 18.43           N  
-ATOM   1549  CA  PHE A 193       5.901  30.066  65.765  1.00 18.03           C  
-ATOM   1550  C   PHE A 193       4.717  29.089  65.713  1.00 18.22           C  
-ATOM   1551  O   PHE A 193       4.597  28.283  64.781  1.00 17.12           O  
-ATOM   1552  CB  PHE A 193       6.793  29.852  67.000  1.00 17.50           C  
-ATOM   1553  CG  PHE A 193       7.404  28.462  67.122  1.00 17.32           C  
-ATOM   1554  CD1 PHE A 193       7.479  27.599  66.037  1.00 16.57           C  
-ATOM   1555  CD2 PHE A 193       7.930  28.040  68.348  1.00 16.78           C  
-ATOM   1556  CE1 PHE A 193       8.037  26.325  66.163  1.00 16.38           C  
-ATOM   1557  CE2 PHE A 193       8.513  26.775  68.486  1.00 16.67           C  
-ATOM   1558  CZ  PHE A 193       8.559  25.914  67.384  1.00 17.66           C  
-ATOM   1559  N   ALA A 194       3.828  29.210  66.700  1.00 18.57           N  
-ATOM   1560  CA  ALA A 194       2.589  28.427  66.750  1.00 19.67           C  
-ATOM   1561  C   ALA A 194       1.826  28.491  65.431  1.00 20.25           C  
-ATOM   1562  O   ALA A 194       1.445  27.459  64.874  1.00 20.13           O  
-ATOM   1563  CB  ALA A 194       1.701  28.896  67.923  1.00 19.21           C  
-ATOM   1564  N   GLU A 195       1.644  29.704  64.917  1.00 21.52           N  
-ATOM   1565  CA  GLU A 195       0.899  29.912  63.675  1.00 22.68           C  
-ATOM   1566  C   GLU A 195       1.515  29.228  62.454  1.00 23.35           C  
-ATOM   1567  O   GLU A 195       0.790  28.710  61.600  1.00 23.39           O  
-ATOM   1568  CB  GLU A 195       0.710  31.406  63.407  1.00 22.99           C  
-ATOM   1569  CG  GLU A 195      -0.492  31.725  62.536  1.00 23.25           C  
-ATOM   1570  CD  GLU A 195      -0.755  33.209  62.455  1.00 23.49           C  
-ATOM   1571  OE1 GLU A 195      -0.624  33.902  63.492  1.00 26.20           O  
-ATOM   1572  OE2 GLU A 195      -1.073  33.688  61.358  1.00 22.81           O  
-ATOM   1573  N   MET A 196       2.842  29.230  62.360  1.00 24.10           N  
-ATOM   1574  CA  MET A 196       3.531  28.549  61.256  1.00 24.97           C  
-ATOM   1575  C   MET A 196       3.256  27.041  61.259  1.00 25.72           C  
-ATOM   1576  O   MET A 196       3.184  26.418  60.202  1.00 25.70           O  
-ATOM   1577  CB  MET A 196       5.046  28.809  61.297  1.00 24.68           C  
-ATOM   1578  CG  MET A 196       5.457  30.214  60.859  1.00 25.02           C  
-ATOM   1579  SD  MET A 196       7.226  30.320  60.490  1.00 26.39           S  
-ATOM   1580  CE  MET A 196       7.895  30.492  62.157  1.00 24.90           C  
-ATOM   1581  N   VAL A 197       3.100  26.464  62.445  1.00 26.71           N  
-ATOM   1582  CA  VAL A 197       2.828  25.031  62.570  1.00 28.27           C  
-ATOM   1583  C   VAL A 197       1.363  24.685  62.222  1.00 29.23           C  
-ATOM   1584  O   VAL A 197       1.108  23.796  61.407  1.00 29.15           O  
-ATOM   1585  CB  VAL A 197       3.198  24.490  63.984  1.00 28.18           C  
-ATOM   1586  CG1 VAL A 197       3.034  22.969  64.036  1.00 28.09           C  
-ATOM   1587  CG2 VAL A 197       4.633  24.890  64.367  1.00 27.88           C  
-ATOM   1588  N   THR A 198       0.415  25.405  62.825  1.00 30.48           N  
-ATOM   1589  CA  THR A 198      -1.019  25.119  62.642  1.00 31.51           C  
-ATOM   1590  C   THR A 198      -1.648  25.852  61.456  1.00 32.29           C  
-ATOM   1591  O   THR A 198      -2.717  25.460  60.974  1.00 32.69           O  
-ATOM   1592  CB  THR A 198      -1.809  25.460  63.909  1.00 31.45           C  
-ATOM   1593  OG1 THR A 198      -1.673  26.860  64.182  1.00 31.94           O  
-ATOM   1594  CG2 THR A 198      -1.207  24.778  65.139  1.00 31.67           C  
-ATOM   1595  N   ARG A 199      -0.986  26.918  61.004  1.00 32.92           N  
-ATOM   1596  CA  ARG A 199      -1.465  27.787  59.920  1.00 33.13           C  
-ATOM   1597  C   ARG A 199      -2.703  28.617  60.299  1.00 32.84           C  
-ATOM   1598  O   ARG A 199      -3.355  29.212  59.433  1.00 33.50           O  
-ATOM   1599  CB  ARG A 199      -1.680  27.002  58.625  1.00 33.77           C  
-ATOM   1600  CG  ARG A 199      -0.399  26.747  57.824  1.00 35.98           C  
-ATOM   1601  CD  ARG A 199      -0.595  25.840  56.624  1.00 39.30           C  
-ATOM   1602  NE  ARG A 199      -0.804  24.444  57.012  1.00 42.86           N  
-ATOM   1603  CZ  ARG A 199      -1.909  23.741  56.771  1.00 45.28           C  
-ATOM   1604  NH1 ARG A 199      -2.946  24.277  56.144  1.00 46.55           N  
-ATOM   1605  NH2 ARG A 199      -1.982  22.483  57.168  1.00 47.30           N  
-ATOM   1606  N   ARG A 200      -3.012  28.670  61.591  1.00 31.74           N  
-ATOM   1607  CA  ARG A 200      -4.054  29.561  62.100  1.00 30.91           C  
-ATOM   1608  C   ARG A 200      -3.581  30.291  63.362  1.00 29.46           C  
-ATOM   1609  O   ARG A 200      -2.728  29.790  64.094  1.00 29.05           O  
-ATOM   1610  CB  ARG A 200      -5.354  28.788  62.362  1.00 31.28           C  
-ATOM   1611  CG  ARG A 200      -5.382  28.062  63.672  1.00 33.77           C  
-ATOM   1612  CD  ARG A 200      -6.502  27.069  63.819  1.00 38.79           C  
-ATOM   1613  NE  ARG A 200      -6.433  26.442  65.130  1.00 42.04           N  
-ATOM   1614  CZ  ARG A 200      -5.994  25.211  65.351  1.00 44.49           C  
-ATOM   1615  NH1 ARG A 200      -5.590  24.444  64.341  1.00 45.68           N  
-ATOM   1616  NH2 ARG A 200      -5.968  24.738  66.592  1.00 45.58           N  
-ATOM   1617  N   ALA A 201      -4.147  31.465  63.622  1.00 27.80           N  
-ATOM   1618  CA  ALA A 201      -3.681  32.283  64.731  1.00 26.31           C  
-ATOM   1619  C   ALA A 201      -3.933  31.591  66.057  1.00 25.27           C  
-ATOM   1620  O   ALA A 201      -4.957  30.957  66.239  1.00 25.00           O  
-ATOM   1621  CB  ALA A 201      -4.319  33.640  64.700  1.00 26.58           C  
-ATOM   1622  N   LEU A 202      -2.969  31.696  66.966  1.00 24.16           N  
-ATOM   1623  CA  LEU A 202      -3.031  31.043  68.269  1.00 22.99           C  
-ATOM   1624  C   LEU A 202      -4.095  31.653  69.184  1.00 22.51           C  
-ATOM   1625  O   LEU A 202      -4.847  30.932  69.842  1.00 22.66           O  
-ATOM   1626  CB  LEU A 202      -1.644  31.101  68.944  1.00 23.03           C  
-ATOM   1627  CG  LEU A 202      -1.462  30.478  70.333  1.00 21.48           C  
-ATOM   1628  CD1 LEU A 202      -1.818  29.000  70.319  1.00 21.61           C  
-ATOM   1629  CD2 LEU A 202      -0.033  30.682  70.813  1.00 19.61           C  
-ATOM   1630  N   PHE A 203      -4.133  32.982  69.225  1.00 21.96           N  
-ATOM   1631  CA  PHE A 203      -5.028  33.728  70.088  1.00 21.59           C  
-ATOM   1632  C   PHE A 203      -5.757  34.790  69.246  1.00 22.34           C  
-ATOM   1633  O   PHE A 203      -5.398  35.974  69.292  1.00 22.33           O  
-ATOM   1634  CB  PHE A 203      -4.243  34.444  71.200  1.00 21.56           C  
-ATOM   1635  CG  PHE A 203      -3.389  33.548  72.055  1.00 20.84           C  
-ATOM   1636  CD1 PHE A 203      -3.943  32.490  72.768  1.00 20.56           C  
-ATOM   1637  CD2 PHE A 203      -2.018  33.802  72.183  1.00 21.01           C  
-ATOM   1638  CE1 PHE A 203      -3.133  31.666  73.585  1.00 20.80           C  
-ATOM   1639  CE2 PHE A 203      -1.208  32.993  72.996  1.00 20.43           C  
-ATOM   1640  CZ  PHE A 203      -1.769  31.931  73.701  1.00 20.37           C  
-ATOM   1641  N   PRO A 204      -6.767  34.388  68.472  1.00 22.46           N  
-ATOM   1642  CA  PRO A 204      -7.459  35.338  67.601  1.00 22.93           C  
-ATOM   1643  C   PRO A 204      -8.609  36.090  68.291  1.00 23.27           C  
-ATOM   1644  O   PRO A 204      -9.745  35.921  67.889  1.00 23.67           O  
-ATOM   1645  CB  PRO A 204      -7.969  34.444  66.463  1.00 22.41           C  
-ATOM   1646  CG  PRO A 204      -8.209  33.113  67.099  1.00 22.70           C  
-ATOM   1647  CD  PRO A 204      -7.311  33.021  68.330  1.00 22.07           C  
-ATOM   1648  N   GLY A 205      -8.310  36.906  69.299  1.00 24.09           N  
-ATOM   1649  CA  GLY A 205      -9.323  37.701  69.991  1.00 25.19           C  
-ATOM   1650  C   GLY A 205      -9.814  38.924  69.221  1.00 26.09           C  
-ATOM   1651  O   GLY A 205      -9.151  39.403  68.296  1.00 26.03           O  
-ATOM   1652  N   ASP A 206     -10.984  39.436  69.599  1.00 27.21           N  
-ATOM   1653  CA  ASP A 206     -11.542  40.627  68.938  1.00 27.96           C  
-ATOM   1654  C   ASP A 206     -11.566  41.846  69.841  1.00 26.92           C  
-ATOM   1655  O   ASP A 206     -11.934  42.941  69.411  1.00 27.73           O  
-ATOM   1656  CB  ASP A 206     -12.958  40.365  68.419  1.00 29.07           C  
-ATOM   1657  CG  ASP A 206     -13.677  39.316  69.212  1.00 33.56           C  
-ATOM   1658  OD1 ASP A 206     -13.900  39.540  70.428  1.00 38.19           O  
-ATOM   1659  OD2 ASP A 206     -14.052  38.228  68.701  1.00 38.71           O  
-ATOM   1660  N   SER A 207     -11.193  41.654  71.097  1.00 25.37           N  
-ATOM   1661  CA  SER A 207     -11.102  42.750  72.045  1.00 24.46           C  
-ATOM   1662  C   SER A 207     -10.019  42.390  73.033  1.00 23.99           C  
-ATOM   1663  O   SER A 207      -9.567  41.249  73.068  1.00 24.09           O  
-ATOM   1664  CB  SER A 207     -12.439  42.953  72.774  1.00 24.20           C  
-ATOM   1665  OG  SER A 207     -12.712  41.854  73.624  1.00 22.56           O  
-ATOM   1666  N   GLU A 208      -9.619  43.358  73.846  1.00 23.83           N  
-ATOM   1667  CA  GLU A 208      -8.563  43.138  74.830  1.00 24.11           C  
-ATOM   1668  C   GLU A 208      -8.938  42.057  75.828  1.00 23.47           C  
-ATOM   1669  O   GLU A 208      -8.141  41.172  76.089  1.00 23.27           O  
-ATOM   1670  CB  GLU A 208      -8.208  44.436  75.553  1.00 24.16           C  
-ATOM   1671  CG  GLU A 208      -7.460  45.417  74.675  1.00 27.91           C  
-ATOM   1672  CD  GLU A 208      -7.062  46.677  75.412  1.00 33.47           C  
-ATOM   1673  OE1 GLU A 208      -6.534  46.584  76.537  1.00 37.42           O  
-ATOM   1674  OE2 GLU A 208      -7.272  47.770  74.868  1.00 38.04           O  
-ATOM   1675  N   ILE A 209     -10.158  42.113  76.365  1.00 23.12           N  
-ATOM   1676  CA  ILE A 209     -10.589  41.126  77.356  1.00 22.68           C  
-ATOM   1677  C   ILE A 209     -10.752  39.730  76.770  1.00 22.14           C  
-ATOM   1678  O   ILE A 209     -10.398  38.724  77.406  1.00 21.86           O  
-ATOM   1679  CB  ILE A 209     -11.842  41.601  78.144  1.00 22.96           C  
-ATOM   1680  CG1 ILE A 209     -11.986  40.776  79.422  1.00 24.18           C  
-ATOM   1681  CG2 ILE A 209     -13.125  41.550  77.283  1.00 23.90           C  
-ATOM   1682  CD1 ILE A 209     -11.019  41.238  80.533  1.00 23.95           C  
-ATOM   1683  N   ASP A 210     -11.260  39.678  75.543  1.00 21.61           N  
-ATOM   1684  CA  ASP A 210     -11.371  38.441  74.787  1.00 21.14           C  
-ATOM   1685  C   ASP A 210      -9.987  37.843  74.524  1.00 20.63           C  
-ATOM   1686  O   ASP A 210      -9.787  36.640  74.687  1.00 20.37           O  
-ATOM   1687  CB  ASP A 210     -12.089  38.715  73.467  1.00 21.43           C  
-ATOM   1688  CG  ASP A 210     -12.275  37.468  72.626  1.00 23.55           C  
-ATOM   1689  OD1 ASP A 210     -12.458  36.364  73.196  1.00 27.18           O  
-ATOM   1690  OD2 ASP A 210     -12.278  37.510  71.375  1.00 26.11           O  
-ATOM   1691  N   GLN A 211      -9.043  38.691  74.113  1.00 20.06           N  
-ATOM   1692  CA  GLN A 211      -7.656  38.272  73.892  1.00 19.84           C  
-ATOM   1693  C   GLN A 211      -7.063  37.643  75.160  1.00 19.21           C  
-ATOM   1694  O   GLN A 211      -6.520  36.536  75.123  1.00 19.00           O  
-ATOM   1695  CB  GLN A 211      -6.805  39.485  73.467  1.00 20.10           C  
-ATOM   1696  CG  GLN A 211      -5.418  39.143  72.956  1.00 20.27           C  
-ATOM   1697  CD  GLN A 211      -5.456  38.333  71.693  1.00 21.27           C  
-ATOM   1698  OE1 GLN A 211      -6.399  38.438  70.899  1.00 22.04           O  
-ATOM   1699  NE2 GLN A 211      -4.448  37.505  71.502  1.00 22.68           N  
-ATOM   1700  N   LEU A 212      -7.178  38.358  76.274  1.00 18.76           N  
-ATOM   1701  CA  LEU A 212      -6.687  37.879  77.567  1.00 18.83           C  
-ATOM   1702  C   LEU A 212      -7.280  36.528  77.947  1.00 18.49           C  
-ATOM   1703  O   LEU A 212      -6.550  35.614  78.344  1.00 17.69           O  
-ATOM   1704  CB  LEU A 212      -6.996  38.894  78.661  1.00 19.20           C  
-ATOM   1705  CG  LEU A 212      -6.005  40.014  78.979  1.00 20.90           C  
-ATOM   1706  CD1 LEU A 212      -6.680  40.997  79.945  1.00 23.08           C  
-ATOM   1707  CD2 LEU A 212      -4.680  39.478  79.582  1.00 20.15           C  
-ATOM   1708  N   PHE A 213      -8.606  36.406  77.813  1.00 18.34           N  
-ATOM   1709  CA  PHE A 213      -9.320  35.175  78.158  1.00 17.81           C  
-ATOM   1710  C   PHE A 213      -8.892  34.012  77.274  1.00 17.90           C  
-ATOM   1711  O   PHE A 213      -8.719  32.910  77.765  1.00 18.21           O  
-ATOM   1712  CB  PHE A 213     -10.850  35.386  78.127  1.00 17.82           C  
-ATOM   1713  CG  PHE A 213     -11.401  36.160  79.316  1.00 17.93           C  
-ATOM   1714  CD1 PHE A 213     -10.568  36.586  80.357  1.00 17.04           C  
-ATOM   1715  CD2 PHE A 213     -12.768  36.463  79.388  1.00 18.32           C  
-ATOM   1716  CE1 PHE A 213     -11.082  37.309  81.450  1.00 16.98           C  
-ATOM   1717  CE2 PHE A 213     -13.290  37.168  80.465  1.00 17.40           C  
-ATOM   1718  CZ  PHE A 213     -12.447  37.602  81.499  1.00 18.07           C  
-ATOM   1719  N   ARG A 214      -8.697  34.246  75.977  1.00 17.99           N  
-ATOM   1720  CA  ARG A 214      -8.172  33.184  75.110  1.00 18.39           C  
-ATOM   1721  C   ARG A 214      -6.785  32.713  75.530  1.00 17.80           C  
-ATOM   1722  O   ARG A 214      -6.474  31.522  75.451  1.00 17.68           O  
-ATOM   1723  CB  ARG A 214      -8.120  33.628  73.653  1.00 18.86           C  
-ATOM   1724  CG  ARG A 214      -9.479  33.719  72.987  1.00 20.16           C  
-ATOM   1725  CD  ARG A 214      -9.411  34.392  71.644  1.00 23.18           C  
-ATOM   1726  NE  ARG A 214     -10.710  34.391  70.962  1.00 24.64           N  
-ATOM   1727  CZ  ARG A 214     -11.135  33.425  70.164  1.00 25.13           C  
-ATOM   1728  NH1 ARG A 214     -10.386  32.347  69.955  1.00 23.18           N  
-ATOM   1729  NH2 ARG A 214     -12.321  33.536  69.572  1.00 25.71           N  
-ATOM   1730  N   ILE A 215      -5.956  33.658  75.949  1.00 17.50           N  
-ATOM   1731  CA  ILE A 215      -4.631  33.341  76.468  1.00 18.05           C  
-ATOM   1732  C   ILE A 215      -4.752  32.569  77.781  1.00 17.94           C  
-ATOM   1733  O   ILE A 215      -4.147  31.514  77.931  1.00 17.96           O  
-ATOM   1734  CB  ILE A 215      -3.785  34.604  76.653  1.00 17.61           C  
-ATOM   1735  CG1 ILE A 215      -3.500  35.236  75.285  1.00 18.38           C  
-ATOM   1736  CG2 ILE A 215      -2.487  34.257  77.392  1.00 18.40           C  
-ATOM   1737  CD1 ILE A 215      -2.849  36.633  75.344  1.00 17.71           C  
-ATOM   1738  N   PHE A 216      -5.560  33.082  78.704  1.00 18.22           N  
-ATOM   1739  CA  PHE A 216      -5.787  32.410  79.985  1.00 18.75           C  
-ATOM   1740  C   PHE A 216      -6.257  30.974  79.825  1.00 19.07           C  
-ATOM   1741  O   PHE A 216      -5.835  30.109  80.575  1.00 19.43           O  
-ATOM   1742  CB  PHE A 216      -6.807  33.160  80.827  1.00 18.87           C  
-ATOM   1743  CG  PHE A 216      -6.326  34.456  81.366  1.00 18.26           C  
-ATOM   1744  CD1 PHE A 216      -5.023  34.904  81.128  1.00 18.48           C  
-ATOM   1745  CD2 PHE A 216      -7.191  35.252  82.112  1.00 18.37           C  
-ATOM   1746  CE1 PHE A 216      -4.597  36.112  81.631  1.00 17.04           C  
-ATOM   1747  CE2 PHE A 216      -6.773  36.470  82.621  1.00 18.09           C  
-ATOM   1748  CZ  PHE A 216      -5.472  36.896  82.387  1.00 18.11           C  
-ATOM   1749  N   ARG A 217      -7.130  30.722  78.852  1.00 19.15           N  
-ATOM   1750  CA  ARG A 217      -7.692  29.385  78.654  1.00 19.43           C  
-ATOM   1751  C   ARG A 217      -6.695  28.418  78.035  1.00 19.66           C  
-ATOM   1752  O   ARG A 217      -6.896  27.201  78.074  1.00 19.03           O  
-ATOM   1753  CB  ARG A 217      -8.940  29.449  77.760  1.00 19.40           C  
-ATOM   1754  CG  ARG A 217     -10.177  30.080  78.429  1.00 19.44           C  
-ATOM   1755  CD  ARG A 217     -11.487  29.745  77.721  1.00 20.75           C  
-ATOM   1756  NE  ARG A 217     -11.592  30.426  76.430  1.00 20.93           N  
-ATOM   1757  CZ  ARG A 217     -12.074  31.661  76.268  1.00 22.58           C  
-ATOM   1758  NH1 ARG A 217     -12.510  32.357  77.316  1.00 22.47           N  
-ATOM   1759  NH2 ARG A 217     -12.137  32.198  75.052  1.00 21.06           N  
-ATOM   1760  N   THR A 218      -5.639  28.965  77.433  1.00 19.44           N  
-ATOM   1761  CA  THR A 218      -4.633  28.156  76.775  1.00 19.05           C  
-ATOM   1762  C   THR A 218      -3.468  27.851  77.709  1.00 19.27           C  
-ATOM   1763  O   THR A 218      -2.941  26.739  77.700  1.00 19.12           O  
-ATOM   1764  CB  THR A 218      -4.121  28.885  75.516  1.00 19.36           C  
-ATOM   1765  OG1 THR A 218      -5.170  28.943  74.547  1.00 19.09           O  
-ATOM   1766  CG2 THR A 218      -3.028  28.084  74.803  1.00 17.04           C  
-ATOM   1767  N   LEU A 219      -3.074  28.849  78.497  1.00 19.43           N  
-ATOM   1768  CA  LEU A 219      -1.870  28.791  79.308  1.00 19.74           C  
-ATOM   1769  C   LEU A 219      -2.168  28.765  80.799  1.00 20.09           C  
-ATOM   1770  O   LEU A 219      -1.251  28.647  81.619  1.00 20.25           O  
-ATOM   1771  CB  LEU A 219      -0.983  30.007  78.995  1.00 20.03           C  
-ATOM   1772  CG  LEU A 219      -0.504  30.193  77.547  1.00 19.49           C  
-ATOM   1773  CD1 LEU A 219       0.341  31.463  77.423  1.00 17.94           C  
-ATOM   1774  CD2 LEU A 219       0.253  28.965  77.057  1.00 17.44           C  
-ATOM   1775  N   GLY A 220      -3.451  28.873  81.143  1.00 20.36           N  
-ATOM   1776  CA  GLY A 220      -3.884  28.980  82.520  1.00 20.80           C  
-ATOM   1777  C   GLY A 220      -3.984  30.439  82.879  1.00 21.94           C  
-ATOM   1778  O   GLY A 220      -3.294  31.272  82.280  1.00 21.98           O  
-ATOM   1779  N   THR A 221      -4.857  30.761  83.830  1.00 22.18           N  
-ATOM   1780  CA  THR A 221      -4.926  32.110  84.361  1.00 23.02           C  
-ATOM   1781  C   THR A 221      -3.725  32.264  85.287  1.00 24.22           C  
-ATOM   1782  O   THR A 221      -3.503  31.401  86.143  1.00 23.76           O  
-ATOM   1783  CB  THR A 221      -6.215  32.290  85.162  1.00 22.69           C  
-ATOM   1784  OG1 THR A 221      -7.337  32.085  84.301  1.00 22.92           O  
-ATOM   1785  CG2 THR A 221      -6.361  33.715  85.643  1.00 21.53           C  
-ATOM   1786  N   PRO A 222      -2.950  33.336  85.130  1.00 25.15           N  
-ATOM   1787  CA  PRO A 222      -1.742  33.498  85.941  1.00 26.41           C  
-ATOM   1788  C   PRO A 222      -2.049  33.969  87.352  1.00 27.17           C  
-ATOM   1789  O   PRO A 222      -2.889  34.840  87.551  1.00 27.51           O  
-ATOM   1790  CB  PRO A 222      -0.917  34.531  85.161  1.00 26.28           C  
-ATOM   1791  CG  PRO A 222      -1.915  35.331  84.367  1.00 25.58           C  
-ATOM   1792  CD  PRO A 222      -3.123  34.446  84.174  1.00 25.54           C  
-ATOM   1793  N   ASP A 223      -1.388  33.350  88.322  1.00 28.41           N  
-ATOM   1794  CA  ASP A 223      -1.425  33.813  89.705  1.00 29.33           C  
-ATOM   1795  C   ASP A 223      -0.037  34.331  90.123  1.00 30.03           C  
-ATOM   1796  O   ASP A 223       0.875  34.461  89.287  1.00 29.53           O  
-ATOM   1797  CB  ASP A 223      -1.917  32.698  90.629  1.00 29.44           C  
-ATOM   1798  CG  ASP A 223      -1.033  31.474  90.596  1.00 30.50           C  
-ATOM   1799  OD1 ASP A 223       0.079  31.526  90.023  1.00 33.96           O  
-ATOM   1800  OD2 ASP A 223      -1.358  30.400  91.131  1.00 32.31           O  
-ATOM   1801  N   GLU A 224       0.111  34.636  91.407  1.00 30.75           N  
-ATOM   1802  CA  GLU A 224       1.344  35.213  91.927  1.00 31.55           C  
-ATOM   1803  C   GLU A 224       2.513  34.226  91.899  1.00 31.70           C  
-ATOM   1804  O   GLU A 224       3.677  34.630  91.896  1.00 32.24           O  
-ATOM   1805  CB  GLU A 224       1.123  35.757  93.338  1.00 31.82           C  
-ATOM   1806  CG  GLU A 224       0.253  37.002  93.372  1.00 32.94           C  
-ATOM   1807  CD  GLU A 224       0.937  38.218  92.783  1.00 34.65           C  
-ATOM   1808  OE1 GLU A 224       2.186  38.217  92.667  1.00 35.51           O  
-ATOM   1809  OE2 GLU A 224       0.224  39.181  92.432  1.00 34.95           O  
-ATOM   1810  N   VAL A 225       2.203  32.936  91.857  1.00 31.58           N  
-ATOM   1811  CA  VAL A 225       3.244  31.925  91.726  1.00 31.47           C  
-ATOM   1812  C   VAL A 225       3.876  32.036  90.339  1.00 31.11           C  
-ATOM   1813  O   VAL A 225       5.077  32.251  90.221  1.00 31.49           O  
-ATOM   1814  CB  VAL A 225       2.717  30.499  91.992  1.00 31.20           C  
-ATOM   1815  CG1 VAL A 225       3.829  29.481  91.826  1.00 32.37           C  
-ATOM   1816  CG2 VAL A 225       2.135  30.397  93.394  1.00 32.36           C  
-ATOM   1817  N   VAL A 226       3.065  31.914  89.292  1.00 30.42           N  
-ATOM   1818  CA  VAL A 226       3.585  31.943  87.926  1.00 29.53           C  
-ATOM   1819  C   VAL A 226       4.123  33.324  87.542  1.00 28.76           C  
-ATOM   1820  O   VAL A 226       5.074  33.420  86.774  1.00 29.01           O  
-ATOM   1821  CB  VAL A 226       2.539  31.392  86.881  1.00 29.19           C  
-ATOM   1822  CG1 VAL A 226       1.255  32.128  86.958  1.00 29.92           C  
-ATOM   1823  CG2 VAL A 226       3.062  31.477  85.475  1.00 30.16           C  
-ATOM   1824  N   TRP A 227       3.536  34.387  88.086  1.00 28.19           N  
-ATOM   1825  CA  TRP A 227       3.869  35.743  87.640  1.00 28.19           C  
-ATOM   1826  C   TRP A 227       3.737  36.754  88.775  1.00 28.76           C  
-ATOM   1827  O   TRP A 227       2.710  37.430  88.894  1.00 27.82           O  
-ATOM   1828  CB  TRP A 227       2.999  36.133  86.421  1.00 27.94           C  
-ATOM   1829  CG  TRP A 227       3.308  37.465  85.750  1.00 26.95           C  
-ATOM   1830  CD1 TRP A 227       4.325  38.332  86.046  1.00 27.59           C  
-ATOM   1831  CD2 TRP A 227       2.573  38.071  84.677  1.00 26.20           C  
-ATOM   1832  NE1 TRP A 227       4.266  39.436  85.228  1.00 27.66           N  
-ATOM   1833  CE2 TRP A 227       3.202  39.302  84.374  1.00 26.65           C  
-ATOM   1834  CE3 TRP A 227       1.440  37.696  83.930  1.00 24.54           C  
-ATOM   1835  CZ2 TRP A 227       2.741  40.160  83.361  1.00 25.70           C  
-ATOM   1836  CZ3 TRP A 227       0.976  38.554  82.931  1.00 24.44           C  
-ATOM   1837  CH2 TRP A 227       1.628  39.770  82.655  1.00 24.87           C  
-ATOM   1838  N   PRO A 228       4.785  36.875  89.604  1.00 29.59           N  
-ATOM   1839  CA  PRO A 228       4.741  37.764  90.770  1.00 30.20           C  
-ATOM   1840  C   PRO A 228       4.391  39.194  90.358  1.00 30.97           C  
-ATOM   1841  O   PRO A 228       4.988  39.716  89.418  1.00 31.13           O  
-ATOM   1842  CB  PRO A 228       6.162  37.664  91.338  1.00 30.14           C  
-ATOM   1843  CG  PRO A 228       6.629  36.322  90.894  1.00 29.77           C  
-ATOM   1844  CD  PRO A 228       6.084  36.180  89.500  1.00 29.67           C  
-ATOM   1845  N   GLY A 229       3.402  39.788  91.027  1.00 31.97           N  
-ATOM   1846  CA  GLY A 229       2.867  41.078  90.628  1.00 32.99           C  
-ATOM   1847  C   GLY A 229       1.580  41.112  89.798  1.00 33.98           C  
-ATOM   1848  O   GLY A 229       0.931  42.162  89.767  1.00 34.58           O  
-ATOM   1849  N   VAL A 230       1.190  40.011  89.137  1.00 34.63           N  
-ATOM   1850  CA  VAL A 230       0.012  40.042  88.235  1.00 34.90           C  
-ATOM   1851  C   VAL A 230      -1.206  40.717  88.826  1.00 35.31           C  
-ATOM   1852  O   VAL A 230      -1.834  41.537  88.158  1.00 35.43           O  
-ATOM   1853  CB  VAL A 230      -0.553  38.658  87.793  1.00 34.80           C  
-ATOM   1854  CG1 VAL A 230      -0.353  38.429  86.318  1.00 34.71           C  
-ATOM   1855  CG2 VAL A 230      -0.100  37.514  88.662  1.00 34.05           C  
-ATOM   1856  N   THR A 231      -1.549  40.325  90.057  1.00 35.91           N  
-ATOM   1857  CA  THR A 231      -2.786  40.743  90.724  1.00 36.49           C  
-ATOM   1858  C   THR A 231      -2.789  42.217  91.076  1.00 36.74           C  
-ATOM   1859  O   THR A 231      -3.830  42.765  91.453  1.00 37.60           O  
-ATOM   1860  CB  THR A 231      -3.060  39.922  92.018  1.00 36.59           C  
-ATOM   1861  OG1 THR A 231      -2.037  40.184  92.990  1.00 36.96           O  
-ATOM   1862  CG2 THR A 231      -2.975  38.426  91.770  1.00 36.30           C  
-ATOM   1863  N   SER A 232      -1.629  42.849  90.955  1.00 36.88           N  
-ATOM   1864  CA  SER A 232      -1.466  44.257  91.300  1.00 36.88           C  
-ATOM   1865  C   SER A 232      -1.462  45.114  90.050  1.00 36.43           C  
-ATOM   1866  O   SER A 232      -1.516  46.342  90.140  1.00 36.85           O  
-ATOM   1867  CB  SER A 232      -0.163  44.482  92.079  1.00 37.00           C  
-ATOM   1868  OG  SER A 232       0.040  43.483  93.068  1.00 38.26           O  
-ATOM   1869  N   MET A 233      -1.398  44.469  88.888  1.00 35.49           N  
-ATOM   1870  CA  MET A 233      -1.358  45.184  87.608  1.00 34.84           C  
-ATOM   1871  C   MET A 233      -2.652  45.941  87.319  1.00 34.00           C  
-ATOM   1872  O   MET A 233      -3.725  45.464  87.665  1.00 33.46           O  
-ATOM   1873  CB  MET A 233      -1.025  44.225  86.467  1.00 34.86           C  
-ATOM   1874  CG  MET A 233       0.326  43.620  86.632  1.00 35.30           C  
-ATOM   1875  SD  MET A 233       0.723  42.518  85.334  1.00 38.70           S  
-ATOM   1876  CE  MET A 233       1.439  43.742  84.141  1.00 33.78           C  
-ATOM   1877  N   PRO A 234      -2.538  47.109  86.679  1.00 33.78           N  
-ATOM   1878  CA  PRO A 234      -3.659  48.050  86.539  1.00 33.36           C  
-ATOM   1879  C   PRO A 234      -4.966  47.473  86.000  1.00 32.81           C  
-ATOM   1880  O   PRO A 234      -6.015  47.942  86.430  1.00 33.83           O  
-ATOM   1881  CB  PRO A 234      -3.099  49.110  85.578  1.00 33.51           C  
-ATOM   1882  CG  PRO A 234      -1.641  49.097  85.841  1.00 33.40           C  
-ATOM   1883  CD  PRO A 234      -1.315  47.639  86.041  1.00 33.88           C  
-ATOM   1884  N   ASP A 235      -4.922  46.493  85.101  1.00 31.85           N  
-ATOM   1885  CA  ASP A 235      -6.152  45.961  84.513  1.00 30.95           C  
-ATOM   1886  C   ASP A 235      -6.388  44.499  84.845  1.00 30.13           C  
-ATOM   1887  O   ASP A 235      -7.177  43.817  84.194  1.00 29.53           O  
-ATOM   1888  CB  ASP A 235      -6.195  46.222  83.006  1.00 30.96           C  
-ATOM   1889  CG  ASP A 235      -6.146  47.699  82.684  1.00 31.95           C  
-ATOM   1890  OD1 ASP A 235      -6.680  48.492  83.481  1.00 32.96           O  
-ATOM   1891  OD2 ASP A 235      -5.579  48.168  81.676  1.00 34.86           O  
-ATOM   1892  N   TYR A 236      -5.691  44.019  85.866  1.00 29.41           N  
-ATOM   1893  CA  TYR A 236      -6.026  42.728  86.432  1.00 28.71           C  
-ATOM   1894  C   TYR A 236      -7.283  42.926  87.253  1.00 27.77           C  
-ATOM   1895  O   TYR A 236      -7.443  43.944  87.937  1.00 27.42           O  
-ATOM   1896  CB  TYR A 236      -4.904  42.170  87.321  1.00 29.16           C  
-ATOM   1897  CG  TYR A 236      -5.294  40.869  87.987  1.00 30.63           C  
-ATOM   1898  CD1 TYR A 236      -5.951  40.865  89.222  1.00 33.85           C  
-ATOM   1899  CD2 TYR A 236      -5.042  39.644  87.374  1.00 32.99           C  
-ATOM   1900  CE1 TYR A 236      -6.330  39.678  89.837  1.00 34.89           C  
-ATOM   1901  CE2 TYR A 236      -5.419  38.443  87.981  1.00 34.87           C  
-ATOM   1902  CZ  TYR A 236      -6.062  38.473  89.211  1.00 36.18           C  
-ATOM   1903  OH  TYR A 236      -6.439  37.295  89.819  1.00 38.86           O  
-ATOM   1904  N   LYS A 237      -8.174  41.948  87.179  1.00 26.74           N  
-ATOM   1905  CA  LYS A 237      -9.372  41.957  87.998  1.00 26.44           C  
-ATOM   1906  C   LYS A 237      -9.527  40.610  88.675  1.00 25.26           C  
-ATOM   1907  O   LYS A 237      -9.388  39.575  88.028  1.00 25.39           O  
-ATOM   1908  CB  LYS A 237     -10.599  42.314  87.148  1.00 26.86           C  
-ATOM   1909  CG  LYS A 237     -10.552  43.752  86.649  1.00 28.90           C  
-ATOM   1910  CD  LYS A 237     -11.423  43.981  85.431  1.00 33.34           C  
-ATOM   1911  CE  LYS A 237     -11.639  45.480  85.213  1.00 35.97           C  
-ATOM   1912  NZ  LYS A 237     -10.353  46.288  85.131  1.00 38.38           N  
-ATOM   1913  N   PRO A 238      -9.793  40.621  89.977  1.00 24.42           N  
-ATOM   1914  CA  PRO A 238      -9.967  39.376  90.734  1.00 24.17           C  
-ATOM   1915  C   PRO A 238     -11.151  38.525  90.246  1.00 23.50           C  
-ATOM   1916  O   PRO A 238     -11.149  37.322  90.467  1.00 23.07           O  
-ATOM   1917  CB  PRO A 238     -10.182  39.861  92.173  1.00 24.19           C  
-ATOM   1918  CG  PRO A 238     -10.644  41.292  92.025  1.00 24.71           C  
-ATOM   1919  CD  PRO A 238      -9.927  41.817  90.828  1.00 24.28           C  
-ATOM   1920  N   SER A 239     -12.119  39.128  89.563  1.00 23.41           N  
-ATOM   1921  CA  SER A 239     -13.223  38.363  88.979  1.00 23.32           C  
-ATOM   1922  C   SER A 239     -12.849  37.532  87.744  1.00 23.11           C  
-ATOM   1923  O   SER A 239     -13.636  36.677  87.324  1.00 23.21           O  
-ATOM   1924  CB  SER A 239     -14.404  39.279  88.644  1.00 23.60           C  
-ATOM   1925  OG  SER A 239     -14.024  40.256  87.693  1.00 24.78           O  
-ATOM   1926  N   PHE A 240     -11.670  37.779  87.158  1.00 22.44           N  
-ATOM   1927  CA  PHE A 240     -11.180  36.977  86.031  1.00 21.94           C  
-ATOM   1928  C   PHE A 240     -11.415  35.504  86.335  1.00 21.05           C  
-ATOM   1929  O   PHE A 240     -11.057  35.048  87.414  1.00 20.73           O  
-ATOM   1930  CB  PHE A 240      -9.667  37.176  85.806  1.00 21.67           C  
-ATOM   1931  CG  PHE A 240      -9.304  38.448  85.074  1.00 23.35           C  
-ATOM   1932  CD1 PHE A 240     -10.282  39.277  84.533  1.00 24.61           C  
-ATOM   1933  CD2 PHE A 240      -7.975  38.819  84.937  1.00 24.90           C  
-ATOM   1934  CE1 PHE A 240      -9.931  40.446  83.859  1.00 26.52           C  
-ATOM   1935  CE2 PHE A 240      -7.620  39.992  84.263  1.00 25.05           C  
-ATOM   1936  CZ  PHE A 240      -8.595  40.797  83.726  1.00 24.66           C  
-ATOM   1937  N   PRO A 241     -12.007  34.760  85.407  1.00 20.63           N  
-ATOM   1938  CA  PRO A 241     -12.115  33.304  85.570  1.00 21.00           C  
-ATOM   1939  C   PRO A 241     -10.730  32.667  85.768  1.00 21.68           C  
-ATOM   1940  O   PRO A 241      -9.735  33.151  85.209  1.00 21.36           O  
-ATOM   1941  CB  PRO A 241     -12.765  32.847  84.263  1.00 20.61           C  
-ATOM   1942  CG  PRO A 241     -13.500  34.063  83.770  1.00 20.44           C  
-ATOM   1943  CD  PRO A 241     -12.647  35.237  84.168  1.00 20.55           C  
-ATOM   1944  N   LYS A 242     -10.670  31.616  86.583  1.00 22.35           N  
-ATOM   1945  CA  LYS A 242      -9.401  30.960  86.882  1.00 23.33           C  
-ATOM   1946  C   LYS A 242      -9.256  29.649  86.134  1.00 22.98           C  
-ATOM   1947  O   LYS A 242      -9.517  28.588  86.694  1.00 23.31           O  
-ATOM   1948  CB  LYS A 242      -9.248  30.727  88.391  1.00 23.50           C  
-ATOM   1949  CG  LYS A 242      -8.692  31.926  89.135  1.00 26.26           C  
-ATOM   1950  CD  LYS A 242      -8.686  31.684  90.643  1.00 31.20           C  
-ATOM   1951  CE  LYS A 242      -8.202  32.907  91.422  1.00 33.28           C  
-ATOM   1952  NZ  LYS A 242      -9.159  34.051  91.301  1.00 37.64           N  
-ATOM   1953  N   TRP A 243      -8.807  29.716  84.885  1.00 22.48           N  
-ATOM   1954  CA  TRP A 243      -8.672  28.508  84.080  1.00 22.41           C  
-ATOM   1955  C   TRP A 243      -7.400  27.739  84.417  1.00 22.90           C  
-ATOM   1956  O   TRP A 243      -6.340  28.327  84.658  1.00 22.87           O  
-ATOM   1957  CB  TRP A 243      -8.688  28.842  82.587  1.00 22.18           C  
-ATOM   1958  CG  TRP A 243     -10.047  29.214  82.062  1.00 21.54           C  
-ATOM   1959  CD1 TRP A 243     -11.100  28.364  81.799  1.00 19.63           C  
-ATOM   1960  CD2 TRP A 243     -10.499  30.526  81.722  1.00 19.98           C  
-ATOM   1961  NE1 TRP A 243     -12.171  29.077  81.317  1.00 19.56           N  
-ATOM   1962  CE2 TRP A 243     -11.835  30.405  81.262  1.00 19.52           C  
-ATOM   1963  CE3 TRP A 243      -9.911  31.802  81.751  1.00 19.60           C  
-ATOM   1964  CZ2 TRP A 243     -12.582  31.502  80.838  1.00 18.67           C  
-ATOM   1965  CZ3 TRP A 243     -10.660  32.894  81.331  1.00 19.24           C  
-ATOM   1966  CH2 TRP A 243     -11.981  32.732  80.874  1.00 18.51           C  
-ATOM   1967  N   ALA A 244      -7.518  26.420  84.426  1.00 23.16           N  
-ATOM   1968  CA  ALA A 244      -6.377  25.543  84.593  1.00 24.11           C  
-ATOM   1969  C   ALA A 244      -5.478  25.636  83.363  1.00 24.84           C  
-ATOM   1970  O   ALA A 244      -5.944  25.888  82.241  1.00 24.70           O  
-ATOM   1971  CB  ALA A 244      -6.844  24.106  84.806  1.00 23.86           C  
-ATOM   1972  N   ARG A 245      -4.184  25.446  83.585  1.00 25.57           N  
-ATOM   1973  CA  ARG A 245      -3.229  25.358  82.497  1.00 26.24           C  
-ATOM   1974  C   ARG A 245      -3.391  24.029  81.759  1.00 26.99           C  
-ATOM   1975  O   ARG A 245      -3.417  22.972  82.371  1.00 26.63           O  
-ATOM   1976  CB  ARG A 245      -1.806  25.483  83.031  1.00 25.85           C  
-ATOM   1977  CG  ARG A 245      -0.738  25.501  81.948  1.00 24.47           C  
-ATOM   1978  CD  ARG A 245       0.627  25.938  82.475  1.00 23.37           C  
-ATOM   1979  NE  ARG A 245       1.691  25.788  81.486  1.00 24.16           N  
-ATOM   1980  CZ  ARG A 245       2.128  26.763  80.693  1.00 26.26           C  
-ATOM   1981  NH1 ARG A 245       1.589  27.986  80.753  1.00 22.99           N  
-ATOM   1982  NH2 ARG A 245       3.121  26.513  79.837  1.00 27.31           N  
-ATOM   1983  N   GLN A 246      -3.477  24.118  80.438  1.00 28.68           N  
-ATOM   1984  CA  GLN A 246      -3.557  22.967  79.544  1.00 30.72           C  
-ATOM   1985  C   GLN A 246      -2.243  22.205  79.462  1.00 30.87           C  
-ATOM   1986  O   GLN A 246      -1.174  22.800  79.583  1.00 31.42           O  
-ATOM   1987  CB  GLN A 246      -3.880  23.457  78.129  1.00 30.86           C  
-ATOM   1988  CG  GLN A 246      -5.159  22.904  77.554  1.00 34.06           C  
-ATOM   1989  CD  GLN A 246      -5.373  23.367  76.126  1.00 36.55           C  
-ATOM   1990  OE1 GLN A 246      -4.588  24.163  75.607  1.00 37.25           O  
-ATOM   1991  NE2 GLN A 246      -6.437  22.874  75.485  1.00 39.17           N  
-ATOM   1992  N   ASP A 247      -2.340  20.897  79.230  1.00 31.14           N  
-ATOM   1993  CA  ASP A 247      -1.219  20.092  78.756  1.00 31.48           C  
-ATOM   1994  C   ASP A 247      -0.664  20.802  77.533  1.00 30.82           C  
-ATOM   1995  O   ASP A 247      -1.350  20.949  76.519  1.00 31.58           O  
-ATOM   1996  CB  ASP A 247      -1.726  18.680  78.406  1.00 32.23           C  
-ATOM   1997  CG  ASP A 247      -0.666  17.787  77.748  1.00 34.49           C  
-ATOM   1998  OD1 ASP A 247       0.490  18.225  77.541  1.00 35.77           O  
-ATOM   1999  OD2 ASP A 247      -0.918  16.599  77.401  1.00 37.95           O  
-ATOM   2000  N   PHE A 248       0.576  21.261  77.632  1.00 29.95           N  
-ATOM   2001  CA  PHE A 248       1.186  22.057  76.573  1.00 28.66           C  
-ATOM   2002  C   PHE A 248       1.344  21.362  75.228  1.00 28.17           C  
-ATOM   2003  O   PHE A 248       1.422  22.023  74.191  1.00 28.27           O  
-ATOM   2004  CB  PHE A 248       2.524  22.648  77.025  1.00 28.93           C  
-ATOM   2005  CG  PHE A 248       2.860  23.938  76.338  1.00 27.81           C  
-ATOM   2006  CD1 PHE A 248       2.311  25.130  76.779  1.00 26.17           C  
-ATOM   2007  CD2 PHE A 248       3.687  23.954  75.224  1.00 26.67           C  
-ATOM   2008  CE1 PHE A 248       2.600  26.328  76.139  1.00 26.64           C  
-ATOM   2009  CE2 PHE A 248       3.967  25.144  74.572  1.00 26.85           C  
-ATOM   2010  CZ  PHE A 248       3.427  26.335  75.038  1.00 25.39           C  
-ATOM   2011  N   SER A 249       1.391  20.035  75.243  1.00 27.19           N  
-ATOM   2012  CA  SER A 249       1.407  19.240  74.014  1.00 26.41           C  
-ATOM   2013  C   SER A 249       0.121  19.375  73.196  1.00 26.29           C  
-ATOM   2014  O   SER A 249       0.083  18.975  72.029  1.00 25.83           O  
-ATOM   2015  CB  SER A 249       1.639  17.763  74.338  1.00 26.24           C  
-ATOM   2016  OG  SER A 249       0.555  17.263  75.099  1.00 24.55           O  
-ATOM   2017  N   LYS A 250      -0.930  19.904  73.821  1.00 25.76           N  
-ATOM   2018  CA  LYS A 250      -2.204  20.112  73.139  1.00 25.62           C  
-ATOM   2019  C   LYS A 250      -2.338  21.489  72.498  1.00 24.88           C  
-ATOM   2020  O   LYS A 250      -3.217  21.687  71.684  1.00 25.09           O  
-ATOM   2021  CB  LYS A 250      -3.389  19.848  74.084  1.00 26.12           C  
-ATOM   2022  CG  LYS A 250      -3.376  18.473  74.738  1.00 26.57           C  
-ATOM   2023  CD  LYS A 250      -3.916  17.409  73.804  1.00 27.73           C  
-ATOM   2024  CE  LYS A 250      -2.867  16.352  73.508  1.00 30.93           C  
-ATOM   2025  NZ  LYS A 250      -2.495  15.532  74.691  1.00 29.31           N  
-ATOM   2026  N   VAL A 251      -1.460  22.429  72.850  1.00 24.47           N  
-ATOM   2027  CA  VAL A 251      -1.492  23.783  72.279  1.00 23.61           C  
-ATOM   2028  C   VAL A 251      -1.089  23.795  70.803  1.00 23.49           C  
-ATOM   2029  O   VAL A 251      -1.725  24.471  69.976  1.00 23.59           O  
-ATOM   2030  CB  VAL A 251      -0.599  24.762  73.068  1.00 23.87           C  
-ATOM   2031  CG1 VAL A 251      -0.721  26.186  72.505  1.00 22.90           C  
-ATOM   2032  CG2 VAL A 251      -0.961  24.732  74.551  1.00 23.90           C  
-ATOM   2033  N   VAL A 252      -0.023  23.061  70.488  1.00 22.20           N  
-ATOM   2034  CA  VAL A 252       0.445  22.885  69.120  1.00 21.46           C  
-ATOM   2035  C   VAL A 252       0.818  21.399  68.971  1.00 21.11           C  
-ATOM   2036  O   VAL A 252       2.004  21.028  69.032  1.00 20.34           O  
-ATOM   2037  CB  VAL A 252       1.644  23.823  68.785  1.00 21.67           C  
-ATOM   2038  CG1 VAL A 252       2.019  23.707  67.322  1.00 22.88           C  
-ATOM   2039  CG2 VAL A 252       1.311  25.280  69.072  1.00 21.19           C  
-ATOM   2040  N   PRO A 253      -0.199  20.547  68.791  1.00 20.85           N  
-ATOM   2041  CA  PRO A 253      -0.008  19.086  68.842  1.00 20.86           C  
-ATOM   2042  C   PRO A 253       1.107  18.517  67.948  1.00 21.05           C  
-ATOM   2043  O   PRO A 253       1.743  17.573  68.408  1.00 19.92           O  
-ATOM   2044  CB  PRO A 253      -1.384  18.524  68.445  1.00 20.68           C  
-ATOM   2045  CG  PRO A 253      -2.372  19.647  68.826  1.00 21.25           C  
-ATOM   2046  CD  PRO A 253      -1.610  20.914  68.528  1.00 20.61           C  
-ATOM   2047  N   PRO A 254       1.360  19.043  66.742  1.00 21.99           N  
-ATOM   2048  CA  PRO A 254       2.454  18.508  65.916  1.00 22.84           C  
-ATOM   2049  C   PRO A 254       3.849  18.746  66.504  1.00 23.68           C  
-ATOM   2050  O   PRO A 254       4.789  18.117  66.035  1.00 24.23           O  
-ATOM   2051  CB  PRO A 254       2.311  19.276  64.602  1.00 22.99           C  
-ATOM   2052  CG  PRO A 254       0.916  19.821  64.622  1.00 22.31           C  
-ATOM   2053  CD  PRO A 254       0.670  20.149  66.050  1.00 21.61           C  
-ATOM   2054  N   LEU A 255       3.992  19.613  67.505  1.00 24.45           N  
-ATOM   2055  CA  LEU A 255       5.329  19.938  68.025  1.00 25.29           C  
-ATOM   2056  C   LEU A 255       5.994  18.824  68.833  1.00 25.86           C  
-ATOM   2057  O   LEU A 255       5.390  18.218  69.726  1.00 25.27           O  
-ATOM   2058  CB  LEU A 255       5.310  21.231  68.845  1.00 25.12           C  
-ATOM   2059  CG  LEU A 255       6.182  22.429  68.424  1.00 25.29           C  
-ATOM   2060  CD1 LEU A 255       6.401  22.586  66.922  1.00 24.26           C  
-ATOM   2061  CD2 LEU A 255       5.591  23.693  69.004  1.00 24.81           C  
-ATOM   2062  N   ASP A 256       7.255  18.577  68.490  1.00 26.74           N  
-ATOM   2063  CA  ASP A 256       8.130  17.665  69.207  1.00 27.88           C  
-ATOM   2064  C   ASP A 256       8.527  18.298  70.536  1.00 27.39           C  
-ATOM   2065  O   ASP A 256       8.276  19.488  70.769  1.00 26.99           O  
-ATOM   2066  CB  ASP A 256       9.387  17.397  68.356  1.00 29.18           C  
-ATOM   2067  CG  ASP A 256      10.118  18.702  67.946  1.00 33.03           C  
-ATOM   2068  OD1 ASP A 256      11.199  18.990  68.515  1.00 35.28           O  
-ATOM   2069  OD2 ASP A 256       9.676  19.501  67.075  1.00 36.68           O  
-ATOM   2070  N   GLU A 257       9.159  17.502  71.393  1.00 27.02           N  
-ATOM   2071  CA  GLU A 257       9.614  17.936  72.719  1.00 27.27           C  
-ATOM   2072  C   GLU A 257      10.399  19.258  72.739  1.00 25.98           C  
-ATOM   2073  O   GLU A 257      10.139  20.131  73.571  1.00 26.06           O  
-ATOM   2074  CB  GLU A 257      10.463  16.836  73.371  1.00 27.73           C  
-ATOM   2075  CG  GLU A 257      10.456  16.917  74.888  1.00 32.23           C  
-ATOM   2076  CD  GLU A 257      11.397  15.935  75.571  1.00 38.41           C  
-ATOM   2077  OE1 GLU A 257      12.063  15.119  74.885  1.00 41.11           O  
-ATOM   2078  OE2 GLU A 257      11.466  15.984  76.821  1.00 42.16           O  
-ATOM   2079  N   ASP A 258      11.351  19.404  71.823  1.00 24.76           N  
-ATOM   2080  CA  ASP A 258      12.184  20.607  71.770  1.00 23.83           C  
-ATOM   2081  C   ASP A 258      11.384  21.848  71.360  1.00 22.89           C  
-ATOM   2082  O   ASP A 258      11.470  22.886  72.010  1.00 22.38           O  
-ATOM   2083  CB  ASP A 258      13.379  20.378  70.842  1.00 23.56           C  
-ATOM   2084  CG  ASP A 258      14.400  19.437  71.445  1.00 24.77           C  
-ATOM   2085  OD1 ASP A 258      14.466  19.357  72.694  1.00 25.36           O  
-ATOM   2086  OD2 ASP A 258      15.162  18.726  70.756  1.00 25.83           O  
-ATOM   2087  N   GLY A 259      10.597  21.725  70.293  1.00 22.41           N  
-ATOM   2088  CA  GLY A 259       9.729  22.810  69.841  1.00 22.16           C  
-ATOM   2089  C   GLY A 259       8.792  23.276  70.935  1.00 21.76           C  
-ATOM   2090  O   GLY A 259       8.647  24.481  71.178  1.00 21.63           O  
-ATOM   2091  N   ARG A 260       8.179  22.313  71.616  1.00 21.61           N  
-ATOM   2092  CA  ARG A 260       7.281  22.593  72.739  1.00 21.80           C  
-ATOM   2093  C   ARG A 260       7.987  23.329  73.861  1.00 20.70           C  
-ATOM   2094  O   ARG A 260       7.449  24.275  74.429  1.00 20.84           O  
-ATOM   2095  CB  ARG A 260       6.669  21.296  73.289  1.00 21.52           C  
-ATOM   2096  CG  ARG A 260       5.391  20.889  72.594  1.00 24.45           C  
-ATOM   2097  CD  ARG A 260       4.523  19.899  73.386  1.00 26.86           C  
-ATOM   2098  NE  ARG A 260       5.313  18.919  74.128  1.00 27.93           N  
-ATOM   2099  CZ  ARG A 260       5.768  17.777  73.629  1.00 28.33           C  
-ATOM   2100  NH1 ARG A 260       5.508  17.436  72.379  1.00 27.06           N  
-ATOM   2101  NH2 ARG A 260       6.490  16.964  74.394  1.00 29.23           N  
-ATOM   2102  N   SER A 261       9.180  22.853  74.198  1.00 20.31           N  
-ATOM   2103  CA  SER A 261      10.026  23.495  75.195  1.00 19.33           C  
-ATOM   2104  C   SER A 261      10.272  24.957  74.800  1.00 18.97           C  
-ATOM   2105  O   SER A 261      10.053  25.871  75.608  1.00 18.71           O  
-ATOM   2106  CB  SER A 261      11.358  22.737  75.340  1.00 19.35           C  
-ATOM   2107  OG  SER A 261      12.311  23.498  76.069  1.00 19.32           O  
-ATOM   2108  N   LEU A 262      10.702  25.170  73.557  1.00 18.40           N  
-ATOM   2109  CA  LEU A 262      10.986  26.524  73.064  1.00 18.04           C  
-ATOM   2110  C   LEU A 262       9.738  27.414  73.053  1.00 17.73           C  
-ATOM   2111  O   LEU A 262       9.778  28.546  73.541  1.00 17.92           O  
-ATOM   2112  CB  LEU A 262      11.659  26.484  71.678  1.00 17.93           C  
-ATOM   2113  CG  LEU A 262      11.887  27.825  70.948  1.00 18.05           C  
-ATOM   2114  CD1 LEU A 262      12.723  28.819  71.781  1.00 18.24           C  
-ATOM   2115  CD2 LEU A 262      12.538  27.589  69.604  1.00 18.55           C  
-ATOM   2116  N   LEU A 263       8.633  26.907  72.505  1.00 17.32           N  
-ATOM   2117  CA  LEU A 263       7.375  27.664  72.503  1.00 17.17           C  
-ATOM   2118  C   LEU A 263       6.979  28.098  73.912  1.00 17.32           C  
-ATOM   2119  O   LEU A 263       6.691  29.272  74.136  1.00 17.16           O  
-ATOM   2120  CB  LEU A 263       6.232  26.880  71.828  1.00 16.53           C  
-ATOM   2121  CG  LEU A 263       4.884  27.615  71.687  1.00 17.04           C  
-ATOM   2122  CD1 LEU A 263       4.997  28.849  70.812  1.00 14.19           C  
-ATOM   2123  CD2 LEU A 263       3.788  26.683  71.146  1.00 14.91           C  
-ATOM   2124  N   SER A 264       7.005  27.166  74.868  1.00 17.97           N  
-ATOM   2125  CA  SER A 264       6.642  27.487  76.257  1.00 18.58           C  
-ATOM   2126  C   SER A 264       7.533  28.579  76.874  1.00 18.74           C  
-ATOM   2127  O   SER A 264       7.077  29.388  77.680  1.00 18.45           O  
-ATOM   2128  CB  SER A 264       6.632  26.225  77.136  1.00 18.39           C  
-ATOM   2129  OG  SER A 264       7.951  25.728  77.336  1.00 21.07           O  
-ATOM   2130  N   GLN A 265       8.802  28.612  76.499  1.00 18.69           N  
-ATOM   2131  CA  GLN A 265       9.671  29.671  77.019  1.00 19.11           C  
-ATOM   2132  C   GLN A 265       9.408  31.011  76.337  1.00 18.85           C  
-ATOM   2133  O   GLN A 265       9.657  32.058  76.914  1.00 19.38           O  
-ATOM   2134  CB  GLN A 265      11.138  29.267  76.903  1.00 19.02           C  
-ATOM   2135  CG  GLN A 265      11.508  28.119  77.835  1.00 20.03           C  
-ATOM   2136  CD  GLN A 265      12.927  27.649  77.630  1.00 21.22           C  
-ATOM   2137  OE1 GLN A 265      13.148  26.570  77.115  1.00 23.47           O  
-ATOM   2138  NE2 GLN A 265      13.887  28.456  78.046  1.00 23.11           N  
-ATOM   2139  N   MET A 266       8.904  30.974  75.110  1.00 19.18           N  
-ATOM   2140  CA  MET A 266       8.494  32.200  74.407  1.00 19.32           C  
-ATOM   2141  C   MET A 266       7.135  32.729  74.893  1.00 20.29           C  
-ATOM   2142  O   MET A 266       6.857  33.924  74.771  1.00 20.30           O  
-ATOM   2143  CB  MET A 266       8.455  31.961  72.896  1.00 18.84           C  
-ATOM   2144  CG  MET A 266       9.811  31.567  72.325  1.00 17.58           C  
-ATOM   2145  SD  MET A 266       9.807  31.289  70.560  1.00 17.60           S  
-ATOM   2146  CE  MET A 266       9.902  32.964  69.980  1.00 17.18           C  
-ATOM   2147  N   LEU A 267       6.304  31.838  75.445  1.00 21.00           N  
-ATOM   2148  CA  LEU A 267       4.954  32.190  75.900  1.00 22.00           C  
-ATOM   2149  C   LEU A 267       4.828  32.236  77.422  1.00 22.97           C  
-ATOM   2150  O   LEU A 267       3.720  32.175  77.984  1.00 23.07           O  
-ATOM   2151  CB  LEU A 267       3.923  31.228  75.316  1.00 21.74           C  
-ATOM   2152  CG  LEU A 267       3.734  31.296  73.800  1.00 21.97           C  
-ATOM   2153  CD1 LEU A 267       2.627  30.359  73.375  1.00 20.17           C  
-ATOM   2154  CD2 LEU A 267       3.438  32.725  73.359  1.00 21.66           C  
-ATOM   2155  N   HIS A 268       5.970  32.358  78.088  1.00 23.53           N  
-ATOM   2156  CA  HIS A 268       5.993  32.514  79.531  1.00 24.29           C  
-ATOM   2157  C   HIS A 268       5.327  33.809  79.943  1.00 23.74           C  
-ATOM   2158  O   HIS A 268       5.589  34.862  79.349  1.00 24.00           O  
-ATOM   2159  CB  HIS A 268       7.426  32.519  80.033  1.00 25.21           C  
-ATOM   2160  CG  HIS A 268       7.587  31.915  81.383  1.00 28.61           C  
-ATOM   2161  ND1 HIS A 268       7.936  30.595  81.569  1.00 32.87           N  
-ATOM   2162  CD2 HIS A 268       7.449  32.449  82.618  1.00 32.13           C  
-ATOM   2163  CE1 HIS A 268       8.017  30.346  82.867  1.00 34.48           C  
-ATOM   2164  NE2 HIS A 268       7.729  31.455  83.525  1.00 33.94           N  
-ATOM   2165  N   TYR A 269       4.482  33.729  80.969  1.00 22.66           N  
-ATOM   2166  CA  TYR A 269       3.726  34.876  81.447  1.00 22.50           C  
-ATOM   2167  C   TYR A 269       4.600  36.021  81.950  1.00 22.43           C  
-ATOM   2168  O   TYR A 269       4.411  37.170  81.551  1.00 22.39           O  
-ATOM   2169  CB  TYR A 269       2.736  34.461  82.545  1.00 22.04           C  
-ATOM   2170  CG  TYR A 269       1.395  34.028  82.011  1.00 22.03           C  
-ATOM   2171  CD1 TYR A 269       0.573  34.930  81.318  1.00 20.70           C  
-ATOM   2172  CD2 TYR A 269       0.942  32.718  82.187  1.00 20.48           C  
-ATOM   2173  CE1 TYR A 269      -0.665  34.540  80.814  1.00 19.66           C  
-ATOM   2174  CE2 TYR A 269      -0.303  32.320  81.684  1.00 19.84           C  
-ATOM   2175  CZ  TYR A 269      -1.100  33.239  81.004  1.00 19.47           C  
-ATOM   2176  OH  TYR A 269      -2.332  32.859  80.500  1.00 18.45           O  
-ATOM   2177  N   ASP A 270       5.530  35.700  82.843  1.00 22.30           N  
-ATOM   2178  CA  ASP A 270       6.400  36.695  83.463  1.00 22.84           C  
-ATOM   2179  C   ASP A 270       7.424  37.194  82.433  1.00 22.40           C  
-ATOM   2180  O   ASP A 270       8.251  36.408  81.979  1.00 22.00           O  
-ATOM   2181  CB  ASP A 270       7.121  36.036  84.642  1.00 23.17           C  
-ATOM   2182  CG  ASP A 270       7.892  37.012  85.495  1.00 24.38           C  
-ATOM   2183  OD1 ASP A 270       8.253  38.108  85.032  1.00 24.72           O  
-ATOM   2184  OD2 ASP A 270       8.200  36.745  86.671  1.00 28.66           O  
-ATOM   2185  N   PRO A 271       7.375  38.478  82.069  1.00 22.34           N  
-ATOM   2186  CA  PRO A 271       8.304  39.039  81.078  1.00 22.74           C  
-ATOM   2187  C   PRO A 271       9.759  38.775  81.465  1.00 23.37           C  
-ATOM   2188  O   PRO A 271      10.560  38.512  80.575  1.00 23.36           O  
-ATOM   2189  CB  PRO A 271       8.018  40.543  81.149  1.00 22.98           C  
-ATOM   2190  CG  PRO A 271       6.582  40.603  81.561  1.00 22.52           C  
-ATOM   2191  CD  PRO A 271       6.464  39.509  82.593  1.00 22.54           C  
-ATOM   2192  N   ASN A 272      10.071  38.826  82.764  1.00 23.65           N  
-ATOM   2193  CA  ASN A 272      11.399  38.486  83.277  1.00 24.60           C  
-ATOM   2194  C   ASN A 272      11.866  37.065  82.977  1.00 24.07           C  
-ATOM   2195  O   ASN A 272      13.048  36.838  82.724  1.00 24.35           O  
-ATOM   2196  CB  ASN A 272      11.476  38.746  84.783  1.00 25.28           C  
-ATOM   2197  CG  ASN A 272      11.520  40.208  85.105  1.00 27.84           C  
-ATOM   2198  OD1 ASN A 272      11.235  41.052  84.249  1.00 32.85           O  
-ATOM   2199  ND2 ASN A 272      11.879  40.534  86.341  1.00 33.00           N  
-ATOM   2200  N   LYS A 273      10.940  36.115  82.993  1.00 22.84           N  
-ATOM   2201  CA  LYS A 273      11.270  34.721  82.720  1.00 21.86           C  
-ATOM   2202  C   LYS A 273      11.174  34.343  81.236  1.00 20.67           C  
-ATOM   2203  O   LYS A 273      11.820  33.398  80.810  1.00 20.86           O  
-ATOM   2204  CB  LYS A 273      10.398  33.791  83.573  1.00 22.17           C  
-ATOM   2205  CG  LYS A 273      10.347  34.172  85.070  1.00 25.17           C  
-ATOM   2206  CD  LYS A 273      10.192  32.941  85.985  1.00 30.18           C  
-ATOM   2207  CE  LYS A 273       8.760  32.779  86.527  1.00 32.61           C  
-ATOM   2208  NZ  LYS A 273       8.221  34.007  87.232  1.00 33.06           N  
-ATOM   2209  N   ARG A 274      10.356  35.058  80.462  1.00 19.24           N  
-ATOM   2210  CA  ARG A 274      10.267  34.835  79.018  1.00 18.54           C  
-ATOM   2211  C   ARG A 274      11.660  34.911  78.368  1.00 18.07           C  
-ATOM   2212  O   ARG A 274      12.446  35.812  78.657  1.00 17.18           O  
-ATOM   2213  CB  ARG A 274       9.326  35.862  78.368  1.00 18.14           C  
-ATOM   2214  CG  ARG A 274       8.739  35.441  77.009  1.00 17.49           C  
-ATOM   2215  CD  ARG A 274       7.592  36.356  76.510  1.00 17.98           C  
-ATOM   2216  NE  ARG A 274       6.627  36.676  77.569  1.00 16.23           N  
-ATOM   2217  CZ  ARG A 274       6.055  37.864  77.761  1.00 16.68           C  
-ATOM   2218  NH1 ARG A 274       6.325  38.893  76.968  1.00 14.71           N  
-ATOM   2219  NH2 ARG A 274       5.206  38.029  78.770  1.00 16.01           N  
-ATOM   2220  N   ILE A 275      11.943  33.966  77.484  1.00 18.00           N  
-ATOM   2221  CA  ILE A 275      13.266  33.856  76.864  1.00 17.85           C  
-ATOM   2222  C   ILE A 275      13.582  35.073  75.984  1.00 18.09           C  
-ATOM   2223  O   ILE A 275      12.699  35.582  75.286  1.00 17.61           O  
-ATOM   2224  CB  ILE A 275      13.349  32.535  76.056  1.00 17.79           C  
-ATOM   2225  CG1 ILE A 275      14.789  32.201  75.632  1.00 18.02           C  
-ATOM   2226  CG2 ILE A 275      12.370  32.541  74.866  1.00 17.94           C  
-ATOM   2227  CD1 ILE A 275      15.006  30.713  75.365  1.00 16.41           C  
-ATOM   2228  N   SER A 276      14.839  35.531  76.043  1.00 17.72           N  
-ATOM   2229  CA  SER A 276      15.356  36.567  75.148  1.00 17.25           C  
-ATOM   2230  C   SER A 276      15.582  35.965  73.774  1.00 17.12           C  
-ATOM   2231  O   SER A 276      15.786  34.768  73.667  1.00 16.70           O  
-ATOM   2232  CB  SER A 276      16.680  37.121  75.684  1.00 17.26           C  
-ATOM   2233  OG  SER A 276      17.756  36.237  75.410  1.00 17.24           O  
-ATOM   2234  N   ALA A 277      15.543  36.782  72.717  1.00 16.95           N  
-ATOM   2235  CA  ALA A 277      15.865  36.267  71.378  1.00 17.20           C  
-ATOM   2236  C   ALA A 277      17.279  35.691  71.345  1.00 17.78           C  
-ATOM   2237  O   ALA A 277      17.549  34.696  70.672  1.00 17.70           O  
-ATOM   2238  CB  ALA A 277      15.708  37.346  70.319  1.00 16.38           C  
-ATOM   2239  N   LYS A 278      18.174  36.332  72.085  1.00 18.19           N  
-ATOM   2240  CA  LYS A 278      19.561  35.910  72.151  1.00 19.23           C  
-ATOM   2241  C   LYS A 278      19.662  34.482  72.709  1.00 18.85           C  
-ATOM   2242  O   LYS A 278      20.265  33.603  72.079  1.00 18.16           O  
-ATOM   2243  CB  LYS A 278      20.325  36.923  73.001  1.00 19.68           C  
-ATOM   2244  CG  LYS A 278      21.772  36.655  73.164  1.00 23.04           C  
-ATOM   2245  CD  LYS A 278      22.536  37.956  73.232  1.00 26.21           C  
-ATOM   2246  CE  LYS A 278      22.504  38.531  74.608  1.00 27.96           C  
-ATOM   2247  NZ  LYS A 278      23.230  39.819  74.585  1.00 29.87           N  
-ATOM   2248  N   ALA A 279      19.043  34.242  73.868  1.00 18.71           N  
-ATOM   2249  CA  ALA A 279      19.081  32.912  74.478  1.00 18.58           C  
-ATOM   2250  C   ALA A 279      18.393  31.851  73.621  1.00 18.49           C  
-ATOM   2251  O   ALA A 279      18.852  30.713  73.562  1.00 18.54           O  
-ATOM   2252  CB  ALA A 279      18.499  32.944  75.897  1.00 18.48           C  
-ATOM   2253  N   ALA A 280      17.329  32.230  72.913  1.00 18.63           N  
-ATOM   2254  CA  ALA A 280      16.581  31.268  72.088  1.00 18.58           C  
-ATOM   2255  C   ALA A 280      17.373  30.684  70.921  1.00 18.16           C  
-ATOM   2256  O   ALA A 280      17.125  29.551  70.498  1.00 18.13           O  
-ATOM   2257  CB  ALA A 280      15.258  31.888  71.579  1.00 19.08           C  
-ATOM   2258  N   LEU A 281      18.315  31.457  70.393  1.00 17.44           N  
-ATOM   2259  CA  LEU A 281      19.140  30.992  69.281  1.00 17.24           C  
-ATOM   2260  C   LEU A 281      19.943  29.736  69.618  1.00 17.46           C  
-ATOM   2261  O   LEU A 281      20.300  28.984  68.721  1.00 17.73           O  
-ATOM   2262  CB  LEU A 281      20.092  32.101  68.814  1.00 17.31           C  
-ATOM   2263  CG  LEU A 281      19.418  33.319  68.173  1.00 15.99           C  
-ATOM   2264  CD1 LEU A 281      20.424  34.451  68.062  1.00 15.24           C  
-ATOM   2265  CD2 LEU A 281      18.862  32.923  66.805  1.00 15.95           C  
-ATOM   2266  N   ALA A 282      20.221  29.526  70.903  1.00 17.37           N  
-ATOM   2267  CA  ALA A 282      20.971  28.358  71.359  1.00 18.05           C  
-ATOM   2268  C   ALA A 282      20.082  27.229  71.881  1.00 18.32           C  
-ATOM   2269  O   ALA A 282      20.576  26.285  72.473  1.00 18.54           O  
-ATOM   2270  CB  ALA A 282      21.975  28.754  72.431  1.00 17.90           C  
-ATOM   2271  N   HIS A 283      18.778  27.315  71.649  1.00 18.73           N  
-ATOM   2272  CA  HIS A 283      17.866  26.261  72.084  1.00 19.04           C  
-ATOM   2273  C   HIS A 283      18.060  24.982  71.260  1.00 19.51           C  
-ATOM   2274  O   HIS A 283      18.230  25.066  70.046  1.00 18.95           O  
-ATOM   2275  CB  HIS A 283      16.406  26.736  71.972  1.00 19.18           C  
-ATOM   2276  CG  HIS A 283      15.440  25.867  72.714  1.00 18.40           C  
-ATOM   2277  ND1 HIS A 283      14.986  24.669  72.214  1.00 17.81           N  
-ATOM   2278  CD2 HIS A 283      14.861  26.011  73.929  1.00 16.97           C  
-ATOM   2279  CE1 HIS A 283      14.171  24.108  73.088  1.00 17.41           C  
-ATOM   2280  NE2 HIS A 283      14.073  24.906  74.134  1.00 18.22           N  
-ATOM   2281  N   PRO A 284      17.984  23.811  71.911  1.00 20.31           N  
-ATOM   2282  CA  PRO A 284      18.108  22.502  71.240  1.00 20.83           C  
-ATOM   2283  C   PRO A 284      17.226  22.307  70.011  1.00 21.30           C  
-ATOM   2284  O   PRO A 284      17.604  21.527  69.130  1.00 21.14           O  
-ATOM   2285  CB  PRO A 284      17.656  21.515  72.319  1.00 20.82           C  
-ATOM   2286  CG  PRO A 284      17.933  22.183  73.581  1.00 21.35           C  
-ATOM   2287  CD  PRO A 284      17.787  23.651  73.362  1.00 20.67           C  
-ATOM   2288  N   PHE A 285      16.070  22.974  69.967  1.00 21.70           N  
-ATOM   2289  CA  PHE A 285      15.193  22.931  68.795  1.00 22.74           C  
-ATOM   2290  C   PHE A 285      15.959  23.255  67.518  1.00 23.23           C  
-ATOM   2291  O   PHE A 285      15.671  22.704  66.471  1.00 23.72           O  
-ATOM   2292  CB  PHE A 285      14.012  23.901  68.961  1.00 22.45           C  
-ATOM   2293  CG  PHE A 285      13.058  23.921  67.789  1.00 22.58           C  
-ATOM   2294  CD1 PHE A 285      12.307  22.791  67.461  1.00 22.18           C  
-ATOM   2295  CD2 PHE A 285      12.894  25.075  67.028  1.00 22.51           C  
-ATOM   2296  CE1 PHE A 285      11.420  22.803  66.403  1.00 21.41           C  
-ATOM   2297  CE2 PHE A 285      11.997  25.107  65.957  1.00 23.13           C  
-ATOM   2298  CZ  PHE A 285      11.259  23.960  65.642  1.00 23.47           C  
-ATOM   2299  N   PHE A 286      16.952  24.129  67.615  1.00 24.08           N  
-ATOM   2300  CA  PHE A 286      17.699  24.546  66.430  1.00 25.17           C  
-ATOM   2301  C   PHE A 286      18.952  23.712  66.105  1.00 27.01           C  
-ATOM   2302  O   PHE A 286      19.689  24.046  65.170  1.00 26.90           O  
-ATOM   2303  CB  PHE A 286      18.041  26.038  66.519  1.00 24.04           C  
-ATOM   2304  CG  PHE A 286      16.828  26.938  66.594  1.00 21.49           C  
-ATOM   2305  CD1 PHE A 286      15.886  26.962  65.560  1.00 19.52           C  
-ATOM   2306  CD2 PHE A 286      16.621  27.752  67.700  1.00 18.44           C  
-ATOM   2307  CE1 PHE A 286      14.766  27.815  65.636  1.00 16.79           C  
-ATOM   2308  CE2 PHE A 286      15.507  28.598  67.775  1.00 16.55           C  
-ATOM   2309  CZ  PHE A 286      14.584  28.623  66.742  1.00 14.46           C  
-ATOM   2310  N   GLN A 287      19.178  22.622  66.840  1.00 29.07           N  
-ATOM   2311  CA  GLN A 287      20.410  21.840  66.684  1.00 31.55           C  
-ATOM   2312  C   GLN A 287      20.720  21.433  65.246  1.00 32.23           C  
-ATOM   2313  O   GLN A 287      21.889  21.434  64.837  1.00 32.78           O  
-ATOM   2314  CB  GLN A 287      20.447  20.628  67.625  1.00 32.07           C  
-ATOM   2315  CG  GLN A 287      19.480  19.477  67.280  1.00 36.63           C  
-ATOM   2316  CD  GLN A 287      19.001  18.737  68.519  1.00 41.11           C  
-ATOM   2317  OE1 GLN A 287      19.815  18.248  69.306  1.00 43.79           O  
-ATOM   2318  NE2 GLN A 287      17.685  18.667  68.704  1.00 43.15           N  
-ATOM   2319  N   ASP A 288      19.686  21.126  64.470  1.00 32.79           N  
-ATOM   2320  CA  ASP A 288      19.883  20.699  63.086  1.00 33.69           C  
-ATOM   2321  C   ASP A 288      19.390  21.704  62.033  1.00 33.49           C  
-ATOM   2322  O   ASP A 288      19.045  21.318  60.912  1.00 33.70           O  
-ATOM   2323  CB  ASP A 288      19.232  19.322  62.865  1.00 34.47           C  
-ATOM   2324  CG  ASP A 288      17.740  19.295  63.231  1.00 36.78           C  
-ATOM   2325  OD1 ASP A 288      17.207  20.303  63.760  1.00 38.45           O  
-ATOM   2326  OD2 ASP A 288      17.019  18.284  63.033  1.00 41.00           O  
-ATOM   2327  N   VAL A 289      19.379  22.989  62.378  1.00 33.23           N  
-ATOM   2328  CA  VAL A 289      18.826  24.009  61.481  1.00 32.67           C  
-ATOM   2329  C   VAL A 289      19.635  24.172  60.184  1.00 33.36           C  
-ATOM   2330  O   VAL A 289      20.869  24.128  60.184  1.00 33.74           O  
-ATOM   2331  CB  VAL A 289      18.604  25.371  62.212  1.00 32.32           C  
-ATOM   2332  CG1 VAL A 289      19.939  26.101  62.487  1.00 31.65           C  
-ATOM   2333  CG2 VAL A 289      17.649  26.252  61.439  1.00 30.71           C  
-ATOM   2334  N   THR A 290      18.914  24.328  59.082  1.00 33.62           N  
-ATOM   2335  CA  THR A 290      19.481  24.707  57.796  1.00 34.46           C  
-ATOM   2336  C   THR A 290      18.588  25.807  57.255  1.00 34.93           C  
-ATOM   2337  O   THR A 290      17.541  26.098  57.842  1.00 35.01           O  
-ATOM   2338  CB  THR A 290      19.461  23.519  56.808  1.00 34.34           C  
-ATOM   2339  OG1 THR A 290      18.269  22.749  57.011  1.00 35.27           O  
-ATOM   2340  CG2 THR A 290      20.573  22.537  57.115  1.00 34.25           C  
-ATOM   2341  N   LYS A 291      18.986  26.400  56.131  1.00 35.18           N  
-ATOM   2342  CA  LYS A 291      18.227  27.476  55.506  1.00 35.53           C  
-ATOM   2343  C   LYS A 291      17.766  27.072  54.100  1.00 35.39           C  
-ATOM   2344  O   LYS A 291      18.311  27.550  53.104  1.00 35.26           O  
-ATOM   2345  CB  LYS A 291      19.082  28.749  55.462  1.00 35.88           C  
-ATOM   2346  CG  LYS A 291      18.364  30.024  55.017  1.00 37.44           C  
-ATOM   2347  CD  LYS A 291      19.183  30.777  53.976  1.00 40.27           C  
-ATOM   2348  CE  LYS A 291      18.739  32.222  53.843  1.00 42.36           C  
-ATOM   2349  NZ  LYS A 291      19.155  33.077  55.009  1.00 44.27           N  
-ATOM   2350  N   PRO A 292      16.756  26.211  54.004  1.00 35.32           N  
-ATOM   2351  CA  PRO A 292      16.304  25.755  52.693  1.00 35.62           C  
-ATOM   2352  C   PRO A 292      15.490  26.835  51.990  1.00 35.90           C  
-ATOM   2353  O   PRO A 292      14.896  27.704  52.624  1.00 35.36           O  
-ATOM   2354  CB  PRO A 292      15.423  24.548  53.028  1.00 35.52           C  
-ATOM   2355  CG  PRO A 292      14.881  24.849  54.375  1.00 35.26           C  
-ATOM   2356  CD  PRO A 292      15.941  25.631  55.087  1.00 35.16           C  
-ATOM   2357  N   VAL A 293      15.506  26.767  50.666  1.00 36.39           N  
-ATOM   2358  CA  VAL A 293      14.678  27.578  49.793  1.00 36.73           C  
-ATOM   2359  C   VAL A 293      13.199  27.282  50.109  1.00 37.34           C  
-ATOM   2360  O   VAL A 293      12.875  26.160  50.520  1.00 36.85           O  
-ATOM   2361  CB  VAL A 293      15.054  27.229  48.324  1.00 36.95           C  
-ATOM   2362  CG1 VAL A 293      13.904  26.610  47.559  1.00 36.78           C  
-ATOM   2363  CG2 VAL A 293      15.661  28.409  47.611  1.00 36.43           C  
-ATOM   2364  N   PRO A 294      12.307  28.272  49.971  1.00 38.07           N  
-ATOM   2365  CA  PRO A 294      10.875  28.010  50.167  1.00 38.80           C  
-ATOM   2366  C   PRO A 294      10.401  26.959  49.172  1.00 39.87           C  
-ATOM   2367  O   PRO A 294      10.848  26.921  48.022  1.00 39.98           O  
-ATOM   2368  CB  PRO A 294      10.202  29.367  49.907  1.00 38.71           C  
-ATOM   2369  CG  PRO A 294      11.240  30.229  49.277  1.00 38.51           C  
-ATOM   2370  CD  PRO A 294      12.574  29.685  49.649  1.00 37.87           C  
-ATOM   2371  N   HIS A 295       9.514  26.091  49.634  1.00 41.06           N  
-ATOM   2372  CA  HIS A 295       9.070  24.948  48.848  1.00 42.07           C  
-ATOM   2373  C   HIS A 295       8.089  25.329  47.736  1.00 42.68           C  
-ATOM   2374  O   HIS A 295       7.769  24.507  46.876  1.00 42.77           O  
-ATOM   2375  CB  HIS A 295       8.462  23.903  49.770  1.00 42.01           C  
-ATOM   2376  CG  HIS A 295       7.266  24.380  50.530  1.00 42.67           C  
-ATOM   2377  ND1 HIS A 295       6.070  23.693  50.539  1.00 43.38           N  
-ATOM   2378  CD2 HIS A 295       7.083  25.467  51.313  1.00 42.86           C  
-ATOM   2379  CE1 HIS A 295       5.200  24.342  51.292  1.00 43.91           C  
-ATOM   2380  NE2 HIS A 295       5.791  25.420  51.777  1.00 43.77           N  
-ATOM   2381  N   LEU A 296       7.640  26.582  47.754  1.00 43.27           N  
-ATOM   2382  CA  LEU A 296       6.664  27.088  46.800  1.00 43.77           C  
-ATOM   2383  C   LEU A 296       7.268  28.218  45.986  1.00 43.92           C  
-ATOM   2384  O   LEU A 296       7.883  29.124  46.564  1.00 44.05           O  
-ATOM   2385  CB  LEU A 296       5.413  27.591  47.530  1.00 43.96           C  
-ATOM   2386  CG  LEU A 296       4.681  26.620  48.459  1.00 44.81           C  
-ATOM   2387  CD1 LEU A 296       3.640  27.351  49.288  1.00 45.40           C  
-ATOM   2388  CD2 LEU A 296       4.018  25.554  47.631  1.00 45.74           C  
-TER    2389      LEU A 296                                                      
-ATOM   2390  N   VAL B 175      16.136  44.482  78.989  1.00 38.30           N  
-ATOM   2391  CA  VAL B 175      16.559  44.258  80.421  1.00 37.87           C  
-ATOM   2392  C   VAL B 175      17.942  43.544  80.501  1.00 37.42           C  
-ATOM   2393  O   VAL B 175      18.791  43.782  79.633  1.00 37.77           O  
-ATOM   2394  CB  VAL B 175      15.432  43.591  81.293  1.00 38.03           C  
-ATOM   2395  CG1 VAL B 175      14.883  44.572  82.336  1.00 38.71           C  
-ATOM   2396  CG2 VAL B 175      14.304  43.017  80.445  1.00 37.71           C  
-ATOM   2397  N   PRO B 176      18.191  42.688  81.501  1.00 36.92           N  
-ATOM   2398  CA  PRO B 176      19.557  42.207  81.768  1.00 36.16           C  
-ATOM   2399  C   PRO B 176      20.289  41.551  80.590  1.00 35.14           C  
-ATOM   2400  O   PRO B 176      21.491  41.774  80.455  1.00 35.01           O  
-ATOM   2401  CB  PRO B 176      19.353  41.193  82.902  1.00 36.36           C  
-ATOM   2402  CG  PRO B 176      17.918  40.786  82.779  1.00 36.69           C  
-ATOM   2403  CD  PRO B 176      17.226  42.065  82.429  1.00 36.60           C  
-ATOM   2404  N   ASP B 177      19.595  40.782  79.754  1.00 33.92           N  
-ATOM   2405  CA  ASP B 177      20.243  40.087  78.631  1.00 33.01           C  
-ATOM   2406  C   ASP B 177      20.937  41.017  77.619  1.00 31.40           C  
-ATOM   2407  O   ASP B 177      21.870  40.589  76.917  1.00 32.13           O  
-ATOM   2408  CB  ASP B 177      19.246  39.179  77.891  1.00 33.49           C  
-ATOM   2409  CG  ASP B 177      19.430  37.701  78.221  1.00 36.60           C  
-ATOM   2410  OD1 ASP B 177      19.269  37.322  79.408  1.00 38.93           O  
-ATOM   2411  OD2 ASP B 177      19.731  36.839  77.358  1.00 39.08           O  
-ATOM   2412  N   TYR B 178      20.498  42.269  77.536  1.00 28.77           N  
-ATOM   2413  CA  TYR B 178      21.039  43.192  76.535  1.00 26.96           C  
-ATOM   2414  C   TYR B 178      21.749  44.420  77.100  1.00 26.31           C  
-ATOM   2415  O   TYR B 178      22.187  45.264  76.335  1.00 25.67           O  
-ATOM   2416  CB  TYR B 178      19.936  43.640  75.557  1.00 26.25           C  
-ATOM   2417  CG  TYR B 178      19.307  42.512  74.794  1.00 24.10           C  
-ATOM   2418  CD1 TYR B 178      19.969  41.912  73.724  1.00 23.20           C  
-ATOM   2419  CD2 TYR B 178      18.053  42.029  75.151  1.00 21.62           C  
-ATOM   2420  CE1 TYR B 178      19.390  40.858  73.017  1.00 21.41           C  
-ATOM   2421  CE2 TYR B 178      17.467  40.982  74.466  1.00 21.95           C  
-ATOM   2422  CZ  TYR B 178      18.139  40.394  73.401  1.00 21.31           C  
-ATOM   2423  OH  TYR B 178      17.551  39.356  72.714  1.00 18.96           O  
-ATOM   2424  N   HIS B 179      21.844  44.525  78.426  1.00 26.39           N  
-ATOM   2425  CA  HIS B 179      22.468  45.673  79.089  1.00 27.09           C  
-ATOM   2426  C   HIS B 179      23.830  46.041  78.459  1.00 26.37           C  
-ATOM   2427  O   HIS B 179      24.035  47.168  78.010  1.00 26.10           O  
-ATOM   2428  CB  HIS B 179      22.661  45.371  80.581  1.00 27.71           C  
-ATOM   2429  CG  HIS B 179      21.421  45.516  81.410  1.00 31.19           C  
-ATOM   2430  ND1 HIS B 179      20.229  46.002  80.912  1.00 34.57           N  
-ATOM   2431  CD2 HIS B 179      21.193  45.237  82.718  1.00 34.59           C  
-ATOM   2432  CE1 HIS B 179      19.323  46.018  81.876  1.00 35.36           C  
-ATOM   2433  NE2 HIS B 179      19.880  45.556  82.980  1.00 35.80           N  
-ATOM   2434  N   GLU B 180      24.734  45.063  78.419  1.00 25.88           N  
-ATOM   2435  CA  GLU B 180      26.084  45.222  77.879  1.00 25.67           C  
-ATOM   2436  C   GLU B 180      26.126  45.528  76.374  1.00 24.35           C  
-ATOM   2437  O   GLU B 180      26.871  46.405  75.955  1.00 24.15           O  
-ATOM   2438  CB  GLU B 180      26.922  43.976  78.190  1.00 26.11           C  
-ATOM   2439  CG  GLU B 180      28.413  44.158  77.935  1.00 30.52           C  
-ATOM   2440  CD  GLU B 180      29.198  42.874  78.112  1.00 35.57           C  
-ATOM   2441  OE1 GLU B 180      29.083  42.232  79.180  1.00 38.63           O  
-ATOM   2442  OE2 GLU B 180      29.933  42.508  77.176  1.00 38.90           O  
-ATOM   2443  N   ASP B 181      25.338  44.807  75.570  1.00 23.09           N  
-ATOM   2444  CA  ASP B 181      25.275  45.048  74.125  1.00 22.14           C  
-ATOM   2445  C   ASP B 181      24.885  46.498  73.837  1.00 20.98           C  
-ATOM   2446  O   ASP B 181      25.513  47.175  73.028  1.00 20.58           O  
-ATOM   2447  CB  ASP B 181      24.220  44.153  73.463  1.00 22.70           C  
-ATOM   2448  CG  ASP B 181      24.611  42.684  73.421  1.00 25.19           C  
-ATOM   2449  OD1 ASP B 181      25.793  42.343  73.660  1.00 27.31           O  
-ATOM   2450  OD2 ASP B 181      23.778  41.790  73.137  1.00 27.65           O  
-ATOM   2451  N   ILE B 182      23.830  46.954  74.508  1.00 19.37           N  
-ATOM   2452  CA  ILE B 182      23.287  48.290  74.316  1.00 17.83           C  
-ATOM   2453  C   ILE B 182      24.280  49.384  74.729  1.00 17.76           C  
-ATOM   2454  O   ILE B 182      24.500  50.330  73.979  1.00 17.30           O  
-ATOM   2455  CB  ILE B 182      21.930  48.426  75.059  1.00 17.63           C  
-ATOM   2456  CG1 ILE B 182      20.883  47.531  74.373  1.00 17.15           C  
-ATOM   2457  CG2 ILE B 182      21.477  49.891  75.102  1.00 15.18           C  
-ATOM   2458  CD1 ILE B 182      19.587  47.317  75.175  1.00 18.06           C  
-ATOM   2459  N   HIS B 183      24.868  49.243  75.915  1.00 17.87           N  
-ATOM   2460  CA  HIS B 183      25.887  50.179  76.385  1.00 18.17           C  
-ATOM   2461  C   HIS B 183      27.057  50.280  75.377  1.00 17.79           C  
-ATOM   2462  O   HIS B 183      27.423  51.372  74.968  1.00 18.21           O  
-ATOM   2463  CB  HIS B 183      26.402  49.790  77.767  1.00 17.50           C  
-ATOM   2464  CG  HIS B 183      27.538  50.643  78.231  1.00 17.95           C  
-ATOM   2465  ND1 HIS B 183      27.350  51.847  78.872  1.00 19.12           N  
-ATOM   2466  CD2 HIS B 183      28.875  50.486  78.106  1.00 16.41           C  
-ATOM   2467  CE1 HIS B 183      28.524  52.391  79.134  1.00 18.07           C  
-ATOM   2468  NE2 HIS B 183      29.463  51.579  78.685  1.00 19.95           N  
-ATOM   2469  N   THR B 184      27.600  49.136  74.974  1.00 17.90           N  
-ATOM   2470  CA  THR B 184      28.605  49.050  73.906  1.00 18.10           C  
-ATOM   2471  C   THR B 184      28.156  49.796  72.666  1.00 18.27           C  
-ATOM   2472  O   THR B 184      28.911  50.603  72.109  1.00 18.10           O  
-ATOM   2473  CB  THR B 184      28.864  47.575  73.557  1.00 18.01           C  
-ATOM   2474  OG1 THR B 184      29.580  46.966  74.631  1.00 19.17           O  
-ATOM   2475  CG2 THR B 184      29.823  47.424  72.353  1.00 17.97           C  
-ATOM   2476  N   TYR B 185      26.922  49.535  72.238  1.00 18.35           N  
-ATOM   2477  CA  TYR B 185      26.408  50.152  71.028  1.00 18.59           C  
-ATOM   2478  C   TYR B 185      26.298  51.678  71.153  1.00 18.57           C  
-ATOM   2479  O   TYR B 185      26.668  52.403  70.228  1.00 17.93           O  
-ATOM   2480  CB  TYR B 185      25.060  49.552  70.627  1.00 18.81           C  
-ATOM   2481  CG  TYR B 185      24.499  50.172  69.370  1.00 20.28           C  
-ATOM   2482  CD1 TYR B 185      25.221  50.128  68.170  1.00 21.76           C  
-ATOM   2483  CD2 TYR B 185      23.262  50.807  69.373  1.00 21.04           C  
-ATOM   2484  CE1 TYR B 185      24.726  50.701  67.012  1.00 22.26           C  
-ATOM   2485  CE2 TYR B 185      22.754  51.385  68.206  1.00 22.54           C  
-ATOM   2486  CZ  TYR B 185      23.495  51.315  67.037  1.00 23.13           C  
-ATOM   2487  OH  TYR B 185      23.017  51.868  65.885  1.00 24.79           O  
-ATOM   2488  N   LEU B 186      25.798  52.160  72.292  1.00 18.29           N  
-ATOM   2489  CA  LEU B 186      25.677  53.599  72.510  1.00 18.90           C  
-ATOM   2490  C   LEU B 186      27.030  54.276  72.604  1.00 19.09           C  
-ATOM   2491  O   LEU B 186      27.162  55.440  72.245  1.00 19.81           O  
-ATOM   2492  CB  LEU B 186      24.877  53.915  73.776  1.00 18.69           C  
-ATOM   2493  CG  LEU B 186      23.436  53.412  73.861  1.00 19.74           C  
-ATOM   2494  CD1 LEU B 186      22.843  53.776  75.227  1.00 19.96           C  
-ATOM   2495  CD2 LEU B 186      22.592  53.943  72.706  1.00 17.77           C  
-ATOM   2496  N   ARG B 187      28.028  53.553  73.101  1.00 19.45           N  
-ATOM   2497  CA  ARG B 187      29.383  54.093  73.183  1.00 20.06           C  
-ATOM   2498  C   ARG B 187      29.957  54.291  71.776  1.00 20.34           C  
-ATOM   2499  O   ARG B 187      30.697  55.239  71.523  1.00 19.82           O  
-ATOM   2500  CB  ARG B 187      30.272  53.182  74.039  1.00 19.44           C  
-ATOM   2501  CG  ARG B 187      30.061  53.380  75.545  1.00 19.93           C  
-ATOM   2502  CD  ARG B 187      30.663  54.670  76.111  1.00 18.09           C  
-ATOM   2503  NE  ARG B 187      32.109  54.689  75.888  1.00 19.05           N  
-ATOM   2504  CZ  ARG B 187      33.012  54.244  76.744  1.00 16.44           C  
-ATOM   2505  NH1 ARG B 187      32.636  53.759  77.915  1.00 16.46           N  
-ATOM   2506  NH2 ARG B 187      34.301  54.284  76.426  1.00 15.13           N  
-ATOM   2507  N   GLU B 188      29.573  53.407  70.857  1.00 21.13           N  
-ATOM   2508  CA  GLU B 188      29.946  53.550  69.453  1.00 22.10           C  
-ATOM   2509  C   GLU B 188      29.191  54.714  68.791  1.00 22.08           C  
-ATOM   2510  O   GLU B 188      29.789  55.516  68.079  1.00 21.52           O  
-ATOM   2511  CB  GLU B 188      29.708  52.232  68.702  1.00 22.46           C  
-ATOM   2512  CG  GLU B 188      29.827  52.329  67.189  1.00 26.08           C  
-ATOM   2513  CD  GLU B 188      29.271  51.113  66.455  1.00 30.14           C  
-ATOM   2514  OE1 GLU B 188      28.923  50.099  67.103  1.00 34.04           O  
-ATOM   2515  OE2 GLU B 188      29.179  51.169  65.213  1.00 32.30           O  
-ATOM   2516  N   MET B 189      27.881  54.801  69.036  1.00 22.05           N  
-ATOM   2517  CA  MET B 189      27.054  55.808  68.391  1.00 22.83           C  
-ATOM   2518  C   MET B 189      27.324  57.231  68.884  1.00 22.60           C  
-ATOM   2519  O   MET B 189      27.180  58.187  68.119  1.00 22.73           O  
-ATOM   2520  CB  MET B 189      25.568  55.479  68.542  1.00 22.94           C  
-ATOM   2521  CG  MET B 189      25.091  54.252  67.771  1.00 25.77           C  
-ATOM   2522  SD  MET B 189      25.918  53.901  66.179  1.00 32.35           S  
-ATOM   2523  CE  MET B 189      25.110  55.106  65.123  1.00 29.45           C  
-ATOM   2524  N   GLU B 190      27.711  57.382  70.149  1.00 22.40           N  
-ATOM   2525  CA  GLU B 190      27.931  58.724  70.687  1.00 22.67           C  
-ATOM   2526  C   GLU B 190      29.112  59.401  69.989  1.00 23.02           C  
-ATOM   2527  O   GLU B 190      29.108  60.616  69.793  1.00 22.74           O  
-ATOM   2528  CB  GLU B 190      28.068  58.726  72.223  1.00 22.01           C  
-ATOM   2529  CG  GLU B 190      29.402  58.223  72.769  1.00 21.49           C  
-ATOM   2530  CD  GLU B 190      29.543  58.412  74.272  1.00 21.22           C  
-ATOM   2531  OE1 GLU B 190      28.788  59.211  74.860  1.00 22.25           O  
-ATOM   2532  OE2 GLU B 190      30.415  57.767  74.870  1.00 19.77           O  
-ATOM   2533  N   VAL B 191      30.106  58.608  69.597  1.00 24.04           N  
-ATOM   2534  CA  VAL B 191      31.232  59.114  68.808  1.00 24.95           C  
-ATOM   2535  C   VAL B 191      30.760  59.524  67.412  1.00 26.27           C  
-ATOM   2536  O   VAL B 191      31.149  60.577  66.897  1.00 27.27           O  
-ATOM   2537  CB  VAL B 191      32.369  58.073  68.706  1.00 25.18           C  
-ATOM   2538  CG1 VAL B 191      33.463  58.536  67.728  1.00 23.52           C  
-ATOM   2539  CG2 VAL B 191      32.949  57.766  70.094  1.00 23.66           C  
-ATOM   2540  N   LYS B 192      29.895  58.714  66.818  1.00 27.50           N  
-ATOM   2541  CA  LYS B 192      29.344  59.008  65.495  1.00 29.28           C  
-ATOM   2542  C   LYS B 192      28.383  60.196  65.470  1.00 29.80           C  
-ATOM   2543  O   LYS B 192      28.254  60.863  64.438  1.00 30.12           O  
-ATOM   2544  CB  LYS B 192      28.676  57.759  64.902  1.00 29.60           C  
-ATOM   2545  CG  LYS B 192      29.677  56.684  64.516  1.00 31.39           C  
-ATOM   2546  CD  LYS B 192      29.025  55.331  64.256  1.00 35.58           C  
-ATOM   2547  CE  LYS B 192      30.097  54.240  64.231  1.00 37.78           C  
-ATOM   2548  NZ  LYS B 192      29.923  53.245  63.135  1.00 41.19           N  
-ATOM   2549  N   CYS B 193      27.716  60.461  66.594  1.00 30.33           N  
-ATOM   2550  CA  CYS B 193      26.704  61.524  66.662  1.00 31.22           C  
-ATOM   2551  C   CYS B 193      27.204  62.802  67.337  1.00 31.16           C  
-ATOM   2552  O   CYS B 193      26.425  63.731  67.583  1.00 30.91           O  
-ATOM   2553  CB  CYS B 193      25.436  61.023  67.366  1.00 31.18           C  
-ATOM   2554  SG  CYS B 193      24.488  59.832  66.375  1.00 35.21           S  
-ATOM   2555  N   LYS B 194      28.502  62.835  67.637  1.00 31.25           N  
-ATOM   2556  CA  LYS B 194      29.121  63.985  68.272  1.00 31.57           C  
-ATOM   2557  C   LYS B 194      29.133  65.188  67.334  1.00 31.53           C  
-ATOM   2558  O   LYS B 194      29.446  65.045  66.153  1.00 32.01           O  
-ATOM   2559  CB  LYS B 194      30.552  63.657  68.709  1.00 31.62           C  
-ATOM   2560  CG  LYS B 194      31.018  64.518  69.867  1.00 32.19           C  
-ATOM   2561  CD  LYS B 194      32.505  64.388  70.126  1.00 33.09           C  
-ATOM   2562  CE  LYS B 194      32.991  65.543  70.988  1.00 33.63           C  
-ATOM   2563  NZ  LYS B 194      34.295  65.227  71.642  1.00 36.94           N  
-ATOM   2564  N   PRO B 195      28.795  66.364  67.855  1.00 31.40           N  
-ATOM   2565  CA  PRO B 195      28.953  67.604  67.097  1.00 31.57           C  
-ATOM   2566  C   PRO B 195      30.442  67.992  67.053  1.00 31.91           C  
-ATOM   2567  O   PRO B 195      31.251  67.439  67.822  1.00 31.38           O  
-ATOM   2568  CB  PRO B 195      28.169  68.632  67.921  1.00 31.32           C  
-ATOM   2569  CG  PRO B 195      27.523  67.880  69.045  1.00 32.04           C  
-ATOM   2570  CD  PRO B 195      28.272  66.605  69.212  1.00 31.73           C  
-ATOM   2571  N   LYS B 196      30.807  68.919  66.175  1.00 32.22           N  
-ATOM   2572  CA  LYS B 196      32.191  69.377  66.156  1.00 33.56           C  
-ATOM   2573  C   LYS B 196      32.469  70.362  67.295  1.00 33.33           C  
-ATOM   2574  O   LYS B 196      31.746  71.345  67.476  1.00 33.25           O  
-ATOM   2575  CB  LYS B 196      32.605  69.916  64.786  1.00 33.89           C  
-ATOM   2576  CG  LYS B 196      32.009  71.240  64.390  1.00 37.39           C  
-ATOM   2577  CD  LYS B 196      33.033  72.098  63.638  1.00 41.05           C  
-ATOM   2578  CE  LYS B 196      33.078  71.771  62.159  1.00 43.16           C  
-ATOM   2579  NZ  LYS B 196      34.402  72.184  61.600  1.00 46.73           N  
-ATOM   2580  N   VAL B 197      33.506  70.057  68.071  1.00 33.34           N  
-ATOM   2581  CA  VAL B 197      33.865  70.827  69.262  1.00 33.87           C  
-ATOM   2582  C   VAL B 197      33.988  72.324  68.994  1.00 33.89           C  
-ATOM   2583  O   VAL B 197      33.693  73.136  69.870  1.00 34.10           O  
-ATOM   2584  CB  VAL B 197      35.210  70.351  69.883  1.00 33.88           C  
-ATOM   2585  CG1 VAL B 197      35.421  70.983  71.247  1.00 34.11           C  
-ATOM   2586  CG2 VAL B 197      35.263  68.840  69.990  1.00 34.23           C  
-ATOM   2587  N   GLY B 198      34.427  72.687  67.791  1.00 33.85           N  
-ATOM   2588  CA  GLY B 198      34.795  74.065  67.521  1.00 34.35           C  
-ATOM   2589  C   GLY B 198      33.832  74.899  66.696  1.00 34.46           C  
-ATOM   2590  O   GLY B 198      34.180  76.024  66.314  1.00 34.89           O  
-ATOM   2591  N   TYR B 199      32.628  74.381  66.446  1.00 33.91           N  
-ATOM   2592  CA  TYR B 199      31.719  74.986  65.469  1.00 33.43           C  
-ATOM   2593  C   TYR B 199      31.375  76.457  65.695  1.00 33.77           C  
-ATOM   2594  O   TYR B 199      31.192  77.200  64.726  1.00 33.53           O  
-ATOM   2595  CB  TYR B 199      30.457  74.130  65.250  1.00 33.04           C  
-ATOM   2596  CG  TYR B 199      29.314  74.328  66.226  1.00 31.42           C  
-ATOM   2597  CD1 TYR B 199      28.519  75.477  66.189  1.00 30.26           C  
-ATOM   2598  CD2 TYR B 199      28.999  73.342  67.155  1.00 29.39           C  
-ATOM   2599  CE1 TYR B 199      27.468  75.651  67.078  1.00 30.02           C  
-ATOM   2600  CE2 TYR B 199      27.946  73.502  68.044  1.00 29.34           C  
-ATOM   2601  CZ  TYR B 199      27.181  74.653  67.998  1.00 29.73           C  
-ATOM   2602  OH  TYR B 199      26.140  74.805  68.877  1.00 29.87           O  
-ATOM   2603  N   MET B 200      31.296  76.876  66.957  1.00 34.10           N  
-ATOM   2604  CA  MET B 200      30.885  78.243  67.274  1.00 34.76           C  
-ATOM   2605  C   MET B 200      31.878  79.287  66.744  1.00 35.34           C  
-ATOM   2606  O   MET B 200      31.466  80.356  66.292  1.00 34.81           O  
-ATOM   2607  CB  MET B 200      30.653  78.417  68.775  1.00 34.79           C  
-ATOM   2608  CG  MET B 200      29.672  79.529  69.128  1.00 34.44           C  
-ATOM   2609  SD  MET B 200      28.014  79.263  68.486  1.00 34.78           S  
-ATOM   2610  CE  MET B 200      27.329  78.248  69.761  1.00 37.15           C  
-ATOM   2611  N   LYS B 201      33.170  78.952  66.781  1.00 36.38           N  
-ATOM   2612  CA  LYS B 201      34.226  79.780  66.191  1.00 37.74           C  
-ATOM   2613  C   LYS B 201      33.941  80.043  64.719  1.00 37.95           C  
-ATOM   2614  O   LYS B 201      34.342  81.072  64.170  1.00 38.50           O  
-ATOM   2615  CB  LYS B 201      35.595  79.104  66.304  1.00 37.85           C  
-ATOM   2616  CG  LYS B 201      35.957  78.571  67.682  1.00 40.21           C  
-ATOM   2617  CD  LYS B 201      37.293  77.825  67.653  1.00 43.58           C  
-ATOM   2618  CE  LYS B 201      37.466  76.942  68.887  1.00 45.84           C  
-ATOM   2619  NZ  LYS B 201      38.848  77.041  69.468  1.00 48.47           N  
-ATOM   2620  N   LYS B 202      33.236  79.107  64.090  1.00 38.25           N  
-ATOM   2621  CA  LYS B 202      32.999  79.138  62.651  1.00 37.96           C  
-ATOM   2622  C   LYS B 202      31.613  79.663  62.307  1.00 37.45           C  
-ATOM   2623  O   LYS B 202      31.236  79.704  61.137  1.00 37.48           O  
-ATOM   2624  CB  LYS B 202      33.210  77.742  62.059  1.00 38.39           C  
-ATOM   2625  CG  LYS B 202      34.649  77.270  62.091  1.00 39.96           C  
-ATOM   2626  CD  LYS B 202      34.973  76.387  60.897  1.00 43.44           C  
-ATOM   2627  CE  LYS B 202      36.455  76.000  60.892  1.00 45.84           C  
-ATOM   2628  NZ  LYS B 202      36.685  74.645  60.291  1.00 47.61           N  
-ATOM   2629  N   GLN B 203      30.851  80.042  63.330  1.00 36.65           N  
-ATOM   2630  CA  GLN B 203      29.572  80.711  63.134  1.00 36.20           C  
-ATOM   2631  C   GLN B 203      29.773  82.221  63.253  1.00 36.37           C  
-ATOM   2632  O   GLN B 203      30.117  82.719  64.324  1.00 36.17           O  
-ATOM   2633  CB  GLN B 203      28.535  80.230  64.146  1.00 35.99           C  
-ATOM   2634  CG  GLN B 203      28.122  78.768  63.977  1.00 34.22           C  
-ATOM   2635  CD  GLN B 203      27.023  78.568  62.951  1.00 31.78           C  
-ATOM   2636  OE1 GLN B 203      26.394  79.531  62.496  1.00 29.22           O  
-ATOM   2637  NE2 GLN B 203      26.774  77.309  62.596  1.00 29.75           N  
-ATOM   2638  N   PRO B 204      29.578  82.943  62.150  1.00 36.52           N  
-ATOM   2639  CA  PRO B 204      29.857  84.382  62.111  1.00 36.60           C  
-ATOM   2640  C   PRO B 204      28.928  85.177  63.017  1.00 36.66           C  
-ATOM   2641  O   PRO B 204      29.372  86.141  63.652  1.00 37.25           O  
-ATOM   2642  CB  PRO B 204      29.596  84.755  60.645  1.00 36.57           C  
-ATOM   2643  CG  PRO B 204      29.602  83.465  59.900  1.00 36.75           C  
-ATOM   2644  CD  PRO B 204      29.086  82.440  60.855  1.00 36.61           C  
-ATOM   2645  N   ASP B 205      27.669  84.754  63.090  1.00 36.32           N  
-ATOM   2646  CA  ASP B 205      26.604  85.561  63.669  1.00 35.85           C  
-ATOM   2647  C   ASP B 205      26.033  85.077  65.003  1.00 35.21           C  
-ATOM   2648  O   ASP B 205      25.198  85.769  65.603  1.00 35.51           O  
-ATOM   2649  CB  ASP B 205      25.469  85.705  62.658  1.00 36.27           C  
-ATOM   2650  CG  ASP B 205      24.617  86.920  62.921  1.00 37.54           C  
-ATOM   2651  OD1 ASP B 205      25.199  88.008  63.132  1.00 40.82           O  
-ATOM   2652  OD2 ASP B 205      23.368  86.884  62.943  1.00 38.18           O  
-ATOM   2653  N   ILE B 206      26.462  83.902  65.464  1.00 33.83           N  
-ATOM   2654  CA  ILE B 206      25.996  83.370  66.745  1.00 32.41           C  
-ATOM   2655  C   ILE B 206      27.149  82.969  67.665  1.00 31.57           C  
-ATOM   2656  O   ILE B 206      28.261  82.700  67.205  1.00 31.21           O  
-ATOM   2657  CB  ILE B 206      24.975  82.201  66.555  1.00 32.83           C  
-ATOM   2658  CG1 ILE B 206      25.586  81.035  65.762  1.00 32.55           C  
-ATOM   2659  CG2 ILE B 206      23.696  82.711  65.880  1.00 32.58           C  
-ATOM   2660  CD1 ILE B 206      24.654  79.828  65.574  1.00 32.93           C  
-ATOM   2661  N   THR B 207      26.861  82.951  68.965  1.00 30.18           N  
-ATOM   2662  CA  THR B 207      27.847  82.739  70.018  1.00 29.45           C  
-ATOM   2663  C   THR B 207      27.350  81.685  70.999  1.00 29.09           C  
-ATOM   2664  O   THR B 207      26.174  81.332  70.999  1.00 28.48           O  
-ATOM   2665  CB  THR B 207      28.074  84.035  70.826  1.00 29.22           C  
-ATOM   2666  OG1 THR B 207      26.818  84.490  71.358  1.00 28.00           O  
-ATOM   2667  CG2 THR B 207      28.548  85.178  69.930  1.00 29.39           C  
-ATOM   2668  N   ASN B 208      28.253  81.224  71.856  1.00 29.09           N  
-ATOM   2669  CA  ASN B 208      27.913  80.287  72.915  1.00 29.47           C  
-ATOM   2670  C   ASN B 208      26.799  80.822  73.808  1.00 29.66           C  
-ATOM   2671  O   ASN B 208      25.943  80.063  74.283  1.00 29.75           O  
-ATOM   2672  CB  ASN B 208      29.159  79.963  73.741  1.00 29.47           C  
-ATOM   2673  CG  ASN B 208      30.142  79.085  72.989  1.00 30.08           C  
-ATOM   2674  OD1 ASN B 208      29.747  78.178  72.261  1.00 31.85           O  
-ATOM   2675  ND2 ASN B 208      31.426  79.358  73.155  1.00 31.98           N  
-ATOM   2676  N   SER B 209      26.811  82.139  74.000  1.00 29.62           N  
-ATOM   2677  CA  SER B 209      25.849  82.833  74.837  1.00 29.88           C  
-ATOM   2678  C   SER B 209      24.446  82.831  74.234  1.00 29.46           C  
-ATOM   2679  O   SER B 209      23.468  82.609  74.947  1.00 29.50           O  
-ATOM   2680  CB  SER B 209      26.332  84.260  75.122  1.00 30.22           C  
-ATOM   2681  OG  SER B 209      25.351  84.982  75.845  1.00 33.04           O  
-ATOM   2682  N   MET B 210      24.337  83.067  72.928  1.00 29.26           N  
-ATOM   2683  CA  MET B 210      23.050  82.914  72.236  1.00 28.91           C  
-ATOM   2684  C   MET B 210      22.541  81.466  72.266  1.00 28.06           C  
-ATOM   2685  O   MET B 210      21.346  81.227  72.424  1.00 27.84           O  
-ATOM   2686  CB  MET B 210      23.149  83.391  70.794  1.00 29.55           C  
-ATOM   2687  CG  MET B 210      23.502  84.868  70.643  1.00 31.97           C  
-ATOM   2688  SD  MET B 210      23.733  85.264  68.905  1.00 36.53           S  
-ATOM   2689  CE  MET B 210      22.143  84.935  68.366  1.00 34.40           C  
-ATOM   2690  N   ARG B 211      23.451  80.506  72.108  1.00 27.59           N  
-ATOM   2691  CA  ARG B 211      23.111  79.087  72.232  1.00 27.08           C  
-ATOM   2692  C   ARG B 211      22.559  78.809  73.631  1.00 26.76           C  
-ATOM   2693  O   ARG B 211      21.529  78.160  73.774  1.00 26.90           O  
-ATOM   2694  CB  ARG B 211      24.333  78.212  71.950  1.00 26.89           C  
-ATOM   2695  CG  ARG B 211      24.066  76.700  71.948  1.00 26.07           C  
-ATOM   2696  CD  ARG B 211      25.335  75.851  71.915  1.00 23.97           C  
-ATOM   2697  NE  ARG B 211      25.073  74.430  72.166  1.00 22.46           N  
-ATOM   2698  CZ  ARG B 211      24.855  73.899  73.372  1.00 22.55           C  
-ATOM   2699  NH1 ARG B 211      24.864  74.663  74.465  1.00 22.06           N  
-ATOM   2700  NH2 ARG B 211      24.633  72.593  73.491  1.00 20.55           N  
-ATOM   2701  N   ALA B 212      23.243  79.334  74.649  1.00 26.49           N  
-ATOM   2702  CA  ALA B 212      22.812  79.221  76.049  1.00 26.30           C  
-ATOM   2703  C   ALA B 212      21.383  79.701  76.225  1.00 26.29           C  
-ATOM   2704  O   ALA B 212      20.570  79.025  76.857  1.00 26.50           O  
-ATOM   2705  CB  ALA B 212      23.747  79.999  76.958  1.00 26.21           C  
-ATOM   2706  N   ILE B 213      21.066  80.848  75.624  1.00 26.10           N  
-ATOM   2707  CA  ILE B 213      19.718  81.397  75.680  1.00 25.84           C  
-ATOM   2708  C   ILE B 213      18.689  80.441  75.052  1.00 25.74           C  
-ATOM   2709  O   ILE B 213      17.640  80.160  75.656  1.00 25.81           O  
-ATOM   2710  CB  ILE B 213      19.678  82.818  75.034  1.00 26.12           C  
-ATOM   2711  CG1 ILE B 213      20.390  83.827  75.944  1.00 26.82           C  
-ATOM   2712  CG2 ILE B 213      18.235  83.264  74.757  1.00 25.22           C  
-ATOM   2713  CD1 ILE B 213      20.798  85.144  75.253  1.00 26.58           C  
-ATOM   2714  N   LEU B 214      19.004  79.934  73.856  1.00 25.26           N  
-ATOM   2715  CA  LEU B 214      18.147  78.974  73.155  1.00 24.61           C  
-ATOM   2716  C   LEU B 214      17.857  77.724  73.994  1.00 24.32           C  
-ATOM   2717  O   LEU B 214      16.706  77.364  74.191  1.00 24.07           O  
-ATOM   2718  CB  LEU B 214      18.761  78.567  71.801  1.00 24.34           C  
-ATOM   2719  CG  LEU B 214      17.998  77.518  70.976  1.00 22.92           C  
-ATOM   2720  CD1 LEU B 214      16.615  78.031  70.612  1.00 23.57           C  
-ATOM   2721  CD2 LEU B 214      18.756  77.103  69.712  1.00 19.91           C  
-ATOM   2722  N   VAL B 215      18.906  77.071  74.483  1.00 24.44           N  
-ATOM   2723  CA  VAL B 215      18.731  75.876  75.302  1.00 24.83           C  
-ATOM   2724  C   VAL B 215      17.892  76.179  76.557  1.00 24.72           C  
-ATOM   2725  O   VAL B 215      17.002  75.407  76.919  1.00 24.53           O  
-ATOM   2726  CB  VAL B 215      20.083  75.221  75.671  1.00 24.78           C  
-ATOM   2727  CG1 VAL B 215      19.857  73.969  76.492  1.00 25.22           C  
-ATOM   2728  CG2 VAL B 215      20.860  74.873  74.415  1.00 25.36           C  
-ATOM   2729  N   ASP B 216      18.152  77.317  77.193  1.00 24.92           N  
-ATOM   2730  CA  ASP B 216      17.368  77.697  78.369  1.00 25.45           C  
-ATOM   2731  C   ASP B 216      15.871  77.816  78.053  1.00 24.76           C  
-ATOM   2732  O   ASP B 216      15.037  77.333  78.808  1.00 25.13           O  
-ATOM   2733  CB  ASP B 216      17.893  78.992  78.994  1.00 25.42           C  
-ATOM   2734  CG  ASP B 216      17.267  79.271  80.342  1.00 26.96           C  
-ATOM   2735  OD1 ASP B 216      16.255  80.002  80.391  1.00 27.11           O  
-ATOM   2736  OD2 ASP B 216      17.712  78.781  81.406  1.00 29.20           O  
-ATOM   2737  N   TRP B 217      15.547  78.462  76.938  1.00 24.57           N  
-ATOM   2738  CA  TRP B 217      14.174  78.511  76.426  1.00 24.19           C  
-ATOM   2739  C   TRP B 217      13.603  77.108  76.156  1.00 24.27           C  
-ATOM   2740  O   TRP B 217      12.450  76.827  76.497  1.00 24.37           O  
-ATOM   2741  CB  TRP B 217      14.126  79.356  75.150  1.00 24.14           C  
-ATOM   2742  CG  TRP B 217      12.773  79.429  74.522  1.00 24.54           C  
-ATOM   2743  CD1 TRP B 217      11.669  80.062  75.020  1.00 24.24           C  
-ATOM   2744  CD2 TRP B 217      12.367  78.840  73.276  1.00 25.20           C  
-ATOM   2745  NE1 TRP B 217      10.609  79.910  74.160  1.00 24.65           N  
-ATOM   2746  CE2 TRP B 217      11.005  79.163  73.083  1.00 25.16           C  
-ATOM   2747  CE3 TRP B 217      13.016  78.069  72.304  1.00 24.57           C  
-ATOM   2748  CZ2 TRP B 217      10.282  78.744  71.961  1.00 26.27           C  
-ATOM   2749  CZ3 TRP B 217      12.302  77.655  71.188  1.00 25.29           C  
-ATOM   2750  CH2 TRP B 217      10.949  77.997  71.023  1.00 26.20           C  
-ATOM   2751  N   LEU B 218      14.407  76.232  75.549  1.00 23.65           N  
-ATOM   2752  CA  LEU B 218      13.975  74.849  75.301  1.00 23.66           C  
-ATOM   2753  C   LEU B 218      13.608  74.115  76.586  1.00 23.25           C  
-ATOM   2754  O   LEU B 218      12.643  73.353  76.603  1.00 22.67           O  
-ATOM   2755  CB  LEU B 218      15.029  74.059  74.510  1.00 23.74           C  
-ATOM   2756  CG  LEU B 218      15.245  74.526  73.065  1.00 24.33           C  
-ATOM   2757  CD1 LEU B 218      16.361  73.711  72.454  1.00 24.22           C  
-ATOM   2758  CD2 LEU B 218      13.958  74.385  72.245  1.00 25.28           C  
-ATOM   2759  N   VAL B 219      14.381  74.343  77.649  1.00 23.21           N  
-ATOM   2760  CA  VAL B 219      14.028  73.834  78.980  1.00 23.87           C  
-ATOM   2761  C   VAL B 219      12.603  74.265  79.383  1.00 24.80           C  
-ATOM   2762  O   VAL B 219      11.813  73.438  79.840  1.00 24.55           O  
-ATOM   2763  CB  VAL B 219      15.069  74.238  80.053  1.00 23.58           C  
-ATOM   2764  CG1 VAL B 219      14.656  73.754  81.460  1.00 23.84           C  
-ATOM   2765  CG2 VAL B 219      16.466  73.688  79.697  1.00 22.10           C  
-ATOM   2766  N   GLU B 220      12.288  75.544  79.169  1.00 25.92           N  
-ATOM   2767  CA  GLU B 220      10.974  76.120  79.462  1.00 27.22           C  
-ATOM   2768  C   GLU B 220       9.876  75.490  78.617  1.00 27.05           C  
-ATOM   2769  O   GLU B 220       8.796  75.171  79.124  1.00 26.74           O  
-ATOM   2770  CB  GLU B 220      10.972  77.624  79.189  1.00 27.71           C  
-ATOM   2771  CG  GLU B 220      12.002  78.433  79.943  1.00 32.04           C  
-ATOM   2772  CD  GLU B 220      11.702  79.916  79.871  1.00 37.13           C  
-ATOM   2773  OE1 GLU B 220      10.787  80.368  80.593  1.00 41.03           O  
-ATOM   2774  OE2 GLU B 220      12.363  80.626  79.081  1.00 39.46           O  
-ATOM   2775  N   VAL B 221      10.148  75.338  77.319  1.00 27.39           N  
-ATOM   2776  CA  VAL B 221       9.204  74.679  76.412  1.00 27.62           C  
-ATOM   2777  C   VAL B 221       8.901  73.279  76.924  1.00 27.98           C  
-ATOM   2778  O   VAL B 221       7.736  72.882  76.997  1.00 27.45           O  
-ATOM   2779  CB  VAL B 221       9.750  74.577  74.976  1.00 27.84           C  
-ATOM   2780  CG1 VAL B 221       8.815  73.739  74.102  1.00 27.07           C  
-ATOM   2781  CG2 VAL B 221       9.961  75.956  74.388  1.00 27.39           C  
-ATOM   2782  N   GLY B 222       9.960  72.546  77.277  1.00 28.37           N  
-ATOM   2783  CA  GLY B 222       9.828  71.215  77.839  1.00 29.58           C  
-ATOM   2784  C   GLY B 222       8.941  71.180  79.076  1.00 30.62           C  
-ATOM   2785  O   GLY B 222       8.126  70.269  79.227  1.00 30.51           O  
-ATOM   2786  N   GLU B 223       9.095  72.176  79.948  1.00 31.51           N  
-ATOM   2787  CA  GLU B 223       8.265  72.308  81.145  1.00 33.26           C  
-ATOM   2788  C   GLU B 223       6.830  72.720  80.825  1.00 33.27           C  
-ATOM   2789  O   GLU B 223       5.890  72.213  81.429  1.00 33.32           O  
-ATOM   2790  CB  GLU B 223       8.874  73.318  82.108  1.00 33.63           C  
-ATOM   2791  CG  GLU B 223      10.122  72.811  82.797  1.00 36.82           C  
-ATOM   2792  CD  GLU B 223       9.781  71.851  83.906  1.00 41.61           C  
-ATOM   2793  OE1 GLU B 223       9.380  72.327  85.002  1.00 43.81           O  
-ATOM   2794  OE2 GLU B 223       9.898  70.623  83.670  1.00 43.74           O  
-ATOM   2795  N   GLU B 224       6.669  73.633  79.872  1.00 33.61           N  
-ATOM   2796  CA  GLU B 224       5.344  74.089  79.457  1.00 34.00           C  
-ATOM   2797  C   GLU B 224       4.505  72.931  78.933  1.00 33.34           C  
-ATOM   2798  O   GLU B 224       3.308  72.845  79.214  1.00 33.31           O  
-ATOM   2799  CB  GLU B 224       5.463  75.198  78.406  1.00 34.54           C  
-ATOM   2800  CG  GLU B 224       4.154  75.660  77.780  1.00 37.51           C  
-ATOM   2801  CD  GLU B 224       3.281  76.452  78.736  1.00 41.52           C  
-ATOM   2802  OE1 GLU B 224       3.752  77.488  79.270  1.00 44.45           O  
-ATOM   2803  OE2 GLU B 224       2.116  76.042  78.948  1.00 42.36           O  
-ATOM   2804  N   TYR B 225       5.142  72.033  78.190  1.00 32.72           N  
-ATOM   2805  CA  TYR B 225       4.427  70.941  77.530  1.00 32.05           C  
-ATOM   2806  C   TYR B 225       4.649  69.604  78.211  1.00 31.22           C  
-ATOM   2807  O   TYR B 225       4.199  68.576  77.722  1.00 31.03           O  
-ATOM   2808  CB  TYR B 225       4.773  70.891  76.035  1.00 32.23           C  
-ATOM   2809  CG  TYR B 225       4.146  72.047  75.301  1.00 33.96           C  
-ATOM   2810  CD1 TYR B 225       4.882  73.186  75.023  1.00 35.85           C  
-ATOM   2811  CD2 TYR B 225       2.798  72.022  74.933  1.00 34.47           C  
-ATOM   2812  CE1 TYR B 225       4.314  74.259  74.379  1.00 37.71           C  
-ATOM   2813  CE2 TYR B 225       2.220  73.093  74.294  1.00 36.46           C  
-ATOM   2814  CZ  TYR B 225       2.987  74.215  74.019  1.00 37.97           C  
-ATOM   2815  OH  TYR B 225       2.438  75.307  73.382  1.00 40.30           O  
-ATOM   2816  N   LYS B 226       5.327  69.640  79.357  1.00 30.80           N  
-ATOM   2817  CA  LYS B 226       5.603  68.451  80.154  1.00 30.08           C  
-ATOM   2818  C   LYS B 226       6.250  67.347  79.301  1.00 29.44           C  
-ATOM   2819  O   LYS B 226       5.785  66.201  79.260  1.00 28.93           O  
-ATOM   2820  CB  LYS B 226       4.325  67.983  80.868  1.00 30.69           C  
-ATOM   2821  CG  LYS B 226       3.934  68.885  82.046  1.00 32.20           C  
-ATOM   2822  CD  LYS B 226       2.548  68.563  82.572  1.00 37.04           C  
-ATOM   2823  CE  LYS B 226       2.161  69.488  83.735  1.00 39.23           C  
-ATOM   2824  NZ  LYS B 226       0.694  69.428  84.049  1.00 41.69           N  
-ATOM   2825  N   LEU B 227       7.324  67.721  78.608  1.00 28.30           N  
-ATOM   2826  CA  LEU B 227       8.062  66.798  77.754  1.00 27.39           C  
-ATOM   2827  C   LEU B 227       9.110  66.055  78.575  1.00 26.87           C  
-ATOM   2828  O   LEU B 227       9.539  66.535  79.622  1.00 26.66           O  
-ATOM   2829  CB  LEU B 227       8.723  67.544  76.583  1.00 27.23           C  
-ATOM   2830  CG  LEU B 227       7.817  68.442  75.725  1.00 26.66           C  
-ATOM   2831  CD1 LEU B 227       8.603  69.158  74.642  1.00 26.07           C  
-ATOM   2832  CD2 LEU B 227       6.671  67.653  75.127  1.00 25.30           C  
-ATOM   2833  N   GLN B 228       9.498  64.877  78.101  1.00 26.15           N  
-ATOM   2834  CA  GLN B 228      10.560  64.094  78.727  1.00 25.96           C  
-ATOM   2835  C   GLN B 228      11.868  64.872  78.705  1.00 25.76           C  
-ATOM   2836  O   GLN B 228      12.082  65.689  77.818  1.00 25.87           O  
-ATOM   2837  CB  GLN B 228      10.744  62.780  77.970  1.00 26.01           C  
-ATOM   2838  CG  GLN B 228       9.558  61.828  78.057  1.00 26.27           C  
-ATOM   2839  CD  GLN B 228       9.261  61.419  79.475  1.00 28.02           C  
-ATOM   2840  OE1 GLN B 228      10.169  61.075  80.234  1.00 30.23           O  
-ATOM   2841  NE2 GLN B 228       7.995  61.477  79.849  1.00 30.79           N  
-ATOM   2842  N   ASN B 229      12.735  64.626  79.682  1.00 25.48           N  
-ATOM   2843  CA  ASN B 229      14.080  65.188  79.657  1.00 25.62           C  
-ATOM   2844  C   ASN B 229      14.868  64.689  78.448  1.00 24.99           C  
-ATOM   2845  O   ASN B 229      15.632  65.445  77.849  1.00 25.53           O  
-ATOM   2846  CB  ASN B 229      14.842  64.874  80.943  1.00 25.71           C  
-ATOM   2847  CG  ASN B 229      14.291  65.624  82.156  1.00 27.17           C  
-ATOM   2848  OD1 ASN B 229      13.502  66.565  82.029  1.00 29.31           O  
-ATOM   2849  ND2 ASN B 229      14.703  65.196  83.338  1.00 27.88           N  
-ATOM   2850  N   GLU B 230      14.660  63.423  78.097  1.00 23.99           N  
-ATOM   2851  CA  GLU B 230      15.260  62.820  76.914  1.00 23.37           C  
-ATOM   2852  C   GLU B 230      15.010  63.652  75.652  1.00 22.90           C  
-ATOM   2853  O   GLU B 230      15.928  63.873  74.859  1.00 22.62           O  
-ATOM   2854  CB  GLU B 230      14.750  61.386  76.739  1.00 23.36           C  
-ATOM   2855  CG  GLU B 230      15.299  60.632  75.531  1.00 23.16           C  
-ATOM   2856  CD  GLU B 230      16.806  60.412  75.566  1.00 24.23           C  
-ATOM   2857  OE1 GLU B 230      17.471  60.807  76.565  1.00 23.25           O  
-ATOM   2858  OE2 GLU B 230      17.325  59.847  74.567  1.00 24.27           O  
-ATOM   2859  N   THR B 231      13.771  64.124  75.495  1.00 22.16           N  
-ATOM   2860  CA  THR B 231      13.379  64.949  74.368  1.00 21.55           C  
-ATOM   2861  C   THR B 231      14.238  66.221  74.289  1.00 21.71           C  
-ATOM   2862  O   THR B 231      14.717  66.583  73.211  1.00 21.36           O  
-ATOM   2863  CB  THR B 231      11.883  65.282  74.455  1.00 21.98           C  
-ATOM   2864  OG1 THR B 231      11.137  64.062  74.585  1.00 20.86           O  
-ATOM   2865  CG2 THR B 231      11.375  65.869  73.129  1.00 20.44           C  
-ATOM   2866  N   LEU B 232      14.459  66.861  75.440  1.00 21.32           N  
-ATOM   2867  CA  LEU B 232      15.330  68.032  75.550  1.00 20.88           C  
-ATOM   2868  C   LEU B 232      16.766  67.704  75.128  1.00 20.13           C  
-ATOM   2869  O   LEU B 232      17.371  68.444  74.353  1.00 19.81           O  
-ATOM   2870  CB  LEU B 232      15.336  68.535  76.998  1.00 20.92           C  
-ATOM   2871  CG  LEU B 232      15.762  69.940  77.448  1.00 22.70           C  
-ATOM   2872  CD1 LEU B 232      16.619  69.868  78.727  1.00 22.72           C  
-ATOM   2873  CD2 LEU B 232      16.411  70.817  76.374  1.00 24.40           C  
-ATOM   2874  N   HIS B 233      17.312  66.610  75.661  1.00 19.10           N  
-ATOM   2875  CA  HIS B 233      18.676  66.181  75.317  1.00 18.39           C  
-ATOM   2876  C   HIS B 233      18.862  65.901  73.825  1.00 17.84           C  
-ATOM   2877  O   HIS B 233      19.874  66.289  73.251  1.00 17.52           O  
-ATOM   2878  CB  HIS B 233      19.101  64.966  76.141  1.00 18.13           C  
-ATOM   2879  CG  HIS B 233      19.551  65.308  77.525  1.00 18.05           C  
-ATOM   2880  ND1 HIS B 233      18.667  65.487  78.570  1.00 20.34           N  
-ATOM   2881  CD2 HIS B 233      20.785  65.514  78.038  1.00 15.77           C  
-ATOM   2882  CE1 HIS B 233      19.338  65.789  79.667  1.00 17.50           C  
-ATOM   2883  NE2 HIS B 233      20.625  65.815  79.371  1.00 18.63           N  
-ATOM   2884  N   LEU B 234      17.885  65.241  73.208  1.00 17.55           N  
-ATOM   2885  CA  LEU B 234      17.910  64.959  71.770  1.00 17.50           C  
-ATOM   2886  C   LEU B 234      17.897  66.230  70.944  1.00 17.96           C  
-ATOM   2887  O   LEU B 234      18.700  66.387  70.006  1.00 17.80           O  
-ATOM   2888  CB  LEU B 234      16.717  64.098  71.354  1.00 16.97           C  
-ATOM   2889  CG  LEU B 234      16.684  62.667  71.873  1.00 17.01           C  
-ATOM   2890  CD1 LEU B 234      15.320  62.045  71.591  1.00 16.20           C  
-ATOM   2891  CD2 LEU B 234      17.838  61.827  71.266  1.00 14.29           C  
-ATOM   2892  N   ALA B 235      16.979  67.128  71.291  1.00 18.18           N  
-ATOM   2893  CA  ALA B 235      16.826  68.381  70.567  1.00 18.77           C  
-ATOM   2894  C   ALA B 235      18.130  69.171  70.568  1.00 19.18           C  
-ATOM   2895  O   ALA B 235      18.552  69.688  69.521  1.00 19.53           O  
-ATOM   2896  CB  ALA B 235      15.687  69.200  71.154  1.00 19.25           C  
-ATOM   2897  N   VAL B 236      18.782  69.245  71.728  1.00 18.96           N  
-ATOM   2898  CA  VAL B 236      20.079  69.915  71.822  1.00 18.97           C  
-ATOM   2899  C   VAL B 236      21.122  69.216  70.938  1.00 18.85           C  
-ATOM   2900  O   VAL B 236      21.877  69.891  70.216  1.00 18.70           O  
-ATOM   2901  CB  VAL B 236      20.582  70.013  73.286  1.00 19.43           C  
-ATOM   2902  CG1 VAL B 236      22.007  70.583  73.323  1.00 19.09           C  
-ATOM   2903  CG2 VAL B 236      19.640  70.904  74.129  1.00 19.49           C  
-ATOM   2904  N   ASN B 237      21.162  67.878  70.982  1.00 18.24           N  
-ATOM   2905  CA  ASN B 237      22.061  67.128  70.101  1.00 18.36           C  
-ATOM   2906  C   ASN B 237      21.823  67.450  68.619  1.00 18.54           C  
-ATOM   2907  O   ASN B 237      22.788  67.616  67.864  1.00 18.43           O  
-ATOM   2908  CB  ASN B 237      21.994  65.615  70.334  1.00 17.98           C  
-ATOM   2909  CG  ASN B 237      22.696  64.825  69.225  1.00 18.44           C  
-ATOM   2910  OD1 ASN B 237      22.096  64.515  68.199  1.00 16.80           O  
-ATOM   2911  ND2 ASN B 237      23.976  64.521  69.424  1.00 17.49           N  
-ATOM   2912  N   TYR B 238      20.551  67.546  68.215  1.00 18.60           N  
-ATOM   2913  CA  TYR B 238      20.208  67.862  66.820  1.00 19.19           C  
-ATOM   2914  C   TYR B 238      20.651  69.269  66.431  1.00 19.92           C  
-ATOM   2915  O   TYR B 238      21.084  69.486  65.285  1.00 19.56           O  
-ATOM   2916  CB  TYR B 238      18.707  67.760  66.548  1.00 18.81           C  
-ATOM   2917  CG  TYR B 238      18.062  66.432  66.881  1.00 17.41           C  
-ATOM   2918  CD1 TYR B 238      18.806  65.271  67.000  1.00 15.41           C  
-ATOM   2919  CD2 TYR B 238      16.687  66.356  67.067  1.00 17.86           C  
-ATOM   2920  CE1 TYR B 238      18.199  64.060  67.320  1.00 16.34           C  
-ATOM   2921  CE2 TYR B 238      16.065  65.157  67.371  1.00 16.81           C  
-ATOM   2922  CZ  TYR B 238      16.824  64.021  67.508  1.00 16.28           C  
-ATOM   2923  OH  TYR B 238      16.195  62.850  67.824  1.00 16.40           O  
-ATOM   2924  N   ILE B 239      20.528  70.207  67.384  1.00 20.16           N  
-ATOM   2925  CA  ILE B 239      20.896  71.604  67.164  1.00 20.54           C  
-ATOM   2926  C   ILE B 239      22.401  71.734  66.975  1.00 20.44           C  
-ATOM   2927  O   ILE B 239      22.845  72.382  66.038  1.00 20.14           O  
-ATOM   2928  CB  ILE B 239      20.429  72.528  68.329  1.00 20.91           C  
-ATOM   2929  CG1 ILE B 239      18.913  72.669  68.343  1.00 21.16           C  
-ATOM   2930  CG2 ILE B 239      21.063  73.933  68.210  1.00 20.25           C  
-ATOM   2931  CD1 ILE B 239      18.390  73.249  69.630  1.00 22.34           C  
-ATOM   2932  N   ASP B 240      23.176  71.123  67.868  1.00 20.63           N  
-ATOM   2933  CA  ASP B 240      24.630  71.220  67.794  1.00 21.13           C  
-ATOM   2934  C   ASP B 240      25.202  70.559  66.531  1.00 20.99           C  
-ATOM   2935  O   ASP B 240      26.183  71.047  65.958  1.00 20.47           O  
-ATOM   2936  CB  ASP B 240      25.275  70.654  69.053  1.00 21.41           C  
-ATOM   2937  CG  ASP B 240      25.040  71.534  70.270  1.00 24.27           C  
-ATOM   2938  OD1 ASP B 240      24.809  72.757  70.103  1.00 27.30           O  
-ATOM   2939  OD2 ASP B 240      25.046  71.094  71.433  1.00 26.66           O  
-ATOM   2940  N   ARG B 241      24.580  69.459  66.112  1.00 20.49           N  
-ATOM   2941  CA  ARG B 241      24.965  68.780  64.886  1.00 20.91           C  
-ATOM   2942  C   ARG B 241      24.599  69.626  63.665  1.00 20.73           C  
-ATOM   2943  O   ARG B 241      25.404  69.767  62.761  1.00 20.50           O  
-ATOM   2944  CB  ARG B 241      24.328  67.396  64.792  1.00 20.31           C  
-ATOM   2945  CG  ARG B 241      25.019  66.346  65.651  1.00 21.08           C  
-ATOM   2946  CD  ARG B 241      24.140  65.118  65.956  1.00 22.20           C  
-ATOM   2947  NE  ARG B 241      23.845  64.378  64.737  1.00 21.83           N  
-ATOM   2948  CZ  ARG B 241      22.819  63.560  64.570  1.00 20.60           C  
-ATOM   2949  NH1 ARG B 241      21.960  63.338  65.562  1.00 17.75           N  
-ATOM   2950  NH2 ARG B 241      22.655  62.958  63.393  1.00 19.31           N  
-ATOM   2951  N   PHE B 242      23.392  70.182  63.655  1.00 21.01           N  
-ATOM   2952  CA  PHE B 242      22.947  71.035  62.558  1.00 21.65           C  
-ATOM   2953  C   PHE B 242      23.875  72.245  62.427  1.00 22.05           C  
-ATOM   2954  O   PHE B 242      24.296  72.604  61.317  1.00 21.94           O  
-ATOM   2955  CB  PHE B 242      21.511  71.494  62.792  1.00 21.48           C  
-ATOM   2956  CG  PHE B 242      20.941  72.303  61.668  1.00 22.03           C  
-ATOM   2957  CD1 PHE B 242      20.223  71.694  60.653  1.00 21.44           C  
-ATOM   2958  CD2 PHE B 242      21.110  73.689  61.629  1.00 23.22           C  
-ATOM   2959  CE1 PHE B 242      19.695  72.448  59.616  1.00 22.72           C  
-ATOM   2960  CE2 PHE B 242      20.584  74.439  60.592  1.00 21.57           C  
-ATOM   2961  CZ  PHE B 242      19.876  73.820  59.590  1.00 22.03           C  
-ATOM   2962  N   LEU B 243      24.212  72.846  63.568  1.00 22.07           N  
-ATOM   2963  CA  LEU B 243      25.075  74.020  63.597  1.00 22.97           C  
-ATOM   2964  C   LEU B 243      26.541  73.699  63.315  1.00 23.55           C  
-ATOM   2965  O   LEU B 243      27.327  74.604  63.085  1.00 23.76           O  
-ATOM   2966  CB  LEU B 243      24.948  74.771  64.928  1.00 22.89           C  
-ATOM   2967  CG  LEU B 243      23.612  75.417  65.267  1.00 23.59           C  
-ATOM   2968  CD1 LEU B 243      23.721  76.141  66.602  1.00 22.95           C  
-ATOM   2969  CD2 LEU B 243      23.142  76.361  64.147  1.00 24.79           C  
-ATOM   2970  N   SER B 244      26.901  72.417  63.336  1.00 24.33           N  
-ATOM   2971  CA  SER B 244      28.230  71.979  62.928  1.00 25.03           C  
-ATOM   2972  C   SER B 244      28.428  72.029  61.394  1.00 26.00           C  
-ATOM   2973  O   SER B 244      29.564  72.119  60.920  1.00 25.81           O  
-ATOM   2974  CB  SER B 244      28.512  70.567  63.459  1.00 24.96           C  
-ATOM   2975  OG  SER B 244      28.545  70.533  64.888  1.00 24.19           O  
-ATOM   2976  N   SER B 245      27.323  71.971  60.644  1.00 26.83           N  
-ATOM   2977  CA  SER B 245      27.324  71.967  59.170  1.00 28.01           C  
-ATOM   2978  C   SER B 245      26.808  73.274  58.588  1.00 28.03           C  
-ATOM   2979  O   SER B 245      27.200  73.668  57.493  1.00 28.60           O  
-ATOM   2980  CB  SER B 245      26.405  70.869  58.615  1.00 27.65           C  
-ATOM   2981  OG  SER B 245      26.284  69.767  59.501  1.00 31.11           O  
-ATOM   2982  N   MET B 246      25.901  73.924  59.307  1.00 27.79           N  
-ATOM   2983  CA  MET B 246      25.119  75.003  58.726  1.00 27.71           C  
-ATOM   2984  C   MET B 246      25.296  76.312  59.473  1.00 28.11           C  
-ATOM   2985  O   MET B 246      24.956  76.438  60.659  1.00 27.88           O  
-ATOM   2986  CB  MET B 246      23.635  74.632  58.674  1.00 27.34           C  
-ATOM   2987  CG  MET B 246      23.344  73.270  58.052  1.00 27.73           C  
-ATOM   2988  SD  MET B 246      23.536  73.271  56.242  1.00 29.13           S  
-ATOM   2989  CE  MET B 246      22.064  74.166  55.748  1.00 25.83           C  
-ATOM   2990  N   SER B 247      25.829  77.282  58.749  1.00 28.17           N  
-ATOM   2991  CA  SER B 247      25.908  78.649  59.203  1.00 28.79           C  
-ATOM   2992  C   SER B 247      24.480  79.191  59.325  1.00 28.59           C  
-ATOM   2993  O   SER B 247      23.667  79.013  58.414  1.00 28.70           O  
-ATOM   2994  CB  SER B 247      26.745  79.454  58.207  1.00 28.49           C  
-ATOM   2995  OG  SER B 247      26.701  80.823  58.522  1.00 31.56           O  
-ATOM   2996  N   VAL B 248      24.170  79.807  60.468  1.00 28.62           N  
-ATOM   2997  CA  VAL B 248      22.817  80.275  60.767  1.00 28.54           C  
-ATOM   2998  C   VAL B 248      22.819  81.703  61.326  1.00 29.16           C  
-ATOM   2999  O   VAL B 248      23.649  82.044  62.165  1.00 29.34           O  
-ATOM   3000  CB  VAL B 248      22.070  79.294  61.747  1.00 28.78           C  
-ATOM   3001  CG1 VAL B 248      20.650  79.766  62.044  1.00 27.68           C  
-ATOM   3002  CG2 VAL B 248      22.030  77.867  61.182  1.00 27.61           C  
-ATOM   3003  N   LEU B 249      21.889  82.535  60.859  1.00 29.79           N  
-ATOM   3004  CA  LEU B 249      21.766  83.907  61.370  1.00 30.51           C  
-ATOM   3005  C   LEU B 249      21.029  83.951  62.710  1.00 30.71           C  
-ATOM   3006  O   LEU B 249      20.141  83.133  62.968  1.00 30.62           O  
-ATOM   3007  CB  LEU B 249      21.067  84.824  60.356  1.00 30.43           C  
-ATOM   3008  CG  LEU B 249      21.784  85.221  59.054  1.00 31.58           C  
-ATOM   3009  CD1 LEU B 249      21.119  86.436  58.443  1.00 31.73           C  
-ATOM   3010  CD2 LEU B 249      23.281  85.471  59.242  1.00 32.08           C  
-ATOM   3011  N   ARG B 250      21.389  84.928  63.542  1.00 30.95           N  
-ATOM   3012  CA  ARG B 250      20.818  85.065  64.888  1.00 31.11           C  
-ATOM   3013  C   ARG B 250      19.292  85.035  64.929  1.00 30.56           C  
-ATOM   3014  O   ARG B 250      18.714  84.401  65.809  1.00 30.50           O  
-ATOM   3015  CB  ARG B 250      21.362  86.309  65.600  1.00 31.23           C  
-ATOM   3016  CG  ARG B 250      20.918  87.655  65.036  1.00 33.00           C  
-ATOM   3017  CD  ARG B 250      21.781  88.826  65.493  1.00 36.19           C  
-ATOM   3018  NE  ARG B 250      23.218  88.547  65.417  1.00 38.46           N  
-ATOM   3019  CZ  ARG B 250      24.144  89.209  66.101  1.00 40.64           C  
-ATOM   3020  NH1 ARG B 250      23.788  90.191  66.923  1.00 42.10           N  
-ATOM   3021  NH2 ARG B 250      25.429  88.892  65.970  1.00 40.78           N  
-ATOM   3022  N   GLY B 251      18.650  85.694  63.965  1.00 30.25           N  
-ATOM   3023  CA  GLY B 251      17.198  85.721  63.878  1.00 29.66           C  
-ATOM   3024  C   GLY B 251      16.561  84.418  63.417  1.00 29.73           C  
-ATOM   3025  O   GLY B 251      15.335  84.287  63.430  1.00 29.45           O  
-ATOM   3026  N   LYS B 252      17.388  83.450  63.019  1.00 29.64           N  
-ATOM   3027  CA  LYS B 252      16.892  82.137  62.601  1.00 29.55           C  
-ATOM   3028  C   LYS B 252      17.228  81.018  63.600  1.00 29.52           C  
-ATOM   3029  O   LYS B 252      16.726  79.900  63.464  1.00 29.45           O  
-ATOM   3030  CB  LYS B 252      17.426  81.782  61.202  1.00 29.76           C  
-ATOM   3031  CG  LYS B 252      16.820  82.610  60.054  1.00 30.32           C  
-ATOM   3032  CD  LYS B 252      15.303  82.465  59.996  1.00 31.72           C  
-ATOM   3033  CE  LYS B 252      14.756  82.850  58.630  1.00 33.03           C  
-ATOM   3034  NZ  LYS B 252      14.669  84.329  58.482  1.00 33.67           N  
-ATOM   3035  N   LEU B 253      18.072  81.319  64.593  1.00 29.26           N  
-ATOM   3036  CA  LEU B 253      18.498  80.315  65.573  1.00 29.07           C  
-ATOM   3037  C   LEU B 253      17.328  79.654  66.284  1.00 28.59           C  
-ATOM   3038  O   LEU B 253      17.325  78.432  66.483  1.00 28.60           O  
-ATOM   3039  CB  LEU B 253      19.477  80.883  66.605  1.00 29.27           C  
-ATOM   3040  CG  LEU B 253      20.107  79.855  67.571  1.00 29.54           C  
-ATOM   3041  CD1 LEU B 253      20.913  78.793  66.834  1.00 29.03           C  
-ATOM   3042  CD2 LEU B 253      20.978  80.523  68.645  1.00 30.27           C  
-ATOM   3043  N   GLN B 254      16.331  80.457  66.638  1.00 27.86           N  
-ATOM   3044  CA  GLN B 254      15.171  79.949  67.345  1.00 27.77           C  
-ATOM   3045  C   GLN B 254      14.313  79.034  66.470  1.00 27.13           C  
-ATOM   3046  O   GLN B 254      13.675  78.105  66.984  1.00 27.50           O  
-ATOM   3047  CB  GLN B 254      14.336  81.088  67.934  1.00 27.85           C  
-ATOM   3048  CG  GLN B 254      13.533  80.679  69.168  1.00 28.93           C  
-ATOM   3049  CD  GLN B 254      12.430  81.673  69.538  1.00 30.50           C  
-ATOM   3050  OE1 GLN B 254      11.597  81.389  70.408  1.00 31.38           O  
-ATOM   3051  NE2 GLN B 254      12.426  82.829  68.888  1.00 30.04           N  
-ATOM   3052  N   LEU B 255      14.301  79.298  65.164  1.00 26.14           N  
-ATOM   3053  CA  LEU B 255      13.606  78.447  64.195  1.00 25.35           C  
-ATOM   3054  C   LEU B 255      14.252  77.068  64.122  1.00 24.80           C  
-ATOM   3055  O   LEU B 255      13.549  76.057  64.098  1.00 24.66           O  
-ATOM   3056  CB  LEU B 255      13.579  79.103  62.801  1.00 25.18           C  
-ATOM   3057  CG  LEU B 255      12.858  78.414  61.637  1.00 24.99           C  
-ATOM   3058  CD1 LEU B 255      11.392  78.171  61.965  1.00 24.45           C  
-ATOM   3059  CD2 LEU B 255      12.983  79.263  60.358  1.00 24.81           C  
-ATOM   3060  N   VAL B 256      15.584  77.040  64.094  1.00 24.53           N  
-ATOM   3061  CA  VAL B 256      16.346  75.785  64.145  1.00 24.16           C  
-ATOM   3062  C   VAL B 256      15.965  75.033  65.423  1.00 23.88           C  
-ATOM   3063  O   VAL B 256      15.526  73.880  65.368  1.00 23.91           O  
-ATOM   3064  CB  VAL B 256      17.873  76.038  64.083  1.00 23.98           C  
-ATOM   3065  CG1 VAL B 256      18.667  74.767  64.371  1.00 23.59           C  
-ATOM   3066  CG2 VAL B 256      18.272  76.617  62.730  1.00 24.70           C  
-ATOM   3067  N   GLY B 257      16.083  75.720  66.561  1.00 23.92           N  
-ATOM   3068  CA  GLY B 257      15.704  75.178  67.856  1.00 23.46           C  
-ATOM   3069  C   GLY B 257      14.299  74.611  67.900  1.00 23.30           C  
-ATOM   3070  O   GLY B 257      14.083  73.509  68.407  1.00 23.31           O  
-ATOM   3071  N   THR B 258      13.337  75.350  67.354  1.00 23.40           N  
-ATOM   3072  CA  THR B 258      11.943  74.900  67.355  1.00 23.39           C  
-ATOM   3073  C   THR B 258      11.730  73.621  66.534  1.00 23.00           C  
-ATOM   3074  O   THR B 258      10.991  72.733  66.955  1.00 23.06           O  
-ATOM   3075  CB  THR B 258      11.008  76.024  66.853  1.00 23.81           C  
-ATOM   3076  OG1 THR B 258      11.185  77.186  67.668  1.00 24.86           O  
-ATOM   3077  CG2 THR B 258       9.556  75.660  67.088  1.00 23.40           C  
-ATOM   3078  N   ALA B 259      12.363  73.541  65.362  1.00 22.46           N  
-ATOM   3079  CA  ALA B 259      12.230  72.367  64.495  1.00 22.09           C  
-ATOM   3080  C   ALA B 259      12.866  71.136  65.152  1.00 21.72           C  
-ATOM   3081  O   ALA B 259      12.312  70.043  65.106  1.00 21.89           O  
-ATOM   3082  CB  ALA B 259      12.871  72.637  63.139  1.00 21.85           C  
-ATOM   3083  N   ALA B 260      14.027  71.341  65.773  1.00 21.62           N  
-ATOM   3084  CA  ALA B 260      14.735  70.287  66.485  1.00 21.35           C  
-ATOM   3085  C   ALA B 260      13.876  69.724  67.612  1.00 21.35           C  
-ATOM   3086  O   ALA B 260      13.829  68.511  67.810  1.00 20.97           O  
-ATOM   3087  CB  ALA B 260      16.062  70.800  67.019  1.00 20.94           C  
-ATOM   3088  N   MET B 261      13.177  70.606  68.323  1.00 21.78           N  
-ATOM   3089  CA  MET B 261      12.348  70.192  69.457  1.00 22.30           C  
-ATOM   3090  C   MET B 261      11.089  69.480  68.958  1.00 22.41           C  
-ATOM   3091  O   MET B 261      10.601  68.546  69.602  1.00 22.62           O  
-ATOM   3092  CB  MET B 261      12.008  71.384  70.358  1.00 22.46           C  
-ATOM   3093  CG  MET B 261      11.465  71.011  71.750  1.00 25.06           C  
-ATOM   3094  SD  MET B 261      12.721  70.345  72.861  1.00 28.84           S  
-ATOM   3095  CE  MET B 261      11.968  70.644  74.522  1.00 30.27           C  
-ATOM   3096  N   LEU B 262      10.588  69.903  67.798  1.00 22.00           N  
-ATOM   3097  CA  LEU B 262       9.510  69.189  67.136  1.00 21.92           C  
-ATOM   3098  C   LEU B 262       9.959  67.778  66.736  1.00 21.61           C  
-ATOM   3099  O   LEU B 262       9.267  66.811  67.026  1.00 21.70           O  
-ATOM   3100  CB  LEU B 262       9.001  69.962  65.908  1.00 22.10           C  
-ATOM   3101  CG  LEU B 262       7.956  69.262  65.020  1.00 22.28           C  
-ATOM   3102  CD1 LEU B 262       6.662  68.910  65.779  1.00 21.66           C  
-ATOM   3103  CD2 LEU B 262       7.643  70.120  63.810  1.00 22.93           C  
-ATOM   3104  N   LEU B 263      11.116  67.676  66.076  1.00 20.75           N  
-ATOM   3105  CA  LEU B 263      11.681  66.382  65.686  1.00 19.81           C  
-ATOM   3106  C   LEU B 263      11.950  65.499  66.894  1.00 19.64           C  
-ATOM   3107  O   LEU B 263      11.581  64.326  66.902  1.00 19.96           O  
-ATOM   3108  CB  LEU B 263      12.976  66.567  64.876  1.00 19.19           C  
-ATOM   3109  CG  LEU B 263      12.766  67.047  63.442  1.00 18.31           C  
-ATOM   3110  CD1 LEU B 263      14.090  67.372  62.772  1.00 18.36           C  
-ATOM   3111  CD2 LEU B 263      12.033  65.980  62.690  1.00 17.87           C  
-ATOM   3112  N   ALA B 264      12.597  66.055  67.915  1.00 19.44           N  
-ATOM   3113  CA  ALA B 264      12.804  65.309  69.153  1.00 19.29           C  
-ATOM   3114  C   ALA B 264      11.488  64.773  69.719  1.00 18.81           C  
-ATOM   3115  O   ALA B 264      11.418  63.615  70.106  1.00 18.45           O  
-ATOM   3116  CB  ALA B 264      13.540  66.159  70.191  1.00 19.21           C  
-ATOM   3117  N   SER B 265      10.450  65.611  69.747  1.00 18.85           N  
-ATOM   3118  CA  SER B 265       9.157  65.218  70.306  1.00 19.20           C  
-ATOM   3119  C   SER B 265       8.501  64.089  69.507  1.00 19.25           C  
-ATOM   3120  O   SER B 265       8.049  63.109  70.094  1.00 19.09           O  
-ATOM   3121  CB  SER B 265       8.206  66.411  70.403  1.00 19.27           C  
-ATOM   3122  OG  SER B 265       8.785  67.462  71.140  1.00 21.64           O  
-ATOM   3123  N   LYS B 266       8.456  64.223  68.178  1.00 19.12           N  
-ATOM   3124  CA  LYS B 266       7.921  63.159  67.328  1.00 19.55           C  
-ATOM   3125  C   LYS B 266       8.690  61.846  67.529  1.00 19.44           C  
-ATOM   3126  O   LYS B 266       8.091  60.773  67.564  1.00 19.56           O  
-ATOM   3127  CB  LYS B 266       7.971  63.563  65.848  1.00 20.25           C  
-ATOM   3128  CG  LYS B 266       6.902  64.570  65.415  1.00 20.63           C  
-ATOM   3129  CD  LYS B 266       7.109  64.979  63.964  1.00 20.59           C  
-ATOM   3130  CE  LYS B 266       5.958  65.823  63.461  1.00 22.83           C  
-ATOM   3131  NZ  LYS B 266       6.179  66.240  62.047  1.00 22.77           N  
-ATOM   3132  N   PHE B 267      10.012  61.932  67.662  1.00 18.87           N  
-ATOM   3133  CA  PHE B 267      10.819  60.733  67.858  1.00 18.88           C  
-ATOM   3134  C   PHE B 267      10.601  60.106  69.252  1.00 18.88           C  
-ATOM   3135  O   PHE B 267      10.437  58.889  69.370  1.00 19.08           O  
-ATOM   3136  CB  PHE B 267      12.309  61.030  67.608  1.00 18.25           C  
-ATOM   3137  CG  PHE B 267      13.215  59.843  67.850  1.00 18.75           C  
-ATOM   3138  CD1 PHE B 267      13.579  58.999  66.792  1.00 15.74           C  
-ATOM   3139  CD2 PHE B 267      13.696  59.564  69.136  1.00 16.76           C  
-ATOM   3140  CE1 PHE B 267      14.395  57.910  67.004  1.00 17.61           C  
-ATOM   3141  CE2 PHE B 267      14.526  58.461  69.371  1.00 17.91           C  
-ATOM   3142  CZ  PHE B 267      14.877  57.627  68.304  1.00 18.63           C  
-ATOM   3143  N   GLU B 268      10.586  60.943  70.289  1.00 18.73           N  
-ATOM   3144  CA  GLU B 268      10.660  60.467  71.679  1.00 18.77           C  
-ATOM   3145  C   GLU B 268       9.349  60.392  72.476  1.00 18.78           C  
-ATOM   3146  O   GLU B 268       9.205  59.523  73.338  1.00 18.23           O  
-ATOM   3147  CB  GLU B 268      11.701  61.279  72.459  1.00 18.46           C  
-ATOM   3148  CG  GLU B 268      12.076  60.700  73.817  1.00 18.67           C  
-ATOM   3149  CD  GLU B 268      12.635  59.284  73.742  1.00 20.67           C  
-ATOM   3150  OE1 GLU B 268      13.390  58.942  72.785  1.00 21.61           O  
-ATOM   3151  OE2 GLU B 268      12.332  58.505  74.662  1.00 19.30           O  
-ATOM   3152  N   GLU B 269       8.405  61.289  72.191  1.00 19.29           N  
-ATOM   3153  CA  GLU B 269       7.188  61.422  73.003  1.00 19.78           C  
-ATOM   3154  C   GLU B 269       6.034  60.505  72.600  1.00 20.21           C  
-ATOM   3155  O   GLU B 269       5.829  60.230  71.421  1.00 19.89           O  
-ATOM   3156  CB  GLU B 269       6.686  62.868  72.980  1.00 19.65           C  
-ATOM   3157  CG  GLU B 269       7.666  63.892  73.525  1.00 20.45           C  
-ATOM   3158  CD  GLU B 269       7.754  63.868  75.034  1.00 22.92           C  
-ATOM   3159  OE1 GLU B 269       6.791  63.411  75.688  1.00 25.24           O  
-ATOM   3160  OE2 GLU B 269       8.792  64.306  75.569  1.00 24.16           O  
-ATOM   3161  N   ILE B 270       5.265  60.058  73.590  1.00 20.85           N  
-ATOM   3162  CA  ILE B 270       4.040  59.303  73.328  1.00 21.96           C  
-ATOM   3163  C   ILE B 270       3.066  60.224  72.603  1.00 23.28           C  
-ATOM   3164  O   ILE B 270       2.506  59.858  71.566  1.00 23.76           O  
-ATOM   3165  CB  ILE B 270       3.418  58.760  74.651  1.00 21.86           C  
-ATOM   3166  CG1 ILE B 270       4.377  57.777  75.345  1.00 20.07           C  
-ATOM   3167  CG2 ILE B 270       2.050  58.129  74.384  1.00 21.52           C  
-ATOM   3168  CD1 ILE B 270       3.975  57.399  76.779  1.00 18.34           C  
-ATOM   3169  N   TYR B 271       2.910  61.433  73.141  1.00 24.50           N  
-ATOM   3170  CA  TYR B 271       2.010  62.441  72.603  1.00 26.17           C  
-ATOM   3171  C   TYR B 271       2.783  63.736  72.342  1.00 26.70           C  
-ATOM   3172  O   TYR B 271       2.822  64.613  73.209  1.00 26.87           O  
-ATOM   3173  CB  TYR B 271       0.870  62.720  73.599  1.00 26.78           C  
-ATOM   3174  CG  TYR B 271      -0.117  61.583  73.793  1.00 28.51           C  
-ATOM   3175  CD1 TYR B 271      -0.838  61.070  72.720  1.00 30.74           C  
-ATOM   3176  CD2 TYR B 271      -0.343  61.033  75.059  1.00 30.52           C  
-ATOM   3177  CE1 TYR B 271      -1.752  60.035  72.895  1.00 32.65           C  
-ATOM   3178  CE2 TYR B 271      -1.254  59.989  75.242  1.00 30.74           C  
-ATOM   3179  CZ  TYR B 271      -1.953  59.502  74.157  1.00 33.21           C  
-ATOM   3180  OH  TYR B 271      -2.865  58.474  74.317  1.00 36.51           O  
-ATOM   3181  N   PRO B 272       3.419  63.858  71.175  1.00 27.45           N  
-ATOM   3182  CA  PRO B 272       4.112  65.104  70.829  1.00 28.44           C  
-ATOM   3183  C   PRO B 272       3.114  66.251  70.680  1.00 29.33           C  
-ATOM   3184  O   PRO B 272       1.989  66.007  70.233  1.00 29.91           O  
-ATOM   3185  CB  PRO B 272       4.784  64.790  69.483  1.00 28.05           C  
-ATOM   3186  CG  PRO B 272       4.097  63.585  68.958  1.00 28.03           C  
-ATOM   3187  CD  PRO B 272       3.555  62.831  70.125  1.00 27.33           C  
-ATOM   3188  N   PRO B 273       3.497  67.465  71.069  1.00 29.92           N  
-ATOM   3189  CA  PRO B 273       2.667  68.647  70.803  1.00 30.65           C  
-ATOM   3190  C   PRO B 273       2.450  68.812  69.306  1.00 31.68           C  
-ATOM   3191  O   PRO B 273       3.356  68.512  68.515  1.00 31.36           O  
-ATOM   3192  CB  PRO B 273       3.516  69.796  71.336  1.00 30.35           C  
-ATOM   3193  CG  PRO B 273       4.408  69.152  72.357  1.00 30.52           C  
-ATOM   3194  CD  PRO B 273       4.728  67.804  71.801  1.00 29.81           C  
-ATOM   3195  N   GLU B 274       1.262  69.264  68.914  1.00 32.90           N  
-ATOM   3196  CA  GLU B 274       1.007  69.523  67.500  1.00 33.98           C  
-ATOM   3197  C   GLU B 274       1.882  70.683  67.034  1.00 33.86           C  
-ATOM   3198  O   GLU B 274       2.379  71.465  67.851  1.00 33.56           O  
-ATOM   3199  CB  GLU B 274      -0.486  69.755  67.206  1.00 34.55           C  
-ATOM   3200  CG  GLU B 274      -1.147  70.909  67.947  1.00 38.20           C  
-ATOM   3201  CD  GLU B 274      -2.526  71.265  67.394  1.00 43.16           C  
-ATOM   3202  OE1 GLU B 274      -2.943  70.686  66.359  1.00 44.95           O  
-ATOM   3203  OE2 GLU B 274      -3.199  72.140  67.996  1.00 45.71           O  
-ATOM   3204  N   VAL B 275       2.094  70.770  65.728  1.00 33.85           N  
-ATOM   3205  CA  VAL B 275       2.955  71.808  65.166  1.00 34.57           C  
-ATOM   3206  C   VAL B 275       2.484  73.221  65.554  1.00 34.93           C  
-ATOM   3207  O   VAL B 275       3.306  74.090  65.833  1.00 35.24           O  
-ATOM   3208  CB  VAL B 275       3.092  71.649  63.636  1.00 34.30           C  
-ATOM   3209  CG1 VAL B 275       3.995  72.719  63.054  1.00 34.70           C  
-ATOM   3210  CG2 VAL B 275       3.620  70.245  63.297  1.00 34.79           C  
-ATOM   3211  N   ALA B 276       1.168  73.431  65.588  1.00 35.40           N  
-ATOM   3212  CA  ALA B 276       0.584  74.716  65.968  1.00 35.88           C  
-ATOM   3213  C   ALA B 276       1.069  75.172  67.346  1.00 36.41           C  
-ATOM   3214  O   ALA B 276       1.300  76.364  67.571  1.00 36.35           O  
-ATOM   3215  CB  ALA B 276      -0.932  74.634  65.943  1.00 36.02           C  
-ATOM   3216  N   GLU B 277       1.232  74.218  68.258  1.00 36.75           N  
-ATOM   3217  CA  GLU B 277       1.715  74.515  69.600  1.00 37.43           C  
-ATOM   3218  C   GLU B 277       3.169  74.992  69.589  1.00 37.16           C  
-ATOM   3219  O   GLU B 277       3.525  75.891  70.356  1.00 37.04           O  
-ATOM   3220  CB  GLU B 277       1.489  73.322  70.542  1.00 38.05           C  
-ATOM   3221  CG  GLU B 277       0.009  73.088  70.853  1.00 40.20           C  
-ATOM   3222  CD  GLU B 277      -0.250  71.922  71.797  1.00 44.34           C  
-ATOM   3223  OE1 GLU B 277       0.260  70.808  71.542  1.00 45.10           O  
-ATOM   3224  OE2 GLU B 277      -0.990  72.113  72.793  1.00 46.57           O  
-ATOM   3225  N   PHE B 278       3.987  74.421  68.701  1.00 36.86           N  
-ATOM   3226  CA  PHE B 278       5.366  74.889  68.505  1.00 36.76           C  
-ATOM   3227  C   PHE B 278       5.446  76.270  67.840  1.00 37.71           C  
-ATOM   3228  O   PHE B 278       6.299  77.086  68.192  1.00 38.09           O  
-ATOM   3229  CB  PHE B 278       6.204  73.864  67.729  1.00 35.93           C  
-ATOM   3230  CG  PHE B 278       6.624  72.675  68.558  1.00 33.23           C  
-ATOM   3231  CD1 PHE B 278       7.658  72.782  69.494  1.00 30.75           C  
-ATOM   3232  CD2 PHE B 278       5.976  71.457  68.417  1.00 29.58           C  
-ATOM   3233  CE1 PHE B 278       8.035  71.681  70.268  1.00 29.75           C  
-ATOM   3234  CE2 PHE B 278       6.347  70.359  69.180  1.00 28.87           C  
-ATOM   3235  CZ  PHE B 278       7.379  70.466  70.103  1.00 27.90           C  
-ATOM   3236  N   VAL B 279       4.564  76.522  66.877  1.00 38.58           N  
-ATOM   3237  CA  VAL B 279       4.442  77.840  66.256  1.00 39.63           C  
-ATOM   3238  C   VAL B 279       4.077  78.894  67.310  1.00 40.74           C  
-ATOM   3239  O   VAL B 279       4.716  79.944  67.390  1.00 40.91           O  
-ATOM   3240  CB  VAL B 279       3.407  77.830  65.095  1.00 39.52           C  
-ATOM   3241  CG1 VAL B 279       3.280  79.213  64.453  1.00 38.96           C  
-ATOM   3242  CG2 VAL B 279       3.798  76.802  64.050  1.00 38.85           C  
-ATOM   3243  N   TYR B 280       3.071  78.587  68.126  1.00 42.09           N  
-ATOM   3244  CA  TYR B 280       2.638  79.450  69.227  1.00 43.94           C  
-ATOM   3245  C   TYR B 280       3.750  79.839  70.223  1.00 44.92           C  
-ATOM   3246  O   TYR B 280       3.869  81.015  70.588  1.00 44.91           O  
-ATOM   3247  CB  TYR B 280       1.453  78.808  69.962  1.00 44.03           C  
-ATOM   3248  CG  TYR B 280       0.896  79.631  71.107  1.00 45.68           C  
-ATOM   3249  CD1 TYR B 280       0.052  80.719  70.869  1.00 47.05           C  
-ATOM   3250  CD2 TYR B 280       1.201  79.313  72.428  1.00 47.21           C  
-ATOM   3251  CE1 TYR B 280      -0.465  81.471  71.917  1.00 47.79           C  
-ATOM   3252  CE2 TYR B 280       0.688  80.061  73.486  1.00 48.73           C  
-ATOM   3253  CZ  TYR B 280      -0.143  81.137  73.221  1.00 49.01           C  
-ATOM   3254  OH  TYR B 280      -0.648  81.878  74.270  1.00 51.44           O  
-ATOM   3255  N   ILE B 281       4.554  78.865  70.653  1.00 46.27           N  
-ATOM   3256  CA  ILE B 281       5.617  79.105  71.646  1.00 47.84           C  
-ATOM   3257  C   ILE B 281       6.743  80.026  71.172  1.00 48.62           C  
-ATOM   3258  O   ILE B 281       7.506  80.546  71.990  1.00 48.61           O  
-ATOM   3259  CB  ILE B 281       6.212  77.777  72.197  1.00 47.81           C  
-ATOM   3260  CG1 ILE B 281       6.689  76.873  71.063  1.00 48.47           C  
-ATOM   3261  CG2 ILE B 281       5.210  77.071  73.065  1.00 48.71           C  
-ATOM   3262  CD1 ILE B 281       7.920  76.055  71.388  1.00 50.81           C  
-ATOM   3263  N   THR B 282       6.841  80.226  69.860  1.00 50.05           N  
-ATOM   3264  CA  THR B 282       7.787  81.188  69.298  1.00 51.45           C  
-ATOM   3265  C   THR B 282       7.185  82.594  69.218  1.00 52.39           C  
-ATOM   3266  O   THR B 282       7.747  83.470  68.559  1.00 52.73           O  
-ATOM   3267  CB  THR B 282       8.302  80.734  67.901  1.00 51.67           C  
-ATOM   3268  OG1 THR B 282       7.199  80.564  67.001  1.00 52.44           O  
-ATOM   3269  CG2 THR B 282       8.922  79.343  67.966  1.00 51.16           C  
-ATOM   3270  N   ASP B 283       6.049  82.800  69.898  1.00 53.42           N  
-ATOM   3271  CA  ASP B 283       5.322  84.084  69.926  1.00 54.33           C  
-ATOM   3272  C   ASP B 283       5.057  84.679  68.531  1.00 54.34           C  
-ATOM   3273  O   ASP B 283       5.119  85.897  68.327  1.00 54.44           O  
-ATOM   3274  CB  ASP B 283       6.038  85.098  70.832  1.00 54.77           C  
-ATOM   3275  CG  ASP B 283       5.098  85.758  71.826  1.00 56.23           C  
-ATOM   3276  OD1 ASP B 283       4.805  85.139  72.879  1.00 57.86           O  
-ATOM   3277  OD2 ASP B 283       4.605  86.894  71.638  1.00 57.53           O  
-ATOM   3278  N   ASP B 284       4.760  83.792  67.583  1.00 54.38           N  
-ATOM   3279  CA  ASP B 284       4.552  84.133  66.167  1.00 54.02           C  
-ATOM   3280  C   ASP B 284       5.698  84.889  65.475  1.00 53.02           C  
-ATOM   3281  O   ASP B 284       5.457  85.666  64.545  1.00 52.90           O  
-ATOM   3282  CB  ASP B 284       3.192  84.814  65.943  1.00 54.58           C  
-ATOM   3283  CG  ASP B 284       2.130  83.846  65.443  1.00 56.15           C  
-ATOM   3284  OD1 ASP B 284       2.230  83.390  64.278  1.00 58.00           O  
-ATOM   3285  OD2 ASP B 284       1.158  83.480  66.143  1.00 58.43           O  
-ATOM   3286  N   THR B 285       6.940  84.657  65.912  1.00 51.74           N  
-ATOM   3287  CA  THR B 285       8.106  85.155  65.166  1.00 50.32           C  
-ATOM   3288  C   THR B 285       8.164  84.489  63.784  1.00 48.81           C  
-ATOM   3289  O   THR B 285       8.564  85.110  62.793  1.00 49.03           O  
-ATOM   3290  CB  THR B 285       9.441  84.914  65.932  1.00 50.56           C  
-ATOM   3291  OG1 THR B 285       9.252  83.936  66.961  1.00 51.82           O  
-ATOM   3292  CG2 THR B 285       9.863  86.156  66.708  1.00 50.72           C  
-ATOM   3293  N   TYR B 286       7.741  83.228  63.734  1.00 46.51           N  
-ATOM   3294  CA  TYR B 286       7.796  82.425  62.521  1.00 44.30           C  
-ATOM   3295  C   TYR B 286       6.429  81.858  62.168  1.00 43.58           C  
-ATOM   3296  O   TYR B 286       5.567  81.708  63.035  1.00 43.87           O  
-ATOM   3297  CB  TYR B 286       8.759  81.257  62.714  1.00 43.73           C  
-ATOM   3298  CG  TYR B 286      10.110  81.609  63.287  1.00 40.44           C  
-ATOM   3299  CD1 TYR B 286      11.038  82.337  62.542  1.00 37.66           C  
-ATOM   3300  CD2 TYR B 286      10.471  81.186  64.568  1.00 37.56           C  
-ATOM   3301  CE1 TYR B 286      12.281  82.644  63.056  1.00 35.41           C  
-ATOM   3302  CE2 TYR B 286      11.711  81.484  65.093  1.00 35.12           C  
-ATOM   3303  CZ  TYR B 286      12.614  82.210  64.333  1.00 35.16           C  
-ATOM   3304  OH  TYR B 286      13.847  82.509  64.851  1.00 33.98           O  
-ATOM   3305  N   THR B 287       6.236  81.528  60.898  1.00 42.41           N  
-ATOM   3306  CA  THR B 287       4.994  80.896  60.467  1.00 41.54           C  
-ATOM   3307  C   THR B 287       5.090  79.381  60.596  1.00 40.99           C  
-ATOM   3308  O   THR B 287       6.186  78.826  60.739  1.00 40.70           O  
-ATOM   3309  CB  THR B 287       4.652  81.274  59.012  1.00 41.69           C  
-ATOM   3310  OG1 THR B 287       5.551  80.606  58.119  1.00 41.61           O  
-ATOM   3311  CG2 THR B 287       4.910  82.767  58.751  1.00 41.38           C  
-ATOM   3312  N   LYS B 288       3.932  78.723  60.549  1.00 40.38           N  
-ATOM   3313  CA  LYS B 288       3.854  77.271  60.475  1.00 39.70           C  
-ATOM   3314  C   LYS B 288       4.675  76.703  59.314  1.00 39.19           C  
-ATOM   3315  O   LYS B 288       5.364  75.693  59.476  1.00 39.01           O  
-ATOM   3316  CB  LYS B 288       2.401  76.826  60.356  1.00 40.04           C  
-ATOM   3317  CG  LYS B 288       2.204  75.342  60.574  1.00 40.43           C  
-ATOM   3318  CD  LYS B 288       0.802  74.925  60.233  1.00 42.35           C  
-ATOM   3319  CE  LYS B 288       0.596  73.466  60.592  1.00 43.99           C  
-ATOM   3320  NZ  LYS B 288      -0.788  72.993  60.303  1.00 46.01           N  
-ATOM   3321  N   LYS B 289       4.597  77.359  58.157  1.00 38.29           N  
-ATOM   3322  CA  LYS B 289       5.318  76.944  56.957  1.00 37.57           C  
-ATOM   3323  C   LYS B 289       6.831  76.958  57.160  1.00 36.53           C  
-ATOM   3324  O   LYS B 289       7.527  76.059  56.693  1.00 36.38           O  
-ATOM   3325  CB  LYS B 289       4.949  77.836  55.768  1.00 37.93           C  
-ATOM   3326  CG  LYS B 289       5.240  77.214  54.416  1.00 39.71           C  
-ATOM   3327  CD  LYS B 289       5.271  78.261  53.319  1.00 42.76           C  
-ATOM   3328  CE  LYS B 289       6.289  77.908  52.244  1.00 44.97           C  
-ATOM   3329  NZ  LYS B 289       5.745  78.110  50.867  1.00 46.97           N  
-ATOM   3330  N   GLN B 290       7.334  77.982  57.845  1.00 35.07           N  
-ATOM   3331  CA  GLN B 290       8.757  78.065  58.162  1.00 34.00           C  
-ATOM   3332  C   GLN B 290       9.211  76.886  59.023  1.00 32.88           C  
-ATOM   3333  O   GLN B 290      10.203  76.230  58.710  1.00 32.54           O  
-ATOM   3334  CB  GLN B 290       9.075  79.383  58.863  1.00 33.92           C  
-ATOM   3335  CG  GLN B 290       9.085  80.578  57.923  1.00 34.89           C  
-ATOM   3336  CD  GLN B 290       9.507  81.839  58.619  1.00 35.11           C  
-ATOM   3337  OE1 GLN B 290       8.779  82.353  59.467  1.00 35.67           O  
-ATOM   3338  NE2 GLN B 290      10.689  82.337  58.282  1.00 34.59           N  
-ATOM   3339  N   VAL B 291       8.466  76.627  60.095  1.00 31.80           N  
-ATOM   3340  CA  VAL B 291       8.772  75.547  61.027  1.00 31.35           C  
-ATOM   3341  C   VAL B 291       8.843  74.220  60.280  1.00 30.44           C  
-ATOM   3342  O   VAL B 291       9.797  73.467  60.425  1.00 30.49           O  
-ATOM   3343  CB  VAL B 291       7.725  75.467  62.183  1.00 31.19           C  
-ATOM   3344  CG1 VAL B 291       7.979  74.250  63.069  1.00 31.49           C  
-ATOM   3345  CG2 VAL B 291       7.738  76.748  63.026  1.00 30.97           C  
-ATOM   3346  N   LEU B 292       7.833  73.969  59.457  1.00 30.00           N  
-ATOM   3347  CA  LEU B 292       7.727  72.736  58.689  1.00 29.55           C  
-ATOM   3348  C   LEU B 292       8.844  72.587  57.652  1.00 28.98           C  
-ATOM   3349  O   LEU B 292       9.362  71.485  57.445  1.00 28.81           O  
-ATOM   3350  CB  LEU B 292       6.338  72.649  58.042  1.00 29.66           C  
-ATOM   3351  CG  LEU B 292       5.367  71.669  58.705  1.00 30.71           C  
-ATOM   3352  CD1 LEU B 292       5.596  71.559  60.215  1.00 31.78           C  
-ATOM   3353  CD2 LEU B 292       3.917  71.994  58.406  1.00 30.72           C  
-ATOM   3354  N   ARG B 293       9.218  73.696  57.012  1.00 28.24           N  
-ATOM   3355  CA  ARG B 293      10.336  73.701  56.075  1.00 28.21           C  
-ATOM   3356  C   ARG B 293      11.645  73.437  56.817  1.00 26.95           C  
-ATOM   3357  O   ARG B 293      12.486  72.682  56.344  1.00 26.55           O  
-ATOM   3358  CB  ARG B 293      10.407  75.024  55.288  1.00 29.02           C  
-ATOM   3359  CG  ARG B 293       9.312  75.193  54.218  1.00 32.19           C  
-ATOM   3360  CD  ARG B 293       9.749  75.993  53.000  1.00 39.61           C  
-ATOM   3361  NE  ARG B 293       8.933  75.682  51.826  1.00 45.64           N  
-ATOM   3362  CZ  ARG B 293       8.989  76.326  50.659  1.00 48.53           C  
-ATOM   3363  NH1 ARG B 293       9.841  77.333  50.471  1.00 49.92           N  
-ATOM   3364  NH2 ARG B 293       8.194  75.946  49.663  1.00 50.16           N  
-ATOM   3365  N   MET B 294      11.801  74.041  57.992  1.00 25.91           N  
-ATOM   3366  CA  MET B 294      12.999  73.812  58.798  1.00 25.33           C  
-ATOM   3367  C   MET B 294      13.052  72.369  59.311  1.00 24.71           C  
-ATOM   3368  O   MET B 294      14.130  71.780  59.373  1.00 24.45           O  
-ATOM   3369  CB  MET B 294      13.129  74.832  59.942  1.00 24.92           C  
-ATOM   3370  CG  MET B 294      14.424  74.737  60.751  1.00 25.45           C  
-ATOM   3371  SD  MET B 294      15.969  75.087  59.867  1.00 26.22           S  
-ATOM   3372  CE  MET B 294      15.916  76.923  59.775  1.00 28.22           C  
-ATOM   3373  N   GLU B 295      11.901  71.798  59.650  1.00 24.70           N  
-ATOM   3374  CA  GLU B 295      11.857  70.401  60.082  1.00 25.31           C  
-ATOM   3375  C   GLU B 295      12.531  69.532  59.029  1.00 25.90           C  
-ATOM   3376  O   GLU B 295      13.423  68.735  59.351  1.00 26.09           O  
-ATOM   3377  CB  GLU B 295      10.423  69.915  60.341  1.00 25.31           C  
-ATOM   3378  CG  GLU B 295      10.350  68.447  60.758  1.00 26.14           C  
-ATOM   3379  CD  GLU B 295       8.937  67.900  60.872  1.00 27.24           C  
-ATOM   3380  OE1 GLU B 295       8.214  67.863  59.852  1.00 27.06           O  
-ATOM   3381  OE2 GLU B 295       8.550  67.484  61.985  1.00 27.92           O  
-ATOM   3382  N   HIS B 296      12.124  69.717  57.772  1.00 26.34           N  
-ATOM   3383  CA  HIS B 296      12.641  68.918  56.671  1.00 26.86           C  
-ATOM   3384  C   HIS B 296      14.116  69.170  56.418  1.00 26.10           C  
-ATOM   3385  O   HIS B 296      14.875  68.224  56.204  1.00 26.33           O  
-ATOM   3386  CB  HIS B 296      11.834  69.143  55.389  1.00 27.80           C  
-ATOM   3387  CG  HIS B 296      11.692  67.909  54.555  1.00 31.51           C  
-ATOM   3388  ND1 HIS B 296      10.550  67.619  53.840  1.00 34.24           N  
-ATOM   3389  CD2 HIS B 296      12.542  66.872  54.346  1.00 34.93           C  
-ATOM   3390  CE1 HIS B 296      10.710  66.466  53.212  1.00 36.31           C  
-ATOM   3391  NE2 HIS B 296      11.907  65.989  53.506  1.00 36.28           N  
-ATOM   3392  N   LEU B 297      14.521  70.441  56.449  1.00 24.94           N  
-ATOM   3393  CA  LEU B 297      15.931  70.804  56.286  1.00 23.82           C  
-ATOM   3394  C   LEU B 297      16.808  70.143  57.346  1.00 23.17           C  
-ATOM   3395  O   LEU B 297      17.856  69.588  57.023  1.00 23.26           O  
-ATOM   3396  CB  LEU B 297      16.119  72.332  56.311  1.00 23.47           C  
-ATOM   3397  CG  LEU B 297      17.556  72.866  56.219  1.00 23.04           C  
-ATOM   3398  CD1 LEU B 297      18.233  72.479  54.891  1.00 22.83           C  
-ATOM   3399  CD2 LEU B 297      17.600  74.379  56.417  1.00 22.96           C  
-ATOM   3400  N   VAL B 298      16.378  70.207  58.608  1.00 22.54           N  
-ATOM   3401  CA  VAL B 298      17.118  69.588  59.716  1.00 22.11           C  
-ATOM   3402  C   VAL B 298      17.262  68.070  59.506  1.00 22.05           C  
-ATOM   3403  O   VAL B 298      18.320  67.507  59.785  1.00 22.10           O  
-ATOM   3404  CB  VAL B 298      16.467  69.903  61.091  1.00 21.89           C  
-ATOM   3405  CG1 VAL B 298      17.125  69.114  62.204  1.00 22.23           C  
-ATOM   3406  CG2 VAL B 298      16.565  71.399  61.397  1.00 21.73           C  
-ATOM   3407  N   LEU B 299      16.212  67.426  58.989  1.00 21.69           N  
-ATOM   3408  CA  LEU B 299      16.236  65.986  58.727  1.00 22.09           C  
-ATOM   3409  C   LEU B 299      17.203  65.655  57.600  1.00 22.24           C  
-ATOM   3410  O   LEU B 299      17.876  64.622  57.629  1.00 22.57           O  
-ATOM   3411  CB  LEU B 299      14.834  65.460  58.389  1.00 21.95           C  
-ATOM   3412  CG  LEU B 299      13.842  65.254  59.532  1.00 21.84           C  
-ATOM   3413  CD1 LEU B 299      12.418  65.212  59.000  1.00 21.91           C  
-ATOM   3414  CD2 LEU B 299      14.154  63.978  60.315  1.00 21.17           C  
-ATOM   3415  N   LYS B 300      17.284  66.553  56.623  1.00 22.65           N  
-ATOM   3416  CA  LYS B 300      18.228  66.419  55.516  1.00 23.21           C  
-ATOM   3417  C   LYS B 300      19.660  66.580  55.998  1.00 22.72           C  
-ATOM   3418  O   LYS B 300      20.510  65.731  55.733  1.00 22.91           O  
-ATOM   3419  CB  LYS B 300      17.912  67.422  54.405  1.00 23.24           C  
-ATOM   3420  CG  LYS B 300      16.637  67.070  53.645  1.00 26.78           C  
-ATOM   3421  CD  LYS B 300      16.408  67.993  52.461  1.00 30.00           C  
-ATOM   3422  CE  LYS B 300      14.993  67.854  51.944  1.00 32.72           C  
-ATOM   3423  NZ  LYS B 300      14.163  68.997  52.451  1.00 35.85           N  
-ATOM   3424  N   VAL B 301      19.929  67.663  56.715  1.00 22.37           N  
-ATOM   3425  CA  VAL B 301      21.268  67.888  57.245  1.00 22.12           C  
-ATOM   3426  C   VAL B 301      21.741  66.735  58.151  1.00 21.94           C  
-ATOM   3427  O   VAL B 301      22.909  66.328  58.092  1.00 21.96           O  
-ATOM   3428  CB  VAL B 301      21.373  69.253  57.972  1.00 22.00           C  
-ATOM   3429  CG1 VAL B 301      22.784  69.461  58.535  1.00 22.05           C  
-ATOM   3430  CG2 VAL B 301      21.022  70.382  57.004  1.00 22.23           C  
-ATOM   3431  N   LEU B 302      20.833  66.214  58.974  1.00 21.58           N  
-ATOM   3432  CA  LEU B 302      21.155  65.113  59.892  1.00 21.50           C  
-ATOM   3433  C   LEU B 302      21.083  63.747  59.213  1.00 21.56           C  
-ATOM   3434  O   LEU B 302      21.360  62.727  59.842  1.00 21.74           O  
-ATOM   3435  CB  LEU B 302      20.229  65.142  61.127  1.00 21.15           C  
-ATOM   3436  CG  LEU B 302      20.262  66.419  61.985  1.00 21.00           C  
-ATOM   3437  CD1 LEU B 302      19.451  66.279  63.267  1.00 22.03           C  
-ATOM   3438  CD2 LEU B 302      21.685  66.853  62.297  1.00 20.52           C  
-ATOM   3439  N   THR B 303      20.712  63.750  57.929  1.00 21.60           N  
-ATOM   3440  CA  THR B 303      20.356  62.555  57.155  1.00 21.51           C  
-ATOM   3441  C   THR B 303      19.495  61.562  57.951  1.00 21.51           C  
-ATOM   3442  O   THR B 303      19.726  60.353  57.913  1.00 21.09           O  
-ATOM   3443  CB  THR B 303      21.591  61.866  56.511  1.00 21.34           C  
-ATOM   3444  OG1 THR B 303      22.546  61.539  57.518  1.00 21.59           O  
-ATOM   3445  CG2 THR B 303      22.337  62.818  55.584  1.00 21.97           C  
-ATOM   3446  N   PHE B 304      18.504  62.102  58.661  1.00 21.33           N  
-ATOM   3447  CA  PHE B 304      17.536  61.312  59.411  1.00 21.57           C  
-ATOM   3448  C   PHE B 304      18.142  60.513  60.578  1.00 21.07           C  
-ATOM   3449  O   PHE B 304      17.485  59.632  61.118  1.00 20.67           O  
-ATOM   3450  CB  PHE B 304      16.776  60.364  58.468  1.00 21.98           C  
-ATOM   3451  CG  PHE B 304      15.703  61.036  57.657  1.00 23.24           C  
-ATOM   3452  CD1 PHE B 304      14.391  61.029  58.091  1.00 23.31           C  
-ATOM   3453  CD2 PHE B 304      16.009  61.668  56.450  1.00 25.19           C  
-ATOM   3454  CE1 PHE B 304      13.393  61.635  57.348  1.00 25.26           C  
-ATOM   3455  CE2 PHE B 304      15.001  62.295  55.697  1.00 26.14           C  
-ATOM   3456  CZ  PHE B 304      13.696  62.270  56.149  1.00 23.85           C  
-ATOM   3457  N   ASP B 305      19.380  60.814  60.960  1.00 20.82           N  
-ATOM   3458  CA  ASP B 305      20.037  60.081  62.034  1.00 20.79           C  
-ATOM   3459  C   ASP B 305      19.662  60.674  63.400  1.00 20.54           C  
-ATOM   3460  O   ASP B 305      20.425  61.440  63.996  1.00 20.61           O  
-ATOM   3461  CB  ASP B 305      21.556  60.036  61.809  1.00 21.26           C  
-ATOM   3462  CG  ASP B 305      21.937  59.277  60.534  1.00 22.92           C  
-ATOM   3463  OD1 ASP B 305      21.473  58.135  60.344  1.00 24.35           O  
-ATOM   3464  OD2 ASP B 305      22.676  59.752  59.646  1.00 27.10           O  
-ATOM   3465  N   LEU B 306      18.478  60.305  63.885  1.00 20.00           N  
-ATOM   3466  CA  LEU B 306      17.879  60.921  65.079  1.00 19.99           C  
-ATOM   3467  C   LEU B 306      18.000  60.140  66.393  1.00 19.22           C  
-ATOM   3468  O   LEU B 306      17.704  60.679  67.475  1.00 19.25           O  
-ATOM   3469  CB  LEU B 306      16.401  61.236  64.818  1.00 20.31           C  
-ATOM   3470  CG  LEU B 306      16.011  62.135  63.634  1.00 21.63           C  
-ATOM   3471  CD1 LEU B 306      14.564  62.532  63.805  1.00 21.82           C  
-ATOM   3472  CD2 LEU B 306      16.889  63.390  63.494  1.00 21.72           C  
-ATOM   3473  N   ALA B 307      18.418  58.879  66.306  1.00 18.45           N  
-ATOM   3474  CA  ALA B 307      18.546  58.014  67.478  1.00 17.93           C  
-ATOM   3475  C   ALA B 307      19.896  58.224  68.168  1.00 18.08           C  
-ATOM   3476  O   ALA B 307      20.717  57.310  68.265  1.00 18.04           O  
-ATOM   3477  CB  ALA B 307      18.353  56.541  67.073  1.00 17.77           C  
-ATOM   3478  N   ALA B 308      20.118  59.440  68.647  1.00 18.24           N  
-ATOM   3479  CA  ALA B 308      21.399  59.831  69.227  1.00 18.83           C  
-ATOM   3480  C   ALA B 308      21.446  59.491  70.719  1.00 19.13           C  
-ATOM   3481  O   ALA B 308      20.463  59.691  71.424  1.00 19.36           O  
-ATOM   3482  CB  ALA B 308      21.615  61.322  69.026  1.00 18.79           C  
-ATOM   3483  N   PRO B 309      22.573  58.957  71.188  1.00 19.54           N  
-ATOM   3484  CA  PRO B 309      22.795  58.768  72.627  1.00 19.69           C  
-ATOM   3485  C   PRO B 309      22.863  60.096  73.351  1.00 19.83           C  
-ATOM   3486  O   PRO B 309      23.427  61.066  72.828  1.00 20.71           O  
-ATOM   3487  CB  PRO B 309      24.155  58.059  72.683  1.00 19.29           C  
-ATOM   3488  CG  PRO B 309      24.310  57.468  71.337  1.00 19.64           C  
-ATOM   3489  CD  PRO B 309      23.713  58.462  70.392  1.00 19.02           C  
-ATOM   3490  N   THR B 310      22.264  60.147  74.535  1.00 19.54           N  
-ATOM   3491  CA  THR B 310      22.248  61.367  75.335  1.00 19.22           C  
-ATOM   3492  C   THR B 310      22.905  61.096  76.685  1.00 18.86           C  
-ATOM   3493  O   THR B 310      23.139  59.948  77.061  1.00 18.08           O  
-ATOM   3494  CB  THR B 310      20.818  61.848  75.579  1.00 19.26           C  
-ATOM   3495  OG1 THR B 310      20.093  60.823  76.273  1.00 20.22           O  
-ATOM   3496  CG2 THR B 310      20.050  62.034  74.265  1.00 19.66           C  
-ATOM   3497  N   VAL B 311      23.193  62.171  77.405  1.00 18.93           N  
-ATOM   3498  CA  VAL B 311      23.705  62.078  78.761  1.00 19.08           C  
-ATOM   3499  C   VAL B 311      22.714  61.272  79.587  1.00 19.52           C  
-ATOM   3500  O   VAL B 311      23.099  60.416  80.382  1.00 19.13           O  
-ATOM   3501  CB  VAL B 311      23.904  63.485  79.360  1.00 19.19           C  
-ATOM   3502  CG1 VAL B 311      23.898  63.439  80.885  1.00 18.72           C  
-ATOM   3503  CG2 VAL B 311      25.192  64.093  78.843  1.00 18.41           C  
-ATOM   3504  N   ASN B 312      21.435  61.544  79.345  1.00 20.34           N  
-ATOM   3505  CA  ASN B 312      20.322  60.879  79.995  1.00 21.48           C  
-ATOM   3506  C   ASN B 312      20.335  59.358  79.840  1.00 21.21           C  
-ATOM   3507  O   ASN B 312      20.244  58.626  80.829  1.00 21.36           O  
-ATOM   3508  CB  ASN B 312      19.001  61.466  79.466  1.00 22.25           C  
-ATOM   3509  CG  ASN B 312      17.791  60.873  80.137  1.00 25.08           C  
-ATOM   3510  OD1 ASN B 312      17.523  61.147  81.308  1.00 26.75           O  
-ATOM   3511  ND2 ASN B 312      17.047  60.039  79.399  1.00 26.80           N  
-ATOM   3512  N   GLN B 313      20.467  58.886  78.604  1.00 20.35           N  
-ATOM   3513  CA  GLN B 313      20.485  57.452  78.340  1.00 19.34           C  
-ATOM   3514  C   GLN B 313      21.593  56.729  79.097  1.00 18.69           C  
-ATOM   3515  O   GLN B 313      21.398  55.599  79.507  1.00 18.64           O  
-ATOM   3516  CB  GLN B 313      20.627  57.170  76.845  1.00 19.40           C  
-ATOM   3517  CG  GLN B 313      19.392  57.453  76.025  1.00 19.08           C  
-ATOM   3518  CD  GLN B 313      19.676  57.345  74.537  1.00 19.52           C  
-ATOM   3519  OE1 GLN B 313      20.199  56.330  74.080  1.00 21.15           O  
-ATOM   3520  NE2 GLN B 313      19.348  58.387  73.785  1.00 17.41           N  
-ATOM   3521  N   PHE B 314      22.755  57.364  79.258  1.00 17.84           N  
-ATOM   3522  CA  PHE B 314      23.854  56.756  80.029  1.00 17.52           C  
-ATOM   3523  C   PHE B 314      23.597  56.822  81.543  1.00 17.37           C  
-ATOM   3524  O   PHE B 314      23.879  55.852  82.254  1.00 17.32           O  
-ATOM   3525  CB  PHE B 314      25.221  57.388  79.690  1.00 16.84           C  
-ATOM   3526  CG  PHE B 314      25.813  56.908  78.377  1.00 17.45           C  
-ATOM   3527  CD1 PHE B 314      26.455  55.665  78.291  1.00 16.99           C  
-ATOM   3528  CD2 PHE B 314      25.734  57.699  77.233  1.00 16.07           C  
-ATOM   3529  CE1 PHE B 314      26.996  55.208  77.077  1.00 16.47           C  
-ATOM   3530  CE2 PHE B 314      26.276  57.252  76.000  1.00 17.41           C  
-ATOM   3531  CZ  PHE B 314      26.912  56.004  75.929  1.00 15.95           C  
-ATOM   3532  N   LEU B 315      23.085  57.962  82.016  1.00 16.85           N  
-ATOM   3533  CA  LEU B 315      22.705  58.148  83.432  1.00 17.64           C  
-ATOM   3534  C   LEU B 315      21.778  57.051  83.961  1.00 17.37           C  
-ATOM   3535  O   LEU B 315      22.049  56.464  85.006  1.00 17.67           O  
-ATOM   3536  CB  LEU B 315      22.048  59.523  83.670  1.00 16.48           C  
-ATOM   3537  CG  LEU B 315      22.952  60.744  83.875  1.00 17.88           C  
-ATOM   3538  CD1 LEU B 315      22.122  62.043  84.058  1.00 16.40           C  
-ATOM   3539  CD2 LEU B 315      23.930  60.534  85.058  1.00 16.42           C  
-ATOM   3540  N   THR B 316      20.695  56.764  83.239  1.00 17.70           N  
-ATOM   3541  CA  THR B 316      19.740  55.739  83.690  1.00 18.05           C  
-ATOM   3542  C   THR B 316      20.373  54.350  83.749  1.00 18.49           C  
-ATOM   3543  O   THR B 316      19.955  53.511  84.541  1.00 18.68           O  
-ATOM   3544  CB  THR B 316      18.471  55.706  82.797  1.00 18.35           C  
-ATOM   3545  OG1 THR B 316      18.831  55.279  81.473  1.00 17.71           O  
-ATOM   3546  CG2 THR B 316      17.896  57.128  82.603  1.00 18.09           C  
-ATOM   3547  N   GLN B 317      21.363  54.084  82.898  1.00 19.06           N  
-ATOM   3548  CA  GLN B 317      22.115  52.833  83.045  1.00 19.64           C  
-ATOM   3549  C   GLN B 317      23.003  52.871  84.278  1.00 19.34           C  
-ATOM   3550  O   GLN B 317      23.103  51.883  84.993  1.00 19.27           O  
-ATOM   3551  CB  GLN B 317      22.969  52.559  81.828  1.00 20.31           C  
-ATOM   3552  CG  GLN B 317      22.185  52.285  80.574  1.00 22.99           C  
-ATOM   3553  CD  GLN B 317      23.112  52.098  79.406  1.00 26.91           C  
-ATOM   3554  OE1 GLN B 317      23.586  53.068  78.828  1.00 31.03           O  
-ATOM   3555  NE2 GLN B 317      23.397  50.862  79.073  1.00 28.78           N  
-ATOM   3556  N   TYR B 318      23.638  54.014  84.530  1.00 18.96           N  
-ATOM   3557  CA  TYR B 318      24.555  54.138  85.659  1.00 19.51           C  
-ATOM   3558  C   TYR B 318      23.798  54.034  86.982  1.00 19.79           C  
-ATOM   3559  O   TYR B 318      24.321  53.520  87.967  1.00 19.11           O  
-ATOM   3560  CB  TYR B 318      25.308  55.473  85.621  1.00 19.05           C  
-ATOM   3561  CG  TYR B 318      26.264  55.682  84.463  1.00 19.10           C  
-ATOM   3562  CD1 TYR B 318      26.490  54.691  83.492  1.00 18.59           C  
-ATOM   3563  CD2 TYR B 318      26.955  56.882  84.344  1.00 17.89           C  
-ATOM   3564  CE1 TYR B 318      27.374  54.911  82.432  1.00 18.04           C  
-ATOM   3565  CE2 TYR B 318      27.828  57.106  83.307  1.00 17.10           C  
-ATOM   3566  CZ  TYR B 318      28.038  56.127  82.354  1.00 18.97           C  
-ATOM   3567  OH  TYR B 318      28.921  56.389  81.327  1.00 17.96           O  
-ATOM   3568  N   PHE B 319      22.563  54.539  86.991  1.00 20.98           N  
-ATOM   3569  CA  PHE B 319      21.685  54.469  88.165  1.00 21.60           C  
-ATOM   3570  C   PHE B 319      21.466  53.036  88.673  1.00 21.99           C  
-ATOM   3571  O   PHE B 319      21.210  52.821  89.859  1.00 21.74           O  
-ATOM   3572  CB  PHE B 319      20.334  55.132  87.862  1.00 21.19           C  
-ATOM   3573  CG  PHE B 319      20.406  56.634  87.688  1.00 21.60           C  
-ATOM   3574  CD1 PHE B 319      21.534  57.350  88.074  1.00 20.96           C  
-ATOM   3575  CD2 PHE B 319      19.335  57.331  87.133  1.00 21.49           C  
-ATOM   3576  CE1 PHE B 319      21.593  58.724  87.915  1.00 20.84           C  
-ATOM   3577  CE2 PHE B 319      19.386  58.705  86.978  1.00 20.85           C  
-ATOM   3578  CZ  PHE B 319      20.519  59.406  87.363  1.00 19.98           C  
-ATOM   3579  N   LEU B 320      21.568  52.061  87.779  1.00 22.64           N  
-ATOM   3580  CA  LEU B 320      21.432  50.664  88.172  1.00 24.03           C  
-ATOM   3581  C   LEU B 320      22.585  50.163  89.066  1.00 25.09           C  
-ATOM   3582  O   LEU B 320      22.504  49.078  89.636  1.00 25.30           O  
-ATOM   3583  CB  LEU B 320      21.257  49.768  86.934  1.00 23.75           C  
-ATOM   3584  CG  LEU B 320      20.074  50.129  86.028  1.00 23.91           C  
-ATOM   3585  CD1 LEU B 320      20.088  49.301  84.743  1.00 24.36           C  
-ATOM   3586  CD2 LEU B 320      18.753  49.952  86.778  1.00 23.60           C  
-ATOM   3587  N   HIS B 321      23.643  50.953  89.182  1.00 26.61           N  
-ATOM   3588  CA  HIS B 321      24.794  50.589  90.009  1.00 29.02           C  
-ATOM   3589  C   HIS B 321      24.805  51.323  91.353  1.00 30.65           C  
-ATOM   3590  O   HIS B 321      25.866  51.546  91.938  1.00 31.47           O  
-ATOM   3591  CB  HIS B 321      26.106  50.836  89.259  1.00 28.07           C  
-ATOM   3592  CG  HIS B 321      26.302  49.942  88.074  1.00 27.88           C  
-ATOM   3593  ND1 HIS B 321      27.309  49.004  88.012  1.00 26.81           N  
-ATOM   3594  CD2 HIS B 321      25.622  49.843  86.907  1.00 26.34           C  
-ATOM   3595  CE1 HIS B 321      27.237  48.360  86.861  1.00 25.82           C  
-ATOM   3596  NE2 HIS B 321      26.224  48.850  86.172  1.00 26.00           N  
-ATOM   3597  N   GLN B 322      23.629  51.711  91.830  1.00 32.65           N  
-ATOM   3598  CA  GLN B 322      23.505  52.276  93.172  1.00 34.77           C  
-ATOM   3599  C   GLN B 322      23.190  51.167  94.167  1.00 36.00           C  
-ATOM   3600  O   GLN B 322      22.477  50.220  93.838  1.00 36.55           O  
-ATOM   3601  CB  GLN B 322      22.378  53.307  93.234  1.00 34.63           C  
-ATOM   3602  CG  GLN B 322      22.580  54.561  92.414  1.00 34.44           C  
-ATOM   3603  CD  GLN B 322      21.292  55.360  92.320  1.00 35.21           C  
-ATOM   3604  OE1 GLN B 322      21.099  56.330  93.069  1.00 35.06           O  
-ATOM   3605  NE2 GLN B 322      20.388  54.937  91.425  1.00 32.81           N  
-ATOM   3606  N   GLN B 323      23.700  51.296  95.388  1.00 37.86           N  
-ATOM   3607  CA  GLN B 323      23.293  50.394  96.467  1.00 39.45           C  
-ATOM   3608  C   GLN B 323      23.166  51.104  97.817  1.00 39.61           C  
-ATOM   3609  O   GLN B 323      24.174  51.371  98.486  1.00 40.30           O  
-ATOM   3610  CB  GLN B 323      24.220  49.176  96.561  1.00 40.09           C  
-ATOM   3611  CG  GLN B 323      23.639  48.013  97.374  1.00 43.09           C  
-ATOM   3612  CD  GLN B 323      22.282  47.534  96.864  1.00 46.79           C  
-ATOM   3613  OE1 GLN B 323      21.326  47.408  97.640  1.00 48.77           O  
-ATOM   3614  NE2 GLN B 323      22.196  47.260  95.563  1.00 48.61           N  
-ATOM   3615  N   PRO B 324      21.932  51.420  98.215  1.00 39.41           N  
-ATOM   3616  CA  PRO B 324      20.734  51.148  97.416  1.00 38.79           C  
-ATOM   3617  C   PRO B 324      20.423  52.325  96.490  1.00 37.99           C  
-ATOM   3618  O   PRO B 324      21.192  53.286  96.475  1.00 38.04           O  
-ATOM   3619  CB  PRO B 324      19.647  51.027  98.486  1.00 38.86           C  
-ATOM   3620  CG  PRO B 324      20.087  51.983  99.563  1.00 38.93           C  
-ATOM   3621  CD  PRO B 324      21.593  52.074  99.494  1.00 39.55           C  
-ATOM   3622  N   ALA B 325      19.318  52.251  95.748  1.00 37.17           N  
-ATOM   3623  CA  ALA B 325      18.894  53.353  94.886  1.00 36.43           C  
-ATOM   3624  C   ALA B 325      18.503  54.569  95.723  1.00 35.94           C  
-ATOM   3625  O   ALA B 325      17.853  54.433  96.769  1.00 36.01           O  
-ATOM   3626  CB  ALA B 325      17.751  52.924  94.007  1.00 36.49           C  
-ATOM   3627  N   ASN B 326      18.910  55.751  95.265  1.00 35.00           N  
-ATOM   3628  CA  ASN B 326      18.646  56.999  95.981  1.00 34.04           C  
-ATOM   3629  C   ASN B 326      18.067  58.055  95.035  1.00 33.55           C  
-ATOM   3630  O   ASN B 326      18.763  58.556  94.148  1.00 33.80           O  
-ATOM   3631  CB  ASN B 326      19.932  57.489  96.663  1.00 33.84           C  
-ATOM   3632  CG  ASN B 326      19.693  58.602  97.670  1.00 34.02           C  
-ATOM   3633  OD1 ASN B 326      19.324  59.722  97.312  1.00 32.87           O  
-ATOM   3634  ND2 ASN B 326      19.930  58.302  98.943  1.00 35.01           N  
-ATOM   3635  N   CYS B 327      16.792  58.386  95.233  1.00 32.48           N  
-ATOM   3636  CA  CYS B 327      16.044  59.272  94.333  1.00 32.10           C  
-ATOM   3637  C   CYS B 327      16.659  60.664  94.163  1.00 30.61           C  
-ATOM   3638  O   CYS B 327      16.569  61.259  93.084  1.00 30.27           O  
-ATOM   3639  CB  CYS B 327      14.579  59.384  94.779  1.00 32.45           C  
-ATOM   3640  SG  CYS B 327      13.574  57.951  94.300  1.00 37.17           S  
-ATOM   3641  N   LYS B 328      17.290  61.161  95.225  1.00 29.03           N  
-ATOM   3642  CA  LYS B 328      17.973  62.448  95.211  1.00 27.72           C  
-ATOM   3643  C   LYS B 328      19.264  62.392  94.381  1.00 26.55           C  
-ATOM   3644  O   LYS B 328      19.624  63.367  93.716  1.00 25.91           O  
-ATOM   3645  CB  LYS B 328      18.279  62.915  96.640  1.00 27.97           C  
-ATOM   3646  CG  LYS B 328      17.051  63.301  97.472  1.00 29.54           C  
-ATOM   3647  CD  LYS B 328      17.445  64.153  98.688  1.00 32.47           C  
-ATOM   3648  CE  LYS B 328      17.194  63.428 100.013  1.00 35.23           C  
-ATOM   3649  NZ  LYS B 328      16.376  64.257 100.972  1.00 37.38           N  
-ATOM   3650  N   VAL B 329      19.958  61.254  94.438  1.00 25.32           N  
-ATOM   3651  CA  VAL B 329      21.162  61.031  93.632  1.00 23.71           C  
-ATOM   3652  C   VAL B 329      20.785  61.081  92.151  1.00 23.08           C  
-ATOM   3653  O   VAL B 329      21.390  61.804  91.377  1.00 22.38           O  
-ATOM   3654  CB  VAL B 329      21.823  59.672  93.971  1.00 23.96           C  
-ATOM   3655  CG1 VAL B 329      22.933  59.306  92.949  1.00 22.86           C  
-ATOM   3656  CG2 VAL B 329      22.376  59.690  95.394  1.00 23.21           C  
-ATOM   3657  N   GLU B 330      19.756  60.325  91.784  1.00 22.70           N  
-ATOM   3658  CA  GLU B 330      19.266  60.277  90.413  1.00 22.54           C  
-ATOM   3659  C   GLU B 330      18.844  61.646  89.889  1.00 22.24           C  
-ATOM   3660  O   GLU B 330      19.345  62.093  88.869  1.00 22.05           O  
-ATOM   3661  CB  GLU B 330      18.117  59.278  90.307  1.00 22.49           C  
-ATOM   3662  CG  GLU B 330      18.568  57.845  90.557  1.00 23.66           C  
-ATOM   3663  CD  GLU B 330      17.472  56.824  90.339  1.00 25.68           C  
-ATOM   3664  OE1 GLU B 330      16.437  57.160  89.722  1.00 29.65           O  
-ATOM   3665  OE2 GLU B 330      17.646  55.676  90.782  1.00 26.34           O  
-ATOM   3666  N   SER B 331      17.936  62.308  90.604  1.00 22.10           N  
-ATOM   3667  CA  SER B 331      17.481  63.650  90.255  1.00 21.95           C  
-ATOM   3668  C   SER B 331      18.630  64.660  90.154  1.00 21.85           C  
-ATOM   3669  O   SER B 331      18.687  65.442  89.202  1.00 21.65           O  
-ATOM   3670  CB  SER B 331      16.454  64.141  91.280  1.00 21.92           C  
-ATOM   3671  OG  SER B 331      15.195  63.534  91.086  1.00 22.73           O  
-ATOM   3672  N   LEU B 332      19.533  64.657  91.135  1.00 21.25           N  
-ATOM   3673  CA  LEU B 332      20.666  65.582  91.099  1.00 21.39           C  
-ATOM   3674  C   LEU B 332      21.603  65.325  89.921  1.00 21.35           C  
-ATOM   3675  O   LEU B 332      22.083  66.267  89.312  1.00 21.41           O  
-ATOM   3676  CB  LEU B 332      21.467  65.566  92.409  1.00 21.25           C  
-ATOM   3677  CG  LEU B 332      22.575  66.609  92.535  1.00 19.80           C  
-ATOM   3678  CD1 LEU B 332      22.034  68.025  92.389  1.00 20.31           C  
-ATOM   3679  CD2 LEU B 332      23.277  66.446  93.886  1.00 20.54           C  
-ATOM   3680  N   ALA B 333      21.864  64.060  89.614  1.00 21.48           N  
-ATOM   3681  CA  ALA B 333      22.691  63.720  88.451  1.00 22.07           C  
-ATOM   3682  C   ALA B 333      22.056  64.242  87.156  1.00 22.37           C  
-ATOM   3683  O   ALA B 333      22.743  64.856  86.330  1.00 22.14           O  
-ATOM   3684  CB  ALA B 333      22.945  62.222  88.383  1.00 21.50           C  
-ATOM   3685  N   MET B 334      20.742  64.044  87.014  1.00 22.98           N  
-ATOM   3686  CA  MET B 334      19.980  64.594  85.879  1.00 24.13           C  
-ATOM   3687  C   MET B 334      20.027  66.116  85.834  1.00 23.69           C  
-ATOM   3688  O   MET B 334      20.180  66.719  84.757  1.00 23.04           O  
-ATOM   3689  CB  MET B 334      18.520  64.131  85.918  1.00 25.07           C  
-ATOM   3690  CG  MET B 334      18.266  62.795  85.239  1.00 29.65           C  
-ATOM   3691  SD  MET B 334      16.772  61.991  85.869  1.00 41.61           S  
-ATOM   3692  CE  MET B 334      15.496  63.203  85.473  1.00 40.50           C  
-ATOM   3693  N   PHE B 335      19.890  66.738  87.007  1.00 23.26           N  
-ATOM   3694  CA  PHE B 335      20.049  68.183  87.135  1.00 22.80           C  
-ATOM   3695  C   PHE B 335      21.390  68.632  86.566  1.00 22.77           C  
-ATOM   3696  O   PHE B 335      21.434  69.530  85.728  1.00 23.14           O  
-ATOM   3697  CB  PHE B 335      19.915  68.609  88.608  1.00 23.16           C  
-ATOM   3698  CG  PHE B 335      20.260  70.056  88.872  1.00 22.89           C  
-ATOM   3699  CD1 PHE B 335      19.566  71.084  88.242  1.00 22.24           C  
-ATOM   3700  CD2 PHE B 335      21.269  70.385  89.773  1.00 23.94           C  
-ATOM   3701  CE1 PHE B 335      19.875  72.416  88.495  1.00 22.59           C  
-ATOM   3702  CE2 PHE B 335      21.586  71.717  90.043  1.00 23.31           C  
-ATOM   3703  CZ  PHE B 335      20.885  72.737  89.393  1.00 24.34           C  
-ATOM   3704  N   LEU B 336      22.477  67.993  87.005  1.00 22.35           N  
-ATOM   3705  CA  LEU B 336      23.822  68.373  86.558  1.00 22.00           C  
-ATOM   3706  C   LEU B 336      24.056  68.101  85.076  1.00 21.69           C  
-ATOM   3707  O   LEU B 336      24.607  68.945  84.369  1.00 21.59           O  
-ATOM   3708  CB  LEU B 336      24.903  67.697  87.413  1.00 21.82           C  
-ATOM   3709  CG  LEU B 336      24.803  67.956  88.928  1.00 21.99           C  
-ATOM   3710  CD1 LEU B 336      25.640  66.956  89.695  1.00 19.92           C  
-ATOM   3711  CD2 LEU B 336      25.196  69.395  89.290  1.00 21.70           C  
-ATOM   3712  N   GLY B 337      23.632  66.926  84.609  1.00 21.68           N  
-ATOM   3713  CA  GLY B 337      23.703  66.601  83.189  1.00 21.38           C  
-ATOM   3714  C   GLY B 337      22.972  67.639  82.357  1.00 21.09           C  
-ATOM   3715  O   GLY B 337      23.427  68.025  81.283  1.00 21.16           O  
-ATOM   3716  N   GLU B 338      21.851  68.122  82.877  1.00 21.26           N  
-ATOM   3717  CA  GLU B 338      21.036  69.103  82.165  1.00 21.76           C  
-ATOM   3718  C   GLU B 338      21.712  70.473  82.085  1.00 21.98           C  
-ATOM   3719  O   GLU B 338      21.600  71.158  81.070  1.00 21.84           O  
-ATOM   3720  CB  GLU B 338      19.657  69.233  82.814  1.00 21.94           C  
-ATOM   3721  CG  GLU B 338      18.600  69.734  81.860  1.00 22.52           C  
-ATOM   3722  CD  GLU B 338      17.195  69.335  82.249  1.00 22.61           C  
-ATOM   3723  OE1 GLU B 338      16.949  68.143  82.523  1.00 22.37           O  
-ATOM   3724  OE2 GLU B 338      16.329  70.228  82.251  1.00 23.59           O  
-ATOM   3725  N   LEU B 339      22.409  70.861  83.156  1.00 22.10           N  
-ATOM   3726  CA  LEU B 339      23.159  72.113  83.189  1.00 22.47           C  
-ATOM   3727  C   LEU B 339      24.249  72.167  82.105  1.00 22.67           C  
-ATOM   3728  O   LEU B 339      24.526  73.227  81.539  1.00 22.32           O  
-ATOM   3729  CB  LEU B 339      23.779  72.326  84.585  1.00 22.70           C  
-ATOM   3730  CG  LEU B 339      22.872  72.834  85.718  1.00 23.11           C  
-ATOM   3731  CD1 LEU B 339      23.655  73.006  87.029  1.00 22.77           C  
-ATOM   3732  CD2 LEU B 339      22.159  74.141  85.345  1.00 21.04           C  
-ATOM   3733  N   SER B 340      24.854  71.012  81.822  1.00 22.98           N  
-ATOM   3734  CA  SER B 340      25.950  70.908  80.852  1.00 23.08           C  
-ATOM   3735  C   SER B 340      25.464  71.159  79.429  1.00 23.17           C  
-ATOM   3736  O   SER B 340      26.253  71.482  78.562  1.00 23.98           O  
-ATOM   3737  CB  SER B 340      26.625  69.536  80.940  1.00 22.99           C  
-ATOM   3738  OG  SER B 340      25.864  68.556  80.246  1.00 22.62           O  
-ATOM   3739  N   LEU B 341      24.161  71.021  79.205  1.00 23.10           N  
-ATOM   3740  CA  LEU B 341      23.549  71.348  77.922  1.00 22.92           C  
-ATOM   3741  C   LEU B 341      23.619  72.856  77.597  1.00 23.24           C  
-ATOM   3742  O   LEU B 341      23.630  73.240  76.421  1.00 23.09           O  
-ATOM   3743  CB  LEU B 341      22.091  70.889  77.898  1.00 22.35           C  
-ATOM   3744  CG  LEU B 341      21.754  69.407  78.105  1.00 23.03           C  
-ATOM   3745  CD1 LEU B 341      20.247  69.249  78.171  1.00 21.80           C  
-ATOM   3746  CD2 LEU B 341      22.330  68.524  76.991  1.00 22.05           C  
-ATOM   3747  N   ILE B 342      23.673  73.698  78.630  1.00 23.40           N  
-ATOM   3748  CA  ILE B 342      23.615  75.152  78.433  1.00 24.02           C  
-ATOM   3749  C   ILE B 342      24.905  75.763  77.893  1.00 24.15           C  
-ATOM   3750  O   ILE B 342      24.861  76.748  77.170  1.00 24.78           O  
-ATOM   3751  CB  ILE B 342      23.196  75.890  79.744  1.00 24.02           C  
-ATOM   3752  CG1 ILE B 342      21.852  75.371  80.274  1.00 23.51           C  
-ATOM   3753  CG2 ILE B 342      23.188  77.421  79.532  1.00 23.37           C  
-ATOM   3754  CD1 ILE B 342      20.613  75.916  79.565  1.00 23.10           C  
-ATOM   3755  N   ASP B 343      26.046  75.197  78.262  1.00 24.90           N  
-ATOM   3756  CA  ASP B 343      27.338  75.824  77.990  1.00 25.44           C  
-ATOM   3757  C   ASP B 343      28.187  75.007  77.001  1.00 25.59           C  
-ATOM   3758  O   ASP B 343      28.841  74.040  77.382  1.00 26.01           O  
-ATOM   3759  CB  ASP B 343      28.109  76.046  79.304  1.00 25.27           C  
-ATOM   3760  CG  ASP B 343      27.316  76.875  80.343  1.00 26.89           C  
-ATOM   3761  OD1 ASP B 343      26.851  77.992  80.024  1.00 27.53           O  
-ATOM   3762  OD2 ASP B 343      27.126  76.495  81.520  1.00 26.99           O  
-ATOM   3763  N   ALA B 344      28.181  75.405  75.732  1.00 26.14           N  
-ATOM   3764  CA  ALA B 344      28.988  74.733  74.697  1.00 25.98           C  
-ATOM   3765  C   ALA B 344      30.445  74.664  75.109  1.00 26.28           C  
-ATOM   3766  O   ALA B 344      31.122  73.652  74.924  1.00 25.87           O  
-ATOM   3767  CB  ALA B 344      28.861  75.458  73.382  1.00 26.12           C  
-ATOM   3768  N   ASP B 345      30.923  75.767  75.661  1.00 26.81           N  
-ATOM   3769  CA  ASP B 345      32.231  75.822  76.265  1.00 27.75           C  
-ATOM   3770  C   ASP B 345      31.991  75.660  77.765  1.00 27.66           C  
-ATOM   3771  O   ASP B 345      31.312  76.485  78.363  1.00 28.32           O  
-ATOM   3772  CB  ASP B 345      32.883  77.171  75.920  1.00 28.66           C  
-ATOM   3773  CG  ASP B 345      34.229  77.368  76.578  1.00 30.63           C  
-ATOM   3774  OD1 ASP B 345      34.811  76.392  77.095  1.00 33.22           O  
-ATOM   3775  OD2 ASP B 345      34.790  78.486  76.624  1.00 35.00           O  
-ATOM   3776  N   PRO B 346      32.527  74.605  78.378  1.00 27.43           N  
-ATOM   3777  CA  PRO B 346      33.384  73.616  77.708  1.00 26.96           C  
-ATOM   3778  C   PRO B 346      32.739  72.269  77.321  1.00 26.56           C  
-ATOM   3779  O   PRO B 346      33.471  71.418  76.843  1.00 27.00           O  
-ATOM   3780  CB  PRO B 346      34.430  73.350  78.778  1.00 26.91           C  
-ATOM   3781  CG  PRO B 346      33.647  73.473  80.072  1.00 27.81           C  
-ATOM   3782  CD  PRO B 346      32.398  74.314  79.813  1.00 27.20           C  
-ATOM   3783  N   TYR B 347      31.433  72.073  77.491  1.00 26.39           N  
-ATOM   3784  CA  TYR B 347      30.871  70.707  77.453  1.00 26.09           C  
-ATOM   3785  C   TYR B 347      30.807  70.014  76.093  1.00 26.28           C  
-ATOM   3786  O   TYR B 347      30.736  68.791  76.037  1.00 25.98           O  
-ATOM   3787  CB  TYR B 347      29.531  70.622  78.211  1.00 25.97           C  
-ATOM   3788  CG  TYR B 347      29.752  70.940  79.659  1.00 24.24           C  
-ATOM   3789  CD1 TYR B 347      30.428  70.043  80.487  1.00 22.98           C  
-ATOM   3790  CD2 TYR B 347      29.371  72.174  80.182  1.00 23.49           C  
-ATOM   3791  CE1 TYR B 347      30.682  70.349  81.823  1.00 23.69           C  
-ATOM   3792  CE2 TYR B 347      29.613  72.494  81.524  1.00 23.41           C  
-ATOM   3793  CZ  TYR B 347      30.268  71.578  82.327  1.00 23.37           C  
-ATOM   3794  OH  TYR B 347      30.519  71.889  83.627  1.00 25.22           O  
-ATOM   3795  N   LEU B 348      30.867  70.792  75.015  1.00 26.34           N  
-ATOM   3796  CA  LEU B 348      30.909  70.244  73.658  1.00 26.98           C  
-ATOM   3797  C   LEU B 348      32.054  69.264  73.443  1.00 26.65           C  
-ATOM   3798  O   LEU B 348      31.968  68.378  72.602  1.00 26.92           O  
-ATOM   3799  CB  LEU B 348      31.001  71.375  72.625  1.00 27.07           C  
-ATOM   3800  CG  LEU B 348      29.820  71.487  71.652  1.00 29.22           C  
-ATOM   3801  CD1 LEU B 348      28.483  71.179  72.343  1.00 29.50           C  
-ATOM   3802  CD2 LEU B 348      29.783  72.853  70.952  1.00 29.00           C  
-ATOM   3803  N   LYS B 349      33.127  69.426  74.205  1.00 26.59           N  
-ATOM   3804  CA  LYS B 349      34.293  68.574  74.048  1.00 26.46           C  
-ATOM   3805  C   LYS B 349      34.182  67.244  74.807  1.00 25.48           C  
-ATOM   3806  O   LYS B 349      35.004  66.353  74.619  1.00 25.26           O  
-ATOM   3807  CB  LYS B 349      35.565  69.343  74.420  1.00 27.06           C  
-ATOM   3808  CG  LYS B 349      35.824  69.505  75.905  1.00 29.64           C  
-ATOM   3809  CD  LYS B 349      37.182  70.176  76.123  1.00 32.26           C  
-ATOM   3810  CE  LYS B 349      37.282  70.799  77.496  1.00 34.53           C  
-ATOM   3811  NZ  LYS B 349      38.706  71.194  77.787  1.00 37.63           N  
-ATOM   3812  N   TYR B 350      33.160  67.104  75.647  1.00 24.36           N  
-ATOM   3813  CA  TYR B 350      32.943  65.843  76.339  1.00 23.70           C  
-ATOM   3814  C   TYR B 350      31.802  65.030  75.740  1.00 23.33           C  
-ATOM   3815  O   TYR B 350      30.759  65.579  75.343  1.00 23.07           O  
-ATOM   3816  CB  TYR B 350      32.702  66.067  77.832  1.00 23.83           C  
-ATOM   3817  CG  TYR B 350      33.793  66.841  78.532  1.00 23.37           C  
-ATOM   3818  CD1 TYR B 350      35.076  66.297  78.696  1.00 23.13           C  
-ATOM   3819  CD2 TYR B 350      33.542  68.117  79.044  1.00 22.71           C  
-ATOM   3820  CE1 TYR B 350      36.081  67.017  79.360  1.00 23.98           C  
-ATOM   3821  CE2 TYR B 350      34.540  68.844  79.701  1.00 22.59           C  
-ATOM   3822  CZ  TYR B 350      35.792  68.289  79.857  1.00 23.49           C  
-ATOM   3823  OH  TYR B 350      36.756  69.010  80.507  1.00 27.39           O  
-ATOM   3824  N   LEU B 351      32.012  63.717  75.679  1.00 22.78           N  
-ATOM   3825  CA  LEU B 351      30.992  62.791  75.193  1.00 22.14           C  
-ATOM   3826  C   LEU B 351      29.921  62.602  76.273  1.00 21.53           C  
-ATOM   3827  O   LEU B 351      30.211  62.748  77.475  1.00 21.09           O  
-ATOM   3828  CB  LEU B 351      31.614  61.435  74.835  1.00 22.62           C  
-ATOM   3829  CG  LEU B 351      32.516  61.314  73.590  1.00 23.09           C  
-ATOM   3830  CD1 LEU B 351      33.296  60.008  73.641  1.00 23.62           C  
-ATOM   3831  CD2 LEU B 351      31.716  61.405  72.291  1.00 22.30           C  
-ATOM   3832  N   PRO B 352      28.691  62.306  75.843  1.00 20.60           N  
-ATOM   3833  CA  PRO B 352      27.583  62.018  76.765  1.00 19.97           C  
-ATOM   3834  C   PRO B 352      27.942  61.062  77.893  1.00 19.34           C  
-ATOM   3835  O   PRO B 352      27.546  61.343  79.028  1.00 19.24           O  
-ATOM   3836  CB  PRO B 352      26.524  61.388  75.850  1.00 20.07           C  
-ATOM   3837  CG  PRO B 352      26.756  62.052  74.506  1.00 20.13           C  
-ATOM   3838  CD  PRO B 352      28.252  62.268  74.433  1.00 20.35           C  
-ATOM   3839  N   SER B 353      28.672  59.980  77.605  1.00 18.49           N  
-ATOM   3840  CA  SER B 353      28.986  58.967  78.617  1.00 18.29           C  
-ATOM   3841  C   SER B 353      29.921  59.517  79.676  1.00 18.04           C  
-ATOM   3842  O   SER B 353      29.873  59.093  80.833  1.00 18.34           O  
-ATOM   3843  CB  SER B 353      29.634  57.731  77.995  1.00 18.45           C  
-ATOM   3844  OG  SER B 353      30.821  58.083  77.293  1.00 18.71           O  
-ATOM   3845  N   VAL B 354      30.785  60.437  79.264  1.00 17.68           N  
-ATOM   3846  CA  VAL B 354      31.714  61.089  80.173  1.00 17.51           C  
-ATOM   3847  C   VAL B 354      31.001  62.134  81.039  1.00 17.73           C  
-ATOM   3848  O   VAL B 354      31.222  62.183  82.239  1.00 18.31           O  
-ATOM   3849  CB  VAL B 354      32.911  61.700  79.423  1.00 17.75           C  
-ATOM   3850  CG1 VAL B 354      33.691  62.687  80.325  1.00 15.96           C  
-ATOM   3851  CG2 VAL B 354      33.826  60.578  78.893  1.00 16.18           C  
-ATOM   3852  N   ILE B 355      30.145  62.957  80.446  1.00 18.09           N  
-ATOM   3853  CA  ILE B 355      29.360  63.915  81.238  1.00 18.30           C  
-ATOM   3854  C   ILE B 355      28.503  63.185  82.260  1.00 19.01           C  
-ATOM   3855  O   ILE B 355      28.460  63.571  83.447  1.00 20.23           O  
-ATOM   3856  CB  ILE B 355      28.492  64.826  80.338  1.00 18.41           C  
-ATOM   3857  CG1 ILE B 355      29.392  65.667  79.427  1.00 17.20           C  
-ATOM   3858  CG2 ILE B 355      27.556  65.710  81.197  1.00 16.64           C  
-ATOM   3859  CD1 ILE B 355      28.645  66.446  78.348  1.00 16.84           C  
-ATOM   3860  N   ALA B 356      27.859  62.106  81.816  1.00 18.60           N  
-ATOM   3861  CA  ALA B 356      27.032  61.290  82.697  1.00 18.41           C  
-ATOM   3862  C   ALA B 356      27.840  60.694  83.837  1.00 18.86           C  
-ATOM   3863  O   ALA B 356      27.346  60.595  84.959  1.00 18.61           O  
-ATOM   3864  CB  ALA B 356      26.311  60.188  81.915  1.00 17.58           C  
-ATOM   3865  N   GLY B 357      29.073  60.280  83.540  1.00 19.49           N  
-ATOM   3866  CA  GLY B 357      29.988  59.795  84.558  1.00 19.87           C  
-ATOM   3867  C   GLY B 357      30.289  60.853  85.614  1.00 20.12           C  
-ATOM   3868  O   GLY B 357      30.125  60.611  86.811  1.00 20.18           O  
-ATOM   3869  N   ALA B 358      30.705  62.035  85.172  1.00 20.23           N  
-ATOM   3870  CA  ALA B 358      30.956  63.142  86.094  1.00 20.89           C  
-ATOM   3871  C   ALA B 358      29.705  63.548  86.880  1.00 21.48           C  
-ATOM   3872  O   ALA B 358      29.779  63.780  88.089  1.00 21.77           O  
-ATOM   3873  CB  ALA B 358      31.537  64.340  85.352  1.00 20.49           C  
-ATOM   3874  N   ALA B 359      28.559  63.614  86.199  1.00 21.73           N  
-ATOM   3875  CA  ALA B 359      27.309  64.009  86.841  1.00 22.10           C  
-ATOM   3876  C   ALA B 359      26.889  63.008  87.898  1.00 22.51           C  
-ATOM   3877  O   ALA B 359      26.402  63.401  88.963  1.00 22.62           O  
-ATOM   3878  CB  ALA B 359      26.199  64.176  85.813  1.00 22.10           C  
-ATOM   3879  N   PHE B 360      27.048  61.719  87.592  1.00 22.34           N  
-ATOM   3880  CA  PHE B 360      26.687  60.672  88.541  1.00 22.69           C  
-ATOM   3881  C   PHE B 360      27.618  60.643  89.758  1.00 22.56           C  
-ATOM   3882  O   PHE B 360      27.137  60.541  90.882  1.00 22.46           O  
-ATOM   3883  CB  PHE B 360      26.602  59.283  87.890  1.00 22.52           C  
-ATOM   3884  CG  PHE B 360      26.180  58.195  88.851  1.00 23.44           C  
-ATOM   3885  CD1 PHE B 360      24.931  58.240  89.473  1.00 23.99           C  
-ATOM   3886  CD2 PHE B 360      27.035  57.152  89.156  1.00 22.00           C  
-ATOM   3887  CE1 PHE B 360      24.536  57.253  90.371  1.00 23.21           C  
-ATOM   3888  CE2 PHE B 360      26.660  56.166  90.053  1.00 23.99           C  
-ATOM   3889  CZ  PHE B 360      25.408  56.206  90.662  1.00 24.69           C  
-ATOM   3890  N   HIS B 361      28.933  60.729  89.547  1.00 22.54           N  
-ATOM   3891  CA  HIS B 361      29.855  60.774  90.689  1.00 22.44           C  
-ATOM   3892  C   HIS B 361      29.562  61.987  91.578  1.00 22.79           C  
-ATOM   3893  O   HIS B 361      29.415  61.849  92.798  1.00 22.17           O  
-ATOM   3894  CB  HIS B 361      31.328  60.797  90.277  1.00 22.26           C  
-ATOM   3895  CG  HIS B 361      32.237  61.220  91.388  1.00 21.73           C  
-ATOM   3896  ND1 HIS B 361      32.657  60.355  92.373  1.00 21.72           N  
-ATOM   3897  CD2 HIS B 361      32.751  62.433  91.710  1.00 22.81           C  
-ATOM   3898  CE1 HIS B 361      33.415  61.010  93.236  1.00 23.11           C  
-ATOM   3899  NE2 HIS B 361      33.489  62.273  92.855  1.00 21.86           N  
-ATOM   3900  N   LEU B 362      29.476  63.162  90.951  1.00 23.06           N  
-ATOM   3901  CA  LEU B 362      29.179  64.410  91.660  1.00 23.48           C  
-ATOM   3902  C   LEU B 362      27.874  64.323  92.468  1.00 23.69           C  
-ATOM   3903  O   LEU B 362      27.838  64.727  93.632  1.00 23.95           O  
-ATOM   3904  CB  LEU B 362      29.174  65.607  90.700  1.00 22.88           C  
-ATOM   3905  CG  LEU B 362      29.183  67.050  91.242  1.00 24.35           C  
-ATOM   3906  CD1 LEU B 362      30.265  67.301  92.322  1.00 23.66           C  
-ATOM   3907  CD2 LEU B 362      29.337  68.060  90.110  1.00 22.53           C  
-ATOM   3908  N   ALA B 363      26.825  63.767  91.866  1.00 23.72           N  
-ATOM   3909  CA  ALA B 363      25.535  63.626  92.549  1.00 24.11           C  
-ATOM   3910  C   ALA B 363      25.634  62.716  93.765  1.00 24.65           C  
-ATOM   3911  O   ALA B 363      25.153  63.054  94.862  1.00 24.24           O  
-ATOM   3912  CB  ALA B 363      24.481  63.107  91.596  1.00 23.49           C  
-ATOM   3913  N   LEU B 364      26.251  61.557  93.549  1.00 25.27           N  
-ATOM   3914  CA  LEU B 364      26.489  60.577  94.590  1.00 26.17           C  
-ATOM   3915  C   LEU B 364      27.299  61.166  95.743  1.00 26.44           C  
-ATOM   3916  O   LEU B 364      26.949  60.980  96.911  1.00 26.70           O  
-ATOM   3917  CB  LEU B 364      27.201  59.360  93.997  1.00 26.23           C  
-ATOM   3918  CG  LEU B 364      27.168  58.016  94.725  1.00 28.29           C  
-ATOM   3919  CD1 LEU B 364      25.755  57.497  94.947  1.00 29.21           C  
-ATOM   3920  CD2 LEU B 364      27.989  56.998  93.937  1.00 30.08           C  
-ATOM   3921  N   TYR B 365      28.371  61.875  95.409  1.00 26.56           N  
-ATOM   3922  CA  TYR B 365      29.238  62.488  96.408  1.00 27.32           C  
-ATOM   3923  C   TYR B 365      28.533  63.567  97.246  1.00 27.31           C  
-ATOM   3924  O   TYR B 365      28.637  63.570  98.473  1.00 27.60           O  
-ATOM   3925  CB  TYR B 365      30.498  63.060  95.754  1.00 27.43           C  
-ATOM   3926  CG  TYR B 365      31.514  63.542  96.757  1.00 28.60           C  
-ATOM   3927  CD1 TYR B 365      32.231  62.640  97.536  1.00 30.40           C  
-ATOM   3928  CD2 TYR B 365      31.754  64.898  96.930  1.00 29.85           C  
-ATOM   3929  CE1 TYR B 365      33.157  63.079  98.478  1.00 32.00           C  
-ATOM   3930  CE2 TYR B 365      32.674  65.345  97.857  1.00 32.19           C  
-ATOM   3931  CZ  TYR B 365      33.377  64.428  98.625  1.00 33.15           C  
-ATOM   3932  OH  TYR B 365      34.301  64.870  99.549  1.00 37.44           O  
-ATOM   3933  N   THR B 366      27.822  64.464  96.570  1.00 26.87           N  
-ATOM   3934  CA  THR B 366      27.046  65.517  97.215  1.00 26.76           C  
-ATOM   3935  C   THR B 366      26.045  64.966  98.237  1.00 27.52           C  
-ATOM   3936  O   THR B 366      25.954  65.469  99.347  1.00 27.41           O  
-ATOM   3937  CB  THR B 366      26.297  66.319  96.133  1.00 26.64           C  
-ATOM   3938  OG1 THR B 366      27.250  66.886  95.229  1.00 25.30           O  
-ATOM   3939  CG2 THR B 366      25.568  67.543  96.723  1.00 26.08           C  
-ATOM   3940  N   VAL B 367      25.297  63.938  97.844  1.00 28.13           N  
-ATOM   3941  CA  VAL B 367      24.179  63.443  98.634  1.00 28.61           C  
-ATOM   3942  C   VAL B 367      24.626  62.453  99.724  1.00 29.13           C  
-ATOM   3943  O   VAL B 367      24.224  62.589 100.887  1.00 28.99           O  
-ATOM   3944  CB  VAL B 367      23.077  62.815  97.733  1.00 28.34           C  
-ATOM   3945  CG1 VAL B 367      21.923  62.280  98.565  1.00 29.10           C  
-ATOM   3946  CG2 VAL B 367      22.554  63.836  96.739  1.00 28.34           C  
-ATOM   3947  N   THR B 368      25.453  61.477  99.343  1.00 29.36           N  
-ATOM   3948  CA  THR B 368      25.791  60.345 100.216  1.00 29.88           C  
-ATOM   3949  C   THR B 368      27.256  60.280 100.654  1.00 30.29           C  
-ATOM   3950  O   THR B 368      27.603  59.486 101.527  1.00 30.56           O  
-ATOM   3951  CB  THR B 368      25.445  59.010  99.528  1.00 29.71           C  
-ATOM   3952  OG1 THR B 368      26.352  58.793  98.438  1.00 29.85           O  
-ATOM   3953  CG2 THR B 368      24.073  59.057  98.872  1.00 29.68           C  
-ATOM   3954  N   GLY B 369      28.115  61.084 100.038  1.00 30.72           N  
-ATOM   3955  CA  GLY B 369      29.537  61.016 100.324  1.00 31.32           C  
-ATOM   3956  C   GLY B 369      30.271  59.870  99.639  1.00 31.81           C  
-ATOM   3957  O   GLY B 369      31.493  59.764  99.767  1.00 32.10           O  
-ATOM   3958  N   GLN B 370      29.543  59.014  98.921  1.00 31.95           N  
-ATOM   3959  CA  GLN B 370      30.148  57.895  98.194  1.00 32.04           C  
-ATOM   3960  C   GLN B 370      30.803  58.381  96.903  1.00 31.33           C  
-ATOM   3961  O   GLN B 370      30.662  59.546  96.527  1.00 31.08           O  
-ATOM   3962  CB  GLN B 370      29.110  56.812  97.856  1.00 32.32           C  
-ATOM   3963  CG  GLN B 370      28.228  56.332  98.998  1.00 35.02           C  
-ATOM   3964  CD  GLN B 370      27.125  55.397  98.503  1.00 38.56           C  
-ATOM   3965  OE1 GLN B 370      27.408  54.282  98.063  1.00 41.49           O  
-ATOM   3966  NE2 GLN B 370      25.876  55.856  98.552  1.00 39.45           N  
-ATOM   3967  N   SER B 371      31.498  57.478  96.217  1.00 30.81           N  
-ATOM   3968  CA  SER B 371      32.223  57.831  94.994  1.00 30.63           C  
-ATOM   3969  C   SER B 371      31.922  56.884  93.834  1.00 29.83           C  
-ATOM   3970  O   SER B 371      31.386  55.798  94.048  1.00 29.67           O  
-ATOM   3971  CB  SER B 371      33.723  57.867  95.276  1.00 31.01           C  
-ATOM   3972  OG  SER B 371      34.416  58.506  94.220  1.00 33.25           O  
-ATOM   3973  N   TRP B 372      32.243  57.319  92.609  1.00 29.25           N  
-ATOM   3974  CA  TRP B 372      32.158  56.492  91.391  1.00 28.13           C  
-ATOM   3975  C   TRP B 372      32.482  55.032  91.702  1.00 28.31           C  
-ATOM   3976  O   TRP B 372      33.616  54.702  92.068  1.00 28.12           O  
-ATOM   3977  CB  TRP B 372      33.128  57.032  90.338  1.00 27.67           C  
-ATOM   3978  CG  TRP B 372      33.107  56.353  88.996  1.00 25.51           C  
-ATOM   3979  CD1 TRP B 372      34.081  55.554  88.467  1.00 25.23           C  
-ATOM   3980  CD2 TRP B 372      32.088  56.454  87.990  1.00 23.08           C  
-ATOM   3981  NE1 TRP B 372      33.722  55.135  87.206  1.00 23.81           N  
-ATOM   3982  CE2 TRP B 372      32.507  55.680  86.886  1.00 22.25           C  
-ATOM   3983  CE3 TRP B 372      30.856  57.126  87.908  1.00 21.13           C  
-ATOM   3984  CZ2 TRP B 372      31.743  55.554  85.723  1.00 22.06           C  
-ATOM   3985  CZ3 TRP B 372      30.098  56.999  86.744  1.00 19.84           C  
-ATOM   3986  CH2 TRP B 372      30.541  56.217  85.675  1.00 20.20           C  
-ATOM   3987  N   PRO B 373      31.475  54.168  91.590  1.00 28.19           N  
-ATOM   3988  CA  PRO B 373      31.601  52.778  92.028  1.00 28.10           C  
-ATOM   3989  C   PRO B 373      32.469  51.910  91.129  1.00 28.12           C  
-ATOM   3990  O   PRO B 373      32.560  52.109  89.915  1.00 28.37           O  
-ATOM   3991  CB  PRO B 373      30.158  52.268  92.018  1.00 27.77           C  
-ATOM   3992  CG  PRO B 373      29.465  53.108  91.048  1.00 28.18           C  
-ATOM   3993  CD  PRO B 373      30.131  54.463  91.059  1.00 28.21           C  
-ATOM   3994  N   GLU B 374      33.084  50.928  91.769  1.00 27.95           N  
-ATOM   3995  CA  GLU B 374      33.943  49.951  91.129  1.00 28.15           C  
-ATOM   3996  C   GLU B 374      33.241  49.258  89.970  1.00 26.74           C  
-ATOM   3997  O   GLU B 374      33.830  49.044  88.910  1.00 26.43           O  
-ATOM   3998  CB  GLU B 374      34.398  48.931  92.182  1.00 28.69           C  
-ATOM   3999  CG  GLU B 374      34.590  47.509  91.676  1.00 33.21           C  
-ATOM   4000  CD  GLU B 374      35.759  47.396  90.724  1.00 37.86           C  
-ATOM   4001  OE1 GLU B 374      36.541  48.375  90.616  1.00 41.00           O  
-ATOM   4002  OE2 GLU B 374      35.887  46.341  90.075  1.00 39.04           O  
-ATOM   4003  N   SER B 375      31.973  48.924  90.183  1.00 25.42           N  
-ATOM   4004  CA  SER B 375      31.175  48.226  89.192  1.00 24.04           C  
-ATOM   4005  C   SER B 375      31.024  49.023  87.878  1.00 23.23           C  
-ATOM   4006  O   SER B 375      30.856  48.429  86.815  1.00 22.90           O  
-ATOM   4007  CB  SER B 375      29.811  47.849  89.784  1.00 23.70           C  
-ATOM   4008  OG  SER B 375      29.026  49.004  90.033  1.00 23.43           O  
-ATOM   4009  N   LEU B 376      31.097  50.350  87.957  1.00 22.39           N  
-ATOM   4010  CA  LEU B 376      30.995  51.199  86.767  1.00 21.96           C  
-ATOM   4011  C   LEU B 376      32.348  51.404  86.078  1.00 22.19           C  
-ATOM   4012  O   LEU B 376      32.405  51.730  84.881  1.00 22.52           O  
-ATOM   4013  CB  LEU B 376      30.322  52.541  87.088  1.00 21.55           C  
-ATOM   4014  CG  LEU B 376      28.796  52.486  87.251  1.00 20.89           C  
-ATOM   4015  CD1 LEU B 376      28.224  53.790  87.821  1.00 19.88           C  
-ATOM   4016  CD2 LEU B 376      28.132  52.154  85.930  1.00 17.99           C  
-ATOM   4017  N   ILE B 377      33.436  51.208  86.816  1.00 22.10           N  
-ATOM   4018  CA  ILE B 377      34.754  51.130  86.180  1.00 22.01           C  
-ATOM   4019  C   ILE B 377      34.768  49.886  85.305  1.00 22.01           C  
-ATOM   4020  O   ILE B 377      35.174  49.939  84.134  1.00 21.85           O  
-ATOM   4021  CB  ILE B 377      35.912  51.094  87.218  1.00 21.86           C  
-ATOM   4022  CG1 ILE B 377      35.896  52.357  88.073  1.00 21.90           C  
-ATOM   4023  CG2 ILE B 377      37.267  50.983  86.500  1.00 21.91           C  
-ATOM   4024  CD1 ILE B 377      36.592  52.205  89.436  1.00 24.60           C  
-ATOM   4025  N   ARG B 378      34.296  48.773  85.856  1.00 21.96           N  
-ATOM   4026  CA  ARG B 378      34.243  47.536  85.086  1.00 22.91           C  
-ATOM   4027  C   ARG B 378      33.386  47.713  83.826  1.00 22.30           C  
-ATOM   4028  O   ARG B 378      33.811  47.322  82.745  1.00 22.82           O  
-ATOM   4029  CB  ARG B 378      33.737  46.367  85.936  1.00 23.34           C  
-ATOM   4030  CG  ARG B 378      34.751  45.872  86.967  1.00 26.83           C  
-ATOM   4031  CD  ARG B 378      34.309  44.622  87.720  1.00 30.62           C  
-ATOM   4032  NE  ARG B 378      33.360  44.925  88.788  1.00 34.31           N  
-ATOM   4033  CZ  ARG B 378      32.184  44.321  88.960  1.00 36.50           C  
-ATOM   4034  NH1 ARG B 378      31.782  43.368  88.123  1.00 36.87           N  
-ATOM   4035  NH2 ARG B 378      31.400  44.676  89.974  1.00 36.16           N  
-ATOM   4036  N   LYS B 379      32.212  48.334  83.973  1.00 21.40           N  
-ATOM   4037  CA  LYS B 379      31.265  48.538  82.865  1.00 20.82           C  
-ATOM   4038  C   LYS B 379      31.770  49.526  81.818  1.00 20.29           C  
-ATOM   4039  O   LYS B 379      31.709  49.249  80.620  1.00 20.02           O  
-ATOM   4040  CB  LYS B 379      29.902  49.010  83.404  1.00 20.69           C  
-ATOM   4041  CG  LYS B 379      28.822  49.279  82.339  1.00 21.80           C  
-ATOM   4042  CD  LYS B 379      27.615  50.042  82.926  1.00 23.03           C  
-ATOM   4043  CE  LYS B 379      26.469  50.200  81.919  1.00 23.07           C  
-ATOM   4044  NZ  LYS B 379      25.923  48.873  81.456  1.00 20.85           N  
-ATOM   4045  N   THR B 380      32.244  50.685  82.271  1.00 20.06           N  
-ATOM   4046  CA  THR B 380      32.562  51.779  81.356  1.00 20.23           C  
-ATOM   4047  C   THR B 380      34.045  51.887  81.045  1.00 20.15           C  
-ATOM   4048  O   THR B 380      34.408  52.458  80.014  1.00 20.13           O  
-ATOM   4049  CB  THR B 380      32.090  53.157  81.894  1.00 19.99           C  
-ATOM   4050  OG1 THR B 380      32.938  53.555  82.987  1.00 21.46           O  
-ATOM   4051  CG2 THR B 380      30.690  53.086  82.504  1.00 18.98           C  
-ATOM   4052  N   GLY B 381      34.895  51.395  81.948  1.00 19.84           N  
-ATOM   4053  CA  GLY B 381      36.335  51.602  81.810  1.00 20.19           C  
-ATOM   4054  C   GLY B 381      36.771  53.004  82.228  1.00 20.27           C  
-ATOM   4055  O   GLY B 381      37.949  53.346  82.123  1.00 20.58           O  
-ATOM   4056  N   TYR B 382      35.824  53.823  82.683  1.00 20.10           N  
-ATOM   4057  CA  TYR B 382      36.149  55.155  83.186  1.00 20.42           C  
-ATOM   4058  C   TYR B 382      36.518  55.061  84.656  1.00 21.02           C  
-ATOM   4059  O   TYR B 382      35.895  54.316  85.404  1.00 20.55           O  
-ATOM   4060  CB  TYR B 382      34.972  56.128  83.034  1.00 19.75           C  
-ATOM   4061  CG  TYR B 382      34.540  56.421  81.614  1.00 19.66           C  
-ATOM   4062  CD1 TYR B 382      35.464  56.464  80.565  1.00 19.44           C  
-ATOM   4063  CD2 TYR B 382      33.197  56.675  81.318  1.00 19.75           C  
-ATOM   4064  CE1 TYR B 382      35.051  56.743  79.256  1.00 20.10           C  
-ATOM   4065  CE2 TYR B 382      32.781  56.950  80.022  1.00 19.41           C  
-ATOM   4066  CZ  TYR B 382      33.710  56.977  78.996  1.00 20.43           C  
-ATOM   4067  OH  TYR B 382      33.296  57.252  77.712  1.00 21.78           O  
-ATOM   4068  N   THR B 383      37.525  55.827  85.063  1.00 22.23           N  
-ATOM   4069  CA  THR B 383      37.861  55.966  86.479  1.00 23.71           C  
-ATOM   4070  C   THR B 383      37.688  57.426  86.859  1.00 25.11           C  
-ATOM   4071  O   THR B 383      37.496  58.282  85.992  1.00 25.23           O  
-ATOM   4072  CB  THR B 383      39.327  55.526  86.771  1.00 23.74           C  
-ATOM   4073  OG1 THR B 383      40.229  56.293  85.966  1.00 23.11           O  
-ATOM   4074  CG2 THR B 383      39.590  54.060  86.339  1.00 23.34           C  
-ATOM   4075  N   LEU B 384      37.782  57.712  88.155  1.00 26.88           N  
-ATOM   4076  CA  LEU B 384      37.768  59.088  88.638  1.00 28.40           C  
-ATOM   4077  C   LEU B 384      38.840  59.913  87.942  1.00 29.37           C  
-ATOM   4078  O   LEU B 384      38.650  61.105  87.690  1.00 29.99           O  
-ATOM   4079  CB  LEU B 384      37.975  59.121  90.154  1.00 28.55           C  
-ATOM   4080  CG  LEU B 384      36.914  59.784  91.039  1.00 29.31           C  
-ATOM   4081  CD1 LEU B 384      35.527  59.869  90.373  1.00 29.12           C  
-ATOM   4082  CD2 LEU B 384      36.832  59.030  92.350  1.00 29.22           C  
-ATOM   4083  N   GLU B 385      39.957  59.264  87.614  1.00 30.24           N  
-ATOM   4084  CA  GLU B 385      41.052  59.912  86.901  1.00 31.14           C  
-ATOM   4085  C   GLU B 385      40.688  60.333  85.476  1.00 30.74           C  
-ATOM   4086  O   GLU B 385      40.999  61.454  85.057  1.00 31.40           O  
-ATOM   4087  CB  GLU B 385      42.298  59.017  86.897  1.00 31.54           C  
-ATOM   4088  CG  GLU B 385      43.574  59.725  86.476  1.00 35.97           C  
-ATOM   4089  CD  GLU B 385      43.991  60.835  87.430  1.00 41.83           C  
-ATOM   4090  OE1 GLU B 385      43.395  61.935  87.374  1.00 44.64           O  
-ATOM   4091  OE2 GLU B 385      44.925  60.618  88.231  1.00 45.76           O  
-ATOM   4092  N   SER B 386      40.047  59.442  84.724  1.00 30.01           N  
-ATOM   4093  CA  SER B 386      39.637  59.777  83.361  1.00 29.21           C  
-ATOM   4094  C   SER B 386      38.503  60.801  83.329  1.00 28.68           C  
-ATOM   4095  O   SER B 386      38.406  61.575  82.377  1.00 28.83           O  
-ATOM   4096  CB  SER B 386      39.254  58.523  82.571  1.00 29.05           C  
-ATOM   4097  OG  SER B 386      38.057  57.958  83.059  1.00 28.96           O  
-ATOM   4098  N   LEU B 387      37.654  60.794  84.361  1.00 27.94           N  
-ATOM   4099  CA  LEU B 387      36.528  61.742  84.481  1.00 27.38           C  
-ATOM   4100  C   LEU B 387      36.920  63.098  85.088  1.00 27.41           C  
-ATOM   4101  O   LEU B 387      36.172  64.078  84.974  1.00 27.48           O  
-ATOM   4102  CB  LEU B 387      35.396  61.141  85.327  1.00 26.63           C  
-ATOM   4103  CG  LEU B 387      34.742  59.832  84.882  1.00 25.35           C  
-ATOM   4104  CD1 LEU B 387      33.833  59.286  85.987  1.00 23.98           C  
-ATOM   4105  CD2 LEU B 387      33.978  60.036  83.578  1.00 20.94           C  
-ATOM   4106  N   LYS B 388      38.077  63.143  85.742  1.00 27.51           N  
-ATOM   4107  CA  LYS B 388      38.540  64.344  86.445  1.00 27.79           C  
-ATOM   4108  C   LYS B 388      38.310  65.658  85.694  1.00 27.08           C  
-ATOM   4109  O   LYS B 388      37.644  66.537  86.235  1.00 27.11           O  
-ATOM   4110  CB  LYS B 388      40.008  64.207  86.881  1.00 28.43           C  
-ATOM   4111  CG  LYS B 388      40.436  65.220  87.927  1.00 30.96           C  
-ATOM   4112  CD  LYS B 388      41.899  65.043  88.299  1.00 35.89           C  
-ATOM   4113  CE  LYS B 388      42.415  66.240  89.095  1.00 38.56           C  
-ATOM   4114  NZ  LYS B 388      43.921  66.313  89.091  1.00 41.75           N  
-ATOM   4115  N   PRO B 389      38.844  65.815  84.477  1.00 26.45           N  
-ATOM   4116  CA  PRO B 389      38.653  67.071  83.732  1.00 26.17           C  
-ATOM   4117  C   PRO B 389      37.190  67.505  83.603  1.00 26.00           C  
-ATOM   4118  O   PRO B 389      36.890  68.670  83.883  1.00 26.07           O  
-ATOM   4119  CB  PRO B 389      39.268  66.793  82.347  1.00 25.95           C  
-ATOM   4120  CG  PRO B 389      39.900  65.452  82.411  1.00 26.24           C  
-ATOM   4121  CD  PRO B 389      39.702  64.862  83.750  1.00 26.36           C  
-ATOM   4122  N   CYS B 390      36.302  66.599  83.189  1.00 25.77           N  
-ATOM   4123  CA  CYS B 390      34.869  66.907  83.123  1.00 25.70           C  
-ATOM   4124  C   CYS B 390      34.313  67.217  84.519  1.00 25.84           C  
-ATOM   4125  O   CYS B 390      33.582  68.193  84.703  1.00 25.70           O  
-ATOM   4126  CB  CYS B 390      34.087  65.750  82.494  1.00 25.48           C  
-ATOM   4127  SG  CYS B 390      32.376  66.172  82.116  1.00 25.76           S  
-ATOM   4128  N   LEU B 391      34.686  66.391  85.493  1.00 26.19           N  
-ATOM   4129  CA  LEU B 391      34.273  66.593  86.879  1.00 27.49           C  
-ATOM   4130  C   LEU B 391      34.701  67.956  87.421  1.00 27.57           C  
-ATOM   4131  O   LEU B 391      33.896  68.657  88.045  1.00 27.35           O  
-ATOM   4132  CB  LEU B 391      34.774  65.449  87.774  1.00 27.47           C  
-ATOM   4133  CG  LEU B 391      34.118  65.309  89.153  1.00 29.52           C  
-ATOM   4134  CD1 LEU B 391      32.606  65.059  89.098  1.00 29.17           C  
-ATOM   4135  CD2 LEU B 391      34.803  64.201  89.924  1.00 31.04           C  
-ATOM   4136  N   MET B 392      35.947  68.346  87.144  1.00 28.12           N  
-ATOM   4137  CA  MET B 392      36.443  69.674  87.499  1.00 28.93           C  
-ATOM   4138  C   MET B 392      35.585  70.782  86.903  1.00 28.53           C  
-ATOM   4139  O   MET B 392      35.319  71.781  87.564  1.00 28.95           O  
-ATOM   4140  CB  MET B 392      37.898  69.855  87.050  1.00 29.76           C  
-ATOM   4141  CG  MET B 392      38.903  69.044  87.833  1.00 32.31           C  
-ATOM   4142  SD  MET B 392      38.738  69.320  89.574  1.00 41.08           S  
-ATOM   4143  CE  MET B 392      38.513  67.676  90.149  1.00 39.68           C  
-ATOM   4144  N   ASP B 393      35.178  70.613  85.646  1.00 28.41           N  
-ATOM   4145  CA  ASP B 393      34.316  71.576  84.967  1.00 27.99           C  
-ATOM   4146  C   ASP B 393      32.908  71.560  85.558  1.00 27.41           C  
-ATOM   4147  O   ASP B 393      32.333  72.610  85.820  1.00 27.28           O  
-ATOM   4148  CB  ASP B 393      34.235  71.269  83.464  1.00 28.45           C  
-ATOM   4149  CG  ASP B 393      35.431  71.796  82.676  1.00 30.11           C  
-ATOM   4150  OD1 ASP B 393      36.074  72.789  83.096  1.00 32.31           O  
-ATOM   4151  OD2 ASP B 393      35.787  71.279  81.600  1.00 30.30           O  
-ATOM   4152  N   LEU B 394      32.350  70.365  85.745  1.00 26.92           N  
-ATOM   4153  CA  LEU B 394      30.986  70.226  86.258  1.00 26.56           C  
-ATOM   4154  C   LEU B 394      30.845  70.791  87.673  1.00 26.52           C  
-ATOM   4155  O   LEU B 394      29.864  71.472  87.978  1.00 25.49           O  
-ATOM   4156  CB  LEU B 394      30.504  68.770  86.210  1.00 25.97           C  
-ATOM   4157  CG  LEU B 394      28.975  68.589  86.133  1.00 25.47           C  
-ATOM   4158  CD1 LEU B 394      28.363  69.319  84.938  1.00 24.58           C  
-ATOM   4159  CD2 LEU B 394      28.615  67.125  86.066  1.00 24.40           C  
-ATOM   4160  N   HIS B 395      31.834  70.503  88.517  1.00 26.79           N  
-ATOM   4161  CA  HIS B 395      31.878  71.026  89.880  1.00 27.51           C  
-ATOM   4162  C   HIS B 395      31.854  72.564  89.894  1.00 27.67           C  
-ATOM   4163  O   HIS B 395      31.129  73.159  90.691  1.00 27.77           O  
-ATOM   4164  CB  HIS B 395      33.108  70.483  90.596  1.00 27.69           C  
-ATOM   4165  CG  HIS B 395      33.285  70.990  91.994  1.00 29.11           C  
-ATOM   4166  ND1 HIS B 395      32.247  71.080  92.899  1.00 30.22           N  
-ATOM   4167  CD2 HIS B 395      34.396  71.392  92.655  1.00 30.24           C  
-ATOM   4168  CE1 HIS B 395      32.712  71.533  94.051  1.00 30.76           C  
-ATOM   4169  NE2 HIS B 395      34.014  71.720  93.931  1.00 30.74           N  
-ATOM   4170  N   GLN B 396      32.616  73.202  89.003  1.00 27.66           N  
-ATOM   4171  CA  GLN B 396      32.535  74.659  88.853  1.00 28.29           C  
-ATOM   4172  C   GLN B 396      31.139  75.103  88.437  1.00 28.00           C  
-ATOM   4173  O   GLN B 396      30.586  76.028  89.034  1.00 28.63           O  
-ATOM   4174  CB  GLN B 396      33.568  75.207  87.855  1.00 28.50           C  
-ATOM   4175  CG  GLN B 396      35.005  75.332  88.393  1.00 31.41           C  
-ATOM   4176  CD  GLN B 396      35.099  76.005  89.760  1.00 34.87           C  
-ATOM   4177  OE1 GLN B 396      35.644  75.424  90.711  1.00 36.27           O  
-ATOM   4178  NE2 GLN B 396      34.574  77.228  89.864  1.00 36.29           N  
-ATOM   4179  N   THR B 397      30.566  74.449  87.424  1.00 27.37           N  
-ATOM   4180  CA  THR B 397      29.246  74.832  86.919  1.00 26.93           C  
-ATOM   4181  C   THR B 397      28.218  74.748  88.038  1.00 26.75           C  
-ATOM   4182  O   THR B 397      27.403  75.652  88.221  1.00 26.73           O  
-ATOM   4183  CB  THR B 397      28.825  73.928  85.735  1.00 27.18           C  
-ATOM   4184  OG1 THR B 397      29.696  74.160  84.620  1.00 26.60           O  
-ATOM   4185  CG2 THR B 397      27.439  74.311  85.222  1.00 26.00           C  
-ATOM   4186  N   TYR B 398      28.278  73.651  88.777  1.00 26.42           N  
-ATOM   4187  CA  TYR B 398      27.469  73.443  89.965  1.00 26.75           C  
-ATOM   4188  C   TYR B 398      27.588  74.621  90.963  1.00 27.63           C  
-ATOM   4189  O   TYR B 398      26.578  75.260  91.288  1.00 27.23           O  
-ATOM   4190  CB  TYR B 398      27.885  72.134  90.625  1.00 25.94           C  
-ATOM   4191  CG  TYR B 398      26.911  71.592  91.633  1.00 24.32           C  
-ATOM   4192  CD1 TYR B 398      25.661  72.185  91.825  1.00 23.58           C  
-ATOM   4193  CD2 TYR B 398      27.234  70.478  92.391  1.00 23.01           C  
-ATOM   4194  CE1 TYR B 398      24.763  71.681  92.750  1.00 22.88           C  
-ATOM   4195  CE2 TYR B 398      26.338  69.959  93.310  1.00 23.55           C  
-ATOM   4196  CZ  TYR B 398      25.109  70.573  93.487  1.00 22.96           C  
-ATOM   4197  OH  TYR B 398      24.218  70.064  94.398  1.00 24.28           O  
-ATOM   4198  N   LEU B 399      28.816  74.918  91.407  1.00 28.37           N  
-ATOM   4199  CA  LEU B 399      29.074  75.984  92.387  1.00 29.60           C  
-ATOM   4200  C   LEU B 399      28.612  77.359  91.908  1.00 30.17           C  
-ATOM   4201  O   LEU B 399      28.197  78.193  92.712  1.00 30.45           O  
-ATOM   4202  CB  LEU B 399      30.558  76.047  92.766  1.00 29.78           C  
-ATOM   4203  CG  LEU B 399      31.148  75.033  93.756  1.00 30.77           C  
-ATOM   4204  CD1 LEU B 399      32.672  75.028  93.638  1.00 31.66           C  
-ATOM   4205  CD2 LEU B 399      30.742  75.323  95.190  1.00 31.08           C  
-ATOM   4206  N   LYS B 400      28.652  77.572  90.596  1.00 30.87           N  
-ATOM   4207  CA  LYS B 400      28.316  78.866  90.006  1.00 31.34           C  
-ATOM   4208  C   LYS B 400      26.899  78.939  89.451  1.00 31.31           C  
-ATOM   4209  O   LYS B 400      26.508  79.960  88.893  1.00 31.47           O  
-ATOM   4210  CB  LYS B 400      29.321  79.215  88.904  1.00 31.68           C  
-ATOM   4211  CG  LYS B 400      30.728  79.434  89.426  1.00 33.37           C  
-ATOM   4212  CD  LYS B 400      31.707  79.782  88.317  1.00 37.48           C  
-ATOM   4213  CE  LYS B 400      33.053  80.217  88.914  1.00 40.54           C  
-ATOM   4214  NZ  LYS B 400      34.239  79.724  88.133  1.00 43.04           N  
-ATOM   4215  N   ALA B 401      26.129  77.866  89.615  1.00 31.31           N  
-ATOM   4216  CA  ALA B 401      24.806  77.767  88.993  1.00 31.29           C  
-ATOM   4217  C   ALA B 401      23.808  78.874  89.412  1.00 31.70           C  
-ATOM   4218  O   ALA B 401      23.095  79.402  88.549  1.00 31.57           O  
-ATOM   4219  CB  ALA B 401      24.204  76.362  89.199  1.00 30.90           C  
-ATOM   4220  N   PRO B 402      23.728  79.218  90.705  1.00 31.72           N  
-ATOM   4221  CA  PRO B 402      22.855  80.325  91.136  1.00 32.11           C  
-ATOM   4222  C   PRO B 402      23.153  81.667  90.458  1.00 32.40           C  
-ATOM   4223  O   PRO B 402      22.248  82.496  90.354  1.00 32.70           O  
-ATOM   4224  CB  PRO B 402      23.119  80.415  92.646  1.00 31.81           C  
-ATOM   4225  CG  PRO B 402      23.547  79.040  93.023  1.00 31.81           C  
-ATOM   4226  CD  PRO B 402      24.390  78.580  91.860  1.00 31.71           C  
-ATOM   4227  N   GLN B 403      24.382  81.850  89.984  1.00 32.94           N  
-ATOM   4228  CA  GLN B 403      24.848  83.110  89.405  1.00 33.46           C  
-ATOM   4229  C   GLN B 403      24.769  83.151  87.872  1.00 33.02           C  
-ATOM   4230  O   GLN B 403      24.847  84.233  87.263  1.00 33.02           O  
-ATOM   4231  CB  GLN B 403      26.293  83.373  89.852  1.00 34.39           C  
-ATOM   4232  CG  GLN B 403      26.433  84.078  91.213  1.00 37.23           C  
-ATOM   4233  CD  GLN B 403      25.911  83.253  92.377  1.00 41.01           C  
-ATOM   4234  OE1 GLN B 403      26.552  82.282  92.795  1.00 44.24           O  
-ATOM   4235  NE2 GLN B 403      24.748  83.633  92.906  1.00 42.43           N  
-ATOM   4236  N   HIS B 404      24.625  81.978  87.254  1.00 32.26           N  
-ATOM   4237  CA  HIS B 404      24.503  81.859  85.795  1.00 31.36           C  
-ATOM   4238  C   HIS B 404      23.318  82.664  85.262  1.00 30.84           C  
-ATOM   4239  O   HIS B 404      22.240  82.644  85.853  1.00 31.15           O  
-ATOM   4240  CB  HIS B 404      24.345  80.390  85.412  1.00 30.82           C  
-ATOM   4241  CG  HIS B 404      24.643  80.094  83.974  1.00 30.30           C  
-ATOM   4242  ND1 HIS B 404      23.838  80.523  82.939  1.00 29.37           N  
-ATOM   4243  CD2 HIS B 404      25.639  79.375  83.402  1.00 28.96           C  
-ATOM   4244  CE1 HIS B 404      24.335  80.093  81.793  1.00 29.47           C  
-ATOM   4245  NE2 HIS B 404      25.427  79.393  82.046  1.00 28.53           N  
-ATOM   4246  N   ALA B 405      23.534  83.361  84.148  1.00 30.39           N  
-ATOM   4247  CA  ALA B 405      22.499  84.155  83.466  1.00 30.17           C  
-ATOM   4248  C   ALA B 405      21.244  83.353  83.112  1.00 30.16           C  
-ATOM   4249  O   ALA B 405      20.141  83.908  83.045  1.00 30.70           O  
-ATOM   4250  CB  ALA B 405      23.071  84.780  82.207  1.00 29.94           C  
-ATOM   4251  N   GLN B 406      21.421  82.057  82.876  1.00 29.47           N  
-ATOM   4252  CA  GLN B 406      20.312  81.164  82.578  1.00 28.89           C  
-ATOM   4253  C   GLN B 406      19.922  80.387  83.836  1.00 28.12           C  
-ATOM   4254  O   GLN B 406      20.770  79.802  84.505  1.00 27.83           O  
-ATOM   4255  CB  GLN B 406      20.689  80.219  81.432  1.00 28.94           C  
-ATOM   4256  CG  GLN B 406      20.498  80.821  80.029  1.00 29.81           C  
-ATOM   4257  CD  GLN B 406      21.454  81.958  79.721  1.00 30.81           C  
-ATOM   4258  OE1 GLN B 406      22.668  81.790  79.796  1.00 31.46           O  
-ATOM   4259  NE2 GLN B 406      20.906  83.119  79.368  1.00 31.18           N  
-ATOM   4260  N   GLN B 407      18.632  80.382  84.148  1.00 27.63           N  
-ATOM   4261  CA  GLN B 407      18.158  79.866  85.435  1.00 26.92           C  
-ATOM   4262  C   GLN B 407      17.024  78.853  85.324  1.00 26.49           C  
-ATOM   4263  O   GLN B 407      16.638  78.242  86.336  1.00 26.60           O  
-ATOM   4264  CB  GLN B 407      17.727  81.026  86.341  1.00 26.57           C  
-ATOM   4265  CG  GLN B 407      18.890  81.821  86.934  1.00 27.09           C  
-ATOM   4266  CD  GLN B 407      19.736  80.999  87.885  1.00 28.23           C  
-ATOM   4267  OE1 GLN B 407      19.202  80.355  88.777  1.00 29.65           O  
-ATOM   4268  NE2 GLN B 407      21.055  81.010  87.691  1.00 27.90           N  
-ATOM   4269  N   SER B 408      16.500  78.654  84.112  1.00 25.53           N  
-ATOM   4270  CA  SER B 408      15.357  77.745  83.918  1.00 25.08           C  
-ATOM   4271  C   SER B 408      15.552  76.319  84.455  1.00 24.07           C  
-ATOM   4272  O   SER B 408      14.596  75.686  84.895  1.00 23.24           O  
-ATOM   4273  CB  SER B 408      14.940  77.686  82.448  1.00 25.42           C  
-ATOM   4274  OG  SER B 408      14.503  78.959  81.995  1.00 26.90           O  
-ATOM   4275  N   ILE B 409      16.777  75.805  84.408  1.00 23.72           N  
-ATOM   4276  CA  ILE B 409      17.015  74.454  84.927  1.00 23.46           C  
-ATOM   4277  C   ILE B 409      16.957  74.401  86.463  1.00 23.80           C  
-ATOM   4278  O   ILE B 409      16.305  73.529  87.021  1.00 23.62           O  
-ATOM   4279  CB  ILE B 409      18.313  73.834  84.365  1.00 23.19           C  
-ATOM   4280  CG1 ILE B 409      18.172  73.620  82.856  1.00 22.51           C  
-ATOM   4281  CG2 ILE B 409      18.616  72.519  85.060  1.00 22.15           C  
-ATOM   4282  CD1 ILE B 409      19.456  73.324  82.146  1.00 22.90           C  
-ATOM   4283  N   ARG B 410      17.617  75.344  87.133  1.00 24.54           N  
-ATOM   4284  CA  ARG B 410      17.499  75.473  88.589  1.00 25.33           C  
-ATOM   4285  C   ARG B 410      16.046  75.563  89.047  1.00 25.47           C  
-ATOM   4286  O   ARG B 410      15.651  74.880  90.000  1.00 25.51           O  
-ATOM   4287  CB  ARG B 410      18.268  76.687  89.098  1.00 25.56           C  
-ATOM   4288  CG  ARG B 410      19.759  76.484  89.162  1.00 26.87           C  
-ATOM   4289  CD  ARG B 410      20.493  77.586  89.894  1.00 29.27           C  
-ATOM   4290  NE  ARG B 410      20.249  77.543  91.340  1.00 29.88           N  
-ATOM   4291  CZ  ARG B 410      19.685  78.521  92.038  1.00 29.18           C  
-ATOM   4292  NH1 ARG B 410      19.283  79.642  91.445  1.00 28.77           N  
-ATOM   4293  NH2 ARG B 410      19.516  78.378  93.341  1.00 30.16           N  
-ATOM   4294  N   GLU B 411      15.258  76.391  88.363  1.00 25.82           N  
-ATOM   4295  CA  GLU B 411      13.837  76.556  88.683  1.00 26.72           C  
-ATOM   4296  C   GLU B 411      13.084  75.255  88.485  1.00 26.31           C  
-ATOM   4297  O   GLU B 411      12.296  74.844  89.347  1.00 26.40           O  
-ATOM   4298  CB  GLU B 411      13.176  77.655  87.835  1.00 26.92           C  
-ATOM   4299  CG  GLU B 411      13.898  78.995  87.817  1.00 31.68           C  
-ATOM   4300  CD  GLU B 411      13.755  79.797  89.101  1.00 37.43           C  
-ATOM   4301  OE1 GLU B 411      12.819  79.537  89.896  1.00 39.60           O  
-ATOM   4302  OE2 GLU B 411      14.595  80.705  89.313  1.00 41.59           O  
-ATOM   4303  N   LYS B 412      13.334  74.611  87.345  1.00 25.70           N  
-ATOM   4304  CA  LYS B 412      12.704  73.344  87.017  1.00 25.36           C  
-ATOM   4305  C   LYS B 412      12.995  72.322  88.111  1.00 25.55           C  
-ATOM   4306  O   LYS B 412      12.089  71.632  88.574  1.00 25.27           O  
-ATOM   4307  CB  LYS B 412      13.198  72.850  85.649  1.00 25.04           C  
-ATOM   4308  CG  LYS B 412      12.930  71.390  85.344  1.00 23.91           C  
-ATOM   4309  CD  LYS B 412      13.293  71.064  83.897  1.00 24.03           C  
-ATOM   4310  CE  LYS B 412      13.199  69.575  83.601  1.00 22.32           C  
-ATOM   4311  NZ  LYS B 412      13.811  69.270  82.275  1.00 22.53           N  
-ATOM   4312  N   TYR B 413      14.254  72.250  88.540  1.00 25.73           N  
-ATOM   4313  CA  TYR B 413      14.669  71.243  89.512  1.00 26.60           C  
-ATOM   4314  C   TYR B 413      14.387  71.578  90.996  1.00 27.42           C  
-ATOM   4315  O   TYR B 413      14.835  70.856  91.898  1.00 27.23           O  
-ATOM   4316  CB  TYR B 413      16.128  70.822  89.267  1.00 26.39           C  
-ATOM   4317  CG  TYR B 413      16.226  69.828  88.129  1.00 26.28           C  
-ATOM   4318  CD1 TYR B 413      16.217  70.262  86.795  1.00 24.79           C  
-ATOM   4319  CD2 TYR B 413      16.274  68.455  88.382  1.00 24.89           C  
-ATOM   4320  CE1 TYR B 413      16.278  69.353  85.744  1.00 25.19           C  
-ATOM   4321  CE2 TYR B 413      16.333  67.533  87.345  1.00 24.71           C  
-ATOM   4322  CZ  TYR B 413      16.333  67.986  86.025  1.00 25.93           C  
-ATOM   4323  OH  TYR B 413      16.385  67.076  84.989  1.00 24.79           O  
-ATOM   4324  N   LYS B 414      13.643  72.660  91.229  1.00 28.34           N  
-ATOM   4325  CA  LYS B 414      13.074  72.959  92.551  1.00 30.04           C  
-ATOM   4326  C   LYS B 414      11.790  72.144  92.786  1.00 31.00           C  
-ATOM   4327  O   LYS B 414      11.406  71.871  93.935  1.00 31.44           O  
-ATOM   4328  CB  LYS B 414      12.786  74.458  92.687  1.00 29.74           C  
-ATOM   4329  CG  LYS B 414      14.031  75.295  92.932  1.00 30.74           C  
-ATOM   4330  CD  LYS B 414      13.716  76.763  93.108  1.00 33.68           C  
-ATOM   4331  CE  LYS B 414      14.830  77.637  92.524  1.00 35.14           C  
-ATOM   4332  NZ  LYS B 414      14.540  79.089  92.738  1.00 37.47           N  
-ATOM   4333  N   ASN B 415      11.132  71.770  91.686  1.00 31.60           N  
-ATOM   4334  CA  ASN B 415       9.925  70.953  91.723  1.00 32.65           C  
-ATOM   4335  C   ASN B 415      10.136  69.602  92.400  1.00 32.77           C  
-ATOM   4336  O   ASN B 415      11.202  68.994  92.271  1.00 33.07           O  
-ATOM   4337  CB  ASN B 415       9.402  70.728  90.305  1.00 32.95           C  
-ATOM   4338  CG  ASN B 415       7.937  70.378  90.277  1.00 34.82           C  
-ATOM   4339  OD1 ASN B 415       7.551  69.224  90.487  1.00 38.14           O  
-ATOM   4340  ND2 ASN B 415       7.101  71.377  90.018  1.00 37.83           N  
-ATOM   4341  N   SER B 416       9.100  69.135  93.095  1.00 32.68           N  
-ATOM   4342  CA  SER B 416       9.132  67.872  93.829  1.00 32.70           C  
-ATOM   4343  C   SER B 416       9.172  66.660  92.903  1.00 32.42           C  
-ATOM   4344  O   SER B 416       9.588  65.579  93.315  1.00 32.22           O  
-ATOM   4345  CB  SER B 416       7.939  67.776  94.790  1.00 32.79           C  
-ATOM   4346  OG  SER B 416       6.711  67.841  94.080  1.00 34.68           O  
-ATOM   4347  N   LYS B 417       8.734  66.845  91.658  1.00 32.13           N  
-ATOM   4348  CA  LYS B 417       8.906  65.842  90.609  1.00 31.95           C  
-ATOM   4349  C   LYS B 417      10.366  65.397  90.559  1.00 31.06           C  
-ATOM   4350  O   LYS B 417      10.662  64.222  90.312  1.00 31.09           O  
-ATOM   4351  CB  LYS B 417       8.487  66.426  89.253  1.00 32.51           C  
-ATOM   4352  CG  LYS B 417       8.907  65.615  88.040  1.00 34.44           C  
-ATOM   4353  CD  LYS B 417       7.824  65.626  86.974  1.00 39.33           C  
-ATOM   4354  CE  LYS B 417       8.088  66.691  85.924  1.00 41.10           C  
-ATOM   4355  NZ  LYS B 417       7.704  68.058  86.407  1.00 43.74           N  
-ATOM   4356  N   TYR B 418      11.261  66.346  90.824  1.00 29.85           N  
-ATOM   4357  CA  TYR B 418      12.705  66.106  90.845  1.00 29.03           C  
-ATOM   4358  C   TYR B 418      13.301  66.230  92.254  1.00 28.31           C  
-ATOM   4359  O   TYR B 418      14.495  66.469  92.402  1.00 28.28           O  
-ATOM   4360  CB  TYR B 418      13.413  67.056  89.864  1.00 28.79           C  
-ATOM   4361  CG  TYR B 418      12.776  67.066  88.485  1.00 29.37           C  
-ATOM   4362  CD1 TYR B 418      12.958  66.000  87.611  1.00 29.44           C  
-ATOM   4363  CD2 TYR B 418      11.972  68.127  88.069  1.00 28.99           C  
-ATOM   4364  CE1 TYR B 418      12.375  65.988  86.361  1.00 29.94           C  
-ATOM   4365  CE2 TYR B 418      11.383  68.126  86.811  1.00 29.78           C  
-ATOM   4366  CZ  TYR B 418      11.592  67.046  85.960  1.00 30.61           C  
-ATOM   4367  OH  TYR B 418      11.014  67.005  84.703  1.00 31.64           O  
-ATOM   4368  N   HIS B 419      12.463  66.066  93.280  1.00 27.62           N  
-ATOM   4369  CA  HIS B 419      12.909  66.032  94.679  1.00 26.96           C  
-ATOM   4370  C   HIS B 419      13.671  67.283  95.103  1.00 26.65           C  
-ATOM   4371  O   HIS B 419      14.581  67.206  95.915  1.00 26.95           O  
-ATOM   4372  CB  HIS B 419      13.736  64.764  94.963  1.00 27.29           C  
-ATOM   4373  CG  HIS B 419      13.127  63.511  94.409  1.00 28.17           C  
-ATOM   4374  ND1 HIS B 419      13.357  63.078  93.118  1.00 30.06           N  
-ATOM   4375  CD2 HIS B 419      12.277  62.613  94.960  1.00 28.71           C  
-ATOM   4376  CE1 HIS B 419      12.678  61.965  92.901  1.00 29.33           C  
-ATOM   4377  NE2 HIS B 419      12.011  61.663  94.000  1.00 29.82           N  
-ATOM   4378  N   GLY B 420      13.294  68.431  94.536  1.00 26.21           N  
-ATOM   4379  CA  GLY B 420      13.908  69.710  94.844  1.00 25.79           C  
-ATOM   4380  C   GLY B 420      15.428  69.769  94.887  1.00 25.85           C  
-ATOM   4381  O   GLY B 420      15.989  70.614  95.604  1.00 26.38           O  
-ATOM   4382  N   VAL B 421      16.100  68.913  94.110  1.00 25.12           N  
-ATOM   4383  CA  VAL B 421      17.566  68.793  94.188  1.00 24.15           C  
-ATOM   4384  C   VAL B 421      18.363  70.049  93.889  1.00 23.99           C  
-ATOM   4385  O   VAL B 421      19.512  70.144  94.307  1.00 23.79           O  
-ATOM   4386  CB  VAL B 421      18.131  67.644  93.319  1.00 24.30           C  
-ATOM   4387  CG1 VAL B 421      17.745  66.291  93.911  1.00 22.95           C  
-ATOM   4388  CG2 VAL B 421      17.712  67.806  91.825  1.00 23.90           C  
-ATOM   4389  N   SER B 422      17.788  71.013  93.173  1.00 24.51           N  
-ATOM   4390  CA  SER B 422      18.511  72.278  92.944  1.00 25.35           C  
-ATOM   4391  C   SER B 422      18.686  73.131  94.205  1.00 25.95           C  
-ATOM   4392  O   SER B 422      19.398  74.137  94.184  1.00 25.96           O  
-ATOM   4393  CB  SER B 422      17.891  73.111  91.826  1.00 24.91           C  
-ATOM   4394  OG  SER B 422      16.550  73.426  92.121  1.00 26.49           O  
-ATOM   4395  N   LEU B 423      18.045  72.732  95.299  1.00 27.01           N  
-ATOM   4396  CA  LEU B 423      18.192  73.468  96.555  1.00 28.19           C  
-ATOM   4397  C   LEU B 423      19.264  72.839  97.442  1.00 28.71           C  
-ATOM   4398  O   LEU B 423      19.695  73.434  98.424  1.00 29.25           O  
-ATOM   4399  CB  LEU B 423      16.850  73.615  97.275  1.00 28.29           C  
-ATOM   4400  CG  LEU B 423      15.726  74.179  96.396  1.00 28.77           C  
-ATOM   4401  CD1 LEU B 423      14.376  73.739  96.913  1.00 30.97           C  
-ATOM   4402  CD2 LEU B 423      15.799  75.705  96.261  1.00 30.45           C  
-ATOM   4403  N   LEU B 424      19.720  71.649  97.064  1.00 29.22           N  
-ATOM   4404  CA  LEU B 424      20.842  71.008  97.740  1.00 29.87           C  
-ATOM   4405  C   LEU B 424      22.090  71.865  97.578  1.00 30.58           C  
-ATOM   4406  O   LEU B 424      22.262  72.524  96.554  1.00 30.91           O  
-ATOM   4407  CB  LEU B 424      21.076  69.602  97.176  1.00 29.53           C  
-ATOM   4408  CG  LEU B 424      19.943  68.573  97.293  1.00 29.44           C  
-ATOM   4409  CD1 LEU B 424      20.359  67.248  96.671  1.00 28.43           C  
-ATOM   4410  CD2 LEU B 424      19.510  68.364  98.753  1.00 29.47           C  
-ATOM   4411  N   ASN B 425      22.960  71.865  98.585  1.00 31.51           N  
-ATOM   4412  CA  ASN B 425      24.216  72.614  98.503  1.00 32.19           C  
-ATOM   4413  C   ASN B 425      25.320  71.795  97.848  1.00 32.43           C  
-ATOM   4414  O   ASN B 425      25.565  70.650  98.244  1.00 32.50           O  
-ATOM   4415  CB  ASN B 425      24.707  73.029  99.887  1.00 32.60           C  
-ATOM   4416  CG  ASN B 425      23.708  73.862 100.641  1.00 33.79           C  
-ATOM   4417  OD1 ASN B 425      23.410  73.567 101.800  1.00 37.25           O  
-ATOM   4418  ND2 ASN B 425      23.196  74.912 100.009  1.00 33.76           N  
-ATOM   4419  N   PRO B 426      26.008  72.382  96.876  1.00 32.65           N  
-ATOM   4420  CA  PRO B 426      27.174  71.731  96.271  1.00 33.35           C  
-ATOM   4421  C   PRO B 426      28.321  71.623  97.281  1.00 34.32           C  
-ATOM   4422  O   PRO B 426      28.416  72.468  98.173  1.00 34.38           O  
-ATOM   4423  CB  PRO B 426      27.562  72.677  95.122  1.00 33.04           C  
-ATOM   4424  CG  PRO B 426      26.924  73.979  95.422  1.00 32.36           C  
-ATOM   4425  CD  PRO B 426      25.736  73.706  96.288  1.00 32.67           C  
-ATOM   4426  N   PRO B 427      29.180  70.617  97.140  1.00 35.25           N  
-ATOM   4427  CA  PRO B 427      30.349  70.492  98.013  1.00 36.12           C  
-ATOM   4428  C   PRO B 427      31.380  71.547  97.620  1.00 37.28           C  
-ATOM   4429  O   PRO B 427      31.478  71.884  96.437  1.00 37.43           O  
-ATOM   4430  CB  PRO B 427      30.859  69.078  97.717  1.00 35.79           C  
-ATOM   4431  CG  PRO B 427      30.401  68.781  96.324  1.00 35.47           C  
-ATOM   4432  CD  PRO B 427      29.121  69.547  96.125  1.00 35.33           C  
-ATOM   4433  N   GLU B 428      32.122  72.075  98.587  1.00 38.71           N  
-ATOM   4434  CA  GLU B 428      33.133  73.090  98.282  1.00 40.22           C  
-ATOM   4435  C   GLU B 428      34.387  72.476  97.654  1.00 40.55           C  
-ATOM   4436  O   GLU B 428      35.085  73.131  96.877  1.00 40.77           O  
-ATOM   4437  CB  GLU B 428      33.469  73.952  99.516  1.00 40.53           C  
-ATOM   4438  CG  GLU B 428      34.100  73.214 100.688  1.00 43.25           C  
-ATOM   4439  CD  GLU B 428      34.387  74.125 101.871  1.00 47.27           C  
-ATOM   4440  OE1 GLU B 428      35.328  74.948 101.780  1.00 48.88           O  
-ATOM   4441  OE2 GLU B 428      33.673  74.017 102.897  1.00 48.70           O  
-ATOM   4442  N   THR B 429      34.671  71.222  97.999  1.00 41.18           N  
-ATOM   4443  CA  THR B 429      35.794  70.496  97.414  1.00 42.22           C  
-ATOM   4444  C   THR B 429      35.384  69.077  97.074  1.00 43.14           C  
-ATOM   4445  O   THR B 429      34.476  68.517  97.689  1.00 43.05           O  
-ATOM   4446  CB  THR B 429      37.051  70.474  98.351  1.00 41.97           C  
-ATOM   4447  OG1 THR B 429      36.761  69.737  99.548  1.00 41.76           O  
-ATOM   4448  CG2 THR B 429      37.409  71.874  98.851  1.00 41.92           C  
-ATOM   4449  N   LEU B 430      36.078  68.500  96.101  1.00 44.73           N  
-ATOM   4450  CA  LEU B 430      35.822  67.138  95.662  1.00 46.55           C  
-ATOM   4451  C   LEU B 430      36.807  66.154  96.272  1.00 48.09           C  
-ATOM   4452  O   LEU B 430      36.565  64.947  96.268  1.00 48.30           O  
-ATOM   4453  CB  LEU B 430      35.868  67.056  94.134  1.00 46.39           C  
-ATOM   4454  CG  LEU B 430      34.828  67.870  93.360  1.00 45.96           C  
-ATOM   4455  CD1 LEU B 430      34.894  67.542  91.879  1.00 46.54           C  
-ATOM   4456  CD2 LEU B 430      33.428  67.624  93.894  1.00 45.09           C  
-ATOM   4457  N   ASN B 431      37.914  66.676  96.801  1.00 49.96           N  
-ATOM   4458  CA  ASN B 431      38.956  65.848  97.407  1.00 51.77           C  
-ATOM   4459  C   ASN B 431      39.387  64.702  96.488  1.00 52.48           C  
-ATOM   4460  O   ASN B 431      39.213  63.523  96.816  1.00 52.56           O  
-ATOM   4461  CB  ASN B 431      38.486  65.311  98.763  1.00 52.18           C  
-ATOM   4462  CG  ASN B 431      38.932  66.179  99.917  1.00 53.81           C  
-ATOM   4463  OD1 ASN B 431      40.034  66.010 100.445  1.00 56.15           O  
-ATOM   4464  ND2 ASN B 431      38.076  67.115 100.322  1.00 55.34           N  
-ATOM   4465  N   LEU B 432      39.936  65.058  95.329  1.00 53.46           N  
-ATOM   4466  CA  LEU B 432      40.304  64.061  94.332  1.00 54.42           C  
-ATOM   4467  C   LEU B 432      41.811  63.894  94.207  1.00 55.00           C  
-ATOM   4468  O   LEU B 432      42.316  62.786  94.434  1.00 55.45           O  
-ATOM   4469  CB  LEU B 432      39.693  64.404  92.973  1.00 54.51           C  
-ATOM   4470  CG  LEU B 432      38.197  64.179  92.735  1.00 54.73           C  
-ATOM   4471  CD1 LEU B 432      37.926  64.313  91.258  1.00 55.23           C  
-ATOM   4472  CD2 LEU B 432      37.716  62.820  93.230  1.00 55.39           C  
-ATOM   4473  OXT LEU B 432      42.513  64.858  93.878  1.00 55.41           O  
-TER    4474      LEU B 432                                                      
-ATOM   4475  N   SER C   0     -21.602  -4.342 102.314  1.00 49.74           N  
-ATOM   4476  CA  SER C   0     -20.137  -4.432 102.604  1.00 49.52           C  
-ATOM   4477  C   SER C   0     -19.652  -5.859 102.398  1.00 48.92           C  
-ATOM   4478  O   SER C   0     -18.996  -6.182 101.403  1.00 49.05           O  
-ATOM   4479  CB  SER C   0     -19.851  -3.985 104.045  1.00 49.40           C  
-ATOM   4480  OG  SER C   0     -19.813  -2.569 104.136  1.00 50.80           O  
-ATOM   4481  N   MET C   1     -20.004  -6.704 103.358  1.00 48.31           N  
-ATOM   4482  CA  MET C   1     -19.669  -8.114 103.354  1.00 47.58           C  
-ATOM   4483  C   MET C   1     -20.803  -8.900 102.722  1.00 46.74           C  
-ATOM   4484  O   MET C   1     -20.697 -10.110 102.528  1.00 46.48           O  
-ATOM   4485  CB  MET C   1     -19.429  -8.580 104.790  1.00 47.88           C  
-ATOM   4486  CG  MET C   1     -18.327  -7.816 105.489  1.00 48.16           C  
-ATOM   4487  SD  MET C   1     -16.768  -8.100 104.668  1.00 50.83           S  
-ATOM   4488  CE  MET C   1     -16.519  -9.800 105.098  1.00 49.84           C  
-ATOM   4489  N   GLU C   2     -21.879  -8.184 102.402  1.00 45.97           N  
-ATOM   4490  CA  GLU C   2     -23.056  -8.716 101.712  1.00 45.54           C  
-ATOM   4491  C   GLU C   2     -22.693  -9.618 100.536  1.00 44.45           C  
-ATOM   4492  O   GLU C   2     -23.351 -10.631 100.307  1.00 44.34           O  
-ATOM   4493  CB  GLU C   2     -23.932  -7.550 101.229  1.00 46.04           C  
-ATOM   4494  CG  GLU C   2     -25.230  -7.932 100.531  1.00 48.35           C  
-ATOM   4495  CD  GLU C   2     -25.714  -6.869  99.551  1.00 52.06           C  
-ATOM   4496  OE1 GLU C   2     -25.367  -5.671  99.716  1.00 53.74           O  
-ATOM   4497  OE2 GLU C   2     -26.456  -7.229  98.608  1.00 53.23           O  
-ATOM   4498  N   ASN C   3     -21.644  -9.250  99.803  1.00 43.10           N  
-ATOM   4499  CA  ASN C   3     -21.232 -10.004  98.624  1.00 42.22           C  
-ATOM   4500  C   ASN C   3     -20.321 -11.206  98.909  1.00 41.21           C  
-ATOM   4501  O   ASN C   3     -19.964 -11.946  97.992  1.00 41.18           O  
-ATOM   4502  CB  ASN C   3     -20.603  -9.069  97.581  1.00 42.38           C  
-ATOM   4503  CG  ASN C   3     -21.626  -8.139  96.938  1.00 43.25           C  
-ATOM   4504  OD1 ASN C   3     -22.782  -8.518  96.713  1.00 43.93           O  
-ATOM   4505  ND2 ASN C   3     -21.208  -6.910  96.653  1.00 43.79           N  
-ATOM   4506  N   PHE C   4     -19.960 -11.408 100.175  1.00 40.07           N  
-ATOM   4507  CA  PHE C   4     -19.051 -12.492 100.538  1.00 38.87           C  
-ATOM   4508  C   PHE C   4     -19.705 -13.602 101.357  1.00 38.65           C  
-ATOM   4509  O   PHE C   4     -20.404 -13.344 102.337  1.00 38.03           O  
-ATOM   4510  CB  PHE C   4     -17.814 -11.946 101.250  1.00 38.62           C  
-ATOM   4511  CG  PHE C   4     -16.884 -11.190 100.345  1.00 37.79           C  
-ATOM   4512  CD1 PHE C   4     -16.022 -11.866  99.486  1.00 37.37           C  
-ATOM   4513  CD2 PHE C   4     -16.877  -9.799 100.343  1.00 37.53           C  
-ATOM   4514  CE1 PHE C   4     -15.161 -11.170  98.641  1.00 36.82           C  
-ATOM   4515  CE2 PHE C   4     -16.022  -9.089  99.503  1.00 36.91           C  
-ATOM   4516  CZ  PHE C   4     -15.162  -9.774  98.651  1.00 36.86           C  
-ATOM   4517  N   GLN C   5     -19.478 -14.840 100.927  1.00 38.41           N  
-ATOM   4518  CA  GLN C   5     -19.934 -16.004 101.666  1.00 38.64           C  
-ATOM   4519  C   GLN C   5     -18.748 -16.672 102.343  1.00 38.63           C  
-ATOM   4520  O   GLN C   5     -17.858 -17.204 101.675  1.00 38.43           O  
-ATOM   4521  CB  GLN C   5     -20.660 -16.988 100.748  1.00 38.66           C  
-ATOM   4522  CG  GLN C   5     -21.099 -18.284 101.432  1.00 39.85           C  
-ATOM   4523  CD  GLN C   5     -22.133 -18.059 102.523  1.00 40.69           C  
-ATOM   4524  OE1 GLN C   5     -23.257 -17.639 102.244  1.00 42.78           O  
-ATOM   4525  NE2 GLN C   5     -21.758 -18.341 103.767  1.00 41.12           N  
-ATOM   4526  N   LYS C   6     -18.738 -16.626 103.672  1.00 38.79           N  
-ATOM   4527  CA  LYS C   6     -17.714 -17.311 104.446  1.00 39.39           C  
-ATOM   4528  C   LYS C   6     -17.876 -18.815 104.255  1.00 39.67           C  
-ATOM   4529  O   LYS C   6     -18.996 -19.332 104.234  1.00 39.66           O  
-ATOM   4530  CB  LYS C   6     -17.795 -16.923 105.926  1.00 39.53           C  
-ATOM   4531  CG  LYS C   6     -17.259 -15.517 106.235  1.00 40.34           C  
-ATOM   4532  CD  LYS C   6     -17.477 -15.140 107.700  1.00 41.51           C  
-ATOM   4533  CE  LYS C   6     -17.111 -13.683 107.970  1.00 42.13           C  
-ATOM   4534  NZ  LYS C   6     -17.926 -13.092 109.080  1.00 43.01           N  
-ATOM   4535  N   VAL C   7     -16.750 -19.496 104.082  1.00 40.33           N  
-ATOM   4536  CA  VAL C   7     -16.721 -20.931 103.826  1.00 41.26           C  
-ATOM   4537  C   VAL C   7     -16.207 -21.672 105.062  1.00 41.99           C  
-ATOM   4538  O   VAL C   7     -16.824 -22.639 105.517  1.00 42.46           O  
-ATOM   4539  CB  VAL C   7     -15.826 -21.271 102.608  1.00 41.06           C  
-ATOM   4540  CG1 VAL C   7     -15.719 -22.781 102.412  1.00 41.12           C  
-ATOM   4541  CG2 VAL C   7     -16.349 -20.600 101.345  1.00 41.40           C  
-ATOM   4542  N   GLU C   8     -15.076 -21.207 105.592  1.00 42.76           N  
-ATOM   4543  CA  GLU C   8     -14.439 -21.806 106.760  1.00 43.50           C  
-ATOM   4544  C   GLU C   8     -13.402 -20.867 107.372  1.00 43.76           C  
-ATOM   4545  O   GLU C   8     -12.932 -19.935 106.715  1.00 43.42           O  
-ATOM   4546  CB  GLU C   8     -13.777 -23.137 106.393  1.00 43.81           C  
-ATOM   4547  CG  GLU C   8     -12.834 -23.085 105.200  1.00 45.38           C  
-ATOM   4548  CD  GLU C   8     -12.264 -24.445 104.845  1.00 47.10           C  
-ATOM   4549  OE1 GLU C   8     -13.041 -25.323 104.402  1.00 48.93           O  
-ATOM   4550  OE2 GLU C   8     -11.039 -24.639 105.007  1.00 47.62           O  
-ATOM   4551  N   LYS C   9     -13.060 -21.112 108.637  1.00 44.08           N  
-ATOM   4552  CA  LYS C   9     -11.929 -20.439 109.264  1.00 44.64           C  
-ATOM   4553  C   LYS C   9     -10.648 -21.126 108.801  1.00 44.85           C  
-ATOM   4554  O   LYS C   9     -10.561 -22.352 108.832  1.00 44.91           O  
-ATOM   4555  CB  LYS C   9     -12.052 -20.468 110.792  1.00 44.76           C  
-ATOM   4556  CG  LYS C   9     -10.741 -20.246 111.543  1.00 44.99           C  
-ATOM   4557  CD  LYS C   9     -10.951 -20.109 113.053  1.00 46.19           C  
-ATOM   4558  CE  LYS C   9      -9.700 -19.534 113.708  1.00 47.30           C  
-ATOM   4559  NZ  LYS C   9      -9.407 -20.106 115.057  1.00 49.41           N  
-ATOM   4560  N   ILE C  10      -9.673 -20.338 108.352  1.00 45.14           N  
-ATOM   4561  CA  ILE C  10      -8.399 -20.887 107.887  1.00 45.75           C  
-ATOM   4562  C   ILE C  10      -7.214 -20.459 108.754  1.00 46.90           C  
-ATOM   4563  O   ILE C  10      -6.082 -20.878 108.514  1.00 46.96           O  
-ATOM   4564  CB  ILE C  10      -8.143 -20.592 106.364  1.00 45.30           C  
-ATOM   4565  CG1 ILE C  10      -8.259 -19.093 106.042  1.00 44.88           C  
-ATOM   4566  CG2 ILE C  10      -9.077 -21.427 105.493  1.00 44.69           C  
-ATOM   4567  CD1 ILE C  10      -7.925 -18.718 104.579  1.00 43.29           C  
-ATOM   4568  N   GLY C  11      -7.483 -19.639 109.766  1.00 48.39           N  
-ATOM   4569  CA  GLY C  11      -6.464 -19.225 110.716  1.00 50.56           C  
-ATOM   4570  C   GLY C  11      -6.929 -18.092 111.606  1.00 52.27           C  
-ATOM   4571  O   GLY C  11      -8.075 -17.648 111.483  1.00 52.22           O  
-ATOM   4572  N   GLU C  12      -6.051 -17.644 112.508  1.00 54.09           N  
-ATOM   4573  CA  GLU C  12      -6.280 -16.444 113.329  1.00 56.27           C  
-ATOM   4574  C   GLU C  12      -5.019 -15.945 114.060  1.00 57.55           C  
-ATOM   4575  O   GLU C  12      -4.134 -15.356 113.433  1.00 57.67           O  
-ATOM   4576  CB  GLU C  12      -7.482 -16.611 114.282  1.00 56.31           C  
-ATOM   4577  CG  GLU C  12      -7.270 -17.502 115.498  1.00 57.49           C  
-ATOM   4578  CD  GLU C  12      -8.144 -17.084 116.666  1.00 58.44           C  
-ATOM   4579  OE1 GLU C  12      -9.154 -17.769 116.922  1.00 59.42           O  
-ATOM   4580  OE2 GLU C  12      -7.827 -16.070 117.325  1.00 59.03           O  
-ATOM   4581  N   GLY C  13      -4.947 -16.186 115.374  1.00 59.14           N  
-ATOM   4582  CA  GLY C  13      -3.838 -15.742 116.207  1.00 60.79           C  
-ATOM   4583  C   GLY C  13      -4.244 -14.595 117.119  1.00 61.98           C  
-ATOM   4584  O   GLY C  13      -4.960 -14.797 118.111  1.00 62.21           O  
-ATOM   4585  N   THR C  14      -3.766 -13.394 116.785  1.00 62.81           N  
-ATOM   4586  CA  THR C  14      -4.173 -12.154 117.452  1.00 63.44           C  
-ATOM   4587  C   THR C  14      -5.186 -11.459 116.538  1.00 63.46           C  
-ATOM   4588  O   THR C  14      -5.634 -12.077 115.569  1.00 63.80           O  
-ATOM   4589  CB  THR C  14      -2.925 -11.264 117.781  1.00 63.56           C  
-ATOM   4590  OG1 THR C  14      -3.337  -9.952 118.189  1.00 64.12           O  
-ATOM   4591  CG2 THR C  14      -2.069 -11.006 116.540  1.00 63.96           C  
-ATOM   4592  N   TYR C  15      -5.566 -10.216 116.862  1.00 63.14           N  
-ATOM   4593  CA  TYR C  15      -6.391  -9.322 116.009  1.00 62.70           C  
-ATOM   4594  C   TYR C  15      -7.798  -9.781 115.588  1.00 61.45           C  
-ATOM   4595  O   TYR C  15      -8.720  -8.963 115.480  1.00 61.63           O  
-ATOM   4596  CB  TYR C  15      -5.610  -8.833 114.771  1.00 63.58           C  
-ATOM   4597  CG  TYR C  15      -5.266  -9.909 113.755  1.00 65.86           C  
-ATOM   4598  CD1 TYR C  15      -6.236 -10.431 112.894  1.00 68.25           C  
-ATOM   4599  CD2 TYR C  15      -3.963 -10.397 113.649  1.00 68.31           C  
-ATOM   4600  CE1 TYR C  15      -5.919 -11.423 111.969  1.00 69.86           C  
-ATOM   4601  CE2 TYR C  15      -3.635 -11.386 112.728  1.00 70.02           C  
-ATOM   4602  CZ  TYR C  15      -4.616 -11.895 111.891  1.00 70.45           C  
-ATOM   4603  OH  TYR C  15      -4.287 -12.871 110.977  1.00 71.03           O  
-ATOM   4604  N   GLY C  16      -7.953 -11.076 115.334  1.00 59.75           N  
-ATOM   4605  CA  GLY C  16      -9.179 -11.612 114.778  1.00 57.21           C  
-ATOM   4606  C   GLY C  16      -8.909 -12.777 113.848  1.00 55.45           C  
-ATOM   4607  O   GLY C  16      -7.760 -13.178 113.649  1.00 55.33           O  
-ATOM   4608  N   VAL C  17      -9.977 -13.314 113.269  1.00 53.36           N  
-ATOM   4609  CA  VAL C  17      -9.900 -14.550 112.500  1.00 51.27           C  
-ATOM   4610  C   VAL C  17      -9.638 -14.298 111.005  1.00 49.65           C  
-ATOM   4611  O   VAL C  17      -9.950 -13.223 110.479  1.00 49.07           O  
-ATOM   4612  CB  VAL C  17     -11.179 -15.404 112.717  1.00 51.36           C  
-ATOM   4613  CG1 VAL C  17     -11.209 -16.616 111.803  1.00 51.55           C  
-ATOM   4614  CG2 VAL C  17     -11.282 -15.843 114.166  1.00 51.71           C  
-ATOM   4615  N   VAL C  18      -9.034 -15.289 110.346  1.00 47.42           N  
-ATOM   4616  CA  VAL C  18      -8.924 -15.301 108.892  1.00 45.43           C  
-ATOM   4617  C   VAL C  18      -9.872 -16.352 108.299  1.00 44.15           C  
-ATOM   4618  O   VAL C  18      -9.759 -17.550 108.597  1.00 43.71           O  
-ATOM   4619  CB  VAL C  18      -7.476 -15.535 108.418  1.00 45.46           C  
-ATOM   4620  CG1 VAL C  18      -7.381 -15.407 106.904  1.00 45.19           C  
-ATOM   4621  CG2 VAL C  18      -6.528 -14.553 109.086  1.00 45.37           C  
-ATOM   4622  N   TYR C  19     -10.804 -15.887 107.467  1.00 42.26           N  
-ATOM   4623  CA  TYR C  19     -11.814 -16.739 106.850  1.00 40.93           C  
-ATOM   4624  C   TYR C  19     -11.555 -17.001 105.367  1.00 39.65           C  
-ATOM   4625  O   TYR C  19     -11.127 -16.110 104.627  1.00 39.28           O  
-ATOM   4626  CB  TYR C  19     -13.196 -16.100 106.965  1.00 41.04           C  
-ATOM   4627  CG  TYR C  19     -13.715 -15.920 108.368  1.00 42.79           C  
-ATOM   4628  CD1 TYR C  19     -13.542 -14.710 109.041  1.00 44.63           C  
-ATOM   4629  CD2 TYR C  19     -14.410 -16.945 109.016  1.00 44.08           C  
-ATOM   4630  CE1 TYR C  19     -14.034 -14.526 110.328  1.00 46.00           C  
-ATOM   4631  CE2 TYR C  19     -14.906 -16.772 110.304  1.00 46.02           C  
-ATOM   4632  CZ  TYR C  19     -14.711 -15.558 110.951  1.00 46.62           C  
-ATOM   4633  OH  TYR C  19     -15.195 -15.366 112.220  1.00 49.00           O  
-ATOM   4634  N   LYS C  20     -11.841 -18.224 104.933  1.00 37.87           N  
-ATOM   4635  CA  LYS C  20     -11.939 -18.505 103.514  1.00 36.18           C  
-ATOM   4636  C   LYS C  20     -13.329 -18.083 103.099  1.00 35.19           C  
-ATOM   4637  O   LYS C  20     -14.309 -18.371 103.789  1.00 34.64           O  
-ATOM   4638  CB  LYS C  20     -11.718 -19.981 103.206  1.00 36.10           C  
-ATOM   4639  CG  LYS C  20     -11.902 -20.321 101.729  1.00 36.59           C  
-ATOM   4640  CD  LYS C  20     -11.763 -21.809 101.467  1.00 36.97           C  
-ATOM   4641  CE  LYS C  20     -11.977 -22.095 100.004  1.00 36.93           C  
-ATOM   4642  NZ  LYS C  20     -11.714 -23.518  99.680  1.00 39.42           N  
-ATOM   4643  N   ALA C  21     -13.409 -17.379 101.979  1.00 34.16           N  
-ATOM   4644  CA  ALA C  21     -14.681 -16.855 101.511  1.00 33.35           C  
-ATOM   4645  C   ALA C  21     -14.727 -16.756  99.994  1.00 32.81           C  
-ATOM   4646  O   ALA C  21     -13.694 -16.776  99.324  1.00 32.09           O  
-ATOM   4647  CB  ALA C  21     -14.953 -15.504 102.147  1.00 33.10           C  
-ATOM   4648  N   ARG C  22     -15.938 -16.664  99.463  1.00 32.88           N  
-ATOM   4649  CA  ARG C  22     -16.128 -16.510  98.031  1.00 33.34           C  
-ATOM   4650  C   ARG C  22     -16.995 -15.291  97.690  1.00 32.99           C  
-ATOM   4651  O   ARG C  22     -17.967 -14.957  98.396  1.00 32.25           O  
-ATOM   4652  CB  ARG C  22     -16.717 -17.783  97.422  1.00 33.55           C  
-ATOM   4653  CG  ARG C  22     -18.149 -18.071  97.837  1.00 36.41           C  
-ATOM   4654  CD  ARG C  22     -18.914 -18.999  96.883  1.00 41.47           C  
-ATOM   4655  NE  ARG C  22     -20.350 -18.937  97.150  1.00 44.48           N  
-ATOM   4656  CZ  ARG C  22     -20.982 -19.671  98.059  1.00 47.35           C  
-ATOM   4657  NH1 ARG C  22     -20.323 -20.565  98.794  1.00 48.46           N  
-ATOM   4658  NH2 ARG C  22     -22.291 -19.520  98.227  1.00 49.32           N  
-ATOM   4659  N   ASN C  23     -16.630 -14.638  96.593  1.00 32.66           N  
-ATOM   4660  CA  ASN C  23     -17.405 -13.529  96.078  1.00 32.51           C  
-ATOM   4661  C   ASN C  23     -18.628 -14.080  95.372  1.00 32.70           C  
-ATOM   4662  O   ASN C  23     -18.511 -14.725  94.330  1.00 33.08           O  
-ATOM   4663  CB  ASN C  23     -16.559 -12.683  95.124  1.00 32.39           C  
-ATOM   4664  CG  ASN C  23     -17.209 -11.349  94.794  1.00 31.90           C  
-ATOM   4665  OD1 ASN C  23     -18.345 -11.302  94.315  1.00 29.57           O  
-ATOM   4666  ND2 ASN C  23     -16.489 -10.254  95.056  1.00 31.30           N  
-ATOM   4667  N   LYS C  24     -19.800 -13.822  95.941  1.00 32.72           N  
-ATOM   4668  CA  LYS C  24     -21.055 -14.335  95.404  1.00 33.12           C  
-ATOM   4669  C   LYS C  24     -21.263 -13.945  93.939  1.00 33.19           C  
-ATOM   4670  O   LYS C  24     -21.791 -14.731  93.146  1.00 33.73           O  
-ATOM   4671  CB  LYS C  24     -22.233 -13.839  96.239  1.00 33.41           C  
-ATOM   4672  CG  LYS C  24     -22.305 -14.414  97.650  1.00 34.67           C  
-ATOM   4673  CD  LYS C  24     -23.389 -13.712  98.463  1.00 36.36           C  
-ATOM   4674  CE  LYS C  24     -23.300 -14.093  99.929  1.00 37.67           C  
-ATOM   4675  NZ  LYS C  24     -24.005 -13.093 100.788  1.00 40.44           N  
-ATOM   4676  N   LEU C  25     -20.833 -12.738  93.585  1.00 32.66           N  
-ATOM   4677  CA  LEU C  25     -21.086 -12.190  92.258  1.00 32.05           C  
-ATOM   4678  C   LEU C  25     -20.070 -12.622  91.202  1.00 31.49           C  
-ATOM   4679  O   LEU C  25     -20.452 -12.937  90.073  1.00 31.50           O  
-ATOM   4680  CB  LEU C  25     -21.189 -10.663  92.333  1.00 32.06           C  
-ATOM   4681  CG  LEU C  25     -22.473 -10.153  93.000  1.00 31.67           C  
-ATOM   4682  CD1 LEU C  25     -22.363  -8.663  93.328  1.00 31.07           C  
-ATOM   4683  CD2 LEU C  25     -23.698 -10.442  92.127  1.00 30.36           C  
-ATOM   4684  N   THR C  26     -18.787 -12.632  91.565  1.00 30.66           N  
-ATOM   4685  CA  THR C  26     -17.719 -12.956  90.614  1.00 29.81           C  
-ATOM   4686  C   THR C  26     -17.230 -14.413  90.685  1.00 29.68           C  
-ATOM   4687  O   THR C  26     -16.620 -14.918  89.741  1.00 29.52           O  
-ATOM   4688  CB  THR C  26     -16.525 -11.998  90.795  1.00 29.91           C  
-ATOM   4689  OG1 THR C  26     -15.883 -12.254  92.053  1.00 28.38           O  
-ATOM   4690  CG2 THR C  26     -16.994 -10.539  90.907  1.00 29.64           C  
-ATOM   4691  N   GLY C  27     -17.487 -15.071  91.811  1.00 29.47           N  
-ATOM   4692  CA  GLY C  27     -16.998 -16.416  92.047  1.00 29.27           C  
-ATOM   4693  C   GLY C  27     -15.579 -16.479  92.581  1.00 29.17           C  
-ATOM   4694  O   GLY C  27     -15.070 -17.573  92.832  1.00 29.71           O  
-ATOM   4695  N   GLU C  28     -14.930 -15.326  92.749  1.00 28.58           N  
-ATOM   4696  CA  GLU C  28     -13.569 -15.301  93.268  1.00 28.18           C  
-ATOM   4697  C   GLU C  28     -13.500 -15.820  94.695  1.00 28.05           C  
-ATOM   4698  O   GLU C  28     -14.335 -15.481  95.533  1.00 28.12           O  
-ATOM   4699  CB  GLU C  28     -12.962 -13.895  93.222  1.00 28.18           C  
-ATOM   4700  CG  GLU C  28     -11.489 -13.887  93.615  1.00 28.52           C  
-ATOM   4701  CD  GLU C  28     -10.894 -12.504  93.699  1.00 29.89           C  
-ATOM   4702  OE1 GLU C  28     -11.649 -11.547  93.956  1.00 30.75           O  
-ATOM   4703  OE2 GLU C  28      -9.663 -12.383  93.498  1.00 31.65           O  
-ATOM   4704  N   VAL C  29     -12.483 -16.634  94.952  1.00 27.66           N  
-ATOM   4705  CA  VAL C  29     -12.210 -17.158  96.279  1.00 27.28           C  
-ATOM   4706  C   VAL C  29     -11.165 -16.268  96.946  1.00 26.68           C  
-ATOM   4707  O   VAL C  29     -10.111 -15.988  96.379  1.00 26.56           O  
-ATOM   4708  CB  VAL C  29     -11.729 -18.634  96.221  1.00 27.55           C  
-ATOM   4709  CG1 VAL C  29     -11.566 -19.218  97.636  1.00 27.10           C  
-ATOM   4710  CG2 VAL C  29     -12.712 -19.472  95.412  1.00 27.55           C  
-ATOM   4711  N   VAL C  30     -11.481 -15.806  98.146  1.00 26.41           N  
-ATOM   4712  CA  VAL C  30     -10.601 -14.891  98.867  1.00 26.20           C  
-ATOM   4713  C   VAL C  30     -10.368 -15.360 100.303  1.00 26.51           C  
-ATOM   4714  O   VAL C  30     -11.043 -16.282 100.796  1.00 26.19           O  
-ATOM   4715  CB  VAL C  30     -11.181 -13.442  98.892  1.00 26.02           C  
-ATOM   4716  CG1 VAL C  30     -11.421 -12.917  97.483  1.00 24.64           C  
-ATOM   4717  CG2 VAL C  30     -12.459 -13.381  99.719  1.00 25.93           C  
-ATOM   4718  N   ALA C  31      -9.414 -14.712 100.967  1.00 26.89           N  
-ATOM   4719  CA  ALA C  31      -9.264 -14.822 102.411  1.00 27.52           C  
-ATOM   4720  C   ALA C  31      -9.599 -13.471 103.015  1.00 28.16           C  
-ATOM   4721  O   ALA C  31      -9.053 -12.444 102.601  1.00 28.36           O  
-ATOM   4722  CB  ALA C  31      -7.849 -15.238 102.788  1.00 27.39           C  
-ATOM   4723  N   LEU C  32     -10.512 -13.478 103.975  1.00 28.83           N  
-ATOM   4724  CA  LEU C  32     -10.887 -12.277 104.691  1.00 29.74           C  
-ATOM   4725  C   LEU C  32     -10.232 -12.310 106.052  1.00 30.27           C  
-ATOM   4726  O   LEU C  32     -10.436 -13.252 106.825  1.00 30.54           O  
-ATOM   4727  CB  LEU C  32     -12.408 -12.183 104.840  1.00 29.88           C  
-ATOM   4728  CG  LEU C  32     -13.210 -12.314 103.543  1.00 30.55           C  
-ATOM   4729  CD1 LEU C  32     -14.681 -12.539 103.859  1.00 30.80           C  
-ATOM   4730  CD2 LEU C  32     -13.016 -11.076 102.674  1.00 29.54           C  
-ATOM   4731  N   LYS C  33      -9.418 -11.296 106.322  1.00 30.60           N  
-ATOM   4732  CA  LYS C  33      -8.758 -11.142 107.607  1.00 31.08           C  
-ATOM   4733  C   LYS C  33      -9.516 -10.081 108.394  1.00 31.65           C  
-ATOM   4734  O   LYS C  33      -9.449  -8.897 108.070  1.00 31.63           O  
-ATOM   4735  CB  LYS C  33      -7.308 -10.715 107.392  1.00 30.95           C  
-ATOM   4736  CG  LYS C  33      -6.432 -10.694 108.630  1.00 30.19           C  
-ATOM   4737  CD  LYS C  33      -4.988 -10.908 108.220  1.00 30.60           C  
-ATOM   4738  CE  LYS C  33      -4.017 -10.141 109.092  1.00 31.50           C  
-ATOM   4739  NZ  LYS C  33      -2.598 -10.459 108.726  1.00 33.48           N  
-ATOM   4740  N   LYS C  34     -10.235 -10.522 109.421  1.00 32.30           N  
-ATOM   4741  CA  LYS C  34     -11.035  -9.644 110.261  1.00 33.32           C  
-ATOM   4742  C   LYS C  34     -10.177  -8.996 111.345  1.00 33.43           C  
-ATOM   4743  O   LYS C  34      -9.493  -9.686 112.094  1.00 33.27           O  
-ATOM   4744  CB  LYS C  34     -12.170 -10.442 110.896  1.00 33.47           C  
-ATOM   4745  CG  LYS C  34     -13.257  -9.599 111.529  1.00 35.79           C  
-ATOM   4746  CD  LYS C  34     -13.836 -10.285 112.768  1.00 40.19           C  
-ATOM   4747  CE  LYS C  34     -15.059 -11.134 112.420  1.00 42.32           C  
-ATOM   4748  NZ  LYS C  34     -15.216 -12.294 113.363  1.00 44.25           N  
-ATOM   4749  N   ILE C  35     -10.210  -7.666 111.402  1.00 33.83           N  
-ATOM   4750  CA  ILE C  35      -9.485  -6.894 112.406  1.00 34.19           C  
-ATOM   4751  C   ILE C  35     -10.491  -6.147 113.277  1.00 34.90           C  
-ATOM   4752  O   ILE C  35     -11.138  -5.200 112.815  1.00 34.52           O  
-ATOM   4753  CB  ILE C  35      -8.522  -5.872 111.737  1.00 34.32           C  
-ATOM   4754  CG1 ILE C  35      -7.607  -6.536 110.685  1.00 33.79           C  
-ATOM   4755  CG2 ILE C  35      -7.742  -5.074 112.802  1.00 33.60           C  
-ATOM   4756  CD1 ILE C  35      -6.437  -7.326 111.247  1.00 33.65           C  
-ATOM   4757  N   ARG C  36     -10.629  -6.561 114.534  1.00 35.82           N  
-ATOM   4758  CA  ARG C  36     -11.555  -5.869 115.425  1.00 37.38           C  
-ATOM   4759  C   ARG C  36     -11.001  -4.511 115.825  1.00 37.11           C  
-ATOM   4760  O   ARG C  36      -9.821  -4.373 116.151  1.00 36.63           O  
-ATOM   4761  CB  ARG C  36     -11.915  -6.692 116.659  1.00 38.41           C  
-ATOM   4762  CG  ARG C  36     -13.382  -6.521 117.080  1.00 42.25           C  
-ATOM   4763  CD  ARG C  36     -13.824  -7.428 118.231  1.00 49.09           C  
-ATOM   4764  NE  ARG C  36     -14.691  -8.520 117.781  1.00 53.75           N  
-ATOM   4765  CZ  ARG C  36     -14.284  -9.771 117.565  1.00 56.24           C  
-ATOM   4766  NH1 ARG C  36     -13.009 -10.114 117.756  1.00 57.65           N  
-ATOM   4767  NH2 ARG C  36     -15.158 -10.687 117.157  1.00 57.31           N  
-ATOM   4768  N   LEU C  37     -11.862  -3.505 115.749  1.00 37.29           N  
-ATOM   4769  CA  LEU C  37     -11.489  -2.159 116.136  1.00 37.38           C  
-ATOM   4770  C   LEU C  37     -12.115  -1.880 117.491  1.00 37.82           C  
-ATOM   4771  O   LEU C  37     -13.306  -2.148 117.712  1.00 37.95           O  
-ATOM   4772  CB  LEU C  37     -11.954  -1.136 115.092  1.00 37.09           C  
-ATOM   4773  CG  LEU C  37     -11.615  -1.364 113.610  1.00 36.46           C  
-ATOM   4774  CD1 LEU C  37     -12.359  -0.379 112.728  1.00 35.13           C  
-ATOM   4775  CD2 LEU C  37     -10.119  -1.291 113.339  1.00 36.01           C  
-ATOM   4776  N   ASP C  38     -11.314  -1.369 118.415  1.00 38.07           N  
-ATOM   4777  CA  ASP C  38     -11.882  -0.953 119.686  1.00 38.22           C  
-ATOM   4778  C   ASP C  38     -12.204   0.527 119.635  1.00 37.46           C  
-ATOM   4779  O   ASP C  38     -11.420   1.390 120.043  1.00 37.28           O  
-ATOM   4780  CB  ASP C  38     -11.017  -1.353 120.879  1.00 38.86           C  
-ATOM   4781  CG  ASP C  38      -9.559  -1.330 120.571  1.00 40.34           C  
-ATOM   4782  OD1 ASP C  38      -9.052  -0.228 120.281  1.00 44.15           O  
-ATOM   4783  OD2 ASP C  38      -8.842  -2.360 120.608  1.00 41.69           O  
-ATOM   4784  N   THR C  39     -13.386   0.770 119.085  1.00 36.77           N  
-ATOM   4785  CA  THR C  39     -13.974   2.073 118.830  1.00 36.46           C  
-ATOM   4786  C   THR C  39     -13.954   2.951 120.064  1.00 36.10           C  
-ATOM   4787  O   THR C  39     -13.944   4.174 119.982  1.00 36.68           O  
-ATOM   4788  CB  THR C  39     -15.410   1.842 118.399  1.00 36.53           C  
-ATOM   4789  OG1 THR C  39     -15.990   0.853 119.264  1.00 36.11           O  
-ATOM   4790  CG2 THR C  39     -15.430   1.176 117.034  1.00 36.57           C  
-ATOM   4791  N   GLU C  40     -13.999   2.301 121.210  1.00 35.47           N  
-ATOM   4792  CA  GLU C  40     -13.632   2.924 122.447  1.00 35.12           C  
-ATOM   4793  C   GLU C  40     -12.422   2.146 122.923  1.00 35.16           C  
-ATOM   4794  O   GLU C  40     -12.423   0.890 122.919  1.00 35.62           O  
-ATOM   4795  CB  GLU C  40     -14.784   2.976 123.468  1.00 35.11           C  
-ATOM   4796  CG  GLU C  40     -15.574   1.698 123.709  1.00 34.48           C  
-ATOM   4797  CD  GLU C  40     -16.256   1.145 122.469  1.00 33.93           C  
-ATOM   4798  OE1 GLU C  40     -16.880   1.917 121.706  1.00 33.36           O  
-ATOM   4799  OE2 GLU C  40     -16.163  -0.083 122.261  1.00 33.62           O  
-ATOM   4800  N   THR C  41     -11.390   2.929 123.247  1.00 33.77           N  
-ATOM   4801  CA  THR C  41     -10.074   2.559 123.793  1.00 33.14           C  
-ATOM   4802  C   THR C  41      -8.953   2.981 122.850  1.00 32.41           C  
-ATOM   4803  O   THR C  41      -8.650   4.170 122.778  1.00 32.43           O  
-ATOM   4804  CB  THR C  41      -9.910   1.097 124.327  1.00 32.92           C  
-ATOM   4805  OG1 THR C  41     -10.331   0.148 123.346  1.00 33.88           O  
-ATOM   4806  CG2 THR C  41     -10.831   0.844 125.527  1.00 34.07           C  
-ATOM   4807  N   GLU C  42      -8.369   2.044 122.111  1.00 31.57           N  
-ATOM   4808  CA  GLU C  42      -7.130   2.334 121.400  1.00 31.57           C  
-ATOM   4809  C   GLU C  42      -7.274   2.593 119.894  1.00 30.15           C  
-ATOM   4810  O   GLU C  42      -6.299   2.942 119.232  1.00 29.70           O  
-ATOM   4811  CB  GLU C  42      -6.079   1.256 121.691  1.00 31.78           C  
-ATOM   4812  CG  GLU C  42      -5.472   1.309 123.096  1.00 36.19           C  
-ATOM   4813  CD  GLU C  42      -5.230   2.724 123.631  1.00 41.08           C  
-ATOM   4814  OE1 GLU C  42      -4.366   3.465 123.087  1.00 43.92           O  
-ATOM   4815  OE2 GLU C  42      -5.902   3.094 124.620  1.00 43.85           O  
-ATOM   4816  N   GLY C  43      -8.482   2.422 119.361  1.00 28.96           N  
-ATOM   4817  CA  GLY C  43      -8.732   2.665 117.948  1.00 27.55           C  
-ATOM   4818  C   GLY C  43      -8.181   1.567 117.061  1.00 26.68           C  
-ATOM   4819  O   GLY C  43      -8.184   0.398 117.452  1.00 26.36           O  
-ATOM   4820  N   VAL C  44      -7.712   1.943 115.868  1.00 25.69           N  
-ATOM   4821  CA  VAL C  44      -7.234   0.979 114.880  1.00 24.34           C  
-ATOM   4822  C   VAL C  44      -5.858   0.522 115.332  1.00 24.20           C  
-ATOM   4823  O   VAL C  44      -4.979   1.366 115.571  1.00 24.46           O  
-ATOM   4824  CB  VAL C  44      -7.172   1.587 113.430  1.00 24.71           C  
-ATOM   4825  CG1 VAL C  44      -6.773   0.520 112.399  1.00 23.65           C  
-ATOM   4826  CG2 VAL C  44      -8.504   2.222 113.025  1.00 23.13           C  
-ATOM   4827  N   PRO C  45      -5.656  -0.789 115.488  1.00 23.78           N  
-ATOM   4828  CA  PRO C  45      -4.367  -1.291 115.991  1.00 24.00           C  
-ATOM   4829  C   PRO C  45      -3.210  -0.910 115.072  1.00 24.55           C  
-ATOM   4830  O   PRO C  45      -3.379  -0.871 113.845  1.00 24.98           O  
-ATOM   4831  CB  PRO C  45      -4.541  -2.818 116.034  1.00 24.05           C  
-ATOM   4832  CG  PRO C  45      -5.840  -3.131 115.357  1.00 23.96           C  
-ATOM   4833  CD  PRO C  45      -6.629  -1.871 115.236  1.00 23.58           C  
-ATOM   4834  N   SER C  46      -2.054  -0.633 115.661  1.00 24.64           N  
-ATOM   4835  CA  SER C  46      -0.903  -0.179 114.895  1.00 25.46           C  
-ATOM   4836  C   SER C  46      -0.402  -1.236 113.918  1.00 25.67           C  
-ATOM   4837  O   SER C  46       0.112  -0.883 112.849  1.00 25.85           O  
-ATOM   4838  CB  SER C  46       0.228   0.261 115.822  1.00 25.52           C  
-ATOM   4839  OG  SER C  46       0.760  -0.856 116.508  1.00 26.25           O  
-ATOM   4840  N   THR C  47      -0.543  -2.517 114.278  1.00 25.40           N  
-ATOM   4841  CA  THR C  47      -0.170  -3.618 113.381  1.00 25.69           C  
-ATOM   4842  C   THR C  47      -0.986  -3.579 112.089  1.00 25.61           C  
-ATOM   4843  O   THR C  47      -0.446  -3.797 111.005  1.00 25.62           O  
-ATOM   4844  CB  THR C  47      -0.338  -5.007 114.062  1.00 25.92           C  
-ATOM   4845  OG1 THR C  47      -1.603  -5.059 114.728  1.00 26.93           O  
-ATOM   4846  CG2 THR C  47       0.662  -5.188 115.211  1.00 26.42           C  
-ATOM   4847  N   ALA C  48      -2.286  -3.305 112.216  1.00 25.35           N  
-ATOM   4848  CA  ALA C  48      -3.183  -3.220 111.065  1.00 25.43           C  
-ATOM   4849  C   ALA C  48      -2.870  -2.010 110.183  1.00 25.41           C  
-ATOM   4850  O   ALA C  48      -2.889  -2.116 108.960  1.00 25.45           O  
-ATOM   4851  CB  ALA C  48      -4.638  -3.202 111.511  1.00 25.17           C  
-ATOM   4852  N   ILE C  49      -2.563  -0.877 110.812  1.00 25.31           N  
-ATOM   4853  CA  ILE C  49      -2.131   0.324 110.093  1.00 25.31           C  
-ATOM   4854  C   ILE C  49      -0.854   0.067 109.280  1.00 25.62           C  
-ATOM   4855  O   ILE C  49      -0.762   0.470 108.107  1.00 25.55           O  
-ATOM   4856  CB  ILE C  49      -1.948   1.516 111.080  1.00 25.27           C  
-ATOM   4857  CG1 ILE C  49      -3.309   2.097 111.465  1.00 24.53           C  
-ATOM   4858  CG2 ILE C  49      -1.031   2.598 110.494  1.00 24.81           C  
-ATOM   4859  CD1 ILE C  49      -3.308   2.839 112.778  1.00 24.90           C  
-ATOM   4860  N   ARG C  50       0.111  -0.620 109.890  1.00 25.51           N  
-ATOM   4861  CA  ARG C  50       1.351  -0.965 109.191  1.00 25.69           C  
-ATOM   4862  C   ARG C  50       1.108  -1.982 108.075  1.00 26.13           C  
-ATOM   4863  O   ARG C  50       1.495  -1.736 106.934  1.00 26.34           O  
-ATOM   4864  CB  ARG C  50       2.420  -1.467 110.160  1.00 25.48           C  
-ATOM   4865  CG  ARG C  50       3.090  -0.376 110.985  1.00 24.45           C  
-ATOM   4866  CD  ARG C  50       4.158  -0.907 111.923  1.00 24.27           C  
-ATOM   4867  NE  ARG C  50       4.843   0.143 112.676  1.00 24.29           N  
-ATOM   4868  CZ  ARG C  50       5.650  -0.087 113.713  1.00 23.98           C  
-ATOM   4869  NH1 ARG C  50       5.868  -1.333 114.132  1.00 22.31           N  
-ATOM   4870  NH2 ARG C  50       6.242   0.927 114.336  1.00 21.89           N  
-ATOM   4871  N   GLU C  51       0.450  -3.103 108.387  1.00 26.50           N  
-ATOM   4872  CA  GLU C  51       0.175  -4.132 107.375  1.00 26.78           C  
-ATOM   4873  C   GLU C  51      -0.489  -3.542 106.128  1.00 26.49           C  
-ATOM   4874  O   GLU C  51       0.013  -3.730 105.028  1.00 26.24           O  
-ATOM   4875  CB  GLU C  51      -0.679  -5.290 107.925  1.00 27.08           C  
-ATOM   4876  CG  GLU C  51      -1.157  -6.254 106.839  1.00 28.91           C  
-ATOM   4877  CD  GLU C  51      -1.483  -7.662 107.333  1.00 32.73           C  
-ATOM   4878  OE1 GLU C  51      -2.114  -7.793 108.402  1.00 33.98           O  
-ATOM   4879  OE2 GLU C  51      -1.116  -8.645 106.636  1.00 34.26           O  
-ATOM   4880  N   ILE C  52      -1.605  -2.836 106.313  1.00 26.19           N  
-ATOM   4881  CA  ILE C  52      -2.352  -2.249 105.203  1.00 26.52           C  
-ATOM   4882  C   ILE C  52      -1.552  -1.192 104.423  1.00 27.09           C  
-ATOM   4883  O   ILE C  52      -1.497  -1.241 103.190  1.00 27.04           O  
-ATOM   4884  CB  ILE C  52      -3.720  -1.684 105.667  1.00 26.21           C  
-ATOM   4885  CG1 ILE C  52      -4.571  -2.791 106.308  1.00 27.07           C  
-ATOM   4886  CG2 ILE C  52      -4.475  -1.079 104.480  1.00 25.94           C  
-ATOM   4887  CD1 ILE C  52      -5.761  -2.286 107.107  1.00 27.19           C  
-ATOM   4888  N   SER C  53      -0.938  -0.246 105.126  1.00 27.45           N  
-ATOM   4889  CA  SER C  53      -0.202   0.812 104.444  1.00 29.05           C  
-ATOM   4890  C   SER C  53       0.960   0.238 103.626  1.00 30.03           C  
-ATOM   4891  O   SER C  53       1.140   0.599 102.467  1.00 30.38           O  
-ATOM   4892  CB  SER C  53       0.287   1.892 105.424  1.00 28.48           C  
-ATOM   4893  OG  SER C  53       1.225   1.369 106.347  1.00 29.00           O  
-ATOM   4894  N   LEU C  54       1.727  -0.668 104.231  1.00 31.11           N  
-ATOM   4895  CA  LEU C  54       2.884  -1.266 103.569  1.00 31.98           C  
-ATOM   4896  C   LEU C  54       2.483  -2.195 102.432  1.00 32.83           C  
-ATOM   4897  O   LEU C  54       3.146  -2.230 101.386  1.00 32.70           O  
-ATOM   4898  CB  LEU C  54       3.771  -1.992 104.581  1.00 31.80           C  
-ATOM   4899  CG  LEU C  54       4.328  -1.111 105.706  1.00 31.74           C  
-ATOM   4900  CD1 LEU C  54       5.102  -1.943 106.715  1.00 30.76           C  
-ATOM   4901  CD2 LEU C  54       5.194   0.018 105.160  1.00 30.99           C  
-ATOM   4902  N   LEU C  55       1.387  -2.927 102.630  1.00 33.91           N  
-ATOM   4903  CA  LEU C  55       0.896  -3.862 101.621  1.00 35.11           C  
-ATOM   4904  C   LEU C  55       0.384  -3.156 100.367  1.00 36.11           C  
-ATOM   4905  O   LEU C  55       0.460  -3.708  99.267  1.00 36.13           O  
-ATOM   4906  CB  LEU C  55      -0.178  -4.774 102.199  1.00 35.19           C  
-ATOM   4907  CG  LEU C  55       0.001  -6.292 102.077  1.00 35.57           C  
-ATOM   4908  CD1 LEU C  55       1.461  -6.710 101.924  1.00 36.31           C  
-ATOM   4909  CD2 LEU C  55      -0.627  -6.963 103.267  1.00 34.19           C  
-ATOM   4910  N   LYS C  56      -0.120  -1.936 100.536  1.00 37.00           N  
-ATOM   4911  CA  LYS C  56      -0.570  -1.123  99.407  1.00 38.12           C  
-ATOM   4912  C   LYS C  56       0.588  -0.734  98.480  1.00 38.66           C  
-ATOM   4913  O   LYS C  56       0.386  -0.534  97.291  1.00 39.02           O  
-ATOM   4914  CB  LYS C  56      -1.340   0.114  99.897  1.00 38.25           C  
-ATOM   4915  CG  LYS C  56      -2.773  -0.206 100.351  1.00 38.98           C  
-ATOM   4916  CD  LYS C  56      -3.623   1.036 100.495  1.00 40.96           C  
-ATOM   4917  CE  LYS C  56      -4.260   1.425  99.164  1.00 41.86           C  
-ATOM   4918  NZ  LYS C  56      -4.433   2.902  99.054  1.00 43.25           N  
-ATOM   4919  N   GLU C  57       1.798  -0.648  99.027  1.00 39.51           N  
-ATOM   4920  CA  GLU C  57       2.986  -0.307  98.244  1.00 40.21           C  
-ATOM   4921  C   GLU C  57       3.673  -1.513  97.604  1.00 40.22           C  
-ATOM   4922  O   GLU C  57       4.400  -1.364  96.617  1.00 40.78           O  
-ATOM   4923  CB  GLU C  57       4.004   0.427  99.109  1.00 40.54           C  
-ATOM   4924  CG  GLU C  57       3.406   1.487 100.009  1.00 42.67           C  
-ATOM   4925  CD  GLU C  57       4.262   2.723 100.098  1.00 44.77           C  
-ATOM   4926  OE1 GLU C  57       5.504   2.612  99.978  1.00 46.24           O  
-ATOM   4927  OE2 GLU C  57       3.685   3.810 100.297  1.00 47.46           O  
-ATOM   4928  N   LEU C  58       3.453  -2.699  98.162  1.00 39.93           N  
-ATOM   4929  CA  LEU C  58       4.172  -3.885  97.713  1.00 39.69           C  
-ATOM   4930  C   LEU C  58       3.371  -4.719  96.707  1.00 39.59           C  
-ATOM   4931  O   LEU C  58       2.733  -5.714  97.061  1.00 39.99           O  
-ATOM   4932  CB  LEU C  58       4.655  -4.721  98.909  1.00 39.21           C  
-ATOM   4933  CG  LEU C  58       5.521  -3.995  99.952  1.00 39.32           C  
-ATOM   4934  CD1 LEU C  58       5.585  -4.784 101.251  1.00 38.63           C  
-ATOM   4935  CD2 LEU C  58       6.931  -3.688  99.448  1.00 38.49           C  
-ATOM   4936  N   ASN C  59       3.412  -4.295  95.448  1.00 39.30           N  
-ATOM   4937  CA  ASN C  59       2.781  -5.031  94.354  1.00 39.00           C  
-ATOM   4938  C   ASN C  59       3.836  -5.864  93.630  1.00 38.03           C  
-ATOM   4939  O   ASN C  59       4.631  -5.333  92.854  1.00 37.87           O  
-ATOM   4940  CB  ASN C  59       2.080  -4.058  93.402  1.00 39.23           C  
-ATOM   4941  CG  ASN C  59       1.245  -4.763  92.338  1.00 42.33           C  
-ATOM   4942  OD1 ASN C  59       1.420  -4.522  91.133  1.00 45.69           O  
-ATOM   4943  ND2 ASN C  59       0.324  -5.624  92.772  1.00 44.53           N  
-ATOM   4944  N   HIS C  60       3.852  -7.166  93.918  1.00 36.81           N  
-ATOM   4945  CA  HIS C  60       4.848  -8.093  93.373  1.00 35.93           C  
-ATOM   4946  C   HIS C  60       4.284  -9.516  93.397  1.00 34.80           C  
-ATOM   4947  O   HIS C  60       3.595  -9.883  94.346  1.00 35.00           O  
-ATOM   4948  CB  HIS C  60       6.158  -8.011  94.171  1.00 36.21           C  
-ATOM   4949  CG  HIS C  60       7.274  -8.828  93.596  1.00 37.64           C  
-ATOM   4950  ND1 HIS C  60       8.290  -8.278  92.841  1.00 38.49           N  
-ATOM   4951  CD2 HIS C  60       7.538 -10.155  93.668  1.00 38.04           C  
-ATOM   4952  CE1 HIS C  60       9.125  -9.231  92.469  1.00 38.07           C  
-ATOM   4953  NE2 HIS C  60       8.689 -10.380  92.953  1.00 38.72           N  
-ATOM   4954  N   PRO C  61       4.545 -10.307  92.352  1.00 33.61           N  
-ATOM   4955  CA  PRO C  61       3.993 -11.670  92.258  1.00 32.57           C  
-ATOM   4956  C   PRO C  61       4.268 -12.598  93.463  1.00 31.33           C  
-ATOM   4957  O   PRO C  61       3.535 -13.570  93.642  1.00 30.80           O  
-ATOM   4958  CB  PRO C  61       4.649 -12.236  90.985  1.00 32.51           C  
-ATOM   4959  CG  PRO C  61       5.766 -11.297  90.649  1.00 33.04           C  
-ATOM   4960  CD  PRO C  61       5.341  -9.956  91.157  1.00 33.54           C  
-ATOM   4961  N   ASN C  62       5.284 -12.293  94.265  1.00 30.18           N  
-ATOM   4962  CA  ASN C  62       5.649 -13.134  95.411  1.00 29.34           C  
-ATOM   4963  C   ASN C  62       5.371 -12.488  96.768  1.00 28.73           C  
-ATOM   4964  O   ASN C  62       6.048 -12.756  97.764  1.00 28.66           O  
-ATOM   4965  CB  ASN C  62       7.095 -13.595  95.302  1.00 28.74           C  
-ATOM   4966  CG  ASN C  62       7.353 -14.376  94.040  1.00 29.40           C  
-ATOM   4967  OD1 ASN C  62       8.191 -13.988  93.220  1.00 30.65           O  
-ATOM   4968  ND2 ASN C  62       6.622 -15.479  93.859  1.00 27.27           N  
-ATOM   4969  N   ILE C  63       4.359 -11.631  96.786  1.00 28.05           N  
-ATOM   4970  CA  ILE C  63       3.878 -11.009  98.008  1.00 27.08           C  
-ATOM   4971  C   ILE C  63       2.369 -11.140  97.935  1.00 26.98           C  
-ATOM   4972  O   ILE C  63       1.768 -10.855  96.902  1.00 26.94           O  
-ATOM   4973  CB  ILE C  63       4.347  -9.528  98.095  1.00 26.88           C  
-ATOM   4974  CG1 ILE C  63       5.868  -9.458  98.262  1.00 25.21           C  
-ATOM   4975  CG2 ILE C  63       3.653  -8.790  99.242  1.00 27.15           C  
-ATOM   4976  CD1 ILE C  63       6.479  -8.122  97.910  1.00 24.51           C  
-ATOM   4977  N   VAL C  64       1.759 -11.635  99.002  1.00 26.78           N  
-ATOM   4978  CA  VAL C  64       0.309 -11.797  99.022  1.00 26.90           C  
-ATOM   4979  C   VAL C  64      -0.361 -10.477  98.598  1.00 26.61           C  
-ATOM   4980  O   VAL C  64       0.043  -9.408  99.039  1.00 26.46           O  
-ATOM   4981  CB  VAL C  64      -0.184 -12.288 100.412  1.00 26.91           C  
-ATOM   4982  CG1 VAL C  64       0.049 -11.236 101.491  1.00 26.64           C  
-ATOM   4983  CG2 VAL C  64      -1.655 -12.717 100.357  1.00 27.60           C  
-ATOM   4984  N   LYS C  65      -1.346 -10.562  97.708  1.00 26.78           N  
-ATOM   4985  CA  LYS C  65      -2.023  -9.378  97.197  1.00 27.07           C  
-ATOM   4986  C   LYS C  65      -3.230  -8.969  98.041  1.00 26.74           C  
-ATOM   4987  O   LYS C  65      -4.169  -9.750  98.234  1.00 26.60           O  
-ATOM   4988  CB  LYS C  65      -2.444  -9.581  95.737  1.00 27.81           C  
-ATOM   4989  CG  LYS C  65      -2.900  -8.306  95.039  1.00 29.56           C  
-ATOM   4990  CD  LYS C  65      -3.450  -8.635  93.651  1.00 34.77           C  
-ATOM   4991  CE  LYS C  65      -3.653  -7.378  92.809  1.00 37.24           C  
-ATOM   4992  NZ  LYS C  65      -4.587  -6.383  93.446  1.00 39.18           N  
-ATOM   4993  N   LEU C  66      -3.180  -7.740  98.549  1.00 26.26           N  
-ATOM   4994  CA  LEU C  66      -4.327  -7.125  99.195  1.00 26.40           C  
-ATOM   4995  C   LEU C  66      -5.265  -6.574  98.122  1.00 26.65           C  
-ATOM   4996  O   LEU C  66      -4.898  -5.687  97.354  1.00 26.98           O  
-ATOM   4997  CB  LEU C  66      -3.883  -6.031 100.166  1.00 25.85           C  
-ATOM   4998  CG  LEU C  66      -4.925  -5.295 101.013  1.00 25.87           C  
-ATOM   4999  CD1 LEU C  66      -5.507  -6.182 102.112  1.00 25.07           C  
-ATOM   5000  CD2 LEU C  66      -4.279  -4.056 101.621  1.00 25.95           C  
-ATOM   5001  N   LEU C  67      -6.469  -7.124  98.065  1.00 26.90           N  
-ATOM   5002  CA  LEU C  67      -7.436  -6.752  97.044  1.00 27.67           C  
-ATOM   5003  C   LEU C  67      -8.327  -5.598  97.482  1.00 28.31           C  
-ATOM   5004  O   LEU C  67      -8.715  -4.773  96.661  1.00 28.32           O  
-ATOM   5005  CB  LEU C  67      -8.300  -7.958  96.646  1.00 27.51           C  
-ATOM   5006  CG  LEU C  67      -7.602  -9.229  96.139  1.00 27.61           C  
-ATOM   5007  CD1 LEU C  67      -8.614 -10.361  96.034  1.00 26.22           C  
-ATOM   5008  CD2 LEU C  67      -6.935  -8.977  94.782  1.00 27.17           C  
-ATOM   5009  N   ASP C  68      -8.653  -5.544  98.772  1.00 29.20           N  
-ATOM   5010  CA  ASP C  68      -9.552  -4.519  99.300  1.00 29.88           C  
-ATOM   5011  C   ASP C  68      -9.434  -4.395 100.816  1.00 30.37           C  
-ATOM   5012  O   ASP C  68      -8.854  -5.256 101.479  1.00 30.17           O  
-ATOM   5013  CB  ASP C  68     -11.006  -4.849  98.927  1.00 29.94           C  
-ATOM   5014  CG  ASP C  68     -11.915  -3.611  98.892  1.00 31.19           C  
-ATOM   5015  OD1 ASP C  68     -11.459  -2.485  99.213  1.00 32.09           O  
-ATOM   5016  OD2 ASP C  68     -13.116  -3.676  98.553  1.00 31.94           O  
-ATOM   5017  N   VAL C  69      -9.983  -3.302 101.343  1.00 31.14           N  
-ATOM   5018  CA  VAL C  69     -10.144  -3.090 102.772  1.00 31.95           C  
-ATOM   5019  C   VAL C  69     -11.573  -2.614 102.937  1.00 32.82           C  
-ATOM   5020  O   VAL C  69     -11.963  -1.590 102.372  1.00 32.82           O  
-ATOM   5021  CB  VAL C  69      -9.157  -2.036 103.330  1.00 31.94           C  
-ATOM   5022  CG1 VAL C  69      -9.413  -1.789 104.813  1.00 31.47           C  
-ATOM   5023  CG2 VAL C  69      -7.713  -2.466 103.107  1.00 31.88           C  
-ATOM   5024  N   ILE C  70     -12.360  -3.380 103.682  1.00 34.03           N  
-ATOM   5025  CA  ILE C  70     -13.779  -3.100 103.835  1.00 35.10           C  
-ATOM   5026  C   ILE C  70     -13.984  -2.529 105.217  1.00 36.08           C  
-ATOM   5027  O   ILE C  70     -13.601  -3.145 106.215  1.00 36.18           O  
-ATOM   5028  CB  ILE C  70     -14.630  -4.370 103.621  1.00 34.91           C  
-ATOM   5029  CG1 ILE C  70     -14.459  -4.888 102.188  1.00 34.97           C  
-ATOM   5030  CG2 ILE C  70     -16.098  -4.081 103.910  1.00 35.00           C  
-ATOM   5031  CD1 ILE C  70     -15.146  -6.212 101.910  1.00 34.68           C  
-ATOM   5032  N   HIS C  71     -14.580  -1.342 105.255  1.00 37.27           N  
-ATOM   5033  CA  HIS C  71     -14.710  -0.572 106.483  1.00 38.60           C  
-ATOM   5034  C   HIS C  71     -16.091  -0.744 107.088  1.00 39.31           C  
-ATOM   5035  O   HIS C  71     -17.103  -0.746 106.380  1.00 39.54           O  
-ATOM   5036  CB  HIS C  71     -14.469   0.918 106.208  1.00 38.59           C  
-ATOM   5037  CG  HIS C  71     -13.024   1.286 106.071  1.00 39.20           C  
-ATOM   5038  ND1 HIS C  71     -12.275   1.759 107.127  1.00 39.12           N  
-ATOM   5039  CD2 HIS C  71     -12.193   1.262 105.001  1.00 39.76           C  
-ATOM   5040  CE1 HIS C  71     -11.043   2.004 106.716  1.00 40.18           C  
-ATOM   5041  NE2 HIS C  71     -10.968   1.712 105.429  1.00 40.46           N  
-ATOM   5042  N   THR C  72     -16.120  -0.907 108.401  1.00 39.92           N  
-ATOM   5043  CA  THR C  72     -17.341  -0.727 109.172  1.00 40.85           C  
-ATOM   5044  C   THR C  72     -16.957   0.119 110.383  1.00 41.51           C  
-ATOM   5045  O   THR C  72     -15.766   0.320 110.647  1.00 41.67           O  
-ATOM   5046  CB  THR C  72     -17.985  -2.086 109.591  1.00 40.88           C  
-ATOM   5047  OG1 THR C  72     -17.169  -2.746 110.567  1.00 40.13           O  
-ATOM   5048  CG2 THR C  72     -18.025  -3.083 108.424  1.00 40.86           C  
-ATOM   5049  N   GLU C  73     -17.951   0.626 111.107  1.00 42.15           N  
-ATOM   5050  CA  GLU C  73     -17.687   1.399 112.324  1.00 42.92           C  
-ATOM   5051  C   GLU C  73     -16.910   0.553 113.333  1.00 42.42           C  
-ATOM   5052  O   GLU C  73     -16.081   1.074 114.073  1.00 42.65           O  
-ATOM   5053  CB  GLU C  73     -19.000   1.924 112.921  1.00 43.22           C  
-ATOM   5054  CG  GLU C  73     -18.952   2.301 114.396  1.00 46.19           C  
-ATOM   5055  CD  GLU C  73     -20.284   2.824 114.918  1.00 49.73           C  
-ATOM   5056  OE1 GLU C  73     -20.618   3.998 114.636  1.00 50.48           O  
-ATOM   5057  OE2 GLU C  73     -20.995   2.062 115.618  1.00 51.78           O  
-ATOM   5058  N   ASN C  74     -17.142  -0.758 113.281  1.00 42.00           N  
-ATOM   5059  CA  ASN C  74     -16.764  -1.721 114.320  1.00 41.47           C  
-ATOM   5060  C   ASN C  74     -15.639  -2.686 113.938  1.00 40.34           C  
-ATOM   5061  O   ASN C  74     -14.909  -3.177 114.804  1.00 40.19           O  
-ATOM   5062  CB  ASN C  74     -18.009  -2.534 114.707  1.00 42.11           C  
-ATOM   5063  CG  ASN C  74     -19.020  -2.664 113.545  1.00 44.47           C  
-ATOM   5064  OD1 ASN C  74     -19.037  -3.669 112.824  1.00 47.53           O  
-ATOM   5065  ND2 ASN C  74     -19.856  -1.638 113.363  1.00 46.46           N  
-ATOM   5066  N   LYS C  75     -15.509  -2.965 112.642  1.00 39.12           N  
-ATOM   5067  CA  LYS C  75     -14.578  -3.983 112.151  1.00 37.81           C  
-ATOM   5068  C   LYS C  75     -13.904  -3.594 110.845  1.00 36.43           C  
-ATOM   5069  O   LYS C  75     -14.468  -2.879 110.026  1.00 36.03           O  
-ATOM   5070  CB  LYS C  75     -15.311  -5.315 111.945  1.00 38.15           C  
-ATOM   5071  CG  LYS C  75     -15.487  -6.142 113.207  1.00 39.41           C  
-ATOM   5072  CD  LYS C  75     -16.110  -7.502 112.919  1.00 42.45           C  
-ATOM   5073  CE  LYS C  75     -17.473  -7.390 112.235  1.00 44.14           C  
-ATOM   5074  NZ  LYS C  75     -18.203  -8.694 112.243  1.00 46.43           N  
-ATOM   5075  N   LEU C  76     -12.690  -4.088 110.660  1.00 35.13           N  
-ATOM   5076  CA  LEU C  76     -11.970  -3.944 109.408  1.00 34.06           C  
-ATOM   5077  C   LEU C  76     -11.816  -5.331 108.773  1.00 33.54           C  
-ATOM   5078  O   LEU C  76     -11.331  -6.258 109.415  1.00 33.13           O  
-ATOM   5079  CB  LEU C  76     -10.597  -3.338 109.686  1.00 33.98           C  
-ATOM   5080  CG  LEU C  76     -10.019  -2.215 108.835  1.00 33.38           C  
-ATOM   5081  CD1 LEU C  76     -10.986  -1.042 108.705  1.00 33.02           C  
-ATOM   5082  CD2 LEU C  76      -8.692  -1.764 109.433  1.00 31.34           C  
-ATOM   5083  N   TYR C  77     -12.247  -5.474 107.522  1.00 33.10           N  
-ATOM   5084  CA  TYR C  77     -12.022  -6.714 106.780  1.00 32.50           C  
-ATOM   5085  C   TYR C  77     -11.040  -6.491 105.645  1.00 31.47           C  
-ATOM   5086  O   TYR C  77     -11.319  -5.715 104.721  1.00 31.09           O  
-ATOM   5087  CB  TYR C  77     -13.326  -7.245 106.198  1.00 33.19           C  
-ATOM   5088  CG  TYR C  77     -14.219  -7.950 107.181  1.00 34.80           C  
-ATOM   5089  CD1 TYR C  77     -14.013  -9.290 107.499  1.00 37.21           C  
-ATOM   5090  CD2 TYR C  77     -15.287  -7.284 107.777  1.00 36.62           C  
-ATOM   5091  CE1 TYR C  77     -14.852  -9.951 108.393  1.00 39.16           C  
-ATOM   5092  CE2 TYR C  77     -16.129  -7.931 108.675  1.00 38.16           C  
-ATOM   5093  CZ  TYR C  77     -15.905  -9.261 108.982  1.00 39.92           C  
-ATOM   5094  OH  TYR C  77     -16.743  -9.908 109.875  1.00 42.55           O  
-ATOM   5095  N   LEU C  78      -9.901  -7.183 105.718  1.00 29.96           N  
-ATOM   5096  CA  LEU C  78      -8.899  -7.154 104.664  1.00 28.74           C  
-ATOM   5097  C   LEU C  78      -9.148  -8.305 103.695  1.00 27.93           C  
-ATOM   5098  O   LEU C  78      -9.225  -9.469 104.095  1.00 27.95           O  
-ATOM   5099  CB  LEU C  78      -7.479  -7.229 105.235  1.00 28.92           C  
-ATOM   5100  CG  LEU C  78      -7.065  -6.488 106.519  1.00 29.62           C  
-ATOM   5101  CD1 LEU C  78      -5.554  -6.429 106.636  1.00 29.26           C  
-ATOM   5102  CD2 LEU C  78      -7.663  -5.101 106.649  1.00 30.10           C  
-ATOM   5103  N   VAL C  79      -9.307  -7.971 102.421  1.00 26.69           N  
-ATOM   5104  CA  VAL C  79      -9.587  -8.973 101.401  1.00 24.95           C  
-ATOM   5105  C   VAL C  79      -8.271  -9.293 100.737  1.00 24.43           C  
-ATOM   5106  O   VAL C  79      -7.614  -8.411 100.200  1.00 23.99           O  
-ATOM   5107  CB  VAL C  79     -10.643  -8.471 100.389  1.00 25.00           C  
-ATOM   5108  CG1 VAL C  79     -11.035  -9.567  99.396  1.00 23.96           C  
-ATOM   5109  CG2 VAL C  79     -11.857  -7.960 101.128  1.00 23.81           C  
-ATOM   5110  N   PHE C  80      -7.868 -10.557 100.851  1.00 24.18           N  
-ATOM   5111  CA  PHE C  80      -6.621 -11.049 100.293  1.00 24.05           C  
-ATOM   5112  C   PHE C  80      -6.948 -12.062  99.215  1.00 24.62           C  
-ATOM   5113  O   PHE C  80      -7.980 -12.728  99.283  1.00 24.33           O  
-ATOM   5114  CB  PHE C  80      -5.780 -11.750 101.370  1.00 23.72           C  
-ATOM   5115  CG  PHE C  80      -5.046 -10.820 102.277  1.00 22.38           C  
-ATOM   5116  CD1 PHE C  80      -3.916 -10.149 101.837  1.00 21.64           C  
-ATOM   5117  CD2 PHE C  80      -5.478 -10.621 103.588  1.00 21.72           C  
-ATOM   5118  CE1 PHE C  80      -3.228  -9.289 102.677  1.00 20.85           C  
-ATOM   5119  CE2 PHE C  80      -4.800  -9.760 104.439  1.00 20.69           C  
-ATOM   5120  CZ  PHE C  80      -3.674  -9.096 103.988  1.00 20.41           C  
-ATOM   5121  N   GLU C  81      -6.077 -12.167  98.217  1.00 25.35           N  
-ATOM   5122  CA  GLU C  81      -6.121 -13.292  97.297  1.00 27.05           C  
-ATOM   5123  C   GLU C  81      -5.999 -14.591  98.108  1.00 27.84           C  
-ATOM   5124  O   GLU C  81      -5.181 -14.679  99.025  1.00 27.00           O  
-ATOM   5125  CB  GLU C  81      -4.982 -13.203  96.278  1.00 27.21           C  
-ATOM   5126  CG  GLU C  81      -3.591 -13.361  96.878  1.00 28.24           C  
-ATOM   5127  CD  GLU C  81      -2.506 -13.507  95.841  1.00 31.04           C  
-ATOM   5128  OE1 GLU C  81      -2.582 -14.446  95.018  1.00 33.83           O  
-ATOM   5129  OE2 GLU C  81      -1.566 -12.688  95.851  1.00 30.90           O  
-ATOM   5130  N   PHE C  82      -6.823 -15.580  97.783  1.00 29.30           N  
-ATOM   5131  CA  PHE C  82      -6.735 -16.873  98.443  1.00 30.80           C  
-ATOM   5132  C   PHE C  82      -5.538 -17.662  97.938  1.00 31.46           C  
-ATOM   5133  O   PHE C  82      -5.302 -17.741  96.735  1.00 31.59           O  
-ATOM   5134  CB  PHE C  82      -8.015 -17.689  98.255  1.00 30.72           C  
-ATOM   5135  CG  PHE C  82      -7.962 -19.042  98.906  1.00 32.06           C  
-ATOM   5136  CD1 PHE C  82      -8.030 -19.165 100.298  1.00 33.30           C  
-ATOM   5137  CD2 PHE C  82      -7.805 -20.192  98.136  1.00 32.48           C  
-ATOM   5138  CE1 PHE C  82      -7.961 -20.422 100.916  1.00 34.23           C  
-ATOM   5139  CE2 PHE C  82      -7.736 -21.452  98.738  1.00 33.60           C  
-ATOM   5140  CZ  PHE C  82      -7.822 -21.571 100.131  1.00 33.96           C  
-ATOM   5141  N   LEU C  83      -4.778 -18.232  98.866  1.00 32.48           N  
-ATOM   5142  CA  LEU C  83      -3.735 -19.195  98.508  1.00 33.97           C  
-ATOM   5143  C   LEU C  83      -4.002 -20.504  99.248  1.00 34.93           C  
-ATOM   5144  O   LEU C  83      -4.756 -20.523 100.219  1.00 35.23           O  
-ATOM   5145  CB  LEU C  83      -2.337 -18.633  98.766  1.00 34.03           C  
-ATOM   5146  CG  LEU C  83      -1.997 -17.451  97.845  1.00 33.92           C  
-ATOM   5147  CD1 LEU C  83      -1.118 -16.425  98.530  1.00 34.65           C  
-ATOM   5148  CD2 LEU C  83      -1.341 -17.948  96.575  1.00 34.81           C  
-ATOM   5149  N   HIS C  84      -3.424 -21.601  98.779  1.00 35.90           N  
-ATOM   5150  CA  HIS C  84      -3.926 -22.918  99.183  1.00 37.11           C  
-ATOM   5151  C   HIS C  84      -3.477 -23.434 100.552  1.00 36.86           C  
-ATOM   5152  O   HIS C  84      -4.268 -24.042 101.271  1.00 36.96           O  
-ATOM   5153  CB  HIS C  84      -3.743 -23.936  98.056  1.00 37.45           C  
-ATOM   5154  CG  HIS C  84      -4.566 -23.615  96.846  1.00 40.18           C  
-ATOM   5155  ND1 HIS C  84      -5.839 -24.114  96.658  1.00 42.71           N  
-ATOM   5156  CD2 HIS C  84      -4.324 -22.799  95.792  1.00 41.85           C  
-ATOM   5157  CE1 HIS C  84      -6.331 -23.646  95.525  1.00 42.88           C  
-ATOM   5158  NE2 HIS C  84      -5.433 -22.844  94.981  1.00 42.89           N  
-ATOM   5159  N   GLN C  85      -2.225 -23.175 100.914  1.00 37.00           N  
-ATOM   5160  CA  GLN C  85      -1.757 -23.411 102.279  1.00 37.01           C  
-ATOM   5161  C   GLN C  85      -0.407 -22.766 102.549  1.00 36.35           C  
-ATOM   5162  O   GLN C  85       0.216 -22.208 101.643  1.00 36.02           O  
-ATOM   5163  CB  GLN C  85      -1.751 -24.910 102.643  1.00 37.56           C  
-ATOM   5164  CG  GLN C  85      -0.791 -25.809 101.869  1.00 39.43           C  
-ATOM   5165  CD  GLN C  85      -0.714 -27.212 102.474  1.00 43.21           C  
-ATOM   5166  OE1 GLN C  85      -1.532 -27.576 103.326  1.00 44.63           O  
-ATOM   5167  NE2 GLN C  85       0.266 -27.997 102.039  1.00 44.27           N  
-ATOM   5168  N   ASP C  86       0.019 -22.814 103.809  1.00 35.79           N  
-ATOM   5169  CA  ASP C  86       1.298 -22.237 104.201  1.00 35.17           C  
-ATOM   5170  C   ASP C  86       2.394 -23.281 104.051  1.00 34.54           C  
-ATOM   5171  O   ASP C  86       2.108 -24.472 103.970  1.00 34.28           O  
-ATOM   5172  CB  ASP C  86       1.243 -21.686 105.630  1.00 35.41           C  
-ATOM   5173  CG  ASP C  86       0.899 -22.748 106.657  1.00 36.24           C  
-ATOM   5174  OD1 ASP C  86       1.775 -23.572 106.979  1.00 36.57           O  
-ATOM   5175  OD2 ASP C  86      -0.224 -22.834 107.195  1.00 39.13           O  
-ATOM   5176  N   LEU C  87       3.639 -22.818 104.005  1.00 33.88           N  
-ATOM   5177  CA  LEU C  87       4.799 -23.678 103.819  1.00 33.38           C  
-ATOM   5178  C   LEU C  87       4.999 -24.684 104.960  1.00 33.19           C  
-ATOM   5179  O   LEU C  87       5.389 -25.819 104.710  1.00 32.99           O  
-ATOM   5180  CB  LEU C  87       6.060 -22.833 103.614  1.00 33.09           C  
-ATOM   5181  CG  LEU C  87       7.335 -23.555 103.180  1.00 32.63           C  
-ATOM   5182  CD1 LEU C  87       7.146 -24.254 101.838  1.00 32.24           C  
-ATOM   5183  CD2 LEU C  87       8.478 -22.579 103.118  1.00 32.17           C  
-ATOM   5184  N   LYS C  88       4.732 -24.275 106.201  1.00 33.36           N  
-ATOM   5185  CA  LYS C  88       4.851 -25.195 107.341  1.00 33.42           C  
-ATOM   5186  C   LYS C  88       3.994 -26.449 107.150  1.00 33.14           C  
-ATOM   5187  O   LYS C  88       4.490 -27.557 107.299  1.00 33.25           O  
-ATOM   5188  CB  LYS C  88       4.518 -24.509 108.674  1.00 33.47           C  
-ATOM   5189  CG  LYS C  88       4.594 -25.439 109.902  1.00 34.15           C  
-ATOM   5190  CD  LYS C  88       6.025 -25.589 110.419  1.00 36.64           C  
-ATOM   5191  CE  LYS C  88       6.409 -27.064 110.609  1.00 37.77           C  
-ATOM   5192  NZ  LYS C  88       7.849 -27.199 111.036  1.00 39.55           N  
-ATOM   5193  N   LYS C  89       2.722 -26.278 106.803  1.00 33.00           N  
-ATOM   5194  CA  LYS C  89       1.840 -27.428 106.609  1.00 33.27           C  
-ATOM   5195  C   LYS C  89       2.268 -28.288 105.417  1.00 33.16           C  
-ATOM   5196  O   LYS C  89       2.129 -29.512 105.451  1.00 33.19           O  
-ATOM   5197  CB  LYS C  89       0.386 -26.996 106.457  1.00 33.42           C  
-ATOM   5198  CG  LYS C  89      -0.210 -26.322 107.692  1.00 34.46           C  
-ATOM   5199  CD  LYS C  89      -1.714 -26.160 107.521  1.00 35.95           C  
-ATOM   5200  CE  LYS C  89      -2.315 -25.282 108.594  1.00 37.54           C  
-ATOM   5201  NZ  LYS C  89      -3.714 -24.887 108.233  1.00 40.36           N  
-ATOM   5202  N   PHE C  90       2.797 -27.640 104.379  1.00 32.73           N  
-ATOM   5203  CA  PHE C  90       3.330 -28.341 103.224  1.00 32.73           C  
-ATOM   5204  C   PHE C  90       4.544 -29.191 103.571  1.00 32.85           C  
-ATOM   5205  O   PHE C  90       4.684 -30.312 103.077  1.00 32.72           O  
-ATOM   5206  CB  PHE C  90       3.705 -27.362 102.120  1.00 32.64           C  
-ATOM   5207  CG  PHE C  90       4.223 -28.028 100.872  1.00 32.44           C  
-ATOM   5208  CD1 PHE C  90       3.383 -28.799 100.081  1.00 32.03           C  
-ATOM   5209  CD2 PHE C  90       5.556 -27.883 100.490  1.00 32.30           C  
-ATOM   5210  CE1 PHE C  90       3.853 -29.404  98.925  1.00 32.82           C  
-ATOM   5211  CE2 PHE C  90       6.037 -28.490  99.331  1.00 32.45           C  
-ATOM   5212  CZ  PHE C  90       5.187 -29.248  98.549  1.00 31.72           C  
-ATOM   5213  N   MET C  91       5.428 -28.642 104.398  1.00 32.90           N  
-ATOM   5214  CA  MET C  91       6.602 -29.373 104.843  1.00 33.46           C  
-ATOM   5215  C   MET C  91       6.181 -30.563 105.715  1.00 33.59           C  
-ATOM   5216  O   MET C  91       6.682 -31.671 105.524  1.00 33.91           O  
-ATOM   5217  CB  MET C  91       7.596 -28.443 105.550  1.00 33.37           C  
-ATOM   5218  CG  MET C  91       8.278 -27.451 104.594  1.00 34.49           C  
-ATOM   5219  SD  MET C  91       9.532 -26.338 105.315  1.00 37.92           S  
-ATOM   5220  CE  MET C  91       8.624 -25.616 106.633  1.00 32.54           C  
-ATOM   5221  N   ASP C  92       5.230 -30.347 106.626  1.00 33.59           N  
-ATOM   5222  CA  ASP C  92       4.718 -31.430 107.467  1.00 34.21           C  
-ATOM   5223  C   ASP C  92       4.092 -32.540 106.639  1.00 34.36           C  
-ATOM   5224  O   ASP C  92       4.298 -33.711 106.931  1.00 34.20           O  
-ATOM   5225  CB  ASP C  92       3.705 -30.917 108.490  1.00 34.18           C  
-ATOM   5226  CG  ASP C  92       4.355 -30.151 109.620  1.00 35.05           C  
-ATOM   5227  OD1 ASP C  92       5.530 -30.426 109.945  1.00 36.93           O  
-ATOM   5228  OD2 ASP C  92       3.760 -29.254 110.250  1.00 36.98           O  
-ATOM   5229  N   ALA C  93       3.340 -32.156 105.604  1.00 34.75           N  
-ATOM   5230  CA  ALA C  93       2.734 -33.098 104.670  1.00 34.90           C  
-ATOM   5231  C   ALA C  93       3.808 -33.846 103.898  1.00 35.20           C  
-ATOM   5232  O   ALA C  93       3.580 -34.960 103.434  1.00 35.61           O  
-ATOM   5233  CB  ALA C  93       1.810 -32.369 103.708  1.00 34.81           C  
-ATOM   5234  N   SER C  94       4.977 -33.226 103.765  1.00 35.56           N  
-ATOM   5235  CA  SER C  94       6.089 -33.812 103.019  1.00 35.92           C  
-ATOM   5236  C   SER C  94       7.120 -34.459 103.938  1.00 36.03           C  
-ATOM   5237  O   SER C  94       8.207 -34.815 103.485  1.00 36.28           O  
-ATOM   5238  CB  SER C  94       6.776 -32.745 102.154  1.00 35.73           C  
-ATOM   5239  OG  SER C  94       5.851 -32.123 101.275  1.00 36.29           O  
-ATOM   5240  N   ALA C  95       6.786 -34.601 105.220  1.00 36.06           N  
-ATOM   5241  CA  ALA C  95       7.730 -35.127 106.210  1.00 36.46           C  
-ATOM   5242  C   ALA C  95       8.367 -36.446 105.776  1.00 36.43           C  
-ATOM   5243  O   ALA C  95       9.554 -36.655 105.975  1.00 36.21           O  
-ATOM   5244  CB  ALA C  95       7.055 -35.284 107.586  1.00 36.34           C  
-ATOM   5245  N   LEU C  96       7.574 -37.323 105.169  1.00 36.85           N  
-ATOM   5246  CA  LEU C  96       8.074 -38.627 104.747  1.00 37.36           C  
-ATOM   5247  C   LEU C  96       8.627 -38.651 103.313  1.00 37.92           C  
-ATOM   5248  O   LEU C  96       9.715 -39.191 103.083  1.00 38.44           O  
-ATOM   5249  CB  LEU C  96       7.011 -39.715 104.978  1.00 37.25           C  
-ATOM   5250  CG  LEU C  96       6.521 -39.817 106.435  1.00 36.62           C  
-ATOM   5251  CD1 LEU C  96       5.583 -41.006 106.626  1.00 36.70           C  
-ATOM   5252  CD2 LEU C  96       7.689 -39.874 107.426  1.00 34.96           C  
-ATOM   5253  N   THR C  97       7.901 -38.053 102.365  1.00 38.07           N  
-ATOM   5254  CA  THR C  97       8.298 -38.078 100.950  1.00 38.10           C  
-ATOM   5255  C   THR C  97       9.484 -37.177 100.660  1.00 38.17           C  
-ATOM   5256  O   THR C  97      10.270 -37.447  99.747  1.00 38.47           O  
-ATOM   5257  CB  THR C  97       7.138 -37.652 100.028  1.00 38.15           C  
-ATOM   5258  OG1 THR C  97       6.867 -36.258 100.224  1.00 39.31           O  
-ATOM   5259  CG2 THR C  97       5.838 -38.322 100.419  1.00 37.95           C  
-ATOM   5260  N   GLY C  98       9.602 -36.091 101.420  1.00 37.99           N  
-ATOM   5261  CA  GLY C  98      10.578 -35.061 101.115  1.00 37.56           C  
-ATOM   5262  C   GLY C  98      10.052 -34.098 100.056  1.00 37.46           C  
-ATOM   5263  O   GLY C  98       8.991 -34.325  99.463  1.00 37.03           O  
-ATOM   5264  N   ILE C  99      10.794 -33.017  99.833  1.00 37.34           N  
-ATOM   5265  CA  ILE C  99      10.452 -32.026  98.811  1.00 37.57           C  
-ATOM   5266  C   ILE C  99      11.483 -32.079  97.676  1.00 37.53           C  
-ATOM   5267  O   ILE C  99      12.680 -31.972  97.926  1.00 37.49           O  
-ATOM   5268  CB  ILE C  99      10.383 -30.587  99.425  1.00 37.48           C  
-ATOM   5269  CG1 ILE C  99       9.453 -30.550 100.647  1.00 37.36           C  
-ATOM   5270  CG2 ILE C  99       9.950 -29.563  98.372  1.00 37.65           C  
-ATOM   5271  CD1 ILE C  99       9.465 -29.239 101.417  1.00 37.60           C  
-ATOM   5272  N   PRO C 100      11.035 -32.247  96.435  1.00 37.99           N  
-ATOM   5273  CA  PRO C 100      11.962 -32.268  95.299  1.00 38.47           C  
-ATOM   5274  C   PRO C 100      12.846 -31.018  95.284  1.00 39.02           C  
-ATOM   5275  O   PRO C 100      12.376 -29.917  95.600  1.00 39.00           O  
-ATOM   5276  CB  PRO C 100      11.027 -32.283  94.085  1.00 38.56           C  
-ATOM   5277  CG  PRO C 100       9.789 -32.898  94.578  1.00 38.33           C  
-ATOM   5278  CD  PRO C 100       9.637 -32.430  96.003  1.00 37.99           C  
-ATOM   5279  N   LEU C 101      14.116 -31.205  94.934  1.00 39.57           N  
-ATOM   5280  CA  LEU C 101      15.103 -30.126  94.913  1.00 39.85           C  
-ATOM   5281  C   LEU C 101      14.737 -28.959  93.989  1.00 39.85           C  
-ATOM   5282  O   LEU C 101      14.973 -27.802  94.358  1.00 39.68           O  
-ATOM   5283  CB  LEU C 101      16.492 -30.669  94.552  1.00 40.03           C  
-ATOM   5284  CG  LEU C 101      17.757 -29.916  94.984  1.00 40.73           C  
-ATOM   5285  CD1 LEU C 101      18.194 -28.911  93.928  1.00 41.98           C  
-ATOM   5286  CD2 LEU C 101      17.622 -29.244  96.361  1.00 41.57           C  
-ATOM   5287  N   PRO C 102      14.202 -29.245  92.792  1.00 39.78           N  
-ATOM   5288  CA  PRO C 102      13.743 -28.182  91.890  1.00 39.57           C  
-ATOM   5289  C   PRO C 102      12.700 -27.278  92.539  1.00 39.44           C  
-ATOM   5290  O   PRO C 102      12.755 -26.069  92.329  1.00 39.56           O  
-ATOM   5291  CB  PRO C 102      13.135 -28.959  90.719  1.00 39.71           C  
-ATOM   5292  CG  PRO C 102      13.880 -30.240  90.712  1.00 39.72           C  
-ATOM   5293  CD  PRO C 102      14.039 -30.574  92.171  1.00 39.85           C  
-ATOM   5294  N   LEU C 103      11.782 -27.854  93.315  1.00 39.13           N  
-ATOM   5295  CA  LEU C 103      10.792 -27.074  94.053  1.00 38.67           C  
-ATOM   5296  C   LEU C 103      11.438 -26.207  95.133  1.00 38.72           C  
-ATOM   5297  O   LEU C 103      11.138 -25.015  95.231  1.00 38.82           O  
-ATOM   5298  CB  LEU C 103       9.702 -27.975  94.644  1.00 38.63           C  
-ATOM   5299  CG  LEU C 103       8.392 -27.303  95.088  1.00 38.43           C  
-ATOM   5300  CD1 LEU C 103       7.690 -26.540  93.948  1.00 37.25           C  
-ATOM   5301  CD2 LEU C 103       7.452 -28.318  95.710  1.00 37.43           C  
-ATOM   5302  N   ILE C 104      12.339 -26.787  95.925  1.00 38.42           N  
-ATOM   5303  CA  ILE C 104      13.039 -26.020  96.955  1.00 38.15           C  
-ATOM   5304  C   ILE C 104      13.760 -24.828  96.316  1.00 38.07           C  
-ATOM   5305  O   ILE C 104      13.685 -23.695  96.816  1.00 37.97           O  
-ATOM   5306  CB  ILE C 104      14.029 -26.898  97.762  1.00 37.96           C  
-ATOM   5307  CG1 ILE C 104      13.286 -28.033  98.483  1.00 38.55           C  
-ATOM   5308  CG2 ILE C 104      14.793 -26.047  98.771  1.00 37.55           C  
-ATOM   5309  CD1 ILE C 104      14.192 -29.088  99.147  1.00 38.19           C  
-ATOM   5310  N   LYS C 105      14.451 -25.099  95.210  1.00 37.77           N  
-ATOM   5311  CA  LYS C 105      15.161 -24.069  94.459  1.00 37.27           C  
-ATOM   5312  C   LYS C 105      14.195 -22.968  94.030  1.00 36.39           C  
-ATOM   5313  O   LYS C 105      14.449 -21.792  94.280  1.00 36.33           O  
-ATOM   5314  CB  LYS C 105      15.865 -24.672  93.238  1.00 37.53           C  
-ATOM   5315  CG  LYS C 105      16.936 -23.773  92.616  1.00 38.80           C  
-ATOM   5316  CD  LYS C 105      17.737 -24.512  91.546  1.00 41.49           C  
-ATOM   5317  CE  LYS C 105      18.827 -25.392  92.156  1.00 43.38           C  
-ATOM   5318  NZ  LYS C 105      19.364 -26.370  91.162  1.00 44.80           N  
-ATOM   5319  N   SER C 106      13.091 -23.374  93.405  1.00 35.53           N  
-ATOM   5320  CA  SER C 106      12.066 -22.460  92.910  1.00 34.82           C  
-ATOM   5321  C   SER C 106      11.468 -21.603  94.023  1.00 34.39           C  
-ATOM   5322  O   SER C 106      11.373 -20.371  93.891  1.00 34.47           O  
-ATOM   5323  CB  SER C 106      10.959 -23.248  92.218  1.00 35.01           C  
-ATOM   5324  OG  SER C 106       9.861 -22.416  91.879  1.00 34.89           O  
-ATOM   5325  N   TYR C 107      11.074 -22.257  95.116  1.00 33.05           N  
-ATOM   5326  CA  TYR C 107      10.482 -21.567  96.255  1.00 32.13           C  
-ATOM   5327  C   TYR C 107      11.457 -20.549  96.836  1.00 31.91           C  
-ATOM   5328  O   TYR C 107      11.078 -19.415  97.111  1.00 31.70           O  
-ATOM   5329  CB  TYR C 107      10.040 -22.563  97.339  1.00 31.57           C  
-ATOM   5330  CG  TYR C 107       8.702 -23.228  97.106  1.00 29.87           C  
-ATOM   5331  CD1 TYR C 107       7.876 -22.855  96.045  1.00 29.24           C  
-ATOM   5332  CD2 TYR C 107       8.259 -24.237  97.958  1.00 29.17           C  
-ATOM   5333  CE1 TYR C 107       6.644 -23.474  95.839  1.00 28.34           C  
-ATOM   5334  CE2 TYR C 107       7.030 -24.858  97.760  1.00 28.63           C  
-ATOM   5335  CZ  TYR C 107       6.234 -24.475  96.705  1.00 28.15           C  
-ATOM   5336  OH  TYR C 107       5.019 -25.094  96.526  1.00 28.56           O  
-ATOM   5337  N   LEU C 108      12.710 -20.950  97.014  1.00 31.85           N  
-ATOM   5338  CA  LEU C 108      13.723 -20.033  97.522  1.00 32.32           C  
-ATOM   5339  C   LEU C 108      13.942 -18.852  96.575  1.00 32.29           C  
-ATOM   5340  O   LEU C 108      14.084 -17.715  97.021  1.00 32.32           O  
-ATOM   5341  CB  LEU C 108      15.049 -20.754  97.791  1.00 32.26           C  
-ATOM   5342  CG  LEU C 108      16.115 -19.902  98.490  1.00 33.51           C  
-ATOM   5343  CD1 LEU C 108      15.636 -19.405  99.855  1.00 34.33           C  
-ATOM   5344  CD2 LEU C 108      17.426 -20.662  98.629  1.00 34.37           C  
-ATOM   5345  N   PHE C 109      13.980 -19.136  95.274  1.00 32.48           N  
-ATOM   5346  CA  PHE C 109      14.147 -18.109  94.250  1.00 32.62           C  
-ATOM   5347  C   PHE C 109      13.027 -17.068  94.370  1.00 32.51           C  
-ATOM   5348  O   PHE C 109      13.290 -15.867  94.434  1.00 32.66           O  
-ATOM   5349  CB  PHE C 109      14.156 -18.756  92.855  1.00 32.88           C  
-ATOM   5350  CG  PHE C 109      14.627 -17.841  91.746  1.00 33.15           C  
-ATOM   5351  CD1 PHE C 109      15.850 -17.184  91.828  1.00 33.70           C  
-ATOM   5352  CD2 PHE C 109      13.854 -17.660  90.612  1.00 33.58           C  
-ATOM   5353  CE1 PHE C 109      16.285 -16.351  90.799  1.00 34.09           C  
-ATOM   5354  CE2 PHE C 109      14.282 -16.824  89.578  1.00 34.02           C  
-ATOM   5355  CZ  PHE C 109      15.493 -16.168  89.679  1.00 33.85           C  
-ATOM   5356  N   GLN C 110      11.790 -17.547  94.445  1.00 32.18           N  
-ATOM   5357  CA  GLN C 110      10.622 -16.687  94.534  1.00 32.20           C  
-ATOM   5358  C   GLN C 110      10.573 -15.864  95.825  1.00 32.48           C  
-ATOM   5359  O   GLN C 110      10.134 -14.708  95.805  1.00 32.47           O  
-ATOM   5360  CB  GLN C 110       9.349 -17.510  94.391  1.00 32.28           C  
-ATOM   5361  CG  GLN C 110       9.103 -18.031  92.986  1.00 32.11           C  
-ATOM   5362  CD  GLN C 110       7.859 -18.870  92.901  1.00 33.55           C  
-ATOM   5363  OE1 GLN C 110       6.749 -18.351  93.036  1.00 34.51           O  
-ATOM   5364  NE2 GLN C 110       8.027 -20.177  92.680  1.00 33.71           N  
-ATOM   5365  N   LEU C 111      11.025 -16.457  96.934  1.00 32.06           N  
-ATOM   5366  CA  LEU C 111      11.018 -15.774  98.229  1.00 31.52           C  
-ATOM   5367  C   LEU C 111      12.047 -14.658  98.249  1.00 31.36           C  
-ATOM   5368  O   LEU C 111      11.778 -13.570  98.758  1.00 30.99           O  
-ATOM   5369  CB  LEU C 111      11.241 -16.757  99.390  1.00 31.31           C  
-ATOM   5370  CG  LEU C 111      10.130 -17.798  99.618  1.00 30.99           C  
-ATOM   5371  CD1 LEU C 111      10.617 -18.976 100.442  1.00 31.16           C  
-ATOM   5372  CD2 LEU C 111       8.885 -17.179 100.251  1.00 31.20           C  
-ATOM   5373  N   LEU C 112      13.218 -14.917  97.675  1.00 31.23           N  
-ATOM   5374  CA  LEU C 112      14.253 -13.894  97.594  1.00 31.39           C  
-ATOM   5375  C   LEU C 112      13.848 -12.722  96.697  1.00 31.49           C  
-ATOM   5376  O   LEU C 112      14.286 -11.595  96.915  1.00 31.63           O  
-ATOM   5377  CB  LEU C 112      15.580 -14.489  97.121  1.00 31.23           C  
-ATOM   5378  CG  LEU C 112      16.314 -15.363  98.136  1.00 31.56           C  
-ATOM   5379  CD1 LEU C 112      17.327 -16.233  97.435  1.00 32.17           C  
-ATOM   5380  CD2 LEU C 112      16.980 -14.526  99.213  1.00 32.56           C  
-ATOM   5381  N   GLN C 113      13.021 -12.996  95.693  1.00 31.70           N  
-ATOM   5382  CA  GLN C 113      12.571 -11.965  94.773  1.00 32.26           C  
-ATOM   5383  C   GLN C 113      11.562 -11.080  95.483  1.00 32.19           C  
-ATOM   5384  O   GLN C 113      11.646  -9.852  95.407  1.00 32.02           O  
-ATOM   5385  CB  GLN C 113      11.933 -12.589  93.540  1.00 32.65           C  
-ATOM   5386  CG  GLN C 113      12.920 -12.984  92.464  1.00 34.18           C  
-ATOM   5387  CD  GLN C 113      12.250 -13.758  91.357  1.00 36.74           C  
-ATOM   5388  OE1 GLN C 113      11.725 -13.169  90.410  1.00 38.08           O  
-ATOM   5389  NE2 GLN C 113      12.240 -15.079  91.480  1.00 37.37           N  
-ATOM   5390  N   GLY C 114      10.620 -11.722  96.179  1.00 31.88           N  
-ATOM   5391  CA  GLY C 114       9.622 -11.036  96.975  1.00 31.69           C  
-ATOM   5392  C   GLY C 114      10.280 -10.204  98.056  1.00 31.61           C  
-ATOM   5393  O   GLY C 114       9.872  -9.073  98.311  1.00 31.69           O  
-ATOM   5394  N   LEU C 115      11.322 -10.759  98.669  1.00 31.69           N  
-ATOM   5395  CA  LEU C 115      12.058 -10.067  99.720  1.00 31.86           C  
-ATOM   5396  C   LEU C 115      12.935  -8.927  99.194  1.00 32.00           C  
-ATOM   5397  O   LEU C 115      12.968  -7.849  99.798  1.00 31.93           O  
-ATOM   5398  CB  LEU C 115      12.893 -11.052 100.538  1.00 31.90           C  
-ATOM   5399  CG  LEU C 115      13.497 -10.511 101.837  1.00 32.37           C  
-ATOM   5400  CD1 LEU C 115      12.412 -10.089 102.823  1.00 31.21           C  
-ATOM   5401  CD2 LEU C 115      14.427 -11.538 102.446  1.00 32.97           C  
-ATOM   5402  N   ALA C 116      13.643  -9.168  98.086  1.00 31.76           N  
-ATOM   5403  CA  ALA C 116      14.453  -8.134  97.440  1.00 31.51           C  
-ATOM   5404  C   ALA C 116      13.592  -6.921  97.115  1.00 31.37           C  
-ATOM   5405  O   ALA C 116      14.020  -5.789  97.302  1.00 31.53           O  
-ATOM   5406  CB  ALA C 116      15.121  -8.670  96.176  1.00 31.43           C  
-ATOM   5407  N   PHE C 117      12.374  -7.179  96.644  1.00 31.42           N  
-ATOM   5408  CA  PHE C 117      11.378  -6.145  96.412  1.00 31.68           C  
-ATOM   5409  C   PHE C 117      10.995  -5.411  97.703  1.00 31.74           C  
-ATOM   5410  O   PHE C 117      10.913  -4.183  97.714  1.00 32.05           O  
-ATOM   5411  CB  PHE C 117      10.138  -6.745  95.752  1.00 31.57           C  
-ATOM   5412  CG  PHE C 117       9.203  -5.721  95.175  1.00 32.86           C  
-ATOM   5413  CD1 PHE C 117       9.376  -5.254  93.877  1.00 33.60           C  
-ATOM   5414  CD2 PHE C 117       8.139  -5.226  95.929  1.00 34.55           C  
-ATOM   5415  CE1 PHE C 117       8.512  -4.311  93.341  1.00 33.89           C  
-ATOM   5416  CE2 PHE C 117       7.272  -4.280  95.403  1.00 33.87           C  
-ATOM   5417  CZ  PHE C 117       7.460  -3.822  94.104  1.00 34.51           C  
-ATOM   5418  N   CYS C 118      10.752  -6.157  98.780  1.00 31.60           N  
-ATOM   5419  CA  CYS C 118      10.483  -5.546 100.083  1.00 31.53           C  
-ATOM   5420  C   CYS C 118      11.611  -4.609 100.471  1.00 31.97           C  
-ATOM   5421  O   CYS C 118      11.379  -3.428 100.736  1.00 32.24           O  
-ATOM   5422  CB  CYS C 118      10.293  -6.605 101.176  1.00 31.38           C  
-ATOM   5423  SG  CYS C 118       8.676  -7.397 101.168  1.00 29.57           S  
-ATOM   5424  N   HIS C 119      12.835  -5.134 100.487  1.00 32.20           N  
-ATOM   5425  CA  HIS C 119      13.991  -4.349 100.905  1.00 32.58           C  
-ATOM   5426  C   HIS C 119      14.229  -3.144  99.991  1.00 32.87           C  
-ATOM   5427  O   HIS C 119      14.659  -2.093 100.464  1.00 32.67           O  
-ATOM   5428  CB  HIS C 119      15.239  -5.229 101.008  1.00 32.57           C  
-ATOM   5429  CG  HIS C 119      15.177  -6.235 102.118  1.00 33.52           C  
-ATOM   5430  ND1 HIS C 119      14.184  -6.232 103.076  1.00 33.62           N  
-ATOM   5431  CD2 HIS C 119      15.986  -7.277 102.421  1.00 34.00           C  
-ATOM   5432  CE1 HIS C 119      14.386  -7.227 103.921  1.00 33.59           C  
-ATOM   5433  NE2 HIS C 119      15.471  -7.879 103.545  1.00 34.34           N  
-ATOM   5434  N   SER C 120      13.921  -3.307  98.699  1.00 32.98           N  
-ATOM   5435  CA  SER C 120      14.064  -2.252  97.696  1.00 33.36           C  
-ATOM   5436  C   SER C 120      13.052  -1.134  97.901  1.00 33.22           C  
-ATOM   5437  O   SER C 120      13.222  -0.021  97.379  1.00 33.31           O  
-ATOM   5438  CB  SER C 120      13.873  -2.832  96.293  1.00 33.25           C  
-ATOM   5439  OG  SER C 120      15.043  -3.508  95.874  1.00 35.29           O  
-ATOM   5440  N   HIS C 121      11.988  -1.457  98.632  1.00 32.74           N  
-ATOM   5441  CA  HIS C 121      10.909  -0.521  98.920  1.00 32.54           C  
-ATOM   5442  C   HIS C 121      10.929  -0.110 100.388  1.00 31.69           C  
-ATOM   5443  O   HIS C 121       9.908   0.283 100.943  1.00 31.74           O  
-ATOM   5444  CB  HIS C 121       9.564  -1.134  98.529  1.00 32.72           C  
-ATOM   5445  CG  HIS C 121       9.305  -1.098  97.057  1.00 34.94           C  
-ATOM   5446  ND1 HIS C 121      10.188  -1.619  96.135  1.00 37.46           N  
-ATOM   5447  CD2 HIS C 121       8.281  -0.575  96.344  1.00 36.92           C  
-ATOM   5448  CE1 HIS C 121       9.714  -1.426  94.918  1.00 38.05           C  
-ATOM   5449  NE2 HIS C 121       8.558  -0.793  95.016  1.00 37.78           N  
-ATOM   5450  N   ARG C 122      12.111  -0.204 100.992  1.00 30.60           N  
-ATOM   5451  CA  ARG C 122      12.368   0.188 102.382  1.00 30.00           C  
-ATOM   5452  C   ARG C 122      11.415  -0.418 103.427  1.00 29.19           C  
-ATOM   5453  O   ARG C 122      11.093   0.221 104.430  1.00 29.30           O  
-ATOM   5454  CB  ARG C 122      12.514   1.726 102.538  1.00 29.69           C  
-ATOM   5455  CG  ARG C 122      11.340   2.595 102.030  1.00 31.13           C  
-ATOM   5456  CD  ARG C 122      10.099   2.633 102.949  1.00 31.37           C  
-ATOM   5457  NE  ARG C 122       9.112   3.639 102.556  1.00 31.11           N  
-ATOM   5458  CZ  ARG C 122       8.052   3.410 101.786  1.00 31.20           C  
-ATOM   5459  NH1 ARG C 122       7.814   2.198 101.292  1.00 30.39           N  
-ATOM   5460  NH2 ARG C 122       7.223   4.405 101.499  1.00 30.62           N  
-ATOM   5461  N   VAL C 123      11.001  -1.664 103.192  1.00 28.56           N  
-ATOM   5462  CA  VAL C 123      10.124  -2.401 104.111  1.00 27.57           C  
-ATOM   5463  C   VAL C 123      10.845  -3.628 104.650  1.00 27.26           C  
-ATOM   5464  O   VAL C 123      11.326  -4.459 103.870  1.00 27.16           O  
-ATOM   5465  CB  VAL C 123       8.797  -2.865 103.430  1.00 27.94           C  
-ATOM   5466  CG1 VAL C 123       7.975  -3.777 104.375  1.00 27.30           C  
-ATOM   5467  CG2 VAL C 123       7.951  -1.674 102.964  1.00 27.10           C  
-ATOM   5468  N   LEU C 124      10.936  -3.727 105.978  1.00 26.47           N  
-ATOM   5469  CA  LEU C 124      11.436  -4.931 106.641  1.00 26.15           C  
-ATOM   5470  C   LEU C 124      10.244  -5.834 106.954  1.00 25.82           C  
-ATOM   5471  O   LEU C 124       9.195  -5.339 107.329  1.00 25.75           O  
-ATOM   5472  CB  LEU C 124      12.160  -4.572 107.943  1.00 25.68           C  
-ATOM   5473  CG  LEU C 124      13.455  -3.766 107.922  1.00 26.66           C  
-ATOM   5474  CD1 LEU C 124      14.019  -3.580 109.334  1.00 25.95           C  
-ATOM   5475  CD2 LEU C 124      14.496  -4.425 107.014  1.00 27.19           C  
-ATOM   5476  N   HIS C 125      10.391  -7.148 106.812  1.00 25.94           N  
-ATOM   5477  CA  HIS C 125       9.265  -8.041 107.103  1.00 26.12           C  
-ATOM   5478  C   HIS C 125       9.207  -8.410 108.591  1.00 26.38           C  
-ATOM   5479  O   HIS C 125       8.166  -8.231 109.237  1.00 26.19           O  
-ATOM   5480  CB  HIS C 125       9.268  -9.285 106.217  1.00 26.10           C  
-ATOM   5481  CG  HIS C 125       8.043 -10.135 106.374  1.00 25.91           C  
-ATOM   5482  ND1 HIS C 125       7.869 -11.002 107.432  1.00 25.29           N  
-ATOM   5483  CD2 HIS C 125       6.929 -10.245 105.611  1.00 25.39           C  
-ATOM   5484  CE1 HIS C 125       6.704 -11.613 107.312  1.00 25.37           C  
-ATOM   5485  NE2 HIS C 125       6.111 -11.168 106.218  1.00 25.50           N  
-ATOM   5486  N   ARG C 126      10.328  -8.923 109.106  1.00 26.67           N  
-ATOM   5487  CA  ARG C 126      10.547  -9.194 110.536  1.00 27.15           C  
-ATOM   5488  C   ARG C 126       9.766 -10.370 111.149  1.00 27.66           C  
-ATOM   5489  O   ARG C 126       9.839 -10.608 112.358  1.00 27.92           O  
-ATOM   5490  CB  ARG C 126      10.335  -7.925 111.381  1.00 27.24           C  
-ATOM   5491  CG  ARG C 126      11.222  -6.749 111.005  1.00 26.24           C  
-ATOM   5492  CD  ARG C 126      11.173  -5.605 112.001  1.00 25.77           C  
-ATOM   5493  NE  ARG C 126       9.799  -5.157 112.222  1.00 25.97           N  
-ATOM   5494  CZ  ARG C 126       9.436  -4.283 113.139  1.00 24.55           C  
-ATOM   5495  NH1 ARG C 126      10.341  -3.743 113.934  1.00 25.13           N  
-ATOM   5496  NH2 ARG C 126       8.162  -3.935 113.249  1.00 24.82           N  
-ATOM   5497  N   ASP C 127       9.041 -11.121 110.331  1.00 27.87           N  
-ATOM   5498  CA  ASP C 127       8.422 -12.347 110.815  1.00 28.31           C  
-ATOM   5499  C   ASP C 127       8.395 -13.441 109.753  1.00 28.06           C  
-ATOM   5500  O   ASP C 127       7.369 -14.094 109.544  1.00 27.86           O  
-ATOM   5501  CB  ASP C 127       7.018 -12.074 111.383  1.00 28.69           C  
-ATOM   5502  CG  ASP C 127       6.544 -13.178 112.322  1.00 30.89           C  
-ATOM   5503  OD1 ASP C 127       7.398 -13.799 113.000  1.00 30.97           O  
-ATOM   5504  OD2 ASP C 127       5.337 -13.510 112.425  1.00 34.58           O  
-ATOM   5505  N   LEU C 128       9.525 -13.641 109.081  1.00 28.17           N  
-ATOM   5506  CA  LEU C 128       9.597 -14.658 108.035  1.00 28.74           C  
-ATOM   5507  C   LEU C 128       9.758 -16.039 108.656  1.00 28.89           C  
-ATOM   5508  O   LEU C 128      10.815 -16.385 109.183  1.00 29.93           O  
-ATOM   5509  CB  LEU C 128      10.707 -14.365 107.013  1.00 28.48           C  
-ATOM   5510  CG  LEU C 128      10.535 -13.117 106.130  1.00 29.10           C  
-ATOM   5511  CD1 LEU C 128      11.819 -12.799 105.383  1.00 29.42           C  
-ATOM   5512  CD2 LEU C 128       9.379 -13.240 105.153  1.00 26.87           C  
-ATOM   5513  N   LYS C 129       8.672 -16.791 108.637  1.00 28.98           N  
-ATOM   5514  CA  LYS C 129       8.642 -18.176 109.088  1.00 29.04           C  
-ATOM   5515  C   LYS C 129       7.698 -18.926 108.142  1.00 28.62           C  
-ATOM   5516  O   LYS C 129       6.881 -18.291 107.466  1.00 28.82           O  
-ATOM   5517  CB  LYS C 129       8.166 -18.262 110.542  1.00 29.09           C  
-ATOM   5518  CG  LYS C 129       6.734 -17.802 110.770  1.00 29.71           C  
-ATOM   5519  CD  LYS C 129       6.360 -17.907 112.234  1.00 30.51           C  
-ATOM   5520  CE  LYS C 129       5.079 -17.167 112.521  1.00 31.42           C  
-ATOM   5521  NZ  LYS C 129       4.867 -17.113 113.986  1.00 35.71           N  
-ATOM   5522  N   PRO C 130       7.804 -20.254 108.084  1.00 28.34           N  
-ATOM   5523  CA  PRO C 130       7.059 -21.052 107.101  1.00 28.08           C  
-ATOM   5524  C   PRO C 130       5.542 -20.862 107.178  1.00 27.82           C  
-ATOM   5525  O   PRO C 130       4.859 -20.977 106.146  1.00 27.43           O  
-ATOM   5526  CB  PRO C 130       7.431 -22.496 107.467  1.00 28.12           C  
-ATOM   5527  CG  PRO C 130       8.715 -22.391 108.201  1.00 28.55           C  
-ATOM   5528  CD  PRO C 130       8.635 -21.105 108.960  1.00 28.78           C  
-ATOM   5529  N   GLN C 131       5.028 -20.587 108.377  1.00 27.43           N  
-ATOM   5530  CA  GLN C 131       3.592 -20.362 108.572  1.00 27.64           C  
-ATOM   5531  C   GLN C 131       3.127 -19.050 107.927  1.00 26.92           C  
-ATOM   5532  O   GLN C 131       1.935 -18.877 107.674  1.00 26.76           O  
-ATOM   5533  CB  GLN C 131       3.225 -20.359 110.061  1.00 27.92           C  
-ATOM   5534  CG  GLN C 131       3.704 -21.580 110.842  1.00 30.27           C  
-ATOM   5535  CD  GLN C 131       5.051 -21.357 111.505  1.00 32.92           C  
-ATOM   5536  OE1 GLN C 131       6.047 -21.107 110.832  1.00 33.54           O  
-ATOM   5537  NE2 GLN C 131       5.082 -21.445 112.831  1.00 37.04           N  
-ATOM   5538  N   ASN C 132       4.063 -18.134 107.681  1.00 26.03           N  
-ATOM   5539  CA  ASN C 132       3.740 -16.861 107.030  1.00 26.15           C  
-ATOM   5540  C   ASN C 132       4.021 -16.848 105.514  1.00 26.12           C  
-ATOM   5541  O   ASN C 132       3.915 -15.809 104.865  1.00 26.12           O  
-ATOM   5542  CB  ASN C 132       4.478 -15.709 107.717  1.00 25.56           C  
-ATOM   5543  CG  ASN C 132       3.872 -15.341 109.063  1.00 25.39           C  
-ATOM   5544  OD1 ASN C 132       2.726 -15.683 109.361  1.00 25.34           O  
-ATOM   5545  ND2 ASN C 132       4.643 -14.628 109.881  1.00 24.13           N  
-ATOM   5546  N   LEU C 133       4.395 -18.002 104.971  1.00 26.45           N  
-ATOM   5547  CA  LEU C 133       4.701 -18.147 103.549  1.00 26.89           C  
-ATOM   5548  C   LEU C 133       3.654 -19.040 102.917  1.00 27.72           C  
-ATOM   5549  O   LEU C 133       3.476 -20.186 103.332  1.00 28.15           O  
-ATOM   5550  CB  LEU C 133       6.098 -18.750 103.351  1.00 26.66           C  
-ATOM   5551  CG  LEU C 133       7.276 -18.081 104.070  1.00 26.04           C  
-ATOM   5552  CD1 LEU C 133       8.565 -18.745 103.684  1.00 24.96           C  
-ATOM   5553  CD2 LEU C 133       7.341 -16.571 103.774  1.00 25.21           C  
-ATOM   5554  N   LEU C 134       2.957 -18.514 101.919  1.00 28.49           N  
-ATOM   5555  CA  LEU C 134       1.803 -19.201 101.352  1.00 29.57           C  
-ATOM   5556  C   LEU C 134       2.076 -19.703  99.963  1.00 30.29           C  
-ATOM   5557  O   LEU C 134       2.730 -19.020  99.171  1.00 30.56           O  
-ATOM   5558  CB  LEU C 134       0.583 -18.278 101.324  1.00 29.41           C  
-ATOM   5559  CG  LEU C 134       0.243 -17.498 102.596  1.00 30.43           C  
-ATOM   5560  CD1 LEU C 134      -0.924 -16.553 102.315  1.00 31.46           C  
-ATOM   5561  CD2 LEU C 134      -0.080 -18.430 103.752  1.00 29.94           C  
-ATOM   5562  N   ILE C 135       1.556 -20.892  99.664  1.00 31.29           N  
-ATOM   5563  CA  ILE C 135       1.764 -21.521  98.363  1.00 32.33           C  
-ATOM   5564  C   ILE C 135       0.448 -21.789  97.638  1.00 33.38           C  
-ATOM   5565  O   ILE C 135      -0.603 -21.934  98.271  1.00 33.53           O  
-ATOM   5566  CB  ILE C 135       2.609 -22.831  98.494  1.00 32.35           C  
-ATOM   5567  CG1 ILE C 135       1.870 -23.903  99.306  1.00 32.28           C  
-ATOM   5568  CG2 ILE C 135       3.980 -22.532  99.096  1.00 31.85           C  
-ATOM   5569  CD1 ILE C 135       2.498 -25.291  99.213  1.00 32.23           C  
-ATOM   5570  N   ASN C 136       0.510 -21.847  96.311  1.00 34.78           N  
-ATOM   5571  CA  ASN C 136      -0.630 -22.291  95.510  1.00 36.45           C  
-ATOM   5572  C   ASN C 136      -0.354 -23.586  94.728  1.00 37.58           C  
-ATOM   5573  O   ASN C 136       0.772 -24.105  94.733  1.00 37.61           O  
-ATOM   5574  CB  ASN C 136      -1.132 -21.173  94.580  1.00 36.45           C  
-ATOM   5575  CG  ASN C 136      -0.140 -20.812  93.482  1.00 36.89           C  
-ATOM   5576  OD1 ASN C 136       0.840 -21.516  93.241  1.00 36.76           O  
-ATOM   5577  ND2 ASN C 136      -0.396 -19.691  92.811  1.00 37.99           N  
-ATOM   5578  N   THR C 137      -1.383 -24.092  94.055  1.00 38.78           N  
-ATOM   5579  CA  THR C 137      -1.268 -25.316  93.264  1.00 40.25           C  
-ATOM   5580  C   THR C 137      -0.414 -25.153  91.990  1.00 40.67           C  
-ATOM   5581  O   THR C 137      -0.072 -26.145  91.345  1.00 41.14           O  
-ATOM   5582  CB  THR C 137      -2.666 -25.863  92.914  1.00 40.26           C  
-ATOM   5583  OG1 THR C 137      -3.407 -24.870  92.194  1.00 42.17           O  
-ATOM   5584  CG2 THR C 137      -3.494 -26.054  94.174  1.00 40.59           C  
-ATOM   5585  N   GLU C 138      -0.049 -23.914  91.657  1.00 40.95           N  
-ATOM   5586  CA  GLU C 138       0.684 -23.608  90.423  1.00 41.26           C  
-ATOM   5587  C   GLU C 138       2.206 -23.484  90.579  1.00 40.43           C  
-ATOM   5588  O   GLU C 138       2.914 -23.264  89.594  1.00 40.86           O  
-ATOM   5589  CB  GLU C 138       0.139 -22.329  89.789  1.00 41.74           C  
-ATOM   5590  CG  GLU C 138      -1.119 -22.530  88.961  1.00 44.74           C  
-ATOM   5591  CD  GLU C 138      -1.316 -21.428  87.931  1.00 49.02           C  
-ATOM   5592  OE1 GLU C 138      -1.092 -20.241  88.270  1.00 50.29           O  
-ATOM   5593  OE2 GLU C 138      -1.695 -21.751  86.776  1.00 51.10           O  
-ATOM   5594  N   GLY C 139       2.710 -23.603  91.802  1.00 39.33           N  
-ATOM   5595  CA  GLY C 139       4.148 -23.545  92.027  1.00 37.79           C  
-ATOM   5596  C   GLY C 139       4.646 -22.208  92.546  1.00 36.47           C  
-ATOM   5597  O   GLY C 139       5.857 -21.977  92.647  1.00 36.45           O  
-ATOM   5598  N   ALA C 140       3.710 -21.324  92.873  1.00 35.35           N  
-ATOM   5599  CA  ALA C 140       4.049 -20.019  93.426  1.00 34.28           C  
-ATOM   5600  C   ALA C 140       4.135 -20.062  94.944  1.00 33.32           C  
-ATOM   5601  O   ALA C 140       3.441 -20.845  95.595  1.00 33.02           O  
-ATOM   5602  CB  ALA C 140       3.035 -18.965  92.985  1.00 34.21           C  
-ATOM   5603  N   ILE C 141       5.009 -19.219  95.488  1.00 32.39           N  
-ATOM   5604  CA  ILE C 141       5.083 -18.958  96.920  1.00 31.05           C  
-ATOM   5605  C   ILE C 141       5.154 -17.442  97.142  1.00 30.70           C  
-ATOM   5606  O   ILE C 141       5.826 -16.733  96.389  1.00 30.51           O  
-ATOM   5607  CB  ILE C 141       6.284 -19.717  97.563  1.00 30.88           C  
-ATOM   5608  CG1 ILE C 141       6.224 -19.653  99.099  1.00 29.48           C  
-ATOM   5609  CG2 ILE C 141       7.626 -19.229  97.000  1.00 30.01           C  
-ATOM   5610  CD1 ILE C 141       7.127 -20.667  99.805  1.00 27.74           C  
-ATOM   5611  N   LYS C 142       4.446 -16.960  98.163  1.00 30.01           N  
-ATOM   5612  CA  LYS C 142       4.342 -15.531  98.445  1.00 29.74           C  
-ATOM   5613  C   LYS C 142       4.582 -15.195  99.922  1.00 29.39           C  
-ATOM   5614  O   LYS C 142       4.163 -15.943 100.811  1.00 29.31           O  
-ATOM   5615  CB  LYS C 142       2.960 -15.004  98.026  1.00 29.64           C  
-ATOM   5616  CG  LYS C 142       2.647 -15.160  96.540  1.00 30.41           C  
-ATOM   5617  CD  LYS C 142       1.218 -14.792  96.211  1.00 30.65           C  
-ATOM   5618  CE  LYS C 142       0.822 -15.316  94.838  1.00 31.06           C  
-ATOM   5619  NZ  LYS C 142      -0.052 -14.345  94.120  1.00 31.30           N  
-ATOM   5620  N   LEU C 143       5.244 -14.067 100.170  1.00 28.95           N  
-ATOM   5621  CA  LEU C 143       5.302 -13.487 101.511  1.00 28.88           C  
-ATOM   5622  C   LEU C 143       3.915 -13.032 101.941  1.00 28.67           C  
-ATOM   5623  O   LEU C 143       3.171 -12.446 101.154  1.00 28.46           O  
-ATOM   5624  CB  LEU C 143       6.262 -12.293 101.580  1.00 28.96           C  
-ATOM   5625  CG  LEU C 143       7.689 -12.393 101.035  1.00 29.73           C  
-ATOM   5626  CD1 LEU C 143       8.483 -11.115 101.362  1.00 29.36           C  
-ATOM   5627  CD2 LEU C 143       8.387 -13.610 101.575  1.00 30.18           C  
-ATOM   5628  N   ALA C 144       3.576 -13.331 103.190  1.00 28.13           N  
-ATOM   5629  CA  ALA C 144       2.328 -12.889 103.790  1.00 27.83           C  
-ATOM   5630  C   ALA C 144       2.552 -12.436 105.231  1.00 27.60           C  
-ATOM   5631  O   ALA C 144       3.683 -12.479 105.752  1.00 27.31           O  
-ATOM   5632  CB  ALA C 144       1.255 -13.997 103.720  1.00 27.36           C  
-ATOM   5633  N   ASP C 145       1.460 -11.999 105.853  1.00 27.38           N  
-ATOM   5634  CA  ASP C 145       1.448 -11.499 107.223  1.00 27.42           C  
-ATOM   5635  C   ASP C 145       2.445 -10.377 107.462  1.00 26.96           C  
-ATOM   5636  O   ASP C 145       3.522 -10.580 108.035  1.00 27.34           O  
-ATOM   5637  CB  ASP C 145       1.659 -12.625 108.232  1.00 27.64           C  
-ATOM   5638  CG  ASP C 145       1.098 -12.288 109.582  1.00 29.06           C  
-ATOM   5639  OD1 ASP C 145       0.949 -11.086 109.894  1.00 30.80           O  
-ATOM   5640  OD2 ASP C 145       0.746 -13.160 110.393  1.00 32.90           O  
-ATOM   5641  N   PHE C 146       2.061  -9.182 107.042  1.00 26.63           N  
-ATOM   5642  CA  PHE C 146       2.911  -8.004 107.196  1.00 26.18           C  
-ATOM   5643  C   PHE C 146       2.598  -7.202 108.463  1.00 25.88           C  
-ATOM   5644  O   PHE C 146       2.977  -6.042 108.574  1.00 25.67           O  
-ATOM   5645  CB  PHE C 146       2.838  -7.146 105.922  1.00 25.98           C  
-ATOM   5646  CG  PHE C 146       3.700  -7.669 104.805  1.00 26.06           C  
-ATOM   5647  CD1 PHE C 146       3.306  -8.781 104.059  1.00 26.66           C  
-ATOM   5648  CD2 PHE C 146       4.924  -7.068 104.515  1.00 26.19           C  
-ATOM   5649  CE1 PHE C 146       4.125  -9.277 103.021  1.00 27.13           C  
-ATOM   5650  CE2 PHE C 146       5.746  -7.550 103.488  1.00 25.85           C  
-ATOM   5651  CZ  PHE C 146       5.347  -8.655 102.739  1.00 25.65           C  
-ATOM   5652  N   GLY C 147       1.938  -7.845 109.430  1.00 25.77           N  
-ATOM   5653  CA  GLY C 147       1.555  -7.200 110.679  1.00 25.50           C  
-ATOM   5654  C   GLY C 147       2.713  -6.717 111.531  1.00 25.78           C  
-ATOM   5655  O   GLY C 147       2.573  -5.761 112.292  1.00 25.76           O  
-ATOM   5656  N   LEU C 148       3.860  -7.379 111.392  1.00 25.86           N  
-ATOM   5657  CA  LEU C 148       5.065  -7.038 112.135  1.00 26.05           C  
-ATOM   5658  C   LEU C 148       6.117  -6.346 111.253  1.00 26.05           C  
-ATOM   5659  O   LEU C 148       7.254  -6.137 111.677  1.00 25.69           O  
-ATOM   5660  CB  LEU C 148       5.634  -8.301 112.790  1.00 26.28           C  
-ATOM   5661  CG  LEU C 148       4.736  -8.894 113.889  1.00 27.57           C  
-ATOM   5662  CD1 LEU C 148       5.179 -10.300 114.278  1.00 28.27           C  
-ATOM   5663  CD2 LEU C 148       4.706  -7.973 115.119  1.00 27.02           C  
-ATOM   5664  N   ALA C 149       5.725  -5.990 110.028  1.00 26.26           N  
-ATOM   5665  CA  ALA C 149       6.602  -5.267 109.106  1.00 26.92           C  
-ATOM   5666  C   ALA C 149       6.752  -3.801 109.521  1.00 27.56           C  
-ATOM   5667  O   ALA C 149       5.965  -3.300 110.318  1.00 27.40           O  
-ATOM   5668  CB  ALA C 149       6.069  -5.361 107.699  1.00 26.45           C  
-ATOM   5669  N   ARG C 150       7.764  -3.123 108.986  1.00 28.41           N  
-ATOM   5670  CA  ARG C 150       7.880  -1.669 109.137  1.00 29.39           C  
-ATOM   5671  C   ARG C 150       8.745  -1.017 108.059  1.00 29.64           C  
-ATOM   5672  O   ARG C 150       9.696  -1.622 107.559  1.00 29.73           O  
-ATOM   5673  CB  ARG C 150       8.348  -1.274 110.549  1.00 29.65           C  
-ATOM   5674  CG  ARG C 150       9.830  -1.047 110.721  1.00 31.18           C  
-ATOM   5675  CD  ARG C 150      10.199   0.345 111.243  1.00 32.53           C  
-ATOM   5676  NE  ARG C 150      10.045   0.449 112.694  1.00 35.43           N  
-ATOM   5677  CZ  ARG C 150       9.667   1.551 113.338  1.00 35.17           C  
-ATOM   5678  NH1 ARG C 150       9.404   2.668 112.670  1.00 33.74           N  
-ATOM   5679  NH2 ARG C 150       9.559   1.537 114.661  1.00 36.05           N  
-ATOM   5680  N   ALA C 151       8.386   0.214 107.705  1.00 29.85           N  
-ATOM   5681  CA  ALA C 151       9.154   1.014 106.756  1.00 30.44           C  
-ATOM   5682  C   ALA C 151      10.423   1.506 107.438  1.00 30.84           C  
-ATOM   5683  O   ALA C 151      10.355   2.205 108.440  1.00 30.96           O  
-ATOM   5684  CB  ALA C 151       8.323   2.189 106.264  1.00 29.91           C  
-ATOM   5685  N   PHE C 152      11.580   1.117 106.919  1.00 31.65           N  
-ATOM   5686  CA  PHE C 152      12.831   1.538 107.543  1.00 32.78           C  
-ATOM   5687  C   PHE C 152      13.413   2.800 106.917  1.00 33.34           C  
-ATOM   5688  O   PHE C 152      12.976   3.234 105.842  1.00 33.58           O  
-ATOM   5689  CB  PHE C 152      13.863   0.387 107.636  1.00 32.28           C  
-ATOM   5690  CG  PHE C 152      14.396  -0.102 106.310  1.00 32.18           C  
-ATOM   5691  CD1 PHE C 152      13.793  -1.169 105.654  1.00 32.78           C  
-ATOM   5692  CD2 PHE C 152      15.545   0.458 105.751  1.00 32.49           C  
-ATOM   5693  CE1 PHE C 152      14.308  -1.656 104.443  1.00 32.69           C  
-ATOM   5694  CE2 PHE C 152      16.058  -0.008 104.545  1.00 31.46           C  
-ATOM   5695  CZ  PHE C 152      15.438  -1.068 103.888  1.00 32.11           C  
-ATOM   5696  N   GLY C 153      14.372   3.397 107.618  1.00 34.21           N  
-ATOM   5697  CA  GLY C 153      15.088   4.563 107.129  1.00 35.18           C  
-ATOM   5698  C   GLY C 153      16.522   4.234 106.750  1.00 35.96           C  
-ATOM   5699  O   GLY C 153      17.006   3.122 106.998  1.00 36.37           O  
-ATOM   5700  N   VAL C 154      17.207   5.204 106.148  1.00 36.47           N  
-ATOM   5701  CA  VAL C 154      18.580   4.999 105.685  1.00 36.85           C  
-ATOM   5702  C   VAL C 154      19.456   6.163 106.152  1.00 37.13           C  
-ATOM   5703  O   VAL C 154      19.313   7.273 105.638  1.00 37.19           O  
-ATOM   5704  CB  VAL C 154      18.662   4.863 104.137  1.00 36.86           C  
-ATOM   5705  CG1 VAL C 154      20.096   4.623 103.704  1.00 37.22           C  
-ATOM   5706  CG2 VAL C 154      17.782   3.742 103.625  1.00 36.18           C  
-ATOM   5707  N   PRO C 155      20.339   5.935 107.132  1.00 37.51           N  
-ATOM   5708  CA  PRO C 155      20.490   4.646 107.827  1.00 37.70           C  
-ATOM   5709  C   PRO C 155      19.382   4.365 108.847  1.00 38.13           C  
-ATOM   5710  O   PRO C 155      18.692   5.288 109.298  1.00 38.04           O  
-ATOM   5711  CB  PRO C 155      21.812   4.817 108.570  1.00 37.63           C  
-ATOM   5712  CG  PRO C 155      21.870   6.283 108.860  1.00 37.65           C  
-ATOM   5713  CD  PRO C 155      21.290   6.939 107.641  1.00 37.40           C  
-ATOM   5714  N   VAL C 156      19.234   3.090 109.199  1.00 38.34           N  
-ATOM   5715  CA  VAL C 156      18.220   2.645 110.145  1.00 38.75           C  
-ATOM   5716  C   VAL C 156      18.476   3.226 111.525  1.00 38.90           C  
-ATOM   5717  O   VAL C 156      19.626   3.446 111.906  1.00 39.34           O  
-ATOM   5718  CB  VAL C 156      18.158   1.085 110.245  1.00 38.75           C  
-ATOM   5719  CG1 VAL C 156      17.758   0.469 108.912  1.00 38.72           C  
-ATOM   5720  CG2 VAL C 156      19.484   0.495 110.731  1.00 38.53           C  
-ATOM   5721  N   ARG C 157      17.407   3.489 112.268  1.00 39.14           N  
-ATOM   5722  CA  ARG C 157      17.544   3.778 113.693  1.00 39.20           C  
-ATOM   5723  C   ARG C 157      17.112   2.552 114.503  1.00 38.99           C  
-ATOM   5724  O   ARG C 157      16.763   1.522 113.927  1.00 38.77           O  
-ATOM   5725  CB  ARG C 157      16.776   5.044 114.088  1.00 39.50           C  
-ATOM   5726  CG  ARG C 157      15.277   4.935 114.006  1.00 39.85           C  
-ATOM   5727  CD  ARG C 157      14.533   5.967 114.832  1.00 41.78           C  
-ATOM   5728  NE  ARG C 157      13.135   5.567 114.992  1.00 42.97           N  
-ATOM   5729  CZ  ARG C 157      12.158   5.891 114.153  1.00 42.73           C  
-ATOM   5730  NH1 ARG C 157      12.405   6.651 113.090  1.00 42.68           N  
-ATOM   5731  NH2 ARG C 157      10.925   5.464 114.385  1.00 42.72           N  
-ATOM   5732  N   THR C 158      17.164   2.655 115.828  1.00 39.00           N  
-ATOM   5733  CA  THR C 158      16.767   1.553 116.699  1.00 38.89           C  
-ATOM   5734  C   THR C 158      15.277   1.276 116.533  1.00 38.73           C  
-ATOM   5735  O   THR C 158      14.451   2.182 116.665  1.00 38.54           O  
-ATOM   5736  CB  THR C 158      17.117   1.862 118.171  1.00 38.90           C  
-ATOM   5737  OG1 THR C 158      18.536   1.780 118.354  1.00 38.71           O  
-ATOM   5738  CG2 THR C 158      16.597   0.762 119.095  1.00 39.68           C  
-ATOM   5739  N   TYR C 159      14.944   0.029 116.207  1.00 38.68           N  
-ATOM   5740  CA  TYR C 159      13.545  -0.379 116.066  1.00 38.67           C  
-ATOM   5741  C   TYR C 159      13.163  -1.336 117.191  1.00 38.82           C  
-ATOM   5742  O   TYR C 159      13.951  -1.534 118.125  1.00 38.57           O  
-ATOM   5743  CB  TYR C 159      13.291  -1.002 114.698  1.00 38.39           C  
-ATOM   5744  CG  TYR C 159      13.648  -0.108 113.534  1.00 38.14           C  
-ATOM   5745  CD1 TYR C 159      13.296   1.242 113.528  1.00 38.24           C  
-ATOM   5746  CD2 TYR C 159      14.333  -0.617 112.429  1.00 37.60           C  
-ATOM   5747  CE1 TYR C 159      13.619   2.058 112.456  1.00 38.02           C  
-ATOM   5748  CE2 TYR C 159      14.659   0.188 111.358  1.00 37.64           C  
-ATOM   5749  CZ  TYR C 159      14.300   1.524 111.377  1.00 38.33           C  
-ATOM   5750  OH  TYR C 159      14.624   2.330 110.316  1.00 39.28           O  
-HETATM 5751  N   TPO C 160      11.964  -1.915 117.111  1.00 38.99           N  
-HETATM 5752  CA  TPO C 160      11.461  -2.789 118.169  1.00 39.33           C  
-HETATM 5753  CB  TPO C 160      10.026  -3.232 117.891  1.00 38.82           C  
-HETATM 5754  CG2 TPO C 160       9.471  -4.040 119.067  1.00 38.21           C  
-HETATM 5755  OG1 TPO C 160       9.205  -2.079 117.692  1.00 37.46           O  
-HETATM 5756  P   TPO C 160       8.651  -1.632 116.240  1.00 33.87           P  
-HETATM 5757  O1P TPO C 160       7.888  -0.250 116.366  1.00 34.93           O  
-HETATM 5758  O2P TPO C 160       9.899  -1.477 115.261  1.00 35.07           O  
-HETATM 5759  O3P TPO C 160       7.644  -2.713 115.679  1.00 34.85           O  
-HETATM 5760  C   TPO C 160      12.391  -3.962 118.380  1.00 40.17           C  
-HETATM 5761  O   TPO C 160      12.732  -4.667 117.450  1.00 40.06           O  
-ATOM   5762  N   HIS C 161      12.812  -4.150 119.629  1.00 41.47           N  
-ATOM   5763  CA  HIS C 161      13.722  -5.231 120.013  1.00 42.51           C  
-ATOM   5764  C   HIS C 161      12.972  -6.557 120.087  1.00 42.38           C  
-ATOM   5765  O   HIS C 161      11.742  -6.576 120.155  1.00 42.28           O  
-ATOM   5766  CB  HIS C 161      14.360  -4.900 121.368  1.00 43.13           C  
-ATOM   5767  CG  HIS C 161      15.618  -5.662 121.669  1.00 46.43           C  
-ATOM   5768  ND1 HIS C 161      16.485  -5.288 122.676  1.00 48.92           N  
-ATOM   5769  CD2 HIS C 161      16.150  -6.779 121.113  1.00 48.38           C  
-ATOM   5770  CE1 HIS C 161      17.495  -6.138 122.724  1.00 49.13           C  
-ATOM   5771  NE2 HIS C 161      17.314  -7.052 121.788  1.00 49.72           N  
-ATOM   5772  N   GLU C 162      13.725  -7.659 120.043  1.00 42.50           N  
-ATOM   5773  CA  GLU C 162      13.210  -9.021 120.234  1.00 42.33           C  
-ATOM   5774  C   GLU C 162      12.115  -9.393 119.225  1.00 41.75           C  
-ATOM   5775  O   GLU C 162      11.204 -10.178 119.521  1.00 41.93           O  
-ATOM   5776  CB  GLU C 162      12.760  -9.242 121.692  1.00 43.03           C  
-ATOM   5777  CG  GLU C 162      13.860  -8.985 122.725  1.00 45.09           C  
-ATOM   5778  CD  GLU C 162      13.402  -9.151 124.170  1.00 48.97           C  
-ATOM   5779  OE1 GLU C 162      12.250  -8.779 124.494  1.00 49.75           O  
-ATOM   5780  OE2 GLU C 162      14.207  -9.651 124.995  1.00 51.11           O  
-ATOM   5781  N   VAL C 163      12.225  -8.811 118.032  1.00 40.54           N  
-ATOM   5782  CA  VAL C 163      11.365  -9.142 116.900  1.00 39.24           C  
-ATOM   5783  C   VAL C 163      11.744 -10.504 116.321  1.00 38.10           C  
-ATOM   5784  O   VAL C 163      12.778 -11.069 116.682  1.00 38.79           O  
-ATOM   5785  CB  VAL C 163      11.461  -8.068 115.788  1.00 39.43           C  
-ATOM   5786  CG1 VAL C 163      10.716  -6.802 116.206  1.00 38.61           C  
-ATOM   5787  CG2 VAL C 163      12.930  -7.770 115.435  1.00 39.01           C  
-ATOM   5788  N   VAL C 164      10.913 -11.010 115.417  1.00 36.35           N  
-ATOM   5789  CA  VAL C 164      11.102 -12.310 114.761  1.00 35.16           C  
-ATOM   5790  C   VAL C 164      10.878 -13.481 115.721  1.00 34.51           C  
-ATOM   5791  O   VAL C 164      11.456 -13.550 116.806  1.00 34.11           O  
-ATOM   5792  CB  VAL C 164      12.475 -12.468 113.993  1.00 35.21           C  
-ATOM   5793  CG1 VAL C 164      12.388 -13.592 112.975  1.00 34.13           C  
-ATOM   5794  CG2 VAL C 164      12.908 -11.169 113.293  1.00 34.89           C  
-ATOM   5795  N   THR C 165      10.008 -14.390 115.310  1.00 33.80           N  
-ATOM   5796  CA  THR C 165       9.786 -15.628 116.038  1.00 33.58           C  
-ATOM   5797  C   THR C 165      11.142 -16.263 116.351  1.00 33.36           C  
-ATOM   5798  O   THR C 165      11.995 -16.373 115.469  1.00 33.23           O  
-ATOM   5799  CB  THR C 165       8.896 -16.542 115.196  1.00 33.44           C  
-ATOM   5800  OG1 THR C 165       7.579 -15.982 115.159  1.00 32.79           O  
-ATOM   5801  CG2 THR C 165       8.697 -17.904 115.855  1.00 33.44           C  
-ATOM   5802  N   LEU C 166      11.335 -16.632 117.617  1.00 33.03           N  
-ATOM   5803  CA  LEU C 166      12.619 -17.125 118.133  1.00 32.77           C  
-ATOM   5804  C   LEU C 166      13.451 -17.962 117.155  1.00 32.51           C  
-ATOM   5805  O   LEU C 166      14.584 -17.601 116.843  1.00 32.65           O  
-ATOM   5806  CB  LEU C 166      12.407 -17.903 119.434  1.00 32.63           C  
-ATOM   5807  CG  LEU C 166      13.638 -18.487 120.142  1.00 33.29           C  
-ATOM   5808  CD1 LEU C 166      14.509 -17.397 120.777  1.00 32.78           C  
-ATOM   5809  CD2 LEU C 166      13.203 -19.508 121.183  1.00 34.23           C  
-ATOM   5810  N   TRP C 167      12.882 -19.064 116.672  1.00 32.31           N  
-ATOM   5811  CA  TRP C 167      13.589 -20.008 115.797  1.00 32.28           C  
-ATOM   5812  C   TRP C 167      14.229 -19.347 114.572  1.00 32.43           C  
-ATOM   5813  O   TRP C 167      15.214 -19.854 114.022  1.00 32.85           O  
-ATOM   5814  CB  TRP C 167      12.642 -21.121 115.334  1.00 31.94           C  
-ATOM   5815  CG  TRP C 167      12.202 -22.063 116.417  1.00 31.28           C  
-ATOM   5816  CD1 TRP C 167      12.469 -21.971 117.759  1.00 31.09           C  
-ATOM   5817  CD2 TRP C 167      11.406 -23.245 116.253  1.00 30.08           C  
-ATOM   5818  NE1 TRP C 167      11.888 -23.021 118.431  1.00 30.29           N  
-ATOM   5819  CE2 TRP C 167      11.229 -23.818 117.532  1.00 29.27           C  
-ATOM   5820  CE3 TRP C 167      10.824 -23.884 115.150  1.00 28.66           C  
-ATOM   5821  CZ2 TRP C 167      10.504 -24.998 117.736  1.00 28.65           C  
-ATOM   5822  CZ3 TRP C 167      10.097 -25.054 115.360  1.00 28.04           C  
-ATOM   5823  CH2 TRP C 167       9.948 -25.596 116.643  1.00 26.25           C  
-ATOM   5824  N   TYR C 168      13.672 -18.215 114.157  1.00 32.37           N  
-ATOM   5825  CA  TYR C 168      14.093 -17.550 112.921  1.00 32.51           C  
-ATOM   5826  C   TYR C 168      14.808 -16.219 113.186  1.00 32.88           C  
-ATOM   5827  O   TYR C 168      15.142 -15.483 112.261  1.00 33.10           O  
-ATOM   5828  CB  TYR C 168      12.892 -17.409 111.975  1.00 32.06           C  
-ATOM   5829  CG  TYR C 168      12.230 -18.751 111.735  1.00 30.66           C  
-ATOM   5830  CD1 TYR C 168      12.702 -19.611 110.748  1.00 30.08           C  
-ATOM   5831  CD2 TYR C 168      11.172 -19.184 112.532  1.00 29.30           C  
-ATOM   5832  CE1 TYR C 168      12.132 -20.859 110.546  1.00 28.17           C  
-ATOM   5833  CE2 TYR C 168      10.586 -20.439 112.336  1.00 28.28           C  
-ATOM   5834  CZ  TYR C 168      11.079 -21.267 111.338  1.00 28.65           C  
-ATOM   5835  OH  TYR C 168      10.521 -22.509 111.128  1.00 28.45           O  
-ATOM   5836  N   ARG C 169      15.063 -15.952 114.463  1.00 33.46           N  
-ATOM   5837  CA  ARG C 169      15.688 -14.719 114.933  1.00 34.22           C  
-ATOM   5838  C   ARG C 169      17.192 -14.726 114.663  1.00 35.01           C  
-ATOM   5839  O   ARG C 169      17.878 -15.711 114.949  1.00 35.00           O  
-ATOM   5840  CB  ARG C 169      15.427 -14.580 116.432  1.00 34.04           C  
-ATOM   5841  CG  ARG C 169      15.789 -13.243 117.060  1.00 34.10           C  
-ATOM   5842  CD  ARG C 169      15.222 -13.065 118.472  1.00 33.61           C  
-ATOM   5843  NE  ARG C 169      13.776 -13.297 118.521  1.00 32.62           N  
-ATOM   5844  CZ  ARG C 169      13.094 -13.589 119.623  1.00 32.75           C  
-ATOM   5845  NH1 ARG C 169      13.715 -13.677 120.796  1.00 32.80           N  
-ATOM   5846  NH2 ARG C 169      11.784 -13.789 119.558  1.00 31.03           N  
-ATOM   5847  N   ALA C 170      17.695 -13.624 114.110  1.00 36.00           N  
-ATOM   5848  CA  ALA C 170      19.122 -13.481 113.790  1.00 36.95           C  
-ATOM   5849  C   ALA C 170      19.964 -13.317 115.061  1.00 37.86           C  
-ATOM   5850  O   ALA C 170      19.449 -12.876 116.094  1.00 38.27           O  
-ATOM   5851  CB  ALA C 170      19.335 -12.302 112.846  1.00 36.64           C  
-ATOM   5852  N   PRO C 171      21.243 -13.692 115.008  1.00 38.88           N  
-ATOM   5853  CA  PRO C 171      22.133 -13.533 116.167  1.00 39.58           C  
-ATOM   5854  C   PRO C 171      22.210 -12.091 116.661  1.00 40.18           C  
-ATOM   5855  O   PRO C 171      22.239 -11.891 117.874  1.00 40.42           O  
-ATOM   5856  CB  PRO C 171      23.494 -14.000 115.635  1.00 39.67           C  
-ATOM   5857  CG  PRO C 171      23.364 -13.947 114.146  1.00 39.24           C  
-ATOM   5858  CD  PRO C 171      21.942 -14.319 113.869  1.00 38.98           C  
-ATOM   5859  N   GLU C 172      22.212 -11.113 115.753  1.00 40.93           N  
-ATOM   5860  CA  GLU C 172      22.254  -9.701 116.149  1.00 41.60           C  
-ATOM   5861  C   GLU C 172      21.045  -9.262 116.993  1.00 42.09           C  
-ATOM   5862  O   GLU C 172      21.162  -8.349 117.816  1.00 42.28           O  
-ATOM   5863  CB  GLU C 172      22.454  -8.776 114.934  1.00 41.61           C  
-ATOM   5864  CG  GLU C 172      21.315  -8.773 113.920  1.00 41.20           C  
-ATOM   5865  CD  GLU C 172      21.592  -9.638 112.705  1.00 40.54           C  
-ATOM   5866  OE1 GLU C 172      22.287 -10.671 112.841  1.00 40.22           O  
-ATOM   5867  OE2 GLU C 172      21.097  -9.293 111.612  1.00 39.57           O  
-ATOM   5868  N   ILE C 173      19.898  -9.917 116.801  1.00 42.56           N  
-ATOM   5869  CA  ILE C 173      18.700  -9.619 117.595  1.00 42.89           C  
-ATOM   5870  C   ILE C 173      18.788 -10.284 118.963  1.00 43.44           C  
-ATOM   5871  O   ILE C 173      18.390  -9.702 119.975  1.00 43.47           O  
-ATOM   5872  CB  ILE C 173      17.392 -10.053 116.868  1.00 42.92           C  
-ATOM   5873  CG1 ILE C 173      17.376  -9.599 115.402  1.00 42.67           C  
-ATOM   5874  CG2 ILE C 173      16.156  -9.531 117.603  1.00 42.58           C  
-ATOM   5875  CD1 ILE C 173      17.667  -8.124 115.213  1.00 43.31           C  
-ATOM   5876  N   LEU C 174      19.319 -11.503 118.982  1.00 43.94           N  
-ATOM   5877  CA  LEU C 174      19.437 -12.277 120.209  1.00 44.56           C  
-ATOM   5878  C   LEU C 174      20.411 -11.629 121.188  1.00 45.10           C  
-ATOM   5879  O   LEU C 174      20.171 -11.617 122.398  1.00 45.01           O  
-ATOM   5880  CB  LEU C 174      19.878 -13.706 119.896  1.00 44.27           C  
-ATOM   5881  CG  LEU C 174      18.811 -14.656 119.354  1.00 44.52           C  
-ATOM   5882  CD1 LEU C 174      19.476 -15.877 118.728  1.00 44.39           C  
-ATOM   5883  CD2 LEU C 174      17.818 -15.069 120.444  1.00 44.06           C  
-ATOM   5884  N   LEU C 175      21.499 -11.085 120.649  1.00 45.78           N  
-ATOM   5885  CA  LEU C 175      22.524 -10.420 121.455  1.00 46.52           C  
-ATOM   5886  C   LEU C 175      22.152  -8.972 121.790  1.00 46.86           C  
-ATOM   5887  O   LEU C 175      22.882  -8.282 122.502  1.00 46.94           O  
-ATOM   5888  CB  LEU C 175      23.882 -10.485 120.748  1.00 46.58           C  
-ATOM   5889  CG  LEU C 175      24.359 -11.889 120.361  1.00 46.73           C  
-ATOM   5890  CD1 LEU C 175      25.342 -11.821 119.212  1.00 46.97           C  
-ATOM   5891  CD2 LEU C 175      24.971 -12.603 121.555  1.00 47.92           C  
-ATOM   5892  N   GLY C 176      21.014  -8.524 121.264  1.00 47.20           N  
-ATOM   5893  CA  GLY C 176      20.479  -7.212 121.568  1.00 47.58           C  
-ATOM   5894  C   GLY C 176      21.283  -6.040 121.047  1.00 47.87           C  
-ATOM   5895  O   GLY C 176      21.536  -5.087 121.787  1.00 48.07           O  
-ATOM   5896  N   CYS C 177      21.671  -6.109 119.774  1.00 48.05           N  
-ATOM   5897  CA  CYS C 177      22.390  -5.025 119.105  1.00 48.20           C  
-ATOM   5898  C   CYS C 177      21.515  -3.779 118.949  1.00 47.65           C  
-ATOM   5899  O   CYS C 177      20.292  -3.886 118.832  1.00 47.72           O  
-ATOM   5900  CB  CYS C 177      22.895  -5.487 117.734  1.00 48.35           C  
-ATOM   5901  SG  CYS C 177      24.187  -6.760 117.795  1.00 51.19           S  
-ATOM   5902  N   LYS C 178      22.156  -2.609 118.955  1.00 47.12           N  
-ATOM   5903  CA  LYS C 178      21.484  -1.310 118.837  1.00 46.45           C  
-ATOM   5904  C   LYS C 178      20.694  -1.190 117.541  1.00 45.68           C  
-ATOM   5905  O   LYS C 178      19.542  -0.759 117.543  1.00 45.70           O  
-ATOM   5906  CB  LYS C 178      22.507  -0.167 118.914  1.00 46.78           C  
-ATOM   5907  CG  LYS C 178      21.903   1.224 119.103  1.00 47.75           C  
-ATOM   5908  CD  LYS C 178      22.982   2.298 119.122  1.00 49.68           C  
-ATOM   5909  CE  LYS C 178      22.405   3.672 119.441  1.00 51.60           C  
-ATOM   5910  NZ  LYS C 178      23.405   4.776 119.244  1.00 52.73           N  
-ATOM   5911  N   TYR C 179      21.326  -1.579 116.441  1.00 44.63           N  
-ATOM   5912  CA  TYR C 179      20.749  -1.415 115.122  1.00 43.70           C  
-ATOM   5913  C   TYR C 179      20.570  -2.761 114.448  1.00 42.67           C  
-ATOM   5914  O   TYR C 179      21.421  -3.655 114.577  1.00 42.64           O  
-ATOM   5915  CB  TYR C 179      21.643  -0.520 114.258  1.00 44.11           C  
-ATOM   5916  CG  TYR C 179      21.838   0.890 114.788  1.00 45.63           C  
-ATOM   5917  CD1 TYR C 179      20.748   1.734 115.010  1.00 47.25           C  
-ATOM   5918  CD2 TYR C 179      23.114   1.384 115.052  1.00 47.22           C  
-ATOM   5919  CE1 TYR C 179      20.925   3.031 115.491  1.00 48.61           C  
-ATOM   5920  CE2 TYR C 179      23.302   2.682 115.535  1.00 48.77           C  
-ATOM   5921  CZ  TYR C 179      22.202   3.498 115.752  1.00 49.28           C  
-ATOM   5922  OH  TYR C 179      22.377   4.782 116.228  1.00 50.85           O  
-ATOM   5923  N   TYR C 180      19.453  -2.904 113.741  1.00 41.07           N  
-ATOM   5924  CA  TYR C 180      19.256  -4.024 112.836  1.00 39.66           C  
-ATOM   5925  C   TYR C 180      18.545  -3.577 111.562  1.00 38.91           C  
-ATOM   5926  O   TYR C 180      17.896  -2.524 111.535  1.00 38.66           O  
-ATOM   5927  CB  TYR C 180      18.538  -5.194 113.522  1.00 39.72           C  
-ATOM   5928  CG  TYR C 180      17.070  -4.972 113.849  1.00 39.11           C  
-ATOM   5929  CD1 TYR C 180      16.080  -5.155 112.879  1.00 38.67           C  
-ATOM   5930  CD2 TYR C 180      16.672  -4.608 115.132  1.00 38.26           C  
-ATOM   5931  CE1 TYR C 180      14.735  -4.964 113.179  1.00 36.98           C  
-ATOM   5932  CE2 TYR C 180      15.327  -4.414 115.442  1.00 37.63           C  
-ATOM   5933  CZ  TYR C 180      14.368  -4.593 114.462  1.00 37.30           C  
-ATOM   5934  OH  TYR C 180      13.041  -4.404 114.764  1.00 36.10           O  
-ATOM   5935  N   SER C 181      18.682  -4.380 110.509  1.00 37.83           N  
-ATOM   5936  CA  SER C 181      18.132  -4.039 109.203  1.00 37.14           C  
-ATOM   5937  C   SER C 181      17.830  -5.278 108.359  1.00 35.98           C  
-ATOM   5938  O   SER C 181      17.472  -6.327 108.896  1.00 36.04           O  
-ATOM   5939  CB  SER C 181      19.078  -3.087 108.458  1.00 37.25           C  
-ATOM   5940  OG  SER C 181      18.454  -2.597 107.282  1.00 39.19           O  
-ATOM   5941  N   THR C 182      17.986  -5.148 107.042  1.00 34.67           N  
-ATOM   5942  CA  THR C 182      17.543  -6.156 106.079  1.00 33.61           C  
-ATOM   5943  C   THR C 182      18.169  -7.531 106.276  1.00 33.28           C  
-ATOM   5944  O   THR C 182      17.615  -8.538 105.821  1.00 33.48           O  
-ATOM   5945  CB  THR C 182      17.807  -5.675 104.641  1.00 33.62           C  
-ATOM   5946  OG1 THR C 182      19.211  -5.460 104.462  1.00 33.14           O  
-ATOM   5947  CG2 THR C 182      17.178  -4.302 104.398  1.00 32.99           C  
-ATOM   5948  N   ALA C 183      19.315  -7.569 106.954  1.00 32.61           N  
-ATOM   5949  CA  ALA C 183      20.035  -8.817 107.182  1.00 32.03           C  
-ATOM   5950  C   ALA C 183      19.262  -9.764 108.092  1.00 31.63           C  
-ATOM   5951  O   ALA C 183      19.471 -10.980 108.033  1.00 31.80           O  
-ATOM   5952  CB  ALA C 183      21.440  -8.551 107.735  1.00 31.94           C  
-ATOM   5953  N   VAL C 184      18.362  -9.223 108.918  1.00 31.20           N  
-ATOM   5954  CA  VAL C 184      17.528 -10.081 109.770  1.00 30.63           C  
-ATOM   5955  C   VAL C 184      16.558 -10.923 108.957  1.00 30.26           C  
-ATOM   5956  O   VAL C 184      16.333 -12.086 109.280  1.00 30.37           O  
-ATOM   5957  CB  VAL C 184      16.804  -9.325 110.933  1.00 30.64           C  
-ATOM   5958  CG1 VAL C 184      17.768  -8.399 111.650  1.00 30.63           C  
-ATOM   5959  CG2 VAL C 184      15.559  -8.574 110.458  1.00 30.63           C  
-ATOM   5960  N   ASP C 185      16.016 -10.363 107.884  1.00 30.29           N  
-ATOM   5961  CA  ASP C 185      15.090 -11.114 107.048  1.00 30.30           C  
-ATOM   5962  C   ASP C 185      15.846 -12.197 106.298  1.00 30.50           C  
-ATOM   5963  O   ASP C 185      15.330 -13.301 106.106  1.00 30.92           O  
-ATOM   5964  CB  ASP C 185      14.364 -10.204 106.051  1.00 30.36           C  
-ATOM   5965  CG  ASP C 185      13.231  -9.400 106.685  1.00 30.77           C  
-ATOM   5966  OD1 ASP C 185      12.664  -9.817 107.723  1.00 29.66           O  
-ATOM   5967  OD2 ASP C 185      12.834  -8.327 106.190  1.00 31.68           O  
-ATOM   5968  N   ILE C 186      17.073 -11.877 105.887  1.00 30.44           N  
-ATOM   5969  CA  ILE C 186      17.908 -12.804 105.133  1.00 30.33           C  
-ATOM   5970  C   ILE C 186      18.242 -14.022 105.982  1.00 30.31           C  
-ATOM   5971  O   ILE C 186      18.190 -15.154 105.501  1.00 30.92           O  
-ATOM   5972  CB  ILE C 186      19.198 -12.098 104.610  1.00 30.12           C  
-ATOM   5973  CG1 ILE C 186      18.871 -11.203 103.405  1.00 29.65           C  
-ATOM   5974  CG2 ILE C 186      20.283 -13.119 104.273  1.00 30.08           C  
-ATOM   5975  CD1 ILE C 186      18.386 -11.946 102.166  1.00 29.41           C  
-ATOM   5976  N   TRP C 187      18.572 -13.787 107.246  1.00 30.19           N  
-ATOM   5977  CA  TRP C 187      18.783 -14.872 108.190  1.00 30.23           C  
-ATOM   5978  C   TRP C 187      17.590 -15.835 108.185  1.00 30.27           C  
-ATOM   5979  O   TRP C 187      17.762 -17.047 107.977  1.00 29.95           O  
-ATOM   5980  CB  TRP C 187      19.004 -14.319 109.597  1.00 30.40           C  
-ATOM   5981  CG  TRP C 187      19.275 -15.386 110.609  1.00 30.99           C  
-ATOM   5982  CD1 TRP C 187      18.356 -16.036 111.386  1.00 31.01           C  
-ATOM   5983  CD2 TRP C 187      20.549 -15.944 110.944  1.00 31.58           C  
-ATOM   5984  NE1 TRP C 187      18.983 -16.953 112.195  1.00 31.39           N  
-ATOM   5985  CE2 TRP C 187      20.330 -16.922 111.942  1.00 31.74           C  
-ATOM   5986  CE3 TRP C 187      21.865 -15.711 110.507  1.00 32.05           C  
-ATOM   5987  CZ2 TRP C 187      21.369 -17.665 112.508  1.00 31.84           C  
-ATOM   5988  CZ3 TRP C 187      22.900 -16.447 111.075  1.00 32.51           C  
-ATOM   5989  CH2 TRP C 187      22.645 -17.411 112.065  1.00 32.49           C  
-ATOM   5990  N   SER C 188      16.390 -15.286 108.404  1.00 30.24           N  
-ATOM   5991  CA  SER C 188      15.162 -16.080 108.470  1.00 30.17           C  
-ATOM   5992  C   SER C 188      14.987 -16.960 107.231  1.00 30.09           C  
-ATOM   5993  O   SER C 188      14.723 -18.156 107.345  1.00 29.99           O  
-ATOM   5994  CB  SER C 188      13.938 -15.175 108.675  1.00 30.38           C  
-ATOM   5995  OG  SER C 188      14.070 -14.396 109.848  1.00 30.37           O  
-ATOM   5996  N   LEU C 189      15.158 -16.370 106.050  1.00 30.24           N  
-ATOM   5997  CA  LEU C 189      15.116 -17.129 104.799  1.00 30.33           C  
-ATOM   5998  C   LEU C 189      16.186 -18.221 104.732  1.00 30.32           C  
-ATOM   5999  O   LEU C 189      15.964 -19.280 104.140  1.00 30.65           O  
-ATOM   6000  CB  LEU C 189      15.221 -16.202 103.587  1.00 30.09           C  
-ATOM   6001  CG  LEU C 189      13.880 -15.863 102.938  1.00 31.13           C  
-ATOM   6002  CD1 LEU C 189      14.046 -15.179 101.574  1.00 31.66           C  
-ATOM   6003  CD2 LEU C 189      13.015 -17.096 102.806  1.00 31.52           C  
-ATOM   6004  N   GLY C 190      17.338 -17.958 105.336  1.00 30.57           N  
-ATOM   6005  CA  GLY C 190      18.381 -18.961 105.479  1.00 31.25           C  
-ATOM   6006  C   GLY C 190      17.891 -20.148 106.287  1.00 31.35           C  
-ATOM   6007  O   GLY C 190      17.966 -21.290 105.826  1.00 31.68           O  
-ATOM   6008  N   CYS C 191      17.372 -19.872 107.486  1.00 31.21           N  
-ATOM   6009  CA  CYS C 191      16.721 -20.891 108.310  1.00 30.81           C  
-ATOM   6010  C   CYS C 191      15.628 -21.634 107.542  1.00 30.73           C  
-ATOM   6011  O   CYS C 191      15.538 -22.858 107.628  1.00 30.47           O  
-ATOM   6012  CB  CYS C 191      16.137 -20.277 109.586  1.00 30.35           C  
-ATOM   6013  SG  CYS C 191      17.378 -19.512 110.639  1.00 30.83           S  
-ATOM   6014  N   ILE C 192      14.813 -20.898 106.782  1.00 30.84           N  
-ATOM   6015  CA  ILE C 192      13.744 -21.514 105.980  1.00 31.02           C  
-ATOM   6016  C   ILE C 192      14.270 -22.417 104.848  1.00 31.06           C  
-ATOM   6017  O   ILE C 192      13.680 -23.454 104.548  1.00 30.91           O  
-ATOM   6018  CB  ILE C 192      12.749 -20.436 105.450  1.00 30.95           C  
-ATOM   6019  CG1 ILE C 192      11.940 -19.853 106.615  1.00 30.83           C  
-ATOM   6020  CG2 ILE C 192      11.808 -21.018 104.383  1.00 30.31           C  
-ATOM   6021  CD1 ILE C 192      11.363 -18.469 106.346  1.00 31.91           C  
-ATOM   6022  N   PHE C 193      15.377 -22.016 104.231  1.00 31.63           N  
-ATOM   6023  CA  PHE C 193      16.007 -22.794 103.161  1.00 32.21           C  
-ATOM   6024  C   PHE C 193      16.432 -24.166 103.706  1.00 32.60           C  
-ATOM   6025  O   PHE C 193      16.067 -25.211 103.149  1.00 32.34           O  
-ATOM   6026  CB  PHE C 193      17.211 -22.015 102.617  1.00 32.41           C  
-ATOM   6027  CG  PHE C 193      17.940 -22.683 101.476  1.00 32.34           C  
-ATOM   6028  CD1 PHE C 193      17.314 -23.611 100.646  1.00 32.83           C  
-ATOM   6029  CD2 PHE C 193      19.265 -22.341 101.215  1.00 32.37           C  
-ATOM   6030  CE1 PHE C 193      18.009 -24.202  99.582  1.00 33.37           C  
-ATOM   6031  CE2 PHE C 193      19.968 -22.930 100.154  1.00 32.57           C  
-ATOM   6032  CZ  PHE C 193      19.336 -23.863  99.340  1.00 32.65           C  
-ATOM   6033  N   ALA C 194      17.174 -24.146 104.812  1.00 32.87           N  
-ATOM   6034  CA  ALA C 194      17.603 -25.364 105.498  1.00 33.18           C  
-ATOM   6035  C   ALA C 194      16.420 -26.243 105.874  1.00 33.60           C  
-ATOM   6036  O   ALA C 194      16.477 -27.465 105.726  1.00 33.93           O  
-ATOM   6037  CB  ALA C 194      18.409 -25.015 106.725  1.00 33.29           C  
-ATOM   6038  N   GLU C 195      15.343 -25.605 106.333  1.00 33.71           N  
-ATOM   6039  CA  GLU C 195      14.136 -26.300 106.774  1.00 33.52           C  
-ATOM   6040  C   GLU C 195      13.386 -26.985 105.633  1.00 33.55           C  
-ATOM   6041  O   GLU C 195      12.823 -28.055 105.824  1.00 33.10           O  
-ATOM   6042  CB  GLU C 195      13.209 -25.341 107.535  1.00 33.23           C  
-ATOM   6043  CG  GLU C 195      12.101 -26.017 108.337  1.00 32.80           C  
-ATOM   6044  CD  GLU C 195      11.384 -25.064 109.282  1.00 32.50           C  
-ATOM   6045  OE1 GLU C 195      12.002 -24.061 109.714  1.00 31.08           O  
-ATOM   6046  OE2 GLU C 195      10.205 -25.321 109.605  1.00 32.46           O  
-ATOM   6047  N   MET C 196      13.368 -26.366 104.454  1.00 33.88           N  
-ATOM   6048  CA  MET C 196      12.764 -26.995 103.274  1.00 33.91           C  
-ATOM   6049  C   MET C 196      13.498 -28.285 102.870  1.00 34.09           C  
-ATOM   6050  O   MET C 196      12.888 -29.208 102.335  1.00 34.05           O  
-ATOM   6051  CB  MET C 196      12.729 -26.026 102.093  1.00 34.08           C  
-ATOM   6052  CG  MET C 196      11.657 -24.937 102.170  1.00 34.33           C  
-ATOM   6053  SD  MET C 196      11.321 -24.219 100.532  1.00 33.79           S  
-ATOM   6054  CE  MET C 196      12.730 -23.145 100.345  1.00 30.37           C  
-ATOM   6055  N   VAL C 197      14.802 -28.336 103.119  1.00 34.46           N  
-ATOM   6056  CA  VAL C 197      15.614 -29.510 102.782  1.00 35.28           C  
-ATOM   6057  C   VAL C 197      15.365 -30.687 103.735  1.00 35.67           C  
-ATOM   6058  O   VAL C 197      15.084 -31.795 103.286  1.00 35.70           O  
-ATOM   6059  CB  VAL C 197      17.134 -29.191 102.754  1.00 35.16           C  
-ATOM   6060  CG1 VAL C 197      17.930 -30.430 102.360  1.00 35.55           C  
-ATOM   6061  CG2 VAL C 197      17.439 -28.042 101.797  1.00 35.11           C  
-ATOM   6062  N   THR C 198      15.463 -30.437 105.041  1.00 36.15           N  
-ATOM   6063  CA  THR C 198      15.312 -31.485 106.051  1.00 36.58           C  
-ATOM   6064  C   THR C 198      13.875 -31.648 106.554  1.00 37.09           C  
-ATOM   6065  O   THR C 198      13.554 -32.646 107.199  1.00 36.94           O  
-ATOM   6066  CB  THR C 198      16.244 -31.221 107.253  1.00 36.48           C  
-ATOM   6067  OG1 THR C 198      15.821 -30.033 107.932  1.00 36.28           O  
-ATOM   6068  CG2 THR C 198      17.674 -30.888 106.796  1.00 36.80           C  
-ATOM   6069  N   ARG C 199      13.024 -30.663 106.270  1.00 37.67           N  
-ATOM   6070  CA  ARG C 199      11.647 -30.588 106.811  1.00 38.25           C  
-ATOM   6071  C   ARG C 199      11.585 -30.602 108.351  1.00 38.31           C  
-ATOM   6072  O   ARG C 199      10.596 -31.056 108.947  1.00 38.16           O  
-ATOM   6073  CB  ARG C 199      10.726 -31.657 106.215  1.00 38.47           C  
-ATOM   6074  CG  ARG C 199      10.730 -31.739 104.702  1.00 40.34           C  
-ATOM   6075  CD  ARG C 199      10.709 -33.159 104.179  1.00 43.73           C  
-ATOM   6076  NE  ARG C 199      12.054 -33.719 104.063  1.00 46.53           N  
-ATOM   6077  CZ  ARG C 199      12.348 -35.007 104.163  1.00 48.32           C  
-ATOM   6078  NH1 ARG C 199      11.396 -35.903 104.387  1.00 48.65           N  
-ATOM   6079  NH2 ARG C 199      13.610 -35.405 104.041  1.00 51.04           N  
-ATOM   6080  N   ARG C 200      12.655 -30.120 108.978  1.00 38.07           N  
-ATOM   6081  CA  ARG C 200      12.648 -29.793 110.400  1.00 38.30           C  
-ATOM   6082  C   ARG C 200      13.386 -28.486 110.615  1.00 38.02           C  
-ATOM   6083  O   ARG C 200      14.345 -28.179 109.901  1.00 37.93           O  
-ATOM   6084  CB  ARG C 200      13.277 -30.893 111.270  1.00 38.62           C  
-ATOM   6085  CG  ARG C 200      13.931 -32.055 110.532  1.00 40.08           C  
-ATOM   6086  CD  ARG C 200      14.667 -33.023 111.454  1.00 42.51           C  
-ATOM   6087  NE  ARG C 200      14.523 -34.416 111.033  1.00 44.37           N  
-ATOM   6088  CZ  ARG C 200      13.584 -35.244 111.479  1.00 45.74           C  
-ATOM   6089  NH1 ARG C 200      12.690 -34.837 112.373  1.00 46.07           N  
-ATOM   6090  NH2 ARG C 200      13.544 -36.492 111.035  1.00 46.65           N  
-ATOM   6091  N   ALA C 201      12.939 -27.720 111.604  1.00 37.64           N  
-ATOM   6092  CA  ALA C 201      13.560 -26.446 111.938  1.00 37.22           C  
-ATOM   6093  C   ALA C 201      15.068 -26.584 112.162  1.00 36.95           C  
-ATOM   6094  O   ALA C 201      15.535 -27.585 112.714  1.00 37.11           O  
-ATOM   6095  CB  ALA C 201      12.890 -25.853 113.148  1.00 37.58           C  
-ATOM   6096  N   LEU C 202      15.824 -25.580 111.721  1.00 36.34           N  
-ATOM   6097  CA  LEU C 202      17.282 -25.608 111.811  1.00 35.70           C  
-ATOM   6098  C   LEU C 202      17.791 -25.286 113.216  1.00 35.34           C  
-ATOM   6099  O   LEU C 202      18.715 -25.932 113.712  1.00 35.18           O  
-ATOM   6100  CB  LEU C 202      17.896 -24.661 110.773  1.00 35.89           C  
-ATOM   6101  CG  LEU C 202      19.411 -24.445 110.707  1.00 35.83           C  
-ATOM   6102  CD1 LEU C 202      20.141 -25.705 110.252  1.00 36.14           C  
-ATOM   6103  CD2 LEU C 202      19.721 -23.297 109.770  1.00 36.41           C  
-ATOM   6104  N   PHE C 203      17.196 -24.279 113.847  1.00 35.14           N  
-ATOM   6105  CA  PHE C 203      17.548 -23.897 115.214  1.00 34.87           C  
-ATOM   6106  C   PHE C 203      16.286 -23.808 116.076  1.00 34.99           C  
-ATOM   6107  O   PHE C 203      15.773 -22.711 116.308  1.00 34.81           O  
-ATOM   6108  CB  PHE C 203      18.296 -22.555 115.243  1.00 34.55           C  
-ATOM   6109  CG  PHE C 203      19.494 -22.489 114.328  1.00 34.14           C  
-ATOM   6110  CD1 PHE C 203      20.573 -23.358 114.497  1.00 33.06           C  
-ATOM   6111  CD2 PHE C 203      19.554 -21.535 113.313  1.00 32.97           C  
-ATOM   6112  CE1 PHE C 203      21.681 -23.294 113.650  1.00 32.91           C  
-ATOM   6113  CE2 PHE C 203      20.661 -21.457 112.469  1.00 32.37           C  
-ATOM   6114  CZ  PHE C 203      21.726 -22.343 112.637  1.00 32.38           C  
-ATOM   6115  N   PRO C 204      15.770 -24.949 116.534  1.00 35.09           N  
-ATOM   6116  CA  PRO C 204      14.570 -24.953 117.378  1.00 35.33           C  
-ATOM   6117  C   PRO C 204      14.870 -24.733 118.863  1.00 35.58           C  
-ATOM   6118  O   PRO C 204      14.721 -25.657 119.665  1.00 35.98           O  
-ATOM   6119  CB  PRO C 204      13.976 -26.344 117.134  1.00 34.95           C  
-ATOM   6120  CG  PRO C 204      15.156 -27.209 116.788  1.00 35.00           C  
-ATOM   6121  CD  PRO C 204      16.259 -26.316 116.270  1.00 35.09           C  
-ATOM   6122  N   GLY C 205      15.283 -23.520 119.220  1.00 35.99           N  
-ATOM   6123  CA  GLY C 205      15.553 -23.186 120.609  1.00 37.04           C  
-ATOM   6124  C   GLY C 205      14.262 -23.080 121.399  1.00 37.99           C  
-ATOM   6125  O   GLY C 205      13.223 -22.716 120.834  1.00 37.70           O  
-ATOM   6126  N   ASP C 206      14.305 -23.417 122.688  1.00 39.05           N  
-ATOM   6127  CA  ASP C 206      13.136 -23.195 123.557  1.00 40.50           C  
-ATOM   6128  C   ASP C 206      13.383 -22.099 124.579  1.00 40.68           C  
-ATOM   6129  O   ASP C 206      12.598 -21.906 125.509  1.00 41.24           O  
-ATOM   6130  CB  ASP C 206      12.620 -24.480 124.224  1.00 40.89           C  
-ATOM   6131  CG  ASP C 206      13.646 -25.577 124.265  1.00 42.34           C  
-ATOM   6132  OD1 ASP C 206      14.755 -25.338 124.787  1.00 45.74           O  
-ATOM   6133  OD2 ASP C 206      13.428 -26.716 123.811  1.00 43.99           O  
-ATOM   6134  N   SER C 207      14.480 -21.380 124.380  1.00 40.84           N  
-ATOM   6135  CA  SER C 207      14.807 -20.183 125.143  1.00 40.88           C  
-ATOM   6136  C   SER C 207      15.799 -19.374 124.318  1.00 40.75           C  
-ATOM   6137  O   SER C 207      16.348 -19.884 123.339  1.00 40.67           O  
-ATOM   6138  CB  SER C 207      15.423 -20.555 126.491  1.00 40.85           C  
-ATOM   6139  OG  SER C 207      16.705 -21.135 126.312  1.00 41.37           O  
-ATOM   6140  N   GLU C 208      16.032 -18.127 124.720  1.00 40.73           N  
-ATOM   6141  CA  GLU C 208      16.990 -17.256 124.045  1.00 41.11           C  
-ATOM   6142  C   GLU C 208      18.413 -17.829 124.070  1.00 40.76           C  
-ATOM   6143  O   GLU C 208      19.150 -17.730 123.086  1.00 40.71           O  
-ATOM   6144  CB  GLU C 208      16.986 -15.871 124.689  1.00 41.25           C  
-ATOM   6145  CG  GLU C 208      16.256 -14.815 123.882  1.00 43.96           C  
-ATOM   6146  CD  GLU C 208      16.338 -13.443 124.522  1.00 46.60           C  
-ATOM   6147  OE1 GLU C 208      17.414 -12.803 124.434  1.00 47.90           O  
-ATOM   6148  OE2 GLU C 208      15.326 -13.009 125.119  1.00 48.87           O  
-ATOM   6149  N   ILE C 209      18.787 -18.425 125.198  1.00 40.30           N  
-ATOM   6150  CA  ILE C 209      20.124 -18.987 125.371  1.00 40.20           C  
-ATOM   6151  C   ILE C 209      20.328 -20.287 124.571  1.00 39.77           C  
-ATOM   6152  O   ILE C 209      21.364 -20.462 123.924  1.00 39.57           O  
-ATOM   6153  CB  ILE C 209      20.455 -19.171 126.879  1.00 40.24           C  
-ATOM   6154  CG1 ILE C 209      21.846 -19.789 127.057  1.00 40.71           C  
-ATOM   6155  CG2 ILE C 209      19.343 -19.945 127.605  1.00 40.83           C  
-ATOM   6156  CD1 ILE C 209      21.971 -20.685 128.258  1.00 42.91           C  
-ATOM   6157  N   ASP C 210      19.333 -21.176 124.615  1.00 39.20           N  
-ATOM   6158  CA  ASP C 210      19.354 -22.428 123.863  1.00 38.82           C  
-ATOM   6159  C   ASP C 210      19.442 -22.126 122.373  1.00 38.66           C  
-ATOM   6160  O   ASP C 210      20.176 -22.795 121.635  1.00 38.25           O  
-ATOM   6161  CB  ASP C 210      18.099 -23.249 124.162  1.00 38.81           C  
-ATOM   6162  CG  ASP C 210      18.105 -24.609 123.487  1.00 39.30           C  
-ATOM   6163  OD1 ASP C 210      19.117 -25.340 123.585  1.00 38.36           O  
-ATOM   6164  OD2 ASP C 210      17.123 -25.037 122.842  1.00 40.34           O  
-ATOM   6165  N   GLN C 211      18.692 -21.106 121.948  1.00 38.32           N  
-ATOM   6166  CA  GLN C 211      18.735 -20.612 120.576  1.00 37.67           C  
-ATOM   6167  C   GLN C 211      20.157 -20.219 120.195  1.00 37.86           C  
-ATOM   6168  O   GLN C 211      20.657 -20.624 119.149  1.00 37.60           O  
-ATOM   6169  CB  GLN C 211      17.785 -19.423 120.408  1.00 37.54           C  
-ATOM   6170  CG  GLN C 211      17.536 -18.986 118.969  1.00 36.12           C  
-ATOM   6171  CD  GLN C 211      16.787 -20.013 118.149  1.00 34.90           C  
-ATOM   6172  OE1 GLN C 211      15.868 -20.672 118.647  1.00 33.91           O  
-ATOM   6173  NE2 GLN C 211      17.169 -20.150 116.884  1.00 34.39           N  
-ATOM   6174  N   LEU C 212      20.815 -19.455 121.061  1.00 38.20           N  
-ATOM   6175  CA  LEU C 212      22.155 -18.960 120.764  1.00 38.65           C  
-ATOM   6176  C   LEU C 212      23.197 -20.088 120.686  1.00 38.93           C  
-ATOM   6177  O   LEU C 212      24.048 -20.099 119.792  1.00 38.75           O  
-ATOM   6178  CB  LEU C 212      22.561 -17.894 121.779  1.00 38.76           C  
-ATOM   6179  CG  LEU C 212      23.629 -16.886 121.350  1.00 39.32           C  
-ATOM   6180  CD1 LEU C 212      23.019 -15.671 120.653  1.00 39.63           C  
-ATOM   6181  CD2 LEU C 212      24.424 -16.455 122.562  1.00 39.61           C  
-ATOM   6182  N   PHE C 213      23.109 -21.044 121.610  1.00 39.20           N  
-ATOM   6183  CA  PHE C 213      24.027 -22.180 121.633  1.00 39.39           C  
-ATOM   6184  C   PHE C 213      23.838 -23.071 120.406  1.00 39.68           C  
-ATOM   6185  O   PHE C 213      24.813 -23.608 119.870  1.00 39.92           O  
-ATOM   6186  CB  PHE C 213      23.871 -22.987 122.929  1.00 39.08           C  
-ATOM   6187  CG  PHE C 213      24.335 -22.258 124.173  1.00 39.47           C  
-ATOM   6188  CD1 PHE C 213      24.719 -20.912 124.126  1.00 39.61           C  
-ATOM   6189  CD2 PHE C 213      24.373 -22.916 125.396  1.00 39.01           C  
-ATOM   6190  CE1 PHE C 213      25.143 -20.243 125.276  1.00 39.68           C  
-ATOM   6191  CE2 PHE C 213      24.797 -22.258 126.551  1.00 39.66           C  
-ATOM   6192  CZ  PHE C 213      25.187 -20.920 126.490  1.00 39.99           C  
-ATOM   6193  N   ARG C 214      22.589 -23.209 119.962  1.00 39.92           N  
-ATOM   6194  CA  ARG C 214      22.254 -23.980 118.765  1.00 40.50           C  
-ATOM   6195  C   ARG C 214      22.882 -23.381 117.507  1.00 41.66           C  
-ATOM   6196  O   ARG C 214      23.355 -24.116 116.629  1.00 41.79           O  
-ATOM   6197  CB  ARG C 214      20.739 -24.064 118.581  1.00 39.94           C  
-ATOM   6198  CG  ARG C 214      20.051 -25.080 119.459  1.00 38.12           C  
-ATOM   6199  CD  ARG C 214      18.544 -25.132 119.266  1.00 35.00           C  
-ATOM   6200  NE  ARG C 214      17.900 -26.051 120.194  1.00 33.27           N  
-ATOM   6201  CZ  ARG C 214      17.804 -27.364 120.012  1.00 33.31           C  
-ATOM   6202  NH1 ARG C 214      18.320 -27.934 118.933  1.00 32.59           N  
-ATOM   6203  NH2 ARG C 214      17.187 -28.116 120.918  1.00 34.04           N  
-ATOM   6204  N   ILE C 215      22.877 -22.054 117.418  1.00 42.96           N  
-ATOM   6205  CA  ILE C 215      23.512 -21.362 116.296  1.00 44.58           C  
-ATOM   6206  C   ILE C 215      25.032 -21.476 116.407  1.00 46.16           C  
-ATOM   6207  O   ILE C 215      25.725 -21.665 115.407  1.00 46.34           O  
-ATOM   6208  CB  ILE C 215      23.068 -19.879 116.218  1.00 44.23           C  
-ATOM   6209  CG1 ILE C 215      21.554 -19.777 115.961  1.00 42.96           C  
-ATOM   6210  CG2 ILE C 215      23.853 -19.134 115.126  1.00 44.40           C  
-ATOM   6211  CD1 ILE C 215      20.992 -18.374 116.092  1.00 40.48           C  
-ATOM   6212  N   PHE C 216      25.538 -21.378 117.631  1.00 48.26           N  
-ATOM   6213  CA  PHE C 216      26.977 -21.442 117.870  1.00 50.41           C  
-ATOM   6214  C   PHE C 216      27.581 -22.827 117.617  1.00 51.81           C  
-ATOM   6215  O   PHE C 216      28.630 -22.938 116.991  1.00 51.83           O  
-ATOM   6216  CB  PHE C 216      27.317 -20.912 119.264  1.00 50.30           C  
-ATOM   6217  CG  PHE C 216      27.287 -19.407 119.359  1.00 50.66           C  
-ATOM   6218  CD1 PHE C 216      27.404 -18.618 118.221  1.00 51.48           C  
-ATOM   6219  CD2 PHE C 216      27.136 -18.777 120.581  1.00 50.65           C  
-ATOM   6220  CE1 PHE C 216      27.371 -17.231 118.305  1.00 51.99           C  
-ATOM   6221  CE2 PHE C 216      27.118 -17.389 120.676  1.00 51.62           C  
-ATOM   6222  CZ  PHE C 216      27.231 -16.616 119.537  1.00 51.79           C  
-ATOM   6223  N   ARG C 217      26.903 -23.878 118.071  1.00 53.95           N  
-ATOM   6224  CA  ARG C 217      27.369 -25.246 117.836  1.00 56.16           C  
-ATOM   6225  C   ARG C 217      27.354 -25.639 116.351  1.00 57.69           C  
-ATOM   6226  O   ARG C 217      28.024 -26.589 115.949  1.00 57.64           O  
-ATOM   6227  CB  ARG C 217      26.568 -26.253 118.676  1.00 56.02           C  
-ATOM   6228  CG  ARG C 217      25.150 -26.538 118.172  1.00 56.56           C  
-ATOM   6229  CD  ARG C 217      24.455 -27.743 118.808  1.00 57.97           C  
-ATOM   6230  NE  ARG C 217      25.348 -28.585 119.609  1.00 58.91           N  
-ATOM   6231  CZ  ARG C 217      25.921 -29.703 119.171  1.00 59.60           C  
-ATOM   6232  NH1 ARG C 217      25.701 -30.133 117.934  1.00 59.90           N  
-ATOM   6233  NH2 ARG C 217      26.716 -30.401 119.971  1.00 59.91           N  
-ATOM   6234  N   THR C 218      26.604 -24.889 115.548  1.00 59.98           N  
-ATOM   6235  CA  THR C 218      26.385 -25.219 114.143  1.00 62.19           C  
-ATOM   6236  C   THR C 218      27.285 -24.457 113.169  1.00 64.13           C  
-ATOM   6237  O   THR C 218      27.707 -25.019 112.156  1.00 64.28           O  
-ATOM   6238  CB  THR C 218      24.899 -25.011 113.779  1.00 61.94           C  
-ATOM   6239  OG1 THR C 218      24.077 -25.702 114.727  1.00 61.89           O  
-ATOM   6240  CG2 THR C 218      24.548 -25.698 112.463  1.00 61.89           C  
-ATOM   6241  N   LEU C 219      27.581 -23.193 113.472  1.00 66.67           N  
-ATOM   6242  CA  LEU C 219      28.254 -22.316 112.507  1.00 69.39           C  
-ATOM   6243  C   LEU C 219      29.598 -21.755 112.967  1.00 71.55           C  
-ATOM   6244  O   LEU C 219      30.306 -21.116 112.181  1.00 71.69           O  
-ATOM   6245  CB  LEU C 219      27.333 -21.159 112.084  1.00 69.10           C  
-ATOM   6246  CG  LEU C 219      25.829 -21.372 111.867  1.00 68.91           C  
-ATOM   6247  CD1 LEU C 219      25.161 -20.044 111.553  1.00 68.28           C  
-ATOM   6248  CD2 LEU C 219      25.540 -22.389 110.770  1.00 68.49           C  
-ATOM   6249  N   GLY C 220      29.946 -21.984 114.231  1.00 74.23           N  
-ATOM   6250  CA  GLY C 220      31.154 -21.413 114.796  1.00 77.77           C  
-ATOM   6251  C   GLY C 220      30.820 -20.446 115.909  1.00 80.33           C  
-ATOM   6252  O   GLY C 220      29.984 -20.745 116.756  1.00 80.51           O  
-ATOM   6253  N   THR C 221      31.489 -19.295 115.913  1.00 83.04           N  
-ATOM   6254  CA  THR C 221      31.173 -18.189 116.821  1.00 85.78           C  
-ATOM   6255  C   THR C 221      31.803 -16.898 116.301  1.00 87.82           C  
-ATOM   6256  O   THR C 221      32.984 -16.890 115.932  1.00 88.00           O  
-ATOM   6257  CB  THR C 221      31.635 -18.483 118.277  1.00 85.69           C  
-ATOM   6258  OG1 THR C 221      30.780 -19.477 118.860  1.00 85.93           O  
-ATOM   6259  CG2 THR C 221      31.395 -17.280 119.183  1.00 85.82           C  
-ATOM   6260  N   PRO C 222      31.017 -15.819 116.259  1.00 89.90           N  
-ATOM   6261  CA  PRO C 222      31.527 -14.501 115.871  1.00 91.54           C  
-ATOM   6262  C   PRO C 222      32.714 -14.061 116.728  1.00 93.26           C  
-ATOM   6263  O   PRO C 222      32.545 -13.610 117.867  1.00 93.38           O  
-ATOM   6264  CB  PRO C 222      30.323 -13.579 116.095  1.00 91.51           C  
-ATOM   6265  CG  PRO C 222      29.404 -14.348 116.985  1.00 90.83           C  
-ATOM   6266  CD  PRO C 222      29.576 -15.767 116.565  1.00 90.00           C  
-ATOM   6267  N   ASP C 223      33.911 -14.240 116.178  1.00 95.27           N  
-ATOM   6268  CA  ASP C 223      35.120 -13.665 116.750  1.00 97.27           C  
-ATOM   6269  C   ASP C 223      35.389 -12.328 116.055  1.00 98.49           C  
-ATOM   6270  O   ASP C 223      34.682 -11.969 115.108  1.00 98.68           O  
-ATOM   6271  CB  ASP C 223      36.305 -14.630 116.614  1.00 97.35           C  
-ATOM   6272  CG  ASP C 223      36.751 -14.815 115.179  1.00 97.89           C  
-ATOM   6273  OD1 ASP C 223      37.762 -14.182 114.793  1.00 98.05           O  
-ATOM   6274  OD2 ASP C 223      36.159 -15.572 114.371  1.00 98.51           O  
-ATOM   6275  N   GLU C 224      36.403 -11.601 116.519  1.00100.06           N  
-ATOM   6276  CA  GLU C 224      36.671 -10.244 116.032  1.00101.56           C  
-ATOM   6277  C   GLU C 224      37.076 -10.159 114.552  1.00102.34           C  
-ATOM   6278  O   GLU C 224      37.043  -9.073 113.966  1.00102.56           O  
-ATOM   6279  CB  GLU C 224      37.708  -9.536 116.917  1.00101.67           C  
-ATOM   6280  CG  GLU C 224      37.197  -9.131 118.297  1.00102.66           C  
-ATOM   6281  CD  GLU C 224      36.371  -7.854 118.285  1.00103.71           C  
-ATOM   6282  OE1 GLU C 224      36.938  -6.768 118.027  1.00104.14           O  
-ATOM   6283  OE2 GLU C 224      35.149  -7.934 118.543  1.00104.22           O  
-ATOM   6284  N   VAL C 225      37.450 -11.292 113.952  1.00103.31           N  
-ATOM   6285  CA  VAL C 225      37.783 -11.324 112.523  1.00104.18           C  
-ATOM   6286  C   VAL C 225      36.553 -11.532 111.630  1.00104.72           C  
-ATOM   6287  O   VAL C 225      36.387 -10.833 110.626  1.00104.85           O  
-ATOM   6288  CB  VAL C 225      38.954 -12.309 112.184  1.00104.19           C  
-ATOM   6289  CG1 VAL C 225      38.453 -13.726 111.880  1.00104.33           C  
-ATOM   6290  CG2 VAL C 225      39.785 -11.769 111.021  1.00104.41           C  
-ATOM   6291  N   VAL C 226      35.700 -12.485 112.008  1.00105.36           N  
-ATOM   6292  CA  VAL C 226      34.485 -12.795 111.252  1.00105.96           C  
-ATOM   6293  C   VAL C 226      33.350 -11.808 111.571  1.00106.29           C  
-ATOM   6294  O   VAL C 226      32.430 -11.628 110.767  1.00106.34           O  
-ATOM   6295  CB  VAL C 226      34.050 -14.285 111.436  1.00105.99           C  
-ATOM   6296  CG1 VAL C 226      33.306 -14.502 112.750  1.00106.08           C  
-ATOM   6297  CG2 VAL C 226      33.221 -14.766 110.247  1.00106.16           C  
-ATOM   6298  N   TRP C 227      33.431 -11.177 112.744  1.00106.71           N  
-ATOM   6299  CA  TRP C 227      32.516 -10.106 113.136  1.00107.08           C  
-ATOM   6300  C   TRP C 227      33.194  -9.133 114.111  1.00107.40           C  
-ATOM   6301  O   TRP C 227      33.349  -9.442 115.297  1.00107.41           O  
-ATOM   6302  CB  TRP C 227      31.219 -10.670 113.738  1.00107.03           C  
-ATOM   6303  CG  TRP C 227      30.135  -9.634 113.969  1.00106.96           C  
-ATOM   6304  CD1 TRP C 227      30.146  -8.321 113.573  1.00106.88           C  
-ATOM   6305  CD2 TRP C 227      28.888  -9.830 114.648  1.00106.97           C  
-ATOM   6306  NE1 TRP C 227      28.988  -7.695 113.964  1.00106.98           N  
-ATOM   6307  CE2 TRP C 227      28.196  -8.596 114.626  1.00107.03           C  
-ATOM   6308  CE3 TRP C 227      28.278 -10.927 115.277  1.00106.78           C  
-ATOM   6309  CZ2 TRP C 227      26.931  -8.430 115.206  1.00106.84           C  
-ATOM   6310  CZ3 TRP C 227      27.023 -10.760 115.854  1.00106.70           C  
-ATOM   6311  CH2 TRP C 227      26.364  -9.520 115.813  1.00106.63           C  
-ATOM   6312  N   PRO C 228      33.602  -7.967 113.606  1.00107.67           N  
-ATOM   6313  CA  PRO C 228      34.207  -6.924 114.445  1.00107.93           C  
-ATOM   6314  C   PRO C 228      33.213  -6.329 115.444  1.00108.16           C  
-ATOM   6315  O   PRO C 228      32.078  -6.015 115.073  1.00108.21           O  
-ATOM   6316  CB  PRO C 228      34.638  -5.860 113.425  1.00107.94           C  
-ATOM   6317  CG  PRO C 228      34.645  -6.564 112.108  1.00107.82           C  
-ATOM   6318  CD  PRO C 228      33.535  -7.559 112.192  1.00107.69           C  
-ATOM   6319  N   GLY C 229      33.642  -6.193 116.697  1.00108.40           N  
-ATOM   6320  CA  GLY C 229      32.820  -5.609 117.743  1.00108.69           C  
-ATOM   6321  C   GLY C 229      31.733  -6.533 118.261  1.00108.88           C  
-ATOM   6322  O   GLY C 229      30.544  -6.212 118.176  1.00108.90           O  
-ATOM   6323  N   VAL C 230      32.144  -7.681 118.796  1.00109.06           N  
-ATOM   6324  CA  VAL C 230      31.208  -8.642 119.386  1.00109.25           C  
-ATOM   6325  C   VAL C 230      31.152  -8.540 120.912  1.00109.43           C  
-ATOM   6326  O   VAL C 230      30.078  -8.679 121.509  1.00109.44           O  
-ATOM   6327  CB  VAL C 230      31.504 -10.107 118.955  1.00109.22           C  
-ATOM   6328  CG1 VAL C 230      31.051 -10.338 117.527  1.00109.15           C  
-ATOM   6329  CG2 VAL C 230      32.987 -10.460 119.121  1.00109.16           C  
-ATOM   6330  N   THR C 231      32.309  -8.284 121.525  1.00109.65           N  
-ATOM   6331  CA  THR C 231      32.433  -8.148 122.978  1.00109.89           C  
-ATOM   6332  C   THR C 231      31.535  -7.049 123.544  1.00110.06           C  
-ATOM   6333  O   THR C 231      30.899  -7.233 124.586  1.00110.08           O  
-ATOM   6334  CB  THR C 231      33.907  -7.890 123.390  1.00109.90           C  
-ATOM   6335  OG1 THR C 231      34.640  -7.345 122.283  1.00109.95           O  
-ATOM   6336  CG2 THR C 231      34.626  -9.200 123.682  1.00109.85           C  
-ATOM   6337  N   SER C 232      31.484  -5.916 122.845  1.00110.25           N  
-ATOM   6338  CA  SER C 232      30.698  -4.761 123.272  1.00110.45           C  
-ATOM   6339  C   SER C 232      29.222  -4.923 122.905  1.00110.56           C  
-ATOM   6340  O   SER C 232      28.731  -4.301 121.959  1.00110.56           O  
-ATOM   6341  CB  SER C 232      31.270  -3.467 122.678  1.00110.47           C  
-ATOM   6342  OG  SER C 232      32.683  -3.531 122.563  1.00110.60           O  
-ATOM   6343  N   MET C 233      28.528  -5.767 123.667  1.00110.75           N  
-ATOM   6344  CA  MET C 233      27.106  -6.044 123.465  1.00110.88           C  
-ATOM   6345  C   MET C 233      26.412  -6.302 124.807  1.00110.90           C  
-ATOM   6346  O   MET C 233      26.939  -7.043 125.643  1.00110.90           O  
-ATOM   6347  CB  MET C 233      26.920  -7.239 122.522  1.00110.92           C  
-ATOM   6348  CG  MET C 233      25.874  -7.038 121.425  1.00111.17           C  
-ATOM   6349  SD  MET C 233      26.000  -5.458 120.549  1.00111.75           S  
-ATOM   6350  CE  MET C 233      27.294  -5.836 119.342  1.00111.93           C  
-ATOM   6351  N   PRO C 234      25.240  -5.693 125.012  1.00110.95           N  
-ATOM   6352  CA  PRO C 234      24.521  -5.772 126.296  1.00110.98           C  
-ATOM   6353  C   PRO C 234      24.144  -7.183 126.765  1.00110.99           C  
-ATOM   6354  O   PRO C 234      23.879  -7.363 127.957  1.00110.98           O  
-ATOM   6355  CB  PRO C 234      23.250  -4.951 126.035  1.00110.98           C  
-ATOM   6356  CG  PRO C 234      23.600  -4.055 124.901  1.00110.98           C  
-ATOM   6357  CD  PRO C 234      24.514  -4.861 124.033  1.00110.97           C  
-ATOM   6358  N   ASP C 235      24.124  -8.155 125.854  1.00110.98           N  
-ATOM   6359  CA  ASP C 235      23.738  -9.526 126.195  1.00110.96           C  
-ATOM   6360  C   ASP C 235      24.849 -10.556 125.956  1.00110.96           C  
-ATOM   6361  O   ASP C 235      24.705 -11.728 126.321  1.00110.97           O  
-ATOM   6362  CB  ASP C 235      22.457  -9.922 125.453  1.00110.96           C  
-ATOM   6363  CG  ASP C 235      21.269  -9.058 125.840  1.00110.97           C  
-ATOM   6364  OD1 ASP C 235      20.804  -9.161 126.997  1.00110.94           O  
-ATOM   6365  OD2 ASP C 235      20.736  -8.245 125.055  1.00110.92           O  
-ATOM   6366  N   TYR C 236      25.946 -10.111 125.345  1.00110.93           N  
-ATOM   6367  CA  TYR C 236      27.140 -10.934 125.150  1.00110.92           C  
-ATOM   6368  C   TYR C 236      27.785 -11.220 126.509  1.00110.81           C  
-ATOM   6369  O   TYR C 236      28.137 -10.294 127.246  1.00110.82           O  
-ATOM   6370  CB  TYR C 236      28.114 -10.215 124.199  1.00110.99           C  
-ATOM   6371  CG  TYR C 236      29.514 -10.798 124.072  1.00111.25           C  
-ATOM   6372  CD1 TYR C 236      30.473 -10.602 125.074  1.00111.45           C  
-ATOM   6373  CD2 TYR C 236      29.892 -11.509 122.929  1.00111.36           C  
-ATOM   6374  CE1 TYR C 236      31.758 -11.124 124.955  1.00111.47           C  
-ATOM   6375  CE2 TYR C 236      31.181 -12.029 122.796  1.00111.36           C  
-ATOM   6376  CZ  TYR C 236      32.107 -11.832 123.814  1.00111.38           C  
-ATOM   6377  OH  TYR C 236      33.381 -12.339 123.700  1.00111.29           O  
-ATOM   6378  N   LYS C 237      27.921 -12.504 126.836  1.00110.67           N  
-ATOM   6379  CA  LYS C 237      28.496 -12.926 128.117  1.00110.50           C  
-ATOM   6380  C   LYS C 237      29.908 -13.497 127.934  1.00110.42           C  
-ATOM   6381  O   LYS C 237      30.124 -14.355 127.071  1.00110.42           O  
-ATOM   6382  CB  LYS C 237      27.579 -13.938 128.822  1.00110.43           C  
-ATOM   6383  CG  LYS C 237      26.155 -13.438 129.082  1.00110.27           C  
-ATOM   6384  CD  LYS C 237      26.071 -12.563 130.333  1.00110.06           C  
-ATOM   6385  CE  LYS C 237      24.774 -11.766 130.360  1.00109.95           C  
-ATOM   6386  NZ  LYS C 237      23.878 -12.204 131.470  1.00109.65           N  
-ATOM   6387  N   PRO C 238      30.862 -13.029 128.745  1.00110.31           N  
-ATOM   6388  CA  PRO C 238      32.282 -13.368 128.561  1.00110.21           C  
-ATOM   6389  C   PRO C 238      32.675 -14.765 129.069  1.00110.09           C  
-ATOM   6390  O   PRO C 238      33.792 -14.955 129.564  1.00110.12           O  
-ATOM   6391  CB  PRO C 238      33.000 -12.276 129.363  1.00110.19           C  
-ATOM   6392  CG  PRO C 238      32.045 -11.934 130.459  1.00110.29           C  
-ATOM   6393  CD  PRO C 238      30.658 -12.138 129.906  1.00110.31           C  
-ATOM   6394  N   SER C 239      31.768 -15.728 128.933  1.00109.91           N  
-ATOM   6395  CA  SER C 239      32.033 -17.108 129.327  1.00109.73           C  
-ATOM   6396  C   SER C 239      31.643 -18.058 128.198  1.00109.57           C  
-ATOM   6397  O   SER C 239      31.025 -19.102 128.440  1.00109.54           O  
-ATOM   6398  CB  SER C 239      31.264 -17.450 130.609  1.00109.75           C  
-ATOM   6399  OG  SER C 239      29.860 -17.334 130.412  1.00109.81           O  
-ATOM   6400  N   PHE C 240      32.009 -17.705 126.964  1.00109.34           N  
-ATOM   6401  CA  PHE C 240      31.483 -18.433 125.810  1.00109.09           C  
-ATOM   6402  C   PHE C 240      32.306 -18.619 124.513  1.00108.82           C  
-ATOM   6403  O   PHE C 240      32.604 -19.753 124.153  1.00108.85           O  
-ATOM   6404  CB  PHE C 240      30.069 -17.951 125.472  1.00109.17           C  
-ATOM   6405  CG  PHE C 240      29.270 -18.964 124.738  1.00109.29           C  
-ATOM   6406  CD1 PHE C 240      29.008 -20.194 125.312  1.00109.58           C  
-ATOM   6407  CD2 PHE C 240      28.809 -18.711 123.462  1.00109.55           C  
-ATOM   6408  CE1 PHE C 240      28.281 -21.145 124.635  1.00109.76           C  
-ATOM   6409  CE2 PHE C 240      28.078 -19.666 122.781  1.00109.74           C  
-ATOM   6410  CZ  PHE C 240      27.817 -20.881 123.362  1.00109.81           C  
-ATOM   6411  N   PRO C 241      32.662 -17.523 123.831  1.00108.53           N  
-ATOM   6412  CA  PRO C 241      32.977 -17.537 122.385  1.00108.28           C  
-ATOM   6413  C   PRO C 241      34.107 -18.447 121.837  1.00108.00           C  
-ATOM   6414  O   PRO C 241      34.764 -19.173 122.586  1.00107.97           O  
-ATOM   6415  CB  PRO C 241      33.302 -16.064 122.097  1.00108.30           C  
-ATOM   6416  CG  PRO C 241      32.587 -15.333 123.166  1.00108.37           C  
-ATOM   6417  CD  PRO C 241      32.803 -16.163 124.391  1.00108.48           C  
-ATOM   6418  N   LYS C 242      34.291 -18.368 120.510  1.00107.66           N  
-ATOM   6419  CA  LYS C 242      35.349 -19.032 119.711  1.00107.34           C  
-ATOM   6420  C   LYS C 242      34.953 -20.403 119.130  1.00107.25           C  
-ATOM   6421  O   LYS C 242      33.825 -20.580 118.669  1.00107.19           O  
-ATOM   6422  CB  LYS C 242      36.710 -19.087 120.440  1.00107.25           C  
-ATOM   6423  CG  LYS C 242      37.252 -17.745 120.964  1.00106.88           C  
-ATOM   6424  CD  LYS C 242      37.364 -16.672 119.884  1.00106.17           C  
-ATOM   6425  CE  LYS C 242      36.382 -15.525 120.128  1.00105.72           C  
-ATOM   6426  NZ  LYS C 242      36.592 -14.814 121.425  1.00105.34           N  
-ATOM   6427  N   TRP C 243      35.909 -21.336 119.117  1.00107.10           N  
-ATOM   6428  CA  TRP C 243      35.707 -22.772 118.824  1.00106.95           C  
-ATOM   6429  C   TRP C 243      34.753 -23.188 117.682  1.00106.93           C  
-ATOM   6430  O   TRP C 243      34.702 -22.545 116.628  1.00106.94           O  
-ATOM   6431  CB  TRP C 243      35.368 -23.546 120.114  1.00106.88           C  
-ATOM   6432  CG  TRP C 243      34.429 -22.837 121.067  1.00106.58           C  
-ATOM   6433  CD1 TRP C 243      34.728 -22.382 122.320  1.00106.33           C  
-ATOM   6434  CD2 TRP C 243      33.042 -22.519 120.850  1.00106.19           C  
-ATOM   6435  NE1 TRP C 243      33.622 -21.800 122.891  1.00106.18           N  
-ATOM   6436  CE2 TRP C 243      32.573 -21.870 122.011  1.00106.03           C  
-ATOM   6437  CE3 TRP C 243      32.145 -22.719 119.789  1.00105.94           C  
-ATOM   6438  CZ2 TRP C 243      31.256 -21.418 122.140  1.00105.84           C  
-ATOM   6439  CZ3 TRP C 243      30.842 -22.269 119.917  1.00105.83           C  
-ATOM   6440  CH2 TRP C 243      30.410 -21.626 121.085  1.00105.86           C  
-ATOM   6441  N   ALA C 244      34.026 -24.287 117.923  1.00106.85           N  
-ATOM   6442  CA  ALA C 244      33.100 -24.935 116.979  1.00106.72           C  
-ATOM   6443  C   ALA C 244      33.777 -25.791 115.896  1.00106.61           C  
-ATOM   6444  O   ALA C 244      34.964 -26.114 116.011  1.00106.57           O  
-ATOM   6445  CB  ALA C 244      32.097 -23.944 116.384  1.00106.72           C  
-ATOM   6446  N   ARG C 245      33.017 -26.151 114.855  1.00106.41           N  
-ATOM   6447  CA  ARG C 245      33.445 -27.156 113.877  1.00106.17           C  
-ATOM   6448  C   ARG C 245      32.601 -27.186 112.590  1.00105.81           C  
-ATOM   6449  O   ARG C 245      31.891 -26.225 112.273  1.00105.76           O  
-ATOM   6450  CB  ARG C 245      33.460 -28.553 114.536  1.00106.27           C  
-ATOM   6451  CG  ARG C 245      32.080 -29.222 114.789  1.00106.73           C  
-ATOM   6452  CD  ARG C 245      30.914 -28.279 115.122  1.00107.47           C  
-ATOM   6453  NE  ARG C 245      29.657 -28.714 114.511  1.00108.07           N  
-ATOM   6454  CZ  ARG C 245      28.978 -28.020 113.600  1.00108.45           C  
-ATOM   6455  NH1 ARG C 245      29.426 -26.843 113.176  1.00108.55           N  
-ATOM   6456  NH2 ARG C 245      27.845 -28.506 113.107  1.00108.54           N  
-ATOM   6457  N   GLN C 246      32.721 -28.309 111.870  1.00105.31           N  
-ATOM   6458  CA  GLN C 246      31.889 -28.692 110.721  1.00104.79           C  
-ATOM   6459  C   GLN C 246      31.611 -27.623 109.662  1.00104.21           C  
-ATOM   6460  O   GLN C 246      30.800 -26.710 109.867  1.00104.24           O  
-ATOM   6461  CB  GLN C 246      30.574 -29.341 111.184  1.00104.94           C  
-ATOM   6462  CG  GLN C 246      30.668 -30.842 111.463  1.00105.39           C  
-ATOM   6463  CD  GLN C 246      29.627 -31.321 112.465  1.00106.10           C  
-ATOM   6464  OE1 GLN C 246      28.431 -31.350 112.163  1.00106.48           O  
-ATOM   6465  NE2 GLN C 246      30.079 -31.702 113.655  1.00106.35           N  
-ATOM   6466  N   ASP C 247      32.291 -27.764 108.525  1.00103.35           N  
-ATOM   6467  CA  ASP C 247      31.988 -26.987 107.327  1.00102.47           C  
-ATOM   6468  C   ASP C 247      30.569 -27.308 106.857  1.00101.68           C  
-ATOM   6469  O   ASP C 247      30.040 -28.388 107.149  1.00101.63           O  
-ATOM   6470  CB  ASP C 247      32.995 -27.299 106.213  1.00102.62           C  
-ATOM   6471  CG  ASP C 247      33.448 -28.756 106.216  1.00102.88           C  
-ATOM   6472  OD1 ASP C 247      32.594 -29.656 106.041  1.00103.23           O  
-ATOM   6473  OD2 ASP C 247      34.638 -29.097 106.388  1.00103.18           O  
-ATOM   6474  N   PHE C 248      29.961 -26.363 106.141  1.00100.54           N  
-ATOM   6475  CA  PHE C 248      28.595 -26.514 105.644  1.00 99.39           C  
-ATOM   6476  C   PHE C 248      28.460 -27.753 104.758  1.00 98.40           C  
-ATOM   6477  O   PHE C 248      28.703 -27.703 103.547  1.00 98.36           O  
-ATOM   6478  CB  PHE C 248      28.149 -25.248 104.904  1.00 99.59           C  
-ATOM   6479  CG  PHE C 248      27.725 -24.132 105.818  1.00 99.81           C  
-ATOM   6480  CD1 PHE C 248      28.674 -23.347 106.468  1.00100.02           C  
-ATOM   6481  CD2 PHE C 248      26.376 -23.870 106.033  1.00100.05           C  
-ATOM   6482  CE1 PHE C 248      28.286 -22.316 107.316  1.00100.31           C  
-ATOM   6483  CE2 PHE C 248      25.977 -22.842 106.881  1.00100.28           C  
-ATOM   6484  CZ  PHE C 248      26.935 -22.062 107.521  1.00100.43           C  
-ATOM   6485  N   SER C 249      28.091 -28.864 105.398  1.00 96.99           N  
-ATOM   6486  CA  SER C 249      27.960 -30.172 104.758  1.00 95.48           C  
-ATOM   6487  C   SER C 249      27.180 -31.115 105.668  1.00 94.34           C  
-ATOM   6488  O   SER C 249      26.261 -31.806 105.223  1.00 94.32           O  
-ATOM   6489  CB  SER C 249      29.336 -30.769 104.437  1.00 95.58           C  
-ATOM   6490  OG  SER C 249      30.147 -30.841 105.597  1.00 95.56           O  
-ATOM   6491  N   LYS C 250      27.556 -31.134 106.945  1.00 92.73           N  
-ATOM   6492  CA  LYS C 250      26.866 -31.946 107.945  1.00 91.14           C  
-ATOM   6493  C   LYS C 250      25.639 -31.210 108.486  1.00 89.81           C  
-ATOM   6494  O   LYS C 250      24.699 -31.835 108.990  1.00 89.66           O  
-ATOM   6495  CB  LYS C 250      27.817 -32.339 109.084  1.00 91.28           C  
-ATOM   6496  CG  LYS C 250      29.160 -32.925 108.634  1.00 91.45           C  
-ATOM   6497  CD  LYS C 250      29.030 -34.366 108.141  1.00 91.93           C  
-ATOM   6498  CE  LYS C 250      30.199 -34.754 107.241  1.00 92.06           C  
-ATOM   6499  NZ  LYS C 250      29.785 -35.637 106.111  1.00 91.84           N  
-ATOM   6500  N   VAL C 251      25.667 -29.881 108.375  1.00 88.04           N  
-ATOM   6501  CA  VAL C 251      24.540 -29.019 108.730  1.00 86.25           C  
-ATOM   6502  C   VAL C 251      23.310 -29.418 107.915  1.00 84.80           C  
-ATOM   6503  O   VAL C 251      22.248 -29.711 108.474  1.00 84.65           O  
-ATOM   6504  CB  VAL C 251      24.864 -27.516 108.474  1.00 86.37           C  
-ATOM   6505  CG1 VAL C 251      23.699 -26.623 108.890  1.00 86.35           C  
-ATOM   6506  CG2 VAL C 251      26.146 -27.098 109.192  1.00 86.41           C  
-ATOM   6507  N   VAL C 252      23.473 -29.425 106.593  1.00 82.82           N  
-ATOM   6508  CA  VAL C 252      22.411 -29.800 105.666  1.00 80.87           C  
-ATOM   6509  C   VAL C 252      22.962 -30.818 104.655  1.00 79.36           C  
-ATOM   6510  O   VAL C 252      23.553 -30.437 103.639  1.00 79.16           O  
-ATOM   6511  CB  VAL C 252      21.804 -28.560 104.954  1.00 80.95           C  
-ATOM   6512  CG1 VAL C 252      20.646 -28.960 104.062  1.00 80.91           C  
-ATOM   6513  CG2 VAL C 252      21.335 -27.528 105.968  1.00 80.89           C  
-ATOM   6514  N   PRO C 253      22.786 -32.108 104.961  1.00 77.73           N  
-ATOM   6515  CA  PRO C 253      23.290 -33.206 104.117  1.00 76.32           C  
-ATOM   6516  C   PRO C 253      22.872 -33.183 102.630  1.00 74.59           C  
-ATOM   6517  O   PRO C 253      23.788 -33.111 101.807  1.00 74.56           O  
-ATOM   6518  CB  PRO C 253      22.767 -34.466 104.824  1.00 76.42           C  
-ATOM   6519  CG  PRO C 253      22.561 -34.048 106.233  1.00 77.07           C  
-ATOM   6520  CD  PRO C 253      22.115 -32.616 106.173  1.00 77.62           C  
-ATOM   6521  N   PRO C 254      21.578 -33.225 102.285  1.00 72.90           N  
-ATOM   6522  CA  PRO C 254      21.165 -33.393 100.882  1.00 71.55           C  
-ATOM   6523  C   PRO C 254      21.364 -32.156  99.998  1.00 70.17           C  
-ATOM   6524  O   PRO C 254      20.743 -32.066  98.936  1.00 70.20           O  
-ATOM   6525  CB  PRO C 254      19.667 -33.720 100.995  1.00 71.55           C  
-ATOM   6526  CG  PRO C 254      19.415 -33.951 102.450  1.00 72.03           C  
-ATOM   6527  CD  PRO C 254      20.406 -33.110 103.169  1.00 72.71           C  
-ATOM   6528  N   LEU C 255      22.221 -31.232 100.422  1.00 68.43           N  
-ATOM   6529  CA  LEU C 255      22.433 -29.988  99.694  1.00 66.81           C  
-ATOM   6530  C   LEU C 255      23.770 -29.983  98.968  1.00 65.80           C  
-ATOM   6531  O   LEU C 255      24.808 -30.281  99.561  1.00 65.71           O  
-ATOM   6532  CB  LEU C 255      22.331 -28.791 100.645  1.00 66.80           C  
-ATOM   6533  CG  LEU C 255      21.760 -27.465 100.129  1.00 66.38           C  
-ATOM   6534  CD1 LEU C 255      20.331 -27.611  99.623  1.00 65.67           C  
-ATOM   6535  CD2 LEU C 255      21.833 -26.405 101.222  1.00 65.90           C  
-ATOM   6536  N   ASP C 256      23.731 -29.639  97.681  1.00 64.45           N  
-ATOM   6537  CA  ASP C 256      24.926 -29.573  96.834  1.00 63.16           C  
-ATOM   6538  C   ASP C 256      25.913 -28.482  97.275  1.00 62.08           C  
-ATOM   6539  O   ASP C 256      25.664 -27.766  98.252  1.00 61.85           O  
-ATOM   6540  CB  ASP C 256      24.526 -29.376  95.363  1.00 63.42           C  
-ATOM   6541  CG  ASP C 256      23.549 -28.221  95.166  1.00 63.63           C  
-ATOM   6542  OD1 ASP C 256      22.339 -28.405  95.431  1.00 63.96           O  
-ATOM   6543  OD2 ASP C 256      23.901 -27.097  94.749  1.00 63.53           O  
-ATOM   6544  N   GLU C 257      27.028 -28.366  96.551  1.00 60.58           N  
-ATOM   6545  CA  GLU C 257      28.086 -27.406  96.881  1.00 59.13           C  
-ATOM   6546  C   GLU C 257      27.593 -25.963  96.821  1.00 57.80           C  
-ATOM   6547  O   GLU C 257      27.876 -25.167  97.722  1.00 57.67           O  
-ATOM   6548  CB  GLU C 257      29.301 -27.592  95.959  1.00 59.41           C  
-ATOM   6549  CG  GLU C 257      30.265 -26.408  95.937  1.00 60.17           C  
-ATOM   6550  CD  GLU C 257      31.502 -26.652  95.093  1.00 61.61           C  
-ATOM   6551  OE1 GLU C 257      31.367 -27.109  93.934  1.00 62.32           O  
-ATOM   6552  OE2 GLU C 257      32.616 -26.376  95.592  1.00 62.15           O  
-ATOM   6553  N   ASP C 258      26.860 -25.642  95.756  1.00 56.11           N  
-ATOM   6554  CA  ASP C 258      26.344 -24.296  95.534  1.00 54.54           C  
-ATOM   6555  C   ASP C 258      25.255 -23.945  96.546  1.00 53.28           C  
-ATOM   6556  O   ASP C 258      25.239 -22.837  97.085  1.00 52.75           O  
-ATOM   6557  CB  ASP C 258      25.813 -24.155  94.105  1.00 54.60           C  
-ATOM   6558  CG  ASP C 258      26.925 -24.118  93.063  1.00 54.83           C  
-ATOM   6559  OD1 ASP C 258      28.097 -23.859  93.427  1.00 53.93           O  
-ATOM   6560  OD2 ASP C 258      26.711 -24.332  91.849  1.00 55.23           O  
-ATOM   6561  N   GLY C 259      24.357 -24.899  96.790  1.00 51.94           N  
-ATOM   6562  CA  GLY C 259      23.319 -24.768  97.798  1.00 50.54           C  
-ATOM   6563  C   GLY C 259      23.881 -24.376  99.150  1.00 49.59           C  
-ATOM   6564  O   GLY C 259      23.430 -23.400  99.749  1.00 49.28           O  
-ATOM   6565  N   ARG C 260      24.876 -25.129  99.617  1.00 48.73           N  
-ATOM   6566  CA  ARG C 260      25.526 -24.849 100.897  1.00 48.07           C  
-ATOM   6567  C   ARG C 260      26.346 -23.569 100.872  1.00 46.96           C  
-ATOM   6568  O   ARG C 260      26.490 -22.912 101.899  1.00 47.08           O  
-ATOM   6569  CB  ARG C 260      26.379 -26.033 101.362  1.00 48.46           C  
-ATOM   6570  CG  ARG C 260      25.556 -27.147 102.010  1.00 50.35           C  
-ATOM   6571  CD  ARG C 260      26.188 -28.542 101.985  1.00 53.79           C  
-ATOM   6572  NE  ARG C 260      27.108 -28.745 100.865  1.00 56.70           N  
-ATOM   6573  CZ  ARG C 260      27.765 -29.875 100.621  1.00 58.70           C  
-ATOM   6574  NH1 ARG C 260      27.609 -30.930 101.414  1.00 60.06           N  
-ATOM   6575  NH2 ARG C 260      28.579 -29.955  99.575  1.00 59.64           N  
-ATOM   6576  N   SER C 261      26.869 -23.205  99.704  1.00 45.61           N  
-ATOM   6577  CA  SER C 261      27.554 -21.924  99.551  1.00 44.50           C  
-ATOM   6578  C   SER C 261      26.599 -20.743  99.784  1.00 43.48           C  
-ATOM   6579  O   SER C 261      26.911 -19.828 100.545  1.00 43.33           O  
-ATOM   6580  CB  SER C 261      28.223 -21.812  98.176  1.00 44.52           C  
-ATOM   6581  OG  SER C 261      28.603 -20.470  97.910  1.00 44.49           O  
-ATOM   6582  N   LEU C 262      25.444 -20.772  99.125  1.00 42.43           N  
-ATOM   6583  CA  LEU C 262      24.422 -19.742  99.307  1.00 41.57           C  
-ATOM   6584  C   LEU C 262      23.878 -19.725 100.741  1.00 41.13           C  
-ATOM   6585  O   LEU C 262      23.717 -18.659 101.335  1.00 40.96           O  
-ATOM   6586  CB  LEU C 262      23.281 -19.931  98.300  1.00 41.33           C  
-ATOM   6587  CG  LEU C 262      21.991 -19.135  98.547  1.00 40.98           C  
-ATOM   6588  CD1 LEU C 262      22.204 -17.634  98.334  1.00 39.34           C  
-ATOM   6589  CD2 LEU C 262      20.880 -19.659  97.666  1.00 40.24           C  
-ATOM   6590  N   LEU C 263      23.602 -20.910 101.287  1.00 40.79           N  
-ATOM   6591  CA  LEU C 263      23.126 -21.031 102.663  1.00 40.39           C  
-ATOM   6592  C   LEU C 263      24.107 -20.432 103.667  1.00 40.30           C  
-ATOM   6593  O   LEU C 263      23.696 -19.729 104.591  1.00 40.33           O  
-ATOM   6594  CB  LEU C 263      22.809 -22.493 103.019  1.00 40.24           C  
-ATOM   6595  CG  LEU C 263      22.329 -22.762 104.455  1.00 39.41           C  
-ATOM   6596  CD1 LEU C 263      21.054 -21.984 104.768  1.00 38.16           C  
-ATOM   6597  CD2 LEU C 263      22.125 -24.241 104.704  1.00 37.88           C  
-ATOM   6598  N   SER C 264      25.398 -20.692 103.473  1.00 40.45           N  
-ATOM   6599  CA  SER C 264      26.428 -20.193 104.384  1.00 40.83           C  
-ATOM   6600  C   SER C 264      26.543 -18.677 104.305  1.00 41.03           C  
-ATOM   6601  O   SER C 264      26.899 -18.017 105.287  1.00 40.90           O  
-ATOM   6602  CB  SER C 264      27.782 -20.840 104.091  1.00 40.83           C  
-ATOM   6603  OG  SER C 264      28.291 -20.405 102.845  1.00 41.65           O  
-ATOM   6604  N   GLN C 265      26.238 -18.140 103.126  1.00 41.25           N  
-ATOM   6605  CA  GLN C 265      26.228 -16.700 102.899  1.00 41.78           C  
-ATOM   6606  C   GLN C 265      25.000 -16.056 103.544  1.00 41.68           C  
-ATOM   6607  O   GLN C 265      25.097 -14.989 104.151  1.00 41.55           O  
-ATOM   6608  CB  GLN C 265      26.287 -16.402 101.396  1.00 41.87           C  
-ATOM   6609  CG  GLN C 265      27.667 -16.649 100.780  1.00 42.88           C  
-ATOM   6610  CD  GLN C 265      27.690 -16.448  99.271  1.00 44.06           C  
-ATOM   6611  OE1 GLN C 265      27.458 -17.387  98.513  1.00 45.43           O  
-ATOM   6612  NE2 GLN C 265      27.978 -15.228  98.838  1.00 44.08           N  
-ATOM   6613  N   MET C 266      23.855 -16.727 103.422  1.00 41.95           N  
-ATOM   6614  CA  MET C 266      22.604 -16.275 104.036  1.00 41.89           C  
-ATOM   6615  C   MET C 266      22.655 -16.379 105.556  1.00 42.27           C  
-ATOM   6616  O   MET C 266      21.931 -15.667 106.246  1.00 42.14           O  
-ATOM   6617  CB  MET C 266      21.410 -17.080 103.513  1.00 41.56           C  
-ATOM   6618  CG  MET C 266      20.990 -16.750 102.102  1.00 39.59           C  
-ATOM   6619  SD  MET C 266      19.793 -17.949 101.522  1.00 37.25           S  
-ATOM   6620  CE  MET C 266      18.262 -17.122 101.900  1.00 36.86           C  
-ATOM   6621  N   LEU C 267      23.510 -17.261 106.069  1.00 42.97           N  
-ATOM   6622  CA  LEU C 267      23.645 -17.446 107.511  1.00 43.91           C  
-ATOM   6623  C   LEU C 267      24.983 -16.963 108.056  1.00 44.77           C  
-ATOM   6624  O   LEU C 267      25.519 -17.541 109.008  1.00 44.79           O  
-ATOM   6625  CB  LEU C 267      23.426 -18.913 107.894  1.00 43.85           C  
-ATOM   6626  CG  LEU C 267      22.041 -19.537 107.713  1.00 43.71           C  
-ATOM   6627  CD1 LEU C 267      22.046 -20.937 108.306  1.00 42.86           C  
-ATOM   6628  CD2 LEU C 267      20.934 -18.680 108.335  1.00 43.30           C  
-ATOM   6629  N   HIS C 268      25.515 -15.899 107.458  1.00 45.78           N  
-ATOM   6630  CA  HIS C 268      26.736 -15.271 107.951  1.00 46.77           C  
-ATOM   6631  C   HIS C 268      26.462 -14.626 109.301  1.00 47.38           C  
-ATOM   6632  O   HIS C 268      25.413 -14.012 109.495  1.00 47.33           O  
-ATOM   6633  CB  HIS C 268      27.230 -14.214 106.961  1.00 46.95           C  
-ATOM   6634  CG  HIS C 268      28.695 -13.921 107.061  1.00 47.70           C  
-ATOM   6635  ND1 HIS C 268      29.556 -14.066 105.992  1.00 49.05           N  
-ATOM   6636  CD2 HIS C 268      29.451 -13.478 108.094  1.00 48.16           C  
-ATOM   6637  CE1 HIS C 268      30.779 -13.735 106.367  1.00 49.22           C  
-ATOM   6638  NE2 HIS C 268      30.743 -13.373 107.638  1.00 48.99           N  
-ATOM   6639  N   TYR C 269      27.402 -14.778 110.230  1.00 48.17           N  
-ATOM   6640  CA  TYR C 269      27.313 -14.137 111.536  1.00 49.18           C  
-ATOM   6641  C   TYR C 269      27.257 -12.617 111.424  1.00 49.19           C  
-ATOM   6642  O   TYR C 269      26.428 -11.974 112.069  1.00 49.39           O  
-ATOM   6643  CB  TYR C 269      28.490 -14.549 112.422  1.00 49.60           C  
-ATOM   6644  CG  TYR C 269      28.291 -15.861 113.148  1.00 51.83           C  
-ATOM   6645  CD1 TYR C 269      27.108 -16.131 113.834  1.00 53.77           C  
-ATOM   6646  CD2 TYR C 269      29.290 -16.832 113.155  1.00 53.79           C  
-ATOM   6647  CE1 TYR C 269      26.924 -17.333 114.504  1.00 55.37           C  
-ATOM   6648  CE2 TYR C 269      29.115 -18.039 113.825  1.00 55.26           C  
-ATOM   6649  CZ  TYR C 269      27.931 -18.282 114.498  1.00 55.73           C  
-ATOM   6650  OH  TYR C 269      27.748 -19.473 115.164  1.00 56.36           O  
-ATOM   6651  N   ASP C 270      28.138 -12.053 110.605  1.00 49.21           N  
-ATOM   6652  CA  ASP C 270      28.197 -10.611 110.418  1.00 49.27           C  
-ATOM   6653  C   ASP C 270      27.047 -10.117 109.542  1.00 49.08           C  
-ATOM   6654  O   ASP C 270      26.913 -10.548 108.392  1.00 48.97           O  
-ATOM   6655  CB  ASP C 270      29.535 -10.194 109.808  1.00 49.42           C  
-ATOM   6656  CG  ASP C 270      29.821  -8.717 109.995  1.00 50.03           C  
-ATOM   6657  OD1 ASP C 270      28.987  -7.878 109.578  1.00 50.04           O  
-ATOM   6658  OD2 ASP C 270      30.855  -8.303 110.555  1.00 51.02           O  
-ATOM   6659  N   PRO C 271      26.219  -9.222 110.088  1.00 48.86           N  
-ATOM   6660  CA  PRO C 271      25.090  -8.646 109.339  1.00 48.71           C  
-ATOM   6661  C   PRO C 271      25.529  -7.941 108.049  1.00 48.56           C  
-ATOM   6662  O   PRO C 271      24.860  -8.087 107.023  1.00 48.33           O  
-ATOM   6663  CB  PRO C 271      24.478  -7.646 110.329  1.00 48.81           C  
-ATOM   6664  CG  PRO C 271      24.932  -8.107 111.681  1.00 48.83           C  
-ATOM   6665  CD  PRO C 271      26.287  -8.713 111.471  1.00 48.68           C  
-ATOM   6666  N   ASN C 272      26.642  -7.212 108.104  1.00 48.46           N  
-ATOM   6667  CA  ASN C 272      27.181  -6.515 106.932  1.00 48.50           C  
-ATOM   6668  C   ASN C 272      27.675  -7.463 105.836  1.00 48.02           C  
-ATOM   6669  O   ASN C 272      27.487  -7.201 104.649  1.00 48.06           O  
-ATOM   6670  CB  ASN C 272      28.297  -5.542 107.337  1.00 48.52           C  
-ATOM   6671  CG  ASN C 272      27.870  -4.585 108.439  1.00 49.64           C  
-ATOM   6672  OD1 ASN C 272      26.971  -3.759 108.246  1.00 50.59           O  
-ATOM   6673  ND2 ASN C 272      28.516  -4.690 109.603  1.00 49.93           N  
-ATOM   6674  N   LYS C 273      28.304  -8.560 106.243  1.00 47.80           N  
-ATOM   6675  CA  LYS C 273      28.807  -9.563 105.303  1.00 47.52           C  
-ATOM   6676  C   LYS C 273      27.704 -10.509 104.806  1.00 46.84           C  
-ATOM   6677  O   LYS C 273      27.853 -11.141 103.756  1.00 46.84           O  
-ATOM   6678  CB  LYS C 273      29.954 -10.367 105.929  1.00 47.92           C  
-ATOM   6679  CG  LYS C 273      31.195  -9.551 106.303  1.00 49.48           C  
-ATOM   6680  CD  LYS C 273      32.141  -9.381 105.114  1.00 52.71           C  
-ATOM   6681  CE  LYS C 273      33.255  -8.378 105.419  1.00 54.39           C  
-ATOM   6682  NZ  LYS C 273      32.764  -6.956 105.430  1.00 56.42           N  
-ATOM   6683  N   ARG C 274      26.609 -10.604 105.561  1.00 45.66           N  
-ATOM   6684  CA  ARG C 274      25.476 -11.448 105.185  1.00 44.68           C  
-ATOM   6685  C   ARG C 274      24.940 -11.019 103.822  1.00 44.25           C  
-ATOM   6686  O   ARG C 274      24.763  -9.823 103.567  1.00 44.24           O  
-ATOM   6687  CB  ARG C 274      24.375 -11.384 106.252  1.00 44.44           C  
-ATOM   6688  CG  ARG C 274      23.408 -12.570 106.248  1.00 43.27           C  
-ATOM   6689  CD  ARG C 274      22.446 -12.597 107.436  1.00 40.79           C  
-ATOM   6690  NE  ARG C 274      23.178 -12.660 108.698  1.00 38.27           N  
-ATOM   6691  CZ  ARG C 274      22.830 -12.032 109.808  1.00 37.48           C  
-ATOM   6692  NH1 ARG C 274      21.733 -11.283 109.850  1.00 38.18           N  
-ATOM   6693  NH2 ARG C 274      23.585 -12.154 110.887  1.00 37.25           N  
-ATOM   6694  N   ILE C 275      24.699 -11.992 102.949  1.00 43.57           N  
-ATOM   6695  CA  ILE C 275      24.291 -11.702 101.576  1.00 42.95           C  
-ATOM   6696  C   ILE C 275      22.935 -10.993 101.515  1.00 42.77           C  
-ATOM   6697  O   ILE C 275      22.044 -11.261 102.331  1.00 42.48           O  
-ATOM   6698  CB  ILE C 275      24.313 -12.987 100.699  1.00 43.00           C  
-ATOM   6699  CG1 ILE C 275      24.215 -12.635  99.212  1.00 43.24           C  
-ATOM   6700  CG2 ILE C 275      23.199 -13.947 101.079  1.00 43.15           C  
-ATOM   6701  CD1 ILE C 275      25.323 -13.225  98.376  1.00 43.68           C  
-ATOM   6702  N   SER C 276      22.806 -10.069 100.562  1.00 42.26           N  
-ATOM   6703  CA  SER C 276      21.539  -9.404 100.291  1.00 41.89           C  
-ATOM   6704  C   SER C 276      20.689 -10.328  99.445  1.00 41.61           C  
-ATOM   6705  O   SER C 276      21.220 -11.206  98.758  1.00 41.49           O  
-ATOM   6706  CB  SER C 276      21.755  -8.077  99.554  1.00 41.91           C  
-ATOM   6707  OG  SER C 276      21.991  -8.291  98.170  1.00 41.63           O  
-ATOM   6708  N   ALA C 277      19.376 -10.124  99.502  1.00 41.21           N  
-ATOM   6709  CA  ALA C 277      18.428 -10.873  98.684  1.00 41.21           C  
-ATOM   6710  C   ALA C 277      18.712 -10.638  97.213  1.00 41.32           C  
-ATOM   6711  O   ALA C 277      18.600 -11.550  96.396  1.00 41.21           O  
-ATOM   6712  CB  ALA C 277      17.015 -10.452  99.008  1.00 41.02           C  
-ATOM   6713  N   LYS C 278      19.073  -9.396  96.902  1.00 41.57           N  
-ATOM   6714  CA  LYS C 278      19.385  -8.960  95.551  1.00 42.04           C  
-ATOM   6715  C   LYS C 278      20.592  -9.712  95.003  1.00 41.82           C  
-ATOM   6716  O   LYS C 278      20.531 -10.270  93.910  1.00 41.58           O  
-ATOM   6717  CB  LYS C 278      19.641  -7.452  95.559  1.00 42.26           C  
-ATOM   6718  CG  LYS C 278      19.893  -6.831  94.205  1.00 43.33           C  
-ATOM   6719  CD  LYS C 278      20.599  -5.495  94.359  1.00 44.59           C  
-ATOM   6720  CE  LYS C 278      19.631  -4.393  94.751  1.00 46.28           C  
-ATOM   6721  NZ  LYS C 278      18.577  -4.181  93.716  1.00 47.31           N  
-ATOM   6722  N   ALA C 279      21.678  -9.735  95.774  1.00 41.99           N  
-ATOM   6723  CA  ALA C 279      22.888 -10.446  95.373  1.00 42.11           C  
-ATOM   6724  C   ALA C 279      22.645 -11.949  95.300  1.00 42.27           C  
-ATOM   6725  O   ALA C 279      23.128 -12.618  94.384  1.00 42.45           O  
-ATOM   6726  CB  ALA C 279      24.031 -10.136  96.320  1.00 42.37           C  
-ATOM   6727  N   ALA C 280      21.871 -12.467  96.250  1.00 42.20           N  
-ATOM   6728  CA  ALA C 280      21.571 -13.891  96.313  1.00 42.32           C  
-ATOM   6729  C   ALA C 280      20.817 -14.397  95.085  1.00 42.46           C  
-ATOM   6730  O   ALA C 280      20.927 -15.572  94.741  1.00 42.40           O  
-ATOM   6731  CB  ALA C 280      20.805 -14.225  97.593  1.00 42.26           C  
-ATOM   6732  N   LEU C 281      20.061 -13.519  94.428  1.00 42.68           N  
-ATOM   6733  CA  LEU C 281      19.318 -13.894  93.216  1.00 43.19           C  
-ATOM   6734  C   LEU C 281      20.234 -14.188  92.020  1.00 43.58           C  
-ATOM   6735  O   LEU C 281      19.818 -14.821  91.054  1.00 43.79           O  
-ATOM   6736  CB  LEU C 281      18.300 -12.815  92.837  1.00 43.01           C  
-ATOM   6737  CG  LEU C 281      17.008 -12.695  93.658  1.00 42.80           C  
-ATOM   6738  CD1 LEU C 281      16.304 -11.368  93.372  1.00 41.74           C  
-ATOM   6739  CD2 LEU C 281      16.077 -13.868  93.408  1.00 42.17           C  
-ATOM   6740  N   ALA C 282      21.477 -13.727  92.097  1.00 44.10           N  
-ATOM   6741  CA  ALA C 282      22.459 -13.948  91.041  1.00 44.51           C  
-ATOM   6742  C   ALA C 282      23.403 -15.115  91.361  1.00 44.82           C  
-ATOM   6743  O   ALA C 282      24.399 -15.323  90.664  1.00 45.17           O  
-ATOM   6744  CB  ALA C 282      23.252 -12.672  90.796  1.00 44.26           C  
-ATOM   6745  N   HIS C 283      23.083 -15.875  92.406  1.00 44.93           N  
-ATOM   6746  CA  HIS C 283      23.938 -16.974  92.857  1.00 45.09           C  
-ATOM   6747  C   HIS C 283      23.931 -18.170  91.885  1.00 45.63           C  
-ATOM   6748  O   HIS C 283      22.876 -18.519  91.341  1.00 45.61           O  
-ATOM   6749  CB  HIS C 283      23.535 -17.414  94.274  1.00 44.71           C  
-ATOM   6750  CG  HIS C 283      24.561 -18.258  94.960  1.00 43.55           C  
-ATOM   6751  ND1 HIS C 283      24.692 -19.608  94.720  1.00 42.30           N  
-ATOM   6752  CD2 HIS C 283      25.517 -17.944  95.867  1.00 42.75           C  
-ATOM   6753  CE1 HIS C 283      25.683 -20.089  95.448  1.00 42.17           C  
-ATOM   6754  NE2 HIS C 283      26.198 -19.101  96.156  1.00 41.85           N  
-ATOM   6755  N   PRO C 284      25.108 -18.773  91.656  1.00 46.13           N  
-ATOM   6756  CA  PRO C 284      25.240 -20.016  90.870  1.00 46.61           C  
-ATOM   6757  C   PRO C 284      24.166 -21.067  91.136  1.00 47.11           C  
-ATOM   6758  O   PRO C 284      23.791 -21.786  90.211  1.00 47.47           O  
-ATOM   6759  CB  PRO C 284      26.600 -20.578  91.311  1.00 46.42           C  
-ATOM   6760  CG  PRO C 284      27.375 -19.416  91.865  1.00 46.42           C  
-ATOM   6761  CD  PRO C 284      26.423 -18.268  92.096  1.00 46.27           C  
-ATOM   6762  N   PHE C 285      23.697 -21.156  92.378  1.00 47.63           N  
-ATOM   6763  CA  PHE C 285      22.659 -22.104  92.771  1.00 48.13           C  
-ATOM   6764  C   PHE C 285      21.393 -21.950  91.933  1.00 48.49           C  
-ATOM   6765  O   PHE C 285      20.714 -22.931  91.652  1.00 48.28           O  
-ATOM   6766  CB  PHE C 285      22.336 -21.929  94.263  1.00 48.19           C  
-ATOM   6767  CG  PHE C 285      21.259 -22.855  94.780  1.00 48.26           C  
-ATOM   6768  CD1 PHE C 285      21.507 -24.218  94.941  1.00 48.18           C  
-ATOM   6769  CD2 PHE C 285      20.003 -22.358  95.118  1.00 47.75           C  
-ATOM   6770  CE1 PHE C 285      20.517 -25.077  95.428  1.00 48.33           C  
-ATOM   6771  CE2 PHE C 285      19.006 -23.202  95.602  1.00 48.25           C  
-ATOM   6772  CZ  PHE C 285      19.264 -24.567  95.763  1.00 48.65           C  
-ATOM   6773  N   PHE C 286      21.089 -20.717  91.534  1.00 49.32           N  
-ATOM   6774  CA  PHE C 286      19.842 -20.420  90.831  1.00 50.27           C  
-ATOM   6775  C   PHE C 286      19.945 -20.478  89.306  1.00 51.34           C  
-ATOM   6776  O   PHE C 286      18.950 -20.262  88.610  1.00 51.39           O  
-ATOM   6777  CB  PHE C 286      19.282 -19.067  91.284  1.00 49.96           C  
-ATOM   6778  CG  PHE C 286      18.844 -19.048  92.721  1.00 48.89           C  
-ATOM   6779  CD1 PHE C 286      17.796 -19.854  93.153  1.00 47.97           C  
-ATOM   6780  CD2 PHE C 286      19.487 -18.236  93.643  1.00 48.07           C  
-ATOM   6781  CE1 PHE C 286      17.393 -19.851  94.484  1.00 47.28           C  
-ATOM   6782  CE2 PHE C 286      19.087 -18.221  94.978  1.00 47.83           C  
-ATOM   6783  CZ  PHE C 286      18.039 -19.033  95.396  1.00 47.43           C  
-ATOM   6784  N   GLN C 287      21.133 -20.798  88.793  1.00 52.74           N  
-ATOM   6785  CA  GLN C 287      21.386 -20.751  87.349  1.00 54.14           C  
-ATOM   6786  C   GLN C 287      20.427 -21.603  86.510  1.00 54.46           C  
-ATOM   6787  O   GLN C 287      20.079 -21.223  85.390  1.00 54.62           O  
-ATOM   6788  CB  GLN C 287      22.866 -21.022  87.017  1.00 54.40           C  
-ATOM   6789  CG  GLN C 287      23.327 -22.469  87.125  1.00 56.63           C  
-ATOM   6790  CD  GLN C 287      24.829 -22.623  86.894  1.00 59.94           C  
-ATOM   6791  OE1 GLN C 287      25.315 -22.445  85.771  1.00 61.34           O  
-ATOM   6792  NE2 GLN C 287      25.565 -22.959  87.954  1.00 60.60           N  
-ATOM   6793  N   ASP C 288      19.980 -22.725  87.077  1.00 55.04           N  
-ATOM   6794  CA  ASP C 288      19.086 -23.665  86.391  1.00 55.44           C  
-ATOM   6795  C   ASP C 288      17.651 -23.705  86.945  1.00 55.37           C  
-ATOM   6796  O   ASP C 288      16.943 -24.705  86.761  1.00 55.35           O  
-ATOM   6797  CB  ASP C 288      19.690 -25.079  86.415  1.00 55.71           C  
-ATOM   6798  CG  ASP C 288      19.865 -25.628  87.834  1.00 57.11           C  
-ATOM   6799  OD1 ASP C 288      18.850 -25.958  88.488  1.00 57.80           O  
-ATOM   6800  OD2 ASP C 288      20.986 -25.778  88.374  1.00 58.98           O  
-ATOM   6801  N   VAL C 289      17.219 -22.633  87.609  1.00 55.24           N  
-ATOM   6802  CA  VAL C 289      15.909 -22.629  88.279  1.00 55.09           C  
-ATOM   6803  C   VAL C 289      14.726 -22.749  87.312  1.00 55.06           C  
-ATOM   6804  O   VAL C 289      14.719 -22.142  86.242  1.00 55.30           O  
-ATOM   6805  CB  VAL C 289      15.737 -21.411  89.253  1.00 55.19           C  
-ATOM   6806  CG1 VAL C 289      15.670 -20.081  88.500  1.00 54.95           C  
-ATOM   6807  CG2 VAL C 289      14.515 -21.593  90.159  1.00 54.77           C  
-ATOM   6808  N   THR C 290      13.752 -23.570  87.695  1.00 55.06           N  
-ATOM   6809  CA  THR C 290      12.480 -23.706  86.980  1.00 55.17           C  
-ATOM   6810  C   THR C 290      11.339 -23.389  87.948  1.00 55.17           C  
-ATOM   6811  O   THR C 290      11.586 -22.999  89.089  1.00 54.94           O  
-ATOM   6812  CB  THR C 290      12.305 -25.141  86.409  1.00 55.16           C  
-ATOM   6813  OG1 THR C 290      12.415 -26.104  87.468  1.00 55.05           O  
-ATOM   6814  CG2 THR C 290      13.449 -25.511  85.470  1.00 55.27           C  
-ATOM   6815  N   LYS C 291      10.097 -23.564  87.500  1.00 55.45           N  
-ATOM   6816  CA  LYS C 291       8.934 -23.391  88.370  1.00 55.86           C  
-ATOM   6817  C   LYS C 291       8.052 -24.644  88.407  1.00 56.47           C  
-ATOM   6818  O   LYS C 291       7.004 -24.692  87.751  1.00 56.58           O  
-ATOM   6819  CB  LYS C 291       8.118 -22.156  87.963  1.00 55.82           C  
-ATOM   6820  CG  LYS C 291       7.199 -21.622  89.061  1.00 55.22           C  
-ATOM   6821  CD  LYS C 291       6.479 -20.366  88.624  1.00 54.37           C  
-ATOM   6822  CE  LYS C 291       5.429 -19.954  89.637  1.00 54.41           C  
-ATOM   6823  NZ  LYS C 291       4.051 -20.308  89.182  1.00 54.91           N  
-ATOM   6824  N   PRO C 292       8.474 -25.652  89.175  1.00 57.06           N  
-ATOM   6825  CA  PRO C 292       7.707 -26.895  89.316  1.00 57.67           C  
-ATOM   6826  C   PRO C 292       6.415 -26.705  90.095  1.00 58.43           C  
-ATOM   6827  O   PRO C 292       6.317 -25.812  90.939  1.00 58.34           O  
-ATOM   6828  CB  PRO C 292       8.645 -27.805  90.118  1.00 57.53           C  
-ATOM   6829  CG  PRO C 292       9.971 -27.143  90.095  1.00 57.37           C  
-ATOM   6830  CD  PRO C 292       9.715 -25.688  89.968  1.00 57.05           C  
-ATOM   6831  N   VAL C 293       5.438 -27.551  89.793  1.00 59.51           N  
-ATOM   6832  CA  VAL C 293       4.196 -27.639  90.548  1.00 60.75           C  
-ATOM   6833  C   VAL C 293       4.422 -28.619  91.709  1.00 61.62           C  
-ATOM   6834  O   VAL C 293       5.036 -29.669  91.513  1.00 61.64           O  
-ATOM   6835  CB  VAL C 293       3.040 -28.119  89.629  1.00 60.67           C  
-ATOM   6836  CG1 VAL C 293       1.822 -28.557  90.428  1.00 61.02           C  
-ATOM   6837  CG2 VAL C 293       2.656 -27.025  88.641  1.00 60.87           C  
-ATOM   6838  N   PRO C 294       3.957 -28.280  92.913  1.00 62.60           N  
-ATOM   6839  CA  PRO C 294       4.101 -29.181  94.065  1.00 63.49           C  
-ATOM   6840  C   PRO C 294       3.172 -30.385  93.959  1.00 64.44           C  
-ATOM   6841  O   PRO C 294       2.189 -30.325  93.215  1.00 64.57           O  
-ATOM   6842  CB  PRO C 294       3.687 -28.304  95.250  1.00 63.39           C  
-ATOM   6843  CG  PRO C 294       2.765 -27.281  94.661  1.00 63.15           C  
-ATOM   6844  CD  PRO C 294       3.270 -27.024  93.274  1.00 62.53           C  
-ATOM   6845  N   HIS C 295       3.481 -31.460  94.682  1.00 65.66           N  
-ATOM   6846  CA  HIS C 295       2.548 -32.578  94.796  1.00 66.78           C  
-ATOM   6847  C   HIS C 295       1.605 -32.347  95.973  1.00 67.07           C  
-ATOM   6848  O   HIS C 295       1.827 -32.854  97.078  1.00 67.10           O  
-ATOM   6849  CB  HIS C 295       3.272 -33.924  94.912  1.00 67.08           C  
-ATOM   6850  CG  HIS C 295       2.365 -35.108  94.761  1.00 68.83           C  
-ATOM   6851  ND1 HIS C 295       1.598 -35.320  93.633  1.00 70.51           N  
-ATOM   6852  CD2 HIS C 295       2.092 -36.136  95.600  1.00 69.99           C  
-ATOM   6853  CE1 HIS C 295       0.898 -36.431  93.782  1.00 70.96           C  
-ATOM   6854  NE2 HIS C 295       1.178 -36.945  94.967  1.00 70.81           N  
-ATOM   6855  N   LEU C 296       0.561 -31.559  95.720  1.00 67.51           N  
-ATOM   6856  CA  LEU C 296      -0.429 -31.210  96.734  1.00 67.92           C  
-ATOM   6857  C   LEU C 296      -1.655 -32.110  96.655  1.00 68.00           C  
-ATOM   6858  O   LEU C 296      -2.321 -32.364  97.663  1.00 68.04           O  
-ATOM   6859  CB  LEU C 296      -0.853 -29.743  96.597  1.00 68.07           C  
-ATOM   6860  CG  LEU C 296      -0.078 -28.682  97.392  1.00 68.60           C  
-ATOM   6861  CD1 LEU C 296      -0.564 -27.280  97.046  1.00 68.71           C  
-ATOM   6862  CD2 LEU C 296      -0.172 -28.923  98.894  1.00 69.05           C  
-TER    6863      LEU C 296                                                      
-ATOM   6864  N   VAL D 175      23.016  -0.165 104.790  1.00 60.53           N  
-ATOM   6865  CA  VAL D 175      22.411  -1.140 103.830  1.00 60.59           C  
-ATOM   6866  C   VAL D 175      22.704  -0.738 102.360  1.00 60.37           C  
-ATOM   6867  O   VAL D 175      21.796  -0.390 101.594  1.00 60.29           O  
-ATOM   6868  CB  VAL D 175      20.886  -1.376 104.144  1.00 60.72           C  
-ATOM   6869  CG1 VAL D 175      20.053  -0.095 103.976  1.00 60.79           C  
-ATOM   6870  CG2 VAL D 175      20.318  -2.529 103.324  1.00 61.17           C  
-ATOM   6871  N   PRO D 176      23.984  -0.798 101.973  1.00 60.19           N  
-ATOM   6872  CA  PRO D 176      24.451  -0.231 100.695  1.00 59.78           C  
-ATOM   6873  C   PRO D 176      23.790  -0.830  99.455  1.00 59.26           C  
-ATOM   6874  O   PRO D 176      23.517  -0.106  98.493  1.00 59.28           O  
-ATOM   6875  CB  PRO D 176      25.949  -0.546 100.701  1.00 59.89           C  
-ATOM   6876  CG  PRO D 176      26.283  -0.754 102.126  1.00 60.30           C  
-ATOM   6877  CD  PRO D 176      25.088  -1.433 102.718  1.00 60.17           C  
-ATOM   6878  N   ASP D 177      23.525  -2.133  99.495  1.00 58.45           N  
-ATOM   6879  CA  ASP D 177      22.934  -2.855  98.373  1.00 57.63           C  
-ATOM   6880  C   ASP D 177      21.573  -2.309  97.901  1.00 56.64           C  
-ATOM   6881  O   ASP D 177      21.106  -2.681  96.824  1.00 56.62           O  
-ATOM   6882  CB  ASP D 177      22.823  -4.346  98.714  1.00 58.06           C  
-ATOM   6883  CG  ASP D 177      24.184  -5.030  98.808  1.00 59.32           C  
-ATOM   6884  OD1 ASP D 177      24.944  -4.737  99.758  1.00 60.88           O  
-ATOM   6885  OD2 ASP D 177      24.579  -5.881  97.982  1.00 60.53           O  
-ATOM   6886  N   TYR D 178      20.950  -1.430  98.692  1.00 55.25           N  
-ATOM   6887  CA  TYR D 178      19.619  -0.895  98.367  1.00 53.94           C  
-ATOM   6888  C   TYR D 178      19.508   0.635  98.377  1.00 53.60           C  
-ATOM   6889  O   TYR D 178      18.435   1.180  98.096  1.00 53.57           O  
-ATOM   6890  CB  TYR D 178      18.553  -1.503  99.293  1.00 53.41           C  
-ATOM   6891  CG  TYR D 178      18.451  -3.004  99.197  1.00 51.22           C  
-ATOM   6892  CD1 TYR D 178      17.750  -3.611  98.158  1.00 49.62           C  
-ATOM   6893  CD2 TYR D 178      19.069  -3.818 100.137  1.00 49.90           C  
-ATOM   6894  CE1 TYR D 178      17.666  -4.995  98.061  1.00 48.26           C  
-ATOM   6895  CE2 TYR D 178      18.989  -5.203 100.054  1.00 48.56           C  
-ATOM   6896  CZ  TYR D 178      18.287  -5.784  99.016  1.00 47.47           C  
-ATOM   6897  OH  TYR D 178      18.211  -7.151  98.935  1.00 44.99           O  
-ATOM   6898  N   HIS D 179      20.612   1.316  98.686  1.00 53.24           N  
-ATOM   6899  CA  HIS D 179      20.639   2.780  98.826  1.00 52.84           C  
-ATOM   6900  C   HIS D 179      20.024   3.522  97.639  1.00 52.14           C  
-ATOM   6901  O   HIS D 179      19.142   4.364  97.824  1.00 52.00           O  
-ATOM   6902  CB  HIS D 179      22.068   3.273  99.075  1.00 53.06           C  
-ATOM   6903  CG  HIS D 179      22.440   3.346 100.523  1.00 54.28           C  
-ATOM   6904  ND1 HIS D 179      22.526   2.230 101.327  1.00 55.73           N  
-ATOM   6905  CD2 HIS D 179      22.758   4.400 101.310  1.00 55.79           C  
-ATOM   6906  CE1 HIS D 179      22.882   2.591 102.547  1.00 55.61           C  
-ATOM   6907  NE2 HIS D 179      23.032   3.903 102.563  1.00 56.09           N  
-ATOM   6908  N   GLU D 180      20.489   3.190  96.434  1.00 51.40           N  
-ATOM   6909  CA  GLU D 180      19.981   3.755  95.182  1.00 50.82           C  
-ATOM   6910  C   GLU D 180      18.520   3.378  94.945  1.00 49.80           C  
-ATOM   6911  O   GLU D 180      17.706   4.220  94.558  1.00 49.59           O  
-ATOM   6912  CB  GLU D 180      20.847   3.276  93.999  1.00 51.32           C  
-ATOM   6913  CG  GLU D 180      20.458   3.828  92.631  1.00 53.02           C  
-ATOM   6914  CD  GLU D 180      21.411   3.393  91.522  1.00 56.15           C  
-ATOM   6915  OE1 GLU D 180      22.599   3.787  91.563  1.00 57.11           O  
-ATOM   6916  OE2 GLU D 180      20.975   2.659  90.601  1.00 57.27           O  
-ATOM   6917  N   ASP D 181      18.200   2.109  95.174  1.00 48.69           N  
-ATOM   6918  CA  ASP D 181      16.844   1.598  94.982  1.00 47.81           C  
-ATOM   6919  C   ASP D 181      15.825   2.320  95.860  1.00 46.79           C  
-ATOM   6920  O   ASP D 181      14.772   2.743  95.376  1.00 46.25           O  
-ATOM   6921  CB  ASP D 181      16.798   0.096  95.262  1.00 48.03           C  
-ATOM   6922  CG  ASP D 181      17.175  -0.734  94.056  1.00 48.77           C  
-ATOM   6923  OD1 ASP D 181      17.145  -0.209  92.917  1.00 50.18           O  
-ATOM   6924  OD2 ASP D 181      17.506  -1.933  94.152  1.00 49.65           O  
-ATOM   6925  N   ILE D 182      16.154   2.451  97.145  1.00 45.80           N  
-ATOM   6926  CA  ILE D 182      15.306   3.145  98.110  1.00 44.92           C  
-ATOM   6927  C   ILE D 182      15.243   4.642  97.790  1.00 44.61           C  
-ATOM   6928  O   ILE D 182      14.159   5.235  97.793  1.00 44.34           O  
-ATOM   6929  CB  ILE D 182      15.803   2.885  99.552  1.00 44.90           C  
-ATOM   6930  CG1 ILE D 182      15.398   1.472 100.001  1.00 44.18           C  
-ATOM   6931  CG2 ILE D 182      15.288   3.962 100.529  1.00 44.41           C  
-ATOM   6932  CD1 ILE D 182      16.366   0.841 100.961  1.00 43.60           C  
-ATOM   6933  N   HIS D 183      16.396   5.242  97.487  1.00 44.16           N  
-ATOM   6934  CA  HIS D 183      16.420   6.652  97.104  1.00 43.64           C  
-ATOM   6935  C   HIS D 183      15.502   6.932  95.927  1.00 43.14           C  
-ATOM   6936  O   HIS D 183      14.695   7.862  95.976  1.00 43.55           O  
-ATOM   6937  CB  HIS D 183      17.822   7.157  96.779  1.00 43.59           C  
-ATOM   6938  CG  HIS D 183      17.835   8.589  96.354  1.00 43.81           C  
-ATOM   6939  ND1 HIS D 183      17.964   9.627  97.251  1.00 44.13           N  
-ATOM   6940  CD2 HIS D 183      17.651   9.158  95.140  1.00 43.18           C  
-ATOM   6941  CE1 HIS D 183      17.898  10.775  96.601  1.00 44.58           C  
-ATOM   6942  NE2 HIS D 183      17.705  10.518  95.319  1.00 44.56           N  
-ATOM   6943  N   THR D 184      15.632   6.122  94.879  1.00 42.52           N  
-ATOM   6944  CA  THR D 184      14.810   6.237  93.676  1.00 41.84           C  
-ATOM   6945  C   THR D 184      13.325   6.045  93.972  1.00 41.43           C  
-ATOM   6946  O   THR D 184      12.478   6.705  93.363  1.00 41.54           O  
-ATOM   6947  CB  THR D 184      15.295   5.229  92.608  1.00 41.87           C  
-ATOM   6948  OG1 THR D 184      16.562   5.658  92.091  1.00 42.66           O  
-ATOM   6949  CG2 THR D 184      14.401   5.243  91.376  1.00 41.68           C  
-ATOM   6950  N   TYR D 185      13.011   5.142  94.901  1.00 40.86           N  
-ATOM   6951  CA  TYR D 185      11.621   4.868  95.263  1.00 40.08           C  
-ATOM   6952  C   TYR D 185      10.971   6.054  95.971  1.00 39.97           C  
-ATOM   6953  O   TYR D 185       9.874   6.482  95.601  1.00 39.71           O  
-ATOM   6954  CB  TYR D 185      11.502   3.616  96.138  1.00 39.82           C  
-ATOM   6955  CG  TYR D 185      10.066   3.284  96.492  1.00 39.41           C  
-ATOM   6956  CD1 TYR D 185       9.097   3.163  95.493  1.00 39.09           C  
-ATOM   6957  CD2 TYR D 185       9.668   3.103  97.819  1.00 39.37           C  
-ATOM   6958  CE1 TYR D 185       7.787   2.861  95.793  1.00 38.72           C  
-ATOM   6959  CE2 TYR D 185       8.336   2.796  98.133  1.00 39.08           C  
-ATOM   6960  CZ  TYR D 185       7.407   2.677  97.112  1.00 38.88           C  
-ATOM   6961  OH  TYR D 185       6.084   2.389  97.382  1.00 39.72           O  
-ATOM   6962  N   LEU D 186      11.655   6.569  96.989  1.00 39.92           N  
-ATOM   6963  CA  LEU D 186      11.168   7.696  97.779  1.00 40.14           C  
-ATOM   6964  C   LEU D 186      10.911   8.916  96.904  1.00 40.66           C  
-ATOM   6965  O   LEU D 186       9.964   9.669  97.140  1.00 40.58           O  
-ATOM   6966  CB  LEU D 186      12.168   8.043  98.886  1.00 39.83           C  
-ATOM   6967  CG  LEU D 186      12.384   7.003  99.988  1.00 39.50           C  
-ATOM   6968  CD1 LEU D 186      13.568   7.402 100.852  1.00 39.14           C  
-ATOM   6969  CD2 LEU D 186      11.121   6.805 100.836  1.00 38.63           C  
-ATOM   6970  N   ARG D 187      11.759   9.090  95.889  1.00 41.38           N  
-ATOM   6971  CA  ARG D 187      11.622  10.176  94.922  1.00 42.09           C  
-ATOM   6972  C   ARG D 187      10.335  10.054  94.116  1.00 42.35           C  
-ATOM   6973  O   ARG D 187       9.673  11.051  93.833  1.00 42.52           O  
-ATOM   6974  CB  ARG D 187      12.841  10.226  93.996  1.00 42.22           C  
-ATOM   6975  CG  ARG D 187      14.076  10.843  94.635  1.00 42.77           C  
-ATOM   6976  CD  ARG D 187      13.999  12.360  94.817  1.00 44.55           C  
-ATOM   6977  NE  ARG D 187      13.771  13.023  93.537  1.00 45.90           N  
-ATOM   6978  CZ  ARG D 187      14.687  13.718  92.878  1.00 46.78           C  
-ATOM   6979  NH1 ARG D 187      15.901  13.875  93.387  1.00 47.18           N  
-ATOM   6980  NH2 ARG D 187      14.383  14.267  91.708  1.00 47.53           N  
-ATOM   6981  N   GLU D 188       9.984   8.824  93.760  1.00 42.99           N  
-ATOM   6982  CA  GLU D 188       8.729   8.534  93.072  1.00 43.53           C  
-ATOM   6983  C   GLU D 188       7.530   8.726  94.005  1.00 43.62           C  
-ATOM   6984  O   GLU D 188       6.494   9.247  93.590  1.00 43.55           O  
-ATOM   6985  CB  GLU D 188       8.765   7.105  92.524  1.00 43.90           C  
-ATOM   6986  CG  GLU D 188       7.506   6.647  91.794  1.00 46.21           C  
-ATOM   6987  CD  GLU D 188       7.473   5.143  91.563  1.00 49.07           C  
-ATOM   6988  OE1 GLU D 188       8.557   4.539  91.385  1.00 50.66           O  
-ATOM   6989  OE2 GLU D 188       6.362   4.562  91.556  1.00 50.11           O  
-ATOM   6990  N   MET D 189       7.684   8.316  95.264  1.00 43.75           N  
-ATOM   6991  CA  MET D 189       6.583   8.354  96.229  1.00 44.07           C  
-ATOM   6992  C   MET D 189       6.268   9.748  96.779  1.00 43.96           C  
-ATOM   6993  O   MET D 189       5.099  10.070  97.009  1.00 44.04           O  
-ATOM   6994  CB  MET D 189       6.820   7.359  97.365  1.00 44.07           C  
-ATOM   6995  CG  MET D 189       6.542   5.905  96.982  1.00 45.50           C  
-ATOM   6996  SD  MET D 189       4.825   5.568  96.496  1.00 49.25           S  
-ATOM   6997  CE  MET D 189       5.038   5.217  94.764  1.00 48.31           C  
-ATOM   6998  N   GLU D 190       7.298  10.573  96.967  1.00 44.10           N  
-ATOM   6999  CA  GLU D 190       7.112  11.947  97.435  1.00 44.33           C  
-ATOM   7000  C   GLU D 190       6.209  12.733  96.483  1.00 44.40           C  
-ATOM   7001  O   GLU D 190       5.434  13.589  96.915  1.00 44.52           O  
-ATOM   7002  CB  GLU D 190       8.460  12.652  97.688  1.00 44.48           C  
-ATOM   7003  CG  GLU D 190       9.182  13.181  96.453  1.00 44.65           C  
-ATOM   7004  CD  GLU D 190      10.425  13.995  96.778  1.00 45.78           C  
-ATOM   7005  OE1 GLU D 190      10.550  14.502  97.915  1.00 45.81           O  
-ATOM   7006  OE2 GLU D 190      11.291  14.135  95.884  1.00 45.72           O  
-ATOM   7007  N   VAL D 191       6.287  12.405  95.194  1.00 44.45           N  
-ATOM   7008  CA  VAL D 191       5.405  12.994  94.189  1.00 44.43           C  
-ATOM   7009  C   VAL D 191       3.935  12.624  94.444  1.00 44.47           C  
-ATOM   7010  O   VAL D 191       3.066  13.495  94.455  1.00 44.32           O  
-ATOM   7011  CB  VAL D 191       5.837  12.599  92.749  1.00 44.49           C  
-ATOM   7012  CG1 VAL D 191       4.856  13.123  91.716  1.00 44.38           C  
-ATOM   7013  CG2 VAL D 191       7.253  13.100  92.450  1.00 44.37           C  
-ATOM   7014  N   LYS D 192       3.662  11.340  94.666  1.00 44.49           N  
-ATOM   7015  CA  LYS D 192       2.281  10.872  94.835  1.00 44.51           C  
-ATOM   7016  C   LYS D 192       1.663  11.251  96.187  1.00 44.12           C  
-ATOM   7017  O   LYS D 192       0.445  11.395  96.293  1.00 43.83           O  
-ATOM   7018  CB  LYS D 192       2.171   9.355  94.609  1.00 44.84           C  
-ATOM   7019  CG  LYS D 192       3.097   8.779  93.535  1.00 46.14           C  
-ATOM   7020  CD  LYS D 192       2.580   9.023  92.123  1.00 48.79           C  
-ATOM   7021  CE  LYS D 192       3.660   8.720  91.086  1.00 50.54           C  
-ATOM   7022  NZ  LYS D 192       3.952   9.894  90.198  1.00 51.42           N  
-ATOM   7023  N   CYS D 193       2.505  11.407  97.209  1.00 43.92           N  
-ATOM   7024  CA  CYS D 193       2.046  11.771  98.553  1.00 43.94           C  
-ATOM   7025  C   CYS D 193       2.049  13.284  98.791  1.00 43.57           C  
-ATOM   7026  O   CYS D 193       1.806  13.746  99.915  1.00 43.54           O  
-ATOM   7027  CB  CYS D 193       2.906  11.080  99.617  1.00 43.93           C  
-ATOM   7028  SG  CYS D 193       2.701   9.287  99.715  1.00 45.59           S  
-ATOM   7029  N   LYS D 194       2.333  14.048  97.737  1.00 43.09           N  
-ATOM   7030  CA  LYS D 194       2.386  15.504  97.818  1.00 42.58           C  
-ATOM   7031  C   LYS D 194       0.997  16.109  98.036  1.00 42.11           C  
-ATOM   7032  O   LYS D 194       0.061  15.811  97.292  1.00 42.00           O  
-ATOM   7033  CB  LYS D 194       3.041  16.096  96.562  1.00 42.74           C  
-ATOM   7034  CG  LYS D 194       3.197  17.612  96.588  1.00 43.35           C  
-ATOM   7035  CD  LYS D 194       3.952  18.135  95.373  1.00 44.01           C  
-ATOM   7036  CE  LYS D 194       4.732  19.399  95.719  1.00 44.34           C  
-ATOM   7037  NZ  LYS D 194       5.185  20.149  94.509  1.00 45.59           N  
-ATOM   7038  N   PRO D 195       0.867  16.952  99.060  1.00 41.60           N  
-ATOM   7039  CA  PRO D 195      -0.381  17.682  99.303  1.00 41.46           C  
-ATOM   7040  C   PRO D 195      -0.663  18.665  98.177  1.00 41.60           C  
-ATOM   7041  O   PRO D 195       0.261  19.076  97.469  1.00 41.33           O  
-ATOM   7042  CB  PRO D 195      -0.097  18.451 100.591  1.00 41.14           C  
-ATOM   7043  CG  PRO D 195       1.067  17.755 101.201  1.00 41.36           C  
-ATOM   7044  CD  PRO D 195       1.895  17.264 100.067  1.00 41.34           C  
-ATOM   7045  N   LYS D 196      -1.933  19.027  98.027  1.00 41.47           N  
-ATOM   7046  CA  LYS D 196      -2.365  19.972  97.013  1.00 41.78           C  
-ATOM   7047  C   LYS D 196      -1.887  21.396  97.345  1.00 41.59           C  
-ATOM   7048  O   LYS D 196      -2.303  21.985  98.354  1.00 41.45           O  
-ATOM   7049  CB  LYS D 196      -3.887  19.874  96.861  1.00 41.98           C  
-ATOM   7050  CG  LYS D 196      -4.595  21.090  96.324  1.00 43.25           C  
-ATOM   7051  CD  LYS D 196      -6.087  20.942  96.566  1.00 45.94           C  
-ATOM   7052  CE  LYS D 196      -6.854  20.872  95.259  1.00 47.60           C  
-ATOM   7053  NZ  LYS D 196      -7.091  22.235  94.685  1.00 49.28           N  
-ATOM   7054  N   VAL D 197      -0.992  21.919  96.501  1.00 41.16           N  
-ATOM   7055  CA  VAL D 197      -0.457  23.280  96.641  1.00 41.00           C  
-ATOM   7056  C   VAL D 197      -1.605  24.284  96.729  1.00 40.72           C  
-ATOM   7057  O   VAL D 197      -2.549  24.228  95.943  1.00 40.94           O  
-ATOM   7058  CB  VAL D 197       0.502  23.664  95.467  1.00 41.08           C  
-ATOM   7059  CG1 VAL D 197       1.054  25.078  95.639  1.00 41.08           C  
-ATOM   7060  CG2 VAL D 197       1.657  22.674  95.349  1.00 41.05           C  
-ATOM   7061  N   GLY D 198      -1.528  25.187  97.701  1.00 40.40           N  
-ATOM   7062  CA  GLY D 198      -2.576  26.173  97.914  1.00 39.69           C  
-ATOM   7063  C   GLY D 198      -3.956  25.568  98.129  1.00 39.25           C  
-ATOM   7064  O   GLY D 198      -4.929  26.034  97.534  1.00 39.81           O  
-ATOM   7065  N   TYR D 199      -4.045  24.524  98.959  1.00 38.03           N  
-ATOM   7066  CA  TYR D 199      -5.343  23.961  99.344  1.00 36.62           C  
-ATOM   7067  C   TYR D 199      -6.093  24.909 100.274  1.00 36.38           C  
-ATOM   7068  O   TYR D 199      -7.321  24.897 100.328  1.00 36.25           O  
-ATOM   7069  CB  TYR D 199      -5.196  22.561  99.980  1.00 36.12           C  
-ATOM   7070  CG  TYR D 199      -4.519  22.508 101.337  1.00 33.40           C  
-ATOM   7071  CD1 TYR D 199      -5.169  22.950 102.491  1.00 31.75           C  
-ATOM   7072  CD2 TYR D 199      -3.237  21.981 101.473  1.00 32.39           C  
-ATOM   7073  CE1 TYR D 199      -4.543  22.902 103.738  1.00 30.16           C  
-ATOM   7074  CE2 TYR D 199      -2.610  21.918 102.713  1.00 31.18           C  
-ATOM   7075  CZ  TYR D 199      -3.269  22.378 103.838  1.00 30.61           C  
-ATOM   7076  OH  TYR D 199      -2.639  22.313 105.061  1.00 30.77           O  
-ATOM   7077  N   MET D 200      -5.330  25.719 101.004  1.00 36.37           N  
-ATOM   7078  CA  MET D 200      -5.853  26.697 101.959  1.00 36.60           C  
-ATOM   7079  C   MET D 200      -6.771  27.732 101.301  1.00 36.52           C  
-ATOM   7080  O   MET D 200      -7.705  28.229 101.930  1.00 36.27           O  
-ATOM   7081  CB  MET D 200      -4.691  27.399 102.664  1.00 36.77           C  
-ATOM   7082  CG  MET D 200      -4.861  27.597 104.164  1.00 37.60           C  
-ATOM   7083  SD  MET D 200      -5.770  26.303 105.021  1.00 39.65           S  
-ATOM   7084  CE  MET D 200      -4.549  25.709 106.157  1.00 40.16           C  
-ATOM   7085  N   LYS D 201      -6.504  28.036 100.032  1.00 36.40           N  
-ATOM   7086  CA  LYS D 201      -7.367  28.912  99.239  1.00 36.68           C  
-ATOM   7087  C   LYS D 201      -8.779  28.333  99.069  1.00 36.33           C  
-ATOM   7088  O   LYS D 201      -9.729  29.066  98.797  1.00 36.14           O  
-ATOM   7089  CB  LYS D 201      -6.755  29.157  97.858  1.00 37.03           C  
-ATOM   7090  CG  LYS D 201      -5.494  30.011  97.841  1.00 38.38           C  
-ATOM   7091  CD  LYS D 201      -4.899  30.066  96.431  1.00 41.45           C  
-ATOM   7092  CE  LYS D 201      -3.652  30.943  96.375  1.00 43.74           C  
-ATOM   7093  NZ  LYS D 201      -3.971  32.411  96.509  1.00 46.02           N  
-ATOM   7094  N   LYS D 202      -8.904  27.017  99.223  1.00 35.73           N  
-ATOM   7095  CA  LYS D 202     -10.180  26.340  99.030  1.00 35.49           C  
-ATOM   7096  C   LYS D 202     -10.878  26.034 100.363  1.00 34.75           C  
-ATOM   7097  O   LYS D 202     -12.013  25.555 100.382  1.00 34.75           O  
-ATOM   7098  CB  LYS D 202      -9.988  25.069  98.190  1.00 36.05           C  
-ATOM   7099  CG  LYS D 202      -9.363  25.312  96.803  1.00 37.42           C  
-ATOM   7100  CD  LYS D 202     -10.416  25.676  95.762  1.00 40.67           C  
-ATOM   7101  CE  LYS D 202     -10.234  24.880  94.468  1.00 42.76           C  
-ATOM   7102  NZ  LYS D 202     -10.503  23.416  94.652  1.00 44.56           N  
-ATOM   7103  N   GLN D 203     -10.195  26.327 101.468  1.00 33.86           N  
-ATOM   7104  CA  GLN D 203     -10.758  26.156 102.805  1.00 33.17           C  
-ATOM   7105  C   GLN D 203     -11.378  27.475 103.243  1.00 33.38           C  
-ATOM   7106  O   GLN D 203     -10.658  28.441 103.482  1.00 34.07           O  
-ATOM   7107  CB  GLN D 203      -9.680  25.718 103.809  1.00 32.55           C  
-ATOM   7108  CG  GLN D 203      -9.081  24.331 103.555  1.00 30.45           C  
-ATOM   7109  CD  GLN D 203      -9.901  23.193 104.150  1.00 28.07           C  
-ATOM   7110  OE1 GLN D 203     -10.917  23.418 104.811  1.00 25.90           O  
-ATOM   7111  NE2 GLN D 203      -9.459  21.962 103.907  1.00 27.40           N  
-ATOM   7112  N   PRO D 204     -12.704  27.526 103.333  1.00 33.61           N  
-ATOM   7113  CA  PRO D 204     -13.403  28.770 103.686  1.00 33.85           C  
-ATOM   7114  C   PRO D 204     -13.250  29.194 105.149  1.00 34.13           C  
-ATOM   7115  O   PRO D 204     -13.431  30.375 105.435  1.00 34.52           O  
-ATOM   7116  CB  PRO D 204     -14.871  28.462 103.368  1.00 33.69           C  
-ATOM   7117  CG  PRO D 204     -14.986  26.962 103.365  1.00 33.71           C  
-ATOM   7118  CD  PRO D 204     -13.634  26.404 103.096  1.00 33.65           C  
-ATOM   7119  N   ASP D 205     -12.905  28.270 106.046  1.00 34.00           N  
-ATOM   7120  CA  ASP D 205     -12.904  28.570 107.475  1.00 33.90           C  
-ATOM   7121  C   ASP D 205     -11.528  28.602 108.128  1.00 33.24           C  
-ATOM   7122  O   ASP D 205     -11.401  29.020 109.277  1.00 33.21           O  
-ATOM   7123  CB  ASP D 205     -13.815  27.588 108.228  1.00 34.20           C  
-ATOM   7124  CG  ASP D 205     -14.437  28.201 109.467  1.00 35.94           C  
-ATOM   7125  OD1 ASP D 205     -15.249  29.148 109.326  1.00 38.43           O  
-ATOM   7126  OD2 ASP D 205     -14.177  27.805 110.627  1.00 38.00           O  
-ATOM   7127  N   ILE D 206     -10.505  28.151 107.410  1.00 32.74           N  
-ATOM   7128  CA  ILE D 206      -9.156  28.078 107.976  1.00 32.12           C  
-ATOM   7129  C   ILE D 206      -8.098  28.677 107.052  1.00 31.88           C  
-ATOM   7130  O   ILE D 206      -8.303  28.774 105.834  1.00 32.18           O  
-ATOM   7131  CB  ILE D 206      -8.778  26.624 108.402  1.00 31.97           C  
-ATOM   7132  CG1 ILE D 206      -8.893  25.642 107.239  1.00 31.71           C  
-ATOM   7133  CG2 ILE D 206      -9.639  26.163 109.571  1.00 32.22           C  
-ATOM   7134  CD1 ILE D 206      -8.210  24.291 107.496  1.00 32.51           C  
-ATOM   7135  N   THR D 207      -6.972  29.071 107.643  1.00 31.12           N  
-ATOM   7136  CA  THR D 207      -5.911  29.775 106.928  1.00 30.54           C  
-ATOM   7137  C   THR D 207      -4.548  29.171 107.250  1.00 30.63           C  
-ATOM   7138  O   THR D 207      -4.437  28.303 108.123  1.00 30.80           O  
-ATOM   7139  CB  THR D 207      -5.892  31.261 107.332  1.00 30.50           C  
-ATOM   7140  OG1 THR D 207      -5.519  31.357 108.705  1.00 29.57           O  
-ATOM   7141  CG2 THR D 207      -7.290  31.873 107.306  1.00 29.97           C  
-ATOM   7142  N   ASN D 208      -3.513  29.656 106.564  1.00 30.65           N  
-ATOM   7143  CA  ASN D 208      -2.137  29.192 106.759  1.00 30.71           C  
-ATOM   7144  C   ASN D 208      -1.600  29.475 108.163  1.00 30.65           C  
-ATOM   7145  O   ASN D 208      -0.772  28.728 108.687  1.00 30.48           O  
-ATOM   7146  CB  ASN D 208      -1.207  29.838 105.727  1.00 30.72           C  
-ATOM   7147  CG  ASN D 208      -1.367  29.250 104.329  1.00 32.10           C  
-ATOM   7148  OD1 ASN D 208      -1.590  28.048 104.162  1.00 33.10           O  
-ATOM   7149  ND2 ASN D 208      -1.229  30.102 103.310  1.00 33.78           N  
-ATOM   7150  N   SER D 209      -2.070  30.577 108.745  1.00 30.58           N  
-ATOM   7151  CA  SER D 209      -1.669  31.032 110.070  1.00 30.03           C  
-ATOM   7152  C   SER D 209      -2.205  30.078 111.132  1.00 29.52           C  
-ATOM   7153  O   SER D 209      -1.527  29.778 112.118  1.00 29.94           O  
-ATOM   7154  CB  SER D 209      -2.207  32.444 110.299  1.00 30.05           C  
-ATOM   7155  OG  SER D 209      -2.170  32.802 111.672  1.00 31.84           O  
-ATOM   7156  N   MET D 210      -3.429  29.605 110.929  1.00 28.82           N  
-ATOM   7157  CA  MET D 210      -4.021  28.603 111.810  1.00 28.02           C  
-ATOM   7158  C   MET D 210      -3.253  27.292 111.706  1.00 27.52           C  
-ATOM   7159  O   MET D 210      -3.003  26.641 112.723  1.00 27.00           O  
-ATOM   7160  CB  MET D 210      -5.493  28.382 111.468  1.00 28.01           C  
-ATOM   7161  CG  MET D 210      -6.365  29.580 111.697  1.00 27.33           C  
-ATOM   7162  SD  MET D 210      -8.042  29.198 111.220  1.00 28.48           S  
-ATOM   7163  CE  MET D 210      -8.769  30.822 111.145  1.00 27.97           C  
-ATOM   7164  N   ARG D 211      -2.880  26.928 110.477  1.00 26.86           N  
-ATOM   7165  CA  ARG D 211      -2.046  25.761 110.208  1.00 27.28           C  
-ATOM   7166  C   ARG D 211      -0.679  25.873 110.888  1.00 27.19           C  
-ATOM   7167  O   ARG D 211      -0.161  24.887 111.419  1.00 27.13           O  
-ATOM   7168  CB  ARG D 211      -1.869  25.572 108.691  1.00 27.38           C  
-ATOM   7169  CG  ARG D 211      -1.136  24.295 108.282  1.00 27.88           C  
-ATOM   7170  CD  ARG D 211      -0.618  24.307 106.840  1.00 29.17           C  
-ATOM   7171  NE  ARG D 211       0.360  23.253 106.575  1.00 29.13           N  
-ATOM   7172  CZ  ARG D 211       1.639  23.307 106.932  1.00 29.78           C  
-ATOM   7173  NH1 ARG D 211       2.114  24.366 107.571  1.00 29.86           N  
-ATOM   7174  NH2 ARG D 211       2.456  22.301 106.646  1.00 30.59           N  
-ATOM   7175  N   ALA D 212      -0.099  27.072 110.857  1.00 27.22           N  
-ATOM   7176  CA  ALA D 212       1.171  27.351 111.537  1.00 27.20           C  
-ATOM   7177  C   ALA D 212       1.033  27.140 113.045  1.00 27.09           C  
-ATOM   7178  O   ALA D 212       1.886  26.510 113.675  1.00 27.15           O  
-ATOM   7179  CB  ALA D 212       1.649  28.778 111.226  1.00 27.15           C  
-ATOM   7180  N   ILE D 213      -0.055  27.646 113.617  1.00 27.19           N  
-ATOM   7181  CA  ILE D 213      -0.355  27.407 115.033  1.00 27.45           C  
-ATOM   7182  C   ILE D 213      -0.444  25.901 115.350  1.00 27.39           C  
-ATOM   7183  O   ILE D 213       0.146  25.422 116.330  1.00 27.23           O  
-ATOM   7184  CB  ILE D 213      -1.648  28.163 115.455  1.00 27.44           C  
-ATOM   7185  CG1 ILE D 213      -1.383  29.676 115.527  1.00 27.04           C  
-ATOM   7186  CG2 ILE D 213      -2.180  27.645 116.795  1.00 27.86           C  
-ATOM   7187  CD1 ILE D 213      -2.647  30.528 115.547  1.00 27.47           C  
-ATOM   7188  N   LEU D 214      -1.168  25.162 114.510  1.00 27.31           N  
-ATOM   7189  CA  LEU D 214      -1.319  23.720 114.687  1.00 26.90           C  
-ATOM   7190  C   LEU D 214       0.026  22.994 114.627  1.00 26.78           C  
-ATOM   7191  O   LEU D 214       0.345  22.206 115.525  1.00 26.97           O  
-ATOM   7192  CB  LEU D 214      -2.293  23.133 113.662  1.00 26.60           C  
-ATOM   7193  CG  LEU D 214      -2.550  21.622 113.732  1.00 26.46           C  
-ATOM   7194  CD1 LEU D 214      -3.318  21.233 115.009  1.00 25.52           C  
-ATOM   7195  CD2 LEU D 214      -3.299  21.158 112.477  1.00 24.88           C  
-ATOM   7196  N   VAL D 215       0.819  23.275 113.596  1.00 26.15           N  
-ATOM   7197  CA  VAL D 215       2.097  22.582 113.428  1.00 26.02           C  
-ATOM   7198  C   VAL D 215       3.050  22.864 114.596  1.00 26.21           C  
-ATOM   7199  O   VAL D 215       3.750  21.965 115.073  1.00 26.13           O  
-ATOM   7200  CB  VAL D 215       2.770  22.885 112.054  1.00 25.95           C  
-ATOM   7201  CG1 VAL D 215       4.125  22.185 111.953  1.00 25.50           C  
-ATOM   7202  CG2 VAL D 215       1.881  22.406 110.904  1.00 25.11           C  
-ATOM   7203  N   ASP D 216       3.049  24.107 115.068  1.00 26.36           N  
-ATOM   7204  CA  ASP D 216       3.875  24.506 116.195  1.00 26.60           C  
-ATOM   7205  C   ASP D 216       3.446  23.790 117.468  1.00 26.47           C  
-ATOM   7206  O   ASP D 216       4.284  23.408 118.284  1.00 26.23           O  
-ATOM   7207  CB  ASP D 216       3.817  26.020 116.385  1.00 27.15           C  
-ATOM   7208  CG  ASP D 216       4.760  26.501 117.460  1.00 28.02           C  
-ATOM   7209  OD1 ASP D 216       4.352  26.513 118.638  1.00 30.59           O  
-ATOM   7210  OD2 ASP D 216       5.929  26.867 117.227  1.00 29.07           O  
-ATOM   7211  N   TRP D 217       2.139  23.594 117.624  1.00 26.41           N  
-ATOM   7212  CA  TRP D 217       1.624  22.810 118.744  1.00 26.47           C  
-ATOM   7213  C   TRP D 217       2.057  21.345 118.638  1.00 26.36           C  
-ATOM   7214  O   TRP D 217       2.341  20.711 119.648  1.00 26.36           O  
-ATOM   7215  CB  TRP D 217       0.098  22.908 118.854  1.00 26.35           C  
-ATOM   7216  CG  TRP D 217      -0.461  21.998 119.904  1.00 27.23           C  
-ATOM   7217  CD1 TRP D 217      -0.267  22.090 121.261  1.00 27.84           C  
-ATOM   7218  CD2 TRP D 217      -1.281  20.841 119.700  1.00 28.26           C  
-ATOM   7219  NE1 TRP D 217      -0.924  21.070 121.908  1.00 27.94           N  
-ATOM   7220  CE2 TRP D 217      -1.558  20.287 120.978  1.00 29.03           C  
-ATOM   7221  CE3 TRP D 217      -1.820  20.212 118.568  1.00 27.80           C  
-ATOM   7222  CZ2 TRP D 217      -2.346  19.138 121.149  1.00 29.41           C  
-ATOM   7223  CZ3 TRP D 217      -2.601  19.069 118.741  1.00 27.89           C  
-ATOM   7224  CH2 TRP D 217      -2.858  18.548 120.020  1.00 27.97           C  
-ATOM   7225  N   LEU D 218       2.112  20.811 117.421  1.00 26.68           N  
-ATOM   7226  CA  LEU D 218       2.539  19.420 117.232  1.00 27.23           C  
-ATOM   7227  C   LEU D 218       3.998  19.179 117.627  1.00 27.43           C  
-ATOM   7228  O   LEU D 218       4.341  18.108 118.132  1.00 27.51           O  
-ATOM   7229  CB  LEU D 218       2.289  18.973 115.795  1.00 27.15           C  
-ATOM   7230  CG  LEU D 218       0.815  18.838 115.425  1.00 27.78           C  
-ATOM   7231  CD1 LEU D 218       0.691  18.322 114.023  1.00 27.92           C  
-ATOM   7232  CD2 LEU D 218       0.093  17.918 116.398  1.00 29.20           C  
-ATOM   7233  N   VAL D 219       4.846  20.178 117.385  1.00 27.84           N  
-ATOM   7234  CA  VAL D 219       6.239  20.155 117.823  1.00 28.07           C  
-ATOM   7235  C   VAL D 219       6.292  20.096 119.365  1.00 28.87           C  
-ATOM   7236  O   VAL D 219       7.017  19.272 119.932  1.00 29.31           O  
-ATOM   7237  CB  VAL D 219       7.033  21.379 117.270  1.00 28.21           C  
-ATOM   7238  CG1 VAL D 219       8.502  21.333 117.687  1.00 27.45           C  
-ATOM   7239  CG2 VAL D 219       6.920  21.476 115.750  1.00 26.63           C  
-ATOM   7240  N   GLU D 220       5.503  20.940 120.032  1.00 29.37           N  
-ATOM   7241  CA  GLU D 220       5.381  20.907 121.497  1.00 30.47           C  
-ATOM   7242  C   GLU D 220       5.004  19.514 121.989  1.00 30.16           C  
-ATOM   7243  O   GLU D 220       5.569  19.012 122.963  1.00 29.81           O  
-ATOM   7244  CB  GLU D 220       4.322  21.899 121.991  1.00 30.91           C  
-ATOM   7245  CG  GLU D 220       4.562  23.344 121.597  1.00 34.41           C  
-ATOM   7246  CD  GLU D 220       3.682  24.308 122.368  1.00 38.33           C  
-ATOM   7247  OE1 GLU D 220       4.046  24.662 123.511  1.00 40.75           O  
-ATOM   7248  OE2 GLU D 220       2.632  24.722 121.831  1.00 41.16           O  
-ATOM   7249  N   VAL D 221       4.045  18.902 121.297  1.00 30.18           N  
-ATOM   7250  CA  VAL D 221       3.563  17.563 121.629  1.00 29.98           C  
-ATOM   7251  C   VAL D 221       4.672  16.540 121.413  1.00 30.72           C  
-ATOM   7252  O   VAL D 221       4.855  15.629 122.227  1.00 30.57           O  
-ATOM   7253  CB  VAL D 221       2.315  17.198 120.786  1.00 29.98           C  
-ATOM   7254  CG1 VAL D 221       1.922  15.721 120.970  1.00 29.53           C  
-ATOM   7255  CG2 VAL D 221       1.166  18.118 121.130  1.00 27.04           C  
-ATOM   7256  N   GLY D 222       5.416  16.710 120.322  1.00 31.39           N  
-ATOM   7257  CA  GLY D 222       6.520  15.829 120.000  1.00 32.16           C  
-ATOM   7258  C   GLY D 222       7.575  15.844 121.088  1.00 33.03           C  
-ATOM   7259  O   GLY D 222       8.153  14.813 121.415  1.00 32.60           O  
-ATOM   7260  N   GLU D 223       7.813  17.022 121.657  1.00 34.25           N  
-ATOM   7261  CA  GLU D 223       8.819  17.180 122.710  1.00 35.61           C  
-ATOM   7262  C   GLU D 223       8.335  16.704 124.064  1.00 35.87           C  
-ATOM   7263  O   GLU D 223       9.099  16.101 124.808  1.00 36.29           O  
-ATOM   7264  CB  GLU D 223       9.302  18.638 122.791  1.00 35.92           C  
-ATOM   7265  CG  GLU D 223      10.096  19.079 121.573  1.00 37.36           C  
-ATOM   7266  CD  GLU D 223      11.002  17.979 121.042  1.00 41.59           C  
-ATOM   7267  OE1 GLU D 223      10.554  17.173 120.180  1.00 42.80           O  
-ATOM   7268  OE2 GLU D 223      12.172  17.921 121.489  1.00 44.10           O  
-ATOM   7269  N   GLU D 224       7.071  16.976 124.377  1.00 36.28           N  
-ATOM   7270  CA  GLU D 224       6.457  16.513 125.619  1.00 36.96           C  
-ATOM   7271  C   GLU D 224       6.497  14.980 125.762  1.00 36.95           C  
-ATOM   7272  O   GLU D 224       6.761  14.454 126.846  1.00 36.87           O  
-ATOM   7273  CB  GLU D 224       5.016  17.022 125.703  1.00 37.20           C  
-ATOM   7274  CG  GLU D 224       4.211  16.516 126.893  1.00 40.20           C  
-ATOM   7275  CD  GLU D 224       4.752  16.988 128.234  1.00 44.06           C  
-ATOM   7276  OE1 GLU D 224       5.177  18.164 128.345  1.00 46.52           O  
-ATOM   7277  OE2 GLU D 224       4.743  16.179 129.188  1.00 46.10           O  
-ATOM   7278  N   TYR D 225       6.232  14.270 124.669  1.00 36.56           N  
-ATOM   7279  CA  TYR D 225       6.207  12.815 124.713  1.00 36.80           C  
-ATOM   7280  C   TYR D 225       7.469  12.200 124.126  1.00 36.50           C  
-ATOM   7281  O   TYR D 225       7.537  10.989 123.925  1.00 36.39           O  
-ATOM   7282  CB  TYR D 225       4.946  12.277 124.032  1.00 36.76           C  
-ATOM   7283  CG  TYR D 225       3.688  12.623 124.788  1.00 38.08           C  
-ATOM   7284  CD1 TYR D 225       3.292  11.880 125.898  1.00 38.72           C  
-ATOM   7285  CD2 TYR D 225       2.901  13.707 124.410  1.00 39.42           C  
-ATOM   7286  CE1 TYR D 225       2.140  12.200 126.604  1.00 38.86           C  
-ATOM   7287  CE2 TYR D 225       1.746  14.032 125.107  1.00 39.58           C  
-ATOM   7288  CZ  TYR D 225       1.370  13.274 126.203  1.00 39.58           C  
-ATOM   7289  OH  TYR D 225       0.223  13.587 126.901  1.00 40.04           O  
-ATOM   7290  N   LYS D 226       8.467  13.052 123.875  1.00 36.48           N  
-ATOM   7291  CA  LYS D 226       9.774  12.645 123.334  1.00 36.26           C  
-ATOM   7292  C   LYS D 226       9.643  11.728 122.118  1.00 35.57           C  
-ATOM   7293  O   LYS D 226      10.175  10.614 122.093  1.00 35.56           O  
-ATOM   7294  CB  LYS D 226      10.658  12.022 124.425  1.00 36.54           C  
-ATOM   7295  CG  LYS D 226      11.007  12.992 125.565  1.00 38.05           C  
-ATOM   7296  CD  LYS D 226      12.117  12.434 126.466  1.00 42.01           C  
-ATOM   7297  CE  LYS D 226      11.571  11.424 127.476  1.00 44.03           C  
-ATOM   7298  NZ  LYS D 226      12.411  11.339 128.714  1.00 46.72           N  
-ATOM   7299  N   LEU D 227       8.922  12.219 121.114  1.00 34.59           N  
-ATOM   7300  CA  LEU D 227       8.663  11.466 119.898  1.00 34.08           C  
-ATOM   7301  C   LEU D 227       9.754  11.687 118.864  1.00 34.07           C  
-ATOM   7302  O   LEU D 227      10.505  12.664 118.942  1.00 34.34           O  
-ATOM   7303  CB  LEU D 227       7.291  11.844 119.322  1.00 34.01           C  
-ATOM   7304  CG  LEU D 227       6.054  11.635 120.205  1.00 33.10           C  
-ATOM   7305  CD1 LEU D 227       4.832  12.237 119.555  1.00 34.21           C  
-ATOM   7306  CD2 LEU D 227       5.816  10.167 120.519  1.00 32.34           C  
-ATOM   7307  N   GLN D 228       9.845  10.771 117.901  1.00 33.90           N  
-ATOM   7308  CA  GLN D 228      10.799  10.888 116.797  1.00 33.43           C  
-ATOM   7309  C   GLN D 228      10.447  12.083 115.928  1.00 33.23           C  
-ATOM   7310  O   GLN D 228       9.263  12.385 115.746  1.00 33.38           O  
-ATOM   7311  CB  GLN D 228      10.781   9.625 115.935  1.00 33.42           C  
-ATOM   7312  CG  GLN D 228      11.397   8.400 116.582  1.00 33.67           C  
-ATOM   7313  CD  GLN D 228      12.822   8.635 117.030  1.00 35.08           C  
-ATOM   7314  OE1 GLN D 228      13.629   9.194 116.284  1.00 35.53           O  
-ATOM   7315  NE2 GLN D 228      13.136   8.220 118.252  1.00 35.55           N  
-ATOM   7316  N   ASN D 229      11.464  12.762 115.394  1.00 32.74           N  
-ATOM   7317  CA  ASN D 229      11.234  13.875 114.468  1.00 32.38           C  
-ATOM   7318  C   ASN D 229      10.466  13.424 113.239  1.00 31.39           C  
-ATOM   7319  O   ASN D 229       9.645  14.180 112.693  1.00 31.02           O  
-ATOM   7320  CB  ASN D 229      12.555  14.528 114.040  1.00 32.90           C  
-ATOM   7321  CG  ASN D 229      13.118  15.462 115.098  1.00 34.65           C  
-ATOM   7322  OD1 ASN D 229      12.389  15.980 115.945  1.00 36.90           O  
-ATOM   7323  ND2 ASN D 229      14.429  15.665 115.062  1.00 37.33           N  
-ATOM   7324  N   GLU D 230      10.742  12.185 112.822  1.00 30.28           N  
-ATOM   7325  CA  GLU D 230      10.078  11.549 111.686  1.00 29.63           C  
-ATOM   7326  C   GLU D 230       8.566  11.511 111.866  1.00 28.98           C  
-ATOM   7327  O   GLU D 230       7.818  11.732 110.910  1.00 28.80           O  
-ATOM   7328  CB  GLU D 230      10.641  10.132 111.465  1.00 29.77           C  
-ATOM   7329  CG  GLU D 230      10.011   9.323 110.333  1.00 30.30           C  
-ATOM   7330  CD  GLU D 230      10.079   9.998 108.973  1.00 31.89           C  
-ATOM   7331  OE1 GLU D 230      10.884  10.946 108.813  1.00 32.42           O  
-ATOM   7332  OE2 GLU D 230       9.324   9.573 108.057  1.00 31.31           O  
-ATOM   7333  N   THR D 231       8.134  11.239 113.100  1.00 28.19           N  
-ATOM   7334  CA  THR D 231       6.720  11.175 113.467  1.00 27.49           C  
-ATOM   7335  C   THR D 231       6.018  12.501 113.207  1.00 26.97           C  
-ATOM   7336  O   THR D 231       4.932  12.533 112.633  1.00 26.95           O  
-ATOM   7337  CB  THR D 231       6.597  10.775 114.952  1.00 27.52           C  
-ATOM   7338  OG1 THR D 231       7.157   9.471 115.124  1.00 28.07           O  
-ATOM   7339  CG2 THR D 231       5.140  10.604 115.376  1.00 27.20           C  
-ATOM   7340  N   LEU D 232       6.662  13.588 113.625  1.00 26.37           N  
-ATOM   7341  CA  LEU D 232       6.188  14.947 113.384  1.00 25.80           C  
-ATOM   7342  C   LEU D 232       6.024  15.240 111.886  1.00 25.25           C  
-ATOM   7343  O   LEU D 232       4.993  15.773 111.459  1.00 25.05           O  
-ATOM   7344  CB  LEU D 232       7.172  15.925 114.019  1.00 25.80           C  
-ATOM   7345  CG  LEU D 232       6.957  17.435 114.149  1.00 27.70           C  
-ATOM   7346  CD1 LEU D 232       7.965  18.146 113.259  1.00 29.01           C  
-ATOM   7347  CD2 LEU D 232       5.536  17.934 113.904  1.00 27.12           C  
-ATOM   7348  N   HIS D 233       7.038  14.885 111.098  1.00 24.46           N  
-ATOM   7349  CA  HIS D 233       7.011  15.100 109.649  1.00 23.95           C  
-ATOM   7350  C   HIS D 233       5.849  14.370 109.000  1.00 23.15           C  
-ATOM   7351  O   HIS D 233       5.075  14.961 108.246  1.00 23.36           O  
-ATOM   7352  CB  HIS D 233       8.334  14.663 109.026  1.00 23.76           C  
-ATOM   7353  CG  HIS D 233       9.419  15.685 109.146  1.00 24.86           C  
-ATOM   7354  ND1 HIS D 233      10.038  15.976 110.344  1.00 24.60           N  
-ATOM   7355  CD2 HIS D 233       9.980  16.503 108.224  1.00 25.22           C  
-ATOM   7356  CE1 HIS D 233      10.939  16.920 110.153  1.00 23.84           C  
-ATOM   7357  NE2 HIS D 233      10.931  17.252 108.875  1.00 25.16           N  
-ATOM   7358  N   LEU D 234       5.711  13.088 109.321  1.00 22.67           N  
-ATOM   7359  CA  LEU D 234       4.582  12.285 108.837  1.00 21.91           C  
-ATOM   7360  C   LEU D 234       3.237  12.908 109.174  1.00 21.56           C  
-ATOM   7361  O   LEU D 234       2.341  13.003 108.317  1.00 21.40           O  
-ATOM   7362  CB  LEU D 234       4.645  10.880 109.428  1.00 21.70           C  
-ATOM   7363  CG  LEU D 234       5.707   9.931 108.887  1.00 20.79           C  
-ATOM   7364  CD1 LEU D 234       5.716   8.698 109.769  1.00 19.40           C  
-ATOM   7365  CD2 LEU D 234       5.450   9.562 107.407  1.00 19.86           C  
-ATOM   7366  N   ALA D 235       3.097  13.336 110.425  1.00 21.42           N  
-ATOM   7367  CA  ALA D 235       1.846  13.929 110.898  1.00 21.27           C  
-ATOM   7368  C   ALA D 235       1.419  15.127 110.040  1.00 21.30           C  
-ATOM   7369  O   ALA D 235       0.250  15.234 109.634  1.00 21.05           O  
-ATOM   7370  CB  ALA D 235       1.970  14.322 112.367  1.00 20.91           C  
-ATOM   7371  N   VAL D 236       2.373  16.012 109.759  1.00 21.29           N  
-ATOM   7372  CA  VAL D 236       2.126  17.195 108.931  1.00 21.55           C  
-ATOM   7373  C   VAL D 236       1.694  16.802 107.518  1.00 21.35           C  
-ATOM   7374  O   VAL D 236       0.790  17.406 106.948  1.00 21.55           O  
-ATOM   7375  CB  VAL D 236       3.373  18.140 108.895  1.00 21.63           C  
-ATOM   7376  CG1 VAL D 236       3.109  19.376 108.048  1.00 20.85           C  
-ATOM   7377  CG2 VAL D 236       3.769  18.553 110.320  1.00 22.17           C  
-ATOM   7378  N   ASN D 237       2.328  15.773 106.967  1.00 21.95           N  
-ATOM   7379  CA  ASN D 237       1.971  15.272 105.641  1.00 22.15           C  
-ATOM   7380  C   ASN D 237       0.536  14.746 105.633  1.00 21.77           C  
-ATOM   7381  O   ASN D 237      -0.228  15.002 104.695  1.00 21.63           O  
-ATOM   7382  CB  ASN D 237       2.978  14.192 105.186  1.00 22.72           C  
-ATOM   7383  CG  ASN D 237       2.556  13.497 103.894  1.00 24.63           C  
-ATOM   7384  OD1 ASN D 237       1.869  12.470 103.920  1.00 28.28           O  
-ATOM   7385  ND2 ASN D 237       2.958  14.057 102.762  1.00 26.71           N  
-ATOM   7386  N   TYR D 238       0.160  14.032 106.693  1.00 22.00           N  
-ATOM   7387  CA  TYR D 238      -1.210  13.502 106.803  1.00 21.73           C  
-ATOM   7388  C   TYR D 238      -2.196  14.657 106.878  1.00 22.09           C  
-ATOM   7389  O   TYR D 238      -3.215  14.658 106.180  1.00 22.12           O  
-ATOM   7390  CB  TYR D 238      -1.382  12.591 108.033  1.00 21.23           C  
-ATOM   7391  CG  TYR D 238      -0.443  11.404 108.129  1.00 21.04           C  
-ATOM   7392  CD1 TYR D 238       0.306  10.968 107.035  1.00 21.42           C  
-ATOM   7393  CD2 TYR D 238      -0.314  10.705 109.329  1.00 22.26           C  
-ATOM   7394  CE1 TYR D 238       1.182   9.877 107.139  1.00 21.70           C  
-ATOM   7395  CE2 TYR D 238       0.544   9.609 109.443  1.00 21.70           C  
-ATOM   7396  CZ  TYR D 238       1.289   9.199 108.350  1.00 22.44           C  
-ATOM   7397  OH  TYR D 238       2.140   8.111 108.478  1.00 20.92           O  
-ATOM   7398  N   ILE D 239      -1.884  15.648 107.719  1.00 22.50           N  
-ATOM   7399  CA  ILE D 239      -2.747  16.832 107.869  1.00 22.71           C  
-ATOM   7400  C   ILE D 239      -2.954  17.538 106.533  1.00 23.07           C  
-ATOM   7401  O   ILE D 239      -4.085  17.781 106.129  1.00 23.57           O  
-ATOM   7402  CB  ILE D 239      -2.185  17.823 108.926  1.00 22.04           C  
-ATOM   7403  CG1 ILE D 239      -2.275  17.205 110.327  1.00 22.55           C  
-ATOM   7404  CG2 ILE D 239      -2.969  19.131 108.901  1.00 21.63           C  
-ATOM   7405  CD1 ILE D 239      -1.239  17.718 111.332  1.00 20.47           C  
-ATOM   7406  N   ASP D 240      -1.856  17.856 105.850  1.00 23.72           N  
-ATOM   7407  CA  ASP D 240      -1.929  18.577 104.577  1.00 24.13           C  
-ATOM   7408  C   ASP D 240      -2.741  17.829 103.521  1.00 23.86           C  
-ATOM   7409  O   ASP D 240      -3.586  18.420 102.856  1.00 24.31           O  
-ATOM   7410  CB  ASP D 240      -0.524  18.911 104.066  1.00 24.00           C  
-ATOM   7411  CG  ASP D 240       0.132  20.038 104.844  1.00 25.61           C  
-ATOM   7412  OD1 ASP D 240      -0.591  20.932 105.354  1.00 27.58           O  
-ATOM   7413  OD2 ASP D 240       1.371  20.116 105.000  1.00 25.23           O  
-ATOM   7414  N   ARG D 241      -2.513  16.525 103.398  1.00 23.92           N  
-ATOM   7415  CA  ARG D 241      -3.295  15.699 102.470  1.00 23.74           C  
-ATOM   7416  C   ARG D 241      -4.765  15.609 102.854  1.00 23.54           C  
-ATOM   7417  O   ARG D 241      -5.631  15.641 101.983  1.00 23.85           O  
-ATOM   7418  CB  ARG D 241      -2.702  14.300 102.336  1.00 23.26           C  
-ATOM   7419  CG  ARG D 241      -1.373  14.266 101.601  1.00 23.97           C  
-ATOM   7420  CD  ARG D 241      -0.552  13.026 101.907  1.00 25.00           C  
-ATOM   7421  NE  ARG D 241      -1.232  11.804 101.483  1.00 25.23           N  
-ATOM   7422  CZ  ARG D 241      -1.046  10.605 102.037  1.00 25.40           C  
-ATOM   7423  NH1 ARG D 241      -0.180  10.449 103.036  1.00 23.94           N  
-ATOM   7424  NH2 ARG D 241      -1.714   9.554 101.573  1.00 24.22           N  
-ATOM   7425  N   PHE D 242      -5.046  15.493 104.152  1.00 23.61           N  
-ATOM   7426  CA  PHE D 242      -6.423  15.434 104.634  1.00 23.43           C  
-ATOM   7427  C   PHE D 242      -7.154  16.730 104.281  1.00 23.70           C  
-ATOM   7428  O   PHE D 242      -8.261  16.702 103.740  1.00 23.73           O  
-ATOM   7429  CB  PHE D 242      -6.473  15.175 106.154  1.00 23.13           C  
-ATOM   7430  CG  PHE D 242      -7.870  15.036 106.705  1.00 22.00           C  
-ATOM   7431  CD1 PHE D 242      -8.486  13.791 106.769  1.00 22.21           C  
-ATOM   7432  CD2 PHE D 242      -8.569  16.146 107.156  1.00 21.56           C  
-ATOM   7433  CE1 PHE D 242      -9.783  13.649 107.280  1.00 21.55           C  
-ATOM   7434  CE2 PHE D 242      -9.863  16.024 107.671  1.00 22.24           C  
-ATOM   7435  CZ  PHE D 242     -10.473  14.773 107.730  1.00 23.08           C  
-ATOM   7436  N   LEU D 243      -6.522  17.864 104.576  1.00 24.43           N  
-ATOM   7437  CA  LEU D 243      -7.109  19.179 104.276  1.00 25.01           C  
-ATOM   7438  C   LEU D 243      -7.126  19.527 102.772  1.00 25.87           C  
-ATOM   7439  O   LEU D 243      -7.797  20.485 102.361  1.00 26.05           O  
-ATOM   7440  CB  LEU D 243      -6.403  20.284 105.077  1.00 24.65           C  
-ATOM   7441  CG  LEU D 243      -6.411  20.217 106.616  1.00 23.79           C  
-ATOM   7442  CD1 LEU D 243      -5.412  21.201 107.179  1.00 22.61           C  
-ATOM   7443  CD2 LEU D 243      -7.779  20.501 107.197  1.00 22.62           C  
-ATOM   7444  N   SER D 244      -6.395  18.742 101.972  1.00 26.20           N  
-ATOM   7445  CA  SER D 244      -6.401  18.844 100.519  1.00 26.84           C  
-ATOM   7446  C   SER D 244      -7.686  18.291  99.903  1.00 27.69           C  
-ATOM   7447  O   SER D 244      -7.979  18.574  98.742  1.00 28.07           O  
-ATOM   7448  CB  SER D 244      -5.198  18.098  99.913  1.00 26.79           C  
-ATOM   7449  OG  SER D 244      -3.970  18.767 100.158  1.00 26.19           O  
-ATOM   7450  N   SER D 245      -8.439  17.491 100.658  1.00 28.36           N  
-ATOM   7451  CA  SER D 245      -9.709  16.953 100.155  1.00 29.24           C  
-ATOM   7452  C   SER D 245     -10.920  17.147 101.070  1.00 29.00           C  
-ATOM   7453  O   SER D 245     -12.052  16.942 100.646  1.00 29.48           O  
-ATOM   7454  CB  SER D 245      -9.577  15.477  99.757  1.00 29.51           C  
-ATOM   7455  OG  SER D 245      -8.928  14.722 100.761  1.00 31.66           O  
-ATOM   7456  N   MET D 246     -10.687  17.535 102.314  1.00 29.02           N  
-ATOM   7457  CA  MET D 246     -11.777  17.703 103.270  1.00 28.87           C  
-ATOM   7458  C   MET D 246     -11.790  19.119 103.815  1.00 28.96           C  
-ATOM   7459  O   MET D 246     -10.791  19.592 104.374  1.00 28.45           O  
-ATOM   7460  CB  MET D 246     -11.629  16.714 104.429  1.00 29.40           C  
-ATOM   7461  CG  MET D 246     -11.557  15.241 104.005  1.00 29.65           C  
-ATOM   7462  SD  MET D 246     -13.153  14.656 103.460  1.00 30.91           S  
-ATOM   7463  CE  MET D 246     -13.971  14.388 105.083  1.00 28.28           C  
-ATOM   7464  N   SER D 247     -12.921  19.800 103.652  1.00 28.83           N  
-ATOM   7465  CA  SER D 247     -13.079  21.105 104.266  1.00 29.21           C  
-ATOM   7466  C   SER D 247     -13.348  20.881 105.753  1.00 28.77           C  
-ATOM   7467  O   SER D 247     -14.157  20.023 106.119  1.00 28.60           O  
-ATOM   7468  CB  SER D 247     -14.191  21.898 103.591  1.00 29.09           C  
-ATOM   7469  OG  SER D 247     -15.439  21.513 104.119  1.00 32.28           O  
-ATOM   7470  N   VAL D 248     -12.627  21.630 106.587  1.00 28.49           N  
-ATOM   7471  CA  VAL D 248     -12.659  21.502 108.046  1.00 28.06           C  
-ATOM   7472  C   VAL D 248     -12.879  22.893 108.652  1.00 28.23           C  
-ATOM   7473  O   VAL D 248     -12.189  23.838 108.284  1.00 28.22           O  
-ATOM   7474  CB  VAL D 248     -11.319  20.887 108.577  1.00 28.19           C  
-ATOM   7475  CG1 VAL D 248     -11.198  20.990 110.101  1.00 27.45           C  
-ATOM   7476  CG2 VAL D 248     -11.176  19.429 108.137  1.00 26.85           C  
-ATOM   7477  N   LEU D 249     -13.854  23.015 109.557  1.00 28.39           N  
-ATOM   7478  CA  LEU D 249     -14.065  24.245 110.321  1.00 28.36           C  
-ATOM   7479  C   LEU D 249     -12.912  24.415 111.306  1.00 28.10           C  
-ATOM   7480  O   LEU D 249     -12.262  23.438 111.668  1.00 27.28           O  
-ATOM   7481  CB  LEU D 249     -15.398  24.192 111.082  1.00 28.71           C  
-ATOM   7482  CG  LEU D 249     -16.712  24.171 110.292  1.00 29.47           C  
-ATOM   7483  CD1 LEU D 249     -17.881  24.258 111.243  1.00 29.21           C  
-ATOM   7484  CD2 LEU D 249     -16.774  25.297 109.271  1.00 29.70           C  
-ATOM   7485  N   ARG D 250     -12.647  25.645 111.739  1.00 28.21           N  
-ATOM   7486  CA  ARG D 250     -11.455  25.885 112.565  1.00 28.78           C  
-ATOM   7487  C   ARG D 250     -11.508  25.267 113.972  1.00 28.16           C  
-ATOM   7488  O   ARG D 250     -10.472  24.910 114.533  1.00 28.68           O  
-ATOM   7489  CB  ARG D 250     -11.073  27.370 112.608  1.00 29.05           C  
-ATOM   7490  CG  ARG D 250     -12.015  28.228 113.373  1.00 31.16           C  
-ATOM   7491  CD  ARG D 250     -11.369  29.440 114.026  1.00 33.62           C  
-ATOM   7492  NE  ARG D 250     -12.395  30.136 114.779  1.00 35.19           N  
-ATOM   7493  CZ  ARG D 250     -12.609  31.438 114.761  1.00 36.16           C  
-ATOM   7494  NH1 ARG D 250     -11.844  32.249 114.035  1.00 36.49           N  
-ATOM   7495  NH2 ARG D 250     -13.599  31.929 115.489  1.00 36.43           N  
-ATOM   7496  N   GLY D 251     -12.711  25.110 114.509  1.00 27.64           N  
-ATOM   7497  CA  GLY D 251     -12.909  24.439 115.782  1.00 27.08           C  
-ATOM   7498  C   GLY D 251     -12.619  22.942 115.761  1.00 26.72           C  
-ATOM   7499  O   GLY D 251     -12.596  22.302 116.821  1.00 26.75           O  
-ATOM   7500  N   LYS D 252     -12.376  22.391 114.569  1.00 25.73           N  
-ATOM   7501  CA  LYS D 252     -12.090  20.962 114.409  1.00 25.10           C  
-ATOM   7502  C   LYS D 252     -10.686  20.710 113.865  1.00 24.78           C  
-ATOM   7503  O   LYS D 252     -10.245  19.559 113.765  1.00 24.48           O  
-ATOM   7504  CB  LYS D 252     -13.142  20.296 113.502  1.00 25.04           C  
-ATOM   7505  CG  LYS D 252     -14.530  20.188 114.108  1.00 24.41           C  
-ATOM   7506  CD  LYS D 252     -14.508  19.483 115.462  1.00 25.00           C  
-ATOM   7507  CE  LYS D 252     -15.876  18.925 115.829  1.00 27.07           C  
-ATOM   7508  NZ  LYS D 252     -16.732  19.991 116.439  1.00 28.34           N  
-ATOM   7509  N   LEU D 253      -9.984  21.792 113.529  1.00 24.37           N  
-ATOM   7510  CA  LEU D 253      -8.619  21.710 113.013  1.00 24.16           C  
-ATOM   7511  C   LEU D 253      -7.667  20.977 113.967  1.00 24.05           C  
-ATOM   7512  O   LEU D 253      -6.860  20.155 113.526  1.00 24.52           O  
-ATOM   7513  CB  LEU D 253      -8.083  23.109 112.668  1.00 24.01           C  
-ATOM   7514  CG  LEU D 253      -6.717  23.224 111.981  1.00 24.51           C  
-ATOM   7515  CD1 LEU D 253      -6.670  22.496 110.626  1.00 24.20           C  
-ATOM   7516  CD2 LEU D 253      -6.326  24.691 111.815  1.00 25.57           C  
-ATOM   7517  N   GLN D 254      -7.760  21.259 115.267  1.00 23.52           N  
-ATOM   7518  CA  GLN D 254      -6.885  20.589 116.228  1.00 23.27           C  
-ATOM   7519  C   GLN D 254      -7.200  19.094 116.342  1.00 22.57           C  
-ATOM   7520  O   GLN D 254      -6.305  18.276 116.606  1.00 22.62           O  
-ATOM   7521  CB  GLN D 254      -6.940  21.252 117.610  1.00 23.27           C  
-ATOM   7522  CG  GLN D 254      -5.623  21.115 118.404  1.00 24.77           C  
-ATOM   7523  CD  GLN D 254      -5.710  21.608 119.867  1.00 27.75           C  
-ATOM   7524  OE1 GLN D 254      -4.884  21.221 120.701  1.00 29.75           O  
-ATOM   7525  NE2 GLN D 254      -6.689  22.452 120.168  1.00 25.93           N  
-ATOM   7526  N   LEU D 255      -8.466  18.751 116.134  1.00 21.62           N  
-ATOM   7527  CA  LEU D 255      -8.906  17.363 116.180  1.00 21.78           C  
-ATOM   7528  C   LEU D 255      -8.255  16.558 115.052  1.00 21.50           C  
-ATOM   7529  O   LEU D 255      -7.809  15.434 115.265  1.00 22.33           O  
-ATOM   7530  CB  LEU D 255     -10.447  17.280 116.139  1.00 21.51           C  
-ATOM   7531  CG  LEU D 255     -11.100  15.888 116.146  1.00 21.83           C  
-ATOM   7532  CD1 LEU D 255     -10.722  15.083 117.405  1.00 20.11           C  
-ATOM   7533  CD2 LEU D 255     -12.617  16.004 115.987  1.00 19.63           C  
-ATOM   7534  N   VAL D 256      -8.183  17.163 113.868  1.00 21.21           N  
-ATOM   7535  CA  VAL D 256      -7.490  16.588 112.715  1.00 20.62           C  
-ATOM   7536  C   VAL D 256      -6.008  16.374 113.015  1.00 20.29           C  
-ATOM   7537  O   VAL D 256      -5.468  15.299 112.756  1.00 20.03           O  
-ATOM   7538  CB  VAL D 256      -7.631  17.490 111.458  1.00 20.41           C  
-ATOM   7539  CG1 VAL D 256      -6.785  16.951 110.304  1.00 20.26           C  
-ATOM   7540  CG2 VAL D 256      -9.089  17.617 111.046  1.00 20.34           C  
-ATOM   7541  N   GLY D 257      -5.362  17.401 113.566  1.00 19.90           N  
-ATOM   7542  CA  GLY D 257      -3.955  17.326 113.920  1.00 19.54           C  
-ATOM   7543  C   GLY D 257      -3.659  16.304 114.999  1.00 19.69           C  
-ATOM   7544  O   GLY D 257      -2.627  15.642 114.946  1.00 19.73           O  
-ATOM   7545  N   THR D 258      -4.559  16.171 115.974  1.00 19.60           N  
-ATOM   7546  CA  THR D 258      -4.409  15.173 117.033  1.00 19.81           C  
-ATOM   7547  C   THR D 258      -4.502  13.747 116.483  1.00 19.47           C  
-ATOM   7548  O   THR D 258      -3.688  12.894 116.823  1.00 18.97           O  
-ATOM   7549  CB  THR D 258      -5.464  15.388 118.147  1.00 20.21           C  
-ATOM   7550  OG1 THR D 258      -5.386  16.738 118.619  1.00 21.22           O  
-ATOM   7551  CG2 THR D 258      -5.134  14.562 119.368  1.00 19.57           C  
-ATOM   7552  N   ALA D 259      -5.496  13.508 115.637  1.00 19.81           N  
-ATOM   7553  CA  ALA D 259      -5.636  12.218 114.946  1.00 20.15           C  
-ATOM   7554  C   ALA D 259      -4.439  11.918 114.053  1.00 19.97           C  
-ATOM   7555  O   ALA D 259      -3.936  10.797 114.057  1.00 20.90           O  
-ATOM   7556  CB  ALA D 259      -6.932  12.172 114.136  1.00 19.52           C  
-ATOM   7557  N   ALA D 260      -3.964  12.919 113.314  1.00 20.10           N  
-ATOM   7558  CA  ALA D 260      -2.793  12.747 112.434  1.00 20.27           C  
-ATOM   7559  C   ALA D 260      -1.575  12.328 113.232  1.00 20.73           C  
-ATOM   7560  O   ALA D 260      -0.826  11.435 112.827  1.00 20.58           O  
-ATOM   7561  CB  ALA D 260      -2.491  14.032 111.685  1.00 19.99           C  
-ATOM   7562  N   MET D 261      -1.383  12.971 114.384  1.00 21.37           N  
-ATOM   7563  CA  MET D 261      -0.222  12.686 115.222  1.00 22.06           C  
-ATOM   7564  C   MET D 261      -0.309  11.286 115.841  1.00 21.97           C  
-ATOM   7565  O   MET D 261       0.704  10.613 116.005  1.00 22.12           O  
-ATOM   7566  CB  MET D 261      -0.075  13.754 116.314  1.00 22.31           C  
-ATOM   7567  CG  MET D 261       1.313  13.800 116.954  1.00 25.09           C  
-ATOM   7568  SD  MET D 261       2.523  14.459 115.815  1.00 29.17           S  
-ATOM   7569  CE  MET D 261       3.936  14.709 116.858  1.00 28.65           C  
-ATOM   7570  N   LEU D 262      -1.522  10.864 116.192  1.00 21.93           N  
-ATOM   7571  CA  LEU D 262      -1.741   9.535 116.746  1.00 22.03           C  
-ATOM   7572  C   LEU D 262      -1.395   8.470 115.702  1.00 21.67           C  
-ATOM   7573  O   LEU D 262      -0.686   7.514 116.000  1.00 21.72           O  
-ATOM   7574  CB  LEU D 262      -3.201   9.394 117.215  1.00 22.33           C  
-ATOM   7575  CG  LEU D 262      -3.722   8.019 117.650  1.00 22.64           C  
-ATOM   7576  CD1 LEU D 262      -2.973   7.491 118.861  1.00 22.85           C  
-ATOM   7577  CD2 LEU D 262      -5.226   8.094 117.930  1.00 22.88           C  
-ATOM   7578  N   LEU D 263      -1.882   8.665 114.476  1.00 21.41           N  
-ATOM   7579  CA  LEU D 263      -1.629   7.738 113.375  1.00 21.21           C  
-ATOM   7580  C   LEU D 263      -0.152   7.653 113.071  1.00 21.02           C  
-ATOM   7581  O   LEU D 263       0.397   6.558 112.927  1.00 20.78           O  
-ATOM   7582  CB  LEU D 263      -2.414   8.153 112.122  1.00 21.28           C  
-ATOM   7583  CG  LEU D 263      -3.915   7.850 112.173  1.00 21.42           C  
-ATOM   7584  CD1 LEU D 263      -4.664   8.467 110.997  1.00 21.25           C  
-ATOM   7585  CD2 LEU D 263      -4.122   6.350 112.206  1.00 21.53           C  
-ATOM   7586  N   ALA D 264       0.491   8.816 112.993  1.00 21.28           N  
-ATOM   7587  CA  ALA D 264       1.928   8.883 112.773  1.00 21.49           C  
-ATOM   7588  C   ALA D 264       2.695   8.212 113.909  1.00 21.79           C  
-ATOM   7589  O   ALA D 264       3.703   7.550 113.669  1.00 22.10           O  
-ATOM   7590  CB  ALA D 264       2.376  10.334 112.599  1.00 21.42           C  
-ATOM   7591  N   SER D 265       2.224   8.386 115.145  1.00 21.86           N  
-ATOM   7592  CA  SER D 265       2.830   7.707 116.294  1.00 21.96           C  
-ATOM   7593  C   SER D 265       2.702   6.186 116.194  1.00 22.09           C  
-ATOM   7594  O   SER D 265       3.662   5.455 116.477  1.00 22.23           O  
-ATOM   7595  CB  SER D 265       2.193   8.194 117.589  1.00 22.24           C  
-ATOM   7596  OG  SER D 265       2.554   9.547 117.817  1.00 23.97           O  
-ATOM   7597  N   LYS D 266       1.519   5.714 115.790  1.00 21.34           N  
-ATOM   7598  CA  LYS D 266       1.286   4.287 115.633  1.00 21.25           C  
-ATOM   7599  C   LYS D 266       2.145   3.691 114.510  1.00 21.57           C  
-ATOM   7600  O   LYS D 266       2.655   2.593 114.634  1.00 21.76           O  
-ATOM   7601  CB  LYS D 266      -0.197   4.018 115.366  1.00 20.86           C  
-ATOM   7602  CG  LYS D 266      -1.052   3.962 116.632  1.00 19.97           C  
-ATOM   7603  CD  LYS D 266      -2.507   3.656 116.296  1.00 16.70           C  
-ATOM   7604  CE  LYS D 266      -3.400   3.730 117.537  1.00 16.66           C  
-ATOM   7605  NZ  LYS D 266      -4.843   3.697 117.156  1.00 15.87           N  
-ATOM   7606  N   PHE D 267       2.284   4.420 113.409  1.00 22.32           N  
-ATOM   7607  CA  PHE D 267       3.084   3.967 112.279  1.00 22.82           C  
-ATOM   7608  C   PHE D 267       4.579   3.924 112.624  1.00 23.41           C  
-ATOM   7609  O   PHE D 267       5.252   2.921 112.370  1.00 23.33           O  
-ATOM   7610  CB  PHE D 267       2.831   4.885 111.085  1.00 22.99           C  
-ATOM   7611  CG  PHE D 267       3.579   4.493 109.842  1.00 23.25           C  
-ATOM   7612  CD1 PHE D 267       4.878   4.963 109.615  1.00 22.22           C  
-ATOM   7613  CD2 PHE D 267       2.989   3.655 108.901  1.00 22.07           C  
-ATOM   7614  CE1 PHE D 267       5.572   4.604 108.455  1.00 23.76           C  
-ATOM   7615  CE2 PHE D 267       3.679   3.285 107.735  1.00 22.91           C  
-ATOM   7616  CZ  PHE D 267       4.964   3.760 107.512  1.00 22.41           C  
-ATOM   7617  N   GLU D 268       5.074   4.997 113.243  1.00 24.15           N  
-ATOM   7618  CA  GLU D 268       6.511   5.244 113.356  1.00 24.94           C  
-ATOM   7619  C   GLU D 268       7.172   4.856 114.688  1.00 25.67           C  
-ATOM   7620  O   GLU D 268       8.331   4.442 114.693  1.00 25.78           O  
-ATOM   7621  CB  GLU D 268       6.799   6.721 113.047  1.00 24.98           C  
-ATOM   7622  CG  GLU D 268       8.262   7.078 112.759  1.00 25.76           C  
-ATOM   7623  CD  GLU D 268       8.888   6.258 111.644  1.00 26.40           C  
-ATOM   7624  OE1 GLU D 268       8.223   6.024 110.610  1.00 26.20           O  
-ATOM   7625  OE2 GLU D 268      10.062   5.860 111.800  1.00 27.05           O  
-ATOM   7626  N   GLU D 269       6.463   5.010 115.809  1.00 26.24           N  
-ATOM   7627  CA  GLU D 269       7.090   4.851 117.133  1.00 26.76           C  
-ATOM   7628  C   GLU D 269       7.147   3.405 117.602  1.00 26.95           C  
-ATOM   7629  O   GLU D 269       6.238   2.618 117.342  1.00 27.00           O  
-ATOM   7630  CB  GLU D 269       6.351   5.670 118.200  1.00 26.93           C  
-ATOM   7631  CG  GLU D 269       6.360   7.175 117.993  1.00 28.18           C  
-ATOM   7632  CD  GLU D 269       7.716   7.803 118.242  1.00 29.54           C  
-ATOM   7633  OE1 GLU D 269       8.463   7.299 119.104  1.00 31.04           O  
-ATOM   7634  OE2 GLU D 269       8.029   8.811 117.578  1.00 29.23           O  
-ATOM   7635  N   ILE D 270       8.210   3.070 118.321  1.00 27.52           N  
-ATOM   7636  CA  ILE D 270       8.276   1.797 119.027  1.00 28.18           C  
-ATOM   7637  C   ILE D 270       7.153   1.745 120.073  1.00 28.70           C  
-ATOM   7638  O   ILE D 270       6.398   0.767 120.135  1.00 29.13           O  
-ATOM   7639  CB  ILE D 270       9.670   1.585 119.666  1.00 28.25           C  
-ATOM   7640  CG1 ILE D 270      10.742   1.473 118.575  1.00 28.50           C  
-ATOM   7641  CG2 ILE D 270       9.676   0.331 120.563  1.00 27.64           C  
-ATOM   7642  CD1 ILE D 270      12.185   1.460 119.096  1.00 29.05           C  
-ATOM   7643  N   TYR D 271       7.034   2.812 120.860  1.00 29.26           N  
-ATOM   7644  CA  TYR D 271       6.036   2.899 121.926  1.00 29.94           C  
-ATOM   7645  C   TYR D 271       5.211   4.179 121.803  1.00 29.93           C  
-ATOM   7646  O   TYR D 271       5.448   5.132 122.548  1.00 30.35           O  
-ATOM   7647  CB  TYR D 271       6.711   2.891 123.305  1.00 30.47           C  
-ATOM   7648  CG  TYR D 271       7.596   1.699 123.597  1.00 32.17           C  
-ATOM   7649  CD1 TYR D 271       7.070   0.414 123.660  1.00 34.54           C  
-ATOM   7650  CD2 TYR D 271       8.959   1.864 123.828  1.00 34.21           C  
-ATOM   7651  CE1 TYR D 271       7.883  -0.683 123.938  1.00 35.56           C  
-ATOM   7652  CE2 TYR D 271       9.780   0.772 124.104  1.00 35.65           C  
-ATOM   7653  CZ  TYR D 271       9.231  -0.493 124.159  1.00 36.20           C  
-ATOM   7654  OH  TYR D 271      10.036  -1.578 124.428  1.00 40.06           O  
-ATOM   7655  N   PRO D 272       4.228   4.202 120.904  1.00 29.66           N  
-ATOM   7656  CA  PRO D 272       3.422   5.408 120.698  1.00 29.99           C  
-ATOM   7657  C   PRO D 272       2.705   5.781 122.000  1.00 30.21           C  
-ATOM   7658  O   PRO D 272       2.434   4.878 122.788  1.00 30.70           O  
-ATOM   7659  CB  PRO D 272       2.398   4.973 119.643  1.00 30.02           C  
-ATOM   7660  CG  PRO D 272       2.398   3.496 119.677  1.00 29.44           C  
-ATOM   7661  CD  PRO D 272       3.775   3.084 120.059  1.00 29.49           C  
-ATOM   7662  N   PRO D 273       2.433   7.061 122.241  1.00 30.01           N  
-ATOM   7663  CA  PRO D 273       1.629   7.447 123.399  1.00 30.11           C  
-ATOM   7664  C   PRO D 273       0.237   6.847 123.273  1.00 30.77           C  
-ATOM   7665  O   PRO D 273      -0.247   6.674 122.149  1.00 30.74           O  
-ATOM   7666  CB  PRO D 273       1.552   8.969 123.292  1.00 29.75           C  
-ATOM   7667  CG  PRO D 273       2.698   9.352 122.419  1.00 30.18           C  
-ATOM   7668  CD  PRO D 273       2.864   8.226 121.444  1.00 30.05           C  
-ATOM   7669  N   GLU D 274      -0.388   6.538 124.407  1.00 31.12           N  
-ATOM   7670  CA  GLU D 274      -1.755   6.036 124.434  1.00 31.87           C  
-ATOM   7671  C   GLU D 274      -2.694   7.126 123.949  1.00 31.27           C  
-ATOM   7672  O   GLU D 274      -2.372   8.309 124.053  1.00 30.96           O  
-ATOM   7673  CB  GLU D 274      -2.162   5.615 125.855  1.00 32.46           C  
-ATOM   7674  CG  GLU D 274      -1.105   4.870 126.668  1.00 35.78           C  
-ATOM   7675  CD  GLU D 274      -1.329   5.002 128.175  1.00 40.27           C  
-ATOM   7676  OE1 GLU D 274      -2.481   5.250 128.601  1.00 42.76           O  
-ATOM   7677  OE2 GLU D 274      -0.352   4.861 128.946  1.00 43.14           O  
-ATOM   7678  N   VAL D 275      -3.849   6.720 123.421  1.00 31.07           N  
-ATOM   7679  CA  VAL D 275      -4.900   7.649 122.986  1.00 30.72           C  
-ATOM   7680  C   VAL D 275      -5.271   8.643 124.096  1.00 30.73           C  
-ATOM   7681  O   VAL D 275      -5.441   9.849 123.840  1.00 30.22           O  
-ATOM   7682  CB  VAL D 275      -6.166   6.884 122.499  1.00 30.88           C  
-ATOM   7683  CG1 VAL D 275      -7.317   7.841 122.196  1.00 31.12           C  
-ATOM   7684  CG2 VAL D 275      -5.854   6.030 121.274  1.00 30.93           C  
-ATOM   7685  N   ALA D 276      -5.369   8.133 125.326  1.00 30.66           N  
-ATOM   7686  CA  ALA D 276      -5.693   8.946 126.499  1.00 30.66           C  
-ATOM   7687  C   ALA D 276      -4.722  10.103 126.664  1.00 30.70           C  
-ATOM   7688  O   ALA D 276      -5.103  11.171 127.141  1.00 30.73           O  
-ATOM   7689  CB  ALA D 276      -5.719   8.085 127.766  1.00 30.52           C  
-ATOM   7690  N   GLU D 277      -3.472   9.885 126.262  1.00 30.85           N  
-ATOM   7691  CA  GLU D 277      -2.454  10.930 126.295  1.00 31.38           C  
-ATOM   7692  C   GLU D 277      -2.692  11.982 125.209  1.00 31.23           C  
-ATOM   7693  O   GLU D 277      -2.493  13.168 125.443  1.00 31.46           O  
-ATOM   7694  CB  GLU D 277      -1.046  10.327 126.189  1.00 31.89           C  
-ATOM   7695  CG  GLU D 277      -0.539   9.752 127.507  1.00 34.01           C  
-ATOM   7696  CD  GLU D 277       0.716   8.906 127.357  1.00 37.23           C  
-ATOM   7697  OE1 GLU D 277       0.754   8.037 126.461  1.00 37.87           O  
-ATOM   7698  OE2 GLU D 277       1.667   9.102 128.155  1.00 40.06           O  
-ATOM   7699  N   PHE D 278      -3.134  11.552 124.032  1.00 30.92           N  
-ATOM   7700  CA  PHE D 278      -3.491  12.494 122.974  1.00 30.88           C  
-ATOM   7701  C   PHE D 278      -4.732  13.321 123.339  1.00 31.65           C  
-ATOM   7702  O   PHE D 278      -4.804  14.514 123.017  1.00 31.27           O  
-ATOM   7703  CB  PHE D 278      -3.665  11.781 121.629  1.00 29.99           C  
-ATOM   7704  CG  PHE D 278      -2.365  11.330 121.018  1.00 28.87           C  
-ATOM   7705  CD1 PHE D 278      -1.582  12.213 120.288  1.00 26.48           C  
-ATOM   7706  CD2 PHE D 278      -1.917  10.024 121.188  1.00 28.06           C  
-ATOM   7707  CE1 PHE D 278      -0.376  11.803 119.726  1.00 27.43           C  
-ATOM   7708  CE2 PHE D 278      -0.707   9.603 120.634  1.00 28.37           C  
-ATOM   7709  CZ  PHE D 278       0.067  10.495 119.899  1.00 26.70           C  
-ATOM   7710  N   VAL D 279      -5.690  12.690 124.019  1.00 32.28           N  
-ATOM   7711  CA  VAL D 279      -6.863  13.402 124.518  1.00 33.86           C  
-ATOM   7712  C   VAL D 279      -6.435  14.429 125.570  1.00 35.12           C  
-ATOM   7713  O   VAL D 279      -6.865  15.578 125.530  1.00 34.75           O  
-ATOM   7714  CB  VAL D 279      -7.943  12.450 125.105  1.00 33.55           C  
-ATOM   7715  CG1 VAL D 279      -9.150  13.243 125.614  1.00 33.23           C  
-ATOM   7716  CG2 VAL D 279      -8.389  11.451 124.072  1.00 33.20           C  
-ATOM   7717  N   TYR D 280      -5.566  14.008 126.486  1.00 37.11           N  
-ATOM   7718  CA  TYR D 280      -5.007  14.905 127.493  1.00 39.27           C  
-ATOM   7719  C   TYR D 280      -4.421  16.196 126.918  1.00 40.29           C  
-ATOM   7720  O   TYR D 280      -4.825  17.278 127.339  1.00 40.43           O  
-ATOM   7721  CB  TYR D 280      -3.981  14.187 128.375  1.00 39.32           C  
-ATOM   7722  CG  TYR D 280      -3.623  14.973 129.619  1.00 41.72           C  
-ATOM   7723  CD1 TYR D 280      -4.545  15.132 130.656  1.00 43.34           C  
-ATOM   7724  CD2 TYR D 280      -2.372  15.574 129.753  1.00 43.42           C  
-ATOM   7725  CE1 TYR D 280      -4.226  15.862 131.797  1.00 44.99           C  
-ATOM   7726  CE2 TYR D 280      -2.040  16.301 130.895  1.00 45.11           C  
-ATOM   7727  CZ  TYR D 280      -2.974  16.442 131.910  1.00 46.02           C  
-ATOM   7728  OH  TYR D 280      -2.656  17.158 133.044  1.00 48.37           O  
-ATOM   7729  N   ILE D 281      -3.501  16.091 125.956  1.00 41.87           N  
-ATOM   7730  CA  ILE D 281      -2.838  17.279 125.386  1.00 43.43           C  
-ATOM   7731  C   ILE D 281      -3.746  18.232 124.597  1.00 44.37           C  
-ATOM   7732  O   ILE D 281      -3.447  19.423 124.506  1.00 44.26           O  
-ATOM   7733  CB  ILE D 281      -1.578  16.925 124.533  1.00 43.56           C  
-ATOM   7734  CG1 ILE D 281      -1.764  15.613 123.776  1.00 44.13           C  
-ATOM   7735  CG2 ILE D 281      -0.324  16.893 125.397  1.00 44.13           C  
-ATOM   7736  CD1 ILE D 281      -1.528  15.733 122.288  1.00 45.90           C  
-ATOM   7737  N   THR D 282      -4.829  17.722 124.012  1.00 45.93           N  
-ATOM   7738  CA  THR D 282      -5.851  18.608 123.444  1.00 47.81           C  
-ATOM   7739  C   THR D 282      -6.601  19.286 124.580  1.00 48.97           C  
-ATOM   7740  O   THR D 282      -7.519  20.074 124.352  1.00 49.68           O  
-ATOM   7741  CB  THR D 282      -6.848  17.866 122.509  1.00 47.98           C  
-ATOM   7742  OG1 THR D 282      -7.126  16.549 123.010  1.00 48.26           O  
-ATOM   7743  CG2 THR D 282      -6.223  17.619 121.155  1.00 47.11           C  
-ATOM   7744  N   ASP D 283      -6.179  18.964 125.801  1.00 50.42           N  
-ATOM   7745  CA  ASP D 283      -6.706  19.525 127.041  1.00 51.69           C  
-ATOM   7746  C   ASP D 283      -8.166  19.137 127.256  1.00 51.68           C  
-ATOM   7747  O   ASP D 283      -8.463  17.958 127.479  1.00 51.95           O  
-ATOM   7748  CB  ASP D 283      -6.470  21.045 127.118  1.00 52.20           C  
-ATOM   7749  CG  ASP D 283      -5.645  21.443 128.332  1.00 54.43           C  
-ATOM   7750  OD1 ASP D 283      -4.652  20.744 128.643  1.00 56.47           O  
-ATOM   7751  OD2 ASP D 283      -5.921  22.437 129.044  1.00 57.29           O  
-ATOM   7752  N   ASP D 284      -9.066  20.113 127.161  1.00 51.33           N  
-ATOM   7753  CA  ASP D 284     -10.485  19.886 127.424  1.00 50.94           C  
-ATOM   7754  C   ASP D 284     -11.335  19.810 126.144  1.00 49.74           C  
-ATOM   7755  O   ASP D 284     -12.462  19.304 126.164  1.00 49.62           O  
-ATOM   7756  CB  ASP D 284     -11.022  20.969 128.375  1.00 51.61           C  
-ATOM   7757  CG  ASP D 284      -9.952  21.498 129.340  1.00 53.85           C  
-ATOM   7758  OD1 ASP D 284      -9.182  20.681 129.906  1.00 55.98           O  
-ATOM   7759  OD2 ASP D 284      -9.811  22.719 129.597  1.00 55.87           O  
-ATOM   7760  N   THR D 285     -10.770  20.287 125.037  1.00 48.30           N  
-ATOM   7761  CA  THR D 285     -11.498  20.495 123.777  1.00 46.57           C  
-ATOM   7762  C   THR D 285     -12.334  19.293 123.301  1.00 44.59           C  
-ATOM   7763  O   THR D 285     -13.562  19.366 123.193  1.00 44.83           O  
-ATOM   7764  CB  THR D 285     -10.514  20.954 122.659  1.00 46.92           C  
-ATOM   7765  OG1 THR D 285      -9.205  20.413 122.903  1.00 47.97           O  
-ATOM   7766  CG2 THR D 285     -10.282  22.459 122.724  1.00 47.14           C  
-ATOM   7767  N   TYR D 286     -11.669  18.178 123.052  1.00 41.73           N  
-ATOM   7768  CA  TYR D 286     -12.323  17.049 122.413  1.00 38.87           C  
-ATOM   7769  C   TYR D 286     -12.519  15.871 123.359  1.00 37.95           C  
-ATOM   7770  O   TYR D 286     -11.877  15.791 124.401  1.00 37.76           O  
-ATOM   7771  CB  TYR D 286     -11.516  16.643 121.179  1.00 38.04           C  
-ATOM   7772  CG  TYR D 286     -11.198  17.809 120.263  1.00 34.08           C  
-ATOM   7773  CD1 TYR D 286     -12.220  18.545 119.659  1.00 30.39           C  
-ATOM   7774  CD2 TYR D 286      -9.881  18.180 120.005  1.00 31.66           C  
-ATOM   7775  CE1 TYR D 286     -11.938  19.619 118.817  1.00 29.03           C  
-ATOM   7776  CE2 TYR D 286      -9.585  19.253 119.163  1.00 29.34           C  
-ATOM   7777  CZ  TYR D 286     -10.623  19.967 118.575  1.00 28.59           C  
-ATOM   7778  OH  TYR D 286     -10.357  21.020 117.735  1.00 28.02           O  
-ATOM   7779  N   THR D 287     -13.422  14.968 122.994  1.00 36.76           N  
-ATOM   7780  CA  THR D 287     -13.599  13.725 123.734  1.00 35.95           C  
-ATOM   7781  C   THR D 287     -12.713  12.650 123.127  1.00 35.22           C  
-ATOM   7782  O   THR D 287     -12.159  12.829 122.039  1.00 34.92           O  
-ATOM   7783  CB  THR D 287     -15.062  13.265 123.712  1.00 35.94           C  
-ATOM   7784  OG1 THR D 287     -15.449  12.980 122.364  1.00 36.76           O  
-ATOM   7785  CG2 THR D 287     -15.998  14.402 124.122  1.00 36.55           C  
-ATOM   7786  N   LYS D 288     -12.581  11.539 123.844  1.00 34.09           N  
-ATOM   7787  CA  LYS D 288     -11.835  10.391 123.373  1.00 33.19           C  
-ATOM   7788  C   LYS D 288     -12.514   9.769 122.147  1.00 32.65           C  
-ATOM   7789  O   LYS D 288     -11.837   9.351 121.203  1.00 32.34           O  
-ATOM   7790  CB  LYS D 288     -11.710   9.368 124.500  1.00 33.05           C  
-ATOM   7791  CG  LYS D 288     -10.614   8.341 124.310  1.00 33.51           C  
-ATOM   7792  CD  LYS D 288     -10.843   7.165 125.247  1.00 34.51           C  
-ATOM   7793  CE  LYS D 288      -9.611   6.298 125.371  1.00 35.73           C  
-ATOM   7794  NZ  LYS D 288      -9.796   5.255 126.416  1.00 37.75           N  
-ATOM   7795  N   LYS D 289     -13.846   9.713 122.163  1.00 31.94           N  
-ATOM   7796  CA  LYS D 289     -14.598   9.151 121.038  1.00 31.64           C  
-ATOM   7797  C   LYS D 289     -14.352   9.954 119.759  1.00 30.43           C  
-ATOM   7798  O   LYS D 289     -14.199   9.372 118.687  1.00 30.35           O  
-ATOM   7799  CB  LYS D 289     -16.100   9.070 121.343  1.00 31.87           C  
-ATOM   7800  CG  LYS D 289     -16.903   8.180 120.379  1.00 34.52           C  
-ATOM   7801  CD  LYS D 289     -16.706   6.680 120.678  1.00 37.93           C  
-ATOM   7802  CE  LYS D 289     -17.967   5.866 120.373  1.00 40.44           C  
-ATOM   7803  NZ  LYS D 289     -17.792   4.376 120.544  1.00 39.73           N  
-ATOM   7804  N   GLN D 290     -14.302  11.281 119.889  1.00 29.03           N  
-ATOM   7805  CA  GLN D 290     -14.021  12.173 118.759  1.00 27.79           C  
-ATOM   7806  C   GLN D 290     -12.639  11.906 118.153  1.00 26.66           C  
-ATOM   7807  O   GLN D 290     -12.498  11.831 116.931  1.00 25.31           O  
-ATOM   7808  CB  GLN D 290     -14.146  13.643 119.175  1.00 28.17           C  
-ATOM   7809  CG  GLN D 290     -15.585  14.127 119.377  1.00 28.47           C  
-ATOM   7810  CD  GLN D 290     -15.650  15.549 119.901  1.00 30.30           C  
-ATOM   7811  OE1 GLN D 290     -15.143  15.835 120.985  1.00 32.03           O  
-ATOM   7812  NE2 GLN D 290     -16.263  16.448 119.129  1.00 30.60           N  
-ATOM   7813  N   VAL D 291     -11.629  11.749 119.011  1.00 25.57           N  
-ATOM   7814  CA  VAL D 291     -10.268  11.447 118.547  1.00 25.01           C  
-ATOM   7815  C   VAL D 291     -10.227  10.110 117.796  1.00 24.60           C  
-ATOM   7816  O   VAL D 291      -9.676  10.018 116.685  1.00 24.11           O  
-ATOM   7817  CB  VAL D 291      -9.252  11.464 119.712  1.00 25.12           C  
-ATOM   7818  CG1 VAL D 291      -7.862  10.988 119.239  1.00 24.93           C  
-ATOM   7819  CG2 VAL D 291      -9.176  12.875 120.338  1.00 24.79           C  
-ATOM   7820  N   LEU D 292     -10.849   9.095 118.396  1.00 24.13           N  
-ATOM   7821  CA  LEU D 292     -10.950   7.762 117.795  1.00 24.13           C  
-ATOM   7822  C   LEU D 292     -11.709   7.765 116.470  1.00 23.46           C  
-ATOM   7823  O   LEU D 292     -11.253   7.170 115.498  1.00 23.40           O  
-ATOM   7824  CB  LEU D 292     -11.601   6.779 118.768  1.00 23.90           C  
-ATOM   7825  CG  LEU D 292     -10.739   5.816 119.588  1.00 25.44           C  
-ATOM   7826  CD1 LEU D 292      -9.347   6.333 119.841  1.00 25.29           C  
-ATOM   7827  CD2 LEU D 292     -11.441   5.522 120.912  1.00 26.85           C  
-ATOM   7828  N   ARG D 293     -12.854   8.432 116.429  1.00 23.34           N  
-ATOM   7829  CA  ARG D 293     -13.617   8.530 115.183  1.00 24.22           C  
-ATOM   7830  C   ARG D 293     -12.870   9.300 114.079  1.00 23.61           C  
-ATOM   7831  O   ARG D 293     -12.936   8.924 112.902  1.00 23.55           O  
-ATOM   7832  CB  ARG D 293     -15.006   9.119 115.433  1.00 24.83           C  
-ATOM   7833  CG  ARG D 293     -15.966   8.138 116.123  1.00 28.10           C  
-ATOM   7834  CD  ARG D 293     -17.432   8.338 115.757  1.00 34.91           C  
-ATOM   7835  NE  ARG D 293     -17.638   8.100 114.327  1.00 40.16           N  
-ATOM   7836  CZ  ARG D 293     -18.018   6.942 113.803  1.00 43.23           C  
-ATOM   7837  NH1 ARG D 293     -18.266   5.892 114.585  1.00 45.72           N  
-ATOM   7838  NH2 ARG D 293     -18.160   6.828 112.490  1.00 45.58           N  
-ATOM   7839  N   MET D 294     -12.153  10.358 114.465  1.00 23.13           N  
-ATOM   7840  CA  MET D 294     -11.339  11.130 113.518  1.00 23.01           C  
-ATOM   7841  C   MET D 294     -10.166  10.324 113.009  1.00 22.44           C  
-ATOM   7842  O   MET D 294      -9.801  10.442 111.847  1.00 22.91           O  
-ATOM   7843  CB  MET D 294     -10.842  12.456 114.110  1.00 22.58           C  
-ATOM   7844  CG  MET D 294      -9.964  13.279 113.147  1.00 22.79           C  
-ATOM   7845  SD  MET D 294     -10.849  13.945 111.708  1.00 23.85           S  
-ATOM   7846  CE  MET D 294     -11.744  15.275 112.523  1.00 20.66           C  
-ATOM   7847  N   GLU D 295      -9.579   9.505 113.873  1.00 22.28           N  
-ATOM   7848  CA  GLU D 295      -8.490   8.622 113.450  1.00 22.04           C  
-ATOM   7849  C   GLU D 295      -8.928   7.764 112.265  1.00 22.35           C  
-ATOM   7850  O   GLU D 295      -8.193   7.613 111.285  1.00 22.28           O  
-ATOM   7851  CB  GLU D 295      -8.027   7.711 114.589  1.00 21.75           C  
-ATOM   7852  CG  GLU D 295      -6.939   6.739 114.151  1.00 20.49           C  
-ATOM   7853  CD  GLU D 295      -6.616   5.684 115.185  1.00 20.66           C  
-ATOM   7854  OE1 GLU D 295      -7.532   4.923 115.569  1.00 19.80           O  
-ATOM   7855  OE2 GLU D 295      -5.442   5.597 115.598  1.00 21.01           O  
-ATOM   7856  N   HIS D 296     -10.130   7.208 112.376  1.00 22.21           N  
-ATOM   7857  CA  HIS D 296     -10.672   6.348 111.349  1.00 22.62           C  
-ATOM   7858  C   HIS D 296     -11.027   7.133 110.089  1.00 22.23           C  
-ATOM   7859  O   HIS D 296     -10.749   6.684 108.979  1.00 22.35           O  
-ATOM   7860  CB  HIS D 296     -11.882   5.568 111.880  1.00 23.16           C  
-ATOM   7861  CG  HIS D 296     -12.167   4.306 111.121  1.00 24.79           C  
-ATOM   7862  ND1 HIS D 296     -13.207   3.462 111.445  1.00 26.70           N  
-ATOM   7863  CD2 HIS D 296     -11.565   3.760 110.037  1.00 26.52           C  
-ATOM   7864  CE1 HIS D 296     -13.225   2.442 110.606  1.00 27.13           C  
-ATOM   7865  NE2 HIS D 296     -12.240   2.600 109.740  1.00 29.02           N  
-ATOM   7866  N   LEU D 297     -11.632   8.305 110.259  1.00 21.98           N  
-ATOM   7867  CA  LEU D 297     -11.926   9.172 109.120  1.00 21.42           C  
-ATOM   7868  C   LEU D 297     -10.649   9.576 108.368  1.00 21.52           C  
-ATOM   7869  O   LEU D 297     -10.638   9.599 107.134  1.00 20.90           O  
-ATOM   7870  CB  LEU D 297     -12.723  10.406 109.547  1.00 21.20           C  
-ATOM   7871  CG  LEU D 297     -13.074  11.428 108.453  1.00 21.19           C  
-ATOM   7872  CD1 LEU D 297     -13.885  10.798 107.309  1.00 21.13           C  
-ATOM   7873  CD2 LEU D 297     -13.835  12.603 109.051  1.00 20.76           C  
-ATOM   7874  N   VAL D 298      -9.580   9.882 109.105  1.00 21.33           N  
-ATOM   7875  CA  VAL D 298      -8.307  10.241 108.465  1.00 21.49           C  
-ATOM   7876  C   VAL D 298      -7.734   9.076 107.650  1.00 21.84           C  
-ATOM   7877  O   VAL D 298      -7.220   9.278 106.548  1.00 21.78           O  
-ATOM   7878  CB  VAL D 298      -7.259  10.779 109.476  1.00 21.19           C  
-ATOM   7879  CG1 VAL D 298      -5.884  10.942 108.822  1.00 20.35           C  
-ATOM   7880  CG2 VAL D 298      -7.713  12.103 110.066  1.00 20.55           C  
-ATOM   7881  N   LEU D 299      -7.823   7.863 108.192  1.00 22.46           N  
-ATOM   7882  CA  LEU D 299      -7.363   6.667 107.475  1.00 22.95           C  
-ATOM   7883  C   LEU D 299      -8.144   6.453 106.192  1.00 23.17           C  
-ATOM   7884  O   LEU D 299      -7.563   6.122 105.174  1.00 23.62           O  
-ATOM   7885  CB  LEU D 299      -7.469   5.412 108.341  1.00 22.65           C  
-ATOM   7886  CG  LEU D 299      -6.389   5.271 109.410  1.00 22.97           C  
-ATOM   7887  CD1 LEU D 299      -6.822   4.232 110.448  1.00 21.85           C  
-ATOM   7888  CD2 LEU D 299      -5.037   4.921 108.789  1.00 21.21           C  
-ATOM   7889  N   LYS D 300      -9.456   6.642 106.258  1.00 23.50           N  
-ATOM   7890  CA  LYS D 300     -10.329   6.490 105.097  1.00 24.37           C  
-ATOM   7891  C   LYS D 300     -10.048   7.537 104.018  1.00 24.16           C  
-ATOM   7892  O   LYS D 300      -9.977   7.200 102.838  1.00 24.47           O  
-ATOM   7893  CB  LYS D 300     -11.806   6.550 105.513  1.00 24.22           C  
-ATOM   7894  CG  LYS D 300     -12.303   5.292 106.208  1.00 25.88           C  
-ATOM   7895  CD  LYS D 300     -13.813   5.339 106.389  1.00 29.17           C  
-ATOM   7896  CE  LYS D 300     -14.242   4.787 107.734  1.00 31.92           C  
-ATOM   7897  NZ  LYS D 300     -14.901   5.846 108.572  1.00 35.50           N  
-ATOM   7898  N   VAL D 301      -9.886   8.793 104.428  1.00 23.75           N  
-ATOM   7899  CA  VAL D 301      -9.568   9.879 103.501  1.00 23.74           C  
-ATOM   7900  C   VAL D 301      -8.235   9.630 102.805  1.00 24.14           C  
-ATOM   7901  O   VAL D 301      -8.137   9.788 101.602  1.00 24.60           O  
-ATOM   7902  CB  VAL D 301      -9.592  11.279 104.203  1.00 23.54           C  
-ATOM   7903  CG1 VAL D 301      -8.948  12.360 103.334  1.00 22.96           C  
-ATOM   7904  CG2 VAL D 301     -11.020  11.669 104.537  1.00 22.87           C  
-ATOM   7905  N   LEU D 302      -7.223   9.214 103.563  1.00 24.99           N  
-ATOM   7906  CA  LEU D 302      -5.886   8.954 103.018  1.00 25.21           C  
-ATOM   7907  C   LEU D 302      -5.769   7.571 102.383  1.00 25.56           C  
-ATOM   7908  O   LEU D 302      -4.708   7.203 101.875  1.00 26.13           O  
-ATOM   7909  CB  LEU D 302      -4.821   9.122 104.117  1.00 25.21           C  
-ATOM   7910  CG  LEU D 302      -4.704  10.487 104.801  1.00 25.19           C  
-ATOM   7911  CD1 LEU D 302      -3.569  10.499 105.831  1.00 25.09           C  
-ATOM   7912  CD2 LEU D 302      -4.502  11.602 103.781  1.00 24.59           C  
-ATOM   7913  N   THR D 303      -6.876   6.832 102.391  1.00 26.19           N  
-ATOM   7914  CA  THR D 303      -6.953   5.432 101.955  1.00 26.63           C  
-ATOM   7915  C   THR D 303      -5.793   4.581 102.466  1.00 26.46           C  
-ATOM   7916  O   THR D 303      -5.208   3.799 101.708  1.00 26.33           O  
-ATOM   7917  CB  THR D 303      -7.095   5.313 100.410  1.00 26.84           C  
-ATOM   7918  OG1 THR D 303      -5.968   5.927  99.771  1.00 28.56           O  
-ATOM   7919  CG2 THR D 303      -8.271   6.109  99.917  1.00 26.02           C  
-ATOM   7920  N   PHE D 304      -5.479   4.749 103.754  1.00 26.12           N  
-ATOM   7921  CA  PHE D 304      -4.426   4.008 104.456  1.00 26.14           C  
-ATOM   7922  C   PHE D 304      -3.006   4.218 103.930  1.00 26.46           C  
-ATOM   7923  O   PHE D 304      -2.119   3.445 104.271  1.00 26.21           O  
-ATOM   7924  CB  PHE D 304      -4.728   2.508 104.469  1.00 26.29           C  
-ATOM   7925  CG  PHE D 304      -5.524   2.055 105.648  1.00 25.69           C  
-ATOM   7926  CD1 PHE D 304      -4.899   1.718 106.846  1.00 26.50           C  
-ATOM   7927  CD2 PHE D 304      -6.896   1.938 105.556  1.00 25.84           C  
-ATOM   7928  CE1 PHE D 304      -5.645   1.278 107.931  1.00 26.02           C  
-ATOM   7929  CE2 PHE D 304      -7.644   1.500 106.636  1.00 26.90           C  
-ATOM   7930  CZ  PHE D 304      -7.024   1.176 107.820  1.00 25.47           C  
-ATOM   7931  N   ASP D 305      -2.792   5.258 103.122  1.00 26.77           N  
-ATOM   7932  CA  ASP D 305      -1.490   5.506 102.505  1.00 27.31           C  
-ATOM   7933  C   ASP D 305      -0.608   6.353 103.415  1.00 27.33           C  
-ATOM   7934  O   ASP D 305      -0.503   7.570 103.247  1.00 27.12           O  
-ATOM   7935  CB  ASP D 305      -1.652   6.165 101.123  1.00 27.64           C  
-ATOM   7936  CG  ASP D 305      -2.442   5.298 100.141  1.00 28.61           C  
-ATOM   7937  OD1 ASP D 305      -2.048   4.137  99.898  1.00 29.64           O  
-ATOM   7938  OD2 ASP D 305      -3.471   5.698  99.558  1.00 30.85           O  
-ATOM   7939  N   LEU D 306       0.040   5.692 104.371  1.00 27.79           N  
-ATOM   7940  CA  LEU D 306       0.724   6.384 105.459  1.00 27.78           C  
-ATOM   7941  C   LEU D 306       2.236   6.429 105.344  1.00 27.83           C  
-ATOM   7942  O   LEU D 306       2.877   7.245 106.009  1.00 27.84           O  
-ATOM   7943  CB  LEU D 306       0.321   5.777 106.809  1.00 28.19           C  
-ATOM   7944  CG  LEU D 306      -1.151   5.914 107.232  1.00 28.76           C  
-ATOM   7945  CD1 LEU D 306      -1.297   5.565 108.697  1.00 28.87           C  
-ATOM   7946  CD2 LEU D 306      -1.723   7.308 106.962  1.00 29.87           C  
-ATOM   7947  N   ALA D 307       2.800   5.563 104.502  1.00 28.09           N  
-ATOM   7948  CA  ALA D 307       4.245   5.455 104.335  1.00 28.48           C  
-ATOM   7949  C   ALA D 307       4.810   6.566 103.453  1.00 29.09           C  
-ATOM   7950  O   ALA D 307       5.473   6.292 102.456  1.00 29.38           O  
-ATOM   7951  CB  ALA D 307       4.610   4.084 103.772  1.00 28.31           C  
-ATOM   7952  N   ALA D 308       4.547   7.816 103.832  1.00 29.70           N  
-ATOM   7953  CA  ALA D 308       4.981   8.986 103.069  1.00 30.10           C  
-ATOM   7954  C   ALA D 308       6.460   9.299 103.276  1.00 30.48           C  
-ATOM   7955  O   ALA D 308       6.979   9.196 104.400  1.00 30.70           O  
-ATOM   7956  CB  ALA D 308       4.136  10.189 103.444  1.00 30.46           C  
-ATOM   7957  N   PRO D 309       7.153   9.680 102.204  1.00 30.88           N  
-ATOM   7958  CA  PRO D 309       8.535  10.157 102.335  1.00 30.95           C  
-ATOM   7959  C   PRO D 309       8.540  11.562 102.929  1.00 31.37           C  
-ATOM   7960  O   PRO D 309       7.670  12.371 102.612  1.00 31.17           O  
-ATOM   7961  CB  PRO D 309       9.045  10.174 100.888  1.00 31.25           C  
-ATOM   7962  CG  PRO D 309       7.970   9.478 100.073  1.00 30.78           C  
-ATOM   7963  CD  PRO D 309       6.694   9.688 100.800  1.00 30.81           C  
-ATOM   7964  N   THR D 310       9.505  11.837 103.798  1.00 32.04           N  
-ATOM   7965  CA  THR D 310       9.566  13.107 104.512  1.00 32.62           C  
-ATOM   7966  C   THR D 310      10.901  13.789 104.252  1.00 33.29           C  
-ATOM   7967  O   THR D 310      11.820  13.176 103.719  1.00 33.62           O  
-ATOM   7968  CB  THR D 310       9.435  12.870 106.030  1.00 32.50           C  
-ATOM   7969  OG1 THR D 310      10.433  11.930 106.446  1.00 31.61           O  
-ATOM   7970  CG2 THR D 310       8.093  12.184 106.392  1.00 32.68           C  
-ATOM   7971  N   VAL D 311      11.012  15.045 104.676  1.00 34.30           N  
-ATOM   7972  CA  VAL D 311      12.268  15.791 104.612  1.00 34.90           C  
-ATOM   7973  C   VAL D 311      13.359  15.087 105.420  1.00 35.64           C  
-ATOM   7974  O   VAL D 311      14.501  14.978 104.974  1.00 35.70           O  
-ATOM   7975  CB  VAL D 311      12.070  17.255 105.092  1.00 34.91           C  
-ATOM   7976  CG1 VAL D 311      13.408  17.965 105.291  1.00 34.30           C  
-ATOM   7977  CG2 VAL D 311      11.197  18.024 104.104  1.00 34.10           C  
-ATOM   7978  N   ASN D 312      12.985  14.600 106.601  1.00 36.42           N  
-ATOM   7979  CA  ASN D 312      13.895  13.903 107.504  1.00 37.09           C  
-ATOM   7980  C   ASN D 312      14.469  12.640 106.854  1.00 37.27           C  
-ATOM   7981  O   ASN D 312      15.657  12.325 107.021  1.00 37.03           O  
-ATOM   7982  CB  ASN D 312      13.165  13.604 108.825  1.00 37.31           C  
-ATOM   7983  CG  ASN D 312      13.921  12.646 109.726  1.00 38.92           C  
-ATOM   7984  OD1 ASN D 312      14.852  13.033 110.430  1.00 40.88           O  
-ATOM   7985  ND2 ASN D 312      13.499  11.387 109.731  1.00 40.51           N  
-ATOM   7986  N   GLN D 313      13.623  11.948 106.090  1.00 37.35           N  
-ATOM   7987  CA  GLN D 313      13.999  10.712 105.405  1.00 37.46           C  
-ATOM   7988  C   GLN D 313      15.106  10.939 104.381  1.00 37.52           C  
-ATOM   7989  O   GLN D 313      16.039  10.132 104.285  1.00 37.49           O  
-ATOM   7990  CB  GLN D 313      12.776  10.060 104.740  1.00 37.38           C  
-ATOM   7991  CG  GLN D 313      12.007   9.102 105.648  1.00 37.59           C  
-ATOM   7992  CD  GLN D 313      10.803   8.475 104.965  1.00 37.13           C  
-ATOM   7993  OE1 GLN D 313      10.955   7.690 104.033  1.00 38.22           O  
-ATOM   7994  NE2 GLN D 313       9.610   8.813 105.433  1.00 36.37           N  
-ATOM   7995  N   PHE D 314      14.995  12.030 103.620  1.00 37.64           N  
-ATOM   7996  CA  PHE D 314      16.046  12.426 102.676  1.00 37.76           C  
-ATOM   7997  C   PHE D 314      17.295  12.960 103.391  1.00 38.40           C  
-ATOM   7998  O   PHE D 314      18.411  12.564 103.054  1.00 38.91           O  
-ATOM   7999  CB  PHE D 314      15.517  13.420 101.641  1.00 37.29           C  
-ATOM   8000  CG  PHE D 314      14.563  12.812 100.645  1.00 36.01           C  
-ATOM   8001  CD1 PHE D 314      15.032  11.978  99.626  1.00 35.21           C  
-ATOM   8002  CD2 PHE D 314      13.200  13.074 100.720  1.00 34.49           C  
-ATOM   8003  CE1 PHE D 314      14.152  11.407  98.702  1.00 34.06           C  
-ATOM   8004  CE2 PHE D 314      12.311  12.512  99.802  1.00 34.39           C  
-ATOM   8005  CZ  PHE D 314      12.789  11.677  98.791  1.00 34.58           C  
-ATOM   8006  N   LEU D 315      17.107  13.824 104.393  1.00 38.73           N  
-ATOM   8007  CA  LEU D 315      18.224  14.385 105.167  1.00 39.06           C  
-ATOM   8008  C   LEU D 315      19.105  13.313 105.799  1.00 39.72           C  
-ATOM   8009  O   LEU D 315      20.322  13.475 105.895  1.00 39.53           O  
-ATOM   8010  CB  LEU D 315      17.718  15.317 106.272  1.00 38.90           C  
-ATOM   8011  CG  LEU D 315      17.408  16.783 105.958  1.00 38.79           C  
-ATOM   8012  CD1 LEU D 315      16.736  17.422 107.155  1.00 38.25           C  
-ATOM   8013  CD2 LEU D 315      18.667  17.562 105.578  1.00 39.40           C  
-ATOM   8014  N   THR D 316      18.476  12.227 106.242  1.00 40.36           N  
-ATOM   8015  CA  THR D 316      19.167  11.123 106.898  1.00 40.98           C  
-ATOM   8016  C   THR D 316      20.121  10.433 105.915  1.00 41.34           C  
-ATOM   8017  O   THR D 316      21.217  10.015 106.286  1.00 41.23           O  
-ATOM   8018  CB  THR D 316      18.122  10.140 107.500  1.00 40.99           C  
-ATOM   8019  OG1 THR D 316      17.490  10.759 108.632  1.00 41.23           O  
-ATOM   8020  CG2 THR D 316      18.790   8.952 108.130  1.00 41.50           C  
-ATOM   8021  N   GLN D 317      19.696  10.342 104.659  1.00 42.01           N  
-ATOM   8022  CA  GLN D 317      20.535   9.819 103.592  1.00 42.91           C  
-ATOM   8023  C   GLN D 317      21.649  10.802 103.238  1.00 43.34           C  
-ATOM   8024  O   GLN D 317      22.781  10.389 102.958  1.00 43.54           O  
-ATOM   8025  CB  GLN D 317      19.702   9.526 102.351  1.00 42.99           C  
-ATOM   8026  CG  GLN D 317      18.748   8.363 102.506  1.00 44.10           C  
-ATOM   8027  CD  GLN D 317      17.721   8.338 101.407  1.00 45.29           C  
-ATOM   8028  OE1 GLN D 317      16.686   9.008 101.505  1.00 46.29           O  
-ATOM   8029  NE2 GLN D 317      18.002   7.584 100.345  1.00 45.68           N  
-ATOM   8030  N   TYR D 318      21.327  12.096 103.260  1.00 43.54           N  
-ATOM   8031  CA  TYR D 318      22.282  13.130 102.867  1.00 43.86           C  
-ATOM   8032  C   TYR D 318      23.457  13.209 103.844  1.00 45.29           C  
-ATOM   8033  O   TYR D 318      24.599  13.443 103.435  1.00 45.51           O  
-ATOM   8034  CB  TYR D 318      21.595  14.497 102.740  1.00 43.10           C  
-ATOM   8035  CG  TYR D 318      20.563  14.631 101.629  1.00 39.63           C  
-ATOM   8036  CD1 TYR D 318      20.354  13.617 100.691  1.00 36.59           C  
-ATOM   8037  CD2 TYR D 318      19.794  15.791 101.517  1.00 37.12           C  
-ATOM   8038  CE1 TYR D 318      19.392  13.759  99.677  1.00 34.54           C  
-ATOM   8039  CE2 TYR D 318      18.846  15.938 100.512  1.00 34.35           C  
-ATOM   8040  CZ  TYR D 318      18.651  14.928  99.599  1.00 33.31           C  
-ATOM   8041  OH  TYR D 318      17.700  15.093  98.623  1.00 33.34           O  
-ATOM   8042  N   PHE D 319      23.168  12.992 105.127  1.00 46.70           N  
-ATOM   8043  CA  PHE D 319      24.165  13.054 106.195  1.00 48.27           C  
-ATOM   8044  C   PHE D 319      25.306  12.054 106.015  1.00 49.83           C  
-ATOM   8045  O   PHE D 319      26.406  12.253 106.544  1.00 49.96           O  
-ATOM   8046  CB  PHE D 319      23.502  12.834 107.558  1.00 48.19           C  
-ATOM   8047  CG  PHE D 319      22.562  13.941 107.978  1.00 47.95           C  
-ATOM   8048  CD1 PHE D 319      22.517  15.156 107.289  1.00 47.47           C  
-ATOM   8049  CD2 PHE D 319      21.718  13.764 109.071  1.00 47.62           C  
-ATOM   8050  CE1 PHE D 319      21.642  16.169 107.679  1.00 47.09           C  
-ATOM   8051  CE2 PHE D 319      20.846  14.773 109.474  1.00 47.13           C  
-ATOM   8052  CZ  PHE D 319      20.806  15.977 108.773  1.00 47.30           C  
-ATOM   8053  N   LEU D 320      25.037  10.982 105.268  1.00 51.50           N  
-ATOM   8054  CA  LEU D 320      26.030   9.946 104.985  1.00 53.06           C  
-ATOM   8055  C   LEU D 320      27.153  10.433 104.059  1.00 54.45           C  
-ATOM   8056  O   LEU D 320      28.199   9.787 103.949  1.00 54.70           O  
-ATOM   8057  CB  LEU D 320      25.342   8.716 104.381  1.00 53.07           C  
-ATOM   8058  CG  LEU D 320      25.018   7.500 105.259  1.00 52.26           C  
-ATOM   8059  CD1 LEU D 320      24.551   7.887 106.651  1.00 51.74           C  
-ATOM   8060  CD2 LEU D 320      23.977   6.651 104.569  1.00 51.89           C  
-ATOM   8061  N   HIS D 321      26.930  11.570 103.400  1.00 55.94           N  
-ATOM   8062  CA  HIS D 321      27.920  12.172 102.508  1.00 57.49           C  
-ATOM   8063  C   HIS D 321      28.679  13.308 103.202  1.00 58.35           C  
-ATOM   8064  O   HIS D 321      29.097  14.272 102.556  1.00 58.46           O  
-ATOM   8065  CB  HIS D 321      27.250  12.682 101.225  1.00 57.53           C  
-ATOM   8066  CG  HIS D 321      26.690  11.598 100.355  1.00 58.50           C  
-ATOM   8067  ND1 HIS D 321      26.613  11.714  98.984  1.00 58.83           N  
-ATOM   8068  CD2 HIS D 321      26.171  10.383 100.659  1.00 59.05           C  
-ATOM   8069  CE1 HIS D 321      26.075  10.617  98.480  1.00 59.09           C  
-ATOM   8070  NE2 HIS D 321      25.798   9.793  99.474  1.00 59.40           N  
-ATOM   8071  N   GLN D 322      28.838  13.180 104.521  1.00 59.46           N  
-ATOM   8072  CA  GLN D 322      29.598  14.122 105.341  1.00 60.36           C  
-ATOM   8073  C   GLN D 322      31.040  13.663 105.434  1.00 60.89           C  
-ATOM   8074  O   GLN D 322      31.316  12.464 105.385  1.00 61.09           O  
-ATOM   8075  CB  GLN D 322      29.021  14.188 106.755  1.00 60.42           C  
-ATOM   8076  CG  GLN D 322      28.175  15.418 107.063  1.00 60.85           C  
-ATOM   8077  CD  GLN D 322      27.550  15.357 108.452  1.00 61.15           C  
-ATOM   8078  OE1 GLN D 322      27.766  16.247 109.275  1.00 61.02           O  
-ATOM   8079  NE2 GLN D 322      26.777  14.307 108.711  1.00 61.22           N  
-ATOM   8080  N   GLN D 323      31.954  14.619 105.586  1.00 61.61           N  
-ATOM   8081  CA  GLN D 323      33.383  14.325 105.678  1.00 62.12           C  
-ATOM   8082  C   GLN D 323      34.127  15.319 106.580  1.00 62.13           C  
-ATOM   8083  O   GLN D 323      34.570  16.372 106.112  1.00 62.22           O  
-ATOM   8084  CB  GLN D 323      34.017  14.287 104.281  1.00 62.30           C  
-ATOM   8085  CG  GLN D 323      33.818  12.974 103.523  1.00 63.35           C  
-ATOM   8086  CD  GLN D 323      34.519  11.790 104.175  1.00 64.91           C  
-ATOM   8087  OE1 GLN D 323      35.603  11.933 104.742  1.00 65.20           O  
-ATOM   8088  NE2 GLN D 323      33.900  10.614 104.091  1.00 65.82           N  
-ATOM   8089  N   PRO D 324      34.243  15.005 107.872  1.00 62.08           N  
-ATOM   8090  CA  PRO D 324      33.574  13.850 108.482  1.00 61.98           C  
-ATOM   8091  C   PRO D 324      32.182  14.228 108.995  1.00 61.66           C  
-ATOM   8092  O   PRO D 324      31.719  15.336 108.717  1.00 61.85           O  
-ATOM   8093  CB  PRO D 324      34.496  13.506 109.651  1.00 61.96           C  
-ATOM   8094  CG  PRO D 324      35.089  14.832 110.061  1.00 62.38           C  
-ATOM   8095  CD  PRO D 324      35.052  15.748 108.855  1.00 62.08           C  
-ATOM   8096  N   ALA D 325      31.533  13.319 109.721  1.00 61.17           N  
-ATOM   8097  CA  ALA D 325      30.239  13.595 110.332  1.00 60.52           C  
-ATOM   8098  C   ALA D 325      30.363  14.702 111.371  1.00 60.10           C  
-ATOM   8099  O   ALA D 325      31.264  14.682 112.214  1.00 59.97           O  
-ATOM   8100  CB  ALA D 325      29.666  12.337 110.963  1.00 60.58           C  
-ATOM   8101  N   ASN D 326      29.460  15.672 111.284  1.00 59.52           N  
-ATOM   8102  CA  ASN D 326      29.399  16.773 112.233  1.00 58.95           C  
-ATOM   8103  C   ASN D 326      28.015  16.849 112.878  1.00 58.48           C  
-ATOM   8104  O   ASN D 326      27.002  16.943 112.186  1.00 58.26           O  
-ATOM   8105  CB  ASN D 326      29.752  18.092 111.543  1.00 59.00           C  
-ATOM   8106  CG  ASN D 326      29.924  19.236 112.521  1.00 59.37           C  
-ATOM   8107  OD1 ASN D 326      28.946  19.795 113.015  1.00 59.34           O  
-ATOM   8108  ND2 ASN D 326      31.174  19.593 112.803  1.00 60.14           N  
-ATOM   8109  N   CYS D 327      27.990  16.808 114.207  1.00 57.95           N  
-ATOM   8110  CA  CYS D 327      26.745  16.786 114.966  1.00 57.41           C  
-ATOM   8111  C   CYS D 327      25.982  18.117 114.913  1.00 56.64           C  
-ATOM   8112  O   CYS D 327      24.747  18.125 114.921  1.00 56.66           O  
-ATOM   8113  CB  CYS D 327      27.009  16.344 116.410  1.00 57.53           C  
-ATOM   8114  SG  CYS D 327      27.346  14.564 116.584  1.00 59.60           S  
-ATOM   8115  N   LYS D 328      26.716  19.229 114.840  1.00 55.49           N  
-ATOM   8116  CA  LYS D 328      26.111  20.558 114.709  1.00 54.44           C  
-ATOM   8117  C   LYS D 328      25.444  20.756 113.344  1.00 53.50           C  
-ATOM   8118  O   LYS D 328      24.406  21.415 113.245  1.00 53.32           O  
-ATOM   8119  CB  LYS D 328      27.147  21.665 114.950  1.00 54.57           C  
-ATOM   8120  CG  LYS D 328      27.695  21.717 116.364  1.00 55.11           C  
-ATOM   8121  CD  LYS D 328      28.228  23.096 116.701  1.00 56.10           C  
-ATOM   8122  CE  LYS D 328      27.369  23.763 117.759  1.00 57.53           C  
-ATOM   8123  NZ  LYS D 328      27.979  25.026 118.260  1.00 59.40           N  
-ATOM   8124  N   VAL D 329      26.047  20.186 112.301  1.00 52.31           N  
-ATOM   8125  CA  VAL D 329      25.508  20.257 110.942  1.00 51.11           C  
-ATOM   8126  C   VAL D 329      24.215  19.447 110.839  1.00 50.38           C  
-ATOM   8127  O   VAL D 329      23.195  19.948 110.349  1.00 50.10           O  
-ATOM   8128  CB  VAL D 329      26.534  19.749 109.892  1.00 51.14           C  
-ATOM   8129  CG1 VAL D 329      25.894  19.599 108.508  1.00 50.86           C  
-ATOM   8130  CG2 VAL D 329      27.737  20.683 109.824  1.00 51.64           C  
-ATOM   8131  N   GLU D 330      24.264  18.200 111.307  1.00 49.28           N  
-ATOM   8132  CA  GLU D 330      23.098  17.321 111.280  1.00 48.36           C  
-ATOM   8133  C   GLU D 330      21.919  17.995 111.978  1.00 47.20           C  
-ATOM   8134  O   GLU D 330      20.868  18.195 111.371  1.00 46.97           O  
-ATOM   8135  CB  GLU D 330      23.422  15.963 111.913  1.00 48.53           C  
-ATOM   8136  CG  GLU D 330      24.352  15.101 111.068  1.00 50.04           C  
-ATOM   8137  CD  GLU D 330      24.505  13.680 111.592  1.00 51.89           C  
-ATOM   8138  OE1 GLU D 330      23.483  13.057 111.968  1.00 52.85           O  
-ATOM   8139  OE2 GLU D 330      25.653  13.178 111.616  1.00 52.36           O  
-ATOM   8140  N   SER D 331      22.123  18.378 113.236  1.00 46.06           N  
-ATOM   8141  CA  SER D 331      21.093  19.037 114.033  1.00 45.12           C  
-ATOM   8142  C   SER D 331      20.553  20.313 113.381  1.00 44.44           C  
-ATOM   8143  O   SER D 331      19.344  20.528 113.361  1.00 44.30           O  
-ATOM   8144  CB  SER D 331      21.615  19.336 115.437  1.00 45.12           C  
-ATOM   8145  OG  SER D 331      21.533  18.183 116.260  1.00 45.11           O  
-ATOM   8146  N   LEU D 332      21.446  21.146 112.843  1.00 43.52           N  
-ATOM   8147  CA  LEU D 332      21.033  22.380 112.171  1.00 42.36           C  
-ATOM   8148  C   LEU D 332      20.178  22.110 110.936  1.00 41.45           C  
-ATOM   8149  O   LEU D 332      19.209  22.823 110.686  1.00 40.92           O  
-ATOM   8150  CB  LEU D 332      22.242  23.263 111.806  1.00 42.44           C  
-ATOM   8151  CG  LEU D 332      21.974  24.643 111.172  1.00 42.12           C  
-ATOM   8152  CD1 LEU D 332      20.871  25.420 111.898  1.00 40.83           C  
-ATOM   8153  CD2 LEU D 332      23.247  25.474 111.114  1.00 41.44           C  
-ATOM   8154  N   ALA D 333      20.538  21.085 110.169  1.00 40.71           N  
-ATOM   8155  CA  ALA D 333      19.754  20.701 108.998  1.00 40.26           C  
-ATOM   8156  C   ALA D 333      18.360  20.187 109.387  1.00 40.09           C  
-ATOM   8157  O   ALA D 333      17.394  20.374 108.642  1.00 39.96           O  
-ATOM   8158  CB  ALA D 333      20.496  19.680 108.172  1.00 40.11           C  
-ATOM   8159  N   MET D 334      18.266  19.551 110.555  1.00 40.00           N  
-ATOM   8160  CA  MET D 334      16.982  19.086 111.086  1.00 40.30           C  
-ATOM   8161  C   MET D 334      16.130  20.278 111.494  1.00 39.54           C  
-ATOM   8162  O   MET D 334      14.943  20.351 111.175  1.00 39.25           O  
-ATOM   8163  CB  MET D 334      17.185  18.168 112.293  1.00 40.70           C  
-ATOM   8164  CG  MET D 334      18.160  17.038 112.045  1.00 43.17           C  
-ATOM   8165  SD  MET D 334      17.381  15.437 112.043  1.00 49.89           S  
-ATOM   8166  CE  MET D 334      16.558  15.477 110.435  1.00 46.12           C  
-ATOM   8167  N   PHE D 335      16.767  21.215 112.186  1.00 38.86           N  
-ATOM   8168  CA  PHE D 335      16.129  22.439 112.643  1.00 38.23           C  
-ATOM   8169  C   PHE D 335      15.454  23.187 111.501  1.00 37.38           C  
-ATOM   8170  O   PHE D 335      14.316  23.631 111.637  1.00 37.21           O  
-ATOM   8171  CB  PHE D 335      17.164  23.328 113.340  1.00 38.32           C  
-ATOM   8172  CG  PHE D 335      16.768  24.777 113.431  1.00 39.19           C  
-ATOM   8173  CD1 PHE D 335      15.761  25.188 114.299  1.00 39.13           C  
-ATOM   8174  CD2 PHE D 335      17.412  25.732 112.653  1.00 39.62           C  
-ATOM   8175  CE1 PHE D 335      15.402  26.523 114.390  1.00 40.13           C  
-ATOM   8176  CE2 PHE D 335      17.058  27.075 112.737  1.00 40.20           C  
-ATOM   8177  CZ  PHE D 335      16.054  27.471 113.609  1.00 39.76           C  
-ATOM   8178  N   LEU D 336      16.158  23.299 110.377  1.00 36.83           N  
-ATOM   8179  CA  LEU D 336      15.685  24.050 109.218  1.00 36.07           C  
-ATOM   8180  C   LEU D 336      14.606  23.299 108.441  1.00 35.70           C  
-ATOM   8181  O   LEU D 336      13.640  23.908 107.958  1.00 35.40           O  
-ATOM   8182  CB  LEU D 336      16.860  24.415 108.300  1.00 36.32           C  
-ATOM   8183  CG  LEU D 336      17.936  25.365 108.851  1.00 36.22           C  
-ATOM   8184  CD1 LEU D 336      19.166  25.344 107.947  1.00 36.02           C  
-ATOM   8185  CD2 LEU D 336      17.404  26.787 109.003  1.00 36.35           C  
-ATOM   8186  N   GLY D 337      14.775  21.980 108.317  1.00 35.19           N  
-ATOM   8187  CA  GLY D 337      13.757  21.130 107.716  1.00 34.36           C  
-ATOM   8188  C   GLY D 337      12.432  21.299 108.440  1.00 34.09           C  
-ATOM   8189  O   GLY D 337      11.368  21.406 107.817  1.00 33.88           O  
-ATOM   8190  N   GLU D 338      12.513  21.372 109.766  1.00 33.52           N  
-ATOM   8191  CA  GLU D 338      11.337  21.496 110.611  1.00 33.15           C  
-ATOM   8192  C   GLU D 338      10.637  22.840 110.483  1.00 32.68           C  
-ATOM   8193  O   GLU D 338       9.412  22.888 110.374  1.00 32.34           O  
-ATOM   8194  CB  GLU D 338      11.715  21.235 112.060  1.00 33.35           C  
-ATOM   8195  CG  GLU D 338      11.455  19.801 112.477  1.00 34.46           C  
-ATOM   8196  CD  GLU D 338      11.652  19.592 113.956  1.00 35.11           C  
-ATOM   8197  OE1 GLU D 338      10.971  20.281 114.753  1.00 35.34           O  
-ATOM   8198  OE2 GLU D 338      12.489  18.740 114.312  1.00 35.49           O  
-ATOM   8199  N   LEU D 339      11.414  23.924 110.488  1.00 32.26           N  
-ATOM   8200  CA  LEU D 339      10.876  25.270 110.306  1.00 31.78           C  
-ATOM   8201  C   LEU D 339      10.017  25.363 109.044  1.00 31.44           C  
-ATOM   8202  O   LEU D 339       9.019  26.074 109.026  1.00 31.37           O  
-ATOM   8203  CB  LEU D 339      12.005  26.311 110.246  1.00 31.98           C  
-ATOM   8204  CG  LEU D 339      12.789  26.708 111.507  1.00 32.61           C  
-ATOM   8205  CD1 LEU D 339      13.761  27.822 111.156  1.00 33.25           C  
-ATOM   8206  CD2 LEU D 339      11.877  27.158 112.640  1.00 32.86           C  
-ATOM   8207  N   SER D 340      10.415  24.640 107.997  1.00 31.24           N  
-ATOM   8208  CA  SER D 340       9.672  24.593 106.738  1.00 31.12           C  
-ATOM   8209  C   SER D 340       8.283  23.971 106.876  1.00 30.83           C  
-ATOM   8210  O   SER D 340       7.411  24.244 106.062  1.00 30.92           O  
-ATOM   8211  CB  SER D 340      10.480  23.873 105.647  1.00 31.59           C  
-ATOM   8212  OG  SER D 340      10.490  22.463 105.829  1.00 31.98           O  
-ATOM   8213  N   LEU D 341       8.069  23.151 107.907  1.00 30.80           N  
-ATOM   8214  CA  LEU D 341       6.737  22.567 108.155  1.00 30.37           C  
-ATOM   8215  C   LEU D 341       5.699  23.603 108.552  1.00 30.65           C  
-ATOM   8216  O   LEU D 341       4.513  23.452 108.241  1.00 30.49           O  
-ATOM   8217  CB  LEU D 341       6.795  21.495 109.238  1.00 30.06           C  
-ATOM   8218  CG  LEU D 341       7.682  20.280 108.987  1.00 29.17           C  
-ATOM   8219  CD1 LEU D 341       7.927  19.606 110.309  1.00 27.67           C  
-ATOM   8220  CD2 LEU D 341       7.040  19.327 107.981  1.00 26.71           C  
-ATOM   8221  N   ILE D 342       6.152  24.646 109.245  1.00 31.04           N  
-ATOM   8222  CA  ILE D 342       5.267  25.665 109.822  1.00 31.90           C  
-ATOM   8223  C   ILE D 342       4.553  26.530 108.772  1.00 32.08           C  
-ATOM   8224  O   ILE D 342       3.393  26.904 108.952  1.00 32.45           O  
-ATOM   8225  CB  ILE D 342       6.060  26.561 110.835  1.00 31.87           C  
-ATOM   8226  CG1 ILE D 342       6.683  25.707 111.949  1.00 31.48           C  
-ATOM   8227  CG2 ILE D 342       5.190  27.705 111.381  1.00 31.80           C  
-ATOM   8228  CD1 ILE D 342       5.753  25.376 113.107  1.00 30.80           C  
-ATOM   8229  N   ASP D 343       5.244  26.839 107.682  1.00 32.54           N  
-ATOM   8230  CA  ASP D 343       4.719  27.784 106.696  1.00 33.24           C  
-ATOM   8231  C   ASP D 343       4.348  27.102 105.386  1.00 33.54           C  
-ATOM   8232  O   ASP D 343       5.221  26.759 104.584  1.00 33.30           O  
-ATOM   8233  CB  ASP D 343       5.722  28.916 106.443  1.00 33.11           C  
-ATOM   8234  CG  ASP D 343       6.115  29.637 107.712  1.00 33.93           C  
-ATOM   8235  OD1 ASP D 343       5.232  30.266 108.335  1.00 35.00           O  
-ATOM   8236  OD2 ASP D 343       7.283  29.634 108.162  1.00 34.75           O  
-ATOM   8237  N   ALA D 344       3.047  26.909 105.184  1.00 34.08           N  
-ATOM   8238  CA  ALA D 344       2.532  26.289 103.966  1.00 34.97           C  
-ATOM   8239  C   ALA D 344       2.963  27.103 102.745  1.00 35.42           C  
-ATOM   8240  O   ALA D 344       3.370  26.549 101.722  1.00 35.35           O  
-ATOM   8241  CB  ALA D 344       1.019  26.167 104.032  1.00 34.81           C  
-ATOM   8242  N   ASP D 345       2.877  28.423 102.880  1.00 35.98           N  
-ATOM   8243  CA  ASP D 345       3.421  29.358 101.912  1.00 36.59           C  
-ATOM   8244  C   ASP D 345       4.800  29.769 102.433  1.00 36.54           C  
-ATOM   8245  O   ASP D 345       4.886  30.402 103.482  1.00 36.70           O  
-ATOM   8246  CB  ASP D 345       2.491  30.574 101.815  1.00 36.96           C  
-ATOM   8247  CG  ASP D 345       2.848  31.522 100.670  1.00 38.49           C  
-ATOM   8248  OD1 ASP D 345       4.038  31.642 100.299  1.00 38.72           O  
-ATOM   8249  OD2 ASP D 345       1.978  32.212 100.091  1.00 41.78           O  
-ATOM   8250  N   PRO D 346       5.880  29.432 101.720  1.00 36.65           N  
-ATOM   8251  CA  PRO D 346       5.841  28.789 100.402  1.00 36.79           C  
-ATOM   8252  C   PRO D 346       6.156  27.283 100.356  1.00 37.07           C  
-ATOM   8253  O   PRO D 346       6.257  26.738  99.257  1.00 36.98           O  
-ATOM   8254  CB  PRO D 346       6.992  29.494  99.699  1.00 36.68           C  
-ATOM   8255  CG  PRO D 346       8.026  29.619 100.802  1.00 36.70           C  
-ATOM   8256  CD  PRO D 346       7.266  29.737 102.120  1.00 36.32           C  
-ATOM   8257  N   TYR D 347       6.329  26.625 101.495  1.00 37.53           N  
-ATOM   8258  CA  TYR D 347       6.986  25.313 101.488  1.00 38.15           C  
-ATOM   8259  C   TYR D 347       6.203  24.154 100.858  1.00 38.45           C  
-ATOM   8260  O   TYR D 347       6.797  23.167 100.431  1.00 38.34           O  
-ATOM   8261  CB  TYR D 347       7.580  24.995 102.865  1.00 37.95           C  
-ATOM   8262  CG  TYR D 347       8.652  26.005 103.180  1.00 38.75           C  
-ATOM   8263  CD1 TYR D 347       9.847  26.022 102.452  1.00 38.63           C  
-ATOM   8264  CD2 TYR D 347       8.448  26.998 104.143  1.00 38.58           C  
-ATOM   8265  CE1 TYR D 347      10.832  26.975 102.705  1.00 39.38           C  
-ATOM   8266  CE2 TYR D 347       9.425  27.960 104.401  1.00 38.42           C  
-ATOM   8267  CZ  TYR D 347      10.612  27.942 103.674  1.00 39.39           C  
-ATOM   8268  OH  TYR D 347      11.585  28.884 103.915  1.00 39.78           O  
-ATOM   8269  N   LEU D 348       4.889  24.315 100.753  1.00 39.12           N  
-ATOM   8270  CA  LEU D 348       4.021  23.334 100.114  1.00 40.37           C  
-ATOM   8271  C   LEU D 348       4.263  23.135  98.603  1.00 41.30           C  
-ATOM   8272  O   LEU D 348       3.736  22.194  98.014  1.00 41.52           O  
-ATOM   8273  CB  LEU D 348       2.553  23.696 100.364  1.00 40.04           C  
-ATOM   8274  CG  LEU D 348       1.614  22.715 101.086  1.00 40.60           C  
-ATOM   8275  CD1 LEU D 348       2.259  22.044 102.297  1.00 39.60           C  
-ATOM   8276  CD2 LEU D 348       0.337  23.430 101.502  1.00 39.89           C  
-ATOM   8277  N   LYS D 349       5.042  24.013  97.971  1.00 42.38           N  
-ATOM   8278  CA  LYS D 349       5.342  23.842  96.543  1.00 43.33           C  
-ATOM   8279  C   LYS D 349       6.699  23.178  96.310  1.00 43.55           C  
-ATOM   8280  O   LYS D 349       7.058  22.848  95.176  1.00 44.08           O  
-ATOM   8281  CB  LYS D 349       5.186  25.152  95.750  1.00 43.65           C  
-ATOM   8282  CG  LYS D 349       6.098  26.298  96.151  1.00 44.85           C  
-ATOM   8283  CD  LYS D 349       5.390  27.632  95.922  1.00 47.25           C  
-ATOM   8284  CE  LYS D 349       6.349  28.801  96.043  1.00 48.65           C  
-ATOM   8285  NZ  LYS D 349       5.636  30.118  96.098  1.00 50.37           N  
-ATOM   8286  N   TYR D 350       7.444  22.980  97.392  1.00 43.58           N  
-ATOM   8287  CA  TYR D 350       8.703  22.253  97.330  1.00 43.69           C  
-ATOM   8288  C   TYR D 350       8.510  20.808  97.780  1.00 43.36           C  
-ATOM   8289  O   TYR D 350       7.680  20.516  98.649  1.00 43.20           O  
-ATOM   8290  CB  TYR D 350       9.764  22.933  98.196  1.00 43.87           C  
-ATOM   8291  CG  TYR D 350      10.068  24.367  97.818  1.00 45.45           C  
-ATOM   8292  CD1 TYR D 350      10.713  24.672  96.617  1.00 46.79           C  
-ATOM   8293  CD2 TYR D 350       9.720  25.421  98.666  1.00 46.13           C  
-ATOM   8294  CE1 TYR D 350      10.997  25.988  96.269  1.00 48.01           C  
-ATOM   8295  CE2 TYR D 350      10.005  26.740  98.330  1.00 46.73           C  
-ATOM   8296  CZ  TYR D 350      10.641  27.015  97.131  1.00 47.85           C  
-ATOM   8297  OH  TYR D 350      10.926  28.312  96.784  1.00 48.56           O  
-ATOM   8298  N   LEU D 351       9.282  19.911  97.177  1.00 42.69           N  
-ATOM   8299  CA  LEU D 351       9.239  18.502  97.521  1.00 42.20           C  
-ATOM   8300  C   LEU D 351      10.178  18.222  98.685  1.00 41.83           C  
-ATOM   8301  O   LEU D 351      11.198  18.904  98.830  1.00 42.25           O  
-ATOM   8302  CB  LEU D 351       9.611  17.644  96.309  1.00 42.40           C  
-ATOM   8303  CG  LEU D 351       8.548  17.532  95.211  1.00 42.46           C  
-ATOM   8304  CD1 LEU D 351       9.169  17.000  93.926  1.00 42.54           C  
-ATOM   8305  CD2 LEU D 351       7.387  16.649  95.650  1.00 43.46           C  
-ATOM   8306  N   PRO D 352       9.836  17.241  99.525  1.00 41.14           N  
-ATOM   8307  CA  PRO D 352      10.688  16.859 100.655  1.00 40.83           C  
-ATOM   8308  C   PRO D 352      12.165  16.730 100.305  1.00 40.46           C  
-ATOM   8309  O   PRO D 352      13.001  17.125 101.112  1.00 40.27           O  
-ATOM   8310  CB  PRO D 352      10.117  15.498 101.073  1.00 40.87           C  
-ATOM   8311  CG  PRO D 352       8.692  15.581 100.730  1.00 40.37           C  
-ATOM   8312  CD  PRO D 352       8.596  16.441  99.494  1.00 40.89           C  
-ATOM   8313  N   SER D 353      12.473  16.199  99.124  1.00 40.34           N  
-ATOM   8314  CA  SER D 353      13.859  16.011  98.701  1.00 40.22           C  
-ATOM   8315  C   SER D 353      14.572  17.347  98.475  1.00 40.28           C  
-ATOM   8316  O   SER D 353      15.733  17.510  98.856  1.00 40.04           O  
-ATOM   8317  CB  SER D 353      13.916  15.165  97.431  1.00 40.14           C  
-ATOM   8318  OG  SER D 353      13.103  15.728  96.419  1.00 39.24           O  
-ATOM   8319  N   VAL D 354      13.858  18.293  97.868  1.00 40.41           N  
-ATOM   8320  CA  VAL D 354      14.384  19.629  97.599  1.00 40.65           C  
-ATOM   8321  C   VAL D 354      14.616  20.408  98.893  1.00 40.79           C  
-ATOM   8322  O   VAL D 354      15.713  20.929  99.113  1.00 40.96           O  
-ATOM   8323  CB  VAL D 354      13.471  20.417  96.629  1.00 40.82           C  
-ATOM   8324  CG1 VAL D 354      14.033  21.797  96.358  1.00 40.78           C  
-ATOM   8325  CG2 VAL D 354      13.312  19.654  95.318  1.00 40.68           C  
-ATOM   8326  N   ILE D 355      13.597  20.464  99.754  1.00 40.79           N  
-ATOM   8327  CA  ILE D 355      13.715  21.136 101.049  1.00 40.52           C  
-ATOM   8328  C   ILE D 355      14.865  20.544 101.860  1.00 40.88           C  
-ATOM   8329  O   ILE D 355      15.641  21.276 102.486  1.00 40.91           O  
-ATOM   8330  CB  ILE D 355      12.372  21.088 101.835  1.00 40.53           C  
-ATOM   8331  CG1 ILE D 355      11.334  22.002 101.178  1.00 40.34           C  
-ATOM   8332  CG2 ILE D 355      12.570  21.501 103.296  1.00 39.82           C  
-ATOM   8333  CD1 ILE D 355       9.894  21.776 101.650  1.00 39.67           C  
-ATOM   8334  N   ALA D 356      14.980  19.219 101.829  1.00 41.18           N  
-ATOM   8335  CA  ALA D 356      16.084  18.521 102.482  1.00 41.63           C  
-ATOM   8336  C   ALA D 356      17.456  18.953 101.944  1.00 42.07           C  
-ATOM   8337  O   ALA D 356      18.396  19.150 102.715  1.00 41.94           O  
-ATOM   8338  CB  ALA D 356      15.910  17.030 102.340  1.00 41.50           C  
-ATOM   8339  N   GLY D 357      17.559  19.089 100.621  1.00 42.73           N  
-ATOM   8340  CA  GLY D 357      18.780  19.548  99.973  1.00 43.57           C  
-ATOM   8341  C   GLY D 357      19.183  20.945 100.415  1.00 44.10           C  
-ATOM   8342  O   GLY D 357      20.340  21.175 100.791  1.00 44.08           O  
-ATOM   8343  N   ALA D 358      18.218  21.864 100.392  1.00 44.72           N  
-ATOM   8344  CA  ALA D 358      18.433  23.241 100.832  1.00 45.77           C  
-ATOM   8345  C   ALA D 358      18.814  23.317 102.307  1.00 46.51           C  
-ATOM   8346  O   ALA D 358      19.704  24.084 102.681  1.00 46.56           O  
-ATOM   8347  CB  ALA D 358      17.208  24.096 100.544  1.00 45.59           C  
-ATOM   8348  N   ALA D 359      18.152  22.509 103.135  1.00 47.49           N  
-ATOM   8349  CA  ALA D 359      18.451  22.457 104.563  1.00 48.37           C  
-ATOM   8350  C   ALA D 359      19.859  21.944 104.838  1.00 49.13           C  
-ATOM   8351  O   ALA D 359      20.537  22.439 105.742  1.00 49.17           O  
-ATOM   8352  CB  ALA D 359      17.423  21.600 105.296  1.00 48.35           C  
-ATOM   8353  N   PHE D 360      20.290  20.950 104.064  1.00 50.03           N  
-ATOM   8354  CA  PHE D 360      21.604  20.348 104.259  1.00 51.04           C  
-ATOM   8355  C   PHE D 360      22.721  21.318 103.870  1.00 51.98           C  
-ATOM   8356  O   PHE D 360      23.679  21.502 104.627  1.00 51.81           O  
-ATOM   8357  CB  PHE D 360      21.726  19.034 103.482  1.00 50.91           C  
-ATOM   8358  CG  PHE D 360      22.983  18.266 103.777  1.00 50.60           C  
-ATOM   8359  CD1 PHE D 360      23.455  18.141 105.077  1.00 50.92           C  
-ATOM   8360  CD2 PHE D 360      23.693  17.664 102.752  1.00 50.65           C  
-ATOM   8361  CE1 PHE D 360      24.621  17.427 105.348  1.00 51.52           C  
-ATOM   8362  CE2 PHE D 360      24.856  16.953 103.011  1.00 51.04           C  
-ATOM   8363  CZ  PHE D 360      25.320  16.831 104.311  1.00 51.59           C  
-ATOM   8364  N   HIS D 361      22.585  21.941 102.698  1.00 53.29           N  
-ATOM   8365  CA  HIS D 361      23.547  22.937 102.243  1.00 54.68           C  
-ATOM   8366  C   HIS D 361      23.674  24.087 103.244  1.00 55.21           C  
-ATOM   8367  O   HIS D 361      24.784  24.446 103.634  1.00 55.42           O  
-ATOM   8368  CB  HIS D 361      23.179  23.483 100.862  1.00 54.87           C  
-ATOM   8369  CG  HIS D 361      23.981  24.683 100.467  1.00 56.35           C  
-ATOM   8370  ND1 HIS D 361      25.332  24.618 100.194  1.00 56.91           N  
-ATOM   8371  CD2 HIS D 361      23.631  25.985 100.330  1.00 57.36           C  
-ATOM   8372  CE1 HIS D 361      25.776  25.826  99.893  1.00 57.46           C  
-ATOM   8373  NE2 HIS D 361      24.764  26.673  99.967  1.00 57.80           N  
-ATOM   8374  N   LEU D 362      22.536  24.640 103.662  1.00 55.84           N  
-ATOM   8375  CA  LEU D 362      22.511  25.778 104.582  1.00 56.64           C  
-ATOM   8376  C   LEU D 362      23.219  25.481 105.904  1.00 57.13           C  
-ATOM   8377  O   LEU D 362      24.007  26.298 106.389  1.00 57.22           O  
-ATOM   8378  CB  LEU D 362      21.068  26.244 104.826  1.00 56.68           C  
-ATOM   8379  CG  LEU D 362      20.760  27.664 105.325  1.00 57.09           C  
-ATOM   8380  CD1 LEU D 362      21.647  28.730 104.680  1.00 56.98           C  
-ATOM   8381  CD2 LEU D 362      19.286  27.995 105.096  1.00 56.83           C  
-ATOM   8382  N   ALA D 363      22.945  24.306 106.465  1.00 57.79           N  
-ATOM   8383  CA  ALA D 363      23.561  23.858 107.714  1.00 58.44           C  
-ATOM   8384  C   ALA D 363      25.068  23.625 107.569  1.00 58.85           C  
-ATOM   8385  O   ALA D 363      25.848  23.963 108.466  1.00 58.84           O  
-ATOM   8386  CB  ALA D 363      22.882  22.595 108.204  1.00 58.39           C  
-ATOM   8387  N   LEU D 364      25.454  23.033 106.440  1.00 59.39           N  
-ATOM   8388  CA  LEU D 364      26.852  22.801 106.086  1.00 60.03           C  
-ATOM   8389  C   LEU D 364      27.629  24.115 106.052  1.00 60.49           C  
-ATOM   8390  O   LEU D 364      28.699  24.231 106.655  1.00 60.64           O  
-ATOM   8391  CB  LEU D 364      26.929  22.127 104.713  1.00 59.93           C  
-ATOM   8392  CG  LEU D 364      27.777  20.883 104.421  1.00 60.01           C  
-ATOM   8393  CD1 LEU D 364      28.242  20.144 105.670  1.00 59.94           C  
-ATOM   8394  CD2 LEU D 364      26.988  19.955 103.508  1.00 59.74           C  
-ATOM   8395  N   TYR D 365      27.066  25.100 105.354  1.00 61.04           N  
-ATOM   8396  CA  TYR D 365      27.675  26.417 105.185  1.00 61.66           C  
-ATOM   8397  C   TYR D 365      27.821  27.190 106.499  1.00 61.59           C  
-ATOM   8398  O   TYR D 365      28.876  27.767 106.770  1.00 61.68           O  
-ATOM   8399  CB  TYR D 365      26.867  27.234 104.174  1.00 62.02           C  
-ATOM   8400  CG  TYR D 365      27.560  28.487 103.696  1.00 63.57           C  
-ATOM   8401  CD1 TYR D 365      27.344  29.709 104.331  1.00 65.07           C  
-ATOM   8402  CD2 TYR D 365      28.426  28.454 102.601  1.00 65.48           C  
-ATOM   8403  CE1 TYR D 365      27.978  30.870 103.897  1.00 66.26           C  
-ATOM   8404  CE2 TYR D 365      29.068  29.612 102.156  1.00 66.76           C  
-ATOM   8405  CZ  TYR D 365      28.837  30.815 102.811  1.00 67.08           C  
-ATOM   8406  OH  TYR D 365      29.461  31.963 102.383  1.00 68.52           O  
-ATOM   8407  N   THR D 366      26.762  27.193 107.305  1.00 61.39           N  
-ATOM   8408  CA  THR D 366      26.733  27.931 108.566  1.00 61.15           C  
-ATOM   8409  C   THR D 366      27.782  27.435 109.570  1.00 61.22           C  
-ATOM   8410  O   THR D 366      28.387  28.234 110.290  1.00 61.26           O  
-ATOM   8411  CB  THR D 366      25.312  27.869 109.186  1.00 61.11           C  
-ATOM   8412  OG1 THR D 366      24.339  28.258 108.207  1.00 60.71           O  
-ATOM   8413  CG2 THR D 366      25.139  28.912 110.280  1.00 60.69           C  
-ATOM   8414  N   VAL D 367      28.001  26.122 109.607  1.00 61.19           N  
-ATOM   8415  CA  VAL D 367      28.883  25.525 110.610  1.00 61.14           C  
-ATOM   8416  C   VAL D 367      30.309  25.266 110.099  1.00 61.06           C  
-ATOM   8417  O   VAL D 367      31.279  25.570 110.795  1.00 61.09           O  
-ATOM   8418  CB  VAL D 367      28.268  24.229 111.228  1.00 61.23           C  
-ATOM   8419  CG1 VAL D 367      29.137  23.692 112.366  1.00 60.95           C  
-ATOM   8420  CG2 VAL D 367      26.853  24.488 111.732  1.00 61.08           C  
-ATOM   8421  N   THR D 368      30.438  24.714 108.895  1.00 60.97           N  
-ATOM   8422  CA  THR D 368      31.754  24.329 108.377  1.00 60.95           C  
-ATOM   8423  C   THR D 368      32.315  25.314 107.355  1.00 60.96           C  
-ATOM   8424  O   THR D 368      33.534  25.443 107.216  1.00 61.09           O  
-ATOM   8425  CB  THR D 368      31.733  22.898 107.766  1.00 60.90           C  
-ATOM   8426  OG1 THR D 368      30.824  22.849 106.660  1.00 60.76           O  
-ATOM   8427  CG2 THR D 368      31.164  21.883 108.747  1.00 60.92           C  
-ATOM   8428  N   GLY D 369      31.425  25.993 106.639  1.00 60.90           N  
-ATOM   8429  CA  GLY D 369      31.820  26.847 105.535  1.00 60.88           C  
-ATOM   8430  C   GLY D 369      31.795  26.094 104.221  1.00 60.96           C  
-ATOM   8431  O   GLY D 369      31.956  26.689 103.155  1.00 61.12           O  
-ATOM   8432  N   GLN D 370      31.588  24.780 104.302  1.00 61.02           N  
-ATOM   8433  CA  GLN D 370      31.511  23.918 103.124  1.00 61.01           C  
-ATOM   8434  C   GLN D 370      30.200  24.120 102.371  1.00 61.01           C  
-ATOM   8435  O   GLN D 370      29.344  24.892 102.800  1.00 60.96           O  
-ATOM   8436  CB  GLN D 370      31.656  22.447 103.527  1.00 61.03           C  
-ATOM   8437  CG  GLN D 370      33.021  22.067 104.077  1.00 61.16           C  
-ATOM   8438  CD  GLN D 370      33.007  20.731 104.799  1.00 61.67           C  
-ATOM   8439  OE1 GLN D 370      32.442  19.757 104.301  1.00 61.56           O  
-ATOM   8440  NE2 GLN D 370      33.632  20.681 105.974  1.00 62.05           N  
-ATOM   8441  N   SER D 371      30.050  23.424 101.247  1.00 61.19           N  
-ATOM   8442  CA  SER D 371      28.830  23.495 100.447  1.00 61.36           C  
-ATOM   8443  C   SER D 371      28.336  22.115 100.012  1.00 61.43           C  
-ATOM   8444  O   SER D 371      29.025  21.113 100.208  1.00 61.32           O  
-ATOM   8445  CB  SER D 371      29.046  24.390  99.226  1.00 61.27           C  
-ATOM   8446  OG  SER D 371      29.100  25.750  99.611  1.00 61.66           O  
-ATOM   8447  N   TRP D 372      27.129  22.093  99.441  1.00 61.63           N  
-ATOM   8448  CA  TRP D 372      26.504  20.914  98.834  1.00 61.89           C  
-ATOM   8449  C   TRP D 372      27.533  20.043  98.099  1.00 62.03           C  
-ATOM   8450  O   TRP D 372      28.020  20.425  97.035  1.00 62.12           O  
-ATOM   8451  CB  TRP D 372      25.411  21.393  97.872  1.00 61.91           C  
-ATOM   8452  CG  TRP D 372      24.574  20.332  97.213  1.00 62.03           C  
-ATOM   8453  CD1 TRP D 372      24.554  20.019  95.886  1.00 62.50           C  
-ATOM   8454  CD2 TRP D 372      23.599  19.485  97.837  1.00 62.10           C  
-ATOM   8455  NE1 TRP D 372      23.644  19.017  95.645  1.00 62.47           N  
-ATOM   8456  CE2 TRP D 372      23.043  18.670  96.826  1.00 62.24           C  
-ATOM   8457  CE3 TRP D 372      23.145  19.321  99.154  1.00 62.24           C  
-ATOM   8458  CZ2 TRP D 372      22.060  17.708  97.088  1.00 62.50           C  
-ATOM   8459  CZ3 TRP D 372      22.166  18.363  99.415  1.00 62.12           C  
-ATOM   8460  CH2 TRP D 372      21.636  17.571  98.385  1.00 62.21           C  
-ATOM   8461  N   PRO D 373      27.872  18.887  98.678  1.00 62.18           N  
-ATOM   8462  CA  PRO D 373      28.952  18.032  98.153  1.00 62.12           C  
-ATOM   8463  C   PRO D 373      28.688  17.456  96.764  1.00 62.13           C  
-ATOM   8464  O   PRO D 373      27.537  17.386  96.323  1.00 62.09           O  
-ATOM   8465  CB  PRO D 373      29.050  16.905  99.188  1.00 62.14           C  
-ATOM   8466  CG  PRO D 373      27.737  16.897  99.884  1.00 62.13           C  
-ATOM   8467  CD  PRO D 373      27.255  18.315  99.891  1.00 62.18           C  
-ATOM   8468  N   GLU D 374      29.767  17.056  96.091  1.00 62.21           N  
-ATOM   8469  CA  GLU D 374      29.701  16.489  94.743  1.00 62.13           C  
-ATOM   8470  C   GLU D 374      29.136  15.075  94.759  1.00 61.77           C  
-ATOM   8471  O   GLU D 374      28.528  14.633  93.783  1.00 61.60           O  
-ATOM   8472  CB  GLU D 374      31.077  16.495  94.066  1.00 62.26           C  
-ATOM   8473  CG  GLU D 374      31.945  17.702  94.399  1.00 63.34           C  
-ATOM   8474  CD  GLU D 374      33.134  17.869  93.463  1.00 64.91           C  
-ATOM   8475  OE1 GLU D 374      33.678  16.854  92.966  1.00 64.80           O  
-ATOM   8476  OE2 GLU D 374      33.531  19.032  93.231  1.00 66.06           O  
-ATOM   8477  N   SER D 375      29.340  14.371  95.870  1.00 61.55           N  
-ATOM   8478  CA  SER D 375      28.799  13.024  96.041  1.00 61.20           C  
-ATOM   8479  C   SER D 375      27.270  13.033  96.040  1.00 60.98           C  
-ATOM   8480  O   SER D 375      26.640  12.036  95.691  1.00 60.88           O  
-ATOM   8481  CB  SER D 375      29.344  12.370  97.316  1.00 61.20           C  
-ATOM   8482  OG  SER D 375      29.196  13.209  98.449  1.00 60.87           O  
-ATOM   8483  N   LEU D 376      26.687  14.174  96.403  1.00 60.90           N  
-ATOM   8484  CA  LEU D 376      25.233  14.322  96.460  1.00 60.87           C  
-ATOM   8485  C   LEU D 376      24.586  14.808  95.165  1.00 60.97           C  
-ATOM   8486  O   LEU D 376      23.428  14.491  94.902  1.00 60.89           O  
-ATOM   8487  CB  LEU D 376      24.820  15.205  97.639  1.00 60.68           C  
-ATOM   8488  CG  LEU D 376      24.549  14.443  98.939  1.00 60.52           C  
-ATOM   8489  CD1 LEU D 376      24.243  15.401 100.057  1.00 60.16           C  
-ATOM   8490  CD2 LEU D 376      23.412  13.443  98.779  1.00 60.20           C  
-ATOM   8491  N   ILE D 377      25.319  15.580  94.362  1.00 61.35           N  
-ATOM   8492  CA  ILE D 377      24.831  15.956  93.029  1.00 61.58           C  
-ATOM   8493  C   ILE D 377      24.789  14.723  92.122  1.00 61.83           C  
-ATOM   8494  O   ILE D 377      23.913  14.599  91.266  1.00 61.76           O  
-ATOM   8495  CB  ILE D 377      25.639  17.148  92.403  1.00 61.55           C  
-ATOM   8496  CG1 ILE D 377      25.442  17.228  90.888  1.00 61.31           C  
-ATOM   8497  CG2 ILE D 377      27.109  17.054  92.706  1.00 61.72           C  
-ATOM   8498  CD1 ILE D 377      24.447  18.264  90.466  1.00 60.81           C  
-ATOM   8499  N   ARG D 378      25.731  13.807  92.337  1.00 62.35           N  
-ATOM   8500  CA  ARG D 378      25.694  12.491  91.708  1.00 62.82           C  
-ATOM   8501  C   ARG D 378      24.416  11.756  92.125  1.00 62.87           C  
-ATOM   8502  O   ARG D 378      23.600  11.378  91.276  1.00 63.00           O  
-ATOM   8503  CB  ARG D 378      26.926  11.669  92.106  1.00 62.98           C  
-ATOM   8504  CG  ARG D 378      28.216  12.061  91.390  1.00 63.70           C  
-ATOM   8505  CD  ARG D 378      29.463  11.379  91.939  1.00 64.42           C  
-ATOM   8506  NE  ARG D 378      30.465  12.354  92.367  1.00 65.76           N  
-ATOM   8507  CZ  ARG D 378      31.375  12.147  93.315  1.00 66.31           C  
-ATOM   8508  NH1 ARG D 378      31.434  10.984  93.959  1.00 66.82           N  
-ATOM   8509  NH2 ARG D 378      32.235  13.109  93.623  1.00 66.11           N  
-ATOM   8510  N   LYS D 379      24.246  11.594  93.438  1.00 62.92           N  
-ATOM   8511  CA  LYS D 379      23.125  10.861  94.028  1.00 62.98           C  
-ATOM   8512  C   LYS D 379      21.755  11.424  93.650  1.00 62.83           C  
-ATOM   8513  O   LYS D 379      20.933  10.722  93.060  1.00 62.76           O  
-ATOM   8514  CB  LYS D 379      23.269  10.817  95.556  1.00 63.06           C  
-ATOM   8515  CG  LYS D 379      22.410   9.759  96.236  1.00 63.36           C  
-ATOM   8516  CD  LYS D 379      22.248  10.040  97.724  1.00 63.90           C  
-ATOM   8517  CE  LYS D 379      21.214   9.114  98.356  1.00 63.87           C  
-ATOM   8518  NZ  LYS D 379      21.706   7.712  98.489  1.00 63.81           N  
-ATOM   8519  N   THR D 380      21.530  12.692  93.984  1.00 62.87           N  
-ATOM   8520  CA  THR D 380      20.210  13.316  93.865  1.00 62.93           C  
-ATOM   8521  C   THR D 380      19.957  13.934  92.494  1.00 62.93           C  
-ATOM   8522  O   THR D 380      18.815  13.976  92.027  1.00 62.87           O  
-ATOM   8523  CB  THR D 380      20.013  14.394  94.963  1.00 62.94           C  
-ATOM   8524  OG1 THR D 380      20.970  15.450  94.790  1.00 63.02           O  
-ATOM   8525  CG2 THR D 380      20.344  13.836  96.340  1.00 62.76           C  
-ATOM   8526  N   GLY D 381      21.024  14.419  91.862  1.00 62.92           N  
-ATOM   8527  CA  GLY D 381      20.912  15.157  90.615  1.00 62.92           C  
-ATOM   8528  C   GLY D 381      20.481  16.590  90.863  1.00 62.92           C  
-ATOM   8529  O   GLY D 381      19.981  17.261  89.958  1.00 62.99           O  
-ATOM   8530  N   TYR D 382      20.667  17.050  92.099  1.00 62.83           N  
-ATOM   8531  CA  TYR D 382      20.330  18.413  92.486  1.00 62.65           C  
-ATOM   8532  C   TYR D 382      21.567  19.296  92.454  1.00 62.77           C  
-ATOM   8533  O   TYR D 382      22.546  19.045  93.164  1.00 62.63           O  
-ATOM   8534  CB  TYR D 382      19.694  18.454  93.885  1.00 62.48           C  
-ATOM   8535  CG  TYR D 382      18.264  17.952  93.956  1.00 61.49           C  
-ATOM   8536  CD1 TYR D 382      17.373  18.161  92.905  1.00 60.64           C  
-ATOM   8537  CD2 TYR D 382      17.802  17.271  95.085  1.00 60.89           C  
-ATOM   8538  CE1 TYR D 382      16.065  17.695  92.967  1.00 60.74           C  
-ATOM   8539  CE2 TYR D 382      16.491  16.801  95.161  1.00 60.35           C  
-ATOM   8540  CZ  TYR D 382      15.629  17.018  94.099  1.00 60.39           C  
-ATOM   8541  OH  TYR D 382      14.333  16.565  94.161  1.00 60.32           O  
-ATOM   8542  N   THR D 383      21.517  20.322  91.612  1.00 62.94           N  
-ATOM   8543  CA  THR D 383      22.553  21.346  91.582  1.00 63.18           C  
-ATOM   8544  C   THR D 383      22.221  22.391  92.640  1.00 63.14           C  
-ATOM   8545  O   THR D 383      21.061  22.528  93.039  1.00 63.13           O  
-ATOM   8546  CB  THR D 383      22.633  22.014  90.185  1.00 63.15           C  
-ATOM   8547  OG1 THR D 383      21.398  22.676  89.897  1.00 63.63           O  
-ATOM   8548  CG2 THR D 383      22.728  20.976  89.073  1.00 63.13           C  
-ATOM   8549  N   LEU D 384      23.234  23.128  93.090  1.00 63.13           N  
-ATOM   8550  CA  LEU D 384      23.014  24.290  93.951  1.00 62.97           C  
-ATOM   8551  C   LEU D 384      22.183  25.353  93.224  1.00 62.80           C  
-ATOM   8552  O   LEU D 384      21.704  26.306  93.839  1.00 62.91           O  
-ATOM   8553  CB  LEU D 384      24.349  24.875  94.417  1.00 62.94           C  
-ATOM   8554  CG  LEU D 384      24.449  25.515  95.806  1.00 63.27           C  
-ATOM   8555  CD1 LEU D 384      23.719  24.711  96.886  1.00 63.39           C  
-ATOM   8556  CD2 LEU D 384      25.915  25.705  96.187  1.00 63.65           C  
-ATOM   8557  N   GLU D 385      22.019  25.167  91.915  1.00 62.50           N  
-ATOM   8558  CA  GLU D 385      21.191  26.028  91.079  1.00 62.32           C  
-ATOM   8559  C   GLU D 385      19.724  25.596  91.113  1.00 61.60           C  
-ATOM   8560  O   GLU D 385      18.829  26.439  91.214  1.00 61.67           O  
-ATOM   8561  CB  GLU D 385      21.719  26.029  89.640  1.00 62.66           C  
-ATOM   8562  CG  GLU D 385      20.782  26.650  88.615  1.00 64.46           C  
-ATOM   8563  CD  GLU D 385      21.180  28.064  88.238  1.00 66.74           C  
-ATOM   8564  OE1 GLU D 385      20.854  28.995  89.007  1.00 67.51           O  
-ATOM   8565  OE2 GLU D 385      21.816  28.243  87.172  1.00 67.59           O  
-ATOM   8566  N   SER D 386      19.484  24.287  91.019  1.00 60.56           N  
-ATOM   8567  CA  SER D 386      18.126  23.737  91.096  1.00 59.54           C  
-ATOM   8568  C   SER D 386      17.545  23.901  92.498  1.00 58.62           C  
-ATOM   8569  O   SER D 386      16.330  24.000  92.671  1.00 58.47           O  
-ATOM   8570  CB  SER D 386      18.100  22.261  90.673  1.00 59.69           C  
-ATOM   8571  OG  SER D 386      19.123  21.515  91.313  1.00 59.59           O  
-ATOM   8572  N   LEU D 387      18.432  23.946  93.487  1.00 57.52           N  
-ATOM   8573  CA  LEU D 387      18.056  24.126  94.882  1.00 56.65           C  
-ATOM   8574  C   LEU D 387      17.938  25.598  95.299  1.00 56.22           C  
-ATOM   8575  O   LEU D 387      17.489  25.889  96.412  1.00 56.15           O  
-ATOM   8576  CB  LEU D 387      19.060  23.410  95.790  1.00 56.56           C  
-ATOM   8577  CG  LEU D 387      19.120  21.883  95.807  1.00 55.92           C  
-ATOM   8578  CD1 LEU D 387      20.355  21.452  96.559  1.00 55.77           C  
-ATOM   8579  CD2 LEU D 387      17.878  21.279  96.442  1.00 56.07           C  
-ATOM   8580  N   LYS D 388      18.325  26.514  94.407  1.00 55.48           N  
-ATOM   8581  CA  LYS D 388      18.378  27.950  94.718  1.00 54.80           C  
-ATOM   8582  C   LYS D 388      17.054  28.571  95.203  1.00 53.98           C  
-ATOM   8583  O   LYS D 388      17.041  29.194  96.267  1.00 53.74           O  
-ATOM   8584  CB  LYS D 388      18.986  28.769  93.561  1.00 54.89           C  
-ATOM   8585  CG  LYS D 388      19.046  30.278  93.834  1.00 55.58           C  
-ATOM   8586  CD  LYS D 388      20.048  31.005  92.937  1.00 57.07           C  
-ATOM   8587  CE  LYS D 388      20.334  32.413  93.465  1.00 57.64           C  
-ATOM   8588  NZ  LYS D 388      20.793  33.369  92.400  1.00 58.30           N  
-ATOM   8589  N   PRO D 389      15.953  28.410  94.460  1.00 53.25           N  
-ATOM   8590  CA  PRO D 389      14.679  29.030  94.860  1.00 52.70           C  
-ATOM   8591  C   PRO D 389      14.276  28.623  96.278  1.00 52.21           C  
-ATOM   8592  O   PRO D 389      13.931  29.498  97.083  1.00 52.05           O  
-ATOM   8593  CB  PRO D 389      13.682  28.489  93.831  1.00 52.58           C  
-ATOM   8594  CG  PRO D 389      14.514  28.158  92.654  1.00 52.84           C  
-ATOM   8595  CD  PRO D 389      15.808  27.634  93.215  1.00 53.19           C  
-ATOM   8596  N   CYS D 390      14.349  27.322  96.574  1.00 51.56           N  
-ATOM   8597  CA  CYS D 390      14.117  26.810  97.922  1.00 50.81           C  
-ATOM   8598  C   CYS D 390      15.147  27.347  98.904  1.00 50.67           C  
-ATOM   8599  O   CYS D 390      14.801  27.712 100.027  1.00 50.34           O  
-ATOM   8600  CB  CYS D 390      14.142  25.281  97.941  1.00 50.87           C  
-ATOM   8601  SG  CYS D 390      13.626  24.576  99.525  1.00 49.25           S  
-ATOM   8602  N   LEU D 391      16.406  27.389  98.471  1.00 50.66           N  
-ATOM   8603  CA  LEU D 391      17.499  27.911  99.292  1.00 50.84           C  
-ATOM   8604  C   LEU D 391      17.209  29.342  99.728  1.00 50.56           C  
-ATOM   8605  O   LEU D 391      17.390  29.686 100.893  1.00 50.47           O  
-ATOM   8606  CB  LEU D 391      18.828  27.862  98.526  1.00 51.02           C  
-ATOM   8607  CG  LEU D 391      20.037  27.068  99.043  1.00 51.87           C  
-ATOM   8608  CD1 LEU D 391      20.056  26.901 100.568  1.00 51.97           C  
-ATOM   8609  CD2 LEU D 391      20.120  25.717  98.344  1.00 52.61           C  
-ATOM   8610  N   MET D 392      16.751  30.161  98.785  1.00 50.48           N  
-ATOM   8611  CA  MET D 392      16.453  31.569  99.049  1.00 50.68           C  
-ATOM   8612  C   MET D 392      15.384  31.689 100.131  1.00 50.22           C  
-ATOM   8613  O   MET D 392      15.587  32.366 101.139  1.00 50.35           O  
-ATOM   8614  CB  MET D 392      16.009  32.295  97.767  1.00 50.89           C  
-ATOM   8615  CG  MET D 392      17.059  32.347  96.650  1.00 52.25           C  
-ATOM   8616  SD  MET D 392      18.509  33.345  97.069  1.00 55.91           S  
-ATOM   8617  CE  MET D 392      19.771  32.101  97.181  1.00 55.14           C  
-ATOM   8618  N   ASP D 393      14.260  31.008  99.918  1.00 49.81           N  
-ATOM   8619  CA  ASP D 393      13.151  30.983 100.868  1.00 49.32           C  
-ATOM   8620  C   ASP D 393      13.589  30.552 102.266  1.00 48.82           C  
-ATOM   8621  O   ASP D 393      13.256  31.207 103.255  1.00 48.50           O  
-ATOM   8622  CB  ASP D 393      12.047  30.058 100.360  1.00 49.43           C  
-ATOM   8623  CG  ASP D 393      11.079  30.759  99.440  1.00 49.91           C  
-ATOM   8624  OD1 ASP D 393      10.799  31.958  99.664  1.00 51.78           O  
-ATOM   8625  OD2 ASP D 393      10.539  30.188  98.468  1.00 50.58           O  
-ATOM   8626  N   LEU D 394      14.349  29.461 102.331  1.00 48.51           N  
-ATOM   8627  CA  LEU D 394      14.780  28.875 103.597  1.00 48.23           C  
-ATOM   8628  C   LEU D 394      15.844  29.716 104.287  1.00 48.28           C  
-ATOM   8629  O   LEU D 394      15.915  29.760 105.521  1.00 48.04           O  
-ATOM   8630  CB  LEU D 394      15.274  27.442 103.375  1.00 48.29           C  
-ATOM   8631  CG  LEU D 394      15.634  26.576 104.586  1.00 47.62           C  
-ATOM   8632  CD1 LEU D 394      14.465  26.428 105.560  1.00 47.35           C  
-ATOM   8633  CD2 LEU D 394      16.100  25.219 104.100  1.00 47.89           C  
-ATOM   8634  N   HIS D 395      16.670  30.375 103.479  1.00 48.52           N  
-ATOM   8635  CA  HIS D 395      17.634  31.355 103.971  1.00 48.65           C  
-ATOM   8636  C   HIS D 395      16.901  32.469 104.710  1.00 48.23           C  
-ATOM   8637  O   HIS D 395      17.272  32.824 105.825  1.00 48.20           O  
-ATOM   8638  CB  HIS D 395      18.448  31.929 102.807  1.00 48.96           C  
-ATOM   8639  CG  HIS D 395      19.424  32.988 103.213  1.00 50.14           C  
-ATOM   8640  ND1 HIS D 395      20.379  32.786 104.187  1.00 51.24           N  
-ATOM   8641  CD2 HIS D 395      19.587  34.260 102.782  1.00 51.02           C  
-ATOM   8642  CE1 HIS D 395      21.090  33.889 104.335  1.00 52.07           C  
-ATOM   8643  NE2 HIS D 395      20.630  34.799 103.495  1.00 51.78           N  
-ATOM   8644  N   GLN D 396      15.846  32.986 104.081  1.00 47.86           N  
-ATOM   8645  CA  GLN D 396      14.990  34.024 104.654  1.00 47.89           C  
-ATOM   8646  C   GLN D 396      14.311  33.593 105.959  1.00 47.45           C  
-ATOM   8647  O   GLN D 396      14.372  34.307 106.967  1.00 47.56           O  
-ATOM   8648  CB  GLN D 396      13.934  34.453 103.631  1.00 48.06           C  
-ATOM   8649  CG  GLN D 396      14.469  35.341 102.520  1.00 50.06           C  
-ATOM   8650  CD  GLN D 396      14.894  36.712 103.028  1.00 52.15           C  
-ATOM   8651  OE1 GLN D 396      16.083  36.961 103.236  1.00 52.34           O  
-ATOM   8652  NE2 GLN D 396      13.920  37.595 103.243  1.00 53.55           N  
-ATOM   8653  N   THR D 397      13.676  32.421 105.931  1.00 46.77           N  
-ATOM   8654  CA  THR D 397      13.004  31.847 107.097  1.00 46.06           C  
-ATOM   8655  C   THR D 397      13.956  31.725 108.295  1.00 45.91           C  
-ATOM   8656  O   THR D 397      13.595  32.064 109.428  1.00 45.68           O  
-ATOM   8657  CB  THR D 397      12.399  30.471 106.711  1.00 46.07           C  
-ATOM   8658  OG1 THR D 397      11.341  30.668 105.761  1.00 45.28           O  
-ATOM   8659  CG2 THR D 397      11.708  29.800 107.901  1.00 45.61           C  
-ATOM   8660  N   TYR D 398      15.167  31.243 108.020  1.00 45.69           N  
-ATOM   8661  CA  TYR D 398      16.238  31.125 109.004  1.00 45.73           C  
-ATOM   8662  C   TYR D 398      16.600  32.498 109.581  1.00 46.18           C  
-ATOM   8663  O   TYR D 398      16.756  32.647 110.805  1.00 46.13           O  
-ATOM   8664  CB  TYR D 398      17.454  30.495 108.321  1.00 45.63           C  
-ATOM   8665  CG  TYR D 398      18.605  30.057 109.207  1.00 44.65           C  
-ATOM   8666  CD1 TYR D 398      18.518  30.086 110.599  1.00 44.52           C  
-ATOM   8667  CD2 TYR D 398      19.785  29.595 108.635  1.00 44.30           C  
-ATOM   8668  CE1 TYR D 398      19.585  29.681 111.394  1.00 43.90           C  
-ATOM   8669  CE2 TYR D 398      20.852  29.184 109.417  1.00 43.95           C  
-ATOM   8670  CZ  TYR D 398      20.747  29.229 110.791  1.00 43.92           C  
-ATOM   8671  OH  TYR D 398      21.806  28.819 111.560  1.00 44.39           O  
-ATOM   8672  N   LEU D 399      16.724  33.491 108.694  1.00 46.48           N  
-ATOM   8673  CA  LEU D 399      17.083  34.858 109.082  1.00 46.59           C  
-ATOM   8674  C   LEU D 399      16.018  35.487 109.971  1.00 46.76           C  
-ATOM   8675  O   LEU D 399      16.341  36.181 110.936  1.00 46.92           O  
-ATOM   8676  CB  LEU D 399      17.319  35.744 107.849  1.00 46.44           C  
-ATOM   8677  CG  LEU D 399      18.527  35.476 106.943  1.00 46.47           C  
-ATOM   8678  CD1 LEU D 399      18.458  36.343 105.698  1.00 46.45           C  
-ATOM   8679  CD2 LEU D 399      19.855  35.668 107.666  1.00 46.35           C  
-ATOM   8680  N   LYS D 400      14.755  35.221 109.648  1.00 46.62           N  
-ATOM   8681  CA  LYS D 400      13.627  35.842 110.338  1.00 46.71           C  
-ATOM   8682  C   LYS D 400      13.061  35.001 111.487  1.00 46.31           C  
-ATOM   8683  O   LYS D 400      12.139  35.440 112.183  1.00 46.19           O  
-ATOM   8684  CB  LYS D 400      12.516  36.164 109.338  1.00 46.84           C  
-ATOM   8685  CG  LYS D 400      12.858  37.286 108.368  1.00 48.37           C  
-ATOM   8686  CD  LYS D 400      12.074  37.160 107.067  1.00 51.33           C  
-ATOM   8687  CE  LYS D 400      10.695  37.801 107.175  1.00 52.85           C  
-ATOM   8688  NZ  LYS D 400       9.687  36.853 107.745  1.00 54.81           N  
-ATOM   8689  N   ALA D 401      13.627  33.811 111.690  1.00 45.91           N  
-ATOM   8690  CA  ALA D 401      13.095  32.832 112.646  1.00 45.64           C  
-ATOM   8691  C   ALA D 401      12.812  33.360 114.056  1.00 45.43           C  
-ATOM   8692  O   ALA D 401      11.779  33.013 114.627  1.00 45.57           O  
-ATOM   8693  CB  ALA D 401      13.980  31.578 112.701  1.00 45.78           C  
-ATOM   8694  N   PRO D 402      13.696  34.195 114.618  1.00 45.09           N  
-ATOM   8695  CA  PRO D 402      13.464  34.764 115.953  1.00 44.71           C  
-ATOM   8696  C   PRO D 402      12.248  35.691 116.053  1.00 44.44           C  
-ATOM   8697  O   PRO D 402      11.795  35.948 117.173  1.00 44.30           O  
-ATOM   8698  CB  PRO D 402      14.750  35.547 116.225  1.00 45.00           C  
-ATOM   8699  CG  PRO D 402      15.763  34.945 115.301  1.00 44.96           C  
-ATOM   8700  CD  PRO D 402      14.994  34.634 114.070  1.00 44.94           C  
-ATOM   8701  N   GLN D 403      11.736  36.167 114.917  1.00 43.95           N  
-ATOM   8702  CA  GLN D 403      10.581  37.070 114.886  1.00 43.61           C  
-ATOM   8703  C   GLN D 403       9.265  36.366 114.539  1.00 42.85           C  
-ATOM   8704  O   GLN D 403       8.179  36.902 114.793  1.00 42.47           O  
-ATOM   8705  CB  GLN D 403      10.820  38.211 113.894  1.00 44.16           C  
-ATOM   8706  CG  GLN D 403      11.725  39.325 114.413  1.00 46.24           C  
-ATOM   8707  CD  GLN D 403      13.187  39.044 114.148  1.00 49.00           C  
-ATOM   8708  OE1 GLN D 403      13.959  38.838 115.083  1.00 51.08           O  
-ATOM   8709  NE2 GLN D 403      13.573  39.029 112.873  1.00 50.36           N  
-ATOM   8710  N   HIS D 404       9.372  35.177 113.945  1.00 41.94           N  
-ATOM   8711  CA  HIS D 404       8.209  34.351 113.620  1.00 41.09           C  
-ATOM   8712  C   HIS D 404       7.318  34.132 114.842  1.00 40.32           C  
-ATOM   8713  O   HIS D 404       7.816  33.854 115.931  1.00 39.95           O  
-ATOM   8714  CB  HIS D 404       8.669  33.002 113.061  1.00 41.16           C  
-ATOM   8715  CG  HIS D 404       7.630  32.290 112.251  1.00 40.77           C  
-ATOM   8716  ND1 HIS D 404       6.415  31.902 112.773  1.00 40.18           N  
-ATOM   8717  CD2 HIS D 404       7.635  31.879 110.962  1.00 40.58           C  
-ATOM   8718  CE1 HIS D 404       5.710  31.293 111.837  1.00 40.69           C  
-ATOM   8719  NE2 HIS D 404       6.428  31.265 110.728  1.00 41.15           N  
-ATOM   8720  N   ALA D 405       6.007  34.269 114.645  1.00 39.79           N  
-ATOM   8721  CA  ALA D 405       5.002  34.050 115.695  1.00 39.30           C  
-ATOM   8722  C   ALA D 405       5.091  32.685 116.388  1.00 38.90           C  
-ATOM   8723  O   ALA D 405       4.682  32.544 117.541  1.00 39.23           O  
-ATOM   8724  CB  ALA D 405       3.602  34.265 115.144  1.00 39.20           C  
-ATOM   8725  N   GLN D 406       5.623  31.692 115.687  1.00 38.38           N  
-ATOM   8726  CA  GLN D 406       5.770  30.349 116.236  1.00 38.10           C  
-ATOM   8727  C   GLN D 406       7.220  30.118 116.630  1.00 37.99           C  
-ATOM   8728  O   GLN D 406       8.122  30.295 115.803  1.00 37.90           O  
-ATOM   8729  CB  GLN D 406       5.294  29.292 115.226  1.00 38.24           C  
-ATOM   8730  CG  GLN D 406       3.910  29.547 114.599  1.00 37.81           C  
-ATOM   8731  CD  GLN D 406       2.809  29.845 115.613  1.00 40.05           C  
-ATOM   8732  OE1 GLN D 406       1.930  30.673 115.351  1.00 41.20           O  
-ATOM   8733  NE2 GLN D 406       2.843  29.169 116.762  1.00 40.31           N  
-ATOM   8734  N   GLN D 407       7.440  29.739 117.892  1.00 37.46           N  
-ATOM   8735  CA  GLN D 407       8.789  29.660 118.457  1.00 37.23           C  
-ATOM   8736  C   GLN D 407       9.151  28.297 119.069  1.00 37.30           C  
-ATOM   8737  O   GLN D 407      10.228  28.154 119.661  1.00 37.65           O  
-ATOM   8738  CB  GLN D 407       8.996  30.762 119.517  1.00 37.15           C  
-ATOM   8739  CG  GLN D 407       9.133  32.197 118.982  1.00 36.84           C  
-ATOM   8740  CD  GLN D 407      10.357  32.408 118.098  1.00 36.97           C  
-ATOM   8741  OE1 GLN D 407      11.484  32.111 118.495  1.00 38.39           O  
-ATOM   8742  NE2 GLN D 407      10.134  32.924 116.899  1.00 37.31           N  
-ATOM   8743  N   SER D 408       8.278  27.298 118.936  1.00 36.83           N  
-ATOM   8744  CA  SER D 408       8.544  25.993 119.552  1.00 36.50           C  
-ATOM   8745  C   SER D 408       9.748  25.261 118.954  1.00 36.29           C  
-ATOM   8746  O   SER D 408      10.491  24.602 119.681  1.00 36.07           O  
-ATOM   8747  CB  SER D 408       7.301  25.109 119.547  1.00 36.41           C  
-ATOM   8748  OG  SER D 408       6.197  25.822 120.079  1.00 36.52           O  
-ATOM   8749  N   ILE D 409       9.945  25.386 117.644  1.00 36.37           N  
-ATOM   8750  CA  ILE D 409      11.106  24.782 116.983  1.00 37.01           C  
-ATOM   8751  C   ILE D 409      12.418  25.383 117.501  1.00 37.89           C  
-ATOM   8752  O   ILE D 409      13.317  24.651 117.936  1.00 37.45           O  
-ATOM   8753  CB  ILE D 409      11.012  24.931 115.449  1.00 36.83           C  
-ATOM   8754  CG1 ILE D 409       9.603  24.524 114.960  1.00 36.75           C  
-ATOM   8755  CG2 ILE D 409      12.175  24.203 114.766  1.00 35.76           C  
-ATOM   8756  CD1 ILE D 409       9.544  23.491 113.865  1.00 34.76           C  
-ATOM   8757  N   ARG D 410      12.514  26.715 117.462  1.00 39.09           N  
-ATOM   8758  CA  ARG D 410      13.683  27.425 117.980  1.00 40.47           C  
-ATOM   8759  C   ARG D 410      13.939  27.065 119.439  1.00 40.99           C  
-ATOM   8760  O   ARG D 410      15.078  26.811 119.825  1.00 41.13           O  
-ATOM   8761  CB  ARG D 410      13.512  28.939 117.837  1.00 40.73           C  
-ATOM   8762  CG  ARG D 410      13.938  29.491 116.488  1.00 41.78           C  
-ATOM   8763  CD  ARG D 410      13.876  31.012 116.384  1.00 44.74           C  
-ATOM   8764  NE  ARG D 410      14.395  31.676 117.581  1.00 46.99           N  
-ATOM   8765  CZ  ARG D 410      15.633  32.132 117.710  1.00 47.89           C  
-ATOM   8766  NH1 ARG D 410      16.497  32.009 116.712  1.00 49.12           N  
-ATOM   8767  NH2 ARG D 410      16.012  32.708 118.844  1.00 48.22           N  
-ATOM   8768  N   GLU D 411      12.877  27.033 120.243  1.00 41.74           N  
-ATOM   8769  CA  GLU D 411      12.993  26.634 121.642  1.00 42.60           C  
-ATOM   8770  C   GLU D 411      13.570  25.226 121.750  1.00 42.85           C  
-ATOM   8771  O   GLU D 411      14.529  24.993 122.496  1.00 42.90           O  
-ATOM   8772  CB  GLU D 411      11.638  26.717 122.353  1.00 42.90           C  
-ATOM   8773  CG  GLU D 411      11.263  28.103 122.857  1.00 45.05           C  
-ATOM   8774  CD  GLU D 411      12.388  28.772 123.628  1.00 48.88           C  
-ATOM   8775  OE1 GLU D 411      12.528  28.497 124.843  1.00 50.63           O  
-ATOM   8776  OE2 GLU D 411      13.140  29.565 123.014  1.00 50.55           O  
-ATOM   8777  N   LYS D 412      12.991  24.303 120.981  1.00 42.94           N  
-ATOM   8778  CA  LYS D 412      13.408  22.904 120.954  1.00 43.06           C  
-ATOM   8779  C   LYS D 412      14.896  22.747 120.640  1.00 43.61           C  
-ATOM   8780  O   LYS D 412      15.599  21.994 121.318  1.00 43.43           O  
-ATOM   8781  CB  LYS D 412      12.554  22.142 119.934  1.00 42.77           C  
-ATOM   8782  CG  LYS D 412      12.895  20.689 119.705  1.00 41.57           C  
-ATOM   8783  CD  LYS D 412      12.017  20.136 118.581  1.00 40.59           C  
-ATOM   8784  CE  LYS D 412      12.528  18.811 118.045  1.00 39.73           C  
-ATOM   8785  NZ  LYS D 412      11.751  18.386 116.849  1.00 39.01           N  
-ATOM   8786  N   TYR D 413      15.366  23.470 119.626  1.00 44.40           N  
-ATOM   8787  CA  TYR D 413      16.735  23.320 119.130  1.00 45.24           C  
-ATOM   8788  C   TYR D 413      17.774  24.197 119.861  1.00 46.11           C  
-ATOM   8789  O   TYR D 413      18.871  24.438 119.346  1.00 45.83           O  
-ATOM   8790  CB  TYR D 413      16.773  23.542 117.611  1.00 45.11           C  
-ATOM   8791  CG  TYR D 413      16.244  22.366 116.813  1.00 44.68           C  
-ATOM   8792  CD1 TYR D 413      17.087  21.335 116.422  1.00 44.52           C  
-ATOM   8793  CD2 TYR D 413      14.895  22.283 116.458  1.00 45.00           C  
-ATOM   8794  CE1 TYR D 413      16.612  20.247 115.695  1.00 44.67           C  
-ATOM   8795  CE2 TYR D 413      14.403  21.196 115.728  1.00 44.65           C  
-ATOM   8796  CZ  TYR D 413      15.271  20.183 115.352  1.00 44.63           C  
-ATOM   8797  OH  TYR D 413      14.814  19.104 114.634  1.00 44.54           O  
-ATOM   8798  N   LYS D 414      17.409  24.673 121.053  1.00 47.15           N  
-ATOM   8799  CA  LYS D 414      18.343  25.348 121.953  1.00 48.43           C  
-ATOM   8800  C   LYS D 414      18.947  24.343 122.923  1.00 49.16           C  
-ATOM   8801  O   LYS D 414      19.974  24.608 123.557  1.00 49.58           O  
-ATOM   8802  CB  LYS D 414      17.636  26.449 122.740  1.00 48.30           C  
-ATOM   8803  CG  LYS D 414      17.583  27.775 122.019  1.00 48.90           C  
-ATOM   8804  CD  LYS D 414      16.630  28.737 122.696  1.00 50.50           C  
-ATOM   8805  CE  LYS D 414      16.361  29.934 121.803  1.00 51.59           C  
-ATOM   8806  NZ  LYS D 414      15.436  30.910 122.446  1.00 52.87           N  
-ATOM   8807  N   ASN D 415      18.300  23.187 123.033  1.00 49.92           N  
-ATOM   8808  CA  ASN D 415      18.729  22.154 123.961  1.00 50.76           C  
-ATOM   8809  C   ASN D 415      19.968  21.392 123.497  1.00 50.98           C  
-ATOM   8810  O   ASN D 415      20.224  21.274 122.297  1.00 50.96           O  
-ATOM   8811  CB  ASN D 415      17.571  21.202 124.271  1.00 50.94           C  
-ATOM   8812  CG  ASN D 415      16.539  21.825 125.200  1.00 51.76           C  
-ATOM   8813  OD1 ASN D 415      15.335  21.626 125.035  1.00 52.97           O  
-ATOM   8814  ND2 ASN D 415      17.009  22.583 126.187  1.00 52.94           N  
-ATOM   8815  N   SER D 416      20.725  20.893 124.475  1.00 51.55           N  
-ATOM   8816  CA  SER D 416      21.966  20.137 124.267  1.00 52.01           C  
-ATOM   8817  C   SER D 416      21.795  18.927 123.349  1.00 52.29           C  
-ATOM   8818  O   SER D 416      22.704  18.583 122.591  1.00 52.46           O  
-ATOM   8819  CB  SER D 416      22.525  19.680 125.616  1.00 52.04           C  
-ATOM   8820  OG  SER D 416      21.558  18.926 126.336  1.00 52.41           O  
-ATOM   8821  N   LYS D 417      20.630  18.287 123.436  1.00 52.65           N  
-ATOM   8822  CA  LYS D 417      20.255  17.166 122.574  1.00 52.87           C  
-ATOM   8823  C   LYS D 417      20.491  17.487 121.095  1.00 52.96           C  
-ATOM   8824  O   LYS D 417      20.914  16.624 120.322  1.00 52.95           O  
-ATOM   8825  CB  LYS D 417      18.791  16.787 122.834  1.00 52.99           C  
-ATOM   8826  CG  LYS D 417      18.076  16.073 121.700  1.00 53.36           C  
-ATOM   8827  CD  LYS D 417      17.344  14.854 122.210  1.00 54.18           C  
-ATOM   8828  CE  LYS D 417      16.488  14.228 121.124  1.00 54.75           C  
-ATOM   8829  NZ  LYS D 417      16.121  12.828 121.475  1.00 55.82           N  
-ATOM   8830  N   TYR D 418      20.225  18.735 120.716  1.00 53.05           N  
-ATOM   8831  CA  TYR D 418      20.465  19.197 119.353  1.00 53.19           C  
-ATOM   8832  C   TYR D 418      21.648  20.164 119.278  1.00 53.23           C  
-ATOM   8833  O   TYR D 418      21.823  20.855 118.279  1.00 53.16           O  
-ATOM   8834  CB  TYR D 418      19.194  19.830 118.761  1.00 53.25           C  
-ATOM   8835  CG  TYR D 418      17.982  18.928 118.817  1.00 53.49           C  
-ATOM   8836  CD1 TYR D 418      17.904  17.780 118.026  1.00 53.80           C  
-ATOM   8837  CD2 TYR D 418      16.917  19.214 119.672  1.00 53.82           C  
-ATOM   8838  CE1 TYR D 418      16.798  16.942 118.082  1.00 54.30           C  
-ATOM   8839  CE2 TYR D 418      15.805  18.384 119.736  1.00 54.36           C  
-ATOM   8840  CZ  TYR D 418      15.752  17.250 118.936  1.00 55.06           C  
-ATOM   8841  OH  TYR D 418      14.656  16.417 118.992  1.00 56.42           O  
-ATOM   8842  N   HIS D 419      22.452  20.198 120.341  1.00 53.51           N  
-ATOM   8843  CA  HIS D 419      23.655  21.039 120.422  1.00 53.79           C  
-ATOM   8844  C   HIS D 419      23.389  22.533 120.203  1.00 53.55           C  
-ATOM   8845  O   HIS D 419      24.146  23.208 119.499  1.00 53.46           O  
-ATOM   8846  CB  HIS D 419      24.742  20.535 119.463  1.00 53.93           C  
-ATOM   8847  CG  HIS D 419      24.905  19.048 119.471  1.00 55.15           C  
-ATOM   8848  ND1 HIS D 419      24.255  18.223 118.577  1.00 56.07           N  
-ATOM   8849  CD2 HIS D 419      25.631  18.235 120.275  1.00 55.85           C  
-ATOM   8850  CE1 HIS D 419      24.581  16.967 118.825  1.00 56.60           C  
-ATOM   8851  NE2 HIS D 419      25.415  16.947 119.850  1.00 56.48           N  
-ATOM   8852  N   GLY D 420      22.305  23.026 120.806  1.00 53.28           N  
-ATOM   8853  CA  GLY D 420      21.937  24.438 120.779  1.00 53.03           C  
-ATOM   8854  C   GLY D 420      22.062  25.140 119.437  1.00 52.72           C  
-ATOM   8855  O   GLY D 420      22.445  26.310 119.376  1.00 52.71           O  
-ATOM   8856  N   VAL D 421      21.720  24.430 118.366  1.00 52.53           N  
-ATOM   8857  CA  VAL D 421      21.977  24.903 117.006  1.00 52.46           C  
-ATOM   8858  C   VAL D 421      21.088  26.062 116.542  1.00 52.70           C  
-ATOM   8859  O   VAL D 421      21.436  26.764 115.592  1.00 52.89           O  
-ATOM   8860  CB  VAL D 421      21.936  23.753 115.974  1.00 52.35           C  
-ATOM   8861  CG1 VAL D 421      23.119  22.811 116.186  1.00 52.05           C  
-ATOM   8862  CG2 VAL D 421      20.599  23.004 116.027  1.00 52.11           C  
-ATOM   8863  N   SER D 422      19.950  26.263 117.203  1.00 52.85           N  
-ATOM   8864  CA  SER D 422      19.079  27.388 116.866  1.00 53.12           C  
-ATOM   8865  C   SER D 422      19.626  28.719 117.398  1.00 53.58           C  
-ATOM   8866  O   SER D 422      19.156  29.786 117.004  1.00 53.56           O  
-ATOM   8867  CB  SER D 422      17.643  27.147 117.346  1.00 52.89           C  
-ATOM   8868  OG  SER D 422      17.583  26.933 118.744  1.00 52.22           O  
-ATOM   8869  N   LEU D 423      20.622  28.642 118.281  1.00 54.41           N  
-ATOM   8870  CA  LEU D 423      21.267  29.826 118.857  1.00 55.19           C  
-ATOM   8871  C   LEU D 423      22.322  30.419 117.935  1.00 55.83           C  
-ATOM   8872  O   LEU D 423      22.656  31.599 118.046  1.00 56.04           O  
-ATOM   8873  CB  LEU D 423      21.902  29.497 120.209  1.00 55.01           C  
-ATOM   8874  CG  LEU D 423      20.957  29.105 121.346  1.00 55.00           C  
-ATOM   8875  CD1 LEU D 423      21.679  28.228 122.350  1.00 54.64           C  
-ATOM   8876  CD2 LEU D 423      20.351  30.332 122.026  1.00 55.07           C  
-ATOM   8877  N   LEU D 424      22.847  29.595 117.033  1.00 56.76           N  
-ATOM   8878  CA  LEU D 424      23.839  30.036 116.058  1.00 57.75           C  
-ATOM   8879  C   LEU D 424      23.278  31.136 115.159  1.00 58.62           C  
-ATOM   8880  O   LEU D 424      22.072  31.179 114.892  1.00 58.77           O  
-ATOM   8881  CB  LEU D 424      24.324  28.854 115.210  1.00 57.56           C  
-ATOM   8882  CG  LEU D 424      24.753  27.552 115.902  1.00 57.33           C  
-ATOM   8883  CD1 LEU D 424      25.248  26.551 114.870  1.00 56.92           C  
-ATOM   8884  CD2 LEU D 424      25.812  27.774 116.982  1.00 56.95           C  
-ATOM   8885  N   ASN D 425      24.150  32.037 114.715  1.00 59.57           N  
-ATOM   8886  CA  ASN D 425      23.741  33.109 113.813  1.00 60.64           C  
-ATOM   8887  C   ASN D 425      23.815  32.644 112.361  1.00 61.26           C  
-ATOM   8888  O   ASN D 425      24.817  32.059 111.949  1.00 61.27           O  
-ATOM   8889  CB  ASN D 425      24.586  34.376 114.024  1.00 60.77           C  
-ATOM   8890  CG  ASN D 425      25.100  34.512 115.452  1.00 61.24           C  
-ATOM   8891  OD1 ASN D 425      24.323  34.643 116.402  1.00 61.89           O  
-ATOM   8892  ND2 ASN D 425      26.419  34.483 115.605  1.00 61.63           N  
-ATOM   8893  N   PRO D 426      22.752  32.888 111.595  1.00 62.06           N  
-ATOM   8894  CA  PRO D 426      22.709  32.490 110.181  1.00 62.69           C  
-ATOM   8895  C   PRO D 426      23.630  33.362 109.327  1.00 63.49           C  
-ATOM   8896  O   PRO D 426      23.898  34.497 109.720  1.00 63.61           O  
-ATOM   8897  CB  PRO D 426      21.245  32.732 109.795  1.00 62.59           C  
-ATOM   8898  CG  PRO D 426      20.758  33.770 110.746  1.00 62.31           C  
-ATOM   8899  CD  PRO D 426      21.509  33.559 112.021  1.00 62.01           C  
-ATOM   8900  N   PRO D 427      24.109  32.851 108.193  1.00 64.31           N  
-ATOM   8901  CA  PRO D 427      24.917  33.660 107.271  1.00 64.91           C  
-ATOM   8902  C   PRO D 427      24.114  34.844 106.744  1.00 65.61           C  
-ATOM   8903  O   PRO D 427      22.921  34.691 106.469  1.00 65.62           O  
-ATOM   8904  CB  PRO D 427      25.243  32.685 106.134  1.00 64.88           C  
-ATOM   8905  CG  PRO D 427      24.213  31.607 106.241  1.00 64.76           C  
-ATOM   8906  CD  PRO D 427      23.927  31.472 107.703  1.00 64.36           C  
-ATOM   8907  N   GLU D 428      24.756  36.005 106.624  1.00 66.47           N  
-ATOM   8908  CA  GLU D 428      24.093  37.210 106.121  1.00 67.33           C  
-ATOM   8909  C   GLU D 428      23.749  37.087 104.639  1.00 67.80           C  
-ATOM   8910  O   GLU D 428      22.689  37.541 104.204  1.00 67.79           O  
-ATOM   8911  CB  GLU D 428      24.924  38.476 106.397  1.00 67.41           C  
-ATOM   8912  CG  GLU D 428      26.419  38.369 106.109  1.00 68.21           C  
-ATOM   8913  CD  GLU D 428      27.008  39.638 105.501  1.00 69.52           C  
-ATOM   8914  OE1 GLU D 428      26.685  40.751 105.988  1.00 69.41           O  
-ATOM   8915  OE2 GLU D 428      27.801  39.521 104.535  1.00 69.46           O  
-ATOM   8916  N   THR D 429      24.648  36.465 103.879  1.00 68.60           N  
-ATOM   8917  CA  THR D 429      24.459  36.237 102.446  1.00 69.43           C  
-ATOM   8918  C   THR D 429      24.834  34.805 102.084  1.00 69.99           C  
-ATOM   8919  O   THR D 429      25.575  34.143 102.813  1.00 70.03           O  
-ATOM   8920  CB  THR D 429      25.307  37.224 101.600  1.00 69.46           C  
-ATOM   8921  OG1 THR D 429      26.599  37.398 102.200  1.00 69.37           O  
-ATOM   8922  CG2 THR D 429      24.701  38.631 101.612  1.00 69.53           C  
-ATOM   8923  N   LEU D 430      24.329  34.340 100.946  1.00 70.83           N  
-ATOM   8924  CA  LEU D 430      24.573  32.973 100.494  1.00 71.69           C  
-ATOM   8925  C   LEU D 430      25.674  32.888  99.439  1.00 72.22           C  
-ATOM   8926  O   LEU D 430      26.465  31.941  99.438  1.00 72.32           O  
-ATOM   8927  CB  LEU D 430      23.275  32.345  99.975  1.00 71.61           C  
-ATOM   8928  CG  LEU D 430      22.654  31.216 100.809  1.00 71.67           C  
-ATOM   8929  CD1 LEU D 430      22.875  31.408 102.310  1.00 71.61           C  
-ATOM   8930  CD2 LEU D 430      21.173  31.084 100.497  1.00 71.39           C  
-ATOM   8931  N   ASN D 431      25.708  33.885  98.554  1.00 72.92           N  
-ATOM   8932  CA  ASN D 431      26.713  34.002  97.492  1.00 73.56           C  
-ATOM   8933  C   ASN D 431      26.680  32.846  96.484  1.00 73.96           C  
-ATOM   8934  O   ASN D 431      27.714  32.270  96.130  1.00 74.12           O  
-ATOM   8935  CB  ASN D 431      28.121  34.218  98.078  1.00 73.63           C  
-ATOM   8936  CG  ASN D 431      28.138  35.250  99.201  1.00 73.80           C  
-ATOM   8937  OD1 ASN D 431      28.278  34.903 100.374  1.00 73.99           O  
-ATOM   8938  ND2 ASN D 431      27.988  36.524  98.843  1.00 73.90           N  
-ATOM   8939  N   LEU D 432      25.473  32.524  96.024  1.00 74.42           N  
-ATOM   8940  CA  LEU D 432      25.265  31.477  95.024  1.00 74.72           C  
-ATOM   8941  C   LEU D 432      24.936  32.084  93.659  1.00 74.80           C  
-ATOM   8942  O   LEU D 432      24.582  33.261  93.541  1.00 74.87           O  
-ATOM   8943  CB  LEU D 432      24.148  30.511  95.459  1.00 74.80           C  
-ATOM   8944  CG  LEU D 432      23.853  30.242  96.944  1.00 74.95           C  
-ATOM   8945  CD1 LEU D 432      22.524  29.522  97.091  1.00 75.30           C  
-ATOM   8946  CD2 LEU D 432      24.961  29.442  97.621  1.00 74.96           C  
-ATOM   8947  OXT LEU D 432      25.009  31.428  92.617  1.00 74.95           O  
-TER    8948      LEU D 432                                                      
-HETATM 8949  C1  TBS A 301       7.536  44.823  50.568  1.00 56.12           C  
-HETATM 8950  C2  TBS A 301       8.541  45.520  51.172  1.00 54.24           C  
-HETATM 8951  C3  TBS A 301       8.205  46.462  52.106  1.00 56.70           C  
-HETATM 8952  C4  TBS A 301       6.210  45.057  50.882  1.00 59.16           C  
-HETATM 8953  N5  TBS A 301       4.619  46.415  52.292  1.00 58.98           N  
-HETATM 8954  C6  TBS A 301       5.849  46.004  51.817  1.00 59.00           C  
-HETATM 8955  C7  TBS A 301       6.905  46.744  52.464  1.00 58.56           C  
-HETATM 8956  N8  TBS A 301       6.371  47.648  53.362  1.00 58.77           N  
-HETATM 8957  N9  TBS A 301       4.962  47.431  53.241  1.00 59.24           N  
-HETATM 8958 BR10 TBS A 301       4.858  44.086  50.030  1.00 65.59          BR  
-HETATM 8959 BR11 TBS A 301       8.072  43.545  49.311  1.00 57.43          BR  
-HETATM 8960 BR12 TBS A 301      10.349  45.157  50.717  1.00 40.21          BR  
-HETATM 8961 BR13 TBS A 301       9.598  47.386  52.901  1.00 63.69          BR  
-HETATM 8962  C1  TBS C 302      -4.121 -17.557 103.890  1.00 69.03           C  
-HETATM 8963  C2  TBS C 302      -4.149 -16.205 103.602  1.00 66.72           C  
-HETATM 8964  C3  TBS C 302      -3.996 -15.289 104.623  1.00 68.96           C  
-HETATM 8965  C4  TBS C 302      -3.941 -17.993 105.203  1.00 72.14           C  
-HETATM 8966  N5  TBS C 302      -3.601 -17.294 107.593  1.00 72.60           N  
-HETATM 8967  C6  TBS C 302      -3.788 -17.095 106.238  1.00 72.25           C  
-HETATM 8968  C7  TBS C 302      -3.815 -15.680 105.937  1.00 71.51           C  
-HETATM 8969  N8  TBS C 302      -3.648 -14.950 107.102  1.00 72.20           N  
-HETATM 8970  N9  TBS C 302      -3.517 -15.961 108.106  1.00 73.10           N  
-HETATM 8971 BR10 TBS C 302      -3.883 -19.818 105.662  1.00 78.07          BR  
-HETATM 8972 BR11 TBS C 302      -4.338 -18.774 102.463  1.00 69.86          BR  
-HETATM 8973 BR12 TBS C 302      -4.381 -15.587 101.822  1.00 53.00          BR  
-HETATM 8974 BR13 TBS C 302      -4.041 -13.464 104.199  1.00 72.68          BR  
-HETATM 8975  O   HOH A 302       9.666  47.909  55.767  1.00 23.43           O  
-HETATM 8976  O   HOH A 303      -2.225  34.727  68.019  1.00 20.30           O  
-HETATM 8977  O   HOH A 304      18.755  42.589  54.777  1.00 16.90           O  
-HETATM 8978  O   HOH A 305      21.390  38.357  66.145  1.00 16.52           O  
-HETATM 8979  O   HOH A 306      12.243  32.598  52.004  1.00 17.79           O  
-HETATM 8980  O   HOH A 307      12.087  56.068  69.013  1.00 19.66           O  
-HETATM 8981  O   HOH A 308      15.167  29.080  54.795  1.00 28.01           O  
-HETATM 8982  O   HOH A 309      -4.162  46.323  75.520  1.00 25.74           O  
-HETATM 8983  O   HOH A 310       3.324  41.466  71.983  1.00 16.27           O  
-HETATM 8984  O   HOH A 311       7.204  48.488  63.881  1.00 18.08           O  
-HETATM 8985  O   HOH A 312       2.749  46.594  79.915  1.00 29.50           O  
-HETATM 8986  O   HOH A 313       2.460  48.466  67.788  1.00 21.74           O  
-HETATM 8987  O   HOH A 314      -0.556  33.414  66.043  1.00 14.71           O  
-HETATM 8988  O   HOH A 315       7.494  43.297  78.644  1.00 17.94           O  
-HETATM 8989  O   HOH A 316      21.294  49.366  42.716  1.00 17.08           O  
-HETATM 8990  O   HOH A 317      18.975  45.570  57.177  1.00 21.96           O  
-HETATM 8991  O   HOH A 318       6.016  41.612  85.529  1.00 23.02           O  
-HETATM 8992  O   HOH A 319      13.940  39.844  75.585  1.00 14.90           O  
-HETATM 8993  O   HOH A 320       2.796  30.460  79.998  1.00 18.71           O  
-HETATM 8994  O   HOH A 321      12.742  38.437  79.153  1.00 29.73           O  
-HETATM 8995  O   HOH A 322       5.678  42.651  68.283  1.00 15.59           O  
-HETATM 8996  O   HOH A 323       7.521  50.502  78.458  1.00 18.45           O  
-HETATM 8997  O   HOH A 324      20.784  24.500  69.109  1.00 22.89           O  
-HETATM 8998  O   HOH A 325       4.585  41.150  49.458  1.00 34.53           O  
-HETATM 8999  O   HOH A 326      -1.974  13.054  74.870  1.00 28.29           O  
-HETATM 9000  O   HOH A 327      -1.444  37.486  72.093  1.00 18.08           O  
-HETATM 9001  O   HOH A 328      19.973  55.880  71.462  1.00 23.51           O  
-HETATM 9002  O   HOH A 329      18.387  50.864  43.555  1.00 30.38           O  
-HETATM 9003  O   HOH A 330     -13.239  38.770  66.338  1.00 47.86           O  
-HETATM 9004  O   HOH A 331      17.985  48.440  57.029  1.00 27.29           O  
-HETATM 9005  O   HOH A 332      18.345  60.755  44.774  1.00 61.45           O  
-HETATM 9006  O   HOH A 333      22.579  32.434  71.947  1.00 22.26           O  
-HETATM 9007  O   HOH A 334      21.491  48.241  46.418  1.00 24.03           O  
-HETATM 9008  O   HOH A 335     -11.866  44.646  76.119  1.00 25.42           O  
-HETATM 9009  O   HOH A 336       4.741  24.297  79.874  1.00 30.81           O  
-HETATM 9010  O   HOH A 337       6.743  44.232  81.258  1.00 24.68           O  
-HETATM 9011  O   HOH A 338      19.524  57.307  64.006  1.00 27.52           O  
-HETATM 9012  O   HOH A 339     -13.341  35.990  69.411  1.00 34.38           O  
-HETATM 9013  O   HOH A 340       6.646  54.031  66.289  1.00 27.37           O  
-HETATM 9014  O   HOH A 341     -15.537  35.233  88.519  1.00 34.55           O  
-HETATM 9015  O   HOH A 342      20.534  34.878  58.803  1.00 28.45           O  
-HETATM 9016  O   HOH A 343     -13.847  39.301  84.836  1.00 25.48           O  
-HETATM 9017  O   HOH A 344      13.348  55.279  77.734  1.00 23.91           O  
-HETATM 9018  O   HOH A 345      22.099  39.905  70.122  1.00 29.84           O  
-HETATM 9019  O   HOH A 346      -0.621  56.014  75.836  1.00 40.80           O  
-HETATM 9020  O   HOH A 347      14.115  48.007  81.615  1.00 32.65           O  
-HETATM 9021  O   HOH A 348      19.455  53.938  78.088  1.00 32.01           O  
-HETATM 9022  O   HOH A 349       2.275  24.168  58.714  1.00 28.30           O  
-HETATM 9023  O   HOH A 350       3.404  46.349  56.579  1.00 43.51           O  
-HETATM 9024  O   HOH A 351      10.324  42.956  78.584  1.00 46.45           O  
-HETATM 9025  O   HOH A 352       5.716  33.195  84.387  1.00 47.91           O  
-HETATM 9026  O   HOH A 353      22.828  56.543  66.513  1.00 32.21           O  
-HETATM 9027  O   HOH A 354      -5.572  41.414  65.697  1.00 35.76           O  
-HETATM 9028  O   HOH A 355      21.417  26.593  67.969  1.00 33.11           O  
-HETATM 9029  O   HOH A 356      -0.849  24.883  78.382  1.00 26.24           O  
-HETATM 9030  O   HOH A 357     -14.236  32.112  68.087  1.00 46.17           O  
-HETATM 9031  O   HOH A 358       2.994  62.396  63.304  1.00 38.14           O  
-HETATM 9032  O   HOH A 359      -5.067  21.864  69.707  1.00 36.04           O  
-HETATM 9033  O   HOH A 360       1.351  55.119  78.143  1.00 42.12           O  
-HETATM 9034  O   HOH A 361      -1.572  48.925  77.321  1.00 37.20           O  
-HETATM 9035  O   HOH A 362      21.415  45.101  55.376  1.00 41.35           O  
-HETATM 9036  O   HOH A 363      19.042  38.812  51.107  1.00 40.72           O  
-HETATM 9037  O   HOH A 364      -4.187  25.805  70.432  1.00 29.84           O  
-HETATM 9038  O   HOH A 365      -7.451  36.886  92.263  1.00 41.55           O  
-HETATM 9039  O   HOH A 366      18.908  35.600  50.668  1.00 39.97           O  
-HETATM 9040  O   HOH A 367      -6.666  32.396  61.910  1.00 46.76           O  
-HETATM 9041  O   HOH A 368       0.216  22.768  58.546  1.00 44.46           O  
-HETATM 9042  O   HOH A 369      15.206  22.480  76.386  1.00 40.63           O  
-HETATM 9043  O   HOH A 370      19.027  56.557  41.432  1.00 45.08           O  
-HETATM 9044  O   HOH A 371     -10.639  46.071  73.755  1.00 33.36           O  
-HETATM 9045  O   HOH A 372      16.560  34.655  78.428  1.00 29.53           O  
-HETATM 9046  O   HOH A 373      15.818  44.124  36.919  1.00 36.96           O  
-HETATM 9047  O   HOH A 374       3.200  46.559  35.109  1.00 47.37           O  
-HETATM 9048  O   HOH A 375      24.856  42.774  60.442  1.00 42.45           O  
-HETATM 9049  O   HOH A 376       3.854  50.664  68.316  1.00 25.91           O  
-HETATM 9050  O   HOH A 377       3.142  38.645  46.841  1.00 44.93           O  
-HETATM 9051  O   HOH A 378      -0.383  29.443  84.426  1.00 37.19           O  
-HETATM 9052  O   HOH A 379      -7.757  31.008  71.314  1.00 36.04           O  
-HETATM 9053  O   HOH A 380      -1.681  51.814  70.565  1.00 37.82           O  
-HETATM 9054  O   HOH A 381      -5.348  45.283  66.480  1.00 37.04           O  
-HETATM 9055  O   HOH A 382      12.493  17.070  69.776  1.00 39.67           O  
-HETATM 9056  O   HOH A 383     -13.143  42.004  89.757  1.00 44.51           O  
-HETATM 9057  O   HOH A 384       2.998  61.035  66.751  1.00 42.17           O  
-HETATM 9058  O   HOH A 385       2.451  22.945  81.310  1.00 45.60           O  
-HETATM 9059  O   HOH A 386       2.537  51.482  78.126  1.00 24.86           O  
-HETATM 9060  O   HOH A 387      -8.418  24.719  81.037  1.00 48.30           O  
-HETATM 9061  O   HOH A 388       4.858  51.095  79.061  1.00 31.75           O  
-HETATM 9062  O   HOH A 389       4.667  29.013  78.793  1.00 31.30           O  
-HETATM 9063  O   HOH A 390      -4.040  27.083  67.363  1.00 47.79           O  
-HETATM 9064  O   HOH A 391      -8.490  22.733  77.241  1.00 43.68           O  
-HETATM 9065  O   HOH A 392      14.210  20.575  74.883  1.00 36.17           O  
-HETATM 9066  O   HOH A 393     -11.538  30.029  72.550  1.00 45.05           O  
-HETATM 9067  O   HOH A 394     -15.312  40.880  73.330  1.00 48.69           O  
-HETATM 9068  O   HOH A 395       1.021  42.852  43.360  1.00 45.07           O  
-HETATM 9069  O   HOH A 396       4.760  51.780  59.078  1.00 44.86           O  
-HETATM 9070  O   HOH A 397      23.335  43.194  56.470  1.00 55.62           O  
-HETATM 9071  O   HOH A 398      -8.532  41.582  66.326  1.00 33.45           O  
-HETATM 9072  O   HOH A 399       6.752  48.485  55.556  1.00 47.20           O  
-HETATM 9073  O   HOH B 433      14.950  39.479  73.186  1.00 15.65           O  
-HETATM 9074  O   HOH B 434      30.422  82.836  66.691  1.00 33.41           O  
-HETATM 9075  O   HOH B 435      16.077  58.462  72.751  1.00 13.91           O  
-HETATM 9076  O   HOH B 436      19.372  76.740  85.699  1.00 23.64           O  
-HETATM 9077  O   HOH B 437      19.429  77.044  82.793  1.00 21.15           O  
-HETATM 9078  O   HOH B 438      32.197  56.201  73.568  1.00 22.14           O  
-HETATM 9079  O   HOH B 439      21.878  71.401  94.204  1.00 26.84           O  
-HETATM 9080  O   HOH B 440      22.803  64.831  76.000  1.00 18.08           O  
-HETATM 9081  O   HOH B 441       6.215  60.512  76.257  1.00 31.48           O  
-HETATM 9082  O   HOH B 442      27.670  62.386  71.125  1.00 19.83           O  
-HETATM 9083  O   HOH B 443      29.063  67.462  75.120  1.00 34.63           O  
-HETATM 9084  O   HOH B 444      13.357  61.364  79.804  1.00 22.37           O  
-HETATM 9085  O   HOH B 445      36.371  53.296  78.065  1.00 28.83           O  
-HETATM 9086  O   HOH B 446      22.051  77.460  83.190  1.00 21.64           O  
-HETATM 9087  O   HOH B 447      12.401  56.769  71.586  1.00 28.28           O  
-HETATM 9088  O   HOH B 448      18.166  57.978  70.818  1.00 16.94           O  
-HETATM 9089  O   HOH B 449      25.713  68.329  77.434  1.00 26.34           O  
-HETATM 9090  O   HOH B 450      24.688  75.780  82.820  1.00 24.83           O  
-HETATM 9091  O   HOH B 451      38.196  55.891  90.257  1.00 34.79           O  
-HETATM 9092  O   HOH B 452      36.873  63.960  81.541  1.00 23.77           O  
-HETATM 9093  O   HOH B 453      23.597  48.914  80.289  1.00 33.21           O  
-HETATM 9094  O   HOH B 454      26.201  82.282  62.395  1.00 29.80           O  
-HETATM 9095  O   HOH B 455      11.426  63.758  82.225  1.00 33.00           O  
-HETATM 9096  O   HOH B 456       6.049  63.573  78.115  1.00 25.90           O  
-HETATM 9097  O   HOH B 457      26.807  71.784  76.080  1.00 21.48           O  
-HETATM 9098  O   HOH B 458      30.946  82.292  71.450  1.00 36.31           O  
-HETATM 9099  O   HOH B 459      29.086  76.131  82.965  1.00 29.70           O  
-HETATM 9100  O   HOH B 460      39.793  67.597  94.355  1.00 47.59           O  
-HETATM 9101  O   HOH B 461      29.779  78.462  76.781  1.00 36.38           O  
-HETATM 9102  O   HOH B 462       8.141  68.973  57.450  1.00 28.44           O  
-HETATM 9103  O   HOH B 463      24.493  64.175  58.389  1.00 34.51           O  
-HETATM 9104  O   HOH B 464      12.247  70.761  80.389  1.00 26.60           O  
-HETATM 9105  O   HOH B 465      26.943  77.679  86.499  1.00 33.61           O  
-HETATM 9106  O   HOH B 466      26.174  77.544  74.913  1.00 31.45           O  
-HETATM 9107  O   HOH B 467      24.304  42.279  76.134  1.00 33.62           O  
-HETATM 9108  O   HOH B 468      19.011  87.759  62.040  1.00 37.15           O  
-HETATM 9109  O   HOH B 469      17.720  53.985  86.145  1.00 24.87           O  
-HETATM 9110  O   HOH B 470      32.921  75.103  84.606  1.00 31.65           O  
-HETATM 9111  O   HOH B 471      16.775  81.944  82.526  1.00 35.68           O  
-HETATM 9112  O   HOH B 472      34.888  63.021  76.095  1.00 25.43           O  
-HETATM 9113  O   HOH B 473      32.471  75.449  69.416  1.00 52.14           O  
-HETATM 9114  O   HOH B 474      22.717  56.160  95.232  1.00 42.27           O  
-HETATM 9115  O   HOH B 475      21.342  56.457 100.187  1.00 42.75           O  
-HETATM 9116  O   HOH B 476      31.496  50.078  71.315  1.00 26.53           O  
-HETATM 9117  O   HOH B 477      38.797  70.576  83.704  1.00 33.60           O  
-HETATM 9118  O   HOH B 478      33.029  65.713  66.433  1.00 37.44           O  
-HETATM 9119  O   HOH B 479      30.072  46.098  86.245  1.00 33.46           O  
-HETATM 9120  O   HOH B 480      23.840  83.522  77.587  1.00 46.22           O  
-HETATM 9121  O   HOH B 481      34.885  63.517  94.911  1.00 29.79           O  
-HETATM 9122  O   HOH B 482      21.352  74.946  92.350  1.00 28.30           O  
-HETATM 9123  O   HOH B 483      15.262  59.981  82.699  1.00 40.99           O  
-HETATM 9124  O   HOH B 484      21.873  77.978  86.315  1.00 35.50           O  
-HETATM 9125  O   HOH B 485       8.807  87.784  62.937  1.00 58.73           O  
-HETATM 9126  O   HOH B 486      33.060  50.397  94.992  1.00 33.51           O  
-HETATM 9127  O   HOH B 487      27.563  46.973  80.390  1.00 35.59           O  
-HETATM 9128  O   HOH B 488      36.556  72.665  89.795  1.00 40.16           O  
-HETATM 9129  O   HOH B 489      32.176  55.138  97.699  1.00 45.33           O  
-HETATM 9130  O   HOH B 490      28.215  82.096  56.610  1.00 41.53           O  
-HETATM 9131  O   HOH B 491      18.428  66.080  82.382  1.00 42.85           O  
-HETATM 9132  O   HOH B 492       3.576  66.152  76.789  1.00 44.78           O  
-HETATM 9133  O   HOH B 493      19.252  53.684  75.193  1.00 35.21           O  
-HETATM 9134  O   HOH B 494      37.814  72.500  80.304  1.00 40.86           O  
-HETATM 9135  O   HOH B 495      15.802  81.919  77.451  1.00 33.27           O  
-HETATM 9136  O   HOH B 496      22.823  69.548 100.925  1.00 50.08           O  
-HETATM 9137  O   HOH B 497      16.467  83.428  66.733  1.00 35.56           O  
-HETATM 9138  O   HOH B 498      18.575  55.055  99.695  1.00 44.33           O  
-HETATM 9139  O   HOH B 499      33.373  53.785  70.795  1.00 39.17           O  
-HETATM 9140  O   HOH B 500      32.566  49.945  78.032  1.00 28.03           O  
-HETATM 9141  O   HOH B 501      22.373  65.656  73.552  1.00 34.98           O  
-HETATM 9142  O   HOH B 502      26.346  68.344  61.101  1.00 45.82           O  
-HETATM 9143  O   HOH B 503      35.165  57.704  75.826  1.00 32.86           O  
-HETATM 9144  O   HOH C 303      -1.475 -12.058 105.003  1.00 24.88           O  
-HETATM 9145  O   HOH C 304     -12.444   4.017 125.182  1.00 45.38           O  
-HETATM 9146  O   HOH C 305      -2.140 -12.911 107.236  1.00 37.92           O  
-HETATM 9147  O   HOH C 306      17.927 -18.427 114.381  1.00 27.76           O  
-HETATM 9148  O   HOH C 307     -17.517  -3.497  99.959  1.00 39.20           O  
-HETATM 9149  O   HOH C 308       3.191 -23.631  94.975  1.00 25.92           O  
-HETATM 9150  O   HOH C 309      29.990 -29.883 117.365  1.00 49.08           O  
-HETATM 9151  O   HOH C 310       1.600   3.790 102.289  1.00 35.29           O  
-HETATM 9152  O   HOH C 311      14.540 -23.332 110.175  1.00 26.01           O  
-HETATM 9153  O   HOH C 312      15.321 -22.535 112.612  1.00 30.05           O  
-HETATM 9154  O   HOH C 313       5.552  -8.919 109.318  1.00 22.50           O  
-HETATM 9155  O   HOH C 314     -13.796 -10.700  92.268  1.00 25.18           O  
-HETATM 9156  O   HOH C 315      16.732 -27.779 108.811  1.00 41.63           O  
-HETATM 9157  O   HOH C 316      11.930 -12.289 109.375  1.00 27.43           O  
-HETATM 9158  O   HOH C 317      -4.132 -30.418  97.549  1.00 66.86           O  
-HETATM 9159  O   HOH C 318       6.405   1.433 109.519  1.00 22.92           O  
-HETATM 9160  O   HOH C 319     -15.494   0.352 103.064  1.00 43.39           O  
-HETATM 9161  O   HOH C 320       1.531   0.083 118.938  1.00 42.83           O  
-HETATM 9162  O   HOH C 321      12.053  -2.054 121.631  1.00 39.70           O  
-HETATM 9163  O   HOH C 322     -13.460 -10.654  95.608  1.00 29.85           O  
-HETATM 9164  O   HOH C 323       7.724 -23.576  91.688  1.00 36.12           O  
-HETATM 9165  O   HOH C 324       0.519 -11.695  94.283  1.00 39.10           O  
-HETATM 9166  O   HOH C 325      17.060  -1.219 113.835  1.00 33.17           O  
-HETATM 9167  O   HOH C 326      27.301 -17.766 131.117  1.00 49.19           O  
-HETATM 9168  O   HOH C 327      -1.909  -0.328 118.440  1.00 36.76           O  
-HETATM 9169  O   HOH C 328      28.598 -13.503 100.715  1.00 58.52           O  
-HETATM 9170  O   HOH C 329      15.996 -13.003 111.941  1.00 25.67           O  
-HETATM 9171  O   HOH C 330      20.326  -7.279 102.823  1.00 34.47           O  
-HETATM 9172  O   HOH C 331     -21.583 -12.044 103.983  1.00 48.70           O  
-HETATM 9173  O   HOH C 332       6.564 -32.646  98.351  1.00 49.83           O  
-HETATM 9174  O   HOH C 333       4.266   6.065  99.328  1.00 44.31           O  
-HETATM 9175  O   HOH C 334      12.755 -31.925 101.761  1.00 43.88           O  
-HETATM 9176  O   HOH C 335       6.539 -33.058 110.510  1.00 38.33           O  
-HETATM 9177  O   HOH C 336       5.223 -37.140 103.598  1.00 38.41           O  
-HETATM 9178  O   HOH C 337      -1.650  -5.215  94.388  1.00 51.81           O  
-HETATM 9179  O   HOH C 338      -3.018 -22.653 105.368  1.00 47.02           O  
-HETATM 9180  O   HOH D 433      21.063  28.800 114.288  1.00 48.67           O  
-HETATM 9181  O   HOH D 434      23.264   2.528 105.519  1.00 46.84           O  
-HETATM 9182  O   HOH D 435      -8.933  23.521 116.254  1.00 24.55           O  
-HETATM 9183  O   HOH D 436     -10.085   4.731 115.214  1.00 23.28           O  
-HETATM 9184  O   HOH D 437     -12.459  25.378 106.108  1.00 24.84           O  
-HETATM 9185  O   HOH D 438      18.467  -8.046 101.337  1.00 28.29           O  
-HETATM 9186  O   HOH D 439      16.698  13.519  95.970  1.00 46.74           O  
-HETATM 9187  O   HOH D 440       7.283   6.674 105.667  1.00 26.20           O  
-HETATM 9188  O   HOH D 441       6.262  20.553 100.886  1.00 41.95           O  
-HETATM 9189  O   HOH D 442      -4.495  32.447 113.020  1.00 32.31           O  
-HETATM 9190  O   HOH D 443       8.535  16.326 105.625  1.00 31.03           O  
-HETATM 9191  O   HOH D 444       2.489  30.341 105.252  1.00 32.35           O  
-HETATM 9192  O   HOH D 445       0.842  27.288 107.461  1.00 31.73           O  
-HETATM 9193  O   HOH D 446       3.729   1.562 116.772  1.00 37.19           O  
-HETATM 9194  O   HOH D 447       8.597  28.532 109.899  1.00 34.99           O  
-HETATM 9195  O   HOH D 448       5.312  28.959 119.634  1.00 41.14           O  
-HETATM 9196  O   HOH D 449      -3.462  32.228 104.171  1.00 49.93           O  
-HETATM 9197  O   HOH D 450       8.604   6.632 108.041  1.00 24.34           O  
-HETATM 9198  O   HOH D 451      29.975  18.091 108.213  1.00 45.37           O  
-HETATM 9199  O   HOH D 452      -2.907  33.126 106.997  1.00 35.49           O  
-HETATM 9200  O   HOH D 453       7.789  27.032 115.605  1.00 33.62           O  
-HETATM 9201  O   HOH D 454     -15.942  19.717 119.476  1.00 40.10           O  
-HETATM 9202  O   HOH D 455      14.117  12.741 116.366  1.00 40.95           O  
-HETATM 9203  O   HOH D 456       8.150  21.122 105.479  1.00 40.57           O  
-HETATM 9204  O   HOH D 457     -10.044  21.180 100.846  1.00 34.06           O  
-HETATM 9205  O   HOH D 458      14.535  24.650  94.578  1.00 41.17           O  
-HETATM 9206  O   HOH D 459      22.785  -5.123 101.992  1.00 47.41           O  
-HETATM 9207  O   HOH D 460      13.202  10.466 113.565  1.00 40.06           O  
-HETATM 9208  O   HOH D 461      12.647  23.407 126.115  1.00 45.87           O  
-HETATM 9209  O   HOH D 462      -7.151  11.995 128.864  1.00 40.22           O  
-HETATM 9210  O   HOH D 463      -2.644  25.541 100.996  1.00 54.34           O  
-HETATM 9211  O   HOH D 464       8.616   5.272 120.776  1.00 37.17           O  
-HETATM 9212  O   HOH D 465      10.986  32.937 109.985  1.00 48.05           O  
-HETATM 9213  O   HOH D 466      -9.279  33.468 113.139  1.00 39.05           O  
-HETATM 9214  O   HOH D 467      -3.211   9.412  99.347  1.00 47.24           O  
-HETATM 9215  O   HOH D 468       3.951   8.281 126.282  1.00 44.57           O  
-HETATM 9216  O   HOH D 469     -16.063  27.859 112.369  1.00 57.44           O  
-CONECT 1267 1277                                                                
-CONECT 1277 1267 1278                                                           
-CONECT 1278 1277 1279 1286                                                      
-CONECT 1279 1278 1280 1281                                                      
-CONECT 1280 1279                                                                
-CONECT 1281 1279 1282                                                           
-CONECT 1282 1281 1283 1284 1285                                                 
-CONECT 1283 1282                                                                
-CONECT 1284 1282                                                                
-CONECT 1285 1282                                                                
-CONECT 1286 1278 1287 1288                                                      
-CONECT 1287 1286                                                                
-CONECT 1288 1286                                                                
-CONECT 5741 5751                                                                
-CONECT 5751 5741 5752                                                           
-CONECT 5752 5751 5753 5760                                                      
-CONECT 5753 5752 5754 5755                                                      
-CONECT 5754 5753                                                                
-CONECT 5755 5753 5756                                                           
-CONECT 5756 5755 5757 5758 5759                                                 
-CONECT 5757 5756                                                                
-CONECT 5758 5756                                                                
-CONECT 5759 5756                                                                
-CONECT 5760 5752 5761 5762                                                      
-CONECT 5761 5760                                                                
-CONECT 5762 5760                                                                
-CONECT 8949 8950 8952 8959                                                      
-CONECT 8950 8949 8951 8960                                                      
-CONECT 8951 8950 8955 8961                                                      
-CONECT 8952 8949 8954 8958                                                      
-CONECT 8953 8954 8957                                                           
-CONECT 8954 8952 8953 8955                                                      
-CONECT 8955 8951 8954 8956                                                      
-CONECT 8956 8955 8957                                                           
-CONECT 8957 8953 8956                                                           
-CONECT 8958 8952                                                                
-CONECT 8959 8949                                                                
-CONECT 8960 8950                                                                
-CONECT 8961 8951                                                                
-CONECT 8962 8963 8965 8972                                                      
-CONECT 8963 8962 8964 8973                                                      
-CONECT 8964 8963 8968 8974                                                      
-CONECT 8965 8962 8967 8971                                                      
-CONECT 8966 8967 8970                                                           
-CONECT 8967 8965 8966 8968                                                      
-CONECT 8968 8964 8967 8969                                                      
-CONECT 8969 8968 8970                                                           
-CONECT 8970 8966 8969                                                           
-CONECT 8971 8965                                                                
-CONECT 8972 8962                                                                
-CONECT 8973 8963                                                                
-CONECT 8974 8964                                                                
-MASTER      314    0    4   63   20    0    6    6 9212    4   52   86          
-END                                                                             
diff --git a/plip/test/pdb/1vsn.pdb b/plip/test/pdb/1vsn.pdb
deleted file mode 100644
index cb841ca..0000000
--- a/plip/test/pdb/1vsn.pdb
+++ /dev/null
@@ -1,2355 +0,0 @@
-HEADER    HYDROLASE                               19-MAR-07   1VSN              
-TITLE     CRYSTAL STRUCTURE OF A POTENT SMALL MOLECULE INHIBITOR                
-TITLE    2 BOUND TO CATHEPSIN K                                                 
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CATHEPSIN K;                                               
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 FRAGMENT: CATHEPSIN K;                                               
-COMPND   5 SYNONYM: CATHEPSIN O, CATHEPSIN X, CATHEPSIN O2;                     
-COMPND   6 EC: 3.4.22.38;                                                       
-COMPND   7 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: CTSK, CTSO, CTSO2;                                             
-SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
-SOURCE   8 EXPRESSION_SYSTEM_STRAIN: GS 115                                     
-KEYWDS    OSTEOPOROSIS, STRUCTURE-GUIDED DRUG DESIGN, PROTEAE,                  
-KEYWDS   2 HYDROLASE                                                            
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    M.MCGRATH                                                             
-REVDAT   2   24-FEB-09 1VSN    1       VERSN                                    
-REVDAT   1   24-APR-07 1VSN    0                                                
-SPRSDE     24-APR-07 1VSN      2FDZ                                             
-JRNL        AUTH   C.S.LI,D.DESCHENES,S.DESMARAIS,J.P.FALGUEYRET,               
-JRNL        AUTH 2 J.Y.GAUTHIER,D.B.KIMMEL,M.E.MCGRATH,D.J.MCKAY,               
-JRNL        AUTH 3 M.D.PERCIVAL,D.RIENDEAU,S.B.RODAN,V.L.TRUONG,                
-JRNL        AUTH 4 G.WESOLOWSKI,R.ZAMBONI,W.C.BLACK                             
-JRNL        TITL   IDENTIFICATION OF A POTENT AND SELECTIVE NON-BASIC           
-JRNL        TITL 2 CATHEPSIN K INHIBITOR.                                       
-JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  1985 2006              
-JRNL        REFN                   ISSN 0960-894X                               
-JRNL        PMID   16413777                                                     
-JRNL        DOI    10.1016/J.BMCL.2005.12.071                                   
-REMARK   1                                                                      
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS                                                  
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.1                           
-REMARK   3   NUMBER OF REFLECTIONS             : 13292                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.171                           
-REMARK   3   FREE R VALUE                     : 0.209                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.400                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1333                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
-REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
-REMARK   3   BIN FREE R VALUE                    : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 1615                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 33                                      
-REMARK   3   SOLVENT ATOMS            : 269                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.47                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
-REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.680                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
-REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : NULL                                                 
-REMARK   3   KSOL        : NULL                                                 
-REMARK   3   BSOL        : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 1VSN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-07.                  
-REMARK 100 THE RCSB ID CODE IS RCSB003012.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-02                          
-REMARK 200  TEMPERATURE           (KELVIN) : 298                                
-REMARK 200  PH                             : 5.6                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : N                                  
-REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
-REMARK 200  MONOCHROMATOR                  : NI FILTER                          
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
-REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : BIOTEX                             
-REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16006                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.730                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 30.620                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 71.6                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 10.9                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
-REMARK 200 SOFTWARE USED: XTALVIEW                                              
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 44.48                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: MG FORMATE, PH 5.6, VAPOR                
-REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       19.21000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.10000            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.50000            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.10000            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.21000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.50000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    LEU A  46   CA  -  CB  -  CG  ANGL. DEV. =  18.8 DEGREES          
-REMARK 500    ARG A1078   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
-REMARK 500    ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.1 DEGREES          
-REMARK 500    ARG A 108   NE  -  CZ  -  NH2 ANGL. DEV. =   5.1 DEGREES          
-REMARK 500    ARG A 111   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES          
-REMARK 500    LEU A 162   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
-REMARK 500    LYS A 193   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    TYR A  86       77.91   -154.23                                   
-REMARK 500    SER A 145      114.53   -171.18                                   
-REMARK 500    ALA A 146      149.94     63.54                                   
-REMARK 500    LYS A 193       57.94   -113.71                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A4315        DISTANCE =  5.25 ANGSTROMS                       
-REMARK 525    HOH A4324        DISTANCE =  6.29 ANGSTROMS                       
-REMARK 525    HOH A4326        DISTANCE =  5.25 ANGSTROMS                       
-REMARK 525    HOH A4355        DISTANCE =  6.75 ANGSTROMS                       
-REMARK 525    HOH A4357        DISTANCE =  6.86 ANGSTROMS                       
-REMARK 525    HOH A4371        DISTANCE =  8.11 ANGSTROMS                       
-REMARK 525    HOH A4397        DISTANCE =  5.57 ANGSTROMS                       
-REMARK 525    HOH A4409        DISTANCE =  6.66 ANGSTROMS                       
-REMARK 525    HOH A4417        DISTANCE =  6.65 ANGSTROMS                       
-REMARK 525    HOH A4419        DISTANCE =  7.91 ANGSTROMS                       
-REMARK 525    HOH A4429        DISTANCE =  6.66 ANGSTROMS                       
-REMARK 525    HOH A4433        DISTANCE =  6.94 ANGSTROMS                       
-REMARK 525    HOH A4434        DISTANCE =  7.13 ANGSTROMS                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NFT A 283                 
-DBREF  1VSN A    1   211  UNP    P43235   CATK_HUMAN     115    329             
-SEQADV 1VSN ILE A    5  UNP  P43235    VAL   119 CONFLICT                       
-SEQADV 1VSN ALA A   41  UNP  P43235    LYS   155 CONFLICT                       
-SEQADV 1VSN ALA A   44  UNP  P43235    LYS   158 CONFLICT                       
-SEQADV 1VSN ALA A   49  UNP  P43235    SER   163 CONFLICT                       
-SEQADV 1VSN ARG A   77  UNP  P43235    LYS   191 CONFLICT                       
-SEQADV 1VSN ASP A   92  UNP  P43235    GLU   207 CONFLICT                       
-SEQADV 1VSN ALA A  119  UNP  P43235    LYS   233 CONFLICT                       
-SEQADV 1VSN ALA A  127  UNP  P43235    ARG   241 CONFLICT                       
-SEQADV 1VSN ALA A  146  UNP  P43235    LYS   261 CONFLICT                       
-SEQADV 1VSN ASN A  152  UNP  P43235    SER   268 CONFLICT                       
-SEQADV 1VSN SER A  154  UNP  P43235    ASN   270 CONFLICT                       
-SEQADV 1VSN ALA A 1156  UNP  P43235    ASN   273 CONFLICT                       
-SEQADV 1VSN ALA A 2168  UNP  P43235    LYS   287 CONFLICT                       
-SEQADV 1VSN SER A  176  UNP  P43235    ASN   301 CONFLICT                       
-SEQADV 1VSN ALA A  184  UNP  P43235    LYS   305 CONFLICT                       
-SEQRES   1 A  215  ALA PRO ASP SER ILE ASP TYR ARG LYS LYS GLY TYR VAL          
-SEQRES   2 A  215  THR PRO VAL LYS ASN GLN GLY GLN CYS GLY SER CYS TRP          
-SEQRES   3 A  215  ALA PHE SER SER VAL GLY ALA LEU GLU GLY GLN LEU LYS          
-SEQRES   4 A  215  LYS ALA THR GLY ALA LEU LEU ASN LEU ALA PRO GLN ASN          
-SEQRES   5 A  215  LEU VAL ASP CYS VAL SER GLU ASN ASP GLY CYS GLY GLY          
-SEQRES   6 A  215  GLY TYR MET THR ASN ALA PHE GLN TYR VAL GLN ARG ASN          
-SEQRES   7 A  215  ARG GLY ILE ASP SER GLU ASP ALA TYR PRO TYR VAL GLY          
-SEQRES   8 A  215  GLN ASP GLU SER CYS MET TYR ASN PRO THR GLY LYS ALA          
-SEQRES   9 A  215  ALA LYS CYS ARG GLY TYR ARG GLU ILE PRO GLU GLY ASN          
-SEQRES  10 A  215  GLU ALA ALA LEU LYS ARG ALA VAL ALA ALA VAL GLY PRO          
-SEQRES  11 A  215  VAL SER VAL ALA ILE ASP ALA SER LEU THR SER PHE GLN          
-SEQRES  12 A  215  PHE TYR SER ALA GLY VAL TYR TYR ASP GLU ASN CYS SER          
-SEQRES  13 A  215  SER ASP ALA LEU ASN HIS ALA VAL LEU ALA VAL GLY TYR          
-SEQRES  14 A  215  GLY ILE GLN ALA GLY ASN LYS HIS TRP ILE ILE LYS ASN          
-SEQRES  15 A  215  SER TRP GLY GLU SER TRP GLY ASN ALA GLY TYR ILE LEU          
-SEQRES  16 A  215  MET ALA ARG ASN LYS ASN ASN ALA CYS GLY ILE ALA ASN          
-SEQRES  17 A  215  LEU ALA SER PHE PRO LYS MET                                  
-HET    NFT  A 283      33                                                       
-HETNAM     NFT N-(2-AMINOETHYL)-N~2~-{(1S)-1-[4'-(AMINOSULFONYL)                
-HETNAM   2 NFT  BIPHENYL-4-YL]-2,2,2-TRIFLUOROETHYL}-L-LEUCINAMIDE              
-FORMUL   2  NFT    C22 H29 F3 N4 O3 S                                           
-FORMUL   3  HOH   *269(H2 O)                                                    
-HELIX    1   1 SER A   24  GLY A   43  1                                  20    
-HELIX    2   2 ALA A   49  VAL A   57  1                                   9    
-HELIX    3   3 ASP A   61  GLY A   65  5                                   5    
-HELIX    4   4 TYR A   67  ARG A 1078  1                                  13    
-HELIX    5   5 ASN A   98  THR A  100  5                                   3    
-HELIX    6   6 ASN A  117  GLY A  128  1                                  13    
-HELIX    7   7 LEU A  138  PHE A  143  1                                   6    
-HELIX    8   8 ASN A  198  ILE A  202  5                                   5    
-SHEET    1   A 3 ILE A   5  ASP A   6  0                                        
-SHEET    2   A 3 HIS A 159  GLN A1168 -1  O  TYR A 166   N  ILE A   5           
-SHEET    3   A 3 VAL A 130  ILE A 134 -1  N  VAL A 132   O  VAL A 161           
-SHEET    1   B 5 ILE A   5  ASP A   6  0                                        
-SHEET    2   B 5 HIS A 159  GLN A1168 -1  O  TYR A 166   N  ILE A   5           
-SHEET    3   B 5 ASN A4168  LYS A 174 -1  O  LYS A 174   N  LEU A 162           
-SHEET    4   B 5 TYR A 186  ALA A 190 -1  O  ILE A 187   N  ILE A 173           
-SHEET    5   B 5 VAL A 148  TYR A 149  1  N  TYR A 149   O  LEU A 188           
-SHEET    1   C 2 ILE A  80  ASP A  81  0                                        
-SHEET    2   C 2 LYS A 102  ALA A 105 -1  O  ALA A 103   N  ILE A  80           
-SHEET    1   D 2 TYR A 110  GLU A 112  0                                        
-SHEET    2   D 2 SER A 207  PRO A 209 -1  O  PHE A 208   N  ARG A 111           
-SSBOND   1 CYS A   22    CYS A   63                          1555   1555  2.03  
-SSBOND   2 CYS A   56    CYS A   95                          1555   1555  2.03  
-SSBOND   3 CYS A  153    CYS A  200                          1555   1555  2.04  
-LINK         SG  CYS A  25                 C44 NFT A 283     1555   1555  1.73  
-SITE     1 AC1 23 SER A   4  ILE A   5  ASP A   6  GLN A  19                    
-SITE     2 AC1 23 GLY A  23  SER A  24  CYS A  25  TRP A  26                    
-SITE     3 AC1 23 GLU A  59  ASN A  60  ASP A  61  GLY A  64                    
-SITE     4 AC1 23 GLY A  65  GLY A  66  TYR A  67  LEU A 157                    
-SITE     5 AC1 23 ASN A 158  TYR A 166  GLY A 167  ILE A 168                    
-SITE     6 AC1 23 HIS A 170  ILE A 172  HOH A4252                               
-CRYST1   38.420   51.000  104.200  90.00  90.00  90.00 P 21 21 21    4          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.026028  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.019608  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.009597        0.00000                         
-ATOM      1  N   ALA A   1      27.346  39.306  13.120  1.00 28.98           N  
-ATOM      2  CA  ALA A   1      26.736  37.958  12.921  1.00 28.56           C  
-ATOM      3  C   ALA A   1      27.753  36.939  12.322  1.00 28.03           C  
-ATOM      4  O   ALA A   1      28.466  37.273  11.366  1.00 28.12           O  
-ATOM      5  CB  ALA A   1      25.513  38.099  12.007  1.00 28.68           C  
-ATOM      6  N   PRO A   2      27.899  35.646  12.829  1.00 26.96           N  
-ATOM      7  CA  PRO A   2      28.842  34.645  12.302  1.00 26.00           C  
-ATOM      8  C   PRO A   2      28.615  34.236  10.849  1.00 24.53           C  
-ATOM      9  O   PRO A   2      27.499  34.353  10.337  1.00 24.44           O  
-ATOM     10  CB  PRO A   2      28.626  33.448  13.229  1.00 26.05           C  
-ATOM     11  CG  PRO A   2      28.166  34.069  14.500  1.00 27.05           C  
-ATOM     12  CD  PRO A   2      27.201  35.111  14.012  1.00 26.89           C  
-ATOM     13  N   ASP A   3      29.680  33.782  10.187  1.00 22.77           N  
-ATOM     14  CA  ASP A   3      29.617  33.327   8.796  1.00 21.36           C  
-ATOM     15  C   ASP A   3      28.960  31.958   8.701  1.00 19.37           C  
-ATOM     16  O   ASP A   3      28.409  31.588   7.662  1.00 18.57           O  
-ATOM     17  CB  ASP A   3      31.019  33.266   8.171  1.00 23.03           C  
-ATOM     18  CG  ASP A   3      31.624  34.660   7.931  1.00 25.11           C  
-ATOM     19  OD1 ASP A   3      30.919  35.588   7.502  1.00 25.60           O  
-ATOM     20  OD2 ASP A   3      32.827  34.803   8.175  1.00 26.38           O  
-ATOM     21  N   SER A   4      28.988  31.226   9.814  1.00 17.32           N  
-ATOM     22  CA  SER A   4      28.407  29.887   9.894  1.00 15.74           C  
-ATOM     23  C   SER A   4      28.136  29.469  11.327  1.00 14.50           C  
-ATOM     24  O   SER A   4      28.890  29.819  12.236  1.00 13.58           O  
-ATOM     25  CB  SER A   4      29.324  28.867   9.200  1.00 15.56           C  
-ATOM     26  OG  SER A   4      30.603  28.882   9.786  1.00 15.60           O  
-ATOM     27  N   ILE A   5      27.049  28.719  11.523  1.00 13.09           N  
-ATOM     28  CA  ILE A   5      26.653  28.212  12.838  1.00 12.84           C  
-ATOM     29  C   ILE A   5      25.792  26.942  12.707  1.00 12.47           C  
-ATOM     30  O   ILE A   5      25.006  26.800  11.771  1.00 12.14           O  
-ATOM     31  CB  ILE A   5      25.905  29.316  13.691  1.00 13.49           C  
-ATOM     32  CG1 ILE A   5      25.677  28.896  15.139  1.00 14.23           C  
-ATOM     33  CG2 ILE A   5      24.562  29.687  13.071  1.00 13.27           C  
-ATOM     34  CD1 ILE A   5      26.917  28.954  15.996  1.00 16.21           C  
-ATOM     35  N   ASP A   6      25.979  26.016  13.641  1.00 12.08           N  
-ATOM     36  CA  ASP A   6      25.208  24.772  13.675  1.00 11.95           C  
-ATOM     37  C   ASP A   6      24.740  24.584  15.122  1.00 11.57           C  
-ATOM     38  O   ASP A   6      25.522  24.176  15.986  1.00 11.43           O  
-ATOM     39  CB  ASP A   6      26.067  23.568  13.181  1.00 11.33           C  
-ATOM     40  CG  ASP A   6      25.276  22.241  13.116  1.00 11.67           C  
-ATOM     41  OD1 ASP A   6      25.879  21.272  12.666  1.00 11.10           O  
-ATOM     42  OD2 ASP A   6      24.100  22.120  13.500  1.00 10.84           O  
-ATOM     43  N   TYR A   7      23.456  24.867  15.365  1.00 11.97           N  
-ATOM     44  CA  TYR A   7      22.838  24.746  16.692  1.00 12.41           C  
-ATOM     45  C   TYR A   7      22.713  23.335  17.257  1.00 12.58           C  
-ATOM     46  O   TYR A   7      22.469  23.163  18.457  1.00 11.76           O  
-ATOM     47  CB  TYR A   7      21.489  25.472  16.725  1.00 12.75           C  
-ATOM     48  CG  TYR A   7      21.636  26.963  16.925  1.00 13.57           C  
-ATOM     49  CD1 TYR A   7      21.684  27.840  15.822  1.00 14.13           C  
-ATOM     50  CD2 TYR A   7      21.780  27.508  18.220  1.00 13.94           C  
-ATOM     51  CE1 TYR A   7      21.884  29.244  16.006  1.00 14.52           C  
-ATOM     52  CE2 TYR A   7      21.973  28.911  18.418  1.00 14.66           C  
-ATOM     53  CZ  TYR A   7      22.025  29.762  17.304  1.00 15.01           C  
-ATOM     54  OH  TYR A   7      22.201  31.112  17.489  1.00 15.43           O  
-ATOM     55  N   ARG A   8      22.944  22.333  16.404  1.00 13.56           N  
-ATOM     56  CA  ARG A   8      22.915  20.923  16.801  1.00 14.46           C  
-ATOM     57  C   ARG A   8      24.143  20.643  17.662  1.00 15.03           C  
-ATOM     58  O   ARG A   8      24.097  19.823  18.579  1.00 15.12           O  
-ATOM     59  CB  ARG A   8      22.938  20.020  15.586  1.00 14.63           C  
-ATOM     60  CG  ARG A   8      21.777  20.177  14.615  1.00 15.28           C  
-ATOM     61  CD  ARG A   8      21.961  19.285  13.398  1.00 14.85           C  
-ATOM     62  NE  ARG A   8      23.094  19.685  12.568  1.00 14.00           N  
-ATOM     63  CZ  ARG A   8      23.403  19.132  11.400  1.00 13.81           C  
-ATOM     64  NH1 ARG A   8      22.680  18.145  10.885  1.00 14.11           N  
-ATOM     65  NH2 ARG A   8      24.466  19.597  10.754  1.00 13.61           N  
-ATOM     66  N   LYS A   9      25.219  21.387  17.395  1.00 15.98           N  
-ATOM     67  CA  LYS A   9      26.481  21.269  18.131  1.00 17.44           C  
-ATOM     68  C   LYS A   9      26.441  21.969  19.480  1.00 17.52           C  
-ATOM     69  O   LYS A   9      27.277  21.699  20.345  1.00 17.96           O  
-ATOM     70  CB  LYS A   9      27.647  21.792  17.297  1.00 18.10           C  
-ATOM     71  CG  LYS A   9      28.012  20.776  16.215  1.00 19.66           C  
-ATOM     72  CD  LYS A   9      29.239  21.221  15.428  1.00 20.79           C  
-ATOM     73  CE  LYS A   9      30.032  20.027  14.911  1.00 22.10           C  
-ATOM     74  NZ  LYS A   9      29.288  19.184  13.924  1.00 23.14           N  
-ATOM     75  N   LYS A  10      25.457  22.854  19.661  1.00 18.08           N  
-ATOM     76  CA  LYS A  10      25.257  23.589  20.914  1.00 18.39           C  
-ATOM     77  C   LYS A  10      24.228  22.907  21.831  1.00 17.96           C  
-ATOM     78  O   LYS A  10      24.009  23.350  22.961  1.00 18.07           O  
-ATOM     79  CB  LYS A  10      24.823  25.026  20.638  1.00 19.77           C  
-ATOM     80  CG  LYS A  10      26.041  25.771  20.123  1.00 21.55           C  
-ATOM     81  CD  LYS A  10      26.120  27.179  20.699  1.00 23.82           C  
-ATOM     82  CE  LYS A  10      25.005  28.055  20.181  1.00 24.42           C  
-ATOM     83  NZ  LYS A  10      25.101  28.057  18.695  1.00 25.72           N  
-ATOM     84  N   GLY A  11      23.601  21.839  21.330  1.00 17.01           N  
-ATOM     85  CA  GLY A  11      22.604  21.102  22.094  1.00 15.96           C  
-ATOM     86  C   GLY A  11      21.232  21.756  22.134  1.00 15.36           C  
-ATOM     87  O   GLY A  11      20.497  21.598  23.108  1.00 15.19           O  
-ATOM     88  N   TYR A  12      20.891  22.495  21.077  1.00 14.68           N  
-ATOM     89  CA  TYR A  12      19.606  23.194  20.977  1.00 14.65           C  
-ATOM     90  C   TYR A  12      18.560  22.434  20.202  1.00 13.78           C  
-ATOM     91  O   TYR A  12      17.407  22.866  20.132  1.00 13.91           O  
-ATOM     92  CB  TYR A  12      19.792  24.534  20.288  1.00 15.87           C  
-ATOM     93  CG  TYR A  12      20.258  25.689  21.152  1.00 17.24           C  
-ATOM     94  CD1 TYR A  12      21.429  25.599  21.942  1.00 17.83           C  
-ATOM     95  CD2 TYR A  12      19.569  26.915  21.122  1.00 18.04           C  
-ATOM     96  CE1 TYR A  12      21.907  26.729  22.689  1.00 18.52           C  
-ATOM     97  CE2 TYR A  12      20.036  28.050  21.858  1.00 18.78           C  
-ATOM     98  CZ  TYR A  12      21.199  27.942  22.630  1.00 19.08           C  
-ATOM     99  OH  TYR A  12      21.643  29.047  23.322  1.00 20.51           O  
-ATOM    100  N   VAL A  13      18.962  21.319  19.591  1.00 12.76           N  
-ATOM    101  CA  VAL A  13      18.079  20.509  18.750  1.00 11.60           C  
-ATOM    102  C   VAL A  13      17.880  19.077  19.279  1.00 11.68           C  
-ATOM    103  O   VAL A  13      18.842  18.360  19.564  1.00 11.34           O  
-ATOM    104  CB  VAL A  13      18.619  20.453  17.281  1.00 11.40           C  
-ATOM    105  CG1 VAL A  13      17.569  19.902  16.324  1.00 10.08           C  
-ATOM    106  CG2 VAL A  13      18.982  21.852  16.775  1.00 10.69           C  
-ATOM    107  N   THR A  14      16.613  18.663  19.329  1.00 10.82           N  
-ATOM    108  CA  THR A  14      16.194  17.338  19.791  1.00 10.93           C  
-ATOM    109  C   THR A  14      16.304  16.282  18.639  1.00 11.50           C  
-ATOM    110  O   THR A  14      16.456  16.685  17.477  1.00 10.60           O  
-ATOM    111  CB  THR A  14      14.704  17.369  20.231  1.00 10.68           C  
-ATOM    112  OG1 THR A  14      13.882  17.733  19.115  1.00  9.19           O  
-ATOM    113  CG2 THR A  14      14.530  18.213  21.480  1.00  9.66           C  
-ATOM    114  N   PRO A  15      16.288  14.876  18.793  1.00 12.54           N  
-ATOM    115  CA  PRO A  15      16.386  13.961  17.644  1.00 12.57           C  
-ATOM    116  C   PRO A  15      15.305  14.158  16.574  1.00 12.97           C  
-ATOM    117  O   PRO A  15      14.239  14.737  16.848  1.00 12.75           O  
-ATOM    118  CB  PRO A  15      16.241  12.599  18.292  1.00 12.72           C  
-ATOM    119  CG  PRO A  15      16.942  12.776  19.583  1.00 13.10           C  
-ATOM    120  CD  PRO A  15      16.399  14.106  20.054  1.00 13.13           C  
-ATOM    121  N   VAL A  16      15.595  13.695  15.360  1.00 12.60           N  
-ATOM    122  CA  VAL A  16      14.662  13.790  14.240  1.00 12.84           C  
-ATOM    123  C   VAL A  16      13.457  12.876  14.514  1.00 12.84           C  
-ATOM    124  O   VAL A  16      13.616  11.724  14.936  1.00 12.61           O  
-ATOM    125  CB  VAL A  16      15.338  13.390  12.903  1.00 12.91           C  
-ATOM    126  CG1 VAL A  16      14.380  13.586  11.720  1.00 13.40           C  
-ATOM    127  CG2 VAL A  16      16.480  14.334  12.591  1.00 13.01           C  
-ATOM    128  N   LYS A  17      12.264  13.426  14.312  1.00 12.00           N  
-ATOM    129  CA  LYS A  17      11.019  12.700  14.518  1.00 12.68           C  
-ATOM    130  C   LYS A  17      10.371  12.334  13.164  1.00 12.58           C  
-ATOM    131  O   LYS A  17      10.805  12.810  12.117  1.00 11.91           O  
-ATOM    132  CB  LYS A  17      10.065  13.553  15.343  1.00 12.95           C  
-ATOM    133  CG  LYS A  17      10.555  14.255  16.622  1.00 12.89           C  
-ATOM    134  CD  LYS A  17      11.162  13.276  17.621  1.00 12.79           C  
-ATOM    135  CE  LYS A  17      11.382  13.934  18.982  1.00 14.16           C  
-ATOM    136  NZ  LYS A  17      12.180  15.193  18.903  1.00 13.12           N  
-ATOM    137  N   ASN A  18       9.375  11.452  13.201  1.00 13.08           N  
-ATOM    138  CA  ASN A  18       8.655  11.028  11.999  1.00 13.42           C  
-ATOM    139  C   ASN A  18       7.195  11.358  12.185  1.00 12.91           C  
-ATOM    140  O   ASN A  18       6.542  10.819  13.081  1.00 13.09           O  
-ATOM    141  CB  ASN A  18       8.820   9.501  11.762  1.00 13.98           C  
-ATOM    142  CG  ASN A  18       8.451   9.074  10.324  1.00 14.78           C  
-ATOM    143  OD1 ASN A  18       9.149   8.182   9.845  1.00 15.89           O  
-ATOM    144  ND2 ASN A  18       7.458   9.645   9.644  1.00 14.29           N  
-ATOM    145  N   GLN A  19       6.671  12.216  11.310  1.00 12.81           N  
-ATOM    146  CA  GLN A  19       5.270  12.643  11.353  1.00 12.22           C  
-ATOM    147  C   GLN A  19       4.284  11.575  10.890  1.00 12.21           C  
-ATOM    148  O   GLN A  19       3.096  11.648  11.212  1.00 10.99           O  
-ATOM    149  CB  GLN A  19       5.067  13.931  10.539  1.00 11.79           C  
-ATOM    150  CG  GLN A  19       5.322  13.853   9.040  1.00 12.62           C  
-ATOM    151  CD  GLN A  19       5.091  15.211   8.411  1.00 12.80           C  
-ATOM    152  OE1 GLN A  19       5.935  16.090   8.573  1.00 12.59           O  
-ATOM    153  NE2 GLN A  19       3.976  15.409   7.712  1.00 13.01           N  
-ATOM    154  N   GLY A  20       4.784  10.588  10.141  1.00 12.60           N  
-ATOM    155  CA  GLY A  20       3.953   9.509   9.633  1.00 13.66           C  
-ATOM    156  C   GLY A  20       2.967   9.981   8.580  1.00 14.62           C  
-ATOM    157  O   GLY A  20       3.215  10.975   7.891  1.00 15.00           O  
-ATOM    158  N   GLN A  21       1.823   9.300   8.497  1.00 15.26           N  
-ATOM    159  CA  GLN A  21       0.762   9.624   7.538  1.00 15.67           C  
-ATOM    160  C   GLN A  21      -0.236  10.637   8.113  1.00 14.96           C  
-ATOM    161  O   GLN A  21      -1.434  10.361   8.247  1.00 14.97           O  
-ATOM    162  CB  GLN A  21       0.052   8.331   7.064  1.00 16.66           C  
-ATOM    163  CG  GLN A  21       0.963   7.467   6.194  1.00 18.46           C  
-ATOM    164  CD  GLN A  21       1.471   8.099   4.875  1.00 19.97           C  
-ATOM    165  OE1 GLN A  21       2.656   7.960   4.568  1.00 21.42           O  
-ATOM    166  NE2 GLN A  21       0.613   8.780   4.121  1.00 20.29           N  
-ATOM    167  N   CYS A  22       0.288  11.815   8.444  1.00 14.03           N  
-ATOM    168  CA  CYS A  22      -0.471  12.928   9.012  1.00 12.75           C  
-ATOM    169  C   CYS A  22       0.251  14.207   8.618  1.00 12.23           C  
-ATOM    170  O   CYS A  22       1.475  14.313   8.776  1.00 12.51           O  
-ATOM    171  CB  CYS A  22      -0.546  12.797  10.569  1.00 12.11           C  
-ATOM    172  SG  CYS A  22      -1.092  14.214  11.585  1.00 11.20           S  
-ATOM    173  N   GLY A  23      -0.507  15.175   8.098  1.00 11.40           N  
-ATOM    174  CA  GLY A  23       0.053  16.455   7.677  1.00 10.04           C  
-ATOM    175  C   GLY A  23       0.249  17.406   8.848  1.00  9.83           C  
-ATOM    176  O   GLY A  23      -0.296  18.510   8.877  1.00  9.59           O  
-ATOM    177  N   SER A  24       1.058  16.963   9.806  1.00  8.75           N  
-ATOM    178  CA  SER A  24       1.358  17.705  11.018  1.00  8.43           C  
-ATOM    179  C   SER A  24       2.765  18.344  11.010  1.00  8.27           C  
-ATOM    180  O   SER A  24       3.324  18.611  12.080  1.00  7.51           O  
-ATOM    181  CB  SER A  24       1.201  16.784  12.254  1.00  8.95           C  
-ATOM    182  OG  SER A  24       2.086  15.666  12.091  1.00  9.91           O  
-ATOM    183  N   CYS A  25       3.306  18.620   9.817  1.00  7.60           N  
-ATOM    184  CA  CYS A  25       4.640  19.230   9.668  1.00  7.85           C  
-ATOM    185  C   CYS A  25       4.757  20.573  10.406  1.00  7.94           C  
-ATOM    186  O   CYS A  25       5.794  20.885  10.982  1.00  7.76           O  
-ATOM    187  CB  CYS A  25       4.975  19.421   8.196  1.00  9.06           C  
-ATOM    188  SG  CYS A  25       3.847  20.506   7.225  1.00  9.43           S  
-ATOM    189  N   TRP A  26       3.657  21.330  10.413  1.00  7.77           N  
-ATOM    190  CA  TRP A  26       3.568  22.628  11.092  1.00  7.59           C  
-ATOM    191  C   TRP A  26       3.761  22.486  12.625  1.00  7.48           C  
-ATOM    192  O   TRP A  26       4.313  23.375  13.278  1.00  8.42           O  
-ATOM    193  CB  TRP A  26       2.207  23.291  10.786  1.00  7.09           C  
-ATOM    194  CG  TRP A  26       1.019  22.455  11.171  1.00  7.14           C  
-ATOM    195  CD1 TRP A  26       0.419  21.491  10.419  1.00  7.12           C  
-ATOM    196  CD2 TRP A  26       0.299  22.512  12.407  1.00  7.43           C  
-ATOM    197  NE1 TRP A  26      -0.637  20.935  11.104  1.00  7.55           N  
-ATOM    198  CE2 TRP A  26      -0.736  21.539  12.331  1.00  8.48           C  
-ATOM    199  CE3 TRP A  26       0.429  23.286  13.583  1.00  7.04           C  
-ATOM    200  CZ2 TRP A  26      -1.648  21.316  13.388  1.00  7.76           C  
-ATOM    201  CZ3 TRP A  26      -0.481  23.064  14.651  1.00  7.83           C  
-ATOM    202  CH2 TRP A  26      -1.507  22.082  14.534  1.00  8.32           C  
-ATOM    203  N   ALA A  27       3.248  21.380  13.176  1.00  7.12           N  
-ATOM    204  CA  ALA A  27       3.338  21.073  14.604  1.00  7.16           C  
-ATOM    205  C   ALA A  27       4.747  20.697  15.002  1.00  6.83           C  
-ATOM    206  O   ALA A  27       5.196  21.069  16.079  1.00  7.28           O  
-ATOM    207  CB  ALA A  27       2.351  19.962  14.984  1.00  7.18           C  
-ATOM    208  N   PHE A  28       5.456  19.986  14.121  1.00  6.90           N  
-ATOM    209  CA  PHE A  28       6.846  19.582  14.373  1.00  7.49           C  
-ATOM    210  C   PHE A  28       7.803  20.750  14.213  1.00  7.03           C  
-ATOM    211  O   PHE A  28       8.791  20.859  14.944  1.00  6.76           O  
-ATOM    212  CB  PHE A  28       7.258  18.451  13.474  1.00  7.67           C  
-ATOM    213  CG  PHE A  28       6.732  17.125  13.910  1.00  8.15           C  
-ATOM    214  CD1 PHE A  28       5.448  16.706  13.521  1.00  9.37           C  
-ATOM    215  CD2 PHE A  28       7.509  16.283  14.723  1.00  8.77           C  
-ATOM    216  CE1 PHE A  28       4.932  15.451  13.939  1.00  9.49           C  
-ATOM    217  CE2 PHE A  28       7.013  15.012  15.158  1.00  9.20           C  
-ATOM    218  CZ  PHE A  28       5.722  14.593  14.766  1.00  9.01           C  
-ATOM    219  N   SER A  29       7.486  21.639  13.273  1.00  7.20           N  
-ATOM    220  CA  SER A  29       8.280  22.841  13.008  1.00  8.29           C  
-ATOM    221  C   SER A  29       8.142  23.800  14.213  1.00  8.18           C  
-ATOM    222  O   SER A  29       9.122  24.393  14.670  1.00  8.38           O  
-ATOM    223  CB  SER A  29       7.776  23.526  11.745  1.00  8.34           C  
-ATOM    224  OG  SER A  29       8.501  24.713  11.450  1.00  9.18           O  
-ATOM    225  N   SER A  30       6.919  23.872  14.749  1.00  8.23           N  
-ATOM    226  CA  SER A  30       6.572  24.710  15.892  1.00  8.52           C  
-ATOM    227  C   SER A  30       7.243  24.284  17.146  1.00  8.09           C  
-ATOM    228  O   SER A  30       7.885  25.106  17.800  1.00  7.75           O  
-ATOM    229  CB  SER A  30       5.050  24.725  16.119  1.00  9.01           C  
-ATOM    230  OG  SER A  30       4.433  25.349  15.039  1.00 11.79           O  
-ATOM    231  N   VAL A  31       7.149  22.991  17.482  1.00  8.25           N  
-ATOM    232  CA  VAL A  31       7.789  22.488  18.705  1.00  8.30           C  
-ATOM    233  C   VAL A  31       9.302  22.565  18.631  1.00  8.47           C  
-ATOM    234  O   VAL A  31       9.954  22.797  19.643  1.00  9.18           O  
-ATOM    235  CB  VAL A  31       7.297  21.068  19.150  1.00  9.00           C  
-ATOM    236  CG1 VAL A  31       5.812  21.085  19.399  1.00  8.45           C  
-ATOM    237  CG2 VAL A  31       7.786  19.972  18.217  1.00  9.42           C  
-ATOM    238  N   GLY A  32       9.847  22.431  17.419  1.00  8.09           N  
-ATOM    239  CA  GLY A  32      11.286  22.497  17.216  1.00  8.24           C  
-ATOM    240  C   GLY A  32      11.837  23.872  17.565  1.00  8.18           C  
-ATOM    241  O   GLY A  32      12.890  23.990  18.201  1.00  7.56           O  
-ATOM    242  N   ALA A  33      11.078  24.909  17.199  1.00  8.47           N  
-ATOM    243  CA  ALA A  33      11.440  26.299  17.471  1.00  8.27           C  
-ATOM    244  C   ALA A  33      11.291  26.599  18.984  1.00  8.73           C  
-ATOM    245  O   ALA A  33      12.150  27.260  19.576  1.00  8.41           O  
-ATOM    246  CB  ALA A  33      10.577  27.229  16.643  1.00  8.24           C  
-ATOM    247  N   LEU A  34      10.240  26.043  19.599  1.00  8.78           N  
-ATOM    248  CA  LEU A  34       9.976  26.196  21.036  1.00  9.27           C  
-ATOM    249  C   LEU A  34      11.036  25.443  21.889  1.00  9.55           C  
-ATOM    250  O   LEU A  34      11.440  25.928  22.943  1.00  8.91           O  
-ATOM    251  CB  LEU A  34       8.558  25.691  21.389  1.00  9.63           C  
-ATOM    252  CG  LEU A  34       7.322  26.551  21.052  1.00 10.22           C  
-ATOM    253  CD1 LEU A  34       6.054  25.717  21.106  1.00 10.83           C  
-ATOM    254  CD2 LEU A  34       7.228  27.732  22.020  1.00 10.68           C  
-ATOM    255  N   GLU A  35      11.492  24.285  21.391  1.00 10.26           N  
-ATOM    256  CA  GLU A  35      12.513  23.459  22.056  1.00 10.25           C  
-ATOM    257  C   GLU A  35      13.855  24.196  22.116  1.00 10.45           C  
-ATOM    258  O   GLU A  35      14.563  24.131  23.123  1.00  9.99           O  
-ATOM    259  CB  GLU A  35      12.699  22.122  21.314  1.00 10.04           C  
-ATOM    260  CG  GLU A  35      11.586  21.105  21.557  1.00 10.06           C  
-ATOM    261  CD  GLU A  35      11.529  19.935  20.580  1.00 10.50           C  
-ATOM    262  OE1 GLU A  35      12.220  19.932  19.563  1.00 10.53           O  
-ATOM    263  OE2 GLU A  35      10.795  18.984  20.821  1.00 11.28           O  
-ATOM    264  N   GLY A  36      14.164  24.929  21.043  1.00 10.50           N  
-ATOM    265  CA  GLY A  36      15.390  25.708  20.951  1.00 11.24           C  
-ATOM    266  C   GLY A  36      15.351  26.888  21.909  1.00 11.65           C  
-ATOM    267  O   GLY A  36      16.354  27.209  22.544  1.00 11.47           O  
-ATOM    268  N   GLN A  37      14.175  27.504  22.042  1.00 11.93           N  
-ATOM    269  CA  GLN A  37      13.982  28.638  22.946  1.00 12.90           C  
-ATOM    270  C   GLN A  37      13.954  28.217  24.403  1.00 13.76           C  
-ATOM    271  O   GLN A  37      14.448  28.947  25.267  1.00 14.05           O  
-ATOM    272  CB  GLN A  37      12.731  29.434  22.579  1.00 12.88           C  
-ATOM    273  CG  GLN A  37      12.900  30.146  21.225  1.00 13.59           C  
-ATOM    274  CD  GLN A  37      14.157  31.029  21.101  1.00 13.94           C  
-ATOM    275  OE1 GLN A  37      14.341  32.000  21.838  1.00 14.44           O  
-ATOM    276  NE2 GLN A  37      15.036  30.654  20.180  1.00 13.13           N  
-ATOM    277  N   LEU A  38      13.451  27.006  24.667  1.00 14.04           N  
-ATOM    278  CA  LEU A  38      13.392  26.456  26.025  1.00 15.48           C  
-ATOM    279  C   LEU A  38      14.824  26.168  26.522  1.00 16.52           C  
-ATOM    280  O   LEU A  38      15.163  26.481  27.669  1.00 16.32           O  
-ATOM    281  CB  LEU A  38      12.538  25.166  26.071  1.00 14.72           C  
-ATOM    282  CG  LEU A  38      12.346  24.411  27.441  1.00 15.65           C  
-ATOM    283  CD1 LEU A  38      11.632  25.301  28.462  1.00 15.95           C  
-ATOM    284  CD2 LEU A  38      11.598  23.112  27.222  1.00 14.79           C  
-ATOM    285  N   LYS A  39      15.664  25.647  25.623  1.00 17.33           N  
-ATOM    286  CA  LYS A  39      17.064  25.331  25.919  1.00 18.97           C  
-ATOM    287  C   LYS A  39      17.908  26.605  26.182  1.00 20.07           C  
-ATOM    288  O   LYS A  39      18.795  26.595  27.035  1.00 20.23           O  
-ATOM    289  CB  LYS A  39      17.693  24.476  24.767  1.00 18.86           C  
-ATOM    290  CG  LYS A  39      19.199  24.211  24.826  1.00 18.48           C  
-ATOM    291  CD  LYS A  39      19.605  23.419  26.062  1.00 19.40           C  
-ATOM    292  CE  LYS A  39      21.124  23.334  26.182  1.00 19.50           C  
-ATOM    293  NZ  LYS A  39      21.530  22.504  27.348  1.00 20.32           N  
-ATOM    294  N   LYS A  40      17.600  27.686  25.463  1.00 21.34           N  
-ATOM    295  CA  LYS A  40      18.299  28.965  25.625  1.00 22.77           C  
-ATOM    296  C   LYS A  40      17.929  29.637  26.963  1.00 23.01           C  
-ATOM    297  O   LYS A  40      18.798  30.161  27.660  1.00 23.28           O  
-ATOM    298  CB  LYS A  40      17.973  29.921  24.452  1.00 23.93           C  
-ATOM    299  CG  LYS A  40      18.555  31.328  24.650  1.00 26.02           C  
-ATOM    300  CD  LYS A  40      18.265  32.250  23.480  1.00 27.77           C  
-ATOM    301  CE  LYS A  40      19.058  31.845  22.256  1.00 29.16           C  
-ATOM    302  NZ  LYS A  40      20.527  31.953  22.481  1.00 30.64           N  
-ATOM    303  N   ALA A  41      16.648  29.570  27.321  1.00 23.30           N  
-ATOM    304  CA  ALA A  41      16.139  30.173  28.550  1.00 23.42           C  
-ATOM    305  C   ALA A  41      16.390  29.392  29.859  1.00 23.41           C  
-ATOM    306  O   ALA A  41      16.725  30.003  30.876  1.00 24.01           O  
-ATOM    307  CB  ALA A  41      14.647  30.487  28.402  1.00 23.66           C  
-ATOM    308  N   THR A  42      16.247  28.063  29.823  1.00 22.44           N  
-ATOM    309  CA  THR A  42      16.409  27.231  31.026  1.00 22.04           C  
-ATOM    310  C   THR A  42      17.643  26.307  31.085  1.00 21.88           C  
-ATOM    311  O   THR A  42      17.966  25.768  32.154  1.00 21.97           O  
-ATOM    312  CB  THR A  42      15.160  26.325  31.279  1.00 21.85           C  
-ATOM    313  OG1 THR A  42      15.029  25.365  30.220  1.00 22.04           O  
-ATOM    314  CG2 THR A  42      13.881  27.157  31.356  1.00 21.49           C  
-ATOM    315  N   GLY A  43      18.287  26.092  29.938  1.00 21.20           N  
-ATOM    316  CA  GLY A  43      19.455  25.224  29.873  1.00 20.45           C  
-ATOM    317  C   GLY A  43      19.110  23.752  29.710  1.00 20.25           C  
-ATOM    318  O   GLY A  43      20.006  22.909  29.625  1.00 20.76           O  
-ATOM    319  N   ALA A  44      17.815  23.444  29.647  1.00 19.68           N  
-ATOM    320  CA  ALA A  44      17.349  22.069  29.507  1.00 19.11           C  
-ATOM    321  C   ALA A  44      16.709  21.806  28.155  1.00 18.56           C  
-ATOM    322  O   ALA A  44      15.876  22.586  27.683  1.00 19.05           O  
-ATOM    323  CB  ALA A  44      16.380  21.722  30.638  1.00 19.02           C  
-ATOM    324  N   LEU A  45      17.132  20.716  27.520  1.00 17.89           N  
-ATOM    325  CA  LEU A  45      16.616  20.297  26.220  1.00 17.49           C  
-ATOM    326  C   LEU A  45      15.602  19.160  26.423  1.00 17.53           C  
-ATOM    327  O   LEU A  45      15.962  18.078  26.895  1.00 17.15           O  
-ATOM    328  CB  LEU A  45      17.771  19.814  25.310  1.00 16.77           C  
-ATOM    329  CG  LEU A  45      17.482  19.328  23.879  1.00 16.32           C  
-ATOM    330  CD1 LEU A  45      17.117  20.506  23.002  1.00 16.52           C  
-ATOM    331  CD2 LEU A  45      18.681  18.601  23.306  1.00 16.40           C  
-ATOM    332  N   LEU A  46      14.338  19.430  26.102  1.00 17.40           N  
-ATOM    333  CA  LEU A  46      13.262  18.442  26.231  1.00 17.65           C  
-ATOM    334  C   LEU A  46      12.438  18.329  24.965  1.00 16.51           C  
-ATOM    335  O   LEU A  46      12.317  19.291  24.203  1.00 16.48           O  
-ATOM    336  CB  LEU A  46      12.303  18.801  27.382  1.00 19.25           C  
-ATOM    337  CG  LEU A  46      12.438  18.854  28.870  1.00 20.94           C  
-ATOM    338  CD1 LEU A  46      13.078  20.170  29.299  1.00 22.36           C  
-ATOM    339  CD2 LEU A  46      11.050  18.843  29.490  1.00 22.13           C  
-ATOM    340  N   ASN A  47      11.860  17.146  24.751  1.00 15.09           N  
-ATOM    341  CA  ASN A  47      10.995  16.887  23.601  1.00 13.97           C  
-ATOM    342  C   ASN A  47       9.626  17.438  23.942  1.00 13.06           C  
-ATOM    343  O   ASN A  47       9.062  17.084  24.978  1.00 12.80           O  
-ATOM    344  CB  ASN A  47      10.856  15.358  23.326  1.00 14.80           C  
-ATOM    345  CG  ASN A  47      12.110  14.745  22.737  1.00 15.78           C  
-ATOM    346  OD1 ASN A  47      12.665  15.189  21.732  1.00 15.00           O  
-ATOM    347  ND2 ASN A  47      12.547  13.671  23.379  1.00 16.53           N  
-ATOM    348  N   LEU A  48       9.137  18.371  23.127  1.00 12.18           N  
-ATOM    349  CA  LEU A  48       7.815  18.953  23.329  1.00 11.60           C  
-ATOM    350  C   LEU A  48       6.812  18.158  22.506  1.00 10.78           C  
-ATOM    351  O   LEU A  48       7.203  17.441  21.580  1.00 10.74           O  
-ATOM    352  CB  LEU A  48       7.803  20.447  22.986  1.00 10.88           C  
-ATOM    353  CG  LEU A  48       8.676  21.291  24.001  1.00 11.86           C  
-ATOM    354  CD1 LEU A  48       8.606  22.764  23.673  1.00 11.78           C  
-ATOM    355  CD2 LEU A  48       8.153  21.186  25.437  1.00 11.92           C  
-ATOM    356  N   ALA A  49       5.530  18.266  22.857  1.00 10.01           N  
-ATOM    357  CA  ALA A  49       4.458  17.502  22.213  1.00  8.35           C  
-ATOM    358  C   ALA A  49       3.754  18.044  20.974  1.00  7.97           C  
-ATOM    359  O   ALA A  49       2.909  18.936  21.091  1.00  7.27           O  
-ATOM    360  CB  ALA A  49       3.412  17.117  23.252  1.00  8.29           C  
-ATOM    361  N   PRO A  50       4.035  17.538  19.711  1.00  6.81           N  
-ATOM    362  CA  PRO A  50       3.361  18.027  18.497  1.00  6.69           C  
-ATOM    363  C   PRO A  50       1.869  17.610  18.460  1.00  7.24           C  
-ATOM    364  O   PRO A  50       1.047  18.314  17.875  1.00  6.92           O  
-ATOM    365  CB  PRO A  50       4.165  17.376  17.365  1.00  7.10           C  
-ATOM    366  CG  PRO A  50       4.766  16.151  18.019  1.00  7.75           C  
-ATOM    367  CD  PRO A  50       5.171  16.667  19.351  1.00  6.98           C  
-ATOM    368  N   GLN A  51       1.539  16.500  19.139  1.00  6.71           N  
-ATOM    369  CA  GLN A  51       0.165  15.977  19.228  1.00  6.84           C  
-ATOM    370  C   GLN A  51      -0.746  16.949  19.980  1.00  7.13           C  
-ATOM    371  O   GLN A  51      -1.937  17.051  19.679  1.00  5.98           O  
-ATOM    372  CB  GLN A  51       0.127  14.590  19.937  1.00  7.13           C  
-ATOM    373  CG  GLN A  51      -1.207  13.848  19.714  1.00  8.25           C  
-ATOM    374  CD  GLN A  51      -1.519  13.423  18.270  1.00  8.38           C  
-ATOM    375  OE1 GLN A  51      -2.581  13.741  17.738  1.00 10.65           O  
-ATOM    376  NE2 GLN A  51      -0.599  12.715  17.642  1.00  7.61           N  
-ATOM    377  N   ASN A  52      -0.164  17.670  20.948  1.00  7.09           N  
-ATOM    378  CA  ASN A  52      -0.863  18.682  21.747  1.00  7.54           C  
-ATOM    379  C   ASN A  52      -1.344  19.793  20.815  1.00  8.17           C  
-ATOM    380  O   ASN A  52      -2.455  20.318  20.964  1.00  8.57           O  
-ATOM    381  CB  ASN A  52       0.092  19.256  22.855  1.00  7.64           C  
-ATOM    382  CG  ASN A  52      -0.634  20.194  23.867  1.00  7.94           C  
-ATOM    383  OD1 ASN A  52      -1.805  20.584  23.815  1.00  9.34           O  
-ATOM    384  ND2 ASN A  52       0.190  20.545  24.839  1.00  6.63           N  
-ATOM    385  N   LEU A  53      -0.533  20.074  19.800  1.00  7.54           N  
-ATOM    386  CA  LEU A  53      -0.853  21.087  18.811  1.00  7.39           C  
-ATOM    387  C   LEU A  53      -1.876  20.581  17.784  1.00  6.97           C  
-ATOM    388  O   LEU A  53      -2.850  21.286  17.529  1.00  6.14           O  
-ATOM    389  CB  LEU A  53       0.413  21.597  18.120  1.00  7.20           C  
-ATOM    390  CG  LEU A  53       1.499  22.284  19.017  1.00  8.43           C  
-ATOM    391  CD1 LEU A  53       2.654  22.759  18.167  1.00  8.16           C  
-ATOM    392  CD2 LEU A  53       0.968  23.538  19.714  1.00  7.48           C  
-ATOM    393  N   VAL A  54      -1.708  19.356  17.260  1.00  7.44           N  
-ATOM    394  CA  VAL A  54      -2.665  18.832  16.260  1.00  7.48           C  
-ATOM    395  C   VAL A  54      -4.113  18.725  16.796  1.00  7.47           C  
-ATOM    396  O   VAL A  54      -5.054  19.122  16.113  1.00  6.60           O  
-ATOM    397  CB  VAL A  54      -2.154  17.540  15.455  1.00  9.06           C  
-ATOM    398  CG1 VAL A  54      -0.661  17.378  15.542  1.00  8.57           C  
-ATOM    399  CG2 VAL A  54      -3.063  16.326  15.660  1.00  9.23           C  
-ATOM    400  N   ASP A  55      -4.246  18.308  18.053  1.00  7.35           N  
-ATOM    401  CA  ASP A  55      -5.541  18.127  18.708  1.00  8.54           C  
-ATOM    402  C   ASP A  55      -6.199  19.375  19.258  1.00  8.72           C  
-ATOM    403  O   ASP A  55      -7.428  19.475  19.266  1.00  9.23           O  
-ATOM    404  CB  ASP A  55      -5.404  17.134  19.894  1.00  8.31           C  
-ATOM    405  CG  ASP A  55      -5.065  15.717  19.457  1.00  9.56           C  
-ATOM    406  OD1 ASP A  55      -4.777  14.966  20.397  1.00 10.19           O  
-ATOM    407  OD2 ASP A  55      -5.095  15.341  18.278  1.00  8.99           O  
-ATOM    408  N   CYS A  56      -5.385  20.333  19.699  1.00  8.52           N  
-ATOM    409  CA  CYS A  56      -5.895  21.535  20.348  1.00  9.17           C  
-ATOM    410  C   CYS A  56      -5.991  22.874  19.605  1.00  9.51           C  
-ATOM    411  O   CYS A  56      -6.826  23.710  19.981  1.00  8.98           O  
-ATOM    412  CB  CYS A  56      -5.171  21.719  21.660  1.00  9.41           C  
-ATOM    413  SG  CYS A  56      -5.194  20.234  22.730  1.00 10.75           S  
-ATOM    414  N   VAL A  57      -5.142  23.097  18.594  1.00  9.00           N  
-ATOM    415  CA  VAL A  57      -5.175  24.359  17.835  1.00  9.28           C  
-ATOM    416  C   VAL A  57      -6.416  24.345  16.926  1.00  9.84           C  
-ATOM    417  O   VAL A  57      -6.434  23.678  15.884  1.00 10.22           O  
-ATOM    418  CB  VAL A  57      -3.876  24.602  17.014  1.00  8.76           C  
-ATOM    419  CG1 VAL A  57      -3.853  26.036  16.466  1.00  8.21           C  
-ATOM    420  CG2 VAL A  57      -2.647  24.490  17.901  1.00  7.97           C  
-ATOM    421  N   SER A  58      -7.450  25.075  17.348  1.00 10.06           N  
-ATOM    422  CA  SER A  58      -8.717  25.150  16.622  1.00 10.87           C  
-ATOM    423  C   SER A  58      -8.665  25.948  15.327  1.00 10.36           C  
-ATOM    424  O   SER A  58      -9.526  25.782  14.470  1.00 10.99           O  
-ATOM    425  CB  SER A  58      -9.827  25.668  17.538  1.00 11.16           C  
-ATOM    426  OG  SER A  58      -9.496  26.924  18.148  1.00 14.45           O  
-ATOM    427  N   GLU A  59      -7.635  26.782  15.175  1.00 10.46           N  
-ATOM    428  CA  GLU A  59      -7.444  27.588  13.964  1.00 11.16           C  
-ATOM    429  C   GLU A  59      -6.707  26.784  12.873  1.00 10.17           C  
-ATOM    430  O   GLU A  59      -6.572  27.238  11.733  1.00  9.36           O  
-ATOM    431  CB  GLU A  59      -6.678  28.893  14.275  1.00 13.10           C  
-ATOM    432  CG  GLU A  59      -7.328  29.924  15.200  1.00 16.70           C  
-ATOM    433  CD  GLU A  59      -7.411  29.597  16.694  1.00 19.34           C  
-ATOM    434  OE1 GLU A  59      -6.711  28.699  17.206  1.00 20.48           O  
-ATOM    435  OE2 GLU A  59      -8.199  30.268  17.353  1.00 22.46           O  
-ATOM    436  N   ASN A  60      -6.195  25.616  13.257  1.00  9.53           N  
-ATOM    437  CA  ASN A  60      -5.503  24.725  12.335  1.00 10.00           C  
-ATOM    438  C   ASN A  60      -6.409  23.518  12.012  1.00 10.02           C  
-ATOM    439  O   ASN A  60      -7.531  23.426  12.531  1.00 10.23           O  
-ATOM    440  CB  ASN A  60      -4.114  24.320  12.866  1.00  9.80           C  
-ATOM    441  CG  ASN A  60      -3.056  25.466  12.704  1.00  9.91           C  
-ATOM    442  OD1 ASN A  60      -3.181  26.328  11.834  1.00 10.02           O  
-ATOM    443  ND2 ASN A  60      -2.016  25.436  13.526  1.00 10.60           N  
-ATOM    444  N   ASP A  61      -5.956  22.656  11.107  1.00  9.20           N  
-ATOM    445  CA  ASP A  61      -6.750  21.509  10.669  1.00 10.36           C  
-ATOM    446  C   ASP A  61      -6.202  20.147  11.099  1.00 10.14           C  
-ATOM    447  O   ASP A  61      -6.568  19.126  10.514  1.00 10.15           O  
-ATOM    448  CB  ASP A  61      -6.900  21.561   9.090  1.00 10.79           C  
-ATOM    449  CG  ASP A  61      -8.182  20.869   8.581  1.00 12.05           C  
-ATOM    450  OD1 ASP A  61      -8.093  20.254   7.522  1.00 12.21           O  
-ATOM    451  OD2 ASP A  61      -9.236  20.949   9.223  1.00 11.89           O  
-ATOM    452  N   GLY A  62      -5.337  20.134  12.114  1.00 10.09           N  
-ATOM    453  CA  GLY A  62      -4.749  18.896  12.612  1.00 10.61           C  
-ATOM    454  C   GLY A  62      -3.884  18.189  11.586  1.00 10.64           C  
-ATOM    455  O   GLY A  62      -2.970  18.797  11.018  1.00 11.12           O  
-ATOM    456  N   CYS A  63      -4.224  16.932  11.289  1.00 10.33           N  
-ATOM    457  CA  CYS A  63      -3.510  16.125  10.292  1.00 10.29           C  
-ATOM    458  C   CYS A  63      -3.789  16.614   8.836  1.00 10.32           C  
-ATOM    459  O   CYS A  63      -3.189  16.125   7.870  1.00 10.35           O  
-ATOM    460  CB  CYS A  63      -3.869  14.618  10.437  1.00 10.18           C  
-ATOM    461  SG  CYS A  63      -3.072  13.896  11.907  1.00 10.12           S  
-ATOM    462  N   GLY A  64      -4.685  17.597   8.720  1.00  9.58           N  
-ATOM    463  CA  GLY A  64      -5.038  18.183   7.439  1.00  9.50           C  
-ATOM    464  C   GLY A  64      -4.143  19.355   7.078  1.00  9.09           C  
-ATOM    465  O   GLY A  64      -4.185  19.858   5.953  1.00  9.08           O  
-ATOM    466  N   GLY A  65      -3.348  19.799   8.049  1.00  9.19           N  
-ATOM    467  CA  GLY A  65      -2.429  20.904   7.840  1.00  9.10           C  
-ATOM    468  C   GLY A  65      -2.647  22.081   8.769  1.00  9.12           C  
-ATOM    469  O   GLY A  65      -3.547  22.063   9.610  1.00  9.37           O  
-ATOM    470  N   GLY A  66      -1.810  23.106   8.621  1.00  8.26           N  
-ATOM    471  CA  GLY A  66      -1.913  24.287   9.457  1.00  7.74           C  
-ATOM    472  C   GLY A  66      -0.715  25.217   9.381  1.00  7.67           C  
-ATOM    473  O   GLY A  66       0.194  25.010   8.576  1.00  7.24           O  
-ATOM    474  N   TYR A  67      -0.718  26.241  10.235  1.00  7.54           N  
-ATOM    475  CA  TYR A  67       0.349  27.239  10.293  1.00  7.74           C  
-ATOM    476  C   TYR A  67       1.015  27.274  11.631  1.00  7.72           C  
-ATOM    477  O   TYR A  67       0.374  27.039  12.659  1.00  8.00           O  
-ATOM    478  CB  TYR A  67      -0.208  28.653   9.973  1.00  7.97           C  
-ATOM    479  CG  TYR A  67      -0.652  28.834   8.540  1.00 10.32           C  
-ATOM    480  CD1 TYR A  67      -2.021  28.950   8.214  1.00 10.39           C  
-ATOM    481  CD2 TYR A  67       0.294  28.886   7.491  1.00 10.92           C  
-ATOM    482  CE1 TYR A  67      -2.449  29.118   6.843  1.00 11.71           C  
-ATOM    483  CE2 TYR A  67      -0.118  29.048   6.124  1.00 12.07           C  
-ATOM    484  CZ  TYR A  67      -1.483  29.161   5.820  1.00 12.31           C  
-ATOM    485  OH  TYR A  67      -1.862  29.303   4.507  1.00 14.17           O  
-ATOM    486  N   MET A  68       2.302  27.623  11.632  1.00  7.03           N  
-ATOM    487  CA  MET A  68       3.103  27.722  12.848  1.00  7.23           C  
-ATOM    488  C   MET A  68       2.696  28.894  13.727  1.00  7.46           C  
-ATOM    489  O   MET A  68       2.756  28.797  14.949  1.00  7.32           O  
-ATOM    490  CB  MET A  68       4.586  27.829  12.517  1.00  7.27           C  
-ATOM    491  CG  MET A  68       5.240  26.595  11.907  1.00  7.75           C  
-ATOM    492  SD  MET A  68       4.928  26.427  10.152  1.00  9.13           S  
-ATOM    493  CE  MET A  68       6.228  27.475   9.503  1.00  8.02           C  
-ATOM    494  N   THR A  69       2.252  29.986  13.100  1.00  7.53           N  
-ATOM    495  CA  THR A  69       1.813  31.195  13.808  1.00  8.51           C  
-ATOM    496  C   THR A  69       0.613  30.909  14.710  1.00  7.72           C  
-ATOM    497  O   THR A  69       0.574  31.356  15.856  1.00  7.91           O  
-ATOM    498  CB  THR A  69       1.513  32.349  12.823  1.00  8.61           C  
-ATOM    499  OG1 THR A  69       0.535  31.927  11.866  1.00  9.01           O  
-ATOM    500  CG2 THR A  69       2.807  32.820  12.141  1.00  9.48           C  
-ATOM    501  N   ASN A  70      -0.307  30.081  14.213  1.00  8.32           N  
-ATOM    502  CA  ASN A  70      -1.510  29.668  14.942  1.00  8.54           C  
-ATOM    503  C   ASN A  70      -1.138  28.764  16.113  1.00  8.61           C  
-ATOM    504  O   ASN A  70      -1.777  28.810  17.166  1.00  8.43           O  
-ATOM    505  CB  ASN A  70      -2.488  28.919  14.012  1.00  9.87           C  
-ATOM    506  CG  ASN A  70      -3.193  29.843  13.008  1.00 11.11           C  
-ATOM    507  OD1 ASN A  70      -3.656  29.316  11.996  1.00 12.21           O  
-ATOM    508  ND2 ASN A  70      -3.302  31.146  13.247  1.00 11.98           N  
-ATOM    509  N   ALA A  71      -0.079  27.967  15.930  1.00  8.59           N  
-ATOM    510  CA  ALA A  71       0.421  27.048  16.962  1.00  8.80           C  
-ATOM    511  C   ALA A  71       1.041  27.826  18.114  1.00  8.92           C  
-ATOM    512  O   ALA A  71       0.755  27.541  19.276  1.00  8.97           O  
-ATOM    513  CB  ALA A  71       1.438  26.070  16.367  1.00  8.37           C  
-ATOM    514  N   PHE A  72       1.816  28.864  17.781  1.00  9.16           N  
-ATOM    515  CA  PHE A  72       2.477  29.731  18.771  1.00  9.01           C  
-ATOM    516  C   PHE A  72       1.454  30.542  19.571  1.00  9.41           C  
-ATOM    517  O   PHE A  72       1.557  30.653  20.797  1.00  8.59           O  
-ATOM    518  CB  PHE A  72       3.475  30.708  18.078  1.00  8.93           C  
-ATOM    519  CG  PHE A  72       4.658  30.034  17.427  1.00  8.94           C  
-ATOM    520  CD1 PHE A  72       5.174  30.539  16.221  1.00  9.52           C  
-ATOM    521  CD2 PHE A  72       5.266  28.898  18.008  1.00  8.78           C  
-ATOM    522  CE1 PHE A  72       6.301  29.920  15.577  1.00 10.22           C  
-ATOM    523  CE2 PHE A  72       6.382  28.263  17.394  1.00  8.89           C  
-ATOM    524  CZ  PHE A  72       6.913  28.768  16.169  1.00  9.35           C  
-ATOM    525  N   GLN A  73       0.442  31.058  18.867  1.00 10.13           N  
-ATOM    526  CA  GLN A  73      -0.638  31.848  19.463  1.00 11.38           C  
-ATOM    527  C   GLN A  73      -1.456  30.992  20.453  1.00 10.81           C  
-ATOM    528  O   GLN A  73      -1.878  31.489  21.496  1.00 10.54           O  
-ATOM    529  CB  GLN A  73      -1.547  32.430  18.370  1.00 13.88           C  
-ATOM    530  CG  GLN A  73      -2.575  33.463  18.849  1.00 18.39           C  
-ATOM    531  CD  GLN A  73      -3.317  34.143  17.693  1.00 20.50           C  
-ATOM    532  OE1 GLN A  73      -2.829  35.097  17.080  1.00 22.47           O  
-ATOM    533  NE2 GLN A  73      -4.509  33.635  17.395  1.00 22.74           N  
-ATOM    534  N   TYR A  74      -1.609  29.699  20.147  1.00  9.91           N  
-ATOM    535  CA  TYR A  74      -2.331  28.774  21.026  1.00  9.46           C  
-ATOM    536  C   TYR A  74      -1.534  28.554  22.310  1.00  9.81           C  
-ATOM    537  O   TYR A  74      -2.103  28.580  23.396  1.00 10.28           O  
-ATOM    538  CB  TYR A  74      -2.631  27.360  20.298  1.00  9.24           C  
-ATOM    539  CG  TYR A  74      -2.924  26.212  21.262  1.00  9.10           C  
-ATOM    540  CD1 TYR A  74      -4.194  26.070  21.867  1.00  8.89           C  
-ATOM    541  CD2 TYR A  74      -1.899  25.312  21.641  1.00  9.18           C  
-ATOM    542  CE1 TYR A  74      -4.432  25.043  22.851  1.00  9.30           C  
-ATOM    543  CE2 TYR A  74      -2.121  24.299  22.612  1.00  9.70           C  
-ATOM    544  CZ  TYR A  74      -3.382  24.171  23.205  1.00  9.94           C  
-ATOM    545  OH  TYR A  74      -3.578  23.164  24.123  1.00 10.81           O  
-ATOM    546  N   VAL A  75      -0.230  28.292  22.170  1.00  9.59           N  
-ATOM    547  CA  VAL A  75       0.673  28.048  23.303  1.00 10.03           C  
-ATOM    548  C   VAL A  75       0.669  29.244  24.259  1.00 10.12           C  
-ATOM    549  O   VAL A  75       0.688  29.072  25.482  1.00 10.20           O  
-ATOM    550  CB  VAL A  75       2.107  27.692  22.809  1.00  9.62           C  
-ATOM    551  CG1 VAL A  75       3.041  27.397  23.979  1.00  9.39           C  
-ATOM    552  CG2 VAL A  75       2.092  26.371  22.065  1.00  9.58           C  
-ATOM    553  N   GLN A  76       0.568  30.442  23.683  1.00 10.62           N  
-ATOM    554  CA  GLN A  76       0.521  31.699  24.430  1.00 11.47           C  
-ATOM    555  C   GLN A  76      -0.777  31.833  25.226  1.00 11.69           C  
-ATOM    556  O   GLN A  76      -0.742  32.059  26.435  1.00 12.65           O  
-ATOM    557  CB  GLN A  76       0.669  32.912  23.472  1.00 11.01           C  
-ATOM    558  CG  GLN A  76       0.595  34.255  24.207  1.00 11.98           C  
-ATOM    559  CD  GLN A  76       0.672  35.507  23.350  1.00 12.39           C  
-ATOM    560  OE1 GLN A  76       1.116  36.556  23.823  1.00 14.29           O  
-ATOM    561  NE2 GLN A  76       0.263  35.410  22.093  1.00 12.92           N  
-ATOM    562  N   ARG A  77      -1.911  31.665  24.543  1.00 12.37           N  
-ATOM    563  CA  ARG A  77      -3.242  31.773  25.151  1.00 13.66           C  
-ATOM    564  C   ARG A  77      -3.547  30.646  26.159  1.00 13.32           C  
-ATOM    565  O   ARG A  77      -4.212  30.870  27.178  1.00 12.21           O  
-ATOM    566  CB  ARG A  77      -4.294  31.807  24.080  1.00 15.34           C  
-ATOM    567  CG  ARG A  77      -4.144  33.068  23.255  1.00 18.38           C  
-ATOM    568  CD  ARG A  77      -5.185  33.128  22.149  1.00 22.00           C  
-ATOM    569  NE  ARG A  77      -5.150  34.406  21.439  1.00 24.78           N  
-ATOM    570  CZ  ARG A  77      -5.967  34.734  20.442  1.00 26.21           C  
-ATOM    571  NH1 ARG A  77      -5.840  35.929  19.879  1.00 26.65           N  
-ATOM    572  NH2 ARG A  77      -6.888  33.881  20.004  1.00 26.71           N  
-ATOM    573  N   ASN A  78      -3.016  29.455  25.876  1.00 13.07           N  
-ATOM    574  CA  ASN A  78      -3.176  28.271  26.721  1.00 13.63           C  
-ATOM    575  C   ASN A  78      -2.232  28.350  27.938  1.00 13.65           C  
-ATOM    576  O   ASN A  78      -2.449  27.674  28.943  1.00 14.04           O  
-ATOM    577  CB  ASN A  78      -2.850  26.982  25.887  1.00 13.63           C  
-ATOM    578  CG  ASN A  78      -3.185  25.689  26.632  1.00 13.99           C  
-ATOM    579  OD1 ASN A  78      -2.306  24.851  26.844  1.00 14.72           O  
-ATOM    580  ND2 ASN A  78      -4.441  25.525  27.030  1.00 12.89           N  
-ATOM    581  N   ARG A1078      -1.193  29.184  27.818  1.00 14.25           N  
-ATOM    582  CA  ARG A1078      -0.158  29.396  28.840  1.00 14.88           C  
-ATOM    583  C   ARG A1078       0.666  28.127  29.051  1.00 14.09           C  
-ATOM    584  O   ARG A1078       1.105  27.819  30.167  1.00 14.24           O  
-ATOM    585  CB  ARG A1078      -0.762  29.887  30.178  1.00 16.53           C  
-ATOM    586  CG  ARG A1078      -1.505  31.211  30.240  1.00 19.56           C  
-ATOM    587  CD  ARG A1078      -2.191  31.331  31.585  1.00 22.09           C  
-ATOM    588  NE  ARG A1078      -2.999  32.537  31.719  1.00 24.91           N  
-ATOM    589  CZ  ARG A1078      -4.178  32.732  31.136  1.00 25.58           C  
-ATOM    590  NH1 ARG A1078      -4.780  33.889  31.379  1.00 25.94           N  
-ATOM    591  NH2 ARG A1078      -4.743  31.841  30.332  1.00 26.35           N  
-ATOM    592  N   GLY A  79       0.835  27.372  27.969  1.00 13.29           N  
-ATOM    593  CA  GLY A  79       1.609  26.151  28.044  1.00 12.34           C  
-ATOM    594  C   GLY A  79       1.380  25.122  26.960  1.00 11.67           C  
-ATOM    595  O   GLY A  79       0.396  25.156  26.221  1.00 11.12           O  
-ATOM    596  N   ILE A  80       2.353  24.224  26.852  1.00 10.87           N  
-ATOM    597  CA  ILE A  80       2.353  23.105  25.923  1.00 10.31           C  
-ATOM    598  C   ILE A  80       2.980  21.945  26.696  1.00 10.15           C  
-ATOM    599  O   ILE A  80       3.910  22.147  27.483  1.00 10.10           O  
-ATOM    600  CB  ILE A  80       3.130  23.417  24.609  1.00 10.19           C  
-ATOM    601  CG1 ILE A  80       3.094  22.128  23.689  1.00  9.66           C  
-ATOM    602  CG2 ILE A  80       4.572  23.909  24.902  1.00  9.19           C  
-ATOM    603  CD1 ILE A  80       3.718  22.323  22.332  1.00  9.35           C  
-ATOM    604  N   ASP A  81       2.451  20.742  26.486  1.00 10.26           N  
-ATOM    605  CA  ASP A  81       2.951  19.537  27.148  1.00 10.45           C  
-ATOM    606  C   ASP A  81       4.224  19.020  26.577  1.00 10.41           C  
-ATOM    607  O   ASP A  81       4.617  19.362  25.457  1.00  9.57           O  
-ATOM    608  CB  ASP A  81       1.913  18.395  27.070  1.00 10.56           C  
-ATOM    609  CG  ASP A  81       0.773  18.570  28.041  1.00 11.03           C  
-ATOM    610  OD1 ASP A  81      -0.345  18.202  27.697  1.00 11.04           O  
-ATOM    611  OD2 ASP A  81       0.990  19.073  29.135  1.00 11.35           O  
-ATOM    612  N   SER A  82       4.892  18.181  27.367  1.00 10.77           N  
-ATOM    613  CA  SER A  82       6.116  17.506  26.953  1.00 11.22           C  
-ATOM    614  C   SER A  82       5.622  16.265  26.160  1.00 11.11           C  
-ATOM    615  O   SER A  82       4.447  15.886  26.279  1.00 10.55           O  
-ATOM    616  CB  SER A  82       6.918  17.047  28.184  1.00 11.51           C  
-ATOM    617  OG  SER A  82       6.158  16.170  29.012  1.00 12.65           O  
-ATOM    618  N   GLU A  83       6.502  15.663  25.357  1.00 11.36           N  
-ATOM    619  CA  GLU A  83       6.156  14.472  24.575  1.00 12.01           C  
-ATOM    620  C   GLU A  83       5.657  13.288  25.459  1.00 12.90           C  
-ATOM    621  O   GLU A  83       4.732  12.578  25.069  1.00 12.49           O  
-ATOM    622  CB  GLU A  83       7.352  14.020  23.692  1.00 11.12           C  
-ATOM    623  CG  GLU A  83       7.178  12.753  22.851  1.00 10.49           C  
-ATOM    624  CD  GLU A  83       6.036  12.720  21.818  1.00 11.22           C  
-ATOM    625  OE1 GLU A  83       5.474  11.650  21.629  1.00 10.77           O  
-ATOM    626  OE2 GLU A  83       5.710  13.747  21.199  1.00 11.44           O  
-ATOM    627  N   ASP A  84       6.230  13.152  26.658  1.00 14.38           N  
-ATOM    628  CA  ASP A  84       5.877  12.097  27.621  1.00 16.37           C  
-ATOM    629  C   ASP A  84       4.481  12.254  28.178  1.00 16.08           C  
-ATOM    630  O   ASP A  84       3.793  11.266  28.443  1.00 16.50           O  
-ATOM    631  CB  ASP A  84       6.863  12.088  28.810  1.00 19.37           C  
-ATOM    632  CG  ASP A  84       8.303  11.867  28.383  1.00 22.48           C  
-ATOM    633  OD1 ASP A  84       9.151  12.497  29.025  1.00 25.19           O  
-ATOM    634  OD2 ASP A  84       8.589  11.096  27.449  1.00 24.92           O  
-ATOM    635  N   ALA A  85       4.056  13.508  28.335  1.00 15.31           N  
-ATOM    636  CA  ALA A  85       2.745  13.846  28.879  1.00 14.33           C  
-ATOM    637  C   ALA A  85       1.618  13.877  27.847  1.00 13.75           C  
-ATOM    638  O   ALA A  85       0.439  13.933  28.213  1.00 13.54           O  
-ATOM    639  CB  ALA A  85       2.822  15.169  29.595  1.00 13.72           C  
-ATOM    640  N   TYR A  86       1.983  13.876  26.566  1.00 12.64           N  
-ATOM    641  CA  TYR A  86       1.005  13.900  25.484  1.00 12.22           C  
-ATOM    642  C   TYR A  86       1.651  13.255  24.238  1.00 12.47           C  
-ATOM    643  O   TYR A  86       2.047  13.968  23.307  1.00 11.75           O  
-ATOM    644  CB  TYR A  86       0.563  15.384  25.183  1.00 11.53           C  
-ATOM    645  CG  TYR A  86      -0.810  15.564  24.552  1.00 11.03           C  
-ATOM    646  CD1 TYR A  86      -1.609  16.664  24.901  1.00 10.51           C  
-ATOM    647  CD2 TYR A  86      -1.315  14.657  23.588  1.00 10.07           C  
-ATOM    648  CE1 TYR A  86      -2.891  16.867  24.295  1.00 10.70           C  
-ATOM    649  CE2 TYR A  86      -2.593  14.847  22.987  1.00 10.42           C  
-ATOM    650  CZ  TYR A  86      -3.366  15.953  23.348  1.00 10.01           C  
-ATOM    651  OH  TYR A  86      -4.600  16.138  22.781  1.00  9.78           O  
-ATOM    652  N   PRO A  87       1.736  11.873  24.182  1.00 12.86           N  
-ATOM    653  CA  PRO A  87       2.329  11.140  23.058  1.00 12.65           C  
-ATOM    654  C   PRO A  87       1.795  11.318  21.664  1.00 12.35           C  
-ATOM    655  O   PRO A  87       0.581  11.424  21.460  1.00 12.14           O  
-ATOM    656  CB  PRO A  87       2.193   9.679  23.496  1.00 13.09           C  
-ATOM    657  CG  PRO A  87       2.213   9.763  24.969  1.00 13.86           C  
-ATOM    658  CD  PRO A  87       1.302  10.921  25.222  1.00 13.32           C  
-ATOM    659  N   TYR A  88       2.707  11.346  20.693  1.00 11.89           N  
-ATOM    660  CA  TYR A  88       2.352  11.501  19.288  1.00 12.11           C  
-ATOM    661  C   TYR A  88       1.798  10.199  18.715  1.00 12.56           C  
-ATOM    662  O   TYR A  88       2.470   9.165  18.757  1.00 13.02           O  
-ATOM    663  CB  TYR A  88       3.584  11.969  18.457  1.00 11.18           C  
-ATOM    664  CG  TYR A  88       3.245  12.296  17.018  1.00 11.05           C  
-ATOM    665  CD1 TYR A  88       2.447  13.414  16.710  1.00 11.13           C  
-ATOM    666  CD2 TYR A  88       3.656  11.451  15.958  1.00 10.73           C  
-ATOM    667  CE1 TYR A  88       2.047  13.695  15.369  1.00 11.07           C  
-ATOM    668  CE2 TYR A  88       3.259  11.721  14.606  1.00 10.65           C  
-ATOM    669  CZ  TYR A  88       2.456  12.847  14.336  1.00 10.42           C  
-ATOM    670  OH  TYR A  88       2.053  13.131  13.057  1.00 10.63           O  
-ATOM    671  N   VAL A  89       0.585  10.261  18.165  1.00 13.21           N  
-ATOM    672  CA  VAL A  89      -0.058   9.086  17.560  1.00 14.46           C  
-ATOM    673  C   VAL A  89      -0.285   9.212  16.048  1.00 14.83           C  
-ATOM    674  O   VAL A  89      -0.561   8.212  15.384  1.00 15.96           O  
-ATOM    675  CB  VAL A  89      -1.345   8.648  18.325  1.00 14.27           C  
-ATOM    676  CG1 VAL A  89      -0.985   8.030  19.668  1.00 14.07           C  
-ATOM    677  CG2 VAL A  89      -2.265   9.825  18.592  1.00 14.47           C  
-ATOM    678  N   GLY A  90      -0.160  10.427  15.511  1.00 15.06           N  
-ATOM    679  CA  GLY A  90      -0.336  10.638  14.078  1.00 15.55           C  
-ATOM    680  C   GLY A  90      -1.750  10.682  13.536  1.00 15.58           C  
-ATOM    681  O   GLY A  90      -1.973  10.388  12.362  1.00 15.65           O  
-ATOM    682  N   GLN A  91      -2.704  11.021  14.394  1.00 16.05           N  
-ATOM    683  CA  GLN A  91      -4.102  11.119  13.995  1.00 17.35           C  
-ATOM    684  C   GLN A  91      -4.825  12.166  14.775  1.00 16.79           C  
-ATOM    685  O   GLN A  91      -4.370  12.587  15.842  1.00 16.61           O  
-ATOM    686  CB  GLN A  91      -4.794   9.780  14.106  1.00 19.46           C  
-ATOM    687  CG  GLN A  91      -4.647   8.892  15.321  1.00 23.22           C  
-ATOM    688  CD  GLN A  91      -5.386   7.557  15.102  1.00 25.57           C  
-ATOM    689  OE1 GLN A  91      -6.037   7.085  16.035  1.00 26.69           O  
-ATOM    690  NE2 GLN A  91      -5.306   6.963  13.910  1.00 26.25           N  
-ATOM    691  N   ASP A  92      -5.947  12.625  14.225  1.00 16.80           N  
-ATOM    692  CA  ASP A  92      -6.782  13.650  14.849  1.00 16.98           C  
-ATOM    693  C   ASP A  92      -7.628  13.088  15.971  1.00 17.20           C  
-ATOM    694  O   ASP A  92      -8.378  12.124  15.781  1.00 17.62           O  
-ATOM    695  CB  ASP A  92      -7.717  14.323  13.797  1.00 17.13           C  
-ATOM    696  CG  ASP A  92      -6.948  15.100  12.733  1.00 17.75           C  
-ATOM    697  OD1 ASP A  92      -7.093  14.810  11.543  1.00 18.16           O  
-ATOM    698  OD2 ASP A  92      -6.202  15.998  13.088  1.00 17.05           O  
-ATOM    699  N   GLU A  93      -7.460  13.660  17.159  1.00 16.67           N  
-ATOM    700  CA  GLU A  93      -8.215  13.274  18.350  1.00 16.47           C  
-ATOM    701  C   GLU A  93      -8.626  14.560  19.061  1.00 15.96           C  
-ATOM    702  O   GLU A  93      -8.143  15.645  18.713  1.00 16.08           O  
-ATOM    703  CB  GLU A  93      -7.353  12.393  19.292  1.00 16.99           C  
-ATOM    704  CG  GLU A  93      -6.946  11.074  18.648  1.00 18.48           C  
-ATOM    705  CD  GLU A  93      -6.273  10.043  19.525  1.00 19.23           C  
-ATOM    706  OE1 GLU A  93      -5.381  10.367  20.295  1.00 19.33           O  
-ATOM    707  OE2 GLU A  93      -6.659   8.889  19.417  1.00 20.13           O  
-ATOM    708  N   SER A  94      -9.503  14.441  20.058  1.00 14.94           N  
-ATOM    709  CA  SER A  94      -9.974  15.597  20.823  1.00 14.71           C  
-ATOM    710  C   SER A  94      -8.860  16.152  21.717  1.00 14.57           C  
-ATOM    711  O   SER A  94      -7.954  15.413  22.112  1.00 14.23           O  
-ATOM    712  CB  SER A  94     -11.205  15.213  21.675  1.00 14.64           C  
-ATOM    713  OG  SER A  94     -10.981  14.165  22.607  1.00 16.33           O  
-ATOM    714  N   CYS A  95      -8.919  17.452  22.010  1.00 14.20           N  
-ATOM    715  CA  CYS A  95      -7.921  18.118  22.853  1.00 14.19           C  
-ATOM    716  C   CYS A  95      -7.905  17.546  24.281  1.00 15.15           C  
-ATOM    717  O   CYS A  95      -8.907  17.593  24.996  1.00 15.58           O  
-ATOM    718  CB  CYS A  95      -8.170  19.630  22.881  1.00 13.26           C  
-ATOM    719  SG  CYS A  95      -6.886  20.478  23.832  1.00 11.94           S  
-ATOM    720  N   MET A  96      -6.761  16.985  24.663  1.00 15.91           N  
-ATOM    721  CA  MET A  96      -6.589  16.380  25.978  1.00 16.65           C  
-ATOM    722  C   MET A  96      -5.375  16.965  26.696  1.00 16.54           C  
-ATOM    723  O   MET A  96      -4.527  16.224  27.208  1.00 15.98           O  
-ATOM    724  CB  MET A  96      -6.440  14.840  25.821  1.00 17.85           C  
-ATOM    725  CG  MET A  96      -6.614  13.966  27.051  1.00 20.00           C  
-ATOM    726  SD  MET A  96      -8.221  14.200  27.813  1.00 22.80           S  
-ATOM    727  CE  MET A  96      -9.293  13.394  26.595  1.00 21.89           C  
-ATOM    728  N   TYR A  97      -5.267  18.296  26.685  1.00 16.53           N  
-ATOM    729  CA  TYR A  97      -4.163  19.004  27.343  1.00 16.92           C  
-ATOM    730  C   TYR A  97      -4.179  18.747  28.856  1.00 17.38           C  
-ATOM    731  O   TYR A  97      -5.214  18.891  29.513  1.00 17.34           O  
-ATOM    732  CB  TYR A  97      -4.222  20.560  27.040  1.00 15.64           C  
-ATOM    733  CG  TYR A  97      -3.183  21.385  27.793  1.00 15.55           C  
-ATOM    734  CD1 TYR A  97      -3.567  22.234  28.852  1.00 14.79           C  
-ATOM    735  CD2 TYR A  97      -1.809  21.302  27.471  1.00 15.35           C  
-ATOM    736  CE1 TYR A  97      -2.602  22.988  29.588  1.00 15.26           C  
-ATOM    737  CE2 TYR A  97      -0.828  22.057  28.203  1.00 15.31           C  
-ATOM    738  CZ  TYR A  97      -1.243  22.891  29.252  1.00 15.45           C  
-ATOM    739  OH  TYR A  97      -0.321  23.638  29.942  1.00 16.29           O  
-ATOM    740  N   ASN A  98      -3.022  18.356  29.383  1.00 18.16           N  
-ATOM    741  CA  ASN A  98      -2.855  18.067  30.802  1.00 19.58           C  
-ATOM    742  C   ASN A  98      -1.970  19.152  31.447  1.00 19.74           C  
-ATOM    743  O   ASN A  98      -0.773  19.202  31.155  1.00 19.47           O  
-ATOM    744  CB  ASN A  98      -2.201  16.661  30.981  1.00 21.27           C  
-ATOM    745  CG  ASN A  98      -2.222  16.165  32.449  1.00 23.24           C  
-ATOM    746  OD1 ASN A  98      -2.504  16.860  33.427  1.00 24.29           O  
-ATOM    747  ND2 ASN A  98      -1.899  14.881  32.556  1.00 24.39           N  
-ATOM    748  N   PRO A  99      -2.454  20.081  32.366  1.00 19.92           N  
-ATOM    749  CA  PRO A  99      -1.595  21.107  32.976  1.00 19.97           C  
-ATOM    750  C   PRO A  99      -0.410  20.639  33.839  1.00 19.92           C  
-ATOM    751  O   PRO A  99       0.593  21.344  33.963  1.00 19.96           O  
-ATOM    752  CB  PRO A  99      -2.596  21.966  33.774  1.00 20.24           C  
-ATOM    753  CG  PRO A  99      -3.699  20.998  34.106  1.00 20.16           C  
-ATOM    754  CD  PRO A  99      -3.854  20.239  32.812  1.00 19.93           C  
-ATOM    755  N   THR A 100      -0.508  19.401  34.335  1.00 19.93           N  
-ATOM    756  CA  THR A 100       0.511  18.763  35.179  1.00 20.34           C  
-ATOM    757  C   THR A 100       1.737  18.352  34.347  1.00 19.20           C  
-ATOM    758  O   THR A 100       2.835  18.166  34.885  1.00 19.50           O  
-ATOM    759  CB  THR A 100      -0.073  17.511  35.896  1.00 21.02           C  
-ATOM    760  OG1 THR A 100      -1.278  17.871  36.579  1.00 22.67           O  
-ATOM    761  CG2 THR A 100       0.831  17.039  37.036  1.00 22.83           C  
-ATOM    762  N   GLY A 101       1.534  18.218  33.039  1.00 17.87           N  
-ATOM    763  CA  GLY A 101       2.613  17.843  32.147  1.00 17.07           C  
-ATOM    764  C   GLY A 101       3.245  18.997  31.394  1.00 16.49           C  
-ATOM    765  O   GLY A 101       4.054  18.766  30.494  1.00 16.29           O  
-ATOM    766  N   LYS A 102       2.889  20.231  31.766  1.00 16.20           N  
-ATOM    767  CA  LYS A 102       3.396  21.463  31.147  1.00 16.20           C  
-ATOM    768  C   LYS A 102       4.921  21.576  31.268  1.00 15.70           C  
-ATOM    769  O   LYS A 102       5.471  21.477  32.365  1.00 15.27           O  
-ATOM    770  CB  LYS A 102       2.725  22.698  31.795  1.00 17.11           C  
-ATOM    771  CG  LYS A 102       3.100  24.095  31.288  1.00 18.88           C  
-ATOM    772  CD  LYS A 102       2.343  25.187  32.041  1.00 19.58           C  
-ATOM    773  CE  LYS A 102       2.746  25.238  33.509  1.00 21.31           C  
-ATOM    774  NZ  LYS A 102       1.888  26.149  34.327  1.00 21.80           N  
-ATOM    775  N   ALA A 103       5.585  21.772  30.129  1.00 15.28           N  
-ATOM    776  CA  ALA A 103       7.043  21.867  30.075  1.00 15.28           C  
-ATOM    777  C   ALA A 103       7.575  23.195  29.578  1.00 14.28           C  
-ATOM    778  O   ALA A 103       8.756  23.498  29.762  1.00 14.55           O  
-ATOM    779  CB  ALA A 103       7.600  20.732  29.228  1.00 15.40           C  
-ATOM    780  N   ALA A 105       6.714  23.978  28.929  1.00 13.66           N  
-ATOM    781  CA  ALA A 105       7.086  25.289  28.391  1.00 13.78           C  
-ATOM    782  C   ALA A 105       5.875  26.100  28.014  1.00 14.11           C  
-ATOM    783  O   ALA A 105       4.754  25.597  27.984  1.00 13.60           O  
-ATOM    784  CB  ALA A 105       7.996  25.128  27.155  1.00 12.70           C  
-ATOM    785  N   LYS A 106       6.112  27.376  27.735  1.00 14.53           N  
-ATOM    786  CA  LYS A 106       5.085  28.306  27.292  1.00 15.49           C  
-ATOM    787  C   LYS A 106       5.774  29.328  26.416  1.00 15.44           C  
-ATOM    788  O   LYS A 106       6.990  29.270  26.220  1.00 15.77           O  
-ATOM    789  CB  LYS A 106       4.396  29.020  28.498  1.00 16.53           C  
-ATOM    790  CG  LYS A 106       5.255  29.977  29.324  1.00 17.80           C  
-ATOM    791  CD  LYS A 106       4.403  31.000  30.057  1.00 18.11           C  
-ATOM    792  CE  LYS A 106       5.282  32.064  30.693  1.00 18.91           C  
-ATOM    793  NZ  LYS A 106       4.449  33.217  31.096  1.00 20.86           N  
-ATOM    794  N   CYS A 107       4.992  30.223  25.831  1.00 15.12           N  
-ATOM    795  CA  CYS A 107       5.556  31.293  25.026  1.00 15.38           C  
-ATOM    796  C   CYS A 107       4.681  32.502  25.151  1.00 15.63           C  
-ATOM    797  O   CYS A 107       3.540  32.405  25.605  1.00 15.49           O  
-ATOM    798  CB  CYS A 107       5.802  30.860  23.537  1.00 15.51           C  
-ATOM    799  SG  CYS A 107       4.439  30.992  22.366  1.00 15.36           S  
-ATOM    800  N   ARG A 108       5.242  33.664  24.836  1.00 15.86           N  
-ATOM    801  CA  ARG A 108       4.523  34.926  24.938  1.00 16.43           C  
-ATOM    802  C   ARG A 108       4.405  35.620  23.590  1.00 16.19           C  
-ATOM    803  O   ARG A 108       4.629  36.828  23.473  1.00 16.50           O  
-ATOM    804  CB  ARG A 108       5.217  35.830  25.967  1.00 17.37           C  
-ATOM    805  CG  ARG A 108       5.243  35.106  27.312  1.00 18.04           C  
-ATOM    806  CD  ARG A 108       6.356  35.633  28.196  1.00 20.05           C  
-ATOM    807  NE  ARG A 108       6.053  36.967  28.685  1.00 20.20           N  
-ATOM    808  CZ  ARG A 108       6.961  37.868  29.037  1.00 19.91           C  
-ATOM    809  NH1 ARG A 108       6.411  38.996  29.455  1.00 19.44           N  
-ATOM    810  NH2 ARG A 108       8.276  37.703  28.964  1.00 19.46           N  
-ATOM    811  N   GLY A 109       4.032  34.844  22.575  1.00 15.71           N  
-ATOM    812  CA  GLY A 109       3.863  35.383  21.239  1.00 15.45           C  
-ATOM    813  C   GLY A 109       4.890  34.902  20.243  1.00 15.77           C  
-ATOM    814  O   GLY A 109       5.654  33.965  20.504  1.00 15.21           O  
-ATOM    815  N   TYR A 110       4.906  35.558  19.090  1.00 15.79           N  
-ATOM    816  CA  TYR A 110       5.823  35.224  18.013  1.00 16.64           C  
-ATOM    817  C   TYR A 110       6.229  36.453  17.235  1.00 17.07           C  
-ATOM    818  O   TYR A 110       5.589  37.500  17.331  1.00 16.96           O  
-ATOM    819  CB  TYR A 110       5.145  34.145  17.023  1.00 16.44           C  
-ATOM    820  CG  TYR A 110       3.884  34.625  16.313  1.00 17.20           C  
-ATOM    821  CD1 TYR A 110       3.958  35.268  15.054  1.00 17.60           C  
-ATOM    822  CD2 TYR A 110       2.613  34.472  16.905  1.00 17.61           C  
-ATOM    823  CE1 TYR A 110       2.786  35.763  14.399  1.00 17.90           C  
-ATOM    824  CE2 TYR A 110       1.423  34.958  16.251  1.00 18.02           C  
-ATOM    825  CZ  TYR A 110       1.534  35.599  15.004  1.00 18.17           C  
-ATOM    826  OH  TYR A 110       0.419  36.068  14.356  1.00 19.12           O  
-ATOM    827  N   ARG A 111       7.276  36.309  16.429  1.00 18.12           N  
-ATOM    828  CA  ARG A 111       7.753  37.381  15.561  1.00 19.38           C  
-ATOM    829  C   ARG A 111       8.041  36.772  14.211  1.00 19.07           C  
-ATOM    830  O   ARG A 111       8.567  35.662  14.123  1.00 17.96           O  
-ATOM    831  CB  ARG A 111       9.013  38.082  16.139  1.00 21.55           C  
-ATOM    832  CG  ARG A 111       8.873  38.877  17.445  1.00 24.88           C  
-ATOM    833  CD  ARG A 111       7.715  39.886  17.404  1.00 28.04           C  
-ATOM    834  NE  ARG A 111       7.545  40.611  18.668  1.00 30.92           N  
-ATOM    835  CZ  ARG A 111       6.815  40.188  19.702  1.00 31.96           C  
-ATOM    836  NH1 ARG A 111       6.740  40.942  20.793  1.00 32.44           N  
-ATOM    837  NH2 ARG A 111       6.137  39.047  19.732  1.00 32.39           N  
-ATOM    838  N   GLU A 112       7.628  37.468  13.155  1.00 19.07           N  
-ATOM    839  CA  GLU A 112       7.828  37.015  11.779  1.00 19.53           C  
-ATOM    840  C   GLU A 112       9.020  37.705  11.132  1.00 19.68           C  
-ATOM    841  O   GLU A 112       9.330  38.850  11.452  1.00 20.00           O  
-ATOM    842  CB  GLU A 112       6.588  37.288  10.955  1.00 20.09           C  
-ATOM    843  CG  GLU A 112       5.369  36.617  11.553  1.00 21.82           C  
-ATOM    844  CD  GLU A 112       4.101  36.929  10.796  1.00 23.02           C  
-ATOM    845  OE1 GLU A 112       3.646  38.073  10.880  1.00 23.61           O  
-ATOM    846  OE2 GLU A 112       3.584  36.023  10.130  1.00 23.76           O  
-ATOM    847  N   ILE A 113       9.696  36.992  10.234  1.00 19.52           N  
-ATOM    848  CA  ILE A 113      10.845  37.521   9.504  1.00 19.72           C  
-ATOM    849  C   ILE A 113      10.284  38.224   8.246  1.00 20.13           C  
-ATOM    850  O   ILE A 113       9.311  37.715   7.676  1.00 19.01           O  
-ATOM    851  CB  ILE A 113      11.867  36.367   9.173  1.00 20.08           C  
-ATOM    852  CG1 ILE A 113      12.762  36.066  10.365  1.00 20.83           C  
-ATOM    853  CG2 ILE A 113      12.757  36.705   7.974  1.00 20.27           C  
-ATOM    854  CD1 ILE A 113      12.159  35.133  11.357  1.00 21.95           C  
-ATOM    855  N   PRO A 114      10.801  39.462   7.767  1.00 20.55           N  
-ATOM    856  CA  PRO A 114      10.304  40.157   6.568  1.00 20.80           C  
-ATOM    857  C   PRO A 114      10.294  39.178   5.383  1.00 20.90           C  
-ATOM    858  O   PRO A 114      11.265  38.450   5.167  1.00 20.40           O  
-ATOM    859  CB  PRO A 114      11.330  41.232   6.364  1.00 20.46           C  
-ATOM    860  CG  PRO A 114      11.625  41.654   7.750  1.00 21.57           C  
-ATOM    861  CD  PRO A 114      11.763  40.326   8.482  1.00 21.05           C  
-ATOM    862  N   GLU A 115       9.162  39.122   4.681  1.00 21.30           N  
-ATOM    863  CA  GLU A 115       8.948  38.236   3.534  1.00 22.00           C  
-ATOM    864  C   GLU A 115      10.026  38.301   2.454  1.00 21.54           C  
-ATOM    865  O   GLU A 115      10.365  39.381   1.967  1.00 21.73           O  
-ATOM    866  CB  GLU A 115       7.583  38.522   2.910  1.00 23.48           C  
-ATOM    867  CG  GLU A 115       7.125  37.705   1.710  1.00 25.52           C  
-ATOM    868  CD  GLU A 115       5.786  38.186   1.162  1.00 27.08           C  
-ATOM    869  OE1 GLU A 115       5.660  39.372   0.813  1.00 28.37           O  
-ATOM    870  OE2 GLU A 115       4.869  37.364   1.091  1.00 27.73           O  
-ATOM    871  N   GLY A 116      10.608  37.140   2.151  1.00 20.84           N  
-ATOM    872  CA  GLY A 116      11.638  37.019   1.127  1.00 20.48           C  
-ATOM    873  C   GLY A 116      13.048  37.470   1.468  1.00 19.91           C  
-ATOM    874  O   GLY A 116      13.941  37.378   0.622  1.00 20.44           O  
-ATOM    875  N   ASN A 117      13.259  37.925   2.701  1.00 18.86           N  
-ATOM    876  CA  ASN A 117      14.566  38.406   3.136  1.00 18.26           C  
-ATOM    877  C   ASN A 117      15.413  37.306   3.816  1.00 17.43           C  
-ATOM    878  O   ASN A 117      15.244  37.034   5.008  1.00 16.58           O  
-ATOM    879  CB  ASN A 117      14.390  39.630   4.095  1.00 18.70           C  
-ATOM    880  CG  ASN A 117      15.638  40.521   4.159  1.00 19.53           C  
-ATOM    881  OD1 ASN A 117      16.790  40.085   4.102  1.00 19.64           O  
-ATOM    882  ND2 ASN A 117      15.370  41.818   4.294  1.00 20.16           N  
-ATOM    883  N   GLU A 118      16.333  36.710   3.052  1.00 16.67           N  
-ATOM    884  CA  GLU A 118      17.224  35.656   3.556  1.00 16.37           C  
-ATOM    885  C   GLU A 118      18.298  36.185   4.503  1.00 15.93           C  
-ATOM    886  O   GLU A 118      18.794  35.443   5.357  1.00 15.72           O  
-ATOM    887  CB  GLU A 118      17.877  34.896   2.422  1.00 16.51           C  
-ATOM    888  CG  GLU A 118      16.943  33.937   1.707  1.00 17.08           C  
-ATOM    889  CD  GLU A 118      17.755  33.011   0.829  1.00 17.52           C  
-ATOM    890  OE1 GLU A 118      17.816  33.272  -0.364  1.00 18.37           O  
-ATOM    891  OE2 GLU A 118      18.327  32.037   1.326  1.00 17.21           O  
-ATOM    892  N   ALA A 119      18.642  37.468   4.355  1.00 15.35           N  
-ATOM    893  CA  ALA A 119      19.633  38.129   5.208  1.00 15.33           C  
-ATOM    894  C   ALA A 119      19.044  38.341   6.617  1.00 15.08           C  
-ATOM    895  O   ALA A 119      19.753  38.192   7.616  1.00 14.57           O  
-ATOM    896  CB  ALA A 119      20.065  39.472   4.598  1.00 15.77           C  
-ATOM    897  N   ALA A 120      17.740  38.640   6.681  1.00 14.69           N  
-ATOM    898  CA  ALA A 120      17.034  38.845   7.955  1.00 14.85           C  
-ATOM    899  C   ALA A 120      16.861  37.509   8.650  1.00 14.42           C  
-ATOM    900  O   ALA A 120      16.957  37.426   9.877  1.00 14.18           O  
-ATOM    901  CB  ALA A 120      15.677  39.498   7.730  1.00 14.68           C  
-ATOM    902  N   LEU A 121      16.651  36.453   7.853  1.00 14.27           N  
-ATOM    903  CA  LEU A 121      16.495  35.089   8.365  1.00 14.05           C  
-ATOM    904  C   LEU A 121      17.829  34.595   8.942  1.00 13.95           C  
-ATOM    905  O   LEU A 121      17.842  33.879   9.942  1.00 13.92           O  
-ATOM    906  CB  LEU A 121      15.983  34.120   7.250  1.00 13.59           C  
-ATOM    907  CG  LEU A 121      15.704  32.580   7.552  1.00 14.00           C  
-ATOM    908  CD1 LEU A 121      14.733  32.415   8.711  1.00 13.44           C  
-ATOM    909  CD2 LEU A 121      15.215  31.874   6.298  1.00 14.07           C  
-ATOM    910  N   LYS A 122      18.939  35.039   8.340  1.00 14.11           N  
-ATOM    911  CA  LYS A 122      20.297  34.687   8.776  1.00 14.44           C  
-ATOM    912  C   LYS A 122      20.602  35.297  10.138  1.00 14.30           C  
-ATOM    913  O   LYS A 122      21.115  34.618  11.028  1.00 13.45           O  
-ATOM    914  CB  LYS A 122      21.342  35.160   7.735  1.00 14.62           C  
-ATOM    915  CG  LYS A 122      22.793  34.848   8.105  1.00 16.15           C  
-ATOM    916  CD  LYS A 122      23.784  35.573   7.198  1.00 16.51           C  
-ATOM    917  CE  LYS A 122      25.188  35.513   7.775  1.00 17.23           C  
-ATOM    918  NZ  LYS A 122      26.158  36.283   6.946  1.00 18.03           N  
-ATOM    919  N   ARG A 123      20.247  36.572  10.301  1.00 14.86           N  
-ATOM    920  CA  ARG A 123      20.454  37.299  11.553  1.00 15.71           C  
-ATOM    921  C   ARG A 123      19.575  36.767  12.653  1.00 14.85           C  
-ATOM    922  O   ARG A 123      19.973  36.774  13.817  1.00 15.34           O  
-ATOM    923  CB  ARG A 123      20.189  38.760  11.375  1.00 18.09           C  
-ATOM    924  CG  ARG A 123      21.170  39.376  10.408  1.00 21.63           C  
-ATOM    925  CD  ARG A 123      21.046  40.887  10.406  1.00 24.90           C  
-ATOM    926  NE  ARG A 123      21.586  41.457   9.176  1.00 27.97           N  
-ATOM    927  CZ  ARG A 123      20.850  42.055   8.243  1.00 29.07           C  
-ATOM    928  NH1 ARG A 123      21.474  42.521   7.170  1.00 30.37           N  
-ATOM    929  NH2 ARG A 123      19.534  42.216   8.354  1.00 29.62           N  
-ATOM    930  N   ALA A 124      18.383  36.286  12.285  1.00 13.69           N  
-ATOM    931  CA  ALA A 124      17.432  35.714  13.241  1.00 13.49           C  
-ATOM    932  C   ALA A 124      17.981  34.396  13.809  1.00 12.76           C  
-ATOM    933  O   ALA A 124      17.997  34.208  15.022  1.00 13.37           O  
-ATOM    934  CB  ALA A 124      16.072  35.489  12.586  1.00 12.98           C  
-ATOM    935  N   VAL A 125      18.522  33.547  12.932  1.00 11.57           N  
-ATOM    936  CA  VAL A 125      19.094  32.256  13.325  1.00 11.28           C  
-ATOM    937  C   VAL A 125      20.327  32.459  14.242  1.00 11.04           C  
-ATOM    938  O   VAL A 125      20.430  31.820  15.285  1.00 10.72           O  
-ATOM    939  CB  VAL A 125      19.415  31.378  12.076  1.00 10.58           C  
-ATOM    940  CG1 VAL A 125      20.038  30.048  12.483  1.00  9.94           C  
-ATOM    941  CG2 VAL A 125      18.123  30.981  11.355  1.00 10.50           C  
-ATOM    942  N   ALA A 126      21.193  33.403  13.875  1.00 11.10           N  
-ATOM    943  CA  ALA A 126      22.404  33.723  14.640  1.00 12.00           C  
-ATOM    944  C   ALA A 126      22.118  34.286  16.033  1.00 12.53           C  
-ATOM    945  O   ALA A 126      22.776  33.905  17.001  1.00 12.64           O  
-ATOM    946  CB  ALA A 126      23.269  34.700  13.865  1.00 11.16           C  
-ATOM    947  N   ALA A 127      21.101  35.144  16.131  1.00 13.76           N  
-ATOM    948  CA  ALA A 127      20.736  35.787  17.392  1.00 14.67           C  
-ATOM    949  C   ALA A 127      19.756  35.038  18.316  1.00 15.19           C  
-ATOM    950  O   ALA A 127      19.996  34.977  19.522  1.00 15.98           O  
-ATOM    951  CB  ALA A 127      20.242  37.214  17.134  1.00 14.61           C  
-ATOM    952  N   VAL A1127      18.673  34.480  17.763  1.00 15.45           N  
-ATOM    953  CA  VAL A1127      17.677  33.771  18.582  1.00 15.62           C  
-ATOM    954  C   VAL A1127      17.833  32.246  18.635  1.00 15.08           C  
-ATOM    955  O   VAL A1127      17.582  31.633  19.671  1.00 15.39           O  
-ATOM    956  CB  VAL A1127      16.190  34.182  18.228  1.00 16.47           C  
-ATOM    957  CG1 VAL A1127      16.065  35.698  18.089  1.00 17.35           C  
-ATOM    958  CG2 VAL A1127      15.672  33.463  16.985  1.00 17.97           C  
-ATOM    959  N   GLY A 128      18.240  31.650  17.518  1.00 13.93           N  
-ATOM    960  CA  GLY A 128      18.397  30.207  17.453  1.00 13.43           C  
-ATOM    961  C   GLY A 128      17.497  29.616  16.385  1.00 12.29           C  
-ATOM    962  O   GLY A 128      17.149  30.327  15.440  1.00 12.67           O  
-ATOM    963  N   PRO A 129      17.112  28.291  16.469  1.00 11.17           N  
-ATOM    964  CA  PRO A 129      16.236  27.659  15.471  1.00 10.65           C  
-ATOM    965  C   PRO A 129      14.912  28.399  15.135  1.00 10.35           C  
-ATOM    966  O   PRO A 129      14.160  28.785  16.033  1.00  9.79           O  
-ATOM    967  CB  PRO A 129      15.983  26.309  16.066  1.00 10.57           C  
-ATOM    968  CG  PRO A 129      17.297  25.980  16.688  1.00 10.76           C  
-ATOM    969  CD  PRO A 129      17.632  27.275  17.404  1.00 11.43           C  
-ATOM    970  N   VAL A 130      14.699  28.646  13.840  1.00  9.92           N  
-ATOM    971  CA  VAL A 130      13.526  29.359  13.321  1.00 10.22           C  
-ATOM    972  C   VAL A 130      12.663  28.427  12.434  1.00  9.96           C  
-ATOM    973  O   VAL A 130      13.201  27.658  11.633  1.00 10.12           O  
-ATOM    974  CB  VAL A 130      13.991  30.620  12.501  1.00 10.97           C  
-ATOM    975  CG1 VAL A 130      12.820  31.342  11.837  1.00 10.67           C  
-ATOM    976  CG2 VAL A 130      14.571  31.691  13.438  1.00 11.56           C  
-ATOM    977  N   SER A 131      11.340  28.499  12.601  1.00  8.91           N  
-ATOM    978  CA  SER A 131      10.388  27.702  11.811  1.00  9.86           C  
-ATOM    979  C   SER A 131      10.245  28.329  10.438  1.00  9.69           C  
-ATOM    980  O   SER A 131      10.042  29.538  10.344  1.00  9.22           O  
-ATOM    981  CB  SER A 131       8.993  27.689  12.478  1.00  9.41           C  
-ATOM    982  OG  SER A 131       8.862  27.089  13.745  1.00 11.61           O  
-ATOM    983  N   VAL A 132      10.410  27.531   9.381  1.00 10.03           N  
-ATOM    984  CA  VAL A 132      10.290  28.017   8.000  1.00 10.79           C  
-ATOM    985  C   VAL A 132       9.356  27.152   7.133  1.00 11.31           C  
-ATOM    986  O   VAL A 132       9.169  25.959   7.398  1.00 11.40           O  
-ATOM    987  CB  VAL A 132      11.673  28.120   7.257  1.00 10.89           C  
-ATOM    988  CG1 VAL A 132      12.602  29.114   7.943  1.00 11.40           C  
-ATOM    989  CG2 VAL A 132      12.418  26.799   7.266  1.00 11.72           C  
-ATOM    990  N   ALA A 133       8.777  27.775   6.105  1.00 11.07           N  
-ATOM    991  CA  ALA A 133       7.886  27.112   5.156  1.00 11.17           C  
-ATOM    992  C   ALA A 133       8.585  27.024   3.795  1.00 11.57           C  
-ATOM    993  O   ALA A 133       9.217  27.990   3.343  1.00 11.46           O  
-ATOM    994  CB  ALA A 133       6.575  27.872   5.025  1.00 10.28           C  
-ATOM    995  N   ILE A 134       8.504  25.852   3.167  1.00 11.38           N  
-ATOM    996  CA  ILE A 134       9.131  25.621   1.866  1.00 11.94           C  
-ATOM    997  C   ILE A 134       8.246  24.829   0.906  1.00 12.34           C  
-ATOM    998  O   ILE A 134       7.188  24.319   1.286  1.00 11.95           O  
-ATOM    999  CB  ILE A 134      10.438  24.759   1.971  1.00 11.41           C  
-ATOM   1000  CG1 ILE A 134      10.171  23.432   2.701  1.00 12.27           C  
-ATOM   1001  CG2 ILE A 134      11.581  25.554   2.606  1.00 12.26           C  
-ATOM   1002  CD1 ILE A 134      11.286  22.417   2.569  1.00 12.21           C  
-ATOM   1003  N   ASP A 135       8.693  24.743  -0.347  1.00 13.23           N  
-ATOM   1004  CA  ASP A 135       8.029  23.957  -1.382  1.00 13.70           C  
-ATOM   1005  C   ASP A 135       8.809  22.634  -1.345  1.00 14.18           C  
-ATOM   1006  O   ASP A 135       9.995  22.592  -1.687  1.00 14.45           O  
-ATOM   1007  CB  ASP A 135       8.174  24.629  -2.760  1.00 14.63           C  
-ATOM   1008  CG  ASP A 135       7.659  23.738  -3.930  1.00 15.18           C  
-ATOM   1009  OD1 ASP A 135       7.995  24.060  -5.055  1.00 16.49           O  
-ATOM   1010  OD2 ASP A 135       6.968  22.733  -3.763  1.00 15.35           O  
-ATOM   1011  N   ALA A 136       8.136  21.572  -0.913  1.00 14.52           N  
-ATOM   1012  CA  ALA A 136       8.741  20.250  -0.805  1.00 15.19           C  
-ATOM   1013  C   ALA A 136       8.037  19.209  -1.680  1.00 14.89           C  
-ATOM   1014  O   ALA A 136       8.160  18.009  -1.437  1.00 14.90           O  
-ATOM   1015  CB  ALA A 136       8.722  19.811   0.649  1.00 15.06           C  
-ATOM   1016  N   SER A 137       7.373  19.673  -2.739  1.00 15.73           N  
-ATOM   1017  CA  SER A 137       6.611  18.807  -3.650  1.00 16.42           C  
-ATOM   1018  C   SER A 137       7.410  18.020  -4.707  1.00 17.14           C  
-ATOM   1019  O   SER A 137       6.939  16.990  -5.203  1.00 17.27           O  
-ATOM   1020  CB  SER A 137       5.541  19.617  -4.348  1.00 16.36           C  
-ATOM   1021  OG  SER A 137       6.133  20.644  -5.152  1.00 16.21           O  
-ATOM   1022  N   LEU A 138       8.603  18.509  -5.043  1.00 17.00           N  
-ATOM   1023  CA  LEU A 138       9.446  17.880  -6.056  1.00 17.51           C  
-ATOM   1024  C   LEU A 138      10.065  16.540  -5.679  1.00 17.91           C  
-ATOM   1025  O   LEU A 138      10.375  16.282  -4.511  1.00 17.28           O  
-ATOM   1026  CB  LEU A 138      10.518  18.831  -6.498  1.00 17.92           C  
-ATOM   1027  CG  LEU A 138      10.074  20.186  -7.056  1.00 18.12           C  
-ATOM   1028  CD1 LEU A 138      11.299  20.989  -7.366  1.00 18.07           C  
-ATOM   1029  CD2 LEU A 138       9.256  20.041  -8.343  1.00 19.04           C  
-ATOM   1030  N   THR A 139      10.250  15.696  -6.699  1.00 18.07           N  
-ATOM   1031  CA  THR A 139      10.832  14.350  -6.591  1.00 18.33           C  
-ATOM   1032  C   THR A 139      12.289  14.426  -6.108  1.00 17.94           C  
-ATOM   1033  O   THR A 139      12.746  13.576  -5.336  1.00 18.18           O  
-ATOM   1034  CB  THR A 139      10.736  13.618  -7.961  1.00 18.44           C  
-ATOM   1035  OG1 THR A 139       9.372  13.604  -8.393  1.00 19.99           O  
-ATOM   1036  CG2 THR A 139      11.085  12.143  -7.842  1.00 19.50           C  
-ATOM   1037  N   SER A 140      12.987  15.480  -6.531  1.00 17.82           N  
-ATOM   1038  CA  SER A 140      14.379  15.718  -6.153  1.00 17.68           C  
-ATOM   1039  C   SER A 140      14.510  15.972  -4.625  1.00 17.67           C  
-ATOM   1040  O   SER A 140      15.550  15.679  -4.027  1.00 17.38           O  
-ATOM   1041  CB  SER A 140      14.941  16.890  -6.945  1.00 17.68           C  
-ATOM   1042  OG  SER A 140      14.081  18.002  -6.828  1.00 18.07           O  
-ATOM   1043  N   PHE A 141      13.440  16.497  -4.018  1.00 17.64           N  
-ATOM   1044  CA  PHE A 141      13.415  16.752  -2.583  1.00 17.91           C  
-ATOM   1045  C   PHE A 141      13.196  15.441  -1.825  1.00 18.53           C  
-ATOM   1046  O   PHE A 141      13.912  15.153  -0.868  1.00 18.30           O  
-ATOM   1047  CB  PHE A 141      12.301  17.813  -2.189  1.00 16.92           C  
-ATOM   1048  CG  PHE A 141      12.363  18.244  -0.740  1.00 16.14           C  
-ATOM   1049  CD1 PHE A 141      13.187  19.315  -0.355  1.00 15.53           C  
-ATOM   1050  CD2 PHE A 141      11.623  17.560   0.252  1.00 15.61           C  
-ATOM   1051  CE1 PHE A 141      13.295  19.708   1.015  1.00 15.21           C  
-ATOM   1052  CE2 PHE A 141      11.712  17.934   1.640  1.00 15.44           C  
-ATOM   1053  CZ  PHE A 141      12.558  19.016   2.020  1.00 14.89           C  
-ATOM   1054  N   GLN A 142      12.217  14.653  -2.270  1.00 20.03           N  
-ATOM   1055  CA  GLN A 142      11.867  13.370  -1.647  1.00 21.74           C  
-ATOM   1056  C   GLN A 142      13.021  12.379  -1.606  1.00 21.50           C  
-ATOM   1057  O   GLN A 142      13.242  11.717  -0.587  1.00 21.31           O  
-ATOM   1058  CB  GLN A 142      10.705  12.722  -2.381  1.00 23.70           C  
-ATOM   1059  CG  GLN A 142       9.597  13.509  -3.065  1.00 27.60           C  
-ATOM   1060  CD  GLN A 142       8.606  14.371  -2.308  1.00 29.63           C  
-ATOM   1061  OE1 GLN A 142       8.966  15.354  -1.657  1.00 31.28           O  
-ATOM   1062  NE2 GLN A 142       7.328  14.008  -2.416  1.00 30.86           N  
-ATOM   1063  N   PHE A 143      13.793  12.332  -2.692  1.00 21.74           N  
-ATOM   1064  CA  PHE A 143      14.923  11.412  -2.810  1.00 22.30           C  
-ATOM   1065  C   PHE A 143      16.289  11.993  -2.542  1.00 22.39           C  
-ATOM   1066  O   PHE A 143      17.309  11.419  -2.948  1.00 22.11           O  
-ATOM   1067  CB  PHE A 143      14.880  10.682  -4.186  1.00 22.81           C  
-ATOM   1068  CG  PHE A 143      13.709   9.747  -4.327  1.00 23.44           C  
-ATOM   1069  CD1 PHE A 143      12.572  10.138  -5.052  1.00 23.30           C  
-ATOM   1070  CD2 PHE A 143      13.730   8.479  -3.710  1.00 24.04           C  
-ATOM   1071  CE1 PHE A 143      11.430   9.271  -5.169  1.00 23.96           C  
-ATOM   1072  CE2 PHE A 143      12.602   7.584  -3.806  1.00 24.28           C  
-ATOM   1073  CZ  PHE A 143      11.442   7.987  -4.542  1.00 24.07           C  
-ATOM   1074  N   TYR A 144      16.321  13.100  -1.796  1.00 22.29           N  
-ATOM   1075  CA  TYR A 144      17.569  13.775  -1.433  1.00 22.27           C  
-ATOM   1076  C   TYR A 144      18.487  12.884  -0.562  1.00 22.92           C  
-ATOM   1077  O   TYR A 144      18.021  12.115   0.276  1.00 23.25           O  
-ATOM   1078  CB  TYR A 144      17.270  15.174  -0.672  1.00 21.02           C  
-ATOM   1079  CG  TYR A 144      18.496  15.835  -0.053  1.00 19.60           C  
-ATOM   1080  CD1 TYR A 144      18.898  15.517   1.268  1.00 19.16           C  
-ATOM   1081  CD2 TYR A 144      19.291  16.736  -0.791  1.00 19.22           C  
-ATOM   1082  CE1 TYR A 144      20.074  16.071   1.843  1.00 18.83           C  
-ATOM   1083  CE2 TYR A 144      20.481  17.316  -0.211  1.00 18.73           C  
-ATOM   1084  CZ  TYR A 144      20.848  16.966   1.106  1.00 18.61           C  
-ATOM   1085  OH  TYR A 144      21.951  17.513   1.713  1.00 18.18           O  
-ATOM   1086  N   SER A 145      19.792  13.080  -0.740  1.00 23.89           N  
-ATOM   1087  CA  SER A 145      20.856  12.390  -0.015  1.00 25.37           C  
-ATOM   1088  C   SER A 145      22.134  13.106  -0.405  1.00 25.78           C  
-ATOM   1089  O   SER A 145      22.496  13.123  -1.586  1.00 27.64           O  
-ATOM   1090  CB  SER A 145      20.946  10.899  -0.428  1.00 25.47           C  
-ATOM   1091  OG  SER A 145      21.275  10.685  -1.799  1.00 26.49           O  
-ATOM   1092  N   ALA A 146      22.772  13.764   0.565  1.00 25.97           N  
-ATOM   1093  CA  ALA A 146      24.039  14.503   0.383  1.00 25.25           C  
-ATOM   1094  C   ALA A 146      24.058  15.736  -0.571  1.00 24.63           C  
-ATOM   1095  O   ALA A 146      23.303  15.807  -1.549  1.00 24.37           O  
-ATOM   1096  CB  ALA A 146      25.183  13.530   0.011  1.00 25.32           C  
-ATOM   1097  N   GLY A 147      24.936  16.690  -0.252  1.00 23.75           N  
-ATOM   1098  CA  GLY A 147      25.109  17.899  -1.046  1.00 22.36           C  
-ATOM   1099  C   GLY A 147      24.166  19.042  -0.737  1.00 21.45           C  
-ATOM   1100  O   GLY A 147      23.289  18.923   0.113  1.00 21.76           O  
-ATOM   1101  N   VAL A 148      24.375  20.169  -1.411  1.00 20.65           N  
-ATOM   1102  CA  VAL A 148      23.538  21.350  -1.242  1.00 19.71           C  
-ATOM   1103  C   VAL A 148      22.407  21.223  -2.260  1.00 19.73           C  
-ATOM   1104  O   VAL A 148      22.648  21.171  -3.467  1.00 19.69           O  
-ATOM   1105  CB  VAL A 148      24.364  22.661  -1.411  1.00 19.83           C  
-ATOM   1106  CG1 VAL A 148      23.479  23.898  -1.245  1.00 19.08           C  
-ATOM   1107  CG2 VAL A 148      25.376  22.809  -0.280  1.00 19.15           C  
-ATOM   1108  N   TYR A 149      21.177  21.151  -1.760  1.00 19.14           N  
-ATOM   1109  CA  TYR A 149      20.000  21.017  -2.610  1.00 18.86           C  
-ATOM   1110  C   TYR A 149      19.569  22.308  -3.284  1.00 19.00           C  
-ATOM   1111  O   TYR A 149      19.422  23.352  -2.648  1.00 17.95           O  
-ATOM   1112  CB  TYR A 149      18.807  20.406  -1.800  1.00 17.61           C  
-ATOM   1113  CG  TYR A 149      17.506  20.250  -2.575  1.00 17.00           C  
-ATOM   1114  CD1 TYR A 149      16.422  21.134  -2.359  1.00 15.83           C  
-ATOM   1115  CD2 TYR A 149      17.364  19.247  -3.556  1.00 16.55           C  
-ATOM   1116  CE1 TYR A 149      15.208  21.024  -3.120  1.00 15.85           C  
-ATOM   1117  CE2 TYR A 149      16.154  19.129  -4.324  1.00 16.07           C  
-ATOM   1118  CZ  TYR A 149      15.093  20.019  -4.095  1.00 15.33           C  
-ATOM   1119  OH  TYR A 149      13.931  19.899  -4.819  1.00 15.00           O  
-ATOM   1120  N   TYR A 150      19.312  22.189  -4.583  1.00 20.07           N  
-ATOM   1121  CA  TYR A 150      18.834  23.269  -5.433  1.00 21.72           C  
-ATOM   1122  C   TYR A 150      18.157  22.629  -6.644  1.00 21.88           C  
-ATOM   1123  O   TYR A 150      18.676  21.680  -7.240  1.00 22.07           O  
-ATOM   1124  CB  TYR A 150      20.018  24.245  -5.898  1.00 23.13           C  
-ATOM   1125  CG  TYR A 150      19.553  25.383  -6.800  1.00 25.27           C  
-ATOM   1126  CD1 TYR A 150      18.778  26.448  -6.285  1.00 26.13           C  
-ATOM   1127  CD2 TYR A 150      19.818  25.365  -8.190  1.00 26.36           C  
-ATOM   1128  CE1 TYR A 150      18.259  27.486  -7.150  1.00 27.23           C  
-ATOM   1129  CE2 TYR A 150      19.302  26.398  -9.069  1.00 27.31           C  
-ATOM   1130  CZ  TYR A 150      18.529  27.440  -8.531  1.00 27.69           C  
-ATOM   1131  OH  TYR A 150      18.023  28.417  -9.361  1.00 29.01           O  
-ATOM   1132  N   ASP A1150      16.992  23.161  -6.992  1.00 22.29           N  
-ATOM   1133  CA  ASP A1150      16.217  22.701  -8.135  1.00 22.75           C  
-ATOM   1134  C   ASP A1150      15.516  23.932  -8.685  1.00 23.20           C  
-ATOM   1135  O   ASP A1150      14.762  24.605  -7.970  1.00 22.34           O  
-ATOM   1136  CB  ASP A1150      15.186  21.626  -7.707  1.00 22.71           C  
-ATOM   1137  CG  ASP A1150      14.626  20.824  -8.901  1.00 23.13           C  
-ATOM   1138  OD1 ASP A1150      14.127  21.373  -9.889  1.00 23.31           O  
-ATOM   1139  OD2 ASP A1150      14.670  19.607  -8.841  1.00 23.26           O  
-ATOM   1140  N   GLU A 151      15.761  24.217  -9.966  1.00 23.90           N  
-ATOM   1141  CA  GLU A 151      15.186  25.370 -10.668  1.00 24.84           C  
-ATOM   1142  C   GLU A 151      13.650  25.349 -10.783  1.00 24.49           C  
-ATOM   1143  O   GLU A 151      13.024  26.391 -10.987  1.00 24.47           O  
-ATOM   1144  CB  GLU A 151      15.814  25.505 -12.059  1.00 26.18           C  
-ATOM   1145  CG  GLU A 151      15.792  24.259 -12.933  1.00 28.30           C  
-ATOM   1146  CD  GLU A 151      16.331  24.523 -14.335  1.00 29.87           C  
-ATOM   1147  OE1 GLU A 151      15.664  24.127 -15.295  1.00 31.22           O  
-ATOM   1148  OE2 GLU A 151      17.401  25.120 -14.478  1.00 30.86           O  
-ATOM   1149  N   ASN A 152      13.062  24.165 -10.611  1.00 24.35           N  
-ATOM   1150  CA  ASN A 152      11.614  23.970 -10.676  1.00 24.57           C  
-ATOM   1151  C   ASN A 152      10.915  24.241  -9.325  1.00 24.15           C  
-ATOM   1152  O   ASN A 152       9.685  24.190  -9.247  1.00 23.88           O  
-ATOM   1153  CB  ASN A 152      11.281  22.537 -11.151  1.00 25.44           C  
-ATOM   1154  CG  ASN A 152      11.848  22.230 -12.526  1.00 26.84           C  
-ATOM   1155  OD1 ASN A 152      12.679  21.329 -12.679  1.00 27.42           O  
-ATOM   1156  ND2 ASN A 152      11.411  22.982 -13.531  1.00 26.90           N  
-ATOM   1157  N   CYS A 153      11.702  24.509  -8.278  1.00 23.30           N  
-ATOM   1158  CA  CYS A 153      11.167  24.801  -6.943  1.00 23.00           C  
-ATOM   1159  C   CYS A 153      10.462  26.137  -6.960  1.00 23.66           C  
-ATOM   1160  O   CYS A 153      10.998  27.129  -7.461  1.00 23.87           O  
-ATOM   1161  CB  CYS A 153      12.288  24.804  -5.879  1.00 21.21           C  
-ATOM   1162  SG  CYS A 153      11.712  24.034  -4.328  1.00 19.35           S  
-ATOM   1163  N   SER A 154       9.225  26.142  -6.472  1.00 24.55           N  
-ATOM   1164  CA  SER A 154       8.407  27.345  -6.435  1.00 25.81           C  
-ATOM   1165  C   SER A 154       8.586  28.143  -5.178  1.00 26.41           C  
-ATOM   1166  O   SER A 154       8.722  27.588  -4.085  1.00 26.90           O  
-ATOM   1167  CB  SER A 154       6.937  26.981  -6.603  1.00 26.30           C  
-ATOM   1168  OG  SER A 154       6.081  28.127  -6.528  1.00 26.45           O  
-ATOM   1169  N   SER A 155       8.554  29.464  -5.332  1.00 26.81           N  
-ATOM   1170  CA  SER A 155       8.681  30.390  -4.216  1.00 27.55           C  
-ATOM   1171  C   SER A 155       7.309  30.793  -3.683  1.00 27.77           C  
-ATOM   1172  O   SER A 155       7.194  31.272  -2.554  1.00 28.10           O  
-ATOM   1173  CB  SER A 155       9.462  31.624  -4.631  1.00 27.73           C  
-ATOM   1174  OG  SER A 155      10.816  31.241  -4.814  1.00 29.05           O  
-ATOM   1175  N   ASP A 156       6.271  30.553  -4.484  1.00 28.19           N  
-ATOM   1176  CA  ASP A 156       4.894  30.897  -4.120  1.00 28.66           C  
-ATOM   1177  C   ASP A 156       4.031  29.724  -3.697  1.00 28.17           C  
-ATOM   1178  O   ASP A 156       2.989  29.925  -3.067  1.00 29.00           O  
-ATOM   1179  CB  ASP A 156       4.214  31.640  -5.253  1.00 29.91           C  
-ATOM   1180  CG  ASP A 156       4.935  32.920  -5.626  1.00 31.05           C  
-ATOM   1181  OD1 ASP A 156       4.969  33.867  -4.828  1.00 31.75           O  
-ATOM   1182  OD2 ASP A 156       5.469  32.927  -6.737  1.00 32.50           O  
-ATOM   1183  N   ALA A1156       4.447  28.508  -4.056  1.00 26.83           N  
-ATOM   1184  CA  ALA A1156       3.709  27.292  -3.706  1.00 25.34           C  
-ATOM   1185  C   ALA A1156       4.285  26.613  -2.460  1.00 23.94           C  
-ATOM   1186  O   ALA A1156       4.911  25.549  -2.544  1.00 24.67           O  
-ATOM   1187  CB  ALA A1156       3.677  26.318  -4.892  1.00 25.67           C  
-ATOM   1188  N   LEU A 157       4.083  27.252  -1.306  1.00 21.93           N  
-ATOM   1189  CA  LEU A 157       4.549  26.736  -0.011  1.00 20.05           C  
-ATOM   1190  C   LEU A 157       3.552  25.655   0.464  1.00 18.38           C  
-ATOM   1191  O   LEU A 157       2.348  25.905   0.550  1.00 17.99           O  
-ATOM   1192  CB  LEU A 157       4.641  27.872   1.012  1.00 20.48           C  
-ATOM   1193  CG  LEU A 157       5.465  29.153   0.728  1.00 21.07           C  
-ATOM   1194  CD1 LEU A 157       5.305  30.148   1.872  1.00 21.65           C  
-ATOM   1195  CD2 LEU A 157       6.942  28.830   0.585  1.00 21.31           C  
-ATOM   1196  N   ASN A 158       4.077  24.476   0.786  1.00 16.21           N  
-ATOM   1197  CA  ASN A 158       3.260  23.333   1.193  1.00 14.89           C  
-ATOM   1198  C   ASN A 158       3.803  22.503   2.360  1.00 13.59           C  
-ATOM   1199  O   ASN A 158       3.137  21.570   2.817  1.00 12.96           O  
-ATOM   1200  CB  ASN A 158       3.071  22.394  -0.040  1.00 14.87           C  
-ATOM   1201  CG  ASN A 158       4.412  22.085  -0.762  1.00 15.64           C  
-ATOM   1202  OD1 ASN A 158       5.321  21.476  -0.194  1.00 15.85           O  
-ATOM   1203  ND2 ASN A 158       4.532  22.551  -2.004  1.00 15.44           N  
-ATOM   1204  N   HIS A 159       5.010  22.831   2.822  1.00 12.42           N  
-ATOM   1205  CA  HIS A 159       5.657  22.077   3.893  1.00 11.21           C  
-ATOM   1206  C   HIS A 159       6.325  22.978   4.929  1.00 11.00           C  
-ATOM   1207  O   HIS A 159       6.798  24.063   4.603  1.00 11.49           O  
-ATOM   1208  CB  HIS A 159       6.686  21.144   3.262  1.00 10.49           C  
-ATOM   1209  CG  HIS A 159       7.217  20.096   4.189  1.00 10.38           C  
-ATOM   1210  ND1 HIS A 159       6.401  19.307   4.971  1.00  9.46           N  
-ATOM   1211  CD2 HIS A 159       8.484  19.699   4.446  1.00 10.17           C  
-ATOM   1212  CE1 HIS A 159       7.145  18.469   5.670  1.00 10.08           C  
-ATOM   1213  NE2 HIS A 159       8.413  18.687   5.370  1.00  9.75           N  
-ATOM   1214  N   ALA A 160       6.384  22.503   6.170  1.00  9.64           N  
-ATOM   1215  CA  ALA A 160       6.998  23.254   7.260  1.00  9.16           C  
-ATOM   1216  C   ALA A 160       8.149  22.487   7.875  1.00  8.85           C  
-ATOM   1217  O   ALA A 160       8.029  21.301   8.205  1.00  7.70           O  
-ATOM   1218  CB  ALA A 160       5.972  23.597   8.307  1.00  8.80           C  
-ATOM   1219  N   VAL A 161       9.279  23.174   8.020  1.00  8.40           N  
-ATOM   1220  CA  VAL A 161      10.502  22.591   8.566  1.00  8.82           C  
-ATOM   1221  C   VAL A 161      11.169  23.523   9.580  1.00  9.03           C  
-ATOM   1222  O   VAL A 161      10.587  24.535   9.971  1.00  9.60           O  
-ATOM   1223  CB  VAL A 161      11.499  22.213   7.429  1.00  8.61           C  
-ATOM   1224  CG1 VAL A 161      11.049  20.973   6.686  1.00  8.90           C  
-ATOM   1225  CG2 VAL A 161      11.585  23.309   6.375  1.00  9.13           C  
-ATOM   1226  N   LEU A 162      12.389  23.186   9.992  1.00  8.88           N  
-ATOM   1227  CA  LEU A 162      13.123  23.986  10.970  1.00  9.26           C  
-ATOM   1228  C   LEU A 162      14.519  24.296  10.494  1.00  9.36           C  
-ATOM   1229  O   LEU A 162      15.267  23.387  10.129  1.00  9.67           O  
-ATOM   1230  CB  LEU A 162      13.230  23.225  12.292  1.00  8.71           C  
-ATOM   1231  CG  LEU A 162      13.056  23.665  13.744  1.00 11.00           C  
-ATOM   1232  CD1 LEU A 162      14.121  23.021  14.609  1.00  8.30           C  
-ATOM   1233  CD2 LEU A 162      13.196  25.156  13.934  1.00  9.93           C  
-ATOM   1234  N   ALA A 163      14.886  25.578  10.528  1.00  9.18           N  
-ATOM   1235  CA  ALA A 163      16.223  26.020  10.136  1.00  9.02           C  
-ATOM   1236  C   ALA A 163      17.050  26.049  11.417  1.00  9.13           C  
-ATOM   1237  O   ALA A 163      16.783  26.847  12.314  1.00  9.91           O  
-ATOM   1238  CB  ALA A 163      16.165  27.401   9.486  1.00  8.33           C  
-ATOM   1239  N   VAL A 164      18.014  25.136  11.517  1.00  9.53           N  
-ATOM   1240  CA  VAL A 164      18.869  25.004  12.705  1.00 10.00           C  
-ATOM   1241  C   VAL A 164      20.279  25.587  12.566  1.00 10.26           C  
-ATOM   1242  O   VAL A 164      21.107  25.462  13.475  1.00 10.91           O  
-ATOM   1243  CB  VAL A 164      18.938  23.521  13.195  1.00  9.98           C  
-ATOM   1244  CG1 VAL A 164      17.547  22.989  13.473  1.00 10.05           C  
-ATOM   1245  CG2 VAL A 164      19.474  22.589  12.116  1.00  9.74           C  
-ATOM   1246  N   GLY A 165      20.541  26.219  11.429  1.00 10.74           N  
-ATOM   1247  CA  GLY A 165      21.838  26.816  11.195  1.00 10.57           C  
-ATOM   1248  C   GLY A 165      22.043  27.176   9.746  1.00 10.69           C  
-ATOM   1249  O   GLY A 165      21.099  27.179   8.955  1.00 10.12           O  
-ATOM   1250  N   TYR A 166      23.280  27.536   9.413  1.00 11.14           N  
-ATOM   1251  CA  TYR A 166      23.663  27.900   8.053  1.00 12.01           C  
-ATOM   1252  C   TYR A 166      25.152  27.787   7.899  1.00 12.98           C  
-ATOM   1253  O   TYR A 166      25.896  28.014   8.854  1.00 12.46           O  
-ATOM   1254  CB  TYR A 166      23.148  29.393   7.654  1.00 12.07           C  
-ATOM   1255  CG  TYR A 166      23.580  30.510   8.589  1.00 11.65           C  
-ATOM   1256  CD1 TYR A 166      24.820  31.167   8.417  1.00 11.52           C  
-ATOM   1257  CD2 TYR A 166      22.770  30.894   9.673  1.00 11.41           C  
-ATOM   1258  CE1 TYR A 166      25.248  32.180   9.323  1.00 11.82           C  
-ATOM   1259  CE2 TYR A 166      23.189  31.915  10.585  1.00 11.51           C  
-ATOM   1260  CZ  TYR A 166      24.428  32.537  10.397  1.00 11.56           C  
-ATOM   1261  OH  TYR A 166      24.861  33.481  11.287  1.00 13.11           O  
-ATOM   1262  N   GLY A 167      25.596  27.457   6.690  1.00 13.82           N  
-ATOM   1263  CA  GLY A 167      27.016  27.324   6.429  1.00 15.44           C  
-ATOM   1264  C   GLY A 167      27.352  27.376   4.957  1.00 17.44           C  
-ATOM   1265  O   GLY A 167      26.599  27.927   4.151  1.00 16.38           O  
-ATOM   1266  N   ILE A 168      28.530  26.850   4.620  1.00 19.53           N  
-ATOM   1267  CA  ILE A 168      29.039  26.800   3.249  1.00 21.47           C  
-ATOM   1268  C   ILE A 168      29.639  25.396   3.000  1.00 22.34           C  
-ATOM   1269  O   ILE A 168      30.517  24.960   3.740  1.00 23.10           O  
-ATOM   1270  CB  ILE A 168      30.146  27.903   2.996  1.00 22.53           C  
-ATOM   1271  CG1 ILE A 168      29.708  29.374   3.293  1.00 23.38           C  
-ATOM   1272  CG2 ILE A 168      30.612  27.871   1.533  1.00 22.05           C  
-ATOM   1273  CD1 ILE A 168      29.950  29.850   4.733  1.00 25.14           C  
-ATOM   1274  N   GLN A1168      29.160  24.710   1.964  1.00 23.13           N  
-ATOM   1275  CA  GLN A1168      29.671  23.383   1.613  1.00 23.84           C  
-ATOM   1276  C   GLN A1168      30.218  23.391   0.181  1.00 24.22           C  
-ATOM   1277  O   GLN A1168      29.451  23.451  -0.785  1.00 24.13           O  
-ATOM   1278  CB  GLN A1168      28.582  22.314   1.764  1.00 24.27           C  
-ATOM   1279  CG  GLN A1168      29.284  20.965   1.694  1.00 25.93           C  
-ATOM   1280  CD  GLN A1168      28.402  19.749   1.827  1.00 26.83           C  
-ATOM   1281  OE1 GLN A1168      27.961  19.401   2.922  1.00 27.85           O  
-ATOM   1282  NE2 GLN A1168      28.148  19.082   0.708  1.00 27.00           N  
-ATOM   1283  N   ALA A2168      31.551  23.345   0.067  1.00 24.81           N  
-ATOM   1284  CA  ALA A2168      32.303  23.343  -1.200  1.00 25.18           C  
-ATOM   1285  C   ALA A2168      31.993  24.548  -2.139  1.00 25.48           C  
-ATOM   1286  O   ALA A2168      31.801  24.381  -3.349  1.00 26.01           O  
-ATOM   1287  CB  ALA A2168      32.126  21.991  -1.939  1.00 25.24           C  
-ATOM   1288  N   GLY A3168      31.924  25.741  -1.546  1.00 25.24           N  
-ATOM   1289  CA  GLY A3168      31.640  26.961  -2.289  1.00 25.06           C  
-ATOM   1290  C   GLY A3168      30.183  27.406  -2.309  1.00 24.79           C  
-ATOM   1291  O   GLY A3168      29.897  28.579  -2.576  1.00 24.91           O  
-ATOM   1292  N   ASN A4168      29.265  26.483  -2.015  1.00 24.09           N  
-ATOM   1293  CA  ASN A4168      27.827  26.776  -2.015  1.00 23.52           C  
-ATOM   1294  C   ASN A4168      27.279  27.049  -0.613  1.00 22.13           C  
-ATOM   1295  O   ASN A4168      27.439  26.228   0.290  1.00 22.03           O  
-ATOM   1296  CB  ASN A4168      27.035  25.601  -2.660  1.00 24.75           C  
-ATOM   1297  CG  ASN A4168      27.532  25.252  -4.065  1.00 25.66           C  
-ATOM   1298  OD1 ASN A4168      28.022  24.145  -4.295  1.00 26.76           O  
-ATOM   1299  ND2 ASN A4168      27.421  26.192  -4.994  1.00 25.51           N  
-ATOM   1300  N   LYS A 169      26.622  28.198  -0.448  1.00 20.84           N  
-ATOM   1301  CA  LYS A 169      26.024  28.603   0.830  1.00 19.30           C  
-ATOM   1302  C   LYS A 169      24.734  27.821   1.079  1.00 18.02           C  
-ATOM   1303  O   LYS A 169      23.957  27.597   0.147  1.00 17.39           O  
-ATOM   1304  CB  LYS A 169      25.735  30.087   0.828  1.00 20.66           C  
-ATOM   1305  CG  LYS A 169      26.979  30.964   0.743  1.00 22.11           C  
-ATOM   1306  CD  LYS A 169      26.599  32.435   0.717  1.00 23.67           C  
-ATOM   1307  CE  LYS A 169      27.826  33.335   0.677  1.00 24.93           C  
-ATOM   1308  NZ  LYS A 169      27.366  34.729   0.385  1.00 26.86           N  
-ATOM   1309  N   HIS A 170      24.512  27.405   2.326  1.00 16.07           N  
-ATOM   1310  CA  HIS A 170      23.324  26.623   2.655  1.00 14.61           C  
-ATOM   1311  C   HIS A 170      22.603  26.965   3.940  1.00 13.56           C  
-ATOM   1312  O   HIS A 170      23.051  27.797   4.729  1.00 13.23           O  
-ATOM   1313  CB  HIS A 170      23.667  25.037   2.638  1.00 14.91           C  
-ATOM   1314  CG  HIS A 170      24.651  24.598   3.687  1.00 15.08           C  
-ATOM   1315  ND1 HIS A 170      25.883  24.066   3.372  1.00 15.93           N  
-ATOM   1316  CD2 HIS A 170      24.570  24.572   5.040  1.00 15.21           C  
-ATOM   1317  CE1 HIS A 170      26.514  23.730   4.482  1.00 15.20           C  
-ATOM   1318  NE2 HIS A 170      25.740  24.028   5.509  1.00 15.74           N  
-ATOM   1319  N   TRP A 171      21.488  26.269   4.152  1.00 12.07           N  
-ATOM   1320  CA  TRP A 171      20.676  26.366   5.364  1.00 11.41           C  
-ATOM   1321  C   TRP A 171      20.614  24.941   5.882  1.00 10.87           C  
-ATOM   1322  O   TRP A 171      20.373  24.023   5.095  1.00 10.99           O  
-ATOM   1323  CB  TRP A 171      19.211  26.816   5.060  1.00 11.10           C  
-ATOM   1324  CG  TRP A 171      19.031  28.224   4.583  1.00 10.70           C  
-ATOM   1325  CD1 TRP A 171      18.684  28.615   3.324  1.00 11.00           C  
-ATOM   1326  CD2 TRP A 171      19.152  29.425   5.357  1.00 10.81           C  
-ATOM   1327  NE1 TRP A 171      18.576  29.983   3.256  1.00 10.09           N  
-ATOM   1328  CE2 TRP A 171      18.860  30.512   4.486  1.00 11.30           C  
-ATOM   1329  CE3 TRP A 171      19.484  29.698   6.704  1.00 11.84           C  
-ATOM   1330  CZ2 TRP A 171      18.891  31.864   4.914  1.00 11.60           C  
-ATOM   1331  CZ3 TRP A 171      19.518  31.056   7.138  1.00 11.74           C  
-ATOM   1332  CH2 TRP A 171      19.222  32.114   6.232  1.00 11.77           C  
-ATOM   1333  N   ILE A 172      20.872  24.737   7.175  1.00  9.79           N  
-ATOM   1334  CA  ILE A 172      20.778  23.395   7.754  1.00  9.07           C  
-ATOM   1335  C   ILE A 172      19.314  23.254   8.137  1.00  8.98           C  
-ATOM   1336  O   ILE A 172      18.803  23.974   9.003  1.00  8.62           O  
-ATOM   1337  CB  ILE A 172      21.752  23.181   8.929  1.00  8.45           C  
-ATOM   1338  CG1 ILE A 172      23.167  23.618   8.543  1.00  8.52           C  
-ATOM   1339  CG2 ILE A 172      21.763  21.703   9.319  1.00  7.98           C  
-ATOM   1340  CD1 ILE A 172      24.133  23.692   9.728  1.00  9.73           C  
-ATOM   1341  N   ILE A 173      18.639  22.334   7.459  1.00  8.55           N  
-ATOM   1342  CA  ILE A 173      17.215  22.116   7.636  1.00  8.69           C  
-ATOM   1343  C   ILE A 173      16.855  20.778   8.257  1.00  8.52           C  
-ATOM   1344  O   ILE A 173      17.188  19.722   7.725  1.00  8.31           O  
-ATOM   1345  CB  ILE A 173      16.505  22.326   6.263  1.00  7.97           C  
-ATOM   1346  CG1 ILE A 173      16.739  23.725   5.668  1.00  8.14           C  
-ATOM   1347  CG2 ILE A 173      15.030  21.964   6.333  1.00  8.26           C  
-ATOM   1348  CD1 ILE A 173      16.151  24.863   6.464  1.00  7.69           C  
-ATOM   1349  N   LYS A 174      16.116  20.841   9.363  1.00  8.66           N  
-ATOM   1350  CA  LYS A 174      15.635  19.664  10.074  1.00  8.75           C  
-ATOM   1351  C   LYS A 174      14.240  19.354   9.577  1.00  9.23           C  
-ATOM   1352  O   LYS A 174      13.350  20.205   9.641  1.00  9.31           O  
-ATOM   1353  CB  LYS A 174      15.596  19.927  11.607  1.00  8.63           C  
-ATOM   1354  CG  LYS A 174      15.289  18.690  12.444  1.00  8.39           C  
-ATOM   1355  CD  LYS A 174      14.907  19.065  13.868  1.00  8.41           C  
-ATOM   1356  CE  LYS A 174      14.760  17.830  14.744  1.00  9.27           C  
-ATOM   1357  NZ  LYS A 174      14.319  18.185  16.128  1.00  8.80           N  
-ATOM   1358  N   ASN A 175      14.059  18.146   9.051  1.00  9.15           N  
-ATOM   1359  CA  ASN A 175      12.763  17.695   8.551  1.00  9.97           C  
-ATOM   1360  C   ASN A 175      12.111  16.796   9.598  1.00  9.75           C  
-ATOM   1361  O   ASN A 175      12.726  16.472  10.613  1.00 10.00           O  
-ATOM   1362  CB  ASN A 175      12.932  16.930   7.217  1.00  9.98           C  
-ATOM   1363  CG  ASN A 175      11.663  16.937   6.363  1.00 10.85           C  
-ATOM   1364  OD1 ASN A 175      10.614  17.497   6.695  1.00 11.17           O  
-ATOM   1365  ND2 ASN A 175      11.793  16.285   5.213  1.00 10.96           N  
-ATOM   1366  N   SER A 176      10.863  16.412   9.348  1.00 10.16           N  
-ATOM   1367  CA  SER A 176      10.109  15.559  10.256  1.00 10.48           C  
-ATOM   1368  C   SER A 176       9.620  14.281   9.557  1.00 11.61           C  
-ATOM   1369  O   SER A 176       8.492  13.826   9.785  1.00 11.31           O  
-ATOM   1370  CB  SER A 176       8.923  16.348  10.853  1.00  9.79           C  
-ATOM   1371  OG  SER A 176       8.160  16.918   9.807  1.00  9.54           O  
-ATOM   1372  N   TRP A 177      10.473  13.719   8.696  1.00 12.51           N  
-ATOM   1373  CA  TRP A 177      10.155  12.499   7.949  1.00 13.19           C  
-ATOM   1374  C   TRP A 177      11.007  11.300   8.381  1.00 13.66           C  
-ATOM   1375  O   TRP A 177      11.189  10.352   7.612  1.00 13.79           O  
-ATOM   1376  CB  TRP A 177      10.308  12.735   6.384  1.00 13.25           C  
-ATOM   1377  CG  TRP A 177       9.303  13.691   5.750  1.00 14.51           C  
-ATOM   1378  CD1 TRP A 177       8.224  14.293   6.350  1.00 14.55           C  
-ATOM   1379  CD2 TRP A 177       9.318  14.167   4.400  1.00 15.00           C  
-ATOM   1380  NE1 TRP A 177       7.577  15.116   5.463  1.00 15.54           N  
-ATOM   1381  CE2 TRP A 177       8.220  15.062   4.256  1.00 15.24           C  
-ATOM   1382  CE3 TRP A 177      10.152  13.928   3.291  1.00 14.73           C  
-ATOM   1383  CZ2 TRP A 177       7.932  15.726   3.039  1.00 15.60           C  
-ATOM   1384  CZ3 TRP A 177       9.869  14.592   2.067  1.00 14.97           C  
-ATOM   1385  CH2 TRP A 177       8.763  15.481   1.961  1.00 14.82           C  
-ATOM   1386  N   GLY A 178      11.524  11.356   9.609  1.00 14.28           N  
-ATOM   1387  CA  GLY A 178      12.345  10.282  10.157  1.00 15.15           C  
-ATOM   1388  C   GLY A 178      13.811  10.341   9.778  1.00 16.37           C  
-ATOM   1389  O   GLY A 178      14.211  11.160   8.949  1.00 15.36           O  
-ATOM   1390  N   GLU A 179      14.605   9.444  10.364  1.00 18.22           N  
-ATOM   1391  CA  GLU A 179      16.045   9.358  10.115  1.00 20.60           C  
-ATOM   1392  C   GLU A 179      16.431   8.631   8.827  1.00 21.14           C  
-ATOM   1393  O   GLU A 179      17.564   8.760   8.363  1.00 21.87           O  
-ATOM   1394  CB  GLU A 179      16.751   8.699  11.284  1.00 22.17           C  
-ATOM   1395  CG  GLU A 179      16.616   9.523  12.546  1.00 24.99           C  
-ATOM   1396  CD  GLU A 179      17.561   9.061  13.636  1.00 26.52           C  
-ATOM   1397  OE1 GLU A 179      18.754   8.860  13.361  1.00 27.31           O  
-ATOM   1398  OE2 GLU A 179      17.079   8.920  14.756  1.00 27.88           O  
-ATOM   1399  N   SER A 180      15.497   7.864   8.263  1.00 21.60           N  
-ATOM   1400  CA  SER A 180      15.727   7.116   7.023  1.00 21.75           C  
-ATOM   1401  C   SER A 180      15.717   8.031   5.800  1.00 21.28           C  
-ATOM   1402  O   SER A 180      16.243   7.679   4.741  1.00 21.59           O  
-ATOM   1403  CB  SER A 180      14.677   6.032   6.853  1.00 23.10           C  
-ATOM   1404  OG  SER A 180      14.812   5.029   7.865  1.00 25.89           O  
-ATOM   1405  N   TRP A 181      15.121   9.211   5.960  1.00 19.86           N  
-ATOM   1406  CA  TRP A 181      15.041  10.192   4.890  1.00 18.43           C  
-ATOM   1407  C   TRP A 181      16.270  11.118   4.899  1.00 18.42           C  
-ATOM   1408  O   TRP A 181      16.780  11.478   5.963  1.00 17.86           O  
-ATOM   1409  CB  TRP A 181      13.709  11.045   5.023  1.00 17.65           C  
-ATOM   1410  CG  TRP A 181      13.541  12.051   3.932  1.00 16.05           C  
-ATOM   1411  CD1 TRP A 181      13.063  11.821   2.675  1.00 15.88           C  
-ATOM   1412  CD2 TRP A 181      13.976  13.415   3.953  1.00 15.45           C  
-ATOM   1413  NE1 TRP A 181      13.190  12.950   1.902  1.00 14.87           N  
-ATOM   1414  CE2 TRP A 181      13.748  13.944   2.656  1.00 15.25           C  
-ATOM   1415  CE3 TRP A 181      14.554  14.243   4.940  1.00 14.94           C  
-ATOM   1416  CZ2 TRP A 181      14.075  15.269   2.312  1.00 15.21           C  
-ATOM   1417  CZ3 TRP A 181      14.885  15.571   4.598  1.00 14.64           C  
-ATOM   1418  CH2 TRP A 181      14.638  16.064   3.288  1.00 15.17           C  
-ATOM   1419  N   GLY A 182      16.678  11.548   3.699  1.00 18.24           N  
-ATOM   1420  CA  GLY A 182      17.803  12.457   3.508  1.00 18.58           C  
-ATOM   1421  C   GLY A 182      19.122  12.047   4.126  1.00 18.89           C  
-ATOM   1422  O   GLY A 182      19.528  10.885   4.036  1.00 19.20           O  
-ATOM   1423  N   ASN A 183      19.793  13.012   4.750  1.00 18.87           N  
-ATOM   1424  CA  ASN A 183      21.062  12.776   5.425  1.00 19.25           C  
-ATOM   1425  C   ASN A 183      20.745  12.743   6.922  1.00 19.21           C  
-ATOM   1426  O   ASN A 183      20.860  13.760   7.618  1.00 19.37           O  
-ATOM   1427  CB  ASN A 183      22.079  13.898   5.100  1.00 20.06           C  
-ATOM   1428  CG  ASN A 183      23.518  13.541   5.531  1.00 21.94           C  
-ATOM   1429  OD1 ASN A 183      23.784  12.539   6.202  1.00 22.94           O  
-ATOM   1430  ND2 ASN A 183      24.450  14.395   5.126  1.00 22.53           N  
-ATOM   1431  N   ALA A 184      20.333  11.562   7.399  1.00 18.22           N  
-ATOM   1432  CA  ALA A 184      19.948  11.305   8.796  1.00 17.71           C  
-ATOM   1433  C   ALA A 184      18.780  12.236   9.283  1.00 16.92           C  
-ATOM   1434  O   ALA A 184      18.744  12.670  10.440  1.00 17.40           O  
-ATOM   1435  CB  ALA A 184      21.175  11.383   9.745  1.00 17.85           C  
-ATOM   1436  N   GLY A 185      17.862  12.532   8.358  1.00 15.78           N  
-ATOM   1437  CA  GLY A 185      16.709  13.376   8.644  1.00 14.61           C  
-ATOM   1438  C   GLY A 185      16.878  14.838   8.281  1.00 14.19           C  
-ATOM   1439  O   GLY A 185      15.911  15.609   8.315  1.00 13.65           O  
-ATOM   1440  N   TYR A 186      18.098  15.206   7.889  1.00 13.74           N  
-ATOM   1441  CA  TYR A 186      18.454  16.575   7.528  1.00 13.27           C  
-ATOM   1442  C   TYR A 186      18.662  16.817   6.046  1.00 13.55           C  
-ATOM   1443  O   TYR A 186      18.934  15.889   5.275  1.00 13.18           O  
-ATOM   1444  CB  TYR A 186      19.713  16.997   8.269  1.00 13.40           C  
-ATOM   1445  CG  TYR A 186      19.512  17.211   9.750  1.00 13.07           C  
-ATOM   1446  CD1 TYR A 186      19.195  18.486  10.255  1.00 12.39           C  
-ATOM   1447  CD2 TYR A 186      19.609  16.137  10.660  1.00 12.60           C  
-ATOM   1448  CE1 TYR A 186      18.963  18.695  11.650  1.00 12.49           C  
-ATOM   1449  CE2 TYR A 186      19.385  16.338  12.064  1.00 12.80           C  
-ATOM   1450  CZ  TYR A 186      19.060  17.618  12.534  1.00 12.89           C  
-ATOM   1451  OH  TYR A 186      18.829  17.823  13.872  1.00 14.30           O  
-ATOM   1452  N   ILE A 187      18.562  18.090   5.663  1.00 13.02           N  
-ATOM   1453  CA  ILE A 187      18.740  18.546   4.288  1.00 13.33           C  
-ATOM   1454  C   ILE A 187      19.441  19.926   4.293  1.00 12.65           C  
-ATOM   1455  O   ILE A 187      19.185  20.755   5.164  1.00 12.10           O  
-ATOM   1456  CB  ILE A 187      17.372  18.430   3.495  1.00 14.28           C  
-ATOM   1457  CG1 ILE A 187      17.331  18.403   1.948  1.00 15.55           C  
-ATOM   1458  CG2 ILE A 187      16.353  19.412   4.012  1.00 13.88           C  
-ATOM   1459  CD1 ILE A 187      17.664  19.651   1.242  1.00 16.97           C  
-ATOM   1460  N   LEU A 188      20.407  20.096   3.393  1.00 11.99           N  
-ATOM   1461  CA  LEU A 188      21.116  21.364   3.248  1.00 12.01           C  
-ATOM   1462  C   LEU A 188      20.510  22.027   2.030  1.00 12.21           C  
-ATOM   1463  O   LEU A 188      20.612  21.499   0.923  1.00 12.69           O  
-ATOM   1464  CB  LEU A 188      22.639  21.140   3.056  1.00 12.23           C  
-ATOM   1465  CG  LEU A 188      23.415  20.308   4.132  1.00 12.35           C  
-ATOM   1466  CD1 LEU A 188      24.863  20.156   3.716  1.00 12.83           C  
-ATOM   1467  CD2 LEU A 188      23.315  20.959   5.506  1.00 12.69           C  
-ATOM   1468  N   MET A 189      19.785  23.121   2.252  1.00 12.13           N  
-ATOM   1469  CA  MET A 189      19.116  23.857   1.176  1.00 13.34           C  
-ATOM   1470  C   MET A 189      19.868  25.106   0.785  1.00 13.79           C  
-ATOM   1471  O   MET A 189      20.400  25.801   1.645  1.00 13.84           O  
-ATOM   1472  CB  MET A 189      17.686  24.224   1.585  1.00 12.83           C  
-ATOM   1473  CG  MET A 189      16.940  22.920   1.828  1.00 13.94           C  
-ATOM   1474  SD  MET A 189      15.184  23.126   2.153  1.00 14.79           S  
-ATOM   1475  CE  MET A 189      14.592  23.468   0.484  1.00 14.82           C  
-ATOM   1476  N   ALA A 190      19.842  25.432  -0.509  1.00 14.04           N  
-ATOM   1477  CA  ALA A 190      20.527  26.598  -1.078  1.00 14.23           C  
-ATOM   1478  C   ALA A 190      20.208  27.946  -0.412  1.00 14.29           C  
-ATOM   1479  O   ALA A 190      19.041  28.298  -0.212  1.00 13.96           O  
-ATOM   1480  CB  ALA A 190      20.256  26.676  -2.583  1.00 13.97           C  
-ATOM   1481  N   ARG A 191      21.264  28.645   0.001  1.00 14.26           N  
-ATOM   1482  CA  ARG A 191      21.148  29.958   0.634  1.00 14.86           C  
-ATOM   1483  C   ARG A 191      21.687  31.025  -0.281  1.00 15.39           C  
-ATOM   1484  O   ARG A 191      22.774  30.890  -0.852  1.00 14.91           O  
-ATOM   1485  CB  ARG A 191      21.888  29.995   2.009  1.00 14.28           C  
-ATOM   1486  CG  ARG A 191      21.907  31.321   2.772  1.00 13.66           C  
-ATOM   1487  CD  ARG A 191      22.348  31.151   4.224  1.00 12.96           C  
-ATOM   1488  NE  ARG A 191      23.705  30.626   4.363  1.00 12.72           N  
-ATOM   1489  CZ  ARG A 191      24.786  31.382   4.541  1.00 13.31           C  
-ATOM   1490  NH1 ARG A 191      25.982  30.812   4.664  1.00 12.50           N  
-ATOM   1491  NH2 ARG A 191      24.675  32.706   4.588  1.00 12.42           N  
-ATOM   1492  N   ASN A 192      20.922  32.109  -0.399  1.00 16.58           N  
-ATOM   1493  CA  ASN A 192      21.236  33.265  -1.240  1.00 18.60           C  
-ATOM   1494  C   ASN A 192      21.174  32.983  -2.755  1.00 19.14           C  
-ATOM   1495  O   ASN A 192      21.894  33.600  -3.541  1.00 20.20           O  
-ATOM   1496  CB  ASN A 192      22.609  33.946  -0.814  1.00 18.56           C  
-ATOM   1497  CG  ASN A 192      22.565  34.530   0.618  1.00 19.84           C  
-ATOM   1498  OD1 ASN A 192      21.508  34.715   1.224  1.00 20.24           O  
-ATOM   1499  ND2 ASN A 192      23.747  34.801   1.154  1.00 20.17           N  
-ATOM   1500  N   LYS A 193      20.326  32.025  -3.136  1.00 19.55           N  
-ATOM   1501  CA  LYS A 193      20.102  31.672  -4.537  1.00 19.87           C  
-ATOM   1502  C   LYS A 193      18.667  32.044  -4.896  1.00 19.56           C  
-ATOM   1503  O   LYS A 193      17.859  31.186  -5.262  1.00 19.41           O  
-ATOM   1504  CB  LYS A 193      20.342  30.164  -4.815  1.00 21.12           C  
-ATOM   1505  CG  LYS A 193      21.660  29.467  -5.100  1.00 22.73           C  
-ATOM   1506  CD  LYS A 193      22.452  29.236  -3.825  1.00 24.30           C  
-ATOM   1507  CE  LYS A 193      23.562  28.208  -4.043  1.00 25.31           C  
-ATOM   1508  NZ  LYS A 193      24.087  27.663  -2.755  1.00 24.39           N  
-ATOM   1509  N   ASN A 194      18.347  33.328  -4.719  1.00 19.21           N  
-ATOM   1510  CA  ASN A 194      17.034  33.917  -5.021  1.00 19.87           C  
-ATOM   1511  C   ASN A 194      15.822  33.352  -4.254  1.00 19.19           C  
-ATOM   1512  O   ASN A 194      14.744  33.170  -4.832  1.00 18.99           O  
-ATOM   1513  CB  ASN A 194      16.763  33.878  -6.554  1.00 21.59           C  
-ATOM   1514  CG  ASN A 194      17.802  34.659  -7.355  1.00 23.69           C  
-ATOM   1515  OD1 ASN A 194      18.636  34.057  -8.042  1.00 25.50           O  
-ATOM   1516  ND2 ASN A 194      17.769  35.987  -7.263  1.00 24.21           N  
-ATOM   1517  N   ASN A 198      16.012  33.086  -2.958  1.00 18.68           N  
-ATOM   1518  CA  ASN A 198      14.969  32.549  -2.071  1.00 17.83           C  
-ATOM   1519  C   ASN A 198      14.433  31.182  -2.576  1.00 16.90           C  
-ATOM   1520  O   ASN A 198      13.221  30.994  -2.732  1.00 16.50           O  
-ATOM   1521  CB  ASN A 198      13.790  33.617  -1.911  1.00 18.94           C  
-ATOM   1522  CG  ASN A 198      12.856  33.310  -0.739  1.00 19.59           C  
-ATOM   1523  OD1 ASN A 198      13.171  32.602   0.218  1.00 19.91           O  
-ATOM   1524  ND2 ASN A 198      11.657  33.870  -0.853  1.00 19.83           N  
-ATOM   1525  N   ALA A 199      15.360  30.258  -2.848  1.00 16.19           N  
-ATOM   1526  CA  ALA A 199      15.056  28.911  -3.355  1.00 15.21           C  
-ATOM   1527  C   ALA A 199      14.054  28.151  -2.502  1.00 14.92           C  
-ATOM   1528  O   ALA A 199      14.222  28.019  -1.286  1.00 14.38           O  
-ATOM   1529  CB  ALA A 199      16.340  28.097  -3.510  1.00 14.96           C  
-ATOM   1530  N   CYS A 200      12.974  27.709  -3.148  1.00 14.74           N  
-ATOM   1531  CA  CYS A 200      11.875  26.972  -2.518  1.00 14.52           C  
-ATOM   1532  C   CYS A 200      11.050  27.819  -1.514  1.00 14.12           C  
-ATOM   1533  O   CYS A 200      10.279  27.274  -0.733  1.00 14.28           O  
-ATOM   1534  CB  CYS A 200      12.385  25.670  -1.852  1.00 15.40           C  
-ATOM   1535  SG  CYS A 200      13.175  24.471  -2.983  1.00 16.54           S  
-ATOM   1536  N   GLY A 201      11.226  29.143  -1.564  1.00 13.90           N  
-ATOM   1537  CA  GLY A 201      10.514  30.073  -0.693  1.00 13.67           C  
-ATOM   1538  C   GLY A 201      10.860  29.982   0.782  1.00 14.07           C  
-ATOM   1539  O   GLY A 201      10.017  30.269   1.639  1.00 14.05           O  
-ATOM   1540  N   ILE A 202      12.122  29.656   1.070  1.00 13.19           N  
-ATOM   1541  CA  ILE A 202      12.633  29.485   2.430  1.00 13.09           C  
-ATOM   1542  C   ILE A 202      12.449  30.683   3.404  1.00 12.95           C  
-ATOM   1543  O   ILE A 202      12.280  30.476   4.606  1.00 12.66           O  
-ATOM   1544  CB  ILE A 202      14.101  28.942   2.397  1.00 13.11           C  
-ATOM   1545  CG1 ILE A 202      14.462  28.411   3.785  1.00 13.07           C  
-ATOM   1546  CG2 ILE A 202      15.091  30.027   1.921  1.00 12.55           C  
-ATOM   1547  CD1 ILE A 202      15.315  27.180   3.753  1.00 14.21           C  
-ATOM   1548  N   ALA A 203      12.444  31.904   2.868  1.00 12.91           N  
-ATOM   1549  CA  ALA A 203      12.281  33.106   3.686  1.00 13.07           C  
-ATOM   1550  C   ALA A 203      10.915  33.793   3.517  1.00 12.94           C  
-ATOM   1551  O   ALA A 203      10.721  34.930   3.966  1.00 12.91           O  
-ATOM   1552  CB  ALA A 203      13.407  34.080   3.396  1.00 13.64           C  
-ATOM   1553  N   ASN A 204       9.963  33.079   2.922  1.00 13.17           N  
-ATOM   1554  CA  ASN A 204       8.625  33.620   2.691  1.00 13.85           C  
-ATOM   1555  C   ASN A 204       7.657  33.559   3.849  1.00 14.07           C  
-ATOM   1556  O   ASN A 204       6.779  34.420   3.961  1.00 14.25           O  
-ATOM   1557  CB  ASN A 204       8.008  33.005   1.456  1.00 14.35           C  
-ATOM   1558  CG  ASN A 204       8.397  33.754   0.166  1.00 15.34           C  
-ATOM   1559  OD1 ASN A 204       9.086  34.774   0.189  1.00 16.95           O  
-ATOM   1560  ND2 ASN A 204       7.926  33.240  -0.962  1.00 15.82           N  
-ATOM   1561  N   LEU A 205       7.834  32.580   4.737  1.00 13.52           N  
-ATOM   1562  CA  LEU A 205       6.947  32.427   5.892  1.00 13.44           C  
-ATOM   1563  C   LEU A 205       7.693  31.882   7.098  1.00 12.92           C  
-ATOM   1564  O   LEU A 205       7.387  30.803   7.615  1.00 12.11           O  
-ATOM   1565  CB  LEU A 205       5.750  31.519   5.521  1.00 14.15           C  
-ATOM   1566  CG  LEU A 205       4.386  31.653   6.222  1.00 14.89           C  
-ATOM   1567  CD1 LEU A 205       3.794  33.038   5.979  1.00 15.17           C  
-ATOM   1568  CD2 LEU A 205       3.440  30.591   5.690  1.00 15.05           C  
-ATOM   1569  N   ALA A 206       8.680  32.651   7.547  1.00 12.05           N  
-ATOM   1570  CA  ALA A 206       9.502  32.273   8.686  1.00 11.72           C  
-ATOM   1571  C   ALA A 206       9.086  32.982   9.950  1.00 11.61           C  
-ATOM   1572  O   ALA A 206       8.722  34.161   9.922  1.00 11.06           O  
-ATOM   1573  CB  ALA A 206      10.978  32.535   8.380  1.00 11.26           C  
-ATOM   1574  N   SER A 207       9.128  32.255  11.067  1.00 11.58           N  
-ATOM   1575  CA  SER A 207       8.761  32.804  12.371  1.00 11.76           C  
-ATOM   1576  C   SER A 207       9.418  32.076  13.533  1.00 12.32           C  
-ATOM   1577  O   SER A 207       9.845  30.921  13.407  1.00 11.99           O  
-ATOM   1578  CB  SER A 207       7.210  32.796  12.562  1.00 11.62           C  
-ATOM   1579  OG  SER A 207       6.597  31.509  12.484  1.00 12.16           O  
-ATOM   1580  N   PHE A 208       9.518  32.770  14.663  1.00 12.46           N  
-ATOM   1581  CA  PHE A 208      10.092  32.197  15.875  1.00 13.31           C  
-ATOM   1582  C   PHE A 208       9.275  32.640  17.099  1.00 13.97           C  
-ATOM   1583  O   PHE A 208       8.755  33.763  17.112  1.00 13.06           O  
-ATOM   1584  CB  PHE A 208      11.659  32.560  16.039  1.00 13.73           C  
-ATOM   1585  CG  PHE A 208      11.960  34.036  16.167  1.00 14.98           C  
-ATOM   1586  CD1 PHE A 208      11.937  34.675  17.428  1.00 15.18           C  
-ATOM   1587  CD2 PHE A 208      12.283  34.789  15.032  1.00 15.51           C  
-ATOM   1588  CE1 PHE A 208      12.236  36.066  17.563  1.00 15.32           C  
-ATOM   1589  CE2 PHE A 208      12.590  36.187  15.131  1.00 15.30           C  
-ATOM   1590  CZ  PHE A 208      12.566  36.830  16.405  1.00 16.06           C  
-ATOM   1591  N   PRO A 209       9.138  31.802  18.159  1.00 14.25           N  
-ATOM   1592  CA  PRO A 209       8.374  32.181  19.346  1.00 15.85           C  
-ATOM   1593  C   PRO A 209       9.165  33.076  20.312  1.00 17.46           C  
-ATOM   1594  O   PRO A 209      10.400  33.092  20.293  1.00 17.78           O  
-ATOM   1595  CB  PRO A 209       8.040  30.853  19.959  1.00 15.48           C  
-ATOM   1596  CG  PRO A 209       9.286  30.036  19.685  1.00 15.28           C  
-ATOM   1597  CD  PRO A 209       9.654  30.423  18.279  1.00 14.63           C  
-ATOM   1598  N   LYS A 210       8.439  33.856  21.104  1.00 19.41           N  
-ATOM   1599  CA  LYS A 210       9.032  34.742  22.101  1.00 21.84           C  
-ATOM   1600  C   LYS A 210       8.748  34.120  23.448  1.00 23.00           C  
-ATOM   1601  O   LYS A 210       7.650  33.606  23.661  1.00 22.90           O  
-ATOM   1602  CB  LYS A 210       8.389  36.136  22.027  1.00 22.77           C  
-ATOM   1603  CG  LYS A 210       8.432  36.808  20.663  1.00 24.62           C  
-ATOM   1604  CD  LYS A 210       9.863  36.983  20.180  1.00 26.73           C  
-ATOM   1605  CE  LYS A 210      10.590  38.097  20.915  1.00 27.98           C  
-ATOM   1606  NZ  LYS A 210      10.184  39.405  20.330  1.00 29.82           N  
-ATOM   1607  N   MET A 211       9.738  34.111  24.339  1.00 24.29           N  
-ATOM   1608  CA  MET A 211       9.546  33.536  25.669  1.00 26.08           C  
-ATOM   1609  C   MET A 211       9.593  34.558  26.799  1.00 26.56           C  
-ATOM   1610  O   MET A 211      10.070  35.666  26.577  1.00 27.32           O  
-ATOM   1611  CB  MET A 211      10.549  32.379  25.936  1.00 27.32           C  
-ATOM   1612  CG  MET A 211      10.175  31.122  25.155  1.00 28.03           C  
-ATOM   1613  SD  MET A 211      10.699  29.612  25.988  1.00 30.09           S  
-ATOM   1614  CE  MET A 211       9.885  28.381  24.988  1.00 29.09           C  
-ATOM   1615  OXT MET A 211       9.119  34.222  27.869  1.00 27.06           O  
-TER    1616      MET A 211                                                      
-HETATM 1617  C46 NFT A 283      -6.190  24.694   7.222  1.00 12.29           C  
-HETATM 1618  C08 NFT A 283      -3.965  25.609   6.583  1.00 12.36           C  
-HETATM 1619  C09 NFT A 283      -4.935  24.568   6.552  1.00 12.57           C  
-HETATM 1620  C10 NFT A 283      -4.577  23.367   5.832  1.00 12.42           C  
-HETATM 1621  C11 NFT A 283      -3.328  23.274   5.214  1.00 12.87           C  
-HETATM 1622  C07 NFT A 283      -2.692  25.499   5.958  1.00 12.95           C  
-HETATM 1623  C06 NFT A 283      -2.376  24.338   5.279  1.00 12.87           C  
-HETATM 1624  C15 NFT A 283      -1.018  24.238   4.640  1.00 13.74           C  
-HETATM 1625  C16 NFT A 283      -0.986  24.919   3.215  1.00 14.46           C  
-HETATM 1626  F35 NFT A 283      -2.039  24.558   2.442  1.00 14.88           F  
-HETATM 1627  F36 NFT A 283      -1.005  26.276   3.287  1.00 15.80           F  
-HETATM 1628  F37 NFT A 283       0.124  24.593   2.500  1.00 15.30           F  
-HETATM 1629  N26 NFT A 283       1.645  21.274   5.306  1.00 12.11           N  
-HETATM 1630  C41 NFT A 283       1.566  19.865   5.675  1.00 10.66           C  
-HETATM 1631  N24 NFT A 283       0.027  24.446   5.449  1.00 13.18           N  
-HETATM 1632  C17 NFT A 283       1.248  23.628   5.439  1.00 13.44           C  
-HETATM 1633  C18 NFT A 283       2.360  24.324   6.156  1.00 13.26           C  
-HETATM 1634  C19 NFT A 283       3.198  25.511   5.640  1.00 14.02           C  
-HETATM 1635  C20 NFT A 283       2.686  26.142   4.352  1.00 14.32           C  
-HETATM 1636  C21 NFT A 283       3.244  26.542   6.729  1.00 14.21           C  
-HETATM 1637  C22 NFT A 283       1.067  22.253   5.986  1.00 12.02           C  
-HETATM 1638  O23 NFT A 283       0.422  22.065   7.006  1.00 12.78           O  
-HETATM 1639  C47 NFT A 283      -7.395  24.225   6.614  1.00 12.55           C  
-HETATM 1640  C48 NFT A 283      -8.608  24.317   7.277  1.00 12.74           C  
-HETATM 1641  C50 NFT A 283      -8.654  24.874   8.569  1.00 13.14           C  
-HETATM 1642  C51 NFT A 283      -7.492  25.349   9.191  1.00 13.77           C  
-HETATM 1643  C52 NFT A 283      -6.270  25.261   8.531  1.00 12.89           C  
-HETATM 1644  S60 NFT A 283     -10.126  24.779   9.476  1.00 13.93           S  
-HETATM 1645  N63 NFT A 283      -9.805  23.545  10.596  1.00 13.33           N  
-HETATM 1646  O61 NFT A 283     -10.339  26.018  10.140  1.00 14.66           O  
-HETATM 1647  O62 NFT A 283     -11.178  24.356   8.575  1.00 14.42           O  
-HETATM 1648  C44 NFT A 283       2.699  19.401   6.542  1.00 11.20           C  
-HETATM 1649  N45 NFT A 283       2.820  18.145   6.806  1.00 10.20           N  
-HETATM 1650  O   HOH A4169      11.020  20.120  11.815  1.00 11.70           O  
-HETATM 1651  O   HOH A4170      -4.917  21.641  14.771  1.00  7.41           O  
-HETATM 1652  O   HOH A4171       3.046  29.885   9.863  1.00  8.58           O  
-HETATM 1653  O   HOH A4172      15.367  23.115  18.127  1.00  8.26           O  
-HETATM 1654  O   HOH A4173      -1.963  11.226  22.800  1.00  8.18           O  
-HETATM 1655  O   HOH A4174       1.367  32.093   9.156  1.00 19.64           O  
-HETATM 1656  O   HOH A4175       9.508  30.299   4.677  1.00  9.62           O  
-HETATM 1657  O   HOH A4176      16.475  26.789  -0.169  1.00 11.58           O  
-HETATM 1658  O   HOH A4177       3.151  14.637  20.783  1.00  5.12           O  
-HETATM 1659  O   HOH A4178      12.073  16.136  13.338  1.00 12.08           O  
-HETATM 1660  O   HOH A4179      15.883  25.018  -5.052  1.00 16.93           O  
-HETATM 1661  O   HOH A4180       8.939  19.517  10.192  1.00 18.78           O  
-HETATM 1662  O   HOH A4181      -2.277  11.583  25.445  1.00 16.75           O  
-HETATM 1663  O   HOH A4182      13.404  13.899   8.481  1.00  9.17           O  
-HETATM 1664  O   HOH A4183      14.522  28.178  18.681  1.00  8.39           O  
-HETATM 1665  O   HOH A4184      16.684  24.989  -2.274  1.00 20.79           O  
-HETATM 1666  O   HOH A4185      18.303  30.562  -1.535  1.00  7.24           O  
-HETATM 1667  O   HOH A4186       5.742  31.133   9.905  1.00 13.74           O  
-HETATM 1668  O   HOH A4187      10.510  17.401  18.560  1.00 21.22           O  
-HETATM 1669  O   HOH A4188     -10.621  11.554  20.315  1.00 12.17           O  
-HETATM 1670  O   HOH A4189      -5.666  23.513  25.627  1.00 16.90           O  
-HETATM 1671  O   HOH A4190      14.543  20.415  17.886  1.00  9.85           O  
-HETATM 1672  O   HOH A4191     -10.741  18.971  20.716  1.00 31.41           O  
-HETATM 1673  O   HOH A4192       5.333  33.696   9.294  1.00 25.48           O  
-HETATM 1674  O   HOH A4193       9.479  35.121   6.493  1.00 14.48           O  
-HETATM 1675  O   HOH A4194      21.329  19.455  19.544  1.00 12.12           O  
-HETATM 1676  O   HOH A4195      21.853  34.497   4.109  1.00 18.90           O  
-HETATM 1677  O   HOH A4196      23.198  15.848   8.518  1.00 29.50           O  
-HETATM 1678  O   HOH A4197       1.540  15.969   4.737  1.00 35.78           O  
-HETATM 1679  O   HOH A4198      12.498  28.745  -5.966  1.00 16.72           O  
-HETATM 1680  O   HOH A4199       6.503  40.899  -3.815  1.00 26.40           O  
-HETATM 1681  O   HOH A4200      -2.681   8.712  22.659  1.00 19.73           O  
-HETATM 1682  O   HOH A4201      -7.177  11.386  11.704  1.00 42.13           O  
-HETATM 1683  O   HOH A4202       7.366  13.583  18.930  1.00 21.47           O  
-HETATM 1684  O   HOH A4203      12.873  34.258  21.317  1.00 27.90           O  
-HETATM 1685  O   HOH A4204      15.674  10.907   0.886  1.00 15.31           O  
-HETATM 1686  O   HOH A4205      -6.828  27.190  19.609  1.00 22.75           O  
-HETATM 1687  O   HOH A4206       1.611  32.366  27.743  1.00 16.61           O  
-HETATM 1688  O   HOH A4207       2.590  13.338   6.005  1.00 31.91           O  
-HETATM 1689  O   HOH A4208      -3.490  13.002   7.048  1.00 45.95           O  
-HETATM 1690  O   HOH A4209      14.396  31.048  -6.618  1.00 45.09           O  
-HETATM 1691  O   HOH A4210      -9.766  18.148   7.862  1.00 32.71           O  
-HETATM 1692  O   HOH A4211      -2.515  14.282  27.466  1.00 33.38           O  
-HETATM 1693  O   HOH A4212      19.052   9.178   2.024  1.00 31.46           O  
-HETATM 1694  O   HOH A4213      -2.799  12.102  33.127  1.00 29.39           O  
-HETATM 1695  O   HOH A4214       6.448  16.625  31.647  1.00 41.56           O  
-HETATM 1696  O   HOH A4215      24.345  31.319  19.249  1.00 38.28           O  
-HETATM 1697  O   HOH A4216      10.745  20.681  -3.645  1.00 11.31           O  
-HETATM 1698  O   HOH A4217      18.797  14.001  22.869  1.00 36.13           O  
-HETATM 1699  O   HOH A4218      -9.405  17.876  17.762  1.00 23.65           O  
-HETATM 1700  O   HOH A4219       8.489  15.586  19.958  1.00 22.15           O  
-HETATM 1701  O   HOH A4220      -6.676  33.822  25.810  1.00 42.65           O  
-HETATM 1702  O   HOH A4221       5.514  16.582  -0.431  1.00 46.17           O  
-HETATM 1703  O   HOH A4222       8.801   9.719   3.296  1.00 49.76           O  
-HETATM 1704  O   HOH A4223      15.967  35.069  28.076  1.00 45.52           O  
-HETATM 1705  O   HOH A4224       8.768  28.381  28.821  1.00 43.39           O  
-HETATM 1706  O   HOH A4225      25.667  19.103   8.012  1.00 32.43           O  
-HETATM 1707  O   HOH A4226      -6.603  26.996  25.299  1.00 43.07           O  
-HETATM 1708  O   HOH A4227      28.046  21.203  -2.509  1.00 47.30           O  
-HETATM 1709  O   HOH A4228      17.138  37.860   0.401  1.00 32.05           O  
-HETATM 1710  O   HOH A4229       6.891  40.944   5.866  1.00 35.59           O  
-HETATM 1711  O   HOH A4230      28.365  15.291   1.748  1.00 49.61           O  
-HETATM 1712  O   HOH A4231      24.194  23.159  -5.517  1.00 49.74           O  
-HETATM 1713  O   HOH A4232      26.230  16.770   2.482  1.00 48.17           O  
-HETATM 1714  O   HOH A4233       4.083  15.747  -2.587  1.00 46.98           O  
-HETATM 1715  O   HOH A4234     -11.380  12.422  15.020  1.00 33.33           O  
-HETATM 1716  O   HOH A4235      -8.681  31.451  25.238  1.00 48.82           O  
-HETATM 1717  O   HOH A4236      19.649  35.776  -3.361  1.00 37.47           O  
-HETATM 1718  O   HOH A4237       6.672  10.654   7.117  1.00 44.18           O  
-HETATM 1719  O   HOH A4238      14.761  27.269  -6.712  1.00 36.43           O  
-HETATM 1720  O   HOH A4239     -11.620  17.169  25.162  1.00 43.98           O  
-HETATM 1721  O   HOH A4240      -8.145  16.915  10.265  1.00 19.18           O  
-HETATM 1722  O   HOH A4241     -15.577  14.625  12.173  1.00 43.61           O  
-HETATM 1723  O   HOH A4242      20.975  40.812   0.252  1.00 47.45           O  
-HETATM 1724  O   HOH A4243      22.553  34.351  -6.857  1.00 38.78           O  
-HETATM 1725  O   HOH A4244      -8.473  19.853  27.089  1.00 43.31           O  
-HETATM 1726  O   HOH A4245      19.288  12.267  -4.836  1.00 37.82           O  
-HETATM 1727  O   HOH A4246      26.427  18.508  13.951  1.00 30.42           O  
-HETATM 1728  O   HOH A4247      14.152  40.729  -0.047  1.00 54.33           O  
-HETATM 1729  O   HOH A4248      15.328  39.261  15.270  1.00 50.00           O  
-HETATM 1730  O   HOH A4249       1.544  11.150   3.128  1.00 24.61           O  
-HETATM 1731  O   HOH A4250       9.323  14.809  26.827  1.00 28.75           O  
-HETATM 1732  O   HOH A4251      -4.319  29.887  17.435  1.00 22.09           O  
-HETATM 1733  O   HOH A4252     -11.544  21.412   7.741  1.00 30.17           O  
-HETATM 1734  O   HOH A4253     -10.180  20.367  11.820  1.00 21.77           O  
-HETATM 1735  O   HOH A4254       4.665  15.397   4.635  1.00 31.02           O  
-HETATM 1736  O   HOH A4255      14.195  22.125  24.849  1.00 18.18           O  
-HETATM 1737  O   HOH A4256       8.415  43.610  -5.493  1.00 25.31           O  
-HETATM 1738  O   HOH A4257      -9.370   9.066  21.528  1.00 48.06           O  
-HETATM 1739  O   HOH A4258      18.117  12.462  15.081  1.00 24.50           O  
-HETATM 1740  O   HOH A4259      -9.845  21.509   5.400  1.00 27.32           O  
-HETATM 1741  O   HOH A4260       0.284  21.160   2.130  1.00 35.65           O  
-HETATM 1742  O   HOH A4261       1.590  18.631   1.783  1.00 49.10           O  
-HETATM 1743  O   HOH A4262      -9.144  23.370  21.831  1.00 38.97           O  
-HETATM 1744  O   HOH A4263      14.532  35.307  25.791  1.00 49.78           O  
-HETATM 1745  O   HOH A4264      26.717  30.069  -2.538  1.00 28.39           O  
-HETATM 1746  O   HOH A4265      17.475  35.633  -1.570  1.00 35.32           O  
-HETATM 1747  O   HOH A4266      18.663  16.054  15.698  1.00 26.99           O  
-HETATM 1748  O   HOH A4267      12.427  14.609  26.672  1.00 36.79           O  
-HETATM 1749  O   HOH A4268      -1.629  25.778  31.330  1.00 25.64           O  
-HETATM 1750  O   HOH A4269       4.112  18.974   0.540  1.00 41.50           O  
-HETATM 1751  O   HOH A4270      11.496  18.225  15.919  1.00 28.83           O  
-HETATM 1752  O   HOH A4271      20.403  37.067   0.132  1.00 43.82           O  
-HETATM 1753  O   HOH A4272       5.704   7.828   6.573  1.00 41.06           O  
-HETATM 1754  O   HOH A4273      -8.575  33.760  23.070  1.00 42.21           O  
-HETATM 1755  O   HOH A4274      -7.136  17.159  15.353  1.00 37.45           O  
-HETATM 1756  O   HOH A4275       4.623  34.655   2.242  1.00 37.70           O  
-HETATM 1757  O   HOH A4276      10.311  14.924  29.892  1.00 49.48           O  
-HETATM 1758  O   HOH A4277       3.860  18.563   3.309  1.00 37.35           O  
-HETATM 1759  O   HOH A4278       6.983  26.295  31.857  1.00 49.68           O  
-HETATM 1760  O   HOH A4279      -7.082   8.992   9.405  1.00 33.25           O  
-HETATM 1761  O   HOH A4280      -7.008  23.126  30.102  1.00 49.46           O  
-HETATM 1762  O   HOH A4281      33.303  25.598   3.058  1.00 43.87           O  
-HETATM 1763  O   HOH A4282      14.783  37.312  -2.463  1.00 44.91           O  
-HETATM 1764  O   HOH A4283       9.790  30.798  -7.602  1.00 47.25           O  
-HETATM 1765  O   HOH A4284      15.680  39.255  18.659  1.00 34.78           O  
-HETATM 1766  O   HOH A4285      23.641  16.671   3.996  1.00 20.72           O  
-HETATM 1767  O   HOH A4286      -7.889  24.482  24.093  1.00 43.37           O  
-HETATM 1768  O   HOH A4287       9.093  10.090  15.685  1.00 27.38           O  
-HETATM 1769  O   HOH A4288      19.506  38.439  -3.583  1.00 48.89           O  
-HETATM 1770  O   HOH A4289      -7.945   6.469  23.253  1.00 40.26           O  
-HETATM 1771  O   HOH A4290      -2.479  24.079  -1.592  1.00 47.57           O  
-HETATM 1772  O   HOH A4291      -1.262  11.047   4.929  1.00 30.62           O  
-HETATM 1773  O   HOH A4292      11.555  40.357  13.388  1.00 45.36           O  
-HETATM 1774  O   HOH A4293      13.430  11.521  20.843  1.00 37.64           O  
-HETATM 1775  O   HOH A4294      33.182  22.431   2.385  1.00 32.69           O  
-HETATM 1776  O   HOH A4295       2.314  18.812  -2.754  1.00 54.35           O  
-HETATM 1777  O   HOH A4296      17.884  41.170   1.416  1.00 45.28           O  
-HETATM 1778  O   HOH A4297      19.360   8.813   6.257  1.00 37.08           O  
-HETATM 1779  O   HOH A4298      19.552  20.858  -9.998  1.00 51.77           O  
-HETATM 1780  O   HOH A4299      15.859  34.157  22.190  1.00 29.96           O  
-HETATM 1781  O   HOH A4300     -12.063  20.157  22.864  1.00 44.22           O  
-HETATM 1782  O   HOH A4301      -9.223  10.654  13.455  1.00 49.85           O  
-HETATM 1783  O   HOH A4302       0.463  29.380   2.313  1.00 39.91           O  
-HETATM 1784  O   HOH A4303       7.331  23.892  -7.861  1.00 43.80           O  
-HETATM 1785  O   HOH A4304      -1.918   3.832  11.602  1.00 39.38           O  
-HETATM 1786  O   HOH A4305       0.338  38.629  21.376  1.00 32.65           O  
-HETATM 1787  O   HOH A4306     -13.791  20.249  25.865  1.00 43.82           O  
-HETATM 1788  O   HOH A4307      11.657  40.733  22.304  1.00 49.13           O  
-HETATM 1789  O   HOH A4308       8.995  36.903  -1.898  1.00 49.42           O  
-HETATM 1790  O   HOH A4309      21.327  27.380  27.490  1.00 39.33           O  
-HETATM 1791  O   HOH A4310       3.146  30.779  33.903  1.00 35.85           O  
-HETATM 1792  O   HOH A4311      19.545  36.063  22.780  1.00 42.46           O  
-HETATM 1793  O   HOH A4312      24.732  36.942  19.218  1.00 35.75           O  
-HETATM 1794  O   HOH A4313       2.928  38.661   8.193  1.00 48.76           O  
-HETATM 1795  O   HOH A4314      26.057  20.102  -3.756  1.00 40.58           O  
-HETATM 1796  O   HOH A4315      -2.219  30.533  -2.868  1.00 50.51           O  
-HETATM 1797  O   HOH A4316      -7.453  22.550  27.437  1.00 34.05           O  
-HETATM 1798  O   HOH A4317      21.434   6.926  11.415  1.00 44.95           O  
-HETATM 1799  O   HOH A4318      21.918  20.411  25.359  1.00 35.22           O  
-HETATM 1800  O   HOH A4319      23.232  25.384  -4.785  1.00 37.03           O  
-HETATM 1801  O   HOH A4320      -6.473  29.226  21.854  1.00 37.07           O  
-HETATM 1802  O   HOH A4321     -11.994  16.942   6.390  1.00 51.30           O  
-HETATM 1803  O   HOH A4322       1.862  28.701  32.774  1.00 41.88           O  
-HETATM 1804  O   HOH A4323      -1.647   6.773  13.067  1.00 39.78           O  
-HETATM 1805  O   HOH A4324      11.044  17.514  32.739  1.00 47.13           O  
-HETATM 1806  O   HOH A4325      11.419  36.505  -2.874  1.00 37.79           O  
-HETATM 1807  O   HOH A4326      16.413   6.852  -0.438  1.00 54.40           O  
-HETATM 1808  O   HOH A4327       1.411  29.011  -0.219  1.00 43.61           O  
-HETATM 1809  O   HOH A4328      -2.342  36.201  21.266  1.00 45.02           O  
-HETATM 1810  O   HOH A4329       0.445  36.217  19.512  1.00 44.31           O  
-HETATM 1811  O   HOH A4330      19.598  12.416  12.982  1.00 29.58           O  
-HETATM 1812  O   HOH A4331      21.397  21.331  -8.087  1.00 45.06           O  
-HETATM 1813  O   HOH A4332      -8.845  35.030  27.298  1.00 37.35           O  
-HETATM 1814  O   HOH A4333      18.525  40.313  -1.896  1.00 51.63           O  
-HETATM 1815  O   HOH A4334      15.252  11.356  25.504  1.00 46.87           O  
-HETATM 1816  O   HOH A4335     -13.029  13.663  24.756  1.00 42.60           O  
-HETATM 1817  O   HOH A4336       3.675  38.918   3.533  1.00 54.70           O  
-HETATM 1818  O   HOH A4337     -12.318  11.455  26.230  1.00 50.56           O  
-HETATM 1819  O   HOH A4338     -10.179   9.139   9.408  1.00 34.22           O  
-HETATM 1820  O   HOH A4339      20.386  38.295  21.663  1.00 50.51           O  
-HETATM 1821  O   HOH A4340      10.190  27.345  31.167  1.00 47.99           O  
-HETATM 1822  O   HOH A4341      11.498  40.604  -0.697  1.00 44.70           O  
-HETATM 1823  O   HOH A4342       6.263   8.945  17.244  1.00 48.42           O  
-HETATM 1824  O   HOH A4343       1.270  21.574  -5.143  1.00 45.02           O  
-HETATM 1825  O   HOH A4344       3.363   6.025  12.265  1.00 39.00           O  
-HETATM 1826  O   HOH A4345       8.273  34.896  -3.490  1.00 44.30           O  
-HETATM 1827  O   HOH A4346      11.976  33.757  -5.107  1.00 37.52           O  
-HETATM 1828  O   HOH A4347      17.754  40.548  -6.406  1.00 42.88           O  
-HETATM 1829  O   HOH A4348      -1.623  15.568  39.798  1.00 54.50           O  
-HETATM 1830  O   HOH A4349       2.313   5.119  14.496  1.00 43.17           O  
-HETATM 1831  O   HOH A4350      25.707  15.219   9.881  1.00 43.77           O  
-HETATM 1832  O   HOH A4351       9.191  30.407  30.410  1.00 46.12           O  
-HETATM 1833  O   HOH A4352      16.616  35.733  24.216  1.00 54.90           O  
-HETATM 1834  O   HOH A4353      12.860  40.944  -2.864  1.00 51.04           O  
-HETATM 1835  O   HOH A4354      24.642  31.379  -3.353  1.00 37.50           O  
-HETATM 1836  O   HOH A4355     -10.865  27.596  27.217  1.00 53.29           O  
-HETATM 1837  O   HOH A4356      18.023  42.016  10.663  1.00 42.41           O  
-HETATM 1838  O   HOH A4357       4.570  19.778 -11.777  1.00 41.80           O  
-HETATM 1839  O   HOH A4358      28.282  25.373  -7.580  1.00 44.79           O  
-HETATM 1840  O   HOH A4359      28.580  36.623   8.466  1.00 38.46           O  
-HETATM 1841  O   HOH A4360      -7.623  29.163  24.215  1.00 50.61           O  
-HETATM 1842  O   HOH A4361       5.435  37.595  -5.698  1.00 51.79           O  
-HETATM 1843  O   HOH A4362      32.491  33.946  11.615  1.00 45.19           O  
-HETATM 1844  O   HOH A4363       6.578   9.336  22.725  1.00 26.29           O  
-HETATM 1845  O   HOH A4364       8.163  37.370  -5.007  1.00 49.47           O  
-HETATM 1846  O   HOH A4365      12.234   7.330   4.164  1.00 54.77           O  
-HETATM 1847  O   HOH A4366      13.473  15.114  31.720  1.00 51.10           O  
-HETATM 1848  O   HOH A4367      -1.910  13.242  35.722  1.00 48.75           O  
-HETATM 1849  O   HOH A4368       2.546  36.608   6.362  1.00 47.04           O  
-HETATM 1850  O   HOH A4369     -11.883  10.658  28.846  1.00 42.87           O  
-HETATM 1851  O   HOH A4370      -4.414  37.997  17.907  1.00 55.68           O  
-HETATM 1852  O   HOH A4371      26.945   6.794  10.977  1.00 48.51           O  
-HETATM 1853  O   HOH A4372       8.338  39.520  -1.986  1.00 54.21           O  
-HETATM 1854  O   HOH A4373       8.354  41.456  10.104  1.00 54.22           O  
-HETATM 1855  O   HOH A4374      13.080  43.225   3.735  1.00 33.29           O  
-HETATM 1856  O   HOH A4375      17.220  42.961  -1.906  1.00 39.29           O  
-HETATM 1857  O   HOH A4376     -15.982  12.194  13.755  1.00 59.03           O  
-HETATM 1858  O   HOH A4377     -13.218  17.427  20.115  1.00 46.00           O  
-HETATM 1859  O   HOH A4378       4.879  23.856  -7.003  1.00 53.97           O  
-HETATM 1860  O   HOH A4379      -4.383  11.192   9.498  1.00 38.49           O  
-HETATM 1861  O   HOH A4380       9.649  14.394  33.501  1.00 46.75           O  
-HETATM 1862  O   HOH A4381      15.954  14.909  23.961  1.00 48.89           O  
-HETATM 1863  O   HOH A4382      18.989  27.151 -12.503  1.00 51.46           O  
-HETATM 1864  O   HOH A4383     -10.010   8.020  14.655  1.00 40.35           O  
-HETATM 1865  O   HOH A4384      -7.459  34.632  17.022  1.00 53.79           O  
-HETATM 1866  O   HOH A4385      11.256  20.281  14.352  1.00 20.16           O  
-HETATM 1867  O   HOH A4386      -3.930  12.397  20.998  1.00 10.01           O  
-HETATM 1868  O   HOH A4387      27.492  14.361   3.863  1.00 42.55           O  
-HETATM 1869  O   HOH A4388      -9.761  13.430  10.854  1.00 47.12           O  
-HETATM 1870  O   HOH A4389      13.138  44.687   5.994  1.00 47.34           O  
-HETATM 1871  O   HOH A4390      -3.796  29.809   1.346  1.00 44.25           O  
-HETATM 1872  O   HOH A4391      32.688  29.425   8.042  1.00 46.67           O  
-HETATM 1873  O   HOH A4392      10.033   8.790   5.517  1.00 50.70           O  
-HETATM 1874  O   HOH A4393      13.309   7.731  12.351  1.00 42.87           O  
-HETATM 1875  O   HOH A4394      -0.492  22.231  -0.082  1.00 34.03           O  
-HETATM 1876  O   HOH A4395       1.473  34.779   8.980  1.00 37.59           O  
-HETATM 1877  O   HOH A4396       6.695  10.869   4.422  1.00 44.31           O  
-HETATM 1878  O   HOH A4397     -10.262  31.203  29.925  1.00 45.39           O  
-HETATM 1879  O   HOH A4398      21.331  32.346  20.038  1.00 39.09           O  
-HETATM 1880  O   HOH A4399     -13.149  13.023  13.034  1.00 49.50           O  
-HETATM 1881  O   HOH A4400     -10.141  37.032  28.168  1.00 45.34           O  
-HETATM 1882  O   HOH A4401       1.016  15.205  39.801  1.00 46.85           O  
-HETATM 1883  O   HOH A4402      19.528  15.720  20.002  1.00 28.90           O  
-HETATM 1884  O   HOH A4403      20.079  43.344  -2.892  1.00 40.91           O  
-HETATM 1885  O   HOH A4404      -6.420   6.809  10.588  1.00 48.52           O  
-HETATM 1886  O   HOH A4405      18.179  34.453  26.698  1.00 51.03           O  
-HETATM 1887  O   HOH A4406      14.398  32.190  24.708  1.00 39.76           O  
-HETATM 1888  O   HOH A4407      -3.744  13.687  29.830  1.00 36.07           O  
-HETATM 1889  O   HOH A4408      13.658  14.546  29.270  1.00 53.24           O  
-HETATM 1890  O   HOH A4409      -7.147  39.952  14.738  1.00 44.55           O  
-HETATM 1891  O   HOH A4410      25.998  25.437  24.523  1.00 45.58           O  
-HETATM 1892  O   HOH A4411      16.664  15.337  31.264  1.00 41.38           O  
-HETATM 1893  O   HOH A4412      24.997  41.520  13.646  1.00 47.15           O  
-HETATM 1894  O   HOH A4413       4.976  40.600  16.298  1.00 52.00           O  
-HETATM 1895  O   HOH A4414     -13.043  17.226  16.682  1.00 47.89           O  
-HETATM 1896  O   HOH A4415       1.770  28.445  -6.125  1.00 53.72           O  
-HETATM 1897  O   HOH A4416      10.214  22.465  31.816  1.00 40.61           O  
-HETATM 1898  O   HOH A4417     -10.540  22.856  29.895  1.00 43.09           O  
-HETATM 1899  O   HOH A4418      -0.474  27.895  -4.529  1.00 43.65           O  
-HETATM 1900  O   HOH A4419     -12.125  24.122  28.265  1.00 49.77           O  
-HETATM 1901  O   HOH A4420      -4.815  28.688  29.982  1.00 52.08           O  
-HETATM 1902  O   HOH A4421       9.509  41.947  -3.896  1.00 46.89           O  
-HETATM 1903  O   HOH A4422      22.880  29.995  25.462  1.00 49.88           O  
-HETATM 1904  O   HOH A4423      -6.285  29.429  28.098  1.00 46.19           O  
-HETATM 1905  O   HOH A4424     -15.315  14.699  20.540  1.00 45.46           O  
-HETATM 1906  O   HOH A4425       4.739  41.427   4.686  1.00 44.24           O  
-HETATM 1907  O   HOH A4426      17.952  40.056  22.199  1.00 48.35           O  
-HETATM 1908  O   HOH A4427       6.245  25.904  34.420  1.00 45.68           O  
-HETATM 1909  O   HOH A4428     -17.438  11.880  16.267  1.00 50.66           O  
-HETATM 1910  O   HOH A4429      15.755  48.217   2.486  1.00 43.31           O  
-HETATM 1911  O   HOH A4430       7.695  34.868 -10.443  1.00 52.08           O  
-HETATM 1912  O   HOH A4431      10.766  42.132   2.607  1.00 47.28           O  
-HETATM 1913  O   HOH A4432      12.688  39.619  19.191  1.00 47.54           O  
-HETATM 1914  O   HOH A4433     -12.714  34.389  23.735  1.00 41.61           O  
-HETATM 1915  O   HOH A4434      19.153  42.372  18.154  1.00 50.29           O  
-HETATM 1916  O   HOH A4435      10.449   8.241   1.951  1.00 50.12           O  
-HETATM 1917  O   HOH A4436     -15.537  12.278  17.906  1.00 49.96           O  
-HETATM 1918  O   HOH A4437       7.808  43.615   6.677  1.00 38.36           O  
-CONECT  172  461                                                                
-CONECT  188 1648                                                                
-CONECT  413  719                                                                
-CONECT  461  172                                                                
-CONECT  719  413                                                                
-CONECT 1162 1535                                                                
-CONECT 1535 1162                                                                
-CONECT 1617 1619 1639 1643                                                      
-CONECT 1618 1619 1622                                                           
-CONECT 1619 1617 1618 1620                                                      
-CONECT 1620 1619 1621                                                           
-CONECT 1621 1620 1623                                                           
-CONECT 1622 1618 1623                                                           
-CONECT 1623 1621 1622 1624                                                      
-CONECT 1624 1623 1625 1631                                                      
-CONECT 1625 1624 1626 1627 1628                                                 
-CONECT 1626 1625                                                                
-CONECT 1627 1625                                                                
-CONECT 1628 1625                                                                
-CONECT 1629 1630 1637                                                           
-CONECT 1630 1629 1648                                                           
-CONECT 1631 1624 1632                                                           
-CONECT 1632 1631 1633 1637                                                      
-CONECT 1633 1632 1634                                                           
-CONECT 1634 1633 1635 1636                                                      
-CONECT 1635 1634                                                                
-CONECT 1636 1634                                                                
-CONECT 1637 1629 1632 1638                                                      
-CONECT 1638 1637                                                                
-CONECT 1639 1617 1640                                                           
-CONECT 1640 1639 1641                                                           
-CONECT 1641 1640 1642 1644                                                      
-CONECT 1642 1641 1643                                                           
-CONECT 1643 1617 1642                                                           
-CONECT 1644 1641 1645 1646 1647                                                 
-CONECT 1645 1644                                                                
-CONECT 1646 1644                                                                
-CONECT 1647 1644                                                                
-CONECT 1648  188 1630 1649                                                      
-CONECT 1649 1648                                                                
-MASTER      285    0    1    8   12    0    6    6 1917    1   40   17          
-END                                                                             
diff --git a/plip/test/pdb/1xdn.pdb b/plip/test/pdb/1xdn.pdb
deleted file mode 100644
index 0c06611..0000000
--- a/plip/test/pdb/1xdn.pdb
+++ /dev/null
@@ -1,5703 +0,0 @@
-HEADER    LIGASE                                  07-SEP-04   1XDN              
-TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF AN EDITOSOME ENZYME FROM         
-TITLE    2 TRYPANOSOMA BRUCEI: RNA EDITING LIGASE 1                             
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: RNA EDITING LIGASE MP52;                                   
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 FRAGMENT: ADENYLATION DOMAIN;                                        
-COMPND   5 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;                             
-SOURCE   3 ORGANISM_TAXID: 5691;                                                
-SOURCE   4 GENE: MP52;                                                          
-SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21GOLD DE3;                              
-SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PSKB3                                     
-KEYWDS    RNA EDITING, LIGASE, TRYPANOSOMA BRUCEI,                              
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    J.DENG,A.SCHNAUFER,R.SALAVATI,K.D.STUART,W.G.HOL                      
-REVDAT   3   10-SEP-14 1XDN    1       JRNL   VERSN                             
-REVDAT   2   24-FEB-09 1XDN    1       VERSN                                    
-REVDAT   1   07-DEC-04 1XDN    0                                                
-JRNL        AUTH   J.DENG,A.SCHNAUFER,R.SALAVATI,K.D.STUART,W.G.HOL             
-JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURE OF A KEY EDITOSOME ENZYME  
-JRNL        TITL 2 FROM TRYPANOSOMA BRUCEI: RNA EDITING LIGASE 1.               
-JRNL        REF    J.MOL.BIOL.                   V. 343   601 2004              
-JRNL        REFN                   ISSN 0022-2836                               
-JRNL        PMID   15465048                                                     
-JRNL        DOI    10.1016/J.JMB.2004.08.041                                    
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
-REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
-REMARK   3   NUMBER OF REFLECTIONS             : 78835                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.129                           
-REMARK   3   R VALUE            (WORKING SET) : 0.128                           
-REMARK   3   FREE R VALUE                     : 0.148                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 4149                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.20                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23                         
-REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4798                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.1170                       
-REMARK   3   BIN FREE R VALUE SET COUNT          : 260                          
-REMARK   3   BIN FREE R VALUE                    : 0.1310                       
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 2119                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 32                                      
-REMARK   3   SOLVENT ATOMS            : 440                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 7.29                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.40                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -0.22000                                             
-REMARK   3    B22 (A**2) : -0.02000                                             
-REMARK   3    B33 (A**2) : 0.28000                                              
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.12000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
-REMARK   3   ESU BASED ON R VALUE                            (A): 0.034         
-REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.033         
-REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.017         
-REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.349         
-REMARK   3                                                                      
-REMARK   3 CORRELATION COEFFICIENTS.                                            
-REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
-REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.972                         
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
-REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2206 ; 0.010 ; 0.021       
-REMARK   3   BOND LENGTHS OTHERS               (A):  1976 ; 0.002 ; 0.020       
-REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2993 ; 1.420 ; 1.978       
-REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4606 ; 0.784 ; 3.000       
-REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   264 ; 5.763 ; 5.000       
-REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
-REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
-REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
-REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   320 ; 0.084 ; 0.200       
-REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2428 ; 0.011 ; 0.020       
-REMARK   3   GENERAL PLANES OTHERS             (A):   457 ; 0.017 ; 0.020       
-REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   423 ; 0.220 ; 0.200       
-REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2349 ; 0.250 ; 0.200       
-REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED TORSION OTHERS         (A):  1304 ; 0.084 ; 0.200       
-REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   304 ; 0.169 ; 0.200       
-REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    11 ; 0.119 ; 0.200       
-REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.217 ; 0.200       
-REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    36 ; 0.177 ; 0.200       
-REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
-REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1319 ; 1.192 ; 1.500       
-REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2128 ; 1.915 ; 2.000       
-REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   887 ; 2.829 ; 3.000       
-REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   865 ; 4.258 ; 4.500       
-REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
-REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS STATISTICS                                           
-REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
-REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
-REMARK   3   VDW PROBE RADIUS   : 1.40                                          
-REMARK   3   ION PROBE RADIUS   : 0.80                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
-REMARK   3  POSITIONS                                                           
-REMARK   4                                                                      
-REMARK   4 1XDN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-04.                  
-REMARK 100 THE RCSB ID CODE IS RCSB030242.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-03                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 7.5                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : APS                                
-REMARK 200  BEAMLINE                       : 19-ID                              
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97885, 0.97899, 0.96112          
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95711                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.8                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : 0.06400                            
-REMARK 200  R SYM                      (I) : 0.06400                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.8000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.8                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.06400                            
-REMARK 200  R SYM FOR SHELL            (I) : 0.06400                            
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 33.800                             
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
-REMARK 200 SOFTWARE USED: SOLVE                                                 
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 45.80                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM CHLORIDE, TRIS,      
-REMARK 280  ATP, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K        
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,Y+1/2,-Z                                             
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.28950            
-REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     GLY A    48                                                      
-REMARK 465     HIS A    49                                                      
-REMARK 465     MET A    50                                                      
-REMARK 465     ASP A    51                                                      
-REMARK 465     LYS A   317                                                      
-REMARK 465     HIS A   318                                                      
-REMARK 465     PRO A   319                                                      
-REMARK 465     GLY A   320                                                      
-REMARK 465     LYS A   321                                                      
-REMARK 465     GLN A   322                                                      
-REMARK 465     LYS A   323                                                      
-REMARK 465     GLU A   324                                                      
-REMARK 480                                                                      
-REMARK 480 ZERO OCCUPANCY ATOM                                                  
-REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
-REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
-REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
-REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
-REMARK 480   M RES C SSEQI ATOMS                                                
-REMARK 480     GLU A  278   CD   OE1  OE2                                       
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   OE1  GLU A   278     O    HOH A   677              2.08            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    TYR A 165       96.21   -160.96                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 620                                                                      
-REMARK 620 METAL COORDINATION                                                   
-REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG A 502  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 ATP A 501   O1G                                                    
-REMARK 620 2 ATP A 501   O2B  86.6                                              
-REMARK 620 3 HOH A 528   O   177.6  94.7                                        
-REMARK 620 4 HOH A 514   O    89.5 173.3  89.4                                  
-REMARK 620 5 HOH A 530   O    90.8  95.6  87.1  89.9                            
-REMARK 620 6 HOH A 520   O    96.9  90.2  85.1  84.9 170.6                      
-REMARK 620 N                    1     2     3     4     5                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 501                 
-DBREF  1XDN A   51   324  GB     11067037 AAG27062        51    324             
-SEQADV 1XDN GLY A   48  GB   11067037            CLONING ARTIFACT               
-SEQADV 1XDN HIS A   49  GB   11067037            CLONING ARTIFACT               
-SEQADV 1XDN MET A   50  GB   11067037            CLONING ARTIFACT               
-SEQADV 1XDN MSE A  115  GB   11067037  MET   115 MODIFIED RESIDUE               
-SEQADV 1XDN MSE A  263  GB   11067037  MET   263 MODIFIED RESIDUE               
-SEQADV 1XDN MSE A  314  GB   11067037  MET   314 MODIFIED RESIDUE               
-SEQRES   1 A  277  GLY HIS MET ASP GLN SER ASP PHE SER PRO TYR ILE GLU          
-SEQRES   2 A  277  ILE ASP LEU PRO SER GLU SER ARG ILE GLN SER LEU HIS          
-SEQRES   3 A  277  LYS SER GLY LEU ALA ALA GLN GLU TRP VAL ALA CYS GLU          
-SEQRES   4 A  277  LYS VAL HIS GLY THR ASN PHE GLY ILE TYR LEU ILE ASN          
-SEQRES   5 A  277  GLN GLY ASP HIS GLU VAL VAL ARG PHE ALA LYS ARG SER          
-SEQRES   6 A  277  GLY ILE MSE ASP PRO ASN GLU ASN PHE PHE GLY TYR HIS          
-SEQRES   7 A  277  ILE LEU ILE ASP GLU PHE THR ALA GLN ILE ARG ILE LEU          
-SEQRES   8 A  277  ASN ASP LEU LEU LYS GLN LYS TYR GLY LEU SER ARG VAL          
-SEQRES   9 A  277  GLY ARG LEU VAL LEU ASN GLY GLU LEU PHE GLY ALA LYS          
-SEQRES  10 A  277  TYR LYS HIS PRO LEU VAL PRO LYS SER GLU LYS TRP CYS          
-SEQRES  11 A  277  THR LEU PRO ASN GLY LYS LYS PHE PRO ILE ALA GLY VAL          
-SEQRES  12 A  277  GLN ILE GLN ARG GLU PRO PHE PRO GLN TYR SER PRO GLU          
-SEQRES  13 A  277  LEU HIS PHE PHE ALA PHE ASP ILE LYS TYR SER VAL SER          
-SEQRES  14 A  277  GLY ALA GLU GLU ASP PHE VAL LEU LEU GLY TYR ASP GLU          
-SEQRES  15 A  277  PHE VAL GLU PHE SER SER LYS VAL PRO ASN LEU LEU TYR          
-SEQRES  16 A  277  ALA ARG ALA LEU VAL ARG GLY THR LEU ASP GLU CYS LEU          
-SEQRES  17 A  277  ALA PHE ASP VAL GLU ASN PHE MSE THR PRO LEU PRO ALA          
-SEQRES  18 A  277  LEU LEU GLY LEU GLY ASN TYR PRO LEU GLU GLY ASN LEU          
-SEQRES  19 A  277  ALA GLU GLY VAL VAL ILE ARG HIS VAL ARG ARG GLY ASP          
-SEQRES  20 A  277  PRO ALA VAL GLU LYS HIS ASN VAL SER THR ILE ILE LYS          
-SEQRES  21 A  277  LEU ARG CYS SER SER PHE MSE GLU LEU LYS HIS PRO GLY          
-SEQRES  22 A  277  LYS GLN LYS GLU                                              
-MODRES 1XDN MSE A  115  MET  SELENOMETHIONINE                                   
-MODRES 1XDN MSE A  263  MET  SELENOMETHIONINE                                   
-MODRES 1XDN MSE A  314  MET  SELENOMETHIONINE                                   
-HET    MSE  A 115       8                                                       
-HET    MSE  A 263       8                                                       
-HET    MSE  A 314      10                                                       
-HET     MG  A 502       1                                                       
-HET    ATP  A 501      31                                                       
-HETNAM     MSE SELENOMETHIONINE                                                 
-HETNAM      MG MAGNESIUM ION                                                    
-HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
-FORMUL   1  MSE    3(C5 H11 N O2 SE)                                            
-FORMUL   2   MG    MG 2+                                                        
-FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
-FORMUL   4  HOH   *440(H2 O)                                                    
-HELIX    1   1 SER A   65  SER A   75  1                                  11    
-HELIX    2   2 GLY A   76  GLN A   80  5                                   5    
-HELIX    3   3 GLY A  123  ILE A  126  5                                   4    
-HELIX    4   4 LEU A  127  GLY A  147  1                                  21    
-HELIX    5   5 ALA A  188  VAL A  190  5                                   3    
-HELIX    6   6 ALA A  218  GLU A  220  5                                   3    
-HELIX    7   7 GLY A  226  LYS A  236  1                                  11    
-HELIX    8   8 THR A  250  ALA A  256  1                                   7    
-HELIX    9   9 ASP A  258  PHE A  262  5                                   5    
-HELIX   10  10 PRO A  265  LEU A  270  1                                   6    
-HELIX   11  11 ASP A  294  LYS A  299  1                                   6    
-HELIX   12  12 CYS A  310  LEU A  316  1                                   7    
-SHEET    1   A 4 VAL A 247  GLY A 249  0                                        
-SHEET    2   A 4 TRP A  82  LYS A  87 -1  N  TRP A  82   O  GLY A 249           
-SHEET    3   A 4 GLY A 284  HIS A 289 -1  O  VAL A 286   N  CYS A  85           
-SHEET    4   A 4 ILE A 305  ARG A 309 -1  O  ILE A 306   N  ILE A 287           
-SHEET    1   B 6 GLY A 113  ILE A 114  0                                        
-SHEET    2   B 6 HIS A 103  LYS A 110 -1  N  LYS A 110   O  GLY A 113           
-SHEET    3   B 6 THR A  91  GLN A 100 -1  N  GLN A 100   O  HIS A 103           
-SHEET    4   B 6 ARG A 153  LYS A 164 -1  O  LEU A 160   N  THR A  91           
-SHEET    5   B 6 SER A 201  SER A 214 -1  O  LYS A 212   N  VAL A 155           
-SHEET    6   B 6 PHE A 222  LEU A 224 -1  O  VAL A 223   N  TYR A 213           
-SHEET    1   C 6 GLY A 113  ILE A 114  0                                        
-SHEET    2   C 6 HIS A 103  LYS A 110 -1  N  LYS A 110   O  GLY A 113           
-SHEET    3   C 6 THR A  91  GLN A 100 -1  N  GLN A 100   O  HIS A 103           
-SHEET    4   C 6 ARG A 153  LYS A 164 -1  O  LEU A 160   N  THR A  91           
-SHEET    5   C 6 SER A 201  SER A 214 -1  O  LYS A 212   N  VAL A 155           
-SHEET    6   C 6 LEU A 241  TYR A 242  1  O  LEU A 241   N  ALA A 208           
-SHEET    1   D 2 TRP A 176  THR A 178  0                                        
-SHEET    2   D 2 LYS A 184  PRO A 186 -1  O  PHE A 185   N  CYS A 177           
-LINK         C   ILE A 114                 N   MSE A 115     1555   1555  1.33  
-LINK         C   MSE A 115                 N   ASP A 116     1555   1555  1.33  
-LINK         C   PHE A 262                 N   MSE A 263     1555   1555  1.33  
-LINK         C   MSE A 263                 N   THR A 264     1555   1555  1.32  
-LINK         C   PHE A 313                 N   MSE A 314     1555   1555  1.33  
-LINK         C   MSE A 314                 N   GLU A 315     1555   1555  1.33  
-LINK        MG    MG A 502                 O1G ATP A 501     1555   1555  2.09  
-LINK        MG    MG A 502                 O2B ATP A 501     1555   1555  2.06  
-LINK        MG    MG A 502                 O   HOH A 528     1555   1555  2.13  
-LINK        MG    MG A 502                 O   HOH A 514     1555   1555  2.07  
-LINK        MG    MG A 502                 O   HOH A 530     1555   1555  2.04  
-LINK        MG    MG A 502                 O   HOH A 520     1555   1555  2.11  
-CISPEP   1 PHE A  197    PRO A  198          0        -7.28                     
-SITE     1 AC1  5 ATP A 501  HOH A 514  HOH A 520  HOH A 528                    
-SITE     2 AC1  5 HOH A 530                                                     
-SITE     1 AC2 27 TYR A  58  ILE A  59  GLU A  60  ILE A  61                    
-SITE     2 AC2 27 GLU A  86  LYS A  87  VAL A  88  ASN A  92                    
-SITE     3 AC2 27 ARG A 111  GLU A 159  PHE A 209  VAL A 286                    
-SITE     4 AC2 27 LYS A 307  ARG A 309   MG A 502  HOH A 514                    
-SITE     5 AC2 27 HOH A 520  HOH A 528  HOH A 530  HOH A 536                    
-SITE     6 AC2 27 HOH A 587  HOH A 634  HOH A 650  HOH A 777                    
-SITE     7 AC2 27 HOH A 829  HOH A 871  HOH A 886                               
-CRYST1   44.911   58.579   52.984  90.00 100.23  90.00 P 1 21 1      2          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.022266  0.000000  0.004018        0.00000                         
-SCALE2      0.000000  0.017071  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.019179        0.00000                         
-ATOM      1  N   GLN A  52      42.237  16.800  35.823  1.00 12.04           N  
-ANISOU    1  N   GLN A  52     1764   1519   1290    -51     85      8       N  
-ATOM      2  CA  GLN A  52      41.667  17.015  34.477  1.00 10.21           C  
-ANISOU    2  CA  GLN A  52     1684   1030   1163     45     63    174       C  
-ATOM      3  C   GLN A  52      40.148  17.010  34.446  1.00 10.33           C  
-ANISOU    3  C   GLN A  52     1788   1017   1117    104    129    163       C  
-ATOM      4  O   GLN A  52      39.564  17.006  33.382  1.00  9.88           O  
-ANISOU    4  O   GLN A  52     1826    876   1049    292    181    182       O  
-ATOM      5  CB  GLN A  52      42.228  15.967  33.522  1.00  9.36           C  
-ANISOU    5  CB  GLN A  52     1554    833   1170     72     15    146       C  
-ATOM      6  CG  GLN A  52      43.734  16.095  33.352  1.00  9.40           C  
-ANISOU    6  CG  GLN A  52     1581    771   1218     86   -200    237       C  
-ATOM      7  CD  GLN A  52      44.170  17.346  32.622  1.00  8.47           C  
-ANISOU    7  CD  GLN A  52     1399    689   1130     22   -142    158       C  
-ATOM      8  OE1 GLN A  52      45.312  17.791  32.785  1.00 12.47           O  
-ANISOU    8  OE1 GLN A  52     1745   1079   1911    -88   -491    288       O  
-ATOM      9  NE2 GLN A  52      43.296  17.915  31.849  1.00  8.79           N  
-ANISOU    9  NE2 GLN A  52     1234   1041   1063     15    -69    506       N  
-ATOM     10  N   SER A  53      39.488  17.025  35.604  1.00 11.01           N  
-ANISOU   10  N   SER A  53     1803   1212   1166    179    187    226       N  
-ATOM     11  CA  SER A  53      38.026  16.949  35.611  1.00 12.75           C  
-ANISOU   11  CA  SER A  53     1863   1569   1413    117    173    171       C  
-ATOM     12  C   SER A  53      37.340  18.091  34.862  1.00 12.38           C  
-ANISOU   12  C   SER A  53     1797   1573   1333    176    171    119       C  
-ATOM     13  O   SER A  53      36.209  17.937  34.426  1.00 14.69           O  
-ANISOU   13  O   SER A  53     2013   1898   1670    142    240    202       O  
-ATOM     14  CB  SER A  53      37.462  16.890  37.026  1.00 13.59           C  
-ANISOU   14  CB  SER A  53     1919   1711   1532    147    222    282       C  
-ATOM     15  OG  SER A  53      37.854  18.006  37.781  1.00 17.90           O  
-ANISOU   15  OG  SER A  53     2616   2299   1887    226    311    383       O  
-ATOM     16  N   ASP A  54      38.012  19.228  34.730  1.00 11.65           N  
-ANISOU   16  N   ASP A  54     1724   1454   1246    264    152    134       N  
-ATOM     17  CA  ASP A  54      37.455  20.341  33.968  1.00 11.85           C  
-ANISOU   17  CA  ASP A  54     1767   1455   1278    249    117    178       C  
-ATOM     18  C   ASP A  54      37.742  20.271  32.474  1.00 10.23           C  
-ANISOU   18  C   ASP A  54     1562   1275   1050    292    187    237       C  
-ATOM     19  O   ASP A  54      37.168  21.045  31.722  1.00 11.10           O  
-ANISOU   19  O   ASP A  54     1719   1326   1173    448    195    446       O  
-ATOM     20  CB  ASP A  54      37.947  21.667  34.531  1.00 13.04           C  
-ANISOU   20  CB  ASP A  54     1995   1543   1413    294     64    201       C  
-ATOM     21  CG  ASP A  54      37.464  21.907  35.937  1.00 16.08           C  
-ANISOU   21  CG  ASP A  54     2341   1811   1956    415     -6    115       C  
-ATOM     22  OD1 ASP A  54      36.280  21.638  36.211  1.00 19.99           O  
-ANISOU   22  OD1 ASP A  54     3244   2206   2145    740    396    -50       O  
-ATOM     23  OD2 ASP A  54      38.207  22.360  36.811  1.00 21.76           O  
-ANISOU   23  OD2 ASP A  54     3388   2268   2612    735      2   -249       O  
-ATOM     24  N   PHE A  55      38.617  19.367  32.044  1.00  9.13           N  
-ANISOU   24  N   PHE A  55     1451   1102    915    233    164    264       N  
-ATOM     25  CA  PHE A  55      38.972  19.219  30.642  1.00  8.35           C  
-ANISOU   25  CA  PHE A  55     1276    990    906    119    108    255       C  
-ATOM     26  C   PHE A  55      37.915  18.485  29.848  1.00  8.87           C  
-ANISOU   26  C   PHE A  55     1313    994   1061     61    120    286       C  
-ATOM     27  O   PHE A  55      37.392  17.475  30.303  1.00 10.67           O  
-ANISOU   27  O   PHE A  55     1623   1170   1260   -158    142    415       O  
-ATOM     28  CB  PHE A  55      40.300  18.470  30.543  1.00  8.52           C  
-ANISOU   28  CB  PHE A  55     1252   1126    858    129     47    237       C  
-ATOM     29  CG  PHE A  55      40.730  18.127  29.138  1.00  7.26           C  
-ANISOU   29  CG  PHE A  55     1080    883    793    155     55    228       C  
-ATOM     30  CD1 PHE A  55      41.050  19.110  28.229  1.00  7.47           C  
-ANISOU   30  CD1 PHE A  55     1050    928    859    -63    -52    233       C  
-ATOM     31  CD2 PHE A  55      40.847  16.803  28.753  1.00  8.45           C  
-ANISOU   31  CD2 PHE A  55     1262    862   1085     80    -70    130       C  
-ATOM     32  CE1 PHE A  55      41.470  18.763  26.957  1.00  8.40           C  
-ANISOU   32  CE1 PHE A  55     1229   1056    906    -61     20    249       C  
-ATOM     33  CE2 PHE A  55      41.266  16.455  27.495  1.00  8.90           C  
-ANISOU   33  CE2 PHE A  55     1324    977   1079     50    -63    -24       C  
-ATOM     34  CZ  PHE A  55      41.584  17.426  26.589  1.00  9.37           C  
-ANISOU   34  CZ  PHE A  55     1038   1362   1158    -23   -149     95       C  
-ATOM     35  N   SER A  56      37.615  18.984  28.653  1.00  8.47           N  
-ANISOU   35  N   SER A  56     1233    979   1006     32    116    228       N  
-ATOM     36  CA  SER A  56      36.702  18.341  27.727  1.00  8.75           C  
-ANISOU   36  CA  SER A  56     1231   1019   1072     38     57    197       C  
-ATOM     37  C   SER A  56      37.409  18.135  26.390  1.00  8.22           C  
-ANISOU   37  C   SER A  56     1168    944   1009     47     69    195       C  
-ATOM     38  O   SER A  56      37.676  19.116  25.681  1.00  8.56           O  
-ANISOU   38  O   SER A  56     1332    879   1041     91    107    301       O  
-ATOM     39  CB  SER A  56      35.476  19.231  27.540  1.00  9.47           C  
-ANISOU   39  CB  SER A  56     1297   1149   1149     85     42    121       C  
-ATOM     40  OG  SER A  56      34.454  18.554  26.839  1.00 11.56           O  
-ANISOU   40  OG  SER A  56     1305   1468   1617    -23    -67    121       O  
-ATOM     41  N   PRO A  57      37.729  16.888  26.033  1.00  8.33           N  
-ANISOU   41  N   PRO A  57     1272    890   1002     32    116    228       N  
-ATOM     42  CA  PRO A  57      38.409  16.649  24.754  1.00  8.76           C  
-ANISOU   42  CA  PRO A  57     1200   1016   1111     46     70    126       C  
-ATOM     43  C   PRO A  57      37.622  17.191  23.585  1.00  8.53           C  
-ANISOU   43  C   PRO A  57     1115   1087   1037     -2     90    120       C  
-ATOM     44  O   PRO A  57      36.400  17.105  23.551  1.00 10.15           O  
-ANISOU   44  O   PRO A  57     1192   1471   1192   -149     81    282       O  
-ATOM     45  CB  PRO A  57      38.525  15.124  24.677  1.00  9.69           C  
-ANISOU   45  CB  PRO A  57     1335   1102   1242     80    109    130       C  
-ATOM     46  CG  PRO A  57      38.403  14.640  26.059  1.00 11.00           C  
-ANISOU   46  CG  PRO A  57     1529   1180   1471    -88    159    137       C  
-ATOM     47  CD  PRO A  57      37.508  15.628  26.772  1.00  9.30           C  
-ANISOU   47  CD  PRO A  57     1414    924   1193    -51    111    240       C  
-ATOM     48  N   TYR A  58      38.339  17.747  22.619  1.00  7.67           N  
-ANISOU   48  N   TYR A  58     1033    891    988     31     36    154       N  
-ATOM     49  CA  TYR A  58      37.722  18.174  21.383  1.00  8.58           C  
-ANISOU   49  CA  TYR A  58     1188    996   1074     55     -4     48       C  
-ATOM     50  C   TYR A  58      37.720  16.916  20.539  1.00 10.08           C  
-ANISOU   50  C   TYR A  58     1394   1110   1326     65    -88     72       C  
-ATOM     51  O   TYR A  58      37.954  15.802  21.051  1.00 12.68           O  
-ANISOU   51  O   TYR A  58     1913   1264   1641     93    -65     79       O  
-ATOM     52  CB  TYR A  58      38.459  19.389  20.783  1.00  7.74           C  
-ANISOU   52  CB  TYR A  58     1048    922    971      4     19    108       C  
-ATOM     53  CG  TYR A  58      37.649  20.058  19.693  1.00  7.14           C  
-ANISOU   53  CG  TYR A  58      861    917    932     -6     51    201       C  
-ATOM     54  CD1 TYR A  58      36.490  20.749  19.989  1.00  7.63           C  
-ANISOU   54  CD1 TYR A  58      917   1131    849     48    144     55       C  
-ATOM     55  CD2 TYR A  58      38.011  19.951  18.354  1.00  7.35           C  
-ANISOU   55  CD2 TYR A  58      888    932    972    137    181    246       C  
-ATOM     56  CE1 TYR A  58      35.725  21.321  18.986  1.00  6.97           C  
-ANISOU   56  CE1 TYR A  58      857    814    975    105     84    107       C  
-ATOM     57  CE2 TYR A  58      37.237  20.520  17.348  1.00  7.25           C  
-ANISOU   57  CE2 TYR A  58      889    973    892    200    133    157       C  
-ATOM     58  CZ  TYR A  58      36.095  21.188  17.671  1.00  6.13           C  
-ANISOU   58  CZ  TYR A  58      822    864    641     39    -21    125       C  
-ATOM     59  OH  TYR A  58      35.360  21.745  16.658  1.00  7.63           O  
-ANISOU   59  OH  TYR A  58      905   1039    954    192    126    112       O  
-ATOM     60  N   ILE A  59      37.333  17.049  19.295  1.00 12.35           N  
-ANISOU   60  N   ILE A  59     1858   1391   1442     67    -54     19       N  
-ATOM     61  CA  ILE A  59      37.115  15.901  18.448  1.00 12.48           C  
-ANISOU   61  CA  ILE A  59     1815   1511   1414    -18      3     -5       C  
-ATOM     62  C   ILE A  59      38.089  15.820  17.302  1.00 11.76           C  
-ANISOU   62  C   ILE A  59     1818   1340   1310   -112     39    106       C  
-ATOM     63  O   ILE A  59      38.750  16.803  16.917  1.00 13.39           O  
-ANISOU   63  O   ILE A  59     2188   1365   1534   -381     75    175       O  
-ATOM     64  CB  ILE A  59      35.694  15.926  17.889  1.00 13.52           C  
-ANISOU   64  CB  ILE A  59     1835   1762   1541    -39    108     14       C  
-ATOM     65  CG1 ILE A  59      35.445  17.222  17.112  1.00 15.44           C  
-ANISOU   65  CG1 ILE A  59     1949   2069   1846     73      0   -114       C  
-ATOM     66  CG2 ILE A  59      34.704  15.759  19.016  1.00 15.64           C  
-ANISOU   66  CG2 ILE A  59     2034   2173   1734    -60    181     -9       C  
-ATOM     67  CD1 ILE A  59      34.256  17.154  16.212  1.00 17.64           C  
-ANISOU   67  CD1 ILE A  59     2133   2466   2102    160    -11    -39       C  
-ATOM     68  N   GLU A  60      38.180  14.611  16.777  1.00 10.67           N  
-ANISOU   68  N   GLU A  60     1639   1280   1133    -23    -37     88       N  
-ATOM     69  CA  GLU A  60      38.661  14.409  15.428  1.00 10.55           C  
-ANISOU   69  CA  GLU A  60     1532   1315   1163     56    -49     68       C  
-ATOM     70  C   GLU A  60      37.481  14.459  14.452  1.00  8.69           C  
-ANISOU   70  C   GLU A  60     1216   1143    942     52     12    -16       C  
-ATOM     71  O   GLU A  60      36.332  14.278  14.839  1.00 10.07           O  
-ANISOU   71  O   GLU A  60     1502   1442    879    -96     30    -26       O  
-ATOM     72  CB  GLU A  60      39.495  13.129  15.350  1.00 12.80           C  
-ANISOU   72  CB  GLU A  60     1738   1695   1428    183     12     58       C  
-ATOM     73  CG  GLU A  60      40.798  13.316  16.137  1.00 17.70           C  
-ANISOU   73  CG  GLU A  60     2231   2365   2126    151     23    142       C  
-ATOM     74  CD  GLU A  60      41.613  12.057  16.350  1.00 21.64           C  
-ANISOU   74  CD  GLU A  60     2708   3021   2493    302   -110    170       C  
-ATOM     75  OE1 GLU A  60      41.570  11.155  15.484  1.00 23.57           O  
-ANISOU   75  OE1 GLU A  60     3086   2940   2929    615    207     -9       O  
-ATOM     76  OE2 GLU A  60      42.308  11.976  17.395  1.00 25.13           O  
-ANISOU   76  OE2 GLU A  60     3159   3620   2769    347    -86    501       O  
-ATOM     77  N   ILE A  61      37.793  14.733  13.206  1.00  6.90           N  
-ANISOU   77  N   ILE A  61      935    872    813      2    -41    -38       N  
-ATOM     78  CA  ILE A  61      36.779  14.950  12.200  1.00  7.13           C  
-ANISOU   78  CA  ILE A  61      905    956    846     47    -10    -79       C  
-ATOM     79  C   ILE A  61      37.084  14.056  11.030  1.00  7.33           C  
-ANISOU   79  C   ILE A  61      914    895    976     45     11   -111       C  
-ATOM     80  O   ILE A  61      38.219  13.998  10.572  1.00  8.79           O  
-ANISOU   80  O   ILE A  61      909   1355   1074     35     25   -277       O  
-ATOM     81  CB  ILE A  61      36.757  16.443  11.793  1.00  6.83           C  
-ANISOU   81  CB  ILE A  61      872    907    815     11      2    -39       C  
-ATOM     82  CG1 ILE A  61      36.419  17.333  12.993  1.00  6.74           C  
-ANISOU   82  CG1 ILE A  61      894    785    881    -42    -61     65       C  
-ATOM     83  CG2 ILE A  61      35.749  16.663  10.695  1.00  6.97           C  
-ANISOU   83  CG2 ILE A  61      825   1030    791     13     -1   -137       C  
-ATOM     84  CD1 ILE A  61      36.548  18.813  12.744  1.00  7.60           C  
-ANISOU   84  CD1 ILE A  61      801    979   1105     37   -192     19       C  
-ATOM     85  N   ASP A  62      36.066  13.372  10.530  1.00  6.96           N  
-ANISOU   85  N   ASP A  62      879    847    917     63     -2   -113       N  
-ATOM     86  CA  ASP A  62      36.254  12.425   9.448  1.00  7.34           C  
-ANISOU   86  CA  ASP A  62     1021    854    911     87     -4   -129       C  
-ATOM     87  C   ASP A  62      36.040  13.011   8.060  1.00  6.96           C  
-ANISOU   87  C   ASP A  62      928    814    901     54    -13   -187       C  
-ATOM     88  O   ASP A  62      35.232  13.916   7.872  1.00  6.52           O  
-ANISOU   88  O   ASP A  62      908    660    910    138      9    -84       O  
-ATOM     89  CB  ASP A  62      35.294  11.244   9.583  1.00  8.39           C  
-ANISOU   89  CB  ASP A  62     1213    924   1048     72    -53    -65       C  
-ATOM     90  CG  ASP A  62      35.411  10.521  10.881  1.00 11.97           C  
-ANISOU   90  CG  ASP A  62     1683   1327   1535     27     30     -2       C  
-ATOM     91  OD1 ASP A  62      36.506  10.494  11.474  1.00 15.65           O  
-ANISOU   91  OD1 ASP A  62     2210   1886   1848    225   -149    466       O  
-ATOM     92  OD2 ASP A  62      34.418   9.952  11.370  1.00 17.75           O  
-ANISOU   92  OD2 ASP A  62     2414   2056   2271    -23     11    498       O  
-ATOM     93  N   LEU A  63      36.758  12.454   7.084  1.00  6.71           N  
-ANISOU   93  N   LEU A  63      874    717    956    136    -25   -252       N  
-ATOM     94  CA  LEU A  63      36.396  12.571   5.682  1.00  6.81           C  
-ANISOU   94  CA  LEU A  63      904    778    905     69     43   -222       C  
-ATOM     95  C   LEU A  63      35.017  11.951   5.504  1.00  7.10           C  
-ANISOU   95  C   LEU A  63      931    775    990     53     -5   -271       C  
-ATOM     96  O   LEU A  63      34.647  11.040   6.252  1.00  7.91           O  
-ANISOU   96  O   LEU A  63     1014    903   1085     -4    -28   -172       O  
-ATOM     97  CB  LEU A  63      37.396  11.824   4.813  1.00  7.22           C  
-ANISOU   97  CB  LEU A  63      943    739   1059    109     54   -290       C  
-ATOM     98  CG  LEU A  63      38.828  12.357   4.856  1.00  7.73           C  
-ANISOU   98  CG  LEU A  63      976    923   1038    116     32   -262       C  
-ATOM     99  CD1 LEU A  63      39.771  11.385   4.148  1.00  8.36           C  
-ANISOU   99  CD1 LEU A  63      942   1034   1198    124    181   -250       C  
-ATOM    100  CD2 LEU A  63      38.933  13.737   4.253  1.00  8.58           C  
-ANISOU  100  CD2 LEU A  63     1048   1104   1109    136    157   -380       C  
-ATOM    101  N   PRO A  64      34.242  12.400   4.526  1.00  7.30           N  
-ANISOU  101  N   PRO A  64      878    898    996     37     15   -243       N  
-ATOM    102  CA  PRO A  64      32.886  11.862   4.349  1.00  7.38           C  
-ANISOU  102  CA  PRO A  64      910    874   1018      0     44   -191       C  
-ATOM    103  C   PRO A  64      32.877  10.416   3.868  1.00  7.74           C  
-ANISOU  103  C   PRO A  64      968    851   1122     11     81   -205       C  
-ATOM    104  O   PRO A  64      33.404  10.094   2.797  1.00  8.70           O  
-ANISOU  104  O   PRO A  64     1187    984   1135    -21     85   -296       O  
-ATOM    105  CB  PRO A  64      32.270  12.793   3.299  1.00  8.12           C  
-ANISOU  105  CB  PRO A  64     1011    975   1099     38      3   -211       C  
-ATOM    106  CG  PRO A  64      33.462  13.342   2.535  1.00  7.13           C  
-ANISOU  106  CG  PRO A  64      901    882    923    108    -19   -170       C  
-ATOM    107  CD  PRO A  64      34.540  13.481   3.572  1.00  7.55           C  
-ANISOU  107  CD  PRO A  64      975    909    984     19     39   -240       C  
-ATOM    108  N   SER A  65      32.257   9.546   4.658  1.00  8.35           N  
-ANISOU  108  N   SER A  65     1040    960   1170    -13    147   -170       N  
-ATOM    109  CA  SER A  65      32.130   8.131   4.315  1.00  8.84           C  
-ANISOU  109  CA  SER A  65     1063    976   1317     41    117   -168       C  
-ATOM    110  C   SER A  65      30.817   7.862   3.590  1.00  8.60           C  
-ANISOU  110  C   SER A  65     1095    888   1282     56    135   -174       C  
-ATOM    111  O   SER A  65      29.878   8.664   3.639  1.00  8.27           O  
-ANISOU  111  O   SER A  65     1084    748   1309     52    143   -317       O  
-ATOM    112  CB  SER A  65      32.191   7.250   5.568  1.00  9.54           C  
-ANISOU  112  CB  SER A  65     1118   1109   1394     36    100   -117       C  
-ATOM    113  OG  SER A  65      31.018   7.423   6.342  1.00 10.43           O  
-ANISOU  113  OG  SER A  65     1032   1304   1625    177    169    -41       O  
-ATOM    114  N   GLU A  66      30.748   6.713   2.924  1.00  9.13           N  
-ANISOU  114  N   GLU A  66     1150    896   1421    100    219   -236       N  
-ATOM    115  CA  GLU A  66      29.508   6.316   2.271  1.00 10.14           C  
-ANISOU  115  CA  GLU A  66     1322   1114   1416     20    180   -273       C  
-ATOM    116  C   GLU A  66      28.356   6.255   3.260  1.00  9.39           C  
-ANISOU  116  C   GLU A  66     1243    968   1354    -10    174   -287       C  
-ATOM    117  O   GLU A  66      27.277   6.760   2.981  1.00  9.78           O  
-ANISOU  117  O   GLU A  66     1233   1039   1443    -76    161   -393       O  
-ATOM    118  CB  GLU A  66      29.642   4.957   1.552  1.00 11.33           C  
-ANISOU  118  CB  GLU A  66     1516   1287   1500     47    250   -342       C  
-ATOM    119  CG  GLU A  66      28.306   4.414   1.019  1.00 15.93           C  
-ANISOU  119  CG  GLU A  66     2181   1857   2012    -25    131   -304       C  
-ATOM    120  CD  GLU A  66      28.433   3.123   0.242  1.00 20.49           C  
-ANISOU  120  CD  GLU A  66     2698   2536   2548     23     78   -291       C  
-ATOM    121  OE1 GLU A  66      28.933   2.141   0.821  1.00 23.61           O  
-ANISOU  121  OE1 GLU A  66     3389   2405   3173     62    213   -304       O  
-ATOM    122  OE2 GLU A  66      28.019   3.089  -0.939  1.00 25.25           O  
-ANISOU  122  OE2 GLU A  66     3394   3150   3050    -68    119   -533       O  
-ATOM    123  N   SER A  67      28.585   5.632   4.407  1.00  9.14           N  
-ANISOU  123  N   SER A  67     1199    902   1370     32    172   -273       N  
-ATOM    124  CA  SER A  67      27.500   5.447   5.369  1.00 10.01           C  
-ANISOU  124  CA  SER A  67     1291   1065   1444     45    173   -145       C  
-ATOM    125  C   SER A  67      27.067   6.771   5.976  1.00  8.81           C  
-ANISOU  125  C   SER A  67     1186    902   1256     79    189   -212       C  
-ATOM    126  O   SER A  67      25.882   6.991   6.211  1.00  9.60           O  
-ANISOU  126  O   SER A  67     1155    969   1524     19    204   -237       O  
-ATOM    127  CB  SER A  67      27.874   4.458   6.473  1.00 11.61           C  
-ANISOU  127  CB  SER A  67     1512   1255   1643     68    210    -99       C  
-ATOM    128  OG  SER A  67      28.977   4.872   7.232  1.00 14.26           O  
-ANISOU  128  OG  SER A  67     1889   1507   2023    157    282    -11       O  
-ATOM    129  N   ARG A  68      28.017   7.667   6.221  1.00  8.58           N  
-ANISOU  129  N   ARG A  68     1052    960   1244     56    157   -229       N  
-ATOM    130  CA  ARG A  68      27.693   8.974   6.785  1.00  8.32           C  
-ANISOU  130  CA  ARG A  68     1039    947   1175     48    105   -202       C  
-ATOM    131  C   ARG A  68      26.824   9.757   5.813  1.00  8.01           C  
-ANISOU  131  C   ARG A  68     1022    890   1132     28    105   -216       C  
-ATOM    132  O   ARG A  68      25.796  10.325   6.203  1.00  7.98           O  
-ANISOU  132  O   ARG A  68      872    844   1316     15    198   -303       O  
-ATOM    133  CB  ARG A  68      28.955   9.785   7.107  1.00  8.65           C  
-ANISOU  133  CB  ARG A  68     1069   1018   1196     81     30   -168       C  
-ATOM    134  CG  ARG A  68      28.649  11.128   7.782  1.00  8.97           C  
-ANISOU  134  CG  ARG A  68     1110    907   1392     50    -97   -146       C  
-ATOM    135  CD  ARG A  68      28.366  10.995   9.266  1.00  9.86           C  
-ANISOU  135  CD  ARG A  68     1105   1188   1452    -60    226   -276       C  
-ATOM    136  NE  ARG A  68      29.617  10.789   9.969  1.00  9.23           N  
-ANISOU  136  NE  ARG A  68     1213   1036   1255   -109    225   -175       N  
-ATOM    137  CZ  ARG A  68      30.474  11.757  10.265  1.00  8.88           C  
-ANISOU  137  CZ  ARG A  68     1105   1141   1126   -174    125   -158       C  
-ATOM    138  NH1 ARG A  68      30.148  13.034  10.076  1.00  9.14           N  
-ANISOU  138  NH1 ARG A  68     1127   1073   1272   -131     62   -183       N  
-ATOM    139  NH2 ARG A  68      31.642  11.441  10.803  1.00  9.93           N  
-ANISOU  139  NH2 ARG A  68     1215   1068   1488    -27     36   -227       N  
-ATOM    140  N   ILE A  69      27.229   9.824   4.555  1.00  7.72           N  
-ANISOU  140  N   ILE A  69      885    910   1135      4    115   -207       N  
-ATOM    141  CA  ILE A  69      26.494  10.586   3.566  1.00  7.90           C  
-ANISOU  141  CA  ILE A  69      959    925   1115     37     72   -232       C  
-ATOM    142  C   ILE A  69      25.093  10.004   3.380  1.00  8.35           C  
-ANISOU  142  C   ILE A  69     1007    994   1170     19     23   -233       C  
-ATOM    143  O   ILE A  69      24.116  10.740   3.335  1.00  8.77           O  
-ANISOU  143  O   ILE A  69      989   1068   1272     37    -30   -256       O  
-ATOM    144  CB  ILE A  69      27.280  10.669   2.238  1.00  8.29           C  
-ANISOU  144  CB  ILE A  69     1035    986   1127     77    115   -182       C  
-ATOM    145  CG1 ILE A  69      28.568  11.485   2.415  1.00  8.01           C  
-ANISOU  145  CG1 ILE A  69      952    904   1187    184    213   -180       C  
-ATOM    146  CG2 ILE A  69      26.414  11.244   1.119  1.00  9.03           C  
-ANISOU  146  CG2 ILE A  69     1110   1183   1137     45    155   -331       C  
-ATOM    147  CD1 ILE A  69      28.371  12.938   2.863  1.00  8.71           C  
-ANISOU  147  CD1 ILE A  69     1037   1033   1238     55    266   -114       C  
-ATOM    148  N   GLN A  70      24.978   8.687   3.301  1.00  9.03           N  
-ANISOU  148  N   GLN A  70     1023   1088   1319    -11     57   -267       N  
-ATOM    149  CA  GLN A  70      23.663   8.065   3.154  1.00  9.97           C  
-ANISOU  149  CA  GLN A  70     1134   1229   1422    -84     36   -257       C  
-ATOM    150  C   GLN A  70      22.760   8.408   4.337  1.00  9.86           C  
-ANISOU  150  C   GLN A  70     1054   1190   1500    -57     46   -275       C  
-ATOM    151  O   GLN A  70      21.590   8.713   4.159  1.00 10.39           O  
-ANISOU  151  O   GLN A  70      953   1295   1697    -79    -36   -383       O  
-ATOM    152  CB  GLN A  70      23.802   6.548   3.000  1.00 11.39           C  
-ANISOU  152  CB  GLN A  70     1280   1362   1685    -84     87   -323       C  
-ATOM    153  CG  GLN A  70      24.345   6.122   1.634  1.00 15.15           C  
-ANISOU  153  CG  GLN A  70     1770   1919   2066    -29     81   -381       C  
-ATOM    154  CD  GLN A  70      24.586   4.613   1.506  1.00 19.50           C  
-ANISOU  154  CD  GLN A  70     2491   2463   2452     25    124   -470       C  
-ATOM    155  OE1 GLN A  70      24.649   4.085   0.390  1.00 25.55           O  
-ANISOU  155  OE1 GLN A  70     3245   3184   3279     -6    196   -531       O  
-ATOM    156  NE2 GLN A  70      24.751   3.927   2.639  1.00 21.99           N  
-ANISOU  156  NE2 GLN A  70     2791   2398   3164    107    233   -469       N  
-ATOM    157  N   SER A  71      23.313   8.370   5.539  1.00  9.16           N  
-ANISOU  157  N   SER A  71     1011   1038   1428    -29    128   -209       N  
-ATOM    158  CA  SER A  71      22.538   8.672   6.737  1.00  9.41           C  
-ANISOU  158  CA  SER A  71     1085   1087   1401   -121    143   -168       C  
-ATOM    159  C   SER A  71      22.139  10.142   6.811  1.00  8.82           C  
-ANISOU  159  C   SER A  71      972   1048   1328    -68    153   -190       C  
-ATOM    160  O   SER A  71      21.038  10.469   7.249  1.00  9.42           O  
-ANISOU  160  O   SER A  71      864   1183   1533   -135    238   -254       O  
-ATOM    161  CB  SER A  71      23.330   8.303   7.980  1.00 10.04           C  
-ANISOU  161  CB  SER A  71     1320   1116   1378    -43    252   -113       C  
-ATOM    162  OG  SER A  71      23.470   6.912   8.117  1.00 14.22           O  
-ANISOU  162  OG  SER A  71     1888   1464   2049    -85    255    -11       O  
-ATOM    163  N   LEU A  72      23.025  11.035   6.393  1.00  7.98           N  
-ANISOU  163  N   LEU A  72      853    960   1218    -38    152   -203       N  
-ATOM    164  CA  LEU A  72      22.700  12.454   6.385  1.00  7.91           C  
-ANISOU  164  CA  LEU A  72      876    981   1146     13    111   -173       C  
-ATOM    165  C   LEU A  72      21.559  12.750   5.425  1.00  8.47           C  
-ANISOU  165  C   LEU A  72      940   1035   1241     20     65   -209       C  
-ATOM    166  O   LEU A  72      20.677  13.537   5.738  1.00  9.08           O  
-ANISOU  166  O   LEU A  72      859   1217   1372    134     55   -196       O  
-ATOM    167  CB  LEU A  72      23.937  13.291   6.066  1.00  7.31           C  
-ANISOU  167  CB  LEU A  72      877    883   1017     -7    164   -205       C  
-ATOM    168  CG  LEU A  72      24.961  13.356   7.203  1.00  7.27           C  
-ANISOU  168  CG  LEU A  72      782    970   1010     81    147   -122       C  
-ATOM    169  CD1 LEU A  72      26.247  13.996   6.730  1.00  7.32           C  
-ANISOU  169  CD1 LEU A  72      919    833   1030     -2     79   -179       C  
-ATOM    170  CD2 LEU A  72      24.421  14.102   8.419  1.00  7.53           C  
-ANISOU  170  CD2 LEU A  72      963    910    985     26    119    -72       C  
-ATOM    171  N   HIS A  73      21.531  12.080   4.287  1.00  9.11           N  
-ANISOU  171  N   HIS A  73      936   1192   1333     26     18   -163       N  
-ATOM    172  CA  HIS A  73      20.392  12.239   3.387  1.00 10.66           C  
-ANISOU  172  CA  HIS A  73     1139   1424   1487     -5    -56   -122       C  
-ATOM    173  C   HIS A  73      19.112  11.631   3.938  1.00 11.06           C  
-ANISOU  173  C   HIS A  73     1124   1461   1617    -29    -60   -150       C  
-ATOM    174  O   HIS A  73      18.081  12.290   3.955  1.00 11.72           O  
-ANISOU  174  O   HIS A  73     1038   1612   1801     16   -126   -182       O  
-ATOM    175  CB  HIS A  73      20.711  11.686   2.016  1.00 11.39           C  
-ANISOU  175  CB  HIS A  73     1278   1573   1474     15   -116   -152       C  
-ATOM    176  CG  HIS A  73      21.579  12.598   1.224  1.00 12.21           C  
-ANISOU  176  CG  HIS A  73     1297   1759   1583     83    -91   -101       C  
-ATOM    177  ND1 HIS A  73      21.077  13.656   0.500  1.00 15.54           N  
-ANISOU  177  ND1 HIS A  73     1835   2168   1901     71    -88     36       N  
-ATOM    178  CD2 HIS A  73      22.925  12.688   1.132  1.00 15.34           C  
-ANISOU  178  CD2 HIS A  73     1519   2398   1910    175     72    141       C  
-ATOM    179  CE1 HIS A  73      22.073  14.308  -0.072  1.00 15.27           C  
-ANISOU  179  CE1 HIS A  73     1888   2106   1807     10    -22     14       C  
-ATOM    180  NE2 HIS A  73      23.205  13.744   0.302  1.00 16.00           N  
-ANISOU  180  NE2 HIS A  73     1822   2420   1836     84     45    153       N  
-ATOM    181  N   LYS A  74      19.190  10.402   4.427  1.00 11.31           N  
-ANISOU  181  N   LYS A  74     1086   1464   1744   -141     37   -145       N  
-ATOM    182  CA  LYS A  74      17.993   9.689   4.878  1.00 12.24           C  
-ANISOU  182  CA  LYS A  74     1281   1570   1798   -131     34   -130       C  
-ATOM    183  C   LYS A  74      17.318  10.385   6.052  1.00 11.98           C  
-ANISOU  183  C   LYS A  74     1172   1529   1848   -100     83   -160       C  
-ATOM    184  O   LYS A  74      16.084  10.418   6.144  1.00 13.11           O  
-ANISOU  184  O   LYS A  74     1020   1757   2203   -117    191   -314       O  
-ATOM    185  CB  LYS A  74      18.335   8.242   5.246  1.00 12.91           C  
-ANISOU  185  CB  LYS A  74     1394   1611   1897   -128     80   -145       C  
-ATOM    186  CG  LYS A  74      17.127   7.395   5.620  1.00 17.37           C  
-ANISOU  186  CG  LYS A  74     2012   2135   2451    -95     49   -125       C  
-ATOM    187  CD  LYS A  74      16.113   7.287   4.476  1.00 22.78           C  
-ANISOU  187  CD  LYS A  74     2845   2894   2915    -59     13     -2       C  
-ATOM    188  CE  LYS A  74      15.121   6.149   4.706  1.00 25.42           C  
-ANISOU  188  CE  LYS A  74     3239   3197   3222    -16    -12    -16       C  
-ATOM    189  NZ  LYS A  74      14.309   5.856   3.497  1.00 28.28           N  
-ANISOU  189  NZ  LYS A  74     3542   3603   3599     90    -46    -41       N  
-ATOM    190  N   SER A  75      18.123  10.938   6.951  1.00 11.07           N  
-ANISOU  190  N   SER A  75     1081   1438   1684    -70    112   -125       N  
-ATOM    191  CA  SER A  75      17.621  11.627   8.128  1.00 11.13           C  
-ANISOU  191  CA  SER A  75     1189   1414   1626    -39    151    -80       C  
-ATOM    192  C   SER A  75      16.975  12.967   7.807  1.00 10.90           C  
-ANISOU  192  C   SER A  75     1076   1392   1673     -5    105   -108       C  
-ATOM    193  O   SER A  75      16.318  13.538   8.663  1.00 12.48           O  
-ANISOU  193  O   SER A  75     1197   1598   1946     39    338   -156       O  
-ATOM    194  CB  SER A  75      18.750  11.878   9.116  1.00 11.16           C  
-ANISOU  194  CB  SER A  75     1209   1384   1648     -4    177   -128       C  
-ATOM    195  OG  SER A  75      19.719  12.744   8.551  1.00 10.33           O  
-ANISOU  195  OG  SER A  75      905   1328   1690    -29    182   -231       O  
-ATOM    196  N   GLY A  76      17.193  13.497   6.610  1.00 10.13           N  
-ANISOU  196  N   GLY A  76      972   1323   1554    -52     19   -131       N  
-ATOM    197  CA  GLY A  76      16.750  14.833   6.275  1.00 10.10           C  
-ANISOU  197  CA  GLY A  76     1028   1288   1520    -39     -5    -61       C  
-ATOM    198  C   GLY A  76      17.766  15.916   6.584  1.00  9.05           C  
-ANISOU  198  C   GLY A  76      888   1173   1375     28    -63    -43       C  
-ATOM    199  O   GLY A  76      17.565  17.064   6.193  1.00 10.10           O  
-ANISOU  199  O   GLY A  76      853   1280   1704      0   -135    -27       O  
-ATOM    200  N   LEU A  77      18.864  15.570   7.261  1.00  8.52           N  
-ANISOU  200  N   LEU A  77      816   1084   1337      3     31    -14       N  
-ATOM    201  CA  LEU A  77      19.818  16.590   7.668  1.00  8.03           C  
-ANISOU  201  CA  LEU A  77      840   1095   1114    -46    -15    -25       C  
-ATOM    202  C   LEU A  77      20.554  17.221   6.488  1.00  7.21           C  
-ANISOU  202  C   LEU A  77      685   1031   1022     39    -18    -62       C  
-ATOM    203  O   LEU A  77      20.877  18.401   6.541  1.00  7.89           O  
-ANISOU  203  O   LEU A  77      765   1107   1124    -38    -36     -9       O  
-ATOM    204  CB  LEU A  77      20.815  16.020   8.660  1.00  8.06           C  
-ANISOU  204  CB  LEU A  77      843   1116   1101    -58     -1      2       C  
-ATOM    205  CG  LEU A  77      20.235  15.696  10.031  1.00  9.09           C  
-ANISOU  205  CG  LEU A  77      935   1227   1289    -72     86    -57       C  
-ATOM    206  CD1 LEU A  77      21.234  14.940  10.837  1.00 10.45           C  
-ANISOU  206  CD1 LEU A  77     1064   1530   1375    -90    -37    175       C  
-ATOM    207  CD2 LEU A  77      19.791  16.934  10.762  1.00 11.72           C  
-ANISOU  207  CD2 LEU A  77     1549   1543   1360   -101    164    -19       C  
-ATOM    208  N   ALA A  78      20.808  16.462   5.424  1.00  7.83           N  
-ANISOU  208  N   ALA A  78      817   1066   1090     -6    -12    -88       N  
-ATOM    209  CA  ALA A  78      21.581  16.968   4.295  1.00  8.47           C  
-ANISOU  209  CA  ALA A  78      916   1187   1113     -6    -13    -75       C  
-ATOM    210  C   ALA A  78      20.884  18.141   3.614  1.00  8.53           C  
-ANISOU  210  C   ALA A  78      876   1196   1167    -54    -61    -41       C  
-ATOM    211  O   ALA A  78      21.533  19.032   3.088  1.00  9.36           O  
-ANISOU  211  O   ALA A  78      961   1353   1239     45   -147     73       O  
-ATOM    212  CB  ALA A  78      21.839  15.872   3.289  1.00  9.03           C  
-ANISOU  212  CB  ALA A  78     1073   1185   1173    -42     50    -92       C  
-ATOM    213  N   ALA A  79      19.550  18.145   3.630  1.00  9.47           N  
-ANISOU  213  N   ALA A  79      963   1316   1318     13   -138     -8       N  
-ATOM    214  CA  ALA A  79      18.752  19.184   2.970  1.00 10.09           C  
-ANISOU  214  CA  ALA A  79     1107   1387   1338     12   -181    -27       C  
-ATOM    215  C   ALA A  79      18.653  20.471   3.783  1.00  9.92           C  
-ANISOU  215  C   ALA A  79     1024   1407   1337     97   -207     -8       C  
-ATOM    216  O   ALA A  79      18.143  21.473   3.292  1.00 11.33           O  
-ANISOU  216  O   ALA A  79     1244   1529   1528    239   -471    -36       O  
-ATOM    217  CB  ALA A  79      17.360  18.646   2.708  1.00 10.82           C  
-ANISOU  217  CB  ALA A  79     1159   1487   1465      3   -228    -80       C  
-ATOM    218  N   GLN A  80      19.116  20.441   5.033  1.00  9.26           N  
-ANISOU  218  N   GLN A  80      919   1321   1277     88   -152    -99       N  
-ATOM    219  CA  GLN A  80      19.085  21.596   5.919  1.00  9.29           C  
-ANISOU  219  CA  GLN A  80      932   1331   1265     96    -60    -96       C  
-ATOM    220  C   GLN A  80      20.326  22.465   5.664  1.00  9.11           C  
-ANISOU  220  C   GLN A  80      898   1340   1223    144    -36   -101       C  
-ATOM    221  O   GLN A  80      20.956  22.333   4.625  1.00  9.99           O  
-ANISOU  221  O   GLN A  80     1023   1631   1142      8    -77   -160       O  
-ATOM    222  CB  GLN A  80      18.933  21.118   7.359  1.00  9.29           C  
-ANISOU  222  CB  GLN A  80      872   1338   1316    124    -29   -168       C  
-ATOM    223  CG  GLN A  80      17.629  20.324   7.551  1.00 10.26           C  
-ANISOU  223  CG  GLN A  80      959   1496   1443     62    -53    -93       C  
-ATOM    224  CD  GLN A  80      17.451  19.716   8.934  1.00 12.16           C  
-ANISOU  224  CD  GLN A  80      827   2060   1732    -70    -84   -122       C  
-ATOM    225  OE1 GLN A  80      18.187  20.005   9.855  1.00 12.95           O  
-ANISOU  225  OE1 GLN A  80      904   2186   1830   -402   -133     92       O  
-ATOM    226  NE2 GLN A  80      16.436  18.870   9.074  1.00 15.56           N  
-ANISOU  226  NE2 GLN A  80     1320   2324   2268   -571    -11   -295       N  
-ATOM    227  N   GLU A  81      20.643  23.377   6.573  1.00  8.73           N  
-ANISOU  227  N   GLU A  81      874   1267   1176    127    -36    -73       N  
-ATOM    228  CA  GLU A  81      21.690  24.368   6.333  1.00  8.29           C  
-ANISOU  228  CA  GLU A  81      841   1119   1188    179    -72     -5       C  
-ATOM    229  C   GLU A  81      23.011  23.942   6.965  1.00  6.84           C  
-ANISOU  229  C   GLU A  81      727    896    975    150    -41    -38       C  
-ATOM    230  O   GLU A  81      23.063  23.575   8.143  1.00  6.87           O  
-ANISOU  230  O   GLU A  81      651    964    996    109      1    -78       O  
-ATOM    231  CB  GLU A  81      21.292  25.723   6.915  1.00  9.67           C  
-ANISOU  231  CB  GLU A  81      961   1236   1475    198    -21      7       C  
-ATOM    232  CG  GLU A  81      20.281  26.580   6.168  1.00 13.76           C  
-ANISOU  232  CG  GLU A  81     1438   1782   2008    177   -116     14       C  
-ATOM    233  CD  GLU A  81      20.492  28.042   6.545  1.00 16.85           C  
-ANISOU  233  CD  GLU A  81     2287   1915   2198    278    -58     70       C  
-ATOM    234  OE1 GLU A  81      21.004  28.826   5.719  1.00 18.18           O  
-ANISOU  234  OE1 GLU A  81     2294   1824   2790    334   -325    -34       O  
-ATOM    235  OE2 GLU A  81      20.210  28.388   7.713  1.00 19.24           O  
-ANISOU  235  OE2 GLU A  81     2620   2215   2476     52   -256    -91       O  
-ATOM    236  N   TRP A  82      24.055  24.069   6.162  1.00  6.78           N  
-ANISOU  236  N   TRP A  82      760    921    893    135    -52     39       N  
-ATOM    237  CA  TRP A  82      25.428  23.727   6.498  1.00  5.64           C  
-ANISOU  237  CA  TRP A  82      657    743    740    114    -92     -8       C  
-ATOM    238  C   TRP A  82      26.323  24.892   6.106  1.00  5.61           C  
-ANISOU  238  C   TRP A  82      721    677    732     96    -87    -28       C  
-ATOM    239  O   TRP A  82      25.987  25.707   5.245  1.00  6.42           O  
-ANISOU  239  O   TRP A  82      772    824    842     91   -149     24       O  
-ATOM    240  CB  TRP A  82      25.861  22.476   5.715  1.00  6.41           C  
-ANISOU  240  CB  TRP A  82      760    795    880     74    -36      0       C  
-ATOM    241  CG  TRP A  82      25.084  21.243   6.054  1.00  6.10           C  
-ANISOU  241  CG  TRP A  82      720    664    931     55    -87   -108       C  
-ATOM    242  CD1 TRP A  82      23.780  20.996   5.757  1.00  6.25           C  
-ANISOU  242  CD1 TRP A  82      618    758    997    116   -177   -159       C  
-ATOM    243  CD2 TRP A  82      25.558  20.090   6.748  1.00  5.81           C  
-ANISOU  243  CD2 TRP A  82      585    740    881     33   -113   -165       C  
-ATOM    244  NE1 TRP A  82      23.407  19.771   6.247  1.00  6.29           N  
-ANISOU  244  NE1 TRP A  82      616    689   1084    -16   -157   -119       N  
-ATOM    245  CE2 TRP A  82      24.477  19.195   6.865  1.00  6.66           C  
-ANISOU  245  CE2 TRP A  82      806    715   1006     15    -42   -191       C  
-ATOM    246  CE3 TRP A  82      26.794  19.722   7.294  1.00  6.08           C  
-ANISOU  246  CE3 TRP A  82      786    598    925    -41    -13   -162       C  
-ATOM    247  CZ2 TRP A  82      24.599  17.961   7.483  1.00  7.04           C  
-ANISOU  247  CZ2 TRP A  82      707    836   1132    -38    -14   -173       C  
-ATOM    248  CZ3 TRP A  82      26.914  18.497   7.903  1.00  6.38           C  
-ANISOU  248  CZ3 TRP A  82      818    792    813     61   -142    -89       C  
-ATOM    249  CH2 TRP A  82      25.832  17.632   7.997  1.00  7.28           C  
-ANISOU  249  CH2 TRP A  82      945    799   1020    -11    -83   -149       C  
-ATOM    250  N   VAL A  83      27.495  24.938   6.725  1.00  5.50           N  
-ANISOU  250  N   VAL A  83      665    673    749     66    -65     13       N  
-ATOM    251  CA  VAL A  83      28.558  25.853   6.334  1.00  5.35           C  
-ANISOU  251  CA  VAL A  83      696    631    705     69    -79    -53       C  
-ATOM    252  C   VAL A  83      29.852  25.080   6.127  1.00  5.46           C  
-ANISOU  252  C   VAL A  83      716    650    706     92    -81      8       C  
-ATOM    253  O   VAL A  83      30.092  24.049   6.745  1.00  6.18           O  
-ANISOU  253  O   VAL A  83      768    727    852     93     43    117       O  
-ATOM    254  CB  VAL A  83      28.792  26.978   7.383  1.00  5.76           C  
-ANISOU  254  CB  VAL A  83      735    662    788     58    -39    -95       C  
-ATOM    255  CG1 VAL A  83      27.590  27.932   7.390  1.00  6.61           C  
-ANISOU  255  CG1 VAL A  83      941    773    794     79    -39   -135       C  
-ATOM    256  CG2 VAL A  83      29.071  26.406   8.787  1.00  6.54           C  
-ANISOU  256  CG2 VAL A  83      887    818    780     69    -36   -168       C  
-ATOM    257  N   ALA A  84      30.707  25.624   5.272  1.00  5.43           N  
-ANISOU  257  N   ALA A  84      692    683    687     65    -39     45       N  
-ATOM    258  CA  ALA A  84      32.110  25.240   5.201  1.00  5.06           C  
-ANISOU  258  CA  ALA A  84      614    693    615     92    -26     35       C  
-ATOM    259  C   ALA A  84      32.946  26.392   5.715  1.00  5.11           C  
-ANISOU  259  C   ALA A  84      646    588    705    138     35     21       C  
-ATOM    260  O   ALA A  84      32.764  27.514   5.253  1.00  5.97           O  
-ANISOU  260  O   ALA A  84      801    619    845     87   -127     82       O  
-ATOM    261  CB  ALA A  84      32.527  24.920   3.791  1.00  6.31           C  
-ANISOU  261  CB  ALA A  84      880    760    757     73      0    -17       C  
-ATOM    262  N   CYS A  85      33.852  26.124   6.654  1.00  4.78           N  
-ANISOU  262  N   CYS A  85      661    567    587     84    -13    -15       N  
-ATOM    263  CA  CYS A  85      34.795  27.114   7.154  1.00  4.73           C  
-ANISOU  263  CA  CYS A  85      631    587    578     63     76     12       C  
-ATOM    264  C   CYS A  85      36.205  26.576   6.987  1.00  4.63           C  
-ANISOU  264  C   CYS A  85      641    575    542     51     33    -21       C  
-ATOM    265  O   CYS A  85      36.421  25.390   6.800  1.00  4.76           O  
-ANISOU  265  O   CYS A  85      673    498    637     81     83    -13       O  
-ATOM    266  CB  CYS A  85      34.535  27.427   8.627  1.00  5.52           C  
-ANISOU  266  CB  CYS A  85      751    705    641     81    115    -47       C  
-ATOM    267  SG  CYS A  85      32.869  28.017   9.012  1.00  7.11           S  
-ANISOU  267  SG  CYS A  85      893    934    871    225    141    -45       S  
-ATOM    268  N   GLU A  86      37.190  27.455   7.078  1.00  4.62           N  
-ANISOU  268  N   GLU A  86      605    473    676     15     22    -20       N  
-ATOM    269  CA  GLU A  86      38.571  27.044   6.878  1.00  4.45           C  
-ANISOU  269  CA  GLU A  86      630    558    502    -11     35     36       C  
-ATOM    270  C   GLU A  86      39.020  26.076   7.969  1.00  4.37           C  
-ANISOU  270  C   GLU A  86      609    540    511     -6     46     11       C  
-ATOM    271  O   GLU A  86      38.754  26.297   9.154  1.00  4.85           O  
-ANISOU  271  O   GLU A  86      800    565    476     61     36     21       O  
-ATOM    272  CB  GLU A  86      39.465  28.281   6.845  1.00  5.19           C  
-ANISOU  272  CB  GLU A  86      731    632    606    -46     22     85       C  
-ATOM    273  CG  GLU A  86      40.931  27.959   6.607  1.00  4.98           C  
-ANISOU  273  CG  GLU A  86      687    627    578   -139     48     -4       C  
-ATOM    274  CD  GLU A  86      41.812  29.159   6.344  1.00  6.64           C  
-ANISOU  274  CD  GLU A  86      815    736    971    -14    -16      2       C  
-ATOM    275  OE1 GLU A  86      41.342  30.314   6.471  1.00  7.94           O  
-ANISOU  275  OE1 GLU A  86      992    736   1286   -127     99     42       O  
-ATOM    276  OE2 GLU A  86      43.012  28.933   6.041  1.00  6.62           O  
-ANISOU  276  OE2 GLU A  86      802    752    959   -115     84    134       O  
-ATOM    277  N   LYS A  87      39.723  25.026   7.552  1.00  3.83           N  
-ANISOU  277  N   LYS A  87      601    433    419     67     40     -9       N  
-ATOM    278  CA  LYS A  87      40.425  24.140   8.472  1.00  3.94           C  
-ANISOU  278  CA  LYS A  87      568    448    478     18     44      8       C  
-ATOM    279  C   LYS A  87      41.850  24.659   8.607  1.00  3.95           C  
-ANISOU  279  C   LYS A  87      554    466    479     23     86    -50       C  
-ATOM    280  O   LYS A  87      42.583  24.714   7.619  1.00  4.64           O  
-ANISOU  280  O   LYS A  87      637    663    460     -4    107   -168       O  
-ATOM    281  CB  LYS A  87      40.406  22.700   7.983  1.00  4.21           C  
-ANISOU  281  CB  LYS A  87      503    526    571    -14    -38     17       C  
-ATOM    282  CG  LYS A  87      40.812  21.716   9.060  1.00  4.82           C  
-ANISOU  282  CG  LYS A  87      656    466    707     53     35    -35       C  
-ATOM    283  CD  LYS A  87      40.599  20.285   8.636  1.00  5.64           C  
-ANISOU  283  CD  LYS A  87      798    543    801     87   -121    -54       C  
-ATOM    284  CE  LYS A  87      40.745  19.292   9.788  1.00  6.04           C  
-ANISOU  284  CE  LYS A  87     1018    427    849    -43    -53    -93       C  
-ATOM    285  NZ  LYS A  87      42.137  19.250  10.300  1.00  6.11           N  
-ANISOU  285  NZ  LYS A  87      888    654    777    170    -43     52       N  
-ATOM    286  N   VAL A  88      42.191  25.106   9.813  1.00  4.11           N  
-ANISOU  286  N   VAL A  88      507    540    514    -46     71    -40       N  
-ATOM    287  CA  VAL A  88      43.484  25.722  10.086  1.00  4.45           C  
-ANISOU  287  CA  VAL A  88      580    547    560    -10     47    -50       C  
-ATOM    288  C   VAL A  88      44.463  24.675  10.618  1.00  3.93           C  
-ANISOU  288  C   VAL A  88      483    537    472    -80     75    -27       C  
-ATOM    289  O   VAL A  88      44.131  23.888  11.506  1.00  4.74           O  
-ANISOU  289  O   VAL A  88      592    592    614    -58     57      6       O  
-ATOM    290  CB  VAL A  88      43.302  26.914  11.068  1.00  4.47           C  
-ANISOU  290  CB  VAL A  88      578    576    542     12     82    -79       C  
-ATOM    291  CG1 VAL A  88      44.644  27.493  11.514  1.00  5.48           C  
-ANISOU  291  CG1 VAL A  88      725    675    681     -4     -7    -89       C  
-ATOM    292  CG2 VAL A  88      42.459  27.975  10.373  1.00  5.25           C  
-ANISOU  292  CG2 VAL A  88      749    608    637    -15     99   -120       C  
-ATOM    293  N   HIS A  89      45.670  24.687  10.054  1.00  4.36           N  
-ANISOU  293  N   HIS A  89      571    532    553    -29      8     -8       N  
-ATOM    294  CA  HIS A  89      46.730  23.760  10.416  1.00  4.44           C  
-ANISOU  294  CA  HIS A  89      528    573    584     46     59    -93       C  
-ATOM    295  C   HIS A  89      47.626  24.352  11.490  1.00  4.47           C  
-ANISOU  295  C   HIS A  89      555    534    610     36     19   -110       C  
-ATOM    296  O   HIS A  89      48.645  24.992  11.200  1.00  5.45           O  
-ANISOU  296  O   HIS A  89      578    818    674   -134     60    -59       O  
-ATOM    297  CB  HIS A  89      47.539  23.442   9.194  1.00  5.39           C  
-ANISOU  297  CB  HIS A  89      625    734    686      7    -29    -72       C  
-ATOM    298  CG  HIS A  89      48.572  22.385   9.383  1.00  5.84           C  
-ANISOU  298  CG  HIS A  89      683    822    713     77    153    -58       C  
-ATOM    299  ND1 HIS A  89      48.273  21.121   9.793  1.00  7.90           N  
-ANISOU  299  ND1 HIS A  89      803    944   1254    199    139     20       N  
-ATOM    300  CD2 HIS A  89      49.912  22.427   9.275  1.00  9.92           C  
-ANISOU  300  CD2 HIS A  89      910    824   2033     33    230     73       C  
-ATOM    301  CE1 HIS A  89      49.367  20.386   9.781  1.00  7.28           C  
-ANISOU  301  CE1 HIS A  89      772    763   1230    171    290     -8       C  
-ATOM    302  NE2 HIS A  89      50.363  21.139   9.389  1.00  7.99           N  
-ANISOU  302  NE2 HIS A  89      863   1003   1169    162    -39   -133       N  
-ATOM    303  N   GLY A  90      47.212  24.171  12.734  1.00  4.84           N  
-ANISOU  303  N   GLY A  90      553    636    650    -38     69    -75       N  
-ATOM    304  CA  GLY A  90      47.977  24.569  13.905  1.00  4.82           C  
-ANISOU  304  CA  GLY A  90      618    568    643     42     67    -55       C  
-ATOM    305  C   GLY A  90      47.968  23.416  14.884  1.00  4.31           C  
-ANISOU  305  C   GLY A  90      547    528    562      8     57    -34       C  
-ATOM    306  O   GLY A  90      48.231  22.268  14.522  1.00  5.30           O  
-ANISOU  306  O   GLY A  90      757    559    695    113    100   -108       O  
-ATOM    307  N   THR A  91      47.650  23.727  16.133  1.00  4.47           N  
-ANISOU  307  N   THR A  91      599    533    564     44     29    -13       N  
-ATOM    308  CA  THR A  91      47.488  22.698  17.144  1.00  5.08           C  
-ANISOU  308  CA  THR A  91      728    552    648     84     71     14       C  
-ATOM    309  C   THR A  91      46.227  23.006  17.947  1.00  4.89           C  
-ANISOU  309  C   THR A  91      691    446    720     54     65     39       C  
-ATOM    310  O   THR A  91      45.848  24.161  18.123  1.00  4.88           O  
-ANISOU  310  O   THR A  91      709    436    707     85     41     53       O  
-ATOM    311  CB  THR A  91      48.776  22.587  17.981  1.00  5.80           C  
-ANISOU  311  CB  THR A  91      754    752    696    103     64     87       C  
-ATOM    312  OG1 THR A  91      48.738  21.401  18.776  1.00  7.22           O  
-ANISOU  312  OG1 THR A  91      846   1011    885    136     13    332       O  
-ATOM    313  CG2 THR A  91      48.947  23.756  18.929  1.00  7.35           C  
-ANISOU  313  CG2 THR A  91      954   1070    768    148    -66     42       C  
-ATOM    314  N   ASN A  92      45.560  21.960  18.391  1.00  4.91           N  
-ANISOU  314  N   ASN A  92      734    470    662     72     86    -18       N  
-ATOM    315  CA  ASN A  92      44.301  22.113  19.093  1.00  5.14           C  
-ANISOU  315  CA  ASN A  92      700    552    700     56     55     -2       C  
-ATOM    316  C   ASN A  92      44.489  22.853  20.414  1.00  4.84           C  
-ANISOU  316  C   ASN A  92      678    526    635    127     40     52       C  
-ATOM    317  O   ASN A  92      45.438  22.578  21.157  1.00  5.79           O  
-ANISOU  317  O   ASN A  92      832    654    714    211      7   -103       O  
-ATOM    318  CB  ASN A  92      43.702  20.727  19.353  1.00  5.44           C  
-ANISOU  318  CB  ASN A  92      772    533    761      0      5    -12       C  
-ATOM    319  CG  ASN A  92      42.298  20.794  19.874  1.00  6.04           C  
-ANISOU  319  CG  ASN A  92      868    686    738    -32    120    -38       C  
-ATOM    320  OD1 ASN A  92      42.067  20.782  21.077  1.00  9.32           O  
-ANISOU  320  OD1 ASN A  92      946   1827    766   -149     64   -114       O  
-ATOM    321  ND2 ASN A  92      41.350  20.907  18.972  1.00  6.71           N  
-ANISOU  321  ND2 ASN A  92      808    944    796    -44    -40     39       N  
-ATOM    322  N   PHE A  93      43.585  23.765  20.710  1.00  5.58           N  
-ANISOU  322  N   PHE A  93      811    681    628    196    -43    -54       N  
-ATOM    323  CA  PHE A  93      43.744  24.595  21.888  1.00  6.28           C  
-ANISOU  323  CA  PHE A  93      963    834    588    201    -12      6       C  
-ATOM    324  C   PHE A  93      42.372  24.872  22.491  1.00  6.64           C  
-ANISOU  324  C   PHE A  93      916   1054    553    354   -124    -30       C  
-ATOM    325  O   PHE A  93      41.336  24.938  21.797  1.00 11.84           O  
-ANISOU  325  O   PHE A  93     1389   2306    801    800     -6   -159       O  
-ATOM    326  CB  PHE A  93      44.514  25.854  21.484  1.00  6.74           C  
-ANISOU  326  CB  PHE A  93     1181    717    662    181     14     60       C  
-ATOM    327  CG  PHE A  93      45.044  26.656  22.642  1.00  6.65           C  
-ANISOU  327  CG  PHE A  93     1039    811    674    144    -33    107       C  
-ATOM    328  CD1 PHE A  93      46.235  26.319  23.260  1.00  8.52           C  
-ANISOU  328  CD1 PHE A  93     1077    981   1177    179     61    127       C  
-ATOM    329  CD2 PHE A  93      44.360  27.767  23.113  1.00  6.80           C  
-ANISOU  329  CD2 PHE A  93     1017    848    718     58    -75   -100       C  
-ATOM    330  CE1 PHE A  93      46.720  27.067  24.325  1.00  9.10           C  
-ANISOU  330  CE1 PHE A  93      986   1179   1293    -19   -240    428       C  
-ATOM    331  CE2 PHE A  93      44.847  28.519  24.178  1.00  8.18           C  
-ANISOU  331  CE2 PHE A  93     1112    990   1005    -40   -108    -19       C  
-ATOM    332  CZ  PHE A  93      46.031  28.162  24.776  1.00  8.89           C  
-ANISOU  332  CZ  PHE A  93     1195   1203    977    -71   -209     59       C  
-ATOM    333  N   GLY A  94      42.300  24.959  23.791  1.00  5.27           N  
-ANISOU  333  N   GLY A  94      761    787    454    128    -38     -5       N  
-ATOM    334  CA  GLY A  94      41.063  25.306  24.447  1.00  5.53           C  
-ANISOU  334  CA  GLY A  94      839    735    525    136     54    -41       C  
-ATOM    335  C   GLY A  94      41.307  26.336  25.528  1.00  5.32           C  
-ANISOU  335  C   GLY A  94      832    726    463    157     -4     27       C  
-ATOM    336  O   GLY A  94      42.275  26.237  26.289  1.00  6.37           O  
-ANISOU  336  O   GLY A  94     1012    887    520    314   -108    -22       O  
-ATOM    337  N   ILE A  95      40.417  27.313  25.600  1.00  5.38           N  
-ANISOU  337  N   ILE A  95      831    743    470    215    -16    -45       N  
-ATOM    338  CA  ILE A  95      40.413  28.316  26.652  1.00  5.67           C  
-ANISOU  338  CA  ILE A  95      878    759    514    144    -31    -49       C  
-ATOM    339  C   ILE A  95      39.185  28.061  27.513  1.00  6.00           C  
-ANISOU  339  C   ILE A  95      908    870    501    185     32   -118       C  
-ATOM    340  O   ILE A  95      38.057  28.034  27.030  1.00  6.51           O  
-ANISOU  340  O   ILE A  95      971    982    520    142     57    -87       O  
-ATOM    341  CB  ILE A  95      40.343  29.725  26.042  1.00  6.28           C  
-ANISOU  341  CB  ILE A  95      912    740    734    156    -36    -83       C  
-ATOM    342  CG1 ILE A  95      41.534  29.973  25.112  1.00  7.15           C  
-ANISOU  342  CG1 ILE A  95     1059    887    768    105     -5    -58       C  
-ATOM    343  CG2 ILE A  95      40.270  30.771  27.132  1.00  7.90           C  
-ANISOU  343  CG2 ILE A  95     1078    921   1003    146     51    -35       C  
-ATOM    344  CD1 ILE A  95      41.367  31.118  24.145  1.00  8.23           C  
-ANISOU  344  CD1 ILE A  95     1155   1027    945    -26    -29    -41       C  
-ATOM    345  N   TYR A  96      39.433  27.859  28.798  1.00  6.44           N  
-ANISOU  345  N   TYR A  96     1054    884    506     73      7    -16       N  
-ATOM    346  CA  TYR A  96      38.417  27.482  29.757  1.00  7.18           C  
-ANISOU  346  CA  TYR A  96     1004   1052    671     95      9    -50       C  
-ATOM    347  C   TYR A  96      38.202  28.577  30.791  1.00  7.54           C  
-ANISOU  347  C   TYR A  96     1138   1140    585    126    -20    -59       C  
-ATOM    348  O   TYR A  96      39.158  29.130  31.312  1.00  8.77           O  
-ANISOU  348  O   TYR A  96     1302   1394    634    165     23   -220       O  
-ATOM    349  CB  TYR A  96      38.872  26.235  30.517  1.00  7.82           C  
-ANISOU  349  CB  TYR A  96     1133   1156    682     61    108     38       C  
-ATOM    350  CG  TYR A  96      38.843  24.964  29.703  1.00  7.38           C  
-ANISOU  350  CG  TYR A  96     1219    939    644    169     31    143       C  
-ATOM    351  CD1 TYR A  96      37.934  23.971  29.993  1.00  7.62           C  
-ANISOU  351  CD1 TYR A  96     1216    947    730    268    123    105       C  
-ATOM    352  CD2 TYR A  96      39.720  24.749  28.639  1.00  7.58           C  
-ANISOU  352  CD2 TYR A  96     1165    999    716     78    117     97       C  
-ATOM    353  CE1 TYR A  96      37.871  22.814  29.270  1.00  8.09           C  
-ANISOU  353  CE1 TYR A  96     1346    887    838    164    150    155       C  
-ATOM    354  CE2 TYR A  96      39.659  23.587  27.890  1.00  7.82           C  
-ANISOU  354  CE2 TYR A  96     1308    852    810    260    124    155       C  
-ATOM    355  CZ  TYR A  96      38.726  22.620  28.218  1.00  7.05           C  
-ANISOU  355  CZ  TYR A  96     1269    792    616    279    107    108       C  
-ATOM    356  OH  TYR A  96      38.628  21.447  27.518  1.00  8.76           O  
-ANISOU  356  OH  TYR A  96     1733    692    902    100    262    234       O  
-ATOM    357  N   LEU A  97      36.940  28.832  31.123  1.00  7.39           N  
-ANISOU  357  N   LEU A  97     1149   1088    570    173     45    -91       N  
-ATOM    358  CA  LEU A  97      36.602  29.617  32.301  1.00  7.48           C  
-ANISOU  358  CA  LEU A  97     1223   1008    609    175      4    -70       C  
-ATOM    359  C   LEU A  97      35.731  28.717  33.170  1.00  8.25           C  
-ANISOU  359  C   LEU A  97     1348   1168    617    225     87    -28       C  
-ATOM    360  O   LEU A  97      34.679  28.249  32.754  1.00  9.30           O  
-ANISOU  360  O   LEU A  97     1550   1407    574    245    261     -4       O  
-ATOM    361  CB  LEU A  97      35.855  30.893  31.933  1.00  8.20           C  
-ANISOU  361  CB  LEU A  97     1342   1028    743    152    -48   -144       C  
-ATOM    362  CG  LEU A  97      35.619  31.870  33.083  1.00 10.44           C  
-ANISOU  362  CG  LEU A  97     1614   1236   1115    233    -57    -79       C  
-ATOM    363  CD1 LEU A  97      36.893  32.376  33.661  1.00 12.92           C  
-ANISOU  363  CD1 LEU A  97     1946   1433   1529    294   -138   -168       C  
-ATOM    364  CD2 LEU A  97      34.813  33.035  32.587  1.00 13.72           C  
-ANISOU  364  CD2 LEU A  97     2087   1508   1617    353   -156   -163       C  
-ATOM    365  N   ILE A  98      36.192  28.453  34.388  1.00  9.59           N  
-ANISOU  365  N   ILE A  98     1524   1364    753    215     82     15       N  
-ATOM    366  CA  ILE A  98      35.572  27.483  35.291  1.00 11.31           C  
-ANISOU  366  CA  ILE A  98     1691   1593   1013    175    189     56       C  
-ATOM    367  C   ILE A  98      35.063  28.195  36.537  1.00 13.03           C  
-ANISOU  367  C   ILE A  98     1847   1841   1262    152    167     19       C  
-ATOM    368  O   ILE A  98      35.846  28.803  37.223  1.00 13.62           O  
-ANISOU  368  O   ILE A  98     2159   2078    936    297    325   -152       O  
-ATOM    369  CB  ILE A  98      36.626  26.432  35.705  1.00 11.51           C  
-ANISOU  369  CB  ILE A  98     1724   1608   1042    195    168    122       C  
-ATOM    370  CG1 ILE A  98      37.266  25.760  34.478  1.00 14.23           C  
-ANISOU  370  CG1 ILE A  98     2031   1808   1564    279    203    247       C  
-ATOM    371  CG2 ILE A  98      36.041  25.420  36.713  1.00 12.82           C  
-ANISOU  371  CG2 ILE A  98     1986   1714   1169    119    185    127       C  
-ATOM    372  CD1 ILE A  98      36.407  24.977  33.692  1.00 17.84           C  
-ANISOU  372  CD1 ILE A  98     2244   2312   2221    197    219    147       C  
-ATOM    373  N   ASN A  99      33.755  28.126  36.771  1.00 13.87           N  
-ANISOU  373  N   ASN A  99     2019   1912   1336    138    294     21       N  
-ATOM    374  CA  ASN A  99      33.124  28.671  37.963  1.00 15.86           C  
-ANISOU  374  CA  ASN A  99     2175   2108   1742     87    207     28       C  
-ATOM    375  C   ASN A  99      33.287  27.740  39.147  1.00 16.91           C  
-ANISOU  375  C   ASN A  99     2413   2136   1874     25    186     29       C  
-ATOM    376  O   ASN A  99      33.064  26.526  39.060  1.00 18.08           O  
-ANISOU  376  O   ASN A  99     2732   2376   1760    -92    408    138       O  
-ATOM    377  CB  ASN A  99      31.634  28.888  37.739  1.00 16.88           C  
-ANISOU  377  CB  ASN A  99     2298   2218   1898     90    208    -52       C  
-ATOM    378  CG  ASN A  99      30.971  29.502  38.937  1.00 18.71           C  
-ANISOU  378  CG  ASN A  99     2533   2550   2025    154    281    -20       C  
-ATOM    379  OD1 ASN A  99      30.409  28.800  39.777  1.00 21.30           O  
-ANISOU  379  OD1 ASN A  99     3158   3203   1732    132    581   -164       O  
-ATOM    380  ND2 ASN A  99      31.073  30.813  39.052  1.00 20.44           N  
-ANISOU  380  ND2 ASN A  99     2942   2626   2195    310    362   -681       N  
-ATOM    381  N   GLN A 100      33.694  28.340  40.249  1.00 17.83           N  
-ANISOU  381  N   GLN A 100     2505   2293   1976     19    126     90       N  
-ATOM    382  CA  GLN A 100      33.844  27.655  41.518  1.00 19.07           C  
-ANISOU  382  CA  GLN A 100     2574   2472   2198     29     74     61       C  
-ATOM    383  C   GLN A 100      33.106  28.467  42.579  1.00 19.98           C  
-ANISOU  383  C   GLN A 100     2669   2583   2340     24     63     35       C  
-ATOM    384  O   GLN A 100      33.696  28.935  43.547  1.00 20.42           O  
-ANISOU  384  O   GLN A 100     2748   2732   2276     54     27    -10       O  
-ATOM    385  CB  GLN A 100      35.326  27.532  41.833  1.00 19.00           C  
-ANISOU  385  CB  GLN A 100     2587   2474   2155     53     78     32       C  
-ATOM    386  CG  GLN A 100      36.072  26.694  40.803  1.00 20.95           C  
-ANISOU  386  CG  GLN A 100     2791   2758   2408     79     81      1       C  
-ATOM    387  CD  GLN A 100      37.569  26.712  40.988  1.00 23.06           C  
-ANISOU  387  CD  GLN A 100     3053   3065   2641      9    112    -19       C  
-ATOM    388  OE1 GLN A 100      38.112  27.582  41.673  1.00 25.81           O  
-ANISOU  388  OE1 GLN A 100     3315   3407   3082    -64    200    -25       O  
-ATOM    389  NE2 GLN A 100      38.248  25.753  40.365  1.00 24.14           N  
-ANISOU  389  NE2 GLN A 100     3146   3221   2803    174    165     27       N  
-ATOM    390  N   GLY A 101      31.803  28.633  42.384  1.00 21.10           N  
-ANISOU  390  N   GLY A 101     2757   2719   2538     36     57      0       N  
-ATOM    391  CA  GLY A 101      30.973  29.381  43.319  1.00 21.76           C  
-ANISOU  391  CA  GLY A 101     2833   2809   2625     44     59    -31       C  
-ATOM    392  C   GLY A 101      31.099  30.883  43.122  1.00 22.45           C  
-ANISOU  392  C   GLY A 101     2950   2860   2719     40     36    -33       C  
-ATOM    393  O   GLY A 101      30.743  31.399  42.061  1.00 22.91           O  
-ANISOU  393  O   GLY A 101     3082   2969   2654    157     68    -92       O  
-ATOM    394  N   ASP A 102      31.617  31.594  44.126  1.00 23.19           N  
-ANISOU  394  N   ASP A 102     3049   2961   2800     21     36    -20       N  
-ATOM    395  CA  ASP A 102      31.788  33.054  44.029  1.00 23.87           C  
-ANISOU  395  CA  ASP A 102     3095   3025   2947      9     24    -19       C  
-ATOM    396  C   ASP A 102      33.144  33.431  43.435  1.00 23.12           C  
-ANISOU  396  C   ASP A 102     3028   2917   2840     11     38    -34       C  
-ATOM    397  O   ASP A 102      33.490  34.611  43.376  1.00 23.97           O  
-ANISOU  397  O   ASP A 102     3166   3004   2935     -3     68    -49       O  
-ATOM    398  CB  ASP A 102      31.616  33.777  45.382  1.00 24.59           C  
-ANISOU  398  CB  ASP A 102     3185   3123   3033      2     25    -19       C  
-ATOM    399  CG  ASP A 102      31.047  32.897  46.460  1.00 27.28           C  
-ANISOU  399  CG  ASP A 102     3476   3507   3382    -11    -57     56       C  
-ATOM    400  OD1 ASP A 102      29.909  32.403  46.292  1.00 31.96           O  
-ANISOU  400  OD1 ASP A 102     4029   4123   3988    -34   -130    104       O  
-ATOM    401  OD2 ASP A 102      31.670  32.656  47.515  1.00 30.79           O  
-ANISOU  401  OD2 ASP A 102     3993   4047   3659    104   -123    197       O  
-ATOM    402  N   HIS A 103      33.911  32.430  43.012  1.00 22.02           N  
-ANISOU  402  N   HIS A 103     2865   2800   2700     28     -7    -28       N  
-ATOM    403  CA  HIS A 103      35.153  32.661  42.291  1.00 20.90           C  
-ANISOU  403  CA  HIS A 103     2740   2706   2492     38    -29    -86       C  
-ATOM    404  C   HIS A 103      35.204  31.797  41.031  1.00 19.27           C  
-ANISOU  404  C   HIS A 103     2570   2510   2239     60    -42   -119       C  
-ATOM    405  O   HIS A 103      34.331  30.965  40.802  1.00 18.91           O  
-ANISOU  405  O   HIS A 103     2720   2524   1938    150     20   -196       O  
-ATOM    406  CB  HIS A 103      36.371  32.411  43.196  1.00 21.40           C  
-ANISOU  406  CB  HIS A 103     2786   2774   2567     28    -35    -79       C  
-ATOM    407  CG  HIS A 103      36.353  31.089  43.900  1.00 23.28           C  
-ANISOU  407  CG  HIS A 103     3066   3025   2751     53    -78    -34       C  
-ATOM    408  ND1 HIS A 103      35.549  30.835  44.992  1.00 25.17           N  
-ANISOU  408  ND1 HIS A 103     3466   3198   2899     42    -53     62       N  
-ATOM    409  CD2 HIS A 103      37.063  29.958  43.684  1.00 25.49           C  
-ANISOU  409  CD2 HIS A 103     3390   3289   3002    111     12    -17       C  
-ATOM    410  CE1 HIS A 103      35.757  29.598  45.410  1.00 25.71           C  
-ANISOU  410  CE1 HIS A 103     3492   3325   2950    122    -29     10       C  
-ATOM    411  NE2 HIS A 103      36.668  29.043  44.630  1.00 26.20           N  
-ANISOU  411  NE2 HIS A 103     3479   3397   3075    103    -51     76       N  
-ATOM    412  N   GLU A 104      36.231  32.023  40.225  1.00 17.29           N  
-ANISOU  412  N   GLU A 104     2383   2336   1848     74    -29   -233       N  
-ATOM    413  CA  GLU A 104      36.398  31.323  38.945  1.00 16.62           C  
-ANISOU  413  CA  GLU A 104     2257   2218   1839     90     -7   -190       C  
-ATOM    414  C   GLU A 104      37.862  31.314  38.534  1.00 16.24           C  
-ANISOU  414  C   GLU A 104     2187   2226   1755     77    -36   -198       C  
-ATOM    415  O   GLU A 104      38.674  32.078  39.031  1.00 16.39           O  
-ANISOU  415  O   GLU A 104     2337   2237   1652     87    -27   -442       O  
-ATOM    416  CB  GLU A 104      35.565  31.995  37.846  1.00 17.03           C  
-ANISOU  416  CB  GLU A 104     2298   2249   1922     92      6   -166       C  
-ATOM    417  CG  GLU A 104      36.061  33.384  37.446  1.00 17.92           C  
-ANISOU  417  CG  GLU A 104     2372   2362   2074     72     51   -111       C  
-ATOM    418  CD  GLU A 104      35.096  34.158  36.557  1.00 20.00           C  
-ANISOU  418  CD  GLU A 104     2535   2592   2472    -48     28    -35       C  
-ATOM    419  OE1 GLU A 104      33.900  33.789  36.452  1.00 21.44           O  
-ANISOU  419  OE1 GLU A 104     2613   2826   2708     12    -60    -34       O  
-ATOM    420  OE2 GLU A 104      35.544  35.162  35.956  1.00 20.94           O  
-ANISOU  420  OE2 GLU A 104     2816   2544   2596   -100    -83   -143       O  
-ATOM    421  N   VAL A 105      38.184  30.479  37.558  1.00 14.06           N  
-ANISOU  421  N   VAL A 105     1937   2057   1345    130    -42   -297       N  
-ATOM    422  CA  VAL A 105      39.554  30.302  37.113  1.00 13.28           C  
-ANISOU  422  CA  VAL A 105     1858   1907   1281    123    -69   -128       C  
-ATOM    423  C   VAL A 105      39.618  30.150  35.600  1.00 11.33           C  
-ANISOU  423  C   VAL A 105     1701   1623    981    194   -141   -209       C  
-ATOM    424  O   VAL A 105      38.731  29.550  34.994  1.00 11.39           O  
-ANISOU  424  O   VAL A 105     1849   1675    802    163   -178   -157       O  
-ATOM    425  CB  VAL A 105      40.213  29.085  37.794  1.00 13.22           C  
-ANISOU  425  CB  VAL A 105     1964   2112    944    142    -13    -63       C  
-ATOM    426  CG1 VAL A 105      39.512  27.779  37.517  1.00 16.04           C  
-ANISOU  426  CG1 VAL A 105     2149   2243   1703    244     49     76       C  
-ATOM    427  CG2 VAL A 105      41.627  28.999  37.422  1.00 16.84           C  
-ANISOU  427  CG2 VAL A 105     2254   2283   1859    105    -89     23       C  
-ATOM    428  N   VAL A 106      40.686  30.681  35.023  1.00 10.61           N  
-ANISOU  428  N   VAL A 106     1629   1518    883    138   -224   -226       N  
-ATOM    429  CA  VAL A 106      40.963  30.535  33.590  1.00 10.24           C  
-ANISOU  429  CA  VAL A 106     1483   1483    923    165   -125   -173       C  
-ATOM    430  C   VAL A 106      42.037  29.464  33.416  1.00 10.18           C  
-ANISOU  430  C   VAL A 106     1454   1494    919    197   -153   -180       C  
-ATOM    431  O   VAL A 106      43.063  29.491  34.094  1.00 11.53           O  
-ANISOU  431  O   VAL A 106     1636   1788    957    303   -303   -329       O  
-ATOM    432  CB  VAL A 106      41.450  31.863  32.985  1.00 11.09           C  
-ANISOU  432  CB  VAL A 106     1522   1526   1165    105   -140   -143       C  
-ATOM    433  CG1 VAL A 106      41.789  31.708  31.521  1.00 11.92           C  
-ANISOU  433  CG1 VAL A 106     1626   1503   1400    175     18     22       C  
-ATOM    434  CG2 VAL A 106      40.417  32.966  33.137  1.00 13.07           C  
-ANISOU  434  CG2 VAL A 106     1903   1608   1455    210    -23   -154       C  
-ATOM    435  N   ARG A 107      41.799  28.513  32.520  1.00  9.45           N  
-ANISOU  435  N   ARG A 107     1402   1393    792    216   -139   -165       N  
-ATOM    436  CA  ARG A 107      42.738  27.431  32.247  1.00  9.04           C  
-ANISOU  436  CA  ARG A 107     1321   1278    835    193    -68    -27       C  
-ATOM    437  C   ARG A 107      42.893  27.256  30.746  1.00  7.69           C  
-ANISOU  437  C   ARG A 107     1225   1013    681    146   -133    -44       C  
-ATOM    438  O   ARG A 107      42.010  27.651  29.969  1.00  7.96           O  
-ANISOU  438  O   ARG A 107     1224   1175    624    301   -169     19       O  
-ATOM    439  CB  ARG A 107      42.226  26.126  32.877  1.00  9.73           C  
-ANISOU  439  CB  ARG A 107     1496   1363    836    306      1    -47       C  
-ATOM    440  CG  ARG A 107      42.115  26.154  34.398  1.00 12.87           C  
-ANISOU  440  CG  ARG A 107     1809   1869   1212    161     53    -34       C  
-ATOM    441  CD  ARG A 107      43.470  26.004  35.041  1.00 15.46           C  
-ANISOU  441  CD  ARG A 107     2199   2174   1500     71      3   -157       C  
-ATOM    442  NE  ARG A 107      43.418  25.960  36.499  1.00 18.29           N  
-ANISOU  442  NE  ARG A 107     2493   2531   1925     18    -82    -80       N  
-ATOM    443  CZ  ARG A 107      43.725  26.971  37.305  1.00 19.33           C  
-ANISOU  443  CZ  ARG A 107     2662   2655   2026    -66      6    -75       C  
-ATOM    444  NH1 ARG A 107      44.081  28.160  36.812  1.00 21.92           N  
-ANISOU  444  NH1 ARG A 107     3057   2875   2396   -100    -51    -82       N  
-ATOM    445  NH2 ARG A 107      43.643  26.809  38.623  1.00 20.68           N  
-ANISOU  445  NH2 ARG A 107     2914   2876   2065     36   -141    -32       N  
-ATOM    446  N   PHE A 108      44.002  26.642  30.358  1.00  6.72           N  
-ANISOU  446  N   PHE A 108     1096    866    588    170   -125     36       N  
-ATOM    447  CA  PHE A 108      44.342  26.451  28.953  1.00  6.30           C  
-ANISOU  447  CA  PHE A 108     1008    810    575    130    -63     38       C  
-ATOM    448  C   PHE A 108      44.654  24.994  28.698  1.00  6.31           C  
-ANISOU  448  C   PHE A 108     1052    744    598    134   -130     84       C  
-ATOM    449  O   PHE A 108      45.341  24.356  29.500  1.00  7.57           O  
-ANISOU  449  O   PHE A 108     1310    872    693    172   -271    121       O  
-ATOM    450  CB  PHE A 108      45.515  27.347  28.570  1.00  6.86           C  
-ANISOU  450  CB  PHE A 108     1079    825    700    157   -110     45       C  
-ATOM    451  CG  PHE A 108      45.228  28.792  28.811  1.00  6.48           C  
-ANISOU  451  CG  PHE A 108     1128    653    680    140    -63     26       C  
-ATOM    452  CD1 PHE A 108      44.420  29.487  27.931  1.00  7.32           C  
-ANISOU  452  CD1 PHE A 108     1199    747    833    114    -84     24       C  
-ATOM    453  CD2 PHE A 108      45.681  29.445  29.948  1.00  8.00           C  
-ANISOU  453  CD2 PHE A 108     1321    851    867     92   -101    -43       C  
-ATOM    454  CE1 PHE A 108      44.107  30.811  28.163  1.00  8.24           C  
-ANISOU  454  CE1 PHE A 108     1243    770   1118     54   -164     76       C  
-ATOM    455  CE2 PHE A 108      45.371  30.771  30.170  1.00  9.23           C  
-ANISOU  455  CE2 PHE A 108     1528    915   1061    -40   -128   -123       C  
-ATOM    456  CZ  PHE A 108      44.577  31.449  29.293  1.00  8.90           C  
-ANISOU  456  CZ  PHE A 108     1483    748   1147     19      4    -16       C  
-ATOM    457  N   ALA A 109      44.159  24.481  27.572  1.00  6.35           N  
-ANISOU  457  N   ALA A 109     1064    717    629    129   -105     38       N  
-ATOM    458  CA  ALA A 109      44.329  23.078  27.230  1.00  6.03           C  
-ANISOU  458  CA  ALA A 109      968    692    631    104    -45     79       C  
-ATOM    459  C   ALA A 109      44.941  22.919  25.860  1.00  5.82           C  
-ANISOU  459  C   ALA A 109      950    677    585    137    -91     46       C  
-ATOM    460  O   ALA A 109      44.664  23.676  24.928  1.00  6.89           O  
-ANISOU  460  O   ALA A 109     1076    874    667    239    -49     83       O  
-ATOM    461  CB  ALA A 109      43.026  22.353  27.254  1.00  6.99           C  
-ANISOU  461  CB  ALA A 109     1095    827    733    103    -25     34       C  
-ATOM    462  N   LYS A 110      45.758  21.876  25.744  1.00  5.87           N  
-ANISOU  462  N   LYS A 110      953    620    657    119    -33     40       N  
-ATOM    463  CA  LYS A 110      46.210  21.340  24.464  1.00  6.05           C  
-ANISOU  463  CA  LYS A 110      900    635    763     72     27     21       C  
-ATOM    464  C   LYS A 110      45.340  20.122  24.132  1.00  5.99           C  
-ANISOU  464  C   LYS A 110      908    652    714    120     43     11       C  
-ATOM    465  O   LYS A 110      44.358  19.851  24.815  1.00  6.73           O  
-ANISOU  465  O   LYS A 110      952    815    787     54     40    -80       O  
-ATOM    466  CB  LYS A 110      47.707  21.005  24.526  1.00  6.39           C  
-ANISOU  466  CB  LYS A 110      897    690    840     19     67      0       C  
-ATOM    467  CG  LYS A 110      48.100  20.021  25.607  1.00  7.59           C  
-ANISOU  467  CG  LYS A 110     1093    788   1003     12   -107    109       C  
-ATOM    468  CD  LYS A 110      49.601  19.769  25.628  1.00  9.27           C  
-ANISOU  468  CD  LYS A 110     1216    949   1357     50   -191      7       C  
-ATOM    469  CE  LYS A 110      49.979  18.842  26.751  1.00 12.58           C  
-ANISOU  469  CE  LYS A 110     1598   1272   1910     88   -263     10       C  
-ATOM    470  NZ  LYS A 110      51.442  18.589  26.775  1.00 14.24           N  
-ANISOU  470  NZ  LYS A 110     1562   1375   2470    197   -760    -12       N  
-ATOM    471  N   ARG A 111      45.694  19.367  23.103  1.00  6.58           N  
-ANISOU  471  N   ARG A 111      958    724    815     10     59    -24       N  
-ATOM    472  CA  ARG A 111      44.888  18.243  22.666  1.00  7.83           C  
-ANISOU  472  CA  ARG A 111     1177    847    949    -36     20    -66       C  
-ATOM    473  C   ARG A 111      44.595  17.264  23.785  1.00  7.77           C  
-ANISOU  473  C   ARG A 111     1163    745   1045   -108     36   -123       C  
-ATOM    474  O   ARG A 111      43.484  16.732  23.888  1.00  8.37           O  
-ANISOU  474  O   ARG A 111     1101    786   1289   -152     35    -90       O  
-ATOM    475  CB  ARG A 111      45.630  17.522  21.531  1.00  8.92           C  
-ANISOU  475  CB  ARG A 111     1412    954   1021   -102     88   -122       C  
-ATOM    476  CG  ARG A 111      45.165  16.130  21.170  1.00 11.40           C  
-ANISOU  476  CG  ARG A 111     1616   1289   1424    -92    -41     14       C  
-ATOM    477  CD  ARG A 111      43.858  16.171  20.472  1.00 12.12           C  
-ANISOU  477  CD  ARG A 111     1537   1409   1656     38   -195    197       C  
-ATOM    478  NE  ARG A 111      43.955  16.802  19.140  1.00 11.82           N  
-ANISOU  478  NE  ARG A 111     1584   1403   1503    -32   -308     37       N  
-ATOM    479  CZ  ARG A 111      42.902  17.211  18.428  1.00 10.37           C  
-ANISOU  479  CZ  ARG A 111     1315   1311   1311     58   -164    148       C  
-ATOM    480  NH1 ARG A 111      41.679  17.073  18.925  1.00 13.27           N  
-ANISOU  480  NH1 ARG A 111     1502   1833   1703     12   -209    401       N  
-ATOM    481  NH2 ARG A 111      43.064  17.777  17.234  1.00  9.71           N  
-ANISOU  481  NH2 ARG A 111     1174   1305   1210    198   -126    -22       N  
-ATOM    482  N   SER A 112      45.608  17.005  24.597  1.00  7.90           N  
-ANISOU  482  N   SER A 112     1133    706   1162    -88    -19    -11       N  
-ATOM    483  CA  SER A 112      45.563  15.939  25.586  1.00  8.27           C  
-ANISOU  483  CA  SER A 112     1177    729   1233    -55     -1     45       C  
-ATOM    484  C   SER A 112      45.229  16.353  27.002  1.00  7.90           C  
-ANISOU  484  C   SER A 112     1191    668   1142     18    -56    109       C  
-ATOM    485  O   SER A 112      45.206  15.493  27.868  1.00  9.49           O  
-ANISOU  485  O   SER A 112     1664    661   1280     10   -176    232       O  
-ATOM    486  CB  SER A 112      46.897  15.198  25.579  1.00  9.62           C  
-ANISOU  486  CB  SER A 112     1342    807   1503    -14     27     65       C  
-ATOM    487  OG  SER A 112      47.950  16.093  25.876  1.00 12.64           O  
-ANISOU  487  OG  SER A 112     1312   1111   2380     23    -47    164       O  
-ATOM    488  N   GLY A 113      44.960  17.629  27.263  1.00  7.00           N  
-ANISOU  488  N   GLY A 113     1059    627    973    -81    -29    115       N  
-ATOM    489  CA  GLY A 113      44.524  18.021  28.587  1.00  7.15           C  
-ANISOU  489  CA  GLY A 113     1056    752    906    -18    -47    108       C  
-ATOM    490  C   GLY A 113      44.823  19.451  28.915  1.00  6.24           C  
-ANISOU  490  C   GLY A 113      982    619    769     23    -69    183       C  
-ATOM    491  O   GLY A 113      45.505  20.161  28.178  1.00  6.75           O  
-ANISOU  491  O   GLY A 113     1130    571    861    -47    -63    162       O  
-ATOM    492  N   ILE A 114      44.272  19.892  30.039  1.00  6.59           N  
-ANISOU  492  N   ILE A 114     1027    688    789    -28    -36    132       N  
-ATOM    493  CA  ILE A 114      44.609  21.180  30.623  1.00  7.51           C  
-ANISOU  493  CA  ILE A 114     1163    821    866     18    -99    118       C  
-ATOM    494  C   ILE A 114      46.071  21.154  31.085  1.00  7.39           C  
-ANISOU  494  C   ILE A 114     1142    758    905     17   -139    164       C  
-ATOM    495  O   ILE A 114      46.553  20.159  31.643  1.00  8.44           O  
-ANISOU  495  O   ILE A 114     1303    752   1150     73   -276    196       O  
-ATOM    496  CB  ILE A 114      43.634  21.521  31.770  1.00  7.94           C  
-ANISOU  496  CB  ILE A 114     1152    957    904     11   -112    104       C  
-ATOM    497  CG1 ILE A 114      42.280  21.933  31.182  1.00  9.49           C  
-ANISOU  497  CG1 ILE A 114     1297   1228   1080     20    -96    -34       C  
-ATOM    498  CG2 ILE A 114      44.175  22.643  32.645  1.00  9.35           C  
-ANISOU  498  CG2 ILE A 114     1377   1178    997     66   -127    -30       C  
-ATOM    499  CD1 ILE A 114      41.160  22.050  32.203  1.00 11.08           C  
-ANISOU  499  CD1 ILE A 114     1448   1451   1311     -2     27     12       C  
-HETATM  500  N   MSE A 115      46.776  22.249  30.817  1.00  7.12           N  
-ANISOU  500  N   MSE A 115     1183    677    843     35   -174    217       N  
-HETATM  501  CA  MSE A 115      48.197  22.356  31.073  1.00  8.29           C  
-ANISOU  501  CA  MSE A 115     1262    837   1050      0   -121    116       C  
-HETATM  502  C   MSE A 115      48.520  23.012  32.399  1.00  8.40           C  
-ANISOU  502  C   MSE A 115     1280    870   1041     39   -218    196       C  
-HETATM  503  O   MSE A 115      47.846  23.932  32.858  1.00  8.84           O  
-ANISOU  503  O   MSE A 115     1500    950    907     -5   -261    151       O  
-HETATM  504  CB  MSE A 115      48.874  23.164  29.970  1.00  7.80           C  
-ANISOU  504  CB  MSE A 115     1186    875    901     -3   -126     83       C  
-HETATM  505  CG  MSE A 115      48.793  22.478  28.625  1.00  8.90           C  
-ANISOU  505  CG  MSE A 115     1353    866   1163      7   -156     71       C  
-HETATM  506 SE   MSE A 115      49.632  23.417  27.200  1.00 17.41          SE  
-ANISOU  506 SE   MSE A 115     2266   2266   2082   -182    -41   -104      SE  
-HETATM  507  CE  MSE A 115      48.262  24.733  26.890  1.00 11.29           C  
-ANISOU  507  CE  MSE A 115     1773   1180   1335    -96   -228     -8       C  
-ATOM    508  N   ASP A 116      49.598  22.540  33.015  1.00  9.01           N  
-ANISOU  508  N   ASP A 116     1344    948   1130    -31   -280    185       N  
-ATOM    509  CA  ASP A 116      50.231  23.259  34.090  1.00  9.89           C  
-ANISOU  509  CA  ASP A 116     1403   1146   1209     -7   -295    171       C  
-ATOM    510  C   ASP A 116      50.637  24.634  33.566  1.00  9.78           C  
-ANISOU  510  C   ASP A 116     1349   1139   1225    -59   -264    131       C  
-ATOM    511  O   ASP A 116      51.114  24.729  32.441  1.00  9.32           O  
-ANISOU  511  O   ASP A 116     1394   1026   1118   -127   -354    120       O  
-ATOM    512  CB  ASP A 116      51.465  22.494  34.566  1.00 11.31           C  
-ANISOU  512  CB  ASP A 116     1570   1310   1416      2   -366    195       C  
-ATOM    513  CG  ASP A 116      52.129  23.152  35.737  1.00 13.59           C  
-ANISOU  513  CG  ASP A 116     1801   1706   1653   -130   -608    413       C  
-ATOM    514  OD1 ASP A 116      51.845  22.754  36.883  1.00 20.03           O  
-ANISOU  514  OD1 ASP A 116     2852   2685   2072   -560   -759    331       O  
-ATOM    515  OD2 ASP A 116      52.931  24.074  35.589  1.00 15.04           O  
-ANISOU  515  OD2 ASP A 116     2185   1753   1774   -199   -935    570       O  
-ATOM    516  N   PRO A 117      50.465  25.691  34.358  1.00 10.22           N  
-ANISOU  516  N   PRO A 117     1374   1209   1298    -45   -151     98       N  
-ATOM    517  CA  PRO A 117      50.810  27.039  33.876  1.00 10.37           C  
-ANISOU  517  CA  PRO A 117     1395   1216   1326    -18   -128     69       C  
-ATOM    518  C   PRO A 117      52.275  27.245  33.468  1.00  9.46           C  
-ANISOU  518  C   PRO A 117     1317   1104   1173     23   -148     67       C  
-ATOM    519  O   PRO A 117      52.540  28.195  32.739  1.00  9.81           O  
-ANISOU  519  O   PRO A 117     1408   1051   1266    -46   -232     89       O  
-ATOM    520  CB  PRO A 117      50.448  27.940  35.058  1.00 11.62           C  
-ANISOU  520  CB  PRO A 117     1566   1358   1488    -33    -83     39       C  
-ATOM    521  CG  PRO A 117      49.481  27.171  35.833  1.00 13.84           C  
-ANISOU  521  CG  PRO A 117     1807   1703   1746    -62     62    -65       C  
-ATOM    522  CD  PRO A 117      49.874  25.734  35.707  1.00 11.98           C  
-ANISOU  522  CD  PRO A 117     1586   1435   1529   -109    -97     18       C  
-ATOM    523  N   ASN A 118      53.195  26.393  33.919  1.00  9.45           N  
-ANISOU  523  N   ASN A 118     1312   1114   1165     30   -177     43       N  
-ATOM    524  CA  ASN A 118      54.593  26.514  33.522  1.00  9.90           C  
-ANISOU  524  CA  ASN A 118     1295   1170   1294     33   -160    -22       C  
-ATOM    525  C   ASN A 118      55.027  25.540  32.428  1.00  9.61           C  
-ANISOU  525  C   ASN A 118     1301   1142   1209     30   -168    -15       C  
-ATOM    526  O   ASN A 118      56.213  25.429  32.133  1.00 10.66           O  
-ANISOU  526  O   ASN A 118     1317   1237   1494     14   -215   -137       O  
-ATOM    527  CB  ASN A 118      55.507  26.458  34.742  1.00 10.36           C  
-ANISOU  527  CB  ASN A 118     1356   1255   1324      6   -170    -58       C  
-ATOM    528  CG  ASN A 118      55.484  27.751  35.500  1.00 10.77           C  
-ANISOU  528  CG  ASN A 118     1359   1314   1417    -31   -189   -126       C  
-ATOM    529  OD1 ASN A 118      55.715  28.815  34.928  1.00 11.74           O  
-ANISOU  529  OD1 ASN A 118     1549   1372   1537    -56   -292   -165       O  
-ATOM    530  ND2 ASN A 118      55.193  27.678  36.782  1.00 14.19           N  
-ANISOU  530  ND2 ASN A 118     2041   1776   1575   -131   -208    -85       N  
-ATOM    531  N   GLU A 119      54.072  24.886  31.777  1.00  9.56           N  
-ANISOU  531  N   GLU A 119     1305   1096   1232     70   -218     67       N  
-ATOM    532  CA  GLU A 119      54.397  24.127  30.576  1.00  9.62           C  
-ANISOU  532  CA  GLU A 119     1324   1112   1217     34   -174     41       C  
-ATOM    533  C   GLU A 119      54.558  25.080  29.396  1.00  9.60           C  
-ANISOU  533  C   GLU A 119     1399   1140   1105     -2   -252     21       C  
-ATOM    534  O   GLU A 119      53.618  25.777  29.030  1.00  9.90           O  
-ANISOU  534  O   GLU A 119     1516   1026   1220    169   -330     92       O  
-ATOM    535  CB  GLU A 119      53.327  23.082  30.240  1.00  9.78           C  
-ANISOU  535  CB  GLU A 119     1368   1032   1316     21   -189     81       C  
-ATOM    536  CG  GLU A 119      53.690  22.332  28.961  1.00 11.09           C  
-ANISOU  536  CG  GLU A 119     1547   1189   1476     30   -171     36       C  
-ATOM    537  CD  GLU A 119      52.706  21.276  28.511  1.00 13.12           C  
-ANISOU  537  CD  GLU A 119     1683   1301   2000    120   -169    -93       C  
-ATOM    538  OE1 GLU A 119      51.808  20.897  29.276  1.00 14.30           O  
-ANISOU  538  OE1 GLU A 119     1718   1426   2287     14   -238   -427       O  
-ATOM    539  OE2 GLU A 119      52.853  20.804  27.364  1.00 15.19           O  
-ANISOU  539  OE2 GLU A 119     1982   1604   2185   -105   -388   -312       O  
-ATOM    540  N   ASN A 120      55.758  25.116  28.828  1.00 10.23           N  
-ANISOU  540  N   ASN A 120     1458   1229   1199     19   -289    104       N  
-ATOM    541  CA  ASN A 120      56.008  25.849  27.595  1.00 10.98           C  
-ANISOU  541  CA  ASN A 120     1625   1311   1234    -89   -218     -5       C  
-ATOM    542  C   ASN A 120      55.334  25.101  26.450  1.00 10.52           C  
-ANISOU  542  C   ASN A 120     1609   1201   1187    -54   -267    -53       C  
-ATOM    543  O   ASN A 120      55.632  23.941  26.216  1.00 12.07           O  
-ANISOU  543  O   ASN A 120     1951   1157   1478     35   -513     18       O  
-ATOM    544  CB  ASN A 120      57.513  25.976  27.344  1.00 12.40           C  
-ANISOU  544  CB  ASN A 120     1845   1569   1297   -192   -232    -42       C  
-ATOM    545  CG  ASN A 120      57.836  26.798  26.106  1.00 15.27           C  
-ANISOU  545  CG  ASN A 120     2290   1660   1850   -515   -100   -140       C  
-ATOM    546  OD1 ASN A 120      57.098  27.713  25.741  1.00 18.02           O  
-ANISOU  546  OD1 ASN A 120     3199   1912   1736  -1134   -166    141       O  
-ATOM    547  ND2 ASN A 120      58.960  26.488  25.473  1.00 18.47           N  
-ANISOU  547  ND2 ASN A 120     3396   1889   1731   -739    358   -170       N  
-ATOM    548  N   PHE A 121      54.407  25.762  25.768  1.00  9.08           N  
-ANISOU  548  N   PHE A 121     1445   1050    952    -63   -299    -48       N  
-ATOM    549  CA  PHE A 121      53.654  25.159  24.671  1.00  8.11           C  
-ANISOU  549  CA  PHE A 121     1257    894    928    -28   -159    -59       C  
-ATOM    550  C   PHE A 121      53.513  26.178  23.546  1.00  7.15           C  
-ANISOU  550  C   PHE A 121     1087    763    865    -29   -161     -4       C  
-ATOM    551  O   PHE A 121      52.587  26.996  23.509  1.00  6.94           O  
-ANISOU  551  O   PHE A 121     1061    757    816    -10   -128    -61       O  
-ATOM    552  CB  PHE A 121      52.304  24.691  25.182  1.00  8.53           C  
-ANISOU  552  CB  PHE A 121     1438    963    838    -65   -184      7       C  
-ATOM    553  CG  PHE A 121      51.474  23.991  24.154  1.00  8.50           C  
-ANISOU  553  CG  PHE A 121     1332    990    905   -161    -91     52       C  
-ATOM    554  CD1 PHE A 121      51.737  22.680  23.811  1.00  9.26           C  
-ANISOU  554  CD1 PHE A 121     1504   1016    997   -113   -195     16       C  
-ATOM    555  CD2 PHE A 121      50.403  24.632  23.549  1.00  9.28           C  
-ANISOU  555  CD2 PHE A 121     1341   1258    924   -138    -80    -78       C  
-ATOM    556  CE1 PHE A 121      50.958  22.022  22.872  1.00 10.37           C  
-ANISOU  556  CE1 PHE A 121     1700   1118   1121   -251    -19     14       C  
-ATOM    557  CE2 PHE A 121      49.628  23.973  22.610  1.00  9.99           C  
-ANISOU  557  CE2 PHE A 121     1330   1573    891   -188    -24    224       C  
-ATOM    558  CZ  PHE A 121      49.902  22.665  22.287  1.00  9.82           C  
-ANISOU  558  CZ  PHE A 121     1436   1347    946   -442    -64    108       C  
-ATOM    559  N   PHE A 122      54.482  26.143  22.648  1.00  7.02           N  
-ANISOU  559  N   PHE A 122      980    781    903     39   -144     -4       N  
-ATOM    560  CA  PHE A 122      54.491  26.952  21.442  1.00  6.44           C  
-ANISOU  560  CA  PHE A 122      859    776    810    -23    -41     -4       C  
-ATOM    561  C   PHE A 122      54.350  28.445  21.728  1.00  6.81           C  
-ANISOU  561  C   PHE A 122      938    794    856    -47    -58     33       C  
-ATOM    562  O   PHE A 122      53.843  29.191  20.903  1.00  8.01           O  
-ANISOU  562  O   PHE A 122     1213    878    951    118    -74     32       O  
-ATOM    563  CB  PHE A 122      53.418  26.473  20.464  1.00  6.74           C  
-ANISOU  563  CB  PHE A 122      877    865    818    -22      4    -38       C  
-ATOM    564  CG  PHE A 122      53.603  25.052  20.018  1.00  6.82           C  
-ANISOU  564  CG  PHE A 122      936    826    829    -57   -104     33       C  
-ATOM    565  CD1 PHE A 122      54.737  24.670  19.311  1.00  7.27           C  
-ANISOU  565  CD1 PHE A 122     1075    716    968    -57    -78     63       C  
-ATOM    566  CD2 PHE A 122      52.630  24.099  20.257  1.00  8.48           C  
-ANISOU  566  CD2 PHE A 122     1029    991   1199    -26     71   -118       C  
-ATOM    567  CE1 PHE A 122      54.907  23.372  18.890  1.00  7.87           C  
-ANISOU  567  CE1 PHE A 122     1179    790   1019    -38    -25     19       C  
-ATOM    568  CE2 PHE A 122      52.785  22.808  19.810  1.00 10.47           C  
-ANISOU  568  CE2 PHE A 122     1376    950   1652   -214     -9   -157       C  
-ATOM    569  CZ  PHE A 122      53.922  22.441  19.119  1.00 10.24           C  
-ANISOU  569  CZ  PHE A 122     1459    862   1566    -27    -24   -141       C  
-ATOM    570  N   GLY A 123      54.840  28.891  22.883  1.00  7.31           N  
-ANISOU  570  N   GLY A 123      961    809   1004    -57    -71    -37       N  
-ATOM    571  CA  GLY A 123      54.855  30.307  23.196  1.00  7.80           C  
-ANISOU  571  CA  GLY A 123     1016    818   1127    -43    -83    -16       C  
-ATOM    572  C   GLY A 123      53.510  30.920  23.516  1.00  7.05           C  
-ANISOU  572  C   GLY A 123      979    760    938    -36    -92     29       C  
-ATOM    573  O   GLY A 123      53.404  32.151  23.519  1.00  7.63           O  
-ANISOU  573  O   GLY A 123     1031    715   1151     18      2     -8       O  
-ATOM    574  N   TYR A 124      52.490  30.105  23.815  1.00  6.43           N  
-ANISOU  574  N   TYR A 124      929    674    840    -29    -55     48       N  
-ATOM    575  CA  TYR A 124      51.128  30.639  23.913  1.00  6.80           C  
-ANISOU  575  CA  TYR A 124      916    715    952    -16   -115     11       C  
-ATOM    576  C   TYR A 124      50.976  31.628  25.049  1.00  6.70           C  
-ANISOU  576  C   TYR A 124      786    742   1017      0   -150     57       C  
-ATOM    577  O   TYR A 124      50.046  32.412  25.055  1.00  7.01           O  
-ANISOU  577  O   TYR A 124      802    685   1173     61   -211     56       O  
-ATOM    578  CB  TYR A 124      50.072  29.528  24.050  1.00  6.55           C  
-ANISOU  578  CB  TYR A 124      830    812    845    -53   -166      0       C  
-ATOM    579  CG  TYR A 124      49.862  29.041  25.461  1.00  6.11           C  
-ANISOU  579  CG  TYR A 124      815    719    785    -49   -209    -86       C  
-ATOM    580  CD1 TYR A 124      48.870  29.605  26.262  1.00  6.80           C  
-ANISOU  580  CD1 TYR A 124      983    822    775      2   -208     91       C  
-ATOM    581  CD2 TYR A 124      50.652  28.044  26.000  1.00  7.29           C  
-ANISOU  581  CD2 TYR A 124      918    944    905    -74    -64   -139       C  
-ATOM    582  CE1 TYR A 124      48.669  29.184  27.555  1.00  7.32           C  
-ANISOU  582  CE1 TYR A 124     1030    953    797    117    -29      1       C  
-ATOM    583  CE2 TYR A 124      50.466  27.618  27.301  1.00  7.63           C  
-ANISOU  583  CE2 TYR A 124     1199    831    866     41    -40    -48       C  
-ATOM    584  CZ  TYR A 124      49.465  28.182  28.072  1.00  7.32           C  
-ANISOU  584  CZ  TYR A 124     1251    838    689     75    -91    -31       C  
-ATOM    585  OH  TYR A 124      49.280  27.772  29.363  1.00  8.99           O  
-ANISOU  585  OH  TYR A 124     1456   1263    697    235     71    135       O  
-ATOM    586  N   HIS A 125      51.896  31.605  26.006  1.00  6.71           N  
-ANISOU  586  N   HIS A 125      855    718    976     67   -214    -16       N  
-ATOM    587  CA  HIS A 125      51.852  32.570  27.082  1.00  7.27           C  
-ANISOU  587  CA  HIS A 125      940    784   1036     52   -207      4       C  
-ATOM    588  C   HIS A 125      51.810  34.008  26.575  1.00  7.37           C  
-ANISOU  588  C   HIS A 125      905    760   1135    132   -266      3       C  
-ATOM    589  O   HIS A 125      51.269  34.862  27.273  1.00  8.57           O  
-ANISOU  589  O   HIS A 125     1174    723   1359    257   -356   -177       O  
-ATOM    590  CB  HIS A 125      53.024  32.380  28.042  1.00  7.59           C  
-ANISOU  590  CB  HIS A 125      953    816   1115     36   -236     18       C  
-ATOM    591  CG  HIS A 125      52.969  31.081  28.758  1.00  8.71           C  
-ANISOU  591  CG  HIS A 125     1107    980   1222      0   -479    -14       C  
-ATOM    592  ND1 HIS A 125      53.320  29.901  28.148  1.00 11.90           N  
-ANISOU  592  ND1 HIS A 125     1581   1075   1866    -32   -717     17       N  
-ATOM    593  CD2 HIS A 125      52.537  30.761  29.998  1.00 10.43           C  
-ANISOU  593  CD2 HIS A 125     1104   1159   1698     14   -377    149       C  
-ATOM    594  CE1 HIS A 125      53.158  28.910  29.000  1.00 12.50           C  
-ANISOU  594  CE1 HIS A 125     1522   1178   2047   -160   -732    367       C  
-ATOM    595  NE2 HIS A 125      52.671  29.400  30.127  1.00 12.18           N  
-ANISOU  595  NE2 HIS A 125     1337   1373   1918    -66   -615    578       N  
-ATOM    596  N   ILE A 126      52.356  34.278  25.382  1.00  7.71           N  
-ANISOU  596  N   ILE A 126      948    707   1274     63   -198     25       N  
-ATOM    597  CA  ILE A 126      52.320  35.625  24.794  1.00  8.53           C  
-ANISOU  597  CA  ILE A 126     1029    816   1394     66   -184     31       C  
-ATOM    598  C   ILE A 126      50.874  36.118  24.576  1.00  8.32           C  
-ANISOU  598  C   ILE A 126      998    819   1340     63   -152      7       C  
-ATOM    599  O   ILE A 126      50.637  37.332  24.518  1.00  9.73           O  
-ANISOU  599  O   ILE A 126     1189    719   1789    111   -251    107       O  
-ATOM    600  CB  ILE A 126      53.146  35.657  23.465  1.00  9.65           C  
-ANISOU  600  CB  ILE A 126     1071    968   1627     72    -83    139       C  
-ATOM    601  CG1 ILE A 126      53.564  37.078  23.095  1.00 11.74           C  
-ANISOU  601  CG1 ILE A 126     1441   1243   1773    -11   -133    146       C  
-ATOM    602  CG2 ILE A 126      52.395  35.082  22.302  1.00  9.93           C  
-ANISOU  602  CG2 ILE A 126     1023   1032   1716    106     67    101       C  
-ATOM    603  CD1 ILE A 126      54.772  37.552  23.802  1.00 14.30           C  
-ANISOU  603  CD1 ILE A 126     1835   1573   2023    -89    -68     83       C  
-ATOM    604  N   LEU A 127      49.921  35.189  24.475  1.00  7.45           N  
-ANISOU  604  N   LEU A 127      926    724   1179     67   -155      6       N  
-ATOM    605  CA  LEU A 127      48.520  35.512  24.242  1.00  7.51           C  
-ANISOU  605  CA  LEU A 127      939    857   1055     91   -144     28       C  
-ATOM    606  C   LEU A 127      47.636  35.413  25.480  1.00  6.84           C  
-ANISOU  606  C   LEU A 127      929    714    956    146   -193    -54       C  
-ATOM    607  O   LEU A 127      46.453  35.712  25.390  1.00  7.31           O  
-ANISOU  607  O   LEU A 127      833    933   1010    191   -167   -118       O  
-ATOM    608  CB  LEU A 127      47.952  34.592  23.156  1.00  7.28           C  
-ANISOU  608  CB  LEU A 127      859    897   1007    102    -86      4       C  
-ATOM    609  CG  LEU A 127      48.616  34.673  21.772  1.00 10.63           C  
-ANISOU  609  CG  LEU A 127     1348   1481   1210   -121     11     -9       C  
-ATOM    610  CD1 LEU A 127      48.038  33.668  20.808  1.00 10.49           C  
-ANISOU  610  CD1 LEU A 127     1246   1538   1202    160    101   -137       C  
-ATOM    611  CD2 LEU A 127      48.526  36.045  21.200  1.00 13.35           C  
-ANISOU  611  CD2 LEU A 127     1808   1736   1526   -102    -75    -43       C  
-ATOM    612  N   ILE A 128      48.170  35.035  26.636  1.00  7.46           N  
-ANISOU  612  N   ILE A 128      891    910   1033    118   -214    -59       N  
-ATOM    613  CA  ILE A 128      47.315  34.801  27.794  1.00  7.64           C  
-ANISOU  613  CA  ILE A 128      976    954    971    210   -222    -80       C  
-ATOM    614  C   ILE A 128      46.564  36.036  28.244  1.00  8.00           C  
-ANISOU  614  C   ILE A 128      989   1011   1039    159   -273    -98       C  
-ATOM    615  O   ILE A 128      45.395  35.946  28.622  1.00  7.90           O  
-ANISOU  615  O   ILE A 128      997   1094    908    240   -250   -167       O  
-ATOM    616  CB  ILE A 128      48.113  34.172  28.965  1.00  8.29           C  
-ANISOU  616  CB  ILE A 128     1085   1020   1042    149   -259    -97       C  
-ATOM    617  CG1 ILE A 128      48.359  32.704  28.654  1.00  8.88           C  
-ANISOU  617  CG1 ILE A 128     1093   1176   1104    191   -140    -73       C  
-ATOM    618  CG2 ILE A 128      47.378  34.331  30.296  1.00  9.36           C  
-ANISOU  618  CG2 ILE A 128     1269   1199   1087    307   -284    -19       C  
-ATOM    619  CD1 ILE A 128      49.231  31.997  29.681  1.00  8.97           C  
-ANISOU  619  CD1 ILE A 128     1293   1079   1035    171   -103     43       C  
-ATOM    620  N   ASP A 129      47.204  37.195  28.238  1.00  8.51           N  
-ANISOU  620  N   ASP A 129     1065    979   1186    173   -246   -178       N  
-ATOM    621  CA  ASP A 129      46.471  38.393  28.669  1.00  9.49           C  
-ANISOU  621  CA  ASP A 129     1216   1110   1277     95   -210   -226       C  
-ATOM    622  C   ASP A 129      45.258  38.658  27.759  1.00  8.91           C  
-ANISOU  622  C   ASP A 129     1109    965   1310     76   -162   -190       C  
-ATOM    623  O   ASP A 129      44.168  38.989  28.229  1.00  9.24           O  
-ANISOU  623  O   ASP A 129     1142   1033   1334    216   -274   -194       O  
-ATOM    624  CB  ASP A 129      47.372  39.622  28.706  1.00 10.89           C  
-ANISOU  624  CB  ASP A 129     1350   1246   1540    131   -243   -271       C  
-ATOM    625  CG  ASP A 129      48.340  39.610  29.856  1.00 13.80           C  
-ANISOU  625  CG  ASP A 129     1765   1539   1939    -72   -300   -297       C  
-ATOM    626  OD1 ASP A 129      48.138  38.856  30.823  1.00 17.48           O  
-ANISOU  626  OD1 ASP A 129     2298   2462   1882     75   -831   -619       O  
-ATOM    627  OD2 ASP A 129      49.323  40.366  29.856  1.00 19.74           O  
-ANISOU  627  OD2 ASP A 129     2156   2426   2917   -246   -730   -406       O  
-ATOM    628  N   GLU A 130      45.460  38.513  26.457  1.00  8.36           N  
-ANISOU  628  N   GLU A 130     1054    862   1258    134   -223   -119       N  
-ATOM    629  CA  GLU A 130      44.391  38.671  25.493  1.00  8.11           C  
-ANISOU  629  CA  GLU A 130     1077    823   1180    123   -166    -90       C  
-ATOM    630  C   GLU A 130      43.299  37.622  25.713  1.00  6.96           C  
-ANISOU  630  C   GLU A 130      964    745    935    196   -173    -89       C  
-ATOM    631  O   GLU A 130      42.112  37.961  25.784  1.00  7.16           O  
-ANISOU  631  O   GLU A 130      953    685   1081    219   -218   -151       O  
-ATOM    632  CB  GLU A 130      44.946  38.571  24.087  1.00  9.64           C  
-ANISOU  632  CB  GLU A 130     1219   1093   1348     53   -205     22       C  
-ATOM    633  CG  GLU A 130      43.852  38.614  23.055  1.00 12.17           C  
-ANISOU  633  CG  GLU A 130     1539   1551   1531    -64   -179    -47       C  
-ATOM    634  CD  GLU A 130      44.363  38.888  21.677  1.00 16.53           C  
-ANISOU  634  CD  GLU A 130     2292   2116   1870   -211   -112   -106       C  
-ATOM    635  OE1 GLU A 130      44.823  40.028  21.454  1.00 19.73           O  
-ANISOU  635  OE1 GLU A 130     3007   2243   2244   -301    -73   -327       O  
-ATOM    636  OE2 GLU A 130      44.281  37.973  20.824  1.00 18.71           O  
-ANISOU  636  OE2 GLU A 130     2725   2564   1820   -166    159   -199       O  
-ATOM    637  N   PHE A 131      43.693  36.354  25.829  1.00  6.20           N  
-ANISOU  637  N   PHE A 131      896    665    793    197   -145    -90       N  
-ATOM    638  CA  PHE A 131      42.727  35.280  26.009  1.00  5.86           C  
-ANISOU  638  CA  PHE A 131      870    677    677    177   -147    -72       C  
-ATOM    639  C   PHE A 131      41.898  35.505  27.276  1.00  5.65           C  
-ANISOU  639  C   PHE A 131      843    640    663    188   -192   -106       C  
-ATOM    640  O   PHE A 131      40.712  35.194  27.325  1.00  6.76           O  
-ANISOU  640  O   PHE A 131      904    878    785    228   -167    -86       O  
-ATOM    641  CB  PHE A 131      43.431  33.935  26.173  1.00  5.88           C  
-ANISOU  641  CB  PHE A 131      886    617    731    112   -192    -87       C  
-ATOM    642  CG  PHE A 131      44.124  33.394  24.936  1.00  5.82           C  
-ANISOU  642  CG  PHE A 131      884    676    648    129   -144    -69       C  
-ATOM    643  CD1 PHE A 131      43.766  33.773  23.652  1.00  5.97           C  
-ANISOU  643  CD1 PHE A 131      925    647    695    190   -185   -179       C  
-ATOM    644  CD2 PHE A 131      45.111  32.440  25.076  1.00  6.62           C  
-ANISOU  644  CD2 PHE A 131     1031    731    752    162   -166      6       C  
-ATOM    645  CE1 PHE A 131      44.392  33.211  22.560  1.00  7.02           C  
-ANISOU  645  CE1 PHE A 131     1134    828    703    174   -102   -112       C  
-ATOM    646  CE2 PHE A 131      45.734  31.866  23.994  1.00  7.07           C  
-ANISOU  646  CE2 PHE A 131     1047    823    814    187    -83    -50       C  
-ATOM    647  CZ  PHE A 131      45.371  32.243  22.729  1.00  7.47           C  
-ANISOU  647  CZ  PHE A 131     1197    917    724    144     -2   -183       C  
-ATOM    648  N   THR A 132      42.555  35.965  28.331  1.00  6.76           N  
-ANISOU  648  N   THR A 132      960    878    728    187   -155   -114       N  
-ATOM    649  CA  THR A 132      41.902  36.153  29.618  1.00  7.15           C  
-ANISOU  649  CA  THR A 132     1094    899    721    206   -179   -158       C  
-ATOM    650  C   THR A 132      40.857  37.266  29.519  1.00  7.41           C  
-ANISOU  650  C   THR A 132     1059    935    819    165   -203   -147       C  
-ATOM    651  O   THR A 132      39.728  37.098  29.968  1.00  8.18           O  
-ANISOU  651  O   THR A 132     1248    984    876    277   -210   -246       O  
-ATOM    652  CB  THR A 132      42.961  36.466  30.671  1.00  8.08           C  
-ANISOU  652  CB  THR A 132     1141   1079    850    244   -220   -171       C  
-ATOM    653  OG1 THR A 132      43.837  35.319  30.799  1.00  9.23           O  
-ANISOU  653  OG1 THR A 132     1307   1342    856    523   -286   -180       O  
-ATOM    654  CG2 THR A 132      42.317  36.703  32.045  1.00  9.02           C  
-ANISOU  654  CG2 THR A 132     1287   1356    784    270   -256   -156       C  
-ATOM    655  N   ALA A 133      41.215  38.379  28.891  1.00  7.29           N  
-ANISOU  655  N   ALA A 133     1005    873    889    205   -189   -176       N  
-ATOM    656  CA  ALA A 133      40.238  39.447  28.691  1.00  7.46           C  
-ANISOU  656  CA  ALA A 133     1002    897    936    180   -166   -165       C  
-ATOM    657  C   ALA A 133      39.079  38.962  27.828  1.00  7.25           C  
-ANISOU  657  C   ALA A 133      975    857    921    206   -173   -169       C  
-ATOM    658  O   ALA A 133      37.913  39.251  28.110  1.00  7.60           O  
-ANISOU  658  O   ALA A 133     1081    884    922    300   -187   -268       O  
-ATOM    659  CB  ALA A 133      40.884  40.648  28.056  1.00  8.36           C  
-ANISOU  659  CB  ALA A 133     1050    952   1173    154   -172   -236       C  
-ATOM    660  N   GLN A 134      39.407  38.205  26.784  1.00  6.26           N  
-ANISOU  660  N   GLN A 134      889    744    744    221   -140   -144       N  
-ATOM    661  CA  GLN A 134      38.394  37.702  25.859  1.00  6.28           C  
-ANISOU  661  CA  GLN A 134      834    761    790    164   -141   -104       C  
-ATOM    662  C   GLN A 134      37.407  36.738  26.509  1.00  6.27           C  
-ANISOU  662  C   GLN A 134      882    710    787    216   -118   -178       C  
-ATOM    663  O   GLN A 134      36.205  36.841  26.290  1.00  6.30           O  
-ANISOU  663  O   GLN A 134      886    793    713    171    -68   -167       O  
-ATOM    664  CB  GLN A 134      39.060  37.054  24.649  1.00  6.43           C  
-ANISOU  664  CB  GLN A 134      851    778    812    245   -121    -28       C  
-ATOM    665  CG  GLN A 134      39.747  38.048  23.740  1.00  6.42           C  
-ANISOU  665  CG  GLN A 134      898    704    834    196   -187    -53       C  
-ATOM    666  CD  GLN A 134      40.540  37.383  22.629  1.00  6.15           C  
-ANISOU  666  CD  GLN A 134      920    693    722    168   -105   -215       C  
-ATOM    667  OE1 GLN A 134      41.037  36.266  22.794  1.00  7.30           O  
-ANISOU  667  OE1 GLN A 134     1214    788    771    261    -54    -43       O  
-ATOM    668  NE2 GLN A 134      40.687  38.079  21.495  1.00  7.31           N  
-ANISOU  668  NE2 GLN A 134     1181    854    741     91   -107    -76       N  
-ATOM    669  N   ILE A 135      37.909  35.763  27.259  1.00  6.39           N  
-ANISOU  669  N   ILE A 135      927    746    754    201   -143    -81       N  
-ATOM    670  CA  ILE A 135      37.024  34.747  27.817  1.00  6.48           C  
-ANISOU  670  CA  ILE A 135      928    745    789    213    -63   -106       C  
-ATOM    671  C   ILE A 135      36.096  35.353  28.876  1.00  6.64           C  
-ANISOU  671  C   ILE A 135      973    734    812    144    -53   -153       C  
-ATOM    672  O   ILE A 135      34.943  34.951  28.996  1.00  7.17           O  
-ANISOU  672  O   ILE A 135     1074    838    812    201    -87   -119       O  
-ATOM    673  CB  ILE A 135      37.833  33.529  28.330  1.00  6.63           C  
-ANISOU  673  CB  ILE A 135      941    827    750    214    -46    -90       C  
-ATOM    674  CG1 ILE A 135      36.926  32.298  28.454  1.00  7.79           C  
-ANISOU  674  CG1 ILE A 135     1223    840    897    233      9   -145       C  
-ATOM    675  CG2 ILE A 135      38.523  33.819  29.643  1.00  7.36           C  
-ANISOU  675  CG2 ILE A 135     1010    890    897    182   -125     43       C  
-ATOM    676  CD1 ILE A 135      36.492  31.699  27.135  1.00  7.75           C  
-ANISOU  676  CD1 ILE A 135     1172    896    874    106     10    -30       C  
-ATOM    677  N   ARG A 136      36.579  36.351  29.603  1.00  7.16           N  
-ANISOU  677  N   ARG A 136     1005    894    818    181    -69   -149       N  
-ATOM    678  CA  ARG A 136      35.733  37.068  30.557  1.00  7.70           C  
-ANISOU  678  CA  ARG A 136     1073   1010    843    162    -15   -197       C  
-ATOM    679  C   ARG A 136      34.602  37.809  29.868  1.00  7.78           C  
-ANISOU  679  C   ARG A 136     1041   1032    883    139     23   -233       C  
-ATOM    680  O   ARG A 136      33.452  37.779  30.320  1.00  8.74           O  
-ANISOU  680  O   ARG A 136     1147   1162   1009    246    -11   -256       O  
-ATOM    681  CB  ARG A 136      36.586  38.024  31.387  1.00  8.82           C  
-ANISOU  681  CB  ARG A 136     1204   1176    971    161    -33   -161       C  
-ATOM    682  CG  ARG A 136      37.486  37.287  32.364  1.00 11.28           C  
-ANISOU  682  CG  ARG A 136     1388   1542   1353     60    -16   -210       C  
-ATOM    683  CD  ARG A 136      38.308  38.210  33.240  1.00 16.68           C  
-ANISOU  683  CD  ARG A 136     2165   2152   2019     94    -75   -203       C  
-ATOM    684  NE  ARG A 136      39.379  37.515  33.958  1.00 19.66           N  
-ANISOU  684  NE  ARG A 136     2454   2804   2211    114    -80   -241       N  
-ATOM    685  CZ  ARG A 136      39.225  36.603  34.933  1.00 25.21           C  
-ANISOU  685  CZ  ARG A 136     3076   3376   3126     43    -45   -129       C  
-ATOM    686  NH1 ARG A 136      38.026  36.220  35.366  1.00 26.61           N  
-ANISOU  686  NH1 ARG A 136     3299   3547   3261    -68    -26   -162       N  
-ATOM    687  NH2 ARG A 136      40.308  36.055  35.490  1.00 27.27           N  
-ANISOU  687  NH2 ARG A 136     3340   3615   3404    139     -1    -91       N  
-ATOM    688  N   ILE A 137      34.923  38.447  28.753  1.00  7.28           N  
-ANISOU  688  N   ILE A 137     1010    884    871    235    -35   -225       N  
-ATOM    689  CA  ILE A 137      33.910  39.150  27.977  1.00  7.52           C  
-ANISOU  689  CA  ILE A 137      976    918    962    252    -71   -209       C  
-ATOM    690  C   ILE A 137      32.882  38.165  27.436  1.00  7.82           C  
-ANISOU  690  C   ILE A 137      994   1041    935    257    -59   -268       C  
-ATOM    691  O   ILE A 137      31.678  38.419  27.509  1.00  8.16           O  
-ANISOU  691  O   ILE A 137     1065   1029   1004    364   -125   -241       O  
-ATOM    692  CB  ILE A 137      34.570  39.969  26.861  1.00  7.44           C  
-ANISOU  692  CB  ILE A 137      930    857   1039    268   -161   -280       C  
-ATOM    693  CG1 ILE A 137      35.288  41.175  27.473  1.00  8.23           C  
-ANISOU  693  CG1 ILE A 137     1182    868   1075    232   -274   -215       C  
-ATOM    694  CG2 ILE A 137      33.541  40.430  25.819  1.00  8.01           C  
-ANISOU  694  CG2 ILE A 137     1162    855   1025    149   -190   -232       C  
-ATOM    695  CD1 ILE A 137      36.288  41.802  26.581  1.00  8.69           C  
-ANISOU  695  CD1 ILE A 137     1260    737   1303    135   -376   -266       C  
-ATOM    696  N   LEU A 138      33.341  37.031  26.914  1.00  7.13           N  
-ANISOU  696  N   LEU A 138      948    865    896    207    -40   -198       N  
-ATOM    697  CA  LEU A 138      32.428  36.052  26.362  1.00  6.77           C  
-ANISOU  697  CA  LEU A 138      882    899    790    199    -22   -162       C  
-ATOM    698  C   LEU A 138      31.484  35.537  27.444  1.00  7.24           C  
-ANISOU  698  C   LEU A 138      942    974    834    213    -39   -209       C  
-ATOM    699  O   LEU A 138      30.280  35.402  27.221  1.00  7.64           O  
-ANISOU  699  O   LEU A 138      965   1126    809    239     27   -263       O  
-ATOM    700  CB  LEU A 138      33.222  34.901  25.751  1.00  6.43           C  
-ANISOU  700  CB  LEU A 138      858    899    685    199    -45   -123       C  
-ATOM    701  CG  LEU A 138      32.372  33.769  25.143  1.00  6.81           C  
-ANISOU  701  CG  LEU A 138      927    879    780    159     40   -161       C  
-ATOM    702  CD1 LEU A 138      31.374  34.259  24.092  1.00  7.37           C  
-ANISOU  702  CD1 LEU A 138      979    930    891    145    -84   -103       C  
-ATOM    703  CD2 LEU A 138      33.283  32.694  24.548  1.00  7.04           C  
-ANISOU  703  CD2 LEU A 138     1021    887    766    116     54   -197       C  
-ATOM    704  N   ASN A 139      32.022  35.227  28.615  1.00  7.69           N  
-ANISOU  704  N   ASN A 139      990   1016    913    249     29   -185       N  
-ATOM    705  CA  ASN A 139      31.179  34.725  29.696  1.00  8.88           C  
-ANISOU  705  CA  ASN A 139     1173   1186   1012    204     22    -88       C  
-ATOM    706  C   ASN A 139      30.121  35.733  30.110  1.00  8.26           C  
-ANISOU  706  C   ASN A 139     1054   1174    907    167     58   -117       C  
-ATOM    707  O   ASN A 139      28.970  35.381  30.359  1.00  8.97           O  
-ANISOU  707  O   ASN A 139     1168   1339    899    215     50   -140       O  
-ATOM    708  CB  ASN A 139      32.006  34.325  30.910  1.00 10.53           C  
-ANISOU  708  CB  ASN A 139     1375   1394   1229    271     51    -31       C  
-ATOM    709  CG  ASN A 139      31.258  33.343  31.811  1.00 13.85           C  
-ANISOU  709  CG  ASN A 139     1751   2062   1449    361     64    100       C  
-ATOM    710  OD1 ASN A 139      30.800  32.294  31.358  1.00 20.46           O  
-ANISOU  710  OD1 ASN A 139     2758   2619   2394    123    682    542       O  
-ATOM    711  ND2 ASN A 139      31.112  33.694  33.074  1.00 20.27           N  
-ANISOU  711  ND2 ASN A 139     2291   3187   2224    553    121    220       N  
-ATOM    712  N   ASP A 140      30.510  36.993  30.192  1.00  8.25           N  
-ANISOU  712  N   ASP A 140     1059   1174    902    242     64   -140       N  
-ATOM    713  CA  ASP A 140      29.551  38.021  30.568  1.00  8.96           C  
-ANISOU  713  CA  ASP A 140     1146   1155   1100    170     37   -180       C  
-ATOM    714  C   ASP A 140      28.439  38.145  29.539  1.00  9.09           C  
-ANISOU  714  C   ASP A 140     1122   1216   1112    171      1   -166       C  
-ATOM    715  O   ASP A 140      27.270  38.315  29.896  1.00  9.58           O  
-ANISOU  715  O   ASP A 140     1123   1333   1183    271      5   -355       O  
-ATOM    716  CB  ASP A 140      30.250  39.360  30.716  1.00  9.99           C  
-ANISOU  716  CB  ASP A 140     1231   1293   1269    160    -25   -140       C  
-ATOM    717  CG  ASP A 140      30.991  39.498  32.014  1.00 13.07           C  
-ANISOU  717  CG  ASP A 140     1784   1496   1686    106    -52    -50       C  
-ATOM    718  OD1 ASP A 140      30.782  38.718  32.969  1.00 15.69           O  
-ANISOU  718  OD1 ASP A 140     2163   2109   1690     34   -249   -128       O  
-ATOM    719  OD2 ASP A 140      31.827  40.389  32.153  1.00 17.33           O  
-ANISOU  719  OD2 ASP A 140     2204   1925   2455   -190   -365   -325       O  
-ATOM    720  N   LEU A 141      28.796  38.069  28.259  1.00  8.34           N  
-ANISOU  720  N   LEU A 141     1011   1180    977    292    -12   -217       N  
-ATOM    721  CA  LEU A 141      27.812  38.139  27.185  1.00  8.76           C  
-ANISOU  721  CA  LEU A 141     1087   1213   1026    243    -19   -161       C  
-ATOM    722  C   LEU A 141      26.823  37.001  27.301  1.00  8.61           C  
-ANISOU  722  C   LEU A 141     1060   1255    953    263    -37   -178       C  
-ATOM    723  O   LEU A 141      25.617  37.197  27.147  1.00  9.66           O  
-ANISOU  723  O   LEU A 141     1096   1453   1121    378    -44   -343       O  
-ATOM    724  CB  LEU A 141      28.499  38.093  25.821  1.00  9.23           C  
-ANISOU  724  CB  LEU A 141     1102   1335   1069    219   -157   -126       C  
-ATOM    725  CG  LEU A 141      29.283  39.331  25.386  1.00 11.63           C  
-ANISOU  725  CG  LEU A 141     1490   1619   1306    209   -148    -50       C  
-ATOM    726  CD1 LEU A 141      30.194  39.025  24.181  1.00 13.38           C  
-ANISOU  726  CD1 LEU A 141     1771   1829   1482    -32   -113    175       C  
-ATOM    727  CD2 LEU A 141      28.340  40.495  25.079  1.00 15.02           C  
-ANISOU  727  CD2 LEU A 141     1973   1769   1965    147    -42     -3       C  
-ATOM    728  N   LEU A 142      27.332  35.794  27.521  1.00  7.77           N  
-ANISOU  728  N   LEU A 142      962   1149    841    285     42   -217       N  
-ATOM    729  CA  LEU A 142      26.488  34.618  27.594  1.00  8.97           C  
-ANISOU  729  CA  LEU A 142     1106   1236   1066    155     -4   -128       C  
-ATOM    730  C   LEU A 142      25.557  34.697  28.794  1.00  8.89           C  
-ANISOU  730  C   LEU A 142     1069   1265   1042     94     39   -117       C  
-ATOM    731  O   LEU A 142      24.374  34.409  28.687  1.00  9.44           O  
-ANISOU  731  O   LEU A 142      987   1395   1203    191     74   -190       O  
-ATOM    732  CB  LEU A 142      27.364  33.370  27.690  1.00  9.17           C  
-ANISOU  732  CB  LEU A 142     1106   1201   1176    162    110   -143       C  
-ATOM    733  CG  LEU A 142      28.029  32.967  26.382  1.00 12.44           C  
-ANISOU  733  CG  LEU A 142     1544   1584   1596    100     50    -30       C  
-ATOM    734  CD1 LEU A 142      29.111  31.926  26.614  1.00 13.30           C  
-ANISOU  734  CD1 LEU A 142     1611   1711   1729    164    142     -6       C  
-ATOM    735  CD2 LEU A 142      27.012  32.481  25.363  1.00 14.86           C  
-ANISOU  735  CD2 LEU A 142     1864   1925   1855    106     53   -209       C  
-ATOM    736  N   LYS A 143      26.086  35.071  29.945  1.00  8.72           N  
-ANISOU  736  N   LYS A 143      961   1298   1051     96     37   -152       N  
-ATOM    737  CA  LYS A 143      25.247  35.179  31.129  1.00  9.43           C  
-ANISOU  737  CA  LYS A 143     1066   1342   1175     61     92    -77       C  
-ATOM    738  C   LYS A 143      24.135  36.190  30.945  1.00  9.12           C  
-ANISOU  738  C   LYS A 143      984   1354   1128     68     80   -143       C  
-ATOM    739  O   LYS A 143      22.986  35.947  31.315  1.00  9.79           O  
-ANISOU  739  O   LYS A 143      988   1465   1265    111    167   -130       O  
-ATOM    740  CB  LYS A 143      26.070  35.573  32.358  1.00 10.87           C  
-ANISOU  740  CB  LYS A 143     1179   1619   1331     89     93    -91       C  
-ATOM    741  CG  LYS A 143      26.927  34.449  32.895  1.00 12.50           C  
-ANISOU  741  CG  LYS A 143     1533   1824   1388     50     20    -26       C  
-ATOM    742  CD  LYS A 143      27.774  34.808  34.134  1.00 17.01           C  
-ANISOU  742  CD  LYS A 143     2088   2316   2057     95   -169     48       C  
-ATOM    743  CE  LYS A 143      27.219  35.909  35.031  1.00 20.35           C  
-ANISOU  743  CE  LYS A 143     2584   2720   2428      4   -127    -29       C  
-ATOM    744  NZ  LYS A 143      28.290  36.404  35.958  1.00 22.49           N  
-ANISOU  744  NZ  LYS A 143     2937   2991   2614    -99   -245   -156       N  
-ATOM    745  N   GLN A 144      24.477  37.338  30.380  1.00  9.33           N  
-ANISOU  745  N   GLN A 144     1043   1271   1229    176    127   -218       N  
-ATOM    746  CA  GLN A 144      23.484  38.386  30.173  1.00  9.90           C  
-ANISOU  746  CA  GLN A 144     1155   1292   1312    188     87   -184       C  
-ATOM    747  C   GLN A 144      22.413  37.949  29.185  1.00  9.92           C  
-ANISOU  747  C   GLN A 144     1078   1385   1304    201    103   -194       C  
-ATOM    748  O   GLN A 144      21.219  38.112  29.441  1.00 10.62           O  
-ANISOU  748  O   GLN A 144     1012   1630   1392    317    161   -325       O  
-ATOM    749  CB  GLN A 144      24.165  39.648  29.681  1.00 11.12           C  
-ANISOU  749  CB  GLN A 144     1309   1399   1515    184     52   -207       C  
-ATOM    750  CG  GLN A 144      23.252  40.863  29.651  1.00 16.66           C  
-ANISOU  750  CG  GLN A 144     2012   2066   2250     86     28    -87       C  
-ATOM    751  CD  GLN A 144      23.946  42.124  29.165  1.00 22.47           C  
-ANISOU  751  CD  GLN A 144     2699   2831   3005    195    227     -4       C  
-ATOM    752  OE1 GLN A 144      25.029  42.061  28.571  1.00 28.37           O  
-ANISOU  752  OE1 GLN A 144     3389   3601   3789    163    316     46       O  
-ATOM    753  NE2 GLN A 144      23.322  43.274  29.408  1.00 27.03           N  
-ANISOU  753  NE2 GLN A 144     3252   3437   3579    208    129     27       N  
-ATOM    754  N   LYS A 145      22.831  37.399  28.051  1.00  9.15           N  
-ANISOU  754  N   LYS A 145     1060   1301   1112    139     66   -192       N  
-ATOM    755  CA  LYS A 145      21.873  37.049  27.008  1.00  9.55           C  
-ANISOU  755  CA  LYS A 145     1132   1332   1164    156     23    -43       C  
-ATOM    756  C   LYS A 145      20.959  35.892  27.422  1.00  9.49           C  
-ANISOU  756  C   LYS A 145     1164   1314   1124    123    -50     11       C  
-ATOM    757  O   LYS A 145      19.757  35.942  27.177  1.00 10.14           O  
-ANISOU  757  O   LYS A 145     1206   1380   1266    194   -106     81       O  
-ATOM    758  CB  LYS A 145      22.595  36.735  25.699  1.00 10.92           C  
-ANISOU  758  CB  LYS A 145     1366   1550   1233    111     15    -53       C  
-ATOM    759  CG  LYS A 145      23.169  37.962  25.020  1.00 14.73           C  
-ANISOU  759  CG  LYS A 145     1803   1985   1809    121     59    -49       C  
-ATOM    760  CD  LYS A 145      22.061  38.815  24.385  1.00 20.01           C  
-ANISOU  760  CD  LYS A 145     2493   2593   2517     78    122     65       C  
-ATOM    761  CE  LYS A 145      22.383  39.270  22.975  1.00 23.04           C  
-ANISOU  761  CE  LYS A 145     2886   2963   2905     20      2     32       C  
-ATOM    762  NZ  LYS A 145      21.226  39.984  22.373  1.00 24.54           N  
-ANISOU  762  NZ  LYS A 145     2974   3091   3259     -4    -10     42       N  
-ATOM    763  N   TYR A 146      21.526  34.871  28.057  1.00  9.20           N  
-ANISOU  763  N   TYR A 146     1065   1160   1268    145    -77     31       N  
-ATOM    764  CA  TYR A 146      20.797  33.655  28.402  1.00  9.85           C  
-ANISOU  764  CA  TYR A 146     1162   1262   1318     78   -141     36       C  
-ATOM    765  C   TYR A 146      20.220  33.676  29.806  1.00  9.54           C  
-ANISOU  765  C   TYR A 146     1083   1241   1298     17   -142     61       C  
-ATOM    766  O   TYR A 146      19.592  32.711  30.224  1.00 10.17           O  
-ANISOU  766  O   TYR A 146     1163   1369   1332    -73   -249    166       O  
-ATOM    767  CB  TYR A 146      21.712  32.449  28.204  1.00 10.46           C  
-ANISOU  767  CB  TYR A 146     1155   1331   1489    169   -223     65       C  
-ATOM    768  CG  TYR A 146      21.706  32.017  26.793  1.00 12.50           C  
-ANISOU  768  CG  TYR A 146     1508   1450   1789    250   -298     58       C  
-ATOM    769  CD1 TYR A 146      20.689  31.196  26.327  1.00 13.87           C  
-ANISOU  769  CD1 TYR A 146     1512   1755   2003    297   -288   -340       C  
-ATOM    770  CD2 TYR A 146      22.652  32.468  25.904  1.00 13.89           C  
-ANISOU  770  CD2 TYR A 146     1901   1620   1755    152   -200    -78       C  
-ATOM    771  CE1 TYR A 146      20.622  30.791  25.045  1.00 17.29           C  
-ANISOU  771  CE1 TYR A 146     2256   2171   2139    317   -319   -203       C  
-ATOM    772  CE2 TYR A 146      22.596  32.067  24.577  1.00 16.58           C  
-ANISOU  772  CE2 TYR A 146     2421   2007   1870    169   -257    -30       C  
-ATOM    773  CZ  TYR A 146      21.550  31.230  24.158  1.00 14.69           C  
-ANISOU  773  CZ  TYR A 146     2195   1796   1590    302   -330   -265       C  
-ATOM    774  OH  TYR A 146      21.427  30.773  22.869  1.00 20.44           O  
-ANISOU  774  OH  TYR A 146     2925   2664   2178    500   -350   -390       O  
-ATOM    775  N   GLY A 147      20.382  34.783  30.533  1.00  9.87           N  
-ANISOU  775  N   GLY A 147     1170   1332   1247     64    -39    -27       N  
-ATOM    776  CA  GLY A 147      19.760  34.911  31.843  1.00 11.72           C  
-ANISOU  776  CA  GLY A 147     1381   1589   1482    -21    -11     32       C  
-ATOM    777  C   GLY A 147      20.317  33.930  32.860  1.00 11.96           C  
-ANISOU  777  C   GLY A 147     1387   1678   1479    -32     12    105       C  
-ATOM    778  O   GLY A 147      19.573  33.338  33.645  1.00 14.02           O  
-ANISOU  778  O   GLY A 147     1488   2116   1723     13     -9    351       O  
-ATOM    779  N   LEU A 148      21.634  33.755  32.833  1.00 12.33           N  
-ANISOU  779  N   LEU A 148     1481   1704   1498     45    -57    124       N  
-ATOM    780  CA  LEU A 148      22.315  32.805  33.699  1.00 13.21           C  
-ANISOU  780  CA  LEU A 148     1637   1783   1598     -7    -45     92       C  
-ATOM    781  C   LEU A 148      23.043  33.542  34.822  1.00 13.34           C  
-ANISOU  781  C   LEU A 148     1670   1912   1485     37      0     46       C  
-ATOM    782  O   LEU A 148      23.757  34.504  34.578  1.00 14.39           O  
-ANISOU  782  O   LEU A 148     1863   2164   1440    -70    -52    115       O  
-ATOM    783  CB  LEU A 148      23.308  32.007  32.874  1.00 13.24           C  
-ANISOU  783  CB  LEU A 148     1638   1742   1649     25   -128     39       C  
-ATOM    784  CG  LEU A 148      22.738  31.345  31.623  1.00 13.77           C  
-ANISOU  784  CG  LEU A 148     1783   1740   1707      5   -232     88       C  
-ATOM    785  CD1 LEU A 148      23.872  30.706  30.851  1.00 14.42           C  
-ANISOU  785  CD1 LEU A 148     1950   1766   1763     55   -258     36       C  
-ATOM    786  CD2 LEU A 148      21.679  30.327  31.985  1.00 15.46           C  
-ANISOU  786  CD2 LEU A 148     1824   1926   2123     94   -174    100       C  
-ATOM    787  N   SER A 149      22.851  33.110  36.065  1.00 14.64           N  
-ANISOU  787  N   SER A 149     1824   2091   1644     28     56      8       N  
-ATOM    788  CA  SER A 149      23.582  33.722  37.180  1.00 15.91           C  
-ANISOU  788  CA  SER A 149     2025   2193   1824     68     71    -74       C  
-ATOM    789  C   SER A 149      25.016  33.220  37.239  1.00 15.74           C  
-ANISOU  789  C   SER A 149     2026   2166   1786     69     28    -75       C  
-ATOM    790  O   SER A 149      25.906  33.933  37.695  1.00 16.72           O  
-ANISOU  790  O   SER A 149     2079   2355   1917    137     31   -236       O  
-ATOM    791  CB  SER A 149      22.890  33.453  38.519  1.00 16.52           C  
-ANISOU  791  CB  SER A 149     2113   2315   1849     68    114    -58       C  
-ATOM    792  OG  SER A 149      22.665  32.072  38.720  1.00 20.31           O  
-ANISOU  792  OG  SER A 149     2682   2906   2129    130    392     -4       O  
-ATOM    793  N   ARG A 150      25.221  31.999  36.748  1.00 15.50           N  
-ANISOU  793  N   ARG A 150     2008   2188   1694    145     47   -118       N  
-ATOM    794  CA  ARG A 150      26.490  31.295  36.843  1.00 16.14           C  
-ANISOU  794  CA  ARG A 150     2073   2187   1872     90     25   -114       C  
-ATOM    795  C   ARG A 150      26.639  30.363  35.652  1.00 14.93           C  
-ANISOU  795  C   ARG A 150     1872   2105   1695     84     72   -179       C  
-ATOM    796  O   ARG A 150      25.674  29.747  35.218  1.00 15.33           O  
-ANISOU  796  O   ARG A 150     1783   2254   1786     95    161   -213       O  
-ATOM    797  CB  ARG A 150      26.466  30.468  38.126  1.00 17.63           C  
-ANISOU  797  CB  ARG A 150     2311   2338   2049    141      2    -95       C  
-ATOM    798  CG  ARG A 150      27.762  29.931  38.658  1.00 21.93           C  
-ANISOU  798  CG  ARG A 150     2832   2766   2733     47     51    -66       C  
-ATOM    799  CD  ARG A 150      27.513  28.940  39.794  1.00 25.74           C  
-ANISOU  799  CD  ARG A 150     3312   3255   3210      4      4     -1       C  
-ATOM    800  NE  ARG A 150      26.772  27.784  39.287  1.00 29.19           N  
-ANISOU  800  NE  ARG A 150     3770   3599   3719    -18      2     -7       N  
-ATOM    801  CZ  ARG A 150      27.311  26.636  38.869  1.00 31.21           C  
-ANISOU  801  CZ  ARG A 150     3973   3915   3969      5     46    -27       C  
-ATOM    802  NH1 ARG A 150      28.625  26.420  38.917  1.00 31.45           N  
-ANISOU  802  NH1 ARG A 150     4035   3979   3934    -26     88     18       N  
-ATOM    803  NH2 ARG A 150      26.515  25.677  38.414  1.00 32.28           N  
-ANISOU  803  NH2 ARG A 150     4139   4069   4056    -20      2    -57       N  
-ATOM    804  N   VAL A 151      27.867  30.218  35.170  1.00 13.94           N  
-ANISOU  804  N   VAL A 151     1731   1999   1564     72    105   -211       N  
-ATOM    805  CA  VAL A 151      28.190  29.245  34.131  1.00 13.24           C  
-ANISOU  805  CA  VAL A 151     1730   1830   1470    106    103    -81       C  
-ATOM    806  C   VAL A 151      29.282  28.382  34.721  1.00 13.11           C  
-ANISOU  806  C   VAL A 151     1733   1840   1406    121    192     -9       C  
-ATOM    807  O   VAL A 151      30.386  28.861  34.915  1.00 14.71           O  
-ANISOU  807  O   VAL A 151     1880   2189   1517    141    157    201       O  
-ATOM    808  CB  VAL A 151      28.658  29.931  32.811  1.00 13.33           C  
-ANISOU  808  CB  VAL A 151     1712   1843   1508    109     82    -70       C  
-ATOM    809  CG1 VAL A 151      29.171  28.898  31.808  1.00 13.35           C  
-ANISOU  809  CG1 VAL A 151     1903   1807   1361    209    172     37       C  
-ATOM    810  CG2 VAL A 151      27.533  30.745  32.208  1.00 14.29           C  
-ANISOU  810  CG2 VAL A 151     1816   1950   1661    101     68    -50       C  
-ATOM    811  N   GLY A 152      28.970  27.123  35.014  1.00 12.98           N  
-ANISOU  811  N   GLY A 152     1688   1855   1388    117    296      7       N  
-ATOM    812  CA  GLY A 152      29.930  26.217  35.624  1.00 12.76           C  
-ANISOU  812  CA  GLY A 152     1703   1827   1317    102    274     67       C  
-ATOM    813  C   GLY A 152      31.217  26.079  34.810  1.00 11.91           C  
-ANISOU  813  C   GLY A 152     1698   1717   1111    128    329    113       C  
-ATOM    814  O   GLY A 152      32.314  26.148  35.350  1.00 12.35           O  
-ANISOU  814  O   GLY A 152     1866   1862    964    235    418    190       O  
-ATOM    815  N   ARG A 153      31.089  25.903  33.500  1.00 10.91           N  
-ANISOU  815  N   ARG A 153     1489   1655   1001    146    369    130       N  
-ATOM    816  CA  ARG A 153      32.245  25.756  32.624  1.00  9.81           C  
-ANISOU  816  CA  ARG A 153     1337   1372   1016    114    299     99       C  
-ATOM    817  C   ARG A 153      31.927  26.335  31.268  1.00  8.79           C  
-ANISOU  817  C   ARG A 153     1242   1240    858     82    201     80       C  
-ATOM    818  O   ARG A 153      30.934  25.977  30.666  1.00  9.93           O  
-ANISOU  818  O   ARG A 153     1416   1430    926    -10    346    203       O  
-ATOM    819  CB  ARG A 153      32.551  24.291  32.430  1.00 11.43           C  
-ANISOU  819  CB  ARG A 153     1428   1533   1382    118    258    118       C  
-ATOM    820  CG  ARG A 153      33.448  23.672  33.433  1.00 14.18           C  
-ANISOU  820  CG  ARG A 153     1884   1923   1579     59    242    113       C  
-ATOM    821  CD  ARG A 153      34.202  22.494  32.854  1.00 15.21           C  
-ANISOU  821  CD  ARG A 153     1975   1883   1922    325    -67     34       C  
-ATOM    822  NE  ARG A 153      33.289  21.370  32.815  1.00 14.87           N  
-ANISOU  822  NE  ARG A 153     2082   1743   1823    422    -38    100       N  
-ATOM    823  CZ  ARG A 153      33.487  20.223  32.189  1.00 14.70           C  
-ANISOU  823  CZ  ARG A 153     2101   1803   1680    306     16     40       C  
-ATOM    824  NH1 ARG A 153      34.570  20.005  31.461  1.00 14.98           N  
-ANISOU  824  NH1 ARG A 153     1979   1849   1861    239     57     91       N  
-ATOM    825  NH2 ARG A 153      32.560  19.289  32.289  1.00 14.65           N  
-ANISOU  825  NH2 ARG A 153     2059   1712   1793    272    153     67       N  
-ATOM    826  N   LEU A 154      32.793  27.225  30.811  1.00  7.68           N  
-ANISOU  826  N   LEU A 154     1164   1036    716     58    180     57       N  
-ATOM    827  CA  LEU A 154      32.731  27.797  29.465  1.00  7.08           C  
-ANISOU  827  CA  LEU A 154     1099   1005    585    109    158     17       C  
-ATOM    828  C   LEU A 154      33.976  27.334  28.740  1.00  6.84           C  
-ANISOU  828  C   LEU A 154     1046    991    560     64    156     22       C  
-ATOM    829  O   LEU A 154      35.084  27.477  29.252  1.00  7.39           O  
-ANISOU  829  O   LEU A 154     1105   1165    536    156    189    -99       O  
-ATOM    830  CB  LEU A 154      32.725  29.319  29.560  1.00  7.50           C  
-ANISOU  830  CB  LEU A 154     1193   1014    642     62    211     70       C  
-ATOM    831  CG  LEU A 154      32.873  30.090  28.246  1.00  7.93           C  
-ANISOU  831  CG  LEU A 154     1275   1002    733    134    177     36       C  
-ATOM    832  CD1 LEU A 154      31.716  29.780  27.296  1.00  8.71           C  
-ANISOU  832  CD1 LEU A 154     1378   1074    855    158    133    103       C  
-ATOM    833  CD2 LEU A 154      32.968  31.599  28.534  1.00  9.02           C  
-ANISOU  833  CD2 LEU A 154     1334   1079   1014     83     79     42       C  
-ATOM    834  N   VAL A 155      33.809  26.791  27.538  1.00  6.03           N  
-ANISOU  834  N   VAL A 155      930    890    471    125    197     24       N  
-ATOM    835  CA  VAL A 155      34.926  26.255  26.773  1.00  5.89           C  
-ANISOU  835  CA  VAL A 155      844    881    511     53    151     63       C  
-ATOM    836  C   VAL A 155      34.917  26.873  25.374  1.00  5.54           C  
-ANISOU  836  C   VAL A 155      771    862    469     94    192     30       C  
-ATOM    837  O   VAL A 155      33.995  26.650  24.604  1.00  6.53           O  
-ANISOU  837  O   VAL A 155      772   1128    581     91    130    125       O  
-ATOM    838  CB  VAL A 155      34.909  24.716  26.680  1.00  6.76           C  
-ANISOU  838  CB  VAL A 155     1029    904    635     98     80     85       C  
-ATOM    839  CG1 VAL A 155      36.202  24.222  26.039  1.00  8.10           C  
-ANISOU  839  CG1 VAL A 155     1260   1126    692    236    151     96       C  
-ATOM    840  CG2 VAL A 155      34.719  24.094  28.047  1.00  7.70           C  
-ANISOU  840  CG2 VAL A 155     1085   1000    838     60    212    118       C  
-ATOM    841  N   LEU A 156      35.971  27.620  25.072  1.00  5.42           N  
-ANISOU  841  N   LEU A 156      750    814    493     44    114     54       N  
-ATOM    842  CA  LEU A 156      36.210  28.228  23.773  1.00  4.94           C  
-ANISOU  842  CA  LEU A 156      694    710    470     54     90      4       C  
-ATOM    843  C   LEU A 156      37.316  27.429  23.090  1.00  4.52           C  
-ANISOU  843  C   LEU A 156      641    635    439     99      4     26       C  
-ATOM    844  O   LEU A 156      38.484  27.506  23.490  1.00  5.44           O  
-ANISOU  844  O   LEU A 156      829    710    526    139     -5    -70       O  
-ATOM    845  CB  LEU A 156      36.607  29.690  23.974  1.00  5.60           C  
-ANISOU  845  CB  LEU A 156      732    807    588    108     78     56       C  
-ATOM    846  CG  LEU A 156      37.126  30.467  22.762  1.00  5.93           C  
-ANISOU  846  CG  LEU A 156      792    804    653     67    130   -111       C  
-ATOM    847  CD1 LEU A 156      36.117  30.508  21.646  1.00  7.16           C  
-ANISOU  847  CD1 LEU A 156     1129    980    611    -82     57    124       C  
-ATOM    848  CD2 LEU A 156      37.515  31.885  23.179  1.00  6.76           C  
-ANISOU  848  CD2 LEU A 156     1002    755    809     31     63   -128       C  
-ATOM    849  N   ASN A 157      36.939  26.585  22.137  1.00  4.47           N  
-ANISOU  849  N   ASN A 157      588    651    458     59     74    -15       N  
-ATOM    850  CA  ASN A 157      37.900  25.754  21.439  1.00  4.44           C  
-ANISOU  850  CA  ASN A 157      649    568    466     68     66     19       C  
-ATOM    851  C   ASN A 157      38.314  26.397  20.134  1.00  4.28           C  
-ANISOU  851  C   ASN A 157      649    544    430     64     25    -33       C  
-ATOM    852  O   ASN A 157      37.515  27.024  19.426  1.00  5.13           O  
-ANISOU  852  O   ASN A 157      635    718    595    144     84     12       O  
-ATOM    853  CB  ASN A 157      37.338  24.354  21.156  1.00  5.45           C  
-ANISOU  853  CB  ASN A 157      838    690    542     19    110     61       C  
-ATOM    854  CG  ASN A 157      37.386  23.438  22.362  1.00  6.41           C  
-ANISOU  854  CG  ASN A 157     1076    641    718     47    147      9       C  
-ATOM    855  OD1 ASN A 157      36.355  23.029  22.888  1.00  7.57           O  
-ANISOU  855  OD1 ASN A 157     1211    775    888    -13    142    212       O  
-ATOM    856  ND2 ASN A 157      38.584  23.089  22.788  1.00  7.23           N  
-ANISOU  856  ND2 ASN A 157     1130    693    921    124     26    144       N  
-ATOM    857  N   GLY A 158      39.575  26.223  19.792  1.00  4.11           N  
-ANISOU  857  N   GLY A 158      596    505    459     92     13     -1       N  
-ATOM    858  CA  GLY A 158      40.106  26.724  18.551  1.00  4.46           C  
-ANISOU  858  CA  GLY A 158      607    560    525     70     49    -53       C  
-ATOM    859  C   GLY A 158      41.468  26.157  18.254  1.00  4.13           C  
-ANISOU  859  C   GLY A 158      592    458    519     46     -2     43       C  
-ATOM    860  O   GLY A 158      41.892  25.186  18.866  1.00  5.49           O  
-ANISOU  860  O   GLY A 158      703    948    434    193    135     64       O  
-ATOM    861  N   GLU A 159      42.113  26.744  17.262  1.00  4.62           N  
-ANISOU  861  N   GLU A 159      601    447    705     77     76     -1       N  
-ATOM    862  CA  GLU A 159      43.398  26.297  16.776  1.00  4.24           C  
-ANISOU  862  CA  GLU A 159      521    473    617     19    106    -54       C  
-ATOM    863  C   GLU A 159      44.436  27.375  17.118  1.00  4.08           C  
-ANISOU  863  C   GLU A 159      533    388    628     50    146    -15       C  
-ATOM    864  O   GLU A 159      44.274  28.539  16.738  1.00  5.04           O  
-ANISOU  864  O   GLU A 159      601    484    831     34     94     18       O  
-ATOM    865  CB  GLU A 159      43.357  26.097  15.255  1.00  4.81           C  
-ANISOU  865  CB  GLU A 159      608    458    759     22     37    -64       C  
-ATOM    866  CG  GLU A 159      44.491  25.209  14.746  1.00  4.82           C  
-ANISOU  866  CG  GLU A 159      643    598    590     53     78    -68       C  
-ATOM    867  CD  GLU A 159      44.255  23.724  14.943  1.00  5.04           C  
-ANISOU  867  CD  GLU A 159      680    574    660     41    189   -167       C  
-ATOM    868  OE1 GLU A 159      43.231  23.336  15.565  1.00  5.75           O  
-ANISOU  868  OE1 GLU A 159      692    603    889     22    190   -110       O  
-ATOM    869  OE2 GLU A 159      45.100  22.944  14.442  1.00  5.39           O  
-ANISOU  869  OE2 GLU A 159      708    557    779     73     78   -146       O  
-ATOM    870  N   LEU A 160      45.512  26.994  17.809  1.00  4.36           N  
-ANISOU  870  N   LEU A 160      617    444    595     14     61     48       N  
-ATOM    871  CA  LEU A 160      46.659  27.846  18.004  1.00  4.34           C  
-ANISOU  871  CA  LEU A 160      646    474    529     10     -1    -35       C  
-ATOM    872  C   LEU A 160      47.510  27.688  16.759  1.00  4.36           C  
-ANISOU  872  C   LEU A 160      527    468    662    -37     14    -10       C  
-ATOM    873  O   LEU A 160      47.818  26.562  16.386  1.00  4.99           O  
-ANISOU  873  O   LEU A 160      679    511    706     17     47   -114       O  
-ATOM    874  CB  LEU A 160      47.418  27.418  19.261  1.00  5.25           C  
-ANISOU  874  CB  LEU A 160      761    590    640     16     31      4       C  
-ATOM    875  CG  LEU A 160      48.573  28.325  19.641  1.00  6.13           C  
-ANISOU  875  CG  LEU A 160      848    750    728      3    -78    -76       C  
-ATOM    876  CD1 LEU A 160      48.077  29.633  20.255  1.00  8.44           C  
-ANISOU  876  CD1 LEU A 160     1196    963   1045    -34   -281    -68       C  
-ATOM    877  CD2 LEU A 160      49.487  27.609  20.622  1.00  7.53           C  
-ANISOU  877  CD2 LEU A 160     1092    875    892    -22   -164   -154       C  
-ATOM    878  N   PHE A 161      47.880  28.783  16.109  1.00  4.43           N  
-ANISOU  878  N   PHE A 161      603    521    558      5     28   -149       N  
-ATOM    879  CA  PHE A 161      48.520  28.686  14.803  1.00  4.57           C  
-ANISOU  879  CA  PHE A 161      602    566    566     12     17    -40       C  
-ATOM    880  C   PHE A 161      49.470  29.848  14.572  1.00  4.40           C  
-ANISOU  880  C   PHE A 161      571    552    548     28     60    -34       C  
-ATOM    881  O   PHE A 161      49.467  30.843  15.289  1.00  4.89           O  
-ANISOU  881  O   PHE A 161      646    602    609    -47    114    -74       O  
-ATOM    882  CB  PHE A 161      47.470  28.598  13.676  1.00  4.76           C  
-ANISOU  882  CB  PHE A 161      667    588    553     -1     40    -51       C  
-ATOM    883  CG  PHE A 161      46.759  29.892  13.374  1.00  4.71           C  
-ANISOU  883  CG  PHE A 161      629    684    473    -64     10     -4       C  
-ATOM    884  CD1 PHE A 161      47.172  30.694  12.326  1.00  6.14           C  
-ANISOU  884  CD1 PHE A 161      857    955    518    168    153     82       C  
-ATOM    885  CD2 PHE A 161      45.676  30.319  14.130  1.00  4.51           C  
-ANISOU  885  CD2 PHE A 161      592    533    588    -57     98    -51       C  
-ATOM    886  CE1 PHE A 161      46.505  31.868  12.005  1.00  7.13           C  
-ANISOU  886  CE1 PHE A 161      983   1035    690    129    206    296       C  
-ATOM    887  CE2 PHE A 161      45.016  31.493  13.827  1.00  5.32           C  
-ANISOU  887  CE2 PHE A 161      623    728    668    -45     61    -27       C  
-ATOM    888  CZ  PHE A 161      45.428  32.269  12.761  1.00  5.93           C  
-ANISOU  888  CZ  PHE A 161      730    841    680     78    154    115       C  
-ATOM    889  N   GLY A 162      50.253  29.706  13.517  1.00  4.75           N  
-ANISOU  889  N   GLY A 162      647    605    553    -16     38     29       N  
-ATOM    890  CA  GLY A 162      51.142  30.763  13.090  1.00  5.04           C  
-ANISOU  890  CA  GLY A 162      632    658    621     33     47     85       C  
-ATOM    891  C   GLY A 162      52.583  30.559  13.483  1.00  4.90           C  
-ANISOU  891  C   GLY A 162      648    627    585     25     15    114       C  
-ATOM    892  O   GLY A 162      53.076  29.439  13.562  1.00  5.37           O  
-ANISOU  892  O   GLY A 162      680    515    842     35     28    127       O  
-ATOM    893  N   ALA A 163      53.268  31.674  13.690  1.00  5.47           N  
-ANISOU  893  N   ALA A 163      700    617    761     -9     -7    127       N  
-ATOM    894  CA  ALA A 163      54.698  31.727  13.990  1.00  6.11           C  
-ANISOU  894  CA  ALA A 163      717    737    866    -35    -10    135       C  
-ATOM    895  C   ALA A 163      55.544  31.086  12.892  1.00  5.70           C  
-ANISOU  895  C   ALA A 163      679    682    804    -53    -18    178       C  
-ATOM    896  O   ALA A 163      56.596  30.512  13.144  1.00  6.58           O  
-ANISOU  896  O   ALA A 163      714    741   1042    -18   -114    115       O  
-ATOM    897  CB  ALA A 163      54.994  31.162  15.378  1.00  6.60           C  
-ANISOU  897  CB  ALA A 163      802    891    813    -75      3     24       C  
-ATOM    898  N   LYS A 164      55.104  31.241  11.644  1.00  5.70           N  
-ANISOU  898  N   LYS A 164      629    742    791    -30    -11    209       N  
-ATOM    899  CA  LYS A 164      55.882  30.826  10.477  1.00  6.12           C  
-ANISOU  899  CA  LYS A 164      711    720    891      9     32    161       C  
-ATOM    900  C   LYS A 164      55.351  31.544   9.254  1.00  5.51           C  
-ANISOU  900  C   LYS A 164      669    626    799    -22    106    192       C  
-ATOM    901  O   LYS A 164      54.186  31.405   8.917  1.00  5.81           O  
-ANISOU  901  O   LYS A 164      650    751    804    -45    166    160       O  
-ATOM    902  CB  LYS A 164      55.801  29.314  10.266  1.00  6.71           C  
-ANISOU  902  CB  LYS A 164      799    785    964     54     35    254       C  
-ATOM    903  CG  LYS A 164      56.576  28.818   9.031  1.00  8.60           C  
-ANISOU  903  CG  LYS A 164     1063    914   1290     66     70    271       C  
-ATOM    904  CD  LYS A 164      56.468  27.308   8.790  1.00 11.35           C  
-ANISOU  904  CD  LYS A 164     1538   1267   1506    200    122     93       C  
-ATOM    905  CE  LYS A 164      57.221  26.868   7.551  1.00 14.30           C  
-ANISOU  905  CE  LYS A 164     1933   1537   1962    203    -61    -38       C  
-ATOM    906  NZ  LYS A 164      57.214  25.386   7.381  1.00 16.78           N  
-ANISOU  906  NZ  LYS A 164     2171   1767   2436    232    -95   -166       N  
-ATOM    907  N   TYR A 165      56.218  32.278   8.563  1.00  6.02           N  
-ANISOU  907  N   TYR A 165      663    736    889    -31     35    268       N  
-ATOM    908  CA  TYR A 165      55.830  32.906   7.305  1.00  5.96           C  
-ANISOU  908  CA  TYR A 165      734    726    801    -17      7    152       C  
-ATOM    909  C   TYR A 165      57.102  33.250   6.543  1.00  6.16           C  
-ANISOU  909  C   TYR A 165      887    649    801    -42     22    213       C  
-ATOM    910  O   TYR A 165      57.720  34.292   6.779  1.00  7.12           O  
-ANISOU  910  O   TYR A 165      954    806    943   -230    -39    231       O  
-ATOM    911  CB  TYR A 165      54.962  34.144   7.528  1.00  6.32           C  
-ANISOU  911  CB  TYR A 165      846    764    788     39     44    145       C  
-ATOM    912  CG  TYR A 165      54.187  34.508   6.293  1.00  5.81           C  
-ANISOU  912  CG  TYR A 165      769    643    794     58     80    213       C  
-ATOM    913  CD1 TYR A 165      52.976  33.902   6.023  1.00  6.02           C  
-ANISOU  913  CD1 TYR A 165      749    703    832     15    179    279       C  
-ATOM    914  CD2 TYR A 165      54.674  35.425   5.367  1.00  6.39           C  
-ANISOU  914  CD2 TYR A 165      747    712    968    -35    -21    247       C  
-ATOM    915  CE1 TYR A 165      52.254  34.211   4.892  1.00  6.30           C  
-ANISOU  915  CE1 TYR A 165      702    675   1015    -74     43    277       C  
-ATOM    916  CE2 TYR A 165      53.964  35.734   4.239  1.00  6.21           C  
-ANISOU  916  CE2 TYR A 165      759    672    927    -80     82    304       C  
-ATOM    917  CZ  TYR A 165      52.745  35.134   4.002  1.00  5.60           C  
-ANISOU  917  CZ  TYR A 165      644    633    848    -12     78    226       C  
-ATOM    918  OH  TYR A 165      52.013  35.422   2.871  1.00  6.88           O  
-ANISOU  918  OH  TYR A 165      829    908    878    -91    -65    297       O  
-ATOM    919  N   LYS A 166      57.500  32.377   5.633  1.00  6.45           N  
-ANISOU  919  N   LYS A 166      761    759    928    -76    108    200       N  
-ATOM    920  CA  LYS A 166      58.833  32.445   5.045  1.00  7.62           C  
-ANISOU  920  CA  LYS A 166      933    886   1074     41    129    201       C  
-ATOM    921  C   LYS A 166      58.873  33.338   3.812  1.00  7.29           C  
-ANISOU  921  C   LYS A 166      978    812    979     -1    210    260       C  
-ATOM    922  O   LYS A 166      59.074  32.889   2.688  1.00  9.59           O  
-ANISOU  922  O   LYS A 166     1551    965   1125     30    115    298       O  
-ATOM    923  CB  LYS A 166      59.318  31.032   4.731  1.00  8.54           C  
-ANISOU  923  CB  LYS A 166      909   1028   1306     36    225    258       C  
-ATOM    924  CG  LYS A 166      59.532  30.172   5.967  1.00 13.17           C  
-ANISOU  924  CG  LYS A 166     1520   1573   1910     63    142    116       C  
-ATOM    925  CD  LYS A 166      59.994  28.757   5.625  1.00 17.90           C  
-ANISOU  925  CD  LYS A 166     2249   2161   2388     74     66    127       C  
-ATOM    926  CE  LYS A 166      61.454  28.711   5.216  1.00 21.76           C  
-ANISOU  926  CE  LYS A 166     2737   2642   2885    121     94     51       C  
-ATOM    927  NZ  LYS A 166      61.883  27.319   4.891  1.00 23.52           N  
-ANISOU  927  NZ  LYS A 166     3019   2798   3119     86    119    -51       N  
-ATOM    928  N   HIS A 167      58.687  34.626   4.037  1.00  7.89           N  
-ANISOU  928  N   HIS A 167     1184    851    961      9    253    225       N  
-ATOM    929  CA  HIS A 167      58.818  35.647   2.997  1.00  7.31           C  
-ANISOU  929  CA  HIS A 167     1034    818    923    -32    187    256       C  
-ATOM    930  C   HIS A 167      59.863  36.638   3.462  1.00  7.93           C  
-ANISOU  930  C   HIS A 167     1085    939    989    -21    214    388       C  
-ATOM    931  O   HIS A 167      59.816  37.080   4.607  1.00  8.60           O  
-ANISOU  931  O   HIS A 167     1139    981   1147    -67    136    377       O  
-ATOM    932  CB  HIS A 167      57.490  36.361   2.794  1.00  7.32           C  
-ANISOU  932  CB  HIS A 167     1035    818    929   -134    214    211       C  
-ATOM    933  CG  HIS A 167      57.449  37.225   1.580  1.00  6.97           C  
-ANISOU  933  CG  HIS A 167      879    745   1023   -144    143    267       C  
-ATOM    934  ND1 HIS A 167      58.188  38.380   1.463  1.00  7.93           N  
-ANISOU  934  ND1 HIS A 167      985    873   1153    -74     64    265       N  
-ATOM    935  CD2 HIS A 167      56.758  37.086   0.425  1.00  7.78           C  
-ANISOU  935  CD2 HIS A 167     1016    832   1106   -148    162    121       C  
-ATOM    936  CE1 HIS A 167      57.937  38.921   0.287  1.00  7.91           C  
-ANISOU  936  CE1 HIS A 167     1056   1004    945   -117    -27    411       C  
-ATOM    937  NE2 HIS A 167      57.070  38.164  -0.360  1.00  8.24           N  
-ANISOU  937  NE2 HIS A 167     1179    888   1064     90    139    235       N  
-ATOM    938  N   PRO A 168      60.808  37.014   2.593  1.00  8.59           N  
-ANISOU  938  N   PRO A 168     1069   1039   1155     33    151    261       N  
-ATOM    939  CA  PRO A 168      61.913  37.873   3.023  1.00  9.49           C  
-ANISOU  939  CA  PRO A 168     1120   1213   1270    -59     72    328       C  
-ATOM    940  C   PRO A 168      61.504  39.276   3.476  1.00  9.50           C  
-ANISOU  940  C   PRO A 168     1107   1176   1324   -107     41    308       C  
-ATOM    941  O   PRO A 168      62.281  39.949   4.142  1.00 11.25           O  
-ANISOU  941  O   PRO A 168     1228   1334   1710   -148   -108    373       O  
-ATOM    942  CB  PRO A 168      62.822  37.933   1.786  1.00 10.48           C  
-ANISOU  942  CB  PRO A 168     1134   1331   1515     -6    169    256       C  
-ATOM    943  CG  PRO A 168      61.959  37.576   0.672  1.00 10.90           C  
-ANISOU  943  CG  PRO A 168     1285   1432   1422     -1    235    241       C  
-ATOM    944  CD  PRO A 168      60.958  36.589   1.193  1.00  9.10           C  
-ANISOU  944  CD  PRO A 168     1085   1192   1181     23    245    253       C  
-ATOM    945  N   LEU A 169      60.311  39.734   3.120  1.00  8.31           N  
-ANISOU  945  N   LEU A 169     1007   1020   1128    -84     45    311       N  
-ATOM    946  CA  LEU A 169      59.836  41.040   3.570  1.00  8.41           C  
-ANISOU  946  CA  LEU A 169     1103    975   1116   -104     24    186       C  
-ATOM    947  C   LEU A 169      59.017  40.970   4.856  1.00  8.86           C  
-ANISOU  947  C   LEU A 169     1270    970   1126    -66     -4    177       C  
-ATOM    948  O   LEU A 169      58.486  41.987   5.300  1.00 10.19           O  
-ANISOU  948  O   LEU A 169     1600   1081   1190     13     52    228       O  
-ATOM    949  CB  LEU A 169      59.023  41.723   2.467  1.00  8.31           C  
-ANISOU  949  CB  LEU A 169     1075    925   1156   -191     31    248       C  
-ATOM    950  CG  LEU A 169      59.792  41.953   1.178  1.00  8.27           C  
-ANISOU  950  CG  LEU A 169      974    959   1208    -93    164    302       C  
-ATOM    951  CD1 LEU A 169      58.910  42.692   0.185  1.00  7.88           C  
-ANISOU  951  CD1 LEU A 169     1003    912   1079   -132    127    289       C  
-ATOM    952  CD2 LEU A 169      61.095  42.704   1.371  1.00  9.21           C  
-ANISOU  952  CD2 LEU A 169     1136   1133   1228   -129     64    442       C  
-ATOM    953  N   VAL A 170      58.907  39.776   5.443  1.00  8.07           N  
-ANISOU  953  N   VAL A 170     1082    960   1021   -120     51    216       N  
-ATOM    954  CA  VAL A 170      58.132  39.565   6.643  1.00  8.21           C  
-ANISOU  954  CA  VAL A 170     1062   1044   1013    -71     71    174       C  
-ATOM    955  C   VAL A 170      59.086  39.053   7.713  1.00  8.68           C  
-ANISOU  955  C   VAL A 170     1150   1094   1054   -206     36    182       C  
-ATOM    956  O   VAL A 170      59.393  37.872   7.771  1.00  8.96           O  
-ANISOU  956  O   VAL A 170     1062   1212   1131    -11     49    233       O  
-ATOM    957  CB  VAL A 170      57.001  38.572   6.386  1.00  7.62           C  
-ANISOU  957  CB  VAL A 170     1017    952    925    -62     77    162       C  
-ATOM    958  CG1 VAL A 170      56.176  38.354   7.649  1.00  8.07           C  
-ANISOU  958  CG1 VAL A 170     1034   1152    880    -45     67    191       C  
-ATOM    959  CG2 VAL A 170      56.118  39.071   5.248  1.00  6.96           C  
-ANISOU  959  CG2 VAL A 170      989    871    784    -95    177    191       C  
-ATOM    960  N   PRO A 171      59.616  39.942   8.543  1.00  9.76           N  
-ANISOU  960  N   PRO A 171     1319   1254   1135   -285    -42    217       N  
-ATOM    961  CA  PRO A 171      60.525  39.500   9.599  1.00 10.36           C  
-ANISOU  961  CA  PRO A 171     1326   1357   1250   -253    -15    182       C  
-ATOM    962  C   PRO A 171      59.898  38.469  10.522  1.00  9.70           C  
-ANISOU  962  C   PRO A 171     1218   1289   1178   -285    -15    214       C  
-ATOM    963  O   PRO A 171      58.702  38.505  10.796  1.00  9.84           O  
-ANISOU  963  O   PRO A 171     1263   1355   1120   -304     -4    243       O  
-ATOM    964  CB  PRO A 171      60.825  40.794  10.357  1.00 11.81           C  
-ANISOU  964  CB  PRO A 171     1562   1527   1398   -282    -59    168       C  
-ATOM    965  CG  PRO A 171      60.617  41.873   9.351  1.00 12.29           C  
-ANISOU  965  CG  PRO A 171     1581   1571   1516   -243    -32    132       C  
-ATOM    966  CD  PRO A 171      59.460  41.410   8.533  1.00 10.90           C  
-ANISOU  966  CD  PRO A 171     1542   1391   1207   -302    -98    155       C  
-ATOM    967  N   LYS A 172      60.722  37.567  11.011  1.00 10.05           N  
-ANISOU  967  N   LYS A 172     1211   1369   1238   -219     36    184       N  
-ATOM    968  CA  LYS A 172      60.276  36.701  12.083  1.00 10.08           C  
-ANISOU  968  CA  LYS A 172     1298   1304   1228   -161    -14    150       C  
-ATOM    969  C   LYS A 172      59.886  37.539  13.303  1.00  9.08           C  
-ANISOU  969  C   LYS A 172     1208   1138   1102   -205   -127    136       C  
-ATOM    970  O   LYS A 172      60.333  38.681  13.476  1.00  9.92           O  
-ANISOU  970  O   LYS A 172     1337   1244   1186   -376   -140    145       O  
-ATOM    971  CB  LYS A 172      61.338  35.656  12.436  1.00 11.58           C  
-ANISOU  971  CB  LYS A 172     1419   1519   1461    -83    -16     86       C  
-ATOM    972  CG  LYS A 172      61.605  34.672  11.313  1.00 13.66           C  
-ANISOU  972  CG  LYS A 172     1667   1910   1611    -50     55     93       C  
-ATOM    973  CD  LYS A 172      62.384  33.454  11.751  1.00 16.99           C  
-ANISOU  973  CD  LYS A 172     2151   2189   2116    -22     21    -48       C  
-ATOM    974  CE  LYS A 172      61.490  32.415  12.416  1.00 18.27           C  
-ANISOU  974  CE  LYS A 172     2336   2281   2325     24    -18     52       C  
-ATOM    975  NZ  LYS A 172      62.228  31.163  12.739  1.00 19.99           N  
-ANISOU  975  NZ  LYS A 172     2623   2455   2516    164   -130     50       N  
-ATOM    976  N   SER A 173      59.056  36.964  14.160  1.00  8.96           N  
-ANISOU  976  N   SER A 173     1220   1022   1159   -217    -67    162       N  
-ATOM    977  CA  SER A 173      58.606  37.657  15.345  1.00  8.59           C  
-ANISOU  977  CA  SER A 173     1136    996   1128   -180    -82     96       C  
-ATOM    978  C   SER A 173      59.796  38.051  16.215  1.00  9.29           C  
-ANISOU  978  C   SER A 173     1226   1070   1232   -177    -96     86       C  
-ATOM    979  O   SER A 173      60.725  37.274  16.402  1.00  9.80           O  
-ANISOU  979  O   SER A 173     1264   1198   1261   -247   -149     81       O  
-ATOM    980  CB  SER A 173      57.679  36.765  16.168  1.00  7.98           C  
-ANISOU  980  CB  SER A 173     1160    910    961   -178    -54    179       C  
-ATOM    981  OG  SER A 173      57.270  37.437  17.349  1.00  8.75           O  
-ANISOU  981  OG  SER A 173     1260    970   1094   -256    -75     21       O  
-ATOM    982  N   GLU A 174      59.717  39.252  16.769  1.00  9.37           N  
-ANISOU  982  N   GLU A 174     1262   1078   1220   -296   -149     77       N  
-ATOM    983  CA  GLU A 174      60.665  39.738  17.763  1.00 10.66           C  
-ANISOU  983  CA  GLU A 174     1340   1259   1449   -274   -118      6       C  
-ATOM    984  C   GLU A 174      60.154  39.528  19.185  1.00  9.97           C  
-ANISOU  984  C   GLU A 174     1334   1146   1308   -259   -147    -69       C  
-ATOM    985  O   GLU A 174      60.818  39.925  20.144  1.00 11.45           O  
-ANISOU  985  O   GLU A 174     1467   1367   1515   -431   -241   -130       O  
-ATOM    986  CB  GLU A 174      60.946  41.223  17.529  1.00 11.75           C  
-ANISOU  986  CB  GLU A 174     1588   1340   1536   -333    -44      5       C  
-ATOM    987  CG  GLU A 174      61.622  41.529  16.198  1.00 16.35           C  
-ANISOU  987  CG  GLU A 174     2128   2017   2063   -375     48      3       C  
-ATOM    988  CD  GLU A 174      61.910  43.012  16.009  1.00 21.99           C  
-ANISOU  988  CD  GLU A 174     2906   2668   2779   -248    189     10       C  
-ATOM    989  OE1 GLU A 174      61.347  43.838  16.756  1.00 26.41           O  
-ANISOU  989  OE1 GLU A 174     3593   2929   3512   -240    175     31       O  
-ATOM    990  OE2 GLU A 174      62.695  43.358  15.107  1.00 27.62           O  
-ANISOU  990  OE2 GLU A 174     3570   3365   3560   -280    200     46       O  
-ATOM    991  N   LYS A 175      58.978  38.921  19.336  1.00  9.11           N  
-ANISOU  991  N   LYS A 175     1238   1008   1212   -187   -154    -66       N  
-ATOM    992  CA  LYS A 175      58.359  38.796  20.649  1.00  8.62           C  
-ANISOU  992  CA  LYS A 175     1194    899   1182   -125   -104   -114       C  
-ATOM    993  C   LYS A 175      58.905  37.613  21.426  1.00  8.33           C  
-ANISOU  993  C   LYS A 175     1180    841   1141   -130    -90    -85       C  
-ATOM    994  O   LYS A 175      59.348  36.621  20.854  1.00  8.34           O  
-ANISOU  994  O   LYS A 175     1153    866   1147    -84    -22   -167       O  
-ATOM    995  CB  LYS A 175      56.859  38.630  20.501  1.00  9.28           C  
-ANISOU  995  CB  LYS A 175     1230   1063   1231    -48   -101    -69       C  
-ATOM    996  CG  LYS A 175      56.179  39.782  19.789  1.00 10.49           C  
-ANISOU  996  CG  LYS A 175     1389   1160   1436     -1   -103   -180       C  
-ATOM    997  CD  LYS A 175      54.665  39.649  19.821  1.00 11.91           C  
-ANISOU  997  CD  LYS A 175     1483   1343   1697    122   -116   -116       C  
-ATOM    998  CE  LYS A 175      54.007  40.621  18.865  1.00 13.49           C  
-ANISOU  998  CE  LYS A 175     1601   1555   1967    176   -258    -97       C  
-ATOM    999  NZ  LYS A 175      52.540  40.684  19.055  1.00 16.30           N  
-ANISOU  999  NZ  LYS A 175     1865   1758   2569      0   -205     48       N  
-ATOM   1000  N   TRP A 176      58.847  37.730  22.746  1.00  9.09           N  
-ANISOU 1000  N   TRP A 176     1273   1028   1152    -24    -68    -58       N  
-ATOM   1001  CA  TRP A 176      59.259  36.679  23.672  1.00  9.48           C  
-ANISOU 1001  CA  TRP A 176     1332   1088   1182      0    -35    -77       C  
-ATOM   1002  C   TRP A 176      58.151  36.516  24.683  1.00 10.05           C  
-ANISOU 1002  C   TRP A 176     1382   1161   1274     88     31    -59       C  
-ATOM   1003  O   TRP A 176      57.694  37.516  25.237  1.00 12.24           O  
-ANISOU 1003  O   TRP A 176     1872   1241   1538    135    274   -132       O  
-ATOM   1004  CB  TRP A 176      60.541  37.066  24.438  1.00 10.67           C  
-ANISOU 1004  CB  TRP A 176     1502   1283   1268     -6   -136    -68       C  
-ATOM   1005  CG  TRP A 176      61.766  37.066  23.591  1.00 11.13           C  
-ANISOU 1005  CG  TRP A 176     1315   1499   1415   -256   -227    -10       C  
-ATOM   1006  CD1 TRP A 176      62.057  37.928  22.581  1.00 13.43           C  
-ANISOU 1006  CD1 TRP A 176     1516   1798   1786   -272   -181     81       C  
-ATOM   1007  CD2 TRP A 176      62.882  36.163  23.670  1.00 11.31           C  
-ANISOU 1007  CD2 TRP A 176     1281   1656   1358   -350   -266   -121       C  
-ATOM   1008  NE1 TRP A 176      63.266  37.607  22.013  1.00 13.19           N  
-ANISOU 1008  NE1 TRP A 176     1509   1817   1685   -366   -157     93       N  
-ATOM   1009  CE2 TRP A 176      63.796  36.533  22.664  1.00 12.63           C  
-ANISOU 1009  CE2 TRP A 176     1320   1818   1661   -385   -218   -101       C  
-ATOM   1010  CE3 TRP A 176      63.206  35.080  24.494  1.00 11.02           C  
-ANISOU 1010  CE3 TRP A 176     1441   1362   1381   -283   -220   -180       C  
-ATOM   1011  CZ2 TRP A 176      65.006  35.866  22.458  1.00 13.38           C  
-ANISOU 1011  CZ2 TRP A 176     1392   1902   1788   -395   -113    -37       C  
-ATOM   1012  CZ3 TRP A 176      64.418  34.420  24.289  1.00 12.37           C  
-ANISOU 1012  CZ3 TRP A 176     1537   1717   1446   -141   -131      6       C  
-ATOM   1013  CH2 TRP A 176      65.288  34.808  23.271  1.00 12.86           C  
-ANISOU 1013  CH2 TRP A 176     1412   1772   1701   -267   -287   -177       C  
-ATOM   1014  N   CYS A 177      57.725  35.287  24.942  1.00  9.33           N  
-ANISOU 1014  N   CYS A 177     1180   1215   1147     69     -9     -8       N  
-ATOM   1015  CA  CYS A 177      56.742  35.045  25.977  1.00  9.81           C  
-ANISOU 1015  CA  CYS A 177     1175   1345   1206     49    -20     16       C  
-ATOM   1016  C   CYS A 177      57.442  34.914  27.313  1.00  9.02           C  
-ANISOU 1016  C   CYS A 177     1052   1284   1091     22     16     17       C  
-ATOM   1017  O   CYS A 177      58.643  34.669  27.369  1.00  9.54           O  
-ANISOU 1017  O   CYS A 177      956   1593   1075     47    -54    -14       O  
-ATOM   1018  CB  CYS A 177      55.923  33.792  25.691  1.00 10.49           C  
-ANISOU 1018  CB  CYS A 177     1255   1573   1155     -3   -100     27       C  
-ATOM   1019  SG  CYS A 177      56.801  32.236  25.857  1.00 10.78           S  
-ANISOU 1019  SG  CYS A 177     1369   1318   1409   -182   -142   -110       S  
-ATOM   1020  N   THR A 178      56.672  35.069  28.383  1.00  9.38           N  
-ANISOU 1020  N   THR A 178     1097   1301   1165     -1     63    -42       N  
-ATOM   1021  CA  THR A 178      57.155  34.888  29.741  1.00  9.89           C  
-ANISOU 1021  CA  THR A 178     1221   1279   1256    -35    121    -81       C  
-ATOM   1022  C   THR A 178      56.216  33.958  30.490  1.00  9.84           C  
-ANISOU 1022  C   THR A 178     1174   1273   1289    -30    127   -110       C  
-ATOM   1023  O   THR A 178      55.011  34.197  30.549  1.00 10.99           O  
-ANISOU 1023  O   THR A 178     1106   1445   1622     24    244     45       O  
-ATOM   1024  CB  THR A 178      57.227  36.230  30.487  1.00 10.65           C  
-ANISOU 1024  CB  THR A 178     1306   1421   1317   -146    178    -66       C  
-ATOM   1025  OG1 THR A 178      58.014  37.179  29.745  1.00 11.94           O  
-ANISOU 1025  OG1 THR A 178     1802   1358   1376   -145    375   -228       O  
-ATOM   1026  CG2 THR A 178      57.939  36.057  31.839  1.00 12.01           C  
-ANISOU 1026  CG2 THR A 178     1629   1471   1461    -86    168   -230       C  
-ATOM   1027  N   LEU A 179      56.772  32.922  31.084  1.00  8.75           N  
-ANISOU 1027  N   LEU A 179     1054   1171   1099   -121     -3   -103       N  
-ATOM   1028  CA  LEU A 179      55.991  31.987  31.881  1.00  9.26           C  
-ANISOU 1028  CA  LEU A 179     1250   1101   1165    -86    -25   -104       C  
-ATOM   1029  C   LEU A 179      55.845  32.517  33.308  1.00  9.40           C  
-ANISOU 1029  C   LEU A 179     1274   1138   1159    -94     -6   -171       C  
-ATOM   1030  O   LEU A 179      56.611  33.385  33.730  1.00  9.19           O  
-ANISOU 1030  O   LEU A 179     1328   1171    990   -216     24   -195       O  
-ATOM   1031  CB  LEU A 179      56.675  30.630  31.928  1.00  9.62           C  
-ANISOU 1031  CB  LEU A 179     1301   1134   1219    -78    -63   -174       C  
-ATOM   1032  CG  LEU A 179      56.414  29.728  30.721  1.00 11.13           C  
-ANISOU 1032  CG  LEU A 179     1568   1287   1371    -55     92   -170       C  
-ATOM   1033  CD1 LEU A 179      56.749  30.366  29.381  1.00 11.24           C  
-ANISOU 1033  CD1 LEU A 179     1577   1393   1298     66   -207   -300       C  
-ATOM   1034  CD2 LEU A 179      57.190  28.440  30.918  1.00 12.55           C  
-ANISOU 1034  CD2 LEU A 179     1823   1410   1532     65    -19   -231       C  
-ATOM   1035  N   PRO A 180      54.898  31.992  34.086  1.00  9.92           N  
-ANISOU 1035  N   PRO A 180     1348   1237   1183   -113     14   -125       N  
-ATOM   1036  CA  PRO A 180      54.786  32.402  35.494  1.00 10.79           C  
-ANISOU 1036  CA  PRO A 180     1468   1324   1306   -119     71   -133       C  
-ATOM   1037  C   PRO A 180      56.083  32.269  36.295  1.00 11.11           C  
-ANISOU 1037  C   PRO A 180     1592   1357   1271    -92     67   -132       C  
-ATOM   1038  O   PRO A 180      56.319  33.083  37.190  1.00 11.48           O  
-ANISOU 1038  O   PRO A 180     1761   1439   1161   -198     54   -332       O  
-ATOM   1039  CB  PRO A 180      53.667  31.500  36.028  1.00 11.43           C  
-ANISOU 1039  CB  PRO A 180     1556   1376   1408   -102     55    -63       C  
-ATOM   1040  CG  PRO A 180      52.839  31.206  34.832  1.00 11.55           C  
-ANISOU 1040  CG  PRO A 180     1542   1312   1533   -139      8    -53       C  
-ATOM   1041  CD  PRO A 180      53.804  31.074  33.705  1.00 10.31           C  
-ANISOU 1041  CD  PRO A 180     1294   1310   1311    -97    -64    -75       C  
-ATOM   1042  N   ASN A 181      56.930  31.302  35.960  1.00 10.92           N  
-ANISOU 1042  N   ASN A 181     1551   1350   1248    -87    -15   -148       N  
-ATOM   1043  CA  ASN A 181      58.205  31.123  36.646  1.00 11.37           C  
-ANISOU 1043  CA  ASN A 181     1569   1427   1324    -58    -79    -87       C  
-ATOM   1044  C   ASN A 181      59.325  32.040  36.119  1.00 11.03           C  
-ANISOU 1044  C   ASN A 181     1519   1407   1265    -66    -74   -122       C  
-ATOM   1045  O   ASN A 181      60.452  31.953  36.582  1.00 12.35           O  
-ANISOU 1045  O   ASN A 181     1571   1815   1304   -115   -241    -93       O  
-ATOM   1046  CB  ASN A 181      58.634  29.655  36.612  1.00 11.75           C  
-ANISOU 1046  CB  ASN A 181     1614   1461   1387    -62   -165    -47       C  
-ATOM   1047  CG  ASN A 181      58.904  29.142  35.203  1.00 10.83           C  
-ANISOU 1047  CG  ASN A 181     1428   1193   1493    -23   -190     23       C  
-ATOM   1048  OD1 ASN A 181      59.071  29.921  34.272  1.00 12.14           O  
-ANISOU 1048  OD1 ASN A 181     1874   1320   1415     83   -236   -134       O  
-ATOM   1049  ND2 ASN A 181      58.969  27.823  35.058  1.00 12.88           N  
-ANISOU 1049  ND2 ASN A 181     1529   1429   1936    141   -568      7       N  
-ATOM   1050  N   GLY A 182      59.030  32.911  35.162  1.00 10.28           N  
-ANISOU 1050  N   GLY A 182     1466   1274   1165    -57    -60   -173       N  
-ATOM   1051  CA  GLY A 182      59.985  33.905  34.694  1.00 10.11           C  
-ANISOU 1051  CA  GLY A 182     1342   1371   1127   -101    -56    -80       C  
-ATOM   1052  C   GLY A 182      60.754  33.509  33.451  1.00  9.60           C  
-ANISOU 1052  C   GLY A 182     1331   1263   1051   -125    -84    -53       C  
-ATOM   1053  O   GLY A 182      61.374  34.354  32.791  1.00  9.78           O  
-ANISOU 1053  O   GLY A 182     1278   1344   1094    -90     10    -68       O  
-ATOM   1054  N   LYS A 183      60.711  32.230  33.112  1.00  9.62           N  
-ANISOU 1054  N   LYS A 183     1234   1297   1121    -12    -81    -14       N  
-ATOM   1055  CA  LYS A 183      61.376  31.783  31.902  1.00  9.57           C  
-ANISOU 1055  CA  LYS A 183     1235   1276   1123     20    -49    -41       C  
-ATOM   1056  C   LYS A 183      60.736  32.417  30.680  1.00  8.58           C  
-ANISOU 1056  C   LYS A 183     1079   1275    906     34    -56   -139       C  
-ATOM   1057  O   LYS A 183      59.523  32.581  30.626  1.00  9.50           O  
-ANISOU 1057  O   LYS A 183      957   1557   1096     29   -122    -80       O  
-ATOM   1058  CB  LYS A 183      61.303  30.273  31.785  1.00 10.30           C  
-ANISOU 1058  CB  LYS A 183     1389   1315   1207     82    -44     12       C  
-ATOM   1059  CG  LYS A 183      62.144  29.538  32.810  1.00 13.57           C  
-ANISOU 1059  CG  LYS A 183     1752   1608   1795     96   -112     47       C  
-ATOM   1060  CD  LYS A 183      62.013  28.037  32.637  1.00 17.46           C  
-ANISOU 1060  CD  LYS A 183     2411   1959   2261      0    -43     95       C  
-ATOM   1061  CE  LYS A 183      62.956  27.266  33.540  1.00 22.00           C  
-ANISOU 1061  CE  LYS A 183     2900   2625   2832     39    -45     41       C  
-ATOM   1062  NZ  LYS A 183      64.337  27.208  32.978  1.00 24.90           N  
-ANISOU 1062  NZ  LYS A 183     3282   2902   3277    -40   -216     62       N  
-ATOM   1063  N   LYS A 184      61.571  32.749  29.709  1.00  8.60           N  
-ANISOU 1063  N   LYS A 184      983   1259   1023    110    -52   -105       N  
-ATOM   1064  CA  LYS A 184      61.136  33.377  28.473  1.00  8.66           C  
-ANISOU 1064  CA  LYS A 184     1091   1179   1020     87    -50   -117       C  
-ATOM   1065  C   LYS A 184      61.575  32.560  27.281  1.00  8.38           C  
-ANISOU 1065  C   LYS A 184     1025   1245    913    102    -57   -188       C  
-ATOM   1066  O   LYS A 184      62.631  31.926  27.296  1.00  9.52           O  
-ANISOU 1066  O   LYS A 184     1046   1500   1070    250   -238   -237       O  
-ATOM   1067  CB  LYS A 184      61.710  34.789  28.341  1.00  8.92           C  
-ANISOU 1067  CB  LYS A 184     1126   1255   1006    -17    -35    -77       C  
-ATOM   1068  CG  LYS A 184      61.308  35.698  29.483  1.00 10.62           C  
-ANISOU 1068  CG  LYS A 184     1419   1331   1285    -56    -19   -182       C  
-ATOM   1069  CD  LYS A 184      61.877  37.106  29.313  1.00 13.78           C  
-ANISOU 1069  CD  LYS A 184     1817   1683   1733    -46    110   -215       C  
-ATOM   1070  CE  LYS A 184      61.080  37.915  28.293  1.00 17.14           C  
-ANISOU 1070  CE  LYS A 184     2327   2051   2135    -17     82   -163       C  
-ATOM   1071  NZ  LYS A 184      61.607  39.295  28.096  1.00 20.06           N  
-ANISOU 1071  NZ  LYS A 184     2561   2442   2617     12     -6   -160       N  
-ATOM   1072  N   PHE A 185      60.745  32.571  26.244  1.00  7.65           N  
-ANISOU 1072  N   PHE A 185      928   1078    899     53   -120   -179       N  
-ATOM   1073  CA  PHE A 185      61.039  31.869  25.000  1.00  8.19           C  
-ANISOU 1073  CA  PHE A 185     1040   1107    963     61    -49   -187       C  
-ATOM   1074  C   PHE A 185      60.693  32.752  23.829  1.00  8.06           C  
-ANISOU 1074  C   PHE A 185      978   1114    967     34   -100   -185       C  
-ATOM   1075  O   PHE A 185      59.695  33.465  23.851  1.00  8.20           O  
-ANISOU 1075  O   PHE A 185      987   1186    940     93    -79   -169       O  
-ATOM   1076  CB  PHE A 185      60.245  30.564  24.923  1.00  8.36           C  
-ANISOU 1076  CB  PHE A 185     1177   1107    892    122    -43   -116       C  
-ATOM   1077  CG  PHE A 185      60.611  29.603  25.989  1.00  9.35           C  
-ANISOU 1077  CG  PHE A 185     1334   1074   1142    155    -74    -53       C  
-ATOM   1078  CD1 PHE A 185      61.731  28.800  25.850  1.00 12.05           C  
-ANISOU 1078  CD1 PHE A 185     1795   1418   1362    286      1     76       C  
-ATOM   1079  CD2 PHE A 185      59.883  29.542  27.163  1.00  9.99           C  
-ANISOU 1079  CD2 PHE A 185     1411   1195   1189    108   -194     22       C  
-ATOM   1080  CE1 PHE A 185      62.118  27.957  26.868  1.00 13.62           C  
-ANISOU 1080  CE1 PHE A 185     1848   1383   1942    307   -130     21       C  
-ATOM   1081  CE2 PHE A 185      60.264  28.693  28.170  1.00 11.92           C  
-ANISOU 1081  CE2 PHE A 185     1797   1458   1272    -24   -198    114       C  
-ATOM   1082  CZ  PHE A 185      61.374  27.891  28.012  1.00 13.60           C  
-ANISOU 1082  CZ  PHE A 185     1973   1559   1633     17   -239     75       C  
-ATOM   1083  N   PRO A 186      61.501  32.693  22.782  1.00  7.82           N  
-ANISOU 1083  N   PRO A 186      842   1064   1063    -13    -52    -89       N  
-ATOM   1084  CA  PRO A 186      61.248  33.531  21.613  1.00  8.41           C  
-ANISOU 1084  CA  PRO A 186      963   1130   1102    -82     -3    -62       C  
-ATOM   1085  C   PRO A 186      60.178  32.945  20.712  1.00  7.33           C  
-ANISOU 1085  C   PRO A 186      851    918   1014    -71     19    -69       C  
-ATOM   1086  O   PRO A 186      60.206  31.761  20.386  1.00  7.40           O  
-ANISOU 1086  O   PRO A 186      937    850   1022    -34      6    -39       O  
-ATOM   1087  CB  PRO A 186      62.593  33.522  20.894  1.00  9.15           C  
-ANISOU 1087  CB  PRO A 186     1021   1241   1214   -119     14     11       C  
-ATOM   1088  CG  PRO A 186      63.220  32.206  21.259  1.00  8.98           C  
-ANISOU 1088  CG  PRO A 186      960   1309   1140    -43    103    -50       C  
-ATOM   1089  CD  PRO A 186      62.744  31.906  22.644  1.00  8.65           C  
-ANISOU 1089  CD  PRO A 186      953   1252   1082      7    -50    -31       C  
-ATOM   1090  N   ILE A 187      59.264  33.792  20.266  1.00  6.81           N  
-ANISOU 1090  N   ILE A 187      847    806    934    -89     -4     -4       N  
-ATOM   1091  CA  ILE A 187      58.280  33.354  19.295  1.00  6.79           C  
-ANISOU 1091  CA  ILE A 187      836    779    965    -71     25      1       C  
-ATOM   1092  C   ILE A 187      58.974  32.954  17.982  1.00  6.34           C  
-ANISOU 1092  C   ILE A 187      752    840    815    -75    -27     63       C  
-ATOM   1093  O   ILE A 187      58.506  32.054  17.290  1.00  6.69           O  
-ANISOU 1093  O   ILE A 187      807    809    923    -78    -28    -23       O  
-ATOM   1094  CB  ILE A 187      57.169  34.405  19.097  1.00  7.03           C  
-ANISOU 1094  CB  ILE A 187      843    883    944    -40     13    -16       C  
-ATOM   1095  CG1 ILE A 187      56.434  34.667  20.428  1.00  7.54           C  
-ANISOU 1095  CG1 ILE A 187      967    885   1010      3     12    -13       C  
-ATOM   1096  CG2 ILE A 187      56.193  33.962  18.009  1.00  7.55           C  
-ANISOU 1096  CG2 ILE A 187      872    838   1156     45     76     76       C  
-ATOM   1097  CD1 ILE A 187      55.840  33.452  21.069  1.00  9.05           C  
-ANISOU 1097  CD1 ILE A 187     1080   1092   1265    -26    240      5       C  
-ATOM   1098  N   ALA A 188      60.127  33.556  17.691  1.00  7.53           N  
-ANISOU 1098  N   ALA A 188      971    909    980   -128     35    -22       N  
-ATOM   1099  CA  ALA A 188      60.921  33.179  16.522  1.00  8.17           C  
-ANISOU 1099  CA  ALA A 188      949   1138   1017   -129     74    -41       C  
-ATOM   1100  C   ALA A 188      61.402  31.735  16.570  1.00  8.28           C  
-ANISOU 1100  C   ALA A 188      886   1217   1043    -92     66    -56       C  
-ATOM   1101  O   ALA A 188      61.772  31.197  15.532  1.00  9.78           O  
-ANISOU 1101  O   ALA A 188     1077   1470   1168    -47    221   -243       O  
-ATOM   1102  CB  ALA A 188      62.115  34.128  16.355  1.00  8.80           C  
-ANISOU 1102  CB  ALA A 188     1029   1296   1018   -187    121    -16       C  
-ATOM   1103  N   GLY A 189      61.413  31.108  17.746  1.00  8.00           N  
-ANISOU 1103  N   GLY A 189      875   1086   1078    -32     24   -134       N  
-ATOM   1104  CA  GLY A 189      61.808  29.720  17.888  1.00  8.74           C  
-ANISOU 1104  CA  GLY A 189     1003   1123   1195     47      0    -96       C  
-ATOM   1105  C   GLY A 189      60.657  28.726  17.836  1.00  8.25           C  
-ANISOU 1105  C   GLY A 189      985    964   1183     63    -34    -53       C  
-ATOM   1106  O   GLY A 189      60.901  27.524  17.876  1.00 10.20           O  
-ANISOU 1106  O   GLY A 189     1201   1047   1626    185    -55    -17       O  
-ATOM   1107  N   VAL A 190      59.416  29.208  17.734  1.00  7.28           N  
-ANISOU 1107  N   VAL A 190      861    812   1092     11    -10    -32       N  
-ATOM   1108  CA  VAL A 190      58.238  28.347  17.741  1.00  7.25           C  
-ANISOU 1108  CA  VAL A 190      921    799   1034     -8    -42     36       C  
-ATOM   1109  C   VAL A 190      57.976  27.745  16.364  1.00  7.08           C  
-ANISOU 1109  C   VAL A 190      853    784   1054     20     -1     74       C  
-ATOM   1110  O   VAL A 190      57.885  28.473  15.381  1.00  8.08           O  
-ANISOU 1110  O   VAL A 190     1170    873   1024    -92     11     78       O  
-ATOM   1111  CB  VAL A 190      57.010  29.141  18.207  1.00  7.51           C  
-ANISOU 1111  CB  VAL A 190      963    853   1036      0      0     42       C  
-ATOM   1112  CG1 VAL A 190      55.741  28.341  18.012  1.00  7.69           C  
-ANISOU 1112  CG1 VAL A 190     1020    857   1045   -140    -23    -74       C  
-ATOM   1113  CG2 VAL A 190      57.199  29.557  19.653  1.00  8.66           C  
-ANISOU 1113  CG2 VAL A 190     1078    857   1353    -35     45    -24       C  
-ATOM   1114  N   GLN A 191      57.850  26.421  16.301  1.00  7.44           N  
-ANISOU 1114  N   GLN A 191      913    821   1090     34    -96      6       N  
-ATOM   1115  CA  GLN A 191      57.515  25.714  15.066  1.00  7.88           C  
-ANISOU 1115  CA  GLN A 191      887    946   1160     98    -59    -64       C  
-ATOM   1116  C   GLN A 191      56.373  24.749  15.330  1.00  7.28           C  
-ANISOU 1116  C   GLN A 191      881    770   1116     88    -99     -8       C  
-ATOM   1117  O   GLN A 191      56.584  23.603  15.702  1.00  8.57           O  
-ANISOU 1117  O   GLN A 191      970    940   1346    227   -139    121       O  
-ATOM   1118  CB  GLN A 191      58.726  24.959  14.498  1.00  9.67           C  
-ANISOU 1118  CB  GLN A 191     1011   1229   1432     32    -21   -135       C  
-ATOM   1119  CG  GLN A 191      58.470  24.328  13.147  1.00 14.30           C  
-ANISOU 1119  CG  GLN A 191     1650   1903   1880     28     13    -95       C  
-ATOM   1120  CD  GLN A 191      59.644  23.508  12.631  1.00 19.11           C  
-ANISOU 1120  CD  GLN A 191     2157   2401   2703    -58    216     30       C  
-ATOM   1121  OE1 GLN A 191      60.633  24.062  12.157  1.00 23.71           O  
-ANISOU 1121  OE1 GLN A 191     2504   3157   3347    127    394    101       O  
-ATOM   1122  NE2 GLN A 191      59.527  22.185  12.715  1.00 21.06           N  
-ANISOU 1122  NE2 GLN A 191     2317   2561   3122    130    352    -23       N  
-ATOM   1123  N   ILE A 192      55.157  25.220  15.121  1.00  6.59           N  
-ANISOU 1123  N   ILE A 192      722    748   1035     81    -87     43       N  
-ATOM   1124  CA  ILE A 192      53.983  24.394  15.377  1.00  7.18           C  
-ANISOU 1124  CA  ILE A 192      829    891   1006      8    -56     38       C  
-ATOM   1125  C   ILE A 192      53.882  23.270  14.339  1.00  7.76           C  
-ANISOU 1125  C   ILE A 192      916    885   1144    -39    -82     25       C  
-ATOM   1126  O   ILE A 192      53.562  22.133  14.671  1.00  9.03           O  
-ANISOU 1126  O   ILE A 192     1095    907   1429    -59    -75     12       O  
-ATOM   1127  CB  ILE A 192      52.688  25.238  15.411  1.00  6.69           C  
-ANISOU 1127  CB  ILE A 192      768    853    918      0    -49    -13       C  
-ATOM   1128  CG1 ILE A 192      52.782  26.330  16.483  1.00  7.20           C  
-ANISOU 1128  CG1 ILE A 192      773    943   1017     32    -53    -31       C  
-ATOM   1129  CG2 ILE A 192      51.467  24.354  15.695  1.00  8.38           C  
-ANISOU 1129  CG2 ILE A 192      822   1139   1221    -93      2   -130       C  
-ATOM   1130  CD1 ILE A 192      51.634  27.319  16.449  1.00  7.82           C  
-ANISOU 1130  CD1 ILE A 192      893   1031   1045    114    -36    -37       C  
-ATOM   1131  N   GLN A 193      54.155  23.613  13.088  1.00  8.10           N  
-ANISOU 1131  N   GLN A 193     1018    952   1106     24    -99    -72       N  
-ATOM   1132  CA  GLN A 193      54.092  22.689  11.962  1.00  9.58           C  
-ANISOU 1132  CA  GLN A 193     1084   1303   1251    -15    -55   -141       C  
-ATOM   1133  C   GLN A 193      55.272  22.871  11.018  1.00 10.17           C  
-ANISOU 1133  C   GLN A 193     1165   1350   1347     51     -9   -148       C  
-ATOM   1134  O   GLN A 193      55.763  23.979  10.814  1.00 11.67           O  
-ANISOU 1134  O   GLN A 193     1375   1560   1496     86     18   -181       O  
-ATOM   1135  CB  GLN A 193      52.793  22.896  11.171  1.00 10.78           C  
-ANISOU 1135  CB  GLN A 193     1266   1476   1353     80   -118   -184       C  
-ATOM   1136  CG  GLN A 193      51.536  22.656  11.979  1.00 11.65           C  
-ANISOU 1136  CG  GLN A 193     1276   1571   1580    177    -47   -289       C  
-ATOM   1137  CD  GLN A 193      51.367  21.212  12.385  1.00 11.12           C  
-ANISOU 1137  CD  GLN A 193      990   1603   1629    122     61   -326       C  
-ATOM   1138  OE1 GLN A 193      52.082  20.337  11.902  1.00 11.75           O  
-ANISOU 1138  OE1 GLN A 193     1116   1549   1800    275    141   -635       O  
-ATOM   1139  NE2 GLN A 193      50.408  20.949  13.253  1.00 13.04           N  
-ANISOU 1139  NE2 GLN A 193     1184   1894   1875    -29    117   -559       N  
-ATOM   1140  N   ARG A 194      55.689  21.765  10.397  1.00 11.17           N  
-ANISOU 1140  N   ARG A 194     1283   1476   1484    144     36   -158       N  
-ATOM   1141  CA  ARG A 194      56.844  21.758   9.498  1.00 13.29           C  
-ANISOU 1141  CA  ARG A 194     1517   1807   1725    159     65    -84       C  
-ATOM   1142  C   ARG A 194      56.466  21.932   8.031  1.00 13.03           C  
-ANISOU 1142  C   ARG A 194     1436   1843   1669    120     75    -97       C  
-ATOM   1143  O   ARG A 194      57.320  22.208   7.199  1.00 14.34           O  
-ANISOU 1143  O   ARG A 194     1500   2120   1827    220    247   -178       O  
-ATOM   1144  CB  ARG A 194      57.678  20.472   9.673  1.00 14.11           C  
-ANISOU 1144  CB  ARG A 194     1570   1941   1849    177     50    -14       C  
-ATOM   1145  CG  ARG A 194      57.071  19.206   9.083  1.00 17.66           C  
-ANISOU 1145  CG  ARG A 194     1999   2383   2325    193     45    -40       C  
-ATOM   1146  CD  ARG A 194      57.966  17.967   9.177  1.00 22.86           C  
-ANISOU 1146  CD  ARG A 194     2759   2952   2975    100     54     56       C  
-ATOM   1147  NE  ARG A 194      57.202  16.731   9.392  1.00 27.76           N  
-ANISOU 1147  NE  ARG A 194     3536   3453   3557     50    -42    -22       N  
-ATOM   1148  CZ  ARG A 194      57.309  15.588   8.694  1.00 31.28           C  
-ANISOU 1148  CZ  ARG A 194     3975   3979   3929      6     67      2       C  
-ATOM   1149  NH1 ARG A 194      58.161  15.453   7.678  1.00 32.04           N  
-ANISOU 1149  NH1 ARG A 194     3948   4145   4081     46    128     -8       N  
-ATOM   1150  NH2 ARG A 194      56.545  14.550   9.026  1.00 32.86           N  
-ANISOU 1150  NH2 ARG A 194     4212   4141   4132     -9     37     10       N  
-ATOM   1151  N   GLU A 195      55.187  21.791   7.705  1.00 12.96           N  
-ANISOU 1151  N   GLU A 195     1448   1801   1673    151     48   -153       N  
-ATOM   1152  CA  GLU A 195      54.752  21.763   6.308  1.00 12.58           C  
-ANISOU 1152  CA  GLU A 195     1469   1709   1600    144     76   -162       C  
-ATOM   1153  C   GLU A 195      54.992  23.114   5.627  1.00 12.65           C  
-ANISOU 1153  C   GLU A 195     1423   1738   1645    151     59   -200       C  
-ATOM   1154  O   GLU A 195      54.856  24.154   6.269  1.00 13.06           O  
-ANISOU 1154  O   GLU A 195     1416   1812   1731    192    106   -295       O  
-ATOM   1155  CB  GLU A 195      53.264  21.376   6.230  1.00 13.24           C  
-ANISOU 1155  CB  GLU A 195     1509   1824   1695    148     20   -140       C  
-ATOM   1156  CG  GLU A 195      52.976  19.888   6.413  1.00 14.44           C  
-ANISOU 1156  CG  GLU A 195     1736   1978   1771    188     23   -200       C  
-ATOM   1157  CD  GLU A 195      53.127  19.383   7.843  1.00 14.99           C  
-ANISOU 1157  CD  GLU A 195     1873   1823   1999    469    -36   -236       C  
-ATOM   1158  OE1 GLU A 195      52.953  20.162   8.801  1.00 12.97           O  
-ANISOU 1158  OE1 GLU A 195     1088   1974   1866    630     99   -450       O  
-ATOM   1159  OE2 GLU A 195      53.432  18.181   8.019  1.00 19.96           O  
-ANISOU 1159  OE2 GLU A 195     2880   2217   2486    414      2   -248       O  
-ATOM   1160  N   PRO A 196      55.345  23.106   4.341  1.00 12.25           N  
-ANISOU 1160  N   PRO A 196     1387   1621   1646    187    141   -186       N  
-ATOM   1161  CA  PRO A 196      55.574  24.356   3.609  1.00 12.41           C  
-ANISOU 1161  CA  PRO A 196     1444   1639   1630     65    155   -162       C  
-ATOM   1162  C   PRO A 196      54.308  25.168   3.340  1.00 11.65           C  
-ANISOU 1162  C   PRO A 196     1363   1466   1597     46    209   -184       C  
-ATOM   1163  O   PRO A 196      54.395  26.354   3.020  1.00 12.10           O  
-ANISOU 1163  O   PRO A 196     1332   1488   1777    -45    273   -297       O  
-ATOM   1164  CB  PRO A 196      56.231  23.887   2.306  1.00 12.98           C  
-ANISOU 1164  CB  PRO A 196     1444   1783   1705    145    186   -109       C  
-ATOM   1165  CG  PRO A 196      55.740  22.533   2.143  1.00 13.34           C  
-ANISOU 1165  CG  PRO A 196     1551   1870   1645    162    244   -172       C  
-ATOM   1166  CD  PRO A 196      55.660  21.930   3.510  1.00 12.89           C  
-ANISOU 1166  CD  PRO A 196     1470   1761   1665    164    131   -238       C  
-ATOM   1167  N   PHE A 197      53.147  24.531   3.435  1.00  9.92           N  
-ANISOU 1167  N   PHE A 197     1181   1241   1345    -39    208   -185       N  
-ATOM   1168  CA  PHE A 197      51.881  25.253   3.394  1.00  9.07           C  
-ANISOU 1168  CA  PHE A 197     1136   1027   1282    -30    163   -112       C  
-ATOM   1169  C   PHE A 197      50.873  24.447   4.181  1.00  7.91           C  
-ANISOU 1169  C   PHE A 197     1066    757   1180    -74    204    -81       C  
-ATOM   1170  O   PHE A 197      51.018  23.235   4.296  1.00  9.46           O  
-ANISOU 1170  O   PHE A 197     1252    812   1527     62    233   -190       O  
-ATOM   1171  CB  PHE A 197      51.379  25.511   1.964  1.00  9.75           C  
-ANISOU 1171  CB  PHE A 197     1189   1218   1296   -101    229   -141       C  
-ATOM   1172  CG  PHE A 197      51.202  24.272   1.149  1.00 11.77           C  
-ANISOU 1172  CG  PHE A 197     1430   1410   1631     42     39   -125       C  
-ATOM   1173  CD1 PHE A 197      52.269  23.754   0.420  1.00 13.98           C  
-ANISOU 1173  CD1 PHE A 197     1712   1789   1810     86     25   -224       C  
-ATOM   1174  CD2 PHE A 197      49.981  23.609   1.102  1.00 13.21           C  
-ANISOU 1174  CD2 PHE A 197     1785   1456   1775   -104      1    -81       C  
-ATOM   1175  CE1 PHE A 197      52.124  22.598  -0.331  1.00 16.01           C  
-ANISOU 1175  CE1 PHE A 197     1953   2040   2088     10     78   -231       C  
-ATOM   1176  CE2 PHE A 197      49.833  22.430   0.354  1.00 14.91           C  
-ANISOU 1176  CE2 PHE A 197     1802   1812   2049    -73    -41   -149       C  
-ATOM   1177  CZ  PHE A 197      50.907  21.937  -0.355  1.00 16.01           C  
-ANISOU 1177  CZ  PHE A 197     2001   1864   2215    -54    -76   -249       C  
-ATOM   1178  N   PRO A 198      49.845  25.095   4.718  1.00  7.29           N  
-ANISOU 1178  N   PRO A 198      950    768   1050    -36    221    -68       N  
-ATOM   1179  CA  PRO A 198      49.670  26.554   4.747  1.00  6.26           C  
-ANISOU 1179  CA  PRO A 198      869    713    795     -6    127     12       C  
-ATOM   1180  C   PRO A 198      50.622  27.252   5.713  1.00  6.09           C  
-ANISOU 1180  C   PRO A 198      850    723    737     36    119     80       C  
-ATOM   1181  O   PRO A 198      50.997  26.681   6.721  1.00  7.17           O  
-ANISOU 1181  O   PRO A 198     1090    728    905    -52     20    148       O  
-ATOM   1182  CB  PRO A 198      48.226  26.708   5.243  1.00  6.74           C  
-ANISOU 1182  CB  PRO A 198      891    837    833    -28     82    -63       C  
-ATOM   1183  CG  PRO A 198      47.954  25.465   6.021  1.00  7.79           C  
-ANISOU 1183  CG  PRO A 198      892    949   1118    -59     68     19       C  
-ATOM   1184  CD  PRO A 198      48.739  24.384   5.377  1.00  7.64           C  
-ANISOU 1184  CD  PRO A 198      969    918   1016   -175    168     42       C  
-ATOM   1185  N   GLN A 199      50.972  28.488   5.391  1.00  5.41           N  
-ANISOU 1185  N   GLN A 199      802    577    674     15     96     22       N  
-ATOM   1186  CA  GLN A 199      51.658  29.403   6.300  1.00  5.67           C  
-ANISOU 1186  CA  GLN A 199      753    615    785      3     66     41       C  
-ATOM   1187  C   GLN A 199      50.791  30.633   6.469  1.00  5.08           C  
-ANISOU 1187  C   GLN A 199      759    493    676     60     31     80       C  
-ATOM   1188  O   GLN A 199      50.200  31.127   5.517  1.00  5.98           O  
-ANISOU 1188  O   GLN A 199     1021    605    645    174     55     59       O  
-ATOM   1189  CB  GLN A 199      53.018  29.827   5.745  1.00  6.20           C  
-ANISOU 1189  CB  GLN A 199      812    641    902     10     78     32       C  
-ATOM   1190  CG  GLN A 199      54.002  28.675   5.642  1.00  7.22           C  
-ANISOU 1190  CG  GLN A 199      832    734   1178     31    166      3       C  
-ATOM   1191  CD  GLN A 199      55.349  29.134   5.155  1.00  7.10           C  
-ANISOU 1191  CD  GLN A 199      752    658   1287   -100    101     46       C  
-ATOM   1192  OE1 GLN A 199      55.901  30.088   5.675  1.00  9.06           O  
-ANISOU 1192  OE1 GLN A 199      884    956   1601   -185    186    102       O  
-ATOM   1193  NE2 GLN A 199      55.899  28.437   4.178  1.00 10.88           N  
-ANISOU 1193  NE2 GLN A 199     1206   1192   1732    -79    588   -227       N  
-ATOM   1194  N   TYR A 200      50.723  31.116   7.706  1.00  4.83           N  
-ANISOU 1194  N   TYR A 200      659    602    572    -12    -22     47       N  
-ATOM   1195  CA  TYR A 200      49.723  32.110   8.070  1.00  4.98           C  
-ANISOU 1195  CA  TYR A 200      633    633    625     58      9     61       C  
-ATOM   1196  C   TYR A 200      50.260  33.483   8.471  1.00  5.10           C  
-ANISOU 1196  C   TYR A 200      699    611    625     42     37    104       C  
-ATOM   1197  O   TYR A 200      49.697  34.490   8.068  1.00  5.80           O  
-ANISOU 1197  O   TYR A 200      764    586    852     54     -3    108       O  
-ATOM   1198  CB  TYR A 200      48.867  31.566   9.201  1.00  5.07           C  
-ANISOU 1198  CB  TYR A 200      664    706    555    -23    130     -4       C  
-ATOM   1199  CG  TYR A 200      48.158  30.263   8.874  1.00  5.20           C  
-ANISOU 1199  CG  TYR A 200      628    726    618     25    128      2       C  
-ATOM   1200  CD1 TYR A 200      47.099  30.234   7.982  1.00  5.47           C  
-ANISOU 1200  CD1 TYR A 200      703    652    723     53    -33     93       C  
-ATOM   1201  CD2 TYR A 200      48.538  29.067   9.467  1.00  5.29           C  
-ANISOU 1201  CD2 TYR A 200      655    708    645    -68     56    101       C  
-ATOM   1202  CE1 TYR A 200      46.418  29.067   7.719  1.00  5.52           C  
-ANISOU 1202  CE1 TYR A 200      582    776    738    -30    -89      8       C  
-ATOM   1203  CE2 TYR A 200      47.871  27.884   9.190  1.00  5.58           C  
-ANISOU 1203  CE2 TYR A 200      726    685    706     27     94     65       C  
-ATOM   1204  CZ  TYR A 200      46.804  27.898   8.329  1.00  4.50           C  
-ANISOU 1204  CZ  TYR A 200      614    581    513     38     72     -2       C  
-ATOM   1205  OH  TYR A 200      46.142  26.725   8.111  1.00  5.39           O  
-ANISOU 1205  OH  TYR A 200      724    591    731   -112     83     48       O  
-ATOM   1206  N   SER A 201      51.298  33.515   9.306  1.00  4.77           N  
-ANISOU 1206  N   SER A 201      643    546    620     17     24     62       N  
-ATOM   1207  CA  SER A 201      51.721  34.757   9.955  1.00  5.39           C  
-ANISOU 1207  CA  SER A 201      725    588    732      9     41     85       C  
-ATOM   1208  C   SER A 201      53.006  34.492  10.711  1.00  4.93           C  
-ANISOU 1208  C   SER A 201      658    602    612     -6     39     77       C  
-ATOM   1209  O   SER A 201      53.189  33.385  11.219  1.00  5.48           O  
-ANISOU 1209  O   SER A 201      744    615    723     27     -9    134       O  
-ATOM   1210  CB  SER A 201      50.667  35.177  10.985  1.00  5.85           C  
-ANISOU 1210  CB  SER A 201      733    668    822      9     34     51       C  
-ATOM   1211  OG  SER A 201      51.086  36.309  11.740  1.00  6.39           O  
-ANISOU 1211  OG  SER A 201      882    608    938    -25    -30    -48       O  
-ATOM   1212  N   PRO A 202      53.862  35.498  10.862  1.00  5.41           N  
-ANISOU 1212  N   PRO A 202      710    641    702    -42     -6    128       N  
-ATOM   1213  CA  PRO A 202      55.037  35.345  11.730  1.00  5.85           C  
-ANISOU 1213  CA  PRO A 202      718    715    788    -44     -5     81       C  
-ATOM   1214  C   PRO A 202      54.701  35.376  13.218  1.00  5.55           C  
-ANISOU 1214  C   PRO A 202      656    663    789   -111     -2    100       C  
-ATOM   1215  O   PRO A 202      55.540  35.009  14.025  1.00  6.38           O  
-ANISOU 1215  O   PRO A 202      789    808    824    -21    -35    102       O  
-ATOM   1216  CB  PRO A 202      55.898  36.566  11.370  1.00  6.63           C  
-ANISOU 1216  CB  PRO A 202      805    929    783   -179     53    123       C  
-ATOM   1217  CG  PRO A 202      54.889  37.605  10.975  1.00  6.82           C  
-ANISOU 1217  CG  PRO A 202      930    869    790   -191    113     70       C  
-ATOM   1218  CD  PRO A 202      53.841  36.826  10.220  1.00  5.90           C  
-ANISOU 1218  CD  PRO A 202      832    614    796    -19     40    193       C  
-ATOM   1219  N   GLU A 203      53.502  35.841  13.570  1.00  5.46           N  
-ANISOU 1219  N   GLU A 203      663    628    782    -52    -10     54       N  
-ATOM   1220  CA  GLU A 203      53.075  35.906  14.956  1.00  5.75           C  
-ANISOU 1220  CA  GLU A 203      820    613    752    -23     -2    -54       C  
-ATOM   1221  C   GLU A 203      52.170  34.727  15.276  1.00  5.55           C  
-ANISOU 1221  C   GLU A 203      783    602    722    -30     42    -23       C  
-ATOM   1222  O   GLU A 203      51.694  34.022  14.379  1.00  5.62           O  
-ANISOU 1222  O   GLU A 203      803    661    668    -54     39    -15       O  
-ATOM   1223  CB  GLU A 203      52.371  37.224  15.280  1.00  6.31           C  
-ANISOU 1223  CB  GLU A 203      878    629    890    -68      1     -5       C  
-ATOM   1224  CG  GLU A 203      53.195  38.455  14.941  1.00  7.90           C  
-ANISOU 1224  CG  GLU A 203     1103    725   1173    -67     81    -21       C  
-ATOM   1225  CD  GLU A 203      54.517  38.574  15.686  1.00  8.63           C  
-ANISOU 1225  CD  GLU A 203     1371    722   1183   -265    187     88       C  
-ATOM   1226  OE1 GLU A 203      54.694  37.962  16.768  1.00  9.23           O  
-ANISOU 1226  OE1 GLU A 203     1170   1008   1329   -330     67    -50       O  
-ATOM   1227  OE2 GLU A 203      55.377  39.339  15.190  1.00 11.13           O  
-ANISOU 1227  OE2 GLU A 203     1495   1177   1556   -398    -68    111       O  
-ATOM   1228  N   LEU A 204      51.972  34.504  16.566  1.00  5.75           N  
-ANISOU 1228  N   LEU A 204      784    700    698   -106    -20      8       N  
-ATOM   1229  CA  LEU A 204      51.072  33.479  17.067  1.00  5.76           C  
-ANISOU 1229  CA  LEU A 204      878    656    654    -74     33    -11       C  
-ATOM   1230  C   LEU A 204      49.646  34.014  17.117  1.00  5.52           C  
-ANISOU 1230  C   LEU A 204      824    557    716    -86     87    -16       C  
-ATOM   1231  O   LEU A 204      49.429  35.159  17.501  1.00  6.90           O  
-ANISOU 1231  O   LEU A 204      952    531   1136    -70    109   -180       O  
-ATOM   1232  CB  LEU A 204      51.513  33.090  18.467  1.00  6.79           C  
-ANISOU 1232  CB  LEU A 204     1020    771    789     44     34     25       C  
-ATOM   1233  CG  LEU A 204      51.116  31.737  19.020  1.00  8.61           C  
-ANISOU 1233  CG  LEU A 204     1078   1049   1141    -46    -66     29       C  
-ATOM   1234  CD1 LEU A 204      51.774  30.615  18.238  1.00  9.26           C  
-ANISOU 1234  CD1 LEU A 204     1531    760   1226    101   -294    -48       C  
-ATOM   1235  CD2 LEU A 204      51.459  31.643  20.510  1.00  9.50           C  
-ANISOU 1235  CD2 LEU A 204     1379   1104   1123    122     69    130       C  
-ATOM   1236  N   HIS A 205      48.695  33.158  16.793  1.00  5.11           N  
-ANISOU 1236  N   HIS A 205      731    545    663    -50     45    -41       N  
-ATOM   1237  CA  HIS A 205      47.291  33.522  16.787  1.00  5.66           C  
-ANISOU 1237  CA  HIS A 205      818    609    723    -33     25    -24       C  
-ATOM   1238  C   HIS A 205      46.425  32.369  17.241  1.00  4.95           C  
-ANISOU 1238  C   HIS A 205      724    568    587    -11     62    -27       C  
-ATOM   1239  O   HIS A 205      46.871  31.225  17.327  1.00  5.39           O  
-ANISOU 1239  O   HIS A 205      785    546    717     20    119    -15       O  
-ATOM   1240  CB  HIS A 205      46.887  33.921  15.380  1.00  6.33           C  
-ANISOU 1240  CB  HIS A 205      779    761    863    -56     60     95       C  
-ATOM   1241  CG  HIS A 205      47.627  35.099  14.856  1.00  8.15           C  
-ANISOU 1241  CG  HIS A 205      998    951   1147    -34     77    113       C  
-ATOM   1242  ND1 HIS A 205      48.615  35.010  13.900  1.00 10.97           N  
-ANISOU 1242  ND1 HIS A 205     1467   1461   1238   -181     77    393       N  
-ATOM   1243  CD2 HIS A 205      47.579  36.399  15.216  1.00 11.21           C  
-ANISOU 1243  CD2 HIS A 205     1874    925   1460    -46    487    126       C  
-ATOM   1244  CE1 HIS A 205      49.079  36.218  13.632  1.00  8.85           C  
-ANISOU 1244  CE1 HIS A 205     1290   1067   1004   -240     25    257       C  
-ATOM   1245  NE2 HIS A 205      48.467  37.079  14.416  1.00 11.87           N  
-ANISOU 1245  NE2 HIS A 205     1734   1250   1523   -247    173    160       N  
-ATOM   1246  N   PHE A 206      45.160  32.676  17.484  1.00  5.04           N  
-ANISOU 1246  N   PHE A 206      697    452    764     -4     73    -46       N  
-ATOM   1247  CA  PHE A 206      44.154  31.697  17.883  1.00  4.86           C  
-ANISOU 1247  CA  PHE A 206      752    496    597     -2     39    -59       C  
-ATOM   1248  C   PHE A 206      42.938  31.843  16.978  1.00  4.41           C  
-ANISOU 1248  C   PHE A 206      753    409    513     53     94    -84       C  
-ATOM   1249  O   PHE A 206      42.390  32.925  16.839  1.00  6.04           O  
-ANISOU 1249  O   PHE A 206     1042    526    726     79   -134    -99       O  
-ATOM   1250  CB  PHE A 206      43.759  31.933  19.333  1.00  5.01           C  
-ANISOU 1250  CB  PHE A 206      793    588    520     80    -39     -8       C  
-ATOM   1251  CG  PHE A 206      42.633  31.062  19.820  1.00  4.47           C  
-ANISOU 1251  CG  PHE A 206      723    549    425    -15     25    -18       C  
-ATOM   1252  CD1 PHE A 206      42.840  29.719  20.106  1.00  4.98           C  
-ANISOU 1252  CD1 PHE A 206      627    606    657     71    -42    -27       C  
-ATOM   1253  CD2 PHE A 206      41.372  31.589  20.036  1.00  5.40           C  
-ANISOU 1253  CD2 PHE A 206      892    562    596    144    118     44       C  
-ATOM   1254  CE1 PHE A 206      41.810  28.920  20.558  1.00  5.46           C  
-ANISOU 1254  CE1 PHE A 206      843    475    754    -39      1    -24       C  
-ATOM   1255  CE2 PHE A 206      40.348  30.783  20.509  1.00  5.26           C  
-ANISOU 1255  CE2 PHE A 206      886    546    566    114    170     30       C  
-ATOM   1256  CZ  PHE A 206      40.565  29.466  20.778  1.00  5.67           C  
-ANISOU 1256  CZ  PHE A 206      827    687    638     51     78    -79       C  
-ATOM   1257  N   PHE A 207      42.541  30.735  16.374  1.00  4.19           N  
-ANISOU 1257  N   PHE A 207      607    384    598     29     58    -29       N  
-ATOM   1258  CA  PHE A 207      41.389  30.696  15.463  1.00  4.08           C  
-ANISOU 1258  CA  PHE A 207      590    409    550     -5     47     -2       C  
-ATOM   1259  C   PHE A 207      40.259  29.956  16.165  1.00  4.08           C  
-ANISOU 1259  C   PHE A 207      556    441    552     16     59    -43       C  
-ATOM   1260  O   PHE A 207      40.292  28.732  16.295  1.00  5.03           O  
-ANISOU 1260  O   PHE A 207      733    468    708    -10    225    -17       O  
-ATOM   1261  CB  PHE A 207      41.810  29.967  14.194  1.00  4.91           C  
-ANISOU 1261  CB  PHE A 207      612    654    599      9     20    -47       C  
-ATOM   1262  CG  PHE A 207      40.757  29.813  13.145  1.00  5.26           C  
-ANISOU 1262  CG  PHE A 207      752    740    506     18    187   -110       C  
-ATOM   1263  CD1 PHE A 207      40.491  30.805  12.229  1.00  7.36           C  
-ANISOU 1263  CD1 PHE A 207      947    962    888    199    -58    -90       C  
-ATOM   1264  CD2 PHE A 207      40.125  28.596  12.994  1.00  7.78           C  
-ANISOU 1264  CD2 PHE A 207      916   1065    975   -110    -61   -338       C  
-ATOM   1265  CE1 PHE A 207      39.559  30.566  11.189  1.00  8.93           C  
-ANISOU 1265  CE1 PHE A 207     1081   1269   1040    375     49    -88       C  
-ATOM   1266  CE2 PHE A 207      39.228  28.365  11.985  1.00  9.30           C  
-ANISOU 1266  CE2 PHE A 207      963   1381   1190   -121    125   -586       C  
-ATOM   1267  CZ  PHE A 207      38.957  29.326  11.076  1.00  9.56           C  
-ANISOU 1267  CZ  PHE A 207      875   1660   1098    196    -18   -460       C  
-ATOM   1268  N   ALA A 208      39.259  30.682  16.646  1.00  4.06           N  
-ANISOU 1268  N   ALA A 208      570    382    589     58    101      2       N  
-ATOM   1269  CA  ALA A 208      38.159  30.053  17.365  1.00  4.22           C  
-ANISOU 1269  CA  ALA A 208      588    539    476     26     29    -20       C  
-ATOM   1270  C   ALA A 208      37.280  29.262  16.420  1.00  4.03           C  
-ANISOU 1270  C   ALA A 208      570    499    460     84    102    -26       C  
-ATOM   1271  O   ALA A 208      36.950  29.759  15.341  1.00  4.52           O  
-ANISOU 1271  O   ALA A 208      644    561    510     -1     64    -28       O  
-ATOM   1272  CB  ALA A 208      37.314  31.116  18.066  1.00  4.33           C  
-ANISOU 1272  CB  ALA A 208      633    482    527    100     43   -123       C  
-ATOM   1273  N   PHE A 209      36.832  28.086  16.847  1.00  4.13           N  
-ANISOU 1273  N   PHE A 209      617    508    443     78    -25    -84       N  
-ATOM   1274  CA  PHE A 209      35.917  27.299  16.032  1.00  4.29           C  
-ANISOU 1274  CA  PHE A 209      586    581    462     17     34    -46       C  
-ATOM   1275  C   PHE A 209      34.767  26.643  16.799  1.00  4.92           C  
-ANISOU 1275  C   PHE A 209      693    558    617      6     15    -26       C  
-ATOM   1276  O   PHE A 209      33.910  26.054  16.175  1.00  5.88           O  
-ANISOU 1276  O   PHE A 209      763    864    606   -210    -42    -73       O  
-ATOM   1277  CB  PHE A 209      36.650  26.307  15.114  1.00  5.20           C  
-ANISOU 1277  CB  PHE A 209      703    638    634     19     13   -128       C  
-ATOM   1278  CG  PHE A 209      37.642  25.401  15.804  1.00  4.47           C  
-ANISOU 1278  CG  PHE A 209      617    513    566     30     24    -87       C  
-ATOM   1279  CD1 PHE A 209      38.946  25.329  15.351  1.00  5.09           C  
-ANISOU 1279  CD1 PHE A 209      815    471    646      7    -46   -174       C  
-ATOM   1280  CD2 PHE A 209      37.277  24.589  16.871  1.00  5.60           C  
-ANISOU 1280  CD2 PHE A 209      755    557    814     69    158    -84       C  
-ATOM   1281  CE1 PHE A 209      39.860  24.487  15.961  1.00  5.54           C  
-ANISOU 1281  CE1 PHE A 209      707    515    881    -13     86   -144       C  
-ATOM   1282  CE2 PHE A 209      38.197  23.770  17.490  1.00  5.62           C  
-ANISOU 1282  CE2 PHE A 209      985    516    633    175    184     14       C  
-ATOM   1283  CZ  PHE A 209      39.485  23.718  17.036  1.00  5.35           C  
-ANISOU 1283  CZ  PHE A 209      915    433    683     71    -48   -239       C  
-ATOM   1284  N   ASP A 210      34.671  26.790  18.117  1.00  4.48           N  
-ANISOU 1284  N   ASP A 210      549    637    515     12     62      7       N  
-ATOM   1285  CA  ASP A 210      33.506  26.278  18.829  1.00  4.54           C  
-ANISOU 1285  CA  ASP A 210      596    600    527     27     61     -7       C  
-ATOM   1286  C   ASP A 210      33.416  26.939  20.186  1.00  4.87           C  
-ANISOU 1286  C   ASP A 210      653    694    503     70     47    -10       C  
-ATOM   1287  O   ASP A 210      34.434  27.243  20.807  1.00  5.37           O  
-ANISOU 1287  O   ASP A 210      615    793    632     47     77    -29       O  
-ATOM   1288  CB  ASP A 210      33.563  24.747  18.986  1.00  5.40           C  
-ANISOU 1288  CB  ASP A 210      715    677    661      2    109    -21       C  
-ATOM   1289  CG  ASP A 210      32.703  24.004  17.990  1.00  6.24           C  
-ANISOU 1289  CG  ASP A 210      583    801    985    123    122   -210       C  
-ATOM   1290  OD1 ASP A 210      31.539  24.400  17.804  1.00  8.24           O  
-ANISOU 1290  OD1 ASP A 210      765    893   1472     -7     91   -371       O  
-ATOM   1291  OD2 ASP A 210      33.146  22.998  17.399  1.00  7.53           O  
-ANISOU 1291  OD2 ASP A 210      822    935   1103    170    -36   -200       O  
-ATOM   1292  N   ILE A 211      32.185  27.142  20.640  1.00  4.68           N  
-ANISOU 1292  N   ILE A 211      494    709    574     20     76    -43       N  
-ATOM   1293  CA  ILE A 211      31.895  27.621  21.985  1.00  5.50           C  
-ANISOU 1293  CA  ILE A 211      690    796    601     -3     81     26       C  
-ATOM   1294  C   ILE A 211      30.826  26.724  22.591  1.00  5.81           C  
-ANISOU 1294  C   ILE A 211      682    784    738     17     96     57       C  
-ATOM   1295  O   ILE A 211      29.774  26.520  21.974  1.00  6.36           O  
-ANISOU 1295  O   ILE A 211      686    929    798    -64    110    155       O  
-ATOM   1296  CB  ILE A 211      31.389  29.070  21.984  1.00  5.68           C  
-ANISOU 1296  CB  ILE A 211      729    788    640     59     81      2       C  
-ATOM   1297  CG1 ILE A 211      32.478  30.027  21.508  1.00  6.23           C  
-ANISOU 1297  CG1 ILE A 211      851    820    696     43     77     66       C  
-ATOM   1298  CG2 ILE A 211      30.879  29.474  23.380  1.00  6.65           C  
-ANISOU 1298  CG2 ILE A 211      873    898    755     35     70    -42       C  
-ATOM   1299  CD1 ILE A 211      31.979  31.393  21.132  1.00  7.18           C  
-ANISOU 1299  CD1 ILE A 211     1059    911    758    -42     34     19       C  
-ATOM   1300  N   LYS A 212      31.084  26.194  23.778  1.00  6.06           N  
-ANISOU 1300  N   LYS A 212      656    883    764     11    150    122       N  
-ATOM   1301  CA  LYS A 212      30.056  25.499  24.530  1.00  6.73           C  
-ANISOU 1301  CA  LYS A 212      762    970    823     -1    170     84       C  
-ATOM   1302  C   LYS A 212      30.102  25.925  25.984  1.00  7.26           C  
-ANISOU 1302  C   LYS A 212      826   1055    877      0    238    164       C  
-ATOM   1303  O   LYS A 212      31.136  26.343  26.501  1.00  7.49           O  
-ANISOU 1303  O   LYS A 212      904   1076    865     44    284    100       O  
-ATOM   1304  CB  LYS A 212      30.178  23.980  24.388  1.00  7.13           C  
-ANISOU 1304  CB  LYS A 212      814    981    913    -70    204     74       C  
-ATOM   1305  CG  LYS A 212      31.438  23.374  24.971  1.00  7.54           C  
-ANISOU 1305  CG  LYS A 212      824    948   1091      5    263    160       C  
-ATOM   1306  CD  LYS A 212      31.516  21.876  24.687  1.00  8.44           C  
-ANISOU 1306  CD  LYS A 212     1024   1066   1115    130     92    148       C  
-ATOM   1307  CE  LYS A 212      32.681  21.200  25.387  1.00  9.61           C  
-ANISOU 1307  CE  LYS A 212     1172   1261   1218    142    169     51       C  
-ATOM   1308  NZ  LYS A 212      32.762  19.757  25.023  1.00 10.24           N  
-ANISOU 1308  NZ  LYS A 212     1316   1018   1556    263     -5   -120       N  
-ATOM   1309  N   TYR A 213      28.964  25.807  26.652  1.00  8.18           N  
-ANISOU 1309  N   TYR A 213      950   1287    868     33    244    140       N  
-ATOM   1310  CA  TYR A 213      28.863  26.173  28.048  1.00  9.10           C  
-ANISOU 1310  CA  TYR A 213     1137   1331    987      9    203    137       C  
-ATOM   1311  C   TYR A 213      28.010  25.152  28.799  1.00  9.79           C  
-ANISOU 1311  C   TYR A 213     1193   1497   1029    -11    272    182       C  
-ATOM   1312  O   TYR A 213      27.052  24.616  28.258  1.00 10.39           O  
-ANISOU 1312  O   TYR A 213     1205   1694   1046    -56    421    310       O  
-ATOM   1313  CB  TYR A 213      28.288  27.585  28.209  1.00  9.99           C  
-ANISOU 1313  CB  TYR A 213     1322   1393   1079     26    194    140       C  
-ATOM   1314  CG  TYR A 213      26.865  27.751  27.724  1.00 10.25           C  
-ANISOU 1314  CG  TYR A 213     1316   1469   1110     94    365     30       C  
-ATOM   1315  CD1 TYR A 213      25.784  27.595  28.598  1.00 12.01           C  
-ANISOU 1315  CD1 TYR A 213     1411   1916   1233    186    314     35       C  
-ATOM   1316  CD2 TYR A 213      26.593  28.052  26.397  1.00 12.38           C  
-ANISOU 1316  CD2 TYR A 213     1510   1827   1366    219    423    145       C  
-ATOM   1317  CE1 TYR A 213      24.475  27.742  28.155  1.00 11.74           C  
-ANISOU 1317  CE1 TYR A 213     1310   1834   1316    213    377    -34       C  
-ATOM   1318  CE2 TYR A 213      25.287  28.190  25.946  1.00 12.74           C  
-ANISOU 1318  CE2 TYR A 213     1591   1979   1270    304    288     78       C  
-ATOM   1319  CZ  TYR A 213      24.232  28.035  26.833  1.00 13.36           C  
-ANISOU 1319  CZ  TYR A 213     1434   2099   1541    234    205     80       C  
-ATOM   1320  OH  TYR A 213      22.926  28.175  26.413  1.00 14.73           O  
-ANISOU 1320  OH  TYR A 213     1467   2497   1633    505    218    -86       O  
-ATOM   1321  N   SER A 214      28.401  24.861  30.028  1.00 10.36           N  
-ANISOU 1321  N   SER A 214     1241   1563   1129     -2    314    240       N  
-ATOM   1322  CA  SER A 214      27.632  23.989  30.905  1.00 11.23           C  
-ANISOU 1322  CA  SER A 214     1409   1606   1251     11    347    179       C  
-ATOM   1323  C   SER A 214      27.269  24.780  32.140  1.00 12.45           C  
-ANISOU 1323  C   SER A 214     1561   1725   1444     64    321    174       C  
-ATOM   1324  O   SER A 214      28.138  25.188  32.900  1.00 12.05           O  
-ANISOU 1324  O   SER A 214     1614   1909   1054    115    608    223       O  
-ATOM   1325  CB  SER A 214      28.446  22.771  31.309  1.00 11.65           C  
-ANISOU 1325  CB  SER A 214     1579   1571   1273     35    305    207       C  
-ATOM   1326  OG  SER A 214      27.737  22.044  32.291  1.00 13.02           O  
-ANISOU 1326  OG  SER A 214     1768   1748   1429      7    533    519       O  
-ATOM   1327  N   VAL A 215      25.977  25.012  32.330  1.00 12.94           N  
-ANISOU 1327  N   VAL A 215     1610   1779   1526     35    396    152       N  
-ATOM   1328  CA  VAL A 215      25.506  25.806  33.460  1.00 14.76           C  
-ANISOU 1328  CA  VAL A 215     1880   1959   1769     27    296     61       C  
-ATOM   1329  C   VAL A 215      25.888  25.132  34.784  1.00 14.82           C  
-ANISOU 1329  C   VAL A 215     1866   2042   1724     17    416     61       C  
-ATOM   1330  O   VAL A 215      26.523  25.743  35.618  1.00 14.66           O  
-ANISOU 1330  O   VAL A 215     1894   2255   1420     -1    794     84       O  
-ATOM   1331  CB  VAL A 215      23.993  26.079  33.344  1.00 15.29           C  
-ANISOU 1331  CB  VAL A 215     1881   2040   1888     26    335     36       C  
-ATOM   1332  CG1 VAL A 215      23.483  26.864  34.552  1.00 17.03           C  
-ANISOU 1332  CG1 VAL A 215     2138   2239   2093     42    310    -36       C  
-ATOM   1333  CG2 VAL A 215      23.682  26.820  32.027  1.00 17.22           C  
-ANISOU 1333  CG2 VAL A 215     2122   2151   2267     44    251     -4       C  
-ATOM   1334  N   SER A 216      25.588  23.846  34.916  1.00 15.58           N  
-ANISOU 1334  N   SER A 216     2032   2081   1806     28    328     62       N  
-ATOM   1335  CA  SER A 216      25.933  23.085  36.117  1.00 16.20           C  
-ANISOU 1335  CA  SER A 216     2132   2148   1873     -3    233     91       C  
-ATOM   1336  C   SER A 216      27.445  22.859  36.224  1.00 16.26           C  
-ANISOU 1336  C   SER A 216     2168   2221   1786      0    241    118       C  
-ATOM   1337  O   SER A 216      27.991  22.721  37.320  1.00 17.40           O  
-ANISOU 1337  O   SER A 216     2345   2574   1689     56    383    151       O  
-ATOM   1338  CB  SER A 216      25.210  21.737  36.095  1.00 16.70           C  
-ANISOU 1338  CB  SER A 216     2213   2217   1914    -19    232    114       C  
-ATOM   1339  OG  SER A 216      25.802  20.883  35.133  1.00 17.35           O  
-ANISOU 1339  OG  SER A 216     2395   2111   2084    -78    485    294       O  
-ATOM   1340  N   GLY A 217      28.118  22.834  35.072  1.00 15.37           N  
-ANISOU 1340  N   GLY A 217     2087   2054   1696     13    247    146       N  
-ATOM   1341  CA  GLY A 217      29.517  22.458  34.985  1.00 15.34           C  
-ANISOU 1341  CA  GLY A 217     2075   1979   1774     -9    122    106       C  
-ATOM   1342  C   GLY A 217      29.713  21.020  34.546  1.00 15.78           C  
-ANISOU 1342  C   GLY A 217     2099   2051   1845     35     90    109       C  
-ATOM   1343  O   GLY A 217      30.794  20.661  34.108  1.00 15.70           O  
-ANISOU 1343  O   GLY A 217     2068   2073   1821    125    168    119       O  
-ATOM   1344  N   ALA A 218      28.673  20.197  34.662  1.00 15.24           N  
-ANISOU 1344  N   ALA A 218     2079   1971   1739     26    123    124       N  
-ATOM   1345  CA  ALA A 218      28.756  18.795  34.282  1.00 15.76           C  
-ANISOU 1345  CA  ALA A 218     2100   1968   1919     28     95    122       C  
-ATOM   1346  C   ALA A 218      28.910  18.623  32.775  1.00 15.52           C  
-ANISOU 1346  C   ALA A 218     2117   1890   1890     35    115    164       C  
-ATOM   1347  O   ALA A 218      28.307  19.363  31.989  1.00 14.57           O  
-ANISOU 1347  O   ALA A 218     2080   1706   1749     47    236    375       O  
-ATOM   1348  CB  ALA A 218      27.532  18.046  34.772  1.00 16.73           C  
-ANISOU 1348  CB  ALA A 218     2222   2101   2030      6    121    142       C  
-ATOM   1349  N   GLU A 219      29.705  17.632  32.382  1.00 16.12           N  
-ANISOU 1349  N   GLU A 219     2184   1953   1987     10     71    142       N  
-ATOM   1350  CA  GLU A 219      29.967  17.343  30.976  1.00 16.67           C  
-ANISOU 1350  CA  GLU A 219     2212   1992   2130    -16     96    109       C  
-ATOM   1351  C   GLU A 219      28.684  17.103  30.180  1.00 16.86           C  
-ANISOU 1351  C   GLU A 219     2215   2028   2163    -51    113    123       C  
-ATOM   1352  O   GLU A 219      28.535  17.568  29.050  1.00 16.76           O  
-ANISOU 1352  O   GLU A 219     2216   2005   2147   -158    175    163       O  
-ATOM   1353  CB  GLU A 219      30.864  16.105  30.858  1.00 17.27           C  
-ANISOU 1353  CB  GLU A 219     2278   2053   2229     15     86     85       C  
-ATOM   1354  CG  GLU A 219      31.492  15.913  29.484  1.00 19.58           C  
-ANISOU 1354  CG  GLU A 219     2592   2342   2506      7    189    106       C  
-ATOM   1355  CD  GLU A 219      32.713  16.793  29.232  1.00 21.43           C  
-ANISOU 1355  CD  GLU A 219     2802   2528   2811    -19    195    102       C  
-ATOM   1356  OE1 GLU A 219      33.159  17.537  30.130  1.00 22.59           O  
-ANISOU 1356  OE1 GLU A 219     2847   2614   3122   -201    481    273       O  
-ATOM   1357  OE2 GLU A 219      33.250  16.717  28.122  1.00 23.75           O  
-ANISOU 1357  OE2 GLU A 219     3102   2903   3016   -455    361    381       O  
-ATOM   1358  N   GLU A 220      27.748  16.376  30.781  1.00 17.05           N  
-ANISOU 1358  N   GLU A 220     2271   2002   2203    -69     88    168       N  
-ATOM   1359  CA  GLU A 220      26.516  16.008  30.093  1.00 17.61           C  
-ANISOU 1359  CA  GLU A 220     2290   2124   2277    -56     92    131       C  
-ATOM   1360  C   GLU A 220      25.578  17.197  29.861  1.00 16.92           C  
-ANISOU 1360  C   GLU A 220     2208   2027   2194    -83     98    161       C  
-ATOM   1361  O   GLU A 220      24.645  17.093  29.075  1.00 17.81           O  
-ANISOU 1361  O   GLU A 220     2386   2074   2304   -142     96    173       O  
-ATOM   1362  CB  GLU A 220      25.789  14.888  30.836  1.00 18.53           C  
-ANISOU 1362  CB  GLU A 220     2410   2217   2410    -75     77    145       C  
-ATOM   1363  CG  GLU A 220      25.267  15.282  32.208  1.00 20.37           C  
-ANISOU 1363  CG  GLU A 220     2725   2393   2620   -105    144    168       C  
-ATOM   1364  CD  GLU A 220      26.232  14.956  33.338  1.00 21.82           C  
-ANISOU 1364  CD  GLU A 220     2966   2493   2830   -199    158    273       C  
-ATOM   1365  OE1 GLU A 220      27.466  14.945  33.101  1.00 21.37           O  
-ANISOU 1365  OE1 GLU A 220     3203   2100   2814   -438    237    401       O  
-ATOM   1366  OE2 GLU A 220      25.751  14.718  34.478  1.00 24.13           O  
-ANISOU 1366  OE2 GLU A 220     3424   2741   3001   -387    309    312       O  
-ATOM   1367  N   ASP A 221      25.822  18.311  30.545  1.00 15.84           N  
-ANISOU 1367  N   ASP A 221     2030   1948   2040    -94    159    201       N  
-ATOM   1368  CA  ASP A 221      24.996  19.506  30.399  1.00 15.23           C  
-ANISOU 1368  CA  ASP A 221     1894   1932   1960   -101    216    197       C  
-ATOM   1369  C   ASP A 221      25.567  20.556  29.458  1.00 13.46           C  
-ANISOU 1369  C   ASP A 221     1608   1759   1747    -67    299    254       C  
-ATOM   1370  O   ASP A 221      25.019  21.653  29.374  1.00 13.72           O  
-ANISOU 1370  O   ASP A 221     1529   1835   1847    -51    501    451       O  
-ATOM   1371  CB  ASP A 221      24.778  20.149  31.765  1.00 15.70           C  
-ANISOU 1371  CB  ASP A 221     1984   1982   1996   -150    227    234       C  
-ATOM   1372  CG  ASP A 221      23.989  19.274  32.694  1.00 18.25           C  
-ANISOU 1372  CG  ASP A 221     2274   2354   2303   -316    366    303       C  
-ATOM   1373  OD1 ASP A 221      23.201  18.448  32.193  1.00 21.13           O  
-ANISOU 1373  OD1 ASP A 221     2593   3022   2412   -563    810    636       O  
-ATOM   1374  OD2 ASP A 221      24.108  19.355  33.929  1.00 20.61           O  
-ANISOU 1374  OD2 ASP A 221     2596   2687   2548   -511    824    453       O  
-ATOM   1375  N   PHE A 222      26.648  20.252  28.748  1.00 12.34           N  
-ANISOU 1375  N   PHE A 222     1465   1604   1619      1    257    248       N  
-ATOM   1376  CA  PHE A 222      27.171  21.223  27.800  1.00 11.54           C  
-ANISOU 1376  CA  PHE A 222     1389   1545   1448    -46    207    161       C  
-ATOM   1377  C   PHE A 222      26.120  21.547  26.740  1.00 11.30           C  
-ANISOU 1377  C   PHE A 222     1265   1523   1505    -46    188    127       C  
-ATOM   1378  O   PHE A 222      25.434  20.654  26.228  1.00 12.86           O  
-ANISOU 1378  O   PHE A 222     1406   1615   1865   -130    165    246       O  
-ATOM   1379  CB  PHE A 222      28.449  20.714  27.121  1.00 11.73           C  
-ANISOU 1379  CB  PHE A 222     1349   1633   1474    -13    251    132       C  
-ATOM   1380  CG  PHE A 222      29.716  21.066  27.861  1.00 11.00           C  
-ANISOU 1380  CG  PHE A 222     1312   1566   1301     23    239    218       C  
-ATOM   1381  CD1 PHE A 222      30.053  22.388  28.100  1.00  9.98           C  
-ANISOU 1381  CD1 PHE A 222     1219   1410   1161     -1    301    211       C  
-ATOM   1382  CD2 PHE A 222      30.572  20.075  28.318  1.00 11.24           C  
-ANISOU 1382  CD2 PHE A 222     1369   1552   1348    -15    240    215       C  
-ATOM   1383  CE1 PHE A 222      31.214  22.716  28.773  1.00 10.17           C  
-ANISOU 1383  CE1 PHE A 222     1341   1468   1052    -67    240    164       C  
-ATOM   1384  CE2 PHE A 222      31.740  20.408  28.987  1.00 11.02           C  
-ANISOU 1384  CE2 PHE A 222     1312   1576   1297     88    159    219       C  
-ATOM   1385  CZ  PHE A 222      32.055  21.727  29.212  1.00 10.77           C  
-ANISOU 1385  CZ  PHE A 222     1205   1547   1339    -65    302    251       C  
-ATOM   1386  N   VAL A 223      26.035  22.828  26.411  1.00 10.43           N  
-ANISOU 1386  N   VAL A 223     1093   1485   1383    -66    249    165       N  
-ATOM   1387  CA  VAL A 223      25.230  23.347  25.315  1.00 10.08           C  
-ANISOU 1387  CA  VAL A 223     1057   1479   1292    -35    236     89       C  
-ATOM   1388  C   VAL A 223      26.205  23.972  24.318  1.00  8.82           C  
-ANISOU 1388  C   VAL A 223      825   1318   1205    -42    219    105       C  
-ATOM   1389  O   VAL A 223      26.967  24.855  24.669  1.00  8.59           O  
-ANISOU 1389  O   VAL A 223      961   1268   1033    -49    276      3       O  
-ATOM   1390  CB  VAL A 223      24.244  24.414  25.819  1.00 10.69           C  
-ANISOU 1390  CB  VAL A 223     1151   1599   1309     18    273    103       C  
-ATOM   1391  CG1 VAL A 223      23.513  25.057  24.660  1.00 11.99           C  
-ANISOU 1391  CG1 VAL A 223     1264   1722   1569    124    257    122       C  
-ATOM   1392  CG2 VAL A 223      23.257  23.799  26.816  1.00 12.04           C  
-ANISOU 1392  CG2 VAL A 223     1234   1875   1463     67    365    110       C  
-ATOM   1393  N   LEU A 224      26.168  23.493  23.088  1.00  8.70           N  
-ANISOU 1393  N   LEU A 224      911   1156   1235    -75    226     72       N  
-ATOM   1394  CA  LEU A 224      27.019  23.989  22.026  1.00  8.23           C  
-ANISOU 1394  CA  LEU A 224      922   1110   1093    -52    157     32       C  
-ATOM   1395  C   LEU A 224      26.317  25.098  21.264  1.00  7.49           C  
-ANISOU 1395  C   LEU A 224      799   1026   1019    -19    129    -16       C  
-ATOM   1396  O   LEU A 224      25.157  24.945  20.894  1.00  8.97           O  
-ANISOU 1396  O   LEU A 224      810   1261   1337   -102     60     -2       O  
-ATOM   1397  CB  LEU A 224      27.327  22.825  21.093  1.00  9.17           C  
-ANISOU 1397  CB  LEU A 224     1020   1219   1242    -78    202      6       C  
-ATOM   1398  CG  LEU A 224      28.348  23.056  19.987  1.00  9.77           C  
-ANISOU 1398  CG  LEU A 224     1242   1286   1180     -7     96    -21       C  
-ATOM   1399  CD1 LEU A 224      29.725  23.376  20.537  1.00  9.18           C  
-ANISOU 1399  CD1 LEU A 224      998   1208   1283    -89    234    -76       C  
-ATOM   1400  CD2 LEU A 224      28.410  21.834  19.078  1.00 10.60           C  
-ANISOU 1400  CD2 LEU A 224     1195   1360   1470   -114    122   -291       C  
-ATOM   1401  N   LEU A 225      26.994  26.218  21.040  1.00  7.19           N  
-ANISOU 1401  N   LEU A 225      804   1023    902      4     79     -6       N  
-ATOM   1402  CA  LEU A 225      26.421  27.253  20.188  1.00  7.00           C  
-ANISOU 1402  CA  LEU A 225      748    955    956     38     77    -16       C  
-ATOM   1403  C   LEU A 225      26.317  26.770  18.758  1.00  6.71           C  
-ANISOU 1403  C   LEU A 225      713    865    968     51     13    -16       C  
-ATOM   1404  O   LEU A 225      27.252  26.178  18.231  1.00  7.13           O  
-ANISOU 1404  O   LEU A 225      790    883   1037    105    -20   -117       O  
-ATOM   1405  CB  LEU A 225      27.243  28.549  20.247  1.00  6.82           C  
-ANISOU 1405  CB  LEU A 225      754    971    867      9     54    -99       C  
-ATOM   1406  CG  LEU A 225      27.296  29.274  21.595  1.00  8.80           C  
-ANISOU 1406  CG  LEU A 225     1091   1242   1010     29     90    -98       C  
-ATOM   1407  CD1 LEU A 225      27.938  30.630  21.427  1.00  8.14           C  
-ANISOU 1407  CD1 LEU A 225      974   1011   1105    176    -40   -235       C  
-ATOM   1408  CD2 LEU A 225      25.946  29.449  22.241  1.00 10.97           C  
-ANISOU 1408  CD2 LEU A 225     1444   1491   1230    -76    111   -200       C  
-ATOM   1409  N   GLY A 226      25.175  27.033  18.133  1.00  7.08           N  
-ANISOU 1409  N   GLY A 226      746    929   1014     54     24    -67       N  
-ATOM   1410  CA  GLY A 226      25.039  26.869  16.704  1.00  6.86           C  
-ANISOU 1410  CA  GLY A 226      773    837    996     84    -25   -108       C  
-ATOM   1411  C   GLY A 226      25.896  27.870  15.955  1.00  6.61           C  
-ANISOU 1411  C   GLY A 226      685    807   1019     70    -25   -145       C  
-ATOM   1412  O   GLY A 226      26.406  28.821  16.539  1.00  7.19           O  
-ANISOU 1412  O   GLY A 226      854    761   1113    -37     -9   -210       O  
-ATOM   1413  N   TYR A 227      26.044  27.687  14.646  1.00  6.91           N  
-ANISOU 1413  N   TYR A 227      781    835   1007    -33     29   -166       N  
-ATOM   1414  CA  TYR A 227      26.919  28.543  13.853  1.00  7.24           C  
-ANISOU 1414  CA  TYR A 227      769    958   1024      2     74   -213       C  
-ATOM   1415  C   TYR A 227      26.574  30.023  13.980  1.00  6.76           C  
-ANISOU 1415  C   TYR A 227      751    954    861     -7     98   -228       C  
-ATOM   1416  O   TYR A 227      27.445  30.851  14.203  1.00  6.25           O  
-ANISOU 1416  O   TYR A 227      736    877    761   -117    102   -198       O  
-ATOM   1417  CB  TYR A 227      26.930  28.122  12.352  1.00  7.91           C  
-ANISOU 1417  CB  TYR A 227      861   1032   1113    -74    180   -343       C  
-ATOM   1418  CG  TYR A 227      27.696  29.136  11.473  1.00  9.15           C  
-ANISOU 1418  CG  TYR A 227     1058   1128   1291   -125    128   -539       C  
-ATOM   1419  CD1 TYR A 227      29.083  29.141  11.432  1.00 10.29           C  
-ANISOU 1419  CD1 TYR A 227     1215   1089   1604     45     -1   -336       C  
-ATOM   1420  CD2 TYR A 227      27.011  30.140  10.784  1.00 10.53           C  
-ANISOU 1420  CD2 TYR A 227     1443   1373   1183   -160    158   -149       C  
-ATOM   1421  CE1 TYR A 227      29.782  30.112  10.719  1.00  8.22           C  
-ANISOU 1421  CE1 TYR A 227     1129    903   1091    -52    312   -114       C  
-ATOM   1422  CE2 TYR A 227      27.690  31.107  10.066  1.00 10.52           C  
-ANISOU 1422  CE2 TYR A 227     1357   1311   1328    185    -27    104       C  
-ATOM   1423  CZ  TYR A 227      29.078  31.065  10.038  1.00  9.31           C  
-ANISOU 1423  CZ  TYR A 227     1053   1274   1209    247    -15   -230       C  
-ATOM   1424  OH  TYR A 227      29.796  32.020   9.359  1.00 10.28           O  
-ANISOU 1424  OH  TYR A 227     1245   1307   1352     49     93     37       O  
-ATOM   1425  N   ASP A 228      25.310  30.366  13.791  1.00  7.22           N  
-ANISOU 1425  N   ASP A 228      775    939   1026      2    -40   -155       N  
-ATOM   1426  CA  ASP A 228      24.946  31.778  13.815  1.00  7.96           C  
-ANISOU 1426  CA  ASP A 228      918   1043   1064     19    -35    -98       C  
-ATOM   1427  C   ASP A 228      25.205  32.398  15.177  1.00  7.24           C  
-ANISOU 1427  C   ASP A 228      826    895   1027    105    -23   -120       C  
-ATOM   1428  O   ASP A 228      25.679  33.525  15.246  1.00  7.82           O  
-ANISOU 1428  O   ASP A 228     1041    880   1050    120    -20    -95       O  
-ATOM   1429  CB  ASP A 228      23.484  31.992  13.407  1.00  9.17           C  
-ANISOU 1429  CB  ASP A 228     1005   1185   1294    -15   -193    -47       C  
-ATOM   1430  CG  ASP A 228      23.252  31.843  11.931  1.00 11.34           C  
-ANISOU 1430  CG  ASP A 228     1204   1629   1476    -18   -180      3       C  
-ATOM   1431  OD1 ASP A 228      24.163  32.145  11.128  1.00 13.40           O  
-ANISOU 1431  OD1 ASP A 228     1646   2215   1228   -106   -400   -120       O  
-ATOM   1432  OD2 ASP A 228      22.162  31.439  11.489  1.00 14.93           O  
-ANISOU 1432  OD2 ASP A 228     1601   2246   1824   -170   -564     99       O  
-ATOM   1433  N   GLU A 229      24.890  31.673  16.250  1.00  7.21           N  
-ANISOU 1433  N   GLU A 229      805    883   1052     77     32   -179       N  
-ATOM   1434  CA  GLU A 229      25.155  32.179  17.590  1.00  7.44           C  
-ANISOU 1434  CA  GLU A 229      923    941    961     50    117   -130       C  
-ATOM   1435  C   GLU A 229      26.655  32.275  17.870  1.00  6.13           C  
-ANISOU 1435  C   GLU A 229      752    789    786     21    157   -132       C  
-ATOM   1436  O   GLU A 229      27.114  33.219  18.502  1.00  6.44           O  
-ANISOU 1436  O   GLU A 229      846    792    805     69    112   -158       O  
-ATOM   1437  CB  GLU A 229      24.560  31.264  18.656  1.00  9.08           C  
-ANISOU 1437  CB  GLU A 229     1083   1342   1025     33    303   -238       C  
-ATOM   1438  CG  GLU A 229      23.087  30.921  18.670  1.00 13.85           C  
-ANISOU 1438  CG  GLU A 229     1646   1902   1712     61    145    -88       C  
-ATOM   1439  CD  GLU A 229      22.817  29.847  19.722  1.00 18.14           C  
-ANISOU 1439  CD  GLU A 229     2025   2446   2420    225    300    -57       C  
-ATOM   1440  OE1 GLU A 229      23.134  28.620  19.554  1.00 17.67           O  
-ANISOU 1440  OE1 GLU A 229     1535   2741   2436    732    602    284       O  
-ATOM   1441  OE2 GLU A 229      22.359  30.263  20.782  1.00 22.73           O  
-ANISOU 1441  OE2 GLU A 229     2889   2959   2786    523    158   -336       O  
-ATOM   1442  N   PHE A 230      27.411  31.281  17.400  1.00  5.77           N  
-ANISOU 1442  N   PHE A 230      699    681    809     31     64   -138       N  
-ATOM   1443  CA  PHE A 230      28.858  31.280  17.530  1.00  5.97           C  
-ANISOU 1443  CA  PHE A 230      728    777    761     48     81    -86       C  
-ATOM   1444  C   PHE A 230      29.440  32.551  16.899  1.00  5.37           C  
-ANISOU 1444  C   PHE A 230      630    704    706      6     39   -128       C  
-ATOM   1445  O   PHE A 230      30.287  33.219  17.494  1.00  5.87           O  
-ANISOU 1445  O   PHE A 230      689    773    768     13     52   -114       O  
-ATOM   1446  CB  PHE A 230      29.439  30.020  16.878  1.00  5.88           C  
-ANISOU 1446  CB  PHE A 230      759    748    724     26    127   -112       C  
-ATOM   1447  CG  PHE A 230      30.927  30.071  16.714  1.00  5.41           C  
-ANISOU 1447  CG  PHE A 230      652    690    711     23    127    -60       C  
-ATOM   1448  CD1 PHE A 230      31.768  29.788  17.779  1.00  5.23           C  
-ANISOU 1448  CD1 PHE A 230      796    610    580     66    126    -76       C  
-ATOM   1449  CD2 PHE A 230      31.489  30.414  15.503  1.00  6.29           C  
-ANISOU 1449  CD2 PHE A 230      903    894    591     80     18    -87       C  
-ATOM   1450  CE1 PHE A 230      33.141  29.846  17.624  1.00  6.07           C  
-ANISOU 1450  CE1 PHE A 230      772    760    773    106     69      0       C  
-ATOM   1451  CE2 PHE A 230      32.870  30.471  15.352  1.00  6.24           C  
-ANISOU 1451  CE2 PHE A 230      656    826    885     95    190     56       C  
-ATOM   1452  CZ  PHE A 230      33.691  30.207  16.413  1.00  6.03           C  
-ANISOU 1452  CZ  PHE A 230      665    687    935    152    174   -128       C  
-ATOM   1453  N   VAL A 231      29.005  32.874  15.692  1.00  6.02           N  
-ANISOU 1453  N   VAL A 231      806    762    719     -4     18   -141       N  
-ATOM   1454  CA  VAL A 231      29.494  34.075  15.026  1.00  7.26           C  
-ANISOU 1454  CA  VAL A 231     1051    875    831    -33    -40   -105       C  
-ATOM   1455  C   VAL A 231      29.042  35.345  15.750  1.00  7.15           C  
-ANISOU 1455  C   VAL A 231     1009    897    810    -23   -114    -78       C  
-ATOM   1456  O   VAL A 231      29.809  36.292  15.914  1.00  7.68           O  
-ANISOU 1456  O   VAL A 231     1107    844    966    -57   -163    -41       O  
-ATOM   1457  CB  VAL A 231      29.039  34.095  13.559  1.00  8.59           C  
-ANISOU 1457  CB  VAL A 231     1406    921    936    -21     42    -85       C  
-ATOM   1458  CG1 VAL A 231      29.184  35.478  12.942  1.00  9.90           C  
-ANISOU 1458  CG1 VAL A 231     1427   1171   1160      1    -20   -138       C  
-ATOM   1459  CG2 VAL A 231      29.770  33.030  12.771  1.00  9.96           C  
-ANISOU 1459  CG2 VAL A 231     1572   1152   1060    -63     84   -111       C  
-ATOM   1460  N   GLU A 232      27.795  35.382  16.192  1.00  7.19           N  
-ANISOU 1460  N   GLU A 232      990    841    898     84   -148   -100       N  
-ATOM   1461  CA  GLU A 232      27.276  36.556  16.891  1.00  8.30           C  
-ANISOU 1461  CA  GLU A 232     1180    962   1011    122   -125   -113       C  
-ATOM   1462  C   GLU A 232      28.099  36.848  18.136  1.00  7.68           C  
-ANISOU 1462  C   GLU A 232     1124    837    957    129   -136   -107       C  
-ATOM   1463  O   GLU A 232      28.558  37.970  18.328  1.00  9.16           O  
-ANISOU 1463  O   GLU A 232     1647    850    983    103   -298    -58       O  
-ATOM   1464  CB  GLU A 232      25.816  36.329  17.257  1.00  9.62           C  
-ANISOU 1464  CB  GLU A 232     1260   1160   1234    235   -137   -197       C  
-ATOM   1465  CG  GLU A 232      25.122  37.393  18.094  1.00 16.37           C  
-ANISOU 1465  CG  GLU A 232     2061   2171   1988    153    -92   -247       C  
-ATOM   1466  CD  GLU A 232      23.752  36.913  18.571  1.00 22.64           C  
-ANISOU 1466  CD  GLU A 232     2843   3210   2546     55    -99   -329       C  
-ATOM   1467  OE1 GLU A 232      23.463  36.970  19.792  1.00 27.98           O  
-ANISOU 1467  OE1 GLU A 232     3432   4141   3058    156    -91   -336       O  
-ATOM   1468  OE2 GLU A 232      22.958  36.454  17.717  1.00 28.26           O  
-ANISOU 1468  OE2 GLU A 232     3207   4231   3297    115   -204   -369       O  
-ATOM   1469  N   PHE A 233      28.283  35.851  18.984  1.00  6.42           N  
-ANISOU 1469  N   PHE A 233      933    812    693     67      1   -128       N  
-ATOM   1470  CA  PHE A 233      29.073  36.053  20.182  1.00  6.59           C  
-ANISOU 1470  CA  PHE A 233      938    840    724     99    -10   -109       C  
-ATOM   1471  C   PHE A 233      30.542  36.335  19.861  1.00  5.94           C  
-ANISOU 1471  C   PHE A 233      885    740    631     90    -52   -165       C  
-ATOM   1472  O   PHE A 233      31.124  37.248  20.425  1.00  6.73           O  
-ANISOU 1472  O   PHE A 233      974    812    769     35   -100   -228       O  
-ATOM   1473  CB  PHE A 233      28.918  34.851  21.126  1.00  7.35           C  
-ANISOU 1473  CB  PHE A 233     1038    973    779     64     -6   -125       C  
-ATOM   1474  CG  PHE A 233      27.628  34.870  21.910  1.00  8.06           C  
-ANISOU 1474  CG  PHE A 233     1255   1091    714    -18    198   -241       C  
-ATOM   1475  CD1 PHE A 233      27.508  35.630  23.064  1.00 11.39           C  
-ANISOU 1475  CD1 PHE A 233     1546   1656   1124   -125    249   -328       C  
-ATOM   1476  CD2 PHE A 233      26.518  34.163  21.494  1.00  9.90           C  
-ANISOU 1476  CD2 PHE A 233     1380   1369   1011    -96    332   -302       C  
-ATOM   1477  CE1 PHE A 233      26.307  35.669  23.781  1.00 11.72           C  
-ANISOU 1477  CE1 PHE A 233     1753   1731    966   -162    259   -620       C  
-ATOM   1478  CE2 PHE A 233      25.323  34.204  22.217  1.00 11.98           C  
-ANISOU 1478  CE2 PHE A 233     1614   1869   1066   -209    223   -414       C  
-ATOM   1479  CZ  PHE A 233      25.219  34.953  23.352  1.00 12.17           C  
-ANISOU 1479  CZ  PHE A 233     1641   1850   1132   -153    336   -408       C  
-ATOM   1480  N   SER A 234      31.141  35.562  18.961  1.00  5.65           N  
-ANISOU 1480  N   SER A 234      790    704    653     -2    -25   -163       N  
-ATOM   1481  CA  SER A 234      32.563  35.737  18.674  1.00  6.07           C  
-ANISOU 1481  CA  SER A 234      829    709    766     48    -15   -100       C  
-ATOM   1482  C   SER A 234      32.854  37.127  18.121  1.00  6.37           C  
-ANISOU 1482  C   SER A 234      809    763    846     21      4   -108       C  
-ATOM   1483  O   SER A 234      33.880  37.712  18.422  1.00  6.95           O  
-ANISOU 1483  O   SER A 234      922    671   1046    -34      1   -102       O  
-ATOM   1484  CB  SER A 234      33.056  34.677  17.690  1.00  6.06           C  
-ANISOU 1484  CB  SER A 234      710    823    768     75    -30    -69       C  
-ATOM   1485  OG  SER A 234      33.032  33.383  18.253  1.00  6.86           O  
-ANISOU 1485  OG  SER A 234      886    681   1037     97      0    -80       O  
-ATOM   1486  N   SER A 235      31.927  37.648  17.327  1.00  6.64           N  
-ANISOU 1486  N   SER A 235      917    808    796    -54    -42    -58       N  
-ATOM   1487  CA  SER A 235      32.088  38.960  16.730  1.00  8.07           C  
-ANISOU 1487  CA  SER A 235     1079    953   1032    -29    -58     61       C  
-ATOM   1488  C   SER A 235      32.074  40.074  17.772  1.00  8.02           C  
-ANISOU 1488  C   SER A 235     1095    840   1112    -14   -143     22       C  
-ATOM   1489  O   SER A 235      32.512  41.179  17.487  1.00  9.81           O  
-ANISOU 1489  O   SER A 235     1516    866   1343   -155    -58     60       O  
-ATOM   1490  CB  SER A 235      30.990  39.214  15.689  1.00  9.11           C  
-ANISOU 1490  CB  SER A 235     1259   1116   1085    -54    -67    108       C  
-ATOM   1491  OG  SER A 235      29.741  39.475  16.288  1.00 11.64           O  
-ANISOU 1491  OG  SER A 235     1518   1472   1432   -129   -382    449       O  
-ATOM   1492  N   LYS A 236      31.562  39.791  18.961  1.00  7.48           N  
-ANISOU 1492  N   LYS A 236     1061    701   1078    116   -173    -45       N  
-ATOM   1493  CA  LYS A 236      31.507  40.755  20.050  1.00  8.33           C  
-ANISOU 1493  CA  LYS A 236     1129    850   1183    139   -124   -103       C  
-ATOM   1494  C   LYS A 236      32.664  40.610  21.030  1.00  7.71           C  
-ANISOU 1494  C   LYS A 236     1111    770   1046    195   -181   -163       C  
-ATOM   1495  O   LYS A 236      32.768  41.369  21.982  1.00  9.97           O  
-ANISOU 1495  O   LYS A 236     1355   1046   1387    390   -242   -485       O  
-ATOM   1496  CB  LYS A 236      30.182  40.620  20.791  1.00  9.18           C  
-ANISOU 1496  CB  LYS A 236     1220    985   1281    209   -146    -88       C  
-ATOM   1497  CG  LYS A 236      28.984  40.959  19.941  1.00 11.90           C  
-ANISOU 1497  CG  LYS A 236     1407   1323   1788    166   -151   -148       C  
-ATOM   1498  CD  LYS A 236      27.680  40.728  20.698  1.00 15.72           C  
-ANISOU 1498  CD  LYS A 236     1878   1944   2149     89   -128    -85       C  
-ATOM   1499  CE  LYS A 236      26.461  40.951  19.825  1.00 18.83           C  
-ANISOU 1499  CE  LYS A 236     2182   2400   2571     75    -50    -68       C  
-ATOM   1500  NZ  LYS A 236      25.221  40.474  20.501  1.00 23.29           N  
-ANISOU 1500  NZ  LYS A 236     2819   2845   3185    -17    138    -65       N  
-ATOM   1501  N   VAL A 237      33.530  39.630  20.824  1.00  7.05           N  
-ANISOU 1501  N   VAL A 237      980    753    944    210   -117   -170       N  
-ATOM   1502  CA  VAL A 237      34.682  39.423  21.688  1.00  7.08           C  
-ANISOU 1502  CA  VAL A 237     1017    783    889     87   -115   -142       C  
-ATOM   1503  C   VAL A 237      35.854  40.128  21.004  1.00  6.95           C  
-ANISOU 1503  C   VAL A 237     1019    715    907    131   -154   -225       C  
-ATOM   1504  O   VAL A 237      36.223  39.774  19.891  1.00  7.15           O  
-ANISOU 1504  O   VAL A 237     1087    660    968     77   -130   -164       O  
-ATOM   1505  CB  VAL A 237      34.966  37.932  21.869  1.00  6.70           C  
-ANISOU 1505  CB  VAL A 237     1010    806    730     94   -117   -190       C  
-ATOM   1506  CG1 VAL A 237      36.233  37.736  22.678  1.00  7.71           C  
-ANISOU 1506  CG1 VAL A 237      992    982    956     55   -210   -115       C  
-ATOM   1507  CG2 VAL A 237      33.807  37.235  22.539  1.00  7.40           C  
-ANISOU 1507  CG2 VAL A 237     1115    907    788    118   -119    -49       C  
-ATOM   1508  N   PRO A 238      36.429  41.156  21.629  1.00  7.80           N  
-ANISOU 1508  N   PRO A 238     1091    786   1085     85    -68   -213       N  
-ATOM   1509  CA  PRO A 238      37.351  42.034  20.903  1.00  7.31           C  
-ANISOU 1509  CA  PRO A 238     1070    662   1042     97    -80   -209       C  
-ATOM   1510  C   PRO A 238      38.607  41.300  20.442  1.00  7.45           C  
-ANISOU 1510  C   PRO A 238     1099    591   1138    104    -98   -179       C  
-ATOM   1511  O   PRO A 238      39.302  40.676  21.236  1.00  7.80           O  
-ANISOU 1511  O   PRO A 238     1160    727   1074    160   -191   -157       O  
-ATOM   1512  CB  PRO A 238      37.703  43.117  21.945  1.00  8.39           C  
-ANISOU 1512  CB  PRO A 238     1186    758   1244     36    -15   -298       C  
-ATOM   1513  CG  PRO A 238      37.468  42.480  23.263  1.00  9.12           C  
-ANISOU 1513  CG  PRO A 238     1340    954   1172    102   -144   -367       C  
-ATOM   1514  CD  PRO A 238      36.278  41.586  23.033  1.00  8.46           C  
-ANISOU 1514  CD  PRO A 238     1172    929   1111     39   -143   -277       C  
-ATOM   1515  N   ASN A 239      38.887  41.433  19.157  1.00  7.49           N  
-ANISOU 1515  N   ASN A 239     1076    568   1200     79    -66    -14       N  
-ATOM   1516  CA  ASN A 239      40.049  40.850  18.509  1.00  7.61           C  
-ANISOU 1516  CA  ASN A 239     1046    694   1151     -1      0    -62       C  
-ATOM   1517  C   ASN A 239      40.062  39.329  18.476  1.00  6.87           C  
-ANISOU 1517  C   ASN A 239      959    598   1053     24     23   -102       C  
-ATOM   1518  O   ASN A 239      41.108  38.726  18.303  1.00  8.98           O  
-ANISOU 1518  O   ASN A 239     1025    768   1615     25     89   -190       O  
-ATOM   1519  CB  ASN A 239      41.345  41.421  19.100  1.00  8.89           C  
-ANISOU 1519  CB  ASN A 239     1198    797   1380    -42     43   -113       C  
-ATOM   1520  CG  ASN A 239      41.437  42.911  18.908  1.00 10.73           C  
-ANISOU 1520  CG  ASN A 239     1502   1006   1567   -249     35   -202       C  
-ATOM   1521  OD1 ASN A 239      41.565  43.687  19.874  1.00 13.13           O  
-ANISOU 1521  OD1 ASN A 239     1800   1159   2029   -227      9   -474       O  
-ATOM   1522  ND2 ASN A 239      41.310  43.338  17.670  1.00 11.23           N  
-ANISOU 1522  ND2 ASN A 239     2070    720   1475   -347    367   -280       N  
-ATOM   1523  N   LEU A 240      38.906  38.699  18.628  1.00  6.33           N  
-ANISOU 1523  N   LEU A 240      878    501   1025     71    -67    -31       N  
-ATOM   1524  CA  LEU A 240      38.835  37.260  18.480  1.00  5.88           C  
-ANISOU 1524  CA  LEU A 240      894    555    782    106    -62    -37       C  
-ATOM   1525  C   LEU A 240      38.710  36.909  17.002  1.00  5.94           C  
-ANISOU 1525  C   LEU A 240      834    607    816     81    -42     12       C  
-ATOM   1526  O   LEU A 240      37.755  37.330  16.346  1.00  7.43           O  
-ANISOU 1526  O   LEU A 240     1044    843    934    239   -156   -110       O  
-ATOM   1527  CB  LEU A 240      37.652  36.692  19.242  1.00  6.12           C  
-ANISOU 1527  CB  LEU A 240      888    658    776     79    -37    -25       C  
-ATOM   1528  CG  LEU A 240      37.560  35.165  19.238  1.00  5.58           C  
-ANISOU 1528  CG  LEU A 240      893    485    739     65    -74    -99       C  
-ATOM   1529  CD1 LEU A 240      38.779  34.527  19.900  1.00  7.37           C  
-ANISOU 1529  CD1 LEU A 240      975    768   1054     35    -72     86       C  
-ATOM   1530  CD2 LEU A 240      36.280  34.719  19.917  1.00  7.15           C  
-ANISOU 1530  CD2 LEU A 240      978    611   1127     72    -28     16       C  
-ATOM   1531  N   LEU A 241      39.662  36.148  16.486  1.00  5.53           N  
-ANISOU 1531  N   LEU A 241      794    592    713     40    -37     -8       N  
-ATOM   1532  CA  LEU A 241      39.554  35.557  15.170  1.00  5.67           C  
-ANISOU 1532  CA  LEU A 241      776    685    691     43     43     69       C  
-ATOM   1533  C   LEU A 241      38.723  34.293  15.250  1.00  5.18           C  
-ANISOU 1533  C   LEU A 241      765    637    565     51     55     37       C  
-ATOM   1534  O   LEU A 241      38.920  33.501  16.165  1.00  5.39           O  
-ANISOU 1534  O   LEU A 241      876    575    593     22    -19     57       O  
-ATOM   1535  CB  LEU A 241      40.940  35.203  14.693  1.00  6.87           C  
-ANISOU 1535  CB  LEU A 241      817    843    949    -35    -47     58       C  
-ATOM   1536  CG  LEU A 241      41.057  34.675  13.300  1.00 10.90           C  
-ANISOU 1536  CG  LEU A 241     1352   1389   1399     81     19    -47       C  
-ATOM   1537  CD1 LEU A 241      40.632  35.696  12.263  1.00 14.35           C  
-ANISOU 1537  CD1 LEU A 241     1824   1947   1680    193    133    -15       C  
-ATOM   1538  CD2 LEU A 241      42.495  34.257  13.101  1.00 12.47           C  
-ANISOU 1538  CD2 LEU A 241     1443   1703   1589     86     79    -49       C  
-ATOM   1539  N   TYR A 242      37.825  34.094  14.294  1.00  5.77           N  
-ANISOU 1539  N   TYR A 242      833    736    624    -54      3    156       N  
-ATOM   1540  CA  TYR A 242      36.907  32.968  14.366  1.00  6.27           C  
-ANISOU 1540  CA  TYR A 242      875    855    651    -64     19     66       C  
-ATOM   1541  C   TYR A 242      36.560  32.453  12.987  1.00  5.79           C  
-ANISOU 1541  C   TYR A 242      755    889    554   -101    -65    123       C  
-ATOM   1542  O   TYR A 242      36.647  33.158  11.996  1.00  7.52           O  
-ANISOU 1542  O   TYR A 242     1089   1151    615   -161    -42    175       O  
-ATOM   1543  CB  TYR A 242      35.637  33.338  15.167  1.00  6.48           C  
-ANISOU 1543  CB  TYR A 242      831    874    757    -97    -12     19       C  
-ATOM   1544  CG  TYR A 242      34.825  34.445  14.570  1.00  7.39           C  
-ANISOU 1544  CG  TYR A 242      867    980    960    -95    122     44       C  
-ATOM   1545  CD1 TYR A 242      33.820  34.167  13.660  1.00  8.98           C  
-ANISOU 1545  CD1 TYR A 242      890   1178   1343     68     10    183       C  
-ATOM   1546  CD2 TYR A 242      35.068  35.766  14.893  1.00  9.16           C  
-ANISOU 1546  CD2 TYR A 242     1147   1127   1206    103     98    153       C  
-ATOM   1547  CE1 TYR A 242      33.080  35.177  13.089  1.00 12.00           C  
-ANISOU 1547  CE1 TYR A 242     1141   1701   1715    208      8    337       C  
-ATOM   1548  CE2 TYR A 242      34.326  36.800  14.306  1.00 11.19           C  
-ANISOU 1548  CE2 TYR A 242     1409   1105   1737    206    165    246       C  
-ATOM   1549  CZ  TYR A 242      33.327  36.485  13.412  1.00 12.73           C  
-ANISOU 1549  CZ  TYR A 242     1420   1690   1726    253    172    427       C  
-ATOM   1550  OH  TYR A 242      32.567  37.453  12.822  1.00 18.33           O  
-ANISOU 1550  OH  TYR A 242     1953   2161   2850    326    117    589       O  
-ATOM   1551  N   ALA A 243      36.145  31.196  12.961  1.00  6.23           N  
-ANISOU 1551  N   ALA A 243      868    935    563    -65      4    -38       N  
-ATOM   1552  CA  ALA A 243      35.753  30.512  11.743  1.00  6.83           C  
-ANISOU 1552  CA  ALA A 243      816   1065    714     -4    -55   -110       C  
-ATOM   1553  C   ALA A 243      34.511  31.147  11.153  1.00  7.34           C  
-ANISOU 1553  C   ALA A 243      868   1194    724     50      0   -114       C  
-ATOM   1554  O   ALA A 243      33.491  31.279  11.815  1.00  9.92           O  
-ANISOU 1554  O   ALA A 243      910   1764   1094    134    -36    -38       O  
-ATOM   1555  CB  ALA A 243      35.491  29.061  12.046  1.00  7.72           C  
-ANISOU 1555  CB  ALA A 243     1067   1178    686    -20    -54   -169       C  
-ATOM   1556  N   ARG A 244      34.626  31.574   9.908  1.00  8.03           N  
-ANISOU 1556  N   ARG A 244      982   1259    807    139    -77    -72       N  
-ATOM   1557  CA  ARG A 244      33.524  32.200   9.191  1.00  9.21           C  
-ANISOU 1557  CA  ARG A 244     1221   1202   1073    147   -112   -109       C  
-ATOM   1558  C   ARG A 244      33.220  31.423   7.931  1.00  7.37           C  
-ANISOU 1558  C   ARG A 244     1040    962    796    100   -114   -100       C  
-ATOM   1559  O   ARG A 244      34.126  30.957   7.237  1.00  7.97           O  
-ANISOU 1559  O   ARG A 244     1006   1246    776    125   -103      0       O  
-ATOM   1560  CB  ARG A 244      33.879  33.637   8.815  1.00 11.88           C  
-ANISOU 1560  CB  ARG A 244     1580   1460   1473     92   -201   -150       C  
-ATOM   1561  CG  ARG A 244      33.823  34.612   9.968  1.00 15.64           C  
-ANISOU 1561  CG  ARG A 244     2068   1988   1886     81   -203    -51       C  
-ATOM   1562  CD  ARG A 244      33.913  36.059   9.546  1.00 21.76           C  
-ANISOU 1562  CD  ARG A 244     2843   2671   2751     19    -88    -57       C  
-ATOM   1563  NE  ARG A 244      32.599  36.600   9.181  1.00 26.84           N  
-ANISOU 1563  NE  ARG A 244     3401   3426   3370     31    -56     34       N  
-ATOM   1564  CZ  ARG A 244      32.152  36.823   7.941  1.00 30.18           C  
-ANISOU 1564  CZ  ARG A 244     3810   3873   3782     32     -8      2       C  
-ATOM   1565  NH1 ARG A 244      32.899  36.555   6.871  1.00 32.17           N  
-ANISOU 1565  NH1 ARG A 244     4076   4071   4074     30     25     33       N  
-ATOM   1566  NH2 ARG A 244      30.929  37.325   7.771  1.00 31.73           N  
-ANISOU 1566  NH2 ARG A 244     4015   4081   3959     58     31     -1       N  
-ATOM   1567  N   ALA A 245      31.945  31.334   7.605  1.00  7.44           N  
-ANISOU 1567  N   ALA A 245     1024    954    848    236    -44    -94       N  
-ATOM   1568  CA  ALA A 245      31.513  30.532   6.477  1.00  7.08           C  
-ANISOU 1568  CA  ALA A 245     1005    866    816    123    -14    -15       C  
-ATOM   1569  C   ALA A 245      32.079  31.037   5.154  1.00  6.63           C  
-ANISOU 1569  C   ALA A 245      995    769    755    181    -26     21       C  
-ATOM   1570  O   ALA A 245      31.967  32.224   4.830  1.00  8.36           O  
-ANISOU 1570  O   ALA A 245     1456    721    999    207      6     91       O  
-ATOM   1571  CB  ALA A 245      30.004  30.502   6.410  1.00  8.07           C  
-ANISOU 1571  CB  ALA A 245     1065   1088    910    104      3    -27       C  
-ATOM   1572  N   LEU A 246      32.673  30.116   4.412  1.00  6.45           N  
-ANISOU 1572  N   LEU A 246      960    726    761    121     26     68       N  
-ATOM   1573  CA  LEU A 246      33.148  30.319   3.054  1.00  7.16           C  
-ANISOU 1573  CA  LEU A 246     1024    901    795    -13      0     69       C  
-ATOM   1574  C   LEU A 246      32.042  30.063   2.046  1.00  7.96           C  
-ANISOU 1574  C   LEU A 246     1150   1057    815     90    -75    142       C  
-ATOM   1575  O   LEU A 246      32.049  30.613   0.943  1.00  9.70           O  
-ANISOU 1575  O   LEU A 246     1410   1422    850    -58   -185    307       O  
-ATOM   1576  CB  LEU A 246      34.289  29.351   2.786  1.00  7.36           C  
-ANISOU 1576  CB  LEU A 246     1010    971    815    -30     42     53       C  
-ATOM   1577  CG  LEU A 246      35.485  29.487   3.723  1.00  8.34           C  
-ANISOU 1577  CG  LEU A 246     1014   1177    978     -9    122     19       C  
-ATOM   1578  CD1 LEU A 246      36.319  28.224   3.681  1.00  8.16           C  
-ANISOU 1578  CD1 LEU A 246     1067   1245    787    126    -40     21       C  
-ATOM   1579  CD2 LEU A 246      36.327  30.698   3.371  1.00 11.23           C  
-ANISOU 1579  CD2 LEU A 246     1385   1369   1511    -42     73     21       C  
-ATOM   1580  N   VAL A 247      31.129  29.180   2.418  1.00  7.89           N  
-ANISOU 1580  N   VAL A 247     1071   1121    802     19   -156     58       N  
-ATOM   1581  CA  VAL A 247      29.928  28.863   1.674  1.00  8.60           C  
-ANISOU 1581  CA  VAL A 247     1142   1132    992     39   -112    -31       C  
-ATOM   1582  C   VAL A 247      28.893  28.400   2.690  1.00  7.60           C  
-ANISOU 1582  C   VAL A 247      970    984    932     75   -134     42       C  
-ATOM   1583  O   VAL A 247      29.244  27.873   3.760  1.00  7.67           O  
-ANISOU 1583  O   VAL A 247     1036    966    912     67   -213    120       O  
-ATOM   1584  CB  VAL A 247      30.189  27.794   0.559  1.00 10.09           C  
-ANISOU 1584  CB  VAL A 247     1262   1445   1123     23   -126   -172       C  
-ATOM   1585  CG1 VAL A 247      30.693  26.520   1.131  1.00 11.96           C  
-ANISOU 1585  CG1 VAL A 247     1617   1561   1366   -112    -61   -200       C  
-ATOM   1586  CG2 VAL A 247      28.960  27.559  -0.292  1.00 13.81           C  
-ANISOU 1586  CG2 VAL A 247     1727   1926   1594    102   -150   -262       C  
-ATOM   1587  N   ARG A 248      27.626  28.610   2.372  1.00  8.03           N  
-ANISOU 1587  N   ARG A 248     1012   1059    980    119   -119    161       N  
-ATOM   1588  CA  ARG A 248      26.515  28.215   3.215  1.00  8.45           C  
-ANISOU 1588  CA  ARG A 248     1042   1101   1066     84   -162     80       C  
-ATOM   1589  C   ARG A 248      25.436  27.690   2.296  1.00  8.57           C  
-ANISOU 1589  C   ARG A 248     1053   1139   1061     81   -186    121       C  
-ATOM   1590  O   ARG A 248      25.138  28.306   1.266  1.00 10.13           O  
-ANISOU 1590  O   ARG A 248     1320   1309   1218     37   -402    327       O  
-ATOM   1591  CB  ARG A 248      26.011  29.411   4.010  1.00  8.73           C  
-ANISOU 1591  CB  ARG A 248     1018   1145   1151     34   -159     67       C  
-ATOM   1592  CG  ARG A 248      24.874  29.107   4.946  1.00 10.20           C  
-ANISOU 1592  CG  ARG A 248     1251   1328   1294    178    -92    -58       C  
-ATOM   1593  CD  ARG A 248      24.629  30.221   5.889  1.00 12.56           C  
-ANISOU 1593  CD  ARG A 248     1517   1713   1540    -16     -9   -161       C  
-ATOM   1594  NE  ARG A 248      23.535  29.925   6.797  1.00 12.40           N  
-ANISOU 1594  NE  ARG A 248     1630   1566   1515     94    -76   -225       N  
-ATOM   1595  CZ  ARG A 248      23.450  30.417   8.019  1.00 12.07           C  
-ANISOU 1595  CZ  ARG A 248     1530   1641   1413    142   -111   -123       C  
-ATOM   1596  NH1 ARG A 248      24.393  31.211   8.491  1.00 14.93           N  
-ANISOU 1596  NH1 ARG A 248     1677   2242   1752    -57   -242    -75       N  
-ATOM   1597  NH2 ARG A 248      22.412  30.111   8.783  1.00 12.80           N  
-ANISOU 1597  NH2 ARG A 248     1444   1780   1637    160   -101   -117       N  
-ATOM   1598  N   GLY A 249      24.828  26.579   2.659  1.00  7.88           N  
-ANISOU 1598  N   GLY A 249      980   1038    977     71   -189     31       N  
-ATOM   1599  CA  GLY A 249      23.780  25.988   1.840  1.00  8.60           C  
-ANISOU 1599  CA  GLY A 249     1086   1113   1067     34   -142    -25       C  
-ATOM   1600  C   GLY A 249      23.474  24.582   2.289  1.00  8.01           C  
-ANISOU 1600  C   GLY A 249      988   1070    985     55   -110    -53       C  
-ATOM   1601  O   GLY A 249      23.702  24.219   3.439  1.00  8.57           O  
-ANISOU 1601  O   GLY A 249     1084   1180    992     -2   -130    -34       O  
-ATOM   1602  N   THR A 250      22.967  23.762   1.382  1.00  7.92           N  
-ANISOU 1602  N   THR A 250      904   1064   1040    113   -182    -55       N  
-ATOM   1603  CA  THR A 250      22.789  22.362   1.694  1.00  7.64           C  
-ANISOU 1603  CA  THR A 250      839   1072    991     85   -148    -86       C  
-ATOM   1604  C   THR A 250      24.148  21.692   1.883  1.00  7.54           C  
-ANISOU 1604  C   THR A 250      800   1013   1051     85   -114    -81       C  
-ATOM   1605  O   THR A 250      25.204  22.225   1.534  1.00  7.53           O  
-ANISOU 1605  O   THR A 250      842   1033    985     80   -125   -149       O  
-ATOM   1606  CB  THR A 250      22.056  21.631   0.575  1.00  8.61           C  
-ANISOU 1606  CB  THR A 250      928   1197   1144     56   -175    -92       C  
-ATOM   1607  OG1 THR A 250      22.873  21.700  -0.596  1.00 10.06           O  
-ANISOU 1607  OG1 THR A 250     1084   1560   1176     79   -216    -90       O  
-ATOM   1608  CG2 THR A 250      20.701  22.271   0.249  1.00  9.74           C  
-ANISOU 1608  CG2 THR A 250     1071   1507   1122     80   -162    -48       C  
-ATOM   1609  N   LEU A 251      24.112  20.488   2.417  1.00  7.42           N  
-ANISOU 1609  N   LEU A 251      852    954   1010     55    -52    -65       N  
-ATOM   1610  CA  LEU A 251      25.330  19.708   2.550  1.00  7.45           C  
-ANISOU 1610  CA  LEU A 251      875    971    981     58    -78    -87       C  
-ATOM   1611  C   LEU A 251      26.045  19.600   1.197  1.00  7.52           C  
-ANISOU 1611  C   LEU A 251      903    954    999      9   -114   -131       C  
-ATOM   1612  O   LEU A 251      27.254  19.795   1.101  1.00  7.88           O  
-ANISOU 1612  O   LEU A 251      891   1049   1054     53    -68   -100       O  
-ATOM   1613  CB  LEU A 251      25.009  18.337   3.126  1.00  7.61           C  
-ANISOU 1613  CB  LEU A 251      928    939   1021     60   -125   -107       C  
-ATOM   1614  CG  LEU A 251      26.156  17.332   3.149  1.00  8.20           C  
-ANISOU 1614  CG  LEU A 251      896   1067   1149     61    -15   -134       C  
-ATOM   1615  CD1 LEU A 251      27.254  17.823   4.081  1.00  9.40           C  
-ANISOU 1615  CD1 LEU A 251     1059   1254   1256    172   -194   -145       C  
-ATOM   1616  CD2 LEU A 251      25.619  15.984   3.574  1.00 10.52           C  
-ANISOU 1616  CD2 LEU A 251     1122   1318   1556    199     96      0       C  
-ATOM   1617  N   ASP A 252      25.303  19.276   0.140  1.00  8.47           N  
-ANISOU 1617  N   ASP A 252      970   1202   1044    -41    -84   -167       N  
-ATOM   1618  CA  ASP A 252      25.914  19.128  -1.173  1.00  9.10           C  
-ANISOU 1618  CA  ASP A 252     1111   1233   1110     12    -85   -146       C  
-ATOM   1619  C   ASP A 252      26.521  20.425  -1.697  1.00  9.20           C  
-ANISOU 1619  C   ASP A 252     1129   1330   1035     55    -37   -175       C  
-ATOM   1620  O   ASP A 252      27.577  20.395  -2.307  1.00  9.74           O  
-ANISOU 1620  O   ASP A 252     1146   1358   1197     -9     -3   -193       O  
-ATOM   1621  CB  ASP A 252      24.906  18.548  -2.167  1.00 10.30           C  
-ANISOU 1621  CB  ASP A 252     1241   1454   1218    -86    -82   -195       C  
-ATOM   1622  CG  ASP A 252      24.785  17.048  -2.057  1.00 11.69           C  
-ANISOU 1622  CG  ASP A 252     1270   1614   1554   -119   -258   -228       C  
-ATOM   1623  OD1 ASP A 252      25.827  16.360  -1.967  1.00 15.13           O  
-ANISOU 1623  OD1 ASP A 252     1863   1765   2119   -276   -291   -357       O  
-ATOM   1624  OD2 ASP A 252      23.678  16.478  -2.067  1.00 16.09           O  
-ANISOU 1624  OD2 ASP A 252     1735   2014   2363   -329   -178   -403       O  
-ATOM   1625  N   GLU A 253      25.881  21.559  -1.434  1.00  8.69           N  
-ANISOU 1625  N   GLU A 253     1082   1231    986     79    -71    -84       N  
-ATOM   1626  CA  GLU A 253      26.433  22.836  -1.854  1.00  9.60           C  
-ANISOU 1626  CA  GLU A 253     1207   1349   1090     92    -30    -25       C  
-ATOM   1627  C   GLU A 253      27.767  23.097  -1.147  1.00  8.93           C  
-ANISOU 1627  C   GLU A 253     1173   1206   1014     40    -21    -37       C  
-ATOM   1628  O   GLU A 253      28.715  23.593  -1.758  1.00 10.39           O  
-ANISOU 1628  O   GLU A 253     1284   1537   1127     -5    -11     39       O  
-ATOM   1629  CB  GLU A 253      25.425  23.960  -1.627  1.00  9.69           C  
-ANISOU 1629  CB  GLU A 253     1304   1295   1083    118    -75     65       C  
-ATOM   1630  CG  GLU A 253      24.331  23.948  -2.685  1.00 11.84           C  
-ANISOU 1630  CG  GLU A 253     1438   1721   1338    256   -191     48       C  
-ATOM   1631  CD  GLU A 253      23.134  24.814  -2.371  1.00 13.84           C  
-ANISOU 1631  CD  GLU A 253     1830   2115   1313    440   -342    140       C  
-ATOM   1632  OE1 GLU A 253      22.884  25.175  -1.210  1.00 13.34           O  
-ANISOU 1632  OE1 GLU A 253     1783   2052   1234    607   -423    -29       O  
-ATOM   1633  OE2 GLU A 253      22.407  25.124  -3.328  1.00 19.92           O  
-ANISOU 1633  OE2 GLU A 253     2554   3162   1852    733   -597    100       O  
-ATOM   1634  N   CYS A 254      27.852  22.762   0.136  1.00  7.64           N  
-ANISOU 1634  N   CYS A 254     1012    984    905     79      1    -65       N  
-ATOM   1635  CA  CYS A 254      29.111  22.939   0.864  1.00  7.21           C  
-ANISOU 1635  CA  CYS A 254      909    859    971     37    -10    -91       C  
-ATOM   1636  C   CYS A 254      30.188  21.962   0.385  1.00  7.28           C  
-ANISOU 1636  C   CYS A 254      933    833   1000     47     -8   -179       C  
-ATOM   1637  O   CYS A 254      31.354  22.322   0.265  1.00  7.83           O  
-ANISOU 1637  O   CYS A 254      901    986   1088    -11      0   -243       O  
-ATOM   1638  CB  CYS A 254      28.871  22.790   2.351  1.00  7.70           C  
-ANISOU 1638  CB  CYS A 254      834    982   1110     22    -17    -93       C  
-ATOM   1639  SG  CYS A 254      27.923  24.157   3.070  1.00  7.64           S  
-ANISOU 1639  SG  CYS A 254      996    929    978     35     31   -160       S  
-ATOM   1640  N   LEU A 255      29.793  20.722   0.112  1.00  7.92           N  
-ANISOU 1640  N   LEU A 255      919    879   1211     79     23   -234       N  
-ATOM   1641  CA  LEU A 255      30.706  19.693  -0.386  1.00  8.45           C  
-ANISOU 1641  CA  LEU A 255      997    999   1214     53     26   -231       C  
-ATOM   1642  C   LEU A 255      31.281  20.029  -1.745  1.00  9.28           C  
-ANISOU 1642  C   LEU A 255     1111   1095   1319     38     61   -252       C  
-ATOM   1643  O   LEU A 255      32.314  19.480  -2.101  1.00 11.10           O  
-ANISOU 1643  O   LEU A 255     1134   1461   1619     75    197   -312       O  
-ATOM   1644  CB  LEU A 255      30.007  18.335  -0.438  1.00  8.64           C  
-ANISOU 1644  CB  LEU A 255     1037    943   1302     63     28   -285       C  
-ATOM   1645  CG  LEU A 255      29.841  17.656   0.910  1.00  9.49           C  
-ANISOU 1645  CG  LEU A 255     1165    940   1498     78     29   -242       C  
-ATOM   1646  CD1 LEU A 255      28.872  16.499   0.750  1.00 10.27           C  
-ANISOU 1646  CD1 LEU A 255     1119   1110   1672    151    131   -232       C  
-ATOM   1647  CD2 LEU A 255      31.168  17.175   1.465  1.00 11.05           C  
-ANISOU 1647  CD2 LEU A 255     1315   1062   1820    -31   -152    -65       C  
-ATOM   1648  N   ALA A 256      30.640  20.922  -2.490  1.00  9.20           N  
-ANISOU 1648  N   ALA A 256     1123   1256   1114     19     89   -258       N  
-ATOM   1649  CA  ALA A 256      31.129  21.362  -3.791  1.00 10.32           C  
-ANISOU 1649  CA  ALA A 256     1265   1444   1210    -50     33   -182       C  
-ATOM   1650  C   ALA A 256      32.193  22.439  -3.700  1.00 10.63           C  
-ANISOU 1650  C   ALA A 256     1286   1567   1185    -94     21   -169       C  
-ATOM   1651  O   ALA A 256      32.742  22.840  -4.719  1.00 12.02           O  
-ANISOU 1651  O   ALA A 256     1438   1939   1191   -245     83   -281       O  
-ATOM   1652  CB  ALA A 256      29.980  21.859  -4.637  1.00 11.40           C  
-ANISOU 1652  CB  ALA A 256     1451   1589   1291    -34     32   -172       C  
-ATOM   1653  N   PHE A 257      32.524  22.896  -2.499  1.00 10.37           N  
-ANISOU 1653  N   PHE A 257     1252   1490   1198   -144      0   -176       N  
-ATOM   1654  CA  PHE A 257      33.544  23.909  -2.344  1.00 10.14           C  
-ANISOU 1654  CA  PHE A 257     1268   1383   1202    -98      1   -156       C  
-ATOM   1655  C   PHE A 257      34.861  23.436  -2.951  1.00 10.83           C  
-ANISOU 1655  C   PHE A 257     1376   1458   1280   -137    -15   -162       C  
-ATOM   1656  O   PHE A 257      35.276  22.305  -2.742  1.00 12.45           O  
-ANISOU 1656  O   PHE A 257     1594   1558   1575   -181    125   -254       O  
-ATOM   1657  CB  PHE A 257      33.740  24.227  -0.868  1.00 10.13           C  
-ANISOU 1657  CB  PHE A 257     1280   1413   1155    -34    -31   -175       C  
-ATOM   1658  CG  PHE A 257      34.707  25.338  -0.625  1.00  9.98           C  
-ANISOU 1658  CG  PHE A 257     1358   1395   1036   -174     39   -160       C  
-ATOM   1659  CD1 PHE A 257      34.322  26.652  -0.808  1.00 12.51           C  
-ANISOU 1659  CD1 PHE A 257     1625   1598   1527   -153     59   -147       C  
-ATOM   1660  CD2 PHE A 257      36.007  25.075  -0.245  1.00 10.29           C  
-ANISOU 1660  CD2 PHE A 257     1430   1546    932   -129      9     63       C  
-ATOM   1661  CE1 PHE A 257      35.213  27.684  -0.604  1.00 12.81           C  
-ANISOU 1661  CE1 PHE A 257     1834   1550   1480   -252     89   -207       C  
-ATOM   1662  CE2 PHE A 257      36.908  26.105  -0.047  1.00 11.11           C  
-ANISOU 1662  CE2 PHE A 257     1541   1860    820   -185     72   -136       C  
-ATOM   1663  CZ  PHE A 257      36.514  27.402  -0.225  1.00 11.91           C  
-ANISOU 1663  CZ  PHE A 257     1665   1655   1204   -356     94   -273       C  
-ATOM   1664  N   ASP A 258      35.528  24.336  -3.658  1.00 11.44           N  
-ANISOU 1664  N   ASP A 258     1443   1633   1268   -173     69   -155       N  
-ATOM   1665  CA  ASP A 258      36.758  24.032  -4.383  1.00 12.78           C  
-ANISOU 1665  CA  ASP A 258     1607   1829   1421   -120     72    -70       C  
-ATOM   1666  C   ASP A 258      37.981  24.047  -3.453  1.00 12.12           C  
-ANISOU 1666  C   ASP A 258     1539   1748   1317   -175     52   -115       C  
-ATOM   1667  O   ASP A 258      38.750  25.011  -3.450  1.00 12.95           O  
-ANISOU 1667  O   ASP A 258     1629   1777   1513   -305   -107     80       O  
-ATOM   1668  CB  ASP A 258      36.924  25.048  -5.532  1.00 13.85           C  
-ANISOU 1668  CB  ASP A 258     1696   2126   1440    -85     97    -45       C  
-ATOM   1669  CG  ASP A 258      38.161  24.804  -6.379  1.00 17.35           C  
-ANISOU 1669  CG  ASP A 258     2103   2631   1855    -18    316    103       C  
-ATOM   1670  OD1 ASP A 258      38.827  23.768  -6.182  1.00 20.95           O  
-ANISOU 1670  OD1 ASP A 258     2382   3389   2190    390    871   -143       O  
-ATOM   1671  OD2 ASP A 258      38.524  25.603  -7.274  1.00 22.02           O  
-ANISOU 1671  OD2 ASP A 258     2564   3638   2162     32    500    247       O  
-ATOM   1672  N   VAL A 259      38.204  22.962  -2.717  1.00 11.97           N  
-ANISOU 1672  N   VAL A 259     1645   1579   1323   -173    130   -199       N  
-ATOM   1673  CA  VAL A 259      39.350  22.899  -1.796  1.00 12.53           C  
-ANISOU 1673  CA  VAL A 259     1838   1551   1370    -74     67   -154       C  
-ATOM   1674  C   VAL A 259      40.679  22.812  -2.502  1.00 11.56           C  
-ANISOU 1674  C   VAL A 259     1758   1505   1128    -86     -7   -256       C  
-ATOM   1675  O   VAL A 259      41.689  23.263  -1.967  1.00 12.04           O  
-ANISOU 1675  O   VAL A 259     1896   1637   1042   -123    -88   -324       O  
-ATOM   1676  CB  VAL A 259      39.329  21.707  -0.794  1.00 13.90           C  
-ANISOU 1676  CB  VAL A 259     2122   1569   1588    -45    180   -182       C  
-ATOM   1677  CG1 VAL A 259      38.391  21.969   0.354  1.00 15.60           C  
-ANISOU 1677  CG1 VAL A 259     2280   1861   1783    -87    118    -91       C  
-ATOM   1678  CG2 VAL A 259      39.043  20.365  -1.501  1.00 13.99           C  
-ANISOU 1678  CG2 VAL A 259     2242   1436   1636    -25    211   -140       C  
-ATOM   1679  N   GLU A 260      40.696  22.234  -3.701  1.00 11.67           N  
-ANISOU 1679  N   GLU A 260     1721   1561   1151   -126    -55   -297       N  
-ATOM   1680  CA  GLU A 260      41.948  22.057  -4.407  1.00 12.24           C  
-ANISOU 1680  CA  GLU A 260     1701   1660   1289    -42    -13   -309       C  
-ATOM   1681  C   GLU A 260      42.641  23.359  -4.725  1.00 12.16           C  
-ANISOU 1681  C   GLU A 260     1659   1744   1214   -111     -3   -369       C  
-ATOM   1682  O   GLU A 260      43.868  23.377  -4.798  1.00 14.65           O  
-ANISOU 1682  O   GLU A 260     1819   2098   1647    -99     32   -524       O  
-ATOM   1683  CB  GLU A 260      41.725  21.268  -5.692  1.00 12.78           C  
-ANISOU 1683  CB  GLU A 260     1743   1778   1334    -73     -4   -327       C  
-ATOM   1684  CG  GLU A 260      41.405  19.815  -5.443  1.00 14.52           C  
-ANISOU 1684  CG  GLU A 260     2004   2016   1495     73    -26   -420       C  
-ATOM   1685  CD  GLU A 260      42.546  19.114  -4.750  1.00 18.53           C  
-ANISOU 1685  CD  GLU A 260     2630   2213   2195    318    203   -385       C  
-ATOM   1686  OE1 GLU A 260      43.674  19.108  -5.296  1.00 21.82           O  
-ANISOU 1686  OE1 GLU A 260     2769   3051   2472    364    109   -214       O  
-ATOM   1687  OE2 GLU A 260      42.319  18.578  -3.667  1.00 20.59           O  
-ANISOU 1687  OE2 GLU A 260     3161   2545   2116    628     47   -683       O  
-ATOM   1688  N   ASN A 261      41.874  24.429  -4.914  1.00 11.57           N  
-ANISOU 1688  N   ASN A 261     1674   1723    997   -129     23   -291       N  
-ATOM   1689  CA  ASN A 261      42.413  25.739  -5.259  1.00 12.22           C  
-ANISOU 1689  CA  ASN A 261     1820   1753   1070   -136     49   -160       C  
-ATOM   1690  C   ASN A 261      42.213  26.799  -4.187  1.00 11.42           C  
-ANISOU 1690  C   ASN A 261     1768   1647    922   -176     40   -129       C  
-ATOM   1691  O   ASN A 261      42.382  27.980  -4.433  1.00 13.10           O  
-ANISOU 1691  O   ASN A 261     2321   1814    840   -244    133      6       O  
-ATOM   1692  CB  ASN A 261      41.770  26.235  -6.547  1.00 12.89           C  
-ANISOU 1692  CB  ASN A 261     1898   1914   1085   -131     84   -148       C  
-ATOM   1693  CG  ASN A 261      42.117  25.381  -7.712  1.00 15.89           C  
-ANISOU 1693  CG  ASN A 261     2156   2491   1389   -263    237   -418       C  
-ATOM   1694  OD1 ASN A 261      43.287  25.262  -8.065  1.00 17.97           O  
-ANISOU 1694  OD1 ASN A 261     2192   3411   1224   -420    198   -697       O  
-ATOM   1695  ND2 ASN A 261      41.118  24.742  -8.291  1.00 18.57           N  
-ANISOU 1695  ND2 ASN A 261     2494   3158   1402   -390    365   -844       N  
-ATOM   1696  N   PHE A 262      41.856  26.378  -2.986  1.00  9.73           N  
-ANISOU 1696  N   PHE A 262     1477   1410    808   -193     39     14       N  
-ATOM   1697  CA  PHE A 262      41.526  27.295  -1.909  1.00  8.47           C  
-ANISOU 1697  CA  PHE A 262     1249   1206    761    -92     -8     17       C  
-ATOM   1698  C   PHE A 262      42.820  27.756  -1.244  1.00  8.66           C  
-ANISOU 1698  C   PHE A 262     1251   1194    844   -107      0     62       C  
-ATOM   1699  O   PHE A 262      43.475  27.009  -0.504  1.00  9.02           O  
-ANISOU 1699  O   PHE A 262     1296   1297    832   -140    -38     72       O  
-ATOM   1700  CB  PHE A 262      40.623  26.577  -0.912  1.00  8.66           C  
-ANISOU 1700  CB  PHE A 262     1248   1160    879   -181      3    100       C  
-ATOM   1701  CG  PHE A 262      40.302  27.344   0.350  1.00  7.88           C  
-ANISOU 1701  CG  PHE A 262     1102   1028    864   -144     -7     34       C  
-ATOM   1702  CD1 PHE A 262      40.049  28.702   0.346  1.00  8.72           C  
-ANISOU 1702  CD1 PHE A 262     1250   1171    891   -173   -147     76       C  
-ATOM   1703  CD2 PHE A 262      40.215  26.663   1.545  1.00  7.66           C  
-ANISOU 1703  CD2 PHE A 262      936   1163    811   -179    -54    -15       C  
-ATOM   1704  CE1 PHE A 262      39.750  29.365   1.521  1.00  8.47           C  
-ANISOU 1704  CE1 PHE A 262     1027   1049   1139    -75    -29    -13       C  
-ATOM   1705  CE2 PHE A 262      39.907  27.317   2.718  1.00  8.62           C  
-ANISOU 1705  CE2 PHE A 262      987   1398    887   -126     20    -33       C  
-ATOM   1706  CZ  PHE A 262      39.678  28.680   2.701  1.00  8.68           C  
-ANISOU 1706  CZ  PHE A 262      959   1373    964   -156     78   -101       C  
-HETATM 1707  N   MSE A 263      43.203  28.997  -1.535  1.00  8.52           N  
-ANISOU 1707  N   MSE A 263     1279   1164    794   -104    -23     73       N  
-HETATM 1708  CA  MSE A 263      44.358  29.641  -0.914  1.00  8.76           C  
-ANISOU 1708  CA  MSE A 263     1223   1158    946   -112     29     43       C  
-HETATM 1709  C   MSE A 263      43.950  30.157   0.452  1.00  8.16           C  
-ANISOU 1709  C   MSE A 263     1170   1053    876   -103     10     44       C  
-HETATM 1710  O   MSE A 263      42.915  30.779   0.575  1.00  9.70           O  
-ANISOU 1710  O   MSE A 263     1259   1425   1000      1   -117     31       O  
-HETATM 1711  CB  MSE A 263      44.829  30.801  -1.787  1.00  9.69           C  
-ANISOU 1711  CB  MSE A 263     1313   1313   1054   -177     47     87       C  
-HETATM 1712  CG  MSE A 263      45.232  30.387  -3.190  1.00 12.20           C  
-ANISOU 1712  CG  MSE A 263     1691   1618   1324    -86    113     87       C  
-HETATM 1713 SE   MSE A 263      46.854  29.332  -3.232  1.00 21.92          SE  
-ANISOU 1713 SE   MSE A 263     3432   2715   2180   -234    613     63      SE  
-HETATM 1714  CE  MSE A 263      48.106  30.765  -2.917  1.00 17.85           C  
-ANISOU 1714  CE  MSE A 263     2469   2182   2130   -116     90    -14       C  
-ATOM   1715  N   THR A 264      44.754  29.951   1.483  1.00  7.18           N  
-ANISOU 1715  N   THR A 264     1007    909    808   -143    -21     48       N  
-ATOM   1716  CA  THR A 264      44.310  30.426   2.790  1.00  6.91           C  
-ANISOU 1716  CA  THR A 264      949    825    848   -132     27     24       C  
-ATOM   1717  C   THR A 264      44.162  31.945   2.755  1.00  6.96           C  
-ANISOU 1717  C   THR A 264      948    847    849   -116    -23     73       C  
-ATOM   1718  O   THR A 264      45.069  32.661   2.305  1.00  6.77           O  
-ANISOU 1718  O   THR A 264      920    769    881    -89     59    124       O  
-ATOM   1719  CB  THR A 264      45.199  30.004   3.962  1.00  6.73           C  
-ANISOU 1719  CB  THR A 264      992    752    813   -110     51     39       C  
-ATOM   1720  OG1 THR A 264      44.766  30.725   5.125  1.00  6.50           O  
-ANISOU 1720  OG1 THR A 264      953    872    644   -137     99     79       O  
-ATOM   1721  CG2 THR A 264      46.672  30.316   3.748  1.00  7.14           C  
-ANISOU 1721  CG2 THR A 264     1165    726    822     25      1     86       C  
-ATOM   1722  N   PRO A 265      43.010  32.460   3.210  1.00  7.37           N  
-ANISOU 1722  N   PRO A 265      917    929    953    -85     60    104       N  
-ATOM   1723  CA  PRO A 265      42.792  33.905   3.288  1.00  7.59           C  
-ANISOU 1723  CA  PRO A 265      927    987    967     -9    -11     86       C  
-ATOM   1724  C   PRO A 265      43.399  34.540   4.522  1.00  6.57           C  
-ANISOU 1724  C   PRO A 265      784    807    902     -2     48    167       C  
-ATOM   1725  O   PRO A 265      43.348  35.776   4.644  1.00  7.40           O  
-ANISOU 1725  O   PRO A 265     1021    787   1002     41    -17    157       O  
-ATOM   1726  CB  PRO A 265      41.271  34.014   3.362  1.00  8.08           C  
-ANISOU 1726  CB  PRO A 265      946   1083   1038    -19    -56     45       C  
-ATOM   1727  CG  PRO A 265      40.877  32.807   4.102  1.00  9.35           C  
-ANISOU 1727  CG  PRO A 265      930   1300   1321    -92     54    126       C  
-ATOM   1728  CD  PRO A 265      41.797  31.718   3.608  1.00  7.90           C  
-ANISOU 1728  CD  PRO A 265     1001    968   1029   -133     60    144       C  
-ATOM   1729  N   LEU A 266      43.947  33.752   5.439  1.00  5.91           N  
-ANISOU 1729  N   LEU A 266      806    670    769    -23    103    151       N  
-ATOM   1730  CA  LEU A 266      44.418  34.304   6.694  1.00  5.83           C  
-ANISOU 1730  CA  LEU A 266      774    653    786     18     97    115       C  
-ATOM   1731  C   LEU A 266      45.612  35.245   6.553  1.00  5.87           C  
-ANISOU 1731  C   LEU A 266      787    633    808     34    106    120       C  
-ATOM   1732  O   LEU A 266      45.612  36.270   7.213  1.00  6.39           O  
-ANISOU 1732  O   LEU A 266      945    664    818     40    101     27       O  
-ATOM   1733  CB  LEU A 266      44.657  33.201   7.723  1.00  6.28           C  
-ANISOU 1733  CB  LEU A 266      828    674    881   -103    106    189       C  
-ATOM   1734  CG  LEU A 266      43.361  32.643   8.324  1.00  7.17           C  
-ANISOU 1734  CG  LEU A 266      966    807    948     18    156    138       C  
-ATOM   1735  CD1 LEU A 266      43.595  31.367   9.083  1.00  8.53           C  
-ANISOU 1735  CD1 LEU A 266     1123    961   1156    -95    246    200       C  
-ATOM   1736  CD2 LEU A 266      42.802  33.658   9.297  1.00 10.46           C  
-ANISOU 1736  CD2 LEU A 266     1483   1143   1347     60    534    171       C  
-ATOM   1737  N   PRO A 267      46.626  34.954   5.736  1.00  5.91           N  
-ANISOU 1737  N   PRO A 267      776    651    818      4    122    111       N  
-ATOM   1738  CA  PRO A 267      47.726  35.925   5.597  1.00  5.93           C  
-ANISOU 1738  CA  PRO A 267      759    622    872     28     82    103       C  
-ATOM   1739  C   PRO A 267      47.230  37.330   5.280  1.00  6.09           C  
-ANISOU 1739  C   PRO A 267      759    647    908     -2    165     94       C  
-ATOM   1740  O   PRO A 267      47.655  38.291   5.911  1.00  6.71           O  
-ANISOU 1740  O   PRO A 267      795    736   1017     -9    161     59       O  
-ATOM   1741  CB  PRO A 267      48.579  35.342   4.465  1.00  6.05           C  
-ANISOU 1741  CB  PRO A 267      738    661    898     23     74    137       C  
-ATOM   1742  CG  PRO A 267      48.381  33.868   4.607  1.00  5.95           C  
-ANISOU 1742  CG  PRO A 267      850    671    738     63    169     93       C  
-ATOM   1743  CD  PRO A 267      46.923  33.707   5.008  1.00  6.39           C  
-ANISOU 1743  CD  PRO A 267      864    790    772    -12     68    140       C  
-ATOM   1744  N   ALA A 268      46.313  37.467   4.336  1.00  6.50           N  
-ANISOU 1744  N   ALA A 268      801    653   1014     -4     73    164       N  
-ATOM   1745  CA  ALA A 268      45.830  38.794   3.975  1.00  7.31           C  
-ANISOU 1745  CA  ALA A 268      998    754   1023     27     75    171       C  
-ATOM   1746  C   ALA A 268      45.059  39.426   5.135  1.00  7.77           C  
-ANISOU 1746  C   ALA A 268      992    773   1183     66    120    202       C  
-ATOM   1747  O   ALA A 268      45.175  40.622   5.400  1.00  9.40           O  
-ANISOU 1747  O   ALA A 268     1354    780   1438     95    332    143       O  
-ATOM   1748  CB  ALA A 268      44.990  38.739   2.733  1.00  8.84           C  
-ANISOU 1748  CB  ALA A 268     1176    989   1191     38     59    208       C  
-ATOM   1749  N   LEU A 269      44.290  38.632   5.858  1.00  7.70           N  
-ANISOU 1749  N   LEU A 269      970    800   1156    120    195    131       N  
-ATOM   1750  CA  LEU A 269      43.571  39.131   7.021  1.00  8.78           C  
-ANISOU 1750  CA  LEU A 269     1078    959   1299    152    181     68       C  
-ATOM   1751  C   LEU A 269      44.513  39.592   8.129  1.00  8.67           C  
-ANISOU 1751  C   LEU A 269     1061    951   1280     99    223     17       C  
-ATOM   1752  O   LEU A 269      44.162  40.465   8.927  1.00 11.70           O  
-ANISOU 1752  O   LEU A 269     1371   1347   1726    327    232   -242       O  
-ATOM   1753  CB  LEU A 269      42.623  38.051   7.538  1.00  9.17           C  
-ANISOU 1753  CB  LEU A 269     1121   1124   1237     93    282     69       C  
-ATOM   1754  CG  LEU A 269      41.425  37.770   6.620  1.00 14.21           C  
-ANISOU 1754  CG  LEU A 269     1698   1784   1915     62    154     80       C  
-ATOM   1755  CD1 LEU A 269      40.796  36.430   6.947  1.00 17.01           C  
-ANISOU 1755  CD1 LEU A 269     1991   2239   2232    -35     98     17       C  
-ATOM   1756  CD2 LEU A 269      40.384  38.891   6.696  1.00 16.85           C  
-ANISOU 1756  CD2 LEU A 269     1920   2137   2342    118     56     70       C  
-ATOM   1757  N   LEU A 270      45.702  39.009   8.182  1.00  8.04           N  
-ANISOU 1757  N   LEU A 270     1111    912   1033    147    163     60       N  
-ATOM   1758  CA  LEU A 270      46.694  39.279   9.211  1.00  8.18           C  
-ANISOU 1758  CA  LEU A 270     1119    906   1082     15    115     72       C  
-ATOM   1759  C   LEU A 270      47.805  40.198   8.699  1.00  7.68           C  
-ANISOU 1759  C   LEU A 270     1080    831   1006     86     86     80       C  
-ATOM   1760  O   LEU A 270      48.890  40.216   9.257  1.00  9.64           O  
-ANISOU 1760  O   LEU A 270     1347    998   1315   -116    -43    151       O  
-ATOM   1761  CB  LEU A 270      47.243  37.949   9.719  1.00  7.97           C  
-ANISOU 1761  CB  LEU A 270     1086    936   1005      7     80     75       C  
-ATOM   1762  CG  LEU A 270      46.165  37.027  10.311  1.00  8.11           C  
-ANISOU 1762  CG  LEU A 270     1061   1051    969    -14    114    211       C  
-ATOM   1763  CD1 LEU A 270      46.769  35.669  10.658  1.00  8.46           C  
-ANISOU 1763  CD1 LEU A 270     1058   1120   1037   -174   -133    236       C  
-ATOM   1764  CD2 LEU A 270      45.498  37.651  11.532  1.00 10.32           C  
-ANISOU 1764  CD2 LEU A 270     1363   1439   1119      2    244     78       C  
-ATOM   1765  N   GLY A 271      47.510  40.991   7.669  1.00  8.18           N  
-ANISOU 1765  N   GLY A 271     1183    904   1021     88     84     76       N  
-ATOM   1766  CA  GLY A 271      48.389  42.078   7.271  1.00  8.56           C  
-ANISOU 1766  CA  GLY A 271     1258    856   1136    -26     93     81       C  
-ATOM   1767  C   GLY A 271      49.392  41.770   6.183  1.00  7.69           C  
-ANISOU 1767  C   GLY A 271     1165    723   1031    -73     82    144       C  
-ATOM   1768  O   GLY A 271      50.221  42.624   5.871  1.00  9.09           O  
-ANISOU 1768  O   GLY A 271     1454    771   1225   -268    201    109       O  
-ATOM   1769  N   LEU A 272      49.310  40.586   5.585  1.00  6.80           N  
-ANISOU 1769  N   LEU A 272      999    714    870    -50     63    154       N  
-ATOM   1770  CA  LEU A 272      50.345  40.113   4.687  1.00  6.41           C  
-ANISOU 1770  CA  LEU A 272      876    673    886    -53     92    155       C  
-ATOM   1771  C   LEU A 272      49.899  40.009   3.248  1.00  6.37           C  
-ANISOU 1771  C   LEU A 272      852    696    871    -55    108    229       C  
-ATOM   1772  O   LEU A 272      50.517  39.307   2.463  1.00  6.70           O  
-ANISOU 1772  O   LEU A 272     1082    658    806    -37    151    298       O  
-ATOM   1773  CB  LEU A 272      50.892  38.781   5.181  1.00  6.24           C  
-ANISOU 1773  CB  LEU A 272      797    668    904    -27     61    214       C  
-ATOM   1774  CG  LEU A 272      51.331  38.756   6.636  1.00  6.83           C  
-ANISOU 1774  CG  LEU A 272      965    794    836     54     27    264       C  
-ATOM   1775  CD1 LEU A 272      51.709  37.345   7.022  1.00  8.25           C  
-ANISOU 1775  CD1 LEU A 272     1128   1050    953     78   -103    221       C  
-ATOM   1776  CD2 LEU A 272      52.459  39.716   6.927  1.00  8.47           C  
-ANISOU 1776  CD2 LEU A 272     1120   1049   1050    -14    -57    173       C  
-ATOM   1777  N   GLY A 273      48.874  40.756   2.872  1.00  7.25           N  
-ANISOU 1777  N   GLY A 273      960    876    917    -19     75    253       N  
-ATOM   1778  CA  GLY A 273      48.369  40.714   1.508  1.00  8.03           C  
-ANISOU 1778  CA  GLY A 273      955   1100    996    -71    112    187       C  
-ATOM   1779  C   GLY A 273      49.389  41.082   0.439  1.00  7.52           C  
-ANISOU 1779  C   GLY A 273      880   1030    944    -71     62    247       C  
-ATOM   1780  O   GLY A 273      49.311  40.593  -0.678  1.00  8.90           O  
-ANISOU 1780  O   GLY A 273     1077   1319    983   -304    -42    280       O  
-ATOM   1781  N   ASN A 274      50.370  41.913   0.763  1.00  6.68           N  
-ANISOU 1781  N   ASN A 274      871    807    858    -25     60    330       N  
-ATOM   1782  CA  ASN A 274      51.383  42.282  -0.214  1.00  6.38           C  
-ANISOU 1782  CA  ASN A 274      882    715    826    -13     69    291       C  
-ATOM   1783  C   ASN A 274      52.530  41.290  -0.329  1.00  6.49           C  
-ANISOU 1783  C   ASN A 274      903    770    790    -34     51    334       C  
-ATOM   1784  O   ASN A 274      53.406  41.491  -1.159  1.00  7.21           O  
-ANISOU 1784  O   ASN A 274      959    790    989     70    199    484       O  
-ATOM   1785  CB  ASN A 274      51.951  43.678   0.087  1.00  7.01           C  
-ANISOU 1785  CB  ASN A 274      920    817    926      4     20    321       C  
-ATOM   1786  CG  ASN A 274      51.003  44.792  -0.247  1.00  7.28           C  
-ANISOU 1786  CG  ASN A 274     1064    720    980    136    231    257       C  
-ATOM   1787  OD1 ASN A 274      50.859  45.761   0.518  1.00 10.65           O  
-ANISOU 1787  OD1 ASN A 274     1612   1077   1359    172    241    277       O  
-ATOM   1788  ND2 ASN A 274      50.366  44.679  -1.370  1.00  6.71           N  
-ANISOU 1788  ND2 ASN A 274     1030    732    784    323    151    454       N  
-ATOM   1789  N   TYR A 275      52.517  40.230   0.484  1.00  6.57           N  
-ANISOU 1789  N   TYR A 275      873    763    858      6     99    314       N  
-ATOM   1790  CA  TYR A 275      53.658  39.312   0.603  1.00  6.85           C  
-ANISOU 1790  CA  TYR A 275      876    810    915    -10     59    235       C  
-ATOM   1791  C   TYR A 275      53.219  37.871   0.374  1.00  7.10           C  
-ANISOU 1791  C   TYR A 275      962    809    925      6     19    286       C  
-ATOM   1792  O   TYR A 275      53.327  37.019   1.241  1.00  7.10           O  
-ANISOU 1792  O   TYR A 275      911    759   1026    -27    103    498       O  
-ATOM   1793  CB  TYR A 275      54.326  39.476   1.969  1.00  7.13           C  
-ANISOU 1793  CB  TYR A 275      867    821   1020     57    -29    283       C  
-ATOM   1794  CG  TYR A 275      54.532  40.920   2.333  1.00  6.92           C  
-ANISOU 1794  CG  TYR A 275      854    877    898     40     33    253       C  
-ATOM   1795  CD1 TYR A 275      55.316  41.748   1.547  1.00  7.46           C  
-ANISOU 1795  CD1 TYR A 275      908    934    990      0    145    160       C  
-ATOM   1796  CD2 TYR A 275      53.901  41.481   3.431  1.00  8.72           C  
-ANISOU 1796  CD2 TYR A 275     1039   1011   1260    -31    237    191       C  
-ATOM   1797  CE1 TYR A 275      55.484  43.092   1.850  1.00  8.44           C  
-ANISOU 1797  CE1 TYR A 275      994    998   1213    -58    137    198       C  
-ATOM   1798  CE2 TYR A 275      54.064  42.814   3.748  1.00  9.37           C  
-ANISOU 1798  CE2 TYR A 275     1229   1078   1252    -33    223     80       C  
-ATOM   1799  CZ  TYR A 275      54.847  43.629   2.946  1.00  8.80           C  
-ANISOU 1799  CZ  TYR A 275      983    930   1430    -13    116    133       C  
-ATOM   1800  OH  TYR A 275      54.991  44.950   3.266  1.00 10.72           O  
-ANISOU 1800  OH  TYR A 275     1292   1126   1653   -119    188    -21       O  
-ATOM   1801  N   PRO A 276      52.701  37.587  -0.810  1.00  8.66           N  
-ANISOU 1801  N   PRO A 276     1367    845   1076    -37   -106    266       N  
-ATOM   1802  CA  PRO A 276      52.164  36.251  -1.076  1.00  9.32           C  
-ANISOU 1802  CA  PRO A 276     1360    994   1187    -47    -50    132       C  
-ATOM   1803  C   PRO A 276      53.257  35.193  -1.120  1.00  9.09           C  
-ANISOU 1803  C   PRO A 276     1271    944   1236   -111     96    244       C  
-ATOM   1804  O   PRO A 276      54.396  35.470  -1.514  1.00 10.10           O  
-ANISOU 1804  O   PRO A 276     1508    961   1369   -188    273    251       O  
-ATOM   1805  CB  PRO A 276      51.504  36.421  -2.443  1.00 10.84           C  
-ANISOU 1805  CB  PRO A 276     1614   1152   1352    -82   -186    140       C  
-ATOM   1806  CG  PRO A 276      52.224  37.542  -3.065  1.00 11.09           C  
-ANISOU 1806  CG  PRO A 276     1828   1148   1238     51   -132    240       C  
-ATOM   1807  CD  PRO A 276      52.552  38.479  -1.975  1.00  9.53           C  
-ANISOU 1807  CD  PRO A 276     1623    930   1068     23   -169    289       C  
-ATOM   1808  N   LEU A 277      52.884  33.977  -0.732  1.00  8.45           N  
-ANISOU 1808  N   LEU A 277     1198    821   1189    -52    118    231       N  
-ATOM   1809  CA  LEU A 277      53.727  32.800  -0.875  1.00  8.89           C  
-ANISOU 1809  CA  LEU A 277     1155    987   1235    -29    155    126       C  
-ATOM   1810  C   LEU A 277      53.105  31.902  -1.932  1.00  9.49           C  
-ANISOU 1810  C   LEU A 277     1334   1094   1177    -68    312     94       C  
-ATOM   1811  O   LEU A 277      51.918  31.569  -1.880  1.00  9.55           O  
-ANISOU 1811  O   LEU A 277     1419   1206   1003   -134    169    -73       O  
-ATOM   1812  CB  LEU A 277      53.835  32.055   0.448  1.00  8.57           C  
-ANISOU 1812  CB  LEU A 277     1119    846   1290    -23     65    135       C  
-ATOM   1813  CG  LEU A 277      54.541  32.810   1.576  1.00 10.34           C  
-ANISOU 1813  CG  LEU A 277     1351    972   1603     30    -32     67       C  
-ATOM   1814  CD1 LEU A 277      54.434  32.070   2.892  1.00 11.22           C  
-ANISOU 1814  CD1 LEU A 277     1531   1200   1532    246   -261    125       C  
-ATOM   1815  CD2 LEU A 277      55.994  33.045   1.225  1.00 13.04           C  
-ANISOU 1815  CD2 LEU A 277     1588   1441   1922      5    -32    122       C  
-ATOM   1816  N   GLU A 278      53.900  31.515  -2.919  1.00 11.82           N  
-ANISOU 1816  N   GLU A 278     1593   1455   1442   -194    396    -12       N  
-ATOM   1817  CA  GLU A 278      53.408  30.657  -3.991  1.00 13.14           C  
-ANISOU 1817  CA  GLU A 278     1798   1636   1559   -141    323    -31       C  
-ATOM   1818  C   GLU A 278      52.920  29.330  -3.423  1.00 12.74           C  
-ANISOU 1818  C   GLU A 278     1734   1631   1474   -127    401    -93       C  
-ATOM   1819  O   GLU A 278      53.570  28.743  -2.584  1.00 13.72           O  
-ANISOU 1819  O   GLU A 278     1802   1518   1892    -63    433   -301       O  
-ATOM   1820  CB  GLU A 278      54.493  30.364  -5.029  1.00 15.03           C  
-ANISOU 1820  CB  GLU A 278     2023   1914   1773   -125    290    -53       C  
-ATOM   1821  CG  GLU A 278      54.884  31.546  -5.895  1.00 19.81           C  
-ANISOU 1821  CG  GLU A 278     2597   2473   2456   -142    170    -20       C  
-ATOM   1822  CD  GLU A 278      56.106  32.291  -5.398  0.00 25.21           C  
-ANISOU 1822  CD  GLU A 278     3296   3137   3144   -184    -40     88       C  
-ATOM   1823  OE1 GLU A 278      56.755  31.833  -4.429  0.00 30.12           O  
-ANISOU 1823  OE1 GLU A 278     3857   3678   3907   -226   -135     76       O  
-ATOM   1824  OE2 GLU A 278      56.425  33.341  -5.991  0.00 28.28           O  
-ANISOU 1824  OE2 GLU A 278     3638   3349   3755   -449     42    153       O  
-ATOM   1825  N   GLY A 279      51.776  28.881  -3.905  1.00 12.54           N  
-ANISOU 1825  N   GLY A 279     1746   1653   1366    -79    327   -127       N  
-ATOM   1826  CA  GLY A 279      51.238  27.597  -3.527  1.00 11.69           C  
-ANISOU 1826  CA  GLY A 279     1632   1468   1340    -95    282   -126       C  
-ATOM   1827  C   GLY A 279      50.755  27.516  -2.090  1.00  9.81           C  
-ANISOU 1827  C   GLY A 279     1374   1235   1117    -85    299   -122       C  
-ATOM   1828  O   GLY A 279      50.645  26.419  -1.557  1.00 10.54           O  
-ANISOU 1828  O   GLY A 279     1528   1166   1310    -89    463   -164       O  
-ATOM   1829  N   ASN A 280      50.441  28.653  -1.468  1.00  8.20           N  
-ANISOU 1829  N   ASN A 280     1244    997    872   -113    323    -50       N  
-ATOM   1830  CA  ASN A 280      50.025  28.690  -0.077  1.00  7.34           C  
-ANISOU 1830  CA  ASN A 280     1063    960    764   -108    179     -2       C  
-ATOM   1831  C   ASN A 280      48.545  28.329   0.098  1.00  6.50           C  
-ANISOU 1831  C   ASN A 280     1005    792    670   -123    166    -41       C  
-ATOM   1832  O   ASN A 280      47.701  29.134   0.514  1.00  7.06           O  
-ANISOU 1832  O   ASN A 280     1085    822    773   -106    158    -48       O  
-ATOM   1833  CB  ASN A 280      50.338  30.049   0.517  1.00  6.94           C  
-ANISOU 1833  CB  ASN A 280      968    824    844   -191    215     96       C  
-ATOM   1834  CG  ASN A 280      50.291  30.041   2.034  1.00  6.68           C  
-ANISOU 1834  CG  ASN A 280      965    841    730   -113    192    171       C  
-ATOM   1835  OD1 ASN A 280      50.340  28.986   2.656  1.00  7.71           O  
-ANISOU 1835  OD1 ASN A 280     1374    782    774   -110    200     80       O  
-ATOM   1836  ND2 ASN A 280      50.208  31.212   2.632  1.00  6.70           N  
-ANISOU 1836  ND2 ASN A 280      935    686    925    -29    210     22       N  
-ATOM   1837  N   LEU A 281      48.253  27.077  -0.217  1.00  7.21           N  
-ANISOU 1837  N   LEU A 281     1115    858    766   -140    163    -38       N  
-ATOM   1838  CA  LEU A 281      46.922  26.508  -0.091  1.00  7.12           C  
-ANISOU 1838  CA  LEU A 281     1040    897    766   -189     88     -3       C  
-ATOM   1839  C   LEU A 281      46.557  26.279   1.364  1.00  6.89           C  
-ANISOU 1839  C   LEU A 281      925    926    765   -188     88     12       C  
-ATOM   1840  O   LEU A 281      47.396  25.904   2.183  1.00  7.27           O  
-ANISOU 1840  O   LEU A 281      979   1122    659   -108     99      7       O  
-ATOM   1841  CB  LEU A 281      46.860  25.180  -0.831  1.00  8.36           C  
-ANISOU 1841  CB  LEU A 281     1229   1017    931   -218    140     -7       C  
-ATOM   1842  CG  LEU A 281      46.948  25.287  -2.354  1.00  9.69           C  
-ANISOU 1842  CG  LEU A 281     1411   1308    961   -205    169   -103       C  
-ATOM   1843  CD1 LEU A 281      47.295  23.940  -2.941  1.00 12.76           C  
-ANISOU 1843  CD1 LEU A 281     1976   1548   1323   -106     58   -154       C  
-ATOM   1844  CD2 LEU A 281      45.634  25.787  -2.931  1.00 11.18           C  
-ANISOU 1844  CD2 LEU A 281     1612   1586   1047   -210    -42   -118       C  
-ATOM   1845  N   ALA A 282      45.292  26.530   1.675  1.00  6.55           N  
-ANISOU 1845  N   ALA A 282      851    878    760   -156     67     86       N  
-ATOM   1846  CA  ALA A 282      44.723  26.126   2.941  1.00  6.25           C  
-ANISOU 1846  CA  ALA A 282      855    832    686    -99     63    -25       C  
-ATOM   1847  C   ALA A 282      44.790  24.620   3.094  1.00  5.72           C  
-ANISOU 1847  C   ALA A 282      739    837    596    -86    116    -33       C  
-ATOM   1848  O   ALA A 282      44.795  23.870   2.119  1.00  6.98           O  
-ANISOU 1848  O   ALA A 282     1111    919    619   -131    216    -60       O  
-ATOM   1849  CB  ALA A 282      43.296  26.593   3.022  1.00  6.29           C  
-ANISOU 1849  CB  ALA A 282      864    859    665   -137    -21      5       C  
-ATOM   1850  N   GLU A 283      44.789  24.160   4.337  1.00  5.17           N  
-ANISOU 1850  N   GLU A 283      790    651    521    -98     98   -104       N  
-ATOM   1851  CA  GLU A 283      44.709  22.726   4.588  1.00  5.70           C  
-ANISOU 1851  CA  GLU A 283      759    716    689    -11     84    -19       C  
-ATOM   1852  C   GLU A 283      43.454  22.121   3.961  1.00  5.30           C  
-ANISOU 1852  C   GLU A 283      730    719    565      2     97   -108       C  
-ATOM   1853  O   GLU A 283      43.499  21.039   3.369  1.00  6.26           O  
-ANISOU 1853  O   GLU A 283      843    847    687     18     81   -279       O  
-ATOM   1854  CB  GLU A 283      44.744  22.461   6.094  1.00  5.69           C  
-ANISOU 1854  CB  GLU A 283      777    770    613    -11     74    -85       C  
-ATOM   1855  CG  GLU A 283      44.480  21.017   6.455  1.00  6.55           C  
-ANISOU 1855  CG  GLU A 283     1049    775    662    -43     77     -8       C  
-ATOM   1856  CD  GLU A 283      44.361  20.745   7.929  1.00  6.26           C  
-ANISOU 1856  CD  GLU A 283      970    518    887     10    129     38       C  
-ATOM   1857  OE1 GLU A 283      44.705  21.602   8.755  1.00  6.99           O  
-ANISOU 1857  OE1 GLU A 283     1106    757    791   -150    -25    -26       O  
-ATOM   1858  OE2 GLU A 283      43.885  19.638   8.249  1.00  8.17           O  
-ANISOU 1858  OE2 GLU A 283     1540    695    867    -82    326    -66       O  
-ATOM   1859  N   GLY A 284      42.330  22.809   4.168  1.00  4.94           N  
-ANISOU 1859  N   GLY A 284      649    608    619    -35     96   -116       N  
-ATOM   1860  CA  GLY A 284      41.047  22.356   3.684  1.00  5.27           C  
-ANISOU 1860  CA  GLY A 284      727    681    591    -35    109   -150       C  
-ATOM   1861  C   GLY A 284      39.944  23.098   4.382  1.00  4.70           C  
-ANISOU 1861  C   GLY A 284      656    638    490    -34     20   -111       C  
-ATOM   1862  O   GLY A 284      40.120  24.239   4.774  1.00  4.81           O  
-ANISOU 1862  O   GLY A 284      750    555    522    -55     37   -107       O  
-ATOM   1863  N   VAL A 285      38.804  22.427   4.504  1.00  4.57           N  
-ANISOU 1863  N   VAL A 285      598    605    531     -4     76    -78       N  
-ATOM   1864  CA  VAL A 285      37.627  22.982   5.159  1.00  4.56           C  
-ANISOU 1864  CA  VAL A 285      604    577    552     17     31    -61       C  
-ATOM   1865  C   VAL A 285      37.010  21.981   6.115  1.00  4.61           C  
-ANISOU 1865  C   VAL A 285      582    544    626     21     31    -54       C  
-ATOM   1866  O   VAL A 285      37.176  20.763   5.970  1.00  4.93           O  
-ANISOU 1866  O   VAL A 285      734    517    621     15    199    -86       O  
-ATOM   1867  CB  VAL A 285      36.548  23.462   4.151  1.00  5.04           C  
-ANISOU 1867  CB  VAL A 285      692    639    583     32     12    -37       C  
-ATOM   1868  CG1 VAL A 285      37.097  24.614   3.321  1.00  6.08           C  
-ANISOU 1868  CG1 VAL A 285      837    743    730     41    -48    -42       C  
-ATOM   1869  CG2 VAL A 285      36.023  22.333   3.287  1.00  6.32           C  
-ANISOU 1869  CG2 VAL A 285      838    785    776    -29    -42   -181       C  
-ATOM   1870  N   VAL A 286      36.294  22.520   7.097  1.00  3.98           N  
-ANISOU 1870  N   VAL A 286      549    429    535      5     56    -69       N  
-ATOM   1871  CA  VAL A 286      35.398  21.760   7.949  1.00  4.31           C  
-ANISOU 1871  CA  VAL A 286      604    488    545     47     80     14       C  
-ATOM   1872  C   VAL A 286      33.979  22.163   7.581  1.00  4.45           C  
-ANISOU 1872  C   VAL A 286      608    485    595     50     62    -11       C  
-ATOM   1873  O   VAL A 286      33.669  23.355   7.470  1.00  5.08           O  
-ANISOU 1873  O   VAL A 286      636    488    803     90     14     20       O  
-ATOM   1874  CB  VAL A 286      35.682  22.050   9.432  1.00  4.84           C  
-ANISOU 1874  CB  VAL A 286      672    576    591     44     70    -25       C  
-ATOM   1875  CG1 VAL A 286      34.632  21.442  10.340  1.00  5.51           C  
-ANISOU 1875  CG1 VAL A 286      781    728    584     57     40     13       C  
-ATOM   1876  CG2 VAL A 286      37.072  21.519   9.801  1.00  5.34           C  
-ANISOU 1876  CG2 VAL A 286      669    679    680    -47     48    -54       C  
-ATOM   1877  N   ILE A 287      33.134  21.156   7.363  1.00  4.90           N  
-ANISOU 1877  N   ILE A 287      627    522    711     73     35     -3       N  
-ATOM   1878  CA  ILE A 287      31.742  21.361   6.970  1.00  4.88           C  
-ANISOU 1878  CA  ILE A 287      591    517    745     60      7     30       C  
-ATOM   1879  C   ILE A 287      30.880  20.861   8.110  1.00  4.87           C  
-ANISOU 1879  C   ILE A 287      507    577    765     65     12     27       C  
-ATOM   1880  O   ILE A 287      31.066  19.749   8.613  1.00  5.64           O  
-ANISOU 1880  O   ILE A 287      644    597    901     81    108    112       O  
-ATOM   1881  CB  ILE A 287      31.454  20.612   5.658  1.00  5.65           C  
-ANISOU 1881  CB  ILE A 287      729    612    803     69    -56    -36       C  
-ATOM   1882  CG1 ILE A 287      32.210  21.311   4.513  1.00  6.69           C  
-ANISOU 1882  CG1 ILE A 287      856    819    864     23    -30      1       C  
-ATOM   1883  CG2 ILE A 287      29.966  20.532   5.390  1.00  6.65           C  
-ANISOU 1883  CG2 ILE A 287      797    924    803    -30    -40    -60       C  
-ATOM   1884  CD1 ILE A 287      32.283  20.504   3.229  1.00  7.77           C  
-ANISOU 1884  CD1 ILE A 287     1042   1004    904     20     36   -109       C  
-ATOM   1885  N   ARG A 288      29.924  21.684   8.530  1.00  5.30           N  
-ANISOU 1885  N   ARG A 288      594    612    808     69    118    120       N  
-ATOM   1886  CA  ARG A 288      29.090  21.339   9.667  1.00  5.35           C  
-ANISOU 1886  CA  ARG A 288      596    634    801     59     21     37       C  
-ATOM   1887  C   ARG A 288      27.683  21.900   9.508  1.00  5.13           C  
-ANISOU 1887  C   ARG A 288      566    602    778     98      1    -13       C  
-ATOM   1888  O   ARG A 288      27.473  22.935   8.895  1.00  5.59           O  
-ANISOU 1888  O   ARG A 288      591    651    880     89     10     13       O  
-ATOM   1889  CB  ARG A 288      29.703  21.830  10.978  1.00  6.21           C  
-ANISOU 1889  CB  ARG A 288      610    887    860     88     75     87       C  
-ATOM   1890  CG  ARG A 288      29.902  23.331  11.047  1.00  7.15           C  
-ANISOU 1890  CG  ARG A 288      779   1019    916    -37    -33     -4       C  
-ATOM   1891  CD  ARG A 288      30.782  23.711  12.205  1.00  8.37           C  
-ANISOU 1891  CD  ARG A 288      916   1228   1034   -116    -48    -76       C  
-ATOM   1892  NE  ARG A 288      30.097  23.543  13.479  1.00  7.60           N  
-ANISOU 1892  NE  ARG A 288      719   1260    908   -209    -26    -49       N  
-ATOM   1893  CZ  ARG A 288      30.712  23.360  14.638  1.00  7.30           C  
-ANISOU 1893  CZ  ARG A 288      750   1067    955   -106   -133    -66       C  
-ATOM   1894  NH1 ARG A 288      32.034  23.243  14.700  1.00  7.77           N  
-ANISOU 1894  NH1 ARG A 288      822   1167    963    132   -108   -255       N  
-ATOM   1895  NH2 ARG A 288      30.000  23.243  15.750  1.00  7.40           N  
-ANISOU 1895  NH2 ARG A 288      723   1166    922    106    -81    -25       N  
-ATOM   1896  N   HIS A 289      26.735  21.216  10.119  1.00  5.36           N  
-ANISOU 1896  N   HIS A 289      601    640    797     97    -49     -5       N  
-ATOM   1897  CA  HIS A 289      25.347  21.661  10.166  1.00  4.88           C  
-ANISOU 1897  CA  HIS A 289      544    606    702    104      1    -30       C  
-ATOM   1898  C   HIS A 289      25.287  22.902  11.031  1.00  5.22           C  
-ANISOU 1898  C   HIS A 289      515    648    820     76    -19    -83       C  
-ATOM   1899  O   HIS A 289      25.900  22.941  12.095  1.00  5.93           O  
-ANISOU 1899  O   HIS A 289      588    809    854     38    -21    -78       O  
-ATOM   1900  CB  HIS A 289      24.492  20.531  10.767  1.00  5.71           C  
-ANISOU 1900  CB  HIS A 289      653    593    923     58     33     10       C  
-ATOM   1901  CG  HIS A 289      23.022  20.736  10.654  1.00  6.16           C  
-ANISOU 1901  CG  HIS A 289      694    750    896     72     73   -124       C  
-ATOM   1902  ND1 HIS A 289      22.381  21.815  11.195  1.00  7.90           N  
-ANISOU 1902  ND1 HIS A 289      669    824   1507   -105     71   -227       N  
-ATOM   1903  CD2 HIS A 289      22.054  19.930  10.165  1.00  8.97           C  
-ANISOU 1903  CD2 HIS A 289      920    882   1604     45     13   -171       C  
-ATOM   1904  CE1 HIS A 289      21.091  21.723  10.938  1.00  7.86           C  
-ANISOU 1904  CE1 HIS A 289      712    691   1580     95     91   -188       C  
-ATOM   1905  NE2 HIS A 289      20.866  20.595  10.304  1.00  8.11           N  
-ANISOU 1905  NE2 HIS A 289      660   1114   1305     87      0    -65       N  
-ATOM   1906  N   VAL A 290      24.521  23.905  10.630  1.00  5.87           N  
-ANISOU 1906  N   VAL A 290      638    731    857     67     -3   -142       N  
-ATOM   1907  CA  VAL A 290      24.488  25.142  11.390  1.00  6.53           C  
-ANISOU 1907  CA  VAL A 290      749    698   1034     38     69   -115       C  
-ATOM   1908  C   VAL A 290      23.858  25.000  12.770  1.00  6.52           C  
-ANISOU 1908  C   VAL A 290      709    676   1089     72     53    -88       C  
-ATOM   1909  O   VAL A 290      24.050  25.878  13.606  1.00  6.88           O  
-ANISOU 1909  O   VAL A 290      777    710   1124      9     71   -223       O  
-ATOM   1910  CB  VAL A 290      23.836  26.310  10.618  1.00  7.79           C  
-ANISOU 1910  CB  VAL A 290      973    774   1212    113    133    -35       C  
-ATOM   1911  CG1 VAL A 290      24.584  26.591   9.329  1.00  8.54           C  
-ANISOU 1911  CG1 VAL A 290     1124    887   1234    139    117     13       C  
-ATOM   1912  CG2 VAL A 290      22.356  26.089  10.409  1.00  8.74           C  
-ANISOU 1912  CG2 VAL A 290     1078   1006   1236    210    101    -29       C  
-ATOM   1913  N   ARG A 291      23.121  23.919  13.011  1.00  6.70           N  
-ANISOU 1913  N   ARG A 291      714    823   1007     32     78    -97       N  
-ATOM   1914  CA  ARG A 291      22.558  23.636  14.325  1.00  7.46           C  
-ANISOU 1914  CA  ARG A 291      743    961   1131     26    172    -87       C  
-ATOM   1915  C   ARG A 291      23.140  22.375  14.932  1.00  7.30           C  
-ANISOU 1915  C   ARG A 291      767    914   1093     20    167   -117       C  
-ATOM   1916  O   ARG A 291      22.545  21.780  15.815  1.00  8.31           O  
-ANISOU 1916  O   ARG A 291      843   1082   1232     40    338    -28       O  
-ATOM   1917  CB  ARG A 291      21.029  23.594  14.277  1.00  8.90           C  
-ANISOU 1917  CB  ARG A 291      913   1153   1314     54    207    -77       C  
-ATOM   1918  CG  ARG A 291      20.465  24.959  13.915  1.00 13.01           C  
-ANISOU 1918  CG  ARG A 291     1252   1805   1886    215    283    154       C  
-ATOM   1919  CD  ARG A 291      20.653  26.061  14.968  1.00 19.77           C  
-ANISOU 1919  CD  ARG A 291     2372   2489   2648     43    122    103       C  
-ATOM   1920  NE  ARG A 291      19.893  25.853  16.209  1.00 23.69           N  
-ANISOU 1920  NE  ARG A 291     2943   2992   3064    114    176    -75       N  
-ATOM   1921  CZ  ARG A 291      19.894  26.689  17.259  1.00 27.86           C  
-ANISOU 1921  CZ  ARG A 291     3511   3546   3527    -68    111    -20       C  
-ATOM   1922  NH1 ARG A 291      20.636  27.794  17.257  1.00 29.34           N  
-ANISOU 1922  NH1 ARG A 291     3791   3645   3711    -37    157    -35       N  
-ATOM   1923  NH2 ARG A 291      19.166  26.403  18.335  1.00 29.81           N  
-ANISOU 1923  NH2 ARG A 291     3798   3779   3749    -44     94      7       N  
-ATOM   1924  N   ARG A 292      24.344  22.007  14.512  1.00  7.26           N  
-ANISOU 1924  N   ARG A 292      815    924   1018     51    171   -129       N  
-ATOM   1925  CA  ARG A 292      25.083  20.949  15.190  1.00  7.74           C  
-ANISOU 1925  CA  ARG A 292      875   1062   1005     48    118    -45       C  
-ATOM   1926  C   ARG A 292      25.039  21.172  16.702  1.00  8.11           C  
-ANISOU 1926  C   ARG A 292      915   1060   1105     60    158    -87       C  
-ATOM   1927  O   ARG A 292      25.284  22.279  17.190  1.00  8.45           O  
-ANISOU 1927  O   ARG A 292      991   1207   1010      3    275   -197       O  
-ATOM   1928  CB  ARG A 292      26.533  20.932  14.719  1.00  7.31           C  
-ANISOU 1928  CB  ARG A 292      823   1004    947     98    181   -148       C  
-ATOM   1929  CG  ARG A 292      27.425  20.000  15.474  1.00  9.06           C  
-ANISOU 1929  CG  ARG A 292      990   1369   1081    314    127    -18       C  
-ATOM   1930  CD  ARG A 292      28.706  19.723  14.710  1.00  9.52           C  
-ANISOU 1930  CD  ARG A 292      925   1522   1167    422     95     81       C  
-ATOM   1931  NE  ARG A 292      29.514  18.683  15.360  1.00 13.46           N  
-ANISOU 1931  NE  ARG A 292     1248   2296   1569    459    461    -50       N  
-ATOM   1932  CZ  ARG A 292      30.316  18.903  16.352  1.00 13.64           C  
-ANISOU 1932  CZ  ARG A 292     1240   2210   1732    376    465    -97       C  
-ATOM   1933  NH1 ARG A 292      30.499  20.135  16.795  1.00 15.43           N  
-ANISOU 1933  NH1 ARG A 292     1683   2119   2059    288    -64   -170       N  
-ATOM   1934  NH2 ARG A 292      30.976  17.893  16.905  1.00 12.06           N  
-ANISOU 1934  NH2 ARG A 292     1453   1560   1568    468     31    151       N  
-ATOM   1935  N   GLY A 293      24.719  20.120  17.436  1.00  9.14           N  
-ANISOU 1935  N   GLY A 293     1071   1290   1111     10    171    -62       N  
-ATOM   1936  CA  GLY A 293      24.597  20.200  18.880  1.00  9.93           C  
-ANISOU 1936  CA  GLY A 293     1212   1387   1173    -53    105    -31       C  
-ATOM   1937  C   GLY A 293      23.178  20.390  19.386  1.00 10.47           C  
-ANISOU 1937  C   GLY A 293     1341   1486   1152    -54    266   -102       C  
-ATOM   1938  O   GLY A 293      22.904  20.105  20.557  1.00 12.86           O  
-ANISOU 1938  O   GLY A 293     1734   1975   1176    -71    361    -10       O  
-ATOM   1939  N   ASP A 294      22.271  20.868  18.544  1.00 10.45           N  
-ANISOU 1939  N   ASP A 294     1297   1434   1239      1    352   -141       N  
-ATOM   1940  CA  ASP A 294      20.880  21.052  18.953  1.00 11.81           C  
-ANISOU 1940  CA  ASP A 294     1447   1553   1488     44    292   -139       C  
-ATOM   1941  C   ASP A 294      20.230  19.687  19.098  1.00 11.76           C  
-ANISOU 1941  C   ASP A 294     1419   1612   1434     14    350   -132       C  
-ATOM   1942  O   ASP A 294      20.431  18.826  18.249  1.00 10.49           O  
-ANISOU 1942  O   ASP A 294     1186   1361   1438     36    360   -201       O  
-ATOM   1943  CB  ASP A 294      20.135  21.853  17.899  1.00 12.62           C  
-ANISOU 1943  CB  ASP A 294     1463   1577   1752    118    316   -138       C  
-ATOM   1944  CG  ASP A 294      18.711  22.155  18.305  1.00 16.43           C  
-ANISOU 1944  CG  ASP A 294     1910   1905   2425    184    255   -129       C  
-ATOM   1945  OD1 ASP A 294      18.454  23.275  18.779  1.00 23.07           O  
-ANISOU 1945  OD1 ASP A 294     2654   2742   3369    331    492   -263       O  
-ATOM   1946  OD2 ASP A 294      17.794  21.334  18.205  1.00 20.46           O  
-ANISOU 1946  OD2 ASP A 294     1908   2522   3341    411    538     32       O  
-ATOM   1947  N   PRO A 295      19.465  19.452  20.170  1.00 13.04           N  
-ANISOU 1947  N   PRO A 295     1646   1729   1579    -45    314   -117       N  
-ATOM   1948  CA  PRO A 295      18.816  18.148  20.347  1.00 13.41           C  
-ANISOU 1948  CA  PRO A 295     1655   1787   1653    -56    298    -57       C  
-ATOM   1949  C   PRO A 295      18.017  17.647  19.148  1.00 12.36           C  
-ANISOU 1949  C   PRO A 295     1440   1669   1585    -45    394    -25       C  
-ATOM   1950  O   PRO A 295      18.015  16.451  18.918  1.00 12.76           O  
-ANISOU 1950  O   PRO A 295     1504   1556   1788      0    502   -101       O  
-ATOM   1951  CB  PRO A 295      17.896  18.370  21.551  1.00 14.58           C  
-ANISOU 1951  CB  PRO A 295     1835   2001   1702    -59    290    -64       C  
-ATOM   1952  CG  PRO A 295      18.516  19.459  22.304  1.00 15.54           C  
-ANISOU 1952  CG  PRO A 295     2001   2045   1857    -23    236    -48       C  
-ATOM   1953  CD  PRO A 295      19.209  20.343  21.320  1.00 14.11           C  
-ANISOU 1953  CD  PRO A 295     1791   1926   1643    -63    305   -109       C  
-ATOM   1954  N   ALA A 296      17.338  18.515  18.414  1.00 12.24           N  
-ANISOU 1954  N   ALA A 296     1357   1626   1664    126    386    -95       N  
-ATOM   1955  CA  ALA A 296      16.563  18.083  17.260  1.00 12.75           C  
-ANISOU 1955  CA  ALA A 296     1489   1645   1708     76    165    -37       C  
-ATOM   1956  C   ALA A 296      17.464  17.609  16.115  1.00 12.44           C  
-ANISOU 1956  C   ALA A 296     1454   1599   1671     89    150    -73       C  
-ATOM   1957  O   ALA A 296      17.038  16.817  15.286  1.00 14.64           O  
-ANISOU 1957  O   ALA A 296     1550   1993   2020    -89     86   -103       O  
-ATOM   1958  CB  ALA A 296      15.620  19.183  16.774  1.00 14.02           C  
-ANISOU 1958  CB  ALA A 296     1638   1813   1875    114     74    -12       C  
-ATOM   1959  N   VAL A 297      18.696  18.101  16.050  1.00 11.35           N  
-ANISOU 1959  N   VAL A 297     1373   1411   1525     62    201   -129       N  
-ATOM   1960  CA  VAL A 297      19.686  17.573  15.102  1.00 11.37           C  
-ANISOU 1960  CA  VAL A 297     1414   1489   1417    -34    187   -137       C  
-ATOM   1961  C   VAL A 297      20.300  16.291  15.638  1.00 10.85           C  
-ANISOU 1961  C   VAL A 297     1226   1405   1490     -5    215   -158       C  
-ATOM   1962  O   VAL A 297      20.427  15.294  14.932  1.00 11.02           O  
-ANISOU 1962  O   VAL A 297     1231   1415   1539     25    238   -377       O  
-ATOM   1963  CB  VAL A 297      20.802  18.600  14.840  1.00 12.26           C  
-ANISOU 1963  CB  VAL A 297     1549   1636   1471    -98    225   -123       C  
-ATOM   1964  CG1 VAL A 297      22.001  17.964  14.107  1.00 12.81           C  
-ANISOU 1964  CG1 VAL A 297     1645   1715   1505   -225    159   -151       C  
-ATOM   1965  CG2 VAL A 297      20.248  19.746  14.046  1.00 14.27           C  
-ANISOU 1965  CG2 VAL A 297     1875   1780   1767    -74      9   -216       C  
-ATOM   1966  N   GLU A 298      20.707  16.327  16.889  1.00 11.35           N  
-ANISOU 1966  N   GLU A 298     1321   1416   1575     67    123    -88       N  
-ATOM   1967  CA  GLU A 298      21.426  15.211  17.495  1.00 12.68           C  
-ANISOU 1967  CA  GLU A 298     1542   1538   1736     90     31    -45       C  
-ATOM   1968  C   GLU A 298      20.585  13.956  17.631  1.00 12.10           C  
-ANISOU 1968  C   GLU A 298     1511   1463   1620    126     49    -31       C  
-ATOM   1969  O   GLU A 298      21.129  12.866  17.694  1.00 12.22           O  
-ANISOU 1969  O   GLU A 298     1590   1419   1633    286     -3     52       O  
-ATOM   1970  CB  GLU A 298      21.936  15.613  18.882  1.00 13.76           C  
-ANISOU 1970  CB  GLU A 298     1685   1670   1872    125    -44    -43       C  
-ATOM   1971  CG  GLU A 298      22.959  16.729  18.859  1.00 15.90           C  
-ANISOU 1971  CG  GLU A 298     1931   1884   2225    144    -25   -112       C  
-ATOM   1972  CD  GLU A 298      24.120  16.391  17.957  1.00 17.80           C  
-ANISOU 1972  CD  GLU A 298     2176   2078   2509     75     61   -165       C  
-ATOM   1973  OE1 GLU A 298      24.715  15.318  18.185  1.00 17.49           O  
-ANISOU 1973  OE1 GLU A 298     2065   2077   2503     33    232    148       O  
-ATOM   1974  OE2 GLU A 298      24.419  17.155  16.998  1.00 18.24           O  
-ANISOU 1974  OE2 GLU A 298     2038   2099   2791    397   -167   -375       O  
-ATOM   1975  N   LYS A 299      19.264  14.103  17.649  1.00 12.00           N  
-ANISOU 1975  N   LYS A 299     1512   1459   1588     39    103     31       N  
-ATOM   1976  CA  LYS A 299      18.387  12.960  17.831  1.00 11.96           C  
-ANISOU 1976  CA  LYS A 299     1481   1481   1580      6    153     67       C  
-ATOM   1977  C   LYS A 299      18.562  11.933  16.722  1.00 11.04           C  
-ANISOU 1977  C   LYS A 299     1355   1393   1447    -12    187    138       C  
-ATOM   1978  O   LYS A 299      18.241  10.778  16.910  1.00 11.87           O  
-ANISOU 1978  O   LYS A 299     1637   1345   1527   -123    335    269       O  
-ATOM   1979  CB  LYS A 299      16.916  13.406  17.924  1.00 13.12           C  
-ANISOU 1979  CB  LYS A 299     1549   1671   1765    -64    245     36       C  
-ATOM   1980  CG  LYS A 299      16.315  13.879  16.622  1.00 14.63           C  
-ANISOU 1980  CG  LYS A 299     1541   1976   2042     61    264      1       C  
-ATOM   1981  CD  LYS A 299      14.823  14.207  16.734  1.00 18.08           C  
-ANISOU 1981  CD  LYS A 299     1921   2520   2428     66    187      2       C  
-ATOM   1982  CE  LYS A 299      14.305  14.851  15.448  1.00 20.05           C  
-ANISOU 1982  CE  LYS A 299     2020   2933   2665    162     44   -155       C  
-ATOM   1983  NZ  LYS A 299      12.830  15.127  15.487  1.00 22.97           N  
-ANISOU 1983  NZ  LYS A 299     2148   3365   3213    147    163   -107       N  
-ATOM   1984  N   HIS A 300      19.021  12.354  15.549  1.00  9.79           N  
-ANISOU 1984  N   HIS A 300     1164   1164   1390     32    207    228       N  
-ATOM   1985  CA  HIS A 300      19.188  11.434  14.433  1.00  8.95           C  
-ANISOU 1985  CA  HIS A 300     1064   1146   1191     17    129    175       C  
-ATOM   1986  C   HIS A 300      20.392  10.511  14.561  1.00  8.41           C  
-ANISOU 1986  C   HIS A 300     1057    977   1160     22    200    164       C  
-ATOM   1987  O   HIS A 300      20.546   9.589  13.774  1.00  9.88           O  
-ANISOU 1987  O   HIS A 300     1229   1194   1330     96    138     66       O  
-ATOM   1988  CB  HIS A 300      19.297  12.219  13.143  1.00  9.44           C  
-ANISOU 1988  CB  HIS A 300     1107   1190   1288    -24     90    138       C  
-ATOM   1989  CG  HIS A 300      18.084  13.033  12.848  1.00  9.82           C  
-ANISOU 1989  CG  HIS A 300      986   1301   1444    102     73     79       C  
-ATOM   1990  ND1 HIS A 300      17.022  12.550  12.117  1.00 13.98           N  
-ANISOU 1990  ND1 HIS A 300     1361   1772   2176    115    -79     40       N  
-ATOM   1991  CD2 HIS A 300      17.739  14.283  13.236  1.00 13.47           C  
-ANISOU 1991  CD2 HIS A 300     1501   1526   2089    151   -257    -39       C  
-ATOM   1992  CE1 HIS A 300      16.102  13.489  12.018  1.00 13.24           C  
-ANISOU 1992  CE1 HIS A 300     1391   1656   1981    284   -190     -4       C  
-ATOM   1993  NE2 HIS A 300      16.508  14.548  12.692  1.00 13.57           N  
-ANISOU 1993  NE2 HIS A 300     1337   1706   2113    419   -221   -144       N  
-ATOM   1994  N   ASN A 301      21.261  10.773  15.525  1.00  8.92           N  
-ANISOU 1994  N   ASN A 301     1128   1026   1234      4    212    102       N  
-ATOM   1995  CA  ASN A 301      22.418   9.916  15.780  1.00  8.79           C  
-ANISOU 1995  CA  ASN A 301     1095   1064   1179     18    179    101       C  
-ATOM   1996  C   ASN A 301      23.349   9.811  14.570  1.00  8.93           C  
-ANISOU 1996  C   ASN A 301     1132   1020   1240    -10    221     65       C  
-ATOM   1997  O   ASN A 301      23.896   8.747  14.298  1.00  9.88           O  
-ANISOU 1997  O   ASN A 301     1418    996   1340     47    459    125       O  
-ATOM   1998  CB  ASN A 301      21.966   8.525  16.227  1.00  9.31           C  
-ANISOU 1998  CB  ASN A 301     1165   1148   1221      4    176    154       C  
-ATOM   1999  CG  ASN A 301      23.099   7.680  16.756  1.00 10.16           C  
-ANISOU 1999  CG  ASN A 301     1264   1316   1278     -2     43    140       C  
-ATOM   2000  OD1 ASN A 301      23.968   8.160  17.495  1.00 11.85           O  
-ANISOU 2000  OD1 ASN A 301     1491   1601   1410     46    -34    294       O  
-ATOM   2001  ND2 ASN A 301      23.075   6.396  16.413  1.00 11.13           N  
-ANISOU 2001  ND2 ASN A 301     1404   1403   1419     94    194    341       N  
-ATOM   2002  N   VAL A 302      23.537  10.932  13.878  1.00  8.78           N  
-ANISOU 2002  N   VAL A 302     1128   1019   1189    -77    281     34       N  
-ATOM   2003  CA  VAL A 302      24.481  11.024  12.775  1.00  9.58           C  
-ANISOU 2003  CA  VAL A 302     1207   1099   1330    -85    261     44       C  
-ATOM   2004  C   VAL A 302      25.357  12.247  12.994  1.00  8.39           C  
-ANISOU 2004  C   VAL A 302     1068    932   1185   -110    264     90       C  
-ATOM   2005  O   VAL A 302      24.862  13.374  13.199  1.00  9.60           O  
-ANISOU 2005  O   VAL A 302     1085    920   1643    -99    364     94       O  
-ATOM   2006  CB  VAL A 302      23.778  11.098  11.420  1.00 10.12           C  
-ANISOU 2006  CB  VAL A 302     1218   1189   1436   -351    296     27       C  
-ATOM   2007  CG1 VAL A 302      22.907  12.263  11.285  1.00 16.11           C  
-ANISOU 2007  CG1 VAL A 302     1962   2211   1947    -70    180     23       C  
-ATOM   2008  CG2 VAL A 302      24.795  11.046  10.295  1.00 11.28           C  
-ANISOU 2008  CG2 VAL A 302     1498   1377   1409   -256    300    -11       C  
-ATOM   2009  N   SER A 303      26.668  12.049  12.975  1.00  8.16           N  
-ANISOU 2009  N   SER A 303     1027    877   1194    -11    209     87       N  
-ATOM   2010  CA  SER A 303      27.566  13.173  13.179  1.00  7.82           C  
-ANISOU 2010  CA  SER A 303     1009    900   1062     -1    135     75       C  
-ATOM   2011  C   SER A 303      27.408  14.210  12.060  1.00  6.73           C  
-ANISOU 2011  C   SER A 303      829    814    914    -11    149     37       C  
-ATOM   2012  O   SER A 303      27.357  13.875  10.881  1.00  7.09           O  
-ANISOU 2012  O   SER A 303      929    837    926    -70    244    -79       O  
-ATOM   2013  CB  SER A 303      29.006  12.687  13.260  1.00  9.01           C  
-ANISOU 2013  CB  SER A 303     1086   1075   1262     30     36    165       C  
-ATOM   2014  OG  SER A 303      29.881  13.779  13.215  1.00 10.60           O  
-ANISOU 2014  OG  SER A 303     1138   1203   1686    -43   -114    141       O  
-ATOM   2015  N   THR A 304      27.349  15.471  12.457  1.00  6.52           N  
-ANISOU 2015  N   THR A 304      812    734    930    -28    104     -4       N  
-ATOM   2016  CA  THR A 304      27.143  16.556  11.494  1.00  7.00           C  
-ANISOU 2016  CA  THR A 304      764    771   1124    -11    110     65       C  
-ATOM   2017  C   THR A 304      28.367  17.437  11.337  1.00  5.94           C  
-ANISOU 2017  C   THR A 304      716    681    859    -46     54     69       C  
-ATOM   2018  O   THR A 304      28.245  18.641  11.132  1.00  6.73           O  
-ANISOU 2018  O   THR A 304      734    685   1136     45     32      4       O  
-ATOM   2019  CB  THR A 304      25.940  17.380  11.818  1.00  9.22           C  
-ANISOU 2019  CB  THR A 304      943   1038   1519     -2    255     62       C  
-ATOM   2020  OG1 THR A 304      26.086  17.865  13.140  1.00 11.87           O  
-ANISOU 2020  OG1 THR A 304      974   1315   2218   -180    748   -234       O  
-ATOM   2021  CG2 THR A 304      24.658  16.565  11.778  1.00 11.20           C  
-ANISOU 2021  CG2 THR A 304     1056   1230   1968     61     95     73       C  
-ATOM   2022  N   ILE A 305      29.539  16.822  11.373  1.00  5.67           N  
-ANISOU 2022  N   ILE A 305      685    618    851     55    101     28       N  
-ATOM   2023  CA  ILE A 305      30.775  17.524  11.063  1.00  5.33           C  
-ANISOU 2023  CA  ILE A 305      725    570    731     26    115     60       C  
-ATOM   2024  C   ILE A 305      31.656  16.609  10.238  1.00  5.43           C  
-ANISOU 2024  C   ILE A 305      726    558    778     12     68     34       C  
-ATOM   2025  O   ILE A 305      31.798  15.420  10.545  1.00  5.98           O  
-ANISOU 2025  O   ILE A 305      929    568    772     78    211    -23       O  
-ATOM   2026  CB  ILE A 305      31.451  18.050  12.354  1.00  5.68           C  
-ANISOU 2026  CB  ILE A 305      762    605    791      5    160     -7       C  
-ATOM   2027  CG1 ILE A 305      32.569  19.040  12.052  1.00  5.86           C  
-ANISOU 2027  CG1 ILE A 305      700    738    788     61     89    -92       C  
-ATOM   2028  CG2 ILE A 305      31.916  16.920  13.274  1.00  6.65           C  
-ANISOU 2028  CG2 ILE A 305      823    802    901    -17    150     68       C  
-ATOM   2029  CD1 ILE A 305      32.917  19.887  13.254  1.00  7.12           C  
-ANISOU 2029  CD1 ILE A 305      879    875    951   -151    206    -76       C  
-ATOM   2030  N   ILE A 306      32.219  17.161   9.169  1.00  5.17           N  
-ANISOU 2030  N   ILE A 306      626    620    716     84     66     60       N  
-ATOM   2031  CA  ILE A 306      33.111  16.423   8.276  1.00  5.81           C  
-ANISOU 2031  CA  ILE A 306      751    749    705    -60     23   -127       C  
-ATOM   2032  C   ILE A 306      34.209  17.376   7.816  1.00  5.02           C  
-ANISOU 2032  C   ILE A 306      630    584    692     30     32   -108       C  
-ATOM   2033  O   ILE A 306      34.140  18.584   8.040  1.00  5.64           O  
-ANISOU 2033  O   ILE A 306      681    595    865     31    136   -101       O  
-ATOM   2034  CB  ILE A 306      32.398  15.812   7.056  1.00  7.65           C  
-ANISOU 2034  CB  ILE A 306      925   1139    841   -140     76    -55       C  
-ATOM   2035  CG1 ILE A 306      31.693  16.886   6.281  1.00  9.32           C  
-ANISOU 2035  CG1 ILE A 306     1033   1166   1339    -97    149   -209       C  
-ATOM   2036  CG2 ILE A 306      31.446  14.687   7.431  1.00  9.83           C  
-ANISOU 2036  CG2 ILE A 306     1238   1345   1149   -142    -59   -171       C  
-ATOM   2037  CD1 ILE A 306      31.159  16.426   4.941  1.00 11.43           C  
-ANISOU 2037  CD1 ILE A 306     1436   1496   1412     99   -115    -75       C  
-ATOM   2038  N   LYS A 307      35.231  16.835   7.169  1.00  5.32           N  
-ANISOU 2038  N   LYS A 307      666    593    761     25    185    -87       N  
-ATOM   2039  CA  LYS A 307      36.295  17.661   6.612  1.00  5.83           C  
-ANISOU 2039  CA  LYS A 307      783    655    777     -5    174    -50       C  
-ATOM   2040  C   LYS A 307      36.569  17.255   5.173  1.00  5.53           C  
-ANISOU 2040  C   LYS A 307      761    546    794     59    200    -95       C  
-ATOM   2041  O   LYS A 307      36.283  16.131   4.755  1.00  6.58           O  
-ANISOU 2041  O   LYS A 307      974    660    866    -56    297   -190       O  
-ATOM   2042  CB  LYS A 307      37.584  17.519   7.428  1.00  6.65           C  
-ANISOU 2042  CB  LYS A 307      845    799    881    -95    113   -139       C  
-ATOM   2043  CG  LYS A 307      38.237  16.162   7.232  1.00  7.79           C  
-ANISOU 2043  CG  LYS A 307      971    909   1080      9     68   -157       C  
-ATOM   2044  CD  LYS A 307      39.383  15.905   8.181  1.00  8.29           C  
-ANISOU 2044  CD  LYS A 307     1108    875   1166     95     28   -331       C  
-ATOM   2045  CE  LYS A 307      39.971  14.529   7.957  1.00  8.40           C  
-ANISOU 2045  CE  LYS A 307      951   1046   1195    139     70   -429       C  
-ATOM   2046  NZ  LYS A 307      40.613  14.028   9.188  1.00  9.13           N  
-ANISOU 2046  NZ  LYS A 307     1192   1128   1145     35    -98   -387       N  
-ATOM   2047  N   LEU A 308      37.139  18.196   4.427  1.00  5.82           N  
-ANISOU 2047  N   LEU A 308      851    586    774    -55    214   -182       N  
-ATOM   2048  CA  LEU A 308      37.752  17.954   3.130  1.00  6.00           C  
-ANISOU 2048  CA  LEU A 308      874    673    732      0    205   -191       C  
-ATOM   2049  C   LEU A 308      39.129  18.587   3.165  1.00  6.06           C  
-ANISOU 2049  C   LEU A 308      831    656    814    -45    152   -165       C  
-ATOM   2050  O   LEU A 308      39.283  19.699   3.664  1.00  7.15           O  
-ANISOU 2050  O   LEU A 308      912    616   1187    -86    271   -268       O  
-ATOM   2051  CB  LEU A 308      36.969  18.622   2.011  1.00  7.02           C  
-ANISOU 2051  CB  LEU A 308     1012    734    921    -10    178   -226       C  
-ATOM   2052  CG  LEU A 308      35.516  18.234   1.803  1.00  7.68           C  
-ANISOU 2052  CG  LEU A 308      919    958   1041     41     82   -168       C  
-ATOM   2053  CD1 LEU A 308      34.886  19.114   0.754  1.00  9.04           C  
-ANISOU 2053  CD1 LEU A 308     1067   1035   1329    202     20   -152       C  
-ATOM   2054  CD2 LEU A 308      35.368  16.778   1.413  1.00  8.18           C  
-ANISOU 2054  CD2 LEU A 308      845   1030   1232    -27     26   -127       C  
-ATOM   2055  N   ARG A 309      40.132  17.898   2.636  1.00  5.98           N  
-ANISOU 2055  N   ARG A 309      807    696    765    -60    151   -174       N  
-ATOM   2056  CA  ARG A 309      41.481  18.443   2.547  1.00  6.61           C  
-ANISOU 2056  CA  ARG A 309      873    827    810    -83     94   -216       C  
-ATOM   2057  C   ARG A 309      41.906  18.560   1.114  1.00  7.19           C  
-ANISOU 2057  C   ARG A 309      957    889    885   -181    131   -220       C  
-ATOM   2058  O   ARG A 309      41.480  17.790   0.243  1.00  8.20           O  
-ANISOU 2058  O   ARG A 309     1059   1144    911   -337    222   -407       O  
-ATOM   2059  CB  ARG A 309      42.493  17.607   3.309  1.00  7.76           C  
-ANISOU 2059  CB  ARG A 309      907    993   1048    -61    124   -192       C  
-ATOM   2060  CG  ARG A 309      42.378  17.774   4.797  1.00  8.42           C  
-ANISOU 2060  CG  ARG A 309     1038   1090   1070     20    -26   -150       C  
-ATOM   2061  CD  ARG A 309      43.117  16.728   5.552  1.00 11.67           C  
-ANISOU 2061  CD  ARG A 309     1737   1481   1213    158      1   -330       C  
-ATOM   2062  NE  ARG A 309      43.581  17.189   6.854  1.00 10.69           N  
-ANISOU 2062  NE  ARG A 309     1510   1323   1226     80     55    -77       N  
-ATOM   2063  CZ  ARG A 309      43.845  16.373   7.856  1.00  9.43           C  
-ANISOU 2063  CZ  ARG A 309     1289   1012   1281    184    135    -89       C  
-ATOM   2064  NH1 ARG A 309      43.625  15.061   7.751  1.00 11.12           N  
-ANISOU 2064  NH1 ARG A 309     1469   1252   1502    -18    175   -165       N  
-ATOM   2065  NH2 ARG A 309      44.341  16.863   8.970  1.00  9.97           N  
-ANISOU 2065  NH2 ARG A 309     1390   1106   1289     22     78    -97       N  
-ATOM   2066  N   CYS A 310      42.770  19.524   0.828  1.00  7.77           N  
-ANISOU 2066  N   CYS A 310      903   1046   1003   -195    144   -203       N  
-ATOM   2067  CA  CYS A 310      43.314  19.567  -0.523  1.00  8.99           C  
-ANISOU 2067  CA  CYS A 310     1041   1195   1178   -147    222   -124       C  
-ATOM   2068  C   CYS A 310      44.339  18.455  -0.711  1.00  9.35           C  
-ANISOU 2068  C   CYS A 310     1097   1235   1218   -106    213   -139       C  
-ATOM   2069  O   CYS A 310      45.044  18.057   0.208  1.00  9.61           O  
-ANISOU 2069  O   CYS A 310     1144   1295   1212     32    415   -268       O  
-ATOM   2070  CB  CYS A 310      43.857  20.929  -0.918  1.00 10.03           C  
-ANISOU 2070  CB  CYS A 310     1125   1254   1431   -148    349    -75       C  
-ATOM   2071  SG  CYS A 310      45.369  21.434  -0.112  1.00 11.95           S  
-ANISOU 2071  SG  CYS A 310     1529   1428   1582   -198    264   -290       S  
-ATOM   2072  N   SER A 311      44.400  17.953  -1.933  1.00 10.32           N  
-ANISOU 2072  N   SER A 311     1274   1380   1266   -102    143   -204       N  
-ATOM   2073  CA  SER A 311      45.300  16.868  -2.266  1.00 11.85           C  
-ANISOU 2073  CA  SER A 311     1534   1567   1400     13     76   -245       C  
-ATOM   2074  C   SER A 311      46.750  17.269  -2.058  1.00 11.66           C  
-ANISOU 2074  C   SER A 311     1530   1565   1334     77    145   -320       C  
-ATOM   2075  O   SER A 311      47.546  16.462  -1.609  1.00 12.98           O  
-ANISOU 2075  O   SER A 311     1654   1729   1545    183    139   -502       O  
-ATOM   2076  CB  SER A 311      45.065  16.404  -3.709  1.00 12.27           C  
-ANISOU 2076  CB  SER A 311     1654   1588   1418    -59     50   -297       C  
-ATOM   2077  OG  SER A 311      45.466  17.394  -4.643  1.00 16.04           O  
-ANISOU 2077  OG  SER A 311     2340   2212   1541     45     62   -368       O  
-ATOM   2078  N   SER A 312      47.073  18.521  -2.352  1.00 12.23           N  
-ANISOU 2078  N   SER A 312     1457   1748   1441     49    187   -243       N  
-ATOM   2079  CA  SER A 312      48.435  19.024  -2.196  1.00 13.57           C  
-ANISOU 2079  CA  SER A 312     1621   1845   1688     -5    111   -191       C  
-ATOM   2080  C   SER A 312      48.900  18.887  -0.744  1.00 12.78           C  
-ANISOU 2080  C   SER A 312     1442   1772   1641     25     93   -280       C  
-ATOM   2081  O   SER A 312      50.044  18.513  -0.483  1.00 14.18           O  
-ANISOU 2081  O   SER A 312     1457   2023   1905     27     23   -469       O  
-ATOM   2082  CB  SER A 312      48.512  20.482  -2.665  1.00 14.03           C  
-ANISOU 2082  CB  SER A 312     1693   1921   1714   -106    112   -114       C  
-ATOM   2083  OG  SER A 312      48.261  20.581  -4.059  1.00 18.53           O  
-ANISOU 2083  OG  SER A 312     2285   2419   2337   -165    154    -13       O  
-ATOM   2084  N   PHE A 313      48.006  19.197   0.198  1.00 12.15           N  
-ANISOU 2084  N   PHE A 313     1458   1664   1491     22     62   -372       N  
-ATOM   2085  CA  PHE A 313      48.311  19.067   1.617  1.00 12.15           C  
-ANISOU 2085  CA  PHE A 313     1537   1541   1537     65     -4   -271       C  
-ATOM   2086  C   PHE A 313      48.464  17.610   2.025  1.00 12.90           C  
-ANISOU 2086  C   PHE A 313     1628   1645   1626    176    -14   -278       C  
-ATOM   2087  O   PHE A 313      49.384  17.264   2.757  1.00 13.39           O  
-ANISOU 2087  O   PHE A 313     1850   1563   1672    439    -47   -429       O  
-ATOM   2088  CB  PHE A 313      47.228  19.736   2.465  1.00 11.67           C  
-ANISOU 2088  CB  PHE A 313     1508   1444   1479    160    -43   -327       C  
-ATOM   2089  CG  PHE A 313      47.461  19.608   3.946  1.00 11.86           C  
-ANISOU 2089  CG  PHE A 313     1459   1552   1494    251   -178   -303       C  
-ATOM   2090  CD1 PHE A 313      48.280  20.508   4.614  1.00 13.24           C  
-ANISOU 2090  CD1 PHE A 313     2056   1296   1678    299   -307   -354       C  
-ATOM   2091  CD2 PHE A 313      46.865  18.594   4.661  1.00 12.34           C  
-ANISOU 2091  CD2 PHE A 313     1542   1726   1421    341   -149   -342       C  
-ATOM   2092  CE1 PHE A 313      48.513  20.373   5.976  1.00 14.12           C  
-ANISOU 2092  CE1 PHE A 313     2008   1601   1756    194   -358   -421       C  
-ATOM   2093  CE2 PHE A 313      47.089  18.456   6.020  1.00 13.24           C  
-ANISOU 2093  CE2 PHE A 313     1587   1752   1689    305    -50   -142       C  
-ATOM   2094  CZ  PHE A 313      47.902  19.359   6.681  1.00 14.42           C  
-ANISOU 2094  CZ  PHE A 313     1947   1899   1633    341   -207   -233       C  
-HETATM 2095  N   MSE A 314      47.546  16.767   1.565  1.00 14.30           N  
-ANISOU 2095  N   MSE A 314     1894   1740   1797     96      7   -207       N  
-HETATM 2096  CA  MSE A 314      47.574  15.344   1.906  1.00 17.04           C  
-ANISOU 2096  CA  MSE A 314     2258   2058   2159     98     -1   -125       C  
-HETATM 2097  C   MSE A 314      48.876  14.697   1.427  1.00 18.17           C  
-ANISOU 2097  C   MSE A 314     2373   2169   2361    104    -47   -110       C  
-HETATM 2098  O   MSE A 314      49.415  13.826   2.101  1.00 19.59           O  
-ANISOU 2098  O   MSE A 314     2667   2301   2474    258   -150   -133       O  
-HETATM 2099  CB  MSE A 314      46.334  14.601   1.354  1.00 17.98           C  
-ANISOU 2099  CB  MSE A 314     2364   2138   2328     63     -1   -119       C  
-HETATM 2100  CG  MSE A 314      44.962  15.138   1.866  1.00 22.32           C  
-ANISOU 2100  CG  MSE A 314     2829   2681   2968    -53     59   -131       C  
-HETATM 2101 SE  AMSE A 314      43.366  14.034   1.742  0.50 25.64          SE  
-ANISOU 2101 SE  AMSE A 314     3149   3024   3566   -111     -2   -185      SE  
-HETATM 2102 SE  BMSE A 314      45.570  14.850   3.710  0.50 33.86          SE  
-ANISOU 2102 SE  BMSE A 314     4508   4213   4142     76    207     61      SE  
-HETATM 2103  CE AMSE A 314      42.742  14.682   0.005  0.50 26.97           C  
-ANISOU 2103  CE AMSE A 314     3350   3394   3502     39    -10    -76       C  
-HETATM 2104  CE BMSE A 314      41.560  14.056   2.331  0.50 28.88           C  
-ANISOU 2104  CE BMSE A 314     3632   3690   3651    -21    182     17       C  
-ATOM   2105  N   GLU A 315      49.404  15.167   0.301  1.00 18.78           N  
-ANISOU 2105  N   GLU A 315     2448   2252   2436    158    -31   -141       N  
-ATOM   2106  CA  GLU A 315      50.629  14.623  -0.282  1.00 20.66           C  
-ANISOU 2106  CA  GLU A 315     2599   2570   2680     92      4    -82       C  
-ATOM   2107  C   GLU A 315      51.880  14.980   0.523  1.00 21.30           C  
-ANISOU 2107  C   GLU A 315     2641   2658   2791    116      0   -120       C  
-ATOM   2108  O   GLU A 315      52.905  14.318   0.386  1.00 22.18           O  
-ANISOU 2108  O   GLU A 315     2650   2752   3024    272    -17   -127       O  
-ATOM   2109  CB  GLU A 315      50.796  15.124  -1.715  1.00 20.60           C  
-ANISOU 2109  CB  GLU A 315     2568   2588   2668    105     40   -100       C  
-ATOM   2110  CG  GLU A 315      49.827  14.509  -2.714  1.00 23.14           C  
-ANISOU 2110  CG  GLU A 315     2931   2910   2949     75     70    -65       C  
-ATOM   2111  CD  GLU A 315      49.696  15.322  -3.992  1.00 26.97           C  
-ANISOU 2111  CD  GLU A 315     3414   3437   3396     -7     85    -55       C  
-ATOM   2112  OE1 GLU A 315      50.562  16.189  -4.251  1.00 29.88           O  
-ANISOU 2112  OE1 GLU A 315     3859   3805   3686   -148    165     34       O  
-ATOM   2113  OE2 GLU A 315      48.725  15.094  -4.744  1.00 30.02           O  
-ANISOU 2113  OE2 GLU A 315     3830   3943   3633     49    127    -90       O  
-ATOM   2114  N   LEU A 316      51.812  16.028   1.343  1.00 22.13           N  
-ANISOU 2114  N   LEU A 316     2742   2802   2864     86    -37    -89       N  
-ATOM   2115  CA  LEU A 316      52.936  16.402   2.205  1.00 22.92           C  
-ANISOU 2115  CA  LEU A 316     2860   2897   2949     24    -21    -58       C  
-ATOM   2116  C   LEU A 316      53.189  15.335   3.270  1.00 23.60           C  
-ANISOU 2116  C   LEU A 316     2931   2973   3061      2    -20    -27       C  
-ATOM   2117  O   LEU A 316      52.284  14.591   3.657  1.00 25.02           O  
-ANISOU 2117  O   LEU A 316     3079   3150   3274     18    -30    -14       O  
-ATOM   2118  CB  LEU A 316      52.680  17.749   2.881  1.00 22.93           C  
-ANISOU 2118  CB  LEU A 316     2861   2935   2916     -1    -53    -90       C  
-ATOM   2119  CG  LEU A 316      52.494  18.953   1.961  1.00 22.56           C  
-ANISOU 2119  CG  LEU A 316     2833   2867   2872      3     17   -110       C  
-ATOM   2120  CD1 LEU A 316      52.050  20.171   2.774  1.00 22.84           C  
-ANISOU 2120  CD1 LEU A 316     2924   2957   2797    -30    -80   -139       C  
-ATOM   2121  CD2 LEU A 316      53.762  19.249   1.167  1.00 22.88           C  
-ANISOU 2121  CD2 LEU A 316     2901   2938   2854     28     11   -101       C  
-TER    2122      LEU A 316                                                      
-HETATM 2123 MG    MG A 502      45.408  19.600  12.379  1.00  5.17          MG  
-ANISOU 2123 MG    MG A 502      683    555    724     49     -8    -33      MG  
-HETATM 2124  PG  ATP A 501      46.034  17.442  14.649  1.00  8.07           P  
-ANISOU 2124  PG  ATP A 501     1049    858   1156    103   -185     10       P  
-HETATM 2125  O1G ATP A 501      46.554  18.251  13.486  1.00  6.46           O  
-ANISOU 2125  O1G ATP A 501      841    780    833    141    -77    -20       O  
-HETATM 2126  O2G ATP A 501      47.012  16.440  15.214  1.00  9.86           O  
-ANISOU 2126  O2G ATP A 501     1237    949   1559    287   -271    142       O  
-HETATM 2127  O3G ATP A 501      45.415  18.289  15.759  1.00  9.14           O  
-ANISOU 2127  O3G ATP A 501     1443    976   1050    128     34    -44       O  
-HETATM 2128  PB  ATP A 501      44.166  16.669  12.640  1.00  6.53           P  
-ANISOU 2128  PB  ATP A 501      865    579   1035     51    -49    -22       P  
-HETATM 2129  O1B ATP A 501      44.846  15.767  11.696  1.00  8.60           O  
-ANISOU 2129  O1B ATP A 501     1217    670   1381    142    -44   -222       O  
-HETATM 2130  O2B ATP A 501      44.015  18.092  12.214  1.00  5.78           O  
-ANISOU 2130  O2B ATP A 501      796    521    879     44    -67    -30       O  
-HETATM 2131  O3B ATP A 501      44.807  16.562  14.092  1.00  7.50           O  
-ANISOU 2131  O3B ATP A 501     1215    778    855      0   -149    143       O  
-HETATM 2132  PA  ATP A 501      41.441  16.004  12.024  1.00  6.54           P  
-ANISOU 2132  PA  ATP A 501      979    589    915    -10   -107   -103       P  
-HETATM 2133  O1A ATP A 501      41.868  15.977  10.607  1.00  8.18           O  
-ANISOU 2133  O1A ATP A 501     1081   1121    905   -142   -154   -199       O  
-HETATM 2134  O2A ATP A 501      40.573  14.911  12.597  1.00  7.34           O  
-ANISOU 2134  O2A ATP A 501     1001    528   1259    -15    -22    -31       O  
-HETATM 2135  O3A ATP A 501      42.720  16.073  13.004  1.00  6.94           O  
-ANISOU 2135  O3A ATP A 501     1019    658    958    -43    -81     52       O  
-HETATM 2136  O5' ATP A 501      40.761  17.421  12.230  1.00  6.65           O  
-ANISOU 2136  O5' ATP A 501     1078    581    868     88   -113    -12       O  
-HETATM 2137  C5' ATP A 501      40.228  17.831  13.474  1.00  6.42           C  
-ANISOU 2137  C5' ATP A 501      807    712    917    -12    -29      5       C  
-HETATM 2138  C4' ATP A 501      41.034  18.978  14.030  1.00  5.20           C  
-ANISOU 2138  C4' ATP A 501      744    524    707    -14     70    -29       C  
-HETATM 2139  O4' ATP A 501      41.042  20.083  13.138  1.00  4.96           O  
-ANISOU 2139  O4' ATP A 501      755    401    727     56     46    -22       O  
-HETATM 2140  C3' ATP A 501      40.382  19.568  15.268  1.00  5.52           C  
-ANISOU 2140  C3' ATP A 501      830    602    665     66    100     63       C  
-HETATM 2141  O3' ATP A 501      40.575  18.803  16.426  1.00  7.48           O  
-ANISOU 2141  O3' ATP A 501     1253    818    768    122    105     91       O  
-HETATM 2142  C2' ATP A 501      40.973  20.967  15.342  1.00  4.80           C  
-ANISOU 2142  C2' ATP A 501      653    589    581    121     53    -44       C  
-HETATM 2143  O2' ATP A 501      42.117  20.993  16.172  1.00  6.19           O  
-ANISOU 2143  O2' ATP A 501      800    944    608     84    -83     32       O  
-HETATM 2144  C1' ATP A 501      41.343  21.265  13.892  1.00  4.22           C  
-ANISOU 2144  C1' ATP A 501      601    442    560     93     58    -77       C  
-HETATM 2145  N9  ATP A 501      40.602  22.354  13.240  1.00  3.78           N  
-ANISOU 2145  N9  ATP A 501      361    535    537     67     30     -5       N  
-HETATM 2146  C8  ATP A 501      41.171  23.310  12.442  1.00  4.18           C  
-ANISOU 2146  C8  ATP A 501      562    558    468    -99     72     -5       C  
-HETATM 2147  N7  ATP A 501      40.249  24.145  11.942  1.00  4.47           N  
-ANISOU 2147  N7  ATP A 501      576    605    515    -10     48     -5       N  
-HETATM 2148  C5  ATP A 501      39.058  23.679  12.418  1.00  3.65           C  
-ANISOU 2148  C5  ATP A 501      505    444    435     33     55    -43       C  
-HETATM 2149  C6  ATP A 501      37.744  24.121  12.264  1.00  4.22           C  
-ANISOU 2149  C6  ATP A 501      607    350    644    120     -7      1       C  
-HETATM 2150  N6  ATP A 501      37.382  25.103  11.430  1.00  5.27           N  
-ANISOU 2150  N6  ATP A 501      745    524    732    137     -9    -94       N  
-HETATM 2151  N1  ATP A 501      36.760  23.458  12.935  1.00  4.95           N  
-ANISOU 2151  N1  ATP A 501      520    746    613    -63    110   -121       N  
-HETATM 2152  C2  ATP A 501      37.057  22.401  13.740  1.00  4.70           C  
-ANISOU 2152  C2  ATP A 501      624    581    579    -41    -22      1       C  
-HETATM 2153  N3  ATP A 501      38.297  21.903  13.909  1.00  4.79           N  
-ANISOU 2153  N3  ATP A 501      667    555    596    -55     83    -64       N  
-HETATM 2154  C4  ATP A 501      39.267  22.569  13.244  1.00  3.29           C  
-ANISOU 2154  C4  ATP A 501      514    379    354    -22     56    -29       C  
-HETATM 2155  O   HOH A 503      44.809  17.970  37.617  1.00 36.08           O  
-ANISOU 2155  O   HOH A 503     4386   5537   3785   -520   -992  -1082       O  
-HETATM 2156  O   HOH A 504      42.954  19.170  36.304  1.00 24.50           O  
-ANISOU 2156  O   HOH A 504     2833   3518   2958     -2   -622  -1395       O  
-HETATM 2157  O   HOH A 505      40.660  20.162  36.149  1.00 27.10           O  
-ANISOU 2157  O   HOH A 505     3805   1890   4602   -257     16    196       O  
-HETATM 2158  O   HOH A 506      44.237  20.691  37.847  1.00 31.69           O  
-ANISOU 2158  O   HOH A 506     3809   4155   4075    198   -499    958       O  
-HETATM 2159  O   HOH A 507      17.460   9.609   1.448  1.00 34.71           O  
-ANISOU 2159  O   HOH A 507     4608   4863   3714   -192   -175   -460       O  
-HETATM 2160  O   HOH A 508      33.710  21.548  35.755  1.00 34.55           O  
-ANISOU 2160  O   HOH A 508     5177   5332   2618    160   -225    101       O  
-HETATM 2161  O   HOH A 509      58.096  33.599  10.856  1.00 10.13           O  
-ANISOU 2161  O   HOH A 509     1082   1042   1723   -139   -196    -17       O  
-HETATM 2162  O   HOH A 510      55.267  27.929  14.039  1.00  7.63           O  
-ANISOU 2162  O   HOH A 510      953    759   1183    -28     38    198       O  
-HETATM 2163  O   HOH A 511      41.922  35.290  18.063  1.00  6.88           O  
-ANISOU 2163  O   HOH A 511      938    678    996    199    -67    -96       O  
-HETATM 2164  O   HOH A 512      58.073  34.302  13.567  1.00  8.10           O  
-ANISOU 2164  O   HOH A 512      801    973   1303    -96     11    107       O  
-HETATM 2165  O   HOH A 513      50.287  27.048  12.279  1.00  8.03           O  
-ANISOU 2165  O   HOH A 513      825    826   1398    -48    156   -300       O  
-HETATM 2166  O   HOH A 514      46.968  20.960  12.454  1.00  5.94           O  
-ANISOU 2166  O   HOH A 514      726    663    867      7     40    -61       O  
-HETATM 2167  O   HOH A 515      35.931  20.580  24.045  1.00 12.46           O  
-ANISOU 2167  O   HOH A 515     1207   1404   2122    -92   -279    833       O  
-HETATM 2168  O   HOH A 516      27.187  24.141  16.304  1.00  7.65           O  
-ANISOU 2168  O   HOH A 516      820   1054   1031    138    -44   -167       O  
-HETATM 2169  O   HOH A 517      39.455  21.182  24.948  1.00  8.14           O  
-ANISOU 2169  O   HOH A 517     1202   1000    890    211     40    119       O  
-HETATM 2170  O   HOH A 518      53.280  36.276  18.496  1.00  7.92           O  
-ANISOU 2170  O   HOH A 518     1150    917    940   -141   -136   -144       O  
-HETATM 2171  O   HOH A 519      61.158  36.077  18.867  1.00  8.92           O  
-ANISOU 2171  O   HOH A 519     1027   1075   1285   -151   -112    101       O  
-HETATM 2172  O   HOH A 520      46.186  19.099  10.482  1.00  6.57           O  
-ANISOU 2172  O   HOH A 520      850    760    883     81    101   -233       O  
-HETATM 2173  O   HOH A 521      30.077  26.561  18.558  1.00  6.94           O  
-ANISOU 2173  O   HOH A 521      729    873   1032     20     12     -4       O  
-HETATM 2174  O   HOH A 522      33.420  13.556  11.668  1.00  7.95           O  
-ANISOU 2174  O   HOH A 522      935    884   1199    134      3     34       O  
-HETATM 2175  O   HOH A 523      27.466  24.688  13.601  1.00  7.89           O  
-ANISOU 2175  O   HOH A 523      897    962   1136    112   -110   -166       O  
-HETATM 2176  O   HOH A 524      57.172  45.969   2.224  1.00 14.78           O  
-ANISOU 2176  O   HOH A 524     1595   1560   2460   -463    604    -55       O  
-HETATM 2177  O   HOH A 525      52.082  29.977   9.907  1.00  6.93           O  
-ANISOU 2177  O   HOH A 525      738   1150    742    -23     52    135       O  
-HETATM 2178  O   HOH A 526      35.850  39.285  16.890  1.00  8.23           O  
-ANISOU 2178  O   HOH A 526     1316    712   1095    172    -99    -30       O  
-HETATM 2179  O   HOH A 527      58.622  31.792  14.517  1.00  7.79           O  
-ANISOU 2179  O   HOH A 527      810   1088   1061   -137    -34    161       O  
-HETATM 2180  O   HOH A 528      44.239  21.032  11.319  1.00  5.59           O  
-ANISOU 2180  O   HOH A 528      709    588    824    106     79      4       O  
-HETATM 2181  O   HOH A 529      23.047  28.449  13.575  1.00  9.59           O  
-ANISOU 2181  O   HOH A 529      883   1043   1717    141     79   -216       O  
-HETATM 2182  O   HOH A 530      44.639  20.395  14.092  1.00  5.86           O  
-ANISOU 2182  O   HOH A 530      773    642    811     34     34    -69       O  
-HETATM 2183  O   HOH A 531      57.423  40.860  16.055  1.00 12.10           O  
-ANISOU 2183  O   HOH A 531     1638   1146   1813   -146    -51    -64       O  
-HETATM 2184  O   HOH A 532      42.580  35.536  20.672  1.00  9.97           O  
-ANISOU 2184  O   HOH A 532     1367   1589    833    600   -127   -187       O  
-HETATM 2185  O   HOH A 533      41.861  14.510  23.280  1.00 10.06           O  
-ANISOU 2185  O   HOH A 533     1393    924   1505    -87   -127    207       O  
-HETATM 2186  O   HOH A 534      58.410  35.573   9.030  1.00 12.96           O  
-ANISOU 2186  O   HOH A 534     2520   1235   1168   -389   -198    159       O  
-HETATM 2187  O   HOH A 535      37.675  41.407  29.946  1.00  9.02           O  
-ANISOU 2187  O   HOH A 535     1505    931    989    160   -126   -352       O  
-HETATM 2188  O   HOH A 536      46.386  19.244  17.947  1.00  9.72           O  
-ANISOU 2188  O   HOH A 536     1343    994   1355    324   -192   -326       O  
-HETATM 2189  O   HOH A 537      33.957  24.389  22.521  1.00  9.05           O  
-ANISOU 2189  O   HOH A 537     1055   1466    915     47    199    108       O  
-HETATM 2190  O   HOH A 538      51.195  26.221  30.174  1.00 11.66           O  
-ANISOU 2190  O   HOH A 538     2295   1123   1011    478   -380    181       O  
-HETATM 2191  O   HOH A 539      36.665  41.930  17.362  1.00 10.20           O  
-ANISOU 2191  O   HOH A 539     1563    923   1389    156   -358    -93       O  
-HETATM 2192  O   HOH A 540      32.690  24.707   9.752  1.00 11.68           O  
-ANISOU 2192  O   HOH A 540     2163    957   1317    146    643     -4       O  
-HETATM 2193  O   HOH A 541      46.038  26.111  32.387  1.00 11.65           O  
-ANISOU 2193  O   HOH A 541     2200   1246    977    631   -426   -152       O  
-HETATM 2194  O   HOH A 542      50.835  38.785  10.605  1.00 12.82           O  
-ANISOU 2194  O   HOH A 542     1363   1021   2485   -104   -227    655       O  
-HETATM 2195  O   HOH A 543      47.253  20.607  20.998  1.00  7.41           O  
-ANISOU 2195  O   HOH A 543     1112    846    856    286     47     69       O  
-HETATM 2196  O   HOH A 544      30.225  18.438  24.882  1.00 19.29           O  
-ANISOU 2196  O   HOH A 544     1980   2601   2748   -454    173    -19       O  
-HETATM 2197  O   HOH A 545      36.676  30.186   7.840  1.00  7.92           O  
-ANISOU 2197  O   HOH A 545     1054    730   1222    199     37   -161       O  
-HETATM 2198  O   HOH A 546      54.547  28.621  26.010  1.00 15.77           O  
-ANISOU 2198  O   HOH A 546     3622    966   1403   -336  -1290      0       O  
-HETATM 2199  O   HOH A 547      23.626  23.992  18.610  1.00 16.59           O  
-ANISOU 2199  O   HOH A 547     1590   1857   2854   -231    342  -1086       O  
-HETATM 2200  O   HOH A 548      24.281  21.253  22.644  1.00 16.66           O  
-ANISOU 2200  O   HOH A 548     2164   2535   1631  -1018    278   -129       O  
-HETATM 2201  O   HOH A 549      41.100  32.482  -0.400  1.00 18.61           O  
-ANISOU 2201  O   HOH A 549     2198   2334   2538    281   -632    745       O  
-HETATM 2202  O   HOH A 550      61.194  35.875   6.823  1.00 18.15           O  
-ANISOU 2202  O   HOH A 550     2126   2545   2223    568    135    331       O  
-HETATM 2203  O   HOH A 551      47.247  31.935   0.640  1.00  8.72           O  
-ANISOU 2203  O   HOH A 551     1243    955   1113   -130    180    167       O  
-HETATM 2204  O   HOH A 552      54.972  40.671  12.879  1.00 13.50           O  
-ANISOU 2204  O   HOH A 552     1909   1159   2060   -135    147    268       O  
-HETATM 2205  O   HOH A 553      41.617  37.400   3.258  1.00 19.94           O  
-ANISOU 2205  O   HOH A 553     2042   1800   3734   -157   -895    900       O  
-HETATM 2206  O   HOH A 554      32.150  10.566   7.405  1.00 10.95           O  
-ANISOU 2206  O   HOH A 554     1188   1779   1193   -186     88   -173       O  
-HETATM 2207  O   HOH A 555      22.644  18.077   0.346  1.00 11.45           O  
-ANISOU 2207  O   HOH A 555     1230   1717   1402   -234   -124   -349       O  
-HETATM 2208  O   HOH A 556      34.011  19.700  22.549  1.00 13.80           O  
-ANISOU 2208  O   HOH A 556     1514   1855   1872    290     52    342       O  
-HETATM 2209  O   HOH A 557      32.974  22.004  21.336  1.00 13.88           O  
-ANISOU 2209  O   HOH A 557     1691   1889   1693    262     53     94       O  
-HETATM 2210  O   HOH A 558      22.426  13.567  14.354  1.00 14.62           O  
-ANISOU 2210  O   HOH A 558     1608   1172   2773     58   1171     94       O  
-HETATM 2211  O   HOH A 559      57.043  40.605  11.123  1.00 13.42           O  
-ANISOU 2211  O   HOH A 559     1666   1380   2051   -368    152   -130       O  
-HETATM 2212  O   HOH A 560      22.846  26.497  21.560  1.00 14.76           O  
-ANISOU 2212  O   HOH A 560     1475   2446   1687    327    299     54       O  
-HETATM 2213  O   HOH A 561      54.395  19.248  11.019  1.00 18.56           O  
-ANISOU 2213  O   HOH A 561     2479   1470   3100    501    293   -315       O  
-HETATM 2214  O   HOH A 562      56.465  34.623  -2.914  1.00 21.44           O  
-ANISOU 2214  O   HOH A 562     2402   1969   3774   -240    981    -22       O  
-HETATM 2215  O   HOH A 563      58.853  41.091  13.616  1.00 17.00           O  
-ANISOU 2215  O   HOH A 563     2137   1617   2705   -196    -68    765       O  
-HETATM 2216  O   HOH A 564      23.463  14.234  -3.586  1.00 27.64           O  
-ANISOU 2216  O   HOH A 564     3858   3156   3488   -563   -689   -919       O  
-HETATM 2217  O   HOH A 565      50.519  43.542   3.186  1.00 10.59           O  
-ANISOU 2217  O   HOH A 565     1406   1059   1557   -150    226    197       O  
-HETATM 2218  O   HOH A 566      41.176  18.078  22.800  1.00 11.00           O  
-ANISOU 2218  O   HOH A 566     1154   1242   1782     49    -68    439       O  
-HETATM 2219  O   HOH A 567      50.137  37.387  27.918  1.00 14.39           O  
-ANISOU 2219  O   HOH A 567     1465   1238   2762    150   -560   -658       O  
-HETATM 2220  O   HOH A 568      32.412   8.815   9.471  1.00 18.92           O  
-ANISOU 2220  O   HOH A 568     3167   1530   2490   -102    286    382       O  
-HETATM 2221  O   HOH A 569      54.697  26.269  11.920  1.00 10.11           O  
-ANISOU 2221  O   HOH A 569     1257   1203   1381    138      4    137       O  
-HETATM 2222  O   HOH A 570      21.011   5.743  14.434  1.00 17.98           O  
-ANISOU 2222  O   HOH A 570     2634   2355   1841   -654   -468    384       O  
-HETATM 2223  O   HOH A 571      42.523  14.177  36.676  1.00 21.25           O  
-ANISOU 2223  O   HOH A 571     3558   2756   1758   1250    353    559       O  
-HETATM 2224  O   HOH A 572      44.619  35.597  17.453  1.00 15.59           O  
-ANISOU 2224  O   HOH A 572     1747    901   3275    176    669     15       O  
-HETATM 2225  O   HOH A 573      34.858  19.666  -3.099  1.00 19.19           O  
-ANISOU 2225  O   HOH A 573     1744   1864   3681   -122    608   -500       O  
-HETATM 2226  O   HOH A 574      41.914  21.004  23.799  1.00 14.88           O  
-ANISOU 2226  O   HOH A 574     1202   3598    853    415    134    244       O  
-HETATM 2227  O   HOH A 575      15.551  17.392  11.850  1.00 16.98           O  
-ANISOU 2227  O   HOH A 575     1992   1850   2609    505    -49    360       O  
-HETATM 2228  O   HOH A 576      63.838  30.155  29.191  1.00 13.60           O  
-ANISOU 2228  O   HOH A 576     1467   1378   2323    112   -458    -17       O  
-HETATM 2229  O   HOH A 577      58.559  24.907  18.682  1.00 13.04           O  
-ANISOU 2229  O   HOH A 577     2065   1317   1570    281   -279    302       O  
-HETATM 2230  O   HOH A 578      48.234  35.299   0.767  1.00 12.38           O  
-ANISOU 2230  O   HOH A 578     1541   1502   1659    -67     73     36       O  
-HETATM 2231  O   HOH A 579      38.917  10.599   7.947  1.00 14.83           O  
-ANISOU 2231  O   HOH A 579     1959   1975   1699   1090    -54     37       O  
-HETATM 2232  O   HOH A 580      38.565  32.821   0.778  1.00 20.24           O  
-ANISOU 2232  O   HOH A 580     2210   2202   3277     47   -556     59       O  
-HETATM 2233  O   HOH A 581      34.182  26.985  -4.302  1.00 25.09           O  
-ANISOU 2233  O   HOH A 581     4209   2850   2472    655    522    427       O  
-HETATM 2234  O   HOH A 582      19.844  17.925  -0.158  1.00 20.36           O  
-ANISOU 2234  O   HOH A 582     1920   3159   2656     69   -350   -621       O  
-HETATM 2235  O   HOH A 583      45.767  35.385   2.173  1.00  8.64           O  
-ANISOU 2235  O   HOH A 583     1221    960   1100    -47     -1    220       O  
-HETATM 2236  O   HOH A 584      50.558  38.912  22.088  1.00 14.41           O  
-ANISOU 2236  O   HOH A 584     2256   1582   1634    329    125     -6       O  
-HETATM 2237  O   HOH A 585      54.110  36.275  27.751  1.00 13.65           O  
-ANISOU 2237  O   HOH A 585     1093   2182   1910    190   -288   -540       O  
-HETATM 2238  O   HOH A 586      56.378  23.928  22.732  1.00 15.42           O  
-ANISOU 2238  O   HOH A 586     1811   2038   2007    644    -58    513       O  
-HETATM 2239  O   HOH A 587      40.913  12.345  11.835  1.00 19.22           O  
-ANISOU 2239  O   HOH A 587     3184   1606   2510    567    174   -372       O  
-HETATM 2240  O   HOH A 588      51.418  37.523  -6.861  1.00 20.80           O  
-ANISOU 2240  O   HOH A 588     2960   1955   2986   -123   -924    320       O  
-HETATM 2241  O   HOH A 589      52.668  40.646  11.267  1.00 25.28           O  
-ANISOU 2241  O   HOH A 589     2432   1558   5615   -323  -1253   -281       O  
-HETATM 2242  O   HOH A 590      29.085   2.121   3.477  1.00 34.85           O  
-ANISOU 2242  O   HOH A 590     4489   4023   4727   -504     68   -610       O  
-HETATM 2243  O   HOH A 591      39.038  31.613   7.222  1.00 11.20           O  
-ANISOU 2243  O   HOH A 591     1262    980   2012   -137     81    130       O  
-HETATM 2244  O   HOH A 592      35.693   8.400   6.469  1.00 16.24           O  
-ANISOU 2244  O   HOH A 592     1834   1312   3025    108   -217     41       O  
-HETATM 2245  O   HOH A 593      57.658  25.838  21.163  1.00 14.54           O  
-ANISOU 2245  O   HOH A 593     1409   1770   2342    190   -242   -273       O  
-HETATM 2246  O   HOH A 594      24.129   4.709   6.271  1.00 21.80           O  
-ANISOU 2246  O   HOH A 594     2581   1758   3942   -439    551   -652       O  
-HETATM 2247  O   HOH A 595      60.720  29.280  21.427  1.00 14.72           O  
-ANISOU 2247  O   HOH A 595     2608   1301   1682    152   -609    -62       O  
-HETATM 2248  O   HOH A 596      37.705  34.223   2.911  1.00 20.54           O  
-ANISOU 2248  O   HOH A 596     2249   2476   3078    463    -77    750       O  
-HETATM 2249  O   HOH A 597      58.920  33.175  -5.180  1.00 21.68           O  
-ANISOU 2249  O   HOH A 597     2110   1639   4487   -411    236   -895       O  
-HETATM 2250  O   HOH A 598      50.548  33.727   1.188  1.00  8.23           O  
-ANISOU 2250  O   HOH A 598     1166    840   1119     20     36    266       O  
-HETATM 2251  O   HOH A 599      40.630  15.011  20.904  1.00 17.50           O  
-ANISOU 2251  O   HOH A 599     2369   2643   1636    576   -617   -183       O  
-HETATM 2252  O   HOH A 600      25.216  35.475  13.354  1.00 17.39           O  
-ANISOU 2252  O   HOH A 600     2807   1752   2047     -5   -643    508       O  
-HETATM 2253  O   HOH A 601      48.564  17.177  23.417  1.00 15.79           O  
-ANISOU 2253  O   HOH A 601     1770   1653   2576   -105    -36   -108       O  
-HETATM 2254  O   HOH A 602      49.882  39.791  16.106  1.00 22.86           O  
-ANISOU 2254  O   HOH A 602     3765   1389   3531    341    486    394       O  
-HETATM 2255  O   HOH A 603      48.221  38.681  25.445  1.00 11.29           O  
-ANISOU 2255  O   HOH A 603     1067   1030   2190    -82   -140   -173       O  
-HETATM 2256  O   HOH A 604      21.741  20.625  -2.803  1.00 19.23           O  
-ANISOU 2256  O   HOH A 604     2083   3302   1922    -56   -193   -513       O  
-HETATM 2257  O   HOH A 605      63.949  36.354  18.812  1.00 14.82           O  
-ANISOU 2257  O   HOH A 605     1212   1955   2462   -194    128   -233       O  
-HETATM 2258  O   HOH A 606      40.519  17.316  38.462  1.00 27.41           O  
-ANISOU 2258  O   HOH A 606     4054   4021   2336   -341    630    274       O  
-HETATM 2259  O   HOH A 607      34.900  33.438   5.438  1.00 21.24           O  
-ANISOU 2259  O   HOH A 607     2459   2421   3188   -418    397   -125       O  
-HETATM 2260  O   HOH A 608      41.275  30.909  -2.808  1.00 20.87           O  
-ANISOU 2260  O   HOH A 608     3104   2138   2687    207  -1551    538       O  
-HETATM 2261  O   HOH A 609      28.469  33.924   8.205  1.00 24.25           O  
-ANISOU 2261  O   HOH A 609     3091   1743   4377    630  -1106    437       O  
-HETATM 2262  O   HOH A 610      52.526  27.199  10.436  1.00 13.00           O  
-ANISOU 2262  O   HOH A 610     1337   1231   2368   -238     80    351       O  
-HETATM 2263  O   HOH A 611      42.200  23.609   0.812  1.00  9.52           O  
-ANISOU 2263  O   HOH A 611     1482   1262    874    -84     94   -187       O  
-HETATM 2264  O   HOH A 612      27.656   9.319  12.658  1.00 15.04           O  
-ANISOU 2264  O   HOH A 612     1796   1022   2895    148    662    188       O  
-HETATM 2265  O   HOH A 613      18.902  24.272   9.246  1.00 16.07           O  
-ANISOU 2265  O   HOH A 613     1228   2242   2636    509    299    -71       O  
-HETATM 2266  O   HOH A 614      41.498  11.681   7.950  1.00 18.55           O  
-ANISOU 2266  O   HOH A 614     2128   1894   3024    583   -438  -1198       O  
-HETATM 2267  O   HOH A 615      22.478  28.245  23.673  1.00 20.84           O  
-ANISOU 2267  O   HOH A 615     3327   2663   1928   1121    -38   -398       O  
-HETATM 2268  O   HOH A 616      50.804  25.462   9.237  1.00 18.30           O  
-ANISOU 2268  O   HOH A 616     2426   2126   2399   -233    194      2       O  
-HETATM 2269  O   HOH A 617      45.489  42.127  25.458  1.00 20.80           O  
-ANISOU 2269  O   HOH A 617     2381   2655   2865    545   -472    -18       O  
-HETATM 2270  O   HOH A 618      41.148  12.471  20.013  1.00 15.50           O  
-ANISOU 2270  O   HOH A 618     2452   1763   1673    517   -596     68       O  
-HETATM 2271  O   HOH A 619      57.813  23.182  29.581  1.00 21.52           O  
-ANISOU 2271  O   HOH A 619     2242   3441   2490   1224    -73    707       O  
-HETATM 2272  O   HOH A 620      48.005  41.266  24.459  1.00 20.52           O  
-ANISOU 2272  O   HOH A 620     2262   1977   3557    173    252    397       O  
-HETATM 2273  O   HOH A 621      63.522  28.681  21.788  1.00 31.85           O  
-ANISOU 2273  O   HOH A 621     4407   2681   5012   1562     34    362       O  
-HETATM 2274  O   HOH A 622      59.384  27.350  22.636  1.00 18.47           O  
-ANISOU 2274  O   HOH A 622     2780   2503   1733   -424      5    -84       O  
-HETATM 2275  O   HOH A 623      49.347  37.793  17.857  1.00 12.90           O  
-ANISOU 2275  O   HOH A 623     2254    951   1696    259   -287    -79       O  
-HETATM 2276  O   HOH A 624      23.354  22.652  33.326  1.00 21.34           O  
-ANISOU 2276  O   HOH A 624     2904   2246   2955     66    557      0       O  
-HETATM 2277  O   HOH A 625      58.073  28.571   2.186  1.00 24.97           O  
-ANISOU 2277  O   HOH A 625     3488   2372   3627   -644   1911   -600       O  
-HETATM 2278  O   HOH A 626      27.350  30.709   0.276  1.00 20.33           O  
-ANISOU 2278  O   HOH A 626     2596   2773   2353    116   -345   1119       O  
-HETATM 2279  O   HOH A 627      51.412  38.126  19.580  1.00 12.82           O  
-ANISOU 2279  O   HOH A 627     1736   1509   1625    452    -35     48       O  
-HETATM 2280  O  AHOH A 628      45.236  31.575  33.709  0.60 15.73           O  
-ANISOU 2280  O  AHOH A 628     2052   2147   1776    140   -192   -109       O  
-HETATM 2281  O  BHOH A 628      46.573  32.468  33.347  0.40 15.50           O  
-ANISOU 2281  O  BHOH A 628     1783   1954   2151     50    -36    120       O  
-HETATM 2282  O   HOH A 629      25.636  34.399  10.900  1.00 25.32           O  
-ANISOU 2282  O   HOH A 629     4450   3090   2078   -986    -83   -248       O  
-HETATM 2283  O   HOH A 630      62.833  39.708  13.130  1.00 25.37           O  
-ANISOU 2283  O   HOH A 630     2155   4479   3006  -1271   -457    723       O  
-HETATM 2284  O   HOH A 631      31.595   6.284   8.704  1.00 20.83           O  
-ANISOU 2284  O   HOH A 631     3294   2376   2243   -245   -318    301       O  
-HETATM 2285  O   HOH A 632      48.053  40.062  21.879  1.00 25.67           O  
-ANISOU 2285  O   HOH A 632     1926   3901   3925    519   -132   -616       O  
-HETATM 2286  O   HOH A 633      45.209  12.625  21.087  1.00 18.80           O  
-ANISOU 2286  O   HOH A 633     2410   2375   2357   -301    722    921       O  
-HETATM 2287  O   HOH A 634      34.021  24.170  12.391  1.00 11.83           O  
-ANISOU 2287  O   HOH A 634     1203   1698   1592     -3    -27   -233       O  
-HETATM 2288  O   HOH A 635      41.173  42.595  22.660  1.00 13.25           O  
-ANISOU 2288  O   HOH A 635     1962   1443   1626     77   -471   -290       O  
-HETATM 2289  O   HOH A 636      15.796  21.601  20.036  1.00 26.90           O  
-ANISOU 2289  O   HOH A 636     2342   3749   4129    602    560    189       O  
-HETATM 2290  O   HOH A 637      32.596  42.014  30.052  1.00 20.53           O  
-ANISOU 2290  O   HOH A 637     2564   2137   3098     42    431   -557       O  
-HETATM 2291  O   HOH A 638      43.911  42.155  23.250  1.00 18.71           O  
-ANISOU 2291  O   HOH A 638     2115   2277   2715     93   -425   -486       O  
-HETATM 2292  O   HOH A 639      47.333  17.062  10.252  1.00 29.87           O  
-ANISOU 2292  O   HOH A 639     4133   3585   3629   1007   -487   -506       O  
-HETATM 2293  O  AHOH A 640      29.272  26.761  15.657  0.50  7.85           O  
-ANISOU 2293  O  AHOH A 640      804   1105   1071    212    -86     67       O  
-HETATM 2294  O  BHOH A 640      30.862  26.742  15.480  0.50 10.13           O  
-ANISOU 2294  O  BHOH A 640     1636   1302    909    -94    -35      0       O  
-HETATM 2295  O   HOH A 641      30.939  41.377  27.960  1.00 17.32           O  
-ANISOU 2295  O   HOH A 641     2391   2306   1881    458    277   -189       O  
-HETATM 2296  O   HOH A 642      37.258  36.211  12.221  1.00 22.48           O  
-ANISOU 2296  O   HOH A 642     4230   2168   2143    358    406    825       O  
-HETATM 2297  O   HOH A 643      31.171  43.189  23.268  1.00 16.97           O  
-ANISOU 2297  O   HOH A 643     2138   1616   2694    427    255   -569       O  
-HETATM 2298  O   HOH A 644      49.519  37.535   0.507  1.00 17.15           O  
-ANISOU 2298  O   HOH A 644     2751   1897   1866   -508     74   -249       O  
-HETATM 2299  O   HOH A 645      63.628  37.693  10.392  1.00 22.43           O  
-ANISOU 2299  O   HOH A 645     1483   3436   3603    -86    474    830       O  
-HETATM 2300  O   HOH A 646      42.725  13.444   5.559  1.00 21.59           O  
-ANISOU 2300  O   HOH A 646     3193   2713   2294  -1075    101   -816       O  
-HETATM 2301  O   HOH A 647      28.516  25.464  -3.798  1.00 23.97           O  
-ANISOU 2301  O   HOH A 647     5325   2131   1650    880    569    781       O  
-HETATM 2302  O   HOH A 648      18.203  15.182   3.312  1.00 15.79           O  
-ANISOU 2302  O   HOH A 648     1398   1979   2620    127    122     -5       O  
-HETATM 2303  O   HOH A 649      34.417  42.956  18.430  1.00 23.30           O  
-ANISOU 2303  O   HOH A 649     1768   2058   5026     41    341   -723       O  
-HETATM 2304  O   HOH A 650      44.203  13.536  10.204  1.00 22.30           O  
-ANISOU 2304  O   HOH A 650     4165   1561   2745    596  -1025   -369       O  
-HETATM 2305  O   HOH A 651      17.174  21.855   0.788  1.00 17.69           O  
-ANISOU 2305  O   HOH A 651     1430   3378   1914    554   -299    229       O  
-HETATM 2306  O   HOH A 652      47.673  33.742  -1.282  1.00 15.96           O  
-ANISOU 2306  O   HOH A 652     2534   1792   1738   -293    379    592       O  
-HETATM 2307  O   HOH A 653      18.650  38.285  26.150  1.00 14.48           O  
-ANISOU 2307  O   HOH A 653     1669   1722   2108    361   -346   -311       O  
-HETATM 2308  O   HOH A 654      44.798  34.387  33.192  1.00 19.47           O  
-ANISOU 2308  O   HOH A 654     2605   3301   1492   1159    -69   -109       O  
-HETATM 2309  O   HOH A 655      38.135  27.725  -3.627  1.00 26.97           O  
-ANISOU 2309  O   HOH A 655     4067   3176   3004    637   -355    155       O  
-HETATM 2310  O   HOH A 656      49.840  39.588  13.347  1.00 26.49           O  
-ANISOU 2310  O   HOH A 656     3803   3237   3025   -685   1057   -227       O  
-HETATM 2311  O   HOH A 657      26.347  32.915   6.934  1.00 20.73           O  
-ANISOU 2311  O   HOH A 657     2432   3554   1889   -892     10   -151       O  
-HETATM 2312  O   HOH A 658      54.753  21.452  25.809  1.00 18.87           O  
-ANISOU 2312  O   HOH A 658     3307   1444   2416   -356    191   -451       O  
-HETATM 2313  O   HOH A 659      20.730  29.028  12.395  1.00 24.49           O  
-ANISOU 2313  O   HOH A 659     2237   4067   3000    638    -14    366       O  
-HETATM 2314  O   HOH A 660      58.881  25.929  32.783  1.00 16.49           O  
-ANISOU 2314  O   HOH A 660     1753   2025   2485    139   -423   -452       O  
-HETATM 2315  O   HOH A 661      61.146  33.326   7.769  1.00 16.44           O  
-ANISOU 2315  O   HOH A 661     1539   2319   2387     39    -84    296       O  
-HETATM 2316  O   HOH A 662      56.836  38.379  27.574  1.00 21.42           O  
-ANISOU 2316  O   HOH A 662     4080   2069   1987    891    600   -298       O  
-HETATM 2317  O   HOH A 663      56.595  43.183   6.890  1.00 24.82           O  
-ANISOU 2317  O   HOH A 663     3859   3356   2214   1140    141   -610       O  
-HETATM 2318  O   HOH A 664      33.125  26.415  13.627  1.00 13.10           O  
-ANISOU 2318  O   HOH A 664     1605   1902   1470    192   -279   -167       O  
-HETATM 2319  O   HOH A 665      19.682  31.699  18.300  1.00 15.89           O  
-ANISOU 2319  O   HOH A 665     1108   3049   1878    177    329   -265       O  
-HETATM 2320  O   HOH A 666      64.236  24.813  26.283  1.00 32.00           O  
-ANISOU 2320  O   HOH A 666     3215   3793   5148    510   -442  -1294       O  
-HETATM 2321  O   HOH A 667      21.980  21.124  24.274  1.00 29.19           O  
-ANISOU 2321  O   HOH A 667     2987   4556   3548   -769    844   -782       O  
-HETATM 2322  O   HOH A 668      26.017   7.441   9.924  1.00 28.06           O  
-ANISOU 2322  O   HOH A 668     3660   4274   2725   1276    395    618       O  
-HETATM 2323  O   HOH A 669      30.036  26.457  13.081  1.00 16.05           O  
-ANISOU 2323  O   HOH A 669     1972   2029   2096    -48   -205   -123       O  
-HETATM 2324  O  AHOH A 670      22.489  32.559  21.370  0.50 24.12           O  
-ANISOU 2324  O  AHOH A 670     2864   3234   3065    -68     35   -127       O  
-HETATM 2325  O  BHOH A 670      22.322  34.197  20.774  0.50 27.00           O  
-ANISOU 2325  O  BHOH A 670     3206   3709   3344     39     15     29       O  
-HETATM 2326  O  AHOH A 671      17.607  24.331  14.881  0.50 28.87           O  
-ANISOU 2326  O  AHOH A 671     3749   3630   3587     34    -20     21       O  
-HETATM 2327  O  BHOH A 671      17.056  25.381  16.221  0.50 26.45           O  
-ANISOU 2327  O  BHOH A 671     3051   3333   3665    176   -158   -455       O  
-HETATM 2328  O   HOH A 672      64.124  25.889  23.919  1.00 33.33           O  
-ANISOU 2328  O   HOH A 672     3352   4636   4674   -750    702   -550       O  
-HETATM 2329  O   HOH A 673      59.251  40.295  26.609  1.00 30.10           O  
-ANISOU 2329  O   HOH A 673     3489   3975   3972    314   -111   -345       O  
-HETATM 2330  O   HOH A 674      58.463  40.260  23.701  1.00 27.18           O  
-ANISOU 2330  O   HOH A 674     5807   2163   2355    312    219    -42       O  
-HETATM 2331  O   HOH A 675      21.011  28.268  28.349  1.00 27.54           O  
-ANISOU 2331  O   HOH A 675     2673   2968   4823    750    -95   -296       O  
-HETATM 2332  O   HOH A 676      20.730  26.426  -0.372  1.00 27.92           O  
-ANISOU 2332  O   HOH A 676     2406   4334   3866   1639   -162   -497       O  
-HETATM 2333  O   HOH A 677      56.911  31.982  -2.357  1.00 28.02           O  
-ANISOU 2333  O   HOH A 677     3186   2080   5377     17   1615   -456       O  
-HETATM 2334  O   HOH A 678      55.340  45.362   5.976  1.00 22.41           O  
-ANISOU 2334  O   HOH A 678     3454   2337   2721    487   -468   -244       O  
-HETATM 2335  O   HOH A 679      59.155  31.943   9.051  1.00 14.23           O  
-ANISOU 2335  O   HOH A 679     1406   1808   2191    191   -199    581       O  
-HETATM 2336  O   HOH A 680      47.542  22.339  36.764  1.00 12.94           O  
-ANISOU 2336  O   HOH A 680     2532   1368   1013   -486   -210    259       O  
-HETATM 2337  O   HOH A 681      20.615  34.137  18.903  1.00 19.88           O  
-ANISOU 2337  O   HOH A 681     1854   2787   2911    161    694    207       O  
-HETATM 2338  O   HOH A 682      37.720  33.632   5.575  1.00 20.92           O  
-ANISOU 2338  O   HOH A 682     2234   2518   3194    643    132    156       O  
-HETATM 2339  O   HOH A 683      57.102  22.010  32.136  1.00 29.76           O  
-ANISOU 2339  O   HOH A 683     4106   3412   3789    652   -437   1029       O  
-HETATM 2340  O   HOH A 684      25.531   7.472  12.589  1.00 16.30           O  
-ANISOU 2340  O   HOH A 684     2239   1742   2210    162    695    191       O  
-HETATM 2341  O   HOH A 685      26.840  27.493  -3.381  1.00 26.93           O  
-ANISOU 2341  O   HOH A 685     4079   3155   2996   1327   -524    748       O  
-HETATM 2342  O   HOH A 686      47.265  25.724  38.339  1.00 38.02           O  
-ANISOU 2342  O   HOH A 686     4618   5516   4311   -234    328   -359       O  
-HETATM 2343  O   HOH A 687      48.345  19.414  34.684  1.00 23.50           O  
-ANISOU 2343  O   HOH A 687     3704   2209   3016    184   -210    769       O  
-HETATM 2344  O   HOH A 688      54.071  25.182  37.709  1.00 21.15           O  
-ANISOU 2344  O   HOH A 688     3177   3029   1828   -962   -470    308       O  
-HETATM 2345  O   HOH A 689      49.889  14.064  26.287  1.00 18.45           O  
-ANISOU 2345  O   HOH A 689     2167   2390   2454   -280   -297    667       O  
-HETATM 2346  O   HOH A 690      14.405  21.937   1.366  1.00 23.86           O  
-ANISOU 2346  O   HOH A 690     2053   4088   2925    749   -104   -315       O  
-HETATM 2347  O   HOH A 691      30.982  14.695  16.103  1.00 25.33           O  
-ANISOU 2347  O   HOH A 691     3608   2517   3500    688    549    903       O  
-HETATM 2348  O   HOH A 692      19.016  15.427   0.720  1.00 19.35           O  
-ANISOU 2348  O   HOH A 692     2239   2787   2323    128   -282   -405       O  
-HETATM 2349  O   HOH A 693      48.273  28.229  31.890  1.00 19.82           O  
-ANISOU 2349  O   HOH A 693     2291   3326   1912   1202   -177    338       O  
-HETATM 2350  O   HOH A 694      58.698  28.969  12.067  1.00 18.35           O  
-ANISOU 2350  O   HOH A 694     1729   2798   2444    655   -226   -336       O  
-HETATM 2351  O   HOH A 695      38.296  30.061  -2.574  1.00 27.20           O  
-ANISOU 2351  O   HOH A 695     4115   3485   2731    214   -411    418       O  
-HETATM 2352  O   HOH A 696      28.439  18.469  -4.005  1.00 24.19           O  
-ANISOU 2352  O   HOH A 696     2615   3177   3397    310   -243  -1128       O  
-HETATM 2353  O   HOH A 697      39.226  10.624  10.659  1.00 19.42           O  
-ANISOU 2353  O   HOH A 697     2611   2357   2408    444   -477    -48       O  
-HETATM 2354  O   HOH A 698      45.996  14.724  30.781  1.00 23.37           O  
-ANISOU 2354  O   HOH A 698     2787   3046   3046   -287   -275   -525       O  
-HETATM 2355  O   HOH A 699      43.794  40.190  30.677  1.00 22.71           O  
-ANISOU 2355  O   HOH A 699     3146   3354   2129    216   -557  -1294       O  
-HETATM 2356  O   HOH A 700      26.837  39.436  32.434  1.00 20.85           O  
-ANISOU 2356  O   HOH A 700     2233   3387   2302    222    215  -1130       O  
-HETATM 2357  O   HOH A 701      36.935  23.003  39.194  1.00 30.47           O  
-ANISOU 2357  O   HOH A 701     3528   4420   3629    -28    230    460       O  
-HETATM 2358  O   HOH A 702      49.563  20.012  16.335  1.00 24.31           O  
-ANISOU 2358  O   HOH A 702     2268   2944   4022   -153    635   -839       O  
-HETATM 2359  O   HOH A 703      45.680  38.737  32.268  1.00 28.30           O  
-ANISOU 2359  O   HOH A 703     3646   4333   2771    126   -648   -975       O  
-HETATM 2360  O   HOH A 704      24.758  27.869  -1.413  1.00 27.20           O  
-ANISOU 2360  O   HOH A 704     4705   3513   2115    443   -665    236       O  
-HETATM 2361  O   HOH A 705      36.976  12.371  18.083  1.00 18.84           O  
-ANISOU 2361  O   HOH A 705     3075   2040   2040   -593    184    205       O  
-HETATM 2362  O   HOH A 706      54.835  19.845  23.846  1.00 30.56           O  
-ANISOU 2362  O   HOH A 706     4479   3059   4071    141    220  -1152       O  
-HETATM 2363  O   HOH A 707      60.141  25.757  30.392  1.00 28.58           O  
-ANISOU 2363  O   HOH A 707     4348   3629   2881   -128    116    343       O  
-HETATM 2364  O   HOH A 708      37.908  38.702  13.871  1.00 26.16           O  
-ANISOU 2364  O   HOH A 708     3973   3242   2722   1067    488    849       O  
-HETATM 2365  O   HOH A 709      64.461  41.681   2.842  1.00 29.89           O  
-ANISOU 2365  O   HOH A 709     3295   4065   3993   -124    185    829       O  
-HETATM 2366  O   HOH A 710      27.225  32.919   4.451  1.00 25.83           O  
-ANISOU 2366  O   HOH A 710     3858   2534   3421   -710    568    300       O  
-HETATM 2367  O   HOH A 711      47.391  15.320  32.554  1.00 23.86           O  
-ANISOU 2367  O   HOH A 711     2417   2505   4142    433    163    -14       O  
-HETATM 2368  O   HOH A 712      58.586  26.092  37.492  1.00 25.83           O  
-ANISOU 2368  O   HOH A 712     3420   2445   3948    277   -493   1137       O  
-HETATM 2369  O   HOH A 713      19.289  21.747  -3.284  1.00 28.20           O  
-ANISOU 2369  O   HOH A 713     2635   4833   3244    985   -574   -266       O  
-HETATM 2370  O   HOH A 714      54.262  34.491  38.300  1.00 17.47           O  
-ANISOU 2370  O   HOH A 714     2304   2076   2257   -300    254   -511       O  
-HETATM 2371  O   HOH A 715      23.873  23.504  30.815  1.00 21.66           O  
-ANISOU 2371  O   HOH A 715     2463   2957   2809     68   1129    608       O  
-HETATM 2372  O   HOH A 716      49.305  31.884  33.285  1.00 24.04           O  
-ANISOU 2372  O   HOH A 716     2986   3706   2441    838   -554   -104       O  
-HETATM 2373  O   HOH A 717      55.037  21.472  21.959  1.00 29.72           O  
-ANISOU 2373  O   HOH A 717     2899   4965   3425   -227   -415     -9       O  
-HETATM 2374  O   HOH A 718      45.360  38.431  -0.899  1.00 28.68           O  
-ANISOU 2374  O   HOH A 718     4495   3142   3259   -965    -24    967       O  
-HETATM 2375  O   HOH A 719      52.996  46.711   2.634  1.00 21.45           O  
-ANISOU 2375  O   HOH A 719     2811   3210   2129    792    -16     80       O  
-HETATM 2376  O   HOH A 720      38.124  33.344   9.407  1.00 25.78           O  
-ANISOU 2376  O   HOH A 720     4268   2946   2580   1744    920    151       O  
-HETATM 2377  O   HOH A 721      38.540  17.840  -4.661  1.00 26.33           O  
-ANISOU 2377  O   HOH A 721     3169   3221   3614   -251   1133      7       O  
-HETATM 2378  O   HOH A 722      42.500  32.397  36.652  1.00 23.34           O  
-ANISOU 2378  O   HOH A 722     3446   3589   1832   -750   -139   -904       O  
-HETATM 2379  O   HOH A 723      31.666  16.565  34.423  1.00 26.59           O  
-ANISOU 2379  O   HOH A 723     4306   2954   2841    493   -364   1163       O  
-HETATM 2380  O   HOH A 724      59.933  18.041   6.476  1.00 19.19           O  
-ANISOU 2380  O   HOH A 724     1196   2488   3606    262   -277    -24       O  
-HETATM 2381  O   HOH A 725      58.583  25.029   4.963  1.00 20.68           O  
-ANISOU 2381  O   HOH A 725     2361   2658   2835    228   -148   -441       O  
-HETATM 2382  O   HOH A 726      28.495  16.946  26.485  1.00 25.96           O  
-ANISOU 2382  O   HOH A 726     3749   2623   3491   -247    711    -46       O  
-HETATM 2383  O   HOH A 727      32.421  30.060  33.667  1.00 20.06           O  
-ANISOU 2383  O   HOH A 727     1940   2772   2906    168    856   -106       O  
-HETATM 2384  O   HOH A 728      20.828  33.320   9.874  1.00 22.09           O  
-ANISOU 2384  O   HOH A 728     2820   3008   2562    476   -318    181       O  
-HETATM 2385  O   HOH A 729      34.245  32.100   0.086  1.00 23.39           O  
-ANISOU 2385  O   HOH A 729     2499   3268   3118   -580    129   1445       O  
-HETATM 2386  O   HOH A 730      33.020  37.179  33.039  1.00 21.61           O  
-ANISOU 2386  O   HOH A 730     3363   3568   1279    322      4      0       O  
-HETATM 2387  O   HOH A 731      60.541  29.003  14.312  1.00 18.50           O  
-ANISOU 2387  O   HOH A 731     1660   2165   3203    238    311   -553       O  
-HETATM 2388  O   HOH A 732      32.460  23.831  37.092  1.00 26.08           O  
-ANISOU 2388  O   HOH A 732     3880   3527   2501    196    217   1237       O  
-HETATM 2389  O   HOH A 733      30.490  34.241   6.083  1.00 22.97           O  
-ANISOU 2389  O   HOH A 733     3601   2136   2990    782    832    220       O  
-HETATM 2390  O   HOH A 734      63.621  40.064  20.176  1.00 27.38           O  
-ANISOU 2390  O   HOH A 734     2469   3791   4141   -780   -410    900       O  
-HETATM 2391  O   HOH A 735      29.836  32.254  35.655  1.00 22.35           O  
-ANISOU 2391  O   HOH A 735     2293   2987   3212    324   -265   -413       O  
-HETATM 2392  O   HOH A 736      33.922  13.330  14.307  1.00 22.64           O  
-ANISOU 2392  O   HOH A 736     3286   3733   1581  -1243   -562    498       O  
-HETATM 2393  O   HOH A 737      34.985  40.551  14.546  1.00 25.02           O  
-ANISOU 2393  O   HOH A 737     3942   2365   3199   -278   -430    520       O  
-HETATM 2394  O   HOH A 738      62.133  41.163   6.507  1.00 24.79           O  
-ANISOU 2394  O   HOH A 738     2458   3782   3177   -653    -91   -709       O  
-HETATM 2395  O   HOH A 739      59.202  30.715   1.121  1.00 18.06           O  
-ANISOU 2395  O   HOH A 739     3086   1484   2289   -547    772   -308       O  
-HETATM 2396  O   HOH A 740      35.784  15.348  30.002  1.00 26.35           O  
-ANISOU 2396  O   HOH A 740     2854   2914   4241   -199   -110    121       O  
-HETATM 2397  O   HOH A 741      53.234  28.474   1.913  1.00 23.22           O  
-ANISOU 2397  O   HOH A 741     2725   2848   3249   -161    -71     71       O  
-HETATM 2398  O   HOH A 742      49.988  33.364  -2.490  1.00 22.74           O  
-ANISOU 2398  O   HOH A 742     2626   2631   3380    -22    367   1317       O  
-HETATM 2399  O   HOH A 743      64.277  40.090  28.362  1.00 38.47           O  
-ANISOU 2399  O   HOH A 743     4745   5198   4672    656    -17   -292       O  
-HETATM 2400  O   HOH A 744      61.877  24.361   7.126  1.00 25.07           O  
-ANISOU 2400  O   HOH A 744     2549   3194   3781    229   -355   -119       O  
-HETATM 2401  O   HOH A 745      28.303   6.259   9.425  1.00 26.35           O  
-ANISOU 2401  O   HOH A 745     2709   3848   3452   -181    275   -401       O  
-HETATM 2402  O   HOH A 746      58.978  20.406   5.604  1.00 26.85           O  
-ANISOU 2402  O   HOH A 746     3295   3615   3291   1028    631    825       O  
-HETATM 2403  O   HOH A 747      49.984  34.014  -4.951  1.00 29.85           O  
-ANISOU 2403  O   HOH A 747     3932   3839   3567   -760   -502    -28       O  
-HETATM 2404  O   HOH A 748      41.775  37.609   0.853  1.00 34.36           O  
-ANISOU 2404  O   HOH A 748     4683   4621   3750    813   -409    668       O  
-HETATM 2405  O   HOH A 749      38.992  36.785   2.816  1.00 26.32           O  
-ANISOU 2405  O   HOH A 749     2609   3109   4281    549   -584    451       O  
-HETATM 2406  O   HOH A 750      41.695  21.224  -9.506  1.00 38.45           O  
-ANISOU 2406  O   HOH A 750     5396   4987   4223    316    200   -928       O  
-HETATM 2407  O   HOH A 751      24.250  12.874  16.797  1.00 23.01           O  
-ANISOU 2407  O   HOH A 751     2669   2423   3648    400    -19   -584       O  
-HETATM 2408  O   HOH A 752      47.586  30.232  33.423  1.00 25.93           O  
-ANISOU 2408  O   HOH A 752     3504   3591   2754    497   -406   -269       O  
-HETATM 2409  O   HOH A 753      60.099  29.568   9.777  1.00 24.60           O  
-ANISOU 2409  O   HOH A 753     2977   2412   3958    693   -301    427       O  
-HETATM 2410  O   HOH A 754      41.697  38.757  34.454  1.00 41.89           O  
-ANISOU 2410  O   HOH A 754     5361   5257   5296   -104    655   -711       O  
-HETATM 2411  O   HOH A 755      41.570  15.861  -2.620  1.00 27.88           O  
-ANISOU 2411  O   HOH A 755     2241   3712   4639  -1020    573    244       O  
-HETATM 2412  O   HOH A 756      27.937  16.046  -3.675  1.00 23.25           O  
-ANISOU 2412  O   HOH A 756     2761   3054   3018      6    197    205       O  
-HETATM 2413  O   HOH A 757      47.465  15.826  29.506  1.00 28.78           O  
-ANISOU 2413  O   HOH A 757     3952   4098   2886    304   -602   -839       O  
-HETATM 2414  O   HOH A 758      64.843  32.255  13.653  1.00 23.52           O  
-ANISOU 2414  O   HOH A 758     2579   3156   3198    356  -1106     23       O  
-HETATM 2415  O   HOH A 759      26.298  37.957  13.702  1.00 26.20           O  
-ANISOU 2415  O   HOH A 759     3530   2380   4042    229   -472    365       O  
-HETATM 2416  O   HOH A 760      17.857  19.682  -0.805  1.00 22.77           O  
-ANISOU 2416  O   HOH A 760     2111   3859   2681    576   -431   -377       O  
-HETATM 2417  O   HOH A 761      37.368  34.762  40.781  1.00 30.12           O  
-ANISOU 2417  O   HOH A 761     4330   4227   2887   -282   -269   -920       O  
-HETATM 2418  O   HOH A 762      23.338  20.995  -5.087  1.00 24.46           O  
-ANISOU 2418  O   HOH A 762     3074   4347   1871   -268      1   -503       O  
-HETATM 2419  O   HOH A 763      59.940  22.806   8.188  1.00 34.80           O  
-ANISOU 2419  O   HOH A 763     3524   4876   4822    402    453     41       O  
-HETATM 2420  O   HOH A 764      16.578   9.815  11.847  1.00 24.93           O  
-ANISOU 2420  O   HOH A 764     3025   2180   4265   -584   -112   -708       O  
-HETATM 2421  O   HOH A 765      22.263  34.136  16.218  1.00 34.15           O  
-ANISOU 2421  O   HOH A 765     3898   3731   5344    572    159    232       O  
-HETATM 2422  O   HOH A 766      25.845  21.397  -5.032  1.00 25.14           O  
-ANISOU 2422  O   HOH A 766     3488   3577   2484   -769   -263   -612       O  
-HETATM 2423  O   HOH A 767      55.518  29.857  38.995  1.00 22.35           O  
-ANISOU 2423  O   HOH A 767     4065   2527   1899   -239    286   -261       O  
-HETATM 2424  O   HOH A 768      27.125  19.316  -6.141  1.00 35.97           O  
-ANISOU 2424  O   HOH A 768     4999   4444   4221    363   -374   -291       O  
-HETATM 2425  O   HOH A 769      43.947  36.357   0.365  1.00 20.93           O  
-ANISOU 2425  O   HOH A 769     3374   1632   2945     17   -974    668       O  
-HETATM 2426  O   HOH A 770      38.154  20.936  -5.053  1.00 26.89           O  
-ANISOU 2426  O   HOH A 770     3498   3394   3324    545   -480  -1694       O  
-HETATM 2427  O   HOH A 771      60.218  43.344  13.167  1.00 30.43           O  
-ANISOU 2427  O   HOH A 771     5576   2192   3793  -1437   -125   -275       O  
-HETATM 2428  O   HOH A 772      45.477  20.873  -4.141  1.00 21.11           O  
-ANISOU 2428  O   HOH A 772     2458   3277   2285   -398    681   -498       O  
-HETATM 2429  O   HOH A 773      62.422  34.677   4.288  1.00 29.88           O  
-ANISOU 2429  O   HOH A 773     3690   2868   4793   1341   -480    777       O  
-HETATM 2430  O   HOH A 774      52.336  33.986  -5.563  1.00 32.42           O  
-ANISOU 2430  O   HOH A 774     3555   4586   4176  -1359   -194   -231       O  
-HETATM 2431  O   HOH A 775      59.494  38.909  31.323  1.00 26.99           O  
-ANISOU 2431  O   HOH A 775     4264   2791   3198  -1135   -491  -1034       O  
-HETATM 2432  O   HOH A 776      62.379  43.859   6.063  1.00 30.21           O  
-ANISOU 2432  O   HOH A 776     4384   3231   3862   -222    -50    -18       O  
-HETATM 2433  O   HOH A 777      46.353  15.691  17.755  1.00 18.73           O  
-ANISOU 2433  O   HOH A 777     2507   2409   2201    562    311    684       O  
-HETATM 2434  O   HOH A 778      27.416  41.759  31.248  1.00 36.13           O  
-ANISOU 2434  O   HOH A 778     4376   4295   5057    -22    561   -243       O  
-HETATM 2435  O   HOH A 779      55.453  41.674   8.977  1.00 24.32           O  
-ANISOU 2435  O   HOH A 779     3591   2805   2842    469     25    318       O  
-HETATM 2436  O   HOH A 780      21.548  24.154  29.857  1.00 26.95           O  
-ANISOU 2436  O   HOH A 780     2273   3590   4374    526    882    -15       O  
-HETATM 2437  O   HOH A 781      14.920  22.599   4.023  1.00 27.82           O  
-ANISOU 2437  O   HOH A 781     3847   3745   2976    243    526   -242       O  
-HETATM 2438  O   HOH A 782      54.557  35.293  -5.132  1.00 19.21           O  
-ANISOU 2438  O   HOH A 782     1895   1667   3735   -213   -263    473       O  
-HETATM 2439  O   HOH A 783      58.999  24.803   9.380  1.00 28.21           O  
-ANISOU 2439  O   HOH A 783     4007   2443   4266    550   -638   -238       O  
-HETATM 2440  O   HOH A 784      25.594  13.965  -0.956  1.00 25.95           O  
-ANISOU 2440  O   HOH A 784     1698   3252   4909    483    622   1204       O  
-HETATM 2441  O   HOH A 785      33.130  39.873  12.905  1.00 22.30           O  
-ANISOU 2441  O   HOH A 785     3590   1937   2944    195   -338    651       O  
-HETATM 2442  O   HOH A 786      46.508  23.982  35.592  1.00 26.51           O  
-ANISOU 2442  O   HOH A 786     3775   3583   2712    656   -898   -990       O  
-HETATM 2443  O   HOH A 787      20.015  10.033  18.784  1.00 41.97           O  
-ANISOU 2443  O   HOH A 787     5863   4711   5373    679    -36   -143       O  
-HETATM 2444  O   HOH A 788      65.337  35.582  11.445  1.00 28.47           O  
-ANISOU 2444  O   HOH A 788     3130   3354   4333    371    178   -368       O  
-HETATM 2445  O   HOH A 789      50.773  33.884  32.528  1.00 28.90           O  
-ANISOU 2445  O   HOH A 789     3185   4185   3608  -1111   -444   -391       O  
-HETATM 2446  O   HOH A 790      18.963  26.917   9.798  1.00 32.93           O  
-ANISOU 2446  O   HOH A 790     3395   3554   5562    814    541    335       O  
-HETATM 2447  O   HOH A 791      21.360  17.947  -2.683  1.00 26.31           O  
-ANISOU 2447  O   HOH A 791     2364   3228   4405   -328   -651   -383       O  
-HETATM 2448  O   HOH A 792      52.149  18.829  -2.280  1.00 29.50           O  
-ANISOU 2448  O   HOH A 792     2746   4730   3731    202   1389   -307       O  
-HETATM 2449  O   HOH A 793      23.201  13.758  34.548  1.00 24.88           O  
-ANISOU 2449  O   HOH A 793     3592   2048   3814    -84     99   1005       O  
-HETATM 2450  O   HOH A 794      31.074  18.446  -5.872  1.00 30.82           O  
-ANISOU 2450  O   HOH A 794     5207   3179   3321    -36    812   -979       O  
-HETATM 2451  O   HOH A 795      49.393  18.881  21.559  1.00 18.08           O  
-ANISOU 2451  O   HOH A 795     2369   1917   2581    541   -120    251       O  
-HETATM 2452  O   HOH A 796      26.158  19.330  23.125  1.00 33.65           O  
-ANISOU 2452  O   HOH A 796     3516   4414   4855    217   -433    600       O  
-HETATM 2453  O   HOH A 797      62.432  40.346  30.679  1.00 32.32           O  
-ANISOU 2453  O   HOH A 797     4578   4205   3496   -145    448    221       O  
-HETATM 2454  O   HOH A 798      53.254  34.203  32.637  1.00 22.99           O  
-ANISOU 2454  O   HOH A 798     3098   2604   3031    198    344    403       O  
-HETATM 2455  O   HOH A 799      51.351  35.238  30.262  1.00 33.31           O  
-ANISOU 2455  O   HOH A 799     4151   4418   4086   -105   -866    -53       O  
-HETATM 2456  O   HOH A 800      31.692  27.292  -3.136  1.00 25.93           O  
-ANISOU 2456  O   HOH A 800     3405   3975   2472    643    194    151       O  
-HETATM 2457  O   HOH A 801      65.919  38.064  19.933  1.00 31.34           O  
-ANISOU 2457  O   HOH A 801     3911   4144   3851   -588    415    183       O  
-HETATM 2458  O   HOH A 802      61.282  36.991  33.536  1.00 23.19           O  
-ANISOU 2458  O   HOH A 802     3605   1922   3283   -627   1339   -824       O  
-HETATM 2459  O   HOH A 803      21.001  31.596  15.983  1.00 20.96           O  
-ANISOU 2459  O   HOH A 803     2632   3092   2239   1187    409    199       O  
-HETATM 2460  O   HOH A 804      64.967  25.793  28.766  1.00 30.03           O  
-ANISOU 2460  O   HOH A 804     3863   2703   4841    815    131    -62       O  
-HETATM 2461  O   HOH A 805      17.424   9.605  19.297  1.00 25.75           O  
-ANISOU 2461  O   HOH A 805     3891   2298   3593    621   1073    877       O  
-HETATM 2462  O   HOH A 806      48.537  17.723  19.154  1.00 23.78           O  
-ANISOU 2462  O   HOH A 806     2715   3713   2606   1132   -412   -820       O  
-HETATM 2463  O   HOH A 807      59.005  26.367   2.642  1.00 39.96           O  
-ANISOU 2463  O   HOH A 807     5168   4982   5030   -110    321   -204       O  
-HETATM 2464  O   HOH A 808      52.418  20.423  16.445  1.00 23.36           O  
-ANISOU 2464  O   HOH A 808     3348   2623   2902  -1288    -35    747       O  
-HETATM 2465  O   HOH A 809      20.134   7.864   1.883  1.00 26.32           O  
-ANISOU 2465  O   HOH A 809     3086   3962   2952   -491   -293   -659       O  
-HETATM 2466  O   HOH A 810      28.793  20.057  23.248  1.00 32.70           O  
-ANISOU 2466  O   HOH A 810     3819   3628   4978   -524   -669    489       O  
-HETATM 2467  O   HOH A 811      28.109  41.722  28.785  1.00 28.51           O  
-ANISOU 2467  O   HOH A 811     3294   4012   3524    855    413    -14       O  
-HETATM 2468  O   HOH A 812      31.020  19.916  20.859  1.00 36.96           O  
-ANISOU 2468  O   HOH A 812     4566   4222   5256   1410   -656   -470       O  
-HETATM 2469  O   HOH A 813      21.519  21.315  29.052  1.00 27.49           O  
-ANISOU 2469  O   HOH A 813     3156   3773   3516   -470    612    718       O  
-HETATM 2470  O   HOH A 814      44.894  41.335  18.827  1.00 33.89           O  
-ANISOU 2470  O   HOH A 814     3335   3886   5654   -541     70    178       O  
-HETATM 2471  O   HOH A 815      45.670  26.252  -6.949  1.00 22.80           O  
-ANISOU 2471  O   HOH A 815     2860   3961   1840   -887     55    222       O  
-HETATM 2472  O   HOH A 816      16.906   8.287   9.104  1.00 35.60           O  
-ANISOU 2472  O   HOH A 816     4527   4423   4575    362   -153    656       O  
-HETATM 2473  O   HOH A 817      35.986  13.870  22.222  1.00 26.67           O  
-ANISOU 2473  O   HOH A 817     4796   2662   2674   -564    216    698       O  
-HETATM 2474  O   HOH A 818      63.923  29.068  14.798  1.00 31.22           O  
-ANISOU 2474  O   HOH A 818     2874   4678   4308    654    559   -401       O  
-HETATM 2475  O   HOH A 819      36.873  31.027  -0.212  1.00 24.08           O  
-ANISOU 2475  O   HOH A 819     2722   3362   3063   -238     77    415       O  
-HETATM 2476  O   HOH A 820      20.505  38.443  32.190  1.00 27.61           O  
-ANISOU 2476  O   HOH A 820     3055   4489   2946   -179   1034  -1047       O  
-HETATM 2477  O   HOH A 821      34.477  15.686  25.096  1.00 29.24           O  
-ANISOU 2477  O   HOH A 821     3201   3923   3983  -1079    807   -222       O  
-HETATM 2478  O   HOH A 822      44.201  19.755  -7.901  1.00 37.51           O  
-ANISOU 2478  O   HOH A 822     5005   5604   3643    463    769    -45       O  
-HETATM 2479  O   HOH A 823      20.024  31.300   6.044  1.00 25.36           O  
-ANISOU 2479  O   HOH A 823     3857   2397   3380    714   -406    522       O  
-HETATM 2480  O   HOH A 824      48.826  15.244  21.599  1.00 22.90           O  
-ANISOU 2480  O   HOH A 824     3170   2908   2620   -520   -462    390       O  
-HETATM 2481  O   HOH A 825      49.658  30.259  -6.068  1.00 37.11           O  
-ANISOU 2481  O   HOH A 825     5209   5251   3637    -29    754    -37       O  
-HETATM 2482  O   HOH A 826      57.991  22.973  24.726  1.00 26.70           O  
-ANISOU 2482  O   HOH A 826     3394   3333   3417    854   -478    421       O  
-HETATM 2483  O   HOH A 827      40.724  39.955  14.855  1.00 40.96           O  
-ANISOU 2483  O   HOH A 827     5645   4924   4993   -330    171   -541       O  
-HETATM 2484  O   HOH A 828      62.630  25.316  30.111  1.00 24.66           O  
-ANISOU 2484  O   HOH A 828     2997   2745   3625    922     13    532       O  
-HETATM 2485  O   HOH A 829      47.103  13.915  14.401  1.00 40.71           O  
-ANISOU 2485  O   HOH A 829     5663   4305   5497    838     70   -112       O  
-HETATM 2486  O   HOH A 830      45.268  37.884  16.123  1.00 25.94           O  
-ANISOU 2486  O   HOH A 830     3091   2755   4007     56    841   -949       O  
-HETATM 2487  O   HOH A 831      26.239   6.866  18.139  1.00 30.27           O  
-ANISOU 2487  O   HOH A 831     2759   3670   5069    908  -1195    573       O  
-HETATM 2488  O   HOH A 832      46.910  38.721  18.628  1.00 25.42           O  
-ANISOU 2488  O   HOH A 832     2606   3646   3406    982     26    -60       O  
-HETATM 2489  O   HOH A 833      25.857  18.066  25.503  1.00 33.70           O  
-ANISOU 2489  O   HOH A 833     4407   3467   4928    382   -323   -478       O  
-HETATM 2490  O   HOH A 834      51.352  17.788  11.298  1.00 35.60           O  
-ANISOU 2490  O   HOH A 834     4642   3142   5740    234   -305   -100       O  
-HETATM 2491  O   HOH A 835      49.381  31.327  35.941  1.00 27.09           O  
-ANISOU 2491  O   HOH A 835     3021   3836   3434    627    364   -234       O  
-HETATM 2492  O   HOH A 836      28.150  41.870  16.398  1.00 34.16           O  
-ANISOU 2492  O   HOH A 836     4108   4209   4662   1194   -480     97       O  
-HETATM 2493  O   HOH A 837      51.974  39.505  25.605  1.00 25.81           O  
-ANISOU 2493  O   HOH A 837     2857   2183   4764   -625   -593   -668       O  
-HETATM 2494  O   HOH A 838      46.969  16.138  34.627  1.00 25.00           O  
-ANISOU 2494  O   HOH A 838     3596   2511   3390    362  -1316   1102       O  
-HETATM 2495  O   HOH A 839      21.987  33.554   7.266  1.00 39.39           O  
-ANISOU 2495  O   HOH A 839     4169   5490   5307    617   -247    370       O  
-HETATM 2496  O   HOH A 840      43.889  38.842  18.208  1.00 29.39           O  
-ANISOU 2496  O   HOH A 840     3748   3548   3871    257    427   -336       O  
-HETATM 2497  O   HOH A 841      34.373  16.053  33.974  1.00 35.62           O  
-ANISOU 2497  O   HOH A 841     5245   3845   4441    -21     -4    394       O  
-HETATM 2498  O   HOH A 842      48.793  18.610  30.765  1.00 30.28           O  
-ANISOU 2498  O   HOH A 842     3246   2973   5284   1130    520    363       O  
-HETATM 2499  O   HOH A 843      27.461  15.845  17.861  1.00 33.03           O  
-ANISOU 2499  O   HOH A 843     2652   5263   4633   -417    760    388       O  
-HETATM 2500  O   HOH A 844      41.380  40.044   3.233  1.00 29.73           O  
-ANISOU 2500  O   HOH A 844     4032   2064   5200    277    198    687       O  
-HETATM 2501  O   HOH A 845      27.731  17.982  19.359  1.00 33.06           O  
-ANISOU 2501  O   HOH A 845     4186   3495   4878   -374    385    681       O  
-HETATM 2502  O   HOH A 846      62.703  30.021  10.049  1.00 31.50           O  
-ANISOU 2502  O   HOH A 846     3554   3822   4589    557   -111    548       O  
-HETATM 2503  O   HOH A 847      12.842  17.151  17.507  1.00 30.10           O  
-ANISOU 2503  O   HOH A 847     3731   3011   4694    211    837    661       O  
-HETATM 2504  O   HOH A 848      45.454  34.322  -2.775  1.00 42.79           O  
-ANISOU 2504  O   HOH A 848     5987   5171   5100    236   -642    548       O  
-HETATM 2505  O   HOH A 849      43.238  34.570  35.389  1.00 26.06           O  
-ANISOU 2505  O   HOH A 849     4637   3636   1626    238    568   -154       O  
-HETATM 2506  O   HOH A 850      45.989  33.376  -5.452  1.00 33.11           O  
-ANISOU 2506  O   HOH A 850     5104   3803   3673   -214   -513    554       O  
-HETATM 2507  O   HOH A 851      60.455  24.303  26.231  1.00 39.74           O  
-ANISOU 2507  O   HOH A 851     5295   5119   4683    306   1082   -298       O  
-HETATM 2508  O   HOH A 852      26.787  23.920  -5.852  1.00 31.28           O  
-ANISOU 2508  O   HOH A 852     4248   4900   2737    112   -749    538       O  
-HETATM 2509  O   HOH A 853      14.508  16.804  19.716  1.00 31.73           O  
-ANISOU 2509  O   HOH A 853     2644   4589   4822    122    811     26       O  
-HETATM 2510  O   HOH A 854      19.794  24.659   3.056  1.00 25.16           O  
-ANISOU 2510  O   HOH A 854     3778   3440   2339   1842   -258    251       O  
-HETATM 2511  O   HOH A 855      55.539  22.621  34.276  1.00 35.67           O  
-ANISOU 2511  O   HOH A 855     3947   4275   5330    134    136    585       O  
-HETATM 2512  O   HOH A 856      16.229  24.906  19.318  1.00 25.20           O  
-ANISOU 2512  O   HOH A 856     2371   2992   4212    -65    315    -51       O  
-HETATM 2513  O   HOH A 857      41.687  41.486   9.570  1.00 33.44           O  
-ANISOU 2513  O   HOH A 857     4040   4330   4335    309    146   -300       O  
-HETATM 2514  O   HOH A 858      34.967  34.172   2.476  1.00 32.57           O  
-ANISOU 2514  O   HOH A 858     3283   3890   5202    638    -55    306       O  
-HETATM 2515  O   HOH A 859      47.335  18.546  36.809  1.00 31.62           O  
-ANISOU 2515  O   HOH A 859     4767   3242   4004  -1190   -468    647       O  
-HETATM 2516  O   HOH A 860      47.272  12.870  -4.358  1.00 32.05           O  
-ANISOU 2516  O   HOH A 860     4314   3574   4286   -252    -48   -566       O  
-HETATM 2517  O   HOH A 861      16.209  22.897  16.373  1.00 35.79           O  
-ANISOU 2517  O   HOH A 861     4252   4717   4626   1039   -607    324       O  
-HETATM 2518  O   HOH A 862      14.383  19.505  20.829  1.00 36.49           O  
-ANISOU 2518  O   HOH A 862     3931   4975   4955    393   -238    328       O  
-HETATM 2519  O   HOH A 863      53.101  42.660   9.543  1.00 32.89           O  
-ANISOU 2519  O   HOH A 863     4609   3868   4018   -140   -797   -143       O  
-HETATM 2520  O   HOH A 864      61.517  25.695  23.135  1.00 27.99           O  
-ANISOU 2520  O   HOH A 864     3264   2963   4406   1026    228    525       O  
-HETATM 2521  O   HOH A 865      60.327  45.390   7.934  1.00 33.57           O  
-ANISOU 2521  O   HOH A 865     5364   3449   3940    -75    347   -113       O  
-HETATM 2522  O   HOH A 866      34.326  14.261  31.905  1.00 29.34           O  
-ANISOU 2522  O   HOH A 866     4414   3301   3431   -455    664   -313       O  
-HETATM 2523  O   HOH A 867      58.352  21.651  16.170  1.00 27.42           O  
-ANISOU 2523  O   HOH A 867     3257   2686   4476   1094   -364   1122       O  
-HETATM 2524  O   HOH A 868      62.356  24.280   4.300  1.00 32.55           O  
-ANISOU 2524  O   HOH A 868     5012   3155   4199    378  -1024    988       O  
-HETATM 2525  O   HOH A 869      24.129  10.187  19.250  1.00 31.89           O  
-ANISOU 2525  O   HOH A 869     4946   3617   3553   -414    118   -575       O  
-HETATM 2526  O   HOH A 870      51.076  29.992  38.005  1.00 34.67           O  
-ANISOU 2526  O   HOH A 870     5448   4982   2743   -476    281     44       O  
-HETATM 2527  O   HOH A 871      49.426  17.465  15.933  1.00 28.04           O  
-ANISOU 2527  O   HOH A 871     2724   3103   4824    718   -547   -738       O  
-HETATM 2528  O   HOH A 872      18.497   6.758  15.373  1.00 28.56           O  
-ANISOU 2528  O   HOH A 872     2898   5100   2852    386     35   1430       O  
-HETATM 2529  O   HOH A 873      55.429  17.042   6.573  1.00 34.56           O  
-ANISOU 2529  O   HOH A 873     3396   4408   5325    329    225   -369       O  
-HETATM 2530  O   HOH A 874      56.254  18.677   4.649  1.00 33.06           O  
-ANISOU 2530  O   HOH A 874     3356   4188   5014   1085    299     96       O  
-HETATM 2531  O   HOH A 875      49.554  36.520  -5.512  1.00 27.45           O  
-ANISOU 2531  O   HOH A 875     3736   3497   3194   -712   -843   -124       O  
-HETATM 2532  O   HOH A 876      17.920  24.176  -0.695  1.00 31.11           O  
-ANISOU 2532  O   HOH A 876     3250   3976   4594    840   -829    549       O  
-HETATM 2533  O   HOH A 877      24.354  25.427  -6.384  1.00 43.39           O  
-ANISOU 2533  O   HOH A 877     5589   5509   5387   -105   -727    254       O  
-HETATM 2534  O   HOH A 878      52.519  17.951  24.013  1.00 32.40           O  
-ANISOU 2534  O   HOH A 878     3657   4147   4506   1241    498   -597       O  
-HETATM 2535  O   HOH A 879      19.047   8.612  11.709  1.00 24.64           O  
-ANISOU 2535  O   HOH A 879     2626   3854   2882   -143   -150   -295       O  
-HETATM 2536  O   HOH A 880      56.904  21.231  13.856  1.00 30.00           O  
-ANISOU 2536  O   HOH A 880     3342   4037   4019    -85   -108   -725       O  
-HETATM 2537  O   HOH A 881      18.235  32.211  35.680  1.00 23.35           O  
-ANISOU 2537  O   HOH A 881     2562   4320   1987     49    244    612       O  
-HETATM 2538  O   HOH A 882      22.809  30.093   1.696  1.00 33.80           O  
-ANISOU 2538  O   HOH A 882     4560   4232   4049    920   -266    637       O  
-HETATM 2539  O   HOH A 883      36.933  10.212  16.059  1.00 29.57           O  
-ANISOU 2539  O   HOH A 883     3372   4252   3609   -121   -378   -106       O  
-HETATM 2540  O   HOH A 884      25.651  42.711  22.635  1.00 37.92           O  
-ANISOU 2540  O   HOH A 884     4839   4574   4995    542     72   -195       O  
-HETATM 2541  O   HOH A 885      46.357  13.692  -6.648  1.00 38.13           O  
-ANISOU 2541  O   HOH A 885     5358   3862   5266   -621   -122   -120       O  
-HETATM 2542  O   HOH A 886      49.183  18.237  13.042  1.00 24.98           O  
-ANISOU 2542  O   HOH A 886     1768   2784   4938    167    434   1420       O  
-HETATM 2543  O   HOH A 887      28.676  43.823  22.300  1.00 26.84           O  
-ANISOU 2543  O   HOH A 887     3683   2746   3768    321  -1180  -1091       O  
-HETATM 2544  O   HOH A 888      62.831  22.797  11.174  1.00 27.99           O  
-ANISOU 2544  O   HOH A 888     1805   4585   4243    769    474     22       O  
-HETATM 2545  O   HOH A 889      44.193  26.545   6.340  1.00  5.93           O  
-ANISOU 2545  O   HOH A 889      666    941    646   -142     33     36       O  
-HETATM 2546  O   HOH A 890      21.864  25.437  17.622  1.00 24.67           O  
-ANISOU 2546  O   HOH A 890     2661   3312   3401    398   -568     16       O  
-HETATM 2547  O   HOH A 891      21.611  23.620  35.078  1.00 35.52           O  
-ANISOU 2547  O   HOH A 891     4791   4165   4537   -114    409    110       O  
-HETATM 2548  O   HOH A 892      51.935  41.819  16.302  1.00 34.17           O  
-ANISOU 2548  O   HOH A 892     4514   4145   4323   1068  -1121   -175       O  
-HETATM 2549  O   HOH A 893      20.950  24.229  21.657  1.00 33.03           O  
-ANISOU 2549  O   HOH A 893     3689   4370   4489   -919   -420    891       O  
-HETATM 2550  O   HOH A 894      24.389  39.038  33.754  1.00 28.67           O  
-ANISOU 2550  O   HOH A 894     3487   3540   3865    203    882  -1170       O  
-HETATM 2551  O   HOH A 895      52.757  25.219   8.099  1.00 24.63           O  
-ANISOU 2551  O   HOH A 895     3420   3874   2063   1996    146    -15       O  
-HETATM 2552  O   HOH A 896      43.112  34.532  -1.430  1.00 42.44           O  
-ANISOU 2552  O   HOH A 896     5566   4902   5654    192   -442    -70       O  
-HETATM 2553  O   HOH A 897      29.061  31.867   2.923  1.00 30.18           O  
-ANISOU 2553  O   HOH A 897     4273   3606   3587    349    -38   -273       O  
-HETATM 2554  O   HOH A 898      21.305  28.395   3.121  1.00 28.52           O  
-ANISOU 2554  O   HOH A 898     3783   4094   2958    636    284   -722       O  
-HETATM 2555  O   HOH A 899      19.588   8.209   8.948  1.00 25.26           O  
-ANISOU 2555  O   HOH A 899     3871   2953   2772   -165    104   -519       O  
-HETATM 2556  O   HOH A 900      54.049  38.881  27.406  1.00 31.41           O  
-ANISOU 2556  O   HOH A 900     3335   3551   5047    783   -238   -225       O  
-HETATM 2557  O   HOH A 901      31.641  29.920  -1.844  1.00 28.57           O  
-ANISOU 2557  O   HOH A 901     4425   4278   2149   -423   -221   -219       O  
-HETATM 2558  O   HOH A 902      18.801  32.151   8.325  1.00 26.95           O  
-ANISOU 2558  O   HOH A 902     2537   3836   3865    564   -162     59       O  
-HETATM 2559  O   HOH A 903      58.374  22.128  18.693  1.00 26.58           O  
-ANISOU 2559  O   HOH A 903     2973   2095   5031    493   -180   -205       O  
-HETATM 2560  O   HOH A 904      51.967  17.265  29.271  1.00 33.39           O  
-ANISOU 2560  O   HOH A 904     4673   4475   3539    -48   -441    618       O  
-HETATM 2561  O   HOH A 905      31.789  12.647  32.154  1.00 30.15           O  
-ANISOU 2561  O   HOH A 905     4420   3110   3925    -66   -633   -648       O  
-HETATM 2562  O   HOH A 906      20.589   5.842   8.379  1.00 33.01           O  
-ANISOU 2562  O   HOH A 906     4352   4095   4093    138    680   -272       O  
-HETATM 2563  O   HOH A 907      22.153  17.902  22.163  1.00 30.75           O  
-ANISOU 2563  O   HOH A 907     4304   3313   4065   -908    274    977       O  
-HETATM 2564  O   HOH A 908      64.343  27.572  29.981  1.00 24.21           O  
-ANISOU 2564  O   HOH A 908     3270   3120   2807    382    272     29       O  
-HETATM 2565  O   HOH A 909      62.763  42.734  12.602  1.00 35.42           O  
-ANISOU 2565  O   HOH A 909     4667   4331   4460   -669   -376   -635       O  
-HETATM 2566  O   HOH A 910      58.712  44.835  16.217  1.00 39.96           O  
-ANISOU 2566  O   HOH A 910     5745   4577   4860   -423    334    544       O  
-HETATM 2567  O   HOH A 911      58.595  15.841   4.732  1.00 36.90           O  
-ANISOU 2567  O   HOH A 911     4125   4941   4954     68   -183   -414       O  
-HETATM 2568  O   HOH A 912      59.823  15.896   9.545  1.00 26.64           O  
-ANISOU 2568  O   HOH A 912     4265   2926   2930   1719    746   -308       O  
-HETATM 2569  O   HOH A 913      32.571  31.455  35.964  1.00 20.77           O  
-ANISOU 2569  O   HOH A 913     2227   2848   2815     48   -336    274       O  
-HETATM 2570  O   HOH A 914      32.282  20.774  18.922  1.00 23.77           O  
-ANISOU 2570  O   HOH A 914     2559   3057   3412    -25    283    -23       O  
-HETATM 2571  O   HOH A 915      41.522  22.667  35.995  1.00 28.37           O  
-ANISOU 2571  O   HOH A 915     5459   3369   1951   1133   -119    578       O  
-HETATM 2572  O   HOH A 916      21.366   5.375   5.849  1.00 27.01           O  
-ANISOU 2572  O   HOH A 916     2475   3086   4700   -433    329   -810       O  
-HETATM 2573  O   HOH A 917      56.894  23.833  37.535  1.00 42.79           O  
-ANISOU 2573  O   HOH A 917     4976   5436   5844     34   -285    277       O  
-HETATM 2574  O   HOH A 918      34.739  37.534  35.019  1.00 29.85           O  
-ANISOU 2574  O   HOH A 918     4093   4274   2974    336   -840    -62       O  
-HETATM 2575  O   HOH A 919      58.024  44.777   8.833  1.00 28.59           O  
-ANISOU 2575  O   HOH A 919     3986   2944   3930   -164   -202   -240       O  
-HETATM 2576  O   HOH A 920      25.504  16.006  14.921  1.00 19.07           O  
-ANISOU 2576  O   HOH A 920     2547   2576   2123   -253    921   -128       O  
-HETATM 2577  O   HOH A 921      64.972  35.188  13.990  1.00 26.90           O  
-ANISOU 2577  O   HOH A 921     2186   4712   3322   -603   -368    -81       O  
-HETATM 2578  O   HOH A 922      30.071  31.308  -0.884  1.00 32.80           O  
-ANISOU 2578  O   HOH A 922     4562   4329   3569    450   -684    744       O  
-HETATM 2579  O   HOH A 923      43.597  32.412  -5.696  1.00 38.82           O  
-ANISOU 2579  O   HOH A 923     5240   4972   4536   -226    129    108       O  
-HETATM 2580  O   HOH A 924      22.877  29.472  16.051  1.00 11.50           O  
-ANISOU 2580  O   HOH A 924     1417   1176   1775    184    266    123       O  
-HETATM 2581  O   HOH A 925      46.878  42.398   4.075  1.00 12.95           O  
-ANISOU 2581  O   HOH A 925     1565   1299   2057    299    646    611       O  
-HETATM 2582  O   HOH A 926      28.569  15.981  15.071  1.00 14.91           O  
-ANISOU 2582  O   HOH A 926     1894   1684   2085   -179    193    120       O  
-HETATM 2583  O   HOH A 927      40.282  23.184  20.626  1.00 13.91           O  
-ANISOU 2583  O   HOH A 927     1852   1536   1896    -41    316    -70       O  
-HETATM 2584  O   HOH A 928      29.397   8.068  10.931  1.00 27.00           O  
-ANISOU 2584  O   HOH A 928     4479   2257   3521    477    813    -54       O  
-HETATM 2585  O   HOH A 929      51.081  20.409  31.746  1.00 15.73           O  
-ANISOU 2585  O   HOH A 929     2336   1210   2429    310    195     84       O  
-HETATM 2586  O   HOH A 930      51.266  24.482  -2.961  1.00 28.66           O  
-ANISOU 2586  O   HOH A 930     4579   2830   3479    522    114  -1017       O  
-HETATM 2587  O   HOH A 931      59.120  46.278   3.983  1.00 23.56           O  
-ANISOU 2587  O   HOH A 931     2922   2714   3315   -696   -897   1282       O  
-HETATM 2588  O   HOH A 932      25.251  40.332  26.256  1.00 32.79           O  
-ANISOU 2588  O   HOH A 932     3700   4729   4028    374    446    -53       O  
-HETATM 2589  O   HOH A 933      48.001  38.515  -1.583  1.00 25.06           O  
-ANISOU 2589  O   HOH A 933     3325   3087   3108  -1390   -551   -365       O  
-HETATM 2590  O   HOH A 934      22.525  40.964  26.745  1.00 36.40           O  
-ANISOU 2590  O   HOH A 934     4234   4058   5536    223    342    -73       O  
-HETATM 2591  O   HOH A 935      59.889  44.197   5.600  1.00 26.57           O  
-ANISOU 2591  O   HOH A 935     4709   2195   3190   -467  -1165      0       O  
-HETATM 2592  O   HOH A 936      22.762  24.292  37.416  1.00 35.61           O  
-ANISOU 2592  O   HOH A 936     4516   4576   4436    -58    897    182       O  
-HETATM 2593  O   HOH A 937      22.233  23.679  -5.606  1.00 33.83           O  
-ANISOU 2593  O   HOH A 937     4157   5022   3672    111    212   -272       O  
-HETATM 2594  O   HOH A 938      15.954   9.146  15.144  1.00 40.23           O  
-ANISOU 2594  O   HOH A 938     5144   4676   5462   -400   -116    708       O  
-HETATM 2595  O   HOH A 939      26.733   1.174  -2.562  1.00 34.97           O  
-ANISOU 2595  O   HOH A 939     4015   4252   5019   -440    274   -362       O  
-HETATM 2596  O   HOH A 940      52.175  41.324  22.151  1.00 33.14           O  
-ANISOU 2596  O   HOH A 940     4232   4168   4191   -200    490   -592       O  
-HETATM 2597  O   HOH A 941      45.057  13.303  18.392  1.00 31.99           O  
-ANISOU 2597  O   HOH A 941     4340   4137   3675   -943    605    569       O  
-HETATM 2598  O   HOH A 942      47.583  44.846   5.544  1.00 28.65           O  
-ANISOU 2598  O   HOH A 942     4042   2640   4203    733     19   1339       O  
-CONECT  494  500                                                                
-CONECT  500  494  501                                                           
-CONECT  501  500  502  504                                                      
-CONECT  502  501  503  508                                                      
-CONECT  503  502                                                                
-CONECT  504  501  505                                                           
-CONECT  505  504  506                                                           
-CONECT  506  505  507                                                           
-CONECT  507  506                                                                
-CONECT  508  502                                                                
-CONECT 1698 1707                                                                
-CONECT 1707 1698 1708                                                           
-CONECT 1708 1707 1709 1711                                                      
-CONECT 1709 1708 1710 1715                                                      
-CONECT 1710 1709                                                                
-CONECT 1711 1708 1712                                                           
-CONECT 1712 1711 1713                                                           
-CONECT 1713 1712 1714                                                           
-CONECT 1714 1713                                                                
-CONECT 1715 1709                                                                
-CONECT 2086 2095                                                                
-CONECT 2095 2086 2096                                                           
-CONECT 2096 2095 2097 2099                                                      
-CONECT 2097 2096 2098 2105                                                      
-CONECT 2098 2097                                                                
-CONECT 2099 2096 2100                                                           
-CONECT 2100 2099 2101 2102                                                      
-CONECT 2101 2100 2103                                                           
-CONECT 2102 2100 2104                                                           
-CONECT 2103 2101                                                                
-CONECT 2104 2102                                                                
-CONECT 2105 2097                                                                
-CONECT 2123 2125 2130 2166 2172                                                 
-CONECT 2123 2180 2182                                                           
-CONECT 2124 2125 2126 2127 2131                                                 
-CONECT 2125 2123 2124                                                           
-CONECT 2126 2124                                                                
-CONECT 2127 2124                                                                
-CONECT 2128 2129 2130 2131 2135                                                 
-CONECT 2129 2128                                                                
-CONECT 2130 2123 2128                                                           
-CONECT 2131 2124 2128                                                           
-CONECT 2132 2133 2134 2135 2136                                                 
-CONECT 2133 2132                                                                
-CONECT 2134 2132                                                                
-CONECT 2135 2128 2132                                                           
-CONECT 2136 2132 2137                                                           
-CONECT 2137 2136 2138                                                           
-CONECT 2138 2137 2139 2140                                                      
-CONECT 2139 2138 2144                                                           
-CONECT 2140 2138 2141 2142                                                      
-CONECT 2141 2140                                                                
-CONECT 2142 2140 2143 2144                                                      
-CONECT 2143 2142                                                                
-CONECT 2144 2139 2142 2145                                                      
-CONECT 2145 2144 2146 2154                                                      
-CONECT 2146 2145 2147                                                           
-CONECT 2147 2146 2148                                                           
-CONECT 2148 2147 2149 2154                                                      
-CONECT 2149 2148 2150 2151                                                      
-CONECT 2150 2149                                                                
-CONECT 2151 2149 2152                                                           
-CONECT 2152 2151 2153                                                           
-CONECT 2153 2152 2154                                                           
-CONECT 2154 2145 2148 2153                                                      
-CONECT 2166 2123                                                                
-CONECT 2172 2123                                                                
-CONECT 2180 2123                                                                
-CONECT 2182 2123                                                                
-MASTER      304    0    5   12   18    0    9    6 2591    1   69   22          
-END                                                                             
diff --git a/plip/test/pdb/2efj.pdb b/plip/test/pdb/2efj.pdb
deleted file mode 100644
index feef7c7..0000000
--- a/plip/test/pdb/2efj.pdb
+++ /dev/null
@@ -1,3525 +0,0 @@
-HEADER    TRANSFERASE                             22-FEB-07   2EFJ              
-TITLE     THE STRUCTURE OF 1,7 DIMETHYLXANTHINE METHYLTRANSFERASE               
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: 3,7-DIMETHYLXANTHINE METHYLTRANSFERASE;                    
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 EC: 2.1.1.-;                                                         
-COMPND   5 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: COFFEA CANEPHORA;                               
-SOURCE   3 ORGANISM_TAXID: 49390;                                               
-SOURCE   4 GENE: DXMT1;                                                         
-SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (RIL);                                
-SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPROEXHTB                                 
-KEYWDS    SAM-DEPENDANT METHYLTRANSFERASE, SAH, THEOBROMINE, TRANSFERASE        
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    A.A.MCCARTHY,J.G.MCCARTHY                                             
-REVDAT   4   13-JUL-11 2EFJ    1       VERSN                                    
-REVDAT   3   24-FEB-09 2EFJ    1       VERSN                                    
-REVDAT   2   19-JUN-07 2EFJ    1       JRNL   REMARK                            
-REVDAT   1   01-MAY-07 2EFJ    0                                                
-JRNL        AUTH   A.A.MCCARTHY,J.G.MCCARTHY                                    
-JRNL        TITL   THE STRUCTURE OF TWO N-METHYLTRANSFERASES FROM THE CAFFEINE  
-JRNL        TITL 2 BIOSYNTHETIC PATHWAY                                         
-JRNL        REF    PLANT PHYSIOL.                V. 144   879 2007              
-JRNL        REFN                   ISSN 0032-0889                               
-JRNL        PMID   17434991                                                     
-JRNL        DOI    10.1104/PP.106.094854                                        
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   A.A.MCCARTHY,L.BIGET,C.LIN,V.PETIARD,S.D.TANKSLEY,           
-REMARK   1  AUTH 2 J.G.MCCARTHY                                                 
-REMARK   1  TITL   CLONING, EXPRESSION, CRYSTALLIZATION AND PRELIMINARY X-RAY   
-REMARK   1  TITL 2 ANALYSIS OF THE XMT AND DXMT N-METHYLTRANSFERASES FROM       
-REMARK   1  TITL 3 COFFEA CANEPHORA (ROBUSTA)                                   
-REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  63   304 2007              
-REMARK   1  REFN                   ESSN 1744-3091                               
-REMARK   1  PMID   17401201                                                     
-REMARK   1  DOI    10.1107/S1744309107009268                                    
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
-REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
-REMARK   3   NUMBER OF REFLECTIONS             : 24209                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
-REMARK   3   R VALUE            (WORKING SET) : 0.220                           
-REMARK   3   FREE R VALUE                     : 0.276                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1297                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
-REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1707                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.06                        
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010                       
-REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
-REMARK   3   BIN FREE R VALUE                    : 0.3600                       
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 2719                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 39                                      
-REMARK   3   SOLVENT ATOMS            : 146                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
-REMARK   3   FROM WILSON PLOT           (A**2) : 35.00                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.31                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -0.68000                                             
-REMARK   3    B22 (A**2) : 1.42000                                              
-REMARK   3    B33 (A**2) : -0.74000                                             
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
-REMARK   3   ESU BASED ON R VALUE                            (A): 0.217         
-REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.196         
-REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
-REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.341        
-REMARK   3                                                                      
-REMARK   3 CORRELATION COEFFICIENTS.                                            
-REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
-REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
-REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2853 ; 0.012 ; 0.022       
-REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
-REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3873 ; 1.564 ; 1.985       
-REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
-REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   349 ; 5.634 ; 5.000       
-REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;37.532 ;24.331       
-REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   467 ;17.281 ;15.000       
-REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;18.178 ;15.000       
-REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   431 ; 0.105 ; 0.200       
-REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2160 ; 0.005 ; 0.020       
-REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1311 ; 0.206 ; 0.200       
-REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1932 ; 0.303 ; 0.200       
-REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   157 ; 0.279 ; 0.200       
-REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    47 ; 0.149 ; 0.200       
-REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.128 ; 0.200       
-REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
-REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1802 ; 0.719 ; 1.500       
-REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2826 ; 1.171 ; 2.000       
-REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1226 ; 1.745 ; 3.000       
-REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1044 ; 2.546 ; 4.500       
-REMARK   3                                                                      
-REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
-REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS STATISTICS                                           
-REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 1                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   A     3        A    27                          
-REMARK   3    ORIGIN FOR THE GROUP (A):   3.9340  19.5330  50.2400              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.0600 T22:  -0.0930                                     
-REMARK   3      T33:  -0.0372 T12:   0.0992                                     
-REMARK   3      T13:  -0.0018 T23:   0.0093                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:  10.1675 L22:   4.4754                                     
-REMARK   3      L33:   1.9622 L12:  -1.2302                                     
-REMARK   3      L13:   4.0267 L23:   0.7737                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.3495 S12:   0.9509 S13:  -1.1168                       
-REMARK   3      S21:  -0.1063 S22:   0.4389 S23:   0.3908                       
-REMARK   3      S31:   0.2223 S32:  -0.0407 S33:  -0.7883                       
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 2                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   A    28        A   231                          
-REMARK   3    RESIDUE RANGE :   A   266        A   302                          
-REMARK   3    RESIDUE RANGE :   A   365        A   379                          
-REMARK   3    ORIGIN FOR THE GROUP (A):   4.4310  33.8670  51.9200              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:  -0.1063 T22:  -0.2303                                     
-REMARK   3      T33:  -0.1783 T12:   0.0876                                     
-REMARK   3      T13:   0.0724 T23:   0.0118                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.1261 L22:   1.0666                                     
-REMARK   3      L33:   2.5178 L12:  -0.7476                                     
-REMARK   3      L13:   0.7132 L23:  -0.6932                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1552 S12:  -0.2872 S13:   0.0732                       
-REMARK   3      S21:   0.3580 S22:   0.2754 S23:   0.0882                       
-REMARK   3      S31:  -0.2113 S32:  -0.1757 S33:  -0.1202                       
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 3                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   A   232        A   265                          
-REMARK   3    RESIDUE RANGE :   A   312        A   364                          
-REMARK   3    ORIGIN FOR THE GROUP (A):  11.5130  10.7620  61.7420              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:  -0.0031 T22:  -0.1668                                     
-REMARK   3      T33:  -0.2105 T12:   0.1539                                     
-REMARK   3      T13:   0.0625 T23:   0.0721                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   5.2790 L22:   3.4891                                     
-REMARK   3      L33:   2.4406 L12:  -0.7196                                     
-REMARK   3      L13:  -0.7959 L23:   0.1829                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.3154 S12:  -0.4022 S13:  -0.7686                       
-REMARK   3      S21:   0.4751 S22:   0.2753 S23:   0.1526                       
-REMARK   3      S31:   0.2889 S32:   0.0447 S33:   0.0401                       
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED : MASK                                                 
-REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
-REMARK   3   VDW PROBE RADIUS   : 1.40                                          
-REMARK   3   ION PROBE RADIUS   : 0.80                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 2EFJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-07.                  
-REMARK 100 THE RCSB ID CODE IS RCSB026601.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-05                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 8.5                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ESRF                               
-REMARK 200  BEAMLINE                       : ID14-4                             
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393                             
-REMARK 200  MONOCHROMATOR                  : A DOUBLE CRYSTAL (SI 111) KHOZU    
-REMARK 200                                   MONOCHROMATOR                      
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
-REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25506                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : 0.05300                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.50200                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
-REMARK 200 SOFTWARE USED: SHARP                                                 
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 42.78                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 23-28% PEG 3350, 200MM LI2SO4, 100MM     
-REMARK 280  TRIS-HCL, 2MM DTT, 1MM SAH, 1MM THEOBROMINE, PH 8.5, VAPOR          
-REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,-Y,Z+1/2                                             
-REMARK 290       3555   -X,Y,-Z+1/2                                             
-REMARK 290       4555   X,-Y,-Z                                                 
-REMARK 290       5555   X+1/2,Y+1/2,Z                                           
-REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
-REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
-REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.47500            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.47500            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       25.08000            
-REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.81500            
-REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       25.08000            
-REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.81500            
-REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.47500            
-REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       25.08000            
-REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.81500            
-REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.47500            
-REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       25.08000            
-REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.81500            
-REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY   
-REMARK 300 THE SYMMETERY OPERATIONS: -X, Y, -Z+1/2.                             
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       70.47500            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     GLU A     2                                                      
-REMARK 465     GLY A    12                                                      
-REMARK 465     GLU A    13                                                      
-REMARK 465     GLY A    14                                                      
-REMARK 465     ASP A    15                                                      
-REMARK 465     GLY A    82                                                      
-REMARK 465     GLN A    83                                                      
-REMARK 465     GLU A    84                                                      
-REMARK 465     LYS A    85                                                      
-REMARK 465     LYS A    86                                                      
-REMARK 465     ASN A    87                                                      
-REMARK 465     GLU A    88                                                      
-REMARK 465     LEU A    89                                                      
-REMARK 465     GLU A    90                                                      
-REMARK 465     ARG A    91                                                      
-REMARK 465     LEU A   169                                                      
-REMARK 465     VAL A   170                                                      
-REMARK 465     THR A   171                                                      
-REMARK 465     GLU A   172                                                      
-REMARK 465     LEU A   173                                                      
-REMARK 465     GLY A   174                                                      
-REMARK 465     ASP A   303                                                      
-REMARK 465     ASP A   304                                                      
-REMARK 465     ASP A   305                                                      
-REMARK 465     TYR A   306                                                      
-REMARK 465     GLN A   307                                                      
-REMARK 465     GLY A   308                                                      
-REMARK 465     ARG A   309                                                      
-REMARK 465     SER A   310                                                      
-REMARK 465     HIS A   311                                                      
-REMARK 465     GLU A   380                                                      
-REMARK 465     LYS A   381                                                      
-REMARK 465     ALA A   382                                                      
-REMARK 465     ASP A   383                                                      
-REMARK 465     MET A   384                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     LYS A  20    CD   CE   NZ                                        
-REMARK 470     LYS A  52    CG   CD   CE   NZ                                   
-REMARK 470     LYS A  80    CE   NZ                                             
-REMARK 470     LYS A 127    CG   CD   CE   NZ                                   
-REMARK 470     ILE A 175    CG1  CG2  CD1                                       
-REMARK 470     SER A 176    OG                                                  
-REMARK 470     LYS A 179    CD   CE   NZ                                        
-REMARK 470     LYS A 186    CG   CD   CE   NZ                                   
-REMARK 470     ARG A 218    NE   CZ   NH1  NH2                                  
-REMARK 470     ASP A 230    CB   CG   OD1  OD2                                  
-REMARK 470     GLU A 231    CG   CD   OE1  OE2                                  
-REMARK 470     ARG A 276    NE   CZ   NH1  NH2                                  
-REMARK 470     SER A 312    OG                                                  
-REMARK 470     LYS A 359    CD   CE   NZ                                        
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    LEU A  26      -62.41    -90.57                                   
-REMARK 500    ASN A  49       -3.24     69.44                                   
-REMARK 500    LYS A  52      -63.87    -94.67                                   
-REMARK 500    ALA A  62     -138.12     56.02                                   
-REMARK 500    ARG A 126      100.82    -36.56                                   
-REMARK 500    TYR A 157       41.69     72.07                                   
-REMARK 500    TYR A 183     -168.78   -160.15                                   
-REMARK 500    PHE A 232      -64.45   -102.21                                   
-REMARK 500    ASP A 233       46.05     85.51                                   
-REMARK 500    PRO A 313     -111.90    -68.14                                   
-REMARK 500    VAL A 314      -24.19   -159.04                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A 596        DISTANCE =  5.43 ANGSTROMS                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 501                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 37T A 502                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 2EG5   RELATED DB: PDB                                   
-REMARK 900 XANTHOSINE METHYLTRANSFERASE                                         
-DBREF  2EFJ A    1   384  UNP    A4GE70   A4GE70_COFCA     1    384             
-SEQRES   1 A  384  MET GLU LEU GLN GLU VAL LEU HIS MET ASN GLY GLY GLU          
-SEQRES   2 A  384  GLY ASP THR SER TYR ALA LYS ASN SER SER TYR ASN LEU          
-SEQRES   3 A  384  PHE LEU ILE ARG VAL LYS PRO VAL LEU GLU GLN CYS ILE          
-SEQRES   4 A  384  GLN GLU LEU LEU ARG ALA ASN LEU PRO ASN ILE ASN LYS          
-SEQRES   5 A  384  CYS PHE LYS VAL GLY ASP LEU GLY CYS ALA SER GLY PRO          
-SEQRES   6 A  384  ASN THR PHE SER THR VAL ARG ASP ILE VAL GLN SER ILE          
-SEQRES   7 A  384  ASP LYS VAL GLY GLN GLU LYS LYS ASN GLU LEU GLU ARG          
-SEQRES   8 A  384  PRO THR ILE GLN ILE PHE LEU ASN ASP LEU PHE GLN ASN          
-SEQRES   9 A  384  ASP PHE ASN SER VAL PHE LYS LEU LEU PRO SER PHE TYR          
-SEQRES  10 A  384  ARG ASN LEU GLU LYS GLU ASN GLY ARG LYS ILE GLY SER          
-SEQRES  11 A  384  CYS LEU ILE GLY ALA MET PRO GLY SER PHE TYR SER ARG          
-SEQRES  12 A  384  LEU PHE PRO GLU GLU SER MET HIS PHE LEU HIS SER CYS          
-SEQRES  13 A  384  TYR CYS LEU HIS TRP LEU SER GLN VAL PRO SER GLY LEU          
-SEQRES  14 A  384  VAL THR GLU LEU GLY ILE SER VAL ASN LYS GLY CYS ILE          
-SEQRES  15 A  384  TYR SER SER LYS ALA SER ARG PRO PRO ILE GLN LYS ALA          
-SEQRES  16 A  384  TYR LEU ASP GLN PHE THR LYS ASP PHE THR THR PHE LEU          
-SEQRES  17 A  384  ARG ILE HIS SER GLU GLU LEU ILE SER ARG GLY ARG MET          
-SEQRES  18 A  384  LEU LEU THR PHE ILE CYS LYS GLU ASP GLU PHE ASP HIS          
-SEQRES  19 A  384  PRO ASN SER MET ASP LEU LEU GLU MET SER ILE ASN ASP          
-SEQRES  20 A  384  LEU VAL ILE GLU GLY HIS LEU GLU GLU GLU LYS LEU ASP          
-SEQRES  21 A  384  SER PHE ASN VAL PRO ILE TYR ALA PRO SER THR GLU GLU          
-SEQRES  22 A  384  VAL LYS ARG ILE VAL GLU GLU GLU GLY SER PHE GLU ILE          
-SEQRES  23 A  384  LEU TYR LEU GLU THR PHE ASN ALA PRO TYR ASP ALA GLY          
-SEQRES  24 A  384  PHE SER ILE ASP ASP ASP TYR GLN GLY ARG SER HIS SER          
-SEQRES  25 A  384  PRO VAL SER CYS ASP GLU HIS ALA ARG ALA ALA HIS VAL          
-SEQRES  26 A  384  ALA SER VAL VAL ARG SER ILE TYR GLU PRO ILE LEU ALA          
-SEQRES  27 A  384  SER HIS PHE GLY GLU ALA ILE LEU PRO ASP LEU SER HIS          
-SEQRES  28 A  384  ARG ILE ALA LYS ASN ALA ALA LYS VAL LEU ARG SER GLY          
-SEQRES  29 A  384  LYS GLY PHE TYR ASP SER VAL ILE ILE SER LEU ALA LYS          
-SEQRES  30 A  384  LYS PRO GLU LYS ALA ASP MET                                  
-HET    SAH  A 501      26                                                       
-HET    37T  A 502      26                                                       
-HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
-HETNAM     37T THEOBROMINE                                                      
-HETSYN     37T 3,7-DIMETHYLXANTHINE, 3,7-DIMETHYLPURINE-2,6-DIONE               
-FORMUL   2  SAH    C14 H20 N6 O5 S                                              
-FORMUL   3  37T    C7 H8 N4 O2                                                  
-FORMUL   4  HOH   *146(H2 O)                                                    
-HELIX    1   1 SER A   17  SER A   22  1                                   6    
-HELIX    2   2 PHE A   27  ALA A   45  1                                  19    
-HELIX    3   3 GLY A   64  ASP A   79  1                                  16    
-HELIX    4   4 ASP A  105  ASN A  124  1                                  20    
-HELIX    5   5 ARG A  189  GLU A  214  1                                  26    
-HELIX    6   6 ASN A  236  GLU A  251  1                                  16    
-HELIX    7   7 GLU A  255  SER A  261  1                                   7    
-HELIX    8   8 SER A  270  GLY A  282  1                                  13    
-HELIX    9   9 VAL A  314  GLY A  342  1                                  29    
-HELIX   10  10 ILE A  345  GLY A  364  1                                  20    
-SHEET    1   A 7 CYS A 131  ALA A 135  0                                        
-SHEET    2   A 7 THR A  93  ASN A  99  1  N  ILE A  94   O  LEU A 132           
-SHEET    3   A 7 CYS A  53  LEU A  59  1  N  ASP A  58   O  ASN A  99           
-SHEET    4   A 7 MET A 150  CYS A 156  1  O  HIS A 154   N  LEU A  59           
-SHEET    5   A 7 LEU A 215  ILE A 226  1  O  ILE A 216   N  MET A 150           
-SHEET    6   A 7 PHE A 367  LYS A 377 -1  O  LEU A 375   N  MET A 221           
-SHEET    7   A 7 PHE A 284  PRO A 295 -1  N  ALA A 294   O  TYR A 368           
-SITE     1 AC1 22 LEU A   7  MET A   9  TYR A  18  GLY A  60                    
-SITE     2 AC1 22 CYS A  61  ALA A  62  ASN A  66  ASN A  99                    
-SITE     3 AC1 22 ASP A 100  GLY A 138  SER A 139  PHE A 140                    
-SITE     4 AC1 22 TYR A 141  CYS A 156  TYR A 157  CYS A 158                    
-SITE     5 AC1 22 37T A 502  HOH A 510  HOH A 517  HOH A 520                    
-SITE     6 AC1 22 HOH A 547  HOH A 647                                          
-SITE     1 AC2 13 TYR A  18  LEU A  26  PHE A  27  TYR A 157                    
-SITE     2 AC2 13 HIS A 160  TRP A 161  ILE A 226  SER A 237                    
-SITE     3 AC2 13 ILE A 332  TYR A 368  SAH A 501  HOH A 509                    
-SITE     4 AC2 13 HOH A 587                                                     
-CRYST1   50.160  105.630  140.950  90.00  90.00  90.00 C 2 2 21      8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.019936  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.009467  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.007095        0.00000                         
-ATOM      1  N   LEU A   3      18.115  22.517  43.440  0.75 46.59           N  
-ATOM      2  CA  LEU A   3      16.845  22.051  44.082  0.75 46.24           C  
-ATOM      3  C   LEU A   3      15.629  22.658  43.396  0.75 46.25           C  
-ATOM      4  O   LEU A   3      14.527  22.116  43.488  0.75 46.60           O  
-ATOM      5  CB  LEU A   3      16.793  22.411  45.570  0.75 46.31           C  
-ATOM      6  CG  LEU A   3      18.025  22.900  46.312  0.75 46.13           C  
-ATOM      7  CD1 LEU A   3      17.539  23.637  47.555  0.75 43.43           C  
-ATOM      8  CD2 LEU A   3      18.997  21.770  46.651  0.75 44.91           C  
-ATOM      9  N   GLN A   4      15.835  23.800  42.739  0.75 46.12           N  
-ATOM     10  CA  GLN A   4      14.815  24.473  41.928  0.75 45.99           C  
-ATOM     11  C   GLN A   4      14.005  23.468  41.101  0.75 46.04           C  
-ATOM     12  O   GLN A   4      12.792  23.622  40.930  0.75 46.14           O  
-ATOM     13  CB  GLN A   4      15.497  25.513  41.015  0.75 46.25           C  
-ATOM     14  CG  GLN A   4      14.578  26.262  40.026  0.75 45.73           C  
-ATOM     15  CD  GLN A   4      15.394  27.107  39.026  0.75 45.93           C  
-ATOM     16  OE1 GLN A   4      15.466  26.773  37.819  0.75 45.09           O  
-ATOM     17  NE2 GLN A   4      16.015  28.203  39.525  0.75 45.75           N  
-ATOM     18  N   GLU A   5      14.687  22.438  40.598  0.75 46.06           N  
-ATOM     19  CA  GLU A   5      14.051  21.407  39.781  0.75 45.82           C  
-ATOM     20  C   GLU A   5      13.916  20.036  40.458  0.75 45.77           C  
-ATOM     21  O   GLU A   5      13.602  19.040  39.802  0.75 45.93           O  
-ATOM     22  CB  GLU A   5      14.740  21.307  38.412  0.75 45.91           C  
-ATOM     23  CG  GLU A   5      14.183  22.310  37.408  0.75 45.60           C  
-ATOM     24  CD  GLU A   5      12.659  22.299  37.399  0.75 45.75           C  
-ATOM     25  OE1 GLU A   5      12.046  23.153  38.091  0.75 47.40           O  
-ATOM     26  OE2 GLU A   5      12.074  21.404  36.746  0.75 45.13           O  
-ATOM     27  N   VAL A   6      14.122  20.009  41.775  0.75 45.62           N  
-ATOM     28  CA  VAL A   6      14.054  18.781  42.571  0.75 45.41           C  
-ATOM     29  C   VAL A   6      13.060  18.938  43.729  0.75 44.95           C  
-ATOM     30  O   VAL A   6      12.280  18.023  44.006  0.75 44.79           O  
-ATOM     31  CB  VAL A   6      15.463  18.372  43.112  0.75 45.64           C  
-ATOM     32  CG1 VAL A   6      15.365  17.317  44.224  0.75 46.42           C  
-ATOM     33  CG2 VAL A   6      16.361  17.879  41.982  0.75 45.48           C  
-ATOM     34  N   LEU A   7      13.089  20.098  44.387  0.75 44.42           N  
-ATOM     35  CA  LEU A   7      12.282  20.338  45.580  0.75 44.13           C  
-ATOM     36  C   LEU A   7      10.805  20.572  45.271  0.75 44.05           C  
-ATOM     37  O   LEU A   7      10.443  21.338  44.373  0.75 43.66           O  
-ATOM     38  CB  LEU A   7      12.852  21.490  46.425  0.75 44.05           C  
-ATOM     39  CG  LEU A   7      12.352  21.780  47.861  0.75 44.34           C  
-ATOM     40  CD1 LEU A   7      11.199  22.748  47.869  0.75 43.47           C  
-ATOM     41  CD2 LEU A   7      11.978  20.534  48.655  0.75 43.77           C  
-ATOM     42  N   HIS A   8       9.970  19.876  46.036  0.75 43.70           N  
-ATOM     43  CA  HIS A   8       8.528  20.020  46.006  0.75 43.56           C  
-ATOM     44  C   HIS A   8       7.968  19.170  47.133  0.75 43.46           C  
-ATOM     45  O   HIS A   8       8.612  18.214  47.576  0.75 43.19           O  
-ATOM     46  CB  HIS A   8       7.943  19.568  44.669  0.75 43.66           C  
-ATOM     47  CG  HIS A   8       8.294  18.161  44.302  0.75 44.02           C  
-ATOM     48  ND1 HIS A   8       7.578  17.073  44.754  0.75 45.08           N  
-ATOM     49  CD2 HIS A   8       9.288  17.663  43.531  0.75 43.65           C  
-ATOM     50  CE1 HIS A   8       8.110  15.966  44.266  0.75 44.74           C  
-ATOM     51  NE2 HIS A   8       9.153  16.296  43.527  0.75 44.53           N  
-ATOM     52  N   MET A   9       6.774  19.532  47.599  0.75 43.22           N  
-ATOM     53  CA  MET A   9       6.062  18.718  48.576  0.75 43.47           C  
-ATOM     54  C   MET A   9       5.536  17.450  47.887  0.75 43.17           C  
-ATOM     55  O   MET A   9       5.432  17.401  46.652  0.75 43.18           O  
-ATOM     56  CB  MET A   9       4.923  19.526  49.228  0.75 43.81           C  
-ATOM     57  CG  MET A   9       5.353  20.844  49.919  0.75 43.25           C  
-ATOM     58  SD  MET A   9       6.548  20.611  51.276  0.75 45.85           S  
-ATOM     59  CE  MET A   9       8.131  20.676  50.418  0.75 40.33           C  
-ATOM     60  N   ASN A  10       5.229  16.427  48.681  0.75 43.08           N  
-ATOM     61  CA  ASN A  10       4.684  15.165  48.166  0.75 42.68           C  
-ATOM     62  C   ASN A  10       3.395  15.404  47.370  0.75 42.71           C  
-ATOM     63  O   ASN A  10       2.434  15.975  47.893  0.75 43.27           O  
-ATOM     64  CB  ASN A  10       4.412  14.209  49.332  0.75 42.62           C  
-ATOM     65  CG  ASN A  10       5.066  12.861  49.154  0.75 41.75           C  
-ATOM     66  OD1 ASN A  10       5.911  12.673  48.279  0.75 40.63           O  
-ATOM     67  ND2 ASN A  10       4.678  11.907  49.994  0.75 41.59           N  
-ATOM     68  N   GLY A  11       3.382  14.981  46.107  0.75 42.75           N  
-ATOM     69  CA  GLY A  11       2.256  15.236  45.201  0.75 42.56           C  
-ATOM     70  C   GLY A  11       0.998  14.462  45.545  0.75 42.37           C  
-ATOM     71  O   GLY A  11       0.307  13.963  44.661  0.75 42.05           O  
-ATOM     72  N   THR A  16       1.867   9.502  52.059  1.00 50.75           N  
-ATOM     73  CA  THR A  16       0.872  10.076  51.152  1.00 50.66           C  
-ATOM     74  C   THR A  16       1.101  11.579  50.900  1.00 50.42           C  
-ATOM     75  O   THR A  16       2.084  12.163  51.375  1.00 50.17           O  
-ATOM     76  CB  THR A  16      -0.601   9.784  51.607  1.00 50.63           C  
-ATOM     77  OG1 THR A  16      -0.735   9.991  53.020  1.00 50.45           O  
-ATOM     78  CG2 THR A  16      -1.001   8.346  51.275  1.00 51.04           C  
-ATOM     79  N   SER A  17       0.182  12.181  50.143  1.00 50.28           N  
-ATOM     80  CA  SER A  17       0.349  13.526  49.588  1.00 49.84           C  
-ATOM     81  C   SER A  17       0.359  14.649  50.628  1.00 49.84           C  
-ATOM     82  O   SER A  17      -0.172  14.496  51.738  1.00 49.55           O  
-ATOM     83  CB  SER A  17      -0.728  13.794  48.523  1.00 49.95           C  
-ATOM     84  OG  SER A  17      -2.039  13.743  49.065  1.00 49.20           O  
-ATOM     85  N   TYR A  18       0.985  15.769  50.255  1.00 49.59           N  
-ATOM     86  CA  TYR A  18       0.917  17.004  51.029  1.00 49.60           C  
-ATOM     87  C   TYR A  18      -0.533  17.501  51.096  1.00 49.67           C  
-ATOM     88  O   TYR A  18      -0.978  17.985  52.144  1.00 49.88           O  
-ATOM     89  CB  TYR A  18       1.840  18.087  50.453  1.00 49.41           C  
-ATOM     90  CG  TYR A  18       1.825  19.381  51.251  0.50 49.55           C  
-ATOM     91  CD1 TYR A  18       2.690  19.563  52.332  0.50 48.73           C  
-ATOM     92  CD2 TYR A  18       0.939  20.414  50.933  0.50 48.69           C  
-ATOM     93  CE1 TYR A  18       2.672  20.732  53.075  0.50 48.87           C  
-ATOM     94  CE2 TYR A  18       0.911  21.594  51.672  0.50 49.37           C  
-ATOM     95  CZ  TYR A  18       1.782  21.747  52.744  0.50 49.64           C  
-ATOM     96  OH  TYR A  18       1.767  22.907  53.492  0.50 49.02           O  
-ATOM     97  N   ALA A  19      -1.261  17.358  49.988  1.00 48.91           N  
-ATOM     98  CA  ALA A  19      -2.679  17.712  49.918  1.00 48.42           C  
-ATOM     99  C   ALA A  19      -3.536  17.016  50.996  1.00 48.30           C  
-ATOM    100  O   ALA A  19      -4.305  17.670  51.704  1.00 47.75           O  
-ATOM    101  CB  ALA A  19      -3.222  17.416  48.518  1.00 48.44           C  
-ATOM    102  N   LYS A  20      -3.395  15.696  51.126  1.00 48.40           N  
-ATOM    103  CA  LYS A  20      -4.221  14.934  52.067  1.00 48.76           C  
-ATOM    104  C   LYS A  20      -3.863  15.194  53.542  1.00 48.99           C  
-ATOM    105  O   LYS A  20      -4.740  15.126  54.418  1.00 49.29           O  
-ATOM    106  CB  LYS A  20      -4.161  13.434  51.744  1.00 48.95           C  
-ATOM    107  CG  LYS A  20      -4.854  12.523  52.753  1.00 49.09           C  
-ATOM    108  N   ASN A  21      -2.590  15.501  53.803  1.00 48.99           N  
-ATOM    109  CA  ASN A  21      -2.070  15.664  55.174  1.00 49.10           C  
-ATOM    110  C   ASN A  21      -1.997  17.112  55.697  1.00 48.85           C  
-ATOM    111  O   ASN A  21      -1.817  17.328  56.912  1.00 49.30           O  
-ATOM    112  CB  ASN A  21      -0.719  14.946  55.315  1.00 49.13           C  
-ATOM    113  CG  ASN A  21      -0.848  13.436  55.201  1.00 50.21           C  
-ATOM    114  OD1 ASN A  21      -1.380  12.773  56.101  1.00 50.61           O  
-ATOM    115  ND2 ASN A  21      -0.364  12.881  54.090  1.00 50.69           N  
-ATOM    116  N   SER A  22      -2.176  18.075  54.782  1.00 48.32           N  
-ATOM    117  CA ASER A  22      -2.189  19.521  55.079  0.50 48.08           C  
-ATOM    118  CA BSER A  22      -2.164  19.506  55.120  0.50 47.94           C  
-ATOM    119  C   SER A  22      -3.389  19.921  55.928  1.00 48.07           C  
-ATOM    120  O   SER A  22      -4.380  19.181  56.012  1.00 48.39           O  
-ATOM    121  CB ASER A  22      -2.220  20.337  53.779  0.50 47.99           C  
-ATOM    122  CB BSER A  22      -2.062  20.360  53.855  0.50 47.85           C  
-ATOM    123  OG ASER A  22      -0.925  20.526  53.224  0.50 47.85           O  
-ATOM    124  OG BSER A  22      -3.031  19.977  52.899  0.50 46.76           O  
-ATOM    125  N   SER A  23      -3.316  21.100  56.543  1.00 47.34           N  
-ATOM    126  CA  SER A  23      -4.441  21.593  57.314  1.00 46.63           C  
-ATOM    127  C   SER A  23      -4.361  23.078  57.495  1.00 46.23           C  
-ATOM    128  O   SER A  23      -3.296  23.634  57.772  1.00 46.08           O  
-ATOM    129  CB  SER A  23      -4.546  20.923  58.695  1.00 46.71           C  
-ATOM    130  OG  SER A  23      -5.743  21.336  59.346  1.00 46.11           O  
-ATOM    131  N   TYR A  24      -5.520  23.702  57.344  1.00 45.75           N  
-ATOM    132  CA  TYR A  24      -5.690  25.106  57.596  1.00 45.66           C  
-ATOM    133  C   TYR A  24      -5.334  25.402  59.054  1.00 45.54           C  
-ATOM    134  O   TYR A  24      -4.763  26.456  59.360  1.00 45.67           O  
-ATOM    135  CB  TYR A  24      -7.143  25.484  57.307  1.00 45.39           C  
-ATOM    136  CG  TYR A  24      -7.379  26.957  57.319  1.00 45.53           C  
-ATOM    137  CD1 TYR A  24      -7.924  27.574  58.434  1.00 45.13           C  
-ATOM    138  CD2 TYR A  24      -7.046  27.743  56.218  1.00 44.00           C  
-ATOM    139  CE1 TYR A  24      -8.139  28.931  58.454  1.00 45.29           C  
-ATOM    140  CE2 TYR A  24      -7.240  29.104  56.238  1.00 43.50           C  
-ATOM    141  CZ  TYR A  24      -7.794  29.689  57.363  1.00 44.39           C  
-ATOM    142  OH  TYR A  24      -8.014  31.038  57.415  1.00 45.00           O  
-ATOM    143  N   ASN A  25      -5.651  24.441  59.927  1.00 45.39           N  
-ATOM    144  CA  ASN A  25      -5.555  24.578  61.379  1.00 45.42           C  
-ATOM    145  C   ASN A  25      -4.137  24.643  61.950  1.00 45.04           C  
-ATOM    146  O   ASN A  25      -3.964  24.826  63.161  1.00 45.49           O  
-ATOM    147  CB  ASN A  25      -6.301  23.426  62.067  1.00 45.40           C  
-ATOM    148  CG  ASN A  25      -7.812  23.508  61.913  1.00 46.52           C  
-ATOM    149  OD1 ASN A  25      -8.363  24.479  61.377  1.00 49.85           O  
-ATOM    150  ND2 ASN A  25      -8.495  22.477  62.393  1.00 47.77           N  
-ATOM    151  N   LEU A  26      -3.125  24.481  61.106  1.00 44.25           N  
-ATOM    152  CA  LEU A  26      -1.766  24.424  61.623  1.00 43.44           C  
-ATOM    153  C   LEU A  26      -1.161  25.816  61.658  1.00 43.14           C  
-ATOM    154  O   LEU A  26      -0.859  26.327  62.736  1.00 42.37           O  
-ATOM    155  CB  LEU A  26      -0.910  23.427  60.835  1.00 43.23           C  
-ATOM    156  CG  LEU A  26       0.286  22.717  61.479  1.00 43.70           C  
-ATOM    157  CD1 LEU A  26      -0.051  21.991  62.779  1.00 41.11           C  
-ATOM    158  CD2 LEU A  26       0.920  21.723  60.498  1.00 43.12           C  
-ATOM    159  N   PHE A  27      -1.021  26.442  60.493  1.00 42.55           N  
-ATOM    160  CA  PHE A  27      -0.425  27.777  60.428  1.00 43.82           C  
-ATOM    161  C   PHE A  27      -1.379  28.839  59.869  1.00 44.65           C  
-ATOM    162  O   PHE A  27      -1.456  29.959  60.408  1.00 44.40           O  
-ATOM    163  CB  PHE A  27       0.907  27.755  59.647  1.00 42.90           C  
-ATOM    164  CG  PHE A  27       1.842  26.629  60.058  1.00 42.99           C  
-ATOM    165  CD1 PHE A  27       2.421  26.599  61.337  1.00 40.87           C  
-ATOM    166  CD2 PHE A  27       2.155  25.613  59.164  1.00 41.70           C  
-ATOM    167  CE1 PHE A  27       3.277  25.560  61.726  1.00 41.76           C  
-ATOM    168  CE2 PHE A  27       3.008  24.569  59.536  1.00 42.08           C  
-ATOM    169  CZ  PHE A  27       3.573  24.537  60.816  1.00 41.19           C  
-ATOM    170  N   LEU A  28      -2.135  28.487  58.828  1.00 45.71           N  
-ATOM    171  CA  LEU A  28      -2.999  29.480  58.151  1.00 46.69           C  
-ATOM    172  C   LEU A  28      -4.016  30.192  59.049  1.00 46.45           C  
-ATOM    173  O   LEU A  28      -4.177  31.415  58.924  1.00 46.06           O  
-ATOM    174  CB  LEU A  28      -3.652  28.906  56.880  1.00 47.31           C  
-ATOM    175  CG  LEU A  28      -2.697  28.554  55.742  1.00 48.96           C  
-ATOM    176  CD1 LEU A  28      -3.423  27.920  54.553  1.00 51.07           C  
-ATOM    177  CD2 LEU A  28      -1.896  29.774  55.278  1.00 49.20           C  
-ATOM    178  N   ILE A  29      -4.662  29.482  59.981  1.00 47.11           N  
-ATOM    179  CA  ILE A  29      -5.549  30.173  60.953  1.00 47.17           C  
-ATOM    180  C   ILE A  29      -4.844  31.229  61.815  1.00 46.93           C  
-ATOM    181  O   ILE A  29      -5.469  32.185  62.260  1.00 47.51           O  
-ATOM    182  CB  ILE A  29      -6.322  29.244  61.930  1.00 48.14           C  
-ATOM    183  CG1 ILE A  29      -5.633  27.906  62.118  1.00 48.31           C  
-ATOM    184  CG2 ILE A  29      -7.829  29.180  61.604  1.00 48.63           C  
-ATOM    185  CD1 ILE A  29      -4.731  27.901  63.323  1.00 51.28           C  
-ATOM    186  N   ARG A  30      -3.555  31.051  62.067  1.00 46.49           N  
-ATOM    187  CA  ARG A  30      -2.793  32.041  62.818  1.00 45.86           C  
-ATOM    188  C   ARG A  30      -2.425  33.224  61.916  1.00 45.11           C  
-ATOM    189  O   ARG A  30      -2.363  34.366  62.373  1.00 45.72           O  
-ATOM    190  CB  ARG A  30      -1.541  31.410  63.430  1.00 45.85           C  
-ATOM    191  CG  ARG A  30      -1.779  30.072  64.143  1.00 47.13           C  
-ATOM    192  CD  ARG A  30      -2.793  30.159  65.306  1.00 49.33           C  
-ATOM    193  NE  ARG A  30      -2.291  30.836  66.505  1.00 48.96           N  
-ATOM    194  CZ  ARG A  30      -1.511  30.276  67.426  1.00 47.78           C  
-ATOM    195  NH1 ARG A  30      -1.096  29.017  67.291  1.00 45.12           N  
-ATOM    196  NH2 ARG A  30      -1.136  30.989  68.486  1.00 45.01           N  
-ATOM    197  N   VAL A  31      -2.203  32.932  60.637  1.00 44.02           N  
-ATOM    198  CA  VAL A  31      -1.875  33.937  59.617  1.00 42.98           C  
-ATOM    199  C   VAL A  31      -3.090  34.817  59.296  1.00 43.21           C  
-ATOM    200  O   VAL A  31      -2.961  36.045  59.192  1.00 42.97           O  
-ATOM    201  CB  VAL A  31      -1.373  33.262  58.285  1.00 42.93           C  
-ATOM    202  CG1 VAL A  31      -1.144  34.301  57.201  1.00 43.05           C  
-ATOM    203  CG2 VAL A  31      -0.099  32.455  58.505  1.00 41.17           C  
-ATOM    204  N   LYS A  32      -4.252  34.176  59.139  1.00 43.12           N  
-ATOM    205  CA  LYS A  32      -5.510  34.829  58.749  1.00 44.48           C  
-ATOM    206  C   LYS A  32      -5.779  36.218  59.358  1.00 44.03           C  
-ATOM    207  O   LYS A  32      -5.958  37.165  58.608  1.00 45.01           O  
-ATOM    208  CB  LYS A  32      -6.716  33.906  58.994  1.00 44.99           C  
-ATOM    209  CG  LYS A  32      -8.018  34.466  58.401  1.00 48.63           C  
-ATOM    210  CD  LYS A  32      -9.193  33.598  58.762  1.00 54.66           C  
-ATOM    211  CE  LYS A  32     -10.246  33.637  57.667  1.00 55.94           C  
-ATOM    212  NZ  LYS A  32     -11.158  34.806  57.826  1.00 56.87           N  
-ATOM    213  N   PRO A  33      -5.833  36.347  60.711  1.00 43.39           N  
-ATOM    214  CA  PRO A  33      -6.094  37.690  61.235  1.00 42.46           C  
-ATOM    215  C   PRO A  33      -5.053  38.744  60.815  1.00 41.85           C  
-ATOM    216  O   PRO A  33      -5.412  39.922  60.618  1.00 40.72           O  
-ATOM    217  CB  PRO A  33      -6.086  37.494  62.763  1.00 42.55           C  
-ATOM    218  CG  PRO A  33      -5.325  36.201  62.981  1.00 43.42           C  
-ATOM    219  CD  PRO A  33      -5.671  35.357  61.793  1.00 43.07           C  
-ATOM    220  N   VAL A  34      -3.788  38.334  60.703  1.00 40.42           N  
-ATOM    221  CA  VAL A  34      -2.712  39.245  60.331  1.00 40.67           C  
-ATOM    222  C   VAL A  34      -2.817  39.593  58.828  1.00 41.30           C  
-ATOM    223  O   VAL A  34      -2.595  40.737  58.446  1.00 40.81           O  
-ATOM    224  CB  VAL A  34      -1.324  38.656  60.661  1.00 40.84           C  
-ATOM    225  CG1 VAL A  34      -0.192  39.621  60.254  1.00 40.58           C  
-ATOM    226  CG2 VAL A  34      -1.229  38.299  62.142  1.00 39.96           C  
-ATOM    227  N   LEU A  35      -3.222  38.622  58.042  1.00 41.85           N  
-ATOM    228  CA  LEU A  35      -3.473  38.766  56.638  1.00 42.75           C  
-ATOM    229  C   LEU A  35      -4.590  39.752  56.431  1.00 43.52           C  
-ATOM    230  O   LEU A  35      -4.505  40.620  55.607  1.00 43.02           O  
-ATOM    231  CB  LEU A  35      -3.815  37.419  56.018  1.00 42.75           C  
-ATOM    232  CG  LEU A  35      -4.262  37.318  54.563  1.00 44.24           C  
-ATOM    233  CD1 LEU A  35      -3.240  37.728  53.604  1.00 45.94           C  
-ATOM    234  CD2 LEU A  35      -4.768  36.031  54.204  1.00 45.54           C  
-ATOM    235  N   GLU A  36      -5.626  39.605  57.225  1.00 44.50           N  
-ATOM    236  CA  GLU A  36      -6.820  40.414  57.111  1.00 45.43           C  
-ATOM    237  C   GLU A  36      -6.514  41.885  57.377  1.00 45.83           C  
-ATOM    238  O   GLU A  36      -6.979  42.769  56.638  1.00 45.55           O  
-ATOM    239  CB  GLU A  36      -7.915  39.905  58.048  1.00 46.34           C  
-ATOM    240  CG  GLU A  36      -8.521  38.551  57.653  1.00 49.87           C  
-ATOM    241  CD  GLU A  36     -10.046  38.539  57.748  1.00 55.20           C  
-ATOM    242  OE1 GLU A  36     -10.597  38.788  58.854  1.00 56.26           O  
-ATOM    243  OE2 GLU A  36     -10.695  38.299  56.698  1.00 57.22           O  
-ATOM    244  N   GLN A  37      -5.716  42.129  58.415  1.00 45.89           N  
-ATOM    245  CA  GLN A  37      -5.361  43.475  58.848  1.00 47.01           C  
-ATOM    246  C   GLN A  37      -4.442  44.099  57.814  1.00 46.79           C  
-ATOM    247  O   GLN A  37      -4.593  45.261  57.460  1.00 46.75           O  
-ATOM    248  CB  GLN A  37      -4.684  43.422  60.227  1.00 46.88           C  
-ATOM    249  CG  GLN A  37      -4.044  44.720  60.690  1.00 47.98           C  
-ATOM    250  CD  GLN A  37      -3.591  44.662  62.140  1.00 48.58           C  
-ATOM    251  OE1 GLN A  37      -4.400  44.484  63.047  1.00 50.87           O  
-ATOM    252  NE2 GLN A  37      -2.292  44.819  62.363  1.00 51.58           N  
-ATOM    253  N   CYS A  38      -3.516  43.294  57.304  1.00 47.47           N  
-ATOM    254  CA  CYS A  38      -2.583  43.745  56.282  1.00 46.66           C  
-ATOM    255  C   CYS A  38      -3.318  44.230  55.027  1.00 45.46           C  
-ATOM    256  O   CYS A  38      -3.105  45.363  54.575  1.00 45.38           O  
-ATOM    257  CB  CYS A  38      -1.605  42.631  55.943  1.00 47.34           C  
-ATOM    258  SG  CYS A  38      -0.306  43.171  54.872  1.00 50.70           S  
-ATOM    259  N   ILE A  39      -4.209  43.392  54.501  1.00 43.29           N  
-ATOM    260  CA  ILE A  39      -4.977  43.732  53.315  1.00 42.31           C  
-ATOM    261  C   ILE A  39      -5.887  44.968  53.488  1.00 42.08           C  
-ATOM    262  O   ILE A  39      -5.891  45.844  52.635  1.00 41.63           O  
-ATOM    263  CB  ILE A  39      -5.727  42.508  52.754  1.00 42.40           C  
-ATOM    264  CG1 ILE A  39      -4.736  41.619  51.985  1.00 41.89           C  
-ATOM    265  CG2 ILE A  39      -6.895  42.934  51.842  1.00 41.36           C  
-ATOM    266  CD1 ILE A  39      -5.167  40.185  51.882  1.00 43.33           C  
-ATOM    267  N   GLN A  40      -6.621  45.039  54.595  1.00 42.49           N  
-ATOM    268  CA  GLN A  40      -7.451  46.217  54.926  1.00 43.43           C  
-ATOM    269  C   GLN A  40      -6.646  47.515  55.019  1.00 43.23           C  
-ATOM    270  O   GLN A  40      -7.116  48.579  54.605  1.00 43.61           O  
-ATOM    271  CB  GLN A  40      -8.229  45.961  56.221  1.00 43.82           C  
-ATOM    272  CG  GLN A  40      -9.310  44.884  56.061  1.00 47.62           C  
-ATOM    273  CD  GLN A  40     -10.494  45.365  55.227  1.00 51.50           C  
-ATOM    274  OE1 GLN A  40     -11.221  46.265  55.639  1.00 54.06           O  
-ATOM    275  NE2 GLN A  40     -10.692  44.763  54.056  1.00 51.66           N  
-ATOM    276  N   GLU A  41      -5.434  47.424  55.562  1.00 43.45           N  
-ATOM    277  CA  GLU A  41      -4.530  48.572  55.666  1.00 43.59           C  
-ATOM    278  C   GLU A  41      -4.050  49.005  54.287  1.00 43.05           C  
-ATOM    279  O   GLU A  41      -3.914  50.206  54.010  1.00 42.67           O  
-ATOM    280  CB  GLU A  41      -3.343  48.265  56.581  1.00 43.78           C  
-ATOM    281  CG  GLU A  41      -3.764  47.793  57.973  1.00 46.63           C  
-ATOM    282  CD  GLU A  41      -2.696  47.967  59.040  1.00 47.87           C  
-ATOM    283  OE1 GLU A  41      -1.498  48.004  58.703  1.00 48.31           O  
-ATOM    284  OE2 GLU A  41      -3.068  48.081  60.227  1.00 48.85           O  
-ATOM    285  N   LEU A  42      -3.832  48.029  53.415  1.00 42.89           N  
-ATOM    286  CA  LEU A  42      -3.452  48.298  52.033  1.00 42.60           C  
-ATOM    287  C   LEU A  42      -4.503  49.073  51.235  1.00 42.58           C  
-ATOM    288  O   LEU A  42      -4.172  50.013  50.518  1.00 41.27           O  
-ATOM    289  CB  LEU A  42      -3.125  46.991  51.324  1.00 43.57           C  
-ATOM    290  CG  LEU A  42      -1.683  46.531  51.449  1.00 42.51           C  
-ATOM    291  CD1 LEU A  42      -1.563  45.094  51.029  1.00 41.35           C  
-ATOM    292  CD2 LEU A  42      -0.853  47.393  50.563  1.00 43.32           C  
-ATOM    293  N   LEU A  43      -5.759  48.653  51.339  1.00 43.03           N  
-ATOM    294  CA  LEU A  43      -6.859  49.342  50.656  1.00 44.21           C  
-ATOM    295  C   LEU A  43      -6.995  50.776  51.154  1.00 44.02           C  
-ATOM    296  O   LEU A  43      -7.246  51.679  50.372  1.00 45.24           O  
-ATOM    297  CB  LEU A  43      -8.183  48.607  50.865  1.00 44.89           C  
-ATOM    298  CG  LEU A  43      -8.333  47.171  50.374  1.00 45.40           C  
-ATOM    299  CD1 LEU A  43      -9.484  46.524  51.121  1.00 46.34           C  
-ATOM    300  CD2 LEU A  43      -8.553  47.130  48.877  1.00 48.03           C  
-ATOM    301  N   ARG A  44      -6.799  50.964  52.456  1.00 43.86           N  
-ATOM    302  CA  ARG A  44      -6.894  52.261  53.102  1.00 43.48           C  
-ATOM    303  C   ARG A  44      -5.746  53.195  52.732  1.00 43.13           C  
-ATOM    304  O   ARG A  44      -5.931  54.405  52.674  1.00 42.88           O  
-ATOM    305  CB  ARG A  44      -6.994  52.078  54.611  1.00 43.86           C  
-ATOM    306  CG  ARG A  44      -8.397  51.721  55.024  1.00 45.78           C  
-ATOM    307  CD  ARG A  44      -8.518  51.053  56.387  1.00 46.50           C  
-ATOM    308  NE  ARG A  44      -9.934  50.807  56.668  1.00 49.26           N  
-ATOM    309  CZ  ARG A  44     -10.711  49.985  55.957  1.00 51.10           C  
-ATOM    310  NH1 ARG A  44     -10.214  49.300  54.923  1.00 51.43           N  
-ATOM    311  NH2 ARG A  44     -11.990  49.846  56.276  1.00 52.31           N  
-ATOM    312  N   ALA A  45      -4.586  52.611  52.444  1.00 42.28           N  
-ATOM    313  CA  ALA A  45      -3.391  53.329  51.982  1.00 42.09           C  
-ATOM    314  C   ALA A  45      -3.499  53.869  50.543  1.00 41.86           C  
-ATOM    315  O   ALA A  45      -2.666  54.681  50.117  1.00 41.73           O  
-ATOM    316  CB  ALA A  45      -2.163  52.423  52.114  1.00 42.29           C  
-ATOM    317  N   ASN A  46      -4.517  53.418  49.808  1.00 41.46           N  
-ATOM    318  CA  ASN A  46      -4.831  53.926  48.466  1.00 40.97           C  
-ATOM    319  C   ASN A  46      -3.641  53.812  47.489  1.00 40.97           C  
-ATOM    320  O   ASN A  46      -3.297  54.778  46.794  1.00 40.83           O  
-ATOM    321  CB  ASN A  46      -5.379  55.375  48.552  1.00 41.67           C  
-ATOM    322  CG  ASN A  46      -6.169  55.785  47.320  1.00 42.86           C  
-ATOM    323  OD1 ASN A  46      -6.774  54.950  46.655  1.00 44.30           O  
-ATOM    324  ND2 ASN A  46      -6.169  57.080  47.012  1.00 44.61           N  
-ATOM    325  N   LEU A  47      -3.005  52.653  47.419  1.00 40.77           N  
-ATOM    326  CA  LEU A  47      -1.905  52.455  46.483  1.00 40.79           C  
-ATOM    327  C   LEU A  47      -2.370  52.664  45.030  1.00 41.57           C  
-ATOM    328  O   LEU A  47      -3.477  52.368  44.740  1.00 40.46           O  
-ATOM    329  CB  LEU A  47      -1.318  51.050  46.699  1.00 40.74           C  
-ATOM    330  CG  LEU A  47      -0.303  50.748  47.809  1.00 40.43           C  
-ATOM    331  CD1 LEU A  47      -0.770  51.025  49.160  1.00 37.72           C  
-ATOM    332  CD2 LEU A  47       0.209  49.333  47.731  1.00 38.44           C  
-ATOM    333  N   PRO A  48      -1.531  53.134  44.111  1.00 42.92           N  
-ATOM    334  CA  PRO A  48      -2.054  53.371  42.765  1.00 44.24           C  
-ATOM    335  C   PRO A  48      -2.745  52.151  42.165  1.00 44.49           C  
-ATOM    336  O   PRO A  48      -2.231  51.033  42.242  1.00 45.24           O  
-ATOM    337  CB  PRO A  48      -0.811  53.773  41.934  1.00 44.32           C  
-ATOM    338  CG  PRO A  48       0.367  53.488  42.768  1.00 43.81           C  
-ATOM    339  CD  PRO A  48      -0.107  53.503  44.219  1.00 43.48           C  
-ATOM    340  N   ASN A  49      -3.932  52.377  41.611  1.00 45.62           N  
-ATOM    341  CA  ASN A  49      -4.714  51.336  40.923  1.00 46.72           C  
-ATOM    342  C   ASN A  49      -5.325  50.206  41.777  1.00 46.03           C  
-ATOM    343  O   ASN A  49      -6.065  49.385  41.262  1.00 46.54           O  
-ATOM    344  CB  ASN A  49      -3.919  50.781  39.736  1.00 47.19           C  
-ATOM    345  CG  ASN A  49      -3.472  51.885  38.785  1.00 50.47           C  
-ATOM    346  OD1 ASN A  49      -4.273  52.746  38.400  1.00 53.20           O  
-ATOM    347  ND2 ASN A  49      -2.190  51.879  38.416  1.00 52.23           N  
-ATOM    348  N   ILE A  50      -5.060  50.193  43.080  1.00 45.59           N  
-ATOM    349  CA  ILE A  50      -5.552  49.122  43.955  1.00 45.12           C  
-ATOM    350  C   ILE A  50      -7.094  48.959  43.995  1.00 45.60           C  
-ATOM    351  O   ILE A  50      -7.608  47.861  44.206  1.00 45.09           O  
-ATOM    352  CB  ILE A  50      -4.950  49.247  45.394  1.00 45.55           C  
-ATOM    353  CG1 ILE A  50      -4.887  47.875  46.084  1.00 43.88           C  
-ATOM    354  CG2 ILE A  50      -5.695  50.305  46.225  1.00 44.09           C  
-ATOM    355  CD1 ILE A  50      -4.086  47.871  47.368  1.00 44.19           C  
-ATOM    356  N   ASN A  51      -7.828  50.044  43.789  1.00 45.62           N  
-ATOM    357  CA  ASN A  51      -9.280  49.949  43.738  1.00 46.16           C  
-ATOM    358  C   ASN A  51      -9.828  49.639  42.339  1.00 45.70           C  
-ATOM    359  O   ASN A  51     -11.030  49.497  42.164  1.00 46.94           O  
-ATOM    360  CB  ASN A  51      -9.930  51.191  44.365  1.00 46.54           C  
-ATOM    361  CG  ASN A  51      -9.513  51.392  45.816  1.00 48.29           C  
-ATOM    362  OD1 ASN A  51      -9.475  50.441  46.620  1.00 48.94           O  
-ATOM    363  ND2 ASN A  51      -9.184  52.626  46.159  1.00 49.17           N  
-ATOM    364  N   LYS A  52      -8.941  49.544  41.352  1.00 45.38           N  
-ATOM    365  CA  LYS A  52      -9.285  49.023  40.025  1.00 43.95           C  
-ATOM    366  C   LYS A  52      -8.935  47.533  40.017  1.00 42.97           C  
-ATOM    367  O   LYS A  52      -9.816  46.684  39.893  1.00 42.33           O  
-ATOM    368  CB  LYS A  52      -8.501  49.749  38.925  1.00 43.75           C  
-ATOM    369  N   CYS A  53      -7.647  47.237  40.164  1.00 42.33           N  
-ATOM    370  CA  CYS A  53      -7.159  45.860  40.216  1.00 41.26           C  
-ATOM    371  C   CYS A  53      -6.131  45.643  41.325  1.00 40.89           C  
-ATOM    372  O   CYS A  53      -5.045  46.231  41.303  1.00 40.98           O  
-ATOM    373  CB  CYS A  53      -6.578  45.429  38.866  1.00 41.51           C  
-ATOM    374  SG  CYS A  53      -6.210  43.698  38.825  1.00 44.22           S  
-ATOM    375  N   PHE A  54      -6.484  44.772  42.267  1.00 39.91           N  
-ATOM    376  CA  PHE A  54      -5.634  44.384  43.404  1.00 40.21           C  
-ATOM    377  C   PHE A  54      -4.767  43.204  42.966  1.00 39.98           C  
-ATOM    378  O   PHE A  54      -5.264  42.107  42.777  1.00 38.85           O  
-ATOM    379  CB  PHE A  54      -6.519  43.999  44.610  1.00 39.86           C  
-ATOM    380  CG  PHE A  54      -5.814  44.036  45.959  1.00 40.91           C  
-ATOM    381  CD1 PHE A  54      -4.583  43.419  46.155  1.00 42.26           C  
-ATOM    382  CD2 PHE A  54      -6.430  44.641  47.058  1.00 43.76           C  
-ATOM    383  CE1 PHE A  54      -3.946  43.433  47.405  1.00 42.38           C  
-ATOM    384  CE2 PHE A  54      -5.800  44.647  48.324  1.00 44.34           C  
-ATOM    385  CZ  PHE A  54      -4.543  44.033  48.474  1.00 43.81           C  
-ATOM    386  N   LYS A  55      -3.473  43.446  42.745  1.00 40.20           N  
-ATOM    387  CA  LYS A  55      -2.577  42.383  42.244  1.00 40.65           C  
-ATOM    388  C   LYS A  55      -1.803  41.726  43.371  1.00 40.94           C  
-ATOM    389  O   LYS A  55      -1.113  42.433  44.129  1.00 40.54           O  
-ATOM    390  CB  LYS A  55      -1.634  42.952  41.172  1.00 41.63           C  
-ATOM    391  CG  LYS A  55      -2.405  43.400  39.932  1.00 43.84           C  
-ATOM    392  CD  LYS A  55      -1.541  44.127  38.920  1.00 47.62           C  
-ATOM    393  CE  LYS A  55      -0.524  43.145  38.279  1.00 48.29           C  
-ATOM    394  NZ  LYS A  55       0.450  43.897  37.423  0.50 47.81           N  
-ATOM    395  N   VAL A  56      -1.935  40.385  43.493  1.00 40.51           N  
-ATOM    396  CA  VAL A  56      -1.431  39.624  44.624  1.00 40.98           C  
-ATOM    397  C   VAL A  56      -0.693  38.376  44.120  1.00 41.70           C  
-ATOM    398  O   VAL A  56      -1.134  37.759  43.159  1.00 41.71           O  
-ATOM    399  CB  VAL A  56      -2.580  39.085  45.531  1.00 41.36           C  
-ATOM    400  CG1 VAL A  56      -1.999  38.386  46.765  1.00 40.81           C  
-ATOM    401  CG2 VAL A  56      -3.518  40.197  45.954  1.00 41.00           C  
-ATOM    402  N   GLY A  57       0.431  38.043  44.761  1.00 42.15           N  
-ATOM    403  CA  GLY A  57       1.191  36.810  44.495  1.00 42.26           C  
-ATOM    404  C   GLY A  57       1.232  35.923  45.735  1.00 43.68           C  
-ATOM    405  O   GLY A  57       1.427  36.424  46.850  1.00 44.16           O  
-ATOM    406  N   ASP A  58       1.021  34.613  45.567  1.00 44.11           N  
-ATOM    407  CA  ASP A  58       1.245  33.643  46.664  1.00 45.15           C  
-ATOM    408  C   ASP A  58       2.489  32.826  46.315  1.00 45.08           C  
-ATOM    409  O   ASP A  58       2.507  32.122  45.324  1.00 43.47           O  
-ATOM    410  CB  ASP A  58       0.038  32.717  46.913  1.00 45.49           C  
-ATOM    411  CG  ASP A  58       0.220  31.818  48.158  1.00 48.70           C  
-ATOM    412  OD1 ASP A  58       0.952  32.186  49.118  1.00 46.97           O  
-ATOM    413  OD2 ASP A  58      -0.371  30.713  48.169  1.00 52.65           O  
-ATOM    414  N   LEU A  59       3.546  33.017  47.104  1.00 45.48           N  
-ATOM    415  CA  LEU A  59       4.884  32.567  46.757  1.00 45.93           C  
-ATOM    416  C   LEU A  59       5.127  31.303  47.555  1.00 46.59           C  
-ATOM    417  O   LEU A  59       5.309  31.372  48.785  1.00 47.10           O  
-ATOM    418  CB  LEU A  59       5.933  33.626  47.127  1.00 45.77           C  
-ATOM    419  CG  LEU A  59       5.815  35.046  46.571  1.00 46.99           C  
-ATOM    420  CD1 LEU A  59       7.087  35.859  46.861  1.00 45.66           C  
-ATOM    421  CD2 LEU A  59       5.503  35.047  45.074  1.00 45.41           C  
-ATOM    422  N   GLY A  60       5.074  30.175  46.852  1.00 47.13           N  
-ATOM    423  CA  GLY A  60       5.218  28.814  47.418  1.00 48.86           C  
-ATOM    424  C   GLY A  60       3.844  28.260  47.770  1.00 49.22           C  
-ATOM    425  O   GLY A  60       3.607  27.787  48.896  1.00 49.94           O  
-ATOM    426  N   CYS A  61       2.934  28.336  46.807  1.00 49.87           N  
-ATOM    427  CA  CYS A  61       1.536  27.973  47.017  1.00 51.67           C  
-ATOM    428  C   CYS A  61       1.344  26.476  47.236  1.00 52.17           C  
-ATOM    429  O   CYS A  61       0.345  26.069  47.844  1.00 52.23           O  
-ATOM    430  CB  CYS A  61       0.670  28.432  45.835  1.00 52.07           C  
-ATOM    431  SG  CYS A  61       1.140  27.727  44.236  1.00 53.82           S  
-ATOM    432  N   ALA A  62       2.291  25.681  46.743  1.00 52.42           N  
-ATOM    433  CA  ALA A  62       2.167  24.206  46.694  1.00 54.12           C  
-ATOM    434  C   ALA A  62       0.901  23.789  45.936  1.00 54.90           C  
-ATOM    435  O   ALA A  62       0.562  24.369  44.905  1.00 55.65           O  
-ATOM    436  CB  ALA A  62       2.201  23.590  48.118  1.00 52.89           C  
-ATOM    437  N   SER A  63       0.211  22.789  46.467  1.00 56.84           N  
-ATOM    438  CA  SER A  63      -1.097  22.337  45.990  1.00 57.66           C  
-ATOM    439  C   SER A  63      -1.916  21.901  47.201  1.00 57.74           C  
-ATOM    440  O   SER A  63      -1.415  21.874  48.347  1.00 58.22           O  
-ATOM    441  CB  SER A  63      -0.948  21.142  45.045  1.00 58.04           C  
-ATOM    442  OG  SER A  63      -0.145  21.476  43.925  1.00 58.84           O  
-ATOM    443  N   GLY A  64      -3.163  21.532  46.942  1.00 57.02           N  
-ATOM    444  CA  GLY A  64      -4.031  21.005  47.971  1.00 56.54           C  
-ATOM    445  C   GLY A  64      -4.973  22.056  48.512  1.00 56.60           C  
-ATOM    446  O   GLY A  64      -5.026  23.190  47.989  1.00 56.05           O  
-ATOM    447  N   PRO A  65      -5.726  21.700  49.563  1.00 56.03           N  
-ATOM    448  CA  PRO A  65      -6.689  22.632  50.137  1.00 55.91           C  
-ATOM    449  C   PRO A  65      -6.060  23.964  50.539  1.00 55.36           C  
-ATOM    450  O   PRO A  65      -6.674  25.001  50.318  1.00 55.25           O  
-ATOM    451  CB  PRO A  65      -7.185  21.885  51.369  1.00 55.73           C  
-ATOM    452  CG  PRO A  65      -7.039  20.448  50.975  1.00 56.61           C  
-ATOM    453  CD  PRO A  65      -5.739  20.408  50.273  1.00 56.21           C  
-ATOM    454  N   ASN A  66      -4.855  23.926  51.118  1.00 54.19           N  
-ATOM    455  CA  ASN A  66      -4.176  25.145  51.553  1.00 53.73           C  
-ATOM    456  C   ASN A  66      -4.017  26.213  50.467  1.00 52.74           C  
-ATOM    457  O   ASN A  66      -4.106  27.404  50.767  1.00 52.99           O  
-ATOM    458  CB  ASN A  66      -2.825  24.825  52.191  1.00 53.58           C  
-ATOM    459  CG  ASN A  66      -2.964  24.238  53.595  1.00 53.77           C  
-ATOM    460  OD1 ASN A  66      -4.062  24.149  54.136  1.00 53.36           O  
-ATOM    461  ND2 ASN A  66      -1.839  23.833  54.187  1.00 53.31           N  
-ATOM    462  N   THR A  67      -3.770  25.783  49.233  1.00 51.87           N  
-ATOM    463  CA  THR A  67      -3.665  26.700  48.069  1.00 52.12           C  
-ATOM    464  C   THR A  67      -4.962  27.507  47.921  1.00 51.15           C  
-ATOM    465  O   THR A  67      -4.946  28.717  47.951  1.00 51.40           O  
-ATOM    466  CB  THR A  67      -3.358  25.939  46.772  1.00 51.26           C  
-ATOM    467  OG1 THR A  67      -2.210  25.115  46.982  1.00 54.08           O  
-ATOM    468  CG2 THR A  67      -3.057  26.907  45.615  1.00 51.91           C  
-ATOM    469  N   PHE A  68      -6.079  26.793  47.821  1.00 51.10           N  
-ATOM    470  CA  PHE A  68      -7.406  27.379  47.784  1.00 49.67           C  
-ATOM    471  C   PHE A  68      -7.817  28.108  49.053  1.00 48.98           C  
-ATOM    472  O   PHE A  68      -8.452  29.167  48.974  1.00 48.47           O  
-ATOM    473  CB  PHE A  68      -8.427  26.329  47.369  1.00 49.95           C  
-ATOM    474  CG  PHE A  68      -8.325  25.944  45.918  1.00 50.75           C  
-ATOM    475  CD1 PHE A  68      -8.827  26.781  44.923  1.00 51.51           C  
-ATOM    476  CD2 PHE A  68      -7.720  24.753  45.536  1.00 52.14           C  
-ATOM    477  CE1 PHE A  68      -8.727  26.435  43.574  1.00 50.73           C  
-ATOM    478  CE2 PHE A  68      -7.623  24.402  44.190  1.00 51.23           C  
-ATOM    479  CZ  PHE A  68      -8.128  25.236  43.212  1.00 50.99           C  
-ATOM    480  N   SER A  69      -7.425  27.590  50.220  1.00 47.54           N  
-ATOM    481  CA  SER A  69      -7.722  28.276  51.474  1.00 47.02           C  
-ATOM    482  C   SER A  69      -7.031  29.637  51.557  1.00 46.54           C  
-ATOM    483  O   SER A  69      -7.624  30.611  52.014  1.00 45.39           O  
-ATOM    484  CB  SER A  69      -7.356  27.402  52.691  1.00 46.83           C  
-ATOM    485  OG  SER A  69      -8.039  26.155  52.659  1.00 47.02           O  
-ATOM    486  N   THR A  70      -5.782  29.707  51.098  1.00 47.06           N  
-ATOM    487  CA  THR A  70      -5.069  30.982  51.072  1.00 47.69           C  
-ATOM    488  C   THR A  70      -5.751  31.976  50.111  1.00 47.53           C  
-ATOM    489  O   THR A  70      -5.980  33.120  50.482  1.00 47.91           O  
-ATOM    490  CB  THR A  70      -3.543  30.802  50.801  1.00 47.77           C  
-ATOM    491  OG1 THR A  70      -2.921  30.306  51.994  1.00 49.80           O  
-ATOM    492  CG2 THR A  70      -2.858  32.147  50.447  1.00 46.90           C  
-ATOM    493  N   VAL A  71      -6.102  31.532  48.907  1.00 48.27           N  
-ATOM    494  CA  VAL A  71      -6.848  32.397  47.952  1.00 48.21           C  
-ATOM    495  C   VAL A  71      -8.149  32.908  48.558  1.00 48.04           C  
-ATOM    496  O   VAL A  71      -8.436  34.122  48.543  1.00 48.39           O  
-ATOM    497  CB  VAL A  71      -7.133  31.692  46.596  1.00 47.90           C  
-ATOM    498  CG1 VAL A  71      -7.946  32.619  45.664  1.00 48.61           C  
-ATOM    499  CG2 VAL A  71      -5.835  31.295  45.900  1.00 48.30           C  
-ATOM    500  N   ARG A  72      -8.937  31.986  49.113  1.00 48.59           N  
-ATOM    501  CA  ARG A  72     -10.174  32.350  49.819  1.00 48.12           C  
-ATOM    502  C   ARG A  72      -9.950  33.410  50.891  1.00 47.77           C  
-ATOM    503  O   ARG A  72     -10.635  34.426  50.903  1.00 46.63           O  
-ATOM    504  CB  ARG A  72     -10.832  31.123  50.434  1.00 49.05           C  
-ATOM    505  CG  ARG A  72     -11.847  30.467  49.528  1.00 51.75           C  
-ATOM    506  CD  ARG A  72     -12.709  29.439  50.266  1.00 55.93           C  
-ATOM    507  NE  ARG A  72     -12.814  28.242  49.436  1.00 59.20           N  
-ATOM    508  CZ  ARG A  72     -12.028  27.172  49.550  1.00 61.91           C  
-ATOM    509  NH1 ARG A  72     -11.098  27.112  50.500  1.00 62.45           N  
-ATOM    510  NH2 ARG A  72     -12.192  26.140  48.729  1.00 62.90           N  
-ATOM    511  N   ASP A  73      -8.993  33.173  51.793  1.00 47.29           N  
-ATOM    512  CA  ASP A  73      -8.633  34.183  52.794  1.00 47.13           C  
-ATOM    513  C   ASP A  73      -8.292  35.549  52.178  1.00 46.53           C  
-ATOM    514  O   ASP A  73      -8.761  36.580  52.659  1.00 47.33           O  
-ATOM    515  CB  ASP A  73      -7.489  33.683  53.694  1.00 46.78           C  
-ATOM    516  CG  ASP A  73      -7.958  32.680  54.745  1.00 48.80           C  
-ATOM    517  OD1 ASP A  73      -9.161  32.310  54.758  0.50 47.88           O  
-ATOM    518  OD2 ASP A  73      -7.111  32.256  55.566  0.50 48.21           O  
-ATOM    519  N   ILE A  74      -7.492  35.565  51.114  1.00 46.40           N  
-ATOM    520  CA  ILE A  74      -7.175  36.823  50.406  1.00 45.09           C  
-ATOM    521  C   ILE A  74      -8.437  37.512  49.902  1.00 45.08           C  
-ATOM    522  O   ILE A  74      -8.690  38.689  50.200  1.00 44.42           O  
-ATOM    523  CB  ILE A  74      -6.152  36.605  49.235  1.00 45.88           C  
-ATOM    524  CG1 ILE A  74      -4.812  36.127  49.787  1.00 44.85           C  
-ATOM    525  CG2 ILE A  74      -5.950  37.906  48.442  1.00 43.25           C  
-ATOM    526  CD1 ILE A  74      -3.841  35.568  48.739  1.00 44.44           C  
-ATOM    527  N   VAL A  75      -9.237  36.755  49.159  1.00 45.52           N  
-ATOM    528  CA  VAL A  75     -10.452  37.271  48.524  1.00 45.75           C  
-ATOM    529  C   VAL A  75     -11.457  37.803  49.559  1.00 46.62           C  
-ATOM    530  O   VAL A  75     -11.974  38.911  49.419  1.00 45.96           O  
-ATOM    531  CB  VAL A  75     -11.097  36.208  47.576  1.00 45.75           C  
-ATOM    532  CG1 VAL A  75     -12.422  36.708  47.033  1.00 45.94           C  
-ATOM    533  CG2 VAL A  75     -10.134  35.855  46.414  1.00 44.70           C  
-ATOM    534  N   GLN A  76     -11.705  37.026  50.614  1.00 46.93           N  
-ATOM    535  CA  GLN A  76     -12.597  37.462  51.680  1.00 47.59           C  
-ATOM    536  C   GLN A  76     -12.038  38.695  52.397  1.00 47.36           C  
-ATOM    537  O   GLN A  76     -12.797  39.589  52.742  1.00 47.14           O  
-ATOM    538  CB  GLN A  76     -12.855  36.325  52.684  1.00 47.70           C  
-ATOM    539  CG  GLN A  76     -13.582  35.095  52.109  1.00 48.84           C  
-ATOM    540  CD  GLN A  76     -13.541  33.864  53.039  1.00 48.71           C  
-ATOM    541  OE1 GLN A  76     -12.537  33.600  53.713  0.50 49.35           O  
-ATOM    542  NE2 GLN A  76     -14.631  33.107  53.060  0.50 48.82           N  
-ATOM    543  N   SER A  77     -10.721  38.747  52.612  1.00 47.20           N  
-ATOM    544  CA  SER A  77     -10.090  39.927  53.223  1.00 48.08           C  
-ATOM    545  C   SER A  77     -10.326  41.200  52.394  1.00 48.49           C  
-ATOM    546  O   SER A  77     -10.677  42.247  52.935  1.00 48.80           O  
-ATOM    547  CB  SER A  77      -8.587  39.731  53.444  1.00 47.49           C  
-ATOM    548  OG  SER A  77      -8.286  38.484  54.035  1.00 49.96           O  
-ATOM    549  N   ILE A  78     -10.147  41.091  51.083  1.00 49.50           N  
-ATOM    550  CA  ILE A  78     -10.367  42.208  50.144  1.00 50.64           C  
-ATOM    551  C   ILE A  78     -11.827  42.675  50.159  1.00 51.88           C  
-ATOM    552  O   ILE A  78     -12.101  43.883  50.117  1.00 52.14           O  
-ATOM    553  CB  ILE A  78      -9.892  41.836  48.689  1.00 49.96           C  
-ATOM    554  CG1 ILE A  78      -8.365  41.747  48.633  1.00 49.49           C  
-ATOM    555  CG2 ILE A  78     -10.380  42.850  47.663  1.00 50.16           C  
-ATOM    556  CD1 ILE A  78      -7.796  41.038  47.392  1.00 50.38           C  
-ATOM    557  N   ASP A  79     -12.755  41.723  50.252  1.00 53.36           N  
-ATOM    558  CA  ASP A  79     -14.198  42.016  50.195  1.00 55.07           C  
-ATOM    559  C   ASP A  79     -14.889  42.278  51.559  1.00 56.13           C  
-ATOM    560  O   ASP A  79     -16.118  42.393  51.627  1.00 55.86           O  
-ATOM    561  CB  ASP A  79     -14.917  40.882  49.448  1.00 55.44           C  
-ATOM    562  CG  ASP A  79     -14.480  40.761  47.985  1.00 57.01           C  
-ATOM    563  OD1 ASP A  79     -13.647  41.566  47.512  1.00 59.16           O  
-ATOM    564  OD2 ASP A  79     -14.975  39.848  47.298  1.00 58.53           O  
-ATOM    565  N   LYS A  80     -14.100  42.394  52.628  1.00 57.21           N  
-ATOM    566  CA  LYS A  80     -14.628  42.550  53.994  1.00 58.84           C  
-ATOM    567  C   LYS A  80     -15.252  43.931  54.269  1.00 59.49           C  
-ATOM    568  O   LYS A  80     -14.597  44.962  54.097  1.00 59.98           O  
-ATOM    569  CB  LYS A  80     -13.529  42.234  55.023  1.00 58.77           C  
-ATOM    570  CG  LYS A  80     -14.041  41.722  56.371  1.00 60.03           C  
-ATOM    571  CD  LYS A  80     -14.096  40.187  56.408  1.00 61.17           C  
-ATOM    572  N   VAL A  81     -16.514  43.940  54.705  1.00 60.26           N  
-ATOM    573  CA  VAL A  81     -17.252  45.181  54.995  1.00 60.86           C  
-ATOM    574  C   VAL A  81     -17.258  45.539  56.489  1.00 61.23           C  
-ATOM    575  O   VAL A  81     -17.614  44.722  57.346  1.00 61.73           O  
-ATOM    576  CB  VAL A  81     -18.706  45.133  54.427  1.00 60.84           C  
-ATOM    577  CG1 VAL A  81     -19.647  46.103  55.168  1.00 61.22           C  
-ATOM    578  CG2 VAL A  81     -18.698  45.433  52.933  1.00 60.99           C  
-ATOM    579  N   PRO A  92     -13.370  46.108  42.953  1.00 46.09           N  
-ATOM    580  CA  PRO A  92     -11.971  45.764  42.624  1.00 45.56           C  
-ATOM    581  C   PRO A  92     -11.826  44.394  41.985  1.00 44.52           C  
-ATOM    582  O   PRO A  92     -12.291  43.399  42.550  1.00 44.21           O  
-ATOM    583  CB  PRO A  92     -11.247  45.783  43.976  1.00 45.53           C  
-ATOM    584  CG  PRO A  92     -12.239  46.134  44.987  1.00 46.15           C  
-ATOM    585  CD  PRO A  92     -13.620  46.170  44.397  1.00 46.57           C  
-ATOM    586  N   THR A  93     -11.197  44.347  40.810  1.00 43.94           N  
-ATOM    587  CA  THR A  93     -10.777  43.071  40.228  1.00 43.69           C  
-ATOM    588  C   THR A  93      -9.630  42.530  41.065  1.00 42.84           C  
-ATOM    589  O   THR A  93      -8.837  43.305  41.596  1.00 42.60           O  
-ATOM    590  CB  THR A  93     -10.336  43.232  38.765  1.00 44.15           C  
-ATOM    591  OG1 THR A  93     -11.446  43.724  38.008  1.00 46.05           O  
-ATOM    592  CG2 THR A  93      -9.877  41.880  38.184  1.00 43.62           C  
-ATOM    593  N   ILE A  94      -9.552  41.203  41.199  1.00 42.53           N  
-ATOM    594  CA  ILE A  94      -8.463  40.583  41.900  1.00 42.04           C  
-ATOM    595  C   ILE A  94      -7.654  39.727  40.910  1.00 42.90           C  
-ATOM    596  O   ILE A  94      -8.205  38.829  40.265  1.00 42.73           O  
-ATOM    597  CB  ILE A  94      -8.964  39.717  43.087  1.00 42.08           C  
-ATOM    598  CG1 ILE A  94      -9.922  40.544  43.978  1.00 41.27           C  
-ATOM    599  CG2 ILE A  94      -7.758  39.156  43.861  1.00 42.95           C  
-ATOM    600  CD1 ILE A  94     -10.738  39.764  45.054  1.00 41.80           C  
-ATOM    601  N   GLN A  95      -6.361  40.013  40.788  1.00 42.10           N  
-ATOM    602  CA  GLN A  95      -5.498  39.194  39.959  1.00 44.02           C  
-ATOM    603  C   GLN A  95      -4.471  38.478  40.839  1.00 43.68           C  
-ATOM    604  O   GLN A  95      -3.586  39.110  41.422  1.00 43.76           O  
-ATOM    605  CB  GLN A  95      -4.832  40.011  38.857  1.00 43.65           C  
-ATOM    606  CG  GLN A  95      -4.130  39.162  37.788  1.00 45.05           C  
-ATOM    607  CD  GLN A  95      -3.395  40.014  36.771  1.00 45.73           C  
-ATOM    608  OE1 GLN A  95      -2.940  41.098  37.089  1.00 45.56           O  
-ATOM    609  NE2 GLN A  95      -3.258  39.510  35.538  1.00 48.34           N  
-ATOM    610  N   ILE A  96      -4.621  37.161  40.941  1.00 43.77           N  
-ATOM    611  CA  ILE A  96      -3.776  36.325  41.798  1.00 44.27           C  
-ATOM    612  C   ILE A  96      -2.797  35.493  40.965  1.00 44.15           C  
-ATOM    613  O   ILE A  96      -3.190  34.783  40.048  1.00 45.47           O  
-ATOM    614  CB  ILE A  96      -4.637  35.419  42.714  1.00 44.68           C  
-ATOM    615  CG1 ILE A  96      -5.441  36.296  43.695  1.00 44.26           C  
-ATOM    616  CG2 ILE A  96      -3.773  34.386  43.485  1.00 46.31           C  
-ATOM    617  CD1 ILE A  96      -6.527  35.578  44.420  1.00 45.72           C  
-ATOM    618  N   PHE A  97      -1.520  35.601  41.285  1.00 43.50           N  
-ATOM    619  CA  PHE A  97      -0.499  34.761  40.667  1.00 43.54           C  
-ATOM    620  C   PHE A  97      -0.027  33.732  41.675  1.00 42.74           C  
-ATOM    621  O   PHE A  97       0.541  34.075  42.712  1.00 42.46           O  
-ATOM    622  CB  PHE A  97       0.696  35.588  40.223  1.00 44.24           C  
-ATOM    623  CG  PHE A  97       0.380  36.666  39.230  1.00 47.16           C  
-ATOM    624  CD1 PHE A  97      -0.150  37.885  39.645  1.00 47.93           C  
-ATOM    625  CD2 PHE A  97       0.673  36.484  37.882  1.00 48.74           C  
-ATOM    626  CE1 PHE A  97      -0.398  38.898  38.733  1.00 50.28           C  
-ATOM    627  CE2 PHE A  97       0.419  37.505  36.958  1.00 50.78           C  
-ATOM    628  CZ  PHE A  97      -0.101  38.703  37.381  1.00 49.17           C  
-ATOM    629  N   LEU A  98      -0.267  32.465  41.376  1.00 43.08           N  
-ATOM    630  CA  LEU A  98       0.212  31.378  42.225  1.00 42.85           C  
-ATOM    631  C   LEU A  98       1.620  30.991  41.786  1.00 44.25           C  
-ATOM    632  O   LEU A  98       1.854  30.681  40.597  1.00 44.68           O  
-ATOM    633  CB  LEU A  98      -0.724  30.180  42.092  1.00 43.12           C  
-ATOM    634  CG  LEU A  98      -2.200  30.415  42.388  1.00 42.40           C  
-ATOM    635  CD1 LEU A  98      -3.019  29.158  42.109  1.00 38.08           C  
-ATOM    636  CD2 LEU A  98      -2.389  30.900  43.846  1.00 43.37           C  
-ATOM    637  N   ASN A  99       2.572  31.029  42.715  1.00 43.79           N  
-ATOM    638  CA  ASN A  99       3.945  30.711  42.354  1.00 44.01           C  
-ATOM    639  C   ASN A  99       4.404  29.497  43.119  1.00 44.64           C  
-ATOM    640  O   ASN A  99       4.190  29.377  44.338  1.00 44.15           O  
-ATOM    641  CB  ASN A  99       4.910  31.871  42.635  1.00 43.07           C  
-ATOM    642  CG  ASN A  99       6.371  31.408  42.840  1.00 44.06           C  
-ATOM    643  OD1 ASN A  99       6.853  31.299  43.979  1.00 42.49           O  
-ATOM    644  ND2 ASN A  99       7.076  31.151  41.731  1.00 41.51           N  
-ATOM    645  N   ASP A 100       5.073  28.617  42.401  1.00 45.87           N  
-ATOM    646  CA  ASP A 100       5.822  27.527  43.042  1.00 47.32           C  
-ATOM    647  C   ASP A 100       6.872  27.027  42.052  1.00 48.10           C  
-ATOM    648  O   ASP A 100       6.953  27.513  40.938  1.00 47.17           O  
-ATOM    649  CB  ASP A 100       4.896  26.423  43.521  1.00 47.61           C  
-ATOM    650  CG  ASP A 100       5.488  25.638  44.713  1.00 51.21           C  
-ATOM    651  OD1 ASP A 100       6.410  24.830  44.485  1.00 49.78           O  
-ATOM    652  OD2 ASP A 100       5.050  25.865  45.874  1.00 53.64           O  
-ATOM    653  N   LEU A 101       7.681  26.060  42.471  1.00 51.04           N  
-ATOM    654  CA  LEU A 101       8.738  25.499  41.626  1.00 52.73           C  
-ATOM    655  C   LEU A 101       8.155  24.870  40.339  1.00 53.32           C  
-ATOM    656  O   LEU A 101       6.973  24.522  40.312  1.00 54.21           O  
-ATOM    657  CB  LEU A 101       9.624  24.553  42.490  1.00 52.54           C  
-ATOM    658  CG  LEU A 101      10.511  25.352  43.463  1.00 53.94           C  
-ATOM    659  CD1 LEU A 101      11.135  24.527  44.590  1.00 54.32           C  
-ATOM    660  CD2 LEU A 101      11.611  26.114  42.723  1.00 53.83           C  
-ATOM    661  N   PHE A 102       8.957  24.775  39.269  1.00 54.07           N  
-ATOM    662  CA  PHE A 102       8.500  24.339  37.923  1.00 54.91           C  
-ATOM    663  C   PHE A 102       7.856  22.923  37.779  1.00 56.00           C  
-ATOM    664  O   PHE A 102       7.217  22.632  36.749  1.00 55.27           O  
-ATOM    665  CB  PHE A 102       9.649  24.430  36.894  1.00 55.09           C  
-ATOM    666  CG  PHE A 102      10.056  25.826  36.528  1.00 53.72           C  
-ATOM    667  CD1 PHE A 102       9.286  26.597  35.657  1.00 53.60           C  
-ATOM    668  CD2 PHE A 102      11.229  26.363  37.038  1.00 54.82           C  
-ATOM    669  CE1 PHE A 102       9.663  27.876  35.327  1.00 52.40           C  
-ATOM    670  CE2 PHE A 102      11.615  27.631  36.720  1.00 52.22           C  
-ATOM    671  CZ  PHE A 102      10.835  28.397  35.848  1.00 54.63           C  
-ATOM    672  N   GLN A 103       8.046  22.071  38.780  1.00 56.63           N  
-ATOM    673  CA  GLN A 103       7.488  20.711  38.828  1.00 59.00           C  
-ATOM    674  C   GLN A 103       6.459  20.565  39.962  1.00 59.31           C  
-ATOM    675  O   GLN A 103       6.214  19.449  40.484  1.00 60.01           O  
-ATOM    676  CB  GLN A 103       8.603  19.673  39.057  1.00 59.25           C  
-ATOM    677  CG  GLN A 103       9.485  19.374  37.863  1.00 60.84           C  
-ATOM    678  CD  GLN A 103      10.001  17.950  37.871  1.00 64.77           C  
-ATOM    679  OE1 GLN A 103      10.036  17.283  38.916  1.00 67.01           O  
-ATOM    680  NE2 GLN A 103      10.405  17.464  36.696  1.00 66.56           N  
-ATOM    681  N   ASN A 104       5.891  21.696  40.382  1.00 59.36           N  
-ATOM    682  CA  ASN A 104       4.761  21.671  41.293  1.00 58.46           C  
-ATOM    683  C   ASN A 104       3.581  21.189  40.488  1.00 57.55           C  
-ATOM    684  O   ASN A 104       3.559  21.329  39.263  1.00 57.63           O  
-ATOM    685  CB  ASN A 104       4.486  23.067  41.884  1.00 58.40           C  
-ATOM    686  CG  ASN A 104       3.294  23.083  42.839  1.00 58.06           C  
-ATOM    687  OD1 ASN A 104       3.313  22.440  43.885  1.00 56.93           O  
-ATOM    688  ND2 ASN A 104       2.265  23.849  42.489  1.00 59.16           N  
-ATOM    689  N   ASP A 105       2.598  20.633  41.186  1.00 57.00           N  
-ATOM    690  CA  ASP A 105       1.421  20.078  40.561  1.00 56.20           C  
-ATOM    691  C   ASP A 105       0.406  21.200  40.310  1.00 55.86           C  
-ATOM    692  O   ASP A 105      -0.549  21.367  41.072  1.00 55.52           O  
-ATOM    693  CB  ASP A 105       0.837  18.987  41.481  1.00 56.37           C  
-ATOM    694  CG  ASP A 105      -0.174  18.096  40.780  1.00 57.18           C  
-ATOM    695  OD1 ASP A 105      -0.479  18.340  39.590  1.00 58.24           O  
-ATOM    696  OD2 ASP A 105      -0.666  17.143  41.435  1.00 57.21           O  
-ATOM    697  N   PHE A 106       0.638  21.980  39.251  1.00 55.64           N  
-ATOM    698  CA  PHE A 106      -0.265  23.074  38.848  1.00 54.98           C  
-ATOM    699  C   PHE A 106      -1.548  22.561  38.167  1.00 54.80           C  
-ATOM    700  O   PHE A 106      -2.638  23.103  38.389  1.00 54.17           O  
-ATOM    701  CB  PHE A 106       0.464  24.085  37.937  1.00 54.84           C  
-ATOM    702  CG  PHE A 106       1.347  25.053  38.687  1.00 54.09           C  
-ATOM    703  CD1 PHE A 106       0.795  26.127  39.381  1.00 53.39           C  
-ATOM    704  CD2 PHE A 106       2.730  24.895  38.692  1.00 54.35           C  
-ATOM    705  CE1 PHE A 106       1.610  27.024  40.098  1.00 54.12           C  
-ATOM    706  CE2 PHE A 106       3.559  25.791  39.386  1.00 54.59           C  
-ATOM    707  CZ  PHE A 106       2.992  26.870  40.090  1.00 54.06           C  
-ATOM    708  N   ASN A 107      -1.400  21.522  37.346  1.00 54.70           N  
-ATOM    709  CA  ASN A 107      -2.500  20.925  36.586  1.00 55.26           C  
-ATOM    710  C   ASN A 107      -3.722  20.578  37.448  1.00 55.35           C  
-ATOM    711  O   ASN A 107      -4.870  20.698  36.989  1.00 55.86           O  
-ATOM    712  CB  ASN A 107      -2.033  19.661  35.838  1.00 54.85           C  
-ATOM    713  CG  ASN A 107      -1.585  19.949  34.409  1.00 55.49           C  
-ATOM    714  OD1 ASN A 107      -1.339  21.105  34.036  1.00 53.62           O  
-ATOM    715  ND2 ASN A 107      -1.484  18.900  33.596  1.00 51.75           N  
-ATOM    716  N   SER A 108      -3.462  20.160  38.681  1.00 55.10           N  
-ATOM    717  CA  SER A 108      -4.513  19.741  39.588  1.00 55.75           C  
-ATOM    718  C   SER A 108      -5.217  20.934  40.236  1.00 54.73           C  
-ATOM    719  O   SER A 108      -6.416  20.866  40.521  1.00 54.89           O  
-ATOM    720  CB  SER A 108      -3.981  18.761  40.638  1.00 55.99           C  
-ATOM    721  OG  SER A 108      -3.202  19.406  41.631  1.00 59.38           O  
-ATOM    722  N   VAL A 109      -4.474  22.019  40.460  1.00 53.45           N  
-ATOM    723  CA  VAL A 109      -5.052  23.263  40.942  1.00 51.84           C  
-ATOM    724  C   VAL A 109      -6.003  23.806  39.890  1.00 51.21           C  
-ATOM    725  O   VAL A 109      -7.129  24.184  40.220  1.00 51.33           O  
-ATOM    726  CB  VAL A 109      -3.959  24.318  41.298  1.00 51.96           C  
-ATOM    727  CG1 VAL A 109      -4.583  25.691  41.633  1.00 51.13           C  
-ATOM    728  CG2 VAL A 109      -3.094  23.809  42.443  1.00 51.40           C  
-ATOM    729  N   PHE A 110      -5.556  23.818  38.628  1.00 50.24           N  
-ATOM    730  CA  PHE A 110      -6.283  24.432  37.517  1.00 49.41           C  
-ATOM    731  C   PHE A 110      -7.578  23.689  37.225  1.00 49.28           C  
-ATOM    732  O   PHE A 110      -8.560  24.264  36.754  1.00 47.73           O  
-ATOM    733  CB  PHE A 110      -5.434  24.445  36.241  1.00 49.35           C  
-ATOM    734  CG  PHE A 110      -4.283  25.426  36.264  1.00 49.97           C  
-ATOM    735  CD1 PHE A 110      -4.077  26.288  37.348  1.00 51.28           C  
-ATOM    736  CD2 PHE A 110      -3.447  25.537  35.159  1.00 51.50           C  
-ATOM    737  CE1 PHE A 110      -3.011  27.217  37.352  1.00 49.96           C  
-ATOM    738  CE2 PHE A 110      -2.376  26.475  35.140  1.00 51.47           C  
-ATOM    739  CZ  PHE A 110      -2.160  27.297  36.254  1.00 50.57           C  
-ATOM    740  N   LYS A 111      -7.556  22.390  37.490  1.00 48.94           N  
-ATOM    741  CA  LYS A 111      -8.713  21.549  37.230  1.00 49.08           C  
-ATOM    742  C   LYS A 111      -9.807  21.779  38.281  1.00 48.46           C  
-ATOM    743  O   LYS A 111     -10.979  21.550  38.025  1.00 49.59           O  
-ATOM    744  CB  LYS A 111      -8.285  20.085  37.205  1.00 49.46           C  
-ATOM    745  CG  LYS A 111      -7.744  19.610  35.862  1.00 51.40           C  
-ATOM    746  CD  LYS A 111      -7.376  18.122  35.950  1.00 55.61           C  
-ATOM    747  CE  LYS A 111      -6.191  17.755  35.069  1.00 57.13           C  
-ATOM    748  NZ  LYS A 111      -5.527  16.561  35.688  1.00 58.78           N  
-ATOM    749  N   LEU A 112      -9.403  22.224  39.461  1.00 47.62           N  
-ATOM    750  CA  LEU A 112     -10.323  22.602  40.517  1.00 46.54           C  
-ATOM    751  C   LEU A 112     -10.795  24.050  40.418  1.00 46.07           C  
-ATOM    752  O   LEU A 112     -11.694  24.456  41.140  1.00 45.70           O  
-ATOM    753  CB  LEU A 112      -9.697  22.319  41.881  1.00 46.63           C  
-ATOM    754  CG  LEU A 112      -9.587  20.825  42.207  1.00 45.91           C  
-ATOM    755  CD1 LEU A 112      -8.657  20.578  43.371  1.00 47.24           C  
-ATOM    756  CD2 LEU A 112     -10.966  20.234  42.482  1.00 47.24           C  
-ATOM    757  N   LEU A 113     -10.202  24.830  39.516  1.00 45.98           N  
-ATOM    758  CA  LEU A 113     -10.619  26.217  39.356  1.00 45.61           C  
-ATOM    759  C   LEU A 113     -12.079  26.440  38.914  1.00 45.86           C  
-ATOM    760  O   LEU A 113     -12.711  27.339  39.425  1.00 46.13           O  
-ATOM    761  CB  LEU A 113      -9.622  27.028  38.494  1.00 45.56           C  
-ATOM    762  CG  LEU A 113      -8.349  27.515  39.204  1.00 44.54           C  
-ATOM    763  CD1 LEU A 113      -7.405  28.233  38.230  1.00 44.73           C  
-ATOM    764  CD2 LEU A 113      -8.689  28.444  40.375  1.00 45.22           C  
-ATOM    765  N   PRO A 114     -12.616  25.641  37.969  1.00 46.52           N  
-ATOM    766  CA  PRO A 114     -14.014  25.889  37.584  1.00 47.45           C  
-ATOM    767  C   PRO A 114     -14.995  25.814  38.773  1.00 48.28           C  
-ATOM    768  O   PRO A 114     -15.889  26.661  38.882  1.00 48.74           O  
-ATOM    769  CB  PRO A 114     -14.307  24.764  36.591  1.00 47.17           C  
-ATOM    770  CG  PRO A 114     -12.948  24.372  36.058  1.00 46.70           C  
-ATOM    771  CD  PRO A 114     -12.047  24.500  37.222  1.00 46.52           C  
-ATOM    772  N   SER A 115     -14.831  24.826  39.644  1.00 48.90           N  
-ATOM    773  CA  SER A 115     -15.714  24.704  40.813  1.00 49.63           C  
-ATOM    774  C   SER A 115     -15.381  25.749  41.867  1.00 49.44           C  
-ATOM    775  O   SER A 115     -16.299  26.364  42.422  1.00 49.46           O  
-ATOM    776  CB  SER A 115     -15.718  23.297  41.401  1.00 49.91           C  
-ATOM    777  OG  SER A 115     -14.425  22.911  41.802  1.00 52.73           O  
-ATOM    778  N   PHE A 116     -14.087  25.982  42.114  1.00 48.86           N  
-ATOM    779  CA  PHE A 116     -13.674  27.118  42.944  1.00 49.08           C  
-ATOM    780  C   PHE A 116     -14.360  28.433  42.551  1.00 48.64           C  
-ATOM    781  O   PHE A 116     -14.862  29.140  43.419  1.00 48.34           O  
-ATOM    782  CB  PHE A 116     -12.154  27.338  42.953  1.00 49.86           C  
-ATOM    783  CG  PHE A 116     -11.733  28.470  43.847  1.00 51.93           C  
-ATOM    784  CD1 PHE A 116     -11.653  28.284  45.234  1.00 52.59           C  
-ATOM    785  CD2 PHE A 116     -11.492  29.750  43.317  1.00 53.98           C  
-ATOM    786  CE1 PHE A 116     -11.297  29.337  46.077  1.00 54.27           C  
-ATOM    787  CE2 PHE A 116     -11.143  30.817  44.151  1.00 54.39           C  
-ATOM    788  CZ  PHE A 116     -11.037  30.612  45.531  1.00 53.63           C  
-ATOM    789  N   TYR A 117     -14.356  28.764  41.255  1.00 48.11           N  
-ATOM    790  CA  TYR A 117     -14.977  30.002  40.758  1.00 47.81           C  
-ATOM    791  C   TYR A 117     -16.498  30.071  40.987  1.00 48.22           C  
-ATOM    792  O   TYR A 117     -17.027  31.130  41.336  1.00 47.66           O  
-ATOM    793  CB  TYR A 117     -14.680  30.216  39.263  1.00 47.27           C  
-ATOM    794  CG  TYR A 117     -13.292  30.721  38.919  1.00 46.68           C  
-ATOM    795  CD1 TYR A 117     -12.684  31.750  39.643  1.00 47.52           C  
-ATOM    796  CD2 TYR A 117     -12.591  30.184  37.833  1.00 45.80           C  
-ATOM    797  CE1 TYR A 117     -11.398  32.234  39.283  1.00 44.50           C  
-ATOM    798  CE2 TYR A 117     -11.333  30.639  37.490  1.00 43.45           C  
-ATOM    799  CZ  TYR A 117     -10.742  31.659  38.213  1.00 45.28           C  
-ATOM    800  OH  TYR A 117      -9.490  32.103  37.832  1.00 47.05           O  
-ATOM    801  N   ARG A 118     -17.185  28.955  40.751  1.00 49.05           N  
-ATOM    802  CA  ARG A 118     -18.625  28.830  41.001  1.00 50.91           C  
-ATOM    803  C   ARG A 118     -18.966  28.960  42.482  1.00 51.47           C  
-ATOM    804  O   ARG A 118     -19.931  29.622  42.847  1.00 51.15           O  
-ATOM    805  CB  ARG A 118     -19.156  27.485  40.501  1.00 51.01           C  
-ATOM    806  CG  ARG A 118     -19.126  27.305  38.996  1.00 52.37           C  
-ATOM    807  CD  ARG A 118     -19.962  26.119  38.561  1.00 55.51           C  
-ATOM    808  NE  ARG A 118     -19.424  24.846  39.051  1.00 57.80           N  
-ATOM    809  CZ  ARG A 118     -18.630  24.045  38.342  1.00 58.73           C  
-ATOM    810  NH1 ARG A 118     -18.274  24.373  37.101  1.00 58.70           N  
-ATOM    811  NH2 ARG A 118     -18.201  22.908  38.869  1.00 59.38           N  
-ATOM    812  N   ASN A 119     -18.162  28.313  43.320  1.00 53.10           N  
-ATOM    813  CA  ASN A 119     -18.337  28.365  44.765  1.00 54.98           C  
-ATOM    814  C   ASN A 119     -18.033  29.756  45.306  1.00 55.85           C  
-ATOM    815  O   ASN A 119     -18.635  30.186  46.282  1.00 56.17           O  
-ATOM    816  CB  ASN A 119     -17.470  27.306  45.455  1.00 55.49           C  
-ATOM    817  CG  ASN A 119     -17.878  25.881  45.098  1.00 56.87           C  
-ATOM    818  OD1 ASN A 119     -18.777  25.656  44.280  1.00 59.84           O  
-ATOM    819  ND2 ASN A 119     -17.216  24.909  45.716  1.00 57.98           N  
-ATOM    820  N   LEU A 120     -17.094  30.446  44.660  1.00 56.87           N  
-ATOM    821  CA  LEU A 120     -16.790  31.849  44.954  1.00 57.73           C  
-ATOM    822  C   LEU A 120     -17.993  32.748  44.647  1.00 58.03           C  
-ATOM    823  O   LEU A 120     -18.252  33.707  45.373  1.00 58.05           O  
-ATOM    824  CB  LEU A 120     -15.590  32.315  44.128  1.00 57.77           C  
-ATOM    825  CG  LEU A 120     -14.490  33.211  44.713  1.00 58.85           C  
-ATOM    826  CD1 LEU A 120     -13.609  33.749  43.585  1.00 58.22           C  
-ATOM    827  CD2 LEU A 120     -15.028  34.358  45.547  1.00 59.66           C  
-ATOM    828  N   GLU A 121     -18.704  32.442  43.560  1.00 58.73           N  
-ATOM    829  CA  GLU A 121     -19.892  33.197  43.158  1.00 59.56           C  
-ATOM    830  C   GLU A 121     -21.118  32.837  43.991  1.00 59.89           C  
-ATOM    831  O   GLU A 121     -21.983  33.686  44.215  1.00 59.90           O  
-ATOM    832  CB  GLU A 121     -20.203  32.993  41.672  1.00 59.67           C  
-ATOM    833  CG  GLU A 121     -21.273  33.948  41.121  1.00 59.81           C  
-ATOM    834  CD  GLU A 121     -21.697  33.637  39.688  1.00 60.68           C  
-ATOM    835  OE1 GLU A 121     -21.200  32.646  39.104  1.00 61.90           O  
-ATOM    836  OE2 GLU A 121     -22.541  34.391  39.144  1.00 61.87           O  
-ATOM    837  N   LYS A 122     -21.205  31.582  44.432  1.00 60.44           N  
-ATOM    838  CA  LYS A 122     -22.302  31.167  45.317  1.00 61.26           C  
-ATOM    839  C   LYS A 122     -22.081  31.701  46.734  1.00 61.90           C  
-ATOM    840  O   LYS A 122     -23.033  32.130  47.380  1.00 62.08           O  
-ATOM    841  CB  LYS A 122     -22.503  29.643  45.313  1.00 61.05           C  
-ATOM    842  CG  LYS A 122     -23.428  29.135  44.206  1.00 60.81           C  
-ATOM    843  CD  LYS A 122     -23.232  27.644  43.936  1.00 60.81           C  
-ATOM    844  CE  LYS A 122     -24.262  27.099  42.933  1.00 61.21           C  
-ATOM    845  NZ  LYS A 122     -25.469  26.438  43.551  1.00 61.18           N  
-ATOM    846  N   GLU A 123     -20.827  31.696  47.197  1.00 62.67           N  
-ATOM    847  CA  GLU A 123     -20.475  32.254  48.512  1.00 63.57           C  
-ATOM    848  C   GLU A 123     -20.572  33.785  48.594  1.00 63.92           C  
-ATOM    849  O   GLU A 123     -21.382  34.309  49.363  1.00 63.75           O  
-ATOM    850  CB  GLU A 123     -19.089  31.785  48.973  1.00 63.55           C  
-ATOM    851  CG  GLU A 123     -19.044  30.366  49.544  1.00 65.24           C  
-ATOM    852  CD  GLU A 123     -19.339  30.296  51.047  1.00 66.94           C  
-ATOM    853  OE1 GLU A 123     -20.273  30.978  51.526  1.00 66.84           O  
-ATOM    854  OE2 GLU A 123     -18.632  29.539  51.756  1.00 68.63           O  
-ATOM    855  N   ASN A 124     -19.761  34.496  47.806  1.00 64.25           N  
-ATOM    856  CA  ASN A 124     -19.617  35.957  47.956  1.00 64.62           C  
-ATOM    857  C   ASN A 124     -20.444  36.835  47.000  1.00 64.75           C  
-ATOM    858  O   ASN A 124     -20.688  38.018  47.278  1.00 64.98           O  
-ATOM    859  CB  ASN A 124     -18.137  36.369  47.877  1.00 64.92           C  
-ATOM    860  CG  ASN A 124     -17.232  35.568  48.834  1.00 66.00           C  
-ATOM    861  OD1 ASN A 124     -17.705  34.788  49.667  1.00 67.01           O  
-ATOM    862  ND2 ASN A 124     -15.917  35.768  48.707  1.00 65.48           N  
-ATOM    863  N   GLY A 125     -20.869  36.266  45.877  1.00 64.60           N  
-ATOM    864  CA  GLY A 125     -21.459  37.059  44.804  1.00 64.10           C  
-ATOM    865  C   GLY A 125     -20.417  37.504  43.789  1.00 63.93           C  
-ATOM    866  O   GLY A 125     -20.768  37.896  42.672  1.00 64.34           O  
-ATOM    867  N   ARG A 126     -19.138  37.453  44.176  1.00 63.36           N  
-ATOM    868  CA  ARG A 126     -18.021  37.676  43.253  1.00 62.38           C  
-ATOM    869  C   ARG A 126     -18.342  37.089  41.888  1.00 62.35           C  
-ATOM    870  O   ARG A 126     -18.238  35.872  41.683  1.00 62.18           O  
-ATOM    871  CB  ARG A 126     -16.731  37.029  43.779  1.00 62.07           C  
-ATOM    872  CG  ARG A 126     -15.875  37.909  44.682  1.00 60.52           C  
-ATOM    873  CD  ARG A 126     -14.787  38.629  43.909  1.00 57.10           C  
-ATOM    874  NE  ARG A 126     -14.343  39.845  44.591  1.00 54.08           N  
-ATOM    875  CZ  ARG A 126     -13.692  40.847  44.001  1.00 51.60           C  
-ATOM    876  NH1 ARG A 126     -13.391  40.779  42.715  1.00 50.24           N  
-ATOM    877  NH2 ARG A 126     -13.341  41.920  44.701  1.00 49.02           N  
-ATOM    878  N   LYS A 127     -18.741  37.965  40.964  1.00 62.29           N  
-ATOM    879  CA  LYS A 127     -19.029  37.581  39.586  1.00 61.86           C  
-ATOM    880  C   LYS A 127     -17.820  36.856  39.003  1.00 61.46           C  
-ATOM    881  O   LYS A 127     -16.676  37.102  39.415  1.00 61.87           O  
-ATOM    882  CB  LYS A 127     -19.388  38.812  38.750  1.00 61.83           C  
-ATOM    883  N   ILE A 128     -18.059  35.940  38.069  1.00 60.62           N  
-ATOM    884  CA  ILE A 128     -16.940  35.185  37.497  1.00 59.75           C  
-ATOM    885  C   ILE A 128     -16.200  36.061  36.472  1.00 58.84           C  
-ATOM    886  O   ILE A 128     -16.821  36.690  35.608  1.00 59.70           O  
-ATOM    887  CB  ILE A 128     -17.371  33.760  37.004  1.00 59.93           C  
-ATOM    888  CG1 ILE A 128     -17.855  32.932  38.218  1.00 59.86           C  
-ATOM    889  CG2 ILE A 128     -16.220  33.063  36.266  1.00 60.44           C  
-ATOM    890  CD1 ILE A 128     -18.505  31.570  37.918  1.00 59.61           C  
-ATOM    891  N   GLY A 129     -14.882  36.154  36.617  1.00 57.11           N  
-ATOM    892  CA  GLY A 129     -14.096  37.106  35.849  1.00 54.72           C  
-ATOM    893  C   GLY A 129     -13.640  38.295  36.676  1.00 53.23           C  
-ATOM    894  O   GLY A 129     -12.863  39.111  36.204  1.00 52.88           O  
-ATOM    895  N   SER A 130     -14.127  38.411  37.910  1.00 51.86           N  
-ATOM    896  CA  SER A 130     -13.680  39.492  38.792  1.00 50.42           C  
-ATOM    897  C   SER A 130     -12.530  39.041  39.709  1.00 49.70           C  
-ATOM    898  O   SER A 130     -11.900  39.869  40.374  1.00 49.71           O  
-ATOM    899  CB  SER A 130     -14.841  40.035  39.627  1.00 50.12           C  
-ATOM    900  OG  SER A 130     -15.273  39.042  40.512  1.00 48.71           O  
-ATOM    901  N   CYS A 131     -12.298  37.727  39.758  1.00 48.38           N  
-ATOM    902  CA  CYS A 131     -11.156  37.133  40.429  1.00 46.95           C  
-ATOM    903  C   CYS A 131     -10.435  36.252  39.406  1.00 46.08           C  
-ATOM    904  O   CYS A 131     -10.970  35.228  38.964  1.00 46.32           O  
-ATOM    905  CB  CYS A 131     -11.588  36.303  41.649  1.00 47.21           C  
-ATOM    906  SG  CYS A 131     -10.186  35.551  42.513  1.00 49.73           S  
-ATOM    907  N   LEU A 132      -9.226  36.664  39.043  1.00 43.66           N  
-ATOM    908  CA  LEU A 132      -8.474  36.073  37.939  1.00 42.62           C  
-ATOM    909  C   LEU A 132      -7.269  35.326  38.507  1.00 41.95           C  
-ATOM    910  O   LEU A 132      -6.322  35.954  38.976  1.00 42.50           O  
-ATOM    911  CB  LEU A 132      -8.033  37.183  36.974  1.00 42.17           C  
-ATOM    912  CG  LEU A 132      -9.146  38.071  36.411  1.00 43.37           C  
-ATOM    913  CD1 LEU A 132      -8.563  39.290  35.713  1.00 43.22           C  
-ATOM    914  CD2 LEU A 132     -10.031  37.280  35.461  1.00 43.89           C  
-ATOM    915  N   ILE A 133      -7.319  33.991  38.487  1.00 40.38           N  
-ATOM    916  CA  ILE A 133      -6.262  33.188  39.080  1.00 40.98           C  
-ATOM    917  C   ILE A 133      -5.373  32.558  38.014  1.00 40.77           C  
-ATOM    918  O   ILE A 133      -5.828  31.765  37.192  1.00 38.94           O  
-ATOM    919  CB  ILE A 133      -6.829  32.107  40.058  1.00 40.50           C  
-ATOM    920  CG1 ILE A 133      -7.688  32.788  41.129  1.00 40.62           C  
-ATOM    921  CG2 ILE A 133      -5.654  31.295  40.693  1.00 41.17           C  
-ATOM    922  CD1 ILE A 133      -8.550  31.822  41.985  1.00 41.56           C  
-ATOM    923  N   GLY A 134      -4.105  32.973  37.994  1.00 42.18           N  
-ATOM    924  CA  GLY A 134      -3.132  32.330  37.122  1.00 42.60           C  
-ATOM    925  C   GLY A 134      -1.921  31.836  37.882  1.00 42.55           C  
-ATOM    926  O   GLY A 134      -1.908  31.784  39.110  1.00 43.00           O  
-ATOM    927  N   ALA A 135      -0.891  31.471  37.150  1.00 42.52           N  
-ATOM    928  CA  ALA A 135       0.305  30.926  37.780  1.00 42.43           C  
-ATOM    929  C   ALA A 135       1.547  31.520  37.164  1.00 43.10           C  
-ATOM    930  O   ALA A 135       1.590  31.783  35.959  1.00 43.02           O  
-ATOM    931  CB  ALA A 135       0.319  29.431  37.638  1.00 42.31           C  
-ATOM    932  N   MET A 136       2.561  31.713  38.003  1.00 43.51           N  
-ATOM    933  CA  MET A 136       3.859  32.169  37.584  1.00 44.44           C  
-ATOM    934  C   MET A 136       4.909  31.222  38.227  1.00 44.50           C  
-ATOM    935  O   MET A 136       5.338  31.416  39.376  1.00 43.93           O  
-ATOM    936  CB  MET A 136       4.054  33.644  37.973  1.00 45.93           C  
-ATOM    937  CG  MET A 136       5.390  34.209  37.574  1.00 46.19           C  
-ATOM    938  SD  MET A 136       5.739  33.933  35.840  1.00 54.29           S  
-ATOM    939  CE  MET A 136       7.543  34.150  35.822  1.00 48.22           C  
-ATOM    940  N   PRO A 137       5.299  30.171  37.487  1.00 44.01           N  
-ATOM    941  CA  PRO A 137       6.218  29.198  38.071  1.00 44.25           C  
-ATOM    942  C   PRO A 137       7.661  29.698  38.144  1.00 44.20           C  
-ATOM    943  O   PRO A 137       8.072  30.523  37.345  1.00 44.25           O  
-ATOM    944  CB  PRO A 137       6.087  27.986  37.148  1.00 44.64           C  
-ATOM    945  CG  PRO A 137       5.646  28.510  35.851  1.00 44.80           C  
-ATOM    946  CD  PRO A 137       4.879  29.799  36.121  1.00 44.81           C  
-ATOM    947  N   GLY A 138       8.399  29.228  39.130  1.00 44.22           N  
-ATOM    948  CA  GLY A 138       9.799  29.568  39.242  1.00 45.01           C  
-ATOM    949  C   GLY A 138      10.226  29.634  40.686  1.00 45.82           C  
-ATOM    950  O   GLY A 138       9.410  29.486  41.588  1.00 45.81           O  
-ATOM    951  N   SER A 139      11.511  29.891  40.901  1.00 46.22           N  
-ATOM    952  CA  SER A 139      12.050  30.088  42.245  1.00 46.67           C  
-ATOM    953  C   SER A 139      11.757  31.495  42.751  1.00 46.95           C  
-ATOM    954  O   SER A 139      11.975  32.471  42.032  1.00 46.62           O  
-ATOM    955  CB  SER A 139      13.565  29.859  42.219  1.00 46.92           C  
-ATOM    956  OG  SER A 139      14.124  30.134  43.478  1.00 47.74           O  
-ATOM    957  N   PHE A 140      11.284  31.620  43.991  1.00 47.22           N  
-ATOM    958  CA  PHE A 140      11.128  32.955  44.543  1.00 47.94           C  
-ATOM    959  C   PHE A 140      12.442  33.617  44.916  1.00 47.84           C  
-ATOM    960  O   PHE A 140      12.448  34.740  45.373  1.00 48.75           O  
-ATOM    961  CB  PHE A 140      10.057  33.069  45.652  1.00 48.74           C  
-ATOM    962  CG  PHE A 140      10.177  32.079  46.777  1.00 50.14           C  
-ATOM    963  CD1 PHE A 140      11.362  31.932  47.511  1.00 50.74           C  
-ATOM    964  CD2 PHE A 140       9.052  31.371  47.182  1.00 51.28           C  
-ATOM    965  CE1 PHE A 140      11.435  31.031  48.573  1.00 49.07           C  
-ATOM    966  CE2 PHE A 140       9.098  30.478  48.251  1.00 50.75           C  
-ATOM    967  CZ  PHE A 140      10.290  30.298  48.951  1.00 52.46           C  
-ATOM    968  N   TYR A 141      13.556  32.927  44.681  1.00 47.68           N  
-ATOM    969  CA  TYR A 141      14.862  33.547  44.788  1.00 47.36           C  
-ATOM    970  C   TYR A 141      15.320  34.206  43.461  1.00 47.34           C  
-ATOM    971  O   TYR A 141      16.434  34.715  43.356  1.00 48.14           O  
-ATOM    972  CB  TYR A 141      15.891  32.538  45.370  1.00 47.55           C  
-ATOM    973  CG  TYR A 141      15.538  32.065  46.789  1.00 46.57           C  
-ATOM    974  CD1 TYR A 141      15.367  32.982  47.812  1.00 42.77           C  
-ATOM    975  CD2 TYR A 141      15.369  30.701  47.095  1.00 44.95           C  
-ATOM    976  CE1 TYR A 141      15.046  32.593  49.086  1.00 44.55           C  
-ATOM    977  CE2 TYR A 141      15.053  30.299  48.397  1.00 44.81           C  
-ATOM    978  CZ  TYR A 141      14.893  31.254  49.379  1.00 46.73           C  
-ATOM    979  OH  TYR A 141      14.566  30.918  50.668  1.00 47.21           O  
-ATOM    980  N   SER A 142      14.455  34.192  42.453  1.00 47.23           N  
-ATOM    981  CA  SER A 142      14.659  34.971  41.240  1.00 48.09           C  
-ATOM    982  C   SER A 142      13.440  35.874  40.948  1.00 47.84           C  
-ATOM    983  O   SER A 142      12.390  35.741  41.601  1.00 47.44           O  
-ATOM    984  CB  SER A 142      14.989  34.049  40.052  1.00 49.28           C  
-ATOM    985  OG  SER A 142      14.229  32.840  40.092  1.00 51.26           O  
-ATOM    986  N   ARG A 143      13.594  36.805  40.003  1.00 46.65           N  
-ATOM    987  CA  ARG A 143      12.493  37.657  39.582  1.00 46.76           C  
-ATOM    988  C   ARG A 143      11.325  36.840  39.043  1.00 45.33           C  
-ATOM    989  O   ARG A 143      11.534  35.938  38.257  1.00 43.64           O  
-ATOM    990  CB  ARG A 143      12.963  38.640  38.526  1.00 46.98           C  
-ATOM    991  CG  ARG A 143      11.854  39.524  37.981  1.00 51.98           C  
-ATOM    992  CD  ARG A 143      12.431  40.802  37.367  1.00 56.77           C  
-ATOM    993  NE  ARG A 143      11.589  41.938  37.736  1.00 62.40           N  
-ATOM    994  CZ  ARG A 143      11.665  42.605  38.886  1.00 63.61           C  
-ATOM    995  NH1 ARG A 143      12.568  42.290  39.820  1.00 66.14           N  
-ATOM    996  NH2 ARG A 143      10.824  43.590  39.107  1.00 62.44           N  
-ATOM    997  N   LEU A 144      10.114  37.182  39.485  1.00 43.59           N  
-ATOM    998  CA  LEU A 144       8.850  36.562  39.044  1.00 43.04           C  
-ATOM    999  C   LEU A 144       7.901  37.532  38.321  1.00 42.37           C  
-ATOM   1000  O   LEU A 144       7.073  37.110  37.514  1.00 42.54           O  
-ATOM   1001  CB  LEU A 144       8.108  35.948  40.253  1.00 42.07           C  
-ATOM   1002  CG  LEU A 144       8.724  34.724  40.929  1.00 42.80           C  
-ATOM   1003  CD1 LEU A 144       8.087  34.415  42.341  1.00 40.25           C  
-ATOM   1004  CD2 LEU A 144       8.678  33.504  39.996  1.00 41.09           C  
-ATOM   1005  N   PHE A 145       8.043  38.825  38.597  1.00 42.44           N  
-ATOM   1006  CA  PHE A 145       7.038  39.837  38.227  1.00 42.62           C  
-ATOM   1007  C   PHE A 145       7.704  41.059  37.689  1.00 42.68           C  
-ATOM   1008  O   PHE A 145       8.814  41.348  38.081  1.00 42.87           O  
-ATOM   1009  CB  PHE A 145       6.150  40.196  39.423  1.00 41.98           C  
-ATOM   1010  CG  PHE A 145       5.457  39.016  40.011  1.00 45.56           C  
-ATOM   1011  CD1 PHE A 145       4.521  38.310  39.264  1.00 45.23           C  
-ATOM   1012  CD2 PHE A 145       5.763  38.583  41.302  1.00 44.56           C  
-ATOM   1013  CE1 PHE A 145       3.894  37.199  39.791  1.00 44.53           C  
-ATOM   1014  CE2 PHE A 145       5.137  37.497  41.838  1.00 43.94           C  
-ATOM   1015  CZ  PHE A 145       4.191  36.788  41.078  1.00 45.55           C  
-ATOM   1016  N   PRO A 146       7.045  41.774  36.756  1.00 44.34           N  
-ATOM   1017  CA  PRO A 146       7.596  43.053  36.313  1.00 44.52           C  
-ATOM   1018  C   PRO A 146       7.791  44.049  37.459  1.00 45.30           C  
-ATOM   1019  O   PRO A 146       7.147  43.951  38.525  1.00 45.40           O  
-ATOM   1020  CB  PRO A 146       6.559  43.570  35.310  1.00 45.47           C  
-ATOM   1021  CG  PRO A 146       5.713  42.394  34.972  1.00 46.05           C  
-ATOM   1022  CD  PRO A 146       5.783  41.437  36.081  1.00 43.71           C  
-ATOM   1023  N   GLU A 147       8.704  44.988  37.237  1.00 45.03           N  
-ATOM   1024  CA  GLU A 147       8.998  46.046  38.211  1.00 45.87           C  
-ATOM   1025  C   GLU A 147       7.753  46.861  38.572  1.00 43.94           C  
-ATOM   1026  O   GLU A 147       6.944  47.221  37.699  1.00 42.94           O  
-ATOM   1027  CB  GLU A 147      10.146  46.948  37.705  1.00 45.59           C  
-ATOM   1028  CG  GLU A 147      11.483  46.173  37.531  1.00 47.76           C  
-ATOM   1029  CD  GLU A 147      12.732  47.052  37.609  1.00 49.37           C  
-ATOM   1030  OE1 GLU A 147      12.659  48.239  37.191  0.50 50.09           O  
-ATOM   1031  OE2 GLU A 147      13.792  46.536  38.081  1.00 53.15           O  
-ATOM   1032  N   GLU A 148       7.593  47.100  39.869  1.00 42.49           N  
-ATOM   1033  CA  GLU A 148       6.515  47.937  40.408  1.00 42.85           C  
-ATOM   1034  C   GLU A 148       5.152  47.555  39.852  1.00 42.26           C  
-ATOM   1035  O   GLU A 148       4.409  48.414  39.373  1.00 41.47           O  
-ATOM   1036  CB  GLU A 148       6.787  49.416  40.131  1.00 42.73           C  
-ATOM   1037  CG  GLU A 148       7.753  50.061  41.075  1.00 45.43           C  
-ATOM   1038  CD  GLU A 148       7.771  51.567  40.943  1.00 52.25           C  
-ATOM   1039  OE1 GLU A 148       6.944  52.249  41.603  1.00 54.04           O  
-ATOM   1040  OE2 GLU A 148       8.632  52.074  40.193  1.00 54.64           O  
-ATOM   1041  N   SER A 149       4.837  46.267  39.923  1.00 41.30           N  
-ATOM   1042  CA  SER A 149       3.606  45.737  39.348  1.00 41.79           C  
-ATOM   1043  C   SER A 149       2.671  45.083  40.366  1.00 41.70           C  
-ATOM   1044  O   SER A 149       1.516  44.787  40.035  1.00 42.46           O  
-ATOM   1045  CB  SER A 149       3.910  44.732  38.230  1.00 41.91           C  
-ATOM   1046  OG  SER A 149       4.600  43.606  38.728  1.00 42.51           O  
-ATOM   1047  N   MET A 150       3.151  44.835  41.589  1.00 41.10           N  
-ATOM   1048  CA  MET A 150       2.374  44.022  42.514  1.00 40.02           C  
-ATOM   1049  C   MET A 150       1.996  44.824  43.750  1.00 39.60           C  
-ATOM   1050  O   MET A 150       2.775  45.640  44.208  1.00 39.28           O  
-ATOM   1051  CB  MET A 150       3.148  42.742  42.907  1.00 40.54           C  
-ATOM   1052  CG  MET A 150       3.534  41.850  41.701  1.00 40.72           C  
-ATOM   1053  SD  MET A 150       2.058  41.145  40.929  1.00 46.69           S  
-ATOM   1054  CE  MET A 150       1.839  39.742  42.033  1.00 41.85           C  
-ATOM   1055  N   HIS A 151       0.812  44.576  44.295  1.00 39.91           N  
-ATOM   1056  CA  HIS A 151       0.402  45.245  45.552  1.00 40.14           C  
-ATOM   1057  C   HIS A 151       0.820  44.470  46.795  1.00 40.19           C  
-ATOM   1058  O   HIS A 151       1.144  45.063  47.824  1.00 40.53           O  
-ATOM   1059  CB  HIS A 151      -1.101  45.489  45.612  1.00 39.77           C  
-ATOM   1060  CG  HIS A 151      -1.607  46.475  44.603  1.00 39.98           C  
-ATOM   1061  ND1 HIS A 151      -2.265  46.084  43.455  1.00 39.79           N  
-ATOM   1062  CD2 HIS A 151      -1.538  47.827  44.555  1.00 37.34           C  
-ATOM   1063  CE1 HIS A 151      -2.583  47.147  42.746  1.00 39.73           C  
-ATOM   1064  NE2 HIS A 151      -2.171  48.221  43.399  1.00 39.46           N  
-ATOM   1065  N   PHE A 152       0.782  43.139  46.719  1.00 40.31           N  
-ATOM   1066  CA  PHE A 152       0.902  42.340  47.917  1.00 40.85           C  
-ATOM   1067  C   PHE A 152       1.442  40.949  47.598  1.00 41.06           C  
-ATOM   1068  O   PHE A 152       0.999  40.330  46.649  1.00 40.89           O  
-ATOM   1069  CB  PHE A 152      -0.469  42.257  48.586  1.00 41.26           C  
-ATOM   1070  CG  PHE A 152      -0.497  41.404  49.825  1.00 44.11           C  
-ATOM   1071  CD1 PHE A 152       0.179  41.802  50.981  1.00 44.68           C  
-ATOM   1072  CD2 PHE A 152      -1.221  40.213  49.842  1.00 44.12           C  
-ATOM   1073  CE1 PHE A 152       0.149  41.027  52.119  1.00 44.67           C  
-ATOM   1074  CE2 PHE A 152      -1.256  39.437  50.985  1.00 47.60           C  
-ATOM   1075  CZ  PHE A 152      -0.566  39.843  52.128  1.00 45.01           C  
-ATOM   1076  N   LEU A 153       2.437  40.503  48.366  1.00 40.96           N  
-ATOM   1077  CA  LEU A 153       3.035  39.174  48.211  1.00 41.86           C  
-ATOM   1078  C   LEU A 153       2.894  38.429  49.526  1.00 41.85           C  
-ATOM   1079  O   LEU A 153       3.126  39.000  50.593  1.00 42.87           O  
-ATOM   1080  CB  LEU A 153       4.515  39.275  47.811  1.00 41.40           C  
-ATOM   1081  CG  LEU A 153       4.798  39.926  46.457  1.00 42.95           C  
-ATOM   1082  CD1 LEU A 153       6.265  40.392  46.290  1.00 40.96           C  
-ATOM   1083  CD2 LEU A 153       4.353  39.020  45.324  1.00 42.32           C  
-ATOM   1084  N   HIS A 154       2.470  37.177  49.451  1.00 41.83           N  
-ATOM   1085  CA  HIS A 154       2.206  36.390  50.633  1.00 42.36           C  
-ATOM   1086  C   HIS A 154       3.022  35.108  50.464  1.00 42.25           C  
-ATOM   1087  O   HIS A 154       3.131  34.600  49.359  1.00 41.50           O  
-ATOM   1088  CB  HIS A 154       0.699  36.049  50.750  1.00 42.90           C  
-ATOM   1089  CG  HIS A 154       0.402  34.992  51.772  1.00 42.51           C  
-ATOM   1090  ND1 HIS A 154       0.278  33.652  51.461  1.00 43.92           N  
-ATOM   1091  CD2 HIS A 154       0.257  35.079  53.116  1.00 41.74           C  
-ATOM   1092  CE1 HIS A 154       0.076  32.961  52.568  1.00 42.78           C  
-ATOM   1093  NE2 HIS A 154       0.047  33.806  53.585  1.00 44.19           N  
-ATOM   1094  N   SER A 155       3.623  34.623  51.544  1.00 42.18           N  
-ATOM   1095  CA  SER A 155       4.231  33.285  51.532  1.00 42.33           C  
-ATOM   1096  C   SER A 155       4.066  32.662  52.898  1.00 42.36           C  
-ATOM   1097  O   SER A 155       4.394  33.295  53.883  1.00 42.41           O  
-ATOM   1098  CB  SER A 155       5.713  33.354  51.173  1.00 41.75           C  
-ATOM   1099  OG  SER A 155       6.311  32.052  51.212  1.00 44.65           O  
-ATOM   1100  N   CYS A 156       3.574  31.420  52.964  1.00 43.05           N  
-ATOM   1101  CA  CYS A 156       3.450  30.748  54.247  1.00 43.05           C  
-ATOM   1102  C   CYS A 156       4.194  29.431  54.209  1.00 43.29           C  
-ATOM   1103  O   CYS A 156       3.846  28.547  53.432  1.00 41.52           O  
-ATOM   1104  CB  CYS A 156       1.980  30.494  54.622  1.00 43.87           C  
-ATOM   1105  SG  CYS A 156       1.753  29.642  56.202  1.00 45.30           S  
-ATOM   1106  N   TYR A 157       5.224  29.332  55.041  1.00 43.10           N  
-ATOM   1107  CA  TYR A 157       5.947  28.093  55.275  1.00 44.15           C  
-ATOM   1108  C   TYR A 157       6.846  27.605  54.141  1.00 44.93           C  
-ATOM   1109  O   TYR A 157       6.950  26.387  53.846  1.00 45.42           O  
-ATOM   1110  CB  TYR A 157       5.020  27.029  55.862  1.00 44.52           C  
-ATOM   1111  CG  TYR A 157       5.319  26.878  57.316  1.00 44.24           C  
-ATOM   1112  CD1 TYR A 157       5.065  27.916  58.223  1.00 44.42           C  
-ATOM   1113  CD2 TYR A 157       5.945  25.732  57.776  1.00 45.43           C  
-ATOM   1114  CE1 TYR A 157       5.396  27.773  59.559  1.00 44.59           C  
-ATOM   1115  CE2 TYR A 157       6.280  25.584  59.073  1.00 45.17           C  
-ATOM   1116  CZ  TYR A 157       6.008  26.588  59.969  1.00 43.84           C  
-ATOM   1117  OH  TYR A 157       6.363  26.373  61.272  1.00 43.13           O  
-ATOM   1118  N   CYS A 158       7.542  28.577  53.554  1.00 44.39           N  
-ATOM   1119  CA  CYS A 158       8.381  28.333  52.400  1.00 45.73           C  
-ATOM   1120  C   CYS A 158       9.791  28.858  52.561  1.00 44.31           C  
-ATOM   1121  O   CYS A 158      10.723  28.219  52.116  1.00 43.38           O  
-ATOM   1122  CB  CYS A 158       7.749  28.938  51.149  1.00 45.93           C  
-ATOM   1123  SG  CYS A 158       6.132  28.283  50.785  1.00 53.25           S  
-ATOM   1124  N   LEU A 159       9.928  30.033  53.175  1.00 44.29           N  
-ATOM   1125  CA  LEU A 159      11.210  30.744  53.212  1.00 44.16           C  
-ATOM   1126  C   LEU A 159      12.321  30.102  54.041  1.00 42.58           C  
-ATOM   1127  O   LEU A 159      13.465  30.496  53.928  1.00 41.80           O  
-ATOM   1128  CB  LEU A 159      11.036  32.191  53.647  1.00 44.34           C  
-ATOM   1129  CG  LEU A 159      10.694  33.059  52.443  1.00 49.07           C  
-ATOM   1130  CD1 LEU A 159       9.897  34.229  52.928  1.00 51.01           C  
-ATOM   1131  CD2 LEU A 159      11.968  33.496  51.720  1.00 51.10           C  
-ATOM   1132  N   HIS A 160      11.989  29.102  54.836  1.00 42.46           N  
-ATOM   1133  CA  HIS A 160      13.030  28.305  55.513  1.00 41.68           C  
-ATOM   1134  C   HIS A 160      13.758  27.360  54.550  1.00 41.43           C  
-ATOM   1135  O   HIS A 160      14.872  26.917  54.839  1.00 40.69           O  
-ATOM   1136  CB  HIS A 160      12.420  27.544  56.694  1.00 41.14           C  
-ATOM   1137  CG  HIS A 160      11.126  26.864  56.368  1.00 41.66           C  
-ATOM   1138  ND1 HIS A 160       9.909  27.325  56.819  1.00 39.37           N  
-ATOM   1139  CD2 HIS A 160      10.865  25.736  55.662  1.00 42.04           C  
-ATOM   1140  CE1 HIS A 160       8.953  26.524  56.388  1.00 44.05           C  
-ATOM   1141  NE2 HIS A 160       9.506  25.549  55.688  1.00 41.01           N  
-ATOM   1142  N   TRP A 161      13.126  27.039  53.417  1.00 41.52           N  
-ATOM   1143  CA  TRP A 161      13.812  26.301  52.330  1.00 41.69           C  
-ATOM   1144  C   TRP A 161      14.850  27.203  51.661  1.00 41.82           C  
-ATOM   1145  O   TRP A 161      14.506  28.283  51.175  1.00 42.54           O  
-ATOM   1146  CB  TRP A 161      12.807  25.778  51.284  1.00 41.92           C  
-ATOM   1147  CG  TRP A 161      11.949  24.662  51.799  1.00 41.02           C  
-ATOM   1148  CD1 TRP A 161      10.671  24.763  52.265  1.00 43.20           C  
-ATOM   1149  CD2 TRP A 161      12.308  23.293  51.917  1.00 41.59           C  
-ATOM   1150  NE1 TRP A 161      10.214  23.542  52.684  1.00 40.90           N  
-ATOM   1151  CE2 TRP A 161      11.195  22.615  52.477  1.00 41.49           C  
-ATOM   1152  CE3 TRP A 161      13.463  22.571  51.626  1.00 42.19           C  
-ATOM   1153  CZ2 TRP A 161      11.198  21.251  52.728  1.00 42.22           C  
-ATOM   1154  CZ3 TRP A 161      13.469  21.195  51.863  1.00 42.87           C  
-ATOM   1155  CH2 TRP A 161      12.345  20.549  52.413  1.00 43.00           C  
-ATOM   1156  N   LEU A 162      16.114  26.777  51.671  1.00 40.69           N  
-ATOM   1157  CA  LEU A 162      17.220  27.539  51.055  1.00 40.45           C  
-ATOM   1158  C   LEU A 162      17.293  27.306  49.534  1.00 41.00           C  
-ATOM   1159  O   LEU A 162      16.741  26.333  49.029  1.00 40.23           O  
-ATOM   1160  CB  LEU A 162      18.555  27.155  51.703  1.00 39.68           C  
-ATOM   1161  CG  LEU A 162      18.605  27.222  53.250  1.00 38.62           C  
-ATOM   1162  CD1 LEU A 162      19.830  26.526  53.791  1.00 35.61           C  
-ATOM   1163  CD2 LEU A 162      18.542  28.666  53.738  1.00 36.12           C  
-ATOM   1164  N   SER A 163      17.976  28.196  48.816  1.00 42.01           N  
-ATOM   1165  CA  SER A 163      18.222  28.006  47.368  1.00 43.45           C  
-ATOM   1166  C   SER A 163      19.148  26.818  47.064  1.00 43.88           C  
-ATOM   1167  O   SER A 163      19.127  26.247  45.952  1.00 43.06           O  
-ATOM   1168  CB  SER A 163      18.808  29.280  46.768  1.00 43.79           C  
-ATOM   1169  OG  SER A 163      20.179  29.432  47.123  1.00 44.62           O  
-ATOM   1170  N   GLN A 164      19.955  26.433  48.052  1.00 44.05           N  
-ATOM   1171  CA  GLN A 164      20.838  25.266  47.914  1.00 45.53           C  
-ATOM   1172  C   GLN A 164      21.301  24.740  49.276  1.00 45.41           C  
-ATOM   1173  O   GLN A 164      21.110  25.399  50.279  1.00 43.75           O  
-ATOM   1174  CB  GLN A 164      22.061  25.615  47.050  1.00 46.04           C  
-ATOM   1175  CG  GLN A 164      22.994  26.642  47.679  1.00 46.63           C  
-ATOM   1176  CD  GLN A 164      24.285  26.820  46.922  1.00 47.04           C  
-ATOM   1177  OE1 GLN A 164      24.330  27.574  45.967  1.00 50.37           O  
-ATOM   1178  NE2 GLN A 164      25.355  26.133  47.358  1.00 49.81           N  
-ATOM   1179  N   VAL A 165      21.926  23.563  49.305  1.00 45.69           N  
-ATOM   1180  CA  VAL A 165      22.625  23.127  50.510  1.00 46.58           C  
-ATOM   1181  C   VAL A 165      23.746  24.149  50.744  1.00 47.32           C  
-ATOM   1182  O   VAL A 165      24.419  24.576  49.782  1.00 46.71           O  
-ATOM   1183  CB  VAL A 165      23.103  21.646  50.410  1.00 47.03           C  
-ATOM   1184  CG1 VAL A 165      24.076  21.267  51.526  1.00 46.39           C  
-ATOM   1185  CG2 VAL A 165      21.893  20.734  50.465  1.00 48.16           C  
-ATOM   1186  N   PRO A 166      23.878  24.639  51.993  1.00 47.88           N  
-ATOM   1187  CA  PRO A 166      24.849  25.694  52.291  1.00 48.79           C  
-ATOM   1188  C   PRO A 166      26.202  25.528  51.626  1.00 49.79           C  
-ATOM   1189  O   PRO A 166      26.813  24.453  51.699  1.00 49.07           O  
-ATOM   1190  CB  PRO A 166      24.950  25.636  53.813  1.00 48.30           C  
-ATOM   1191  CG  PRO A 166      23.556  25.349  54.186  1.00 48.30           C  
-ATOM   1192  CD  PRO A 166      23.082  24.310  53.195  1.00 47.69           C  
-ATOM   1193  N   SER A 167      26.652  26.602  50.975  1.00 51.61           N  
-ATOM   1194  CA  SER A 167      27.844  26.529  50.131  1.00 53.46           C  
-ATOM   1195  C   SER A 167      29.143  26.351  50.920  1.00 54.20           C  
-ATOM   1196  O   SER A 167      30.236  26.533  50.379  1.00 54.04           O  
-ATOM   1197  CB  SER A 167      27.900  27.668  49.081  1.00 53.57           C  
-ATOM   1198  OG  SER A 167      27.851  28.962  49.657  1.00 55.05           O  
-ATOM   1199  N   GLY A 168      28.996  25.967  52.195  1.00 55.37           N  
-ATOM   1200  CA  GLY A 168      30.092  25.470  53.034  1.00 55.48           C  
-ATOM   1201  C   GLY A 168      30.230  23.951  52.963  1.00 56.56           C  
-ATOM   1202  O   GLY A 168      30.755  23.382  51.976  1.00 56.81           O  
-ATOM   1203  N   ILE A 175      29.656  18.843  50.836  1.00 59.79           N  
-ATOM   1204  CA  ILE A 175      30.849  18.006  50.958  1.00 59.71           C  
-ATOM   1205  C   ILE A 175      31.385  17.923  52.390  1.00 59.49           C  
-ATOM   1206  O   ILE A 175      31.796  16.852  52.821  1.00 60.13           O  
-ATOM   1207  CB  ILE A 175      31.979  18.454  50.007  1.00 59.93           C  
-ATOM   1208  N   SER A 176      31.379  19.034  53.129  1.00 58.88           N  
-ATOM   1209  CA  SER A 176      31.852  19.018  54.523  1.00 58.12           C  
-ATOM   1210  C   SER A 176      30.950  18.132  55.398  1.00 57.24           C  
-ATOM   1211  O   SER A 176      29.747  18.000  55.122  1.00 56.94           O  
-ATOM   1212  CB  SER A 176      31.944  20.438  55.107  1.00 58.56           C  
-ATOM   1213  N   VAL A 177      31.534  17.529  56.435  1.00 55.62           N  
-ATOM   1214  CA  VAL A 177      30.803  16.581  57.280  1.00 54.21           C  
-ATOM   1215  C   VAL A 177      30.043  17.218  58.466  1.00 52.79           C  
-ATOM   1216  O   VAL A 177      30.644  17.757  59.415  1.00 52.39           O  
-ATOM   1217  CB  VAL A 177      31.713  15.398  57.747  1.00 54.59           C  
-ATOM   1218  CG1 VAL A 177      30.953  14.441  58.663  1.00 54.82           C  
-ATOM   1219  CG2 VAL A 177      32.250  14.642  56.541  1.00 55.03           C  
-ATOM   1220  N   ASN A 178      28.713  17.149  58.372  1.00 50.57           N  
-ATOM   1221  CA  ASN A 178      27.794  17.447  59.464  1.00 49.09           C  
-ATOM   1222  C   ASN A 178      27.420  16.116  60.160  1.00 48.90           C  
-ATOM   1223  O   ASN A 178      26.414  15.487  59.823  1.00 49.09           O  
-ATOM   1224  CB  ASN A 178      26.560  18.191  58.902  1.00 48.38           C  
-ATOM   1225  CG  ASN A 178      25.635  18.743  59.989  1.00 46.76           C  
-ATOM   1226  OD1 ASN A 178      26.031  18.918  61.140  1.00 43.07           O  
-ATOM   1227  ND2 ASN A 178      24.390  19.039  59.611  1.00 40.26           N  
-ATOM   1228  N   LYS A 179      28.263  15.682  61.110  1.00 48.08           N  
-ATOM   1229  CA  LYS A 179      28.129  14.375  61.786  1.00 47.19           C  
-ATOM   1230  C   LYS A 179      26.893  14.265  62.663  1.00 45.98           C  
-ATOM   1231  O   LYS A 179      26.705  15.074  63.569  1.00 46.29           O  
-ATOM   1232  CB  LYS A 179      29.352  14.073  62.677  1.00 46.74           C  
-ATOM   1233  CG  LYS A 179      30.563  13.623  61.943  1.00 48.26           C  
-ATOM   1234  N   GLY A 180      26.083  13.238  62.406  1.00 45.01           N  
-ATOM   1235  CA  GLY A 180      24.888  12.931  63.197  1.00 43.74           C  
-ATOM   1236  C   GLY A 180      23.723  13.895  63.047  1.00 43.28           C  
-ATOM   1237  O   GLY A 180      22.728  13.789  63.775  1.00 43.36           O  
-ATOM   1238  N   CYS A 181      23.845  14.821  62.095  1.00 42.02           N  
-ATOM   1239  CA  CYS A 181      22.897  15.910  61.908  1.00 41.50           C  
-ATOM   1240  C   CYS A 181      22.493  16.078  60.437  1.00 40.47           C  
-ATOM   1241  O   CYS A 181      23.230  15.681  59.537  1.00 39.97           O  
-ATOM   1242  CB  CYS A 181      23.509  17.208  62.436  1.00 41.18           C  
-ATOM   1243  SG  CYS A 181      23.767  17.229  64.248  1.00 45.11           S  
-ATOM   1244  N   ILE A 182      21.338  16.697  60.189  1.00 39.52           N  
-ATOM   1245  CA  ILE A 182      20.878  16.888  58.808  1.00 38.64           C  
-ATOM   1246  C   ILE A 182      20.777  18.368  58.412  1.00 38.71           C  
-ATOM   1247  O   ILE A 182      20.606  18.689  57.240  1.00 36.85           O  
-ATOM   1248  CB  ILE A 182      19.564  16.082  58.510  1.00 38.20           C  
-ATOM   1249  CG1 ILE A 182      18.382  16.633  59.306  1.00 39.01           C  
-ATOM   1250  CG2 ILE A 182      19.766  14.615  58.829  1.00 36.96           C  
-ATOM   1251  CD1 ILE A 182      17.021  16.109  58.874  1.00 39.04           C  
-ATOM   1252  N   TYR A 183      20.912  19.252  59.406  1.00 38.00           N  
-ATOM   1253  CA  TYR A 183      20.898  20.702  59.178  1.00 38.49           C  
-ATOM   1254  C   TYR A 183      21.566  21.368  60.405  1.00 38.80           C  
-ATOM   1255  O   TYR A 183      22.192  20.680  61.225  1.00 38.67           O  
-ATOM   1256  CB  TYR A 183      19.454  21.215  58.874  1.00 38.49           C  
-ATOM   1257  CG  TYR A 183      18.612  21.484  60.106  1.00 37.90           C  
-ATOM   1258  CD1 TYR A 183      18.300  20.464  61.011  1.00 36.69           C  
-ATOM   1259  CD2 TYR A 183      18.162  22.790  60.391  1.00 37.74           C  
-ATOM   1260  CE1 TYR A 183      17.537  20.751  62.201  1.00 36.73           C  
-ATOM   1261  CE2 TYR A 183      17.422  23.070  61.530  1.00 37.61           C  
-ATOM   1262  CZ  TYR A 183      17.112  22.051  62.434  1.00 38.76           C  
-ATOM   1263  OH  TYR A 183      16.376  22.363  63.576  1.00 40.49           O  
-ATOM   1264  N   SER A 184      21.454  22.683  60.511  1.00 38.35           N  
-ATOM   1265  CA  SER A 184      21.983  23.429  61.626  1.00 39.63           C  
-ATOM   1266  C   SER A 184      21.126  23.213  62.888  1.00 39.76           C  
-ATOM   1267  O   SER A 184      20.557  24.146  63.427  1.00 40.01           O  
-ATOM   1268  CB  SER A 184      22.075  24.915  61.270  1.00 39.28           C  
-ATOM   1269  OG  SER A 184      20.905  25.351  60.613  1.00 41.52           O  
-ATOM   1270  N   SER A 185      21.017  21.969  63.346  1.00 40.34           N  
-ATOM   1271  CA  SER A 185      20.244  21.720  64.558  1.00 41.68           C  
-ATOM   1272  C   SER A 185      21.024  22.266  65.751  1.00 42.42           C  
-ATOM   1273  O   SER A 185      22.200  22.644  65.613  1.00 41.65           O  
-ATOM   1274  CB  SER A 185      19.969  20.227  64.746  1.00 41.24           C  
-ATOM   1275  OG  SER A 185      21.172  19.498  64.721  1.00 43.10           O  
-ATOM   1276  N   LYS A 186      20.371  22.292  66.917  1.00 43.92           N  
-ATOM   1277  CA  LYS A 186      21.027  22.708  68.167  1.00 44.89           C  
-ATOM   1278  C   LYS A 186      22.263  21.869  68.504  1.00 45.21           C  
-ATOM   1279  O   LYS A 186      23.229  22.361  69.107  1.00 46.87           O  
-ATOM   1280  CB  LYS A 186      20.026  22.688  69.334  1.00 45.48           C  
-ATOM   1281  N   ALA A 187      22.225  20.598  68.133  1.00 44.93           N  
-ATOM   1282  CA  ALA A 187      23.357  19.704  68.307  1.00 44.27           C  
-ATOM   1283  C   ALA A 187      24.461  19.804  67.235  1.00 43.92           C  
-ATOM   1284  O   ALA A 187      25.524  19.205  67.407  1.00 43.67           O  
-ATOM   1285  CB  ALA A 187      22.860  18.263  68.420  1.00 45.10           C  
-ATOM   1286  N   SER A 188      24.225  20.537  66.136  1.00 43.01           N  
-ATOM   1287  CA  SER A 188      25.257  20.687  65.101  1.00 42.38           C  
-ATOM   1288  C   SER A 188      26.398  21.624  65.556  1.00 41.81           C  
-ATOM   1289  O   SER A 188      26.169  22.586  66.305  1.00 40.89           O  
-ATOM   1290  CB  SER A 188      24.650  21.173  63.770  1.00 41.31           C  
-ATOM   1291  OG  SER A 188      24.187  22.493  63.918  1.00 42.77           O  
-ATOM   1292  N   ARG A 189      27.608  21.362  65.058  1.00 41.17           N  
-ATOM   1293  CA  ARG A 189      28.787  22.147  65.445  1.00 40.28           C  
-ATOM   1294  C   ARG A 189      28.731  23.574  64.869  1.00 39.44           C  
-ATOM   1295  O   ARG A 189      28.059  23.825  63.837  1.00 38.29           O  
-ATOM   1296  CB  ARG A 189      30.071  21.428  65.041  1.00 40.76           C  
-ATOM   1297  CG  ARG A 189      30.089  19.936  65.381  1.00 41.57           C  
-ATOM   1298  CD  ARG A 189      30.829  19.618  66.663  1.00 47.28           C  
-ATOM   1299  NE  ARG A 189      30.206  20.171  67.863  1.00 49.08           N  
-ATOM   1300  CZ  ARG A 189      30.517  19.791  69.104  1.00 51.58           C  
-ATOM   1301  NH1 ARG A 189      31.416  18.844  69.313  1.00 52.43           N  
-ATOM   1302  NH2 ARG A 189      29.921  20.355  70.142  1.00 50.97           N  
-ATOM   1303  N   PRO A 190      29.387  24.535  65.551  1.00 38.34           N  
-ATOM   1304  CA  PRO A 190      29.260  25.922  65.068  1.00 37.91           C  
-ATOM   1305  C   PRO A 190      29.680  26.255  63.612  1.00 36.73           C  
-ATOM   1306  O   PRO A 190      29.121  27.193  63.076  1.00 37.00           O  
-ATOM   1307  CB  PRO A 190      30.094  26.720  66.080  1.00 37.85           C  
-ATOM   1308  CG  PRO A 190      30.005  25.881  67.341  1.00 37.97           C  
-ATOM   1309  CD  PRO A 190      30.179  24.485  66.801  1.00 37.90           C  
-ATOM   1310  N   PRO A 191      30.664  25.544  62.998  1.00 36.92           N  
-ATOM   1311  CA  PRO A 191      30.907  25.910  61.586  1.00 36.75           C  
-ATOM   1312  C   PRO A 191      29.703  25.587  60.682  1.00 37.20           C  
-ATOM   1313  O   PRO A 191      29.505  26.249  59.640  1.00 36.10           O  
-ATOM   1314  CB  PRO A 191      32.103  25.041  61.186  1.00 37.08           C  
-ATOM   1315  CG  PRO A 191      32.742  24.574  62.505  1.00 36.51           C  
-ATOM   1316  CD  PRO A 191      31.564  24.455  63.431  1.00 36.53           C  
-ATOM   1317  N   ILE A 192      28.929  24.571  61.078  1.00 37.22           N  
-ATOM   1318  CA  ILE A 192      27.702  24.195  60.368  1.00 37.93           C  
-ATOM   1319  C   ILE A 192      26.641  25.262  60.546  1.00 38.02           C  
-ATOM   1320  O   ILE A 192      26.041  25.726  59.558  1.00 37.09           O  
-ATOM   1321  CB  ILE A 192      27.141  22.820  60.825  1.00 38.49           C  
-ATOM   1322  CG1 ILE A 192      28.196  21.709  60.624  1.00 38.02           C  
-ATOM   1323  CG2 ILE A 192      25.790  22.505  60.095  1.00 38.77           C  
-ATOM   1324  CD1 ILE A 192      28.613  21.475  59.169  1.00 42.85           C  
-ATOM   1325  N   GLN A 193      26.437  25.660  61.802  1.00 37.68           N  
-ATOM   1326  CA  GLN A 193      25.496  26.707  62.154  1.00 38.85           C  
-ATOM   1327  C   GLN A 193      25.821  27.976  61.364  1.00 38.05           C  
-ATOM   1328  O   GLN A 193      24.931  28.619  60.842  1.00 38.30           O  
-ATOM   1329  CB  GLN A 193      25.556  26.993  63.667  1.00 39.02           C  
-ATOM   1330  CG  GLN A 193      25.174  25.815  64.591  1.00 40.00           C  
-ATOM   1331  CD  GLN A 193      25.156  26.215  66.076  1.00 41.09           C  
-ATOM   1332  OE1 GLN A 193      24.601  27.264  66.455  1.00 45.12           O  
-ATOM   1333  NE2 GLN A 193      25.760  25.389  66.915  1.00 40.77           N  
-ATOM   1334  N   LYS A 194      27.104  28.350  61.299  1.00 38.17           N  
-ATOM   1335  CA  LYS A 194      27.493  29.576  60.562  1.00 38.44           C  
-ATOM   1336  C   LYS A 194      27.287  29.426  59.048  1.00 36.78           C  
-ATOM   1337  O   LYS A 194      26.861  30.355  58.375  1.00 36.96           O  
-ATOM   1338  CB  LYS A 194      28.944  29.973  60.872  1.00 37.76           C  
-ATOM   1339  CG  LYS A 194      29.406  31.276  60.191  1.00 39.82           C  
-ATOM   1340  CD  LYS A 194      30.787  31.738  60.669  1.00 40.68           C  
-ATOM   1341  CE  LYS A 194      31.461  32.659  59.654  1.00 45.37           C  
-ATOM   1342  NZ  LYS A 194      32.066  31.884  58.517  1.00 48.40           N  
-ATOM   1343  N   ALA A 195      27.628  28.259  58.508  1.00 37.00           N  
-ATOM   1344  CA  ALA A 195      27.375  27.964  57.091  1.00 36.08           C  
-ATOM   1345  C   ALA A 195      25.889  28.066  56.718  1.00 35.81           C  
-ATOM   1346  O   ALA A 195      25.529  28.640  55.679  1.00 35.39           O  
-ATOM   1347  CB  ALA A 195      27.958  26.553  56.701  1.00 37.13           C  
-ATOM   1348  N   TYR A 196      25.022  27.507  57.553  1.00 36.03           N  
-ATOM   1349  CA  TYR A 196      23.562  27.597  57.316  1.00 36.26           C  
-ATOM   1350  C   TYR A 196      23.014  29.034  57.460  1.00 36.71           C  
-ATOM   1351  O   TYR A 196      22.204  29.459  56.633  1.00 36.88           O  
-ATOM   1352  CB  TYR A 196      22.794  26.618  58.211  1.00 36.27           C  
-ATOM   1353  CG  TYR A 196      22.623  25.206  57.610  1.00 36.31           C  
-ATOM   1354  CD1 TYR A 196      23.611  24.241  57.724  1.00 36.64           C  
-ATOM   1355  CD2 TYR A 196      21.454  24.859  56.943  1.00 39.10           C  
-ATOM   1356  CE1 TYR A 196      23.449  22.951  57.175  1.00 37.58           C  
-ATOM   1357  CE2 TYR A 196      21.279  23.581  56.380  1.00 37.86           C  
-ATOM   1358  CZ  TYR A 196      22.264  22.647  56.491  1.00 37.17           C  
-ATOM   1359  OH  TYR A 196      22.046  21.412  55.935  1.00 34.74           O  
-ATOM   1360  N   LEU A 197      23.459  29.771  58.488  1.00 36.81           N  
-ATOM   1361  CA  LEU A 197      23.052  31.181  58.667  1.00 37.08           C  
-ATOM   1362  C   LEU A 197      23.477  32.034  57.487  1.00 37.13           C  
-ATOM   1363  O   LEU A 197      22.661  32.777  56.950  1.00 38.81           O  
-ATOM   1364  CB  LEU A 197      23.550  31.800  60.004  1.00 37.08           C  
-ATOM   1365  CG  LEU A 197      23.331  33.333  60.143  1.00 36.96           C  
-ATOM   1366  CD1 LEU A 197      21.835  33.720  60.033  1.00 36.03           C  
-ATOM   1367  CD2 LEU A 197      23.972  33.949  61.412  1.00 37.77           C  
-ATOM   1368  N   ASP A 198      24.746  31.934  57.092  1.00 37.70           N  
-ATOM   1369  CA  ASP A 198      25.275  32.671  55.940  1.00 38.13           C  
-ATOM   1370  C   ASP A 198      24.489  32.374  54.670  1.00 37.81           C  
-ATOM   1371  O   ASP A 198      24.258  33.281  53.902  1.00 37.56           O  
-ATOM   1372  CB  ASP A 198      26.763  32.393  55.687  1.00 38.62           C  
-ATOM   1373  CG  ASP A 198      27.695  33.069  56.702  1.00 40.32           C  
-ATOM   1374  OD1 ASP A 198      27.327  34.074  57.366  1.00 43.63           O  
-ATOM   1375  OD2 ASP A 198      28.843  32.592  56.795  1.00 43.53           O  
-ATOM   1376  N   GLN A 199      24.080  31.118  54.457  1.00 37.46           N  
-ATOM   1377  CA  GLN A 199      23.240  30.767  53.299  1.00 38.20           C  
-ATOM   1378  C   GLN A 199      21.862  31.443  53.375  1.00 38.97           C  
-ATOM   1379  O   GLN A 199      21.449  32.093  52.406  1.00 39.19           O  
-ATOM   1380  CB  GLN A 199      23.094  29.237  53.105  1.00 37.64           C  
-ATOM   1381  CG  GLN A 199      22.320  28.811  51.831  1.00 37.52           C  
-ATOM   1382  CD  GLN A 199      23.039  29.226  50.533  1.00 39.95           C  
-ATOM   1383  OE1 GLN A 199      24.217  28.957  50.361  1.00 41.67           O  
-ATOM   1384  NE2 GLN A 199      22.332  29.889  49.640  1.00 41.18           N  
-ATOM   1385  N   PHE A 200      21.171  31.303  54.517  1.00 38.88           N  
-ATOM   1386  CA  PHE A 200      19.894  32.016  54.762  1.00 39.75           C  
-ATOM   1387  C   PHE A 200      19.960  33.535  54.533  1.00 39.92           C  
-ATOM   1388  O   PHE A 200      19.046  34.135  53.944  1.00 40.12           O  
-ATOM   1389  CB  PHE A 200      19.345  31.740  56.189  1.00 39.56           C  
-ATOM   1390  CG  PHE A 200      17.946  32.301  56.421  1.00 41.73           C  
-ATOM   1391  CD1 PHE A 200      16.847  31.807  55.701  1.00 41.00           C  
-ATOM   1392  CD2 PHE A 200      17.735  33.341  57.316  1.00 38.98           C  
-ATOM   1393  CE1 PHE A 200      15.551  32.356  55.901  1.00 41.41           C  
-ATOM   1394  CE2 PHE A 200      16.445  33.870  57.528  1.00 40.96           C  
-ATOM   1395  CZ  PHE A 200      15.364  33.388  56.824  1.00 39.40           C  
-ATOM   1396  N   THR A 201      21.036  34.142  55.022  1.00 40.20           N  
-ATOM   1397  CA  THR A 201      21.325  35.568  54.853  1.00 40.52           C  
-ATOM   1398  C   THR A 201      21.397  35.961  53.391  1.00 41.32           C  
-ATOM   1399  O   THR A 201      20.784  36.967  53.007  1.00 41.05           O  
-ATOM   1400  CB  THR A 201      22.642  35.973  55.585  1.00 39.93           C  
-ATOM   1401  OG1 THR A 201      22.475  35.754  56.985  1.00 40.29           O  
-ATOM   1402  CG2 THR A 201      22.993  37.431  55.373  1.00 39.96           C  
-ATOM   1403  N   LYS A 202      22.155  35.188  52.604  1.00 40.94           N  
-ATOM   1404  CA  LYS A 202      22.283  35.400  51.164  1.00 42.61           C  
-ATOM   1405  C   LYS A 202      20.907  35.302  50.520  1.00 42.33           C  
-ATOM   1406  O   LYS A 202      20.484  36.214  49.799  1.00 43.16           O  
-ATOM   1407  CB  LYS A 202      23.179  34.338  50.489  1.00 41.94           C  
-ATOM   1408  CG  LYS A 202      24.574  34.083  51.085  1.00 43.78           C  
-ATOM   1409  CD  LYS A 202      25.388  33.067  50.240  1.00 44.01           C  
-ATOM   1410  CE  LYS A 202      26.264  32.118  51.096  1.00 47.04           C  
-ATOM   1411  NZ  LYS A 202      27.427  32.807  51.751  1.00 46.87           N  
-ATOM   1412  N   ASP A 203      20.237  34.180  50.778  1.00 42.33           N  
-ATOM   1413  CA  ASP A 203      18.940  33.832  50.193  1.00 42.91           C  
-ATOM   1414  C   ASP A 203      17.845  34.851  50.510  1.00 43.10           C  
-ATOM   1415  O   ASP A 203      17.209  35.375  49.598  1.00 43.77           O  
-ATOM   1416  CB  ASP A 203      18.523  32.414  50.627  1.00 42.66           C  
-ATOM   1417  CG  ASP A 203      19.333  31.327  49.914  1.00 43.96           C  
-ATOM   1418  OD1 ASP A 203      19.910  31.621  48.846  1.00 45.24           O  
-ATOM   1419  OD2 ASP A 203      19.414  30.189  50.415  1.00 44.06           O  
-ATOM   1420  N   PHE A 204      17.665  35.132  51.792  1.00 42.37           N  
-ATOM   1421  CA  PHE A 204      16.648  36.079  52.286  1.00 42.88           C  
-ATOM   1422  C   PHE A 204      16.909  37.526  51.857  1.00 42.46           C  
-ATOM   1423  O   PHE A 204      15.983  38.253  51.530  1.00 43.18           O  
-ATOM   1424  CB  PHE A 204      16.510  35.946  53.808  1.00 42.62           C  
-ATOM   1425  CG  PHE A 204      15.296  36.636  54.386  1.00 44.24           C  
-ATOM   1426  CD1 PHE A 204      14.065  36.614  53.717  1.00 45.02           C  
-ATOM   1427  CD2 PHE A 204      15.375  37.278  55.619  1.00 43.35           C  
-ATOM   1428  CE1 PHE A 204      12.943  37.264  54.252  1.00 45.15           C  
-ATOM   1429  CE2 PHE A 204      14.245  37.925  56.171  1.00 43.42           C  
-ATOM   1430  CZ  PHE A 204      13.039  37.911  55.494  1.00 43.00           C  
-ATOM   1431  N   THR A 205      18.169  37.937  51.842  1.00 42.18           N  
-ATOM   1432  CA  THR A 205      18.536  39.246  51.322  1.00 42.11           C  
-ATOM   1433  C   THR A 205      18.139  39.367  49.834  1.00 42.03           C  
-ATOM   1434  O   THR A 205      17.605  40.401  49.417  1.00 41.52           O  
-ATOM   1435  CB  THR A 205      20.046  39.517  51.498  1.00 42.02           C  
-ATOM   1436  OG1 THR A 205      20.390  39.395  52.886  1.00 42.89           O  
-ATOM   1437  CG2 THR A 205      20.420  40.938  51.009  1.00 42.72           C  
-ATOM   1438  N   THR A 206      18.443  38.334  49.051  1.00 40.52           N  
-ATOM   1439  CA  THR A 206      18.073  38.270  47.609  1.00 41.38           C  
-ATOM   1440  C   THR A 206      16.549  38.316  47.401  1.00 41.36           C  
-ATOM   1441  O   THR A 206      16.046  39.096  46.575  1.00 41.98           O  
-ATOM   1442  CB  THR A 206      18.608  36.960  46.968  1.00 40.96           C  
-ATOM   1443  OG1 THR A 206      20.032  36.957  47.031  1.00 41.86           O  
-ATOM   1444  CG2 THR A 206      18.165  36.795  45.517  1.00 42.92           C  
-ATOM   1445  N   PHE A 207      15.837  37.477  48.146  1.00 40.35           N  
-ATOM   1446  CA  PHE A 207      14.385  37.486  48.201  1.00 40.76           C  
-ATOM   1447  C   PHE A 207      13.845  38.919  48.391  1.00 40.06           C  
-ATOM   1448  O   PHE A 207      12.977  39.378  47.656  1.00 38.04           O  
-ATOM   1449  CB  PHE A 207      13.920  36.596  49.360  1.00 41.98           C  
-ATOM   1450  CG  PHE A 207      12.429  36.383  49.410  1.00 45.03           C  
-ATOM   1451  CD1 PHE A 207      11.613  37.235  50.150  1.00 46.67           C  
-ATOM   1452  CD2 PHE A 207      11.838  35.347  48.696  1.00 46.11           C  
-ATOM   1453  CE1 PHE A 207      10.230  37.072  50.176  1.00 45.78           C  
-ATOM   1454  CE2 PHE A 207      10.439  35.156  48.743  1.00 46.60           C  
-ATOM   1455  CZ  PHE A 207       9.643  36.025  49.491  1.00 46.58           C  
-ATOM   1456  N   LEU A 208      14.389  39.616  49.371  1.00 40.20           N  
-ATOM   1457  CA  LEU A 208      13.918  40.942  49.726  1.00 40.89           C  
-ATOM   1458  C   LEU A 208      14.258  41.977  48.650  1.00 42.14           C  
-ATOM   1459  O   LEU A 208      13.411  42.831  48.278  1.00 43.28           O  
-ATOM   1460  CB  LEU A 208      14.497  41.337  51.082  1.00 41.05           C  
-ATOM   1461  CG  LEU A 208      14.013  40.599  52.338  1.00 39.42           C  
-ATOM   1462  CD1 LEU A 208      14.974  40.845  53.483  1.00 35.38           C  
-ATOM   1463  CD2 LEU A 208      12.578  41.037  52.747  1.00 40.86           C  
-ATOM   1464  N   ARG A 209      15.497  41.928  48.161  1.00 42.26           N  
-ATOM   1465  CA  ARG A 209      15.940  42.874  47.143  1.00 42.93           C  
-ATOM   1466  C   ARG A 209      15.085  42.731  45.882  1.00 43.32           C  
-ATOM   1467  O   ARG A 209      14.582  43.724  45.366  1.00 43.30           O  
-ATOM   1468  CB  ARG A 209      17.418  42.700  46.808  1.00 42.94           C  
-ATOM   1469  CG  ARG A 209      17.880  43.652  45.702  1.00 45.12           C  
-ATOM   1470  CD  ARG A 209      19.298  43.359  45.232  1.00 49.00           C  
-ATOM   1471  NE  ARG A 209      19.499  41.956  44.864  1.00 49.28           N  
-ATOM   1472  CZ  ARG A 209      19.203  41.443  43.674  1.00 53.45           C  
-ATOM   1473  NH1 ARG A 209      18.677  42.204  42.714  1.00 52.95           N  
-ATOM   1474  NH2 ARG A 209      19.433  40.153  43.445  1.00 55.71           N  
-ATOM   1475  N   ILE A 210      14.901  41.493  45.431  1.00 43.41           N  
-ATOM   1476  CA  ILE A 210      14.155  41.196  44.197  1.00 44.41           C  
-ATOM   1477  C   ILE A 210      12.672  41.510  44.277  1.00 44.38           C  
-ATOM   1478  O   ILE A 210      12.116  42.169  43.376  1.00 45.57           O  
-ATOM   1479  CB  ILE A 210      14.365  39.732  43.765  1.00 44.79           C  
-ATOM   1480  CG1 ILE A 210      15.773  39.600  43.176  1.00 44.77           C  
-ATOM   1481  CG2 ILE A 210      13.268  39.286  42.779  1.00 45.66           C  
-ATOM   1482  CD1 ILE A 210      16.160  38.237  42.859  1.00 47.33           C  
-ATOM   1483  N   HIS A 211      12.027  41.067  45.345  1.00 43.08           N  
-ATOM   1484  CA  HIS A 211      10.599  41.307  45.456  1.00 43.33           C  
-ATOM   1485  C   HIS A 211      10.212  42.755  45.813  1.00 42.65           C  
-ATOM   1486  O   HIS A 211       9.152  43.217  45.406  1.00 41.95           O  
-ATOM   1487  CB  HIS A 211       9.939  40.246  46.337  1.00 43.50           C  
-ATOM   1488  CG  HIS A 211      10.155  38.849  45.811  1.00 44.60           C  
-ATOM   1489  ND1 HIS A 211       9.680  38.441  44.583  1.00 44.79           N  
-ATOM   1490  CD2 HIS A 211      10.853  37.802  46.309  1.00 45.51           C  
-ATOM   1491  CE1 HIS A 211      10.067  37.197  44.354  1.00 46.50           C  
-ATOM   1492  NE2 HIS A 211      10.777  36.783  45.389  1.00 45.50           N  
-ATOM   1493  N   SER A 212      11.059  43.460  46.553  1.00 42.45           N  
-ATOM   1494  CA  SER A 212      10.824  44.905  46.747  1.00 43.07           C  
-ATOM   1495  C   SER A 212      10.684  45.585  45.399  1.00 42.50           C  
-ATOM   1496  O   SER A 212       9.798  46.408  45.233  1.00 43.13           O  
-ATOM   1497  CB  SER A 212      11.904  45.574  47.585  1.00 43.09           C  
-ATOM   1498  OG  SER A 212      13.129  45.612  46.892  1.00 47.06           O  
-ATOM   1499  N   GLU A 213      11.537  45.228  44.434  1.00 42.70           N  
-ATOM   1500  CA  GLU A 213      11.492  45.836  43.094  1.00 43.36           C  
-ATOM   1501  C   GLU A 213      10.177  45.573  42.355  1.00 42.09           C  
-ATOM   1502  O   GLU A 213       9.739  46.408  41.569  1.00 41.45           O  
-ATOM   1503  CB  GLU A 213      12.668  45.366  42.228  1.00 43.73           C  
-ATOM   1504  CG  GLU A 213      14.048  45.743  42.758  1.00 46.82           C  
-ATOM   1505  CD  GLU A 213      15.194  45.283  41.855  0.75 46.16           C  
-ATOM   1506  OE1 GLU A 213      14.971  45.059  40.637  0.75 49.75           O  
-ATOM   1507  OE2 GLU A 213      16.334  45.169  42.366  0.75 51.07           O  
-ATOM   1508  N   GLU A 214       9.586  44.400  42.592  1.00 41.22           N  
-ATOM   1509  CA  GLU A 214       8.295  43.996  41.998  1.00 41.05           C  
-ATOM   1510  C   GLU A 214       7.071  44.715  42.586  1.00 41.33           C  
-ATOM   1511  O   GLU A 214       6.006  44.803  41.949  1.00 41.48           O  
-ATOM   1512  CB  GLU A 214       8.106  42.481  42.162  1.00 40.96           C  
-ATOM   1513  CG  GLU A 214       9.113  41.667  41.361  1.00 40.10           C  
-ATOM   1514  CD  GLU A 214       9.159  40.206  41.770  1.00 42.49           C  
-ATOM   1515  OE1 GLU A 214       8.520  39.830  42.768  1.00 44.53           O  
-ATOM   1516  OE2 GLU A 214       9.856  39.442  41.091  1.00 42.19           O  
-ATOM   1517  N   LEU A 215       7.214  45.219  43.808  1.00 40.67           N  
-ATOM   1518  CA  LEU A 215       6.115  45.871  44.495  1.00 40.73           C  
-ATOM   1519  C   LEU A 215       5.925  47.323  44.087  1.00 40.88           C  
-ATOM   1520  O   LEU A 215       6.890  48.067  43.945  1.00 40.88           O  
-ATOM   1521  CB  LEU A 215       6.337  45.810  46.011  1.00 40.78           C  
-ATOM   1522  CG  LEU A 215       6.132  44.472  46.694  1.00 39.37           C  
-ATOM   1523  CD1 LEU A 215       6.655  44.571  48.113  1.00 38.72           C  
-ATOM   1524  CD2 LEU A 215       4.649  44.094  46.682  1.00 40.00           C  
-ATOM   1525  N   ILE A 216       4.665  47.703  43.888  1.00 40.60           N  
-ATOM   1526  CA  ILE A 216       4.265  49.106  43.782  1.00 40.87           C  
-ATOM   1527  C   ILE A 216       4.626  49.806  45.079  1.00 41.34           C  
-ATOM   1528  O   ILE A 216       4.698  49.191  46.128  1.00 40.12           O  
-ATOM   1529  CB  ILE A 216       2.732  49.209  43.511  1.00 40.88           C  
-ATOM   1530  CG1 ILE A 216       2.438  48.775  42.078  1.00 40.02           C  
-ATOM   1531  CG2 ILE A 216       2.161  50.630  43.785  1.00 39.78           C  
-ATOM   1532  CD1 ILE A 216       1.080  48.088  41.897  1.00 40.52           C  
-ATOM   1533  N   SER A 217       4.853  51.111  44.992  1.00 41.75           N  
-ATOM   1534  CA  SER A 217       5.223  51.896  46.146  1.00 43.43           C  
-ATOM   1535  C   SER A 217       4.294  51.654  47.355  1.00 42.75           C  
-ATOM   1536  O   SER A 217       3.053  51.657  47.223  1.00 42.34           O  
-ATOM   1537  CB  SER A 217       5.244  53.368  45.762  1.00 42.57           C  
-ATOM   1538  OG  SER A 217       5.950  54.084  46.730  1.00 48.54           O  
-ATOM   1539  N   ARG A 218       4.923  51.427  48.512  1.00 42.52           N  
-ATOM   1540  CA  ARG A 218       4.246  51.111  49.782  1.00 41.54           C  
-ATOM   1541  C   ARG A 218       3.499  49.754  49.770  1.00 41.90           C  
-ATOM   1542  O   ARG A 218       2.702  49.456  50.673  1.00 41.70           O  
-ATOM   1543  CB  ARG A 218       3.371  52.296  50.234  1.00 42.65           C  
-ATOM   1544  CG  ARG A 218       4.187  53.559  50.531  1.00 40.05           C  
-ATOM   1545  CD  ARG A 218       3.405  54.801  50.162  1.00 46.10           C  
-ATOM   1546  N   GLY A 219       3.804  48.922  48.766  1.00 41.18           N  
-ATOM   1547  CA  GLY A 219       3.286  47.532  48.682  1.00 40.32           C  
-ATOM   1548  C   GLY A 219       3.805  46.679  49.825  1.00 40.75           C  
-ATOM   1549  O   GLY A 219       4.804  47.019  50.450  1.00 41.35           O  
-ATOM   1550  N   ARG A 220       3.144  45.562  50.125  1.00 40.84           N  
-ATOM   1551  CA  ARG A 220       3.528  44.812  51.318  1.00 41.57           C  
-ATOM   1552  C   ARG A 220       3.778  43.355  51.044  1.00 41.69           C  
-ATOM   1553  O   ARG A 220       3.308  42.822  50.044  1.00 39.56           O  
-ATOM   1554  CB  ARG A 220       2.492  44.961  52.431  1.00 41.87           C  
-ATOM   1555  CG  ARG A 220       2.313  46.369  52.918  1.00 42.09           C  
-ATOM   1556  CD  ARG A 220       1.271  46.397  53.983  1.00 43.96           C  
-ATOM   1557  NE  ARG A 220       0.994  47.761  54.432  1.00 42.54           N  
-ATOM   1558  CZ  ARG A 220       0.338  48.048  55.548  1.00 42.05           C  
-ATOM   1559  NH1 ARG A 220      -0.100  47.069  56.324  1.00 40.15           N  
-ATOM   1560  NH2 ARG A 220       0.130  49.309  55.891  1.00 39.96           N  
-ATOM   1561  N   MET A 221       4.559  42.738  51.932  1.00 42.61           N  
-ATOM   1562  CA  MET A 221       4.737  41.279  51.973  1.00 44.42           C  
-ATOM   1563  C   MET A 221       4.324  40.775  53.343  1.00 42.90           C  
-ATOM   1564  O   MET A 221       4.534  41.459  54.355  1.00 42.93           O  
-ATOM   1565  CB  MET A 221       6.189  40.839  51.689  1.00 44.53           C  
-ATOM   1566  CG  MET A 221       6.866  41.506  50.486  1.00 47.30           C  
-ATOM   1567  SD  MET A 221       8.163  40.449  49.773  1.00 49.39           S  
-ATOM   1568  CE  MET A 221       9.417  40.484  51.034  1.00 49.25           C  
-ATOM   1569  N   LEU A 222       3.717  39.591  53.373  1.00 41.61           N  
-ATOM   1570  CA  LEU A 222       3.396  38.923  54.620  1.00 40.91           C  
-ATOM   1571  C   LEU A 222       4.047  37.548  54.538  1.00 40.29           C  
-ATOM   1572  O   LEU A 222       3.669  36.761  53.692  1.00 38.86           O  
-ATOM   1573  CB  LEU A 222       1.897  38.701  54.744  1.00 41.26           C  
-ATOM   1574  CG  LEU A 222       1.185  38.535  56.102  1.00 44.56           C  
-ATOM   1575  CD1 LEU A 222       0.235  37.342  56.062  1.00 45.71           C  
-ATOM   1576  CD2 LEU A 222       2.112  38.425  57.287  1.00 43.99           C  
-ATOM   1577  N   LEU A 223       4.996  37.273  55.432  1.00 39.52           N  
-ATOM   1578  CA  LEU A 223       5.789  36.043  55.367  1.00 39.61           C  
-ATOM   1579  C   LEU A 223       5.691  35.279  56.659  1.00 39.45           C  
-ATOM   1580  O   LEU A 223       5.814  35.847  57.724  1.00 38.91           O  
-ATOM   1581  CB  LEU A 223       7.253  36.351  55.078  1.00 39.37           C  
-ATOM   1582  CG  LEU A 223       7.600  37.371  53.986  1.00 39.53           C  
-ATOM   1583  CD1 LEU A 223       9.084  37.667  54.047  1.00 41.10           C  
-ATOM   1584  CD2 LEU A 223       7.160  36.924  52.596  1.00 36.85           C  
-ATOM   1585  N   THR A 224       5.499  33.966  56.548  1.00 40.00           N  
-ATOM   1586  CA  THR A 224       5.421  33.081  57.698  1.00 39.94           C  
-ATOM   1587  C   THR A 224       6.344  31.882  57.417  1.00 40.07           C  
-ATOM   1588  O   THR A 224       6.345  31.371  56.321  1.00 39.93           O  
-ATOM   1589  CB  THR A 224       3.957  32.594  57.951  1.00 40.69           C  
-ATOM   1590  OG1 THR A 224       3.097  33.718  58.174  1.00 41.83           O  
-ATOM   1591  CG2 THR A 224       3.865  31.674  59.178  1.00 39.61           C  
-ATOM   1592  N   PHE A 225       7.206  31.528  58.363  1.00 39.94           N  
-ATOM   1593  CA  PHE A 225       8.130  30.398  58.162  1.00 40.21           C  
-ATOM   1594  C   PHE A 225       8.636  29.919  59.506  1.00 40.16           C  
-ATOM   1595  O   PHE A 225       8.318  30.514  60.537  1.00 38.90           O  
-ATOM   1596  CB  PHE A 225       9.283  30.749  57.176  1.00 40.79           C  
-ATOM   1597  CG  PHE A 225       9.960  32.059  57.469  1.00 41.25           C  
-ATOM   1598  CD1 PHE A 225      11.102  32.092  58.258  1.00 41.35           C  
-ATOM   1599  CD2 PHE A 225       9.417  33.274  57.003  1.00 42.63           C  
-ATOM   1600  CE1 PHE A 225      11.722  33.302  58.562  1.00 43.28           C  
-ATOM   1601  CE2 PHE A 225      10.027  34.468  57.266  1.00 43.03           C  
-ATOM   1602  CZ  PHE A 225      11.186  34.505  58.064  1.00 43.44           C  
-ATOM   1603  N   ILE A 226       9.363  28.805  59.504  1.00 40.58           N  
-ATOM   1604  CA  ILE A 226       9.882  28.209  60.727  1.00 42.09           C  
-ATOM   1605  C   ILE A 226      10.836  29.171  61.426  1.00 42.81           C  
-ATOM   1606  O   ILE A 226      11.658  29.784  60.774  1.00 43.58           O  
-ATOM   1607  CB  ILE A 226      10.627  26.871  60.425  1.00 42.12           C  
-ATOM   1608  CG1 ILE A 226       9.657  25.803  59.915  1.00 40.89           C  
-ATOM   1609  CG2 ILE A 226      11.357  26.348  61.668  1.00 43.17           C  
-ATOM   1610  CD1 ILE A 226      10.372  24.552  59.424  1.00 41.75           C  
-ATOM   1611  N   CYS A 227      10.730  29.303  62.746  1.00 44.18           N  
-ATOM   1612  CA  CYS A 227      11.826  29.923  63.489  1.00 45.03           C  
-ATOM   1613  C   CYS A 227      12.375  29.104  64.687  1.00 45.15           C  
-ATOM   1614  O   CYS A 227      11.763  28.151  65.163  1.00 43.98           O  
-ATOM   1615  CB  CYS A 227      11.513  31.376  63.861  1.00 45.44           C  
-ATOM   1616  SG  CYS A 227      10.488  31.550  65.290  1.00 47.77           S  
-ATOM   1617  N   LYS A 228      13.578  29.469  65.101  1.00 46.25           N  
-ATOM   1618  CA  LYS A 228      14.246  28.865  66.234  1.00 48.56           C  
-ATOM   1619  C   LYS A 228      14.212  29.888  67.353  1.00 49.85           C  
-ATOM   1620  O   LYS A 228      14.519  31.066  67.152  1.00 50.86           O  
-ATOM   1621  CB  LYS A 228      15.660  28.423  65.839  1.00 48.81           C  
-ATOM   1622  CG  LYS A 228      16.771  28.646  66.849  1.00 51.88           C  
-ATOM   1623  CD  LYS A 228      17.677  29.833  66.460  1.00 52.14           C  
-ATOM   1624  CE  LYS A 228      18.469  29.545  65.187  1.00 50.80           C  
-ATOM   1625  NZ  LYS A 228      19.596  30.508  64.964  1.00 50.50           N  
-ATOM   1626  N   GLU A 229      13.754  29.442  68.509  1.00 50.42           N  
-ATOM   1627  CA  GLU A 229      13.669  30.266  69.704  1.00 52.11           C  
-ATOM   1628  C   GLU A 229      14.591  29.665  70.752  1.00 52.38           C  
-ATOM   1629  O   GLU A 229      14.404  28.516  71.165  1.00 52.12           O  
-ATOM   1630  CB  GLU A 229      12.240  30.273  70.251  1.00 52.35           C  
-ATOM   1631  CG  GLU A 229      11.132  30.585  69.238  1.00 53.84           C  
-ATOM   1632  CD  GLU A 229       9.979  31.307  69.906  1.00 55.40           C  
-ATOM   1633  OE1 GLU A 229      10.273  32.134  70.792  1.00 57.36           O  
-ATOM   1634  OE2 GLU A 229       8.796  31.062  69.567  1.00 55.07           O  
-ATOM   1635  N   ASP A 230      15.603  30.432  71.149  1.00 53.08           N  
-ATOM   1636  CA  ASP A 230      16.547  30.020  72.198  1.00 53.58           C  
-ATOM   1637  C   ASP A 230      15.846  29.641  73.507  1.00 53.71           C  
-ATOM   1638  O   ASP A 230      16.205  28.648  74.140  1.00 53.85           O  
-ATOM   1639  N   GLU A 231      14.825  30.411  73.872  1.00 54.01           N  
-ATOM   1640  CA  GLU A 231      14.118  30.253  75.146  1.00 54.33           C  
-ATOM   1641  C   GLU A 231      13.285  28.977  75.348  1.00 54.26           C  
-ATOM   1642  O   GLU A 231      12.924  28.666  76.476  1.00 54.76           O  
-ATOM   1643  CB  GLU A 231      13.238  31.482  75.397  1.00 54.54           C  
-ATOM   1644  N   PHE A 232      12.987  28.230  74.283  1.00 54.33           N  
-ATOM   1645  CA  PHE A 232      11.967  27.163  74.393  1.00 53.64           C  
-ATOM   1646  C   PHE A 232      12.412  25.695  74.516  1.00 52.88           C  
-ATOM   1647  O   PHE A 232      12.173  25.067  75.558  1.00 53.14           O  
-ATOM   1648  CB  PHE A 232      10.892  27.341  73.311  1.00 53.78           C  
-ATOM   1649  CG  PHE A 232       9.968  28.492  73.583  1.00 53.46           C  
-ATOM   1650  CD1 PHE A 232       9.645  28.829  74.888  1.00 52.45           C  
-ATOM   1651  CD2 PHE A 232       9.419  29.227  72.544  1.00 52.97           C  
-ATOM   1652  CE1 PHE A 232       8.802  29.896  75.162  1.00 53.25           C  
-ATOM   1653  CE2 PHE A 232       8.564  30.299  72.805  1.00 52.81           C  
-ATOM   1654  CZ  PHE A 232       8.259  30.631  74.115  1.00 53.86           C  
-ATOM   1655  N   ASP A 233      13.059  25.198  73.460  1.00 51.55           N  
-ATOM   1656  CA  ASP A 233      13.447  23.786  73.198  1.00 50.72           C  
-ATOM   1657  C   ASP A 233      12.368  22.892  72.530  1.00 49.36           C  
-ATOM   1658  O   ASP A 233      12.141  21.753  72.953  1.00 49.42           O  
-ATOM   1659  CB  ASP A 233      14.097  23.100  74.402  1.00 51.38           C  
-ATOM   1660  CG  ASP A 233      15.276  22.205  74.009  1.00 52.80           C  
-ATOM   1661  OD1 ASP A 233      15.656  22.176  72.818  1.00 55.22           O  
-ATOM   1662  OD2 ASP A 233      15.846  21.537  74.907  1.00 56.35           O  
-ATOM   1663  N   HIS A 234      11.724  23.414  71.486  1.00 47.38           N  
-ATOM   1664  CA  HIS A 234      10.717  22.655  70.726  1.00 45.96           C  
-ATOM   1665  C   HIS A 234      11.240  22.158  69.385  1.00 45.38           C  
-ATOM   1666  O   HIS A 234      11.532  22.977  68.490  1.00 46.14           O  
-ATOM   1667  CB  HIS A 234       9.465  23.489  70.428  1.00 45.59           C  
-ATOM   1668  CG  HIS A 234       8.915  24.218  71.609  1.00 43.30           C  
-ATOM   1669  ND1 HIS A 234       8.463  25.517  71.531  1.00 39.99           N  
-ATOM   1670  CD2 HIS A 234       8.761  23.840  72.902  1.00 42.80           C  
-ATOM   1671  CE1 HIS A 234       8.043  25.903  72.722  1.00 42.87           C  
-ATOM   1672  NE2 HIS A 234       8.213  24.905  73.570  1.00 40.89           N  
-ATOM   1673  N   PRO A 235      11.274  20.822  69.205  1.00 44.27           N  
-ATOM   1674  CA  PRO A 235      11.731  20.195  67.963  1.00 44.10           C  
-ATOM   1675  C   PRO A 235      10.813  20.530  66.797  1.00 44.23           C  
-ATOM   1676  O   PRO A 235       9.603  20.295  66.859  1.00 44.30           O  
-ATOM   1677  CB  PRO A 235      11.644  18.693  68.262  1.00 43.48           C  
-ATOM   1678  CG  PRO A 235      11.617  18.598  69.814  1.00 44.15           C  
-ATOM   1679  CD  PRO A 235      10.857  19.818  70.207  1.00 44.61           C  
-ATOM   1680  N   ASN A 236      11.399  21.075  65.738  1.00 44.10           N  
-ATOM   1681  CA  ASN A 236      10.692  21.299  64.498  1.00 43.42           C  
-ATOM   1682  C   ASN A 236      10.662  19.997  63.677  1.00 43.82           C  
-ATOM   1683  O   ASN A 236      11.215  18.982  64.108  1.00 44.52           O  
-ATOM   1684  CB  ASN A 236      11.329  22.485  63.768  1.00 43.67           C  
-ATOM   1685  CG  ASN A 236      12.826  22.318  63.549  1.00 43.43           C  
-ATOM   1686  OD1 ASN A 236      13.298  21.244  63.176  1.00 40.92           O  
-ATOM   1687  ND2 ASN A 236      13.580  23.394  63.766  1.00 41.90           N  
-ATOM   1688  N   SER A 237      10.023  20.002  62.508  1.00 44.69           N  
-ATOM   1689  CA  SER A 237       9.918  18.788  61.679  1.00 44.30           C  
-ATOM   1690  C   SER A 237      11.271  18.207  61.236  1.00 43.77           C  
-ATOM   1691  O   SER A 237      11.430  16.968  61.171  1.00 42.95           O  
-ATOM   1692  CB  SER A 237       9.021  19.051  60.460  1.00 44.00           C  
-ATOM   1693  OG  SER A 237       9.580  20.052  59.638  1.00 45.81           O  
-ATOM   1694  N   MET A 238      12.250  19.075  60.965  1.00 44.01           N  
-ATOM   1695  CA  MET A 238      13.617  18.599  60.638  1.00 44.12           C  
-ATOM   1696  C   MET A 238      14.233  17.946  61.857  1.00 44.22           C  
-ATOM   1697  O   MET A 238      14.960  16.960  61.713  1.00 44.78           O  
-ATOM   1698  CB  MET A 238      14.567  19.714  60.188  1.00 44.29           C  
-ATOM   1699  CG  MET A 238      14.149  20.514  58.975  1.00 46.19           C  
-ATOM   1700  SD  MET A 238      13.054  21.878  59.479  1.00 48.79           S  
-ATOM   1701  CE  MET A 238      14.143  23.028  60.300  1.00 45.37           C  
-ATOM   1702  N   ASP A 239      13.972  18.496  63.058  1.00 44.19           N  
-ATOM   1703  CA  ASP A 239      14.520  17.882  64.310  1.00 43.13           C  
-ATOM   1704  C   ASP A 239      13.941  16.488  64.536  1.00 43.22           C  
-ATOM   1705  O   ASP A 239      14.672  15.549  64.900  1.00 41.72           O  
-ATOM   1706  CB  ASP A 239      14.286  18.732  65.569  1.00 43.68           C  
-ATOM   1707  CG  ASP A 239      14.967  20.088  65.512  1.00 46.30           C  
-ATOM   1708  OD1 ASP A 239      16.135  20.197  65.054  1.00 46.99           O  
-ATOM   1709  OD2 ASP A 239      14.315  21.066  65.930  1.00 47.47           O  
-ATOM   1710  N   LEU A 240      12.632  16.341  64.325  1.00 43.38           N  
-ATOM   1711  CA  LEU A 240      11.968  15.021  64.422  1.00 43.20           C  
-ATOM   1712  C   LEU A 240      12.565  14.044  63.419  1.00 43.40           C  
-ATOM   1713  O   LEU A 240      12.819  12.850  63.742  1.00 43.71           O  
-ATOM   1714  CB  LEU A 240      10.457  15.152  64.174  1.00 43.84           C  
-ATOM   1715  CG  LEU A 240       9.621  15.916  65.208  1.00 44.51           C  
-ATOM   1716  CD1 LEU A 240       8.177  16.149  64.746  1.00 44.79           C  
-ATOM   1717  CD2 LEU A 240       9.686  15.145  66.536  1.00 41.76           C  
-ATOM   1718  N   LEU A 241      12.805  14.538  62.203  1.00 43.16           N  
-ATOM   1719  CA  LEU A 241      13.431  13.729  61.171  1.00 43.15           C  
-ATOM   1720  C   LEU A 241      14.838  13.327  61.603  1.00 43.58           C  
-ATOM   1721  O   LEU A 241      15.187  12.166  61.510  1.00 42.53           O  
-ATOM   1722  CB  LEU A 241      13.451  14.473  59.822  1.00 43.41           C  
-ATOM   1723  CG  LEU A 241      13.972  13.789  58.566  1.00 43.79           C  
-ATOM   1724  CD1 LEU A 241      13.312  12.433  58.359  1.00 42.01           C  
-ATOM   1725  CD2 LEU A 241      13.814  14.726  57.327  1.00 41.35           C  
-ATOM   1726  N   GLU A 242      15.633  14.299  62.055  1.00 44.03           N  
-ATOM   1727  CA  GLU A 242      17.039  14.056  62.428  1.00 45.50           C  
-ATOM   1728  C   GLU A 242      17.151  12.991  63.522  1.00 46.41           C  
-ATOM   1729  O   GLU A 242      17.953  12.056  63.415  1.00 46.05           O  
-ATOM   1730  CB  GLU A 242      17.709  15.366  62.861  1.00 45.98           C  
-ATOM   1731  CG  GLU A 242      19.235  15.339  63.039  1.00 45.85           C  
-ATOM   1732  CD  GLU A 242      19.792  16.725  63.292  1.00 46.93           C  
-ATOM   1733  OE1 GLU A 242      19.865  17.517  62.326  1.00 47.36           O  
-ATOM   1734  OE2 GLU A 242      20.151  17.042  64.453  1.00 49.59           O  
-ATOM   1735  N   MET A 243      16.325  13.116  64.561  1.00 46.81           N  
-ATOM   1736  CA  MET A 243      16.372  12.167  65.660  1.00 47.81           C  
-ATOM   1737  C   MET A 243      15.933  10.766  65.225  1.00 46.00           C  
-ATOM   1738  O   MET A 243      16.426   9.784  65.747  1.00 45.20           O  
-ATOM   1739  CB  MET A 243      15.602  12.677  66.891  1.00 47.22           C  
-ATOM   1740  CG  MET A 243      14.108  12.880  66.749  1.00 49.65           C  
-ATOM   1741  SD  MET A 243      13.357  13.327  68.346  1.00 53.89           S  
-ATOM   1742  CE  MET A 243      13.266  15.102  68.223  1.00 52.26           C  
-ATOM   1743  N   SER A 244      15.037  10.697  64.241  1.00 44.87           N  
-ATOM   1744  CA  SER A 244      14.510   9.428  63.741  1.00 44.18           C  
-ATOM   1745  C   SER A 244      15.501   8.692  62.801  1.00 43.74           C  
-ATOM   1746  O   SER A 244      15.610   7.466  62.844  1.00 42.85           O  
-ATOM   1747  CB  SER A 244      13.171   9.682  63.060  1.00 44.05           C  
-ATOM   1748  OG  SER A 244      12.290  10.300  63.993  1.00 45.10           O  
-ATOM   1749  N   ILE A 245      16.208   9.451  61.957  1.00 42.77           N  
-ATOM   1750  CA  ILE A 245      17.344   8.891  61.204  1.00 42.87           C  
-ATOM   1751  C   ILE A 245      18.446   8.400  62.159  1.00 42.92           C  
-ATOM   1752  O   ILE A 245      18.993   7.309  61.972  1.00 42.69           O  
-ATOM   1753  CB  ILE A 245      17.917   9.895  60.195  1.00 42.50           C  
-ATOM   1754  CG1 ILE A 245      16.833  10.307  59.186  1.00 40.85           C  
-ATOM   1755  CG2 ILE A 245      19.143   9.285  59.504  1.00 42.86           C  
-ATOM   1756  CD1 ILE A 245      17.211  11.445  58.245  1.00 42.04           C  
-ATOM   1757  N   ASN A 246      18.748   9.191  63.189  1.00 43.10           N  
-ATOM   1758  CA  ASN A 246      19.686   8.742  64.246  1.00 44.20           C  
-ATOM   1759  C   ASN A 246      19.303   7.440  64.918  1.00 44.13           C  
-ATOM   1760  O   ASN A 246      20.168   6.624  65.176  1.00 44.61           O  
-ATOM   1761  CB  ASN A 246      19.898   9.805  65.319  1.00 44.48           C  
-ATOM   1762  CG  ASN A 246      21.089  10.680  65.032  1.00 46.03           C  
-ATOM   1763  OD1 ASN A 246      22.244  10.251  65.166  1.00 45.67           O  
-ATOM   1764  ND2 ASN A 246      20.819  11.926  64.634  1.00 47.18           N  
-ATOM   1765  N   ASP A 247      18.020   7.256  65.228  1.00 44.73           N  
-ATOM   1766  CA  ASP A 247      17.542   5.994  65.815  1.00 44.98           C  
-ATOM   1767  C   ASP A 247      17.971   4.834  64.929  1.00 44.95           C  
-ATOM   1768  O   ASP A 247      18.518   3.844  65.415  1.00 44.98           O  
-ATOM   1769  CB  ASP A 247      16.002   5.984  65.962  1.00 45.60           C  
-ATOM   1770  CG  ASP A 247      15.470   7.068  66.912  1.00 46.11           C  
-ATOM   1771  OD1 ASP A 247      16.212   7.517  67.820  1.00 48.39           O  
-ATOM   1772  OD2 ASP A 247      14.289   7.460  66.759  1.00 45.43           O  
-ATOM   1773  N   LEU A 248      17.746   4.988  63.622  1.00 44.73           N  
-ATOM   1774  CA  LEU A 248      17.998   3.935  62.640  1.00 44.07           C  
-ATOM   1775  C   LEU A 248      19.469   3.530  62.469  1.00 44.35           C  
-ATOM   1776  O   LEU A 248      19.765   2.358  62.187  1.00 43.75           O  
-ATOM   1777  CB  LEU A 248      17.358   4.284  61.288  1.00 44.17           C  
-ATOM   1778  CG  LEU A 248      15.818   4.309  61.219  1.00 44.10           C  
-ATOM   1779  CD1 LEU A 248      15.325   4.704  59.829  1.00 44.64           C  
-ATOM   1780  CD2 LEU A 248      15.214   2.950  61.624  1.00 44.68           C  
-ATOM   1781  N   VAL A 249      20.386   4.478  62.636  1.00 44.50           N  
-ATOM   1782  CA  VAL A 249      21.799   4.137  62.585  1.00 44.94           C  
-ATOM   1783  C   VAL A 249      22.198   3.405  63.874  1.00 45.53           C  
-ATOM   1784  O   VAL A 249      22.838   2.374  63.809  1.00 45.08           O  
-ATOM   1785  CB  VAL A 249      22.756   5.326  62.227  1.00 45.05           C  
-ATOM   1786  CG1 VAL A 249      22.115   6.286  61.226  1.00 43.46           C  
-ATOM   1787  CG2 VAL A 249      23.263   6.055  63.454  1.00 46.64           C  
-ATOM   1788  N   ILE A 250      21.763   3.929  65.021  1.00 46.13           N  
-ATOM   1789  CA  ILE A 250      21.968   3.302  66.336  1.00 46.53           C  
-ATOM   1790  C   ILE A 250      21.412   1.871  66.363  1.00 47.08           C  
-ATOM   1791  O   ILE A 250      22.049   0.952  66.896  1.00 46.88           O  
-ATOM   1792  CB  ILE A 250      21.317   4.171  67.452  1.00 46.57           C  
-ATOM   1793  CG1 ILE A 250      22.123   5.460  67.670  1.00 46.21           C  
-ATOM   1794  CG2 ILE A 250      21.183   3.396  68.748  1.00 47.33           C  
-ATOM   1795  CD1 ILE A 250      21.329   6.588  68.308  1.00 48.40           C  
-ATOM   1796  N   GLU A 251      20.239   1.689  65.760  1.00 47.70           N  
-ATOM   1797  CA  GLU A 251      19.582   0.378  65.687  1.00 48.12           C  
-ATOM   1798  C   GLU A 251      20.281  -0.573  64.706  1.00 48.15           C  
-ATOM   1799  O   GLU A 251      20.176  -1.800  64.835  1.00 48.63           O  
-ATOM   1800  CB  GLU A 251      18.106   0.548  65.310  1.00 48.06           C  
-ATOM   1801  CG  GLU A 251      17.193  -0.561  65.838  1.00 48.50           C  
-ATOM   1802  CD  GLU A 251      15.703  -0.253  65.678  1.00 48.64           C  
-ATOM   1803  OE1 GLU A 251      15.340   0.900  65.333  1.00 47.71           O  
-ATOM   1804  OE2 GLU A 251      14.891  -1.184  65.897  1.00 48.12           O  
-ATOM   1805  N   GLY A 252      20.989  -0.002  63.732  1.00 48.23           N  
-ATOM   1806  CA  GLY A 252      21.770  -0.776  62.765  1.00 48.58           C  
-ATOM   1807  C   GLY A 252      21.169  -0.832  61.370  1.00 48.79           C  
-ATOM   1808  O   GLY A 252      21.758  -1.433  60.461  1.00 49.04           O  
-ATOM   1809  N   HIS A 253      20.002  -0.212  61.201  1.00 48.70           N  
-ATOM   1810  CA  HIS A 253      19.250  -0.264  59.940  1.00 49.30           C  
-ATOM   1811  C   HIS A 253      19.862   0.581  58.823  1.00 49.20           C  
-ATOM   1812  O   HIS A 253      19.577   0.372  57.636  1.00 49.59           O  
-ATOM   1813  CB  HIS A 253      17.786   0.146  60.152  1.00 49.18           C  
-ATOM   1814  CG  HIS A 253      17.042  -0.731  61.110  1.00 50.84           C  
-ATOM   1815  ND1 HIS A 253      16.855  -2.081  60.896  1.00 53.05           N  
-ATOM   1816  CD2 HIS A 253      16.430  -0.451  62.284  1.00 52.62           C  
-ATOM   1817  CE1 HIS A 253      16.173  -2.597  61.902  1.00 53.40           C  
-ATOM   1818  NE2 HIS A 253      15.902  -1.629  62.759  1.00 53.32           N  
-ATOM   1819  N   LEU A 254      20.708   1.530  59.213  1.00 48.89           N  
-ATOM   1820  CA  LEU A 254      21.277   2.504  58.297  1.00 48.29           C  
-ATOM   1821  C   LEU A 254      22.726   2.750  58.693  1.00 48.16           C  
-ATOM   1822  O   LEU A 254      23.034   2.845  59.879  1.00 47.60           O  
-ATOM   1823  CB  LEU A 254      20.458   3.794  58.383  1.00 48.56           C  
-ATOM   1824  CG  LEU A 254      20.271   4.728  57.191  1.00 48.71           C  
-ATOM   1825  CD1 LEU A 254      19.974   3.974  55.888  1.00 48.62           C  
-ATOM   1826  CD2 LEU A 254      19.154   5.669  57.522  1.00 48.68           C  
-ATOM   1827  N   GLU A 255      23.620   2.819  57.709  1.00 48.37           N  
-ATOM   1828  CA  GLU A 255      25.030   3.063  57.992  1.00 48.69           C  
-ATOM   1829  C   GLU A 255      25.175   4.527  58.366  1.00 48.56           C  
-ATOM   1830  O   GLU A 255      24.464   5.380  57.834  1.00 48.40           O  
-ATOM   1831  CB  GLU A 255      25.919   2.693  56.797  1.00 49.05           C  
-ATOM   1832  CG  GLU A 255      27.307   2.148  57.168  1.00 50.37           C  
-ATOM   1833  CD  GLU A 255      28.463   3.078  56.787  0.75 51.39           C  
-ATOM   1834  OE1 GLU A 255      29.167   2.760  55.800  0.75 50.44           O  
-ATOM   1835  OE2 GLU A 255      28.680   4.110  57.470  0.75 50.06           O  
-ATOM   1836  N   GLU A 256      26.061   4.794  59.319  1.00 48.63           N  
-ATOM   1837  CA  GLU A 256      26.331   6.141  59.797  1.00 48.93           C  
-ATOM   1838  C   GLU A 256      26.725   7.078  58.646  1.00 48.85           C  
-ATOM   1839  O   GLU A 256      26.460   8.276  58.714  1.00 48.26           O  
-ATOM   1840  CB  GLU A 256      27.402   6.106  60.897  1.00 48.86           C  
-ATOM   1841  CG  GLU A 256      27.841   7.466  61.437  1.00 49.62           C  
-ATOM   1842  CD  GLU A 256      28.572   7.381  62.774  1.00 50.18           C  
-ATOM   1843  OE1 GLU A 256      29.252   6.370  63.029  1.00 50.43           O  
-ATOM   1844  OE2 GLU A 256      28.463   8.335  63.577  1.00 53.49           O  
-ATOM   1845  N   GLU A 257      27.347   6.534  57.594  1.00 48.62           N  
-ATOM   1846  CA  GLU A 257      27.731   7.358  56.445  1.00 48.90           C  
-ATOM   1847  C   GLU A 257      26.530   7.977  55.705  1.00 48.75           C  
-ATOM   1848  O   GLU A 257      26.628   9.099  55.186  1.00 48.14           O  
-ATOM   1849  CB  GLU A 257      28.643   6.610  55.475  1.00 49.09           C  
-ATOM   1850  CG  GLU A 257      29.220   7.481  54.342  1.00 50.29           C  
-ATOM   1851  CD  GLU A 257      29.838   8.794  54.831  0.50 51.56           C  
-ATOM   1852  OE1 GLU A 257      30.554   8.791  55.866  0.50 51.76           O  
-ATOM   1853  OE2 GLU A 257      29.608   9.831  54.169  0.50 50.81           O  
-ATOM   1854  N   LYS A 258      25.413   7.255  55.657  1.00 48.58           N  
-ATOM   1855  CA  LYS A 258      24.198   7.791  55.030  1.00 49.16           C  
-ATOM   1856  C   LYS A 258      23.693   9.052  55.736  1.00 48.82           C  
-ATOM   1857  O   LYS A 258      23.288  10.014  55.071  1.00 49.68           O  
-ATOM   1858  CB  LYS A 258      23.089   6.729  54.935  1.00 49.18           C  
-ATOM   1859  CG  LYS A 258      23.205   5.799  53.706  1.00 49.02           C  
-ATOM   1860  CD  LYS A 258      23.082   6.596  52.406  1.00 48.65           C  
-ATOM   1861  CE  LYS A 258      22.523   5.771  51.223  1.00 49.08           C  
-ATOM   1862  NZ  LYS A 258      23.042   4.407  51.111  1.00 44.33           N  
-ATOM   1863  N   LEU A 259      23.735   9.041  57.071  1.00 48.25           N  
-ATOM   1864  CA  LEU A 259      23.308  10.171  57.894  1.00 48.32           C  
-ATOM   1865  C   LEU A 259      24.323  11.309  57.813  1.00 48.06           C  
-ATOM   1866  O   LEU A 259      23.942  12.459  57.662  1.00 48.49           O  
-ATOM   1867  CB  LEU A 259      23.164   9.739  59.358  1.00 48.28           C  
-ATOM   1868  CG  LEU A 259      22.216  10.410  60.355  1.00 48.57           C  
-ATOM   1869  CD1 LEU A 259      22.723  10.206  61.796  1.00 47.31           C  
-ATOM   1870  CD2 LEU A 259      21.884  11.901  60.086  1.00 49.41           C  
-ATOM   1871  N   ASP A 260      25.610  10.970  57.926  1.00 47.66           N  
-ATOM   1872  CA  ASP A 260      26.697  11.944  57.815  1.00 47.15           C  
-ATOM   1873  C   ASP A 260      26.771  12.666  56.451  1.00 47.10           C  
-ATOM   1874  O   ASP A 260      27.261  13.792  56.382  1.00 47.15           O  
-ATOM   1875  CB  ASP A 260      28.042  11.280  58.122  1.00 47.64           C  
-ATOM   1876  CG  ASP A 260      28.202  10.890  59.593  1.00 47.77           C  
-ATOM   1877  OD1 ASP A 260      27.292  11.140  60.420  1.00 48.61           O  
-ATOM   1878  OD2 ASP A 260      29.269  10.331  59.917  1.00 47.36           O  
-ATOM   1879  N   SER A 261      26.300  12.022  55.380  1.00 46.56           N  
-ATOM   1880  CA  SER A 261      26.236  12.654  54.047  1.00 45.94           C  
-ATOM   1881  C   SER A 261      24.921  13.413  53.695  1.00 45.11           C  
-ATOM   1882  O   SER A 261      24.851  14.107  52.676  1.00 45.34           O  
-ATOM   1883  CB  SER A 261      26.572  11.630  52.946  1.00 46.22           C  
-ATOM   1884  OG  SER A 261      25.745  10.482  53.023  1.00 47.64           O  
-ATOM   1885  N   PHE A 262      23.889  13.252  54.511  1.00 43.61           N  
-ATOM   1886  CA  PHE A 262      22.574  13.834  54.240  1.00 42.94           C  
-ATOM   1887  C   PHE A 262      22.507  15.235  54.829  1.00 42.74           C  
-ATOM   1888  O   PHE A 262      22.635  15.409  56.044  1.00 43.56           O  
-ATOM   1889  CB  PHE A 262      21.488  12.934  54.828  1.00 42.88           C  
-ATOM   1890  CG  PHE A 262      20.064  13.350  54.509  1.00 42.84           C  
-ATOM   1891  CD1 PHE A 262      19.610  13.440  53.190  1.00 43.73           C  
-ATOM   1892  CD2 PHE A 262      19.161  13.588  55.546  1.00 44.22           C  
-ATOM   1893  CE1 PHE A 262      18.294  13.779  52.901  1.00 43.33           C  
-ATOM   1894  CE2 PHE A 262      17.826  13.942  55.278  1.00 44.47           C  
-ATOM   1895  CZ  PHE A 262      17.393  14.040  53.946  1.00 43.30           C  
-ATOM   1896  N   ASN A 263      22.331  16.234  53.979  1.00 41.37           N  
-ATOM   1897  CA  ASN A 263      22.126  17.599  54.456  1.00 41.89           C  
-ATOM   1898  C   ASN A 263      20.925  18.248  53.785  1.00 41.84           C  
-ATOM   1899  O   ASN A 263      20.839  18.269  52.570  1.00 41.87           O  
-ATOM   1900  CB  ASN A 263      23.362  18.452  54.225  1.00 42.22           C  
-ATOM   1901  CG  ASN A 263      24.536  18.019  55.088  1.00 41.30           C  
-ATOM   1902  OD1 ASN A 263      24.448  18.000  56.320  1.00 49.82           O  
-ATOM   1903  ND2 ASN A 263      25.613  17.693  54.463  1.00 42.71           N  
-ATOM   1904  N   VAL A 264      20.007  18.767  54.587  1.00 41.10           N  
-ATOM   1905  CA  VAL A 264      18.778  19.362  54.051  1.00 41.31           C  
-ATOM   1906  C   VAL A 264      18.987  20.868  53.822  1.00 40.46           C  
-ATOM   1907  O   VAL A 264      19.584  21.544  54.671  1.00 39.05           O  
-ATOM   1908  CB  VAL A 264      17.547  19.042  54.999  1.00 42.07           C  
-ATOM   1909  CG1 VAL A 264      16.252  19.608  54.440  1.00 44.60           C  
-ATOM   1910  CG2 VAL A 264      17.373  17.535  55.112  1.00 43.57           C  
-ATOM   1911  N   PRO A 265      18.520  21.393  52.663  1.00 39.76           N  
-ATOM   1912  CA  PRO A 265      18.643  22.818  52.388  1.00 39.30           C  
-ATOM   1913  C   PRO A 265      17.569  23.643  53.132  1.00 38.73           C  
-ATOM   1914  O   PRO A 265      16.666  24.214  52.515  1.00 38.53           O  
-ATOM   1915  CB  PRO A 265      18.490  22.885  50.858  1.00 38.12           C  
-ATOM   1916  CG  PRO A 265      17.523  21.775  50.557  1.00 39.07           C  
-ATOM   1917  CD  PRO A 265      17.920  20.660  51.516  1.00 40.54           C  
-ATOM   1918  N   ILE A 266      17.681  23.699  54.454  1.00 38.65           N  
-ATOM   1919  CA AILE A 266      16.656  24.322  55.287  0.50 38.61           C  
-ATOM   1920  CA BILE A 266      16.657  24.335  55.303  0.50 38.57           C  
-ATOM   1921  C   ILE A 266      17.317  24.993  56.501  1.00 38.88           C  
-ATOM   1922  O   ILE A 266      18.195  24.403  57.131  1.00 38.61           O  
-ATOM   1923  CB AILE A 266      15.568  23.272  55.706  0.50 38.40           C  
-ATOM   1924  CB BILE A 266      15.615  23.335  55.870  0.50 38.44           C  
-ATOM   1925  CG1AILE A 266      14.299  23.948  56.252  0.50 38.55           C  
-ATOM   1926  CG1BILE A 266      14.654  22.854  54.795  0.50 38.78           C  
-ATOM   1927  CG2AILE A 266      16.129  22.245  56.687  0.50 38.27           C  
-ATOM   1928  CG2BILE A 266      14.775  24.009  56.975  0.50 37.82           C  
-ATOM   1929  CD1AILE A 266      13.077  23.035  56.219  0.50 38.93           C  
-ATOM   1930  CD1BILE A 266      13.514  22.019  55.356  0.50 38.77           C  
-ATOM   1931  N   TYR A 267      16.913  26.226  56.794  1.00 39.15           N  
-ATOM   1932  CA  TYR A 267      17.412  26.900  57.978  1.00 39.40           C  
-ATOM   1933  C   TYR A 267      16.264  27.284  58.906  1.00 39.96           C  
-ATOM   1934  O   TYR A 267      15.164  27.605  58.454  1.00 40.91           O  
-ATOM   1935  CB  TYR A 267      18.298  28.088  57.612  1.00 39.20           C  
-ATOM   1936  CG  TYR A 267      18.932  28.764  58.791  1.00 39.78           C  
-ATOM   1937  CD1 TYR A 267      19.823  28.092  59.618  1.00 40.55           C  
-ATOM   1938  CD2 TYR A 267      18.640  30.092  59.076  1.00 40.76           C  
-ATOM   1939  CE1 TYR A 267      20.409  28.742  60.716  1.00 40.69           C  
-ATOM   1940  CE2 TYR A 267      19.216  30.746  60.138  1.00 41.51           C  
-ATOM   1941  CZ  TYR A 267      20.082  30.070  60.960  1.00 39.92           C  
-ATOM   1942  OH  TYR A 267      20.631  30.759  62.012  1.00 38.22           O  
-ATOM   1943  N   ALA A 268      16.495  27.209  60.211  1.00 39.88           N  
-ATOM   1944  CA  ALA A 268      15.537  27.778  61.167  1.00 39.95           C  
-ATOM   1945  C   ALA A 268      16.115  29.055  61.817  1.00 40.21           C  
-ATOM   1946  O   ALA A 268      16.934  28.956  62.727  1.00 39.64           O  
-ATOM   1947  CB  ALA A 268      15.175  26.742  62.218  1.00 39.68           C  
-ATOM   1948  N   PRO A 269      15.716  30.261  61.343  1.00 40.85           N  
-ATOM   1949  CA  PRO A 269      16.314  31.462  61.909  1.00 41.06           C  
-ATOM   1950  C   PRO A 269      15.686  31.918  63.220  1.00 41.83           C  
-ATOM   1951  O   PRO A 269      14.553  31.567  63.524  1.00 42.28           O  
-ATOM   1952  CB  PRO A 269      16.006  32.529  60.846  1.00 40.49           C  
-ATOM   1953  CG  PRO A 269      14.680  32.117  60.360  1.00 40.63           C  
-ATOM   1954  CD  PRO A 269      14.752  30.606  60.277  1.00 40.91           C  
-ATOM   1955  N   SER A 270      16.413  32.748  63.958  1.00 41.88           N  
-ATOM   1956  CA  SER A 270      15.845  33.435  65.108  1.00 41.97           C  
-ATOM   1957  C   SER A 270      15.174  34.706  64.579  1.00 42.02           C  
-ATOM   1958  O   SER A 270      15.427  35.123  63.439  1.00 41.75           O  
-ATOM   1959  CB  SER A 270      16.938  33.752  66.131  1.00 41.31           C  
-ATOM   1960  OG  SER A 270      17.755  34.806  65.656  1.00 40.45           O  
-ATOM   1961  N   THR A 271      14.308  35.303  65.392  1.00 43.17           N  
-ATOM   1962  CA  THR A 271      13.629  36.548  65.015  1.00 43.71           C  
-ATOM   1963  C   THR A 271      14.628  37.688  64.917  1.00 43.64           C  
-ATOM   1964  O   THR A 271      14.471  38.572  64.081  1.00 44.32           O  
-ATOM   1965  CB  THR A 271      12.487  36.933  65.996  1.00 44.30           C  
-ATOM   1966  OG1 THR A 271      13.036  37.265  67.272  1.00 46.02           O  
-ATOM   1967  CG2 THR A 271      11.495  35.787  66.164  1.00 43.73           C  
-ATOM   1968  N   GLU A 272      15.660  37.662  65.764  1.00 43.12           N  
-ATOM   1969  CA  GLU A 272      16.718  38.674  65.724  1.00 42.60           C  
-ATOM   1970  C   GLU A 272      17.520  38.613  64.419  1.00 41.48           C  
-ATOM   1971  O   GLU A 272      17.881  39.654  63.845  1.00 40.67           O  
-ATOM   1972  CB  GLU A 272      17.642  38.540  66.937  1.00 43.25           C  
-ATOM   1973  CG  GLU A 272      17.526  37.195  67.676  1.00 46.61           C  
-ATOM   1974  CD  GLU A 272      16.301  37.106  68.606  1.00 49.78           C  
-ATOM   1975  OE1 GLU A 272      16.001  38.095  69.320  0.50 49.23           O  
-ATOM   1976  OE2 GLU A 272      15.644  36.039  68.619  1.00 51.04           O  
-ATOM   1977  N   GLU A 273      17.788  37.391  63.964  1.00 40.51           N  
-ATOM   1978  CA  GLU A 273      18.419  37.127  62.663  1.00 40.44           C  
-ATOM   1979  C   GLU A 273      17.535  37.590  61.507  1.00 40.31           C  
-ATOM   1980  O   GLU A 273      18.023  38.206  60.560  1.00 40.84           O  
-ATOM   1981  CB  GLU A 273      18.733  35.633  62.495  1.00 39.90           C  
-ATOM   1982  CG  GLU A 273      19.972  35.156  63.288  1.00 40.56           C  
-ATOM   1983  CD  GLU A 273      20.010  33.647  63.507  1.00 41.06           C  
-ATOM   1984  OE1 GLU A 273      19.320  32.923  62.787  1.00 43.77           O  
-ATOM   1985  OE2 GLU A 273      20.732  33.177  64.417  1.00 45.82           O  
-ATOM   1986  N   VAL A 274      16.242  37.291  61.580  1.00 39.91           N  
-ATOM   1987  CA  VAL A 274      15.300  37.780  60.582  1.00 40.35           C  
-ATOM   1988  C   VAL A 274      15.328  39.302  60.558  1.00 40.42           C  
-ATOM   1989  O   VAL A 274      15.481  39.897  59.499  1.00 40.69           O  
-ATOM   1990  CB  VAL A 274      13.872  37.201  60.787  1.00 40.54           C  
-ATOM   1991  CG1 VAL A 274      12.854  37.861  59.851  1.00 40.67           C  
-ATOM   1992  CG2 VAL A 274      13.890  35.676  60.516  1.00 40.97           C  
-ATOM   1993  N   LYS A 275      15.240  39.914  61.738  1.00 41.30           N  
-ATOM   1994  CA  LYS A 275      15.189  41.379  61.891  1.00 41.88           C  
-ATOM   1995  C   LYS A 275      16.444  42.063  61.334  1.00 41.65           C  
-ATOM   1996  O   LYS A 275      16.344  43.041  60.585  1.00 42.10           O  
-ATOM   1997  CB  LYS A 275      14.980  41.720  63.379  1.00 41.70           C  
-ATOM   1998  CG  LYS A 275      14.508  43.131  63.687  1.00 42.93           C  
-ATOM   1999  CD  LYS A 275      14.263  43.270  65.212  1.00 43.63           C  
-ATOM   2000  CE  LYS A 275      13.324  44.421  65.523  1.00 46.09           C  
-ATOM   2001  NZ  LYS A 275      13.472  44.914  66.921  1.00 48.29           N  
-ATOM   2002  N   ARG A 276      17.625  41.562  61.704  1.00 41.77           N  
-ATOM   2003  CA  ARG A 276      18.897  42.115  61.210  1.00 41.65           C  
-ATOM   2004  C   ARG A 276      18.993  42.078  59.679  1.00 41.90           C  
-ATOM   2005  O   ARG A 276      19.398  43.065  59.046  1.00 41.51           O  
-ATOM   2006  CB  ARG A 276      20.078  41.370  61.845  1.00 41.90           C  
-ATOM   2007  CG  ARG A 276      21.441  41.633  61.217  1.00 42.04           C  
-ATOM   2008  CD  ARG A 276      22.580  41.170  62.134  1.00 42.24           C  
-ATOM   2009  N   ILE A 277      18.618  40.943  59.092  1.00 42.23           N  
-ATOM   2010  CA  ILE A 277      18.655  40.756  57.623  1.00 42.04           C  
-ATOM   2011  C   ILE A 277      17.796  41.812  56.907  1.00 42.22           C  
-ATOM   2012  O   ILE A 277      18.256  42.469  55.970  1.00 42.60           O  
-ATOM   2013  CB  ILE A 277      18.269  39.295  57.207  1.00 42.05           C  
-ATOM   2014  CG1 ILE A 277      19.306  38.304  57.741  1.00 40.92           C  
-ATOM   2015  CG2 ILE A 277      18.167  39.154  55.675  1.00 41.41           C  
-ATOM   2016  CD1 ILE A 277      18.867  36.860  57.697  1.00 41.32           C  
-ATOM   2017  N   VAL A 278      16.559  41.973  57.368  1.00 43.03           N  
-ATOM   2018  CA  VAL A 278      15.600  42.946  56.796  1.00 42.96           C  
-ATOM   2019  C   VAL A 278      16.130  44.375  56.888  1.00 43.77           C  
-ATOM   2020  O   VAL A 278      16.096  45.121  55.904  1.00 43.61           O  
-ATOM   2021  CB  VAL A 278      14.203  42.851  57.471  1.00 42.43           C  
-ATOM   2022  CG1 VAL A 278      13.286  44.018  57.056  1.00 41.88           C  
-ATOM   2023  CG2 VAL A 278      13.537  41.518  57.155  1.00 41.75           C  
-ATOM   2024  N   GLU A 279      16.642  44.738  58.064  1.00 44.66           N  
-ATOM   2025  CA  GLU A 279      17.141  46.095  58.307  1.00 45.91           C  
-ATOM   2026  C   GLU A 279      18.398  46.384  57.491  1.00 46.26           C  
-ATOM   2027  O   GLU A 279      18.602  47.509  57.027  1.00 46.48           O  
-ATOM   2028  CB  GLU A 279      17.398  46.310  59.789  1.00 46.00           C  
-ATOM   2029  CG  GLU A 279      16.122  46.348  60.622  1.00 47.49           C  
-ATOM   2030  CD  GLU A 279      16.365  46.753  62.074  1.00 47.59           C  
-ATOM   2031  OE1 GLU A 279      17.028  47.794  62.325  1.00 50.44           O  
-ATOM   2032  OE2 GLU A 279      15.876  46.026  62.968  1.00 48.89           O  
-ATOM   2033  N   GLU A 280      19.222  45.352  57.313  1.00 46.60           N  
-ATOM   2034  CA  GLU A 280      20.432  45.400  56.491  1.00 47.33           C  
-ATOM   2035  C   GLU A 280      20.112  45.634  55.006  1.00 46.81           C  
-ATOM   2036  O   GLU A 280      20.702  46.520  54.370  1.00 47.18           O  
-ATOM   2037  CB  GLU A 280      21.176  44.072  56.632  1.00 48.12           C  
-ATOM   2038  CG  GLU A 280      22.675  44.166  56.600  1.00 50.34           C  
-ATOM   2039  CD  GLU A 280      23.268  44.038  57.983  1.00 53.40           C  
-ATOM   2040  OE1 GLU A 280      23.104  44.993  58.776  1.00 54.54           O  
-ATOM   2041  OE2 GLU A 280      23.895  42.983  58.267  1.00 53.44           O  
-ATOM   2042  N   GLU A 281      19.188  44.831  54.472  1.00 46.26           N  
-ATOM   2043  CA  GLU A 281      18.687  44.940  53.087  1.00 45.41           C  
-ATOM   2044  C   GLU A 281      18.226  46.359  52.790  1.00 44.96           C  
-ATOM   2045  O   GLU A 281      18.540  46.916  51.738  1.00 44.93           O  
-ATOM   2046  CB  GLU A 281      17.524  43.957  52.856  1.00 45.84           C  
-ATOM   2047  CG  GLU A 281      16.448  44.437  51.800  1.00 45.40           C  
-ATOM   2048  CD  GLU A 281      16.968  44.334  50.403  1.00 45.99           C  
-ATOM   2049  OE1 GLU A 281      17.859  43.480  50.193  0.50 48.10           O  
-ATOM   2050  OE2 GLU A 281      16.513  45.075  49.507  1.00 45.17           O  
-ATOM   2051  N   GLY A 282      17.459  46.924  53.716  1.00 44.81           N  
-ATOM   2052  CA  GLY A 282      17.076  48.335  53.665  1.00 44.58           C  
-ATOM   2053  C   GLY A 282      15.806  48.632  52.881  1.00 44.38           C  
-ATOM   2054  O   GLY A 282      15.265  49.715  53.014  1.00 44.93           O  
-ATOM   2055  N   SER A 283      15.328  47.674  52.081  1.00 43.99           N  
-ATOM   2056  CA  SER A 283      14.155  47.873  51.200  1.00 43.11           C  
-ATOM   2057  C   SER A 283      12.821  48.009  51.921  1.00 42.99           C  
-ATOM   2058  O   SER A 283      11.952  48.771  51.465  1.00 43.72           O  
-ATOM   2059  CB  SER A 283      14.057  46.767  50.168  1.00 42.95           C  
-ATOM   2060  OG  SER A 283      15.126  46.870  49.257  1.00 42.72           O  
-ATOM   2061  N   PHE A 284      12.702  47.341  53.072  1.00 41.20           N  
-ATOM   2062  CA  PHE A 284      11.450  47.226  53.806  1.00 40.43           C  
-ATOM   2063  C   PHE A 284      11.483  47.733  55.244  1.00 40.31           C  
-ATOM   2064  O   PHE A 284      12.429  47.464  55.994  1.00 40.02           O  
-ATOM   2065  CB  PHE A 284      11.018  45.752  53.869  1.00 39.54           C  
-ATOM   2066  CG  PHE A 284      10.585  45.198  52.566  1.00 39.00           C  
-ATOM   2067  CD1 PHE A 284       9.305  45.436  52.095  1.00 39.06           C  
-ATOM   2068  CD2 PHE A 284      11.459  44.429  51.788  1.00 40.04           C  
-ATOM   2069  CE1 PHE A 284       8.883  44.930  50.881  1.00 37.38           C  
-ATOM   2070  CE2 PHE A 284      11.041  43.893  50.572  1.00 39.54           C  
-ATOM   2071  CZ  PHE A 284       9.749  44.157  50.108  1.00 39.83           C  
-ATOM   2072  N   GLU A 285      10.405  48.407  55.627  1.00 40.13           N  
-ATOM   2073  CA  GLU A 285      10.101  48.682  57.024  1.00 40.29           C  
-ATOM   2074  C   GLU A 285       9.335  47.493  57.619  1.00 39.75           C  
-ATOM   2075  O   GLU A 285       8.468  46.939  56.971  1.00 37.79           O  
-ATOM   2076  CB  GLU A 285       9.229  49.923  57.121  1.00 40.23           C  
-ATOM   2077  CG  GLU A 285       8.747  50.202  58.510  1.00 42.09           C  
-ATOM   2078  CD  GLU A 285       7.571  51.153  58.552  1.00 44.35           C  
-ATOM   2079  OE1 GLU A 285       7.120  51.602  57.467  1.00 45.39           O  
-ATOM   2080  OE2 GLU A 285       7.106  51.442  59.680  1.00 46.51           O  
-ATOM   2081  N   ILE A 286       9.616  47.145  58.873  1.00 40.58           N  
-ATOM   2082  CA  ILE A 286       8.891  46.037  59.523  1.00 41.34           C  
-ATOM   2083  C   ILE A 286       7.668  46.642  60.200  1.00 41.35           C  
-ATOM   2084  O   ILE A 286       7.811  47.500  61.053  1.00 41.25           O  
-ATOM   2085  CB  ILE A 286       9.777  45.327  60.587  1.00 41.65           C  
-ATOM   2086  CG1 ILE A 286      11.040  44.759  59.935  1.00 41.78           C  
-ATOM   2087  CG2 ILE A 286       8.978  44.284  61.386  1.00 42.04           C  
-ATOM   2088  CD1 ILE A 286      12.025  44.083  60.921  1.00 41.73           C  
-ATOM   2089  N   LEU A 287       6.471  46.216  59.799  1.00 41.56           N  
-ATOM   2090  CA  LEU A 287       5.219  46.683  60.440  1.00 41.38           C  
-ATOM   2091  C   LEU A 287       4.842  45.823  61.626  1.00 41.72           C  
-ATOM   2092  O   LEU A 287       4.277  46.314  62.598  1.00 41.79           O  
-ATOM   2093  CB  LEU A 287       4.044  46.636  59.452  1.00 41.22           C  
-ATOM   2094  CG  LEU A 287       4.342  47.070  58.016  1.00 41.99           C  
-ATOM   2095  CD1 LEU A 287       3.365  46.500  56.988  1.00 44.17           C  
-ATOM   2096  CD2 LEU A 287       4.367  48.555  57.966  1.00 36.16           C  
-ATOM   2097  N   TYR A 288       5.153  44.534  61.518  1.00 42.22           N  
-ATOM   2098  CA  TYR A 288       4.681  43.494  62.425  1.00 42.58           C  
-ATOM   2099  C   TYR A 288       5.720  42.364  62.451  1.00 41.93           C  
-ATOM   2100  O   TYR A 288       6.243  41.995  61.413  1.00 41.28           O  
-ATOM   2101  CB  TYR A 288       3.329  42.960  61.925  1.00 44.08           C  
-ATOM   2102  CG  TYR A 288       2.609  41.978  62.843  1.00 45.27           C  
-ATOM   2103  CD1 TYR A 288       1.750  42.426  63.848  1.00 46.82           C  
-ATOM   2104  CD2 TYR A 288       2.765  40.606  62.677  1.00 46.43           C  
-ATOM   2105  CE1 TYR A 288       1.078  41.512  64.693  1.00 48.33           C  
-ATOM   2106  CE2 TYR A 288       2.115  39.691  63.502  1.00 47.26           C  
-ATOM   2107  CZ  TYR A 288       1.279  40.136  64.501  1.00 48.62           C  
-ATOM   2108  OH  TYR A 288       0.638  39.201  65.307  1.00 48.62           O  
-ATOM   2109  N   LEU A 289       6.030  41.833  63.623  1.00 41.62           N  
-ATOM   2110  CA  LEU A 289       6.901  40.682  63.779  1.00 41.88           C  
-ATOM   2111  C   LEU A 289       6.629  39.934  65.043  1.00 41.75           C  
-ATOM   2112  O   LEU A 289       6.934  40.396  66.079  1.00 42.00           O  
-ATOM   2113  CB  LEU A 289       8.364  41.090  63.700  1.00 42.05           C  
-ATOM   2114  CG  LEU A 289       9.543  40.180  64.029  1.00 42.26           C  
-ATOM   2115  CD1 LEU A 289       9.536  38.935  63.282  1.00 42.14           C  
-ATOM   2116  CD2 LEU A 289      10.841  40.848  63.886  1.00 42.43           C  
-ATOM   2117  N   GLU A 290       6.067  38.757  64.932  1.00 41.66           N  
-ATOM   2118  CA AGLU A 290       5.731  37.921  66.090  0.50 41.78           C  
-ATOM   2119  CA BGLU A 290       5.734  37.923  66.089  0.50 41.94           C  
-ATOM   2120  C   GLU A 290       6.128  36.471  65.826  1.00 42.09           C  
-ATOM   2121  O   GLU A 290       6.358  36.076  64.679  1.00 41.55           O  
-ATOM   2122  CB AGLU A 290       4.234  38.006  66.426  0.50 41.89           C  
-ATOM   2123  CB BGLU A 290       4.237  38.006  66.400  0.50 42.27           C  
-ATOM   2124  CG AGLU A 290       3.346  37.030  65.645  0.50 41.63           C  
-ATOM   2125  CG BGLU A 290       3.758  39.341  66.958  0.50 43.20           C  
-ATOM   2126  CD AGLU A 290       2.028  36.692  66.340  0.50 42.21           C  
-ATOM   2127  CD BGLU A 290       3.898  39.445  68.468  0.50 45.79           C  
-ATOM   2128  OE1AGLU A 290       2.025  36.526  67.584  0.50 40.84           O  
-ATOM   2129  OE1BGLU A 290       2.913  39.137  69.176  0.50 45.77           O  
-ATOM   2130  OE2AGLU A 290       0.996  36.574  65.632  0.50 41.98           O  
-ATOM   2131  OE2BGLU A 290       4.995  39.820  68.950  0.50 47.26           O  
-ATOM   2132  N   THR A 291       6.226  35.685  66.893  1.00 41.71           N  
-ATOM   2133  CA  THR A 291       6.398  34.243  66.750  1.00 42.08           C  
-ATOM   2134  C   THR A 291       5.118  33.652  67.320  1.00 41.51           C  
-ATOM   2135  O   THR A 291       4.366  34.349  67.978  1.00 41.20           O  
-ATOM   2136  CB  THR A 291       7.619  33.707  67.513  1.00 41.49           C  
-ATOM   2137  OG1 THR A 291       7.499  34.028  68.897  1.00 43.29           O  
-ATOM   2138  CG2 THR A 291       8.880  34.325  66.993  1.00 42.36           C  
-ATOM   2139  N   PHE A 292       4.839  32.403  66.991  1.00 41.29           N  
-ATOM   2140  CA  PHE A 292       3.737  31.670  67.576  1.00 41.28           C  
-ATOM   2141  C   PHE A 292       4.122  30.212  67.533  1.00 41.34           C  
-ATOM   2142  O   PHE A 292       4.962  29.804  66.722  1.00 40.37           O  
-ATOM   2143  CB  PHE A 292       2.409  31.920  66.849  1.00 42.20           C  
-ATOM   2144  CG  PHE A 292       2.371  31.459  65.393  1.00 43.76           C  
-ATOM   2145  CD1 PHE A 292       1.997  30.151  65.055  1.00 44.52           C  
-ATOM   2146  CD2 PHE A 292       2.632  32.359  64.362  1.00 45.48           C  
-ATOM   2147  CE1 PHE A 292       1.924  29.749  63.716  1.00 42.97           C  
-ATOM   2148  CE2 PHE A 292       2.565  31.957  63.025  1.00 43.86           C  
-ATOM   2149  CZ  PHE A 292       2.211  30.646  62.712  1.00 44.55           C  
-ATOM   2150  N   ASN A 293       3.509  29.421  68.398  1.00 40.30           N  
-ATOM   2151  CA  ASN A 293       3.883  28.026  68.499  1.00 40.70           C  
-ATOM   2152  C   ASN A 293       2.671  27.172  68.160  1.00 40.37           C  
-ATOM   2153  O   ASN A 293       1.645  27.271  68.814  1.00 39.82           O  
-ATOM   2154  CB  ASN A 293       4.425  27.730  69.899  1.00 40.65           C  
-ATOM   2155  CG  ASN A 293       5.311  28.859  70.433  1.00 40.43           C  
-ATOM   2156  OD1 ASN A 293       4.832  29.757  71.125  1.00 38.68           O  
-ATOM   2157  ND2 ASN A 293       6.596  28.826  70.088  1.00 37.19           N  
-ATOM   2158  N   ALA A 294       2.793  26.352  67.115  1.00 39.00           N  
-ATOM   2159  CA  ALA A 294       1.680  25.545  66.635  1.00 38.13           C  
-ATOM   2160  C   ALA A 294       1.860  24.112  67.096  1.00 38.11           C  
-ATOM   2161  O   ALA A 294       2.878  23.488  66.752  1.00 38.40           O  
-ATOM   2162  CB  ALA A 294       1.623  25.615  65.084  1.00 37.75           C  
-ATOM   2163  N   PRO A 295       0.878  23.555  67.830  1.00 38.30           N  
-ATOM   2164  CA  PRO A 295       0.957  22.141  68.267  1.00 38.24           C  
-ATOM   2165  C   PRO A 295       1.103  21.201  67.060  1.00 38.32           C  
-ATOM   2166  O   PRO A 295       0.564  21.526  66.023  1.00 38.09           O  
-ATOM   2167  CB  PRO A 295      -0.384  21.898  68.980  1.00 38.18           C  
-ATOM   2168  CG  PRO A 295      -1.001  23.241  69.188  1.00 37.98           C  
-ATOM   2169  CD  PRO A 295      -0.365  24.220  68.272  1.00 38.46           C  
-ATOM   2170  N   TYR A 296       1.815  20.061  67.189  1.00 39.34           N  
-ATOM   2171  CA  TYR A 296       2.086  19.170  66.029  1.00 39.54           C  
-ATOM   2172  C   TYR A 296       0.812  18.671  65.364  1.00 40.50           C  
-ATOM   2173  O   TYR A 296       0.742  18.561  64.147  1.00 40.11           O  
-ATOM   2174  CB  TYR A 296       2.906  17.915  66.389  1.00 39.48           C  
-ATOM   2175  CG  TYR A 296       4.337  18.094  66.824  1.00 38.22           C  
-ATOM   2176  CD1 TYR A 296       5.038  19.259  66.545  1.00 36.66           C  
-ATOM   2177  CD2 TYR A 296       5.011  17.052  67.484  1.00 37.39           C  
-ATOM   2178  CE1 TYR A 296       6.357  19.407  66.941  1.00 37.85           C  
-ATOM   2179  CE2 TYR A 296       6.338  17.190  67.876  1.00 36.12           C  
-ATOM   2180  CZ  TYR A 296       6.996  18.378  67.588  1.00 37.24           C  
-ATOM   2181  OH  TYR A 296       8.293  18.541  67.972  1.00 40.04           O  
-ATOM   2182  N   ASP A 297      -0.179  18.334  66.176  1.00 41.76           N  
-ATOM   2183  CA  ASP A 297      -1.394  17.681  65.692  1.00 43.59           C  
-ATOM   2184  C   ASP A 297      -2.636  18.602  65.579  1.00 44.52           C  
-ATOM   2185  O   ASP A 297      -3.762  18.117  65.633  1.00 44.76           O  
-ATOM   2186  CB  ASP A 297      -1.706  16.490  66.590  1.00 43.54           C  
-ATOM   2187  CG  ASP A 297      -1.786  16.878  68.070  1.00 45.45           C  
-ATOM   2188  OD1 ASP A 297      -1.334  17.991  68.435  1.00 47.04           O  
-ATOM   2189  OD2 ASP A 297      -2.301  16.074  68.867  1.00 45.26           O  
-ATOM   2190  N   ALA A 298      -2.418  19.910  65.405  1.00 45.96           N  
-ATOM   2191  CA  ALA A 298      -3.500  20.912  65.273  1.00 47.57           C  
-ATOM   2192  C   ALA A 298      -4.409  20.631  64.075  1.00 49.06           C  
-ATOM   2193  O   ALA A 298      -5.604  20.950  64.089  1.00 49.48           O  
-ATOM   2194  CB  ALA A 298      -2.917  22.336  65.196  1.00 46.60           C  
-ATOM   2195  N   GLY A 299      -3.836  20.025  63.041  1.00 50.97           N  
-ATOM   2196  CA  GLY A 299      -4.613  19.575  61.889  1.00 53.09           C  
-ATOM   2197  C   GLY A 299      -5.248  18.186  61.976  1.00 54.10           C  
-ATOM   2198  O   GLY A 299      -5.694  17.656  60.957  1.00 54.37           O  
-ATOM   2199  N   PHE A 300      -5.311  17.598  63.172  1.00 55.21           N  
-ATOM   2200  CA  PHE A 300      -5.781  16.213  63.326  1.00 56.20           C  
-ATOM   2201  C   PHE A 300      -7.198  16.117  63.913  1.00 57.41           C  
-ATOM   2202  O   PHE A 300      -7.492  16.742  64.937  1.00 57.69           O  
-ATOM   2203  CB  PHE A 300      -4.799  15.415  64.197  1.00 56.11           C  
-ATOM   2204  CG  PHE A 300      -5.326  14.071  64.636  1.00 56.13           C  
-ATOM   2205  CD1 PHE A 300      -6.126  13.953  65.774  1.00 56.83           C  
-ATOM   2206  CD2 PHE A 300      -5.038  12.928  63.906  1.00 55.88           C  
-ATOM   2207  CE1 PHE A 300      -6.628  12.716  66.175  1.00 56.47           C  
-ATOM   2208  CE2 PHE A 300      -5.524  11.691  64.292  1.00 55.56           C  
-ATOM   2209  CZ  PHE A 300      -6.322  11.579  65.436  1.00 56.64           C  
-ATOM   2210  N   SER A 301      -8.057  15.304  63.295  1.00 58.50           N  
-ATOM   2211  CA  SER A 301      -9.415  15.075  63.827  1.00 59.60           C  
-ATOM   2212  C   SER A 301      -9.718  13.614  64.194  1.00 60.38           C  
-ATOM   2213  O   SER A 301      -9.182  12.678  63.592  1.00 60.56           O  
-ATOM   2214  CB  SER A 301     -10.486  15.641  62.877  1.00 59.86           C  
-ATOM   2215  OG  SER A 301     -10.459  17.067  62.849  1.00 59.51           O  
-ATOM   2216  N   ILE A 302     -10.574  13.435  65.201  1.00 61.31           N  
-ATOM   2217  CA  ILE A 302     -10.969  12.108  65.694  1.00 61.85           C  
-ATOM   2218  C   ILE A 302     -12.152  11.523  64.914  1.00 62.29           C  
-ATOM   2219  O   ILE A 302     -12.212  11.621  63.682  1.00 62.76           O  
-ATOM   2220  CB  ILE A 302     -11.317  12.129  67.208  1.00 61.98           C  
-ATOM   2221  CG1 ILE A 302     -11.947  13.481  67.600  1.00 61.94           C  
-ATOM   2222  CG2 ILE A 302     -10.073  11.789  68.044  1.00 61.97           C  
-ATOM   2223  CD1 ILE A 302     -12.540  13.543  68.997  1.00 61.86           C  
-ATOM   2224  N   SER A 312     -13.090   4.403  71.787  1.00 57.62           N  
-ATOM   2225  CA  SER A 312     -11.633   4.368  71.884  1.00 57.48           C  
-ATOM   2226  C   SER A 312     -11.156   4.476  73.339  1.00 57.41           C  
-ATOM   2227  O   SER A 312     -11.810   5.137  74.156  1.00 57.47           O  
-ATOM   2228  CB  SER A 312     -11.021   5.491  71.041  1.00 57.70           C  
-ATOM   2229  N   PRO A 313     -10.041   3.790  73.682  1.00 57.19           N  
-ATOM   2230  CA  PRO A 313      -9.335   4.046  74.944  1.00 56.86           C  
-ATOM   2231  C   PRO A 313      -8.683   5.440  74.920  1.00 56.50           C  
-ATOM   2232  O   PRO A 313      -9.405   6.442  74.922  1.00 56.56           O  
-ATOM   2233  CB  PRO A 313      -8.286   2.921  75.002  1.00 56.86           C  
-ATOM   2234  CG  PRO A 313      -8.752   1.895  74.012  1.00 56.94           C  
-ATOM   2235  CD  PRO A 313      -9.410   2.690  72.932  1.00 57.16           C  
-ATOM   2236  N   VAL A 314      -7.351   5.510  74.894  1.00 55.87           N  
-ATOM   2237  CA  VAL A 314      -6.638   6.792  74.799  1.00 55.28           C  
-ATOM   2238  C   VAL A 314      -5.220   6.588  74.279  1.00 54.74           C  
-ATOM   2239  O   VAL A 314      -4.627   7.507  73.708  1.00 54.42           O  
-ATOM   2240  CB  VAL A 314      -6.663   7.620  76.138  1.00 55.46           C  
-ATOM   2241  CG1 VAL A 314      -5.697   7.053  77.187  1.00 55.97           C  
-ATOM   2242  CG2 VAL A 314      -6.396   9.110  75.880  1.00 55.60           C  
-ATOM   2243  N   SER A 315      -4.690   5.380  74.471  1.00 54.07           N  
-ATOM   2244  CA  SER A 315      -3.425   4.983  73.852  1.00 53.40           C  
-ATOM   2245  C   SER A 315      -3.610   4.874  72.342  1.00 52.96           C  
-ATOM   2246  O   SER A 315      -2.659   5.059  71.577  1.00 52.65           O  
-ATOM   2247  CB  SER A 315      -2.941   3.650  74.413  1.00 53.47           C  
-ATOM   2248  OG  SER A 315      -3.017   3.642  75.826  1.00 53.99           O  
-ATOM   2249  N   CYS A 316      -4.843   4.569  71.932  1.00 52.41           N  
-ATOM   2250  CA  CYS A 316      -5.246   4.579  70.528  1.00 52.28           C  
-ATOM   2251  C   CYS A 316      -5.259   6.008  69.998  1.00 52.00           C  
-ATOM   2252  O   CYS A 316      -4.687   6.289  68.939  1.00 51.98           O  
-ATOM   2253  CB  CYS A 316      -6.627   3.942  70.353  1.00 52.07           C  
-ATOM   2254  SG  CYS A 316      -6.728   2.224  70.919  1.00 53.52           S  
-ATOM   2255  N   ASP A 317      -5.906   6.900  70.750  1.00 51.79           N  
-ATOM   2256  CA  ASP A 317      -5.990   8.324  70.410  1.00 51.80           C  
-ATOM   2257  C   ASP A 317      -4.607   8.922  70.159  1.00 51.47           C  
-ATOM   2258  O   ASP A 317      -4.371   9.548  69.113  1.00 51.40           O  
-ATOM   2259  CB  ASP A 317      -6.706   9.112  71.521  1.00 52.04           C  
-ATOM   2260  CG  ASP A 317      -8.185   8.752  71.655  1.00 52.97           C  
-ATOM   2261  OD1 ASP A 317      -8.674   7.881  70.899  1.00 54.12           O  
-ATOM   2262  OD2 ASP A 317      -8.862   9.350  72.526  1.00 53.41           O  
-ATOM   2263  N   GLU A 318      -3.696   8.711  71.111  1.00 51.12           N  
-ATOM   2264  CA  GLU A 318      -2.331   9.245  71.016  1.00 50.80           C  
-ATOM   2265  C   GLU A 318      -1.457   8.534  69.968  1.00 50.37           C  
-ATOM   2266  O   GLU A 318      -0.569   9.158  69.383  1.00 49.98           O  
-ATOM   2267  CB  GLU A 318      -1.658   9.315  72.398  1.00 50.99           C  
-ATOM   2268  CG  GLU A 318      -0.865   8.093  72.840  1.00 51.02           C  
-ATOM   2269  CD  GLU A 318      -0.602   8.089  74.344  0.50 51.05           C  
-ATOM   2270  OE1 GLU A 318      -0.590   9.183  74.956  0.50 50.72           O  
-ATOM   2271  OE2 GLU A 318      -0.416   6.989  74.917  0.50 51.43           O  
-ATOM   2272  N   HIS A 319      -1.718   7.243  69.730  1.00 49.93           N  
-ATOM   2273  CA  HIS A 319      -1.061   6.512  68.640  1.00 49.38           C  
-ATOM   2274  C   HIS A 319      -1.375   7.176  67.301  1.00 48.36           C  
-ATOM   2275  O   HIS A 319      -0.468   7.534  66.547  1.00 48.37           O  
-ATOM   2276  CB  HIS A 319      -1.464   5.021  68.619  1.00 49.77           C  
-ATOM   2277  CG  HIS A 319      -0.697   4.202  67.617  1.00 51.52           C  
-ATOM   2278  ND1 HIS A 319      -1.089   4.074  66.300  1.00 53.13           N  
-ATOM   2279  CD2 HIS A 319       0.452   3.493  67.735  1.00 53.21           C  
-ATOM   2280  CE1 HIS A 319      -0.220   3.315  65.654  1.00 53.86           C  
-ATOM   2281  NE2 HIS A 319       0.724   2.948  66.502  1.00 53.90           N  
-ATOM   2282  N   ALA A 320      -2.669   7.348  67.035  1.00 47.34           N  
-ATOM   2283  CA  ALA A 320      -3.174   7.959  65.804  1.00 46.13           C  
-ATOM   2284  C   ALA A 320      -2.685   9.393  65.619  1.00 45.49           C  
-ATOM   2285  O   ALA A 320      -2.336   9.782  64.507  1.00 45.54           O  
-ATOM   2286  CB  ALA A 320      -4.697   7.911  65.782  1.00 46.40           C  
-ATOM   2287  N   ARG A 321      -2.662  10.175  66.702  1.00 44.35           N  
-ATOM   2288  CA  ARG A 321      -2.114  11.536  66.652  0.50 43.21           C  
-ATOM   2289  C   ARG A 321      -0.637  11.540  66.260  1.00 43.24           C  
-ATOM   2290  O   ARG A 321      -0.230  12.366  65.437  1.00 43.92           O  
-ATOM   2291  CB  ARG A 321      -2.335  12.287  67.965  0.50 42.76           C  
-ATOM   2292  CG  ARG A 321      -3.776  12.667  68.191  0.50 40.66           C  
-ATOM   2293  CD  ARG A 321      -4.019  13.306  69.555  0.50 37.72           C  
-ATOM   2294  NE  ARG A 321      -5.409  13.723  69.676  0.50 34.23           N  
-ATOM   2295  CZ  ARG A 321      -5.874  14.922  69.337  0.50 34.41           C  
-ATOM   2296  NH1 ARG A 321      -5.060  15.859  68.866  0.50 31.91           N  
-ATOM   2297  NH2 ARG A 321      -7.165  15.195  69.484  0.50 34.69           N  
-ATOM   2298  N   ALA A 322       0.140  10.605  66.814  1.00 42.90           N  
-ATOM   2299  CA  ALA A 322       1.570  10.457  66.501  1.00 42.79           C  
-ATOM   2300  C   ALA A 322       1.796   9.986  65.059  1.00 43.02           C  
-ATOM   2301  O   ALA A 322       2.755  10.404  64.406  1.00 42.20           O  
-ATOM   2302  CB  ALA A 322       2.240   9.484  67.484  1.00 42.92           C  
-ATOM   2303  N   ALA A 323       0.918   9.101  64.589  1.00 43.64           N  
-ATOM   2304  CA  ALA A 323       0.970   8.558  63.231  1.00 44.29           C  
-ATOM   2305  C   ALA A 323       0.665   9.649  62.210  1.00 44.51           C  
-ATOM   2306  O   ALA A 323       1.290   9.711  61.158  1.00 44.85           O  
-ATOM   2307  CB  ALA A 323      -0.007   7.415  63.088  1.00 44.23           C  
-ATOM   2308  N   HIS A 324      -0.302  10.503  62.534  1.00 44.78           N  
-ATOM   2309  CA  HIS A 324      -0.611  11.679  61.738  1.00 44.54           C  
-ATOM   2310  C   HIS A 324       0.607  12.593  61.605  1.00 44.50           C  
-ATOM   2311  O   HIS A 324       0.912  13.060  60.515  1.00 44.41           O  
-ATOM   2312  CB  HIS A 324      -1.818  12.425  62.335  1.00 44.45           C  
-ATOM   2313  CG  HIS A 324      -1.959  13.837  61.853  1.00 44.79           C  
-ATOM   2314  ND1 HIS A 324      -2.571  14.157  60.663  1.00 45.37           N  
-ATOM   2315  CD2 HIS A 324      -1.558  15.011  62.397  1.00 45.96           C  
-ATOM   2316  CE1 HIS A 324      -2.550  15.469  60.498  1.00 47.42           C  
-ATOM   2317  NE2 HIS A 324      -1.942  16.011  61.537  1.00 46.10           N  
-ATOM   2318  N   VAL A 325       1.304  12.836  62.713  1.00 44.53           N  
-ATOM   2319  CA  VAL A 325       2.457  13.728  62.712  1.00 44.08           C  
-ATOM   2320  C   VAL A 325       3.487  13.161  61.769  1.00 45.08           C  
-ATOM   2321  O   VAL A 325       4.010  13.897  60.925  1.00 44.54           O  
-ATOM   2322  CB  VAL A 325       3.066  13.951  64.122  1.00 44.85           C  
-ATOM   2323  CG1 VAL A 325       4.328  14.798  64.054  1.00 42.03           C  
-ATOM   2324  CG2 VAL A 325       2.041  14.574  65.063  1.00 43.30           C  
-ATOM   2325  N   ALA A 326       3.750  11.851  61.890  1.00 44.90           N  
-ATOM   2326  CA  ALA A 326       4.709  11.159  61.028  1.00 45.46           C  
-ATOM   2327  C   ALA A 326       4.347  11.243  59.541  1.00 45.45           C  
-ATOM   2328  O   ALA A 326       5.234  11.386  58.682  1.00 45.81           O  
-ATOM   2329  CB  ALA A 326       4.854   9.714  61.447  1.00 44.66           C  
-ATOM   2330  N   SER A 327       3.059  11.123  59.228  1.00 45.96           N  
-ATOM   2331  CA  SER A 327       2.595  11.316  57.840  1.00 46.75           C  
-ATOM   2332  C   SER A 327       2.869  12.719  57.322  1.00 46.61           C  
-ATOM   2333  O   SER A 327       3.303  12.885  56.184  1.00 47.12           O  
-ATOM   2334  CB  SER A 327       1.108  10.987  57.696  1.00 46.83           C  
-ATOM   2335  OG  SER A 327       0.920   9.586  57.791  1.00 47.73           O  
-ATOM   2336  N   VAL A 328       2.594  13.724  58.140  1.00 46.96           N  
-ATOM   2337  CA  VAL A 328       2.846  15.114  57.763  1.00 47.59           C  
-ATOM   2338  C   VAL A 328       4.351  15.285  57.501  1.00 48.05           C  
-ATOM   2339  O   VAL A 328       4.743  15.787  56.453  1.00 49.13           O  
-ATOM   2340  CB  VAL A 328       2.332  16.113  58.831  1.00 47.65           C  
-ATOM   2341  CG1 VAL A 328       2.868  17.524  58.591  1.00 48.61           C  
-ATOM   2342  CG2 VAL A 328       0.801  16.133  58.879  1.00 48.13           C  
-ATOM   2343  N   VAL A 329       5.187  14.826  58.430  1.00 48.68           N  
-ATOM   2344  CA  VAL A 329       6.650  14.907  58.271  1.00 48.56           C  
-ATOM   2345  C   VAL A 329       7.160  14.132  57.024  1.00 48.89           C  
-ATOM   2346  O   VAL A 329       8.024  14.625  56.275  1.00 48.86           O  
-ATOM   2347  CB  VAL A 329       7.385  14.460  59.573  1.00 48.40           C  
-ATOM   2348  CG1 VAL A 329       8.907  14.438  59.365  1.00 46.77           C  
-ATOM   2349  CG2 VAL A 329       7.012  15.398  60.745  1.00 47.28           C  
-ATOM   2350  N   ARG A 330       6.637  12.933  56.790  1.00 48.83           N  
-ATOM   2351  CA  ARG A 330       7.003  12.205  55.568  1.00 49.46           C  
-ATOM   2352  C   ARG A 330       6.570  12.978  54.307  1.00 49.39           C  
-ATOM   2353  O   ARG A 330       7.296  12.988  53.281  1.00 49.58           O  
-ATOM   2354  CB  ARG A 330       6.411  10.787  55.575  1.00 49.50           C  
-ATOM   2355  CG  ARG A 330       7.129   9.781  54.692  1.00 52.62           C  
-ATOM   2356  CD  ARG A 330       6.362   8.463  54.686  1.00 57.36           C  
-ATOM   2357  NE  ARG A 330       6.990   7.432  53.860  1.00 60.12           N  
-ATOM   2358  CZ  ARG A 330       6.368   6.735  52.909  1.00 61.54           C  
-ATOM   2359  NH1 ARG A 330       5.086   6.947  52.642  1.00 63.28           N  
-ATOM   2360  NH2 ARG A 330       7.028   5.818  52.217  1.00 62.48           N  
-ATOM   2361  N   SER A 331       5.412  13.639  54.371  1.00 48.70           N  
-ATOM   2362  CA  SER A 331       4.906  14.348  53.185  1.00 49.07           C  
-ATOM   2363  C   SER A 331       5.739  15.579  52.783  1.00 48.17           C  
-ATOM   2364  O   SER A 331       5.724  15.959  51.619  1.00 50.09           O  
-ATOM   2365  CB  SER A 331       3.427  14.703  53.304  1.00 48.78           C  
-ATOM   2366  OG  SER A 331       3.233  15.753  54.228  1.00 52.09           O  
-ATOM   2367  N   ILE A 332       6.432  16.187  53.748  1.00 47.26           N  
-ATOM   2368  CA  ILE A 332       7.335  17.320  53.526  1.00 45.45           C  
-ATOM   2369  C   ILE A 332       8.653  16.856  52.928  1.00 45.03           C  
-ATOM   2370  O   ILE A 332       9.175  17.469  51.983  1.00 44.07           O  
-ATOM   2371  CB  ILE A 332       7.632  18.064  54.863  1.00 45.40           C  
-ATOM   2372  CG1 ILE A 332       6.343  18.610  55.478  1.00 44.25           C  
-ATOM   2373  CG2 ILE A 332       8.613  19.204  54.651  1.00 44.84           C  
-ATOM   2374  CD1 ILE A 332       6.443  18.689  56.958  1.00 42.13           C  
-ATOM   2375  N   TYR A 333       9.166  15.738  53.430  1.00 44.11           N  
-ATOM   2376  CA  TYR A 333      10.529  15.327  53.091  1.00 44.53           C  
-ATOM   2377  C   TYR A 333      10.705  14.127  52.157  1.00 44.57           C  
-ATOM   2378  O   TYR A 333      11.840  13.838  51.777  1.00 44.32           O  
-ATOM   2379  CB  TYR A 333      11.370  15.136  54.380  1.00 44.15           C  
-ATOM   2380  CG  TYR A 333      11.391  16.379  55.263  1.00 44.56           C  
-ATOM   2381  CD1 TYR A 333      12.192  17.474  54.939  1.00 43.28           C  
-ATOM   2382  CD2 TYR A 333      10.619  16.445  56.445  1.00 42.24           C  
-ATOM   2383  CE1 TYR A 333      12.205  18.627  55.747  1.00 43.55           C  
-ATOM   2384  CE2 TYR A 333      10.631  17.574  57.255  1.00 41.17           C  
-ATOM   2385  CZ  TYR A 333      11.426  18.663  56.896  1.00 43.41           C  
-ATOM   2386  OH  TYR A 333      11.452  19.789  57.680  1.00 45.46           O  
-ATOM   2387  N   GLU A 334       9.626  13.440  51.759  1.00 44.71           N  
-ATOM   2388  CA  GLU A 334       9.803  12.184  51.009  1.00 45.30           C  
-ATOM   2389  C   GLU A 334      10.659  12.329  49.736  1.00 44.90           C  
-ATOM   2390  O   GLU A 334      11.586  11.554  49.544  1.00 43.82           O  
-ATOM   2391  CB  GLU A 334       8.478  11.477  50.678  1.00 46.30           C  
-ATOM   2392  CG  GLU A 334       8.709  10.075  50.098  1.00 48.05           C  
-ATOM   2393  CD  GLU A 334       7.476   9.194  50.091  1.00 51.73           C  
-ATOM   2394  OE1 GLU A 334       6.609   9.368  50.970  1.00 54.33           O  
-ATOM   2395  OE2 GLU A 334       7.397   8.297  49.214  1.00 53.60           O  
-ATOM   2396  N   PRO A 335      10.381  13.344  48.890  1.00 45.32           N  
-ATOM   2397  CA  PRO A 335      11.207  13.491  47.693  1.00 45.59           C  
-ATOM   2398  C   PRO A 335      12.718  13.505  47.992  1.00 45.92           C  
-ATOM   2399  O   PRO A 335      13.479  12.774  47.361  1.00 45.60           O  
-ATOM   2400  CB  PRO A 335      10.735  14.839  47.128  1.00 46.07           C  
-ATOM   2401  CG  PRO A 335       9.301  14.869  47.486  1.00 46.00           C  
-ATOM   2402  CD  PRO A 335       9.323  14.378  48.927  1.00 44.97           C  
-ATOM   2403  N   ILE A 336      13.142  14.305  48.966  1.00 47.08           N  
-ATOM   2404  CA  ILE A 336      14.563  14.407  49.294  1.00 47.49           C  
-ATOM   2405  C   ILE A 336      15.071  13.140  49.993  1.00 47.07           C  
-ATOM   2406  O   ILE A 336      16.144  12.638  49.662  1.00 47.93           O  
-ATOM   2407  CB  ILE A 336      14.943  15.741  50.014  1.00 48.37           C  
-ATOM   2408  CG1 ILE A 336      14.537  15.754  51.476  1.00 48.93           C  
-ATOM   2409  CG2 ILE A 336      14.372  16.959  49.247  1.00 50.12           C  
-ATOM   2410  CD1 ILE A 336      15.231  16.818  52.249  1.00 53.95           C  
-ATOM   2411  N   LEU A 337      14.263  12.580  50.889  1.00 46.19           N  
-ATOM   2412  CA  LEU A 337      14.603  11.310  51.532  1.00 45.77           C  
-ATOM   2413  C   LEU A 337      14.782  10.160  50.526  1.00 45.82           C  
-ATOM   2414  O   LEU A 337      15.741   9.374  50.647  1.00 45.85           O  
-ATOM   2415  CB  LEU A 337      13.560  10.941  52.599  1.00 45.71           C  
-ATOM   2416  CG  LEU A 337      13.480  11.800  53.862  1.00 44.59           C  
-ATOM   2417  CD1 LEU A 337      12.171  11.530  54.667  1.00 42.99           C  
-ATOM   2418  CD2 LEU A 337      14.714  11.574  54.725  1.00 44.35           C  
-ATOM   2419  N   ALA A 338      13.879  10.053  49.551  1.00 45.11           N  
-ATOM   2420  CA  ALA A 338      13.968   8.991  48.540  1.00 45.11           C  
-ATOM   2421  C   ALA A 338      15.209   9.156  47.677  1.00 45.38           C  
-ATOM   2422  O   ALA A 338      15.864   8.175  47.377  1.00 45.05           O  
-ATOM   2423  CB  ALA A 338      12.738   8.933  47.682  1.00 44.83           C  
-ATOM   2424  N   SER A 339      15.559  10.390  47.306  1.00 45.57           N  
-ATOM   2425  CA  SER A 339      16.732  10.552  46.454  1.00 47.44           C  
-ATOM   2426  C   SER A 339      18.031  10.200  47.172  1.00 47.21           C  
-ATOM   2427  O   SER A 339      18.917   9.618  46.557  1.00 46.53           O  
-ATOM   2428  CB  SER A 339      16.793  11.885  45.693  1.00 46.95           C  
-ATOM   2429  OG  SER A 339      16.765  12.990  46.551  1.00 52.86           O  
-ATOM   2430  N   HIS A 340      18.118  10.508  48.469  1.00 46.87           N  
-ATOM   2431  CA  HIS A 340      19.324  10.213  49.227  1.00 47.10           C  
-ATOM   2432  C   HIS A 340      19.397   8.765  49.734  1.00 47.47           C  
-ATOM   2433  O   HIS A 340      20.405   8.078  49.538  1.00 46.62           O  
-ATOM   2434  CB  HIS A 340      19.544  11.223  50.366  1.00 47.19           C  
-ATOM   2435  CG  HIS A 340      20.872  11.068  51.044  1.00 47.74           C  
-ATOM   2436  ND1 HIS A 340      22.040  11.573  50.514  1.00 47.88           N  
-ATOM   2437  CD2 HIS A 340      21.219  10.448  52.198  1.00 47.02           C  
-ATOM   2438  CE1 HIS A 340      23.051  11.262  51.307  1.00 48.59           C  
-ATOM   2439  NE2 HIS A 340      22.578  10.582  52.338  1.00 47.96           N  
-ATOM   2440  N   PHE A 341      18.320   8.294  50.353  1.00 47.41           N  
-ATOM   2441  CA  PHE A 341      18.357   7.027  51.069  1.00 47.14           C  
-ATOM   2442  C   PHE A 341      17.816   5.824  50.296  1.00 47.39           C  
-ATOM   2443  O   PHE A 341      18.102   4.683  50.661  1.00 47.42           O  
-ATOM   2444  CB  PHE A 341      17.593   7.157  52.389  1.00 46.23           C  
-ATOM   2445  CG  PHE A 341      18.244   8.073  53.385  1.00 46.28           C  
-ATOM   2446  CD1 PHE A 341      17.807   9.388  53.518  1.00 44.75           C  
-ATOM   2447  CD2 PHE A 341      19.294   7.622  54.207  1.00 45.47           C  
-ATOM   2448  CE1 PHE A 341      18.396  10.237  54.440  1.00 45.36           C  
-ATOM   2449  CE2 PHE A 341      19.888   8.488  55.130  1.00 42.28           C  
-ATOM   2450  CZ  PHE A 341      19.439   9.791  55.235  1.00 44.20           C  
-ATOM   2451  N   GLY A 342      17.027   6.085  49.254  1.00 47.79           N  
-ATOM   2452  CA  GLY A 342      16.232   5.049  48.589  1.00 48.27           C  
-ATOM   2453  C   GLY A 342      14.919   4.830  49.324  1.00 48.90           C  
-ATOM   2454  O   GLY A 342      14.732   5.341  50.429  1.00 49.16           O  
-ATOM   2455  N   GLU A 343      14.019   4.056  48.720  1.00 49.53           N  
-ATOM   2456  CA  GLU A 343      12.662   3.849  49.256  1.00 50.27           C  
-ATOM   2457  C   GLU A 343      12.499   2.807  50.385  1.00 50.10           C  
-ATOM   2458  O   GLU A 343      11.484   2.816  51.096  1.00 50.14           O  
-ATOM   2459  CB  GLU A 343      11.683   3.530  48.113  1.00 50.52           C  
-ATOM   2460  CG  GLU A 343      10.778   4.695  47.704  1.00 51.44           C  
-ATOM   2461  CD  GLU A 343      11.276   5.476  46.498  0.50 52.71           C  
-ATOM   2462  OE1 GLU A 343      12.256   5.053  45.836  0.50 53.04           O  
-ATOM   2463  OE2 GLU A 343      10.657   6.521  46.199  0.50 53.48           O  
-ATOM   2464  N   ALA A 344      13.484   1.926  50.551  1.00 49.78           N  
-ATOM   2465  CA  ALA A 344      13.359   0.803  51.479  1.00 49.81           C  
-ATOM   2466  C   ALA A 344      13.284   1.167  52.976  1.00 49.85           C  
-ATOM   2467  O   ALA A 344      12.679   0.435  53.753  1.00 50.12           O  
-ATOM   2468  CB  ALA A 344      14.453  -0.243  51.212  1.00 49.48           C  
-ATOM   2469  N   ILE A 345      13.868   2.298  53.371  1.00 49.99           N  
-ATOM   2470  CA  ILE A 345      13.883   2.702  54.790  1.00 50.25           C  
-ATOM   2471  C   ILE A 345      12.697   3.568  55.232  1.00 49.83           C  
-ATOM   2472  O   ILE A 345      12.477   3.740  56.434  1.00 50.03           O  
-ATOM   2473  CB  ILE A 345      15.188   3.442  55.196  1.00 50.45           C  
-ATOM   2474  CG1 ILE A 345      15.518   4.560  54.201  1.00 49.84           C  
-ATOM   2475  CG2 ILE A 345      16.351   2.467  55.334  1.00 51.96           C  
-ATOM   2476  CD1 ILE A 345      15.082   5.907  54.648  1.00 51.82           C  
-ATOM   2477  N   LEU A 346      11.946   4.107  54.274  1.00 49.26           N  
-ATOM   2478  CA  LEU A 346      10.838   5.037  54.572  1.00 48.63           C  
-ATOM   2479  C   LEU A 346       9.735   4.546  55.545  1.00 48.25           C  
-ATOM   2480  O   LEU A 346       9.259   5.334  56.368  1.00 48.62           O  
-ATOM   2481  CB  LEU A 346      10.230   5.603  53.283  1.00 48.85           C  
-ATOM   2482  CG  LEU A 346      11.151   6.380  52.323  1.00 49.85           C  
-ATOM   2483  CD1 LEU A 346      10.409   6.826  51.070  1.00 49.27           C  
-ATOM   2484  CD2 LEU A 346      11.801   7.573  53.009  1.00 50.93           C  
-ATOM   2485  N   PRO A 347       9.299   3.270  55.446  1.00 48.08           N  
-ATOM   2486  CA  PRO A 347       8.383   2.769  56.486  1.00 47.87           C  
-ATOM   2487  C   PRO A 347       9.020   2.667  57.883  1.00 47.72           C  
-ATOM   2488  O   PRO A 347       8.351   2.929  58.885  1.00 47.22           O  
-ATOM   2489  CB  PRO A 347       7.997   1.372  55.981  1.00 47.20           C  
-ATOM   2490  CG  PRO A 347       8.350   1.357  54.553  1.00 47.68           C  
-ATOM   2491  CD  PRO A 347       9.529   2.252  54.405  1.00 48.28           C  
-ATOM   2492  N   ASP A 348      10.289   2.264  57.946  1.00 47.71           N  
-ATOM   2493  CA  ASP A 348      11.024   2.284  59.207  1.00 47.85           C  
-ATOM   2494  C   ASP A 348      11.171   3.717  59.700  1.00 47.16           C  
-ATOM   2495  O   ASP A 348      11.051   3.981  60.898  1.00 46.68           O  
-ATOM   2496  CB  ASP A 348      12.407   1.678  59.044  1.00 47.85           C  
-ATOM   2497  CG  ASP A 348      12.347   0.267  58.576  1.00 49.53           C  
-ATOM   2498  OD1 ASP A 348      11.907  -0.595  59.372  1.00 50.29           O  
-ATOM   2499  OD2 ASP A 348      12.720   0.028  57.407  1.00 53.00           O  
-ATOM   2500  N   LEU A 349      11.462   4.620  58.776  1.00 47.11           N  
-ATOM   2501  CA  LEU A 349      11.565   6.036  59.135  1.00 48.22           C  
-ATOM   2502  C   LEU A 349      10.242   6.541  59.696  1.00 48.23           C  
-ATOM   2503  O   LEU A 349      10.223   7.110  60.781  1.00 49.31           O  
-ATOM   2504  CB  LEU A 349      12.010   6.907  57.961  1.00 48.18           C  
-ATOM   2505  CG  LEU A 349      13.246   7.789  58.176  1.00 49.08           C  
-ATOM   2506  CD1 LEU A 349      13.328   8.803  57.058  1.00 50.06           C  
-ATOM   2507  CD2 LEU A 349      13.333   8.466  59.542  1.00 45.21           C  
-ATOM   2508  N   SER A 350       9.138   6.328  58.980  1.00 48.54           N  
-ATOM   2509  CA  SER A 350       7.816   6.756  59.492  1.00 48.98           C  
-ATOM   2510  C   SER A 350       7.527   6.194  60.884  1.00 48.60           C  
-ATOM   2511  O   SER A 350       6.909   6.860  61.710  1.00 48.96           O  
-ATOM   2512  CB  SER A 350       6.696   6.334  58.554  1.00 49.20           C  
-ATOM   2513  OG  SER A 350       6.842   6.955  57.304  1.00 51.58           O  
-ATOM   2514  N   HIS A 351       7.974   4.969  61.145  1.00 48.04           N  
-ATOM   2515  CA  HIS A 351       7.761   4.378  62.461  1.00 47.40           C  
-ATOM   2516  C   HIS A 351       8.553   5.068  63.582  1.00 46.57           C  
-ATOM   2517  O   HIS A 351       8.023   5.277  64.676  1.00 46.19           O  
-ATOM   2518  CB  HIS A 351       8.046   2.883  62.465  1.00 47.86           C  
-ATOM   2519  CG  HIS A 351       7.750   2.234  63.780  1.00 49.44           C  
-ATOM   2520  ND1 HIS A 351       8.705   2.071  64.761  1.00 52.30           N  
-ATOM   2521  CD2 HIS A 351       6.598   1.741  64.292  1.00 51.26           C  
-ATOM   2522  CE1 HIS A 351       8.161   1.481  65.810  1.00 51.95           C  
-ATOM   2523  NE2 HIS A 351       6.883   1.266  65.549  1.00 52.26           N  
-ATOM   2524  N   ARG A 352       9.812   5.406  63.320  1.00 45.17           N  
-ATOM   2525  CA  ARG A 352      10.594   6.162  64.295  1.00 44.86           C  
-ATOM   2526  C   ARG A 352      10.099   7.608  64.507  1.00 44.45           C  
-ATOM   2527  O   ARG A 352      10.163   8.127  65.626  1.00 44.36           O  
-ATOM   2528  CB  ARG A 352      12.089   6.160  63.938  1.00 45.12           C  
-ATOM   2529  CG  ARG A 352      12.835   4.833  64.132  1.00 44.63           C  
-ATOM   2530  CD  ARG A 352      12.661   4.207  65.537  1.00 47.34           C  
-ATOM   2531  NE  ARG A 352      12.667   5.205  66.615  1.00 48.38           N  
-ATOM   2532  CZ  ARG A 352      12.205   4.996  67.848  1.00 47.56           C  
-ATOM   2533  NH1 ARG A 352      11.686   3.824  68.187  1.00 48.44           N  
-ATOM   2534  NH2 ARG A 352      12.252   5.969  68.747  1.00 48.55           N  
-ATOM   2535  N   ILE A 353       9.637   8.266  63.443  1.00 43.78           N  
-ATOM   2536  CA  ILE A 353       9.119   9.634  63.584  1.00 43.40           C  
-ATOM   2537  C   ILE A 353       7.898   9.661  64.522  1.00 43.27           C  
-ATOM   2538  O   ILE A 353       7.748  10.609  65.316  1.00 43.54           O  
-ATOM   2539  CB  ILE A 353       8.769  10.321  62.226  1.00 42.82           C  
-ATOM   2540  CG1 ILE A 353       9.983  10.409  61.283  1.00 42.11           C  
-ATOM   2541  CG2 ILE A 353       8.229  11.725  62.457  1.00 42.40           C  
-ATOM   2542  CD1 ILE A 353       9.620  10.491  59.824  1.00 41.63           C  
-ATOM   2543  N   ALA A 354       7.030   8.651  64.410  1.00 42.59           N  
-ATOM   2544  CA  ALA A 354       5.823   8.556  65.240  1.00 42.64           C  
-ATOM   2545  C   ALA A 354       6.199   8.342  66.697  1.00 42.66           C  
-ATOM   2546  O   ALA A 354       5.683   9.010  67.581  1.00 42.80           O  
-ATOM   2547  CB  ALA A 354       4.884   7.427  64.741  1.00 42.18           C  
-ATOM   2548  N   LYS A 355       7.118   7.416  66.943  1.00 42.97           N  
-ATOM   2549  CA  LYS A 355       7.577   7.149  68.309  1.00 43.14           C  
-ATOM   2550  C   LYS A 355       8.178   8.400  68.946  1.00 43.35           C  
-ATOM   2551  O   LYS A 355       7.826   8.759  70.073  1.00 42.74           O  
-ATOM   2552  CB  LYS A 355       8.568   5.990  68.323  1.00 43.24           C  
-ATOM   2553  CG  LYS A 355       7.943   4.668  67.954  1.00 44.16           C  
-ATOM   2554  CD  LYS A 355       6.915   4.244  68.989  1.00 46.45           C  
-ATOM   2555  CE  LYS A 355       6.507   2.785  68.826  1.00 46.72           C  
-ATOM   2556  NZ  LYS A 355       7.353   1.831  69.621  1.00 48.32           N  
-ATOM   2557  N   ASN A 356       9.071   9.061  68.211  1.00 43.13           N  
-ATOM   2558  CA  ASN A 356       9.641  10.341  68.633  1.00 43.98           C  
-ATOM   2559  C   ASN A 356       8.613  11.464  68.844  1.00 43.98           C  
-ATOM   2560  O   ASN A 356       8.697  12.197  69.829  1.00 43.76           O  
-ATOM   2561  CB  ASN A 356      10.749  10.787  67.676  1.00 43.70           C  
-ATOM   2562  CG  ASN A 356      12.016   9.941  67.816  1.00 45.13           C  
-ATOM   2563  OD1 ASN A 356      12.445   9.629  68.922  1.00 43.37           O  
-ATOM   2564  ND2 ASN A 356      12.609   9.570  66.694  1.00 45.51           N  
-ATOM   2565  N   ALA A 357       7.659  11.579  67.917  1.00 44.08           N  
-ATOM   2566  CA  ALA A 357       6.551  12.547  68.001  1.00 43.92           C  
-ATOM   2567  C   ALA A 357       5.734  12.423  69.290  1.00 44.06           C  
-ATOM   2568  O   ALA A 357       5.423  13.419  69.942  1.00 44.24           O  
-ATOM   2569  CB  ALA A 357       5.639  12.391  66.792  1.00 43.88           C  
-ATOM   2570  N   ALA A 358       5.388  11.189  69.639  1.00 43.93           N  
-ATOM   2571  CA  ALA A 358       4.637  10.898  70.848  1.00 43.97           C  
-ATOM   2572  C   ALA A 358       5.388  11.265  72.125  1.00 43.81           C  
-ATOM   2573  O   ALA A 358       4.778  11.722  73.072  1.00 44.13           O  
-ATOM   2574  CB  ALA A 358       4.219   9.438  70.865  1.00 43.49           C  
-ATOM   2575  N   LYS A 359       6.705  11.067  72.152  1.00 43.93           N  
-ATOM   2576  CA  LYS A 359       7.494  11.350  73.367  1.00 43.41           C  
-ATOM   2577  C   LYS A 359       7.550  12.871  73.560  1.00 43.22           C  
-ATOM   2578  O   LYS A 359       7.449  13.367  74.675  1.00 42.14           O  
-ATOM   2579  CB  LYS A 359       8.915  10.772  73.247  1.00 43.02           C  
-ATOM   2580  CG  LYS A 359       9.775  10.932  74.513  1.00 44.11           C  
-ATOM   2581  N   VAL A 360       7.698  13.594  72.447  1.00 42.50           N  
-ATOM   2582  CA  VAL A 360       7.780  15.051  72.464  1.00 42.97           C  
-ATOM   2583  C   VAL A 360       6.475  15.683  72.967  1.00 42.51           C  
-ATOM   2584  O   VAL A 360       6.490  16.540  73.859  1.00 42.84           O  
-ATOM   2585  CB  VAL A 360       8.184  15.610  71.069  1.00 42.79           C  
-ATOM   2586  CG1 VAL A 360       8.335  17.117  71.134  1.00 43.68           C  
-ATOM   2587  CG2 VAL A 360       9.502  14.983  70.632  1.00 44.41           C  
-ATOM   2588  N   LEU A 361       5.352  15.228  72.419  1.00 42.81           N  
-ATOM   2589  CA  LEU A 361       4.018  15.744  72.786  1.00 42.79           C  
-ATOM   2590  C   LEU A 361       3.718  15.522  74.265  1.00 42.90           C  
-ATOM   2591  O   LEU A 361       3.189  16.405  74.954  1.00 42.38           O  
-ATOM   2592  CB  LEU A 361       2.924  15.105  71.904  1.00 42.76           C  
-ATOM   2593  CG  LEU A 361       2.749  15.531  70.436  1.00 42.65           C  
-ATOM   2594  CD1 LEU A 361       2.104  14.403  69.629  1.00 41.35           C  
-ATOM   2595  CD2 LEU A 361       1.931  16.816  70.333  1.00 42.51           C  
-ATOM   2596  N   ARG A 362       4.080  14.336  74.747  1.00 43.29           N  
-ATOM   2597  CA  ARG A 362       3.963  13.999  76.153  1.00 43.56           C  
-ATOM   2598  C   ARG A 362       4.762  14.895  77.111  1.00 43.04           C  
-ATOM   2599  O   ARG A 362       4.277  15.203  78.207  1.00 43.12           O  
-ATOM   2600  CB  ARG A 362       4.270  12.513  76.377  1.00 44.22           C  
-ATOM   2601  CG  ARG A 362       3.090  11.616  76.016  1.00 46.12           C  
-ATOM   2602  CD  ARG A 362       3.188  10.212  76.588  1.00 50.23           C  
-ATOM   2603  NE  ARG A 362       1.848   9.694  76.898  1.00 52.87           N  
-ATOM   2604  CZ  ARG A 362       1.407   9.345  78.109  1.00 54.47           C  
-ATOM   2605  NH1 ARG A 362       2.193   9.408  79.183  1.00 54.61           N  
-ATOM   2606  NH2 ARG A 362       0.162   8.903  78.243  1.00 54.96           N  
-ATOM   2607  N   SER A 363       5.953  15.332  76.695  1.00 42.48           N  
-ATOM   2608  CA  SER A 363       6.737  16.297  77.477  1.00 42.10           C  
-ATOM   2609  C   SER A 363       6.187  17.741  77.421  1.00 41.93           C  
-ATOM   2610  O   SER A 363       6.614  18.591  78.262  1.00 41.98           O  
-ATOM   2611  CB  SER A 363       8.214  16.291  77.037  1.00 42.11           C  
-ATOM   2612  OG  SER A 363       8.390  16.981  75.790  1.00 42.73           O  
-ATOM   2613  N   GLY A 364       5.254  18.013  76.453  1.00 41.03           N  
-ATOM   2614  CA  GLY A 364       4.635  19.346  76.339  1.00 40.74           C  
-ATOM   2615  C   GLY A 364       5.484  20.362  75.586  1.00 40.63           C  
-ATOM   2616  O   GLY A 364       5.372  21.582  75.818  1.00 40.13           O  
-ATOM   2617  N   LYS A 365       6.333  19.844  74.694  1.00 40.60           N  
-ATOM   2618  CA  LYS A 365       7.223  20.641  73.839  1.00 41.08           C  
-ATOM   2619  C   LYS A 365       6.981  20.347  72.351  1.00 40.64           C  
-ATOM   2620  O   LYS A 365       7.793  20.703  71.503  1.00 40.90           O  
-ATOM   2621  CB  LYS A 365       8.700  20.421  74.223  1.00 41.10           C  
-ATOM   2622  CG  LYS A 365       9.071  21.005  75.601  1.00 41.89           C  
-ATOM   2623  CD  LYS A 365      10.502  20.666  76.027  1.00 41.76           C  
-ATOM   2624  CE  LYS A 365      10.726  20.982  77.525  1.00 44.11           C  
-ATOM   2625  NZ  LYS A 365      10.906  22.454  77.787  1.00 47.32           N  
-ATOM   2626  N   GLY A 366       5.829  19.736  72.056  1.00 40.56           N  
-ATOM   2627  CA  GLY A 366       5.411  19.395  70.688  1.00 40.48           C  
-ATOM   2628  C   GLY A 366       4.758  20.497  69.890  1.00 39.44           C  
-ATOM   2629  O   GLY A 366       3.573  20.433  69.547  1.00 40.13           O  
-ATOM   2630  N   PHE A 367       5.550  21.515  69.589  1.00 38.89           N  
-ATOM   2631  CA  PHE A 367       5.103  22.670  68.849  1.00 38.87           C  
-ATOM   2632  C   PHE A 367       6.057  22.946  67.729  1.00 38.74           C  
-ATOM   2633  O   PHE A 367       7.268  22.856  67.915  1.00 38.64           O  
-ATOM   2634  CB  PHE A 367       5.075  23.913  69.742  1.00 38.50           C  
-ATOM   2635  CG  PHE A 367       4.214  23.769  70.928  1.00 38.11           C  
-ATOM   2636  CD1 PHE A 367       2.899  24.207  70.898  1.00 38.78           C  
-ATOM   2637  CD2 PHE A 367       4.706  23.187  72.092  1.00 39.30           C  
-ATOM   2638  CE1 PHE A 367       2.089  24.068  72.008  1.00 38.35           C  
-ATOM   2639  CE2 PHE A 367       3.892  23.055  73.202  1.00 39.33           C  
-ATOM   2640  CZ  PHE A 367       2.584  23.493  73.150  1.00 38.60           C  
-ATOM   2641  N   TYR A 368       5.503  23.288  66.570  1.00 39.28           N  
-ATOM   2642  CA  TYR A 368       6.281  23.899  65.507  1.00 39.89           C  
-ATOM   2643  C   TYR A 368       6.329  25.412  65.741  1.00 40.48           C  
-ATOM   2644  O   TYR A 368       5.308  26.084  65.669  1.00 40.96           O  
-ATOM   2645  CB  TYR A 368       5.635  23.642  64.151  1.00 40.17           C  
-ATOM   2646  CG  TYR A 368       5.495  22.206  63.762  1.00 39.23           C  
-ATOM   2647  CD1 TYR A 368       6.616  21.360  63.707  1.00 38.19           C  
-ATOM   2648  CD2 TYR A 368       4.248  21.689  63.413  1.00 38.46           C  
-ATOM   2649  CE1 TYR A 368       6.503  20.037  63.328  1.00 37.72           C  
-ATOM   2650  CE2 TYR A 368       4.118  20.358  63.025  1.00 38.63           C  
-ATOM   2651  CZ  TYR A 368       5.258  19.539  62.974  1.00 39.93           C  
-ATOM   2652  OH  TYR A 368       5.144  18.215  62.608  1.00 40.43           O  
-ATOM   2653  N   ASP A 369       7.521  25.940  66.005  1.00 41.06           N  
-ATOM   2654  CA  ASP A 369       7.711  27.366  66.265  1.00 40.83           C  
-ATOM   2655  C   ASP A 369       7.791  28.091  64.933  1.00 41.45           C  
-ATOM   2656  O   ASP A 369       8.541  27.663  64.038  1.00 39.00           O  
-ATOM   2657  CB  ASP A 369       9.015  27.600  67.044  1.00 41.33           C  
-ATOM   2658  CG  ASP A 369       8.984  27.030  68.466  1.00 42.81           C  
-ATOM   2659  OD1 ASP A 369       7.892  26.863  69.047  1.00 42.08           O  
-ATOM   2660  OD2 ASP A 369      10.078  26.757  69.011  1.00 45.85           O  
-ATOM   2661  N   SER A 370       7.033  29.194  64.811  1.00 40.93           N  
-ATOM   2662  CA  SER A 370       6.918  29.930  63.559  1.00 42.29           C  
-ATOM   2663  C   SER A 370       6.984  31.441  63.814  1.00 42.35           C  
-ATOM   2664  O   SER A 370       6.623  31.903  64.879  1.00 40.97           O  
-ATOM   2665  CB  SER A 370       5.586  29.592  62.903  1.00 43.25           C  
-ATOM   2666  OG  SER A 370       5.421  28.177  62.834  1.00 43.86           O  
-ATOM   2667  N   VAL A 371       7.514  32.176  62.847  1.00 42.93           N  
-ATOM   2668  CA  VAL A 371       7.550  33.622  62.883  1.00 43.35           C  
-ATOM   2669  C   VAL A 371       6.658  34.144  61.746  1.00 44.03           C  
-ATOM   2670  O   VAL A 371       6.530  33.516  60.675  1.00 44.49           O  
-ATOM   2671  CB  VAL A 371       9.011  34.163  62.753  1.00 43.11           C  
-ATOM   2672  CG1 VAL A 371       9.668  33.714  61.464  1.00 42.74           C  
-ATOM   2673  CG2 VAL A 371       9.053  35.693  62.880  1.00 44.36           C  
-ATOM   2674  N   ILE A 372       6.043  35.289  61.988  1.00 43.56           N  
-ATOM   2675  CA  ILE A 372       5.243  35.949  60.991  1.00 43.85           C  
-ATOM   2676  C   ILE A 372       5.725  37.416  60.965  1.00 43.18           C  
-ATOM   2677  O   ILE A 372       5.904  38.037  62.013  1.00 43.09           O  
-ATOM   2678  CB  ILE A 372       3.733  35.763  61.317  1.00 44.48           C  
-ATOM   2679  CG1 ILE A 372       2.833  36.502  60.324  1.00 44.43           C  
-ATOM   2680  CG2 ILE A 372       3.425  36.210  62.745  1.00 44.99           C  
-ATOM   2681  CD1 ILE A 372       1.380  36.139  60.484  1.00 43.67           C  
-ATOM   2682  N   ILE A 373       6.015  37.917  59.767  1.00 42.94           N  
-ATOM   2683  CA  ILE A 373       6.568  39.269  59.584  1.00 41.31           C  
-ATOM   2684  C   ILE A 373       5.891  40.016  58.429  1.00 41.28           C  
-ATOM   2685  O   ILE A 373       5.838  39.529  57.287  1.00 39.80           O  
-ATOM   2686  CB  ILE A 373       8.118  39.251  59.397  1.00 41.84           C  
-ATOM   2687  CG1 ILE A 373       8.690  40.675  59.404  1.00 41.53           C  
-ATOM   2688  CG2 ILE A 373       8.522  38.447  58.133  1.00 39.08           C  
-ATOM   2689  CD1 ILE A 373      10.234  40.759  59.388  1.00 41.37           C  
-ATOM   2690  N   SER A 374       5.375  41.202  58.758  1.00 40.75           N  
-ATOM   2691  CA  SER A 374       4.717  42.051  57.811  1.00 40.92           C  
-ATOM   2692  C   SER A 374       5.653  43.199  57.403  1.00 40.90           C  
-ATOM   2693  O   SER A 374       6.143  43.945  58.245  1.00 40.51           O  
-ATOM   2694  CB  SER A 374       3.437  42.602  58.445  1.00 41.10           C  
-ATOM   2695  OG  SER A 374       2.612  43.167  57.464  1.00 43.28           O  
-ATOM   2696  N   LEU A 375       5.877  43.332  56.101  1.00 40.74           N  
-ATOM   2697  CA  LEU A 375       6.825  44.287  55.541  1.00 40.20           C  
-ATOM   2698  C   LEU A 375       6.158  45.267  54.589  1.00 40.28           C  
-ATOM   2699  O   LEU A 375       5.379  44.847  53.759  1.00 41.33           O  
-ATOM   2700  CB  LEU A 375       7.887  43.500  54.756  1.00 39.15           C  
-ATOM   2701  CG  LEU A 375       8.635  42.426  55.558  1.00 39.10           C  
-ATOM   2702  CD1 LEU A 375       9.455  41.522  54.641  1.00 38.41           C  
-ATOM   2703  CD2 LEU A 375       9.505  43.103  56.683  1.00 39.13           C  
-ATOM   2704  N   ALA A 376       6.472  46.556  54.711  1.00 40.46           N  
-ATOM   2705  CA  ALA A 376       6.079  47.575  53.734  1.00 39.64           C  
-ATOM   2706  C   ALA A 376       7.295  48.133  52.997  1.00 39.53           C  
-ATOM   2707  O   ALA A 376       8.306  48.460  53.633  1.00 38.94           O  
-ATOM   2708  CB  ALA A 376       5.327  48.722  54.422  1.00 39.90           C  
-ATOM   2709  N   LYS A 377       7.178  48.271  51.676  1.00 39.76           N  
-ATOM   2710  CA  LYS A 377       8.217  48.891  50.827  1.00 40.69           C  
-ATOM   2711  C   LYS A 377       8.435  50.368  51.179  1.00 41.93           C  
-ATOM   2712  O   LYS A 377       7.488  51.165  51.156  1.00 41.62           O  
-ATOM   2713  CB  LYS A 377       7.861  48.740  49.334  1.00 40.75           C  
-ATOM   2714  CG  LYS A 377       8.960  49.165  48.352  1.00 40.45           C  
-ATOM   2715  CD  LYS A 377       8.552  49.004  46.870  1.00 41.42           C  
-ATOM   2716  CE  LYS A 377       9.578  49.661  45.933  1.00 41.84           C  
-ATOM   2717  NZ  LYS A 377       9.309  49.422  44.471  1.00 43.63           N  
-ATOM   2718  N   LYS A 378       9.676  50.718  51.516  1.00 42.70           N  
-ATOM   2719  CA  LYS A 378      10.025  52.093  51.915  1.00 44.33           C  
-ATOM   2720  C   LYS A 378       9.939  53.029  50.713  1.00 45.41           C  
-ATOM   2721  O   LYS A 378      10.229  52.612  49.581  1.00 46.36           O  
-ATOM   2722  CB  LYS A 378      11.449  52.149  52.471  1.00 43.39           C  
-ATOM   2723  CG  LYS A 378      11.655  51.558  53.847  1.00 44.56           C  
-ATOM   2724  CD  LYS A 378      13.149  51.356  54.065  1.00 45.39           C  
-ATOM   2725  CE  LYS A 378      13.515  50.958  55.487  1.00 46.24           C  
-ATOM   2726  NZ  LYS A 378      15.001  51.016  55.688  1.00 45.55           N  
-ATOM   2727  N   PRO A 379       9.552  54.298  50.939  1.00 47.29           N  
-ATOM   2728  CA  PRO A 379       9.619  55.223  49.799  1.00 48.12           C  
-ATOM   2729  C   PRO A 379      11.070  55.420  49.326  1.00 48.97           C  
-ATOM   2730  O   PRO A 379      12.031  55.003  50.001  1.00 48.80           O  
-ATOM   2731  CB  PRO A 379       9.061  56.526  50.370  1.00 48.06           C  
-ATOM   2732  CG  PRO A 379       9.250  56.415  51.854  1.00 47.92           C  
-ATOM   2733  CD  PRO A 379       9.060  54.961  52.164  1.00 46.71           C  
-TER    2734      PRO A 379                                                      
-HETATM 2735  N   SAH A 501       2.188  28.012  51.378  1.00 37.24           N  
-HETATM 2736  CA  SAH A 501       1.648  26.623  51.249  1.00 37.27           C  
-HETATM 2737  CB  SAH A 501       2.766  25.622  50.946  1.00 37.87           C  
-HETATM 2738  CG  SAH A 501       3.891  25.509  51.965  1.00 37.26           C  
-HETATM 2739  SD  SAH A 501       4.821  23.957  51.734  1.00 41.41           S  
-HETATM 2740  C   SAH A 501       0.881  26.161  52.486  1.00 37.42           C  
-HETATM 2741  O   SAH A 501       0.557  26.950  53.390  1.00 37.75           O  
-HETATM 2742  OXT SAH A 501       0.571  24.975  52.587  1.00 36.75           O  
-HETATM 2743  C5' SAH A 501       6.343  24.751  51.173  1.00 38.01           C  
-HETATM 2744  C4' SAH A 501       6.348  25.039  49.683  1.00 35.18           C  
-HETATM 2745  O4' SAH A 501       7.458  25.848  49.470  1.00 33.47           O  
-HETATM 2746  C3' SAH A 501       6.527  23.846  48.735  1.00 33.89           C  
-HETATM 2747  O3' SAH A 501       5.438  23.722  47.839  1.00 31.17           O  
-HETATM 2748  C2' SAH A 501       7.818  24.165  47.982  1.00 35.34           C  
-HETATM 2749  O2' SAH A 501       7.885  23.701  46.641  1.00 38.30           O  
-HETATM 2750  C1' SAH A 501       7.845  25.676  48.115  1.00 33.04           C  
-HETATM 2751  N9  SAH A 501       9.173  26.272  47.853  1.00 33.43           N  
-HETATM 2752  C8  SAH A 501      10.351  26.058  48.525  1.00 34.11           C  
-HETATM 2753  N7  SAH A 501      11.343  26.800  47.957  1.00 34.36           N  
-HETATM 2754  C5  SAH A 501      10.803  27.503  46.930  1.00 34.55           C  
-HETATM 2755  C6  SAH A 501      11.339  28.429  46.023  1.00 32.75           C  
-HETATM 2756  N6  SAH A 501      12.627  28.758  46.067  1.00 32.47           N  
-HETATM 2757  N1  SAH A 501      10.519  28.999  45.076  1.00 31.96           N  
-HETATM 2758  C2  SAH A 501       9.175  28.670  45.010  1.00 34.77           C  
-HETATM 2759  N3  SAH A 501       8.639  27.748  45.908  1.00 34.00           N  
-HETATM 2760  C4  SAH A 501       9.437  27.183  46.859  1.00 34.77           C  
-HETATM 2761  O6 A37T A 502       7.984  21.918  59.473  0.33 24.90           O  
-HETATM 2762  O6 B37T A 502       3.836  22.513  55.693  0.33 21.99           O  
-HETATM 2763  C6 A37T A 502       7.454  22.194  58.379  0.33 26.32           C  
-HETATM 2764  C6 B37T A 502       5.049  22.531  55.971  0.33 21.97           C  
-HETATM 2765  N1 A37T A 502       8.193  22.637  57.328  0.33 25.65           N  
-HETATM 2766  N1 B37T A 502       5.955  22.950  55.047  0.33 21.58           N  
-HETATM 2767  C5 A37T A 502       5.991  22.076  58.137  0.33 26.36           C  
-HETATM 2768  C5 B37T A 502       5.601  22.119  57.300  0.33 21.77           C  
-HETATM 2769  N7 A37T A 502       4.948  21.690  58.877  0.33 25.73           N  
-HETATM 2770  N7 B37T A 502       5.072  21.645  58.448  0.33 22.13           N  
-HETATM 2771  C13A37T A 502       5.007  21.245  60.270  0.33 25.46           C  
-HETATM 2772  C13B37T A 502       3.643  21.396  58.730  0.33 21.07           C  
-HETATM 2773  C8 A37T A 502       3.838  21.782  58.105  0.33 25.33           C  
-HETATM 2774  C8 B37T A 502       6.100  21.432  59.316  0.33 21.17           C  
-HETATM 2775  N9 A37T A 502       4.140  22.230  56.852  0.33 25.42           N  
-HETATM 2776  N9 B37T A 502       7.305  21.746  58.749  0.33 21.40           N  
-HETATM 2777  C4 A37T A 502       5.478  22.430  56.830  0.33 26.10           C  
-HETATM 2778  C4 B37T A 502       7.042  22.178  57.483  0.33 20.97           C  
-HETATM 2779  N3 A37T A 502       6.310  22.847  55.872  0.33 26.21           N  
-HETATM 2780  N3 B37T A 502       7.839  22.614  56.496  0.33 20.89           N  
-HETATM 2781  C12A37T A 502       5.767  23.191  54.561  0.33 25.77           C  
-HETATM 2782  C12B37T A 502       9.291  22.660  56.710  0.33 21.30           C  
-HETATM 2783  C2 A37T A 502       7.635  22.946  56.120  0.33 25.33           C  
-HETATM 2784  C2 B37T A 502       7.298  22.992  55.303  0.33 20.88           C  
-HETATM 2785  O2 A37T A 502       8.393  23.335  55.205  0.33 25.21           O  
-HETATM 2786  O2 B37T A 502       8.039  23.392  54.381  0.33 21.11           O  
-HETATM 2787  O   HOH A 503       7.268  31.348  53.588  1.00 24.96           O  
-HETATM 2788  O   HOH A 504       2.769  41.274  37.573  1.00 32.52           O  
-HETATM 2789  O   HOH A 505      27.198  29.136  53.541  1.00 29.72           O  
-HETATM 2790  O   HOH A 506       2.190  34.100  55.577  1.00 26.50           O  
-HETATM 2791  O   HOH A 507      20.048   4.295  52.538  1.00 40.72           O  
-HETATM 2792  O   HOH A 508       1.390  20.148  55.958  1.00 59.56           O  
-HETATM 2793  O   HOH A 509       8.748  22.482  61.604  0.50 13.72           O  
-HETATM 2794  O   HOH A 510       5.125  21.717  46.482  1.00 43.82           O  
-HETATM 2795  O   HOH A 511      25.860  35.597  53.635  1.00 39.09           O  
-HETATM 2796  O   HOH A 512       3.028  18.862  73.485  1.00 43.98           O  
-HETATM 2797  O   HOH A 513      -4.874  37.394  34.684  1.00 31.50           O  
-HETATM 2798  O   HOH A 514       8.477  25.026  63.159  1.00 50.48           O  
-HETATM 2799  O   HOH A 515      13.573  33.808  67.660  1.00 40.08           O  
-HETATM 2800  O   HOH A 516      15.194  46.425  45.802  1.00 54.33           O  
-HETATM 2801  O   HOH A 517       2.632  30.481  50.446  1.00 28.88           O  
-HETATM 2802  O   HOH A 518      -4.636  21.149  33.890  1.00 46.67           O  
-HETATM 2803  O   HOH A 519      13.108  30.608  38.518  1.00 41.43           O  
-HETATM 2804  O   HOH A 520      14.110  26.852  47.630  1.00 29.54           O  
-HETATM 2805  O   HOH A 521      15.043  25.654  45.353  1.00 48.67           O  
-HETATM 2806  O   HOH A 522       1.208  17.472  54.453  1.00 71.78           O  
-HETATM 2807  O   HOH A 523       9.759  23.895  66.516  1.00 36.75           O  
-HETATM 2808  O   HOH A 524      14.409  44.907  53.906  1.00 42.71           O  
-HETATM 2809  O   HOH A 525       6.143  37.664  69.520  1.00 42.51           O  
-HETATM 2810  O   HOH A 526      24.719  15.412  57.558  1.00 34.73           O  
-HETATM 2811  O   HOH A 527      14.851   2.651  67.749  1.00 53.99           O  
-HETATM 2812  O   HOH A 528      16.641   2.611  51.589  1.00 38.82           O  
-HETATM 2813  O   HOH A 529      -1.626  25.668  57.582  1.00 33.85           O  
-HETATM 2814  O   HOH A 530       9.551  45.440  34.396  1.00 33.61           O  
-HETATM 2815  O   HOH A 531      -0.391  22.174  56.844  1.00 44.15           O  
-HETATM 2816  O   HOH A 532      10.677  21.077  41.573  1.00 62.99           O  
-HETATM 2817  O   HOH A 533      21.810  11.667  47.497  1.00 54.10           O  
-HETATM 2818  O   HOH A 534      -7.342  52.546  42.342  1.00 40.74           O  
-HETATM 2819  O   HOH A 535      18.452  26.629  62.342  1.00 39.05           O  
-HETATM 2820  O   HOH A 536      10.632  31.679  36.485  1.00 33.85           O  
-HETATM 2821  O   HOH A 537      -4.176  58.464  48.362  1.00 50.40           O  
-HETATM 2822  O   HOH A 538      14.400   1.247  48.097  1.00 73.00           O  
-HETATM 2823  O   HOH A 539      -9.536  54.547  42.130  1.00 44.49           O  
-HETATM 2824  O   HOH A 540       0.722  44.811  58.240  1.00 47.62           O  
-HETATM 2825  O   HOH A 541       3.204  23.030  76.563  1.00 33.51           O  
-HETATM 2826  O   HOH A 542      22.557  15.125  51.096  1.00 43.56           O  
-HETATM 2827  O   HOH A 543      -4.630  32.653  55.860  1.00 39.95           O  
-HETATM 2828  O   HOH A 544       6.980  23.894  77.482  1.00 40.93           O  
-HETATM 2829  O   HOH A 545      -2.796  21.930  50.881  1.00 38.23           O  
-HETATM 2830  O   HOH A 546      -6.719  16.459  49.954  1.00 64.50           O  
-HETATM 2831  O   HOH A 547      -0.633  29.095  51.245  1.00 50.16           O  
-HETATM 2832  O   HOH A 548      12.758  25.729  65.148  1.00 37.46           O  
-HETATM 2833  O   HOH A 549       0.285  10.693  47.485  1.00 50.26           O  
-HETATM 2834  O   HOH A 550      -3.054  32.733  54.051  1.00 37.34           O  
-HETATM 2835  O   HOH A 551       0.622  46.450  37.352  1.00 39.35           O  
-HETATM 2836  O   HOH A 552      11.409   1.664  67.344  1.00 49.27           O  
-HETATM 2837  O   HOH A 553     -16.135  21.580  36.966  1.00 54.67           O  
-HETATM 2838  O   HOH A 554      -0.826  43.164  59.562  1.00 43.39           O  
-HETATM 2839  O   HOH A 555      25.953   8.637  50.906  1.00 53.67           O  
-HETATM 2840  O   HOH A 556       1.127  19.869  71.418  1.00 38.54           O  
-HETATM 2841  O   HOH A 557      11.110  16.679  50.001  1.00 38.11           O  
-HETATM 2842  O   HOH A 558       5.869  52.291  53.758  1.00 53.70           O  
-HETATM 2843  O   HOH A 559       5.345  49.891  36.728  1.00 45.68           O  
-HETATM 2844  O   HOH A 560      14.136  56.364  47.566  1.00 56.03           O  
-HETATM 2845  O   HOH A 561      27.718  19.199  63.104  1.00 35.94           O  
-HETATM 2846  O   HOH A 562      -7.583  18.178  39.962  1.00 48.17           O  
-HETATM 2847  O   HOH A 563      19.849  33.315  46.751  1.00 58.38           O  
-HETATM 2848  O   HOH A 564       1.776  11.336  72.587  1.00 54.65           O  
-HETATM 2849  O   HOH A 565      24.631  17.371  50.427  1.00 44.14           O  
-HETATM 2850  O   HOH A 566      26.449   9.613  63.331  1.00 63.40           O  
-HETATM 2851  O   HOH A 567      -1.115  47.952  38.814  1.00 46.11           O  
-HETATM 2852  O   HOH A 568      20.783  40.710  46.959  1.00 50.00           O  
-HETATM 2853  O   HOH A 569       5.312  43.608  65.994  1.00 45.28           O  
-HETATM 2854  O   HOH A 570      22.512  27.932  63.474  1.00 49.25           O  
-HETATM 2855  O   HOH A 571      18.177  35.983  41.694  1.00 47.05           O  
-HETATM 2856  O   HOH A 572      23.245  28.442  68.180  1.00 57.13           O  
-HETATM 2857  O   HOH A 573      11.717  48.786  60.086  1.00 44.62           O  
-HETATM 2858  O   HOH A 574      -2.315  44.160  35.598  1.00 45.69           O  
-HETATM 2859  O   HOH A 575      -9.440  24.764  50.435  1.00 51.14           O  
-HETATM 2860  O   HOH A 576      -7.427  14.069  49.599  1.00 52.56           O  
-HETATM 2861  O   HOH A 577       7.496  47.251  34.762  1.00 49.08           O  
-HETATM 2862  O   HOH A 578      27.942   2.830  60.830  1.00 55.69           O  
-HETATM 2863  O   HOH A 579      -7.467  40.922  61.955  1.00 44.94           O  
-HETATM 2864  O   HOH A 580      15.184  32.899  52.553  1.00 42.85           O  
-HETATM 2865  O   HOH A 581      12.801  11.468  45.222  1.00 45.06           O  
-HETATM 2866  O   HOH A 582      -0.995  34.164  68.459  1.00 60.10           O  
-HETATM 2867  O   HOH A 583      21.342  46.144  50.132  1.00 62.79           O  
-HETATM 2868  O   HOH A 584       0.325  46.707  60.175  1.00 46.19           O  
-HETATM 2869  O   HOH A 585     -11.151  35.188  55.304  1.00 45.71           O  
-HETATM 2870  O   HOH A 586      -5.601  48.322  60.995  1.00 53.03           O  
-HETATM 2871  O   HOH A 587       1.485  23.557  56.059  1.00 44.62           O  
-HETATM 2872  O   HOH A 588      -8.436  44.159  60.160  1.00 63.34           O  
-HETATM 2873  O   HOH A 589      23.701  31.255  47.232  1.00 47.01           O  
-HETATM 2874  O   HOH A 590      20.417  27.036  64.308  1.00 52.45           O  
-HETATM 2875  O   HOH A 591      22.187  22.451  46.676  1.00 48.63           O  
-HETATM 2876  O   HOH A 592      12.405  50.329  49.228  1.00 45.54           O  
-HETATM 2877  O   HOH A 593      21.447  42.995  48.272  1.00 41.78           O  
-HETATM 2878  O   HOH A 594      18.302   6.590  45.593  1.00 60.20           O  
-HETATM 2879  O   HOH A 595      -0.999  45.111  64.584  1.00 58.08           O  
-HETATM 2880  O   HOH A 596      -1.100   8.667  46.213  1.00 62.47           O  
-HETATM 2881  O   HOH A 597       5.674  -1.073  67.682  1.00 55.61           O  
-HETATM 2882  O   HOH A 598      13.360  26.305  71.470  1.00 47.17           O  
-HETATM 2883  O   HOH A 599       9.111  56.055  46.503  1.00 49.20           O  
-HETATM 2884  O   HOH A 600       4.917  42.292  68.116  1.00 52.54           O  
-HETATM 2885  O   HOH A 601      33.684  31.653  56.541  1.00 55.75           O  
-HETATM 2886  O   HOH A 602     -13.016  32.767  60.276  1.00 57.25           O  
-HETATM 2887  O   HOH A 603      -4.443  11.965  72.549  1.00 55.37           O  
-HETATM 2888  O   HOH A 604      22.489  20.135  46.117  1.00 50.10           O  
-HETATM 2889  O   HOH A 605      12.137  18.761  73.488  1.00 56.72           O  
-HETATM 2890  O   HOH A 606      20.654  41.836  54.427  1.00 41.60           O  
-HETATM 2891  O   HOH A 607      16.315  29.181  43.827  1.00 38.02           O  
-HETATM 2892  O   HOH A 608      17.569  24.739  64.800  1.00 53.19           O  
-HETATM 2893  O   HOH A 609      16.352  37.075  38.567  1.00 47.41           O  
-HETATM 2894  O   HOH A 610      -8.028  30.995  36.075  1.00 27.92           O  
-HETATM 2895  O   HOH A 611      12.172  33.160  39.153  1.00 38.03           O  
-HETATM 2896  O   HOH A 612      30.984  19.099  61.732  1.00 50.37           O  
-HETATM 2897  O   HOH A 613      22.410  40.955  56.130  1.00 48.60           O  
-HETATM 2898  O   HOH A 614      -1.684  26.441  65.614  1.00 45.98           O  
-HETATM 2899  O   HOH A 615      19.348  33.156  44.258  1.00 49.45           O  
-HETATM 2900  O   HOH A 616       4.399   8.381  48.787  1.00 56.54           O  
-HETATM 2901  O   HOH A 617      13.037  58.107  49.218  1.00 67.97           O  
-HETATM 2902  O   HOH A 618      13.015  27.401  68.974  1.00 40.69           O  
-HETATM 2903  O   HOH A 619      23.096  37.783  59.051  1.00 39.88           O  
-HETATM 2904  O   HOH A 620      -7.167  49.139  58.970  1.00 56.26           O  
-HETATM 2905  O   HOH A 621      24.148  45.913  52.882  1.00 52.42           O  
-HETATM 2906  O   HOH A 622       2.496  17.764  62.092  1.00 52.10           O  
-HETATM 2907  O   HOH A 623     -15.072  44.624  41.078  1.00 54.55           O  
-HETATM 2908  O   HOH A 624      -1.262  48.771  62.741  1.00 47.91           O  
-HETATM 2909  O   HOH A 625      19.150  10.828  68.529  1.00 45.76           O  
-HETATM 2910  O   HOH A 626      16.975   3.727  68.790  1.00 53.48           O  
-HETATM 2911  O   HOH A 627      22.990   9.019  48.307  1.00 51.62           O  
-HETATM 2912  O   HOH A 628     -16.168  33.805  40.846  1.00 53.56           O  
-HETATM 2913  O   HOH A 629      33.205  16.096  60.989  1.00 50.30           O  
-HETATM 2914  O   HOH A 630      28.188  25.643  46.554  1.00 56.78           O  
-HETATM 2915  O   HOH A 631      29.551  30.439  54.767  1.00 59.56           O  
-HETATM 2916  O   HOH A 632       1.490  53.717  47.104  1.00 44.54           O  
-HETATM 2917  O   HOH A 633       2.204  20.111  44.646  1.00 43.36           O  
-HETATM 2918  O   HOH A 634      -1.878  16.499  36.764  1.00 43.53           O  
-HETATM 2919  O   HOH A 635     -17.837  43.996  50.213  1.00 65.29           O  
-HETATM 2920  O   HOH A 636     -13.839  45.504  48.010  1.00 49.61           O  
-HETATM 2921  O   HOH A 637      17.665  20.978  66.935  1.00 50.28           O  
-HETATM 2922  O   HOH A 638      -9.225  10.891  61.566  1.00 63.86           O  
-HETATM 2923  O   HOH A 639       1.399  42.062  35.662  1.00 46.66           O  
-HETATM 2924  O   HOH A 640      -3.775  47.107  38.929  1.00 32.64           O  
-HETATM 2925  O   HOH A 641      15.194  42.350  40.068  1.00 48.87           O  
-HETATM 2926  O   HOH A 642       8.854  54.839  43.889  1.00 61.84           O  
-HETATM 2927  O   HOH A 643      18.498  40.041  39.644  1.00 50.05           O  
-HETATM 2928  O   HOH A 644     -16.810  28.302  36.978  1.00 47.76           O  
-HETATM 2929  O   HOH A 645     -11.620  24.904  46.388  1.00 49.14           O  
-HETATM 2930  O   HOH A 646     -13.966  35.078  39.234  1.00 70.83           O  
-HETATM 2931  O   HOH A 647       0.401  25.878  56.086  1.00 39.48           O  
-HETATM 2932  O   HOH A 648      14.959   9.024  69.817  1.00 48.58           O  
-CONECT 2735 2736                                                                
-CONECT 2736 2735 2737 2740                                                      
-CONECT 2737 2736 2738                                                           
-CONECT 2738 2737 2739                                                           
-CONECT 2739 2738 2743                                                           
-CONECT 2740 2736 2741 2742                                                      
-CONECT 2741 2740                                                                
-CONECT 2742 2740                                                                
-CONECT 2743 2739 2744                                                           
-CONECT 2744 2743 2745 2746                                                      
-CONECT 2745 2744 2750                                                           
-CONECT 2746 2744 2747 2748                                                      
-CONECT 2747 2746                                                                
-CONECT 2748 2746 2749 2750                                                      
-CONECT 2749 2748                                                                
-CONECT 2750 2745 2748 2751                                                      
-CONECT 2751 2750 2752 2760                                                      
-CONECT 2752 2751 2753                                                           
-CONECT 2753 2752 2754                                                           
-CONECT 2754 2753 2755 2760                                                      
-CONECT 2755 2754 2756 2757                                                      
-CONECT 2756 2755                                                                
-CONECT 2757 2755 2758                                                           
-CONECT 2758 2757 2759                                                           
-CONECT 2759 2758 2760                                                           
-CONECT 2760 2751 2754 2759                                                      
-CONECT 2761 2763                                                                
-CONECT 2762 2764                                                                
-CONECT 2763 2761 2765 2767                                                      
-CONECT 2764 2762 2766 2768                                                      
-CONECT 2765 2763 2783                                                           
-CONECT 2766 2764 2784                                                           
-CONECT 2767 2763 2769 2777                                                      
-CONECT 2768 2764 2770 2778                                                      
-CONECT 2769 2767 2771 2773                                                      
-CONECT 2770 2768 2772 2774                                                      
-CONECT 2771 2769                                                                
-CONECT 2772 2770                                                                
-CONECT 2773 2769 2775                                                           
-CONECT 2774 2770 2776                                                           
-CONECT 2775 2773 2777                                                           
-CONECT 2776 2774 2778                                                           
-CONECT 2777 2767 2775 2779                                                      
-CONECT 2778 2768 2776 2780                                                      
-CONECT 2779 2777 2781 2783                                                      
-CONECT 2780 2778 2782 2784                                                      
-CONECT 2781 2779                                                                
-CONECT 2782 2780                                                                
-CONECT 2783 2765 2779 2785                                                      
-CONECT 2784 2766 2780 2786                                                      
-CONECT 2785 2783                                                                
-CONECT 2786 2784                                                                
-MASTER      436    0    2   10    7    0   10    6 2904    1   52   30          
-END                                                                             
diff --git a/plip/test/pdb/2iuz.pdb b/plip/test/pdb/2iuz.pdb
deleted file mode 100644
index d157fdc..0000000
--- a/plip/test/pdb/2iuz.pdb
+++ /dev/null
@@ -1,8056 +0,0 @@
-HEADER    HYDROLASE                               08-JUN-06   2IUZ              
-TITLE     CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS CHITINASE B1 IN            
-TITLE    2 COMPLEX WITH C2-DICAFFEINE                                           
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CHITINASE;                                                 
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 FRAGMENT: RESIDUES 1-433;                                            
-COMPND   5 SYNONYM: ASPERGILLUS FUMIGATUS CHITINASE B1, CLASS V                 
-COMPND   6  CHITINASE CHIB1;                                                    
-COMPND   7 EC: 3.2.1.14;                                                        
-COMPND   8 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;                          
-SOURCE   3 ORGANISM_TAXID: 5085;                                                
-SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
-SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
-SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PGEX-6P-1;                                 
-SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PLYSS                                     
-KEYWDS    HYDROLASE, GLYCOSIDASE, (BETA-ALPHA)8 BARREL, CHITINASE-              
-KEYWDS   2 C2DICAFFEINE COMPLEX                                                 
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    A.W.SCHUTTELKOPF,O.A.ANDERSEN,F.V.RAO,M.ALLWOOD,C.M.LLOYD,            
-AUTHOR   2 I.M.EGGLESTON,D.M.F.VAN AALTEN                                       
-REVDAT   3   24-FEB-09 2IUZ    1       VERSN                                    
-REVDAT   2   18-SEP-06 2IUZ    1       JRNL                                     
-REVDAT   1   12-JUN-06 2IUZ    0                                                
-JRNL        AUTH   A.W.SCHUTTELKOPF,O.A.ANDERSEN,F.V.RAO,M.ALLWOOD,             
-JRNL        AUTH 2 C.M.LLOYD,I.M.EGGLESTON,D.M.F.VAN AALTEN                     
-JRNL        TITL   SCREENING-BASED DISCOVERY AND STRUCTURAL                     
-JRNL        TITL 2 DISSECTION OF A NOVEL FAMILY 18 CHITINASE                    
-JRNL        TITL 3 INHIBITOR                                                    
-JRNL        REF    J.BIOL.CHEM.                  V. 281 27278 2006              
-JRNL        REFN                   ISSN 0021-9258                               
-JRNL        PMID   16844689                                                     
-JRNL        DOI    10.1074/JBC.M604048200                                       
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS 1.0                                              
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : NULL                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.0                           
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
-REMARK   3   NUMBER OF REFLECTIONS             : 96114                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.1867                          
-REMARK   3   FREE R VALUE                     : 0.2233                          
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.0                             
-REMARK   3   FREE R VALUE TEST SET COUNT      : 966                             
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 19                           
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99                           
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4853                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.285                        
-REMARK   3   BIN FREE R VALUE                    : 0.361                        
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1                            
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 57                           
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.048                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 6153                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 167                                     
-REMARK   3   SOLVENT ATOMS            : 881                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 24.4                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.3                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -0.719                                               
-REMARK   3    B22 (A**2) : -0.719                                               
-REMARK   3    B33 (A**2) : 1.439                                                
-REMARK   3    B12 (A**2) : 0.000                                                
-REMARK   3    B13 (A**2) : 0.000                                                
-REMARK   3    B23 (A**2) : 0.000                                                
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.222                           
-REMARK   3   ESD FROM SIGMAA              (A) : 0.225                           
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5                               
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.268                           
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.266                           
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.010389                        
-REMARK   3   BOND ANGLES            (DEGREES) : 1.49698                         
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.7                            
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.55  ; 1.50                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.33  ; 2.00                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.12  ; 2.00                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.15  ; 2.50                 
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : ANISOTROPIC                                          
-REMARK   3   KSOL        : 0.367202                                             
-REMARK   3   BSOL        : 51.6564                                              
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
-REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
-REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
-REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
-REMARK   3  PARAMETER FILE  5  : DRGCNS.PAR                                     
-REMARK   3  PARAMETER FILE  6  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
-REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
-REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
-REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
-REMARK   3  TOPOLOGY FILE  5   : DRGCNS.TOP                                     
-REMARK   3  TOPOLOGY FILE  6   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 2IUZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  08-JUN-06.                 
-REMARK 100 THE PDBE ID CODE IS EBI-29029.                                       
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 03-OCT-04                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
-REMARK 200  PH                             : 9.50                               
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ESRF                               
-REMARK 200  BEAMLINE                       : BM14                               
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
-REMARK 200  MONOCHROMATOR                  : SI(111)                            
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 96150                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
-REMARK 200  DATA REDUNDANCY                : 2.900                              
-REMARK 200  R MERGE                    (I) : 0.06000                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.0000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.45000                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
-REMARK 200 SOFTWARE USED: NULL                                                  
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: REFINEMENT STARTED FROM STRUCTURE 1W9P                       
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 66                                        
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.6                      
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS/HCL PH 9.5, 1.4 M             
-REMARK 280  LI2SO4                                                              
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,-Y,Z+1/2                                             
-REMARK 290       3555   -Y,X,Z+1/4                                              
-REMARK 290       4555   Y,-X,Z+3/4                                              
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.71000            
-REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.85500            
-REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.56500            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2                                                    
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 GENERATING THE BIOMOLECULE                                           
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE:  1                                                      
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PQS                                                   
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350 BIOMOLECULE:  2                                                      
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PQS                                                   
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     ARG A     2                                                      
-REMARK 465     PHE A     3                                                      
-REMARK 465     ALA A     4                                                      
-REMARK 465     THR A     5                                                      
-REMARK 465     SER A     6                                                      
-REMARK 465     THR A     7                                                      
-REMARK 465     ILE A     8                                                      
-REMARK 465     VAL A     9                                                      
-REMARK 465     LYS A    10                                                      
-REMARK 465     VAL A    11                                                      
-REMARK 465     ALA A    12                                                      
-REMARK 465     LEU A    13                                                      
-REMARK 465     LEU A    14                                                      
-REMARK 465     LEU A    15                                                      
-REMARK 465     SER A    16                                                      
-REMARK 465     SER A    17                                                      
-REMARK 465     LEU A    18                                                      
-REMARK 465     CYS A    19                                                      
-REMARK 465     VAL A    20                                                      
-REMARK 465     ASP A    21                                                      
-REMARK 465     ALA A    22                                                      
-REMARK 465     ALA A    23                                                      
-REMARK 465     VAL A    24                                                      
-REMARK 465     MET A    25                                                      
-REMARK 465     TRP A    26                                                      
-REMARK 465     ASN A    27                                                      
-REMARK 465     ARG A    28                                                      
-REMARK 465     ASP A    29                                                      
-REMARK 465     THR A    30                                                      
-REMARK 465     SER A    31                                                      
-REMARK 465     SER A    32                                                      
-REMARK 465     THR A    33                                                      
-REMARK 465     ASP A    34                                                      
-REMARK 465     LEU A    35                                                      
-REMARK 465     GLU A    36                                                      
-REMARK 465     ALA A    37                                                      
-REMARK 465     ARG A    38                                                      
-REMARK 465     MET B     1                                                      
-REMARK 465     ARG B     2                                                      
-REMARK 465     PHE B     3                                                      
-REMARK 465     ALA B     4                                                      
-REMARK 465     THR B     5                                                      
-REMARK 465     SER B     6                                                      
-REMARK 465     THR B     7                                                      
-REMARK 465     ILE B     8                                                      
-REMARK 465     VAL B     9                                                      
-REMARK 465     LYS B    10                                                      
-REMARK 465     VAL B    11                                                      
-REMARK 465     ALA B    12                                                      
-REMARK 465     LEU B    13                                                      
-REMARK 465     LEU B    14                                                      
-REMARK 465     LEU B    15                                                      
-REMARK 465     SER B    16                                                      
-REMARK 465     SER B    17                                                      
-REMARK 465     LEU B    18                                                      
-REMARK 465     CYS B    19                                                      
-REMARK 465     VAL B    20                                                      
-REMARK 465     ASP B    21                                                      
-REMARK 465     ALA B    22                                                      
-REMARK 465     ALA B    23                                                      
-REMARK 465     VAL B    24                                                      
-REMARK 465     MET B    25                                                      
-REMARK 465     TRP B    26                                                      
-REMARK 465     ASN B    27                                                      
-REMARK 465     ARG B    28                                                      
-REMARK 465     ASP B    29                                                      
-REMARK 465     THR B    30                                                      
-REMARK 465     SER B    31                                                      
-REMARK 465     SER B    32                                                      
-REMARK 465     THR B    33                                                      
-REMARK 465     ASP B    34                                                      
-REMARK 465     LEU B    35                                                      
-REMARK 465     GLU B    36                                                      
-REMARK 465     ALA B    37                                                      
-REMARK 465     ARG B    38                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     THR B 433    CA   C    O    CB   OG1  CG2                        
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASP A  90       86.53   -160.05                                   
-REMARK 500    ALA A 259       23.41   -150.68                                   
-REMARK 500    ASN A 267       63.46   -159.28                                   
-REMARK 500    LEU A 298       42.74   -108.34                                   
-REMARK 500    GLN B 210      129.07    -36.92                                   
-REMARK 500    ALA B 259       24.16   -150.09                                   
-REMARK 500    ASN B 267       63.13   -154.91                                   
-REMARK 500    SER B 413      115.08   -166.22                                   
-REMARK 500    MET B 431       72.24     53.09                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 700                                                                      
-REMARK 700 SHEET                                                                
-REMARK 700 DETERMINATION METHOD: DSSP                                           
-REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
-REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY       
-REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
-REMARK 700 ARE IDENTICAL.                                                       
-REMARK 700                                                                      
-REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS          
-REMARK 700 BELOW IS ACTUALLY AN  9-STRANDED BARREL THIS IS REPRESENTED BY       
-REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
-REMARK 700 ARE IDENTICAL.                                                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1434                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1435                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1436                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1437                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1438                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1439                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1433                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1434                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1435                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1436                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1437                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1H A1440                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1H B1438                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 1W9P   RELATED DB: PDB                                   
-REMARK 900  SPECIFICITY AND AFFINITY OF NATURAL PRODUCT                         
-REMARK 900  CYCLOPENTAPEPTIDE INHIBITORS AGAINST ASPERGILLUS                    
-REMARK 900  FUMIGATUS, HUMAN AND BACTERIAL CHITINASEFRA                         
-REMARK 900 RELATED ID: 1W9U   RELATED DB: PDB                                   
-REMARK 900  SPECIFICITY AND AFFNITY OF NATURAL PRODUCT                          
-REMARK 900  CYCLOPENTAPEPTIDE INHIBITOR ARGADIN AGAINST                         
-REMARK 900  ASPERGILLUS FUMIGATUS CHITINASE                                     
-REMARK 900 RELATED ID: 1W9V   RELATED DB: PDB                                   
-REMARK 900  SPECIFICITY AND AFFINITY OF NATURAL PRODUCT                         
-REMARK 900  CYCLOPENTAPEPTIDE ARGIFIN AGAINST ASPERGILLUS                       
-REMARK 900  FUMIGATUS                                                           
-REMARK 900 RELATED ID: 2A3A   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS                          
-REMARK 900  CHITINASE B1 INCOMPLEX WITH THEOPHYLLINE                            
-REMARK 900 RELATED ID: 2A3B   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS                          
-REMARK 900  CHITINASE B1 INCOMPLEX WITH CAFFEINE                                
-REMARK 900 RELATED ID: 2A3C   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS                          
-REMARK 900  CHITINASE B1 INCOMPLEX WITH PENTOXIFYLLINE                          
-REMARK 900 RELATED ID: 2A3E   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS                          
-REMARK 900  CHITINASE B1 INCOMPLEX WITH ALLOSAMIDIN                             
-DBREF  2IUZ A    1   433  UNP    Q873X9   Q873X9_ASPFU     1    433             
-DBREF  2IUZ B    1   433  UNP    Q873X9   Q873X9_ASPFU     1    433             
-SEQRES   1 A  433  MET ARG PHE ALA THR SER THR ILE VAL LYS VAL ALA LEU          
-SEQRES   2 A  433  LEU LEU SER SER LEU CYS VAL ASP ALA ALA VAL MET TRP          
-SEQRES   3 A  433  ASN ARG ASP THR SER SER THR ASP LEU GLU ALA ARG ALA          
-SEQRES   4 A  433  SER SER GLY TYR ARG SER VAL VAL TYR PHE VAL ASN TRP          
-SEQRES   5 A  433  ALA ILE TYR GLY ARG ASN HIS ASN PRO GLN ASP LEU PRO          
-SEQRES   6 A  433  VAL GLU ARG LEU THR HIS VAL LEU TYR ALA PHE ALA ASN          
-SEQRES   7 A  433  VAL ARG PRO GLU THR GLY GLU VAL TYR MET THR ASP SER          
-SEQRES   8 A  433  TRP ALA ASP ILE GLU LYS HIS TYR PRO GLY ASP SER TRP          
-SEQRES   9 A  433  SER ASP THR GLY ASN ASN VAL TYR GLY CYS ILE LYS GLN          
-SEQRES  10 A  433  LEU TYR LEU LEU LYS LYS GLN ASN ARG ASN LEU LYS VAL          
-SEQRES  11 A  433  LEU LEU SER ILE GLY GLY TRP THR TYR SER PRO ASN PHE          
-SEQRES  12 A  433  ALA PRO ALA ALA SER THR ASP ALA GLY ARG LYS ASN PHE          
-SEQRES  13 A  433  ALA LYS THR ALA VAL LYS LEU LEU GLN ASP LEU GLY PHE          
-SEQRES  14 A  433  ASP GLY LEU ASP ILE ASP TRP GLU TYR PRO GLU ASN ASP          
-SEQRES  15 A  433  GLN GLN ALA ASN ASP PHE VAL LEU LEU LEU LYS GLU VAL          
-SEQRES  16 A  433  ARG THR ALA LEU ASP SER TYR SER ALA ALA ASN ALA GLY          
-SEQRES  17 A  433  GLY GLN HIS PHE LEU LEU THR VAL ALA SER PRO ALA GLY          
-SEQRES  18 A  433  PRO ASP LYS ILE LYS VAL LEU HIS LEU LYS ASP MET ASP          
-SEQRES  19 A  433  GLN GLN LEU ASP PHE TRP ASN LEU MET ALA TYR ASP TYR          
-SEQRES  20 A  433  ALA GLY SER PHE SER SER LEU SER GLY HIS GLN ALA ASN          
-SEQRES  21 A  433  VAL TYR ASN ASP THR SER ASN PRO LEU SER THR PRO PHE          
-SEQRES  22 A  433  ASN THR GLN THR ALA LEU ASP LEU TYR ARG ALA GLY GLY          
-SEQRES  23 A  433  VAL PRO ALA ASN LYS ILE VAL LEU GLY MET PRO LEU TYR          
-SEQRES  24 A  433  GLY ARG SER PHE ALA ASN THR ASP GLY PRO GLY LYS PRO          
-SEQRES  25 A  433  TYR ASN GLY VAL GLY GLN GLY SER TRP GLU ASN GLY VAL          
-SEQRES  26 A  433  TRP ASP TYR LYS ALA LEU PRO GLN ALA GLY ALA THR GLU          
-SEQRES  27 A  433  HIS VAL LEU PRO ASP ILE MET ALA SER TYR SER TYR ASP          
-SEQRES  28 A  433  ALA THR ASN LYS PHE LEU ILE SER TYR ASP ASN PRO GLN          
-SEQRES  29 A  433  VAL ALA ASN LEU LYS SER GLY TYR ILE LYS SER LEU GLY          
-SEQRES  30 A  433  LEU GLY GLY ALA MET TRP TRP ASP SER SER SER ASP LYS          
-SEQRES  31 A  433  THR GLY SER ASP SER LEU ILE THR THR VAL VAL ASN ALA          
-SEQRES  32 A  433  LEU GLY GLY THR GLY VAL PHE GLU GLN SER GLN ASN GLU          
-SEQRES  33 A  433  LEU ASP TYR PRO VAL SER GLN TYR ASP ASN LEU ARG ASN          
-SEQRES  34 A  433  GLY MET GLN THR                                              
-SEQRES   1 B  433  MET ARG PHE ALA THR SER THR ILE VAL LYS VAL ALA LEU          
-SEQRES   2 B  433  LEU LEU SER SER LEU CYS VAL ASP ALA ALA VAL MET TRP          
-SEQRES   3 B  433  ASN ARG ASP THR SER SER THR ASP LEU GLU ALA ARG ALA          
-SEQRES   4 B  433  SER SER GLY TYR ARG SER VAL VAL TYR PHE VAL ASN TRP          
-SEQRES   5 B  433  ALA ILE TYR GLY ARG ASN HIS ASN PRO GLN ASP LEU PRO          
-SEQRES   6 B  433  VAL GLU ARG LEU THR HIS VAL LEU TYR ALA PHE ALA ASN          
-SEQRES   7 B  433  VAL ARG PRO GLU THR GLY GLU VAL TYR MET THR ASP SER          
-SEQRES   8 B  433  TRP ALA ASP ILE GLU LYS HIS TYR PRO GLY ASP SER TRP          
-SEQRES   9 B  433  SER ASP THR GLY ASN ASN VAL TYR GLY CYS ILE LYS GLN          
-SEQRES  10 B  433  LEU TYR LEU LEU LYS LYS GLN ASN ARG ASN LEU LYS VAL          
-SEQRES  11 B  433  LEU LEU SER ILE GLY GLY TRP THR TYR SER PRO ASN PHE          
-SEQRES  12 B  433  ALA PRO ALA ALA SER THR ASP ALA GLY ARG LYS ASN PHE          
-SEQRES  13 B  433  ALA LYS THR ALA VAL LYS LEU LEU GLN ASP LEU GLY PHE          
-SEQRES  14 B  433  ASP GLY LEU ASP ILE ASP TRP GLU TYR PRO GLU ASN ASP          
-SEQRES  15 B  433  GLN GLN ALA ASN ASP PHE VAL LEU LEU LEU LYS GLU VAL          
-SEQRES  16 B  433  ARG THR ALA LEU ASP SER TYR SER ALA ALA ASN ALA GLY          
-SEQRES  17 B  433  GLY GLN HIS PHE LEU LEU THR VAL ALA SER PRO ALA GLY          
-SEQRES  18 B  433  PRO ASP LYS ILE LYS VAL LEU HIS LEU LYS ASP MET ASP          
-SEQRES  19 B  433  GLN GLN LEU ASP PHE TRP ASN LEU MET ALA TYR ASP TYR          
-SEQRES  20 B  433  ALA GLY SER PHE SER SER LEU SER GLY HIS GLN ALA ASN          
-SEQRES  21 B  433  VAL TYR ASN ASP THR SER ASN PRO LEU SER THR PRO PHE          
-SEQRES  22 B  433  ASN THR GLN THR ALA LEU ASP LEU TYR ARG ALA GLY GLY          
-SEQRES  23 B  433  VAL PRO ALA ASN LYS ILE VAL LEU GLY MET PRO LEU TYR          
-SEQRES  24 B  433  GLY ARG SER PHE ALA ASN THR ASP GLY PRO GLY LYS PRO          
-SEQRES  25 B  433  TYR ASN GLY VAL GLY GLN GLY SER TRP GLU ASN GLY VAL          
-SEQRES  26 B  433  TRP ASP TYR LYS ALA LEU PRO GLN ALA GLY ALA THR GLU          
-SEQRES  27 B  433  HIS VAL LEU PRO ASP ILE MET ALA SER TYR SER TYR ASP          
-SEQRES  28 B  433  ALA THR ASN LYS PHE LEU ILE SER TYR ASP ASN PRO GLN          
-SEQRES  29 B  433  VAL ALA ASN LEU LYS SER GLY TYR ILE LYS SER LEU GLY          
-SEQRES  30 B  433  LEU GLY GLY ALA MET TRP TRP ASP SER SER SER ASP LYS          
-SEQRES  31 B  433  THR GLY SER ASP SER LEU ILE THR THR VAL VAL ASN ALA          
-SEQRES  32 B  433  LEU GLY GLY THR GLY VAL PHE GLU GLN SER GLN ASN GLU          
-SEQRES  33 B  433  LEU ASP TYR PRO VAL SER GLN TYR ASP ASN LEU ARG ASN          
-SEQRES  34 B  433  GLY MET GLN THR                                              
-HET    SO4  A1434       5                                                       
-HET    SO4  A1435       5                                                       
-HET    SO4  A1436       5                                                       
-HET    SO4  A1437       5                                                       
-HET    SO4  A1438       5                                                       
-HET    SO4  A1439       5                                                       
-HET    SO4  B1433       5                                                       
-HET    SO4  B1434       5                                                       
-HET    SO4  B1435       5                                                       
-HET    SO4  B1436       5                                                       
-HET    SO4  B1437       5                                                       
-HET    D1H  A1440      56                                                       
-HET    D1H  B1438      56                                                       
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM     D1H 1,1'-ETHANE-1,2-DIYLBIS(3,7-DIMETHYL-3,7-                        
-HETNAM   2 D1H  DIHYDRO-1H-PURINE-2,6-DIONE)                                    
-HETSYN     D1H 1-(2-(THEOBROMINE-1-YL)ETHYL)-BROMINE                            
-FORMUL   3  SO4    11(O4 S 2-)                                                  
-FORMUL  14  D1H    2(C16 H18 N8 O4)                                             
-FORMUL  16  HOH   *881(H2 O1)                                                   
-HELIX    1   1 TRP A   52  TYR A   55  5                                   4    
-HELIX    2   2 ASN A   60  LEU A   64  5                                   5    
-HELIX    3   3 PRO A   65  LEU A   69  5                                   5    
-HELIX    4   4 ASP A   90  GLU A   96  1                                   7    
-HELIX    5   5 TYR A  112  ASN A  125  1                                  14    
-HELIX    6   6 GLY A  136  SER A  140  1                                   5    
-HELIX    7   7 ASN A  142  SER A  148  1                                   7    
-HELIX    8   8 THR A  149  GLY A  168  1                                  20    
-HELIX    9   9 ASN A  181  ALA A  207  1                                  27    
-HELIX   10  10 GLY A  221  LEU A  228  1                                   8    
-HELIX   11  11 HIS A  229  LEU A  237  1                                   9    
-HELIX   12  12 ASN A  267  THR A  271  5                                   5    
-HELIX   13  13 ASN A  274  GLY A  285  1                                  12    
-HELIX   14  14 PRO A  288  ASN A  290  5                                   3    
-HELIX   15  15 LYS A  329  LEU A  331  5                                   3    
-HELIX   16  16 PRO A  342  MET A  345  5                                   4    
-HELIX   17  17 ASN A  362  GLY A  377  1                                  16    
-HELIX   18  18 ASP A  385  ASP A  389  5                                   5    
-HELIX   19  19 THR A  391  ASP A  394  5                                   4    
-HELIX   20  20 SER A  395  LEU A  404  1                                  10    
-HELIX   21  21 GLY A  406  VAL A  409  5                                   4    
-HELIX   22  22 TYR A  424  ASN A  429  1                                   6    
-HELIX   23  23 TRP B   52  TYR B   55  5                                   4    
-HELIX   24  24 ASN B   60  LEU B   64  5                                   5    
-HELIX   25  25 PRO B   65  LEU B   69  5                                   5    
-HELIX   26  26 ASP B   90  ILE B   95  1                                   6    
-HELIX   27  27 TYR B  112  ASN B  125  1                                  14    
-HELIX   28  28 TYR B  139  PRO B  141  5                                   3    
-HELIX   29  29 ASN B  142  SER B  148  1                                   7    
-HELIX   30  30 THR B  149  GLY B  168  1                                  20    
-HELIX   31  31 ASN B  181  ALA B  207  1                                  27    
-HELIX   32  32 GLY B  221  LEU B  228  1                                   8    
-HELIX   33  33 HIS B  229  LEU B  237  1                                   9    
-HELIX   34  34 ASN B  267  THR B  271  5                                   5    
-HELIX   35  35 ASN B  274  GLY B  285  1                                  12    
-HELIX   36  36 PRO B  288  ASN B  290  5                                   3    
-HELIX   37  37 LYS B  329  LEU B  331  5                                   3    
-HELIX   38  38 PRO B  342  MET B  345  5                                   4    
-HELIX   39  39 ASN B  362  GLY B  377  1                                  16    
-HELIX   40  40 ASP B  385  ASP B  389  5                                   5    
-HELIX   41  41 THR B  391  ASP B  394  5                                   4    
-HELIX   42  42 SER B  395  GLY B  405  1                                  11    
-HELIX   43  43 GLY B  406  VAL B  409  5                                   4    
-HELIX   44  44 TYR B  424  ASN B  429  1                                   6    
-SHEET    1  AA11 ARG A  44  VAL A  50  0                                        
-SHEET    2  AA11 GLY A 380  TRP A 384  1  O  ALA A 381   N  VAL A  46           
-SHEET    3  AA11 ILE A 292  PRO A 297  1  O  LEU A 294   N  MET A 382           
-SHEET    4  AA11 PHE A 239  LEU A 242  1  O  TRP A 240   N  VAL A 293           
-SHEET    5  AA11 LEU A 213  SER A 218  1  O  VAL A 216   N  ASN A 241           
-SHEET    6  AA11 GLY A 171  ASP A 175  1  O  LEU A 172   N  THR A 215           
-SHEET    7  AA11 LYS A 129  GLY A 135  1  O  LEU A 132   N  ASP A 173           
-SHEET    8  AA11 HIS A  71  VAL A  79  4  O  VAL A  72   N  LEU A 131           
-SHEET    9  AA11 ARG A  44  VAL A  50  1  O  VAL A  47   N  LEU A  73           
-SHEET   10  AA11 GLY A 380  TRP A 384  1  O  ALA A 381   N  VAL A  46           
-SHEET   11  AA11 ARG A  44  VAL A  50  1  O  ARG A  44   N  ALA A 381           
-SHEET    1  AB 5 VAL A 325  ASP A 327  0                                        
-SHEET    2  AB 5 TYR A 299  PHE A 303 -1  O  GLY A 300   N  TRP A 326           
-SHEET    3  AB 5 PHE A 356  SER A 359 -1  O  LEU A 357   N  PHE A 303           
-SHEET    4  AB 5 ALA A 346  ASP A 351 -1  O  SER A 349   N  ILE A 358           
-SHEET    5  AB 5 THR A 337  LEU A 341 -1  O  THR A 337   N  TYR A 350           
-SHEET    1  BA10 ARG B  44  VAL B  50  0                                        
-SHEET    2  BA10 GLY B 380  TRP B 384  1  O  ALA B 381   N  VAL B  46           
-SHEET    3  BA10 ILE B 292  PRO B 297  1  O  LEU B 294   N  MET B 382           
-SHEET    4  BA10 PHE B 239  LEU B 242  1  O  TRP B 240   N  VAL B 293           
-SHEET    5  BA10 LEU B 213  SER B 218  1  O  VAL B 216   N  ASN B 241           
-SHEET    6  BA10 GLY B 171  ASP B 175  1  O  LEU B 172   N  THR B 215           
-SHEET    7  BA10 LYS B 129  GLY B 135  1  O  LEU B 132   N  ASP B 173           
-SHEET    8  BA10 HIS B  71  VAL B  79 18  O  VAL B  72   N  LEU B 131           
-SHEET    9  BA10 ARG B  44  VAL B  50  1  O  VAL B  47   N  LEU B  73           
-SHEET   10  BA10 ARG B  44  VAL B  50 15  N  VAL B  50   O  TYR B  48           
-SHEET    1  BB 5 VAL B 325  ASP B 327  0                                        
-SHEET    2  BB 5 TYR B 299  PHE B 303 -1  O  GLY B 300   N  TRP B 326           
-SHEET    3  BB 5 PHE B 356  SER B 359 -1  O  LEU B 357   N  PHE B 303           
-SHEET    4  BB 5 ALA B 346  ASP B 351 -1  O  SER B 349   N  ILE B 358           
-SHEET    5  BB 5 THR B 337  LEU B 341 -1  O  THR B 337   N  TYR B 350           
-CISPEP   1 ALA A   75    PHE A   76          0        -4.16                     
-CISPEP   2 GLU A  177    TYR A  178          0        -1.06                     
-CISPEP   3 LEU A  331    PRO A  332          0         0.02                     
-CISPEP   4 TRP A  384    ASP A  385          0        -5.43                     
-CISPEP   5 ALA B   75    PHE B   76          0        -0.24                     
-CISPEP   6 GLU B  177    TYR B  178          0        -0.91                     
-CISPEP   7 LEU B  331    PRO B  332          0        -0.25                     
-CISPEP   8 TRP B  384    ASP B  385          0       -10.07                     
-SITE     1 AC1  4 ARG A 126  GLN A 414  HOH A2442  SER B 103                    
-SITE     1 AC2  4 THR A 149  ASP A 150  HOH A2168  HOH A2457                    
-SITE     1 AC3  3 ASN A 181  ASP A 182  HOH A2458                               
-SITE     1 AC4  7 HIS A 229  LEU A 230  LYS A 231  ASP A 232                    
-SITE     2 AC4  7 HOH A2247  HOH A2459  HOH A2460                               
-SITE     1 AC5  3 ASN A 354  HOH A2461  HOH A2462                               
-SITE     1 AC6  7 LEU A 341  TYR A 348  HOH A2369  HOH A2463                    
-SITE     2 AC6  7 HOH A2464  PRO B  81  HOH B2137                               
-SITE     1 AC7  4 THR B 149  ASP B 150  HOH B2403  HOH B2404                    
-SITE     1 AC8  6 ASN A 323  GLU B 338  HIS B 339  HOH B2406                    
-SITE     2 AC8  6 HOH B2407  HOH B2408                                          
-SITE     1 AC9  2 ASN B 181  ASP B 182                                          
-SITE     1 BC1  5 ARG B 283  ALA B 289  HOH B2263  HOH B2409                    
-SITE     2 BC1  5 HOH B2410                                                     
-SITE     1 BC2  6 HIS B 229  LEU B 230  LYS B 231  ASP B 232                    
-SITE     2 BC2  6 HOH B2411  HOH B2412                                          
-SITE     1 BC3 12 TRP A  52  PHE A  76  GLY A 136  TRP A 137                    
-SITE     2 BC3 12 THR A 138  TYR A 139  ASP A 246  TYR A 299                    
-SITE     3 BC3 12 TRP A 384  HOH A2262  HOH A2465  HOH A2466                    
-SITE     1 BC4 16 GLN A 364  TRP B  52  PHE B  76  GLY B 136                    
-SITE     2 BC4 16 TRP B 137  THR B 138  TYR B 245  ASP B 246                    
-SITE     3 BC4 16 TYR B 299  TRP B 384  HOH B2005  HOH B2126                    
-SITE     4 BC4 16 HOH B2221  HOH B2291  HOH B2413  HOH B2415                    
-CRYST1  116.782  116.782   99.420  90.00  90.00  90.00 P 41          8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.008563  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.008563  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.010058        0.00000                         
-ATOM      1  N   ALA A  39      75.702  54.127  15.792  1.00 54.07           N  
-ATOM      2  CA  ALA A  39      75.898  53.812  17.243  1.00 53.00           C  
-ATOM      3  C   ALA A  39      75.952  55.088  18.087  1.00 52.37           C  
-ATOM      4  O   ALA A  39      75.206  55.208  19.062  1.00 53.13           O  
-ATOM      5  CB  ALA A  39      77.179  52.981  17.454  1.00 52.47           C  
-ATOM      6  N   SER A  40      76.828  56.031  17.725  1.00 49.06           N  
-ATOM      7  CA  SER A  40      76.943  57.303  18.456  1.00 46.72           C  
-ATOM      8  C   SER A  40      77.586  58.450  17.656  1.00 44.58           C  
-ATOM      9  O   SER A  40      78.356  58.229  16.727  1.00 41.59           O  
-ATOM     10  CB  SER A  40      77.703  57.105  19.781  1.00 47.03           C  
-ATOM     11  OG  SER A  40      79.023  56.634  19.594  1.00 47.11           O  
-ATOM     12  N   SER A  41      77.247  59.680  18.022  1.00 41.92           N  
-ATOM     13  CA  SER A  41      77.779  60.863  17.356  1.00 39.86           C  
-ATOM     14  C   SER A  41      79.201  61.141  17.835  1.00 37.28           C  
-ATOM     15  O   SER A  41      79.643  60.592  18.848  1.00 37.24           O  
-ATOM     16  CB  SER A  41      76.909  62.067  17.681  1.00 41.45           C  
-ATOM     17  OG  SER A  41      76.938  62.292  19.084  1.00 44.65           O  
-ATOM     18  N   GLY A  42      79.905  62.006  17.108  1.00 32.87           N  
-ATOM     19  CA  GLY A  42      81.275  62.346  17.457  1.00 27.74           C  
-ATOM     20  C   GLY A  42      81.996  62.861  16.220  1.00 25.49           C  
-ATOM     21  O   GLY A  42      81.369  63.109  15.173  1.00 22.27           O  
-ATOM     22  N   TYR A  43      83.311  63.013  16.319  1.00 20.67           N  
-ATOM     23  CA  TYR A  43      84.072  63.524  15.189  1.00 20.56           C  
-ATOM     24  C   TYR A  43      84.302  62.495  14.078  1.00 18.87           C  
-ATOM     25  O   TYR A  43      84.318  61.284  14.309  1.00 20.16           O  
-ATOM     26  CB  TYR A  43      85.426  64.063  15.670  1.00 20.20           C  
-ATOM     27  CG  TYR A  43      85.310  65.216  16.640  1.00 21.06           C  
-ATOM     28  CD1 TYR A  43      84.762  66.443  16.242  1.00 21.63           C  
-ATOM     29  CD2 TYR A  43      85.716  65.075  17.969  1.00 21.02           C  
-ATOM     30  CE1 TYR A  43      84.617  67.499  17.145  1.00 22.89           C  
-ATOM     31  CE2 TYR A  43      85.573  66.127  18.883  1.00 23.17           C  
-ATOM     32  CZ  TYR A  43      85.024  67.328  18.466  1.00 24.36           C  
-ATOM     33  OH  TYR A  43      84.857  68.363  19.365  1.00 25.48           O  
-ATOM     34  N   ARG A  44      84.447  62.991  12.859  1.00 16.87           N  
-ATOM     35  CA  ARG A  44      84.746  62.128  11.736  1.00 16.55           C  
-ATOM     36  C   ARG A  44      86.240  62.376  11.431  1.00 15.04           C  
-ATOM     37  O   ARG A  44      86.756  63.456  11.720  1.00 14.13           O  
-ATOM     38  CB  ARG A  44      83.902  62.522  10.526  1.00 16.32           C  
-ATOM     39  CG  ARG A  44      82.395  62.498  10.827  1.00 14.07           C  
-ATOM     40  CD  ARG A  44      81.608  63.068   9.663  1.00 17.86           C  
-ATOM     41  NE  ARG A  44      80.162  63.181   9.902  1.00 17.38           N  
-ATOM     42  CZ  ARG A  44      79.578  64.122  10.643  1.00 20.42           C  
-ATOM     43  NH1 ARG A  44      80.303  65.044  11.258  1.00 21.00           N  
-ATOM     44  NH2 ARG A  44      78.248  64.200  10.695  1.00 20.31           N  
-ATOM     45  N   SER A  45      86.913  61.381  10.854  1.00 15.55           N  
-ATOM     46  CA  SER A  45      88.334  61.476  10.476  1.00 14.77           C  
-ATOM     47  C   SER A  45      88.289  60.933   9.053  1.00 14.47           C  
-ATOM     48  O   SER A  45      88.163  59.722   8.834  1.00 14.47           O  
-ATOM     49  CB  SER A  45      89.206  60.581  11.357  1.00 16.94           C  
-ATOM     50  OG  SER A  45      90.556  60.691  10.930  1.00 15.11           O  
-ATOM     51  N   VAL A  46      88.420  61.855   8.105  1.00 14.10           N  
-ATOM     52  CA  VAL A  46      88.240  61.588   6.689  1.00 12.79           C  
-ATOM     53  C   VAL A  46      89.471  61.783   5.847  1.00 13.76           C  
-ATOM     54  O   VAL A  46      90.155  62.790   5.976  1.00 15.93           O  
-ATOM     55  CB  VAL A  46      87.125  62.556   6.153  1.00 14.06           C  
-ATOM     56  CG1 VAL A  46      86.735  62.235   4.692  1.00 12.79           C  
-ATOM     57  CG2 VAL A  46      85.919  62.478   7.085  1.00 14.06           C  
-ATOM     58  N   VAL A  47      89.767  60.841   4.965  1.00 14.74           N  
-ATOM     59  CA  VAL A  47      90.933  61.080   4.130  1.00 13.58           C  
-ATOM     60  C   VAL A  47      90.707  60.595   2.708  1.00 13.38           C  
-ATOM     61  O   VAL A  47      89.999  59.619   2.454  1.00 14.90           O  
-ATOM     62  CB  VAL A  47      92.215  60.402   4.721  1.00 13.59           C  
-ATOM     63  CG1 VAL A  47      92.147  58.879   4.536  1.00 11.72           C  
-ATOM     64  CG2 VAL A  47      93.466  60.965   4.035  1.00 11.29           C  
-ATOM     65  N   TYR A  48      91.308  61.318   1.776  1.00 14.53           N  
-ATOM     66  CA  TYR A  48      91.220  60.935   0.402  1.00 14.04           C  
-ATOM     67  C   TYR A  48      92.316  59.942   0.106  1.00 15.59           C  
-ATOM     68  O   TYR A  48      93.474  60.153   0.509  1.00 14.40           O  
-ATOM     69  CB  TYR A  48      91.437  62.135  -0.527  1.00 14.46           C  
-ATOM     70  CG  TYR A  48      90.211  62.977  -0.754  1.00 14.28           C  
-ATOM     71  CD1 TYR A  48      89.940  64.079   0.052  1.00 14.89           C  
-ATOM     72  CD2 TYR A  48      89.316  62.659  -1.774  1.00 14.24           C  
-ATOM     73  CE1 TYR A  48      88.808  64.851  -0.154  1.00 16.90           C  
-ATOM     74  CE2 TYR A  48      88.186  63.416  -1.991  1.00 14.59           C  
-ATOM     75  CZ  TYR A  48      87.942  64.509  -1.180  1.00 13.37           C  
-ATOM     76  OH  TYR A  48      86.843  65.263  -1.392  1.00 16.82           O  
-ATOM     77  N   PHE A  49      91.943  58.841  -0.541  1.00 14.39           N  
-ATOM     78  CA  PHE A  49      92.923  57.878  -1.034  1.00 15.34           C  
-ATOM     79  C   PHE A  49      92.723  58.021  -2.554  1.00 16.66           C  
-ATOM     80  O   PHE A  49      91.609  57.781  -3.062  1.00 15.20           O  
-ATOM     81  CB  PHE A  49      92.633  56.428  -0.643  1.00 15.88           C  
-ATOM     82  CG  PHE A  49      93.600  55.474  -1.274  1.00 16.62           C  
-ATOM     83  CD1 PHE A  49      93.388  54.996  -2.579  1.00 15.27           C  
-ATOM     84  CD2 PHE A  49      94.804  55.171  -0.627  1.00 13.94           C  
-ATOM     85  CE1 PHE A  49      94.365  54.240  -3.233  1.00 16.34           C  
-ATOM     86  CE2 PHE A  49      95.784  54.417  -1.265  1.00 13.96           C  
-ATOM     87  CZ  PHE A  49      95.576  53.945  -2.579  1.00 15.09           C  
-ATOM     88  N   VAL A  50      93.760  58.439  -3.277  1.00 14.08           N  
-ATOM     89  CA  VAL A  50      93.634  58.660  -4.730  1.00 12.26           C  
-ATOM     90  C   VAL A  50      94.206  57.500  -5.478  1.00 14.92           C  
-ATOM     91  O   VAL A  50      95.362  57.075  -5.237  1.00 15.14           O  
-ATOM     92  CB  VAL A  50      94.298  59.998  -5.139  1.00 14.42           C  
-ATOM     93  CG1 VAL A  50      93.668  61.099  -4.326  1.00 12.96           C  
-ATOM     94  CG2 VAL A  50      95.807  60.001  -4.842  1.00 13.50           C  
-ATOM     95  N   ASN A  51      93.422  56.986  -6.414  1.00 14.64           N  
-ATOM     96  CA  ASN A  51      93.863  55.777  -7.069  1.00 15.04           C  
-ATOM     97  C   ASN A  51      95.184  55.840  -7.818  1.00 16.28           C  
-ATOM     98  O   ASN A  51      95.796  54.792  -8.028  1.00 18.37           O  
-ATOM     99  CB  ASN A  51      92.718  55.146  -7.908  1.00 15.46           C  
-ATOM    100  CG  ASN A  51      92.369  55.908  -9.175  1.00 20.49           C  
-ATOM    101  OD1 ASN A  51      92.934  56.955  -9.493  1.00 21.03           O  
-ATOM    102  ND2 ASN A  51      91.392  55.358  -9.922  1.00 22.21           N  
-ATOM    103  N   TRP A  52      95.660  57.037  -8.175  1.00 14.65           N  
-ATOM    104  CA  TRP A  52      96.965  57.136  -8.854  1.00 14.82           C  
-ATOM    105  C   TRP A  52      98.125  57.130  -7.840  1.00 17.19           C  
-ATOM    106  O   TRP A  52      99.285  57.213  -8.225  1.00 16.41           O  
-ATOM    107  CB  TRP A  52      97.032  58.401  -9.715  1.00 15.36           C  
-ATOM    108  CG  TRP A  52      96.787  59.690  -8.970  1.00 14.76           C  
-ATOM    109  CD1 TRP A  52      97.725  60.493  -8.392  1.00 16.56           C  
-ATOM    110  CD2 TRP A  52      95.516  60.331  -8.748  1.00 16.75           C  
-ATOM    111  NE1 TRP A  52      97.124  61.604  -7.830  1.00 17.63           N  
-ATOM    112  CE2 TRP A  52      95.770  61.527  -8.035  1.00 18.75           C  
-ATOM    113  CE3 TRP A  52      94.191  60.006  -9.083  1.00 19.12           C  
-ATOM    114  CZ2 TRP A  52      94.751  62.408  -7.649  1.00 17.63           C  
-ATOM    115  CZ3 TRP A  52      93.167  60.882  -8.699  1.00 19.54           C  
-ATOM    116  CH2 TRP A  52      93.462  62.075  -7.987  1.00 20.15           C  
-ATOM    117  N   ALA A  53      97.804  57.033  -6.549  1.00 15.21           N  
-ATOM    118  CA  ALA A  53      98.824  57.015  -5.503  1.00 15.06           C  
-ATOM    119  C   ALA A  53      99.633  55.727  -5.542  1.00 14.49           C  
-ATOM    120  O   ALA A  53     100.747  55.657  -5.009  1.00 16.16           O  
-ATOM    121  CB  ALA A  53      98.160  57.173  -4.111  1.00 13.36           C  
-ATOM    122  N   ILE A  54      99.080  54.696  -6.171  1.00 16.02           N  
-ATOM    123  CA  ILE A  54      99.801  53.434  -6.236  1.00 14.14           C  
-ATOM    124  C   ILE A  54     100.975  53.471  -7.229  1.00 14.90           C  
-ATOM    125  O   ILE A  54     101.786  52.542  -7.289  1.00 15.86           O  
-ATOM    126  CB  ILE A  54      98.873  52.265  -6.641  1.00 14.41           C  
-ATOM    127  CG1 ILE A  54      98.507  52.386  -8.113  1.00 15.71           C  
-ATOM    128  CG2 ILE A  54      97.585  52.252  -5.762  1.00 16.86           C  
-ATOM    129  CD1 ILE A  54      97.625  51.210  -8.608  1.00 17.37           C  
-ATOM    130  N   TYR A  55     101.068  54.530  -8.015  1.00 14.38           N  
-ATOM    131  CA  TYR A  55     102.138  54.584  -8.999  1.00 15.52           C  
-ATOM    132  C   TYR A  55     103.391  55.247  -8.417  1.00 15.95           C  
-ATOM    133  O   TYR A  55     104.046  54.668  -7.550  1.00 16.33           O  
-ATOM    134  CB  TYR A  55     101.615  55.317 -10.231  1.00 13.67           C  
-ATOM    135  CG  TYR A  55     100.445  54.575 -10.868  1.00 17.24           C  
-ATOM    136  CD1 TYR A  55     100.603  53.282 -11.375  1.00 16.86           C  
-ATOM    137  CD2 TYR A  55      99.181  55.162 -10.955  1.00 15.36           C  
-ATOM    138  CE1 TYR A  55      99.523  52.595 -11.956  1.00 18.01           C  
-ATOM    139  CE2 TYR A  55      98.110  54.485 -11.534  1.00 16.73           C  
-ATOM    140  CZ  TYR A  55      98.282  53.203 -12.034  1.00 17.31           C  
-ATOM    141  OH  TYR A  55      97.195  52.552 -12.631  1.00 17.86           O  
-ATOM    142  N   GLY A  56     103.705  56.461  -8.868  1.00 16.22           N  
-ATOM    143  CA  GLY A  56     104.887  57.150  -8.370  1.00 16.16           C  
-ATOM    144  C   GLY A  56     104.948  57.302  -6.862  1.00 18.13           C  
-ATOM    145  O   GLY A  56     106.018  57.158  -6.257  1.00 16.49           O  
-ATOM    146  N   ARG A  57     103.814  57.625  -6.247  1.00 15.28           N  
-ATOM    147  CA  ARG A  57     103.783  57.784  -4.806  1.00 14.58           C  
-ATOM    148  C   ARG A  57     103.944  56.451  -4.076  1.00 13.98           C  
-ATOM    149  O   ARG A  57     104.132  56.441  -2.866  1.00 14.66           O  
-ATOM    150  CB  ARG A  57     102.474  58.467  -4.374  1.00 13.56           C  
-ATOM    151  CG  ARG A  57     102.354  59.904  -4.843  1.00 15.45           C  
-ATOM    152  CD  ARG A  57     100.895  60.406  -4.716  1.00 14.60           C  
-ATOM    153  NE  ARG A  57     100.777  61.841  -4.975  1.00 15.22           N  
-ATOM    154  CZ  ARG A  57     100.795  62.390  -6.190  1.00 16.87           C  
-ATOM    155  NH1 ARG A  57     100.930  61.619  -7.258  1.00 13.95           N  
-ATOM    156  NH2 ARG A  57     100.664  63.708  -6.340  1.00 16.68           N  
-ATOM    157  N   ASN A  58     103.836  55.333  -4.792  1.00 12.82           N  
-ATOM    158  CA  ASN A  58     104.029  54.003  -4.176  1.00 15.26           C  
-ATOM    159  C   ASN A  58     103.248  53.847  -2.881  1.00 17.46           C  
-ATOM    160  O   ASN A  58     103.744  53.271  -1.904  1.00 18.34           O  
-ATOM    161  CB  ASN A  58     105.543  53.766  -3.927  1.00 15.36           C  
-ATOM    162  CG  ASN A  58     105.857  52.359  -3.456  1.00 14.09           C  
-ATOM    163  OD1 ASN A  58     105.273  51.394  -3.937  1.00 18.90           O  
-ATOM    164  ND2 ASN A  58     106.783  52.236  -2.500  1.00 13.31           N  
-ATOM    165  N   HIS A  59     102.009  54.345  -2.901  1.00 17.01           N  
-ATOM    166  CA  HIS A  59     101.108  54.333  -1.748  1.00 16.27           C  
-ATOM    167  C   HIS A  59      99.889  53.471  -2.075  1.00 15.78           C  
-ATOM    168  O   HIS A  59      99.213  53.709  -3.077  1.00 14.14           O  
-ATOM    169  CB  HIS A  59     100.674  55.779  -1.473  1.00 15.46           C  
-ATOM    170  CG  HIS A  59      99.705  55.932  -0.340  1.00 14.49           C  
-ATOM    171  ND1 HIS A  59     100.037  55.671   0.977  1.00 13.67           N  
-ATOM    172  CD2 HIS A  59      98.432  56.393  -0.320  1.00 12.19           C  
-ATOM    173  CE1 HIS A  59      99.012  55.976   1.755  1.00 16.44           C  
-ATOM    174  NE2 HIS A  59      98.028  56.419   0.995  1.00 14.81           N  
-ATOM    175  N   ASN A  60      99.609  52.487  -1.221  1.00 15.86           N  
-ATOM    176  CA  ASN A  60      98.487  51.560  -1.439  1.00 15.41           C  
-ATOM    177  C   ASN A  60      97.507  51.579  -0.264  1.00 14.69           C  
-ATOM    178  O   ASN A  60      97.843  52.075   0.826  1.00 15.33           O  
-ATOM    179  CB  ASN A  60      99.034  50.143  -1.689  1.00 13.41           C  
-ATOM    180  CG  ASN A  60      99.865  50.079  -2.981  1.00 17.57           C  
-ATOM    181  OD1 ASN A  60      99.326  49.877  -4.070  1.00 15.47           O  
-ATOM    182  ND2 ASN A  60     101.179  50.306  -2.855  1.00 13.95           N  
-ATOM    183  N   PRO A  61      96.285  51.037  -0.457  1.00 14.40           N  
-ATOM    184  CA  PRO A  61      95.311  51.052   0.645  1.00 15.76           C  
-ATOM    185  C   PRO A  61      95.828  50.500   1.957  1.00 16.68           C  
-ATOM    186  O   PRO A  61      95.522  51.042   3.035  1.00 15.60           O  
-ATOM    187  CB  PRO A  61      94.133  50.250   0.078  1.00 15.12           C  
-ATOM    188  CG  PRO A  61      94.180  50.641  -1.414  1.00 14.69           C  
-ATOM    189  CD  PRO A  61      95.681  50.476  -1.685  1.00 14.25           C  
-ATOM    190  N   GLN A  62      96.603  49.419   1.860  1.00 16.10           N  
-ATOM    191  CA  GLN A  62      97.180  48.784   3.036  1.00 17.44           C  
-ATOM    192  C   GLN A  62      97.986  49.760   3.890  1.00 19.26           C  
-ATOM    193  O   GLN A  62      98.249  49.470   5.054  1.00 17.00           O  
-ATOM    194  CB  GLN A  62      98.104  47.623   2.640  1.00 21.51           C  
-ATOM    195  CG  GLN A  62      97.414  46.474   1.915  1.00 22.82           C  
-ATOM    196  CD  GLN A  62      97.504  46.614   0.397  1.00 24.94           C  
-ATOM    197  OE1 GLN A  62      97.122  47.639  -0.170  1.00 21.00           O  
-ATOM    198  NE2 GLN A  62      98.017  45.581  -0.262  1.00 25.81           N  
-ATOM    199  N   ASP A  63      98.406  50.892   3.319  1.00 17.19           N  
-ATOM    200  CA  ASP A  63      99.190  51.887   4.072  1.00 17.40           C  
-ATOM    201  C   ASP A  63      98.280  52.854   4.823  1.00 17.47           C  
-ATOM    202  O   ASP A  63      98.762  53.677   5.610  1.00 15.50           O  
-ATOM    203  CB  ASP A  63     100.053  52.742   3.135  1.00 19.11           C  
-ATOM    204  CG  ASP A  63     101.071  51.922   2.362  1.00 19.56           C  
-ATOM    205  OD1 ASP A  63     101.757  51.120   3.009  1.00 18.58           O  
-ATOM    206  OD2 ASP A  63     101.184  52.084   1.128  1.00 20.37           O  
-ATOM    207  N   LEU A  64      96.972  52.784   4.584  1.00 15.25           N  
-ATOM    208  CA  LEU A  64      96.077  53.736   5.261  1.00 14.32           C  
-ATOM    209  C   LEU A  64      96.047  53.494   6.773  1.00 16.99           C  
-ATOM    210  O   LEU A  64      96.119  52.355   7.228  1.00 16.89           O  
-ATOM    211  CB  LEU A  64      94.647  53.624   4.695  1.00 14.91           C  
-ATOM    212  CG  LEU A  64      94.425  54.164   3.279  1.00 13.58           C  
-ATOM    213  CD1 LEU A  64      93.111  53.599   2.689  1.00 12.13           C  
-ATOM    214  CD2 LEU A  64      94.372  55.696   3.336  1.00 15.58           C  
-ATOM    215  N   PRO A  65      95.958  54.573   7.572  1.00 17.08           N  
-ATOM    216  CA  PRO A  65      95.916  54.412   9.037  1.00 17.02           C  
-ATOM    217  C   PRO A  65      94.452  54.128   9.446  1.00 19.65           C  
-ATOM    218  O   PRO A  65      93.819  54.917  10.141  1.00 16.94           O  
-ATOM    219  CB  PRO A  65      96.433  55.764   9.535  1.00 16.15           C  
-ATOM    220  CG  PRO A  65      95.835  56.725   8.517  1.00 15.38           C  
-ATOM    221  CD  PRO A  65      96.090  55.997   7.191  1.00 16.69           C  
-ATOM    222  N   VAL A  66      93.933  52.979   9.019  1.00 19.66           N  
-ATOM    223  CA  VAL A  66      92.527  52.648   9.253  1.00 19.94           C  
-ATOM    224  C   VAL A  66      91.998  52.756  10.667  1.00 21.64           C  
-ATOM    225  O   VAL A  66      90.810  53.054  10.875  1.00 20.15           O  
-ATOM    226  CB  VAL A  66      92.180  51.248   8.692  1.00 21.67           C  
-ATOM    227  CG1 VAL A  66      92.285  51.299   7.191  1.00 23.33           C  
-ATOM    228  CG2 VAL A  66      93.127  50.190   9.267  1.00 25.37           C  
-ATOM    229  N   GLU A  67      92.848  52.544  11.659  1.00 22.36           N  
-ATOM    230  CA  GLU A  67      92.324  52.655  13.014  1.00 23.53           C  
-ATOM    231  C   GLU A  67      92.063  54.096  13.404  1.00 22.14           C  
-ATOM    232  O   GLU A  67      91.304  54.362  14.322  1.00 22.67           O  
-ATOM    233  CB  GLU A  67      93.279  51.998  13.999  1.00 29.64           C  
-ATOM    234  CG  GLU A  67      93.265  50.477  13.841  1.00 38.68           C  
-ATOM    235  CD  GLU A  67      91.840  49.908  13.920  1.00 44.90           C  
-ATOM    236  OE1 GLU A  67      91.543  48.943  13.172  1.00 47.25           O  
-ATOM    237  OE2 GLU A  67      91.021  50.421  14.730  1.00 47.66           O  
-ATOM    238  N   ARG A  68      92.641  55.032  12.662  1.00 18.41           N  
-ATOM    239  CA  ARG A  68      92.491  56.453  12.989  1.00 17.11           C  
-ATOM    240  C   ARG A  68      91.578  57.216  12.052  1.00 18.99           C  
-ATOM    241  O   ARG A  68      91.578  58.450  12.030  1.00 19.65           O  
-ATOM    242  CB  ARG A  68      93.881  57.096  12.984  1.00 19.81           C  
-ATOM    243  CG  ARG A  68      94.812  56.527  14.070  1.00 23.99           C  
-ATOM    244  CD  ARG A  68      96.150  57.279  14.142  1.00 25.58           C  
-ATOM    245  NE  ARG A  68      97.019  56.956  13.018  1.00 29.71           N  
-ATOM    246  CZ  ARG A  68      97.829  55.909  12.982  1.00 30.11           C  
-ATOM    247  NH1 ARG A  68      97.875  55.085  14.014  1.00 32.97           N  
-ATOM    248  NH2 ARG A  68      98.616  55.704  11.931  1.00 31.00           N  
-ATOM    249  N   LEU A  69      90.799  56.479  11.277  1.00 16.49           N  
-ATOM    250  CA  LEU A  69      89.909  57.090  10.300  1.00 14.93           C  
-ATOM    251  C   LEU A  69      88.492  56.563  10.465  1.00 17.56           C  
-ATOM    252  O   LEU A  69      88.295  55.439  10.944  1.00 14.96           O  
-ATOM    253  CB  LEU A  69      90.377  56.695   8.899  1.00 16.07           C  
-ATOM    254  CG  LEU A  69      91.769  57.129   8.419  1.00 14.09           C  
-ATOM    255  CD1 LEU A  69      92.176  56.320   7.192  1.00 13.69           C  
-ATOM    256  CD2 LEU A  69      91.719  58.606   8.080  1.00 11.62           C  
-ATOM    257  N   THR A  70      87.515  57.381  10.073  1.00 15.65           N  
-ATOM    258  CA  THR A  70      86.138  56.936  10.082  1.00 16.22           C  
-ATOM    259  C   THR A  70      85.698  56.800   8.600  1.00 17.15           C  
-ATOM    260  O   THR A  70      84.823  55.961   8.288  1.00 18.52           O  
-ATOM    261  CB  THR A  70      85.217  57.945  10.795  1.00 15.00           C  
-ATOM    262  OG1 THR A  70      85.385  59.260  10.220  1.00 13.75           O  
-ATOM    263  CG2 THR A  70      85.544  57.969  12.296  1.00 15.41           C  
-ATOM    264  N   HIS A  71      86.324  57.584   7.702  1.00 15.36           N  
-ATOM    265  CA  HIS A  71      85.966  57.568   6.283  1.00 16.00           C  
-ATOM    266  C   HIS A  71      87.110  57.698   5.286  1.00 16.33           C  
-ATOM    267  O   HIS A  71      87.959  58.545   5.446  1.00 16.89           O  
-ATOM    268  CB  HIS A  71      85.012  58.736   5.963  1.00 15.02           C  
-ATOM    269  CG  HIS A  71      83.750  58.774   6.785  1.00 18.14           C  
-ATOM    270  ND1 HIS A  71      83.695  59.260   8.077  1.00 16.83           N  
-ATOM    271  CD2 HIS A  71      82.489  58.381   6.480  1.00 16.43           C  
-ATOM    272  CE1 HIS A  71      82.456  59.150   8.532  1.00 16.59           C  
-ATOM    273  NE2 HIS A  71      81.704  58.617   7.586  1.00 14.40           N  
-ATOM    274  N   VAL A  72      87.117  56.853   4.267  1.00 15.00           N  
-ATOM    275  CA  VAL A  72      88.102  56.966   3.201  1.00 15.38           C  
-ATOM    276  C   VAL A  72      87.313  57.386   1.946  1.00 15.23           C  
-ATOM    277  O   VAL A  72      86.275  56.787   1.644  1.00 16.09           O  
-ATOM    278  CB  VAL A  72      88.776  55.631   2.889  1.00 16.93           C  
-ATOM    279  CG1 VAL A  72      89.638  55.793   1.641  1.00 14.14           C  
-ATOM    280  CG2 VAL A  72      89.620  55.156   4.092  1.00 15.89           C  
-ATOM    281  N   LEU A  73      87.779  58.417   1.240  1.00 15.42           N  
-ATOM    282  CA  LEU A  73      87.126  58.867   0.000  1.00 15.13           C  
-ATOM    283  C   LEU A  73      88.029  58.348  -1.127  1.00 16.91           C  
-ATOM    284  O   LEU A  73      89.161  58.790  -1.280  1.00 15.46           O  
-ATOM    285  CB  LEU A  73      87.020  60.403  -0.047  1.00 14.09           C  
-ATOM    286  CG  LEU A  73      86.376  60.992   1.229  1.00 16.12           C  
-ATOM    287  CD1 LEU A  73      86.234  62.493   1.108  1.00 15.41           C  
-ATOM    288  CD2 LEU A  73      85.003  60.337   1.469  1.00 16.95           C  
-ATOM    289  N   TYR A  74      87.531  57.380  -1.891  1.00 16.70           N  
-ATOM    290  CA  TYR A  74      88.308  56.802  -2.975  1.00 16.09           C  
-ATOM    291  C   TYR A  74      88.102  57.625  -4.244  1.00 18.02           C  
-ATOM    292  O   TYR A  74      87.029  57.605  -4.851  1.00 19.03           O  
-ATOM    293  CB  TYR A  74      87.869  55.366  -3.198  1.00 18.54           C  
-ATOM    294  CG  TYR A  74      88.737  54.635  -4.174  1.00 16.50           C  
-ATOM    295  CD1 TYR A  74      90.030  54.240  -3.823  1.00 17.38           C  
-ATOM    296  CD2 TYR A  74      88.253  54.299  -5.437  1.00 18.53           C  
-ATOM    297  CE1 TYR A  74      90.820  53.509  -4.705  1.00 17.67           C  
-ATOM    298  CE2 TYR A  74      89.036  53.575  -6.338  1.00 18.27           C  
-ATOM    299  CZ  TYR A  74      90.307  53.182  -5.961  1.00 15.31           C  
-ATOM    300  OH  TYR A  74      91.043  52.458  -6.836  1.00 14.41           O  
-ATOM    301  N   ALA A  75      89.149  58.348  -4.636  1.00 18.10           N  
-ATOM    302  CA  ALA A  75      89.109  59.253  -5.786  1.00 18.79           C  
-ATOM    303  C   ALA A  75      89.848  58.729  -7.019  1.00 18.53           C  
-ATOM    304  O   ALA A  75      90.920  58.139  -6.876  1.00 18.65           O  
-ATOM    305  CB  ALA A  75      89.711  60.583  -5.366  1.00 16.45           C  
-ATOM    306  N   PHE A  76      89.325  58.983  -8.224  1.00 19.11           N  
-ATOM    307  CA  PHE A  76      88.031  59.662  -8.481  1.00 17.97           C  
-ATOM    308  C   PHE A  76      87.320  58.873  -9.592  1.00 20.51           C  
-ATOM    309  O   PHE A  76      87.984  58.303 -10.471  1.00 19.01           O  
-ATOM    310  CB  PHE A  76      88.220  61.066  -9.083  1.00 18.02           C  
-ATOM    311  CG  PHE A  76      88.467  62.157  -8.082  1.00 18.61           C  
-ATOM    312  CD1 PHE A  76      87.530  62.424  -7.089  1.00 16.63           C  
-ATOM    313  CD2 PHE A  76      89.627  62.935  -8.144  1.00 18.52           C  
-ATOM    314  CE1 PHE A  76      87.731  63.445  -6.175  1.00 17.25           C  
-ATOM    315  CE2 PHE A  76      89.847  63.975  -7.220  1.00 19.31           C  
-ATOM    316  CZ  PHE A  76      88.892  64.230  -6.231  1.00 18.42           C  
-ATOM    317  N   ALA A  77      85.989  58.834  -9.557  1.00 18.62           N  
-ATOM    318  CA  ALA A  77      85.222  58.231 -10.645  1.00 18.29           C  
-ATOM    319  C   ALA A  77      84.948  59.472 -11.499  1.00 18.02           C  
-ATOM    320  O   ALA A  77      84.975  60.603 -10.982  1.00 17.62           O  
-ATOM    321  CB  ALA A  77      83.887  57.643 -10.150  1.00 17.54           C  
-ATOM    322  N   ASN A  78      84.716  59.273 -12.795  1.00 17.32           N  
-ATOM    323  CA  ASN A  78      84.448  60.379 -13.712  1.00 17.75           C  
-ATOM    324  C   ASN A  78      82.959  60.293 -14.090  1.00 19.70           C  
-ATOM    325  O   ASN A  78      82.270  59.343 -13.693  1.00 20.23           O  
-ATOM    326  CB  ASN A  78      85.300  60.236 -14.985  1.00 17.60           C  
-ATOM    327  CG  ASN A  78      85.379  61.538 -15.807  1.00 21.68           C  
-ATOM    328  OD1 ASN A  78      84.688  62.524 -15.518  1.00 21.63           O  
-ATOM    329  ND2 ASN A  78      86.232  61.538 -16.837  1.00 21.59           N  
-ATOM    330  N   VAL A  79      82.491  61.271 -14.864  1.00 19.21           N  
-ATOM    331  CA  VAL A  79      81.099  61.347 -15.293  1.00 23.86           C  
-ATOM    332  C   VAL A  79      80.976  61.670 -16.785  1.00 24.15           C  
-ATOM    333  O   VAL A  79      81.648  62.561 -17.285  1.00 24.65           O  
-ATOM    334  CB  VAL A  79      80.345  62.459 -14.536  1.00 22.37           C  
-ATOM    335  CG1 VAL A  79      78.868  62.417 -14.891  1.00 25.41           C  
-ATOM    336  CG2 VAL A  79      80.529  62.281 -13.035  1.00 28.21           C  
-ATOM    337  N   ARG A  80      80.126  60.927 -17.485  1.00 25.82           N  
-ATOM    338  CA  ARG A  80      79.887  61.149 -18.916  1.00 27.56           C  
-ATOM    339  C   ARG A  80      78.951  62.346 -19.018  1.00 27.83           C  
-ATOM    340  O   ARG A  80      77.793  62.285 -18.593  1.00 28.12           O  
-ATOM    341  CB  ARG A  80      79.265  59.898 -19.520  1.00 28.49           C  
-ATOM    342  CG  ARG A  80      80.275  58.787 -19.702  1.00 34.91           C  
-ATOM    343  CD  ARG A  80      80.768  58.779 -21.139  1.00 41.03           C  
-ATOM    344  NE  ARG A  80      82.170  58.394 -21.280  1.00 45.49           N  
-ATOM    345  CZ  ARG A  80      82.685  57.230 -20.894  1.00 47.23           C  
-ATOM    346  NH1 ARG A  80      81.916  56.307 -20.322  1.00 49.71           N  
-ATOM    347  NH2 ARG A  80      83.974  56.985 -21.096  1.00 48.41           N  
-ATOM    348  N   PRO A  81      79.446  63.460 -19.572  1.00 28.14           N  
-ATOM    349  CA  PRO A  81      78.646  64.673 -19.705  1.00 29.85           C  
-ATOM    350  C   PRO A  81      77.378  64.535 -20.523  1.00 31.82           C  
-ATOM    351  O   PRO A  81      76.404  65.251 -20.289  1.00 29.05           O  
-ATOM    352  CB  PRO A  81      79.623  65.668 -20.311  1.00 28.78           C  
-ATOM    353  CG  PRO A  81      80.517  64.797 -21.132  1.00 31.01           C  
-ATOM    354  CD  PRO A  81      80.754  63.616 -20.228  1.00 29.23           C  
-ATOM    355  N   GLU A  82      77.369  63.602 -21.463  1.00 33.18           N  
-ATOM    356  CA  GLU A  82      76.193  63.453 -22.302  1.00 34.19           C  
-ATOM    357  C   GLU A  82      75.153  62.492 -21.773  1.00 32.36           C  
-ATOM    358  O   GLU A  82      73.981  62.589 -22.135  1.00 34.64           O  
-ATOM    359  CB  GLU A  82      76.619  63.031 -23.708  1.00 37.26           C  
-ATOM    360  CG  GLU A  82      77.434  64.093 -24.419  1.00 40.58           C  
-ATOM    361  CD  GLU A  82      76.736  65.455 -24.396  1.00 46.68           C  
-ATOM    362  OE1 GLU A  82      75.545  65.531 -24.795  1.00 47.44           O  
-ATOM    363  OE2 GLU A  82      77.380  66.449 -23.973  1.00 48.09           O  
-ATOM    364  N   THR A  83      75.564  61.584 -20.901  1.00 28.39           N  
-ATOM    365  CA  THR A  83      74.654  60.581 -20.367  1.00 26.96           C  
-ATOM    366  C   THR A  83      74.480  60.583 -18.846  1.00 27.05           C  
-ATOM    367  O   THR A  83      73.545  59.962 -18.322  1.00 27.05           O  
-ATOM    368  CB  THR A  83      75.131  59.177 -20.756  1.00 26.00           C  
-ATOM    369  OG1 THR A  83      76.344  58.877 -20.052  1.00 24.62           O  
-ATOM    370  CG2 THR A  83      75.404  59.112 -22.243  1.00 28.01           C  
-ATOM    371  N   GLY A  84      75.387  61.247 -18.139  1.00 25.60           N  
-ATOM    372  CA  GLY A  84      75.305  61.265 -16.689  1.00 24.36           C  
-ATOM    373  C   GLY A  84      75.949  60.025 -16.081  1.00 24.64           C  
-ATOM    374  O   GLY A  84      76.057  59.923 -14.866  1.00 25.96           O  
-ATOM    375  N   GLU A  85      76.381  59.077 -16.908  1.00 22.60           N  
-ATOM    376  CA  GLU A  85      77.000  57.858 -16.384  1.00 23.05           C  
-ATOM    377  C   GLU A  85      78.255  58.124 -15.552  1.00 21.94           C  
-ATOM    378  O   GLU A  85      79.135  58.870 -15.959  1.00 23.71           O  
-ATOM    379  CB  GLU A  85      77.386  56.897 -17.515  1.00 23.89           C  
-ATOM    380  CG  GLU A  85      78.231  55.743 -17.019  1.00 25.79           C  
-ATOM    381  CD  GLU A  85      78.797  54.893 -18.143  1.00 31.49           C  
-ATOM    382  OE1 GLU A  85      78.974  55.415 -19.264  1.00 33.18           O  
-ATOM    383  OE2 GLU A  85      79.086  53.709 -17.898  1.00 32.56           O  
-ATOM    384  N   VAL A  86      78.327  57.481 -14.396  1.00 22.93           N  
-ATOM    385  CA  VAL A  86      79.481  57.591 -13.497  1.00 21.46           C  
-ATOM    386  C   VAL A  86      80.309  56.345 -13.741  1.00 21.15           C  
-ATOM    387  O   VAL A  86      79.775  55.234 -13.813  1.00 22.69           O  
-ATOM    388  CB  VAL A  86      79.020  57.654 -12.013  1.00 21.62           C  
-ATOM    389  CG1 VAL A  86      80.230  57.538 -11.037  1.00 21.17           C  
-ATOM    390  CG2 VAL A  86      78.287  58.979 -11.796  1.00 19.74           C  
-ATOM    391  N   TYR A  87      81.614  56.508 -13.908  1.00 19.38           N  
-ATOM    392  CA  TYR A  87      82.436  55.345 -14.148  1.00 19.13           C  
-ATOM    393  C   TYR A  87      83.844  55.430 -13.529  1.00 19.59           C  
-ATOM    394  O   TYR A  87      84.384  56.526 -13.292  1.00 20.73           O  
-ATOM    395  CB  TYR A  87      82.517  55.099 -15.656  1.00 19.19           C  
-ATOM    396  CG  TYR A  87      83.135  56.226 -16.420  1.00 20.50           C  
-ATOM    397  CD1 TYR A  87      82.436  57.415 -16.656  1.00 20.07           C  
-ATOM    398  CD2 TYR A  87      84.428  56.102 -16.929  1.00 25.54           C  
-ATOM    399  CE1 TYR A  87      83.012  58.458 -17.391  1.00 17.89           C  
-ATOM    400  CE2 TYR A  87      85.012  57.131 -17.662  1.00 22.95           C  
-ATOM    401  CZ  TYR A  87      84.310  58.298 -17.891  1.00 23.60           C  
-ATOM    402  OH  TYR A  87      84.935  59.287 -18.615  1.00 22.86           O  
-ATOM    403  N   MET A  88      84.418  54.263 -13.256  1.00 22.53           N  
-ATOM    404  CA  MET A  88      85.756  54.183 -12.657  1.00 23.60           C  
-ATOM    405  C   MET A  88      86.740  54.572 -13.729  1.00 24.27           C  
-ATOM    406  O   MET A  88      86.544  54.264 -14.896  1.00 26.27           O  
-ATOM    407  CB  MET A  88      86.012  52.776 -12.152  1.00 21.97           C  
-ATOM    408  CG  MET A  88      84.954  52.362 -11.149  1.00 23.10           C  
-ATOM    409  SD  MET A  88      84.849  53.531  -9.759  1.00 25.14           S  
-ATOM    410  CE  MET A  88      86.204  52.852  -8.629  1.00 20.91           C  
-ATOM    411  N   THR A  89      87.826  55.199 -13.315  1.00 25.71           N  
-ATOM    412  CA  THR A  89      88.791  55.742 -14.250  1.00 27.00           C  
-ATOM    413  C   THR A  89      90.143  55.055 -14.445  1.00 26.97           C  
-ATOM    414  O   THR A  89      90.966  55.553 -15.210  1.00 30.56           O  
-ATOM    415  CB  THR A  89      89.028  57.213 -13.867  1.00 26.51           C  
-ATOM    416  OG1 THR A  89      89.510  57.268 -12.518  1.00 25.22           O  
-ATOM    417  CG2 THR A  89      87.703  57.999 -13.917  1.00 22.85           C  
-ATOM    418  N   ASP A  90      90.377  53.919 -13.794  1.00 23.37           N  
-ATOM    419  CA  ASP A  90      91.661  53.219 -13.932  1.00 21.26           C  
-ATOM    420  C   ASP A  90      91.414  51.781 -13.496  1.00 20.09           C  
-ATOM    421  O   ASP A  90      91.623  51.425 -12.346  1.00 17.29           O  
-ATOM    422  CB  ASP A  90      92.695  53.876 -13.023  1.00 19.89           C  
-ATOM    423  CG  ASP A  90      94.093  53.299 -13.199  1.00 21.49           C  
-ATOM    424  OD1 ASP A  90      94.212  52.123 -13.598  1.00 18.92           O  
-ATOM    425  OD2 ASP A  90      95.061  54.030 -12.905  1.00 20.80           O  
-ATOM    426  N   SER A  91      90.973  50.949 -14.422  1.00 17.36           N  
-ATOM    427  CA  SER A  91      90.656  49.571 -14.069  1.00 18.51           C  
-ATOM    428  C   SER A  91      91.833  48.812 -13.467  1.00 18.86           C  
-ATOM    429  O   SER A  91      91.650  48.000 -12.559  1.00 17.11           O  
-ATOM    430  CB  SER A  91      90.141  48.843 -15.302  1.00 20.58           C  
-ATOM    431  OG  SER A  91      91.191  48.641 -16.223  1.00 24.90           O  
-ATOM    432  N   TRP A  92      93.052  49.081 -13.936  1.00 19.22           N  
-ATOM    433  CA  TRP A  92      94.180  48.332 -13.380  1.00 17.32           C  
-ATOM    434  C   TRP A  92      94.296  48.639 -11.902  1.00 17.68           C  
-ATOM    435  O   TRP A  92      94.298  47.735 -11.050  1.00 19.35           O  
-ATOM    436  CB  TRP A  92      95.502  48.670 -14.095  1.00 17.26           C  
-ATOM    437  CG  TRP A  92      96.587  47.722 -13.692  1.00 15.86           C  
-ATOM    438  CD1 TRP A  92      96.700  46.404 -14.047  1.00 14.81           C  
-ATOM    439  CD2 TRP A  92      97.615  47.965 -12.727  1.00 15.02           C  
-ATOM    440  NE1 TRP A  92      97.717  45.810 -13.344  1.00 16.46           N  
-ATOM    441  CE2 TRP A  92      98.302  46.745 -12.530  1.00 17.11           C  
-ATOM    442  CE3 TRP A  92      98.021  49.096 -12.008  1.00 15.45           C  
-ATOM    443  CZ2 TRP A  92      99.376  46.621 -11.641  1.00 13.04           C  
-ATOM    444  CZ3 TRP A  92      99.089  48.976 -11.115  1.00 15.76           C  
-ATOM    445  CH2 TRP A  92      99.753  47.740 -10.943  1.00 16.73           C  
-ATOM    446  N   ALA A  93      94.357  49.926 -11.597  1.00 17.00           N  
-ATOM    447  CA  ALA A  93      94.480  50.348 -10.214  1.00 17.58           C  
-ATOM    448  C   ALA A  93      93.278  49.959  -9.393  1.00 16.63           C  
-ATOM    449  O   ALA A  93      93.428  49.445  -8.295  1.00 16.54           O  
-ATOM    450  CB  ALA A  93      94.643  51.847 -10.139  1.00 13.88           C  
-ATOM    451  N   ASP A  94      92.087  50.223  -9.926  1.00 15.31           N  
-ATOM    452  CA  ASP A  94      90.848  49.947  -9.198  1.00 17.07           C  
-ATOM    453  C   ASP A  94      90.586  48.475  -8.934  1.00 15.14           C  
-ATOM    454  O   ASP A  94      90.359  48.083  -7.793  1.00 18.11           O  
-ATOM    455  CB  ASP A  94      89.637  50.517  -9.950  1.00 16.44           C  
-ATOM    456  CG  ASP A  94      89.686  52.018 -10.086  1.00 20.87           C  
-ATOM    457  OD1 ASP A  94      90.288  52.718  -9.221  1.00 20.25           O  
-ATOM    458  OD2 ASP A  94      89.097  52.506 -11.070  1.00 22.37           O  
-ATOM    459  N   ILE A  95      90.639  47.650  -9.978  1.00 18.11           N  
-ATOM    460  CA  ILE A  95      90.302  46.238  -9.788  1.00 18.12           C  
-ATOM    461  C   ILE A  95      91.201  45.148 -10.332  1.00 18.50           C  
-ATOM    462  O   ILE A  95      90.928  43.970 -10.102  1.00 18.30           O  
-ATOM    463  CB  ILE A  95      88.899  45.951 -10.354  1.00 20.05           C  
-ATOM    464  CG1 ILE A  95      88.906  46.046 -11.880  1.00 19.86           C  
-ATOM    465  CG2 ILE A  95      87.932  46.965  -9.842  1.00 14.15           C  
-ATOM    466  CD1 ILE A  95      87.545  45.793 -12.504  1.00 25.87           C  
-ATOM    467  N   GLU A  96      92.270  45.496 -11.036  1.00 16.84           N  
-ATOM    468  CA  GLU A  96      93.121  44.452 -11.597  1.00 18.58           C  
-ATOM    469  C   GLU A  96      94.448  44.207 -10.925  1.00 18.51           C  
-ATOM    470  O   GLU A  96      94.947  43.085 -10.966  1.00 18.52           O  
-ATOM    471  CB  GLU A  96      93.408  44.736 -13.081  1.00 19.22           C  
-ATOM    472  CG  GLU A  96      92.159  44.937 -13.917  1.00 22.32           C  
-ATOM    473  CD  GLU A  96      92.501  45.457 -15.310  1.00 22.82           C  
-ATOM    474  OE1 GLU A  96      93.689  45.488 -15.652  1.00 26.01           O  
-ATOM    475  OE2 GLU A  96      91.591  45.832 -16.047  1.00 27.48           O  
-ATOM    476  N   LYS A  97      95.044  45.234 -10.320  1.00 18.04           N  
-ATOM    477  CA  LYS A  97      96.361  45.023  -9.718  1.00 16.87           C  
-ATOM    478  C   LYS A  97      96.352  43.882  -8.726  1.00 17.37           C  
-ATOM    479  O   LYS A  97      95.460  43.790  -7.889  1.00 14.83           O  
-ATOM    480  CB  LYS A  97      96.866  46.292  -9.019  1.00 15.21           C  
-ATOM    481  CG  LYS A  97      98.113  46.057  -8.152  1.00 16.27           C  
-ATOM    482  CD  LYS A  97      98.688  47.407  -7.642  1.00 14.18           C  
-ATOM    483  CE  LYS A  97      99.917  47.208  -6.742  1.00 14.68           C  
-ATOM    484  NZ  LYS A  97     100.504  48.510  -6.293  1.00 18.76           N  
-ATOM    485  N   HIS A  98      97.351  43.012  -8.820  1.00 17.24           N  
-ATOM    486  CA  HIS A  98      97.433  41.903  -7.891  1.00 22.29           C  
-ATOM    487  C   HIS A  98      98.472  42.199  -6.842  1.00 24.44           C  
-ATOM    488  O   HIS A  98      99.629  42.457  -7.174  1.00 22.95           O  
-ATOM    489  CB  HIS A  98      97.825  40.595  -8.593  1.00 20.65           C  
-ATOM    490  CG  HIS A  98      96.682  39.907  -9.275  1.00 21.43           C  
-ATOM    491  ND1 HIS A  98      95.810  40.569 -10.115  1.00 19.61           N  
-ATOM    492  CD2 HIS A  98      96.267  38.615  -9.242  1.00 21.28           C  
-ATOM    493  CE1 HIS A  98      94.908  39.712 -10.571  1.00 23.96           C  
-ATOM    494  NE2 HIS A  98      95.164  38.522 -10.058  1.00 20.84           N  
-ATOM    495  N   TYR A  99      98.055  42.162  -5.584  1.00 25.47           N  
-ATOM    496  CA  TYR A  99      98.968  42.348  -4.466  1.00 29.83           C  
-ATOM    497  C   TYR A  99      99.188  40.942  -3.954  1.00 34.40           C  
-ATOM    498  O   TYR A  99      98.553  39.995  -4.428  1.00 35.40           O  
-ATOM    499  CB  TYR A  99      98.312  43.111  -3.320  1.00 23.56           C  
-ATOM    500  CG  TYR A  99      97.996  44.537  -3.615  1.00 21.47           C  
-ATOM    501  CD1 TYR A  99      96.765  44.887  -4.155  1.00 16.97           C  
-ATOM    502  CD2 TYR A  99      98.922  45.550  -3.338  1.00 19.18           C  
-ATOM    503  CE1 TYR A  99      96.443  46.221  -4.413  1.00 18.37           C  
-ATOM    504  CE2 TYR A  99      98.614  46.900  -3.592  1.00 18.02           C  
-ATOM    505  CZ  TYR A  99      97.369  47.223  -4.125  1.00 18.04           C  
-ATOM    506  OH  TYR A  99      97.004  48.533  -4.338  1.00 16.16           O  
-ATOM    507  N   PRO A 100     100.082  40.783  -2.970  1.00 37.76           N  
-ATOM    508  CA  PRO A 100     100.298  39.431  -2.442  1.00 38.22           C  
-ATOM    509  C   PRO A 100      98.978  38.933  -1.837  1.00 40.83           C  
-ATOM    510  O   PRO A 100      98.254  39.683  -1.153  1.00 40.27           O  
-ATOM    511  CB  PRO A 100     101.379  39.649  -1.388  1.00 40.80           C  
-ATOM    512  CG  PRO A 100     102.226  40.768  -2.026  1.00 40.61           C  
-ATOM    513  CD  PRO A 100     101.145  41.713  -2.541  1.00 36.58           C  
-ATOM    514  N   GLY A 101      98.657  37.668  -2.090  1.00 41.72           N  
-ATOM    515  CA  GLY A 101      97.418  37.115  -1.577  1.00 40.86           C  
-ATOM    516  C   GLY A 101      96.367  37.087  -2.674  1.00 40.31           C  
-ATOM    517  O   GLY A 101      95.300  36.478  -2.516  1.00 41.79           O  
-ATOM    518  N   ASP A 102      96.660  37.758  -3.787  1.00 36.84           N  
-ATOM    519  CA  ASP A 102      95.736  37.786  -4.913  1.00 33.45           C  
-ATOM    520  C   ASP A 102      96.080  36.672  -5.889  1.00 33.59           C  
-ATOM    521  O   ASP A 102      97.164  36.638  -6.487  1.00 30.09           O  
-ATOM    522  CB  ASP A 102      95.773  39.137  -5.625  1.00 31.41           C  
-ATOM    523  CG  ASP A 102      95.250  40.246  -4.761  1.00 29.99           C  
-ATOM    524  OD1 ASP A 102      94.613  39.910  -3.733  1.00 25.67           O  
-ATOM    525  OD2 ASP A 102      95.459  41.440  -5.100  1.00 30.02           O  
-ATOM    526  N   SER A 103      95.135  35.754  -6.034  1.00 32.69           N  
-ATOM    527  CA  SER A 103      95.308  34.616  -6.909  1.00 32.20           C  
-ATOM    528  C   SER A 103      95.272  34.986  -8.377  1.00 30.06           C  
-ATOM    529  O   SER A 103      94.519  35.863  -8.800  1.00 30.28           O  
-ATOM    530  CB  SER A 103      94.213  33.589  -6.633  1.00 32.20           C  
-ATOM    531  OG  SER A 103      94.250  32.554  -7.597  1.00 35.06           O  
-ATOM    532  N   TRP A 104      96.096  34.309  -9.158  1.00 31.58           N  
-ATOM    533  CA  TRP A 104      96.118  34.526 -10.595  1.00 33.52           C  
-ATOM    534  C   TRP A 104      95.243  33.484 -11.285  1.00 37.20           C  
-ATOM    535  O   TRP A 104      94.769  33.697 -12.405  1.00 37.14           O  
-ATOM    536  CB  TRP A 104      97.542  34.397 -11.128  1.00 33.86           C  
-ATOM    537  CG  TRP A 104      98.411  35.556 -10.771  1.00 32.22           C  
-ATOM    538  CD1 TRP A 104      99.402  35.597  -9.821  1.00 33.32           C  
-ATOM    539  CD2 TRP A 104      98.353  36.855 -11.348  1.00 31.45           C  
-ATOM    540  NE1 TRP A 104      99.964  36.857  -9.781  1.00 33.72           N  
-ATOM    541  CE2 TRP A 104      99.336  37.645 -10.709  1.00 31.79           C  
-ATOM    542  CE3 TRP A 104      97.562  37.432 -12.343  1.00 30.92           C  
-ATOM    543  CZ2 TRP A 104      99.545  38.977 -11.039  1.00 32.35           C  
-ATOM    544  CZ3 TRP A 104      97.770  38.751 -12.667  1.00 29.97           C  
-ATOM    545  CH2 TRP A 104      98.754  39.511 -12.018  1.00 31.79           C  
-ATOM    546  N   SER A 105      95.036  32.360 -10.600  1.00 39.97           N  
-ATOM    547  CA  SER A 105      94.262  31.245 -11.143  1.00 43.59           C  
-ATOM    548  C   SER A 105      92.849  31.070 -10.589  1.00 44.50           C  
-ATOM    549  O   SER A 105      92.142  30.149 -10.994  1.00 46.45           O  
-ATOM    550  CB  SER A 105      95.040  29.937 -10.942  1.00 44.21           C  
-ATOM    551  OG  SER A 105      95.297  29.694  -9.562  1.00 45.71           O  
-ATOM    552  N   ASP A 106      92.436  31.938  -9.673  1.00 45.41           N  
-ATOM    553  CA  ASP A 106      91.095  31.855  -9.086  1.00 44.64           C  
-ATOM    554  C   ASP A 106      90.038  31.988 -10.183  1.00 43.53           C  
-ATOM    555  O   ASP A 106      90.051  32.942 -10.957  1.00 43.02           O  
-ATOM    556  CB  ASP A 106      90.901  32.967  -8.048  1.00 48.06           C  
-ATOM    557  CG  ASP A 106      90.846  32.439  -6.615  1.00 52.29           C  
-ATOM    558  OD1 ASP A 106      91.660  31.545  -6.272  1.00 53.68           O  
-ATOM    559  OD2 ASP A 106      89.995  32.931  -5.829  1.00 52.19           O  
-ATOM    560  N   THR A 107      89.112  31.040 -10.247  1.00 39.26           N  
-ATOM    561  CA  THR A 107      88.089  31.113 -11.283  1.00 36.48           C  
-ATOM    562  C   THR A 107      87.001  32.079 -10.829  1.00 33.07           C  
-ATOM    563  O   THR A 107      86.901  32.399  -9.652  1.00 29.24           O  
-ATOM    564  CB  THR A 107      87.476  29.731 -11.543  1.00 37.15           C  
-ATOM    565  OG1 THR A 107      86.558  29.415 -10.491  1.00 36.90           O  
-ATOM    566  CG2 THR A 107      88.567  28.667 -11.563  1.00 37.54           C  
-ATOM    567  N   GLY A 108      86.191  32.557 -11.762  1.00 30.29           N  
-ATOM    568  CA  GLY A 108      85.149  33.484 -11.381  1.00 28.55           C  
-ATOM    569  C   GLY A 108      85.455  34.907 -11.806  1.00 25.40           C  
-ATOM    570  O   GLY A 108      86.504  35.171 -12.385  1.00 25.37           O  
-ATOM    571  N   ASN A 109      84.518  35.809 -11.524  1.00 23.72           N  
-ATOM    572  CA  ASN A 109      84.622  37.224 -11.855  1.00 23.65           C  
-ATOM    573  C   ASN A 109      85.086  37.900 -10.562  1.00 22.44           C  
-ATOM    574  O   ASN A 109      84.275  38.310  -9.753  1.00 22.81           O  
-ATOM    575  CB  ASN A 109      83.244  37.738 -12.272  1.00 22.89           C  
-ATOM    576  CG  ASN A 109      83.269  39.189 -12.684  1.00 23.13           C  
-ATOM    577  OD1 ASN A 109      84.219  39.643 -13.323  1.00 26.32           O  
-ATOM    578  ND2 ASN A 109      82.220  39.925 -12.340  1.00 21.88           N  
-ATOM    579  N   ASN A 110      86.394  38.020 -10.386  1.00 21.91           N  
-ATOM    580  CA  ASN A 110      86.945  38.554  -9.152  1.00 21.84           C  
-ATOM    581  C   ASN A 110      87.532  39.941  -9.241  1.00 22.94           C  
-ATOM    582  O   ASN A 110      88.111  40.315 -10.264  1.00 19.79           O  
-ATOM    583  CB  ASN A 110      87.991  37.571  -8.615  1.00 22.83           C  
-ATOM    584  CG  ASN A 110      87.400  36.178  -8.368  1.00 24.98           C  
-ATOM    585  OD1 ASN A 110      86.376  36.050  -7.690  1.00 20.79           O  
-ATOM    586  ND2 ASN A 110      88.047  35.142  -8.903  1.00 21.50           N  
-ATOM    587  N   VAL A 111      87.367  40.693  -8.151  1.00 20.18           N  
-ATOM    588  CA  VAL A 111      87.876  42.045  -8.066  1.00 20.27           C  
-ATOM    589  C   VAL A 111      89.160  42.051  -7.226  1.00 21.91           C  
-ATOM    590  O   VAL A 111      89.248  41.383  -6.184  1.00 19.28           O  
-ATOM    591  CB  VAL A 111      86.831  42.992  -7.443  1.00 20.83           C  
-ATOM    592  CG1 VAL A 111      86.541  42.578  -5.983  1.00 18.93           C  
-ATOM    593  CG2 VAL A 111      87.328  44.461  -7.524  1.00 18.16           C  
-ATOM    594  N   TYR A 112      90.173  42.776  -7.692  1.00 18.00           N  
-ATOM    595  CA  TYR A 112      91.425  42.855  -6.951  1.00 18.97           C  
-ATOM    596  C   TYR A 112      91.728  44.334  -6.856  1.00 18.11           C  
-ATOM    597  O   TYR A 112      90.849  45.105  -6.481  1.00 17.89           O  
-ATOM    598  CB  TYR A 112      92.542  42.095  -7.692  1.00 19.95           C  
-ATOM    599  CG  TYR A 112      92.257  40.600  -7.803  1.00 21.25           C  
-ATOM    600  CD1 TYR A 112      92.384  39.759  -6.693  1.00 20.84           C  
-ATOM    601  CD2 TYR A 112      91.812  40.040  -9.005  1.00 22.33           C  
-ATOM    602  CE1 TYR A 112      92.075  38.401  -6.772  1.00 21.11           C  
-ATOM    603  CE2 TYR A 112      91.497  38.675  -9.099  1.00 19.79           C  
-ATOM    604  CZ  TYR A 112      91.634  37.866  -7.974  1.00 22.76           C  
-ATOM    605  OH  TYR A 112      91.347  36.515  -8.033  1.00 21.98           O  
-ATOM    606  N   GLY A 113      92.951  44.733  -7.207  1.00 18.06           N  
-ATOM    607  CA  GLY A 113      93.310  46.146  -7.166  1.00 16.49           C  
-ATOM    608  C   GLY A 113      93.047  46.808  -5.824  1.00 16.03           C  
-ATOM    609  O   GLY A 113      93.011  46.137  -4.784  1.00 16.85           O  
-ATOM    610  N   CYS A 114      92.884  48.126  -5.834  1.00 16.40           N  
-ATOM    611  CA  CYS A 114      92.617  48.848  -4.588  1.00 17.00           C  
-ATOM    612  C   CYS A 114      91.289  48.453  -3.961  1.00 15.26           C  
-ATOM    613  O   CYS A 114      91.152  48.413  -2.745  1.00 14.69           O  
-ATOM    614  CB  CYS A 114      92.592  50.351  -4.853  1.00 16.01           C  
-ATOM    615  SG  CYS A 114      94.258  50.996  -5.246  1.00 18.40           S  
-ATOM    616  N   ILE A 115      90.299  48.193  -4.799  1.00 16.11           N  
-ATOM    617  CA  ILE A 115      88.968  47.865  -4.279  1.00 16.27           C  
-ATOM    618  C   ILE A 115      88.988  46.694  -3.321  1.00 14.57           C  
-ATOM    619  O   ILE A 115      88.421  46.775  -2.235  1.00 18.65           O  
-ATOM    620  CB  ILE A 115      87.992  47.565  -5.407  1.00 14.07           C  
-ATOM    621  CG1 ILE A 115      87.857  48.803  -6.275  1.00 17.29           C  
-ATOM    622  CG2 ILE A 115      86.647  47.103  -4.812  1.00 15.89           C  
-ATOM    623  CD1 ILE A 115      87.265  49.990  -5.562  1.00 19.21           C  
-ATOM    624  N   LYS A 116      89.625  45.605  -3.717  1.00 14.87           N  
-ATOM    625  CA  LYS A 116      89.682  44.455  -2.819  1.00 17.73           C  
-ATOM    626  C   LYS A 116      90.363  44.833  -1.507  1.00 19.60           C  
-ATOM    627  O   LYS A 116      89.910  44.458  -0.424  1.00 15.37           O  
-ATOM    628  CB  LYS A 116      90.451  43.298  -3.451  1.00 17.46           C  
-ATOM    629  CG  LYS A 116      90.704  42.116  -2.496  1.00 19.09           C  
-ATOM    630  CD  LYS A 116      91.367  40.911  -3.204  1.00 19.32           C  
-ATOM    631  CE  LYS A 116      91.760  39.823  -2.181  1.00 20.69           C  
-ATOM    632  NZ  LYS A 116      92.438  38.616  -2.773  1.00 18.38           N  
-ATOM    633  N   GLN A 117      91.465  45.574  -1.604  1.00 18.97           N  
-ATOM    634  CA  GLN A 117      92.185  45.939  -0.386  1.00 18.84           C  
-ATOM    635  C   GLN A 117      91.346  46.792   0.532  1.00 17.87           C  
-ATOM    636  O   GLN A 117      91.397  46.628   1.741  1.00 19.07           O  
-ATOM    637  CB  GLN A 117      93.493  46.656  -0.723  1.00 18.39           C  
-ATOM    638  CG  GLN A 117      94.460  45.782  -1.470  1.00 18.68           C  
-ATOM    639  CD  GLN A 117      94.738  44.473  -0.766  1.00 21.24           C  
-ATOM    640  OE1 GLN A 117      95.080  44.453   0.418  1.00 21.33           O  
-ATOM    641  NE2 GLN A 117      94.604  43.364  -1.493  1.00 16.47           N  
-ATOM    642  N   LEU A 118      90.582  47.711  -0.041  1.00 17.07           N  
-ATOM    643  CA  LEU A 118      89.732  48.567   0.772  1.00 17.69           C  
-ATOM    644  C   LEU A 118      88.643  47.733   1.455  1.00 18.34           C  
-ATOM    645  O   LEU A 118      88.304  47.951   2.628  1.00 19.36           O  
-ATOM    646  CB  LEU A 118      89.109  49.647  -0.103  1.00 14.22           C  
-ATOM    647  CG  LEU A 118      90.159  50.695  -0.509  1.00 16.17           C  
-ATOM    648  CD1 LEU A 118      89.657  51.482  -1.731  1.00 14.15           C  
-ATOM    649  CD2 LEU A 118      90.485  51.613   0.727  1.00 16.24           C  
-ATOM    650  N   TYR A 119      88.093  46.769   0.729  1.00 19.53           N  
-ATOM    651  CA  TYR A 119      87.070  45.919   1.321  1.00 17.18           C  
-ATOM    652  C   TYR A 119      87.682  45.175   2.497  1.00 17.38           C  
-ATOM    653  O   TYR A 119      87.085  45.103   3.567  1.00 19.86           O  
-ATOM    654  CB  TYR A 119      86.515  44.921   0.292  1.00 18.63           C  
-ATOM    655  CG  TYR A 119      85.434  44.032   0.879  1.00 16.78           C  
-ATOM    656  CD1 TYR A 119      84.122  44.490   1.025  1.00 19.03           C  
-ATOM    657  CD2 TYR A 119      85.733  42.745   1.316  1.00 18.29           C  
-ATOM    658  CE1 TYR A 119      83.127  43.676   1.600  1.00 17.03           C  
-ATOM    659  CE2 TYR A 119      84.758  41.933   1.886  1.00 19.43           C  
-ATOM    660  CZ  TYR A 119      83.464  42.407   2.028  1.00 18.52           C  
-ATOM    661  OH  TYR A 119      82.526  41.620   2.654  1.00 20.32           O  
-ATOM    662  N   LEU A 120      88.887  44.643   2.323  1.00 15.65           N  
-ATOM    663  CA  LEU A 120      89.529  43.918   3.424  1.00 15.01           C  
-ATOM    664  C   LEU A 120      89.759  44.815   4.641  1.00 18.33           C  
-ATOM    665  O   LEU A 120      89.636  44.358   5.786  1.00 17.45           O  
-ATOM    666  CB  LEU A 120      90.846  43.291   2.953  1.00 17.34           C  
-ATOM    667  CG  LEU A 120      90.669  42.072   2.044  1.00 18.04           C  
-ATOM    668  CD1 LEU A 120      92.021  41.638   1.515  1.00 15.69           C  
-ATOM    669  CD2 LEU A 120      89.986  40.930   2.816  1.00 15.32           C  
-ATOM    670  N   LEU A 121      90.075  46.090   4.404  1.00 16.28           N  
-ATOM    671  CA  LEU A 121      90.272  47.028   5.513  1.00 16.18           C  
-ATOM    672  C   LEU A 121      88.952  47.261   6.237  1.00 18.25           C  
-ATOM    673  O   LEU A 121      88.936  47.511   7.446  1.00 18.88           O  
-ATOM    674  CB  LEU A 121      90.812  48.360   4.999  1.00 16.73           C  
-ATOM    675  CG  LEU A 121      92.244  48.309   4.437  1.00 17.65           C  
-ATOM    676  CD1 LEU A 121      92.530  49.685   3.827  1.00 18.88           C  
-ATOM    677  CD2 LEU A 121      93.271  47.960   5.533  1.00 17.82           C  
-ATOM    678  N   LYS A 122      87.838  47.175   5.513  1.00 18.14           N  
-ATOM    679  CA  LYS A 122      86.531  47.370   6.146  1.00 18.66           C  
-ATOM    680  C   LYS A 122      86.279  46.263   7.164  1.00 17.59           C  
-ATOM    681  O   LYS A 122      85.552  46.471   8.133  1.00 20.01           O  
-ATOM    682  CB  LYS A 122      85.417  47.401   5.094  1.00 13.61           C  
-ATOM    683  CG  LYS A 122      85.414  48.740   4.341  1.00 16.94           C  
-ATOM    684  CD  LYS A 122      84.382  48.824   3.197  1.00 18.20           C  
-ATOM    685  CE  LYS A 122      83.022  48.292   3.592  1.00 15.45           C  
-ATOM    686  NZ  LYS A 122      81.887  48.928   2.829  1.00 16.45           N  
-ATOM    687  N   LYS A 123      86.885  45.104   6.964  1.00 18.86           N  
-ATOM    688  CA  LYS A 123      86.718  44.024   7.937  1.00 24.34           C  
-ATOM    689  C   LYS A 123      87.625  44.239   9.138  1.00 26.49           C  
-ATOM    690  O   LYS A 123      87.328  43.757  10.224  1.00 27.72           O  
-ATOM    691  CB  LYS A 123      87.006  42.657   7.312  1.00 24.69           C  
-ATOM    692  CG  LYS A 123      85.959  42.300   6.279  1.00 27.85           C  
-ATOM    693  CD  LYS A 123      86.271  41.066   5.454  1.00 29.55           C  
-ATOM    694  CE  LYS A 123      86.055  39.817   6.233  1.00 34.68           C  
-ATOM    695  NZ  LYS A 123      85.635  38.671   5.345  1.00 31.20           N  
-ATOM    696  N   GLN A 124      88.717  44.977   8.964  1.00 26.01           N  
-ATOM    697  CA  GLN A 124      89.626  45.206  10.088  1.00 26.33           C  
-ATOM    698  C   GLN A 124      89.080  46.285  11.009  1.00 24.90           C  
-ATOM    699  O   GLN A 124      89.312  46.251  12.215  1.00 23.23           O  
-ATOM    700  CB  GLN A 124      91.018  45.609   9.593  1.00 30.15           C  
-ATOM    701  CG  GLN A 124      91.690  44.534   8.753  1.00 35.18           C  
-ATOM    702  CD  GLN A 124      91.932  43.264   9.552  1.00 40.85           C  
-ATOM    703  OE1 GLN A 124      91.843  42.147   9.023  1.00 40.70           O  
-ATOM    704  NE2 GLN A 124      92.245  43.428  10.839  1.00 42.75           N  
-ATOM    705  N   ASN A 125      88.378  47.258  10.435  1.00 22.75           N  
-ATOM    706  CA  ASN A 125      87.782  48.333  11.214  1.00 20.48           C  
-ATOM    707  C   ASN A 125      86.352  48.492  10.740  1.00 21.34           C  
-ATOM    708  O   ASN A 125      86.092  49.100   9.689  1.00 17.32           O  
-ATOM    709  CB  ASN A 125      88.537  49.669  11.048  1.00 20.29           C  
-ATOM    710  CG  ASN A 125      87.956  50.776  11.939  1.00 23.17           C  
-ATOM    711  OD1 ASN A 125      87.002  50.533  12.704  1.00 18.77           O  
-ATOM    712  ND2 ASN A 125      88.520  51.989  11.850  1.00 20.09           N  
-ATOM    713  N   ARG A 126      85.427  47.939  11.526  1.00 20.89           N  
-ATOM    714  CA  ARG A 126      84.007  47.980  11.204  1.00 18.89           C  
-ATOM    715  C   ARG A 126      83.479  49.388  11.226  1.00 18.31           C  
-ATOM    716  O   ARG A 126      82.362  49.639  10.780  1.00 18.43           O  
-ATOM    717  CB  ARG A 126      83.204  47.104  12.186  1.00 20.68           C  
-ATOM    718  CG  ARG A 126      83.469  45.625  12.032  1.00 19.94           C  
-ATOM    719  CD  ARG A 126      83.408  45.211  10.553  1.00 20.19           C  
-ATOM    720  NE  ARG A 126      82.164  45.632   9.896  1.00 24.53           N  
-ATOM    721  CZ  ARG A 126      80.981  45.065  10.098  1.00 25.81           C  
-ATOM    722  NH1 ARG A 126      80.873  44.040  10.945  1.00 23.96           N  
-ATOM    723  NH2 ARG A 126      79.908  45.523   9.460  1.00 24.98           N  
-ATOM    724  N   ASN A 127      84.270  50.313  11.766  1.00 16.06           N  
-ATOM    725  CA  ASN A 127      83.843  51.703  11.801  1.00 15.40           C  
-ATOM    726  C   ASN A 127      84.375  52.516  10.610  1.00 15.71           C  
-ATOM    727  O   ASN A 127      84.116  53.725  10.488  1.00 15.52           O  
-ATOM    728  CB  ASN A 127      84.279  52.370  13.112  1.00 17.24           C  
-ATOM    729  CG  ASN A 127      83.505  53.639  13.378  1.00 16.48           C  
-ATOM    730  OD1 ASN A 127      82.285  53.636  13.315  1.00 18.47           O  
-ATOM    731  ND2 ASN A 127      84.202  54.731  13.651  1.00 16.12           N  
-ATOM    732  N   LEU A 128      85.118  51.845   9.736  1.00 15.25           N  
-ATOM    733  CA  LEU A 128      85.695  52.492   8.551  1.00 14.76           C  
-ATOM    734  C   LEU A 128      84.745  52.444   7.337  1.00 14.78           C  
-ATOM    735  O   LEU A 128      84.471  51.372   6.805  1.00 16.50           O  
-ATOM    736  CB  LEU A 128      87.017  51.802   8.167  1.00 14.31           C  
-ATOM    737  CG  LEU A 128      87.682  52.382   6.901  1.00 17.52           C  
-ATOM    738  CD1 LEU A 128      88.198  53.801   7.210  1.00 20.65           C  
-ATOM    739  CD2 LEU A 128      88.852  51.506   6.448  1.00 18.35           C  
-ATOM    740  N   LYS A 129      84.237  53.593   6.908  1.00 16.13           N  
-ATOM    741  CA  LYS A 129      83.355  53.606   5.742  1.00 17.18           C  
-ATOM    742  C   LYS A 129      84.207  54.025   4.553  1.00 19.13           C  
-ATOM    743  O   LYS A 129      85.084  54.871   4.693  1.00 17.55           O  
-ATOM    744  CB  LYS A 129      82.190  54.587   5.931  1.00 17.06           C  
-ATOM    745  CG  LYS A 129      81.034  54.027   6.788  1.00 16.20           C  
-ATOM    746  CD  LYS A 129      81.438  53.813   8.254  1.00 17.10           C  
-ATOM    747  CE  LYS A 129      81.620  55.158   8.987  1.00 17.06           C  
-ATOM    748  NZ  LYS A 129      81.785  54.938  10.464  1.00 17.91           N  
-ATOM    749  N   VAL A 130      83.976  53.413   3.395  1.00 16.11           N  
-ATOM    750  CA  VAL A 130      84.735  53.764   2.204  1.00 16.62           C  
-ATOM    751  C   VAL A 130      83.725  54.268   1.191  1.00 18.30           C  
-ATOM    752  O   VAL A 130      82.827  53.525   0.800  1.00 18.62           O  
-ATOM    753  CB  VAL A 130      85.461  52.527   1.599  1.00 16.66           C  
-ATOM    754  CG1 VAL A 130      86.272  52.958   0.392  1.00 20.36           C  
-ATOM    755  CG2 VAL A 130      86.336  51.826   2.665  1.00 15.57           C  
-ATOM    756  N   LEU A 131      83.868  55.520   0.776  1.00 18.60           N  
-ATOM    757  CA  LEU A 131      82.963  56.127  -0.194  1.00 17.37           C  
-ATOM    758  C   LEU A 131      83.654  56.288  -1.543  1.00 20.52           C  
-ATOM    759  O   LEU A 131      84.869  56.476  -1.605  1.00 18.57           O  
-ATOM    760  CB  LEU A 131      82.527  57.513   0.276  1.00 16.03           C  
-ATOM    761  CG  LEU A 131      81.545  57.554   1.461  1.00 19.25           C  
-ATOM    762  CD1 LEU A 131      82.239  57.009   2.693  1.00 19.44           C  
-ATOM    763  CD2 LEU A 131      81.095  58.982   1.694  1.00 16.76           C  
-ATOM    764  N   LEU A 132      82.875  56.193  -2.620  1.00 18.96           N  
-ATOM    765  CA  LEU A 132      83.420  56.414  -3.945  1.00 16.68           C  
-ATOM    766  C   LEU A 132      83.305  57.922  -4.119  1.00 19.09           C  
-ATOM    767  O   LEU A 132      82.222  58.501  -3.937  1.00 18.85           O  
-ATOM    768  CB  LEU A 132      82.584  55.714  -5.021  1.00 17.28           C  
-ATOM    769  CG  LEU A 132      82.966  56.163  -6.436  1.00 17.65           C  
-ATOM    770  CD1 LEU A 132      84.466  55.891  -6.639  1.00 16.69           C  
-ATOM    771  CD2 LEU A 132      82.122  55.411  -7.501  1.00 17.83           C  
-ATOM    772  N   SER A 133      84.417  58.562  -4.465  1.00 17.64           N  
-ATOM    773  CA  SER A 133      84.437  59.997  -4.664  1.00 17.40           C  
-ATOM    774  C   SER A 133      84.358  60.246  -6.168  1.00 19.97           C  
-ATOM    775  O   SER A 133      85.173  59.723  -6.943  1.00 17.26           O  
-ATOM    776  CB  SER A 133      85.724  60.577  -4.083  1.00 17.66           C  
-ATOM    777  OG  SER A 133      85.690  61.982  -4.073  1.00 23.00           O  
-ATOM    778  N   ILE A 134      83.384  61.065  -6.562  1.00 17.37           N  
-ATOM    779  CA  ILE A 134      83.104  61.365  -7.955  1.00 16.41           C  
-ATOM    780  C   ILE A 134      83.392  62.814  -8.274  1.00 18.06           C  
-ATOM    781  O   ILE A 134      82.885  63.702  -7.600  1.00 18.11           O  
-ATOM    782  CB  ILE A 134      81.613  61.107  -8.265  1.00 16.64           C  
-ATOM    783  CG1 ILE A 134      81.260  59.661  -7.928  1.00 16.75           C  
-ATOM    784  CG2 ILE A 134      81.325  61.415  -9.756  1.00 14.47           C  
-ATOM    785  CD1 ILE A 134      79.731  59.397  -7.766  1.00 20.37           C  
-ATOM    786  N   GLY A 135      84.193  63.068  -9.302  1.00 17.16           N  
-ATOM    787  CA  GLY A 135      84.481  64.449  -9.640  1.00 15.15           C  
-ATOM    788  C   GLY A 135      85.944  64.819  -9.488  1.00 18.25           C  
-ATOM    789  O   GLY A 135      86.821  64.127 -10.023  1.00 19.93           O  
-ATOM    790  N   GLY A 136      86.204  65.899  -8.758  1.00 16.51           N  
-ATOM    791  CA  GLY A 136      87.570  66.358  -8.575  1.00 19.19           C  
-ATOM    792  C   GLY A 136      87.880  67.454  -9.587  1.00 21.27           C  
-ATOM    793  O   GLY A 136      87.070  67.731 -10.482  1.00 23.75           O  
-ATOM    794  N   TRP A 137      89.045  68.075  -9.469  1.00 19.52           N  
-ATOM    795  CA  TRP A 137      89.404  69.162 -10.369  1.00 22.17           C  
-ATOM    796  C   TRP A 137      89.389  68.791 -11.844  1.00 22.52           C  
-ATOM    797  O   TRP A 137      88.929  69.554 -12.686  1.00 22.15           O  
-ATOM    798  CB  TRP A 137      90.799  69.684 -10.053  1.00 23.80           C  
-ATOM    799  CG  TRP A 137      90.953  70.282  -8.702  1.00 27.96           C  
-ATOM    800  CD1 TRP A 137      89.959  70.581  -7.810  1.00 27.58           C  
-ATOM    801  CD2 TRP A 137      92.180  70.714  -8.100  1.00 29.85           C  
-ATOM    802  NE1 TRP A 137      90.497  71.178  -6.688  1.00 29.23           N  
-ATOM    803  CE2 TRP A 137      91.857  71.270  -6.842  1.00 30.47           C  
-ATOM    804  CE3 TRP A 137      93.520  70.685  -8.503  1.00 29.87           C  
-ATOM    805  CZ2 TRP A 137      92.828  71.797  -5.983  1.00 32.28           C  
-ATOM    806  CZ3 TRP A 137      94.489  71.209  -7.645  1.00 32.05           C  
-ATOM    807  CH2 TRP A 137      94.134  71.759  -6.399  1.00 30.77           C  
-ATOM    808  N   THR A 138      89.898  67.620 -12.166  1.00 22.62           N  
-ATOM    809  CA  THR A 138      89.971  67.235 -13.563  1.00 23.42           C  
-ATOM    810  C   THR A 138      88.642  66.905 -14.188  1.00 23.39           C  
-ATOM    811  O   THR A 138      88.371  67.292 -15.330  1.00 20.97           O  
-ATOM    812  CB  THR A 138      90.863  66.009 -13.755  1.00 24.11           C  
-ATOM    813  OG1 THR A 138      92.127  66.276 -13.150  1.00 24.91           O  
-ATOM    814  CG2 THR A 138      91.057  65.703 -15.269  1.00 21.48           C  
-ATOM    815  N   TYR A 139      87.810  66.200 -13.438  1.00 20.81           N  
-ATOM    816  CA  TYR A 139      86.544  65.762 -13.989  1.00 19.65           C  
-ATOM    817  C   TYR A 139      85.344  66.672 -13.781  1.00 21.72           C  
-ATOM    818  O   TYR A 139      84.294  66.459 -14.392  1.00 20.79           O  
-ATOM    819  CB  TYR A 139      86.219  64.375 -13.454  1.00 20.67           C  
-ATOM    820  CG  TYR A 139      87.309  63.335 -13.651  1.00 20.70           C  
-ATOM    821  CD1 TYR A 139      88.094  63.318 -14.807  1.00 23.51           C  
-ATOM    822  CD2 TYR A 139      87.539  62.354 -12.682  1.00 20.49           C  
-ATOM    823  CE1 TYR A 139      89.095  62.341 -14.992  1.00 24.40           C  
-ATOM    824  CE2 TYR A 139      88.534  61.374 -12.849  1.00 22.09           C  
-ATOM    825  CZ  TYR A 139      89.309  61.380 -14.005  1.00 22.68           C  
-ATOM    826  OH  TYR A 139      90.316  60.465 -14.149  1.00 26.10           O  
-ATOM    827  N   SER A 140      85.486  67.681 -12.933  1.00 20.91           N  
-ATOM    828  CA  SER A 140      84.362  68.570 -12.663  1.00 21.67           C  
-ATOM    829  C   SER A 140      83.703  69.237 -13.883  1.00 23.78           C  
-ATOM    830  O   SER A 140      82.528  69.590 -13.819  1.00 20.61           O  
-ATOM    831  CB  SER A 140      84.765  69.640 -11.630  1.00 22.56           C  
-ATOM    832  OG  SER A 140      84.744  69.085 -10.310  1.00 20.17           O  
-ATOM    833  N   PRO A 141      84.442  69.431 -14.997  1.00 23.65           N  
-ATOM    834  CA  PRO A 141      83.741  70.072 -16.124  1.00 25.28           C  
-ATOM    835  C   PRO A 141      82.570  69.227 -16.643  1.00 25.52           C  
-ATOM    836  O   PRO A 141      81.689  69.722 -17.358  1.00 25.47           O  
-ATOM    837  CB  PRO A 141      84.846  70.232 -17.179  1.00 26.13           C  
-ATOM    838  CG  PRO A 141      86.103  70.432 -16.320  1.00 27.96           C  
-ATOM    839  CD  PRO A 141      85.897  69.377 -15.237  1.00 25.23           C  
-ATOM    840  N   ASN A 142      82.553  67.949 -16.288  1.00 21.72           N  
-ATOM    841  CA  ASN A 142      81.484  67.092 -16.750  1.00 23.63           C  
-ATOM    842  C   ASN A 142      80.193  67.138 -15.967  1.00 23.03           C  
-ATOM    843  O   ASN A 142      79.195  66.587 -16.420  1.00 23.45           O  
-ATOM    844  CB  ASN A 142      81.957  65.652 -16.820  1.00 21.21           C  
-ATOM    845  CG  ASN A 142      83.074  65.481 -17.810  1.00 26.67           C  
-ATOM    846  OD1 ASN A 142      83.078  66.136 -18.855  1.00 22.40           O  
-ATOM    847  ND2 ASN A 142      84.029  64.611 -17.497  1.00 21.50           N  
-ATOM    848  N   PHE A 143      80.204  67.787 -14.805  1.00 24.60           N  
-ATOM    849  CA  PHE A 143      79.001  67.852 -13.965  1.00 23.58           C  
-ATOM    850  C   PHE A 143      77.840  68.670 -14.539  1.00 24.00           C  
-ATOM    851  O   PHE A 143      76.731  68.169 -14.633  1.00 24.10           O  
-ATOM    852  CB  PHE A 143      79.335  68.403 -12.566  1.00 22.81           C  
-ATOM    853  CG  PHE A 143      79.962  67.390 -11.641  1.00 21.35           C  
-ATOM    854  CD1 PHE A 143      79.238  66.283 -11.207  1.00 22.98           C  
-ATOM    855  CD2 PHE A 143      81.261  67.555 -11.187  1.00 21.20           C  
-ATOM    856  CE1 PHE A 143      79.802  65.355 -10.326  1.00 24.68           C  
-ATOM    857  CE2 PHE A 143      81.834  66.621 -10.300  1.00 19.10           C  
-ATOM    858  CZ  PHE A 143      81.105  65.529  -9.872  1.00 19.79           C  
-ATOM    859  N   ALA A 144      78.103  69.920 -14.906  1.00 24.87           N  
-ATOM    860  CA  ALA A 144      77.048  70.790 -15.415  1.00 26.24           C  
-ATOM    861  C   ALA A 144      76.184  70.114 -16.485  1.00 25.99           C  
-ATOM    862  O   ALA A 144      74.968  70.048 -16.352  1.00 26.24           O  
-ATOM    863  CB  ALA A 144      77.640  72.095 -15.935  1.00 24.73           C  
-ATOM    864  N   PRO A 145      76.803  69.581 -17.543  1.00 26.42           N  
-ATOM    865  CA  PRO A 145      75.975  68.929 -18.567  1.00 26.30           C  
-ATOM    866  C   PRO A 145      75.320  67.645 -18.065  1.00 27.20           C  
-ATOM    867  O   PRO A 145      74.141  67.389 -18.302  1.00 26.74           O  
-ATOM    868  CB  PRO A 145      76.966  68.693 -19.719  1.00 27.44           C  
-ATOM    869  CG  PRO A 145      78.327  68.594 -18.994  1.00 26.82           C  
-ATOM    870  CD  PRO A 145      78.208  69.710 -17.988  1.00 25.78           C  
-ATOM    871  N   ALA A 146      76.080  66.842 -17.340  1.00 25.68           N  
-ATOM    872  CA  ALA A 146      75.526  65.603 -16.836  1.00 25.74           C  
-ATOM    873  C   ALA A 146      74.288  65.836 -15.975  1.00 26.85           C  
-ATOM    874  O   ALA A 146      73.294  65.121 -16.099  1.00 27.34           O  
-ATOM    875  CB  ALA A 146      76.572  64.859 -16.033  1.00 24.61           C  
-ATOM    876  N   ALA A 147      74.347  66.838 -15.103  1.00 25.51           N  
-ATOM    877  CA  ALA A 147      73.233  67.101 -14.197  1.00 27.67           C  
-ATOM    878  C   ALA A 147      72.128  67.999 -14.754  1.00 28.31           C  
-ATOM    879  O   ALA A 147      71.119  68.221 -14.079  1.00 26.30           O  
-ATOM    880  CB  ALA A 147      73.766  67.708 -12.898  1.00 26.64           C  
-ATOM    881  N   SER A 148      72.331  68.512 -15.968  1.00 28.93           N  
-ATOM    882  CA  SER A 148      71.386  69.422 -16.603  1.00 30.22           C  
-ATOM    883  C   SER A 148      70.028  68.820 -16.948  1.00 31.09           C  
-ATOM    884  O   SER A 148      69.044  69.555 -17.057  1.00 31.71           O  
-ATOM    885  CB  SER A 148      71.995  70.024 -17.869  1.00 30.17           C  
-ATOM    886  OG  SER A 148      72.174  69.012 -18.848  1.00 30.04           O  
-ATOM    887  N   THR A 149      69.958  67.504 -17.115  1.00 31.46           N  
-ATOM    888  CA  THR A 149      68.684  66.878 -17.444  1.00 31.63           C  
-ATOM    889  C   THR A 149      68.259  65.810 -16.454  1.00 33.30           C  
-ATOM    890  O   THR A 149      69.081  65.196 -15.765  1.00 31.87           O  
-ATOM    891  CB  THR A 149      68.701  66.211 -18.816  1.00 32.26           C  
-ATOM    892  OG1 THR A 149      69.502  65.025 -18.743  1.00 30.08           O  
-ATOM    893  CG2 THR A 149      69.253  67.166 -19.879  1.00 32.17           C  
-ATOM    894  N   ASP A 150      66.954  65.571 -16.420  1.00 33.32           N  
-ATOM    895  CA  ASP A 150      66.391  64.586 -15.528  1.00 31.98           C  
-ATOM    896  C   ASP A 150      66.941  63.205 -15.790  1.00 32.08           C  
-ATOM    897  O   ASP A 150      67.258  62.471 -14.855  1.00 31.44           O  
-ATOM    898  CB  ASP A 150      64.881  64.540 -15.673  1.00 35.32           C  
-ATOM    899  CG  ASP A 150      64.254  63.662 -14.637  1.00 35.89           C  
-ATOM    900  OD1 ASP A 150      64.352  64.032 -13.451  1.00 38.57           O  
-ATOM    901  OD2 ASP A 150      63.695  62.605 -14.993  1.00 37.53           O  
-ATOM    902  N   ALA A 151      67.034  62.841 -17.068  1.00 30.44           N  
-ATOM    903  CA  ALA A 151      67.554  61.536 -17.450  1.00 30.30           C  
-ATOM    904  C   ALA A 151      69.008  61.375 -16.992  1.00 28.29           C  
-ATOM    905  O   ALA A 151      69.394  60.311 -16.526  1.00 28.80           O  
-ATOM    906  CB  ALA A 151      67.480  61.366 -18.964  1.00 31.36           C  
-ATOM    907  N   GLY A 152      69.792  62.432 -17.164  1.00 27.77           N  
-ATOM    908  CA  GLY A 152      71.198  62.425 -16.782  1.00 31.31           C  
-ATOM    909  C   GLY A 152      71.367  62.245 -15.286  1.00 31.12           C  
-ATOM    910  O   GLY A 152      72.150  61.406 -14.837  1.00 30.43           O  
-ATOM    911  N   ARG A 153      70.628  63.027 -14.510  1.00 31.21           N  
-ATOM    912  CA  ARG A 153      70.707  62.922 -13.057  1.00 30.43           C  
-ATOM    913  C   ARG A 153      70.314  61.523 -12.639  1.00 30.04           C  
-ATOM    914  O   ARG A 153      70.983  60.896 -11.822  1.00 29.09           O  
-ATOM    915  CB  ARG A 153      69.793  63.949 -12.403  1.00 28.50           C  
-ATOM    916  CG  ARG A 153      70.220  65.358 -12.690  1.00 28.34           C  
-ATOM    917  CD  ARG A 153      69.432  66.338 -11.854  1.00 29.80           C  
-ATOM    918  NE  ARG A 153      68.026  66.420 -12.260  1.00 29.19           N  
-ATOM    919  CZ  ARG A 153      67.566  67.249 -13.195  1.00 29.85           C  
-ATOM    920  NH1 ARG A 153      68.398  68.063 -13.831  1.00 28.74           N  
-ATOM    921  NH2 ARG A 153      66.265  67.300 -13.467  1.00 28.33           N  
-ATOM    922  N   LYS A 154      69.235  61.010 -13.218  1.00 29.28           N  
-ATOM    923  CA  LYS A 154      68.805  59.670 -12.873  1.00 28.01           C  
-ATOM    924  C   LYS A 154      69.821  58.594 -13.251  1.00 26.98           C  
-ATOM    925  O   LYS A 154      69.996  57.621 -12.517  1.00 26.98           O  
-ATOM    926  CB  LYS A 154      67.455  59.364 -13.531  1.00 31.98           C  
-ATOM    927  CG  LYS A 154      66.301  60.145 -12.928  1.00 36.53           C  
-ATOM    928  CD  LYS A 154      64.968  59.814 -13.600  1.00 40.06           C  
-ATOM    929  CE  LYS A 154      63.802  60.516 -12.889  1.00 41.93           C  
-ATOM    930  NZ  LYS A 154      62.480  60.246 -13.552  1.00 44.15           N  
-ATOM    931  N   ASN A 155      70.477  58.746 -14.399  1.00 25.97           N  
-ATOM    932  CA  ASN A 155      71.467  57.742 -14.824  1.00 25.29           C  
-ATOM    933  C   ASN A 155      72.724  57.858 -13.957  1.00 22.59           C  
-ATOM    934  O   ASN A 155      73.383  56.856 -13.685  1.00 23.38           O  
-ATOM    935  CB  ASN A 155      71.820  57.913 -16.308  1.00 25.08           C  
-ATOM    936  CG  ASN A 155      72.624  56.738 -16.866  1.00 26.12           C  
-ATOM    937  OD1 ASN A 155      72.312  55.569 -16.619  1.00 22.69           O  
-ATOM    938  ND2 ASN A 155      73.666  57.054 -17.635  1.00 26.37           N  
-ATOM    939  N   PHE A 156      73.045  59.083 -13.540  1.00 22.52           N  
-ATOM    940  CA  PHE A 156      74.191  59.340 -12.660  1.00 22.16           C  
-ATOM    941  C   PHE A 156      73.974  58.475 -11.417  1.00 22.52           C  
-ATOM    942  O   PHE A 156      74.794  57.600 -11.074  1.00 23.36           O  
-ATOM    943  CB  PHE A 156      74.215  60.821 -12.286  1.00 18.69           C  
-ATOM    944  CG  PHE A 156      75.399  61.230 -11.427  1.00 22.55           C  
-ATOM    945  CD1 PHE A 156      75.449  60.895 -10.072  1.00 22.09           C  
-ATOM    946  CD2 PHE A 156      76.430  61.995 -11.967  1.00 20.37           C  
-ATOM    947  CE1 PHE A 156      76.516  61.328  -9.261  1.00 21.06           C  
-ATOM    948  CE2 PHE A 156      77.503  62.436 -11.175  1.00 22.46           C  
-ATOM    949  CZ  PHE A 156      77.540  62.099  -9.821  1.00 22.53           C  
-ATOM    950  N   ALA A 157      72.831  58.692 -10.767  1.00 23.40           N  
-ATOM    951  CA  ALA A 157      72.465  57.955  -9.563  1.00 22.92           C  
-ATOM    952  C   ALA A 157      72.464  56.450  -9.766  1.00 23.85           C  
-ATOM    953  O   ALA A 157      73.015  55.704  -8.964  1.00 23.71           O  
-ATOM    954  CB  ALA A 157      71.079  58.404  -9.078  1.00 23.72           C  
-ATOM    955  N   LYS A 158      71.821  55.999 -10.839  1.00 22.71           N  
-ATOM    956  CA  LYS A 158      71.739  54.580 -11.122  1.00 22.69           C  
-ATOM    957  C   LYS A 158      73.105  53.923 -11.345  1.00 23.13           C  
-ATOM    958  O   LYS A 158      73.388  52.851 -10.813  1.00 23.00           O  
-ATOM    959  CB  LYS A 158      70.848  54.367 -12.351  1.00 26.16           C  
-ATOM    960  CG  LYS A 158      70.537  52.913 -12.673  1.00 34.22           C  
-ATOM    961  CD  LYS A 158      69.520  52.812 -13.826  1.00 39.42           C  
-ATOM    962  CE  LYS A 158      69.067  51.369 -14.069  1.00 44.22           C  
-ATOM    963  NZ  LYS A 158      68.050  51.224 -15.175  1.00 44.54           N  
-ATOM    964  N   THR A 159      73.952  54.557 -12.141  1.00 21.95           N  
-ATOM    965  CA  THR A 159      75.257  53.967 -12.416  1.00 21.90           C  
-ATOM    966  C   THR A 159      76.178  54.049 -11.180  1.00 21.60           C  
-ATOM    967  O   THR A 159      76.932  53.116 -10.898  1.00 22.67           O  
-ATOM    968  CB  THR A 159      75.905  54.651 -13.618  1.00 21.76           C  
-ATOM    969  OG1 THR A 159      75.984  56.056 -13.372  1.00 20.81           O  
-ATOM    970  CG2 THR A 159      75.065  54.399 -14.899  1.00 19.90           C  
-ATOM    971  N   ALA A 160      76.103  55.151 -10.439  1.00 23.56           N  
-ATOM    972  CA  ALA A 160      76.917  55.292  -9.234  1.00 22.76           C  
-ATOM    973  C   ALA A 160      76.532  54.217  -8.215  1.00 22.54           C  
-ATOM    974  O   ALA A 160      77.397  53.568  -7.632  1.00 22.20           O  
-ATOM    975  CB  ALA A 160      76.759  56.692  -8.633  1.00 21.79           C  
-ATOM    976  N   VAL A 161      75.239  53.999  -8.002  1.00 24.03           N  
-ATOM    977  CA  VAL A 161      74.828  52.974  -7.049  1.00 22.92           C  
-ATOM    978  C   VAL A 161      75.223  51.596  -7.561  1.00 24.43           C  
-ATOM    979  O   VAL A 161      75.486  50.674  -6.777  1.00 24.65           O  
-ATOM    980  CB  VAL A 161      73.306  53.028  -6.781  1.00 25.68           C  
-ATOM    981  CG1 VAL A 161      72.903  51.932  -5.811  1.00 26.97           C  
-ATOM    982  CG2 VAL A 161      72.950  54.380  -6.213  1.00 25.62           C  
-ATOM    983  N   LYS A 162      75.284  51.437  -8.879  1.00 23.97           N  
-ATOM    984  CA  LYS A 162      75.708  50.146  -9.422  1.00 25.03           C  
-ATOM    985  C   LYS A 162      77.186  49.934  -9.030  1.00 22.79           C  
-ATOM    986  O   LYS A 162      77.593  48.832  -8.664  1.00 21.96           O  
-ATOM    987  CB  LYS A 162      75.532  50.130 -10.944  1.00 27.98           C  
-ATOM    988  CG  LYS A 162      76.126  48.906 -11.645  1.00 33.84           C  
-ATOM    989  CD  LYS A 162      75.557  47.591 -11.130  1.00 33.69           C  
-ATOM    990  CE  LYS A 162      75.638  46.486 -12.198  1.00 36.03           C  
-ATOM    991  NZ  LYS A 162      77.016  46.025 -12.608  1.00 30.84           N  
-ATOM    992  N   LEU A 163      77.995  50.987  -9.090  1.00 22.18           N  
-ATOM    993  CA  LEU A 163      79.407  50.828  -8.677  1.00 21.00           C  
-ATOM    994  C   LEU A 163      79.450  50.444  -7.178  1.00 20.34           C  
-ATOM    995  O   LEU A 163      80.195  49.558  -6.756  1.00 21.18           O  
-ATOM    996  CB  LEU A 163      80.163  52.142  -8.894  1.00 19.30           C  
-ATOM    997  CG  LEU A 163      80.332  52.523 -10.369  1.00 22.80           C  
-ATOM    998  CD1 LEU A 163      80.931  53.903 -10.490  1.00 18.66           C  
-ATOM    999  CD2 LEU A 163      81.206  51.491 -11.050  1.00 20.37           C  
-ATOM   1000  N   LEU A 164      78.644  51.136  -6.381  1.00 20.81           N  
-ATOM   1001  CA  LEU A 164      78.566  50.877  -4.945  1.00 20.77           C  
-ATOM   1002  C   LEU A 164      78.201  49.424  -4.636  1.00 22.04           C  
-ATOM   1003  O   LEU A 164      78.836  48.775  -3.796  1.00 22.52           O  
-ATOM   1004  CB  LEU A 164      77.535  51.828  -4.299  1.00 19.74           C  
-ATOM   1005  CG  LEU A 164      77.343  51.641  -2.774  1.00 20.19           C  
-ATOM   1006  CD1 LEU A 164      77.227  52.976  -2.086  1.00 16.81           C  
-ATOM   1007  CD2 LEU A 164      76.115  50.790  -2.512  1.00 23.14           C  
-ATOM   1008  N   GLN A 165      77.195  48.895  -5.335  1.00 21.97           N  
-ATOM   1009  CA  GLN A 165      76.748  47.530  -5.077  1.00 21.30           C  
-ATOM   1010  C   GLN A 165      77.739  46.477  -5.499  1.00 20.02           C  
-ATOM   1011  O   GLN A 165      77.798  45.369  -4.938  1.00 20.45           O  
-ATOM   1012  CB  GLN A 165      75.387  47.279  -5.747  1.00 24.95           C  
-ATOM   1013  CG  GLN A 165      75.396  47.041  -7.258  1.00 28.40           C  
-ATOM   1014  CD  GLN A 165      73.970  46.800  -7.801  1.00 33.29           C  
-ATOM   1015  OE1 GLN A 165      73.072  47.635  -7.630  1.00 33.62           O  
-ATOM   1016  NE2 GLN A 165      73.767  45.652  -8.434  1.00 34.29           N  
-ATOM   1017  N   ASP A 166      78.535  46.808  -6.501  1.00 19.41           N  
-ATOM   1018  CA  ASP A 166      79.515  45.848  -6.972  1.00 16.75           C  
-ATOM   1019  C   ASP A 166      80.848  45.943  -6.250  1.00 17.53           C  
-ATOM   1020  O   ASP A 166      81.446  44.921  -5.920  1.00 17.50           O  
-ATOM   1021  CB  ASP A 166      79.801  46.065  -8.461  1.00 19.08           C  
-ATOM   1022  CG  ASP A 166      78.736  45.460  -9.356  1.00 20.42           C  
-ATOM   1023  OD1 ASP A 166      78.020  44.529  -8.910  1.00 20.33           O  
-ATOM   1024  OD2 ASP A 166      78.653  45.915 -10.504  1.00 21.85           O  
-ATOM   1025  N   LEU A 167      81.305  47.173  -6.031  1.00 17.10           N  
-ATOM   1026  CA  LEU A 167      82.612  47.419  -5.433  1.00 19.22           C  
-ATOM   1027  C   LEU A 167      82.714  47.441  -3.907  1.00 19.65           C  
-ATOM   1028  O   LEU A 167      83.823  47.473  -3.374  1.00 20.65           O  
-ATOM   1029  CB  LEU A 167      83.203  48.705  -6.049  1.00 17.08           C  
-ATOM   1030  CG  LEU A 167      83.245  48.638  -7.601  1.00 17.72           C  
-ATOM   1031  CD1 LEU A 167      83.671  49.959  -8.212  1.00 16.41           C  
-ATOM   1032  CD2 LEU A 167      84.221  47.553  -8.052  1.00 14.71           C  
-ATOM   1033  N   GLY A 168      81.577  47.418  -3.208  1.00 19.24           N  
-ATOM   1034  CA  GLY A 168      81.584  47.405  -1.747  1.00 20.03           C  
-ATOM   1035  C   GLY A 168      81.732  48.753  -1.039  1.00 21.12           C  
-ATOM   1036  O   GLY A 168      82.344  48.836   0.032  1.00 20.49           O  
-ATOM   1037  N   PHE A 169      81.178  49.815  -1.612  1.00 20.13           N  
-ATOM   1038  CA  PHE A 169      81.295  51.120  -0.970  1.00 18.89           C  
-ATOM   1039  C   PHE A 169      80.186  51.337   0.043  1.00 22.50           C  
-ATOM   1040  O   PHE A 169      79.127  50.677  -0.008  1.00 21.18           O  
-ATOM   1041  CB  PHE A 169      81.261  52.238  -2.005  1.00 18.71           C  
-ATOM   1042  CG  PHE A 169      82.451  52.239  -2.934  1.00 22.40           C  
-ATOM   1043  CD1 PHE A 169      83.736  52.377  -2.428  1.00 22.55           C  
-ATOM   1044  CD2 PHE A 169      82.286  52.114  -4.307  1.00 21.01           C  
-ATOM   1045  CE1 PHE A 169      84.849  52.395  -3.282  1.00 25.12           C  
-ATOM   1046  CE2 PHE A 169      83.391  52.131  -5.169  1.00 22.10           C  
-ATOM   1047  CZ  PHE A 169      84.670  52.272  -4.651  1.00 20.97           C  
-ATOM   1048  N   ASP A 170      80.429  52.272   0.955  1.00 20.84           N  
-ATOM   1049  CA  ASP A 170      79.465  52.636   1.992  1.00 21.25           C  
-ATOM   1050  C   ASP A 170      78.719  53.897   1.639  1.00 20.55           C  
-ATOM   1051  O   ASP A 170      77.875  54.360   2.400  1.00 20.18           O  
-ATOM   1052  CB  ASP A 170      80.187  52.856   3.315  1.00 18.98           C  
-ATOM   1053  CG  ASP A 170      80.777  51.604   3.824  1.00 18.80           C  
-ATOM   1054  OD1 ASP A 170      80.026  50.787   4.407  1.00 19.27           O  
-ATOM   1055  OD2 ASP A 170      81.980  51.403   3.599  1.00 18.07           O  
-ATOM   1056  N   GLY A 171      79.032  54.463   0.485  1.00 20.31           N  
-ATOM   1057  CA  GLY A 171      78.383  55.693   0.116  1.00 17.01           C  
-ATOM   1058  C   GLY A 171      79.104  56.381  -1.020  1.00 18.25           C  
-ATOM   1059  O   GLY A 171      80.052  55.837  -1.597  1.00 20.64           O  
-ATOM   1060  N   LEU A 172      78.666  57.596  -1.307  1.00 15.93           N  
-ATOM   1061  CA  LEU A 172      79.184  58.363  -2.423  1.00 16.98           C  
-ATOM   1062  C   LEU A 172      79.485  59.767  -2.009  1.00 17.58           C  
-ATOM   1063  O   LEU A 172      78.699  60.388  -1.284  1.00 21.61           O  
-ATOM   1064  CB  LEU A 172      78.130  58.409  -3.537  1.00 14.27           C  
-ATOM   1065  CG  LEU A 172      77.608  57.050  -4.010  1.00 18.68           C  
-ATOM   1066  CD1 LEU A 172      76.397  57.228  -4.916  1.00 18.96           C  
-ATOM   1067  CD2 LEU A 172      78.711  56.311  -4.744  1.00 15.49           C  
-ATOM   1068  N   ASP A 173      80.609  60.278  -2.499  1.00 17.06           N  
-ATOM   1069  CA  ASP A 173      81.033  61.645  -2.217  1.00 16.70           C  
-ATOM   1070  C   ASP A 173      81.107  62.351  -3.577  1.00 18.46           C  
-ATOM   1071  O   ASP A 173      81.733  61.843  -4.520  1.00 18.78           O  
-ATOM   1072  CB  ASP A 173      82.413  61.636  -1.545  1.00 16.56           C  
-ATOM   1073  CG  ASP A 173      83.027  63.012  -1.456  1.00 19.01           C  
-ATOM   1074  OD1 ASP A 173      82.452  63.879  -0.755  1.00 17.92           O  
-ATOM   1075  OD2 ASP A 173      84.083  63.243  -2.088  1.00 18.71           O  
-ATOM   1076  N   ILE A 174      80.456  63.499  -3.697  1.00 18.54           N  
-ATOM   1077  CA  ILE A 174      80.460  64.225  -4.960  1.00 18.84           C  
-ATOM   1078  C   ILE A 174      81.278  65.493  -4.817  1.00 19.55           C  
-ATOM   1079  O   ILE A 174      81.000  66.335  -3.955  1.00 19.83           O  
-ATOM   1080  CB  ILE A 174      79.028  64.556  -5.396  1.00 20.44           C  
-ATOM   1081  CG1 ILE A 174      78.239  63.246  -5.549  1.00 23.48           C  
-ATOM   1082  CG2 ILE A 174      79.055  65.387  -6.684  1.00 16.68           C  
-ATOM   1083  CD1 ILE A 174      76.733  63.459  -5.847  1.00 28.25           C  
-ATOM   1084  N   ASP A 175      82.292  65.612  -5.675  1.00 17.98           N  
-ATOM   1085  CA  ASP A 175      83.229  66.732  -5.656  1.00 18.41           C  
-ATOM   1086  C   ASP A 175      83.129  67.516  -6.956  1.00 20.75           C  
-ATOM   1087  O   ASP A 175      83.850  67.241  -7.938  1.00 19.27           O  
-ATOM   1088  CB  ASP A 175      84.666  66.211  -5.488  1.00 19.03           C  
-ATOM   1089  CG  ASP A 175      84.869  65.452  -4.183  1.00 24.23           C  
-ATOM   1090  OD1 ASP A 175      86.043  65.079  -3.905  1.00 23.99           O  
-ATOM   1091  OD2 ASP A 175      83.863  65.218  -3.447  1.00 19.64           O  
-ATOM   1092  N   TRP A 176      82.223  68.479  -6.948  1.00 18.40           N  
-ATOM   1093  CA  TRP A 176      81.973  69.310  -8.105  1.00 19.82           C  
-ATOM   1094  C   TRP A 176      82.588  70.674  -7.851  1.00 20.58           C  
-ATOM   1095  O   TRP A 176      82.098  71.477  -7.024  1.00 20.33           O  
-ATOM   1096  CB  TRP A 176      80.448  69.383  -8.340  1.00 21.82           C  
-ATOM   1097  CG  TRP A 176      79.972  70.271  -9.480  1.00 21.44           C  
-ATOM   1098  CD1 TRP A 176      80.694  71.200 -10.156  1.00 21.38           C  
-ATOM   1099  CD2 TRP A 176      78.639  70.332 -10.013  1.00 22.04           C  
-ATOM   1100  NE1 TRP A 176      79.900  71.842 -11.078  1.00 22.07           N  
-ATOM   1101  CE2 TRP A 176      78.633  71.327 -11.009  1.00 21.72           C  
-ATOM   1102  CE3 TRP A 176      77.446  69.636  -9.737  1.00 23.95           C  
-ATOM   1103  CZ2 TRP A 176      77.476  71.653 -11.742  1.00 23.15           C  
-ATOM   1104  CZ3 TRP A 176      76.286  69.959 -10.467  1.00 23.96           C  
-ATOM   1105  CH2 TRP A 176      76.315  70.959 -11.453  1.00 23.57           C  
-ATOM   1106  N   GLU A 177      83.707  70.922  -8.523  1.00 17.94           N  
-ATOM   1107  CA  GLU A 177      84.382  72.198  -8.393  1.00 21.86           C  
-ATOM   1108  C   GLU A 177      84.278  72.944  -9.732  1.00 25.09           C  
-ATOM   1109  O   GLU A 177      85.114  72.721 -10.609  1.00 24.48           O  
-ATOM   1110  CB  GLU A 177      85.863  71.995  -8.031  1.00 24.08           C  
-ATOM   1111  CG  GLU A 177      86.087  71.459  -6.613  1.00 25.14           C  
-ATOM   1112  CD  GLU A 177      85.959  69.954  -6.537  1.00 30.27           C  
-ATOM   1113  OE1 GLU A 177      85.237  69.454  -5.646  1.00 33.39           O  
-ATOM   1114  OE2 GLU A 177      86.588  69.269  -7.367  1.00 30.28           O  
-ATOM   1115  N   TYR A 178      83.288  73.826  -9.904  1.00 23.82           N  
-ATOM   1116  CA  TYR A 178      82.260  74.133  -8.913  1.00 26.02           C  
-ATOM   1117  C   TYR A 178      81.019  74.610  -9.660  1.00 27.30           C  
-ATOM   1118  O   TYR A 178      81.099  75.061 -10.813  1.00 28.57           O  
-ATOM   1119  CB  TYR A 178      82.660  75.298  -7.998  1.00 27.56           C  
-ATOM   1120  CG  TYR A 178      84.032  75.241  -7.360  1.00 31.57           C  
-ATOM   1121  CD1 TYR A 178      85.149  75.726  -8.032  1.00 33.52           C  
-ATOM   1122  CD2 TYR A 178      84.207  74.750  -6.054  1.00 31.89           C  
-ATOM   1123  CE1 TYR A 178      86.409  75.737  -7.424  1.00 34.77           C  
-ATOM   1124  CE2 TYR A 178      85.467  74.753  -5.437  1.00 32.12           C  
-ATOM   1125  CZ  TYR A 178      86.555  75.250  -6.127  1.00 34.66           C  
-ATOM   1126  OH  TYR A 178      87.792  75.296  -5.521  1.00 38.83           O  
-ATOM   1127  N   PRO A 179      79.850  74.522  -9.019  1.00 26.13           N  
-ATOM   1128  CA  PRO A 179      78.664  75.001  -9.740  1.00 26.40           C  
-ATOM   1129  C   PRO A 179      78.957  76.468 -10.039  1.00 27.28           C  
-ATOM   1130  O   PRO A 179      79.429  77.189  -9.154  1.00 26.21           O  
-ATOM   1131  CB  PRO A 179      77.557  74.812  -8.720  1.00 25.77           C  
-ATOM   1132  CG  PRO A 179      77.993  73.526  -8.010  1.00 23.54           C  
-ATOM   1133  CD  PRO A 179      79.482  73.778  -7.799  1.00 23.04           C  
-ATOM   1134  N   GLU A 180      78.708  76.901 -11.279  1.00 26.35           N  
-ATOM   1135  CA  GLU A 180      79.010  78.274 -11.688  1.00 29.62           C  
-ATOM   1136  C   GLU A 180      77.840  79.253 -11.680  1.00 29.65           C  
-ATOM   1137  O   GLU A 180      78.041  80.456 -11.790  1.00 32.92           O  
-ATOM   1138  CB  GLU A 180      79.617  78.266 -13.098  1.00 35.15           C  
-ATOM   1139  CG  GLU A 180      80.664  77.186 -13.331  1.00 40.64           C  
-ATOM   1140  CD  GLU A 180      81.160  77.142 -14.769  1.00 44.88           C  
-ATOM   1141  OE1 GLU A 180      80.345  76.907 -15.695  1.00 47.31           O  
-ATOM   1142  OE2 GLU A 180      82.376  77.342 -14.970  1.00 49.01           O  
-ATOM   1143  N   ASN A 181      76.625  78.745 -11.567  1.00 30.12           N  
-ATOM   1144  CA  ASN A 181      75.462  79.616 -11.567  1.00 31.03           C  
-ATOM   1145  C   ASN A 181      74.270  78.968 -10.904  1.00 30.27           C  
-ATOM   1146  O   ASN A 181      74.312  77.799 -10.519  1.00 29.59           O  
-ATOM   1147  CB  ASN A 181      75.100  80.036 -12.998  1.00 31.47           C  
-ATOM   1148  CG  ASN A 181      74.879  78.858 -13.913  1.00 29.64           C  
-ATOM   1149  OD1 ASN A 181      74.158  77.916 -13.580  1.00 30.23           O  
-ATOM   1150  ND2 ASN A 181      75.494  78.906 -15.083  1.00 30.91           N  
-ATOM   1151  N   ASP A 182      73.198  79.737 -10.776  1.00 31.62           N  
-ATOM   1152  CA  ASP A 182      72.000  79.253 -10.119  1.00 32.74           C  
-ATOM   1153  C   ASP A 182      71.447  77.964 -10.707  1.00 31.98           C  
-ATOM   1154  O   ASP A 182      71.007  77.074  -9.981  1.00 30.57           O  
-ATOM   1155  CB  ASP A 182      70.913  80.336 -10.134  1.00 37.01           C  
-ATOM   1156  CG  ASP A 182      69.787  80.026  -9.176  1.00 39.20           C  
-ATOM   1157  OD1 ASP A 182      70.077  79.910  -7.970  1.00 44.46           O  
-ATOM   1158  OD2 ASP A 182      68.627  79.874  -9.605  1.00 43.35           O  
-ATOM   1159  N   GLN A 183      71.471  77.859 -12.029  1.00 31.92           N  
-ATOM   1160  CA  GLN A 183      70.945  76.677 -12.689  1.00 30.11           C  
-ATOM   1161  C   GLN A 183      71.705  75.423 -12.261  1.00 28.43           C  
-ATOM   1162  O   GLN A 183      71.117  74.375 -11.966  1.00 26.87           O  
-ATOM   1163  CB  GLN A 183      71.061  76.842 -14.198  1.00 33.64           C  
-ATOM   1164  CG  GLN A 183      70.427  75.712 -14.942  1.00 37.66           C  
-ATOM   1165  CD  GLN A 183      68.951  75.616 -14.638  1.00 41.67           C  
-ATOM   1166  OE1 GLN A 183      68.190  76.551 -14.901  1.00 42.62           O  
-ATOM   1167  NE2 GLN A 183      68.535  74.490 -14.071  1.00 44.48           N  
-ATOM   1168  N   GLN A 184      73.023  75.544 -12.262  1.00 26.62           N  
-ATOM   1169  CA  GLN A 184      73.887  74.437 -11.864  1.00 27.05           C  
-ATOM   1170  C   GLN A 184      73.657  74.147 -10.375  1.00 25.49           C  
-ATOM   1171  O   GLN A 184      73.527  72.992  -9.971  1.00 26.45           O  
-ATOM   1172  CB  GLN A 184      75.343  74.815 -12.153  1.00 24.90           C  
-ATOM   1173  CG  GLN A 184      75.618  74.944 -13.659  1.00 26.03           C  
-ATOM   1174  CD  GLN A 184      77.079  75.153 -13.968  1.00 29.54           C  
-ATOM   1175  OE1 GLN A 184      77.941  74.756 -13.190  1.00 28.75           O  
-ATOM   1176  NE2 GLN A 184      77.374  75.762 -15.123  1.00 26.67           N  
-ATOM   1177  N   ALA A 185      73.569  75.202  -9.567  1.00 26.62           N  
-ATOM   1178  CA  ALA A 185      73.339  75.017  -8.132  1.00 27.61           C  
-ATOM   1179  C   ALA A 185      72.055  74.228  -7.942  1.00 28.19           C  
-ATOM   1180  O   ALA A 185      71.993  73.304  -7.130  1.00 28.57           O  
-ATOM   1181  CB  ALA A 185      73.255  76.361  -7.431  1.00 26.42           C  
-ATOM   1182  N   ASN A 186      71.027  74.578  -8.717  1.00 29.14           N  
-ATOM   1183  CA  ASN A 186      69.749  73.879  -8.633  1.00 26.31           C  
-ATOM   1184  C   ASN A 186      69.868  72.434  -9.077  1.00 23.58           C  
-ATOM   1185  O   ASN A 186      69.325  71.541  -8.444  1.00 23.52           O  
-ATOM   1186  CB  ASN A 186      68.709  74.590  -9.504  1.00 31.65           C  
-ATOM   1187  CG  ASN A 186      68.009  75.696  -8.764  1.00 37.71           C  
-ATOM   1188  OD1 ASN A 186      67.765  76.776  -9.309  1.00 43.10           O  
-ATOM   1189  ND2 ASN A 186      67.669  75.432  -7.506  1.00 37.74           N  
-ATOM   1190  N   ASP A 187      70.556  72.216 -10.192  1.00 21.64           N  
-ATOM   1191  CA  ASP A 187      70.748  70.868 -10.710  1.00 23.44           C  
-ATOM   1192  C   ASP A 187      71.546  70.027  -9.717  1.00 20.94           C  
-ATOM   1193  O   ASP A 187      71.292  68.829  -9.555  1.00 22.91           O  
-ATOM   1194  CB  ASP A 187      71.468  70.927 -12.067  1.00 24.74           C  
-ATOM   1195  CG  ASP A 187      70.635  71.650 -13.137  1.00 32.19           C  
-ATOM   1196  OD1 ASP A 187      69.390  71.712 -12.967  1.00 27.82           O  
-ATOM   1197  OD2 ASP A 187      71.218  72.133 -14.132  1.00 28.95           O  
-ATOM   1198  N   PHE A 188      72.497  70.660  -9.040  1.00 21.50           N  
-ATOM   1199  CA  PHE A 188      73.308  69.926  -8.066  1.00 21.58           C  
-ATOM   1200  C   PHE A 188      72.358  69.354  -7.012  1.00 22.84           C  
-ATOM   1201  O   PHE A 188      72.417  68.163  -6.669  1.00 24.00           O  
-ATOM   1202  CB  PHE A 188      74.359  70.860  -7.432  1.00 19.07           C  
-ATOM   1203  CG  PHE A 188      75.468  70.124  -6.689  1.00 19.60           C  
-ATOM   1204  CD1 PHE A 188      75.555  68.730  -6.729  1.00 19.46           C  
-ATOM   1205  CD2 PHE A 188      76.409  70.826  -5.962  1.00 19.94           C  
-ATOM   1206  CE1 PHE A 188      76.574  68.055  -6.044  1.00 23.11           C  
-ATOM   1207  CE2 PHE A 188      77.426  70.161  -5.278  1.00 21.12           C  
-ATOM   1208  CZ  PHE A 188      77.502  68.779  -5.323  1.00 20.16           C  
-ATOM   1209  N   VAL A 189      71.441  70.192  -6.529  1.00 24.14           N  
-ATOM   1210  CA  VAL A 189      70.455  69.732  -5.546  1.00 23.52           C  
-ATOM   1211  C   VAL A 189      69.612  68.606  -6.107  1.00 21.61           C  
-ATOM   1212  O   VAL A 189      69.356  67.608  -5.443  1.00 22.31           O  
-ATOM   1213  CB  VAL A 189      69.503  70.879  -5.128  1.00 25.84           C  
-ATOM   1214  CG1 VAL A 189      68.297  70.318  -4.385  1.00 23.57           C  
-ATOM   1215  CG2 VAL A 189      70.254  71.869  -4.246  1.00 22.52           C  
-ATOM   1216  N   LEU A 190      69.168  68.773  -7.349  1.00 23.97           N  
-ATOM   1217  CA  LEU A 190      68.329  67.752  -7.966  1.00 23.29           C  
-ATOM   1218  C   LEU A 190      69.095  66.441  -8.088  1.00 22.06           C  
-ATOM   1219  O   LEU A 190      68.544  65.356  -7.895  1.00 20.39           O  
-ATOM   1220  CB  LEU A 190      67.861  68.238  -9.334  1.00 24.30           C  
-ATOM   1221  CG  LEU A 190      66.926  69.451  -9.257  1.00 25.44           C  
-ATOM   1222  CD1 LEU A 190      66.465  69.869 -10.659  1.00 27.76           C  
-ATOM   1223  CD2 LEU A 190      65.711  69.093  -8.397  1.00 25.07           C  
-ATOM   1224  N   LEU A 191      70.379  66.552  -8.410  1.00 22.46           N  
-ATOM   1225  CA  LEU A 191      71.251  65.382  -8.534  1.00 21.37           C  
-ATOM   1226  C   LEU A 191      71.359  64.645  -7.188  1.00 22.14           C  
-ATOM   1227  O   LEU A 191      71.159  63.424  -7.097  1.00 24.35           O  
-ATOM   1228  CB  LEU A 191      72.643  65.865  -8.955  1.00 21.16           C  
-ATOM   1229  CG  LEU A 191      73.732  64.819  -9.152  1.00 23.87           C  
-ATOM   1230  CD1 LEU A 191      73.283  63.811 -10.224  1.00 22.33           C  
-ATOM   1231  CD2 LEU A 191      75.041  65.542  -9.552  1.00 22.87           C  
-ATOM   1232  N   LEU A 192      71.693  65.402  -6.144  1.00 22.55           N  
-ATOM   1233  CA  LEU A 192      71.854  64.823  -4.811  1.00 21.62           C  
-ATOM   1234  C   LEU A 192      70.617  64.055  -4.403  1.00 23.42           C  
-ATOM   1235  O   LEU A 192      70.695  62.952  -3.847  1.00 22.75           O  
-ATOM   1236  CB  LEU A 192      72.138  65.940  -3.809  1.00 20.13           C  
-ATOM   1237  CG  LEU A 192      73.546  66.529  -3.909  1.00 24.60           C  
-ATOM   1238  CD1 LEU A 192      73.683  67.802  -3.055  1.00 20.45           C  
-ATOM   1239  CD2 LEU A 192      74.537  65.451  -3.465  1.00 24.80           C  
-ATOM   1240  N   LYS A 193      69.456  64.638  -4.694  1.00 26.20           N  
-ATOM   1241  CA  LYS A 193      68.200  63.999  -4.332  1.00 26.61           C  
-ATOM   1242  C   LYS A 193      68.070  62.684  -5.055  1.00 26.86           C  
-ATOM   1243  O   LYS A 193      67.675  61.662  -4.486  1.00 26.90           O  
-ATOM   1244  CB  LYS A 193      67.031  64.918  -4.687  1.00 31.36           C  
-ATOM   1245  CG  LYS A 193      65.690  64.352  -4.280  1.00 38.35           C  
-ATOM   1246  CD  LYS A 193      64.656  65.461  -4.084  1.00 43.51           C  
-ATOM   1247  CE  LYS A 193      63.310  64.862  -3.662  1.00 47.04           C  
-ATOM   1248  NZ  LYS A 193      62.825  63.882  -4.695  1.00 48.50           N  
-ATOM   1249  N   GLU A 194      68.420  62.708  -6.334  1.00 27.72           N  
-ATOM   1250  CA  GLU A 194      68.349  61.509  -7.135  1.00 25.82           C  
-ATOM   1251  C   GLU A 194      69.301  60.449  -6.563  1.00 23.68           C  
-ATOM   1252  O   GLU A 194      68.967  59.273  -6.486  1.00 23.87           O  
-ATOM   1253  CB  GLU A 194      68.713  61.875  -8.576  1.00 30.26           C  
-ATOM   1254  CG  GLU A 194      67.892  61.160  -9.620  1.00 34.95           C  
-ATOM   1255  CD  GLU A 194      66.388  61.301  -9.384  1.00 34.34           C  
-ATOM   1256  OE1 GLU A 194      65.822  62.395  -9.604  1.00 34.14           O  
-ATOM   1257  OE2 GLU A 194      65.784  60.302  -8.964  1.00 34.11           O  
-ATOM   1258  N   VAL A 195      70.492  60.858  -6.143  1.00 24.11           N  
-ATOM   1259  CA  VAL A 195      71.419  59.874  -5.593  1.00 21.97           C  
-ATOM   1260  C   VAL A 195      70.916  59.343  -4.248  1.00 22.18           C  
-ATOM   1261  O   VAL A 195      70.921  58.141  -3.997  1.00 23.27           O  
-ATOM   1262  CB  VAL A 195      72.804  60.489  -5.405  1.00 22.11           C  
-ATOM   1263  CG1 VAL A 195      73.724  59.472  -4.783  1.00 18.28           C  
-ATOM   1264  CG2 VAL A 195      73.342  60.963  -6.750  1.00 22.65           C  
-ATOM   1265  N   ARG A 196      70.478  60.250  -3.384  1.00 24.85           N  
-ATOM   1266  CA  ARG A 196      69.965  59.847  -2.075  1.00 24.62           C  
-ATOM   1267  C   ARG A 196      68.849  58.819  -2.246  1.00 25.98           C  
-ATOM   1268  O   ARG A 196      68.782  57.825  -1.528  1.00 27.23           O  
-ATOM   1269  CB  ARG A 196      69.432  61.070  -1.344  1.00 25.45           C  
-ATOM   1270  CG  ARG A 196      68.960  60.799   0.086  1.00 28.56           C  
-ATOM   1271  CD  ARG A 196      70.125  60.410   0.996  1.00 23.54           C  
-ATOM   1272  NE  ARG A 196      70.260  58.965   1.079  1.00 23.60           N  
-ATOM   1273  CZ  ARG A 196      71.271  58.340   1.662  1.00 23.49           C  
-ATOM   1274  NH1 ARG A 196      72.256  59.043   2.211  1.00 21.96           N  
-ATOM   1275  NH2 ARG A 196      71.268  57.012   1.733  1.00 19.57           N  
-ATOM   1276  N   THR A 197      67.955  59.063  -3.202  1.00 26.74           N  
-ATOM   1277  CA  THR A 197      66.849  58.131  -3.443  1.00 26.76           C  
-ATOM   1278  C   THR A 197      67.336  56.763  -3.936  1.00 24.24           C  
-ATOM   1279  O   THR A 197      66.851  55.712  -3.507  1.00 24.46           O  
-ATOM   1280  CB  THR A 197      65.871  58.719  -4.494  1.00 27.77           C  
-ATOM   1281  OG1 THR A 197      65.311  59.944  -3.992  1.00 28.46           O  
-ATOM   1282  CG2 THR A 197      64.758  57.731  -4.795  1.00 30.88           C  
-ATOM   1283  N   ALA A 198      68.311  56.760  -4.834  1.00 24.19           N  
-ATOM   1284  CA  ALA A 198      68.788  55.479  -5.361  1.00 25.31           C  
-ATOM   1285  C   ALA A 198      69.478  54.666  -4.269  1.00 23.15           C  
-ATOM   1286  O   ALA A 198      69.317  53.439  -4.178  1.00 23.79           O  
-ATOM   1287  CB  ALA A 198      69.730  55.715  -6.529  1.00 24.38           C  
-ATOM   1288  N   LEU A 199      70.244  55.352  -3.429  1.00 23.83           N  
-ATOM   1289  CA  LEU A 199      70.929  54.678  -2.326  1.00 21.19           C  
-ATOM   1290  C   LEU A 199      69.889  54.040  -1.406  1.00 21.55           C  
-ATOM   1291  O   LEU A 199      70.015  52.881  -1.005  1.00 22.15           O  
-ATOM   1292  CB  LEU A 199      71.755  55.703  -1.532  1.00 22.21           C  
-ATOM   1293  CG  LEU A 199      73.033  56.197  -2.237  1.00 19.66           C  
-ATOM   1294  CD1 LEU A 199      73.627  57.380  -1.481  1.00 21.71           C  
-ATOM   1295  CD2 LEU A 199      74.007  55.051  -2.321  1.00 22.34           C  
-ATOM   1296  N   ASP A 200      68.851  54.800  -1.074  1.00 23.48           N  
-ATOM   1297  CA  ASP A 200      67.820  54.271  -0.182  1.00 25.75           C  
-ATOM   1298  C   ASP A 200      67.110  53.059  -0.766  1.00 25.30           C  
-ATOM   1299  O   ASP A 200      66.865  52.079  -0.059  1.00 25.61           O  
-ATOM   1300  CB  ASP A 200      66.839  55.388   0.185  1.00 26.79           C  
-ATOM   1301  CG  ASP A 200      67.493  56.453   1.077  1.00 30.71           C  
-ATOM   1302  OD1 ASP A 200      68.484  56.106   1.756  1.00 34.02           O  
-ATOM   1303  OD2 ASP A 200      67.030  57.614   1.114  1.00 31.04           O  
-ATOM   1304  N   SER A 201      66.801  53.123  -2.062  1.00 25.83           N  
-ATOM   1305  CA  SER A 201      66.143  52.018  -2.747  1.00 25.98           C  
-ATOM   1306  C   SER A 201      67.044  50.806  -2.749  1.00 26.08           C  
-ATOM   1307  O   SER A 201      66.609  49.706  -2.418  1.00 22.62           O  
-ATOM   1308  CB  SER A 201      65.835  52.377  -4.203  1.00 28.46           C  
-ATOM   1309  OG  SER A 201      64.898  53.427  -4.260  1.00 40.64           O  
-ATOM   1310  N   TYR A 202      68.303  50.998  -3.146  1.00 26.23           N  
-ATOM   1311  CA  TYR A 202      69.236  49.875  -3.167  1.00 24.22           C  
-ATOM   1312  C   TYR A 202      69.312  49.265  -1.776  1.00 22.47           C  
-ATOM   1313  O   TYR A 202      69.267  48.042  -1.607  1.00 23.35           O  
-ATOM   1314  CB  TYR A 202      70.642  50.331  -3.589  1.00 25.27           C  
-ATOM   1315  CG  TYR A 202      71.682  49.271  -3.318  1.00 25.03           C  
-ATOM   1316  CD1 TYR A 202      71.776  48.140  -4.131  1.00 22.05           C  
-ATOM   1317  CD2 TYR A 202      72.504  49.346  -2.193  1.00 23.38           C  
-ATOM   1318  CE1 TYR A 202      72.653  47.106  -3.824  1.00 22.09           C  
-ATOM   1319  CE2 TYR A 202      73.379  48.322  -1.879  1.00 21.39           C  
-ATOM   1320  CZ  TYR A 202      73.450  47.213  -2.682  1.00 20.10           C  
-ATOM   1321  OH  TYR A 202      74.273  46.177  -2.348  1.00 22.28           O  
-ATOM   1322  N   SER A 203      69.420  50.121  -0.768  1.00 24.00           N  
-ATOM   1323  CA  SER A 203      69.544  49.608   0.595  1.00 24.09           C  
-ATOM   1324  C   SER A 203      68.314  48.841   1.052  1.00 24.83           C  
-ATOM   1325  O   SER A 203      68.425  47.777   1.653  1.00 23.36           O  
-ATOM   1326  CB  SER A 203      69.812  50.744   1.572  1.00 24.43           C  
-ATOM   1327  OG  SER A 203      69.880  50.208   2.872  1.00 23.63           O  
-ATOM   1328  N   ALA A 204      67.138  49.395   0.774  1.00 28.00           N  
-ATOM   1329  CA  ALA A 204      65.896  48.730   1.163  1.00 29.95           C  
-ATOM   1330  C   ALA A 204      65.831  47.343   0.545  1.00 30.05           C  
-ATOM   1331  O   ALA A 204      65.315  46.416   1.148  1.00 32.24           O  
-ATOM   1332  CB  ALA A 204      64.692  49.561   0.717  1.00 29.62           C  
-ATOM   1333  N   ALA A 205      66.389  47.186  -0.650  1.00 30.65           N  
-ATOM   1334  CA  ALA A 205      66.346  45.892  -1.322  1.00 29.41           C  
-ATOM   1335  C   ALA A 205      67.522  44.960  -1.053  1.00 30.34           C  
-ATOM   1336  O   ALA A 205      67.359  43.737  -1.014  1.00 30.26           O  
-ATOM   1337  CB  ALA A 205      66.211  46.114  -2.833  1.00 30.63           C  
-ATOM   1338  N   ASN A 206      68.710  45.522  -0.856  1.00 29.76           N  
-ATOM   1339  CA  ASN A 206      69.887  44.681  -0.666  1.00 28.37           C  
-ATOM   1340  C   ASN A 206      70.758  44.931   0.561  1.00 30.16           C  
-ATOM   1341  O   ASN A 206      71.758  44.234   0.745  1.00 31.16           O  
-ATOM   1342  CB  ASN A 206      70.755  44.786  -1.915  1.00 28.41           C  
-ATOM   1343  CG  ASN A 206      70.026  44.323  -3.155  1.00 28.31           C  
-ATOM   1344  OD1 ASN A 206      69.790  43.136  -3.321  1.00 25.55           O  
-ATOM   1345  ND2 ASN A 206      69.658  45.259  -4.021  1.00 28.52           N  
-ATOM   1346  N   ALA A 207      70.405  45.905   1.394  1.00 29.90           N  
-ATOM   1347  CA  ALA A 207      71.222  46.188   2.587  1.00 32.26           C  
-ATOM   1348  C   ALA A 207      70.374  46.283   3.854  1.00 33.68           C  
-ATOM   1349  O   ALA A 207      70.786  46.891   4.846  1.00 34.38           O  
-ATOM   1350  CB  ALA A 207      72.014  47.493   2.393  1.00 29.48           C  
-ATOM   1351  N   GLY A 208      69.180  45.703   3.809  1.00 34.26           N  
-ATOM   1352  CA  GLY A 208      68.306  45.725   4.966  1.00 31.16           C  
-ATOM   1353  C   GLY A 208      68.145  47.106   5.563  1.00 30.52           C  
-ATOM   1354  O   GLY A 208      68.060  47.256   6.779  1.00 32.54           O  
-ATOM   1355  N   GLY A 209      68.105  48.126   4.718  1.00 27.39           N  
-ATOM   1356  CA  GLY A 209      67.941  49.468   5.234  1.00 26.33           C  
-ATOM   1357  C   GLY A 209      69.211  50.167   5.707  1.00 25.90           C  
-ATOM   1358  O   GLY A 209      69.135  51.294   6.184  1.00 26.84           O  
-ATOM   1359  N   GLN A 210      70.366  49.516   5.596  1.00 26.26           N  
-ATOM   1360  CA  GLN A 210      71.650  50.140   5.994  1.00 26.17           C  
-ATOM   1361  C   GLN A 210      71.692  51.567   5.428  1.00 23.88           C  
-ATOM   1362  O   GLN A 210      71.368  51.778   4.274  1.00 26.47           O  
-ATOM   1363  CB  GLN A 210      72.827  49.325   5.424  1.00 27.70           C  
-ATOM   1364  CG  GLN A 210      74.185  50.012   5.515  1.00 27.92           C  
-ATOM   1365  CD  GLN A 210      74.811  49.839   6.878  1.00 29.93           C  
-ATOM   1366  OE1 GLN A 210      74.193  49.281   7.785  1.00 29.00           O  
-ATOM   1367  NE2 GLN A 210      76.042  50.317   7.036  1.00 25.60           N  
-ATOM   1368  N   HIS A 211      72.068  52.543   6.242  1.00 23.32           N  
-ATOM   1369  CA  HIS A 211      72.124  53.914   5.748  1.00 24.05           C  
-ATOM   1370  C   HIS A 211      73.427  54.230   5.036  1.00 24.73           C  
-ATOM   1371  O   HIS A 211      74.451  54.429   5.694  1.00 23.09           O  
-ATOM   1372  CB  HIS A 211      71.966  54.927   6.881  1.00 23.66           C  
-ATOM   1373  CG  HIS A 211      72.047  56.358   6.436  1.00 25.89           C  
-ATOM   1374  ND1 HIS A 211      71.099  56.973   5.639  1.00 24.37           N  
-ATOM   1375  CD2 HIS A 211      72.998  57.287   6.660  1.00 26.02           C  
-ATOM   1376  CE1 HIS A 211      71.483  58.214   5.383  1.00 24.30           C  
-ATOM   1377  NE2 HIS A 211      72.636  58.428   5.988  1.00 25.24           N  
-ATOM   1378  N   PHE A 212      73.403  54.260   3.708  1.00 21.11           N  
-ATOM   1379  CA  PHE A 212      74.600  54.584   2.943  1.00 22.67           C  
-ATOM   1380  C   PHE A 212      74.743  56.082   2.927  1.00 21.64           C  
-ATOM   1381  O   PHE A 212      73.758  56.814   2.947  1.00 25.48           O  
-ATOM   1382  CB  PHE A 212      74.502  54.022   1.533  1.00 21.83           C  
-ATOM   1383  CG  PHE A 212      74.557  52.541   1.500  1.00 22.24           C  
-ATOM   1384  CD1 PHE A 212      75.685  51.863   1.962  1.00 19.25           C  
-ATOM   1385  CD2 PHE A 212      73.452  51.803   1.083  1.00 21.33           C  
-ATOM   1386  CE1 PHE A 212      75.710  50.467   2.014  1.00 20.93           C  
-ATOM   1387  CE2 PHE A 212      73.461  50.403   1.129  1.00 20.54           C  
-ATOM   1388  CZ  PHE A 212      74.578  49.725   1.591  1.00 21.72           C  
-ATOM   1389  N   LEU A 213      75.982  56.549   2.875  1.00 22.22           N  
-ATOM   1390  CA  LEU A 213      76.265  57.976   2.948  1.00 18.53           C  
-ATOM   1391  C   LEU A 213      76.335  58.724   1.636  1.00 20.03           C  
-ATOM   1392  O   LEU A 213      76.632  58.153   0.575  1.00 20.56           O  
-ATOM   1393  CB  LEU A 213      77.591  58.156   3.699  1.00 20.48           C  
-ATOM   1394  CG  LEU A 213      77.685  57.425   5.041  1.00 20.24           C  
-ATOM   1395  CD1 LEU A 213      79.148  57.370   5.563  1.00 16.98           C  
-ATOM   1396  CD2 LEU A 213      76.784  58.159   6.024  1.00 19.67           C  
-ATOM   1397  N   LEU A 214      76.073  60.017   1.721  1.00 17.78           N  
-ATOM   1398  CA  LEU A 214      76.147  60.889   0.569  1.00 19.54           C  
-ATOM   1399  C   LEU A 214      76.750  62.161   1.145  1.00 18.18           C  
-ATOM   1400  O   LEU A 214      76.197  62.756   2.073  1.00 19.35           O  
-ATOM   1401  CB  LEU A 214      74.742  61.152  -0.022  1.00 19.81           C  
-ATOM   1402  CG  LEU A 214      74.674  62.125  -1.212  1.00 23.42           C  
-ATOM   1403  CD1 LEU A 214      75.609  61.640  -2.337  1.00 22.56           C  
-ATOM   1404  CD2 LEU A 214      73.218  62.219  -1.733  1.00 20.78           C  
-ATOM   1405  N   THR A 215      77.913  62.546   0.622  1.00 18.45           N  
-ATOM   1406  CA  THR A 215      78.625  63.725   1.093  1.00 15.79           C  
-ATOM   1407  C   THR A 215      79.106  64.524  -0.106  1.00 17.72           C  
-ATOM   1408  O   THR A 215      78.952  64.089  -1.249  1.00 20.92           O  
-ATOM   1409  CB  THR A 215      79.881  63.318   1.875  1.00 18.71           C  
-ATOM   1410  OG1 THR A 215      80.794  62.653   0.983  1.00 17.78           O  
-ATOM   1411  CG2 THR A 215      79.524  62.366   3.014  1.00 13.88           C  
-ATOM   1412  N   VAL A 216      79.688  65.688   0.153  1.00 17.23           N  
-ATOM   1413  CA  VAL A 216      80.249  66.524  -0.908  1.00 18.72           C  
-ATOM   1414  C   VAL A 216      81.482  67.282  -0.433  1.00 20.28           C  
-ATOM   1415  O   VAL A 216      81.593  67.629   0.741  1.00 20.42           O  
-ATOM   1416  CB  VAL A 216      79.280  67.619  -1.389  1.00 18.46           C  
-ATOM   1417  CG1 VAL A 216      78.049  66.999  -2.035  1.00 18.93           C  
-ATOM   1418  CG2 VAL A 216      78.891  68.514  -0.198  1.00 21.19           C  
-ATOM   1419  N   ALA A 217      82.393  67.560  -1.362  1.00 18.88           N  
-ATOM   1420  CA  ALA A 217      83.561  68.366  -1.051  1.00 19.98           C  
-ATOM   1421  C   ALA A 217      82.978  69.768  -1.221  1.00 21.54           C  
-ATOM   1422  O   ALA A 217      82.258  70.024  -2.186  1.00 24.23           O  
-ATOM   1423  CB  ALA A 217      84.694  68.106  -2.091  1.00 20.56           C  
-ATOM   1424  N   SER A 218      83.300  70.675  -0.311  1.00 20.97           N  
-ATOM   1425  CA  SER A 218      82.737  72.016  -0.345  1.00 19.65           C  
-ATOM   1426  C   SER A 218      83.784  73.103  -0.434  1.00 20.43           C  
-ATOM   1427  O   SER A 218      84.861  73.004   0.170  1.00 19.08           O  
-ATOM   1428  CB ASER A 218      81.856  72.242   0.888  0.50 19.67           C  
-ATOM   1429  OG ASER A 218      82.554  71.917   2.074  0.50 17.09           O  
-ATOM   1430  CB BSER A 218      81.882  72.223   0.907  0.50 20.76           C  
-ATOM   1431  OG BSER A 218      81.144  71.040   1.195  0.50 21.85           O  
-ATOM   1432  N   PRO A 219      83.472  74.180  -1.178  1.00 19.93           N  
-ATOM   1433  CA  PRO A 219      84.406  75.294  -1.352  1.00 19.11           C  
-ATOM   1434  C   PRO A 219      84.588  76.197  -0.150  1.00 19.78           C  
-ATOM   1435  O   PRO A 219      83.683  76.361   0.654  1.00 18.70           O  
-ATOM   1436  CB  PRO A 219      83.817  76.051  -2.549  1.00 20.94           C  
-ATOM   1437  CG  PRO A 219      82.329  75.874  -2.332  1.00 21.85           C  
-ATOM   1438  CD  PRO A 219      82.228  74.403  -1.943  1.00 21.51           C  
-ATOM   1439  N   ALA A 220      85.779  76.784  -0.050  1.00 19.27           N  
-ATOM   1440  CA  ALA A 220      86.090  77.741   1.003  1.00 21.25           C  
-ATOM   1441  C   ALA A 220      85.989  79.161   0.393  1.00 21.51           C  
-ATOM   1442  O   ALA A 220      85.948  80.159   1.116  1.00 21.94           O  
-ATOM   1443  CB  ALA A 220      87.529  77.491   1.557  1.00 18.02           C  
-ATOM   1444  N   GLY A 221      85.955  79.249  -0.936  1.00 20.32           N  
-ATOM   1445  CA  GLY A 221      85.894  80.561  -1.584  1.00 20.24           C  
-ATOM   1446  C   GLY A 221      84.512  81.187  -1.436  1.00 20.86           C  
-ATOM   1447  O   GLY A 221      83.529  80.585  -1.848  1.00 20.19           O  
-ATOM   1448  N   PRO A 222      84.410  82.391  -0.851  1.00 21.76           N  
-ATOM   1449  CA  PRO A 222      83.100  83.042  -0.670  1.00 24.15           C  
-ATOM   1450  C   PRO A 222      82.244  83.068  -1.933  1.00 25.33           C  
-ATOM   1451  O   PRO A 222      81.062  82.731  -1.893  1.00 25.45           O  
-ATOM   1452  CB  PRO A 222      83.468  84.450  -0.188  1.00 20.82           C  
-ATOM   1453  CG  PRO A 222      84.751  84.226   0.573  1.00 23.40           C  
-ATOM   1454  CD  PRO A 222      85.502  83.241  -0.334  1.00 21.64           C  
-ATOM   1455  N   ASP A 223      82.846  83.455  -3.053  1.00 27.45           N  
-ATOM   1456  CA  ASP A 223      82.120  83.506  -4.317  1.00 31.41           C  
-ATOM   1457  C   ASP A 223      81.512  82.157  -4.695  1.00 30.51           C  
-ATOM   1458  O   ASP A 223      80.379  82.082  -5.172  1.00 30.75           O  
-ATOM   1459  CB  ASP A 223      83.045  83.994  -5.427  1.00 36.50           C  
-ATOM   1460  CG  ASP A 223      83.498  85.424  -5.209  1.00 41.52           C  
-ATOM   1461  OD1 ASP A 223      82.699  86.203  -4.637  1.00 44.08           O  
-ATOM   1462  OD2 ASP A 223      84.633  85.774  -5.614  1.00 44.87           O  
-ATOM   1463  N   LYS A 224      82.258  81.084  -4.468  1.00 27.31           N  
-ATOM   1464  CA  LYS A 224      81.757  79.752  -4.783  1.00 24.04           C  
-ATOM   1465  C   LYS A 224      80.649  79.334  -3.818  1.00 23.55           C  
-ATOM   1466  O   LYS A 224      79.631  78.762  -4.210  1.00 20.92           O  
-ATOM   1467  CB  LYS A 224      82.889  78.728  -4.678  1.00 26.40           C  
-ATOM   1468  CG  LYS A 224      84.159  79.085  -5.416  1.00 27.79           C  
-ATOM   1469  CD  LYS A 224      83.955  79.052  -6.901  1.00 33.09           C  
-ATOM   1470  CE  LYS A 224      85.287  79.168  -7.623  1.00 34.73           C  
-ATOM   1471  NZ  LYS A 224      85.977  80.440  -7.324  1.00 37.07           N  
-ATOM   1472  N   ILE A 225      80.860  79.596  -2.537  1.00 21.32           N  
-ATOM   1473  CA  ILE A 225      79.862  79.206  -1.545  1.00 21.41           C  
-ATOM   1474  C   ILE A 225      78.491  79.861  -1.841  1.00 21.37           C  
-ATOM   1475  O   ILE A 225      77.447  79.214  -1.768  1.00 21.90           O  
-ATOM   1476  CB  ILE A 225      80.328  79.637  -0.127  1.00 21.82           C  
-ATOM   1477  CG1 ILE A 225      81.637  78.909   0.240  1.00 18.21           C  
-ATOM   1478  CG2 ILE A 225      79.248  79.298   0.895  1.00 21.94           C  
-ATOM   1479  CD1 ILE A 225      82.301  79.416   1.544  1.00 16.46           C  
-ATOM   1480  N   LYS A 226      78.526  81.140  -2.195  1.00 21.63           N  
-ATOM   1481  CA  LYS A 226      77.310  81.899  -2.443  1.00 27.55           C  
-ATOM   1482  C   LYS A 226      76.498  81.386  -3.606  1.00 28.10           C  
-ATOM   1483  O   LYS A 226      75.291  81.609  -3.649  1.00 30.86           O  
-ATOM   1484  CB  LYS A 226      77.655  83.372  -2.624  1.00 27.50           C  
-ATOM   1485  CG  LYS A 226      78.302  83.952  -1.369  1.00 33.74           C  
-ATOM   1486  CD  LYS A 226      78.665  85.420  -1.521  1.00 36.52           C  
-ATOM   1487  CE  LYS A 226      79.352  85.946  -0.267  1.00 38.35           C  
-ATOM   1488  NZ  LYS A 226      79.562  87.424  -0.278  1.00 40.55           N  
-ATOM   1489  N   VAL A 227      77.138  80.672  -4.530  1.00 26.26           N  
-ATOM   1490  CA  VAL A 227      76.411  80.132  -5.664  1.00 26.00           C  
-ATOM   1491  C   VAL A 227      75.573  78.961  -5.189  1.00 26.14           C  
-ATOM   1492  O   VAL A 227      74.488  78.699  -5.699  1.00 25.04           O  
-ATOM   1493  CB  VAL A 227      77.361  79.613  -6.768  1.00 26.82           C  
-ATOM   1494  CG1 VAL A 227      76.542  78.897  -7.846  1.00 28.68           C  
-ATOM   1495  CG2 VAL A 227      78.138  80.766  -7.368  1.00 23.22           C  
-ATOM   1496  N   LEU A 228      76.072  78.254  -4.186  1.00 22.63           N  
-ATOM   1497  CA  LEU A 228      75.367  77.078  -3.695  1.00 21.69           C  
-ATOM   1498  C   LEU A 228      74.065  77.364  -2.961  1.00 20.93           C  
-ATOM   1499  O   LEU A 228      73.909  78.412  -2.373  1.00 22.73           O  
-ATOM   1500  CB  LEU A 228      76.289  76.299  -2.751  1.00 23.48           C  
-ATOM   1501  CG  LEU A 228      77.603  75.775  -3.322  1.00 24.07           C  
-ATOM   1502  CD1 LEU A 228      78.422  75.175  -2.179  1.00 22.47           C  
-ATOM   1503  CD2 LEU A 228      77.313  74.725  -4.414  1.00 23.10           C  
-ATOM   1504  N   HIS A 229      73.151  76.400  -2.998  1.00 22.93           N  
-ATOM   1505  CA  HIS A 229      71.862  76.438  -2.298  1.00 25.57           C  
-ATOM   1506  C   HIS A 229      72.097  75.543  -1.091  1.00 23.20           C  
-ATOM   1507  O   HIS A 229      71.738  74.351  -1.089  1.00 23.44           O  
-ATOM   1508  CB  HIS A 229      70.767  75.871  -3.192  1.00 27.05           C  
-ATOM   1509  CG  HIS A 229      70.466  76.762  -4.345  1.00 30.92           C  
-ATOM   1510  ND1 HIS A 229      69.689  76.386  -5.419  1.00 34.09           N  
-ATOM   1511  CD2 HIS A 229      70.834  78.036  -4.575  1.00 34.02           C  
-ATOM   1512  CE1 HIS A 229      69.599  77.408  -6.258  1.00 34.19           C  
-ATOM   1513  NE2 HIS A 229      70.283  78.419  -5.765  1.00 34.88           N  
-ATOM   1514  N   LEU A 230      72.732  76.124  -0.070  1.00 25.39           N  
-ATOM   1515  CA  LEU A 230      73.132  75.392   1.129  1.00 23.44           C  
-ATOM   1516  C   LEU A 230      72.069  74.532   1.805  1.00 24.47           C  
-ATOM   1517  O   LEU A 230      72.292  73.346   2.054  1.00 23.51           O  
-ATOM   1518  CB  LEU A 230      73.737  76.379   2.130  1.00 23.56           C  
-ATOM   1519  CG  LEU A 230      74.910  77.195   1.575  1.00 23.79           C  
-ATOM   1520  CD1 LEU A 230      75.444  78.104   2.657  1.00 23.64           C  
-ATOM   1521  CD2 LEU A 230      76.008  76.264   1.076  1.00 23.48           C  
-ATOM   1522  N   LYS A 231      70.899  75.104   2.097  1.00 27.08           N  
-ATOM   1523  CA  LYS A 231      69.863  74.322   2.769  1.00 26.09           C  
-ATOM   1524  C   LYS A 231      69.334  73.152   1.959  1.00 25.80           C  
-ATOM   1525  O   LYS A 231      69.143  72.050   2.489  1.00 24.87           O  
-ATOM   1526  CB  LYS A 231      68.689  75.221   3.202  1.00 31.27           C  
-ATOM   1527  CG  LYS A 231      68.979  76.032   4.448  1.00 34.59           C  
-ATOM   1528  CD  LYS A 231      67.793  76.901   4.891  1.00 41.23           C  
-ATOM   1529  CE  LYS A 231      67.620  78.118   3.989  1.00 44.04           C  
-ATOM   1530  NZ  LYS A 231      66.801  79.205   4.630  1.00 49.70           N  
-ATOM   1531  N   ASP A 232      69.075  73.385   0.678  1.00 24.93           N  
-ATOM   1532  CA  ASP A 232      68.562  72.329  -0.173  1.00 24.04           C  
-ATOM   1533  C   ASP A 232      69.564  71.198  -0.254  1.00 23.89           C  
-ATOM   1534  O   ASP A 232      69.201  70.020  -0.246  1.00 25.11           O  
-ATOM   1535  CB  ASP A 232      68.261  72.883  -1.569  1.00 27.99           C  
-ATOM   1536  CG  ASP A 232      67.034  73.810  -1.574  1.00 33.79           C  
-ATOM   1537  OD1 ASP A 232      66.201  73.692  -0.643  1.00 30.81           O  
-ATOM   1538  OD2 ASP A 232      66.904  74.636  -2.504  1.00 34.85           O  
-ATOM   1539  N   MET A 233      70.836  71.558  -0.320  1.00 24.21           N  
-ATOM   1540  CA  MET A 233      71.890  70.544  -0.377  1.00 22.81           C  
-ATOM   1541  C   MET A 233      71.982  69.795   0.939  1.00 20.93           C  
-ATOM   1542  O   MET A 233      71.999  68.567   0.957  1.00 21.55           O  
-ATOM   1543  CB  MET A 233      73.243  71.212  -0.677  1.00 20.35           C  
-ATOM   1544  CG  MET A 233      73.463  71.549  -2.155  1.00 19.32           C  
-ATOM   1545  SD  MET A 233      74.981  72.505  -2.412  1.00 23.59           S  
-ATOM   1546  CE  MET A 233      76.249  71.167  -2.173  1.00 23.07           C  
-ATOM   1547  N   ASP A 234      72.010  70.551   2.038  1.00 23.62           N  
-ATOM   1548  CA  ASP A 234      72.176  69.974   3.379  1.00 24.47           C  
-ATOM   1549  C   ASP A 234      71.169  68.886   3.681  1.00 24.65           C  
-ATOM   1550  O   ASP A 234      71.490  67.878   4.317  1.00 23.22           O  
-ATOM   1551  CB  ASP A 234      72.112  71.079   4.450  1.00 27.34           C  
-ATOM   1552  CG  ASP A 234      72.682  70.621   5.815  1.00 32.91           C  
-ATOM   1553  OD1 ASP A 234      73.662  69.842   5.843  1.00 29.90           O  
-ATOM   1554  OD2 ASP A 234      72.160  71.052   6.865  1.00 37.18           O  
-ATOM   1555  N   GLN A 235      69.946  69.090   3.198  1.00 26.41           N  
-ATOM   1556  CA  GLN A 235      68.867  68.142   3.406  1.00 26.54           C  
-ATOM   1557  C   GLN A 235      69.190  66.763   2.818  1.00 26.44           C  
-ATOM   1558  O   GLN A 235      68.706  65.735   3.305  1.00 26.92           O  
-ATOM   1559  CB  GLN A 235      67.571  68.695   2.788  1.00 31.22           C  
-ATOM   1560  CG  GLN A 235      66.404  67.740   2.910  1.00 39.65           C  
-ATOM   1561  CD  GLN A 235      65.075  68.359   2.489  1.00 45.82           C  
-ATOM   1562  OE1 GLN A 235      64.015  67.910   2.956  1.00 51.03           O  
-ATOM   1563  NE2 GLN A 235      65.107  69.349   1.589  1.00 46.51           N  
-ATOM   1564  N   GLN A 236      70.018  66.738   1.781  1.00 24.96           N  
-ATOM   1565  CA  GLN A 236      70.373  65.479   1.135  1.00 24.82           C  
-ATOM   1566  C   GLN A 236      71.714  64.919   1.604  1.00 23.98           C  
-ATOM   1567  O   GLN A 236      72.063  63.789   1.264  1.00 26.47           O  
-ATOM   1568  CB  GLN A 236      70.465  65.679  -0.380  1.00 24.04           C  
-ATOM   1569  CG  GLN A 236      69.215  66.255  -1.030  1.00 26.22           C  
-ATOM   1570  CD  GLN A 236      67.970  65.438  -0.743  1.00 26.79           C  
-ATOM   1571  OE1 GLN A 236      68.004  64.205  -0.736  1.00 28.47           O  
-ATOM   1572  NE2 GLN A 236      66.854  66.123  -0.520  1.00 29.71           N  
-ATOM   1573  N   LEU A 237      72.445  65.688   2.407  1.00 22.71           N  
-ATOM   1574  CA  LEU A 237      73.802  65.295   2.824  1.00 21.89           C  
-ATOM   1575  C   LEU A 237      74.039  64.757   4.222  1.00 21.83           C  
-ATOM   1576  O   LEU A 237      73.364  65.134   5.162  1.00 21.65           O  
-ATOM   1577  CB  LEU A 237      74.727  66.494   2.617  1.00 21.56           C  
-ATOM   1578  CG  LEU A 237      74.807  66.985   1.170  1.00 23.81           C  
-ATOM   1579  CD1 LEU A 237      75.617  68.285   1.074  1.00 20.65           C  
-ATOM   1580  CD2 LEU A 237      75.424  65.865   0.343  1.00 21.45           C  
-ATOM   1581  N   ASP A 238      75.028  63.884   4.359  1.00 21.97           N  
-ATOM   1582  CA  ASP A 238      75.375  63.353   5.673  1.00 21.83           C  
-ATOM   1583  C   ASP A 238      76.377  64.295   6.309  1.00 21.91           C  
-ATOM   1584  O   ASP A 238      76.389  64.469   7.528  1.00 22.92           O  
-ATOM   1585  CB  ASP A 238      75.941  61.957   5.529  1.00 21.64           C  
-ATOM   1586  CG  ASP A 238      74.868  60.948   5.241  1.00 23.30           C  
-ATOM   1587  OD1 ASP A 238      74.224  60.488   6.210  1.00 22.04           O  
-ATOM   1588  OD2 ASP A 238      74.661  60.649   4.044  1.00 18.66           O  
-ATOM   1589  N   PHE A 239      77.235  64.883   5.472  1.00 20.36           N  
-ATOM   1590  CA  PHE A 239      78.205  65.889   5.914  1.00 17.09           C  
-ATOM   1591  C   PHE A 239      78.937  66.552   4.762  1.00 16.89           C  
-ATOM   1592  O   PHE A 239      78.877  66.104   3.614  1.00 16.89           O  
-ATOM   1593  CB  PHE A 239      79.179  65.354   6.977  1.00 17.68           C  
-ATOM   1594  CG  PHE A 239      79.993  64.179   6.553  1.00 17.21           C  
-ATOM   1595  CD1 PHE A 239      81.241  64.362   5.974  1.00 18.20           C  
-ATOM   1596  CD2 PHE A 239      79.548  62.889   6.797  1.00 16.63           C  
-ATOM   1597  CE1 PHE A 239      82.034  63.276   5.653  1.00 16.91           C  
-ATOM   1598  CE2 PHE A 239      80.335  61.789   6.482  1.00 20.22           C  
-ATOM   1599  CZ  PHE A 239      81.580  61.978   5.910  1.00 17.19           C  
-ATOM   1600  N   TRP A 240      79.558  67.675   5.076  1.00 16.11           N  
-ATOM   1601  CA  TRP A 240      80.276  68.473   4.094  1.00 18.41           C  
-ATOM   1602  C   TRP A 240      81.755  68.430   4.463  1.00 17.79           C  
-ATOM   1603  O   TRP A 240      82.097  68.605   5.623  1.00 17.98           O  
-ATOM   1604  CB  TRP A 240      79.826  69.930   4.171  1.00 18.16           C  
-ATOM   1605  CG  TRP A 240      78.345  70.172   3.986  1.00 20.49           C  
-ATOM   1606  CD1 TRP A 240      77.318  69.724   4.787  1.00 23.21           C  
-ATOM   1607  CD2 TRP A 240      77.741  70.992   2.981  1.00 21.40           C  
-ATOM   1608  NE1 TRP A 240      76.111  70.229   4.338  1.00 21.32           N  
-ATOM   1609  CE2 TRP A 240      76.343  71.012   3.237  1.00 22.90           C  
-ATOM   1610  CE3 TRP A 240      78.241  71.719   1.893  1.00 21.23           C  
-ATOM   1611  CZ2 TRP A 240      75.444  71.738   2.443  1.00 24.47           C  
-ATOM   1612  CZ3 TRP A 240      77.337  72.445   1.095  1.00 22.88           C  
-ATOM   1613  CH2 TRP A 240      75.959  72.445   1.381  1.00 21.94           C  
-ATOM   1614  N   ASN A 241      82.610  68.217   3.475  1.00 16.79           N  
-ATOM   1615  CA  ASN A 241      84.049  68.206   3.709  1.00 17.81           C  
-ATOM   1616  C   ASN A 241      84.563  69.503   3.132  1.00 19.87           C  
-ATOM   1617  O   ASN A 241      84.635  69.666   1.906  1.00 20.47           O  
-ATOM   1618  CB  ASN A 241      84.672  67.018   3.001  1.00 17.09           C  
-ATOM   1619  CG  ASN A 241      84.234  65.711   3.605  1.00 18.45           C  
-ATOM   1620  OD1 ASN A 241      84.322  65.519   4.822  1.00 17.62           O  
-ATOM   1621  ND2 ASN A 241      83.761  64.803   2.771  1.00 17.31           N  
-ATOM   1622  N   LEU A 242      84.866  70.455   4.005  1.00 16.82           N  
-ATOM   1623  CA  LEU A 242      85.314  71.760   3.553  1.00 17.42           C  
-ATOM   1624  C   LEU A 242      86.768  71.729   3.089  1.00 17.92           C  
-ATOM   1625  O   LEU A 242      87.675  71.396   3.868  1.00 17.38           O  
-ATOM   1626  CB  LEU A 242      85.159  72.780   4.695  1.00 16.53           C  
-ATOM   1627  CG  LEU A 242      85.660  74.201   4.449  1.00 18.46           C  
-ATOM   1628  CD1 LEU A 242      84.940  74.827   3.250  1.00 19.53           C  
-ATOM   1629  CD2 LEU A 242      85.412  75.030   5.704  1.00 19.07           C  
-ATOM   1630  N   MET A 243      86.988  72.093   1.836  1.00 16.44           N  
-ATOM   1631  CA  MET A 243      88.335  72.116   1.292  1.00 19.59           C  
-ATOM   1632  C   MET A 243      89.019  73.403   1.691  1.00 19.08           C  
-ATOM   1633  O   MET A 243      89.203  74.309   0.868  1.00 19.72           O  
-ATOM   1634  CB  MET A 243      88.282  71.953  -0.230  1.00 21.63           C  
-ATOM   1635  CG  MET A 243      87.785  70.572  -0.600  1.00 22.46           C  
-ATOM   1636  SD  MET A 243      87.724  70.318  -2.379  1.00 26.69           S  
-ATOM   1637  CE  MET A 243      86.227  71.461  -2.828  1.00 24.25           C  
-ATOM   1638  N   ALA A 244      89.417  73.470   2.968  1.00 18.46           N  
-ATOM   1639  CA  ALA A 244      90.081  74.658   3.525  1.00 16.92           C  
-ATOM   1640  C   ALA A 244      91.590  74.673   3.265  1.00 17.23           C  
-ATOM   1641  O   ALA A 244      92.414  74.632   4.184  1.00 16.36           O  
-ATOM   1642  CB  ALA A 244      89.812  74.740   5.038  1.00 17.98           C  
-ATOM   1643  N   TYR A 245      91.951  74.716   1.998  1.00 19.13           N  
-ATOM   1644  CA  TYR A 245      93.339  74.757   1.637  1.00 17.33           C  
-ATOM   1645  C   TYR A 245      93.426  75.258   0.202  1.00 19.79           C  
-ATOM   1646  O   TYR A 245      92.399  75.607  -0.406  1.00 15.85           O  
-ATOM   1647  CB  TYR A 245      93.985  73.374   1.861  1.00 18.13           C  
-ATOM   1648  CG  TYR A 245      93.127  72.194   1.450  1.00 20.61           C  
-ATOM   1649  CD1 TYR A 245      92.771  71.984   0.114  1.00 18.83           C  
-ATOM   1650  CD2 TYR A 245      92.691  71.270   2.395  1.00 20.50           C  
-ATOM   1651  CE1 TYR A 245      91.997  70.871  -0.271  1.00 21.68           C  
-ATOM   1652  CE2 TYR A 245      91.926  70.156   2.022  1.00 22.94           C  
-ATOM   1653  CZ  TYR A 245      91.583  69.962   0.689  1.00 22.39           C  
-ATOM   1654  OH  TYR A 245      90.852  68.844   0.352  1.00 25.36           O  
-ATOM   1655  N   ASP A 246      94.641  75.286  -0.340  1.00 18.26           N  
-ATOM   1656  CA  ASP A 246      94.874  75.856  -1.663  1.00 18.86           C  
-ATOM   1657  C   ASP A 246      94.406  77.306  -1.741  1.00 20.81           C  
-ATOM   1658  O   ASP A 246      93.947  77.756  -2.803  1.00 18.39           O  
-ATOM   1659  CB  ASP A 246      94.184  75.061  -2.757  1.00 20.93           C  
-ATOM   1660  CG  ASP A 246      94.676  73.656  -2.815  1.00 23.13           C  
-ATOM   1661  OD1 ASP A 246      95.888  73.452  -2.589  1.00 21.92           O  
-ATOM   1662  OD2 ASP A 246      93.858  72.764  -3.079  1.00 24.84           O  
-ATOM   1663  N   TYR A 247      94.506  78.049  -0.635  1.00 19.11           N  
-ATOM   1664  CA  TYR A 247      94.090  79.459  -0.679  1.00 16.98           C  
-ATOM   1665  C   TYR A 247      95.107  80.334  -1.435  1.00 19.69           C  
-ATOM   1666  O   TYR A 247      94.837  81.491  -1.743  1.00 20.79           O  
-ATOM   1667  CB  TYR A 247      93.942  80.027   0.726  1.00 16.74           C  
-ATOM   1668  CG  TYR A 247      92.930  79.352   1.613  1.00 18.43           C  
-ATOM   1669  CD1 TYR A 247      91.920  78.554   1.079  1.00 16.69           C  
-ATOM   1670  CD2 TYR A 247      92.936  79.583   2.989  1.00 16.96           C  
-ATOM   1671  CE1 TYR A 247      90.922  78.007   1.895  1.00 21.10           C  
-ATOM   1672  CE2 TYR A 247      91.943  79.041   3.817  1.00 17.85           C  
-ATOM   1673  CZ  TYR A 247      90.944  78.263   3.265  1.00 18.45           C  
-ATOM   1674  OH  TYR A 247      89.950  77.764   4.072  1.00 19.84           O  
-ATOM   1675  N   ALA A 248      96.294  79.797  -1.696  1.00 19.13           N  
-ATOM   1676  CA  ALA A 248      97.319  80.550  -2.416  1.00 20.43           C  
-ATOM   1677  C   ALA A 248      98.181  79.547  -3.147  1.00 21.19           C  
-ATOM   1678  O   ALA A 248      98.363  78.419  -2.667  1.00 20.37           O  
-ATOM   1679  CB  ALA A 248      98.175  81.360  -1.436  1.00 19.12           C  
-ATOM   1680  N   GLY A 249      98.714  79.960  -4.299  1.00 21.35           N  
-ATOM   1681  CA  GLY A 249      99.547  79.082  -5.101  1.00 23.45           C  
-ATOM   1682  C   GLY A 249     100.022  79.794  -6.359  1.00 24.91           C  
-ATOM   1683  O   GLY A 249     100.049  81.020  -6.403  1.00 25.24           O  
-ATOM   1684  N   SER A 250     100.375  79.040  -7.393  1.00 25.97           N  
-ATOM   1685  CA  SER A 250     100.862  79.655  -8.629  1.00 26.79           C  
-ATOM   1686  C   SER A 250      99.805  80.570  -9.251  1.00 28.31           C  
-ATOM   1687  O   SER A 250     100.135  81.493 -10.000  1.00 27.54           O  
-ATOM   1688  CB  SER A 250     101.254  78.571  -9.627  1.00 27.68           C  
-ATOM   1689  OG  SER A 250     100.126  77.791  -9.975  1.00 28.40           O  
-ATOM   1690  N   PHE A 251      98.542  80.303  -8.922  1.00 26.61           N  
-ATOM   1691  CA  PHE A 251      97.403  81.066  -9.424  1.00 27.39           C  
-ATOM   1692  C   PHE A 251      97.212  82.380  -8.669  1.00 27.37           C  
-ATOM   1693  O   PHE A 251      96.317  83.158  -9.000  1.00 26.99           O  
-ATOM   1694  CB  PHE A 251      96.119  80.223  -9.307  1.00 28.78           C  
-ATOM   1695  CG  PHE A 251      95.995  79.486  -7.988  1.00 28.59           C  
-ATOM   1696  CD1 PHE A 251      95.572  80.147  -6.840  1.00 29.92           C  
-ATOM   1697  CD2 PHE A 251      96.392  78.153  -7.884  1.00 28.89           C  
-ATOM   1698  CE1 PHE A 251      95.555  79.496  -5.602  1.00 31.47           C  
-ATOM   1699  CE2 PHE A 251      96.382  77.486  -6.656  1.00 29.83           C  
-ATOM   1700  CZ  PHE A 251      95.965  78.160  -5.509  1.00 30.94           C  
-ATOM   1701  N   SER A 252      98.057  82.632  -7.669  1.00 26.11           N  
-ATOM   1702  CA  SER A 252      97.941  83.840  -6.856  1.00 25.94           C  
-ATOM   1703  C   SER A 252      98.848  84.969  -7.341  1.00 28.10           C  
-ATOM   1704  O   SER A 252      99.931  84.717  -7.891  1.00 26.05           O  
-ATOM   1705  CB  SER A 252      98.282  83.521  -5.387  1.00 25.77           C  
-ATOM   1706  OG  SER A 252      97.515  82.433  -4.891  1.00 23.84           O  
-ATOM   1707  N   SER A 253      98.408  86.212  -7.129  1.00 28.80           N  
-ATOM   1708  CA  SER A 253      99.202  87.383  -7.522  1.00 30.71           C  
-ATOM   1709  C   SER A 253     100.439  87.495  -6.641  1.00 29.47           C  
-ATOM   1710  O   SER A 253     101.511  87.891  -7.106  1.00 30.22           O  
-ATOM   1711  CB  SER A 253      98.374  88.662  -7.373  1.00 31.29           C  
-ATOM   1712  OG  SER A 253      97.234  88.609  -8.210  1.00 36.39           O  
-ATOM   1713  N   LEU A 254     100.288  87.124  -5.373  1.00 27.12           N  
-ATOM   1714  CA  LEU A 254     101.385  87.203  -4.406  1.00 26.79           C  
-ATOM   1715  C   LEU A 254     101.516  85.917  -3.570  1.00 26.26           C  
-ATOM   1716  O   LEU A 254     100.565  85.136  -3.471  1.00 24.22           O  
-ATOM   1717  CB  LEU A 254     101.123  88.377  -3.451  1.00 28.06           C  
-ATOM   1718  CG  LEU A 254     100.989  89.783  -4.060  1.00 30.97           C  
-ATOM   1719  CD1 LEU A 254     100.349  90.743  -3.064  1.00 28.36           C  
-ATOM   1720  CD2 LEU A 254     102.372  90.274  -4.471  1.00 28.46           C  
-ATOM   1721  N   SER A 255     102.680  85.712  -2.957  1.00 25.79           N  
-ATOM   1722  CA  SER A 255     102.855  84.542  -2.104  1.00 26.96           C  
-ATOM   1723  C   SER A 255     101.849  84.682  -0.946  1.00 26.84           C  
-ATOM   1724  O   SER A 255     101.425  85.793  -0.607  1.00 24.60           O  
-ATOM   1725  CB  SER A 255     104.275  84.483  -1.549  1.00 26.79           C  
-ATOM   1726  OG  SER A 255     104.502  85.577  -0.683  1.00 30.82           O  
-ATOM   1727  N   GLY A 256     101.450  83.556  -0.360  1.00 25.02           N  
-ATOM   1728  CA  GLY A 256     100.503  83.601   0.738  1.00 24.34           C  
-ATOM   1729  C   GLY A 256     100.312  82.269   1.449  1.00 24.02           C  
-ATOM   1730  O   GLY A 256     100.899  81.269   1.045  1.00 21.12           O  
-ATOM   1731  N   HIS A 257      99.513  82.265   2.514  1.00 21.91           N  
-ATOM   1732  CA  HIS A 257      99.201  81.057   3.277  1.00 19.36           C  
-ATOM   1733  C   HIS A 257      98.082  80.349   2.540  1.00 20.20           C  
-ATOM   1734  O   HIS A 257      97.110  80.978   2.111  1.00 18.75           O  
-ATOM   1735  CB  HIS A 257      98.746  81.461   4.671  1.00 19.42           C  
-ATOM   1736  CG  HIS A 257      99.728  82.348   5.378  1.00 19.33           C  
-ATOM   1737  ND1 HIS A 257     100.966  81.922   5.824  1.00 19.46           N  
-ATOM   1738  CD2 HIS A 257      99.666  83.668   5.657  1.00 20.14           C  
-ATOM   1739  CE1 HIS A 257     101.620  82.950   6.341  1.00 21.24           C  
-ATOM   1740  NE2 HIS A 257     100.858  84.024   6.246  1.00 20.76           N  
-ATOM   1741  N   GLN A 258      98.218  79.038   2.393  1.00 17.60           N  
-ATOM   1742  CA  GLN A 258      97.223  78.290   1.662  1.00 18.85           C  
-ATOM   1743  C   GLN A 258      96.085  77.709   2.485  1.00 18.29           C  
-ATOM   1744  O   GLN A 258      95.116  77.229   1.907  1.00 19.51           O  
-ATOM   1745  CB  GLN A 258      97.895  77.147   0.914  1.00 18.02           C  
-ATOM   1746  CG  GLN A 258      98.444  76.055   1.846  1.00 17.25           C  
-ATOM   1747  CD  GLN A 258      98.231  74.667   1.255  1.00 20.24           C  
-ATOM   1748  OE1 GLN A 258      97.230  74.424   0.562  1.00 17.15           O  
-ATOM   1749  NE2 GLN A 258      99.145  73.751   1.543  1.00 17.87           N  
-ATOM   1750  N   ALA A 259      96.170  77.771   3.814  1.00 18.21           N  
-ATOM   1751  CA  ALA A 259      95.137  77.143   4.618  1.00 16.60           C  
-ATOM   1752  C   ALA A 259      94.877  77.789   5.986  1.00 18.05           C  
-ATOM   1753  O   ALA A 259      94.379  77.128   6.896  1.00 18.07           O  
-ATOM   1754  CB  ALA A 259      95.511  75.666   4.799  1.00 15.86           C  
-ATOM   1755  N   ASN A 260      95.224  79.063   6.116  1.00 16.35           N  
-ATOM   1756  CA  ASN A 260      95.070  79.811   7.349  1.00 17.50           C  
-ATOM   1757  C   ASN A 260      93.606  79.902   7.802  1.00 19.21           C  
-ATOM   1758  O   ASN A 260      92.693  80.071   6.986  1.00 18.31           O  
-ATOM   1759  CB  ASN A 260      95.616  81.222   7.132  1.00 18.09           C  
-ATOM   1760  CG  ASN A 260      94.931  81.904   5.974  1.00 19.06           C  
-ATOM   1761  OD1 ASN A 260      95.104  81.510   4.819  1.00 21.28           O  
-ATOM   1762  ND2 ASN A 260      94.102  82.887   6.278  1.00 19.28           N  
-ATOM   1763  N   VAL A 261      93.390  79.817   9.110  1.00 17.66           N  
-ATOM   1764  CA  VAL A 261      92.044  79.868   9.660  1.00 17.19           C  
-ATOM   1765  C   VAL A 261      91.486  81.295   9.710  1.00 18.96           C  
-ATOM   1766  O   VAL A 261      90.292  81.497   9.487  1.00 17.38           O  
-ATOM   1767  CB  VAL A 261      92.029  79.278  11.093  1.00 19.35           C  
-ATOM   1768  CG1 VAL A 261      90.686  79.552  11.771  1.00 16.65           C  
-ATOM   1769  CG2 VAL A 261      92.315  77.784  11.044  1.00 16.28           C  
-ATOM   1770  N   TYR A 262      92.354  82.264  10.018  1.00 17.99           N  
-ATOM   1771  CA  TYR A 262      91.935  83.650  10.129  1.00 19.98           C  
-ATOM   1772  C   TYR A 262      92.708  84.576   9.208  1.00 21.02           C  
-ATOM   1773  O   TYR A 262      93.856  84.306   8.818  1.00 18.26           O  
-ATOM   1774  CB  TYR A 262      92.124  84.168  11.568  1.00 18.97           C  
-ATOM   1775  CG  TYR A 262      91.358  83.406  12.633  1.00 20.33           C  
-ATOM   1776  CD1 TYR A 262      89.972  83.449  12.684  1.00 19.15           C  
-ATOM   1777  CD2 TYR A 262      92.025  82.651  13.599  1.00 22.16           C  
-ATOM   1778  CE1 TYR A 262      89.258  82.770  13.660  1.00 22.17           C  
-ATOM   1779  CE2 TYR A 262      91.310  81.955  14.601  1.00 24.40           C  
-ATOM   1780  CZ  TYR A 262      89.923  82.025  14.618  1.00 25.81           C  
-ATOM   1781  OH  TYR A 262      89.196  81.367  15.588  1.00 25.32           O  
-ATOM   1782  N   ASN A 263      92.068  85.688   8.874  1.00 20.66           N  
-ATOM   1783  CA  ASN A 263      92.697  86.702   8.048  1.00 23.92           C  
-ATOM   1784  C   ASN A 263      93.824  87.288   8.902  1.00 24.70           C  
-ATOM   1785  O   ASN A 263      93.714  87.362  10.137  1.00 24.89           O  
-ATOM   1786  CB  ASN A 263      91.679  87.799   7.679  1.00 26.66           C  
-ATOM   1787  CG  ASN A 263      92.325  88.969   6.968  1.00 28.03           C  
-ATOM   1788  OD1 ASN A 263      92.801  88.841   5.840  1.00 26.74           O  
-ATOM   1789  ND2 ASN A 263      92.359  90.117   7.633  1.00 29.86           N  
-ATOM   1790  N   ASP A 264      94.922  87.668   8.256  1.00 24.45           N  
-ATOM   1791  CA  ASP A 264      96.057  88.247   8.965  1.00 26.43           C  
-ATOM   1792  C   ASP A 264      95.960  89.769   8.855  1.00 25.63           C  
-ATOM   1793  O   ASP A 264      96.339  90.347   7.832  1.00 25.07           O  
-ATOM   1794  CB  ASP A 264      97.374  87.778   8.341  1.00 25.54           C  
-ATOM   1795  CG  ASP A 264      98.587  88.197   9.158  1.00 30.90           C  
-ATOM   1796  OD1 ASP A 264      98.438  89.071  10.046  1.00 29.97           O  
-ATOM   1797  OD2 ASP A 264      99.690  87.662   8.903  1.00 28.73           O  
-ATOM   1798  N   THR A 265      95.472  90.415   9.910  1.00 27.04           N  
-ATOM   1799  CA  THR A 265      95.301  91.870   9.882  1.00 30.08           C  
-ATOM   1800  C   THR A 265      96.613  92.635   9.739  1.00 31.34           C  
-ATOM   1801  O   THR A 265      96.623  93.779   9.290  1.00 32.67           O  
-ATOM   1802  CB  THR A 265      94.535  92.389  11.153  1.00 30.64           C  
-ATOM   1803  OG1 THR A 265      95.252  92.030  12.346  1.00 33.52           O  
-ATOM   1804  CG2 THR A 265      93.147  91.786  11.213  1.00 30.16           C  
-ATOM   1805  N   SER A 266      97.718  91.995  10.099  1.00 30.29           N  
-ATOM   1806  CA  SER A 266      99.014  92.642  10.002  1.00 31.01           C  
-ATOM   1807  C   SER A 266      99.612  92.486   8.605  1.00 30.58           C  
-ATOM   1808  O   SER A 266     100.570  93.166   8.250  1.00 30.05           O  
-ATOM   1809  CB  SER A 266      99.972  92.030  11.018  1.00 34.81           C  
-ATOM   1810  OG  SER A 266     100.346  90.725  10.603  1.00 37.54           O  
-ATOM   1811  N   ASN A 267      99.061  91.583   7.807  1.00 29.89           N  
-ATOM   1812  CA  ASN A 267      99.604  91.356   6.469  1.00 28.39           C  
-ATOM   1813  C   ASN A 267      98.500  90.702   5.671  1.00 29.07           C  
-ATOM   1814  O   ASN A 267      98.615  89.562   5.223  1.00 29.35           O  
-ATOM   1815  CB  ASN A 267     100.827  90.442   6.565  1.00 27.21           C  
-ATOM   1816  CG  ASN A 267     101.461  90.179   5.217  1.00 32.37           C  
-ATOM   1817  OD1 ASN A 267     101.038  90.741   4.200  1.00 31.98           O  
-ATOM   1818  ND2 ASN A 267     102.480  89.320   5.196  1.00 25.73           N  
-ATOM   1819  N   PRO A 268      97.400  91.437   5.485  1.00 27.76           N  
-ATOM   1820  CA  PRO A 268      96.242  90.947   4.753  1.00 26.64           C  
-ATOM   1821  C   PRO A 268      96.549  90.392   3.386  1.00 26.07           C  
-ATOM   1822  O   PRO A 268      95.866  89.476   2.934  1.00 25.92           O  
-ATOM   1823  CB  PRO A 268      95.306  92.163   4.729  1.00 26.53           C  
-ATOM   1824  CG  PRO A 268      96.268  93.317   4.754  1.00 27.03           C  
-ATOM   1825  CD  PRO A 268      97.267  92.874   5.784  1.00 25.92           C  
-ATOM   1826  N   LEU A 269      97.575  90.912   2.722  1.00 25.82           N  
-ATOM   1827  CA  LEU A 269      97.903  90.390   1.384  1.00 26.58           C  
-ATOM   1828  C   LEU A 269      98.306  88.912   1.405  1.00 26.20           C  
-ATOM   1829  O   LEU A 269      98.189  88.214   0.396  1.00 24.22           O  
-ATOM   1830  CB  LEU A 269      99.040  91.196   0.743  1.00 28.19           C  
-ATOM   1831  CG  LEU A 269      98.711  92.606   0.225  1.00 29.12           C  
-ATOM   1832  CD1 LEU A 269      99.975  93.269  -0.258  1.00 31.76           C  
-ATOM   1833  CD2 LEU A 269      97.702  92.533  -0.897  1.00 32.10           C  
-ATOM   1834  N   SER A 270      98.790  88.445   2.551  1.00 24.59           N  
-ATOM   1835  CA  SER A 270      99.236  87.059   2.668  1.00 23.22           C  
-ATOM   1836  C   SER A 270      98.082  86.100   2.896  1.00 22.98           C  
-ATOM   1837  O   SER A 270      98.261  84.887   2.822  1.00 22.75           O  
-ATOM   1838  CB  SER A 270     100.232  86.925   3.821  1.00 23.67           C  
-ATOM   1839  OG  SER A 270      99.584  87.076   5.074  1.00 20.72           O  
-ATOM   1840  N   THR A 271      96.904  86.642   3.198  1.00 22.28           N  
-ATOM   1841  CA  THR A 271      95.746  85.811   3.433  1.00 21.16           C  
-ATOM   1842  C   THR A 271      94.573  86.173   2.544  1.00 23.26           C  
-ATOM   1843  O   THR A 271      93.583  86.738   3.003  1.00 24.05           O  
-ATOM   1844  CB  THR A 271      95.290  85.861   4.898  1.00 21.77           C  
-ATOM   1845  OG1 THR A 271      95.102  87.228   5.313  1.00 19.27           O  
-ATOM   1846  CG2 THR A 271      96.347  85.178   5.789  1.00 22.59           C  
-ATOM   1847  N   PRO A 272      94.672  85.846   1.247  1.00 24.61           N  
-ATOM   1848  CA  PRO A 272      93.574  86.154   0.324  1.00 22.87           C  
-ATOM   1849  C   PRO A 272      92.290  85.428   0.724  1.00 23.56           C  
-ATOM   1850  O   PRO A 272      91.186  85.805   0.315  1.00 23.94           O  
-ATOM   1851  CB  PRO A 272      94.130  85.726  -1.040  1.00 22.98           C  
-ATOM   1852  CG  PRO A 272      95.174  84.712  -0.713  1.00 25.56           C  
-ATOM   1853  CD  PRO A 272      95.833  85.288   0.530  1.00 20.73           C  
-ATOM   1854  N   PHE A 273      92.420  84.383   1.530  1.00 22.40           N  
-ATOM   1855  CA  PHE A 273      91.236  83.671   1.985  1.00 19.32           C  
-ATOM   1856  C   PHE A 273      91.467  83.264   3.436  1.00 20.55           C  
-ATOM   1857  O   PHE A 273      92.599  83.315   3.925  1.00 20.72           O  
-ATOM   1858  CB  PHE A 273      91.002  82.400   1.163  1.00 22.96           C  
-ATOM   1859  CG  PHE A 273      90.649  82.643  -0.278  1.00 21.27           C  
-ATOM   1860  CD1 PHE A 273      91.635  82.657  -1.263  1.00 24.12           C  
-ATOM   1861  CD2 PHE A 273      89.325  82.819  -0.651  1.00 21.32           C  
-ATOM   1862  CE1 PHE A 273      91.304  82.838  -2.616  1.00 25.16           C  
-ATOM   1863  CE2 PHE A 273      88.973  83.002  -1.997  1.00 24.70           C  
-ATOM   1864  CZ  PHE A 273      89.964  83.010  -2.984  1.00 23.42           C  
-ATOM   1865  N   ASN A 274      90.402  82.889   4.132  1.00 18.76           N  
-ATOM   1866  CA  ASN A 274      90.546  82.391   5.502  1.00 21.43           C  
-ATOM   1867  C   ASN A 274      89.363  81.475   5.764  1.00 18.93           C  
-ATOM   1868  O   ASN A 274      88.263  81.703   5.273  1.00 21.29           O  
-ATOM   1869  CB  ASN A 274      90.634  83.529   6.543  1.00 19.99           C  
-ATOM   1870  CG  ASN A 274      89.300  84.237   6.758  1.00 24.05           C  
-ATOM   1871  OD1 ASN A 274      88.464  83.799   7.549  1.00 23.29           O  
-ATOM   1872  ND2 ASN A 274      89.101  85.339   6.037  1.00 24.68           N  
-ATOM   1873  N   THR A 275      89.606  80.405   6.503  1.00 17.38           N  
-ATOM   1874  CA  THR A 275      88.568  79.431   6.787  1.00 15.79           C  
-ATOM   1875  C   THR A 275      87.376  79.988   7.562  1.00 19.05           C  
-ATOM   1876  O   THR A 275      86.239  79.601   7.317  1.00 19.32           O  
-ATOM   1877  CB  THR A 275      89.184  78.272   7.574  1.00 15.84           C  
-ATOM   1878  OG1 THR A 275      90.199  77.673   6.751  1.00 17.58           O  
-ATOM   1879  CG2 THR A 275      88.122  77.209   7.939  1.00 15.78           C  
-ATOM   1880  N   GLN A 276      87.639  80.899   8.491  1.00 20.53           N  
-ATOM   1881  CA  GLN A 276      86.559  81.445   9.312  1.00 20.63           C  
-ATOM   1882  C   GLN A 276      85.440  82.056   8.468  1.00 21.03           C  
-ATOM   1883  O   GLN A 276      84.269  81.822   8.729  1.00 20.89           O  
-ATOM   1884  CB  GLN A 276      87.101  82.504  10.279  1.00 21.48           C  
-ATOM   1885  CG  GLN A 276      86.017  83.043  11.240  1.00 22.94           C  
-ATOM   1886  CD  GLN A 276      85.513  81.994  12.217  1.00 23.37           C  
-ATOM   1887  OE1 GLN A 276      86.294  81.397  12.975  1.00 23.58           O  
-ATOM   1888  NE2 GLN A 276      84.209  81.759  12.207  1.00 24.47           N  
-ATOM   1889  N   THR A 277      85.805  82.855   7.473  1.00 21.49           N  
-ATOM   1890  CA  THR A 277      84.805  83.483   6.602  1.00 20.50           C  
-ATOM   1891  C   THR A 277      83.909  82.434   5.940  1.00 21.89           C  
-ATOM   1892  O   THR A 277      82.689  82.606   5.839  1.00 22.40           O  
-ATOM   1893  CB  THR A 277      85.505  84.317   5.533  1.00 19.87           C  
-ATOM   1894  OG1 THR A 277      86.112  85.441   6.175  1.00 21.44           O  
-ATOM   1895  CG2 THR A 277      84.530  84.790   4.452  1.00 20.74           C  
-ATOM   1896  N   ALA A 278      84.513  81.335   5.496  1.00 19.77           N  
-ATOM   1897  CA  ALA A 278      83.736  80.292   4.853  1.00 20.81           C  
-ATOM   1898  C   ALA A 278      82.771  79.657   5.860  1.00 22.13           C  
-ATOM   1899  O   ALA A 278      81.583  79.452   5.556  1.00 22.69           O  
-ATOM   1900  CB  ALA A 278      84.672  79.230   4.230  1.00 18.31           C  
-ATOM   1901  N   LEU A 279      83.275  79.357   7.054  1.00 20.24           N  
-ATOM   1902  CA  LEU A 279      82.443  78.745   8.085  1.00 18.81           C  
-ATOM   1903  C   LEU A 279      81.295  79.693   8.473  1.00 17.97           C  
-ATOM   1904  O   LEU A 279      80.198  79.255   8.758  1.00 18.72           O  
-ATOM   1905  CB  LEU A 279      83.310  78.361   9.310  1.00 18.79           C  
-ATOM   1906  CG  LEU A 279      84.237  77.141   9.073  1.00 16.71           C  
-ATOM   1907  CD1 LEU A 279      85.065  76.842  10.323  1.00 15.26           C  
-ATOM   1908  CD2 LEU A 279      83.394  75.916   8.715  1.00 12.06           C  
-ATOM   1909  N   ASP A 280      81.554  80.986   8.479  1.00 20.05           N  
-ATOM   1910  CA  ASP A 280      80.493  81.948   8.790  1.00 21.56           C  
-ATOM   1911  C   ASP A 280      79.396  81.843   7.730  1.00 21.89           C  
-ATOM   1912  O   ASP A 280      78.213  81.805   8.044  1.00 23.70           O  
-ATOM   1913  CB  ASP A 280      81.074  83.351   8.810  1.00 22.74           C  
-ATOM   1914  CG  ASP A 280      82.042  83.543   9.943  1.00 21.57           C  
-ATOM   1915  OD1 ASP A 280      82.014  82.706  10.873  1.00 22.51           O  
-ATOM   1916  OD2 ASP A 280      82.810  84.520   9.910  1.00 22.21           O  
-ATOM   1917  N   LEU A 281      79.799  81.784   6.464  1.00 21.79           N  
-ATOM   1918  CA  LEU A 281      78.830  81.643   5.383  1.00 20.93           C  
-ATOM   1919  C   LEU A 281      78.035  80.328   5.482  1.00 20.17           C  
-ATOM   1920  O   LEU A 281      76.812  80.319   5.314  1.00 18.30           O  
-ATOM   1921  CB  LEU A 281      79.540  81.700   4.022  1.00 21.64           C  
-ATOM   1922  CG  LEU A 281      80.158  83.044   3.666  1.00 24.77           C  
-ATOM   1923  CD1 LEU A 281      80.994  82.936   2.367  1.00 24.07           C  
-ATOM   1924  CD2 LEU A 281      79.015  84.056   3.502  1.00 29.25           C  
-ATOM   1925  N   TYR A 282      78.711  79.210   5.736  1.00 16.02           N  
-ATOM   1926  CA  TYR A 282      77.987  77.940   5.818  1.00 15.90           C  
-ATOM   1927  C   TYR A 282      76.997  77.904   6.957  1.00 16.42           C  
-ATOM   1928  O   TYR A 282      75.866  77.490   6.784  1.00 19.42           O  
-ATOM   1929  CB  TYR A 282      78.943  76.748   5.985  1.00 14.89           C  
-ATOM   1930  CG  TYR A 282      79.585  76.316   4.677  1.00 18.45           C  
-ATOM   1931  CD1 TYR A 282      78.861  75.603   3.724  1.00 21.69           C  
-ATOM   1932  CD2 TYR A 282      80.891  76.689   4.365  1.00 17.13           C  
-ATOM   1933  CE1 TYR A 282      79.424  75.267   2.469  1.00 22.98           C  
-ATOM   1934  CE2 TYR A 282      81.472  76.364   3.120  1.00 20.02           C  
-ATOM   1935  CZ  TYR A 282      80.722  75.652   2.176  1.00 23.88           C  
-ATOM   1936  OH  TYR A 282      81.270  75.339   0.946  1.00 21.48           O  
-ATOM   1937  N   ARG A 283      77.444  78.333   8.129  1.00 18.15           N  
-ATOM   1938  CA  ARG A 283      76.600  78.297   9.317  1.00 19.18           C  
-ATOM   1939  C   ARG A 283      75.431  79.287   9.226  1.00 20.36           C  
-ATOM   1940  O   ARG A 283      74.272  78.914   9.443  1.00 22.97           O  
-ATOM   1941  CB  ARG A 283      77.487  78.545  10.538  1.00 18.25           C  
-ATOM   1942  CG  ARG A 283      78.457  77.328  10.805  1.00 18.88           C  
-ATOM   1943  CD  ARG A 283      79.414  77.593  11.964  1.00 13.91           C  
-ATOM   1944  NE  ARG A 283      80.162  78.836  11.758  1.00 16.37           N  
-ATOM   1945  CZ  ARG A 283      80.742  79.508  12.748  1.00 17.10           C  
-ATOM   1946  NH1 ARG A 283      80.651  79.034  13.988  1.00 19.89           N  
-ATOM   1947  NH2 ARG A 283      81.358  80.663  12.523  1.00 16.38           N  
-ATOM   1948  N   ALA A 284      75.726  80.532   8.878  1.00 21.00           N  
-ATOM   1949  CA  ALA A 284      74.671  81.522   8.737  1.00 23.49           C  
-ATOM   1950  C   ALA A 284      73.716  81.030   7.649  1.00 25.00           C  
-ATOM   1951  O   ALA A 284      72.521  81.331   7.673  1.00 25.29           O  
-ATOM   1952  CB  ALA A 284      75.257  82.845   8.343  1.00 22.36           C  
-ATOM   1953  N   GLY A 285      74.241  80.252   6.703  1.00 24.47           N  
-ATOM   1954  CA  GLY A 285      73.413  79.739   5.621  1.00 22.81           C  
-ATOM   1955  C   GLY A 285      72.549  78.574   6.045  1.00 23.84           C  
-ATOM   1956  O   GLY A 285      71.796  78.023   5.239  1.00 24.31           O  
-ATOM   1957  N   GLY A 286      72.674  78.179   7.310  1.00 22.16           N  
-ATOM   1958  CA  GLY A 286      71.847  77.102   7.825  1.00 22.48           C  
-ATOM   1959  C   GLY A 286      72.491  75.743   7.972  1.00 25.15           C  
-ATOM   1960  O   GLY A 286      71.841  74.777   8.415  1.00 23.72           O  
-ATOM   1961  N   VAL A 287      73.759  75.627   7.607  1.00 21.12           N  
-ATOM   1962  CA  VAL A 287      74.393  74.317   7.747  1.00 23.84           C  
-ATOM   1963  C   VAL A 287      74.902  74.173   9.181  1.00 21.36           C  
-ATOM   1964  O   VAL A 287      75.629  75.024   9.672  1.00 22.16           O  
-ATOM   1965  CB  VAL A 287      75.566  74.149   6.751  1.00 22.08           C  
-ATOM   1966  CG1 VAL A 287      76.196  72.771   6.935  1.00 22.41           C  
-ATOM   1967  CG2 VAL A 287      75.054  74.296   5.321  1.00 17.75           C  
-ATOM   1968  N   PRO A 288      74.506  73.104   9.878  1.00 22.20           N  
-ATOM   1969  CA  PRO A 288      75.002  72.982  11.254  1.00 22.08           C  
-ATOM   1970  C   PRO A 288      76.506  72.692  11.295  1.00 22.21           C  
-ATOM   1971  O   PRO A 288      77.043  71.935  10.459  1.00 19.13           O  
-ATOM   1972  CB  PRO A 288      74.154  71.855  11.849  1.00 24.24           C  
-ATOM   1973  CG  PRO A 288      73.730  71.038  10.654  1.00 27.38           C  
-ATOM   1974  CD  PRO A 288      73.574  72.018   9.514  1.00 24.14           C  
-ATOM   1975  N   ALA A 289      77.195  73.312  12.245  1.00 20.07           N  
-ATOM   1976  CA  ALA A 289      78.634  73.114  12.368  1.00 20.92           C  
-ATOM   1977  C   ALA A 289      79.062  71.655  12.446  1.00 20.71           C  
-ATOM   1978  O   ALA A 289      80.088  71.277  11.862  1.00 21.82           O  
-ATOM   1979  CB  ALA A 289      79.153  73.868  13.590  1.00 23.05           C  
-ATOM   1980  N   ASN A 290      78.295  70.814  13.139  1.00 20.92           N  
-ATOM   1981  CA  ASN A 290      78.722  69.418  13.284  1.00 20.67           C  
-ATOM   1982  C   ASN A 290      78.595  68.531  12.063  1.00 19.61           C  
-ATOM   1983  O   ASN A 290      78.808  67.324  12.158  1.00 18.27           O  
-ATOM   1984  CB  ASN A 290      78.074  68.763  14.517  1.00 20.09           C  
-ATOM   1985  CG  ASN A 290      76.593  68.610  14.360  1.00 24.06           C  
-ATOM   1986  OD1 ASN A 290      75.879  68.470  15.381  1.00 27.19           O  
-ATOM   1987  ND2 ASN A 290      76.109  68.585  13.147  1.00 18.19           N  
-ATOM   1988  N   LYS A 291      78.220  69.139  10.941  1.00 20.05           N  
-ATOM   1989  CA  LYS A 291      78.105  68.430   9.674  1.00 20.13           C  
-ATOM   1990  C   LYS A 291      79.199  68.962   8.731  1.00 19.24           C  
-ATOM   1991  O   LYS A 291      79.296  68.575   7.558  1.00 16.82           O  
-ATOM   1992  CB  LYS A 291      76.717  68.632   9.039  1.00 21.93           C  
-ATOM   1993  CG  LYS A 291      75.584  67.863   9.702  1.00 23.10           C  
-ATOM   1994  CD  LYS A 291      74.249  68.009   8.923  1.00 24.99           C  
-ATOM   1995  CE  LYS A 291      74.290  67.268   7.585  1.00 24.20           C  
-ATOM   1996  NZ  LYS A 291      72.989  67.285   6.843  1.00 23.00           N  
-ATOM   1997  N   ILE A 292      79.989  69.906   9.237  1.00 18.45           N  
-ATOM   1998  CA  ILE A 292      81.065  70.462   8.436  1.00 17.65           C  
-ATOM   1999  C   ILE A 292      82.411  69.909   8.931  1.00 19.58           C  
-ATOM   2000  O   ILE A 292      82.849  70.193  10.058  1.00 17.54           O  
-ATOM   2001  CB  ILE A 292      81.102  71.969   8.505  1.00 17.47           C  
-ATOM   2002  CG1 ILE A 292      79.711  72.547   8.192  1.00 18.27           C  
-ATOM   2003  CG2 ILE A 292      82.083  72.505   7.436  1.00 19.64           C  
-ATOM   2004  CD1 ILE A 292      79.678  74.055   8.231  1.00 17.06           C  
-ATOM   2005  N   VAL A 293      83.063  69.126   8.079  1.00 19.79           N  
-ATOM   2006  CA  VAL A 293      84.359  68.521   8.423  1.00 18.47           C  
-ATOM   2007  C   VAL A 293      85.475  69.436   7.951  1.00 19.84           C  
-ATOM   2008  O   VAL A 293      85.462  69.880   6.808  1.00 20.55           O  
-ATOM   2009  CB  VAL A 293      84.486  67.148   7.781  1.00 18.06           C  
-ATOM   2010  CG1 VAL A 293      85.846  66.510   8.149  1.00 17.51           C  
-ATOM   2011  CG2 VAL A 293      83.314  66.262   8.273  1.00 17.43           C  
-ATOM   2012  N   LEU A 294      86.433  69.750   8.825  1.00 17.74           N  
-ATOM   2013  CA  LEU A 294      87.491  70.666   8.420  1.00 16.88           C  
-ATOM   2014  C   LEU A 294      88.619  70.011   7.630  1.00 17.46           C  
-ATOM   2015  O   LEU A 294      89.424  69.256   8.183  1.00 17.27           O  
-ATOM   2016  CB  LEU A 294      88.092  71.394   9.643  1.00 16.32           C  
-ATOM   2017  CG  LEU A 294      89.252  72.316   9.290  1.00 17.44           C  
-ATOM   2018  CD1 LEU A 294      88.719  73.481   8.468  1.00 14.21           C  
-ATOM   2019  CD2 LEU A 294      89.945  72.828  10.570  1.00 17.78           C  
-ATOM   2020  N   GLY A 295      88.670  70.315   6.339  1.00 16.07           N  
-ATOM   2021  CA  GLY A 295      89.713  69.776   5.485  1.00 15.61           C  
-ATOM   2022  C   GLY A 295      91.040  70.447   5.793  1.00 15.43           C  
-ATOM   2023  O   GLY A 295      91.098  71.648   6.107  1.00 14.00           O  
-ATOM   2024  N   MET A 296      92.112  69.669   5.707  1.00 16.18           N  
-ATOM   2025  CA  MET A 296      93.438  70.199   5.969  1.00 15.81           C  
-ATOM   2026  C   MET A 296      94.432  69.587   4.992  1.00 15.66           C  
-ATOM   2027  O   MET A 296      94.297  68.433   4.585  1.00 14.44           O  
-ATOM   2028  CB  MET A 296      93.840  69.916   7.421  1.00 15.96           C  
-ATOM   2029  CG  MET A 296      93.032  70.738   8.443  1.00 16.18           C  
-ATOM   2030  SD  MET A 296      93.380  70.223  10.168  1.00 16.98           S  
-ATOM   2031  CE  MET A 296      92.428  68.761  10.262  1.00 15.61           C  
-ATOM   2032  N   PRO A 297      95.459  70.355   4.613  1.00 14.22           N  
-ATOM   2033  CA  PRO A 297      96.439  69.825   3.668  1.00 15.45           C  
-ATOM   2034  C   PRO A 297      97.569  69.001   4.271  1.00 17.03           C  
-ATOM   2035  O   PRO A 297      98.088  69.331   5.343  1.00 17.91           O  
-ATOM   2036  CB  PRO A 297      96.967  71.079   2.996  1.00 16.05           C  
-ATOM   2037  CG  PRO A 297      96.990  72.086   4.158  1.00 14.63           C  
-ATOM   2038  CD  PRO A 297      95.783  71.734   5.017  1.00 16.02           C  
-ATOM   2039  N   LEU A 298      97.929  67.924   3.572  1.00 15.48           N  
-ATOM   2040  CA  LEU A 298      99.054  67.081   3.976  1.00 14.63           C  
-ATOM   2041  C   LEU A 298     100.131  67.395   2.925  1.00 15.27           C  
-ATOM   2042  O   LEU A 298     100.818  66.512   2.416  1.00 13.75           O  
-ATOM   2043  CB  LEU A 298      98.652  65.603   3.942  1.00 13.55           C  
-ATOM   2044  CG  LEU A 298      97.701  65.258   5.099  1.00 14.32           C  
-ATOM   2045  CD1 LEU A 298      97.366  63.759   5.036  1.00 14.36           C  
-ATOM   2046  CD2 LEU A 298      98.334  65.649   6.442  1.00 14.23           C  
-ATOM   2047  N   TYR A 299     100.260  68.680   2.614  1.00 14.50           N  
-ATOM   2048  CA  TYR A 299     101.207  69.117   1.610  1.00 15.22           C  
-ATOM   2049  C   TYR A 299     101.398  70.620   1.707  1.00 17.10           C  
-ATOM   2050  O   TYR A 299     100.602  71.326   2.339  1.00 16.18           O  
-ATOM   2051  CB  TYR A 299     100.685  68.768   0.212  1.00 15.89           C  
-ATOM   2052  CG  TYR A 299      99.358  69.431  -0.130  1.00 15.54           C  
-ATOM   2053  CD1 TYR A 299      98.143  68.812   0.173  1.00 18.28           C  
-ATOM   2054  CD2 TYR A 299      99.319  70.701  -0.715  1.00 16.55           C  
-ATOM   2055  CE1 TYR A 299      96.907  69.442  -0.095  1.00 17.44           C  
-ATOM   2056  CE2 TYR A 299      98.092  71.344  -0.997  1.00 17.61           C  
-ATOM   2057  CZ  TYR A 299      96.891  70.709  -0.688  1.00 18.64           C  
-ATOM   2058  OH  TYR A 299      95.687  71.333  -1.012  1.00 19.93           O  
-ATOM   2059  N   GLY A 300     102.458  71.104   1.068  1.00 19.20           N  
-ATOM   2060  CA  GLY A 300     102.741  72.528   1.084  1.00 16.93           C  
-ATOM   2061  C   GLY A 300     102.730  73.102  -0.321  1.00 19.69           C  
-ATOM   2062  O   GLY A 300     102.957  72.379  -1.303  1.00 18.27           O  
-ATOM   2063  N   ARG A 301     102.422  74.392  -0.416  1.00 18.08           N  
-ATOM   2064  CA  ARG A 301     102.409  75.109  -1.691  1.00 19.20           C  
-ATOM   2065  C   ARG A 301     103.610  76.052  -1.616  1.00 18.48           C  
-ATOM   2066  O   ARG A 301     103.710  76.851  -0.690  1.00 18.32           O  
-ATOM   2067  CB  ARG A 301     101.129  75.937  -1.822  1.00 21.25           C  
-ATOM   2068  CG  ARG A 301      99.902  75.106  -2.070  1.00 21.29           C  
-ATOM   2069  CD  ARG A 301      99.387  75.337  -3.458  1.00 23.22           C  
-ATOM   2070  NE  ARG A 301      98.330  74.389  -3.711  1.00 21.95           N  
-ATOM   2071  CZ  ARG A 301      98.089  73.876  -4.898  1.00 23.72           C  
-ATOM   2072  NH1 ARG A 301      98.832  74.257  -5.929  1.00 20.83           N  
-ATOM   2073  NH2 ARG A 301      97.161  72.937  -5.036  1.00 21.60           N  
-ATOM   2074  N   SER A 302     104.508  75.982  -2.582  1.00 18.70           N  
-ATOM   2075  CA  SER A 302     105.688  76.836  -2.523  1.00 18.09           C  
-ATOM   2076  C   SER A 302     105.674  78.050  -3.448  1.00 19.38           C  
-ATOM   2077  O   SER A 302     104.931  78.110  -4.427  1.00 19.14           O  
-ATOM   2078  CB  SER A 302     106.931  76.001  -2.810  1.00 18.92           C  
-ATOM   2079  OG  SER A 302     106.831  75.348  -4.067  1.00 19.37           O  
-ATOM   2080  N   PHE A 303     106.524  79.016  -3.120  1.00 20.69           N  
-ATOM   2081  CA  PHE A 303     106.661  80.236  -3.903  1.00 22.04           C  
-ATOM   2082  C   PHE A 303     108.157  80.528  -3.964  1.00 22.22           C  
-ATOM   2083  O   PHE A 303     108.821  80.576  -2.931  1.00 21.35           O  
-ATOM   2084  CB  PHE A 303     105.942  81.385  -3.208  1.00 21.24           C  
-ATOM   2085  CG  PHE A 303     104.486  81.133  -2.987  1.00 22.74           C  
-ATOM   2086  CD1 PHE A 303     104.041  80.527  -1.818  1.00 22.45           C  
-ATOM   2087  CD2 PHE A 303     103.550  81.492  -3.958  1.00 21.89           C  
-ATOM   2088  CE1 PHE A 303     102.662  80.279  -1.620  1.00 23.40           C  
-ATOM   2089  CE2 PHE A 303     102.185  81.251  -3.771  1.00 23.41           C  
-ATOM   2090  CZ  PHE A 303     101.741  80.646  -2.602  1.00 21.72           C  
-ATOM   2091  N   ALA A 304     108.677  80.710  -5.167  1.00 21.94           N  
-ATOM   2092  CA  ALA A 304     110.094  80.956  -5.340  1.00 23.07           C  
-ATOM   2093  C   ALA A 304     110.413  82.442  -5.508  1.00 25.94           C  
-ATOM   2094  O   ALA A 304     109.564  83.232  -5.936  1.00 27.80           O  
-ATOM   2095  CB  ALA A 304     110.613  80.158  -6.545  1.00 23.97           C  
-ATOM   2096  N   ASN A 305     111.638  82.816  -5.148  1.00 27.09           N  
-ATOM   2097  CA  ASN A 305     112.093  84.199  -5.277  1.00 29.05           C  
-ATOM   2098  C   ASN A 305     111.112  85.172  -4.614  1.00 28.62           C  
-ATOM   2099  O   ASN A 305     110.641  86.107  -5.258  1.00 29.04           O  
-ATOM   2100  CB  ASN A 305     112.234  84.539  -6.766  1.00 29.52           C  
-ATOM   2101  CG  ASN A 305     113.021  83.488  -7.527  1.00 31.37           C  
-ATOM   2102  OD1 ASN A 305     114.185  83.247  -7.221  1.00 36.97           O  
-ATOM   2103  ND2 ASN A 305     112.387  82.845  -8.513  1.00 31.21           N  
-ATOM   2104  N   THR A 306     110.803  84.959  -3.337  1.00 27.26           N  
-ATOM   2105  CA  THR A 306     109.863  85.836  -2.634  1.00 27.09           C  
-ATOM   2106  C   THR A 306     110.457  86.238  -1.293  1.00 27.58           C  
-ATOM   2107  O   THR A 306     111.143  85.444  -0.654  1.00 29.21           O  
-ATOM   2108  CB  THR A 306     108.490  85.128  -2.434  1.00 27.56           C  
-ATOM   2109  OG1 THR A 306     107.528  86.060  -1.912  1.00 26.41           O  
-ATOM   2110  CG2 THR A 306     108.627  83.925  -1.471  1.00 25.80           C  
-ATOM   2111  N   ASP A 307     110.215  87.473  -0.869  1.00 27.28           N  
-ATOM   2112  CA  ASP A 307     110.759  87.940   0.396  1.00 28.11           C  
-ATOM   2113  C   ASP A 307     110.027  87.382   1.607  1.00 28.82           C  
-ATOM   2114  O   ASP A 307     110.570  87.347   2.713  1.00 30.66           O  
-ATOM   2115  CB  ASP A 307     110.729  89.469   0.463  1.00 32.23           C  
-ATOM   2116  CG  ASP A 307     111.626  90.117  -0.586  1.00 35.54           C  
-ATOM   2117  OD1 ASP A 307     112.710  89.562  -0.869  1.00 34.82           O  
-ATOM   2118  OD2 ASP A 307     111.247  91.178  -1.115  1.00 38.37           O  
-ATOM   2119  N   GLY A 308     108.791  86.954   1.411  1.00 26.92           N  
-ATOM   2120  CA  GLY A 308     108.041  86.424   2.525  1.00 24.50           C  
-ATOM   2121  C   GLY A 308     106.584  86.298   2.159  1.00 22.96           C  
-ATOM   2122  O   GLY A 308     106.223  86.499   1.006  1.00 23.60           O  
-ATOM   2123  N   PRO A 309     105.720  85.956   3.118  1.00 25.11           N  
-ATOM   2124  CA  PRO A 309     104.283  85.806   2.858  1.00 26.36           C  
-ATOM   2125  C   PRO A 309     103.663  87.114   2.377  1.00 27.85           C  
-ATOM   2126  O   PRO A 309     103.989  88.185   2.904  1.00 28.06           O  
-ATOM   2127  CB  PRO A 309     103.727  85.387   4.215  1.00 26.46           C  
-ATOM   2128  CG  PRO A 309     104.905  84.705   4.881  1.00 29.97           C  
-ATOM   2129  CD  PRO A 309     106.039  85.621   4.517  1.00 26.58           C  
-ATOM   2130  N   GLY A 310     102.765  87.018   1.398  1.00 27.59           N  
-ATOM   2131  CA  GLY A 310     102.094  88.199   0.871  1.00 28.60           C  
-ATOM   2132  C   GLY A 310     103.016  89.134   0.108  1.00 30.66           C  
-ATOM   2133  O   GLY A 310     102.819  90.350   0.113  1.00 31.70           O  
-ATOM   2134  N   LYS A 311     104.012  88.564  -0.558  1.00 26.73           N  
-ATOM   2135  CA  LYS A 311     104.974  89.336  -1.312  1.00 29.01           C  
-ATOM   2136  C   LYS A 311     105.065  88.818  -2.734  1.00 29.43           C  
-ATOM   2137  O   LYS A 311     104.675  87.695  -3.033  1.00 29.42           O  
-ATOM   2138  CB  LYS A 311     106.354  89.223  -0.671  1.00 29.90           C  
-ATOM   2139  CG  LYS A 311     106.464  89.807   0.728  1.00 34.50           C  
-ATOM   2140  CD  LYS A 311     106.515  91.330   0.676  1.00 39.86           C  
-ATOM   2141  CE  LYS A 311     106.917  91.937   2.023  1.00 42.70           C  
-ATOM   2142  NZ  LYS A 311     107.063  93.429   1.903  1.00 47.54           N  
-ATOM   2143  N   PRO A 312     105.598  89.643  -3.638  1.00 30.48           N  
-ATOM   2144  CA  PRO A 312     105.727  89.210  -5.028  1.00 29.16           C  
-ATOM   2145  C   PRO A 312     106.634  87.987  -5.049  1.00 28.67           C  
-ATOM   2146  O   PRO A 312     107.481  87.817  -4.167  1.00 26.80           O  
-ATOM   2147  CB  PRO A 312     106.375  90.422  -5.702  1.00 32.34           C  
-ATOM   2148  CG  PRO A 312     105.858  91.591  -4.852  1.00 31.81           C  
-ATOM   2149  CD  PRO A 312     106.019  91.045  -3.465  1.00 30.75           C  
-ATOM   2150  N   TYR A 313     106.436  87.125  -6.033  1.00 27.37           N  
-ATOM   2151  CA  TYR A 313     107.263  85.939  -6.169  1.00 27.68           C  
-ATOM   2152  C   TYR A 313     107.395  85.694  -7.660  1.00 28.02           C  
-ATOM   2153  O   TYR A 313     106.738  86.353  -8.464  1.00 27.93           O  
-ATOM   2154  CB  TYR A 313     106.609  84.712  -5.481  1.00 25.76           C  
-ATOM   2155  CG  TYR A 313     105.337  84.217  -6.147  1.00 22.76           C  
-ATOM   2156  CD1 TYR A 313     104.118  84.883  -5.974  1.00 23.21           C  
-ATOM   2157  CD2 TYR A 313     105.364  83.102  -6.985  1.00 24.10           C  
-ATOM   2158  CE1 TYR A 313     102.949  84.444  -6.631  1.00 23.40           C  
-ATOM   2159  CE2 TYR A 313     104.205  82.654  -7.647  1.00 24.58           C  
-ATOM   2160  CZ  TYR A 313     103.005  83.327  -7.464  1.00 24.86           C  
-ATOM   2161  OH  TYR A 313     101.872  82.864  -8.102  1.00 25.86           O  
-ATOM   2162  N   ASN A 314     108.254  84.759  -8.032  1.00 27.60           N  
-ATOM   2163  CA  ASN A 314     108.423  84.437  -9.435  1.00 28.47           C  
-ATOM   2164  C   ASN A 314     108.604  82.925  -9.591  1.00 26.67           C  
-ATOM   2165  O   ASN A 314     109.675  82.389  -9.338  1.00 25.92           O  
-ATOM   2166  CB  ASN A 314     109.620  85.205  -9.985  1.00 32.28           C  
-ATOM   2167  CG  ASN A 314     109.993  84.767 -11.375  1.00 37.10           C  
-ATOM   2168  OD1 ASN A 314     109.127  84.407 -12.183  1.00 38.56           O  
-ATOM   2169  ND2 ASN A 314     111.292  84.800 -11.674  1.00 38.73           N  
-ATOM   2170  N   GLY A 315     107.539  82.245  -9.998  1.00 27.47           N  
-ATOM   2171  CA  GLY A 315     107.607  80.803 -10.157  1.00 26.54           C  
-ATOM   2172  C   GLY A 315     107.352  80.089  -8.831  1.00 25.50           C  
-ATOM   2173  O   GLY A 315     107.432  80.707  -7.769  1.00 22.92           O  
-ATOM   2174  N   VAL A 316     107.039  78.794  -8.885  1.00 24.33           N  
-ATOM   2175  CA  VAL A 316     106.786  78.025  -7.665  1.00 24.93           C  
-ATOM   2176  C   VAL A 316     107.829  76.930  -7.418  1.00 26.00           C  
-ATOM   2177  O   VAL A 316     107.715  76.157  -6.462  1.00 25.38           O  
-ATOM   2178  CB  VAL A 316     105.390  77.397  -7.688  1.00 24.68           C  
-ATOM   2179  CG1 VAL A 316     104.347  78.501  -7.672  1.00 24.26           C  
-ATOM   2180  CG2 VAL A 316     105.221  76.516  -8.928  1.00 24.44           C  
-ATOM   2181  N   GLY A 317     108.851  76.866  -8.268  1.00 23.20           N  
-ATOM   2182  CA  GLY A 317     109.884  75.852  -8.079  1.00 22.24           C  
-ATOM   2183  C   GLY A 317     109.427  74.448  -8.447  1.00 22.82           C  
-ATOM   2184  O   GLY A 317     108.418  74.261  -9.124  1.00 21.18           O  
-ATOM   2185  N   GLN A 318     110.163  73.442  -8.004  1.00 23.78           N  
-ATOM   2186  CA  GLN A 318     109.773  72.086  -8.322  1.00 24.15           C  
-ATOM   2187  C   GLN A 318     108.716  71.594  -7.323  1.00 23.61           C  
-ATOM   2188  O   GLN A 318     108.028  72.395  -6.695  1.00 23.03           O  
-ATOM   2189  CB  GLN A 318     111.012  71.184  -8.309  1.00 27.79           C  
-ATOM   2190  CG  GLN A 318     112.019  71.522  -9.427  1.00 31.84           C  
-ATOM   2191  CD  GLN A 318     111.386  71.383 -10.808  1.00 36.85           C  
-ATOM   2192  OE1 GLN A 318     111.189  72.409 -11.511  1.00 37.64           O  
-ATOM   2193  NE2 GLN A 318     111.064  70.167 -11.217  1.00 36.11           N  
-ATOM   2194  N   GLY A 319     108.565  70.280  -7.204  1.00 21.69           N  
-ATOM   2195  CA  GLY A 319     107.604  69.732  -6.261  1.00 22.95           C  
-ATOM   2196  C   GLY A 319     107.829  68.247  -6.093  1.00 21.77           C  
-ATOM   2197  O   GLY A 319     108.679  67.665  -6.779  1.00 20.59           O  
-ATOM   2198  N   SER A 320     107.087  67.620  -5.185  1.00 18.76           N  
-ATOM   2199  CA  SER A 320     107.237  66.191  -4.993  1.00 19.16           C  
-ATOM   2200  C   SER A 320     106.757  65.430  -6.222  1.00 20.10           C  
-ATOM   2201  O   SER A 320     107.455  64.548  -6.720  1.00 17.22           O  
-ATOM   2202  CB  SER A 320     106.440  65.719  -3.770  1.00 18.61           C  
-ATOM   2203  OG  SER A 320     106.910  66.362  -2.597  1.00 15.57           O  
-ATOM   2204  N   TRP A 321     105.569  65.774  -6.721  1.00 17.95           N  
-ATOM   2205  CA  TRP A 321     105.014  65.061  -7.867  1.00 18.61           C  
-ATOM   2206  C   TRP A 321     104.589  66.013  -8.987  1.00 20.47           C  
-ATOM   2207  O   TRP A 321     104.491  65.608 -10.141  1.00 19.95           O  
-ATOM   2208  CB  TRP A 321     103.829  64.221  -7.395  1.00 17.27           C  
-ATOM   2209  CG  TRP A 321     104.218  63.391  -6.222  1.00 17.23           C  
-ATOM   2210  CD1 TRP A 321     103.882  63.590  -4.906  1.00 16.92           C  
-ATOM   2211  CD2 TRP A 321     105.100  62.272  -6.249  1.00 16.88           C  
-ATOM   2212  NE1 TRP A 321     104.509  62.665  -4.118  1.00 16.20           N  
-ATOM   2213  CE2 TRP A 321     105.265  61.841  -4.918  1.00 17.76           C  
-ATOM   2214  CE3 TRP A 321     105.780  61.590  -7.282  1.00 17.62           C  
-ATOM   2215  CZ2 TRP A 321     106.083  60.754  -4.579  1.00 18.52           C  
-ATOM   2216  CZ3 TRP A 321     106.591  60.517  -6.951  1.00 15.66           C  
-ATOM   2217  CH2 TRP A 321     106.738  60.107  -5.605  1.00 18.68           C  
-ATOM   2218  N   GLU A 322     104.311  67.261  -8.623  1.00 18.70           N  
-ATOM   2219  CA  GLU A 322     103.967  68.289  -9.599  1.00 21.09           C  
-ATOM   2220  C   GLU A 322     104.578  69.561  -9.062  1.00 20.12           C  
-ATOM   2221  O   GLU A 322     104.722  69.711  -7.844  1.00 20.68           O  
-ATOM   2222  CB  GLU A 322     102.467  68.459  -9.742  1.00 23.90           C  
-ATOM   2223  CG  GLU A 322     101.816  69.086  -8.554  1.00 25.69           C  
-ATOM   2224  CD  GLU A 322     100.326  69.192  -8.746  1.00 33.96           C  
-ATOM   2225  OE1 GLU A 322      99.594  68.410  -8.106  1.00 34.46           O  
-ATOM   2226  OE2 GLU A 322      99.894  70.045  -9.557  1.00 33.47           O  
-ATOM   2227  N   ASN A 323     104.924  70.491  -9.946  1.00 19.09           N  
-ATOM   2228  CA  ASN A 323     105.561  71.717  -9.498  1.00 21.41           C  
-ATOM   2229  C   ASN A 323     104.730  72.550  -8.522  1.00 19.18           C  
-ATOM   2230  O   ASN A 323     103.520  72.658  -8.664  1.00 19.54           O  
-ATOM   2231  CB  ASN A 323     105.971  72.580 -10.710  1.00 22.59           C  
-ATOM   2232  CG  ASN A 323     107.006  71.880 -11.602  1.00 30.25           C  
-ATOM   2233  OD1 ASN A 323     107.809  71.064 -11.129  1.00 26.66           O  
-ATOM   2234  ND2 ASN A 323     106.999  72.211 -12.887  1.00 31.63           N  
-ATOM   2235  N   GLY A 324     105.412  73.124  -7.532  1.00 19.86           N  
-ATOM   2236  CA  GLY A 324     104.767  73.984  -6.549  1.00 18.05           C  
-ATOM   2237  C   GLY A 324     104.052  73.283  -5.410  1.00 19.69           C  
-ATOM   2238  O   GLY A 324     103.551  73.944  -4.499  1.00 19.79           O  
-ATOM   2239  N   VAL A 325     104.000  71.952  -5.449  1.00 18.27           N  
-ATOM   2240  CA  VAL A 325     103.333  71.189  -4.400  1.00 17.01           C  
-ATOM   2241  C   VAL A 325     104.286  70.149  -3.830  1.00 19.50           C  
-ATOM   2242  O   VAL A 325     104.875  69.347  -4.574  1.00 21.09           O  
-ATOM   2243  CB  VAL A 325     102.069  70.503  -4.958  1.00 18.59           C  
-ATOM   2244  CG1 VAL A 325     101.371  69.708  -3.885  1.00 15.81           C  
-ATOM   2245  CG2 VAL A 325     101.143  71.561  -5.509  1.00 17.33           C  
-ATOM   2246  N   TRP A 326     104.428  70.158  -2.503  1.00 17.82           N  
-ATOM   2247  CA  TRP A 326     105.344  69.243  -1.822  1.00 16.84           C  
-ATOM   2248  C   TRP A 326     104.657  68.412  -0.747  1.00 17.72           C  
-ATOM   2249  O   TRP A 326     103.903  68.950   0.057  1.00 13.26           O  
-ATOM   2250  CB  TRP A 326     106.458  70.030  -1.123  1.00 15.75           C  
-ATOM   2251  CG  TRP A 326     107.246  70.922  -2.033  1.00 18.91           C  
-ATOM   2252  CD1 TRP A 326     106.950  72.201  -2.404  1.00 21.39           C  
-ATOM   2253  CD2 TRP A 326     108.448  70.569  -2.710  1.00 19.85           C  
-ATOM   2254  NE1 TRP A 326     107.915  72.677  -3.286  1.00 21.84           N  
-ATOM   2255  CE2 TRP A 326     108.841  71.683  -3.488  1.00 23.20           C  
-ATOM   2256  CE3 TRP A 326     109.233  69.408  -2.743  1.00 20.11           C  
-ATOM   2257  CZ2 TRP A 326     109.990  71.664  -4.291  1.00 22.09           C  
-ATOM   2258  CZ3 TRP A 326     110.370  69.395  -3.543  1.00 23.41           C  
-ATOM   2259  CH2 TRP A 326     110.732  70.515  -4.303  1.00 21.83           C  
-ATOM   2260  N   ASP A 327     104.945  67.110  -0.716  1.00 17.63           N  
-ATOM   2261  CA  ASP A 327     104.360  66.238   0.313  1.00 16.22           C  
-ATOM   2262  C   ASP A 327     104.786  66.760   1.686  1.00 16.42           C  
-ATOM   2263  O   ASP A 327     105.943  67.139   1.883  1.00 14.23           O  
-ATOM   2264  CB  ASP A 327     104.918  64.813   0.225  1.00 14.52           C  
-ATOM   2265  CG  ASP A 327     104.435  64.050  -1.000  1.00 18.03           C  
-ATOM   2266  OD1 ASP A 327     103.449  64.463  -1.657  1.00 16.70           O  
-ATOM   2267  OD2 ASP A 327     105.043  63.017  -1.292  1.00 19.20           O  
-ATOM   2268  N   TYR A 328     103.872  66.740   2.644  1.00 15.59           N  
-ATOM   2269  CA  TYR A 328     104.234  67.156   3.986  1.00 15.78           C  
-ATOM   2270  C   TYR A 328     105.398  66.295   4.478  1.00 16.41           C  
-ATOM   2271  O   TYR A 328     106.265  66.767   5.212  1.00 14.75           O  
-ATOM   2272  CB  TYR A 328     103.067  66.966   4.955  1.00 15.33           C  
-ATOM   2273  CG  TYR A 328     103.475  67.240   6.376  1.00 14.54           C  
-ATOM   2274  CD1 TYR A 328     103.958  68.493   6.730  1.00 16.12           C  
-ATOM   2275  CD2 TYR A 328     103.407  66.249   7.367  1.00 16.93           C  
-ATOM   2276  CE1 TYR A 328     104.361  68.769   8.013  1.00 15.63           C  
-ATOM   2277  CE2 TYR A 328     103.819  66.526   8.684  1.00 16.30           C  
-ATOM   2278  CZ  TYR A 328     104.293  67.790   8.986  1.00 17.14           C  
-ATOM   2279  OH  TYR A 328     104.740  68.129  10.239  1.00 23.09           O  
-ATOM   2280  N   LYS A 329     105.443  65.030   4.079  1.00 15.49           N  
-ATOM   2281  CA  LYS A 329     106.550  64.222   4.590  1.00 19.17           C  
-ATOM   2282  C   LYS A 329     107.931  64.748   4.228  1.00 21.26           C  
-ATOM   2283  O   LYS A 329     108.903  64.408   4.887  1.00 21.00           O  
-ATOM   2284  CB  LYS A 329     106.416  62.770   4.175  1.00 23.18           C  
-ATOM   2285  CG  LYS A 329     106.059  62.573   2.771  1.00 29.60           C  
-ATOM   2286  CD  LYS A 329     105.840  61.090   2.512  1.00 38.30           C  
-ATOM   2287  CE  LYS A 329     105.377  60.846   1.080  1.00 39.07           C  
-ATOM   2288  NZ  LYS A 329     105.327  59.378   0.811  1.00 43.24           N  
-ATOM   2289  N   ALA A 330     108.000  65.621   3.231  1.00 19.01           N  
-ATOM   2290  CA  ALA A 330     109.260  66.212   2.790  1.00 20.91           C  
-ATOM   2291  C   ALA A 330     109.553  67.549   3.474  1.00 20.67           C  
-ATOM   2292  O   ALA A 330     110.611  68.143   3.281  1.00 22.38           O  
-ATOM   2293  CB  ALA A 330     109.196  66.432   1.290  1.00 20.99           C  
-ATOM   2294  N   LEU A 331     108.647  68.006   4.319  1.00 17.96           N  
-ATOM   2295  CA  LEU A 331     108.805  69.329   4.904  1.00 19.12           C  
-ATOM   2296  C   LEU A 331     109.045  69.375   6.401  1.00 20.79           C  
-ATOM   2297  O   LEU A 331     108.480  68.579   7.137  1.00 20.16           O  
-ATOM   2298  CB  LEU A 331     107.544  70.130   4.589  1.00 18.83           C  
-ATOM   2299  CG  LEU A 331     107.149  70.122   3.113  1.00 17.31           C  
-ATOM   2300  CD1 LEU A 331     105.732  70.749   2.913  1.00 14.47           C  
-ATOM   2301  CD2 LEU A 331     108.216  70.902   2.357  1.00 16.30           C  
-ATOM   2302  N   PRO A 332     109.864  70.342   6.871  1.00 20.24           N  
-ATOM   2303  CA  PRO A 332     110.558  71.370   6.078  1.00 20.91           C  
-ATOM   2304  C   PRO A 332     111.753  70.796   5.339  1.00 21.19           C  
-ATOM   2305  O   PRO A 332     112.324  69.786   5.754  1.00 22.07           O  
-ATOM   2306  CB  PRO A 332     111.008  72.369   7.129  1.00 19.72           C  
-ATOM   2307  CG  PRO A 332     111.395  71.467   8.262  1.00 24.56           C  
-ATOM   2308  CD  PRO A 332     110.236  70.451   8.292  1.00 23.10           C  
-ATOM   2309  N   GLN A 333     112.139  71.443   4.253  1.00 21.93           N  
-ATOM   2310  CA  GLN A 333     113.284  70.987   3.486  1.00 21.09           C  
-ATOM   2311  C   GLN A 333     114.583  71.447   4.146  1.00 23.09           C  
-ATOM   2312  O   GLN A 333     114.597  72.416   4.898  1.00 22.29           O  
-ATOM   2313  CB  GLN A 333     113.227  71.561   2.070  1.00 22.18           C  
-ATOM   2314  CG  GLN A 333     111.911  71.277   1.332  1.00 20.73           C  
-ATOM   2315  CD  GLN A 333     111.915  71.852  -0.064  1.00 20.69           C  
-ATOM   2316  OE1 GLN A 333     112.181  73.027  -0.233  1.00 19.95           O  
-ATOM   2317  NE2 GLN A 333     111.635  71.027  -1.070  1.00 17.63           N  
-ATOM   2318  N   ALA A 334     115.677  70.749   3.853  1.00 25.03           N  
-ATOM   2319  CA  ALA A 334     116.974  71.110   4.404  1.00 25.35           C  
-ATOM   2320  C   ALA A 334     117.204  72.572   4.057  1.00 25.19           C  
-ATOM   2321  O   ALA A 334     116.849  73.003   2.962  1.00 24.61           O  
-ATOM   2322  CB  ALA A 334     118.071  70.251   3.774  1.00 26.74           C  
-ATOM   2323  N   GLY A 335     117.759  73.335   4.996  1.00 25.82           N  
-ATOM   2324  CA  GLY A 335     118.055  74.740   4.745  1.00 26.95           C  
-ATOM   2325  C   GLY A 335     116.959  75.727   5.080  1.00 26.74           C  
-ATOM   2326  O   GLY A 335     117.193  76.929   5.116  1.00 26.58           O  
-ATOM   2327  N   ALA A 336     115.755  75.237   5.334  1.00 24.30           N  
-ATOM   2328  CA  ALA A 336     114.680  76.156   5.635  1.00 23.56           C  
-ATOM   2329  C   ALA A 336     114.399  76.243   7.117  1.00 24.75           C  
-ATOM   2330  O   ALA A 336     114.690  75.322   7.886  1.00 22.21           O  
-ATOM   2331  CB  ALA A 336     113.425  75.741   4.906  1.00 24.40           C  
-ATOM   2332  N   THR A 337     113.834  77.373   7.515  1.00 22.59           N  
-ATOM   2333  CA  THR A 337     113.462  77.581   8.897  1.00 23.31           C  
-ATOM   2334  C   THR A 337     111.941  77.712   8.927  1.00 23.45           C  
-ATOM   2335  O   THR A 337     111.357  78.357   8.069  1.00 22.32           O  
-ATOM   2336  CB  THR A 337     114.092  78.869   9.444  1.00 26.18           C  
-ATOM   2337  OG1 THR A 337     115.514  78.710   9.478  1.00 28.18           O  
-ATOM   2338  CG2 THR A 337     113.590  79.158  10.847  1.00 26.01           C  
-ATOM   2339  N   GLU A 338     111.314  77.104   9.926  1.00 22.80           N  
-ATOM   2340  CA  GLU A 338     109.879  77.148  10.070  1.00 24.58           C  
-ATOM   2341  C   GLU A 338     109.442  78.392  10.824  1.00 26.28           C  
-ATOM   2342  O   GLU A 338     110.143  78.862  11.720  1.00 26.24           O  
-ATOM   2343  CB  GLU A 338     109.409  75.900  10.816  1.00 24.65           C  
-ATOM   2344  CG  GLU A 338     108.408  75.098  10.060  1.00 29.34           C  
-ATOM   2345  CD  GLU A 338     108.121  73.741  10.688  1.00 27.92           C  
-ATOM   2346  OE1 GLU A 338     107.893  73.667  11.919  1.00 27.20           O  
-ATOM   2347  OE2 GLU A 338     108.112  72.754   9.929  1.00 30.49           O  
-ATOM   2348  N   HIS A 339     108.276  78.922  10.462  1.00 25.38           N  
-ATOM   2349  CA  HIS A 339     107.738  80.098  11.121  1.00 26.04           C  
-ATOM   2350  C   HIS A 339     106.265  79.832  11.399  1.00 26.08           C  
-ATOM   2351  O   HIS A 339     105.562  79.294  10.539  1.00 24.18           O  
-ATOM   2352  CB  HIS A 339     107.872  81.323  10.217  1.00 30.02           C  
-ATOM   2353  CG  HIS A 339     109.288  81.702   9.922  1.00 34.73           C  
-ATOM   2354  ND1 HIS A 339     110.116  82.279  10.863  1.00 38.28           N  
-ATOM   2355  CD2 HIS A 339     110.026  81.578   8.794  1.00 34.92           C  
-ATOM   2356  CE1 HIS A 339     111.302  82.499  10.322  1.00 39.71           C  
-ATOM   2357  NE2 HIS A 339     111.273  82.084   9.068  1.00 36.25           N  
-ATOM   2358  N   VAL A 340     105.802  80.208  12.588  1.00 22.93           N  
-ATOM   2359  CA  VAL A 340     104.406  79.999  12.938  1.00 20.33           C  
-ATOM   2360  C   VAL A 340     103.732  81.312  13.342  1.00 21.81           C  
-ATOM   2361  O   VAL A 340     104.286  82.128  14.080  1.00 20.18           O  
-ATOM   2362  CB  VAL A 340     104.265  78.952  14.059  1.00 21.32           C  
-ATOM   2363  CG1 VAL A 340     102.779  78.699  14.360  1.00 20.69           C  
-ATOM   2364  CG2 VAL A 340     104.938  77.636  13.621  1.00 19.93           C  
-ATOM   2365  N   LEU A 341     102.536  81.513  12.812  1.00 21.68           N  
-ATOM   2366  CA  LEU A 341     101.753  82.707  13.080  1.00 22.70           C  
-ATOM   2367  C   LEU A 341     100.488  82.181  13.737  1.00 21.37           C  
-ATOM   2368  O   LEU A 341      99.513  81.859  13.059  1.00 21.93           O  
-ATOM   2369  CB  LEU A 341     101.427  83.418  11.761  1.00 22.63           C  
-ATOM   2370  CG  LEU A 341     102.656  83.916  11.008  1.00 26.36           C  
-ATOM   2371  CD1 LEU A 341     102.290  84.342   9.574  1.00 26.42           C  
-ATOM   2372  CD2 LEU A 341     103.277  85.081  11.813  1.00 28.71           C  
-ATOM   2373  N   PRO A 342     100.508  82.064  15.072  1.00 21.85           N  
-ATOM   2374  CA  PRO A 342      99.387  81.569  15.872  1.00 22.41           C  
-ATOM   2375  C   PRO A 342      98.071  82.315  15.628  1.00 22.83           C  
-ATOM   2376  O   PRO A 342      97.011  81.695  15.589  1.00 24.45           O  
-ATOM   2377  CB  PRO A 342      99.883  81.736  17.308  1.00 20.69           C  
-ATOM   2378  CG  PRO A 342     101.358  81.620  17.181  1.00 21.26           C  
-ATOM   2379  CD  PRO A 342     101.641  82.429  15.939  1.00 21.35           C  
-ATOM   2380  N   ASP A 343      98.140  83.635  15.460  1.00 24.46           N  
-ATOM   2381  CA  ASP A 343      96.936  84.435  15.225  1.00 25.85           C  
-ATOM   2382  C   ASP A 343      96.111  83.915  14.049  1.00 25.55           C  
-ATOM   2383  O   ASP A 343      94.886  84.011  14.067  1.00 28.70           O  
-ATOM   2384  CB  ASP A 343      97.277  85.904  14.933  1.00 27.20           C  
-ATOM   2385  CG  ASP A 343      97.649  86.687  16.174  1.00 31.43           C  
-ATOM   2386  OD1 ASP A 343      97.325  86.239  17.294  1.00 30.06           O  
-ATOM   2387  OD2 ASP A 343      98.257  87.774  16.017  1.00 33.87           O  
-ATOM   2388  N   ILE A 344      96.762  83.369  13.027  1.00 22.05           N  
-ATOM   2389  CA  ILE A 344      96.000  82.889  11.874  1.00 21.31           C  
-ATOM   2390  C   ILE A 344      96.055  81.382  11.683  1.00 21.21           C  
-ATOM   2391  O   ILE A 344      95.539  80.860  10.698  1.00 20.83           O  
-ATOM   2392  CB  ILE A 344      96.474  83.578  10.584  1.00 20.46           C  
-ATOM   2393  CG1 ILE A 344      97.949  83.244  10.314  1.00 22.31           C  
-ATOM   2394  CG2 ILE A 344      96.348  85.112  10.740  1.00 22.08           C  
-ATOM   2395  CD1 ILE A 344      98.426  83.698   8.960  1.00 21.36           C  
-ATOM   2396  N   MET A 345      96.689  80.697  12.632  1.00 20.65           N  
-ATOM   2397  CA  MET A 345      96.850  79.248  12.596  1.00 17.69           C  
-ATOM   2398  C   MET A 345      97.498  78.794  11.311  1.00 17.16           C  
-ATOM   2399  O   MET A 345      96.968  77.948  10.587  1.00 18.48           O  
-ATOM   2400  CB  MET A 345      95.506  78.543  12.802  1.00 19.79           C  
-ATOM   2401  CG  MET A 345      94.895  78.797  14.192  1.00 17.26           C  
-ATOM   2402  SD  MET A 345      93.489  77.758  14.565  1.00 19.15           S  
-ATOM   2403  CE  MET A 345      93.052  78.491  16.195  1.00 16.39           C  
-ATOM   2404  N   ALA A 346      98.663  79.358  11.032  1.00 16.74           N  
-ATOM   2405  CA  ALA A 346      99.371  78.990   9.819  1.00 17.22           C  
-ATOM   2406  C   ALA A 346     100.838  78.943  10.138  1.00 17.12           C  
-ATOM   2407  O   ALA A 346     101.318  79.645  11.036  1.00 17.53           O  
-ATOM   2408  CB  ALA A 346      99.115  80.019   8.710  1.00 17.61           C  
-ATOM   2409  N   SER A 347     101.542  78.105   9.396  1.00 16.24           N  
-ATOM   2410  CA  SER A 347     102.966  77.957   9.546  1.00 16.30           C  
-ATOM   2411  C   SER A 347     103.536  77.928   8.135  1.00 17.39           C  
-ATOM   2412  O   SER A 347     102.816  77.692   7.163  1.00 17.17           O  
-ATOM   2413  CB  SER A 347     103.285  76.644  10.261  1.00 18.67           C  
-ATOM   2414  OG  SER A 347     102.612  75.534   9.669  1.00 16.52           O  
-ATOM   2415  N   TYR A 348     104.824  78.209   8.012  1.00 17.53           N  
-ATOM   2416  CA  TYR A 348     105.463  78.146   6.712  1.00 18.53           C  
-ATOM   2417  C   TYR A 348     106.957  77.999   6.923  1.00 18.39           C  
-ATOM   2418  O   TYR A 348     107.468  78.276   8.013  1.00 21.42           O  
-ATOM   2419  CB  TYR A 348     105.167  79.399   5.876  1.00 19.65           C  
-ATOM   2420  CG  TYR A 348     105.703  80.691   6.431  1.00 19.87           C  
-ATOM   2421  CD1 TYR A 348     104.974  81.429   7.357  1.00 22.36           C  
-ATOM   2422  CD2 TYR A 348     106.945  81.187   6.021  1.00 22.10           C  
-ATOM   2423  CE1 TYR A 348     105.464  82.639   7.868  1.00 23.58           C  
-ATOM   2424  CE2 TYR A 348     107.447  82.396   6.525  1.00 23.81           C  
-ATOM   2425  CZ  TYR A 348     106.692  83.114   7.450  1.00 25.40           C  
-ATOM   2426  OH  TYR A 348     107.178  84.311   7.951  1.00 25.35           O  
-ATOM   2427  N   SER A 349     107.652  77.521   5.899  1.00 18.10           N  
-ATOM   2428  CA  SER A 349     109.104  77.386   5.984  1.00 18.82           C  
-ATOM   2429  C   SER A 349     109.652  78.446   5.048  1.00 20.05           C  
-ATOM   2430  O   SER A 349     109.006  78.820   4.054  1.00 19.25           O  
-ATOM   2431  CB  SER A 349     109.553  75.997   5.518  1.00 19.94           C  
-ATOM   2432  OG  SER A 349     109.318  75.815   4.130  1.00 17.89           O  
-ATOM   2433  N   TYR A 350     110.822  78.967   5.379  1.00 21.76           N  
-ATOM   2434  CA  TYR A 350     111.448  79.959   4.524  1.00 21.76           C  
-ATOM   2435  C   TYR A 350     112.938  79.727   4.517  1.00 22.32           C  
-ATOM   2436  O   TYR A 350     113.550  79.489   5.564  1.00 23.70           O  
-ATOM   2437  CB  TYR A 350     111.182  81.370   5.014  1.00 22.46           C  
-ATOM   2438  CG  TYR A 350     111.675  82.422   4.043  1.00 23.83           C  
-ATOM   2439  CD1 TYR A 350     111.080  82.566   2.792  1.00 27.63           C  
-ATOM   2440  CD2 TYR A 350     112.705  83.297   4.385  1.00 25.94           C  
-ATOM   2441  CE1 TYR A 350     111.486  83.562   1.897  1.00 28.58           C  
-ATOM   2442  CE2 TYR A 350     113.128  84.304   3.498  1.00 28.93           C  
-ATOM   2443  CZ  TYR A 350     112.504  84.430   2.254  1.00 30.76           C  
-ATOM   2444  OH  TYR A 350     112.848  85.440   1.377  1.00 30.80           O  
-ATOM   2445  N   ASP A 351     113.508  79.788   3.326  1.00 23.02           N  
-ATOM   2446  CA  ASP A 351     114.933  79.618   3.142  1.00 24.91           C  
-ATOM   2447  C   ASP A 351     115.421  80.954   2.577  1.00 26.07           C  
-ATOM   2448  O   ASP A 351     115.225  81.255   1.396  1.00 24.90           O  
-ATOM   2449  CB  ASP A 351     115.211  78.504   2.145  1.00 24.32           C  
-ATOM   2450  CG  ASP A 351     116.688  78.220   2.009  1.00 28.72           C  
-ATOM   2451  OD1 ASP A 351     117.465  79.182   2.183  1.00 29.30           O  
-ATOM   2452  OD2 ASP A 351     117.063  77.064   1.733  1.00 24.87           O  
-ATOM   2453  N   ALA A 352     116.046  81.758   3.424  1.00 27.19           N  
-ATOM   2454  CA  ALA A 352     116.519  83.064   2.979  1.00 31.28           C  
-ATOM   2455  C   ALA A 352     117.646  82.980   1.944  1.00 33.49           C  
-ATOM   2456  O   ALA A 352     117.810  83.890   1.129  1.00 33.32           O  
-ATOM   2457  CB  ALA A 352     116.963  83.896   4.185  1.00 32.56           C  
-ATOM   2458  N   THR A 353     118.412  81.891   1.953  1.00 34.29           N  
-ATOM   2459  CA  THR A 353     119.502  81.765   0.992  1.00 35.68           C  
-ATOM   2460  C   THR A 353     119.003  81.686  -0.451  1.00 35.70           C  
-ATOM   2461  O   THR A 353     119.735  82.008  -1.377  1.00 36.94           O  
-ATOM   2462  CB  THR A 353     120.379  80.539   1.277  1.00 36.39           C  
-ATOM   2463  OG1 THR A 353     119.673  79.340   0.923  1.00 38.59           O  
-ATOM   2464  CG2 THR A 353     120.747  80.497   2.743  1.00 36.37           C  
-ATOM   2465  N   ASN A 354     117.767  81.247  -0.660  1.00 33.84           N  
-ATOM   2466  CA  ASN A 354     117.256  81.192  -2.022  1.00 30.38           C  
-ATOM   2467  C   ASN A 354     115.844  81.773  -2.129  1.00 28.50           C  
-ATOM   2468  O   ASN A 354     115.208  81.693  -3.173  1.00 28.05           O  
-ATOM   2469  CB  ASN A 354     117.303  79.752  -2.564  1.00 31.67           C  
-ATOM   2470  CG  ASN A 354     116.484  78.778  -1.728  1.00 31.92           C  
-ATOM   2471  OD1 ASN A 354     115.852  79.165  -0.746  1.00 30.31           O  
-ATOM   2472  ND2 ASN A 354     116.496  77.506  -2.118  1.00 30.61           N  
-ATOM   2473  N   LYS A 355     115.367  82.370  -1.043  1.00 27.02           N  
-ATOM   2474  CA  LYS A 355     114.037  82.979  -1.016  1.00 28.32           C  
-ATOM   2475  C   LYS A 355     112.909  82.036  -1.431  1.00 26.01           C  
-ATOM   2476  O   LYS A 355     111.993  82.423  -2.171  1.00 26.55           O  
-ATOM   2477  CB  LYS A 355     114.008  84.223  -1.906  1.00 31.97           C  
-ATOM   2478  CG  LYS A 355     114.937  85.332  -1.433  1.00 35.35           C  
-ATOM   2479  CD  LYS A 355     114.712  86.589  -2.257  1.00 37.77           C  
-ATOM   2480  CE  LYS A 355     115.400  87.787  -1.615  1.00 42.21           C  
-ATOM   2481  NZ  LYS A 355     115.069  89.062  -2.317  1.00 44.44           N  
-ATOM   2482  N   PHE A 356     112.981  80.798  -0.953  1.00 24.71           N  
-ATOM   2483  CA  PHE A 356     111.960  79.807  -1.262  1.00 22.12           C  
-ATOM   2484  C   PHE A 356     111.059  79.721  -0.039  1.00 22.99           C  
-ATOM   2485  O   PHE A 356     111.532  79.516   1.090  1.00 20.72           O  
-ATOM   2486  CB  PHE A 356     112.589  78.443  -1.523  1.00 23.75           C  
-ATOM   2487  CG  PHE A 356     111.695  77.507  -2.274  1.00 24.13           C  
-ATOM   2488  CD1 PHE A 356     111.190  77.864  -3.518  1.00 21.96           C  
-ATOM   2489  CD2 PHE A 356     111.399  76.250  -1.765  1.00 23.00           C  
-ATOM   2490  CE1 PHE A 356     110.403  76.971  -4.250  1.00 23.86           C  
-ATOM   2491  CE2 PHE A 356     110.612  75.346  -2.493  1.00 22.80           C  
-ATOM   2492  CZ  PHE A 356     110.115  75.709  -3.736  1.00 22.88           C  
-ATOM   2493  N   LEU A 357     109.763  79.887  -0.259  1.00 22.94           N  
-ATOM   2494  CA  LEU A 357     108.803  79.850   0.837  1.00 23.53           C  
-ATOM   2495  C   LEU A 357     107.791  78.732   0.595  1.00 21.77           C  
-ATOM   2496  O   LEU A 357     107.352  78.524  -0.535  1.00 19.90           O  
-ATOM   2497  CB  LEU A 357     108.075  81.207   0.928  1.00 27.12           C  
-ATOM   2498  CG  LEU A 357     107.074  81.411   2.091  1.00 31.14           C  
-ATOM   2499  CD1 LEU A 357     106.902  82.893   2.374  1.00 32.60           C  
-ATOM   2500  CD2 LEU A 357     105.735  80.793   1.732  1.00 30.07           C  
-ATOM   2501  N   ILE A 358     107.427  78.002   1.647  1.00 20.48           N  
-ATOM   2502  CA  ILE A 358     106.447  76.934   1.472  1.00 18.35           C  
-ATOM   2503  C   ILE A 358     105.394  77.014   2.560  1.00 18.79           C  
-ATOM   2504  O   ILE A 358     105.733  77.037   3.747  1.00 18.91           O  
-ATOM   2505  CB  ILE A 358     107.080  75.530   1.538  1.00 18.44           C  
-ATOM   2506  CG1 ILE A 358     108.288  75.432   0.593  1.00 16.73           C  
-ATOM   2507  CG2 ILE A 358     106.033  74.489   1.123  1.00 14.30           C  
-ATOM   2508  CD1 ILE A 358     109.004  74.048   0.623  1.00 16.77           C  
-ATOM   2509  N   SER A 359     104.126  77.058   2.141  1.00 16.67           N  
-ATOM   2510  CA  SER A 359     102.995  77.128   3.059  1.00 16.01           C  
-ATOM   2511  C   SER A 359     102.413  75.714   3.258  1.00 15.20           C  
-ATOM   2512  O   SER A 359     101.886  75.109   2.321  1.00 14.87           O  
-ATOM   2513  CB  SER A 359     101.928  78.071   2.495  1.00 15.97           C  
-ATOM   2514  OG  SER A 359     100.761  78.084   3.297  1.00 13.78           O  
-ATOM   2515  N   TYR A 360     102.553  75.210   4.486  1.00 15.49           N  
-ATOM   2516  CA  TYR A 360     102.064  73.899   4.903  1.00 14.93           C  
-ATOM   2517  C   TYR A 360     101.848  73.972   6.408  1.00 15.01           C  
-ATOM   2518  O   TYR A 360     102.386  74.861   7.063  1.00 15.93           O  
-ATOM   2519  CB  TYR A 360     103.079  72.794   4.598  1.00 15.14           C  
-ATOM   2520  CG  TYR A 360     104.391  72.952   5.337  1.00 18.70           C  
-ATOM   2521  CD1 TYR A 360     105.417  73.758   4.825  1.00 19.78           C  
-ATOM   2522  CD2 TYR A 360     104.593  72.325   6.562  1.00 18.53           C  
-ATOM   2523  CE1 TYR A 360     106.604  73.929   5.514  1.00 19.90           C  
-ATOM   2524  CE2 TYR A 360     105.771  72.490   7.265  1.00 20.47           C  
-ATOM   2525  CZ  TYR A 360     106.775  73.293   6.736  1.00 20.77           C  
-ATOM   2526  OH  TYR A 360     107.938  73.476   7.437  1.00 22.56           O  
-ATOM   2527  N   ASP A 361     101.059  73.044   6.953  1.00 14.40           N  
-ATOM   2528  CA  ASP A 361     100.795  73.012   8.386  1.00 13.33           C  
-ATOM   2529  C   ASP A 361     101.780  72.085   9.074  1.00 14.52           C  
-ATOM   2530  O   ASP A 361     102.036  70.981   8.596  1.00 14.79           O  
-ATOM   2531  CB  ASP A 361      99.407  72.454   8.695  1.00 14.68           C  
-ATOM   2532  CG  ASP A 361      98.284  73.326   8.165  1.00 15.69           C  
-ATOM   2533  OD1 ASP A 361      98.532  74.515   7.857  1.00 16.27           O  
-ATOM   2534  OD2 ASP A 361      97.155  72.808   8.087  1.00 16.18           O  
-ATOM   2535  N   ASN A 362     102.304  72.518  10.206  1.00 14.62           N  
-ATOM   2536  CA  ASN A 362     103.199  71.666  10.956  1.00 14.85           C  
-ATOM   2537  C   ASN A 362     102.408  71.135  12.151  1.00 15.47           C  
-ATOM   2538  O   ASN A 362     101.219  71.456  12.327  1.00 14.53           O  
-ATOM   2539  CB  ASN A 362     104.455  72.444  11.371  1.00 15.62           C  
-ATOM   2540  CG  ASN A 362     104.167  73.543  12.368  1.00 19.49           C  
-ATOM   2541  OD1 ASN A 362     103.028  73.708  12.837  1.00 16.46           O  
-ATOM   2542  ND2 ASN A 362     105.210  74.299  12.715  1.00 18.83           N  
-ATOM   2543  N   PRO A 363     103.047  70.313  12.992  1.00 16.29           N  
-ATOM   2544  CA  PRO A 363     102.356  69.753  14.154  1.00 16.50           C  
-ATOM   2545  C   PRO A 363     101.685  70.788  15.032  1.00 16.20           C  
-ATOM   2546  O   PRO A 363     100.569  70.572  15.499  1.00 17.19           O  
-ATOM   2547  CB  PRO A 363     103.466  68.966  14.877  1.00 20.69           C  
-ATOM   2548  CG  PRO A 363     104.366  68.532  13.712  1.00 20.41           C  
-ATOM   2549  CD  PRO A 363     104.424  69.788  12.879  1.00 20.23           C  
-ATOM   2550  N   GLN A 364     102.353  71.912  15.254  1.00 15.13           N  
-ATOM   2551  CA  GLN A 364     101.759  72.947  16.094  1.00 16.48           C  
-ATOM   2552  C   GLN A 364     100.440  73.438  15.521  1.00 15.36           C  
-ATOM   2553  O   GLN A 364      99.482  73.652  16.243  1.00 14.27           O  
-ATOM   2554  CB  GLN A 364     102.687  74.163  16.222  1.00 18.90           C  
-ATOM   2555  CG  GLN A 364     102.018  75.286  17.015  1.00 22.13           C  
-ATOM   2556  CD  GLN A 364     102.890  76.501  17.208  1.00 22.58           C  
-ATOM   2557  OE1 GLN A 364     104.078  76.493  16.874  1.00 26.94           O  
-ATOM   2558  NE2 GLN A 364     102.305  77.563  17.756  1.00 23.52           N  
-ATOM   2559  N   VAL A 365     100.410  73.639  14.211  1.00 15.71           N  
-ATOM   2560  CA  VAL A 365      99.205  74.135  13.553  1.00 14.90           C  
-ATOM   2561  C   VAL A 365      98.113  73.077  13.581  1.00 15.22           C  
-ATOM   2562  O   VAL A 365      96.942  73.386  13.778  1.00 18.40           O  
-ATOM   2563  CB  VAL A 365      99.539  74.595  12.116  1.00 14.96           C  
-ATOM   2564  CG1 VAL A 365      98.254  74.984  11.352  1.00 15.82           C  
-ATOM   2565  CG2 VAL A 365     100.456  75.801  12.204  1.00 16.37           C  
-ATOM   2566  N   ALA A 366      98.502  71.817  13.431  1.00 15.16           N  
-ATOM   2567  CA  ALA A 366      97.525  70.745  13.491  1.00 15.38           C  
-ATOM   2568  C   ALA A 366      96.839  70.748  14.858  1.00 15.06           C  
-ATOM   2569  O   ALA A 366      95.642  70.501  14.950  1.00 16.83           O  
-ATOM   2570  CB  ALA A 366      98.193  69.386  13.240  1.00 14.53           C  
-ATOM   2571  N   ASN A 367      97.593  71.001  15.922  1.00 15.00           N  
-ATOM   2572  CA  ASN A 367      96.979  71.031  17.249  1.00 15.60           C  
-ATOM   2573  C   ASN A 367      96.056  72.240  17.336  1.00 16.53           C  
-ATOM   2574  O   ASN A 367      94.942  72.151  17.849  1.00 18.17           O  
-ATOM   2575  CB  ASN A 367      98.044  71.110  18.345  1.00 15.66           C  
-ATOM   2576  CG  ASN A 367      98.673  69.750  18.631  1.00 19.09           C  
-ATOM   2577  OD1 ASN A 367      97.982  68.791  18.991  1.00 19.09           O  
-ATOM   2578  ND2 ASN A 367      99.981  69.662  18.445  1.00 20.23           N  
-ATOM   2579  N   LEU A 368      96.531  73.371  16.831  1.00 15.77           N  
-ATOM   2580  CA  LEU A 368      95.722  74.582  16.860  1.00 17.24           C  
-ATOM   2581  C   LEU A 368      94.386  74.358  16.152  1.00 17.37           C  
-ATOM   2582  O   LEU A 368      93.334  74.717  16.686  1.00 18.46           O  
-ATOM   2583  CB  LEU A 368      96.466  75.744  16.209  1.00 14.47           C  
-ATOM   2584  CG  LEU A 368      97.610  76.348  17.035  1.00 20.31           C  
-ATOM   2585  CD1 LEU A 368      98.302  77.419  16.204  1.00 17.96           C  
-ATOM   2586  CD2 LEU A 368      97.067  76.940  18.360  1.00 18.01           C  
-ATOM   2587  N   LYS A 369      94.429  73.760  14.965  1.00 17.12           N  
-ATOM   2588  CA  LYS A 369      93.215  73.514  14.211  1.00 16.33           C  
-ATOM   2589  C   LYS A 369      92.327  72.519  14.915  1.00 17.13           C  
-ATOM   2590  O   LYS A 369      91.111  72.547  14.733  1.00 19.38           O  
-ATOM   2591  CB  LYS A 369      93.544  73.047  12.776  1.00 14.65           C  
-ATOM   2592  CG  LYS A 369      94.137  74.169  11.923  1.00 15.37           C  
-ATOM   2593  CD  LYS A 369      94.291  73.807  10.437  1.00 15.26           C  
-ATOM   2594  CE  LYS A 369      94.793  75.016   9.631  1.00 15.33           C  
-ATOM   2595  NZ  LYS A 369      95.142  74.714   8.189  1.00 14.88           N  
-ATOM   2596  N   SER A 370      92.919  71.640  15.725  1.00 16.06           N  
-ATOM   2597  CA  SER A 370      92.124  70.656  16.477  1.00 14.53           C  
-ATOM   2598  C   SER A 370      91.353  71.416  17.548  1.00 14.79           C  
-ATOM   2599  O   SER A 370      90.180  71.159  17.757  1.00 16.63           O  
-ATOM   2600  CB  SER A 370      93.030  69.607  17.138  1.00 16.06           C  
-ATOM   2601  OG  SER A 370      93.736  68.861  16.146  1.00 15.92           O  
-ATOM   2602  N   GLY A 371      92.010  72.358  18.226  1.00 16.68           N  
-ATOM   2603  CA  GLY A 371      91.283  73.140  19.214  1.00 16.71           C  
-ATOM   2604  C   GLY A 371      90.157  73.897  18.493  1.00 18.17           C  
-ATOM   2605  O   GLY A 371      89.044  74.040  19.011  1.00 18.93           O  
-ATOM   2606  N   TYR A 372      90.444  74.361  17.280  1.00 16.25           N  
-ATOM   2607  CA  TYR A 372      89.471  75.107  16.479  1.00 16.02           C  
-ATOM   2608  C   TYR A 372      88.243  74.265  16.211  1.00 15.63           C  
-ATOM   2609  O   TYR A 372      87.113  74.701  16.437  1.00 17.85           O  
-ATOM   2610  CB  TYR A 372      90.112  75.563  15.168  1.00 17.81           C  
-ATOM   2611  CG  TYR A 372      89.227  76.475  14.324  1.00 19.66           C  
-ATOM   2612  CD1 TYR A 372      88.888  77.765  14.760  1.00 19.87           C  
-ATOM   2613  CD2 TYR A 372      88.799  76.075  13.061  1.00 19.98           C  
-ATOM   2614  CE1 TYR A 372      88.145  78.653  13.931  1.00 21.23           C  
-ATOM   2615  CE2 TYR A 372      88.062  76.937  12.222  1.00 20.13           C  
-ATOM   2616  CZ  TYR A 372      87.744  78.220  12.653  1.00 21.82           C  
-ATOM   2617  OH  TYR A 372      87.062  79.065  11.791  1.00 20.78           O  
-ATOM   2618  N   ILE A 373      88.471  73.037  15.770  1.00 15.98           N  
-ATOM   2619  CA  ILE A 373      87.405  72.088  15.502  1.00 15.16           C  
-ATOM   2620  C   ILE A 373      86.561  71.872  16.744  1.00 17.03           C  
-ATOM   2621  O   ILE A 373      85.328  71.896  16.690  1.00 19.85           O  
-ATOM   2622  CB  ILE A 373      87.997  70.742  15.069  1.00 16.65           C  
-ATOM   2623  CG1 ILE A 373      88.529  70.871  13.644  1.00 14.55           C  
-ATOM   2624  CG2 ILE A 373      86.958  69.624  15.220  1.00 14.52           C  
-ATOM   2625  CD1 ILE A 373      89.434  69.690  13.199  1.00 14.68           C  
-ATOM   2626  N   LYS A 374      87.228  71.653  17.873  1.00 16.92           N  
-ATOM   2627  CA  LYS A 374      86.515  71.418  19.125  1.00 17.39           C  
-ATOM   2628  C   LYS A 374      85.767  72.672  19.556  1.00 19.88           C  
-ATOM   2629  O   LYS A 374      84.617  72.603  19.985  1.00 19.51           O  
-ATOM   2630  CB  LYS A 374      87.504  71.006  20.222  1.00 21.74           C  
-ATOM   2631  CG  LYS A 374      88.158  69.652  19.946  1.00 27.83           C  
-ATOM   2632  CD  LYS A 374      89.160  69.246  21.029  1.00 33.95           C  
-ATOM   2633  CE  LYS A 374      88.461  68.791  22.308  1.00 39.54           C  
-ATOM   2634  NZ  LYS A 374      87.782  67.462  22.198  1.00 40.25           N  
-ATOM   2635  N   SER A 375      86.426  73.813  19.419  1.00 18.81           N  
-ATOM   2636  CA  SER A 375      85.846  75.077  19.821  1.00 20.69           C  
-ATOM   2637  C   SER A 375      84.582  75.391  19.041  1.00 21.68           C  
-ATOM   2638  O   SER A 375      83.562  75.753  19.618  1.00 21.91           O  
-ATOM   2639  CB  SER A 375      86.866  76.196  19.640  1.00 20.86           C  
-ATOM   2640  OG  SER A 375      86.318  77.432  20.079  1.00 23.67           O  
-ATOM   2641  N   LEU A 376      84.639  75.253  17.726  1.00 19.80           N  
-ATOM   2642  CA  LEU A 376      83.455  75.522  16.912  1.00 21.24           C  
-ATOM   2643  C   LEU A 376      82.470  74.349  16.806  1.00 20.65           C  
-ATOM   2644  O   LEU A 376      81.401  74.483  16.225  1.00 23.23           O  
-ATOM   2645  CB  LEU A 376      83.883  75.993  15.509  1.00 20.79           C  
-ATOM   2646  CG  LEU A 376      84.114  77.507  15.315  1.00 21.72           C  
-ATOM   2647  CD1 LEU A 376      85.238  78.051  16.202  1.00 22.81           C  
-ATOM   2648  CD2 LEU A 376      84.465  77.746  13.854  1.00 19.95           C  
-ATOM   2649  N   GLY A 377      82.811  73.197  17.367  1.00 19.78           N  
-ATOM   2650  CA  GLY A 377      81.910  72.062  17.267  1.00 17.99           C  
-ATOM   2651  C   GLY A 377      81.795  71.573  15.827  1.00 18.64           C  
-ATOM   2652  O   GLY A 377      80.709  71.175  15.381  1.00 17.45           O  
-ATOM   2653  N   LEU A 378      82.914  71.586  15.094  1.00 17.06           N  
-ATOM   2654  CA  LEU A 378      82.890  71.139  13.699  1.00 16.72           C  
-ATOM   2655  C   LEU A 378      82.716  69.631  13.618  1.00 15.70           C  
-ATOM   2656  O   LEU A 378      82.831  68.930  14.620  1.00 15.47           O  
-ATOM   2657  CB  LEU A 378      84.160  71.598  12.949  1.00 14.03           C  
-ATOM   2658  CG  LEU A 378      84.309  73.132  12.925  1.00 17.57           C  
-ATOM   2659  CD1 LEU A 378      85.575  73.515  12.167  1.00 15.97           C  
-ATOM   2660  CD2 LEU A 378      83.057  73.799  12.280  1.00 16.37           C  
-ATOM   2661  N   GLY A 379      82.455  69.125  12.415  1.00 15.58           N  
-ATOM   2662  CA  GLY A 379      82.200  67.704  12.259  1.00 14.61           C  
-ATOM   2663  C   GLY A 379      83.399  66.775  12.241  1.00 14.41           C  
-ATOM   2664  O   GLY A 379      83.248  65.552  12.134  1.00 14.28           O  
-ATOM   2665  N   GLY A 380      84.592  67.335  12.363  1.00 14.60           N  
-ATOM   2666  CA  GLY A 380      85.759  66.481  12.353  1.00 15.39           C  
-ATOM   2667  C   GLY A 380      86.835  67.041  11.467  1.00 16.34           C  
-ATOM   2668  O   GLY A 380      86.823  68.230  11.170  1.00 16.17           O  
-ATOM   2669  N   ALA A 381      87.752  66.171  11.041  1.00 15.14           N  
-ATOM   2670  CA  ALA A 381      88.873  66.563  10.186  1.00 13.94           C  
-ATOM   2671  C   ALA A 381      88.872  65.756   8.880  1.00 13.18           C  
-ATOM   2672  O   ALA A 381      88.430  64.606   8.858  1.00 11.42           O  
-ATOM   2673  CB  ALA A 381      90.204  66.318  10.940  1.00 12.69           C  
-ATOM   2674  N   MET A 382      89.334  66.375   7.790  1.00 12.88           N  
-ATOM   2675  CA  MET A 382      89.467  65.684   6.501  1.00 12.97           C  
-ATOM   2676  C   MET A 382      90.847  66.053   5.966  1.00 13.94           C  
-ATOM   2677  O   MET A 382      91.351  67.129   6.287  1.00 14.31           O  
-ATOM   2678  CB  MET A 382      88.406  66.151   5.482  1.00 13.80           C  
-ATOM   2679  CG  MET A 382      88.619  65.589   4.062  1.00 12.67           C  
-ATOM   2680  SD  MET A 382      89.720  66.642   3.091  1.00 17.59           S  
-ATOM   2681  CE  MET A 382      88.525  67.908   2.550  1.00 13.63           C  
-ATOM   2682  N   TRP A 383      91.463  65.176   5.170  1.00 12.46           N  
-ATOM   2683  CA  TRP A 383      92.777  65.501   4.603  1.00 14.31           C  
-ATOM   2684  C   TRP A 383      92.947  65.081   3.158  1.00 13.18           C  
-ATOM   2685  O   TRP A 383      92.507  64.000   2.754  1.00 12.74           O  
-ATOM   2686  CB  TRP A 383      93.917  64.782   5.345  1.00 12.45           C  
-ATOM   2687  CG  TRP A 383      94.145  65.227   6.749  1.00 15.27           C  
-ATOM   2688  CD1 TRP A 383      94.920  66.276   7.169  1.00 13.19           C  
-ATOM   2689  CD2 TRP A 383      93.587  64.642   7.921  1.00 12.64           C  
-ATOM   2690  NE1 TRP A 383      94.878  66.380   8.532  1.00 16.90           N  
-ATOM   2691  CE2 TRP A 383      94.060  65.391   9.023  1.00 15.40           C  
-ATOM   2692  CE3 TRP A 383      92.731  63.554   8.152  1.00 14.74           C  
-ATOM   2693  CZ2 TRP A 383      93.704  65.089  10.341  1.00 15.22           C  
-ATOM   2694  CZ3 TRP A 383      92.379  63.250   9.464  1.00 13.78           C  
-ATOM   2695  CH2 TRP A 383      92.864  64.015  10.544  1.00 16.19           C  
-ATOM   2696  N   TRP A 384      93.647  65.929   2.420  1.00 10.80           N  
-ATOM   2697  CA  TRP A 384      94.045  65.629   1.055  1.00 15.09           C  
-ATOM   2698  C   TRP A 384      95.581  65.552   1.192  1.00 13.84           C  
-ATOM   2699  O   TRP A 384      96.199  66.584   1.474  1.00 15.26           O  
-ATOM   2700  CB  TRP A 384      93.730  66.787   0.112  1.00 14.97           C  
-ATOM   2701  CG  TRP A 384      94.199  66.444  -1.282  1.00 19.70           C  
-ATOM   2702  CD1 TRP A 384      95.479  66.534  -1.785  1.00 17.52           C  
-ATOM   2703  CD2 TRP A 384      93.397  65.871  -2.311  1.00 17.48           C  
-ATOM   2704  NE1 TRP A 384      95.507  66.040  -3.082  1.00 16.29           N  
-ATOM   2705  CE2 TRP A 384      94.243  65.626  -3.422  1.00 17.60           C  
-ATOM   2706  CE3 TRP A 384      92.042  65.534  -2.398  1.00 20.75           C  
-ATOM   2707  CZ2 TRP A 384      93.772  65.062  -4.600  1.00 18.18           C  
-ATOM   2708  CZ3 TRP A 384      91.570  64.970  -3.571  1.00 20.57           C  
-ATOM   2709  CH2 TRP A 384      92.437  64.738  -4.662  1.00 22.11           C  
-ATOM   2710  N   ASP A 385      96.217  64.400   0.960  1.00 16.25           N  
-ATOM   2711  CA  ASP A 385      95.580  63.109   0.679  1.00 13.25           C  
-ATOM   2712  C   ASP A 385      96.431  62.138   1.471  1.00 15.33           C  
-ATOM   2713  O   ASP A 385      97.524  62.510   1.917  1.00 14.20           O  
-ATOM   2714  CB  ASP A 385      95.567  62.756  -0.820  1.00 13.23           C  
-ATOM   2715  CG  ASP A 385      96.963  62.502  -1.395  1.00 16.96           C  
-ATOM   2716  OD1 ASP A 385      97.427  61.341  -1.372  1.00 15.86           O  
-ATOM   2717  OD2 ASP A 385      97.592  63.476  -1.863  1.00 19.41           O  
-ATOM   2718  N   SER A 386      95.938  60.910   1.647  1.00 10.73           N  
-ATOM   2719  CA  SER A 386      96.613  59.912   2.465  1.00 14.10           C  
-ATOM   2720  C   SER A 386      98.074  59.592   2.171  1.00 13.30           C  
-ATOM   2721  O   SER A 386      98.807  59.187   3.066  1.00 13.14           O  
-ATOM   2722  CB  SER A 386      95.846  58.585   2.410  1.00 12.07           C  
-ATOM   2723  OG  SER A 386      95.935  58.026   1.098  1.00 13.68           O  
-ATOM   2724  N   SER A 387      98.498  59.769   0.933  1.00 14.56           N  
-ATOM   2725  CA  SER A 387      99.868  59.394   0.568  1.00 15.71           C  
-ATOM   2726  C   SER A 387     101.006  60.274   1.025  1.00 16.89           C  
-ATOM   2727  O   SER A 387     102.162  59.848   0.981  1.00 14.81           O  
-ATOM   2728  CB  SER A 387      99.995  59.326  -0.959  1.00 15.36           C  
-ATOM   2729  OG  SER A 387      99.958  60.649  -1.515  1.00 15.15           O  
-ATOM   2730  N   SER A 388     100.694  61.488   1.452  1.00 17.25           N  
-ATOM   2731  CA  SER A 388     101.756  62.452   1.740  1.00 17.07           C  
-ATOM   2732  C   SER A 388     102.060  62.856   3.186  1.00 17.26           C  
-ATOM   2733  O   SER A 388     102.765  63.849   3.416  1.00 18.18           O  
-ATOM   2734  CB  SER A 388     101.449  63.707   0.916  1.00 14.98           C  
-ATOM   2735  OG  SER A 388     100.233  64.277   1.395  1.00 15.44           O  
-ATOM   2736  N   ASP A 389     101.564  62.089   4.156  1.00 14.78           N  
-ATOM   2737  CA  ASP A 389     101.751  62.431   5.567  1.00 15.00           C  
-ATOM   2738  C   ASP A 389     103.103  61.886   6.005  1.00 16.24           C  
-ATOM   2739  O   ASP A 389     103.690  61.081   5.297  1.00 15.89           O  
-ATOM   2740  CB  ASP A 389     100.652  61.741   6.418  1.00 10.26           C  
-ATOM   2741  CG  ASP A 389     100.439  62.400   7.775  1.00 14.22           C  
-ATOM   2742  OD1 ASP A 389     101.159  63.380   8.123  1.00 15.45           O  
-ATOM   2743  OD2 ASP A 389      99.522  61.955   8.502  1.00 14.13           O  
-ATOM   2744  N   LYS A 390     103.600  62.339   7.148  1.00 14.48           N  
-ATOM   2745  CA  LYS A 390     104.834  61.770   7.686  1.00 16.39           C  
-ATOM   2746  C   LYS A 390     104.325  60.523   8.427  1.00 18.26           C  
-ATOM   2747  O   LYS A 390     103.121  60.348   8.596  1.00 17.11           O  
-ATOM   2748  CB  LYS A 390     105.515  62.734   8.660  1.00 17.49           C  
-ATOM   2749  CG  LYS A 390     106.144  63.965   8.011  1.00 18.71           C  
-ATOM   2750  CD  LYS A 390     106.821  64.793   9.090  1.00 21.22           C  
-ATOM   2751  CE  LYS A 390     107.434  66.069   8.553  1.00 25.91           C  
-ATOM   2752  NZ  LYS A 390     108.485  65.785   7.576  1.00 26.19           N  
-ATOM   2753  N   THR A 391     105.235  59.664   8.868  1.00 18.28           N  
-ATOM   2754  CA  THR A 391     104.881  58.442   9.555  1.00 20.01           C  
-ATOM   2755  C   THR A 391     105.125  58.531  11.050  1.00 21.39           C  
-ATOM   2756  O   THR A 391     105.719  59.490  11.552  1.00 19.17           O  
-ATOM   2757  CB  THR A 391     105.705  57.275   8.978  1.00 24.29           C  
-ATOM   2758  OG1 THR A 391     107.087  57.558   9.163  1.00 24.48           O  
-ATOM   2759  CG2 THR A 391     105.432  57.126   7.476  1.00 21.63           C  
-ATOM   2760  N   GLY A 392     104.649  57.531  11.775  1.00 21.47           N  
-ATOM   2761  CA  GLY A 392     104.838  57.546  13.211  1.00 22.79           C  
-ATOM   2762  C   GLY A 392     104.198  58.734  13.900  1.00 23.15           C  
-ATOM   2763  O   GLY A 392     103.158  59.238  13.466  1.00 23.97           O  
-ATOM   2764  N   SER A 393     104.827  59.203  14.972  1.00 19.20           N  
-ATOM   2765  CA  SER A 393     104.281  60.311  15.730  1.00 19.97           C  
-ATOM   2766  C   SER A 393     104.383  61.656  15.036  1.00 18.14           C  
-ATOM   2767  O   SER A 393     103.915  62.653  15.569  1.00 21.89           O  
-ATOM   2768  CB  SER A 393     104.977  60.383  17.096  1.00 24.05           C  
-ATOM   2769  OG  SER A 393     104.940  59.107  17.689  1.00 29.75           O  
-ATOM   2770  N   ASP A 394     105.003  61.699  13.861  1.00 17.89           N  
-ATOM   2771  CA  ASP A 394     105.105  62.957  13.125  1.00 14.89           C  
-ATOM   2772  C   ASP A 394     103.893  63.102  12.213  1.00 14.28           C  
-ATOM   2773  O   ASP A 394     103.689  64.147  11.615  1.00 16.14           O  
-ATOM   2774  CB  ASP A 394     106.393  62.996  12.294  1.00 14.60           C  
-ATOM   2775  CG  ASP A 394     107.639  63.226  13.161  1.00 18.65           C  
-ATOM   2776  OD1 ASP A 394     107.470  63.589  14.354  1.00 17.66           O  
-ATOM   2777  OD2 ASP A 394     108.757  63.039  12.639  1.00 18.64           O  
-ATOM   2778  N   SER A 395     103.083  62.054  12.119  1.00 14.47           N  
-ATOM   2779  CA  SER A 395     101.883  62.110  11.266  1.00 15.74           C  
-ATOM   2780  C   SER A 395     100.913  63.195  11.717  1.00 14.75           C  
-ATOM   2781  O   SER A 395     100.588  63.310  12.908  1.00 14.81           O  
-ATOM   2782  CB  SER A 395     101.145  60.767  11.280  1.00 16.63           C  
-ATOM   2783  OG  SER A 395      99.774  60.929  10.897  1.00 18.46           O  
-ATOM   2784  N   LEU A 396     100.443  63.996  10.777  1.00 14.26           N  
-ATOM   2785  CA  LEU A 396      99.488  65.038  11.150  1.00 15.05           C  
-ATOM   2786  C   LEU A 396      98.133  64.418  11.452  1.00 14.69           C  
-ATOM   2787  O   LEU A 396      97.430  64.850  12.360  1.00 16.57           O  
-ATOM   2788  CB  LEU A 396      99.363  66.086  10.044  1.00 15.31           C  
-ATOM   2789  CG  LEU A 396     100.619  66.936   9.812  1.00 17.43           C  
-ATOM   2790  CD1 LEU A 396     100.321  67.988   8.750  1.00 18.03           C  
-ATOM   2791  CD2 LEU A 396     101.044  67.611  11.100  1.00 16.58           C  
-ATOM   2792  N   ILE A 397      97.754  63.398  10.699  1.00 15.30           N  
-ATOM   2793  CA  ILE A 397      96.473  62.739  10.971  1.00 15.65           C  
-ATOM   2794  C   ILE A 397      96.495  62.240  12.424  1.00 16.58           C  
-ATOM   2795  O   ILE A 397      95.585  62.521  13.206  1.00 16.14           O  
-ATOM   2796  CB  ILE A 397      96.256  61.558  10.007  1.00 15.04           C  
-ATOM   2797  CG1 ILE A 397      95.986  62.098   8.590  1.00 16.32           C  
-ATOM   2798  CG2 ILE A 397      95.094  60.717  10.457  1.00 14.81           C  
-ATOM   2799  CD1 ILE A 397      95.711  60.996   7.578  1.00 18.16           C  
-ATOM   2800  N   THR A 398      97.553  61.519  12.788  1.00 15.91           N  
-ATOM   2801  CA  THR A 398      97.694  60.989  14.155  1.00 15.37           C  
-ATOM   2802  C   THR A 398      97.668  62.111  15.200  1.00 14.90           C  
-ATOM   2803  O   THR A 398      97.006  61.992  16.230  1.00 17.35           O  
-ATOM   2804  CB  THR A 398      99.007  60.183  14.277  1.00 16.63           C  
-ATOM   2805  OG1 THR A 398      98.961  59.078  13.354  1.00 15.43           O  
-ATOM   2806  CG2 THR A 398      99.203  59.660  15.719  1.00 19.61           C  
-ATOM   2807  N   THR A 399      98.349  63.221  14.916  1.00 15.35           N  
-ATOM   2808  CA  THR A 399      98.369  64.343  15.849  1.00 14.76           C  
-ATOM   2809  C   THR A 399      96.971  64.902  16.054  1.00 15.53           C  
-ATOM   2810  O   THR A 399      96.528  65.128  17.188  1.00 13.49           O  
-ATOM   2811  CB  THR A 399      99.297  65.455  15.321  1.00 18.52           C  
-ATOM   2812  OG1 THR A 399     100.636  64.945  15.285  1.00 19.14           O  
-ATOM   2813  CG2 THR A 399      99.242  66.708  16.212  1.00 13.64           C  
-ATOM   2814  N   VAL A 400      96.257  65.119  14.952  1.00 14.24           N  
-ATOM   2815  CA  VAL A 400      94.896  65.647  15.073  1.00 13.18           C  
-ATOM   2816  C   VAL A 400      93.976  64.681  15.780  1.00 13.15           C  
-ATOM   2817  O   VAL A 400      93.280  65.062  16.737  1.00 15.35           O  
-ATOM   2818  CB  VAL A 400      94.315  65.993  13.682  1.00 13.98           C  
-ATOM   2819  CG1 VAL A 400      92.844  66.437  13.786  1.00 13.90           C  
-ATOM   2820  CG2 VAL A 400      95.162  67.110  13.064  1.00 14.07           C  
-ATOM   2821  N   VAL A 401      93.948  63.430  15.327  1.00 11.75           N  
-ATOM   2822  CA  VAL A 401      93.053  62.464  15.956  1.00 12.26           C  
-ATOM   2823  C   VAL A 401      93.232  62.443  17.468  1.00 14.17           C  
-ATOM   2824  O   VAL A 401      92.256  62.425  18.217  1.00 15.29           O  
-ATOM   2825  CB  VAL A 401      93.250  61.038  15.359  1.00 13.79           C  
-ATOM   2826  CG1 VAL A 401      92.496  60.006  16.193  1.00 17.19           C  
-ATOM   2827  CG2 VAL A 401      92.681  60.987  13.936  1.00 12.86           C  
-ATOM   2828  N   ASN A 402      94.472  62.467  17.930  1.00 14.82           N  
-ATOM   2829  CA  ASN A 402      94.700  62.456  19.375  1.00 17.22           C  
-ATOM   2830  C   ASN A 402      94.404  63.803  20.003  1.00 15.85           C  
-ATOM   2831  O   ASN A 402      93.958  63.864  21.154  1.00 14.76           O  
-ATOM   2832  CB  ASN A 402      96.126  61.999  19.673  1.00 18.33           C  
-ATOM   2833  CG  ASN A 402      96.297  60.523  19.395  1.00 24.91           C  
-ATOM   2834  OD1 ASN A 402      95.496  59.700  19.856  1.00 26.82           O  
-ATOM   2835  ND2 ASN A 402      97.318  60.176  18.638  1.00 29.19           N  
-ATOM   2836  N   ALA A 403      94.612  64.876  19.245  1.00 13.84           N  
-ATOM   2837  CA  ALA A 403      94.323  66.209  19.778  1.00 16.09           C  
-ATOM   2838  C   ALA A 403      92.823  66.362  20.032  1.00 17.34           C  
-ATOM   2839  O   ALA A 403      92.420  67.089  20.942  1.00 16.85           O  
-ATOM   2840  CB  ALA A 403      94.792  67.307  18.795  1.00 16.20           C  
-ATOM   2841  N   LEU A 404      92.001  65.708  19.209  1.00 16.67           N  
-ATOM   2842  CA  LEU A 404      90.555  65.788  19.376  1.00 16.75           C  
-ATOM   2843  C   LEU A 404      90.073  64.911  20.517  1.00 16.83           C  
-ATOM   2844  O   LEU A 404      88.918  65.021  20.924  1.00 18.15           O  
-ATOM   2845  CB  LEU A 404      89.832  65.360  18.106  1.00 13.89           C  
-ATOM   2846  CG  LEU A 404      90.095  66.244  16.878  1.00 16.52           C  
-ATOM   2847  CD1 LEU A 404      89.500  65.590  15.628  1.00 16.63           C  
-ATOM   2848  CD2 LEU A 404      89.516  67.616  17.126  1.00 17.80           C  
-ATOM   2849  N   GLY A 405      90.937  64.034  21.024  1.00 18.35           N  
-ATOM   2850  CA  GLY A 405      90.524  63.173  22.121  1.00 19.26           C  
-ATOM   2851  C   GLY A 405      90.749  61.686  21.869  1.00 20.88           C  
-ATOM   2852  O   GLY A 405      90.426  60.851  22.716  1.00 20.90           O  
-ATOM   2853  N   GLY A 406      91.290  61.335  20.708  1.00 19.11           N  
-ATOM   2854  CA  GLY A 406      91.547  59.926  20.454  1.00 19.22           C  
-ATOM   2855  C   GLY A 406      90.446  59.276  19.658  1.00 20.90           C  
-ATOM   2856  O   GLY A 406      89.368  59.837  19.513  1.00 20.73           O  
-ATOM   2857  N   THR A 407      90.690  58.077  19.157  1.00 22.59           N  
-ATOM   2858  CA  THR A 407      89.675  57.416  18.342  1.00 24.65           C  
-ATOM   2859  C   THR A 407      88.380  57.215  19.121  1.00 24.88           C  
-ATOM   2860  O   THR A 407      87.316  57.061  18.536  1.00 26.33           O  
-ATOM   2861  CB  THR A 407      90.182  56.075  17.827  1.00 26.64           C  
-ATOM   2862  OG1 THR A 407      90.466  55.222  18.938  1.00 27.16           O  
-ATOM   2863  CG2 THR A 407      91.459  56.287  16.986  1.00 23.72           C  
-ATOM   2864  N   GLY A 408      88.465  57.251  20.444  1.00 25.40           N  
-ATOM   2865  CA  GLY A 408      87.267  57.093  21.251  1.00 25.36           C  
-ATOM   2866  C   GLY A 408      86.212  58.187  21.086  1.00 25.35           C  
-ATOM   2867  O   GLY A 408      85.045  57.958  21.391  1.00 25.60           O  
-ATOM   2868  N   VAL A 409      86.596  59.381  20.636  1.00 24.98           N  
-ATOM   2869  CA  VAL A 409      85.624  60.465  20.456  1.00 22.46           C  
-ATOM   2870  C   VAL A 409      85.059  60.490  19.012  1.00 23.01           C  
-ATOM   2871  O   VAL A 409      84.276  61.377  18.632  1.00 20.42           O  
-ATOM   2872  CB  VAL A 409      86.257  61.850  20.790  1.00 24.81           C  
-ATOM   2873  CG1 VAL A 409      86.790  61.842  22.233  1.00 25.24           C  
-ATOM   2874  CG2 VAL A 409      87.378  62.171  19.826  1.00 24.04           C  
-ATOM   2875  N   PHE A 410      85.467  59.513  18.213  1.00 20.51           N  
-ATOM   2876  CA  PHE A 410      84.996  59.408  16.827  1.00 21.40           C  
-ATOM   2877  C   PHE A 410      83.525  59.018  16.737  1.00 20.01           C  
-ATOM   2878  O   PHE A 410      83.025  58.219  17.540  1.00 18.95           O  
-ATOM   2879  CB  PHE A 410      85.730  58.287  16.087  1.00 22.09           C  
-ATOM   2880  CG  PHE A 410      87.118  58.621  15.653  1.00 26.89           C  
-ATOM   2881  CD1 PHE A 410      87.659  59.879  15.899  1.00 24.95           C  
-ATOM   2882  CD2 PHE A 410      87.877  57.672  14.940  1.00 25.01           C  
-ATOM   2883  CE1 PHE A 410      88.937  60.207  15.443  1.00 30.18           C  
-ATOM   2884  CE2 PHE A 410      89.178  57.995  14.474  1.00 27.25           C  
-ATOM   2885  CZ  PHE A 410      89.695  59.263  14.729  1.00 25.09           C  
-ATOM   2886  N   GLU A 411      82.856  59.529  15.719  1.00 20.49           N  
-ATOM   2887  CA  GLU A 411      81.482  59.148  15.447  1.00 19.98           C  
-ATOM   2888  C   GLU A 411      81.569  57.639  15.206  1.00 20.88           C  
-ATOM   2889  O   GLU A 411      82.523  57.176  14.568  1.00 18.17           O  
-ATOM   2890  CB  GLU A 411      81.029  59.838  14.158  1.00 23.29           C  
-ATOM   2891  CG  GLU A 411      79.706  59.350  13.645  1.00 28.07           C  
-ATOM   2892  CD  GLU A 411      79.454  59.818  12.224  1.00 30.62           C  
-ATOM   2893  OE1 GLU A 411      78.628  60.736  12.036  1.00 29.19           O  
-ATOM   2894  OE2 GLU A 411      80.106  59.264  11.310  1.00 32.75           O  
-ATOM   2895  N   GLN A 412      80.611  56.873  15.735  1.00 21.03           N  
-ATOM   2896  CA  GLN A 412      80.586  55.416  15.567  1.00 21.64           C  
-ATOM   2897  C   GLN A 412      79.381  55.085  14.700  1.00 25.34           C  
-ATOM   2898  O   GLN A 412      78.256  55.475  15.026  1.00 23.91           O  
-ATOM   2899  CB  GLN A 412      80.422  54.693  16.907  1.00 26.07           C  
-ATOM   2900  CG  GLN A 412      81.554  54.912  17.906  1.00 26.10           C  
-ATOM   2901  CD  GLN A 412      82.869  54.403  17.383  1.00 26.75           C  
-ATOM   2902  OE1 GLN A 412      83.002  53.221  17.078  1.00 28.17           O  
-ATOM   2903  NE2 GLN A 412      83.853  55.292  17.267  1.00 27.64           N  
-ATOM   2904  N   SER A 413      79.623  54.361  13.608  1.00 23.99           N  
-ATOM   2905  CA  SER A 413      78.583  53.963  12.664  1.00 22.91           C  
-ATOM   2906  C   SER A 413      79.169  52.776  11.904  1.00 24.12           C  
-ATOM   2907  O   SER A 413      80.164  52.926  11.178  1.00 21.03           O  
-ATOM   2908  CB  SER A 413      78.294  55.122  11.716  1.00 23.17           C  
-ATOM   2909  OG  SER A 413      77.413  54.712  10.706  1.00 33.59           O  
-ATOM   2910  N   GLN A 414      78.571  51.600  12.072  1.00 20.79           N  
-ATOM   2911  CA  GLN A 414      79.097  50.395  11.438  1.00 21.36           C  
-ATOM   2912  C   GLN A 414      79.001  50.431   9.916  1.00 22.01           C  
-ATOM   2913  O   GLN A 414      78.025  50.948   9.360  1.00 18.38           O  
-ATOM   2914  CB  GLN A 414      78.379  49.152  11.992  1.00 25.23           C  
-ATOM   2915  CG  GLN A 414      78.897  47.826  11.469  1.00 28.62           C  
-ATOM   2916  CD  GLN A 414      78.595  46.659  12.423  1.00 36.74           C  
-ATOM   2917  OE1 GLN A 414      79.222  46.527  13.476  1.00 35.53           O  
-ATOM   2918  NE2 GLN A 414      77.628  45.815  12.051  1.00 37.21           N  
-ATOM   2919  N   ASN A 415      80.036  49.908   9.255  1.00 19.61           N  
-ATOM   2920  CA  ASN A 415      80.069  49.873   7.806  1.00 19.67           C  
-ATOM   2921  C   ASN A 415      79.299  48.666   7.284  1.00 19.16           C  
-ATOM   2922  O   ASN A 415      78.805  47.854   8.071  1.00 18.74           O  
-ATOM   2923  CB  ASN A 415      81.518  49.849   7.279  1.00 16.93           C  
-ATOM   2924  CG  ASN A 415      82.311  48.626   7.712  1.00 19.73           C  
-ATOM   2925  OD1 ASN A 415      81.756  47.577   8.103  1.00 18.74           O  
-ATOM   2926  ND2 ASN A 415      83.642  48.737   7.610  1.00 14.45           N  
-ATOM   2927  N   GLU A 416      79.205  48.570   5.960  1.00 19.29           N  
-ATOM   2928  CA  GLU A 416      78.511  47.465   5.278  1.00 19.32           C  
-ATOM   2929  C   GLU A 416      79.522  46.470   4.692  1.00 19.42           C  
-ATOM   2930  O   GLU A 416      80.447  46.851   3.996  1.00 20.07           O  
-ATOM   2931  CB  GLU A 416      77.649  48.002   4.130  1.00 20.31           C  
-ATOM   2932  CG  GLU A 416      76.910  46.883   3.394  1.00 20.64           C  
-ATOM   2933  CD  GLU A 416      75.947  46.154   4.334  1.00 22.51           C  
-ATOM   2934  OE1 GLU A 416      74.966  46.789   4.760  1.00 24.66           O  
-ATOM   2935  OE2 GLU A 416      76.184  44.976   4.661  1.00 22.38           O  
-ATOM   2936  N   LEU A 417      79.358  45.195   4.989  1.00 18.06           N  
-ATOM   2937  CA  LEU A 417      80.244  44.195   4.441  1.00 18.77           C  
-ATOM   2938  C   LEU A 417      79.487  43.289   3.466  1.00 20.75           C  
-ATOM   2939  O   LEU A 417      80.100  42.508   2.750  1.00 21.62           O  
-ATOM   2940  CB  LEU A 417      80.826  43.335   5.557  1.00 18.06           C  
-ATOM   2941  CG  LEU A 417      81.793  44.119   6.451  1.00 19.02           C  
-ATOM   2942  CD1 LEU A 417      82.287  43.216   7.569  1.00 17.99           C  
-ATOM   2943  CD2 LEU A 417      82.942  44.642   5.593  1.00 13.30           C  
-ATOM   2944  N   ASP A 418      78.160  43.393   3.464  1.00 21.78           N  
-ATOM   2945  CA  ASP A 418      77.315  42.535   2.623  1.00 25.08           C  
-ATOM   2946  C   ASP A 418      76.908  43.203   1.319  1.00 22.04           C  
-ATOM   2947  O   ASP A 418      76.227  44.223   1.325  1.00 20.50           O  
-ATOM   2948  CB AASP A 418      76.066  42.124   3.403  0.50 27.33           C  
-ATOM   2949  CG AASP A 418      76.401  41.404   4.690  0.50 29.20           C  
-ATOM   2950  OD1AASP A 418      77.076  40.360   4.631  0.50 29.43           O  
-ATOM   2951  OD2AASP A 418      75.990  41.887   5.766  0.50 32.54           O  
-ATOM   2952  CB BASP A 418      76.046  42.138   3.398  0.50 28.45           C  
-ATOM   2953  CG BASP A 418      75.396  40.866   2.862  0.50 31.83           C  
-ATOM   2954  OD1BASP A 418      75.696  40.468   1.718  0.50 32.49           O  
-ATOM   2955  OD2BASP A 418      74.573  40.261   3.585  0.50 36.28           O  
-ATOM   2956  N   TYR A 419      77.333  42.621   0.204  1.00 21.25           N  
-ATOM   2957  CA  TYR A 419      76.993  43.146  -1.115  1.00 20.92           C  
-ATOM   2958  C   TYR A 419      76.493  41.921  -1.895  1.00 23.50           C  
-ATOM   2959  O   TYR A 419      77.211  41.341  -2.714  1.00 20.59           O  
-ATOM   2960  CB  TYR A 419      78.234  43.787  -1.742  1.00 20.45           C  
-ATOM   2961  CG  TYR A 419      78.635  45.036  -0.972  1.00 19.63           C  
-ATOM   2962  CD1 TYR A 419      79.412  44.960   0.200  1.00 17.26           C  
-ATOM   2963  CD2 TYR A 419      78.134  46.278  -1.348  1.00 19.51           C  
-ATOM   2964  CE1 TYR A 419      79.668  46.133   0.986  1.00 18.27           C  
-ATOM   2965  CE2 TYR A 419      78.370  47.427  -0.585  1.00 19.60           C  
-ATOM   2966  CZ  TYR A 419      79.137  47.345   0.583  1.00 18.23           C  
-ATOM   2967  OH  TYR A 419      79.318  48.508   1.306  1.00 19.90           O  
-ATOM   2968  N   PRO A 420      75.236  41.510  -1.617  1.00 23.29           N  
-ATOM   2969  CA  PRO A 420      74.567  40.358  -2.222  1.00 23.77           C  
-ATOM   2970  C   PRO A 420      74.337  40.385  -3.728  1.00 22.33           C  
-ATOM   2971  O   PRO A 420      74.109  39.337  -4.331  1.00 22.19           O  
-ATOM   2972  CB  PRO A 420      73.273  40.251  -1.404  1.00 23.07           C  
-ATOM   2973  CG  PRO A 420      72.926  41.687  -1.193  1.00 25.19           C  
-ATOM   2974  CD  PRO A 420      74.294  42.262  -0.763  1.00 23.86           C  
-ATOM   2975  N   VAL A 421      74.382  41.557  -4.344  1.00 21.33           N  
-ATOM   2976  CA  VAL A 421      74.231  41.587  -5.789  1.00 23.55           C  
-ATOM   2977  C   VAL A 421      75.476  42.110  -6.498  1.00 24.69           C  
-ATOM   2978  O   VAL A 421      75.415  42.608  -7.617  1.00 25.09           O  
-ATOM   2979  CB  VAL A 421      72.985  42.358  -6.241  1.00 22.77           C  
-ATOM   2980  CG1 VAL A 421      71.748  41.500  -5.931  1.00 22.06           C  
-ATOM   2981  CG2 VAL A 421      72.899  43.712  -5.578  1.00 24.12           C  
-ATOM   2982  N   SER A 422      76.619  41.942  -5.841  1.00 24.32           N  
-ATOM   2983  CA  SER A 422      77.894  42.341  -6.420  1.00 23.24           C  
-ATOM   2984  C   SER A 422      78.229  41.352  -7.535  1.00 22.54           C  
-ATOM   2985  O   SER A 422      78.085  40.145  -7.342  1.00 21.62           O  
-ATOM   2986  CB  SER A 422      79.004  42.283  -5.364  1.00 21.57           C  
-ATOM   2987  OG  SER A 422      80.262  42.445  -5.979  1.00 22.27           O  
-ATOM   2988  N   GLN A 423      78.690  41.857  -8.684  1.00 22.03           N  
-ATOM   2989  CA  GLN A 423      79.058  40.992  -9.815  1.00 20.46           C  
-ATOM   2990  C   GLN A 423      80.311  40.215  -9.496  1.00 22.10           C  
-ATOM   2991  O   GLN A 423      80.626  39.224 -10.168  1.00 23.23           O  
-ATOM   2992  CB  GLN A 423      79.330  41.821 -11.076  1.00 20.58           C  
-ATOM   2993  CG  GLN A 423      80.537  42.758 -10.945  1.00 20.39           C  
-ATOM   2994  CD  GLN A 423      80.946  43.400 -12.271  1.00 18.42           C  
-ATOM   2995  OE1 GLN A 423      81.666  42.803 -13.057  1.00 21.56           O  
-ATOM   2996  NE2 GLN A 423      80.476  44.610 -12.512  1.00 16.61           N  
-ATOM   2997  N   TYR A 424      81.043  40.657  -8.473  1.00 20.55           N  
-ATOM   2998  CA  TYR A 424      82.298  39.992  -8.129  1.00 20.53           C  
-ATOM   2999  C   TYR A 424      82.136  38.832  -7.141  1.00 22.47           C  
-ATOM   3000  O   TYR A 424      81.791  39.017  -5.967  1.00 23.93           O  
-ATOM   3001  CB  TYR A 424      83.305  41.040  -7.603  1.00 20.13           C  
-ATOM   3002  CG  TYR A 424      83.587  42.130  -8.635  1.00 19.48           C  
-ATOM   3003  CD1 TYR A 424      84.231  41.829  -9.836  1.00 18.93           C  
-ATOM   3004  CD2 TYR A 424      83.164  43.439  -8.432  1.00 18.37           C  
-ATOM   3005  CE1 TYR A 424      84.444  42.812 -10.822  1.00 17.60           C  
-ATOM   3006  CE2 TYR A 424      83.371  44.438  -9.412  1.00 19.36           C  
-ATOM   3007  CZ  TYR A 424      84.015  44.101 -10.606  1.00 19.17           C  
-ATOM   3008  OH  TYR A 424      84.228  45.054 -11.585  1.00 18.70           O  
-ATOM   3009  N   ASP A 425      82.420  37.634  -7.625  1.00 21.78           N  
-ATOM   3010  CA  ASP A 425      82.280  36.441  -6.808  1.00 23.61           C  
-ATOM   3011  C   ASP A 425      83.094  36.427  -5.519  1.00 25.28           C  
-ATOM   3012  O   ASP A 425      82.598  35.978  -4.477  1.00 22.82           O  
-ATOM   3013  CB  ASP A 425      82.616  35.230  -7.652  1.00 23.06           C  
-ATOM   3014  CG  ASP A 425      81.735  35.150  -8.877  1.00 22.87           C  
-ATOM   3015  OD1 ASP A 425      80.513  35.365  -8.726  1.00 22.03           O  
-ATOM   3016  OD2 ASP A 425      82.249  34.912  -9.985  1.00 23.79           O  
-ATOM   3017  N   ASN A 426      84.331  36.913  -5.564  1.00 22.37           N  
-ATOM   3018  CA  ASN A 426      85.109  36.878  -4.334  1.00 23.42           C  
-ATOM   3019  C   ASN A 426      84.559  37.825  -3.285  1.00 21.99           C  
-ATOM   3020  O   ASN A 426      84.418  37.438  -2.138  1.00 24.41           O  
-ATOM   3021  CB  ASN A 426      86.626  37.110  -4.584  1.00 21.46           C  
-ATOM   3022  CG  ASN A 426      86.965  38.454  -5.256  1.00 23.09           C  
-ATOM   3023  OD1 ASN A 426      86.121  39.137  -5.846  1.00 19.92           O  
-ATOM   3024  ND2 ASN A 426      88.243  38.815  -5.173  1.00 18.99           N  
-ATOM   3025  N   LEU A 427      84.208  39.040  -3.689  1.00 21.05           N  
-ATOM   3026  CA  LEU A 427      83.690  40.023  -2.755  1.00 23.42           C  
-ATOM   3027  C   LEU A 427      82.284  39.704  -2.261  1.00 23.12           C  
-ATOM   3028  O   LEU A 427      81.947  39.994  -1.108  1.00 22.27           O  
-ATOM   3029  CB  LEU A 427      83.711  41.426  -3.383  1.00 22.53           C  
-ATOM   3030  CG  LEU A 427      83.407  42.639  -2.492  1.00 23.75           C  
-ATOM   3031  CD1 LEU A 427      84.026  43.904  -3.111  1.00 22.62           C  
-ATOM   3032  CD2 LEU A 427      81.923  42.862  -2.327  1.00 23.02           C  
-ATOM   3033  N   ARG A 428      81.454  39.138  -3.139  1.00 23.35           N  
-ATOM   3034  CA  ARG A 428      80.087  38.792  -2.763  1.00 22.53           C  
-ATOM   3035  C   ARG A 428      80.132  37.682  -1.702  1.00 21.74           C  
-ATOM   3036  O   ARG A 428      79.232  37.573  -0.871  1.00 23.52           O  
-ATOM   3037  CB  ARG A 428      79.276  38.339  -3.998  1.00 23.93           C  
-ATOM   3038  CG  ARG A 428      77.755  38.239  -3.748  1.00 24.21           C  
-ATOM   3039  CD  ARG A 428      76.982  37.787  -5.009  1.00 22.40           C  
-ATOM   3040  NE  ARG A 428      77.465  36.474  -5.405  1.00 20.50           N  
-ATOM   3041  CZ  ARG A 428      78.321  36.280  -6.395  1.00 20.00           C  
-ATOM   3042  NH1 ARG A 428      78.761  37.323  -7.096  1.00 20.13           N  
-ATOM   3043  NH2 ARG A 428      78.765  35.060  -6.648  1.00 21.25           N  
-ATOM   3044  N   ASN A 429      81.190  36.880  -1.720  1.00 22.62           N  
-ATOM   3045  CA  ASN A 429      81.339  35.818  -0.737  1.00 22.74           C  
-ATOM   3046  C   ASN A 429      82.201  36.238   0.451  1.00 24.04           C  
-ATOM   3047  O   ASN A 429      82.781  35.396   1.130  1.00 23.60           O  
-ATOM   3048  CB  ASN A 429      81.888  34.569  -1.394  1.00 25.74           C  
-ATOM   3049  CG  ASN A 429      80.848  33.893  -2.280  1.00 32.86           C  
-ATOM   3050  OD1 ASN A 429      81.063  33.761  -3.516  1.00 33.05           O  
-ATOM   3051  ND2 ASN A 429      79.751  33.486  -1.709  1.00 27.88           N  
-ATOM   3052  N   GLY A 430      82.269  37.550   0.670  1.00 22.02           N  
-ATOM   3053  CA  GLY A 430      83.021  38.072   1.817  1.00 23.86           C  
-ATOM   3054  C   GLY A 430      84.537  38.144   1.717  1.00 23.81           C  
-ATOM   3055  O   GLY A 430      85.199  38.324   2.722  1.00 20.64           O  
-ATOM   3056  N   MET A 431      85.073  37.969   0.514  1.00 25.17           N  
-ATOM   3057  CA  MET A 431      86.518  38.057   0.297  1.00 24.38           C  
-ATOM   3058  C   MET A 431      87.309  37.151   1.228  1.00 26.88           C  
-ATOM   3059  O   MET A 431      88.121  37.629   2.035  1.00 24.55           O  
-ATOM   3060  CB  MET A 431      86.977  39.513   0.491  1.00 24.98           C  
-ATOM   3061  CG  MET A 431      88.213  39.877  -0.309  1.00 24.50           C  
-ATOM   3062  SD  MET A 431      88.018  39.731  -2.084  1.00 22.58           S  
-ATOM   3063  CE  MET A 431      87.181  41.214  -2.447  1.00 19.97           C  
-ATOM   3064  N   GLN A 432      87.081  35.843   1.114  1.00 26.01           N  
-ATOM   3065  CA  GLN A 432      87.785  34.890   1.965  1.00 29.48           C  
-ATOM   3066  C   GLN A 432      89.251  34.896   1.558  1.00 32.70           C  
-ATOM   3067  O   GLN A 432      89.579  34.800   0.367  1.00 30.18           O  
-ATOM   3068  CB  GLN A 432      87.174  33.489   1.809  1.00 27.66           C  
-ATOM   3069  CG  GLN A 432      85.682  33.446   2.159  1.00 26.54           C  
-ATOM   3070  CD  GLN A 432      85.384  34.030   3.538  1.00 29.48           C  
-ATOM   3071  OE1 GLN A 432      86.017  33.653   4.532  1.00 28.23           O  
-ATOM   3072  NE2 GLN A 432      84.417  34.949   3.606  1.00 26.37           N  
-ATOM   3073  N   THR A 433      90.146  35.023   2.530  1.00 35.72           N  
-ATOM   3074  CA  THR A 433      91.575  35.079   2.188  1.00 42.93           C  
-ATOM   3075  C   THR A 433      92.462  34.623   3.331  1.00 44.61           C  
-ATOM   3076  O   THR A 433      93.389  33.827   3.059  1.00 46.51           O  
-ATOM   3077  CB  THR A 433      92.047  36.534   1.771  1.00 45.37           C  
-ATOM   3078  OG1 THR A 433      91.277  37.517   2.475  1.00 45.15           O  
-ATOM   3079  CG2 THR A 433      91.940  36.762   0.230  1.00 47.15           C  
-ATOM   3080  OXT THR A 433      92.231  35.088   4.468  1.00 45.94           O  
-TER    3081      THR A 433                                                      
-ATOM   3082  N   ALA B  39      85.362   8.124  28.908  1.00 52.37           N  
-ATOM   3083  CA  ALA B  39      84.835   7.261  27.812  1.00 52.87           C  
-ATOM   3084  C   ALA B  39      84.298   5.927  28.359  1.00 52.65           C  
-ATOM   3085  O   ALA B  39      84.682   5.484  29.447  1.00 53.15           O  
-ATOM   3086  CB  ALA B  39      85.933   7.012  26.761  1.00 52.72           C  
-ATOM   3087  N   SER B  40      83.403   5.296  27.602  1.00 49.69           N  
-ATOM   3088  CA  SER B  40      82.803   4.027  28.003  1.00 47.01           C  
-ATOM   3089  C   SER B  40      82.105   3.379  26.809  1.00 44.81           C  
-ATOM   3090  O   SER B  40      81.552   4.078  25.958  1.00 43.20           O  
-ATOM   3091  CB  SER B  40      81.789   4.249  29.132  1.00 46.92           C  
-ATOM   3092  OG  SER B  40      80.675   5.011  28.691  1.00 48.46           O  
-ATOM   3093  N   SER B  41      82.127   2.046  26.751  1.00 41.77           N  
-ATOM   3094  CA  SER B  41      81.498   1.317  25.650  1.00 39.42           C  
-ATOM   3095  C   SER B  41      79.973   1.428  25.685  1.00 36.98           C  
-ATOM   3096  O   SER B  41      79.380   1.800  26.704  1.00 36.36           O  
-ATOM   3097  CB  SER B  41      81.891  -0.162  25.700  1.00 40.35           C  
-ATOM   3098  OG  SER B  41      81.226  -0.810  26.775  1.00 39.26           O  
-ATOM   3099  N   GLY B  42      79.335   1.093  24.571  1.00 33.62           N  
-ATOM   3100  CA  GLY B  42      77.886   1.164  24.518  1.00 29.46           C  
-ATOM   3101  C   GLY B  42      77.393   1.148  23.083  1.00 26.82           C  
-ATOM   3102  O   GLY B  42      78.172   0.940  22.155  1.00 25.49           O  
-ATOM   3103  N   TYR B  43      76.100   1.361  22.891  1.00 23.93           N  
-ATOM   3104  CA  TYR B  43      75.572   1.347  21.538  1.00 23.02           C  
-ATOM   3105  C   TYR B  43      75.875   2.654  20.805  1.00 21.57           C  
-ATOM   3106  O   TYR B  43      75.946   3.729  21.411  1.00 19.80           O  
-ATOM   3107  CB  TYR B  43      74.058   1.097  21.551  1.00 21.92           C  
-ATOM   3108  CG  TYR B  43      73.654  -0.246  22.112  1.00 23.35           C  
-ATOM   3109  CD1 TYR B  43      74.034  -1.424  21.480  1.00 23.53           C  
-ATOM   3110  CD2 TYR B  43      72.882  -0.334  23.279  1.00 23.62           C  
-ATOM   3111  CE1 TYR B  43      73.656  -2.672  21.986  1.00 23.41           C  
-ATOM   3112  CE2 TYR B  43      72.504  -1.566  23.800  1.00 25.21           C  
-ATOM   3113  CZ  TYR B  43      72.898  -2.729  23.139  1.00 23.38           C  
-ATOM   3114  OH  TYR B  43      72.530  -3.947  23.634  1.00 24.97           O  
-ATOM   3115  N   ARG B  44      76.093   2.546  19.503  1.00 20.22           N  
-ATOM   3116  CA  ARG B  44      76.322   3.727  18.679  1.00 19.42           C  
-ATOM   3117  C   ARG B  44      74.996   4.048  17.988  1.00 20.18           C  
-ATOM   3118  O   ARG B  44      74.192   3.143  17.742  1.00 20.74           O  
-ATOM   3119  CB  ARG B  44      77.385   3.446  17.620  1.00 20.52           C  
-ATOM   3120  CG  ARG B  44      78.720   3.007  18.200  1.00 21.23           C  
-ATOM   3121  CD  ARG B  44      79.647   2.497  17.109  1.00 24.24           C  
-ATOM   3122  NE  ARG B  44      80.915   1.940  17.605  1.00 25.01           N  
-ATOM   3123  CZ  ARG B  44      81.086   0.708  18.100  1.00 28.46           C  
-ATOM   3124  NH1 ARG B  44      80.071  -0.157  18.206  1.00 27.03           N  
-ATOM   3125  NH2 ARG B  44      82.305   0.305  18.444  1.00 26.06           N  
-ATOM   3126  N   SER B  45      74.765   5.332  17.696  1.00 18.78           N  
-ATOM   3127  CA  SER B  45      73.559   5.796  17.012  1.00 18.34           C  
-ATOM   3128  C   SER B  45      74.152   6.682  15.914  1.00 19.71           C  
-ATOM   3129  O   SER B  45      74.618   7.804  16.161  1.00 20.78           O  
-ATOM   3130  CB  SER B  45      72.682   6.596  17.958  1.00 17.58           C  
-ATOM   3131  OG  SER B  45      71.526   7.038  17.262  1.00 20.57           O  
-ATOM   3132  N   VAL B  46      74.144   6.130  14.710  1.00 19.87           N  
-ATOM   3133  CA  VAL B  46      74.773   6.710  13.541  1.00 20.16           C  
-ATOM   3134  C   VAL B  46      73.778   7.091  12.452  1.00 19.30           C  
-ATOM   3135  O   VAL B  46      72.875   6.310  12.146  1.00 16.69           O  
-ATOM   3136  CB  VAL B  46      75.759   5.659  12.953  1.00 20.21           C  
-ATOM   3137  CG1 VAL B  46      76.572   6.252  11.805  1.00 16.80           C  
-ATOM   3138  CG2 VAL B  46      76.664   5.088  14.095  1.00 17.21           C  
-ATOM   3139  N   VAL B  47      73.939   8.273  11.862  1.00 17.06           N  
-ATOM   3140  CA  VAL B  47      73.010   8.647  10.796  1.00 16.56           C  
-ATOM   3141  C   VAL B  47      73.780   9.342   9.686  1.00 18.31           C  
-ATOM   3142  O   VAL B  47      74.732  10.083   9.950  1.00 18.73           O  
-ATOM   3143  CB  VAL B  47      71.891   9.575  11.316  1.00 15.83           C  
-ATOM   3144  CG1 VAL B  47      72.438  10.988  11.592  1.00 15.95           C  
-ATOM   3145  CG2 VAL B  47      70.743   9.637  10.293  1.00 16.50           C  
-ATOM   3146  N   TYR B  48      73.400   9.070   8.443  1.00 14.99           N  
-ATOM   3147  CA  TYR B  48      74.035   9.749   7.338  1.00 14.86           C  
-ATOM   3148  C   TYR B  48      73.347  11.091   7.177  1.00 17.34           C  
-ATOM   3149  O   TYR B  48      72.115  11.189   7.299  1.00 18.00           O  
-ATOM   3150  CB  TYR B  48      73.845   8.994   6.016  1.00 14.86           C  
-ATOM   3151  CG  TYR B  48      74.842   7.913   5.797  1.00 16.57           C  
-ATOM   3152  CD1 TYR B  48      74.604   6.615   6.241  1.00 18.55           C  
-ATOM   3153  CD2 TYR B  48      76.045   8.188   5.144  1.00 17.65           C  
-ATOM   3154  CE1 TYR B  48      75.547   5.605   6.033  1.00 20.46           C  
-ATOM   3155  CE2 TYR B  48      76.980   7.201   4.938  1.00 21.15           C  
-ATOM   3156  CZ  TYR B  48      76.731   5.915   5.380  1.00 21.89           C  
-ATOM   3157  OH  TYR B  48      77.686   4.955   5.150  1.00 24.79           O  
-ATOM   3158  N   PHE B  49      74.139  12.131   6.954  1.00 15.80           N  
-ATOM   3159  CA  PHE B  49      73.581  13.433   6.645  1.00 14.57           C  
-ATOM   3160  C   PHE B  49      74.140  13.652   5.248  1.00 15.00           C  
-ATOM   3161  O   PHE B  49      75.369  13.676   5.080  1.00 16.26           O  
-ATOM   3162  CB  PHE B  49      74.097  14.550   7.537  1.00 20.26           C  
-ATOM   3163  CG  PHE B  49      73.581  15.886   7.111  1.00 16.59           C  
-ATOM   3164  CD1 PHE B  49      74.229  16.608   6.105  1.00 18.89           C  
-ATOM   3165  CD2 PHE B  49      72.371  16.352   7.595  1.00 16.44           C  
-ATOM   3166  CE1 PHE B  49      73.662  17.777   5.589  1.00 19.77           C  
-ATOM   3167  CE2 PHE B  49      71.798  17.516   7.092  1.00 19.36           C  
-ATOM   3168  CZ  PHE B  49      72.442  18.231   6.086  1.00 19.37           C  
-ATOM   3169  N   VAL B  50      73.268  13.774   4.246  1.00 15.99           N  
-ATOM   3170  CA  VAL B  50      73.729  13.918   2.855  1.00 15.27           C  
-ATOM   3171  C   VAL B  50      73.770  15.377   2.446  1.00 14.95           C  
-ATOM   3172  O   VAL B  50      72.809  16.108   2.663  1.00 18.33           O  
-ATOM   3173  CB  VAL B  50      72.842  13.074   1.885  1.00 14.92           C  
-ATOM   3174  CG1 VAL B  50      72.838  11.624   2.358  1.00 14.18           C  
-ATOM   3175  CG2 VAL B  50      71.404  13.594   1.845  1.00 14.32           C  
-ATOM   3176  N   ASN B  51      74.864  15.797   1.819  1.00 15.51           N  
-ATOM   3177  CA  ASN B  51      74.968  17.207   1.524  1.00 18.30           C  
-ATOM   3178  C   ASN B  51      73.931  17.774   0.578  1.00 18.37           C  
-ATOM   3179  O   ASN B  51      73.663  18.976   0.629  1.00 18.26           O  
-ATOM   3180  CB  ASN B  51      76.415  17.614   1.149  1.00 21.09           C  
-ATOM   3181  CG  ASN B  51      76.886  17.095  -0.193  1.00 24.54           C  
-ATOM   3182  OD1 ASN B  51      76.127  16.568  -0.997  1.00 24.73           O  
-ATOM   3183  ND2 ASN B  51      78.178  17.286  -0.453  1.00 25.50           N  
-ATOM   3184  N   TRP B  52      73.310  16.922  -0.239  1.00 13.98           N  
-ATOM   3185  CA  TRP B  52      72.250  17.391  -1.142  1.00 14.56           C  
-ATOM   3186  C   TRP B  52      70.898  17.526  -0.394  1.00 14.02           C  
-ATOM   3187  O   TRP B  52      69.895  17.912  -0.974  1.00 16.65           O  
-ATOM   3188  CB  TRP B  52      72.123  16.445  -2.361  1.00 15.52           C  
-ATOM   3189  CG  TRP B  52      71.839  15.019  -2.022  1.00 17.22           C  
-ATOM   3190  CD1 TRP B  52      70.606  14.428  -1.919  1.00 20.02           C  
-ATOM   3191  CD2 TRP B  52      72.804  13.992  -1.756  1.00 17.14           C  
-ATOM   3192  NE1 TRP B  52      70.748  13.085  -1.609  1.00 18.22           N  
-ATOM   3193  CE2 TRP B  52      72.086  12.797  -1.506  1.00 18.35           C  
-ATOM   3194  CE3 TRP B  52      74.214  13.966  -1.704  1.00 18.15           C  
-ATOM   3195  CZ2 TRP B  52      72.723  11.584  -1.211  1.00 17.42           C  
-ATOM   3196  CZ3 TRP B  52      74.852  12.759  -1.409  1.00 20.02           C  
-ATOM   3197  CH2 TRP B  52      74.095  11.576  -1.167  1.00 18.91           C  
-ATOM   3198  N   ALA B  53      70.880  17.229   0.903  1.00 15.13           N  
-ATOM   3199  CA  ALA B  53      69.637  17.369   1.675  1.00 15.18           C  
-ATOM   3200  C   ALA B  53      69.244  18.844   1.837  1.00 16.61           C  
-ATOM   3201  O   ALA B  53      68.086  19.161   2.138  1.00 16.52           O  
-ATOM   3202  CB  ALA B  53      69.801  16.747   3.063  1.00 13.18           C  
-ATOM   3203  N   ILE B  54      70.215  19.741   1.659  1.00 16.79           N  
-ATOM   3204  CA  ILE B  54      69.918  21.150   1.838  1.00 18.95           C  
-ATOM   3205  C   ILE B  54      69.110  21.709   0.681  1.00 20.92           C  
-ATOM   3206  O   ILE B  54      68.667  22.865   0.739  1.00 20.67           O  
-ATOM   3207  CB  ILE B  54      71.184  21.995   1.972  1.00 20.58           C  
-ATOM   3208  CG1 ILE B  54      72.041  21.841   0.714  1.00 22.71           C  
-ATOM   3209  CG2 ILE B  54      71.941  21.596   3.222  1.00 20.76           C  
-ATOM   3210  CD1 ILE B  54      72.526  23.159   0.164  1.00 27.00           C  
-ATOM   3211  N   TYR B  55      68.912  20.899  -0.362  1.00 17.61           N  
-ATOM   3212  CA  TYR B  55      68.150  21.368  -1.520  1.00 17.07           C  
-ATOM   3213  C   TYR B  55      66.663  21.054  -1.366  1.00 15.30           C  
-ATOM   3214  O   TYR B  55      66.028  21.553  -0.441  1.00 16.91           O  
-ATOM   3215  CB  TYR B  55      68.736  20.767  -2.810  1.00 14.59           C  
-ATOM   3216  CG  TYR B  55      70.149  21.257  -3.087  1.00 16.80           C  
-ATOM   3217  CD1 TYR B  55      70.405  22.608  -3.340  1.00 18.16           C  
-ATOM   3218  CD2 TYR B  55      71.227  20.386  -3.058  1.00 17.10           C  
-ATOM   3219  CE1 TYR B  55      71.700  23.067  -3.551  1.00 17.62           C  
-ATOM   3220  CE2 TYR B  55      72.535  20.844  -3.271  1.00 18.16           C  
-ATOM   3221  CZ  TYR B  55      72.759  22.178  -3.515  1.00 17.98           C  
-ATOM   3222  OH  TYR B  55      74.045  22.633  -3.730  1.00 19.38           O  
-ATOM   3223  N   GLY B  56      66.109  20.208  -2.226  1.00 14.92           N  
-ATOM   3224  CA  GLY B  56      64.681  19.926  -2.143  1.00 16.21           C  
-ATOM   3225  C   GLY B  56      64.188  19.408  -0.805  1.00 17.78           C  
-ATOM   3226  O   GLY B  56      63.085  19.730  -0.355  1.00 18.92           O  
-ATOM   3227  N   ARG B  57      65.007  18.589  -0.170  1.00 19.06           N  
-ATOM   3228  CA  ARG B  57      64.649  18.004   1.122  1.00 16.82           C  
-ATOM   3229  C   ARG B  57      64.625  19.075   2.194  1.00 16.35           C  
-ATOM   3230  O   ARG B  57      64.097  18.848   3.275  1.00 17.61           O  
-ATOM   3231  CB  ARG B  57      65.660  16.909   1.483  1.00 16.33           C  
-ATOM   3232  CG  ARG B  57      65.659  15.728   0.507  1.00 15.55           C  
-ATOM   3233  CD  ARG B  57      66.854  14.809   0.795  1.00 18.25           C  
-ATOM   3234  NE  ARG B  57      66.831  13.526   0.086  1.00 16.22           N  
-ATOM   3235  CZ  ARG B  57      66.970  13.360  -1.232  1.00 20.55           C  
-ATOM   3236  NH1 ARG B  57      67.135  14.397  -2.044  1.00 18.86           N  
-ATOM   3237  NH2 ARG B  57      66.970  12.133  -1.744  1.00 19.34           N  
-ATOM   3238  N   ASN B  58      65.215  20.237   1.905  1.00 16.21           N  
-ATOM   3239  CA  ASN B  58      65.222  21.354   2.855  1.00 16.78           C  
-ATOM   3240  C   ASN B  58      65.553  20.879   4.265  1.00 18.54           C  
-ATOM   3241  O   ASN B  58      64.834  21.167   5.222  1.00 18.97           O  
-ATOM   3242  CB  ASN B  58      63.844  22.037   2.850  1.00 19.98           C  
-ATOM   3243  CG  ASN B  58      63.821  23.333   3.659  1.00 23.51           C  
-ATOM   3244  OD1 ASN B  58      64.792  24.082   3.666  1.00 28.18           O  
-ATOM   3245  ND2 ASN B  58      62.706  23.600   4.334  1.00 25.37           N  
-ATOM   3246  N   HIS B  59      66.667  20.170   4.385  1.00 18.04           N  
-ATOM   3247  CA  HIS B  59      67.089  19.564   5.650  1.00 18.38           C  
-ATOM   3248  C   HIS B  59      68.526  19.986   5.909  1.00 17.42           C  
-ATOM   3249  O   HIS B  59      69.397  19.695   5.098  1.00 15.73           O  
-ATOM   3250  CB  HIS B  59      66.995  18.044   5.480  1.00 18.73           C  
-ATOM   3251  CG  HIS B  59      67.490  17.261   6.656  1.00 20.39           C  
-ATOM   3252  ND1 HIS B  59      66.810  17.205   7.856  1.00 17.05           N  
-ATOM   3253  CD2 HIS B  59      68.576  16.459   6.796  1.00 17.87           C  
-ATOM   3254  CE1 HIS B  59      67.453  16.392   8.678  1.00 20.78           C  
-ATOM   3255  NE2 HIS B  59      68.525  15.925   8.060  1.00 16.75           N  
-ATOM   3256  N   ASN B  60      68.754  20.649   7.043  1.00 16.92           N  
-ATOM   3257  CA  ASN B  60      70.080  21.158   7.393  1.00 19.62           C  
-ATOM   3258  C   ASN B  60      70.643  20.465   8.631  1.00 18.47           C  
-ATOM   3259  O   ASN B  60      69.892  19.952   9.447  1.00 18.97           O  
-ATOM   3260  CB  ASN B  60      69.978  22.681   7.656  1.00 21.92           C  
-ATOM   3261  CG  ASN B  60      69.225  23.403   6.528  1.00 25.47           C  
-ATOM   3262  OD1 ASN B  60      69.728  23.442   5.383  1.00 22.66           O  
-ATOM   3263  ND2 ASN B  60      68.082  23.964   6.818  1.00 26.13           N  
-ATOM   3264  N   PRO B  61      71.975  20.481   8.814  1.00 19.37           N  
-ATOM   3265  CA  PRO B  61      72.567  19.819   9.988  1.00 20.34           C  
-ATOM   3266  C   PRO B  61      71.907  20.239  11.286  1.00 22.27           C  
-ATOM   3267  O   PRO B  61      71.754  19.417  12.178  1.00 23.32           O  
-ATOM   3268  CB  PRO B  61      74.031  20.217   9.906  1.00 18.70           C  
-ATOM   3269  CG  PRO B  61      74.249  20.380   8.394  1.00 18.20           C  
-ATOM   3270  CD  PRO B  61      73.018  21.174   8.032  1.00 19.12           C  
-ATOM   3271  N   GLN B  62      71.534  21.515  11.383  1.00 22.02           N  
-ATOM   3272  CA  GLN B  62      70.855  22.060  12.560  1.00 24.64           C  
-ATOM   3273  C   GLN B  62      69.600  21.272  12.879  1.00 23.66           C  
-ATOM   3274  O   GLN B  62      69.116  21.337  13.998  1.00 22.79           O  
-ATOM   3275  CB  GLN B  62      70.395  23.512  12.333  1.00 27.84           C  
-ATOM   3276  CG  GLN B  62      71.464  24.514  11.988  1.00 32.35           C  
-ATOM   3277  CD  GLN B  62      71.717  24.604  10.500  1.00 32.09           C  
-ATOM   3278  OE1 GLN B  62      72.101  23.626   9.873  1.00 31.07           O  
-ATOM   3279  NE2 GLN B  62      71.509  25.791   9.926  1.00 34.64           N  
-ATOM   3280  N   ASP B  63      69.043  20.564  11.892  1.00 22.75           N  
-ATOM   3281  CA  ASP B  63      67.818  19.788  12.115  1.00 21.84           C  
-ATOM   3282  C   ASP B  63      68.074  18.397  12.704  1.00 22.07           C  
-ATOM   3283  O   ASP B  63      67.133  17.689  13.057  1.00 21.53           O  
-ATOM   3284  CB  ASP B  63      67.047  19.603  10.799  1.00 24.34           C  
-ATOM   3285  CG  ASP B  63      66.656  20.925  10.152  1.00 25.93           C  
-ATOM   3286  OD1 ASP B  63      66.264  21.843  10.894  1.00 27.27           O  
-ATOM   3287  OD2 ASP B  63      66.736  21.035   8.917  1.00 23.40           O  
-ATOM   3288  N   LEU B  64      69.335  17.995  12.776  1.00 19.84           N  
-ATOM   3289  CA  LEU B  64      69.672  16.671  13.291  1.00 19.89           C  
-ATOM   3290  C   LEU B  64      69.316  16.476  14.769  1.00 21.50           C  
-ATOM   3291  O   LEU B  64      69.446  17.400  15.574  1.00 19.07           O  
-ATOM   3292  CB  LEU B  64      71.158  16.417  13.114  1.00 19.60           C  
-ATOM   3293  CG  LEU B  64      71.603  16.208  11.670  1.00 20.81           C  
-ATOM   3294  CD1 LEU B  64      73.125  16.271  11.596  1.00 19.86           C  
-ATOM   3295  CD2 LEU B  64      71.103  14.855  11.189  1.00 20.63           C  
-ATOM   3296  N   PRO B  65      68.851  15.270  15.143  1.00 21.94           N  
-ATOM   3297  CA  PRO B  65      68.491  14.988  16.546  1.00 22.83           C  
-ATOM   3298  C   PRO B  65      69.783  14.686  17.287  1.00 25.06           C  
-ATOM   3299  O   PRO B  65      70.030  13.546  17.694  1.00 23.37           O  
-ATOM   3300  CB  PRO B  65      67.611  13.759  16.433  1.00 22.33           C  
-ATOM   3301  CG  PRO B  65      68.228  13.012  15.271  1.00 21.82           C  
-ATOM   3302  CD  PRO B  65      68.498  14.139  14.264  1.00 23.52           C  
-ATOM   3303  N   VAL B  66      70.602  15.720  17.469  1.00 26.38           N  
-ATOM   3304  CA  VAL B  66      71.903  15.535  18.089  1.00 26.18           C  
-ATOM   3305  C   VAL B  66      71.946  14.807  19.419  1.00 27.66           C  
-ATOM   3306  O   VAL B  66      72.898  14.077  19.678  1.00 25.81           O  
-ATOM   3307  CB  VAL B  66      72.657  16.873  18.249  1.00 28.15           C  
-ATOM   3308  CG1 VAL B  66      73.075  17.394  16.877  1.00 33.25           C  
-ATOM   3309  CG2 VAL B  66      71.795  17.873  18.956  1.00 30.39           C  
-ATOM   3310  N   GLU B  67      70.933  14.986  20.254  1.00 26.30           N  
-ATOM   3311  CA  GLU B  67      70.945  14.336  21.561  1.00 30.29           C  
-ATOM   3312  C   GLU B  67      70.740  12.832  21.459  1.00 29.60           C  
-ATOM   3313  O   GLU B  67      71.046  12.083  22.395  1.00 31.18           O  
-ATOM   3314  CB  GLU B  67      69.849  14.931  22.437  1.00 36.21           C  
-ATOM   3315  CG  GLU B  67      70.044  16.425  22.734  1.00 47.93           C  
-ATOM   3316  CD  GLU B  67      68.813  17.073  23.384  1.00 53.61           C  
-ATOM   3317  OE1 GLU B  67      67.783  17.280  22.689  1.00 56.84           O  
-ATOM   3318  OE2 GLU B  67      68.877  17.368  24.601  1.00 58.06           O  
-ATOM   3319  N   ARG B  68      70.239  12.393  20.313  1.00 26.68           N  
-ATOM   3320  CA  ARG B  68      69.945  10.982  20.106  1.00 24.28           C  
-ATOM   3321  C   ARG B  68      70.893  10.276  19.165  1.00 22.54           C  
-ATOM   3322  O   ARG B  68      70.580   9.186  18.659  1.00 22.68           O  
-ATOM   3323  CB  ARG B  68      68.505  10.845  19.613  1.00 26.25           C  
-ATOM   3324  CG  ARG B  68      67.481  11.306  20.649  1.00 26.09           C  
-ATOM   3325  CD  ARG B  68      66.071  10.978  20.203  1.00 30.12           C  
-ATOM   3326  NE  ARG B  68      65.588  11.820  19.113  1.00 32.08           N  
-ATOM   3327  CZ  ARG B  68      64.928  12.960  19.292  1.00 33.10           C  
-ATOM   3328  NH1 ARG B  68      64.687  13.390  20.521  1.00 34.35           N  
-ATOM   3329  NH2 ARG B  68      64.464  13.641  18.249  1.00 27.55           N  
-ATOM   3330  N   LEU B  69      72.056  10.889  18.949  1.00 18.49           N  
-ATOM   3331  CA  LEU B  69      73.065  10.339  18.060  1.00 18.52           C  
-ATOM   3332  C   LEU B  69      74.452  10.331  18.690  1.00 19.83           C  
-ATOM   3333  O   LEU B  69      74.742  11.125  19.582  1.00 19.34           O  
-ATOM   3334  CB  LEU B  69      73.149  11.181  16.773  1.00 18.96           C  
-ATOM   3335  CG  LEU B  69      71.898  11.304  15.882  1.00 20.13           C  
-ATOM   3336  CD1 LEU B  69      71.993  12.546  15.014  1.00 19.74           C  
-ATOM   3337  CD2 LEU B  69      71.787  10.079  14.993  1.00 19.86           C  
-ATOM   3338  N   THR B  70      75.308   9.431  18.210  1.00 19.40           N  
-ATOM   3339  CA  THR B  70      76.697   9.403  18.648  1.00 18.61           C  
-ATOM   3340  C   THR B  70      77.567   9.777  17.448  1.00 20.31           C  
-ATOM   3341  O   THR B  70      78.621  10.382  17.608  1.00 22.43           O  
-ATOM   3342  CB  THR B  70      77.142   7.999  19.158  1.00 20.26           C  
-ATOM   3343  OG1 THR B  70      76.893   7.009  18.146  1.00 20.22           O  
-ATOM   3344  CG2 THR B  70      76.405   7.633  20.436  1.00 15.77           C  
-ATOM   3345  N   HIS B  71      77.114   9.452  16.236  1.00 20.72           N  
-ATOM   3346  CA  HIS B  71      77.907   9.742  15.041  1.00 19.37           C  
-ATOM   3347  C   HIS B  71      77.075  10.244  13.871  1.00 21.93           C  
-ATOM   3348  O   HIS B  71      75.975   9.744  13.626  1.00 21.29           O  
-ATOM   3349  CB  HIS B  71      78.628   8.494  14.518  1.00 19.34           C  
-ATOM   3350  CG  HIS B  71      79.536   7.838  15.509  1.00 24.14           C  
-ATOM   3351  ND1 HIS B  71      79.072   7.174  16.625  1.00 25.57           N  
-ATOM   3352  CD2 HIS B  71      80.886   7.725  15.539  1.00 24.06           C  
-ATOM   3353  CE1 HIS B  71      80.096   6.679  17.298  1.00 26.39           C  
-ATOM   3354  NE2 HIS B  71      81.209   7.000  16.661  1.00 24.78           N  
-ATOM   3355  N   VAL B  72      77.633  11.195  13.125  1.00 20.46           N  
-ATOM   3356  CA  VAL B  72      76.974  11.711  11.931  1.00 20.20           C  
-ATOM   3357  C   VAL B  72      77.938  11.443  10.788  1.00 21.55           C  
-ATOM   3358  O   VAL B  72      79.118  11.758  10.895  1.00 23.69           O  
-ATOM   3359  CB  VAL B  72      76.690  13.220  12.028  1.00 23.34           C  
-ATOM   3360  CG1 VAL B  72      76.275  13.779  10.651  1.00 20.48           C  
-ATOM   3361  CG2 VAL B  72      75.566  13.460  13.011  1.00 20.36           C  
-ATOM   3362  N   LEU B  73      77.461  10.811   9.714  1.00 20.94           N  
-ATOM   3363  CA  LEU B  73      78.327  10.542   8.562  1.00 18.55           C  
-ATOM   3364  C   LEU B  73      77.952  11.557   7.488  1.00 20.46           C  
-ATOM   3365  O   LEU B  73      76.805  11.560   7.003  1.00 18.18           O  
-ATOM   3366  CB  LEU B  73      78.099   9.118   8.043  1.00 19.79           C  
-ATOM   3367  CG  LEU B  73      78.233   8.019   9.108  1.00 20.55           C  
-ATOM   3368  CD1 LEU B  73      77.930   6.636   8.483  1.00 19.72           C  
-ATOM   3369  CD2 LEU B  73      79.643   8.047   9.697  1.00 21.29           C  
-ATOM   3370  N   TYR B  74      78.910  12.407   7.104  1.00 18.11           N  
-ATOM   3371  CA  TYR B  74      78.657  13.462   6.115  1.00 18.31           C  
-ATOM   3372  C   TYR B  74      78.981  12.952   4.719  1.00 18.69           C  
-ATOM   3373  O   TYR B  74      80.144  12.714   4.396  1.00 17.72           O  
-ATOM   3374  CB  TYR B  74      79.496  14.713   6.435  1.00 19.18           C  
-ATOM   3375  CG  TYR B  74      79.147  15.917   5.572  1.00 20.97           C  
-ATOM   3376  CD1 TYR B  74      77.916  16.546   5.684  1.00 19.24           C  
-ATOM   3377  CD2 TYR B  74      80.056  16.415   4.634  1.00 22.06           C  
-ATOM   3378  CE1 TYR B  74      77.594  17.645   4.884  1.00 21.16           C  
-ATOM   3379  CE2 TYR B  74      79.749  17.500   3.839  1.00 20.97           C  
-ATOM   3380  CZ  TYR B  74      78.519  18.113   3.966  1.00 22.05           C  
-ATOM   3381  OH  TYR B  74      78.238  19.197   3.165  1.00 19.43           O  
-ATOM   3382  N   ALA B  75      77.936  12.770   3.909  1.00 17.06           N  
-ATOM   3383  CA  ALA B  75      78.052  12.227   2.562  1.00 16.47           C  
-ATOM   3384  C   ALA B  75      77.933  13.300   1.477  1.00 15.46           C  
-ATOM   3385  O   ALA B  75      77.029  14.118   1.533  1.00 17.39           O  
-ATOM   3386  CB  ALA B  75      76.960  11.169   2.364  1.00 15.11           C  
-ATOM   3387  N   PHE B  76      78.825  13.304   0.491  1.00 16.08           N  
-ATOM   3388  CA  PHE B  76      79.945  12.359   0.339  1.00 15.94           C  
-ATOM   3389  C   PHE B  76      81.123  13.173  -0.216  1.00 20.46           C  
-ATOM   3390  O   PHE B  76      80.907  14.225  -0.824  1.00 20.09           O  
-ATOM   3391  CB  PHE B  76      79.658  11.325  -0.768  1.00 17.23           C  
-ATOM   3392  CG  PHE B  76      78.850  10.123  -0.331  1.00 16.90           C  
-ATOM   3393  CD1 PHE B  76      79.284   9.318   0.725  1.00 16.74           C  
-ATOM   3394  CD2 PHE B  76      77.670   9.783  -0.995  1.00 16.03           C  
-ATOM   3395  CE1 PHE B  76      78.544   8.180   1.118  1.00 17.62           C  
-ATOM   3396  CE2 PHE B  76      76.922   8.649  -0.614  1.00 17.26           C  
-ATOM   3397  CZ  PHE B  76      77.360   7.849   0.447  1.00 14.35           C  
-ATOM   3398  N   ALA B  77      82.349  12.676  -0.008  1.00 20.87           N  
-ATOM   3399  CA  ALA B  77      83.542  13.276  -0.633  1.00 22.38           C  
-ATOM   3400  C   ALA B  77      83.782  12.275  -1.770  1.00 21.51           C  
-ATOM   3401  O   ALA B  77      83.406  11.101  -1.648  1.00 21.89           O  
-ATOM   3402  CB  ALA B  77      84.759  13.279   0.324  1.00 22.48           C  
-ATOM   3403  N   ASN B  78      84.373  12.720  -2.874  1.00 18.92           N  
-ATOM   3404  CA  ASN B  78      84.646  11.830  -3.997  1.00 21.48           C  
-ATOM   3405  C   ASN B  78      86.138  11.480  -3.961  1.00 24.47           C  
-ATOM   3406  O   ASN B  78      86.888  12.059  -3.176  1.00 24.12           O  
-ATOM   3407  CB  ASN B  78      84.293  12.537  -5.316  1.00 21.85           C  
-ATOM   3408  CG  ASN B  78      84.355  11.616  -6.522  1.00 21.08           C  
-ATOM   3409  OD1 ASN B  78      84.458  10.402  -6.388  1.00 20.95           O  
-ATOM   3410  ND2 ASN B  78      84.261  12.198  -7.717  1.00 23.15           N  
-ATOM   3411  N   VAL B  79      86.546  10.505  -4.771  1.00 24.43           N  
-ATOM   3412  CA  VAL B  79      87.942  10.105  -4.849  1.00 26.69           C  
-ATOM   3413  C   VAL B  79      88.347  10.024  -6.322  1.00 27.99           C  
-ATOM   3414  O   VAL B  79      87.695   9.343  -7.116  1.00 26.77           O  
-ATOM   3415  CB  VAL B  79      88.211   8.743  -4.161  1.00 28.11           C  
-ATOM   3416  CG1 VAL B  79      87.362   7.609  -4.792  1.00 27.30           C  
-ATOM   3417  CG2 VAL B  79      89.684   8.418  -4.267  1.00 28.57           C  
-ATOM   3418  N   ARG B  80      89.393  10.760  -6.688  1.00 26.84           N  
-ATOM   3419  CA  ARG B  80      89.890  10.765  -8.067  1.00 28.54           C  
-ATOM   3420  C   ARG B  80      90.540   9.442  -8.396  1.00 28.32           C  
-ATOM   3421  O   ARG B  80      91.515   9.042  -7.758  1.00 28.76           O  
-ATOM   3422  CB  ARG B  80      90.906  11.883  -8.275  1.00 30.08           C  
-ATOM   3423  CG  ARG B  80      90.313  13.132  -8.867  1.00 34.18           C  
-ATOM   3424  CD  ARG B  80      91.345  14.222  -9.021  1.00 33.26           C  
-ATOM   3425  NE  ARG B  80      90.926  15.415  -8.302  1.00 34.12           N  
-ATOM   3426  CZ  ARG B  80      89.885  16.166  -8.650  1.00 33.82           C  
-ATOM   3427  NH1 ARG B  80      89.154  15.854  -9.723  1.00 33.54           N  
-ATOM   3428  NH2 ARG B  80      89.570  17.215  -7.909  1.00 32.33           N  
-ATOM   3429  N   PRO B  81      90.025   8.746  -9.412  1.00 28.81           N  
-ATOM   3430  CA  PRO B  81      90.575   7.445  -9.806  1.00 31.16           C  
-ATOM   3431  C   PRO B  81      92.043   7.422 -10.232  1.00 33.67           C  
-ATOM   3432  O   PRO B  81      92.752   6.454  -9.967  1.00 34.38           O  
-ATOM   3433  CB  PRO B  81      89.652   7.004 -10.936  1.00 30.16           C  
-ATOM   3434  CG  PRO B  81      89.161   8.305 -11.511  1.00 30.41           C  
-ATOM   3435  CD  PRO B  81      88.925   9.152 -10.299  1.00 29.44           C  
-ATOM   3436  N   GLU B  82      92.491   8.491 -10.880  1.00 35.10           N  
-ATOM   3437  CA  GLU B  82      93.855   8.555 -11.372  1.00 37.65           C  
-ATOM   3438  C   GLU B  82      94.886   8.952 -10.330  1.00 36.55           C  
-ATOM   3439  O   GLU B  82      96.052   8.586 -10.451  1.00 37.52           O  
-ATOM   3440  CB  GLU B  82      93.938   9.489 -12.591  1.00 38.74           C  
-ATOM   3441  CG  GLU B  82      93.271  10.841 -12.412  1.00 44.78           C  
-ATOM   3442  CD  GLU B  82      91.738  10.775 -12.438  1.00 46.86           C  
-ATOM   3443  OE1 GLU B  82      91.148  10.488 -13.507  1.00 49.77           O  
-ATOM   3444  OE2 GLU B  82      91.127  11.012 -11.381  1.00 47.75           O  
-ATOM   3445  N   THR B  83      94.466   9.665  -9.294  1.00 35.32           N  
-ATOM   3446  CA  THR B  83      95.408  10.089  -8.271  1.00 33.73           C  
-ATOM   3447  C   THR B  83      95.096   9.616  -6.855  1.00 33.59           C  
-ATOM   3448  O   THR B  83      95.978   9.601  -5.996  1.00 31.21           O  
-ATOM   3449  CB  THR B  83      95.518  11.611  -8.234  1.00 34.50           C  
-ATOM   3450  OG1 THR B  83      94.283  12.164  -7.766  1.00 35.23           O  
-ATOM   3451  CG2 THR B  83      95.824  12.147  -9.628  1.00 33.99           C  
-ATOM   3452  N   GLY B  84      93.849   9.242  -6.590  1.00 31.70           N  
-ATOM   3453  CA  GLY B  84      93.525   8.819  -5.241  1.00 27.91           C  
-ATOM   3454  C   GLY B  84      93.178  10.010  -4.373  1.00 25.48           C  
-ATOM   3455  O   GLY B  84      92.909   9.865  -3.184  1.00 26.98           O  
-ATOM   3456  N   GLU B  85      93.180  11.206  -4.950  1.00 25.65           N  
-ATOM   3457  CA  GLU B  85      92.833  12.390  -4.166  1.00 25.13           C  
-ATOM   3458  C   GLU B  85      91.372  12.365  -3.702  1.00 26.60           C  
-ATOM   3459  O   GLU B  85      90.474  12.141  -4.511  1.00 25.13           O  
-ATOM   3460  CB  GLU B  85      93.029  13.672  -4.983  1.00 26.36           C  
-ATOM   3461  CG  GLU B  85      92.472  14.907  -4.270  1.00 28.57           C  
-ATOM   3462  CD  GLU B  85      92.476  16.154  -5.136  1.00 32.19           C  
-ATOM   3463  OE1 GLU B  85      92.615  16.030  -6.372  1.00 33.97           O  
-ATOM   3464  OE2 GLU B  85      92.322  17.260  -4.581  1.00 33.22           O  
-ATOM   3465  N   VAL B  86      91.141  12.629  -2.417  1.00 27.55           N  
-ATOM   3466  CA  VAL B  86      89.784  12.678  -1.869  1.00 27.77           C  
-ATOM   3467  C   VAL B  86      89.412  14.156  -1.817  1.00 27.72           C  
-ATOM   3468  O   VAL B  86      90.224  14.982  -1.377  1.00 25.82           O  
-ATOM   3469  CB  VAL B  86      89.741  12.061  -0.462  1.00 27.43           C  
-ATOM   3470  CG1 VAL B  86      88.380  12.306   0.198  1.00 25.62           C  
-ATOM   3471  CG2 VAL B  86      90.034  10.565  -0.567  1.00 25.64           C  
-ATOM   3472  N   TYR B  87      88.207  14.508  -2.284  1.00 24.41           N  
-ATOM   3473  CA  TYR B  87      87.807  15.919  -2.278  1.00 23.05           C  
-ATOM   3474  C   TYR B  87      86.314  16.149  -2.068  1.00 24.83           C  
-ATOM   3475  O   TYR B  87      85.483  15.292  -2.432  1.00 20.82           O  
-ATOM   3476  CB  TYR B  87      88.239  16.590  -3.585  1.00 21.75           C  
-ATOM   3477  CG  TYR B  87      87.607  16.017  -4.835  1.00 22.54           C  
-ATOM   3478  CD1 TYR B  87      88.033  14.793  -5.357  1.00 19.90           C  
-ATOM   3479  CD2 TYR B  87      86.602  16.710  -5.512  1.00 23.13           C  
-ATOM   3480  CE1 TYR B  87      87.486  14.282  -6.519  1.00 21.57           C  
-ATOM   3481  CE2 TYR B  87      86.040  16.194  -6.686  1.00 21.23           C  
-ATOM   3482  CZ  TYR B  87      86.492  14.982  -7.178  1.00 19.26           C  
-ATOM   3483  OH  TYR B  87      85.960  14.440  -8.331  1.00 21.04           O  
-ATOM   3484  N   MET B  88      85.982  17.300  -1.481  1.00 24.74           N  
-ATOM   3485  CA  MET B  88      84.582  17.663  -1.222  1.00 23.55           C  
-ATOM   3486  C   MET B  88      83.885  17.887  -2.554  1.00 24.43           C  
-ATOM   3487  O   MET B  88      84.508  18.276  -3.544  1.00 22.17           O  
-ATOM   3488  CB  MET B  88      84.502  18.897  -0.331  1.00 23.92           C  
-ATOM   3489  CG  MET B  88      85.291  18.716   0.981  1.00 21.40           C  
-ATOM   3490  SD  MET B  88      84.747  17.235   1.897  1.00 19.47           S  
-ATOM   3491  CE  MET B  88      83.336  17.975   2.690  1.00 18.66           C  
-ATOM   3492  N   THR B  89      82.577  17.684  -2.566  1.00 22.62           N  
-ATOM   3493  CA  THR B  89      81.842  17.720  -3.813  1.00 21.42           C  
-ATOM   3494  C   THR B  89      80.804  18.794  -4.084  1.00 21.20           C  
-ATOM   3495  O   THR B  89      80.236  18.814  -5.170  1.00 22.82           O  
-ATOM   3496  CB  THR B  89      81.160  16.370  -3.966  1.00 20.42           C  
-ATOM   3497  OG1 THR B  89      80.315  16.170  -2.821  1.00 20.43           O  
-ATOM   3498  CG2 THR B  89      82.192  15.242  -3.984  1.00 19.23           C  
-ATOM   3499  N   ASP B  90      80.523  19.673  -3.133  1.00 20.78           N  
-ATOM   3500  CA  ASP B  90      79.515  20.709  -3.388  1.00 22.52           C  
-ATOM   3501  C   ASP B  90      79.913  21.909  -2.555  1.00 23.54           C  
-ATOM   3502  O   ASP B  90      79.525  22.021  -1.385  1.00 23.50           O  
-ATOM   3503  CB  ASP B  90      78.126  20.210  -2.982  1.00 20.13           C  
-ATOM   3504  CG  ASP B  90      77.001  21.202  -3.327  1.00 23.49           C  
-ATOM   3505  OD1 ASP B  90      77.263  22.411  -3.448  1.00 19.00           O  
-ATOM   3506  OD2 ASP B  90      75.837  20.755  -3.454  1.00 24.14           O  
-ATOM   3507  N   SER B  91      80.680  22.812  -3.167  1.00 23.50           N  
-ATOM   3508  CA  SER B  91      81.174  23.976  -2.442  1.00 23.81           C  
-ATOM   3509  C   SER B  91      80.057  24.756  -1.793  1.00 24.05           C  
-ATOM   3510  O   SER B  91      80.221  25.245  -0.676  1.00 24.84           O  
-ATOM   3511  CB  SER B  91      82.007  24.899  -3.359  1.00 26.76           C  
-ATOM   3512  OG  SER B  91      81.193  25.603  -4.274  1.00 28.52           O  
-ATOM   3513  N   TRP B  92      78.916  24.867  -2.472  1.00 21.15           N  
-ATOM   3514  CA  TRP B  92      77.795  25.611  -1.913  1.00 22.93           C  
-ATOM   3515  C   TRP B  92      77.307  24.940  -0.638  1.00 24.89           C  
-ATOM   3516  O   TRP B  92      77.296  25.550   0.434  1.00 22.64           O  
-ATOM   3517  CB  TRP B  92      76.652  25.703  -2.938  1.00 23.28           C  
-ATOM   3518  CG  TRP B  92      75.361  26.291  -2.412  1.00 25.79           C  
-ATOM   3519  CD1 TRP B  92      74.169  25.633  -2.223  1.00 26.86           C  
-ATOM   3520  CD2 TRP B  92      75.131  27.643  -2.022  1.00 27.12           C  
-ATOM   3521  NE1 TRP B  92      73.216  26.500  -1.743  1.00 26.97           N  
-ATOM   3522  CE2 TRP B  92      73.781  27.738  -1.608  1.00 25.85           C  
-ATOM   3523  CE3 TRP B  92      75.936  28.788  -1.978  1.00 26.96           C  
-ATOM   3524  CZ2 TRP B  92      73.218  28.929  -1.161  1.00 28.35           C  
-ATOM   3525  CZ3 TRP B  92      75.379  29.974  -1.535  1.00 31.47           C  
-ATOM   3526  CH2 TRP B  92      74.029  30.039  -1.133  1.00 32.17           C  
-ATOM   3527  N   ALA B  93      76.916  23.674  -0.752  1.00 21.82           N  
-ATOM   3528  CA  ALA B  93      76.419  22.964   0.416  1.00 22.16           C  
-ATOM   3529  C   ALA B  93      77.503  22.756   1.470  1.00 20.16           C  
-ATOM   3530  O   ALA B  93      77.262  22.958   2.652  1.00 22.33           O  
-ATOM   3531  CB  ALA B  93      75.832  21.605   0.007  1.00 17.85           C  
-ATOM   3532  N   ASP B  94      78.682  22.334   1.038  1.00 20.11           N  
-ATOM   3533  CA  ASP B  94      79.749  22.064   1.978  1.00 21.37           C  
-ATOM   3534  C   ASP B  94      80.225  23.256   2.787  1.00 24.26           C  
-ATOM   3535  O   ASP B  94      80.170  23.239   4.017  1.00 24.09           O  
-ATOM   3536  CB  ASP B  94      80.972  21.471   1.273  1.00 19.87           C  
-ATOM   3537  CG  ASP B  94      80.703  20.114   0.665  1.00 20.11           C  
-ATOM   3538  OD1 ASP B  94      79.769  19.419   1.126  1.00 22.23           O  
-ATOM   3539  OD2 ASP B  94      81.447  19.730  -0.267  1.00 17.88           O  
-ATOM   3540  N   ILE B  95      80.673  24.304   2.102  1.00 24.50           N  
-ATOM   3541  CA  ILE B  95      81.260  25.427   2.830  1.00 27.96           C  
-ATOM   3542  C   ILE B  95      80.833  26.862   2.550  1.00 29.41           C  
-ATOM   3543  O   ILE B  95      81.101  27.738   3.362  1.00 30.84           O  
-ATOM   3544  CB  ILE B  95      82.804  25.368   2.688  1.00 28.68           C  
-ATOM   3545  CG1 ILE B  95      83.198  25.610   1.228  1.00 30.49           C  
-ATOM   3546  CG2 ILE B  95      83.318  23.990   3.085  1.00 25.26           C  
-ATOM   3547  CD1 ILE B  95      84.692  25.571   0.975  1.00 34.40           C  
-ATOM   3548  N   GLU B  96      80.157  27.118   1.435  1.00 29.64           N  
-ATOM   3549  CA  GLU B  96      79.770  28.489   1.117  1.00 31.08           C  
-ATOM   3550  C   GLU B  96      78.378  28.946   1.524  1.00 30.92           C  
-ATOM   3551  O   GLU B  96      78.180  30.133   1.792  1.00 29.95           O  
-ATOM   3552  CB  GLU B  96      79.953  28.735  -0.384  1.00 32.75           C  
-ATOM   3553  CG  GLU B  96      81.345  28.386  -0.863  1.00 37.24           C  
-ATOM   3554  CD  GLU B  96      81.503  28.566  -2.352  1.00 40.60           C  
-ATOM   3555  OE1 GLU B  96      80.660  28.049  -3.109  1.00 42.17           O  
-ATOM   3556  OE2 GLU B  96      82.479  29.217  -2.758  1.00 44.57           O  
-ATOM   3557  N   LYS B  97      77.412  28.032   1.569  1.00 28.93           N  
-ATOM   3558  CA  LYS B  97      76.052  28.428   1.928  1.00 29.93           C  
-ATOM   3559  C   LYS B  97      76.004  29.177   3.248  1.00 32.48           C  
-ATOM   3560  O   LYS B  97      76.666  28.800   4.217  1.00 29.84           O  
-ATOM   3561  CB  LYS B  97      75.124  27.214   2.014  1.00 31.10           C  
-ATOM   3562  CG  LYS B  97      73.673  27.557   2.382  1.00 33.39           C  
-ATOM   3563  CD  LYS B  97      72.844  26.272   2.471  1.00 35.98           C  
-ATOM   3564  CE  LYS B  97      71.403  26.512   2.899  1.00 37.13           C  
-ATOM   3565  NZ  LYS B  97      70.702  27.368   1.907  1.00 39.91           N  
-ATOM   3566  N   HIS B  98      75.202  30.235   3.274  1.00 33.55           N  
-ATOM   3567  CA  HIS B  98      75.052  31.060   4.454  1.00 35.42           C  
-ATOM   3568  C   HIS B  98      73.822  30.677   5.247  1.00 34.68           C  
-ATOM   3569  O   HIS B  98      72.726  30.528   4.705  1.00 33.46           O  
-ATOM   3570  CB  HIS B  98      74.948  32.537   4.059  1.00 42.06           C  
-ATOM   3571  CG  HIS B  98      76.067  33.379   4.584  1.00 46.13           C  
-ATOM   3572  ND1 HIS B  98      77.388  32.986   4.516  1.00 47.36           N  
-ATOM   3573  CD2 HIS B  98      76.065  34.601   5.170  1.00 47.70           C  
-ATOM   3574  CE1 HIS B  98      78.151  33.930   5.039  1.00 48.83           C  
-ATOM   3575  NE2 HIS B  98      77.374  34.922   5.442  1.00 48.13           N  
-ATOM   3576  N   TYR B  99      74.012  30.518   6.547  1.00 31.84           N  
-ATOM   3577  CA  TYR B  99      72.921  30.174   7.428  1.00 31.25           C  
-ATOM   3578  C   TYR B  99      72.812  31.330   8.403  1.00 32.78           C  
-ATOM   3579  O   TYR B  99      73.758  32.121   8.532  1.00 32.00           O  
-ATOM   3580  CB  TYR B  99      73.253  28.883   8.179  1.00 31.01           C  
-ATOM   3581  CG  TYR B  99      73.021  27.630   7.369  1.00 28.29           C  
-ATOM   3582  CD1 TYR B  99      71.727  27.216   7.061  1.00 30.16           C  
-ATOM   3583  CD2 TYR B  99      74.088  26.855   6.918  1.00 27.69           C  
-ATOM   3584  CE1 TYR B  99      71.493  26.053   6.319  1.00 29.78           C  
-ATOM   3585  CE2 TYR B  99      73.866  25.676   6.171  1.00 28.50           C  
-ATOM   3586  CZ  TYR B  99      72.571  25.286   5.879  1.00 30.19           C  
-ATOM   3587  OH  TYR B  99      72.322  24.133   5.147  1.00 31.13           O  
-ATOM   3588  N   PRO B 100      71.663  31.460   9.082  1.00 32.34           N  
-ATOM   3589  CA  PRO B 100      71.496  32.547  10.045  1.00 34.01           C  
-ATOM   3590  C   PRO B 100      72.639  32.457  11.050  1.00 33.40           C  
-ATOM   3591  O   PRO B 100      72.950  31.374  11.559  1.00 33.23           O  
-ATOM   3592  CB  PRO B 100      70.128  32.253  10.662  1.00 34.24           C  
-ATOM   3593  CG  PRO B 100      69.381  31.647   9.488  1.00 34.53           C  
-ATOM   3594  CD  PRO B 100      70.416  30.687   8.945  1.00 33.28           C  
-ATOM   3595  N   GLY B 101      73.279  33.591  11.305  1.00 32.66           N  
-ATOM   3596  CA  GLY B 101      74.391  33.599  12.226  1.00 34.20           C  
-ATOM   3597  C   GLY B 101      75.722  33.622  11.498  1.00 35.26           C  
-ATOM   3598  O   GLY B 101      76.772  33.757  12.143  1.00 36.01           O  
-ATOM   3599  N   ASP B 102      75.712  33.474  10.171  1.00 32.59           N  
-ATOM   3600  CA  ASP B 102      76.977  33.533   9.428  1.00 33.96           C  
-ATOM   3601  C   ASP B 102      77.225  34.987   9.013  1.00 34.98           C  
-ATOM   3602  O   ASP B 102      76.322  35.657   8.518  1.00 34.26           O  
-ATOM   3603  CB  ASP B 102      76.944  32.646   8.181  1.00 35.56           C  
-ATOM   3604  CG  ASP B 102      76.845  31.166   8.517  1.00 36.45           C  
-ATOM   3605  OD1 ASP B 102      77.251  30.778   9.631  1.00 35.55           O  
-ATOM   3606  OD2 ASP B 102      76.371  30.387   7.663  1.00 35.79           O  
-ATOM   3607  N   SER B 103      78.449  35.469   9.208  1.00 37.51           N  
-ATOM   3608  CA  SER B 103      78.781  36.854   8.877  1.00 38.56           C  
-ATOM   3609  C   SER B 103      80.122  37.016   8.169  1.00 38.24           C  
-ATOM   3610  O   SER B 103      81.096  36.340   8.500  1.00 38.29           O  
-ATOM   3611  CB  SER B 103      78.799  37.699  10.160  1.00 40.11           C  
-ATOM   3612  OG  SER B 103      79.191  39.040   9.893  1.00 40.76           O  
-ATOM   3613  N   TRP B 104      80.179  37.937   7.209  1.00 38.97           N  
-ATOM   3614  CA  TRP B 104      81.419  38.194   6.486  1.00 38.48           C  
-ATOM   3615  C   TRP B 104      82.397  38.972   7.384  1.00 38.30           C  
-ATOM   3616  O   TRP B 104      83.535  39.213   6.998  1.00 37.54           O  
-ATOM   3617  CB  TRP B 104      81.135  38.992   5.214  1.00 41.42           C  
-ATOM   3618  CG  TRP B 104      80.227  38.294   4.207  1.00 42.86           C  
-ATOM   3619  CD1 TRP B 104      79.247  38.878   3.457  1.00 43.21           C  
-ATOM   3620  CD2 TRP B 104      80.292  36.925   3.781  1.00 44.38           C  
-ATOM   3621  NE1 TRP B 104      78.704  37.966   2.587  1.00 44.20           N  
-ATOM   3622  CE2 TRP B 104      79.324  36.759   2.761  1.00 44.48           C  
-ATOM   3623  CE3 TRP B 104      81.075  35.825   4.152  1.00 44.85           C  
-ATOM   3624  CZ2 TRP B 104      79.119  35.538   2.107  1.00 45.39           C  
-ATOM   3625  CZ3 TRP B 104      80.872  34.603   3.496  1.00 47.12           C  
-ATOM   3626  CH2 TRP B 104      79.900  34.475   2.484  1.00 46.18           C  
-ATOM   3627  N   SER B 105      81.957  39.355   8.581  1.00 37.08           N  
-ATOM   3628  CA  SER B 105      82.824  40.081   9.513  1.00 35.48           C  
-ATOM   3629  C   SER B 105      83.984  39.185   9.924  1.00 35.06           C  
-ATOM   3630  O   SER B 105      85.001  39.664  10.416  1.00 35.77           O  
-ATOM   3631  CB  SER B 105      82.052  40.523  10.767  1.00 37.49           C  
-ATOM   3632  OG  SER B 105      81.754  39.422  11.616  1.00 37.46           O  
-ATOM   3633  N   ASP B 106      83.835  37.877   9.741  1.00 33.47           N  
-ATOM   3634  CA  ASP B 106      84.922  36.959  10.080  1.00 31.32           C  
-ATOM   3635  C   ASP B 106      86.057  37.301   9.128  1.00 30.98           C  
-ATOM   3636  O   ASP B 106      85.848  37.361   7.918  1.00 25.69           O  
-ATOM   3637  CB  ASP B 106      84.505  35.493   9.866  1.00 32.31           C  
-ATOM   3638  CG  ASP B 106      83.317  35.091  10.717  1.00 34.37           C  
-ATOM   3639  OD1 ASP B 106      83.147  35.694  11.801  1.00 33.90           O  
-ATOM   3640  OD2 ASP B 106      82.560  34.165  10.312  1.00 32.78           O  
-ATOM   3641  N   THR B 107      87.248  37.533   9.670  1.00 29.66           N  
-ATOM   3642  CA  THR B 107      88.388  37.880   8.847  1.00 30.91           C  
-ATOM   3643  C   THR B 107      89.100  36.618   8.424  1.00 30.97           C  
-ATOM   3644  O   THR B 107      88.861  35.548   8.977  1.00 32.83           O  
-ATOM   3645  CB  THR B 107      89.409  38.762   9.618  1.00 33.93           C  
-ATOM   3646  OG1 THR B 107      89.868  38.053  10.780  1.00 35.14           O  
-ATOM   3647  CG2 THR B 107      88.785  40.086  10.031  1.00 32.60           C  
-ATOM   3648  N   GLY B 108      90.000  36.746   7.460  1.00 28.96           N  
-ATOM   3649  CA  GLY B 108      90.734  35.587   6.999  1.00 30.01           C  
-ATOM   3650  C   GLY B 108      89.859  34.700   6.129  1.00 31.35           C  
-ATOM   3651  O   GLY B 108      88.874  35.174   5.551  1.00 31.18           O  
-ATOM   3652  N   ASN B 109      90.219  33.419   6.073  1.00 30.87           N  
-ATOM   3653  CA  ASN B 109      89.547  32.397   5.271  1.00 32.10           C  
-ATOM   3654  C   ASN B 109      88.614  31.581   6.162  1.00 32.56           C  
-ATOM   3655  O   ASN B 109      89.062  30.892   7.080  1.00 29.89           O  
-ATOM   3656  CB  ASN B 109      90.613  31.497   4.658  1.00 32.51           C  
-ATOM   3657  CG  ASN B 109      90.050  30.503   3.686  1.00 33.41           C  
-ATOM   3658  OD1 ASN B 109      89.033  30.749   3.035  1.00 33.87           O  
-ATOM   3659  ND2 ASN B 109      90.726  29.374   3.560  1.00 36.69           N  
-ATOM   3660  N   ASN B 110      87.320  31.652   5.873  1.00 33.37           N  
-ATOM   3661  CA  ASN B 110      86.325  30.988   6.691  1.00 32.62           C  
-ATOM   3662  C   ASN B 110      85.474  29.920   6.036  1.00 32.41           C  
-ATOM   3663  O   ASN B 110      85.232  29.944   4.833  1.00 29.80           O  
-ATOM   3664  CB  ASN B 110      85.426  32.050   7.288  1.00 32.64           C  
-ATOM   3665  CG  ASN B 110      86.200  33.012   8.155  1.00 37.47           C  
-ATOM   3666  OD1 ASN B 110      86.581  32.676   9.281  1.00 31.78           O  
-ATOM   3667  ND2 ASN B 110      86.464  34.202   7.629  1.00 35.26           N  
-ATOM   3668  N   VAL B 111      85.003  28.984   6.850  1.00 30.65           N  
-ATOM   3669  CA  VAL B 111      84.167  27.908   6.336  1.00 30.18           C  
-ATOM   3670  C   VAL B 111      82.764  28.061   6.884  1.00 28.37           C  
-ATOM   3671  O   VAL B 111      82.585  28.299   8.070  1.00 29.38           O  
-ATOM   3672  CB  VAL B 111      84.754  26.511   6.717  1.00 31.58           C  
-ATOM   3673  CG1 VAL B 111      84.849  26.360   8.236  1.00 32.94           C  
-ATOM   3674  CG2 VAL B 111      83.906  25.395   6.108  1.00 31.98           C  
-ATOM   3675  N   TYR B 112      81.768  27.988   6.003  1.00 26.45           N  
-ATOM   3676  CA  TYR B 112      80.370  28.065   6.423  1.00 23.26           C  
-ATOM   3677  C   TYR B 112      79.639  26.794   5.943  1.00 22.87           C  
-ATOM   3678  O   TYR B 112      80.167  25.688   6.072  1.00 25.05           O  
-ATOM   3679  CB  TYR B 112      79.705  29.317   5.857  1.00 25.16           C  
-ATOM   3680  CG  TYR B 112      80.425  30.577   6.290  1.00 27.28           C  
-ATOM   3681  CD1 TYR B 112      81.460  31.111   5.522  1.00 28.67           C  
-ATOM   3682  CD2 TYR B 112      80.130  31.185   7.514  1.00 29.09           C  
-ATOM   3683  CE1 TYR B 112      82.194  32.228   5.962  1.00 31.93           C  
-ATOM   3684  CE2 TYR B 112      80.859  32.302   7.973  1.00 30.81           C  
-ATOM   3685  CZ  TYR B 112      81.890  32.814   7.186  1.00 32.83           C  
-ATOM   3686  OH  TYR B 112      82.635  33.893   7.624  1.00 33.01           O  
-ATOM   3687  N   GLY B 113      78.439  26.949   5.396  1.00 20.82           N  
-ATOM   3688  CA  GLY B 113      77.718  25.792   4.887  1.00 22.92           C  
-ATOM   3689  C   GLY B 113      77.509  24.699   5.926  1.00 22.63           C  
-ATOM   3690  O   GLY B 113      77.562  24.975   7.122  1.00 20.18           O  
-ATOM   3691  N   CYS B 114      77.255  23.465   5.483  1.00 20.96           N  
-ATOM   3692  CA  CYS B 114      77.041  22.372   6.421  1.00 20.16           C  
-ATOM   3693  C   CYS B 114      78.254  22.116   7.322  1.00 22.58           C  
-ATOM   3694  O   CYS B 114      78.085  21.729   8.484  1.00 20.43           O  
-ATOM   3695  CB  CYS B 114      76.696  21.078   5.666  1.00 19.48           C  
-ATOM   3696  SG  CYS B 114      75.128  21.152   4.761  1.00 19.16           S  
-ATOM   3697  N   ILE B 115      79.465  22.306   6.786  1.00 22.18           N  
-ATOM   3698  CA  ILE B 115      80.668  22.062   7.575  1.00 24.90           C  
-ATOM   3699  C   ILE B 115      80.671  22.882   8.856  1.00 24.97           C  
-ATOM   3700  O   ILE B 115      80.955  22.357   9.927  1.00 26.90           O  
-ATOM   3701  CB  ILE B 115      81.958  22.368   6.780  1.00 26.39           C  
-ATOM   3702  CG1 ILE B 115      82.122  21.360   5.655  1.00 26.27           C  
-ATOM   3703  CG2 ILE B 115      83.183  22.301   7.708  1.00 27.92           C  
-ATOM   3704  CD1 ILE B 115      82.163  19.912   6.119  1.00 25.72           C  
-ATOM   3705  N   LYS B 116      80.349  24.162   8.763  1.00 24.85           N  
-ATOM   3706  CA  LYS B 116      80.328  24.979   9.969  1.00 25.92           C  
-ATOM   3707  C   LYS B 116      79.215  24.524  10.901  1.00 25.30           C  
-ATOM   3708  O   LYS B 116      79.433  24.394  12.103  1.00 24.57           O  
-ATOM   3709  CB  LYS B 116      80.122  26.462   9.646  1.00 25.39           C  
-ATOM   3710  CG  LYS B 116      79.820  27.318  10.897  1.00 27.46           C  
-ATOM   3711  CD  LYS B 116      79.721  28.821  10.576  1.00 25.14           C  
-ATOM   3712  CE  LYS B 116      79.491  29.641  11.848  1.00 28.12           C  
-ATOM   3713  NZ  LYS B 116      79.419  31.103  11.567  1.00 25.75           N  
-ATOM   3714  N   GLN B 117      78.026  24.292  10.344  1.00 24.02           N  
-ATOM   3715  CA  GLN B 117      76.876  23.860  11.143  1.00 24.80           C  
-ATOM   3716  C   GLN B 117      77.131  22.535  11.863  1.00 24.31           C  
-ATOM   3717  O   GLN B 117      76.678  22.345  12.987  1.00 27.98           O  
-ATOM   3718  CB  GLN B 117      75.628  23.759  10.260  1.00 27.04           C  
-ATOM   3719  CG  GLN B 117      75.219  25.118   9.698  1.00 26.27           C  
-ATOM   3720  CD  GLN B 117      75.004  26.129  10.806  1.00 28.59           C  
-ATOM   3721  OE1 GLN B 117      75.370  27.305  10.688  1.00 28.00           O  
-ATOM   3722  NE2 GLN B 117      74.403  25.676  11.896  1.00 24.24           N  
-ATOM   3723  N   LEU B 118      77.860  21.633  11.221  1.00 22.76           N  
-ATOM   3724  CA  LEU B 118      78.186  20.350  11.842  1.00 25.01           C  
-ATOM   3725  C   LEU B 118      79.164  20.582  12.999  1.00 25.79           C  
-ATOM   3726  O   LEU B 118      79.005  20.004  14.076  1.00 23.71           O  
-ATOM   3727  CB  LEU B 118      78.813  19.396  10.826  1.00 21.16           C  
-ATOM   3728  CG  LEU B 118      77.763  18.835   9.860  1.00 20.51           C  
-ATOM   3729  CD1 LEU B 118      78.439  18.174   8.658  1.00 19.64           C  
-ATOM   3730  CD2 LEU B 118      76.871  17.851  10.647  1.00 20.45           C  
-ATOM   3731  N   TYR B 119      80.164  21.435  12.783  1.00 24.54           N  
-ATOM   3732  CA  TYR B 119      81.125  21.735  13.841  1.00 24.96           C  
-ATOM   3733  C   TYR B 119      80.391  22.304  15.041  1.00 24.47           C  
-ATOM   3734  O   TYR B 119      80.680  21.940  16.177  1.00 26.51           O  
-ATOM   3735  CB  TYR B 119      82.171  22.761  13.386  1.00 27.88           C  
-ATOM   3736  CG  TYR B 119      83.208  23.055  14.466  1.00 27.24           C  
-ATOM   3737  CD1 TYR B 119      84.321  22.227  14.642  1.00 29.06           C  
-ATOM   3738  CD2 TYR B 119      83.054  24.137  15.333  1.00 28.62           C  
-ATOM   3739  CE1 TYR B 119      85.260  22.478  15.667  1.00 30.20           C  
-ATOM   3740  CE2 TYR B 119      83.982  24.397  16.358  1.00 29.89           C  
-ATOM   3741  CZ  TYR B 119      85.076  23.563  16.518  1.00 30.84           C  
-ATOM   3742  OH  TYR B 119      85.972  23.796  17.548  1.00 32.42           O  
-ATOM   3743  N   LEU B 120      79.447  23.207  14.789  1.00 25.77           N  
-ATOM   3744  CA  LEU B 120      78.673  23.814  15.868  1.00 26.05           C  
-ATOM   3745  C   LEU B 120      77.962  22.738  16.691  1.00 28.24           C  
-ATOM   3746  O   LEU B 120      77.921  22.815  17.919  1.00 26.92           O  
-ATOM   3747  CB  LEU B 120      77.654  24.795  15.306  1.00 27.01           C  
-ATOM   3748  CG  LEU B 120      78.199  26.148  14.802  1.00 29.91           C  
-ATOM   3749  CD1 LEU B 120      77.060  26.950  14.185  1.00 25.32           C  
-ATOM   3750  CD2 LEU B 120      78.827  26.921  15.967  1.00 29.23           C  
-ATOM   3751  N   LEU B 121      77.401  21.735  16.017  1.00 26.28           N  
-ATOM   3752  CA  LEU B 121      76.721  20.660  16.727  1.00 25.22           C  
-ATOM   3753  C   LEU B 121      77.721  19.956  17.634  1.00 25.60           C  
-ATOM   3754  O   LEU B 121      77.395  19.609  18.762  1.00 27.68           O  
-ATOM   3755  CB  LEU B 121      76.123  19.640  15.746  1.00 25.02           C  
-ATOM   3756  CG  LEU B 121      75.021  20.157  14.822  1.00 23.30           C  
-ATOM   3757  CD1 LEU B 121      74.467  18.991  13.989  1.00 24.65           C  
-ATOM   3758  CD2 LEU B 121      73.909  20.785  15.652  1.00 26.47           C  
-ATOM   3759  N   LYS B 122      78.932  19.751  17.124  1.00 25.05           N  
-ATOM   3760  CA  LYS B 122      79.983  19.091  17.873  1.00 25.97           C  
-ATOM   3761  C   LYS B 122      80.285  19.823  19.175  1.00 30.20           C  
-ATOM   3762  O   LYS B 122      80.591  19.189  20.190  1.00 29.27           O  
-ATOM   3763  CB  LYS B 122      81.248  18.990  17.018  1.00 27.79           C  
-ATOM   3764  CG  LYS B 122      81.205  17.873  15.980  1.00 24.90           C  
-ATOM   3765  CD  LYS B 122      82.506  17.730  15.186  1.00 25.96           C  
-ATOM   3766  CE  LYS B 122      83.777  17.742  16.075  1.00 21.52           C  
-ATOM   3767  NZ  LYS B 122      84.953  17.138  15.362  1.00 21.87           N  
-ATOM   3768  N   LYS B 123      80.196  21.153  19.143  1.00 31.15           N  
-ATOM   3769  CA  LYS B 123      80.438  21.974  20.330  1.00 35.10           C  
-ATOM   3770  C   LYS B 123      79.295  21.858  21.321  1.00 35.85           C  
-ATOM   3771  O   LYS B 123      79.497  21.918  22.531  1.00 34.58           O  
-ATOM   3772  CB  LYS B 123      80.570  23.454  19.958  1.00 36.84           C  
-ATOM   3773  CG  LYS B 123      81.816  23.822  19.180  1.00 40.12           C  
-ATOM   3774  CD  LYS B 123      81.871  25.340  18.881  1.00 42.34           C  
-ATOM   3775  CE  LYS B 123      81.881  26.222  20.140  1.00 39.90           C  
-ATOM   3776  NZ  LYS B 123      82.064  27.673  19.795  1.00 41.74           N  
-ATOM   3777  N   GLN B 124      78.081  21.721  20.805  1.00 36.06           N  
-ATOM   3778  CA  GLN B 124      76.922  21.623  21.685  1.00 37.04           C  
-ATOM   3779  C   GLN B 124      76.724  20.217  22.205  1.00 35.99           C  
-ATOM   3780  O   GLN B 124      76.006  20.005  23.173  1.00 35.75           O  
-ATOM   3781  CB  GLN B 124      75.674  22.090  20.954  1.00 40.51           C  
-ATOM   3782  CG  GLN B 124      75.672  23.595  20.702  1.00 44.92           C  
-ATOM   3783  CD  GLN B 124      75.347  23.974  19.251  1.00 47.94           C  
-ATOM   3784  OE1 GLN B 124      75.890  24.975  18.737  1.00 47.91           O  
-ATOM   3785  NE2 GLN B 124      74.448  23.236  18.606  1.00 46.96           N  
-ATOM   3786  N   ASN B 125      77.383  19.253  21.578  1.00 35.50           N  
-ATOM   3787  CA  ASN B 125      77.227  17.860  21.981  1.00 33.57           C  
-ATOM   3788  C   ASN B 125      78.579  17.197  21.870  1.00 30.37           C  
-ATOM   3789  O   ASN B 125      78.928  16.654  20.821  1.00 24.10           O  
-ATOM   3790  CB  ASN B 125      76.228  17.206  21.036  1.00 39.29           C  
-ATOM   3791  CG  ASN B 125      74.993  18.068  20.824  1.00 44.01           C  
-ATOM   3792  OD1 ASN B 125      74.083  18.085  21.659  1.00 45.82           O  
-ATOM   3793  ND2 ASN B 125      74.965  18.810  19.712  1.00 46.35           N  
-ATOM   3794  N   ARG B 126      79.339  17.239  22.962  1.00 27.74           N  
-ATOM   3795  CA  ARG B 126      80.683  16.686  22.982  1.00 27.41           C  
-ATOM   3796  C   ARG B 126      80.804  15.193  22.691  1.00 27.22           C  
-ATOM   3797  O   ARG B 126      81.907  14.702  22.412  1.00 28.17           O  
-ATOM   3798  CB  ARG B 126      81.349  17.019  24.327  1.00 29.42           C  
-ATOM   3799  CG  ARG B 126      81.528  18.525  24.556  1.00 29.55           C  
-ATOM   3800  CD  ARG B 126      82.156  19.228  23.321  1.00 29.91           C  
-ATOM   3801  NE  ARG B 126      83.378  18.574  22.858  1.00 31.29           N  
-ATOM   3802  CZ  ARG B 126      84.531  18.575  23.522  1.00 33.78           C  
-ATOM   3803  NH1 ARG B 126      84.629  19.214  24.684  1.00 35.99           N  
-ATOM   3804  NH2 ARG B 126      85.574  17.893  23.056  1.00 33.05           N  
-ATOM   3805  N   ASN B 127      79.686  14.472  22.771  1.00 27.33           N  
-ATOM   3806  CA  ASN B 127      79.701  13.043  22.479  1.00 27.97           C  
-ATOM   3807  C   ASN B 127      79.328  12.747  21.026  1.00 27.54           C  
-ATOM   3808  O   ASN B 127      79.285  11.581  20.609  1.00 27.98           O  
-ATOM   3809  CB  ASN B 127      78.740  12.278  23.391  1.00 26.54           C  
-ATOM   3810  CG  ASN B 127      78.986  10.781  23.341  1.00 27.52           C  
-ATOM   3811  OD1 ASN B 127      80.119  10.338  23.467  1.00 27.34           O  
-ATOM   3812  ND2 ASN B 127      77.925   9.996  23.142  1.00 25.62           N  
-ATOM   3813  N   LEU B 128      79.068  13.796  20.252  1.00 25.92           N  
-ATOM   3814  CA  LEU B 128      78.693  13.637  18.844  1.00 23.72           C  
-ATOM   3815  C   LEU B 128      79.905  13.741  17.933  1.00 23.94           C  
-ATOM   3816  O   LEU B 128      80.545  14.784  17.852  1.00 25.20           O  
-ATOM   3817  CB  LEU B 128      77.665  14.704  18.459  1.00 23.66           C  
-ATOM   3818  CG  LEU B 128      77.124  14.650  17.025  1.00 25.87           C  
-ATOM   3819  CD1 LEU B 128      76.126  13.478  16.878  1.00 27.40           C  
-ATOM   3820  CD2 LEU B 128      76.459  15.984  16.692  1.00 22.44           C  
-ATOM   3821  N   LYS B 129      80.234  12.656  17.249  1.00 23.27           N  
-ATOM   3822  CA  LYS B 129      81.363  12.665  16.337  1.00 23.01           C  
-ATOM   3823  C   LYS B 129      80.839  12.840  14.904  1.00 23.47           C  
-ATOM   3824  O   LYS B 129      79.762  12.335  14.559  1.00 22.02           O  
-ATOM   3825  CB  LYS B 129      82.162  11.353  16.452  1.00 22.20           C  
-ATOM   3826  CG  LYS B 129      83.154  11.309  17.652  1.00 22.10           C  
-ATOM   3827  CD  LYS B 129      82.443  11.287  18.981  1.00 19.70           C  
-ATOM   3828  CE  LYS B 129      81.881   9.898  19.240  1.00 23.11           C  
-ATOM   3829  NZ  LYS B 129      81.119   9.866  20.515  1.00 19.76           N  
-ATOM   3830  N   VAL B 130      81.579  13.582  14.086  1.00 21.15           N  
-ATOM   3831  CA  VAL B 130      81.182  13.792  12.690  1.00 21.52           C  
-ATOM   3832  C   VAL B 130      82.291  13.274  11.793  1.00 22.86           C  
-ATOM   3833  O   VAL B 130      83.419  13.752  11.862  1.00 23.60           O  
-ATOM   3834  CB  VAL B 130      80.954  15.272  12.381  1.00 20.35           C  
-ATOM   3835  CG1 VAL B 130      80.504  15.451  10.925  1.00 17.36           C  
-ATOM   3836  CG2 VAL B 130      79.934  15.829  13.341  1.00 17.16           C  
-ATOM   3837  N   LEU B 131      81.973  12.272  10.975  1.00 22.10           N  
-ATOM   3838  CA  LEU B 131      82.953  11.699  10.062  1.00 20.38           C  
-ATOM   3839  C   LEU B 131      82.625  12.098   8.635  1.00 21.08           C  
-ATOM   3840  O   LEU B 131      81.455  12.345   8.289  1.00 18.03           O  
-ATOM   3841  CB  LEU B 131      82.949  10.170  10.137  1.00 19.77           C  
-ATOM   3842  CG  LEU B 131      83.346   9.477  11.454  1.00 21.68           C  
-ATOM   3843  CD1 LEU B 131      82.366   9.825  12.548  1.00 24.13           C  
-ATOM   3844  CD2 LEU B 131      83.375   7.965  11.219  1.00 22.65           C  
-ATOM   3845  N   LEU B 132      83.659  12.157   7.808  1.00 19.74           N  
-ATOM   3846  CA  LEU B 132      83.487  12.479   6.410  1.00 20.71           C  
-ATOM   3847  C   LEU B 132      83.327  11.133   5.729  1.00 20.49           C  
-ATOM   3848  O   LEU B 132      84.162  10.232   5.898  1.00 21.46           O  
-ATOM   3849  CB  LEU B 132      84.727  13.190   5.868  1.00 21.12           C  
-ATOM   3850  CG  LEU B 132      84.690  13.362   4.350  1.00 20.41           C  
-ATOM   3851  CD1 LEU B 132      83.557  14.344   3.972  1.00 18.61           C  
-ATOM   3852  CD2 LEU B 132      86.043  13.876   3.855  1.00 19.51           C  
-ATOM   3853  N   SER B 133      82.244  10.960   4.983  1.00 21.39           N  
-ATOM   3854  CA  SER B 133      82.049   9.687   4.299  1.00 20.84           C  
-ATOM   3855  C   SER B 133      82.552   9.835   2.868  1.00 21.95           C  
-ATOM   3856  O   SER B 133      82.204  10.787   2.160  1.00 22.82           O  
-ATOM   3857  CB ASER B 133      80.574   9.278   4.327  0.50 20.01           C  
-ATOM   3858  OG ASER B 133      80.410   7.991   3.753  0.50 16.43           O  
-ATOM   3859  CB BSER B 133      80.562   9.302   4.292  0.50 22.29           C  
-ATOM   3860  OG BSER B 133      80.176   8.698   5.512  0.50 25.13           O  
-ATOM   3861  N   ILE B 134      83.386   8.886   2.458  1.00 21.34           N  
-ATOM   3862  CA  ILE B 134      83.979   8.898   1.145  1.00 20.73           C  
-ATOM   3863  C   ILE B 134      83.450   7.760   0.323  1.00 21.39           C  
-ATOM   3864  O   ILE B 134      83.516   6.601   0.736  1.00 21.04           O  
-ATOM   3865  CB  ILE B 134      85.508   8.766   1.231  1.00 20.63           C  
-ATOM   3866  CG1 ILE B 134      86.062   9.868   2.132  1.00 20.46           C  
-ATOM   3867  CG2 ILE B 134      86.129   8.846  -0.159  1.00 21.91           C  
-ATOM   3868  CD1 ILE B 134      87.506   9.589   2.629  1.00 24.32           C  
-ATOM   3869  N   GLY B 135      82.912   8.084  -0.851  1.00 19.96           N  
-ATOM   3870  CA  GLY B 135      82.399   7.026  -1.694  1.00 19.67           C  
-ATOM   3871  C   GLY B 135      80.917   7.141  -1.966  1.00 20.39           C  
-ATOM   3872  O   GLY B 135      80.423   8.205  -2.340  1.00 18.62           O  
-ATOM   3873  N   GLY B 136      80.197   6.048  -1.757  1.00 19.76           N  
-ATOM   3874  CA  GLY B 136      78.780   6.078  -2.049  1.00 18.23           C  
-ATOM   3875  C   GLY B 136      78.551   5.417  -3.393  1.00 19.05           C  
-ATOM   3876  O   GLY B 136      79.507   5.060  -4.111  1.00 19.25           O  
-ATOM   3877  N   TRP B 137      77.284   5.252  -3.754  1.00 18.58           N  
-ATOM   3878  CA  TRP B 137      76.951   4.585  -5.001  1.00 20.19           C  
-ATOM   3879  C   TRP B 137      77.504   5.256  -6.237  1.00 20.65           C  
-ATOM   3880  O   TRP B 137      78.006   4.579  -7.132  1.00 20.67           O  
-ATOM   3881  CB  TRP B 137      75.439   4.477  -5.176  1.00 22.28           C  
-ATOM   3882  CG  TRP B 137      74.767   3.606  -4.176  1.00 25.86           C  
-ATOM   3883  CD1 TRP B 137      75.357   2.748  -3.290  1.00 28.82           C  
-ATOM   3884  CD2 TRP B 137      73.361   3.456  -4.011  1.00 29.09           C  
-ATOM   3885  NE1 TRP B 137      74.396   2.065  -2.588  1.00 29.50           N  
-ATOM   3886  CE2 TRP B 137      73.161   2.482  -3.010  1.00 30.51           C  
-ATOM   3887  CE3 TRP B 137      72.245   4.050  -4.616  1.00 30.35           C  
-ATOM   3888  CZ2 TRP B 137      71.885   2.084  -2.597  1.00 31.11           C  
-ATOM   3889  CZ3 TRP B 137      70.973   3.655  -4.207  1.00 31.76           C  
-ATOM   3890  CH2 TRP B 137      70.807   2.681  -3.207  1.00 31.93           C  
-ATOM   3891  N   THR B 138      77.412   6.578  -6.296  1.00 19.32           N  
-ATOM   3892  CA  THR B 138      77.876   7.284  -7.485  1.00 20.02           C  
-ATOM   3893  C   THR B 138      79.384   7.220  -7.672  1.00 20.89           C  
-ATOM   3894  O   THR B 138      79.870   6.993  -8.779  1.00 19.99           O  
-ATOM   3895  CB  THR B 138      77.477   8.786  -7.454  1.00 20.48           C  
-ATOM   3896  OG1 THR B 138      76.055   8.897  -7.400  1.00 20.79           O  
-ATOM   3897  CG2 THR B 138      77.977   9.511  -8.716  1.00 17.51           C  
-ATOM   3898  N   TYR B 139      80.111   7.429  -6.586  1.00 21.54           N  
-ATOM   3899  CA  TYR B 139      81.554   7.467  -6.657  1.00 20.90           C  
-ATOM   3900  C   TYR B 139      82.308   6.160  -6.515  1.00 23.53           C  
-ATOM   3901  O   TYR B 139      83.515   6.132  -6.782  1.00 23.49           O  
-ATOM   3902  CB  TYR B 139      82.097   8.437  -5.613  1.00 21.47           C  
-ATOM   3903  CG  TYR B 139      81.468   9.809  -5.632  1.00 19.72           C  
-ATOM   3904  CD1 TYR B 139      81.281  10.492  -6.834  1.00 20.00           C  
-ATOM   3905  CD2 TYR B 139      81.080  10.441  -4.445  1.00 20.81           C  
-ATOM   3906  CE1 TYR B 139      80.718  11.773  -6.861  1.00 19.46           C  
-ATOM   3907  CE2 TYR B 139      80.515  11.732  -4.456  1.00 18.97           C  
-ATOM   3908  CZ  TYR B 139      80.337  12.386  -5.674  1.00 21.08           C  
-ATOM   3909  OH  TYR B 139      79.793  13.656  -5.731  1.00 22.59           O  
-ATOM   3910  N   SER B 140      81.627   5.079  -6.131  1.00 21.31           N  
-ATOM   3911  CA  SER B 140      82.322   3.794  -5.923  1.00 21.57           C  
-ATOM   3912  C   SER B 140      83.220   3.240  -7.043  1.00 22.24           C  
-ATOM   3913  O   SER B 140      84.208   2.569  -6.764  1.00 21.65           O  
-ATOM   3914  CB  SER B 140      81.333   2.710  -5.471  1.00 20.74           C  
-ATOM   3915  OG  SER B 140      81.105   2.840  -4.061  1.00 22.66           O  
-ATOM   3916  N   PRO B 141      82.892   3.504  -8.313  1.00 23.82           N  
-ATOM   3917  CA  PRO B 141      83.732   2.993  -9.404  1.00 24.46           C  
-ATOM   3918  C   PRO B 141      85.155   3.565  -9.356  1.00 24.05           C  
-ATOM   3919  O   PRO B 141      86.059   3.059 -10.019  1.00 22.88           O  
-ATOM   3920  CB  PRO B 141      82.997   3.465 -10.652  1.00 23.05           C  
-ATOM   3921  CG  PRO B 141      81.533   3.512 -10.184  1.00 25.96           C  
-ATOM   3922  CD  PRO B 141      81.688   4.172  -8.844  1.00 23.67           C  
-ATOM   3923  N   ASN B 142      85.348   4.623  -8.577  1.00 22.63           N  
-ATOM   3924  CA  ASN B 142      86.662   5.262  -8.511  1.00 24.67           C  
-ATOM   3925  C   ASN B 142      87.613   4.618  -7.513  1.00 25.82           C  
-ATOM   3926  O   ASN B 142      88.810   4.905  -7.515  1.00 26.15           O  
-ATOM   3927  CB  ASN B 142      86.517   6.739  -8.159  1.00 21.20           C  
-ATOM   3928  CG  ASN B 142      85.716   7.513  -9.197  1.00 23.94           C  
-ATOM   3929  OD1 ASN B 142      85.633   7.114 -10.360  1.00 22.83           O  
-ATOM   3930  ND2 ASN B 142      85.133   8.630  -8.780  1.00 22.81           N  
-ATOM   3931  N   PHE B 143      87.082   3.750  -6.661  1.00 24.73           N  
-ATOM   3932  CA  PHE B 143      87.915   3.106  -5.660  1.00 23.41           C  
-ATOM   3933  C   PHE B 143      88.941   2.135  -6.236  1.00 23.64           C  
-ATOM   3934  O   PHE B 143      90.123   2.229  -5.927  1.00 26.40           O  
-ATOM   3935  CB  PHE B 143      87.044   2.378  -4.625  1.00 22.75           C  
-ATOM   3936  CG  PHE B 143      86.462   3.288  -3.574  1.00 21.39           C  
-ATOM   3937  CD1 PHE B 143      87.280   3.920  -2.650  1.00 22.04           C  
-ATOM   3938  CD2 PHE B 143      85.094   3.510  -3.512  1.00 22.16           C  
-ATOM   3939  CE1 PHE B 143      86.751   4.764  -1.676  1.00 24.70           C  
-ATOM   3940  CE2 PHE B 143      84.547   4.356  -2.541  1.00 20.83           C  
-ATOM   3941  CZ  PHE B 143      85.364   4.983  -1.626  1.00 24.09           C  
-ATOM   3942  N   ALA B 144      88.501   1.211  -7.068  1.00 23.59           N  
-ATOM   3943  CA  ALA B 144      89.421   0.230  -7.617  1.00 27.57           C  
-ATOM   3944  C   ALA B 144      90.695   0.890  -8.189  1.00 30.28           C  
-ATOM   3945  O   ALA B 144      91.814   0.575  -7.764  1.00 30.88           O  
-ATOM   3946  CB  ALA B 144      88.716  -0.604  -8.672  1.00 27.47           C  
-ATOM   3947  N   PRO B 145      90.542   1.834  -9.133  1.00 30.33           N  
-ATOM   3948  CA  PRO B 145      91.752   2.459  -9.673  1.00 31.46           C  
-ATOM   3949  C   PRO B 145      92.554   3.259  -8.653  1.00 31.98           C  
-ATOM   3950  O   PRO B 145      93.775   3.104  -8.547  1.00 30.57           O  
-ATOM   3951  CB  PRO B 145      91.219   3.320 -10.827  1.00 30.60           C  
-ATOM   3952  CG  PRO B 145      89.787   3.601 -10.425  1.00 32.71           C  
-ATOM   3953  CD  PRO B 145      89.339   2.277  -9.860  1.00 30.17           C  
-ATOM   3954  N   ALA B 146      91.874   4.106  -7.891  1.00 31.32           N  
-ATOM   3955  CA  ALA B 146      92.564   4.920  -6.911  1.00 32.25           C  
-ATOM   3956  C   ALA B 146      93.378   4.090  -5.921  1.00 34.30           C  
-ATOM   3957  O   ALA B 146      94.496   4.457  -5.570  1.00 36.12           O  
-ATOM   3958  CB  ALA B 146      91.579   5.767  -6.168  1.00 32.64           C  
-ATOM   3959  N   ALA B 147      92.836   2.966  -5.474  1.00 32.85           N  
-ATOM   3960  CA  ALA B 147      93.553   2.160  -4.490  1.00 33.88           C  
-ATOM   3961  C   ALA B 147      94.496   1.113  -5.082  1.00 32.58           C  
-ATOM   3962  O   ALA B 147      95.163   0.403  -4.338  1.00 32.27           O  
-ATOM   3963  CB  ALA B 147      92.551   1.481  -3.558  1.00 30.61           C  
-ATOM   3964  N   SER B 148      94.552   1.042  -6.409  1.00 32.47           N  
-ATOM   3965  CA  SER B 148      95.362   0.044  -7.102  1.00 33.15           C  
-ATOM   3966  C   SER B 148      96.870   0.205  -6.969  1.00 35.00           C  
-ATOM   3967  O   SER B 148      97.608  -0.744  -7.217  1.00 34.70           O  
-ATOM   3968  CB  SER B 148      95.004   0.016  -8.585  1.00 32.46           C  
-ATOM   3969  OG  SER B 148      95.374   1.235  -9.205  1.00 33.84           O  
-ATOM   3970  N   THR B 149      97.319   1.400  -6.593  1.00 35.75           N  
-ATOM   3971  CA  THR B 149      98.746   1.661  -6.438  1.00 37.01           C  
-ATOM   3972  C   THR B 149      99.049   2.227  -5.053  1.00 38.70           C  
-ATOM   3973  O   THR B 149      98.180   2.802  -4.384  1.00 38.45           O  
-ATOM   3974  CB  THR B 149      99.275   2.682  -7.485  1.00 35.27           C  
-ATOM   3975  OG1 THR B 149      98.832   3.990  -7.129  1.00 35.03           O  
-ATOM   3976  CG2 THR B 149      98.762   2.365  -8.873  1.00 33.50           C  
-ATOM   3977  N   ASP B 150     100.297   2.068  -4.632  1.00 38.99           N  
-ATOM   3978  CA  ASP B 150     100.740   2.557  -3.339  1.00 39.00           C  
-ATOM   3979  C   ASP B 150     100.663   4.084  -3.336  1.00 38.20           C  
-ATOM   3980  O   ASP B 150     100.273   4.711  -2.342  1.00 37.22           O  
-ATOM   3981  CB  ASP B 150     102.178   2.074  -3.097  1.00 44.14           C  
-ATOM   3982  CG  ASP B 150     102.794   2.653  -1.839  1.00 45.58           C  
-ATOM   3983  OD1 ASP B 150     102.350   2.304  -0.722  1.00 46.82           O  
-ATOM   3984  OD2 ASP B 150     103.729   3.471  -1.978  1.00 47.88           O  
-ATOM   3985  N   ALA B 151     101.038   4.685  -4.458  1.00 38.50           N  
-ATOM   3986  CA  ALA B 151     100.993   6.139  -4.573  1.00 37.81           C  
-ATOM   3987  C   ALA B 151      99.546   6.601  -4.398  1.00 36.85           C  
-ATOM   3988  O   ALA B 151      99.277   7.557  -3.672  1.00 36.65           O  
-ATOM   3989  CB  ALA B 151     101.525   6.575  -5.932  1.00 37.45           C  
-ATOM   3990  N   GLY B 152      98.623   5.910  -5.064  1.00 36.10           N  
-ATOM   3991  CA  GLY B 152      97.210   6.264  -4.970  1.00 36.32           C  
-ATOM   3992  C   GLY B 152      96.672   6.185  -3.550  1.00 35.04           C  
-ATOM   3993  O   GLY B 152      96.039   7.130  -3.053  1.00 34.66           O  
-ATOM   3994  N   ARG B 153      96.937   5.057  -2.889  1.00 35.07           N  
-ATOM   3995  CA  ARG B 153      96.482   4.845  -1.512  1.00 32.50           C  
-ATOM   3996  C   ARG B 153      97.060   5.882  -0.566  1.00 32.10           C  
-ATOM   3997  O   ARG B 153      96.353   6.434   0.282  1.00 29.43           O  
-ATOM   3998  CB  ARG B 153      96.871   3.452  -1.037  1.00 30.65           C  
-ATOM   3999  CG  ARG B 153      96.267   2.351  -1.855  1.00 31.74           C  
-ATOM   4000  CD  ARG B 153      96.602   0.996  -1.261  1.00 35.03           C  
-ATOM   4001  NE  ARG B 153      98.005   0.636  -1.457  1.00 34.27           N  
-ATOM   4002  CZ  ARG B 153      98.483  -0.035  -2.501  1.00 37.71           C  
-ATOM   4003  NH1 ARG B 153      97.685  -0.443  -3.486  1.00 37.74           N  
-ATOM   4004  NH2 ARG B 153      99.778  -0.320  -2.549  1.00 39.69           N  
-ATOM   4005  N   LYS B 154      98.352   6.154  -0.708  1.00 32.34           N  
-ATOM   4006  CA  LYS B 154      98.988   7.137   0.156  1.00 33.12           C  
-ATOM   4007  C   LYS B 154      98.399   8.523  -0.047  1.00 29.42           C  
-ATOM   4008  O   LYS B 154      98.206   9.263   0.907  1.00 29.36           O  
-ATOM   4009  CB  LYS B 154     100.500   7.165  -0.096  1.00 35.15           C  
-ATOM   4010  CG  LYS B 154     101.196   5.943   0.456  1.00 40.65           C  
-ATOM   4011  CD  LYS B 154     102.684   5.928   0.145  1.00 43.23           C  
-ATOM   4012  CE  LYS B 154     103.336   4.660   0.695  1.00 44.47           C  
-ATOM   4013  NZ  LYS B 154     104.776   4.606   0.332  1.00 47.67           N  
-ATOM   4014  N   ASN B 155      98.110   8.869  -1.293  1.00 29.04           N  
-ATOM   4015  CA  ASN B 155      97.549  10.184  -1.573  1.00 30.60           C  
-ATOM   4016  C   ASN B 155      96.105  10.288  -1.064  1.00 28.65           C  
-ATOM   4017  O   ASN B 155      95.651  11.353  -0.640  1.00 25.74           O  
-ATOM   4018  CB  ASN B 155      97.610  10.464  -3.070  1.00 31.84           C  
-ATOM   4019  CG  ASN B 155      97.259  11.899  -3.398  1.00 34.80           C  
-ATOM   4020  OD1 ASN B 155      97.735  12.829  -2.738  1.00 35.44           O  
-ATOM   4021  ND2 ASN B 155      96.420  12.091  -4.421  1.00 35.36           N  
-ATOM   4022  N   PHE B 156      95.393   9.170  -1.113  1.00 27.59           N  
-ATOM   4023  CA  PHE B 156      94.019   9.128  -0.615  1.00 27.68           C  
-ATOM   4024  C   PHE B 156      94.101   9.482   0.865  1.00 27.37           C  
-ATOM   4025  O   PHE B 156      93.442  10.402   1.335  1.00 26.86           O  
-ATOM   4026  CB  PHE B 156      93.466   7.714  -0.813  1.00 25.68           C  
-ATOM   4027  CG  PHE B 156      92.061   7.515  -0.306  1.00 26.40           C  
-ATOM   4028  CD1 PHE B 156      91.776   7.536   1.060  1.00 26.19           C  
-ATOM   4029  CD2 PHE B 156      91.028   7.248  -1.205  1.00 25.06           C  
-ATOM   4030  CE1 PHE B 156      90.469   7.285   1.527  1.00 28.04           C  
-ATOM   4031  CE2 PHE B 156      89.726   6.999  -0.756  1.00 25.59           C  
-ATOM   4032  CZ  PHE B 156      89.443   7.015   0.603  1.00 24.57           C  
-ATOM   4033  N   ALA B 157      94.950   8.763   1.599  1.00 29.18           N  
-ATOM   4034  CA  ALA B 157      95.092   9.021   3.029  1.00 28.27           C  
-ATOM   4035  C   ALA B 157      95.495  10.455   3.304  1.00 28.54           C  
-ATOM   4036  O   ALA B 157      94.909  11.140   4.154  1.00 26.76           O  
-ATOM   4037  CB  ALA B 157      96.134   8.064   3.642  1.00 30.61           C  
-ATOM   4038  N   LYS B 158      96.502  10.920   2.573  1.00 28.22           N  
-ATOM   4039  CA  LYS B 158      96.992  12.264   2.804  1.00 28.59           C  
-ATOM   4040  C   LYS B 158      95.923  13.311   2.562  1.00 26.30           C  
-ATOM   4041  O   LYS B 158      95.693  14.175   3.398  1.00 26.68           O  
-ATOM   4042  CB  LYS B 158      98.207  12.525   1.909  1.00 30.92           C  
-ATOM   4043  CG  LYS B 158      98.877  13.873   2.129  1.00 36.34           C  
-ATOM   4044  CD  LYS B 158      99.892  14.124   1.015  1.00 42.00           C  
-ATOM   4045  CE  LYS B 158     100.727  15.389   1.226  1.00 44.41           C  
-ATOM   4046  NZ  LYS B 158     101.738  15.545   0.114  1.00 47.47           N  
-ATOM   4047  N   THR B 159      95.258  13.223   1.417  1.00 26.41           N  
-ATOM   4048  CA  THR B 159      94.233  14.211   1.090  1.00 26.49           C  
-ATOM   4049  C   THR B 159      93.014  14.122   2.019  1.00 25.56           C  
-ATOM   4050  O   THR B 159      92.486  15.144   2.430  1.00 26.73           O  
-ATOM   4051  CB  THR B 159      93.801  14.085  -0.392  1.00 25.70           C  
-ATOM   4052  OG1 THR B 159      93.445  12.726  -0.682  1.00 24.39           O  
-ATOM   4053  CG2 THR B 159      94.972  14.513  -1.326  1.00 24.73           C  
-ATOM   4054  N   ALA B 160      92.589  12.910   2.370  1.00 24.95           N  
-ATOM   4055  CA  ALA B 160      91.433  12.760   3.253  1.00 24.08           C  
-ATOM   4056  C   ALA B 160      91.758  13.328   4.624  1.00 24.98           C  
-ATOM   4057  O   ALA B 160      90.942  14.054   5.231  1.00 22.86           O  
-ATOM   4058  CB  ALA B 160      91.024  11.277   3.358  1.00 22.97           C  
-ATOM   4059  N   VAL B 161      92.964  13.030   5.115  1.00 25.28           N  
-ATOM   4060  CA  VAL B 161      93.348  13.542   6.421  1.00 26.62           C  
-ATOM   4061  C   VAL B 161      93.479  15.051   6.370  1.00 26.50           C  
-ATOM   4062  O   VAL B 161      93.183  15.740   7.344  1.00 27.81           O  
-ATOM   4063  CB  VAL B 161      94.634  12.869   6.933  1.00 28.60           C  
-ATOM   4064  CG1 VAL B 161      95.163  13.591   8.173  1.00 30.42           C  
-ATOM   4065  CG2 VAL B 161      94.306  11.458   7.337  1.00 29.73           C  
-ATOM   4066  N   LYS B 162      93.901  15.579   5.225  1.00 28.42           N  
-ATOM   4067  CA  LYS B 162      93.990  17.030   5.073  1.00 28.92           C  
-ATOM   4068  C   LYS B 162      92.573  17.640   5.213  1.00 27.48           C  
-ATOM   4069  O   LYS B 162      92.394  18.702   5.821  1.00 25.86           O  
-ATOM   4070  CB  LYS B 162      94.583  17.356   3.699  1.00 32.21           C  
-ATOM   4071  CG  LYS B 162      94.691  18.832   3.372  1.00 36.94           C  
-ATOM   4072  CD  LYS B 162      95.738  19.523   4.212  1.00 40.23           C  
-ATOM   4073  CE  LYS B 162      96.095  20.879   3.616  1.00 42.55           C  
-ATOM   4074  NZ  LYS B 162      94.912  21.797   3.505  1.00 43.51           N  
-ATOM   4075  N   LEU B 163      91.555  16.966   4.665  1.00 25.36           N  
-ATOM   4076  CA  LEU B 163      90.185  17.486   4.785  1.00 23.45           C  
-ATOM   4077  C   LEU B 163      89.739  17.479   6.240  1.00 21.52           C  
-ATOM   4078  O   LEU B 163      89.080  18.414   6.733  1.00 21.92           O  
-ATOM   4079  CB  LEU B 163      89.212  16.643   3.941  1.00 23.03           C  
-ATOM   4080  CG  LEU B 163      89.479  16.733   2.436  1.00 25.45           C  
-ATOM   4081  CD1 LEU B 163      88.550  15.799   1.650  1.00 24.98           C  
-ATOM   4082  CD2 LEU B 163      89.272  18.167   2.023  1.00 23.35           C  
-ATOM   4083  N   LEU B 164      90.099  16.408   6.931  1.00 22.54           N  
-ATOM   4084  CA  LEU B 164      89.740  16.282   8.331  1.00 24.12           C  
-ATOM   4085  C   LEU B 164      90.348  17.389   9.169  1.00 23.76           C  
-ATOM   4086  O   LEU B 164      89.678  17.942  10.036  1.00 25.09           O  
-ATOM   4087  CB  LEU B 164      90.186  14.919   8.873  1.00 22.97           C  
-ATOM   4088  CG  LEU B 164      89.926  14.675  10.359  1.00 26.64           C  
-ATOM   4089  CD1 LEU B 164      89.619  13.180  10.587  1.00 26.29           C  
-ATOM   4090  CD2 LEU B 164      91.132  15.133  11.178  1.00 27.10           C  
-ATOM   4091  N   GLN B 165      91.608  17.725   8.918  1.00 25.39           N  
-ATOM   4092  CA  GLN B 165      92.240  18.768   9.730  1.00 27.38           C  
-ATOM   4093  C   GLN B 165      91.672  20.147   9.456  1.00 27.10           C  
-ATOM   4094  O   GLN B 165      91.618  21.001  10.347  1.00 27.29           O  
-ATOM   4095  CB  GLN B 165      93.754  18.756   9.529  1.00 29.87           C  
-ATOM   4096  CG  GLN B 165      94.245  19.374   8.251  1.00 34.47           C  
-ATOM   4097  CD  GLN B 165      95.768  19.389   8.167  1.00 37.56           C  
-ATOM   4098  OE1 GLN B 165      96.429  18.356   8.302  1.00 38.97           O  
-ATOM   4099  NE2 GLN B 165      96.326  20.562   7.927  1.00 41.43           N  
-ATOM   4100  N   ASP B 166      91.214  20.361   8.227  1.00 27.27           N  
-ATOM   4101  CA  ASP B 166      90.630  21.646   7.879  1.00 26.47           C  
-ATOM   4102  C   ASP B 166      89.165  21.782   8.234  1.00 27.63           C  
-ATOM   4103  O   ASP B 166      88.751  22.817   8.755  1.00 26.86           O  
-ATOM   4104  CB  ASP B 166      90.745  21.916   6.380  1.00 29.44           C  
-ATOM   4105  CG  ASP B 166      92.150  22.264   5.950  1.00 31.48           C  
-ATOM   4106  OD1 ASP B 166      92.962  22.703   6.791  1.00 34.24           O  
-ATOM   4107  OD2 ASP B 166      92.422  22.113   4.754  1.00 32.49           O  
-ATOM   4108  N   LEU B 167      88.382  20.730   7.966  1.00 27.90           N  
-ATOM   4109  CA  LEU B 167      86.933  20.797   8.162  1.00 26.37           C  
-ATOM   4110  C   LEU B 167      86.381  20.336   9.511  1.00 26.59           C  
-ATOM   4111  O   LEU B 167      85.173  20.419   9.751  1.00 24.93           O  
-ATOM   4112  CB  LEU B 167      86.247  20.063   6.996  1.00 26.55           C  
-ATOM   4113  CG  LEU B 167      86.785  20.497   5.616  1.00 25.08           C  
-ATOM   4114  CD1 LEU B 167      86.195  19.639   4.485  1.00 24.23           C  
-ATOM   4115  CD2 LEU B 167      86.456  21.975   5.402  1.00 22.30           C  
-ATOM   4116  N   GLY B 168      87.265  19.857  10.385  1.00 26.43           N  
-ATOM   4117  CA  GLY B 168      86.856  19.465  11.726  1.00 23.51           C  
-ATOM   4118  C   GLY B 168      86.164  18.131  11.919  1.00 22.87           C  
-ATOM   4119  O   GLY B 168      85.237  18.031  12.721  1.00 23.63           O  
-ATOM   4120  N   PHE B 169      86.622  17.107  11.215  1.00 23.84           N  
-ATOM   4121  CA  PHE B 169      86.011  15.791  11.325  1.00 25.38           C  
-ATOM   4122  C   PHE B 169      86.661  14.936  12.416  1.00 28.13           C  
-ATOM   4123  O   PHE B 169      87.839  15.101  12.758  1.00 25.87           O  
-ATOM   4124  CB  PHE B 169      86.079  15.065   9.977  1.00 26.56           C  
-ATOM   4125  CG  PHE B 169      85.277  15.738   8.877  1.00 28.25           C  
-ATOM   4126  CD1 PHE B 169      83.928  16.009   9.051  1.00 30.30           C  
-ATOM   4127  CD2 PHE B 169      85.875  16.105   7.677  1.00 27.55           C  
-ATOM   4128  CE1 PHE B 169      83.179  16.642   8.039  1.00 31.66           C  
-ATOM   4129  CE2 PHE B 169      85.139  16.734   6.669  1.00 28.64           C  
-ATOM   4130  CZ  PHE B 169      83.794  17.003   6.851  1.00 27.81           C  
-ATOM   4131  N   ASP B 170      85.879  14.014  12.959  1.00 26.55           N  
-ATOM   4132  CA  ASP B 170      86.354  13.122  14.005  1.00 25.61           C  
-ATOM   4133  C   ASP B 170      86.849  11.824  13.416  1.00 25.09           C  
-ATOM   4134  O   ASP B 170      87.308  10.939  14.136  1.00 24.22           O  
-ATOM   4135  CB  ASP B 170      85.226  12.835  14.977  1.00 23.58           C  
-ATOM   4136  CG  ASP B 170      84.855  14.028  15.768  1.00 25.13           C  
-ATOM   4137  OD1 ASP B 170      85.670  14.400  16.651  1.00 26.74           O  
-ATOM   4138  OD2 ASP B 170      83.763  14.604  15.526  1.00 22.07           O  
-ATOM   4139  N   GLY B 171      86.751  11.710  12.099  1.00 23.90           N  
-ATOM   4140  CA  GLY B 171      87.191  10.495  11.450  1.00 22.05           C  
-ATOM   4141  C   GLY B 171      86.693  10.412  10.019  1.00 23.31           C  
-ATOM   4142  O   GLY B 171      86.056  11.340   9.492  1.00 23.69           O  
-ATOM   4143  N   LEU B 172      86.978   9.279   9.402  1.00 21.15           N  
-ATOM   4144  CA  LEU B 172      86.611   9.047   8.030  1.00 21.44           C  
-ATOM   4145  C   LEU B 172      85.843   7.754   7.922  1.00 21.40           C  
-ATOM   4146  O   LEU B 172      86.097   6.797   8.661  1.00 21.88           O  
-ATOM   4147  CB  LEU B 172      87.868   8.950   7.173  1.00 20.50           C  
-ATOM   4148  CG  LEU B 172      88.831  10.147   7.253  1.00 22.57           C  
-ATOM   4149  CD1 LEU B 172      90.142   9.794   6.569  1.00 23.28           C  
-ATOM   4150  CD2 LEU B 172      88.193  11.353   6.605  1.00 21.94           C  
-ATOM   4151  N   ASP B 173      84.911   7.740   6.980  1.00 19.93           N  
-ATOM   4152  CA  ASP B 173      84.097   6.575   6.716  1.00 21.16           C  
-ATOM   4153  C   ASP B 173      84.264   6.281   5.228  1.00 22.11           C  
-ATOM   4154  O   ASP B 173      84.081   7.173   4.387  1.00 20.70           O  
-ATOM   4155  CB  ASP B 173      82.633   6.873   7.054  1.00 21.37           C  
-ATOM   4156  CG  ASP B 173      81.694   5.765   6.605  1.00 21.61           C  
-ATOM   4157  OD1 ASP B 173      81.838   4.620   7.092  1.00 18.40           O  
-ATOM   4158  OD2 ASP B 173      80.824   6.047   5.745  1.00 22.86           O  
-ATOM   4159  N   ILE B 174      84.634   5.045   4.900  1.00 21.29           N  
-ATOM   4160  CA  ILE B 174      84.826   4.679   3.503  1.00 22.28           C  
-ATOM   4161  C   ILE B 174      83.675   3.775   3.040  1.00 23.28           C  
-ATOM   4162  O   ILE B 174      83.424   2.726   3.621  1.00 21.71           O  
-ATOM   4163  CB AILE B 174      86.184   3.974   3.309  0.50 22.52           C  
-ATOM   4164  CG1AILE B 174      87.309   4.899   3.787  0.50 24.21           C  
-ATOM   4165  CG2AILE B 174      86.394   3.625   1.848  0.50 22.95           C  
-ATOM   4166  CD1AILE B 174      88.680   4.289   3.718  0.50 21.71           C  
-ATOM   4167  CB BILE B 174      86.184   3.947   3.290  0.50 22.47           C  
-ATOM   4168  CG1BILE B 174      87.342   4.785   3.855  0.50 24.19           C  
-ATOM   4169  CG2BILE B 174      86.393   3.662   1.815  0.50 23.00           C  
-ATOM   4170  CD1BILE B 174      87.059   6.276   3.922  0.50 21.59           C  
-ATOM   4171  N   ASP B 175      82.969   4.221   2.001  1.00 21.80           N  
-ATOM   4172  CA  ASP B 175      81.824   3.504   1.455  1.00 21.12           C  
-ATOM   4173  C   ASP B 175      82.112   3.040   0.043  1.00 21.41           C  
-ATOM   4174  O   ASP B 175      81.850   3.750  -0.934  1.00 20.04           O  
-ATOM   4175  CB  ASP B 175      80.601   4.421   1.466  1.00 22.35           C  
-ATOM   4176  CG  ASP B 175      80.208   4.830   2.857  1.00 23.91           C  
-ATOM   4177  OD1 ASP B 175      79.164   5.510   3.013  1.00 23.34           O  
-ATOM   4178  OD2 ASP B 175      80.946   4.469   3.811  1.00 26.47           O  
-ATOM   4179  N   TRP B 176      82.658   1.840  -0.070  1.00 21.40           N  
-ATOM   4180  CA  TRP B 176      83.016   1.319  -1.377  1.00 22.07           C  
-ATOM   4181  C   TRP B 176      82.026   0.238  -1.740  1.00 21.98           C  
-ATOM   4182  O   TRP B 176      82.035  -0.845  -1.158  1.00 21.41           O  
-ATOM   4183  CB  TRP B 176      84.439   0.758  -1.311  1.00 22.63           C  
-ATOM   4184  CG  TRP B 176      85.002   0.135  -2.580  1.00 25.64           C  
-ATOM   4185  CD1 TRP B 176      84.314  -0.259  -3.698  1.00 26.07           C  
-ATOM   4186  CD2 TRP B 176      86.372  -0.208  -2.809  1.00 25.15           C  
-ATOM   4187  NE1 TRP B 176      85.180  -0.827  -4.610  1.00 25.34           N  
-ATOM   4188  CE2 TRP B 176      86.449  -0.806  -4.085  1.00 27.35           C  
-ATOM   4189  CE3 TRP B 176      87.550  -0.067  -2.051  1.00 27.00           C  
-ATOM   4190  CZ2 TRP B 176      87.663  -1.267  -4.625  1.00 27.20           C  
-ATOM   4191  CZ3 TRP B 176      88.755  -0.525  -2.591  1.00 25.98           C  
-ATOM   4192  CH2 TRP B 176      88.797  -1.117  -3.863  1.00 24.60           C  
-ATOM   4193  N   GLU B 177      81.168   0.535  -2.705  1.00 22.41           N  
-ATOM   4194  CA  GLU B 177      80.180  -0.433  -3.150  1.00 23.87           C  
-ATOM   4195  C   GLU B 177      80.452  -0.860  -4.591  1.00 24.15           C  
-ATOM   4196  O   GLU B 177      79.955  -0.216  -5.522  1.00 23.19           O  
-ATOM   4197  CB  GLU B 177      78.776   0.174  -3.022  1.00 25.59           C  
-ATOM   4198  CG  GLU B 177      78.357   0.366  -1.577  1.00 29.34           C  
-ATOM   4199  CD  GLU B 177      78.736   1.707  -1.011  1.00 34.14           C  
-ATOM   4200  OE1 GLU B 177      79.200   1.762   0.160  1.00 36.84           O  
-ATOM   4201  OE2 GLU B 177      78.556   2.717  -1.729  1.00 36.38           O  
-ATOM   4202  N   TYR B 178      81.214  -1.938  -4.801  1.00 23.81           N  
-ATOM   4203  CA  TYR B 178      81.848  -2.765  -3.763  1.00 25.99           C  
-ATOM   4204  C   TYR B 178      83.100  -3.394  -4.380  1.00 27.31           C  
-ATOM   4205  O   TYR B 178      83.228  -3.467  -5.605  1.00 29.21           O  
-ATOM   4206  CB  TYR B 178      80.962  -3.955  -3.335  1.00 28.30           C  
-ATOM   4207  CG  TYR B 178      79.528  -3.636  -2.994  1.00 29.67           C  
-ATOM   4208  CD1 TYR B 178      78.563  -3.548  -3.997  1.00 29.84           C  
-ATOM   4209  CD2 TYR B 178      79.133  -3.418  -1.665  1.00 28.53           C  
-ATOM   4210  CE1 TYR B 178      77.223  -3.249  -3.693  1.00 32.48           C  
-ATOM   4211  CE2 TYR B 178      77.793  -3.112  -1.346  1.00 31.38           C  
-ATOM   4212  CZ  TYR B 178      76.848  -3.035  -2.370  1.00 31.61           C  
-ATOM   4213  OH  TYR B 178      75.529  -2.776  -2.080  1.00 36.70           O  
-ATOM   4214  N   PRO B 179      84.037  -3.861  -3.540  1.00 27.68           N  
-ATOM   4215  CA  PRO B 179      85.252  -4.495  -4.063  1.00 27.65           C  
-ATOM   4216  C   PRO B 179      84.769  -5.672  -4.906  1.00 29.10           C  
-ATOM   4217  O   PRO B 179      83.963  -6.485  -4.437  1.00 29.23           O  
-ATOM   4218  CB  PRO B 179      85.963  -4.932  -2.793  1.00 29.59           C  
-ATOM   4219  CG  PRO B 179      85.630  -3.797  -1.849  1.00 27.22           C  
-ATOM   4220  CD  PRO B 179      84.148  -3.630  -2.087  1.00 26.46           C  
-ATOM   4221  N   GLU B 180      85.242  -5.760  -6.145  1.00 29.16           N  
-ATOM   4222  CA  GLU B 180      84.784  -6.813  -7.052  1.00 32.52           C  
-ATOM   4223  C   GLU B 180      85.630  -8.079  -7.116  1.00 33.80           C  
-ATOM   4224  O   GLU B 180      85.152  -9.125  -7.562  1.00 35.93           O  
-ATOM   4225  CB  GLU B 180      84.642  -6.243  -8.460  1.00 35.36           C  
-ATOM   4226  CG  GLU B 180      83.776  -4.997  -8.517  1.00 42.29           C  
-ATOM   4227  CD  GLU B 180      83.853  -4.277  -9.857  1.00 46.00           C  
-ATOM   4228  OE1 GLU B 180      84.978  -3.976 -10.339  1.00 51.09           O  
-ATOM   4229  OE2 GLU B 180      82.779  -3.993 -10.419  1.00 50.11           O  
-ATOM   4230  N   ASN B 181      86.876  -7.994  -6.676  1.00 33.42           N  
-ATOM   4231  CA  ASN B 181      87.751  -9.159  -6.712  1.00 34.89           C  
-ATOM   4232  C   ASN B 181      88.735  -9.165  -5.567  1.00 34.09           C  
-ATOM   4233  O   ASN B 181      88.828  -8.203  -4.793  1.00 33.44           O  
-ATOM   4234  CB  ASN B 181      88.527  -9.220  -8.030  1.00 33.75           C  
-ATOM   4235  CG  ASN B 181      89.260  -7.937  -8.328  1.00 33.50           C  
-ATOM   4236  OD1 ASN B 181      89.902  -7.354  -7.454  1.00 36.51           O  
-ATOM   4237  ND2 ASN B 181      89.175  -7.488  -9.574  1.00 35.29           N  
-ATOM   4238  N   ASP B 182      89.480 -10.262  -5.483  1.00 35.06           N  
-ATOM   4239  CA  ASP B 182      90.470 -10.447  -4.440  1.00 34.80           C  
-ATOM   4240  C   ASP B 182      91.498  -9.329  -4.428  1.00 33.66           C  
-ATOM   4241  O   ASP B 182      91.878  -8.863  -3.360  1.00 32.33           O  
-ATOM   4242  CB  ASP B 182      91.168 -11.795  -4.611  1.00 38.22           C  
-ATOM   4243  CG  ASP B 182      92.014 -12.150  -3.417  1.00 40.88           C  
-ATOM   4244  OD1 ASP B 182      91.454 -12.208  -2.300  1.00 43.82           O  
-ATOM   4245  OD2 ASP B 182      93.232 -12.358  -3.581  1.00 44.40           O  
-ATOM   4246  N   GLN B 183      91.939  -8.890  -5.610  1.00 34.63           N  
-ATOM   4247  CA  GLN B 183      92.931  -7.810  -5.705  1.00 33.89           C  
-ATOM   4248  C   GLN B 183      92.387  -6.514  -5.100  1.00 33.30           C  
-ATOM   4249  O   GLN B 183      93.071  -5.819  -4.332  1.00 32.00           O  
-ATOM   4250  CB  GLN B 183      93.321  -7.557  -7.164  1.00 38.38           C  
-ATOM   4251  CG  GLN B 183      94.426  -6.501  -7.331  1.00 42.56           C  
-ATOM   4252  CD  GLN B 183      95.732  -6.900  -6.643  1.00 45.31           C  
-ATOM   4253  OE1 GLN B 183      96.337  -7.915  -6.984  1.00 46.91           O  
-ATOM   4254  NE2 GLN B 183      96.165  -6.100  -5.668  1.00 46.46           N  
-ATOM   4255  N   GLN B 184      91.155  -6.182  -5.468  1.00 30.19           N  
-ATOM   4256  CA  GLN B 184      90.502  -4.992  -4.936  1.00 27.98           C  
-ATOM   4257  C   GLN B 184      90.328  -5.161  -3.420  1.00 27.76           C  
-ATOM   4258  O   GLN B 184      90.524  -4.215  -2.647  1.00 25.82           O  
-ATOM   4259  CB  GLN B 184      89.136  -4.799  -5.617  1.00 27.07           C  
-ATOM   4260  CG  GLN B 184      89.253  -4.210  -7.022  1.00 26.74           C  
-ATOM   4261  CD  GLN B 184      87.926  -4.092  -7.750  1.00 30.90           C  
-ATOM   4262  OE1 GLN B 184      86.889  -3.780  -7.151  1.00 28.03           O  
-ATOM   4263  NE2 GLN B 184      87.956  -4.320  -9.058  1.00 29.70           N  
-ATOM   4264  N   ALA B 185      89.986  -6.376  -2.992  1.00 25.10           N  
-ATOM   4265  CA  ALA B 185      89.798  -6.633  -1.570  1.00 27.25           C  
-ATOM   4266  C   ALA B 185      91.107  -6.328  -0.825  1.00 29.17           C  
-ATOM   4267  O   ALA B 185      91.107  -5.679   0.229  1.00 27.84           O  
-ATOM   4268  CB  ALA B 185      89.360  -8.095  -1.361  1.00 25.29           C  
-ATOM   4269  N   ASN B 186      92.225  -6.782  -1.395  1.00 29.88           N  
-ATOM   4270  CA  ASN B 186      93.544  -6.538  -0.804  1.00 31.02           C  
-ATOM   4271  C   ASN B 186      93.877  -5.050  -0.807  1.00 29.70           C  
-ATOM   4272  O   ASN B 186      94.347  -4.495   0.188  1.00 28.02           O  
-ATOM   4273  CB  ASN B 186      94.621  -7.316  -1.581  1.00 32.77           C  
-ATOM   4274  CG  ASN B 186      94.665  -8.779  -1.194  1.00 36.16           C  
-ATOM   4275  OD1 ASN B 186      94.764  -9.097  -0.014  1.00 39.99           O  
-ATOM   4276  ND2 ASN B 186      94.589  -9.674  -2.177  1.00 36.43           N  
-ATOM   4277  N   ASP B 187      93.619  -4.396  -1.932  1.00 30.60           N  
-ATOM   4278  CA  ASP B 187      93.900  -2.974  -2.017  1.00 30.71           C  
-ATOM   4279  C   ASP B 187      93.101  -2.202  -0.987  1.00 29.71           C  
-ATOM   4280  O   ASP B 187      93.605  -1.242  -0.392  1.00 29.60           O  
-ATOM   4281  CB  ASP B 187      93.601  -2.463  -3.421  1.00 32.53           C  
-ATOM   4282  CG  ASP B 187      94.519  -3.083  -4.464  1.00 34.98           C  
-ATOM   4283  OD1 ASP B 187      95.567  -3.619  -4.059  1.00 34.80           O  
-ATOM   4284  OD2 ASP B 187      94.206  -3.026  -5.668  1.00 31.71           O  
-ATOM   4285  N   PHE B 188      91.859  -2.635  -0.762  1.00 28.17           N  
-ATOM   4286  CA  PHE B 188      90.997  -1.965   0.205  1.00 26.73           C  
-ATOM   4287  C   PHE B 188      91.664  -2.012   1.576  1.00 26.70           C  
-ATOM   4288  O   PHE B 188      91.717  -1.009   2.293  1.00 27.14           O  
-ATOM   4289  CB  PHE B 188      89.615  -2.650   0.258  1.00 25.90           C  
-ATOM   4290  CG  PHE B 188      88.538  -1.823   0.951  1.00 25.13           C  
-ATOM   4291  CD1 PHE B 188      88.824  -0.560   1.467  1.00 22.49           C  
-ATOM   4292  CD2 PHE B 188      87.239  -2.313   1.067  1.00 26.27           C  
-ATOM   4293  CE1 PHE B 188      87.834   0.214   2.095  1.00 26.58           C  
-ATOM   4294  CE2 PHE B 188      86.234  -1.557   1.690  1.00 27.00           C  
-ATOM   4295  CZ  PHE B 188      86.531  -0.290   2.206  1.00 24.17           C  
-ATOM   4296  N   VAL B 189      92.156  -3.191   1.944  1.00 26.92           N  
-ATOM   4297  CA  VAL B 189      92.846  -3.353   3.224  1.00 29.24           C  
-ATOM   4298  C   VAL B 189      94.073  -2.444   3.267  1.00 28.04           C  
-ATOM   4299  O   VAL B 189      94.300  -1.726   4.241  1.00 29.32           O  
-ATOM   4300  CB  VAL B 189      93.313  -4.802   3.433  1.00 29.78           C  
-ATOM   4301  CG1 VAL B 189      94.200  -4.893   4.688  1.00 28.92           C  
-ATOM   4302  CG2 VAL B 189      92.101  -5.709   3.561  1.00 30.83           C  
-ATOM   4303  N   LEU B 190      94.862  -2.470   2.198  1.00 29.36           N  
-ATOM   4304  CA  LEU B 190      96.053  -1.627   2.145  1.00 29.74           C  
-ATOM   4305  C   LEU B 190      95.627  -0.174   2.307  1.00 30.08           C  
-ATOM   4306  O   LEU B 190      96.241   0.588   3.052  1.00 29.20           O  
-ATOM   4307  CB  LEU B 190      96.782  -1.820   0.816  1.00 30.20           C  
-ATOM   4308  CG  LEU B 190      97.377  -3.213   0.592  1.00 34.58           C  
-ATOM   4309  CD1 LEU B 190      98.045  -3.278  -0.789  1.00 34.84           C  
-ATOM   4310  CD2 LEU B 190      98.386  -3.514   1.715  1.00 36.19           C  
-ATOM   4311  N   LEU B 191      94.551   0.202   1.621  1.00 29.51           N  
-ATOM   4312  CA  LEU B 191      94.063   1.575   1.705  1.00 28.89           C  
-ATOM   4313  C   LEU B 191      93.751   1.957   3.145  1.00 27.30           C  
-ATOM   4314  O   LEU B 191      94.181   3.000   3.633  1.00 30.36           O  
-ATOM   4315  CB  LEU B 191      92.804   1.755   0.835  1.00 29.23           C  
-ATOM   4316  CG  LEU B 191      92.143   3.143   0.911  1.00 27.95           C  
-ATOM   4317  CD1 LEU B 191      93.065   4.171   0.290  1.00 29.53           C  
-ATOM   4318  CD2 LEU B 191      90.806   3.134   0.180  1.00 29.58           C  
-ATOM   4319  N   LEU B 192      92.993   1.105   3.821  1.00 27.61           N  
-ATOM   4320  CA  LEU B 192      92.607   1.354   5.206  1.00 27.36           C  
-ATOM   4321  C   LEU B 192      93.841   1.522   6.096  1.00 26.22           C  
-ATOM   4322  O   LEU B 192      93.923   2.445   6.916  1.00 28.08           O  
-ATOM   4323  CB  LEU B 192      91.739   0.187   5.714  1.00 25.81           C  
-ATOM   4324  CG  LEU B 192      90.327   0.059   5.103  1.00 26.47           C  
-ATOM   4325  CD1 LEU B 192      89.603  -1.181   5.666  1.00 26.45           C  
-ATOM   4326  CD2 LEU B 192      89.527   1.328   5.422  1.00 23.12           C  
-ATOM   4327  N   LYS B 193      94.803   0.626   5.931  1.00 28.06           N  
-ATOM   4328  CA  LYS B 193      96.021   0.693   6.731  1.00 31.58           C  
-ATOM   4329  C   LYS B 193      96.672   2.065   6.545  1.00 30.75           C  
-ATOM   4330  O   LYS B 193      97.073   2.723   7.515  1.00 29.26           O  
-ATOM   4331  CB  LYS B 193      96.967  -0.425   6.294  1.00 35.77           C  
-ATOM   4332  CG  LYS B 193      98.367  -0.338   6.867  1.00 43.79           C  
-ATOM   4333  CD  LYS B 193      98.397  -0.543   8.375  1.00 49.03           C  
-ATOM   4334  CE  LYS B 193      99.834  -0.785   8.857  1.00 50.07           C  
-ATOM   4335  NZ  LYS B 193      99.904  -1.090  10.325  1.00 52.29           N  
-ATOM   4336  N   GLU B 194      96.733   2.503   5.290  1.00 29.79           N  
-ATOM   4337  CA  GLU B 194      97.327   3.795   4.940  1.00 30.66           C  
-ATOM   4338  C   GLU B 194      96.584   4.945   5.626  1.00 29.78           C  
-ATOM   4339  O   GLU B 194      97.190   5.880   6.153  1.00 28.83           O  
-ATOM   4340  CB  GLU B 194      97.282   3.958   3.413  1.00 33.47           C  
-ATOM   4341  CG  GLU B 194      98.507   4.576   2.785  1.00 37.78           C  
-ATOM   4342  CD  GLU B 194      99.794   3.875   3.206  1.00 38.51           C  
-ATOM   4343  OE1 GLU B 194     100.127   2.795   2.665  1.00 39.09           O  
-ATOM   4344  OE2 GLU B 194     100.452   4.420   4.105  1.00 39.28           O  
-ATOM   4345  N   VAL B 195      95.256   4.875   5.629  1.00 29.29           N  
-ATOM   4346  CA  VAL B 195      94.467   5.934   6.246  1.00 26.50           C  
-ATOM   4347  C   VAL B 195      94.615   5.929   7.760  1.00 26.32           C  
-ATOM   4348  O   VAL B 195      94.741   6.981   8.387  1.00 26.88           O  
-ATOM   4349  CB  VAL B 195      92.967   5.796   5.890  1.00 26.39           C  
-ATOM   4350  CG1 VAL B 195      92.180   6.888   6.595  1.00 23.99           C  
-ATOM   4351  CG2 VAL B 195      92.777   5.886   4.372  1.00 24.77           C  
-ATOM   4352  N   ARG B 196      94.588   4.730   8.341  1.00 28.24           N  
-ATOM   4353  CA  ARG B 196      94.729   4.560   9.786  1.00 29.70           C  
-ATOM   4354  C   ARG B 196      96.055   5.199  10.224  1.00 30.43           C  
-ATOM   4355  O   ARG B 196      96.113   5.975  11.191  1.00 30.20           O  
-ATOM   4356  CB  ARG B 196      94.715   3.058  10.117  1.00 31.30           C  
-ATOM   4357  CG  ARG B 196      94.779   2.717  11.597  1.00 31.78           C  
-ATOM   4358  CD  ARG B 196      93.558   3.218  12.344  1.00 32.10           C  
-ATOM   4359  NE  ARG B 196      93.739   4.554  12.902  1.00 29.56           N  
-ATOM   4360  CZ  ARG B 196      92.748   5.292  13.393  1.00 31.57           C  
-ATOM   4361  NH1 ARG B 196      91.497   4.826  13.387  1.00 32.94           N  
-ATOM   4362  NH2 ARG B 196      93.005   6.487  13.911  1.00 27.08           N  
-ATOM   4363  N   THR B 197      97.110   4.897   9.473  1.00 31.71           N  
-ATOM   4364  CA  THR B 197      98.434   5.429   9.778  1.00 33.64           C  
-ATOM   4365  C   THR B 197      98.421   6.939   9.711  1.00 34.12           C  
-ATOM   4366  O   THR B 197      98.928   7.617  10.605  1.00 32.06           O  
-ATOM   4367  CB  THR B 197      99.468   4.906   8.792  1.00 34.74           C  
-ATOM   4368  OG1 THR B 197      99.502   3.476   8.865  1.00 36.16           O  
-ATOM   4369  CG2 THR B 197     100.850   5.465   9.123  1.00 37.87           C  
-ATOM   4370  N   ALA B 198      97.825   7.468   8.646  1.00 33.53           N  
-ATOM   4371  CA  ALA B 198      97.756   8.907   8.480  1.00 32.33           C  
-ATOM   4372  C   ALA B 198      96.976   9.564   9.615  1.00 31.43           C  
-ATOM   4373  O   ALA B 198      97.388  10.597  10.132  1.00 32.57           O  
-ATOM   4374  CB  ALA B 198      97.131   9.255   7.115  1.00 32.87           C  
-ATOM   4375  N   LEU B 199      95.857   8.973  10.021  1.00 30.85           N  
-ATOM   4376  CA  LEU B 199      95.060   9.565  11.102  1.00 30.90           C  
-ATOM   4377  C   LEU B 199      95.845   9.630  12.416  1.00 31.07           C  
-ATOM   4378  O   LEU B 199      95.771  10.619  13.166  1.00 30.15           O  
-ATOM   4379  CB  LEU B 199      93.752   8.771  11.307  1.00 28.55           C  
-ATOM   4380  CG  LEU B 199      92.670   8.919  10.218  1.00 28.64           C  
-ATOM   4381  CD1 LEU B 199      91.643   7.785  10.353  1.00 26.12           C  
-ATOM   4382  CD2 LEU B 199      92.003  10.299  10.335  1.00 25.18           C  
-ATOM   4383  N   ASP B 200      96.602   8.579  12.694  1.00 33.13           N  
-ATOM   4384  CA  ASP B 200      97.388   8.550  13.926  1.00 36.00           C  
-ATOM   4385  C   ASP B 200      98.519   9.573  13.867  1.00 36.33           C  
-ATOM   4386  O   ASP B 200      98.708  10.349  14.807  1.00 38.16           O  
-ATOM   4387  CB  ASP B 200      97.924   7.144  14.164  1.00 37.47           C  
-ATOM   4388  CG  ASP B 200      96.815   6.146  14.366  1.00 39.46           C  
-ATOM   4389  OD1 ASP B 200      95.779   6.527  14.963  1.00 40.02           O  
-ATOM   4390  OD2 ASP B 200      96.976   4.986  13.938  1.00 41.56           O  
-ATOM   4391  N   SER B 201      99.244   9.595  12.754  1.00 36.28           N  
-ATOM   4392  CA  SER B 201     100.330  10.563  12.568  1.00 37.43           C  
-ATOM   4393  C   SER B 201      99.821  11.976  12.791  1.00 35.67           C  
-ATOM   4394  O   SER B 201     100.397  12.719  13.572  1.00 36.21           O  
-ATOM   4395  CB  SER B 201     100.896  10.449  11.161  1.00 40.01           C  
-ATOM   4396  OG  SER B 201     101.379   9.133  10.949  1.00 46.87           O  
-ATOM   4397  N   TYR B 202      98.742  12.352  12.102  1.00 32.85           N  
-ATOM   4398  CA  TYR B 202      98.162  13.681  12.275  1.00 31.19           C  
-ATOM   4399  C   TYR B 202      97.746  13.919  13.714  1.00 30.85           C  
-ATOM   4400  O   TYR B 202      97.856  15.025  14.236  1.00 32.39           O  
-ATOM   4401  CB  TYR B 202      96.905  13.861  11.395  1.00 32.42           C  
-ATOM   4402  CG  TYR B 202      96.067  15.068  11.797  1.00 29.61           C  
-ATOM   4403  CD1 TYR B 202      96.447  16.358  11.429  1.00 28.60           C  
-ATOM   4404  CD2 TYR B 202      94.961  14.928  12.635  1.00 25.67           C  
-ATOM   4405  CE1 TYR B 202      95.760  17.471  11.894  1.00 24.86           C  
-ATOM   4406  CE2 TYR B 202      94.266  16.034  13.099  1.00 26.32           C  
-ATOM   4407  CZ  TYR B 202      94.680  17.304  12.729  1.00 25.98           C  
-ATOM   4408  OH  TYR B 202      94.059  18.416  13.245  1.00 27.73           O  
-ATOM   4409  N   SER B 203      97.230  12.881  14.354  1.00 30.93           N  
-ATOM   4410  CA  SER B 203      96.765  13.023  15.728  1.00 32.42           C  
-ATOM   4411  C   SER B 203      97.908  13.247  16.709  1.00 32.98           C  
-ATOM   4412  O   SER B 203      97.821  14.080  17.608  1.00 31.76           O  
-ATOM   4413  CB  SER B 203      95.984  11.773  16.142  1.00 30.63           C  
-ATOM   4414  OG  SER B 203      95.634  11.846  17.509  1.00 30.76           O  
-ATOM   4415  N   ALA B 204      98.962  12.467  16.544  1.00 35.50           N  
-ATOM   4416  CA  ALA B 204     100.115  12.579  17.423  1.00 39.26           C  
-ATOM   4417  C   ALA B 204     100.657  14.001  17.327  1.00 40.92           C  
-ATOM   4418  O   ALA B 204     101.069  14.601  18.325  1.00 40.47           O  
-ATOM   4419  CB  ALA B 204     101.185  11.579  17.002  1.00 38.11           C  
-ATOM   4420  N   ALA B 205     100.607  14.542  16.114  1.00 42.49           N  
-ATOM   4421  CA  ALA B 205     101.115  15.869  15.846  1.00 42.31           C  
-ATOM   4422  C   ALA B 205     100.200  17.041  16.166  1.00 42.73           C  
-ATOM   4423  O   ALA B 205     100.686  18.105  16.547  1.00 41.90           O  
-ATOM   4424  CB  ALA B 205     101.561  15.948  14.384  1.00 40.98           C  
-ATOM   4425  N   ASN B 206      98.887  16.867  16.035  1.00 42.85           N  
-ATOM   4426  CA  ASN B 206      97.978  17.995  16.263  1.00 43.37           C  
-ATOM   4427  C   ASN B 206      96.712  17.701  17.046  1.00 44.14           C  
-ATOM   4428  O   ASN B 206      95.850  18.572  17.172  1.00 42.10           O  
-ATOM   4429  CB  ASN B 206      97.564  18.594  14.921  1.00 43.32           C  
-ATOM   4430  CG  ASN B 206      98.741  19.089  14.116  1.00 43.70           C  
-ATOM   4431  OD1 ASN B 206      99.302  20.140  14.407  1.00 46.07           O  
-ATOM   4432  ND2 ASN B 206      99.125  18.329  13.097  1.00 43.54           N  
-ATOM   4433  N   ALA B 207      96.583  16.488  17.566  1.00 44.61           N  
-ATOM   4434  CA  ALA B 207      95.380  16.150  18.310  1.00 46.19           C  
-ATOM   4435  C   ALA B 207      95.716  15.535  19.668  1.00 46.81           C  
-ATOM   4436  O   ALA B 207      94.851  14.972  20.342  1.00 45.83           O  
-ATOM   4437  CB  ALA B 207      94.506  15.199  17.479  1.00 45.73           C  
-ATOM   4438  N   GLY B 208      96.978  15.652  20.068  1.00 46.42           N  
-ATOM   4439  CA  GLY B 208      97.397  15.112  21.346  1.00 45.46           C  
-ATOM   4440  C   GLY B 208      97.017  13.654  21.522  1.00 45.24           C  
-ATOM   4441  O   GLY B 208      96.540  13.254  22.583  1.00 46.33           O  
-ATOM   4442  N   GLY B 209      97.216  12.851  20.484  1.00 43.51           N  
-ATOM   4443  CA  GLY B 209      96.888  11.444  20.586  1.00 41.82           C  
-ATOM   4444  C   GLY B 209      95.424  11.087  20.377  1.00 40.03           C  
-ATOM   4445  O   GLY B 209      95.103   9.907  20.278  1.00 39.37           O  
-ATOM   4446  N   GLN B 210      94.546  12.089  20.324  1.00 38.79           N  
-ATOM   4447  CA  GLN B 210      93.108  11.871  20.093  1.00 38.60           C  
-ATOM   4448  C   GLN B 210      92.897  10.725  19.097  1.00 35.79           C  
-ATOM   4449  O   GLN B 210      93.481  10.722  18.021  1.00 35.07           O  
-ATOM   4450  CB  GLN B 210      92.460  13.144  19.526  1.00 40.22           C  
-ATOM   4451  CG  GLN B 210      91.019  12.950  19.071  1.00 42.82           C  
-ATOM   4452  CD  GLN B 210      90.082  12.769  20.227  1.00 43.84           C  
-ATOM   4453  OE1 GLN B 210      90.472  12.235  21.261  1.00 48.97           O  
-ATOM   4454  NE2 GLN B 210      88.834  13.201  20.068  1.00 43.66           N  
-ATOM   4455  N   HIS B 211      92.056   9.761  19.451  1.00 33.52           N  
-ATOM   4456  CA  HIS B 211      91.836   8.654  18.542  1.00 33.41           C  
-ATOM   4457  C   HIS B 211      90.781   8.952  17.487  1.00 33.87           C  
-ATOM   4458  O   HIS B 211      89.592   8.999  17.808  1.00 32.49           O  
-ATOM   4459  CB  HIS B 211      91.404   7.404  19.292  1.00 31.12           C  
-ATOM   4460  CG  HIS B 211      91.041   6.263  18.393  1.00 32.90           C  
-ATOM   4461  ND1 HIS B 211      91.954   5.584  17.607  1.00 32.23           N  
-ATOM   4462  CD2 HIS B 211      89.847   5.685  18.160  1.00 31.23           C  
-ATOM   4463  CE1 HIS B 211      91.321   4.636  16.928  1.00 31.81           C  
-ATOM   4464  NE2 HIS B 211      90.040   4.683  17.245  1.00 32.12           N  
-ATOM   4465  N   PHE B 212      91.202   9.154  16.239  1.00 33.21           N  
-ATOM   4466  CA  PHE B 212      90.249   9.420  15.165  1.00 32.40           C  
-ATOM   4467  C   PHE B 212      89.683   8.114  14.636  1.00 32.39           C  
-ATOM   4468  O   PHE B 212      90.361   7.063  14.597  1.00 32.24           O  
-ATOM   4469  CB  PHE B 212      90.893  10.237  14.045  1.00 31.86           C  
-ATOM   4470  CG  PHE B 212      91.223  11.634  14.460  1.00 32.29           C  
-ATOM   4471  CD1 PHE B 212      90.217  12.495  14.904  1.00 29.86           C  
-ATOM   4472  CD2 PHE B 212      92.542  12.064  14.503  1.00 31.67           C  
-ATOM   4473  CE1 PHE B 212      90.528  13.760  15.393  1.00 32.36           C  
-ATOM   4474  CE2 PHE B 212      92.861  13.330  14.993  1.00 31.73           C  
-ATOM   4475  CZ  PHE B 212      91.867  14.174  15.436  1.00 30.38           C  
-ATOM   4476  N   LEU B 213      88.426   8.186  14.221  1.00 29.03           N  
-ATOM   4477  CA  LEU B 213      87.731   7.012  13.748  1.00 28.05           C  
-ATOM   4478  C   LEU B 213      87.904   6.702  12.275  1.00 29.13           C  
-ATOM   4479  O   LEU B 213      88.064   7.598  11.454  1.00 29.08           O  
-ATOM   4480  CB  LEU B 213      86.249   7.168  14.066  1.00 26.52           C  
-ATOM   4481  CG  LEU B 213      85.962   7.398  15.549  1.00 27.62           C  
-ATOM   4482  CD1 LEU B 213      84.508   7.871  15.736  1.00 25.36           C  
-ATOM   4483  CD2 LEU B 213      86.253   6.098  16.330  1.00 26.39           C  
-ATOM   4484  N   LEU B 214      87.882   5.413  11.961  1.00 27.47           N  
-ATOM   4485  CA  LEU B 214      87.963   4.925  10.594  1.00 26.17           C  
-ATOM   4486  C   LEU B 214      86.903   3.821  10.546  1.00 26.87           C  
-ATOM   4487  O   LEU B 214      87.002   2.837  11.277  1.00 25.70           O  
-ATOM   4488  CB  LEU B 214      89.345   4.340  10.281  1.00 27.80           C  
-ATOM   4489  CG  LEU B 214      89.518   3.785   8.854  1.00 28.28           C  
-ATOM   4490  CD1 LEU B 214      89.105   4.855   7.831  1.00 27.72           C  
-ATOM   4491  CD2 LEU B 214      90.968   3.354   8.622  1.00 28.18           C  
-ATOM   4492  N   THR B 215      85.883   4.011   9.709  1.00 25.72           N  
-ATOM   4493  CA  THR B 215      84.781   3.057   9.562  1.00 24.09           C  
-ATOM   4494  C   THR B 215      84.460   2.801   8.082  1.00 23.56           C  
-ATOM   4495  O   THR B 215      84.948   3.508   7.197  1.00 23.53           O  
-ATOM   4496  CB  THR B 215      83.493   3.618  10.198  1.00 25.35           C  
-ATOM   4497  OG1 THR B 215      83.073   4.781   9.462  1.00 21.71           O  
-ATOM   4498  CG2 THR B 215      83.729   4.018  11.647  1.00 21.06           C  
-ATOM   4499  N   VAL B 216      83.654   1.780   7.811  1.00 21.94           N  
-ATOM   4500  CA  VAL B 216      83.231   1.517   6.441  1.00 21.00           C  
-ATOM   4501  C   VAL B 216      81.758   1.110   6.413  1.00 21.99           C  
-ATOM   4502  O   VAL B 216      81.209   0.651   7.422  1.00 19.28           O  
-ATOM   4503  CB  VAL B 216      84.000   0.370   5.756  1.00 22.40           C  
-ATOM   4504  CG1 VAL B 216      85.487   0.730   5.574  1.00 23.26           C  
-ATOM   4505  CG2 VAL B 216      83.821  -0.924   6.558  1.00 24.03           C  
-ATOM   4506  N   ALA B 217      81.137   1.300   5.250  1.00 18.59           N  
-ATOM   4507  CA  ALA B 217      79.762   0.879   5.029  1.00 20.84           C  
-ATOM   4508  C   ALA B 217      80.009  -0.533   4.567  1.00 22.19           C  
-ATOM   4509  O   ALA B 217      80.938  -0.764   3.786  1.00 22.22           O  
-ATOM   4510  CB  ALA B 217      79.101   1.700   3.885  1.00 20.40           C  
-ATOM   4511  N   SER B 218      79.211  -1.488   5.029  1.00 22.04           N  
-ATOM   4512  CA  SER B 218      79.445  -2.849   4.611  1.00 22.42           C  
-ATOM   4513  C   SER B 218      78.225  -3.497   3.995  1.00 20.65           C  
-ATOM   4514  O   SER B 218      77.087  -3.244   4.394  1.00 20.35           O  
-ATOM   4515  CB  SER B 218      80.001  -3.670   5.785  1.00 24.91           C  
-ATOM   4516  OG  SER B 218      79.311  -3.383   6.977  1.00 28.96           O  
-ATOM   4517  N   PRO B 219      78.456  -4.367   3.006  1.00 21.33           N  
-ATOM   4518  CA  PRO B 219      77.386  -5.062   2.296  1.00 21.20           C  
-ATOM   4519  C   PRO B 219      76.641  -6.108   3.076  1.00 21.73           C  
-ATOM   4520  O   PRO B 219      77.197  -6.746   3.969  1.00 18.61           O  
-ATOM   4521  CB  PRO B 219      78.106  -5.686   1.112  1.00 21.56           C  
-ATOM   4522  CG  PRO B 219      79.421  -6.090   1.746  1.00 22.78           C  
-ATOM   4523  CD  PRO B 219      79.776  -4.832   2.547  1.00 22.92           C  
-ATOM   4524  N   ALA B 220      75.379  -6.296   2.696  1.00 19.72           N  
-ATOM   4525  CA  ALA B 220      74.555  -7.314   3.320  1.00 19.77           C  
-ATOM   4526  C   ALA B 220      74.457  -8.454   2.319  1.00 19.35           C  
-ATOM   4527  O   ALA B 220      74.027  -9.543   2.659  1.00 21.99           O  
-ATOM   4528  CB  ALA B 220      73.148  -6.765   3.646  1.00 19.27           C  
-ATOM   4529  N   GLY B 221      74.867  -8.211   1.078  1.00 19.59           N  
-ATOM   4530  CA  GLY B 221      74.786  -9.264   0.076  1.00 17.84           C  
-ATOM   4531  C   GLY B 221      75.875 -10.304   0.304  1.00 22.16           C  
-ATOM   4532  O   GLY B 221      77.046  -9.937   0.362  1.00 20.82           O  
-ATOM   4533  N   PRO B 222      75.524 -11.600   0.471  1.00 23.55           N  
-ATOM   4534  CA  PRO B 222      76.530 -12.640   0.692  1.00 24.89           C  
-ATOM   4535  C   PRO B 222      77.618 -12.620  -0.386  1.00 25.39           C  
-ATOM   4536  O   PRO B 222      78.793 -12.743  -0.067  1.00 23.08           O  
-ATOM   4537  CB  PRO B 222      75.702 -13.929   0.672  1.00 26.98           C  
-ATOM   4538  CG  PRO B 222      74.407 -13.475   1.336  1.00 27.74           C  
-ATOM   4539  CD  PRO B 222      74.163 -12.157   0.601  1.00 24.15           C  
-ATOM   4540  N   ASP B 223      77.229 -12.451  -1.648  1.00 26.02           N  
-ATOM   4541  CA  ASP B 223      78.213 -12.431  -2.732  1.00 31.53           C  
-ATOM   4542  C   ASP B 223      79.246 -11.332  -2.549  1.00 30.13           C  
-ATOM   4543  O   ASP B 223      80.414 -11.511  -2.873  1.00 32.20           O  
-ATOM   4544  CB  ASP B 223      77.540 -12.257  -4.097  1.00 36.67           C  
-ATOM   4545  CG  ASP B 223      76.769 -13.485  -4.527  1.00 42.63           C  
-ATOM   4546  OD1 ASP B 223      77.087 -14.598  -4.042  1.00 45.44           O  
-ATOM   4547  OD2 ASP B 223      75.851 -13.335  -5.363  1.00 47.10           O  
-ATOM   4548  N   LYS B 224      78.816 -10.195  -2.023  1.00 27.85           N  
-ATOM   4549  CA  LYS B 224      79.720  -9.071  -1.790  1.00 27.98           C  
-ATOM   4550  C   LYS B 224      80.597  -9.319  -0.577  1.00 26.52           C  
-ATOM   4551  O   LYS B 224      81.800  -9.070  -0.590  1.00 28.46           O  
-ATOM   4552  CB  LYS B 224      78.921  -7.789  -1.550  1.00 29.59           C  
-ATOM   4553  CG  LYS B 224      78.558  -7.028  -2.799  1.00 35.14           C  
-ATOM   4554  CD  LYS B 224      77.773  -7.846  -3.771  1.00 36.81           C  
-ATOM   4555  CE  LYS B 224      77.408  -7.005  -4.982  1.00 39.07           C  
-ATOM   4556  NZ  LYS B 224      76.572  -7.810  -5.904  1.00 41.44           N  
-ATOM   4557  N   ILE B 225      79.974  -9.800   0.485  1.00 25.81           N  
-ATOM   4558  CA  ILE B 225      80.691 -10.069   1.714  1.00 24.61           C  
-ATOM   4559  C   ILE B 225      81.845 -11.054   1.459  1.00 25.31           C  
-ATOM   4560  O   ILE B 225      82.933 -10.858   1.963  1.00 24.80           O  
-ATOM   4561  CB  ILE B 225      79.727 -10.669   2.782  1.00 25.14           C  
-ATOM   4562  CG1 ILE B 225      78.673  -9.618   3.175  1.00 21.17           C  
-ATOM   4563  CG2 ILE B 225      80.529 -11.096   4.028  1.00 24.17           C  
-ATOM   4564  CD1 ILE B 225      77.498 -10.177   3.984  1.00 22.11           C  
-ATOM   4565  N   LYS B 226      81.576 -12.107   0.691  1.00 26.47           N  
-ATOM   4566  CA  LYS B 226      82.570 -13.133   0.384  1.00 30.05           C  
-ATOM   4567  C   LYS B 226      83.869 -12.564  -0.181  1.00 31.35           C  
-ATOM   4568  O   LYS B 226      84.950 -13.117   0.053  1.00 32.93           O  
-ATOM   4569  CB  LYS B 226      82.029 -14.152  -0.630  1.00 32.72           C  
-ATOM   4570  CG  LYS B 226      80.694 -14.812  -0.283  1.00 41.59           C  
-ATOM   4571  CD  LYS B 226      80.727 -15.612   1.017  1.00 43.01           C  
-ATOM   4572  CE  LYS B 226      79.307 -15.995   1.475  1.00 43.71           C  
-ATOM   4573  NZ  LYS B 226      78.546 -16.844   0.508  1.00 42.25           N  
-ATOM   4574  N   VAL B 227      83.775 -11.473  -0.936  1.00 29.67           N  
-ATOM   4575  CA  VAL B 227      84.961 -10.863  -1.544  1.00 28.29           C  
-ATOM   4576  C   VAL B 227      85.869 -10.155  -0.530  1.00 27.59           C  
-ATOM   4577  O   VAL B 227      87.094 -10.136  -0.676  1.00 25.37           O  
-ATOM   4578  CB  VAL B 227      84.530  -9.855  -2.651  1.00 28.30           C  
-ATOM   4579  CG1 VAL B 227      85.748  -9.130  -3.248  1.00 31.44           C  
-ATOM   4580  CG2 VAL B 227      83.778 -10.592  -3.737  1.00 27.65           C  
-ATOM   4581  N   LEU B 228      85.271  -9.609   0.521  1.00 25.95           N  
-ATOM   4582  CA  LEU B 228      86.036  -8.874   1.508  1.00 26.70           C  
-ATOM   4583  C   LEU B 228      86.992  -9.721   2.366  1.00 29.07           C  
-ATOM   4584  O   LEU B 228      86.780 -10.922   2.572  1.00 27.51           O  
-ATOM   4585  CB  LEU B 228      85.081  -8.105   2.424  1.00 25.17           C  
-ATOM   4586  CG  LEU B 228      84.080  -7.134   1.773  1.00 24.88           C  
-ATOM   4587  CD1 LEU B 228      83.229  -6.478   2.849  1.00 24.50           C  
-ATOM   4588  CD2 LEU B 228      84.825  -6.069   0.996  1.00 22.19           C  
-ATOM   4589  N   HIS B 229      88.054  -9.077   2.840  1.00 28.69           N  
-ATOM   4590  CA  HIS B 229      89.018  -9.713   3.732  1.00 31.31           C  
-ATOM   4591  C   HIS B 229      88.649  -9.118   5.072  1.00 29.98           C  
-ATOM   4592  O   HIS B 229      89.233  -8.126   5.524  1.00 29.65           O  
-ATOM   4593  CB  HIS B 229      90.442  -9.342   3.334  1.00 32.73           C  
-ATOM   4594  CG  HIS B 229      90.862  -9.950   2.037  1.00 35.92           C  
-ATOM   4595  ND1 HIS B 229      92.118  -9.771   1.498  1.00 37.75           N  
-ATOM   4596  CD2 HIS B 229      90.200 -10.769   1.186  1.00 37.11           C  
-ATOM   4597  CE1 HIS B 229      92.211 -10.457   0.373  1.00 38.75           C  
-ATOM   4598  NE2 HIS B 229      91.061 -11.073   0.161  1.00 37.84           N  
-ATOM   4599  N   LEU B 230      87.648  -9.732   5.691  1.00 30.48           N  
-ATOM   4600  CA  LEU B 230      87.098  -9.245   6.946  1.00 29.79           C  
-ATOM   4601  C   LEU B 230      88.095  -9.017   8.059  1.00 30.26           C  
-ATOM   4602  O   LEU B 230      88.133  -7.931   8.646  1.00 31.43           O  
-ATOM   4603  CB  LEU B 230      85.983 -10.188   7.411  1.00 27.37           C  
-ATOM   4604  CG  LEU B 230      84.908 -10.412   6.338  1.00 30.47           C  
-ATOM   4605  CD1 LEU B 230      83.894 -11.466   6.828  1.00 27.97           C  
-ATOM   4606  CD2 LEU B 230      84.218  -9.070   5.996  1.00 26.94           C  
-ATOM   4607  N   LYS B 231      88.913 -10.025   8.350  1.00 30.19           N  
-ATOM   4608  CA  LYS B 231      89.882  -9.894   9.435  1.00 31.35           C  
-ATOM   4609  C   LYS B 231      90.867  -8.775   9.206  1.00 29.98           C  
-ATOM   4610  O   LYS B 231      91.046  -7.922  10.069  1.00 28.92           O  
-ATOM   4611  CB  LYS B 231      90.640 -11.206   9.654  1.00 35.68           C  
-ATOM   4612  CG  LYS B 231      89.778 -12.338  10.174  1.00 41.44           C  
-ATOM   4613  CD  LYS B 231      90.648 -13.513  10.631  1.00 47.13           C  
-ATOM   4614  CE  LYS B 231      89.836 -14.546  11.410  1.00 50.05           C  
-ATOM   4615  NZ  LYS B 231      90.707 -15.486  12.204  1.00 55.39           N  
-ATOM   4616  N   ASP B 232      91.513  -8.767   8.048  1.00 29.15           N  
-ATOM   4617  CA  ASP B 232      92.463  -7.701   7.776  1.00 30.39           C  
-ATOM   4618  C   ASP B 232      91.762  -6.356   7.849  1.00 29.37           C  
-ATOM   4619  O   ASP B 232      92.317  -5.382   8.347  1.00 29.52           O  
-ATOM   4620  CB  ASP B 232      93.093  -7.866   6.397  1.00 33.53           C  
-ATOM   4621  CG  ASP B 232      93.887  -9.159   6.267  1.00 36.85           C  
-ATOM   4622  OD1 ASP B 232      94.293  -9.723   7.314  1.00 35.22           O  
-ATOM   4623  OD2 ASP B 232      94.106  -9.594   5.114  1.00 36.60           O  
-ATOM   4624  N   MET B 233      90.530  -6.295   7.358  1.00 29.05           N  
-ATOM   4625  CA  MET B 233      89.817  -5.030   7.410  1.00 25.24           C  
-ATOM   4626  C   MET B 233      89.539  -4.631   8.837  1.00 23.86           C  
-ATOM   4627  O   MET B 233      89.847  -3.518   9.256  1.00 23.61           O  
-ATOM   4628  CB  MET B 233      88.496  -5.127   6.642  1.00 24.41           C  
-ATOM   4629  CG  MET B 233      88.670  -5.080   5.152  1.00 21.73           C  
-ATOM   4630  SD  MET B 233      87.092  -5.222   4.285  1.00 24.83           S  
-ATOM   4631  CE  MET B 233      86.387  -3.608   4.619  1.00 21.41           C  
-ATOM   4632  N   ASP B 234      88.974  -5.557   9.599  1.00 24.90           N  
-ATOM   4633  CA  ASP B 234      88.599  -5.251  10.973  1.00 27.95           C  
-ATOM   4634  C   ASP B 234      89.730  -4.714  11.822  1.00 28.64           C  
-ATOM   4635  O   ASP B 234      89.514  -3.929  12.745  1.00 26.73           O  
-ATOM   4636  CB  ASP B 234      87.991  -6.492  11.634  1.00 29.61           C  
-ATOM   4637  CG  ASP B 234      87.353  -6.186  12.976  1.00 31.97           C  
-ATOM   4638  OD1 ASP B 234      86.509  -5.257  13.064  1.00 31.87           O  
-ATOM   4639  OD2 ASP B 234      87.691  -6.885  13.954  1.00 36.79           O  
-ATOM   4640  N   GLN B 235      90.946  -5.133  11.495  1.00 31.61           N  
-ATOM   4641  CA  GLN B 235      92.114  -4.716  12.247  1.00 32.62           C  
-ATOM   4642  C   GLN B 235      92.330  -3.211  12.116  1.00 32.71           C  
-ATOM   4643  O   GLN B 235      92.929  -2.582  12.981  1.00 31.74           O  
-ATOM   4644  CB  GLN B 235      93.339  -5.501  11.748  1.00 39.16           C  
-ATOM   4645  CG  GLN B 235      94.549  -5.443  12.672  1.00 45.46           C  
-ATOM   4646  CD  GLN B 235      94.192  -5.757  14.128  1.00 49.50           C  
-ATOM   4647  OE1 GLN B 235      93.618  -6.815  14.434  1.00 52.36           O  
-ATOM   4648  NE2 GLN B 235      94.529  -4.836  15.030  1.00 51.51           N  
-ATOM   4649  N   GLN B 236      91.810  -2.624  11.045  1.00 31.65           N  
-ATOM   4650  CA  GLN B 236      91.983  -1.195  10.831  1.00 30.80           C  
-ATOM   4651  C   GLN B 236      90.748  -0.377  11.171  1.00 31.55           C  
-ATOM   4652  O   GLN B 236      90.790   0.860  11.127  1.00 29.55           O  
-ATOM   4653  CB  GLN B 236      92.315  -0.929   9.367  1.00 31.73           C  
-ATOM   4654  CG  GLN B 236      93.453  -1.751   8.804  1.00 32.31           C  
-ATOM   4655  CD  GLN B 236      94.733  -1.577   9.602  1.00 32.76           C  
-ATOM   4656  OE1 GLN B 236      95.094  -0.461   9.993  1.00 30.52           O  
-ATOM   4657  NE2 GLN B 236      95.427  -2.681   9.841  1.00 32.62           N  
-ATOM   4658  N   LEU B 237      89.659  -1.054  11.529  1.00 28.91           N  
-ATOM   4659  CA  LEU B 237      88.394  -0.360  11.763  1.00 28.71           C  
-ATOM   4660  C   LEU B 237      87.854  -0.224  13.173  1.00 28.77           C  
-ATOM   4661  O   LEU B 237      88.033  -1.106  14.019  1.00 27.01           O  
-ATOM   4662  CB  LEU B 237      87.315  -1.030  10.911  1.00 27.69           C  
-ATOM   4663  CG  LEU B 237      87.566  -1.043   9.397  1.00 29.01           C  
-ATOM   4664  CD1 LEU B 237      86.742  -2.142   8.721  1.00 25.61           C  
-ATOM   4665  CD2 LEU B 237      87.247   0.335   8.834  1.00 26.36           C  
-ATOM   4666  N   ASP B 238      87.173   0.897  13.402  1.00 27.08           N  
-ATOM   4667  CA  ASP B 238      86.515   1.157  14.665  1.00 26.64           C  
-ATOM   4668  C   ASP B 238      85.154   0.445  14.647  1.00 27.11           C  
-ATOM   4669  O   ASP B 238      84.658  -0.009  15.672  1.00 25.64           O  
-ATOM   4670  CB  ASP B 238      86.351   2.652  14.843  1.00 26.26           C  
-ATOM   4671  CG  ASP B 238      87.660   3.315  15.229  1.00 29.23           C  
-ATOM   4672  OD1 ASP B 238      88.036   3.221  16.418  1.00 26.09           O  
-ATOM   4673  OD2 ASP B 238      88.323   3.894  14.347  1.00 30.68           O  
-ATOM   4674  N   PHE B 239      84.542   0.371  13.472  1.00 26.71           N  
-ATOM   4675  CA  PHE B 239      83.273  -0.331  13.332  1.00 25.88           C  
-ATOM   4676  C   PHE B 239      82.783  -0.342  11.905  1.00 25.89           C  
-ATOM   4677  O   PHE B 239      83.297   0.384  11.042  1.00 23.26           O  
-ATOM   4678  CB  PHE B 239      82.204   0.193  14.314  1.00 25.00           C  
-ATOM   4679  CG  PHE B 239      81.848   1.643  14.163  1.00 27.01           C  
-ATOM   4680  CD1 PHE B 239      80.786   2.030  13.339  1.00 24.85           C  
-ATOM   4681  CD2 PHE B 239      82.493   2.617  14.937  1.00 24.67           C  
-ATOM   4682  CE1 PHE B 239      80.364   3.363  13.300  1.00 25.05           C  
-ATOM   4683  CE2 PHE B 239      82.083   3.957  14.909  1.00 24.48           C  
-ATOM   4684  CZ  PHE B 239      81.017   4.338  14.096  1.00 25.28           C  
-ATOM   4685  N   TRP B 240      81.817  -1.218  11.664  1.00 24.14           N  
-ATOM   4686  CA  TRP B 240      81.248  -1.421  10.347  1.00 25.00           C  
-ATOM   4687  C   TRP B 240      79.771  -1.041  10.358  1.00 23.05           C  
-ATOM   4688  O   TRP B 240      79.029  -1.464  11.233  1.00 21.73           O  
-ATOM   4689  CB  TRP B 240      81.349  -2.898   9.968  1.00 26.47           C  
-ATOM   4690  CG  TRP B 240      82.720  -3.542  10.100  1.00 26.21           C  
-ATOM   4691  CD1 TRP B 240      83.485  -3.637  11.235  1.00 25.90           C  
-ATOM   4692  CD2 TRP B 240      83.416  -4.278   9.086  1.00 25.38           C  
-ATOM   4693  NE1 TRP B 240      84.613  -4.401  10.984  1.00 25.73           N  
-ATOM   4694  CE2 TRP B 240      84.592  -4.803   9.675  1.00 26.18           C  
-ATOM   4695  CE3 TRP B 240      83.160  -4.550   7.735  1.00 26.24           C  
-ATOM   4696  CZ2 TRP B 240      85.507  -5.579   8.960  1.00 25.57           C  
-ATOM   4697  CZ3 TRP B 240      84.082  -5.330   7.022  1.00 25.23           C  
-ATOM   4698  CH2 TRP B 240      85.237  -5.830   7.642  1.00 24.83           C  
-ATOM   4699  N   ASN B 241      79.338  -0.249   9.388  1.00 22.11           N  
-ATOM   4700  CA  ASN B 241      77.918   0.115   9.323  1.00 20.58           C  
-ATOM   4701  C   ASN B 241      77.324  -0.777   8.257  1.00 19.29           C  
-ATOM   4702  O   ASN B 241      77.566  -0.587   7.071  1.00 20.60           O  
-ATOM   4703  CB  ASN B 241      77.792   1.592   8.970  1.00 20.50           C  
-ATOM   4704  CG  ASN B 241      78.409   2.465  10.040  1.00 24.72           C  
-ATOM   4705  OD1 ASN B 241      78.114   2.290  11.226  1.00 21.39           O  
-ATOM   4706  ND2 ASN B 241      79.271   3.394   9.642  1.00 21.28           N  
-ATOM   4707  N   LEU B 242      76.574  -1.786   8.688  1.00 21.03           N  
-ATOM   4708  CA  LEU B 242      75.975  -2.741   7.763  1.00 18.45           C  
-ATOM   4709  C   LEU B 242      74.764  -2.143   7.062  1.00 19.69           C  
-ATOM   4710  O   LEU B 242      73.808  -1.744   7.708  1.00 20.35           O  
-ATOM   4711  CB  LEU B 242      75.539  -3.995   8.516  1.00 19.83           C  
-ATOM   4712  CG  LEU B 242      74.897  -5.086   7.658  1.00 20.13           C  
-ATOM   4713  CD1 LEU B 242      75.892  -5.573   6.617  1.00 20.25           C  
-ATOM   4714  CD2 LEU B 242      74.486  -6.243   8.559  1.00 21.69           C  
-ATOM   4715  N   MET B 243      74.798  -2.132   5.740  1.00 17.35           N  
-ATOM   4716  CA  MET B 243      73.705  -1.581   4.960  1.00 18.71           C  
-ATOM   4717  C   MET B 243      72.634  -2.636   4.725  1.00 16.08           C  
-ATOM   4718  O   MET B 243      72.476  -3.177   3.631  1.00 15.65           O  
-ATOM   4719  CB  MET B 243      74.274  -1.034   3.653  1.00 18.17           C  
-ATOM   4720  CG  MET B 243      75.183   0.170   3.932  1.00 20.89           C  
-ATOM   4721  SD  MET B 243      75.854   0.827   2.397  1.00 27.47           S  
-ATOM   4722  CE  MET B 243      77.133  -0.483   1.964  1.00 27.25           C  
-ATOM   4723  N   ALA B 244      71.899  -2.896   5.800  1.00 17.47           N  
-ATOM   4724  CA  ALA B 244      70.838  -3.891   5.830  1.00 15.84           C  
-ATOM   4725  C   ALA B 244      69.559  -3.346   5.225  1.00 16.22           C  
-ATOM   4726  O   ALA B 244      68.533  -3.277   5.893  1.00 15.26           O  
-ATOM   4727  CB  ALA B 244      70.586  -4.319   7.266  1.00 15.29           C  
-ATOM   4728  N   TYR B 245      69.629  -2.930   3.967  1.00 14.92           N  
-ATOM   4729  CA  TYR B 245      68.454  -2.418   3.295  1.00 15.09           C  
-ATOM   4730  C   TYR B 245      68.669  -2.507   1.799  1.00 16.51           C  
-ATOM   4731  O   TYR B 245      69.723  -2.998   1.355  1.00 16.02           O  
-ATOM   4732  CB  TYR B 245      68.138  -0.997   3.778  1.00 15.14           C  
-ATOM   4733  CG  TYR B 245      69.342  -0.127   4.028  1.00 17.51           C  
-ATOM   4734  CD1 TYR B 245      70.122   0.337   2.975  1.00 18.67           C  
-ATOM   4735  CD2 TYR B 245      69.660   0.281   5.320  1.00 19.84           C  
-ATOM   4736  CE1 TYR B 245      71.199   1.207   3.200  1.00 20.70           C  
-ATOM   4737  CE2 TYR B 245      70.726   1.153   5.566  1.00 20.80           C  
-ATOM   4738  CZ  TYR B 245      71.490   1.612   4.501  1.00 24.51           C  
-ATOM   4739  OH  TYR B 245      72.538   2.479   4.752  1.00 23.95           O  
-ATOM   4740  N   ASP B 246      67.673  -2.063   1.026  1.00 15.18           N  
-ATOM   4741  CA  ASP B 246      67.709  -2.157  -0.440  1.00 15.86           C  
-ATOM   4742  C   ASP B 246      67.810  -3.604  -0.903  1.00 17.21           C  
-ATOM   4743  O   ASP B 246      68.429  -3.894  -1.933  1.00 16.49           O  
-ATOM   4744  CB  ASP B 246      68.883  -1.386  -1.045  1.00 19.73           C  
-ATOM   4745  CG  ASP B 246      68.830   0.093  -0.730  1.00 22.85           C  
-ATOM   4746  OD1 ASP B 246      67.715   0.642  -0.583  1.00 21.61           O  
-ATOM   4747  OD2 ASP B 246      69.909   0.696  -0.642  1.00 23.76           O  
-ATOM   4748  N   TYR B 247      67.201  -4.519  -0.153  1.00 16.32           N  
-ATOM   4749  CA  TYR B 247      67.215  -5.929  -0.545  1.00 15.64           C  
-ATOM   4750  C   TYR B 247      66.289  -6.178  -1.729  1.00 19.89           C  
-ATOM   4751  O   TYR B 247      66.380  -7.220  -2.385  1.00 19.83           O  
-ATOM   4752  CB  TYR B 247      66.741  -6.831   0.601  1.00 16.19           C  
-ATOM   4753  CG  TYR B 247      67.619  -6.836   1.827  1.00 13.12           C  
-ATOM   4754  CD1 TYR B 247      68.947  -6.445   1.767  1.00 16.05           C  
-ATOM   4755  CD2 TYR B 247      67.116  -7.265   3.052  1.00 14.72           C  
-ATOM   4756  CE1 TYR B 247      69.772  -6.484   2.927  1.00 16.82           C  
-ATOM   4757  CE2 TYR B 247      67.912  -7.310   4.192  1.00 15.24           C  
-ATOM   4758  CZ  TYR B 247      69.239  -6.921   4.130  1.00 17.72           C  
-ATOM   4759  OH  TYR B 247      70.003  -6.966   5.283  1.00 15.20           O  
-ATOM   4760  N   ALA B 248      65.365  -5.255  -1.969  1.00 17.31           N  
-ATOM   4761  CA  ALA B 248      64.434  -5.399  -3.082  1.00 19.77           C  
-ATOM   4762  C   ALA B 248      64.065  -4.013  -3.606  1.00 19.20           C  
-ATOM   4763  O   ALA B 248      64.006  -3.049  -2.851  1.00 19.40           O  
-ATOM   4764  CB  ALA B 248      63.160  -6.158  -2.639  1.00 19.13           C  
-ATOM   4765  N   GLY B 249      63.827  -3.929  -4.908  1.00 20.08           N  
-ATOM   4766  CA  GLY B 249      63.476  -2.671  -5.535  1.00 17.27           C  
-ATOM   4767  C   GLY B 249      63.276  -2.887  -7.017  1.00 19.28           C  
-ATOM   4768  O   GLY B 249      63.008  -4.007  -7.463  1.00 17.34           O  
-ATOM   4769  N   SER B 250      63.439  -1.825  -7.799  1.00 20.50           N  
-ATOM   4770  CA  SER B 250      63.242  -1.913  -9.243  1.00 21.98           C  
-ATOM   4771  C   SER B 250      64.223  -2.888  -9.871  1.00 23.53           C  
-ATOM   4772  O   SER B 250      64.002  -3.385 -10.959  1.00 27.45           O  
-ATOM   4773  CB  SER B 250      63.411  -0.526  -9.872  1.00 23.08           C  
-ATOM   4774  OG  SER B 250      64.717  -0.051  -9.651  1.00 22.88           O  
-ATOM   4775  N   PHE B 251      65.315  -3.161  -9.178  1.00 25.19           N  
-ATOM   4776  CA  PHE B 251      66.310  -4.092  -9.689  1.00 23.73           C  
-ATOM   4777  C   PHE B 251      65.910  -5.549  -9.399  1.00 26.12           C  
-ATOM   4778  O   PHE B 251      66.610  -6.477  -9.797  1.00 26.38           O  
-ATOM   4779  CB  PHE B 251      67.653  -3.779  -9.035  1.00 25.44           C  
-ATOM   4780  CG  PHE B 251      67.547  -3.535  -7.558  1.00 24.60           C  
-ATOM   4781  CD1 PHE B 251      67.451  -4.600  -6.665  1.00 24.20           C  
-ATOM   4782  CD2 PHE B 251      67.466  -2.239  -7.067  1.00 24.21           C  
-ATOM   4783  CE1 PHE B 251      67.269  -4.373  -5.294  1.00 24.20           C  
-ATOM   4784  CE2 PHE B 251      67.288  -1.995  -5.700  1.00 24.45           C  
-ATOM   4785  CZ  PHE B 251      67.188  -3.065  -4.811  1.00 23.91           C  
-ATOM   4786  N   SER B 252      64.784  -5.747  -8.713  1.00 26.42           N  
-ATOM   4787  CA  SER B 252      64.329  -7.090  -8.359  1.00 24.76           C  
-ATOM   4788  C   SER B 252      63.343  -7.708  -9.342  1.00 25.14           C  
-ATOM   4789  O   SER B 252      62.511  -7.015  -9.924  1.00 24.90           O  
-ATOM   4790  CB  SER B 252      63.668  -7.068  -6.981  1.00 25.67           C  
-ATOM   4791  OG  SER B 252      64.468  -6.393  -6.037  1.00 24.73           O  
-ATOM   4792  N   SER B 253      63.413  -9.029  -9.500  1.00 27.56           N  
-ATOM   4793  CA  SER B 253      62.484  -9.720 -10.390  1.00 29.13           C  
-ATOM   4794  C   SER B 253      61.071  -9.627  -9.844  1.00 28.34           C  
-ATOM   4795  O   SER B 253      60.114  -9.551 -10.605  1.00 29.65           O  
-ATOM   4796  CB  SER B 253      62.863 -11.194 -10.523  1.00 30.38           C  
-ATOM   4797  OG  SER B 253      64.227 -11.311 -10.880  1.00 38.14           O  
-ATOM   4798  N   LEU B 254      60.931  -9.630  -8.522  1.00 25.87           N  
-ATOM   4799  CA  LEU B 254      59.598  -9.578  -7.918  1.00 24.47           C  
-ATOM   4800  C   LEU B 254      59.562  -8.591  -6.781  1.00 24.12           C  
-ATOM   4801  O   LEU B 254      60.615  -8.213  -6.262  1.00 24.33           O  
-ATOM   4802  CB  LEU B 254      59.226 -10.946  -7.343  1.00 25.61           C  
-ATOM   4803  CG  LEU B 254      59.304 -12.139  -8.298  1.00 28.22           C  
-ATOM   4804  CD1 LEU B 254      59.241 -13.449  -7.501  1.00 28.15           C  
-ATOM   4805  CD2 LEU B 254      58.164 -12.027  -9.316  1.00 26.92           C  
-ATOM   4806  N   SER B 255      58.355  -8.206  -6.368  1.00 23.07           N  
-ATOM   4807  CA  SER B 255      58.230  -7.284  -5.253  1.00 21.95           C  
-ATOM   4808  C   SER B 255      58.830  -8.002  -4.051  1.00 23.34           C  
-ATOM   4809  O   SER B 255      58.948  -9.225  -4.049  1.00 21.26           O  
-ATOM   4810  CB  SER B 255      56.765  -6.945  -4.984  1.00 23.94           C  
-ATOM   4811  OG  SER B 255      56.059  -8.090  -4.549  1.00 23.60           O  
-ATOM   4812  N   GLY B 256      59.217  -7.248  -3.028  1.00 22.78           N  
-ATOM   4813  CA  GLY B 256      59.812  -7.882  -1.866  1.00 20.30           C  
-ATOM   4814  C   GLY B 256      60.136  -6.921  -0.738  1.00 20.65           C  
-ATOM   4815  O   GLY B 256      59.998  -5.706  -0.892  1.00 19.96           O  
-ATOM   4816  N   HIS B 257      60.548  -7.469   0.397  1.00 17.47           N  
-ATOM   4817  CA  HIS B 257      60.922  -6.690   1.572  1.00 18.92           C  
-ATOM   4818  C   HIS B 257      62.357  -6.241   1.353  1.00 18.14           C  
-ATOM   4819  O   HIS B 257      63.199  -7.058   0.983  1.00 19.79           O  
-ATOM   4820  CB  HIS B 257      60.846  -7.590   2.796  1.00 18.38           C  
-ATOM   4821  CG  HIS B 257      59.499  -8.202   3.002  1.00 19.74           C  
-ATOM   4822  ND1 HIS B 257      58.372  -7.469   3.324  1.00 18.77           N  
-ATOM   4823  CD2 HIS B 257      59.077  -9.465   2.808  1.00 18.87           C  
-ATOM   4824  CE1 HIS B 257      57.314  -8.263   3.295  1.00 20.76           C  
-ATOM   4825  NE2 HIS B 257      57.715  -9.478   2.978  1.00 19.37           N  
-ATOM   4826  N   GLN B 258      62.633  -4.963   1.595  1.00 16.96           N  
-ATOM   4827  CA  GLN B 258      63.981  -4.435   1.360  1.00 16.78           C  
-ATOM   4828  C   GLN B 258      64.907  -4.453   2.558  1.00 16.20           C  
-ATOM   4829  O   GLN B 258      66.073  -4.130   2.404  1.00 18.64           O  
-ATOM   4830  CB  GLN B 258      63.918  -2.964   0.894  1.00 15.16           C  
-ATOM   4831  CG  GLN B 258      63.425  -2.006   2.020  1.00 15.04           C  
-ATOM   4832  CD  GLN B 258      64.105  -0.612   1.979  1.00 19.19           C  
-ATOM   4833  OE1 GLN B 258      65.283  -0.500   1.666  1.00 16.37           O  
-ATOM   4834  NE2 GLN B 258      63.351   0.439   2.325  1.00 15.34           N  
-ATOM   4835  N   ALA B 259      64.416  -4.810   3.745  1.00 15.13           N  
-ATOM   4836  CA  ALA B 259      65.288  -4.751   4.922  1.00 13.86           C  
-ATOM   4837  C   ALA B 259      64.988  -5.761   6.027  1.00 14.80           C  
-ATOM   4838  O   ALA B 259      65.338  -5.552   7.192  1.00 14.20           O  
-ATOM   4839  CB  ALA B 259      65.239  -3.345   5.490  1.00 14.80           C  
-ATOM   4840  N   ASN B 260      64.355  -6.861   5.647  1.00 15.85           N  
-ATOM   4841  CA  ASN B 260      63.957  -7.897   6.602  1.00 17.73           C  
-ATOM   4842  C   ASN B 260      65.127  -8.564   7.302  1.00 16.49           C  
-ATOM   4843  O   ASN B 260      66.198  -8.768   6.718  1.00 17.65           O  
-ATOM   4844  CB  ASN B 260      63.135  -8.951   5.865  1.00 15.64           C  
-ATOM   4845  CG  ASN B 260      63.901  -9.545   4.703  1.00 19.67           C  
-ATOM   4846  OD1 ASN B 260      64.099  -8.889   3.666  1.00 18.65           O  
-ATOM   4847  ND2 ASN B 260      64.373 -10.775   4.876  1.00 15.91           N  
-ATOM   4848  N   VAL B 261      64.912  -8.934   8.554  1.00 16.09           N  
-ATOM   4849  CA  VAL B 261      65.965  -9.587   9.318  1.00 16.24           C  
-ATOM   4850  C   VAL B 261      66.122 -11.076   9.027  1.00 17.46           C  
-ATOM   4851  O   VAL B 261      67.242 -11.571   8.877  1.00 15.79           O  
-ATOM   4852  CB  VAL B 261      65.727  -9.371  10.828  1.00 17.87           C  
-ATOM   4853  CG1 VAL B 261      66.727 -10.183  11.656  1.00 15.82           C  
-ATOM   4854  CG2 VAL B 261      65.889  -7.882  11.158  1.00 14.19           C  
-ATOM   4855  N   TYR B 262      64.997 -11.779   8.930  1.00 17.70           N  
-ATOM   4856  CA  TYR B 262      64.990 -13.216   8.702  1.00 18.74           C  
-ATOM   4857  C   TYR B 262      64.348 -13.583   7.370  1.00 19.92           C  
-ATOM   4858  O   TYR B 262      63.597 -12.800   6.802  1.00 18.00           O  
-ATOM   4859  CB  TYR B 262      64.196 -13.883   9.829  1.00 17.48           C  
-ATOM   4860  CG  TYR B 262      64.802 -13.659  11.193  1.00 15.94           C  
-ATOM   4861  CD1 TYR B 262      66.000 -14.264  11.539  1.00 13.62           C  
-ATOM   4862  CD2 TYR B 262      64.168 -12.855  12.146  1.00 17.21           C  
-ATOM   4863  CE1 TYR B 262      66.567 -14.090  12.812  1.00 14.09           C  
-ATOM   4864  CE2 TYR B 262      64.719 -12.660  13.415  1.00 14.24           C  
-ATOM   4865  CZ  TYR B 262      65.918 -13.287  13.742  1.00 14.72           C  
-ATOM   4866  OH  TYR B 262      66.463 -13.116  14.999  1.00 14.92           O  
-ATOM   4867  N   ASN B 263      64.656 -14.789   6.898  1.00 19.28           N  
-ATOM   4868  CA  ASN B 263      64.091 -15.277   5.640  1.00 21.62           C  
-ATOM   4869  C   ASN B 263      62.614 -15.614   5.868  1.00 22.27           C  
-ATOM   4870  O   ASN B 263      62.227 -16.098   6.941  1.00 21.69           O  
-ATOM   4871  CB  ASN B 263      64.875 -16.499   5.163  1.00 23.38           C  
-ATOM   4872  CG  ASN B 263      64.332 -17.084   3.879  1.00 26.31           C  
-ATOM   4873  OD1 ASN B 263      63.832 -18.237   3.899  1.00 26.45           O  
-ATOM   4874  ND2 ASN B 263      64.390 -16.356   2.798  1.00 23.96           N  
-ATOM   4875  N   ASP B 264      61.768 -15.332   4.888  1.00 22.51           N  
-ATOM   4876  CA  ASP B 264      60.346 -15.618   5.042  1.00 22.33           C  
-ATOM   4877  C   ASP B 264      60.117 -17.011   4.468  1.00 25.02           C  
-ATOM   4878  O   ASP B 264      59.840 -17.164   3.273  1.00 22.23           O  
-ATOM   4879  CB  ASP B 264      59.490 -14.596   4.277  1.00 24.18           C  
-ATOM   4880  CG  ASP B 264      58.012 -14.757   4.581  1.00 26.66           C  
-ATOM   4881  OD1 ASP B 264      57.649 -15.849   5.073  1.00 27.80           O  
-ATOM   4882  OD2 ASP B 264      57.223 -13.821   4.330  1.00 26.56           O  
-ATOM   4883  N   THR B 265      60.244 -18.026   5.318  1.00 25.88           N  
-ATOM   4884  CA  THR B 265      60.073 -19.409   4.873  1.00 29.34           C  
-ATOM   4885  C   THR B 265      58.763 -19.685   4.126  1.00 28.52           C  
-ATOM   4886  O   THR B 265      58.750 -20.469   3.186  1.00 30.15           O  
-ATOM   4887  CB  THR B 265      60.164 -20.381   6.067  1.00 30.35           C  
-ATOM   4888  OG1 THR B 265      58.961 -20.297   6.842  1.00 35.52           O  
-ATOM   4889  CG2 THR B 265      61.302 -20.003   6.944  1.00 27.48           C  
-ATOM   4890  N   SER B 266      57.675 -19.047   4.541  1.00 28.49           N  
-ATOM   4891  CA  SER B 266      56.379 -19.248   3.897  1.00 31.36           C  
-ATOM   4892  C   SER B 266      56.239 -18.497   2.563  1.00 31.73           C  
-ATOM   4893  O   SER B 266      55.331 -18.769   1.772  1.00 29.83           O  
-ATOM   4894  CB  SER B 266      55.256 -18.795   4.830  1.00 32.48           C  
-ATOM   4895  OG  SER B 266      55.216 -17.378   4.909  1.00 38.28           O  
-ATOM   4896  N   ASN B 267      57.124 -17.541   2.312  1.00 30.25           N  
-ATOM   4897  CA  ASN B 267      57.039 -16.783   1.068  1.00 28.48           C  
-ATOM   4898  C   ASN B 267      58.433 -16.283   0.801  1.00 28.49           C  
-ATOM   4899  O   ASN B 267      58.687 -15.076   0.781  1.00 29.75           O  
-ATOM   4900  CB  ASN B 267      56.050 -15.631   1.235  1.00 27.51           C  
-ATOM   4901  CG  ASN B 267      55.909 -14.795  -0.017  1.00 28.89           C  
-ATOM   4902  OD1 ASN B 267      56.408 -15.158  -1.081  1.00 30.59           O  
-ATOM   4903  ND2 ASN B 267      55.230 -13.666   0.105  1.00 27.02           N  
-ATOM   4904  N   PRO B 268      59.365 -17.223   0.593  1.00 27.89           N  
-ATOM   4905  CA  PRO B 268      60.772 -16.931   0.333  1.00 26.08           C  
-ATOM   4906  C   PRO B 268      61.029 -15.975  -0.829  1.00 26.45           C  
-ATOM   4907  O   PRO B 268      62.044 -15.269  -0.833  1.00 26.01           O  
-ATOM   4908  CB  PRO B 268      61.381 -18.317   0.109  1.00 27.66           C  
-ATOM   4909  CG  PRO B 268      60.261 -19.083  -0.506  1.00 28.76           C  
-ATOM   4910  CD  PRO B 268      59.070 -18.646   0.330  1.00 29.49           C  
-ATOM   4911  N   LEU B 269      60.123 -15.930  -1.802  1.00 24.67           N  
-ATOM   4912  CA  LEU B 269      60.334 -15.041  -2.942  1.00 24.38           C  
-ATOM   4913  C   LEU B 269      60.267 -13.588  -2.526  1.00 23.38           C  
-ATOM   4914  O   LEU B 269      60.792 -12.726  -3.222  1.00 23.25           O  
-ATOM   4915  CB  LEU B 269      59.305 -15.302  -4.047  1.00 23.89           C  
-ATOM   4916  CG  LEU B 269      59.439 -16.628  -4.800  1.00 26.50           C  
-ATOM   4917  CD1 LEU B 269      58.279 -16.787  -5.774  1.00 29.37           C  
-ATOM   4918  CD2 LEU B 269      60.746 -16.676  -5.552  1.00 26.47           C  
-ATOM   4919  N   SER B 270      59.620 -13.317  -1.393  1.00 23.73           N  
-ATOM   4920  CA  SER B 270      59.488 -11.944  -0.904  1.00 18.89           C  
-ATOM   4921  C   SER B 270      60.710 -11.493  -0.129  1.00 19.69           C  
-ATOM   4922  O   SER B 270      60.831 -10.311   0.221  1.00 18.41           O  
-ATOM   4923  CB  SER B 270      58.274 -11.802   0.006  1.00 17.86           C  
-ATOM   4924  OG  SER B 270      58.531 -12.390   1.271  1.00 20.05           O  
-ATOM   4925  N   THR B 271      61.600 -12.433   0.180  1.00 19.05           N  
-ATOM   4926  CA  THR B 271      62.809 -12.093   0.916  1.00 16.53           C  
-ATOM   4927  C   THR B 271      64.058 -12.624   0.199  1.00 19.43           C  
-ATOM   4928  O   THR B 271      64.657 -13.611   0.631  1.00 18.85           O  
-ATOM   4929  CB  THR B 271      62.776 -12.658   2.376  1.00 19.46           C  
-ATOM   4930  OG1 THR B 271      62.602 -14.083   2.346  1.00 19.06           O  
-ATOM   4931  CG2 THR B 271      61.628 -12.025   3.182  1.00 17.73           C  
-ATOM   4932  N   PRO B 272      64.453 -11.980  -0.923  1.00 18.97           N  
-ATOM   4933  CA  PRO B 272      65.645 -12.421  -1.668  1.00 19.36           C  
-ATOM   4934  C   PRO B 272      66.905 -12.320  -0.804  1.00 21.05           C  
-ATOM   4935  O   PRO B 272      67.940 -12.924  -1.101  1.00 21.30           O  
-ATOM   4936  CB  PRO B 272      65.679 -11.477  -2.894  1.00 19.72           C  
-ATOM   4937  CG  PRO B 272      64.826 -10.245  -2.446  1.00 17.58           C  
-ATOM   4938  CD  PRO B 272      63.704 -10.953  -1.679  1.00 17.59           C  
-ATOM   4939  N   PHE B 273      66.822 -11.556   0.276  1.00 19.68           N  
-ATOM   4940  CA  PHE B 273      67.967 -11.425   1.173  1.00 19.35           C  
-ATOM   4941  C   PHE B 273      67.441 -11.359   2.602  1.00 18.31           C  
-ATOM   4942  O   PHE B 273      66.241 -11.201   2.825  1.00 19.07           O  
-ATOM   4943  CB  PHE B 273      68.729 -10.113   0.887  1.00 18.92           C  
-ATOM   4944  CG  PHE B 273      69.400 -10.060  -0.463  1.00 19.96           C  
-ATOM   4945  CD1 PHE B 273      68.753  -9.502  -1.563  1.00 21.62           C  
-ATOM   4946  CD2 PHE B 273      70.699 -10.540  -0.627  1.00 19.28           C  
-ATOM   4947  CE1 PHE B 273      69.388  -9.415  -2.815  1.00 22.77           C  
-ATOM   4948  CE2 PHE B 273      71.348 -10.464  -1.868  1.00 20.72           C  
-ATOM   4949  CZ  PHE B 273      70.693  -9.898  -2.970  1.00 23.14           C  
-ATOM   4950  N   ASN B 274      68.326 -11.495   3.573  1.00 16.95           N  
-ATOM   4951  CA  ASN B 274      67.905 -11.311   4.951  1.00 16.68           C  
-ATOM   4952  C   ASN B 274      69.147 -10.935   5.749  1.00 17.31           C  
-ATOM   4953  O   ASN B 274      70.247 -11.394   5.463  1.00 15.96           O  
-ATOM   4954  CB  ASN B 274      67.209 -12.559   5.500  1.00 20.39           C  
-ATOM   4955  CG  ASN B 274      68.164 -13.694   5.731  1.00 21.07           C  
-ATOM   4956  OD1 ASN B 274      68.884 -13.715   6.724  1.00 20.10           O  
-ATOM   4957  ND2 ASN B 274      68.193 -14.634   4.801  1.00 21.87           N  
-ATOM   4958  N   THR B 275      68.974 -10.071   6.737  1.00 17.42           N  
-ATOM   4959  CA  THR B 275      70.100  -9.603   7.525  1.00 17.31           C  
-ATOM   4960  C   THR B 275      70.803 -10.700   8.332  1.00 20.23           C  
-ATOM   4961  O   THR B 275      72.032 -10.699   8.446  1.00 20.07           O  
-ATOM   4962  CB  THR B 275      69.625  -8.473   8.461  1.00 16.40           C  
-ATOM   4963  OG1 THR B 275      69.037  -7.433   7.666  1.00 16.43           O  
-ATOM   4964  CG2 THR B 275      70.783  -7.887   9.256  1.00 18.91           C  
-ATOM   4965  N   GLN B 276      70.039 -11.635   8.885  1.00 18.47           N  
-ATOM   4966  CA  GLN B 276      70.659 -12.671   9.712  1.00 20.21           C  
-ATOM   4967  C   GLN B 276      71.789 -13.373   8.975  1.00 18.83           C  
-ATOM   4968  O   GLN B 276      72.849 -13.555   9.522  1.00 20.93           O  
-ATOM   4969  CB  GLN B 276      69.640 -13.718  10.171  1.00 20.30           C  
-ATOM   4970  CG  GLN B 276      70.269 -14.736  11.148  1.00 18.22           C  
-ATOM   4971  CD  GLN B 276      70.754 -14.078  12.427  1.00 17.13           C  
-ATOM   4972  OE1 GLN B 276      69.977 -13.433  13.133  1.00 17.70           O  
-ATOM   4973  NE2 GLN B 276      72.048 -14.238  12.739  1.00 15.42           N  
-ATOM   4974  N   THR B 277      71.543 -13.753   7.731  1.00 20.99           N  
-ATOM   4975  CA  THR B 277      72.544 -14.440   6.934  1.00 21.16           C  
-ATOM   4976  C   THR B 277      73.814 -13.607   6.869  1.00 21.86           C  
-ATOM   4977  O   THR B 277      74.911 -14.119   7.084  1.00 22.69           O  
-ATOM   4978  CB  THR B 277      71.986 -14.717   5.515  1.00 21.08           C  
-ATOM   4979  OG1 THR B 277      70.982 -15.736   5.606  1.00 19.13           O  
-ATOM   4980  CG2 THR B 277      73.085 -15.183   4.557  1.00 23.27           C  
-ATOM   4981  N   ALA B 278      73.668 -12.314   6.594  1.00 21.89           N  
-ATOM   4982  CA  ALA B 278      74.832 -11.433   6.502  1.00 19.32           C  
-ATOM   4983  C   ALA B 278      75.573 -11.366   7.840  1.00 21.77           C  
-ATOM   4984  O   ALA B 278      76.797 -11.492   7.892  1.00 23.18           O  
-ATOM   4985  CB  ALA B 278      74.407 -10.034   6.045  1.00 19.34           C  
-ATOM   4986  N   LEU B 279      74.846 -11.193   8.935  1.00 21.66           N  
-ATOM   4987  CA  LEU B 279      75.512 -11.133  10.224  1.00 21.81           C  
-ATOM   4988  C   LEU B 279      76.255 -12.438  10.541  1.00 23.01           C  
-ATOM   4989  O   LEU B 279      77.342 -12.411  11.126  1.00 24.83           O  
-ATOM   4990  CB  LEU B 279      74.494 -10.821  11.324  1.00 22.99           C  
-ATOM   4991  CG  LEU B 279      73.978  -9.371  11.273  1.00 25.48           C  
-ATOM   4992  CD1 LEU B 279      72.944  -9.142  12.377  1.00 22.55           C  
-ATOM   4993  CD2 LEU B 279      75.149  -8.408  11.439  1.00 24.58           C  
-ATOM   4994  N   ASP B 280      75.679 -13.573  10.157  1.00 21.60           N  
-ATOM   4995  CA  ASP B 280      76.350 -14.849  10.416  1.00 23.64           C  
-ATOM   4996  C   ASP B 280      77.673 -14.908   9.618  1.00 24.39           C  
-ATOM   4997  O   ASP B 280      78.677 -15.415  10.118  1.00 24.58           O  
-ATOM   4998  CB  ASP B 280      75.452 -16.024  10.031  1.00 23.43           C  
-ATOM   4999  CG  ASP B 280      74.399 -16.346  11.101  1.00 26.63           C  
-ATOM   5000  OD1 ASP B 280      74.425 -15.733  12.192  1.00 23.57           O  
-ATOM   5001  OD2 ASP B 280      73.561 -17.246  10.840  1.00 27.95           O  
-ATOM   5002  N   LEU B 281      77.677 -14.389   8.390  1.00 23.82           N  
-ATOM   5003  CA  LEU B 281      78.905 -14.383   7.588  1.00 24.40           C  
-ATOM   5004  C   LEU B 281      79.955 -13.470   8.222  1.00 24.70           C  
-ATOM   5005  O   LEU B 281      81.140 -13.804   8.245  1.00 25.08           O  
-ATOM   5006  CB  LEU B 281      78.624 -13.926   6.161  1.00 23.15           C  
-ATOM   5007  CG  LEU B 281      77.843 -14.948   5.349  1.00 25.97           C  
-ATOM   5008  CD1 LEU B 281      77.382 -14.309   4.055  1.00 24.29           C  
-ATOM   5009  CD2 LEU B 281      78.728 -16.178   5.081  1.00 26.64           C  
-ATOM   5010  N   TYR B 282      79.537 -12.315   8.736  1.00 24.14           N  
-ATOM   5011  CA  TYR B 282      80.494 -11.414   9.377  1.00 23.78           C  
-ATOM   5012  C   TYR B 282      81.044 -12.018  10.670  1.00 25.22           C  
-ATOM   5013  O   TYR B 282      82.239 -11.917  10.954  1.00 23.50           O  
-ATOM   5014  CB  TYR B 282      79.865 -10.054   9.706  1.00 24.82           C  
-ATOM   5015  CG  TYR B 282      79.759  -9.119   8.520  1.00 25.44           C  
-ATOM   5016  CD1 TYR B 282      78.562  -8.975   7.820  1.00 22.98           C  
-ATOM   5017  CD2 TYR B 282      80.875  -8.401   8.074  1.00 24.60           C  
-ATOM   5018  CE1 TYR B 282      78.477  -8.138   6.700  1.00 22.66           C  
-ATOM   5019  CE2 TYR B 282      80.802  -7.566   6.962  1.00 24.81           C  
-ATOM   5020  CZ  TYR B 282      79.593  -7.437   6.278  1.00 25.42           C  
-ATOM   5021  OH  TYR B 282      79.510  -6.591   5.190  1.00 25.82           O  
-ATOM   5022  N   ARG B 283      80.178 -12.644  11.459  1.00 23.34           N  
-ATOM   5023  CA  ARG B 283      80.642 -13.220  12.710  1.00 26.89           C  
-ATOM   5024  C   ARG B 283      81.561 -14.419  12.455  1.00 27.76           C  
-ATOM   5025  O   ARG B 283      82.583 -14.554  13.115  1.00 27.79           O  
-ATOM   5026  CB  ARG B 283      79.455 -13.608  13.593  1.00 27.84           C  
-ATOM   5027  CG  ARG B 283      78.650 -12.387  14.078  1.00 33.54           C  
-ATOM   5028  CD  ARG B 283      77.829 -12.717  15.335  1.00 41.86           C  
-ATOM   5029  NE  ARG B 283      76.728 -13.659  15.106  1.00 46.43           N  
-ATOM   5030  CZ  ARG B 283      76.388 -14.663  15.922  1.00 45.86           C  
-ATOM   5031  NH1 ARG B 283      77.059 -14.906  17.048  1.00 44.61           N  
-ATOM   5032  NH2 ARG B 283      75.342 -15.409  15.617  1.00 46.03           N  
-ATOM   5033  N   ALA B 284      81.198 -15.264  11.490  1.00 26.90           N  
-ATOM   5034  CA  ALA B 284      81.994 -16.427  11.144  1.00 29.12           C  
-ATOM   5035  C   ALA B 284      83.323 -15.961  10.556  1.00 31.74           C  
-ATOM   5036  O   ALA B 284      84.334 -16.672  10.628  1.00 31.48           O  
-ATOM   5037  CB  ALA B 284      81.268 -17.280  10.133  1.00 24.48           C  
-ATOM   5038  N   GLY B 285      83.312 -14.765   9.971  1.00 30.41           N  
-ATOM   5039  CA  GLY B 285      84.513 -14.210   9.375  1.00 30.15           C  
-ATOM   5040  C   GLY B 285      85.401 -13.582  10.428  1.00 31.34           C  
-ATOM   5041  O   GLY B 285      86.488 -13.106  10.117  1.00 33.05           O  
-ATOM   5042  N   GLY B 286      84.940 -13.547  11.674  1.00 29.89           N  
-ATOM   5043  CA  GLY B 286      85.787 -12.993  12.712  1.00 29.79           C  
-ATOM   5044  C   GLY B 286      85.526 -11.581  13.174  1.00 31.33           C  
-ATOM   5045  O   GLY B 286      86.239 -11.076  14.042  1.00 32.04           O  
-ATOM   5046  N   VAL B 287      84.514 -10.928  12.613  1.00 28.92           N  
-ATOM   5047  CA  VAL B 287      84.215  -9.571  13.032  1.00 26.87           C  
-ATOM   5048  C   VAL B 287      83.379  -9.618  14.307  1.00 26.80           C  
-ATOM   5049  O   VAL B 287      82.354 -10.288  14.349  1.00 27.19           O  
-ATOM   5050  CB  VAL B 287      83.445  -8.814  11.937  1.00 27.99           C  
-ATOM   5051  CG1 VAL B 287      83.075  -7.436  12.447  1.00 24.83           C  
-ATOM   5052  CG2 VAL B 287      84.299  -8.733  10.670  1.00 25.97           C  
-ATOM   5053  N   PRO B 288      83.819  -8.910  15.364  1.00 28.10           N  
-ATOM   5054  CA  PRO B 288      83.106  -8.874  16.646  1.00 28.36           C  
-ATOM   5055  C   PRO B 288      81.698  -8.291  16.447  1.00 29.02           C  
-ATOM   5056  O   PRO B 288      81.525  -7.310  15.722  1.00 27.44           O  
-ATOM   5057  CB  PRO B 288      83.977  -7.961  17.510  1.00 30.30           C  
-ATOM   5058  CG  PRO B 288      85.360  -8.094  16.890  1.00 32.77           C  
-ATOM   5059  CD  PRO B 288      85.038  -8.089  15.412  1.00 29.75           C  
-ATOM   5060  N   ALA B 289      80.703  -8.884  17.094  1.00 27.14           N  
-ATOM   5061  CA  ALA B 289      79.336  -8.393  16.970  1.00 25.88           C  
-ATOM   5062  C   ALA B 289      79.242  -6.927  17.338  1.00 24.72           C  
-ATOM   5063  O   ALA B 289      78.590  -6.164  16.640  1.00 24.59           O  
-ATOM   5064  CB  ALA B 289      78.400  -9.187  17.861  1.00 24.80           C  
-ATOM   5065  N   ASN B 290      79.901  -6.525  18.423  1.00 22.08           N  
-ATOM   5066  CA  ASN B 290      79.798  -5.142  18.864  1.00 22.04           C  
-ATOM   5067  C   ASN B 290      80.501  -4.112  18.008  1.00 18.44           C  
-ATOM   5068  O   ASN B 290      80.575  -2.943  18.384  1.00 20.29           O  
-ATOM   5069  CB  ASN B 290      80.228  -4.990  20.330  1.00 24.83           C  
-ATOM   5070  CG  ASN B 290      81.698  -5.277  20.548  1.00 27.88           C  
-ATOM   5071  OD1 ASN B 290      82.140  -5.428  21.689  1.00 33.82           O  
-ATOM   5072  ND2 ASN B 290      82.460  -5.357  19.469  1.00 25.57           N  
-ATOM   5073  N   LYS B 291      81.032  -4.543  16.873  1.00 19.83           N  
-ATOM   5074  CA  LYS B 291      81.668  -3.620  15.924  1.00 21.36           C  
-ATOM   5075  C   LYS B 291      80.798  -3.509  14.663  1.00 23.54           C  
-ATOM   5076  O   LYS B 291      81.162  -2.823  13.695  1.00 23.95           O  
-ATOM   5077  CB  LYS B 291      83.080  -4.110  15.538  1.00 21.92           C  
-ATOM   5078  CG  LYS B 291      84.081  -3.958  16.691  1.00 26.59           C  
-ATOM   5079  CD  LYS B 291      85.514  -4.304  16.283  1.00 25.90           C  
-ATOM   5080  CE  LYS B 291      86.113  -3.191  15.438  1.00 28.01           C  
-ATOM   5081  NZ  LYS B 291      87.460  -3.520  14.912  1.00 24.44           N  
-ATOM   5082  N   ILE B 292      79.644  -4.181  14.677  1.00 21.47           N  
-ATOM   5083  CA  ILE B 292      78.734  -4.150  13.527  1.00 18.51           C  
-ATOM   5084  C   ILE B 292      77.502  -3.357  13.933  1.00 21.15           C  
-ATOM   5085  O   ILE B 292      76.778  -3.751  14.854  1.00 20.90           O  
-ATOM   5086  CB  ILE B 292      78.333  -5.571  13.109  1.00 20.37           C  
-ATOM   5087  CG1 ILE B 292      79.607  -6.431  12.973  1.00 19.50           C  
-ATOM   5088  CG2 ILE B 292      77.592  -5.548  11.745  1.00 15.69           C  
-ATOM   5089  CD1 ILE B 292      79.336  -7.850  12.560  1.00 22.10           C  
-ATOM   5090  N   VAL B 293      77.295  -2.221  13.261  1.00 18.77           N  
-ATOM   5091  CA  VAL B 293      76.164  -1.343  13.527  1.00 18.32           C  
-ATOM   5092  C   VAL B 293      75.067  -1.699  12.521  1.00 18.19           C  
-ATOM   5093  O   VAL B 293      75.335  -1.832  11.325  1.00 16.98           O  
-ATOM   5094  CB  VAL B 293      76.594   0.134  13.375  1.00 18.85           C  
-ATOM   5095  CG1 VAL B 293      75.408   1.049  13.611  1.00 16.72           C  
-ATOM   5096  CG2 VAL B 293      77.731   0.442  14.377  1.00 16.36           C  
-ATOM   5097  N   LEU B 294      73.838  -1.882  13.007  1.00 18.12           N  
-ATOM   5098  CA  LEU B 294      72.757  -2.285  12.118  1.00 17.55           C  
-ATOM   5099  C   LEU B 294      72.165  -1.117  11.342  1.00 16.69           C  
-ATOM   5100  O   LEU B 294      71.475  -0.289  11.910  1.00 16.33           O  
-ATOM   5101  CB  LEU B 294      71.622  -2.964  12.907  1.00 15.31           C  
-ATOM   5102  CG  LEU B 294      70.456  -3.483  12.071  1.00 16.24           C  
-ATOM   5103  CD1 LEU B 294      70.919  -4.565  11.085  1.00 14.91           C  
-ATOM   5104  CD2 LEU B 294      69.397  -4.037  13.018  1.00 15.69           C  
-ATOM   5105  N   GLY B 295      72.441  -1.074  10.052  1.00 17.35           N  
-ATOM   5106  CA  GLY B 295      71.872  -0.042   9.208  1.00 18.62           C  
-ATOM   5107  C   GLY B 295      70.377  -0.275   9.035  1.00 19.38           C  
-ATOM   5108  O   GLY B 295      69.923  -1.410   8.911  1.00 18.23           O  
-ATOM   5109  N   MET B 296      69.602   0.808   9.045  1.00 18.45           N  
-ATOM   5110  CA  MET B 296      68.164   0.711   8.864  1.00 16.20           C  
-ATOM   5111  C   MET B 296      67.716   1.847   7.952  1.00 17.25           C  
-ATOM   5112  O   MET B 296      68.239   2.973   8.019  1.00 16.65           O  
-ATOM   5113  CB  MET B 296      67.441   0.741  10.222  1.00 16.37           C  
-ATOM   5114  CG  MET B 296      67.625  -0.569  11.020  1.00 16.21           C  
-ATOM   5115  SD  MET B 296      67.024  -0.447  12.710  1.00 16.91           S  
-ATOM   5116  CE  MET B 296      68.247   0.616  13.438  1.00 16.55           C  
-ATOM   5117  N   PRO B 297      66.735   1.572   7.091  1.00 15.77           N  
-ATOM   5118  CA  PRO B 297      66.258   2.599   6.164  1.00 15.66           C  
-ATOM   5119  C   PRO B 297      65.224   3.552   6.717  1.00 17.30           C  
-ATOM   5120  O   PRO B 297      64.319   3.137   7.441  1.00 15.38           O  
-ATOM   5121  CB  PRO B 297      65.668   1.767   5.027  1.00 14.84           C  
-ATOM   5122  CG  PRO B 297      65.000   0.627   5.793  1.00 14.28           C  
-ATOM   5123  CD  PRO B 297      65.935   0.333   6.980  1.00 13.78           C  
-ATOM   5124  N   LEU B 298      65.361   4.832   6.377  1.00 17.33           N  
-ATOM   5125  CA  LEU B 298      64.348   5.806   6.773  1.00 15.80           C  
-ATOM   5126  C   LEU B 298      63.568   6.165   5.493  1.00 14.44           C  
-ATOM   5127  O   LEU B 298      63.196   7.314   5.264  1.00 14.80           O  
-ATOM   5128  CB  LEU B 298      65.006   7.037   7.386  1.00 16.24           C  
-ATOM   5129  CG  LEU B 298      65.669   6.784   8.745  1.00 16.36           C  
-ATOM   5130  CD1 LEU B 298      66.436   8.054   9.210  1.00 15.67           C  
-ATOM   5131  CD2 LEU B 298      64.599   6.416   9.765  1.00 13.82           C  
-ATOM   5132  N   TYR B 299      63.320   5.157   4.666  1.00 11.77           N  
-ATOM   5133  CA  TYR B 299      62.613   5.348   3.399  1.00 13.13           C  
-ATOM   5134  C   TYR B 299      62.023   4.019   2.992  1.00 15.57           C  
-ATOM   5135  O   TYR B 299      62.370   2.970   3.563  1.00 16.12           O  
-ATOM   5136  CB  TYR B 299      63.583   5.802   2.305  1.00 11.60           C  
-ATOM   5137  CG  TYR B 299      64.747   4.838   2.084  1.00 14.71           C  
-ATOM   5138  CD1 TYR B 299      65.922   4.929   2.837  1.00 16.45           C  
-ATOM   5139  CD2 TYR B 299      64.646   3.801   1.158  1.00 15.07           C  
-ATOM   5140  CE1 TYR B 299      66.970   3.996   2.672  1.00 14.09           C  
-ATOM   5141  CE2 TYR B 299      65.672   2.878   0.979  1.00 14.82           C  
-ATOM   5142  CZ  TYR B 299      66.830   2.982   1.734  1.00 16.84           C  
-ATOM   5143  OH  TYR B 299      67.864   2.113   1.475  1.00 20.47           O  
-ATOM   5144  N   GLY B 300      61.135   4.056   2.002  1.00 16.24           N  
-ATOM   5145  CA  GLY B 300      60.536   2.827   1.531  1.00 13.40           C  
-ATOM   5146  C   GLY B 300      60.765   2.645   0.049  1.00 16.22           C  
-ATOM   5147  O   GLY B 300      60.976   3.610  -0.705  1.00 13.97           O  
-ATOM   5148  N   ARG B 301      60.755   1.386  -0.364  1.00 15.99           N  
-ATOM   5149  CA  ARG B 301      60.908   1.028  -1.763  1.00 17.32           C  
-ATOM   5150  C   ARG B 301      59.535   0.536  -2.235  1.00 18.51           C  
-ATOM   5151  O   ARG B 301      58.962  -0.395  -1.634  1.00 16.04           O  
-ATOM   5152  CB  ARG B 301      61.940  -0.084  -1.893  1.00 20.99           C  
-ATOM   5153  CG  ARG B 301      63.373   0.385  -1.585  1.00 24.21           C  
-ATOM   5154  CD  ARG B 301      64.324   0.087  -2.740  1.00 23.89           C  
-ATOM   5155  NE  ARG B 301      65.616   0.716  -2.493  1.00 24.68           N  
-ATOM   5156  CZ  ARG B 301      66.215   1.541  -3.349  1.00 22.37           C  
-ATOM   5157  NH1 ARG B 301      65.648   1.821  -4.518  1.00 21.88           N  
-ATOM   5158  NH2 ARG B 301      67.352   2.119  -3.011  1.00 19.51           N  
-ATOM   5159  N   SER B 302      59.026   1.126  -3.316  1.00 15.96           N  
-ATOM   5160  CA  SER B 302      57.706   0.772  -3.822  1.00 18.04           C  
-ATOM   5161  C   SER B 302      57.664  -0.101  -5.071  1.00 20.70           C  
-ATOM   5162  O   SER B 302      58.623  -0.168  -5.857  1.00 20.65           O  
-ATOM   5163  CB  SER B 302      56.881   2.052  -4.066  1.00 18.05           C  
-ATOM   5164  OG  SER B 302      57.547   2.959  -4.947  1.00 17.18           O  
-ATOM   5165  N   PHE B 303      56.543  -0.802  -5.218  1.00 18.67           N  
-ATOM   5166  CA  PHE B 303      56.312  -1.674  -6.361  1.00 19.30           C  
-ATOM   5167  C   PHE B 303      54.863  -1.454  -6.764  1.00 20.76           C  
-ATOM   5168  O   PHE B 303      53.964  -1.546  -5.927  1.00 21.49           O  
-ATOM   5169  CB  PHE B 303      56.530  -3.146  -5.992  1.00 16.98           C  
-ATOM   5170  CG  PHE B 303      57.871  -3.423  -5.349  1.00 16.37           C  
-ATOM   5171  CD1 PHE B 303      58.034  -3.305  -3.974  1.00 16.05           C  
-ATOM   5172  CD2 PHE B 303      58.961  -3.798  -6.122  1.00 18.28           C  
-ATOM   5173  CE1 PHE B 303      59.268  -3.556  -3.366  1.00 14.66           C  
-ATOM   5174  CE2 PHE B 303      60.209  -4.052  -5.527  1.00 17.32           C  
-ATOM   5175  CZ  PHE B 303      60.354  -3.929  -4.145  1.00 15.95           C  
-ATOM   5176  N   ALA B 304      54.654  -1.124  -8.038  1.00 20.66           N  
-ATOM   5177  CA  ALA B 304      53.316  -0.873  -8.550  1.00 21.74           C  
-ATOM   5178  C   ALA B 304      52.750  -2.107  -9.219  1.00 21.07           C  
-ATOM   5179  O   ALA B 304      53.495  -2.993  -9.655  1.00 23.16           O  
-ATOM   5180  CB  ALA B 304      53.340   0.268  -9.573  1.00 21.01           C  
-ATOM   5181  N   ASN B 305      51.425  -2.126  -9.321  1.00 24.00           N  
-ATOM   5182  CA  ASN B 305      50.713  -3.202  -9.985  1.00 25.15           C  
-ATOM   5183  C   ASN B 305      51.151  -4.578  -9.479  1.00 25.31           C  
-ATOM   5184  O   ASN B 305      51.482  -5.460 -10.271  1.00 25.14           O  
-ATOM   5185  CB  ASN B 305      50.960  -3.106 -11.498  1.00 27.99           C  
-ATOM   5186  CG  ASN B 305      50.597  -1.739 -12.067  1.00 31.32           C  
-ATOM   5187  OD1 ASN B 305      49.452  -1.295 -11.961  1.00 33.16           O  
-ATOM   5188  ND2 ASN B 305      51.581  -1.057 -12.663  1.00 32.63           N  
-ATOM   5189  N   THR B 306      51.154  -4.760  -8.164  1.00 24.38           N  
-ATOM   5190  CA  THR B 306      51.568  -6.033  -7.607  1.00 24.49           C  
-ATOM   5191  C   THR B 306      50.487  -6.519  -6.664  1.00 24.42           C  
-ATOM   5192  O   THR B 306      49.788  -5.709  -6.037  1.00 23.72           O  
-ATOM   5193  CB  THR B 306      52.926  -5.896  -6.855  1.00 23.06           C  
-ATOM   5194  OG1 THR B 306      53.418  -7.195  -6.516  1.00 21.82           O  
-ATOM   5195  CG2 THR B 306      52.759  -5.060  -5.582  1.00 21.17           C  
-ATOM   5196  N   ASP B 307      50.323  -7.835  -6.570  1.00 26.51           N  
-ATOM   5197  CA  ASP B 307      49.291  -8.388  -5.683  1.00 26.20           C  
-ATOM   5198  C   ASP B 307      49.749  -8.395  -4.247  1.00 25.77           C  
-ATOM   5199  O   ASP B 307      48.928  -8.425  -3.334  1.00 26.88           O  
-ATOM   5200  CB  ASP B 307      48.931  -9.818  -6.078  1.00 29.36           C  
-ATOM   5201  CG  ASP B 307      48.325  -9.898  -7.466  1.00 31.38           C  
-ATOM   5202  OD1 ASP B 307      47.496  -9.029  -7.800  1.00 29.95           O  
-ATOM   5203  OD2 ASP B 307      48.689 -10.830  -8.206  1.00 37.42           O  
-ATOM   5204  N   GLY B 308      51.064  -8.383  -4.050  1.00 24.55           N  
-ATOM   5205  CA  GLY B 308      51.594  -8.396  -2.705  1.00 22.22           C  
-ATOM   5206  C   GLY B 308      53.076  -8.705  -2.704  1.00 22.66           C  
-ATOM   5207  O   GLY B 308      53.709  -8.760  -3.765  1.00 23.36           O  
-ATOM   5208  N   PRO B 309      53.661  -8.940  -1.523  1.00 24.43           N  
-ATOM   5209  CA  PRO B 309      55.092  -9.237  -1.416  1.00 22.98           C  
-ATOM   5210  C   PRO B 309      55.466 -10.516  -2.109  1.00 24.25           C  
-ATOM   5211  O   PRO B 309      54.759 -11.520  -1.979  1.00 23.97           O  
-ATOM   5212  CB  PRO B 309      55.322  -9.347   0.088  1.00 24.35           C  
-ATOM   5213  CG  PRO B 309      54.213  -8.553   0.676  1.00 26.69           C  
-ATOM   5214  CD  PRO B 309      53.036  -8.893  -0.193  1.00 24.23           C  
-ATOM   5215  N   GLY B 310      56.591 -10.471  -2.818  1.00 21.41           N  
-ATOM   5216  CA  GLY B 310      57.099 -11.636  -3.520  1.00 22.66           C  
-ATOM   5217  C   GLY B 310      56.254 -11.996  -4.727  1.00 25.37           C  
-ATOM   5218  O   GLY B 310      56.119 -13.171  -5.078  1.00 24.60           O  
-ATOM   5219  N   LYS B 311      55.700 -10.980  -5.375  1.00 25.54           N  
-ATOM   5220  CA  LYS B 311      54.847 -11.192  -6.535  1.00 26.14           C  
-ATOM   5221  C   LYS B 311      55.270 -10.305  -7.684  1.00 27.46           C  
-ATOM   5222  O   LYS B 311      56.027  -9.345  -7.505  1.00 25.65           O  
-ATOM   5223  CB  LYS B 311      53.395 -10.864  -6.195  1.00 28.16           C  
-ATOM   5224  CG  LYS B 311      52.758 -11.759  -5.135  1.00 31.17           C  
-ATOM   5225  CD  LYS B 311      52.410 -13.125  -5.708  1.00 33.57           C  
-ATOM   5226  CE  LYS B 311      51.599 -13.943  -4.706  1.00 35.85           C  
-ATOM   5227  NZ  LYS B 311      51.106 -15.227  -5.299  1.00 40.04           N  
-ATOM   5228  N   PRO B 312      54.798 -10.634  -8.892  1.00 27.56           N  
-ATOM   5229  CA  PRO B 312      55.134  -9.837 -10.067  1.00 26.38           C  
-ATOM   5230  C   PRO B 312      54.662  -8.402  -9.844  1.00 25.04           C  
-ATOM   5231  O   PRO B 312      53.702  -8.146  -9.103  1.00 23.21           O  
-ATOM   5232  CB  PRO B 312      54.342 -10.526 -11.193  1.00 28.72           C  
-ATOM   5233  CG  PRO B 312      54.321 -11.983 -10.756  1.00 28.62           C  
-ATOM   5234  CD  PRO B 312      54.089 -11.881  -9.261  1.00 27.21           C  
-ATOM   5235  N   TYR B 313      55.348  -7.456 -10.467  1.00 24.99           N  
-ATOM   5236  CA  TYR B 313      54.946  -6.059 -10.349  1.00 23.82           C  
-ATOM   5237  C   TYR B 313      55.322  -5.397 -11.653  1.00 24.67           C  
-ATOM   5238  O   TYR B 313      56.062  -5.971 -12.452  1.00 23.01           O  
-ATOM   5239  CB  TYR B 313      55.676  -5.351  -9.187  1.00 22.33           C  
-ATOM   5240  CG  TYR B 313      57.160  -5.149  -9.411  1.00 22.23           C  
-ATOM   5241  CD1 TYR B 313      58.058  -6.201  -9.226  1.00 22.27           C  
-ATOM   5242  CD2 TYR B 313      57.669  -3.904  -9.801  1.00 21.75           C  
-ATOM   5243  CE1 TYR B 313      59.425  -6.027  -9.421  1.00 21.76           C  
-ATOM   5244  CE2 TYR B 313      59.050  -3.720 -10.001  1.00 23.16           C  
-ATOM   5245  CZ  TYR B 313      59.910  -4.779  -9.812  1.00 22.07           C  
-ATOM   5246  OH  TYR B 313      61.255  -4.625 -10.035  1.00 25.91           O  
-ATOM   5247  N   ASN B 314      54.818  -4.186 -11.862  1.00 26.63           N  
-ATOM   5248  CA  ASN B 314      55.126  -3.452 -13.079  1.00 27.93           C  
-ATOM   5249  C   ASN B 314      55.343  -1.977 -12.752  1.00 26.07           C  
-ATOM   5250  O   ASN B 314      54.387  -1.230 -12.524  1.00 28.90           O  
-ATOM   5251  CB  ASN B 314      53.987  -3.616 -14.106  1.00 29.20           C  
-ATOM   5252  CG  ASN B 314      54.204  -2.767 -15.353  1.00 34.95           C  
-ATOM   5253  OD1 ASN B 314      55.344  -2.567 -15.786  1.00 35.73           O  
-ATOM   5254  ND2 ASN B 314      53.114  -2.273 -15.938  1.00 37.59           N  
-ATOM   5255  N   GLY B 315      56.604  -1.562 -12.737  1.00 26.61           N  
-ATOM   5256  CA  GLY B 315      56.925  -0.181 -12.416  1.00 25.58           C  
-ATOM   5257  C   GLY B 315      57.044  -0.002 -10.914  1.00 25.66           C  
-ATOM   5258  O   GLY B 315      56.684  -0.903 -10.150  1.00 23.92           O  
-ATOM   5259  N   VAL B 316      57.559   1.148 -10.480  1.00 25.39           N  
-ATOM   5260  CA  VAL B 316      57.705   1.409  -9.050  1.00 23.24           C  
-ATOM   5261  C   VAL B 316      57.004   2.677  -8.655  1.00 22.99           C  
-ATOM   5262  O   VAL B 316      57.127   3.127  -7.530  1.00 22.39           O  
-ATOM   5263  CB  VAL B 316      59.181   1.502  -8.635  1.00 24.26           C  
-ATOM   5264  CG1 VAL B 316      59.820   0.142  -8.793  1.00 17.97           C  
-ATOM   5265  CG2 VAL B 316      59.921   2.551  -9.478  1.00 18.23           C  
-ATOM   5266  N   GLY B 317      56.256   3.257  -9.590  1.00 22.84           N  
-ATOM   5267  CA  GLY B 317      55.530   4.476  -9.279  1.00 23.05           C  
-ATOM   5268  C   GLY B 317      56.462   5.652  -9.058  1.00 22.64           C  
-ATOM   5269  O   GLY B 317      57.627   5.600  -9.446  1.00 23.03           O  
-ATOM   5270  N   GLN B 318      55.974   6.712  -8.423  1.00 21.47           N  
-ATOM   5271  CA  GLN B 318      56.825   7.878  -8.217  1.00 22.17           C  
-ATOM   5272  C   GLN B 318      57.631   7.762  -6.921  1.00 21.60           C  
-ATOM   5273  O   GLN B 318      57.978   6.654  -6.506  1.00 22.39           O  
-ATOM   5274  CB  GLN B 318      55.976   9.158  -8.267  1.00 24.07           C  
-ATOM   5275  CG  GLN B 318      55.410   9.420  -9.678  1.00 30.50           C  
-ATOM   5276  CD  GLN B 318      54.594  10.724  -9.788  1.00 36.12           C  
-ATOM   5277  OE1 GLN B 318      55.084  11.820  -9.483  1.00 36.13           O  
-ATOM   5278  NE2 GLN B 318      53.348  10.600 -10.238  1.00 38.05           N  
-ATOM   5279  N   GLY B 319      57.944   8.873  -6.279  1.00 19.65           N  
-ATOM   5280  CA  GLY B 319      58.722   8.757  -5.061  1.00 20.55           C  
-ATOM   5281  C   GLY B 319      58.878  10.141  -4.520  1.00 20.01           C  
-ATOM   5282  O   GLY B 319      58.279  11.055  -5.058  1.00 18.06           O  
-ATOM   5283  N   SER B 320      59.679  10.305  -3.477  1.00 18.56           N  
-ATOM   5284  CA  SER B 320      59.862  11.619  -2.880  1.00 18.03           C  
-ATOM   5285  C   SER B 320      60.849  12.474  -3.646  1.00 18.61           C  
-ATOM   5286  O   SER B 320      60.564  13.631  -3.969  1.00 16.14           O  
-ATOM   5287  CB  SER B 320      60.347  11.491  -1.437  1.00 17.39           C  
-ATOM   5288  OG  SER B 320      59.379  10.838  -0.639  1.00 16.32           O  
-ATOM   5289  N   TRP B 321      62.008  11.900  -3.942  1.00 16.92           N  
-ATOM   5290  CA  TRP B 321      63.058  12.635  -4.615  1.00 17.97           C  
-ATOM   5291  C   TRP B 321      63.580  11.875  -5.815  1.00 19.74           C  
-ATOM   5292  O   TRP B 321      64.321  12.420  -6.625  1.00 19.06           O  
-ATOM   5293  CB  TRP B 321      64.198  12.877  -3.609  1.00 17.54           C  
-ATOM   5294  CG  TRP B 321      63.664  13.422  -2.311  1.00 18.51           C  
-ATOM   5295  CD1 TRP B 321      63.532  12.745  -1.113  1.00 19.32           C  
-ATOM   5296  CD2 TRP B 321      63.050  14.701  -2.116  1.00 17.65           C  
-ATOM   5297  NE1 TRP B 321      62.861  13.528  -0.203  1.00 16.38           N  
-ATOM   5298  CE2 TRP B 321      62.554  14.733  -0.792  1.00 18.82           C  
-ATOM   5299  CE3 TRP B 321      62.865  15.828  -2.942  1.00 18.79           C  
-ATOM   5300  CZ2 TRP B 321      61.875  15.851  -0.267  1.00 21.91           C  
-ATOM   5301  CZ3 TRP B 321      62.182  16.953  -2.414  1.00 20.19           C  
-ATOM   5302  CH2 TRP B 321      61.698  16.948  -1.095  1.00 22.80           C  
-ATOM   5303  N   GLU B 322      63.149  10.622  -5.936  1.00 19.24           N  
-ATOM   5304  CA  GLU B 322      63.586   9.726  -7.003  1.00 19.31           C  
-ATOM   5305  C   GLU B 322      62.464   8.703  -7.105  1.00 18.98           C  
-ATOM   5306  O   GLU B 322      61.917   8.326  -6.077  1.00 17.80           O  
-ATOM   5307  CB  GLU B 322      64.874   9.059  -6.522  1.00 23.44           C  
-ATOM   5308  CG  GLU B 322      65.240   7.767  -7.133  1.00 35.00           C  
-ATOM   5309  CD  GLU B 322      66.536   7.235  -6.534  1.00 35.06           C  
-ATOM   5310  OE1 GLU B 322      67.095   6.266  -7.087  1.00 39.18           O  
-ATOM   5311  OE2 GLU B 322      66.978   7.802  -5.512  1.00 36.25           O  
-ATOM   5312  N   ASN B 323      62.116   8.251  -8.310  1.00 17.75           N  
-ATOM   5313  CA  ASN B 323      61.018   7.299  -8.424  1.00 18.79           C  
-ATOM   5314  C   ASN B 323      61.343   5.965  -7.753  1.00 17.99           C  
-ATOM   5315  O   ASN B 323      62.479   5.480  -7.834  1.00 18.78           O  
-ATOM   5316  CB  ASN B 323      60.644   7.069  -9.887  1.00 20.82           C  
-ATOM   5317  CG  ASN B 323      59.928   8.262 -10.489  1.00 23.31           C  
-ATOM   5318  OD1 ASN B 323      59.495   9.168  -9.763  1.00 24.34           O  
-ATOM   5319  ND2 ASN B 323      59.791   8.273 -11.813  1.00 22.31           N  
-ATOM   5320  N   GLY B 324      60.338   5.413  -7.073  1.00 19.78           N  
-ATOM   5321  CA  GLY B 324      60.468   4.126  -6.404  1.00 18.99           C  
-ATOM   5322  C   GLY B 324      60.944   4.195  -4.966  1.00 19.58           C  
-ATOM   5323  O   GLY B 324      60.982   3.172  -4.277  1.00 20.40           O  
-ATOM   5324  N   VAL B 325      61.309   5.391  -4.505  1.00 18.14           N  
-ATOM   5325  CA  VAL B 325      61.825   5.564  -3.151  1.00 14.93           C  
-ATOM   5326  C   VAL B 325      61.055   6.685  -2.454  1.00 17.60           C  
-ATOM   5327  O   VAL B 325      60.939   7.817  -2.972  1.00 17.10           O  
-ATOM   5328  CB  VAL B 325      63.335   5.905  -3.184  1.00 16.92           C  
-ATOM   5329  CG1 VAL B 325      63.876   6.053  -1.737  1.00 15.77           C  
-ATOM   5330  CG2 VAL B 325      64.101   4.827  -3.981  1.00 16.99           C  
-ATOM   5331  N   TRP B 326      60.542   6.368  -1.274  1.00 14.92           N  
-ATOM   5332  CA  TRP B 326      59.734   7.308  -0.529  1.00 15.91           C  
-ATOM   5333  C   TRP B 326      60.247   7.573   0.856  1.00 15.17           C  
-ATOM   5334  O   TRP B 326      60.590   6.647   1.567  1.00 17.19           O  
-ATOM   5335  CB  TRP B 326      58.292   6.788  -0.400  1.00 15.11           C  
-ATOM   5336  CG  TRP B 326      57.603   6.480  -1.698  1.00 17.07           C  
-ATOM   5337  CD1 TRP B 326      57.673   5.316  -2.413  1.00 16.66           C  
-ATOM   5338  CD2 TRP B 326      56.747   7.364  -2.448  1.00 17.56           C  
-ATOM   5339  NE1 TRP B 326      56.909   5.422  -3.568  1.00 16.77           N  
-ATOM   5340  CE2 TRP B 326      56.330   6.665  -3.607  1.00 17.10           C  
-ATOM   5341  CE3 TRP B 326      56.300   8.680  -2.253  1.00 18.09           C  
-ATOM   5342  CZ2 TRP B 326      55.479   7.239  -4.571  1.00 17.19           C  
-ATOM   5343  CZ3 TRP B 326      55.463   9.253  -3.209  1.00 19.29           C  
-ATOM   5344  CH2 TRP B 326      55.061   8.531  -4.354  1.00 17.80           C  
-ATOM   5345  N   ASP B 327      60.262   8.839   1.250  1.00 14.90           N  
-ATOM   5346  CA  ASP B 327      60.686   9.192   2.602  1.00 15.79           C  
-ATOM   5347  C   ASP B 327      59.743   8.500   3.590  1.00 17.17           C  
-ATOM   5348  O   ASP B 327      58.520   8.470   3.388  1.00 16.81           O  
-ATOM   5349  CB  ASP B 327      60.529  10.692   2.878  1.00 15.07           C  
-ATOM   5350  CG  ASP B 327      61.581  11.553   2.183  1.00 18.33           C  
-ATOM   5351  OD1 ASP B 327      62.528  11.000   1.583  1.00 15.75           O  
-ATOM   5352  OD2 ASP B 327      61.441  12.791   2.263  1.00 21.02           O  
-ATOM   5353  N   TYR B 328      60.304   7.983   4.674  1.00 15.23           N  
-ATOM   5354  CA  TYR B 328      59.480   7.356   5.688  1.00 15.66           C  
-ATOM   5355  C   TYR B 328      58.463   8.377   6.203  1.00 15.68           C  
-ATOM   5356  O   TYR B 328      57.313   8.032   6.444  1.00 15.50           O  
-ATOM   5357  CB  TYR B 328      60.349   6.892   6.861  1.00 14.41           C  
-ATOM   5358  CG  TYR B 328      59.571   6.648   8.134  1.00 15.67           C  
-ATOM   5359  CD1 TYR B 328      58.604   5.636   8.204  1.00 14.88           C  
-ATOM   5360  CD2 TYR B 328      59.828   7.401   9.277  1.00 14.67           C  
-ATOM   5361  CE1 TYR B 328      57.920   5.376   9.392  1.00 15.51           C  
-ATOM   5362  CE2 TYR B 328      59.157   7.162  10.472  1.00 15.62           C  
-ATOM   5363  CZ  TYR B 328      58.209   6.150  10.528  1.00 17.41           C  
-ATOM   5364  OH  TYR B 328      57.566   5.908  11.724  1.00 18.66           O  
-ATOM   5365  N   LYS B 329      58.862   9.640   6.337  1.00 15.84           N  
-ATOM   5366  CA  LYS B 329      57.922  10.618   6.867  1.00 17.88           C  
-ATOM   5367  C   LYS B 329      56.703  10.833   5.988  1.00 19.03           C  
-ATOM   5368  O   LYS B 329      55.724  11.435   6.424  1.00 21.20           O  
-ATOM   5369  CB  LYS B 329      58.612  11.945   7.181  1.00 19.59           C  
-ATOM   5370  CG  LYS B 329      59.166  12.713   5.996  1.00 19.30           C  
-ATOM   5371  CD  LYS B 329      59.854  13.978   6.524  1.00 23.29           C  
-ATOM   5372  CE  LYS B 329      60.532  14.737   5.396  1.00 25.10           C  
-ATOM   5373  NZ  LYS B 329      61.286  15.912   5.907  1.00 28.07           N  
-ATOM   5374  N   ALA B 330      56.744  10.310   4.769  1.00 17.45           N  
-ATOM   5375  CA  ALA B 330      55.613  10.418   3.854  1.00 19.40           C  
-ATOM   5376  C   ALA B 330      54.690   9.208   3.961  1.00 21.87           C  
-ATOM   5377  O   ALA B 330      53.640   9.155   3.315  1.00 22.14           O  
-ATOM   5378  CB  ALA B 330      56.128  10.509   2.424  1.00 19.66           C  
-ATOM   5379  N   LEU B 331      55.063   8.245   4.794  1.00 20.23           N  
-ATOM   5380  CA  LEU B 331      54.323   6.995   4.866  1.00 20.87           C  
-ATOM   5381  C   LEU B 331      53.610   6.724   6.184  1.00 21.60           C  
-ATOM   5382  O   LEU B 331      54.030   7.209   7.231  1.00 24.54           O  
-ATOM   5383  CB  LEU B 331      55.307   5.854   4.567  1.00 17.86           C  
-ATOM   5384  CG  LEU B 331      56.243   6.076   3.361  1.00 16.81           C  
-ATOM   5385  CD1 LEU B 331      57.316   4.962   3.271  1.00 17.37           C  
-ATOM   5386  CD2 LEU B 331      55.396   6.089   2.091  1.00 17.26           C  
-ATOM   5387  N   PRO B 332      52.513   5.949   6.145  1.00 21.57           N  
-ATOM   5388  CA  PRO B 332      51.941   5.346   4.940  1.00 21.90           C  
-ATOM   5389  C   PRO B 332      51.177   6.427   4.190  1.00 22.81           C  
-ATOM   5390  O   PRO B 332      50.759   7.410   4.798  1.00 21.51           O  
-ATOM   5391  CB  PRO B 332      51.002   4.281   5.504  1.00 21.92           C  
-ATOM   5392  CG  PRO B 332      50.495   4.955   6.759  1.00 23.67           C  
-ATOM   5393  CD  PRO B 332      51.755   5.543   7.347  1.00 23.10           C  
-ATOM   5394  N   GLN B 333      51.021   6.248   2.882  1.00 23.05           N  
-ATOM   5395  CA  GLN B 333      50.279   7.194   2.037  1.00 24.79           C  
-ATOM   5396  C   GLN B 333      48.775   6.992   2.210  1.00 26.38           C  
-ATOM   5397  O   GLN B 333      48.322   5.883   2.522  1.00 23.20           O  
-ATOM   5398  CB  GLN B 333      50.599   6.945   0.574  1.00 22.15           C  
-ATOM   5399  CG  GLN B 333      52.065   6.950   0.297  1.00 21.75           C  
-ATOM   5400  CD  GLN B 333      52.388   6.783  -1.171  1.00 20.21           C  
-ATOM   5401  OE1 GLN B 333      51.926   5.842  -1.826  1.00 20.57           O  
-ATOM   5402  NE2 GLN B 333      53.194   7.699  -1.699  1.00 23.04           N  
-ATOM   5403  N   ALA B 334      47.997   8.045   1.971  1.00 26.63           N  
-ATOM   5404  CA  ALA B 334      46.546   7.925   2.097  1.00 27.78           C  
-ATOM   5405  C   ALA B 334      46.087   6.755   1.246  1.00 26.71           C  
-ATOM   5406  O   ALA B 334      46.600   6.542   0.145  1.00 27.03           O  
-ATOM   5407  CB  ALA B 334      45.855   9.222   1.624  1.00 29.57           C  
-ATOM   5408  N   GLY B 335      45.143   5.979   1.780  1.00 29.06           N  
-ATOM   5409  CA  GLY B 335      44.596   4.844   1.058  1.00 28.19           C  
-ATOM   5410  C   GLY B 335      45.264   3.501   1.310  1.00 29.40           C  
-ATOM   5411  O   GLY B 335      44.691   2.457   0.999  1.00 28.24           O  
-ATOM   5412  N   ALA B 336      46.471   3.511   1.866  1.00 27.00           N  
-ATOM   5413  CA  ALA B 336      47.178   2.258   2.114  1.00 25.28           C  
-ATOM   5414  C   ALA B 336      47.009   1.810   3.553  1.00 24.63           C  
-ATOM   5415  O   ALA B 336      46.736   2.611   4.447  1.00 25.71           O  
-ATOM   5416  CB  ALA B 336      48.666   2.410   1.802  1.00 23.60           C  
-ATOM   5417  N   THR B 337      47.189   0.515   3.758  1.00 23.43           N  
-ATOM   5418  CA  THR B 337      47.083  -0.091   5.075  1.00 24.92           C  
-ATOM   5419  C   THR B 337      48.436  -0.751   5.335  1.00 21.57           C  
-ATOM   5420  O   THR B 337      48.982  -1.384   4.453  1.00 22.03           O  
-ATOM   5421  CB  THR B 337      45.980  -1.178   5.068  1.00 27.13           C  
-ATOM   5422  OG1 THR B 337      44.747  -0.574   4.662  1.00 31.24           O  
-ATOM   5423  CG2 THR B 337      45.811  -1.807   6.459  1.00 29.00           C  
-ATOM   5424  N   GLU B 338      48.964  -0.585   6.536  1.00 22.62           N  
-ATOM   5425  CA  GLU B 338      50.241  -1.169   6.918  1.00 23.26           C  
-ATOM   5426  C   GLU B 338      50.023  -2.612   7.347  1.00 25.13           C  
-ATOM   5427  O   GLU B 338      48.970  -2.937   7.896  1.00 27.41           O  
-ATOM   5428  CB  GLU B 338      50.853  -0.384   8.086  1.00 23.09           C  
-ATOM   5429  CG  GLU B 338      51.782   0.751   7.659  1.00 26.38           C  
-ATOM   5430  CD  GLU B 338      52.396   1.535   8.824  1.00 25.71           C  
-ATOM   5431  OE1 GLU B 338      52.297   1.105   9.990  1.00 26.96           O  
-ATOM   5432  OE2 GLU B 338      53.001   2.597   8.569  1.00 29.28           O  
-ATOM   5433  N   HIS B 339      51.008  -3.473   7.084  1.00 24.80           N  
-ATOM   5434  CA  HIS B 339      50.959  -4.884   7.476  1.00 25.78           C  
-ATOM   5435  C   HIS B 339      52.343  -5.196   8.054  1.00 25.83           C  
-ATOM   5436  O   HIS B 339      53.358  -4.737   7.521  1.00 24.41           O  
-ATOM   5437  CB  HIS B 339      50.698  -5.773   6.261  1.00 27.30           C  
-ATOM   5438  CG  HIS B 339      49.379  -5.512   5.600  1.00 31.68           C  
-ATOM   5439  ND1 HIS B 339      48.174  -5.811   6.199  1.00 30.51           N  
-ATOM   5440  CD2 HIS B 339      49.075  -4.951   4.404  1.00 31.34           C  
-ATOM   5441  CE1 HIS B 339      47.184  -5.448   5.402  1.00 30.71           C  
-ATOM   5442  NE2 HIS B 339      47.702  -4.924   4.306  1.00 31.22           N  
-ATOM   5443  N   VAL B 340      52.388  -5.958   9.144  1.00 23.87           N  
-ATOM   5444  CA  VAL B 340      53.654  -6.305   9.784  1.00 20.82           C  
-ATOM   5445  C   VAL B 340      53.837  -7.823   9.803  1.00 22.37           C  
-ATOM   5446  O   VAL B 340      52.866  -8.564   9.974  1.00 20.77           O  
-ATOM   5447  CB  VAL B 340      53.694  -5.756  11.237  1.00 22.21           C  
-ATOM   5448  CG1 VAL B 340      55.057  -5.990  11.854  1.00 18.88           C  
-ATOM   5449  CG2 VAL B 340      53.397  -4.268  11.231  1.00 20.27           C  
-ATOM   5450  N   LEU B 341      55.074  -8.268   9.561  1.00 18.60           N  
-ATOM   5451  CA  LEU B 341      55.458  -9.677   9.566  1.00 18.22           C  
-ATOM   5452  C   LEU B 341      56.550  -9.704  10.629  1.00 16.61           C  
-ATOM   5453  O   LEU B 341      57.728  -9.615  10.338  1.00 15.86           O  
-ATOM   5454  CB  LEU B 341      55.998 -10.094   8.204  1.00 17.56           C  
-ATOM   5455  CG  LEU B 341      54.890 -10.143   7.134  1.00 21.94           C  
-ATOM   5456  CD1 LEU B 341      55.492 -10.304   5.734  1.00 20.78           C  
-ATOM   5457  CD2 LEU B 341      53.949 -11.324   7.456  1.00 24.34           C  
-ATOM   5458  N   PRO B 342      56.143  -9.808  11.895  1.00 19.66           N  
-ATOM   5459  CA  PRO B 342      57.111  -9.814  12.990  1.00 16.35           C  
-ATOM   5460  C   PRO B 342      58.218 -10.857  12.925  1.00 17.83           C  
-ATOM   5461  O   PRO B 342      59.358 -10.556  13.281  1.00 19.66           O  
-ATOM   5462  CB  PRO B 342      56.228  -9.906  14.247  1.00 19.81           C  
-ATOM   5463  CG  PRO B 342      54.946 -10.543  13.746  1.00 22.99           C  
-ATOM   5464  CD  PRO B 342      54.755  -9.968  12.371  1.00 19.90           C  
-ATOM   5465  N   ASP B 343      57.926 -12.056  12.430  1.00 15.32           N  
-ATOM   5466  CA  ASP B 343      58.959 -13.066  12.406  1.00 15.82           C  
-ATOM   5467  C   ASP B 343      60.050 -12.857  11.372  1.00 17.53           C  
-ATOM   5468  O   ASP B 343      61.006 -13.618  11.347  1.00 17.86           O  
-ATOM   5469  CB  ASP B 343      58.346 -14.474  12.329  1.00 15.10           C  
-ATOM   5470  CG  ASP B 343      57.678 -14.868  13.641  1.00 19.14           C  
-ATOM   5471  OD1 ASP B 343      57.984 -14.240  14.682  1.00 19.29           O  
-ATOM   5472  OD2 ASP B 343      56.853 -15.794  13.649  1.00 23.51           O  
-ATOM   5473  N   ILE B 344      59.904 -11.857  10.502  1.00 16.75           N  
-ATOM   5474  CA  ILE B 344      61.005 -11.537   9.582  1.00 16.60           C  
-ATOM   5475  C   ILE B 344      61.369 -10.050   9.837  1.00 17.04           C  
-ATOM   5476  O   ILE B 344      62.225  -9.475   9.157  1.00 17.01           O  
-ATOM   5477  CB  ILE B 344      60.650 -11.723   8.095  1.00 15.48           C  
-ATOM   5478  CG1 ILE B 344      59.514 -10.762   7.701  1.00 17.67           C  
-ATOM   5479  CG2 ILE B 344      60.259 -13.190   7.815  1.00 16.34           C  
-ATOM   5480  CD1 ILE B 344      59.339 -10.672   6.196  1.00 21.12           C  
-ATOM   5481  N   MET B 345      60.720  -9.468  10.850  1.00 17.57           N  
-ATOM   5482  CA  MET B 345      60.897  -8.069  11.251  1.00 16.92           C  
-ATOM   5483  C   MET B 345      60.804  -7.156  10.027  1.00 18.58           C  
-ATOM   5484  O   MET B 345      61.738  -6.420   9.679  1.00 17.18           O  
-ATOM   5485  CB  MET B 345      62.238  -7.869  11.991  1.00 15.32           C  
-ATOM   5486  CG  MET B 345      62.357  -8.757  13.248  1.00 15.82           C  
-ATOM   5487  SD  MET B 345      63.809  -8.322  14.229  1.00 16.17           S  
-ATOM   5488  CE  MET B 345      63.547  -9.322  15.701  1.00 18.50           C  
-ATOM   5489  N   ALA B 346      59.662  -7.225   9.358  1.00 16.49           N  
-ATOM   5490  CA  ALA B 346      59.469  -6.405   8.184  1.00 16.99           C  
-ATOM   5491  C   ALA B 346      58.044  -5.880   8.226  1.00 16.72           C  
-ATOM   5492  O   ALA B 346      57.158  -6.471   8.856  1.00 18.57           O  
-ATOM   5493  CB  ALA B 346      59.704  -7.246   6.903  1.00 15.97           C  
-ATOM   5494  N   SER B 347      57.833  -4.749   7.589  1.00 16.63           N  
-ATOM   5495  CA  SER B 347      56.508  -4.179   7.528  1.00 14.53           C  
-ATOM   5496  C   SER B 347      56.379  -3.611   6.134  1.00 17.84           C  
-ATOM   5497  O   SER B 347      57.389  -3.400   5.434  1.00 13.86           O  
-ATOM   5498  CB  SER B 347      56.319  -3.081   8.585  1.00 16.98           C  
-ATOM   5499  OG  SER B 347      57.348  -2.091   8.541  1.00 19.27           O  
-ATOM   5500  N   TYR B 348      55.139  -3.381   5.717  1.00 15.64           N  
-ATOM   5501  CA  TYR B 348      54.918  -2.813   4.412  1.00 16.22           C  
-ATOM   5502  C   TYR B 348      53.517  -2.226   4.347  1.00 18.56           C  
-ATOM   5503  O   TYR B 348      52.654  -2.558   5.157  1.00 19.07           O  
-ATOM   5504  CB  TYR B 348      55.104  -3.873   3.315  1.00 16.32           C  
-ATOM   5505  CG  TYR B 348      54.082  -5.010   3.322  1.00 21.20           C  
-ATOM   5506  CD1 TYR B 348      54.277  -6.151   4.109  1.00 17.95           C  
-ATOM   5507  CD2 TYR B 348      52.922  -4.941   2.537  1.00 21.69           C  
-ATOM   5508  CE1 TYR B 348      53.342  -7.201   4.113  1.00 23.54           C  
-ATOM   5509  CE2 TYR B 348      51.984  -5.986   2.526  1.00 22.96           C  
-ATOM   5510  CZ  TYR B 348      52.206  -7.111   3.319  1.00 25.73           C  
-ATOM   5511  OH  TYR B 348      51.296  -8.140   3.322  1.00 25.96           O  
-ATOM   5512  N   SER B 349      53.291  -1.327   3.406  1.00 18.62           N  
-ATOM   5513  CA  SER B 349      51.945  -0.769   3.261  1.00 19.45           C  
-ATOM   5514  C   SER B 349      51.445  -1.312   1.952  1.00 21.13           C  
-ATOM   5515  O   SER B 349      52.226  -1.544   1.030  1.00 19.19           O  
-ATOM   5516  CB  SER B 349      51.975   0.757   3.184  1.00 21.21           C  
-ATOM   5517  OG  SER B 349      52.672   1.173   2.021  1.00 20.10           O  
-ATOM   5518  N   TYR B 350      50.136  -1.533   1.859  1.00 23.64           N  
-ATOM   5519  CA  TYR B 350      49.573  -2.022   0.615  1.00 22.66           C  
-ATOM   5520  C   TYR B 350      48.246  -1.297   0.368  1.00 24.56           C  
-ATOM   5521  O   TYR B 350      47.471  -1.061   1.290  1.00 26.84           O  
-ATOM   5522  CB  TYR B 350      49.367  -3.546   0.677  1.00 23.22           C  
-ATOM   5523  CG  TYR B 350      48.928  -4.114  -0.655  1.00 25.20           C  
-ATOM   5524  CD1 TYR B 350      49.792  -4.090  -1.758  1.00 25.00           C  
-ATOM   5525  CD2 TYR B 350      47.625  -4.607  -0.842  1.00 26.42           C  
-ATOM   5526  CE1 TYR B 350      49.382  -4.530  -3.011  1.00 22.67           C  
-ATOM   5527  CE2 TYR B 350      47.197  -5.059  -2.110  1.00 24.64           C  
-ATOM   5528  CZ  TYR B 350      48.075  -5.017  -3.181  1.00 26.12           C  
-ATOM   5529  OH  TYR B 350      47.688  -5.457  -4.424  1.00 25.44           O  
-ATOM   5530  N   ASP B 351      48.015  -0.904  -0.875  1.00 26.27           N  
-ATOM   5531  CA  ASP B 351      46.772  -0.222  -1.239  1.00 28.83           C  
-ATOM   5532  C   ASP B 351      46.175  -1.138  -2.282  1.00 28.76           C  
-ATOM   5533  O   ASP B 351      46.639  -1.180  -3.423  1.00 29.11           O  
-ATOM   5534  CB  ASP B 351      47.051   1.145  -1.857  1.00 25.73           C  
-ATOM   5535  CG  ASP B 351      45.777   1.915  -2.163  1.00 30.61           C  
-ATOM   5536  OD1 ASP B 351      44.752   1.273  -2.485  1.00 30.88           O  
-ATOM   5537  OD2 ASP B 351      45.810   3.162  -2.086  1.00 27.29           O  
-ATOM   5538  N   ALA B 352      45.171  -1.899  -1.872  1.00 29.31           N  
-ATOM   5539  CA  ALA B 352      44.537  -2.858  -2.765  1.00 31.18           C  
-ATOM   5540  C   ALA B 352      43.825  -2.202  -3.942  1.00 32.50           C  
-ATOM   5541  O   ALA B 352      43.700  -2.815  -4.996  1.00 34.90           O  
-ATOM   5542  CB  ALA B 352      43.566  -3.737  -1.982  1.00 31.64           C  
-ATOM   5543  N   THR B 353      43.378  -0.961  -3.780  1.00 34.56           N  
-ATOM   5544  CA  THR B 353      42.684  -0.285  -4.874  1.00 36.61           C  
-ATOM   5545  C   THR B 353      43.581  -0.085  -6.089  1.00 36.75           C  
-ATOM   5546  O   THR B 353      43.164  -0.341  -7.213  1.00 36.79           O  
-ATOM   5547  CB  THR B 353      42.142   1.076  -4.447  1.00 37.01           C  
-ATOM   5548  OG1 THR B 353      43.231   1.960  -4.159  1.00 42.31           O  
-ATOM   5549  CG2 THR B 353      41.271   0.929  -3.217  1.00 36.36           C  
-ATOM   5550  N   ASN B 354      44.810   0.374  -5.875  1.00 36.74           N  
-ATOM   5551  CA  ASN B 354      45.728   0.570  -6.994  1.00 35.47           C  
-ATOM   5552  C   ASN B 354      46.872  -0.437  -7.014  1.00 33.44           C  
-ATOM   5553  O   ASN B 354      47.760  -0.355  -7.857  1.00 31.38           O  
-ATOM   5554  CB  ASN B 354      46.284   1.995  -6.988  1.00 38.69           C  
-ATOM   5555  CG  ASN B 354      46.829   2.399  -5.634  1.00 41.74           C  
-ATOM   5556  OD1 ASN B 354      47.090   1.552  -4.782  1.00 40.95           O  
-ATOM   5557  ND2 ASN B 354      47.011   3.702  -5.431  1.00 44.02           N  
-ATOM   5558  N   LYS B 355      46.843  -1.398  -6.093  1.00 32.37           N  
-ATOM   5559  CA  LYS B 355      47.882  -2.440  -6.031  1.00 30.06           C  
-ATOM   5560  C   LYS B 355      49.317  -1.892  -5.897  1.00 26.92           C  
-ATOM   5561  O   LYS B 355      50.258  -2.374  -6.531  1.00 25.09           O  
-ATOM   5562  CB  LYS B 355      47.787  -3.338  -7.261  1.00 34.07           C  
-ATOM   5563  CG  LYS B 355      46.503  -4.165  -7.329  1.00 36.79           C  
-ATOM   5564  CD  LYS B 355      46.664  -5.325  -8.290  1.00 41.83           C  
-ATOM   5565  CE  LYS B 355      45.468  -6.275  -8.217  1.00 45.49           C  
-ATOM   5566  NZ  LYS B 355      45.625  -7.380  -9.210  1.00 46.84           N  
-ATOM   5567  N   PHE B 356      49.460  -0.879  -5.059  1.00 25.33           N  
-ATOM   5568  CA  PHE B 356      50.756  -0.251  -4.802  1.00 24.54           C  
-ATOM   5569  C   PHE B 356      51.279  -0.768  -3.459  1.00 21.32           C  
-ATOM   5570  O   PHE B 356      50.614  -0.616  -2.434  1.00 19.09           O  
-ATOM   5571  CB  PHE B 356      50.595   1.269  -4.711  1.00 22.63           C  
-ATOM   5572  CG  PHE B 356      51.869   2.037  -4.943  1.00 23.40           C  
-ATOM   5573  CD1 PHE B 356      52.560   1.907  -6.139  1.00 20.84           C  
-ATOM   5574  CD2 PHE B 356      52.337   2.946  -3.993  1.00 24.08           C  
-ATOM   5575  CE1 PHE B 356      53.705   2.685  -6.396  1.00 21.81           C  
-ATOM   5576  CE2 PHE B 356      53.482   3.729  -4.238  1.00 23.27           C  
-ATOM   5577  CZ  PHE B 356      54.160   3.596  -5.443  1.00 22.37           C  
-ATOM   5578  N   LEU B 357      52.474  -1.355  -3.471  1.00 21.48           N  
-ATOM   5579  CA  LEU B 357      53.087  -1.874  -2.253  1.00 20.50           C  
-ATOM   5580  C   LEU B 357      54.352  -1.088  -1.925  1.00 20.19           C  
-ATOM   5581  O   LEU B 357      55.128  -0.773  -2.847  1.00 18.47           O  
-ATOM   5582  CB  LEU B 357      53.466  -3.346  -2.443  1.00 22.01           C  
-ATOM   5583  CG  LEU B 357      53.879  -4.133  -1.190  1.00 27.66           C  
-ATOM   5584  CD1 LEU B 357      53.477  -5.615  -1.330  1.00 29.30           C  
-ATOM   5585  CD2 LEU B 357      55.359  -3.999  -0.987  1.00 28.44           C  
-ATOM   5586  N   ILE B 358      54.573  -0.787  -0.635  1.00 16.33           N  
-ATOM   5587  CA  ILE B 358      55.802  -0.080  -0.244  1.00 17.59           C  
-ATOM   5588  C   ILE B 358      56.504  -0.754   0.942  1.00 17.56           C  
-ATOM   5589  O   ILE B 358      55.908  -0.962   1.992  1.00 19.53           O  
-ATOM   5590  CB  ILE B 358      55.546   1.406   0.124  1.00 17.90           C  
-ATOM   5591  CG1 ILE B 358      54.652   2.084  -0.940  1.00 16.14           C  
-ATOM   5592  CG2 ILE B 358      56.883   2.147   0.162  1.00 17.12           C  
-ATOM   5593  CD1 ILE B 358      54.399   3.578  -0.667  1.00 17.48           C  
-ATOM   5594  N   SER B 359      57.772  -1.107   0.763  1.00 15.94           N  
-ATOM   5595  CA  SER B 359      58.524  -1.763   1.832  1.00 15.53           C  
-ATOM   5596  C   SER B 359      59.321  -0.732   2.601  1.00 15.22           C  
-ATOM   5597  O   SER B 359      60.246  -0.128   2.056  1.00 14.16           O  
-ATOM   5598  CB  SER B 359      59.487  -2.816   1.261  1.00 13.61           C  
-ATOM   5599  OG  SER B 359      60.280  -3.336   2.313  1.00 16.65           O  
-ATOM   5600  N   TYR B 360      58.942  -0.543   3.863  1.00 14.72           N  
-ATOM   5601  CA  TYR B 360      59.595   0.390   4.753  1.00 14.97           C  
-ATOM   5602  C   TYR B 360      59.330  -0.110   6.162  1.00 17.09           C  
-ATOM   5603  O   TYR B 360      58.427  -0.925   6.370  1.00 20.47           O  
-ATOM   5604  CB  TYR B 360      59.034   1.801   4.608  1.00 15.13           C  
-ATOM   5605  CG  TYR B 360      57.577   1.939   4.972  1.00 16.25           C  
-ATOM   5606  CD1 TYR B 360      56.580   1.624   4.052  1.00 18.58           C  
-ATOM   5607  CD2 TYR B 360      57.193   2.388   6.244  1.00 17.28           C  
-ATOM   5608  CE1 TYR B 360      55.210   1.761   4.385  1.00 20.19           C  
-ATOM   5609  CE2 TYR B 360      55.845   2.526   6.593  1.00 18.34           C  
-ATOM   5610  CZ  TYR B 360      54.859   2.214   5.651  1.00 21.37           C  
-ATOM   5611  OH  TYR B 360      53.530   2.387   5.963  1.00 23.64           O  
-ATOM   5612  N   ASP B 361      60.112   0.371   7.122  1.00 14.78           N  
-ATOM   5613  CA  ASP B 361      59.958  -0.033   8.522  1.00 13.41           C  
-ATOM   5614  C   ASP B 361      59.074   0.954   9.256  1.00 14.00           C  
-ATOM   5615  O   ASP B 361      59.276   2.162   9.125  1.00 15.43           O  
-ATOM   5616  CB  ASP B 361      61.309  -0.027   9.259  1.00 11.71           C  
-ATOM   5617  CG  ASP B 361      62.276  -1.123   8.783  1.00 13.46           C  
-ATOM   5618  OD1 ASP B 361      61.859  -2.069   8.085  1.00 12.81           O  
-ATOM   5619  OD2 ASP B 361      63.469  -1.039   9.146  1.00 15.46           O  
-ATOM   5620  N   ASN B 362      58.115   0.443  10.037  1.00 15.91           N  
-ATOM   5621  CA  ASN B 362      57.267   1.295  10.864  1.00 15.97           C  
-ATOM   5622  C   ASN B 362      57.838   1.208  12.293  1.00 17.82           C  
-ATOM   5623  O   ASN B 362      58.808   0.483  12.543  1.00 18.35           O  
-ATOM   5624  CB  ASN B 362      55.769   0.873  10.814  1.00 14.79           C  
-ATOM   5625  CG  ASN B 362      55.532  -0.570  11.266  1.00 18.30           C  
-ATOM   5626  OD1 ASN B 362      56.426  -1.228  11.813  1.00 17.62           O  
-ATOM   5627  ND2 ASN B 362      54.307  -1.060  11.045  1.00 17.81           N  
-ATOM   5628  N   PRO B 363      57.263   1.962  13.240  1.00 17.82           N  
-ATOM   5629  CA  PRO B 363      57.757   1.937  14.618  1.00 18.14           C  
-ATOM   5630  C   PRO B 363      57.815   0.542  15.207  1.00 18.70           C  
-ATOM   5631  O   PRO B 363      58.746   0.209  15.958  1.00 18.34           O  
-ATOM   5632  CB  PRO B 363      56.782   2.855  15.351  1.00 18.92           C  
-ATOM   5633  CG  PRO B 363      56.475   3.886  14.278  1.00 20.32           C  
-ATOM   5634  CD  PRO B 363      56.248   3.022  13.063  1.00 20.39           C  
-ATOM   5635  N   GLN B 364      56.823  -0.284  14.887  1.00 18.01           N  
-ATOM   5636  CA  GLN B 364      56.846  -1.642  15.408  1.00 18.63           C  
-ATOM   5637  C   GLN B 364      58.109  -2.376  14.936  1.00 18.00           C  
-ATOM   5638  O   GLN B 364      58.799  -3.030  15.717  1.00 17.94           O  
-ATOM   5639  CB  GLN B 364      55.628  -2.433  14.957  1.00 18.24           C  
-ATOM   5640  CG  GLN B 364      55.481  -3.687  15.813  1.00 26.13           C  
-ATOM   5641  CD  GLN B 364      54.378  -4.618  15.355  1.00 27.87           C  
-ATOM   5642  OE1 GLN B 364      53.404  -4.198  14.719  1.00 25.61           O  
-ATOM   5643  NE2 GLN B 364      54.519  -5.892  15.699  1.00 23.13           N  
-ATOM   5644  N   VAL B 365      58.415  -2.276  13.654  1.00 17.01           N  
-ATOM   5645  CA  VAL B 365      59.590  -2.955  13.148  1.00 16.57           C  
-ATOM   5646  C   VAL B 365      60.857  -2.400  13.780  1.00 17.27           C  
-ATOM   5647  O   VAL B 365      61.803  -3.146  14.069  1.00 17.07           O  
-ATOM   5648  CB  VAL B 365      59.643  -2.857  11.625  1.00 17.39           C  
-ATOM   5649  CG1 VAL B 365      61.045  -3.287  11.089  1.00 18.91           C  
-ATOM   5650  CG2 VAL B 365      58.540  -3.755  11.060  1.00 16.92           C  
-ATOM   5651  N   ALA B 366      60.866  -1.089  14.005  1.00 16.73           N  
-ATOM   5652  CA  ALA B 366      62.010  -0.441  14.623  1.00 17.80           C  
-ATOM   5653  C   ALA B 366      62.184  -0.976  16.040  1.00 17.68           C  
-ATOM   5654  O   ALA B 366      63.311  -1.196  16.490  1.00 18.37           O  
-ATOM   5655  CB  ALA B 366      61.815   1.083  14.639  1.00 19.29           C  
-ATOM   5656  N   ASN B 367      61.081  -1.178  16.756  1.00 15.10           N  
-ATOM   5657  CA  ASN B 367      61.199  -1.746  18.107  1.00 18.47           C  
-ATOM   5658  C   ASN B 367      61.782  -3.170  18.017  1.00 17.63           C  
-ATOM   5659  O   ASN B 367      62.652  -3.556  18.796  1.00 17.71           O  
-ATOM   5660  CB  ASN B 367      59.838  -1.794  18.798  1.00 22.12           C  
-ATOM   5661  CG  ASN B 367      59.475  -0.471  19.426  1.00 25.52           C  
-ATOM   5662  OD1 ASN B 367      60.214   0.042  20.256  1.00 29.35           O  
-ATOM   5663  ND2 ASN B 367      58.337   0.084  19.040  1.00 29.50           N  
-ATOM   5664  N   LEU B 368      61.299  -3.943  17.054  1.00 16.35           N  
-ATOM   5665  CA  LEU B 368      61.799  -5.304  16.867  1.00 15.31           C  
-ATOM   5666  C   LEU B 368      63.296  -5.327  16.548  1.00 16.56           C  
-ATOM   5667  O   LEU B 368      64.048  -6.139  17.104  1.00 16.62           O  
-ATOM   5668  CB  LEU B 368      61.033  -5.990  15.745  1.00 14.27           C  
-ATOM   5669  CG  LEU B 368      59.586  -6.345  16.123  1.00 15.96           C  
-ATOM   5670  CD1 LEU B 368      58.836  -6.832  14.874  1.00 14.36           C  
-ATOM   5671  CD2 LEU B 368      59.606  -7.420  17.216  1.00 19.51           C  
-ATOM   5672  N   LYS B 369      63.739  -4.446  15.661  1.00 14.72           N  
-ATOM   5673  CA  LYS B 369      65.153  -4.446  15.294  1.00 15.23           C  
-ATOM   5674  C   LYS B 369      66.015  -3.996  16.456  1.00 14.84           C  
-ATOM   5675  O   LYS B 369      67.194  -4.369  16.551  1.00 15.78           O  
-ATOM   5676  CB  LYS B 369      65.406  -3.550  14.062  1.00 15.10           C  
-ATOM   5677  CG  LYS B 369      64.741  -4.125  12.806  1.00 14.19           C  
-ATOM   5678  CD  LYS B 369      65.094  -3.354  11.524  1.00 11.85           C  
-ATOM   5679  CE  LYS B 369      64.647  -4.133  10.287  1.00 13.04           C  
-ATOM   5680  NZ  LYS B 369      64.901  -3.367   9.017  1.00  9.82           N  
-ATOM   5681  N   SER B 370      65.444  -3.170  17.326  1.00 14.66           N  
-ATOM   5682  CA  SER B 370      66.186  -2.714  18.496  1.00 16.48           C  
-ATOM   5683  C   SER B 370      66.408  -3.909  19.447  1.00 17.56           C  
-ATOM   5684  O   SER B 370      67.483  -4.048  20.042  1.00 17.95           O  
-ATOM   5685  CB  SER B 370      65.406  -1.621  19.234  1.00 17.24           C  
-ATOM   5686  OG  SER B 370      65.260  -0.479  18.394  1.00 22.44           O  
-ATOM   5687  N   GLY B 371      65.374  -4.736  19.615  1.00 16.38           N  
-ATOM   5688  CA  GLY B 371      65.509  -5.913  20.467  1.00 17.98           C  
-ATOM   5689  C   GLY B 371      66.549  -6.826  19.826  1.00 18.05           C  
-ATOM   5690  O   GLY B 371      67.334  -7.509  20.497  1.00 18.43           O  
-ATOM   5691  N   TYR B 372      66.562  -6.823  18.498  1.00 17.04           N  
-ATOM   5692  CA  TYR B 372      67.511  -7.642  17.742  1.00 16.49           C  
-ATOM   5693  C   TYR B 372      68.941  -7.187  18.021  1.00 18.18           C  
-ATOM   5694  O   TYR B 372      69.821  -8.001  18.306  1.00 17.44           O  
-ATOM   5695  CB  TYR B 372      67.196  -7.533  16.256  1.00 16.87           C  
-ATOM   5696  CG  TYR B 372      68.036  -8.425  15.372  1.00 18.02           C  
-ATOM   5697  CD1 TYR B 372      67.903  -9.816  15.427  1.00 18.53           C  
-ATOM   5698  CD2 TYR B 372      68.919  -7.878  14.434  1.00 17.62           C  
-ATOM   5699  CE1 TYR B 372      68.618 -10.654  14.553  1.00 17.59           C  
-ATOM   5700  CE2 TYR B 372      69.652  -8.712  13.555  1.00 17.95           C  
-ATOM   5701  CZ  TYR B 372      69.481 -10.088  13.619  1.00 18.28           C  
-ATOM   5702  OH  TYR B 372      70.093 -10.900  12.689  1.00 17.35           O  
-ATOM   5703  N   ILE B 373      69.175  -5.878  17.926  1.00 17.69           N  
-ATOM   5704  CA  ILE B 373      70.495  -5.298  18.202  1.00 16.15           C  
-ATOM   5705  C   ILE B 373      70.948  -5.711  19.615  1.00 18.20           C  
-ATOM   5706  O   ILE B 373      72.075  -6.150  19.809  1.00 18.33           O  
-ATOM   5707  CB  ILE B 373      70.433  -3.755  18.123  1.00 15.18           C  
-ATOM   5708  CG1 ILE B 373      70.403  -3.309  16.650  1.00 13.74           C  
-ATOM   5709  CG2 ILE B 373      71.600  -3.147  18.872  1.00 15.66           C  
-ATOM   5710  CD1 ILE B 373      69.890  -1.880  16.459  1.00 14.71           C  
-ATOM   5711  N   LYS B 374      70.078  -5.557  20.601  1.00 16.34           N  
-ATOM   5712  CA  LYS B 374      70.435  -5.945  21.958  1.00 19.37           C  
-ATOM   5713  C   LYS B 374      70.677  -7.439  22.088  1.00 20.41           C  
-ATOM   5714  O   LYS B 374      71.633  -7.860  22.729  1.00 19.56           O  
-ATOM   5715  CB  LYS B 374      69.332  -5.563  22.947  1.00 21.96           C  
-ATOM   5716  CG  LYS B 374      69.091  -4.069  23.024  1.00 29.98           C  
-ATOM   5717  CD  LYS B 374      68.412  -3.650  24.329  1.00 33.50           C  
-ATOM   5718  CE  LYS B 374      67.065  -4.315  24.521  1.00 37.62           C  
-ATOM   5719  NZ  LYS B 374      66.030  -3.810  23.582  1.00 43.76           N  
-ATOM   5720  N   SER B 375      69.831  -8.244  21.457  1.00 18.89           N  
-ATOM   5721  CA  SER B 375      69.970  -9.688  21.588  1.00 22.17           C  
-ATOM   5722  C   SER B 375      71.268 -10.197  20.996  1.00 23.39           C  
-ATOM   5723  O   SER B 375      71.815 -11.182  21.472  1.00 22.03           O  
-ATOM   5724  CB  SER B 375      68.800 -10.417  20.921  1.00 20.61           C  
-ATOM   5725  OG  SER B 375      68.903 -10.290  19.508  1.00 27.34           O  
-ATOM   5726  N   LEU B 376      71.756  -9.535  19.958  1.00 21.80           N  
-ATOM   5727  CA  LEU B 376      72.990  -9.974  19.314  1.00 23.18           C  
-ATOM   5728  C   LEU B 376      74.215  -9.228  19.850  1.00 20.58           C  
-ATOM   5729  O   LEU B 376      75.357  -9.563  19.545  1.00 23.78           O  
-ATOM   5730  CB  LEU B 376      72.858  -9.787  17.794  1.00 21.54           C  
-ATOM   5731  CG  LEU B 376      72.491 -11.041  16.969  1.00 26.35           C  
-ATOM   5732  CD1 LEU B 376      71.234 -11.664  17.513  1.00 27.85           C  
-ATOM   5733  CD2 LEU B 376      72.316 -10.708  15.503  1.00 25.63           C  
-ATOM   5734  N   GLY B 377      73.971  -8.224  20.666  1.00 20.71           N  
-ATOM   5735  CA  GLY B 377      75.068  -7.433  21.176  1.00 20.62           C  
-ATOM   5736  C   GLY B 377      75.708  -6.685  20.015  1.00 22.25           C  
-ATOM   5737  O   GLY B 377      76.935  -6.505  19.992  1.00 21.81           O  
-ATOM   5738  N   LEU B 378      74.903  -6.269  19.033  1.00 19.07           N  
-ATOM   5739  CA  LEU B 378      75.446  -5.522  17.882  1.00 18.29           C  
-ATOM   5740  C   LEU B 378      75.999  -4.197  18.359  1.00 17.87           C  
-ATOM   5741  O   LEU B 378      75.723  -3.778  19.478  1.00 20.40           O  
-ATOM   5742  CB  LEU B 378      74.368  -5.281  16.819  1.00 17.44           C  
-ATOM   5743  CG  LEU B 378      73.881  -6.612  16.229  1.00 17.18           C  
-ATOM   5744  CD1 LEU B 378      72.866  -6.344  15.145  1.00 17.55           C  
-ATOM   5745  CD2 LEU B 378      75.046  -7.390  15.605  1.00 17.46           C  
-ATOM   5746  N   GLY B 379      76.762  -3.531  17.499  1.00 19.86           N  
-ATOM   5747  CA  GLY B 379      77.386  -2.268  17.864  1.00 19.67           C  
-ATOM   5748  C   GLY B 379      76.497  -1.048  17.903  1.00 20.44           C  
-ATOM   5749  O   GLY B 379      76.952   0.035  18.275  1.00 23.12           O  
-ATOM   5750  N   GLY B 380      75.232  -1.207  17.532  1.00 18.87           N  
-ATOM   5751  CA  GLY B 380      74.328  -0.071  17.556  1.00 17.59           C  
-ATOM   5752  C   GLY B 380      73.482  -0.002  16.299  1.00 16.38           C  
-ATOM   5753  O   GLY B 380      73.340  -0.992  15.586  1.00 17.88           O  
-ATOM   5754  N   ALA B 381      72.939   1.180  16.035  1.00 16.26           N  
-ATOM   5755  CA  ALA B 381      72.050   1.428  14.901  1.00 16.09           C  
-ATOM   5756  C   ALA B 381      72.625   2.513  13.989  1.00 15.75           C  
-ATOM   5757  O   ALA B 381      73.347   3.394  14.449  1.00 16.92           O  
-ATOM   5758  CB  ALA B 381      70.674   1.887  15.417  1.00 15.01           C  
-ATOM   5759  N   MET B 382      72.301   2.420  12.700  1.00 15.89           N  
-ATOM   5760  CA  MET B 382      72.714   3.395  11.691  1.00 14.46           C  
-ATOM   5761  C   MET B 382      71.505   3.582  10.784  1.00 15.50           C  
-ATOM   5762  O   MET B 382      70.697   2.651  10.616  1.00 15.20           O  
-ATOM   5763  CB  MET B 382      73.891   2.877  10.853  1.00 13.45           C  
-ATOM   5764  CG  MET B 382      74.288   3.788   9.681  1.00 15.34           C  
-ATOM   5765  SD  MET B 382      73.314   3.428   8.156  1.00 17.56           S  
-ATOM   5766  CE  MET B 382      74.244   2.154   7.484  1.00 16.04           C  
-ATOM   5767  N   TRP B 383      71.387   4.765  10.191  1.00 13.85           N  
-ATOM   5768  CA  TRP B 383      70.260   5.053   9.306  1.00 15.30           C  
-ATOM   5769  C   TRP B 383      70.653   5.869   8.086  1.00 15.32           C  
-ATOM   5770  O   TRP B 383      71.521   6.739   8.150  1.00 16.60           O  
-ATOM   5771  CB  TRP B 383      69.182   5.879  10.017  1.00 16.63           C  
-ATOM   5772  CG  TRP B 383      68.441   5.209  11.126  1.00 16.69           C  
-ATOM   5773  CD1 TRP B 383      67.319   4.428  11.028  1.00 14.72           C  
-ATOM   5774  CD2 TRP B 383      68.780   5.267  12.510  1.00 17.50           C  
-ATOM   5775  NE1 TRP B 383      66.944   3.998  12.277  1.00 16.47           N  
-ATOM   5776  CE2 TRP B 383      67.827   4.494  13.205  1.00 17.14           C  
-ATOM   5777  CE3 TRP B 383      69.805   5.901  13.237  1.00 17.71           C  
-ATOM   5778  CZ2 TRP B 383      67.866   4.325  14.597  1.00 17.02           C  
-ATOM   5779  CZ3 TRP B 383      69.839   5.731  14.633  1.00 17.75           C  
-ATOM   5780  CH2 TRP B 383      68.876   4.946  15.287  1.00 15.03           C  
-ATOM   5781  N   TRP B 384      69.974   5.586   6.983  1.00 15.76           N  
-ATOM   5782  CA  TRP B 384      70.136   6.348   5.753  1.00 14.65           C  
-ATOM   5783  C   TRP B 384      68.694   6.808   5.526  1.00 16.08           C  
-ATOM   5784  O   TRP B 384      67.851   5.948   5.313  1.00 15.33           O  
-ATOM   5785  CB  TRP B 384      70.525   5.446   4.585  1.00 15.79           C  
-ATOM   5786  CG  TRP B 384      70.623   6.212   3.290  1.00 16.02           C  
-ATOM   5787  CD1 TRP B 384      69.593   6.633   2.500  1.00 17.73           C  
-ATOM   5788  CD2 TRP B 384      71.817   6.741   2.713  1.00 18.21           C  
-ATOM   5789  NE1 TRP B 384      70.075   7.412   1.470  1.00 16.54           N  
-ATOM   5790  CE2 TRP B 384      71.436   7.491   1.574  1.00 16.66           C  
-ATOM   5791  CE3 TRP B 384      73.180   6.657   3.051  1.00 18.37           C  
-ATOM   5792  CZ2 TRP B 384      72.364   8.155   0.767  1.00 18.02           C  
-ATOM   5793  CZ3 TRP B 384      74.112   7.320   2.248  1.00 17.74           C  
-ATOM   5794  CH2 TRP B 384      73.692   8.063   1.114  1.00 17.53           C  
-ATOM   5795  N   ASP B 385      68.422   8.119   5.454  1.00 16.06           N  
-ATOM   5796  CA  ASP B 385      69.380   9.182   5.787  1.00 16.51           C  
-ATOM   5797  C   ASP B 385      68.576  10.127   6.674  1.00 17.91           C  
-ATOM   5798  O   ASP B 385      67.356  10.023   6.731  1.00 16.56           O  
-ATOM   5799  CB  ASP B 385      69.927   9.913   4.555  1.00 16.27           C  
-ATOM   5800  CG  ASP B 385      68.891  10.716   3.862  1.00 19.34           C  
-ATOM   5801  OD1 ASP B 385      68.678  11.882   4.263  1.00 18.71           O  
-ATOM   5802  OD2 ASP B 385      68.278  10.169   2.916  1.00 20.24           O  
-ATOM   5803  N   SER B 386      69.255  11.042   7.353  1.00 16.95           N  
-ATOM   5804  CA  SER B 386      68.597  11.907   8.325  1.00 16.77           C  
-ATOM   5805  C   SER B 386      67.431  12.777   7.924  1.00 17.71           C  
-ATOM   5806  O   SER B 386      66.650  13.176   8.782  1.00 15.79           O  
-ATOM   5807  CB  SER B 386      69.626  12.805   9.007  1.00 17.82           C  
-ATOM   5808  OG  SER B 386      70.113  13.782   8.100  1.00 19.03           O  
-ATOM   5809  N   SER B 387      67.299  13.061   6.633  1.00 17.56           N  
-ATOM   5810  CA  SER B 387      66.256  13.953   6.159  1.00 17.19           C  
-ATOM   5811  C   SER B 387      64.860  13.389   6.063  1.00 19.12           C  
-ATOM   5812  O   SER B 387      63.910  14.158   5.938  1.00 19.05           O  
-ATOM   5813  CB  SER B 387      66.607  14.453   4.755  1.00 16.85           C  
-ATOM   5814  OG  SER B 387      66.415  13.384   3.823  1.00 17.31           O  
-ATOM   5815  N   SER B 388      64.715  12.066   6.112  1.00 19.17           N  
-ATOM   5816  CA  SER B 388      63.390  11.481   5.908  1.00 18.63           C  
-ATOM   5817  C   SER B 388      62.669  10.852   7.090  1.00 18.25           C  
-ATOM   5818  O   SER B 388      61.655  10.189   6.914  1.00 18.91           O  
-ATOM   5819  CB  SER B 388      63.473  10.473   4.770  1.00 19.01           C  
-ATOM   5820  OG  SER B 388      64.545   9.576   5.004  1.00 20.46           O  
-ATOM   5821  N   ASP B 389      63.178  11.061   8.291  1.00 20.17           N  
-ATOM   5822  CA  ASP B 389      62.528  10.505   9.459  1.00 21.38           C  
-ATOM   5823  C   ASP B 389      61.335  11.383   9.816  1.00 22.76           C  
-ATOM   5824  O   ASP B 389      61.214  12.527   9.344  1.00 23.39           O  
-ATOM   5825  CB  ASP B 389      63.503  10.475  10.634  1.00 18.61           C  
-ATOM   5826  CG  ASP B 389      63.049   9.543  11.754  1.00 22.24           C  
-ATOM   5827  OD1 ASP B 389      62.031   8.837  11.576  1.00 18.13           O  
-ATOM   5828  OD2 ASP B 389      63.720   9.509  12.813  1.00 18.81           O  
-ATOM   5829  N   LYS B 390      60.443  10.837  10.630  1.00 20.85           N  
-ATOM   5830  CA  LYS B 390      59.300  11.592  11.107  1.00 20.84           C  
-ATOM   5831  C   LYS B 390      59.786  12.239  12.384  1.00 22.94           C  
-ATOM   5832  O   LYS B 390      60.885  11.930  12.870  1.00 20.73           O  
-ATOM   5833  CB  LYS B 390      58.118  10.681  11.428  1.00 18.00           C  
-ATOM   5834  CG  LYS B 390      57.431  10.133  10.202  1.00 16.66           C  
-ATOM   5835  CD  LYS B 390      56.191   9.343  10.588  1.00 18.87           C  
-ATOM   5836  CE  LYS B 390      55.531   8.722   9.364  1.00 17.33           C  
-ATOM   5837  NZ  LYS B 390      54.190   8.138   9.663  1.00 18.51           N  
-ATOM   5838  N   THR B 391      58.975  13.146  12.917  1.00 22.69           N  
-ATOM   5839  CA  THR B 391      59.295  13.828  14.166  1.00 25.88           C  
-ATOM   5840  C   THR B 391      58.357  13.244  15.219  1.00 27.07           C  
-ATOM   5841  O   THR B 391      57.434  12.497  14.892  1.00 26.14           O  
-ATOM   5842  CB  THR B 391      59.022  15.346  14.049  1.00 29.28           C  
-ATOM   5843  OG1 THR B 391      57.640  15.550  13.732  1.00 27.46           O  
-ATOM   5844  CG2 THR B 391      59.844  15.945  12.933  1.00 30.19           C  
-ATOM   5845  N   GLY B 392      58.595  13.573  16.482  1.00 27.62           N  
-ATOM   5846  CA  GLY B 392      57.730  13.058  17.523  1.00 29.27           C  
-ATOM   5847  C   GLY B 392      58.012  11.597  17.816  1.00 30.06           C  
-ATOM   5848  O   GLY B 392      59.073  11.080  17.453  1.00 28.22           O  
-ATOM   5849  N   SER B 393      57.059  10.930  18.464  1.00 30.37           N  
-ATOM   5850  CA  SER B 393      57.223   9.530  18.841  1.00 30.92           C  
-ATOM   5851  C   SER B 393      57.369   8.565  17.665  1.00 29.04           C  
-ATOM   5852  O   SER B 393      57.966   7.501  17.821  1.00 29.64           O  
-ATOM   5853  CB  SER B 393      56.058   9.097  19.741  1.00 33.85           C  
-ATOM   5854  OG  SER B 393      54.815   9.344  19.109  1.00 36.33           O  
-ATOM   5855  N   ASP B 394      56.836   8.935  16.495  1.00 25.81           N  
-ATOM   5856  CA  ASP B 394      56.930   8.080  15.310  1.00 24.60           C  
-ATOM   5857  C   ASP B 394      58.307   8.131  14.634  1.00 22.11           C  
-ATOM   5858  O   ASP B 394      58.529   7.465  13.627  1.00 21.94           O  
-ATOM   5859  CB  ASP B 394      55.854   8.435  14.281  1.00 29.18           C  
-ATOM   5860  CG  ASP B 394      54.453   8.054  14.741  1.00 35.36           C  
-ATOM   5861  OD1 ASP B 394      54.303   7.025  15.448  1.00 34.58           O  
-ATOM   5862  OD2 ASP B 394      53.503   8.778  14.377  1.00 37.94           O  
-ATOM   5863  N   SER B 395      59.215   8.929  15.181  1.00 18.37           N  
-ATOM   5864  CA  SER B 395      60.562   9.007  14.652  1.00 19.16           C  
-ATOM   5865  C   SER B 395      61.146   7.625  14.863  1.00 19.55           C  
-ATOM   5866  O   SER B 395      61.046   7.076  15.978  1.00 17.43           O  
-ATOM   5867  CB  SER B 395      61.396   9.988  15.449  1.00 16.16           C  
-ATOM   5868  OG  SER B 395      62.776   9.711  15.248  1.00 17.55           O  
-ATOM   5869  N   LEU B 396      61.745   7.054  13.828  1.00 17.12           N  
-ATOM   5870  CA  LEU B 396      62.328   5.715  13.980  1.00 18.66           C  
-ATOM   5871  C   LEU B 396      63.592   5.796  14.810  1.00 18.17           C  
-ATOM   5872  O   LEU B 396      63.900   4.886  15.578  1.00 21.08           O  
-ATOM   5873  CB  LEU B 396      62.634   5.079  12.622  1.00 14.86           C  
-ATOM   5874  CG  LEU B 396      61.374   4.820  11.780  1.00 18.73           C  
-ATOM   5875  CD1 LEU B 396      61.781   4.028  10.532  1.00 14.64           C  
-ATOM   5876  CD2 LEU B 396      60.311   4.049  12.584  1.00 15.02           C  
-ATOM   5877  N   ILE B 397      64.325   6.895  14.674  1.00 18.63           N  
-ATOM   5878  CA  ILE B 397      65.533   7.050  15.465  1.00 18.32           C  
-ATOM   5879  C   ILE B 397      65.166   7.121  16.953  1.00 19.75           C  
-ATOM   5880  O   ILE B 397      65.762   6.443  17.793  1.00 19.81           O  
-ATOM   5881  CB  ILE B 397      66.290   8.323  15.049  1.00 17.98           C  
-ATOM   5882  CG1 ILE B 397      66.908   8.114  13.651  1.00 17.74           C  
-ATOM   5883  CG2 ILE B 397      67.327   8.667  16.103  1.00 17.62           C  
-ATOM   5884  CD1 ILE B 397      67.726   9.305  13.118  1.00 17.60           C  
-ATOM   5885  N   THR B 398      64.197   7.961  17.286  1.00 19.63           N  
-ATOM   5886  CA  THR B 398      63.778   8.081  18.686  1.00 20.12           C  
-ATOM   5887  C   THR B 398      63.287   6.718  19.189  1.00 20.56           C  
-ATOM   5888  O   THR B 398      63.667   6.269  20.272  1.00 21.89           O  
-ATOM   5889  CB  THR B 398      62.669   9.121  18.807  1.00 20.41           C  
-ATOM   5890  OG1 THR B 398      63.180  10.372  18.321  1.00 20.66           O  
-ATOM   5891  CG2 THR B 398      62.211   9.293  20.277  1.00 22.77           C  
-ATOM   5892  N   THR B 399      62.471   6.058  18.376  1.00 20.20           N  
-ATOM   5893  CA  THR B 399      61.913   4.753  18.720  1.00 20.72           C  
-ATOM   5894  C   THR B 399      63.013   3.744  19.052  1.00 20.46           C  
-ATOM   5895  O   THR B 399      62.924   3.023  20.049  1.00 19.26           O  
-ATOM   5896  CB  THR B 399      61.072   4.190  17.550  1.00 21.67           C  
-ATOM   5897  OG1 THR B 399      59.936   5.032  17.333  1.00 22.49           O  
-ATOM   5898  CG2 THR B 399      60.594   2.772  17.855  1.00 18.92           C  
-ATOM   5899  N   VAL B 400      64.046   3.697  18.218  1.00 19.21           N  
-ATOM   5900  CA  VAL B 400      65.140   2.754  18.424  1.00 17.81           C  
-ATOM   5901  C   VAL B 400      65.951   3.123  19.662  1.00 19.85           C  
-ATOM   5902  O   VAL B 400      66.254   2.262  20.498  1.00 20.03           O  
-ATOM   5903  CB  VAL B 400      66.077   2.712  17.192  1.00 18.47           C  
-ATOM   5904  CG1 VAL B 400      67.331   1.952  17.513  1.00 20.03           C  
-ATOM   5905  CG2 VAL B 400      65.365   2.057  16.011  1.00 15.33           C  
-ATOM   5906  N   VAL B 401      66.292   4.402  19.789  1.00 18.20           N  
-ATOM   5907  CA  VAL B 401      67.089   4.856  20.928  1.00 17.65           C  
-ATOM   5908  C   VAL B 401      66.339   4.545  22.224  1.00 20.26           C  
-ATOM   5909  O   VAL B 401      66.940   4.120  23.205  1.00 22.96           O  
-ATOM   5910  CB  VAL B 401      67.384   6.388  20.826  1.00 19.12           C  
-ATOM   5911  CG1 VAL B 401      68.033   6.909  22.121  1.00 17.44           C  
-ATOM   5912  CG2 VAL B 401      68.310   6.639  19.649  1.00 16.57           C  
-ATOM   5913  N   ASN B 402      65.029   4.742  22.229  1.00 17.96           N  
-ATOM   5914  CA  ASN B 402      64.264   4.441  23.425  1.00 19.40           C  
-ATOM   5915  C   ASN B 402      64.305   2.931  23.688  1.00 20.23           C  
-ATOM   5916  O   ASN B 402      64.538   2.482  24.819  1.00 18.62           O  
-ATOM   5917  CB  ASN B 402      62.807   4.874  23.267  1.00 19.84           C  
-ATOM   5918  CG  ASN B 402      62.631   6.393  23.355  1.00 26.24           C  
-ATOM   5919  OD1 ASN B 402      63.506   7.097  23.854  1.00 27.26           O  
-ATOM   5920  ND2 ASN B 402      61.487   6.891  22.897  1.00 27.87           N  
-ATOM   5921  N   ALA B 403      64.073   2.153  22.639  1.00 19.49           N  
-ATOM   5922  CA  ALA B 403      64.039   0.697  22.778  1.00 22.92           C  
-ATOM   5923  C   ALA B 403      65.395   0.124  23.198  1.00 23.63           C  
-ATOM   5924  O   ALA B 403      65.448  -0.912  23.848  1.00 22.78           O  
-ATOM   5925  CB  ALA B 403      63.570   0.056  21.472  1.00 22.25           C  
-ATOM   5926  N   LEU B 404      66.486   0.786  22.824  1.00 21.90           N  
-ATOM   5927  CA  LEU B 404      67.802   0.305  23.214  1.00 22.42           C  
-ATOM   5928  C   LEU B 404      68.113   0.609  24.680  1.00 23.76           C  
-ATOM   5929  O   LEU B 404      69.090   0.089  25.228  1.00 23.51           O  
-ATOM   5930  CB  LEU B 404      68.887   0.948  22.365  1.00 21.10           C  
-ATOM   5931  CG  LEU B 404      68.971   0.525  20.898  1.00 22.71           C  
-ATOM   5932  CD1 LEU B 404      70.101   1.308  20.257  1.00 20.56           C  
-ATOM   5933  CD2 LEU B 404      69.236  -0.983  20.767  1.00 16.60           C  
-ATOM   5934  N   GLY B 405      67.317   1.482  25.295  1.00 24.89           N  
-ATOM   5935  CA  GLY B 405      67.551   1.833  26.688  1.00 25.69           C  
-ATOM   5936  C   GLY B 405      67.765   3.325  26.910  1.00 27.39           C  
-ATOM   5937  O   GLY B 405      68.087   3.752  28.028  1.00 24.91           O  
-ATOM   5938  N   GLY B 406      67.588   4.137  25.867  1.00 25.41           N  
-ATOM   5939  CA  GLY B 406      67.797   5.569  26.047  1.00 25.08           C  
-ATOM   5940  C   GLY B 406      69.230   6.007  25.787  1.00 25.26           C  
-ATOM   5941  O   GLY B 406      70.111   5.182  25.560  1.00 23.21           O  
-ATOM   5942  N   THR B 407      69.478   7.314  25.826  1.00 27.63           N  
-ATOM   5943  CA  THR B 407      70.817   7.827  25.549  1.00 28.54           C  
-ATOM   5944  C   THR B 407      71.841   7.347  26.568  1.00 27.11           C  
-ATOM   5945  O   THR B 407      73.043   7.379  26.324  1.00 28.32           O  
-ATOM   5946  CB  THR B 407      70.792   9.354  25.500  1.00 30.91           C  
-ATOM   5947  OG1 THR B 407      70.295   9.854  26.742  1.00 31.83           O  
-ATOM   5948  CG2 THR B 407      69.851   9.824  24.382  1.00 27.16           C  
-ATOM   5949  N   GLY B 408      71.353   6.874  27.706  1.00 28.08           N  
-ATOM   5950  CA  GLY B 408      72.244   6.377  28.735  1.00 25.57           C  
-ATOM   5951  C   GLY B 408      73.059   5.170  28.311  1.00 26.75           C  
-ATOM   5952  O   GLY B 408      74.130   4.923  28.864  1.00 28.91           O  
-ATOM   5953  N   VAL B 409      72.576   4.408  27.335  1.00 24.66           N  
-ATOM   5954  CA  VAL B 409      73.307   3.218  26.900  1.00 24.02           C  
-ATOM   5955  C   VAL B 409      74.233   3.490  25.701  1.00 24.35           C  
-ATOM   5956  O   VAL B 409      74.867   2.578  25.159  1.00 26.00           O  
-ATOM   5957  CB  VAL B 409      72.319   2.073  26.575  1.00 23.75           C  
-ATOM   5958  CG1 VAL B 409      71.426   1.815  27.792  1.00 25.36           C  
-ATOM   5959  CG2 VAL B 409      71.472   2.416  25.366  1.00 18.73           C  
-ATOM   5960  N   PHE B 410      74.323   4.755  25.298  1.00 24.17           N  
-ATOM   5961  CA  PHE B 410      75.193   5.139  24.186  1.00 23.95           C  
-ATOM   5962  C   PHE B 410      76.668   5.013  24.523  1.00 24.96           C  
-ATOM   5963  O   PHE B 410      77.076   5.280  25.655  1.00 24.17           O  
-ATOM   5964  CB  PHE B 410      74.979   6.609  23.800  1.00 23.96           C  
-ATOM   5965  CG  PHE B 410      73.739   6.868  23.009  1.00 25.53           C  
-ATOM   5966  CD1 PHE B 410      72.914   5.815  22.612  1.00 23.10           C  
-ATOM   5967  CD2 PHE B 410      73.419   8.171  22.607  1.00 24.87           C  
-ATOM   5968  CE1 PHE B 410      71.802   6.056  21.827  1.00 23.02           C  
-ATOM   5969  CE2 PHE B 410      72.293   8.416  21.813  1.00 24.91           C  
-ATOM   5970  CZ  PHE B 410      71.485   7.348  21.422  1.00 24.64           C  
-ATOM   5971  N   GLU B 411      77.464   4.633  23.532  1.00 25.91           N  
-ATOM   5972  CA  GLU B 411      78.912   4.573  23.692  1.00 27.09           C  
-ATOM   5973  C   GLU B 411      79.332   6.025  23.999  1.00 27.72           C  
-ATOM   5974  O   GLU B 411      78.875   6.946  23.334  1.00 26.59           O  
-ATOM   5975  CB  GLU B 411      79.561   4.155  22.378  1.00 28.22           C  
-ATOM   5976  CG  GLU B 411      81.071   4.337  22.352  1.00 31.96           C  
-ATOM   5977  CD  GLU B 411      81.643   4.148  20.958  1.00 34.95           C  
-ATOM   5978  OE1 GLU B 411      81.384   5.012  20.085  1.00 36.42           O  
-ATOM   5979  OE2 GLU B 411      82.345   3.136  20.737  1.00 34.85           O  
-ATOM   5980  N   GLN B 412      80.182   6.229  24.999  1.00 28.36           N  
-ATOM   5981  CA  GLN B 412      80.635   7.570  25.358  1.00 30.22           C  
-ATOM   5982  C   GLN B 412      82.081   7.784  24.952  1.00 31.07           C  
-ATOM   5983  O   GLN B 412      82.945   6.992  25.322  1.00 32.13           O  
-ATOM   5984  CB  GLN B 412      80.547   7.783  26.864  1.00 32.98           C  
-ATOM   5985  CG  GLN B 412      79.159   7.722  27.426  1.00 34.81           C  
-ATOM   5986  CD  GLN B 412      78.251   8.798  26.867  1.00 36.96           C  
-ATOM   5987  OE1 GLN B 412      78.602   9.978  26.849  1.00 38.03           O  
-ATOM   5988  NE2 GLN B 412      77.072   8.397  26.417  1.00 34.69           N  
-ATOM   5989  N   SER B 413      82.346   8.839  24.183  1.00 31.24           N  
-ATOM   5990  CA  SER B 413      83.712   9.169  23.776  1.00 33.61           C  
-ATOM   5991  C   SER B 413      83.697  10.589  23.214  1.00 35.40           C  
-ATOM   5992  O   SER B 413      83.055  10.859  22.193  1.00 36.03           O  
-ATOM   5993  CB  SER B 413      84.243   8.180  22.735  1.00 33.81           C  
-ATOM   5994  OG  SER B 413      83.774   8.498  21.443  1.00 38.57           O  
-ATOM   5995  N   GLN B 414      84.393  11.491  23.907  1.00 34.61           N  
-ATOM   5996  CA  GLN B 414      84.468  12.904  23.540  1.00 34.28           C  
-ATOM   5997  C   GLN B 414      84.958  13.132  22.132  1.00 29.65           C  
-ATOM   5998  O   GLN B 414      85.911  12.498  21.682  1.00 29.64           O  
-ATOM   5999  CB  GLN B 414      85.395  13.656  24.503  1.00 37.72           C  
-ATOM   6000  CG  GLN B 414      84.870  13.707  25.921  1.00 45.15           C  
-ATOM   6001  CD  GLN B 414      83.975  14.907  26.176  1.00 46.60           C  
-ATOM   6002  OE1 GLN B 414      84.462  16.027  26.345  1.00 48.86           O  
-ATOM   6003  NE2 GLN B 414      82.663  14.679  26.206  1.00 47.77           N  
-ATOM   6004  N   ASN B 415      84.299  14.032  21.418  1.00 29.92           N  
-ATOM   6005  CA  ASN B 415      84.752  14.318  20.062  1.00 28.53           C  
-ATOM   6006  C   ASN B 415      85.958  15.256  20.169  1.00 29.49           C  
-ATOM   6007  O   ASN B 415      86.398  15.587  21.279  1.00 26.63           O  
-ATOM   6008  CB  ASN B 415      83.641  14.980  19.230  1.00 27.51           C  
-ATOM   6009  CG  ASN B 415      83.101  16.238  19.858  1.00 26.39           C  
-ATOM   6010  OD1 ASN B 415      83.787  16.921  20.621  1.00 25.83           O  
-ATOM   6011  ND2 ASN B 415      81.861  16.577  19.512  1.00 27.17           N  
-ATOM   6012  N   GLU B 416      86.479  15.665  19.012  1.00 29.02           N  
-ATOM   6013  CA  GLU B 416      87.613  16.569  18.920  1.00 29.40           C  
-ATOM   6014  C   GLU B 416      87.133  17.945  18.491  1.00 31.44           C  
-ATOM   6015  O   GLU B 416      86.467  18.066  17.463  1.00 29.89           O  
-ATOM   6016  CB  GLU B 416      88.615  16.063  17.880  1.00 30.21           C  
-ATOM   6017  CG  GLU B 416      89.762  17.054  17.646  1.00 31.19           C  
-ATOM   6018  CD  GLU B 416      90.597  17.258  18.915  1.00 32.88           C  
-ATOM   6019  OE1 GLU B 416      91.457  16.400  19.189  1.00 35.85           O  
-ATOM   6020  OE2 GLU B 416      90.377  18.252  19.641  1.00 29.92           O  
-ATOM   6021  N   LEU B 417      87.464  18.988  19.252  1.00 30.95           N  
-ATOM   6022  CA  LEU B 417      87.038  20.332  18.864  1.00 31.52           C  
-ATOM   6023  C   LEU B 417      88.190  21.221  18.389  1.00 34.00           C  
-ATOM   6024  O   LEU B 417      87.977  22.254  17.756  1.00 32.60           O  
-ATOM   6025  CB  LEU B 417      86.303  21.032  20.008  1.00 31.06           C  
-ATOM   6026  CG  LEU B 417      84.941  20.481  20.457  1.00 32.22           C  
-ATOM   6027  CD1 LEU B 417      84.360  21.394  21.523  1.00 31.34           C  
-ATOM   6028  CD2 LEU B 417      83.981  20.404  19.284  1.00 29.38           C  
-ATOM   6029  N   ASP B 418      89.413  20.802  18.672  1.00 34.79           N  
-ATOM   6030  CA  ASP B 418      90.573  21.581  18.295  1.00 34.25           C  
-ATOM   6031  C   ASP B 418      91.159  21.130  16.972  1.00 33.43           C  
-ATOM   6032  O   ASP B 418      91.441  19.954  16.781  1.00 32.70           O  
-ATOM   6033  CB  ASP B 418      91.628  21.479  19.405  1.00 37.78           C  
-ATOM   6034  CG  ASP B 418      92.771  22.475  19.231  1.00 41.11           C  
-ATOM   6035  OD1 ASP B 418      92.498  23.693  19.102  1.00 40.41           O  
-ATOM   6036  OD2 ASP B 418      93.939  22.032  19.237  1.00 43.17           O  
-ATOM   6037  N   TYR B 419      91.330  22.082  16.057  1.00 32.55           N  
-ATOM   6038  CA  TYR B 419      91.908  21.819  14.739  1.00 33.43           C  
-ATOM   6039  C   TYR B 419      92.874  22.981  14.481  1.00 36.30           C  
-ATOM   6040  O   TYR B 419      92.590  23.882  13.694  1.00 33.57           O  
-ATOM   6041  CB  TYR B 419      90.796  21.753  13.677  1.00 31.98           C  
-ATOM   6042  CG  TYR B 419      89.941  20.509  13.839  1.00 30.96           C  
-ATOM   6043  CD1 TYR B 419      88.892  20.470  14.763  1.00 28.54           C  
-ATOM   6044  CD2 TYR B 419      90.268  19.329  13.170  1.00 30.36           C  
-ATOM   6045  CE1 TYR B 419      88.192  19.267  15.028  1.00 29.46           C  
-ATOM   6046  CE2 TYR B 419      89.579  18.124  13.430  1.00 31.46           C  
-ATOM   6047  CZ  TYR B 419      88.551  18.107  14.362  1.00 27.28           C  
-ATOM   6048  OH  TYR B 419      87.908  16.922  14.656  1.00 32.49           O  
-ATOM   6049  N   PRO B 420      94.035  22.960  15.164  1.00 37.74           N  
-ATOM   6050  CA  PRO B 420      95.079  23.984  15.070  1.00 38.51           C  
-ATOM   6051  C   PRO B 420      95.722  24.241  13.714  1.00 38.63           C  
-ATOM   6052  O   PRO B 420      96.178  25.348  13.477  1.00 41.04           O  
-ATOM   6053  CB  PRO B 420      96.087  23.544  16.133  1.00 38.24           C  
-ATOM   6054  CG  PRO B 420      95.988  22.068  16.092  1.00 38.86           C  
-ATOM   6055  CD  PRO B 420      94.482  21.845  16.020  1.00 38.44           C  
-ATOM   6056  N   VAL B 421      95.771  23.246  12.835  1.00 37.55           N  
-ATOM   6057  CA  VAL B 421      96.362  23.453  11.519  1.00 37.58           C  
-ATOM   6058  C   VAL B 421      95.298  23.594  10.416  1.00 38.49           C  
-ATOM   6059  O   VAL B 421      95.575  23.342   9.233  1.00 38.40           O  
-ATOM   6060  CB  VAL B 421      97.327  22.315  11.134  1.00 38.98           C  
-ATOM   6061  CG1 VAL B 421      98.601  22.412  11.964  1.00 41.44           C  
-ATOM   6062  CG2 VAL B 421      96.655  20.972  11.340  1.00 42.90           C  
-ATOM   6063  N   SER B 422      94.087  23.990  10.806  1.00 35.67           N  
-ATOM   6064  CA  SER B 422      93.005  24.181   9.842  1.00 34.14           C  
-ATOM   6065  C   SER B 422      93.242  25.476   9.083  1.00 34.55           C  
-ATOM   6066  O   SER B 422      93.561  26.501   9.682  1.00 33.36           O  
-ATOM   6067  CB  SER B 422      91.652  24.285  10.540  1.00 32.41           C  
-ATOM   6068  OG  SER B 422      90.662  24.742   9.620  1.00 27.50           O  
-ATOM   6069  N   GLN B 423      93.071  25.429   7.769  1.00 34.07           N  
-ATOM   6070  CA  GLN B 423      93.258  26.610   6.947  1.00 33.43           C  
-ATOM   6071  C   GLN B 423      92.133  27.612   7.192  1.00 32.29           C  
-ATOM   6072  O   GLN B 423      92.227  28.764   6.793  1.00 31.75           O  
-ATOM   6073  CB  GLN B 423      93.279  26.232   5.460  1.00 35.22           C  
-ATOM   6074  CG  GLN B 423      91.969  25.670   4.959  1.00 35.83           C  
-ATOM   6075  CD  GLN B 423      91.860  25.695   3.439  1.00 39.35           C  
-ATOM   6076  OE1 GLN B 423      91.718  26.763   2.835  1.00 38.74           O  
-ATOM   6077  NE2 GLN B 423      91.927  24.516   2.814  1.00 37.75           N  
-ATOM   6078  N   TYR B 424      91.059  27.182   7.841  1.00 28.48           N  
-ATOM   6079  CA  TYR B 424      89.957  28.101   8.088  1.00 27.67           C  
-ATOM   6080  C   TYR B 424      90.072  28.737   9.458  1.00 29.70           C  
-ATOM   6081  O   TYR B 424      90.035  28.048  10.484  1.00 29.04           O  
-ATOM   6082  CB  TYR B 424      88.611  27.382   7.952  1.00 29.05           C  
-ATOM   6083  CG  TYR B 424      88.420  26.795   6.574  1.00 30.50           C  
-ATOM   6084  CD1 TYR B 424      88.231  27.628   5.466  1.00 30.36           C  
-ATOM   6085  CD2 TYR B 424      88.491  25.418   6.361  1.00 28.14           C  
-ATOM   6086  CE1 TYR B 424      88.117  27.107   4.171  1.00 32.13           C  
-ATOM   6087  CE2 TYR B 424      88.383  24.880   5.064  1.00 31.31           C  
-ATOM   6088  CZ  TYR B 424      88.196  25.735   3.977  1.00 31.99           C  
-ATOM   6089  OH  TYR B 424      88.109  25.236   2.697  1.00 34.73           O  
-ATOM   6090  N   ASP B 425      90.186  30.060   9.466  1.00 29.40           N  
-ATOM   6091  CA  ASP B 425      90.341  30.820  10.698  1.00 31.27           C  
-ATOM   6092  C   ASP B 425      89.206  30.637  11.679  1.00 30.38           C  
-ATOM   6093  O   ASP B 425      89.435  30.444  12.877  1.00 30.14           O  
-ATOM   6094  CB  ASP B 425      90.489  32.303  10.373  1.00 35.20           C  
-ATOM   6095  CG  ASP B 425      91.693  32.581   9.501  1.00 38.48           C  
-ATOM   6096  OD1 ASP B 425      92.825  32.550  10.022  1.00 42.61           O  
-ATOM   6097  OD2 ASP B 425      91.512  32.809   8.287  1.00 42.11           O  
-ATOM   6098  N   ASN B 426      87.976  30.705  11.195  1.00 28.84           N  
-ATOM   6099  CA  ASN B 426      86.875  30.544  12.118  1.00 28.02           C  
-ATOM   6100  C   ASN B 426      86.830  29.173  12.803  1.00 29.81           C  
-ATOM   6101  O   ASN B 426      86.581  29.094  14.012  1.00 29.20           O  
-ATOM   6102  CB  ASN B 426      85.540  30.884  11.441  1.00 27.18           C  
-ATOM   6103  CG  ASN B 426      85.171  29.950  10.278  1.00 22.89           C  
-ATOM   6104  OD1 ASN B 426      86.011  29.297   9.650  1.00 24.74           O  
-ATOM   6105  ND2 ASN B 426      83.888  29.932   9.973  1.00 20.11           N  
-ATOM   6106  N   LEU B 427      87.103  28.107  12.059  1.00 30.11           N  
-ATOM   6107  CA  LEU B 427      87.074  26.767  12.641  1.00 32.05           C  
-ATOM   6108  C   LEU B 427      88.300  26.531  13.521  1.00 34.58           C  
-ATOM   6109  O   LEU B 427      88.205  25.899  14.584  1.00 32.13           O  
-ATOM   6110  CB  LEU B 427      87.027  25.701  11.544  1.00 29.35           C  
-ATOM   6111  CG  LEU B 427      86.593  24.295  12.000  1.00 34.03           C  
-ATOM   6112  CD1 LEU B 427      85.743  23.626  10.891  1.00 30.31           C  
-ATOM   6113  CD2 LEU B 427      87.816  23.450  12.353  1.00 28.62           C  
-ATOM   6114  N   ARG B 428      89.451  27.042  13.083  1.00 34.76           N  
-ATOM   6115  CA  ARG B 428      90.675  26.859  13.853  1.00 36.19           C  
-ATOM   6116  C   ARG B 428      90.512  27.495  15.219  1.00 35.77           C  
-ATOM   6117  O   ARG B 428      91.007  26.972  16.216  1.00 36.56           O  
-ATOM   6118  CB  ARG B 428      91.871  27.489  13.140  1.00 37.88           C  
-ATOM   6119  CG  ARG B 428      93.203  27.149  13.780  1.00 39.08           C  
-ATOM   6120  CD  ARG B 428      94.346  27.832  13.039  1.00 43.45           C  
-ATOM   6121  NE  ARG B 428      94.211  29.280  13.101  1.00 43.61           N  
-ATOM   6122  CZ  ARG B 428      93.931  30.046  12.057  1.00 45.65           C  
-ATOM   6123  NH1 ARG B 428      93.763  29.492  10.856  1.00 46.87           N  
-ATOM   6124  NH2 ARG B 428      93.799  31.362  12.219  1.00 44.98           N  
-ATOM   6125  N   ASN B 429      89.803  28.617  15.251  1.00 36.03           N  
-ATOM   6126  CA  ASN B 429      89.565  29.344  16.486  1.00 37.95           C  
-ATOM   6127  C   ASN B 429      88.377  28.808  17.273  1.00 37.58           C  
-ATOM   6128  O   ASN B 429      87.945  29.439  18.228  1.00 37.03           O  
-ATOM   6129  CB  ASN B 429      89.348  30.833  16.199  1.00 41.49           C  
-ATOM   6130  CG  ASN B 429      90.587  31.508  15.611  1.00 45.99           C  
-ATOM   6131  OD1 ASN B 429      90.499  32.612  15.066  1.00 50.29           O  
-ATOM   6132  ND2 ASN B 429      91.742  30.857  15.725  1.00 45.50           N  
-ATOM   6133  N   GLY B 430      87.832  27.661  16.868  1.00 36.93           N  
-ATOM   6134  CA  GLY B 430      86.719  27.081  17.608  1.00 34.73           C  
-ATOM   6135  C   GLY B 430      85.333  27.631  17.334  1.00 34.64           C  
-ATOM   6136  O   GLY B 430      84.409  27.468  18.148  1.00 30.27           O  
-ATOM   6137  N   MET B 431      85.191  28.304  16.198  1.00 34.62           N  
-ATOM   6138  CA  MET B 431      83.903  28.843  15.781  1.00 35.01           C  
-ATOM   6139  C   MET B 431      83.240  29.711  16.838  1.00 37.22           C  
-ATOM   6140  O   MET B 431      82.251  29.317  17.447  1.00 37.93           O  
-ATOM   6141  CB  MET B 431      82.964  27.682  15.412  1.00 33.88           C  
-ATOM   6142  CG  MET B 431      81.971  27.972  14.299  1.00 33.27           C  
-ATOM   6143  SD  MET B 431      82.776  28.396  12.727  1.00 29.72           S  
-ATOM   6144  CE  MET B 431      83.400  26.825  12.147  1.00 30.13           C  
-ATOM   6145  N   GLN B 432      83.776  30.903  17.052  1.00 39.91           N  
-ATOM   6146  CA  GLN B 432      83.205  31.816  18.029  1.00 41.13           C  
-ATOM   6147  C   GLN B 432      82.015  32.558  17.433  1.00 41.61           C  
-ATOM   6148  O   GLN B 432      81.890  32.559  16.188  1.00 41.59           O  
-ATOM   6149  CB  GLN B 432      84.267  32.814  18.472  1.00 43.02           C  
-ATOM   6150  CG  GLN B 432      85.541  32.155  18.961  1.00 46.05           C  
-ATOM   6151  CD  GLN B 432      85.261  31.127  20.037  1.00 48.41           C  
-ATOM   6152  OE1 GLN B 432      84.325  31.282  20.826  1.00 49.05           O  
-ATOM   6153  NE2 GLN B 432      86.072  30.074  20.082  1.00 49.09           N  
-ATOM   6154  N   THR B 433      81.231  33.148  18.213  1.00 42.23           N  
-TER    6155      THR B 433                                                      
-HETATM 6156  S   SO4 A1434      77.668  42.132  10.391  0.75 49.73           S  
-HETATM 6157  O1  SO4 A1434      78.418  42.027   9.127  0.75 52.73           O  
-HETATM 6158  O2  SO4 A1434      77.191  43.519  10.554  0.75 53.57           O  
-HETATM 6159  O3  SO4 A1434      76.517  41.222  10.343  0.75 53.04           O  
-HETATM 6160  O4  SO4 A1434      78.530  41.775  11.529  0.75 51.73           O  
-HETATM 6161  S   SO4 A1435      64.865  67.633 -18.919  0.75 54.16           S  
-HETATM 6162  O1  SO4 A1435      64.043  68.853 -18.927  0.75 56.35           O  
-HETATM 6163  O2  SO4 A1435      65.630  67.598 -17.665  0.75 56.17           O  
-HETATM 6164  O3  SO4 A1435      64.003  66.441 -18.975  0.75 54.64           O  
-HETATM 6165  O4  SO4 A1435      65.778  67.648 -20.077  0.75 54.82           O  
-HETATM 6166  S   SO4 A1436      73.469  83.302 -12.101  0.75 55.07           S  
-HETATM 6167  O1  SO4 A1436      74.012  82.559 -10.949  0.75 56.45           O  
-HETATM 6168  O2  SO4 A1436      72.997  84.623 -11.652  0.75 55.56           O  
-HETATM 6169  O3  SO4 A1436      74.535  83.489 -13.105  0.75 56.14           O  
-HETATM 6170  O4  SO4 A1436      72.346  82.550 -12.686  0.75 54.11           O  
-HETATM 6171  S   SO4 A1437      68.972  77.475   0.142  1.00 36.63           S  
-HETATM 6172  O1  SO4 A1437      69.519  78.443  -0.827  1.00 33.19           O  
-HETATM 6173  O2  SO4 A1437      67.568  77.801   0.485  1.00 38.60           O  
-HETATM 6174  O3  SO4 A1437      69.013  76.088  -0.364  1.00 29.72           O  
-HETATM 6175  O4  SO4 A1437      69.804  77.597   1.359  1.00 39.32           O  
-HETATM 6176  S   SO4 A1438     119.333  76.647  -4.581  0.50 49.45           S  
-HETATM 6177  O1  SO4 A1438     120.284  76.735  -5.700  0.50 50.70           O  
-HETATM 6178  O2  SO4 A1438     119.830  77.470  -3.464  0.50 50.15           O  
-HETATM 6179  O3  SO4 A1438     118.012  77.141  -5.016  0.50 49.36           O  
-HETATM 6180  O4  SO4 A1438     119.218  75.247  -4.145  0.50 49.51           O  
-HETATM 6181  S   SO4 A1439     106.861  85.964  10.813  0.75 52.37           S  
-HETATM 6182  O1  SO4 A1439     108.235  85.973  10.261  0.75 53.26           O  
-HETATM 6183  O2  SO4 A1439     106.621  87.212  11.559  0.75 50.05           O  
-HETATM 6184  O3  SO4 A1439     105.880  85.857   9.707  0.75 53.71           O  
-HETATM 6185  O4  SO4 A1439     106.709  84.812  11.717  0.75 51.23           O  
-HETATM 6186  O6 AD1H A1440      95.330  67.469  -6.707  0.75 26.94           O  
-HETATM 6187  C6 AD1H A1440      94.166  67.622  -6.343  0.75 29.99           C  
-HETATM 6188  C5 AD1H A1440      93.865  68.436  -5.255  0.75 28.91           C  
-HETATM 6189  N7 AD1H A1440      94.595  69.061  -4.338  0.75 30.08           N  
-HETATM 6190  CAAAD1H A1440      96.074  69.133  -4.309  0.75 30.28           C  
-HETATM 6191  C8 AD1H A1440      93.799  69.648  -3.448  0.75 30.99           C  
-HETATM 6192  N9 AD1H A1440      92.540  69.404  -3.804  0.75 29.86           N  
-HETATM 6193  C4 AD1H A1440      92.539  68.665  -4.910  0.75 28.29           C  
-HETATM 6194  N3 AD1H A1440      91.497  68.102  -5.661  0.75 28.07           N  
-HETATM 6195  CACAD1H A1440      90.093  68.350  -5.270  0.75 25.83           C  
-HETATM 6196  C2 AD1H A1440      91.795  67.279  -6.757  0.75 28.66           C  
-HETATM 6197  O2 AD1H A1440      90.903  66.844  -7.486  0.75 28.63           O  
-HETATM 6198  N1 AD1H A1440      93.132  67.015  -7.073  0.75 31.82           N  
-HETATM 6199  CAKAD1H A1440      93.448  65.853  -7.930  0.75 28.89           C  
-HETATM 6200  CALAD1H A1440      93.584  66.254  -9.399  0.75 28.89           C  
-HETATM 6201  NBBAD1H A1440      93.835  65.003 -10.142  0.75 27.79           N  
-HETATM 6202  CAPAD1H A1440      95.148  64.531 -10.291  0.75 27.90           C  
-HETATM 6203  OAFAD1H A1440      96.078  65.122  -9.744  0.75 26.45           O  
-HETATM 6204  CAVAD1H A1440      95.385  63.352 -10.990  0.75 25.99           C  
-HETATM 6205  NAXAD1H A1440      96.480  62.655 -11.273  0.75 28.94           N  
-HETATM 6206  CABAD1H A1440      97.860  63.037 -10.892  0.75 29.03           C  
-HETATM 6207  CAJAD1H A1440      96.156  61.558 -11.952  0.75 28.12           C  
-HETATM 6208  NANAD1H A1440      94.833  61.551 -12.108  0.75 28.28           N  
-HETATM 6209  CATAD1H A1440      94.323  62.638 -11.533  0.75 28.15           C  
-HETATM 6210  NAZAD1H A1440      93.008  63.102 -11.387  0.75 26.70           N  
-HETATM 6211  CADAD1H A1440      91.889  62.353 -12.001  0.75 25.04           C  
-HETATM 6212  CARAD1H A1440      92.759  64.288 -10.684  0.75 28.32           C  
-HETATM 6213  OAHAD1H A1440      91.606  64.671 -10.479  0.75 28.49           O  
-HETATM 6214  O6 BD1H A1440      95.318  68.062  -6.938  0.25 32.34           O  
-HETATM 6215  C6 BD1H A1440      94.153  68.066  -6.545  0.25 32.67           C  
-HETATM 6216  C5 BD1H A1440      93.850  68.556  -5.279  0.25 32.85           C  
-HETATM 6217  N7 BD1H A1440      94.570  69.052  -4.276  0.25 33.37           N  
-HETATM 6218  CAABD1H A1440      96.036  69.256  -4.282  0.25 33.68           C  
-HETATM 6219  C8 BD1H A1440      93.779  69.352  -3.251  0.25 33.50           C  
-HETATM 6220  N9 BD1H A1440      92.529  69.053  -3.599  0.25 32.99           N  
-HETATM 6221  C4 BD1H A1440      92.532  68.564  -4.837  0.25 32.65           C  
-HETATM 6222  N3 BD1H A1440      91.504  68.085  -5.660  0.25 32.57           N  
-HETATM 6223  CACBD1H A1440      90.109  68.089  -5.166  0.25 32.15           C  
-HETATM 6224  C2 BD1H A1440      91.804  67.588  -6.936  0.25 32.45           C  
-HETATM 6225  O2 BD1H A1440      90.908  67.171  -7.670  0.25 32.52           O  
-HETATM 6226  N1 BD1H A1440      93.135  67.574  -7.375  0.25 33.01           N  
-HETATM 6227  CAKBD1H A1440      93.469  66.933  -8.669  0.25 31.58           C  
-HETATM 6228  CALBD1H A1440      93.666  65.437  -8.411  0.25 30.66           C  
-HETATM 6229  NBBBD1H A1440      93.891  64.667  -9.656  0.25 30.44           N  
-HETATM 6230  CAPBD1H A1440      95.192  64.293 -10.022  0.25 30.90           C  
-HETATM 6231  OAFBD1H A1440      96.156  64.773  -9.427  0.25 30.38           O  
-HETATM 6232  CAVBD1H A1440      95.397  63.391 -11.061  0.25 30.53           C  
-HETATM 6233  NAXBD1H A1440      96.469  62.803 -11.580  0.25 31.66           N  
-HETATM 6234  CABBD1H A1440      97.870  63.038 -11.168  0.25 31.81           C  
-HETATM 6235  CAJBD1H A1440      96.105  61.960 -12.541  0.25 31.97           C  
-HETATM 6236  NANBD1H A1440      94.779  62.003 -12.642  0.25 31.78           N  
-HETATM 6237  CATBD1H A1440      94.307  62.868 -11.747  0.25 31.10           C  
-HETATM 6238  NAZBD1H A1440      93.004  63.253 -11.409  0.25 30.48           N  
-HETATM 6239  CADBD1H A1440      91.856  62.680 -12.148  0.25 29.64           C  
-HETATM 6240  CARBD1H A1440      92.790  64.162 -10.364  0.25 30.69           C  
-HETATM 6241  OAHBD1H A1440      91.649  64.517 -10.071  0.25 30.01           O  
-HETATM 6242  S   SO4 B1433     102.551   0.083  -7.188  0.75 55.90           S  
-HETATM 6243  O1  SO4 B1433     101.505  -0.934  -7.375  0.75 58.34           O  
-HETATM 6244  O2  SO4 B1433     102.451   0.657  -5.838  0.75 57.04           O  
-HETATM 6245  O3  SO4 B1433     103.869  -0.555  -7.350  0.75 57.84           O  
-HETATM 6246  O4  SO4 B1433     102.385   1.156  -8.185  0.75 56.65           O  
-HETATM 6247  S   SO4 B1434      47.660  -7.560   9.197  0.75 59.52           S  
-HETATM 6248  O1  SO4 B1434      48.907  -8.328   9.324  0.75 59.34           O  
-HETATM 6249  O2  SO4 B1434      46.877  -7.650  10.446  0.75 61.52           O  
-HETATM 6250  O3  SO4 B1434      48.007  -6.158   8.956  0.75 60.57           O  
-HETATM 6251  O4  SO4 B1434      46.857  -8.079   8.074  0.75 59.31           O  
-HETATM 6252  S   SO4 B1435      89.099 -13.091  -7.882  1.00 65.11           S  
-HETATM 6253  O1  SO4 B1435      88.592 -12.646  -6.573  1.00 66.18           O  
-HETATM 6254  O2  SO4 B1435      89.343 -14.545  -7.829  1.00 65.41           O  
-HETATM 6255  O3  SO4 B1435      88.109 -12.801  -8.936  1.00 65.43           O  
-HETATM 6256  O4  SO4 B1435      90.353 -12.368  -8.190  1.00 66.82           O  
-HETATM 6257  S   SO4 B1436      80.013 -12.608  18.743  0.75 45.64           S  
-HETATM 6258  O1  SO4 B1436      80.813 -11.409  19.112  0.75 42.59           O  
-HETATM 6259  O2  SO4 B1436      78.641 -12.459  19.266  0.75 44.34           O  
-HETATM 6260  O3  SO4 B1436      80.008 -12.755  17.268  0.75 44.55           O  
-HETATM 6261  O4  SO4 B1436      80.573 -13.834  19.339  0.75 45.68           O  
-HETATM 6262  S   SO4 B1437      90.602 -12.295   6.143  1.00 40.12           S  
-HETATM 6263  O1  SO4 B1437      91.672 -13.185   6.643  1.00 44.10           O  
-HETATM 6264  O2  SO4 B1437      91.086 -10.908   6.238  1.00 37.04           O  
-HETATM 6265  O3  SO4 B1437      90.276 -12.652   4.744  1.00 39.59           O  
-HETATM 6266  O4  SO4 B1437      89.384 -12.484   6.975  1.00 42.70           O  
-HETATM 6267  O6 AD1H B1438      71.474  10.071  -4.526  0.75 26.86           O  
-HETATM 6268  C6 AD1H B1438      72.634  10.470  -4.614  0.75 29.06           C  
-HETATM 6269  C5 AD1H B1438      72.906  11.816  -4.852  0.75 28.42           C  
-HETATM 6270  N7 AD1H B1438      72.178  12.918  -5.018  0.75 28.49           N  
-HETATM 6271  CAAAD1H B1438      70.702  13.000  -5.077  0.75 28.31           C  
-HETATM 6272  C8 AD1H B1438      72.973  13.973  -5.174  0.75 28.22           C  
-HETATM 6273  N9 AD1H B1438      74.233  13.556  -5.099  0.75 26.51           N  
-HETATM 6274  C4 AD1H B1438      74.229  12.241  -4.902  0.75 27.30           C  
-HETATM 6275  N3 AD1H B1438      75.288  11.339  -4.730  0.75 28.80           N  
-HETATM 6276  CACAD1H B1438      76.685  11.827  -4.810  0.75 25.96           C  
-HETATM 6277  C2 AD1H B1438      75.021   9.983  -4.496  0.75 26.98           C  
-HETATM 6278  O2 AD1H B1438      75.929   9.180  -4.282  0.75 26.37           O  
-HETATM 6279  N1 AD1H B1438      73.688   9.558  -4.432  0.75 28.66           N  
-HETATM 6280  CAKAD1H B1438      73.409   8.147  -4.077  0.75 28.49           C  
-HETATM 6281  CALAD1H B1438      73.242   8.129  -2.557  0.75 27.34           C  
-HETATM 6282  NBBAD1H B1438      73.047   6.755  -2.047  0.75 29.07           N  
-HETATM 6283  CAPAD1H B1438      71.744   6.304  -1.794  0.75 27.55           C  
-HETATM 6284  OAFAD1H B1438      70.786   6.871  -2.318  0.75 25.25           O  
-HETATM 6285  CAVAD1H B1438      71.541   5.190  -0.988  0.75 26.13           C  
-HETATM 6286  NAXAD1H B1438      70.461   4.593  -0.498  0.75 26.86           N  
-HETATM 6287  CABAD1H B1438      69.061   4.952  -0.814  0.75 23.96           C  
-HETATM 6288  CAJAD1H B1438      70.821   3.597   0.305  0.75 26.23           C  
-HETATM 6289  NANAD1H B1438      72.151   3.554   0.334  0.75 25.76           N  
-HETATM 6290  CATAD1H B1438      72.630   4.518  -0.447  0.75 27.00           C  
-HETATM 6291  NAZAD1H B1438      73.937   4.933  -0.731  0.75 25.06           N  
-HETATM 6292  CADAD1H B1438      75.080   4.206  -0.136  0.75 23.97           C  
-HETATM 6293  CARAD1H B1438      74.153   6.049  -1.553  0.75 27.67           C  
-HETATM 6294  OAHAD1H B1438      75.288   6.360  -1.912  0.75 26.04           O  
-HETATM 6295  O6 BD1H B1438      71.470  10.070  -3.745  0.25 30.89           O  
-HETATM 6296  C6 BD1H B1438      72.599  10.472  -4.025  0.25 31.89           C  
-HETATM 6297  C5 BD1H B1438      72.751  11.645  -4.757  0.25 32.68           C  
-HETATM 6298  N7 BD1H B1438      71.902  12.553  -5.227  0.25 32.88           N  
-HETATM 6299  CAABD1H B1438      70.427  12.492  -5.117  0.25 33.18           C  
-HETATM 6300  C8 BD1H B1438      72.575  13.530  -5.830  0.25 33.58           C  
-HETATM 6301  N9 BD1H B1438      73.873  13.245  -5.743  0.25 33.43           N  
-HETATM 6302  C4 BD1H B1438      74.023  12.093  -5.094  0.25 32.29           C  
-HETATM 6303  N3 BD1H B1438      75.155  11.364  -4.709  0.25 32.51           N  
-HETATM 6304  CACBD1H B1438      76.505  11.853  -5.070  0.25 31.77           C  
-HETATM 6305  C2 BD1H B1438      75.010  10.178  -3.973  0.25 31.95           C  
-HETATM 6306  O2 BD1H B1438      75.995   9.513  -3.659  0.25 32.42           O  
-HETATM 6307  N1 BD1H B1438      73.725   9.743  -3.620  0.25 31.82           N  
-HETATM 6308  CAKBD1H B1438      73.563   8.623  -2.665  0.25 30.83           C  
-HETATM 6309  CALBD1H B1438      73.410   7.281  -3.382  0.25 29.00           C  
-HETATM 6310  NBBBD1H B1438      73.141   6.254  -2.351  0.25 27.78           N  
-HETATM 6311  CAPBD1H B1438      71.817   5.988  -1.968  0.25 26.72           C  
-HETATM 6312  OAFBD1H B1438      70.885   6.540  -2.549  0.25 25.31           O  
-HETATM 6313  CAVBD1H B1438      71.557   5.100  -0.929  0.25 26.17           C  
-HETATM 6314  NAXBD1H B1438      70.445   4.673  -0.339  0.25 26.40           N  
-HETATM 6315  CABBD1H B1438      69.069   5.080  -0.703  0.25 25.51           C  
-HETATM 6316  CAJBD1H B1438      70.749   3.823   0.636  0.25 25.73           C  
-HETATM 6317  NANBD1H B1438      72.074   3.701   0.674  0.25 25.44           N  
-HETATM 6318  CATBD1H B1438      72.606   4.470  -0.273  0.25 26.65           C  
-HETATM 6319  NAZBD1H B1438      73.932   4.721  -0.653  0.25 26.40           N  
-HETATM 6320  CADBD1H B1438      75.039   4.035   0.051  0.25 26.38           C  
-HETATM 6321  CARBD1H B1438      74.203   5.616  -1.696  0.25 27.78           C  
-HETATM 6322  OAHBD1H B1438      75.365   5.844  -2.039  0.25 27.87           O  
-HETATM 6323  O   HOH A2001      74.589  53.372  12.784  1.00 32.33           O  
-HETATM 6324  O   HOH A2002      81.033  62.398  21.260  1.00 42.15           O  
-HETATM 6325  O   HOH A2003      81.349  58.709  19.826  1.00 47.56           O  
-HETATM 6326  O   HOH A2004      79.094  64.751  18.720  1.00 48.90           O  
-HETATM 6327  O   HOH A2005      80.570  65.738  14.586  1.00 39.91           O  
-HETATM 6328  O   HOH A2006      81.638  65.407  18.459  1.00 49.03           O  
-HETATM 6329  O   HOH A2007      84.123  67.530  22.145  1.00 46.74           O  
-HETATM 6330  O   HOH A2008      91.163  58.710 -10.672  1.00 28.87           O  
-HETATM 6331  O   HOH A2009     101.423  58.639  -7.804  1.00 16.02           O  
-HETATM 6332  O   HOH A2010     102.763  50.661  -5.499  1.00 18.95           O  
-HETATM 6333  O   HOH A2011      84.107  64.936  22.174  1.00 39.43           O  
-HETATM 6334  O   HOH A2012      98.271  51.551 -14.879  1.00 25.57           O  
-HETATM 6335  O   HOH A2013     107.499  56.931  -4.248  1.00 24.29           O  
-HETATM 6336  O   HOH A2014     101.311  66.379  -4.871  1.00 34.13           O  
-HETATM 6337  O   HOH A2015      99.945  63.829  -3.301  1.00 32.67           O  
-HETATM 6338  O   HOH A2016     100.112  65.190  -8.721  1.00 29.33           O  
-HETATM 6339  O   HOH A2017     104.457  53.618   0.592  1.00 30.96           O  
-HETATM 6340  O   HOH A2018     108.310  54.385  -1.511  1.00 39.97           O  
-HETATM 6341  O   HOH A2019     106.728  51.335  -6.401  1.00 19.61           O  
-HETATM 6342  O   HOH A2020     109.284  55.024  -4.055  1.00 33.71           O  
-HETATM 6343  O   HOH A2021     100.751  64.950 -11.369  1.00 37.92           O  
-HETATM 6344  O   HOH A2022     102.748  55.251   1.895  1.00 18.74           O  
-HETATM 6345  O   HOH A2023     103.291  55.657   4.058  1.00 41.14           O  
-HETATM 6346  O   HOH A2024     100.303  44.154   3.129  1.00 44.77           O  
-HETATM 6347  O   HOH A2025     101.890  57.204   5.749  1.00 31.37           O  
-HETATM 6348  O   HOH A2026     100.451  43.837   0.680  1.00 47.40           O  
-HETATM 6349  O   HOH A2027     102.779  50.823  -0.480  1.00 27.01           O  
-HETATM 6350  O   HOH A2028     102.412  51.823   5.693  1.00 49.16           O  
-HETATM 6351  O   HOH A2029      99.535  54.021   8.324  1.00 45.75           O  
-HETATM 6352  O   HOH A2030      99.656  55.985   5.182  1.00 26.79           O  
-HETATM 6353  O   HOH A2031      84.808  44.613 -18.407  1.00 41.28           O  
-HETATM 6354  O   HOH A2032      95.799  51.943  11.667  1.00 33.37           O  
-HETATM 6355  O   HOH A2033      88.670  53.846  15.344  1.00 34.06           O  
-HETATM 6356  O   HOH A2034      78.806  59.532 -23.884  1.00 43.92           O  
-HETATM 6357  O   HOH A2035      82.073  62.304 -23.800  1.00 52.26           O  
-HETATM 6358  O   HOH A2036      75.856  50.693 -14.885  1.00 30.94           O  
-HETATM 6359  O   HOH A2037      81.103  50.706 -14.896  1.00 40.32           O  
-HETATM 6360  O   HOH A2038      84.449  49.472 -13.073  1.00 38.62           O  
-HETATM 6361  O   HOH A2039      87.054  54.502  13.159  1.00 20.27           O  
-HETATM 6362  O   HOH A2040      88.559  42.557 -14.174  1.00 24.82           O  
-HETATM 6363  O   HOH A2041      92.128  40.317 -12.523  1.00 46.38           O  
-HETATM 6364  O   HOH A2042      87.213  46.719 -15.873  1.00 35.83           O  
-HETATM 6365  O   HOH A2043      91.478  37.808 -13.139  1.00 54.06           O  
-HETATM 6366  O   HOH A2044      94.597  38.947   0.574  1.00 39.85           O  
-HETATM 6367  O   HOH A2045      86.538  42.028 -17.258  1.00 45.06           O  
-HETATM 6368  O   HOH A2046      88.376  59.528 -17.169  1.00 38.23           O  
-HETATM 6369  O   HOH A2047      86.939  63.889 -18.601  1.00 40.70           O  
-HETATM 6370  O   HOH A2048      94.707  40.452   3.241  1.00 48.01           O  
-HETATM 6371  O   HOH A2049      97.071  42.993   4.257  1.00 50.40           O  
-HETATM 6372  O   HOH A2050      94.607  44.539   4.819  1.00 44.52           O  
-HETATM 6373  O   HOH A2051      73.774  66.204 -20.996  1.00 40.63           O  
-HETATM 6374  O   HOH A2052      91.499  84.956  -5.666  1.00 45.53           O  
-HETATM 6375  O   HOH A2053      79.513  61.939 -22.747  1.00 40.00           O  
-HETATM 6376  O   HOH A2054      71.272  59.189 -19.776  1.00 33.17           O  
-HETATM 6377  O   HOH A2055      77.368  56.649 -20.835  1.00 25.64           O  
-HETATM 6378  O   HOH A2056      77.207  52.068 -17.308  1.00 44.59           O  
-HETATM 6379  O   HOH A2057      90.423  65.469 -18.715  1.00 45.86           O  
-HETATM 6380  O   HOH A2058      93.975  66.848 -16.586  1.00 50.77           O  
-HETATM 6381  O   HOH A2059      79.548  52.831 -15.028  1.00 27.65           O  
-HETATM 6382  O   HOH A2060      87.399  58.720 -20.223  1.00 46.67           O  
-HETATM 6383  O   HOH A2061      83.619  61.538 -19.208  1.00 28.22           O  
-HETATM 6384  O   HOH A2062      85.131  52.478 -16.404  1.00 43.26           O  
-HETATM 6385  O   HOH A2063      87.958  54.490 -17.308  1.00 37.45           O  
-HETATM 6386  O   HOH A2064      88.168  52.203 -15.983  1.00 51.08           O  
-HETATM 6387  O   HOH A2065      83.338  51.532 -14.287  1.00 20.86           O  
-HETATM 6388  O   HOH A2066      89.005  56.651 -17.765  1.00 44.70           O  
-HETATM 6389  O   HOH A2067      88.093  55.245 -10.385  1.00 31.75           O  
-HETATM 6390  O   HOH A2068      93.953  54.788 -16.480  1.00 37.39           O  
-HETATM 6391  O   HOH A2069      96.795  55.758 -15.122  1.00 46.08           O  
-HETATM 6392  O   HOH A2070      93.971  50.759 -16.183  1.00 27.47           O  
-HETATM 6393  O   HOH A2071      94.748  56.405 -11.641  1.00 17.64           O  
-HETATM 6394  O   HOH A2072      66.879  64.453 -21.657  1.00 52.10           O  
-HETATM 6395  O   HOH A2073     113.451  68.730  -6.287  1.00 37.47           O  
-HETATM 6396  O   HOH A2074     112.055  62.009  -2.190  1.00 48.94           O  
-HETATM 6397  O   HOH A2075      90.668  52.144 -17.282  1.00 26.30           O  
-HETATM 6398  O   HOH A2076      67.893  54.336 -10.074  1.00 35.12           O  
-HETATM 6399  O   HOH A2077      69.840  52.495  -8.732  1.00 32.75           O  
-HETATM 6400  O   HOH A2078      79.313  49.397 -13.300  1.00 27.01           O  
-HETATM 6401  O   HOH A2079      87.943  50.318 -12.576  1.00 46.03           O  
-HETATM 6402  O   HOH A2080      89.692  42.117 -11.534  1.00 21.87           O  
-HETATM 6403  O   HOH A2081      68.832  43.996  -7.371  1.00 35.56           O  
-HETATM 6404  O   HOH A2082      91.949  45.191 -18.581  1.00 40.99           O  
-HETATM 6405  O   HOH A2083      95.359  43.768 -16.580  1.00 36.06           O  
-HETATM 6406  O   HOH A2084      94.312  47.402 -17.631  1.00 32.69           O  
-HETATM 6407  O   HOH A2085      89.063  44.943 -15.620  1.00 24.13           O  
-HETATM 6408  O   HOH A2086     101.199  50.026  -8.422  1.00 17.77           O  
-HETATM 6409  O   HOH A2087     102.489  47.107  -4.862  1.00 24.92           O  
-HETATM 6410  O   HOH A2088     101.946  43.276  -6.445  1.00 36.61           O  
-HETATM 6411  O   HOH A2089      93.597  36.839 -11.749  1.00 36.32           O  
-HETATM 6412  O   HOH A2090      83.213  78.388 -10.474  1.00 31.35           O  
-HETATM 6413  O   HOH A2091      86.983  75.749 -11.503  1.00 43.57           O  
-HETATM 6414  O   HOH A2092      98.792  41.578   0.256  1.00 36.72           O  
-HETATM 6415  O   HOH A2093      95.524  40.525  -1.200  1.00 23.89           O  
-HETATM 6416  O   HOH A2094      93.714  43.233  -4.158  1.00 18.26           O  
-HETATM 6417  O   HOH A2095      92.956  35.827  -4.343  1.00 37.80           O  
-HETATM 6418  O   HOH A2096      92.024  33.347 -13.071  1.00 37.38           O  
-HETATM 6419  O   HOH A2097      97.973  32.013  -8.381  1.00 47.25           O  
-HETATM 6420  O   HOH A2098      90.674  35.455  -5.351  1.00 35.39           O  
-HETATM 6421  O   HOH A2099      87.878  33.831  -3.206  1.00 50.18           O  
-HETATM 6422  O   HOH A2100      64.717  50.609   4.401  1.00 37.83           O  
-HETATM 6423  O   HOH A2101      69.024  59.962   4.620  1.00 44.01           O  
-HETATM 6424  O   HOH A2102      67.722  56.505   7.033  1.00 44.21           O  
-HETATM 6425  O   HOH A2103      63.521  47.979  -5.594  1.00 43.99           O  
-HETATM 6426  O   HOH A2104      62.499  51.046  -2.114  1.00 42.93           O  
-HETATM 6427  O   HOH A2105      87.283  36.444 -14.853  1.00 45.94           O  
-HETATM 6428  O   HOH A2106      89.118  36.926 -12.135  1.00 43.28           O  
-HETATM 6429  O   HOH A2107      85.770  41.971 -14.425  1.00 27.51           O  
-HETATM 6430  O   HOH A2108      85.767  38.450 -15.516  1.00 32.56           O  
-HETATM 6431  O   HOH A2109      85.854  33.873  -6.411  1.00 29.28           O  
-HETATM 6432  O   HOH A2110      91.682  35.254 -10.277  1.00 41.65           O  
-HETATM 6433  O   HOH A2111      88.136  79.946  -4.208  1.00 33.71           O  
-HETATM 6434  O   HOH A2112      75.864  84.058  -6.369  1.00 44.67           O  
-HETATM 6435  O   HOH A2113      86.469  85.758  -2.071  1.00 50.45           O  
-HETATM 6436  O   HOH A2114      85.989  47.855  -1.581  1.00 31.66           O  
-HETATM 6437  O   HOH A2115      76.099  82.183   1.281  1.00 35.17           O  
-HETATM 6438  O   HOH A2116      72.498  80.614   2.189  1.00 48.01           O  
-HETATM 6439  O   HOH A2117      96.047  42.591   1.939  1.00 27.77           O  
-HETATM 6440  O   HOH A2118      93.879  45.635   2.600  1.00 18.06           O  
-HETATM 6441  O   HOH A2119      70.587  62.214   4.885  1.00 38.16           O  
-HETATM 6442  O   HOH A2120      90.535  41.939   6.514  1.00 21.27           O  
-HETATM 6443  O   HOH A2121      73.626  64.978  11.785  1.00 46.55           O  
-HETATM 6444  O   HOH A2122      89.844  79.701  -2.085  1.00 37.37           O  
-HETATM 6445  O   HOH A2123      89.002  47.829  14.602  1.00 43.56           O  
-HETATM 6446  O   HOH A2124     103.861  78.383 -12.122  1.00 47.58           O  
-HETATM 6447  O   HOH A2125      87.167  51.140  15.258  1.00 26.72           O  
-HETATM 6448  O   HOH A2126      93.063  82.623  -5.729  1.00 31.03           O  
-HETATM 6449  O   HOH A2127      95.108  85.715  -4.175  1.00 27.05           O  
-HETATM 6450  O   HOH A2128     104.787  90.142  -9.173  1.00 53.21           O  
-HETATM 6451  O   HOH A2129      86.252  46.924  14.193  1.00 25.06           O  
-HETATM 6452  O   HOH A2130      82.014  42.930  13.360  1.00 31.18           O  
-HETATM 6453  O   HOH A2131      80.959  51.254  14.245  1.00 29.95           O  
-HETATM 6454  O   HOH A2132      90.097  78.250  18.400  1.00 35.79           O  
-HETATM 6455  O   HOH A2133      87.658  88.406   8.270  1.00 41.68           O  
-HETATM 6456  O   HOH A2134      98.113  95.560   2.689  1.00 44.11           O  
-HETATM 6457  O   HOH A2135      92.442  86.779  -4.199  1.00 40.06           O  
-HETATM 6458  O   HOH A2136      85.123  88.161   2.780  1.00 41.61           O  
-HETATM 6459  O   HOH A2137      81.642  86.716   3.371  1.00 39.67           O  
-HETATM 6460  O   HOH A2138      84.491  88.878  10.087  1.00 44.09           O  
-HETATM 6461  O   HOH A2139      76.099  85.033   5.452  1.00 34.34           O  
-HETATM 6462  O   HOH A2140      68.838  82.800   9.757  1.00 45.46           O  
-HETATM 6463  O   HOH A2141      89.722  71.800  -3.858  1.00 35.94           O  
-HETATM 6464  O   HOH A2142      68.476  76.779   8.726  1.00 37.84           O  
-HETATM 6465  O   HOH A2143      87.748  66.374 -17.790  1.00 36.85           O  
-HETATM 6466  O   HOH A2144      89.809  68.912 -16.811  1.00 32.60           O  
-HETATM 6467  O   HOH A2145      94.223  65.094 -13.962  1.00 34.60           O  
-HETATM 6468  O   HOH A2146      74.534  64.987  16.776  1.00 42.36           O  
-HETATM 6469  O   HOH A2147      78.891  69.592  18.185  1.00 31.02           O  
-HETATM 6470  O   HOH A2148      71.969  70.298  13.969  1.00 37.88           O  
-HETATM 6471  O   HOH A2149      80.620  71.411 -14.712  1.00 19.95           O  
-HETATM 6472  O   HOH A2150      81.641  71.182 -19.676  1.00 45.51           O  
-HETATM 6473  O   HOH A2151      81.155  72.719 -17.086  1.00 41.52           O  
-HETATM 6474  O   HOH A2152      82.365  68.445 -20.273  1.00 31.23           O  
-HETATM 6475  O   HOH A2153      73.898  73.461 -16.750  1.00 35.70           O  
-HETATM 6476  O   HOH A2154      75.726  72.630 -18.802  1.00 38.30           O  
-HETATM 6477  O   HOH A2155     101.790  94.068  -3.482  1.00 40.19           O  
-HETATM 6478  O   HOH A2156      74.224  68.675 -21.721  1.00 43.32           O  
-HETATM 6479  O   HOH A2157      74.342  71.259 -20.738  1.00 40.52           O  
-HETATM 6480  O   HOH A2158      66.530  71.345 -17.326  1.00 46.13           O  
-HETATM 6481  O   HOH A2159      70.750  70.178 -20.994  1.00 45.71           O  
-HETATM 6482  O   HOH A2160      72.239  65.269 -18.762  1.00 29.82           O  
-HETATM 6483  O   HOH A2161     112.743  77.938  -8.390  1.00 36.77           O  
-HETATM 6484  O   HOH A2162     113.537  75.368  -4.646  1.00 34.98           O  
-HETATM 6485  O   HOH A2163     113.913  71.639  -6.044  1.00 39.20           O  
-HETATM 6486  O   HOH A2164     113.602  75.233  -9.610  1.00 41.16           O  
-HETATM 6487  O   HOH A2165      64.063  61.023 -17.244  1.00 43.83           O  
-HETATM 6488  O   HOH A2166     109.263  61.680  -3.087  1.00 47.14           O  
-HETATM 6489  O   HOH A2167     111.338  65.660  -1.934  1.00 32.29           O  
-HETATM 6490  O   HOH A2168      65.558  63.869 -19.245  1.00 42.28           O  
-HETATM 6491  O   HOH A2169      68.122  58.182 -16.954  1.00 41.66           O  
-HETATM 6492  O   HOH A2170     102.350  67.851 -12.960  1.00 48.15           O  
-HETATM 6493  O   HOH A2171      66.332  64.502 -11.643  1.00 37.17           O  
-HETATM 6494  O   HOH A2172     109.830  62.677   1.220  1.00 34.65           O  
-HETATM 6495  O   HOH A2173      68.002  56.634 -10.685  1.00 28.09           O  
-HETATM 6496  O   HOH A2174     114.425  68.853  -2.185  1.00 33.87           O  
-HETATM 6497  O   HOH A2175     114.480  71.318  -3.521  1.00 34.32           O  
-HETATM 6498  O   HOH A2176     116.243  69.326  -0.159  1.00 39.78           O  
-HETATM 6499  O   HOH A2177     116.896  66.691   3.059  1.00 43.90           O  
-HETATM 6500  O   HOH A2178      74.793  55.187 -19.518  1.00 37.04           O  
-HETATM 6501  O   HOH A2179      68.437  56.184 -15.362  1.00 46.33           O  
-HETATM 6502  O   HOH A2180     115.472  84.116   7.846  1.00 46.72           O  
-HETATM 6503  O   HOH A2181      71.837  51.120  -9.875  1.00 29.56           O  
-HETATM 6504  O   HOH A2182      77.781  51.785 -13.195  1.00 26.02           O  
-HETATM 6505  O   HOH A2183      78.589  47.136 -14.532  1.00 31.35           O  
-HETATM 6506  O   HOH A2184     113.866  77.948  -5.432  1.00 38.57           O  
-HETATM 6507  O   HOH A2185      70.273  46.693  -7.760  1.00 42.21           O  
-HETATM 6508  O   HOH A2186      80.572  47.963 -11.169  1.00 23.45           O  
-HETATM 6509  O   HOH A2187      76.085  43.534 -10.579  1.00 25.67           O  
-HETATM 6510  O   HOH A2188      85.242  49.609   0.186  1.00 30.09           O  
-HETATM 6511  O   HOH A2189      84.373  65.522   0.113  1.00 23.48           O  
-HETATM 6512  O   HOH A2190      80.930  69.041  -4.417  1.00 16.97           O  
-HETATM 6513  O   HOH A2191     112.708  64.682  10.073  1.00 48.95           O  
-HETATM 6514  O   HOH A2192     108.061  68.322  15.261  1.00 52.53           O  
-HETATM 6515  O   HOH A2193      84.790  72.432 -13.359  1.00 26.87           O  
-HETATM 6516  O   HOH A2194      90.601  76.047  -4.402  1.00 37.64           O  
-HETATM 6517  O   HOH A2195      87.658  73.762  -3.335  1.00 40.07           O  
-HETATM 6518  O   HOH A2196      83.872  75.935 -11.676  1.00 38.55           O  
-HETATM 6519  O   HOH A2197      81.457  78.927  -8.928  1.00 29.69           O  
-HETATM 6520  O   HOH A2198      79.812  76.809  -6.399  1.00 30.18           O  
-HETATM 6521  O   HOH A2199      92.617  62.966  25.092  1.00 31.76           O  
-HETATM 6522  O   HOH A2200      88.080  63.808  25.001  1.00 47.26           O  
-HETATM 6523  O   HOH A2201      77.428  81.050 -16.086  1.00 48.32           O  
-HETATM 6524  O   HOH A2202      74.798  75.960 -16.885  1.00 35.20           O  
-HETATM 6525  O   HOH A2203      80.338  73.719 -13.292  1.00 27.05           O  
-HETATM 6526  O   HOH A2204      73.550  73.853  -4.883  1.00 20.94           O  
-HETATM 6527  O   HOH A2205      84.609  45.363 -15.933  1.00 27.38           O  
-HETATM 6528  O   HOH A2206      67.099  72.360  -7.046  1.00 30.47           O  
-HETATM 6529  O   HOH A2207      67.955  74.301  -5.103  1.00 31.08           O  
-HETATM 6530  O   HOH A2208      84.464  32.121  -0.895  1.00 50.99           O  
-HETATM 6531  O   HOH A2209      69.597  72.329 -16.239  1.00 29.09           O  
-HETATM 6532  O   HOH A2210      67.644  70.863 -14.864  1.00 41.82           O  
-HETATM 6533  O   HOH A2211      73.800  71.914 -14.794  1.00 26.88           O  
-HETATM 6534  O   HOH A2212      65.872  64.993  -8.384  1.00 34.84           O  
-HETATM 6535  O   HOH A2213      67.315  58.290  -8.427  1.00 37.82           O  
-HETATM 6536  O   HOH A2214      70.808  54.148   2.161  1.00 23.65           O  
-HETATM 6537  O   HOH A2215      64.248  55.591  -2.358  1.00 33.28           O  
-HETATM 6538  O   HOH A2216      68.742  52.130  -6.320  1.00 36.18           O  
-HETATM 6539  O   HOH A2217      66.414  52.371   2.724  1.00 31.63           O  
-HETATM 6540  O   HOH A2218      68.642  53.703   3.939  1.00 37.24           O  
-HETATM 6541  O   HOH A2219      66.969  59.465   3.023  1.00 44.11           O  
-HETATM 6542  O   HOH A2220      68.757  56.379   4.373  1.00 32.98           O  
-HETATM 6543  O   HOH A2221      64.010  48.973  -3.007  1.00 34.40           O  
-HETATM 6544  O   HOH A2222      75.492  44.146  -3.797  1.00 21.87           O  
-HETATM 6545  O   HOH A2223      74.699  46.101   0.180  1.00 29.42           O  
-HETATM 6546  O   HOH A2224      62.874  46.455  -1.569  1.00 49.58           O  
-HETATM 6547  O   HOH A2225      68.348  47.189  -5.899  1.00 49.23           O  
-HETATM 6548  O   HOH A2226      69.759  40.869  -2.186  1.00 41.38           O  
-HETATM 6549  O   HOH A2227      67.919  42.330  -5.170  1.00 44.05           O  
-HETATM 6550  O   HOH A2228      72.638  42.774   2.546  1.00 42.30           O  
-HETATM 6551  O   HOH A2229      71.185  46.168   7.889  1.00 50.00           O  
-HETATM 6552  O   HOH A2230      67.512  44.171   2.156  1.00 35.90           O  
-HETATM 6553  O   HOH A2231      77.431  51.418   5.006  1.00 21.39           O  
-HETATM 6554  O   HOH A2232      74.905  48.361  10.613  1.00 39.16           O  
-HETATM 6555  O   HOH A2233      75.092  54.870   8.303  1.00 41.32           O  
-HETATM 6556  O   HOH A2234      72.747  52.255   8.925  1.00 28.81           O  
-HETATM 6557  O   HOH A2235      77.246  53.903   5.852  1.00 27.75           O  
-HETATM 6558  O   HOH A2236      83.319  71.614  -4.336  1.00 33.99           O  
-HETATM 6559  O   HOH A2237      86.887  82.003   2.768  1.00 21.88           O  
-HETATM 6560  O   HOH A2238      86.618  77.595  -3.238  1.00 26.16           O  
-HETATM 6561  O   HOH A2239      81.253  81.624  -8.521  1.00 39.38           O  
-HETATM 6562  O   HOH A2240      78.678  83.989  -6.241  1.00 30.01           O  
-HETATM 6563  O   HOH A2241      85.422  83.195  -3.950  1.00 40.84           O  
-HETATM 6564  O   HOH A2242      83.994  82.641  -8.564  1.00 47.26           O  
-HETATM 6565  O   HOH A2243      86.991  82.102  -5.185  1.00 33.80           O  
-HETATM 6566  O   HOH A2244      72.408  81.546  -4.353  1.00 46.64           O  
-HETATM 6567  O   HOH A2245      72.922  80.468  -6.968  1.00 27.22           O  
-HETATM 6568  O   HOH A2246      75.113  80.031  -0.382  1.00 19.97           O  
-HETATM 6569  O   HOH A2247      72.366  79.147   0.113  1.00 33.47           O  
-HETATM 6570  O   HOH A2248      68.239  71.307   5.100  1.00 44.61           O  
-HETATM 6571  O   HOH A2249      64.216  78.640   3.850  1.00 43.99           O  
-HETATM 6572  O   HOH A2250      66.463  77.066  -2.910  1.00 49.41           O  
-HETATM 6573  O   HOH A2251      66.735  69.120  -0.786  1.00 25.98           O  
-HETATM 6574  O   HOH A2252      70.685  70.186   9.026  1.00 36.50           O  
-HETATM 6575  O   HOH A2253      68.206  63.342   2.914  1.00 45.84           O  
-HETATM 6576  O   HOH A2254      70.257  65.511   5.866  1.00 39.83           O  
-HETATM 6577  O   HOH A2255      63.852  65.572   0.395  1.00 47.41           O  
-HETATM 6578  O   HOH A2256      75.399  63.498   9.538  1.00 34.49           O  
-HETATM 6579  O   HOH A2257      72.493  61.805   3.005  1.00 17.99           O  
-HETATM 6580  O   HOH A2258      75.271  60.613   8.652  1.00 32.43           O  
-HETATM 6581  O   HOH A2259      88.083  75.359  -1.241  1.00 18.40           O  
-HETATM 6582  O   HOH A2260      92.589  73.759   6.675  1.00 14.73           O  
-HETATM 6583  O   HOH A2261      90.324  76.908  -1.768  1.00 22.57           O  
-HETATM 6584  O   HOH A2262      90.455  68.478  -1.975  1.00 42.47           O  
-HETATM 6585  O   HOH A2263      91.381  73.511  -2.924  1.00 47.44           O  
-HETATM 6586  O   HOH A2264      92.880  77.317  -5.184  1.00 45.93           O  
-HETATM 6587  O   HOH A2265      98.280  75.667  -9.404  1.00 42.51           O  
-HETATM 6588  O   HOH A2266      98.273  78.552 -12.222  1.00 47.87           O  
-HETATM 6589  O   HOH A2267      99.240  83.714 -11.232  1.00 46.02           O  
-HETATM 6590  O   HOH A2268     102.823  81.976 -10.815  1.00 35.49           O  
-HETATM 6591  O   HOH A2269     102.215  75.694 -11.388  1.00 40.72           O  
-HETATM 6592  O   HOH A2270      95.131  83.103  -4.038  1.00 18.36           O  
-HETATM 6593  O   HOH A2271     101.346  85.872  -9.931  1.00 36.51           O  
-HETATM 6594  O   HOH A2272     104.218  87.982  -7.626  1.00 32.65           O  
-HETATM 6595  O   HOH A2273      95.536  86.401  -6.820  1.00 28.08           O  
-HETATM 6596  O   HOH A2274      97.566  86.751  -3.689  1.00 32.65           O  
-HETATM 6597  O   HOH A2275      98.691  85.882  -1.444  1.00 23.79           O  
-HETATM 6598  O   HOH A2276      98.272  78.253   5.802  1.00 18.48           O  
-HETATM 6599  O   HOH A2277      94.912  82.729   2.368  1.00 17.68           O  
-HETATM 6600  O   HOH A2278      86.759  81.794  15.659  1.00 34.62           O  
-HETATM 6601  O   HOH A2279      90.799  80.695  17.729  1.00 42.57           O  
-HETATM 6602  O   HOH A2280      91.358  88.437  11.274  1.00 45.60           O  
-HETATM 6603  O   HOH A2281      90.051  90.289   9.776  1.00 33.36           O  
-HETATM 6604  O   HOH A2282      92.808  93.154   6.981  1.00 41.94           O  
-HETATM 6605  O   HOH A2283      89.589  86.164  10.167  1.00 20.36           O  
-HETATM 6606  O   HOH A2284      95.054  88.651  12.252  1.00 27.70           O  
-HETATM 6607  O   HOH A2285      97.683  88.716  12.880  1.00 37.17           O  
-HETATM 6608  O   HOH A2286     101.413  86.533   7.244  1.00 25.77           O  
-HETATM 6609  O   HOH A2287      94.715  94.831   8.062  1.00 40.84           O  
-HETATM 6610  O   HOH A2288     102.599  93.686   6.023  1.00 47.20           O  
-HETATM 6611  O   HOH A2289     100.174  95.482   6.353  1.00 51.25           O  
-HETATM 6612  O   HOH A2290      99.472  92.932   3.435  1.00 28.53           O  
-HETATM 6613  O   HOH A2291      96.856  88.808  -1.668  1.00 46.37           O  
-HETATM 6614  O   HOH A2292      91.369  86.379   4.400  1.00 31.38           O  
-HETATM 6615  O   HOH A2293      88.439  85.836   0.242  1.00 27.92           O  
-HETATM 6616  O   HOH A2294      91.100  87.312  -1.867  1.00 32.94           O  
-HETATM 6617  O   HOH A2295      88.773  88.593   5.894  1.00 47.68           O  
-HETATM 6618  O   HOH A2296      87.073  85.962   9.020  1.00 26.73           O  
-HETATM 6619  O   HOH A2297      87.913  84.455   2.508  1.00 22.81           O  
-HETATM 6620  O   HOH A2298      87.737  86.929   3.577  1.00 30.28           O  
-HETATM 6621  O   HOH A2299      91.945  76.224   7.886  1.00 16.36           O  
-HETATM 6622  O   HOH A2300      81.300  85.026   5.743  1.00 35.76           O  
-HETATM 6623  O   HOH A2301      84.582  87.689   6.813  1.00 32.94           O  
-HETATM 6624  O   HOH A2302      82.176  86.496   8.128  1.00 31.68           O  
-HETATM 6625  O   HOH A2303      84.639  86.212  10.447  1.00 27.44           O  
-HETATM 6626  O   HOH A2304      78.636  85.123   6.768  1.00 37.97           O  
-HETATM 6627  O   HOH A2305      75.455  82.028   3.909  1.00 32.10           O  
-HETATM 6628  O   HOH A2306      73.928  76.972  11.182  1.00 24.90           O  
-HETATM 6629  O   HOH A2307      69.928  81.423   6.452  1.00 41.89           O  
-HETATM 6630  O   HOH A2308      70.884  81.128   9.699  1.00 22.25           O  
-HETATM 6631  O   HOH A2309      70.433  73.587   6.724  1.00 40.56           O  
-HETATM 6632  O   HOH A2310      69.813  73.602   9.742  1.00 40.41           O  
-HETATM 6633  O   HOH A2311      75.851  74.569  14.640  1.00 29.02           O  
-HETATM 6634  O   HOH A2312      73.651  71.151  15.739  1.00 32.87           O  
-HETATM 6635  O   HOH A2313      78.126  65.240  14.372  1.00 41.23           O  
-HETATM 6636  O   HOH A2314      76.947  68.229  17.999  1.00 31.45           O  
-HETATM 6637  O   HOH A2315      73.016  66.881  15.630  1.00 43.42           O  
-HETATM 6638  O   HOH A2316      76.189  71.909  15.039  1.00 17.10           O  
-HETATM 6639  O   HOH A2317      77.437  65.719  17.086  1.00 43.53           O  
-HETATM 6640  O   HOH A2318      76.409  65.955  12.475  1.00 26.97           O  
-HETATM 6641  O   HOH A2319      73.584  68.324  12.620  1.00 32.37           O  
-HETATM 6642  O   HOH A2320      71.379  66.286   8.793  1.00 39.15           O  
-HETATM 6643  O   HOH A2321      97.233  69.968   7.821  1.00 17.07           O  
-HETATM 6644  O   HOH A2322     100.715  70.354   5.946  1.00 16.53           O  
-HETATM 6645  O   HOH A2323     100.619  76.163  -6.773  1.00 22.84           O  
-HETATM 6646  O   HOH A2324      97.852  71.934  -7.440  1.00 49.50           O  
-HETATM 6647  O   HOH A2325     110.328  87.700  -7.397  1.00 45.05           O  
-HETATM 6648  O   HOH A2326     109.833  92.616   0.803  1.00 45.60           O  
-HETATM 6649  O   HOH A2327     106.025  89.278   4.398  1.00 42.57           O  
-HETATM 6650  O   HOH A2328     103.218  92.588  -1.564  1.00 32.16           O  
-HETATM 6651  O   HOH A2329     102.973  91.728   2.480  1.00 30.63           O  
-HETATM 6652  O   HOH A2330     109.100  89.234  -2.778  1.00 28.82           O  
-HETATM 6653  O   HOH A2331     104.114  86.001  -9.920  1.00 33.66           O  
-HETATM 6654  O   HOH A2332     105.202  83.568 -10.648  1.00 30.32           O  
-HETATM 6655  O   HOH A2333     107.068  77.838 -11.489  1.00 34.61           O  
-HETATM 6656  O   HOH A2334     108.263  75.302 -11.599  1.00 42.85           O  
-HETATM 6657  O   HOH A2335     110.499  78.355 -10.116  1.00 38.00           O  
-HETATM 6658  O   HOH A2336     112.461  73.887  -6.430  1.00 23.06           O  
-HETATM 6659  O   HOH A2337     108.774  64.319  -9.295  1.00 38.45           O  
-HETATM 6660  O   HOH A2338     109.272  63.145  -5.256  1.00 30.93           O  
-HETATM 6661  O   HOH A2339     108.978  65.096  -2.240  1.00 31.58           O  
-HETATM 6662  O   HOH A2340     107.702  65.372 -11.460  1.00 43.42           O  
-HETATM 6663  O   HOH A2341      99.249  67.478  -5.703  1.00 37.04           O  
-HETATM 6664  O   HOH A2342     104.333  69.648 -12.644  1.00 25.98           O  
-HETATM 6665  O   HOH A2343     101.815  71.881 -10.615  1.00 37.31           O  
-HETATM 6666  O   HOH A2344     101.689  74.738  -8.876  1.00 25.26           O  
-HETATM 6667  O   HOH A2345     102.679  76.498  -5.123  1.00 17.46           O  
-HETATM 6668  O   HOH A2346     103.708  67.332  -5.736  1.00 15.88           O  
-HETATM 6669  O   HOH A2347     107.727  62.669  -0.823  1.00 39.64           O  
-HETATM 6670  O   HOH A2348     101.665  66.132  -2.493  1.00 33.39           O  
-HETATM 6671  O   HOH A2349     107.392  69.352   9.915  1.00 37.07           O  
-HETATM 6672  O   HOH A2350     104.456  59.802  -1.667  1.00 29.02           O  
-HETATM 6673  O   HOH A2351     103.424  57.526   0.201  1.00 32.72           O  
-HETATM 6674  O   HOH A2352     111.676  65.295   5.353  1.00 43.99           O  
-HETATM 6675  O   HOH A2353     112.784  67.484   1.906  1.00 30.07           O  
-HETATM 6676  O   HOH A2354     111.328  67.398   7.052  1.00 29.30           O  
-HETATM 6677  O   HOH A2355     112.053  68.074  -0.680  1.00 31.69           O  
-HETATM 6678  O   HOH A2356     112.624  75.048   1.596  1.00 19.72           O  
-HETATM 6679  O   HOH A2357     111.046  73.686   3.482  1.00 18.53           O  
-HETATM 6680  O   HOH A2358     113.630  73.640  -2.418  1.00 24.90           O  
-HETATM 6681  O   HOH A2359     115.018  72.494   7.697  1.00 33.41           O  
-HETATM 6682  O   HOH A2360     117.107  72.138   0.363  1.00 32.54           O  
-HETATM 6683  O   HOH A2361     115.357  68.503   2.111  1.00 25.78           O  
-HETATM 6684  O   HOH A2362     118.809  72.011   7.535  1.00 46.14           O  
-HETATM 6685  O   HOH A2363     119.666  77.987   4.336  1.00 47.04           O  
-HETATM 6686  O   HOH A2364     116.769  78.671   7.209  1.00 30.93           O  
-HETATM 6687  O   HOH A2365     107.489  71.606  13.685  1.00 31.17           O  
-HETATM 6688  O   HOH A2366     112.624  75.247  11.656  1.00 25.41           O  
-HETATM 6689  O   HOH A2367     108.169  75.336  14.040  1.00 34.13           O  
-HETATM 6690  O   HOH A2368     113.674  81.868   7.768  1.00 33.76           O  
-HETATM 6691  O   HOH A2369     105.857  84.368  14.358  1.00 20.11           O  
-HETATM 6692  O   HOH A2370     107.796  81.218  14.377  1.00 16.95           O  
-HETATM 6693  O   HOH A2371      96.184  80.122  17.620  1.00 27.37           O  
-HETATM 6694  O   HOH A2372      96.931  88.102  19.350  1.00 27.26           O  
-HETATM 6695  O   HOH A2373      93.099  84.636  15.982  1.00 41.77           O  
-HETATM 6696  O   HOH A2374      97.384  84.008  18.738  1.00 29.85           O  
-HETATM 6697  O   HOH A2375      97.011  76.897   8.047  1.00 17.29           O  
-HETATM 6698  O   HOH A2376     111.092  77.087   2.490  1.00 22.01           O  
-HETATM 6699  O   HOH A2377     119.275  76.295   0.719  1.00 37.96           O  
-HETATM 6700  O   HOH A2378     115.360  75.045   1.711  1.00 21.29           O  
-HETATM 6701  O   HOH A2379     116.671  81.151   6.107  1.00 35.00           O  
-HETATM 6702  O   HOH A2380     115.611  74.803  -0.946  1.00 28.42           O  
-HETATM 6703  O   HOH A2381     113.134  80.418  -4.474  1.00 36.69           O  
-HETATM 6704  O   HOH A2382     100.959  79.110   5.503  1.00 20.11           O  
-HETATM 6705  O   HOH A2383      99.025  74.920   5.015  1.00 30.71           O  
-HETATM 6706  O   HOH A2384     100.231  76.473   7.406  1.00 19.16           O  
-HETATM 6707  O   HOH A2385     105.334  72.106  15.454  1.00 20.19           O  
-HETATM 6708  O   HOH A2386      99.825  73.821  19.295  1.00 26.52           O  
-HETATM 6709  O   HOH A2387     105.875  74.608  16.041  1.00 23.05           O  
-HETATM 6710  O   HOH A2388      98.534  66.913  20.636  1.00 17.23           O  
-HETATM 6711  O   HOH A2389     102.037  67.658  19.485  1.00 28.55           O  
-HETATM 6712  O   HOH A2390      88.072  79.217  19.700  1.00 37.78           O  
-HETATM 6713  O   HOH A2391      84.249  79.065  19.550  1.00 27.48           O  
-HETATM 6714  O   HOH A2392      81.096  74.257  19.824  1.00 31.21           O  
-HETATM 6715  O   HOH A2393      79.975  76.564  15.240  1.00 20.81           O  
-HETATM 6716  O   HOH A2394      78.418  71.566  16.709  1.00 21.20           O  
-HETATM 6717  O   HOH A2395      81.350  67.684  16.465  1.00 36.25           O  
-HETATM 6718  O   HOH A2396      96.195  68.493   9.920  1.00 18.37           O  
-HETATM 6719  O   HOH A2397      97.835  65.470  -4.810  1.00 35.06           O  
-HETATM 6720  O   HOH A2398      96.178  58.915  -1.545  1.00 13.27           O  
-HETATM 6721  O   HOH A2399      98.826  65.520  -0.756  1.00 16.58           O  
-HETATM 6722  O   HOH A2400     101.302  59.243   4.083  1.00 20.01           O  
-HETATM 6723  O   HOH A2401      97.990  58.256   5.496  1.00 15.27           O  
-HETATM 6724  O   HOH A2402     102.674  61.364  -1.615  1.00 31.33           O  
-HETATM 6725  O   HOH A2403      98.867  59.202   8.007  1.00 17.17           O  
-HETATM 6726  O   HOH A2404     110.541  64.299   8.842  1.00 34.13           O  
-HETATM 6727  O   HOH A2405     101.380  58.331   8.094  1.00 20.06           O  
-HETATM 6728  O   HOH A2406     107.999  56.780  11.553  1.00 33.59           O  
-HETATM 6729  O   HOH A2407     107.898  60.327   7.829  1.00 37.52           O  
-HETATM 6730  O   HOH A2408     102.030  55.775  10.542  1.00 47.46           O  
-HETATM 6731  O   HOH A2409     101.533  62.196  16.084  1.00 38.11           O  
-HETATM 6732  O   HOH A2410     109.322  62.211  10.364  1.00 43.29           O  
-HETATM 6733  O   HOH A2411     106.608  66.050  14.449  1.00 25.89           O  
-HETATM 6734  O   HOH A2412     105.254  66.134  11.885  1.00 32.50           O  
-HETATM 6735  O   HOH A2413      98.291  58.398  10.724  1.00 15.60           O  
-HETATM 6736  O   HOH A2414     101.107  57.603  13.004  1.00 21.17           O  
-HETATM 6737  O   HOH A2415     102.806  65.571  13.949  1.00 34.05           O  
-HETATM 6738  O   HOH A2416      98.377  64.625  19.387  1.00 16.07           O  
-HETATM 6739  O   HOH A2417      99.872  62.563  18.461  1.00 30.00           O  
-HETATM 6740  O   HOH A2418      93.798  61.927  23.091  1.00 27.62           O  
-HETATM 6741  O   HOH A2419      98.522  59.448  21.348  1.00 41.18           O  
-HETATM 6742  O   HOH A2420      90.814  67.230  22.979  1.00 30.91           O  
-HETATM 6743  O   HOH A2421      89.027  61.533  24.867  1.00 34.26           O  
-HETATM 6744  O   HOH A2422      89.828  58.340  22.687  1.00 30.85           O  
-HETATM 6745  O   HOH A2423      93.398  57.069  19.954  1.00 39.24           O  
-HETATM 6746  O   HOH A2424      92.054  53.126  17.449  1.00 48.89           O  
-HETATM 6747  O   HOH A2425      82.915  63.433  19.963  1.00 45.05           O  
-HETATM 6748  O   HOH A2426      76.331  58.722  12.074  1.00 40.60           O  
-HETATM 6749  O   HOH A2427      81.739  57.416  11.580  1.00 15.83           O  
-HETATM 6750  O   HOH A2428      78.304  62.402  14.308  1.00 27.10           O  
-HETATM 6751  O   HOH A2429      79.231  58.617   8.809  1.00 21.64           O  
-HETATM 6752  O   HOH A2430      77.981  61.301   9.564  1.00 25.15           O  
-HETATM 6753  O   HOH A2431      76.197  56.968  14.364  1.00 38.03           O  
-HETATM 6754  O   HOH A2432      86.548  54.735  16.728  1.00 36.41           O  
-HETATM 6755  O   HOH A2433      85.036  51.794  16.677  1.00 39.28           O  
-HETATM 6756  O   HOH A2434      76.555  57.539   9.354  1.00 49.19           O  
-HETATM 6757  O   HOH A2435      77.762  53.439   8.470  1.00 31.77           O  
-HETATM 6758  O   HOH A2436      76.089  51.535  13.953  1.00 40.62           O  
-HETATM 6759  O   HOH A2437      81.106  45.544  15.005  1.00 47.73           O  
-HETATM 6760  O   HOH A2438      76.414  46.917   9.105  1.00 33.66           O  
-HETATM 6761  O   HOH A2439      73.349  45.559   6.173  1.00 29.90           O  
-HETATM 6762  O   HOH A2440      73.153  43.131   5.336  1.00 44.65           O  
-HETATM 6763  O   HOH A2441      72.980  39.207   2.304  1.00 53.89           O  
-HETATM 6764  O   HOH A2442      77.636  43.918   6.868  1.00 29.13           O  
-HETATM 6765  O   HOH A2443      73.988  37.903  -6.775  1.00 19.74           O  
-HETATM 6766  O   HOH A2444      75.754  39.056  -8.478  1.00 23.49           O  
-HETATM 6767  O   HOH A2445      84.188  43.809 -13.942  1.00 22.30           O  
-HETATM 6768  O   HOH A2446      83.243  47.407 -11.669  1.00 25.65           O  
-HETATM 6769  O   HOH A2447      90.111  37.174  -3.890  1.00 21.49           O  
-HETATM 6770  O   HOH A2448      85.630  35.142  -1.166  1.00 26.52           O  
-HETATM 6771  O   HOH A2449      79.764  40.851   0.350  1.00 19.05           O  
-HETATM 6772  O   HOH A2450      76.905  38.645  -0.032  1.00 38.79           O  
-HETATM 6773  O   HOH A2451      83.452  32.774  -5.019  1.00 46.95           O  
-HETATM 6774  O   HOH A2452      77.880  31.893  -2.332  1.00 35.36           O  
-HETATM 6775  O   HOH A2453      82.165  32.009   1.333  1.00 45.06           O  
-HETATM 6776  O   HOH A2454      88.183  37.834   4.719  1.00 24.37           O  
-HETATM 6777  O   HOH A2455      91.034  33.545  -1.242  1.00 37.50           O  
-HETATM 6778  O   HOH A2456      89.654  36.485  -1.547  1.00 37.14           O  
-HETATM 6779  O   HOH A2457      64.676  68.899 -15.478  1.00 48.44           O  
-HETATM 6780  O   HOH A2458      71.664  80.240 -13.875  1.00 38.28           O  
-HETATM 6781  O   HOH A2459      65.679  76.118   0.359  1.00 46.40           O  
-HETATM 6782  O   HOH A2460      70.589  79.535   3.090  1.00 44.04           O  
-HETATM 6783  O   HOH A2461     116.431  74.772  -4.946  1.00 44.27           O  
-HETATM 6784  O   HOH A2462     118.449  74.717  -1.345  1.00 42.51           O  
-HETATM 6785  O   HOH A2463     103.753  87.473   8.268  1.00 42.11           O  
-HETATM 6786  O   HOH A2464     104.683  88.293  12.777  1.00 39.56           O  
-HETATM 6787  O   HOH A2465      97.710  64.457  -7.373  1.00 36.70           O  
-HETATM 6788  O   HOH A2466      89.168  64.889 -11.014  1.00 17.84           O  
-HETATM 6789  O   HOH B2001      83.638  10.106  27.443  1.00 51.86           O  
-HETATM 6790  O   HOH B2002      78.754  -1.434  21.028  1.00 36.58           O  
-HETATM 6791  O   HOH B2003      76.454  -1.879  24.264  1.00 43.57           O  
-HETATM 6792  O   HOH B2004      71.545  -3.930  26.011  1.00 33.06           O  
-HETATM 6793  O   HOH B2005      76.227   3.673   2.717  1.00 49.22           O  
-HETATM 6794  O   HOH B2006      79.249   3.622   6.897  1.00 25.43           O  
-HETATM 6795  O   HOH B2007      67.343  17.237  -1.650  1.00 16.47           O  
-HETATM 6796  O   HOH B2008      68.114  24.092   3.096  1.00 22.93           O  
-HETATM 6797  O   HOH B2009      73.333  -1.544  27.607  1.00 36.71           O  
-HETATM 6798  O   HOH B2010      65.689  24.150   0.306  1.00 29.86           O  
-HETATM 6799  O   HOH B2011      61.055  19.452   1.454  1.00 28.65           O  
-HETATM 6800  O   HOH B2012      60.991  20.442  -2.011  1.00 31.19           O  
-HETATM 6801  O   HOH B2013      66.390  11.176   1.258  1.00 31.69           O  
-HETATM 6802  O   HOH B2014      65.688   9.368  -2.260  1.00 39.58           O  
-HETATM 6803  O   HOH B2015      67.367  10.949  -4.418  1.00 29.48           O  
-HETATM 6804  O   HOH B2016      66.264  25.751   5.359  1.00 48.50           O  
-HETATM 6805  O   HOH B2017      62.872  19.028   6.130  1.00 46.31           O  
-HETATM 6806  O   HOH B2018      63.561  26.755   3.182  1.00 53.11           O  
-HETATM 6807  O   HOH B2019      59.759  16.674   2.303  1.00 38.44           O  
-HETATM 6808  O   HOH B2020      64.397  18.264   8.403  1.00 24.80           O  
-HETATM 6809  O   HOH B2021      63.517  15.075  11.659  1.00 33.74           O  
-HETATM 6810  O   HOH B2022      75.974  13.879  25.421  1.00 45.66           O  
-HETATM 6811  O   HOH B2023      68.940  27.813  11.077  1.00 48.29           O  
-HETATM 6812  O   HOH B2024      61.039  12.942  20.652  1.00 31.60           O  
-HETATM 6813  O   HOH B2025      64.928  22.504   7.739  1.00 34.12           O  
-HETATM 6814  O   HOH B2026      66.073  15.658  11.631  1.00 25.23           O  
-HETATM 6815  O   HOH B2027      67.175  24.213   9.689  1.00 35.69           O  
-HETATM 6816  O   HOH B2028      65.650  16.723  15.274  1.00 40.91           O  
-HETATM 6817  O   HOH B2029      75.305  13.865  21.056  1.00 27.25           O  
-HETATM 6818  O   HOH B2030      68.500  16.506  20.029  1.00 38.46           O  
-HETATM 6819  O   HOH B2031      73.615  11.831  23.958  1.00 37.31           O  
-HETATM 6820  O   HOH B2032      93.885  15.486 -10.463  1.00 39.19           O  
-HETATM 6821  O   HOH B2033      91.189  21.019  -3.622  1.00 50.28           O  
-HETATM 6822  O   HOH B2034      63.087  11.634  22.935  1.00 37.15           O  
-HETATM 6823  O   HOH B2035      64.838  11.620  16.249  1.00 17.69           O  
-HETATM 6824  O   HOH B2036      90.531  19.498  -1.389  1.00 30.83           O  
-HETATM 6825  O   HOH B2037      86.979  21.387   0.142  1.00 37.82           O  
-HETATM 6826  O   HOH B2038      84.663  22.001  -3.483  1.00 56.73           O  
-HETATM 6827  O   HOH B2039      75.560  11.230  22.210  1.00 22.44           O  
-HETATM 6828  O   HOH B2040      81.211  31.532  -6.719  1.00 30.34           O  
-HETATM 6829  O   HOH B2041      82.376   0.563 -12.533  1.00 44.30           O  
-HETATM 6830  O   HOH B2042      76.095  30.449  14.256  1.00 34.10           O  
-HETATM 6831  O   HOH B2043      94.342  -6.405 -10.334  1.00 45.16           O  
-HETATM 6832  O   HOH B2044      84.362  42.435  13.530  1.00 26.79           O  
-HETATM 6833  O   HOH B2045      93.406  41.602   5.540  1.00 37.38           O  
-HETATM 6834  O   HOH B2046      89.483  14.463 -12.079  1.00 51.92           O  
-HETATM 6835  O   HOH B2047      87.200  16.978 -12.221  1.00 37.00           O  
-HETATM 6836  O   HOH B2048      95.056   4.993 -10.414  1.00 38.66           O  
-HETATM 6837  O   HOH B2049      69.795 -10.464  -6.456  1.00 37.81           O  
-HETATM 6838  O   HOH B2050      70.741  -6.490  -4.913  1.00 47.57           O  
-HETATM 6839  O   HOH B2051      92.571  13.648 -11.958  1.00 51.84           O  
-HETATM 6840  O   HOH B2052      98.672   9.649  -6.431  1.00 39.27           O  
-HETATM 6841  O   HOH B2053      94.379  14.928  -7.787  1.00 39.08           O  
-HETATM 6842  O   HOH B2054      93.108  18.541  -7.478  1.00 43.75           O  
-HETATM 6843  O   HOH B2055      90.665  19.101  -5.680  1.00 44.08           O  
-HETATM 6844  O   HOH B2056      77.929   2.742 -10.383  1.00 34.22           O  
-HETATM 6845  O   HOH B2057      73.290   0.806  -6.184  1.00 41.17           O  
-HETATM 6846  O   HOH B2058      75.821   5.932 -10.432  1.00 40.34           O  
-HETATM 6847  O   HOH B2059      74.355   4.741  -8.625  1.00 41.57           O  
-HETATM 6848  O   HOH B2060      91.399  17.252  -1.756  1.00 27.52           O  
-HETATM 6849  O   HOH B2061      85.290  16.428 -10.363  1.00 22.25           O  
-HETATM 6850  O   HOH B2062      86.804  12.348  -9.867  1.00 31.33           O  
-HETATM 6851  O   HOH B2063      88.849  -1.047 -12.484  1.00 46.70           O  
-HETATM 6852  O   HOH B2064      86.503  20.071  -3.546  1.00 30.67           O  
-HETATM 6853  O   HOH B2065      87.802  19.471  -1.333  1.00 21.60           O  
-HETATM 6854  O   HOH B2066      92.045  -3.068  -9.146  1.00 30.28           O  
-HETATM 6855  O   HOH B2067      81.439  16.904  -0.308  1.00 20.46           O  
-HETATM 6856  O   HOH B2068      78.526  14.266  -3.401  1.00 29.74           O  
-HETATM 6857  O   HOH B2069      95.170  -2.159 -11.971  1.00 49.25           O  
-HETATM 6858  O   HOH B2070      75.278  18.086  -3.369  1.00 21.48           O  
-HETATM 6859  O   HOH B2071      76.380  23.799  -5.802  1.00 21.12           O  
-HETATM 6860  O   HOH B2072     103.835   8.045  -2.636  1.00 41.26           O  
-HETATM 6861  O   HOH B2073      49.083   6.965  -7.507  1.00 39.56           O  
-HETATM 6862  O   HOH B2074      78.808  24.479  -5.559  1.00 44.14           O  
-HETATM 6863  O   HOH B2075      80.729  23.005  -6.068  1.00 25.23           O  
-HETATM 6864  O   HOH B2076     100.255  11.321   4.816  1.00 50.19           O  
-HETATM 6865  O   HOH B2077      95.237  18.143  -0.248  1.00 33.70           O  
-HETATM 6866  O   HOH B2078      91.993  19.980   1.138  1.00 33.87           O  
-HETATM 6867  O   HOH B2079      83.060  21.483  -1.407  1.00 29.56           O  
-HETATM 6868  O   HOH B2080      82.408  28.457  -5.562  1.00 44.33           O  
-HETATM 6869  O   HOH B2081      84.646  27.865  -1.999  1.00 43.01           O  
-HETATM 6870  O   HOH B2082      69.887  -7.132  26.840  1.00 50.05           O  
-HETATM 6871  O   HOH B2083      70.064  25.413  -0.305  1.00 38.60           O  
-HETATM 6872  O   HOH B2084      77.914  -2.132  -8.011  1.00 42.43           O  
-HETATM 6873  O   HOH B2085      79.594   0.795 -10.915  1.00 41.22           O  
-HETATM 6874  O   HOH B2086      80.070  -5.844  -7.053  1.00 32.92           O  
-HETATM 6875  O   HOH B2087      71.757  29.050  12.204  1.00 39.86           O  
-HETATM 6876  O   HOH B2088      75.699  30.125  11.523  1.00 25.03           O  
-HETATM 6877  O   HOH B2089      77.317  27.759   8.276  1.00 23.60           O  
-HETATM 6878  O   HOH B2090      97.209  -6.656   3.794  1.00 39.99           O  
-HETATM 6879  O   HOH B2091      94.749  -3.741  -9.531  1.00 40.66           O  
-HETATM 6880  O   HOH B2092      79.674  34.193  11.057  1.00 30.59           O  
-HETATM 6881  O   HOH B2093      85.224  42.251  11.002  1.00 31.11           O  
-HETATM 6882  O   HOH B2094      82.214  31.754  11.522  1.00 29.40           O  
-HETATM 6883  O   HOH B2095      84.188  35.822   6.305  1.00 28.50           O  
-HETATM 6884  O   HOH B2096      87.032  38.049  12.662  1.00 50.33           O  
-HETATM 6885  O   HOH B2097      91.968  39.705  12.492  1.00 52.70           O  
-HETATM 6886  O   HOH B2098      92.867  38.447   6.276  1.00 46.56           O  
-HETATM 6887  O   HOH B2099      90.193  39.250   6.089  1.00 25.07           O  
-HETATM 6888  O   HOH B2100      83.512  29.631   2.725  1.00 29.82           O  
-HETATM 6889  O   HOH B2101      87.248  34.232  11.185  1.00 28.21           O  
-HETATM 6890  O   HOH B2102      73.680  -7.101  -2.590  1.00 36.35           O  
-HETATM 6891  O   HOH B2103      72.796 -13.559  -2.354  1.00 43.57           O  
-HETATM 6892  O   HOH B2104      82.370 -14.522   4.014  1.00 37.18           O  
-HETATM 6893  O   HOH B2105      79.386  32.508  13.915  1.00 30.89           O  
-HETATM 6894  O   HOH B2106      73.322 -17.168   1.089  1.00 43.53           O  
-HETATM 6895  O   HOH B2107      74.550  23.705  13.696  1.00 20.94           O  
-HETATM 6896  O   HOH B2108      73.072  27.568  13.655  1.00 33.56           O  
-HETATM 6897  O   HOH B2109      78.279  21.452  25.242  1.00 38.80           O  
-HETATM 6898  O   HOH B2110      71.474  -7.017  -0.822  1.00 33.26           O  
-HETATM 6899  O   HOH B2111      72.830  21.391  19.880  1.00 37.05           O  
-HETATM 6900  O   HOH B2112      73.339  24.240  15.776  1.00 40.38           O  
-HETATM 6901  O   HOH B2113      74.031  15.725  23.297  1.00 49.23           O  
-HETATM 6902  O   HOH B2114      71.987  19.235  22.811  1.00 42.02           O  
-HETATM 6903  O   HOH B2115      65.553 -10.435  -6.114  1.00 28.41           O  
-HETATM 6904  O   HOH B2116      69.014  -7.892  -5.898  1.00 26.36           O  
-HETATM 6905  O   HOH B2117      56.985 -10.266 -13.757  1.00 52.51           O  
-HETATM 6906  O   HOH B2118      77.930  18.221  25.842  1.00 41.28           O  
-HETATM 6907  O   HOH B2119      87.932  18.671  25.528  1.00 47.65           O  
-HETATM 6908  O   HOH B2120      81.807  11.604  25.455  1.00 36.65           O  
-HETATM 6909  O   HOH B2121      76.685  15.088  23.073  1.00 37.81           O  
-HETATM 6910  O   HOH B2122      60.038 -23.013  -0.573  1.00 44.79           O  
-HETATM 6911  O   HOH B2123      58.856 -16.337   8.723  1.00 43.45           O  
-HETATM 6912  O   HOH B2124      67.342 -12.449  -5.782  1.00 41.38           O  
-HETATM 6913  O   HOH B2125      79.980 -19.149   7.447  1.00 39.54           O  
-HETATM 6914  O   HOH B2126      78.549   8.381  -4.271  1.00 17.01           O  
-HETATM 6915  O   HOH B2127      81.885 -17.929   6.347  1.00 39.27           O  
-HETATM 6916  O   HOH B2128      75.142  -0.275  -4.893  1.00 41.38           O  
-HETATM 6917  O   HOH B2129      77.534   2.126  -7.738  1.00 43.50           O  
-HETATM 6918  O   HOH B2130      74.227   0.570  -0.159  1.00 25.93           O  
-HETATM 6919  O   HOH B2131      74.372   6.916  -7.130  1.00 31.73           O  
-HETATM 6920  O   HOH B2132      78.549   5.531 -10.593  1.00 24.98           O  
-HETATM 6921  O   HOH B2133      83.495  -9.100  21.564  1.00 40.65           O  
-HETATM 6922  O   HOH B2134      85.838   0.752  -7.792  1.00 27.47           O  
-HETATM 6923  O   HOH B2135      86.282   0.486 -11.005  1.00 45.65           O  
-HETATM 6924  O   HOH B2136      86.338   5.721 -12.589  1.00 41.23           O  
-HETATM 6925  O   HOH B2137      83.575   7.806 -11.856  1.00 25.60           O  
-HETATM 6926  O   HOH B2138      91.939  -1.931  -6.785  1.00 33.31           O  
-HETATM 6927  O   HOH B2139      91.324  -0.960 -10.799  1.00 44.13           O  
-HETATM 6928  O   HOH B2140      96.874  -0.165 -11.246  1.00 40.44           O  
-HETATM 6929  O   HOH B2141      75.598 -10.809  23.453  1.00 43.30           O  
-HETATM 6930  O   HOH B2142      96.305   4.778  -7.830  1.00 36.21           O  
-HETATM 6931  O   HOH B2143      52.363   3.591 -10.756  1.00 43.87           O  
-HETATM 6932  O   HOH B2144      57.933  16.057  -6.310  1.00 37.49           O  
-HETATM 6933  O   HOH B2145      51.195   5.471  -6.818  1.00 31.54           O  
-HETATM 6934  O   HOH B2146      51.151   8.882  -4.554  1.00 30.91           O  
-HETATM 6935  O   HOH B2147      53.813  11.766  -5.814  1.00 39.94           O  
-HETATM 6936  O   HOH B2148     104.284   5.691  -3.275  1.00 44.74           O  
-HETATM 6937  O   HOH B2149      56.730  15.008  -4.152  1.00 43.77           O  
-HETATM 6938  O   HOH B2150      55.121  12.377  -0.800  1.00 24.44           O  
-HETATM 6939  O   HOH B2151     101.136   9.295  -2.905  1.00 38.53           O  
-HETATM 6940  O   HOH B2152      63.225   3.176 -11.150  1.00 53.35           O  
-HETATM 6941  O   HOH B2153      99.955   1.279   0.161  1.00 44.46           O  
-HETATM 6942  O   HOH B2154      56.776  13.918   3.596  1.00 27.47           O  
-HETATM 6943  O   HOH B2155      54.551  13.647   2.224  1.00 39.27           O  
-HETATM 6944  O   HOH B2156      99.700   9.174   3.317  1.00 30.35           O  
-HETATM 6945  O   HOH B2157      51.685  10.894  -2.688  1.00 33.90           O  
-HETATM 6946  O   HOH B2158      96.514  15.113  -5.479  1.00 48.95           O  
-HETATM 6947  O   HOH B2159      44.024  -5.117   1.633  1.00 44.07           O  
-HETATM 6948  O   HOH B2160      97.678  14.965   5.216  1.00 38.80           O  
-HETATM 6949  O   HOH B2161      53.008 -13.254  11.076  1.00 36.20           O  
-HETATM 6950  O   HOH B2162      54.454 -18.446  10.123  1.00 44.38           O  
-HETATM 6951  O   HOH B2163      92.857  17.372   0.729  1.00 26.28           O  
-HETATM 6952  O   HOH B2164      50.656   3.227  -8.547  1.00 37.15           O  
-HETATM 6953  O   HOH B2165      90.437  21.305   2.969  1.00 28.02           O  
-HETATM 6954  O   HOH B2166      95.750  22.888   6.207  1.00 41.59           O  
-HETATM 6955  O   HOH B2167      53.643   1.083  16.614  1.00 39.13           O  
-HETATM 6956  O   HOH B2168      82.596  20.045  10.250  1.00 39.92           O  
-HETATM 6957  O   HOH B2169      82.380  18.168  11.984  1.00 31.77           O  
-HETATM 6958  O   HOH B2170      68.205  -8.807  25.062  1.00 43.08           O  
-HETATM 6959  O   HOH B2171      87.610  12.831  17.509  1.00 29.52           O  
-HETATM 6960  O   HOH B2172      83.047   0.347   2.201  1.00 22.38           O  
-HETATM 6961  O   HOH B2173      81.224   0.475  -7.989  1.00 28.84           O  
-HETATM 6962  O   HOH B2174      77.540   0.137  -6.207  1.00 37.69           O  
-HETATM 6963  O   HOH B2175      72.361  -3.153  -2.019  1.00 34.42           O  
-HETATM 6964  O   HOH B2176      75.476  -2.204   0.211  1.00 32.42           O  
-HETATM 6965  O   HOH B2177      80.835  -3.078  -7.345  1.00 31.58           O  
-HETATM 6966  O   HOH B2178      81.361  -7.394  -5.393  1.00 29.84           O  
-HETATM 6967  O   HOH B2179      90.800  -4.763 -10.313  1.00 29.59           O  
-HETATM 6968  O   HOH B2180      84.974  -1.737  -7.314  1.00 43.98           O  
-HETATM 6969  O   HOH B2181      88.805  -6.485   1.747  1.00 22.48           O  
-HETATM 6970  O   HOH B2182      95.958  -6.511   1.742  1.00 30.81           O  
-HETATM 6971  O   HOH B2183      98.155  -3.111  -4.819  1.00 48.45           O  
-HETATM 6972  O   HOH B2184      96.186  -3.379  -7.420  1.00 33.05           O  
-HETATM 6973  O   HOH B2185      98.406  -3.084  11.807  1.00 46.24           O  
-HETATM 6974  O   HOH B2186      99.634   6.731   4.863  1.00 41.33           O  
-HETATM 6975  O   HOH B2187      99.181  11.896   8.572  1.00 44.38           O  
-HETATM 6976  O   HOH B2188      98.332   9.240  17.314  1.00 32.44           O  
-HETATM 6977  O   HOH B2189      94.779   6.403  17.512  1.00 40.76           O  
-HETATM 6978  O   HOH B2190     103.305  12.144  13.668  1.00 48.87           O  
-HETATM 6979  O   HOH B2191     101.004   6.763  12.375  1.00 38.13           O  
-HETATM 6980  O   HOH B2192      93.793  21.007  12.178  1.00 29.47           O  
-HETATM 6981  O   HOH B2193      93.175  18.167  15.664  1.00 39.50           O  
-HETATM 6982  O   HOH B2194      99.386  17.029  19.722  1.00 41.45           O  
-HETATM 6983  O   HOH B2195      87.863   7.911  19.859  1.00 42.90           O  
-HETATM 6984  O   HOH B2196      87.072  10.130  17.408  1.00 28.29           O  
-HETATM 6985  O   HOH B2197      90.745   9.608  21.706  1.00 42.57           O  
-HETATM 6986  O   HOH B2198      93.940   9.071  15.484  1.00 27.75           O  
-HETATM 6987  O   HOH B2199      80.049  -1.121   1.082  1.00 34.44           O  
-HETATM 6988  O   HOH B2200      75.302  -5.939  -0.683  1.00 23.38           O  
-HETATM 6989  O   HOH B2201      81.820 -13.321  -4.021  1.00 39.05           O  
-HETATM 6990  O   HOH B2202      74.793 -11.812  -2.937  1.00 39.42           O  
-HETATM 6991  O   HOH B2203      80.757  -9.918  -5.953  1.00 33.71           O  
-HETATM 6992  O   HOH B2204      74.773  -6.073  -7.850  1.00 48.08           O  
-HETATM 6993  O   HOH B2205      78.437  -9.717  -7.128  1.00 38.31           O  
-HETATM 6994  O   HOH B2206      82.887  -6.588  -1.709  1.00 31.64           O  
-HETATM 6995  O   HOH B2207      74.233  -9.588  -4.016  1.00 32.88           O  
-HETATM 6996  O   HOH B2208      84.492 -12.586   3.393  1.00 28.57           O  
-HETATM 6997  O   HOH B2209      86.856 -14.100   1.926  1.00 37.20           O  
-HETATM 6998  O   HOH B2210      75.782 -17.100   1.921  1.00 41.94           O  
-HETATM 6999  O   HOH B2211      93.920  -8.262   2.688  1.00 45.23           O  
-HETATM 7000  O   HOH B2212      91.416  -8.710  12.594  1.00 44.60           O  
-HETATM 7001  O   HOH B2213      94.824  -5.132   8.625  1.00 34.62           O  
-HETATM 7002  O   HOH B2214      93.660  -0.417  13.690  1.00 46.51           O  
-HETATM 7003  O   HOH B2215      90.380   2.189  13.185  1.00 26.67           O  
-HETATM 7004  O   HOH B2216      86.521   3.065  18.338  1.00 37.26           O  
-HETATM 7005  O   HOH B2217      85.468   0.310  18.172  1.00 32.05           O  
-HETATM 7006  O   HOH B2218      73.980  -4.019   1.531  1.00 19.46           O  
-HETATM 7007  O   HOH B2219      67.778  -2.999   8.459  1.00 15.45           O  
-HETATM 7008  O   HOH B2220      71.522  -4.537   0.111  1.00 17.70           O  
-HETATM 7009  O   HOH B2221      73.518   3.152   2.717  1.00 26.73           O  
-HETATM 7010  O   HOH B2222      72.106  -1.095   0.230  1.00 43.81           O  
-HETATM 7011  O   HOH B2223      63.683   0.660  -6.452  1.00 19.18           O  
-HETATM 7012  O   HOH B2224      61.727  -6.849 -12.611  1.00 35.56           O  
-HETATM 7013  O   HOH B2225      66.497  -7.757  -5.011  1.00 24.13           O  
-HETATM 7014  O   HOH B2226      57.701  -8.511 -11.617  1.00 28.09           O  
-HETATM 7015  O   HOH B2227      65.907 -10.412  -8.749  1.00 25.79           O  
-HETATM 7016  O   HOH B2228      65.514 -13.411  -8.930  1.00 46.99           O  
-HETATM 7017  O   HOH B2229      62.920 -10.735  -6.485  1.00 22.07           O  
-HETATM 7018  O   HOH B2230      61.560 -10.051  -4.218  1.00 20.86           O  
-HETATM 7019  O   HOH B2231      56.058 -11.772   2.741  1.00 27.75           O  
-HETATM 7020  O   HOH B2232      61.893  -4.998   4.881  1.00 16.94           O  
-HETATM 7021  O   HOH B2233      64.727  -9.520   1.165  1.00 14.41           O  
-HETATM 7022  O   HOH B2234      64.944 -12.309  17.008  1.00 19.24           O  
-HETATM 7023  O   HOH B2235      66.476 -16.229   8.279  1.00 31.72           O  
-HETATM 7024  O   HOH B2236      63.082 -20.462   1.721  1.00 44.80           O  
-HETATM 7025  O   HOH B2237      62.867 -17.571   9.156  1.00 27.25           O  
-HETATM 7026  O   HOH B2238      65.001 -16.846   0.135  1.00 48.71           O  
-HETATM 7027  O   HOH B2239      54.321 -14.193   4.491  1.00 36.28           O  
-HETATM 7028  O   HOH B2240      60.769 -21.651   2.053  1.00 38.25           O  
-HETATM 7029  O   HOH B2241      57.012 -18.009   6.984  1.00 48.93           O  
-HETATM 7030  O   HOH B2242      52.810 -16.050   3.492  1.00 42.25           O  
-HETATM 7031  O   HOH B2243      55.358 -15.223  -3.513  1.00 26.79           O  
-HETATM 7032  O   HOH B2244      57.547 -17.265  -2.449  1.00 28.61           O  
-HETATM 7033  O   HOH B2245      64.051 -15.901  -2.353  1.00 49.69           O  
-HETATM 7034  O   HOH B2246      62.642 -13.284  -4.890  1.00 35.77           O  
-HETATM 7035  O   HOH B2247      66.348 -14.446   2.588  1.00 24.62           O  
-HETATM 7036  O   HOH B2248      70.426 -13.822  -0.664  1.00 30.85           O  
-HETATM 7037  O   HOH B2249      68.228 -13.653  -3.529  1.00 32.21           O  
-HETATM 7038  O   HOH B2250      70.715 -13.213   2.248  1.00 19.79           O  
-HETATM 7039  O   HOH B2251      72.057 -11.398   3.410  1.00 24.32           O  
-HETATM 7040  O   HOH B2252      67.523  -5.777   8.867  1.00 14.47           O  
-HETATM 7041  O   HOH B2253      69.611 -14.153  15.856  1.00 17.81           O  
-HETATM 7042  O   HOH B2254      75.228 -16.986   6.905  1.00 34.46           O  
-HETATM 7043  O   HOH B2255      70.251 -15.866   2.667  1.00 28.79           O  
-HETATM 7044  O   HOH B2256      78.012 -17.705   8.636  1.00 40.85           O  
-HETATM 7045  O   HOH B2257      73.182 -18.266   8.012  1.00 43.63           O  
-HETATM 7046  O   HOH B2258      82.328 -15.435   6.427  1.00 27.00           O  
-HETATM 7047  O   HOH B2259      73.525 -16.996  14.481  1.00 18.45           O  
-HETATM 7048  O   HOH B2260      72.325 -14.949  15.843  1.00 19.94           O  
-HETATM 7049  O   HOH B2261      81.129  -1.895  21.708  1.00 46.48           O  
-HETATM 7050  O   HOH B2262      85.279  -5.731  19.911  1.00 33.45           O  
-HETATM 7051  O   HOH B2263      81.110  -8.587  20.314  1.00 28.27           O  
-HETATM 7052  O   HOH B2264      82.766  -2.070  19.711  1.00 27.61           O  
-HETATM 7053  O   HOH B2265      61.520   2.876   7.077  1.00 18.85           O  
-HETATM 7054  O   HOH B2266      61.214   0.639  -5.421  1.00 15.94           O  
-HETATM 7055  O   HOH B2267      47.299  -2.971 -11.016  1.00 43.09           O  
-HETATM 7056  O   HOH B2268      49.085 -13.480  -6.825  1.00 50.01           O  
-HETATM 7057  O   HOH B2269      49.966 -11.498  -2.463  1.00 44.72           O  
-HETATM 7058  O   HOH B2270      52.238 -12.011  -1.374  1.00 31.00           O  
-HETATM 7059  O   HOH B2271      55.549 -14.610  -7.450  1.00 27.42           O  
-HETATM 7060  O   HOH B2272      52.953 -16.220  -7.171  1.00 50.56           O  
-HETATM 7061  O   HOH B2273      51.300  -9.217  -8.768  1.00 31.25           O  
-HETATM 7062  O   HOH B2274      58.936  -6.054 -13.113  1.00 33.89           O  
-HETATM 7063  O   HOH B2275      61.404  -2.792 -12.390  1.00 40.22           O  
-HETATM 7064  O   HOH B2276      53.956   1.140 -13.898  1.00 38.21           O  
-HETATM 7065  O   HOH B2277      58.673  -3.338 -13.260  1.00 27.28           O  
-HETATM 7066  O   HOH B2278      58.625   2.677 -12.797  1.00 29.19           O  
-HETATM 7067  O   HOH B2279      54.898   2.981 -12.134  1.00 39.99           O  
-HETATM 7068  O   HOH B2280      57.959   4.971 -12.149  1.00 31.13           O  
-HETATM 7069  O   HOH B2281      52.506   9.480  -6.921  1.00 32.21           O  
-HETATM 7070  O   HOH B2282      53.246   6.696  -7.732  1.00 29.93           O  
-HETATM 7071  O   HOH B2283      57.085  14.008  -8.398  1.00 47.69           O  
-HETATM 7072  O   HOH B2284      56.002  12.541  -4.389  1.00 39.82           O  
-HETATM 7073  O   HOH B2285      57.630  12.718  -0.289  1.00 23.46           O  
-HETATM 7074  O   HOH B2286      58.633  14.711  -2.314  1.00 31.03           O  
-HETATM 7075  O   HOH B2287      60.301  15.591  -5.768  1.00 27.17           O  
-HETATM 7076  O   HOH B2288      65.928  12.175  -8.932  1.00 21.52           O  
-HETATM 7077  O   HOH B2289      64.988  15.080  -6.407  1.00 34.33           O  
-HETATM 7078  O   HOH B2290      63.051   9.668  -2.809  1.00 16.69           O  
-HETATM 7079  O   HOH B2291      67.929  12.230  -6.822  1.00 28.38           O  
-HETATM 7080  O   HOH B2292      63.779   2.978  -8.062  1.00 24.43           O  
-HETATM 7081  O   HOH B2293      64.474   6.077 -10.062  1.00 32.84           O  
-HETATM 7082  O   HOH B2294      63.738  14.016   2.860  1.00 20.12           O  
-HETATM 7083  O   HOH B2295      58.847  13.771   2.152  1.00 20.75           O  
-HETATM 7084  O   HOH B2296      63.227   8.900   0.045  1.00 31.09           O  
-HETATM 7085  O   HOH B2297      55.101  12.752   8.861  1.00 36.37           O  
-HETATM 7086  O   HOH B2298      62.260  16.607   3.352  1.00 25.31           O  
-HETATM 7087  O   HOH B2299      62.598  15.816   8.265  1.00 35.46           O  
-HETATM 7088  O   HOH B2300      52.310  10.814   1.785  1.00 33.11           O  
-HETATM 7089  O   HOH B2301      50.515   3.698  -0.888  1.00 18.73           O  
-HETATM 7090  O   HOH B2302      51.262   6.132  -4.298  1.00 31.11           O  
-HETATM 7091  O   HOH B2303      51.770   3.849   1.736  1.00 18.92           O  
-HETATM 7092  O   HOH B2304      53.414  10.422  -0.577  1.00 29.52           O  
-HETATM 7093  O   HOH B2305      47.557   8.209  -1.739  1.00 32.63           O  
-HETATM 7094  O   HOH B2306      49.326  10.431   1.098  1.00 31.19           O  
-HETATM 7095  O   HOH B2307      42.434   2.073  -0.482  1.00 48.07           O  
-HETATM 7096  O   HOH B2308      43.448   7.025   4.311  1.00 53.98           O  
-HETATM 7097  O   HOH B2309      46.860   5.286   5.272  1.00 35.21           O  
-HETATM 7098  O   HOH B2310      42.801  -2.701   4.494  1.00 47.75           O  
-HETATM 7099  O   HOH B2311      44.026   0.287   2.403  1.00 26.50           O  
-HETATM 7100  O   HOH B2312      50.913  -0.969  11.662  1.00 37.68           O  
-HETATM 7101  O   HOH B2313      47.464   0.768   8.540  1.00 46.24           O  
-HETATM 7102  O   HOH B2314      52.820   2.302  12.796  1.00 30.33           O  
-HETATM 7103  O   HOH B2315      46.009  -3.810   2.519  1.00 34.63           O  
-HETATM 7104  O   HOH B2316      56.830 -17.505  11.720  1.00 36.15           O  
-HETATM 7105  O   HOH B2317      54.552 -15.518  14.872  1.00 18.94           O  
-HETATM 7106  O   HOH B2318      54.715 -15.979  11.119  1.00 51.06           O  
-HETATM 7107  O   HOH B2319      55.783 -12.707  10.484  1.00 25.88           O  
-HETATM 7108  O   HOH B2320      61.151 -16.253  10.585  1.00 26.85           O  
-HETATM 7109  O   HOH B2321      51.869 -10.240   4.892  1.00 44.28           O  
-HETATM 7110  O   HOH B2322      48.036   4.560  -1.290  1.00 26.62           O  
-HETATM 7111  O   HOH B2323      43.898   4.988  -2.777  1.00 39.58           O  
-HETATM 7112  O   HOH B2324      44.055  -1.787   0.783  1.00 36.83           O  
-HETATM 7113  O   HOH B2325      50.273   0.228  -8.251  1.00 32.28           O  
-HETATM 7114  O   HOH B2326      45.878   6.925  -4.397  1.00 44.67           O  
-HETATM 7115  O   HOH B2327      48.356   5.500  -3.732  1.00 36.62           O  
-HETATM 7116  O   HOH B2328      51.226   0.892  -0.297  1.00 17.88           O  
-HETATM 7117  O   HOH B2329      59.097  -4.802   3.929  1.00 15.51           O  
-HETATM 7118  O   HOH B2330      62.098  -1.814   5.043  1.00 39.11           O  
-HETATM 7119  O   HOH B2331      62.566  -4.641   7.634  1.00 13.35           O  
-HETATM 7120  O   HOH B2332      59.971  -3.261   6.643  1.00 18.08           O  
-HETATM 7121  O   HOH B2333      64.181   1.450   9.792  1.00 17.16           O  
-HETATM 7122  O   HOH B2334      52.634  -1.833  13.888  1.00 27.39           O  
-HETATM 7123  O   HOH B2335      54.087   0.409  14.134  1.00 19.56           O  
-HETATM 7124  O   HOH B2336      56.034  -6.678  17.682  1.00 47.49           O  
-HETATM 7125  O   HOH B2337      62.612  -4.102  21.405  1.00 30.69           O  
-HETATM 7126  O   HOH B2338      60.721  -1.897  22.606  1.00 41.67           O  
-HETATM 7127  O   HOH B2339      57.032   2.460  20.053  1.00 32.10           O  
-HETATM 7128  O   HOH B2340      60.694   2.379  21.364  1.00 17.82           O  
-HETATM 7129  O   HOH B2341      63.506  -8.196  18.766  1.00 15.28           O  
-HETATM 7130  O   HOH B2342      66.739  -8.091  23.065  1.00 21.30           O  
-HETATM 7131  O   HOH B2343      73.461  -6.555  24.211  1.00 43.16           O  
-HETATM 7132  O   HOH B2344      64.093  -6.562  24.138  1.00 38.64           O  
-HETATM 7133  O   HOH B2345      68.409 -12.823  18.045  1.00 20.92           O  
-HETATM 7134  O   HOH B2346      78.596  -8.061  21.656  1.00 22.88           O  
-HETATM 7135  O   HOH B2347      77.062  -3.447  21.892  1.00 27.40           O  
-HETATM 7136  O   HOH B2348      64.844   1.991  12.541  1.00 16.10           O  
-HETATM 7137  O   HOH B2349      68.823   9.023  -0.565  1.00 36.75           O  
-HETATM 7138  O   HOH B2350      70.398  13.633   5.185  1.00 14.58           O  
-HETATM 7139  O   HOH B2351      66.705  13.078  11.534  1.00 21.14           O  
-HETATM 7140  O   HOH B2352      64.091  13.827   9.176  1.00 28.26           O  
-HETATM 7141  O   HOH B2353      66.156   8.455   3.299  1.00 15.93           O  
-HETATM 7142  O   HOH B2354      65.136  11.706  13.381  1.00 19.26           O  
-HETATM 7143  O   HOH B2355      60.382  15.160   9.956  1.00 36.01           O  
-HETATM 7144  O   HOH B2356      62.897  13.506  13.496  1.00 24.83           O  
-HETATM 7145  O   HOH B2357      54.768   6.111  11.359  1.00 19.92           O  
-HETATM 7146  O   HOH B2358      53.011  10.962  10.158  1.00 38.00           O  
-HETATM 7147  O   HOH B2359      56.610  14.156  10.850  1.00 32.04           O  
-HETATM 7148  O   HOH B2360      55.140  11.238  15.703  1.00 38.04           O  
-HETATM 7149  O   HOH B2361      55.999  15.827  15.920  1.00 54.37           O  
-HETATM 7150  O   HOH B2362      59.294   7.211  20.154  1.00 34.24           O  
-HETATM 7151  O   HOH B2363      58.645  11.900  21.130  1.00 46.11           O  
-HETATM 7152  O   HOH B2364      54.049  10.959  12.866  1.00 52.58           O  
-HETATM 7153  O   HOH B2365      55.345   5.684  17.746  1.00 31.35           O  
-HETATM 7154  O   HOH B2366      61.347  12.151  18.118  1.00 23.70           O  
-HETATM 7155  O   HOH B2367      57.485   4.649  18.782  1.00 25.70           O  
-HETATM 7156  O   HOH B2368      63.863   0.391  26.645  1.00 35.19           O  
-HETATM 7157  O   HOH B2369      60.941   9.744  23.577  1.00 38.30           O  
-HETATM 7158  O   HOH B2370      58.966   9.137  21.992  1.00 29.99           O  
-HETATM 7159  O   HOH B2371      64.909   9.326  23.077  1.00 38.89           O  
-HETATM 7160  O   HOH B2372      64.521   4.106  27.052  1.00 36.94           O  
-HETATM 7161  O   HOH B2373      59.551   4.924  21.918  1.00 30.97           O  
-HETATM 7162  O   HOH B2374      64.919   7.075  26.268  1.00 46.41           O  
-HETATM 7163  O   HOH B2375      60.958   1.508  23.974  1.00 33.82           O  
-HETATM 7164  O   HOH B2376      66.044  -1.307  26.619  1.00 49.07           O  
-HETATM 7165  O   HOH B2377      69.772  -1.901  27.121  1.00 36.51           O  
-HETATM 7166  O   HOH B2378      69.131   5.972  29.019  1.00 32.97           O  
-HETATM 7167  O   HOH B2379      68.526   1.998  30.023  1.00 28.44           O  
-HETATM 7168  O   HOH B2380      66.973   8.786  26.473  1.00 31.01           O  
-HETATM 7169  O   HOH B2381      75.252  -0.196  26.202  1.00 31.30           O  
-HETATM 7170  O   HOH B2382      83.096   6.074  18.466  1.00 22.04           O  
-HETATM 7171  O   HOH B2383      83.614   3.033  18.338  1.00 32.95           O  
-HETATM 7172  O   HOH B2384      81.333   0.980  22.408  1.00 32.16           O  
-HETATM 7173  O   HOH B2385      80.178   7.216  20.903  1.00 23.20           O  
-HETATM 7174  O   HOH B2386      74.872  10.047  28.566  1.00 48.18           O  
-HETATM 7175  O   HOH B2387      74.674   9.640  25.859  1.00 35.94           O  
-HETATM 7176  O   HOH B2388      86.018  10.306  26.305  1.00 42.18           O  
-HETATM 7177  O   HOH B2389      85.779  10.267  20.341  1.00 41.07           O  
-HETATM 7178  O   HOH B2390      87.912  10.964  22.847  1.00 44.61           O  
-HETATM 7179  O   HOH B2391      88.856  19.061  21.903  1.00 36.85           O  
-HETATM 7180  O   HOH B2392      92.817  16.187  21.281  1.00 40.84           O  
-HETATM 7181  O   HOH B2393      93.162  25.229  17.086  1.00 45.11           O  
-HETATM 7182  O   HOH B2394      89.935  25.414  18.931  1.00 45.21           O  
-HETATM 7183  O   HOH B2395      89.572  24.207  16.347  1.00 26.20           O  
-HETATM 7184  O   HOH B2396      91.420  24.299  -0.017  1.00 42.68           O  
-HETATM 7185  O   HOH B2397      88.041  26.941   0.707  1.00 39.84           O  
-HETATM 7186  O   HOH B2398      88.596  22.575   1.909  1.00 37.78           O  
-HETATM 7187  O   HOH B2399      86.087  31.303  15.433  1.00 40.95           O  
-HETATM 7188  O   HOH B2400      95.447  32.659  14.592  1.00 54.46           O  
-HETATM 7189  O   HOH B2401      87.724  33.579  15.945  1.00 41.83           O  
-HETATM 7190  O   HOH B2402      81.895  34.196  14.006  1.00 40.68           O  
-HETATM 7191  O   HOH B2403     102.802   3.498  -6.684  1.00 42.54           O  
-HETATM 7192  O   HOH B2404     101.177  -1.971  -4.819  1.00 41.95           O  
-HETATM 7193  O   HOH B2405     102.094   4.415  -9.578  1.00 46.75           O  
-HETATM 7194  O   HOH B2406      49.722  -6.478  10.820  1.00 36.25           O  
-HETATM 7195  O   HOH B2407      50.886  -9.052   7.851  1.00 43.32           O  
-HETATM 7196  O   HOH B2408      46.575  -3.966   9.094  1.00 44.53           O  
-HETATM 7197  O   HOH B2409      77.728 -10.787  21.207  1.00 43.64           O  
-HETATM 7198  O   HOH B2410      75.971 -12.109  18.025  1.00 33.91           O  
-HETATM 7199  O   HOH B2411      93.795 -12.311   7.998  1.00 49.02           O  
-HETATM 7200  O   HOH B2412      87.255 -12.758   4.918  1.00 35.22           O  
-HETATM 7201  O   HOH B2413      76.267  15.373  -4.274  1.00 43.35           O  
-HETATM 7202  O   HOH B2414      70.075  10.822  -7.789  1.00 32.84           O  
-HETATM 7203  O   HOH B2415      69.311  10.417  -2.508  1.00 34.24           O  
-CONECT 6156 6157 6158 6159 6160                                                 
-CONECT 6157 6156                                                                
-CONECT 6158 6156                                                                
-CONECT 6159 6156                                                                
-CONECT 6160 6156                                                                
-CONECT 6161 6162 6163 6164 6165                                                 
-CONECT 6162 6161                                                                
-CONECT 6163 6161                                                                
-CONECT 6164 6161                                                                
-CONECT 6165 6161                                                                
-CONECT 6166 6167 6168 6169 6170                                                 
-CONECT 6167 6166                                                                
-CONECT 6168 6166                                                                
-CONECT 6169 6166                                                                
-CONECT 6170 6166                                                                
-CONECT 6171 6172 6173 6174 6175                                                 
-CONECT 6172 6171                                                                
-CONECT 6173 6171                                                                
-CONECT 6174 6171                                                                
-CONECT 6175 6171                                                                
-CONECT 6176 6177 6178 6179 6180                                                 
-CONECT 6177 6176                                                                
-CONECT 6178 6176                                                                
-CONECT 6179 6176                                                                
-CONECT 6180 6176                                                                
-CONECT 6181 6182 6183 6184 6185                                                 
-CONECT 6182 6181                                                                
-CONECT 6183 6181                                                                
-CONECT 6184 6181                                                                
-CONECT 6185 6181                                                                
-CONECT 6186 6187                                                                
-CONECT 6187 6186 6188 6198                                                      
-CONECT 6188 6187 6189 6193                                                      
-CONECT 6189 6188 6190 6191                                                      
-CONECT 6190 6189                                                                
-CONECT 6191 6189 6192                                                           
-CONECT 6192 6191 6193                                                           
-CONECT 6193 6188 6192 6194                                                      
-CONECT 6194 6193 6195 6196                                                      
-CONECT 6195 6194                                                                
-CONECT 6196 6194 6197 6198                                                      
-CONECT 6197 6196                                                                
-CONECT 6198 6187 6196 6199                                                      
-CONECT 6199 6198 6200                                                           
-CONECT 6200 6199 6201                                                           
-CONECT 6201 6200 6202 6212                                                      
-CONECT 6202 6201 6203 6204                                                      
-CONECT 6203 6202                                                                
-CONECT 6204 6202 6205 6209                                                      
-CONECT 6205 6204 6206 6207                                                      
-CONECT 6206 6205                                                                
-CONECT 6207 6205 6208                                                           
-CONECT 6208 6207 6209                                                           
-CONECT 6209 6204 6208 6210                                                      
-CONECT 6210 6209 6211 6212                                                      
-CONECT 6211 6210                                                                
-CONECT 6212 6201 6210 6213                                                      
-CONECT 6213 6212                                                                
-CONECT 6214 6215                                                                
-CONECT 6215 6214 6216 6226                                                      
-CONECT 6216 6215 6217 6221                                                      
-CONECT 6217 6216 6218 6219                                                      
-CONECT 6218 6217                                                                
-CONECT 6219 6217 6220                                                           
-CONECT 6220 6219 6221                                                           
-CONECT 6221 6216 6220 6222                                                      
-CONECT 6222 6221 6223 6224                                                      
-CONECT 6223 6222                                                                
-CONECT 6224 6222 6225 6226                                                      
-CONECT 6225 6224                                                                
-CONECT 6226 6215 6224 6227                                                      
-CONECT 6227 6226 6228                                                           
-CONECT 6228 6227 6229                                                           
-CONECT 6229 6228 6230 6240                                                      
-CONECT 6230 6229 6231 6232                                                      
-CONECT 6231 6230                                                                
-CONECT 6232 6230 6233 6237                                                      
-CONECT 6233 6232 6234 6235                                                      
-CONECT 6234 6233                                                                
-CONECT 6235 6233 6236                                                           
-CONECT 6236 6235 6237                                                           
-CONECT 6237 6232 6236 6238                                                      
-CONECT 6238 6237 6239 6240                                                      
-CONECT 6239 6238                                                                
-CONECT 6240 6229 6238 6241                                                      
-CONECT 6241 6240                                                                
-CONECT 6242 6243 6244 6245 6246                                                 
-CONECT 6243 6242                                                                
-CONECT 6244 6242                                                                
-CONECT 6245 6242                                                                
-CONECT 6246 6242                                                                
-CONECT 6247 6248 6249 6250 6251                                                 
-CONECT 6248 6247                                                                
-CONECT 6249 6247                                                                
-CONECT 6250 6247                                                                
-CONECT 6251 6247                                                                
-CONECT 6252 6253 6254 6255 6256                                                 
-CONECT 6253 6252                                                                
-CONECT 6254 6252                                                                
-CONECT 6255 6252                                                                
-CONECT 6256 6252                                                                
-CONECT 6257 6258 6259 6260 6261                                                 
-CONECT 6258 6257                                                                
-CONECT 6259 6257                                                                
-CONECT 6260 6257                                                                
-CONECT 6261 6257                                                                
-CONECT 6262 6263 6264 6265 6266                                                 
-CONECT 6263 6262                                                                
-CONECT 6264 6262                                                                
-CONECT 6265 6262                                                                
-CONECT 6266 6262                                                                
-CONECT 6267 6268                                                                
-CONECT 6268 6267 6269 6279                                                      
-CONECT 6269 6268 6270 6274                                                      
-CONECT 6270 6269 6271 6272                                                      
-CONECT 6271 6270                                                                
-CONECT 6272 6270 6273                                                           
-CONECT 6273 6272 6274                                                           
-CONECT 6274 6269 6273 6275                                                      
-CONECT 6275 6274 6276 6277                                                      
-CONECT 6276 6275                                                                
-CONECT 6277 6275 6278 6279                                                      
-CONECT 6278 6277                                                                
-CONECT 6279 6268 6277 6280                                                      
-CONECT 6280 6279 6281                                                           
-CONECT 6281 6280 6282                                                           
-CONECT 6282 6281 6283 6293                                                      
-CONECT 6283 6282 6284 6285                                                      
-CONECT 6284 6283                                                                
-CONECT 6285 6283 6286 6290                                                      
-CONECT 6286 6285 6287 6288                                                      
-CONECT 6287 6286                                                                
-CONECT 6288 6286 6289                                                           
-CONECT 6289 6288 6290                                                           
-CONECT 6290 6285 6289 6291                                                      
-CONECT 6291 6290 6292 6293                                                      
-CONECT 6292 6291                                                                
-CONECT 6293 6282 6291 6294                                                      
-CONECT 6294 6293                                                                
-CONECT 6295 6296                                                                
-CONECT 6296 6295 6297 6307                                                      
-CONECT 6297 6296 6298 6302                                                      
-CONECT 6298 6297 6299 6300                                                      
-CONECT 6299 6298                                                                
-CONECT 6300 6298 6301                                                           
-CONECT 6301 6300 6302                                                           
-CONECT 6302 6297 6301 6303                                                      
-CONECT 6303 6302 6304 6305                                                      
-CONECT 6304 6303                                                                
-CONECT 6305 6303 6306 6307                                                      
-CONECT 6306 6305                                                                
-CONECT 6307 6296 6305 6308                                                      
-CONECT 6308 6307 6309                                                           
-CONECT 6309 6308 6310                                                           
-CONECT 6310 6309 6311 6321                                                      
-CONECT 6311 6310 6312 6313                                                      
-CONECT 6312 6311                                                                
-CONECT 6313 6311 6314 6318                                                      
-CONECT 6314 6313 6315 6316                                                      
-CONECT 6315 6314                                                                
-CONECT 6316 6314 6317                                                           
-CONECT 6317 6316 6318                                                           
-CONECT 6318 6313 6317 6319                                                      
-CONECT 6319 6318 6320 6321                                                      
-CONECT 6320 6319                                                                
-CONECT 6321 6310 6319 6322                                                      
-CONECT 6322 6321                                                                
-MASTER      445    0   13   44   31    0   23    6 7201    2  167   68          
-END                                                                             
diff --git a/plip/test/pdb/2reg.pdb b/plip/test/pdb/2reg.pdb
deleted file mode 100644
index 94c7f7d..0000000
--- a/plip/test/pdb/2reg.pdb
+++ /dev/null
@@ -1,5374 +0,0 @@
-HEADER    TRANSPORT PROTEIN                       26-SEP-07   2REG              
-TITLE     ABC-TRANSPORTER CHOLINE BINDING PROTEIN IN COMPLEX WITH CHOLINE       
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: PUTATIVE GLYCINE BETAINE-BINDING ABC TRANSPORTER PROTEIN;  
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 ENGINEERED: YES;                                                     
-COMPND   5 MUTATION: YES                                                        
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: RHIZOBIUM MELILOTI;                             
-SOURCE   3 ORGANISM_COMMON: SINORHIZOBIUM MELILOTI;                             
-SOURCE   4 GENE: OPUC;                                                          
-SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
-KEYWDS    ABC-TRANSPORTER, TYPE II BINDING PROTEIN, AROMATIC BOX, TRANSPORT     
-KEYWDS   2 PROTEIN                                                              
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    C.OSWALD,L.SCHIMTT,S.H.J.SMITS,M.HOEING,L.SOHN-BOESER,E.BREMER        
-REVDAT   5   13-JUL-11 2REG    1       VERSN                                    
-REVDAT   4   09-JUN-09 2REG    1       REVDAT                                   
-REVDAT   3   24-FEB-09 2REG    1       VERSN                                    
-REVDAT   2   13-JAN-09 2REG    1       JRNL                                     
-REVDAT   1   16-SEP-08 2REG    0                                                
-JRNL        AUTH   C.OSWALD,S.H.SMITS,M.HOING,L.SOHN-BOSSER,L.DUPONT,           
-JRNL        AUTH 2 D.LE RUDULIER,L.SCHMITT,E.BREMER                             
-JRNL        TITL   CRYSTAL STRUCTURES OF THE CHOLINE/ACETYLCHOLINE              
-JRNL        TITL 2 SUBSTRATE-BINDING PROTEIN CHOX FROM SINORHIZOBIUM MELILOTI   
-JRNL        TITL 3 IN THE LIGANDED AND UNLIGANDED-CLOSED STATES.                
-JRNL        REF    J.BIOL.CHEM.                  V. 283 32848 2008              
-JRNL        REFN                   ISSN 0021-9258                               
-JRNL        PMID   18779321                                                     
-JRNL        DOI    10.1074/JBC.M806021200                                       
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
-REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.2                           
-REMARK   3   NUMBER OF REFLECTIONS             : 31972                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
-REMARK   3   R VALUE            (WORKING SET) : 0.180                           
-REMARK   3   FREE R VALUE                     : 0.222                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1687                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
-REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2201                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.00                        
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
-REMARK   3   BIN FREE R VALUE SET COUNT          : 116                          
-REMARK   3   BIN FREE R VALUE                    : 0.2710                       
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 4384                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 14                                      
-REMARK   3   SOLVENT ATOMS            : 269                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.99                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 0.03000                                              
-REMARK   3    B22 (A**2) : -1.62000                                             
-REMARK   3    B33 (A**2) : 1.60000                                              
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.11000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
-REMARK   3   ESU BASED ON R VALUE                            (A): 0.218         
-REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
-REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.112         
-REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.908         
-REMARK   3                                                                      
-REMARK   3 CORRELATION COEFFICIENTS.                                            
-REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
-REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
-REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4577 ; 0.007 ; 0.022       
-REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
-REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6229 ; 1.050 ; 1.955       
-REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
-REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   599 ; 5.369 ; 5.000       
-REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   204 ;39.207 ;26.373       
-REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   766 ;14.639 ;15.000       
-REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;15.323 ;15.000       
-REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   694 ; 0.076 ; 0.200       
-REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3494 ; 0.003 ; 0.020       
-REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2315 ; 0.187 ; 0.200       
-REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3188 ; 0.296 ; 0.200       
-REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   291 ; 0.106 ; 0.200       
-REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    80 ; 0.156 ; 0.200       
-REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.137 ; 0.200       
-REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
-REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3003 ; 0.325 ; 1.500       
-REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4682 ; 0.523 ; 2.000       
-REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1804 ; 0.832 ; 3.000       
-REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1541 ; 1.312 ; 4.500       
-REMARK   3                                                                      
-REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
-REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS STATISTICS                                           
-REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 1                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   A    31        A   114                          
-REMARK   3    RESIDUE RANGE :   A   235        A   314                          
-REMARK   3    ORIGIN FOR THE GROUP (A):  16.2510  -9.0220  16.0700              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   -.0404 T22:   -.0360                                     
-REMARK   3      T33:   -.0257 T12:   -.0256                                     
-REMARK   3      T13:   -.0128 T23:    .0363                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.4407 L22:   1.4411                                     
-REMARK   3      L33:   1.0859 L12:    .0902                                     
-REMARK   3      L13:   -.1617 L23:   -.2315                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:    .0311 S12:   -.0608 S13:   -.3351                       
-REMARK   3      S21:    .1418 S22:   -.0132 S23:   -.0530                       
-REMARK   3      S31:    .1020 S32:    .0209 S33:   -.0179                       
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 2                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   A   120        A   230                          
-REMARK   3    ORIGIN FOR THE GROUP (A):  15.2720  14.4850    .5590              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   -.0336 T22:    .0114                                     
-REMARK   3      T33:   -.0862 T12:   -.0136                                     
-REMARK   3      T13:    .0124 T23:    .0153                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:    .9136 L22:   1.8065                                     
-REMARK   3      L33:   1.4590 L12:    .2561                                     
-REMARK   3      L13:    .2198 L23:   -.5289                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   -.0177 S12:    .0289 S13:    .0783                       
-REMARK   3      S21:   -.0890 S22:    .0211 S23:   -.0050                       
-REMARK   3      S31:   -.1916 S32:   -.0798 S33:   -.0033                       
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 3                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   B    31        B   114                          
-REMARK   3    RESIDUE RANGE :   B   235        B   314                          
-REMARK   3    ORIGIN FOR THE GROUP (A):   2.3320 -37.2670   4.9120              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   -.0093 T22:   -.0831                                     
-REMARK   3      T33:   -.0342 T12:   -.0005                                     
-REMARK   3      T13:   -.0646 T23:    .0042                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:    .7759 L22:   2.2822                                     
-REMARK   3      L33:   3.0136 L12:    .4424                                     
-REMARK   3      L13:    .5718 L23:    .3544                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   -.2335 S12:    .0716 S13:    .2677                       
-REMARK   3      S21:   -.2776 S22:   -.0950 S23:    .0979                       
-REMARK   3      S31:   -.5017 S32:    .0636 S33:    .3285                       
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 4                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   B   120        B   230                          
-REMARK   3    ORIGIN FOR THE GROUP (A):    .2550 -60.8910  20.3980              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   -.0743 T22:   -.0528                                     
-REMARK   3      T33:   -.0847 T12:   -.0082                                     
-REMARK   3      T13:    .0336 T23:   -.0339                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.5806 L22:   2.2816                                     
-REMARK   3      L33:   2.0747 L12:   -.4200                                     
-REMARK   3      L13:   -.0191 L23:   -.3633                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   -.0768 S12:   -.0617 S13:   -.1297                       
-REMARK   3      S21:    .0794 S22:   -.0681 S23:    .0659                       
-REMARK   3      S31:    .2335 S32:   -.1025 S33:    .1449                       
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
-REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
-REMARK   3   VDW PROBE RADIUS   : 1.20                                          
-REMARK   3   ION PROBE RADIUS   : 0.80                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
-REMARK   3  POSITIONS                                                           
-REMARK   4                                                                      
-REMARK   4 2REG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-07.                  
-REMARK 100 THE RCSB ID CODE IS RCSB044760.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 26-APR-05                          
-REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
-REMARK 200  PH                             : 4.6                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
-REMARK 200  BEAMLINE                       : BW6                                
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05                               
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
-REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
-REMARK 200  DATA SCALING SOFTWARE          : HKL                                
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37385                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY                : 14.100                             
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : 0.04500                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: MOLREP                                                
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 36.73                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA ACETATE PH 4.6, 18% PEG 3350,    
-REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,Y+1/2,-Z                                             
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       92.70700            
-REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2                                                    
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     ALA A    28                                                      
-REMARK 465     GLU A   319                                                      
-REMARK 465     HIS A   320                                                      
-REMARK 465     HIS A   321                                                      
-REMARK 465     HIS A   322                                                      
-REMARK 465     HIS A   323                                                      
-REMARK 465     HIS A   324                                                      
-REMARK 465     HIS A   325                                                      
-REMARK 465     ALA B    28                                                      
-REMARK 465     LEU B   318                                                      
-REMARK 465     GLU B   319                                                      
-REMARK 465     HIS B   320                                                      
-REMARK 465     HIS B   321                                                      
-REMARK 465     HIS B   322                                                      
-REMARK 465     HIS B   323                                                      
-REMARK 465     HIS B   324                                                      
-REMARK 465     HIS B   325                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    ASP B 223   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    GLU A  31      -46.31     63.11                                   
-REMARK 500    ILE A 152     -137.17   -113.77                                   
-REMARK 500    SER A 181      -84.22   -152.71                                   
-REMARK 500    HIS A 208      138.34   -171.44                                   
-REMARK 500    LYS B 105        3.70     80.23                                   
-REMARK 500    ILE B 152     -140.01   -111.50                                   
-REMARK 500    ASP B 172       52.36     27.95                                   
-REMARK 500    SER B 181      -83.93   -158.28                                   
-REMARK 500    HIS B 208      138.06   -173.91                                   
-REMARK 500    ALA B 241     -132.92     49.94                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
-REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
-REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
-REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
-REMARK 500                                 MODEL     OMEGA                      
-REMARK 500 SER B  106     VAL B  107                   36.45                    
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
-REMARK 500                                                                      
-REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
-REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
-REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
-REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
-REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
-REMARK 500    VAL B  41        22.6      L          L   OUTSIDE RANGE           
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHT A 1                   
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHT B 1                   
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 2REJ   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 2RF1   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 2RIN   RELATED DB: PDB                                   
-DBREF  2REG A   28   318  UNP    Q92N37   Q92N37_RHIME    28    318             
-DBREF  2REG B   28   318  UNP    Q92N37   Q92N37_RHIME    28    318             
-SEQADV 2REG ASP A  251  UNP  Q92N37    GLY   251 ENGINEERED                     
-SEQADV 2REG GLU A  319  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS A  320  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS A  321  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS A  322  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS A  323  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS A  324  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS A  325  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG ASP B  251  UNP  Q92N37    GLY   251 ENGINEERED                     
-SEQADV 2REG GLU B  319  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS B  320  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS B  321  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS B  322  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS B  323  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS B  324  UNP  Q92N37              EXPRESSION TAG                 
-SEQADV 2REG HIS B  325  UNP  Q92N37              EXPRESSION TAG                 
-SEQRES   1 A  298  ALA GLU PRO GLU SER CYS GLY THR VAL ARG PHE SER ASP          
-SEQRES   2 A  298  VAL GLY TRP THR ASP ILE THR ALA THR THR ALA THR ALA          
-SEQRES   3 A  298  THR THR ILE LEU GLU ALA LEU GLY TYR GLU THR ASP VAL          
-SEQRES   4 A  298  LYS VAL LEU SER VAL PRO VAL THR TYR THR SER LEU LYS          
-SEQRES   5 A  298  ASN LYS ASP ILE ASP VAL PHE LEU GLY ASN TRP MET PRO          
-SEQRES   6 A  298  THR MET GLU ALA ASP ILE ALA PRO TYR ARG GLU ASP LYS          
-SEQRES   7 A  298  SER VAL GLU THR VAL ARG GLU ASN LEU ALA GLY ALA LYS          
-SEQRES   8 A  298  TYR THR LEU ALA THR ASN ALA LYS GLY ALA GLU LEU GLY          
-SEQRES   9 A  298  ILE LYS ASP PHE LYS ASP ILE ALA ALA HIS LYS ASP GLU          
-SEQRES  10 A  298  LEU ASP GLY LYS ILE TYR GLY ILE GLU PRO GLY ASN ASP          
-SEQRES  11 A  298  GLY ASN ARG LEU ILE ILE ASP MET VAL GLU LYS GLY THR          
-SEQRES  12 A  298  PHE ASP LEU LYS GLY PHE GLU VAL VAL GLU SER SER GLU          
-SEQRES  13 A  298  GLN GLY MET LEU ALA GLN VAL ALA ARG ALA GLU LYS SER          
-SEQRES  14 A  298  GLY ASP PRO ILE VAL PHE LEU GLY TRP GLU PRO HIS PRO          
-SEQRES  15 A  298  MET ASN ALA ASN PHE LYS LEU THR TYR LEU SER GLY GLY          
-SEQRES  16 A  298  ASP ASP VAL PHE GLY PRO ASN TYR GLY GLY ALA THR VAL          
-SEQRES  17 A  298  HIS THR ASN VAL ARG ALA GLY TYR THR THR GLU CYS PRO          
-SEQRES  18 A  298  ASN VAL ASP LYS LEU LEU GLN ASN LEU SER PHE SER LEU          
-SEQRES  19 A  298  GLN MET GLU ASN GLU ILE MET GLY LYS ILE LEU ASN ASP          
-SEQRES  20 A  298  GLY GLU ASP PRO GLU LYS ALA ALA ALA ALA TRP LEU LYS          
-SEQRES  21 A  298  ASP ASN PRO GLN SER ILE GLU PRO TRP LEU SER GLY VAL          
-SEQRES  22 A  298  ALA THR LYS ASP GLY GLY ASP GLY LEU ALA ALA VAL LYS          
-SEQRES  23 A  298  ALA ALA LEU GLY LEU GLU HIS HIS HIS HIS HIS HIS              
-SEQRES   1 B  298  ALA GLU PRO GLU SER CYS GLY THR VAL ARG PHE SER ASP          
-SEQRES   2 B  298  VAL GLY TRP THR ASP ILE THR ALA THR THR ALA THR ALA          
-SEQRES   3 B  298  THR THR ILE LEU GLU ALA LEU GLY TYR GLU THR ASP VAL          
-SEQRES   4 B  298  LYS VAL LEU SER VAL PRO VAL THR TYR THR SER LEU LYS          
-SEQRES   5 B  298  ASN LYS ASP ILE ASP VAL PHE LEU GLY ASN TRP MET PRO          
-SEQRES   6 B  298  THR MET GLU ALA ASP ILE ALA PRO TYR ARG GLU ASP LYS          
-SEQRES   7 B  298  SER VAL GLU THR VAL ARG GLU ASN LEU ALA GLY ALA LYS          
-SEQRES   8 B  298  TYR THR LEU ALA THR ASN ALA LYS GLY ALA GLU LEU GLY          
-SEQRES   9 B  298  ILE LYS ASP PHE LYS ASP ILE ALA ALA HIS LYS ASP GLU          
-SEQRES  10 B  298  LEU ASP GLY LYS ILE TYR GLY ILE GLU PRO GLY ASN ASP          
-SEQRES  11 B  298  GLY ASN ARG LEU ILE ILE ASP MET VAL GLU LYS GLY THR          
-SEQRES  12 B  298  PHE ASP LEU LYS GLY PHE GLU VAL VAL GLU SER SER GLU          
-SEQRES  13 B  298  GLN GLY MET LEU ALA GLN VAL ALA ARG ALA GLU LYS SER          
-SEQRES  14 B  298  GLY ASP PRO ILE VAL PHE LEU GLY TRP GLU PRO HIS PRO          
-SEQRES  15 B  298  MET ASN ALA ASN PHE LYS LEU THR TYR LEU SER GLY GLY          
-SEQRES  16 B  298  ASP ASP VAL PHE GLY PRO ASN TYR GLY GLY ALA THR VAL          
-SEQRES  17 B  298  HIS THR ASN VAL ARG ALA GLY TYR THR THR GLU CYS PRO          
-SEQRES  18 B  298  ASN VAL ASP LYS LEU LEU GLN ASN LEU SER PHE SER LEU          
-SEQRES  19 B  298  GLN MET GLU ASN GLU ILE MET GLY LYS ILE LEU ASN ASP          
-SEQRES  20 B  298  GLY GLU ASP PRO GLU LYS ALA ALA ALA ALA TRP LEU LYS          
-SEQRES  21 B  298  ASP ASN PRO GLN SER ILE GLU PRO TRP LEU SER GLY VAL          
-SEQRES  22 B  298  ALA THR LYS ASP GLY GLY ASP GLY LEU ALA ALA VAL LYS          
-SEQRES  23 B  298  ALA ALA LEU GLY LEU GLU HIS HIS HIS HIS HIS HIS              
-HET    CHT  A   1       7                                                       
-HET    CHT  B   1       7                                                       
-HETNAM     CHT CHOLINE ION                                                      
-FORMUL   3  CHT    2(C5 H14 N O 1+)                                             
-FORMUL   5  HOH   *269(H2 O)                                                    
-HELIX    1   1 GLU A   31  CYS A   33  5                                   3    
-HELIX    2   2 TRP A   43  LEU A   60  1                                  18    
-HELIX    3   3 SER A   70  ASN A   80  1                                  11    
-HELIX    4   4 MET A   94  ASP A  104  1                                  11    
-HELIX    5   5 ASN A  124  LEU A  130  1                                   7    
-HELIX    6   6 ASP A  134  LYS A  142  5                                   9    
-HELIX    7   7 ASN A  156  GLY A  169  1                                  14    
-HELIX    8   8 THR A  170  LEU A  173  5                                   4    
-HELIX    9   9 SER A  182  GLY A  197  1                                  16    
-HELIX   10  10 PRO A  209  PHE A  214  1                                   6    
-HELIX   11  11 GLY A  227  GLY A  231  1                                   5    
-HELIX   12  12 GLY A  242  CYS A  247  1                                   6    
-HELIX   13  13 CYS A  247  LEU A  257  1                                  11    
-HELIX   14  14 SER A  260  ASN A  273  1                                  14    
-HELIX   15  15 ASP A  277  ASN A  289  1                                  13    
-HELIX   16  16 SER A  292  LEU A  297  1                                   6    
-HELIX   17  17 ASP A  307  LEU A  316  1                                  10    
-HELIX   18  18 PRO B   30  CYS B   33  5                                   4    
-HELIX   19  19 TRP B   43  LEU B   60  1                                  18    
-HELIX   20  20 SER B   70  ASN B   80  1                                  11    
-HELIX   21  21 MET B   94  ASP B  104  1                                  11    
-HELIX   22  22 ASN B  124  GLY B  131  1                                   8    
-HELIX   23  23 ASP B  134  LYS B  142  5                                   9    
-HELIX   24  24 ASN B  156  GLY B  169  1                                  14    
-HELIX   25  25 THR B  170  LEU B  173  5                                   4    
-HELIX   26  26 SER B  182  GLY B  197  1                                  16    
-HELIX   27  27 PRO B  209  PHE B  214  1                                   6    
-HELIX   28  28 GLY B  227  GLY B  231  1                                   5    
-HELIX   29  29 GLY B  242  CYS B  247  1                                   6    
-HELIX   30  30 CYS B  247  LEU B  257  1                                  11    
-HELIX   31  31 SER B  260  ASN B  273  1                                  14    
-HELIX   32  32 ASP B  277  ASN B  289  1                                  13    
-HELIX   33  33 SER B  292  SER B  298  1                                   7    
-HELIX   34  34 ASP B  307  LEU B  316  1                                  10    
-SHEET    1   A 2 THR A  35  ASP A  40  0                                        
-SHEET    2   A 2 GLU A  63  VAL A  68  1  O  LYS A  67   N  PHE A  38           
-SHEET    1   B 4 VAL A  85  MET A  91  0                                        
-SHEET    2   B 4 GLY A 232  ARG A 240 -1  O  ASN A 238   N  PHE A  86           
-SHEET    3   B 4 VAL A 107  THR A 123 -1  N  GLU A 108   O  VAL A 239           
-SHEET    4   B 4 VAL A 201  GLU A 206 -1  O  PHE A 202   N  ALA A 122           
-SHEET    1   C 4 VAL A  85  MET A  91  0                                        
-SHEET    2   C 4 GLY A 232  ARG A 240 -1  O  ASN A 238   N  PHE A  86           
-SHEET    3   C 4 VAL A 107  THR A 123 -1  N  GLU A 108   O  VAL A 239           
-SHEET    4   C 4 THR A 217  TYR A 218 -1  O  THR A 217   N  THR A 123           
-SHEET    1   D 2 LYS A 148  TYR A 150  0                                        
-SHEET    2   D 2 GLU A 177  VAL A 179  1  O  VAL A 179   N  ILE A 149           
-SHEET    1   E 6 GLU B  63  VAL B  68  0                                        
-SHEET    2   E 6 THR B  35  ASP B  40  1  N  PHE B  38   O  ASP B  65           
-SHEET    3   E 6 VAL B  85  MET B  91  1  O  VAL B  85   N  ARG B  37           
-SHEET    4   E 6 GLY B 232  VAL B 239 -1  O  ASN B 238   N  PHE B  86           
-SHEET    5   E 6 GLU B 108  THR B 123 -1  N  ARG B 111   O  THR B 237           
-SHEET    6   E 6 VAL B 201  GLU B 206 -1  O  PHE B 202   N  ALA B 122           
-SHEET    1   F 6 GLU B  63  VAL B  68  0                                        
-SHEET    2   F 6 THR B  35  ASP B  40  1  N  PHE B  38   O  ASP B  65           
-SHEET    3   F 6 VAL B  85  MET B  91  1  O  VAL B  85   N  ARG B  37           
-SHEET    4   F 6 GLY B 232  VAL B 239 -1  O  ASN B 238   N  PHE B  86           
-SHEET    5   F 6 GLU B 108  THR B 123 -1  N  ARG B 111   O  THR B 237           
-SHEET    6   F 6 THR B 217  TYR B 218 -1  O  THR B 217   N  THR B 123           
-SHEET    1   G 2 LYS B 148  TYR B 150  0                                        
-SHEET    2   G 2 GLU B 177  VAL B 179  1  O  VAL B 179   N  ILE B 149           
-SSBOND   1 CYS A   33    CYS A  247                          1555   1555  2.03  
-SSBOND   2 CYS B   33    CYS B  247                          1555   1555  2.03  
-CISPEP   1 MET A   91    PRO A   92          0        14.08                     
-CISPEP   2 GLU A  206    PRO A  207          0         1.00                     
-CISPEP   3 VAL B   41    GLY B   42          0         1.87                     
-CISPEP   4 MET B   91    PRO B   92          0        12.46                     
-CISPEP   5 GLU B  206    PRO B  207          0         1.77                     
-CISPEP   6 ALA B  241    GLY B  242          0        -3.70                     
-SITE     1 AC1  8 TRP A  43  ASP A  45  TRP A  90  TYR A 119                    
-SITE     2 AC1  8 ILE A 152  ASN A 156  ASP A 157  TRP A 205                    
-SITE     1 AC2  8 TRP B  43  ASP B  45  TRP B  90  TYR B 119                    
-SITE     2 AC2  8 ILE B 152  ASN B 156  ASP B 157  TRP B 205                    
-CRYST1   30.796  185.414   42.529  90.00  91.83  90.00 P 1 21 1      4          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.032472  0.000000  0.001037        0.00000                         
-SCALE2      0.000000  0.005393  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.023525        0.00000                         
-ATOM      1  N   GLU A  29      21.640 -26.553  22.328  1.00 34.37           N  
-ATOM      2  CA  GLU A  29      22.407 -25.635  21.435  1.00 34.24           C  
-ATOM      3  C   GLU A  29      23.906 -25.675  21.758  1.00 34.18           C  
-ATOM      4  O   GLU A  29      24.290 -25.622  22.928  1.00 34.25           O  
-ATOM      5  CB  GLU A  29      21.853 -24.210  21.534  1.00 34.35           C  
-ATOM      6  CG  GLU A  29      20.443 -24.057  20.972  1.00 34.14           C  
-ATOM      7  CD  GLU A  29      19.910 -22.639  21.070  1.00 34.02           C  
-ATOM      8  OE1 GLU A  29      20.107 -21.990  22.119  1.00 33.91           O  
-ATOM      9  OE2 GLU A  29      19.283 -22.173  20.098  1.00 33.60           O  
-ATOM     10  N   PRO A  30      24.745 -25.767  20.721  1.00 34.10           N  
-ATOM     11  CA  PRO A  30      26.178 -26.033  20.889  1.00 33.91           C  
-ATOM     12  C   PRO A  30      27.037 -24.834  21.311  1.00 33.65           C  
-ATOM     13  O   PRO A  30      27.881 -24.373  20.535  1.00 34.02           O  
-ATOM     14  CB  PRO A  30      26.598 -26.542  19.503  1.00 34.10           C  
-ATOM     15  CG  PRO A  30      25.655 -25.870  18.548  1.00 34.10           C  
-ATOM     16  CD  PRO A  30      24.374 -25.641  19.299  1.00 34.04           C  
-ATOM     17  N   GLU A  31      26.812 -24.350  22.535  1.00 32.93           N  
-ATOM     18  CA  GLU A  31      27.674 -23.363  23.219  1.00 32.11           C  
-ATOM     19  C   GLU A  31      27.804 -21.974  22.578  1.00 31.21           C  
-ATOM     20  O   GLU A  31      27.713 -20.965  23.281  1.00 31.23           O  
-ATOM     21  CB  GLU A  31      29.062 -23.960  23.520  1.00 32.34           C  
-ATOM     22  CG  GLU A  31      29.866 -23.214  24.583  1.00 33.25           C  
-ATOM     23  CD  GLU A  31      29.199 -23.196  25.953  1.00 34.30           C  
-ATOM     24  OE1 GLU A  31      28.427 -24.129  26.269  1.00 34.87           O  
-ATOM     25  OE2 GLU A  31      29.451 -22.242  26.722  1.00 34.60           O  
-ATOM     26  N   SER A  32      28.027 -21.921  21.265  1.00 29.96           N  
-ATOM     27  CA  SER A  32      28.159 -20.648  20.548  1.00 28.80           C  
-ATOM     28  C   SER A  32      26.861 -19.840  20.590  1.00 27.69           C  
-ATOM     29  O   SER A  32      26.879 -18.609  20.498  1.00 27.52           O  
-ATOM     30  CB  SER A  32      28.579 -20.887  19.092  1.00 29.07           C  
-ATOM     31  OG  SER A  32      27.526 -21.463  18.333  1.00 29.26           O  
-ATOM     32  N   CYS A  33      25.746 -20.551  20.741  1.00 26.21           N  
-ATOM     33  CA  CYS A  33      24.409 -19.959  20.744  1.00 24.87           C  
-ATOM     34  C   CYS A  33      24.103 -19.127  21.990  1.00 24.18           C  
-ATOM     35  O   CYS A  33      23.147 -18.345  21.996  1.00 24.15           O  
-ATOM     36  CB  CYS A  33      23.359 -21.060  20.597  1.00 24.68           C  
-ATOM     37  SG  CYS A  33      23.518 -22.022  19.079  1.00 23.49           S  
-ATOM     38  N   GLY A  34      24.909 -19.308  23.037  1.00 23.32           N  
-ATOM     39  CA  GLY A  34      24.725 -18.616  24.314  1.00 22.35           C  
-ATOM     40  C   GLY A  34      24.859 -17.106  24.229  1.00 21.72           C  
-ATOM     41  O   GLY A  34      24.335 -16.384  25.080  1.00 21.68           O  
-ATOM     42  N   THR A  35      25.573 -16.639  23.205  1.00 21.03           N  
-ATOM     43  CA  THR A  35      25.690 -15.217  22.904  1.00 20.29           C  
-ATOM     44  C   THR A  35      25.232 -14.951  21.470  1.00 19.81           C  
-ATOM     45  O   THR A  35      25.822 -15.461  20.514  1.00 19.88           O  
-ATOM     46  CB  THR A  35      27.140 -14.717  23.132  1.00 20.40           C  
-ATOM     47  OG1 THR A  35      27.477 -14.841  24.519  1.00 20.48           O  
-ATOM     48  CG2 THR A  35      27.236 -13.211  22.899  1.00 20.10           C  
-ATOM     49  N   VAL A  36      24.174 -14.153  21.336  1.00 18.89           N  
-ATOM     50  CA  VAL A  36      23.605 -13.817  20.033  1.00 18.02           C  
-ATOM     51  C   VAL A  36      24.092 -12.431  19.583  1.00 17.64           C  
-ATOM     52  O   VAL A  36      23.851 -11.426  20.257  1.00 17.77           O  
-ATOM     53  CB  VAL A  36      22.054 -13.868  20.055  1.00 18.13           C  
-ATOM     54  CG1 VAL A  36      21.490 -13.720  18.649  1.00 17.97           C  
-ATOM     55  CG2 VAL A  36      21.557 -15.171  20.684  1.00 17.64           C  
-ATOM     56  N   ARG A  37      24.777 -12.389  18.443  1.00 16.97           N  
-ATOM     57  CA  ARG A  37      25.349 -11.148  17.923  1.00 16.40           C  
-ATOM     58  C   ARG A  37      24.427 -10.495  16.894  1.00 15.84           C  
-ATOM     59  O   ARG A  37      24.071 -11.117  15.893  1.00 15.61           O  
-ATOM     60  CB  ARG A  37      26.725 -11.404  17.300  1.00 16.30           C  
-ATOM     61  CG  ARG A  37      27.821 -11.813  18.278  1.00 16.94           C  
-ATOM     62  CD  ARG A  37      29.025 -12.488  17.611  1.00 17.12           C  
-ATOM     63  NE  ARG A  37      28.599 -13.544  16.687  1.00 19.04           N  
-ATOM     64  CZ  ARG A  37      29.413 -14.341  16.000  1.00 19.56           C  
-ATOM     65  NH1 ARG A  37      30.731 -14.237  16.121  1.00 20.29           N  
-ATOM     66  NH2 ARG A  37      28.901 -15.256  15.189  1.00 19.73           N  
-ATOM     67  N   PHE A  38      24.056  -9.240  17.158  1.00 15.47           N  
-ATOM     68  CA  PHE A  38      23.216  -8.436  16.276  1.00 15.25           C  
-ATOM     69  C   PHE A  38      24.015  -7.312  15.627  1.00 15.48           C  
-ATOM     70  O   PHE A  38      25.019  -6.847  16.178  1.00 15.45           O  
-ATOM     71  CB  PHE A  38      22.083  -7.766  17.065  1.00 15.03           C  
-ATOM     72  CG  PHE A  38      21.023  -8.706  17.555  1.00 14.28           C  
-ATOM     73  CD1 PHE A  38      21.203  -9.428  18.735  1.00 14.04           C  
-ATOM     74  CD2 PHE A  38      19.823  -8.837  16.864  1.00 13.38           C  
-ATOM     75  CE1 PHE A  38      20.218 -10.288  19.201  1.00 13.56           C  
-ATOM     76  CE2 PHE A  38      18.822  -9.696  17.327  1.00 13.28           C  
-ATOM     77  CZ  PHE A  38      19.022 -10.421  18.497  1.00 14.66           C  
-ATOM     78  N   SER A  39      23.548  -6.866  14.464  1.00 15.52           N  
-ATOM     79  CA  SER A  39      23.981  -5.594  13.909  1.00 15.29           C  
-ATOM     80  C   SER A  39      22.917  -4.533  14.144  1.00 15.34           C  
-ATOM     81  O   SER A  39      21.731  -4.739  13.854  1.00 15.18           O  
-ATOM     82  CB  SER A  39      24.252  -5.699  12.411  1.00 15.07           C  
-ATOM     83  OG  SER A  39      24.402  -4.410  11.852  1.00 14.89           O  
-ATOM     84  N   ASP A  40      23.366  -3.399  14.662  1.00 15.25           N  
-ATOM     85  CA  ASP A  40      22.530  -2.226  14.843  1.00 15.81           C  
-ATOM     86  C   ASP A  40      23.197  -1.095  14.078  1.00 15.68           C  
-ATOM     87  O   ASP A  40      24.256  -0.613  14.476  1.00 15.64           O  
-ATOM     88  CB  ASP A  40      22.432  -1.893  16.332  1.00 15.92           C  
-ATOM     89  CG  ASP A  40      21.603  -0.652  16.619  1.00 16.79           C  
-ATOM     90  OD1 ASP A  40      21.101   0.007  15.681  1.00 17.82           O  
-ATOM     91  OD2 ASP A  40      21.413  -0.255  17.786  1.00 19.39           O  
-ATOM     92  N   VAL A  41      22.581  -0.683  12.973  1.00 15.78           N  
-ATOM     93  CA  VAL A  41      23.169   0.349  12.110  1.00 15.92           C  
-ATOM     94  C   VAL A  41      23.137   1.720  12.785  1.00 16.19           C  
-ATOM     95  O   VAL A  41      23.963   2.596  12.486  1.00 16.57           O  
-ATOM     96  CB  VAL A  41      22.513   0.374  10.703  1.00 15.84           C  
-ATOM     97  CG1 VAL A  41      23.245   1.335   9.780  1.00 15.67           C  
-ATOM     98  CG2 VAL A  41      22.531  -1.022  10.096  1.00 16.11           C  
-ATOM     99  N   GLY A  42      22.202   1.885  13.713  1.00 15.88           N  
-ATOM    100  CA  GLY A  42      22.136   3.082  14.535  1.00 15.70           C  
-ATOM    101  C   GLY A  42      20.886   3.924  14.379  1.00 15.32           C  
-ATOM    102  O   GLY A  42      20.671   4.848  15.172  1.00 15.23           O  
-ATOM    103  N   TRP A  43      20.067   3.630  13.366  1.00 14.72           N  
-ATOM    104  CA  TRP A  43      18.776   4.308  13.227  1.00 14.44           C  
-ATOM    105  C   TRP A  43      17.932   3.984  14.459  1.00 14.06           C  
-ATOM    106  O   TRP A  43      18.069   2.906  15.035  1.00 14.14           O  
-ATOM    107  CB  TRP A  43      18.013   3.876  11.963  1.00 14.50           C  
-ATOM    108  CG  TRP A  43      18.857   3.505  10.769  1.00 14.78           C  
-ATOM    109  CD1 TRP A  43      19.788   4.286  10.137  1.00 14.91           C  
-ATOM    110  CD2 TRP A  43      18.823   2.267  10.053  1.00 14.20           C  
-ATOM    111  NE1 TRP A  43      20.343   3.600   9.082  1.00 14.90           N  
-ATOM    112  CE2 TRP A  43      19.769   2.358   9.008  1.00 14.43           C  
-ATOM    113  CE3 TRP A  43      18.084   1.081  10.186  1.00 14.13           C  
-ATOM    114  CZ2 TRP A  43      19.995   1.308   8.105  1.00 14.63           C  
-ATOM    115  CZ3 TRP A  43      18.314   0.039   9.297  1.00 14.56           C  
-ATOM    116  CH2 TRP A  43      19.260   0.162   8.266  1.00 14.58           C  
-ATOM    117  N   THR A  44      17.062   4.907  14.857  1.00 13.58           N  
-ATOM    118  CA  THR A  44      16.229   4.697  16.050  1.00 13.07           C  
-ATOM    119  C   THR A  44      15.366   3.431  15.946  1.00 12.89           C  
-ATOM    120  O   THR A  44      15.203   2.719  16.929  1.00 12.25           O  
-ATOM    121  CB  THR A  44      15.358   5.934  16.326  1.00 13.11           C  
-ATOM    122  OG1 THR A  44      16.191   7.100  16.371  1.00 12.54           O  
-ATOM    123  CG2 THR A  44      14.740   5.865  17.735  1.00 13.56           C  
-ATOM    124  N   ASP A  45      14.834   3.144  14.756  1.00 12.67           N  
-ATOM    125  CA  ASP A  45      13.958   1.979  14.592  1.00 12.87           C  
-ATOM    126  C   ASP A  45      14.693   0.650  14.775  1.00 13.06           C  
-ATOM    127  O   ASP A  45      14.203  -0.233  15.477  1.00 13.06           O  
-ATOM    128  CB  ASP A  45      13.188   2.019  13.260  1.00 13.01           C  
-ATOM    129  CG  ASP A  45      14.059   1.705  12.059  1.00 13.25           C  
-ATOM    130  OD1 ASP A  45      15.134   2.341  11.907  1.00 14.05           O  
-ATOM    131  OD2 ASP A  45      13.732   0.849  11.201  1.00 13.00           O  
-ATOM    132  N   ILE A  46      15.868   0.512  14.158  1.00 13.12           N  
-ATOM    133  CA  ILE A  46      16.648  -0.722  14.301  1.00 13.55           C  
-ATOM    134  C   ILE A  46      17.199  -0.860  15.723  1.00 13.70           C  
-ATOM    135  O   ILE A  46      17.346  -1.969  16.223  1.00 13.30           O  
-ATOM    136  CB  ILE A  46      17.763  -0.847  13.206  1.00 13.63           C  
-ATOM    137  CG1 ILE A  46      18.452  -2.215  13.258  1.00 13.94           C  
-ATOM    138  CG2 ILE A  46      18.797   0.261  13.335  1.00 14.03           C  
-ATOM    139  CD1 ILE A  46      17.523  -3.407  13.070  1.00 13.44           C  
-ATOM    140  N   THR A  47      17.474   0.267  16.384  1.00 14.15           N  
-ATOM    141  CA  THR A  47      17.887   0.227  17.788  1.00 14.72           C  
-ATOM    142  C   THR A  47      16.727  -0.263  18.660  1.00 14.48           C  
-ATOM    143  O   THR A  47      16.931  -1.016  19.615  1.00 14.70           O  
-ATOM    144  CB  THR A  47      18.408   1.604  18.247  1.00 14.88           C  
-ATOM    145  OG1 THR A  47      19.530   1.978  17.436  1.00 15.66           O  
-ATOM    146  CG2 THR A  47      19.022   1.523  19.646  1.00 16.13           C  
-ATOM    147  N   ALA A  48      15.515   0.167  18.315  1.00 14.28           N  
-ATOM    148  CA  ALA A  48      14.303  -0.202  19.046  1.00 14.12           C  
-ATOM    149  C   ALA A  48      13.950  -1.678  18.886  1.00 13.83           C  
-ATOM    150  O   ALA A  48      13.683  -2.357  19.877  1.00 13.54           O  
-ATOM    151  CB  ALA A  48      13.129   0.678  18.618  1.00 14.05           C  
-ATOM    152  N   THR A  49      13.951  -2.172  17.648  1.00 13.66           N  
-ATOM    153  CA  THR A  49      13.629  -3.581  17.402  1.00 13.40           C  
-ATOM    154  C   THR A  49      14.694  -4.504  17.988  1.00 13.28           C  
-ATOM    155  O   THR A  49      14.371  -5.555  18.535  1.00 13.49           O  
-ATOM    156  CB  THR A  49      13.441  -3.883  15.900  1.00 13.46           C  
-ATOM    157  OG1 THR A  49      14.556  -3.379  15.153  1.00 13.38           O  
-ATOM    158  CG2 THR A  49      12.238  -3.145  15.346  1.00 13.62           C  
-ATOM    159  N   THR A  50      15.955  -4.099  17.875  1.00 13.35           N  
-ATOM    160  CA  THR A  50      17.071  -4.867  18.426  1.00 13.41           C  
-ATOM    161  C   THR A  50      17.010  -4.928  19.954  1.00 13.87           C  
-ATOM    162  O   THR A  50      17.235  -5.984  20.541  1.00 13.92           O  
-ATOM    163  CB  THR A  50      18.428  -4.289  17.936  1.00 13.57           C  
-ATOM    164  OG1 THR A  50      18.471  -4.324  16.503  1.00 12.93           O  
-ATOM    165  CG2 THR A  50      19.590  -5.195  18.337  1.00 12.85           C  
-ATOM    166  N   ALA A  51      16.699  -3.795  20.585  1.00 14.36           N  
-ATOM    167  CA  ALA A  51      16.560  -3.714  22.047  1.00 14.62           C  
-ATOM    168  C   ALA A  51      15.424  -4.594  22.559  1.00 14.92           C  
-ATOM    169  O   ALA A  51      15.515  -5.158  23.649  1.00 15.11           O  
-ATOM    170  CB  ALA A  51      16.346  -2.271  22.485  1.00 14.56           C  
-ATOM    171  N   THR A  52      14.356  -4.689  21.767  1.00 15.22           N  
-ATOM    172  CA  THR A  52      13.231  -5.585  22.049  1.00 15.32           C  
-ATOM    173  C   THR A  52      13.690  -7.042  22.021  1.00 15.10           C  
-ATOM    174  O   THR A  52      13.384  -7.804  22.928  1.00 14.66           O  
-ATOM    175  CB  THR A  52      12.086  -5.353  21.033  1.00 15.24           C  
-ATOM    176  OG1 THR A  52      11.601  -4.010  21.147  1.00 16.32           O  
-ATOM    177  CG2 THR A  52      10.859  -6.192  21.380  1.00 15.31           C  
-ATOM    178  N   ALA A  53      14.436  -7.412  20.981  1.00 14.92           N  
-ATOM    179  CA  ALA A  53      14.986  -8.762  20.854  1.00 14.78           C  
-ATOM    180  C   ALA A  53      15.953  -9.110  21.984  1.00 14.72           C  
-ATOM    181  O   ALA A  53      15.851 -10.195  22.567  1.00 14.83           O  
-ATOM    182  CB  ALA A  53      15.666  -8.942  19.492  1.00 14.89           C  
-ATOM    183  N   THR A  54      16.879  -8.197  22.295  1.00 14.69           N  
-ATOM    184  CA  THR A  54      17.876  -8.444  23.341  1.00 14.54           C  
-ATOM    185  C   THR A  54      17.243  -8.518  24.731  1.00 14.75           C  
-ATOM    186  O   THR A  54      17.696  -9.292  25.572  1.00 14.49           O  
-ATOM    187  CB  THR A  54      19.043  -7.406  23.327  1.00 14.55           C  
-ATOM    188  OG1 THR A  54      18.532  -6.085  23.522  1.00 13.96           O  
-ATOM    189  CG2 THR A  54      19.721  -7.340  21.961  1.00 14.28           C  
-ATOM    190  N   THR A  55      16.200  -7.720  24.960  1.00 14.77           N  
-ATOM    191  CA  THR A  55      15.431  -7.785  26.206  1.00 14.91           C  
-ATOM    192  C   THR A  55      14.840  -9.181  26.412  1.00 15.04           C  
-ATOM    193  O   THR A  55      14.961  -9.762  27.495  1.00 14.83           O  
-ATOM    194  CB  THR A  55      14.308  -6.724  26.216  1.00 15.00           C  
-ATOM    195  OG1 THR A  55      14.892  -5.418  26.251  1.00 14.96           O  
-ATOM    196  CG2 THR A  55      13.517  -6.781  27.524  1.00 15.45           C  
-ATOM    197  N   ILE A  56      14.208  -9.712  25.367  1.00 15.02           N  
-ATOM    198  CA  ILE A  56      13.593 -11.039  25.435  1.00 15.24           C  
-ATOM    199  C   ILE A  56      14.659 -12.120  25.584  1.00 15.53           C  
-ATOM    200  O   ILE A  56      14.520 -13.029  26.407  1.00 15.13           O  
-ATOM    201  CB  ILE A  56      12.694 -11.312  24.200  1.00 15.43           C  
-ATOM    202  CG1 ILE A  56      11.496 -10.352  24.200  1.00 16.07           C  
-ATOM    203  CG2 ILE A  56      12.231 -12.785  24.184  1.00 14.44           C  
-ATOM    204  CD1 ILE A  56      10.749 -10.268  22.889  1.00 18.21           C  
-ATOM    205  N   LEU A  57      15.720 -12.009  24.786  1.00 16.05           N  
-ATOM    206  CA  LEU A  57      16.799 -12.996  24.795  1.00 16.59           C  
-ATOM    207  C   LEU A  57      17.512 -13.088  26.137  1.00 16.95           C  
-ATOM    208  O   LEU A  57      17.792 -14.187  26.610  1.00 17.17           O  
-ATOM    209  CB  LEU A  57      17.798 -12.729  23.668  1.00 16.47           C  
-ATOM    210  CG  LEU A  57      17.400 -13.273  22.296  1.00 16.51           C  
-ATOM    211  CD1 LEU A  57      18.336 -12.717  21.228  1.00 15.91           C  
-ATOM    212  CD2 LEU A  57      17.404 -14.800  22.275  1.00 16.37           C  
-ATOM    213  N   GLU A  58      17.794 -11.939  26.749  1.00 17.41           N  
-ATOM    214  CA  GLU A  58      18.422 -11.918  28.076  1.00 17.97           C  
-ATOM    215  C   GLU A  58      17.476 -12.426  29.167  1.00 17.70           C  
-ATOM    216  O   GLU A  58      17.921 -13.025  30.149  1.00 17.56           O  
-ATOM    217  CB  GLU A  58      18.980 -10.530  28.411  1.00 18.03           C  
-ATOM    218  CG  GLU A  58      20.215 -10.155  27.592  1.00 18.86           C  
-ATOM    219  CD  GLU A  58      20.536  -8.669  27.622  1.00 19.40           C  
-ATOM    220  OE1 GLU A  58      19.937  -7.927  28.436  1.00 21.66           O  
-ATOM    221  OE2 GLU A  58      21.394  -8.237  26.821  1.00 20.87           O  
-ATOM    222  N   ALA A  59      16.176 -12.210  28.980  1.00 17.58           N  
-ATOM    223  CA  ALA A  59      15.159 -12.803  29.849  1.00 17.59           C  
-ATOM    224  C   ALA A  59      15.154 -14.327  29.705  1.00 17.63           C  
-ATOM    225  O   ALA A  59      14.805 -15.048  30.639  1.00 17.61           O  
-ATOM    226  CB  ALA A  59      13.787 -12.232  29.531  1.00 17.65           C  
-ATOM    227  N   LEU A  60      15.559 -14.803  28.531  1.00 17.63           N  
-ATOM    228  CA  LEU A  60      15.620 -16.231  28.239  1.00 17.69           C  
-ATOM    229  C   LEU A  60      16.926 -16.889  28.691  1.00 18.00           C  
-ATOM    230  O   LEU A  60      17.103 -18.098  28.537  1.00 18.18           O  
-ATOM    231  CB  LEU A  60      15.391 -16.478  26.744  1.00 17.48           C  
-ATOM    232  CG  LEU A  60      13.975 -16.250  26.205  1.00 16.77           C  
-ATOM    233  CD1 LEU A  60      13.979 -16.284  24.697  1.00 15.82           C  
-ATOM    234  CD2 LEU A  60      13.007 -17.284  26.771  1.00 16.23           C  
-ATOM    235  N   GLY A  61      17.836 -16.096  29.247  1.00 18.24           N  
-ATOM    236  CA  GLY A  61      19.110 -16.620  29.730  1.00 18.41           C  
-ATOM    237  C   GLY A  61      20.255 -16.509  28.740  1.00 18.60           C  
-ATOM    238  O   GLY A  61      21.352 -17.011  29.001  1.00 18.61           O  
-ATOM    239  N   TYR A  62      20.006 -15.854  27.607  1.00 18.60           N  
-ATOM    240  CA  TYR A  62      21.042 -15.619  26.600  1.00 18.67           C  
-ATOM    241  C   TYR A  62      21.780 -14.312  26.861  1.00 18.84           C  
-ATOM    242  O   TYR A  62      21.225 -13.376  27.437  1.00 19.05           O  
-ATOM    243  CB  TYR A  62      20.440 -15.564  25.191  1.00 18.42           C  
-ATOM    244  CG  TYR A  62      19.870 -16.868  24.685  1.00 18.38           C  
-ATOM    245  CD1 TYR A  62      18.546 -17.224  24.950  1.00 18.25           C  
-ATOM    246  CD2 TYR A  62      20.647 -17.739  23.926  1.00 18.57           C  
-ATOM    247  CE1 TYR A  62      18.017 -18.423  24.483  1.00 18.36           C  
-ATOM    248  CE2 TYR A  62      20.129 -18.944  23.454  1.00 18.33           C  
-ATOM    249  CZ  TYR A  62      18.813 -19.276  23.734  1.00 18.68           C  
-ATOM    250  OH  TYR A  62      18.295 -20.459  23.266  1.00 18.39           O  
-ATOM    251  N   GLU A  63      23.035 -14.255  26.435  1.00 18.84           N  
-ATOM    252  CA  GLU A  63      23.750 -12.991  26.371  1.00 18.83           C  
-ATOM    253  C   GLU A  63      23.599 -12.456  24.952  1.00 18.77           C  
-ATOM    254  O   GLU A  63      23.344 -13.217  24.013  1.00 18.82           O  
-ATOM    255  CB  GLU A  63      25.228 -13.166  26.732  1.00 18.75           C  
-ATOM    256  CG  GLU A  63      25.500 -13.867  28.063  1.00 19.45           C  
-ATOM    257  CD  GLU A  63      25.158 -13.031  29.291  1.00 20.24           C  
-ATOM    258  OE1 GLU A  63      25.132 -11.786  29.204  1.00 21.01           O  
-ATOM    259  OE2 GLU A  63      24.918 -13.629  30.362  1.00 21.97           O  
-ATOM    260  N   THR A  64      23.719 -11.144  24.800  1.00 18.81           N  
-ATOM    261  CA  THR A  64      23.684 -10.528  23.478  1.00 18.67           C  
-ATOM    262  C   THR A  64      24.869  -9.590  23.309  1.00 18.56           C  
-ATOM    263  O   THR A  64      25.419  -9.069  24.286  1.00 18.44           O  
-ATOM    264  CB  THR A  64      22.355  -9.762  23.223  1.00 18.54           C  
-ATOM    265  OG1 THR A  64      22.176  -8.752  24.223  1.00 19.42           O  
-ATOM    266  CG2 THR A  64      21.136 -10.672  23.396  1.00 18.96           C  
-ATOM    267  N   ASP A  65      25.265  -9.396  22.058  1.00 18.54           N  
-ATOM    268  CA  ASP A  65      26.293  -8.436  21.712  1.00 18.82           C  
-ATOM    269  C   ASP A  65      25.804  -7.698  20.482  1.00 18.58           C  
-ATOM    270  O   ASP A  65      25.577  -8.300  19.433  1.00 18.80           O  
-ATOM    271  CB  ASP A  65      27.635  -9.132  21.448  1.00 19.04           C  
-ATOM    272  CG  ASP A  65      28.761  -8.150  21.155  1.00 20.08           C  
-ATOM    273  OD1 ASP A  65      28.674  -6.977  21.578  1.00 21.39           O  
-ATOM    274  OD2 ASP A  65      29.776  -8.465  20.503  1.00 21.83           O  
-ATOM    275  N   VAL A  66      25.606  -6.396  20.634  1.00 18.38           N  
-ATOM    276  CA  VAL A  66      25.094  -5.568  19.552  1.00 18.22           C  
-ATOM    277  C   VAL A  66      26.238  -4.742  18.977  1.00 18.12           C  
-ATOM    278  O   VAL A  66      26.834  -3.921  19.674  1.00 18.04           O  
-ATOM    279  CB  VAL A  66      23.939  -4.661  20.039  1.00 18.28           C  
-ATOM    280  CG1 VAL A  66      23.432  -3.789  18.910  1.00 17.92           C  
-ATOM    281  CG2 VAL A  66      22.800  -5.505  20.603  1.00 17.75           C  
-ATOM    282  N   LYS A  67      26.550  -4.980  17.709  1.00 17.66           N  
-ATOM    283  CA  LYS A  67      27.618  -4.247  17.039  1.00 17.71           C  
-ATOM    284  C   LYS A  67      27.036  -3.149  16.161  1.00 17.02           C  
-ATOM    285  O   LYS A  67      26.090  -3.381  15.413  1.00 17.48           O  
-ATOM    286  CB  LYS A  67      28.480  -5.189  16.195  1.00 17.90           C  
-ATOM    287  CG  LYS A  67      29.324  -6.168  17.003  1.00 19.91           C  
-ATOM    288  CD  LYS A  67      30.668  -6.410  16.322  1.00 22.29           C  
-ATOM    289  CE  LYS A  67      30.611  -7.533  15.297  1.00 23.20           C  
-ATOM    290  NZ  LYS A  67      31.048  -8.848  15.869  1.00 23.19           N  
-ATOM    291  N   VAL A  68      27.597  -1.951  16.267  1.00 16.55           N  
-ATOM    292  CA  VAL A  68      27.228  -0.858  15.372  1.00 15.71           C  
-ATOM    293  C   VAL A  68      28.039  -1.010  14.086  1.00 15.36           C  
-ATOM    294  O   VAL A  68      29.271  -0.930  14.101  1.00 15.45           O  
-ATOM    295  CB  VAL A  68      27.422   0.533  16.030  1.00 15.67           C  
-ATOM    296  CG1 VAL A  68      27.021   1.655  15.081  1.00 15.33           C  
-ATOM    297  CG2 VAL A  68      26.613   0.626  17.329  1.00 15.92           C  
-ATOM    298  N   LEU A  69      27.329  -1.260  12.989  1.00 14.54           N  
-ATOM    299  CA  LEU A  69      27.934  -1.542  11.687  1.00 14.16           C  
-ATOM    300  C   LEU A  69      27.149  -0.856  10.582  1.00 13.98           C  
-ATOM    301  O   LEU A  69      25.941  -0.645  10.722  1.00 14.35           O  
-ATOM    302  CB  LEU A  69      27.925  -3.053  11.418  1.00 14.08           C  
-ATOM    303  CG  LEU A  69      28.550  -3.989  12.459  1.00 13.94           C  
-ATOM    304  CD1 LEU A  69      28.202  -5.449  12.169  1.00 13.67           C  
-ATOM    305  CD2 LEU A  69      30.064  -3.792  12.525  1.00 14.14           C  
-ATOM    306  N   SER A  70      27.825  -0.534   9.478  1.00 13.32           N  
-ATOM    307  CA  SER A  70      27.148  -0.005   8.296  1.00 12.63           C  
-ATOM    308  C   SER A  70      26.301  -1.090   7.626  1.00 12.90           C  
-ATOM    309  O   SER A  70      26.418  -2.279   7.950  1.00 12.34           O  
-ATOM    310  CB  SER A  70      28.161   0.558   7.296  1.00 12.66           C  
-ATOM    311  OG  SER A  70      28.895  -0.484   6.668  1.00 11.14           O  
-ATOM    312  N   VAL A  71      25.439  -0.677   6.700  1.00 12.94           N  
-ATOM    313  CA  VAL A  71      24.625  -1.631   5.945  1.00 12.59           C  
-ATOM    314  C   VAL A  71      25.487  -2.658   5.169  1.00 12.29           C  
-ATOM    315  O   VAL A  71      25.267  -3.857   5.315  1.00 12.48           O  
-ATOM    316  CB  VAL A  71      23.553  -0.929   5.058  1.00 12.77           C  
-ATOM    317  CG1 VAL A  71      22.871  -1.931   4.118  1.00 12.92           C  
-ATOM    318  CG2 VAL A  71      22.508  -0.256   5.936  1.00 12.54           C  
-ATOM    319  N   PRO A  72      26.468  -2.214   4.374  1.00 12.21           N  
-ATOM    320  CA  PRO A  72      27.350  -3.162   3.674  1.00 11.89           C  
-ATOM    321  C   PRO A  72      28.140  -4.074   4.624  1.00 11.56           C  
-ATOM    322  O   PRO A  72      28.221  -5.281   4.389  1.00 11.24           O  
-ATOM    323  CB  PRO A  72      28.301  -2.251   2.885  1.00 11.96           C  
-ATOM    324  CG  PRO A  72      27.561  -0.962   2.752  1.00 12.50           C  
-ATOM    325  CD  PRO A  72      26.803  -0.814   4.040  1.00 11.80           C  
-ATOM    326  N   VAL A  73      28.697  -3.504   5.693  1.00 11.37           N  
-ATOM    327  CA  VAL A  73      29.449  -4.300   6.674  1.00 11.06           C  
-ATOM    328  C   VAL A  73      28.546  -5.331   7.370  1.00 11.17           C  
-ATOM    329  O   VAL A  73      28.978  -6.444   7.662  1.00 11.27           O  
-ATOM    330  CB  VAL A  73      30.202  -3.404   7.697  1.00 11.16           C  
-ATOM    331  CG1 VAL A  73      30.884  -4.240   8.768  1.00 10.18           C  
-ATOM    332  CG2 VAL A  73      31.236  -2.537   6.973  1.00 10.43           C  
-ATOM    333  N   THR A  74      27.290  -4.970   7.612  1.00 11.06           N  
-ATOM    334  CA  THR A  74      26.325  -5.914   8.180  1.00 10.85           C  
-ATOM    335  C   THR A  74      26.284  -7.228   7.381  1.00 10.77           C  
-ATOM    336  O   THR A  74      26.376  -8.315   7.960  1.00 10.47           O  
-ATOM    337  CB  THR A  74      24.917  -5.266   8.279  1.00 11.22           C  
-ATOM    338  OG1 THR A  74      24.919  -4.266   9.309  1.00 11.14           O  
-ATOM    339  CG2 THR A  74      23.899  -6.271   8.779  1.00 10.78           C  
-ATOM    340  N   TYR A  75      26.177  -7.125   6.058  1.00 10.51           N  
-ATOM    341  CA  TYR A  75      26.083  -8.316   5.218  1.00 10.75           C  
-ATOM    342  C   TYR A  75      27.400  -9.074   5.098  1.00 10.83           C  
-ATOM    343  O   TYR A  75      27.418 -10.310   5.081  1.00 10.32           O  
-ATOM    344  CB  TYR A  75      25.448  -7.979   3.867  1.00 11.01           C  
-ATOM    345  CG  TYR A  75      23.982  -7.697   4.064  1.00 11.23           C  
-ATOM    346  CD1 TYR A  75      23.489  -6.393   4.056  1.00 11.79           C  
-ATOM    347  CD2 TYR A  75      23.094  -8.738   4.332  1.00 11.81           C  
-ATOM    348  CE1 TYR A  75      22.137  -6.138   4.282  1.00 11.69           C  
-ATOM    349  CE2 TYR A  75      21.746  -8.494   4.557  1.00 11.48           C  
-ATOM    350  CZ  TYR A  75      21.275  -7.200   4.529  1.00 11.59           C  
-ATOM    351  OH  TYR A  75      19.941  -6.971   4.754  1.00 11.70           O  
-ATOM    352  N   THR A  76      28.496  -8.321   5.048  1.00 10.78           N  
-ATOM    353  CA  THR A  76      29.831  -8.896   5.081  1.00 11.23           C  
-ATOM    354  C   THR A  76      30.036  -9.705   6.364  1.00 11.19           C  
-ATOM    355  O   THR A  76      30.592 -10.810   6.328  1.00 11.45           O  
-ATOM    356  CB  THR A  76      30.880  -7.776   4.959  1.00 11.32           C  
-ATOM    357  OG1 THR A  76      30.730  -7.128   3.686  1.00 11.82           O  
-ATOM    358  CG2 THR A  76      32.287  -8.355   4.893  1.00 11.95           C  
-ATOM    359  N   SER A  77      29.571  -9.155   7.488  1.00 11.21           N  
-ATOM    360  CA  SER A  77      29.749  -9.773   8.805  1.00 11.40           C  
-ATOM    361  C   SER A  77      28.907 -11.028   8.983  1.00 11.93           C  
-ATOM    362  O   SER A  77      29.362 -12.001   9.590  1.00 12.05           O  
-ATOM    363  CB  SER A  77      29.440  -8.769   9.916  1.00 11.29           C  
-ATOM    364  OG  SER A  77      30.313  -7.653   9.847  1.00 11.19           O  
-ATOM    365  N   LEU A  78      27.679 -11.000   8.467  1.00 12.23           N  
-ATOM    366  CA  LEU A  78      26.830 -12.192   8.442  1.00 12.94           C  
-ATOM    367  C   LEU A  78      27.486 -13.301   7.622  1.00 13.42           C  
-ATOM    368  O   LEU A  78      27.560 -14.447   8.073  1.00 13.06           O  
-ATOM    369  CB  LEU A  78      25.439 -11.861   7.893  1.00 12.78           C  
-ATOM    370  CG  LEU A  78      24.478 -11.064   8.784  1.00 13.08           C  
-ATOM    371  CD1 LEU A  78      23.436 -10.341   7.936  1.00 12.89           C  
-ATOM    372  CD2 LEU A  78      23.799 -11.960   9.825  1.00 13.22           C  
-ATOM    373  N   LYS A  79      27.978 -12.955   6.430  1.00 14.05           N  
-ATOM    374  CA  LYS A  79      28.688 -13.922   5.585  1.00 14.63           C  
-ATOM    375  C   LYS A  79      29.906 -14.504   6.315  1.00 14.81           C  
-ATOM    376  O   LYS A  79      30.105 -15.720   6.320  1.00 14.85           O  
-ATOM    377  CB  LYS A  79      29.104 -13.297   4.244  1.00 14.76           C  
-ATOM    378  CG  LYS A  79      29.785 -14.288   3.279  1.00 15.17           C  
-ATOM    379  CD  LYS A  79      30.370 -13.603   2.046  1.00 15.39           C  
-ATOM    380  CE  LYS A  79      30.971 -14.625   1.080  1.00 16.14           C  
-ATOM    381  NZ  LYS A  79      31.837 -13.975   0.049  1.00 17.92           N  
-ATOM    382  N   ASN A  80      30.696 -13.631   6.942  1.00 15.04           N  
-ATOM    383  CA  ASN A  80      31.909 -14.030   7.670  1.00 15.63           C  
-ATOM    384  C   ASN A  80      31.642 -14.705   9.020  1.00 15.60           C  
-ATOM    385  O   ASN A  80      32.579 -15.137   9.698  1.00 15.46           O  
-ATOM    386  CB  ASN A  80      32.827 -12.819   7.884  1.00 15.62           C  
-ATOM    387  CG  ASN A  80      33.527 -12.376   6.613  1.00 16.71           C  
-ATOM    388  OD1 ASN A  80      33.644 -13.138   5.650  1.00 18.17           O  
-ATOM    389  ND2 ASN A  80      34.012 -11.138   6.610  1.00 16.93           N  
-ATOM    390  N   LYS A  81      30.368 -14.787   9.397  1.00 15.68           N  
-ATOM    391  CA  LYS A  81      29.932 -15.359  10.679  1.00 16.16           C  
-ATOM    392  C   LYS A  81      30.378 -14.529  11.890  1.00 16.23           C  
-ATOM    393  O   LYS A  81      30.511 -15.055  12.998  1.00 16.44           O  
-ATOM    394  CB  LYS A  81      30.376 -16.825  10.831  1.00 16.11           C  
-ATOM    395  CG  LYS A  81      29.969 -17.747   9.690  1.00 16.36           C  
-ATOM    396  CD  LYS A  81      30.474 -19.167   9.933  1.00 16.86           C  
-ATOM    397  CE  LYS A  81      30.145 -20.086   8.765  1.00 17.87           C  
-ATOM    398  NZ  LYS A  81      28.678 -20.302   8.622  1.00 18.81           N  
-ATOM    399  N   ASP A  82      30.591 -13.234  11.669  1.00 16.03           N  
-ATOM    400  CA  ASP A  82      30.991 -12.310  12.729  1.00 16.33           C  
-ATOM    401  C   ASP A  82      29.805 -11.738  13.500  1.00 16.23           C  
-ATOM    402  O   ASP A  82      29.971 -11.225  14.608  1.00 16.62           O  
-ATOM    403  CB  ASP A  82      31.863 -11.185  12.167  1.00 16.32           C  
-ATOM    404  CG  ASP A  82      33.237 -11.668  11.768  1.00 16.92           C  
-ATOM    405  OD1 ASP A  82      33.692 -12.685  12.326  1.00 16.89           O  
-ATOM    406  OD2 ASP A  82      33.940 -11.099  10.911  1.00 18.17           O  
-ATOM    407  N   ILE A  83      28.619 -11.825  12.904  1.00 16.05           N  
-ATOM    408  CA  ILE A  83      27.357 -11.555  13.597  1.00 15.83           C  
-ATOM    409  C   ILE A  83      26.332 -12.613  13.181  1.00 15.43           C  
-ATOM    410  O   ILE A  83      26.502 -13.271  12.154  1.00 15.11           O  
-ATOM    411  CB  ILE A  83      26.808 -10.125  13.321  1.00 16.17           C  
-ATOM    412  CG1 ILE A  83      26.538  -9.908  11.825  1.00 16.38           C  
-ATOM    413  CG2 ILE A  83      27.722  -9.047  13.915  1.00 16.32           C  
-ATOM    414  CD1 ILE A  83      25.599  -8.753  11.542  1.00 17.78           C  
-ATOM    415  N   ASP A  84      25.272 -12.764  13.974  1.00 14.92           N  
-ATOM    416  CA  ASP A  84      24.287 -13.826  13.750  1.00 14.59           C  
-ATOM    417  C   ASP A  84      22.984 -13.322  13.137  1.00 14.37           C  
-ATOM    418  O   ASP A  84      22.396 -13.997  12.286  1.00 14.39           O  
-ATOM    419  CB  ASP A  84      23.980 -14.560  15.063  1.00 14.67           C  
-ATOM    420  CG  ASP A  84      25.233 -15.036  15.771  1.00 15.08           C  
-ATOM    421  OD1 ASP A  84      26.004 -15.813  15.167  1.00 15.74           O  
-ATOM    422  OD2 ASP A  84      25.533 -14.669  16.926  1.00 15.52           O  
-ATOM    423  N   VAL A  85      22.538 -12.146  13.580  1.00 13.82           N  
-ATOM    424  CA  VAL A  85      21.189 -11.651  13.277  1.00 13.59           C  
-ATOM    425  C   VAL A  85      21.203 -10.194  12.820  1.00 13.45           C  
-ATOM    426  O   VAL A  85      22.019  -9.397  13.287  1.00 13.57           O  
-ATOM    427  CB  VAL A  85      20.249 -11.764  14.519  1.00 13.52           C  
-ATOM    428  CG1 VAL A  85      18.797 -11.432  14.143  1.00 14.19           C  
-ATOM    429  CG2 VAL A  85      20.319 -13.155  15.146  1.00 13.87           C  
-ATOM    430  N   PHE A  86      20.287  -9.859  11.909  1.00 13.15           N  
-ATOM    431  CA  PHE A  86      20.018  -8.472  11.521  1.00 12.88           C  
-ATOM    432  C   PHE A  86      18.522  -8.296  11.321  1.00 12.58           C  
-ATOM    433  O   PHE A  86      17.924  -8.970  10.483  1.00 12.21           O  
-ATOM    434  CB  PHE A  86      20.780  -8.104  10.235  1.00 12.63           C  
-ATOM    435  CG  PHE A  86      20.572  -6.676   9.773  1.00 12.55           C  
-ATOM    436  CD1 PHE A  86      20.764  -5.602  10.644  1.00 12.03           C  
-ATOM    437  CD2 PHE A  86      20.219  -6.409   8.456  1.00 12.83           C  
-ATOM    438  CE1 PHE A  86      20.589  -4.287  10.216  1.00 12.67           C  
-ATOM    439  CE2 PHE A  86      20.048  -5.095   8.015  1.00 13.20           C  
-ATOM    440  CZ  PHE A  86      20.237  -4.031   8.900  1.00 12.04           C  
-ATOM    441  N   LEU A  87      17.926  -7.380  12.084  1.00 12.60           N  
-ATOM    442  CA  LEU A  87      16.471  -7.148  12.027  1.00 12.42           C  
-ATOM    443  C   LEU A  87      16.067  -6.004  11.101  1.00 12.58           C  
-ATOM    444  O   LEU A  87      14.882  -5.655  11.017  1.00 12.68           O  
-ATOM    445  CB  LEU A  87      15.912  -6.870  13.427  1.00 12.21           C  
-ATOM    446  CG  LEU A  87      16.222  -7.847  14.560  1.00 11.82           C  
-ATOM    447  CD1 LEU A  87      15.629  -7.307  15.849  1.00 12.46           C  
-ATOM    448  CD2 LEU A  87      15.685  -9.256  14.250  1.00 12.06           C  
-ATOM    449  N   GLY A  88      17.040  -5.422  10.405  1.00 12.46           N  
-ATOM    450  CA  GLY A  88      16.804  -4.172   9.687  1.00 12.42           C  
-ATOM    451  C   GLY A  88      16.910  -4.250   8.173  1.00 12.27           C  
-ATOM    452  O   GLY A  88      17.322  -3.279   7.535  1.00 12.16           O  
-ATOM    453  N   ASN A  89      16.546  -5.397   7.603  1.00 11.88           N  
-ATOM    454  CA  ASN A  89      16.547  -5.567   6.144  1.00 11.95           C  
-ATOM    455  C   ASN A  89      15.353  -4.861   5.490  1.00 12.15           C  
-ATOM    456  O   ASN A  89      14.249  -5.412   5.432  1.00 11.97           O  
-ATOM    457  CB  ASN A  89      16.562  -7.059   5.783  1.00 11.73           C  
-ATOM    458  CG  ASN A  89      16.575  -7.312   4.273  1.00 11.89           C  
-ATOM    459  OD1 ASN A  89      17.078  -6.507   3.486  1.00 12.92           O  
-ATOM    460  ND2 ASN A  89      16.022  -8.443   3.872  1.00 11.89           N  
-ATOM    461  N   TRP A  90      15.578  -3.634   5.013  1.00 12.20           N  
-ATOM    462  CA  TRP A  90      14.527  -2.853   4.353  1.00 12.40           C  
-ATOM    463  C   TRP A  90      14.476  -3.200   2.869  1.00 12.75           C  
-ATOM    464  O   TRP A  90      15.493  -3.151   2.174  1.00 13.02           O  
-ATOM    465  CB  TRP A  90      14.727  -1.335   4.560  1.00 12.16           C  
-ATOM    466  CG  TRP A  90      14.284  -0.842   5.934  1.00 11.70           C  
-ATOM    467  CD1 TRP A  90      14.815  -1.199   7.136  1.00 11.86           C  
-ATOM    468  CD2 TRP A  90      13.223   0.082   6.229  1.00 12.11           C  
-ATOM    469  NE1 TRP A  90      14.147  -0.572   8.161  1.00 11.22           N  
-ATOM    470  CE2 TRP A  90      13.169   0.226   7.635  1.00 11.58           C  
-ATOM    471  CE3 TRP A  90      12.305   0.800   5.449  1.00 12.22           C  
-ATOM    472  CZ2 TRP A  90      12.244   1.061   8.273  1.00 11.72           C  
-ATOM    473  CZ3 TRP A  90      11.384   1.631   6.086  1.00 11.86           C  
-ATOM    474  CH2 TRP A  90      11.360   1.753   7.481  1.00 11.69           C  
-ATOM    475  N   MET A  91      13.286  -3.564   2.399  1.00 13.09           N  
-ATOM    476  CA  MET A  91      13.056  -3.901   0.997  1.00 13.24           C  
-ATOM    477  C   MET A  91      11.899  -3.053   0.465  1.00 13.24           C  
-ATOM    478  O   MET A  91      10.902  -2.887   1.164  1.00 13.54           O  
-ATOM    479  CB  MET A  91      12.752  -5.398   0.858  1.00 13.31           C  
-ATOM    480  CG  MET A  91      13.889  -6.315   1.325  1.00 14.49           C  
-ATOM    481  SD  MET A  91      15.369  -6.218   0.294  1.00 15.59           S  
-ATOM    482  CE  MET A  91      14.916  -7.321  -1.041  1.00 16.54           C  
-ATOM    483  N   PRO A  92      11.985  -2.553  -0.771  1.00 13.31           N  
-ATOM    484  CA  PRO A  92      12.964  -2.988  -1.772  1.00 13.27           C  
-ATOM    485  C   PRO A  92      14.341  -2.292  -1.818  1.00 13.10           C  
-ATOM    486  O   PRO A  92      15.187  -2.715  -2.602  1.00 12.78           O  
-ATOM    487  CB  PRO A  92      12.229  -2.707  -3.080  1.00 13.32           C  
-ATOM    488  CG  PRO A  92      11.445  -1.452  -2.784  1.00 13.37           C  
-ATOM    489  CD  PRO A  92      11.080  -1.519  -1.310  1.00 13.30           C  
-ATOM    490  N   THR A  93      14.571  -1.260  -1.007  1.00 13.14           N  
-ATOM    491  CA  THR A  93      15.796  -0.439  -1.166  1.00 13.15           C  
-ATOM    492  C   THR A  93      17.120  -1.186  -0.951  1.00 13.41           C  
-ATOM    493  O   THR A  93      18.120  -0.867  -1.596  1.00 13.68           O  
-ATOM    494  CB  THR A  93      15.757   0.850  -0.314  1.00 12.81           C  
-ATOM    495  OG1 THR A  93      15.437   0.525   1.047  1.00 12.43           O  
-ATOM    496  CG2 THR A  93      14.622   1.774  -0.773  1.00 12.91           C  
-ATOM    497  N   MET A  94      17.123  -2.184  -0.070  1.00 13.91           N  
-ATOM    498  CA  MET A  94      18.344  -2.958   0.205  1.00 14.19           C  
-ATOM    499  C   MET A  94      18.621  -4.107  -0.757  1.00 14.32           C  
-ATOM    500  O   MET A  94      19.513  -4.914  -0.496  1.00 14.35           O  
-ATOM    501  CB  MET A  94      18.329  -3.519   1.624  1.00 14.56           C  
-ATOM    502  CG  MET A  94      18.732  -2.527   2.670  1.00 14.25           C  
-ATOM    503  SD  MET A  94      18.967  -3.308   4.265  1.00 14.73           S  
-ATOM    504  CE  MET A  94      18.994  -1.852   5.305  1.00 14.27           C  
-ATOM    505  N   GLU A  95      17.873  -4.184  -1.854  1.00 14.44           N  
-ATOM    506  CA  GLU A  95      18.059  -5.254  -2.842  1.00 14.61           C  
-ATOM    507  C   GLU A  95      19.526  -5.440  -3.250  1.00 14.58           C  
-ATOM    508  O   GLU A  95      20.038  -6.559  -3.225  1.00 14.39           O  
-ATOM    509  CB  GLU A  95      17.158  -5.038  -4.066  1.00 14.65           C  
-ATOM    510  CG  GLU A  95      17.423  -5.960  -5.255  1.00 15.47           C  
-ATOM    511  CD  GLU A  95      17.150  -7.436  -4.981  1.00 16.98           C  
-ATOM    512  OE1 GLU A  95      16.351  -7.766  -4.077  1.00 18.10           O  
-ATOM    513  OE2 GLU A  95      17.742  -8.278  -5.689  1.00 17.72           O  
-ATOM    514  N   ALA A  96      20.200  -4.342  -3.591  1.00 14.48           N  
-ATOM    515  CA  ALA A  96      21.594  -4.391  -4.042  1.00 14.58           C  
-ATOM    516  C   ALA A  96      22.555  -4.843  -2.943  1.00 14.63           C  
-ATOM    517  O   ALA A  96      23.571  -5.480  -3.221  1.00 14.46           O  
-ATOM    518  CB  ALA A  96      22.022  -3.036  -4.606  1.00 14.54           C  
-ATOM    519  N   ASP A  97      22.224  -4.515  -1.698  1.00 14.80           N  
-ATOM    520  CA  ASP A  97      23.048  -4.897  -0.552  1.00 14.93           C  
-ATOM    521  C   ASP A  97      22.967  -6.390  -0.239  1.00 15.10           C  
-ATOM    522  O   ASP A  97      23.990  -7.026   0.036  1.00 14.79           O  
-ATOM    523  CB  ASP A  97      22.656  -4.090   0.688  1.00 14.79           C  
-ATOM    524  CG  ASP A  97      22.845  -2.596   0.497  1.00 15.64           C  
-ATOM    525  OD1 ASP A  97      24.000  -2.148   0.311  1.00 14.67           O  
-ATOM    526  OD2 ASP A  97      21.892  -1.794   0.524  1.00 16.49           O  
-ATOM    527  N   ILE A  98      21.752  -6.936  -0.272  1.00 14.91           N  
-ATOM    528  CA  ILE A  98      21.520  -8.326   0.123  1.00 15.05           C  
-ATOM    529  C   ILE A  98      21.629  -9.324  -1.039  1.00 14.97           C  
-ATOM    530  O   ILE A  98      21.959 -10.489  -0.814  1.00 15.12           O  
-ATOM    531  CB  ILE A  98      20.154  -8.478   0.870  1.00 14.89           C  
-ATOM    532  CG1 ILE A  98      20.076  -9.838   1.584  1.00 15.12           C  
-ATOM    533  CG2 ILE A  98      18.975  -8.262  -0.083  1.00 14.89           C  
-ATOM    534  CD1 ILE A  98      18.913  -9.980   2.543  1.00 14.99           C  
-ATOM    535  N   ALA A  99      21.375  -8.860  -2.267  1.00 15.11           N  
-ATOM    536  CA  ALA A  99      21.351  -9.736  -3.455  1.00 15.15           C  
-ATOM    537  C   ALA A  99      22.511 -10.743  -3.577  1.00 15.23           C  
-ATOM    538  O   ALA A  99      22.249 -11.939  -3.719  1.00 15.13           O  
-ATOM    539  CB  ALA A  99      21.190  -8.928  -4.746  1.00 15.16           C  
-ATOM    540  N   PRO A 100      23.771 -10.288  -3.518  1.00 15.34           N  
-ATOM    541  CA  PRO A 100      24.916 -11.200  -3.653  1.00 15.60           C  
-ATOM    542  C   PRO A 100      24.950 -12.303  -2.596  1.00 15.79           C  
-ATOM    543  O   PRO A 100      25.456 -13.398  -2.866  1.00 15.65           O  
-ATOM    544  CB  PRO A 100      26.126 -10.275  -3.471  1.00 15.53           C  
-ATOM    545  CG  PRO A 100      25.621  -8.911  -3.806  1.00 15.60           C  
-ATOM    546  CD  PRO A 100      24.214  -8.893  -3.325  1.00 15.38           C  
-ATOM    547  N   TYR A 101      24.413 -12.003  -1.415  1.00 16.03           N  
-ATOM    548  CA  TYR A 101      24.433 -12.907  -0.259  1.00 16.67           C  
-ATOM    549  C   TYR A 101      23.249 -13.874  -0.242  1.00 17.38           C  
-ATOM    550  O   TYR A 101      23.359 -14.996   0.260  1.00 17.09           O  
-ATOM    551  CB  TYR A 101      24.469 -12.094   1.037  1.00 16.37           C  
-ATOM    552  CG  TYR A 101      25.664 -11.175   1.128  1.00 16.36           C  
-ATOM    553  CD1 TYR A 101      25.593  -9.858   0.674  1.00 15.88           C  
-ATOM    554  CD2 TYR A 101      26.873 -11.630   1.648  1.00 15.82           C  
-ATOM    555  CE1 TYR A 101      26.694  -9.016   0.743  1.00 15.86           C  
-ATOM    556  CE2 TYR A 101      27.980 -10.796   1.725  1.00 16.04           C  
-ATOM    557  CZ  TYR A 101      27.882  -9.491   1.272  1.00 15.77           C  
-ATOM    558  OH  TYR A 101      28.976  -8.663   1.342  1.00 17.57           O  
-ATOM    559  N   ARG A 102      22.117 -13.424  -0.775  1.00 18.45           N  
-ATOM    560  CA  ARG A 102      20.967 -14.291  -1.004  1.00 19.64           C  
-ATOM    561  C   ARG A 102      21.326 -15.319  -2.073  1.00 19.81           C  
-ATOM    562  O   ARG A 102      20.961 -16.493  -1.967  1.00 20.15           O  
-ATOM    563  CB  ARG A 102      19.746 -13.461  -1.428  1.00 19.51           C  
-ATOM    564  CG  ARG A 102      18.522 -14.281  -1.829  1.00 20.50           C  
-ATOM    565  CD  ARG A 102      17.361 -13.460  -2.386  1.00 20.66           C  
-ATOM    566  NE  ARG A 102      17.730 -12.733  -3.603  1.00 22.98           N  
-ATOM    567  CZ  ARG A 102      17.687 -11.411  -3.740  1.00 22.79           C  
-ATOM    568  NH1 ARG A 102      17.270 -10.639  -2.745  1.00 23.48           N  
-ATOM    569  NH2 ARG A 102      18.047 -10.859  -4.891  1.00 22.83           N  
-ATOM    570  N   GLU A 103      22.063 -14.863  -3.085  1.00 20.33           N  
-ATOM    571  CA  GLU A 103      22.502 -15.695  -4.203  1.00 20.76           C  
-ATOM    572  C   GLU A 103      23.466 -16.812  -3.796  1.00 20.50           C  
-ATOM    573  O   GLU A 103      23.249 -17.973  -4.150  1.00 20.48           O  
-ATOM    574  CB  GLU A 103      23.119 -14.829  -5.306  1.00 20.78           C  
-ATOM    575  CG  GLU A 103      22.093 -14.048  -6.118  1.00 21.63           C  
-ATOM    576  CD  GLU A 103      22.720 -13.022  -7.047  1.00 21.71           C  
-ATOM    577  OE1 GLU A 103      23.840 -13.268  -7.549  1.00 23.11           O  
-ATOM    578  OE2 GLU A 103      22.085 -11.970  -7.283  1.00 22.76           O  
-ATOM    579  N   ASP A 104      24.523 -16.471  -3.059  1.00 20.28           N  
-ATOM    580  CA  ASP A 104      25.481 -17.486  -2.602  1.00 19.89           C  
-ATOM    581  C   ASP A 104      25.003 -18.228  -1.343  1.00 19.64           C  
-ATOM    582  O   ASP A 104      25.676 -19.142  -0.855  1.00 19.61           O  
-ATOM    583  CB  ASP A 104      26.897 -16.901  -2.435  1.00 19.98           C  
-ATOM    584  CG  ASP A 104      27.015 -15.919  -1.277  1.00 20.18           C  
-ATOM    585  OD1 ASP A 104      26.094 -15.823  -0.440  1.00 20.54           O  
-ATOM    586  OD2 ASP A 104      28.020 -15.200  -1.120  1.00 20.65           O  
-ATOM    587  N   LYS A 105      23.834 -17.820  -0.845  1.00 19.25           N  
-ATOM    588  CA  LYS A 105      23.153 -18.429   0.311  1.00 19.06           C  
-ATOM    589  C   LYS A 105      23.907 -18.311   1.642  1.00 18.71           C  
-ATOM    590  O   LYS A 105      23.672 -19.085   2.572  1.00 18.57           O  
-ATOM    591  CB  LYS A 105      22.753 -19.887   0.022  1.00 19.17           C  
-ATOM    592  CG  LYS A 105      21.653 -20.028  -1.020  1.00 19.25           C  
-ATOM    593  CD  LYS A 105      21.191 -21.465  -1.156  1.00 19.59           C  
-ATOM    594  CE  LYS A 105      20.229 -21.633  -2.326  1.00 20.47           C  
-ATOM    595  NZ  LYS A 105      20.833 -21.221  -3.627  1.00 20.85           N  
-ATOM    596  N   SER A 106      24.797 -17.327   1.734  1.00 18.28           N  
-ATOM    597  CA  SER A 106      25.508 -17.054   2.980  1.00 17.89           C  
-ATOM    598  C   SER A 106      24.627 -16.303   3.978  1.00 17.62           C  
-ATOM    599  O   SER A 106      24.911 -16.292   5.178  1.00 17.59           O  
-ATOM    600  CB  SER A 106      26.794 -16.274   2.706  1.00 17.76           C  
-ATOM    601  OG  SER A 106      26.505 -15.022   2.114  1.00 17.94           O  
-ATOM    602  N   VAL A 107      23.559 -15.684   3.470  1.00 17.29           N  
-ATOM    603  CA  VAL A 107      22.596 -14.942   4.282  1.00 16.76           C  
-ATOM    604  C   VAL A 107      21.177 -15.426   3.964  1.00 16.98           C  
-ATOM    605  O   VAL A 107      20.800 -15.540   2.794  1.00 16.79           O  
-ATOM    606  CB  VAL A 107      22.714 -13.404   4.049  1.00 16.93           C  
-ATOM    607  CG1 VAL A 107      21.580 -12.646   4.731  1.00 16.56           C  
-ATOM    608  CG2 VAL A 107      24.052 -12.880   4.554  1.00 16.07           C  
-ATOM    609  N   GLU A 108      20.412 -15.727   5.010  1.00 16.91           N  
-ATOM    610  CA  GLU A 108      19.030 -16.183   4.863  1.00 17.32           C  
-ATOM    611  C   GLU A 108      18.044 -15.135   5.363  1.00 17.35           C  
-ATOM    612  O   GLU A 108      18.361 -14.350   6.260  1.00 17.15           O  
-ATOM    613  CB  GLU A 108      18.816 -17.500   5.614  1.00 17.20           C  
-ATOM    614  CG  GLU A 108      19.529 -18.692   4.993  1.00 18.42           C  
-ATOM    615  CD  GLU A 108      19.607 -19.891   5.920  1.00 19.42           C  
-ATOM    616  OE1 GLU A 108      18.781 -19.992   6.854  1.00 19.39           O  
-ATOM    617  OE2 GLU A 108      20.498 -20.744   5.709  1.00 20.93           O  
-ATOM    618  N   THR A 109      16.848 -15.126   4.779  1.00 17.50           N  
-ATOM    619  CA  THR A 109      15.779 -14.245   5.235  1.00 17.92           C  
-ATOM    620  C   THR A 109      14.723 -15.068   5.975  1.00 18.03           C  
-ATOM    621  O   THR A 109      14.061 -15.922   5.384  1.00 18.34           O  
-ATOM    622  CB  THR A 109      15.175 -13.443   4.052  1.00 18.02           C  
-ATOM    623  OG1 THR A 109      16.166 -12.557   3.512  1.00 18.00           O  
-ATOM    624  CG2 THR A 109      14.094 -12.483   4.537  1.00 18.27           C  
-ATOM    625  N   VAL A 110      14.589 -14.806   7.273  1.00 18.05           N  
-ATOM    626  CA  VAL A 110      13.750 -15.615   8.166  1.00 17.96           C  
-ATOM    627  C   VAL A 110      12.279 -15.241   8.054  1.00 17.76           C  
-ATOM    628  O   VAL A 110      11.412 -16.116   7.928  1.00 17.69           O  
-ATOM    629  CB  VAL A 110      14.197 -15.468   9.655  1.00 18.28           C  
-ATOM    630  CG1 VAL A 110      13.293 -16.268  10.591  1.00 18.62           C  
-ATOM    631  CG2 VAL A 110      15.626 -15.915   9.828  1.00 18.50           C  
-ATOM    632  N   ARG A 111      12.009 -13.940   8.096  1.00 17.14           N  
-ATOM    633  CA  ARG A 111      10.658 -13.444   8.291  1.00 16.90           C  
-ATOM    634  C   ARG A 111      10.537 -11.997   7.846  1.00 16.14           C  
-ATOM    635  O   ARG A 111      11.514 -11.252   7.858  1.00 15.79           O  
-ATOM    636  CB  ARG A 111      10.305 -13.517   9.782  1.00 16.94           C  
-ATOM    637  CG  ARG A 111       8.821 -13.627  10.074  1.00 18.72           C  
-ATOM    638  CD  ARG A 111       8.406 -12.945  11.367  1.00 19.56           C  
-ATOM    639  NE  ARG A 111       7.242 -13.596  11.959  1.00 21.88           N  
-ATOM    640  CZ  ARG A 111       5.982 -13.284  11.694  1.00 21.89           C  
-ATOM    641  NH1 ARG A 111       5.009 -13.951  12.293  1.00 21.81           N  
-ATOM    642  NH2 ARG A 111       5.690 -12.311  10.835  1.00 21.51           N  
-ATOM    643  N   GLU A 112       9.324 -11.608   7.467  1.00 15.54           N  
-ATOM    644  CA  GLU A 112       8.977 -10.204   7.349  1.00 15.56           C  
-ATOM    645  C   GLU A 112       8.549  -9.745   8.737  1.00 14.79           C  
-ATOM    646  O   GLU A 112       7.510 -10.180   9.249  1.00 15.01           O  
-ATOM    647  CB  GLU A 112       7.852 -10.012   6.329  1.00 15.75           C  
-ATOM    648  CG  GLU A 112       7.338  -8.587   6.209  1.00 16.52           C  
-ATOM    649  CD  GLU A 112       6.431  -8.404   5.005  1.00 17.12           C  
-ATOM    650  OE1 GLU A 112       5.339  -7.830   5.171  1.00 19.35           O  
-ATOM    651  OE2 GLU A 112       6.806  -8.843   3.893  1.00 19.29           O  
-ATOM    652  N   ASN A 113       9.363  -8.893   9.357  1.00 13.84           N  
-ATOM    653  CA  ASN A 113       9.091  -8.458  10.725  1.00 13.22           C  
-ATOM    654  C   ASN A 113       8.265  -7.178  10.820  1.00 12.57           C  
-ATOM    655  O   ASN A 113       7.770  -6.837  11.895  1.00 12.71           O  
-ATOM    656  CB  ASN A 113      10.375  -8.404  11.573  1.00 12.94           C  
-ATOM    657  CG  ASN A 113      11.319  -7.271  11.174  1.00 13.23           C  
-ATOM    658  OD1 ASN A 113      10.921  -6.107  11.068  1.00 12.76           O  
-ATOM    659  ND2 ASN A 113      12.595  -7.606  11.010  1.00 11.92           N  
-ATOM    660  N   LEU A 114       8.111  -6.486   9.691  1.00 12.35           N  
-ATOM    661  CA  LEU A 114       7.307  -5.260   9.627  1.00 11.61           C  
-ATOM    662  C   LEU A 114       6.731  -5.002   8.242  1.00 11.30           C  
-ATOM    663  O   LEU A 114       7.458  -4.994   7.244  1.00 10.95           O  
-ATOM    664  CB  LEU A 114       8.122  -4.030  10.065  1.00 11.79           C  
-ATOM    665  CG  LEU A 114       7.335  -2.716  10.142  1.00 11.19           C  
-ATOM    666  CD1 LEU A 114       6.406  -2.737  11.348  1.00 11.81           C  
-ATOM    667  CD2 LEU A 114       8.270  -1.515  10.203  1.00 11.64           C  
-ATOM    668  N   ALA A 115       5.423  -4.770   8.195  1.00 10.61           N  
-ATOM    669  CA  ALA A 115       4.755  -4.383   6.956  1.00 10.39           C  
-ATOM    670  C   ALA A 115       4.208  -2.965   7.095  1.00 10.10           C  
-ATOM    671  O   ALA A 115       4.014  -2.473   8.214  1.00  9.54           O  
-ATOM    672  CB  ALA A 115       3.632  -5.367   6.629  1.00 10.39           C  
-ATOM    673  N   GLY A 116       3.964  -2.310   5.962  1.00  9.85           N  
-ATOM    674  CA  GLY A 116       3.344  -0.988   5.955  1.00  9.60           C  
-ATOM    675  C   GLY A 116       4.299   0.143   6.291  1.00  9.85           C  
-ATOM    676  O   GLY A 116       3.873   1.217   6.713  1.00  9.67           O  
-ATOM    677  N   ALA A 117       5.594  -0.110   6.120  1.00  9.43           N  
-ATOM    678  CA  ALA A 117       6.599   0.933   6.262  1.00  9.61           C  
-ATOM    679  C   ALA A 117       6.683   1.728   4.959  1.00  9.59           C  
-ATOM    680  O   ALA A 117       6.076   1.349   3.951  1.00  9.45           O  
-ATOM    681  CB  ALA A 117       7.951   0.316   6.614  1.00  9.53           C  
-ATOM    682  N   LYS A 118       7.412   2.840   4.983  1.00  9.92           N  
-ATOM    683  CA  LYS A 118       7.726   3.573   3.754  1.00  9.68           C  
-ATOM    684  C   LYS A 118       9.094   4.232   3.860  1.00  9.08           C  
-ATOM    685  O   LYS A 118       9.562   4.520   4.958  1.00  8.87           O  
-ATOM    686  CB  LYS A 118       6.645   4.603   3.421  1.00 10.07           C  
-ATOM    687  CG  LYS A 118       6.657   5.846   4.301  1.00 11.88           C  
-ATOM    688  CD  LYS A 118       5.259   6.326   4.653  1.00 15.78           C  
-ATOM    689  CE  LYS A 118       4.322   6.311   3.459  1.00 17.52           C  
-ATOM    690  NZ  LYS A 118       4.469   7.528   2.634  1.00 19.32           N  
-ATOM    691  N   TYR A 119       9.726   4.458   2.712  1.00  8.22           N  
-ATOM    692  CA  TYR A 119      11.069   5.021   2.664  1.00  7.98           C  
-ATOM    693  C   TYR A 119      11.260   5.672   1.306  1.00  8.26           C  
-ATOM    694  O   TYR A 119      11.308   4.986   0.292  1.00  8.10           O  
-ATOM    695  CB  TYR A 119      12.106   3.908   2.858  1.00  7.36           C  
-ATOM    696  CG  TYR A 119      13.542   4.355   3.091  1.00  6.63           C  
-ATOM    697  CD1 TYR A 119      13.841   5.586   3.684  1.00  5.74           C  
-ATOM    698  CD2 TYR A 119      14.600   3.515   2.751  1.00  6.77           C  
-ATOM    699  CE1 TYR A 119      15.173   5.982   3.911  1.00  5.49           C  
-ATOM    700  CE2 TYR A 119      15.931   3.895   2.975  1.00  7.00           C  
-ATOM    701  CZ  TYR A 119      16.204   5.123   3.555  1.00  6.10           C  
-ATOM    702  OH  TYR A 119      17.511   5.484   3.778  1.00  7.15           O  
-ATOM    703  N   THR A 120      11.341   6.997   1.289  1.00  8.66           N  
-ATOM    704  CA  THR A 120      11.604   7.729   0.048  1.00  9.18           C  
-ATOM    705  C   THR A 120      12.044   9.149   0.381  1.00  9.49           C  
-ATOM    706  O   THR A 120      12.193   9.503   1.558  1.00  9.35           O  
-ATOM    707  CB  THR A 120      10.349   7.698  -0.886  1.00  9.02           C  
-ATOM    708  OG1 THR A 120      10.682   8.224  -2.179  1.00  9.63           O  
-ATOM    709  CG2 THR A 120       9.245   8.621  -0.382  1.00  8.63           C  
-ATOM    710  N   LEU A 121      12.267   9.964  -0.644  1.00 10.01           N  
-ATOM    711  CA  LEU A 121      12.616  11.359  -0.417  1.00 10.62           C  
-ATOM    712  C   LEU A 121      11.409  12.166   0.055  1.00 10.95           C  
-ATOM    713  O   LEU A 121      10.281  11.946  -0.391  1.00 11.41           O  
-ATOM    714  CB  LEU A 121      13.245  11.984  -1.666  1.00 10.89           C  
-ATOM    715  CG  LEU A 121      14.662  11.545  -2.036  1.00 10.87           C  
-ATOM    716  CD1 LEU A 121      15.072  12.187  -3.359  1.00 11.50           C  
-ATOM    717  CD2 LEU A 121      15.658  11.896  -0.929  1.00 11.42           C  
-ATOM    718  N   ALA A 122      11.669  13.082   0.983  1.00 11.13           N  
-ATOM    719  CA  ALA A 122      10.648  13.926   1.569  1.00 11.41           C  
-ATOM    720  C   ALA A 122      11.131  15.364   1.571  1.00 11.61           C  
-ATOM    721  O   ALA A 122      12.323  15.632   1.403  1.00 11.78           O  
-ATOM    722  CB  ALA A 122      10.348  13.478   2.998  1.00 10.72           C  
-ATOM    723  N   THR A 123      10.196  16.283   1.776  1.00 11.79           N  
-ATOM    724  CA  THR A 123      10.534  17.686   1.953  1.00 11.84           C  
-ATOM    725  C   THR A 123       9.774  18.241   3.152  1.00 12.05           C  
-ATOM    726  O   THR A 123       8.868  17.586   3.671  1.00 12.08           O  
-ATOM    727  CB  THR A 123      10.273  18.491   0.649  1.00 12.02           C  
-ATOM    728  OG1 THR A 123      10.808  19.813   0.790  1.00 11.74           O  
-ATOM    729  CG2 THR A 123       8.779  18.723   0.409  1.00 11.30           C  
-ATOM    730  N   ASN A 124      10.163  19.428   3.610  1.00 12.44           N  
-ATOM    731  CA  ASN A 124       9.471  20.074   4.722  1.00 12.48           C  
-ATOM    732  C   ASN A 124       8.298  20.929   4.239  1.00 12.66           C  
-ATOM    733  O   ASN A 124       7.993  20.949   3.049  1.00 12.40           O  
-ATOM    734  CB  ASN A 124      10.449  20.893   5.574  1.00 12.43           C  
-ATOM    735  CG  ASN A 124      11.184  21.973   4.778  1.00 12.31           C  
-ATOM    736  OD1 ASN A 124      11.048  22.084   3.556  1.00 12.54           O  
-ATOM    737  ND2 ASN A 124      11.974  22.772   5.482  1.00 11.85           N  
-ATOM    738  N   ALA A 125       7.646  21.624   5.169  1.00 12.63           N  
-ATOM    739  CA  ALA A 125       6.532  22.520   4.848  1.00 13.00           C  
-ATOM    740  C   ALA A 125       6.909  23.596   3.821  1.00 13.24           C  
-ATOM    741  O   ALA A 125       6.125  23.894   2.917  1.00 13.49           O  
-ATOM    742  CB  ALA A 125       5.981  23.157   6.119  1.00 13.05           C  
-ATOM    743  N   LYS A 126       8.107  24.165   3.958  1.00 13.39           N  
-ATOM    744  CA  LYS A 126       8.578  25.219   3.055  1.00 13.47           C  
-ATOM    745  C   LYS A 126       8.808  24.683   1.645  1.00 13.45           C  
-ATOM    746  O   LYS A 126       8.496  25.355   0.659  1.00 13.31           O  
-ATOM    747  CB  LYS A 126       9.858  25.869   3.591  1.00 13.48           C  
-ATOM    748  CG  LYS A 126      10.384  27.040   2.756  1.00 14.20           C  
-ATOM    749  CD  LYS A 126       9.495  28.274   2.854  1.00 15.58           C  
-ATOM    750  CE  LYS A 126       9.978  29.360   1.905  1.00 16.81           C  
-ATOM    751  NZ  LYS A 126       9.303  30.671   2.135  1.00 17.61           N  
-ATOM    752  N   GLY A 127       9.364  23.478   1.563  1.00 13.47           N  
-ATOM    753  CA  GLY A 127       9.546  22.790   0.290  1.00 13.52           C  
-ATOM    754  C   GLY A 127       8.226  22.605  -0.438  1.00 13.59           C  
-ATOM    755  O   GLY A 127       8.113  22.950  -1.616  1.00 13.21           O  
-ATOM    756  N   ALA A 128       7.227  22.079   0.273  1.00 13.85           N  
-ATOM    757  CA  ALA A 128       5.893  21.853  -0.298  1.00 14.54           C  
-ATOM    758  C   ALA A 128       5.227  23.166  -0.701  1.00 14.90           C  
-ATOM    759  O   ALA A 128       4.539  23.226  -1.718  1.00 15.20           O  
-ATOM    760  CB  ALA A 128       5.011  21.080   0.668  1.00 14.41           C  
-ATOM    761  N   GLU A 129       5.451  24.206   0.105  1.00 15.13           N  
-ATOM    762  CA  GLU A 129       5.009  25.569  -0.185  1.00 15.61           C  
-ATOM    763  C   GLU A 129       5.605  26.076  -1.502  1.00 15.17           C  
-ATOM    764  O   GLU A 129       4.961  26.828  -2.232  1.00 15.03           O  
-ATOM    765  CB  GLU A 129       5.430  26.486   0.961  1.00 15.44           C  
-ATOM    766  CG  GLU A 129       4.844  27.890   0.945  1.00 17.15           C  
-ATOM    767  CD  GLU A 129       5.273  28.701   2.157  1.00 17.01           C  
-ATOM    768  OE1 GLU A 129       5.610  28.085   3.192  1.00 19.94           O  
-ATOM    769  OE2 GLU A 129       5.272  29.950   2.077  1.00 19.05           O  
-ATOM    770  N   LEU A 130       6.832  25.652  -1.795  1.00 14.81           N  
-ATOM    771  CA  LEU A 130       7.537  26.068  -3.009  1.00 14.62           C  
-ATOM    772  C   LEU A 130       7.218  25.203  -4.231  1.00 14.36           C  
-ATOM    773  O   LEU A 130       7.662  25.497  -5.340  1.00 14.13           O  
-ATOM    774  CB  LEU A 130       9.049  26.114  -2.758  1.00 14.68           C  
-ATOM    775  CG  LEU A 130       9.662  27.451  -2.329  1.00 15.28           C  
-ATOM    776  CD1 LEU A 130       8.745  28.277  -1.427  1.00 16.26           C  
-ATOM    777  CD2 LEU A 130      11.014  27.242  -1.672  1.00 14.81           C  
-ATOM    778  N   GLY A 131       6.446  24.143  -4.025  1.00 14.12           N  
-ATOM    779  CA  GLY A 131       6.026  23.285  -5.126  1.00 14.01           C  
-ATOM    780  C   GLY A 131       6.897  22.059  -5.316  1.00 13.81           C  
-ATOM    781  O   GLY A 131       6.874  21.436  -6.378  1.00 13.60           O  
-ATOM    782  N   ILE A 132       7.680  21.724  -4.295  1.00 13.21           N  
-ATOM    783  CA  ILE A 132       8.429  20.470  -4.290  1.00 13.34           C  
-ATOM    784  C   ILE A 132       7.489  19.361  -3.810  1.00 13.01           C  
-ATOM    785  O   ILE A 132       7.300  19.170  -2.608  1.00 13.07           O  
-ATOM    786  CB  ILE A 132       9.700  20.564  -3.397  1.00 13.11           C  
-ATOM    787  CG1 ILE A 132      10.540  21.800  -3.759  1.00 13.44           C  
-ATOM    788  CG2 ILE A 132      10.536  19.283  -3.519  1.00 13.91           C  
-ATOM    789  CD1 ILE A 132      11.747  22.055  -2.836  1.00 13.24           C  
-ATOM    790  N   LYS A 133       6.887  18.655  -4.763  1.00 12.97           N  
-ATOM    791  CA  LYS A 133       5.922  17.597  -4.459  1.00 13.17           C  
-ATOM    792  C   LYS A 133       6.302  16.258  -5.093  1.00 12.88           C  
-ATOM    793  O   LYS A 133       5.726  15.219  -4.755  1.00 12.77           O  
-ATOM    794  CB  LYS A 133       4.513  17.991  -4.924  1.00 13.11           C  
-ATOM    795  CG  LYS A 133       3.890  19.187  -4.208  1.00 14.95           C  
-ATOM    796  CD  LYS A 133       3.526  18.879  -2.742  1.00 17.25           C  
-ATOM    797  CE  LYS A 133       2.402  19.791  -2.238  1.00 19.44           C  
-ATOM    798  NZ  LYS A 133       2.518  21.207  -2.714  1.00 20.69           N  
-ATOM    799  N   ASP A 134       7.264  16.301  -6.011  1.00 12.66           N  
-ATOM    800  CA  ASP A 134       7.646  15.148  -6.821  1.00 12.75           C  
-ATOM    801  C   ASP A 134       9.161  15.123  -6.999  1.00 12.58           C  
-ATOM    802  O   ASP A 134       9.805  16.167  -6.955  1.00 12.73           O  
-ATOM    803  CB  ASP A 134       6.957  15.239  -8.193  1.00 12.78           C  
-ATOM    804  CG  ASP A 134       7.029  13.944  -8.979  1.00 13.36           C  
-ATOM    805  OD1 ASP A 134       8.082  13.666  -9.594  1.00 14.07           O  
-ATOM    806  OD2 ASP A 134       6.066  13.155  -9.061  1.00 13.62           O  
-ATOM    807  N   PHE A 135       9.723  13.931  -7.198  1.00 12.54           N  
-ATOM    808  CA  PHE A 135      11.156  13.771  -7.479  1.00 12.57           C  
-ATOM    809  C   PHE A 135      11.594  14.697  -8.620  1.00 12.74           C  
-ATOM    810  O   PHE A 135      12.709  15.237  -8.608  1.00 12.52           O  
-ATOM    811  CB  PHE A 135      11.464  12.313  -7.854  1.00 12.64           C  
-ATOM    812  CG  PHE A 135      11.809  11.423  -6.684  1.00 12.88           C  
-ATOM    813  CD1 PHE A 135      13.003  10.704  -6.679  1.00 11.84           C  
-ATOM    814  CD2 PHE A 135      10.940  11.284  -5.601  1.00 12.44           C  
-ATOM    815  CE1 PHE A 135      13.331   9.862  -5.624  1.00 12.26           C  
-ATOM    816  CE2 PHE A 135      11.261  10.450  -4.527  1.00 12.29           C  
-ATOM    817  CZ  PHE A 135      12.463   9.737  -4.537  1.00 12.27           C  
-ATOM    818  N   LYS A 136      10.693  14.890  -9.587  1.00 12.51           N  
-ATOM    819  CA  LYS A 136      10.942  15.734 -10.756  1.00 12.89           C  
-ATOM    820  C   LYS A 136      11.008  17.236 -10.428  1.00 12.73           C  
-ATOM    821  O   LYS A 136      11.404  18.030 -11.279  1.00 12.36           O  
-ATOM    822  CB  LYS A 136       9.866  15.475 -11.823  1.00 12.80           C  
-ATOM    823  CG  LYS A 136      10.280  15.798 -13.267  1.00 14.86           C  
-ATOM    824  CD  LYS A 136      11.177  14.701 -13.848  1.00 17.68           C  
-ATOM    825  CE  LYS A 136      12.087  15.223 -14.954  1.00 18.39           C  
-ATOM    826  NZ  LYS A 136      11.377  15.397 -16.244  1.00 19.30           N  
-ATOM    827  N   ASP A 137      10.621  17.617  -9.208  1.00 12.26           N  
-ATOM    828  CA  ASP A 137      10.589  19.032  -8.804  1.00 12.39           C  
-ATOM    829  C   ASP A 137      11.874  19.501  -8.122  1.00 12.38           C  
-ATOM    830  O   ASP A 137      12.116  20.704  -8.018  1.00 12.51           O  
-ATOM    831  CB  ASP A 137       9.420  19.304  -7.849  1.00 12.25           C  
-ATOM    832  CG  ASP A 137       8.072  19.055  -8.483  1.00 12.79           C  
-ATOM    833  OD1 ASP A 137       7.899  19.355  -9.690  1.00 12.81           O  
-ATOM    834  OD2 ASP A 137       7.118  18.569  -7.842  1.00 11.03           O  
-ATOM    835  N   ILE A 138      12.680  18.554  -7.650  1.00 12.05           N  
-ATOM    836  CA  ILE A 138      13.866  18.874  -6.851  1.00 12.11           C  
-ATOM    837  C   ILE A 138      14.845  19.776  -7.613  1.00 12.09           C  
-ATOM    838  O   ILE A 138      15.225  20.836  -7.110  1.00 11.94           O  
-ATOM    839  CB  ILE A 138      14.569  17.591  -6.344  1.00 11.91           C  
-ATOM    840  CG1 ILE A 138      13.599  16.728  -5.521  1.00 11.62           C  
-ATOM    841  CG2 ILE A 138      15.790  17.956  -5.495  1.00 12.41           C  
-ATOM    842  CD1 ILE A 138      14.073  15.292  -5.294  1.00 12.24           C  
-ATOM    843  N   ALA A 139      15.216  19.366  -8.828  1.00 11.72           N  
-ATOM    844  CA  ALA A 139      16.200  20.094  -9.638  1.00 11.88           C  
-ATOM    845  C   ALA A 139      15.746  21.510  -9.990  1.00 12.00           C  
-ATOM    846  O   ALA A 139      16.573  22.420 -10.117  1.00 12.00           O  
-ATOM    847  CB  ALA A 139      16.530  19.312 -10.911  1.00 12.15           C  
-ATOM    848  N   ALA A 140      14.435  21.683 -10.151  1.00 11.56           N  
-ATOM    849  CA  ALA A 140      13.836  22.990 -10.417  1.00 11.75           C  
-ATOM    850  C   ALA A 140      14.096  23.981  -9.280  1.00 11.79           C  
-ATOM    851  O   ALA A 140      14.061  25.194  -9.494  1.00 11.49           O  
-ATOM    852  CB  ALA A 140      12.340  22.843 -10.658  1.00 11.71           C  
-ATOM    853  N   HIS A 141      14.355  23.454  -8.083  1.00 11.73           N  
-ATOM    854  CA  HIS A 141      14.642  24.277  -6.906  1.00 11.92           C  
-ATOM    855  C   HIS A 141      16.089  24.137  -6.406  1.00 11.93           C  
-ATOM    856  O   HIS A 141      16.367  24.314  -5.215  1.00 11.35           O  
-ATOM    857  CB  HIS A 141      13.634  23.964  -5.798  1.00 11.98           C  
-ATOM    858  CG  HIS A 141      12.216  24.233  -6.194  1.00 12.29           C  
-ATOM    859  ND1 HIS A 141      11.626  25.471  -6.049  1.00 13.49           N  
-ATOM    860  CD2 HIS A 141      11.283  23.436  -6.768  1.00 12.82           C  
-ATOM    861  CE1 HIS A 141      10.385  25.419  -6.498  1.00 13.90           C  
-ATOM    862  NE2 HIS A 141      10.151  24.196  -6.940  1.00 13.60           N  
-ATOM    863  N   LYS A 142      17.010  23.857  -7.330  1.00 11.86           N  
-ATOM    864  CA  LYS A 142      18.421  23.616  -6.983  1.00 11.97           C  
-ATOM    865  C   LYS A 142      19.089  24.795  -6.262  1.00 12.17           C  
-ATOM    866  O   LYS A 142      19.911  24.589  -5.367  1.00 12.12           O  
-ATOM    867  CB  LYS A 142      19.233  23.199  -8.219  1.00 12.05           C  
-ATOM    868  CG  LYS A 142      19.194  24.200  -9.368  1.00 12.04           C  
-ATOM    869  CD  LYS A 142      19.766  23.615 -10.645  1.00 12.13           C  
-ATOM    870  CE  LYS A 142      19.691  24.637 -11.766  1.00 13.10           C  
-ATOM    871  NZ  LYS A 142      20.225  24.106 -13.056  1.00 13.27           N  
-ATOM    872  N   ASP A 143      18.730  26.023  -6.638  1.00 11.90           N  
-ATOM    873  CA  ASP A 143      19.294  27.204  -5.974  1.00 12.23           C  
-ATOM    874  C   ASP A 143      18.805  27.350  -4.534  1.00 12.00           C  
-ATOM    875  O   ASP A 143      19.599  27.627  -3.633  1.00 11.85           O  
-ATOM    876  CB  ASP A 143      19.024  28.483  -6.777  1.00 12.19           C  
-ATOM    877  CG  ASP A 143      19.784  28.520  -8.096  1.00 13.11           C  
-ATOM    878  OD1 ASP A 143      20.717  27.709  -8.289  1.00 14.60           O  
-ATOM    879  OD2 ASP A 143      19.517  29.329  -9.002  1.00 12.43           O  
-ATOM    880  N   GLU A 144      17.504  27.142  -4.324  1.00 11.98           N  
-ATOM    881  CA  GLU A 144      16.890  27.269  -3.000  1.00 12.30           C  
-ATOM    882  C   GLU A 144      17.355  26.177  -2.046  1.00 12.21           C  
-ATOM    883  O   GLU A 144      17.408  26.384  -0.828  1.00 11.91           O  
-ATOM    884  CB  GLU A 144      15.363  27.233  -3.095  1.00 12.53           C  
-ATOM    885  CG  GLU A 144      14.749  28.373  -3.887  1.00 13.44           C  
-ATOM    886  CD  GLU A 144      14.374  27.976  -5.302  1.00 16.18           C  
-ATOM    887  OE1 GLU A 144      15.238  27.455  -6.047  1.00 15.17           O  
-ATOM    888  OE2 GLU A 144      13.202  28.201  -5.673  1.00 17.73           O  
-ATOM    889  N   LEU A 145      17.675  25.015  -2.608  1.00 12.07           N  
-ATOM    890  CA  LEU A 145      18.178  23.886  -1.837  1.00 12.47           C  
-ATOM    891  C   LEU A 145      19.701  23.896  -1.697  1.00 12.96           C  
-ATOM    892  O   LEU A 145      20.270  23.000  -1.070  1.00 13.08           O  
-ATOM    893  CB  LEU A 145      17.727  22.571  -2.482  1.00 12.37           C  
-ATOM    894  CG  LEU A 145      16.222  22.280  -2.529  1.00 12.15           C  
-ATOM    895  CD1 LEU A 145      15.953  21.071  -3.406  1.00 11.08           C  
-ATOM    896  CD2 LEU A 145      15.644  22.065  -1.129  1.00 11.99           C  
-ATOM    897  N   ASP A 146      20.352  24.897  -2.296  1.00 13.38           N  
-ATOM    898  CA  ASP A 146      21.823  24.983  -2.352  1.00 13.90           C  
-ATOM    899  C   ASP A 146      22.457  23.719  -2.968  1.00 13.70           C  
-ATOM    900  O   ASP A 146      23.561  23.317  -2.595  1.00 13.86           O  
-ATOM    901  CB  ASP A 146      22.407  25.297  -0.962  1.00 13.99           C  
-ATOM    902  CG  ASP A 146      23.861  25.756  -1.013  1.00 15.51           C  
-ATOM    903  OD1 ASP A 146      24.312  26.278  -2.058  1.00 16.00           O  
-ATOM    904  OD2 ASP A 146      24.635  25.630  -0.041  1.00 17.86           O  
-ATOM    905  N   GLY A 147      21.742  23.105  -3.913  1.00 13.59           N  
-ATOM    906  CA  GLY A 147      22.213  21.912  -4.618  1.00 13.04           C  
-ATOM    907  C   GLY A 147      22.555  20.738  -3.717  1.00 12.99           C  
-ATOM    908  O   GLY A 147      23.492  19.984  -4.003  1.00 12.83           O  
-ATOM    909  N   LYS A 148      21.795  20.586  -2.630  1.00 12.17           N  
-ATOM    910  CA  LYS A 148      22.024  19.520  -1.661  1.00 12.19           C  
-ATOM    911  C   LYS A 148      20.789  18.650  -1.463  1.00 11.74           C  
-ATOM    912  O   LYS A 148      19.655  19.130  -1.524  1.00 10.99           O  
-ATOM    913  CB  LYS A 148      22.470  20.097  -0.308  1.00 12.15           C  
-ATOM    914  CG  LYS A 148      23.878  20.673  -0.297  1.00 13.59           C  
-ATOM    915  CD  LYS A 148      24.087  21.568   0.921  1.00 16.09           C  
-ATOM    916  CE  LYS A 148      25.564  21.788   1.231  1.00 17.70           C  
-ATOM    917  NZ  LYS A 148      26.325  22.378   0.083  1.00 19.42           N  
-ATOM    918  N   ILE A 149      21.031  17.360  -1.244  1.00 11.50           N  
-ATOM    919  CA  ILE A 149      20.030  16.443  -0.695  1.00 11.16           C  
-ATOM    920  C   ILE A 149      20.669  15.806   0.527  1.00 11.40           C  
-ATOM    921  O   ILE A 149      21.818  15.372   0.464  1.00 11.23           O  
-ATOM    922  CB  ILE A 149      19.635  15.356  -1.721  1.00 11.30           C  
-ATOM    923  CG1 ILE A 149      18.877  15.979  -2.895  1.00 10.65           C  
-ATOM    924  CG2 ILE A 149      18.794  14.248  -1.046  1.00 11.03           C  
-ATOM    925  CD1 ILE A 149      18.826  15.097  -4.137  1.00 12.78           C  
-ATOM    926  N   TYR A 150      19.930  15.761   1.631  1.00 11.16           N  
-ATOM    927  CA  TYR A 150      20.458  15.239   2.889  1.00 11.90           C  
-ATOM    928  C   TYR A 150      20.104  13.785   3.133  1.00 11.90           C  
-ATOM    929  O   TYR A 150      18.926  13.422   3.221  1.00 12.35           O  
-ATOM    930  CB  TYR A 150      20.001  16.110   4.058  1.00 11.76           C  
-ATOM    931  CG  TYR A 150      20.682  17.447   4.050  1.00 12.50           C  
-ATOM    932  CD1 TYR A 150      20.163  18.512   3.312  1.00 12.40           C  
-ATOM    933  CD2 TYR A 150      21.872  17.642   4.751  1.00 13.12           C  
-ATOM    934  CE1 TYR A 150      20.801  19.742   3.289  1.00 13.12           C  
-ATOM    935  CE2 TYR A 150      22.521  18.865   4.731  1.00 13.87           C  
-ATOM    936  CZ  TYR A 150      21.980  19.910   4.001  1.00 13.21           C  
-ATOM    937  OH  TYR A 150      22.616  21.125   3.984  1.00 13.02           O  
-ATOM    938  N   GLY A 151      21.138  12.958   3.243  1.00 11.78           N  
-ATOM    939  CA  GLY A 151      20.959  11.539   3.520  1.00 11.88           C  
-ATOM    940  C   GLY A 151      21.319  11.192   4.951  1.00 11.73           C  
-ATOM    941  O   GLY A 151      21.381  12.069   5.820  1.00 11.48           O  
-ATOM    942  N   ILE A 152      21.552   9.906   5.200  1.00 11.73           N  
-ATOM    943  CA  ILE A 152      21.980   9.454   6.524  1.00 11.80           C  
-ATOM    944  C   ILE A 152      23.414   8.892   6.503  1.00 11.89           C  
-ATOM    945  O   ILE A 152      24.282   9.479   5.856  1.00 11.83           O  
-ATOM    946  CB  ILE A 152      20.926   8.508   7.161  1.00 11.64           C  
-ATOM    947  CG1 ILE A 152      20.542   7.370   6.206  1.00 11.72           C  
-ATOM    948  CG2 ILE A 152      19.677   9.306   7.525  1.00 13.03           C  
-ATOM    949  CD1 ILE A 152      19.482   6.441   6.765  1.00 11.33           C  
-ATOM    950  N   GLU A 153      23.672   7.773   7.181  1.00 12.00           N  
-ATOM    951  CA  GLU A 153      25.058   7.304   7.362  1.00 12.14           C  
-ATOM    952  C   GLU A 153      25.688   6.748   6.073  1.00 12.25           C  
-ATOM    953  O   GLU A 153      24.985   6.183   5.227  1.00 12.49           O  
-ATOM    954  CB  GLU A 153      25.167   6.305   8.535  1.00 12.26           C  
-ATOM    955  CG  GLU A 153      24.816   4.844   8.224  1.00 12.09           C  
-ATOM    956  CD  GLU A 153      23.343   4.604   7.925  1.00 11.17           C  
-ATOM    957  OE1 GLU A 153      23.022   3.546   7.341  1.00 11.67           O  
-ATOM    958  OE2 GLU A 153      22.504   5.459   8.262  1.00 12.22           O  
-ATOM    959  N   PRO A 154      26.997   6.931   5.905  1.00 12.22           N  
-ATOM    960  CA  PRO A 154      27.706   6.313   4.782  1.00 12.06           C  
-ATOM    961  C   PRO A 154      27.376   4.825   4.647  1.00 11.88           C  
-ATOM    962  O   PRO A 154      27.175   4.129   5.649  1.00 11.70           O  
-ATOM    963  CB  PRO A 154      29.174   6.530   5.141  1.00 12.12           C  
-ATOM    964  CG  PRO A 154      29.157   7.827   5.889  1.00 12.40           C  
-ATOM    965  CD  PRO A 154      27.898   7.770   6.725  1.00 12.14           C  
-ATOM    966  N   GLY A 155      27.281   4.360   3.406  1.00 11.82           N  
-ATOM    967  CA  GLY A 155      26.947   2.968   3.130  1.00 11.63           C  
-ATOM    968  C   GLY A 155      25.455   2.696   3.065  1.00 11.72           C  
-ATOM    969  O   GLY A 155      25.042   1.639   2.592  1.00 11.99           O  
-ATOM    970  N   ASN A 156      24.637   3.640   3.533  1.00 11.56           N  
-ATOM    971  CA  ASN A 156      23.187   3.429   3.579  1.00 11.42           C  
-ATOM    972  C   ASN A 156      22.585   3.123   2.209  1.00 11.44           C  
-ATOM    973  O   ASN A 156      23.063   3.620   1.191  1.00 11.29           O  
-ATOM    974  CB  ASN A 156      22.466   4.626   4.192  1.00 11.60           C  
-ATOM    975  CG  ASN A 156      21.018   4.319   4.508  1.00 11.51           C  
-ATOM    976  OD1 ASN A 156      20.109   4.707   3.767  1.00 10.74           O  
-ATOM    977  ND2 ASN A 156      20.794   3.604   5.605  1.00 11.00           N  
-ATOM    978  N   ASP A 157      21.539   2.299   2.204  1.00 11.51           N  
-ATOM    979  CA  ASP A 157      20.849   1.912   0.981  1.00 11.62           C  
-ATOM    980  C   ASP A 157      20.133   3.092   0.338  1.00 12.02           C  
-ATOM    981  O   ASP A 157      20.152   3.227  -0.876  1.00 11.71           O  
-ATOM    982  CB  ASP A 157      19.888   0.738   1.223  1.00 11.55           C  
-ATOM    983  CG  ASP A 157      18.998   0.940   2.434  1.00 11.89           C  
-ATOM    984  OD1 ASP A 157      19.517   1.277   3.519  1.00 10.60           O  
-ATOM    985  OD2 ASP A 157      17.763   0.758   2.395  1.00 12.39           O  
-ATOM    986  N   GLY A 158      19.510   3.939   1.158  1.00 11.98           N  
-ATOM    987  CA  GLY A 158      18.895   5.179   0.670  1.00 12.21           C  
-ATOM    988  C   GLY A 158      19.925   6.145   0.109  1.00 12.14           C  
-ATOM    989  O   GLY A 158      19.757   6.666  -0.995  1.00 12.46           O  
-ATOM    990  N   ASN A 159      21.004   6.373   0.859  1.00 11.91           N  
-ATOM    991  CA  ASN A 159      22.134   7.166   0.362  1.00 11.69           C  
-ATOM    992  C   ASN A 159      22.594   6.724  -1.026  1.00 11.98           C  
-ATOM    993  O   ASN A 159      22.758   7.547  -1.922  1.00 11.83           O  
-ATOM    994  CB  ASN A 159      23.321   7.089   1.326  1.00 11.90           C  
-ATOM    995  CG  ASN A 159      23.165   8.007   2.514  1.00 11.42           C  
-ATOM    996  OD1 ASN A 159      24.150   8.541   3.040  1.00 14.57           O  
-ATOM    997  ND2 ASN A 159      21.933   8.198   2.949  1.00  8.90           N  
-ATOM    998  N   ARG A 160      22.795   5.417  -1.179  1.00 11.44           N  
-ATOM    999  CA  ARG A 160      23.253   4.816  -2.428  1.00 11.79           C  
-ATOM   1000  C   ARG A 160      22.331   5.146  -3.600  1.00 11.59           C  
-ATOM   1001  O   ARG A 160      22.800   5.518  -4.677  1.00 11.77           O  
-ATOM   1002  CB  ARG A 160      23.383   3.300  -2.250  1.00 11.48           C  
-ATOM   1003  CG  ARG A 160      23.722   2.534  -3.518  1.00 12.17           C  
-ATOM   1004  CD  ARG A 160      23.956   1.040  -3.304  1.00 12.12           C  
-ATOM   1005  NE  ARG A 160      23.022   0.417  -2.357  1.00 11.75           N  
-ATOM   1006  CZ  ARG A 160      21.764   0.072  -2.638  1.00 12.73           C  
-ATOM   1007  NH1 ARG A 160      21.245   0.314  -3.835  1.00 11.94           N  
-ATOM   1008  NH2 ARG A 160      21.013  -0.500  -1.707  1.00 12.00           N  
-ATOM   1009  N   LEU A 161      21.023   5.004  -3.388  1.00 11.74           N  
-ATOM   1010  CA  LEU A 161      20.043   5.311  -4.437  1.00 11.85           C  
-ATOM   1011  C   LEU A 161      20.073   6.782  -4.859  1.00 12.05           C  
-ATOM   1012  O   LEU A 161      20.013   7.073  -6.045  1.00 12.16           O  
-ATOM   1013  CB  LEU A 161      18.631   4.889  -4.015  1.00 11.57           C  
-ATOM   1014  CG  LEU A 161      18.427   3.376  -3.868  1.00 12.20           C  
-ATOM   1015  CD1 LEU A 161      17.100   3.071  -3.176  1.00 12.45           C  
-ATOM   1016  CD2 LEU A 161      18.507   2.680  -5.220  1.00 12.28           C  
-ATOM   1017  N   ILE A 162      20.171   7.700  -3.897  1.00 12.21           N  
-ATOM   1018  CA  ILE A 162      20.287   9.128  -4.228  1.00 12.29           C  
-ATOM   1019  C   ILE A 162      21.598   9.426  -4.950  1.00 12.35           C  
-ATOM   1020  O   ILE A 162      21.601  10.142  -5.954  1.00 12.59           O  
-ATOM   1021  CB  ILE A 162      20.179  10.043  -2.985  1.00 12.46           C  
-ATOM   1022  CG1 ILE A 162      18.987   9.672  -2.097  1.00 12.46           C  
-ATOM   1023  CG2 ILE A 162      20.090  11.519  -3.416  1.00 12.03           C  
-ATOM   1024  CD1 ILE A 162      19.075  10.291  -0.707  1.00 12.48           C  
-ATOM   1025  N   ILE A 163      22.705   8.885  -4.438  1.00 12.31           N  
-ATOM   1026  CA  ILE A 163      24.019   9.091  -5.061  1.00 12.37           C  
-ATOM   1027  C   ILE A 163      24.019   8.606  -6.514  1.00 12.73           C  
-ATOM   1028  O   ILE A 163      24.578   9.271  -7.391  1.00 12.47           O  
-ATOM   1029  CB  ILE A 163      25.149   8.415  -4.233  1.00 12.90           C  
-ATOM   1030  CG1 ILE A 163      25.343   9.137  -2.887  1.00 11.98           C  
-ATOM   1031  CG2 ILE A 163      26.458   8.370  -5.025  1.00 11.89           C  
-ATOM   1032  CD1 ILE A 163      26.041   8.301  -1.831  1.00 13.18           C  
-ATOM   1033  N   ASP A 164      23.386   7.459  -6.767  1.00 12.94           N  
-ATOM   1034  CA AASP A 164      23.288   6.920  -8.124  0.50 13.13           C  
-ATOM   1035  CA BASP A 164      23.282   6.921  -8.128  0.50 13.32           C  
-ATOM   1036  C   ASP A 164      22.492   7.844  -9.053  1.00 13.15           C  
-ATOM   1037  O   ASP A 164      22.866   8.034 -10.218  1.00 13.20           O  
-ATOM   1038  CB AASP A 164      22.671   5.519  -8.108  0.50 13.24           C  
-ATOM   1039  CB BASP A 164      22.656   5.523  -8.118  0.50 13.65           C  
-ATOM   1040  CG AASP A 164      22.876   4.778  -9.414  0.50 13.48           C  
-ATOM   1041  CG BASP A 164      23.584   4.470  -7.547  0.50 14.50           C  
-ATOM   1042  OD1AASP A 164      24.040   4.618  -9.838  0.50 13.09           O  
-ATOM   1043  OD1BASP A 164      24.818   4.606  -7.680  0.50 16.20           O  
-ATOM   1044  OD2AASP A 164      21.930   4.314 -10.082  0.50 14.49           O  
-ATOM   1045  OD2BASP A 164      23.169   3.460  -6.944  0.50 16.91           O  
-ATOM   1046  N   MET A 165      21.399   8.404  -8.535  1.00 13.28           N  
-ATOM   1047  CA  MET A 165      20.578   9.366  -9.279  1.00 13.64           C  
-ATOM   1048  C   MET A 165      21.410  10.578  -9.664  1.00 13.62           C  
-ATOM   1049  O   MET A 165      21.438  10.968 -10.831  1.00 13.62           O  
-ATOM   1050  CB  MET A 165      19.361   9.830  -8.470  1.00 13.38           C  
-ATOM   1051  CG  MET A 165      18.178   8.868  -8.456  1.00 13.94           C  
-ATOM   1052  SD  MET A 165      16.640   9.648  -7.890  1.00 14.52           S  
-ATOM   1053  CE  MET A 165      17.149  10.356  -6.323  1.00 13.59           C  
-ATOM   1054  N   VAL A 166      22.095  11.157  -8.679  1.00 13.75           N  
-ATOM   1055  CA  VAL A 166      22.964  12.324  -8.898  1.00 13.99           C  
-ATOM   1056  C   VAL A 166      24.057  12.062  -9.944  1.00 14.55           C  
-ATOM   1057  O   VAL A 166      24.261  12.878 -10.848  1.00 14.20           O  
-ATOM   1058  CB  VAL A 166      23.575  12.836  -7.557  1.00 14.03           C  
-ATOM   1059  CG1 VAL A 166      24.684  13.863  -7.801  1.00 14.24           C  
-ATOM   1060  CG2 VAL A 166      22.491  13.420  -6.676  1.00 13.07           C  
-ATOM   1061  N   GLU A 167      24.749  10.929  -9.824  1.00 14.97           N  
-ATOM   1062  CA  GLU A 167      25.822  10.573 -10.761  1.00 16.00           C  
-ATOM   1063  C   GLU A 167      25.304  10.332 -12.178  1.00 15.61           C  
-ATOM   1064  O   GLU A 167      25.959  10.693 -13.159  1.00 15.70           O  
-ATOM   1065  CB  GLU A 167      26.592   9.345 -10.274  1.00 15.90           C  
-ATOM   1066  CG  GLU A 167      27.343   9.553  -8.966  1.00 17.70           C  
-ATOM   1067  CD  GLU A 167      27.986   8.280  -8.450  1.00 18.08           C  
-ATOM   1068  OE1 GLU A 167      27.512   7.172  -8.801  1.00 21.44           O  
-ATOM   1069  OE2 GLU A 167      28.970   8.388  -7.688  1.00 21.95           O  
-ATOM   1070  N   LYS A 168      24.128   9.717 -12.275  1.00 15.31           N  
-ATOM   1071  CA  LYS A 168      23.476   9.479 -13.562  1.00 15.34           C  
-ATOM   1072  C   LYS A 168      22.794  10.716 -14.133  1.00 14.78           C  
-ATOM   1073  O   LYS A 168      22.534  10.787 -15.332  1.00 14.36           O  
-ATOM   1074  CB  LYS A 168      22.453   8.352 -13.444  1.00 15.35           C  
-ATOM   1075  CG  LYS A 168      22.913   7.036 -14.021  1.00 16.70           C  
-ATOM   1076  CD  LYS A 168      23.645   6.187 -13.005  1.00 18.28           C  
-ATOM   1077  CE  LYS A 168      23.778   4.764 -13.520  1.00 18.42           C  
-ATOM   1078  NZ  LYS A 168      23.856   3.783 -12.418  1.00 19.92           N  
-ATOM   1079  N   GLY A 169      22.493  11.682 -13.269  1.00 14.41           N  
-ATOM   1080  CA  GLY A 169      21.735  12.860 -13.676  1.00 14.06           C  
-ATOM   1081  C   GLY A 169      20.262  12.524 -13.822  1.00 14.11           C  
-ATOM   1082  O   GLY A 169      19.548  13.158 -14.603  1.00 14.01           O  
-ATOM   1083  N   THR A 170      19.814  11.517 -13.069  1.00 13.83           N  
-ATOM   1084  CA  THR A 170      18.405  11.152 -13.021  1.00 13.95           C  
-ATOM   1085  C   THR A 170      17.636  12.305 -12.394  1.00 13.96           C  
-ATOM   1086  O   THR A 170      18.096  12.903 -11.416  1.00 13.77           O  
-ATOM   1087  CB  THR A 170      18.215   9.850 -12.219  1.00 14.07           C  
-ATOM   1088  OG1 THR A 170      18.998   8.810 -12.818  1.00 13.98           O  
-ATOM   1089  CG2 THR A 170      16.782   9.332 -12.329  1.00 14.00           C  
-ATOM   1090  N   PHE A 171      16.482  12.623 -12.979  1.00 13.99           N  
-ATOM   1091  CA  PHE A 171      15.665  13.772 -12.563  1.00 13.83           C  
-ATOM   1092  C   PHE A 171      16.454  15.091 -12.584  1.00 13.86           C  
-ATOM   1093  O   PHE A 171      16.207  15.985 -11.769  1.00 13.78           O  
-ATOM   1094  CB  PHE A 171      15.008  13.519 -11.195  1.00 13.55           C  
-ATOM   1095  CG  PHE A 171      14.125  12.301 -11.168  1.00 13.25           C  
-ATOM   1096  CD1 PHE A 171      14.442  11.215 -10.361  1.00 13.49           C  
-ATOM   1097  CD2 PHE A 171      12.986  12.231 -11.969  1.00 13.96           C  
-ATOM   1098  CE1 PHE A 171      13.638  10.080 -10.343  1.00 13.15           C  
-ATOM   1099  CE2 PHE A 171      12.169  11.099 -11.953  1.00 14.43           C  
-ATOM   1100  CZ  PHE A 171      12.498  10.022 -11.137  1.00 13.61           C  
-ATOM   1101  N   ASP A 172      17.394  15.182 -13.529  1.00 13.78           N  
-ATOM   1102  CA AASP A 172      18.229  16.373 -13.733  0.50 13.76           C  
-ATOM   1103  CA BASP A 172      18.224  16.380 -13.723  0.50 13.90           C  
-ATOM   1104  C   ASP A 172      19.043  16.753 -12.484  1.00 13.83           C  
-ATOM   1105  O   ASP A 172      19.345  17.929 -12.253  1.00 13.53           O  
-ATOM   1106  CB AASP A 172      17.374  17.551 -14.235  0.50 13.68           C  
-ATOM   1107  CB BASP A 172      17.371  17.574 -14.183  0.50 13.97           C  
-ATOM   1108  CG AASP A 172      18.208  18.709 -14.762  0.50 13.80           C  
-ATOM   1109  CG BASP A 172      17.044  17.530 -15.664  0.50 14.60           C  
-ATOM   1110  OD1AASP A 172      19.343  18.480 -15.239  0.50 13.62           O  
-ATOM   1111  OD1BASP A 172      17.430  16.558 -16.346  0.50 15.94           O  
-ATOM   1112  OD2AASP A 172      17.802  19.889 -14.736  0.50 13.69           O  
-ATOM   1113  OD2BASP A 172      16.403  18.434 -16.238  0.50 15.18           O  
-ATOM   1114  N   LEU A 173      19.421  15.747 -11.698  1.00 13.93           N  
-ATOM   1115  CA  LEU A 173      20.113  15.982 -10.420  1.00 14.11           C  
-ATOM   1116  C   LEU A 173      21.640  16.049 -10.510  1.00 14.18           C  
-ATOM   1117  O   LEU A 173      22.324  16.037  -9.488  1.00 14.10           O  
-ATOM   1118  CB  LEU A 173      19.687  14.943  -9.378  1.00 14.04           C  
-ATOM   1119  CG  LEU A 173      18.234  15.008  -8.896  1.00 14.35           C  
-ATOM   1120  CD1 LEU A 173      17.909  13.803  -8.027  1.00 13.32           C  
-ATOM   1121  CD2 LEU A 173      17.955  16.321  -8.154  1.00 14.31           C  
-ATOM   1122  N   LYS A 174      22.173  16.140 -11.725  1.00 14.63           N  
-ATOM   1123  CA  LYS A 174      23.620  16.218 -11.907  1.00 15.20           C  
-ATOM   1124  C   LYS A 174      24.179  17.458 -11.217  1.00 15.00           C  
-ATOM   1125  O   LYS A 174      23.628  18.547 -11.336  1.00 15.25           O  
-ATOM   1126  CB  LYS A 174      23.985  16.227 -13.395  1.00 15.65           C  
-ATOM   1127  CG  LYS A 174      25.306  15.551 -13.691  1.00 17.62           C  
-ATOM   1128  CD  LYS A 174      25.604  15.503 -15.181  1.00 19.81           C  
-ATOM   1129  CE  LYS A 174      26.874  14.702 -15.463  1.00 21.58           C  
-ATOM   1130  NZ  LYS A 174      26.718  13.261 -15.113  1.00 22.44           N  
-ATOM   1131  N   GLY A 175      25.268  17.286 -10.479  1.00 14.86           N  
-ATOM   1132  CA  GLY A 175      25.872  18.409  -9.767  1.00 14.46           C  
-ATOM   1133  C   GLY A 175      25.318  18.653  -8.374  1.00 14.10           C  
-ATOM   1134  O   GLY A 175      25.800  19.534  -7.664  1.00 13.50           O  
-ATOM   1135  N   PHE A 176      24.301  17.885  -7.983  1.00 14.21           N  
-ATOM   1136  CA  PHE A 176      23.830  17.886  -6.601  1.00 14.47           C  
-ATOM   1137  C   PHE A 176      24.855  17.205  -5.703  1.00 14.57           C  
-ATOM   1138  O   PHE A 176      25.684  16.416  -6.167  1.00 14.69           O  
-ATOM   1139  CB  PHE A 176      22.474  17.180  -6.472  1.00 14.56           C  
-ATOM   1140  CG  PHE A 176      21.290  18.110  -6.519  1.00 14.57           C  
-ATOM   1141  CD1 PHE A 176      20.886  18.687  -7.719  1.00 15.50           C  
-ATOM   1142  CD2 PHE A 176      20.569  18.391  -5.363  1.00 15.79           C  
-ATOM   1143  CE1 PHE A 176      19.785  19.546  -7.765  1.00 15.77           C  
-ATOM   1144  CE2 PHE A 176      19.464  19.246  -5.394  1.00 15.82           C  
-ATOM   1145  CZ  PHE A 176      19.074  19.824  -6.601  1.00 15.21           C  
-ATOM   1146  N   GLU A 177      24.800  17.526  -4.416  1.00 14.68           N  
-ATOM   1147  CA  GLU A 177      25.645  16.890  -3.422  1.00 15.09           C  
-ATOM   1148  C   GLU A 177      24.740  16.123  -2.472  1.00 14.43           C  
-ATOM   1149  O   GLU A 177      23.723  16.652  -2.021  1.00 14.24           O  
-ATOM   1150  CB  GLU A 177      26.433  17.951  -2.652  1.00 15.25           C  
-ATOM   1151  CG  GLU A 177      27.397  17.402  -1.613  1.00 16.53           C  
-ATOM   1152  CD  GLU A 177      28.123  18.497  -0.854  1.00 17.00           C  
-ATOM   1153  OE1 GLU A 177      28.264  19.615  -1.393  1.00 19.25           O  
-ATOM   1154  OE2 GLU A 177      28.562  18.235   0.287  1.00 20.60           O  
-ATOM   1155  N   VAL A 178      25.097  14.873  -2.192  1.00 13.90           N  
-ATOM   1156  CA  VAL A 178      24.397  14.088  -1.185  1.00 13.21           C  
-ATOM   1157  C   VAL A 178      25.171  14.245   0.119  1.00 12.96           C  
-ATOM   1158  O   VAL A 178      26.310  13.778   0.241  1.00 12.60           O  
-ATOM   1159  CB  VAL A 178      24.253  12.599  -1.587  1.00 13.47           C  
-ATOM   1160  CG1 VAL A 178      23.408  11.852  -0.571  1.00 12.76           C  
-ATOM   1161  CG2 VAL A 178      23.635  12.472  -2.985  1.00 13.50           C  
-ATOM   1162  N   VAL A 179      24.564  14.939   1.077  1.00 12.38           N  
-ATOM   1163  CA  VAL A 179      25.237  15.236   2.332  1.00 12.08           C  
-ATOM   1164  C   VAL A 179      24.992  14.066   3.276  1.00 11.87           C  
-ATOM   1165  O   VAL A 179      23.853  13.796   3.663  1.00 11.45           O  
-ATOM   1166  CB  VAL A 179      24.745  16.552   2.969  1.00 12.10           C  
-ATOM   1167  CG1 VAL A 179      25.613  16.914   4.169  1.00 12.06           C  
-ATOM   1168  CG2 VAL A 179      24.731  17.691   1.945  1.00 11.62           C  
-ATOM   1169  N   GLU A 180      26.065  13.362   3.618  1.00 11.81           N  
-ATOM   1170  CA  GLU A 180      25.960  12.170   4.465  1.00 12.14           C  
-ATOM   1171  C   GLU A 180      26.339  12.483   5.900  1.00 12.10           C  
-ATOM   1172  O   GLU A 180      27.287  13.227   6.153  1.00 11.96           O  
-ATOM   1173  CB  GLU A 180      26.857  11.051   3.937  1.00 12.46           C  
-ATOM   1174  CG  GLU A 180      26.711  10.790   2.450  1.00 12.39           C  
-ATOM   1175  CD  GLU A 180      27.369   9.494   2.039  1.00 13.53           C  
-ATOM   1176  OE1 GLU A 180      28.620   9.469   1.955  1.00 13.91           O  
-ATOM   1177  OE2 GLU A 180      26.635   8.505   1.809  1.00 12.09           O  
-ATOM   1178  N   SER A 181      25.594  11.907   6.839  1.00 12.07           N  
-ATOM   1179  CA  SER A 181      25.902  12.055   8.257  1.00 11.98           C  
-ATOM   1180  C   SER A 181      25.385  10.843   9.014  1.00 11.98           C  
-ATOM   1181  O   SER A 181      26.126   9.883   9.248  1.00 11.67           O  
-ATOM   1182  CB  SER A 181      25.316  13.358   8.823  1.00 12.16           C  
-ATOM   1183  OG  SER A 181      23.935  13.488   8.521  1.00 12.06           O  
-ATOM   1184  N   SER A 182      24.101  10.901   9.361  1.00 11.98           N  
-ATOM   1185  CA  SER A 182      23.399   9.874  10.128  1.00 11.77           C  
-ATOM   1186  C   SER A 182      21.946  10.310  10.225  1.00 11.89           C  
-ATOM   1187  O   SER A 182      21.610  11.434   9.858  1.00 11.39           O  
-ATOM   1188  CB  SER A 182      23.983   9.754  11.538  1.00 12.24           C  
-ATOM   1189  OG  SER A 182      23.845  10.974  12.255  1.00 11.50           O  
-ATOM   1190  N   GLU A 183      21.085   9.432  10.731  1.00 11.60           N  
-ATOM   1191  CA  GLU A 183      19.708   9.816  11.008  1.00 11.68           C  
-ATOM   1192  C   GLU A 183      19.672  11.082  11.868  1.00 11.59           C  
-ATOM   1193  O   GLU A 183      18.931  12.031  11.578  1.00 11.49           O  
-ATOM   1194  CB  GLU A 183      18.960   8.688  11.717  1.00 11.56           C  
-ATOM   1195  CG  GLU A 183      17.565   9.105  12.151  1.00 12.20           C  
-ATOM   1196  CD  GLU A 183      16.943   8.145  13.132  1.00 11.93           C  
-ATOM   1197  OE1 GLU A 183      16.908   6.934  12.838  1.00 13.53           O  
-ATOM   1198  OE2 GLU A 183      16.470   8.615  14.183  1.00 12.06           O  
-ATOM   1199  N  AGLN A 184      20.503  11.081  12.901  0.70 11.69           N  
-ATOM   1200  N  BGLN A 184      20.464  11.081  12.942  0.30 11.67           N  
-ATOM   1201  CA AGLN A 184      20.556  12.140  13.886  0.70 11.77           C  
-ATOM   1202  CA BGLN A 184      20.525  12.208  13.874  0.30 11.73           C  
-ATOM   1203  C  AGLN A 184      21.042  13.457  13.247  0.70 11.78           C  
-ATOM   1204  C  BGLN A 184      20.996  13.480  13.180  0.30 11.73           C  
-ATOM   1205  O  AGLN A 184      20.450  14.518  13.468  0.70 11.77           O  
-ATOM   1206  O  BGLN A 184      20.372  14.535  13.321  0.30 11.69           O  
-ATOM   1207  CB AGLN A 184      21.433  11.685  15.064  0.70 11.86           C  
-ATOM   1208  CB BGLN A 184      21.427  11.892  15.073  0.30 11.78           C  
-ATOM   1209  CG AGLN A 184      20.881  10.449  15.859  0.70 12.45           C  
-ATOM   1210  CG BGLN A 184      20.800  10.958  16.098  0.30 12.14           C  
-ATOM   1211  CD AGLN A 184      21.005   9.079  15.141  0.70 12.58           C  
-ATOM   1212  CD BGLN A 184      21.486  11.004  17.452  0.30 12.14           C  
-ATOM   1213  OE1AGLN A 184      20.269   8.128  15.467  0.70 13.41           O  
-ATOM   1214  OE1BGLN A 184      22.715  11.045  17.537  0.30 12.74           O  
-ATOM   1215  NE2AGLN A 184      21.931   8.974  14.196  0.70  8.45           N  
-ATOM   1216  NE2BGLN A 184      20.691  10.987  18.515  0.30 11.85           N  
-ATOM   1217  N   GLY A 185      22.087  13.371  12.424  1.00 11.76           N  
-ATOM   1218  CA  GLY A 185      22.617  14.520  11.671  1.00 11.69           C  
-ATOM   1219  C   GLY A 185      21.616  15.109  10.689  1.00 12.00           C  
-ATOM   1220  O   GLY A 185      21.431  16.328  10.635  1.00 11.70           O  
-ATOM   1221  N   MET A 186      20.961  14.236   9.921  1.00 12.04           N  
-ATOM   1222  CA  MET A 186      19.958  14.648   8.934  1.00 12.23           C  
-ATOM   1223  C   MET A 186      18.794  15.386   9.603  1.00 12.44           C  
-ATOM   1224  O   MET A 186      18.417  16.470   9.174  1.00 11.89           O  
-ATOM   1225  CB  MET A 186      19.446  13.428   8.149  1.00 12.10           C  
-ATOM   1226  CG  MET A 186      18.412  13.746   7.082  1.00 11.58           C  
-ATOM   1227  SD  MET A 186      17.457  12.312   6.525  1.00 12.65           S  
-ATOM   1228  CE  MET A 186      16.449  12.014   7.980  1.00 12.54           C  
-ATOM   1229  N   LEU A 187      18.255  14.803  10.673  1.00 12.67           N  
-ATOM   1230  CA  LEU A 187      17.145  15.418  11.407  1.00 13.26           C  
-ATOM   1231  C   LEU A 187      17.502  16.724  12.101  1.00 13.07           C  
-ATOM   1232  O   LEU A 187      16.641  17.590  12.264  1.00 12.98           O  
-ATOM   1233  CB  LEU A 187      16.536  14.433  12.407  1.00 13.37           C  
-ATOM   1234  CG  LEU A 187      15.819  13.247  11.752  1.00 14.61           C  
-ATOM   1235  CD1 LEU A 187      15.477  12.202  12.791  1.00 14.72           C  
-ATOM   1236  CD2 LEU A 187      14.568  13.676  10.985  1.00 16.49           C  
-ATOM   1237  N   ALA A 188      18.762  16.859  12.512  1.00 13.21           N  
-ATOM   1238  CA  ALA A 188      19.264  18.111  13.072  1.00 13.31           C  
-ATOM   1239  C   ALA A 188      19.209  19.213  12.011  1.00 13.46           C  
-ATOM   1240  O   ALA A 188      18.840  20.350  12.299  1.00 13.24           O  
-ATOM   1241  CB  ALA A 188      20.685  17.930  13.583  1.00 13.23           C  
-ATOM   1242  N   GLN A 189      19.569  18.851  10.782  1.00 13.81           N  
-ATOM   1243  CA  GLN A 189      19.539  19.765   9.646  1.00 13.98           C  
-ATOM   1244  C   GLN A 189      18.104  20.136   9.254  1.00 13.85           C  
-ATOM   1245  O   GLN A 189      17.820  21.294   8.937  1.00 13.52           O  
-ATOM   1246  CB  GLN A 189      20.294  19.145   8.459  1.00 14.41           C  
-ATOM   1247  CG  GLN A 189      20.443  20.049   7.239  1.00 15.38           C  
-ATOM   1248  CD  GLN A 189      21.258  21.307   7.500  1.00 17.22           C  
-ATOM   1249  OE1 GLN A 189      20.984  22.354   6.912  1.00 19.78           O  
-ATOM   1250  NE2 GLN A 189      22.257  21.210   8.371  1.00 17.35           N  
-ATOM   1251  N   VAL A 190      17.202  19.156   9.284  1.00 13.86           N  
-ATOM   1252  CA  VAL A 190      15.775  19.417   9.064  1.00 14.02           C  
-ATOM   1253  C   VAL A 190      15.253  20.421  10.102  1.00 14.30           C  
-ATOM   1254  O   VAL A 190      14.514  21.350   9.762  1.00 14.13           O  
-ATOM   1255  CB  VAL A 190      14.948  18.102   9.099  1.00 14.45           C  
-ATOM   1256  CG1 VAL A 190      13.451  18.376   9.064  1.00 14.20           C  
-ATOM   1257  CG2 VAL A 190      15.347  17.192   7.939  1.00 13.67           C  
-ATOM   1258  N   ALA A 191      15.654  20.234  11.359  1.00 14.30           N  
-ATOM   1259  CA  ALA A 191      15.268  21.143  12.438  1.00 14.45           C  
-ATOM   1260  C   ALA A 191      15.785  22.555  12.170  1.00 14.48           C  
-ATOM   1261  O   ALA A 191      15.058  23.532  12.335  1.00 14.45           O  
-ATOM   1262  CB  ALA A 191      15.769  20.625  13.778  1.00 14.43           C  
-ATOM   1263  N   ARG A 192      17.035  22.654  11.728  1.00 14.46           N  
-ATOM   1264  CA  ARG A 192      17.642  23.944  11.411  1.00 14.69           C  
-ATOM   1265  C   ARG A 192      16.966  24.630  10.220  1.00 14.76           C  
-ATOM   1266  O   ARG A 192      16.833  25.855  10.198  1.00 14.57           O  
-ATOM   1267  CB  ARG A 192      19.145  23.781  11.182  1.00 14.65           C  
-ATOM   1268  CG  ARG A 192      19.916  23.449  12.466  1.00 14.87           C  
-ATOM   1269  CD  ARG A 192      21.430  23.469  12.319  1.00 15.13           C  
-ATOM   1270  NE  ARG A 192      21.913  22.393  11.451  1.00 16.40           N  
-ATOM   1271  CZ  ARG A 192      22.383  21.227  11.889  1.00 15.90           C  
-ATOM   1272  NH1 ARG A 192      22.439  20.963  13.189  1.00 15.62           N  
-ATOM   1273  NH2 ARG A 192      22.806  20.322  11.023  1.00 15.89           N  
-ATOM   1274  N   ALA A 193      16.525  23.830   9.250  1.00 14.86           N  
-ATOM   1275  CA  ALA A 193      15.780  24.326   8.090  1.00 15.10           C  
-ATOM   1276  C   ALA A 193      14.439  24.927   8.507  1.00 15.57           C  
-ATOM   1277  O   ALA A 193      13.988  25.922   7.925  1.00 15.62           O  
-ATOM   1278  CB  ALA A 193      15.578  23.213   7.072  1.00 14.87           C  
-ATOM   1279  N   GLU A 194      13.819  24.325   9.522  1.00 15.92           N  
-ATOM   1280  CA  GLU A 194      12.571  24.830  10.097  1.00 16.64           C  
-ATOM   1281  C   GLU A 194      12.752  26.233  10.669  1.00 16.56           C  
-ATOM   1282  O   GLU A 194      11.910  27.110  10.456  1.00 16.80           O  
-ATOM   1283  CB  GLU A 194      12.056  23.888  11.195  1.00 16.81           C  
-ATOM   1284  CG  GLU A 194      11.442  22.586  10.701  1.00 18.28           C  
-ATOM   1285  CD  GLU A 194      10.172  22.798   9.895  1.00 20.60           C  
-ATOM   1286  OE1 GLU A 194       9.195  23.352  10.443  1.00 21.58           O  
-ATOM   1287  OE2 GLU A 194      10.148  22.404   8.716  1.00 20.32           O  
-ATOM   1288  N   LYS A 195      13.857  26.439  11.385  1.00 16.50           N  
-ATOM   1289  CA  LYS A 195      14.151  27.725  12.018  1.00 16.49           C  
-ATOM   1290  C   LYS A 195      14.584  28.788  11.005  1.00 16.18           C  
-ATOM   1291  O   LYS A 195      14.229  29.959  11.142  1.00 15.83           O  
-ATOM   1292  CB  LYS A 195      15.214  27.574  13.118  1.00 16.92           C  
-ATOM   1293  CG  LYS A 195      14.733  26.869  14.391  1.00 18.16           C  
-ATOM   1294  CD  LYS A 195      14.975  25.365  14.317  1.00 20.80           C  
-ATOM   1295  CE  LYS A 195      14.238  24.586  15.403  1.00 21.43           C  
-ATOM   1296  NZ  LYS A 195      15.023  24.484  16.667  1.00 22.25           N  
-ATOM   1297  N   SER A 196      15.342  28.375   9.991  1.00 15.73           N  
-ATOM   1298  CA  SER A 196      15.836  29.304   8.974  1.00 15.77           C  
-ATOM   1299  C   SER A 196      14.768  29.652   7.931  1.00 15.50           C  
-ATOM   1300  O   SER A 196      14.885  30.654   7.221  1.00 15.59           O  
-ATOM   1301  CB  SER A 196      17.090  28.745   8.292  1.00 15.88           C  
-ATOM   1302  OG  SER A 196      16.775  27.654   7.443  1.00 16.50           O  
-ATOM   1303  N   GLY A 197      13.734  28.817   7.841  1.00 15.04           N  
-ATOM   1304  CA  GLY A 197      12.656  29.014   6.877  1.00 14.48           C  
-ATOM   1305  C   GLY A 197      13.028  28.606   5.463  1.00 14.25           C  
-ATOM   1306  O   GLY A 197      12.436  29.089   4.499  1.00 14.24           O  
-ATOM   1307  N   ASP A 198      14.007  27.713   5.336  1.00 13.85           N  
-ATOM   1308  CA  ASP A 198      14.448  27.229   4.031  1.00 13.57           C  
-ATOM   1309  C   ASP A 198      13.807  25.882   3.708  1.00 12.88           C  
-ATOM   1310  O   ASP A 198      13.454  25.134   4.622  1.00 13.05           O  
-ATOM   1311  CB  ASP A 198      15.972  27.089   4.001  1.00 13.86           C  
-ATOM   1312  CG  ASP A 198      16.677  28.425   3.909  1.00 15.15           C  
-ATOM   1313  OD1 ASP A 198      16.452  29.154   2.915  1.00 15.68           O  
-ATOM   1314  OD2 ASP A 198      17.476  28.828   4.782  1.00 16.61           O  
-ATOM   1315  N   PRO A 199      13.645  25.581   2.417  1.00 12.54           N  
-ATOM   1316  CA  PRO A 199      13.261  24.242   1.990  1.00 12.01           C  
-ATOM   1317  C   PRO A 199      14.434  23.280   2.169  1.00 11.93           C  
-ATOM   1318  O   PRO A 199      15.594  23.702   2.138  1.00 11.54           O  
-ATOM   1319  CB  PRO A 199      12.959  24.424   0.499  1.00 12.14           C  
-ATOM   1320  CG  PRO A 199      13.812  25.589   0.084  1.00 12.05           C  
-ATOM   1321  CD  PRO A 199      13.814  26.496   1.272  1.00 12.36           C  
-ATOM   1322  N   ILE A 200      14.126  22.005   2.370  1.00 11.66           N  
-ATOM   1323  CA  ILE A 200      15.143  20.956   2.466  1.00 11.74           C  
-ATOM   1324  C   ILE A 200      14.565  19.673   1.876  1.00 11.78           C  
-ATOM   1325  O   ILE A 200      13.363  19.429   1.988  1.00 11.82           O  
-ATOM   1326  CB  ILE A 200      15.617  20.759   3.947  1.00 11.89           C  
-ATOM   1327  CG1 ILE A 200      16.806  19.783   4.021  1.00 12.45           C  
-ATOM   1328  CG2 ILE A 200      14.454  20.323   4.850  1.00 11.59           C  
-ATOM   1329  CD1 ILE A 200      17.373  19.578   5.447  1.00 11.83           C  
-ATOM   1330  N   VAL A 201      15.414  18.885   1.216  1.00 11.57           N  
-ATOM   1331  CA  VAL A 201      15.025  17.581   0.684  1.00 11.51           C  
-ATOM   1332  C   VAL A 201      15.910  16.521   1.329  1.00 11.35           C  
-ATOM   1333  O   VAL A 201      17.133  16.668   1.379  1.00 11.16           O  
-ATOM   1334  CB  VAL A 201      15.104  17.529  -0.869  1.00 11.76           C  
-ATOM   1335  CG1 VAL A 201      14.802  16.125  -1.396  1.00 11.62           C  
-ATOM   1336  CG2 VAL A 201      14.138  18.538  -1.481  1.00 11.93           C  
-ATOM   1337  N   PHE A 202      15.276  15.463   1.834  1.00 11.11           N  
-ATOM   1338  CA  PHE A 202      15.958  14.470   2.661  1.00 11.22           C  
-ATOM   1339  C   PHE A 202      15.244  13.120   2.636  1.00 11.29           C  
-ATOM   1340  O   PHE A 202      14.198  12.967   2.006  1.00 11.42           O  
-ATOM   1341  CB  PHE A 202      16.048  14.978   4.104  1.00 10.67           C  
-ATOM   1342  CG  PHE A 202      14.707  15.211   4.742  1.00 11.26           C  
-ATOM   1343  CD1 PHE A 202      14.137  14.244   5.570  1.00 10.85           C  
-ATOM   1344  CD2 PHE A 202      14.007  16.397   4.515  1.00 10.34           C  
-ATOM   1345  CE1 PHE A 202      12.885  14.447   6.150  1.00 11.52           C  
-ATOM   1346  CE2 PHE A 202      12.762  16.608   5.087  1.00 11.79           C  
-ATOM   1347  CZ  PHE A 202      12.200  15.634   5.915  1.00 10.91           C  
-ATOM   1348  N   LEU A 203      15.808  12.147   3.345  1.00 11.71           N  
-ATOM   1349  CA  LEU A 203      15.199  10.826   3.453  1.00 11.70           C  
-ATOM   1350  C   LEU A 203      14.190  10.790   4.586  1.00 12.11           C  
-ATOM   1351  O   LEU A 203      14.546  11.001   5.746  1.00 11.90           O  
-ATOM   1352  CB  LEU A 203      16.278   9.762   3.687  1.00 11.94           C  
-ATOM   1353  CG  LEU A 203      17.235   9.484   2.526  1.00 11.83           C  
-ATOM   1354  CD1 LEU A 203      18.429   8.669   3.014  1.00 11.18           C  
-ATOM   1355  CD2 LEU A 203      16.511   8.769   1.387  1.00 12.06           C  
-ATOM   1356  N   GLY A 204      12.929  10.526   4.251  1.00 11.84           N  
-ATOM   1357  CA  GLY A 204      11.900  10.344   5.271  1.00 12.11           C  
-ATOM   1358  C   GLY A 204      11.471   8.890   5.319  1.00 11.88           C  
-ATOM   1359  O   GLY A 204      11.548   8.187   4.305  1.00 12.39           O  
-ATOM   1360  N   TRP A 205      11.029   8.437   6.487  1.00 11.68           N  
-ATOM   1361  CA  TRP A 205      10.471   7.092   6.616  1.00 11.68           C  
-ATOM   1362  C   TRP A 205       9.429   6.949   7.721  1.00 11.46           C  
-ATOM   1363  O   TRP A 205       9.416   7.723   8.678  1.00 11.65           O  
-ATOM   1364  CB  TRP A 205      11.576   6.022   6.764  1.00 11.18           C  
-ATOM   1365  CG  TRP A 205      12.476   6.172   7.954  1.00 11.52           C  
-ATOM   1366  CD1 TRP A 205      12.319   5.589   9.183  1.00 11.31           C  
-ATOM   1367  CD2 TRP A 205      13.688   6.933   8.027  1.00 11.04           C  
-ATOM   1368  NE1 TRP A 205      13.353   5.947  10.015  1.00 11.88           N  
-ATOM   1369  CE2 TRP A 205      14.205   6.778   9.335  1.00 12.12           C  
-ATOM   1370  CE3 TRP A 205      14.386   7.746   7.122  1.00 12.40           C  
-ATOM   1371  CZ2 TRP A 205      15.390   7.399   9.759  1.00 11.27           C  
-ATOM   1372  CZ3 TRP A 205      15.570   8.363   7.544  1.00 11.78           C  
-ATOM   1373  CH2 TRP A 205      16.052   8.185   8.854  1.00 11.54           C  
-ATOM   1374  N   GLU A 206       8.535   5.976   7.546  1.00 11.69           N  
-ATOM   1375  CA  GLU A 206       7.698   5.454   8.629  1.00 12.08           C  
-ATOM   1376  C   GLU A 206       8.148   4.012   8.852  1.00 12.10           C  
-ATOM   1377  O   GLU A 206       8.423   3.311   7.873  1.00 11.88           O  
-ATOM   1378  CB  GLU A 206       6.213   5.474   8.250  1.00 12.38           C  
-ATOM   1379  CG  GLU A 206       5.516   6.821   8.423  1.00 13.95           C  
-ATOM   1380  CD  GLU A 206       4.986   7.073   9.834  1.00 16.11           C  
-ATOM   1381  OE1 GLU A 206       5.484   6.468  10.816  1.00 16.70           O  
-ATOM   1382  OE2 GLU A 206       4.058   7.900   9.967  1.00 16.69           O  
-ATOM   1383  N   PRO A 207       8.242   3.557  10.106  1.00 11.89           N  
-ATOM   1384  CA  PRO A 207       7.920   4.347  11.300  1.00 11.84           C  
-ATOM   1385  C   PRO A 207       9.065   5.244  11.766  1.00 11.79           C  
-ATOM   1386  O   PRO A 207      10.230   4.844  11.716  1.00 11.40           O  
-ATOM   1387  CB  PRO A 207       7.661   3.273  12.358  1.00 11.84           C  
-ATOM   1388  CG  PRO A 207       8.576   2.137  11.958  1.00 11.93           C  
-ATOM   1389  CD  PRO A 207       8.669   2.188  10.449  1.00 12.02           C  
-ATOM   1390  N   HIS A 208       8.713   6.450  12.210  1.00 12.04           N  
-ATOM   1391  CA  HIS A 208       9.652   7.370  12.857  1.00 11.94           C  
-ATOM   1392  C   HIS A 208       8.902   8.576  13.440  1.00 12.48           C  
-ATOM   1393  O   HIS A 208       7.987   9.094  12.797  1.00 12.92           O  
-ATOM   1394  CB  HIS A 208      10.746   7.836  11.889  1.00 11.83           C  
-ATOM   1395  CG  HIS A 208      11.905   8.489  12.571  1.00 10.74           C  
-ATOM   1396  ND1 HIS A 208      11.850   9.779  13.050  1.00  9.65           N  
-ATOM   1397  CD2 HIS A 208      13.142   8.027  12.872  1.00 10.15           C  
-ATOM   1398  CE1 HIS A 208      13.005  10.088  13.611  1.00 10.80           C  
-ATOM   1399  NE2 HIS A 208      13.804   9.039  13.526  1.00 10.24           N  
-ATOM   1400  N   PRO A 209       9.273   9.014  14.650  1.00 12.66           N  
-ATOM   1401  CA  PRO A 209       8.702  10.234  15.252  1.00 12.90           C  
-ATOM   1402  C   PRO A 209       8.732  11.505  14.381  1.00 12.86           C  
-ATOM   1403  O   PRO A 209       7.979  12.443  14.655  1.00 12.39           O  
-ATOM   1404  CB  PRO A 209       9.555  10.433  16.514  1.00 12.90           C  
-ATOM   1405  CG  PRO A 209       9.994   9.054  16.884  1.00 12.51           C  
-ATOM   1406  CD  PRO A 209      10.225   8.356  15.564  1.00 12.51           C  
-ATOM   1407  N   MET A 210       9.577  11.536  13.351  1.00 13.34           N  
-ATOM   1408  CA  MET A 210       9.678  12.706  12.465  1.00 13.73           C  
-ATOM   1409  C   MET A 210       8.332  13.063  11.830  1.00 14.03           C  
-ATOM   1410  O   MET A 210       8.060  14.232  11.540  1.00 13.99           O  
-ATOM   1411  CB  MET A 210      10.755  12.508  11.383  1.00 13.78           C  
-ATOM   1412  CG  MET A 210      10.444  11.440  10.331  1.00 13.35           C  
-ATOM   1413  SD  MET A 210      11.648  11.392   8.987  1.00 13.72           S  
-ATOM   1414  CE  MET A 210      12.812  10.171   9.605  1.00 10.69           C  
-ATOM   1415  N   ASN A 211       7.501  12.044  11.628  1.00 14.68           N  
-ATOM   1416  CA  ASN A 211       6.192  12.192  11.003  1.00 15.25           C  
-ATOM   1417  C   ASN A 211       5.215  12.979  11.868  1.00 15.79           C  
-ATOM   1418  O   ASN A 211       4.373  13.721  11.351  1.00 16.01           O  
-ATOM   1419  CB  ASN A 211       5.635  10.812  10.648  1.00 15.10           C  
-ATOM   1420  CG  ASN A 211       6.458  10.123   9.572  1.00 15.00           C  
-ATOM   1421  OD1 ASN A 211       6.341  10.444   8.392  1.00 14.34           O  
-ATOM   1422  ND2 ASN A 211       7.308   9.181   9.980  1.00 14.70           N  
-ATOM   1423  N   ALA A 212       5.351  12.819  13.183  1.00 16.30           N  
-ATOM   1424  CA  ALA A 212       4.566  13.559  14.160  1.00 17.03           C  
-ATOM   1425  C   ALA A 212       5.251  14.856  14.600  1.00 17.66           C  
-ATOM   1426  O   ALA A 212       4.579  15.846  14.906  1.00 17.51           O  
-ATOM   1427  CB  ALA A 212       4.280  12.682  15.367  1.00 16.99           C  
-ATOM   1428  N   ASN A 213       6.583  14.838  14.643  1.00 18.15           N  
-ATOM   1429  CA  ASN A 213       7.367  15.976  15.132  1.00 18.84           C  
-ATOM   1430  C   ASN A 213       7.540  17.082  14.089  1.00 19.09           C  
-ATOM   1431  O   ASN A 213       7.701  18.250  14.440  1.00 19.34           O  
-ATOM   1432  CB  ASN A 213       8.735  15.512  15.658  1.00 18.73           C  
-ATOM   1433  CG  ASN A 213       8.626  14.642  16.904  1.00 19.14           C  
-ATOM   1434  OD1 ASN A 213       7.602  14.634  17.585  1.00 19.76           O  
-ATOM   1435  ND2 ASN A 213       9.693  13.908  17.211  1.00 19.07           N  
-ATOM   1436  N   PHE A 214       7.515  16.707  12.814  1.00 19.61           N  
-ATOM   1437  CA  PHE A 214       7.601  17.666  11.715  1.00 20.09           C  
-ATOM   1438  C   PHE A 214       6.430  17.453  10.761  1.00 20.31           C  
-ATOM   1439  O   PHE A 214       5.840  16.373  10.722  1.00 20.32           O  
-ATOM   1440  CB  PHE A 214       8.921  17.504  10.943  1.00 20.30           C  
-ATOM   1441  CG  PHE A 214      10.155  17.721  11.777  1.00 21.29           C  
-ATOM   1442  CD1 PHE A 214      10.861  16.640  12.294  1.00 21.40           C  
-ATOM   1443  CD2 PHE A 214      10.622  19.012  12.032  1.00 21.88           C  
-ATOM   1444  CE1 PHE A 214      12.010  16.838  13.068  1.00 22.57           C  
-ATOM   1445  CE2 PHE A 214      11.766  19.222  12.799  1.00 22.36           C  
-ATOM   1446  CZ  PHE A 214      12.462  18.130  13.321  1.00 21.63           C  
-ATOM   1447  N   LYS A 215       6.093  18.484   9.993  1.00 20.35           N  
-ATOM   1448  CA  LYS A 215       5.095  18.343   8.943  1.00 20.60           C  
-ATOM   1449  C   LYS A 215       5.820  18.134   7.619  1.00 20.19           C  
-ATOM   1450  O   LYS A 215       6.194  19.095   6.937  1.00 20.58           O  
-ATOM   1451  CB  LYS A 215       4.148  19.555   8.890  1.00 20.69           C  
-ATOM   1452  CG  LYS A 215       3.380  19.818  10.193  1.00 21.80           C  
-ATOM   1453  CD  LYS A 215       2.349  18.726  10.494  1.00 23.62           C  
-ATOM   1454  CE  LYS A 215       2.082  18.591  11.996  1.00 25.02           C  
-ATOM   1455  NZ  LYS A 215       3.207  17.912  12.714  1.00 26.28           N  
-ATOM   1456  N   LEU A 216       6.041  16.869   7.274  1.00 19.67           N  
-ATOM   1457  CA  LEU A 216       6.729  16.537   6.027  1.00 19.02           C  
-ATOM   1458  C   LEU A 216       5.797  16.085   4.919  1.00 18.22           C  
-ATOM   1459  O   LEU A 216       4.675  15.632   5.162  1.00 17.79           O  
-ATOM   1460  CB  LEU A 216       7.871  15.519   6.222  1.00 19.59           C  
-ATOM   1461  CG  LEU A 216       7.897  14.407   7.273  1.00 20.61           C  
-ATOM   1462  CD1 LEU A 216       8.706  13.221   6.785  1.00 21.08           C  
-ATOM   1463  CD2 LEU A 216       8.500  14.944   8.534  1.00 21.36           C  
-ATOM   1464  N   THR A 217       6.292  16.218   3.695  1.00 17.08           N  
-ATOM   1465  CA  THR A 217       5.601  15.759   2.509  1.00 16.40           C  
-ATOM   1466  C   THR A 217       6.513  14.767   1.824  1.00 15.65           C  
-ATOM   1467  O   THR A 217       7.617  15.126   1.414  1.00 15.57           O  
-ATOM   1468  CB  THR A 217       5.316  16.946   1.571  1.00 16.32           C  
-ATOM   1469  OG1 THR A 217       4.391  17.841   2.196  1.00 16.48           O  
-ATOM   1470  CG2 THR A 217       4.583  16.486   0.307  1.00 16.97           C  
-ATOM   1471  N   TYR A 218       6.064  13.517   1.725  1.00 14.71           N  
-ATOM   1472  CA  TYR A 218       6.770  12.515   0.931  1.00 14.01           C  
-ATOM   1473  C   TYR A 218       6.542  12.836  -0.540  1.00 13.78           C  
-ATOM   1474  O   TYR A 218       5.423  13.176  -0.938  1.00 13.09           O  
-ATOM   1475  CB  TYR A 218       6.270  11.107   1.263  1.00 14.04           C  
-ATOM   1476  CG  TYR A 218       6.687  10.636   2.643  1.00 13.76           C  
-ATOM   1477  CD1 TYR A 218       5.919  10.939   3.767  1.00 14.23           C  
-ATOM   1478  CD2 TYR A 218       7.854   9.892   2.822  1.00 13.15           C  
-ATOM   1479  CE1 TYR A 218       6.305  10.515   5.034  1.00 13.99           C  
-ATOM   1480  CE2 TYR A 218       8.247   9.459   4.084  1.00 13.75           C  
-ATOM   1481  CZ  TYR A 218       7.471   9.777   5.186  1.00 14.52           C  
-ATOM   1482  OH  TYR A 218       7.853   9.356   6.443  1.00 14.08           O  
-ATOM   1483  N   LEU A 219       7.606  12.747  -1.333  1.00 13.49           N  
-ATOM   1484  CA  LEU A 219       7.539  13.103  -2.750  1.00 13.58           C  
-ATOM   1485  C   LEU A 219       7.068  11.931  -3.600  1.00 13.70           C  
-ATOM   1486  O   LEU A 219       7.506  10.795  -3.399  1.00 14.22           O  
-ATOM   1487  CB  LEU A 219       8.900  13.591  -3.263  1.00 13.42           C  
-ATOM   1488  CG  LEU A 219       9.700  14.634  -2.477  1.00 13.48           C  
-ATOM   1489  CD1 LEU A 219      10.969  14.992  -3.250  1.00 12.46           C  
-ATOM   1490  CD2 LEU A 219       8.871  15.885  -2.180  1.00 12.90           C  
-ATOM   1491  N   SER A 220       6.179  12.219  -4.551  1.00 13.75           N  
-ATOM   1492  CA  SER A 220       5.759  11.240  -5.549  1.00 13.28           C  
-ATOM   1493  C   SER A 220       6.814  11.156  -6.646  1.00 13.36           C  
-ATOM   1494  O   SER A 220       7.822  11.870  -6.596  1.00 13.12           O  
-ATOM   1495  CB  SER A 220       4.397  11.622  -6.138  1.00 13.71           C  
-ATOM   1496  OG  SER A 220       4.423  12.922  -6.697  1.00 13.22           O  
-ATOM   1497  N   GLY A 221       6.596  10.276  -7.620  1.00 13.04           N  
-ATOM   1498  CA  GLY A 221       7.487  10.168  -8.775  1.00 13.23           C  
-ATOM   1499  C   GLY A 221       8.778   9.408  -8.523  1.00 13.22           C  
-ATOM   1500  O   GLY A 221       9.601   9.273  -9.426  1.00 13.08           O  
-ATOM   1501  N   GLY A 222       8.952   8.906  -7.301  1.00 13.33           N  
-ATOM   1502  CA  GLY A 222      10.138   8.121  -6.949  1.00 13.67           C  
-ATOM   1503  C   GLY A 222       9.971   6.629  -7.178  1.00 13.85           C  
-ATOM   1504  O   GLY A 222      10.863   5.840  -6.852  1.00 14.27           O  
-ATOM   1505  N   ASP A 223       8.831   6.250  -7.748  1.00 13.88           N  
-ATOM   1506  CA  ASP A 223       8.448   4.846  -7.950  1.00 13.98           C  
-ATOM   1507  C   ASP A 223       9.566   3.934  -8.465  1.00 13.79           C  
-ATOM   1508  O   ASP A 223       9.724   2.809  -7.993  1.00 13.57           O  
-ATOM   1509  CB  ASP A 223       7.260   4.759  -8.912  1.00 14.38           C  
-ATOM   1510  CG  ASP A 223       6.006   5.414  -8.365  1.00 15.12           C  
-ATOM   1511  OD1 ASP A 223       6.109   6.398  -7.602  1.00 16.89           O  
-ATOM   1512  OD2 ASP A 223       4.863   5.011  -8.659  1.00 16.05           O  
-ATOM   1513  N   ASP A 224      10.331   4.422  -9.438  1.00 13.65           N  
-ATOM   1514  CA  ASP A 224      11.320   3.591 -10.123  1.00 13.82           C  
-ATOM   1515  C   ASP A 224      12.647   3.481  -9.371  1.00 14.03           C  
-ATOM   1516  O   ASP A 224      13.537   2.732  -9.777  1.00 14.42           O  
-ATOM   1517  CB  ASP A 224      11.544   4.110 -11.548  1.00 13.56           C  
-ATOM   1518  CG  ASP A 224      10.270   4.097 -12.385  1.00 12.83           C  
-ATOM   1519  OD1 ASP A 224       9.233   3.615 -11.894  1.00 11.02           O  
-ATOM   1520  OD2 ASP A 224      10.211   4.540 -13.551  1.00 13.53           O  
-ATOM   1521  N   VAL A 225      12.759   4.217  -8.265  1.00 14.30           N  
-ATOM   1522  CA  VAL A 225      13.993   4.300  -7.487  1.00 14.00           C  
-ATOM   1523  C   VAL A 225      13.784   3.746  -6.072  1.00 14.36           C  
-ATOM   1524  O   VAL A 225      14.444   2.782  -5.672  1.00 14.65           O  
-ATOM   1525  CB  VAL A 225      14.528   5.763  -7.450  1.00 13.90           C  
-ATOM   1526  CG1 VAL A 225      15.802   5.875  -6.612  1.00 13.91           C  
-ATOM   1527  CG2 VAL A 225      14.774   6.289  -8.883  1.00 13.51           C  
-ATOM   1528  N   PHE A 226      12.856   4.345  -5.333  1.00 14.13           N  
-ATOM   1529  CA  PHE A 226      12.563   3.926  -3.962  1.00 14.03           C  
-ATOM   1530  C   PHE A 226      11.369   2.974  -3.877  1.00 14.36           C  
-ATOM   1531  O   PHE A 226      11.106   2.386  -2.819  1.00 14.92           O  
-ATOM   1532  CB  PHE A 226      12.363   5.153  -3.058  1.00 13.66           C  
-ATOM   1533  CG  PHE A 226      13.652   5.784  -2.602  1.00 13.26           C  
-ATOM   1534  CD1 PHE A 226      14.338   6.671  -3.425  1.00 14.02           C  
-ATOM   1535  CD2 PHE A 226      14.187   5.484  -1.349  1.00 13.56           C  
-ATOM   1536  CE1 PHE A 226      15.541   7.248  -3.008  1.00 13.78           C  
-ATOM   1537  CE2 PHE A 226      15.387   6.061  -0.924  1.00 13.49           C  
-ATOM   1538  CZ  PHE A 226      16.061   6.943  -1.758  1.00 13.23           C  
-ATOM   1539  N   GLY A 227      10.671   2.800  -4.997  1.00 14.45           N  
-ATOM   1540  CA  GLY A 227       9.477   1.961  -5.034  1.00 14.74           C  
-ATOM   1541  C   GLY A 227       8.202   2.786  -5.051  1.00 14.85           C  
-ATOM   1542  O   GLY A 227       8.191   3.931  -4.583  1.00 15.05           O  
-ATOM   1543  N   PRO A 228       7.124   2.204  -5.577  1.00 15.10           N  
-ATOM   1544  CA  PRO A 228       5.828   2.894  -5.687  1.00 15.42           C  
-ATOM   1545  C   PRO A 228       5.163   3.141  -4.332  1.00 15.64           C  
-ATOM   1546  O   PRO A 228       5.647   2.643  -3.310  1.00 15.81           O  
-ATOM   1547  CB  PRO A 228       4.984   1.929  -6.535  1.00 15.40           C  
-ATOM   1548  CG  PRO A 228       5.609   0.587  -6.340  1.00 15.41           C  
-ATOM   1549  CD  PRO A 228       7.072   0.833  -6.117  1.00 15.09           C  
-ATOM   1550  N   ASN A 229       4.060   3.896  -4.348  1.00 15.61           N  
-ATOM   1551  CA AASN A 229       3.338   4.283  -3.131  0.50 15.59           C  
-ATOM   1552  CA BASN A 229       3.339   4.274  -3.133  0.50 15.59           C  
-ATOM   1553  C   ASN A 229       4.274   4.933  -2.106  1.00 15.45           C  
-ATOM   1554  O   ASN A 229       4.332   4.531  -0.940  1.00 15.17           O  
-ATOM   1555  CB AASN A 229       2.581   3.086  -2.527  0.50 15.73           C  
-ATOM   1556  CB BASN A 229       2.600   3.062  -2.539  0.50 15.73           C  
-ATOM   1557  CG AASN A 229       1.574   3.500  -1.457  0.50 16.09           C  
-ATOM   1558  CG BASN A 229       1.757   2.319  -3.573  0.50 16.09           C  
-ATOM   1559  OD1AASN A 229       0.898   4.523  -1.579  0.50 16.12           O  
-ATOM   1560  OD1BASN A 229       0.945   2.917  -4.283  0.50 16.25           O  
-ATOM   1561  ND2AASN A 229       1.465   2.692  -0.410  0.50 16.05           N  
-ATOM   1562  ND2BASN A 229       1.950   1.006  -3.659  0.50 16.16           N  
-ATOM   1563  N   TYR A 230       5.015   5.943  -2.561  1.00 15.19           N  
-ATOM   1564  CA  TYR A 230       5.952   6.696  -1.717  1.00 15.12           C  
-ATOM   1565  C   TYR A 230       6.966   5.782  -1.018  1.00 14.50           C  
-ATOM   1566  O   TYR A 230       7.262   5.930   0.169  1.00 14.95           O  
-ATOM   1567  CB  TYR A 230       5.191   7.609  -0.741  1.00 15.62           C  
-ATOM   1568  CG  TYR A 230       4.178   8.485  -1.451  1.00 15.84           C  
-ATOM   1569  CD1 TYR A 230       2.846   8.081  -1.591  1.00 16.47           C  
-ATOM   1570  CD2 TYR A 230       4.556   9.704  -2.011  1.00 15.72           C  
-ATOM   1571  CE1 TYR A 230       1.918   8.877  -2.265  1.00 16.79           C  
-ATOM   1572  CE2 TYR A 230       3.637  10.506  -2.680  1.00 16.29           C  
-ATOM   1573  CZ  TYR A 230       2.324  10.088  -2.808  1.00 16.84           C  
-ATOM   1574  OH  TYR A 230       1.414  10.887  -3.477  1.00 17.19           O  
-ATOM   1575  N   GLY A 231       7.497   4.833  -1.781  1.00 13.90           N  
-ATOM   1576  CA  GLY A 231       8.512   3.915  -1.280  1.00 13.24           C  
-ATOM   1577  C   GLY A 231       7.981   2.964  -0.227  1.00 12.81           C  
-ATOM   1578  O   GLY A 231       8.679   2.653   0.739  1.00 13.23           O  
-ATOM   1579  N   GLY A 232       6.740   2.512  -0.416  1.00 12.46           N  
-ATOM   1580  CA  GLY A 232       6.146   1.472   0.419  1.00 11.86           C  
-ATOM   1581  C   GLY A 232       7.147   0.354   0.628  1.00 11.80           C  
-ATOM   1582  O   GLY A 232       7.692  -0.186  -0.337  1.00 11.70           O  
-ATOM   1583  N   ALA A 233       7.399   0.020   1.892  1.00 11.20           N  
-ATOM   1584  CA  ALA A 233       8.496  -0.869   2.246  1.00 11.33           C  
-ATOM   1585  C   ALA A 233       8.099  -1.945   3.251  1.00 11.26           C  
-ATOM   1586  O   ALA A 233       7.100  -1.823   3.958  1.00 11.40           O  
-ATOM   1587  CB  ALA A 233       9.687  -0.054   2.780  1.00 11.08           C  
-ATOM   1588  N   THR A 234       8.886  -3.013   3.290  1.00 11.58           N  
-ATOM   1589  CA  THR A 234       8.745  -4.032   4.326  1.00 11.51           C  
-ATOM   1590  C   THR A 234      10.105  -4.243   4.969  1.00 11.65           C  
-ATOM   1591  O   THR A 234      11.138  -4.003   4.340  1.00 11.46           O  
-ATOM   1592  CB  THR A 234       8.207  -5.355   3.747  1.00 11.81           C  
-ATOM   1593  OG1 THR A 234       9.060  -5.796   2.686  1.00 11.15           O  
-ATOM   1594  CG2 THR A 234       6.840  -5.151   3.069  1.00 10.62           C  
-ATOM   1595  N   VAL A 235      10.108  -4.660   6.230  1.00 11.95           N  
-ATOM   1596  CA  VAL A 235      11.369  -4.889   6.935  1.00 11.76           C  
-ATOM   1597  C   VAL A 235      11.463  -6.360   7.311  1.00 11.88           C  
-ATOM   1598  O   VAL A 235      10.480  -6.965   7.733  1.00 11.90           O  
-ATOM   1599  CB  VAL A 235      11.523  -4.005   8.183  1.00 12.06           C  
-ATOM   1600  CG1 VAL A 235      12.966  -4.065   8.694  1.00 11.43           C  
-ATOM   1601  CG2 VAL A 235      11.135  -2.561   7.874  1.00 11.50           C  
-ATOM   1602  N   HIS A 236      12.653  -6.923   7.143  1.00 11.95           N  
-ATOM   1603  CA  HIS A 236      12.851  -8.357   7.259  1.00 12.57           C  
-ATOM   1604  C   HIS A 236      13.970  -8.711   8.225  1.00 12.76           C  
-ATOM   1605  O   HIS A 236      14.886  -7.914   8.473  1.00 12.71           O  
-ATOM   1606  CB  HIS A 236      13.139  -8.966   5.878  1.00 12.37           C  
-ATOM   1607  CG  HIS A 236      12.043  -8.744   4.881  1.00 13.11           C  
-ATOM   1608  ND1 HIS A 236      11.145  -9.731   4.529  1.00 12.88           N  
-ATOM   1609  CD2 HIS A 236      11.690  -7.645   4.169  1.00 12.77           C  
-ATOM   1610  CE1 HIS A 236      10.284  -9.249   3.650  1.00 11.68           C  
-ATOM   1611  NE2 HIS A 236      10.595  -7.987   3.411  1.00 12.02           N  
-ATOM   1612  N   THR A 237      13.884  -9.924   8.758  1.00 13.20           N  
-ATOM   1613  CA  THR A 237      14.903 -10.469   9.629  1.00 13.57           C  
-ATOM   1614  C   THR A 237      15.837 -11.366   8.832  1.00 13.68           C  
-ATOM   1615  O   THR A 237      15.393 -12.320   8.182  1.00 13.41           O  
-ATOM   1616  CB  THR A 237      14.228 -11.263  10.762  1.00 13.52           C  
-ATOM   1617  OG1 THR A 237      13.576 -10.346  11.643  1.00 13.63           O  
-ATOM   1618  CG2 THR A 237      15.264 -11.967  11.654  1.00 14.36           C  
-ATOM   1619  N   ASN A 238      17.131 -11.052   8.887  1.00 13.80           N  
-ATOM   1620  CA  ASN A 238      18.148 -11.888   8.263  1.00 14.39           C  
-ATOM   1621  C   ASN A 238      18.970 -12.615   9.313  1.00 14.54           C  
-ATOM   1622  O   ASN A 238      19.208 -12.089  10.403  1.00 14.19           O  
-ATOM   1623  CB  ASN A 238      19.107 -11.072   7.388  1.00 14.19           C  
-ATOM   1624  CG  ASN A 238      18.404 -10.251   6.329  1.00 14.63           C  
-ATOM   1625  OD1 ASN A 238      17.415 -10.676   5.728  1.00 15.49           O  
-ATOM   1626  ND2 ASN A 238      18.938  -9.069   6.072  1.00 13.50           N  
-ATOM   1627  N   VAL A 239      19.409 -13.821   8.968  1.00 15.06           N  
-ATOM   1628  CA  VAL A 239      20.352 -14.578   9.788  1.00 15.61           C  
-ATOM   1629  C   VAL A 239      21.469 -15.118   8.899  1.00 16.04           C  
-ATOM   1630  O   VAL A 239      21.275 -15.297   7.691  1.00 16.21           O  
-ATOM   1631  CB  VAL A 239      19.672 -15.764  10.535  1.00 15.66           C  
-ATOM   1632  CG1 VAL A 239      18.603 -15.267  11.500  1.00 16.04           C  
-ATOM   1633  CG2 VAL A 239      19.092 -16.786   9.548  1.00 16.26           C  
-ATOM   1634  N   ARG A 240      22.629 -15.383   9.495  1.00 16.35           N  
-ATOM   1635  CA  ARG A 240      23.726 -16.024   8.771  1.00 16.89           C  
-ATOM   1636  C   ARG A 240      23.365 -17.475   8.433  1.00 17.27           C  
-ATOM   1637  O   ARG A 240      22.560 -18.092   9.129  1.00 17.22           O  
-ATOM   1638  CB  ARG A 240      25.033 -15.949   9.571  1.00 16.80           C  
-ATOM   1639  CG  ARG A 240      25.053 -16.732  10.881  1.00 16.58           C  
-ATOM   1640  CD  ARG A 240      26.432 -16.802  11.525  1.00 17.10           C  
-ATOM   1641  NE  ARG A 240      26.378 -17.387  12.862  1.00 18.70           N  
-ATOM   1642  CZ  ARG A 240      26.560 -18.676  13.135  1.00 19.04           C  
-ATOM   1643  NH1 ARG A 240      26.819 -19.543  12.166  1.00 19.20           N  
-ATOM   1644  NH2 ARG A 240      26.484 -19.100  14.390  1.00 18.63           N  
-ATOM   1645  N   ALA A 241      23.955 -18.005   7.365  1.00 18.04           N  
-ATOM   1646  CA  ALA A 241      23.649 -19.359   6.896  1.00 18.79           C  
-ATOM   1647  C   ALA A 241      23.822 -20.417   7.985  1.00 19.25           C  
-ATOM   1648  O   ALA A 241      24.774 -20.373   8.768  1.00 19.38           O  
-ATOM   1649  CB  ALA A 241      24.495 -19.708   5.684  1.00 18.85           C  
-ATOM   1650  N   GLY A 242      22.878 -21.354   8.035  1.00 19.92           N  
-ATOM   1651  CA  GLY A 242      22.953 -22.491   8.950  1.00 20.31           C  
-ATOM   1652  C   GLY A 242      22.564 -22.185  10.385  1.00 20.79           C  
-ATOM   1653  O   GLY A 242      22.639 -23.061  11.240  1.00 20.93           O  
-ATOM   1654  N   TYR A 243      22.145 -20.948  10.654  1.00 21.08           N  
-ATOM   1655  CA  TYR A 243      21.805 -20.533  12.017  1.00 21.37           C  
-ATOM   1656  C   TYR A 243      20.512 -21.175  12.518  1.00 21.64           C  
-ATOM   1657  O   TYR A 243      20.342 -21.373  13.724  1.00 21.66           O  
-ATOM   1658  CB  TYR A 243      21.715 -19.007  12.110  1.00 21.44           C  
-ATOM   1659  CG  TYR A 243      21.711 -18.469  13.521  1.00 21.12           C  
-ATOM   1660  CD1 TYR A 243      22.867 -18.490  14.298  1.00 20.72           C  
-ATOM   1661  CD2 TYR A 243      20.554 -17.931  14.076  1.00 21.49           C  
-ATOM   1662  CE1 TYR A 243      22.867 -17.995  15.594  1.00 21.37           C  
-ATOM   1663  CE2 TYR A 243      20.544 -17.429  15.370  1.00 21.57           C  
-ATOM   1664  CZ  TYR A 243      21.702 -17.467  16.123  1.00 21.19           C  
-ATOM   1665  OH  TYR A 243      21.701 -16.974  17.404  1.00 21.88           O  
-ATOM   1666  N   THR A 244      19.617 -21.508  11.586  1.00 21.83           N  
-ATOM   1667  CA  THR A 244      18.326 -22.125  11.910  1.00 22.14           C  
-ATOM   1668  C   THR A 244      18.496 -23.522  12.501  1.00 22.14           C  
-ATOM   1669  O   THR A 244      17.686 -23.962  13.321  1.00 22.24           O  
-ATOM   1670  CB  THR A 244      17.402 -22.186  10.661  1.00 22.23           C  
-ATOM   1671  OG1 THR A 244      17.986 -23.036   9.664  1.00 22.80           O  
-ATOM   1672  CG2 THR A 244      17.319 -20.827   9.972  1.00 22.54           C  
-ATOM   1673  N   THR A 245      19.555 -24.208  12.077  1.00 22.06           N  
-ATOM   1674  CA  THR A 245      19.850 -25.553  12.558  1.00 22.16           C  
-ATOM   1675  C   THR A 245      20.908 -25.554  13.669  1.00 21.85           C  
-ATOM   1676  O   THR A 245      20.892 -26.419  14.546  1.00 21.75           O  
-ATOM   1677  CB  THR A 245      20.235 -26.490  11.373  1.00 22.20           C  
-ATOM   1678  OG1 THR A 245      20.334 -27.841  11.835  1.00 22.99           O  
-ATOM   1679  CG2 THR A 245      21.632 -26.188  10.830  1.00 22.41           C  
-ATOM   1680  N   GLU A 246      21.812 -24.575  13.632  1.00 21.57           N  
-ATOM   1681  CA  GLU A 246      22.850 -24.440  14.648  1.00 21.30           C  
-ATOM   1682  C   GLU A 246      22.258 -23.936  15.957  1.00 20.88           C  
-ATOM   1683  O   GLU A 246      22.601 -24.431  17.031  1.00 20.73           O  
-ATOM   1684  CB  GLU A 246      23.950 -23.485  14.180  1.00 21.60           C  
-ATOM   1685  CG  GLU A 246      25.199 -23.520  15.051  1.00 22.66           C  
-ATOM   1686  CD  GLU A 246      26.139 -22.359  14.791  1.00 24.19           C  
-ATOM   1687  OE1 GLU A 246      26.452 -22.084  13.607  1.00 24.81           O  
-ATOM   1688  OE2 GLU A 246      26.578 -21.729  15.778  1.00 25.04           O  
-ATOM   1689  N   CYS A 247      21.367 -22.952  15.855  1.00 20.16           N  
-ATOM   1690  CA  CYS A 247      20.750 -22.336  17.025  1.00 19.97           C  
-ATOM   1691  C   CYS A 247      19.218 -22.334  16.913  1.00 19.30           C  
-ATOM   1692  O   CYS A 247      18.610 -21.276  16.744  1.00 18.95           O  
-ATOM   1693  CB  CYS A 247      21.284 -20.910  17.200  1.00 20.13           C  
-ATOM   1694  SG  CYS A 247      23.061 -20.807  17.522  1.00 21.42           S  
-ATOM   1695  N   PRO A 248      18.597 -23.514  17.021  1.00 18.87           N  
-ATOM   1696  CA  PRO A 248      17.162 -23.665  16.747  1.00 18.45           C  
-ATOM   1697  C   PRO A 248      16.225 -22.931  17.714  1.00 18.18           C  
-ATOM   1698  O   PRO A 248      15.134 -22.525  17.307  1.00 17.87           O  
-ATOM   1699  CB  PRO A 248      16.942 -25.180  16.835  1.00 18.58           C  
-ATOM   1700  CG  PRO A 248      18.050 -25.680  17.688  1.00 18.73           C  
-ATOM   1701  CD  PRO A 248      19.217 -24.793  17.416  1.00 18.75           C  
-ATOM   1702  N   ASN A 249      16.631 -22.764  18.972  1.00 17.77           N  
-ATOM   1703  CA  ASN A 249      15.770 -22.086  19.945  1.00 17.68           C  
-ATOM   1704  C   ASN A 249      15.641 -20.587  19.669  1.00 17.50           C  
-ATOM   1705  O   ASN A 249      14.535 -20.049  19.641  1.00 17.30           O  
-ATOM   1706  CB  ASN A 249      16.231 -22.329  21.386  1.00 17.54           C  
-ATOM   1707  CG  ASN A 249      15.257 -21.763  22.412  1.00 17.64           C  
-ATOM   1708  OD1 ASN A 249      14.075 -22.104  22.419  1.00 17.06           O  
-ATOM   1709  ND2 ASN A 249      15.752 -20.890  23.278  1.00 17.66           N  
-ATOM   1710  N   VAL A 250      16.775 -19.924  19.462  1.00 17.52           N  
-ATOM   1711  CA  VAL A 250      16.782 -18.498  19.125  1.00 17.67           C  
-ATOM   1712  C   VAL A 250      16.166 -18.250  17.740  1.00 17.69           C  
-ATOM   1713  O   VAL A 250      15.449 -17.264  17.547  1.00 17.42           O  
-ATOM   1714  CB  VAL A 250      18.199 -17.862  19.272  1.00 17.81           C  
-ATOM   1715  CG1 VAL A 250      19.245 -18.700  18.596  1.00 18.69           C  
-ATOM   1716  CG2 VAL A 250      18.235 -16.425  18.738  1.00 17.60           C  
-ATOM   1717  N   ASP A 251      16.427 -19.158  16.797  1.00 17.68           N  
-ATOM   1718  CA  ASP A 251      15.801 -19.098  15.473  1.00 17.76           C  
-ATOM   1719  C   ASP A 251      14.279 -19.128  15.579  1.00 17.44           C  
-ATOM   1720  O   ASP A 251      13.587 -18.424  14.844  1.00 17.18           O  
-ATOM   1721  CB  ASP A 251      16.279 -20.243  14.572  1.00 18.11           C  
-ATOM   1722  CG  ASP A 251      15.472 -20.342  13.278  1.00 19.05           C  
-ATOM   1723  OD1 ASP A 251      15.474 -19.371  12.493  1.00 21.84           O  
-ATOM   1724  OD2 ASP A 251      14.803 -21.345  12.967  1.00 21.13           O  
-ATOM   1725  N   LYS A 252      13.770 -19.945  16.498  1.00 17.15           N  
-ATOM   1726  CA  LYS A 252      12.336 -20.035  16.750  1.00 17.05           C  
-ATOM   1727  C   LYS A 252      11.749 -18.669  17.122  1.00 16.62           C  
-ATOM   1728  O   LYS A 252      10.706 -18.276  16.596  1.00 16.22           O  
-ATOM   1729  CB  LYS A 252      12.050 -21.074  17.841  1.00 17.19           C  
-ATOM   1730  CG  LYS A 252      10.598 -21.519  17.943  1.00 18.67           C  
-ATOM   1731  CD  LYS A 252      10.199 -22.422  16.774  1.00 20.81           C  
-ATOM   1732  CE  LYS A 252       8.760 -22.905  16.900  1.00 21.37           C  
-ATOM   1733  NZ  LYS A 252       7.778 -21.790  16.786  1.00 22.16           N  
-ATOM   1734  N   LEU A 253      12.433 -17.954  18.016  1.00 16.38           N  
-ATOM   1735  CA  LEU A 253      12.034 -16.604  18.418  1.00 16.51           C  
-ATOM   1736  C   LEU A 253      11.988 -15.658  17.221  1.00 16.60           C  
-ATOM   1737  O   LEU A 253      11.041 -14.882  17.071  1.00 16.23           O  
-ATOM   1738  CB  LEU A 253      12.985 -16.049  19.489  1.00 16.32           C  
-ATOM   1739  CG  LEU A 253      12.762 -14.596  19.934  1.00 16.59           C  
-ATOM   1740  CD1 LEU A 253      11.431 -14.435  20.678  1.00 16.59           C  
-ATOM   1741  CD2 LEU A 253      13.927 -14.096  20.767  1.00 16.76           C  
-ATOM   1742  N   LEU A 254      13.010 -15.748  16.374  1.00 16.98           N  
-ATOM   1743  CA  LEU A 254      13.142 -14.890  15.193  1.00 17.76           C  
-ATOM   1744  C   LEU A 254      12.068 -15.194  14.147  1.00 17.87           C  
-ATOM   1745  O   LEU A 254      11.612 -14.300  13.432  1.00 17.95           O  
-ATOM   1746  CB  LEU A 254      14.550 -15.011  14.597  1.00 17.70           C  
-ATOM   1747  CG  LEU A 254      15.737 -14.700  15.523  1.00 18.42           C  
-ATOM   1748  CD1 LEU A 254      17.060 -15.054  14.851  1.00 17.92           C  
-ATOM   1749  CD2 LEU A 254      15.742 -13.243  16.006  1.00 17.13           C  
-ATOM   1750  N   GLN A 255      11.659 -16.457  14.070  1.00 17.94           N  
-ATOM   1751  CA  GLN A 255      10.523 -16.847  13.238  1.00 18.40           C  
-ATOM   1752  C   GLN A 255       9.216 -16.223  13.714  1.00 18.10           C  
-ATOM   1753  O   GLN A 255       8.313 -15.986  12.910  1.00 18.22           O  
-ATOM   1754  CB  GLN A 255      10.367 -18.369  13.202  1.00 18.32           C  
-ATOM   1755  CG  GLN A 255      11.394 -19.081  12.342  1.00 19.08           C  
-ATOM   1756  CD  GLN A 255      11.082 -20.557  12.141  1.00 19.32           C  
-ATOM   1757  OE1 GLN A 255      11.579 -21.171  11.193  1.00 21.32           O  
-ATOM   1758  NE2 GLN A 255      10.264 -21.129  13.026  1.00 19.73           N  
-ATOM   1759  N   ASN A 256       9.123 -15.967  15.019  1.00 17.85           N  
-ATOM   1760  CA  ASN A 256       7.901 -15.446  15.628  1.00 17.74           C  
-ATOM   1761  C   ASN A 256       7.863 -13.924  15.749  1.00 17.62           C  
-ATOM   1762  O   ASN A 256       6.782 -13.335  15.717  1.00 17.26           O  
-ATOM   1763  CB  ASN A 256       7.682 -16.046  17.019  1.00 17.61           C  
-ATOM   1764  CG  ASN A 256       7.610 -17.563  17.015  1.00 18.37           C  
-ATOM   1765  OD1 ASN A 256       7.325 -18.193  15.995  1.00 18.92           O  
-ATOM   1766  ND2 ASN A 256       7.863 -18.157  18.176  1.00 18.09           N  
-ATOM   1767  N   LEU A 257       9.034 -13.302  15.894  1.00 17.59           N  
-ATOM   1768  CA  LEU A 257       9.131 -11.855  16.147  1.00 17.98           C  
-ATOM   1769  C   LEU A 257       8.568 -10.999  15.018  1.00 17.77           C  
-ATOM   1770  O   LEU A 257       9.141 -10.925  13.928  1.00 17.57           O  
-ATOM   1771  CB  LEU A 257      10.572 -11.432  16.443  1.00 18.17           C  
-ATOM   1772  CG  LEU A 257      11.018 -11.171  17.882  1.00 20.05           C  
-ATOM   1773  CD1 LEU A 257      12.428 -10.600  17.860  1.00 20.15           C  
-ATOM   1774  CD2 LEU A 257      10.071 -10.220  18.630  1.00 20.87           C  
-ATOM   1775  N   SER A 258       7.440 -10.356  15.305  1.00 17.54           N  
-ATOM   1776  CA  SER A 258       6.745  -9.512  14.346  1.00 17.39           C  
-ATOM   1777  C   SER A 258       6.383  -8.187  15.008  1.00 17.00           C  
-ATOM   1778  O   SER A 258       5.873  -8.166  16.132  1.00 17.01           O  
-ATOM   1779  CB  SER A 258       5.475 -10.212  13.856  1.00 17.30           C  
-ATOM   1780  OG  SER A 258       4.769  -9.399  12.938  1.00 19.03           O  
-ATOM   1781  N   PHE A 259       6.640  -7.089  14.306  1.00 16.50           N  
-ATOM   1782  CA  PHE A 259       6.382  -5.754  14.835  1.00 16.58           C  
-ATOM   1783  C   PHE A 259       5.226  -5.072  14.097  1.00 16.25           C  
-ATOM   1784  O   PHE A 259       4.687  -5.609  13.122  1.00 16.26           O  
-ATOM   1785  CB  PHE A 259       7.652  -4.888  14.753  1.00 16.73           C  
-ATOM   1786  CG  PHE A 259       8.893  -5.556  15.299  1.00 17.30           C  
-ATOM   1787  CD1 PHE A 259       9.933  -5.918  14.450  1.00 17.72           C  
-ATOM   1788  CD2 PHE A 259       9.019  -5.825  16.661  1.00 18.04           C  
-ATOM   1789  CE1 PHE A 259      11.084  -6.536  14.943  1.00 18.00           C  
-ATOM   1790  CE2 PHE A 259      10.163  -6.443  17.164  1.00 18.44           C  
-ATOM   1791  CZ  PHE A 259      11.198  -6.802  16.307  1.00 18.20           C  
-ATOM   1792  N   SER A 260       4.850  -3.889  14.572  1.00 15.93           N  
-ATOM   1793  CA  SER A 260       3.905  -3.028  13.869  1.00 15.75           C  
-ATOM   1794  C   SER A 260       4.413  -1.592  13.899  1.00 15.78           C  
-ATOM   1795  O   SER A 260       5.227  -1.240  14.756  1.00 15.70           O  
-ATOM   1796  CB  SER A 260       2.514  -3.115  14.492  1.00 15.90           C  
-ATOM   1797  OG  SER A 260       2.493  -2.561  15.796  1.00 14.25           O  
-ATOM   1798  N   LEU A 261       3.944  -0.771  12.958  1.00 15.84           N  
-ATOM   1799  CA  LEU A 261       4.265   0.662  12.953  1.00 16.28           C  
-ATOM   1800  C   LEU A 261       3.910   1.328  14.281  1.00 16.27           C  
-ATOM   1801  O   LEU A 261       4.682   2.141  14.791  1.00 16.48           O  
-ATOM   1802  CB  LEU A 261       3.555   1.372  11.800  1.00 16.36           C  
-ATOM   1803  CG  LEU A 261       4.416   1.896  10.652  1.00 16.91           C  
-ATOM   1804  CD1 LEU A 261       5.123   0.777   9.890  1.00 17.91           C  
-ATOM   1805  CD2 LEU A 261       3.560   2.737   9.722  1.00 16.66           C  
-ATOM   1806  N  AGLN A 262       2.748   0.959  14.823  0.50 16.15           N  
-ATOM   1807  N  CGLN A 262       2.749   0.974  14.830  0.50 16.36           N  
-ATOM   1808  CA AGLN A 262       2.245   1.471  16.097  0.25 16.22           C  
-ATOM   1809  CA BGLN A 262       0.857   2.588  17.952  0.25  2.00           C  
-ATOM   1810  CA CGLN A 262       2.296   1.476  16.125  0.50 16.60           C  
-ATOM   1811  C  AGLN A 262       3.261   1.254  17.216  0.50 16.32           C  
-ATOM   1812  C  CGLN A 262       3.275   1.106  17.241  0.50 16.73           C  
-ATOM   1813  O  AGLN A 262       3.661   2.199  17.904  0.50 16.30           O  
-ATOM   1814  O  CGLN A 262       3.830   1.982  17.913  0.50 16.78           O  
-ATOM   1815  CB AGLN A 262       0.913   0.789  16.455  0.25 16.24           C  
-ATOM   1816  CB BGLN A 262       1.209   1.836  16.669  0.25  2.00           C  
-ATOM   1817  CB CGLN A 262       0.904   0.916  16.440  0.50 16.71           C  
-ATOM   1818  CG AGLN A 262       1.029  -0.347  17.483  0.50 16.49           C  
-ATOM   1819  CG CGLN A 262       0.338   1.329  17.801  0.50 17.35           C  
-ATOM   1820  CD AGLN A 262      -0.123  -1.343  17.442  0.50 16.14           C  
-ATOM   1821  CD CGLN A 262      -0.562   2.555  17.746  0.50 18.20           C  
-ATOM   1822  OE1AGLN A 262      -0.922  -1.413  18.376  0.50 15.45           O  
-ATOM   1823  OE1CGLN A 262      -1.408   2.733  18.622  0.50 18.67           O  
-ATOM   1824  NE2AGLN A 262      -0.197  -2.124  16.370  0.50 15.25           N  
-ATOM   1825  NE2CGLN A 262      -0.390   3.394  16.726  0.50 18.10           N  
-ATOM   1826  N  AMET A 263       3.680   0.005  17.389  0.50 16.18           N  
-ATOM   1827  N  BMET A 263       3.576  -0.085  17.388  0.50 14.92           N  
-ATOM   1828  CA AMET A 263       4.573  -0.343  18.490  0.50 16.40           C  
-ATOM   1829  CA BMET A 263       4.567  -0.501  18.376  0.50 15.23           C  
-ATOM   1830  C  AMET A 263       6.014   0.120  18.301  0.50 15.87           C  
-ATOM   1831  C  BMET A 263       5.876   0.276  18.249  0.50 15.17           C  
-ATOM   1832  O  AMET A 263       6.721   0.357  19.284  0.50 15.83           O  
-ATOM   1833  O  BMET A 263       6.347   0.882  19.215  0.50 15.22           O  
-ATOM   1834  CB AMET A 263       4.516  -1.844  18.800  0.50 16.45           C  
-ATOM   1835  CB BMET A 263       4.832  -2.008  18.263  0.50 15.15           C  
-ATOM   1836  CG AMET A 263       5.156  -2.769  17.783  0.50 17.06           C  
-ATOM   1837  CG BMET A 263       6.053  -2.489  19.030  0.50 15.02           C  
-ATOM   1838  SD AMET A 263       5.055  -4.487  18.310  0.50 17.96           S  
-ATOM   1839  SD BMET A 263       6.430  -4.231  18.783  0.50 15.97           S  
-ATOM   1840  CE AMET A 263       3.289  -4.788  18.198  0.50 17.73           C  
-ATOM   1841  CE BMET A 263       7.824  -4.403  19.896  0.50 14.82           C  
-ATOM   1842  N   GLU A 264       6.456   0.248  17.052  1.00 15.33           N  
-ATOM   1843  CA  GLU A 264       7.770   0.832  16.793  1.00 14.94           C  
-ATOM   1844  C   GLU A 264       7.792   2.338  17.071  1.00 15.03           C  
-ATOM   1845  O   GLU A 264       8.703   2.829  17.735  1.00 14.99           O  
-ATOM   1846  CB  GLU A 264       8.261   0.501  15.383  1.00 14.44           C  
-ATOM   1847  CG  GLU A 264       8.629  -0.971  15.218  1.00 13.96           C  
-ATOM   1848  CD  GLU A 264       9.489  -1.245  14.004  1.00 13.50           C  
-ATOM   1849  OE1 GLU A 264      10.247  -0.346  13.605  1.00 12.57           O  
-ATOM   1850  OE2 GLU A 264       9.419  -2.371  13.465  1.00 13.37           O  
-ATOM   1851  N   ASN A 265       6.773   3.048  16.590  1.00 15.07           N  
-ATOM   1852  CA  ASN A 265       6.625   4.478  16.858  1.00 15.63           C  
-ATOM   1853  C   ASN A 265       6.558   4.785  18.360  1.00 15.73           C  
-ATOM   1854  O   ASN A 265       7.099   5.797  18.811  1.00 15.76           O  
-ATOM   1855  CB  ASN A 265       5.410   5.062  16.111  1.00 15.30           C  
-ATOM   1856  CG  ASN A 265       5.764   5.584  14.718  1.00 16.37           C  
-ATOM   1857  OD1 ASN A 265       6.804   6.214  14.522  1.00 16.85           O  
-ATOM   1858  ND2 ASN A 265       4.883   5.339  13.747  1.00 17.05           N  
-ATOM   1859  N   GLU A 266       5.926   3.900  19.132  1.00 16.14           N  
-ATOM   1860  CA  GLU A 266       5.817   4.096  20.584  1.00 16.76           C  
-ATOM   1861  C   GLU A 266       7.186   4.001  21.267  1.00 16.28           C  
-ATOM   1862  O   GLU A 266       7.554   4.886  22.036  1.00 16.46           O  
-ATOM   1863  CB  GLU A 266       4.789   3.137  21.221  1.00 16.90           C  
-ATOM   1864  CG  GLU A 266       3.343   3.432  20.826  1.00 17.85           C  
-ATOM   1865  CD  GLU A 266       2.303   2.618  21.588  1.00 18.82           C  
-ATOM   1866  OE1 GLU A 266       2.548   1.435  21.924  1.00 20.81           O  
-ATOM   1867  OE2 GLU A 266       1.211   3.170  21.838  1.00 21.69           O  
-ATOM   1868  N   ILE A 267       7.943   2.946  20.969  1.00 15.84           N  
-ATOM   1869  CA  ILE A 267       9.285   2.774  21.543  1.00 15.57           C  
-ATOM   1870  C   ILE A 267      10.262   3.852  21.065  1.00 15.41           C  
-ATOM   1871  O   ILE A 267      11.039   4.393  21.861  1.00 14.85           O  
-ATOM   1872  CB  ILE A 267       9.841   1.358  21.254  1.00 15.72           C  
-ATOM   1873  CG1 ILE A 267       8.876   0.289  21.781  1.00 15.53           C  
-ATOM   1874  CG2 ILE A 267      11.225   1.191  21.875  1.00 15.79           C  
-ATOM   1875  CD1 ILE A 267       9.157  -1.129  21.297  1.00 15.83           C  
-ATOM   1876  N   MET A 268      10.217   4.159  19.769  1.00 14.93           N  
-ATOM   1877  CA  MET A 268      11.076   5.197  19.191  1.00 15.12           C  
-ATOM   1878  C   MET A 268      10.774   6.571  19.788  1.00 14.84           C  
-ATOM   1879  O   MET A 268      11.677   7.386  19.971  1.00 14.58           O  
-ATOM   1880  CB  MET A 268      10.928   5.241  17.673  1.00 15.11           C  
-ATOM   1881  CG  MET A 268      11.388   3.992  16.945  1.00 15.05           C  
-ATOM   1882  SD  MET A 268      10.885   4.034  15.200  1.00 16.23           S  
-ATOM   1883  CE  MET A 268      12.011   5.271  14.581  1.00 15.55           C  
-ATOM   1884  N   GLY A 269       9.501   6.817  20.096  1.00 14.94           N  
-ATOM   1885  CA  GLY A 269       9.095   8.028  20.807  1.00 14.74           C  
-ATOM   1886  C   GLY A 269       9.757   8.159  22.175  1.00 15.10           C  
-ATOM   1887  O   GLY A 269      10.238   9.235  22.534  1.00 14.86           O  
-ATOM   1888  N   LYS A 270       9.788   7.062  22.930  1.00 15.12           N  
-ATOM   1889  CA  LYS A 270      10.464   7.022  24.238  1.00 15.41           C  
-ATOM   1890  C   LYS A 270      11.952   7.347  24.099  1.00 15.56           C  
-ATOM   1891  O   LYS A 270      12.507   8.115  24.887  1.00 15.48           O  
-ATOM   1892  CB  LYS A 270      10.322   5.642  24.883  1.00 15.39           C  
-ATOM   1893  CG  LYS A 270       8.917   5.246  25.312  1.00 16.00           C  
-ATOM   1894  CD  LYS A 270       8.886   3.765  25.698  1.00 15.32           C  
-ATOM   1895  CE  LYS A 270       7.466   3.271  25.946  1.00 15.84           C  
-ATOM   1896  NZ  LYS A 270       6.834   3.865  27.171  1.00 14.12           N  
-ATOM   1897  N   ILE A 271      12.583   6.748  23.091  1.00 15.79           N  
-ATOM   1898  CA  ILE A 271      14.009   6.921  22.831  1.00 16.20           C  
-ATOM   1899  C   ILE A 271      14.317   8.346  22.372  1.00 16.57           C  
-ATOM   1900  O   ILE A 271      15.183   9.015  22.942  1.00 16.13           O  
-ATOM   1901  CB  ILE A 271      14.500   5.884  21.777  1.00 16.36           C  
-ATOM   1902  CG1 ILE A 271      14.422   4.465  22.350  1.00 16.05           C  
-ATOM   1903  CG2 ILE A 271      15.922   6.229  21.286  1.00 16.38           C  
-ATOM   1904  CD1 ILE A 271      14.458   3.361  21.301  1.00 16.35           C  
-ATOM   1905  N   LEU A 272      13.599   8.807  21.350  1.00 16.95           N  
-ATOM   1906  CA  LEU A 272      13.916  10.080  20.710  1.00 17.45           C  
-ATOM   1907  C   LEU A 272      13.363  11.310  21.411  1.00 17.47           C  
-ATOM   1908  O   LEU A 272      14.100  12.274  21.650  1.00 17.52           O  
-ATOM   1909  CB  LEU A 272      13.486  10.073  19.242  1.00 17.86           C  
-ATOM   1910  CG  LEU A 272      14.551   9.701  18.218  1.00 18.82           C  
-ATOM   1911  CD1 LEU A 272      13.991   9.912  16.822  1.00 19.34           C  
-ATOM   1912  CD2 LEU A 272      15.808  10.535  18.401  1.00 19.73           C  
-ATOM   1913  N   ASN A 273      12.071  11.286  21.728  1.00 17.44           N  
-ATOM   1914  CA  ASN A 273      11.422  12.438  22.357  1.00 17.78           C  
-ATOM   1915  C   ASN A 273      11.804  12.609  23.821  1.00 17.57           C  
-ATOM   1916  O   ASN A 273      11.919  13.734  24.310  1.00 17.36           O  
-ATOM   1917  CB  ASN A 273       9.899  12.353  22.218  1.00 17.69           C  
-ATOM   1918  CG  ASN A 273       9.448  12.251  20.774  1.00 18.16           C  
-ATOM   1919  OD1 ASN A 273      10.066  12.820  19.867  1.00 18.30           O  
-ATOM   1920  ND2 ASN A 273       8.361  11.521  20.550  1.00 18.91           N  
-ATOM   1921  N   ASP A 274      12.006  11.487  24.509  1.00 17.53           N  
-ATOM   1922  CA  ASP A 274      12.265  11.500  25.943  1.00 17.65           C  
-ATOM   1923  C   ASP A 274      13.689  11.066  26.315  1.00 17.44           C  
-ATOM   1924  O   ASP A 274      14.061  11.088  27.492  1.00 17.54           O  
-ATOM   1925  CB  ASP A 274      11.217  10.650  26.676  1.00 17.94           C  
-ATOM   1926  CG  ASP A 274       9.791  11.166  26.473  1.00 19.21           C  
-ATOM   1927  OD1 ASP A 274       9.608  12.372  26.196  1.00 20.62           O  
-ATOM   1928  OD2 ASP A 274       8.788  10.435  26.573  1.00 21.01           O  
-ATOM   1929  N   GLY A 275      14.478  10.677  25.312  1.00 17.07           N  
-ATOM   1930  CA  GLY A 275      15.885  10.327  25.516  1.00 16.64           C  
-ATOM   1931  C   GLY A 275      16.121   9.091  26.366  1.00 16.59           C  
-ATOM   1932  O   GLY A 275      17.164   8.966  27.015  1.00 16.26           O  
-ATOM   1933  N   GLU A 276      15.154   8.177  26.369  1.00 16.64           N  
-ATOM   1934  CA  GLU A 276      15.260   6.954  27.160  1.00 16.77           C  
-ATOM   1935  C   GLU A 276      16.256   5.979  26.553  1.00 17.01           C  
-ATOM   1936  O   GLU A 276      16.445   5.941  25.333  1.00 16.63           O  
-ATOM   1937  CB  GLU A 276      13.900   6.266  27.307  1.00 16.88           C  
-ATOM   1938  CG  GLU A 276      12.919   6.970  28.232  1.00 17.25           C  
-ATOM   1939  CD  GLU A 276      11.640   6.179  28.435  1.00 16.97           C  
-ATOM   1940  OE1 GLU A 276      11.661   4.945  28.270  1.00 18.12           O  
-ATOM   1941  OE2 GLU A 276      10.607   6.789  28.764  1.00 18.40           O  
-ATOM   1942  N   ASP A 277      16.893   5.197  27.419  1.00 17.18           N  
-ATOM   1943  CA  ASP A 277      17.716   4.073  26.989  1.00 17.86           C  
-ATOM   1944  C   ASP A 277      16.846   3.079  26.203  1.00 17.67           C  
-ATOM   1945  O   ASP A 277      15.771   2.704  26.672  1.00 17.50           O  
-ATOM   1946  CB  ASP A 277      18.332   3.386  28.210  1.00 18.19           C  
-ATOM   1947  CG  ASP A 277      19.220   2.220  27.832  1.00 19.58           C  
-ATOM   1948  OD1 ASP A 277      20.302   2.456  27.256  1.00 20.89           O  
-ATOM   1949  OD2 ASP A 277      18.910   1.036  28.063  1.00 20.89           O  
-ATOM   1950  N   PRO A 278      17.287   2.676  25.008  1.00 17.76           N  
-ATOM   1951  CA  PRO A 278      16.512   1.746  24.179  1.00 18.01           C  
-ATOM   1952  C   PRO A 278      16.074   0.469  24.909  1.00 18.20           C  
-ATOM   1953  O   PRO A 278      14.919   0.064  24.785  1.00 18.08           O  
-ATOM   1954  CB  PRO A 278      17.471   1.424  23.029  1.00 17.83           C  
-ATOM   1955  CG  PRO A 278      18.325   2.649  22.923  1.00 18.14           C  
-ATOM   1956  CD  PRO A 278      18.540   3.088  24.345  1.00 17.58           C  
-ATOM   1957  N   GLU A 279      16.971  -0.138  25.683  1.00 18.89           N  
-ATOM   1958  CA  GLU A 279      16.644  -1.374  26.399  1.00 19.67           C  
-ATOM   1959  C   GLU A 279      15.597  -1.135  27.493  1.00 19.63           C  
-ATOM   1960  O   GLU A 279      14.703  -1.963  27.694  1.00 19.61           O  
-ATOM   1961  CB  GLU A 279      17.910  -2.050  26.950  1.00 19.83           C  
-ATOM   1962  CG  GLU A 279      18.868  -2.527  25.859  1.00 20.94           C  
-ATOM   1963  CD  GLU A 279      20.255  -2.873  26.382  1.00 21.26           C  
-ATOM   1964  OE1 GLU A 279      20.420  -3.956  26.978  1.00 23.08           O  
-ATOM   1965  OE2 GLU A 279      21.192  -2.068  26.179  1.00 24.22           O  
-ATOM   1966  N   LYS A 280      15.704   0.005  28.176  1.00 19.61           N  
-ATOM   1967  CA  LYS A 280      14.715   0.423  29.174  1.00 19.56           C  
-ATOM   1968  C   LYS A 280      13.380   0.741  28.514  1.00 19.37           C  
-ATOM   1969  O   LYS A 280      12.324   0.425  29.060  1.00 19.16           O  
-ATOM   1970  CB  LYS A 280      15.208   1.648  29.947  1.00 19.83           C  
-ATOM   1971  CG  LYS A 280      16.370   1.366  30.871  1.00 20.88           C  
-ATOM   1972  CD  LYS A 280      16.402   2.354  32.025  1.00 22.60           C  
-ATOM   1973  CE  LYS A 280      17.273   1.843  33.157  1.00 23.60           C  
-ATOM   1974  NZ  LYS A 280      16.684   0.664  33.870  1.00 23.86           N  
-ATOM   1975  N   ALA A 281      13.450   1.366  27.337  1.00 19.09           N  
-ATOM   1976  CA  ALA A 281      12.273   1.741  26.556  1.00 18.93           C  
-ATOM   1977  C   ALA A 281      11.536   0.512  26.031  1.00 18.70           C  
-ATOM   1978  O   ALA A 281      10.305   0.448  26.099  1.00 18.52           O  
-ATOM   1979  CB  ALA A 281      12.672   2.663  25.403  1.00 18.98           C  
-ATOM   1980  N   ALA A 282      12.296  -0.455  25.513  1.00 18.45           N  
-ATOM   1981  CA  ALA A 282      11.732  -1.716  25.022  1.00 18.38           C  
-ATOM   1982  C   ALA A 282      11.098  -2.523  26.156  1.00 18.23           C  
-ATOM   1983  O   ALA A 282       9.966  -2.999  26.027  1.00 18.11           O  
-ATOM   1984  CB  ALA A 282      12.798  -2.537  24.307  1.00 18.21           C  
-ATOM   1985  N   ALA A 283      11.821  -2.663  27.266  1.00 18.21           N  
-ATOM   1986  CA  ALA A 283      11.306  -3.379  28.437  1.00 18.53           C  
-ATOM   1987  C   ALA A 283      10.016  -2.737  28.945  1.00 18.60           C  
-ATOM   1988  O   ALA A 283       9.052  -3.431  29.267  1.00 18.49           O  
-ATOM   1989  CB  ALA A 283      12.353  -3.426  29.546  1.00 18.52           C  
-ATOM   1990  N   ALA A 284      10.007  -1.407  28.997  1.00 18.72           N  
-ATOM   1991  CA  ALA A 284       8.833  -0.654  29.438  1.00 18.85           C  
-ATOM   1992  C   ALA A 284       7.612  -0.968  28.579  1.00 18.74           C  
-ATOM   1993  O   ALA A 284       6.527  -1.229  29.097  1.00 18.46           O  
-ATOM   1994  CB  ALA A 284       9.129   0.826  29.409  1.00 18.73           C  
-ATOM   1995  N   TRP A 285       7.801  -0.950  27.264  1.00 19.09           N  
-ATOM   1996  CA  TRP A 285       6.712  -1.205  26.327  1.00 19.36           C  
-ATOM   1997  C   TRP A 285       6.171  -2.635  26.445  1.00 19.68           C  
-ATOM   1998  O   TRP A 285       4.959  -2.850  26.385  1.00 19.82           O  
-ATOM   1999  CB  TRP A 285       7.145  -0.898  24.889  1.00 19.33           C  
-ATOM   2000  CG  TRP A 285       6.000  -0.980  23.936  1.00 19.54           C  
-ATOM   2001  CD1 TRP A 285       5.190   0.043  23.531  1.00 19.72           C  
-ATOM   2002  CD2 TRP A 285       5.509  -2.158  23.288  1.00 19.24           C  
-ATOM   2003  NE1 TRP A 285       4.232  -0.427  22.666  1.00 19.03           N  
-ATOM   2004  CE2 TRP A 285       4.406  -1.776  22.499  1.00 19.04           C  
-ATOM   2005  CE3 TRP A 285       5.895  -3.506  23.291  1.00 19.54           C  
-ATOM   2006  CZ2 TRP A 285       3.680  -2.691  21.730  1.00 19.39           C  
-ATOM   2007  CZ3 TRP A 285       5.177  -4.411  22.521  1.00 19.57           C  
-ATOM   2008  CH2 TRP A 285       4.086  -3.997  21.750  1.00 19.71           C  
-ATOM   2009  N   LEU A 286       7.072  -3.600  26.620  1.00 20.20           N  
-ATOM   2010  CA  LEU A 286       6.698  -5.013  26.769  1.00 20.62           C  
-ATOM   2011  C   LEU A 286       5.857  -5.261  28.018  1.00 20.98           C  
-ATOM   2012  O   LEU A 286       4.899  -6.043  27.984  1.00 21.11           O  
-ATOM   2013  CB  LEU A 286       7.946  -5.903  26.797  1.00 20.50           C  
-ATOM   2014  CG  LEU A 286       8.799  -6.013  25.529  1.00 20.90           C  
-ATOM   2015  CD1 LEU A 286      10.146  -6.646  25.848  1.00 21.17           C  
-ATOM   2016  CD2 LEU A 286       8.076  -6.792  24.432  1.00 21.11           C  
-ATOM   2017  N   LYS A 287       6.224  -4.596  29.114  1.00 21.49           N  
-ATOM   2018  CA  LYS A 287       5.490  -4.689  30.378  1.00 21.93           C  
-ATOM   2019  C   LYS A 287       4.096  -4.078  30.264  1.00 22.15           C  
-ATOM   2020  O   LYS A 287       3.153  -4.540  30.916  1.00 21.91           O  
-ATOM   2021  CB  LYS A 287       6.266  -3.996  31.503  1.00 22.06           C  
-ATOM   2022  CG  LYS A 287       7.472  -4.773  32.007  1.00 22.70           C  
-ATOM   2023  CD  LYS A 287       8.560  -3.834  32.514  1.00 24.41           C  
-ATOM   2024  CE  LYS A 287       9.687  -4.597  33.201  1.00 25.22           C  
-ATOM   2025  NZ  LYS A 287      10.989  -3.876  33.110  1.00 26.09           N  
-ATOM   2026  N   ASP A 288       3.986  -3.036  29.441  1.00 22.32           N  
-ATOM   2027  CA  ASP A 288       2.734  -2.322  29.217  1.00 22.77           C  
-ATOM   2028  C   ASP A 288       1.874  -3.021  28.168  1.00 23.02           C  
-ATOM   2029  O   ASP A 288       0.679  -2.746  28.056  1.00 22.97           O  
-ATOM   2030  CB  ASP A 288       3.013  -0.875  28.788  1.00 22.81           C  
-ATOM   2031  CG  ASP A 288       1.806   0.027  28.959  1.00 23.52           C  
-ATOM   2032  OD1 ASP A 288       1.242   0.070  30.075  1.00 24.24           O  
-ATOM   2033  OD2 ASP A 288       1.350   0.733  28.037  1.00 24.34           O  
-ATOM   2034  N   ASN A 289       2.488  -3.921  27.404  1.00 23.44           N  
-ATOM   2035  CA  ASN A 289       1.780  -4.702  26.386  1.00 23.94           C  
-ATOM   2036  C   ASN A 289       2.048  -6.214  26.513  1.00 24.13           C  
-ATOM   2037  O   ASN A 289       2.597  -6.828  25.588  1.00 24.28           O  
-ATOM   2038  CB  ASN A 289       2.132  -4.199  24.980  1.00 23.98           C  
-ATOM   2039  CG  ASN A 289       1.782  -2.732  24.776  1.00 24.38           C  
-ATOM   2040  OD1 ASN A 289       2.594  -1.843  25.041  1.00 25.30           O  
-ATOM   2041  ND2 ASN A 289       0.572  -2.475  24.294  1.00 24.18           N  
-ATOM   2042  N   PRO A 290       1.651  -6.812  27.642  1.00 24.19           N  
-ATOM   2043  CA  PRO A 290       2.010  -8.203  27.951  1.00 24.34           C  
-ATOM   2044  C   PRO A 290       1.467  -9.256  26.975  1.00 24.41           C  
-ATOM   2045  O   PRO A 290       2.098 -10.298  26.790  1.00 24.35           O  
-ATOM   2046  CB  PRO A 290       1.419  -8.418  29.352  1.00 24.28           C  
-ATOM   2047  CG  PRO A 290       0.333  -7.411  29.472  1.00 24.43           C  
-ATOM   2048  CD  PRO A 290       0.824  -6.217  28.710  1.00 24.21           C  
-ATOM   2049  N  AGLN A 291       0.315  -8.977  26.366  0.70 24.47           N  
-ATOM   2050  N  BGLN A 291       0.320  -8.979  26.361  0.30 24.44           N  
-ATOM   2051  CA AGLN A 291      -0.337  -9.899  25.428  0.70 24.60           C  
-ATOM   2052  CA BGLN A 291      -0.315  -9.925  25.443  0.30 24.52           C  
-ATOM   2053  C  AGLN A 291       0.492 -10.108  24.162  0.70 24.62           C  
-ATOM   2054  C  BGLN A 291       0.425 -10.063  24.111  0.30 24.57           C  
-ATOM   2055  O  AGLN A 291       0.370 -11.141  23.498  0.70 24.72           O  
-ATOM   2056  O  BGLN A 291       0.185 -11.008  23.356  0.30 24.60           O  
-ATOM   2057  CB AGLN A 291      -1.736  -9.399  25.025  0.70 24.67           C  
-ATOM   2058  CB BGLN A 291      -1.786  -9.554  25.209  0.30 24.55           C  
-ATOM   2059  CG AGLN A 291      -2.349  -8.302  25.904  0.70 24.72           C  
-ATOM   2060  CG BGLN A 291      -2.662  -9.581  26.467  0.30 24.46           C  
-ATOM   2061  CD AGLN A 291      -1.804  -6.910  25.590  0.70 24.77           C  
-ATOM   2062  CD BGLN A 291      -2.625 -10.913  27.207  0.30 24.64           C  
-ATOM   2063  OE1AGLN A 291      -1.460  -6.161  26.500  0.70 24.68           O  
-ATOM   2064  OE1BGLN A 291      -2.637 -10.939  28.439  0.30 24.64           O  
-ATOM   2065  NE2AGLN A 291      -1.722  -6.569  24.309  0.70 24.53           N  
-ATOM   2066  NE2BGLN A 291      -2.578 -12.014  26.462  0.30 24.72           N  
-ATOM   2067  N   SER A 292       1.325  -9.121  23.835  1.00 24.59           N  
-ATOM   2068  CA  SER A 292       2.104  -9.119  22.592  1.00 24.75           C  
-ATOM   2069  C   SER A 292       3.230 -10.158  22.545  1.00 24.66           C  
-ATOM   2070  O   SER A 292       3.641 -10.571  21.459  1.00 24.49           O  
-ATOM   2071  CB  SER A 292       2.669  -7.722  22.317  1.00 24.79           C  
-ATOM   2072  OG  SER A 292       3.675  -7.389  23.257  1.00 25.91           O  
-ATOM   2073  N   ILE A 293       3.725 -10.575  23.710  1.00 24.49           N  
-ATOM   2074  CA  ILE A 293       4.847 -11.524  23.766  1.00 24.51           C  
-ATOM   2075  C   ILE A 293       4.424 -12.987  23.608  1.00 24.21           C  
-ATOM   2076  O   ILE A 293       5.258 -13.844  23.312  1.00 24.15           O  
-ATOM   2077  CB  ILE A 293       5.714 -11.332  25.051  1.00 24.71           C  
-ATOM   2078  CG1 ILE A 293       4.956 -11.773  26.306  1.00 24.71           C  
-ATOM   2079  CG2 ILE A 293       6.208  -9.885  25.158  1.00 24.66           C  
-ATOM   2080  CD1 ILE A 293       5.847 -12.167  27.475  1.00 25.47           C  
-ATOM   2081  N   GLU A 294       3.139 -13.266  23.813  1.00 23.97           N  
-ATOM   2082  CA  GLU A 294       2.611 -14.627  23.679  1.00 23.84           C  
-ATOM   2083  C   GLU A 294       2.972 -15.297  22.340  1.00 23.36           C  
-ATOM   2084  O   GLU A 294       3.598 -16.359  22.352  1.00 23.43           O  
-ATOM   2085  CB  GLU A 294       1.101 -14.681  23.946  1.00 24.01           C  
-ATOM   2086  CG  GLU A 294       0.721 -15.086  25.360  1.00 25.04           C  
-ATOM   2087  CD  GLU A 294       0.493 -13.905  26.285  1.00 26.20           C  
-ATOM   2088  OE1 GLU A 294       1.376 -13.026  26.383  1.00 27.19           O  
-ATOM   2089  OE2 GLU A 294      -0.573 -13.864  26.929  1.00 26.05           O  
-ATOM   2090  N   PRO A 295       2.611 -14.693  21.200  1.00 23.03           N  
-ATOM   2091  CA  PRO A 295       2.955 -15.275  19.898  1.00 22.53           C  
-ATOM   2092  C   PRO A 295       4.462 -15.335  19.625  1.00 22.05           C  
-ATOM   2093  O   PRO A 295       4.918 -16.257  18.948  1.00 21.69           O  
-ATOM   2094  CB  PRO A 295       2.253 -14.350  18.891  1.00 22.74           C  
-ATOM   2095  CG  PRO A 295       2.021 -13.085  19.614  1.00 22.87           C  
-ATOM   2096  CD  PRO A 295       1.838 -13.446  21.048  1.00 22.92           C  
-ATOM   2097  N   TRP A 296       5.218 -14.373  20.157  1.00 21.63           N  
-ATOM   2098  CA  TRP A 296       6.669 -14.322  19.953  1.00 21.40           C  
-ATOM   2099  C   TRP A 296       7.398 -15.484  20.623  1.00 21.09           C  
-ATOM   2100  O   TRP A 296       8.398 -15.977  20.101  1.00 21.05           O  
-ATOM   2101  CB  TRP A 296       7.259 -12.993  20.441  1.00 21.95           C  
-ATOM   2102  CG  TRP A 296       6.716 -11.774  19.747  1.00 22.22           C  
-ATOM   2103  CD1 TRP A 296       6.062 -11.727  18.546  1.00 23.01           C  
-ATOM   2104  CD2 TRP A 296       6.811 -10.421  20.200  1.00 23.09           C  
-ATOM   2105  NE1 TRP A 296       5.726 -10.431  18.237  1.00 23.10           N  
-ATOM   2106  CE2 TRP A 296       6.178  -9.606  19.233  1.00 23.02           C  
-ATOM   2107  CE3 TRP A 296       7.361  -9.807  21.336  1.00 22.94           C  
-ATOM   2108  CZ2 TRP A 296       6.080  -8.217  19.365  1.00 22.74           C  
-ATOM   2109  CZ3 TRP A 296       7.262  -8.426  21.466  1.00 23.09           C  
-ATOM   2110  CH2 TRP A 296       6.627  -7.647  20.485  1.00 22.95           C  
-ATOM   2111  N   LEU A 297       6.881 -15.919  21.771  1.00 20.55           N  
-ATOM   2112  CA  LEU A 297       7.520 -16.963  22.572  1.00 20.12           C  
-ATOM   2113  C   LEU A 297       6.915 -18.350  22.354  1.00 19.75           C  
-ATOM   2114  O   LEU A 297       7.239 -19.298  23.082  1.00 19.53           O  
-ATOM   2115  CB  LEU A 297       7.492 -16.589  24.062  1.00 20.32           C  
-ATOM   2116  CG  LEU A 297       8.504 -15.571  24.618  1.00 20.69           C  
-ATOM   2117  CD1 LEU A 297       9.946 -16.051  24.440  1.00 21.88           C  
-ATOM   2118  CD2 LEU A 297       8.326 -14.180  24.022  1.00 21.89           C  
-ATOM   2119  N   SER A 298       6.052 -18.469  21.348  1.00 19.37           N  
-ATOM   2120  CA  SER A 298       5.435 -19.752  21.008  1.00 19.40           C  
-ATOM   2121  C   SER A 298       6.483 -20.739  20.495  1.00 19.15           C  
-ATOM   2122  O   SER A 298       7.149 -20.488  19.489  1.00 18.87           O  
-ATOM   2123  CB  SER A 298       4.316 -19.567  19.978  1.00 19.38           C  
-ATOM   2124  OG  SER A 298       3.735 -20.815  19.642  1.00 19.96           O  
-ATOM   2125  N   GLY A 299       6.630 -21.853  21.210  1.00 19.02           N  
-ATOM   2126  CA  GLY A 299       7.620 -22.874  20.873  1.00 18.93           C  
-ATOM   2127  C   GLY A 299       9.025 -22.515  21.318  1.00 18.93           C  
-ATOM   2128  O   GLY A 299       9.976 -23.255  21.051  1.00 18.90           O  
-ATOM   2129  N   VAL A 300       9.153 -21.381  22.004  1.00 18.96           N  
-ATOM   2130  CA  VAL A 300      10.451 -20.875  22.437  1.00 18.98           C  
-ATOM   2131  C   VAL A 300      10.733 -21.284  23.877  1.00 19.17           C  
-ATOM   2132  O   VAL A 300       9.923 -21.059  24.777  1.00 18.86           O  
-ATOM   2133  CB  VAL A 300      10.564 -19.335  22.280  1.00 18.99           C  
-ATOM   2134  CG1 VAL A 300      11.927 -18.835  22.752  1.00 19.07           C  
-ATOM   2135  CG2 VAL A 300      10.326 -18.918  20.831  1.00 18.80           C  
-ATOM   2136  N   ALA A 301      11.890 -21.906  24.071  1.00 19.50           N  
-ATOM   2137  CA  ALA A 301      12.360 -22.291  25.388  1.00 19.81           C  
-ATOM   2138  C   ALA A 301      13.362 -21.262  25.903  1.00 20.05           C  
-ATOM   2139  O   ALA A 301      13.842 -20.413  25.149  1.00 20.18           O  
-ATOM   2140  CB  ALA A 301      12.998 -23.677  25.330  1.00 19.68           C  
-ATOM   2141  N   THR A 302      13.669 -21.340  27.194  1.00 20.32           N  
-ATOM   2142  CA  THR A 302      14.769 -20.580  27.763  1.00 20.56           C  
-ATOM   2143  C   THR A 302      16.066 -21.284  27.334  1.00 20.69           C  
-ATOM   2144  O   THR A 302      16.015 -22.381  26.768  1.00 20.48           O  
-ATOM   2145  CB  THR A 302      14.605 -20.481  29.306  1.00 20.66           C  
-ATOM   2146  OG1 THR A 302      15.407 -19.415  29.820  1.00 21.75           O  
-ATOM   2147  CG2 THR A 302      15.160 -21.698  30.005  1.00 20.38           C  
-ATOM   2148  N   LYS A 303      17.217 -20.662  27.583  1.00 20.87           N  
-ATOM   2149  CA  LYS A 303      18.505 -21.233  27.165  1.00 21.24           C  
-ATOM   2150  C   LYS A 303      18.748 -22.663  27.684  1.00 21.32           C  
-ATOM   2151  O   LYS A 303      19.317 -23.493  26.967  1.00 21.38           O  
-ATOM   2152  CB  LYS A 303      19.668 -20.309  27.554  1.00 21.25           C  
-ATOM   2153  CG  LYS A 303      20.972 -20.593  26.812  1.00 21.73           C  
-ATOM   2154  CD  LYS A 303      22.183 -20.244  27.666  1.00 22.71           C  
-ATOM   2155  CE  LYS A 303      23.442 -20.929  27.150  1.00 23.48           C  
-ATOM   2156  NZ  LYS A 303      24.372 -21.317  28.259  1.00 23.83           N  
-ATOM   2157  N  AASP A 304      18.290 -22.936  28.905  0.60 21.45           N  
-ATOM   2158  N  BASP A 304      18.330 -22.948  28.917  0.40 21.43           N  
-ATOM   2159  CA AASP A 304      18.498 -24.229  29.565  0.60 21.54           C  
-ATOM   2160  CA BASP A 304      18.544 -24.279  29.498  0.40 21.50           C  
-ATOM   2161  C  AASP A 304      17.354 -25.231  29.358  0.60 21.57           C  
-ATOM   2162  C  BASP A 304      17.452 -25.299  29.146  0.40 21.55           C  
-ATOM   2163  O  AASP A 304      17.406 -26.357  29.864  0.60 21.59           O  
-ATOM   2164  O  BASP A 304      17.633 -26.502  29.353  0.40 21.59           O  
-ATOM   2165  CB AASP A 304      18.768 -24.017  31.058  0.60 21.64           C  
-ATOM   2166  CB BASP A 304      18.787 -24.208  31.019  0.40 21.56           C  
-ATOM   2167  CG AASP A 304      20.052 -23.249  31.312  0.60 21.78           C  
-ATOM   2168  CG BASP A 304      17.547 -23.808  31.815  0.40 21.61           C  
-ATOM   2169  OD1AASP A 304      19.978 -22.133  31.868  0.60 22.02           O  
-ATOM   2170  OD1BASP A 304      16.413 -24.132  31.404  0.40 21.82           O  
-ATOM   2171  OD2AASP A 304      21.179 -23.675  30.976  0.60 22.06           O  
-ATOM   2172  OD2BASP A 304      17.621 -23.181  32.893  0.40 21.62           O  
-ATOM   2173  N   GLY A 305      16.329 -24.816  28.617  1.00 21.56           N  
-ATOM   2174  CA  GLY A 305      15.228 -25.701  28.221  1.00 21.65           C  
-ATOM   2175  C   GLY A 305      13.905 -25.541  28.951  1.00 21.71           C  
-ATOM   2176  O   GLY A 305      12.963 -26.293  28.696  1.00 21.82           O  
-ATOM   2177  N   GLY A 306      13.830 -24.572  29.859  1.00 21.70           N  
-ATOM   2178  CA  GLY A 306      12.577 -24.247  30.546  1.00 21.68           C  
-ATOM   2179  C   GLY A 306      11.650 -23.463  29.635  1.00 21.73           C  
-ATOM   2180  O   GLY A 306      12.032 -23.103  28.520  1.00 21.51           O  
-ATOM   2181  N   ASP A 307      10.432 -23.197  30.106  1.00 21.72           N  
-ATOM   2182  CA  ASP A 307       9.446 -22.465  29.308  1.00 21.83           C  
-ATOM   2183  C   ASP A 307       9.833 -20.994  29.141  1.00 21.52           C  
-ATOM   2184  O   ASP A 307      10.081 -20.290  30.124  1.00 21.41           O  
-ATOM   2185  CB  ASP A 307       8.045 -22.586  29.914  1.00 22.05           C  
-ATOM   2186  CG  ASP A 307       6.987 -21.898  29.068  1.00 23.03           C  
-ATOM   2187  OD1 ASP A 307       6.544 -22.491  28.060  1.00 23.89           O  
-ATOM   2188  OD2 ASP A 307       6.541 -20.764  29.330  1.00 23.90           O  
-ATOM   2189  N   GLY A 308       9.878 -20.546  27.887  1.00 21.27           N  
-ATOM   2190  CA  GLY A 308      10.296 -19.187  27.548  1.00 21.05           C  
-ATOM   2191  C   GLY A 308       9.342 -18.110  28.027  1.00 20.98           C  
-ATOM   2192  O   GLY A 308       9.763 -17.135  28.652  1.00 20.82           O  
-ATOM   2193  N   LEU A 309       8.057 -18.295  27.733  1.00 20.96           N  
-ATOM   2194  CA  LEU A 309       7.006 -17.364  28.144  1.00 20.95           C  
-ATOM   2195  C   LEU A 309       6.979 -17.164  29.661  1.00 21.23           C  
-ATOM   2196  O   LEU A 309       6.882 -16.031  30.139  1.00 21.11           O  
-ATOM   2197  CB  LEU A 309       5.641 -17.843  27.639  1.00 20.86           C  
-ATOM   2198  CG  LEU A 309       4.421 -16.944  27.856  1.00 20.88           C  
-ATOM   2199  CD1 LEU A 309       4.516 -15.665  27.028  1.00 20.28           C  
-ATOM   2200  CD2 LEU A 309       3.145 -17.703  27.526  1.00 20.70           C  
-ATOM   2201  N   ALA A 310       7.074 -18.265  30.407  1.00 21.55           N  
-ATOM   2202  CA  ALA A 310       7.135 -18.212  31.867  1.00 22.10           C  
-ATOM   2203  C   ALA A 310       8.321 -17.371  32.341  1.00 22.48           C  
-ATOM   2204  O   ALA A 310       8.170 -16.516  33.216  1.00 22.45           O  
-ATOM   2205  CB  ALA A 310       7.206 -19.615  32.451  1.00 22.01           C  
-ATOM   2206  N   ALA A 311       9.487 -17.608  31.742  1.00 23.15           N  
-ATOM   2207  CA  ALA A 311      10.723 -16.908  32.104  1.00 23.83           C  
-ATOM   2208  C   ALA A 311      10.690 -15.415  31.771  1.00 24.28           C  
-ATOM   2209  O   ALA A 311      11.163 -14.588  32.559  1.00 24.31           O  
-ATOM   2210  CB  ALA A 311      11.923 -17.578  31.446  1.00 23.89           C  
-ATOM   2211  N   VAL A 312      10.137 -15.075  30.607  1.00 24.86           N  
-ATOM   2212  CA  VAL A 312      10.031 -13.678  30.182  1.00 25.43           C  
-ATOM   2213  C   VAL A 312       9.028 -12.911  31.058  1.00 26.00           C  
-ATOM   2214  O   VAL A 312       9.259 -11.751  31.394  1.00 26.10           O  
-ATOM   2215  CB  VAL A 312       9.690 -13.543  28.669  1.00 25.31           C  
-ATOM   2216  CG1 VAL A 312       9.473 -12.082  28.280  1.00 25.21           C  
-ATOM   2217  CG2 VAL A 312      10.795 -14.142  27.807  1.00 24.87           C  
-ATOM   2218  N   LYS A 313       7.929 -13.563  31.434  1.00 26.71           N  
-ATOM   2219  CA  LYS A 313       6.967 -12.970  32.369  1.00 27.46           C  
-ATOM   2220  C   LYS A 313       7.623 -12.627  33.708  1.00 28.02           C  
-ATOM   2221  O   LYS A 313       7.470 -11.514  34.211  1.00 28.18           O  
-ATOM   2222  CB  LYS A 313       5.771 -13.897  32.600  1.00 27.45           C  
-ATOM   2223  CG  LYS A 313       4.713 -13.875  31.505  1.00 27.45           C  
-ATOM   2224  CD  LYS A 313       3.501 -14.679  31.950  1.00 27.68           C  
-ATOM   2225  CE  LYS A 313       2.671 -15.165  30.776  1.00 27.83           C  
-ATOM   2226  NZ  LYS A 313       1.739 -16.253  31.201  1.00 27.46           N  
-ATOM   2227  N   ALA A 314       8.364 -13.584  34.265  1.00 28.64           N  
-ATOM   2228  CA  ALA A 314       9.013 -13.427  35.568  1.00 29.41           C  
-ATOM   2229  C   ALA A 314      10.112 -12.362  35.576  1.00 29.92           C  
-ATOM   2230  O   ALA A 314      10.305 -11.674  36.583  1.00 30.10           O  
-ATOM   2231  CB  ALA A 314       9.563 -14.766  36.053  1.00 29.28           C  
-ATOM   2232  N   ALA A 315      10.826 -12.234  34.460  1.00 30.52           N  
-ATOM   2233  CA  ALA A 315      11.900 -11.245  34.340  1.00 30.99           C  
-ATOM   2234  C   ALA A 315      11.347  -9.832  34.198  1.00 31.34           C  
-ATOM   2235  O   ALA A 315      11.949  -8.872  34.679  1.00 31.53           O  
-ATOM   2236  CB  ALA A 315      12.807 -11.584  33.168  1.00 30.95           C  
-ATOM   2237  N   LEU A 316      10.193  -9.721  33.543  1.00 31.76           N  
-ATOM   2238  CA  LEU A 316       9.537  -8.440  33.298  1.00 32.24           C  
-ATOM   2239  C   LEU A 316       8.477  -8.127  34.363  1.00 32.58           C  
-ATOM   2240  O   LEU A 316       7.774  -7.118  34.271  1.00 32.62           O  
-ATOM   2241  CB  LEU A 316       8.906  -8.429  31.894  1.00 32.27           C  
-ATOM   2242  CG  LEU A 316       9.737  -8.276  30.600  1.00 32.36           C  
-ATOM   2243  CD1 LEU A 316      10.210  -6.840  30.377  1.00 32.48           C  
-ATOM   2244  CD2 LEU A 316      10.920  -9.251  30.503  1.00 32.78           C  
-ATOM   2245  N   GLY A 317       8.370  -8.992  35.372  1.00 33.03           N  
-ATOM   2246  CA  GLY A 317       7.370  -8.842  36.433  1.00 33.48           C  
-ATOM   2247  C   GLY A 317       5.949  -8.865  35.900  1.00 33.85           C  
-ATOM   2248  O   GLY A 317       5.114  -8.053  36.310  1.00 33.98           O  
-ATOM   2249  N   LEU A 318       5.691  -9.801  34.985  1.00 34.13           N  
-ATOM   2250  CA  LEU A 318       4.404  -9.960  34.291  1.00 34.51           C  
-ATOM   2251  C   LEU A 318       4.284  -9.035  33.082  1.00 34.71           C  
-ATOM   2252  O   LEU A 318       4.692  -9.392  31.973  1.00 34.85           O  
-ATOM   2253  CB  LEU A 318       3.203  -9.790  35.242  1.00 34.65           C  
-ATOM   2254  CG  LEU A 318       2.671 -10.983  36.054  1.00 34.96           C  
-ATOM   2255  CD1 LEU A 318       1.977 -12.007  35.157  1.00 35.49           C  
-ATOM   2256  CD2 LEU A 318       3.757 -11.651  36.904  1.00 35.29           C  
-TER    2257      LEU A 318                                                      
-ATOM   2258  N   GLU B  29       7.302 -19.129   0.429  1.00 37.20           N  
-ATOM   2259  CA  GLU B  29       8.219 -20.220   0.867  1.00 36.93           C  
-ATOM   2260  C   GLU B  29       9.623 -20.015   0.310  1.00 36.81           C  
-ATOM   2261  O   GLU B  29       9.777 -19.706  -0.875  1.00 37.09           O  
-ATOM   2262  CB  GLU B  29       7.704 -21.582   0.399  1.00 36.98           C  
-ATOM   2263  CG  GLU B  29       6.310 -21.956   0.870  1.00 36.91           C  
-ATOM   2264  CD  GLU B  29       6.023 -23.436   0.694  1.00 36.99           C  
-ATOM   2265  OE1 GLU B  29       6.436 -24.014  -0.337  1.00 36.82           O  
-ATOM   2266  OE2 GLU B  29       5.386 -24.024   1.592  1.00 36.89           O  
-ATOM   2267  N   PRO B  30      10.641 -20.189   1.156  1.00 36.53           N  
-ATOM   2268  CA  PRO B  30      12.035 -20.229   0.701  1.00 36.26           C  
-ATOM   2269  C   PRO B  30      12.356 -21.522  -0.055  1.00 35.80           C  
-ATOM   2270  O   PRO B  30      11.520 -22.429  -0.113  1.00 36.09           O  
-ATOM   2271  CB  PRO B  30      12.828 -20.179   2.011  1.00 36.33           C  
-ATOM   2272  CG  PRO B  30      11.911 -20.777   3.022  1.00 36.44           C  
-ATOM   2273  CD  PRO B  30      10.537 -20.332   2.620  1.00 36.57           C  
-ATOM   2274  N   GLU B  31      13.562 -21.609  -0.610  1.00 35.08           N  
-ATOM   2275  CA  GLU B  31      13.955 -22.757  -1.433  1.00 34.29           C  
-ATOM   2276  C   GLU B  31      14.211 -24.030  -0.626  1.00 33.57           C  
-ATOM   2277  O   GLU B  31      14.308 -25.120  -1.195  1.00 33.60           O  
-ATOM   2278  CB  GLU B  31      15.168 -22.418  -2.309  1.00 34.38           C  
-ATOM   2279  CG  GLU B  31      14.972 -21.222  -3.238  1.00 34.85           C  
-ATOM   2280  CD  GLU B  31      13.781 -21.361  -4.178  1.00 35.25           C  
-ATOM   2281  OE1 GLU B  31      13.499 -22.486  -4.651  1.00 35.59           O  
-ATOM   2282  OE2 GLU B  31      13.129 -20.331  -4.453  1.00 35.23           O  
-ATOM   2283  N   SER B  32      14.308 -23.888   0.695  1.00 32.59           N  
-ATOM   2284  CA  SER B  32      14.447 -25.029   1.601  1.00 31.65           C  
-ATOM   2285  C   SER B  32      13.152 -25.845   1.703  1.00 30.77           C  
-ATOM   2286  O   SER B  32      13.158 -26.970   2.211  1.00 30.82           O  
-ATOM   2287  CB  SER B  32      14.885 -24.558   2.990  1.00 31.78           C  
-ATOM   2288  OG  SER B  32      13.962 -23.626   3.527  1.00 31.95           O  
-ATOM   2289  N   CYS B  33      12.053 -25.272   1.214  1.00 29.62           N  
-ATOM   2290  CA  CYS B  33      10.747 -25.931   1.218  1.00 28.37           C  
-ATOM   2291  C   CYS B  33      10.525 -26.826  -0.003  1.00 27.75           C  
-ATOM   2292  O   CYS B  33       9.649 -27.695   0.015  1.00 27.46           O  
-ATOM   2293  CB  CYS B  33       9.628 -24.890   1.298  1.00 28.30           C  
-ATOM   2294  SG  CYS B  33       9.570 -23.971   2.850  1.00 27.52           S  
-ATOM   2295  N   GLY B  34      11.317 -26.607  -1.053  1.00 26.96           N  
-ATOM   2296  CA  GLY B  34      11.177 -27.322  -2.328  1.00 26.04           C  
-ATOM   2297  C   GLY B  34      11.222 -28.838  -2.238  1.00 25.30           C  
-ATOM   2298  O   GLY B  34      10.604 -29.531  -3.048  1.00 25.23           O  
-ATOM   2299  N   THR B  35      11.964 -29.345  -1.254  1.00 24.67           N  
-ATOM   2300  CA  THR B  35      12.024 -30.778  -0.965  1.00 23.89           C  
-ATOM   2301  C   THR B  35      11.403 -31.075   0.402  1.00 23.68           C  
-ATOM   2302  O   THR B  35      11.880 -30.589   1.430  1.00 23.59           O  
-ATOM   2303  CB  THR B  35      13.484 -31.288  -1.028  1.00 23.94           C  
-ATOM   2304  OG1 THR B  35      13.997 -31.114  -2.355  1.00 23.78           O  
-ATOM   2305  CG2 THR B  35      13.543 -32.797  -0.834  1.00 23.27           C  
-ATOM   2306  N   VAL B  36      10.337 -31.874   0.401  1.00 23.13           N  
-ATOM   2307  CA  VAL B  36       9.648 -32.256   1.633  1.00 22.88           C  
-ATOM   2308  C   VAL B  36      10.140 -33.632   2.089  1.00 22.73           C  
-ATOM   2309  O   VAL B  36       9.955 -34.632   1.388  1.00 22.57           O  
-ATOM   2310  CB  VAL B  36       8.107 -32.280   1.447  1.00 22.83           C  
-ATOM   2311  CG1 VAL B  36       7.401 -32.385   2.795  1.00 22.66           C  
-ATOM   2312  CG2 VAL B  36       7.628 -31.046   0.691  1.00 22.75           C  
-ATOM   2313  N   ARG B  37      10.761 -33.671   3.266  1.00 22.60           N  
-ATOM   2314  CA  ARG B  37      11.364 -34.898   3.792  1.00 22.41           C  
-ATOM   2315  C   ARG B  37      10.430 -35.623   4.765  1.00 22.23           C  
-ATOM   2316  O   ARG B  37       9.953 -35.037   5.744  1.00 22.18           O  
-ATOM   2317  CB  ARG B  37      12.711 -34.595   4.464  1.00 22.39           C  
-ATOM   2318  CG  ARG B  37      13.724 -33.863   3.572  1.00 22.81           C  
-ATOM   2319  CD  ARG B  37      14.859 -33.191   4.334  1.00 22.60           C  
-ATOM   2320  NE  ARG B  37      14.365 -32.134   5.221  1.00 23.66           N  
-ATOM   2321  CZ  ARG B  37      15.108 -31.456   6.090  1.00 23.46           C  
-ATOM   2322  NH1 ARG B  37      16.407 -31.702   6.212  1.00 23.09           N  
-ATOM   2323  NH2 ARG B  37      14.547 -30.520   6.842  1.00 24.19           N  
-ATOM   2324  N   PHE B  38      10.183 -36.902   4.483  1.00 21.96           N  
-ATOM   2325  CA  PHE B  38       9.295 -37.747   5.289  1.00 21.94           C  
-ATOM   2326  C   PHE B  38      10.051 -38.877   5.978  1.00 21.95           C  
-ATOM   2327  O   PHE B  38      11.062 -39.363   5.464  1.00 21.90           O  
-ATOM   2328  CB  PHE B  38       8.227 -38.400   4.407  1.00 21.77           C  
-ATOM   2329  CG  PHE B  38       7.168 -37.460   3.924  1.00 21.93           C  
-ATOM   2330  CD1 PHE B  38       7.356 -36.714   2.762  1.00 21.68           C  
-ATOM   2331  CD2 PHE B  38       5.963 -37.343   4.610  1.00 21.33           C  
-ATOM   2332  CE1 PHE B  38       6.366 -35.851   2.301  1.00 21.43           C  
-ATOM   2333  CE2 PHE B  38       4.966 -36.487   4.157  1.00 21.78           C  
-ATOM   2334  CZ  PHE B  38       5.169 -35.735   3.001  1.00 21.55           C  
-ATOM   2335  N   SER B  39       9.542 -39.300   7.132  1.00 22.10           N  
-ATOM   2336  CA  SER B  39       9.900 -40.599   7.693  1.00 22.39           C  
-ATOM   2337  C   SER B  39       8.827 -41.627   7.350  1.00 22.80           C  
-ATOM   2338  O   SER B  39       7.629 -41.357   7.472  1.00 23.00           O  
-ATOM   2339  CB  SER B  39      10.071 -40.527   9.208  1.00 22.17           C  
-ATOM   2340  OG  SER B  39      10.219 -41.832   9.751  1.00 22.34           O  
-ATOM   2341  N   ASP B  40       9.280 -42.803   6.922  1.00 23.21           N  
-ATOM   2342  CA  ASP B  40       8.430 -43.952   6.629  1.00 23.78           C  
-ATOM   2343  C   ASP B  40       9.042 -45.129   7.390  1.00 23.96           C  
-ATOM   2344  O   ASP B  40      10.161 -45.536   7.096  1.00 24.09           O  
-ATOM   2345  CB  ASP B  40       8.436 -44.217   5.117  1.00 23.89           C  
-ATOM   2346  CG  ASP B  40       7.551 -45.391   4.704  1.00 24.55           C  
-ATOM   2347  OD1 ASP B  40       7.069 -46.139   5.575  1.00 23.59           O  
-ATOM   2348  OD2 ASP B  40       7.291 -45.639   3.509  1.00 26.07           O  
-ATOM   2349  N   VAL B  41       8.307 -45.678   8.356  1.00 24.52           N  
-ATOM   2350  CA  VAL B  41       8.890 -46.594   9.370  1.00 24.91           C  
-ATOM   2351  C   VAL B  41       9.482 -47.987   8.979  1.00 25.16           C  
-ATOM   2352  O   VAL B  41      10.501 -48.364   9.549  1.00 26.31           O  
-ATOM   2353  CB  VAL B  41       8.017 -46.668  10.668  1.00 24.67           C  
-ATOM   2354  CG1 VAL B  41       8.639 -47.596  11.697  1.00 24.51           C  
-ATOM   2355  CG2 VAL B  41       7.857 -45.273  11.280  1.00 24.89           C  
-ATOM   2356  N   GLY B  42       8.919 -48.766   8.052  1.00 25.31           N  
-ATOM   2357  CA  GLY B  42       7.747 -48.468   7.254  1.00 24.00           C  
-ATOM   2358  C   GLY B  42       6.808 -49.663   7.172  1.00 23.44           C  
-ATOM   2359  O   GLY B  42       6.998 -50.601   6.382  1.00 23.29           O  
-ATOM   2360  N   TRP B  43       5.786 -49.610   8.011  1.00 22.43           N  
-ATOM   2361  CA  TRP B  43       4.651 -50.509   7.946  1.00 21.64           C  
-ATOM   2362  C   TRP B  43       3.883 -50.227   6.644  1.00 21.29           C  
-ATOM   2363  O   TRP B  43       4.092 -49.189   6.006  1.00 21.00           O  
-ATOM   2364  CB  TRP B  43       3.762 -50.267   9.167  1.00 21.19           C  
-ATOM   2365  CG  TRP B  43       4.519 -49.834  10.417  1.00 20.96           C  
-ATOM   2366  CD1 TRP B  43       5.455 -50.554  11.111  1.00 20.49           C  
-ATOM   2367  CD2 TRP B  43       4.381 -48.589  11.115  1.00 20.48           C  
-ATOM   2368  NE1 TRP B  43       5.909 -49.832  12.190  1.00 20.56           N  
-ATOM   2369  CE2 TRP B  43       5.265 -48.622  12.218  1.00 20.52           C  
-ATOM   2370  CE3 TRP B  43       3.594 -47.445  10.922  1.00 20.36           C  
-ATOM   2371  CZ2 TRP B  43       5.384 -47.554  13.124  1.00 20.11           C  
-ATOM   2372  CZ3 TRP B  43       3.720 -46.379  11.817  1.00 20.83           C  
-ATOM   2373  CH2 TRP B  43       4.607 -46.446  12.905  1.00 20.46           C  
-ATOM   2374  N   THR B  44       3.002 -51.136   6.239  1.00 20.78           N  
-ATOM   2375  CA  THR B  44       2.280 -50.960   4.971  1.00 20.31           C  
-ATOM   2376  C   THR B  44       1.397 -49.702   4.976  1.00 20.19           C  
-ATOM   2377  O   THR B  44       1.294 -49.013   3.960  1.00 19.77           O  
-ATOM   2378  CB  THR B  44       1.455 -52.221   4.621  1.00 20.60           C  
-ATOM   2379  OG1 THR B  44       2.328 -53.356   4.553  1.00 18.90           O  
-ATOM   2380  CG2 THR B  44       0.879 -52.118   3.200  1.00 20.45           C  
-ATOM   2381  N   ASP B  45       0.783 -49.401   6.119  1.00 19.68           N  
-ATOM   2382  CA  ASP B  45      -0.098 -48.233   6.216  1.00 19.84           C  
-ATOM   2383  C   ASP B  45       0.666 -46.914   6.062  1.00 19.76           C  
-ATOM   2384  O   ASP B  45       0.263 -46.071   5.263  1.00 19.96           O  
-ATOM   2385  CB  ASP B  45      -0.938 -48.254   7.500  1.00 19.67           C  
-ATOM   2386  CG  ASP B  45      -0.120 -47.998   8.744  1.00 19.55           C  
-ATOM   2387  OD1 ASP B  45       0.874 -48.728   8.976  1.00 18.56           O  
-ATOM   2388  OD2 ASP B  45      -0.411 -47.085   9.546  1.00 19.91           O  
-ATOM   2389  N   ILE B  46       1.781 -46.762   6.786  1.00 19.55           N  
-ATOM   2390  CA  ILE B  46       2.599 -45.546   6.687  1.00 19.47           C  
-ATOM   2391  C   ILE B  46       3.256 -45.395   5.308  1.00 19.47           C  
-ATOM   2392  O   ILE B  46       3.409 -44.284   4.825  1.00 19.01           O  
-ATOM   2393  CB  ILE B  46       3.641 -45.423   7.854  1.00 19.30           C  
-ATOM   2394  CG1 ILE B  46       4.368 -44.070   7.820  1.00 19.29           C  
-ATOM   2395  CG2 ILE B  46       4.663 -46.547   7.825  1.00 19.64           C  
-ATOM   2396  CD1 ILE B  46       3.458 -42.863   7.849  1.00 18.77           C  
-ATOM   2397  N   THR B  47       3.632 -46.506   4.680  1.00 19.90           N  
-ATOM   2398  CA  THR B  47       4.134 -46.453   3.302  1.00 20.21           C  
-ATOM   2399  C   THR B  47       3.042 -45.957   2.358  1.00 20.07           C  
-ATOM   2400  O   THR B  47       3.307 -45.133   1.477  1.00 19.91           O  
-ATOM   2401  CB  THR B  47       4.680 -47.819   2.843  1.00 20.27           C  
-ATOM   2402  OG1 THR B  47       5.705 -48.247   3.748  1.00 21.15           O  
-ATOM   2403  CG2 THR B  47       5.437 -47.678   1.524  1.00 20.58           C  
-ATOM   2404  N   ALA B  48       1.821 -46.453   2.558  1.00 20.02           N  
-ATOM   2405  CA  ALA B  48       0.666 -46.044   1.753  1.00 19.98           C  
-ATOM   2406  C   ALA B  48       0.328 -44.557   1.899  1.00 20.00           C  
-ATOM   2407  O   ALA B  48       0.141 -43.866   0.895  1.00 20.14           O  
-ATOM   2408  CB  ALA B  48      -0.552 -46.904   2.083  1.00 19.87           C  
-ATOM   2409  N   THR B  49       0.254 -44.065   3.137  1.00 19.96           N  
-ATOM   2410  CA  THR B  49      -0.117 -42.664   3.366  1.00 20.10           C  
-ATOM   2411  C   THR B  49       0.992 -41.722   2.922  1.00 20.09           C  
-ATOM   2412  O   THR B  49       0.725 -40.663   2.346  1.00 19.96           O  
-ATOM   2413  CB  THR B  49      -0.508 -42.384   4.842  1.00 20.26           C  
-ATOM   2414  OG1 THR B  49       0.498 -42.889   5.730  1.00 21.16           O  
-ATOM   2415  CG2 THR B  49      -1.767 -43.145   5.225  1.00 20.18           C  
-ATOM   2416  N   THR B  50       2.235 -42.119   3.182  1.00 20.01           N  
-ATOM   2417  CA  THR B  50       3.394 -41.342   2.753  1.00 19.92           C  
-ATOM   2418  C   THR B  50       3.439 -41.256   1.226  1.00 19.68           C  
-ATOM   2419  O   THR B  50       3.662 -40.184   0.675  1.00 19.70           O  
-ATOM   2420  CB  THR B  50       4.690 -41.936   3.334  1.00 19.82           C  
-ATOM   2421  OG1 THR B  50       4.643 -41.843   4.764  1.00 20.28           O  
-ATOM   2422  CG2 THR B  50       5.902 -41.072   2.973  1.00 19.69           C  
-ATOM   2423  N   ALA B  51       3.199 -42.383   0.559  1.00 19.73           N  
-ATOM   2424  CA  ALA B  51       3.182 -42.438  -0.907  1.00 19.81           C  
-ATOM   2425  C   ALA B  51       2.064 -41.584  -1.512  1.00 19.96           C  
-ATOM   2426  O   ALA B  51       2.235 -40.995  -2.585  1.00 19.97           O  
-ATOM   2427  CB  ALA B  51       3.077 -43.875  -1.384  1.00 19.61           C  
-ATOM   2428  N   THR B  52       0.926 -41.530  -0.822  1.00 20.07           N  
-ATOM   2429  CA  THR B  52      -0.186 -40.663  -1.207  1.00 20.30           C  
-ATOM   2430  C   THR B  52       0.256 -39.201  -1.121  1.00 20.06           C  
-ATOM   2431  O   THR B  52       0.049 -38.426  -2.053  1.00 19.79           O  
-ATOM   2432  CB  THR B  52      -1.409 -40.913  -0.289  1.00 20.43           C  
-ATOM   2433  OG1 THR B  52      -1.828 -42.284  -0.391  1.00 21.28           O  
-ATOM   2434  CG2 THR B  52      -2.624 -40.129  -0.779  1.00 20.48           C  
-ATOM   2435  N   ALA B  53       0.878 -38.848   0.002  1.00 19.91           N  
-ATOM   2436  CA  ALA B  53       1.370 -37.494   0.242  1.00 19.79           C  
-ATOM   2437  C   ALA B  53       2.429 -37.068  -0.770  1.00 19.70           C  
-ATOM   2438  O   ALA B  53       2.391 -35.936  -1.261  1.00 19.49           O  
-ATOM   2439  CB  ALA B  53       1.899 -37.360   1.671  1.00 19.78           C  
-ATOM   2440  N   THR B  54       3.364 -37.968  -1.082  1.00 19.56           N  
-ATOM   2441  CA  THR B  54       4.431 -37.654  -2.040  1.00 19.48           C  
-ATOM   2442  C   THR B  54       3.900 -37.559  -3.469  1.00 19.48           C  
-ATOM   2443  O   THR B  54       4.394 -36.761  -4.257  1.00 19.41           O  
-ATOM   2444  CB  THR B  54       5.624 -38.645  -1.957  1.00 19.51           C  
-ATOM   2445  OG1 THR B  54       5.170 -39.988  -2.157  1.00 19.44           O  
-ATOM   2446  CG2 THR B  54       6.222 -38.662  -0.553  1.00 19.23           C  
-ATOM   2447  N   THR B  55       2.888 -38.366  -3.791  1.00 19.60           N  
-ATOM   2448  CA  THR B  55       2.235 -38.294  -5.100  1.00 19.57           C  
-ATOM   2449  C   THR B  55       1.632 -36.901  -5.299  1.00 19.48           C  
-ATOM   2450  O   THR B  55       1.868 -36.258  -6.325  1.00 19.24           O  
-ATOM   2451  CB  THR B  55       1.151 -39.389  -5.246  1.00 19.65           C  
-ATOM   2452  OG1 THR B  55       1.758 -40.685  -5.161  1.00 19.68           O  
-ATOM   2453  CG2 THR B  55       0.556 -39.387  -6.658  1.00 19.71           C  
-ATOM   2454  N   ILE B  56       0.875 -36.441  -4.302  1.00 19.43           N  
-ATOM   2455  CA  ILE B  56       0.279 -35.102  -4.318  1.00 19.54           C  
-ATOM   2456  C   ILE B  56       1.353 -34.028  -4.464  1.00 19.65           C  
-ATOM   2457  O   ILE B  56       1.262 -33.166  -5.339  1.00 19.71           O  
-ATOM   2458  CB  ILE B  56      -0.563 -34.835  -3.027  1.00 19.52           C  
-ATOM   2459  CG1 ILE B  56      -1.686 -35.864  -2.857  1.00 19.91           C  
-ATOM   2460  CG2 ILE B  56      -1.129 -33.402  -3.021  1.00 19.68           C  
-ATOM   2461  CD1 ILE B  56      -2.723 -35.864  -3.949  1.00 20.33           C  
-ATOM   2462  N   LEU B  57       2.365 -34.091  -3.600  1.00 19.63           N  
-ATOM   2463  CA  LEU B  57       3.411 -33.068  -3.551  1.00 19.72           C  
-ATOM   2464  C   LEU B  57       4.202 -32.958  -4.849  1.00 19.87           C  
-ATOM   2465  O   LEU B  57       4.515 -31.851  -5.295  1.00 19.67           O  
-ATOM   2466  CB  LEU B  57       4.347 -33.306  -2.364  1.00 19.43           C  
-ATOM   2467  CG  LEU B  57       3.828 -32.819  -1.010  1.00 19.19           C  
-ATOM   2468  CD1 LEU B  57       4.639 -33.429   0.114  1.00 18.18           C  
-ATOM   2469  CD2 LEU B  57       3.841 -31.285  -0.918  1.00 19.00           C  
-ATOM   2470  N   GLU B  58       4.509 -34.102  -5.457  1.00 20.22           N  
-ATOM   2471  CA  GLU B  58       5.245 -34.116  -6.721  1.00 20.76           C  
-ATOM   2472  C   GLU B  58       4.397 -33.592  -7.881  1.00 20.86           C  
-ATOM   2473  O   GLU B  58       4.922 -32.970  -8.810  1.00 20.64           O  
-ATOM   2474  CB  GLU B  58       5.829 -35.502  -7.004  1.00 21.05           C  
-ATOM   2475  CG  GLU B  58       7.050 -35.812  -6.145  1.00 22.27           C  
-ATOM   2476  CD  GLU B  58       7.447 -37.274  -6.161  1.00 24.30           C  
-ATOM   2477  OE1 GLU B  58       7.097 -37.987  -7.126  1.00 24.98           O  
-ATOM   2478  OE2 GLU B  58       8.114 -37.711  -5.200  1.00 25.20           O  
-ATOM   2479  N   ALA B  59       3.087 -33.827  -7.811  1.00 20.92           N  
-ATOM   2480  CA  ALA B  59       2.147 -33.240  -8.770  1.00 21.31           C  
-ATOM   2481  C   ALA B  59       2.057 -31.719  -8.600  1.00 21.36           C  
-ATOM   2482  O   ALA B  59       1.731 -30.997  -9.548  1.00 21.70           O  
-ATOM   2483  CB  ALA B  59       0.775 -33.886  -8.639  1.00 21.21           C  
-ATOM   2484  N   LEU B  60       2.355 -31.246  -7.389  1.00 21.43           N  
-ATOM   2485  CA  LEU B  60       2.415 -29.816  -7.084  1.00 21.40           C  
-ATOM   2486  C   LEU B  60       3.782 -29.213  -7.422  1.00 21.59           C  
-ATOM   2487  O   LEU B  60       4.025 -28.026  -7.179  1.00 21.72           O  
-ATOM   2488  CB  LEU B  60       2.066 -29.554  -5.612  1.00 21.33           C  
-ATOM   2489  CG  LEU B  60       0.630 -29.813  -5.142  1.00 21.07           C  
-ATOM   2490  CD1 LEU B  60       0.544 -29.826  -3.629  1.00 20.88           C  
-ATOM   2491  CD2 LEU B  60      -0.329 -28.781  -5.711  1.00 20.73           C  
-ATOM   2492  N   GLY B  61       4.668 -30.028  -7.988  1.00 21.51           N  
-ATOM   2493  CA  GLY B  61       5.990 -29.559  -8.403  1.00 21.66           C  
-ATOM   2494  C   GLY B  61       7.020 -29.537  -7.290  1.00 21.67           C  
-ATOM   2495  O   GLY B  61       8.128 -29.021  -7.467  1.00 21.67           O  
-ATOM   2496  N   TYR B  62       6.653 -30.082  -6.134  1.00 21.83           N  
-ATOM   2497  CA  TYR B  62       7.600 -30.278  -5.047  1.00 22.00           C  
-ATOM   2498  C   TYR B  62       8.445 -31.513  -5.312  1.00 22.16           C  
-ATOM   2499  O   TYR B  62       8.060 -32.390  -6.085  1.00 22.22           O  
-ATOM   2500  CB  TYR B  62       6.876 -30.445  -3.709  1.00 22.03           C  
-ATOM   2501  CG  TYR B  62       6.292 -29.174  -3.145  1.00 22.19           C  
-ATOM   2502  CD1 TYR B  62       4.970 -28.816  -3.407  1.00 22.48           C  
-ATOM   2503  CD2 TYR B  62       7.059 -28.331  -2.340  1.00 22.30           C  
-ATOM   2504  CE1 TYR B  62       4.428 -27.648  -2.884  1.00 22.27           C  
-ATOM   2505  CE2 TYR B  62       6.531 -27.161  -1.818  1.00 22.13           C  
-ATOM   2506  CZ  TYR B  62       5.214 -26.827  -2.091  1.00 22.42           C  
-ATOM   2507  OH  TYR B  62       4.686 -25.669  -1.573  1.00 22.22           O  
-ATOM   2508  N   GLU B  63       9.607 -31.568  -4.674  1.00 22.35           N  
-ATOM   2509  CA  GLU B  63      10.378 -32.797  -4.604  1.00 22.54           C  
-ATOM   2510  C   GLU B  63      10.128 -33.407  -3.238  1.00 22.60           C  
-ATOM   2511  O   GLU B  63       9.829 -32.691  -2.279  1.00 22.49           O  
-ATOM   2512  CB  GLU B  63      11.865 -32.515  -4.799  1.00 22.67           C  
-ATOM   2513  CG  GLU B  63      12.210 -31.976  -6.178  1.00 23.50           C  
-ATOM   2514  CD  GLU B  63      13.661 -31.556  -6.290  1.00 24.64           C  
-ATOM   2515  OE1 GLU B  63      14.540 -32.427  -6.121  1.00 25.68           O  
-ATOM   2516  OE2 GLU B  63      13.922 -30.362  -6.551  1.00 25.09           O  
-ATOM   2517  N   THR B  64      10.215 -34.730  -3.152  1.00 22.77           N  
-ATOM   2518  CA  THR B  64      10.094 -35.401  -1.866  1.00 22.87           C  
-ATOM   2519  C   THR B  64      11.283 -36.321  -1.616  1.00 22.90           C  
-ATOM   2520  O   THR B  64      11.978 -36.729  -2.547  1.00 22.68           O  
-ATOM   2521  CB  THR B  64       8.763 -36.195  -1.748  1.00 22.86           C  
-ATOM   2522  OG1 THR B  64       8.758 -37.283  -2.680  1.00 23.22           O  
-ATOM   2523  CG2 THR B  64       7.564 -35.352  -2.168  1.00 22.77           C  
-ATOM   2524  N   ASP B  65      11.509 -36.625  -0.343  1.00 22.96           N  
-ATOM   2525  CA  ASP B  65      12.485 -37.620   0.064  1.00 23.22           C  
-ATOM   2526  C   ASP B  65      11.895 -38.430   1.207  1.00 23.12           C  
-ATOM   2527  O   ASP B  65      11.432 -37.867   2.201  1.00 23.20           O  
-ATOM   2528  CB  ASP B  65      13.789 -36.959   0.509  1.00 23.49           C  
-ATOM   2529  CG  ASP B  65      14.864 -37.973   0.859  1.00 24.33           C  
-ATOM   2530  OD1 ASP B  65      15.368 -38.658  -0.056  1.00 25.48           O  
-ATOM   2531  OD2 ASP B  65      15.274 -38.147   2.022  1.00 25.34           O  
-ATOM   2532  N   VAL B  66      11.910 -39.749   1.058  1.00 22.80           N  
-ATOM   2533  CA  VAL B  66      11.372 -40.637   2.079  1.00 22.80           C  
-ATOM   2534  C   VAL B  66      12.505 -41.458   2.690  1.00 22.65           C  
-ATOM   2535  O   VAL B  66      13.226 -42.159   1.981  1.00 22.52           O  
-ATOM   2536  CB  VAL B  66      10.261 -41.555   1.507  1.00 22.72           C  
-ATOM   2537  CG1 VAL B  66       9.737 -42.498   2.573  1.00 22.88           C  
-ATOM   2538  CG2 VAL B  66       9.114 -40.728   0.941  1.00 22.89           C  
-ATOM   2539  N   LYS B  67      12.666 -41.349   4.006  1.00 22.56           N  
-ATOM   2540  CA  LYS B  67      13.704 -42.092   4.721  1.00 22.32           C  
-ATOM   2541  C   LYS B  67      13.097 -43.137   5.647  1.00 22.03           C  
-ATOM   2542  O   LYS B  67      12.156 -42.845   6.391  1.00 21.88           O  
-ATOM   2543  CB  LYS B  67      14.615 -41.143   5.501  1.00 22.49           C  
-ATOM   2544  CG  LYS B  67      15.420 -40.209   4.611  1.00 23.30           C  
-ATOM   2545  CD  LYS B  67      16.801 -39.936   5.179  1.00 24.33           C  
-ATOM   2546  CE  LYS B  67      17.621 -39.062   4.233  1.00 24.61           C  
-ATOM   2547  NZ  LYS B  67      17.691 -39.621   2.844  1.00 24.54           N  
-ATOM   2548  N   VAL B  68      13.633 -44.357   5.588  1.00 21.56           N  
-ATOM   2549  CA  VAL B  68      13.135 -45.459   6.410  1.00 20.94           C  
-ATOM   2550  C   VAL B  68      13.800 -45.425   7.787  1.00 20.56           C  
-ATOM   2551  O   VAL B  68      14.987 -45.733   7.936  1.00 20.27           O  
-ATOM   2552  CB  VAL B  68      13.304 -46.850   5.733  1.00 21.04           C  
-ATOM   2553  CG1 VAL B  68      12.632 -47.931   6.571  1.00 20.83           C  
-ATOM   2554  CG2 VAL B  68      12.720 -46.845   4.321  1.00 20.88           C  
-ATOM   2555  N   LEU B  69      13.009 -45.029   8.778  1.00 20.02           N  
-ATOM   2556  CA  LEU B  69      13.488 -44.727  10.122  1.00 19.85           C  
-ATOM   2557  C   LEU B  69      12.647 -45.458  11.158  1.00 19.48           C  
-ATOM   2558  O   LEU B  69      11.444 -45.618  10.977  1.00 19.50           O  
-ATOM   2559  CB  LEU B  69      13.364 -43.220  10.374  1.00 20.04           C  
-ATOM   2560  CG  LEU B  69      14.502 -42.228  10.113  1.00 20.69           C  
-ATOM   2561  CD1 LEU B  69      15.323 -42.519   8.864  1.00 21.24           C  
-ATOM   2562  CD2 LEU B  69      13.936 -40.811  10.058  1.00 20.82           C  
-ATOM   2563  N   SER B  70      13.273 -45.873  12.255  1.00 19.13           N  
-ATOM   2564  CA  SER B  70      12.524 -46.417  13.384  1.00 18.97           C  
-ATOM   2565  C   SER B  70      11.675 -45.318  14.032  1.00 18.70           C  
-ATOM   2566  O   SER B  70      11.838 -44.131  13.726  1.00 18.58           O  
-ATOM   2567  CB  SER B  70      13.475 -47.013  14.415  1.00 18.92           C  
-ATOM   2568  OG  SER B  70      14.221 -45.991  15.045  1.00 19.40           O  
-ATOM   2569  N   VAL B  71      10.772 -45.717  14.924  1.00 18.70           N  
-ATOM   2570  CA  VAL B  71       9.964 -44.759  15.684  1.00 18.71           C  
-ATOM   2571  C   VAL B  71      10.840 -43.761  16.477  1.00 18.49           C  
-ATOM   2572  O   VAL B  71      10.692 -42.561  16.271  1.00 18.82           O  
-ATOM   2573  CB  VAL B  71       8.876 -45.454  16.570  1.00 18.62           C  
-ATOM   2574  CG1 VAL B  71       8.129 -44.438  17.438  1.00 18.92           C  
-ATOM   2575  CG2 VAL B  71       7.890 -46.226  15.700  1.00 18.82           C  
-ATOM   2576  N   PRO B  72      11.757 -44.219  17.344  1.00 18.43           N  
-ATOM   2577  CA  PRO B  72      12.590 -43.281  18.115  1.00 18.23           C  
-ATOM   2578  C   PRO B  72      13.424 -42.357  17.222  1.00 18.30           C  
-ATOM   2579  O   PRO B  72      13.535 -41.156  17.506  1.00 18.14           O  
-ATOM   2580  CB  PRO B  72      13.512 -44.199  18.929  1.00 18.35           C  
-ATOM   2581  CG  PRO B  72      12.821 -45.512  18.968  1.00 18.50           C  
-ATOM   2582  CD  PRO B  72      12.088 -45.621  17.666  1.00 17.96           C  
-ATOM   2583  N   VAL B  73      13.995 -42.916  16.156  1.00 18.11           N  
-ATOM   2584  CA  VAL B  73      14.833 -42.148  15.222  1.00 18.14           C  
-ATOM   2585  C   VAL B  73      14.016 -41.114  14.436  1.00 18.03           C  
-ATOM   2586  O   VAL B  73      14.497 -40.015  14.157  1.00 18.16           O  
-ATOM   2587  CB  VAL B  73      15.630 -43.072  14.265  1.00 17.79           C  
-ATOM   2588  CG1 VAL B  73      16.349 -42.263  13.185  1.00 18.40           C  
-ATOM   2589  CG2 VAL B  73      16.636 -43.889  15.049  1.00 18.15           C  
-ATOM   2590  N   THR B  74      12.780 -41.469  14.093  1.00 17.84           N  
-ATOM   2591  CA  THR B  74      11.857 -40.526  13.463  1.00 17.68           C  
-ATOM   2592  C   THR B  74      11.777 -39.214  14.250  1.00 17.57           C  
-ATOM   2593  O   THR B  74      11.802 -38.129  13.666  1.00 17.44           O  
-ATOM   2594  CB  THR B  74      10.464 -41.168  13.330  1.00 17.49           C  
-ATOM   2595  OG1 THR B  74      10.507 -42.187  12.324  1.00 17.32           O  
-ATOM   2596  CG2 THR B  74       9.456 -40.173  12.780  1.00 17.82           C  
-ATOM   2597  N   TYR B  75      11.699 -39.327  15.574  1.00 17.59           N  
-ATOM   2598  CA  TYR B  75      11.571 -38.161  16.447  1.00 17.99           C  
-ATOM   2599  C   TYR B  75      12.879 -37.392  16.684  1.00 18.16           C  
-ATOM   2600  O   TYR B  75      12.862 -36.162  16.759  1.00 18.16           O  
-ATOM   2601  CB  TYR B  75      10.862 -38.542  17.751  1.00 18.17           C  
-ATOM   2602  CG  TYR B  75       9.392 -38.797  17.513  1.00 18.26           C  
-ATOM   2603  CD1 TYR B  75       8.885 -40.096  17.462  1.00 17.82           C  
-ATOM   2604  CD2 TYR B  75       8.518 -37.736  17.278  1.00 17.96           C  
-ATOM   2605  CE1 TYR B  75       7.535 -40.327  17.214  1.00 18.21           C  
-ATOM   2606  CE2 TYR B  75       7.175 -37.955  17.031  1.00 18.64           C  
-ATOM   2607  CZ  TYR B  75       6.688 -39.249  16.999  1.00 18.69           C  
-ATOM   2608  OH  TYR B  75       5.354 -39.458  16.749  1.00 19.20           O  
-ATOM   2609  N   THR B  76      14.005 -38.101  16.776  1.00 18.50           N  
-ATOM   2610  CA  THR B  76      15.313 -37.432  16.844  1.00 18.75           C  
-ATOM   2611  C   THR B  76      15.647 -36.695  15.540  1.00 18.61           C  
-ATOM   2612  O   THR B  76      16.281 -35.635  15.569  1.00 18.74           O  
-ATOM   2613  CB  THR B  76      16.462 -38.407  17.218  1.00 19.05           C  
-ATOM   2614  OG1 THR B  76      16.582 -39.431  16.225  1.00 19.75           O  
-ATOM   2615  CG2 THR B  76      16.141 -39.182  18.494  1.00 19.36           C  
-ATOM   2616  N   SER B  77      15.215 -37.257  14.410  1.00 18.57           N  
-ATOM   2617  CA  SER B  77      15.418 -36.646  13.090  1.00 18.54           C  
-ATOM   2618  C   SER B  77      14.543 -35.411  12.872  1.00 18.66           C  
-ATOM   2619  O   SER B  77      14.963 -34.454  12.210  1.00 18.58           O  
-ATOM   2620  CB  SER B  77      15.169 -37.665  11.975  1.00 18.61           C  
-ATOM   2621  OG  SER B  77      15.970 -38.820  12.157  1.00 18.64           O  
-ATOM   2622  N   LEU B  78      13.320 -35.451  13.402  1.00 18.50           N  
-ATOM   2623  CA  LEU B  78      12.434 -34.286  13.402  1.00 18.43           C  
-ATOM   2624  C   LEU B  78      13.016 -33.171  14.270  1.00 18.56           C  
-ATOM   2625  O   LEU B  78      13.058 -32.012  13.852  1.00 18.24           O  
-ATOM   2626  CB  LEU B  78      11.031 -34.665  13.892  1.00 18.49           C  
-ATOM   2627  CG  LEU B  78      10.042 -35.278  12.892  1.00 18.19           C  
-ATOM   2628  CD1 LEU B  78       8.901 -35.968  13.625  1.00 17.48           C  
-ATOM   2629  CD2 LEU B  78       9.496 -34.224  11.928  1.00 17.94           C  
-ATOM   2630  N   LYS B  79      13.476 -33.530  15.469  1.00 18.89           N  
-ATOM   2631  CA  LYS B  79      14.136 -32.576  16.364  1.00 19.17           C  
-ATOM   2632  C   LYS B  79      15.372 -31.969  15.700  1.00 19.55           C  
-ATOM   2633  O   LYS B  79      15.571 -30.750  15.745  1.00 19.58           O  
-ATOM   2634  CB  LYS B  79      14.499 -33.238  17.705  1.00 19.21           C  
-ATOM   2635  CG  LYS B  79      15.313 -32.359  18.665  1.00 19.39           C  
-ATOM   2636  CD  LYS B  79      15.310 -32.917  20.089  1.00 19.34           C  
-ATOM   2637  CE  LYS B  79      16.273 -32.164  21.009  1.00 19.91           C  
-ATOM   2638  NZ  LYS B  79      15.932 -30.715  21.181  1.00 19.79           N  
-ATOM   2639  N   ASN B  80      16.190 -32.817  15.079  1.00 19.79           N  
-ATOM   2640  CA  ASN B  80      17.421 -32.366  14.423  1.00 20.21           C  
-ATOM   2641  C   ASN B  80      17.198 -31.636  13.096  1.00 20.19           C  
-ATOM   2642  O   ASN B  80      18.152 -31.151  12.491  1.00 20.24           O  
-ATOM   2643  CB  ASN B  80      18.393 -33.535  14.233  1.00 20.42           C  
-ATOM   2644  CG  ASN B  80      19.322 -33.717  15.417  1.00 21.27           C  
-ATOM   2645  OD1 ASN B  80      20.083 -32.810  15.772  1.00 22.52           O  
-ATOM   2646  ND2 ASN B  80      19.280 -34.898  16.027  1.00 22.04           N  
-ATOM   2647  N   LYS B  81      15.940 -31.561  12.659  1.00 20.08           N  
-ATOM   2648  CA  LYS B  81      15.554 -30.903  11.401  1.00 20.27           C  
-ATOM   2649  C   LYS B  81      16.071 -31.658  10.163  1.00 20.36           C  
-ATOM   2650  O   LYS B  81      16.259 -31.073   9.093  1.00 19.98           O  
-ATOM   2651  CB  LYS B  81      15.962 -29.413  11.389  1.00 20.21           C  
-ATOM   2652  CG  LYS B  81      15.381 -28.600  12.554  1.00 20.19           C  
-ATOM   2653  CD  LYS B  81      15.696 -27.111  12.453  1.00 20.41           C  
-ATOM   2654  CE  LYS B  81      15.044 -26.344  13.600  1.00 20.46           C  
-ATOM   2655  NZ  LYS B  81      15.117 -24.864  13.431  1.00 20.76           N  
-ATOM   2656  N   ASP B  82      16.288 -32.963  10.329  1.00 20.66           N  
-ATOM   2657  CA  ASP B  82      16.708 -33.850   9.244  1.00 20.90           C  
-ATOM   2658  C   ASP B  82      15.517 -34.377   8.466  1.00 21.07           C  
-ATOM   2659  O   ASP B  82      15.663 -34.924   7.368  1.00 21.02           O  
-ATOM   2660  CB  ASP B  82      17.505 -35.024   9.805  1.00 21.02           C  
-ATOM   2661  CG  ASP B  82      18.907 -34.629  10.200  1.00 21.78           C  
-ATOM   2662  OD1 ASP B  82      19.440 -35.203  11.171  1.00 23.20           O  
-ATOM   2663  OD2 ASP B  82      19.549 -33.749   9.597  1.00 22.45           O  
-ATOM   2664  N   ILE B  83      14.337 -34.226   9.053  1.00 21.04           N  
-ATOM   2665  CA  ILE B  83      13.112 -34.614   8.387  1.00 21.18           C  
-ATOM   2666  C   ILE B  83      12.026 -33.586   8.719  1.00 20.76           C  
-ATOM   2667  O   ILE B  83      12.074 -32.943   9.772  1.00 20.59           O  
-ATOM   2668  CB  ILE B  83      12.767 -36.086   8.755  1.00 21.59           C  
-ATOM   2669  CG1 ILE B  83      12.713 -36.932   7.484  1.00 22.43           C  
-ATOM   2670  CG2 ILE B  83      11.508 -36.205   9.606  1.00 22.31           C  
-ATOM   2671  CD1 ILE B  83      13.463 -38.227   7.587  1.00 22.89           C  
-ATOM   2672  N   ASP B  84      11.085 -33.397   7.798  1.00 20.25           N  
-ATOM   2673  CA  ASP B  84      10.085 -32.339   7.926  1.00 19.81           C  
-ATOM   2674  C   ASP B  84       8.745 -32.839   8.461  1.00 19.54           C  
-ATOM   2675  O   ASP B  84       8.127 -32.184   9.302  1.00 19.23           O  
-ATOM   2676  CB  ASP B  84       9.870 -31.635   6.577  1.00 20.01           C  
-ATOM   2677  CG  ASP B  84      11.147 -31.034   6.016  1.00 20.05           C  
-ATOM   2678  OD1 ASP B  84      11.778 -30.206   6.706  1.00 20.51           O  
-ATOM   2679  OD2 ASP B  84      11.593 -31.326   4.887  1.00 20.03           O  
-ATOM   2680  N   VAL B  85       8.307 -33.997   7.965  1.00 18.96           N  
-ATOM   2681  CA  VAL B  85       6.951 -34.488   8.200  1.00 18.73           C  
-ATOM   2682  C   VAL B  85       6.956 -35.974   8.568  1.00 18.62           C  
-ATOM   2683  O   VAL B  85       7.770 -36.742   8.053  1.00 18.60           O  
-ATOM   2684  CB  VAL B  85       6.042 -34.278   6.947  1.00 18.81           C  
-ATOM   2685  CG1 VAL B  85       4.579 -34.534   7.281  1.00 18.33           C  
-ATOM   2686  CG2 VAL B  85       6.206 -32.868   6.359  1.00 18.68           C  
-ATOM   2687  N   PHE B  86       6.045 -36.355   9.466  1.00 18.66           N  
-ATOM   2688  CA  PHE B  86       5.772 -37.754   9.798  1.00 18.71           C  
-ATOM   2689  C   PHE B  86       4.262 -37.956   9.901  1.00 18.60           C  
-ATOM   2690  O   PHE B  86       3.590 -37.285  10.684  1.00 18.10           O  
-ATOM   2691  CB  PHE B  86       6.463 -38.143  11.112  1.00 18.76           C  
-ATOM   2692  CG  PHE B  86       6.210 -39.570  11.554  1.00 19.36           C  
-ATOM   2693  CD1 PHE B  86       6.378 -40.636  10.676  1.00 19.59           C  
-ATOM   2694  CD2 PHE B  86       5.834 -39.842  12.867  1.00 19.83           C  
-ATOM   2695  CE1 PHE B  86       6.156 -41.952  11.091  1.00 19.78           C  
-ATOM   2696  CE2 PHE B  86       5.618 -41.158  13.294  1.00 20.18           C  
-ATOM   2697  CZ  PHE B  86       5.781 -42.209  12.406  1.00 20.07           C  
-ATOM   2698  N   LEU B  87       3.742 -38.886   9.101  1.00 18.55           N  
-ATOM   2699  CA  LEU B  87       2.307 -39.167   9.046  1.00 18.59           C  
-ATOM   2700  C   LEU B  87       1.859 -40.301   9.976  1.00 18.54           C  
-ATOM   2701  O   LEU B  87       0.672 -40.648  10.006  1.00 18.58           O  
-ATOM   2702  CB  LEU B  87       1.905 -39.508   7.604  1.00 18.62           C  
-ATOM   2703  CG  LEU B  87       1.452 -38.460   6.579  1.00 19.60           C  
-ATOM   2704  CD1 LEU B  87       2.087 -37.105   6.759  1.00 20.26           C  
-ATOM   2705  CD2 LEU B  87       1.718 -38.970   5.171  1.00 19.84           C  
-ATOM   2706  N   GLY B  88       2.791 -40.879  10.729  1.00 18.33           N  
-ATOM   2707  CA  GLY B  88       2.515 -42.129  11.447  1.00 18.52           C  
-ATOM   2708  C   GLY B  88       2.464 -42.088  12.961  1.00 18.49           C  
-ATOM   2709  O   GLY B  88       2.793 -43.084  13.616  1.00 18.65           O  
-ATOM   2710  N   ASN B  89       2.063 -40.946  13.520  1.00 18.56           N  
-ATOM   2711  CA  ASN B  89       1.962 -40.783  14.979  1.00 18.35           C  
-ATOM   2712  C   ASN B  89       0.716 -41.460  15.556  1.00 18.26           C  
-ATOM   2713  O   ASN B  89      -0.341 -40.831  15.701  1.00 17.90           O  
-ATOM   2714  CB  ASN B  89       2.011 -39.291  15.365  1.00 18.23           C  
-ATOM   2715  CG  ASN B  89       1.922 -39.053  16.880  1.00 19.01           C  
-ATOM   2716  OD1 ASN B  89       2.356 -39.877  17.693  1.00 20.54           O  
-ATOM   2717  ND2 ASN B  89       1.357 -37.916  17.255  1.00 17.78           N  
-ATOM   2718  N   TRP B  90       0.853 -42.743  15.891  1.00 17.90           N  
-ATOM   2719  CA  TRP B  90      -0.240 -43.514  16.483  1.00 17.82           C  
-ATOM   2720  C   TRP B  90      -0.410 -43.177  17.965  1.00 17.83           C  
-ATOM   2721  O   TRP B  90       0.533 -43.300  18.739  1.00 17.58           O  
-ATOM   2722  CB  TRP B  90       0.002 -45.016  16.297  1.00 17.71           C  
-ATOM   2723  CG  TRP B  90      -0.324 -45.498  14.908  1.00 17.69           C  
-ATOM   2724  CD1 TRP B  90       0.302 -45.141  13.748  1.00 17.81           C  
-ATOM   2725  CD2 TRP B  90      -1.361 -46.413  14.538  1.00 17.42           C  
-ATOM   2726  NE1 TRP B  90      -0.281 -45.779  12.679  1.00 17.79           N  
-ATOM   2727  CE2 TRP B  90      -1.310 -46.562  13.135  1.00 17.97           C  
-ATOM   2728  CE3 TRP B  90      -2.337 -47.128  15.252  1.00 17.78           C  
-ATOM   2729  CZ2 TRP B  90      -2.186 -47.398  12.435  1.00 17.43           C  
-ATOM   2730  CZ3 TRP B  90      -3.204 -47.960  14.555  1.00 17.43           C  
-ATOM   2731  CH2 TRP B  90      -3.124 -48.083  13.164  1.00 17.58           C  
-ATOM   2732  N   MET B  91      -1.607 -42.735  18.351  1.00 17.84           N  
-ATOM   2733  CA  MET B  91      -1.895 -42.421  19.760  1.00 18.23           C  
-ATOM   2734  C   MET B  91      -3.056 -43.288  20.264  1.00 18.15           C  
-ATOM   2735  O   MET B  91      -4.015 -43.500  19.519  1.00 18.36           O  
-ATOM   2736  CB  MET B  91      -2.196 -40.926  19.929  1.00 18.64           C  
-ATOM   2737  CG  MET B  91      -1.015 -40.012  19.579  1.00 19.84           C  
-ATOM   2738  SD  MET B  91       0.402 -40.163  20.701  1.00 21.32           S  
-ATOM   2739  CE  MET B  91      -0.151 -39.138  22.064  1.00 21.77           C  
-ATOM   2740  N   PRO B  92      -3.015 -43.759  21.517  1.00 17.98           N  
-ATOM   2741  CA  PRO B  92      -2.075 -43.307  22.546  1.00 17.90           C  
-ATOM   2742  C   PRO B  92      -0.727 -44.042  22.700  1.00 17.88           C  
-ATOM   2743  O   PRO B  92       0.069 -43.632  23.549  1.00 18.03           O  
-ATOM   2744  CB  PRO B  92      -2.892 -43.488  23.830  1.00 17.69           C  
-ATOM   2745  CG  PRO B  92      -3.749 -44.702  23.549  1.00 18.30           C  
-ATOM   2746  CD  PRO B  92      -3.949 -44.771  22.048  1.00 17.95           C  
-ATOM   2747  N   THR B  93      -0.465 -45.093  21.918  1.00 17.58           N  
-ATOM   2748  CA  THR B  93       0.730 -45.930  22.154  1.00 17.88           C  
-ATOM   2749  C   THR B  93       2.073 -45.206  22.004  1.00 18.06           C  
-ATOM   2750  O   THR B  93       3.031 -45.537  22.707  1.00 18.26           O  
-ATOM   2751  CB  THR B  93       0.728 -47.240  21.320  1.00 17.62           C  
-ATOM   2752  OG1 THR B  93       0.542 -46.936  19.930  1.00 17.25           O  
-ATOM   2753  CG2 THR B  93      -0.472 -48.134  21.688  1.00 17.37           C  
-ATOM   2754  N   MET B  94       2.137 -44.214  21.116  1.00 18.52           N  
-ATOM   2755  CA  MET B  94       3.370 -43.433  20.920  1.00 18.84           C  
-ATOM   2756  C   MET B  94       3.593 -42.300  21.915  1.00 19.21           C  
-ATOM   2757  O   MET B  94       4.502 -41.484  21.720  1.00 19.45           O  
-ATOM   2758  CB  MET B  94       3.449 -42.869  19.500  1.00 19.16           C  
-ATOM   2759  CG  MET B  94       4.106 -43.789  18.530  1.00 19.61           C  
-ATOM   2760  SD  MET B  94       4.415 -43.018  16.938  1.00 18.64           S  
-ATOM   2761  CE  MET B  94       4.499 -44.484  15.920  1.00 19.84           C  
-ATOM   2762  N   GLU B  95       2.787 -42.251  22.975  1.00 19.41           N  
-ATOM   2763  CA  GLU B  95       2.886 -41.179  23.973  1.00 19.68           C  
-ATOM   2764  C   GLU B  95       4.297 -41.004  24.544  1.00 19.65           C  
-ATOM   2765  O   GLU B  95       4.793 -39.884  24.615  1.00 19.54           O  
-ATOM   2766  CB  GLU B  95       1.857 -41.366  25.098  1.00 19.78           C  
-ATOM   2767  CG  GLU B  95       2.056 -40.477  26.327  1.00 21.09           C  
-ATOM   2768  CD  GLU B  95       1.909 -38.983  26.060  1.00 22.49           C  
-ATOM   2769  OE1 GLU B  95       1.416 -38.590  24.981  1.00 22.73           O  
-ATOM   2770  OE2 GLU B  95       2.283 -38.187  26.954  1.00 23.45           O  
-ATOM   2771  N   ALA B  96       4.937 -42.109  24.931  1.00 19.80           N  
-ATOM   2772  CA  ALA B  96       6.280 -42.062  25.518  1.00 20.07           C  
-ATOM   2773  C   ALA B  96       7.339 -41.628  24.507  1.00 20.16           C  
-ATOM   2774  O   ALA B  96       8.358 -41.044  24.881  1.00 20.12           O  
-ATOM   2775  CB  ALA B  96       6.647 -43.407  26.144  1.00 20.12           C  
-ATOM   2776  N   ASP B  97       7.091 -41.910  23.231  1.00 20.28           N  
-ATOM   2777  CA  ASP B  97       7.999 -41.506  22.159  1.00 20.43           C  
-ATOM   2778  C   ASP B  97       7.926 -40.011  21.858  1.00 20.47           C  
-ATOM   2779  O   ASP B  97       8.955 -39.352  21.728  1.00 20.46           O  
-ATOM   2780  CB  ASP B  97       7.710 -42.300  20.890  1.00 20.46           C  
-ATOM   2781  CG  ASP B  97       7.950 -43.778  21.070  1.00 20.65           C  
-ATOM   2782  OD1 ASP B  97       9.106 -44.162  21.347  1.00 20.49           O  
-ATOM   2783  OD2 ASP B  97       7.040 -44.621  20.952  1.00 20.87           O  
-ATOM   2784  N   ILE B  98       6.711 -39.481  21.754  1.00 20.46           N  
-ATOM   2785  CA  ILE B  98       6.527 -38.080  21.373  1.00 20.66           C  
-ATOM   2786  C   ILE B  98       6.656 -37.105  22.554  1.00 20.86           C  
-ATOM   2787  O   ILE B  98       7.089 -35.962  22.372  1.00 20.76           O  
-ATOM   2788  CB  ILE B  98       5.195 -37.886  20.575  1.00 20.69           C  
-ATOM   2789  CG1 ILE B  98       5.187 -36.531  19.854  1.00 20.76           C  
-ATOM   2790  CG2 ILE B  98       3.964 -38.087  21.478  1.00 20.82           C  
-ATOM   2791  CD1 ILE B  98       4.011 -36.328  18.910  1.00 20.64           C  
-ATOM   2792  N   ALA B  99       6.316 -37.572  23.758  1.00 21.20           N  
-ATOM   2793  CA  ALA B  99       6.271 -36.720  24.956  1.00 21.41           C  
-ATOM   2794  C   ALA B  99       7.499 -35.822  25.189  1.00 21.74           C  
-ATOM   2795  O   ALA B  99       7.320 -34.626  25.429  1.00 21.67           O  
-ATOM   2796  CB  ALA B  99       5.951 -37.549  26.210  1.00 21.50           C  
-ATOM   2797  N   PRO B 100       8.726 -36.359  25.110  1.00 22.15           N  
-ATOM   2798  CA  PRO B 100       9.925 -35.538  25.339  1.00 22.53           C  
-ATOM   2799  C   PRO B 100      10.076 -34.417  24.313  1.00 22.93           C  
-ATOM   2800  O   PRO B 100      10.660 -33.373  24.615  1.00 22.95           O  
-ATOM   2801  CB  PRO B 100      11.076 -36.540  25.186  1.00 22.60           C  
-ATOM   2802  CG  PRO B 100      10.454 -37.877  25.389  1.00 22.61           C  
-ATOM   2803  CD  PRO B 100       9.085 -37.758  24.805  1.00 22.02           C  
-ATOM   2804  N   TYR B 101       9.539 -34.648  23.118  1.00 23.32           N  
-ATOM   2805  CA  TYR B 101       9.634 -33.717  22.000  1.00 23.87           C  
-ATOM   2806  C   TYR B 101       8.496 -32.704  22.009  1.00 24.46           C  
-ATOM   2807  O   TYR B 101       8.671 -31.547  21.616  1.00 24.43           O  
-ATOM   2808  CB  TYR B 101       9.680 -34.497  20.683  1.00 23.54           C  
-ATOM   2809  CG  TYR B 101      10.854 -35.439  20.633  1.00 23.33           C  
-ATOM   2810  CD1 TYR B 101      10.724 -36.766  21.046  1.00 22.79           C  
-ATOM   2811  CD2 TYR B 101      12.106 -34.994  20.218  1.00 23.14           C  
-ATOM   2812  CE1 TYR B 101      11.810 -37.629  21.029  1.00 23.44           C  
-ATOM   2813  CE2 TYR B 101      13.196 -35.850  20.193  1.00 23.66           C  
-ATOM   2814  CZ  TYR B 101      13.040 -37.163  20.597  1.00 23.21           C  
-ATOM   2815  OH  TYR B 101      14.117 -38.006  20.573  1.00 23.21           O  
-ATOM   2816  N   ARG B 102       7.331 -33.141  22.474  1.00 25.25           N  
-ATOM   2817  CA  ARG B 102       6.214 -32.236  22.702  1.00 26.41           C  
-ATOM   2818  C   ARG B 102       6.560 -31.228  23.806  1.00 26.64           C  
-ATOM   2819  O   ARG B 102       6.242 -30.039  23.689  1.00 26.90           O  
-ATOM   2820  CB  ARG B 102       4.953 -33.035  23.039  1.00 26.40           C  
-ATOM   2821  CG  ARG B 102       3.672 -32.218  23.120  1.00 27.35           C  
-ATOM   2822  CD  ARG B 102       2.437 -33.033  23.492  1.00 27.43           C  
-ATOM   2823  NE  ARG B 102       2.595 -33.730  24.768  1.00 29.24           N  
-ATOM   2824  CZ  ARG B 102       2.544 -35.051  24.925  1.00 29.21           C  
-ATOM   2825  NH1 ARG B 102       2.323 -35.850  23.889  1.00 29.46           N  
-ATOM   2826  NH2 ARG B 102       2.700 -35.576  26.132  1.00 29.66           N  
-ATOM   2827  N   GLU B 103       7.249 -31.703  24.846  1.00 26.86           N  
-ATOM   2828  CA AGLU B 103       7.562 -30.852  25.990  0.70 27.01           C  
-ATOM   2829  CA BGLU B 103       7.601 -30.898  26.022  0.30 26.90           C  
-ATOM   2830  C   GLU B 103       8.790 -29.963  25.789  1.00 27.04           C  
-ATOM   2831  O   GLU B 103       8.880 -28.893  26.400  1.00 27.02           O  
-ATOM   2832  CB AGLU B 103       7.657 -31.672  27.284  0.70 27.11           C  
-ATOM   2833  CB BGLU B 103       7.893 -31.808  27.220  0.30 26.91           C  
-ATOM   2834  CG AGLU B 103       6.336 -32.307  27.712  0.70 27.28           C  
-ATOM   2835  CG BGLU B 103       6.668 -32.499  27.807  0.30 26.70           C  
-ATOM   2836  CD AGLU B 103       5.157 -31.344  27.639  0.70 27.78           C  
-ATOM   2837  CD BGLU B 103       7.011 -33.725  28.641  0.30 26.55           C  
-ATOM   2838  OE1AGLU B 103       5.138 -30.355  28.403  0.70 27.99           O  
-ATOM   2839  OE1BGLU B 103       8.210 -33.989  28.878  0.30 26.41           O  
-ATOM   2840  OE2AGLU B 103       4.244 -31.579  26.816  0.70 27.82           O  
-ATOM   2841  OE2BGLU B 103       6.072 -34.431  29.063  0.30 26.20           O  
-ATOM   2842  N   ASP B 104       9.719 -30.380  24.927  1.00 27.04           N  
-ATOM   2843  CA  ASP B 104      10.872 -29.524  24.598  1.00 27.11           C  
-ATOM   2844  C   ASP B 104      10.619 -28.626  23.371  1.00 27.06           C  
-ATOM   2845  O   ASP B 104      11.512 -27.897  22.929  1.00 27.04           O  
-ATOM   2846  CB  ASP B 104      12.188 -30.324  24.504  1.00 27.09           C  
-ATOM   2847  CG  ASP B 104      12.381 -31.027  23.166  1.00 27.33           C  
-ATOM   2848  OD1 ASP B 104      11.422 -31.139  22.376  1.00 27.18           O  
-ATOM   2849  OD2 ASP B 104      13.482 -31.508  22.823  1.00 27.55           O  
-ATOM   2850  N   LYS B 105       9.396 -28.707  22.838  1.00 27.04           N  
-ATOM   2851  CA  LYS B 105       8.852 -27.778  21.822  1.00 27.10           C  
-ATOM   2852  C   LYS B 105       9.284 -28.025  20.365  1.00 27.21           C  
-ATOM   2853  O   LYS B 105       8.944 -27.254  19.460  1.00 26.97           O  
-ATOM   2854  CB  LYS B 105       9.033 -26.314  22.249  1.00 27.02           C  
-ATOM   2855  CG  LYS B 105       8.261 -25.976  23.515  1.00 26.91           C  
-ATOM   2856  CD  LYS B 105       8.739 -24.686  24.139  1.00 27.63           C  
-ATOM   2857  CE  LYS B 105       8.094 -24.473  25.495  1.00 27.95           C  
-ATOM   2858  NZ  LYS B 105       8.483 -23.167  26.080  1.00 28.18           N  
-ATOM   2859  N   SER B 106      10.041 -29.094  20.159  1.00 27.29           N  
-ATOM   2860  CA  SER B 106      10.199 -29.713  18.854  1.00 27.79           C  
-ATOM   2861  C   SER B 106      10.043 -31.168  19.240  1.00 27.82           C  
-ATOM   2862  O   SER B 106      10.971 -31.734  19.838  1.00 27.90           O  
-ATOM   2863  CB  SER B 106      11.596 -29.456  18.299  1.00 27.85           C  
-ATOM   2864  OG  SER B 106      12.571 -30.178  19.035  1.00 28.52           O  
-ATOM   2865  N   VAL B 107       8.934 -31.822  18.890  1.00 27.57           N  
-ATOM   2866  CA  VAL B 107       8.163 -31.674  17.647  1.00 26.79           C  
-ATOM   2867  C   VAL B 107       6.738 -31.094  17.818  1.00 26.25           C  
-ATOM   2868  O   VAL B 107       6.247 -30.966  18.940  1.00 25.93           O  
-ATOM   2869  CB  VAL B 107       8.069 -33.109  17.046  1.00 26.92           C  
-ATOM   2870  CG1 VAL B 107       7.464 -33.134  15.660  1.00 27.14           C  
-ATOM   2871  CG2 VAL B 107       9.449 -33.765  17.037  1.00 26.63           C  
-ATOM   2872  N   GLU B 108       6.084 -30.755  16.700  1.00 25.62           N  
-ATOM   2873  CA  GLU B 108       4.678 -30.308  16.689  1.00 25.36           C  
-ATOM   2874  C   GLU B 108       3.711 -31.330  16.065  1.00 25.23           C  
-ATOM   2875  O   GLU B 108       4.110 -32.148  15.233  1.00 24.65           O  
-ATOM   2876  CB  GLU B 108       4.539 -28.982  15.934  1.00 25.45           C  
-ATOM   2877  CG  GLU B 108       5.062 -27.756  16.673  1.00 25.66           C  
-ATOM   2878  CD  GLU B 108       4.963 -26.482  15.847  1.00 25.71           C  
-ATOM   2879  OE1 GLU B 108       4.195 -26.451  14.862  1.00 27.24           O  
-ATOM   2880  OE2 GLU B 108       5.658 -25.502  16.180  1.00 26.93           O  
-ATOM   2881  N   THR B 109       2.436 -31.253  16.455  1.00 24.95           N  
-ATOM   2882  CA  THR B 109       1.375 -32.085  15.865  1.00 24.80           C  
-ATOM   2883  C   THR B 109       0.358 -31.210  15.138  1.00 24.62           C  
-ATOM   2884  O   THR B 109      -0.300 -30.377  15.759  1.00 24.83           O  
-ATOM   2885  CB  THR B 109       0.673 -32.921  16.958  1.00 24.78           C  
-ATOM   2886  OG1 THR B 109       1.629 -33.776  17.594  1.00 25.12           O  
-ATOM   2887  CG2 THR B 109      -0.318 -33.910  16.341  1.00 24.79           C  
-ATOM   2888  N   VAL B 110       0.223 -31.401  13.828  1.00 24.47           N  
-ATOM   2889  CA  VAL B 110      -0.655 -30.538  13.032  1.00 24.21           C  
-ATOM   2890  C   VAL B 110      -2.127 -30.970  13.023  1.00 23.78           C  
-ATOM   2891  O   VAL B 110      -3.015 -30.130  13.169  1.00 23.47           O  
-ATOM   2892  CB  VAL B 110      -0.126 -30.274  11.584  1.00 24.41           C  
-ATOM   2893  CG1 VAL B 110       1.120 -29.401  11.615  1.00 25.11           C  
-ATOM   2894  CG2 VAL B 110       0.142 -31.551  10.839  1.00 24.63           C  
-ATOM   2895  N   ARG B 111      -2.386 -32.267  12.865  1.00 23.32           N  
-ATOM   2896  CA  ARG B 111      -3.762 -32.770  12.899  1.00 22.93           C  
-ATOM   2897  C   ARG B 111      -3.871 -34.284  13.032  1.00 22.83           C  
-ATOM   2898  O   ARG B 111      -2.883 -35.008  12.915  1.00 22.67           O  
-ATOM   2899  CB  ARG B 111      -4.558 -32.295  11.672  1.00 22.89           C  
-ATOM   2900  CG  ARG B 111      -4.181 -32.963  10.354  1.00 22.97           C  
-ATOM   2901  CD  ARG B 111      -5.269 -32.867   9.291  1.00 23.10           C  
-ATOM   2902  NE  ARG B 111      -6.473 -33.600   9.680  1.00 23.17           N  
-ATOM   2903  CZ  ARG B 111      -7.700 -33.350   9.233  1.00 23.04           C  
-ATOM   2904  NH1 ARG B 111      -7.929 -32.368   8.369  1.00 22.50           N  
-ATOM   2905  NH2 ARG B 111      -8.710 -34.087   9.665  1.00 22.87           N  
-ATOM   2906  N   GLU B 112      -5.095 -34.739  13.283  1.00 22.62           N  
-ATOM   2907  CA  GLU B 112      -5.450 -36.149  13.251  1.00 22.57           C  
-ATOM   2908  C   GLU B 112      -5.765 -36.514  11.802  1.00 21.98           C  
-ATOM   2909  O   GLU B 112      -6.730 -36.005  11.223  1.00 21.85           O  
-ATOM   2910  CB  GLU B 112      -6.674 -36.376  14.141  1.00 22.79           C  
-ATOM   2911  CG  GLU B 112      -7.027 -37.826  14.426  1.00 23.26           C  
-ATOM   2912  CD  GLU B 112      -8.065 -37.942  15.525  1.00 24.11           C  
-ATOM   2913  OE1 GLU B 112      -7.762 -37.560  16.681  1.00 26.06           O  
-ATOM   2914  OE2 GLU B 112      -9.188 -38.405  15.238  1.00 26.58           O  
-ATOM   2915  N   ASN B 113      -4.937 -37.375  11.215  1.00 21.07           N  
-ATOM   2916  CA  ASN B 113      -5.118 -37.783   9.826  1.00 20.59           C  
-ATOM   2917  C   ASN B 113      -5.905 -39.084   9.666  1.00 20.36           C  
-ATOM   2918  O   ASN B 113      -6.273 -39.458   8.552  1.00 20.47           O  
-ATOM   2919  CB  ASN B 113      -3.775 -37.836   9.078  1.00 20.29           C  
-ATOM   2920  CG  ASN B 113      -2.885 -38.976   9.530  1.00 19.97           C  
-ATOM   2921  OD1 ASN B 113      -3.318 -40.124   9.621  1.00 19.53           O  
-ATOM   2922  ND2 ASN B 113      -1.620 -38.667   9.790  1.00 18.95           N  
-ATOM   2923  N   LEU B 114      -6.150 -39.770  10.782  1.00 19.99           N  
-ATOM   2924  CA  LEU B 114      -6.962 -40.990  10.786  1.00 19.79           C  
-ATOM   2925  C   LEU B 114      -7.610 -41.240  12.142  1.00 19.35           C  
-ATOM   2926  O   LEU B 114      -6.943 -41.216  13.179  1.00 19.47           O  
-ATOM   2927  CB  LEU B 114      -6.135 -42.214  10.360  1.00 20.02           C  
-ATOM   2928  CG  LEU B 114      -6.880 -43.538  10.145  1.00 20.34           C  
-ATOM   2929  CD1 LEU B 114      -7.822 -43.466   8.937  1.00 20.98           C  
-ATOM   2930  CD2 LEU B 114      -5.901 -44.700   9.993  1.00 19.68           C  
-ATOM   2931  N   ALA B 115      -8.918 -41.470  12.121  1.00 18.80           N  
-ATOM   2932  CA  ALA B 115      -9.655 -41.870  13.309  1.00 18.22           C  
-ATOM   2933  C   ALA B 115     -10.216 -43.279  13.108  1.00 18.03           C  
-ATOM   2934  O   ALA B 115     -10.359 -43.737  11.971  1.00 17.99           O  
-ATOM   2935  CB  ALA B 115     -10.777 -40.878  13.591  1.00 18.45           C  
-ATOM   2936  N   GLY B 116     -10.517 -43.960  14.210  1.00 17.47           N  
-ATOM   2937  CA  GLY B 116     -11.165 -45.267  14.158  1.00 17.21           C  
-ATOM   2938  C   GLY B 116     -10.225 -46.438  13.952  1.00 16.90           C  
-ATOM   2939  O   GLY B 116     -10.659 -47.543  13.612  1.00 16.48           O  
-ATOM   2940  N   ALA B 117      -8.935 -46.189  14.155  1.00 16.35           N  
-ATOM   2941  CA  ALA B 117      -7.926 -47.237  14.072  1.00 16.30           C  
-ATOM   2942  C   ALA B 117      -7.933 -48.015  15.384  1.00 16.23           C  
-ATOM   2943  O   ALA B 117      -8.587 -47.605  16.344  1.00 16.34           O  
-ATOM   2944  CB  ALA B 117      -6.548 -46.628  13.795  1.00 15.82           C  
-ATOM   2945  N   LYS B 118      -7.240 -49.149  15.419  1.00 16.22           N  
-ATOM   2946  CA  LYS B 118      -7.035 -49.881  16.675  1.00 16.56           C  
-ATOM   2947  C   LYS B 118      -5.710 -50.633  16.653  1.00 15.84           C  
-ATOM   2948  O   LYS B 118      -5.247 -51.048  15.594  1.00 15.64           O  
-ATOM   2949  CB  LYS B 118      -8.215 -50.814  17.012  1.00 16.63           C  
-ATOM   2950  CG  LYS B 118      -8.526 -51.881  15.975  1.00 18.09           C  
-ATOM   2951  CD  LYS B 118      -9.835 -52.621  16.285  1.00 18.15           C  
-ATOM   2952  CE  LYS B 118      -9.637 -53.774  17.253  1.00 20.75           C  
-ATOM   2953  NZ  LYS B 118     -10.868 -54.628  17.361  1.00 22.15           N  
-ATOM   2954  N   TYR B 119      -5.107 -50.798  17.826  1.00 15.26           N  
-ATOM   2955  CA  TYR B 119      -3.776 -51.381  17.940  1.00 14.75           C  
-ATOM   2956  C   TYR B 119      -3.642 -52.029  19.310  1.00 14.96           C  
-ATOM   2957  O   TYR B 119      -3.652 -51.345  20.334  1.00 14.79           O  
-ATOM   2958  CB  TYR B 119      -2.723 -50.279  17.734  1.00 14.53           C  
-ATOM   2959  CG  TYR B 119      -1.271 -50.716  17.653  1.00 14.34           C  
-ATOM   2960  CD1 TYR B 119      -0.908 -51.965  17.134  1.00 13.90           C  
-ATOM   2961  CD2 TYR B 119      -0.254 -49.849  18.053  1.00 14.65           C  
-ATOM   2962  CE1 TYR B 119       0.435 -52.347  17.049  1.00 14.15           C  
-ATOM   2963  CE2 TYR B 119       1.084 -50.222  17.972  1.00 14.64           C  
-ATOM   2964  CZ  TYR B 119       1.421 -51.464  17.464  1.00 14.32           C  
-ATOM   2965  OH  TYR B 119       2.746 -51.821  17.378  1.00 14.77           O  
-ATOM   2966  N   THR B 120      -3.550 -53.355  19.329  1.00 15.04           N  
-ATOM   2967  CA  THR B 120      -3.349 -54.091  20.580  1.00 15.67           C  
-ATOM   2968  C   THR B 120      -2.906 -55.527  20.299  1.00 16.02           C  
-ATOM   2969  O   THR B 120      -2.676 -55.888  19.144  1.00 16.24           O  
-ATOM   2970  CB  THR B 120      -4.617 -54.017  21.478  1.00 15.54           C  
-ATOM   2971  OG1 THR B 120      -4.302 -54.469  22.807  1.00 15.44           O  
-ATOM   2972  CG2 THR B 120      -5.716 -54.943  20.984  1.00 14.86           C  
-ATOM   2973  N   LEU B 121      -2.743 -56.333  21.349  1.00 16.16           N  
-ATOM   2974  CA  LEU B 121      -2.380 -57.731  21.163  1.00 16.51           C  
-ATOM   2975  C   LEU B 121      -3.540 -58.526  20.570  1.00 16.69           C  
-ATOM   2976  O   LEU B 121      -4.707 -58.286  20.892  1.00 16.63           O  
-ATOM   2977  CB  LEU B 121      -1.902 -58.370  22.475  1.00 16.68           C  
-ATOM   2978  CG  LEU B 121      -0.564 -57.890  23.048  1.00 16.89           C  
-ATOM   2979  CD1 LEU B 121      -0.202 -58.673  24.317  1.00 17.16           C  
-ATOM   2980  CD2 LEU B 121       0.555 -57.990  22.027  1.00 16.41           C  
-ATOM   2981  N   ALA B 122      -3.196 -59.461  19.690  1.00 16.82           N  
-ATOM   2982  CA  ALA B 122      -4.166 -60.300  19.005  1.00 17.39           C  
-ATOM   2983  C   ALA B 122      -3.670 -61.741  18.983  1.00 17.68           C  
-ATOM   2984  O   ALA B 122      -2.482 -62.007  19.182  1.00 17.84           O  
-ATOM   2985  CB  ALA B 122      -4.388 -59.795  17.585  1.00 17.20           C  
-ATOM   2986  N   THR B 123      -4.589 -62.667  18.748  1.00 17.87           N  
-ATOM   2987  CA  THR B 123      -4.237 -64.067  18.571  1.00 17.99           C  
-ATOM   2988  C   THR B 123      -4.958 -64.652  17.352  1.00 18.09           C  
-ATOM   2989  O   THR B 123      -5.836 -64.007  16.771  1.00 17.85           O  
-ATOM   2990  CB  THR B 123      -4.535 -64.870  19.864  1.00 17.79           C  
-ATOM   2991  OG1 THR B 123      -3.994 -66.187  19.740  1.00 18.49           O  
-ATOM   2992  CG2 THR B 123      -6.041 -65.100  20.059  1.00 18.03           C  
-ATOM   2993  N   ASN B 124      -4.576 -65.866  16.962  1.00 18.41           N  
-ATOM   2994  CA  ASN B 124      -5.232 -66.543  15.844  1.00 18.65           C  
-ATOM   2995  C   ASN B 124      -6.418 -67.406  16.293  1.00 18.76           C  
-ATOM   2996  O   ASN B 124      -6.761 -67.439  17.478  1.00 18.71           O  
-ATOM   2997  CB  ASN B 124      -4.214 -67.346  15.015  1.00 18.70           C  
-ATOM   2998  CG  ASN B 124      -3.544 -68.459  15.805  1.00 18.91           C  
-ATOM   2999  OD1 ASN B 124      -3.615 -68.508  17.036  1.00 19.42           O  
-ATOM   3000  ND2 ASN B 124      -2.878 -69.364  15.091  1.00 18.90           N  
-ATOM   3001  N   ALA B 125      -7.047 -68.099  15.344  1.00 19.08           N  
-ATOM   3002  CA  ALA B 125      -8.194 -68.958  15.652  1.00 19.08           C  
-ATOM   3003  C   ALA B 125      -7.861 -70.018  16.705  1.00 19.23           C  
-ATOM   3004  O   ALA B 125      -8.667 -70.285  17.600  1.00 19.20           O  
-ATOM   3005  CB  ALA B 125      -8.731 -69.607  14.385  1.00 19.31           C  
-ATOM   3006  N   LYS B 126      -6.665 -70.601  16.603  1.00 19.17           N  
-ATOM   3007  CA  LYS B 126      -6.193 -71.608  17.551  1.00 19.38           C  
-ATOM   3008  C   LYS B 126      -6.054 -71.048  18.969  1.00 19.29           C  
-ATOM   3009  O   LYS B 126      -6.472 -71.688  19.938  1.00 19.24           O  
-ATOM   3010  CB  LYS B 126      -4.866 -72.218  17.068  1.00 19.58           C  
-ATOM   3011  CG  LYS B 126      -4.322 -73.379  17.917  1.00 20.23           C  
-ATOM   3012  CD  LYS B 126      -5.322 -74.522  18.097  1.00 21.65           C  
-ATOM   3013  CE  LYS B 126      -5.514 -75.331  16.827  1.00 22.68           C  
-ATOM   3014  NZ  LYS B 126      -6.345 -76.539  17.087  1.00 24.21           N  
-ATOM   3015  N   GLY B 127      -5.467 -69.857  19.081  1.00 19.31           N  
-ATOM   3016  CA  GLY B 127      -5.323 -69.172  20.367  1.00 19.37           C  
-ATOM   3017  C   GLY B 127      -6.668 -68.934  21.027  1.00 19.35           C  
-ATOM   3018  O   GLY B 127      -6.846 -69.235  22.210  1.00 19.25           O  
-ATOM   3019  N   ALA B 128      -7.613 -68.412  20.245  1.00 19.42           N  
-ATOM   3020  CA  ALA B 128      -8.995 -68.203  20.689  1.00 19.90           C  
-ATOM   3021  C   ALA B 128      -9.679 -69.511  21.104  1.00 20.05           C  
-ATOM   3022  O   ALA B 128     -10.394 -69.548  22.110  1.00 20.25           O  
-ATOM   3023  CB  ALA B 128      -9.803 -67.489  19.602  1.00 19.70           C  
-ATOM   3024  N   GLU B 129      -9.451 -70.578  20.336  1.00 20.24           N  
-ATOM   3025  CA  GLU B 129     -10.007 -71.900  20.647  1.00 20.51           C  
-ATOM   3026  C   GLU B 129      -9.478 -72.411  21.987  1.00 20.48           C  
-ATOM   3027  O   GLU B 129     -10.210 -73.038  22.757  1.00 20.59           O  
-ATOM   3028  CB  GLU B 129      -9.690 -72.905  19.529  1.00 20.52           C  
-ATOM   3029  CG  GLU B 129     -10.338 -74.275  19.707  1.00 20.98           C  
-ATOM   3030  CD  GLU B 129      -9.849 -75.314  18.707  1.00 21.18           C  
-ATOM   3031  OE1 GLU B 129      -8.979 -74.989  17.868  1.00 22.29           O  
-ATOM   3032  OE2 GLU B 129     -10.342 -76.466  18.758  1.00 22.03           O  
-ATOM   3033  N   LEU B 130      -8.205 -72.123  22.252  1.00 20.44           N  
-ATOM   3034  CA  LEU B 130      -7.536 -72.526  23.486  1.00 20.47           C  
-ATOM   3035  C   LEU B 130      -7.917 -71.673  24.703  1.00 20.39           C  
-ATOM   3036  O   LEU B 130      -7.604 -72.031  25.840  1.00 20.53           O  
-ATOM   3037  CB  LEU B 130      -6.017 -72.523  23.281  1.00 20.49           C  
-ATOM   3038  CG  LEU B 130      -5.270 -73.852  23.092  1.00 20.93           C  
-ATOM   3039  CD1 LEU B 130      -6.142 -74.981  22.532  1.00 20.91           C  
-ATOM   3040  CD2 LEU B 130      -4.048 -73.636  22.205  1.00 20.82           C  
-ATOM   3041  N   GLY B 131      -8.584 -70.549  24.461  1.00 20.10           N  
-ATOM   3042  CA  GLY B 131      -9.046 -69.684  25.543  1.00 19.81           C  
-ATOM   3043  C   GLY B 131      -8.253 -68.403  25.732  1.00 19.48           C  
-ATOM   3044  O   GLY B 131      -8.456 -67.691  26.717  1.00 19.47           O  
-ATOM   3045  N   ILE B 132      -7.350 -68.097  24.802  1.00 19.28           N  
-ATOM   3046  CA  ILE B 132      -6.665 -66.802  24.840  1.00 19.23           C  
-ATOM   3047  C   ILE B 132      -7.601 -65.733  24.268  1.00 19.16           C  
-ATOM   3048  O   ILE B 132      -7.703 -65.564  23.048  1.00 19.25           O  
-ATOM   3049  CB  ILE B 132      -5.304 -66.828  24.094  1.00 19.15           C  
-ATOM   3050  CG1 ILE B 132      -4.440 -68.012  24.549  1.00 19.27           C  
-ATOM   3051  CG2 ILE B 132      -4.549 -65.517  24.323  1.00 19.30           C  
-ATOM   3052  CD1 ILE B 132      -3.325 -68.380  23.567  1.00 19.18           C  
-ATOM   3053  N   LYS B 133      -8.302 -65.035  25.159  1.00 18.90           N  
-ATOM   3054  CA  LYS B 133      -9.226 -63.968  24.757  1.00 18.83           C  
-ATOM   3055  C   LYS B 133      -8.914 -62.641  25.434  1.00 18.42           C  
-ATOM   3056  O   LYS B 133      -9.424 -61.599  25.025  1.00 18.36           O  
-ATOM   3057  CB  LYS B 133     -10.685 -64.354  25.031  1.00 19.04           C  
-ATOM   3058  CG  LYS B 133     -11.317 -65.262  23.982  1.00 20.30           C  
-ATOM   3059  CD  LYS B 133     -11.288 -66.707  24.422  1.00 22.29           C  
-ATOM   3060  CE  LYS B 133     -12.483 -67.466  23.873  1.00 23.23           C  
-ATOM   3061  NZ  LYS B 133     -12.768 -68.681  24.683  1.00 23.65           N  
-ATOM   3062  N   ASP B 134      -8.073 -62.688  26.464  1.00 18.19           N  
-ATOM   3063  CA  ASP B 134      -7.733 -61.513  27.262  1.00 17.77           C  
-ATOM   3064  C   ASP B 134      -6.216 -61.452  27.471  1.00 17.62           C  
-ATOM   3065  O   ASP B 134      -5.527 -62.468  27.358  1.00 17.14           O  
-ATOM   3066  CB  ASP B 134      -8.463 -61.592  28.612  1.00 17.80           C  
-ATOM   3067  CG  ASP B 134      -8.484 -60.268  29.357  1.00 18.07           C  
-ATOM   3068  OD1 ASP B 134      -7.479 -59.946  30.029  1.00 17.35           O  
-ATOM   3069  OD2 ASP B 134      -9.473 -59.500  29.350  1.00 16.47           O  
-ATOM   3070  N   PHE B 135      -5.700 -60.259  27.768  1.00 17.47           N  
-ATOM   3071  CA  PHE B 135      -4.284 -60.085  28.114  1.00 17.53           C  
-ATOM   3072  C   PHE B 135      -3.871 -61.018  29.254  1.00 17.93           C  
-ATOM   3073  O   PHE B 135      -2.747 -61.530  29.273  1.00 17.84           O  
-ATOM   3074  CB  PHE B 135      -4.009 -58.631  28.509  1.00 17.18           C  
-ATOM   3075  CG  PHE B 135      -3.612 -57.740  27.357  1.00 17.02           C  
-ATOM   3076  CD1 PHE B 135      -4.403 -57.651  26.210  1.00 16.83           C  
-ATOM   3077  CD2 PHE B 135      -2.465 -56.962  27.439  1.00 15.68           C  
-ATOM   3078  CE1 PHE B 135      -4.044 -56.817  25.154  1.00 16.44           C  
-ATOM   3079  CE2 PHE B 135      -2.098 -56.122  26.387  1.00 16.54           C  
-ATOM   3080  CZ  PHE B 135      -2.891 -56.055  25.242  1.00 16.15           C  
-ATOM   3081  N   LYS B 136      -4.798 -61.237  30.187  1.00 18.28           N  
-ATOM   3082  CA  LYS B 136      -4.566 -62.074  31.365  1.00 19.00           C  
-ATOM   3083  C   LYS B 136      -4.464 -63.577  31.055  1.00 18.82           C  
-ATOM   3084  O   LYS B 136      -3.988 -64.350  31.896  1.00 18.95           O  
-ATOM   3085  CB  LYS B 136      -5.669 -61.827  32.406  1.00 19.16           C  
-ATOM   3086  CG  LYS B 136      -5.254 -62.084  33.856  1.00 21.09           C  
-ATOM   3087  CD  LYS B 136      -4.676 -60.826  34.516  1.00 24.12           C  
-ATOM   3088  CE  LYS B 136      -3.873 -61.156  35.775  1.00 25.07           C  
-ATOM   3089  NZ  LYS B 136      -2.541 -61.748  35.443  1.00 25.30           N  
-ATOM   3090  N   ASP B 137      -4.904 -63.984  29.861  1.00 18.61           N  
-ATOM   3091  CA  ASP B 137      -4.922 -65.403  29.465  1.00 18.46           C  
-ATOM   3092  C   ASP B 137      -3.619 -65.885  28.822  1.00 18.12           C  
-ATOM   3093  O   ASP B 137      -3.382 -67.092  28.723  1.00 18.17           O  
-ATOM   3094  CB  ASP B 137      -6.075 -65.688  28.491  1.00 18.47           C  
-ATOM   3095  CG  ASP B 137      -7.439 -65.348  29.064  1.00 19.27           C  
-ATOM   3096  OD1 ASP B 137      -7.663 -65.567  30.274  1.00 19.59           O  
-ATOM   3097  OD2 ASP B 137      -8.360 -64.870  28.366  1.00 19.23           O  
-ATOM   3098  N   ILE B 138      -2.797 -64.946  28.361  1.00 17.83           N  
-ATOM   3099  CA  ILE B 138      -1.547 -65.265  27.657  1.00 17.22           C  
-ATOM   3100  C   ILE B 138      -0.609 -66.129  28.502  1.00 17.12           C  
-ATOM   3101  O   ILE B 138      -0.124 -67.163  28.037  1.00 17.07           O  
-ATOM   3102  CB  ILE B 138      -0.815 -63.966  27.218  1.00 17.23           C  
-ATOM   3103  CG1 ILE B 138      -1.698 -63.124  26.290  1.00 16.74           C  
-ATOM   3104  CG2 ILE B 138       0.524 -64.305  26.558  1.00 16.39           C  
-ATOM   3105  CD1 ILE B 138      -1.283 -61.651  26.198  1.00 17.19           C  
-ATOM   3106  N   ALA B 139      -0.357 -65.692  29.734  1.00 17.02           N  
-ATOM   3107  CA  ALA B 139       0.565 -66.379  30.639  1.00 17.24           C  
-ATOM   3108  C   ALA B 139       0.099 -67.792  30.984  1.00 17.34           C  
-ATOM   3109  O   ALA B 139       0.921 -68.690  31.177  1.00 17.35           O  
-ATOM   3110  CB  ALA B 139       0.779 -65.565  31.895  1.00 17.58           C  
-ATOM   3111  N   ALA B 140      -1.220 -67.980  31.042  1.00 17.39           N  
-ATOM   3112  CA  ALA B 140      -1.826 -69.294  31.262  1.00 17.59           C  
-ATOM   3113  C   ALA B 140      -1.509 -70.281  30.138  1.00 17.66           C  
-ATOM   3114  O   ALA B 140      -1.603 -71.496  30.323  1.00 17.77           O  
-ATOM   3115  CB  ALA B 140      -3.335 -69.155  31.431  1.00 17.88           C  
-ATOM   3116  N   HIS B 141      -1.125 -69.754  28.979  1.00 17.48           N  
-ATOM   3117  CA  HIS B 141      -0.836 -70.582  27.815  1.00 17.53           C  
-ATOM   3118  C   HIS B 141       0.618 -70.458  27.354  1.00 17.38           C  
-ATOM   3119  O   HIS B 141       0.925 -70.629  26.170  1.00 17.60           O  
-ATOM   3120  CB  HIS B 141      -1.832 -70.264  26.692  1.00 17.57           C  
-ATOM   3121  CG  HIS B 141      -3.253 -70.566  27.062  1.00 18.13           C  
-ATOM   3122  ND1 HIS B 141      -4.035 -69.691  27.788  1.00 18.85           N  
-ATOM   3123  CD2 HIS B 141      -4.017 -71.661  26.845  1.00 18.03           C  
-ATOM   3124  CE1 HIS B 141      -5.226 -70.228  27.986  1.00 19.00           C  
-ATOM   3125  NE2 HIS B 141      -5.242 -71.423  27.422  1.00 18.90           N  
-ATOM   3126  N   LYS B 142       1.506 -70.187  28.312  1.00 17.08           N  
-ATOM   3127  CA  LYS B 142       2.925 -69.947  28.036  1.00 16.89           C  
-ATOM   3128  C   LYS B 142       3.650 -71.130  27.376  1.00 16.69           C  
-ATOM   3129  O   LYS B 142       4.499 -70.930  26.502  1.00 16.67           O  
-ATOM   3130  CB  LYS B 142       3.659 -69.466  29.300  1.00 16.83           C  
-ATOM   3131  CG  LYS B 142       3.658 -70.435  30.471  1.00 16.85           C  
-ATOM   3132  CD  LYS B 142       4.130 -69.755  31.747  1.00 17.32           C  
-ATOM   3133  CE  LYS B 142       4.031 -70.695  32.935  1.00 17.99           C  
-ATOM   3134  NZ  LYS B 142       4.522 -70.067  34.192  1.00 19.05           N  
-ATOM   3135  N   ASP B 143       3.305 -72.353  27.773  1.00 16.57           N  
-ATOM   3136  CA  ASP B 143       3.915 -73.538  27.165  1.00 16.37           C  
-ATOM   3137  C   ASP B 143       3.481 -73.714  25.713  1.00 16.37           C  
-ATOM   3138  O   ASP B 143       4.313 -73.982  24.843  1.00 16.01           O  
-ATOM   3139  CB  ASP B 143       3.621 -74.797  27.980  1.00 16.35           C  
-ATOM   3140  CG  ASP B 143       4.363 -74.821  29.299  1.00 16.42           C  
-ATOM   3141  OD1 ASP B 143       5.320 -74.031  29.463  1.00 16.62           O  
-ATOM   3142  OD2 ASP B 143       4.056 -75.591  30.229  1.00 15.64           O  
-ATOM   3143  N  AGLU B 144       2.181 -73.543  25.473  0.60 16.34           N  
-ATOM   3144  N  BGLU B 144       2.183 -73.557  25.456  0.40 16.23           N  
-ATOM   3145  CA AGLU B 144       1.589 -73.662  24.140  0.60 16.45           C  
-ATOM   3146  CA BGLU B 144       1.633 -73.686  24.104  0.40 16.21           C  
-ATOM   3147  C  AGLU B 144       2.114 -72.588  23.182  0.60 16.25           C  
-ATOM   3148  C  BGLU B 144       2.134 -72.587  23.167  0.40 16.16           C  
-ATOM   3149  O  AGLU B 144       2.217 -72.813  21.972  0.60 16.04           O  
-ATOM   3150  O  BGLU B 144       2.234 -72.791  21.953  0.40 16.01           O  
-ATOM   3151  CB AGLU B 144       0.058 -73.599  24.234  0.60 16.49           C  
-ATOM   3152  CB BGLU B 144       0.102 -73.702  24.144  0.40 16.18           C  
-ATOM   3153  CG AGLU B 144      -0.576 -74.761  24.995  0.60 16.97           C  
-ATOM   3154  CG BGLU B 144      -0.487 -75.017  24.635  0.40 15.94           C  
-ATOM   3155  CD AGLU B 144      -0.873 -74.455  26.461  0.60 17.68           C  
-ATOM   3156  CD BGLU B 144      -1.967 -74.918  24.955  0.40 15.68           C  
-ATOM   3157  OE1AGLU B 144      -1.898 -74.962  26.967  0.60 18.00           O  
-ATOM   3158  OE1BGLU B 144      -2.362 -73.984  25.686  0.40 15.22           O  
-ATOM   3159  OE2AGLU B 144      -0.098 -73.723  27.117  0.60 16.80           O  
-ATOM   3160  OE2BGLU B 144      -2.736 -75.780  24.484  0.40 15.72           O  
-ATOM   3161  N   LEU B 145       2.455 -71.429  23.742  1.00 16.26           N  
-ATOM   3162  CA  LEU B 145       3.008 -70.306  22.980  1.00 16.24           C  
-ATOM   3163  C   LEU B 145       4.536 -70.296  22.929  1.00 16.43           C  
-ATOM   3164  O   LEU B 145       5.130 -69.402  22.308  1.00 15.90           O  
-ATOM   3165  CB  LEU B 145       2.521 -68.978  23.566  1.00 16.10           C  
-ATOM   3166  CG  LEU B 145       1.019 -68.690  23.547  1.00 15.95           C  
-ATOM   3167  CD1 LEU B 145       0.727 -67.510  24.456  1.00 16.60           C  
-ATOM   3168  CD2 LEU B 145       0.517 -68.439  22.125  1.00 16.40           C  
-ATOM   3169  N   ASP B 146       5.163 -71.272  23.590  1.00 16.71           N  
-ATOM   3170  CA  ASP B 146       6.627 -71.366  23.665  1.00 17.12           C  
-ATOM   3171  C   ASP B 146       7.251 -70.092  24.272  1.00 17.16           C  
-ATOM   3172  O   ASP B 146       8.355 -69.679  23.899  1.00 17.20           O  
-ATOM   3173  CB  ASP B 146       7.213 -71.687  22.277  1.00 17.52           C  
-ATOM   3174  CG  ASP B 146       8.656 -72.172  22.336  1.00 18.33           C  
-ATOM   3175  OD1 ASP B 146       9.087 -72.686  23.388  1.00 19.07           O  
-ATOM   3176  OD2 ASP B 146       9.436 -72.074  21.367  1.00 19.96           O  
-ATOM   3177  N   GLY B 147       6.524 -69.475  25.204  1.00 17.12           N  
-ATOM   3178  CA  GLY B 147       6.978 -68.269  25.902  1.00 17.12           C  
-ATOM   3179  C   GLY B 147       7.369 -67.121  24.984  1.00 17.26           C  
-ATOM   3180  O   GLY B 147       8.309 -66.382  25.278  1.00 16.95           O  
-ATOM   3181  N   LYS B 148       6.643 -66.974  23.875  1.00 17.22           N  
-ATOM   3182  CA  LYS B 148       6.934 -65.931  22.890  1.00 17.70           C  
-ATOM   3183  C   LYS B 148       5.719 -65.065  22.565  1.00 17.25           C  
-ATOM   3184  O   LYS B 148       4.603 -65.566  22.433  1.00 17.11           O  
-ATOM   3185  CB  LYS B 148       7.500 -66.535  21.597  1.00 17.59           C  
-ATOM   3186  CG  LYS B 148       8.895 -67.158  21.734  1.00 18.10           C  
-ATOM   3187  CD  LYS B 148       9.384 -67.737  20.411  1.00 18.86           C  
-ATOM   3188  CE  LYS B 148      10.622 -68.614  20.610  1.00 20.35           C  
-ATOM   3189  NZ  LYS B 148      11.215 -69.070  19.312  1.00 22.94           N  
-ATOM   3190  N   ILE B 149       5.954 -63.758  22.465  1.00 17.37           N  
-ATOM   3191  CA  ILE B 149       5.006 -62.829  21.850  1.00 17.13           C  
-ATOM   3192  C   ILE B 149       5.718 -62.147  20.686  1.00 16.93           C  
-ATOM   3193  O   ILE B 149       6.877 -61.746  20.811  1.00 16.95           O  
-ATOM   3194  CB  ILE B 149       4.481 -61.780  22.860  1.00 17.16           C  
-ATOM   3195  CG1 ILE B 149       3.662 -62.456  23.964  1.00 17.16           C  
-ATOM   3196  CG2 ILE B 149       3.634 -60.712  22.134  1.00 17.04           C  
-ATOM   3197  CD1 ILE B 149       3.428 -61.586  25.197  1.00 17.38           C  
-ATOM   3198  N   TYR B 150       5.028 -62.029  19.554  1.00 16.59           N  
-ATOM   3199  CA  TYR B 150       5.652 -61.539  18.325  1.00 16.40           C  
-ATOM   3200  C   TYR B 150       5.343 -60.070  18.065  1.00 16.10           C  
-ATOM   3201  O   TYR B 150       4.182 -59.677  17.963  1.00 16.32           O  
-ATOM   3202  CB  TYR B 150       5.243 -62.410  17.137  1.00 16.81           C  
-ATOM   3203  CG  TYR B 150       5.927 -63.762  17.137  1.00 16.92           C  
-ATOM   3204  CD1 TYR B 150       5.419 -64.823  17.891  1.00 16.49           C  
-ATOM   3205  CD2 TYR B 150       7.085 -63.974  16.398  1.00 17.09           C  
-ATOM   3206  CE1 TYR B 150       6.053 -66.067  17.903  1.00 17.59           C  
-ATOM   3207  CE2 TYR B 150       7.730 -65.217  16.403  1.00 17.89           C  
-ATOM   3208  CZ  TYR B 150       7.204 -66.255  17.151  1.00 17.77           C  
-ATOM   3209  OH  TYR B 150       7.830 -67.478  17.157  1.00 18.69           O  
-ATOM   3210  N   GLY B 151       6.392 -59.257  18.000  1.00 15.70           N  
-ATOM   3211  CA  GLY B 151       6.238 -57.831  17.747  1.00 15.21           C  
-ATOM   3212  C   GLY B 151       6.665 -57.500  16.331  1.00 14.93           C  
-ATOM   3213  O   GLY B 151       6.813 -58.390  15.495  1.00 14.94           O  
-ATOM   3214  N   ILE B 152       6.875 -56.217  16.064  1.00 14.57           N  
-ATOM   3215  CA  ILE B 152       7.342 -55.785  14.748  1.00 14.47           C  
-ATOM   3216  C   ILE B 152       8.776 -55.243  14.813  1.00 14.68           C  
-ATOM   3217  O   ILE B 152       9.598 -55.822  15.523  1.00 15.06           O  
-ATOM   3218  CB  ILE B 152       6.303 -54.868  14.045  1.00 14.33           C  
-ATOM   3219  CG1 ILE B 152       5.943 -53.659  14.911  1.00 13.99           C  
-ATOM   3220  CG2 ILE B 152       5.039 -55.689  13.697  1.00 13.61           C  
-ATOM   3221  CD1 ILE B 152       4.932 -52.740  14.275  1.00 14.66           C  
-ATOM   3222  N   GLU B 153       9.087 -54.164  14.089  1.00 14.69           N  
-ATOM   3223  CA  GLU B 153      10.477 -53.697  13.980  1.00 14.73           C  
-ATOM   3224  C   GLU B 153      11.011 -53.148  15.307  1.00 14.84           C  
-ATOM   3225  O   GLU B 153      10.233 -52.617  16.104  1.00 15.21           O  
-ATOM   3226  CB  GLU B 153      10.637 -52.679  12.830  1.00 14.75           C  
-ATOM   3227  CG  GLU B 153      10.306 -51.220  13.153  1.00 14.21           C  
-ATOM   3228  CD  GLU B 153       8.828 -50.959  13.396  1.00 14.27           C  
-ATOM   3229  OE1 GLU B 153       7.981 -51.773  12.965  1.00 15.61           O  
-ATOM   3230  OE2 GLU B 153       8.509 -49.929  14.028  1.00 13.98           O  
-ATOM   3231  N   PRO B 154      12.313 -53.311  15.567  1.00 14.62           N  
-ATOM   3232  CA  PRO B 154      12.942 -52.707  16.746  1.00 14.66           C  
-ATOM   3233  C   PRO B 154      12.593 -51.229  16.921  1.00 14.40           C  
-ATOM   3234  O   PRO B 154      12.491 -50.480  15.936  1.00 14.15           O  
-ATOM   3235  CB  PRO B 154      14.441 -52.869  16.468  1.00 14.79           C  
-ATOM   3236  CG  PRO B 154      14.530 -54.118  15.633  1.00 14.94           C  
-ATOM   3237  CD  PRO B 154      13.277 -54.114  14.787  1.00 14.84           C  
-ATOM   3238  N   GLY B 155      12.397 -50.832  18.174  1.00 14.55           N  
-ATOM   3239  CA  GLY B 155      12.084 -49.451  18.516  1.00 14.15           C  
-ATOM   3240  C   GLY B 155      10.608 -49.112  18.440  1.00 14.17           C  
-ATOM   3241  O   GLY B 155      10.212 -48.012  18.814  1.00 14.36           O  
-ATOM   3242  N   ASN B 156       9.790 -50.043  17.952  1.00 14.33           N  
-ATOM   3243  CA  ASN B 156       8.354 -49.792  17.810  1.00 14.63           C  
-ATOM   3244  C   ASN B 156       7.693 -49.521  19.155  1.00 15.01           C  
-ATOM   3245  O   ASN B 156       8.067 -50.120  20.165  1.00 15.14           O  
-ATOM   3246  CB  ASN B 156       7.649 -50.964  17.121  1.00 14.61           C  
-ATOM   3247  CG  ASN B 156       6.218 -50.628  16.718  1.00 14.45           C  
-ATOM   3248  OD1 ASN B 156       5.263 -50.967  17.425  1.00 15.48           O  
-ATOM   3249  ND2 ASN B 156       6.065 -49.946  15.592  1.00 13.27           N  
-ATOM   3250  N   ASP B 157       6.714 -48.619  19.150  1.00 15.44           N  
-ATOM   3251  CA  ASP B 157       5.914 -48.299  20.338  1.00 15.61           C  
-ATOM   3252  C   ASP B 157       5.178 -49.513  20.906  1.00 15.88           C  
-ATOM   3253  O   ASP B 157       5.163 -49.715  22.121  1.00 16.02           O  
-ATOM   3254  CB  ASP B 157       4.932 -47.150  20.049  1.00 15.48           C  
-ATOM   3255  CG  ASP B 157       4.169 -47.327  18.736  1.00 15.63           C  
-ATOM   3256  OD1 ASP B 157       4.789 -47.648  17.704  1.00 15.04           O  
-ATOM   3257  OD2 ASP B 157       2.939 -47.143  18.635  1.00 17.10           O  
-ATOM   3258  N   GLY B 158       4.582 -50.317  20.023  1.00 15.94           N  
-ATOM   3259  CA  GLY B 158       3.975 -51.596  20.406  1.00 16.15           C  
-ATOM   3260  C   GLY B 158       4.959 -52.557  21.056  1.00 16.05           C  
-ATOM   3261  O   GLY B 158       4.703 -53.071  22.147  1.00 15.83           O  
-ATOM   3262  N   ASN B 159       6.083 -52.802  20.383  1.00 16.06           N  
-ATOM   3263  CA  ASN B 159       7.173 -53.605  20.945  1.00 16.00           C  
-ATOM   3264  C   ASN B 159       7.537 -53.132  22.352  1.00 16.22           C  
-ATOM   3265  O   ASN B 159       7.599 -53.932  23.283  1.00 16.11           O  
-ATOM   3266  CB  ASN B 159       8.422 -53.520  20.064  1.00 16.06           C  
-ATOM   3267  CG  ASN B 159       8.335 -54.389  18.816  1.00 16.08           C  
-ATOM   3268  OD1 ASN B 159       9.341 -54.941  18.363  1.00 18.57           O  
-ATOM   3269  ND2 ASN B 159       7.151 -54.505  18.255  1.00 13.92           N  
-ATOM   3270  N   ARG B 160       7.769 -51.824  22.478  1.00 15.98           N  
-ATOM   3271  CA  ARG B 160       8.118 -51.176  23.744  1.00 16.30           C  
-ATOM   3272  C   ARG B 160       7.143 -51.497  24.875  1.00 15.98           C  
-ATOM   3273  O   ARG B 160       7.565 -51.834  25.986  1.00 15.88           O  
-ATOM   3274  CB  ARG B 160       8.213 -49.661  23.535  1.00 16.23           C  
-ATOM   3275  CG  ARG B 160       8.519 -48.855  24.781  1.00 16.63           C  
-ATOM   3276  CD  ARG B 160       8.737 -47.361  24.537  1.00 16.82           C  
-ATOM   3277  NE  ARG B 160       7.800 -46.778  23.571  1.00 17.82           N  
-ATOM   3278  CZ  ARG B 160       6.545 -46.431  23.838  1.00 18.38           C  
-ATOM   3279  NH1 ARG B 160       5.793 -45.906  22.886  1.00 18.53           N  
-ATOM   3280  NH2 ARG B 160       6.029 -46.620  25.045  1.00 18.42           N  
-ATOM   3281  N   LEU B 161       5.848 -51.387  24.592  1.00 15.99           N  
-ATOM   3282  CA  LEU B 161       4.818 -51.675  25.596  1.00 15.91           C  
-ATOM   3283  C   LEU B 161       4.807 -53.144  26.030  1.00 15.79           C  
-ATOM   3284  O   LEU B 161       4.617 -53.436  27.213  1.00 15.43           O  
-ATOM   3285  CB  LEU B 161       3.435 -51.238  25.107  1.00 16.08           C  
-ATOM   3286  CG  LEU B 161       3.241 -49.717  25.017  1.00 15.91           C  
-ATOM   3287  CD1 LEU B 161       2.010 -49.387  24.188  1.00 16.46           C  
-ATOM   3288  CD2 LEU B 161       3.152 -49.072  26.395  1.00 17.27           C  
-ATOM   3289  N   ILE B 162       5.014 -54.054  25.080  1.00 15.73           N  
-ATOM   3290  CA  ILE B 162       5.089 -55.487  25.388  1.00 16.03           C  
-ATOM   3291  C   ILE B 162       6.328 -55.777  26.222  1.00 16.18           C  
-ATOM   3292  O   ILE B 162       6.236 -56.421  27.269  1.00 16.20           O  
-ATOM   3293  CB  ILE B 162       5.101 -56.367  24.106  1.00 16.22           C  
-ATOM   3294  CG1 ILE B 162       3.896 -56.074  23.217  1.00 16.52           C  
-ATOM   3295  CG2 ILE B 162       5.115 -57.868  24.482  1.00 15.71           C  
-ATOM   3296  CD1 ILE B 162       4.019 -56.668  21.820  1.00 15.89           C  
-ATOM   3297  N   ILE B 163       7.480 -55.295  25.753  1.00 16.38           N  
-ATOM   3298  CA  ILE B 163       8.744 -55.455  26.478  1.00 16.91           C  
-ATOM   3299  C   ILE B 163       8.638 -54.961  27.927  1.00 16.97           C  
-ATOM   3300  O   ILE B 163       9.142 -55.618  28.838  1.00 16.76           O  
-ATOM   3301  CB  ILE B 163       9.914 -54.773  25.713  1.00 17.01           C  
-ATOM   3302  CG1 ILE B 163      10.174 -55.506  24.389  1.00 17.14           C  
-ATOM   3303  CG2 ILE B 163      11.178 -54.731  26.569  1.00 17.05           C  
-ATOM   3304  CD1 ILE B 163      11.043 -54.737  23.377  1.00 17.28           C  
-ATOM   3305  N   ASP B 164       7.971 -53.821  28.130  1.00 17.17           N  
-ATOM   3306  CA AASP B 164       7.764 -53.282  29.473  0.50 17.45           C  
-ATOM   3307  CA BASP B 164       7.745 -53.276  29.472  0.50 17.36           C  
-ATOM   3308  C   ASP B 164       6.946 -54.234  30.348  1.00 17.45           C  
-ATOM   3309  O   ASP B 164       7.285 -54.448  31.519  1.00 17.39           O  
-ATOM   3310  CB AASP B 164       7.095 -51.903  29.415  0.50 17.48           C  
-ATOM   3311  CB BASP B 164       7.021 -51.929  29.397  0.50 17.31           C  
-ATOM   3312  CG AASP B 164       7.151 -51.170  30.746  0.50 17.92           C  
-ATOM   3313  CG BASP B 164       7.946 -50.781  29.050  0.50 17.35           C  
-ATOM   3314  OD1AASP B 164       8.230 -51.155  31.373  0.50 18.62           O  
-ATOM   3315  OD1BASP B 164       9.146 -51.017  28.805  0.50 17.49           O  
-ATOM   3316  OD2AASP B 164       6.170 -50.571  31.239  0.50 18.58           O  
-ATOM   3317  OD2BASP B 164       7.554 -49.598  29.007  0.50 17.87           O  
-ATOM   3318  N   MET B 165       5.877 -54.796  29.779  1.00 17.65           N  
-ATOM   3319  CA  MET B 165       5.029 -55.767  30.483  1.00 18.39           C  
-ATOM   3320  C   MET B 165       5.842 -56.975  30.921  1.00 18.41           C  
-ATOM   3321  O   MET B 165       5.760 -57.399  32.076  1.00 18.25           O  
-ATOM   3322  CB  MET B 165       3.859 -56.236  29.607  1.00 18.44           C  
-ATOM   3323  CG  MET B 165       2.729 -55.226  29.425  1.00 18.50           C  
-ATOM   3324  SD  MET B 165       1.225 -55.970  28.747  1.00 19.69           S  
-ATOM   3325  CE  MET B 165       1.732 -56.414  27.081  1.00 17.75           C  
-ATOM   3326  N   VAL B 166       6.637 -57.508  29.993  1.00 18.49           N  
-ATOM   3327  CA  VAL B 166       7.464 -58.686  30.246  1.00 18.68           C  
-ATOM   3328  C   VAL B 166       8.501 -58.438  31.344  1.00 19.01           C  
-ATOM   3329  O   VAL B 166       8.626 -59.242  32.268  1.00 18.87           O  
-ATOM   3330  CB  VAL B 166       8.148 -59.205  28.945  1.00 18.58           C  
-ATOM   3331  CG1 VAL B 166       9.123 -60.334  29.253  1.00 18.75           C  
-ATOM   3332  CG2 VAL B 166       7.105 -59.667  27.920  1.00 18.39           C  
-ATOM   3333  N   GLU B 167       9.229 -57.325  31.243  1.00 19.50           N  
-ATOM   3334  CA  GLU B 167      10.252 -56.967  32.227  1.00 20.20           C  
-ATOM   3335  C   GLU B 167       9.675 -56.698  33.615  1.00 19.98           C  
-ATOM   3336  O   GLU B 167      10.342 -56.936  34.621  1.00 19.77           O  
-ATOM   3337  CB  GLU B 167      11.053 -55.749  31.767  1.00 20.23           C  
-ATOM   3338  CG  GLU B 167      11.948 -56.002  30.564  1.00 21.32           C  
-ATOM   3339  CD  GLU B 167      12.696 -54.758  30.106  1.00 21.52           C  
-ATOM   3340  OE1 GLU B 167      12.304 -53.630  30.492  1.00 23.31           O  
-ATOM   3341  OE2 GLU B 167      13.682 -54.910  29.352  1.00 23.19           O  
-ATOM   3342  N   LYS B 168       8.441 -56.198  33.666  1.00 19.70           N  
-ATOM   3343  CA  LYS B 168       7.799 -55.891  34.944  1.00 19.55           C  
-ATOM   3344  C   LYS B 168       6.940 -57.035  35.481  1.00 19.06           C  
-ATOM   3345  O   LYS B 168       6.563 -57.039  36.655  1.00 18.75           O  
-ATOM   3346  CB  LYS B 168       6.979 -54.603  34.843  1.00 19.83           C  
-ATOM   3347  CG  LYS B 168       7.825 -53.354  34.666  1.00 20.94           C  
-ATOM   3348  CD  LYS B 168       7.059 -52.108  35.067  1.00 22.94           C  
-ATOM   3349  CE  LYS B 168       7.993 -50.912  35.209  1.00 23.67           C  
-ATOM   3350  NZ  LYS B 168       8.344 -50.339  33.881  1.00 24.29           N  
-ATOM   3351  N   GLY B 169       6.644 -58.007  34.623  1.00 18.44           N  
-ATOM   3352  CA  GLY B 169       5.804 -59.142  35.004  1.00 18.04           C  
-ATOM   3353  C   GLY B 169       4.322 -58.813  35.027  1.00 17.74           C  
-ATOM   3354  O   GLY B 169       3.552 -59.446  35.752  1.00 17.48           O  
-ATOM   3355  N   THR B 170       3.927 -57.812  34.242  1.00 17.55           N  
-ATOM   3356  CA  THR B 170       2.518 -57.451  34.064  1.00 17.59           C  
-ATOM   3357  C   THR B 170       1.788 -58.639  33.439  1.00 18.00           C  
-ATOM   3358  O   THR B 170       2.322 -59.286  32.536  1.00 18.17           O  
-ATOM   3359  CB  THR B 170       2.401 -56.200  33.161  1.00 17.43           C  
-ATOM   3360  OG1 THR B 170       3.266 -55.170  33.652  1.00 17.17           O  
-ATOM   3361  CG2 THR B 170       1.013 -55.573  33.260  1.00 17.09           C  
-ATOM   3362  N   PHE B 171       0.585 -58.929  33.935  1.00 18.56           N  
-ATOM   3363  CA  PHE B 171      -0.176 -60.127  33.538  1.00 18.87           C  
-ATOM   3364  C   PHE B 171       0.695 -61.396  33.596  1.00 19.42           C  
-ATOM   3365  O   PHE B 171       0.605 -62.273  32.728  1.00 19.37           O  
-ATOM   3366  CB  PHE B 171      -0.817 -59.929  32.153  1.00 19.00           C  
-ATOM   3367  CG  PHE B 171      -1.638 -58.666  32.037  1.00 18.72           C  
-ATOM   3368  CD1 PHE B 171      -1.305 -57.683  31.106  1.00 19.13           C  
-ATOM   3369  CD2 PHE B 171      -2.731 -58.452  32.871  1.00 18.63           C  
-ATOM   3370  CE1 PHE B 171      -2.058 -56.516  30.997  1.00 18.55           C  
-ATOM   3371  CE2 PHE B 171      -3.490 -57.286  32.778  1.00 18.77           C  
-ATOM   3372  CZ  PHE B 171      -3.150 -56.314  31.838  1.00 19.26           C  
-ATOM   3373  N   ASP B 172       1.504 -61.475  34.659  1.00 19.75           N  
-ATOM   3374  CA  ASP B 172       2.634 -62.420  34.830  1.00 20.39           C  
-ATOM   3375  C   ASP B 172       3.332 -62.915  33.553  1.00 19.88           C  
-ATOM   3376  O   ASP B 172       3.526 -64.121  33.342  1.00 19.83           O  
-ATOM   3377  CB  ASP B 172       2.319 -63.553  35.833  1.00 21.16           C  
-ATOM   3378  CG  ASP B 172       1.275 -64.531  35.325  1.00 23.59           C  
-ATOM   3379  OD1 ASP B 172       0.202 -64.086  34.866  1.00 26.12           O  
-ATOM   3380  OD2 ASP B 172       1.439 -65.774  35.372  1.00 25.70           O  
-ATOM   3381  N   LEU B 173       3.735 -61.953  32.726  1.00 19.30           N  
-ATOM   3382  CA  LEU B 173       4.450 -62.227  31.481  1.00 18.69           C  
-ATOM   3383  C   LEU B 173       5.965 -62.333  31.674  1.00 18.79           C  
-ATOM   3384  O   LEU B 173       6.718 -62.364  30.703  1.00 18.33           O  
-ATOM   3385  CB  LEU B 173       4.108 -61.166  30.429  1.00 18.42           C  
-ATOM   3386  CG  LEU B 173       2.673 -61.188  29.885  1.00 18.24           C  
-ATOM   3387  CD1 LEU B 173       2.431 -60.021  28.928  1.00 18.03           C  
-ATOM   3388  CD2 LEU B 173       2.360 -62.520  29.206  1.00 18.39           C  
-ATOM   3389  N   LYS B 174       6.412 -62.384  32.929  1.00 18.99           N  
-ATOM   3390  CA  LYS B 174       7.828 -62.609  33.217  1.00 19.57           C  
-ATOM   3391  C   LYS B 174       8.322 -63.871  32.521  1.00 19.26           C  
-ATOM   3392  O   LYS B 174       7.644 -64.899  32.529  1.00 19.45           O  
-ATOM   3393  CB  LYS B 174       8.080 -62.712  34.724  1.00 19.83           C  
-ATOM   3394  CG  LYS B 174       8.771 -61.497  35.317  1.00 21.81           C  
-ATOM   3395  CD  LYS B 174       9.091 -61.714  36.787  1.00 24.08           C  
-ATOM   3396  CE  LYS B 174       9.989 -60.609  37.337  1.00 25.98           C  
-ATOM   3397  NZ  LYS B 174      11.433 -60.821  37.003  1.00 27.41           N  
-ATOM   3398  N   GLY B 175       9.494 -63.777  31.903  1.00 19.02           N  
-ATOM   3399  CA  GLY B 175      10.122 -64.931  31.272  1.00 18.68           C  
-ATOM   3400  C   GLY B 175       9.721 -65.146  29.827  1.00 18.38           C  
-ATOM   3401  O   GLY B 175      10.206 -66.077  29.185  1.00 18.34           O  
-ATOM   3402  N   PHE B 176       8.828 -64.294  29.323  1.00 18.24           N  
-ATOM   3403  CA  PHE B 176       8.457 -64.291  27.911  1.00 18.10           C  
-ATOM   3404  C   PHE B 176       9.535 -63.611  27.077  1.00 18.10           C  
-ATOM   3405  O   PHE B 176      10.284 -62.772  27.571  1.00 18.15           O  
-ATOM   3406  CB  PHE B 176       7.127 -63.562  27.700  1.00 17.97           C  
-ATOM   3407  CG  PHE B 176       5.925 -64.469  27.665  1.00 17.84           C  
-ATOM   3408  CD1 PHE B 176       5.439 -65.054  28.832  1.00 17.38           C  
-ATOM   3409  CD2 PHE B 176       5.264 -64.718  26.462  1.00 17.71           C  
-ATOM   3410  CE1 PHE B 176       4.319 -65.887  28.800  1.00 17.39           C  
-ATOM   3411  CE2 PHE B 176       4.143 -65.547  26.419  1.00 17.84           C  
-ATOM   3412  CZ  PHE B 176       3.672 -66.135  27.593  1.00 17.45           C  
-ATOM   3413  N   GLU B 177       9.610 -63.986  25.808  1.00 18.01           N  
-ATOM   3414  CA  GLU B 177      10.504 -63.328  24.875  1.00 18.21           C  
-ATOM   3415  C   GLU B 177       9.661 -62.558  23.874  1.00 17.73           C  
-ATOM   3416  O   GLU B 177       8.689 -63.090  23.333  1.00 17.34           O  
-ATOM   3417  CB  GLU B 177      11.382 -64.356  24.166  1.00 18.65           C  
-ATOM   3418  CG  GLU B 177      12.439 -63.754  23.252  1.00 20.64           C  
-ATOM   3419  CD  GLU B 177      13.097 -64.779  22.355  1.00 23.05           C  
-ATOM   3420  OE1 GLU B 177      12.894 -65.994  22.572  1.00 24.11           O  
-ATOM   3421  OE2 GLU B 177      13.821 -64.365  21.424  1.00 24.66           O  
-ATOM   3422  N   VAL B 178      10.008 -61.293  23.659  1.00 17.41           N  
-ATOM   3423  CA  VAL B 178       9.372 -60.514  22.610  1.00 17.36           C  
-ATOM   3424  C   VAL B 178      10.212 -60.680  21.352  1.00 17.49           C  
-ATOM   3425  O   VAL B 178      11.368 -60.247  21.304  1.00 17.32           O  
-ATOM   3426  CB  VAL B 178       9.238 -59.018  22.971  1.00 17.86           C  
-ATOM   3427  CG1 VAL B 178       8.443 -58.280  21.896  1.00 17.03           C  
-ATOM   3428  CG2 VAL B 178       8.595 -58.846  24.355  1.00 16.76           C  
-ATOM   3429  N   VAL B 179       9.634 -61.334  20.351  1.00 17.29           N  
-ATOM   3430  CA  VAL B 179      10.353 -61.612  19.116  1.00 17.49           C  
-ATOM   3431  C   VAL B 179      10.150 -60.438  18.172  1.00 17.43           C  
-ATOM   3432  O   VAL B 179       9.038 -60.181  17.714  1.00 17.29           O  
-ATOM   3433  CB  VAL B 179       9.913 -62.944  18.461  1.00 17.41           C  
-ATOM   3434  CG1 VAL B 179      10.625 -63.151  17.122  1.00 17.45           C  
-ATOM   3435  CG2 VAL B 179      10.190 -64.121  19.395  1.00 17.28           C  
-ATOM   3436  N   GLU B 180      11.235 -59.714  17.914  1.00 17.66           N  
-ATOM   3437  CA  GLU B 180      11.188 -58.521  17.074  1.00 17.98           C  
-ATOM   3438  C   GLU B 180      11.684 -58.852  15.675  1.00 17.76           C  
-ATOM   3439  O   GLU B 180      12.606 -59.651  15.512  1.00 17.82           O  
-ATOM   3440  CB  GLU B 180      12.039 -57.402  17.682  1.00 17.88           C  
-ATOM   3441  CG  GLU B 180      11.769 -57.138  19.156  1.00 18.39           C  
-ATOM   3442  CD  GLU B 180      12.498 -55.919  19.672  1.00 18.91           C  
-ATOM   3443  OE1 GLU B 180      13.721 -56.009  19.931  1.00 19.88           O  
-ATOM   3444  OE2 GLU B 180      11.843 -54.869  19.830  1.00 19.30           O  
-ATOM   3445  N   SER B 181      11.062 -58.238  14.671  1.00 17.47           N  
-ATOM   3446  CA  SER B 181      11.455 -58.410  13.275  1.00 17.19           C  
-ATOM   3447  C   SER B 181      10.951 -57.223  12.463  1.00 17.00           C  
-ATOM   3448  O   SER B 181      11.677 -56.251  12.254  1.00 16.67           O  
-ATOM   3449  CB  SER B 181      10.937 -59.746  12.703  1.00 17.14           C  
-ATOM   3450  OG  SER B 181       9.528 -59.867  12.832  1.00 17.04           O  
-ATOM   3451  N   SER B 182       9.690 -57.298  12.042  1.00 16.96           N  
-ATOM   3452  CA  SER B 182       9.057 -56.272  11.218  1.00 16.89           C  
-ATOM   3453  C   SER B 182       7.598 -56.659  11.082  1.00 16.74           C  
-ATOM   3454  O   SER B 182       7.202 -57.730  11.539  1.00 16.67           O  
-ATOM   3455  CB  SER B 182       9.706 -56.218   9.832  1.00 17.08           C  
-ATOM   3456  OG  SER B 182       9.571 -57.460   9.157  1.00 17.22           O  
-ATOM   3457  N   GLU B 183       6.799 -55.802  10.447  1.00 16.50           N  
-ATOM   3458  CA  GLU B 183       5.412 -56.157  10.150  1.00 16.24           C  
-ATOM   3459  C   GLU B 183       5.385 -57.405   9.274  1.00 16.35           C  
-ATOM   3460  O   GLU B 183       4.614 -58.338   9.510  1.00 16.22           O  
-ATOM   3461  CB  GLU B 183       4.695 -55.013   9.433  1.00 16.13           C  
-ATOM   3462  CG  GLU B 183       3.355 -55.424   8.841  1.00 15.75           C  
-ATOM   3463  CD  GLU B 183       2.795 -54.407   7.872  1.00 15.28           C  
-ATOM   3464  OE1 GLU B 183       2.734 -53.211   8.227  1.00 15.10           O  
-ATOM   3465  OE2 GLU B 183       2.401 -54.815   6.758  1.00 14.38           O  
-ATOM   3466  N   GLN B 184       6.243 -57.391   8.263  1.00 16.70           N  
-ATOM   3467  CA  GLN B 184       6.356 -58.449   7.280  1.00 17.12           C  
-ATOM   3468  C   GLN B 184       6.773 -59.763   7.949  1.00 17.07           C  
-ATOM   3469  O   GLN B 184       6.157 -60.806   7.712  1.00 17.26           O  
-ATOM   3470  CB  GLN B 184       7.337 -58.021   6.175  1.00 17.43           C  
-ATOM   3471  CG  GLN B 184       6.905 -56.738   5.375  1.00 19.47           C  
-ATOM   3472  CD  GLN B 184       6.953 -55.405   6.175  1.00 20.99           C  
-ATOM   3473  OE1 GLN B 184       6.193 -54.465   5.879  1.00 22.88           O  
-ATOM   3474  NE2 GLN B 184       7.842 -55.321   7.155  1.00 19.80           N  
-ATOM   3475  N   GLY B 185       7.790 -59.695   8.805  1.00 16.99           N  
-ATOM   3476  CA  GLY B 185       8.280 -60.854   9.557  1.00 16.72           C  
-ATOM   3477  C   GLY B 185       7.267 -61.441  10.530  1.00 16.71           C  
-ATOM   3478  O   GLY B 185       7.113 -62.662  10.610  1.00 16.40           O  
-ATOM   3479  N   MET B 186       6.580 -60.567  11.268  1.00 16.63           N  
-ATOM   3480  CA  MET B 186       5.537 -60.978  12.222  1.00 16.84           C  
-ATOM   3481  C   MET B 186       4.413 -61.722  11.493  1.00 16.73           C  
-ATOM   3482  O   MET B 186       4.012 -62.813  11.905  1.00 16.21           O  
-ATOM   3483  CB  MET B 186       4.988 -59.760  12.988  1.00 16.79           C  
-ATOM   3484  CG  MET B 186       3.942 -60.074  14.068  1.00 16.81           C  
-ATOM   3485  SD  MET B 186       2.904 -58.654  14.515  1.00 17.99           S  
-ATOM   3486  CE  MET B 186       1.973 -58.435  12.998  1.00 17.32           C  
-ATOM   3487  N   LEU B 187       3.941 -61.140  10.391  1.00 16.85           N  
-ATOM   3488  CA  LEU B 187       2.854 -61.730   9.607  1.00 17.22           C  
-ATOM   3489  C   LEU B 187       3.229 -63.051   8.943  1.00 17.26           C  
-ATOM   3490  O   LEU B 187       2.385 -63.943   8.812  1.00 17.22           O  
-ATOM   3491  CB  LEU B 187       2.313 -60.737   8.575  1.00 17.46           C  
-ATOM   3492  CG  LEU B 187       1.469 -59.593   9.154  1.00 18.03           C  
-ATOM   3493  CD1 LEU B 187       1.194 -58.574   8.072  1.00 19.55           C  
-ATOM   3494  CD2 LEU B 187       0.160 -60.109   9.756  1.00 19.14           C  
-ATOM   3495  N   ALA B 188       4.488 -63.166   8.525  1.00 17.37           N  
-ATOM   3496  CA  ALA B 188       5.021 -64.438   8.036  1.00 17.22           C  
-ATOM   3497  C   ALA B 188       4.892 -65.521   9.111  1.00 17.16           C  
-ATOM   3498  O   ALA B 188       4.486 -66.644   8.817  1.00 17.38           O  
-ATOM   3499  CB  ALA B 188       6.467 -64.280   7.602  1.00 17.19           C  
-ATOM   3500  N   GLN B 189       5.227 -65.172  10.354  1.00 17.08           N  
-ATOM   3501  CA  GLN B 189       5.141 -66.110  11.475  1.00 16.87           C  
-ATOM   3502  C   GLN B 189       3.698 -66.477  11.820  1.00 16.59           C  
-ATOM   3503  O   GLN B 189       3.420 -67.622  12.180  1.00 16.10           O  
-ATOM   3504  CB  GLN B 189       5.876 -65.568  12.708  1.00 17.27           C  
-ATOM   3505  CG  GLN B 189       6.032 -66.577  13.853  1.00 18.06           C  
-ATOM   3506  CD  GLN B 189       6.717 -67.871  13.439  1.00 20.22           C  
-ATOM   3507  OE1 GLN B 189       6.254 -68.963  13.789  1.00 21.54           O  
-ATOM   3508  NE2 GLN B 189       7.811 -67.760  12.689  1.00 19.55           N  
-ATOM   3509  N   VAL B 190       2.789 -65.507  11.710  1.00 16.34           N  
-ATOM   3510  CA  VAL B 190       1.359 -65.759  11.912  1.00 16.24           C  
-ATOM   3511  C   VAL B 190       0.884 -66.832  10.927  1.00 16.28           C  
-ATOM   3512  O   VAL B 190       0.217 -67.793  11.324  1.00 15.88           O  
-ATOM   3513  CB  VAL B 190       0.503 -64.467  11.771  1.00 16.25           C  
-ATOM   3514  CG1 VAL B 190      -0.994 -64.787  11.833  1.00 16.31           C  
-ATOM   3515  CG2 VAL B 190       0.869 -63.454  12.849  1.00 16.28           C  
-ATOM   3516  N   ALA B 191       1.253 -66.673   9.655  1.00 16.17           N  
-ATOM   3517  CA  ALA B 191       0.916 -67.653   8.612  1.00 16.33           C  
-ATOM   3518  C   ALA B 191       1.498 -69.037   8.905  1.00 16.44           C  
-ATOM   3519  O   ALA B 191       0.843 -70.055   8.661  1.00 16.49           O  
-ATOM   3520  CB  ALA B 191       1.382 -67.165   7.251  1.00 16.11           C  
-ATOM   3521  N   ARG B 192       2.725 -69.071   9.422  1.00 16.60           N  
-ATOM   3522  CA  ARG B 192       3.379 -70.337   9.758  1.00 16.98           C  
-ATOM   3523  C   ARG B 192       2.705 -71.022  10.946  1.00 17.03           C  
-ATOM   3524  O   ARG B 192       2.562 -72.243  10.957  1.00 16.67           O  
-ATOM   3525  CB  ARG B 192       4.876 -70.139  10.015  1.00 17.16           C  
-ATOM   3526  CG  ARG B 192       5.681 -69.807   8.759  1.00 16.86           C  
-ATOM   3527  CD  ARG B 192       7.187 -69.794   8.960  1.00 17.56           C  
-ATOM   3528  NE  ARG B 192       7.637 -68.638   9.736  1.00 18.81           N  
-ATOM   3529  CZ  ARG B 192       8.142 -67.522   9.215  1.00 19.05           C  
-ATOM   3530  NH1 ARG B 192       8.522 -66.535  10.011  1.00 19.28           N  
-ATOM   3531  NH2 ARG B 192       8.275 -67.387   7.903  1.00 20.21           N  
-ATOM   3532  N   ALA B 193       2.280 -70.231  11.934  1.00 17.29           N  
-ATOM   3533  CA  ALA B 193       1.496 -70.759  13.057  1.00 17.85           C  
-ATOM   3534  C   ALA B 193       0.165 -71.332  12.569  1.00 18.22           C  
-ATOM   3535  O   ALA B 193      -0.268 -72.392  13.028  1.00 18.03           O  
-ATOM   3536  CB  ALA B 193       1.261 -69.685  14.109  1.00 17.87           C  
-ATOM   3537  N   GLU B 194      -0.468 -70.626  11.633  1.00 18.68           N  
-ATOM   3538  CA  GLU B 194      -1.711 -71.081  11.005  1.00 19.40           C  
-ATOM   3539  C   GLU B 194      -1.544 -72.431  10.323  1.00 19.32           C  
-ATOM   3540  O   GLU B 194      -2.402 -73.312  10.443  1.00 19.38           O  
-ATOM   3541  CB  GLU B 194      -2.215 -70.044   9.988  1.00 19.64           C  
-ATOM   3542  CG  GLU B 194      -2.687 -68.732  10.594  1.00 21.49           C  
-ATOM   3543  CD  GLU B 194      -3.965 -68.872  11.400  1.00 23.70           C  
-ATOM   3544  OE1 GLU B 194      -3.983 -69.649  12.378  1.00 24.61           O  
-ATOM   3545  OE2 GLU B 194      -4.951 -68.187  11.061  1.00 25.55           O  
-ATOM   3546  N   LYS B 195      -0.433 -72.585   9.607  1.00 19.17           N  
-ATOM   3547  CA  LYS B 195      -0.135 -73.822   8.892  1.00 19.08           C  
-ATOM   3548  C   LYS B 195       0.139 -74.985   9.853  1.00 18.84           C  
-ATOM   3549  O   LYS B 195      -0.394 -76.080   9.671  1.00 18.69           O  
-ATOM   3550  CB  LYS B 195       1.035 -73.611   7.917  1.00 19.11           C  
-ATOM   3551  CG  LYS B 195       1.590 -74.882   7.268  1.00 19.81           C  
-ATOM   3552  CD  LYS B 195       0.556 -75.598   6.409  1.00 20.92           C  
-ATOM   3553  CE  LYS B 195       1.100 -76.917   5.894  1.00 21.41           C  
-ATOM   3554  NZ  LYS B 195       0.019 -77.769   5.337  1.00 22.10           N  
-ATOM   3555  N   SER B 196       0.956 -74.742  10.874  1.00 18.59           N  
-ATOM   3556  CA  SER B 196       1.316 -75.795  11.822  1.00 18.73           C  
-ATOM   3557  C   SER B 196       0.212 -76.131  12.836  1.00 18.43           C  
-ATOM   3558  O   SER B 196       0.250 -77.187  13.465  1.00 18.47           O  
-ATOM   3559  CB  SER B 196       2.626 -75.460  12.539  1.00 18.75           C  
-ATOM   3560  OG  SER B 196       2.486 -74.338  13.379  1.00 19.55           O  
-ATOM   3561  N   GLY B 197      -0.761 -75.236  12.990  1.00 18.10           N  
-ATOM   3562  CA  GLY B 197      -1.861 -75.438  13.939  1.00 17.75           C  
-ATOM   3563  C   GLY B 197      -1.549 -75.014  15.368  1.00 17.58           C  
-ATOM   3564  O   GLY B 197      -2.134 -75.542  16.317  1.00 17.50           O  
-ATOM   3565  N   ASP B 198      -0.625 -74.066  15.518  1.00 17.22           N  
-ATOM   3566  CA  ASP B 198      -0.220 -73.554  16.830  1.00 16.93           C  
-ATOM   3567  C   ASP B 198      -0.925 -72.236  17.142  1.00 16.40           C  
-ATOM   3568  O   ASP B 198      -1.277 -71.501  16.222  1.00 16.14           O  
-ATOM   3569  CB  ASP B 198       1.292 -73.308  16.863  1.00 17.17           C  
-ATOM   3570  CG  ASP B 198       2.098 -74.590  16.857  1.00 18.12           C  
-ATOM   3571  OD1 ASP B 198       1.906 -75.433  17.759  1.00 18.16           O  
-ATOM   3572  OD2 ASP B 198       2.963 -74.826  15.990  1.00 19.64           O  
-ATOM   3573  N   PRO B 199      -1.130 -71.936  18.429  1.00 16.17           N  
-ATOM   3574  CA  PRO B 199      -1.578 -70.604  18.840  1.00 16.17           C  
-ATOM   3575  C   PRO B 199      -0.428 -69.614  18.718  1.00 15.97           C  
-ATOM   3576  O   PRO B 199       0.732 -70.009  18.829  1.00 16.04           O  
-ATOM   3577  CB  PRO B 199      -1.939 -70.791  20.323  1.00 15.90           C  
-ATOM   3578  CG  PRO B 199      -1.085 -71.929  20.780  1.00 16.52           C  
-ATOM   3579  CD  PRO B 199      -0.947 -72.838  19.585  1.00 16.16           C  
-ATOM   3580  N   ILE B 200      -0.750 -68.346  18.483  1.00 15.78           N  
-ATOM   3581  CA  ILE B 200       0.253 -67.285  18.454  1.00 15.75           C  
-ATOM   3582  C   ILE B 200      -0.343 -65.997  19.017  1.00 15.87           C  
-ATOM   3583  O   ILE B 200      -1.539 -65.749  18.877  1.00 15.83           O  
-ATOM   3584  CB  ILE B 200       0.845 -67.089  17.010  1.00 15.48           C  
-ATOM   3585  CG1 ILE B 200       2.077 -66.175  17.034  1.00 15.41           C  
-ATOM   3586  CG2 ILE B 200      -0.213 -66.590  16.011  1.00 15.65           C  
-ATOM   3587  CD1 ILE B 200       2.859 -66.153  15.716  1.00 15.56           C  
-ATOM   3588  N   VAL B 201       0.490 -65.206  19.687  1.00 15.82           N  
-ATOM   3589  CA  VAL B 201       0.086 -63.892  20.178  1.00 15.94           C  
-ATOM   3590  C   VAL B 201       1.015 -62.860  19.548  1.00 16.18           C  
-ATOM   3591  O   VAL B 201       2.241 -63.010  19.579  1.00 16.28           O  
-ATOM   3592  CB  VAL B 201       0.123 -63.793  21.725  1.00 15.85           C  
-ATOM   3593  CG1 VAL B 201      -0.302 -62.396  22.197  1.00 15.53           C  
-ATOM   3594  CG2 VAL B 201      -0.765 -64.850  22.357  1.00 16.01           C  
-ATOM   3595  N   PHE B 202       0.420 -61.826  18.960  1.00 16.50           N  
-ATOM   3596  CA  PHE B 202       1.165 -60.850  18.171  1.00 16.65           C  
-ATOM   3597  C   PHE B 202       0.470 -59.493  18.187  1.00 16.68           C  
-ATOM   3598  O   PHE B 202      -0.600 -59.339  18.785  1.00 16.70           O  
-ATOM   3599  CB  PHE B 202       1.316 -61.350  16.728  1.00 16.58           C  
-ATOM   3600  CG  PHE B 202       0.004 -61.560  16.023  1.00 17.23           C  
-ATOM   3601  CD1 PHE B 202      -0.465 -60.622  15.105  1.00 17.67           C  
-ATOM   3602  CD2 PHE B 202      -0.773 -62.686  16.291  1.00 17.59           C  
-ATOM   3603  CE1 PHE B 202      -1.687 -60.809  14.457  1.00 17.08           C  
-ATOM   3604  CE2 PHE B 202      -1.990 -62.876  15.658  1.00 17.58           C  
-ATOM   3605  CZ  PHE B 202      -2.447 -61.938  14.738  1.00 17.19           C  
-ATOM   3606  N   LEU B 203       1.085 -58.511  17.531  1.00 16.63           N  
-ATOM   3607  CA  LEU B 203       0.487 -57.183  17.389  1.00 16.91           C  
-ATOM   3608  C   LEU B 203      -0.463 -57.122  16.196  1.00 17.06           C  
-ATOM   3609  O   LEU B 203      -0.052 -57.286  15.042  1.00 17.01           O  
-ATOM   3610  CB  LEU B 203       1.578 -56.114  17.245  1.00 16.87           C  
-ATOM   3611  CG  LEU B 203       2.402 -55.799  18.491  1.00 16.94           C  
-ATOM   3612  CD1 LEU B 203       3.680 -55.059  18.137  1.00 16.15           C  
-ATOM   3613  CD2 LEU B 203       1.569 -55.006  19.473  1.00 17.65           C  
-ATOM   3614  N   GLY B 204      -1.740 -56.897  16.483  1.00 17.17           N  
-ATOM   3615  CA  GLY B 204      -2.738 -56.704  15.436  1.00 17.19           C  
-ATOM   3616  C   GLY B 204      -3.160 -55.249  15.368  1.00 17.20           C  
-ATOM   3617  O   GLY B 204      -3.144 -54.546  16.381  1.00 17.17           O  
-ATOM   3618  N   TRP B 205      -3.533 -54.795  14.174  1.00 16.86           N  
-ATOM   3619  CA  TRP B 205      -4.075 -53.449  14.018  1.00 16.63           C  
-ATOM   3620  C   TRP B 205      -5.016 -53.285  12.831  1.00 16.39           C  
-ATOM   3621  O   TRP B 205      -4.918 -54.004  11.831  1.00 15.97           O  
-ATOM   3622  CB  TRP B 205      -2.956 -52.394  13.959  1.00 16.11           C  
-ATOM   3623  CG  TRP B 205      -1.994 -52.537  12.813  1.00 16.07           C  
-ATOM   3624  CD1 TRP B 205      -2.095 -51.959  11.577  1.00 15.57           C  
-ATOM   3625  CD2 TRP B 205      -0.770 -53.285  12.804  1.00 16.18           C  
-ATOM   3626  NE1 TRP B 205      -1.019 -52.313  10.798  1.00 15.67           N  
-ATOM   3627  CE2 TRP B 205      -0.187 -53.123  11.527  1.00 15.99           C  
-ATOM   3628  CE3 TRP B 205      -0.102 -54.080  13.748  1.00 16.53           C  
-ATOM   3629  CZ2 TRP B 205       1.030 -53.723  11.169  1.00 16.31           C  
-ATOM   3630  CZ3 TRP B 205       1.113 -54.677  13.392  1.00 15.98           C  
-ATOM   3631  CH2 TRP B 205       1.660 -54.495  12.111  1.00 15.64           C  
-ATOM   3632  N   GLU B 206      -5.927 -52.327  12.976  1.00 16.60           N  
-ATOM   3633  CA  GLU B 206      -6.772 -51.835  11.889  1.00 17.13           C  
-ATOM   3634  C   GLU B 206      -6.408 -50.364  11.669  1.00 16.80           C  
-ATOM   3635  O   GLU B 206      -6.224 -49.637  12.647  1.00 16.35           O  
-ATOM   3636  CB  GLU B 206      -8.250 -51.950  12.265  1.00 16.96           C  
-ATOM   3637  CG  GLU B 206      -8.723 -53.375  12.505  1.00 18.27           C  
-ATOM   3638  CD  GLU B 206     -10.155 -53.452  13.001  1.00 19.20           C  
-ATOM   3639  OE1 GLU B 206     -10.589 -54.567  13.376  1.00 22.68           O  
-ATOM   3640  OE2 GLU B 206     -10.845 -52.406  13.025  1.00 20.88           O  
-ATOM   3641  N   PRO B 207      -6.301 -49.913  10.414  1.00 16.56           N  
-ATOM   3642  CA  PRO B 207      -6.547 -50.731   9.226  1.00 16.32           C  
-ATOM   3643  C   PRO B 207      -5.339 -51.563   8.788  1.00 16.09           C  
-ATOM   3644  O   PRO B 207      -4.191 -51.126   8.934  1.00 15.93           O  
-ATOM   3645  CB  PRO B 207      -6.863 -49.684   8.161  1.00 16.59           C  
-ATOM   3646  CG  PRO B 207      -6.018 -48.497   8.553  1.00 16.28           C  
-ATOM   3647  CD  PRO B 207      -5.930 -48.530  10.060  1.00 16.71           C  
-ATOM   3648  N   HIS B 208      -5.618 -52.751   8.253  1.00 15.96           N  
-ATOM   3649  CA  HIS B 208      -4.607 -53.622   7.647  1.00 15.40           C  
-ATOM   3650  C   HIS B 208      -5.287 -54.829   7.001  1.00 15.46           C  
-ATOM   3651  O   HIS B 208      -6.226 -55.384   7.576  1.00 15.49           O  
-ATOM   3652  CB  HIS B 208      -3.579 -54.101   8.680  1.00 15.71           C  
-ATOM   3653  CG  HIS B 208      -2.388 -54.774   8.069  1.00 15.10           C  
-ATOM   3654  ND1 HIS B 208      -1.197 -54.117   7.846  1.00 15.30           N  
-ATOM   3655  CD2 HIS B 208      -2.219 -56.031   7.596  1.00 14.51           C  
-ATOM   3656  CE1 HIS B 208      -0.339 -54.949   7.282  1.00 14.66           C  
-ATOM   3657  NE2 HIS B 208      -0.935 -56.116   7.117  1.00 15.08           N  
-ATOM   3658  N   PRO B 209      -4.834 -55.220   5.804  1.00 15.49           N  
-ATOM   3659  CA  PRO B 209      -5.311 -56.445   5.145  1.00 15.32           C  
-ATOM   3660  C   PRO B 209      -5.312 -57.712   6.022  1.00 15.23           C  
-ATOM   3661  O   PRO B 209      -6.048 -58.650   5.725  1.00 14.93           O  
-ATOM   3662  CB  PRO B 209      -4.330 -56.614   3.984  1.00 15.53           C  
-ATOM   3663  CG  PRO B 209      -3.902 -55.225   3.653  1.00 15.42           C  
-ATOM   3664  CD  PRO B 209      -3.861 -54.492   4.962  1.00 15.36           C  
-ATOM   3665  N   MET B 210      -4.503 -57.737   7.082  1.00 15.52           N  
-ATOM   3666  CA  MET B 210      -4.460 -58.881   8.015  1.00 15.69           C  
-ATOM   3667  C   MET B 210      -5.838 -59.208   8.585  1.00 15.71           C  
-ATOM   3668  O   MET B 210      -6.120 -60.354   8.932  1.00 15.94           O  
-ATOM   3669  CB  MET B 210      -3.452 -58.645   9.161  1.00 15.71           C  
-ATOM   3670  CG  MET B 210      -3.917 -57.682  10.276  1.00 15.55           C  
-ATOM   3671  SD  MET B 210      -2.803 -57.637  11.710  1.00 15.99           S  
-ATOM   3672  CE  MET B 210      -1.548 -56.475  11.160  1.00 15.51           C  
-ATOM   3673  N   ASN B 211      -6.689 -58.191   8.686  1.00 15.94           N  
-ATOM   3674  CA  ASN B 211      -8.033 -58.364   9.226  1.00 16.22           C  
-ATOM   3675  C   ASN B 211      -8.960 -59.142   8.290  1.00 16.07           C  
-ATOM   3676  O   ASN B 211      -9.921 -59.766   8.743  1.00 15.98           O  
-ATOM   3677  CB  ASN B 211      -8.627 -57.010   9.616  1.00 16.11           C  
-ATOM   3678  CG  ASN B 211      -7.818 -56.324  10.694  1.00 16.72           C  
-ATOM   3679  OD1 ASN B 211      -7.891 -56.691  11.868  1.00 17.37           O  
-ATOM   3680  ND2 ASN B 211      -7.025 -55.331  10.300  1.00 16.15           N  
-ATOM   3681  N   ALA B 212      -8.658 -59.109   6.992  1.00 16.27           N  
-ATOM   3682  CA  ALA B 212      -9.386 -59.908   6.006  1.00 16.48           C  
-ATOM   3683  C   ALA B 212      -8.639 -61.185   5.611  1.00 16.74           C  
-ATOM   3684  O   ALA B 212      -9.263 -62.187   5.265  1.00 16.18           O  
-ATOM   3685  CB  ALA B 212      -9.704 -59.074   4.775  1.00 16.89           C  
-ATOM   3686  N   ASN B 213      -7.306 -61.146   5.666  1.00 16.98           N  
-ATOM   3687  CA  ASN B 213      -6.476 -62.285   5.250  1.00 17.46           C  
-ATOM   3688  C   ASN B 213      -6.361 -63.369   6.320  1.00 17.66           C  
-ATOM   3689  O   ASN B 213      -6.074 -64.532   6.016  1.00 17.63           O  
-ATOM   3690  CB  ASN B 213      -5.077 -61.814   4.830  1.00 17.57           C  
-ATOM   3691  CG  ASN B 213      -5.090 -60.951   3.571  1.00 17.99           C  
-ATOM   3692  OD1 ASN B 213      -4.108 -60.273   3.268  1.00 17.87           O  
-ATOM   3693  ND2 ASN B 213      -6.199 -60.972   2.836  1.00 18.82           N  
-ATOM   3694  N   PHE B 214      -6.577 -62.972   7.570  1.00 18.01           N  
-ATOM   3695  CA  PHE B 214      -6.547 -63.889   8.697  1.00 18.61           C  
-ATOM   3696  C   PHE B 214      -7.805 -63.711   9.538  1.00 18.88           C  
-ATOM   3697  O   PHE B 214      -8.398 -62.629   9.572  1.00 18.64           O  
-ATOM   3698  CB  PHE B 214      -5.328 -63.615   9.592  1.00 18.69           C  
-ATOM   3699  CG  PHE B 214      -3.999 -63.826   8.920  1.00 19.20           C  
-ATOM   3700  CD1 PHE B 214      -3.258 -62.740   8.461  1.00 19.93           C  
-ATOM   3701  CD2 PHE B 214      -3.473 -65.108   8.770  1.00 19.86           C  
-ATOM   3702  CE1 PHE B 214      -2.019 -62.927   7.849  1.00 20.18           C  
-ATOM   3703  CE2 PHE B 214      -2.238 -65.306   8.152  1.00 20.18           C  
-ATOM   3704  CZ  PHE B 214      -1.511 -64.215   7.691  1.00 19.75           C  
-ATOM   3705  N   LYS B 215      -8.208 -64.780  10.212  1.00 19.32           N  
-ATOM   3706  CA ALYS B 215      -9.290 -64.707  11.182  0.50 19.60           C  
-ATOM   3707  CA BLYS B 215      -9.298 -64.708  11.176  0.50 19.65           C  
-ATOM   3708  C   LYS B 215      -8.696 -64.537  12.570  1.00 19.78           C  
-ATOM   3709  O   LYS B 215      -8.244 -65.506  13.195  1.00 20.11           O  
-ATOM   3710  CB ALYS B 215     -10.198 -65.939  11.091  0.50 19.70           C  
-ATOM   3711  CB BLYS B 215     -10.194 -65.950  11.089  0.50 19.77           C  
-ATOM   3712  CG ALYS B 215     -11.537 -65.670  10.413  0.50 19.73           C  
-ATOM   3713  CG BLYS B 215     -11.653 -65.689  11.450  0.50 20.09           C  
-ATOM   3714  CD ALYS B 215     -11.380 -64.982   9.059  0.50 20.04           C  
-ATOM   3715  CD BLYS B 215     -11.893 -65.757  12.950  0.50 20.36           C  
-ATOM   3716  CE ALYS B 215     -12.582 -64.108   8.740  0.50 19.99           C  
-ATOM   3717  CE BLYS B 215     -13.081 -64.901  13.368  0.50 20.96           C  
-ATOM   3718  NZ ALYS B 215     -13.805 -64.906   8.477  0.50 19.75           N  
-ATOM   3719  NZ BLYS B 215     -12.734 -63.448  13.383  0.50 21.16           N  
-ATOM   3720  N   LEU B 216      -8.679 -63.291  13.034  1.00 19.75           N  
-ATOM   3721  CA  LEU B 216      -7.995 -62.924  14.264  1.00 19.72           C  
-ATOM   3722  C   LEU B 216      -8.944 -62.496  15.368  1.00 19.45           C  
-ATOM   3723  O   LEU B 216     -10.068 -62.060  15.114  1.00 19.18           O  
-ATOM   3724  CB  LEU B 216      -6.991 -61.794  14.001  1.00 19.95           C  
-ATOM   3725  CG  LEU B 216      -6.072 -61.898  12.783  1.00 20.92           C  
-ATOM   3726  CD1 LEU B 216      -5.247 -60.624  12.650  1.00 22.05           C  
-ATOM   3727  CD2 LEU B 216      -5.185 -63.149  12.857  1.00 21.43           C  
-ATOM   3728  N   THR B 217      -8.454 -62.616  16.596  1.00 19.26           N  
-ATOM   3729  CA  THR B 217      -9.178 -62.201  17.782  1.00 19.14           C  
-ATOM   3730  C   THR B 217      -8.320 -61.177  18.505  1.00 19.04           C  
-ATOM   3731  O   THR B 217      -7.214 -61.499  18.937  1.00 19.06           O  
-ATOM   3732  CB  THR B 217      -9.432 -63.425  18.691  1.00 19.51           C  
-ATOM   3733  OG1 THR B 217     -10.284 -64.359  18.013  1.00 18.92           O  
-ATOM   3734  CG2 THR B 217     -10.238 -63.032  19.928  1.00 19.32           C  
-ATOM   3735  N   TYR B 218      -8.816 -59.945  18.615  1.00 18.70           N  
-ATOM   3736  CA  TYR B 218      -8.149 -58.928  19.419  1.00 18.53           C  
-ATOM   3737  C   TYR B 218      -8.429 -59.238  20.879  1.00 18.50           C  
-ATOM   3738  O   TYR B 218      -9.550 -59.615  21.228  1.00 18.27           O  
-ATOM   3739  CB  TYR B 218      -8.638 -57.522  19.051  1.00 18.57           C  
-ATOM   3740  CG  TYR B 218      -8.115 -57.036  17.718  1.00 18.65           C  
-ATOM   3741  CD1 TYR B 218      -8.811 -57.291  16.538  1.00 18.67           C  
-ATOM   3742  CD2 TYR B 218      -6.917 -56.327  17.639  1.00 18.84           C  
-ATOM   3743  CE1 TYR B 218      -8.327 -56.853  15.309  1.00 19.49           C  
-ATOM   3744  CE2 TYR B 218      -6.424 -55.884  16.420  1.00 18.77           C  
-ATOM   3745  CZ  TYR B 218      -7.131 -56.146  15.261  1.00 19.08           C  
-ATOM   3746  OH  TYR B 218      -6.641 -55.705  14.054  1.00 19.15           O  
-ATOM   3747  N   LEU B 219      -7.413 -59.105  21.724  1.00 17.83           N  
-ATOM   3748  CA  LEU B 219      -7.555 -59.493  23.123  1.00 17.90           C  
-ATOM   3749  C   LEU B 219      -8.115 -58.340  23.940  1.00 17.75           C  
-ATOM   3750  O   LEU B 219      -7.734 -57.192  23.730  1.00 17.66           O  
-ATOM   3751  CB  LEU B 219      -6.214 -59.959  23.712  1.00 17.60           C  
-ATOM   3752  CG  LEU B 219      -5.451 -61.084  23.003  1.00 17.85           C  
-ATOM   3753  CD1 LEU B 219      -4.114 -61.355  23.701  1.00 16.88           C  
-ATOM   3754  CD2 LEU B 219      -6.274 -62.365  22.894  1.00 16.44           C  
-ATOM   3755  N   SER B 220      -9.030 -58.656  24.855  1.00 17.86           N  
-ATOM   3756  CA  SER B 220      -9.528 -57.686  25.824  1.00 17.92           C  
-ATOM   3757  C   SER B 220      -8.490 -57.508  26.932  1.00 18.00           C  
-ATOM   3758  O   SER B 220      -7.468 -58.202  26.950  1.00 17.55           O  
-ATOM   3759  CB  SER B 220     -10.872 -58.143  26.413  1.00 18.35           C  
-ATOM   3760  OG  SER B 220     -10.789 -59.457  26.947  1.00 18.13           O  
-ATOM   3761  N   GLY B 221      -8.738 -56.556  27.830  1.00 17.72           N  
-ATOM   3762  CA  GLY B 221      -7.923 -56.397  29.030  1.00 18.03           C  
-ATOM   3763  C   GLY B 221      -6.592 -55.683  28.882  1.00 17.97           C  
-ATOM   3764  O   GLY B 221      -5.806 -55.636  29.829  1.00 17.74           O  
-ATOM   3765  N   GLY B 222      -6.329 -55.126  27.702  1.00 18.18           N  
-ATOM   3766  CA  GLY B 222      -5.119 -54.333  27.488  1.00 18.30           C  
-ATOM   3767  C   GLY B 222      -5.345 -52.840  27.630  1.00 18.38           C  
-ATOM   3768  O   GLY B 222      -4.496 -52.043  27.243  1.00 18.47           O  
-ATOM   3769  N   ASP B 223      -6.492 -52.474  28.204  1.00 18.43           N  
-ATOM   3770  CA  ASP B 223      -6.923 -51.080  28.346  1.00 18.41           C  
-ATOM   3771  C   ASP B 223      -5.851 -50.143  28.905  1.00 18.27           C  
-ATOM   3772  O   ASP B 223      -5.680 -49.022  28.422  1.00 18.03           O  
-ATOM   3773  CB  ASP B 223      -8.157 -51.002  29.253  1.00 18.70           C  
-ATOM   3774  CG  ASP B 223      -9.370 -51.704  28.667  1.00 19.09           C  
-ATOM   3775  OD1 ASP B 223     -10.489 -51.178  28.835  1.00 19.45           O  
-ATOM   3776  OD2 ASP B 223      -9.312 -52.778  28.036  1.00 20.56           O  
-ATOM   3777  N   ASP B 224      -5.147 -50.608  29.933  1.00 17.90           N  
-ATOM   3778  CA  ASP B 224      -4.224 -49.766  30.687  1.00 17.90           C  
-ATOM   3779  C   ASP B 224      -2.853 -49.688  30.022  1.00 17.77           C  
-ATOM   3780  O   ASP B 224      -1.999 -48.897  30.431  1.00 17.87           O  
-ATOM   3781  CB  ASP B 224      -4.087 -50.286  32.122  1.00 17.51           C  
-ATOM   3782  CG  ASP B 224      -5.419 -50.382  32.849  1.00 17.79           C  
-ATOM   3783  OD1 ASP B 224      -6.437 -49.848  32.354  1.00 17.33           O  
-ATOM   3784  OD2 ASP B 224      -5.539 -50.966  33.947  1.00 18.24           O  
-ATOM   3785  N   VAL B 225      -2.661 -50.504  28.988  1.00 17.76           N  
-ATOM   3786  CA  VAL B 225      -1.386 -50.613  28.289  1.00 17.54           C  
-ATOM   3787  C   VAL B 225      -1.508 -50.047  26.868  1.00 17.59           C  
-ATOM   3788  O   VAL B 225      -0.843 -49.064  26.518  1.00 17.62           O  
-ATOM   3789  CB  VAL B 225      -0.906 -52.093  28.251  1.00 17.52           C  
-ATOM   3790  CG1 VAL B 225       0.475 -52.211  27.611  1.00 16.79           C  
-ATOM   3791  CG2 VAL B 225      -0.906 -52.692  29.653  1.00 17.62           C  
-ATOM   3792  N   PHE B 226      -2.375 -50.659  26.068  1.00 17.41           N  
-ATOM   3793  CA  PHE B 226      -2.581 -50.258  24.674  1.00 17.42           C  
-ATOM   3794  C   PHE B 226      -3.763 -49.301  24.511  1.00 17.54           C  
-ATOM   3795  O   PHE B 226      -3.888 -48.621  23.488  1.00 17.62           O  
-ATOM   3796  CB  PHE B 226      -2.751 -51.494  23.778  1.00 17.19           C  
-ATOM   3797  CG  PHE B 226      -1.446 -52.138  23.379  1.00 17.09           C  
-ATOM   3798  CD1 PHE B 226      -0.783 -52.997  24.250  1.00 17.68           C  
-ATOM   3799  CD2 PHE B 226      -0.881 -51.877  22.130  1.00 16.94           C  
-ATOM   3800  CE1 PHE B 226       0.428 -53.591  23.892  1.00 17.29           C  
-ATOM   3801  CE2 PHE B 226       0.324 -52.465  21.756  1.00 17.02           C  
-ATOM   3802  CZ  PHE B 226       0.982 -53.326  22.643  1.00 17.23           C  
-ATOM   3803  N   GLY B 227      -4.621 -49.244  25.526  1.00 17.77           N  
-ATOM   3804  CA  GLY B 227      -5.794 -48.382  25.480  1.00 18.20           C  
-ATOM   3805  C   GLY B 227      -7.091 -49.166  25.456  1.00 18.72           C  
-ATOM   3806  O   GLY B 227      -7.117 -50.324  25.010  1.00 18.63           O  
-ATOM   3807  N   PRO B 228      -8.167 -48.539  25.939  1.00 19.01           N  
-ATOM   3808  CA  PRO B 228      -9.493 -49.155  25.953  1.00 19.31           C  
-ATOM   3809  C   PRO B 228     -10.033 -49.452  24.559  1.00 19.64           C  
-ATOM   3810  O   PRO B 228      -9.485 -48.972  23.556  1.00 19.36           O  
-ATOM   3811  CB  PRO B 228     -10.365 -48.099  26.643  1.00 19.43           C  
-ATOM   3812  CG  PRO B 228      -9.633 -46.820  26.463  1.00 19.62           C  
-ATOM   3813  CD  PRO B 228      -8.184 -47.190  26.536  1.00 19.12           C  
-ATOM   3814  N   ASN B 229     -11.105 -50.241  24.517  1.00 19.90           N  
-ATOM   3815  CA  ASN B 229     -11.762 -50.637  23.273  1.00 20.33           C  
-ATOM   3816  C   ASN B 229     -10.777 -51.253  22.277  1.00 20.19           C  
-ATOM   3817  O   ASN B 229     -10.665 -50.810  21.133  1.00 20.12           O  
-ATOM   3818  CB  ASN B 229     -12.530 -49.457  22.662  1.00 20.56           C  
-ATOM   3819  CG  ASN B 229     -13.556 -48.873  23.615  1.00 21.36           C  
-ATOM   3820  OD1 ASN B 229     -14.340 -49.601  24.230  1.00 22.81           O  
-ATOM   3821  ND2 ASN B 229     -13.558 -47.553  23.742  1.00 22.53           N  
-ATOM   3822  N   TYR B 230     -10.052 -52.265  22.751  1.00 20.34           N  
-ATOM   3823  CA  TYR B 230      -9.079 -53.013  21.951  1.00 20.50           C  
-ATOM   3824  C   TYR B 230      -8.017 -52.101  21.327  1.00 20.21           C  
-ATOM   3825  O   TYR B 230      -7.655 -52.247  20.155  1.00 20.79           O  
-ATOM   3826  CB  TYR B 230      -9.795 -53.872  20.897  1.00 20.72           C  
-ATOM   3827  CG  TYR B 230     -10.836 -54.791  21.493  1.00 21.18           C  
-ATOM   3828  CD1 TYR B 230     -12.180 -54.412  21.541  1.00 21.31           C  
-ATOM   3829  CD2 TYR B 230     -10.477 -56.028  22.033  1.00 21.04           C  
-ATOM   3830  CE1 TYR B 230     -13.143 -55.246  22.103  1.00 21.89           C  
-ATOM   3831  CE2 TYR B 230     -11.434 -56.872  22.593  1.00 21.41           C  
-ATOM   3832  CZ  TYR B 230     -12.764 -56.475  22.625  1.00 21.89           C  
-ATOM   3833  OH  TYR B 230     -13.718 -57.305  23.180  1.00 22.39           O  
-ATOM   3834  N   GLY B 231      -7.528 -51.160  22.131  1.00 19.81           N  
-ATOM   3835  CA  GLY B 231      -6.518 -50.202  21.704  1.00 19.15           C  
-ATOM   3836  C   GLY B 231      -7.005 -49.214  20.664  1.00 18.76           C  
-ATOM   3837  O   GLY B 231      -6.278 -48.895  19.721  1.00 18.58           O  
-ATOM   3838  N   GLY B 232      -8.236 -48.730  20.829  1.00 18.59           N  
-ATOM   3839  CA  GLY B 232      -8.771 -47.682  19.960  1.00 18.21           C  
-ATOM   3840  C   GLY B 232      -7.729 -46.597  19.771  1.00 18.05           C  
-ATOM   3841  O   GLY B 232      -7.239 -46.022  20.744  1.00 18.13           O  
-ATOM   3842  N   ALA B 233      -7.375 -46.334  18.516  1.00 17.58           N  
-ATOM   3843  CA  ALA B 233      -6.280 -45.426  18.208  1.00 17.32           C  
-ATOM   3844  C   ALA B 233      -6.653 -44.337  17.209  1.00 17.22           C  
-ATOM   3845  O   ALA B 233      -7.637 -44.456  16.472  1.00 17.13           O  
-ATOM   3846  CB  ALA B 233      -5.066 -46.219  17.697  1.00 17.24           C  
-ATOM   3847  N   THR B 234      -5.854 -43.273  17.207  1.00 17.04           N  
-ATOM   3848  CA  THR B 234      -5.908 -42.240  16.177  1.00 17.14           C  
-ATOM   3849  C   THR B 234      -4.499 -41.995  15.653  1.00 17.15           C  
-ATOM   3850  O   THR B 234      -3.523 -42.160  16.385  1.00 17.02           O  
-ATOM   3851  CB  THR B 234      -6.492 -40.915  16.731  1.00 17.24           C  
-ATOM   3852  OG1 THR B 234      -5.743 -40.499  17.879  1.00 16.90           O  
-ATOM   3853  CG2 THR B 234      -7.902 -41.114  17.266  1.00 16.91           C  
-ATOM   3854  N   VAL B 235      -4.393 -41.619  14.383  1.00 17.33           N  
-ATOM   3855  CA  VAL B 235      -3.091 -41.384  13.765  1.00 17.31           C  
-ATOM   3856  C   VAL B 235      -2.961 -39.903  13.454  1.00 17.51           C  
-ATOM   3857  O   VAL B 235      -3.895 -39.281  12.934  1.00 17.47           O  
-ATOM   3858  CB  VAL B 235      -2.886 -42.218  12.481  1.00 17.16           C  
-ATOM   3859  CG1 VAL B 235      -1.411 -42.205  12.063  1.00 17.43           C  
-ATOM   3860  CG2 VAL B 235      -3.358 -43.658  12.687  1.00 16.50           C  
-ATOM   3861  N   HIS B 236      -1.799 -39.346  13.777  1.00 17.73           N  
-ATOM   3862  CA  HIS B 236      -1.585 -37.909  13.697  1.00 18.17           C  
-ATOM   3863  C   HIS B 236      -0.404 -37.557  12.804  1.00 18.52           C  
-ATOM   3864  O   HIS B 236       0.543 -38.340  12.658  1.00 18.36           O  
-ATOM   3865  CB  HIS B 236      -1.389 -37.320  15.097  1.00 18.28           C  
-ATOM   3866  CG  HIS B 236      -2.552 -37.546  16.013  1.00 18.29           C  
-ATOM   3867  ND1 HIS B 236      -3.467 -36.560  16.312  1.00 18.08           N  
-ATOM   3868  CD2 HIS B 236      -2.954 -38.649  16.687  1.00 18.68           C  
-ATOM   3869  CE1 HIS B 236      -4.381 -37.043  17.134  1.00 18.12           C  
-ATOM   3870  NE2 HIS B 236      -4.096 -38.311  17.374  1.00 18.75           N  
-ATOM   3871  N   THR B 237      -0.487 -36.382  12.189  1.00 18.79           N  
-ATOM   3872  CA  THR B 237       0.597 -35.855  11.378  1.00 19.14           C  
-ATOM   3873  C   THR B 237       1.463 -34.959  12.264  1.00 19.48           C  
-ATOM   3874  O   THR B 237       0.956 -34.050  12.925  1.00 19.54           O  
-ATOM   3875  CB  THR B 237       0.028 -35.072  10.173  1.00 19.06           C  
-ATOM   3876  OG1 THR B 237      -0.715 -35.959   9.331  1.00 18.70           O  
-ATOM   3877  CG2 THR B 237       1.142 -34.576   9.257  1.00 19.30           C  
-ATOM   3878  N   ASN B 238       2.761 -35.252  12.298  1.00 19.72           N  
-ATOM   3879  CA  ASN B 238       3.728 -34.440  13.027  1.00 20.00           C  
-ATOM   3880  C   ASN B 238       4.632 -33.672  12.075  1.00 20.44           C  
-ATOM   3881  O   ASN B 238       4.933 -34.145  10.972  1.00 20.10           O  
-ATOM   3882  CB  ASN B 238       4.609 -35.303  13.929  1.00 19.98           C  
-ATOM   3883  CG  ASN B 238       3.823 -36.075  14.980  1.00 19.89           C  
-ATOM   3884  OD1 ASN B 238       2.708 -35.709  15.362  1.00 21.76           O  
-ATOM   3885  ND2 ASN B 238       4.419 -37.144  15.464  1.00 18.00           N  
-ATOM   3886  N   VAL B 239       5.061 -32.487  12.507  1.00 20.91           N  
-ATOM   3887  CA  VAL B 239       6.052 -31.706  11.770  1.00 21.76           C  
-ATOM   3888  C   VAL B 239       7.126 -31.170  12.710  1.00 21.97           C  
-ATOM   3889  O   VAL B 239       6.873 -30.963  13.896  1.00 21.78           O  
-ATOM   3890  CB  VAL B 239       5.425 -30.526  10.975  1.00 21.76           C  
-ATOM   3891  CG1 VAL B 239       4.495 -31.034   9.879  1.00 22.07           C  
-ATOM   3892  CG2 VAL B 239       4.711 -29.544  11.907  1.00 22.31           C  
-ATOM   3893  N   ARG B 240       8.318 -30.941  12.168  1.00 22.64           N  
-ATOM   3894  CA  ARG B 240       9.416 -30.347  12.932  1.00 23.28           C  
-ATOM   3895  C   ARG B 240       9.166 -28.865  13.213  1.00 23.66           C  
-ATOM   3896  O   ARG B 240       8.204 -28.286  12.699  1.00 23.70           O  
-ATOM   3897  CB  ARG B 240      10.739 -30.512  12.176  1.00 23.38           C  
-ATOM   3898  CG  ARG B 240      10.802 -29.792  10.833  1.00 23.11           C  
-ATOM   3899  CD  ARG B 240      12.217 -29.559  10.335  1.00 23.56           C  
-ATOM   3900  NE  ARG B 240      12.245 -28.818   9.078  1.00 24.16           N  
-ATOM   3901  CZ  ARG B 240      12.249 -27.494   8.982  1.00 24.50           C  
-ATOM   3902  NH1 ARG B 240      12.220 -26.738  10.074  1.00 23.99           N  
-ATOM   3903  NH2 ARG B 240      12.279 -26.923   7.789  1.00 24.39           N  
-ATOM   3904  N   ALA B 241      10.040 -28.264  14.023  1.00 24.22           N  
-ATOM   3905  CA  ALA B 241      10.063 -26.807  14.245  1.00 24.77           C  
-ATOM   3906  C   ALA B 241       8.654 -26.270  14.592  1.00 25.15           C  
-ATOM   3907  O   ALA B 241       8.006 -26.882  15.444  1.00 25.60           O  
-ATOM   3908  CB  ALA B 241      10.698 -26.102  13.057  1.00 24.51           C  
-ATOM   3909  N   GLY B 242       8.152 -25.180  13.994  1.00 25.01           N  
-ATOM   3910  CA  GLY B 242       8.842 -24.318  13.027  1.00 25.18           C  
-ATOM   3911  C   GLY B 242       8.296 -24.384  11.606  1.00 25.21           C  
-ATOM   3912  O   GLY B 242       8.270 -23.377  10.892  1.00 25.04           O  
-ATOM   3913  N   TYR B 243       7.865 -25.577  11.199  1.00 25.26           N  
-ATOM   3914  CA  TYR B 243       7.436 -25.836   9.823  1.00 25.50           C  
-ATOM   3915  C   TYR B 243       6.144 -25.105   9.455  1.00 25.91           C  
-ATOM   3916  O   TYR B 243       5.912 -24.792   8.284  1.00 26.13           O  
-ATOM   3917  CB  TYR B 243       7.279 -27.342   9.601  1.00 25.29           C  
-ATOM   3918  CG  TYR B 243       7.445 -27.776   8.164  1.00 24.83           C  
-ATOM   3919  CD1 TYR B 243       8.697 -27.750   7.548  1.00 24.21           C  
-ATOM   3920  CD2 TYR B 243       6.356 -28.228   7.426  1.00 24.40           C  
-ATOM   3921  CE1 TYR B 243       8.855 -28.152   6.225  1.00 24.36           C  
-ATOM   3922  CE2 TYR B 243       6.503 -28.634   6.103  1.00 24.66           C  
-ATOM   3923  CZ  TYR B 243       7.753 -28.593   5.509  1.00 24.57           C  
-ATOM   3924  OH  TYR B 243       7.895 -28.998   4.203  1.00 24.89           O  
-ATOM   3925  N   THR B 244       5.319 -24.842  10.469  1.00 26.47           N  
-ATOM   3926  CA  THR B 244       4.052 -24.117  10.342  1.00 27.04           C  
-ATOM   3927  C   THR B 244       4.213 -22.805   9.584  1.00 27.19           C  
-ATOM   3928  O   THR B 244       3.361 -22.431   8.773  1.00 27.58           O  
-ATOM   3929  CB  THR B 244       3.496 -23.777  11.747  1.00 27.09           C  
-ATOM   3930  OG1 THR B 244       4.037 -24.675  12.727  1.00 27.81           O  
-ATOM   3931  CG2 THR B 244       1.991 -24.007  11.804  1.00 27.23           C  
-ATOM   3932  N   THR B 245       5.309 -22.110   9.871  1.00 27.26           N  
-ATOM   3933  CA  THR B 245       5.541 -20.758   9.373  1.00 27.12           C  
-ATOM   3934  C   THR B 245       6.606 -20.731   8.281  1.00 26.94           C  
-ATOM   3935  O   THR B 245       6.582 -19.865   7.406  1.00 26.86           O  
-ATOM   3936  CB  THR B 245       5.949 -19.829  10.538  1.00 27.28           C  
-ATOM   3937  OG1 THR B 245       7.131 -20.337  11.168  1.00 27.49           O  
-ATOM   3938  CG2 THR B 245       4.913 -19.875  11.656  1.00 27.26           C  
-ATOM   3939  N   GLU B 246       7.535 -21.683   8.345  1.00 26.71           N  
-ATOM   3940  CA  GLU B 246       8.634 -21.780   7.385  1.00 26.59           C  
-ATOM   3941  C   GLU B 246       8.126 -22.185   6.004  1.00 26.16           C  
-ATOM   3942  O   GLU B 246       8.555 -21.625   4.991  1.00 26.09           O  
-ATOM   3943  CB  GLU B 246       9.681 -22.782   7.882  1.00 26.66           C  
-ATOM   3944  CG  GLU B 246      11.047 -22.664   7.219  1.00 27.09           C  
-ATOM   3945  CD  GLU B 246      12.055 -23.658   7.773  1.00 27.33           C  
-ATOM   3946  OE1 GLU B 246      12.221 -23.725   9.015  1.00 28.36           O  
-ATOM   3947  OE2 GLU B 246      12.690 -24.372   6.965  1.00 28.10           O  
-ATOM   3948  N   CYS B 247       7.205 -23.151   5.976  1.00 25.57           N  
-ATOM   3949  CA  CYS B 247       6.645 -23.679   4.730  1.00 25.02           C  
-ATOM   3950  C   CYS B 247       5.111 -23.667   4.741  1.00 24.50           C  
-ATOM   3951  O   CYS B 247       4.482 -24.726   4.848  1.00 24.56           O  
-ATOM   3952  CB  CYS B 247       7.163 -25.098   4.481  1.00 25.10           C  
-ATOM   3953  SG  CYS B 247       8.957 -25.203   4.342  1.00 25.28           S  
-ATOM   3954  N   PRO B 248       4.513 -22.479   4.612  1.00 23.91           N  
-ATOM   3955  CA  PRO B 248       3.066 -22.313   4.785  1.00 23.48           C  
-ATOM   3956  C   PRO B 248       2.196 -23.070   3.778  1.00 22.96           C  
-ATOM   3957  O   PRO B 248       1.098 -23.492   4.130  1.00 22.76           O  
-ATOM   3958  CB  PRO B 248       2.862 -20.802   4.630  1.00 23.55           C  
-ATOM   3959  CG  PRO B 248       4.041 -20.328   3.861  1.00 23.95           C  
-ATOM   3960  CD  PRO B 248       5.176 -21.200   4.296  1.00 23.93           C  
-ATOM   3961  N   ASN B 249       2.675 -23.233   2.547  1.00 22.57           N  
-ATOM   3962  CA  ASN B 249       1.904 -23.937   1.521  1.00 22.28           C  
-ATOM   3963  C   ASN B 249       1.857 -25.445   1.767  1.00 22.13           C  
-ATOM   3964  O   ASN B 249       0.784 -26.048   1.715  1.00 22.01           O  
-ATOM   3965  CB  ASN B 249       2.435 -23.634   0.120  1.00 22.23           C  
-ATOM   3966  CG  ASN B 249       1.517 -24.153  -0.978  1.00 22.22           C  
-ATOM   3967  OD1 ASN B 249       0.326 -23.833  -1.017  1.00 21.62           O  
-ATOM   3968  ND2 ASN B 249       2.073 -24.953  -1.878  1.00 21.68           N  
-ATOM   3969  N   VAL B 250       3.018 -26.044   2.039  1.00 22.04           N  
-ATOM   3970  CA  VAL B 250       3.091 -27.465   2.399  1.00 22.04           C  
-ATOM   3971  C   VAL B 250       2.256 -27.721   3.651  1.00 22.39           C  
-ATOM   3972  O   VAL B 250       1.513 -28.701   3.715  1.00 22.48           O  
-ATOM   3973  CB  VAL B 250       4.549 -27.946   2.642  1.00 22.09           C  
-ATOM   3974  CG1 VAL B 250       4.580 -29.434   3.028  1.00 21.58           C  
-ATOM   3975  CG2 VAL B 250       5.414 -27.704   1.420  1.00 21.78           C  
-ATOM   3976  N   ASP B 251       2.377 -26.823   4.629  1.00 22.76           N  
-ATOM   3977  CA  ASP B 251       1.655 -26.928   5.898  1.00 23.27           C  
-ATOM   3978  C   ASP B 251       0.141 -26.962   5.686  1.00 23.26           C  
-ATOM   3979  O   ASP B 251      -0.571 -27.691   6.381  1.00 23.62           O  
-ATOM   3980  CB  ASP B 251       2.041 -25.774   6.831  1.00 23.53           C  
-ATOM   3981  CG  ASP B 251       1.435 -25.908   8.217  1.00 24.29           C  
-ATOM   3982  OD1 ASP B 251       1.714 -26.911   8.906  1.00 26.21           O  
-ATOM   3983  OD2 ASP B 251       0.675 -25.049   8.707  1.00 26.64           O  
-ATOM   3984  N   LYS B 252      -0.334 -26.188   4.714  1.00 23.09           N  
-ATOM   3985  CA  LYS B 252      -1.754 -26.139   4.366  1.00 22.92           C  
-ATOM   3986  C   LYS B 252      -2.274 -27.493   3.877  1.00 22.64           C  
-ATOM   3987  O   LYS B 252      -3.376 -27.908   4.244  1.00 22.50           O  
-ATOM   3988  CB  LYS B 252      -2.007 -25.062   3.308  1.00 22.92           C  
-ATOM   3989  CG  LYS B 252      -3.380 -24.398   3.401  1.00 23.77           C  
-ATOM   3990  CD  LYS B 252      -3.498 -23.497   4.633  1.00 24.55           C  
-ATOM   3991  CE  LYS B 252      -2.659 -22.229   4.495  1.00 25.44           C  
-ATOM   3992  NZ  LYS B 252      -2.655 -21.422   5.745  1.00 25.39           N  
-ATOM   3993  N   LEU B 253      -1.479 -28.172   3.052  1.00 22.41           N  
-ATOM   3994  CA  LEU B 253      -1.818 -29.518   2.591  1.00 22.16           C  
-ATOM   3995  C   LEU B 253      -1.919 -30.479   3.771  1.00 22.25           C  
-ATOM   3996  O   LEU B 253      -2.812 -31.323   3.816  1.00 22.10           O  
-ATOM   3997  CB  LEU B 253      -0.793 -30.024   1.568  1.00 21.91           C  
-ATOM   3998  CG  LEU B 253      -0.952 -31.461   1.051  1.00 21.47           C  
-ATOM   3999  CD1 LEU B 253      -2.174 -31.622   0.159  1.00 20.26           C  
-ATOM   4000  CD2 LEU B 253       0.307 -31.927   0.337  1.00 20.89           C  
-ATOM   4001  N   LEU B 254      -1.012 -30.329   4.732  1.00 22.55           N  
-ATOM   4002  CA  LEU B 254      -0.987 -31.189   5.911  1.00 22.90           C  
-ATOM   4003  C   LEU B 254      -2.166 -30.921   6.845  1.00 23.16           C  
-ATOM   4004  O   LEU B 254      -2.639 -31.832   7.520  1.00 23.16           O  
-ATOM   4005  CB  LEU B 254       0.353 -31.068   6.644  1.00 22.81           C  
-ATOM   4006  CG  LEU B 254       1.601 -31.397   5.813  1.00 22.87           C  
-ATOM   4007  CD1 LEU B 254       2.857 -31.157   6.629  1.00 23.23           C  
-ATOM   4008  CD2 LEU B 254       1.582 -32.830   5.258  1.00 22.55           C  
-ATOM   4009  N   GLN B 255      -2.638 -29.674   6.862  1.00 23.66           N  
-ATOM   4010  CA  GLN B 255      -3.843 -29.283   7.603  1.00 24.01           C  
-ATOM   4011  C   GLN B 255      -5.102 -29.928   7.019  1.00 23.93           C  
-ATOM   4012  O   GLN B 255      -6.056 -30.214   7.744  1.00 23.96           O  
-ATOM   4013  CB  GLN B 255      -4.020 -27.760   7.578  1.00 24.05           C  
-ATOM   4014  CG  GLN B 255      -3.120 -26.971   8.523  1.00 24.36           C  
-ATOM   4015  CD  GLN B 255      -3.223 -25.466   8.302  1.00 24.89           C  
-ATOM   4016  OE1 GLN B 255      -2.205 -24.775   8.251  1.00 26.98           O  
-ATOM   4017  NE2 GLN B 255      -4.448 -24.958   8.161  1.00 25.58           N  
-ATOM   4018  N   ASN B 256      -5.105 -30.122   5.702  1.00 23.90           N  
-ATOM   4019  CA  ASN B 256      -6.261 -30.666   4.995  1.00 23.90           C  
-ATOM   4020  C   ASN B 256      -6.216 -32.187   4.873  1.00 24.08           C  
-ATOM   4021  O   ASN B 256      -7.257 -32.834   4.736  1.00 24.16           O  
-ATOM   4022  CB  ASN B 256      -6.369 -30.058   3.590  1.00 23.64           C  
-ATOM   4023  CG  ASN B 256      -6.581 -28.547   3.601  1.00 23.49           C  
-ATOM   4024  OD1 ASN B 256      -7.032 -27.966   4.590  1.00 22.21           O  
-ATOM   4025  ND2 ASN B 256      -6.265 -27.908   2.480  1.00 22.99           N  
-ATOM   4026  N   LEU B 257      -5.008 -32.747   4.925  1.00 24.12           N  
-ATOM   4027  CA  LEU B 257      -4.788 -34.153   4.593  1.00 24.30           C  
-ATOM   4028  C   LEU B 257      -5.332 -35.098   5.661  1.00 24.46           C  
-ATOM   4029  O   LEU B 257      -4.757 -35.230   6.744  1.00 24.49           O  
-ATOM   4030  CB  LEU B 257      -3.297 -34.415   4.337  1.00 24.38           C  
-ATOM   4031  CG  LEU B 257      -2.834 -35.695   3.632  1.00 24.29           C  
-ATOM   4032  CD1 LEU B 257      -3.469 -35.860   2.252  1.00 24.56           C  
-ATOM   4033  CD2 LEU B 257      -1.314 -35.693   3.523  1.00 24.26           C  
-ATOM   4034  N   SER B 258      -6.456 -35.737   5.344  1.00 24.43           N  
-ATOM   4035  CA  SER B 258      -7.035 -36.759   6.206  1.00 24.35           C  
-ATOM   4036  C   SER B 258      -7.424 -37.978   5.381  1.00 24.35           C  
-ATOM   4037  O   SER B 258      -7.949 -37.858   4.270  1.00 24.34           O  
-ATOM   4038  CB  SER B 258      -8.249 -36.225   6.963  1.00 24.35           C  
-ATOM   4039  OG  SER B 258      -9.354 -36.056   6.098  1.00 24.82           O  
-ATOM   4040  N   PHE B 259      -7.174 -39.149   5.945  1.00 24.22           N  
-ATOM   4041  CA  PHE B 259      -7.398 -40.398   5.240  1.00 24.11           C  
-ATOM   4042  C   PHE B 259      -8.663 -41.074   5.769  1.00 24.35           C  
-ATOM   4043  O   PHE B 259      -9.358 -40.523   6.627  1.00 24.32           O  
-ATOM   4044  CB  PHE B 259      -6.160 -41.297   5.383  1.00 24.07           C  
-ATOM   4045  CG  PHE B 259      -4.855 -40.585   5.105  1.00 23.41           C  
-ATOM   4046  CD1 PHE B 259      -3.994 -40.254   6.144  1.00 23.30           C  
-ATOM   4047  CD2 PHE B 259      -4.496 -40.237   3.805  1.00 23.51           C  
-ATOM   4048  CE1 PHE B 259      -2.797 -39.596   5.894  1.00 23.34           C  
-ATOM   4049  CE2 PHE B 259      -3.301 -39.582   3.539  1.00 23.08           C  
-ATOM   4050  CZ  PHE B 259      -2.447 -39.260   4.589  1.00 24.33           C  
-ATOM   4051  N   SER B 260      -8.981 -42.245   5.228  1.00 24.34           N  
-ATOM   4052  CA  SER B 260     -10.060 -43.063   5.763  1.00 24.49           C  
-ATOM   4053  C   SER B 260      -9.576 -44.501   5.910  1.00 24.53           C  
-ATOM   4054  O   SER B 260      -8.581 -44.889   5.293  1.00 24.26           O  
-ATOM   4055  CB  SER B 260     -11.304 -42.993   4.870  1.00 24.57           C  
-ATOM   4056  OG  SER B 260     -11.064 -43.585   3.606  1.00 24.84           O  
-ATOM   4057  N   LEU B 261     -10.273 -45.275   6.739  1.00 24.75           N  
-ATOM   4058  CA  LEU B 261     -10.001 -46.707   6.902  1.00 25.06           C  
-ATOM   4059  C   LEU B 261     -10.079 -47.465   5.580  1.00 25.04           C  
-ATOM   4060  O   LEU B 261      -9.248 -48.330   5.306  1.00 24.96           O  
-ATOM   4061  CB  LEU B 261     -10.986 -47.321   7.900  1.00 25.09           C  
-ATOM   4062  CG  LEU B 261     -10.576 -47.596   9.352  1.00 25.53           C  
-ATOM   4063  CD1 LEU B 261      -9.627 -46.558   9.927  1.00 26.05           C  
-ATOM   4064  CD2 LEU B 261     -11.820 -47.731  10.221  1.00 25.23           C  
-ATOM   4065  N   GLN B 262     -11.081 -47.121   4.773  1.00 25.12           N  
-ATOM   4066  CA  GLN B 262     -11.351 -47.778   3.491  1.00 25.52           C  
-ATOM   4067  C   GLN B 262     -10.278 -47.428   2.461  1.00 25.37           C  
-ATOM   4068  O   GLN B 262      -9.764 -48.306   1.761  1.00 25.04           O  
-ATOM   4069  CB  GLN B 262     -12.742 -47.368   2.989  1.00 25.51           C  
-ATOM   4070  CG  GLN B 262     -13.342 -48.265   1.911  1.00 26.27           C  
-ATOM   4071  CD  GLN B 262     -14.776 -47.888   1.562  1.00 26.34           C  
-ATOM   4072  OE1 GLN B 262     -15.162 -46.718   1.659  1.00 27.85           O  
-ATOM   4073  NE2 GLN B 262     -15.568 -48.877   1.152  1.00 27.12           N  
-ATOM   4074  N   MET B 263      -9.940 -46.142   2.390  1.00 25.18           N  
-ATOM   4075  CA  MET B 263      -8.877 -45.647   1.523  1.00 25.51           C  
-ATOM   4076  C   MET B 263      -7.560 -46.361   1.791  1.00 24.43           C  
-ATOM   4077  O   MET B 263      -6.913 -46.853   0.866  1.00 24.27           O  
-ATOM   4078  CB  MET B 263      -8.684 -44.148   1.739  1.00 25.47           C  
-ATOM   4079  CG  MET B 263      -7.712 -43.507   0.778  1.00 26.29           C  
-ATOM   4080  SD  MET B 263      -6.760 -42.207   1.555  1.00 28.57           S  
-ATOM   4081  CE  MET B 263      -5.329 -43.168   2.024  1.00 27.05           C  
-ATOM   4082  N   GLU B 264      -7.165 -46.407   3.062  1.00 23.66           N  
-ATOM   4083  CA  GLU B 264      -5.899 -47.020   3.449  1.00 22.85           C  
-ATOM   4084  C   GLU B 264      -5.905 -48.526   3.186  1.00 22.60           C  
-ATOM   4085  O   GLU B 264      -4.936 -49.063   2.662  1.00 22.05           O  
-ATOM   4086  CB  GLU B 264      -5.558 -46.703   4.906  1.00 22.86           C  
-ATOM   4087  CG  GLU B 264      -5.107 -45.265   5.118  1.00 21.77           C  
-ATOM   4088  CD  GLU B 264      -4.506 -45.014   6.484  1.00 21.35           C  
-ATOM   4089  OE1 GLU B 264      -3.932 -45.950   7.077  1.00 21.66           O  
-ATOM   4090  OE2 GLU B 264      -4.592 -43.863   6.959  1.00 20.88           O  
-ATOM   4091  N   ASN B 265      -7.003 -49.192   3.540  1.00 22.30           N  
-ATOM   4092  CA  ASN B 265      -7.166 -50.613   3.256  1.00 22.31           C  
-ATOM   4093  C   ASN B 265      -7.033 -50.957   1.775  1.00 22.25           C  
-ATOM   4094  O   ASN B 265      -6.396 -51.947   1.424  1.00 21.93           O  
-ATOM   4095  CB  ASN B 265      -8.486 -51.143   3.826  1.00 22.45           C  
-ATOM   4096  CG  ASN B 265      -8.325 -51.710   5.221  1.00 22.79           C  
-ATOM   4097  OD1 ASN B 265      -7.323 -52.358   5.523  1.00 24.10           O  
-ATOM   4098  ND2 ASN B 265      -9.310 -51.472   6.079  1.00 22.95           N  
-ATOM   4099  N   GLU B 266      -7.609 -50.121   0.916  1.00 22.22           N  
-ATOM   4100  CA  GLU B 266      -7.563 -50.353  -0.528  1.00 22.87           C  
-ATOM   4101  C   GLU B 266      -6.145 -50.237  -1.087  1.00 22.38           C  
-ATOM   4102  O   GLU B 266      -5.701 -51.107  -1.840  1.00 22.22           O  
-ATOM   4103  CB  GLU B 266      -8.529 -49.422  -1.262  1.00 22.70           C  
-ATOM   4104  CG  GLU B 266      -9.991 -49.745  -0.995  1.00 23.91           C  
-ATOM   4105  CD  GLU B 266     -10.953 -48.865  -1.772  1.00 24.30           C  
-ATOM   4106  OE1 GLU B 266     -10.513 -48.189  -2.730  1.00 26.56           O  
-ATOM   4107  OE2 GLU B 266     -12.156 -48.858  -1.426  1.00 25.50           O  
-ATOM   4108  N   ILE B 267      -5.435 -49.176  -0.700  1.00 22.00           N  
-ATOM   4109  CA  ILE B 267      -4.047 -48.989  -1.130  1.00 21.52           C  
-ATOM   4110  C   ILE B 267      -3.139 -50.057  -0.515  1.00 21.44           C  
-ATOM   4111  O   ILE B 267      -2.287 -50.615  -1.203  1.00 20.90           O  
-ATOM   4112  CB  ILE B 267      -3.531 -47.555  -0.810  1.00 21.57           C  
-ATOM   4113  CG1 ILE B 267      -4.449 -46.502  -1.442  1.00 21.53           C  
-ATOM   4114  CG2 ILE B 267      -2.077 -47.375  -1.284  1.00 21.17           C  
-ATOM   4115  CD1 ILE B 267      -4.058 -45.058  -1.155  1.00 21.19           C  
-ATOM   4116  N   MET B 268      -3.338 -50.347   0.771  1.00 21.32           N  
-ATOM   4117  CA  MET B 268      -2.593 -51.419   1.437  1.00 21.71           C  
-ATOM   4118  C   MET B 268      -2.816 -52.774   0.762  1.00 21.38           C  
-ATOM   4119  O   MET B 268      -1.882 -53.572   0.635  1.00 21.37           O  
-ATOM   4120  CB  MET B 268      -2.963 -51.506   2.919  1.00 21.42           C  
-ATOM   4121  CG  MET B 268      -2.353 -50.417   3.778  1.00 21.60           C  
-ATOM   4122  SD  MET B 268      -2.712 -50.668   5.530  1.00 23.57           S  
-ATOM   4123  CE  MET B 268      -4.404 -50.156   5.643  1.00 22.89           C  
-ATOM   4124  N   GLY B 269      -4.054 -53.019   0.332  1.00 21.04           N  
-ATOM   4125  CA  GLY B 269      -4.407 -54.237  -0.394  1.00 20.85           C  
-ATOM   4126  C   GLY B 269      -3.634 -54.377  -1.694  1.00 20.84           C  
-ATOM   4127  O   GLY B 269      -3.118 -55.446  -1.996  1.00 20.37           O  
-ATOM   4128  N   LYS B 270      -3.542 -53.283  -2.448  1.00 20.82           N  
-ATOM   4129  CA  LYS B 270      -2.757 -53.245  -3.684  1.00 21.25           C  
-ATOM   4130  C   LYS B 270      -1.286 -53.572  -3.404  1.00 21.51           C  
-ATOM   4131  O   LYS B 270      -0.691 -54.411  -4.076  1.00 21.57           O  
-ATOM   4132  CB  LYS B 270      -2.865 -51.866  -4.344  1.00 20.90           C  
-ATOM   4133  CG  LYS B 270      -4.259 -51.471  -4.796  1.00 21.16           C  
-ATOM   4134  CD  LYS B 270      -4.276 -50.037  -5.315  1.00 21.29           C  
-ATOM   4135  CE  LYS B 270      -5.675 -49.589  -5.727  1.00 21.85           C  
-ATOM   4136  NZ  LYS B 270      -6.187 -50.321  -6.927  1.00 21.19           N  
-ATOM   4137  N   ILE B 271      -0.718 -52.917  -2.393  1.00 21.86           N  
-ATOM   4138  CA  ILE B 271       0.679 -53.120  -2.005  1.00 22.11           C  
-ATOM   4139  C   ILE B 271       0.952 -54.542  -1.496  1.00 22.36           C  
-ATOM   4140  O   ILE B 271       1.871 -55.207  -1.985  1.00 22.13           O  
-ATOM   4141  CB  ILE B 271       1.120 -52.044  -0.967  1.00 22.18           C  
-ATOM   4142  CG1 ILE B 271       1.058 -50.646  -1.598  1.00 22.17           C  
-ATOM   4143  CG2 ILE B 271       2.528 -52.328  -0.439  1.00 22.33           C  
-ATOM   4144  CD1 ILE B 271       1.055 -49.494  -0.603  1.00 22.34           C  
-ATOM   4145  N   LEU B 272       0.152 -55.002  -0.533  1.00 22.41           N  
-ATOM   4146  CA  LEU B 272       0.387 -56.295   0.125  1.00 22.77           C  
-ATOM   4147  C   LEU B 272      -0.126 -57.512  -0.632  1.00 22.66           C  
-ATOM   4148  O   LEU B 272       0.616 -58.477  -0.834  1.00 22.57           O  
-ATOM   4149  CB  LEU B 272      -0.199 -56.305   1.542  1.00 22.90           C  
-ATOM   4150  CG  LEU B 272       0.673 -55.780   2.679  1.00 23.67           C  
-ATOM   4151  CD1 LEU B 272       0.018 -56.122   3.999  1.00 25.10           C  
-ATOM   4152  CD2 LEU B 272       2.083 -56.357   2.627  1.00 25.27           C  
-ATOM   4153  N   ASN B 273      -1.400 -57.480  -1.017  1.00 22.58           N  
-ATOM   4154  CA  ASN B 273      -2.014 -58.620  -1.691  1.00 22.97           C  
-ATOM   4155  C   ASN B 273      -1.523 -58.747  -3.124  1.00 23.10           C  
-ATOM   4156  O   ASN B 273      -1.235 -59.846  -3.586  1.00 23.31           O  
-ATOM   4157  CB  ASN B 273      -3.543 -58.528  -1.667  1.00 22.84           C  
-ATOM   4158  CG  ASN B 273      -4.115 -58.544  -0.260  1.00 23.30           C  
-ATOM   4159  OD1 ASN B 273      -3.560 -59.159   0.644  1.00 22.51           O  
-ATOM   4160  ND2 ASN B 273      -5.242 -57.863  -0.074  1.00 24.08           N  
-ATOM   4161  N   ASP B 274      -1.413 -57.613  -3.812  1.00 23.35           N  
-ATOM   4162  CA  ASP B 274      -1.073 -57.597  -5.231  1.00 23.36           C  
-ATOM   4163  C   ASP B 274       0.391 -57.239  -5.507  1.00 23.33           C  
-ATOM   4164  O   ASP B 274       0.831 -57.246  -6.662  1.00 23.03           O  
-ATOM   4165  CB  ASP B 274      -2.017 -56.656  -5.991  1.00 23.61           C  
-ATOM   4166  CG  ASP B 274      -3.471 -57.106  -5.925  1.00 24.48           C  
-ATOM   4167  OD1 ASP B 274      -3.730 -58.282  -5.587  1.00 24.69           O  
-ATOM   4168  OD2 ASP B 274      -4.424 -56.349  -6.204  1.00 26.01           O  
-ATOM   4169  N   GLY B 275       1.131 -56.914  -4.448  1.00 23.17           N  
-ATOM   4170  CA  GLY B 275       2.567 -56.642  -4.548  1.00 23.22           C  
-ATOM   4171  C   GLY B 275       2.932 -55.396  -5.336  1.00 23.16           C  
-ATOM   4172  O   GLY B 275       4.044 -55.296  -5.861  1.00 23.32           O  
-ATOM   4173  N   GLU B 276       2.003 -54.443  -5.403  1.00 23.11           N  
-ATOM   4174  CA  GLU B 276       2.191 -53.214  -6.172  1.00 22.93           C  
-ATOM   4175  C   GLU B 276       3.148 -52.237  -5.504  1.00 23.32           C  
-ATOM   4176  O   GLU B 276       3.285 -52.223  -4.275  1.00 23.31           O  
-ATOM   4177  CB  GLU B 276       0.851 -52.520  -6.410  1.00 22.99           C  
-ATOM   4178  CG  GLU B 276      -0.002 -53.170  -7.485  1.00 22.32           C  
-ATOM   4179  CD  GLU B 276      -1.255 -52.382  -7.802  1.00 22.34           C  
-ATOM   4180  OE1 GLU B 276      -1.245 -51.138  -7.669  1.00 21.26           O  
-ATOM   4181  OE2 GLU B 276      -2.249 -53.015  -8.210  1.00 22.92           O  
-ATOM   4182  N   ASP B 277       3.805 -51.430  -6.334  1.00 23.51           N  
-ATOM   4183  CA  ASP B 277       4.627 -50.323  -5.871  1.00 23.69           C  
-ATOM   4184  C   ASP B 277       3.727 -49.300  -5.173  1.00 23.68           C  
-ATOM   4185  O   ASP B 277       2.694 -48.913  -5.719  1.00 23.62           O  
-ATOM   4186  CB  ASP B 277       5.359 -49.678  -7.051  1.00 23.89           C  
-ATOM   4187  CG  ASP B 277       6.198 -48.484  -6.637  1.00 24.60           C  
-ATOM   4188  OD1 ASP B 277       7.278 -48.685  -6.039  1.00 25.33           O  
-ATOM   4189  OD2 ASP B 277       5.855 -47.307  -6.870  1.00 25.09           O  
-ATOM   4190  N   PRO B 278       4.109 -48.882  -3.966  1.00 23.60           N  
-ATOM   4191  CA  PRO B 278       3.305 -47.945  -3.175  1.00 23.75           C  
-ATOM   4192  C   PRO B 278       2.914 -46.667  -3.915  1.00 23.88           C  
-ATOM   4193  O   PRO B 278       1.762 -46.242  -3.827  1.00 23.89           O  
-ATOM   4194  CB  PRO B 278       4.216 -47.629  -1.989  1.00 23.57           C  
-ATOM   4195  CG  PRO B 278       5.029 -48.866  -1.836  1.00 23.80           C  
-ATOM   4196  CD  PRO B 278       5.331 -49.293  -3.250  1.00 23.48           C  
-ATOM   4197  N   GLU B 279       3.856 -46.074  -4.648  1.00 24.08           N  
-ATOM   4198  CA  GLU B 279       3.587 -44.842  -5.386  1.00 24.45           C  
-ATOM   4199  C   GLU B 279       2.633 -45.091  -6.548  1.00 23.91           C  
-ATOM   4200  O   GLU B 279       1.738 -44.285  -6.807  1.00 23.65           O  
-ATOM   4201  CB  GLU B 279       4.887 -44.199  -5.875  1.00 24.42           C  
-ATOM   4202  CG  GLU B 279       5.635 -43.436  -4.791  1.00 25.55           C  
-ATOM   4203  CD  GLU B 279       6.973 -42.902  -5.263  1.00 25.72           C  
-ATOM   4204  OE1 GLU B 279       7.842 -43.716  -5.655  1.00 27.68           O  
-ATOM   4205  OE2 GLU B 279       7.160 -41.667  -5.237  1.00 27.56           O  
-ATOM   4206  N   LYS B 280       2.822 -46.219  -7.229  1.00 23.68           N  
-ATOM   4207  CA  LYS B 280       1.943 -46.614  -8.326  1.00 23.56           C  
-ATOM   4208  C   LYS B 280       0.538 -46.964  -7.824  1.00 23.12           C  
-ATOM   4209  O   LYS B 280      -0.455 -46.631  -8.472  1.00 22.83           O  
-ATOM   4210  CB  LYS B 280       2.558 -47.761  -9.135  1.00 23.56           C  
-ATOM   4211  CG  LYS B 280       3.732 -47.329 -10.014  1.00 24.11           C  
-ATOM   4212  CD  LYS B 280       4.155 -48.426 -10.988  1.00 24.21           C  
-ATOM   4213  CE  LYS B 280       5.308 -47.963 -11.867  1.00 25.74           C  
-ATOM   4214  NZ  LYS B 280       5.777 -49.028 -12.809  1.00 26.22           N  
-ATOM   4215  N   ALA B 281       0.466 -47.618  -6.664  1.00 22.77           N  
-ATOM   4216  CA  ALA B 281      -0.808 -47.951  -6.015  1.00 22.58           C  
-ATOM   4217  C   ALA B 281      -1.548 -46.715  -5.484  1.00 22.50           C  
-ATOM   4218  O   ALA B 281      -2.776 -46.622  -5.602  1.00 22.35           O  
-ATOM   4219  CB  ALA B 281      -0.589 -48.958  -4.895  1.00 22.52           C  
-ATOM   4220  N   ALA B 282      -0.802 -45.776  -4.901  1.00 22.16           N  
-ATOM   4221  CA  ALA B 282      -1.383 -44.517  -4.422  1.00 22.20           C  
-ATOM   4222  C   ALA B 282      -1.949 -43.700  -5.580  1.00 22.12           C  
-ATOM   4223  O   ALA B 282      -3.072 -43.206  -5.500  1.00 22.07           O  
-ATOM   4224  CB  ALA B 282      -0.354 -43.699  -3.641  1.00 22.25           C  
-ATOM   4225  N   ALA B 283      -1.171 -43.579  -6.657  1.00 22.39           N  
-ATOM   4226  CA  ALA B 283      -1.577 -42.805  -7.832  1.00 22.52           C  
-ATOM   4227  C   ALA B 283      -2.816 -43.400  -8.487  1.00 22.60           C  
-ATOM   4228  O   ALA B 283      -3.722 -42.667  -8.880  1.00 22.57           O  
-ATOM   4229  CB  ALA B 283      -0.431 -42.701  -8.837  1.00 22.50           C  
-ATOM   4230  N   ALA B 284      -2.854 -44.730  -8.584  1.00 22.95           N  
-ATOM   4231  CA  ALA B 284      -3.991 -45.440  -9.171  1.00 23.13           C  
-ATOM   4232  C   ALA B 284      -5.270 -45.225  -8.369  1.00 23.38           C  
-ATOM   4233  O   ALA B 284      -6.334 -44.973  -8.945  1.00 23.49           O  
-ATOM   4234  CB  ALA B 284      -3.687 -46.922  -9.295  1.00 23.30           C  
-ATOM   4235  N   TRP B 285      -5.158 -45.324  -7.044  1.00 23.62           N  
-ATOM   4236  CA  TRP B 285      -6.287 -45.078  -6.148  1.00 23.85           C  
-ATOM   4237  C   TRP B 285      -6.811 -43.652  -6.290  1.00 23.97           C  
-ATOM   4238  O   TRP B 285      -8.024 -43.431  -6.290  1.00 24.23           O  
-ATOM   4239  CB  TRP B 285      -5.922 -45.355  -4.685  1.00 23.90           C  
-ATOM   4240  CG  TRP B 285      -7.131 -45.317  -3.796  1.00 24.15           C  
-ATOM   4241  CD1 TRP B 285      -7.911 -46.379  -3.427  1.00 24.43           C  
-ATOM   4242  CD2 TRP B 285      -7.728 -44.157  -3.200  1.00 24.43           C  
-ATOM   4243  NE1 TRP B 285      -8.948 -45.953  -2.631  1.00 24.53           N  
-ATOM   4244  CE2 TRP B 285      -8.861 -44.594  -2.474  1.00 24.58           C  
-ATOM   4245  CE3 TRP B 285      -7.418 -42.787  -3.198  1.00 24.61           C  
-ATOM   4246  CZ2 TRP B 285      -9.682 -43.715  -1.759  1.00 23.96           C  
-ATOM   4247  CZ3 TRP B 285      -8.238 -41.912  -2.485  1.00 24.29           C  
-ATOM   4248  CH2 TRP B 285      -9.354 -42.382  -1.776  1.00 24.01           C  
-ATOM   4249  N   LEU B 286      -5.895 -42.692  -6.402  1.00 24.00           N  
-ATOM   4250  CA  LEU B 286      -6.263 -41.287  -6.588  1.00 24.15           C  
-ATOM   4251  C   LEU B 286      -6.998 -41.073  -7.909  1.00 24.35           C  
-ATOM   4252  O   LEU B 286      -7.957 -40.304  -7.968  1.00 24.37           O  
-ATOM   4253  CB  LEU B 286      -5.027 -40.382  -6.519  1.00 23.94           C  
-ATOM   4254  CG  LEU B 286      -4.334 -40.197  -5.165  1.00 23.91           C  
-ATOM   4255  CD1 LEU B 286      -2.973 -39.546  -5.355  1.00 23.47           C  
-ATOM   4256  CD2 LEU B 286      -5.191 -39.396  -4.191  1.00 23.11           C  
-ATOM   4257  N   LYS B 287      -6.546 -41.756  -8.958  1.00 24.72           N  
-ATOM   4258  CA  LYS B 287      -7.168 -41.655 -10.282  1.00 25.05           C  
-ATOM   4259  C   LYS B 287      -8.567 -42.264 -10.295  1.00 25.24           C  
-ATOM   4260  O   LYS B 287      -9.457 -41.783 -11.001  1.00 25.16           O  
-ATOM   4261  CB  LYS B 287      -6.303 -42.335 -11.346  1.00 25.22           C  
-ATOM   4262  CG  LYS B 287      -4.994 -41.631 -11.649  1.00 25.58           C  
-ATOM   4263  CD  LYS B 287      -4.208 -42.397 -12.699  1.00 27.46           C  
-ATOM   4264  CE  LYS B 287      -2.768 -41.919 -12.777  1.00 27.77           C  
-ATOM   4265  NZ  LYS B 287      -2.094 -42.471 -13.988  1.00 28.87           N  
-ATOM   4266  N   ASP B 288      -8.744 -43.326  -9.513  1.00 25.44           N  
-ATOM   4267  CA  ASP B 288     -10.022 -44.021  -9.406  1.00 25.79           C  
-ATOM   4268  C   ASP B 288     -10.958 -43.339  -8.407  1.00 25.97           C  
-ATOM   4269  O   ASP B 288     -12.163 -43.586  -8.410  1.00 25.89           O  
-ATOM   4270  CB  ASP B 288      -9.796 -45.482  -9.004  1.00 25.74           C  
-ATOM   4271  CG  ASP B 288     -11.019 -46.350  -9.240  1.00 25.81           C  
-ATOM   4272  OD1 ASP B 288     -11.672 -46.199 -10.297  1.00 25.37           O  
-ATOM   4273  OD2 ASP B 288     -11.401 -47.212  -8.424  1.00 25.52           O  
-ATOM   4274  N   ASN B 289     -10.392 -42.491  -7.552  1.00 26.33           N  
-ATOM   4275  CA  ASN B 289     -11.163 -41.733  -6.566  1.00 26.75           C  
-ATOM   4276  C   ASN B 289     -10.807 -40.246  -6.660  1.00 27.06           C  
-ATOM   4277  O   ASN B 289     -10.211 -39.681  -5.733  1.00 27.00           O  
-ATOM   4278  CB  ASN B 289     -10.925 -42.273  -5.148  1.00 26.83           C  
-ATOM   4279  CG  ASN B 289     -11.275 -43.749  -5.012  1.00 27.14           C  
-ATOM   4280  OD1 ASN B 289     -12.351 -44.100  -4.529  1.00 27.62           O  
-ATOM   4281  ND2 ASN B 289     -10.370 -44.620  -5.453  1.00 27.39           N  
-ATOM   4282  N   PRO B 290     -11.187 -39.615  -7.775  1.00 27.26           N  
-ATOM   4283  CA  PRO B 290     -10.644 -38.306  -8.151  1.00 27.49           C  
-ATOM   4284  C   PRO B 290     -11.083 -37.142  -7.262  1.00 27.73           C  
-ATOM   4285  O   PRO B 290     -10.358 -36.147  -7.159  1.00 27.92           O  
-ATOM   4286  CB  PRO B 290     -11.158 -38.111  -9.581  1.00 27.37           C  
-ATOM   4287  CG  PRO B 290     -12.403 -38.917  -9.652  1.00 27.42           C  
-ATOM   4288  CD  PRO B 290     -12.187 -40.093  -8.749  1.00 27.26           C  
-ATOM   4289  N   GLN B 291     -12.247 -37.265  -6.628  1.00 27.88           N  
-ATOM   4290  CA  GLN B 291     -12.781 -36.191  -5.790  1.00 28.06           C  
-ATOM   4291  C   GLN B 291     -11.994 -35.981  -4.499  1.00 28.21           C  
-ATOM   4292  O   GLN B 291     -11.834 -34.846  -4.047  1.00 28.25           O  
-ATOM   4293  CB  GLN B 291     -14.253 -36.433  -5.462  1.00 28.08           C  
-ATOM   4294  CG  GLN B 291     -14.912 -35.249  -4.773  1.00 28.45           C  
-ATOM   4295  CD  GLN B 291     -16.385 -35.452  -4.525  1.00 29.09           C  
-ATOM   4296  OE1 GLN B 291     -17.118 -35.896  -5.412  1.00 29.18           O  
-ATOM   4297  NE2 GLN B 291     -16.832 -35.114  -3.322  1.00 29.34           N  
-ATOM   4298  N   SER B 292     -11.505 -37.076  -3.918  1.00 28.44           N  
-ATOM   4299  CA  SER B 292     -10.812 -37.055  -2.625  1.00 28.62           C  
-ATOM   4300  C   SER B 292      -9.693 -36.015  -2.551  1.00 28.71           C  
-ATOM   4301  O   SER B 292      -9.318 -35.558  -1.469  1.00 28.48           O  
-ATOM   4302  CB  SER B 292     -10.253 -38.444  -2.306  1.00 28.63           C  
-ATOM   4303  OG  SER B 292      -9.275 -38.832  -3.256  1.00 28.87           O  
-ATOM   4304  N   ILE B 293      -9.184 -35.643  -3.719  1.00 28.90           N  
-ATOM   4305  CA  ILE B 293      -8.056 -34.734  -3.851  1.00 29.11           C  
-ATOM   4306  C   ILE B 293      -8.432 -33.275  -3.562  1.00 29.20           C  
-ATOM   4307  O   ILE B 293      -7.576 -32.467  -3.194  1.00 29.24           O  
-ATOM   4308  CB  ILE B 293      -7.453 -34.916  -5.271  1.00 29.30           C  
-ATOM   4309  CG1 ILE B 293      -5.929 -34.926  -5.232  1.00 29.23           C  
-ATOM   4310  CG2 ILE B 293      -8.038 -33.940  -6.293  1.00 28.97           C  
-ATOM   4311  CD1 ILE B 293      -5.352 -35.991  -6.139  1.00 29.75           C  
-ATOM   4312  N   GLU B 294      -9.719 -32.962  -3.706  1.00 29.13           N  
-ATOM   4313  CA  GLU B 294     -10.216 -31.587  -3.609  1.00 29.22           C  
-ATOM   4314  C   GLU B 294     -10.191 -30.997  -2.188  1.00 29.04           C  
-ATOM   4315  O   GLU B 294      -9.653 -29.904  -2.002  1.00 28.98           O  
-ATOM   4316  CB  GLU B 294     -11.611 -31.466  -4.228  1.00 29.25           C  
-ATOM   4317  CG  GLU B 294     -11.684 -31.856  -5.699  1.00 29.36           C  
-ATOM   4318  CD  GLU B 294     -13.097 -31.807  -6.247  1.00 29.61           C  
-ATOM   4319  OE1 GLU B 294     -13.969 -31.199  -5.591  1.00 30.43           O  
-ATOM   4320  OE2 GLU B 294     -13.337 -32.372  -7.336  1.00 30.06           O  
-ATOM   4321  N   PRO B 295     -10.758 -31.692  -1.192  1.00 28.91           N  
-ATOM   4322  CA  PRO B 295     -10.694 -31.214   0.195  1.00 28.65           C  
-ATOM   4323  C   PRO B 295      -9.266 -31.154   0.734  1.00 28.30           C  
-ATOM   4324  O   PRO B 295      -9.006 -30.411   1.681  1.00 28.47           O  
-ATOM   4325  CB  PRO B 295     -11.509 -32.256   0.967  1.00 28.64           C  
-ATOM   4326  CG  PRO B 295     -12.376 -32.889  -0.062  1.00 29.02           C  
-ATOM   4327  CD  PRO B 295     -11.519 -32.953  -1.287  1.00 28.96           C  
-ATOM   4328  N   TRP B 296      -8.357 -31.925   0.135  1.00 27.79           N  
-ATOM   4329  CA  TRP B 296      -6.944 -31.887   0.514  1.00 27.34           C  
-ATOM   4330  C   TRP B 296      -6.209 -30.685  -0.073  1.00 26.98           C  
-ATOM   4331  O   TRP B 296      -5.225 -30.211   0.506  1.00 26.79           O  
-ATOM   4332  CB  TRP B 296      -6.215 -33.165   0.090  1.00 27.43           C  
-ATOM   4333  CG  TRP B 296      -6.717 -34.435   0.711  1.00 27.51           C  
-ATOM   4334  CD1 TRP B 296      -7.480 -34.564   1.840  1.00 27.48           C  
-ATOM   4335  CD2 TRP B 296      -6.455 -35.765   0.254  1.00 27.47           C  
-ATOM   4336  NE1 TRP B 296      -7.723 -35.892   2.098  1.00 27.56           N  
-ATOM   4337  CE2 TRP B 296      -7.104 -36.652   1.141  1.00 27.65           C  
-ATOM   4338  CE3 TRP B 296      -5.737 -36.301  -0.825  1.00 27.89           C  
-ATOM   4339  CZ2 TRP B 296      -7.056 -38.045   0.984  1.00 27.68           C  
-ATOM   4340  CZ3 TRP B 296      -5.692 -37.687  -0.980  1.00 27.70           C  
-ATOM   4341  CH2 TRP B 296      -6.347 -38.539  -0.079  1.00 27.63           C  
-ATOM   4342  N   LEU B 297      -6.682 -30.203  -1.221  1.00 26.47           N  
-ATOM   4343  CA  LEU B 297      -5.985 -29.155  -1.967  1.00 26.10           C  
-ATOM   4344  C   LEU B 297      -6.657 -27.782  -1.905  1.00 26.03           C  
-ATOM   4345  O   LEU B 297      -6.222 -26.845  -2.582  1.00 25.99           O  
-ATOM   4346  CB  LEU B 297      -5.774 -29.577  -3.425  1.00 26.01           C  
-ATOM   4347  CG  LEU B 297      -4.781 -30.705  -3.720  1.00 25.64           C  
-ATOM   4348  CD1 LEU B 297      -4.963 -31.190  -5.146  1.00 25.72           C  
-ATOM   4349  CD2 LEU B 297      -3.335 -30.277  -3.471  1.00 25.86           C  
-ATOM   4350  N   SER B 298      -7.706 -27.665  -1.091  1.00 25.88           N  
-ATOM   4351  CA  SER B 298      -8.397 -26.388  -0.896  1.00 25.83           C  
-ATOM   4352  C   SER B 298      -7.457 -25.370  -0.257  1.00 25.58           C  
-ATOM   4353  O   SER B 298      -6.952 -25.582   0.849  1.00 25.62           O  
-ATOM   4354  CB  SER B 298      -9.663 -26.569  -0.052  1.00 25.82           C  
-ATOM   4355  OG  SER B 298      -9.397 -27.332   1.111  1.00 26.27           O  
-ATOM   4356  N   GLY B 299      -7.212 -24.279  -0.980  1.00 25.28           N  
-ATOM   4357  CA  GLY B 299      -6.284 -23.242  -0.541  1.00 25.00           C  
-ATOM   4358  C   GLY B 299      -4.819 -23.615  -0.686  1.00 24.75           C  
-ATOM   4359  O   GLY B 299      -3.945 -22.916  -0.166  1.00 24.85           O  
-ATOM   4360  N   VAL B 300      -4.551 -24.715  -1.389  1.00 24.42           N  
-ATOM   4361  CA  VAL B 300      -3.184 -25.188  -1.611  1.00 24.09           C  
-ATOM   4362  C   VAL B 300      -2.722 -24.817  -3.020  1.00 24.05           C  
-ATOM   4363  O   VAL B 300      -3.435 -25.049  -3.998  1.00 23.91           O  
-ATOM   4364  CB  VAL B 300      -3.054 -26.722  -1.381  1.00 24.01           C  
-ATOM   4365  CG1 VAL B 300      -1.626 -27.197  -1.621  1.00 23.64           C  
-ATOM   4366  CG2 VAL B 300      -3.504 -27.099   0.024  1.00 23.73           C  
-ATOM   4367  N   ALA B 301      -1.532 -24.230  -3.110  1.00 23.92           N  
-ATOM   4368  CA  ALA B 301      -0.946 -23.849  -4.391  1.00 23.76           C  
-ATOM   4369  C   ALA B 301       0.179 -24.804  -4.791  1.00 23.78           C  
-ATOM   4370  O   ALA B 301       0.598 -25.656  -3.998  1.00 23.69           O  
-ATOM   4371  CB  ALA B 301      -0.436 -22.412  -4.329  1.00 23.75           C  
-ATOM   4372  N   THR B 302       0.655 -24.662  -6.026  1.00 23.62           N  
-ATOM   4373  CA  THR B 302       1.838 -25.377  -6.497  1.00 23.73           C  
-ATOM   4374  C   THR B 302       3.080 -24.760  -5.831  1.00 23.77           C  
-ATOM   4375  O   THR B 302       2.985 -23.700  -5.207  1.00 23.60           O  
-ATOM   4376  CB  THR B 302       1.901 -25.332  -8.059  1.00 23.82           C  
-ATOM   4377  OG1 THR B 302       2.726 -26.391  -8.554  1.00 24.57           O  
-ATOM   4378  CG2 THR B 302       2.604 -24.095  -8.565  1.00 23.55           C  
-ATOM   4379  N   LYS B 303       4.232 -25.422  -5.947  1.00 23.96           N  
-ATOM   4380  CA  LYS B 303       5.481 -24.900  -5.379  1.00 24.15           C  
-ATOM   4381  C   LYS B 303       5.829 -23.523  -5.957  1.00 24.35           C  
-ATOM   4382  O   LYS B 303       6.326 -22.649  -5.244  1.00 24.37           O  
-ATOM   4383  CB  LYS B 303       6.637 -25.876  -5.615  1.00 24.08           C  
-ATOM   4384  CG  LYS B 303       7.894 -25.569  -4.799  1.00 24.48           C  
-ATOM   4385  CD  LYS B 303       9.148 -26.134  -5.452  1.00 24.97           C  
-ATOM   4386  CE  LYS B 303       9.654 -25.216  -6.556  1.00 25.90           C  
-ATOM   4387  NZ  LYS B 303      10.618 -25.897  -7.463  1.00 26.93           N  
-ATOM   4388  N   ASP B 304       5.549 -23.342  -7.246  1.00 24.48           N  
-ATOM   4389  CA  ASP B 304       5.866 -22.104  -7.963  1.00 24.73           C  
-ATOM   4390  C   ASP B 304       4.752 -21.046  -7.918  1.00 24.73           C  
-ATOM   4391  O   ASP B 304       4.840 -20.019  -8.595  1.00 24.76           O  
-ATOM   4392  CB  ASP B 304       6.257 -22.421  -9.413  1.00 24.77           C  
-ATOM   4393  CG  ASP B 304       7.487 -23.316  -9.505  1.00 25.36           C  
-ATOM   4394  OD1 ASP B 304       8.471 -23.066  -8.773  1.00 25.55           O  
-ATOM   4395  OD2 ASP B 304       7.559 -24.293 -10.284  1.00 25.66           O  
-ATOM   4396  N   GLY B 305       3.716 -21.301  -7.120  1.00 24.80           N  
-ATOM   4397  CA  GLY B 305       2.655 -20.322  -6.870  1.00 24.89           C  
-ATOM   4398  C   GLY B 305       1.470 -20.317  -7.823  1.00 24.93           C  
-ATOM   4399  O   GLY B 305       0.736 -19.328  -7.897  1.00 25.11           O  
-ATOM   4400  N   GLY B 306       1.284 -21.412  -8.555  1.00 24.92           N  
-ATOM   4401  CA  GLY B 306       0.125 -21.581  -9.435  1.00 24.80           C  
-ATOM   4402  C   GLY B 306      -0.988 -22.366  -8.763  1.00 24.82           C  
-ATOM   4403  O   GLY B 306      -0.882 -22.720  -7.586  1.00 24.59           O  
-ATOM   4404  N   ASP B 307      -2.052 -22.645  -9.514  1.00 24.88           N  
-ATOM   4405  CA  ASP B 307      -3.222 -23.352  -8.986  1.00 25.08           C  
-ATOM   4406  C   ASP B 307      -2.905 -24.810  -8.649  1.00 25.04           C  
-ATOM   4407  O   ASP B 307      -2.572 -25.603  -9.532  1.00 24.96           O  
-ATOM   4408  CB  ASP B 307      -4.390 -23.269  -9.977  1.00 25.14           C  
-ATOM   4409  CG  ASP B 307      -5.726 -23.604  -9.336  1.00 25.51           C  
-ATOM   4410  OD1 ASP B 307      -5.999 -24.800  -9.095  1.00 25.76           O  
-ATOM   4411  OD2 ASP B 307      -6.571 -22.730  -9.042  1.00 26.37           O  
-ATOM   4412  N   GLY B 308      -3.018 -25.147  -7.365  1.00 25.25           N  
-ATOM   4413  CA  GLY B 308      -2.659 -26.471  -6.855  1.00 25.32           C  
-ATOM   4414  C   GLY B 308      -3.541 -27.610  -7.332  1.00 25.58           C  
-ATOM   4415  O   GLY B 308      -3.041 -28.614  -7.838  1.00 25.51           O  
-ATOM   4416  N   LEU B 309      -4.854 -27.450  -7.169  1.00 25.76           N  
-ATOM   4417  CA  LEU B 309      -5.839 -28.440  -7.610  1.00 25.97           C  
-ATOM   4418  C   LEU B 309      -5.703 -28.734  -9.106  1.00 26.16           C  
-ATOM   4419  O   LEU B 309      -5.736 -29.894  -9.520  1.00 26.13           O  
-ATOM   4420  CB  LEU B 309      -7.260 -27.943  -7.315  1.00 26.04           C  
-ATOM   4421  CG  LEU B 309      -8.377 -28.890  -6.843  1.00 26.23           C  
-ATOM   4422  CD1 LEU B 309      -9.738 -28.314  -7.215  1.00 25.89           C  
-ATOM   4423  CD2 LEU B 309      -8.241 -30.336  -7.338  1.00 26.12           C  
-ATOM   4424  N   ALA B 310      -5.544 -27.676  -9.901  1.00 26.36           N  
-ATOM   4425  CA  ALA B 310      -5.431 -27.788 -11.357  1.00 26.63           C  
-ATOM   4426  C   ALA B 310      -4.195 -28.570 -11.792  1.00 26.83           C  
-ATOM   4427  O   ALA B 310      -4.269 -29.395 -12.704  1.00 26.76           O  
-ATOM   4428  CB  ALA B 310      -5.439 -26.407 -11.998  1.00 26.62           C  
-ATOM   4429  N   ALA B 311      -3.066 -28.310 -11.133  1.00 27.01           N  
-ATOM   4430  CA  ALA B 311      -1.804 -28.970 -11.464  1.00 27.31           C  
-ATOM   4431  C   ALA B 311      -1.831 -30.462 -11.135  1.00 27.59           C  
-ATOM   4432  O   ALA B 311      -1.249 -31.274 -11.859  1.00 27.60           O  
-ATOM   4433  CB  ALA B 311      -0.643 -28.286 -10.760  1.00 27.31           C  
-ATOM   4434  N   VAL B 312      -2.516 -30.817 -10.051  1.00 27.85           N  
-ATOM   4435  CA  VAL B 312      -2.587 -32.212  -9.619  1.00 28.21           C  
-ATOM   4436  C   VAL B 312      -3.521 -33.023 -10.514  1.00 28.47           C  
-ATOM   4437  O   VAL B 312      -3.146 -34.098 -10.989  1.00 28.38           O  
-ATOM   4438  CB  VAL B 312      -2.996 -32.349  -8.133  1.00 28.18           C  
-ATOM   4439  CG1 VAL B 312      -3.122 -33.814  -7.744  1.00 28.01           C  
-ATOM   4440  CG2 VAL B 312      -1.977 -31.671  -7.234  1.00 28.18           C  
-ATOM   4441  N   LYS B 313      -4.723 -32.502 -10.755  1.00 28.87           N  
-ATOM   4442  CA  LYS B 313      -5.698 -33.201 -11.598  1.00 29.30           C  
-ATOM   4443  C   LYS B 313      -5.228 -33.340 -13.053  1.00 29.53           C  
-ATOM   4444  O   LYS B 313      -5.633 -34.268 -13.750  1.00 29.59           O  
-ATOM   4445  CB  LYS B 313      -7.098 -32.573 -11.490  1.00 29.19           C  
-ATOM   4446  CG  LYS B 313      -7.267 -31.202 -12.132  1.00 29.41           C  
-ATOM   4447  CD  LYS B 313      -8.458 -30.439 -11.542  1.00 29.43           C  
-ATOM   4448  CE  LYS B 313      -9.798 -31.062 -11.918  1.00 30.00           C  
-ATOM   4449  NZ  LYS B 313     -10.942 -30.137 -11.662  1.00 30.53           N  
-ATOM   4450  N   ALA B 314      -4.363 -32.424 -13.488  1.00 29.92           N  
-ATOM   4451  CA  ALA B 314      -3.747 -32.491 -14.815  1.00 30.31           C  
-ATOM   4452  C   ALA B 314      -2.604 -33.508 -14.859  1.00 30.63           C  
-ATOM   4453  O   ALA B 314      -2.459 -34.241 -15.839  1.00 30.70           O  
-ATOM   4454  CB  ALA B 314      -3.255 -31.121 -15.248  1.00 30.22           C  
-ATOM   4455  N   ALA B 315      -1.800 -33.546 -13.797  1.00 30.93           N  
-ATOM   4456  CA  ALA B 315      -0.669 -34.472 -13.700  1.00 31.26           C  
-ATOM   4457  C   ALA B 315      -1.127 -35.924 -13.574  1.00 31.29           C  
-ATOM   4458  O   ALA B 315      -0.416 -36.839 -13.990  1.00 31.39           O  
-ATOM   4459  CB  ALA B 315       0.238 -34.095 -12.533  1.00 31.33           C  
-ATOM   4460  N   LEU B 316      -2.311 -36.122 -12.999  1.00 31.49           N  
-ATOM   4461  CA  LEU B 316      -2.901 -37.452 -12.872  1.00 31.55           C  
-ATOM   4462  C   LEU B 316      -3.817 -37.806 -14.046  1.00 31.55           C  
-ATOM   4463  O   LEU B 316      -4.345 -38.919 -14.108  1.00 31.40           O  
-ATOM   4464  CB  LEU B 316      -3.674 -37.582 -11.558  1.00 31.49           C  
-ATOM   4465  CG  LEU B 316      -2.903 -37.572 -10.236  1.00 31.82           C  
-ATOM   4466  CD1 LEU B 316      -3.878 -37.772  -9.093  1.00 32.25           C  
-ATOM   4467  CD2 LEU B 316      -1.811 -38.635 -10.202  1.00 31.74           C  
-ATOM   4468  N   GLY B 317      -4.003 -36.854 -14.960  1.00 31.63           N  
-ATOM   4469  CA  GLY B 317      -4.837 -37.053 -16.149  1.00 31.69           C  
-ATOM   4470  C   GLY B 317      -6.327 -37.105 -15.857  1.00 31.79           C  
-ATOM   4471  O   GLY B 317      -6.782 -36.678 -14.792  1.00 31.83           O  
-TER    4472      GLY B 317                                                      
-HETATM 4473  C4  CHT A   1      16.808   1.778   5.637  1.00  7.51           C  
-HETATM 4474  C5  CHT A   1      16.421   2.061   7.097  1.00  6.35           C  
-HETATM 4475  C6  CHT A   1      15.357   3.339   8.764  1.00  5.88           C  
-HETATM 4476  C7  CHT A   1      16.625   4.531   7.176  1.00  4.71           C  
-HETATM 4477  C8  CHT A   1      14.539   3.544   6.526  1.00  5.57           C  
-HETATM 4478  O6  CHT A   1      17.965   2.542   5.274  1.00  8.52           O  
-HETATM 4479  N1  CHT A   1      15.747   3.356   7.343  1.00  6.17           N  
-HETATM 4480  C4  CHT B   1       2.133 -48.174  15.449  1.00  8.47           C  
-HETATM 4481  C5  CHT B   1       1.842 -48.355  13.948  1.00  6.83           C  
-HETATM 4482  C6  CHT B   1       0.894 -49.591  12.147  1.00  5.23           C  
-HETATM 4483  C7  CHT B   1       2.133 -50.803  13.751  1.00  5.95           C  
-HETATM 4484  C8  CHT B   1      -0.027 -49.933  14.309  1.00  6.40           C  
-HETATM 4485  O6  CHT B   1       3.283 -48.951  15.828  1.00  9.79           O  
-HETATM 4486  N1  CHT B   1       1.219 -49.657  13.582  1.00  6.87           N  
-HETATM 4487  O   HOH A 319      31.060  -0.492   9.891  1.00  6.58           O  
-HETATM 4488  O   HOH A 320      14.781   5.204  12.370  1.00  7.39           O  
-HETATM 4489  O   HOH A 321      11.715  -0.745  11.442  1.00  8.35           O  
-HETATM 4490  O   HOH A 322      11.254   1.765   0.065  1.00  7.47           O  
-HETATM 4491  O   HOH A 323      22.812  14.377   6.135  1.00  8.48           O  
-HETATM 4492  O   HOH A 324       1.137   1.124   7.394  1.00 13.01           O  
-HETATM 4493  O   HOH A 325      25.196   2.201   6.176  1.00  8.74           O  
-HETATM 4494  O   HOH A 326      17.982  19.910   0.739  1.00  8.43           O  
-HETATM 4495  O   HOH A 327      13.017  -0.346   1.365  1.00  9.74           O  
-HETATM 4496  O   HOH A 328       9.394   6.558  -4.013  1.00 14.54           O  
-HETATM 4497  O   HOH A 329      11.253  -3.535  11.706  1.00  8.96           O  
-HETATM 4498  O   HOH A 330      13.999  -3.500  12.551  1.00  7.99           O  
-HETATM 4499  O   HOH A 331      15.195  -1.390  10.866  1.00  7.62           O  
-HETATM 4500  O   HOH A 332       5.048   7.316  -5.103  1.00 16.18           O  
-HETATM 4501  O   HOH A 333      14.363  16.901 -10.038  1.00 19.75           O  
-HETATM 4502  O   HOH A 334       2.627  -2.374  10.601  1.00 15.06           O  
-HETATM 4503  O   HOH A 335       7.534   8.436  -4.817  1.00 13.16           O  
-HETATM 4504  O   HOH A 336      12.253  13.408  15.167  1.00 18.42           O  
-HETATM 4505  O   HOH A 337      10.747 -12.502   4.672  1.00 21.40           O  
-HETATM 4506  O   HOH A 338       7.083   0.132  -2.982  1.00 16.78           O  
-HETATM 4507  O   HOH A 339      27.518   6.007   1.168  1.00 18.14           O  
-HETATM 4508  O   HOH A 340      25.448   4.437   0.193  1.00 11.19           O  
-HETATM 4509  O   HOH A 341      22.986   4.643 -16.937  1.00 27.80           O  
-HETATM 4510  O   HOH A 342      11.278  25.904   6.740  1.00 27.99           O  
-HETATM 4511  O   HOH A 343      18.983  -1.588  -4.154  1.00 11.72           O  
-HETATM 4512  O   HOH A 344      10.363   7.037 -10.649  1.00 16.84           O  
-HETATM 4513  O   HOH A 345       7.235 -13.540   6.898  1.00 23.47           O  
-HETATM 4514  O   HOH A 346       7.953  21.052   7.964  1.00 21.25           O  
-HETATM 4515  O   HOH A 347      21.894  24.946   8.962  1.00 22.20           O  
-HETATM 4516  O   HOH A 348       3.284  13.145   2.503  1.00 17.49           O  
-HETATM 4517  O   HOH A 349       3.653  -5.392  10.466  1.00 17.98           O  
-HETATM 4518  O   HOH A 350      31.647  -4.445   3.283  1.00 16.53           O  
-HETATM 4519  O   HOH A 351      22.177   6.757  10.706  1.00 12.37           O  
-HETATM 4520  O   HOH A 352      28.433  -6.122   1.728  1.00 12.35           O  
-HETATM 4521  O   HOH A 353      11.718 -11.696  12.955  1.00 17.08           O  
-HETATM 4522  O   HOH A 354      19.167  14.979  15.611  1.00 20.58           O  
-HETATM 4523  O   HOH A 355      22.441   0.981  -6.291  1.00 20.63           O  
-HETATM 4524  O   HOH A 356      19.553  22.232   1.331  1.00 14.97           O  
-HETATM 4525  O   HOH A 357      19.438  -6.155  14.349  1.00  9.67           O  
-HETATM 4526  O   HOH A 358      28.713  14.062   2.913  1.00 14.95           O  
-HETATM 4527  O   HOH A 359      14.058 -19.779  10.223  1.00 30.80           O  
-HETATM 4528  O   HOH A 360      31.385   0.031  13.068  1.00 13.49           O  
-HETATM 4529  O   HOH A 361      27.504  13.753  -3.561  1.00 21.95           O  
-HETATM 4530  O   HOH A 362      15.740  14.597 -16.433  1.00 35.77           O  
-HETATM 4531  O   HOH A 363       4.423   8.666  -7.972  1.00 21.07           O  
-HETATM 4532  O   HOH A 364      28.502   4.294   7.990  1.00 10.78           O  
-HETATM 4533  O   HOH A 365      15.257 -10.287   2.126  1.00 18.65           O  
-HETATM 4534  O   HOH A 366       2.969   4.894  -6.840  1.00 27.51           O  
-HETATM 4535  O   HOH A 367       5.283   9.567  13.975  1.00 22.73           O  
-HETATM 4536  O   HOH A 368      12.461  21.426   8.025  1.00 19.33           O  
-HETATM 4537  O   HOH A 369      24.407   0.451   0.298  1.00 13.44           O  
-HETATM 4538  O   HOH A 370      30.579   0.577   4.940  1.00 13.96           O  
-HETATM 4539  O   HOH A 371       2.082   4.534  14.220  1.00 22.93           O  
-HETATM 4540  O   HOH A 372      15.860   0.888  -7.114  1.00 31.98           O  
-HETATM 4541  O   HOH A 373       2.728  -9.818  19.021  1.00 19.59           O  
-HETATM 4542  O   HOH A 374      15.613  -8.912  29.907  1.00 20.35           O  
-HETATM 4543  O   HOH A 375      18.005  10.656  22.369  1.00 37.18           O  
-HETATM 4544  O   HOH A 376      23.465  -6.265  24.311  1.00 32.26           O  
-HETATM 4545  O   HOH A 377       3.927  14.785  -2.744  1.00 14.26           O  
-HETATM 4546  O   HOH A 378      30.425   2.979   3.840  1.00 23.26           O  
-HETATM 4547  O   HOH A 379       4.830  19.578   4.448  1.00 33.44           O  
-HETATM 4548  O   HOH A 380       9.485  -0.061  -9.364  1.00 21.42           O  
-HETATM 4549  O   HOH A 381      20.814  21.669  15.487  1.00 31.92           O  
-HETATM 4550  O   HOH A 382       7.260  -2.888  -0.585  1.00 20.60           O  
-HETATM 4551  O   HOH A 383      15.850  17.066  15.075  1.00 18.78           O  
-HETATM 4552  O   HOH A 384      18.332  17.437  16.376  1.00 31.40           O  
-HETATM 4553  O   HOH A 385       4.649  18.605  -8.619  1.00 16.62           O  
-HETATM 4554  O   HOH A 386       4.643  -2.269   2.679  1.00 29.46           O  
-HETATM 4555  O   HOH A 387       8.331  -2.078  -4.528  1.00 23.13           O  
-HETATM 4556  O   HOH A 388      12.240  -1.078  -6.151  1.00 33.01           O  
-HETATM 4557  O   HOH A 389       4.304  12.002   7.806  1.00 16.81           O  
-HETATM 4558  O   HOH A 390       9.189  24.243   6.741  1.00 18.90           O  
-HETATM 4559  O   HOH A 391       4.292 -14.219  15.600  1.00 36.92           O  
-HETATM 4560  O   HOH A 392       8.526   9.741 -12.013  1.00 35.51           O  
-HETATM 4561  O   HOH A 393       2.654  -7.926  13.611  1.00 31.21           O  
-HETATM 4562  O   HOH A 394      29.206  15.094   0.457  1.00 30.31           O  
-HETATM 4563  O   HOH A 395      23.816   5.565  12.382  1.00 27.50           O  
-HETATM 4564  O   HOH A 396      18.217 -20.438  30.602  1.00 30.93           O  
-HETATM 4565  O   HOH A 397      11.344  -8.353  -0.136  1.00 26.01           O  
-HETATM 4566  O   HOH A 398      22.599 -30.500  11.883  1.00 34.48           O  
-HETATM 4567  O   HOH A 399       4.092  14.947   8.938  1.00 26.80           O  
-HETATM 4568  O   HOH A 400       3.145  -7.359  16.235  1.00 26.26           O  
-HETATM 4569  O   HOH A 401       7.222  19.593 -13.858  1.00 30.09           O  
-HETATM 4570  O   HOH A 402      16.330  26.912  -8.517  1.00 28.51           O  
-HETATM 4571  O   HOH A 403      12.028   0.102  31.700  1.00 24.49           O  
-HETATM 4572  O   HOH A 404       5.925   6.704  23.041  1.00 24.65           O  
-HETATM 4573  O   HOH A 405       4.008  -7.323   2.852  1.00 20.54           O  
-HETATM 4574  O   HOH A 406      16.805 -10.385  31.768  1.00 28.91           O  
-HETATM 4575  O   HOH A 407      16.517  28.892   0.251  1.00 23.07           O  
-HETATM 4576  O   HOH A 408      26.680   2.819  11.198  1.00 32.93           O  
-HETATM 4577  O   HOH A 409      19.921  -2.108  20.015  1.00 19.77           O  
-HETATM 4578  O   HOH A 410      15.812 -11.138  -0.515  1.00 28.14           O  
-HETATM 4579  O   HOH A 411      13.704  29.462  -0.218  1.00 23.16           O  
-HETATM 4580  O   HOH A 412      20.248  31.696  -5.793  1.00 37.94           O  
-HETATM 4581  O   HOH A 413      24.107  -9.489  27.306  1.00 29.48           O  
-HETATM 4582  O   HOH A 414      19.756   5.865  21.963  1.00 20.00           O  
-HETATM 4583  O   HOH A 415       3.933   3.584  24.719  1.00 33.52           O  
-HETATM 4584  O   HOH A 416      21.227  19.540 -11.153  1.00 22.98           O  
-HETATM 4585  O   HOH A 417      24.631 -17.117  18.418  1.00 32.10           O  
-HETATM 4586  O   HOH A 418      26.679 -18.686  17.085  1.00 31.82           O  
-HETATM 4587  O   HOH A 419       2.111  11.744   9.365  1.00 41.02           O  
-HETATM 4588  O   HOH A 420      19.360  13.745 -17.222  1.00 33.63           O  
-HETATM 4589  O   HOH A 421       7.505  21.274  13.279  1.00 42.49           O  
-HETATM 4590  O   HOH A 422      16.443   5.564  30.167  1.00 24.45           O  
-HETATM 4591  O   HOH A 423       1.624  -0.632  20.720  1.00 41.23           O  
-HETATM 4592  O   HOH A 424      13.468  17.574 -12.968  1.00 23.12           O  
-HETATM 4593  O   HOH A 425       2.481   9.878   1.994  1.00 30.38           O  
-HETATM 4594  O   HOH A 426       3.170  -0.401  -0.931  1.00 39.91           O  
-HETATM 4595  O   HOH A 427      30.215 -17.830  14.618  1.00 41.93           O  
-HETATM 4596  O   HOH A 428      23.961 -22.265  24.067  1.00 40.14           O  
-HETATM 4597  O   HOH A 429       6.848   1.984 -11.469  1.00 28.43           O  
-HETATM 4598  O   HOH A 430      20.280 -25.042  33.999  1.00 30.12           O  
-HETATM 4599  O   HOH A 431      16.011  -1.495  -4.963  1.00 35.88           O  
-HETATM 4600  O   HOH A 432      25.218  -7.161  26.534  1.00 51.91           O  
-HETATM 4601  O   HOH A 433      35.553  -8.681   9.936  1.00 42.30           O  
-HETATM 4602  O   HOH A 434       3.421  23.577   3.081  1.00 32.52           O  
-HETATM 4603  O   HOH A 435      20.716   4.468  17.838  1.00 32.05           O  
-HETATM 4604  O   HOH A 436       3.553  11.109  -9.916  1.00 39.13           O  
-HETATM 4605  O   HOH A 437       8.673   8.535  28.239  1.00 24.37           O  
-HETATM 4606  O   HOH A 438      27.099 -13.522  -5.276  1.00 34.74           O  
-HETATM 4607  O   HOH A 439      29.272 -14.457  20.277  1.00 41.87           O  
-HETATM 4608  O   HOH A 440      26.070 -11.892  -7.378  1.00 45.31           O  
-HETATM 4609  O   HOH A 441       7.159   6.033 -12.458  1.00 32.11           O  
-HETATM 4610  O   HOH A 442       7.991  23.009  -8.353  1.00 27.82           O  
-HETATM 4611  O   HOH A 443      18.708 -14.390  -5.653  1.00 46.39           O  
-HETATM 4612  O   HOH A 444      27.816  -5.869  -2.459  1.00 29.07           O  
-HETATM 4613  O   HOH A 445       2.131   8.507   5.411  1.00 41.63           O  
-HETATM 4614  O   HOH A 446      17.648  10.682  15.454  1.00 13.33           O  
-HETATM 4615  O   HOH A 447      25.762   4.882  -5.314  1.00 21.02           O  
-HETATM 4616  O   HOH A 448      21.028   2.652  -7.592  1.00 31.67           O  
-HETATM 4617  O   HOH A 449      19.063   5.185  -8.069  1.00 17.29           O  
-HETATM 4618  O   HOH A 450      26.775  14.813 -10.594  1.00 33.24           O  
-HETATM 4619  O   HOH A 451       8.690  -5.093   0.173  1.00 18.87           O  
-HETATM 4620  O   HOH A 452       2.695   8.422  -5.965  1.00 32.85           O  
-HETATM 4621  O   HOH A 453      26.239  12.172  12.114  1.00 24.08           O  
-HETATM 4622  O   HOH A 454      18.496   6.891  23.967  1.00 19.88           O  
-HETATM 4623  O   HOH A 455      21.299  16.727 -14.668  1.00 27.66           O  
-HETATM 4624  O   HOH A 456      17.289  13.250  16.230  1.00 20.04           O  
-HETATM 4625  O   HOH A 457      -1.002 -11.902  21.171  1.00 29.42           O  
-HETATM 4626  O   HOH A 458      25.154   1.932  -6.745  1.00 29.76           O  
-HETATM 4627  O   HOH A 459       4.116   8.518 -10.658  1.00 44.11           O  
-HETATM 4628  O   HOH A 460       6.683  -6.938  -0.939  1.00 29.68           O  
-HETATM 4629  O   HOH A 461       6.871  12.170  18.217  1.00 30.44           O  
-HETATM 4630  O   HOH A 462      10.356  -5.914  -2.281  1.00 32.84           O  
-HETATM 4631  O   HOH A 463       6.721  10.251  22.417  1.00 22.86           O  
-HETATM 4632  O   HOH A 464       6.940   7.888  17.071  1.00 53.40           O  
-HETATM 4633  O   HOH A 465      27.087  12.260  -5.695  1.00 41.89           O  
-HETATM 4634  O   HOH A 466      19.814 -22.347   8.065  1.00 46.86           O  
-HETATM 4635  O   HOH A 467      10.457  -1.188  33.217  1.00 31.80           O  
-HETATM 4636  O   HOH A 468      15.741  14.101  19.512  1.00 32.08           O  
-HETATM 4637  O   HOH A 469       5.388 -17.126  13.543  1.00 28.85           O  
-HETATM 4638  O   HOH A 470       3.964   3.597   5.742  1.00 18.42           O  
-HETATM 4639  O   HOH A 471       1.079  -1.193   3.298  1.00 23.70           O  
-HETATM 4640  O   HOH A 472      23.847  24.796   2.297  1.00 28.85           O  
-HETATM 4641  O   HOH A 473      23.718  19.233 -15.082  1.00 33.93           O  
-HETATM 4642  O   HOH A 474      14.144   0.410  -4.544  1.00 32.01           O  
-HETATM 4643  O   HOH B 318      10.490 -48.598  15.240  1.00 14.10           O  
-HETATM 4644  O   HOH B 319      -1.935 -46.132  19.444  1.00 12.13           O  
-HETATM 4645  O   HOH B 320      -0.168 -42.591   8.360  1.00 16.71           O  
-HETATM 4646  O   HOH B 321       3.710 -44.879  25.234  1.00 11.16           O  
-HETATM 4647  O   HOH B 322      -3.853 -33.624  16.306  1.00 23.50           O  
-HETATM 4648  O   HOH B 323       8.149 -60.688  15.067  1.00 17.03           O  
-HETATM 4649  O   HOH B 324       5.312 -40.060   6.894  1.00 12.09           O  
-HETATM 4650  O   HOH B 325       0.901 -44.809  10.227  1.00 12.90           O  
-HETATM 4651  O   HOH B 326       7.759 -53.175  10.557  1.00 14.37           O  
-HETATM 4652  O   HOH B 327       3.094 -66.310  20.282  1.00 11.34           O  
-HETATM 4653  O   HOH B 328      -9.152 -53.410   8.808  1.00 13.43           O  
-HETATM 4654  O   HOH B 329      -3.684 -48.034  20.561  1.00 15.95           O  
-HETATM 4655  O   HOH B 330       9.445 -46.836  21.209  1.00 13.18           O  
-HETATM 4656  O   HOH B 331       5.664 -75.036  32.260  1.00 28.22           O  
-HETATM 4657  O   HOH B 332      13.897 -60.491  18.488  1.00 19.40           O  
-HETATM 4658  O   HOH B 333      -2.765 -42.814   8.915  1.00  8.03           O  
-HETATM 4659  O   HOH B 334      13.744 -50.460  13.427  1.00 23.45           O  
-HETATM 4660  O   HOH B 335      -0.248 -26.400  10.952  1.00 64.10           O  
-HETATM 4661  O   HOH B 336      -8.822 -55.908   6.065  1.00 19.71           O  
-HETATM 4662  O   HOH B 337      -2.693 -45.709   9.333  1.00 19.81           O  
-HETATM 4663  O   HOH B 338      12.522 -52.593  20.548  1.00 14.94           O  
-HETATM 4664  O   HOH B 339     -10.289 -53.574  25.312  1.00 13.86           O  
-HETATM 4665  O   HOH B 340      -7.744 -54.700  25.074  1.00 18.10           O  
-HETATM 4666  O   HOH B 341       0.574 -51.415   8.420  1.00 12.60           O  
-HETATM 4667  O   HOH B 342      13.511 -40.534  20.205  1.00 19.86           O  
-HETATM 4668  O   HOH B 343      -9.863 -61.296  11.442  1.00 18.39           O  
-HETATM 4669  O   HOH B 344      10.549 -67.144  26.743  1.00 15.33           O  
-HETATM 4670  O   HOH B 345     -11.155 -45.393  22.684  1.00 26.60           O  
-HETATM 4671  O   HOH B 346      -9.538 -65.827  15.816  1.00 18.55           O  
-HETATM 4672  O   HOH B 347      16.335 -45.961  12.191  1.00 18.32           O  
-HETATM 4673  O   HOH B 348     -11.662 -59.282  17.486  1.00 16.36           O  
-HETATM 4674  O   HOH B 349       4.872 -61.447   5.523  1.00 17.51           O  
-HETATM 4675  O   HOH B 350     -12.665 -44.147  10.627  1.00 17.76           O  
-HETATM 4676  O   HOH B 351       3.233 -51.793  -9.176  1.00 25.33           O  
-HETATM 4677  O   HOH B 352       6.791 -68.169   5.694  1.00 31.26           O  
-HETATM 4678  O   HOH B 353     -10.279 -40.407   9.574  1.00 29.37           O  
-HETATM 4679  O   HOH B 354      -1.295 -63.235  30.650  1.00 21.51           O  
-HETATM 4680  O   HOH B 355       6.652 -50.769   3.331  1.00 22.16           O  
-HETATM 4681  O   HOH B 356       4.610 -68.405  19.732  1.00 23.96           O  
-HETATM 4682  O   HOH B 357       3.711 -51.679  29.115  1.00 17.17           O  
-HETATM 4683  O   HOH B 358     -13.291 -47.678  13.918  1.00 19.76           O  
-HETATM 4684  O   HOH B 359      -2.247 -34.428   7.689  1.00 24.74           O  
-HETATM 4685  O   HOH B 360      -5.535 -25.740  -5.324  1.00 23.56           O  
-HETATM 4686  O   HOH B 361      -8.018 -46.589  23.252  1.00 14.16           O  
-HETATM 4687  O   HOH B 362     -12.506 -43.846   7.910  1.00 23.20           O  
-HETATM 4688  O   HOH B 363      -7.733 -43.456  21.046  1.00 22.58           O  
-HETATM 4689  O   HOH B 364       9.823 -39.805  -2.678  1.00 25.76           O  
-HETATM 4690  O   HOH B 365     -10.284 -36.712   0.584  1.00 32.53           O  
-HETATM 4691  O   HOH B 366      10.639 -50.891  21.515  1.00 21.17           O  
-HETATM 4692  O   HOH B 367      11.160 -36.163  -5.650  1.00 26.21           O  
-HETATM 4693  O   HOH B 368      11.894 -58.834   9.611  1.00 19.57           O  
-HETATM 4694  O   HOH B 369       8.063 -32.577  -8.881  1.00 36.08           O  
-HETATM 4695  O   HOH B 370       7.771 -71.212  12.373  1.00 21.23           O  
-HETATM 4696  O   HOH B 371      -2.780 -72.366  14.131  1.00 48.24           O  
-HETATM 4697  O   HOH B 372       0.175 -36.158  18.884  1.00 21.40           O  
-HETATM 4698  O   HOH B 373      -6.381 -46.051 -11.602  1.00 26.88           O  
-HETATM 4699  O   HOH B 374      -5.492 -53.226  31.251  1.00 26.39           O  
-HETATM 4700  O   HOH B 375     -11.133 -61.200  22.928  1.00 24.22           O  
-HETATM 4701  O   HOH B 376     -10.138 -58.354  12.402  1.00 22.63           O  
-HETATM 4702  O   HOH B 377       1.819 -63.460   6.014  1.00 17.64           O  
-HETATM 4703  O   HOH B 378       6.848 -47.511  27.685  1.00 27.00           O  
-HETATM 4704  O   HOH B 379      17.012 -42.358  18.230  1.00 30.48           O  
-HETATM 4705  O   HOH B 380      -6.755 -67.530   9.161  1.00 26.01           O  
-HETATM 4706  O   HOH B 381      11.625 -47.983  22.294  1.00 27.39           O  
-HETATM 4707  O   HOH B 382      10.419 -51.189  26.858  1.00 22.27           O  
-HETATM 4708  O   HOH B 383      -9.871 -32.327   4.666  1.00 32.08           O  
-HETATM 4709  O   HOH B 384       5.475 -25.817  -9.117  1.00 34.20           O  
-HETATM 4710  O   HOH B 385       9.706 -63.742  11.410  1.00 31.21           O  
-HETATM 4711  O   HOH B 386      11.876 -51.223  24.753  1.00 28.73           O  
-HETATM 4712  O   HOH B 387     -12.290 -51.460  26.942  1.00 23.74           O  
-HETATM 4713  O   HOH B 388      -8.480 -48.347  31.608  1.00 22.31           O  
-HETATM 4714  O   HOH B 389      -2.728 -62.277   0.178  1.00 47.52           O  
-HETATM 4715  O   HOH B 390      12.621 -48.974  11.061  1.00 34.66           O  
-HETATM 4716  O   HOH B 391      -2.050 -40.684  26.341  1.00 35.35           O  
-HETATM 4717  O   HOH B 392     -16.307 -56.257  23.090  1.00 32.22           O  
-HETATM 4718  O   HOH B 393      13.203 -58.951  22.681  1.00 33.34           O  
-HETATM 4719  O   HOH B 394     -11.792 -67.198  15.898  1.00 26.49           O  
-HETATM 4720  O   HOH B 395      -2.250 -36.186  19.741  1.00 33.17           O  
-HETATM 4721  O   HOH B 396      -3.668 -45.056 -15.392  1.00 24.75           O  
-HETATM 4722  O   HOH B 397       5.548 -17.387  -8.440  1.00 37.50           O  
-HETATM 4723  O   HOH B 398      15.813 -41.646  20.950  1.00 28.77           O  
-HETATM 4724  O   HOH B 399       2.793 -60.059  38.243  1.00 35.94           O  
-HETATM 4725  O   HOH B 400      -6.441 -56.291  -2.241  1.00 30.27           O  
-HETATM 4726  O   HOH B 401     -11.308 -41.338  17.828  1.00 33.95           O  
-HETATM 4727  O   HOH B 402      -7.859 -35.293  18.170  1.00 37.44           O  
-HETATM 4728  O   HOH B 403     -11.335 -47.865  17.437  1.00 40.75           O  
-HETATM 4729  O   HOH B 404      12.430 -40.789  -1.602  1.00 29.88           O  
-HETATM 4730  O   HOH B 405      -8.576 -77.893  20.716  1.00 39.83           O  
-HETATM 4731  O   HOH B 406      19.888 -31.286  10.591  1.00 26.73           O  
-HETATM 4732  O   HOH B 407      -1.807 -59.608   5.393  1.00 12.47           O  
-HETATM 4733  O   HOH B 408       1.267 -73.048  29.715  1.00 34.06           O  
-HETATM 4734  O   HOH B 409       8.548 -73.475  25.717  1.00 29.81           O  
-HETATM 4735  O   HOH B 410      -5.521 -70.967  14.123  1.00 23.15           O  
-HETATM 4736  O   HOH B 411      -8.399 -56.267   3.280  1.00 19.67           O  
-HETATM 4737  O   HOH B 412       1.139 -18.577 -10.822  1.00 38.30           O  
-HETATM 4738  O   HOH B 413       3.614 -57.261   5.542  1.00 16.77           O  
-HETATM 4739  O   HOH B 414     -11.157 -54.959  28.263  1.00 25.40           O  
-HETATM 4740  O   HOH B 415      -9.106 -49.439  -4.680  1.00 54.92           O  
-HETATM 4741  O   HOH B 416      -8.762 -27.113 -11.086  1.00 33.45           O  
-HETATM 4742  O   HOH B 417      -5.738 -74.291  26.334  1.00 48.41           O  
-HETATM 4743  O   HOH B 418     -14.173 -36.875  -1.862  1.00 56.36           O  
-HETATM 4744  O   HOH B 419      -7.883 -48.157  -7.617  1.00 25.60           O  
-HETATM 4745  O   HOH B 420      -6.650 -67.530  12.657  1.00 29.47           O  
-HETATM 4746  O   HOH B 421       9.859 -28.782   2.650  1.00 25.82           O  
-HETATM 4747  O   HOH B 422      17.135 -45.755   6.131  1.00 26.38           O  
-HETATM 4748  O   HOH B 423      16.066 -47.052  16.513  1.00 26.96           O  
-HETATM 4749  O   HOH B 424      -4.563 -40.608  23.125  1.00 34.14           O  
-HETATM 4750  O   HOH B 425      -5.881 -53.039  24.439  1.00 12.80           O  
-HETATM 4751  O   HOH B 426     -11.357 -70.126  17.386  1.00 27.70           O  
-HETATM 4752  O   HOH B 427      14.866 -48.801  20.809  1.00 26.56           O  
-HETATM 4753  O   HOH B 428     -14.605 -44.669   4.007  1.00 24.23           O  
-HETATM 4754  O   HOH B 429      -6.937 -54.014   3.312  1.00 63.70           O  
-HETATM 4755  O   HOH B 430      -8.403 -27.220 -13.663  1.00 26.98           O  
-CONECT   37 1694                                                                
-CONECT 1694   37                                                                
-CONECT 2294 3953                                                                
-CONECT 3953 2294                                                                
-CONECT 4473 4474 4478                                                           
-CONECT 4474 4473 4479                                                           
-CONECT 4475 4479                                                                
-CONECT 4476 4479                                                                
-CONECT 4477 4479                                                                
-CONECT 4478 4473                                                                
-CONECT 4479 4474 4475 4476 4477                                                 
-CONECT 4480 4481 4485                                                           
-CONECT 4481 4480 4486                                                           
-CONECT 4482 4486                                                                
-CONECT 4483 4486                                                                
-CONECT 4484 4486                                                                
-CONECT 4485 4480                                                                
-CONECT 4486 4481 4482 4483 4484                                                 
-MASTER      420    0    2   34   26    0    4    6 4667    2   18   46          
-END                                                                             
diff --git a/plip/test/pdb/2w0s.pdb b/plip/test/pdb/2w0s.pdb
deleted file mode 100644
index 9e81051..0000000
--- a/plip/test/pdb/2w0s.pdb
+++ /dev/null
@@ -1,3928 +0,0 @@
-HEADER    TRANSFERASE                             08-OCT-08   2W0S              
-TITLE     CRYSTAL STRUCTURE OF VACCINIA VIRUS THYMIDYLATE KINASE                
-TITLE    2 BOUND TO BRIVUDIN-5'-MONOPHOSPHATE                                   
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: THYMIDYLATE KINASE;                                        
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 SYNONYM: DTMP KINASE;                                                
-COMPND   5 EC: 2.7.4.9;                                                         
-COMPND   6 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS COPENHAGEN;                      
-SOURCE   3 ORGANISM_TAXID: 10249;                                               
-SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
-SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) ROSETTA PLYSS;                   
-SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
-KEYWDS    NUCLEOTIDE BIOSYNTHESIS, ATP-BINDING, NUCLEOTIDE-BINDING,             
-KEYWDS   2 KINASE, POXVIRUS, TMP KINASE, TRANSFERASE                            
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    C.CAILLAT,D.TOPALIS,L.A.AGROFOGLIO,S.POCHET,J.BALZARINI,              
-AUTHOR   2 D.DEVILLE-BONNE,P.MEYER                                              
-REVDAT   5   20-NOV-13 2W0S    1       JRNL   REMARK VERSN                      
-REVDAT   4   16-JUN-09 2W0S    1       REMARK                                   
-REVDAT   3   24-FEB-09 2W0S    1       VERSN                                    
-REVDAT   2   18-NOV-08 2W0S    1       JRNL                                     
-REVDAT   1   21-OCT-08 2W0S    0                                                
-JRNL        AUTH   C.CAILLAT,D.TOPALIS,L.A.AGROFOGLIO,S.POCHET,                 
-JRNL        AUTH 2 J.BALZARINI,D.DEVILLE-BONNE,P.MEYER                          
-JRNL        TITL   CRYSTAL STRUCTURE OF POXVIRUS THYMIDYLATE KINASE:            
-JRNL        TITL 2 AN UNEXPECTED DIMERIZATION HAS IMPLICATIONS FOR              
-JRNL        TITL 3 ANTIVIRAL THERAPY                                            
-JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105 16900 2008              
-JRNL        REFN                   ISSN 0027-8424                               
-JRNL        PMID   18971333                                                     
-JRNL        DOI    10.1073/PNAS.0804525105                                      
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.92 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : ML                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.918                          
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.852                         
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.45                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.54                          
-REMARK   3   NUMBER OF REFLECTIONS             : 18237                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2196                          
-REMARK   3   R VALUE            (WORKING SET) : 0.2124                          
-REMARK   3   FREE R VALUE                     : 0.2828                          
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.11                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1843                            
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 36.8547 -  6.8468    0.99     1251   142  0.1780 0.2295        
-REMARK   3     2  6.8468 -  5.4402    1.00     1276   144  0.1908 0.2530        
-REMARK   3     3  5.4402 -  4.7541    1.00     1269   146  0.1612 0.2219        
-REMARK   3     4  4.7541 -  4.3202    1.00     1257   144  0.1577 0.2449        
-REMARK   3     5  4.3202 -  4.0109    1.00     1256   142  0.1871 0.2277        
-REMARK   3     6  4.0109 -  3.7747    1.00     1267   141  0.2107 0.2828        
-REMARK   3     7  3.7747 -  3.5858    1.00     1271   143  0.2104 0.3475        
-REMARK   3     8  3.5858 -  3.4298    1.00     1255   141  0.2349 0.3458        
-REMARK   3     9  3.4298 -  3.2979    1.00     1286   144  0.2418 0.3516        
-REMARK   3    10  3.2979 -  3.1842    1.00     1269   143  0.2415 0.3369        
-REMARK   3    11  3.1842 -  3.0846    1.00     1249   136  0.2572 0.2850        
-REMARK   3    12  3.0846 -  2.9965    1.00     1270   144  0.2773 0.3240        
-REMARK   3    13  2.9965 -  2.9177    0.96     1218   133  0.3070 0.3897        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.11                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
-REMARK   3   K_SOL              : 0.335                                         
-REMARK   3   B_SOL              : 24.359                                        
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.44             
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.12            
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 41.23                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -7.6175                                              
-REMARK   3    B22 (A**2) : 19.3659                                              
-REMARK   3    B33 (A**2) : -11.7485                                             
-REMARK   3    B12 (A**2) : 0.0000                                               
-REMARK   3    B13 (A**2) : -0.0000                                              
-REMARK   3    B23 (A**2) : 0.0000                                               
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.010           3388                                  
-REMARK   3   ANGLE     :  1.361           4581                                  
-REMARK   3   CHIRALITY :  0.082            512                                  
-REMARK   3   PLANARITY :  0.005            574                                  
-REMARK   3   DIHEDRAL  : 21.782           1253                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : 2                                           
-REMARK   3   NCS GROUP : 1                                                      
-REMARK   3    NCS OPERATOR : 1                                                  
-REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:60 )                  
-REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 2:60 )                  
-REMARK   3     ATOM PAIRS NUMBER  : 466                                         
-REMARK   3     RMSD               : 0.052                                       
-REMARK   3   NCS GROUP : 2                                                      
-REMARK   3    NCS OPERATOR : 1                                                  
-REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 64:204 )                
-REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 64:204 )                
-REMARK   3     ATOM PAIRS NUMBER  : 1132                                        
-REMARK   3     RMSD               : 0.052                                       
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 2W0S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  08-OCT-08.                 
-REMARK 100 THE PDBE ID CODE IS EBI-37704.                                       
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : NULL                               
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : NULL                               
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ESRF                               
-REMARK 200  BEAMLINE                       : ID23-1                             
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9198                             
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
-REMARK 200  DATA SCALING SOFTWARE          : XDS                                
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69977                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.92                               
-REMARK 200  RESOLUTION RANGE LOW       (A) : 49.75                              
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
-REMARK 200  DATA REDUNDANCY                : 7                                  
-REMARK 200  R MERGE                    (I) : 0.12                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.90                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.92                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.07                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 7                                  
-REMARK 200  R MERGE FOR SHELL          (I) : 0.52                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASER                                                
-REMARK 200 STARTING MODEL: PDB ENTRY 2V54                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NONE                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 43.5                                      
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 2000 MME, 100 MM                 
-REMARK 280  TRIS-HCL PH 8.5, 5 MM MGCL2, 28 MM BVDU                             
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.18500            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.52000            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.17500            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.52000            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.18500            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.17500            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2                                                    
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 300 DETAILS: THIS ENTRY CONTAINS A SECONDARY BVP (BVP 1209)              
-REMARK 300  BINDING SITE THAT IS PRESENT AT THE DIMERIC INTERFACE.              
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 4210 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 17550 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.22 KCAL/MOL                       
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000      -29.18500            
-REMARK 350   BIOMT2   1  0.000000 -1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000      -47.52000            
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 4040 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 17710 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.05 KCAL/MOL                       
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -29.18500            
-REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       47.52000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     MET B     1                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     ASN A  31    CB   CG   OD1  ND2                                  
-REMARK 470     LYS A 133    CB   CG   CD   CE   NZ                              
-REMARK 470     ASN B  31    CB   CG   OD1  ND2                                  
-REMARK 470     LYS B 133    CB   CG   CD   CE   NZ                              
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
-REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
-REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
-REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
-REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
-REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
-REMARK 500                                                                      
-REMARK 500 DISTANCE CUTOFF:                                                     
-REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
-REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
-REMARK 500                                                                      
-REMARK 500   O    SER A   114     ND2  ASN B    60     2455      2.01           
-REMARK 500   O    SER A   117     OD1  ASN B    60     2455      1.99           
-REMARK 500   OD1  ASN B    60     O    SER A   117     2454      1.99           
-REMARK 500   ND2  ASN B    60     O    SER A   114     2454      2.01           
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    THR A  43     -172.15    -66.91                                   
-REMARK 500    LYS A  57      144.23   -178.19                                   
-REMARK 500    ARG A  93      149.29     60.00                                   
-REMARK 500    TYR A  94     -156.91   -160.52                                   
-REMARK 500    LYS A 133        6.97    -65.02                                   
-REMARK 500    THR B  43     -174.48    -64.66                                   
-REMARK 500    LYS B  57      143.67   -179.49                                   
-REMARK 500    ARG B  93      147.30     63.35                                   
-REMARK 500    TYR B  94     -156.02   -159.66                                   
-REMARK 500    LYS B 133        6.53    -64.72                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 620                                                                      
-REMARK 620 METAL COORDINATION                                                   
-REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
-REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG A1206  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 GLU A 145   OE2                                                    
-REMARK 620 2 ASP A  13   OD1  81.9                                              
-REMARK 620 N                    1                                               
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG B1206  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 ASP B  13   OD1                                                    
-REMARK 620 2 GLU B 145   OE2  76.1                                              
-REMARK 620 3 BVP B1207   O3P  85.5 161.5                                        
-REMARK 620 N                    1     2                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1205                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1205                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1206                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1206                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BVP A1207                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BVP B1207                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1208                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1208                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BVP B1209                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 2V54   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF VACCINIA VIRUS                                 
-REMARK 900  THYMIDYLATE KINASE BOUND TO TDP                                     
-DBREF  2W0S A    1   204  UNP    P68693   KTHY_VACCC       1    204             
-DBREF  2W0S B    1   204  UNP    P68693   KTHY_VACCC       1    204             
-SEQRES   1 A  204  MET SER ARG GLY ALA LEU ILE VAL PHE GLU GLY LEU ASP          
-SEQRES   2 A  204  LYS SER GLY LYS THR THR GLN CYS MET ASN ILE MET GLU          
-SEQRES   3 A  204  SER ILE PRO ALA ASN THR ILE LYS TYR LEU ASN PHE PRO          
-SEQRES   4 A  204  GLN ARG SER THR VAL THR GLY LYS MET ILE ASP ASP TYR          
-SEQRES   5 A  204  LEU THR ARG LYS LYS THR TYR ASN ASP HIS ILE VAL ASN          
-SEQRES   6 A  204  LEU LEU PHE CYS ALA ASN ARG TRP GLU PHE ALA SER PHE          
-SEQRES   7 A  204  ILE GLN GLU GLN LEU GLU GLN GLY ILE THR LEU ILE VAL          
-SEQRES   8 A  204  ASP ARG TYR ALA PHE SER GLY VAL ALA TYR ALA ALA ALA          
-SEQRES   9 A  204  LYS GLY ALA SER MET THR LEU SER LYS SER TYR GLU SER          
-SEQRES  10 A  204  GLY LEU PRO LYS PRO ASP LEU VAL ILE PHE LEU GLU SER          
-SEQRES  11 A  204  GLY SER LYS GLU ILE ASN ARG ASN VAL GLY GLU GLU ILE          
-SEQRES  12 A  204  TYR GLU ASP VAL THR PHE GLN GLN LYS VAL LEU GLN GLU          
-SEQRES  13 A  204  TYR LYS LYS MET ILE GLU GLU GLY ASP ILE HIS TRP GLN          
-SEQRES  14 A  204  ILE ILE SER SER GLU PHE GLU GLU ASP VAL LYS LYS GLU          
-SEQRES  15 A  204  LEU ILE LYS ASN ILE VAL ILE GLU ALA ILE HIS THR VAL          
-SEQRES  16 A  204  THR GLY PRO VAL GLY GLN LEU TRP MET                          
-SEQRES   1 B  204  MET SER ARG GLY ALA LEU ILE VAL PHE GLU GLY LEU ASP          
-SEQRES   2 B  204  LYS SER GLY LYS THR THR GLN CYS MET ASN ILE MET GLU          
-SEQRES   3 B  204  SER ILE PRO ALA ASN THR ILE LYS TYR LEU ASN PHE PRO          
-SEQRES   4 B  204  GLN ARG SER THR VAL THR GLY LYS MET ILE ASP ASP TYR          
-SEQRES   5 B  204  LEU THR ARG LYS LYS THR TYR ASN ASP HIS ILE VAL ASN          
-SEQRES   6 B  204  LEU LEU PHE CYS ALA ASN ARG TRP GLU PHE ALA SER PHE          
-SEQRES   7 B  204  ILE GLN GLU GLN LEU GLU GLN GLY ILE THR LEU ILE VAL          
-SEQRES   8 B  204  ASP ARG TYR ALA PHE SER GLY VAL ALA TYR ALA ALA ALA          
-SEQRES   9 B  204  LYS GLY ALA SER MET THR LEU SER LYS SER TYR GLU SER          
-SEQRES  10 B  204  GLY LEU PRO LYS PRO ASP LEU VAL ILE PHE LEU GLU SER          
-SEQRES  11 B  204  GLY SER LYS GLU ILE ASN ARG ASN VAL GLY GLU GLU ILE          
-SEQRES  12 B  204  TYR GLU ASP VAL THR PHE GLN GLN LYS VAL LEU GLN GLU          
-SEQRES  13 B  204  TYR LYS LYS MET ILE GLU GLU GLY ASP ILE HIS TRP GLN          
-SEQRES  14 B  204  ILE ILE SER SER GLU PHE GLU GLU ASP VAL LYS LYS GLU          
-SEQRES  15 B  204  LEU ILE LYS ASN ILE VAL ILE GLU ALA ILE HIS THR VAL          
-SEQRES  16 B  204  THR GLY PRO VAL GLY GLN LEU TRP MET                          
-HET     MG  B1205       1                                                       
-HET     MG  A1205       1                                                       
-HET     MG  A1206       1                                                       
-HET     MG  B1206       1                                                       
-HET    BVP  A1207      23                                                       
-HET    BVP  B1207      23                                                       
-HET    SO4  A1208       5                                                       
-HET    SO4  B1208       5                                                       
-HET    BVP  B1209      23                                                       
-HETNAM     BVP (E)-5-(2-BROMOVINYL)-2'-DEOXYURIDINE-5'-                         
-HETNAM   2 BVP  MONOPHOSPHATE                                                   
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM      MG MAGNESIUM ION                                                    
-FORMUL   3  BVP    3(C11 H14 BR N2 O8 P)                                        
-FORMUL   4  SO4    2(O4 S 2-)                                                   
-FORMUL   5   MG    4(MG 2+)                                                     
-FORMUL   6  HOH   *6(H2 O1)                                                     
-HELIX    1   1 GLY A   16  ILE A   28  1                                  13    
-HELIX    2   2 THR A   43  THR A   54  1                                  12    
-HELIX    3   3 ASN A   60  GLU A   74  1                                  15    
-HELIX    4   4 PHE A   75  GLN A   85  1                                  11    
-HELIX    5   5 TYR A   94  LYS A  105  1                                  12    
-HELIX    6   6 SER A  108  SER A  117  1                                  10    
-HELIX    7   7 GLY A  131  ASN A  136  1                                   6    
-HELIX    8   8 ASP A  146  GLU A  162  1                                  17    
-HELIX    9   9 GLU A  176  THR A  194  1                                  19    
-HELIX   10  10 GLY B   16  ILE B   28  1                                  13    
-HELIX   11  11 THR B   43  THR B   54  1                                  12    
-HELIX   12  12 ASN B   60  GLU B   74  1                                  15    
-HELIX   13  13 PHE B   75  GLN B   85  1                                  11    
-HELIX   14  14 TYR B   94  LYS B  105  1                                  12    
-HELIX   15  15 SER B  108  SER B  117  1                                  10    
-HELIX   16  16 GLY B  131  ASN B  136  1                                   6    
-HELIX   17  17 ASP B  146  GLU B  163  1                                  18    
-HELIX   18  18 GLU B  176  THR B  194  1                                  19    
-SHEET    1  AA 5 ILE A  33  ASN A  37  0                                        
-SHEET    2  AA 5 THR A  88  ASP A  92  1  O  THR A  88   N  LYS A  34           
-SHEET    3  AA 5 LEU A   6  GLY A  11  1  O  ILE A   7   N  VAL A  91           
-SHEET    4  AA 5 LEU A 124  LEU A 128  1  O  LEU A 124   N  VAL A   8           
-SHEET    5  AA 5 TRP A 168  ILE A 171  1  O  GLN A 169   N  PHE A 127           
-SHEET    1  AB 2 PRO A 120  LYS A 121  0                                        
-SHEET    2  AB 2 GLY A 200  GLN A 201 -1  O  GLY A 200   N  LYS A 121           
-SHEET    1  BA 5 ILE B  33  ASN B  37  0                                        
-SHEET    2  BA 5 THR B  88  ASP B  92  1  O  THR B  88   N  LYS B  34           
-SHEET    3  BA 5 LEU B   6  GLY B  11  1  O  ILE B   7   N  VAL B  91           
-SHEET    4  BA 5 LEU B 124  LEU B 128  1  O  LEU B 124   N  VAL B   8           
-SHEET    5  BA 5 TRP B 168  ILE B 171  1  O  GLN B 169   N  PHE B 127           
-SHEET    1  BB 2 PRO B 120  LYS B 121  0                                        
-SHEET    2  BB 2 GLY B 200  GLN B 201 -1  O  GLY B 200   N  LYS B 121           
-LINK        MG    MG A1206                 OE2 GLU A 145     1555   1555  2.53  
-LINK        MG    MG A1206                 OD1 ASP A  13     1555   1555  2.43  
-LINK        MG    MG B1205                 OD2 ASP B  92     1555   1555  2.66  
-LINK        MG    MG B1206                 OE2 GLU B 145     1555   1555  2.90  
-LINK        MG    MG B1206                 O3P BVP B1207     1555   1555  2.55  
-LINK        MG    MG B1206                 OD1 ASP B  13     1555   1555  2.42  
-CISPEP   1 PHE A   38    PRO A   39          0         3.18                     
-CISPEP   2 PHE B   38    PRO B   39          0         4.58                     
-SITE     1 AC1  4 THR B  18  ASN B  37  ASP B  92  BVP B1207                    
-SITE     1 AC2  4 THR A  18  ASN A  37  ASP A  92  BVP A1207                    
-SITE     1 AC3  4 ASP A  13  GLU A 142  GLU A 145  BVP A1207                    
-SITE     1 AC4  4 ASP B  13  GLU B 142  GLU B 145  BVP B1207                    
-SITE     1 AC5 14 ASP A  13  PHE A  38  ARG A  41  VAL A  64                    
-SITE     2 AC5 14 ASN A  65  PHE A  68  ARG A  72  ARG A  93                    
-SITE     3 AC5 14 GLY A  98  TYR A 101  LYS A 105  TYR A 144                    
-SITE     4 AC5 14  MG A1205   MG A1206                                          
-SITE     1 AC6 14 ASP B  13  PHE B  38  ARG B  41  ASN B  65                    
-SITE     2 AC6 14 PHE B  68  ARG B  72  ARG B  93  GLY B  98                    
-SITE     3 AC6 14 TYR B 101  ALA B 102  LYS B 105  TYR B 144                    
-SITE     4 AC6 14  MG B1205   MG B1206                                          
-SITE     1 AC7  5 LYS A  14  SER A  15  GLY A  16  LYS A  17                    
-SITE     2 AC7  5 THR A  18                                                     
-SITE     1 AC8  5 LYS B  14  SER B  15  GLY B  16  LYS B  17                    
-SITE     2 AC8  5 THR B  18                                                     
-SITE     1 AC9  4 ASN A  60  HIS A  62  ILE A  63  TRP B  73                    
-CRYST1   58.370   78.350   95.040  90.00  90.00  90.00 P 21 21 21    8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.017132  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.012763  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.010522        0.00000                         
-ATOM      1  N   SER A   2     -14.274  18.869 -18.571  1.00 56.66           N  
-ATOM      2  CA  SER A   2     -14.287  17.623 -19.332  1.00 68.41           C  
-ATOM      3  C   SER A   2     -14.030  16.425 -18.421  1.00 66.84           C  
-ATOM      4  O   SER A   2     -13.205  15.557 -18.719  1.00 65.01           O  
-ATOM      5  CB  SER A   2     -13.262  17.657 -20.465  1.00 60.00           C  
-ATOM      6  OG  SER A   2     -13.356  16.487 -21.262  1.00 64.40           O  
-ATOM      7  N   ARG A   3     -14.741  16.391 -17.303  1.00 47.49           N  
-ATOM      8  CA  ARG A   3     -14.696  15.248 -16.400  1.00 48.49           C  
-ATOM      9  C   ARG A   3     -15.296  14.021 -17.059  1.00 44.50           C  
-ATOM     10  O   ARG A   3     -15.763  14.082 -18.199  1.00 36.51           O  
-ATOM     11  CB  ARG A   3     -15.495  15.555 -15.142  1.00 30.04           C  
-ATOM     12  CG  ARG A   3     -16.711  16.396 -15.434  1.00 41.38           C  
-ATOM     13  CD  ARG A   3     -17.551  16.618 -14.192  1.00 47.98           C  
-ATOM     14  NE  ARG A   3     -18.825  15.905 -14.262  1.00 41.36           N  
-ATOM     15  CZ  ARG A   3     -19.986  16.511 -14.480  1.00 44.53           C  
-ATOM     16  NH1 ARG A   3     -21.098  15.811 -14.528  1.00 43.95           N  
-ATOM     17  NH2 ARG A   3     -20.033  17.828 -14.644  1.00 58.68           N  
-ATOM     18  N   GLY A   4     -15.272  12.905 -16.331  1.00 34.95           N  
-ATOM     19  CA  GLY A   4     -16.114  11.763 -16.640  1.00 32.89           C  
-ATOM     20  C   GLY A   4     -17.562  12.072 -16.270  1.00 39.88           C  
-ATOM     21  O   GLY A   4     -17.874  13.076 -15.606  1.00 30.54           O  
-ATOM     22  N   ALA A   5     -18.464  11.213 -16.720  1.00 38.26           N  
-ATOM     23  CA  ALA A   5     -19.864  11.359 -16.374  1.00 34.81           C  
-ATOM     24  C   ALA A   5     -20.233  10.423 -15.221  1.00 34.04           C  
-ATOM     25  O   ALA A   5     -19.730   9.297 -15.128  1.00 26.72           O  
-ATOM     26  CB  ALA A   5     -20.739  11.096 -17.595  1.00 31.37           C  
-ATOM     27  N   LEU A   6     -21.094  10.903 -14.330  1.00 35.29           N  
-ATOM     28  CA  LEU A   6     -21.632  10.042 -13.288  1.00 34.86           C  
-ATOM     29  C   LEU A   6     -22.944   9.435 -13.741  1.00 32.11           C  
-ATOM     30  O   LEU A   6     -23.977  10.104 -13.743  1.00 33.41           O  
-ATOM     31  CB  LEU A   6     -21.856  10.798 -11.988  1.00 34.19           C  
-ATOM     32  CG  LEU A   6     -22.438   9.878 -10.915  1.00 34.24           C  
-ATOM     33  CD1 LEU A   6     -21.523   8.651 -10.719  1.00 28.19           C  
-ATOM     34  CD2 LEU A   6     -22.668  10.643  -9.616  1.00 28.92           C  
-ATOM     35  N   ILE A   7     -22.904   8.163 -14.111  1.00 28.19           N  
-ATOM     36  CA  ILE A   7     -24.096   7.481 -14.590  1.00 30.93           C  
-ATOM     37  C   ILE A   7     -24.619   6.438 -13.592  1.00 29.31           C  
-ATOM     38  O   ILE A   7     -23.911   5.506 -13.218  1.00 28.58           O  
-ATOM     39  CB  ILE A   7     -23.820   6.864 -15.962  1.00 27.12           C  
-ATOM     40  CG1 ILE A   7     -23.349   7.976 -16.895  1.00 26.53           C  
-ATOM     41  CG2 ILE A   7     -25.063   6.154 -16.509  1.00 26.97           C  
-ATOM     42  CD1 ILE A   7     -23.009   7.501 -18.279  1.00 40.59           C  
-ATOM     43  N   VAL A   8     -25.865   6.600 -13.169  1.00 21.72           N  
-ATOM     44  CA  VAL A   8     -26.440   5.689 -12.192  1.00 27.71           C  
-ATOM     45  C   VAL A   8     -27.582   4.833 -12.722  1.00 33.18           C  
-ATOM     46  O   VAL A   8     -28.507   5.333 -13.368  1.00 33.42           O  
-ATOM     47  CB  VAL A   8     -26.979   6.456 -10.984  1.00 33.28           C  
-ATOM     48  CG1 VAL A   8     -27.646   5.503 -10.024  1.00 23.46           C  
-ATOM     49  CG2 VAL A   8     -25.853   7.246 -10.330  1.00 31.57           C  
-ATOM     50  N   PHE A   9     -27.522   3.540 -12.421  1.00 33.62           N  
-ATOM     51  CA  PHE A   9     -28.600   2.620 -12.756  1.00 31.73           C  
-ATOM     52  C   PHE A   9     -29.498   2.383 -11.554  1.00 25.64           C  
-ATOM     53  O   PHE A   9     -29.008   2.039 -10.490  1.00 24.85           O  
-ATOM     54  CB  PHE A   9     -28.029   1.282 -13.237  1.00 30.55           C  
-ATOM     55  CG  PHE A   9     -27.738   1.236 -14.714  1.00 36.65           C  
-ATOM     56  CD1 PHE A   9     -26.491   1.567 -15.189  1.00 37.29           C  
-ATOM     57  CD2 PHE A   9     -28.715   0.858 -15.625  1.00 39.06           C  
-ATOM     58  CE1 PHE A   9     -26.216   1.519 -16.553  1.00 41.28           C  
-ATOM     59  CE2 PHE A   9     -28.455   0.817 -16.986  1.00 37.38           C  
-ATOM     60  CZ  PHE A   9     -27.203   1.141 -17.450  1.00 40.88           C  
-ATOM     61  N   GLU A  10     -30.808   2.579 -11.727  1.00 35.38           N  
-ATOM     62  CA  GLU A  10     -31.816   2.266 -10.697  1.00 27.30           C  
-ATOM     63  C   GLU A  10     -32.930   1.363 -11.248  1.00 34.27           C  
-ATOM     64  O   GLU A  10     -33.049   1.150 -12.455  1.00 38.67           O  
-ATOM     65  CB  GLU A  10     -32.447   3.540 -10.121  1.00 21.34           C  
-ATOM     66  CG  GLU A  10     -31.538   4.446  -9.277  1.00 27.11           C  
-ATOM     67  CD  GLU A  10     -31.210   3.873  -7.886  1.00 30.84           C  
-ATOM     68  OE1 GLU A  10     -31.709   2.772  -7.569  1.00 32.01           O  
-ATOM     69  OE2 GLU A  10     -30.453   4.520  -7.111  1.00 25.94           O  
-ATOM     70  N   GLY A  11     -33.759   0.858 -10.347  1.00 43.09           N  
-ATOM     71  CA  GLY A  11     -34.859  -0.025 -10.696  1.00 39.34           C  
-ATOM     72  C   GLY A  11     -35.139  -0.988  -9.556  1.00 37.63           C  
-ATOM     73  O   GLY A  11     -34.388  -1.037  -8.579  1.00 38.10           O  
-ATOM     74  N   LEU A  12     -36.214  -1.755  -9.672  1.00 36.58           N  
-ATOM     75  CA  LEU A  12     -36.516  -2.777  -8.674  1.00 35.28           C  
-ATOM     76  C   LEU A  12     -35.480  -3.888  -8.717  1.00 36.63           C  
-ATOM     77  O   LEU A  12     -34.588  -3.879  -9.565  1.00 34.00           O  
-ATOM     78  CB  LEU A  12     -37.913  -3.351  -8.892  1.00 29.84           C  
-ATOM     79  CG  LEU A  12     -39.037  -2.304  -8.910  1.00 35.45           C  
-ATOM     80  CD1 LEU A  12     -40.359  -2.991  -9.134  1.00 40.56           C  
-ATOM     81  CD2 LEU A  12     -39.095  -1.452  -7.638  1.00 34.03           C  
-ATOM     82  N   ASP A  13     -35.577  -4.825  -7.779  1.00 37.56           N  
-ATOM     83  CA  ASP A  13     -34.745  -6.017  -7.830  1.00 42.80           C  
-ATOM     84  C   ASP A  13     -35.162  -6.835  -9.060  1.00 52.77           C  
-ATOM     85  O   ASP A  13     -36.341  -6.864  -9.427  1.00 57.87           O  
-ATOM     86  CB  ASP A  13     -34.877  -6.867  -6.550  1.00 51.30           C  
-ATOM     87  CG  ASP A  13     -33.756  -6.622  -5.550  1.00 42.41           C  
-ATOM     88  OD1 ASP A  13     -32.847  -7.481  -5.394  1.00 31.52           O  
-ATOM     89  OD2 ASP A  13     -33.801  -5.563  -4.907  1.00 41.76           O  
-ATOM     90  N   LYS A  14     -34.189  -7.482  -9.696  1.00 49.67           N  
-ATOM     91  CA  LYS A  14     -34.445  -8.359 -10.832  1.00 44.73           C  
-ATOM     92  C   LYS A  14     -34.893  -7.589 -12.078  1.00 47.50           C  
-ATOM     93  O   LYS A  14     -35.418  -8.181 -13.023  1.00 55.73           O  
-ATOM     94  CB  LYS A  14     -35.492  -9.408 -10.450  1.00 54.25           C  
-ATOM     95  CG  LYS A  14     -35.251 -10.074  -9.099  1.00 52.55           C  
-ATOM     96  CD  LYS A  14     -34.008 -10.960  -9.130  1.00 54.35           C  
-ATOM     97  CE  LYS A  14     -33.718 -11.590  -7.774  1.00 50.97           C  
-ATOM     98  NZ  LYS A  14     -32.458 -12.375  -7.814  1.00 56.60           N  
-ATOM     99  N   SER A  15     -34.695  -6.271 -12.073  1.00 47.11           N  
-ATOM    100  CA  SER A  15     -34.983  -5.437 -13.244  1.00 39.36           C  
-ATOM    101  C   SER A  15     -33.846  -5.545 -14.230  1.00 36.76           C  
-ATOM    102  O   SER A  15     -33.887  -4.925 -15.286  1.00 34.58           O  
-ATOM    103  CB  SER A  15     -35.143  -3.968 -12.858  1.00 38.75           C  
-ATOM    104  OG  SER A  15     -33.908  -3.454 -12.391  1.00 46.00           O  
-ATOM    105  N   GLY A  16     -32.814  -6.310 -13.858  1.00 45.79           N  
-ATOM    106  CA  GLY A  16     -31.679  -6.596 -14.729  1.00 46.39           C  
-ATOM    107  C   GLY A  16     -30.654  -5.488 -14.925  1.00 41.45           C  
-ATOM    108  O   GLY A  16     -29.898  -5.519 -15.886  1.00 27.30           O  
-ATOM    109  N   LYS A  17     -30.615  -4.519 -14.010  1.00 50.26           N  
-ATOM    110  CA  LYS A  17     -29.657  -3.430 -14.119  1.00 44.97           C  
-ATOM    111  C   LYS A  17     -28.207  -3.914 -14.017  1.00 35.61           C  
-ATOM    112  O   LYS A  17     -27.295  -3.277 -14.560  1.00 36.76           O  
-ATOM    113  CB  LYS A  17     -29.964  -2.298 -13.137  1.00 36.94           C  
-ATOM    114  CG  LYS A  17     -30.256  -2.746 -11.743  1.00 43.30           C  
-ATOM    115  CD  LYS A  17     -30.662  -1.567 -10.881  1.00 36.81           C  
-ATOM    116  CE  LYS A  17     -31.049  -2.081  -9.512  1.00 41.82           C  
-ATOM    117  NZ  LYS A  17     -30.154  -3.222  -9.091  1.00 54.10           N  
-ATOM    118  N   THR A  18     -27.988  -5.049 -13.369  1.00 28.96           N  
-ATOM    119  CA  THR A  18     -26.648  -5.656 -13.404  1.00 47.55           C  
-ATOM    120  C   THR A  18     -26.229  -6.102 -14.835  1.00 44.18           C  
-ATOM    121  O   THR A  18     -25.126  -5.794 -15.301  1.00 29.37           O  
-ATOM    122  CB  THR A  18     -26.496  -6.810 -12.373  1.00 41.31           C  
-ATOM    123  OG1 THR A  18     -27.042  -6.404 -11.111  1.00 58.77           O  
-ATOM    124  CG2 THR A  18     -25.036  -7.149 -12.180  1.00 39.67           C  
-ATOM    125  N   THR A  19     -27.122  -6.805 -15.531  1.00 42.38           N  
-ATOM    126  CA  THR A  19     -26.907  -7.128 -16.936  1.00 40.24           C  
-ATOM    127  C   THR A  19     -26.509  -5.898 -17.756  1.00 43.15           C  
-ATOM    128  O   THR A  19     -25.458  -5.871 -18.400  1.00 39.26           O  
-ATOM    129  CB  THR A  19     -28.183  -7.690 -17.566  1.00 46.28           C  
-ATOM    130  OG1 THR A  19     -28.805  -8.607 -16.657  1.00 61.29           O  
-ATOM    131  CG2 THR A  19     -27.860  -8.382 -18.885  1.00 39.78           C  
-ATOM    132  N   GLN A  20     -27.375  -4.891 -17.742  1.00 40.47           N  
-ATOM    133  CA  GLN A  20     -27.151  -3.668 -18.502  1.00 45.43           C  
-ATOM    134  C   GLN A  20     -25.833  -2.979 -18.146  1.00 45.60           C  
-ATOM    135  O   GLN A  20     -25.182  -2.380 -19.012  1.00 44.18           O  
-ATOM    136  CB  GLN A  20     -28.337  -2.711 -18.356  1.00 34.50           C  
-ATOM    137  CG  GLN A  20     -29.567  -3.182 -19.116  1.00 37.04           C  
-ATOM    138  CD  GLN A  20     -29.318  -3.373 -20.618  1.00 46.07           C  
-ATOM    139  OE1 GLN A  20     -28.419  -2.751 -21.209  1.00 47.55           O  
-ATOM    140  NE2 GLN A  20     -30.132  -4.227 -21.245  1.00 42.90           N  
-ATOM    141  N   CYS A  21     -25.439  -3.074 -16.879  1.00 41.94           N  
-ATOM    142  CA  CYS A  21     -24.142  -2.562 -16.457  1.00 42.47           C  
-ATOM    143  C   CYS A  21     -23.041  -3.334 -17.142  1.00 42.29           C  
-ATOM    144  O   CYS A  21     -22.030  -2.770 -17.573  1.00 36.30           O  
-ATOM    145  CB  CYS A  21     -23.982  -2.660 -14.945  1.00 36.51           C  
-ATOM    146  SG  CYS A  21     -24.636  -1.224 -14.095  1.00 40.66           S  
-ATOM    147  N   MET A  22     -23.251  -4.636 -17.237  1.00 45.05           N  
-ATOM    148  CA  MET A  22     -22.324  -5.493 -17.950  1.00 47.98           C  
-ATOM    149  C   MET A  22     -22.164  -5.081 -19.413  1.00 45.11           C  
-ATOM    150  O   MET A  22     -21.047  -5.029 -19.914  1.00 38.72           O  
-ATOM    151  CB  MET A  22     -22.767  -6.945 -17.848  1.00 54.22           C  
-ATOM    152  CG  MET A  22     -22.588  -7.508 -16.460  1.00 51.60           C  
-ATOM    153  SD  MET A  22     -20.841  -7.582 -16.020  1.00 95.28           S  
-ATOM    154  CE  MET A  22     -20.235  -8.782 -17.216  1.00 67.69           C  
-ATOM    155  N   ASN A  23     -23.273  -4.794 -20.097  1.00 45.82           N  
-ATOM    156  CA  ASN A  23     -23.196  -4.277 -21.461  1.00 48.02           C  
-ATOM    157  C   ASN A  23     -22.305  -3.039 -21.573  1.00 42.42           C  
-ATOM    158  O   ASN A  23     -21.336  -3.024 -22.311  1.00 37.06           O  
-ATOM    159  CB  ASN A  23     -24.589  -3.981 -22.017  1.00 49.17           C  
-ATOM    160  CG  ASN A  23     -25.381  -5.241 -22.275  1.00 67.05           C  
-ATOM    161  OD1 ASN A  23     -24.860  -6.348 -22.123  1.00 74.82           O  
-ATOM    162  ND2 ASN A  23     -26.645  -5.088 -22.667  1.00 71.85           N  
-ATOM    163  N   ILE A  24     -22.627  -1.994 -20.830  1.00 45.34           N  
-ATOM    164  CA  ILE A  24     -21.838  -0.782 -20.915  1.00 40.69           C  
-ATOM    165  C   ILE A  24     -20.343  -1.066 -20.708  1.00 36.00           C  
-ATOM    166  O   ILE A  24     -19.499  -0.471 -21.366  1.00 35.00           O  
-ATOM    167  CB  ILE A  24     -22.353   0.294 -19.945  1.00 31.30           C  
-ATOM    168  CG1 ILE A  24     -23.433   1.128 -20.620  1.00 33.72           C  
-ATOM    169  CG2 ILE A  24     -21.235   1.225 -19.531  1.00 32.55           C  
-ATOM    170  CD1 ILE A  24     -24.520   0.313 -21.272  1.00 51.75           C  
-ATOM    171  N   MET A  25     -20.015  -1.986 -19.813  1.00 41.82           N  
-ATOM    172  CA  MET A  25     -18.610  -2.260 -19.503  1.00 46.29           C  
-ATOM    173  C   MET A  25     -17.888  -2.928 -20.670  1.00 46.70           C  
-ATOM    174  O   MET A  25     -16.667  -2.782 -20.849  1.00 47.15           O  
-ATOM    175  CB  MET A  25     -18.495  -3.117 -18.237  1.00 39.79           C  
-ATOM    176  CG  MET A  25     -18.955  -2.388 -16.982  1.00 50.05           C  
-ATOM    177  SD  MET A  25     -18.273  -0.714 -16.848  1.00 65.89           S  
-ATOM    178  CE  MET A  25     -16.503  -1.057 -16.727  1.00 47.68           C  
-ATOM    179  N   GLU A  26     -18.658  -3.660 -21.460  1.00 39.82           N  
-ATOM    180  CA  GLU A  26     -18.127  -4.345 -22.621  1.00 38.94           C  
-ATOM    181  C   GLU A  26     -18.126  -3.422 -23.853  1.00 36.46           C  
-ATOM    182  O   GLU A  26     -17.260  -3.524 -24.713  1.00 40.17           O  
-ATOM    183  CB  GLU A  26     -18.938  -5.624 -22.866  1.00 44.80           C  
-ATOM    184  CG  GLU A  26     -18.795  -6.650 -21.738  1.00 61.99           C  
-ATOM    185  CD  GLU A  26     -20.022  -7.537 -21.562  1.00 81.17           C  
-ATOM    186  OE1 GLU A  26     -20.825  -7.666 -22.522  1.00 64.89           O  
-ATOM    187  OE2 GLU A  26     -20.180  -8.103 -20.452  1.00 78.59           O  
-ATOM    188  N   SER A  27     -19.088  -2.507 -23.904  1.00 30.54           N  
-ATOM    189  CA  SER A  27     -19.250  -1.587 -25.016  1.00 23.37           C  
-ATOM    190  C   SER A  27     -18.276  -0.393 -25.026  1.00 36.58           C  
-ATOM    191  O   SER A  27     -18.229   0.373 -25.995  1.00 31.38           O  
-ATOM    192  CB  SER A  27     -20.692  -1.073 -25.051  1.00 34.95           C  
-ATOM    193  OG  SER A  27     -21.563  -1.954 -25.769  1.00 52.61           O  
-ATOM    194  N   ILE A  28     -17.497  -0.231 -23.965  1.00 29.50           N  
-ATOM    195  CA  ILE A  28     -16.658   0.954 -23.829  1.00 28.90           C  
-ATOM    196  C   ILE A  28     -15.288   0.581 -23.285  1.00 35.45           C  
-ATOM    197  O   ILE A  28     -15.155  -0.338 -22.471  1.00 41.11           O  
-ATOM    198  CB  ILE A  28     -17.321   2.052 -22.925  1.00 30.51           C  
-ATOM    199  CG1 ILE A  28     -18.640   2.537 -23.541  1.00 22.75           C  
-ATOM    200  CG2 ILE A  28     -16.354   3.218 -22.652  1.00 22.01           C  
-ATOM    201  CD1 ILE A  28     -19.437   3.444 -22.653  1.00 24.01           C  
-ATOM    202  N   PRO A  29     -14.246   1.275 -23.764  1.00 35.08           N  
-ATOM    203  CA  PRO A  29     -12.892   0.943 -23.350  1.00 35.42           C  
-ATOM    204  C   PRO A  29     -12.669   1.175 -21.860  1.00 42.52           C  
-ATOM    205  O   PRO A  29     -12.979   2.250 -21.338  1.00 45.98           O  
-ATOM    206  CB  PRO A  29     -12.042   1.892 -24.196  1.00 35.42           C  
-ATOM    207  CG  PRO A  29     -12.860   2.091 -25.425  1.00 27.96           C  
-ATOM    208  CD  PRO A  29     -14.245   2.223 -24.895  1.00 30.66           C  
-ATOM    209  N   ALA A  30     -12.110   0.164 -21.198  1.00 35.40           N  
-ATOM    210  CA  ALA A  30     -11.993   0.160 -19.754  1.00 32.24           C  
-ATOM    211  C   ALA A  30     -10.985   1.145 -19.182  1.00 32.97           C  
-ATOM    212  O   ALA A  30     -10.987   1.378 -17.977  1.00 39.65           O  
-ATOM    213  CB  ALA A  30     -11.701  -1.250 -19.248  1.00 35.27           C  
-ATOM    214  N   ASN A  31     -10.117   1.715 -20.008  1.00 34.43           N  
-ATOM    215  CA  ASN A  31      -9.172   2.683 -19.464  1.00 35.36           C  
-ATOM    216  C   ASN A  31      -9.853   4.023 -19.129  1.00 38.09           C  
-ATOM    217  O   ASN A  31      -9.225   4.921 -18.584  1.00 40.09           O  
-ATOM    218  N   THR A  32     -11.152   4.129 -19.415  1.00 31.21           N  
-ATOM    219  CA  THR A  32     -11.886   5.397 -19.311  1.00 29.80           C  
-ATOM    220  C   THR A  32     -13.161   5.263 -18.479  1.00 41.01           C  
-ATOM    221  O   THR A  32     -13.869   6.246 -18.238  1.00 36.96           O  
-ATOM    222  CB  THR A  32     -12.339   5.898 -20.703  1.00 35.40           C  
-ATOM    223  OG1 THR A  32     -13.492   5.152 -21.145  1.00 29.21           O  
-ATOM    224  CG2 THR A  32     -11.216   5.751 -21.719  1.00 29.32           C  
-ATOM    225  N   ILE A  33     -13.462   4.044 -18.045  1.00 37.49           N  
-ATOM    226  CA  ILE A  33     -14.721   3.781 -17.376  1.00 33.92           C  
-ATOM    227  C   ILE A  33     -14.532   2.898 -16.126  1.00 36.19           C  
-ATOM    228  O   ILE A  33     -13.605   2.084 -16.065  1.00 34.31           O  
-ATOM    229  CB  ILE A  33     -15.701   3.149 -18.385  1.00 39.54           C  
-ATOM    230  CG1 ILE A  33     -17.145   3.445 -18.016  1.00 39.67           C  
-ATOM    231  CG2 ILE A  33     -15.465   1.641 -18.561  1.00 36.20           C  
-ATOM    232  CD1 ILE A  33     -18.091   2.836 -19.021  1.00 39.47           C  
-ATOM    233  N   LYS A  34     -15.397   3.068 -15.126  1.00 33.69           N  
-ATOM    234  CA  LYS A  34     -15.251   2.356 -13.854  1.00 32.78           C  
-ATOM    235  C   LYS A  34     -16.585   1.883 -13.320  1.00 30.58           C  
-ATOM    236  O   LYS A  34     -17.515   2.673 -13.179  1.00 30.18           O  
-ATOM    237  CB  LYS A  34     -14.583   3.258 -12.807  1.00 33.52           C  
-ATOM    238  CG  LYS A  34     -14.606   2.701 -11.393  1.00 29.53           C  
-ATOM    239  CD  LYS A  34     -13.787   1.428 -11.267  1.00 29.82           C  
-ATOM    240  CE  LYS A  34     -13.785   0.911  -9.833  1.00 28.45           C  
-ATOM    241  NZ  LYS A  34     -12.900  -0.269  -9.719  1.00 30.03           N  
-ATOM    242  N   TYR A  35     -16.672   0.594 -13.004  1.00 35.24           N  
-ATOM    243  CA  TYR A  35     -17.931   0.012 -12.529  1.00 35.12           C  
-ATOM    244  C   TYR A  35     -18.018  -0.006 -10.999  1.00 32.63           C  
-ATOM    245  O   TYR A  35     -17.115  -0.505 -10.326  1.00 25.71           O  
-ATOM    246  CB  TYR A  35     -18.126  -1.402 -13.097  1.00 27.09           C  
-ATOM    247  CG  TYR A  35     -19.293  -2.165 -12.502  1.00 30.65           C  
-ATOM    248  CD1 TYR A  35     -20.568  -1.623 -12.494  1.00 37.95           C  
-ATOM    249  CD2 TYR A  35     -19.121  -3.433 -11.963  1.00 31.32           C  
-ATOM    250  CE1 TYR A  35     -21.641  -2.322 -11.954  1.00 44.67           C  
-ATOM    251  CE2 TYR A  35     -20.192  -4.142 -11.421  1.00 36.37           C  
-ATOM    252  CZ  TYR A  35     -21.449  -3.584 -11.421  1.00 42.77           C  
-ATOM    253  OH  TYR A  35     -22.516  -4.289 -10.892  1.00 54.05           O  
-ATOM    254  N   LEU A  36     -19.118   0.526 -10.470  1.00 22.82           N  
-ATOM    255  CA  LEU A  36     -19.312   0.619  -9.038  1.00 27.67           C  
-ATOM    256  C   LEU A  36     -20.650   0.020  -8.579  1.00 30.37           C  
-ATOM    257  O   LEU A  36     -21.691   0.579  -8.877  1.00 33.44           O  
-ATOM    258  CB  LEU A  36     -19.243   2.090  -8.625  1.00 36.90           C  
-ATOM    259  CG  LEU A  36     -18.280   2.436  -7.472  1.00 40.45           C  
-ATOM    260  CD1 LEU A  36     -18.602   3.775  -6.812  1.00 26.31           C  
-ATOM    261  CD2 LEU A  36     -18.288   1.341  -6.433  1.00 41.78           C  
-ATOM    262  N   ASN A  37     -20.630  -1.103  -7.855  1.00 33.40           N  
-ATOM    263  CA  ASN A  37     -21.868  -1.703  -7.323  1.00 35.46           C  
-ATOM    264  C   ASN A  37     -22.207  -1.183  -5.911  1.00 36.43           C  
-ATOM    265  O   ASN A  37     -21.327  -1.028  -5.074  1.00 43.26           O  
-ATOM    266  CB  ASN A  37     -21.778  -3.249  -7.310  1.00 38.46           C  
-ATOM    267  CG  ASN A  37     -23.157  -3.947  -7.447  1.00 45.74           C  
-ATOM    268  OD1 ASN A  37     -24.131  -3.589  -6.778  1.00 51.59           O  
-ATOM    269  ND2 ASN A  37     -23.227  -4.959  -8.316  1.00 48.55           N  
-ATOM    270  N   PHE A  38     -23.477  -0.897  -5.652  1.00 33.41           N  
-ATOM    271  CA  PHE A  38     -23.947  -0.676  -4.290  1.00 25.06           C  
-ATOM    272  C   PHE A  38     -25.084  -1.643  -3.970  1.00 26.36           C  
-ATOM    273  O   PHE A  38     -25.939  -1.900  -4.818  1.00 28.90           O  
-ATOM    274  CB  PHE A  38     -24.417   0.751  -4.114  1.00 22.03           C  
-ATOM    275  CG  PHE A  38     -23.311   1.734  -4.043  1.00 25.37           C  
-ATOM    276  CD1 PHE A  38     -23.103   2.643  -5.058  1.00 36.15           C  
-ATOM    277  CD2 PHE A  38     -22.459   1.748  -2.958  1.00 28.14           C  
-ATOM    278  CE1 PHE A  38     -22.058   3.567  -4.979  1.00 31.73           C  
-ATOM    279  CE2 PHE A  38     -21.432   2.657  -2.879  1.00 29.13           C  
-ATOM    280  CZ  PHE A  38     -21.227   3.569  -3.893  1.00 24.54           C  
-ATOM    281  N   PRO A  39     -25.087  -2.196  -2.747  1.00 37.45           N  
-ATOM    282  CA  PRO A  39     -24.088  -1.837  -1.737  1.00 31.99           C  
-ATOM    283  C   PRO A  39     -22.759  -2.555  -1.963  1.00 34.34           C  
-ATOM    284  O   PRO A  39     -22.657  -3.614  -2.602  1.00 31.41           O  
-ATOM    285  CB  PRO A  39     -24.696  -2.341  -0.431  1.00 18.97           C  
-ATOM    286  CG  PRO A  39     -25.857  -3.230  -0.827  1.00 37.44           C  
-ATOM    287  CD  PRO A  39     -25.881  -3.361  -2.323  1.00 35.65           C  
-ATOM    288  N   GLN A  40     -21.732  -1.953  -1.394  1.00 32.73           N  
-ATOM    289  CA  GLN A  40     -20.379  -2.421  -1.512  1.00 26.80           C  
-ATOM    290  C   GLN A  40     -20.217  -3.371  -0.331  1.00 27.76           C  
-ATOM    291  O   GLN A  40     -19.795  -2.971   0.743  1.00 32.33           O  
-ATOM    292  CB  GLN A  40     -19.475  -1.177  -1.425  1.00 25.24           C  
-ATOM    293  CG  GLN A  40     -18.054  -1.298  -1.935  1.00 33.92           C  
-ATOM    294  CD  GLN A  40     -17.970  -1.718  -3.372  1.00 34.02           C  
-ATOM    295  OE1 GLN A  40     -16.904  -2.072  -3.861  1.00 32.61           O  
-ATOM    296  NE2 GLN A  40     -19.100  -1.717  -4.053  1.00 35.09           N  
-ATOM    297  N   ARG A  41     -20.608  -4.627  -0.517  1.00 32.74           N  
-ATOM    298  CA  ARG A  41     -20.730  -5.564   0.605  1.00 29.73           C  
-ATOM    299  C   ARG A  41     -19.412  -5.987   1.238  1.00 31.98           C  
-ATOM    300  O   ARG A  41     -19.398  -6.771   2.189  1.00 35.59           O  
-ATOM    301  CB  ARG A  41     -21.496  -6.816   0.178  1.00 17.66           C  
-ATOM    302  CG  ARG A  41     -22.904  -6.534  -0.254  1.00 21.98           C  
-ATOM    303  CD  ARG A  41     -23.671  -7.822  -0.512  1.00 30.25           C  
-ATOM    304  NE  ARG A  41     -24.815  -7.605  -1.397  1.00 43.80           N  
-ATOM    305  CZ  ARG A  41     -25.926  -8.335  -1.366  1.00 44.66           C  
-ATOM    306  NH1 ARG A  41     -26.054  -9.324  -0.481  1.00 40.29           N  
-ATOM    307  NH2 ARG A  41     -26.914  -8.071  -2.213  1.00 36.14           N  
-ATOM    308  N   SER A  42     -18.306  -5.498   0.701  1.00 24.85           N  
-ATOM    309  CA  SER A  42     -16.996  -5.915   1.200  1.00 30.60           C  
-ATOM    310  C   SER A  42     -16.568  -5.137   2.448  1.00 30.25           C  
-ATOM    311  O   SER A  42     -15.904  -5.683   3.324  1.00 33.36           O  
-ATOM    312  CB  SER A  42     -15.929  -5.837   0.089  1.00 29.79           C  
-ATOM    313  OG  SER A  42     -16.382  -5.023  -0.996  1.00 39.81           O  
-ATOM    314  N   THR A  43     -16.987  -3.878   2.541  1.00 36.18           N  
-ATOM    315  CA  THR A  43     -16.593  -3.005   3.651  1.00 47.87           C  
-ATOM    316  C   THR A  43     -17.139  -3.406   5.027  1.00 42.94           C  
-ATOM    317  O   THR A  43     -17.727  -4.470   5.200  1.00 40.84           O  
-ATOM    318  CB  THR A  43     -17.006  -1.562   3.396  1.00 35.36           C  
-ATOM    319  OG1 THR A  43     -18.416  -1.442   3.609  1.00 44.76           O  
-ATOM    320  CG2 THR A  43     -16.663  -1.176   1.975  1.00 26.99           C  
-ATOM    321  N   VAL A  44     -16.927  -2.541   6.010  1.00 43.43           N  
-ATOM    322  CA  VAL A  44     -17.367  -2.842   7.357  1.00 42.88           C  
-ATOM    323  C   VAL A  44     -18.867  -2.725   7.392  1.00 33.57           C  
-ATOM    324  O   VAL A  44     -19.553  -3.568   7.972  1.00 30.62           O  
-ATOM    325  CB  VAL A  44     -16.781  -1.884   8.413  1.00 45.58           C  
-ATOM    326  CG1 VAL A  44     -17.035  -2.453   9.794  1.00 32.38           C  
-ATOM    327  CG2 VAL A  44     -15.278  -1.636   8.193  1.00 37.19           C  
-ATOM    328  N   THR A  45     -19.377  -1.672   6.764  1.00 32.26           N  
-ATOM    329  CA  THR A  45     -20.820  -1.472   6.702  1.00 30.75           C  
-ATOM    330  C   THR A  45     -21.432  -2.409   5.671  1.00 38.80           C  
-ATOM    331  O   THR A  45     -22.630  -2.701   5.711  1.00 33.62           O  
-ATOM    332  CB  THR A  45     -21.171  -0.040   6.340  1.00 27.36           C  
-ATOM    333  OG1 THR A  45     -20.476   0.313   5.143  1.00 32.81           O  
-ATOM    334  CG2 THR A  45     -20.785   0.925   7.485  1.00 31.44           C  
-ATOM    335  N   GLY A  46     -20.594  -2.880   4.746  1.00 38.65           N  
-ATOM    336  CA  GLY A  46     -21.012  -3.849   3.752  1.00 29.85           C  
-ATOM    337  C   GLY A  46     -21.324  -5.198   4.367  1.00 27.67           C  
-ATOM    338  O   GLY A  46     -22.387  -5.764   4.131  1.00 23.98           O  
-ATOM    339  N   LYS A  47     -20.399  -5.724   5.161  1.00 32.38           N  
-ATOM    340  CA  LYS A  47     -20.572  -7.073   5.688  1.00 36.96           C  
-ATOM    341  C   LYS A  47     -21.799  -7.109   6.559  1.00 30.35           C  
-ATOM    342  O   LYS A  47     -22.535  -8.088   6.582  1.00 22.50           O  
-ATOM    343  CB  LYS A  47     -19.344  -7.537   6.459  1.00 40.12           C  
-ATOM    344  CG  LYS A  47     -18.121  -7.841   5.577  1.00 57.51           C  
-ATOM    345  CD  LYS A  47     -17.167  -8.841   6.262  1.00 80.79           C  
-ATOM    346  CE  LYS A  47     -15.830  -8.942   5.551  1.00 68.61           C  
-ATOM    347  NZ  LYS A  47     -15.151  -7.615   5.553  1.00 69.88           N  
-ATOM    348  N   MET A  48     -22.018  -6.013   7.264  1.00 33.20           N  
-ATOM    349  CA  MET A  48     -23.192  -5.889   8.090  1.00 30.96           C  
-ATOM    350  C   MET A  48     -24.443  -5.847   7.217  1.00 29.01           C  
-ATOM    351  O   MET A  48     -25.413  -6.555   7.478  1.00 34.39           O  
-ATOM    352  CB  MET A  48     -23.075  -4.654   8.987  1.00 37.95           C  
-ATOM    353  CG  MET A  48     -22.142  -4.851  10.168  1.00 36.96           C  
-ATOM    354  SD  MET A  48     -22.382  -3.590  11.431  1.00 49.50           S  
-ATOM    355  CE  MET A  48     -21.146  -2.404  10.928  1.00 35.31           C  
-ATOM    356  N   ILE A  49     -24.423  -5.028   6.173  1.00 31.97           N  
-ATOM    357  CA  ILE A  49     -25.541  -5.023   5.237  1.00 35.78           C  
-ATOM    358  C   ILE A  49     -25.786  -6.433   4.687  1.00 33.06           C  
-ATOM    359  O   ILE A  49     -26.934  -6.858   4.550  1.00 27.47           O  
-ATOM    360  CB  ILE A  49     -25.348  -4.012   4.082  1.00 33.20           C  
-ATOM    361  CG1 ILE A  49     -25.127  -2.603   4.638  1.00 36.66           C  
-ATOM    362  CG2 ILE A  49     -26.556  -4.037   3.146  1.00 20.36           C  
-ATOM    363  CD1 ILE A  49     -24.873  -1.548   3.566  1.00 30.14           C  
-ATOM    364  N   ASP A  50     -24.709  -7.160   4.391  1.00 26.58           N  
-ATOM    365  CA  ASP A  50     -24.848  -8.512   3.895  1.00 27.74           C  
-ATOM    366  C   ASP A  50     -25.613  -9.399   4.895  1.00 37.09           C  
-ATOM    367  O   ASP A  50     -26.516 -10.144   4.513  1.00 34.64           O  
-ATOM    368  CB  ASP A  50     -23.480  -9.105   3.541  1.00 23.74           C  
-ATOM    369  CG  ASP A  50     -23.583 -10.280   2.553  1.00 42.77           C  
-ATOM    370  OD1 ASP A  50     -24.540 -10.308   1.745  1.00 46.71           O  
-ATOM    371  OD2 ASP A  50     -22.709 -11.175   2.575  1.00 41.10           O  
-ATOM    372  N   ASP A  51     -25.265  -9.300   6.175  1.00 35.89           N  
-ATOM    373  CA  ASP A  51     -25.892 -10.126   7.210  1.00 38.28           C  
-ATOM    374  C   ASP A  51     -27.399  -9.863   7.246  1.00 39.95           C  
-ATOM    375  O   ASP A  51     -28.200 -10.784   7.425  1.00 37.45           O  
-ATOM    376  CB  ASP A  51     -25.258  -9.871   8.600  1.00 40.50           C  
-ATOM    377  CG  ASP A  51     -23.848 -10.496   8.759  1.00 49.11           C  
-ATOM    378  OD1 ASP A  51     -23.464 -11.401   7.981  1.00 34.38           O  
-ATOM    379  OD2 ASP A  51     -23.116 -10.078   9.686  1.00 53.27           O  
-ATOM    380  N   TYR A  52     -27.774  -8.600   7.057  1.00 31.59           N  
-ATOM    381  CA  TYR A  52     -29.173  -8.188   7.137  1.00 34.66           C  
-ATOM    382  C   TYR A  52     -30.009  -8.646   5.941  1.00 45.70           C  
-ATOM    383  O   TYR A  52     -31.155  -9.069   6.108  1.00 49.13           O  
-ATOM    384  CB  TYR A  52     -29.270  -6.670   7.288  1.00 30.99           C  
-ATOM    385  CG  TYR A  52     -30.672  -6.090   7.170  1.00 39.18           C  
-ATOM    386  CD1 TYR A  52     -31.580  -6.176   8.230  1.00 44.93           C  
-ATOM    387  CD2 TYR A  52     -31.084  -5.425   6.012  1.00 40.25           C  
-ATOM    388  CE1 TYR A  52     -32.869  -5.626   8.133  1.00 42.39           C  
-ATOM    389  CE2 TYR A  52     -32.368  -4.868   5.911  1.00 44.65           C  
-ATOM    390  CZ  TYR A  52     -33.255  -4.974   6.974  1.00 44.08           C  
-ATOM    391  OH  TYR A  52     -34.522  -4.431   6.888  1.00 45.45           O  
-ATOM    392  N   LEU A  53     -29.441  -8.555   4.739  1.00 44.02           N  
-ATOM    393  CA  LEU A  53     -30.143  -8.966   3.523  1.00 40.75           C  
-ATOM    394  C   LEU A  53     -30.289 -10.486   3.441  1.00 43.67           C  
-ATOM    395  O   LEU A  53     -31.274 -10.987   2.888  1.00 36.95           O  
-ATOM    396  CB  LEU A  53     -29.408  -8.464   2.280  1.00 43.78           C  
-ATOM    397  CG  LEU A  53     -29.403  -6.970   1.966  1.00 32.27           C  
-ATOM    398  CD1 LEU A  53     -28.437  -6.670   0.839  1.00 37.60           C  
-ATOM    399  CD2 LEU A  53     -30.790  -6.506   1.606  1.00 33.95           C  
-ATOM    400  N   THR A  54     -29.297 -11.207   3.973  1.00 37.65           N  
-ATOM    401  CA  THR A  54     -29.319 -12.674   4.008  1.00 38.84           C  
-ATOM    402  C   THR A  54     -29.968 -13.257   5.277  1.00 40.92           C  
-ATOM    403  O   THR A  54     -29.813 -14.444   5.568  1.00 36.66           O  
-ATOM    404  CB  THR A  54     -27.894 -13.270   3.846  1.00 41.57           C  
-ATOM    405  OG1 THR A  54     -27.144 -13.093   5.056  1.00 48.25           O  
-ATOM    406  CG2 THR A  54     -27.161 -12.594   2.715  1.00 40.67           C  
-ATOM    407  N   ARG A  55     -30.664 -12.408   6.033  1.00 32.98           N  
-ATOM    408  CA  ARG A  55     -31.454 -12.852   7.173  1.00 38.78           C  
-ATOM    409  C   ARG A  55     -30.671 -13.534   8.309  1.00 38.81           C  
-ATOM    410  O   ARG A  55     -31.217 -14.390   9.027  1.00 33.70           O  
-ATOM    411  CB  ARG A  55     -32.573 -13.794   6.698  1.00 40.29           C  
-ATOM    412  CG  ARG A  55     -33.690 -13.157   5.865  1.00 38.44           C  
-ATOM    413  CD  ARG A  55     -34.538 -14.272   5.267  1.00 44.20           C  
-ATOM    414  NE  ARG A  55     -35.240 -13.907   4.032  1.00 51.41           N  
-ATOM    415  CZ  ARG A  55     -36.216 -13.007   3.972  1.00 52.92           C  
-ATOM    416  NH1 ARG A  55     -36.814 -12.742   2.817  1.00 34.87           N  
-ATOM    417  NH2 ARG A  55     -36.576 -12.356   5.072  1.00 50.62           N  
-ATOM    418  N   LYS A  56     -29.406 -13.174   8.486  1.00 41.22           N  
-ATOM    419  CA  LYS A  56     -28.639 -13.741   9.600  1.00 45.38           C  
-ATOM    420  C   LYS A  56     -28.293 -12.692  10.687  1.00 45.57           C  
-ATOM    421  O   LYS A  56     -27.367 -12.858  11.487  1.00 42.34           O  
-ATOM    422  CB  LYS A  56     -27.409 -14.489   9.084  1.00 34.62           C  
-ATOM    423  CG  LYS A  56     -26.449 -13.621   8.313  1.00 49.45           C  
-ATOM    424  CD  LYS A  56     -25.232 -14.418   7.842  1.00 60.73           C  
-ATOM    425  CE  LYS A  56     -25.589 -15.387   6.728  1.00 44.99           C  
-ATOM    426  NZ  LYS A  56     -24.406 -15.667   5.873  1.00 53.69           N  
-ATOM    427  N   LYS A  57     -29.089 -11.630  10.701  1.00 34.29           N  
-ATOM    428  CA  LYS A  57     -28.997 -10.567  11.670  1.00 36.94           C  
-ATOM    429  C   LYS A  57     -30.107  -9.579  11.363  1.00 39.36           C  
-ATOM    430  O   LYS A  57     -30.457  -9.383  10.201  1.00 34.75           O  
-ATOM    431  CB  LYS A  57     -27.636  -9.880  11.600  1.00 42.78           C  
-ATOM    432  CG  LYS A  57     -26.633 -10.313  12.660  1.00 43.52           C  
-ATOM    433  CD  LYS A  57     -25.301  -9.628  12.445  1.00 51.24           C  
-ATOM    434  CE  LYS A  57     -24.208 -10.284  13.267  1.00 63.61           C  
-ATOM    435  NZ  LYS A  57     -24.102 -11.744  12.987  1.00 51.20           N  
-ATOM    436  N   THR A  58     -30.693  -8.984  12.399  1.00 48.10           N  
-ATOM    437  CA  THR A  58     -31.607  -7.867  12.177  1.00 47.72           C  
-ATOM    438  C   THR A  58     -31.079  -6.614  12.852  1.00 41.01           C  
-ATOM    439  O   THR A  58     -30.154  -6.664  13.667  1.00 30.55           O  
-ATOM    440  CB  THR A  58     -33.071  -8.156  12.613  1.00 45.10           C  
-ATOM    441  OG1 THR A  58     -33.089  -9.120  13.671  1.00 45.57           O  
-ATOM    442  CG2 THR A  58     -33.868  -8.701  11.455  1.00 48.95           C  
-ATOM    443  N   TYR A  59     -31.669  -5.489  12.486  1.00 24.89           N  
-ATOM    444  CA  TYR A  59     -31.275  -4.215  13.029  1.00 29.53           C  
-ATOM    445  C   TYR A  59     -32.512  -3.342  13.075  1.00 41.44           C  
-ATOM    446  O   TYR A  59     -33.509  -3.669  12.434  1.00 44.84           O  
-ATOM    447  CB  TYR A  59     -30.244  -3.571  12.109  1.00 33.40           C  
-ATOM    448  CG  TYR A  59     -28.914  -4.298  12.024  1.00 40.38           C  
-ATOM    449  CD1 TYR A  59     -28.671  -5.266  11.042  1.00 29.97           C  
-ATOM    450  CD2 TYR A  59     -27.889  -3.988  12.904  1.00 41.73           C  
-ATOM    451  CE1 TYR A  59     -27.443  -5.917  10.957  1.00 30.27           C  
-ATOM    452  CE2 TYR A  59     -26.651  -4.626  12.827  1.00 44.12           C  
-ATOM    453  CZ  TYR A  59     -26.425  -5.595  11.857  1.00 47.53           C  
-ATOM    454  OH  TYR A  59     -25.184  -6.231  11.809  1.00 40.03           O  
-ATOM    455  N   ASN A  60     -32.457  -2.248  13.835  1.00 41.81           N  
-ATOM    456  CA  ASN A  60     -33.440  -1.170  13.711  1.00 43.28           C  
-ATOM    457  C   ASN A  60     -33.611  -0.737  12.283  1.00 52.21           C  
-ATOM    458  O   ASN A  60     -32.638  -0.693  11.529  1.00 51.76           O  
-ATOM    459  CB  ASN A  60     -32.941   0.075  14.415  1.00 48.73           C  
-ATOM    460  CG  ASN A  60     -33.690   0.369  15.665  1.00 57.20           C  
-ATOM    461  OD1 ASN A  60     -33.994  -0.528  16.437  1.00 62.70           O  
-ATOM    462  ND2 ASN A  60     -33.993   1.636  15.889  1.00 58.21           N  
-ATOM    463  N   ASP A  61     -34.827  -0.334  11.936  1.00 51.11           N  
-ATOM    464  CA  ASP A  61     -35.049   0.312  10.657  1.00 55.99           C  
-ATOM    465  C   ASP A  61     -34.106   1.507  10.622  1.00 55.08           C  
-ATOM    466  O   ASP A  61     -33.533   1.842   9.583  1.00 55.32           O  
-ATOM    467  CB  ASP A  61     -36.516   0.724  10.495  1.00 53.00           C  
-ATOM    468  CG  ASP A  61     -37.432  -0.474  10.246  1.00 74.57           C  
-ATOM    469  OD1 ASP A  61     -37.096  -1.310   9.379  1.00 80.54           O  
-ATOM    470  OD2 ASP A  61     -38.483  -0.584  10.917  1.00 76.75           O  
-ATOM    471  N   HIS A  62     -33.903   2.105  11.787  1.00 50.94           N  
-ATOM    472  CA  HIS A  62     -32.994   3.237  11.928  1.00 55.94           C  
-ATOM    473  C   HIS A  62     -31.553   2.889  11.619  1.00 50.41           C  
-ATOM    474  O   HIS A  62     -30.793   3.720  11.129  1.00 50.07           O  
-ATOM    475  CB  HIS A  62     -33.083   3.805  13.341  1.00 47.08           C  
-ATOM    476  CG  HIS A  62     -34.217   4.764  13.521  1.00 69.00           C  
-ATOM    477  ND1 HIS A  62     -34.093   6.116  13.276  1.00 59.32           N  
-ATOM    478  CD2 HIS A  62     -35.507   4.565  13.888  1.00 70.92           C  
-ATOM    479  CE1 HIS A  62     -35.250   6.712  13.503  1.00 45.37           C  
-ATOM    480  NE2 HIS A  62     -36.126   5.794  13.875  1.00 64.36           N  
-ATOM    481  N   ILE A  63     -31.169   1.659  11.908  1.00 45.67           N  
-ATOM    482  CA  ILE A  63     -29.770   1.308  11.785  1.00 41.81           C  
-ATOM    483  C   ILE A  63     -29.479   0.945  10.351  1.00 45.53           C  
-ATOM    484  O   ILE A  63     -28.403   1.234   9.846  1.00 48.92           O  
-ATOM    485  CB  ILE A  63     -29.365   0.154  12.743  1.00 53.60           C  
-ATOM    486  CG1 ILE A  63     -29.256   0.648  14.201  1.00 49.56           C  
-ATOM    487  CG2 ILE A  63     -28.021  -0.425  12.343  1.00 34.88           C  
-ATOM    488  CD1 ILE A  63     -30.196   1.808  14.583  1.00 51.13           C  
-ATOM    489  N   VAL A  64     -30.447   0.329   9.681  1.00 42.82           N  
-ATOM    490  CA  VAL A  64     -30.182  -0.122   8.332  1.00 36.20           C  
-ATOM    491  C   VAL A  64     -30.163   1.088   7.415  1.00 41.45           C  
-ATOM    492  O   VAL A  64     -29.301   1.190   6.552  1.00 41.98           O  
-ATOM    493  CB  VAL A  64     -31.155  -1.245   7.835  1.00 42.55           C  
-ATOM    494  CG1 VAL A  64     -31.584  -2.135   8.979  1.00 35.25           C  
-ATOM    495  CG2 VAL A  64     -32.370  -0.671   7.124  1.00 54.16           C  
-ATOM    496  N   ASN A  65     -31.083   2.026   7.623  1.00 47.19           N  
-ATOM    497  CA  ASN A  65     -31.122   3.213   6.777  1.00 44.57           C  
-ATOM    498  C   ASN A  65     -29.764   3.884   6.734  1.00 47.41           C  
-ATOM    499  O   ASN A  65     -29.318   4.319   5.664  1.00 41.69           O  
-ATOM    500  CB  ASN A  65     -32.182   4.215   7.237  1.00 42.74           C  
-ATOM    501  CG  ASN A  65     -33.588   3.804   6.843  1.00 57.51           C  
-ATOM    502  OD1 ASN A  65     -33.849   2.640   6.544  1.00 61.27           O  
-ATOM    503  ND2 ASN A  65     -34.506   4.759   6.854  1.00 60.13           N  
-ATOM    504  N   LEU A  66     -29.098   3.959   7.886  1.00 35.44           N  
-ATOM    505  CA  LEU A  66     -27.827   4.668   7.925  1.00 37.89           C  
-ATOM    506  C   LEU A  66     -26.615   3.803   7.584  1.00 33.59           C  
-ATOM    507  O   LEU A  66     -25.570   4.306   7.209  1.00 35.69           O  
-ATOM    508  CB  LEU A  66     -27.633   5.448   9.231  1.00 43.82           C  
-ATOM    509  CG  LEU A  66     -27.217   4.807  10.559  1.00 58.81           C  
-ATOM    510  CD1 LEU A  66     -26.680   3.398  10.407  1.00 56.51           C  
-ATOM    511  CD2 LEU A  66     -26.192   5.674  11.276  1.00 36.18           C  
-ATOM    512  N   LEU A  67     -26.748   2.499   7.702  1.00 32.16           N  
-ATOM    513  CA  LEU A  67     -25.688   1.633   7.223  1.00 35.32           C  
-ATOM    514  C   LEU A  67     -25.492   1.811   5.712  1.00 35.13           C  
-ATOM    515  O   LEU A  67     -24.363   1.906   5.230  1.00 28.85           O  
-ATOM    516  CB  LEU A  67     -26.035   0.178   7.514  1.00 39.66           C  
-ATOM    517  CG  LEU A  67     -25.745  -0.287   8.931  1.00 38.93           C  
-ATOM    518  CD1 LEU A  67     -25.990  -1.780   9.034  1.00 33.38           C  
-ATOM    519  CD2 LEU A  67     -24.307   0.049   9.263  1.00 36.67           C  
-ATOM    520  N   PHE A  68     -26.610   1.837   4.983  1.00 32.05           N  
-ATOM    521  CA  PHE A  68     -26.624   1.995   3.542  1.00 25.37           C  
-ATOM    522  C   PHE A  68     -26.057   3.338   3.129  1.00 27.56           C  
-ATOM    523  O   PHE A  68     -25.252   3.434   2.206  1.00 30.24           O  
-ATOM    524  CB  PHE A  68     -28.050   1.872   3.030  1.00 31.95           C  
-ATOM    525  CG  PHE A  68     -28.468   0.466   2.743  1.00 32.09           C  
-ATOM    526  CD1 PHE A  68     -27.932  -0.222   1.671  1.00 36.59           C  
-ATOM    527  CD2 PHE A  68     -29.407  -0.158   3.529  1.00 27.54           C  
-ATOM    528  CE1 PHE A  68     -28.315  -1.503   1.395  1.00 32.09           C  
-ATOM    529  CE2 PHE A  68     -29.799  -1.437   3.261  1.00 29.00           C  
-ATOM    530  CZ  PHE A  68     -29.252  -2.113   2.194  1.00 38.20           C  
-ATOM    531  N   CYS A  69     -26.497   4.376   3.818  1.00 31.88           N  
-ATOM    532  CA  CYS A  69     -26.000   5.712   3.578  1.00 37.91           C  
-ATOM    533  C   CYS A  69     -24.485   5.762   3.810  1.00 37.31           C  
-ATOM    534  O   CYS A  69     -23.699   6.082   2.894  1.00 32.15           O  
-ATOM    535  CB  CYS A  69     -26.714   6.700   4.489  1.00 31.31           C  
-ATOM    536  SG  CYS A  69     -26.573   8.388   3.933  1.00 44.50           S  
-ATOM    537  N   ALA A  70     -24.071   5.431   5.026  1.00 26.11           N  
-ATOM    538  CA  ALA A  70     -22.646   5.420   5.340  1.00 32.86           C  
-ATOM    539  C   ALA A  70     -21.855   4.568   4.347  1.00 35.81           C  
-ATOM    540  O   ALA A  70     -20.729   4.922   3.982  1.00 33.24           O  
-ATOM    541  CB  ALA A  70     -22.416   4.944   6.753  1.00 26.40           C  
-ATOM    542  N   ASN A  71     -22.456   3.460   3.909  1.00 30.73           N  
-ATOM    543  CA  ASN A  71     -21.870   2.618   2.882  1.00 28.66           C  
-ATOM    544  C   ASN A  71     -21.561   3.415   1.605  1.00 31.55           C  
-ATOM    545  O   ASN A  71     -20.559   3.177   0.924  1.00 28.56           O  
-ATOM    546  CB  ASN A  71     -22.779   1.426   2.594  1.00 20.93           C  
-ATOM    547  CG  ASN A  71     -22.132   0.410   1.675  1.00 33.31           C  
-ATOM    548  OD1 ASN A  71     -22.587   0.211   0.551  1.00 30.37           O  
-ATOM    549  ND2 ASN A  71     -21.053  -0.228   2.139  1.00 27.26           N  
-ATOM    550  N   ARG A  72     -22.408   4.381   1.286  1.00 27.95           N  
-ATOM    551  CA  ARG A  72     -22.141   5.204   0.114  1.00 28.88           C  
-ATOM    552  C   ARG A  72     -21.026   6.220   0.399  1.00 35.91           C  
-ATOM    553  O   ARG A  72     -20.061   6.325  -0.369  1.00 35.58           O  
-ATOM    554  CB  ARG A  72     -23.425   5.882  -0.416  1.00 32.37           C  
-ATOM    555  CG  ARG A  72     -24.314   4.976  -1.303  1.00 29.79           C  
-ATOM    556  CD  ARG A  72     -25.650   5.647  -1.699  1.00 34.29           C  
-ATOM    557  NE  ARG A  72     -26.579   5.756  -0.576  1.00 22.27           N  
-ATOM    558  CZ  ARG A  72     -27.426   4.796  -0.207  1.00 30.93           C  
-ATOM    559  NH1 ARG A  72     -27.481   3.651  -0.884  1.00 29.72           N  
-ATOM    560  NH2 ARG A  72     -28.220   4.981   0.843  1.00 31.50           N  
-ATOM    561  N   TRP A  73     -21.139   6.945   1.508  1.00 33.71           N  
-ATOM    562  CA  TRP A  73     -20.156   7.967   1.832  1.00 31.55           C  
-ATOM    563  C   TRP A  73     -18.691   7.510   1.836  1.00 34.51           C  
-ATOM    564  O   TRP A  73     -17.814   8.301   1.482  1.00 36.88           O  
-ATOM    565  CB  TRP A  73     -20.518   8.647   3.144  1.00 36.42           C  
-ATOM    566  CG  TRP A  73     -21.665   9.545   2.968  1.00 34.97           C  
-ATOM    567  CD1 TRP A  73     -22.977   9.240   3.155  1.00 38.28           C  
-ATOM    568  CD2 TRP A  73     -21.627  10.900   2.518  1.00 35.39           C  
-ATOM    569  NE1 TRP A  73     -23.764  10.330   2.864  1.00 35.01           N  
-ATOM    570  CE2 TRP A  73     -22.952  11.365   2.468  1.00 40.66           C  
-ATOM    571  CE3 TRP A  73     -20.596  11.772   2.154  1.00 30.44           C  
-ATOM    572  CZ2 TRP A  73     -23.276  12.657   2.072  1.00 38.44           C  
-ATOM    573  CZ3 TRP A  73     -20.919  13.051   1.766  1.00 32.27           C  
-ATOM    574  CH2 TRP A  73     -22.247  13.485   1.727  1.00 38.23           C  
-ATOM    575  N   GLU A  74     -18.411   6.264   2.227  1.00 29.89           N  
-ATOM    576  CA  GLU A  74     -17.036   5.754   2.116  1.00 33.63           C  
-ATOM    577  C   GLU A  74     -16.459   6.082   0.752  1.00 38.29           C  
-ATOM    578  O   GLU A  74     -15.270   6.353   0.608  1.00 44.29           O  
-ATOM    579  CB  GLU A  74     -16.960   4.240   2.328  1.00 31.76           C  
-ATOM    580  CG  GLU A  74     -17.528   3.753   3.660  1.00 56.33           C  
-ATOM    581  CD  GLU A  74     -17.199   2.290   3.958  1.00 62.85           C  
-ATOM    582  OE1 GLU A  74     -16.211   1.775   3.388  1.00 68.56           O  
-ATOM    583  OE2 GLU A  74     -17.915   1.660   4.773  1.00 48.24           O  
-ATOM    584  N   PHE A  75     -17.328   6.075  -0.251  1.00 38.68           N  
-ATOM    585  CA  PHE A  75     -16.889   6.148  -1.631  1.00 36.29           C  
-ATOM    586  C   PHE A  75     -17.116   7.499  -2.305  1.00 32.16           C  
-ATOM    587  O   PHE A  75     -16.732   7.687  -3.460  1.00 38.71           O  
-ATOM    588  CB  PHE A  75     -17.566   5.046  -2.427  1.00 33.04           C  
-ATOM    589  CG  PHE A  75     -17.083   3.680  -2.085  1.00 27.32           C  
-ATOM    590  CD1 PHE A  75     -17.693   2.951  -1.087  1.00 29.67           C  
-ATOM    591  CD2 PHE A  75     -16.024   3.119  -2.771  1.00 28.84           C  
-ATOM    592  CE1 PHE A  75     -17.258   1.681  -0.778  1.00 31.60           C  
-ATOM    593  CE2 PHE A  75     -15.582   1.851  -2.474  1.00 31.51           C  
-ATOM    594  CZ  PHE A  75     -16.196   1.128  -1.472  1.00 29.46           C  
-ATOM    595  N   ALA A  76     -17.730   8.434  -1.597  1.00 25.39           N  
-ATOM    596  CA  ALA A  76     -17.941   9.765  -2.149  1.00 31.79           C  
-ATOM    597  C   ALA A  76     -16.616  10.467  -2.557  1.00 41.29           C  
-ATOM    598  O   ALA A  76     -16.547  11.158  -3.585  1.00 33.51           O  
-ATOM    599  CB  ALA A  76     -18.741  10.612  -1.174  1.00 28.16           C  
-ATOM    600  N   SER A  77     -15.563  10.280  -1.764  1.00 40.53           N  
-ATOM    601  CA  SER A  77     -14.256  10.782  -2.153  1.00 40.94           C  
-ATOM    602  C   SER A  77     -13.796  10.164  -3.468  1.00 38.89           C  
-ATOM    603  O   SER A  77     -13.436  10.868  -4.411  1.00 29.08           O  
-ATOM    604  CB  SER A  77     -13.236  10.484  -1.067  1.00 42.93           C  
-ATOM    605  OG  SER A  77     -13.019  11.640  -0.292  1.00 33.78           O  
-ATOM    606  N   PHE A  78     -13.804   8.839  -3.508  1.00 34.89           N  
-ATOM    607  CA  PHE A  78     -13.420   8.079  -4.683  1.00 32.97           C  
-ATOM    608  C   PHE A  78     -14.188   8.478  -5.942  1.00 33.99           C  
-ATOM    609  O   PHE A  78     -13.607   8.651  -7.018  1.00 37.23           O  
-ATOM    610  CB  PHE A  78     -13.620   6.605  -4.408  1.00 24.59           C  
-ATOM    611  CG  PHE A  78     -13.236   5.720  -5.539  1.00 31.49           C  
-ATOM    612  CD1 PHE A  78     -11.914   5.360  -5.728  1.00 36.17           C  
-ATOM    613  CD2 PHE A  78     -14.200   5.218  -6.402  1.00 35.04           C  
-ATOM    614  CE1 PHE A  78     -11.544   4.521  -6.769  1.00 40.01           C  
-ATOM    615  CE2 PHE A  78     -13.844   4.379  -7.449  1.00 39.22           C  
-ATOM    616  CZ  PHE A  78     -12.504   4.030  -7.636  1.00 41.58           C  
-ATOM    617  N   ILE A  79     -15.495   8.620  -5.813  1.00 27.65           N  
-ATOM    618  CA  ILE A  79     -16.300   9.017  -6.954  1.00 36.33           C  
-ATOM    619  C   ILE A  79     -15.812  10.351  -7.524  1.00 41.40           C  
-ATOM    620  O   ILE A  79     -15.357  10.438  -8.672  1.00 40.14           O  
-ATOM    621  CB  ILE A  79     -17.772   9.119  -6.566  1.00 32.60           C  
-ATOM    622  CG1 ILE A  79     -18.294   7.741  -6.175  1.00 31.16           C  
-ATOM    623  CG2 ILE A  79     -18.586   9.666  -7.726  1.00 26.64           C  
-ATOM    624  CD1 ILE A  79     -19.556   7.792  -5.366  1.00 29.33           C  
-ATOM    625  N   GLN A  80     -15.917  11.387  -6.706  1.00 38.06           N  
-ATOM    626  CA  GLN A  80     -15.365  12.694  -7.014  1.00 37.84           C  
-ATOM    627  C   GLN A  80     -13.980  12.656  -7.700  1.00 43.19           C  
-ATOM    628  O   GLN A  80     -13.803  13.251  -8.762  1.00 39.08           O  
-ATOM    629  CB  GLN A  80     -15.286  13.499  -5.720  1.00 43.56           C  
-ATOM    630  CG  GLN A  80     -14.618  14.834  -5.875  1.00 57.26           C  
-ATOM    631  CD  GLN A  80     -15.447  15.757  -6.724  1.00 65.37           C  
-ATOM    632  OE1 GLN A  80     -16.667  15.592  -6.817  1.00 66.31           O  
-ATOM    633  NE2 GLN A  80     -14.797  16.734  -7.358  1.00 47.16           N  
-ATOM    634  N   GLU A  81     -13.005  11.974  -7.091  1.00 40.88           N  
-ATOM    635  CA  GLU A  81     -11.654  11.880  -7.660  1.00 44.79           C  
-ATOM    636  C   GLU A  81     -11.634  11.308  -9.095  1.00 47.20           C  
-ATOM    637  O   GLU A  81     -10.980  11.853  -9.996  1.00 41.91           O  
-ATOM    638  CB  GLU A  81     -10.722  11.070  -6.750  1.00 39.67           C  
-ATOM    639  CG  GLU A  81     -10.233  11.842  -5.520  1.00 63.19           C  
-ATOM    640  CD  GLU A  81     -10.167  10.996  -4.241  1.00 83.95           C  
-ATOM    641  OE1 GLU A  81      -9.999  11.596  -3.155  1.00 82.31           O  
-ATOM    642  OE2 GLU A  81     -10.291   9.747  -4.305  1.00 73.85           O  
-ATOM    643  N   GLN A  82     -12.355  10.218  -9.311  1.00 36.77           N  
-ATOM    644  CA  GLN A  82     -12.375   9.585 -10.615  1.00 34.81           C  
-ATOM    645  C   GLN A  82     -12.945  10.502 -11.702  1.00 39.85           C  
-ATOM    646  O   GLN A  82     -12.369  10.662 -12.789  1.00 32.40           O  
-ATOM    647  CB  GLN A  82     -13.189   8.300 -10.529  1.00 33.61           C  
-ATOM    648  CG  GLN A  82     -12.590   7.292  -9.566  1.00 43.36           C  
-ATOM    649  CD  GLN A  82     -11.208   6.823  -9.992  1.00 41.73           C  
-ATOM    650  OE1 GLN A  82     -11.076   6.059 -10.953  1.00 35.61           O  
-ATOM    651  NE2 GLN A  82     -10.173   7.271  -9.274  1.00 30.59           N  
-ATOM    652  N   LEU A  83     -14.095  11.092 -11.408  1.00 38.02           N  
-ATOM    653  CA  LEU A  83     -14.739  11.968 -12.360  1.00 26.76           C  
-ATOM    654  C   LEU A  83     -13.786  13.086 -12.746  1.00 35.21           C  
-ATOM    655  O   LEU A  83     -13.568  13.340 -13.920  1.00 39.33           O  
-ATOM    656  CB  LEU A  83     -16.026  12.518 -11.773  1.00 31.18           C  
-ATOM    657  CG  LEU A  83     -17.094  11.452 -11.515  1.00 36.15           C  
-ATOM    658  CD1 LEU A  83     -18.381  12.070 -10.964  1.00 33.50           C  
-ATOM    659  CD2 LEU A  83     -17.386  10.656 -12.770  1.00 28.31           C  
-ATOM    660  N   GLU A  84     -13.200  13.753 -11.763  1.00 41.42           N  
-ATOM    661  CA  GLU A  84     -12.214  14.784 -12.068  1.00 43.86           C  
-ATOM    662  C   GLU A  84     -11.060  14.250 -12.927  1.00 43.09           C  
-ATOM    663  O   GLU A  84     -10.611  14.935 -13.854  1.00 41.16           O  
-ATOM    664  CB  GLU A  84     -11.688  15.429 -10.787  1.00 49.31           C  
-ATOM    665  CG  GLU A  84     -12.592  16.511 -10.233  1.00 45.57           C  
-ATOM    666  CD  GLU A  84     -12.183  16.947  -8.839  1.00 73.05           C  
-ATOM    667  OE1 GLU A  84     -11.397  16.220  -8.192  1.00 72.31           O  
-ATOM    668  OE2 GLU A  84     -12.651  18.015  -8.383  1.00 81.94           O  
-ATOM    669  N   GLN A  85     -10.595  13.033 -12.624  1.00 40.63           N  
-ATOM    670  CA  GLN A  85      -9.538  12.375 -13.402  1.00 36.07           C  
-ATOM    671  C   GLN A  85     -10.019  11.913 -14.776  1.00 35.32           C  
-ATOM    672  O   GLN A  85      -9.309  11.196 -15.485  1.00 42.52           O  
-ATOM    673  CB  GLN A  85      -8.952  11.177 -12.639  1.00 47.38           C  
-ATOM    674  CG  GLN A  85      -7.639  11.458 -11.907  1.00 65.60           C  
-ATOM    675  CD  GLN A  85      -7.066  10.221 -11.224  1.00 88.91           C  
-ATOM    676  OE1 GLN A  85      -7.809   9.386 -10.704  1.00 84.93           O  
-ATOM    677  NE2 GLN A  85      -5.739  10.103 -11.217  1.00105.87           N  
-ATOM    678  N   GLY A  86     -11.229  12.308 -15.145  1.00 31.75           N  
-ATOM    679  CA  GLY A  86     -11.735  12.009 -16.467  1.00 26.69           C  
-ATOM    680  C   GLY A  86     -12.330  10.627 -16.654  1.00 29.71           C  
-ATOM    681  O   GLY A  86     -12.723  10.277 -17.764  1.00 30.46           O  
-ATOM    682  N   ILE A  87     -12.407   9.836 -15.583  1.00 33.94           N  
-ATOM    683  CA  ILE A  87     -13.063   8.524 -15.658  1.00 30.65           C  
-ATOM    684  C   ILE A  87     -14.575   8.636 -15.471  1.00 28.96           C  
-ATOM    685  O   ILE A  87     -15.053   9.315 -14.568  1.00 28.40           O  
-ATOM    686  CB  ILE A  87     -12.526   7.522 -14.619  1.00 28.70           C  
-ATOM    687  CG1 ILE A  87     -11.111   7.056 -14.974  1.00 29.11           C  
-ATOM    688  CG2 ILE A  87     -13.434   6.298 -14.564  1.00 24.94           C  
-ATOM    689  CD1 ILE A  87     -10.298   8.025 -15.791  1.00 36.05           C  
-ATOM    690  N   THR A  88     -15.326   7.964 -16.334  1.00 34.47           N  
-ATOM    691  CA  THR A  88     -16.775   7.940 -16.227  1.00 32.45           C  
-ATOM    692  C   THR A  88     -17.207   6.827 -15.299  1.00 27.47           C  
-ATOM    693  O   THR A  88     -16.636   5.736 -15.318  1.00 29.08           O  
-ATOM    694  CB  THR A  88     -17.426   7.785 -17.623  1.00 36.25           C  
-ATOM    695  OG1 THR A  88     -17.517   9.079 -18.234  1.00 25.62           O  
-ATOM    696  CG2 THR A  88     -18.828   7.136 -17.547  1.00 25.89           C  
-ATOM    697  N   LEU A  89     -18.210   7.112 -14.478  1.00 30.18           N  
-ATOM    698  CA  LEU A  89     -18.670   6.156 -13.470  1.00 33.83           C  
-ATOM    699  C   LEU A  89     -19.995   5.526 -13.850  1.00 26.80           C  
-ATOM    700  O   LEU A  89     -20.960   6.230 -14.166  1.00 25.01           O  
-ATOM    701  CB  LEU A  89     -18.768   6.815 -12.082  1.00 22.25           C  
-ATOM    702  CG  LEU A  89     -17.413   6.801 -11.419  1.00 22.10           C  
-ATOM    703  CD1 LEU A  89     -17.503   7.332 -10.036  1.00 47.30           C  
-ATOM    704  CD2 LEU A  89     -16.954   5.371 -11.373  1.00 37.62           C  
-ATOM    705  N   ILE A  90     -20.017   4.197 -13.821  1.00 23.60           N  
-ATOM    706  CA  ILE A  90     -21.236   3.420 -14.014  1.00 24.53           C  
-ATOM    707  C   ILE A  90     -21.610   2.729 -12.703  1.00 26.71           C  
-ATOM    708  O   ILE A  90     -20.916   1.836 -12.222  1.00 33.02           O  
-ATOM    709  CB  ILE A  90     -21.075   2.399 -15.157  1.00 27.16           C  
-ATOM    710  CG1 ILE A  90     -20.749   3.135 -16.464  1.00 28.41           C  
-ATOM    711  CG2 ILE A  90     -22.305   1.475 -15.264  1.00 21.91           C  
-ATOM    712  CD1 ILE A  90     -21.747   4.217 -16.834  1.00 32.43           C  
-ATOM    713  N   VAL A  91     -22.711   3.166 -12.122  1.00 23.56           N  
-ATOM    714  CA  VAL A  91     -23.032   2.818 -10.752  1.00 21.95           C  
-ATOM    715  C   VAL A  91     -24.342   2.080 -10.620  1.00 23.75           C  
-ATOM    716  O   VAL A  91     -25.393   2.618 -10.942  1.00 29.81           O  
-ATOM    717  CB  VAL A  91     -23.165   4.075  -9.919  1.00 25.15           C  
-ATOM    718  CG1 VAL A  91     -23.416   3.705  -8.484  1.00 23.76           C  
-ATOM    719  CG2 VAL A  91     -21.923   4.937 -10.067  1.00 23.26           C  
-ATOM    720  N   ASP A  92     -24.267   0.848 -10.132  1.00 29.15           N  
-ATOM    721  CA  ASP A  92     -25.434   0.020  -9.843  1.00 29.78           C  
-ATOM    722  C   ASP A  92     -25.995   0.474  -8.497  1.00 24.39           C  
-ATOM    723  O   ASP A  92     -25.310   0.359  -7.484  1.00 27.80           O  
-ATOM    724  CB  ASP A  92     -24.978  -1.440  -9.777  1.00 37.26           C  
-ATOM    725  CG  ASP A  92     -26.093  -2.426 -10.037  1.00 45.50           C  
-ATOM    726  OD1 ASP A  92     -27.276  -2.025 -10.037  1.00 42.02           O  
-ATOM    727  OD2 ASP A  92     -25.779  -3.617 -10.237  1.00 47.76           O  
-ATOM    728  N   ARG A  93     -27.215   1.014  -8.494  1.00 22.64           N  
-ATOM    729  CA  ARG A  93     -27.854   1.602  -7.287  1.00 29.67           C  
-ATOM    730  C   ARG A  93     -27.106   2.771  -6.653  1.00 20.90           C  
-ATOM    731  O   ARG A  93     -25.896   2.821  -6.678  1.00 26.34           O  
-ATOM    732  CB  ARG A  93     -28.142   0.543  -6.203  1.00 28.88           C  
-ATOM    733  CG  ARG A  93     -29.124  -0.531  -6.621  1.00 23.72           C  
-ATOM    734  CD  ARG A  93     -29.539  -1.373  -5.467  1.00 21.67           C  
-ATOM    735  NE  ARG A  93     -30.483  -2.391  -5.876  1.00 30.56           N  
-ATOM    736  CZ  ARG A  93     -31.756  -2.152  -6.195  1.00 36.81           C  
-ATOM    737  NH1 ARG A  93     -32.257  -0.916  -6.174  1.00 26.85           N  
-ATOM    738  NH2 ARG A  93     -32.524  -3.164  -6.563  1.00 40.62           N  
-ATOM    739  N   TYR A  94     -27.845   3.681  -6.046  1.00 27.75           N  
-ATOM    740  CA  TYR A  94     -27.258   4.880  -5.454  1.00 32.68           C  
-ATOM    741  C   TYR A  94     -28.201   5.527  -4.415  1.00 31.85           C  
-ATOM    742  O   TYR A  94     -29.081   4.877  -3.850  1.00 23.96           O  
-ATOM    743  CB  TYR A  94     -26.939   5.861  -6.590  1.00 34.79           C  
-ATOM    744  CG  TYR A  94     -25.899   6.943  -6.320  1.00 29.83           C  
-ATOM    745  CD1 TYR A  94     -24.647   6.626  -5.803  1.00 21.72           C  
-ATOM    746  CD2 TYR A  94     -26.159   8.284  -6.633  1.00 23.95           C  
-ATOM    747  CE1 TYR A  94     -23.691   7.612  -5.572  1.00 22.14           C  
-ATOM    748  CE2 TYR A  94     -25.202   9.276  -6.413  1.00 26.80           C  
-ATOM    749  CZ  TYR A  94     -23.962   8.934  -5.878  1.00 25.40           C  
-ATOM    750  OH  TYR A  94     -22.998   9.899  -5.643  1.00 16.71           O  
-ATOM    751  N   ALA A  95     -28.008   6.815  -4.176  1.00 28.96           N  
-ATOM    752  CA  ALA A  95     -28.879   7.583  -3.289  1.00 34.60           C  
-ATOM    753  C   ALA A  95     -30.336   7.168  -3.381  1.00 34.57           C  
-ATOM    754  O   ALA A  95     -30.992   6.993  -2.363  1.00 41.13           O  
-ATOM    755  CB  ALA A  95     -28.765   9.080  -3.568  1.00 33.37           C  
-ATOM    756  N   PHE A  96     -30.845   7.015  -4.600  1.00 37.50           N  
-ATOM    757  CA  PHE A  96     -32.273   6.752  -4.806  1.00 38.86           C  
-ATOM    758  C   PHE A  96     -32.692   5.375  -4.319  1.00 35.09           C  
-ATOM    759  O   PHE A  96     -33.767   5.217  -3.742  1.00 35.38           O  
-ATOM    760  CB  PHE A  96     -32.654   6.971  -6.264  1.00 29.26           C  
-ATOM    761  CG  PHE A  96     -31.939   8.126  -6.884  1.00 29.04           C  
-ATOM    762  CD1 PHE A  96     -32.480   9.408  -6.828  1.00 28.52           C  
-ATOM    763  CD2 PHE A  96     -30.705   7.941  -7.494  1.00 29.23           C  
-ATOM    764  CE1 PHE A  96     -31.811  10.499  -7.386  1.00 37.92           C  
-ATOM    765  CE2 PHE A  96     -30.025   9.019  -8.058  1.00 38.90           C  
-ATOM    766  CZ  PHE A  96     -30.580  10.307  -8.005  1.00 39.92           C  
-ATOM    767  N   SER A  97     -31.835   4.380  -4.520  1.00 36.57           N  
-ATOM    768  CA  SER A  97     -32.085   3.077  -3.917  1.00 35.96           C  
-ATOM    769  C   SER A  97     -32.332   3.269  -2.420  1.00 37.41           C  
-ATOM    770  O   SER A  97     -33.240   2.661  -1.852  1.00 36.14           O  
-ATOM    771  CB  SER A  97     -30.916   2.122  -4.167  1.00 27.94           C  
-ATOM    772  OG  SER A  97     -31.095   1.356  -5.343  1.00 27.06           O  
-ATOM    773  N   GLY A  98     -31.523   4.136  -1.804  1.00 31.49           N  
-ATOM    774  CA  GLY A  98     -31.643   4.471  -0.401  1.00 24.37           C  
-ATOM    775  C   GLY A  98     -32.996   5.041  -0.025  1.00 36.11           C  
-ATOM    776  O   GLY A  98     -33.739   4.432   0.741  1.00 40.56           O  
-ATOM    777  N   VAL A  99     -33.323   6.206  -0.578  1.00 37.82           N  
-ATOM    778  CA  VAL A  99     -34.554   6.902  -0.248  1.00 28.93           C  
-ATOM    779  C   VAL A  99     -35.802   6.091  -0.557  1.00 32.63           C  
-ATOM    780  O   VAL A  99     -36.726   6.060   0.235  1.00 42.33           O  
-ATOM    781  CB  VAL A  99     -34.645   8.231  -0.991  1.00 36.40           C  
-ATOM    782  CG1 VAL A  99     -35.855   9.011  -0.513  1.00 42.16           C  
-ATOM    783  CG2 VAL A  99     -33.378   9.038  -0.781  1.00 35.44           C  
-ATOM    784  N   ALA A 100     -35.838   5.440  -1.712  1.00 32.26           N  
-ATOM    785  CA  ALA A 100     -37.043   4.723  -2.128  1.00 38.35           C  
-ATOM    786  C   ALA A 100     -37.312   3.506  -1.243  1.00 41.48           C  
-ATOM    787  O   ALA A 100     -38.456   3.183  -0.909  1.00 39.58           O  
-ATOM    788  CB  ALA A 100     -36.942   4.307  -3.583  1.00 36.49           C  
-ATOM    789  N   TYR A 101     -36.243   2.825  -0.870  1.00 40.10           N  
-ATOM    790  CA  TYR A 101     -36.374   1.640  -0.055  1.00 32.62           C  
-ATOM    791  C   TYR A 101     -36.605   2.022   1.396  1.00 36.47           C  
-ATOM    792  O   TYR A 101     -37.405   1.388   2.075  1.00 41.69           O  
-ATOM    793  CB  TYR A 101     -35.150   0.747  -0.207  1.00 24.98           C  
-ATOM    794  CG  TYR A 101     -35.216  -0.180  -1.390  1.00 31.50           C  
-ATOM    795  CD1 TYR A 101     -34.963   0.282  -2.681  1.00 37.27           C  
-ATOM    796  CD2 TYR A 101     -35.522  -1.524  -1.220  1.00 35.27           C  
-ATOM    797  CE1 TYR A 101     -35.015  -0.578  -3.775  1.00 32.78           C  
-ATOM    798  CE2 TYR A 101     -35.576  -2.391  -2.297  1.00 38.45           C  
-ATOM    799  CZ  TYR A 101     -35.324  -1.921  -3.575  1.00 44.91           C  
-ATOM    800  OH  TYR A 101     -35.393  -2.796  -4.648  1.00 37.22           O  
-ATOM    801  N   ALA A 102     -35.910   3.054   1.872  1.00 31.66           N  
-ATOM    802  CA  ALA A 102     -36.127   3.547   3.233  1.00 38.05           C  
-ATOM    803  C   ALA A 102     -37.564   4.097   3.380  1.00 51.83           C  
-ATOM    804  O   ALA A 102     -38.258   3.798   4.370  1.00 45.22           O  
-ATOM    805  CB  ALA A 102     -35.090   4.603   3.609  1.00 26.26           C  
-ATOM    806  N   ALA A 103     -38.010   4.859   2.377  1.00 39.73           N  
-ATOM    807  CA  ALA A 103     -39.324   5.473   2.391  1.00 37.52           C  
-ATOM    808  C   ALA A 103     -40.446   4.446   2.254  1.00 42.56           C  
-ATOM    809  O   ALA A 103     -41.525   4.620   2.815  1.00 47.87           O  
-ATOM    810  CB  ALA A 103     -39.415   6.514   1.295  1.00 45.38           C  
-ATOM    811  N   ALA A 104     -40.190   3.384   1.501  1.00 37.15           N  
-ATOM    812  CA  ALA A 104     -41.161   2.312   1.333  1.00 36.99           C  
-ATOM    813  C   ALA A 104     -41.449   1.644   2.669  1.00 44.14           C  
-ATOM    814  O   ALA A 104     -42.548   1.122   2.885  1.00 37.59           O  
-ATOM    815  CB  ALA A 104     -40.634   1.282   0.360  1.00 36.28           C  
-ATOM    816  N   LYS A 105     -40.434   1.643   3.536  1.00 38.10           N  
-ATOM    817  CA  LYS A 105     -40.512   1.086   4.887  1.00 37.93           C  
-ATOM    818  C   LYS A 105     -41.058   2.087   5.909  1.00 49.19           C  
-ATOM    819  O   LYS A 105     -40.896   1.912   7.110  1.00 61.01           O  
-ATOM    820  CB  LYS A 105     -39.133   0.609   5.355  1.00 46.63           C  
-ATOM    821  CG  LYS A 105     -38.954  -0.906   5.393  1.00 54.60           C  
-ATOM    822  CD  LYS A 105     -37.571  -1.359   4.841  1.00 58.84           C  
-ATOM    823  CE  LYS A 105     -36.409  -1.307   5.861  1.00 56.64           C  
-ATOM    824  NZ  LYS A 105     -35.875   0.069   6.090  1.00 52.21           N  
-ATOM    825  N   GLY A 106     -41.691   3.146   5.434  1.00 44.56           N  
-ATOM    826  CA  GLY A 106     -42.314   4.083   6.334  1.00 33.75           C  
-ATOM    827  C   GLY A 106     -41.470   5.254   6.798  1.00 37.40           C  
-ATOM    828  O   GLY A 106     -41.901   6.044   7.640  1.00 43.78           O  
-ATOM    829  N   ALA A 107     -40.276   5.402   6.255  1.00 44.15           N  
-ATOM    830  CA  ALA A 107     -39.453   6.552   6.635  1.00 42.59           C  
-ATOM    831  C   ALA A 107     -39.845   7.807   5.858  1.00 48.77           C  
-ATOM    832  O   ALA A 107     -40.518   7.733   4.817  1.00 39.13           O  
-ATOM    833  CB  ALA A 107     -37.982   6.253   6.442  1.00 40.62           C  
-ATOM    834  N   SER A 108     -39.417   8.952   6.381  1.00 42.19           N  
-ATOM    835  CA  SER A 108     -39.698  10.236   5.765  1.00 38.17           C  
-ATOM    836  C   SER A 108     -38.817  10.418   4.568  1.00 39.67           C  
-ATOM    837  O   SER A 108     -37.595  10.365   4.683  1.00 34.67           O  
-ATOM    838  CB  SER A 108     -39.438  11.381   6.749  1.00 51.62           C  
-ATOM    839  OG  SER A 108     -39.215  12.617   6.079  1.00 39.35           O  
-ATOM    840  N   MET A 109     -39.456  10.664   3.426  1.00 52.49           N  
-ATOM    841  CA  MET A 109     -38.782  10.910   2.145  1.00 48.72           C  
-ATOM    842  C   MET A 109     -37.863  12.141   2.148  1.00 35.61           C  
-ATOM    843  O   MET A 109     -36.795  12.118   1.555  1.00 43.27           O  
-ATOM    844  CB  MET A 109     -39.828  11.013   1.021  1.00 54.00           C  
-ATOM    845  CG  MET A 109     -39.461  11.910  -0.176  1.00 54.23           C  
-ATOM    846  SD  MET A 109     -39.195  11.017  -1.719  1.00 59.81           S  
-ATOM    847  CE  MET A 109     -40.345   9.641  -1.576  1.00 52.14           C  
-ATOM    848  N   THR A 110     -38.277  13.213   2.807  1.00 41.04           N  
-ATOM    849  CA  THR A 110     -37.446  14.414   2.880  1.00 47.22           C  
-ATOM    850  C   THR A 110     -36.265  14.190   3.822  1.00 41.81           C  
-ATOM    851  O   THR A 110     -35.174  14.718   3.611  1.00 40.77           O  
-ATOM    852  CB  THR A 110     -38.259  15.630   3.357  1.00 35.01           C  
-ATOM    853  OG1 THR A 110     -38.878  15.310   4.601  1.00 49.77           O  
-ATOM    854  CG2 THR A 110     -39.359  15.962   2.364  1.00 37.06           C  
-ATOM    855  N   LEU A 111     -36.492  13.396   4.859  1.00 38.58           N  
-ATOM    856  CA  LEU A 111     -35.433  13.042   5.789  1.00 49.71           C  
-ATOM    857  C   LEU A 111     -34.409  12.054   5.170  1.00 48.01           C  
-ATOM    858  O   LEU A 111     -33.200  12.188   5.364  1.00 38.27           O  
-ATOM    859  CB  LEU A 111     -36.055  12.481   7.070  1.00 44.23           C  
-ATOM    860  CG  LEU A 111     -35.107  12.127   8.209  1.00 54.66           C  
-ATOM    861  CD1 LEU A 111     -34.390  13.385   8.741  1.00 45.49           C  
-ATOM    862  CD2 LEU A 111     -35.867  11.389   9.313  1.00 56.94           C  
-ATOM    863  N   SER A 112     -34.894  11.063   4.430  1.00 38.10           N  
-ATOM    864  CA  SER A 112     -33.998  10.128   3.781  1.00 35.58           C  
-ATOM    865  C   SER A 112     -33.088  10.930   2.871  1.00 38.53           C  
-ATOM    866  O   SER A 112     -31.896  10.659   2.750  1.00 37.67           O  
-ATOM    867  CB  SER A 112     -34.778   9.098   2.954  1.00 42.19           C  
-ATOM    868  OG  SER A 112     -35.585   8.254   3.758  1.00 45.91           O  
-ATOM    869  N   LYS A 113     -33.667  11.932   2.227  1.00 36.68           N  
-ATOM    870  CA  LYS A 113     -32.932  12.721   1.255  1.00 37.17           C  
-ATOM    871  C   LYS A 113     -31.828  13.490   1.947  1.00 33.45           C  
-ATOM    872  O   LYS A 113     -30.687  13.401   1.561  1.00 32.34           O  
-ATOM    873  CB  LYS A 113     -33.874  13.650   0.476  1.00 42.29           C  
-ATOM    874  CG  LYS A 113     -34.702  12.916  -0.587  1.00 45.78           C  
-ATOM    875  CD  LYS A 113     -35.945  13.685  -1.051  1.00 44.56           C  
-ATOM    876  CE  LYS A 113     -35.648  14.662  -2.188  1.00 38.88           C  
-ATOM    877  NZ  LYS A 113     -36.899  15.152  -2.872  1.00 34.08           N  
-ATOM    878  N   SER A 114     -32.172  14.226   2.993  1.00 39.34           N  
-ATOM    879  CA  SER A 114     -31.175  14.936   3.783  1.00 39.52           C  
-ATOM    880  C   SER A 114     -29.879  14.150   4.014  1.00 38.11           C  
-ATOM    881  O   SER A 114     -28.804  14.716   3.904  1.00 38.35           O  
-ATOM    882  CB  SER A 114     -31.766  15.356   5.121  1.00 37.66           C  
-ATOM    883  OG  SER A 114     -32.435  14.263   5.718  1.00 38.99           O  
-ATOM    884  N   TYR A 115     -29.973  12.863   4.338  1.00 35.33           N  
-ATOM    885  CA  TYR A 115     -28.770  12.075   4.615  1.00 38.35           C  
-ATOM    886  C   TYR A 115     -27.895  11.909   3.384  1.00 39.58           C  
-ATOM    887  O   TYR A 115     -26.678  11.890   3.497  1.00 45.94           O  
-ATOM    888  CB  TYR A 115     -29.087  10.686   5.192  1.00 49.88           C  
-ATOM    889  CG  TYR A 115     -29.974  10.666   6.423  1.00 56.57           C  
-ATOM    890  CD1 TYR A 115     -30.986   9.716   6.554  1.00 53.76           C  
-ATOM    891  CD2 TYR A 115     -29.804  11.590   7.447  1.00 49.07           C  
-ATOM    892  CE1 TYR A 115     -31.801   9.691   7.657  1.00 58.36           C  
-ATOM    893  CE2 TYR A 115     -30.612  11.567   8.557  1.00 55.55           C  
-ATOM    894  CZ  TYR A 115     -31.610  10.617   8.661  1.00 61.51           C  
-ATOM    895  OH  TYR A 115     -32.421  10.602   9.774  1.00 55.50           O  
-ATOM    896  N   GLU A 116     -28.512  11.764   2.215  1.00 41.89           N  
-ATOM    897  CA  GLU A 116     -27.770  11.659   0.950  1.00 38.85           C  
-ATOM    898  C   GLU A 116     -27.257  13.029   0.485  1.00 34.08           C  
-ATOM    899  O   GLU A 116     -26.309  13.127  -0.285  1.00 29.68           O  
-ATOM    900  CB  GLU A 116     -28.653  11.049  -0.147  1.00 33.24           C  
-ATOM    901  CG  GLU A 116     -29.530   9.899   0.305  1.00 38.79           C  
-ATOM    902  CD  GLU A 116     -28.734   8.646   0.542  1.00 45.04           C  
-ATOM    903  OE1 GLU A 116     -27.513   8.676   0.274  1.00 38.23           O  
-ATOM    904  OE2 GLU A 116     -29.326   7.638   0.992  1.00 47.52           O  
-ATOM    905  N   SER A 117     -27.903  14.079   0.970  1.00 37.36           N  
-ATOM    906  CA  SER A 117     -27.661  15.439   0.520  1.00 40.56           C  
-ATOM    907  C   SER A 117     -26.201  15.769   0.645  1.00 40.07           C  
-ATOM    908  O   SER A 117     -25.688  15.835   1.747  1.00 44.53           O  
-ATOM    909  CB  SER A 117     -28.475  16.424   1.370  1.00 43.75           C  
-ATOM    910  OG  SER A 117     -28.087  17.766   1.133  1.00 49.39           O  
-ATOM    911  N   GLY A 118     -25.533  15.993  -0.481  1.00 29.78           N  
-ATOM    912  CA  GLY A 118     -24.113  16.298  -0.462  1.00 32.02           C  
-ATOM    913  C   GLY A 118     -23.299  15.412  -1.388  1.00 35.89           C  
-ATOM    914  O   GLY A 118     -22.247  15.821  -1.876  1.00 36.30           O  
-ATOM    915  N   LEU A 119     -23.786  14.202  -1.644  1.00 33.27           N  
-ATOM    916  CA  LEU A 119     -23.075  13.281  -2.532  1.00 37.30           C  
-ATOM    917  C   LEU A 119     -22.938  13.867  -3.929  1.00 40.12           C  
-ATOM    918  O   LEU A 119     -23.715  14.736  -4.326  1.00 32.35           O  
-ATOM    919  CB  LEU A 119     -23.792  11.931  -2.644  1.00 28.70           C  
-ATOM    920  CG  LEU A 119     -23.902  11.068  -1.393  1.00 37.27           C  
-ATOM    921  CD1 LEU A 119     -24.902   9.967  -1.676  1.00 41.75           C  
-ATOM    922  CD2 LEU A 119     -22.546  10.498  -0.933  1.00 29.73           C  
-ATOM    923  N   PRO A 120     -21.939  13.382  -4.683  1.00 36.39           N  
-ATOM    924  CA  PRO A 120     -21.806  13.635  -6.119  1.00 31.69           C  
-ATOM    925  C   PRO A 120     -23.134  13.434  -6.878  1.00 41.12           C  
-ATOM    926  O   PRO A 120     -23.799  12.391  -6.725  1.00 30.77           O  
-ATOM    927  CB  PRO A 120     -20.811  12.562  -6.555  1.00 26.16           C  
-ATOM    928  CG  PRO A 120     -19.994  12.321  -5.379  1.00 25.65           C  
-ATOM    929  CD  PRO A 120     -20.851  12.535  -4.174  1.00 28.31           C  
-ATOM    930  N   LYS A 121     -23.495  14.416  -7.711  1.00 38.79           N  
-ATOM    931  CA  LYS A 121     -24.772  14.406  -8.411  1.00 32.42           C  
-ATOM    932  C   LYS A 121     -24.634  13.783  -9.788  1.00 34.08           C  
-ATOM    933  O   LYS A 121     -23.803  14.221 -10.577  1.00 41.76           O  
-ATOM    934  CB  LYS A 121     -25.318  15.828  -8.540  1.00 34.77           C  
-ATOM    935  CG  LYS A 121     -26.598  15.919  -9.364  1.00 33.04           C  
-ATOM    936  CD  LYS A 121     -27.113  17.338  -9.419  1.00 35.21           C  
-ATOM    937  CE  LYS A 121     -28.303  17.449 -10.353  1.00 46.98           C  
-ATOM    938  NZ  LYS A 121     -29.238  18.562 -10.006  1.00 48.94           N  
-ATOM    939  N   PRO A 122     -25.460  12.759 -10.080  1.00 34.68           N  
-ATOM    940  CA  PRO A 122     -25.515  12.035 -11.360  1.00 33.55           C  
-ATOM    941  C   PRO A 122     -25.888  12.933 -12.532  1.00 36.66           C  
-ATOM    942  O   PRO A 122     -26.604  13.921 -12.351  1.00 39.90           O  
-ATOM    943  CB  PRO A 122     -26.636  11.017 -11.134  1.00 27.54           C  
-ATOM    944  CG  PRO A 122     -26.681  10.827  -9.684  1.00 29.12           C  
-ATOM    945  CD  PRO A 122     -26.380  12.172  -9.095  1.00 28.38           C  
-ATOM    946  N   ASP A 123     -25.410  12.579 -13.720  1.00 36.98           N  
-ATOM    947  CA  ASP A 123     -25.670  13.356 -14.924  1.00 31.43           C  
-ATOM    948  C   ASP A 123     -26.753  12.664 -15.683  1.00 34.23           C  
-ATOM    949  O   ASP A 123     -27.348  13.214 -16.597  1.00 45.07           O  
-ATOM    950  CB  ASP A 123     -24.421  13.422 -15.789  1.00 31.82           C  
-ATOM    951  CG  ASP A 123     -23.291  14.170 -15.111  1.00 36.98           C  
-ATOM    952  OD1 ASP A 123     -23.474  15.369 -14.819  1.00 39.23           O  
-ATOM    953  OD2 ASP A 123     -22.230  13.560 -14.865  1.00 27.81           O  
-ATOM    954  N   LEU A 124     -27.022  11.441 -15.274  1.00 35.10           N  
-ATOM    955  CA  LEU A 124     -27.923  10.605 -16.008  1.00 28.72           C  
-ATOM    956  C   LEU A 124     -28.303   9.505 -15.071  1.00 26.84           C  
-ATOM    957  O   LEU A 124     -27.431   8.873 -14.467  1.00 36.03           O  
-ATOM    958  CB  LEU A 124     -27.166   9.997 -17.189  1.00 33.96           C  
-ATOM    959  CG  LEU A 124     -28.017   9.161 -18.138  1.00 34.21           C  
-ATOM    960  CD1 LEU A 124     -29.230   9.978 -18.556  1.00 32.75           C  
-ATOM    961  CD2 LEU A 124     -27.207   8.700 -19.350  1.00 37.67           C  
-ATOM    962  N   VAL A 125     -29.591   9.256 -14.939  1.00 23.18           N  
-ATOM    963  CA  VAL A 125     -30.035   8.146 -14.097  1.00 32.51           C  
-ATOM    964  C   VAL A 125     -30.931   7.204 -14.889  1.00 28.96           C  
-ATOM    965  O   VAL A 125     -32.061   7.533 -15.251  1.00 31.00           O  
-ATOM    966  CB  VAL A 125     -30.771   8.622 -12.817  1.00 30.44           C  
-ATOM    967  CG1 VAL A 125     -30.905   7.464 -11.852  1.00 32.80           C  
-ATOM    968  CG2 VAL A 125     -30.030   9.783 -12.165  1.00 23.07           C  
-ATOM    969  N   ILE A 126     -30.432   6.021 -15.170  1.00 30.04           N  
-ATOM    970  CA  ILE A 126     -31.195   5.147 -16.033  1.00 33.18           C  
-ATOM    971  C   ILE A 126     -32.046   4.211 -15.201  1.00 41.78           C  
-ATOM    972  O   ILE A 126     -31.541   3.371 -14.451  1.00 44.83           O  
-ATOM    973  CB  ILE A 126     -30.292   4.407 -17.012  1.00 30.47           C  
-ATOM    974  CG1 ILE A 126     -29.713   5.405 -18.018  1.00 27.44           C  
-ATOM    975  CG2 ILE A 126     -31.051   3.337 -17.737  1.00 27.05           C  
-ATOM    976  CD1 ILE A 126     -28.519   4.849 -18.814  1.00 32.87           C  
-ATOM    977  N   PHE A 127     -33.351   4.391 -15.316  1.00 36.28           N  
-ATOM    978  CA  PHE A 127     -34.287   3.600 -14.549  1.00 33.50           C  
-ATOM    979  C   PHE A 127     -34.841   2.480 -15.424  1.00 38.34           C  
-ATOM    980  O   PHE A 127     -35.365   2.714 -16.519  1.00 38.83           O  
-ATOM    981  CB  PHE A 127     -35.403   4.497 -13.998  1.00 38.34           C  
-ATOM    982  CG  PHE A 127     -36.381   3.773 -13.131  1.00 49.19           C  
-ATOM    983  CD1 PHE A 127     -36.159   3.655 -11.763  1.00 35.26           C  
-ATOM    984  CD2 PHE A 127     -37.514   3.190 -13.687  1.00 46.03           C  
-ATOM    985  CE1 PHE A 127     -37.048   2.980 -10.964  1.00 31.96           C  
-ATOM    986  CE2 PHE A 127     -38.415   2.508 -12.891  1.00 44.28           C  
-ATOM    987  CZ  PHE A 127     -38.181   2.401 -11.526  1.00 47.53           C  
-ATOM    988  N   LEU A 128     -34.697   1.257 -14.944  1.00 36.36           N  
-ATOM    989  CA  LEU A 128     -35.189   0.099 -15.667  1.00 32.54           C  
-ATOM    990  C   LEU A 128     -36.563  -0.345 -15.171  1.00 35.35           C  
-ATOM    991  O   LEU A 128     -36.693  -0.826 -14.041  1.00 42.05           O  
-ATOM    992  CB  LEU A 128     -34.211  -1.064 -15.512  1.00 24.07           C  
-ATOM    993  CG  LEU A 128     -33.017  -1.117 -16.458  1.00 30.17           C  
-ATOM    994  CD1 LEU A 128     -32.447   0.273 -16.680  1.00 29.41           C  
-ATOM    995  CD2 LEU A 128     -31.951  -2.113 -15.960  1.00 34.69           C  
-ATOM    996  N   GLU A 129     -37.585  -0.216 -16.015  1.00 40.50           N  
-ATOM    997  CA  GLU A 129     -38.912  -0.726 -15.656  1.00 40.64           C  
-ATOM    998  C   GLU A 129     -38.907  -2.245 -15.578  1.00 42.86           C  
-ATOM    999  O   GLU A 129     -38.215  -2.917 -16.352  1.00 39.78           O  
-ATOM   1000  CB  GLU A 129     -39.989  -0.266 -16.641  1.00 36.96           C  
-ATOM   1001  CG  GLU A 129     -40.283   1.212 -16.603  1.00 36.93           C  
-ATOM   1002  CD  GLU A 129     -41.614   1.553 -17.261  1.00 69.27           C  
-ATOM   1003  OE1 GLU A 129     -41.997   0.869 -18.242  1.00 63.37           O  
-ATOM   1004  OE2 GLU A 129     -42.281   2.505 -16.790  1.00 81.01           O  
-ATOM   1005  N   SER A 130     -39.672  -2.779 -14.628  1.00 61.39           N  
-ATOM   1006  CA  SER A 130     -39.870  -4.223 -14.520  1.00 66.54           C  
-ATOM   1007  C   SER A 130     -41.307  -4.555 -14.915  1.00 62.88           C  
-ATOM   1008  O   SER A 130     -42.252  -4.023 -14.336  1.00 56.37           O  
-ATOM   1009  CB  SER A 130     -39.577  -4.707 -13.098  1.00 47.40           C  
-ATOM   1010  OG  SER A 130     -38.469  -4.014 -12.539  1.00 42.35           O  
-ATOM   1011  N   GLY A 131     -41.475  -5.411 -15.917  1.00 54.02           N  
-ATOM   1012  CA  GLY A 131     -42.807  -5.796 -16.342  1.00 65.01           C  
-ATOM   1013  C   GLY A 131     -43.322  -7.003 -15.584  1.00 75.88           C  
-ATOM   1014  O   GLY A 131     -43.006  -7.185 -14.407  1.00 74.13           O  
-ATOM   1015  N   SER A 132     -44.109  -7.837 -16.260  1.00 86.06           N  
-ATOM   1016  CA  SER A 132     -44.646  -9.056 -15.654  1.00 88.83           C  
-ATOM   1017  C   SER A 132     -43.542 -10.022 -15.199  1.00 80.96           C  
-ATOM   1018  O   SER A 132     -43.288 -10.181 -13.999  1.00 74.95           O  
-ATOM   1019  CB  SER A 132     -45.608  -9.760 -16.627  1.00 92.06           C  
-ATOM   1020  OG  SER A 132     -45.969 -11.060 -16.177  1.00 78.42           O  
-ATOM   1021  N   LYS A 133     -42.885 -10.657 -16.161  1.00 79.23           N  
-ATOM   1022  CA  LYS A 133     -41.922 -11.706 -15.860  1.00 78.50           C  
-ATOM   1023  C   LYS A 133     -40.696 -11.209 -15.096  1.00 76.61           C  
-ATOM   1024  O   LYS A 133     -39.743 -11.961 -14.899  1.00 78.26           O  
-ATOM   1025  N   GLU A 134     -40.712  -9.945 -14.676  1.00 84.30           N  
-ATOM   1026  CA  GLU A 134     -39.586  -9.379 -13.929  1.00 77.98           C  
-ATOM   1027  C   GLU A 134     -39.916  -9.124 -12.463  1.00 75.02           C  
-ATOM   1028  O   GLU A 134     -39.145  -9.508 -11.584  1.00 68.39           O  
-ATOM   1029  CB  GLU A 134     -39.052  -8.098 -14.580  1.00 70.29           C  
-ATOM   1030  CG  GLU A 134     -38.266  -8.330 -15.862  1.00 78.39           C  
-ATOM   1031  CD  GLU A 134     -39.036  -7.914 -17.106  1.00 84.70           C  
-ATOM   1032  OE1 GLU A 134     -38.397  -7.712 -18.165  1.00 95.36           O  
-ATOM   1033  OE2 GLU A 134     -40.275  -7.774 -17.021  1.00 68.33           O  
-ATOM   1034  N   ILE A 135     -41.044  -8.472 -12.192  1.00 67.98           N  
-ATOM   1035  CA  ILE A 135     -41.449  -8.288 -10.807  1.00 67.96           C  
-ATOM   1036  C   ILE A 135     -41.616  -9.655 -10.170  1.00 72.19           C  
-ATOM   1037  O   ILE A 135     -41.100  -9.910  -9.082  1.00 73.90           O  
-ATOM   1038  CB  ILE A 135     -42.754  -7.502 -10.655  1.00 59.96           C  
-ATOM   1039  CG1 ILE A 135     -42.597  -6.092 -11.222  1.00 76.32           C  
-ATOM   1040  CG2 ILE A 135     -43.126  -7.406  -9.196  1.00 61.75           C  
-ATOM   1041  CD1 ILE A 135     -43.771  -5.152 -10.910  1.00 71.07           C  
-ATOM   1042  N   ASN A 136     -42.317 -10.542 -10.867  1.00 71.91           N  
-ATOM   1043  CA  ASN A 136     -42.589 -11.872 -10.341  1.00 68.21           C  
-ATOM   1044  C   ASN A 136     -41.369 -12.766 -10.371  1.00 56.99           C  
-ATOM   1045  O   ASN A 136     -41.467 -13.973 -10.180  1.00 58.14           O  
-ATOM   1046  CB  ASN A 136     -43.772 -12.520 -11.066  1.00 73.66           C  
-ATOM   1047  CG  ASN A 136     -45.064 -11.733 -10.877  1.00 83.04           C  
-ATOM   1048  OD1 ASN A 136     -45.233 -10.655 -11.449  1.00 78.75           O  
-ATOM   1049  ND2 ASN A 136     -45.975 -12.266 -10.064  1.00 75.40           N  
-ATOM   1050  N   ARG A 137     -40.216 -12.155 -10.611  1.00 59.51           N  
-ATOM   1051  CA  ARG A 137     -38.934 -12.841 -10.493  1.00 68.68           C  
-ATOM   1052  C   ARG A 137     -38.489 -12.867  -9.031  1.00 67.60           C  
-ATOM   1053  O   ARG A 137     -37.632 -13.675  -8.643  1.00 56.41           O  
-ATOM   1054  CB  ARG A 137     -37.875 -12.134 -11.345  1.00 66.59           C  
-ATOM   1055  CG  ARG A 137     -37.613 -12.785 -12.691  1.00 73.65           C  
-ATOM   1056  CD  ARG A 137     -37.018 -14.181 -12.518  1.00 87.74           C  
-ATOM   1057  NE  ARG A 137     -36.182 -14.576 -13.652  1.00105.71           N  
-ATOM   1058  CZ  ARG A 137     -36.620 -15.234 -14.722  1.00107.41           C  
-ATOM   1059  NH1 ARG A 137     -37.899 -15.582 -14.817  1.00103.63           N  
-ATOM   1060  NH2 ARG A 137     -35.775 -15.546 -15.698  1.00 79.03           N  
-ATOM   1061  N   ASN A 138     -39.085 -11.971  -8.237  1.00 58.91           N  
-ATOM   1062  CA  ASN A 138     -38.752 -11.798  -6.825  1.00 63.15           C  
-ATOM   1063  C   ASN A 138     -39.271 -12.923  -5.920  1.00 66.12           C  
-ATOM   1064  O   ASN A 138     -40.455 -12.959  -5.563  1.00 56.90           O  
-ATOM   1065  CB  ASN A 138     -39.262 -10.440  -6.322  1.00 62.50           C  
-ATOM   1066  CG  ASN A 138     -38.418  -9.266  -6.824  1.00 69.53           C  
-ATOM   1067  OD1 ASN A 138     -37.218  -9.180  -6.545  1.00 63.48           O  
-ATOM   1068  ND2 ASN A 138     -39.052  -8.347  -7.552  1.00 62.97           N  
-ATOM   1069  N   VAL A 139     -38.368 -13.821  -5.532  1.00 60.99           N  
-ATOM   1070  CA  VAL A 139     -38.739 -14.995  -4.748  1.00 54.82           C  
-ATOM   1071  C   VAL A 139     -38.144 -15.001  -3.334  1.00 60.96           C  
-ATOM   1072  O   VAL A 139     -37.953 -16.065  -2.736  1.00 49.41           O  
-ATOM   1073  CB  VAL A 139     -38.322 -16.283  -5.470  1.00 53.56           C  
-ATOM   1074  CG1 VAL A 139     -39.159 -16.470  -6.720  1.00 47.93           C  
-ATOM   1075  CG2 VAL A 139     -36.825 -16.242  -5.797  1.00 54.33           C  
-ATOM   1076  N   GLY A 140     -37.835 -13.813  -2.817  1.00 64.73           N  
-ATOM   1077  CA  GLY A 140     -37.439 -13.649  -1.428  1.00 43.95           C  
-ATOM   1078  C   GLY A 140     -36.197 -14.394  -0.977  1.00 48.04           C  
-ATOM   1079  O   GLY A 140     -36.102 -14.764   0.197  1.00 48.87           O  
-ATOM   1080  N   GLU A 141     -35.242 -14.620  -1.881  1.00 50.71           N  
-ATOM   1081  CA  GLU A 141     -33.963 -15.177  -1.456  1.00 50.70           C  
-ATOM   1082  C   GLU A 141     -33.237 -14.139  -0.617  1.00 42.88           C  
-ATOM   1083  O   GLU A 141     -32.434 -14.487   0.241  1.00 51.40           O  
-ATOM   1084  CB  GLU A 141     -33.104 -15.638  -2.636  1.00 42.85           C  
-ATOM   1085  CG  GLU A 141     -33.124 -14.704  -3.821  1.00 75.34           C  
-ATOM   1086  CD  GLU A 141     -32.588 -15.349  -5.081  1.00 89.33           C  
-ATOM   1087  OE1 GLU A 141     -31.586 -16.095  -4.969  1.00 89.54           O  
-ATOM   1088  OE2 GLU A 141     -33.170 -15.108  -6.173  1.00 68.81           O  
-ATOM   1089  N   GLU A 142     -33.530 -12.863  -0.859  1.00 34.57           N  
-ATOM   1090  CA  GLU A 142     -33.007 -11.795  -0.005  1.00 43.06           C  
-ATOM   1091  C   GLU A 142     -34.114 -10.945   0.626  1.00 41.04           C  
-ATOM   1092  O   GLU A 142     -35.281 -11.050   0.265  1.00 34.76           O  
-ATOM   1093  CB  GLU A 142     -31.972 -10.932  -0.736  1.00 50.79           C  
-ATOM   1094  CG  GLU A 142     -30.638 -11.643  -0.932  1.00 52.28           C  
-ATOM   1095  CD  GLU A 142     -29.506 -10.713  -1.321  1.00 59.70           C  
-ATOM   1096  OE1 GLU A 142     -29.787  -9.646  -1.926  1.00 54.24           O  
-ATOM   1097  OE2 GLU A 142     -28.332 -11.065  -1.028  1.00 48.41           O  
-ATOM   1098  N   ILE A 143     -33.750 -10.104   1.584  1.00 45.65           N  
-ATOM   1099  CA  ILE A 143     -34.772  -9.558   2.475  1.00 51.64           C  
-ATOM   1100  C   ILE A 143     -35.859  -8.709   1.791  1.00 42.58           C  
-ATOM   1101  O   ILE A 143     -37.046  -8.921   2.022  1.00 45.26           O  
-ATOM   1102  CB  ILE A 143     -34.165  -8.854   3.725  1.00 48.61           C  
-ATOM   1103  CG1 ILE A 143     -35.177  -8.865   4.895  1.00 44.34           C  
-ATOM   1104  CG2 ILE A 143     -33.625  -7.466   3.356  1.00 40.94           C  
-ATOM   1105  CD1 ILE A 143     -34.781  -8.029   6.139  1.00 38.90           C  
-ATOM   1106  N   TYR A 144     -35.467  -7.769   0.949  1.00 39.88           N  
-ATOM   1107  CA  TYR A 144     -36.453  -6.915   0.314  1.00 39.18           C  
-ATOM   1108  C   TYR A 144     -37.090  -7.545  -0.917  1.00 45.65           C  
-ATOM   1109  O   TYR A 144     -37.954  -6.924  -1.531  1.00 44.89           O  
-ATOM   1110  CB  TYR A 144     -35.825  -5.610  -0.108  1.00 35.57           C  
-ATOM   1111  CG  TYR A 144     -35.303  -4.785   1.022  1.00 40.58           C  
-ATOM   1112  CD1 TYR A 144     -36.170  -4.106   1.843  1.00 39.60           C  
-ATOM   1113  CD2 TYR A 144     -33.936  -4.653   1.257  1.00 43.69           C  
-ATOM   1114  CE1 TYR A 144     -35.707  -3.316   2.887  1.00 48.48           C  
-ATOM   1115  CE2 TYR A 144     -33.460  -3.853   2.300  1.00 44.17           C  
-ATOM   1116  CZ  TYR A 144     -34.363  -3.183   3.113  1.00 48.93           C  
-ATOM   1117  OH  TYR A 144     -33.952  -2.381   4.166  1.00 53.40           O  
-ATOM   1118  N   GLU A 145     -36.663  -8.756  -1.283  1.00 36.69           N  
-ATOM   1119  CA  GLU A 145     -37.177  -9.428  -2.484  1.00 48.63           C  
-ATOM   1120  C   GLU A 145     -38.606 -10.007  -2.346  1.00 42.08           C  
-ATOM   1121  O   GLU A 145     -38.832 -11.217  -2.411  1.00 32.22           O  
-ATOM   1122  CB  GLU A 145     -36.177 -10.476  -2.987  1.00 45.08           C  
-ATOM   1123  CG  GLU A 145     -34.896  -9.869  -3.527  1.00 37.43           C  
-ATOM   1124  CD  GLU A 145     -33.903 -10.915  -3.969  1.00 53.86           C  
-ATOM   1125  OE1 GLU A 145     -34.278 -12.106  -3.953  1.00 64.28           O  
-ATOM   1126  OE2 GLU A 145     -32.758 -10.555  -4.335  1.00 49.08           O  
-ATOM   1127  N   ASP A 146     -39.562  -9.107  -2.163  1.00 35.77           N  
-ATOM   1128  CA  ASP A 146     -40.948  -9.483  -2.026  1.00 47.28           C  
-ATOM   1129  C   ASP A 146     -41.825  -8.575  -2.868  1.00 53.21           C  
-ATOM   1130  O   ASP A 146     -41.835  -7.348  -2.693  1.00 46.14           O  
-ATOM   1131  CB  ASP A 146     -41.405  -9.449  -0.566  1.00 58.07           C  
-ATOM   1132  CG  ASP A 146     -42.920  -9.532  -0.435  1.00 74.57           C  
-ATOM   1133  OD1 ASP A 146     -43.563 -10.172  -1.300  1.00 78.13           O  
-ATOM   1134  OD2 ASP A 146     -43.475  -8.950   0.521  1.00 74.11           O  
-ATOM   1135  N   VAL A 147     -42.561  -9.221  -3.773  1.00 56.51           N  
-ATOM   1136  CA  VAL A 147     -43.445  -8.591  -4.747  1.00 48.83           C  
-ATOM   1137  C   VAL A 147     -44.289  -7.466  -4.188  1.00 58.60           C  
-ATOM   1138  O   VAL A 147     -44.368  -6.391  -4.783  1.00 62.21           O  
-ATOM   1139  CB  VAL A 147     -44.391  -9.636  -5.327  1.00 58.04           C  
-ATOM   1140  CG1 VAL A 147     -45.176  -9.060  -6.516  1.00 69.44           C  
-ATOM   1141  CG2 VAL A 147     -43.600 -10.880  -5.716  1.00 64.05           C  
-ATOM   1142  N   THR A 148     -44.939  -7.721  -3.058  1.00 57.36           N  
-ATOM   1143  CA  THR A 148     -45.826  -6.729  -2.465  1.00 59.75           C  
-ATOM   1144  C   THR A 148     -45.041  -5.498  -1.964  1.00 55.91           C  
-ATOM   1145  O   THR A 148     -45.525  -4.355  -2.028  1.00 50.78           O  
-ATOM   1146  CB  THR A 148     -46.740  -7.353  -1.349  1.00 61.08           C  
-ATOM   1147  OG1 THR A 148     -45.944  -7.810  -0.253  1.00 79.94           O  
-ATOM   1148  CG2 THR A 148     -47.508  -8.544  -1.880  1.00 53.12           C  
-ATOM   1149  N   PHE A 149     -43.818  -5.727  -1.486  1.00 51.49           N  
-ATOM   1150  CA  PHE A 149     -42.988  -4.626  -0.989  1.00 51.64           C  
-ATOM   1151  C   PHE A 149     -42.390  -3.795  -2.137  1.00 51.03           C  
-ATOM   1152  O   PHE A 149     -42.412  -2.563  -2.092  1.00 37.41           O  
-ATOM   1153  CB  PHE A 149     -41.895  -5.138  -0.036  1.00 50.37           C  
-ATOM   1154  CG  PHE A 149     -40.979  -4.051   0.472  1.00 45.00           C  
-ATOM   1155  CD1 PHE A 149     -41.453  -3.068   1.339  1.00 49.75           C  
-ATOM   1156  CD2 PHE A 149     -39.653  -3.997   0.074  1.00 40.99           C  
-ATOM   1157  CE1 PHE A 149     -40.621  -2.043   1.807  1.00 42.59           C  
-ATOM   1158  CE2 PHE A 149     -38.825  -2.975   0.526  1.00 48.94           C  
-ATOM   1159  CZ  PHE A 149     -39.316  -1.993   1.400  1.00 40.95           C  
-ATOM   1160  N   GLN A 150     -41.868  -4.477  -3.160  1.00 45.62           N  
-ATOM   1161  CA  GLN A 150     -41.335  -3.819  -4.354  1.00 43.58           C  
-ATOM   1162  C   GLN A 150     -42.358  -2.864  -4.988  1.00 48.54           C  
-ATOM   1163  O   GLN A 150     -42.018  -1.758  -5.404  1.00 45.79           O  
-ATOM   1164  CB  GLN A 150     -40.881  -4.859  -5.378  1.00 43.57           C  
-ATOM   1165  CG  GLN A 150     -39.863  -5.881  -4.843  1.00 59.99           C  
-ATOM   1166  CD  GLN A 150     -38.405  -5.405  -4.944  1.00 60.45           C  
-ATOM   1167  OE1 GLN A 150     -38.143  -4.273  -5.361  1.00 55.55           O  
-ATOM   1168  NE2 GLN A 150     -37.454  -6.275  -4.560  1.00 45.41           N  
-ATOM   1169  N   GLN A 151     -43.614  -3.292  -5.056  1.00 55.57           N  
-ATOM   1170  CA  GLN A 151     -44.690  -2.432  -5.551  1.00 57.93           C  
-ATOM   1171  C   GLN A 151     -44.716  -1.124  -4.758  1.00 51.71           C  
-ATOM   1172  O   GLN A 151     -45.072  -0.060  -5.282  1.00 46.03           O  
-ATOM   1173  CB  GLN A 151     -46.048  -3.155  -5.458  1.00 54.60           C  
-ATOM   1174  CG  GLN A 151     -47.185  -2.481  -6.218  1.00 62.94           C  
-ATOM   1175  CD  GLN A 151     -46.820  -2.157  -7.662  1.00 82.27           C  
-ATOM   1176  OE1 GLN A 151     -45.984  -2.833  -8.277  1.00 68.37           O  
-ATOM   1177  NE2 GLN A 151     -47.450  -1.115  -8.211  1.00 71.86           N  
-ATOM   1178  N   LYS A 152     -44.325  -1.219  -3.490  1.00 48.06           N  
-ATOM   1179  CA  LYS A 152     -44.287  -0.067  -2.598  1.00 51.63           C  
-ATOM   1180  C   LYS A 152     -43.079   0.852  -2.867  1.00 52.00           C  
-ATOM   1181  O   LYS A 152     -43.194   2.088  -2.835  1.00 43.12           O  
-ATOM   1182  CB  LYS A 152     -44.287  -0.545  -1.145  1.00 52.19           C  
-ATOM   1183  CG  LYS A 152     -45.647  -1.006  -0.639  1.00 66.20           C  
-ATOM   1184  CD  LYS A 152     -46.463   0.181  -0.149  1.00 90.45           C  
-ATOM   1185  CE  LYS A 152     -47.834  -0.244   0.357  1.00 97.59           C  
-ATOM   1186  NZ  LYS A 152     -48.479   0.831   1.174  1.00 99.66           N  
-ATOM   1187  N   VAL A 153     -41.924   0.243  -3.125  1.00 47.75           N  
-ATOM   1188  CA  VAL A 153     -40.722   0.994  -3.462  1.00 47.06           C  
-ATOM   1189  C   VAL A 153     -40.971   1.818  -4.719  1.00 47.33           C  
-ATOM   1190  O   VAL A 153     -40.568   2.987  -4.800  1.00 38.11           O  
-ATOM   1191  CB  VAL A 153     -39.512   0.058  -3.729  1.00 43.94           C  
-ATOM   1192  CG1 VAL A 153     -38.258   0.877  -3.966  1.00 40.22           C  
-ATOM   1193  CG2 VAL A 153     -39.303  -0.908  -2.580  1.00 39.64           C  
-ATOM   1194  N   LEU A 154     -41.647   1.185  -5.686  1.00 40.99           N  
-ATOM   1195  CA  LEU A 154     -41.926   1.764  -6.993  1.00 35.21           C  
-ATOM   1196  C   LEU A 154     -42.719   3.051  -6.879  1.00 39.38           C  
-ATOM   1197  O   LEU A 154     -42.502   3.992  -7.643  1.00 42.46           O  
-ATOM   1198  CB  LEU A 154     -42.688   0.762  -7.851  1.00 46.40           C  
-ATOM   1199  CG  LEU A 154     -42.939   1.154  -9.309  1.00 44.70           C  
-ATOM   1200  CD1 LEU A 154     -41.637   1.439 -10.034  1.00 42.28           C  
-ATOM   1201  CD2 LEU A 154     -43.687   0.047  -9.982  1.00 35.89           C  
-ATOM   1202  N   GLN A 155     -43.640   3.079  -5.924  1.00 42.03           N  
-ATOM   1203  CA  GLN A 155     -44.391   4.286  -5.610  1.00 41.52           C  
-ATOM   1204  C   GLN A 155     -43.456   5.425  -5.252  1.00 48.03           C  
-ATOM   1205  O   GLN A 155     -43.661   6.572  -5.655  1.00 48.55           O  
-ATOM   1206  CB  GLN A 155     -45.334   4.026  -4.445  1.00 51.39           C  
-ATOM   1207  CG  GLN A 155     -46.306   2.886  -4.697  1.00 63.39           C  
-ATOM   1208  CD  GLN A 155     -47.002   3.014  -6.042  1.00 82.52           C  
-ATOM   1209  OE1 GLN A 155     -47.905   3.838  -6.213  1.00 74.48           O  
-ATOM   1210  NE2 GLN A 155     -46.582   2.195  -7.009  1.00 67.28           N  
-ATOM   1211  N   GLU A 156     -42.416   5.096  -4.495  1.00 47.95           N  
-ATOM   1212  CA  GLU A 156     -41.459   6.096  -4.045  1.00 52.83           C  
-ATOM   1213  C   GLU A 156     -40.492   6.517  -5.163  1.00 46.53           C  
-ATOM   1214  O   GLU A 156     -40.055   7.669  -5.220  1.00 42.96           O  
-ATOM   1215  CB  GLU A 156     -40.710   5.585  -2.801  1.00 47.42           C  
-ATOM   1216  CG  GLU A 156     -41.607   4.936  -1.739  1.00 48.36           C  
-ATOM   1217  CD  GLU A 156     -42.642   5.884  -1.126  1.00 58.86           C  
-ATOM   1218  OE1 GLU A 156     -42.364   7.099  -0.980  1.00 44.85           O  
-ATOM   1219  OE2 GLU A 156     -43.741   5.394  -0.772  1.00 58.82           O  
-ATOM   1220  N   TYR A 157     -40.166   5.579  -6.049  1.00 39.30           N  
-ATOM   1221  CA  TYR A 157     -39.304   5.876  -7.191  1.00 41.17           C  
-ATOM   1222  C   TYR A 157     -40.011   6.874  -8.103  1.00 51.30           C  
-ATOM   1223  O   TYR A 157     -39.486   7.959  -8.400  1.00 43.28           O  
-ATOM   1224  CB  TYR A 157     -38.977   4.603  -7.971  1.00 32.82           C  
-ATOM   1225  CG  TYR A 157     -37.638   3.937  -7.646  1.00 30.39           C  
-ATOM   1226  CD1 TYR A 157     -37.534   2.547  -7.558  1.00 28.45           C  
-ATOM   1227  CD2 TYR A 157     -36.473   4.690  -7.459  1.00 29.85           C  
-ATOM   1228  CE1 TYR A 157     -36.317   1.925  -7.293  1.00 30.42           C  
-ATOM   1229  CE2 TYR A 157     -35.236   4.072  -7.179  1.00 27.32           C  
-ATOM   1230  CZ  TYR A 157     -35.166   2.687  -7.098  1.00 32.53           C  
-ATOM   1231  OH  TYR A 157     -33.957   2.057  -6.833  1.00 20.63           O  
-ATOM   1232  N   LYS A 158     -41.216   6.503  -8.532  1.00 52.68           N  
-ATOM   1233  CA  LYS A 158     -42.028   7.360  -9.392  1.00 55.28           C  
-ATOM   1234  C   LYS A 158     -42.120   8.790  -8.833  1.00 52.12           C  
-ATOM   1235  O   LYS A 158     -41.961   9.755  -9.582  1.00 58.65           O  
-ATOM   1236  CB  LYS A 158     -43.425   6.747  -9.632  1.00 59.48           C  
-ATOM   1237  CG  LYS A 158     -43.450   5.461 -10.491  1.00 52.83           C  
-ATOM   1238  CD  LYS A 158     -43.014   5.724 -11.950  1.00 68.94           C  
-ATOM   1239  CE  LYS A 158     -42.975   4.437 -12.800  1.00 71.82           C  
-ATOM   1240  NZ  LYS A 158     -42.142   4.525 -14.052  1.00 34.02           N  
-ATOM   1241  N   LYS A 159     -42.356   8.918  -7.526  1.00 48.94           N  
-ATOM   1242  CA  LYS A 159     -42.424  10.222  -6.864  1.00 54.47           C  
-ATOM   1243  C   LYS A 159     -41.200  11.082  -7.151  1.00 51.98           C  
-ATOM   1244  O   LYS A 159     -41.322  12.259  -7.503  1.00 55.64           O  
-ATOM   1245  CB  LYS A 159     -42.568  10.044  -5.349  1.00 53.80           C  
-ATOM   1246  CG  LYS A 159     -43.968   9.656  -4.888  1.00 62.40           C  
-ATOM   1247  CD  LYS A 159     -43.968   8.791  -3.611  1.00 69.63           C  
-ATOM   1248  CE  LYS A 159     -44.425   9.544  -2.350  1.00 71.68           C  
-ATOM   1249  NZ  LYS A 159     -43.367  10.388  -1.720  1.00 70.45           N  
-ATOM   1250  N   MET A 160     -40.021  10.484  -6.998  1.00 51.84           N  
-ATOM   1251  CA  MET A 160     -38.747  11.191  -7.167  1.00 58.05           C  
-ATOM   1252  C   MET A 160     -38.446  11.588  -8.594  1.00 52.04           C  
-ATOM   1253  O   MET A 160     -37.833  12.623  -8.841  1.00 48.81           O  
-ATOM   1254  CB  MET A 160     -37.602  10.313  -6.704  1.00 47.83           C  
-ATOM   1255  CG  MET A 160     -37.554  10.133  -5.245  1.00 40.48           C  
-ATOM   1256  SD  MET A 160     -35.989   9.365  -4.893  1.00 44.49           S  
-ATOM   1257  CE  MET A 160     -36.362   7.636  -5.199  1.00 33.67           C  
-ATOM   1258  N   ILE A 161     -38.827  10.720  -9.519  1.00 48.97           N  
-ATOM   1259  CA  ILE A 161     -38.727  11.018 -10.928  1.00 45.25           C  
-ATOM   1260  C   ILE A 161     -39.514  12.297 -11.222  1.00 44.98           C  
-ATOM   1261  O   ILE A 161     -38.978  13.256 -11.776  1.00 45.19           O  
-ATOM   1262  CB  ILE A 161     -39.227   9.826 -11.757  1.00 41.07           C  
-ATOM   1263  CG1 ILE A 161     -38.272   8.642 -11.566  1.00 43.74           C  
-ATOM   1264  CG2 ILE A 161     -39.303  10.185 -13.210  1.00 44.19           C  
-ATOM   1265  CD1 ILE A 161     -38.686   7.373 -12.279  1.00 39.09           C  
-ATOM   1266  N   GLU A 162     -40.772  12.324 -10.802  1.00 48.50           N  
-ATOM   1267  CA  GLU A 162     -41.651  13.456 -11.082  1.00 52.43           C  
-ATOM   1268  C   GLU A 162     -41.113  14.779 -10.540  1.00 48.87           C  
-ATOM   1269  O   GLU A 162     -41.579  15.863 -10.949  1.00 40.67           O  
-ATOM   1270  CB  GLU A 162     -43.057  13.170 -10.547  1.00 46.12           C  
-ATOM   1271  CG  GLU A 162     -43.871  12.262 -11.461  1.00 62.97           C  
-ATOM   1272  CD  GLU A 162     -44.796  11.330 -10.703  1.00 99.89           C  
-ATOM   1273  OE1 GLU A 162     -44.985  11.530  -9.474  1.00 91.86           O  
-ATOM   1274  OE2 GLU A 162     -45.327  10.392 -11.346  1.00 89.65           O  
-ATOM   1275  N   GLU A 163     -40.136  14.678  -9.633  1.00 38.27           N  
-ATOM   1276  CA  GLU A 163     -39.521  15.848  -9.010  1.00 46.41           C  
-ATOM   1277  C   GLU A 163     -38.419  16.414  -9.886  1.00 49.40           C  
-ATOM   1278  O   GLU A 163     -37.816  17.447  -9.562  1.00 41.45           O  
-ATOM   1279  CB  GLU A 163     -38.872  15.471  -7.686  1.00 55.60           C  
-ATOM   1280  CG  GLU A 163     -39.803  15.071  -6.562  1.00 65.62           C  
-ATOM   1281  CD  GLU A 163     -39.031  14.800  -5.273  1.00 66.35           C  
-ATOM   1282  OE1 GLU A 163     -37.882  14.307  -5.373  1.00 59.21           O  
-ATOM   1283  OE2 GLU A 163     -39.566  15.084  -4.174  1.00 64.68           O  
-ATOM   1284  N   GLY A 164     -38.159  15.709 -10.981  1.00 49.35           N  
-ATOM   1285  CA  GLY A 164     -36.984  15.902 -11.811  1.00 47.72           C  
-ATOM   1286  C   GLY A 164     -36.200  17.200 -11.765  1.00 52.11           C  
-ATOM   1287  O   GLY A 164     -36.519  18.159 -12.467  1.00 59.70           O  
-ATOM   1288  N   ASP A 165     -35.171  17.224 -10.929  1.00 45.81           N  
-ATOM   1289  CA  ASP A 165     -34.118  18.221 -11.033  1.00 43.57           C  
-ATOM   1290  C   ASP A 165     -32.934  17.395 -11.469  1.00 53.81           C  
-ATOM   1291  O   ASP A 165     -31.834  17.892 -11.649  1.00 63.54           O  
-ATOM   1292  CB  ASP A 165     -33.845  18.949  -9.698  1.00 64.93           C  
-ATOM   1293  CG  ASP A 165     -33.482  17.990  -8.521  1.00 91.03           C  
-ATOM   1294  OD1 ASP A 165     -32.467  18.238  -7.819  1.00 69.21           O  
-ATOM   1295  OD2 ASP A 165     -34.219  17.009  -8.264  1.00 93.93           O  
-ATOM   1296  N   ILE A 166     -33.199  16.105 -11.634  1.00 50.36           N  
-ATOM   1297  CA  ILE A 166     -32.196  15.114 -11.984  1.00 51.07           C  
-ATOM   1298  C   ILE A 166     -32.524  14.593 -13.366  1.00 43.32           C  
-ATOM   1299  O   ILE A 166     -33.691  14.311 -13.665  1.00 41.44           O  
-ATOM   1300  CB  ILE A 166     -32.267  13.904 -11.015  1.00 58.81           C  
-ATOM   1301  CG1 ILE A 166     -31.979  14.337  -9.576  1.00 51.97           C  
-ATOM   1302  CG2 ILE A 166     -31.341  12.775 -11.459  1.00 44.18           C  
-ATOM   1303  CD1 ILE A 166     -30.670  15.019  -9.416  1.00 49.25           C  
-ATOM   1304  N   HIS A 167     -31.510  14.440 -14.209  1.00 36.57           N  
-ATOM   1305  CA  HIS A 167     -31.739  13.893 -15.551  1.00 39.67           C  
-ATOM   1306  C   HIS A 167     -32.003  12.381 -15.533  1.00 32.26           C  
-ATOM   1307  O   HIS A 167     -31.082  11.583 -15.354  1.00 36.18           O  
-ATOM   1308  CB  HIS A 167     -30.554  14.211 -16.457  1.00 43.21           C  
-ATOM   1309  CG  HIS A 167     -30.776  13.884 -17.899  1.00 51.45           C  
-ATOM   1310  ND1 HIS A 167     -30.225  14.623 -18.922  1.00 60.50           N  
-ATOM   1311  CD2 HIS A 167     -31.491  12.895 -18.494  1.00 49.34           C  
-ATOM   1312  CE1 HIS A 167     -30.579  14.103 -20.085  1.00 56.30           C  
-ATOM   1313  NE2 HIS A 167     -31.349  13.053 -19.850  1.00 48.66           N  
-ATOM   1314  N   TRP A 168     -33.263  12.005 -15.716  1.00 26.62           N  
-ATOM   1315  CA  TRP A 168     -33.668  10.599 -15.734  1.00 39.20           C  
-ATOM   1316  C   TRP A 168     -33.959  10.063 -17.157  1.00 43.35           C  
-ATOM   1317  O   TRP A 168     -34.595  10.734 -17.978  1.00 36.61           O  
-ATOM   1318  CB  TRP A 168     -34.952  10.399 -14.925  1.00 43.18           C  
-ATOM   1319  CG  TRP A 168     -34.878  10.539 -13.424  1.00 49.55           C  
-ATOM   1320  CD1 TRP A 168     -35.033  11.690 -12.690  1.00 50.03           C  
-ATOM   1321  CD2 TRP A 168     -34.732   9.476 -12.471  1.00 47.62           C  
-ATOM   1322  NE1 TRP A 168     -34.956  11.408 -11.345  1.00 46.35           N  
-ATOM   1323  CE2 TRP A 168     -34.773  10.055 -11.182  1.00 44.25           C  
-ATOM   1324  CE3 TRP A 168     -34.560   8.088 -12.581  1.00 46.35           C  
-ATOM   1325  CZ2 TRP A 168     -34.631   9.302 -10.013  1.00 41.20           C  
-ATOM   1326  CZ3 TRP A 168     -34.423   7.337 -11.421  1.00 52.66           C  
-ATOM   1327  CH2 TRP A 168     -34.458   7.947 -10.152  1.00 46.72           C  
-ATOM   1328  N   GLN A 169     -33.527   8.837 -17.434  1.00 37.34           N  
-ATOM   1329  CA  GLN A 169     -33.975   8.135 -18.633  1.00 39.63           C  
-ATOM   1330  C   GLN A 169     -34.670   6.822 -18.275  1.00 40.57           C  
-ATOM   1331  O   GLN A 169     -34.044   5.882 -17.790  1.00 40.04           O  
-ATOM   1332  CB  GLN A 169     -32.820   7.888 -19.607  1.00 40.75           C  
-ATOM   1333  CG  GLN A 169     -32.404   9.121 -20.416  1.00 52.12           C  
-ATOM   1334  CD  GLN A 169     -33.492   9.616 -21.365  1.00 47.52           C  
-ATOM   1335  OE1 GLN A 169     -33.944  10.767 -21.282  1.00 41.84           O  
-ATOM   1336  NE2 GLN A 169     -33.917   8.747 -22.271  1.00 47.43           N  
-ATOM   1337  N   ILE A 170     -35.971   6.760 -18.525  1.00 44.32           N  
-ATOM   1338  CA  ILE A 170     -36.779   5.598 -18.152  1.00 45.55           C  
-ATOM   1339  C   ILE A 170     -36.897   4.555 -19.265  1.00 38.88           C  
-ATOM   1340  O   ILE A 170     -37.521   4.791 -20.301  1.00 44.43           O  
-ATOM   1341  CB  ILE A 170     -38.211   6.033 -17.760  1.00 46.96           C  
-ATOM   1342  CG1 ILE A 170     -38.170   7.132 -16.685  1.00 47.17           C  
-ATOM   1343  CG2 ILE A 170     -39.024   4.822 -17.318  1.00 40.01           C  
-ATOM   1344  CD1 ILE A 170     -39.306   8.157 -16.813  1.00 51.05           C  
-ATOM   1345  N   ILE A 171     -36.326   3.386 -19.052  1.00 30.82           N  
-ATOM   1346  CA  ILE A 171     -36.368   2.386 -20.103  1.00 33.54           C  
-ATOM   1347  C   ILE A 171     -37.474   1.358 -19.928  1.00 46.62           C  
-ATOM   1348  O   ILE A 171     -37.484   0.602 -18.950  1.00 47.56           O  
-ATOM   1349  CB  ILE A 171     -35.058   1.639 -20.173  1.00 33.70           C  
-ATOM   1350  CG1 ILE A 171     -33.899   2.636 -20.182  1.00 37.62           C  
-ATOM   1351  CG2 ILE A 171     -35.041   0.723 -21.373  1.00 33.52           C  
-ATOM   1352  CD1 ILE A 171     -33.851   3.531 -21.397  1.00 36.21           C  
-ATOM   1353  N   SER A 172     -38.375   1.306 -20.905  1.00 55.01           N  
-ATOM   1354  CA  SER A 172     -39.510   0.382 -20.872  1.00 53.92           C  
-ATOM   1355  C   SER A 172     -39.107  -1.069 -20.681  1.00 58.23           C  
-ATOM   1356  O   SER A 172     -38.026  -1.506 -21.109  1.00 55.63           O  
-ATOM   1357  CB  SER A 172     -40.369   0.498 -22.137  1.00 59.82           C  
-ATOM   1358  OG  SER A 172     -41.346  -0.538 -22.192  1.00 60.13           O  
-ATOM   1359  N   SER A 173     -40.012  -1.802 -20.040  1.00 54.83           N  
-ATOM   1360  CA  SER A 173     -39.872  -3.231 -19.804  1.00 59.52           C  
-ATOM   1361  C   SER A 173     -40.000  -4.022 -21.102  1.00 68.24           C  
-ATOM   1362  O   SER A 173     -39.438  -5.118 -21.236  1.00 61.06           O  
-ATOM   1363  CB  SER A 173     -40.976  -3.640 -18.851  1.00 52.10           C  
-ATOM   1364  OG  SER A 173     -42.011  -2.666 -18.923  1.00 52.14           O  
-ATOM   1365  N   GLU A 174     -40.721  -3.432 -22.056  1.00 55.48           N  
-ATOM   1366  CA  GLU A 174     -41.177  -4.125 -23.253  1.00 61.87           C  
-ATOM   1367  C   GLU A 174     -40.185  -4.200 -24.410  1.00 70.86           C  
-ATOM   1368  O   GLU A 174     -40.476  -4.816 -25.439  1.00 79.83           O  
-ATOM   1369  CB  GLU A 174     -42.466  -3.481 -23.751  1.00 74.97           C  
-ATOM   1370  CG  GLU A 174     -43.648  -3.715 -22.845  1.00 83.49           C  
-ATOM   1371  CD  GLU A 174     -44.748  -2.705 -23.074  1.00 86.00           C  
-ATOM   1372  OE1 GLU A 174     -44.585  -1.547 -22.629  1.00 80.62           O  
-ATOM   1373  OE2 GLU A 174     -45.771  -3.072 -23.691  1.00 75.89           O  
-ATOM   1374  N   PHE A 175     -39.025  -3.576 -24.265  1.00 68.69           N  
-ATOM   1375  CA  PHE A 175     -38.007  -3.689 -25.303  1.00 68.10           C  
-ATOM   1376  C   PHE A 175     -37.402  -5.089 -25.379  1.00 74.17           C  
-ATOM   1377  O   PHE A 175     -37.545  -5.905 -24.462  1.00 72.62           O  
-ATOM   1378  CB  PHE A 175     -36.922  -2.634 -25.118  1.00 62.37           C  
-ATOM   1379  CG  PHE A 175     -37.320  -1.288 -25.621  1.00 71.71           C  
-ATOM   1380  CD1 PHE A 175     -38.266  -0.533 -24.948  1.00 77.29           C  
-ATOM   1381  CD2 PHE A 175     -36.769  -0.785 -26.781  1.00 75.73           C  
-ATOM   1382  CE1 PHE A 175     -38.645   0.709 -25.421  1.00 85.22           C  
-ATOM   1383  CE2 PHE A 175     -37.144   0.455 -27.258  1.00 79.70           C  
-ATOM   1384  CZ  PHE A 175     -38.085   1.205 -26.576  1.00 81.96           C  
-ATOM   1385  N   GLU A 176     -36.737  -5.364 -26.490  1.00 75.49           N  
-ATOM   1386  CA  GLU A 176     -36.102  -6.653 -26.681  1.00 77.10           C  
-ATOM   1387  C   GLU A 176     -34.675  -6.583 -26.153  1.00 70.84           C  
-ATOM   1388  O   GLU A 176     -34.001  -5.572 -26.340  1.00 69.95           O  
-ATOM   1389  CB  GLU A 176     -36.106  -7.019 -28.168  1.00 80.48           C  
-ATOM   1390  CG  GLU A 176     -36.188  -8.509 -28.406  1.00 81.33           C  
-ATOM   1391  CD  GLU A 176     -37.268  -9.141 -27.550  1.00 85.05           C  
-ATOM   1392  OE1 GLU A 176     -38.436  -9.157 -27.989  1.00 82.04           O  
-ATOM   1393  OE2 GLU A 176     -36.951  -9.611 -26.434  1.00 95.21           O  
-ATOM   1394  N   GLU A 177     -34.215  -7.647 -25.501  1.00 52.65           N  
-ATOM   1395  CA  GLU A 177     -32.871  -7.658 -24.911  1.00 68.29           C  
-ATOM   1396  C   GLU A 177     -31.760  -6.924 -25.696  1.00 73.31           C  
-ATOM   1397  O   GLU A 177     -31.136  -5.996 -25.164  1.00 70.67           O  
-ATOM   1398  CB  GLU A 177     -32.432  -9.086 -24.550  1.00 59.14           C  
-ATOM   1399  CG  GLU A 177     -32.938  -9.512 -23.179  1.00 85.76           C  
-ATOM   1400  CD  GLU A 177     -32.968  -8.346 -22.190  1.00112.12           C  
-ATOM   1401  OE1 GLU A 177     -31.905  -7.708 -21.992  1.00105.61           O  
-ATOM   1402  OE2 GLU A 177     -34.053  -8.066 -21.617  1.00103.75           O  
-ATOM   1403  N   ASP A 178     -31.521  -7.347 -26.941  1.00 61.23           N  
-ATOM   1404  CA  ASP A 178     -30.478  -6.781 -27.796  1.00 52.28           C  
-ATOM   1405  C   ASP A 178     -30.740  -5.315 -28.149  1.00 59.59           C  
-ATOM   1406  O   ASP A 178     -29.807  -4.530 -28.352  1.00 52.01           O  
-ATOM   1407  CB  ASP A 178     -30.350  -7.614 -29.073  1.00 77.92           C  
-ATOM   1408  CG  ASP A 178     -31.714  -7.968 -29.690  1.00 95.71           C  
-ATOM   1409  OD1 ASP A 178     -32.523  -8.662 -29.029  1.00 90.31           O  
-ATOM   1410  OD2 ASP A 178     -31.976  -7.562 -30.846  1.00 97.58           O  
-ATOM   1411  N   VAL A 179     -32.019  -4.963 -28.219  1.00 55.12           N  
-ATOM   1412  CA  VAL A 179     -32.458  -3.609 -28.537  1.00 49.41           C  
-ATOM   1413  C   VAL A 179     -32.336  -2.660 -27.356  1.00 51.81           C  
-ATOM   1414  O   VAL A 179     -31.959  -1.491 -27.517  1.00 48.08           O  
-ATOM   1415  CB  VAL A 179     -33.914  -3.617 -28.994  1.00 50.60           C  
-ATOM   1416  CG1 VAL A 179     -34.485  -2.198 -29.004  1.00 45.95           C  
-ATOM   1417  CG2 VAL A 179     -34.002  -4.269 -30.364  1.00 56.25           C  
-ATOM   1418  N   LYS A 180     -32.683  -3.172 -26.173  1.00 62.01           N  
-ATOM   1419  CA  LYS A 180     -32.506  -2.456 -24.909  1.00 59.48           C  
-ATOM   1420  C   LYS A 180     -31.020  -2.182 -24.757  1.00 48.97           C  
-ATOM   1421  O   LYS A 180     -30.603  -1.032 -24.555  1.00 49.11           O  
-ATOM   1422  CB  LYS A 180     -32.995  -3.315 -23.739  1.00 61.78           C  
-ATOM   1423  CG  LYS A 180     -33.593  -2.553 -22.555  1.00 40.84           C  
-ATOM   1424  CD  LYS A 180     -33.763  -3.520 -21.390  1.00 57.05           C  
-ATOM   1425  CE  LYS A 180     -35.121  -3.397 -20.714  1.00 75.26           C  
-ATOM   1426  NZ  LYS A 180     -35.371  -4.560 -19.808  1.00 68.22           N  
-ATOM   1427  N   LYS A 181     -30.231  -3.246 -24.876  1.00 32.76           N  
-ATOM   1428  CA  LYS A 181     -28.782  -3.143 -24.834  1.00 43.36           C  
-ATOM   1429  C   LYS A 181     -28.246  -2.023 -25.736  1.00 42.61           C  
-ATOM   1430  O   LYS A 181     -27.424  -1.212 -25.306  1.00 29.75           O  
-ATOM   1431  CB  LYS A 181     -28.166  -4.508 -25.180  1.00 54.52           C  
-ATOM   1432  CG  LYS A 181     -27.036  -4.493 -26.209  1.00 74.42           C  
-ATOM   1433  CD  LYS A 181     -25.656  -4.253 -25.601  1.00 79.43           C  
-ATOM   1434  CE  LYS A 181     -24.592  -4.138 -26.707  1.00 91.05           C  
-ATOM   1435  NZ  LYS A 181     -23.193  -4.021 -26.181  1.00 78.62           N  
-ATOM   1436  N   GLU A 182     -28.723  -1.987 -26.979  1.00 46.58           N  
-ATOM   1437  CA  GLU A 182     -28.302  -0.976 -27.940  1.00 43.88           C  
-ATOM   1438  C   GLU A 182     -28.741   0.422 -27.536  1.00 40.88           C  
-ATOM   1439  O   GLU A 182     -27.951   1.360 -27.577  1.00 43.28           O  
-ATOM   1440  CB  GLU A 182     -28.828  -1.301 -29.337  1.00 47.58           C  
-ATOM   1441  CG  GLU A 182     -27.751  -1.793 -30.307  1.00 58.21           C  
-ATOM   1442  CD  GLU A 182     -26.773  -0.694 -30.697  1.00 67.09           C  
-ATOM   1443  OE1 GLU A 182     -27.204   0.291 -31.343  1.00 50.44           O  
-ATOM   1444  OE2 GLU A 182     -25.573  -0.820 -30.354  1.00 72.72           O  
-ATOM   1445  N   LEU A 183     -30.003   0.546 -27.146  1.00 33.70           N  
-ATOM   1446  CA  LEU A 183     -30.576   1.832 -26.794  1.00 32.30           C  
-ATOM   1447  C   LEU A 183     -29.837   2.484 -25.642  1.00 39.17           C  
-ATOM   1448  O   LEU A 183     -29.466   3.660 -25.718  1.00 37.50           O  
-ATOM   1449  CB  LEU A 183     -32.039   1.668 -26.403  1.00 40.34           C  
-ATOM   1450  CG  LEU A 183     -32.919   2.896 -26.670  1.00 43.82           C  
-ATOM   1451  CD1 LEU A 183     -34.145   2.838 -25.767  1.00 50.73           C  
-ATOM   1452  CD2 LEU A 183     -32.172   4.230 -26.498  1.00 33.32           C  
-ATOM   1453  N   ILE A 184     -29.654   1.730 -24.563  1.00 39.26           N  
-ATOM   1454  CA  ILE A 184     -28.898   2.209 -23.400  1.00 34.45           C  
-ATOM   1455  C   ILE A 184     -27.472   2.629 -23.799  1.00 36.13           C  
-ATOM   1456  O   ILE A 184     -27.045   3.768 -23.549  1.00 29.76           O  
-ATOM   1457  CB  ILE A 184     -28.864   1.126 -22.282  1.00 36.53           C  
-ATOM   1458  CG1 ILE A 184     -30.301   0.736 -21.895  1.00 36.27           C  
-ATOM   1459  CG2 ILE A 184     -28.054   1.608 -21.081  1.00 36.90           C  
-ATOM   1460  CD1 ILE A 184     -30.407  -0.289 -20.796  1.00 32.64           C  
-ATOM   1461  N   LYS A 185     -26.757   1.697 -24.431  1.00 35.09           N  
-ATOM   1462  CA  LYS A 185     -25.424   1.935 -24.979  1.00 37.16           C  
-ATOM   1463  C   LYS A 185     -25.329   3.270 -25.718  1.00 34.12           C  
-ATOM   1464  O   LYS A 185     -24.304   3.947 -25.685  1.00 25.98           O  
-ATOM   1465  CB  LYS A 185     -25.057   0.792 -25.924  1.00 47.36           C  
-ATOM   1466  CG  LYS A 185     -23.592   0.739 -26.338  1.00 43.42           C  
-ATOM   1467  CD  LYS A 185     -23.374   1.372 -27.706  1.00 47.98           C  
-ATOM   1468  CE  LYS A 185     -22.167   0.767 -28.426  1.00 58.26           C  
-ATOM   1469  NZ  LYS A 185     -22.416  -0.607 -28.956  1.00 55.49           N  
-ATOM   1470  N   ASN A 186     -26.406   3.652 -26.380  1.00 34.06           N  
-ATOM   1471  CA  ASN A 186     -26.423   4.926 -27.086  1.00 38.15           C  
-ATOM   1472  C   ASN A 186     -26.610   6.170 -26.223  1.00 41.45           C  
-ATOM   1473  O   ASN A 186     -25.967   7.193 -26.466  1.00 49.21           O  
-ATOM   1474  CB  ASN A 186     -27.451   4.905 -28.207  1.00 38.89           C  
-ATOM   1475  CG  ASN A 186     -26.981   4.090 -29.382  1.00 45.90           C  
-ATOM   1476  OD1 ASN A 186     -25.775   3.997 -29.626  1.00 44.79           O  
-ATOM   1477  ND2 ASN A 186     -27.919   3.485 -30.117  1.00 44.95           N  
-ATOM   1478  N   ILE A 187     -27.494   6.109 -25.231  1.00 36.47           N  
-ATOM   1479  CA  ILE A 187     -27.650   7.259 -24.344  1.00 39.26           C  
-ATOM   1480  C   ILE A 187     -26.424   7.379 -23.450  1.00 42.42           C  
-ATOM   1481  O   ILE A 187     -26.009   8.485 -23.085  1.00 34.36           O  
-ATOM   1482  CB  ILE A 187     -28.948   7.213 -23.496  1.00 44.35           C  
-ATOM   1483  CG1 ILE A 187     -29.405   5.772 -23.277  1.00 39.24           C  
-ATOM   1484  CG2 ILE A 187     -30.061   7.983 -24.193  1.00 58.69           C  
-ATOM   1485  CD1 ILE A 187     -30.914   5.644 -23.172  1.00 38.08           C  
-ATOM   1486  N   VAL A 188     -25.819   6.241 -23.121  1.00 38.13           N  
-ATOM   1487  CA  VAL A 188     -24.646   6.284 -22.270  1.00 35.58           C  
-ATOM   1488  C   VAL A 188     -23.505   7.026 -22.941  1.00 37.22           C  
-ATOM   1489  O   VAL A 188     -22.997   7.995 -22.382  1.00 39.11           O  
-ATOM   1490  CB  VAL A 188     -24.181   4.900 -21.821  1.00 33.81           C  
-ATOM   1491  CG1 VAL A 188     -22.892   5.034 -20.984  1.00 31.99           C  
-ATOM   1492  CG2 VAL A 188     -25.280   4.215 -21.030  1.00 27.30           C  
-ATOM   1493  N   ILE A 189     -23.106   6.589 -24.134  1.00 40.55           N  
-ATOM   1494  CA  ILE A 189     -21.997   7.260 -24.819  1.00 46.40           C  
-ATOM   1495  C   ILE A 189     -22.333   8.718 -25.068  1.00 43.30           C  
-ATOM   1496  O   ILE A 189     -21.438   9.562 -25.115  1.00 45.25           O  
-ATOM   1497  CB  ILE A 189     -21.552   6.604 -26.158  1.00 33.12           C  
-ATOM   1498  CG1 ILE A 189     -22.635   6.762 -27.207  1.00 50.67           C  
-ATOM   1499  CG2 ILE A 189     -21.173   5.140 -25.970  1.00 36.51           C  
-ATOM   1500  CD1 ILE A 189     -22.671   5.624 -28.217  1.00 61.13           C  
-ATOM   1501  N   GLU A 190     -23.614   9.037 -25.212  1.00 33.30           N  
-ATOM   1502  CA  GLU A 190     -23.942  10.436 -25.384  1.00 38.36           C  
-ATOM   1503  C   GLU A 190     -23.743  11.246 -24.102  1.00 47.24           C  
-ATOM   1504  O   GLU A 190     -23.143  12.326 -24.118  1.00 45.19           O  
-ATOM   1505  CB  GLU A 190     -25.341  10.640 -25.920  1.00 36.21           C  
-ATOM   1506  CG  GLU A 190     -25.603  12.119 -26.103  1.00 41.79           C  
-ATOM   1507  CD  GLU A 190     -27.005  12.423 -26.529  1.00 71.30           C  
-ATOM   1508  OE1 GLU A 190     -27.724  11.483 -26.955  1.00 66.01           O  
-ATOM   1509  OE2 GLU A 190     -27.376  13.615 -26.433  1.00 86.16           O  
-ATOM   1510  N   ALA A 191     -24.254  10.724 -22.991  1.00 48.76           N  
-ATOM   1511  CA  ALA A 191     -24.041  11.349 -21.694  1.00 37.24           C  
-ATOM   1512  C   ALA A 191     -22.572  11.700 -21.532  1.00 36.95           C  
-ATOM   1513  O   ALA A 191     -22.235  12.737 -20.973  1.00 37.04           O  
-ATOM   1514  CB  ALA A 191     -24.471  10.420 -20.611  1.00 27.66           C  
-ATOM   1515  N   ILE A 192     -21.703  10.835 -22.048  1.00 34.77           N  
-ATOM   1516  CA  ILE A 192     -20.261  10.970 -21.848  1.00 39.10           C  
-ATOM   1517  C   ILE A 192     -19.571  12.035 -22.715  1.00 44.24           C  
-ATOM   1518  O   ILE A 192     -18.622  12.684 -22.263  1.00 40.09           O  
-ATOM   1519  CB  ILE A 192     -19.545   9.630 -22.061  1.00 33.98           C  
-ATOM   1520  CG1 ILE A 192     -20.045   8.595 -21.064  1.00 35.16           C  
-ATOM   1521  CG2 ILE A 192     -18.042   9.794 -21.942  1.00 23.35           C  
-ATOM   1522  CD1 ILE A 192     -19.288   7.277 -21.155  1.00 44.89           C  
-ATOM   1523  N   HIS A 193     -20.016  12.207 -23.958  1.00 43.88           N  
-ATOM   1524  CA  HIS A 193     -19.418  13.243 -24.804  1.00 51.40           C  
-ATOM   1525  C   HIS A 193     -20.020  14.614 -24.503  1.00 51.24           C  
-ATOM   1526  O   HIS A 193     -19.339  15.635 -24.611  1.00 60.02           O  
-ATOM   1527  CB  HIS A 193     -19.509  12.910 -26.305  1.00 56.85           C  
-ATOM   1528  CG  HIS A 193     -18.775  11.663 -26.696  1.00 68.64           C  
-ATOM   1529  ND1 HIS A 193     -19.106  10.921 -27.811  1.00 75.06           N  
-ATOM   1530  CD2 HIS A 193     -17.745  11.014 -26.104  1.00 61.25           C  
-ATOM   1531  CE1 HIS A 193     -18.303   9.875 -27.894  1.00 81.39           C  
-ATOM   1532  NE2 HIS A 193     -17.470   9.906 -26.869  1.00 74.00           N  
-ATOM   1533  N   THR A 194     -21.280  14.628 -24.085  1.00 44.77           N  
-ATOM   1534  CA  THR A 194     -21.988  15.878 -23.835  1.00 51.21           C  
-ATOM   1535  C   THR A 194     -21.843  16.449 -22.398  1.00 46.97           C  
-ATOM   1536  O   THR A 194     -22.556  17.380 -22.023  1.00 55.37           O  
-ATOM   1537  CB  THR A 194     -23.501  15.752 -24.256  1.00 59.93           C  
-ATOM   1538  OG1 THR A 194     -24.269  15.095 -23.237  1.00 59.16           O  
-ATOM   1539  CG2 THR A 194     -23.629  14.952 -25.543  1.00 51.04           C  
-ATOM   1540  N   VAL A 195     -20.926  15.909 -21.601  1.00 44.83           N  
-ATOM   1541  CA  VAL A 195     -20.779  16.346 -20.200  1.00 61.54           C  
-ATOM   1542  C   VAL A 195     -19.896  17.593 -20.036  1.00 68.10           C  
-ATOM   1543  O   VAL A 195     -18.847  17.698 -20.673  1.00 65.56           O  
-ATOM   1544  CB  VAL A 195     -20.213  15.204 -19.292  1.00 45.45           C  
-ATOM   1545  CG1 VAL A 195     -19.386  15.769 -18.167  1.00 40.29           C  
-ATOM   1546  CG2 VAL A 195     -21.328  14.365 -18.725  1.00 45.87           C  
-ATOM   1547  N   THR A 196     -20.311  18.529 -19.180  1.00 65.95           N  
-ATOM   1548  CA  THR A 196     -19.484  19.707 -18.879  1.00 78.80           C  
-ATOM   1549  C   THR A 196     -19.615  20.235 -17.454  1.00 74.76           C  
-ATOM   1550  O   THR A 196     -20.652  20.067 -16.804  1.00 61.12           O  
-ATOM   1551  CB  THR A 196     -19.804  20.906 -19.804  1.00 72.44           C  
-ATOM   1552  OG1 THR A 196     -21.226  21.035 -19.953  1.00 64.31           O  
-ATOM   1553  CG2 THR A 196     -19.140  20.741 -21.164  1.00 74.89           C  
-ATOM   1554  N   GLY A 197     -18.557  20.898 -16.992  1.00 68.56           N  
-ATOM   1555  CA  GLY A 197     -18.617  21.687 -15.777  1.00 60.30           C  
-ATOM   1556  C   GLY A 197     -18.164  20.947 -14.540  1.00 66.60           C  
-ATOM   1557  O   GLY A 197     -17.470  19.932 -14.633  1.00 62.73           O  
-ATOM   1558  N   PRO A 198     -18.568  21.447 -13.362  1.00 65.96           N  
-ATOM   1559  CA  PRO A 198     -18.195  20.830 -12.099  1.00 55.18           C  
-ATOM   1560  C   PRO A 198     -19.134  19.682 -11.797  1.00 54.91           C  
-ATOM   1561  O   PRO A 198     -20.279  19.700 -12.255  1.00 49.59           O  
-ATOM   1562  CB  PRO A 198     -18.465  21.956 -11.116  1.00 58.24           C  
-ATOM   1563  CG  PRO A 198     -19.743  22.535 -11.633  1.00 58.12           C  
-ATOM   1564  CD  PRO A 198     -19.594  22.489 -13.155  1.00 66.44           C  
-ATOM   1565  N   VAL A 199     -18.658  18.701 -11.040  1.00 50.40           N  
-ATOM   1566  CA  VAL A 199     -19.540  17.691 -10.480  1.00 51.44           C  
-ATOM   1567  C   VAL A 199     -20.587  18.345  -9.578  1.00 52.18           C  
-ATOM   1568  O   VAL A 199     -20.258  19.123  -8.686  1.00 39.06           O  
-ATOM   1569  CB  VAL A 199     -18.750  16.665  -9.679  1.00 43.38           C  
-ATOM   1570  CG1 VAL A 199     -19.626  15.446  -9.378  1.00 34.63           C  
-ATOM   1571  CG2 VAL A 199     -17.499  16.278 -10.451  1.00 38.27           C  
-ATOM   1572  N   GLY A 200     -21.856  18.040  -9.818  1.00 58.54           N  
-ATOM   1573  CA  GLY A 200     -22.912  18.589  -8.990  1.00 52.57           C  
-ATOM   1574  C   GLY A 200     -22.993  17.908  -7.633  1.00 52.04           C  
-ATOM   1575  O   GLY A 200     -22.475  16.803  -7.451  1.00 50.80           O  
-ATOM   1576  N   GLN A 201     -23.638  18.569  -6.675  1.00 51.53           N  
-ATOM   1577  CA  GLN A 201     -23.848  17.987  -5.360  1.00 38.75           C  
-ATOM   1578  C   GLN A 201     -25.314  17.647  -5.247  1.00 38.25           C  
-ATOM   1579  O   GLN A 201     -26.172  18.462  -5.563  1.00 51.75           O  
-ATOM   1580  CB  GLN A 201     -23.419  18.967  -4.278  1.00 45.75           C  
-ATOM   1581  CG  GLN A 201     -22.098  19.643  -4.608  1.00 56.43           C  
-ATOM   1582  CD  GLN A 201     -21.831  20.838  -3.742  1.00 60.83           C  
-ATOM   1583  OE1 GLN A 201     -21.816  21.975  -4.221  1.00 60.38           O  
-ATOM   1584  NE2 GLN A 201     -21.633  20.596  -2.451  1.00 55.63           N  
-ATOM   1585  N   LEU A 202     -25.601  16.426  -4.829  1.00 32.80           N  
-ATOM   1586  CA  LEU A 202     -26.966  15.937  -4.850  1.00 34.93           C  
-ATOM   1587  C   LEU A 202     -27.856  16.629  -3.806  1.00 43.54           C  
-ATOM   1588  O   LEU A 202     -27.437  16.860  -2.667  1.00 46.53           O  
-ATOM   1589  CB  LEU A 202     -26.982  14.414  -4.688  1.00 34.75           C  
-ATOM   1590  CG  LEU A 202     -28.350  13.717  -4.699  1.00 36.28           C  
-ATOM   1591  CD1 LEU A 202     -29.107  14.024  -5.975  1.00 33.60           C  
-ATOM   1592  CD2 LEU A 202     -28.187  12.222  -4.530  1.00 38.10           C  
-ATOM   1593  N   TRP A 203     -29.072  16.980  -4.224  1.00 41.47           N  
-ATOM   1594  CA  TRP A 203     -30.090  17.534  -3.338  1.00 44.06           C  
-ATOM   1595  C   TRP A 203     -29.594  18.618  -2.405  1.00 56.67           C  
-ATOM   1596  O   TRP A 203     -29.893  18.615  -1.206  1.00 43.94           O  
-ATOM   1597  CB  TRP A 203     -30.716  16.451  -2.493  1.00 37.29           C  
-ATOM   1598  CG  TRP A 203     -31.529  15.535  -3.259  1.00 37.61           C  
-ATOM   1599  CD1 TRP A 203     -32.406  15.854  -4.240  1.00 37.33           C  
-ATOM   1600  CD2 TRP A 203     -31.582  14.107  -3.106  1.00 43.93           C  
-ATOM   1601  NE1 TRP A 203     -33.003  14.711  -4.723  1.00 41.33           N  
-ATOM   1602  CE2 TRP A 203     -32.510  13.627  -4.042  1.00 43.47           C  
-ATOM   1603  CE3 TRP A 203     -30.925  13.195  -2.274  1.00 39.65           C  
-ATOM   1604  CZ2 TRP A 203     -32.807  12.260  -4.167  1.00 45.63           C  
-ATOM   1605  CZ3 TRP A 203     -31.213  11.845  -2.400  1.00 37.36           C  
-ATOM   1606  CH2 TRP A 203     -32.149  11.390  -3.334  1.00 43.64           C  
-ATOM   1607  N   MET A 204     -28.840  19.554  -2.949  1.00 63.85           N  
-ATOM   1608  CA  MET A 204     -28.463  20.704  -2.165  1.00 61.25           C  
-ATOM   1609  C   MET A 204     -28.932  21.980  -2.845  1.00 91.68           C  
-ATOM   1610  O   MET A 204     -28.884  22.099  -4.078  1.00 88.52           O  
-ATOM   1611  CB  MET A 204     -26.965  20.692  -1.913  1.00 51.96           C  
-ATOM   1612  CG  MET A 204     -26.590  19.763  -0.781  1.00 49.18           C  
-ATOM   1613  SD  MET A 204     -24.848  19.899  -0.470  1.00 68.07           S  
-ATOM   1614  CE  MET A 204     -24.508  21.458  -1.306  1.00 58.63           C  
-ATOM   1615  OXT MET A 204     -29.404  22.894  -2.161  1.00 92.95           O  
-TER    1616      MET A 204                                                      
-ATOM   1617  N   SER B   2       4.969  -2.132  -2.797  1.00 57.74           N  
-ATOM   1618  CA  SER B   2       3.586  -2.362  -2.347  1.00 74.09           C  
-ATOM   1619  C   SER B   2       2.564  -1.990  -3.420  1.00 69.59           C  
-ATOM   1620  O   SER B   2       1.516  -1.382  -3.146  1.00 55.51           O  
-ATOM   1621  CB  SER B   2       3.269  -1.616  -1.048  1.00 60.92           C  
-ATOM   1622  OG  SER B   2       1.958  -1.939  -0.601  1.00 67.49           O  
-ATOM   1623  N   ARG B   3       2.885  -2.361  -4.649  1.00 46.85           N  
-ATOM   1624  CA  ARG B   3       1.959  -2.224  -5.751  1.00 47.56           C  
-ATOM   1625  C   ARG B   3       0.694  -3.063  -5.550  1.00 41.95           C  
-ATOM   1626  O   ARG B   3       0.549  -3.790  -4.567  1.00 36.48           O  
-ATOM   1627  CB  ARG B   3       2.656  -2.698  -7.017  1.00 38.84           C  
-ATOM   1628  CG  ARG B   3       3.539  -3.931  -6.791  1.00 40.99           C  
-ATOM   1629  CD  ARG B   3       4.090  -4.465  -8.087  1.00 46.21           C  
-ATOM   1630  NE  ARG B   3       3.518  -5.750  -8.454  1.00 43.27           N  
-ATOM   1631  CZ  ARG B   3       4.179  -6.888  -8.342  1.00 44.52           C  
-ATOM   1632  NH1 ARG B   3       3.618  -8.026  -8.698  1.00 45.75           N  
-ATOM   1633  NH2 ARG B   3       5.416  -6.878  -7.882  1.00 58.31           N  
-ATOM   1634  N   GLY B   4      -0.216  -2.958  -6.503  1.00 28.46           N  
-ATOM   1635  CA  GLY B   4      -1.299  -3.908  -6.596  1.00 32.87           C  
-ATOM   1636  C   GLY B   4      -0.760  -5.208  -7.170  1.00 38.75           C  
-ATOM   1637  O   GLY B   4       0.396  -5.293  -7.585  1.00 29.78           O  
-ATOM   1638  N   ALA B   5      -1.601  -6.235  -7.186  1.00 35.25           N  
-ATOM   1639  CA  ALA B   5      -1.222  -7.518  -7.753  1.00 29.96           C  
-ATOM   1640  C   ALA B   5      -1.850  -7.650  -9.135  1.00 37.09           C  
-ATOM   1641  O   ALA B   5      -2.960  -7.165  -9.378  1.00 35.12           O  
-ATOM   1642  CB  ALA B   5      -1.687  -8.643  -6.857  1.00 28.99           C  
-ATOM   1643  N   LEU B   6      -1.133  -8.283 -10.053  1.00 36.95           N  
-ATOM   1644  CA  LEU B   6      -1.707  -8.578 -11.350  1.00 31.64           C  
-ATOM   1645  C   LEU B   6      -2.242  -9.997 -11.338  1.00 30.16           C  
-ATOM   1646  O   LEU B   6      -1.470 -10.958 -11.379  1.00 31.97           O  
-ATOM   1647  CB  LEU B   6      -0.671  -8.418 -12.459  1.00 34.81           C  
-ATOM   1648  CG  LEU B   6      -1.249  -8.801 -13.824  1.00 37.39           C  
-ATOM   1649  CD1 LEU B   6      -2.522  -7.973 -14.112  1.00 28.07           C  
-ATOM   1650  CD2 LEU B   6      -0.203  -8.674 -14.931  1.00 31.45           C  
-ATOM   1651  N   ILE B   7      -3.563 -10.124 -11.292  1.00 23.78           N  
-ATOM   1652  CA  ILE B   7      -4.184 -11.433 -11.223  1.00 27.12           C  
-ATOM   1653  C   ILE B   7      -4.919 -11.771 -12.518  1.00 30.32           C  
-ATOM   1654  O   ILE B   7      -5.805 -11.034 -12.956  1.00 30.80           O  
-ATOM   1655  CB  ILE B   7      -5.108 -11.507  -9.994  1.00 27.23           C  
-ATOM   1656  CG1 ILE B   7      -4.288 -11.216  -8.740  1.00 25.65           C  
-ATOM   1657  CG2 ILE B   7      -5.786 -12.859  -9.873  1.00 26.09           C  
-ATOM   1658  CD1 ILE B   7      -5.093 -11.207  -7.502  1.00 35.95           C  
-ATOM   1659  N   VAL B   8      -4.546 -12.881 -13.145  1.00 25.57           N  
-ATOM   1660  CA  VAL B   8      -5.173 -13.251 -14.411  1.00 26.56           C  
-ATOM   1661  C   VAL B   8      -5.976 -14.536 -14.346  1.00 33.68           C  
-ATOM   1662  O   VAL B   8      -5.498 -15.549 -13.838  1.00 33.56           O  
-ATOM   1663  CB  VAL B   8      -4.126 -13.450 -15.469  1.00 32.24           C  
-ATOM   1664  CG1 VAL B   8      -4.776 -13.966 -16.725  1.00 28.79           C  
-ATOM   1665  CG2 VAL B   8      -3.370 -12.141 -15.702  1.00 30.20           C  
-ATOM   1666  N   PHE B   9      -7.194 -14.498 -14.879  1.00 35.52           N  
-ATOM   1667  CA  PHE B   9      -8.028 -15.698 -14.994  1.00 29.52           C  
-ATOM   1668  C   PHE B   9      -7.892 -16.307 -16.385  1.00 27.91           C  
-ATOM   1669  O   PHE B   9      -8.000 -15.592 -17.380  1.00 29.16           O  
-ATOM   1670  CB  PHE B   9      -9.490 -15.349 -14.736  1.00 27.34           C  
-ATOM   1671  CG  PHE B   9      -9.866 -15.377 -13.290  1.00 36.67           C  
-ATOM   1672  CD1 PHE B   9      -9.740 -14.246 -12.499  1.00 33.06           C  
-ATOM   1673  CD2 PHE B   9     -10.347 -16.548 -12.712  1.00 40.40           C  
-ATOM   1674  CE1 PHE B   9     -10.093 -14.287 -11.159  1.00 33.79           C  
-ATOM   1675  CE2 PHE B   9     -10.690 -16.596 -11.367  1.00 35.14           C  
-ATOM   1676  CZ  PHE B   9     -10.567 -15.469 -10.591  1.00 35.65           C  
-ATOM   1677  N   GLU B  10      -7.632 -17.611 -16.452  1.00 33.31           N  
-ATOM   1678  CA  GLU B  10      -7.623 -18.344 -17.724  1.00 29.59           C  
-ATOM   1679  C   GLU B  10      -8.491 -19.592 -17.642  1.00 35.50           C  
-ATOM   1680  O   GLU B  10      -8.969 -19.971 -16.572  1.00 37.38           O  
-ATOM   1681  CB  GLU B  10      -6.206 -18.743 -18.157  1.00 23.66           C  
-ATOM   1682  CG  GLU B  10      -5.277 -17.574 -18.510  1.00 30.23           C  
-ATOM   1683  CD  GLU B  10      -5.552 -16.980 -19.883  1.00 29.24           C  
-ATOM   1684  OE1 GLU B  10      -6.492 -17.462 -20.547  1.00 28.51           O  
-ATOM   1685  OE2 GLU B  10      -4.833 -16.033 -20.291  1.00 23.93           O  
-ATOM   1686  N   GLY B  11      -8.673 -20.238 -18.788  1.00 46.56           N  
-ATOM   1687  CA  GLY B  11      -9.501 -21.429 -18.893  1.00 42.09           C  
-ATOM   1688  C   GLY B  11     -10.177 -21.482 -20.252  1.00 38.14           C  
-ATOM   1689  O   GLY B  11     -10.089 -20.521 -21.025  1.00 34.14           O  
-ATOM   1690  N   LEU B  12     -10.848 -22.599 -20.546  1.00 37.70           N  
-ATOM   1691  CA  LEU B  12     -11.561 -22.747 -21.812  1.00 35.88           C  
-ATOM   1692  C   LEU B  12     -12.765 -21.814 -21.820  1.00 38.53           C  
-ATOM   1693  O   LEU B  12     -13.037 -21.154 -20.816  1.00 41.50           O  
-ATOM   1694  CB  LEU B  12     -12.000 -24.191 -22.025  1.00 30.14           C  
-ATOM   1695  CG  LEU B  12     -10.887 -25.239 -22.006  1.00 36.07           C  
-ATOM   1696  CD1 LEU B  12     -11.442 -26.625 -22.262  1.00 39.14           C  
-ATOM   1697  CD2 LEU B  12      -9.788 -24.919 -23.008  1.00 33.99           C  
-ATOM   1698  N   ASP B  13     -13.464 -21.723 -22.949  1.00 34.82           N  
-ATOM   1699  CA  ASP B  13     -14.729 -20.994 -22.976  1.00 40.80           C  
-ATOM   1700  C   ASP B  13     -15.747 -21.727 -22.104  1.00 54.88           C  
-ATOM   1701  O   ASP B  13     -15.734 -22.964 -22.030  1.00 63.28           O  
-ATOM   1702  CB  ASP B  13     -15.283 -20.883 -24.393  1.00 55.13           C  
-ATOM   1703  CG  ASP B  13     -14.936 -19.579 -25.059  1.00 42.41           C  
-ATOM   1704  OD1 ASP B  13     -15.838 -18.722 -25.205  1.00 35.04           O  
-ATOM   1705  OD2 ASP B  13     -13.766 -19.427 -25.449  1.00 42.52           O  
-ATOM   1706  N   LYS B  14     -16.621 -20.969 -21.441  1.00 46.39           N  
-ATOM   1707  CA  LYS B  14     -17.664 -21.557 -20.603  1.00 44.62           C  
-ATOM   1708  C   LYS B  14     -17.124 -22.234 -19.335  1.00 45.22           C  
-ATOM   1709  O   LYS B  14     -17.822 -23.029 -18.699  1.00 56.31           O  
-ATOM   1710  CB  LYS B  14     -18.499 -22.553 -21.419  1.00 50.69           C  
-ATOM   1711  CG  LYS B  14     -18.891 -22.043 -22.803  1.00 51.22           C  
-ATOM   1712  CD  LYS B  14     -19.898 -20.894 -22.723  1.00 50.48           C  
-ATOM   1713  CE  LYS B  14     -20.193 -20.290 -24.099  1.00 51.85           C  
-ATOM   1714  NZ  LYS B  14     -21.133 -19.131 -24.012  1.00 56.64           N  
-ATOM   1715  N   SER B  15     -15.883 -21.924 -18.982  1.00 42.63           N  
-ATOM   1716  CA  SER B  15     -15.291 -22.417 -17.747  1.00 37.59           C  
-ATOM   1717  C   SER B  15     -15.733 -21.543 -16.585  1.00 36.88           C  
-ATOM   1718  O   SER B  15     -15.369 -21.797 -15.440  1.00 39.43           O  
-ATOM   1719  CB  SER B  15     -13.772 -22.381 -17.822  1.00 38.32           C  
-ATOM   1720  OG  SER B  15     -13.328 -21.037 -17.892  1.00 43.18           O  
-ATOM   1721  N   GLY B  16     -16.500 -20.503 -16.886  1.00 39.22           N  
-ATOM   1722  CA  GLY B  16     -17.059 -19.642 -15.859  1.00 40.03           C  
-ATOM   1723  C   GLY B  16     -16.101 -18.637 -15.235  1.00 38.55           C  
-ATOM   1724  O   GLY B  16     -16.335 -18.123 -14.141  1.00 29.01           O  
-ATOM   1725  N   LYS B  17     -15.016 -18.325 -15.927  1.00 45.08           N  
-ATOM   1726  CA  LYS B  17     -14.090 -17.370 -15.361  1.00 40.98           C  
-ATOM   1727  C   LYS B  17     -14.690 -15.983 -15.220  1.00 34.53           C  
-ATOM   1728  O   LYS B  17     -14.275 -15.224 -14.339  1.00 35.82           O  
-ATOM   1729  CB  LYS B  17     -12.754 -17.355 -16.100  1.00 35.46           C  
-ATOM   1730  CG  LYS B  17     -12.856 -17.368 -17.573  1.00 40.42           C  
-ATOM   1731  CD  LYS B  17     -11.466 -17.499 -18.192  1.00 36.91           C  
-ATOM   1732  CE  LYS B  17     -11.585 -17.578 -19.711  1.00 40.98           C  
-ATOM   1733  NZ  LYS B  17     -12.717 -16.718 -20.220  1.00 55.39           N  
-ATOM   1734  N   THR B  18     -15.671 -15.657 -16.058  1.00 33.38           N  
-ATOM   1735  CA  THR B  18     -16.429 -14.397 -15.899  1.00 47.38           C  
-ATOM   1736  C   THR B  18     -17.234 -14.362 -14.565  1.00 41.31           C  
-ATOM   1737  O   THR B  18     -17.206 -13.382 -13.826  1.00 29.38           O  
-ATOM   1738  CB  THR B  18     -17.332 -14.067 -17.148  1.00 42.88           C  
-ATOM   1739  OG1 THR B  18     -16.605 -14.296 -18.363  1.00 55.18           O  
-ATOM   1740  CG2 THR B  18     -17.756 -12.616 -17.144  1.00 39.68           C  
-ATOM   1741  N   THR B  19     -17.930 -15.444 -14.251  1.00 39.32           N  
-ATOM   1742  CA  THR B  19     -18.564 -15.572 -12.950  1.00 36.10           C  
-ATOM   1743  C   THR B  19     -17.576 -15.295 -11.822  1.00 43.74           C  
-ATOM   1744  O   THR B  19     -17.786 -14.413 -10.982  1.00 43.53           O  
-ATOM   1745  CB  THR B  19     -19.098 -16.989 -12.733  1.00 41.71           C  
-ATOM   1746  OG1 THR B  19     -19.758 -17.440 -13.920  1.00 61.59           O  
-ATOM   1747  CG2 THR B  19     -20.068 -17.015 -11.570  1.00 40.96           C  
-ATOM   1748  N   GLN B  20     -16.501 -16.072 -11.789  1.00 42.25           N  
-ATOM   1749  CA  GLN B  20     -15.517 -15.944 -10.719  1.00 44.21           C  
-ATOM   1750  C   GLN B  20     -14.877 -14.556 -10.626  1.00 44.18           C  
-ATOM   1751  O   GLN B  20     -14.561 -14.091  -9.528  1.00 46.53           O  
-ATOM   1752  CB  GLN B  20     -14.456 -17.024 -10.851  1.00 36.61           C  
-ATOM   1753  CG  GLN B  20     -14.997 -18.403 -10.545  1.00 35.54           C  
-ATOM   1754  CD  GLN B  20     -15.447 -18.537  -9.113  1.00 37.88           C  
-ATOM   1755  OE1 GLN B  20     -15.041 -17.757  -8.250  1.00 47.02           O  
-ATOM   1756  NE2 GLN B  20     -16.280 -19.533  -8.845  1.00 37.65           N  
-ATOM   1757  N   CYS B  21     -14.688 -13.900 -11.768  1.00 38.00           N  
-ATOM   1758  CA  CYS B  21     -14.291 -12.498 -11.763  1.00 37.73           C  
-ATOM   1759  C   CYS B  21     -15.335 -11.648 -11.061  1.00 42.62           C  
-ATOM   1760  O   CYS B  21     -15.005 -10.746 -10.284  1.00 43.71           O  
-ATOM   1761  CB  CYS B  21     -14.048 -11.972 -13.172  1.00 37.08           C  
-ATOM   1762  SG  CYS B  21     -12.387 -12.322 -13.805  1.00 34.56           S  
-ATOM   1763  N   MET B  22     -16.600 -11.943 -11.325  1.00 46.82           N  
-ATOM   1764  CA  MET B  22     -17.686 -11.250 -10.651  1.00 50.57           C  
-ATOM   1765  C   MET B  22     -17.606 -11.405  -9.138  1.00 41.27           C  
-ATOM   1766  O   MET B  22     -17.783 -10.432  -8.421  1.00 41.04           O  
-ATOM   1767  CB  MET B  22     -19.036 -11.721 -11.184  1.00 53.78           C  
-ATOM   1768  CG  MET B  22     -19.297 -11.251 -12.588  1.00 46.39           C  
-ATOM   1769  SD  MET B  22     -19.396  -9.461 -12.618  1.00 84.51           S  
-ATOM   1770  CE  MET B  22     -20.911  -9.203 -11.678  1.00 74.46           C  
-ATOM   1771  N   ASN B  23     -17.335 -12.612  -8.651  1.00 43.84           N  
-ATOM   1772  CA  ASN B  23     -17.153 -12.811  -7.200  1.00 53.81           C  
-ATOM   1773  C   ASN B  23     -16.076 -11.895  -6.620  1.00 45.77           C  
-ATOM   1774  O   ASN B  23     -16.325 -11.145  -5.675  1.00 37.95           O  
-ATOM   1775  CB  ASN B  23     -16.842 -14.274  -6.846  1.00 53.56           C  
-ATOM   1776  CG  ASN B  23     -18.034 -15.189  -7.059  1.00 69.67           C  
-ATOM   1777  OD1 ASN B  23     -19.135 -14.725  -7.352  1.00 83.49           O  
-ATOM   1778  ND2 ASN B  23     -17.822 -16.494  -6.917  1.00 69.14           N  
-ATOM   1779  N   ILE B  24     -14.879 -11.948  -7.196  1.00 42.35           N  
-ATOM   1780  CA  ILE B  24     -13.793 -11.142  -6.681  1.00 37.28           C  
-ATOM   1781  C   ILE B  24     -14.172  -9.670  -6.617  1.00 31.83           C  
-ATOM   1782  O   ILE B  24     -13.836  -8.988  -5.671  1.00 31.52           O  
-ATOM   1783  CB  ILE B  24     -12.488 -11.377  -7.455  1.00 30.91           C  
-ATOM   1784  CG1 ILE B  24     -11.701 -12.511  -6.800  1.00 33.18           C  
-ATOM   1785  CG2 ILE B  24     -11.610 -10.158  -7.396  1.00 34.29           C  
-ATOM   1786  CD1 ILE B  24     -12.502 -13.770  -6.565  1.00 46.12           C  
-ATOM   1787  N   MET B  25     -14.901  -9.192  -7.610  1.00 37.32           N  
-ATOM   1788  CA  MET B  25     -15.283  -7.782  -7.656  1.00 43.92           C  
-ATOM   1789  C   MET B  25     -16.265  -7.387  -6.546  1.00 45.43           C  
-ATOM   1790  O   MET B  25     -16.302  -6.237  -6.077  1.00 42.89           O  
-ATOM   1791  CB  MET B  25     -15.865  -7.438  -9.032  1.00 40.44           C  
-ATOM   1792  CG  MET B  25     -14.837  -7.509 -10.176  1.00 50.46           C  
-ATOM   1793  SD  MET B  25     -13.251  -6.681  -9.842  1.00 66.70           S  
-ATOM   1794  CE  MET B  25     -13.780  -4.980  -9.618  1.00 44.55           C  
-ATOM   1795  N   GLU B  26     -17.058  -8.360  -6.127  1.00 41.33           N  
-ATOM   1796  CA  GLU B  26     -18.024  -8.148  -5.069  1.00 41.06           C  
-ATOM   1797  C   GLU B  26     -17.398  -8.382  -3.681  1.00 35.66           C  
-ATOM   1798  O   GLU B  26     -17.780  -7.742  -2.711  1.00 37.05           O  
-ATOM   1799  CB  GLU B  26     -19.225  -9.061  -5.304  1.00 44.30           C  
-ATOM   1800  CG  GLU B  26     -20.015  -8.715  -6.573  1.00 61.03           C  
-ATOM   1801  CD  GLU B  26     -20.722  -9.926  -7.213  1.00 84.61           C  
-ATOM   1802  OE1 GLU B  26     -20.976 -10.939  -6.510  1.00 71.38           O  
-ATOM   1803  OE2 GLU B  26     -21.025  -9.862  -8.431  1.00 77.16           O  
-ATOM   1804  N   SER B  27     -16.429  -9.287  -3.607  1.00 30.57           N  
-ATOM   1805  CA  SER B  27     -15.749  -9.621  -2.361  1.00 23.38           C  
-ATOM   1806  C   SER B  27     -14.677  -8.624  -1.890  1.00 36.82           C  
-ATOM   1807  O   SER B  27     -14.154  -8.761  -0.780  1.00 29.62           O  
-ATOM   1808  CB  SER B  27     -15.106 -10.995  -2.481  1.00 31.81           C  
-ATOM   1809  OG  SER B  27     -16.036 -12.018  -2.203  1.00 49.48           O  
-ATOM   1810  N   ILE B  28     -14.332  -7.639  -2.722  1.00 33.85           N  
-ATOM   1811  CA  ILE B  28     -13.268  -6.691  -2.385  1.00 28.55           C  
-ATOM   1812  C   ILE B  28     -13.671  -5.262  -2.695  1.00 30.48           C  
-ATOM   1813  O   ILE B  28     -14.390  -5.013  -3.653  1.00 36.61           O  
-ATOM   1814  CB  ILE B  28     -11.958  -7.031  -3.113  1.00 30.41           C  
-ATOM   1815  CG1 ILE B  28     -11.444  -8.403  -2.659  1.00 24.98           C  
-ATOM   1816  CG2 ILE B  28     -10.910  -5.959  -2.863  1.00 25.77           C  
-ATOM   1817  CD1 ILE B  28     -10.289  -8.957  -3.464  1.00 26.48           C  
-ATOM   1818  N   PRO B  29     -13.218  -4.315  -1.867  1.00 33.96           N  
-ATOM   1819  CA  PRO B  29     -13.607  -2.915  -2.069  1.00 36.40           C  
-ATOM   1820  C   PRO B  29     -13.075  -2.323  -3.388  1.00 41.81           C  
-ATOM   1821  O   PRO B  29     -11.890  -2.433  -3.715  1.00 48.04           O  
-ATOM   1822  CB  PRO B  29     -12.990  -2.217  -0.857  1.00 33.08           C  
-ATOM   1823  CG  PRO B  29     -12.883  -3.286   0.162  1.00 28.11           C  
-ATOM   1824  CD  PRO B  29     -12.460  -4.482  -0.620  1.00 29.10           C  
-ATOM   1825  N   ALA B  30     -13.967  -1.683  -4.133  1.00 35.71           N  
-ATOM   1826  CA  ALA B  30     -13.677  -1.273  -5.497  1.00 31.31           C  
-ATOM   1827  C   ALA B  30     -12.729  -0.087  -5.598  1.00 34.76           C  
-ATOM   1828  O   ALA B  30     -12.248   0.205  -6.685  1.00 39.55           O  
-ATOM   1829  CB  ALA B  30     -14.965  -0.996  -6.263  1.00 32.72           C  
-ATOM   1830  N   ASN B  31     -12.443   0.597  -4.492  1.00 36.24           N  
-ATOM   1831  CA  ASN B  31     -11.501   1.692  -4.584  1.00 34.57           C  
-ATOM   1832  C   ASN B  31     -10.072   1.168  -4.723  1.00 39.34           C  
-ATOM   1833  O   ASN B  31      -9.140   1.955  -4.882  1.00 42.86           O  
-ATOM   1834  N   THR B  32      -9.909  -0.159  -4.707  1.00 30.11           N  
-ATOM   1835  CA  THR B  32      -8.580  -0.780  -4.670  1.00 33.31           C  
-ATOM   1836  C   THR B  32      -8.362  -1.794  -5.795  1.00 40.58           C  
-ATOM   1837  O   THR B  32      -7.255  -2.294  -6.016  1.00 37.41           O  
-ATOM   1838  CB  THR B  32      -8.321  -1.500  -3.314  1.00 35.00           C  
-ATOM   1839  OG1 THR B  32      -9.037  -2.741  -3.267  1.00 28.65           O  
-ATOM   1840  CG2 THR B  32      -8.771  -0.645  -2.159  1.00 31.36           C  
-ATOM   1841  N   ILE B  33      -9.422  -2.090  -6.519  1.00 39.03           N  
-ATOM   1842  CA  ILE B  33      -9.372  -3.188  -7.460  1.00 35.52           C  
-ATOM   1843  C   ILE B  33      -9.994  -2.751  -8.787  1.00 36.74           C  
-ATOM   1844  O   ILE B  33     -10.896  -1.916  -8.796  1.00 33.39           O  
-ATOM   1845  CB  ILE B  33     -10.095  -4.393  -6.845  1.00 37.58           C  
-ATOM   1846  CG1 ILE B  33      -9.562  -5.702  -7.411  1.00 39.57           C  
-ATOM   1847  CG2 ILE B  33     -11.610  -4.258  -7.000  1.00 38.31           C  
-ATOM   1848  CD1 ILE B  33     -10.208  -6.911  -6.780  1.00 38.73           C  
-ATOM   1849  N   LYS B  34      -9.491  -3.289  -9.900  1.00 38.42           N  
-ATOM   1850  CA  LYS B  34      -9.961  -2.934 -11.253  1.00 35.59           C  
-ATOM   1851  C   LYS B  34     -10.181  -4.159 -12.149  1.00 30.46           C  
-ATOM   1852  O   LYS B  34      -9.274  -4.978 -12.324  1.00 35.29           O  
-ATOM   1853  CB  LYS B  34      -8.945  -1.996 -11.925  1.00 34.20           C  
-ATOM   1854  CG  LYS B  34      -9.173  -1.749 -13.417  1.00 26.09           C  
-ATOM   1855  CD  LYS B  34     -10.452  -0.993 -13.640  1.00 26.42           C  
-ATOM   1856  CE  LYS B  34     -10.683  -0.670 -15.098  1.00 31.90           C  
-ATOM   1857  NZ  LYS B  34     -11.917   0.163 -15.338  1.00 28.46           N  
-ATOM   1858  N   TYR B  35     -11.365  -4.275 -12.733  1.00 33.82           N  
-ATOM   1859  CA  TYR B  35     -11.667  -5.411 -13.624  1.00 34.18           C  
-ATOM   1860  C   TYR B  35     -11.331  -5.138 -15.094  1.00 35.17           C  
-ATOM   1861  O   TYR B  35     -11.728  -4.111 -15.660  1.00 30.65           O  
-ATOM   1862  CB  TYR B  35     -13.132  -5.796 -13.497  1.00 23.73           C  
-ATOM   1863  CG  TYR B  35     -13.616  -6.852 -14.463  1.00 31.43           C  
-ATOM   1864  CD1 TYR B  35     -12.977  -8.076 -14.567  1.00 39.80           C  
-ATOM   1865  CD2 TYR B  35     -14.742  -6.638 -15.247  1.00 32.38           C  
-ATOM   1866  CE1 TYR B  35     -13.435  -9.050 -15.442  1.00 39.85           C  
-ATOM   1867  CE2 TYR B  35     -15.195  -7.600 -16.113  1.00 33.55           C  
-ATOM   1868  CZ  TYR B  35     -14.542  -8.804 -16.205  1.00 39.81           C  
-ATOM   1869  OH  TYR B  35     -14.993  -9.777 -17.072  1.00 56.87           O  
-ATOM   1870  N   LEU B  36     -10.613  -6.070 -15.712  1.00 25.25           N  
-ATOM   1871  CA  LEU B  36     -10.214  -5.915 -17.101  1.00 27.40           C  
-ATOM   1872  C   LEU B  36     -10.561  -7.159 -17.928  1.00 30.01           C  
-ATOM   1873  O   LEU B  36      -9.981  -8.225 -17.711  1.00 31.65           O  
-ATOM   1874  CB  LEU B  36      -8.708  -5.668 -17.154  1.00 36.10           C  
-ATOM   1875  CG  LEU B  36      -8.231  -4.479 -17.976  1.00 39.85           C  
-ATOM   1876  CD1 LEU B  36      -6.738  -4.589 -18.328  1.00 28.22           C  
-ATOM   1877  CD2 LEU B  36      -9.092  -4.369 -19.226  1.00 37.62           C  
-ATOM   1878  N   ASN B  37     -11.496  -7.033 -18.873  1.00 33.62           N  
-ATOM   1879  CA  ASN B  37     -11.819  -8.147 -19.782  1.00 34.33           C  
-ATOM   1880  C   ASN B  37     -10.991  -8.113 -21.066  1.00 34.16           C  
-ATOM   1881  O   ASN B  37     -10.741  -7.050 -21.622  1.00 40.99           O  
-ATOM   1882  CB  ASN B  37     -13.316  -8.158 -20.145  1.00 41.62           C  
-ATOM   1883  CG  ASN B  37     -13.855  -9.575 -20.464  1.00 47.36           C  
-ATOM   1884  OD1 ASN B  37     -13.254 -10.333 -21.225  1.00 48.54           O  
-ATOM   1885  ND2 ASN B  37     -15.003  -9.921 -19.878  1.00 49.45           N  
-ATOM   1886  N   PHE B  38     -10.565  -9.281 -21.532  1.00 34.02           N  
-ATOM   1887  CA  PHE B  38      -9.974  -9.422 -22.862  1.00 26.15           C  
-ATOM   1888  C   PHE B  38     -10.686 -10.520 -23.654  1.00 23.78           C  
-ATOM   1889  O   PHE B  38     -10.982 -11.587 -23.124  1.00 32.63           O  
-ATOM   1890  CB  PHE B  38      -8.487  -9.747 -22.754  1.00 27.48           C  
-ATOM   1891  CG  PHE B  38      -7.633  -8.578 -22.365  1.00 24.53           C  
-ATOM   1892  CD1 PHE B  38      -6.973  -8.559 -21.161  1.00 33.30           C  
-ATOM   1893  CD2 PHE B  38      -7.483  -7.509 -23.213  1.00 27.12           C  
-ATOM   1894  CE1 PHE B  38      -6.180  -7.487 -20.805  1.00 30.64           C  
-ATOM   1895  CE2 PHE B  38      -6.695  -6.440 -22.870  1.00 29.75           C  
-ATOM   1896  CZ  PHE B  38      -6.041  -6.427 -21.667  1.00 25.41           C  
-ATOM   1897  N   PRO B  39     -10.969 -10.257 -24.927  1.00 35.82           N  
-ATOM   1898  CA  PRO B  39     -10.539  -9.026 -25.586  1.00 33.77           C  
-ATOM   1899  C   PRO B  39     -11.418  -7.841 -25.246  1.00 25.97           C  
-ATOM   1900  O   PRO B  39     -12.564  -7.944 -24.831  1.00 20.29           O  
-ATOM   1901  CB  PRO B  39     -10.687  -9.342 -27.085  1.00 23.72           C  
-ATOM   1902  CG  PRO B  39     -11.448 -10.663 -27.171  1.00 36.58           C  
-ATOM   1903  CD  PRO B  39     -11.894 -11.027 -25.776  1.00 37.83           C  
-ATOM   1904  N   GLN B  40     -10.827  -6.692 -25.474  1.00 28.00           N  
-ATOM   1905  CA  GLN B  40     -11.419  -5.425 -25.176  1.00 28.55           C  
-ATOM   1906  C   GLN B  40     -12.123  -5.020 -26.474  1.00 27.64           C  
-ATOM   1907  O   GLN B  40     -11.565  -4.311 -27.291  1.00 29.03           O  
-ATOM   1908  CB  GLN B  40     -10.283  -4.472 -24.767  1.00 22.39           C  
-ATOM   1909  CG  GLN B  40     -10.679  -3.217 -24.031  1.00 34.82           C  
-ATOM   1910  CD  GLN B  40     -11.407  -3.464 -22.721  1.00 37.59           C  
-ATOM   1911  OE1 GLN B  40     -11.910  -2.521 -22.099  1.00 38.85           O  
-ATOM   1912  NE2 GLN B  40     -11.479  -4.724 -22.297  1.00 30.62           N  
-ATOM   1913  N   ARG B  41     -13.346  -5.509 -26.675  1.00 33.70           N  
-ATOM   1914  CA  ARG B  41     -14.008  -5.441 -27.996  1.00 32.26           C  
-ATOM   1915  C   ARG B  41     -14.436  -4.033 -28.417  1.00 34.95           C  
-ATOM   1916  O   ARG B  41     -14.979  -3.839 -29.508  1.00 36.73           O  
-ATOM   1917  CB  ARG B  41     -15.231  -6.378 -28.077  1.00 20.54           C  
-ATOM   1918  CG  ARG B  41     -14.917  -7.851 -27.976  1.00 23.72           C  
-ATOM   1919  CD  ARG B  41     -16.187  -8.690 -28.066  1.00 29.14           C  
-ATOM   1920  NE  ARG B  41     -16.029  -9.985 -27.405  1.00 50.40           N  
-ATOM   1921  CZ  ARG B  41     -16.592 -11.117 -27.822  1.00 45.68           C  
-ATOM   1922  NH1 ARG B  41     -17.337 -11.112 -28.911  1.00 39.97           N  
-ATOM   1923  NH2 ARG B  41     -16.398 -12.254 -27.164  1.00 35.52           N  
-ATOM   1924  N   SER B  42     -14.201  -3.058 -27.556  1.00 24.54           N  
-ATOM   1925  CA  SER B  42     -14.636  -1.717 -27.853  1.00 26.41           C  
-ATOM   1926  C   SER B  42     -13.657  -1.008 -28.806  1.00 29.76           C  
-ATOM   1927  O   SER B  42     -14.058  -0.243 -29.678  1.00 32.23           O  
-ATOM   1928  CB  SER B  42     -14.878  -0.944 -26.550  1.00 27.95           C  
-ATOM   1929  OG  SER B  42     -14.231  -1.575 -25.450  1.00 38.94           O  
-ATOM   1930  N   THR B  43     -12.371  -1.301 -28.659  1.00 41.06           N  
-ATOM   1931  CA  THR B  43     -11.315  -0.602 -29.400  1.00 47.12           C  
-ATOM   1932  C   THR B  43     -11.376  -0.825 -30.908  1.00 45.63           C  
-ATOM   1933  O   THR B  43     -12.315  -1.455 -31.419  1.00 42.66           O  
-ATOM   1934  CB  THR B  43      -9.907  -1.003 -28.894  1.00 37.54           C  
-ATOM   1935  OG1 THR B  43      -9.582  -2.327 -29.344  1.00 39.88           O  
-ATOM   1936  CG2 THR B  43      -9.869  -0.961 -27.390  1.00 25.90           C  
-ATOM   1937  N   VAL B  44     -10.370  -0.304 -31.616  1.00 44.79           N  
-ATOM   1938  CA  VAL B  44     -10.286  -0.498 -33.062  1.00 46.89           C  
-ATOM   1939  C   VAL B  44      -9.990  -1.954 -33.390  1.00 37.81           C  
-ATOM   1940  O   VAL B  44     -10.575  -2.540 -34.311  1.00 32.25           O  
-ATOM   1941  CB  VAL B  44      -9.185   0.349 -33.707  1.00 45.56           C  
-ATOM   1942  CG1 VAL B  44      -9.423   0.402 -35.201  1.00 29.80           C  
-ATOM   1943  CG2 VAL B  44      -9.132   1.750 -33.083  1.00 40.70           C  
-ATOM   1944  N   THR B  45      -9.061  -2.528 -32.632  1.00 37.04           N  
-ATOM   1945  CA  THR B  45      -8.709  -3.925 -32.806  1.00 34.79           C  
-ATOM   1946  C   THR B  45      -9.766  -4.798 -32.163  1.00 38.37           C  
-ATOM   1947  O   THR B  45      -9.864  -5.988 -32.462  1.00 36.49           O  
-ATOM   1948  CB  THR B  45      -7.356  -4.229 -32.198  1.00 30.20           C  
-ATOM   1949  OG1 THR B  45      -7.346  -3.805 -30.827  1.00 37.17           O  
-ATOM   1950  CG2 THR B  45      -6.244  -3.503 -32.991  1.00 27.48           C  
-ATOM   1951  N   GLY B  46     -10.563  -4.191 -31.286  1.00 32.97           N  
-ATOM   1952  CA  GLY B  46     -11.642  -4.900 -30.643  1.00 29.64           C  
-ATOM   1953  C   GLY B  46     -12.777  -5.166 -31.606  1.00 29.72           C  
-ATOM   1954  O   GLY B  46     -13.219  -6.306 -31.767  1.00 22.50           O  
-ATOM   1955  N   LYS B  47     -13.251  -4.103 -32.253  1.00 37.02           N  
-ATOM   1956  CA  LYS B  47     -14.397  -4.218 -33.151  1.00 38.91           C  
-ATOM   1957  C   LYS B  47     -14.096  -5.218 -34.238  1.00 30.46           C  
-ATOM   1958  O   LYS B  47     -14.957  -5.983 -34.650  1.00 28.06           O  
-ATOM   1959  CB  LYS B  47     -14.795  -2.867 -33.753  1.00 39.81           C  
-ATOM   1960  CG  LYS B  47     -15.412  -1.911 -32.725  1.00 62.63           C  
-ATOM   1961  CD  LYS B  47     -16.377  -0.908 -33.374  1.00 87.30           C  
-ATOM   1962  CE  LYS B  47     -16.755   0.225 -32.410  1.00 76.63           C  
-ATOM   1963  NZ  LYS B  47     -15.539   0.967 -31.934  1.00 69.63           N  
-ATOM   1964  N   MET B  48     -12.850  -5.225 -34.678  1.00 32.00           N  
-ATOM   1965  CA  MET B  48     -12.419  -6.182 -35.672  1.00 29.38           C  
-ATOM   1966  C   MET B  48     -12.419  -7.590 -35.106  1.00 31.26           C  
-ATOM   1967  O   MET B  48     -12.906  -8.516 -35.743  1.00 38.85           O  
-ATOM   1968  CB  MET B  48     -11.050  -5.801 -36.206  1.00 36.39           C  
-ATOM   1969  CG  MET B  48     -11.103  -4.594 -37.128  1.00 44.50           C  
-ATOM   1970  SD  MET B  48      -9.626  -4.411 -38.125  1.00 62.70           S  
-ATOM   1971  CE  MET B  48      -8.670  -3.329 -37.080  1.00 35.72           C  
-ATOM   1972  N   ILE B  49     -11.883  -7.760 -33.904  1.00 34.36           N  
-ATOM   1973  CA  ILE B  49     -11.969  -9.058 -33.247  1.00 34.96           C  
-ATOM   1974  C   ILE B  49     -13.439  -9.491 -33.124  1.00 31.54           C  
-ATOM   1975  O   ILE B  49     -13.781 -10.657 -33.344  1.00 25.85           O  
-ATOM   1976  CB  ILE B  49     -11.273  -9.053 -31.867  1.00 30.36           C  
-ATOM   1977  CG1 ILE B  49      -9.804  -8.656 -32.018  1.00 37.03           C  
-ATOM   1978  CG2 ILE B  49     -11.386 -10.424 -31.205  1.00 21.15           C  
-ATOM   1979  CD1 ILE B  49      -9.047  -8.545 -30.703  1.00 28.52           C  
-ATOM   1980  N   ASP B  50     -14.311  -8.542 -32.794  1.00 26.53           N  
-ATOM   1981  CA  ASP B  50     -15.723  -8.866 -32.646  1.00 30.59           C  
-ATOM   1982  C   ASP B  50     -16.306  -9.436 -33.961  1.00 41.39           C  
-ATOM   1983  O   ASP B  50     -17.041 -10.445 -33.946  1.00 33.39           O  
-ATOM   1984  CB  ASP B  50     -16.525  -7.656 -32.150  1.00 22.34           C  
-ATOM   1985  CG  ASP B  50     -17.860  -8.063 -31.522  1.00 45.29           C  
-ATOM   1986  OD1 ASP B  50     -17.924  -9.192 -30.993  1.00 51.19           O  
-ATOM   1987  OD2 ASP B  50     -18.845  -7.276 -31.550  1.00 47.28           O  
-ATOM   1988  N   ASP B  51     -15.957  -8.800 -35.087  1.00 34.51           N  
-ATOM   1989  CA  ASP B  51     -16.441  -9.226 -36.403  1.00 39.72           C  
-ATOM   1990  C   ASP B  51     -16.017 -10.660 -36.711  1.00 42.97           C  
-ATOM   1991  O   ASP B  51     -16.795 -11.448 -37.277  1.00 42.92           O  
-ATOM   1992  CB  ASP B  51     -15.978  -8.284 -37.527  1.00 38.65           C  
-ATOM   1993  CG  ASP B  51     -16.706  -6.918 -37.515  1.00 51.47           C  
-ATOM   1994  OD1 ASP B  51     -17.773  -6.776 -36.872  1.00 41.65           O  
-ATOM   1995  OD2 ASP B  51     -16.204  -5.971 -38.163  1.00 56.94           O  
-ATOM   1996  N   TYR B  52     -14.798 -11.005 -36.311  1.00 31.43           N  
-ATOM   1997  CA  TYR B  52     -14.262 -12.343 -36.553  1.00 34.49           C  
-ATOM   1998  C   TYR B  52     -14.876 -13.435 -35.681  1.00 43.07           C  
-ATOM   1999  O   TYR B  52     -15.105 -14.549 -36.156  1.00 48.84           O  
-ATOM   2000  CB  TYR B  52     -12.757 -12.325 -36.358  1.00 33.03           C  
-ATOM   2001  CG  TYR B  52     -12.073 -13.669 -36.401  1.00 35.46           C  
-ATOM   2002  CD1 TYR B  52     -11.836 -14.306 -37.603  1.00 38.92           C  
-ATOM   2003  CD2 TYR B  52     -11.615 -14.277 -35.238  1.00 38.03           C  
-ATOM   2004  CE1 TYR B  52     -11.182 -15.529 -37.654  1.00 41.39           C  
-ATOM   2005  CE2 TYR B  52     -10.951 -15.497 -35.279  1.00 46.29           C  
-ATOM   2006  CZ  TYR B  52     -10.735 -16.124 -36.497  1.00 42.58           C  
-ATOM   2007  OH  TYR B  52     -10.070 -17.343 -36.565  1.00 44.07           O  
-ATOM   2008  N   LEU B  53     -15.130 -13.127 -34.411  1.00 39.79           N  
-ATOM   2009  CA  LEU B  53     -15.690 -14.118 -33.501  1.00 40.20           C  
-ATOM   2010  C   LEU B  53     -17.154 -14.375 -33.824  1.00 42.17           C  
-ATOM   2011  O   LEU B  53     -17.640 -15.496 -33.678  1.00 37.27           O  
-ATOM   2012  CB  LEU B  53     -15.553 -13.658 -32.050  1.00 43.17           C  
-ATOM   2013  CG  LEU B  53     -14.178 -13.653 -31.387  1.00 33.33           C  
-ATOM   2014  CD1 LEU B  53     -14.257 -12.941 -30.042  1.00 41.77           C  
-ATOM   2015  CD2 LEU B  53     -13.638 -15.062 -31.218  1.00 32.27           C  
-ATOM   2016  N   THR B  54     -17.849 -13.321 -34.253  1.00 36.40           N  
-ATOM   2017  CA  THR B  54     -19.255 -13.415 -34.651  1.00 38.89           C  
-ATOM   2018  C   THR B  54     -19.462 -13.775 -36.140  1.00 43.88           C  
-ATOM   2019  O   THR B  54     -20.561 -13.595 -36.683  1.00 40.53           O  
-ATOM   2020  CB  THR B  54     -20.039 -12.115 -34.320  1.00 40.90           C  
-ATOM   2021  OG1 THR B  54     -19.705 -11.073 -35.249  1.00 42.52           O  
-ATOM   2022  CG2 THR B  54     -19.707 -11.649 -32.921  1.00 43.23           C  
-ATOM   2023  N   ARG B  55     -18.414 -14.279 -36.790  1.00 34.47           N  
-ATOM   2024  CA  ARG B  55     -18.515 -14.819 -38.150  1.00 38.37           C  
-ATOM   2025  C   ARG B  55     -18.972 -13.828 -39.223  1.00 39.88           C  
-ATOM   2026  O   ARG B  55     -19.532 -14.240 -40.226  1.00 37.76           O  
-ATOM   2027  CB  ARG B  55     -19.440 -16.047 -38.186  1.00 30.93           C  
-ATOM   2028  CG  ARG B  55     -18.945 -17.274 -37.418  1.00 41.65           C  
-ATOM   2029  CD  ARG B  55     -20.078 -18.300 -37.245  1.00 45.22           C  
-ATOM   2030  NE  ARG B  55     -19.883 -19.240 -36.141  1.00 44.68           N  
-ATOM   2031  CZ  ARG B  55     -18.909 -20.151 -36.104  1.00 54.17           C  
-ATOM   2032  NH1 ARG B  55     -18.808 -20.978 -35.066  1.00 40.79           N  
-ATOM   2033  NH2 ARG B  55     -18.019 -20.229 -37.099  1.00 52.57           N  
-ATOM   2034  N   LYS B  56     -18.747 -12.533 -39.035  1.00 40.13           N  
-ATOM   2035  CA  LYS B  56     -19.179 -11.566 -40.049  1.00 42.49           C  
-ATOM   2036  C   LYS B  56     -17.981 -10.901 -40.750  1.00 48.04           C  
-ATOM   2037  O   LYS B  56     -18.064  -9.789 -41.301  1.00 45.39           O  
-ATOM   2038  CB  LYS B  56     -20.156 -10.538 -39.461  1.00 34.42           C  
-ATOM   2039  CG  LYS B  56     -19.560  -9.666 -38.379  1.00 49.52           C  
-ATOM   2040  CD  LYS B  56     -20.574  -8.674 -37.808  1.00 57.70           C  
-ATOM   2041  CE  LYS B  56     -21.717  -9.362 -37.075  1.00 46.06           C  
-ATOM   2042  NZ  LYS B  56     -22.309  -8.425 -36.083  1.00 57.99           N  
-ATOM   2043  N   LYS B  57     -16.872 -11.629 -40.714  1.00 42.97           N  
-ATOM   2044  CA  LYS B  57     -15.620 -11.276 -41.374  1.00 39.81           C  
-ATOM   2045  C   LYS B  57     -14.592 -12.386 -41.097  1.00 41.04           C  
-ATOM   2046  O   LYS B  57     -14.576 -12.999 -40.016  1.00 33.27           O  
-ATOM   2047  CB  LYS B  57     -15.095  -9.932 -40.879  1.00 43.94           C  
-ATOM   2048  CG  LYS B  57     -15.421  -8.743 -41.766  1.00 48.28           C  
-ATOM   2049  CD  LYS B  57     -14.946  -7.437 -41.119  1.00 57.26           C  
-ATOM   2050  CE  LYS B  57     -15.545  -6.214 -41.810  1.00 66.56           C  
-ATOM   2051  NZ  LYS B  57     -17.040  -6.291 -41.918  1.00 60.70           N  
-ATOM   2052  N   THR B  58     -13.754 -12.679 -42.081  1.00 48.52           N  
-ATOM   2053  CA  THR B  58     -12.625 -13.557 -41.807  1.00 53.08           C  
-ATOM   2054  C   THR B  58     -11.322 -12.849 -42.086  1.00 44.88           C  
-ATOM   2055  O   THR B  58     -11.290 -11.803 -42.745  1.00 35.17           O  
-ATOM   2056  CB  THR B  58     -12.662 -14.884 -42.582  1.00 50.42           C  
-ATOM   2057  OG1 THR B  58     -13.326 -14.686 -43.830  1.00 41.45           O  
-ATOM   2058  CG2 THR B  58     -13.384 -15.962 -41.771  1.00 45.68           C  
-ATOM   2059  N   TYR B  59     -10.253 -13.430 -41.562  1.00 28.18           N  
-ATOM   2060  CA  TYR B  59      -8.955 -12.841 -41.683  1.00 31.14           C  
-ATOM   2061  C   TYR B  59      -7.974 -13.995 -41.744  1.00 44.20           C  
-ATOM   2062  O   TYR B  59      -8.329 -15.122 -41.398  1.00 46.00           O  
-ATOM   2063  CB  TYR B  59      -8.672 -11.998 -40.456  1.00 32.23           C  
-ATOM   2064  CG  TYR B  59      -9.520 -10.748 -40.280  1.00 41.81           C  
-ATOM   2065  CD1 TYR B  59     -10.711 -10.781 -39.559  1.00 31.40           C  
-ATOM   2066  CD2 TYR B  59      -9.098  -9.517 -40.789  1.00 45.71           C  
-ATOM   2067  CE1 TYR B  59     -11.467  -9.632 -39.375  1.00 31.51           C  
-ATOM   2068  CE2 TYR B  59      -9.842  -8.360 -40.598  1.00 39.34           C  
-ATOM   2069  CZ  TYR B  59     -11.022  -8.422 -39.897  1.00 46.29           C  
-ATOM   2070  OH  TYR B  59     -11.747  -7.261 -39.734  1.00 50.36           O  
-ATOM   2071  N   ASN B  60      -6.756 -13.722 -42.209  1.00 48.12           N  
-ATOM   2072  CA  ASN B  60      -5.628 -14.635 -42.027  1.00 47.84           C  
-ATOM   2073  C   ASN B  60      -5.605 -15.140 -40.586  1.00 53.79           C  
-ATOM   2074  O   ASN B  60      -5.760 -14.350 -39.660  1.00 53.30           O  
-ATOM   2075  CB  ASN B  60      -4.306 -13.902 -42.301  1.00 47.66           C  
-ATOM   2076  CG  ASN B  60      -3.679 -14.310 -43.602  1.00 56.12           C  
-ATOM   2077  OD1 ASN B  60      -4.365 -14.470 -44.610  1.00 56.25           O  
-ATOM   2078  ND2 ASN B  60      -2.375 -14.482 -43.596  1.00 51.99           N  
-ATOM   2079  N   ASP B  61      -5.439 -16.443 -40.377  1.00 49.46           N  
-ATOM   2080  CA  ASP B  61      -5.180 -16.937 -39.021  1.00 48.56           C  
-ATOM   2081  C   ASP B  61      -4.111 -16.069 -38.359  1.00 50.16           C  
-ATOM   2082  O   ASP B  61      -4.229 -15.657 -37.205  1.00 48.78           O  
-ATOM   2083  CB  ASP B  61      -4.677 -18.375 -39.058  1.00 48.75           C  
-ATOM   2084  CG  ASP B  61      -5.758 -19.360 -39.415  1.00 61.43           C  
-ATOM   2085  OD1 ASP B  61      -6.761 -19.419 -38.673  1.00 45.85           O  
-ATOM   2086  OD2 ASP B  61      -5.599 -20.080 -40.431  1.00 63.02           O  
-ATOM   2087  N   HIS B  62      -3.069 -15.794 -39.128  1.00 52.71           N  
-ATOM   2088  CA  HIS B  62      -1.909 -15.056 -38.663  1.00 53.64           C  
-ATOM   2089  C   HIS B  62      -2.250 -13.606 -38.336  1.00 54.24           C  
-ATOM   2090  O   HIS B  62      -1.676 -13.018 -37.427  1.00 67.25           O  
-ATOM   2091  CB  HIS B  62      -0.804 -15.161 -39.717  1.00 54.61           C  
-ATOM   2092  CG  HIS B  62      -0.643 -16.548 -40.261  1.00 59.19           C  
-ATOM   2093  ND1 HIS B  62       0.486 -17.311 -40.046  1.00 65.84           N  
-ATOM   2094  CD2 HIS B  62      -1.493 -17.329 -40.972  1.00 52.02           C  
-ATOM   2095  CE1 HIS B  62       0.332 -18.493 -40.618  1.00 64.05           C  
-ATOM   2096  NE2 HIS B  62      -0.860 -18.530 -41.185  1.00 48.85           N  
-ATOM   2097  N   ILE B  63      -3.199 -13.030 -39.058  1.00 54.34           N  
-ATOM   2098  CA  ILE B  63      -3.602 -11.670 -38.754  1.00 50.09           C  
-ATOM   2099  C   ILE B  63      -4.407 -11.670 -37.438  1.00 43.09           C  
-ATOM   2100  O   ILE B  63      -4.118 -10.890 -36.525  1.00 46.84           O  
-ATOM   2101  CB  ILE B  63      -4.322 -10.991 -39.963  1.00 48.48           C  
-ATOM   2102  CG1 ILE B  63      -4.431  -9.486 -39.762  1.00 33.49           C  
-ATOM   2103  CG2 ILE B  63      -5.687 -11.574 -40.179  1.00 51.85           C  
-ATOM   2104  CD1 ILE B  63      -5.330  -8.820 -40.748  1.00 44.60           C  
-ATOM   2105  N   VAL B  64      -5.375 -12.567 -37.300  1.00 38.36           N  
-ATOM   2106  CA  VAL B  64      -6.151 -12.590 -36.055  1.00 43.47           C  
-ATOM   2107  C   VAL B  64      -5.219 -12.710 -34.861  1.00 44.28           C  
-ATOM   2108  O   VAL B  64      -5.418 -12.042 -33.848  1.00 36.96           O  
-ATOM   2109  CB  VAL B  64      -7.242 -13.697 -36.016  1.00 45.33           C  
-ATOM   2110  CG1 VAL B  64      -7.838 -13.889 -37.403  1.00 41.00           C  
-ATOM   2111  CG2 VAL B  64      -6.696 -15.006 -35.464  1.00 46.98           C  
-ATOM   2112  N   ASN B  65      -4.180 -13.534 -34.998  1.00 49.73           N  
-ATOM   2113  CA  ASN B  65      -3.177 -13.669 -33.943  1.00 42.99           C  
-ATOM   2114  C   ASN B  65      -2.655 -12.315 -33.482  1.00 48.06           C  
-ATOM   2115  O   ASN B  65      -2.519 -12.092 -32.275  1.00 36.47           O  
-ATOM   2116  CB  ASN B  65      -1.998 -14.533 -34.391  1.00 46.93           C  
-ATOM   2117  CG  ASN B  65      -2.322 -16.024 -34.408  1.00 60.34           C  
-ATOM   2118  OD1 ASN B  65      -3.485 -16.418 -34.448  1.00 63.78           O  
-ATOM   2119  ND2 ASN B  65      -1.286 -16.858 -34.394  1.00 62.87           N  
-ATOM   2120  N   LEU B  66      -2.359 -11.419 -34.433  1.00 38.98           N  
-ATOM   2121  CA  LEU B  66      -1.813 -10.114 -34.075  1.00 37.17           C  
-ATOM   2122  C   LEU B  66      -2.871  -9.058 -33.739  1.00 35.19           C  
-ATOM   2123  O   LEU B  66      -2.558  -8.058 -33.097  1.00 37.96           O  
-ATOM   2124  CB  LEU B  66      -0.787  -9.601 -35.099  1.00 43.40           C  
-ATOM   2125  CG  LEU B  66      -1.204  -8.953 -36.425  1.00 58.72           C  
-ATOM   2126  CD1 LEU B  66      -2.675  -8.512 -36.497  1.00 54.88           C  
-ATOM   2127  CD2 LEU B  66      -0.266  -7.793 -36.722  1.00 41.95           C  
-ATOM   2128  N   LEU B  67      -4.119  -9.269 -34.152  1.00 36.40           N  
-ATOM   2129  CA  LEU B  67      -5.205  -8.412 -33.655  1.00 38.88           C  
-ATOM   2130  C   LEU B  67      -5.354  -8.553 -32.144  1.00 32.34           C  
-ATOM   2131  O   LEU B  67      -5.523  -7.573 -31.430  1.00 28.78           O  
-ATOM   2132  CB  LEU B  67      -6.530  -8.753 -34.322  1.00 34.42           C  
-ATOM   2133  CG  LEU B  67      -6.674  -8.134 -35.697  1.00 37.32           C  
-ATOM   2134  CD1 LEU B  67      -8.040  -8.445 -36.264  1.00 39.93           C  
-ATOM   2135  CD2 LEU B  67      -6.469  -6.644 -35.594  1.00 37.04           C  
-ATOM   2136  N   PHE B  68      -5.298  -9.795 -31.679  1.00 31.31           N  
-ATOM   2137  CA  PHE B  68      -5.471 -10.111 -30.272  1.00 31.28           C  
-ATOM   2138  C   PHE B  68      -4.325  -9.564 -29.456  1.00 33.38           C  
-ATOM   2139  O   PHE B  68      -4.521  -8.997 -28.372  1.00 31.28           O  
-ATOM   2140  CB  PHE B  68      -5.544 -11.616 -30.072  1.00 31.23           C  
-ATOM   2141  CG  PHE B  68      -6.925 -12.167 -30.199  1.00 34.67           C  
-ATOM   2142  CD1 PHE B  68      -7.889 -11.872 -29.245  1.00 38.70           C  
-ATOM   2143  CD2 PHE B  68      -7.265 -12.984 -31.269  1.00 33.61           C  
-ATOM   2144  CE1 PHE B  68      -9.170 -12.388 -29.360  1.00 36.86           C  
-ATOM   2145  CE2 PHE B  68      -8.536 -13.505 -31.391  1.00 29.62           C  
-ATOM   2146  CZ  PHE B  68      -9.490 -13.207 -30.442  1.00 37.59           C  
-ATOM   2147  N   CYS B  69      -3.123  -9.752 -29.982  1.00 34.60           N  
-ATOM   2148  CA  CYS B  69      -1.936  -9.255 -29.322  1.00 37.59           C  
-ATOM   2149  C   CYS B  69      -2.033  -7.739 -29.194  1.00 36.78           C  
-ATOM   2150  O   CYS B  69      -1.985  -7.201 -28.078  1.00 28.46           O  
-ATOM   2151  CB  CYS B  69      -0.687  -9.651 -30.108  1.00 33.65           C  
-ATOM   2152  SG  CYS B  69       0.837  -9.480 -29.151  1.00 46.57           S  
-ATOM   2153  N   ALA B  70      -2.189  -7.064 -30.336  1.00 24.77           N  
-ATOM   2154  CA  ALA B  70      -2.240  -5.608 -30.362  1.00 32.88           C  
-ATOM   2155  C   ALA B  70      -3.355  -5.089 -29.443  1.00 39.97           C  
-ATOM   2156  O   ALA B  70      -3.223  -4.053 -28.774  1.00 36.12           O  
-ATOM   2157  CB  ALA B  70      -2.425  -5.104 -31.779  1.00 28.10           C  
-ATOM   2158  N   ASN B  71      -4.454  -5.826 -29.409  1.00 34.77           N  
-ATOM   2159  CA  ASN B  71      -5.536  -5.535 -28.487  1.00 33.43           C  
-ATOM   2160  C   ASN B  71      -5.062  -5.482 -27.008  1.00 34.26           C  
-ATOM   2161  O   ASN B  71      -5.531  -4.650 -26.219  1.00 29.40           O  
-ATOM   2162  CB  ASN B  71      -6.664  -6.554 -28.689  1.00 25.83           C  
-ATOM   2163  CG  ASN B  71      -7.905  -6.211 -27.893  1.00 37.38           C  
-ATOM   2164  OD1 ASN B  71      -8.311  -6.976 -27.014  1.00 35.40           O  
-ATOM   2165  ND2 ASN B  71      -8.509  -5.051 -28.182  1.00 27.63           N  
-ATOM   2166  N   ARG B  72      -4.122  -6.352 -26.640  1.00 30.00           N  
-ATOM   2167  CA  ARG B  72      -3.553  -6.325 -25.294  1.00 25.98           C  
-ATOM   2168  C   ARG B  72      -2.579  -5.154 -25.084  1.00 33.45           C  
-ATOM   2169  O   ARG B  72      -2.688  -4.415 -24.117  1.00 28.72           O  
-ATOM   2170  CB  ARG B  72      -2.879  -7.651 -24.965  1.00 30.81           C  
-ATOM   2171  CG  ARG B  72      -3.857  -8.751 -24.554  1.00 27.52           C  
-ATOM   2172  CD  ARG B  72      -3.138 -10.079 -24.262  1.00 33.18           C  
-ATOM   2173  NE  ARG B  72      -2.704 -10.754 -25.468  1.00 20.02           N  
-ATOM   2174  CZ  ARG B  72      -3.473 -11.565 -26.187  1.00 32.48           C  
-ATOM   2175  NH1 ARG B  72      -4.723 -11.819 -25.818  1.00 28.99           N  
-ATOM   2176  NH2 ARG B  72      -2.992 -12.125 -27.291  1.00 42.18           N  
-ATOM   2177  N   TRP B  73      -1.642  -4.963 -26.004  1.00 38.92           N  
-ATOM   2178  CA  TRP B  73      -0.724  -3.822 -25.914  1.00 33.44           C  
-ATOM   2179  C   TRP B  73      -1.330  -2.411 -25.723  1.00 33.22           C  
-ATOM   2180  O   TRP B  73      -0.718  -1.582 -25.064  1.00 32.56           O  
-ATOM   2181  CB  TRP B  73       0.238  -3.825 -27.081  1.00 30.10           C  
-ATOM   2182  CG  TRP B  73       1.199  -4.921 -26.977  1.00 32.59           C  
-ATOM   2183  CD1 TRP B  73       1.101  -6.160 -27.551  1.00 38.85           C  
-ATOM   2184  CD2 TRP B  73       2.418  -4.912 -26.238  1.00 34.35           C  
-ATOM   2185  NE1 TRP B  73       2.196  -6.923 -27.220  1.00 36.84           N  
-ATOM   2186  CE2 TRP B  73       3.017  -6.185 -26.414  1.00 42.41           C  
-ATOM   2187  CE3 TRP B  73       3.061  -3.956 -25.450  1.00 32.53           C  
-ATOM   2188  CZ2 TRP B  73       4.245  -6.519 -25.818  1.00 38.40           C  
-ATOM   2189  CZ3 TRP B  73       4.280  -4.289 -24.866  1.00 36.35           C  
-ATOM   2190  CH2 TRP B  73       4.856  -5.560 -25.052  1.00 42.60           C  
-ATOM   2191  N   GLU B  74      -2.504  -2.121 -26.289  1.00 31.97           N  
-ATOM   2192  CA  GLU B  74      -3.153  -0.823 -26.033  1.00 34.22           C  
-ATOM   2193  C   GLU B  74      -3.217  -0.542 -24.531  1.00 38.88           C  
-ATOM   2194  O   GLU B  74      -3.208   0.603 -24.078  1.00 38.42           O  
-ATOM   2195  CB  GLU B  74      -4.576  -0.768 -26.595  1.00 33.65           C  
-ATOM   2196  CG  GLU B  74      -4.713  -1.062 -28.094  1.00 62.38           C  
-ATOM   2197  CD  GLU B  74      -6.133  -0.819 -28.611  1.00 66.61           C  
-ATOM   2198  OE1 GLU B  74      -6.842   0.007 -27.987  1.00 65.91           O  
-ATOM   2199  OE2 GLU B  74      -6.531  -1.443 -29.633  1.00 50.81           O  
-ATOM   2200  N   PHE B  75      -3.274  -1.611 -23.757  1.00 39.15           N  
-ATOM   2201  CA  PHE B  75      -3.570  -1.498 -22.346  1.00 34.75           C  
-ATOM   2202  C   PHE B  75      -2.366  -1.788 -21.462  1.00 32.64           C  
-ATOM   2203  O   PHE B  75      -2.446  -1.681 -20.247  1.00 35.20           O  
-ATOM   2204  CB  PHE B  75      -4.716  -2.447 -22.005  1.00 34.36           C  
-ATOM   2205  CG  PHE B  75      -6.041  -2.001 -22.536  1.00 29.35           C  
-ATOM   2206  CD1 PHE B  75      -6.483  -2.422 -23.776  1.00 31.55           C  
-ATOM   2207  CD2 PHE B  75      -6.846  -1.152 -21.789  1.00 32.24           C  
-ATOM   2208  CE1 PHE B  75      -7.715  -2.007 -24.263  1.00 32.39           C  
-ATOM   2209  CE2 PHE B  75      -8.074  -0.733 -22.265  1.00 33.87           C  
-ATOM   2210  CZ  PHE B  75      -8.510  -1.163 -23.506  1.00 28.61           C  
-ATOM   2211  N   ALA B  76      -1.248  -2.161 -22.068  1.00 32.01           N  
-ATOM   2212  CA  ALA B  76      -0.051  -2.459 -21.289  1.00 33.99           C  
-ATOM   2213  C   ALA B  76       0.406  -1.250 -20.460  1.00 39.52           C  
-ATOM   2214  O   ALA B  76       0.870  -1.403 -19.332  1.00 35.36           O  
-ATOM   2215  CB  ALA B  76       1.058  -2.964 -22.191  1.00 27.00           C  
-ATOM   2216  N   SER B  77       0.269  -0.053 -21.024  1.00 40.57           N  
-ATOM   2217  CA  SER B  77       0.553   1.178 -20.290  1.00 41.02           C  
-ATOM   2218  C   SER B  77      -0.353   1.305 -19.081  1.00 41.54           C  
-ATOM   2219  O   SER B  77       0.105   1.544 -17.968  1.00 33.60           O  
-ATOM   2220  CB  SER B  77       0.338   2.400 -21.182  1.00 41.75           C  
-ATOM   2221  OG  SER B  77       1.567   2.880 -21.670  1.00 34.95           O  
-ATOM   2222  N   PHE B  78      -1.652   1.166 -19.332  1.00 42.25           N  
-ATOM   2223  CA  PHE B  78      -2.681   1.257 -18.305  1.00 35.06           C  
-ATOM   2224  C   PHE B  78      -2.462   0.258 -17.168  1.00 35.78           C  
-ATOM   2225  O   PHE B  78      -2.530   0.616 -15.993  1.00 39.96           O  
-ATOM   2226  CB  PHE B  78      -4.040   1.012 -18.948  1.00 29.73           C  
-ATOM   2227  CG  PHE B  78      -5.192   1.081 -17.989  1.00 34.77           C  
-ATOM   2228  CD1 PHE B  78      -5.721   2.307 -17.606  1.00 38.66           C  
-ATOM   2229  CD2 PHE B  78      -5.771  -0.081 -17.495  1.00 36.80           C  
-ATOM   2230  CE1 PHE B  78      -6.801   2.377 -16.737  1.00 42.59           C  
-ATOM   2231  CE2 PHE B  78      -6.849  -0.018 -16.618  1.00 38.01           C  
-ATOM   2232  CZ  PHE B  78      -7.364   1.212 -16.238  1.00 40.01           C  
-ATOM   2233  N   ILE B  79      -2.218  -0.996 -17.520  1.00 29.93           N  
-ATOM   2234  CA  ILE B  79      -1.982  -2.020 -16.523  1.00 34.87           C  
-ATOM   2235  C   ILE B  79      -0.860  -1.593 -15.580  1.00 39.05           C  
-ATOM   2236  O   ILE B  79      -1.070  -1.454 -14.370  1.00 36.38           O  
-ATOM   2237  CB  ILE B  79      -1.617  -3.347 -17.182  1.00 33.80           C  
-ATOM   2238  CG1 ILE B  79      -2.807  -3.865 -17.990  1.00 33.28           C  
-ATOM   2239  CG2 ILE B  79      -1.208  -4.354 -16.125  1.00 28.50           C  
-ATOM   2240  CD1 ILE B  79      -2.440  -4.882 -19.055  1.00 27.91           C  
-ATOM   2241  N   GLN B  80       0.325  -1.399 -16.157  1.00 39.99           N  
-ATOM   2242  CA  GLN B  80       1.508  -0.875 -15.467  1.00 39.07           C  
-ATOM   2243  C   GLN B  80       1.180   0.300 -14.526  1.00 42.55           C  
-ATOM   2244  O   GLN B  80       1.505   0.270 -13.339  1.00 38.66           O  
-ATOM   2245  CB  GLN B  80       2.558  -0.456 -16.512  1.00 42.19           C  
-ATOM   2246  CG  GLN B  80       3.792   0.215 -15.954  1.00 54.95           C  
-ATOM   2247  CD  GLN B  80       4.578  -0.727 -15.083  1.00 65.54           C  
-ATOM   2248  OE1 GLN B  80       4.511  -1.944 -15.270  1.00 66.19           O  
-ATOM   2249  NE2 GLN B  80       5.321  -0.181 -14.120  1.00 48.72           N  
-ATOM   2250  N   GLU B  81       0.527   1.329 -15.059  1.00 41.76           N  
-ATOM   2251  CA  GLU B  81       0.186   2.510 -14.273  1.00 44.32           C  
-ATOM   2252  C   GLU B  81      -0.649   2.196 -13.031  1.00 43.87           C  
-ATOM   2253  O   GLU B  81      -0.342   2.664 -11.939  1.00 38.46           O  
-ATOM   2254  CB  GLU B  81      -0.523   3.546 -15.145  1.00 37.35           C  
-ATOM   2255  CG  GLU B  81       0.436   4.336 -16.008  1.00 61.04           C  
-ATOM   2256  CD  GLU B  81      -0.115   4.647 -17.400  1.00 89.06           C  
-ATOM   2257  OE1 GLU B  81       0.678   5.114 -18.256  1.00 89.65           O  
-ATOM   2258  OE2 GLU B  81      -1.329   4.423 -17.645  1.00 80.42           O  
-ATOM   2259  N   GLN B  82      -1.706   1.412 -13.204  1.00 39.89           N  
-ATOM   2260  CA  GLN B  82      -2.572   1.023 -12.092  1.00 36.52           C  
-ATOM   2261  C   GLN B  82      -1.836   0.245 -10.997  1.00 36.92           C  
-ATOM   2262  O   GLN B  82      -1.938   0.557  -9.812  1.00 32.01           O  
-ATOM   2263  CB  GLN B  82      -3.738   0.183 -12.613  1.00 37.81           C  
-ATOM   2264  CG  GLN B  82      -4.571   0.896 -13.640  1.00 43.04           C  
-ATOM   2265  CD  GLN B  82      -5.280   2.099 -13.060  1.00 41.20           C  
-ATOM   2266  OE1 GLN B  82      -6.251   1.960 -12.312  1.00 32.47           O  
-ATOM   2267  NE2 GLN B  82      -4.807   3.291 -13.410  1.00 32.35           N  
-ATOM   2268  N   LEU B  83      -1.111  -0.789 -11.388  1.00 34.38           N  
-ATOM   2269  CA  LEU B  83      -0.373  -1.569 -10.410  1.00 31.32           C  
-ATOM   2270  C   LEU B  83       0.531  -0.661  -9.568  1.00 38.55           C  
-ATOM   2271  O   LEU B  83       0.508  -0.714  -8.338  1.00 37.25           O  
-ATOM   2272  CB  LEU B  83       0.437  -2.660 -11.106  1.00 34.92           C  
-ATOM   2273  CG  LEU B  83      -0.428  -3.677 -11.851  1.00 35.93           C  
-ATOM   2274  CD1 LEU B  83       0.416  -4.722 -12.567  1.00 30.36           C  
-ATOM   2275  CD2 LEU B  83      -1.375  -4.333 -10.864  1.00 27.38           C  
-ATOM   2276  N   GLU B  84       1.314   0.184 -10.234  1.00 42.85           N  
-ATOM   2277  CA  GLU B  84       2.148   1.151  -9.525  1.00 44.49           C  
-ATOM   2278  C   GLU B  84       1.333   2.041  -8.586  1.00 39.95           C  
-ATOM   2279  O   GLU B  84       1.788   2.348  -7.487  1.00 39.78           O  
-ATOM   2280  CB  GLU B  84       2.980   2.000 -10.499  1.00 46.61           C  
-ATOM   2281  CG  GLU B  84       4.279   1.321 -10.956  1.00 50.19           C  
-ATOM   2282  CD  GLU B  84       4.948   2.026 -12.132  1.00 74.25           C  
-ATOM   2283  OE1 GLU B  84       4.295   2.879 -12.778  1.00 74.75           O  
-ATOM   2284  OE2 GLU B  84       6.128   1.721 -12.418  1.00 80.66           O  
-ATOM   2285  N   GLN B  85       0.139   2.443  -9.024  1.00 36.47           N  
-ATOM   2286  CA  GLN B  85      -0.758   3.278  -8.224  1.00 31.76           C  
-ATOM   2287  C   GLN B  85      -1.463   2.475  -7.164  1.00 33.09           C  
-ATOM   2288  O   GLN B  85      -2.405   2.960  -6.552  1.00 40.22           O  
-ATOM   2289  CB  GLN B  85      -1.825   3.964  -9.080  1.00 44.10           C  
-ATOM   2290  CG  GLN B  85      -1.533   5.409  -9.445  1.00 62.65           C  
-ATOM   2291  CD  GLN B  85      -2.645   6.044 -10.277  1.00 88.83           C  
-ATOM   2292  OE1 GLN B  85      -3.265   5.390 -11.121  1.00 79.83           O  
-ATOM   2293  NE2 GLN B  85      -2.898   7.330 -10.045  1.00110.15           N  
-ATOM   2294  N   GLY B  86      -1.026   1.241  -6.953  1.00 33.56           N  
-ATOM   2295  CA  GLY B  86      -1.519   0.455  -5.836  1.00 25.69           C  
-ATOM   2296  C   GLY B  86      -2.830  -0.267  -6.084  1.00 32.11           C  
-ATOM   2297  O   GLY B  86      -3.315  -0.959  -5.193  1.00 33.06           O  
-ATOM   2298  N   ILE B  87      -3.404  -0.123  -7.280  1.00 34.47           N  
-ATOM   2299  CA  ILE B  87      -4.602  -0.889  -7.650  1.00 30.44           C  
-ATOM   2300  C   ILE B  87      -4.255  -2.287  -8.160  1.00 26.61           C  
-ATOM   2301  O   ILE B  87      -3.375  -2.461  -8.983  1.00 24.13           O  
-ATOM   2302  CB  ILE B  87      -5.436  -0.203  -8.741  1.00 30.27           C  
-ATOM   2303  CG1 ILE B  87      -6.106   1.054  -8.209  1.00 30.05           C  
-ATOM   2304  CG2 ILE B  87      -6.519  -1.132  -9.206  1.00 27.45           C  
-ATOM   2305  CD1 ILE B  87      -5.361   1.715  -7.085  1.00 38.76           C  
-ATOM   2306  N   THR B  88      -4.973  -3.276  -7.658  1.00 34.96           N  
-ATOM   2307  CA  THR B  88      -4.839  -4.662  -8.084  1.00 30.71           C  
-ATOM   2308  C   THR B  88      -5.693  -4.924  -9.340  1.00 28.29           C  
-ATOM   2309  O   THR B  88      -6.801  -4.383  -9.504  1.00 27.06           O  
-ATOM   2310  CB  THR B  88      -5.259  -5.612  -6.931  1.00 32.99           C  
-ATOM   2311  OG1 THR B  88      -4.171  -5.755  -6.009  1.00 24.57           O  
-ATOM   2312  CG2 THR B  88      -5.712  -6.975  -7.450  1.00 25.75           C  
-ATOM   2313  N   LEU B  89      -5.172  -5.743 -10.239  1.00 29.59           N  
-ATOM   2314  CA  LEU B  89      -5.839  -5.967 -11.516  1.00 29.60           C  
-ATOM   2315  C   LEU B  89      -6.384  -7.353 -11.612  1.00 25.54           C  
-ATOM   2316  O   LEU B  89      -5.653  -8.331 -11.427  1.00 26.26           O  
-ATOM   2317  CB  LEU B  89      -4.888  -5.724 -12.675  1.00 21.80           C  
-ATOM   2318  CG  LEU B  89      -4.901  -4.247 -13.032  1.00 25.17           C  
-ATOM   2319  CD1 LEU B  89      -4.078  -3.992 -14.260  1.00 45.43           C  
-ATOM   2320  CD2 LEU B  89      -6.335  -3.857 -13.284  1.00 37.04           C  
-ATOM   2321  N   ILE B  90      -7.680  -7.424 -11.887  1.00 21.42           N  
-ATOM   2322  CA  ILE B  90      -8.357  -8.699 -12.130  1.00 25.06           C  
-ATOM   2323  C   ILE B  90      -8.730  -8.824 -13.609  1.00 28.26           C  
-ATOM   2324  O   ILE B  90      -9.631  -8.141 -14.106  1.00 27.03           O  
-ATOM   2325  CB  ILE B  90      -9.601  -8.870 -11.251  1.00 24.83           C  
-ATOM   2326  CG1 ILE B  90      -9.199  -8.875  -9.768  1.00 31.33           C  
-ATOM   2327  CG2 ILE B  90     -10.358 -10.135 -11.642  1.00 21.37           C  
-ATOM   2328  CD1 ILE B  90      -8.138  -9.908  -9.397  1.00 31.78           C  
-ATOM   2329  N   VAL B  91      -8.022  -9.711 -14.302  1.00 25.76           N  
-ATOM   2330  CA  VAL B  91      -8.061  -9.766 -15.744  1.00 22.14           C  
-ATOM   2331  C   VAL B  91      -8.608 -11.084 -16.248  1.00 25.04           C  
-ATOM   2332  O   VAL B  91      -8.054 -12.154 -15.947  1.00 27.87           O  
-ATOM   2333  CB  VAL B  91      -6.656  -9.611 -16.290  1.00 27.89           C  
-ATOM   2334  CG1 VAL B  91      -6.674  -9.559 -17.822  1.00 23.21           C  
-ATOM   2335  CG2 VAL B  91      -6.008  -8.384 -15.677  1.00 24.78           C  
-ATOM   2336  N   ASP B  92      -9.693 -10.975 -17.015  1.00 27.91           N  
-ATOM   2337  CA  ASP B  92     -10.307 -12.077 -17.759  1.00 30.08           C  
-ATOM   2338  C   ASP B  92      -9.527 -12.291 -19.063  1.00 27.08           C  
-ATOM   2339  O   ASP B  92      -9.537 -11.422 -19.938  1.00 23.91           O  
-ATOM   2340  CB  ASP B  92     -11.756 -11.694 -18.073  1.00 38.08           C  
-ATOM   2341  CG  ASP B  92     -12.651 -12.880 -18.218  1.00 43.10           C  
-ATOM   2342  OD1 ASP B  92     -12.116 -14.002 -18.300  1.00 40.15           O  
-ATOM   2343  OD2 ASP B  92     -13.886 -12.684 -18.242  1.00 44.14           O  
-ATOM   2344  N   ARG B  93      -8.832 -13.430 -19.173  1.00 26.36           N  
-ATOM   2345  CA  ARG B  93      -7.990 -13.773 -20.343  1.00 27.70           C  
-ATOM   2346  C   ARG B  93      -6.828 -12.819 -20.531  1.00 26.01           C  
-ATOM   2347  O   ARG B  93      -6.953 -11.629 -20.253  1.00 30.21           O  
-ATOM   2348  CB  ARG B  93      -8.792 -13.834 -21.652  1.00 26.67           C  
-ATOM   2349  CG  ARG B  93      -9.748 -14.992 -21.749  1.00 22.08           C  
-ATOM   2350  CD  ARG B  93     -10.255 -15.162 -23.138  1.00 20.43           C  
-ATOM   2351  NE  ARG B  93     -11.257 -16.211 -23.190  1.00 32.08           N  
-ATOM   2352  CZ  ARG B  93     -10.989 -17.503 -23.033  1.00 37.97           C  
-ATOM   2353  NH1 ARG B  93      -9.747 -17.893 -22.819  1.00 32.95           N  
-ATOM   2354  NH2 ARG B  93     -11.962 -18.404 -23.083  1.00 41.55           N  
-ATOM   2355  N   TYR B  94      -5.709 -13.340 -21.039  1.00 28.95           N  
-ATOM   2356  CA  TYR B  94      -4.489 -12.551 -21.172  1.00 32.00           C  
-ATOM   2357  C   TYR B  94      -3.575 -13.206 -22.205  1.00 36.52           C  
-ATOM   2358  O   TYR B  94      -4.054 -13.950 -23.081  1.00 29.82           O  
-ATOM   2359  CB  TYR B  94      -3.790 -12.470 -19.806  1.00 34.34           C  
-ATOM   2360  CG  TYR B  94      -2.799 -11.328 -19.618  1.00 28.94           C  
-ATOM   2361  CD1 TYR B  94      -3.133 -10.023 -19.935  1.00 21.33           C  
-ATOM   2362  CD2 TYR B  94      -1.538 -11.565 -19.079  1.00 26.18           C  
-ATOM   2363  CE1 TYR B  94      -2.230  -8.992 -19.744  1.00 23.60           C  
-ATOM   2364  CE2 TYR B  94      -0.627 -10.546 -18.880  1.00 26.20           C  
-ATOM   2365  CZ  TYR B  94      -0.975  -9.260 -19.212  1.00 27.92           C  
-ATOM   2366  OH  TYR B  94      -0.054  -8.254 -19.008  1.00 23.44           O  
-ATOM   2367  N   ALA B  95      -2.271 -12.923 -22.088  1.00 30.05           N  
-ATOM   2368  CA  ALA B  95      -1.235 -13.488 -22.952  1.00 35.33           C  
-ATOM   2369  C   ALA B  95      -1.455 -14.958 -23.288  1.00 34.41           C  
-ATOM   2370  O   ALA B  95      -1.312 -15.366 -24.435  1.00 38.93           O  
-ATOM   2371  CB  ALA B  95       0.125 -13.309 -22.305  1.00 34.19           C  
-ATOM   2372  N   PHE B  96      -1.797 -15.747 -22.282  1.00 34.51           N  
-ATOM   2373  CA  PHE B  96      -1.962 -17.185 -22.463  1.00 36.19           C  
-ATOM   2374  C   PHE B  96      -3.173 -17.537 -23.323  1.00 34.60           C  
-ATOM   2375  O   PHE B  96      -3.110 -18.454 -24.131  1.00 39.88           O  
-ATOM   2376  CB  PHE B  96      -2.005 -17.883 -21.098  1.00 32.24           C  
-ATOM   2377  CG  PHE B  96      -1.087 -17.257 -20.092  1.00 31.38           C  
-ATOM   2378  CD1 PHE B  96       0.221 -17.718 -19.944  1.00 27.18           C  
-ATOM   2379  CD2 PHE B  96      -1.515 -16.162 -19.331  1.00 32.11           C  
-ATOM   2380  CE1 PHE B  96       1.087 -17.117 -19.030  1.00 37.09           C  
-ATOM   2381  CE2 PHE B  96      -0.659 -15.550 -18.408  1.00 37.33           C  
-ATOM   2382  CZ  PHE B  96       0.648 -16.026 -18.258  1.00 41.12           C  
-ATOM   2383  N   SER B  97      -4.274 -16.819 -23.163  1.00 32.50           N  
-ATOM   2384  CA  SER B  97      -5.389 -17.031 -24.073  1.00 36.65           C  
-ATOM   2385  C   SER B  97      -4.852 -16.908 -25.508  1.00 39.66           C  
-ATOM   2386  O   SER B  97      -5.227 -17.676 -26.404  1.00 37.84           O  
-ATOM   2387  CB  SER B  97      -6.516 -16.019 -23.822  1.00 30.53           C  
-ATOM   2388  OG  SER B  97      -7.498 -16.525 -22.928  1.00 27.66           O  
-ATOM   2389  N   GLY B  98      -3.954 -15.945 -25.701  1.00 32.55           N  
-ATOM   2390  CA  GLY B  98      -3.341 -15.710 -26.990  1.00 26.81           C  
-ATOM   2391  C   GLY B  98      -2.582 -16.912 -27.502  1.00 33.95           C  
-ATOM   2392  O   GLY B  98      -2.956 -17.505 -28.515  1.00 40.35           O  
-ATOM   2393  N   VAL B  99      -1.518 -17.270 -26.793  1.00 33.64           N  
-ATOM   2394  CA  VAL B  99      -0.652 -18.370 -27.192  1.00 32.06           C  
-ATOM   2395  C   VAL B  99      -1.383 -19.712 -27.359  1.00 39.16           C  
-ATOM   2396  O   VAL B  99      -1.180 -20.418 -28.353  1.00 44.68           O  
-ATOM   2397  CB  VAL B  99       0.489 -18.569 -26.195  1.00 35.67           C  
-ATOM   2398  CG1 VAL B  99       1.471 -19.594 -26.744  1.00 42.24           C  
-ATOM   2399  CG2 VAL B  99       1.176 -17.249 -25.919  1.00 33.55           C  
-ATOM   2400  N   ALA B 100      -2.227 -20.067 -26.396  1.00 31.16           N  
-ATOM   2401  CA  ALA B 100      -2.891 -21.367 -26.427  1.00 36.56           C  
-ATOM   2402  C   ALA B 100      -3.855 -21.502 -27.587  1.00 41.32           C  
-ATOM   2403  O   ALA B 100      -3.952 -22.560 -28.206  1.00 42.60           O  
-ATOM   2404  CB  ALA B 100      -3.621 -21.616 -25.132  1.00 39.24           C  
-ATOM   2405  N   TYR B 101      -4.592 -20.430 -27.855  1.00 40.41           N  
-ATOM   2406  CA  TYR B 101      -5.529 -20.417 -28.957  1.00 33.61           C  
-ATOM   2407  C   TYR B 101      -4.779 -20.293 -30.301  1.00 36.53           C  
-ATOM   2408  O   TYR B 101      -5.101 -20.982 -31.271  1.00 37.26           O  
-ATOM   2409  CB  TYR B 101      -6.539 -19.295 -28.759  1.00 26.93           C  
-ATOM   2410  CG  TYR B 101      -7.684 -19.675 -27.855  1.00 33.15           C  
-ATOM   2411  CD1 TYR B 101      -7.536 -19.694 -26.471  1.00 37.64           C  
-ATOM   2412  CD2 TYR B 101      -8.924 -20.003 -28.383  1.00 40.15           C  
-ATOM   2413  CE1 TYR B 101      -8.600 -20.049 -25.625  1.00 32.74           C  
-ATOM   2414  CE2 TYR B 101      -9.993 -20.359 -27.553  1.00 45.24           C  
-ATOM   2415  CZ  TYR B 101      -9.821 -20.379 -26.173  1.00 46.29           C  
-ATOM   2416  OH  TYR B 101     -10.866 -20.728 -25.348  1.00 41.33           O  
-ATOM   2417  N   ALA B 102      -3.763 -19.441 -30.354  1.00 28.43           N  
-ATOM   2418  CA  ALA B 102      -2.971 -19.325 -31.571  1.00 38.29           C  
-ATOM   2419  C   ALA B 102      -2.260 -20.644 -31.900  1.00 46.72           C  
-ATOM   2420  O   ALA B 102      -2.213 -21.097 -33.050  1.00 42.17           O  
-ATOM   2421  CB  ALA B 102      -1.970 -18.185 -31.447  1.00 30.82           C  
-ATOM   2422  N   ALA B 103      -1.711 -21.265 -30.871  1.00 42.91           N  
-ATOM   2423  CA  ALA B 103      -0.971 -22.500 -31.044  1.00 42.12           C  
-ATOM   2424  C   ALA B 103      -1.885 -23.666 -31.391  1.00 44.01           C  
-ATOM   2425  O   ALA B 103      -1.472 -24.598 -32.077  1.00 49.20           O  
-ATOM   2426  CB  ALA B 103      -0.197 -22.808 -29.793  1.00 43.63           C  
-ATOM   2427  N   ALA B 104      -3.118 -23.626 -30.901  1.00 34.48           N  
-ATOM   2428  CA  ALA B 104      -4.059 -24.705 -31.155  1.00 37.22           C  
-ATOM   2429  C   ALA B 104      -4.396 -24.739 -32.633  1.00 44.34           C  
-ATOM   2430  O   ALA B 104      -4.683 -25.798 -33.192  1.00 38.03           O  
-ATOM   2431  CB  ALA B 104      -5.317 -24.503 -30.341  1.00 38.37           C  
-ATOM   2432  N   LYS B 105      -4.365 -23.550 -33.238  1.00 42.98           N  
-ATOM   2433  CA  LYS B 105      -4.627 -23.334 -34.657  1.00 37.48           C  
-ATOM   2434  C   LYS B 105      -3.390 -23.579 -35.533  1.00 48.92           C  
-ATOM   2435  O   LYS B 105      -3.326 -23.131 -36.680  1.00 60.28           O  
-ATOM   2436  CB  LYS B 105      -5.139 -21.906 -34.870  1.00 43.78           C  
-ATOM   2437  CG  LYS B 105      -6.614 -21.811 -35.232  1.00 51.27           C  
-ATOM   2438  CD  LYS B 105      -7.294 -20.639 -34.539  1.00 53.55           C  
-ATOM   2439  CE  LYS B 105      -7.147 -19.314 -35.277  1.00 56.82           C  
-ATOM   2440  NZ  LYS B 105      -5.834 -18.663 -35.018  1.00 53.71           N  
-ATOM   2441  N   GLY B 106      -2.409 -24.286 -34.988  1.00 45.64           N  
-ATOM   2442  CA  GLY B 106      -1.206 -24.602 -35.727  1.00 32.85           C  
-ATOM   2443  C   GLY B 106      -0.048 -23.617 -35.698  1.00 35.44           C  
-ATOM   2444  O   GLY B 106       0.954 -23.833 -36.366  1.00 44.93           O  
-ATOM   2445  N   ALA B 107      -0.154 -22.543 -34.932  1.00 41.93           N  
-ATOM   2446  CA  ALA B 107       0.945 -21.591 -34.881  1.00 37.31           C  
-ATOM   2447  C   ALA B 107       2.076 -22.087 -33.972  1.00 47.06           C  
-ATOM   2448  O   ALA B 107       1.892 -23.021 -33.179  1.00 46.86           O  
-ATOM   2449  CB  ALA B 107       0.448 -20.229 -34.446  1.00 40.74           C  
-ATOM   2450  N   SER B 108       3.247 -21.466 -34.102  1.00 41.48           N  
-ATOM   2451  CA  SER B 108       4.393 -21.802 -33.271  1.00 40.13           C  
-ATOM   2452  C   SER B 108       4.217 -21.210 -31.888  1.00 44.23           C  
-ATOM   2453  O   SER B 108       4.025 -19.995 -31.747  1.00 37.01           O  
-ATOM   2454  CB  SER B 108       5.687 -21.263 -33.891  1.00 52.45           C  
-ATOM   2455  OG  SER B 108       6.751 -21.203 -32.938  1.00 43.86           O  
-ATOM   2456  N   MET B 109       4.300 -22.079 -30.882  1.00 50.73           N  
-ATOM   2457  CA  MET B 109       4.168 -21.701 -29.474  1.00 46.84           C  
-ATOM   2458  C   MET B 109       5.237 -20.704 -29.030  1.00 36.29           C  
-ATOM   2459  O   MET B 109       4.944 -19.786 -28.278  1.00 44.72           O  
-ATOM   2460  CB  MET B 109       4.175 -22.958 -28.594  1.00 50.66           C  
-ATOM   2461  CG  MET B 109       4.722 -22.791 -27.181  1.00 52.76           C  
-ATOM   2462  SD  MET B 109       3.472 -22.910 -25.879  1.00 61.72           S  
-ATOM   2463  CE  MET B 109       2.349 -24.137 -26.546  1.00 52.08           C  
-ATOM   2464  N   THR B 110       6.461 -20.874 -29.512  1.00 42.21           N  
-ATOM   2465  CA  THR B 110       7.574 -20.003 -29.128  1.00 47.45           C  
-ATOM   2466  C   THR B 110       7.454 -18.652 -29.826  1.00 39.88           C  
-ATOM   2467  O   THR B 110       7.833 -17.614 -29.286  1.00 37.56           O  
-ATOM   2468  CB  THR B 110       8.947 -20.640 -29.476  1.00 37.90           C  
-ATOM   2469  OG1 THR B 110       8.963 -20.981 -30.866  1.00 50.44           O  
-ATOM   2470  CG2 THR B 110       9.213 -21.903 -28.634  1.00 35.75           C  
-ATOM   2471  N   LEU B 111       6.927 -18.677 -31.039  1.00 39.65           N  
-ATOM   2472  CA  LEU B 111       6.662 -17.450 -31.774  1.00 46.44           C  
-ATOM   2473  C   LEU B 111       5.464 -16.657 -31.190  1.00 49.25           C  
-ATOM   2474  O   LEU B 111       5.501 -15.429 -31.065  1.00 38.43           O  
-ATOM   2475  CB  LEU B 111       6.423 -17.789 -33.243  1.00 42.36           C  
-ATOM   2476  CG  LEU B 111       6.201 -16.627 -34.215  1.00 50.01           C  
-ATOM   2477  CD1 LEU B 111       7.401 -15.702 -34.275  1.00 34.57           C  
-ATOM   2478  CD2 LEU B 111       5.850 -17.155 -35.602  1.00 53.77           C  
-ATOM   2479  N   SER B 112       4.394 -17.357 -30.841  1.00 41.57           N  
-ATOM   2480  CA  SER B 112       3.258 -16.692 -30.231  1.00 38.85           C  
-ATOM   2481  C   SER B 112       3.763 -15.972 -28.980  1.00 43.47           C  
-ATOM   2482  O   SER B 112       3.360 -14.837 -28.683  1.00 41.51           O  
-ATOM   2483  CB  SER B 112       2.162 -17.711 -29.854  1.00 48.60           C  
-ATOM   2484  OG  SER B 112       1.589 -18.362 -30.988  1.00 49.36           O  
-ATOM   2485  N   LYS B 113       4.651 -16.641 -28.249  1.00 36.81           N  
-ATOM   2486  CA  LYS B 113       5.154 -16.095 -26.997  1.00 40.11           C  
-ATOM   2487  C   LYS B 113       5.936 -14.813 -27.276  1.00 35.35           C  
-ATOM   2488  O   LYS B 113       5.668 -13.770 -26.695  1.00 38.96           O  
-ATOM   2489  CB  LYS B 113       6.000 -17.132 -26.231  1.00 38.93           C  
-ATOM   2490  CG  LYS B 113       5.158 -18.221 -25.551  1.00 45.68           C  
-ATOM   2491  CD  LYS B 113       5.940 -19.494 -25.189  1.00 41.89           C  
-ATOM   2492  CE  LYS B 113       6.566 -19.409 -23.817  1.00 35.91           C  
-ATOM   2493  NZ  LYS B 113       7.042 -20.732 -23.362  1.00 31.09           N  
-ATOM   2494  N   SER B 114       6.890 -14.883 -28.181  1.00 34.40           N  
-ATOM   2495  CA  SER B 114       7.639 -13.697 -28.551  1.00 38.12           C  
-ATOM   2496  C   SER B 114       6.796 -12.420 -28.682  1.00 39.37           C  
-ATOM   2497  O   SER B 114       7.213 -11.365 -28.209  1.00 39.35           O  
-ATOM   2498  CB  SER B 114       8.373 -13.947 -29.858  1.00 36.29           C  
-ATOM   2499  OG  SER B 114       7.494 -14.504 -30.804  1.00 35.30           O  
-ATOM   2500  N   TYR B 115       5.635 -12.500 -29.336  1.00 36.85           N  
-ATOM   2501  CA  TYR B 115       4.765 -11.323 -29.485  1.00 38.51           C  
-ATOM   2502  C   TYR B 115       4.253 -10.760 -28.151  1.00 42.13           C  
-ATOM   2503  O   TYR B 115       4.132  -9.545 -28.000  1.00 41.59           O  
-ATOM   2504  CB  TYR B 115       3.549 -11.605 -30.385  1.00 53.13           C  
-ATOM   2505  CG  TYR B 115       3.863 -12.173 -31.749  1.00 62.13           C  
-ATOM   2506  CD1 TYR B 115       3.069 -13.179 -32.300  1.00 58.93           C  
-ATOM   2507  CD2 TYR B 115       4.951 -11.712 -32.488  1.00 60.99           C  
-ATOM   2508  CE1 TYR B 115       3.351 -13.715 -33.552  1.00 66.99           C  
-ATOM   2509  CE2 TYR B 115       5.248 -12.243 -33.748  1.00 63.92           C  
-ATOM   2510  CZ  TYR B 115       4.444 -13.246 -34.277  1.00 70.87           C  
-ATOM   2511  OH  TYR B 115       4.718 -13.783 -35.528  1.00 65.82           O  
-ATOM   2512  N   GLU B 116       3.927 -11.644 -27.204  1.00 44.63           N  
-ATOM   2513  CA  GLU B 116       3.485 -11.232 -25.874  1.00 37.99           C  
-ATOM   2514  C   GLU B 116       4.662 -10.778 -25.020  1.00 36.24           C  
-ATOM   2515  O   GLU B 116       4.488 -10.012 -24.062  1.00 34.25           O  
-ATOM   2516  CB  GLU B 116       2.784 -12.384 -25.160  1.00 33.94           C  
-ATOM   2517  CG  GLU B 116       1.844 -13.168 -26.023  1.00 41.07           C  
-ATOM   2518  CD  GLU B 116       0.595 -12.393 -26.345  1.00 48.46           C  
-ATOM   2519  OE1 GLU B 116       0.456 -11.276 -25.801  1.00 40.59           O  
-ATOM   2520  OE2 GLU B 116      -0.236 -12.899 -27.140  1.00 51.56           O  
-ATOM   2521  N   SER B 117       5.849 -11.274 -25.363  1.00 37.55           N  
-ATOM   2522  CA  SER B 117       7.069 -10.994 -24.607  1.00 42.74           C  
-ATOM   2523  C   SER B 117       7.254  -9.501 -24.356  1.00 39.39           C  
-ATOM   2524  O   SER B 117       7.433  -8.732 -25.298  1.00 45.04           O  
-ATOM   2525  CB  SER B 117       8.279 -11.544 -25.353  1.00 42.94           C  
-ATOM   2526  OG  SER B 117       9.487 -11.147 -24.725  1.00 55.47           O  
-ATOM   2527  N   GLY B 118       7.209  -9.096 -23.092  1.00 24.61           N  
-ATOM   2528  CA  GLY B 118       7.307  -7.691 -22.776  1.00 28.02           C  
-ATOM   2529  C   GLY B 118       6.166  -7.146 -21.933  1.00 37.65           C  
-ATOM   2530  O   GLY B 118       6.349  -6.159 -21.212  1.00 42.90           O  
-ATOM   2531  N   LEU B 119       4.995  -7.773 -22.015  1.00 33.60           N  
-ATOM   2532  CA  LEU B 119       3.835  -7.349 -21.227  1.00 35.81           C  
-ATOM   2533  C   LEU B 119       4.057  -7.545 -19.734  1.00 37.91           C  
-ATOM   2534  O   LEU B 119       4.844  -8.406 -19.329  1.00 31.29           O  
-ATOM   2535  CB  LEU B 119       2.595  -8.151 -21.614  1.00 30.93           C  
-ATOM   2536  CG  LEU B 119       2.056  -8.036 -23.028  1.00 35.23           C  
-ATOM   2537  CD1 LEU B 119       1.023  -9.123 -23.245  1.00 41.15           C  
-ATOM   2538  CD2 LEU B 119       1.465  -6.652 -23.263  1.00 30.59           C  
-ATOM   2539  N   PRO B 120       3.338  -6.761 -18.914  1.00 31.80           N  
-ATOM   2540  CA  PRO B 120       3.319  -6.932 -17.462  1.00 31.61           C  
-ATOM   2541  C   PRO B 120       3.115  -8.401 -17.099  1.00 36.59           C  
-ATOM   2542  O   PRO B 120       2.276  -9.080 -17.702  1.00 29.50           O  
-ATOM   2543  CB  PRO B 120       2.112  -6.103 -17.030  1.00 28.48           C  
-ATOM   2544  CG  PRO B 120       2.006  -5.028 -18.073  1.00 27.10           C  
-ATOM   2545  CD  PRO B 120       2.484  -5.642 -19.358  1.00 27.40           C  
-ATOM   2546  N   LYS B 121       3.892  -8.877 -16.131  1.00 34.91           N  
-ATOM   2547  CA  LYS B 121       3.876 -10.275 -15.738  1.00 31.66           C  
-ATOM   2548  C   LYS B 121       2.986 -10.459 -14.515  1.00 33.15           C  
-ATOM   2549  O   LYS B 121       3.176  -9.788 -13.507  1.00 38.08           O  
-ATOM   2550  CB  LYS B 121       5.299 -10.774 -15.456  1.00 31.92           C  
-ATOM   2551  CG  LYS B 121       5.369 -12.185 -14.905  1.00 31.63           C  
-ATOM   2552  CD  LYS B 121       6.798 -12.630 -14.649  1.00 36.75           C  
-ATOM   2553  CE  LYS B 121       6.833 -13.975 -13.907  1.00 50.89           C  
-ATOM   2554  NZ  LYS B 121       8.086 -14.763 -14.127  1.00 52.72           N  
-ATOM   2555  N   PRO B 122       2.001 -11.368 -14.618  1.00 30.86           N  
-ATOM   2556  CA  PRO B 122       1.044 -11.762 -13.581  1.00 30.34           C  
-ATOM   2557  C   PRO B 122       1.716 -12.354 -12.365  1.00 35.11           C  
-ATOM   2558  O   PRO B 122       2.765 -12.991 -12.494  1.00 42.69           O  
-ATOM   2559  CB  PRO B 122       0.242 -12.867 -14.261  1.00 32.43           C  
-ATOM   2560  CG  PRO B 122       0.343 -12.553 -15.718  1.00 35.13           C  
-ATOM   2561  CD  PRO B 122       1.735 -12.058 -15.891  1.00 28.80           C  
-ATOM   2562  N   ASP B 123       1.104 -12.165 -11.202  1.00 37.08           N  
-ATOM   2563  CA  ASP B 123       1.640 -12.677  -9.933  1.00 34.02           C  
-ATOM   2564  C   ASP B 123       0.919 -13.957  -9.597  1.00 35.65           C  
-ATOM   2565  O   ASP B 123       1.339 -14.728  -8.740  1.00 44.64           O  
-ATOM   2566  CB  ASP B 123       1.400 -11.669  -8.811  1.00 32.33           C  
-ATOM   2567  CG  ASP B 123       2.144 -10.373  -9.032  1.00 39.56           C  
-ATOM   2568  OD1 ASP B 123       3.393 -10.435  -9.113  1.00 38.43           O  
-ATOM   2569  OD2 ASP B 123       1.489  -9.300  -9.121  1.00 30.80           O  
-ATOM   2570  N   LEU B 124      -0.182 -14.172 -10.298  1.00 39.15           N  
-ATOM   2571  CA  LEU B 124      -1.079 -15.263 -10.006  1.00 31.86           C  
-ATOM   2572  C   LEU B 124      -1.885 -15.497 -11.247  1.00 24.04           C  
-ATOM   2573  O   LEU B 124      -2.464 -14.565 -11.789  1.00 31.22           O  
-ATOM   2574  CB  LEU B 124      -2.018 -14.846  -8.881  1.00 31.45           C  
-ATOM   2575  CG  LEU B 124      -2.913 -15.954  -8.347  1.00 31.00           C  
-ATOM   2576  CD1 LEU B 124      -2.077 -17.193  -8.061  1.00 29.48           C  
-ATOM   2577  CD2 LEU B 124      -3.662 -15.483  -7.103  1.00 34.10           C  
-ATOM   2578  N   VAL B 125      -1.929 -16.729 -11.705  1.00 21.22           N  
-ATOM   2579  CA  VAL B 125      -2.782 -17.042 -12.842  1.00 30.29           C  
-ATOM   2580  C   VAL B 125      -3.760 -18.152 -12.470  1.00 26.62           C  
-ATOM   2581  O   VAL B 125      -3.389 -19.295 -12.252  1.00 26.05           O  
-ATOM   2582  CB  VAL B 125      -1.971 -17.417 -14.101  1.00 29.79           C  
-ATOM   2583  CG1 VAL B 125      -2.866 -17.382 -15.310  1.00 31.44           C  
-ATOM   2584  CG2 VAL B 125      -0.815 -16.463 -14.291  1.00 20.76           C  
-ATOM   2585  N   ILE B 126      -5.026 -17.806 -12.376  1.00 30.63           N  
-ATOM   2586  CA  ILE B 126      -5.980 -18.783 -11.923  1.00 32.20           C  
-ATOM   2587  C   ILE B 126      -6.601 -19.465 -13.112  1.00 40.34           C  
-ATOM   2588  O   ILE B 126      -7.305 -18.848 -13.909  1.00 41.86           O  
-ATOM   2589  CB  ILE B 126      -7.017 -18.158 -10.997  1.00 30.08           C  
-ATOM   2590  CG1 ILE B 126      -6.300 -17.676  -9.721  1.00 26.75           C  
-ATOM   2591  CG2 ILE B 126      -8.116 -19.163 -10.706  1.00 24.80           C  
-ATOM   2592  CD1 ILE B 126      -7.121 -16.802  -8.831  1.00 32.40           C  
-ATOM   2593  N   PHE B 127      -6.289 -20.745 -13.246  1.00 39.39           N  
-ATOM   2594  CA  PHE B 127      -6.830 -21.554 -14.317  1.00 31.39           C  
-ATOM   2595  C   PHE B 127      -8.053 -22.364 -13.853  1.00 35.36           C  
-ATOM   2596  O   PHE B 127      -7.997 -23.123 -12.876  1.00 31.24           O  
-ATOM   2597  CB  PHE B 127      -5.741 -22.467 -14.861  1.00 34.25           C  
-ATOM   2598  CG  PHE B 127      -6.169 -23.270 -16.049  1.00 44.58           C  
-ATOM   2599  CD1 PHE B 127      -6.073 -22.740 -17.319  1.00 32.77           C  
-ATOM   2600  CD2 PHE B 127      -6.684 -24.552 -15.891  1.00 42.11           C  
-ATOM   2601  CE1 PHE B 127      -6.472 -23.464 -18.399  1.00 33.48           C  
-ATOM   2602  CE2 PHE B 127      -7.086 -25.284 -16.971  1.00 37.61           C  
-ATOM   2603  CZ  PHE B 127      -6.982 -24.741 -18.232  1.00 43.28           C  
-ATOM   2604  N   LEU B 128      -9.161 -22.190 -14.561  1.00 35.62           N  
-ATOM   2605  CA  LEU B 128     -10.395 -22.893 -14.233  1.00 35.76           C  
-ATOM   2606  C   LEU B 128     -10.570 -24.133 -15.089  1.00 29.49           C  
-ATOM   2607  O   LEU B 128     -10.785 -24.036 -16.281  1.00 32.48           O  
-ATOM   2608  CB  LEU B 128     -11.613 -21.969 -14.418  1.00 28.31           C  
-ATOM   2609  CG  LEU B 128     -11.979 -21.005 -13.288  1.00 30.90           C  
-ATOM   2610  CD1 LEU B 128     -10.744 -20.391 -12.652  1.00 29.34           C  
-ATOM   2611  CD2 LEU B 128     -12.922 -19.928 -13.776  1.00 32.22           C  
-ATOM   2612  N   GLU B 129     -10.495 -25.299 -14.471  1.00 35.81           N  
-ATOM   2613  CA  GLU B 129     -10.791 -26.536 -15.173  1.00 39.58           C  
-ATOM   2614  C   GLU B 129     -12.260 -26.618 -15.595  1.00 41.83           C  
-ATOM   2615  O   GLU B 129     -13.154 -26.191 -14.857  1.00 41.63           O  
-ATOM   2616  CB  GLU B 129     -10.428 -27.745 -14.304  1.00 38.68           C  
-ATOM   2617  CG  GLU B 129      -8.942 -27.949 -14.099  1.00 34.11           C  
-ATOM   2618  CD  GLU B 129      -8.606 -29.368 -13.677  1.00 64.58           C  
-ATOM   2619  OE1 GLU B 129      -9.431 -30.001 -12.975  1.00 61.76           O  
-ATOM   2620  OE2 GLU B 129      -7.516 -29.855 -14.054  1.00 79.93           O  
-ATOM   2621  N   SER B 130     -12.500 -27.163 -16.790  1.00 60.25           N  
-ATOM   2622  CA  SER B 130     -13.860 -27.438 -17.268  1.00 66.21           C  
-ATOM   2623  C   SER B 130     -14.107 -28.945 -17.272  1.00 61.95           C  
-ATOM   2624  O   SER B 130     -13.390 -29.695 -17.938  1.00 57.55           O  
-ATOM   2625  CB  SER B 130     -14.087 -26.882 -18.683  1.00 44.00           C  
-ATOM   2626  OG  SER B 130     -13.458 -25.634 -18.851  1.00 44.40           O  
-ATOM   2627  N   GLY B 131     -15.120 -29.385 -16.531  1.00 53.65           N  
-ATOM   2628  CA  GLY B 131     -15.470 -30.794 -16.487  1.00 63.14           C  
-ATOM   2629  C   GLY B 131     -16.419 -31.197 -17.602  1.00 75.20           C  
-ATOM   2630  O   GLY B 131     -16.372 -30.650 -18.703  1.00 70.92           O  
-ATOM   2631  N   SER B 132     -17.285 -32.162 -17.317  1.00 90.20           N  
-ATOM   2632  CA  SER B 132     -18.289 -32.617 -18.283  1.00 89.05           C  
-ATOM   2633  C   SER B 132     -19.234 -31.491 -18.703  1.00 78.41           C  
-ATOM   2634  O   SER B 132     -19.154 -30.976 -19.819  1.00 64.76           O  
-ATOM   2635  CB  SER B 132     -19.094 -33.792 -17.700  1.00 93.23           C  
-ATOM   2636  OG  SER B 132     -20.240 -34.098 -18.486  1.00 76.86           O  
-ATOM   2637  N   LYS B 133     -20.122 -31.108 -17.790  1.00 82.28           N  
-ATOM   2638  CA  LYS B 133     -21.186 -30.163 -18.097  1.00 80.76           C  
-ATOM   2639  C   LYS B 133     -20.676 -28.774 -18.454  1.00 74.60           C  
-ATOM   2640  O   LYS B 133     -21.466 -27.851 -18.618  1.00 80.79           O  
-ATOM   2641  N   GLU B 134     -19.363 -28.619 -18.576  1.00 81.34           N  
-ATOM   2642  CA  GLU B 134     -18.797 -27.316 -18.925  1.00 78.46           C  
-ATOM   2643  C   GLU B 134     -18.191 -27.276 -20.326  1.00 75.93           C  
-ATOM   2644  O   GLU B 134     -18.424 -26.322 -21.069  1.00 73.02           O  
-ATOM   2645  CB  GLU B 134     -17.766 -26.838 -17.896  1.00 74.83           C  
-ATOM   2646  CG  GLU B 134     -18.341 -26.396 -16.567  1.00 72.01           C  
-ATOM   2647  CD  GLU B 134     -18.108 -27.413 -15.455  1.00 82.17           C  
-ATOM   2648  OE1 GLU B 134     -18.176 -27.015 -14.273  1.00 92.02           O  
-ATOM   2649  OE2 GLU B 134     -17.852 -28.602 -15.754  1.00 68.24           O  
-ATOM   2650  N   ILE B 135     -17.398 -28.283 -20.687  1.00 69.40           N  
-ATOM   2651  CA  ILE B 135     -16.878 -28.338 -22.049  1.00 67.36           C  
-ATOM   2652  C   ILE B 135     -18.062 -28.424 -23.006  1.00 73.69           C  
-ATOM   2653  O   ILE B 135     -18.142 -27.679 -23.984  1.00 69.38           O  
-ATOM   2654  CB  ILE B 135     -15.933 -29.536 -22.290  1.00 58.28           C  
-ATOM   2655  CG1 ILE B 135     -14.699 -29.456 -21.385  1.00 82.25           C  
-ATOM   2656  CG2 ILE B 135     -15.461 -29.539 -23.722  1.00 65.01           C  
-ATOM   2657  CD1 ILE B 135     -13.574 -30.457 -21.737  1.00 71.57           C  
-ATOM   2658  N   ASN B 136     -18.993 -29.327 -22.699  1.00 77.09           N  
-ATOM   2659  CA  ASN B 136     -20.161 -29.552 -23.549  1.00 69.17           C  
-ATOM   2660  C   ASN B 136     -21.170 -28.420 -23.450  1.00 60.47           C  
-ATOM   2661  O   ASN B 136     -22.305 -28.530 -23.906  1.00 63.11           O  
-ATOM   2662  CB  ASN B 136     -20.809 -30.909 -23.252  1.00 68.58           C  
-ATOM   2663  CG  ASN B 136     -19.867 -32.066 -23.520  1.00 84.54           C  
-ATOM   2664  OD1 ASN B 136     -18.920 -32.300 -22.760  1.00 86.60           O  
-ATOM   2665  ND2 ASN B 136     -20.108 -32.787 -24.612  1.00 79.03           N  
-ATOM   2666  N   ARG B 137     -20.739 -27.325 -22.848  1.00 59.52           N  
-ATOM   2667  CA  ARG B 137     -21.518 -26.100 -22.841  1.00 66.70           C  
-ATOM   2668  C   ARG B 137     -21.260 -25.324 -24.127  1.00 64.53           C  
-ATOM   2669  O   ARG B 137     -22.008 -24.411 -24.470  1.00 57.21           O  
-ATOM   2670  CB  ARG B 137     -21.124 -25.235 -21.639  1.00 70.57           C  
-ATOM   2671  CG  ARG B 137     -22.051 -25.321 -20.450  1.00 71.58           C  
-ATOM   2672  CD  ARG B 137     -23.428 -24.773 -20.807  1.00 92.11           C  
-ATOM   2673  NE  ARG B 137     -24.146 -24.252 -19.644  1.00112.45           N  
-ATOM   2674  CZ  ARG B 137     -24.973 -24.966 -18.882  1.00110.86           C  
-ATOM   2675  NH1 ARG B 137     -25.194 -26.248 -19.154  1.00100.57           N  
-ATOM   2676  NH2 ARG B 137     -25.581 -24.395 -17.846  1.00 85.11           N  
-ATOM   2677  N   ASN B 138     -20.181 -25.684 -24.822  1.00 62.64           N  
-ATOM   2678  CA  ASN B 138     -19.763 -25.007 -26.053  1.00 64.15           C  
-ATOM   2679  C   ASN B 138     -20.628 -25.375 -27.267  1.00 63.79           C  
-ATOM   2680  O   ASN B 138     -20.496 -26.461 -27.833  1.00 58.71           O  
-ATOM   2681  CB  ASN B 138     -18.282 -25.303 -26.345  1.00 59.86           C  
-ATOM   2682  CG  ASN B 138     -17.330 -24.535 -25.427  1.00 66.25           C  
-ATOM   2683  OD1 ASN B 138     -17.329 -23.300 -25.408  1.00 56.68           O  
-ATOM   2684  ND2 ASN B 138     -16.506 -25.267 -24.673  1.00 61.45           N  
-ATOM   2685  N   VAL B 139     -21.505 -24.461 -27.667  1.00 54.01           N  
-ATOM   2686  CA  VAL B 139     -22.444 -24.727 -28.752  1.00 50.63           C  
-ATOM   2687  C   VAL B 139     -22.223 -23.830 -29.977  1.00 58.54           C  
-ATOM   2688  O   VAL B 139     -23.139 -23.594 -30.765  1.00 47.46           O  
-ATOM   2689  CB  VAL B 139     -23.887 -24.568 -28.270  1.00 51.79           C  
-ATOM   2690  CG1 VAL B 139     -24.206 -25.657 -27.263  1.00 48.29           C  
-ATOM   2691  CG2 VAL B 139     -24.103 -23.166 -27.671  1.00 50.97           C  
-ATOM   2692  N   GLY B 140     -21.010 -23.316 -30.123  1.00 61.26           N  
-ATOM   2693  CA  GLY B 140     -20.619 -22.629 -31.339  1.00 47.76           C  
-ATOM   2694  C   GLY B 140     -21.335 -21.335 -31.672  1.00 45.63           C  
-ATOM   2695  O   GLY B 140     -21.402 -20.950 -32.832  1.00 40.54           O  
-ATOM   2696  N   GLU B 141     -21.862 -20.643 -30.671  1.00 51.74           N  
-ATOM   2697  CA  GLU B 141     -22.440 -19.327 -30.944  1.00 53.43           C  
-ATOM   2698  C   GLU B 141     -21.337 -18.357 -31.354  1.00 41.87           C  
-ATOM   2699  O   GLU B 141     -21.586 -17.371 -32.036  1.00 50.13           O  
-ATOM   2700  CB  GLU B 141     -23.246 -18.783 -29.754  1.00 43.21           C  
-ATOM   2701  CG  GLU B 141     -22.592 -19.056 -28.402  1.00 82.64           C  
-ATOM   2702  CD  GLU B 141     -23.529 -18.843 -27.217  1.00 90.55           C  
-ATOM   2703  OE1 GLU B 141     -24.346 -17.891 -27.272  1.00 87.13           O  
-ATOM   2704  OE2 GLU B 141     -23.432 -19.625 -26.235  1.00 66.72           O  
-ATOM   2705  N   GLU B 142     -20.114 -18.643 -30.943  1.00 37.02           N  
-ATOM   2706  CA  GLU B 142     -18.973 -17.861 -31.400  1.00 40.39           C  
-ATOM   2707  C   GLU B 142     -17.900 -18.755 -32.015  1.00 38.50           C  
-ATOM   2708  O   GLU B 142     -17.970 -19.982 -31.926  1.00 38.04           O  
-ATOM   2709  CB  GLU B 142     -18.415 -16.992 -30.273  1.00 56.48           C  
-ATOM   2710  CG  GLU B 142     -19.299 -15.789 -29.927  1.00 51.63           C  
-ATOM   2711  CD  GLU B 142     -18.552 -14.705 -29.147  1.00 61.65           C  
-ATOM   2712  OE1 GLU B 142     -17.586 -15.033 -28.408  1.00 61.14           O  
-ATOM   2713  OE2 GLU B 142     -18.938 -13.521 -29.281  1.00 46.37           O  
-ATOM   2714  N   ILE B 143     -16.904 -18.145 -32.638  1.00 41.98           N  
-ATOM   2715  CA  ILE B 143     -16.075 -18.894 -33.578  1.00 47.40           C  
-ATOM   2716  C   ILE B 143     -15.250 -20.046 -32.974  1.00 42.40           C  
-ATOM   2717  O   ILE B 143     -15.226 -21.150 -33.527  1.00 50.24           O  
-ATOM   2718  CB  ILE B 143     -15.224 -17.962 -34.482  1.00 45.53           C  
-ATOM   2719  CG1 ILE B 143     -14.843 -18.687 -35.787  1.00 50.80           C  
-ATOM   2720  CG2 ILE B 143     -14.030 -17.454 -33.742  1.00 39.87           C  
-ATOM   2721  CD1 ILE B 143     -13.865 -17.932 -36.707  1.00 41.40           C  
-ATOM   2722  N   TYR B 144     -14.603 -19.818 -31.841  1.00 41.05           N  
-ATOM   2723  CA  TYR B 144     -13.785 -20.875 -31.242  1.00 43.11           C  
-ATOM   2724  C   TYR B 144     -14.606 -21.819 -30.383  1.00 45.87           C  
-ATOM   2725  O   TYR B 144     -14.062 -22.781 -29.831  1.00 47.76           O  
-ATOM   2726  CB  TYR B 144     -12.651 -20.291 -30.396  1.00 37.22           C  
-ATOM   2727  CG  TYR B 144     -11.662 -19.481 -31.189  1.00 41.85           C  
-ATOM   2728  CD1 TYR B 144     -10.745 -20.105 -32.025  1.00 37.32           C  
-ATOM   2729  CD2 TYR B 144     -11.643 -18.092 -31.107  1.00 41.22           C  
-ATOM   2730  CE1 TYR B 144      -9.835 -19.378 -32.760  1.00 45.83           C  
-ATOM   2731  CE2 TYR B 144     -10.729 -17.347 -31.852  1.00 47.06           C  
-ATOM   2732  CZ  TYR B 144      -9.819 -18.000 -32.678  1.00 51.12           C  
-ATOM   2733  OH  TYR B 144      -8.890 -17.280 -33.421  1.00 52.43           O  
-ATOM   2734  N   GLU B 145     -15.905 -21.550 -30.258  1.00 36.42           N  
-ATOM   2735  CA  GLU B 145     -16.748 -22.368 -29.383  1.00 49.98           C  
-ATOM   2736  C   GLU B 145     -17.108 -23.751 -29.947  1.00 40.77           C  
-ATOM   2737  O   GLU B 145     -18.259 -24.071 -30.191  1.00 33.03           O  
-ATOM   2738  CB  GLU B 145     -17.977 -21.591 -28.907  1.00 42.68           C  
-ATOM   2739  CG  GLU B 145     -17.618 -20.418 -27.986  1.00 43.95           C  
-ATOM   2740  CD  GLU B 145     -18.827 -19.598 -27.581  1.00 58.72           C  
-ATOM   2741  OE1 GLU B 145     -19.948 -20.015 -27.949  1.00 66.86           O  
-ATOM   2742  OE2 GLU B 145     -18.664 -18.552 -26.903  1.00 52.42           O  
-ATOM   2743  N   ASP B 146     -16.089 -24.580 -30.113  1.00 35.22           N  
-ATOM   2744  CA  ASP B 146     -16.285 -25.939 -30.562  1.00 47.00           C  
-ATOM   2745  C   ASP B 146     -15.498 -26.938 -29.717  1.00 47.06           C  
-ATOM   2746  O   ASP B 146     -14.277 -26.892 -29.659  1.00 52.82           O  
-ATOM   2747  CB  ASP B 146     -15.898 -26.066 -32.037  1.00 62.21           C  
-ATOM   2748  CG  ASP B 146     -15.781 -27.521 -32.489  1.00 79.95           C  
-ATOM   2749  OD1 ASP B 146     -16.509 -28.390 -31.933  1.00 79.63           O  
-ATOM   2750  OD2 ASP B 146     -14.965 -27.794 -33.406  1.00 81.33           O  
-ATOM   2751  N   VAL B 147     -16.229 -27.840 -29.082  1.00 43.20           N  
-ATOM   2752  CA  VAL B 147     -15.690 -28.909 -28.257  1.00 45.03           C  
-ATOM   2753  C   VAL B 147     -14.378 -29.541 -28.746  1.00 60.32           C  
-ATOM   2754  O   VAL B 147     -13.411 -29.651 -27.986  1.00 64.74           O  
-ATOM   2755  CB  VAL B 147     -16.735 -30.031 -28.138  1.00 60.84           C  
-ATOM   2756  CG1 VAL B 147     -16.340 -31.037 -27.057  1.00 67.03           C  
-ATOM   2757  CG2 VAL B 147     -18.124 -29.434 -27.882  1.00 65.12           C  
-ATOM   2758  N   THR B 148     -14.347 -29.986 -30.000  1.00 63.35           N  
-ATOM   2759  CA  THR B 148     -13.155 -30.644 -30.534  1.00 61.27           C  
-ATOM   2760  C   THR B 148     -11.960 -29.678 -30.607  1.00 51.46           C  
-ATOM   2761  O   THR B 148     -10.815 -30.088 -30.439  1.00 47.97           O  
-ATOM   2762  CB  THR B 148     -13.421 -31.338 -31.913  1.00 61.43           C  
-ATOM   2763  OG1 THR B 148     -13.689 -30.355 -32.920  1.00 82.89           O  
-ATOM   2764  CG2 THR B 148     -14.604 -32.290 -31.828  1.00 48.29           C  
-ATOM   2765  N   PHE B 149     -12.226 -28.398 -30.838  1.00 42.39           N  
-ATOM   2766  CA  PHE B 149     -11.145 -27.420 -30.884  1.00 51.64           C  
-ATOM   2767  C   PHE B 149     -10.634 -27.034 -29.484  1.00 52.53           C  
-ATOM   2768  O   PHE B 149      -9.420 -26.882 -29.278  1.00 41.96           O  
-ATOM   2769  CB  PHE B 149     -11.545 -26.172 -31.685  1.00 48.68           C  
-ATOM   2770  CG  PHE B 149     -10.479 -25.110 -31.713  1.00 42.63           C  
-ATOM   2771  CD1 PHE B 149      -9.303 -25.310 -32.425  1.00 49.18           C  
-ATOM   2772  CD2 PHE B 149     -10.641 -23.919 -31.014  1.00 43.83           C  
-ATOM   2773  CE1 PHE B 149      -8.295 -24.335 -32.453  1.00 46.37           C  
-ATOM   2774  CE2 PHE B 149      -9.645 -22.939 -31.035  1.00 53.32           C  
-ATOM   2775  CZ  PHE B 149      -8.466 -23.148 -31.762  1.00 45.16           C  
-ATOM   2776  N   GLN B 150     -11.562 -26.874 -28.537  1.00 45.75           N  
-ATOM   2777  CA  GLN B 150     -11.228 -26.550 -27.152  1.00 41.82           C  
-ATOM   2778  C   GLN B 150     -10.342 -27.624 -26.529  1.00 45.36           C  
-ATOM   2779  O   GLN B 150      -9.400 -27.317 -25.802  1.00 46.02           O  
-ATOM   2780  CB  GLN B 150     -12.493 -26.368 -26.321  1.00 46.94           C  
-ATOM   2781  CG  GLN B 150     -13.453 -25.306 -26.862  1.00 57.24           C  
-ATOM   2782  CD  GLN B 150     -13.169 -23.900 -26.341  1.00 55.57           C  
-ATOM   2783  OE1 GLN B 150     -12.224 -23.676 -25.579  1.00 45.90           O  
-ATOM   2784  NE2 GLN B 150     -14.001 -22.945 -26.752  1.00 43.54           N  
-ATOM   2785  N   GLN B 151     -10.636 -28.883 -26.825  1.00 49.21           N  
-ATOM   2786  CA  GLN B 151      -9.764 -29.979 -26.412  1.00 52.19           C  
-ATOM   2787  C   GLN B 151      -8.306 -29.777 -26.869  1.00 49.14           C  
-ATOM   2788  O   GLN B 151      -7.351 -30.204 -26.209  1.00 43.44           O  
-ATOM   2789  CB  GLN B 151     -10.315 -31.308 -26.929  1.00 50.83           C  
-ATOM   2790  CG  GLN B 151      -9.650 -32.526 -26.293  1.00 69.88           C  
-ATOM   2791  CD  GLN B 151      -9.691 -32.504 -24.755  1.00 88.06           C  
-ATOM   2792  OE1 GLN B 151     -10.589 -31.904 -24.149  1.00 77.64           O  
-ATOM   2793  NE2 GLN B 151      -8.718 -33.165 -24.124  1.00 72.45           N  
-ATOM   2794  N   LYS B 152      -8.157 -29.113 -28.008  1.00 47.75           N  
-ATOM   2795  CA  LYS B 152      -6.858 -28.807 -28.574  1.00 46.65           C  
-ATOM   2796  C   LYS B 152      -6.167 -27.645 -27.852  1.00 47.90           C  
-ATOM   2797  O   LYS B 152      -4.954 -27.679 -27.618  1.00 41.10           O  
-ATOM   2798  CB  LYS B 152      -7.032 -28.496 -30.057  1.00 50.46           C  
-ATOM   2799  CG  LYS B 152      -7.232 -29.725 -30.925  1.00 60.54           C  
-ATOM   2800  CD  LYS B 152      -5.890 -30.345 -31.281  1.00 87.22           C  
-ATOM   2801  CE  LYS B 152      -6.047 -31.572 -32.163  1.00 95.03           C  
-ATOM   2802  NZ  LYS B 152      -4.766 -31.960 -32.821  1.00 93.59           N  
-ATOM   2803  N   VAL B 153      -6.940 -26.613 -27.508  1.00 51.64           N  
-ATOM   2804  CA  VAL B 153      -6.423 -25.463 -26.754  1.00 51.76           C  
-ATOM   2805  C   VAL B 153      -5.875 -25.903 -25.401  1.00 46.16           C  
-ATOM   2806  O   VAL B 153      -4.815 -25.457 -24.960  1.00 39.68           O  
-ATOM   2807  CB  VAL B 153      -7.510 -24.399 -26.490  1.00 40.80           C  
-ATOM   2808  CG1 VAL B 153      -6.884 -23.192 -25.832  1.00 40.79           C  
-ATOM   2809  CG2 VAL B 153      -8.209 -23.998 -27.778  1.00 38.94           C  
-ATOM   2810  N   LEU B 154      -6.624 -26.785 -24.756  1.00 37.56           N  
-ATOM   2811  CA  LEU B 154      -6.263 -27.339 -23.470  1.00 35.69           C  
-ATOM   2812  C   LEU B 154      -4.893 -27.996 -23.454  1.00 41.00           C  
-ATOM   2813  O   LEU B 154      -4.164 -27.874 -22.477  1.00 42.31           O  
-ATOM   2814  CB  LEU B 154      -7.312 -28.364 -23.064  1.00 47.59           C  
-ATOM   2815  CG  LEU B 154      -7.238 -28.929 -21.648  1.00 45.12           C  
-ATOM   2816  CD1 LEU B 154      -7.275 -27.826 -20.609  1.00 42.83           C  
-ATOM   2817  CD2 LEU B 154      -8.390 -29.883 -21.453  1.00 36.90           C  
-ATOM   2818  N   GLN B 155      -4.565 -28.719 -24.523  1.00 47.38           N  
-ATOM   2819  CA  GLN B 155      -3.240 -29.312 -24.703  1.00 37.36           C  
-ATOM   2820  C   GLN B 155      -2.169 -28.243 -24.593  1.00 42.02           C  
-ATOM   2821  O   GLN B 155      -1.124 -28.456 -23.985  1.00 42.70           O  
-ATOM   2822  CB  GLN B 155      -3.137 -29.979 -26.082  1.00 54.38           C  
-ATOM   2823  CG  GLN B 155      -4.198 -31.032 -26.340  1.00 66.88           C  
-ATOM   2824  CD  GLN B 155      -4.292 -32.004 -25.185  1.00 88.20           C  
-ATOM   2825  OE1 GLN B 155      -3.417 -32.863 -25.008  1.00 78.22           O  
-ATOM   2826  NE2 GLN B 155      -5.348 -31.863 -24.374  1.00 70.99           N  
-ATOM   2827  N   GLU B 156      -2.442 -27.090 -25.193  1.00 45.02           N  
-ATOM   2828  CA  GLU B 156      -1.491 -25.985 -25.220  1.00 50.01           C  
-ATOM   2829  C   GLU B 156      -1.435 -25.246 -23.874  1.00 49.32           C  
-ATOM   2830  O   GLU B 156      -0.368 -24.758 -23.478  1.00 50.14           O  
-ATOM   2831  CB  GLU B 156      -1.818 -25.010 -26.363  1.00 49.05           C  
-ATOM   2832  CG  GLU B 156      -2.122 -25.676 -27.715  1.00 51.93           C  
-ATOM   2833  CD  GLU B 156      -0.954 -26.483 -28.303  1.00 60.55           C  
-ATOM   2834  OE1 GLU B 156       0.239 -26.115 -28.111  1.00 42.94           O  
-ATOM   2835  OE2 GLU B 156      -1.254 -27.491 -28.980  1.00 57.91           O  
-ATOM   2836  N   TYR B 157      -2.571 -25.160 -23.178  1.00 35.77           N  
-ATOM   2837  CA  TYR B 157      -2.589 -24.611 -21.821  1.00 39.64           C  
-ATOM   2838  C   TYR B 157      -1.720 -25.470 -20.889  1.00 47.74           C  
-ATOM   2839  O   TYR B 157      -0.798 -24.974 -20.224  1.00 38.74           O  
-ATOM   2840  CB  TYR B 157      -4.023 -24.525 -21.255  1.00 34.99           C  
-ATOM   2841  CG  TYR B 157      -4.745 -23.195 -21.444  1.00 25.25           C  
-ATOM   2842  CD1 TYR B 157      -6.080 -23.161 -21.803  1.00 24.99           C  
-ATOM   2843  CD2 TYR B 157      -4.089 -21.986 -21.271  1.00 27.69           C  
-ATOM   2844  CE1 TYR B 157      -6.755 -21.961 -21.981  1.00 28.36           C  
-ATOM   2845  CE2 TYR B 157      -4.744 -20.768 -21.456  1.00 27.25           C  
-ATOM   2846  CZ  TYR B 157      -6.084 -20.762 -21.810  1.00 35.49           C  
-ATOM   2847  OH  TYR B 157      -6.765 -19.567 -21.984  1.00 25.55           O  
-ATOM   2848  N   LYS B 158      -2.024 -26.763 -20.848  1.00 48.34           N  
-ATOM   2849  CA  LYS B 158      -1.291 -27.694 -19.996  1.00 56.22           C  
-ATOM   2850  C   LYS B 158       0.222 -27.573 -20.204  1.00 50.55           C  
-ATOM   2851  O   LYS B 158       0.980 -27.488 -19.240  1.00 58.28           O  
-ATOM   2852  CB  LYS B 158      -1.785 -29.139 -20.204  1.00 59.83           C  
-ATOM   2853  CG  LYS B 158      -3.222 -29.420 -19.685  1.00 55.32           C  
-ATOM   2854  CD  LYS B 158      -3.333 -29.286 -18.142  1.00 72.04           C  
-ATOM   2855  CE  LYS B 158      -4.774 -29.488 -17.624  1.00 72.53           C  
-ATOM   2856  NZ  LYS B 158      -5.051 -28.843 -16.282  1.00 39.39           N  
-ATOM   2857  N   LYS B 159       0.650 -27.541 -21.459  1.00 47.99           N  
-ATOM   2858  CA  LYS B 159       2.064 -27.335 -21.790  1.00 58.09           C  
-ATOM   2859  C   LYS B 159       2.681 -26.140 -21.043  1.00 50.50           C  
-ATOM   2860  O   LYS B 159       3.737 -26.260 -20.434  1.00 50.54           O  
-ATOM   2861  CB  LYS B 159       2.251 -27.159 -23.314  1.00 58.25           C  
-ATOM   2862  CG  LYS B 159       2.106 -28.448 -24.135  1.00 61.30           C  
-ATOM   2863  CD  LYS B 159       1.519 -28.200 -25.544  1.00 75.17           C  
-ATOM   2864  CE  LYS B 159       2.555 -28.272 -26.685  1.00 76.67           C  
-ATOM   2865  NZ  LYS B 159       3.425 -27.053 -26.826  1.00 74.77           N  
-ATOM   2866  N   MET B 160       2.015 -24.992 -21.095  1.00 50.47           N  
-ATOM   2867  CA  MET B 160       2.547 -23.752 -20.528  1.00 53.99           C  
-ATOM   2868  C   MET B 160       2.595 -23.753 -19.013  1.00 50.29           C  
-ATOM   2869  O   MET B 160       3.461 -23.127 -18.398  1.00 39.56           O  
-ATOM   2870  CB  MET B 160       1.682 -22.583 -20.959  1.00 48.98           C  
-ATOM   2871  CG  MET B 160       1.786 -22.246 -22.406  1.00 37.96           C  
-ATOM   2872  SD  MET B 160       0.989 -20.670 -22.680  1.00 40.13           S  
-ATOM   2873  CE  MET B 160      -0.735 -21.192 -22.686  1.00 31.11           C  
-ATOM   2874  N   ILE B 161       1.615 -24.420 -18.419  1.00 51.17           N  
-ATOM   2875  CA  ILE B 161       1.582 -24.633 -16.983  1.00 45.19           C  
-ATOM   2876  C   ILE B 161       2.828 -25.412 -16.544  1.00 46.04           C  
-ATOM   2877  O   ILE B 161       3.560 -24.977 -15.658  1.00 46.55           O  
-ATOM   2878  CB  ILE B 161       0.296 -25.379 -16.578  1.00 41.17           C  
-ATOM   2879  CG1 ILE B 161      -0.918 -24.473 -16.784  1.00 42.53           C  
-ATOM   2880  CG2 ILE B 161       0.355 -25.809 -15.143  1.00 44.35           C  
-ATOM   2881  CD1 ILE B 161      -2.223 -25.130 -16.460  1.00 34.83           C  
-ATOM   2882  N   GLU B 162       3.080 -26.549 -17.186  1.00 47.30           N  
-ATOM   2883  CA  GLU B 162       4.260 -27.361 -16.883  1.00 47.28           C  
-ATOM   2884  C   GLU B 162       5.607 -26.629 -17.023  1.00 48.47           C  
-ATOM   2885  O   GLU B 162       6.618 -27.086 -16.514  1.00 42.17           O  
-ATOM   2886  CB  GLU B 162       4.257 -28.620 -17.743  1.00 40.29           C  
-ATOM   2887  CG  GLU B 162       3.270 -29.667 -17.262  1.00 65.24           C  
-ATOM   2888  CD  GLU B 162       2.588 -30.432 -18.399  1.00107.51           C  
-ATOM   2889  OE1 GLU B 162       3.035 -30.319 -19.570  1.00100.78           O  
-ATOM   2890  OE2 GLU B 162       1.592 -31.147 -18.116  1.00100.44           O  
-ATOM   2891  N   GLU B 163       5.618 -25.502 -17.724  1.00 44.33           N  
-ATOM   2892  CA  GLU B 163       6.825 -24.696 -17.883  1.00 46.00           C  
-ATOM   2893  C   GLU B 163       7.054 -23.798 -16.669  1.00 48.77           C  
-ATOM   2894  O   GLU B 163       8.058 -23.089 -16.588  1.00 40.19           O  
-ATOM   2895  CB  GLU B 163       6.695 -23.775 -19.102  1.00 55.56           C  
-ATOM   2896  CG  GLU B 163       6.583 -24.437 -20.452  1.00 60.37           C  
-ATOM   2897  CD  GLU B 163       6.482 -23.411 -21.566  1.00 64.21           C  
-ATOM   2898  OE1 GLU B 163       5.856 -22.349 -21.341  1.00 59.52           O  
-ATOM   2899  OE2 GLU B 163       7.031 -23.665 -22.661  1.00 69.49           O  
-ATOM   2900  N   GLY B 164       6.095 -23.822 -15.752  1.00 50.46           N  
-ATOM   2901  CA  GLY B 164       5.962 -22.848 -14.681  1.00 47.56           C  
-ATOM   2902  C   GLY B 164       7.125 -21.971 -14.261  1.00 54.42           C  
-ATOM   2903  O   GLY B 164       7.910 -22.333 -13.378  1.00 57.94           O  
-ATOM   2904  N   ASP B 165       7.236 -20.805 -14.887  1.00 52.77           N  
-ATOM   2905  CA  ASP B 165       8.059 -19.737 -14.330  1.00 51.80           C  
-ATOM   2906  C   ASP B 165       7.040 -18.731 -13.859  1.00 56.03           C  
-ATOM   2907  O   ASP B 165       7.376 -17.664 -13.345  1.00 61.79           O  
-ATOM   2908  CB  ASP B 165       9.020 -19.118 -15.364  1.00 66.98           C  
-ATOM   2909  CG  ASP B 165       8.300 -18.559 -16.604  1.00 93.45           C  
-ATOM   2910  OD1 ASP B 165       8.590 -17.399 -16.997  1.00 73.95           O  
-ATOM   2911  OD2 ASP B 165       7.462 -19.284 -17.200  1.00 98.90           O  
-ATOM   2912  N   ILE B 166       5.779 -19.109 -14.052  1.00 49.43           N  
-ATOM   2913  CA  ILE B 166       4.633 -18.281 -13.716  1.00 52.48           C  
-ATOM   2914  C   ILE B 166       3.884 -18.922 -12.571  1.00 42.41           C  
-ATOM   2915  O   ILE B 166       3.680 -20.143 -12.572  1.00 42.67           O  
-ATOM   2916  CB  ILE B 166       3.658 -18.176 -14.922  1.00 61.77           C  
-ATOM   2917  CG1 ILE B 166       4.355 -17.554 -16.137  1.00 57.10           C  
-ATOM   2918  CG2 ILE B 166       2.388 -17.396 -14.557  1.00 40.76           C  
-ATOM   2919  CD1 ILE B 166       4.908 -16.175 -15.877  1.00 50.36           C  
-ATOM   2920  N   HIS B 167       3.453 -18.116 -11.601  1.00 35.55           N  
-ATOM   2921  CA  HIS B 167       2.672 -18.663 -10.492  1.00 36.82           C  
-ATOM   2922  C   HIS B 167       1.244 -19.040 -10.899  1.00 29.93           C  
-ATOM   2923  O   HIS B 167       0.387 -18.171 -11.023  1.00 34.20           O  
-ATOM   2924  CB  HIS B 167       2.629 -17.684  -9.329  1.00 35.23           C  
-ATOM   2925  CG  HIS B 167       2.053 -18.271  -8.075  1.00 47.44           C  
-ATOM   2926  ND1 HIS B 167       2.476 -17.900  -6.817  1.00 62.17           N  
-ATOM   2927  CD2 HIS B 167       1.107 -19.217  -7.892  1.00 46.48           C  
-ATOM   2928  CE1 HIS B 167       1.797 -18.582  -5.912  1.00 59.61           C  
-ATOM   2929  NE2 HIS B 167       0.961 -19.389  -6.536  1.00 41.21           N  
-ATOM   2930  N   TRP B 168       0.991 -20.332 -11.083  1.00 24.65           N  
-ATOM   2931  CA  TRP B 168      -0.343 -20.816 -11.462  1.00 39.43           C  
-ATOM   2932  C   TRP B 168      -1.125 -21.451 -10.306  1.00 36.50           C  
-ATOM   2933  O   TRP B 168      -0.584 -22.242  -9.542  1.00 32.97           O  
-ATOM   2934  CB  TRP B 168      -0.260 -21.897 -12.558  1.00 44.13           C  
-ATOM   2935  CG  TRP B 168       0.173 -21.486 -13.938  1.00 47.70           C  
-ATOM   2936  CD1 TRP B 168       1.455 -21.427 -14.412  1.00 51.66           C  
-ATOM   2937  CD2 TRP B 168      -0.678 -21.158 -15.049  1.00 49.45           C  
-ATOM   2938  NE1 TRP B 168       1.451 -21.052 -15.739  1.00 48.92           N  
-ATOM   2939  CE2 TRP B 168       0.159 -20.881 -16.150  1.00 41.77           C  
-ATOM   2940  CE3 TRP B 168      -2.064 -21.066 -15.215  1.00 51.83           C  
-ATOM   2941  CZ2 TRP B 168      -0.347 -20.509 -17.389  1.00 38.13           C  
-ATOM   2942  CZ3 TRP B 168      -2.563 -20.698 -16.459  1.00 49.26           C  
-ATOM   2943  CH2 TRP B 168      -1.705 -20.426 -17.525  1.00 43.65           C  
-ATOM   2944  N   GLN B 169      -2.415 -21.155 -10.223  1.00 35.00           N  
-ATOM   2945  CA  GLN B 169      -3.292 -21.907  -9.340  1.00 39.26           C  
-ATOM   2946  C   GLN B 169      -4.403 -22.566 -10.140  1.00 39.85           C  
-ATOM   2947  O   GLN B 169      -5.260 -21.877 -10.705  1.00 39.15           O  
-ATOM   2948  CB  GLN B 169      -3.872 -21.007  -8.241  1.00 43.66           C  
-ATOM   2949  CG  GLN B 169      -2.898 -20.709  -7.086  1.00 50.34           C  
-ATOM   2950  CD  GLN B 169      -2.472 -21.955  -6.325  1.00 42.51           C  
-ATOM   2951  OE1 GLN B 169      -1.294 -22.311  -6.316  1.00 34.89           O  
-ATOM   2952  NE2 GLN B 169      -3.431 -22.627  -5.691  1.00 43.70           N  
-ATOM   2953  N   ILE B 170      -4.381 -23.898 -10.184  1.00 41.02           N  
-ATOM   2954  CA  ILE B 170      -5.363 -24.684 -10.940  1.00 41.55           C  
-ATOM   2955  C   ILE B 170      -6.590 -25.106 -10.121  1.00 33.86           C  
-ATOM   2956  O   ILE B 170      -6.493 -25.901  -9.200  1.00 39.54           O  
-ATOM   2957  CB  ILE B 170      -4.703 -25.944 -11.492  1.00 38.59           C  
-ATOM   2958  CG1 ILE B 170      -3.444 -25.575 -12.263  1.00 39.52           C  
-ATOM   2959  CG2 ILE B 170      -5.676 -26.734 -12.344  1.00 41.09           C  
-ATOM   2960  CD1 ILE B 170      -2.390 -26.636 -12.183  1.00 45.62           C  
-ATOM   2961  N   ILE B 171      -7.754 -24.599 -10.477  1.00 31.12           N  
-ATOM   2962  CA  ILE B 171      -8.944 -24.923  -9.715  1.00 32.62           C  
-ATOM   2963  C   ILE B 171      -9.794 -26.002 -10.372  1.00 43.92           C  
-ATOM   2964  O   ILE B 171     -10.318 -25.815 -11.477  1.00 40.29           O  
-ATOM   2965  CB  ILE B 171      -9.806 -23.697  -9.528  1.00 31.09           C  
-ATOM   2966  CG1 ILE B 171      -8.948 -22.520  -9.084  1.00 31.98           C  
-ATOM   2967  CG2 ILE B 171     -10.904 -23.994  -8.553  1.00 36.52           C  
-ATOM   2968  CD1 ILE B 171      -8.340 -22.692  -7.742  1.00 32.09           C  
-ATOM   2969  N   SER B 172      -9.948 -27.117  -9.663  1.00 51.90           N  
-ATOM   2970  CA  SER B 172     -10.725 -28.260 -10.137  1.00 48.28           C  
-ATOM   2971  C   SER B 172     -12.134 -27.906 -10.559  1.00 50.93           C  
-ATOM   2972  O   SER B 172     -12.762 -26.997 -10.023  1.00 53.80           O  
-ATOM   2973  CB  SER B 172     -10.791 -29.352  -9.067  1.00 60.30           C  
-ATOM   2974  OG  SER B 172     -11.729 -30.352  -9.422  1.00 62.41           O  
-ATOM   2975  N   SER B 173     -12.619 -28.663 -11.528  1.00 52.41           N  
-ATOM   2976  CA  SER B 173     -13.986 -28.570 -12.014  1.00 58.53           C  
-ATOM   2977  C   SER B 173     -15.016 -29.018 -10.968  1.00 64.63           C  
-ATOM   2978  O   SER B 173     -16.158 -28.559 -10.968  1.00 53.46           O  
-ATOM   2979  CB  SER B 173     -14.080 -29.472 -13.227  1.00 49.57           C  
-ATOM   2980  OG  SER B 173     -13.028 -30.428 -13.153  1.00 45.02           O  
-ATOM   2981  N   GLU B 174     -14.580 -29.894 -10.067  1.00 55.96           N  
-ATOM   2982  CA  GLU B 174     -15.466 -30.664  -9.206  1.00 57.23           C  
-ATOM   2983  C   GLU B 174     -15.871 -29.973  -7.920  1.00 66.93           C  
-ATOM   2984  O   GLU B 174     -16.632 -30.523  -7.138  1.00 73.34           O  
-ATOM   2985  CB  GLU B 174     -14.802 -31.991  -8.852  1.00 75.95           C  
-ATOM   2986  CG  GLU B 174     -14.687 -32.954 -10.024  1.00 87.03           C  
-ATOM   2987  CD  GLU B 174     -13.637 -34.031  -9.799  1.00 89.29           C  
-ATOM   2988  OE1 GLU B 174     -12.429 -33.728  -9.941  1.00 89.85           O  
-ATOM   2989  OE2 GLU B 174     -14.023 -35.180  -9.494  1.00 75.11           O  
-ATOM   2990  N   PHE B 175     -15.359 -28.777  -7.684  1.00 68.21           N  
-ATOM   2991  CA  PHE B 175     -15.780 -28.028  -6.513  1.00 66.11           C  
-ATOM   2992  C   PHE B 175     -17.229 -27.551  -6.626  1.00 71.31           C  
-ATOM   2993  O   PHE B 175     -17.809 -27.541  -7.704  1.00 62.10           O  
-ATOM   2994  CB  PHE B 175     -14.822 -26.868  -6.230  1.00 59.27           C  
-ATOM   2995  CG  PHE B 175     -13.585 -27.293  -5.512  1.00 71.13           C  
-ATOM   2996  CD1 PHE B 175     -12.610 -28.025  -6.169  1.00 82.28           C  
-ATOM   2997  CD2 PHE B 175     -13.406 -26.998  -4.175  1.00 71.68           C  
-ATOM   2998  CE1 PHE B 175     -11.462 -28.443  -5.505  1.00 89.36           C  
-ATOM   2999  CE2 PHE B 175     -12.265 -27.412  -3.507  1.00 76.60           C  
-ATOM   3000  CZ  PHE B 175     -11.291 -28.134  -4.173  1.00 83.13           C  
-ATOM   3001  N   GLU B 176     -17.812 -27.170  -5.493  1.00 79.47           N  
-ATOM   3002  CA  GLU B 176     -19.178 -26.666  -5.455  1.00 71.84           C  
-ATOM   3003  C   GLU B 176     -19.173 -25.150  -5.584  1.00 68.69           C  
-ATOM   3004  O   GLU B 176     -18.313 -24.489  -5.014  1.00 69.43           O  
-ATOM   3005  CB  GLU B 176     -19.828 -27.052  -4.140  1.00 73.06           C  
-ATOM   3006  CG  GLU B 176     -21.299 -27.250  -4.262  1.00 75.70           C  
-ATOM   3007  CD  GLU B 176     -21.634 -28.154  -5.413  1.00 81.26           C  
-ATOM   3008  OE1 GLU B 176     -21.632 -29.389  -5.217  1.00 69.56           O  
-ATOM   3009  OE2 GLU B 176     -21.898 -27.625  -6.515  1.00 95.17           O  
-ATOM   3010  N   GLU B 177     -20.141 -24.601  -6.309  1.00 51.53           N  
-ATOM   3011  CA  GLU B 177     -20.113 -23.184  -6.658  1.00 59.15           C  
-ATOM   3012  C   GLU B 177     -19.687 -22.239  -5.537  1.00 65.80           C  
-ATOM   3013  O   GLU B 177     -18.777 -21.424  -5.708  1.00 69.65           O  
-ATOM   3014  CB  GLU B 177     -21.445 -22.734  -7.254  1.00 56.04           C  
-ATOM   3015  CG  GLU B 177     -21.518 -22.945  -8.765  1.00 87.09           C  
-ATOM   3016  CD  GLU B 177     -20.177 -22.689  -9.463  1.00110.73           C  
-ATOM   3017  OE1 GLU B 177     -19.614 -21.581  -9.303  1.00104.90           O  
-ATOM   3018  OE2 GLU B 177     -19.681 -23.595 -10.174  1.00102.70           O  
-ATOM   3019  N   ASP B 178     -20.351 -22.347  -4.398  1.00 58.77           N  
-ATOM   3020  CA  ASP B 178     -20.100 -21.471  -3.259  1.00 54.32           C  
-ATOM   3021  C   ASP B 178     -18.704 -21.697  -2.647  1.00 63.89           C  
-ATOM   3022  O   ASP B 178     -18.070 -20.763  -2.108  1.00 48.48           O  
-ATOM   3023  CB  ASP B 178     -21.192 -21.696  -2.202  1.00 80.28           C  
-ATOM   3024  CG  ASP B 178     -21.521 -23.188  -1.991  1.00 92.80           C  
-ATOM   3025  OD1 ASP B 178     -21.961 -23.863  -2.950  1.00 89.09           O  
-ATOM   3026  OD2 ASP B 178     -21.355 -23.687  -0.857  1.00 95.90           O  
-ATOM   3027  N   VAL B 179     -18.246 -22.949  -2.738  1.00 58.40           N  
-ATOM   3028  CA  VAL B 179     -16.945 -23.369  -2.228  1.00 48.69           C  
-ATOM   3029  C   VAL B 179     -15.799 -22.949  -3.134  1.00 48.97           C  
-ATOM   3030  O   VAL B 179     -14.734 -22.576  -2.651  1.00 51.85           O  
-ATOM   3031  CB  VAL B 179     -16.887 -24.886  -2.072  1.00 48.13           C  
-ATOM   3032  CG1 VAL B 179     -15.463 -25.329  -1.823  1.00 46.76           C  
-ATOM   3033  CG2 VAL B 179     -17.769 -25.316  -0.948  1.00 50.79           C  
-ATOM   3034  N   LYS B 180     -16.016 -23.054  -4.443  1.00 53.06           N  
-ATOM   3035  CA  LYS B 180     -15.087 -22.540  -5.441  1.00 56.37           C  
-ATOM   3036  C   LYS B 180     -14.953 -21.049  -5.207  1.00 44.73           C  
-ATOM   3037  O   LYS B 180     -13.846 -20.537  -5.034  1.00 44.31           O  
-ATOM   3038  CB  LYS B 180     -15.623 -22.782  -6.858  1.00 60.69           C  
-ATOM   3039  CG  LYS B 180     -14.570 -23.041  -7.932  1.00 39.02           C  
-ATOM   3040  CD  LYS B 180     -15.231 -23.004  -9.290  1.00 55.47           C  
-ATOM   3041  CE  LYS B 180     -14.820 -24.177 -10.168  1.00 66.56           C  
-ATOM   3042  NZ  LYS B 180     -15.748 -24.358 -11.327  1.00 66.48           N  
-ATOM   3043  N   LYS B 181     -16.093 -20.362  -5.195  1.00 30.03           N  
-ATOM   3044  CA  LYS B 181     -16.131 -18.940  -4.890  1.00 39.23           C  
-ATOM   3045  C   LYS B 181     -15.291 -18.568  -3.650  1.00 42.59           C  
-ATOM   3046  O   LYS B 181     -14.472 -17.643  -3.696  1.00 31.63           O  
-ATOM   3047  CB  LYS B 181     -17.582 -18.483  -4.756  1.00 49.53           C  
-ATOM   3048  CG  LYS B 181     -17.890 -17.630  -3.521  1.00 77.24           C  
-ATOM   3049  CD  LYS B 181     -17.703 -16.127  -3.745  1.00 82.25           C  
-ATOM   3050  CE  LYS B 181     -17.908 -15.362  -2.427  1.00 87.16           C  
-ATOM   3051  NZ  LYS B 181     -17.870 -13.883  -2.607  1.00 85.51           N  
-ATOM   3052  N   GLU B 182     -15.490 -19.295  -2.551  1.00 44.48           N  
-ATOM   3053  CA  GLU B 182     -14.727 -19.069  -1.326  1.00 39.07           C  
-ATOM   3054  C   GLU B 182     -13.236 -19.305  -1.492  1.00 40.45           C  
-ATOM   3055  O   GLU B 182     -12.427 -18.480  -1.063  1.00 45.10           O  
-ATOM   3056  CB  GLU B 182     -15.253 -19.933  -0.178  1.00 44.27           C  
-ATOM   3057  CG  GLU B 182     -16.034 -19.134   0.864  1.00 59.76           C  
-ATOM   3058  CD  GLU B 182     -15.159 -18.165   1.672  1.00 65.22           C  
-ATOM   3059  OE1 GLU B 182     -14.297 -18.634   2.455  1.00 50.49           O  
-ATOM   3060  OE2 GLU B 182     -15.351 -16.933   1.543  1.00 68.64           O  
-ATOM   3061  N   LEU B 183     -12.884 -20.431  -2.113  1.00 32.49           N  
-ATOM   3062  CA  LEU B 183     -11.497 -20.823  -2.287  1.00 27.03           C  
-ATOM   3063  C   LEU B 183     -10.723 -19.781  -3.069  1.00 34.50           C  
-ATOM   3064  O   LEU B 183      -9.663 -19.333  -2.643  1.00 31.65           O  
-ATOM   3065  CB  LEU B 183     -11.420 -22.148  -3.015  1.00 34.78           C  
-ATOM   3066  CG  LEU B 183     -10.203 -23.008  -2.668  1.00 39.78           C  
-ATOM   3067  CD1 LEU B 183      -9.924 -24.000  -3.782  1.00 45.10           C  
-ATOM   3068  CD2 LEU B 183      -8.969 -22.172  -2.372  1.00 32.32           C  
-ATOM   3069  N   ILE B 184     -11.255 -19.404  -4.229  1.00 37.48           N  
-ATOM   3070  CA  ILE B 184     -10.622 -18.405  -5.078  1.00 29.27           C  
-ATOM   3071  C   ILE B 184     -10.475 -17.086  -4.334  1.00 32.00           C  
-ATOM   3072  O   ILE B 184      -9.394 -16.491  -4.326  1.00 28.76           O  
-ATOM   3073  CB  ILE B 184     -11.407 -18.210  -6.391  1.00 33.96           C  
-ATOM   3074  CG1 ILE B 184     -11.512 -19.538  -7.131  1.00 32.11           C  
-ATOM   3075  CG2 ILE B 184     -10.743 -17.158  -7.294  1.00 33.47           C  
-ATOM   3076  CD1 ILE B 184     -12.279 -19.464  -8.434  1.00 33.56           C  
-ATOM   3077  N   LYS B 185     -11.571 -16.649  -3.713  1.00 29.00           N  
-ATOM   3078  CA  LYS B 185     -11.602 -15.438  -2.912  1.00 32.35           C  
-ATOM   3079  C   LYS B 185     -10.451 -15.420  -1.943  1.00 31.40           C  
-ATOM   3080  O   LYS B 185      -9.849 -14.376  -1.691  1.00 24.00           O  
-ATOM   3081  CB  LYS B 185     -12.911 -15.347  -2.142  1.00 44.13           C  
-ATOM   3082  CG  LYS B 185     -13.160 -13.999  -1.478  1.00 38.46           C  
-ATOM   3083  CD  LYS B 185     -12.909 -14.073   0.004  1.00 41.44           C  
-ATOM   3084  CE  LYS B 185     -13.779 -13.091   0.789  1.00 56.13           C  
-ATOM   3085  NZ  LYS B 185     -15.209 -13.513   0.915  1.00 52.12           N  
-ATOM   3086  N   ASN B 186     -10.127 -16.591  -1.414  1.00 35.28           N  
-ATOM   3087  CA  ASN B 186      -9.033 -16.696  -0.452  1.00 36.92           C  
-ATOM   3088  C   ASN B 186      -7.640 -16.591  -1.025  1.00 38.47           C  
-ATOM   3089  O   ASN B 186      -6.782 -15.953  -0.413  1.00 49.32           O  
-ATOM   3090  CB  ASN B 186      -9.160 -17.954   0.392  1.00 37.91           C  
-ATOM   3091  CG  ASN B 186     -10.195 -17.806   1.470  1.00 42.95           C  
-ATOM   3092  OD1 ASN B 186     -10.446 -16.697   1.946  1.00 40.96           O  
-ATOM   3093  ND2 ASN B 186     -10.819 -18.912   1.852  1.00 45.06           N  
-ATOM   3094  N   ILE B 187      -7.395 -17.221  -2.175  1.00 31.31           N  
-ATOM   3095  CA  ILE B 187      -6.074 -17.116  -2.781  1.00 34.55           C  
-ATOM   3096  C   ILE B 187      -5.872 -15.712  -3.313  1.00 37.71           C  
-ATOM   3097  O   ILE B 187      -4.768 -15.170  -3.261  1.00 32.20           O  
-ATOM   3098  CB  ILE B 187      -5.791 -18.193  -3.862  1.00 40.72           C  
-ATOM   3099  CG1 ILE B 187      -7.072 -18.723  -4.459  1.00 35.73           C  
-ATOM   3100  CG2 ILE B 187      -5.075 -19.390  -3.254  1.00 58.56           C  
-ATOM   3101  CD1 ILE B 187      -6.949 -20.159  -4.867  1.00 28.87           C  
-ATOM   3102  N   VAL B 188      -6.953 -15.108  -3.790  1.00 38.08           N  
-ATOM   3103  CA  VAL B 188      -6.839 -13.778  -4.351  1.00 32.64           C  
-ATOM   3104  C   VAL B 188      -6.382 -12.785  -3.295  1.00 38.97           C  
-ATOM   3105  O   VAL B 188      -5.356 -12.129  -3.470  1.00 41.65           O  
-ATOM   3106  CB  VAL B 188      -8.123 -13.309  -4.996  1.00 30.93           C  
-ATOM   3107  CG1 VAL B 188      -7.950 -11.884  -5.492  1.00 28.09           C  
-ATOM   3108  CG2 VAL B 188      -8.510 -14.245  -6.130  1.00 26.63           C  
-ATOM   3109  N   ILE B 189      -7.123 -12.672  -2.193  1.00 43.88           N  
-ATOM   3110  CA  ILE B 189      -6.736 -11.704  -1.168  1.00 44.69           C  
-ATOM   3111  C   ILE B 189      -5.326 -11.985  -0.683  1.00 41.92           C  
-ATOM   3112  O   ILE B 189      -4.629 -11.067  -0.277  1.00 46.30           O  
-ATOM   3113  CB  ILE B 189      -7.721 -11.626   0.040  1.00 35.81           C  
-ATOM   3114  CG1 ILE B 189      -7.635 -12.885   0.912  1.00 48.57           C  
-ATOM   3115  CG2 ILE B 189      -9.139 -11.344  -0.443  1.00 34.95           C  
-ATOM   3116  CD1 ILE B 189      -8.961 -13.269   1.600  1.00 58.38           C  
-ATOM   3117  N   GLU B 190      -4.896 -13.244  -0.730  1.00 35.84           N  
-ATOM   3118  CA  GLU B 190      -3.537 -13.547  -0.294  1.00 40.56           C  
-ATOM   3119  C   GLU B 190      -2.511 -13.052  -1.304  1.00 46.22           C  
-ATOM   3120  O   GLU B 190      -1.528 -12.412  -0.948  1.00 49.72           O  
-ATOM   3121  CB  GLU B 190      -3.308 -15.025  -0.045  1.00 34.29           C  
-ATOM   3122  CG  GLU B 190      -1.904 -15.225   0.451  1.00 41.19           C  
-ATOM   3123  CD  GLU B 190      -1.534 -16.660   0.614  1.00 73.74           C  
-ATOM   3124  OE1 GLU B 190      -2.450 -17.519   0.581  1.00 74.18           O  
-ATOM   3125  OE2 GLU B 190      -0.319 -16.921   0.775  1.00 85.77           O  
-ATOM   3126  N   ALA B 191      -2.735 -13.358  -2.568  1.00 44.19           N  
-ATOM   3127  CA  ALA B 191      -1.909 -12.780  -3.609  1.00 41.97           C  
-ATOM   3128  C   ALA B 191      -1.725 -11.290  -3.365  1.00 38.23           C  
-ATOM   3129  O   ALA B 191      -0.653 -10.749  -3.602  1.00 38.95           O  
-ATOM   3130  CB  ALA B 191      -2.532 -13.014  -4.983  1.00 27.53           C  
-ATOM   3131  N   ILE B 192      -2.772 -10.631  -2.890  1.00 31.14           N  
-ATOM   3132  CA  ILE B 192      -2.740  -9.185  -2.748  1.00 39.80           C  
-ATOM   3133  C   ILE B 192      -1.944  -8.652  -1.545  1.00 41.39           C  
-ATOM   3134  O   ILE B 192      -1.326  -7.593  -1.638  1.00 41.82           O  
-ATOM   3135  CB  ILE B 192      -4.154  -8.612  -2.715  1.00 33.64           C  
-ATOM   3136  CG1 ILE B 192      -4.853  -8.900  -4.014  1.00 31.98           C  
-ATOM   3137  CG2 ILE B 192      -4.136  -7.104  -2.507  1.00 26.43           C  
-ATOM   3138  CD1 ILE B 192      -6.213  -8.273  -4.054  1.00 47.32           C  
-ATOM   3139  N   HIS B 193      -1.966  -9.357  -0.420  1.00 38.99           N  
-ATOM   3140  CA  HIS B 193      -1.212  -8.892   0.739  1.00 52.44           C  
-ATOM   3141  C   HIS B 193       0.256  -9.313   0.630  1.00 53.01           C  
-ATOM   3142  O   HIS B 193       1.162  -8.610   1.099  1.00 58.27           O  
-ATOM   3143  CB  HIS B 193      -1.842  -9.352   2.066  1.00 54.64           C  
-ATOM   3144  CG  HIS B 193      -3.210  -8.794   2.315  1.00 68.22           C  
-ATOM   3145  ND1 HIS B 193      -4.121  -9.395   3.159  1.00 77.17           N  
-ATOM   3146  CD2 HIS B 193      -3.831  -7.697   1.814  1.00 67.50           C  
-ATOM   3147  CE1 HIS B 193      -5.240  -8.689   3.173  1.00 83.14           C  
-ATOM   3148  NE2 HIS B 193      -5.093  -7.656   2.362  1.00 73.42           N  
-ATOM   3149  N   THR B 194       0.486 -10.442  -0.027  1.00 46.83           N  
-ATOM   3150  CA  THR B 194       1.831 -10.999  -0.144  1.00 51.95           C  
-ATOM   3151  C   THR B 194       2.652 -10.541  -1.375  1.00 44.89           C  
-ATOM   3152  O   THR B 194       3.669 -11.151  -1.697  1.00 52.41           O  
-ATOM   3153  CB  THR B 194       1.783 -12.548  -0.081  1.00 55.18           C  
-ATOM   3154  OG1 THR B 194       1.435 -13.079  -1.366  1.00 61.00           O  
-ATOM   3155  CG2 THR B 194       0.760 -13.011   0.951  1.00 42.97           C  
-ATOM   3156  N   VAL B 195       2.234  -9.465  -2.038  1.00 45.68           N  
-ATOM   3157  CA  VAL B 195       2.938  -8.971  -3.232  1.00 57.10           C  
-ATOM   3158  C   VAL B 195       4.081  -8.012  -2.892  1.00 64.17           C  
-ATOM   3159  O   VAL B 195       3.940  -7.154  -2.009  1.00 63.11           O  
-ATOM   3160  CB  VAL B 195       1.966  -8.280  -4.231  1.00 40.63           C  
-ATOM   3161  CG1 VAL B 195       2.649  -7.200  -4.994  1.00 38.74           C  
-ATOM   3162  CG2 VAL B 195       1.425  -9.280  -5.208  1.00 45.95           C  
-ATOM   3163  N   THR B 196       5.209  -8.167  -3.591  1.00 64.72           N  
-ATOM   3164  CA  THR B 196       6.346  -7.235  -3.467  1.00 80.88           C  
-ATOM   3165  C   THR B 196       7.190  -7.033  -4.728  1.00 72.33           C  
-ATOM   3166  O   THR B 196       7.288  -7.907  -5.592  1.00 53.76           O  
-ATOM   3167  CB  THR B 196       7.346  -7.659  -2.370  1.00 69.86           C  
-ATOM   3168  OG1 THR B 196       7.613  -9.063  -2.483  1.00 61.18           O  
-ATOM   3169  CG2 THR B 196       6.809  -7.328  -0.992  1.00 72.63           C  
-ATOM   3170  N   GLY B 197       7.826  -5.869  -4.793  1.00 71.34           N  
-ATOM   3171  CA  GLY B 197       8.836  -5.607  -5.793  1.00 63.18           C  
-ATOM   3172  C   GLY B 197       8.301  -4.899  -7.013  1.00 65.89           C  
-ATOM   3173  O   GLY B 197       7.236  -4.278  -6.967  1.00 61.78           O  
-ATOM   3174  N   PRO B 198       9.047  -4.993  -8.119  1.00 65.45           N  
-ATOM   3175  CA  PRO B 198       8.671  -4.369  -9.382  1.00 57.36           C  
-ATOM   3176  C   PRO B 198       7.711  -5.274 -10.132  1.00 57.18           C  
-ATOM   3177  O   PRO B 198       7.739  -6.503  -9.962  1.00 51.64           O  
-ATOM   3178  CB  PRO B 198      10.001  -4.326 -10.119  1.00 57.71           C  
-ATOM   3179  CG  PRO B 198      10.625  -5.634  -9.753  1.00 56.68           C  
-ATOM   3180  CD  PRO B 198      10.221  -5.870  -8.290  1.00 63.87           C  
-ATOM   3181  N   VAL B 199       6.861  -4.676 -10.953  1.00 50.40           N  
-ATOM   3182  CA  VAL B 199       6.106  -5.468 -11.907  1.00 56.55           C  
-ATOM   3183  C   VAL B 199       7.052  -6.248 -12.843  1.00 55.67           C  
-ATOM   3184  O   VAL B 199       7.961  -5.685 -13.459  1.00 40.03           O  
-ATOM   3185  CB  VAL B 199       5.178  -4.590 -12.735  1.00 43.33           C  
-ATOM   3186  CG1 VAL B 199       4.142  -5.464 -13.448  1.00 29.62           C  
-ATOM   3187  CG2 VAL B 199       4.529  -3.549 -11.832  1.00 39.70           C  
-ATOM   3188  N   GLY B 200       6.841  -7.554 -12.941  1.00 57.80           N  
-ATOM   3189  CA  GLY B 200       7.648  -8.362 -13.832  1.00 49.18           C  
-ATOM   3190  C   GLY B 200       7.310  -8.135 -15.293  1.00 48.14           C  
-ATOM   3191  O   GLY B 200       6.249  -7.618 -15.625  1.00 48.08           O  
-ATOM   3192  N   GLN B 201       8.217  -8.520 -16.182  1.00 50.89           N  
-ATOM   3193  CA  GLN B 201       7.926  -8.459 -17.607  1.00 41.28           C  
-ATOM   3194  C   GLN B 201       7.771  -9.883 -18.121  1.00 39.05           C  
-ATOM   3195  O   GLN B 201       8.580 -10.757 -17.799  1.00 49.18           O  
-ATOM   3196  CB  GLN B 201       9.028  -7.708 -18.344  1.00 45.44           C  
-ATOM   3197  CG  GLN B 201       9.502  -6.488 -17.587  1.00 56.32           C  
-ATOM   3198  CD  GLN B 201      10.833  -5.969 -18.088  1.00 65.62           C  
-ATOM   3199  OE1 GLN B 201      11.852  -6.048 -17.391  1.00 62.08           O  
-ATOM   3200  NE2 GLN B 201      10.836  -5.437 -19.306  1.00 58.63           N  
-ATOM   3201  N   LEU B 202       6.719 -10.119 -18.899  1.00 32.52           N  
-ATOM   3202  CA  LEU B 202       6.368 -11.473 -19.282  1.00 37.64           C  
-ATOM   3203  C   LEU B 202       7.347 -12.060 -20.295  1.00 42.33           C  
-ATOM   3204  O   LEU B 202       7.758 -11.390 -21.247  1.00 39.80           O  
-ATOM   3205  CB  LEU B 202       4.924 -11.545 -19.790  1.00 35.63           C  
-ATOM   3206  CG  LEU B 202       4.388 -12.935 -20.165  1.00 35.32           C  
-ATOM   3207  CD1 LEU B 202       4.530 -13.948 -19.038  1.00 31.84           C  
-ATOM   3208  CD2 LEU B 202       2.940 -12.811 -20.564  1.00 39.60           C  
-ATOM   3209  N   TRP B 203       7.727 -13.314 -20.050  1.00 44.83           N  
-ATOM   3210  CA  TRP B 203       8.567 -14.090 -20.956  1.00 45.45           C  
-ATOM   3211  C   TRP B 203       9.753 -13.318 -21.492  1.00 56.10           C  
-ATOM   3212  O   TRP B 203      10.009 -13.300 -22.694  1.00 44.77           O  
-ATOM   3213  CB  TRP B 203       7.765 -14.598 -22.137  1.00 38.28           C  
-ATOM   3214  CG  TRP B 203       6.792 -15.627 -21.791  1.00 36.32           C  
-ATOM   3215  CD1 TRP B 203       6.991 -16.693 -20.984  1.00 40.57           C  
-ATOM   3216  CD2 TRP B 203       5.445 -15.715 -22.264  1.00 45.15           C  
-ATOM   3217  NE1 TRP B 203       5.845 -17.449 -20.913  1.00 41.40           N  
-ATOM   3218  CE2 TRP B 203       4.882 -16.869 -21.695  1.00 37.83           C  
-ATOM   3219  CE3 TRP B 203       4.661 -14.925 -23.116  1.00 41.32           C  
-ATOM   3220  CZ2 TRP B 203       3.572 -17.256 -21.942  1.00 40.22           C  
-ATOM   3221  CZ3 TRP B 203       3.367 -15.308 -23.362  1.00 37.74           C  
-ATOM   3222  CH2 TRP B 203       2.830 -16.466 -22.774  1.00 44.95           C  
-ATOM   3223  N   MET B 204      10.482 -12.677 -20.599  1.00 62.09           N  
-ATOM   3224  CA  MET B 204      11.718 -12.060 -21.000  1.00 59.17           C  
-ATOM   3225  C   MET B 204      12.866 -12.589 -20.155  1.00 92.50           C  
-ATOM   3226  O   MET B 204      12.727 -12.792 -18.942  1.00 91.55           O  
-ATOM   3227  CB  MET B 204      11.587 -10.556 -20.916  1.00 49.60           C  
-ATOM   3228  CG  MET B 204      10.923  -9.997 -22.140  1.00 51.05           C  
-ATOM   3229  SD  MET B 204      11.008  -8.215 -22.108  1.00 68.80           S  
-ATOM   3230  CE  MET B 204      12.202  -7.985 -20.788  1.00 60.17           C  
-ATOM   3231  OXT MET B 204      13.947 -12.850 -20.690  1.00 94.57           O  
-TER    3232      MET B 204                                                      
-HETATM 3233 MG    MG A1205     -26.421  -5.811  -8.246  1.00 41.80          MG  
-HETATM 3234 MG    MG A1206     -30.944  -8.965  -5.101  1.00 27.56          MG  
-HETATM 3235  O3' BVP A1207     -33.449  -4.828  -2.108  1.00 51.90           O  
-HETATM 3236  C3' BVP A1207     -32.223  -4.370  -2.663  1.00 32.80           C  
-HETATM 3237  C2' BVP A1207     -32.038  -2.856  -2.546  1.00 31.83           C  
-HETATM 3238  C1' BVP A1207     -31.508  -2.771  -1.136  1.00 29.29           C  
-HETATM 3239  O4' BVP A1207     -30.437  -3.699  -1.192  1.00 27.08           O  
-HETATM 3240  C4' BVP A1207     -31.072  -4.873  -1.769  1.00 36.32           C  
-HETATM 3241  C5' BVP A1207     -30.070  -5.780  -2.464  1.00 37.05           C  
-HETATM 3242  O5' BVP A1207     -29.585  -5.101  -3.615  1.00 40.84           O  
-HETATM 3243  P   BVP A1207     -28.857  -5.895  -4.805  1.00 42.04           P  
-HETATM 3244  O1P BVP A1207     -30.006  -6.243  -5.936  1.00 48.31           O  
-HETATM 3245  O2P BVP A1207     -27.931  -4.736  -5.507  1.00 42.01           O  
-HETATM 3246  O3P BVP A1207     -28.143  -7.115  -4.361  1.00 23.49           O  
-HETATM 3247  N1  BVP A1207     -31.153  -1.405  -0.615  1.00 31.79           N  
-HETATM 3248  C6  BVP A1207     -31.736  -0.812   0.499  1.00 28.28           C  
-HETATM 3249  C5  BVP A1207     -31.331   0.479   0.852  1.00 35.33           C  
-HETATM 3250  C5A BVP A1207     -31.837   1.098   1.996  1.00 41.08           C  
-HETATM 3251  C5B BVP A1207     -32.765   0.237   2.881  1.00 42.22           C  
-HETATM 3252 BR   BVP A1207     -33.399   1.103   4.386  0.63 43.02          BR  
-HETATM 3253  C4  BVP A1207     -30.311   1.131   0.156  1.00 36.04           C  
-HETATM 3254  O4  BVP A1207     -29.917   2.249   0.473  1.00 46.13           O  
-HETATM 3255  N3  BVP A1207     -29.726   0.535  -0.930  1.00 29.77           N  
-HETATM 3256  C2  BVP A1207     -30.186  -0.735  -1.288  1.00 43.61           C  
-HETATM 3257  O2  BVP A1207     -29.664  -1.262  -2.269  1.00 42.64           O  
-HETATM 3258  S   SO4 A1208     -30.673  -7.087 -10.885  1.00 72.55           S  
-HETATM 3259  O1  SO4 A1208     -30.947  -8.098 -11.921  1.00 49.67           O  
-HETATM 3260  O2  SO4 A1208     -31.181  -7.515  -9.571  1.00 53.87           O  
-HETATM 3261  O3  SO4 A1208     -31.269  -5.806 -11.284  1.00 34.19           O  
-HETATM 3262  O4  SO4 A1208     -29.238  -6.917 -10.721  1.00 52.97           O  
-HETATM 3263 MG    MG B1205     -14.736 -12.888 -20.755  1.00 38.83          MG  
-HETATM 3264 MG    MG B1206     -17.009 -16.623 -25.507  1.00 21.10          MG  
-HETATM 3265  O3' BVP B1207     -12.366 -18.355 -27.598  1.00 44.51           O  
-HETATM 3266  C3' BVP B1207     -12.215 -17.222 -26.797  1.00 30.57           C  
-HETATM 3267  C2' BVP B1207     -10.712 -16.964 -26.536  1.00 43.02           C  
-HETATM 3268  C1' BVP B1207     -10.372 -16.012 -27.688  1.00 42.35           C  
-HETATM 3269  O4' BVP B1207     -11.513 -15.067 -27.703  1.00 36.26           O  
-HETATM 3270  C4' BVP B1207     -12.672 -15.977 -27.626  1.00 32.15           C  
-HETATM 3271  C5' BVP B1207     -13.977 -15.284 -27.153  1.00 31.66           C  
-HETATM 3272  O5' BVP B1207     -13.704 -14.352 -26.087  1.00 49.00           O  
-HETATM 3273  P   BVP B1207     -14.462 -14.296 -24.612  1.00 40.10           P  
-HETATM 3274  O1P BVP B1207     -13.305 -13.817 -23.527  1.00 25.58           O  
-HETATM 3275  O2P BVP B1207     -15.568 -13.101 -24.668  1.00 18.93           O  
-HETATM 3276  O3P BVP B1207     -15.069 -15.586 -24.212  1.00 51.55           O  
-HETATM 3277  N1  BVP B1207      -8.943 -15.454 -27.808  1.00 37.86           N  
-HETATM 3278  C6  BVP B1207      -8.112 -15.841 -28.872  1.00 29.62           C  
-HETATM 3279  C5  BVP B1207      -6.816 -15.323 -28.945  1.00 32.98           C  
-HETATM 3280  C5A BVP B1207      -5.960 -15.641 -29.998  1.00 34.04           C  
-HETATM 3281  C5B BVP B1207      -6.558 -16.554 -31.061  1.00 37.50           C  
-HETATM 3282 BR   BVP B1207      -5.398 -16.961 -32.443  0.43 32.49          BR  
-HETATM 3283  C4  BVP B1207      -6.358 -14.417 -28.001  1.00 36.58           C  
-HETATM 3284  O4  BVP B1207      -5.227 -13.937 -28.073  1.00 43.19           O  
-HETATM 3285  N3  BVP B1207      -7.173 -14.042 -26.963  1.00 28.04           N  
-HETATM 3286  C2  BVP B1207      -8.449 -14.567 -26.887  1.00 36.33           C  
-HETATM 3287  O2  BVP B1207      -9.100 -14.161 -25.924  1.00 40.04           O  
-HETATM 3288  S   SO4 B1208     -16.625 -17.690 -19.521  1.00 52.58           S  
-HETATM 3289  O1  SO4 B1208     -15.564 -18.493 -18.898  1.00 36.52           O  
-HETATM 3290  O2  SO4 B1208     -17.862 -17.805 -18.752  1.00 38.17           O  
-HETATM 3291  O3  SO4 B1208     -16.889 -18.170 -20.883  1.00 50.99           O  
-HETATM 3292  O4  SO4 B1208     -16.181 -16.295 -19.618  1.00 53.30           O  
-HETATM 3293  O3' BVP B1209       8.376  -5.052 -26.128  1.00 59.19           O  
-HETATM 3294  C3' BVP B1209       7.927  -5.500 -27.423  1.00 78.72           C  
-HETATM 3295  C2' BVP B1209       6.436  -5.269 -27.669  1.00 63.92           C  
-HETATM 3296  C1' BVP B1209       6.482  -3.934 -28.413  1.00 66.52           C  
-HETATM 3297  O4' BVP B1209       7.288  -4.398 -29.423  1.00 81.20           O  
-HETATM 3298  C4' BVP B1209       8.466  -4.623 -28.615  1.00100.68           C  
-HETATM 3299  C5' BVP B1209       9.589  -5.167 -29.462  1.00104.72           C  
-HETATM 3300  O5' BVP B1209       9.513  -4.589 -30.764  1.00 78.23           O  
-HETATM 3301  P   BVP B1209      10.576  -5.158 -31.786  1.00113.16           P  
-HETATM 3302  O1P BVP B1209       9.747  -5.979 -32.906  1.00107.54           O  
-HETATM 3303  O2P BVP B1209      11.232  -3.899 -32.557  1.00108.72           O  
-HETATM 3304  O3P BVP B1209      11.605  -6.004 -31.123  1.00122.54           O  
-HETATM 3305  N1  BVP B1209       5.124  -3.528 -28.784  1.00 59.60           N  
-HETATM 3306  C6  BVP B1209       4.498  -4.467 -29.590  1.00 53.91           C  
-HETATM 3307  C5  BVP B1209       3.196  -4.344 -30.016  1.00 41.39           C  
-HETATM 3308  C5A BVP B1209       2.770  -5.331 -30.906  1.00 52.45           C  
-HETATM 3309  C5B BVP B1209       1.348  -5.304 -31.464  1.00 56.42           C  
-HETATM 3310 BR   BVP B1209       0.984  -6.698 -32.625  1.00 91.24          BR  
-HETATM 3311  C4  BVP B1209       2.473  -3.230 -29.594  1.00 45.05           C  
-HETATM 3312  O4  BVP B1209       1.308  -3.033 -29.937  1.00 61.29           O  
-HETATM 3313  N3  BVP B1209       3.092  -2.310 -28.723  1.00 53.24           N  
-HETATM 3314  C2  BVP B1209       4.417  -2.521 -28.269  1.00 60.70           C  
-HETATM 3315  O2  BVP B1209       4.976  -1.709 -27.533  1.00 66.02           O  
-HETATM 3316  O   HOH A2001     -13.551  -2.040 -11.630  1.00 33.56           O  
-HETATM 3317  O   HOH A2002     -37.351 -10.870   7.249  1.00 23.63           O  
-HETATM 3318  O   HOH A2003     -35.737  13.875  -9.148  1.00 36.45           O  
-HETATM 3319  O   HOH A2004     -41.314  15.811 -13.542  1.00 37.60           O  
-HETATM 3320  O   HOH B2001       0.536   0.994 -24.051  1.00 18.74           O  
-HETATM 3321  O   HOH B2002      -6.084 -28.763  -8.689  1.00 26.62           O  
-CONECT   88 3234                                                                
-CONECT 1126 3234                                                                
-CONECT 1704 3264                                                                
-CONECT 2343 3263                                                                
-CONECT 2742 3264                                                                
-CONECT 3234   88 1126                                                           
-CONECT 3235 3236                                                                
-CONECT 3236 3235 3237 3240                                                      
-CONECT 3237 3236 3238                                                           
-CONECT 3238 3237 3239 3247                                                      
-CONECT 3239 3238 3240                                                           
-CONECT 3240 3236 3239 3241                                                      
-CONECT 3241 3240 3242                                                           
-CONECT 3242 3241 3243                                                           
-CONECT 3243 3242 3244 3245 3246                                                 
-CONECT 3244 3243                                                                
-CONECT 3245 3243                                                                
-CONECT 3246 3243                                                                
-CONECT 3247 3238 3248 3256                                                      
-CONECT 3248 3247 3249                                                           
-CONECT 3249 3248 3250 3253                                                      
-CONECT 3250 3249 3251                                                           
-CONECT 3251 3250 3252                                                           
-CONECT 3252 3251                                                                
-CONECT 3253 3249 3254 3255                                                      
-CONECT 3254 3253                                                                
-CONECT 3255 3253 3256                                                           
-CONECT 3256 3247 3255 3257                                                      
-CONECT 3257 3256                                                                
-CONECT 3258 3259 3260 3261 3262                                                 
-CONECT 3259 3258                                                                
-CONECT 3260 3258                                                                
-CONECT 3261 3258                                                                
-CONECT 3262 3258                                                                
-CONECT 3263 2343                                                                
-CONECT 3264 1704 2742 3276                                                      
-CONECT 3265 3266                                                                
-CONECT 3266 3265 3267 3270                                                      
-CONECT 3267 3266 3268                                                           
-CONECT 3268 3267 3269 3277                                                      
-CONECT 3269 3268 3270                                                           
-CONECT 3270 3266 3269 3271                                                      
-CONECT 3271 3270 3272                                                           
-CONECT 3272 3271 3273                                                           
-CONECT 3273 3272 3274 3275 3276                                                 
-CONECT 3274 3273                                                                
-CONECT 3275 3273                                                                
-CONECT 3276 3264 3273                                                           
-CONECT 3277 3268 3278 3286                                                      
-CONECT 3278 3277 3279                                                           
-CONECT 3279 3278 3280 3283                                                      
-CONECT 3280 3279 3281                                                           
-CONECT 3281 3280 3282                                                           
-CONECT 3282 3281                                                                
-CONECT 3283 3279 3284 3285                                                      
-CONECT 3284 3283                                                                
-CONECT 3285 3283 3286                                                           
-CONECT 3286 3277 3285 3287                                                      
-CONECT 3287 3286                                                                
-CONECT 3288 3289 3290 3291 3292                                                 
-CONECT 3289 3288                                                                
-CONECT 3290 3288                                                                
-CONECT 3291 3288                                                                
-CONECT 3292 3288                                                                
-CONECT 3293 3294                                                                
-CONECT 3294 3293 3295 3298                                                      
-CONECT 3295 3294 3296                                                           
-CONECT 3296 3295 3297 3305                                                      
-CONECT 3297 3296 3298                                                           
-CONECT 3298 3294 3297 3299                                                      
-CONECT 3299 3298 3300                                                           
-CONECT 3300 3299 3301                                                           
-CONECT 3301 3300 3302 3303 3304                                                 
-CONECT 3302 3301                                                                
-CONECT 3303 3301                                                                
-CONECT 3304 3301                                                                
-CONECT 3305 3296 3306 3314                                                      
-CONECT 3306 3305 3307                                                           
-CONECT 3307 3306 3308 3311                                                      
-CONECT 3308 3307 3309                                                           
-CONECT 3309 3308 3310                                                           
-CONECT 3310 3309                                                                
-CONECT 3311 3307 3312 3313                                                      
-CONECT 3312 3311                                                                
-CONECT 3313 3311 3314                                                           
-CONECT 3314 3305 3313 3315                                                      
-CONECT 3315 3314                                                                
-MASTER      368    0    9   18   14    0   17    6 3319    2   87   32          
-END                                                                             
diff --git a/plip/test/pdb/2zoz.pdb b/plip/test/pdb/2zoz.pdb
deleted file mode 100644
index aeee190..0000000
--- a/plip/test/pdb/2zoz.pdb
+++ /dev/null
@@ -1,3856 +0,0 @@
-HEADER    TRANSCRIPTION                           20-JUN-08   2ZOZ              
-TITLE     CRYSTAL STRUCTURE OF THE ETHIDIUM-BOUND FORM OF THE MULTI-DRUG BINDING
-TITLE    2 TRANSCRIPTIONAL REPRESSOR CGMR                                       
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: TRANSCRIPTIONAL REGULATOR;                                 
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 FRAGMENT: UNP RESIDUES 1-175;                                        
-COMPND   5 SYNONYM: BACTERIAL REGULATORY PROTEIN, TETR FAMILY, CGMR;            
-COMPND   6 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM;                     
-SOURCE   3 ORGANISM_COMMON: CORYNEBACTERIUM GLUTAMICUM;                         
-SOURCE   4 ORGANISM_TAXID: 196627;                                              
-SOURCE   5 STRAIN: ATCC13032;                                                   
-SOURCE   6 GENE: CGL2612;                                                       
-SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21STAR(DE3);                             
-SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET26B                                    
-KEYWDS    HELIX TURN HELIX, DNA-BINDING, TRANSCRIPTION, TRANSCRIPTION           
-KEYWDS   2 REGULATION                                                           
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    H.ITOU,Y.SHIRAKIHARA,I.TANAKA                                         
-REVDAT   5   13-JUL-11 2ZOZ    1       VERSN                                    
-REVDAT   4   13-OCT-10 2ZOZ    1       JRNL                                     
-REVDAT   3   18-AUG-10 2ZOZ    1       JRNL                                     
-REVDAT   2   24-FEB-09 2ZOZ    1       VERSN                                    
-REVDAT   1   08-JUL-08 2ZOZ    0                                                
-SPRSDE     08-JUL-08 2ZOZ      2DH0                                             
-JRNL        AUTH   H.ITOU,N.WATANABE,M.YAO,Y.SHIRAKIHARA,I.TANAKA               
-JRNL        TITL   CRYSTAL STRUCTURES OF THE MULTIDRUG BINDING REPRESSOR        
-JRNL        TITL 2 CORYNEBACTERIUMGLUTAMICUM CGMR IN COMPLEX WITH INDUCERS AND  
-JRNL        TITL 3 WITH AN OPERATOR                                             
-JRNL        REF    J.MOL.BIOL.                   V. 403   174 2010              
-JRNL        REFN                   ISSN 0022-2836                               
-JRNL        PMID   20691702                                                     
-JRNL        DOI    10.1016/J.JMB.2010.07.042                                    
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS 1.1                                              
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.74                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1550448.480                    
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.3                           
-REMARK   3   NUMBER OF REFLECTIONS             : 44692                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.207                           
-REMARK   3   FREE R VALUE                     : 0.235                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 4408                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.40                        
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6543                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
-REMARK   3   BIN FREE R VALUE                    : 0.2860                       
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 715                          
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 2854                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 75                                      
-REMARK   3   SOLVENT ATOMS            : 357                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 18.10                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.00                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -4.10000                                             
-REMARK   3    B22 (A**2) : 14.10000                                             
-REMARK   3    B33 (A**2) : -9.99000                                             
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.26                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.006                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.10                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.72                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.330 ; 1.500                
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.010 ; 2.000                
-REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.160 ; 2.000                
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.190 ; 2.500                
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : FLAT MODEL                                           
-REMARK   3   KSOL        : 0.38                                                 
-REMARK   3   BSOL        : 59.72                                                
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
-REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
-REMARK   3  PARAMETER FILE  3  : ET_GOL_SO4.PARAM                               
-REMARK   3  PARAMETER FILE  4  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
-REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
-REMARK   3  TOPOLOGY FILE  3   : ET_GOL_SO4.TOP                                 
-REMARK   3  TOPOLOGY FILE  4   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 2ZOZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-08.                  
-REMARK 100 THE RCSB ID CODE IS RCSB028243.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-06                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 7.0                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
-REMARK 200  BEAMLINE                       : BL-6A                              
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
-REMARK 200  MONOCHROMATOR                  : SI (111)                           
-REMARK 200  OPTICS                         : MIRROR, MONOCHROMATOR              
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45773                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
-REMARK 200  DATA REDUNDANCY                : 7.300                              
-REMARK 200  R MERGE                    (I) : 0.07600                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.24500                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: AMORE                                                 
-REMARK 200 STARTING MODEL: PDB ENTRY 1V7B                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 66.01                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M LISO4, 10MM MGCL2, 0.1M HEPES,      
-REMARK 280  1MM ETHIDIUM BROMIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,        
-REMARK 280  TEMPERATURE 293K                                                    
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.37250            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.84200            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.11300            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.84200            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.37250            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.11300            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2                                                    
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 6700 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 17250 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 3080 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 20880 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -31.37250            
-REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       46.11300            
-REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      105.68400            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     ARG A     2                                                      
-REMARK 465     SER A   175                                                      
-REMARK 465     GLU A   176                                                      
-REMARK 465     LEU A   177                                                      
-REMARK 465     HIS A   178                                                      
-REMARK 465     HIS A   179                                                      
-REMARK 465     HIS A   180                                                      
-REMARK 465     HIS A   181                                                      
-REMARK 465     HIS A   182                                                      
-REMARK 465     HIS A   183                                                      
-REMARK 465     HIS B   182                                                      
-REMARK 465     HIS B   183                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    TYR A  20      -93.33   -116.72                                   
-REMARK 500    ARG A  72      -74.44    -56.86                                   
-REMARK 500    TYR B  20     -105.39   -127.36                                   
-REMARK 500    PRO B  74        8.11    -65.21                                   
-REMARK 500    TRP B 120      -40.37   -131.23                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH B 308        DISTANCE =  5.91 ANGSTROMS                       
-REMARK 525    HOH B 309        DISTANCE =  5.74 ANGSTROMS                       
-REMARK 525    HOH B 337        DISTANCE =  5.39 ANGSTROMS                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ET B 184                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 185                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 186                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 184                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 185                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 187                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 188                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 186                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 187                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 188                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 2ZOY   RELATED DB: PDB                                   
-REMARK 900 LIGAND FREE FORM OF CGMR                                             
-REMARK 900 RELATED ID: 2YVE   RELATED DB: PDB                                   
-REMARK 900 METHYLENE BLUE-COMPLEX OF CGMR                                       
-REMARK 900 RELATED ID: 2YVH   RELATED DB: PDB                                   
-REMARK 900 OPERATOR-COMPLEX OF CGMR                                             
-DBREF  2ZOZ A    1   175  UNP    Q8NMG3   Q8NMG3_CORGL     1    175             
-DBREF  2ZOZ B    1   175  UNP    Q8NMG3   Q8NMG3_CORGL     1    175             
-SEQADV 2ZOZ GLU A  176  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ LEU A  177  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS A  178  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS A  179  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS A  180  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS A  181  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS A  182  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS A  183  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ GLU B  176  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ LEU B  177  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS B  178  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS B  179  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS B  180  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS B  181  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS B  182  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQADV 2ZOZ HIS B  183  UNP  Q8NMG3              EXPRESSION TAG                 
-SEQRES   1 A  183  MET ARG THR SER LYS LYS GLU MET ILE LEU ARG THR ALA          
-SEQRES   2 A  183  ILE ASP TYR ILE GLY GLU TYR SER LEU GLU THR LEU SER          
-SEQRES   3 A  183  TYR ASP SER LEU ALA GLU ALA THR GLY LEU SER LYS SER          
-SEQRES   4 A  183  GLY LEU ILE TYR HIS PHE PRO SER ARG HIS ALA LEU LEU          
-SEQRES   5 A  183  LEU GLY MET HIS GLU LEU LEU ALA ASP ASP TRP ASP LYS          
-SEQRES   6 A  183  GLU LEU ARG ASP ILE THR ARG ASP PRO GLU ASP PRO LEU          
-SEQRES   7 A  183  GLU ARG LEU ARG ALA VAL VAL VAL THR LEU ALA GLU ASN          
-SEQRES   8 A  183  VAL SER ARG PRO GLU LEU LEU LEU LEU ILE ASP ALA PRO          
-SEQRES   9 A  183  SER HIS PRO ASP PHE LEU ASN ALA TRP ARG THR VAL ASN          
-SEQRES  10 A  183  HIS GLN TRP ILE PRO ASP THR ASP ASP LEU GLU ASN ASP          
-SEQRES  11 A  183  ALA HIS LYS ARG ALA VAL TYR LEU VAL GLN LEU ALA ALA          
-SEQRES  12 A  183  ASP GLY LEU PHE VAL HIS ASP TYR ILE HIS ASP ASP VAL          
-SEQRES  13 A  183  LEU SER LYS SER LYS ARG GLN ALA MET LEU GLU THR ILE          
-SEQRES  14 A  183  LEU GLU LEU ILE PRO SER GLU LEU HIS HIS HIS HIS HIS          
-SEQRES  15 A  183  HIS                                                          
-SEQRES   1 B  183  MET ARG THR SER LYS LYS GLU MET ILE LEU ARG THR ALA          
-SEQRES   2 B  183  ILE ASP TYR ILE GLY GLU TYR SER LEU GLU THR LEU SER          
-SEQRES   3 B  183  TYR ASP SER LEU ALA GLU ALA THR GLY LEU SER LYS SER          
-SEQRES   4 B  183  GLY LEU ILE TYR HIS PHE PRO SER ARG HIS ALA LEU LEU          
-SEQRES   5 B  183  LEU GLY MET HIS GLU LEU LEU ALA ASP ASP TRP ASP LYS          
-SEQRES   6 B  183  GLU LEU ARG ASP ILE THR ARG ASP PRO GLU ASP PRO LEU          
-SEQRES   7 B  183  GLU ARG LEU ARG ALA VAL VAL VAL THR LEU ALA GLU ASN          
-SEQRES   8 B  183  VAL SER ARG PRO GLU LEU LEU LEU LEU ILE ASP ALA PRO          
-SEQRES   9 B  183  SER HIS PRO ASP PHE LEU ASN ALA TRP ARG THR VAL ASN          
-SEQRES  10 B  183  HIS GLN TRP ILE PRO ASP THR ASP ASP LEU GLU ASN ASP          
-SEQRES  11 B  183  ALA HIS LYS ARG ALA VAL TYR LEU VAL GLN LEU ALA ALA          
-SEQRES  12 B  183  ASP GLY LEU PHE VAL HIS ASP TYR ILE HIS ASP ASP VAL          
-SEQRES  13 B  183  LEU SER LYS SER LYS ARG GLN ALA MET LEU GLU THR ILE          
-SEQRES  14 B  183  LEU GLU LEU ILE PRO SER GLU LEU HIS HIS HIS HIS HIS          
-SEQRES  15 B  183  HIS                                                          
-HET     ET  B 184      24                                                       
-HET    SO4  A 184       5                                                       
-HET    SO4  B 185       5                                                       
-HET    SO4  B 186       5                                                       
-HET    GOL  A 185       6                                                       
-HET    GOL  A 186       6                                                       
-HET    GOL  A 187       6                                                       
-HET    GOL  A 188       6                                                       
-HET    GOL  B 187       6                                                       
-HET    GOL  B 188       6                                                       
-HETNAM      ET ETHIDIUM                                                         
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM     GOL GLYCEROL                                                         
-HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
-FORMUL   3   ET    C21 H20 N3 1+                                                
-FORMUL   4  SO4    3(O4 S 2-)                                                   
-FORMUL   7  GOL    6(C3 H8 O3)                                                  
-FORMUL  13  HOH   *357(H2 O)                                                    
-HELIX    1   1 SER A    4  TYR A   20  1                                  17    
-HELIX    2   2 SER A   26  GLY A   35  1                                  10    
-HELIX    3   3 SER A   37  PHE A   45  1                                   9    
-HELIX    4   4 SER A   47  THR A   71  1                                  25    
-HELIX    5   5 ASP A   76  ALA A   89  1                                  14    
-HELIX    6   6 SER A   93  ALA A  103  1                                  11    
-HELIX    7   7 HIS A  106  ILE A  121  1                                  16    
-HELIX    8   8 ASP A  126  ASN A  129  5                                   4    
-HELIX    9   9 ASP A  130  HIS A  153  1                                  24    
-HELIX   10  10 SER A  158  ILE A  173  1                                  16    
-HELIX   11  11 LYS B    5  TYR B   20  1                                  16    
-HELIX   12  12 SER B   26  GLY B   35  1                                  10    
-HELIX   13  13 SER B   37  PHE B   45  1                                   9    
-HELIX   14  14 SER B   47  THR B   71  1                                  25    
-HELIX   15  15 ASP B   76  THR B   87  1                                  12    
-HELIX   16  16 LEU B   88  GLU B   90  5                                   3    
-HELIX   17  17 SER B   93  ILE B  101  1                                   9    
-HELIX   18  18 ASP B  102  SER B  105  5                                   4    
-HELIX   19  19 HIS B  106  ILE B  121  1                                  16    
-HELIX   20  20 ASP B  126  ASN B  129  5                                   4    
-HELIX   21  21 ASP B  130  HIS B  153  1                                  24    
-HELIX   22  22 SER B  158  ILE B  173  1                                  16    
-SITE     1 AC1 11 ILE A 152  HIS A 153  LEU B  59  TRP B  63                    
-SITE     2 AC1 11 THR B  87  LEU B  88  LEU B 100  TRP B 113                    
-SITE     3 AC1 11 GLN B 140  ASP B 144  PHE B 147                               
-SITE     1 AC2  5 SER B  47  ARG B  48  HIS B  49  HIS B 180                    
-SITE     2 AC2  5 HIS B 181                                                     
-SITE     1 AC3  4 SER A  37  LYS A  38  SER A  39  ASP B 154                    
-SITE     1 AC4  6 SER A  26  TYR A  27  ASP A  28  LYS A  38                    
-SITE     2 AC4  6 SER B 158  LYS B 159                                          
-SITE     1 AC5  6 TYR A  16  TYR A  20  THR A  24  SER A  29                    
-SITE     2 AC5  6 GLU A  32  GLU B  23                                          
-SITE     1 AC6  6 GLU A  23  TYR B  16  TYR B  20  THR B  24                    
-SITE     2 AC6  6 SER B  29  GLU B  32                                          
-SITE     1 AC7  4 TYR A  20  SER A  21  LEU B  22  LEU B  98                    
-SITE     1 AC8  2 ARG A  48  LYS B 159                                          
-SITE     1 AC9  6 TYR A  27  ILE A  42  PRO A  46  ASN B  91                    
-SITE     2 AC9  6 SER B 158  LYS B 159                                          
-SITE     1 BC1  4 TRP A  63  GLU A  96  LEU A 100  PHE A 147                    
-CRYST1   62.745   92.226  105.684  90.00  90.00  90.00 P 21 21 21    8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.015938  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.010843  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.009462        0.00000                         
-ATOM      1  N   THR A   3       6.759  30.254  40.449  1.00 54.63           N  
-ATOM      2  CA  THR A   3       6.088  28.964  40.122  1.00 54.98           C  
-ATOM      3  C   THR A   3       5.697  28.207  41.389  1.00 51.69           C  
-ATOM      4  O   THR A   3       4.842  28.661  42.147  1.00 51.40           O  
-ATOM      5  CB  THR A   3       7.010  28.077  39.254  1.00 57.99           C  
-ATOM      6  OG1 THR A   3       6.439  26.769  39.119  1.00 62.38           O  
-ATOM      7  CG2 THR A   3       8.397  27.985  39.875  1.00 61.02           C  
-ATOM      8  N   SER A   4       6.323  27.054  41.610  1.00 49.40           N  
-ATOM      9  CA  SER A   4       6.051  26.243  42.793  1.00 46.26           C  
-ATOM     10  C   SER A   4       6.286  27.065  44.049  1.00 42.85           C  
-ATOM     11  O   SER A   4       7.101  27.987  44.055  1.00 39.86           O  
-ATOM     12  CB  SER A   4       6.970  25.019  42.829  1.00 47.10           C  
-ATOM     13  OG  SER A   4       6.663  24.118  41.786  1.00 51.89           O  
-ATOM     14  N   LYS A   5       5.561  26.736  45.110  1.00 39.35           N  
-ATOM     15  CA  LYS A   5       5.734  27.433  46.371  1.00 37.93           C  
-ATOM     16  C   LYS A   5       7.154  27.060  46.788  1.00 34.25           C  
-ATOM     17  O   LYS A   5       7.909  27.872  47.320  1.00 31.40           O  
-ATOM     18  CB  LYS A   5       4.730  26.910  47.400  1.00 40.95           C  
-ATOM     19  CG  LYS A   5       4.307  27.931  48.434  1.00 44.98           C  
-ATOM     20  CD  LYS A   5       3.461  29.023  47.791  1.00 48.90           C  
-ATOM     21  CE  LYS A   5       2.968  30.029  48.819  1.00 51.12           C  
-ATOM     22  NZ  LYS A   5       2.092  31.062  48.197  1.00 53.40           N  
-ATOM     23  N   LYS A   6       7.507  25.811  46.506  1.00 31.80           N  
-ATOM     24  CA  LYS A   6       8.822  25.285  46.828  1.00 31.88           C  
-ATOM     25  C   LYS A   6       9.918  26.016  46.054  1.00 30.22           C  
-ATOM     26  O   LYS A   6      10.973  26.327  46.609  1.00 27.86           O  
-ATOM     27  CB  LYS A   6       8.864  23.784  46.525  1.00 34.35           C  
-ATOM     28  CG  LYS A   6      10.167  23.116  46.891  1.00 38.56           C  
-ATOM     29  CD  LYS A   6      10.102  21.607  46.695  1.00 41.45           C  
-ATOM     30  CE  LYS A   6      11.424  20.955  47.088  1.00 43.42           C  
-ATOM     31  NZ  LYS A   6      11.391  19.466  46.959  1.00 45.68           N  
-ATOM     32  N   GLU A   7       9.678  26.300  44.776  1.00 27.34           N  
-ATOM     33  CA  GLU A   7      10.693  27.007  44.001  1.00 27.24           C  
-ATOM     34  C   GLU A   7      10.776  28.449  44.461  1.00 24.88           C  
-ATOM     35  O   GLU A   7      11.848  29.043  44.451  1.00 22.36           O  
-ATOM     36  CB  GLU A   7      10.406  26.981  42.497  1.00 29.09           C  
-ATOM     37  CG  GLU A   7      11.602  27.510  41.698  1.00 34.78           C  
-ATOM     38  CD  GLU A   7      11.396  27.500  40.199  1.00 38.73           C  
-ATOM     39  OE1 GLU A   7      11.025  26.437  39.654  1.00 41.69           O  
-ATOM     40  OE2 GLU A   7      11.619  28.555  39.565  1.00 37.91           O  
-ATOM     41  N   MET A   8       9.638  29.013  44.850  1.00 24.58           N  
-ATOM     42  CA  MET A   8       9.599  30.391  45.330  1.00 25.40           C  
-ATOM     43  C   MET A   8      10.507  30.524  46.551  1.00 23.90           C  
-ATOM     44  O   MET A   8      11.253  31.495  46.689  1.00 24.14           O  
-ATOM     45  CB  MET A   8       8.162  30.777  45.701  1.00 26.43           C  
-ATOM     46  CG  MET A   8       8.003  32.166  46.322  1.00 31.95           C  
-ATOM     47  SD  MET A   8       8.424  32.261  48.082  1.00 33.79           S  
-ATOM     48  CE  MET A   8       6.854  31.745  48.840  1.00 35.55           C  
-ATOM     49  N   ILE A   9      10.435  29.538  47.436  1.00 22.65           N  
-ATOM     50  CA  ILE A   9      11.245  29.534  48.643  1.00 21.56           C  
-ATOM     51  C   ILE A   9      12.724  29.516  48.275  1.00 21.47           C  
-ATOM     52  O   ILE A   9      13.513  30.305  48.792  1.00 22.06           O  
-ATOM     53  CB  ILE A   9      10.905  28.304  49.521  1.00 21.91           C  
-ATOM     54  CG1 ILE A   9       9.480  28.442  50.069  1.00 20.95           C  
-ATOM     55  CG2 ILE A   9      11.903  28.184  50.671  1.00 19.46           C  
-ATOM     56  CD1 ILE A   9       8.929  27.173  50.699  1.00 22.35           C  
-ATOM     57  N   LEU A  10      13.086  28.611  47.373  1.00 20.92           N  
-ATOM     58  CA  LEU A  10      14.464  28.467  46.911  1.00 21.88           C  
-ATOM     59  C   LEU A  10      14.988  29.752  46.251  1.00 22.44           C  
-ATOM     60  O   LEU A  10      16.095  30.197  46.554  1.00 19.57           O  
-ATOM     61  CB  LEU A  10      14.543  27.290  45.930  1.00 21.00           C  
-ATOM     62  CG  LEU A  10      15.173  25.955  46.353  1.00 26.08           C  
-ATOM     63  CD1 LEU A  10      15.264  25.813  47.863  1.00 23.35           C  
-ATOM     64  CD2 LEU A  10      14.381  24.817  45.729  1.00 23.73           C  
-ATOM     65  N   ARG A  11      14.191  30.348  45.364  1.00 20.79           N  
-ATOM     66  CA  ARG A  11      14.596  31.581  44.682  1.00 22.42           C  
-ATOM     67  C   ARG A  11      14.827  32.707  45.689  1.00 21.22           C  
-ATOM     68  O   ARG A  11      15.779  33.486  45.565  1.00 22.54           O  
-ATOM     69  CB  ARG A  11      13.528  32.019  43.670  1.00 23.75           C  
-ATOM     70  CG  ARG A  11      13.290  31.046  42.518  1.00 24.87           C  
-ATOM     71  CD  ARG A  11      14.475  30.938  41.565  1.00 26.06           C  
-ATOM     72  NE  ARG A  11      14.195  30.009  40.468  1.00 24.38           N  
-ATOM     73  CZ  ARG A  11      15.107  29.547  39.616  1.00 24.76           C  
-ATOM     74  NH1 ARG A  11      16.378  29.925  39.718  1.00 21.41           N  
-ATOM     75  NH2 ARG A  11      14.752  28.683  38.672  1.00 21.33           N  
-ATOM     76  N   THR A  12      13.954  32.788  46.686  1.00 18.75           N  
-ATOM     77  CA  THR A  12      14.056  33.806  47.723  1.00 19.52           C  
-ATOM     78  C   THR A  12      15.331  33.620  48.553  1.00 20.02           C  
-ATOM     79  O   THR A  12      16.010  34.594  48.891  1.00 18.73           O  
-ATOM     80  CB  THR A  12      12.815  33.759  48.644  1.00 20.96           C  
-ATOM     81  OG1 THR A  12      11.632  33.886  47.842  1.00 23.72           O  
-ATOM     82  CG2 THR A  12      12.848  34.891  49.660  1.00 20.80           C  
-ATOM     83  N   ALA A  13      15.658  32.367  48.870  1.00 19.07           N  
-ATOM     84  CA  ALA A  13      16.864  32.056  49.642  1.00 20.35           C  
-ATOM     85  C   ALA A  13      18.114  32.404  48.837  1.00 19.60           C  
-ATOM     86  O   ALA A  13      19.106  32.882  49.390  1.00 20.22           O  
-ATOM     87  CB  ALA A  13      16.891  30.577  50.014  1.00 19.02           C  
-ATOM     88  N   ILE A  14      18.068  32.143  47.534  1.00 18.93           N  
-ATOM     89  CA  ILE A  14      19.202  32.441  46.664  1.00 19.28           C  
-ATOM     90  C   ILE A  14      19.425  33.955  46.626  1.00 21.50           C  
-ATOM     91  O   ILE A  14      20.553  34.429  46.795  1.00 19.68           O  
-ATOM     92  CB  ILE A  14      18.959  31.858  45.248  1.00 18.51           C  
-ATOM     93  CG1 ILE A  14      18.980  30.326  45.338  1.00 19.36           C  
-ATOM     94  CG2 ILE A  14      20.035  32.326  44.268  1.00 20.22           C  
-ATOM     95  CD1 ILE A  14      18.630  29.619  44.060  1.00 22.34           C  
-ATOM     96  N   ASP A  15      18.350  34.717  46.439  1.00 21.84           N  
-ATOM     97  CA  ASP A  15      18.467  36.176  46.413  1.00 25.32           C  
-ATOM     98  C   ASP A  15      18.980  36.681  47.757  1.00 23.79           C  
-ATOM     99  O   ASP A  15      19.760  37.633  47.826  1.00 24.16           O  
-ATOM    100  CB  ASP A  15      17.116  36.845  46.131  1.00 28.00           C  
-ATOM    101  CG  ASP A  15      16.646  36.655  44.699  1.00 33.80           C  
-ATOM    102  OD1 ASP A  15      17.496  36.494  43.798  1.00 37.29           O  
-ATOM    103  OD2 ASP A  15      15.416  36.687  44.473  1.00 38.49           O  
-ATOM    104  N   TYR A  16      18.533  36.042  48.830  1.00 22.28           N  
-ATOM    105  CA  TYR A  16      18.941  36.443  50.169  1.00 21.85           C  
-ATOM    106  C   TYR A  16      20.445  36.393  50.428  1.00 20.90           C  
-ATOM    107  O   TYR A  16      21.009  37.340  50.978  1.00 20.07           O  
-ATOM    108  CB  TYR A  16      18.226  35.592  51.229  1.00 20.65           C  
-ATOM    109  CG  TYR A  16      18.667  35.897  52.649  1.00 22.57           C  
-ATOM    110  CD1 TYR A  16      19.815  35.312  53.188  1.00 21.53           C  
-ATOM    111  CD2 TYR A  16      17.961  36.812  53.437  1.00 21.89           C  
-ATOM    112  CE1 TYR A  16      20.251  35.634  54.478  1.00 21.46           C  
-ATOM    113  CE2 TYR A  16      18.389  37.142  54.725  1.00 21.35           C  
-ATOM    114  CZ  TYR A  16      19.531  36.554  55.238  1.00 22.12           C  
-ATOM    115  OH  TYR A  16      19.971  36.903  56.496  1.00 21.23           O  
-ATOM    116  N   ILE A  17      21.099  35.299  50.044  1.00 18.85           N  
-ATOM    117  CA  ILE A  17      22.529  35.174  50.317  1.00 19.12           C  
-ATOM    118  C   ILE A  17      23.370  36.177  49.550  1.00 19.68           C  
-ATOM    119  O   ILE A  17      24.482  36.496  49.961  1.00 19.81           O  
-ATOM    120  CB  ILE A  17      23.051  33.758  50.024  1.00 20.06           C  
-ATOM    121  CG1 ILE A  17      22.982  33.472  48.522  1.00 21.58           C  
-ATOM    122  CG2 ILE A  17      22.247  32.735  50.842  1.00 22.13           C  
-ATOM    123  CD1 ILE A  17      23.725  32.229  48.107  1.00 23.77           C  
-ATOM    124  N   GLY A  18      22.840  36.673  48.439  1.00 21.70           N  
-ATOM    125  CA  GLY A  18      23.570  37.655  47.658  1.00 23.10           C  
-ATOM    126  C   GLY A  18      23.521  39.014  48.330  1.00 26.22           C  
-ATOM    127  O   GLY A  18      24.473  39.795  48.256  1.00 26.65           O  
-ATOM    128  N   GLU A  19      22.407  39.294  48.998  1.00 26.46           N  
-ATOM    129  CA  GLU A  19      22.216  40.568  49.681  1.00 27.86           C  
-ATOM    130  C   GLU A  19      22.778  40.565  51.095  1.00 26.65           C  
-ATOM    131  O   GLU A  19      23.256  41.586  51.584  1.00 28.29           O  
-ATOM    132  CB  GLU A  19      20.725  40.921  49.709  1.00 30.60           C  
-ATOM    133  CG  GLU A  19      20.376  42.119  50.586  1.00 37.41           C  
-ATOM    134  CD  GLU A  19      18.955  42.619  50.362  1.00 41.54           C  
-ATOM    135  OE1 GLU A  19      18.043  41.778  50.197  1.00 42.79           O  
-ATOM    136  OE2 GLU A  19      18.750  43.854  50.365  1.00 43.83           O  
-ATOM    137  N   TYR A  20      22.726  39.416  51.756  1.00 25.02           N  
-ATOM    138  CA  TYR A  20      23.238  39.315  53.114  1.00 22.91           C  
-ATOM    139  C   TYR A  20      24.403  38.342  53.142  1.00 22.29           C  
-ATOM    140  O   TYR A  20      25.542  38.737  52.898  1.00 21.24           O  
-ATOM    141  CB  TYR A  20      22.108  38.883  54.044  1.00 22.91           C  
-ATOM    142  CG  TYR A  20      21.045  39.949  54.149  1.00 24.20           C  
-ATOM    143  CD1 TYR A  20      21.234  41.065  54.967  1.00 26.95           C  
-ATOM    144  CD2 TYR A  20      19.879  39.882  53.383  1.00 25.34           C  
-ATOM    145  CE1 TYR A  20      20.291  42.089  55.022  1.00 27.16           C  
-ATOM    146  CE2 TYR A  20      18.927  40.905  53.427  1.00 26.95           C  
-ATOM    147  CZ  TYR A  20      19.142  42.004  54.249  1.00 28.44           C  
-ATOM    148  OH  TYR A  20      18.217  43.023  54.297  1.00 29.17           O  
-ATOM    149  N   SER A  21      24.130  37.076  53.436  1.00 20.03           N  
-ATOM    150  CA  SER A  21      25.188  36.077  53.441  1.00 20.32           C  
-ATOM    151  C   SER A  21      24.624  34.682  53.580  1.00 20.73           C  
-ATOM    152  O   SER A  21      23.459  34.494  53.936  1.00 20.99           O  
-ATOM    153  CB  SER A  21      26.179  36.317  54.590  1.00 19.31           C  
-ATOM    154  OG  SER A  21      25.607  35.989  55.847  1.00 17.68           O  
-ATOM    155  N   LEU A  22      25.474  33.706  53.294  1.00 20.40           N  
-ATOM    156  CA  LEU A  22      25.116  32.304  53.424  1.00 21.48           C  
-ATOM    157  C   LEU A  22      24.982  32.044  54.929  1.00 20.46           C  
-ATOM    158  O   LEU A  22      24.048  31.381  55.381  1.00 18.87           O  
-ATOM    159  CB  LEU A  22      26.239  31.453  52.833  1.00 22.97           C  
-ATOM    160  CG  LEU A  22      26.000  30.290  51.865  1.00 29.63           C  
-ATOM    161  CD1 LEU A  22      24.695  30.418  51.119  1.00 28.35           C  
-ATOM    162  CD2 LEU A  22      27.179  30.245  50.892  1.00 28.43           C  
-ATOM    163  N   GLU A  23      25.904  32.603  55.711  1.00 20.09           N  
-ATOM    164  CA  GLU A  23      25.881  32.394  57.157  1.00 20.50           C  
-ATOM    165  C   GLU A  23      24.570  32.744  57.846  1.00 20.11           C  
-ATOM    166  O   GLU A  23      24.089  31.976  58.687  1.00 20.16           O  
-ATOM    167  CB  GLU A  23      27.012  33.166  57.852  1.00 21.07           C  
-ATOM    168  CG  GLU A  23      26.924  33.072  59.376  1.00 21.23           C  
-ATOM    169  CD  GLU A  23      27.925  33.949  60.109  1.00 23.52           C  
-ATOM    170  OE1 GLU A  23      28.501  34.877  59.496  1.00 19.86           O  
-ATOM    171  OE2 GLU A  23      28.124  33.710  61.318  1.00 25.43           O  
-ATOM    172  N   THR A  24      23.991  33.893  57.511  1.00 18.81           N  
-ATOM    173  CA  THR A  24      22.754  34.304  58.161  1.00 21.05           C  
-ATOM    174  C   THR A  24      21.476  33.778  57.517  1.00 20.36           C  
-ATOM    175  O   THR A  24      20.380  34.185  57.895  1.00 20.03           O  
-ATOM    176  CB  THR A  24      22.662  35.849  58.288  1.00 19.89           C  
-ATOM    177  OG1 THR A  24      22.558  36.439  56.990  1.00 19.65           O  
-ATOM    178  CG2 THR A  24      23.903  36.389  58.988  1.00 21.59           C  
-ATOM    179  N   LEU A  25      21.605  32.881  56.543  1.00 20.12           N  
-ATOM    180  CA  LEU A  25      20.416  32.298  55.934  1.00 20.41           C  
-ATOM    181  C   LEU A  25      19.897  31.313  56.980  1.00 21.44           C  
-ATOM    182  O   LEU A  25      20.547  30.306  57.273  1.00 21.16           O  
-ATOM    183  CB  LEU A  25      20.763  31.558  54.640  1.00 19.69           C  
-ATOM    184  CG  LEU A  25      19.639  30.710  54.025  1.00 19.74           C  
-ATOM    185  CD1 LEU A  25      18.411  31.569  53.730  1.00 20.52           C  
-ATOM    186  CD2 LEU A  25      20.162  30.057  52.745  1.00 23.02           C  
-ATOM    187  N   SER A  26      18.739  31.623  57.553  1.00 21.44           N  
-ATOM    188  CA  SER A  26      18.140  30.794  58.595  1.00 21.41           C  
-ATOM    189  C   SER A  26      16.634  30.705  58.388  1.00 20.77           C  
-ATOM    190  O   SER A  26      16.084  31.360  57.508  1.00 18.87           O  
-ATOM    191  CB  SER A  26      18.410  31.415  59.965  1.00 23.26           C  
-ATOM    192  OG  SER A  26      17.753  32.673  60.081  1.00 23.43           O  
-ATOM    193  N   TYR A  27      15.954  29.898  59.192  1.00 20.99           N  
-ATOM    194  CA  TYR A  27      14.516  29.823  59.022  1.00 21.76           C  
-ATOM    195  C   TYR A  27      13.911  31.162  59.411  1.00 23.14           C  
-ATOM    196  O   TYR A  27      12.910  31.588  58.842  1.00 23.30           O  
-ATOM    197  CB  TYR A  27      13.928  28.680  59.844  1.00 21.19           C  
-ATOM    198  CG  TYR A  27      14.127  27.346  59.159  1.00 20.50           C  
-ATOM    199  CD1 TYR A  27      15.335  26.659  59.261  1.00 19.59           C  
-ATOM    200  CD2 TYR A  27      13.123  26.799  58.362  1.00 19.09           C  
-ATOM    201  CE1 TYR A  27      15.541  25.452  58.580  1.00 20.71           C  
-ATOM    202  CE2 TYR A  27      13.315  25.597  57.681  1.00 21.25           C  
-ATOM    203  CZ  TYR A  27      14.524  24.929  57.794  1.00 20.71           C  
-ATOM    204  OH  TYR A  27      14.705  23.730  57.138  1.00 22.74           O  
-ATOM    205  N   ASP A  28      14.544  31.844  60.362  1.00 23.38           N  
-ATOM    206  CA  ASP A  28      14.059  33.152  60.783  1.00 24.64           C  
-ATOM    207  C   ASP A  28      14.168  34.158  59.637  1.00 23.80           C  
-ATOM    208  O   ASP A  28      13.186  34.807  59.284  1.00 23.15           O  
-ATOM    209  CB  ASP A  28      14.855  33.663  61.982  1.00 29.60           C  
-ATOM    210  CG  ASP A  28      14.309  34.969  62.520  1.00 35.83           C  
-ATOM    211  OD1 ASP A  28      13.181  34.966  63.055  1.00 39.20           O  
-ATOM    212  OD2 ASP A  28      15.001  35.999  62.400  1.00 40.34           O  
-ATOM    213  N   SER A  29      15.357  34.280  59.047  1.00 21.93           N  
-ATOM    214  CA  SER A  29      15.546  35.226  57.952  1.00 22.02           C  
-ATOM    215  C   SER A  29      14.807  34.811  56.681  1.00 21.48           C  
-ATOM    216  O   SER A  29      14.342  35.665  55.932  1.00 20.57           O  
-ATOM    217  CB  SER A  29      17.044  35.436  57.654  1.00 22.25           C  
-ATOM    218  OG  SER A  29      17.677  34.251  57.192  1.00 22.86           O  
-ATOM    219  N   LEU A  30      14.687  33.509  56.431  1.00 20.65           N  
-ATOM    220  CA  LEU A  30      13.986  33.057  55.230  1.00 20.02           C  
-ATOM    221  C   LEU A  30      12.477  33.258  55.400  1.00 19.64           C  
-ATOM    222  O   LEU A  30      11.765  33.545  54.434  1.00 20.92           O  
-ATOM    223  CB  LEU A  30      14.296  31.579  54.939  1.00 19.45           C  
-ATOM    224  CG  LEU A  30      13.727  30.992  53.639  1.00 21.16           C  
-ATOM    225  CD1 LEU A  30      14.172  31.826  52.436  1.00 19.90           C  
-ATOM    226  CD2 LEU A  30      14.205  29.543  53.480  1.00 21.18           C  
-ATOM    227  N   ALA A  31      11.987  33.104  56.625  1.00 19.40           N  
-ATOM    228  CA  ALA A  31      10.562  33.303  56.884  1.00 20.82           C  
-ATOM    229  C   ALA A  31      10.224  34.771  56.627  1.00 21.99           C  
-ATOM    230  O   ALA A  31       9.208  35.093  56.006  1.00 23.60           O  
-ATOM    231  CB  ALA A  31      10.225  32.938  58.328  1.00 20.59           C  
-ATOM    232  N   GLU A  32      11.082  35.661  57.106  1.00 24.88           N  
-ATOM    233  CA  GLU A  32      10.851  37.086  56.917  1.00 27.09           C  
-ATOM    234  C   GLU A  32      10.873  37.422  55.430  1.00 26.22           C  
-ATOM    235  O   GLU A  32      10.029  38.171  54.938  1.00 26.42           O  
-ATOM    236  CB  GLU A  32      11.920  37.897  57.649  1.00 30.77           C  
-ATOM    237  CG  GLU A  32      11.620  39.386  57.712  1.00 38.84           C  
-ATOM    238  CD  GLU A  32      12.674  40.160  58.480  1.00 42.89           C  
-ATOM    239  OE1 GLU A  32      12.969  39.781  59.635  1.00 46.78           O  
-ATOM    240  OE2 GLU A  32      13.203  41.149  57.932  1.00 47.00           O  
-ATOM    241  N   ALA A  33      11.833  36.846  54.713  1.00 24.68           N  
-ATOM    242  CA  ALA A  33      11.977  37.090  53.283  1.00 23.93           C  
-ATOM    243  C   ALA A  33      10.830  36.543  52.428  1.00 24.50           C  
-ATOM    244  O   ALA A  33      10.420  37.185  51.465  1.00 22.31           O  
-ATOM    245  CB  ALA A  33      13.306  36.514  52.792  1.00 22.38           C  
-ATOM    246  N   THR A  34      10.323  35.358  52.768  1.00 24.03           N  
-ATOM    247  CA  THR A  34       9.235  34.743  51.998  1.00 22.92           C  
-ATOM    248  C   THR A  34       7.834  35.105  52.489  1.00 23.57           C  
-ATOM    249  O   THR A  34       6.865  34.991  51.741  1.00 25.88           O  
-ATOM    250  CB  THR A  34       9.311  33.200  52.030  1.00 22.03           C  
-ATOM    251  OG1 THR A  34       9.205  32.757  53.388  1.00 17.73           O  
-ATOM    252  CG2 THR A  34      10.620  32.700  51.424  1.00 20.95           C  
-ATOM    253  N   GLY A  35       7.721  35.525  53.743  1.00 24.28           N  
-ATOM    254  CA  GLY A  35       6.411  35.850  54.281  1.00 24.36           C  
-ATOM    255  C   GLY A  35       5.723  34.594  54.797  1.00 26.04           C  
-ATOM    256  O   GLY A  35       4.572  34.635  55.235  1.00 26.63           O  
-ATOM    257  N   LEU A  36       6.428  33.466  54.726  1.00 24.31           N  
-ATOM    258  CA  LEU A  36       5.903  32.193  55.211  1.00 24.27           C  
-ATOM    259  C   LEU A  36       6.381  31.957  56.639  1.00 24.26           C  
-ATOM    260  O   LEU A  36       7.412  32.483  57.047  1.00 24.00           O  
-ATOM    261  CB  LEU A  36       6.400  31.039  54.340  1.00 24.89           C  
-ATOM    262  CG  LEU A  36       5.756  30.740  52.989  1.00 28.32           C  
-ATOM    263  CD1 LEU A  36       5.699  31.987  52.130  1.00 33.78           C  
-ATOM    264  CD2 LEU A  36       6.570  29.640  52.305  1.00 27.91           C  
-ATOM    265  N   SER A  37       5.630  31.167  57.400  1.00 22.14           N  
-ATOM    266  CA  SER A  37       6.015  30.853  58.770  1.00 21.53           C  
-ATOM    267  C   SER A  37       7.103  29.784  58.708  1.00 21.20           C  
-ATOM    268  O   SER A  37       7.315  29.172  57.658  1.00 20.10           O  
-ATOM    269  CB  SER A  37       4.814  30.294  59.539  1.00 23.03           C  
-ATOM    270  OG  SER A  37       4.348  29.098  58.922  1.00 21.73           O  
-ATOM    271  N   LYS A  38       7.798  29.561  59.820  1.00 19.95           N  
-ATOM    272  CA  LYS A  38       8.817  28.521  59.844  1.00 22.39           C  
-ATOM    273  C   LYS A  38       8.125  27.173  59.618  1.00 20.92           C  
-ATOM    274  O   LYS A  38       8.685  26.284  58.978  1.00 20.07           O  
-ATOM    275  CB  LYS A  38       9.559  28.514  61.186  1.00 23.71           C  
-ATOM    276  CG  LYS A  38      10.465  29.725  61.399  1.00 26.65           C  
-ATOM    277  CD  LYS A  38      11.303  29.564  62.660  1.00 28.40           C  
-ATOM    278  CE  LYS A  38      12.231  30.744  62.874  1.00 32.33           C  
-ATOM    279  NZ  LYS A  38      13.081  30.577  64.095  1.00 32.12           N  
-ATOM    280  N   SER A  39       6.904  27.032  60.137  1.00 20.21           N  
-ATOM    281  CA  SER A  39       6.137  25.797  59.965  1.00 20.33           C  
-ATOM    282  C   SER A  39       5.960  25.532  58.475  1.00 21.53           C  
-ATOM    283  O   SER A  39       6.105  24.398  58.011  1.00 19.85           O  
-ATOM    284  CB  SER A  39       4.746  25.909  60.613  1.00 20.43           C  
-ATOM    285  OG  SER A  39       4.818  26.032  62.024  1.00 20.18           O  
-ATOM    286  N   GLY A  40       5.642  26.594  57.734  1.00 19.89           N  
-ATOM    287  CA  GLY A  40       5.439  26.480  56.301  1.00 19.27           C  
-ATOM    288  C   GLY A  40       6.713  26.127  55.551  1.00 19.33           C  
-ATOM    289  O   GLY A  40       6.672  25.417  54.544  1.00 18.17           O  
-ATOM    290  N   LEU A  41       7.844  26.626  56.041  1.00 18.20           N  
-ATOM    291  CA  LEU A  41       9.134  26.356  55.418  1.00 17.51           C  
-ATOM    292  C   LEU A  41       9.538  24.900  55.638  1.00 18.33           C  
-ATOM    293  O   LEU A  41       9.964  24.219  54.704  1.00 19.35           O  
-ATOM    294  CB  LEU A  41      10.207  27.279  56.006  1.00 16.22           C  
-ATOM    295  CG  LEU A  41      10.064  28.772  55.677  1.00 19.26           C  
-ATOM    296  CD1 LEU A  41      11.159  29.570  56.387  1.00 18.28           C  
-ATOM    297  CD2 LEU A  41      10.160  28.961  54.164  1.00 16.38           C  
-ATOM    298  N   ILE A  42       9.401  24.437  56.878  1.00 18.50           N  
-ATOM    299  CA  ILE A  42       9.750  23.062  57.250  1.00 19.80           C  
-ATOM    300  C   ILE A  42       8.958  22.047  56.437  1.00 20.54           C  
-ATOM    301  O   ILE A  42       9.465  20.977  56.074  1.00 19.34           O  
-ATOM    302  CB  ILE A  42       9.493  22.834  58.757  1.00 21.87           C  
-ATOM    303  CG1 ILE A  42      10.476  23.673  59.569  1.00 24.63           C  
-ATOM    304  CG2 ILE A  42       9.646  21.357  59.113  1.00 23.79           C  
-ATOM    305  CD1 ILE A  42      10.185  23.696  61.056  1.00 27.34           C  
-ATOM    306  N   TYR A  43       7.707  22.398  56.159  1.00 19.01           N  
-ATOM    307  CA  TYR A  43       6.804  21.563  55.382  1.00 19.44           C  
-ATOM    308  C   TYR A  43       7.475  21.157  54.077  1.00 19.92           C  
-ATOM    309  O   TYR A  43       7.278  20.042  53.591  1.00 19.12           O  
-ATOM    310  CB  TYR A  43       5.528  22.354  55.080  1.00 19.54           C  
-ATOM    311  CG  TYR A  43       4.439  21.590  54.367  1.00 20.21           C  
-ATOM    312  CD1 TYR A  43       3.511  20.828  55.084  1.00 21.51           C  
-ATOM    313  CD2 TYR A  43       4.297  21.673  52.984  1.00 19.89           C  
-ATOM    314  CE1 TYR A  43       2.463  20.177  54.437  1.00 21.53           C  
-ATOM    315  CE2 TYR A  43       3.255  21.025  52.326  1.00 22.11           C  
-ATOM    316  CZ  TYR A  43       2.339  20.280  53.062  1.00 21.98           C  
-ATOM    317  OH  TYR A  43       1.295  19.655  52.421  1.00 23.92           O  
-ATOM    318  N   HIS A  44       8.270  22.069  53.515  1.00 20.36           N  
-ATOM    319  CA  HIS A  44       8.967  21.817  52.255  1.00 21.47           C  
-ATOM    320  C   HIS A  44      10.454  21.484  52.395  1.00 21.82           C  
-ATOM    321  O   HIS A  44      10.986  20.673  51.636  1.00 22.01           O  
-ATOM    322  CB  HIS A  44       8.813  23.021  51.317  1.00 22.72           C  
-ATOM    323  CG  HIS A  44       7.419  23.207  50.806  1.00 26.01           C  
-ATOM    324  ND1 HIS A  44       6.596  24.225  51.237  1.00 26.45           N  
-ATOM    325  CD2 HIS A  44       6.696  22.490  49.914  1.00 24.07           C  
-ATOM    326  CE1 HIS A  44       5.427  24.130  50.630  1.00 27.44           C  
-ATOM    327  NE2 HIS A  44       5.461  23.085  49.821  1.00 26.42           N  
-ATOM    328  N   PHE A  45      11.127  22.121  53.346  1.00 22.03           N  
-ATOM    329  CA  PHE A  45      12.553  21.875  53.566  1.00 21.43           C  
-ATOM    330  C   PHE A  45      12.732  21.643  55.058  1.00 20.20           C  
-ATOM    331  O   PHE A  45      12.686  22.580  55.853  1.00 20.45           O  
-ATOM    332  CB  PHE A  45      13.363  23.079  53.073  1.00 23.13           C  
-ATOM    333  CG  PHE A  45      13.207  23.333  51.600  1.00 23.90           C  
-ATOM    334  CD1 PHE A  45      13.886  22.548  50.669  1.00 22.66           C  
-ATOM    335  CD2 PHE A  45      12.323  24.307  51.141  1.00 24.07           C  
-ATOM    336  CE1 PHE A  45      13.685  22.726  49.299  1.00 26.11           C  
-ATOM    337  CE2 PHE A  45      12.114  24.494  49.778  1.00 25.09           C  
-ATOM    338  CZ  PHE A  45      12.795  23.702  48.852  1.00 24.96           C  
-ATOM    339  N   PRO A  46      12.947  20.374  55.451  1.00 21.03           N  
-ATOM    340  CA  PRO A  46      13.129  19.903  56.829  1.00 22.85           C  
-ATOM    341  C   PRO A  46      14.305  20.489  57.591  1.00 21.99           C  
-ATOM    342  O   PRO A  46      14.244  20.644  58.812  1.00 21.63           O  
-ATOM    343  CB  PRO A  46      13.292  18.384  56.675  1.00 21.82           C  
-ATOM    344  CG  PRO A  46      12.877  18.085  55.276  1.00 26.43           C  
-ATOM    345  CD  PRO A  46      13.248  19.296  54.496  1.00 21.16           C  
-ATOM    346  N   SER A  47      15.381  20.796  56.879  1.00 19.69           N  
-ATOM    347  CA  SER A  47      16.571  21.328  57.532  1.00 20.23           C  
-ATOM    348  C   SER A  47      17.280  22.340  56.650  1.00 19.50           C  
-ATOM    349  O   SER A  47      16.997  22.445  55.459  1.00 19.09           O  
-ATOM    350  CB  SER A  47      17.537  20.188  57.834  1.00 18.42           C  
-ATOM    351  OG  SER A  47      17.996  19.621  56.617  1.00 20.75           O  
-ATOM    352  N   ARG A  48      18.210  23.075  57.248  1.00 19.87           N  
-ATOM    353  CA  ARG A  48      18.977  24.073  56.515  1.00 20.08           C  
-ATOM    354  C   ARG A  48      19.797  23.352  55.456  1.00 20.38           C  
-ATOM    355  O   ARG A  48      20.023  23.873  54.356  1.00 18.36           O  
-ATOM    356  CB  ARG A  48      19.893  24.843  57.473  1.00 20.87           C  
-ATOM    357  CG  ARG A  48      20.718  25.942  56.813  1.00 22.32           C  
-ATOM    358  CD  ARG A  48      21.282  26.898  57.868  1.00 24.86           C  
-ATOM    359  NE  ARG A  48      22.105  27.952  57.279  1.00 24.02           N  
-ATOM    360  CZ  ARG A  48      23.365  27.795  56.893  1.00 24.90           C  
-ATOM    361  NH1 ARG A  48      23.965  26.620  57.035  1.00 22.58           N  
-ATOM    362  NH2 ARG A  48      24.025  28.817  56.364  1.00 25.69           N  
-ATOM    363  N   HIS A  49      20.240  22.142  55.783  1.00 20.34           N  
-ATOM    364  CA  HIS A  49      21.014  21.367  54.824  1.00 21.05           C  
-ATOM    365  C   HIS A  49      20.158  21.073  53.591  1.00 21.27           C  
-ATOM    366  O   HIS A  49      20.625  21.184  52.455  1.00 19.62           O  
-ATOM    367  CB  HIS A  49      21.469  20.041  55.433  1.00 22.69           C  
-ATOM    368  CG  HIS A  49      22.319  19.229  54.510  1.00 21.95           C  
-ATOM    369  ND1 HIS A  49      23.666  19.463  54.343  1.00 22.76           N  
-ATOM    370  CD2 HIS A  49      22.002  18.229  53.655  1.00 23.44           C  
-ATOM    371  CE1 HIS A  49      24.143  18.643  53.424  1.00 22.42           C  
-ATOM    372  NE2 HIS A  49      23.153  17.884  52.989  1.00 25.70           N  
-ATOM    373  N   ALA A  50      18.907  20.683  53.821  1.00 19.38           N  
-ATOM    374  CA  ALA A  50      17.996  20.367  52.720  1.00 20.26           C  
-ATOM    375  C   ALA A  50      17.761  21.614  51.870  1.00 18.58           C  
-ATOM    376  O   ALA A  50      17.683  21.543  50.643  1.00 18.64           O  
-ATOM    377  CB  ALA A  50      16.668  19.845  53.267  1.00 19.31           C  
-ATOM    378  N   LEU A  51      17.647  22.759  52.532  1.00 18.68           N  
-ATOM    379  CA  LEU A  51      17.434  24.021  51.829  1.00 18.60           C  
-ATOM    380  C   LEU A  51      18.630  24.335  50.916  1.00 18.69           C  
-ATOM    381  O   LEU A  51      18.464  24.591  49.718  1.00 18.82           O  
-ATOM    382  CB  LEU A  51      17.237  25.148  52.846  1.00 17.82           C  
-ATOM    383  CG  LEU A  51      17.096  26.560  52.283  1.00 22.53           C  
-ATOM    384  CD1 LEU A  51      15.742  26.696  51.577  1.00 23.35           C  
-ATOM    385  CD2 LEU A  51      17.211  27.574  53.427  1.00 21.61           C  
-ATOM    386  N   LEU A  52      19.834  24.317  51.484  1.00 19.92           N  
-ATOM    387  CA  LEU A  52      21.050  24.591  50.713  1.00 19.79           C  
-ATOM    388  C   LEU A  52      21.179  23.627  49.532  1.00 19.07           C  
-ATOM    389  O   LEU A  52      21.508  24.031  48.417  1.00 18.28           O  
-ATOM    390  CB  LEU A  52      22.284  24.468  51.616  1.00 21.65           C  
-ATOM    391  CG  LEU A  52      22.833  25.687  52.366  1.00 26.85           C  
-ATOM    392  CD1 LEU A  52      21.738  26.662  52.714  1.00 30.69           C  
-ATOM    393  CD2 LEU A  52      23.568  25.205  53.621  1.00 26.70           C  
-ATOM    394  N   LEU A  53      20.933  22.345  49.781  1.00 17.74           N  
-ATOM    395  CA  LEU A  53      21.012  21.355  48.717  1.00 17.69           C  
-ATOM    396  C   LEU A  53      20.028  21.728  47.612  1.00 16.90           C  
-ATOM    397  O   LEU A  53      20.354  21.669  46.427  1.00 18.49           O  
-ATOM    398  CB  LEU A  53      20.677  19.960  49.258  1.00 19.20           C  
-ATOM    399  CG  LEU A  53      20.638  18.843  48.214  1.00 19.09           C  
-ATOM    400  CD1 LEU A  53      21.970  18.783  47.470  1.00 18.82           C  
-ATOM    401  CD2 LEU A  53      20.347  17.509  48.905  1.00 20.43           C  
-ATOM    402  N   GLY A  54      18.822  22.116  48.010  1.00 17.71           N  
-ATOM    403  CA  GLY A  54      17.819  22.501  47.032  1.00 17.73           C  
-ATOM    404  C   GLY A  54      18.272  23.689  46.197  1.00 18.01           C  
-ATOM    405  O   GLY A  54      18.002  23.755  45.000  1.00 17.04           O  
-ATOM    406  N   MET A  55      18.971  24.627  46.831  1.00 18.23           N  
-ATOM    407  CA  MET A  55      19.460  25.816  46.142  1.00 17.35           C  
-ATOM    408  C   MET A  55      20.512  25.442  45.100  1.00 17.74           C  
-ATOM    409  O   MET A  55      20.477  25.928  43.972  1.00 19.11           O  
-ATOM    410  CB  MET A  55      20.030  26.800  47.163  1.00 18.60           C  
-ATOM    411  CG  MET A  55      18.977  27.317  48.139  1.00 17.85           C  
-ATOM    412  SD  MET A  55      19.639  28.088  49.620  1.00 20.18           S  
-ATOM    413  CE  MET A  55      20.428  29.583  48.912  1.00 17.61           C  
-ATOM    414  N   HIS A  56      21.447  24.578  45.479  1.00 18.97           N  
-ATOM    415  CA  HIS A  56      22.486  24.122  44.559  1.00 18.30           C  
-ATOM    416  C   HIS A  56      21.877  23.366  43.373  1.00 19.54           C  
-ATOM    417  O   HIS A  56      22.251  23.594  42.220  1.00 19.02           O  
-ATOM    418  CB  HIS A  56      23.464  23.204  45.288  1.00 18.76           C  
-ATOM    419  CG  HIS A  56      24.440  23.928  46.162  1.00 18.53           C  
-ATOM    420  ND1 HIS A  56      25.564  24.552  45.664  1.00 18.13           N  
-ATOM    421  CD2 HIS A  56      24.480  24.096  47.505  1.00 19.37           C  
-ATOM    422  CE1 HIS A  56      26.259  25.068  46.663  1.00 17.04           C  
-ATOM    423  NE2 HIS A  56      25.623  24.805  47.791  1.00 18.71           N  
-ATOM    424  N   GLU A  57      20.955  22.451  43.661  1.00 19.98           N  
-ATOM    425  CA  GLU A  57      20.301  21.671  42.608  1.00 20.20           C  
-ATOM    426  C   GLU A  57      19.528  22.575  41.646  1.00 19.47           C  
-ATOM    427  O   GLU A  57      19.493  22.327  40.441  1.00 19.81           O  
-ATOM    428  CB  GLU A  57      19.334  20.641  43.218  1.00 20.73           C  
-ATOM    429  CG  GLU A  57      19.996  19.642  44.171  1.00 22.80           C  
-ATOM    430  CD  GLU A  57      19.008  18.646  44.765  1.00 25.41           C  
-ATOM    431  OE1 GLU A  57      17.858  19.041  45.046  1.00 25.82           O  
-ATOM    432  OE2 GLU A  57      19.388  17.473  44.965  1.00 24.04           O  
-ATOM    433  N   LEU A  58      18.905  23.622  42.177  1.00 20.26           N  
-ATOM    434  CA  LEU A  58      18.133  24.532  41.341  1.00 19.87           C  
-ATOM    435  C   LEU A  58      19.025  25.262  40.337  1.00 21.17           C  
-ATOM    436  O   LEU A  58      18.707  25.337  39.148  1.00 21.28           O  
-ATOM    437  CB  LEU A  58      17.377  25.546  42.206  1.00 19.64           C  
-ATOM    438  CG  LEU A  58      16.460  26.510  41.438  1.00 21.59           C  
-ATOM    439  CD1 LEU A  58      15.416  25.718  40.654  1.00 24.79           C  
-ATOM    440  CD2 LEU A  58      15.776  27.453  42.407  1.00 22.58           C  
-ATOM    441  N   LEU A  59      20.145  25.794  40.814  1.00 20.81           N  
-ATOM    442  CA  LEU A  59      21.070  26.514  39.946  1.00 22.05           C  
-ATOM    443  C   LEU A  59      21.688  25.591  38.906  1.00 22.11           C  
-ATOM    444  O   LEU A  59      21.867  25.976  37.747  1.00 20.42           O  
-ATOM    445  CB  LEU A  59      22.163  27.180  40.788  1.00 23.29           C  
-ATOM    446  CG  LEU A  59      21.903  28.648  41.152  1.00 27.13           C  
-ATOM    447  CD1 LEU A  59      20.427  28.914  41.290  1.00 29.58           C  
-ATOM    448  CD2 LEU A  59      22.650  29.002  42.422  1.00 26.14           C  
-ATOM    449  N   ALA A  60      22.006  24.371  39.319  1.00 20.46           N  
-ATOM    450  CA  ALA A  60      22.589  23.396  38.409  1.00 23.31           C  
-ATOM    451  C   ALA A  60      21.581  23.052  37.314  1.00 24.62           C  
-ATOM    452  O   ALA A  60      21.940  22.936  36.141  1.00 24.27           O  
-ATOM    453  CB  ALA A  60      22.984  22.138  39.173  1.00 22.40           C  
-ATOM    454  N   ASP A  61      20.319  22.897  37.706  1.00 25.39           N  
-ATOM    455  CA  ASP A  61      19.253  22.568  36.761  1.00 28.15           C  
-ATOM    456  C   ASP A  61      19.020  23.743  35.814  1.00 27.81           C  
-ATOM    457  O   ASP A  61      18.792  23.551  34.623  1.00 27.24           O  
-ATOM    458  CB  ASP A  61      17.959  22.241  37.512  1.00 30.58           C  
-ATOM    459  CG  ASP A  61      16.822  21.872  36.578  1.00 36.68           C  
-ATOM    460  OD1 ASP A  61      16.937  20.847  35.871  1.00 38.02           O  
-ATOM    461  OD2 ASP A  61      15.813  22.609  36.544  1.00 39.03           O  
-ATOM    462  N   ASP A  62      19.077  24.956  36.354  1.00 26.75           N  
-ATOM    463  CA  ASP A  62      18.901  26.165  35.554  1.00 26.98           C  
-ATOM    464  C   ASP A  62      19.916  26.193  34.414  1.00 25.68           C  
-ATOM    465  O   ASP A  62      19.573  26.461  33.266  1.00 26.32           O  
-ATOM    466  CB  ASP A  62      19.132  27.421  36.399  1.00 25.79           C  
-ATOM    467  CG  ASP A  62      17.921  27.830  37.212  1.00 28.77           C  
-ATOM    468  OD1 ASP A  62      16.852  27.195  37.096  1.00 26.33           O  
-ATOM    469  OD2 ASP A  62      18.052  28.813  37.975  1.00 26.97           O  
-ATOM    470  N   TRP A  63      21.176  25.935  34.746  1.00 24.42           N  
-ATOM    471  CA  TRP A  63      22.239  25.963  33.750  1.00 24.09           C  
-ATOM    472  C   TRP A  63      22.037  24.873  32.699  1.00 25.24           C  
-ATOM    473  O   TRP A  63      22.150  25.131  31.500  1.00 23.05           O  
-ATOM    474  CB  TRP A  63      23.602  25.818  34.439  1.00 23.79           C  
-ATOM    475  CG  TRP A  63      24.779  26.088  33.543  1.00 25.03           C  
-ATOM    476  CD1 TRP A  63      24.852  27.015  32.541  1.00 26.29           C  
-ATOM    477  CD2 TRP A  63      26.057  25.445  33.586  1.00 25.61           C  
-ATOM    478  NE1 TRP A  63      26.098  26.986  31.956  1.00 25.97           N  
-ATOM    479  CE2 TRP A  63      26.856  26.032  32.579  1.00 26.96           C  
-ATOM    480  CE3 TRP A  63      26.606  24.430  34.380  1.00 28.16           C  
-ATOM    481  CZ2 TRP A  63      28.176  25.636  32.343  1.00 28.95           C  
-ATOM    482  CZ3 TRP A  63      27.920  24.035  34.147  1.00 29.74           C  
-ATOM    483  CH2 TRP A  63      28.689  24.639  33.135  1.00 29.92           C  
-ATOM    484  N   ASP A  64      21.720  23.662  33.146  1.00 23.87           N  
-ATOM    485  CA  ASP A  64      21.501  22.558  32.217  1.00 27.53           C  
-ATOM    486  C   ASP A  64      20.396  22.904  31.218  1.00 28.39           C  
-ATOM    487  O   ASP A  64      20.536  22.664  30.018  1.00 28.35           O  
-ATOM    488  CB  ASP A  64      21.125  21.286  32.977  1.00 28.30           C  
-ATOM    489  CG  ASP A  64      20.855  20.114  32.049  1.00 32.30           C  
-ATOM    490  OD1 ASP A  64      21.804  19.638  31.389  1.00 29.95           O  
-ATOM    491  OD2 ASP A  64      19.688  19.677  31.975  1.00 33.23           O  
-ATOM    492  N   LYS A  65      19.302  23.473  31.712  1.00 29.65           N  
-ATOM    493  CA  LYS A  65      18.188  23.839  30.846  1.00 33.21           C  
-ATOM    494  C   LYS A  65      18.582  24.934  29.863  1.00 33.96           C  
-ATOM    495  O   LYS A  65      18.171  24.918  28.700  1.00 32.47           O  
-ATOM    496  CB  LYS A  65      16.990  24.298  31.681  1.00 36.16           C  
-ATOM    497  CG  LYS A  65      16.357  23.185  32.504  1.00 40.37           C  
-ATOM    498  CD  LYS A  65      15.119  23.667  33.251  1.00 43.72           C  
-ATOM    499  CE  LYS A  65      14.420  22.508  33.953  1.00 46.02           C  
-ATOM    500  NZ  LYS A  65      13.257  22.967  34.765  1.00 48.79           N  
-ATOM    501  N   GLU A  66      19.382  25.884  30.337  1.00 33.48           N  
-ATOM    502  CA  GLU A  66      19.836  26.987  29.501  1.00 33.47           C  
-ATOM    503  C   GLU A  66      20.708  26.471  28.356  1.00 33.88           C  
-ATOM    504  O   GLU A  66      20.575  26.915  27.215  1.00 32.74           O  
-ATOM    505  CB  GLU A  66      20.617  27.994  30.350  1.00 34.75           C  
-ATOM    506  CG  GLU A  66      21.255  29.116  29.557  1.00 38.34           C  
-ATOM    507  CD  GLU A  66      21.985  30.110  30.442  1.00 39.99           C  
-ATOM    508  OE1 GLU A  66      22.580  29.680  31.455  1.00 39.87           O  
-ATOM    509  OE2 GLU A  66      21.977  31.316  30.117  1.00 38.58           O  
-ATOM    510  N   LEU A  67      21.589  25.525  28.670  1.00 32.23           N  
-ATOM    511  CA  LEU A  67      22.487  24.934  27.680  1.00 33.60           C  
-ATOM    512  C   LEU A  67      21.720  24.126  26.636  1.00 35.84           C  
-ATOM    513  O   LEU A  67      21.942  24.284  25.433  1.00 35.21           O  
-ATOM    514  CB  LEU A  67      23.515  24.039  28.380  1.00 30.43           C  
-ATOM    515  CG  LEU A  67      24.710  24.730  29.052  1.00 30.81           C  
-ATOM    516  CD1 LEU A  67      24.295  26.073  29.592  1.00 33.46           C  
-ATOM    517  CD2 LEU A  67      25.258  23.851  30.165  1.00 28.62           C  
-ATOM    518  N   ARG A  68      20.825  23.260  27.102  1.00 36.40           N  
-ATOM    519  CA  ARG A  68      20.012  22.432  26.215  1.00 39.67           C  
-ATOM    520  C   ARG A  68      19.197  23.311  25.271  1.00 40.79           C  
-ATOM    521  O   ARG A  68      18.995  22.976  24.103  1.00 40.47           O  
-ATOM    522  CB  ARG A  68      19.056  21.564  27.038  1.00 39.87           C  
-ATOM    523  CG  ARG A  68      19.686  20.346  27.688  1.00 43.60           C  
-ATOM    524  CD  ARG A  68      18.773  19.793  28.773  1.00 47.21           C  
-ATOM    525  NE  ARG A  68      18.816  18.336  28.875  1.00 51.86           N  
-ATOM    526  CZ  ARG A  68      19.909  17.620  29.125  1.00 54.27           C  
-ATOM    527  NH1 ARG A  68      21.080  18.218  29.302  1.00 54.24           N  
-ATOM    528  NH2 ARG A  68      19.829  16.298  29.201  1.00 54.48           N  
-ATOM    529  N   ASP A  69      18.738  24.442  25.794  1.00 41.68           N  
-ATOM    530  CA  ASP A  69      17.925  25.383  25.038  1.00 44.88           C  
-ATOM    531  C   ASP A  69      18.638  26.073  23.874  1.00 45.55           C  
-ATOM    532  O   ASP A  69      18.015  26.364  22.855  1.00 45.15           O  
-ATOM    533  CB  ASP A  69      17.359  26.442  25.990  1.00 47.07           C  
-ATOM    534  CG  ASP A  69      16.544  27.501  25.274  1.00 51.34           C  
-ATOM    535  OD1 ASP A  69      17.118  28.256  24.460  1.00 54.94           O  
-ATOM    536  OD2 ASP A  69      15.324  27.583  25.528  1.00 54.24           O  
-ATOM    537  N   ILE A  70      19.934  26.335  24.010  1.00 45.23           N  
-ATOM    538  CA  ILE A  70      20.657  27.022  22.941  1.00 46.00           C  
-ATOM    539  C   ILE A  70      21.657  26.169  22.169  1.00 47.11           C  
-ATOM    540  O   ILE A  70      22.326  26.664  21.262  1.00 47.01           O  
-ATOM    541  CB  ILE A  70      21.406  28.259  23.483  1.00 45.45           C  
-ATOM    542  CG1 ILE A  70      22.544  27.821  24.409  1.00 44.43           C  
-ATOM    543  CG2 ILE A  70      20.435  29.162  24.225  1.00 44.92           C  
-ATOM    544  CD1 ILE A  70      23.370  28.971  24.949  1.00 44.35           C  
-ATOM    545  N   THR A  71      21.763  24.894  22.519  1.00 48.54           N  
-ATOM    546  CA  THR A  71      22.700  24.017  21.835  1.00 51.25           C  
-ATOM    547  C   THR A  71      22.141  23.492  20.520  1.00 54.38           C  
-ATOM    548  O   THR A  71      21.077  22.872  20.488  1.00 54.45           O  
-ATOM    549  CB  THR A  71      23.096  22.823  22.719  1.00 50.48           C  
-ATOM    550  OG1 THR A  71      23.750  23.303  23.900  1.00 49.18           O  
-ATOM    551  CG2 THR A  71      24.045  21.897  21.968  1.00 50.25           C  
-ATOM    552  N   ARG A  72      22.870  23.752  19.438  1.00 57.83           N  
-ATOM    553  CA  ARG A  72      22.472  23.305  18.109  1.00 60.92           C  
-ATOM    554  C   ARG A  72      22.308  21.791  18.152  1.00 61.65           C  
-ATOM    555  O   ARG A  72      21.191  21.273  18.153  1.00 61.98           O  
-ATOM    556  CB  ARG A  72      23.551  23.668  17.088  1.00 63.14           C  
-ATOM    557  CG  ARG A  72      24.104  25.082  17.218  1.00 65.83           C  
-ATOM    558  CD  ARG A  72      23.058  26.144  16.925  1.00 67.54           C  
-ATOM    559  NE  ARG A  72      23.651  27.479  16.897  1.00 69.93           N  
-ATOM    560  CZ  ARG A  72      22.979  28.595  16.629  1.00 71.26           C  
-ATOM    561  NH1 ARG A  72      21.679  28.546  16.363  1.00 71.70           N  
-ATOM    562  NH2 ARG A  72      23.608  29.764  16.625  1.00 71.17           N  
-ATOM    563  N   ASP A  73      23.436  21.089  18.190  1.00 61.84           N  
-ATOM    564  CA  ASP A  73      23.444  19.633  18.251  1.00 62.43           C  
-ATOM    565  C   ASP A  73      24.107  19.207  19.556  1.00 61.78           C  
-ATOM    566  O   ASP A  73      25.327  19.280  19.692  1.00 62.01           O  
-ATOM    567  CB  ASP A  73      24.223  19.058  17.068  1.00 63.48           C  
-ATOM    568  CG  ASP A  73      24.326  17.547  17.118  1.00 64.43           C  
-ATOM    569  OD1 ASP A  73      25.063  16.975  16.287  1.00 65.96           O  
-ATOM    570  OD2 ASP A  73      23.669  16.929  17.983  1.00 64.89           O  
-ATOM    571  N   PRO A  74      23.310  18.751  20.532  1.00 61.57           N  
-ATOM    572  CA  PRO A  74      23.840  18.317  21.828  1.00 61.38           C  
-ATOM    573  C   PRO A  74      24.846  17.174  21.737  1.00 61.14           C  
-ATOM    574  O   PRO A  74      25.542  16.875  22.708  1.00 60.77           O  
-ATOM    575  CB  PRO A  74      22.582  17.930  22.602  1.00 61.66           C  
-ATOM    576  CG  PRO A  74      21.662  17.453  21.517  1.00 62.14           C  
-ATOM    577  CD  PRO A  74      21.861  18.501  20.450  1.00 61.97           C  
-ATOM    578  N   GLU A  75      24.924  16.541  20.571  1.00 60.92           N  
-ATOM    579  CA  GLU A  75      25.851  15.434  20.366  1.00 60.71           C  
-ATOM    580  C   GLU A  75      27.205  15.900  19.844  1.00 59.36           C  
-ATOM    581  O   GLU A  75      28.193  15.171  19.928  1.00 59.61           O  
-ATOM    582  CB  GLU A  75      25.247  14.410  19.402  1.00 62.63           C  
-ATOM    583  CG  GLU A  75      24.592  13.222  20.093  1.00 64.62           C  
-ATOM    584  CD  GLU A  75      23.615  13.639  21.176  1.00 66.51           C  
-ATOM    585  OE1 GLU A  75      22.642  14.358  20.858  1.00 67.85           O  
-ATOM    586  OE2 GLU A  75      23.820  13.247  22.345  1.00 66.65           O  
-ATOM    587  N   ASP A  76      27.246  17.116  19.308  1.00 57.46           N  
-ATOM    588  CA  ASP A  76      28.484  17.680  18.783  1.00 55.37           C  
-ATOM    589  C   ASP A  76      29.250  18.414  19.886  1.00 53.41           C  
-ATOM    590  O   ASP A  76      28.765  19.399  20.441  1.00 53.13           O  
-ATOM    591  CB  ASP A  76      28.176  18.642  17.634  1.00 56.14           C  
-ATOM    592  CG  ASP A  76      29.427  19.252  17.034  1.00 56.68           C  
-ATOM    593  OD1 ASP A  76      29.298  20.069  16.099  1.00 57.35           O  
-ATOM    594  OD2 ASP A  76      30.539  18.915  17.496  1.00 57.94           O  
-ATOM    595  N   PRO A  77      30.462  17.939  20.212  1.00 51.75           N  
-ATOM    596  CA  PRO A  77      31.314  18.532  21.249  1.00 50.20           C  
-ATOM    597  C   PRO A  77      31.575  20.024  21.059  1.00 49.24           C  
-ATOM    598  O   PRO A  77      31.579  20.788  22.024  1.00 48.33           O  
-ATOM    599  CB  PRO A  77      32.597  17.710  21.148  1.00 50.81           C  
-ATOM    600  CG  PRO A  77      32.096  16.370  20.713  1.00 51.74           C  
-ATOM    601  CD  PRO A  77      31.097  16.737  19.644  1.00 51.31           C  
-ATOM    602  N   LEU A  78      31.798  20.433  19.814  1.00 47.87           N  
-ATOM    603  CA  LEU A  78      32.073  21.832  19.514  1.00 47.01           C  
-ATOM    604  C   LEU A  78      30.850  22.720  19.708  1.00 44.89           C  
-ATOM    605  O   LEU A  78      30.984  23.901  20.023  1.00 42.47           O  
-ATOM    606  CB  LEU A  78      32.606  21.979  18.084  1.00 48.47           C  
-ATOM    607  CG  LEU A  78      33.969  21.344  17.772  1.00 50.05           C  
-ATOM    608  CD1 LEU A  78      35.028  21.893  18.718  1.00 50.60           C  
-ATOM    609  CD2 LEU A  78      33.877  19.833  17.907  1.00 52.20           C  
-ATOM    610  N   GLU A  79      29.660  22.156  19.518  1.00 43.22           N  
-ATOM    611  CA  GLU A  79      28.434  22.923  19.702  1.00 42.66           C  
-ATOM    612  C   GLU A  79      28.106  23.034  21.188  1.00 40.64           C  
-ATOM    613  O   GLU A  79      27.511  24.018  21.630  1.00 38.97           O  
-ATOM    614  CB  GLU A  79      27.270  22.281  18.942  1.00 45.54           C  
-ATOM    615  CG  GLU A  79      27.346  22.483  17.433  1.00 50.43           C  
-ATOM    616  CD  GLU A  79      27.318  23.957  17.031  1.00 52.81           C  
-ATOM    617  OE1 GLU A  79      27.477  24.251  15.826  1.00 55.02           O  
-ATOM    618  OE2 GLU A  79      27.135  24.822  17.913  1.00 53.81           O  
-ATOM    619  N   ARG A  80      28.485  22.019  21.958  1.00 38.41           N  
-ATOM    620  CA  ARG A  80      28.257  22.058  23.396  1.00 38.11           C  
-ATOM    621  C   ARG A  80      29.188  23.137  23.942  1.00 35.77           C  
-ATOM    622  O   ARG A  80      28.789  23.965  24.761  1.00 35.19           O  
-ATOM    623  CB  ARG A  80      28.612  20.725  24.054  1.00 39.15           C  
-ATOM    624  CG  ARG A  80      27.738  19.545  23.667  1.00 42.61           C  
-ATOM    625  CD  ARG A  80      28.164  18.323  24.467  1.00 45.28           C  
-ATOM    626  NE  ARG A  80      28.251  17.130  23.632  1.00 50.33           N  
-ATOM    627  CZ  ARG A  80      29.201  16.209  23.749  1.00 50.70           C  
-ATOM    628  NH1 ARG A  80      30.148  16.341  24.669  1.00 50.86           N  
-ATOM    629  NH2 ARG A  80      29.209  15.159  22.939  1.00 53.67           N  
-ATOM    630  N   LEU A  81      30.434  23.120  23.472  1.00 33.50           N  
-ATOM    631  CA  LEU A  81      31.426  24.097  23.908  1.00 31.75           C  
-ATOM    632  C   LEU A  81      30.945  25.512  23.610  1.00 30.75           C  
-ATOM    633  O   LEU A  81      31.081  26.412  24.438  1.00 27.95           O  
-ATOM    634  CB  LEU A  81      32.766  23.848  23.209  1.00 30.96           C  
-ATOM    635  CG  LEU A  81      33.897  24.822  23.560  1.00 30.64           C  
-ATOM    636  CD1 LEU A  81      34.181  24.765  25.059  1.00 30.73           C  
-ATOM    637  CD2 LEU A  81      35.145  24.465  22.766  1.00 31.45           C  
-ATOM    638  N   ARG A  82      30.373  25.707  22.427  1.00 30.43           N  
-ATOM    639  CA  ARG A  82      29.875  27.022  22.041  1.00 30.02           C  
-ATOM    640  C   ARG A  82      28.771  27.469  22.993  1.00 28.89           C  
-ATOM    641  O   ARG A  82      28.718  28.631  23.397  1.00 26.69           O  
-ATOM    642  CB  ARG A  82      29.342  26.980  20.605  1.00 33.67           C  
-ATOM    643  CG  ARG A  82      29.130  28.343  19.966  1.00 38.32           C  
-ATOM    644  CD  ARG A  82      28.838  28.197  18.475  1.00 43.87           C  
-ATOM    645  NE  ARG A  82      28.871  29.472  17.760  1.00 46.99           N  
-ATOM    646  CZ  ARG A  82      27.989  30.452  17.929  1.00 48.56           C  
-ATOM    647  NH1 ARG A  82      26.991  30.312  18.793  1.00 49.29           N  
-ATOM    648  NH2 ARG A  82      28.102  31.574  17.229  1.00 49.56           N  
-ATOM    649  N   ALA A  83      27.887  26.542  23.349  1.00 27.23           N  
-ATOM    650  CA  ALA A  83      26.787  26.850  24.257  1.00 27.08           C  
-ATOM    651  C   ALA A  83      27.340  27.242  25.628  1.00 26.22           C  
-ATOM    652  O   ALA A  83      26.842  28.162  26.272  1.00 25.75           O  
-ATOM    653  CB  ALA A  83      25.857  25.642  24.383  1.00 26.91           C  
-ATOM    654  N   VAL A  84      28.373  26.535  26.068  1.00 27.04           N  
-ATOM    655  CA  VAL A  84      28.994  26.828  27.356  1.00 26.28           C  
-ATOM    656  C   VAL A  84      29.556  28.247  27.332  1.00 26.58           C  
-ATOM    657  O   VAL A  84      29.306  29.036  28.243  1.00 25.11           O  
-ATOM    658  CB  VAL A  84      30.126  25.826  27.661  1.00 26.25           C  
-ATOM    659  CG1 VAL A  84      30.906  26.265  28.898  1.00 27.31           C  
-ATOM    660  CG2 VAL A  84      29.529  24.435  27.886  1.00 28.67           C  
-ATOM    661  N   VAL A  85      30.312  28.567  26.284  1.00 25.03           N  
-ATOM    662  CA  VAL A  85      30.893  29.898  26.146  1.00 25.41           C  
-ATOM    663  C   VAL A  85      29.806  30.963  26.205  1.00 25.00           C  
-ATOM    664  O   VAL A  85      29.916  31.934  26.954  1.00 24.69           O  
-ATOM    665  CB  VAL A  85      31.660  30.050  24.808  1.00 25.63           C  
-ATOM    666  CG1 VAL A  85      32.084  31.505  24.610  1.00 24.51           C  
-ATOM    667  CG2 VAL A  85      32.883  29.150  24.803  1.00 24.05           C  
-ATOM    668  N   VAL A  86      28.755  30.779  25.412  1.00 25.82           N  
-ATOM    669  CA  VAL A  86      27.656  31.736  25.374  1.00 24.82           C  
-ATOM    670  C   VAL A  86      26.970  31.936  26.728  1.00 24.90           C  
-ATOM    671  O   VAL A  86      26.695  33.072  27.117  1.00 24.51           O  
-ATOM    672  CB  VAL A  86      26.590  31.321  24.327  1.00 26.22           C  
-ATOM    673  CG1 VAL A  86      25.385  32.242  24.414  1.00 26.84           C  
-ATOM    674  CG2 VAL A  86      27.187  31.376  22.931  1.00 26.63           C  
-ATOM    675  N   THR A  87      26.695  30.850  27.446  1.00 23.84           N  
-ATOM    676  CA  THR A  87      26.031  30.972  28.744  1.00 25.81           C  
-ATOM    677  C   THR A  87      26.941  31.593  29.805  1.00 24.99           C  
-ATOM    678  O   THR A  87      26.474  32.295  30.698  1.00 25.54           O  
-ATOM    679  CB  THR A  87      25.525  29.606  29.259  1.00 27.27           C  
-ATOM    680  OG1 THR A  87      26.632  28.722  29.474  1.00 28.11           O  
-ATOM    681  CG2 THR A  87      24.566  28.984  28.246  1.00 28.73           C  
-ATOM    682  N   LEU A  88      28.239  31.344  29.698  1.00 24.38           N  
-ATOM    683  CA  LEU A  88      29.193  31.892  30.659  1.00 25.03           C  
-ATOM    684  C   LEU A  88      29.611  33.328  30.313  1.00 24.86           C  
-ATOM    685  O   LEU A  88      30.290  33.984  31.101  1.00 21.16           O  
-ATOM    686  CB  LEU A  88      30.429  30.987  30.733  1.00 24.33           C  
-ATOM    687  CG  LEU A  88      30.498  29.917  31.833  1.00 29.50           C  
-ATOM    688  CD1 LEU A  88      29.127  29.387  32.165  1.00 28.19           C  
-ATOM    689  CD2 LEU A  88      31.437  28.797  31.394  1.00 24.65           C  
-ATOM    690  N   ALA A  89      29.194  33.812  29.142  1.00 24.79           N  
-ATOM    691  CA  ALA A  89      29.536  35.164  28.692  1.00 25.23           C  
-ATOM    692  C   ALA A  89      28.781  36.244  29.457  1.00 24.83           C  
-ATOM    693  O   ALA A  89      29.147  37.420  29.414  1.00 25.54           O  
-ATOM    694  CB  ALA A  89      29.274  35.304  27.192  1.00 24.69           C  
-ATOM    695  N   GLU A  90      27.715  35.847  30.141  1.00 24.63           N  
-ATOM    696  CA  GLU A  90      26.944  36.783  30.943  1.00 25.98           C  
-ATOM    697  C   GLU A  90      27.543  36.756  32.349  1.00 25.64           C  
-ATOM    698  O   GLU A  90      27.816  35.681  32.890  1.00 24.74           O  
-ATOM    699  CB  GLU A  90      25.467  36.370  30.984  1.00 29.79           C  
-ATOM    700  CG  GLU A  90      24.630  37.163  31.979  1.00 36.68           C  
-ATOM    701  CD  GLU A  90      23.145  36.852  31.882  1.00 40.76           C  
-ATOM    702  OE1 GLU A  90      22.783  35.659  31.819  1.00 44.86           O  
-ATOM    703  OE2 GLU A  90      22.339  37.803  31.876  1.00 44.40           O  
-ATOM    704  N   ASN A  91      27.757  37.936  32.926  1.00 22.94           N  
-ATOM    705  CA  ASN A  91      28.337  38.057  34.259  1.00 22.85           C  
-ATOM    706  C   ASN A  91      27.579  37.205  35.277  1.00 21.57           C  
-ATOM    707  O   ASN A  91      26.353  37.251  35.341  1.00 20.41           O  
-ATOM    708  CB  ASN A  91      28.318  39.525  34.696  1.00 22.95           C  
-ATOM    709  CG  ASN A  91      28.965  39.744  36.048  1.00 22.75           C  
-ATOM    710  OD1 ASN A  91      30.093  39.317  36.283  1.00 24.09           O  
-ATOM    711  ND2 ASN A  91      28.256  40.428  36.943  1.00 23.13           N  
-ATOM    712  N   VAL A  92      28.311  36.420  36.063  1.00 20.82           N  
-ATOM    713  CA  VAL A  92      27.684  35.579  37.077  1.00 19.52           C  
-ATOM    714  C   VAL A  92      27.021  36.457  38.143  1.00 21.21           C  
-ATOM    715  O   VAL A  92      27.482  37.566  38.417  1.00 22.20           O  
-ATOM    716  CB  VAL A  92      28.726  34.652  37.761  1.00 21.11           C  
-ATOM    717  CG1 VAL A  92      29.785  35.479  38.484  1.00 18.13           C  
-ATOM    718  CG2 VAL A  92      28.030  33.708  38.730  1.00 20.04           C  
-ATOM    719  N   SER A  93      25.923  35.974  38.720  1.00 21.16           N  
-ATOM    720  CA  SER A  93      25.233  36.714  39.771  1.00 20.69           C  
-ATOM    721  C   SER A  93      25.972  36.415  41.072  1.00 19.52           C  
-ATOM    722  O   SER A  93      26.653  35.391  41.181  1.00 18.25           O  
-ATOM    723  CB  SER A  93      23.772  36.258  39.888  1.00 21.68           C  
-ATOM    724  OG  SER A  93      23.681  34.928  40.385  1.00 25.12           O  
-ATOM    725  N   ARG A  94      25.847  37.300  42.054  1.00 17.31           N  
-ATOM    726  CA  ARG A  94      26.510  37.096  43.338  1.00 19.36           C  
-ATOM    727  C   ARG A  94      26.107  35.788  44.030  1.00 18.36           C  
-ATOM    728  O   ARG A  94      26.962  35.052  44.521  1.00 16.74           O  
-ATOM    729  CB  ARG A  94      26.223  38.267  44.282  1.00 22.61           C  
-ATOM    730  CG  ARG A  94      27.020  39.525  43.994  1.00 26.53           C  
-ATOM    731  CD  ARG A  94      26.612  40.636  44.956  1.00 28.28           C  
-ATOM    732  NE  ARG A  94      26.675  40.198  46.349  1.00 28.26           N  
-ATOM    733  CZ  ARG A  94      27.803  39.962  47.010  1.00 28.24           C  
-ATOM    734  NH1 ARG A  94      28.977  40.125  46.408  1.00 27.63           N  
-ATOM    735  NH2 ARG A  94      27.757  39.555  48.272  1.00 26.48           N  
-ATOM    736  N   PRO A  95      24.797  35.488  44.088  1.00 19.04           N  
-ATOM    737  CA  PRO A  95      24.352  34.252  44.744  1.00 18.39           C  
-ATOM    738  C   PRO A  95      24.952  33.001  44.119  1.00 17.84           C  
-ATOM    739  O   PRO A  95      25.390  32.097  44.825  1.00 19.14           O  
-ATOM    740  CB  PRO A  95      22.837  34.297  44.579  1.00 19.60           C  
-ATOM    741  CG  PRO A  95      22.541  35.763  44.571  1.00 20.07           C  
-ATOM    742  CD  PRO A  95      23.641  36.303  43.675  1.00 19.39           C  
-ATOM    743  N   GLU A  96      24.965  32.941  42.793  1.00 18.57           N  
-ATOM    744  CA  GLU A  96      25.518  31.775  42.122  1.00 19.48           C  
-ATOM    745  C   GLU A  96      27.024  31.669  42.364  1.00 18.86           C  
-ATOM    746  O   GLU A  96      27.547  30.580  42.595  1.00 16.99           O  
-ATOM    747  CB  GLU A  96      25.211  31.824  40.619  1.00 21.21           C  
-ATOM    748  CG  GLU A  96      25.788  30.654  39.831  1.00 24.80           C  
-ATOM    749  CD  GLU A  96      24.998  30.345  38.564  1.00 30.27           C  
-ATOM    750  OE1 GLU A  96      24.552  31.295  37.882  1.00 29.99           O  
-ATOM    751  OE2 GLU A  96      24.833  29.148  38.242  1.00 31.87           O  
-ATOM    752  N   LEU A  97      27.727  32.795  42.322  1.00 17.59           N  
-ATOM    753  CA  LEU A  97      29.169  32.766  42.560  1.00 16.86           C  
-ATOM    754  C   LEU A  97      29.455  32.282  43.986  1.00 15.22           C  
-ATOM    755  O   LEU A  97      30.373  31.493  44.211  1.00 16.43           O  
-ATOM    756  CB  LEU A  97      29.783  34.159  42.333  1.00 18.88           C  
-ATOM    757  CG  LEU A  97      31.305  34.279  42.513  1.00 20.61           C  
-ATOM    758  CD1 LEU A  97      32.025  33.225  41.668  1.00 20.14           C  
-ATOM    759  CD2 LEU A  97      31.758  35.688  42.128  1.00 21.15           C  
-ATOM    760  N   LEU A  98      28.650  32.739  44.942  1.00 16.00           N  
-ATOM    761  CA  LEU A  98      28.822  32.354  46.341  1.00 17.32           C  
-ATOM    762  C   LEU A  98      28.540  30.862  46.570  1.00 18.48           C  
-ATOM    763  O   LEU A  98      29.259  30.186  47.313  1.00 16.48           O  
-ATOM    764  CB  LEU A  98      27.898  33.200  47.218  1.00 19.30           C  
-ATOM    765  CG  LEU A  98      28.472  34.297  48.120  1.00 26.62           C  
-ATOM    766  CD1 LEU A  98      29.823  34.788  47.632  1.00 25.30           C  
-ATOM    767  CD2 LEU A  98      27.453  35.428  48.202  1.00 22.06           C  
-ATOM    768  N   LEU A  99      27.492  30.346  45.942  1.00 16.15           N  
-ATOM    769  CA  LEU A  99      27.170  28.930  46.109  1.00 15.88           C  
-ATOM    770  C   LEU A  99      28.245  28.072  45.451  1.00 15.19           C  
-ATOM    771  O   LEU A  99      28.663  27.053  46.007  1.00 16.23           O  
-ATOM    772  CB  LEU A  99      25.774  28.636  45.531  1.00 15.14           C  
-ATOM    773  CG  LEU A  99      24.657  29.187  46.437  1.00 15.64           C  
-ATOM    774  CD1 LEU A  99      23.348  29.312  45.672  1.00 16.30           C  
-ATOM    775  CD2 LEU A  99      24.486  28.267  47.652  1.00 18.43           C  
-ATOM    776  N   LEU A 100      28.712  28.495  44.278  1.00 15.38           N  
-ATOM    777  CA  LEU A 100      29.763  27.769  43.561  1.00 17.85           C  
-ATOM    778  C   LEU A 100      31.012  27.641  44.445  1.00 17.38           C  
-ATOM    779  O   LEU A 100      31.587  26.559  44.585  1.00 14.70           O  
-ATOM    780  CB  LEU A 100      30.115  28.515  42.263  1.00 20.48           C  
-ATOM    781  CG  LEU A 100      29.847  27.915  40.872  1.00 26.26           C  
-ATOM    782  CD1 LEU A 100      28.807  26.814  40.904  1.00 24.01           C  
-ATOM    783  CD2 LEU A 100      29.436  29.042  39.930  1.00 21.31           C  
-ATOM    784  N   ILE A 101      31.429  28.751  45.042  1.00 15.84           N  
-ATOM    785  CA  ILE A 101      32.605  28.742  45.906  1.00 15.40           C  
-ATOM    786  C   ILE A 101      32.359  27.908  47.172  1.00 16.54           C  
-ATOM    787  O   ILE A 101      33.271  27.256  47.679  1.00 16.71           O  
-ATOM    788  CB  ILE A 101      32.996  30.180  46.322  1.00 16.38           C  
-ATOM    789  CG1 ILE A 101      33.437  30.982  45.083  1.00 15.83           C  
-ATOM    790  CG2 ILE A 101      34.122  30.130  47.353  1.00 15.37           C  
-ATOM    791  CD1 ILE A 101      33.586  32.494  45.327  1.00 16.79           C  
-ATOM    792  N   ASP A 102      31.127  27.909  47.671  1.00 16.52           N  
-ATOM    793  CA  ASP A 102      30.824  27.160  48.890  1.00 17.69           C  
-ATOM    794  C   ASP A 102      30.453  25.692  48.702  1.00 18.80           C  
-ATOM    795  O   ASP A 102      30.402  24.935  49.672  1.00 17.49           O  
-ATOM    796  CB  ASP A 102      29.700  27.840  49.669  1.00 19.66           C  
-ATOM    797  CG  ASP A 102      29.698  27.445  51.134  1.00 22.19           C  
-ATOM    798  OD1 ASP A 102      30.718  27.707  51.809  1.00 22.99           O  
-ATOM    799  OD2 ASP A 102      28.691  26.871  51.605  1.00 21.64           O  
-ATOM    800  N   ALA A 103      30.199  25.291  47.463  1.00 18.09           N  
-ATOM    801  CA  ALA A 103      29.803  23.917  47.173  1.00 17.86           C  
-ATOM    802  C   ALA A 103      30.594  22.829  47.905  1.00 20.33           C  
-ATOM    803  O   ALA A 103      29.998  21.900  48.449  1.00 19.68           O  
-ATOM    804  CB  ALA A 103      29.852  23.676  45.680  1.00 18.39           C  
-ATOM    805  N   PRO A 104      31.940  22.926  47.935  1.00 21.15           N  
-ATOM    806  CA  PRO A 104      32.762  21.912  48.616  1.00 21.63           C  
-ATOM    807  C   PRO A 104      32.537  21.772  50.122  1.00 22.43           C  
-ATOM    808  O   PRO A 104      33.133  20.894  50.757  1.00 24.35           O  
-ATOM    809  CB  PRO A 104      34.197  22.350  48.298  1.00 21.02           C  
-ATOM    810  CG  PRO A 104      34.061  23.090  46.999  1.00 21.45           C  
-ATOM    811  CD  PRO A 104      32.797  23.893  47.223  1.00 19.79           C  
-ATOM    812  N   SER A 105      31.692  22.623  50.701  1.00 21.35           N  
-ATOM    813  CA  SER A 105      31.426  22.544  52.137  1.00 21.49           C  
-ATOM    814  C   SER A 105      30.772  21.216  52.521  1.00 21.83           C  
-ATOM    815  O   SER A 105      30.790  20.818  53.686  1.00 20.10           O  
-ATOM    816  CB  SER A 105      30.543  23.712  52.602  1.00 22.62           C  
-ATOM    817  OG  SER A 105      29.316  23.767  51.892  1.00 21.68           O  
-ATOM    818  N   HIS A 106      30.187  20.533  51.544  1.00 21.19           N  
-ATOM    819  CA  HIS A 106      29.557  19.242  51.808  1.00 21.21           C  
-ATOM    820  C   HIS A 106      29.441  18.439  50.521  1.00 20.49           C  
-ATOM    821  O   HIS A 106      29.057  18.970  49.478  1.00 21.33           O  
-ATOM    822  CB  HIS A 106      28.165  19.423  52.415  1.00 21.11           C  
-ATOM    823  CG  HIS A 106      27.572  18.149  52.928  1.00 22.21           C  
-ATOM    824  ND1 HIS A 106      27.646  17.774  54.253  1.00 24.54           N  
-ATOM    825  CD2 HIS A 106      26.956  17.130  52.282  1.00 20.37           C  
-ATOM    826  CE1 HIS A 106      27.101  16.578  54.400  1.00 22.60           C  
-ATOM    827  NE2 HIS A 106      26.676  16.165  53.219  1.00 23.47           N  
-ATOM    828  N   PRO A 107      29.773  17.141  50.572  1.00 21.35           N  
-ATOM    829  CA  PRO A 107      29.685  16.317  49.363  1.00 21.24           C  
-ATOM    830  C   PRO A 107      28.341  16.373  48.633  1.00 19.26           C  
-ATOM    831  O   PRO A 107      28.299  16.235  47.408  1.00 18.82           O  
-ATOM    832  CB  PRO A 107      30.041  14.908  49.870  1.00 22.47           C  
-ATOM    833  CG  PRO A 107      29.714  14.956  51.324  1.00 25.21           C  
-ATOM    834  CD  PRO A 107      30.178  16.332  51.734  1.00 22.17           C  
-ATOM    835  N   ASP A 108      27.249  16.578  49.366  1.00 18.10           N  
-ATOM    836  CA  ASP A 108      25.925  16.652  48.733  1.00 19.39           C  
-ATOM    837  C   ASP A 108      25.812  17.841  47.780  1.00 19.30           C  
-ATOM    838  O   ASP A 108      25.202  17.736  46.718  1.00 17.92           O  
-ATOM    839  CB  ASP A 108      24.807  16.789  49.774  1.00 20.14           C  
-ATOM    840  CG  ASP A 108      24.563  15.514  50.556  1.00 23.98           C  
-ATOM    841  OD1 ASP A 108      25.150  14.471  50.204  1.00 24.37           O  
-ATOM    842  OD2 ASP A 108      23.775  15.567  51.525  1.00 21.89           O  
-ATOM    843  N   PHE A 109      26.380  18.978  48.171  1.00 18.87           N  
-ATOM    844  CA  PHE A 109      26.306  20.175  47.330  1.00 18.79           C  
-ATOM    845  C   PHE A 109      27.131  19.995  46.063  1.00 18.52           C  
-ATOM    846  O   PHE A 109      26.688  20.334  44.965  1.00 18.77           O  
-ATOM    847  CB  PHE A 109      26.790  21.409  48.103  1.00 18.39           C  
-ATOM    848  CG  PHE A 109      26.120  21.594  49.437  1.00 20.19           C  
-ATOM    849  CD1 PHE A 109      24.819  21.136  49.655  1.00 19.81           C  
-ATOM    850  CD2 PHE A 109      26.782  22.250  50.477  1.00 20.65           C  
-ATOM    851  CE1 PHE A 109      24.188  21.327  50.888  1.00 19.84           C  
-ATOM    852  CE2 PHE A 109      26.158  22.448  51.715  1.00 22.11           C  
-ATOM    853  CZ  PHE A 109      24.857  21.984  51.919  1.00 20.09           C  
-ATOM    854  N   LEU A 110      28.332  19.453  46.219  1.00 19.69           N  
-ATOM    855  CA  LEU A 110      29.208  19.198  45.080  1.00 21.52           C  
-ATOM    856  C   LEU A 110      28.501  18.243  44.112  1.00 21.70           C  
-ATOM    857  O   LEU A 110      28.525  18.432  42.894  1.00 19.95           O  
-ATOM    858  CB  LEU A 110      30.508  18.563  45.576  1.00 25.39           C  
-ATOM    859  CG  LEU A 110      31.862  19.254  45.367  1.00 29.92           C  
-ATOM    860  CD1 LEU A 110      31.737  20.761  45.389  1.00 29.44           C  
-ATOM    861  CD2 LEU A 110      32.812  18.766  46.456  1.00 29.17           C  
-ATOM    862  N   ASN A 111      27.861  17.219  44.663  1.00 22.44           N  
-ATOM    863  CA  ASN A 111      27.170  16.235  43.837  1.00 22.96           C  
-ATOM    864  C   ASN A 111      26.054  16.860  43.017  1.00 23.23           C  
-ATOM    865  O   ASN A 111      25.786  16.429  41.897  1.00 25.38           O  
-ATOM    866  CB  ASN A 111      26.606  15.108  44.705  1.00 24.05           C  
-ATOM    867  CG  ASN A 111      25.950  14.016  43.879  1.00 28.10           C  
-ATOM    868  OD1 ASN A 111      26.570  13.446  42.985  1.00 29.80           O  
-ATOM    869  ND2 ASN A 111      24.690  13.723  44.174  1.00 30.22           N  
-ATOM    870  N   ALA A 112      25.406  17.882  43.570  1.00 23.12           N  
-ATOM    871  CA  ALA A 112      24.325  18.554  42.865  1.00 23.55           C  
-ATOM    872  C   ALA A 112      24.806  19.119  41.530  1.00 23.45           C  
-ATOM    873  O   ALA A 112      24.046  19.160  40.561  1.00 23.78           O  
-ATOM    874  CB  ALA A 112      23.750  19.668  43.725  1.00 25.32           C  
-ATOM    875  N   TRP A 113      26.065  19.551  41.480  1.00 22.89           N  
-ATOM    876  CA  TRP A 113      26.640  20.123  40.256  1.00 23.76           C  
-ATOM    877  C   TRP A 113      27.359  19.099  39.375  1.00 24.98           C  
-ATOM    878  O   TRP A 113      27.725  19.397  38.236  1.00 25.19           O  
-ATOM    879  CB  TRP A 113      27.647  21.225  40.603  1.00 23.44           C  
-ATOM    880  CG  TRP A 113      27.053  22.430  41.249  1.00 22.52           C  
-ATOM    881  CD1 TRP A 113      26.887  22.654  42.586  1.00 23.23           C  
-ATOM    882  CD2 TRP A 113      26.520  23.578  40.578  1.00 22.27           C  
-ATOM    883  NE1 TRP A 113      26.282  23.877  42.788  1.00 22.30           N  
-ATOM    884  CE2 TRP A 113      26.046  24.461  41.572  1.00 21.71           C  
-ATOM    885  CE3 TRP A 113      26.397  23.943  39.231  1.00 23.43           C  
-ATOM    886  CZ2 TRP A 113      25.456  25.690  41.263  1.00 21.81           C  
-ATOM    887  CZ3 TRP A 113      25.809  25.167  38.923  1.00 22.49           C  
-ATOM    888  CH2 TRP A 113      25.347  26.024  39.938  1.00 22.07           C  
-ATOM    889  N   ARG A 114      27.563  17.899  39.904  1.00 27.10           N  
-ATOM    890  CA  ARG A 114      28.289  16.862  39.182  1.00 28.72           C  
-ATOM    891  C   ARG A 114      27.794  16.529  37.778  1.00 28.37           C  
-ATOM    892  O   ARG A 114      28.568  16.567  36.822  1.00 27.30           O  
-ATOM    893  CB  ARG A 114      28.338  15.575  40.013  1.00 32.03           C  
-ATOM    894  CG  ARG A 114      29.282  14.532  39.433  1.00 37.99           C  
-ATOM    895  CD  ARG A 114      29.362  13.272  40.282  1.00 43.45           C  
-ATOM    896  NE  ARG A 114      30.430  12.398  39.800  1.00 50.40           N  
-ATOM    897  CZ  ARG A 114      30.684  11.181  40.273  1.00 52.85           C  
-ATOM    898  NH1 ARG A 114      29.944  10.673  41.252  1.00 53.45           N  
-ATOM    899  NH2 ARG A 114      31.683  10.471  39.765  1.00 54.33           N  
-ATOM    900  N   THR A 115      26.515  16.202  37.646  1.00 28.45           N  
-ATOM    901  CA  THR A 115      25.978  15.828  36.344  1.00 30.65           C  
-ATOM    902  C   THR A 115      26.105  16.900  35.267  1.00 30.48           C  
-ATOM    903  O   THR A 115      26.553  16.611  34.158  1.00 30.70           O  
-ATOM    904  CB  THR A 115      24.505  15.390  36.456  1.00 31.86           C  
-ATOM    905  OG1 THR A 115      24.411  14.271  37.348  1.00 34.13           O  
-ATOM    906  CG2 THR A 115      23.968  14.976  35.092  1.00 33.65           C  
-ATOM    907  N   VAL A 116      25.722  18.134  35.575  1.00 29.97           N  
-ATOM    908  CA  VAL A 116      25.821  19.187  34.573  1.00 29.54           C  
-ATOM    909  C   VAL A 116      27.284  19.448  34.199  1.00 30.24           C  
-ATOM    910  O   VAL A 116      27.589  19.742  33.044  1.00 30.26           O  
-ATOM    911  CB  VAL A 116      25.150  20.499  35.053  1.00 29.70           C  
-ATOM    912  CG1 VAL A 116      25.943  21.117  36.194  1.00 27.25           C  
-ATOM    913  CG2 VAL A 116      25.017  21.462  33.885  1.00 28.33           C  
-ATOM    914  N   ASN A 117      28.185  19.333  35.173  1.00 29.73           N  
-ATOM    915  CA  ASN A 117      29.613  19.532  34.918  1.00 30.16           C  
-ATOM    916  C   ASN A 117      30.127  18.428  33.999  1.00 31.55           C  
-ATOM    917  O   ASN A 117      30.835  18.682  33.025  1.00 30.76           O  
-ATOM    918  CB  ASN A 117      30.418  19.479  36.221  1.00 30.49           C  
-ATOM    919  CG  ASN A 117      30.588  20.841  36.867  1.00 33.17           C  
-ATOM    920  OD1 ASN A 117      29.663  21.378  37.479  1.00 32.53           O  
-ATOM    921  ND2 ASN A 117      31.782  21.409  36.731  1.00 30.94           N  
-ATOM    922  N   HIS A 118      29.773  17.192  34.328  1.00 31.71           N  
-ATOM    923  CA  HIS A 118      30.207  16.046  33.544  1.00 32.85           C  
-ATOM    924  C   HIS A 118      29.720  16.090  32.096  1.00 31.73           C  
-ATOM    925  O   HIS A 118      30.456  15.734  31.178  1.00 32.09           O  
-ATOM    926  CB  HIS A 118      29.720  14.753  34.203  1.00 35.66           C  
-ATOM    927  CG  HIS A 118      30.052  13.518  33.425  1.00 40.35           C  
-ATOM    928  ND1 HIS A 118      31.348  13.105  33.201  1.00 41.95           N  
-ATOM    929  CD2 HIS A 118      29.256  12.617  32.801  1.00 41.84           C  
-ATOM    930  CE1 HIS A 118      31.336  12.003  32.472  1.00 44.19           C  
-ATOM    931  NE2 HIS A 118      30.079  11.686  32.216  1.00 43.83           N  
-ATOM    932  N   GLN A 119      28.487  16.537  31.890  1.00 30.97           N  
-ATOM    933  CA  GLN A 119      27.914  16.581  30.549  1.00 33.00           C  
-ATOM    934  C   GLN A 119      28.293  17.763  29.658  1.00 32.72           C  
-ATOM    935  O   GLN A 119      28.243  17.651  28.432  1.00 31.07           O  
-ATOM    936  CB  GLN A 119      26.387  16.500  30.637  1.00 35.48           C  
-ATOM    937  CG  GLN A 119      25.873  15.183  31.200  1.00 40.87           C  
-ATOM    938  CD  GLN A 119      24.357  15.109  31.248  1.00 43.97           C  
-ATOM    939  OE1 GLN A 119      23.787  14.087  31.635  1.00 47.69           O  
-ATOM    940  NE2 GLN A 119      23.694  16.192  30.857  1.00 45.71           N  
-ATOM    941  N   TRP A 120      28.681  18.887  30.252  1.00 31.05           N  
-ATOM    942  CA  TRP A 120      29.007  20.058  29.444  1.00 30.81           C  
-ATOM    943  C   TRP A 120      30.440  20.581  29.496  1.00 30.68           C  
-ATOM    944  O   TRP A 120      30.885  21.249  28.564  1.00 30.18           O  
-ATOM    945  CB  TRP A 120      28.041  21.192  29.780  1.00 31.00           C  
-ATOM    946  CG  TRP A 120      26.612  20.833  29.544  1.00 32.17           C  
-ATOM    947  CD1 TRP A 120      25.739  20.284  30.443  1.00 32.08           C  
-ATOM    948  CD2 TRP A 120      25.890  20.977  28.317  1.00 32.25           C  
-ATOM    949  NE1 TRP A 120      24.514  20.079  29.849  1.00 33.67           N  
-ATOM    950  CE2 TRP A 120      24.580  20.495  28.544  1.00 33.82           C  
-ATOM    951  CE3 TRP A 120      26.223  21.466  27.046  1.00 32.82           C  
-ATOM    952  CZ2 TRP A 120      23.599  20.490  27.544  1.00 33.18           C  
-ATOM    953  CZ3 TRP A 120      25.247  21.462  26.051  1.00 33.70           C  
-ATOM    954  CH2 TRP A 120      23.950  20.976  26.309  1.00 32.85           C  
-ATOM    955  N   ILE A 121      31.162  20.299  30.574  1.00 29.25           N  
-ATOM    956  CA  ILE A 121      32.541  20.761  30.672  1.00 29.26           C  
-ATOM    957  C   ILE A 121      33.446  19.735  29.995  1.00 29.98           C  
-ATOM    958  O   ILE A 121      33.345  18.542  30.266  1.00 27.82           O  
-ATOM    959  CB  ILE A 121      32.971  20.934  32.146  1.00 29.99           C  
-ATOM    960  CG1 ILE A 121      32.055  21.949  32.834  1.00 28.83           C  
-ATOM    961  CG2 ILE A 121      34.425  21.393  32.222  1.00 29.23           C  
-ATOM    962  CD1 ILE A 121      32.011  23.308  32.146  1.00 30.16           C  
-ATOM    963  N   PRO A 122      34.343  20.188  29.101  1.00 32.23           N  
-ATOM    964  CA  PRO A 122      35.253  19.279  28.395  1.00 33.17           C  
-ATOM    965  C   PRO A 122      36.181  18.500  29.316  1.00 34.16           C  
-ATOM    966  O   PRO A 122      36.535  18.972  30.397  1.00 33.85           O  
-ATOM    967  CB  PRO A 122      36.009  20.212  27.449  1.00 34.47           C  
-ATOM    968  CG  PRO A 122      36.001  21.523  28.185  1.00 33.86           C  
-ATOM    969  CD  PRO A 122      34.589  21.586  28.705  1.00 32.81           C  
-ATOM    970  N   ASP A 123      36.569  17.303  28.884  1.00 34.73           N  
-ATOM    971  CA  ASP A 123      37.456  16.461  29.676  1.00 36.87           C  
-ATOM    972  C   ASP A 123      38.904  16.901  29.508  1.00 36.03           C  
-ATOM    973  O   ASP A 123      39.222  17.713  28.637  1.00 36.16           O  
-ATOM    974  CB  ASP A 123      37.325  14.992  29.263  1.00 39.34           C  
-ATOM    975  CG  ASP A 123      37.922  14.717  27.898  1.00 41.31           C  
-ATOM    976  OD1 ASP A 123      37.308  15.105  26.885  1.00 45.07           O  
-ATOM    977  OD2 ASP A 123      39.017  14.123  27.838  1.00 43.14           O  
-ATOM    978  N   THR A 124      39.777  16.349  30.343  1.00 34.95           N  
-ATOM    979  CA  THR A 124      41.193  16.688  30.302  1.00 35.63           C  
-ATOM    980  C   THR A 124      42.060  15.441  30.161  1.00 36.09           C  
-ATOM    981  O   THR A 124      43.211  15.428  30.593  1.00 35.75           O  
-ATOM    982  CB  THR A 124      41.609  17.432  31.581  1.00 33.85           C  
-ATOM    983  OG1 THR A 124      41.389  16.585  32.717  1.00 33.24           O  
-ATOM    984  CG2 THR A 124      40.786  18.704  31.744  1.00 33.50           C  
-ATOM    985  N   ASP A 125      41.509  14.399  29.549  1.00 37.99           N  
-ATOM    986  CA  ASP A 125      42.244  13.152  29.373  1.00 40.28           C  
-ATOM    987  C   ASP A 125      43.563  13.349  28.633  1.00 40.34           C  
-ATOM    988  O   ASP A 125      43.590  13.851  27.510  1.00 40.58           O  
-ATOM    989  CB  ASP A 125      41.386  12.127  28.626  1.00 42.82           C  
-ATOM    990  CG  ASP A 125      40.085  11.827  29.341  1.00 44.90           C  
-ATOM    991  OD1 ASP A 125      40.073  11.859  30.590  1.00 46.62           O  
-ATOM    992  OD2 ASP A 125      39.078  11.547  28.656  1.00 46.70           O  
-ATOM    993  N   ASP A 126      44.655  12.946  29.277  1.00 41.03           N  
-ATOM    994  CA  ASP A 126      45.989  13.063  28.699  1.00 41.09           C  
-ATOM    995  C   ASP A 126      46.246  14.501  28.255  1.00 40.46           C  
-ATOM    996  O   ASP A 126      46.945  14.755  27.271  1.00 40.65           O  
-ATOM    997  CB  ASP A 126      46.128  12.099  27.515  1.00 42.55           C  
-ATOM    998  CG  ASP A 126      47.566  11.926  27.068  1.00 45.05           C  
-ATOM    999  OD1 ASP A 126      48.447  11.761  27.940  1.00 45.80           O  
-ATOM   1000  OD2 ASP A 126      47.814  11.944  25.845  1.00 48.01           O  
-ATOM   1001  N   LEU A 127      45.673  15.434  29.007  1.00 38.51           N  
-ATOM   1002  CA  LEU A 127      45.798  16.861  28.737  1.00 37.48           C  
-ATOM   1003  C   LEU A 127      47.248  17.282  28.499  1.00 36.97           C  
-ATOM   1004  O   LEU A 127      47.543  18.014  27.552  1.00 35.26           O  
-ATOM   1005  CB  LEU A 127      45.206  17.649  29.917  1.00 38.75           C  
-ATOM   1006  CG  LEU A 127      45.037  19.172  29.879  1.00 38.48           C  
-ATOM   1007  CD1 LEU A 127      46.392  19.851  29.886  1.00 42.09           C  
-ATOM   1008  CD2 LEU A 127      44.227  19.567  28.660  1.00 39.20           C  
-ATOM   1009  N   GLU A 128      48.151  16.809  29.353  1.00 36.23           N  
-ATOM   1010  CA  GLU A 128      49.559  17.167  29.242  1.00 37.74           C  
-ATOM   1011  C   GLU A 128      50.231  16.730  27.942  1.00 38.62           C  
-ATOM   1012  O   GLU A 128      51.272  17.270  27.572  1.00 38.97           O  
-ATOM   1013  CB  GLU A 128      50.341  16.607  30.432  1.00 38.19           C  
-ATOM   1014  CG  GLU A 128      49.782  17.018  31.786  1.00 39.53           C  
-ATOM   1015  CD  GLU A 128      48.869  15.965  32.389  1.00 40.39           C  
-ATOM   1016  OE1 GLU A 128      48.005  15.425  31.664  1.00 40.01           O  
-ATOM   1017  OE2 GLU A 128      49.015  15.683  33.597  1.00 39.51           O  
-ATOM   1018  N   ASN A 129      49.640  15.767  27.242  1.00 39.56           N  
-ATOM   1019  CA  ASN A 129      50.228  15.288  25.996  1.00 41.31           C  
-ATOM   1020  C   ASN A 129      49.313  15.454  24.787  1.00 41.61           C  
-ATOM   1021  O   ASN A 129      49.589  14.908  23.719  1.00 42.26           O  
-ATOM   1022  CB  ASN A 129      50.617  13.815  26.139  1.00 42.55           C  
-ATOM   1023  CG  ASN A 129      51.459  13.555  27.370  1.00 43.20           C  
-ATOM   1024  OD1 ASN A 129      51.086  12.762  28.232  1.00 45.67           O  
-ATOM   1025  ND2 ASN A 129      52.601  14.226  27.462  1.00 43.89           N  
-ATOM   1026  N   ASP A 130      48.231  16.209  24.951  1.00 40.14           N  
-ATOM   1027  CA  ASP A 130      47.284  16.426  23.863  1.00 39.92           C  
-ATOM   1028  C   ASP A 130      47.052  17.919  23.646  1.00 40.11           C  
-ATOM   1029  O   ASP A 130      46.270  18.548  24.360  1.00 39.11           O  
-ATOM   1030  CB  ASP A 130      45.956  15.740  24.183  1.00 41.34           C  
-ATOM   1031  CG  ASP A 130      45.031  15.666  22.982  1.00 42.73           C  
-ATOM   1032  OD1 ASP A 130      44.885  16.683  22.269  1.00 43.69           O  
-ATOM   1033  OD2 ASP A 130      44.441  14.589  22.758  1.00 44.12           O  
-ATOM   1034  N   ALA A 131      47.731  18.479  22.650  1.00 39.31           N  
-ATOM   1035  CA  ALA A 131      47.612  19.898  22.338  1.00 39.55           C  
-ATOM   1036  C   ALA A 131      46.183  20.319  22.006  1.00 39.48           C  
-ATOM   1037  O   ALA A 131      45.769  21.429  22.339  1.00 39.81           O  
-ATOM   1038  CB  ALA A 131      48.545  20.258  21.182  1.00 39.18           C  
-ATOM   1039  N   HIS A 132      45.427  19.445  21.348  1.00 39.19           N  
-ATOM   1040  CA  HIS A 132      44.053  19.787  21.000  1.00 38.57           C  
-ATOM   1041  C   HIS A 132      43.187  19.827  22.249  1.00 37.93           C  
-ATOM   1042  O   HIS A 132      42.269  20.642  22.352  1.00 37.42           O  
-ATOM   1043  CB  HIS A 132      43.475  18.788  19.994  1.00 38.74           C  
-ATOM   1044  CG  HIS A 132      42.050  19.067  19.628  1.00 38.87           C  
-ATOM   1045  ND1 HIS A 132      40.984  18.539  20.326  1.00 39.61           N  
-ATOM   1046  CD2 HIS A 132      41.514  19.860  18.670  1.00 38.99           C  
-ATOM   1047  CE1 HIS A 132      39.855  18.996  19.814  1.00 39.52           C  
-ATOM   1048  NE2 HIS A 132      40.149  19.800  18.809  1.00 38.45           N  
-ATOM   1049  N   LYS A 133      43.485  18.944  23.197  1.00 37.11           N  
-ATOM   1050  CA  LYS A 133      42.743  18.891  24.449  1.00 35.78           C  
-ATOM   1051  C   LYS A 133      42.952  20.228  25.168  1.00 34.13           C  
-ATOM   1052  O   LYS A 133      42.003  20.826  25.685  1.00 32.39           O  
-ATOM   1053  CB  LYS A 133      43.262  17.740  25.315  1.00 37.08           C  
-ATOM   1054  CG  LYS A 133      42.363  17.374  26.491  1.00 41.19           C  
-ATOM   1055  CD  LYS A 133      41.090  16.671  26.031  1.00 42.04           C  
-ATOM   1056  CE  LYS A 133      41.404  15.330  25.376  1.00 42.31           C  
-ATOM   1057  NZ  LYS A 133      40.172  14.602  24.962  1.00 42.19           N  
-ATOM   1058  N   ARG A 134      44.200  20.692  25.181  1.00 31.51           N  
-ATOM   1059  CA  ARG A 134      44.554  21.959  25.820  1.00 31.34           C  
-ATOM   1060  C   ARG A 134      43.930  23.161  25.110  1.00 29.92           C  
-ATOM   1061  O   ARG A 134      43.540  24.136  25.754  1.00 27.97           O  
-ATOM   1062  CB  ARG A 134      46.077  22.138  25.854  1.00 30.26           C  
-ATOM   1063  CG  ARG A 134      46.821  21.118  26.708  1.00 32.77           C  
-ATOM   1064  CD  ARG A 134      48.236  21.592  27.028  1.00 33.10           C  
-ATOM   1065  NE  ARG A 134      49.094  21.662  25.846  1.00 35.26           N  
-ATOM   1066  CZ  ARG A 134      49.603  20.601  25.226  1.00 36.59           C  
-ATOM   1067  NH1 ARG A 134      49.345  19.379  25.672  1.00 35.10           N  
-ATOM   1068  NH2 ARG A 134      50.371  20.760  24.155  1.00 36.55           N  
-ATOM   1069  N   ALA A 135      43.847  23.095  23.783  1.00 28.49           N  
-ATOM   1070  CA  ALA A 135      43.264  24.186  23.004  1.00 27.75           C  
-ATOM   1071  C   ALA A 135      41.791  24.333  23.364  1.00 28.01           C  
-ATOM   1072  O   ALA A 135      41.270  25.444  23.472  1.00 28.19           O  
-ATOM   1073  CB  ALA A 135      43.417  23.906  21.509  1.00 30.47           C  
-ATOM   1074  N   VAL A 136      41.124  23.201  23.556  1.00 25.86           N  
-ATOM   1075  CA  VAL A 136      39.714  23.198  23.918  1.00 26.47           C  
-ATOM   1076  C   VAL A 136      39.517  23.711  25.345  1.00 25.90           C  
-ATOM   1077  O   VAL A 136      38.629  24.520  25.601  1.00 25.75           O  
-ATOM   1078  CB  VAL A 136      39.113  21.777  23.809  1.00 26.44           C  
-ATOM   1079  CG1 VAL A 136      37.783  21.703  24.558  1.00 25.58           C  
-ATOM   1080  CG2 VAL A 136      38.907  21.419  22.340  1.00 28.15           C  
-ATOM   1081  N   TYR A 137      40.345  23.241  26.272  1.00 25.79           N  
-ATOM   1082  CA  TYR A 137      40.204  23.671  27.655  1.00 26.13           C  
-ATOM   1083  C   TYR A 137      40.550  25.147  27.803  1.00 25.72           C  
-ATOM   1084  O   TYR A 137      40.048  25.821  28.701  1.00 24.77           O  
-ATOM   1085  CB  TYR A 137      41.079  22.829  28.586  1.00 26.43           C  
-ATOM   1086  CG  TYR A 137      40.398  22.576  29.912  1.00 26.13           C  
-ATOM   1087  CD1 TYR A 137      39.326  21.691  30.001  1.00 25.91           C  
-ATOM   1088  CD2 TYR A 137      40.759  23.291  31.054  1.00 25.87           C  
-ATOM   1089  CE1 TYR A 137      38.624  21.528  31.191  1.00 27.22           C  
-ATOM   1090  CE2 TYR A 137      40.066  23.138  32.249  1.00 25.35           C  
-ATOM   1091  CZ  TYR A 137      38.996  22.257  32.311  1.00 26.29           C  
-ATOM   1092  OH  TYR A 137      38.280  22.121  33.479  1.00 25.94           O  
-ATOM   1093  N   LEU A 138      41.407  25.646  26.918  1.00 25.34           N  
-ATOM   1094  CA  LEU A 138      41.794  27.053  26.948  1.00 24.18           C  
-ATOM   1095  C   LEU A 138      40.548  27.903  26.716  1.00 22.53           C  
-ATOM   1096  O   LEU A 138      40.391  28.975  27.302  1.00 22.80           O  
-ATOM   1097  CB  LEU A 138      42.841  27.334  25.862  1.00 25.26           C  
-ATOM   1098  CG  LEU A 138      43.383  28.761  25.777  1.00 26.49           C  
-ATOM   1099  CD1 LEU A 138      44.098  29.120  27.076  1.00 26.57           C  
-ATOM   1100  CD2 LEU A 138      44.343  28.866  24.590  1.00 24.87           C  
-ATOM   1101  N   VAL A 139      39.659  27.421  25.854  1.00 22.39           N  
-ATOM   1102  CA  VAL A 139      38.415  28.128  25.577  1.00 22.16           C  
-ATOM   1103  C   VAL A 139      37.555  28.130  26.846  1.00 22.08           C  
-ATOM   1104  O   VAL A 139      36.946  29.144  27.208  1.00 21.49           O  
-ATOM   1105  CB  VAL A 139      37.631  27.444  24.432  1.00 22.18           C  
-ATOM   1106  CG1 VAL A 139      36.301  28.145  24.220  1.00 22.21           C  
-ATOM   1107  CG2 VAL A 139      38.453  27.475  23.147  1.00 24.95           C  
-ATOM   1108  N   GLN A 140      37.508  26.989  27.527  1.00 21.30           N  
-ATOM   1109  CA  GLN A 140      36.728  26.893  28.755  1.00 20.70           C  
-ATOM   1110  C   GLN A 140      37.244  27.914  29.761  1.00 20.72           C  
-ATOM   1111  O   GLN A 140      36.470  28.604  30.414  1.00 19.91           O  
-ATOM   1112  CB  GLN A 140      36.847  25.497  29.361  1.00 22.85           C  
-ATOM   1113  CG  GLN A 140      36.066  25.348  30.663  1.00 23.22           C  
-ATOM   1114  CD  GLN A 140      34.571  25.465  30.447  1.00 25.09           C  
-ATOM   1115  OE1 GLN A 140      33.892  26.287  31.077  1.00 27.20           O  
-ATOM   1116  NE2 GLN A 140      34.048  24.644  29.551  1.00 21.50           N  
-ATOM   1117  N   LEU A 141      38.564  27.990  29.879  1.00 21.04           N  
-ATOM   1118  CA  LEU A 141      39.214  28.916  30.802  1.00 22.94           C  
-ATOM   1119  C   LEU A 141      38.851  30.369  30.509  1.00 21.70           C  
-ATOM   1120  O   LEU A 141      38.499  31.120  31.418  1.00 21.29           O  
-ATOM   1121  CB  LEU A 141      40.728  28.727  30.723  1.00 22.96           C  
-ATOM   1122  CG  LEU A 141      41.469  28.098  31.905  1.00 28.28           C  
-ATOM   1123  CD1 LEU A 141      40.643  27.005  32.554  1.00 25.72           C  
-ATOM   1124  CD2 LEU A 141      42.813  27.576  31.423  1.00 25.16           C  
-ATOM   1125  N   ALA A 142      38.938  30.765  29.241  1.00 20.87           N  
-ATOM   1126  CA  ALA A 142      38.611  32.137  28.856  1.00 21.75           C  
-ATOM   1127  C   ALA A 142      37.140  32.429  29.131  1.00 20.40           C  
-ATOM   1128  O   ALA A 142      36.789  33.520  29.583  1.00 19.43           O  
-ATOM   1129  CB  ALA A 142      38.925  32.362  27.373  1.00 21.98           C  
-ATOM   1130  N   ALA A 143      36.277  31.452  28.859  1.00 19.24           N  
-ATOM   1131  CA  ALA A 143      34.846  31.626  29.101  1.00 20.09           C  
-ATOM   1132  C   ALA A 143      34.618  31.800  30.601  1.00 18.43           C  
-ATOM   1133  O   ALA A 143      33.814  32.635  31.025  1.00 19.55           O  
-ATOM   1134  CB  ALA A 143      34.066  30.415  28.583  1.00 19.65           C  
-ATOM   1135  N   ASP A 144      35.325  31.005  31.403  1.00 20.09           N  
-ATOM   1136  CA  ASP A 144      35.206  31.109  32.856  1.00 19.70           C  
-ATOM   1137  C   ASP A 144      35.630  32.508  33.298  1.00 19.58           C  
-ATOM   1138  O   ASP A 144      35.027  33.096  34.196  1.00 20.01           O  
-ATOM   1139  CB  ASP A 144      36.096  30.078  33.562  1.00 20.21           C  
-ATOM   1140  CG  ASP A 144      35.572  28.661  33.426  1.00 21.46           C  
-ATOM   1141  OD1 ASP A 144      34.354  28.493  33.227  1.00 22.24           O  
-ATOM   1142  OD2 ASP A 144      36.379  27.717  33.534  1.00 22.93           O  
-ATOM   1143  N   GLY A 145      36.683  33.032  32.675  1.00 20.18           N  
-ATOM   1144  CA  GLY A 145      37.157  34.360  33.040  1.00 18.55           C  
-ATOM   1145  C   GLY A 145      36.129  35.438  32.742  1.00 18.46           C  
-ATOM   1146  O   GLY A 145      35.906  36.345  33.541  1.00 20.54           O  
-ATOM   1147  N   LEU A 146      35.492  35.346  31.582  1.00 20.44           N  
-ATOM   1148  CA  LEU A 146      34.488  36.336  31.206  1.00 20.28           C  
-ATOM   1149  C   LEU A 146      33.309  36.261  32.183  1.00 19.72           C  
-ATOM   1150  O   LEU A 146      32.709  37.269  32.538  1.00 19.53           O  
-ATOM   1151  CB  LEU A 146      34.022  36.075  29.771  1.00 22.41           C  
-ATOM   1152  CG  LEU A 146      33.160  37.159  29.124  1.00 24.84           C  
-ATOM   1153  CD1 LEU A 146      33.862  38.512  29.242  1.00 23.57           C  
-ATOM   1154  CD2 LEU A 146      32.926  36.806  27.660  1.00 26.02           C  
-ATOM   1155  N   PHE A 147      33.010  35.048  32.628  1.00 20.06           N  
-ATOM   1156  CA  PHE A 147      31.927  34.775  33.575  1.00 19.73           C  
-ATOM   1157  C   PHE A 147      32.131  35.509  34.916  1.00 18.96           C  
-ATOM   1158  O   PHE A 147      31.205  36.116  35.447  1.00 18.46           O  
-ATOM   1159  CB  PHE A 147      31.869  33.259  33.791  1.00 19.86           C  
-ATOM   1160  CG  PHE A 147      30.713  32.781  34.637  1.00 21.24           C  
-ATOM   1161  CD1 PHE A 147      29.396  33.081  34.294  1.00 18.59           C  
-ATOM   1162  CD2 PHE A 147      30.948  31.945  35.728  1.00 21.53           C  
-ATOM   1163  CE1 PHE A 147      28.328  32.547  35.019  1.00 22.10           C  
-ATOM   1164  CE2 PHE A 147      29.887  31.403  36.464  1.00 22.21           C  
-ATOM   1165  CZ  PHE A 147      28.575  31.704  36.106  1.00 24.07           C  
-ATOM   1166  N   VAL A 148      33.349  35.471  35.449  1.00 18.97           N  
-ATOM   1167  CA  VAL A 148      33.629  36.105  36.739  1.00 18.61           C  
-ATOM   1168  C   VAL A 148      34.385  37.431  36.660  1.00 19.68           C  
-ATOM   1169  O   VAL A 148      34.609  38.084  37.681  1.00 19.38           O  
-ATOM   1170  CB  VAL A 148      34.451  35.162  37.647  1.00 19.27           C  
-ATOM   1171  CG1 VAL A 148      33.744  33.818  37.785  1.00 18.02           C  
-ATOM   1172  CG2 VAL A 148      35.853  34.963  37.064  1.00 17.30           C  
-ATOM   1173  N   HIS A 149      34.776  37.819  35.453  1.00 20.24           N  
-ATOM   1174  CA  HIS A 149      35.543  39.048  35.239  1.00 20.41           C  
-ATOM   1175  C   HIS A 149      35.195  40.240  36.124  1.00 20.61           C  
-ATOM   1176  O   HIS A 149      36.067  40.790  36.797  1.00 20.52           O  
-ATOM   1177  CB  HIS A 149      35.440  39.477  33.769  1.00 19.87           C  
-ATOM   1178  CG  HIS A 149      36.209  40.723  33.450  1.00 21.12           C  
-ATOM   1179  ND1 HIS A 149      35.780  41.978  33.822  1.00 20.33           N  
-ATOM   1180  CD2 HIS A 149      37.397  40.901  32.823  1.00 20.40           C  
-ATOM   1181  CE1 HIS A 149      36.671  42.877  33.441  1.00 23.01           C  
-ATOM   1182  NE2 HIS A 149      37.662  42.249  32.833  1.00 22.83           N  
-ATOM   1183  N   ASP A 150      33.926  40.636  36.124  1.00 21.44           N  
-ATOM   1184  CA  ASP A 150      33.491  41.803  36.889  1.00 21.40           C  
-ATOM   1185  C   ASP A 150      33.640  41.750  38.413  1.00 22.88           C  
-ATOM   1186  O   ASP A 150      33.504  42.779  39.082  1.00 21.94           O  
-ATOM   1187  CB  ASP A 150      32.047  42.153  36.514  1.00 23.45           C  
-ATOM   1188  CG  ASP A 150      31.925  42.709  35.095  1.00 24.77           C  
-ATOM   1189  OD1 ASP A 150      32.965  42.958  34.445  1.00 24.67           O  
-ATOM   1190  OD2 ASP A 150      30.787  42.900  34.629  1.00 23.32           O  
-ATOM   1191  N   TYR A 151      33.920  40.568  38.963  1.00 20.97           N  
-ATOM   1192  CA  TYR A 151      34.103  40.424  40.408  1.00 21.41           C  
-ATOM   1193  C   TYR A 151      35.577  40.414  40.807  1.00 21.63           C  
-ATOM   1194  O   TYR A 151      35.913  40.719  41.952  1.00 20.42           O  
-ATOM   1195  CB  TYR A 151      33.465  39.123  40.914  1.00 18.49           C  
-ATOM   1196  CG  TYR A 151      31.962  39.110  40.822  1.00 20.75           C  
-ATOM   1197  CD1 TYR A 151      31.176  39.607  41.860  1.00 20.84           C  
-ATOM   1198  CD2 TYR A 151      31.324  38.635  39.679  1.00 20.41           C  
-ATOM   1199  CE1 TYR A 151      29.786  39.630  41.760  1.00 22.77           C  
-ATOM   1200  CE2 TYR A 151      29.945  38.657  39.568  1.00 21.29           C  
-ATOM   1201  CZ  TYR A 151      29.182  39.153  40.610  1.00 20.92           C  
-ATOM   1202  OH  TYR A 151      27.816  39.160  40.495  1.00 24.22           O  
-ATOM   1203  N   ILE A 152      36.455  40.065  39.869  1.00 20.76           N  
-ATOM   1204  CA  ILE A 152      37.875  39.985  40.185  1.00 21.36           C  
-ATOM   1205  C   ILE A 152      38.763  41.074  39.584  1.00 22.45           C  
-ATOM   1206  O   ILE A 152      39.982  41.032  39.733  1.00 23.51           O  
-ATOM   1207  CB  ILE A 152      38.435  38.598  39.806  1.00 20.77           C  
-ATOM   1208  CG1 ILE A 152      38.327  38.380  38.296  1.00 21.47           C  
-ATOM   1209  CG2 ILE A 152      37.657  37.508  40.564  1.00 19.61           C  
-ATOM   1210  CD1 ILE A 152      38.923  37.076  37.825  1.00 21.20           C  
-ATOM   1211  N   HIS A 153      38.152  42.034  38.896  1.00 24.00           N  
-ATOM   1212  CA  HIS A 153      38.883  43.161  38.315  1.00 25.56           C  
-ATOM   1213  C   HIS A 153      38.395  44.408  39.050  1.00 26.75           C  
-ATOM   1214  O   HIS A 153      37.291  44.412  39.598  1.00 24.99           O  
-ATOM   1215  CB  HIS A 153      38.586  43.293  36.818  1.00 24.56           C  
-ATOM   1216  CG  HIS A 153      39.307  42.296  35.966  1.00 26.19           C  
-ATOM   1217  ND1 HIS A 153      40.541  42.549  35.405  1.00 27.83           N  
-ATOM   1218  CD2 HIS A 153      38.965  41.047  35.574  1.00 24.68           C  
-ATOM   1219  CE1 HIS A 153      40.925  41.501  34.698  1.00 29.72           C  
-ATOM   1220  NE2 HIS A 153      39.985  40.575  34.784  1.00 26.69           N  
-ATOM   1221  N   ASP A 154      39.212  45.459  39.067  1.00 28.24           N  
-ATOM   1222  CA  ASP A 154      38.843  46.694  39.754  1.00 30.71           C  
-ATOM   1223  C   ASP A 154      37.793  47.501  38.993  1.00 31.91           C  
-ATOM   1224  O   ASP A 154      37.341  48.546  39.459  1.00 32.65           O  
-ATOM   1225  CB  ASP A 154      40.092  47.548  40.007  1.00 34.30           C  
-ATOM   1226  CG  ASP A 154      40.838  47.879  38.732  1.00 35.98           C  
-ATOM   1227  OD1 ASP A 154      40.290  48.629  37.905  1.00 38.21           O  
-ATOM   1228  OD2 ASP A 154      41.968  47.378  38.552  1.00 42.57           O  
-ATOM   1229  N   ASP A 155      37.413  47.018  37.814  1.00 31.86           N  
-ATOM   1230  CA  ASP A 155      36.388  47.679  37.018  1.00 31.83           C  
-ATOM   1231  C   ASP A 155      35.718  46.660  36.102  1.00 31.28           C  
-ATOM   1232  O   ASP A 155      36.315  45.643  35.749  1.00 31.11           O  
-ATOM   1233  CB  ASP A 155      36.984  48.823  36.192  1.00 35.17           C  
-ATOM   1234  CG  ASP A 155      35.915  49.744  35.622  1.00 38.74           C  
-ATOM   1235  OD1 ASP A 155      34.734  49.601  36.017  1.00 36.64           O  
-ATOM   1236  OD2 ASP A 155      36.254  50.613  34.789  1.00 40.31           O  
-ATOM   1237  N   VAL A 156      34.476  46.938  35.724  1.00 30.11           N  
-ATOM   1238  CA  VAL A 156      33.704  46.038  34.873  1.00 30.60           C  
-ATOM   1239  C   VAL A 156      33.881  46.288  33.376  1.00 30.93           C  
-ATOM   1240  O   VAL A 156      34.336  47.354  32.957  1.00 29.97           O  
-ATOM   1241  CB  VAL A 156      32.200  46.146  35.195  1.00 30.44           C  
-ATOM   1242  CG1 VAL A 156      31.967  45.915  36.679  1.00 31.57           C  
-ATOM   1243  CG2 VAL A 156      31.676  47.522  34.789  1.00 33.72           C  
-ATOM   1244  N   LEU A 157      33.515  45.290  32.578  1.00 29.73           N  
-ATOM   1245  CA  LEU A 157      33.591  45.396  31.125  1.00 31.22           C  
-ATOM   1246  C   LEU A 157      32.335  46.086  30.626  1.00 30.73           C  
-ATOM   1247  O   LEU A 157      31.240  45.804  31.108  1.00 29.06           O  
-ATOM   1248  CB  LEU A 157      33.659  44.011  30.474  1.00 31.26           C  
-ATOM   1249  CG  LEU A 157      34.984  43.255  30.432  1.00 31.10           C  
-ATOM   1250  CD1 LEU A 157      34.755  41.860  29.866  1.00 31.06           C  
-ATOM   1251  CD2 LEU A 157      35.978  44.024  29.574  1.00 31.33           C  
-ATOM   1252  N   SER A 158      32.486  46.992  29.666  1.00 31.44           N  
-ATOM   1253  CA  SER A 158      31.326  47.671  29.105  1.00 31.96           C  
-ATOM   1254  C   SER A 158      30.591  46.604  28.301  1.00 32.76           C  
-ATOM   1255  O   SER A 158      31.161  45.558  27.996  1.00 32.56           O  
-ATOM   1256  CB  SER A 158      31.764  48.803  28.175  1.00 31.32           C  
-ATOM   1257  OG  SER A 158      32.512  48.291  27.089  1.00 29.49           O  
-ATOM   1258  N   LYS A 159      29.335  46.862  27.953  1.00 34.18           N  
-ATOM   1259  CA  LYS A 159      28.564  45.896  27.184  1.00 34.95           C  
-ATOM   1260  C   LYS A 159      29.244  45.552  25.860  1.00 34.26           C  
-ATOM   1261  O   LYS A 159      29.328  44.381  25.482  1.00 33.27           O  
-ATOM   1262  CB  LYS A 159      27.162  46.433  26.904  1.00 38.47           C  
-ATOM   1263  CG  LYS A 159      26.279  45.446  26.162  1.00 42.51           C  
-ATOM   1264  CD  LYS A 159      24.982  46.085  25.688  1.00 46.31           C  
-ATOM   1265  CE  LYS A 159      24.087  45.054  25.010  1.00 48.12           C  
-ATOM   1266  NZ  LYS A 159      24.797  44.339  23.907  1.00 50.35           N  
-ATOM   1267  N   SER A 160      29.731  46.573  25.158  1.00 33.53           N  
-ATOM   1268  CA  SER A 160      30.387  46.367  23.870  1.00 32.40           C  
-ATOM   1269  C   SER A 160      31.695  45.593  23.994  1.00 30.97           C  
-ATOM   1270  O   SER A 160      31.977  44.712  23.183  1.00 30.90           O  
-ATOM   1271  CB  SER A 160      30.649  47.715  23.181  1.00 34.58           C  
-ATOM   1272  OG  SER A 160      31.569  48.506  23.915  1.00 37.31           O  
-ATOM   1273  N   LYS A 161      32.495  45.914  25.004  1.00 29.74           N  
-ATOM   1274  CA  LYS A 161      33.763  45.219  25.185  1.00 29.27           C  
-ATOM   1275  C   LYS A 161      33.554  43.754  25.556  1.00 27.61           C  
-ATOM   1276  O   LYS A 161      34.326  42.892  25.140  1.00 26.73           O  
-ATOM   1277  CB  LYS A 161      34.618  45.936  26.236  1.00 29.13           C  
-ATOM   1278  CG  LYS A 161      35.120  47.296  25.747  1.00 31.01           C  
-ATOM   1279  CD  LYS A 161      36.085  47.961  26.717  1.00 30.83           C  
-ATOM   1280  CE  LYS A 161      36.572  49.297  26.149  1.00 32.92           C  
-ATOM   1281  NZ  LYS A 161      37.581  49.965  27.024  1.00 32.70           N  
-ATOM   1282  N   ARG A 162      32.507  43.475  26.327  1.00 27.66           N  
-ATOM   1283  CA  ARG A 162      32.199  42.101  26.728  1.00 27.21           C  
-ATOM   1284  C   ARG A 162      31.798  41.310  25.490  1.00 27.44           C  
-ATOM   1285  O   ARG A 162      32.207  40.164  25.314  1.00 27.28           O  
-ATOM   1286  CB  ARG A 162      31.056  42.084  27.749  1.00 26.90           C  
-ATOM   1287  CG  ARG A 162      30.565  40.685  28.142  1.00 25.39           C  
-ATOM   1288  CD  ARG A 162      29.569  40.766  29.308  1.00 23.73           C  
-ATOM   1289  NE  ARG A 162      30.238  41.139  30.552  1.00 23.58           N  
-ATOM   1290  CZ  ARG A 162      30.843  40.281  31.370  1.00 23.86           C  
-ATOM   1291  NH1 ARG A 162      30.860  38.981  31.092  1.00 21.92           N  
-ATOM   1292  NH2 ARG A 162      31.460  40.730  32.457  1.00 24.50           N  
-ATOM   1293  N   GLN A 163      30.998  41.934  24.630  1.00 27.99           N  
-ATOM   1294  CA  GLN A 163      30.559  41.289  23.397  1.00 27.88           C  
-ATOM   1295  C   GLN A 163      31.768  41.041  22.500  1.00 26.89           C  
-ATOM   1296  O   GLN A 163      31.903  39.973  21.907  1.00 27.47           O  
-ATOM   1297  CB  GLN A 163      29.538  42.174  22.671  1.00 29.70           C  
-ATOM   1298  CG  GLN A 163      28.972  41.575  21.382  1.00 32.41           C  
-ATOM   1299  CD  GLN A 163      28.277  40.241  21.603  1.00 34.05           C  
-ATOM   1300  OE1 GLN A 163      27.552  40.061  22.582  1.00 35.05           O  
-ATOM   1301  NE2 GLN A 163      28.485  39.303  20.684  1.00 34.02           N  
-ATOM   1302  N   ALA A 164      32.651  42.032  22.406  1.00 27.19           N  
-ATOM   1303  CA  ALA A 164      33.844  41.893  21.582  1.00 27.80           C  
-ATOM   1304  C   ALA A 164      34.671  40.704  22.061  1.00 27.99           C  
-ATOM   1305  O   ALA A 164      35.198  39.938  21.253  1.00 27.98           O  
-ATOM   1306  CB  ALA A 164      34.676  43.167  21.640  1.00 28.97           C  
-ATOM   1307  N   MET A 165      34.782  40.539  23.376  1.00 26.84           N  
-ATOM   1308  CA  MET A 165      35.557  39.422  23.904  1.00 27.64           C  
-ATOM   1309  C   MET A 165      34.848  38.083  23.716  1.00 25.18           C  
-ATOM   1310  O   MET A 165      35.495  37.057  23.514  1.00 25.08           O  
-ATOM   1311  CB  MET A 165      35.896  39.652  25.378  1.00 25.80           C  
-ATOM   1312  CG  MET A 165      36.886  40.791  25.586  1.00 27.28           C  
-ATOM   1313  SD  MET A 165      38.282  40.722  24.435  1.00 28.77           S  
-ATOM   1314  CE  MET A 165      38.996  39.122  24.823  1.00 26.36           C  
-ATOM   1315  N   LEU A 166      33.522  38.091  23.779  1.00 26.62           N  
-ATOM   1316  CA  LEU A 166      32.758  36.862  23.572  1.00 26.34           C  
-ATOM   1317  C   LEU A 166      33.056  36.344  22.168  1.00 27.37           C  
-ATOM   1318  O   LEU A 166      33.362  35.162  21.966  1.00 25.94           O  
-ATOM   1319  CB  LEU A 166      31.259  37.139  23.709  1.00 26.39           C  
-ATOM   1320  CG  LEU A 166      30.299  36.090  23.135  1.00 25.98           C  
-ATOM   1321  CD1 LEU A 166      30.567  34.722  23.751  1.00 26.60           C  
-ATOM   1322  CD2 LEU A 166      28.863  36.528  23.395  1.00 26.07           C  
-ATOM   1323  N   GLU A 167      32.968  37.240  21.191  1.00 27.92           N  
-ATOM   1324  CA  GLU A 167      33.237  36.866  19.813  1.00 28.88           C  
-ATOM   1325  C   GLU A 167      34.681  36.391  19.682  1.00 27.86           C  
-ATOM   1326  O   GLU A 167      34.968  35.458  18.934  1.00 27.85           O  
-ATOM   1327  CB  GLU A 167      32.966  38.061  18.894  1.00 31.97           C  
-ATOM   1328  CG  GLU A 167      31.585  38.653  19.124  1.00 39.60           C  
-ATOM   1329  CD  GLU A 167      31.247  39.795  18.186  1.00 44.57           C  
-ATOM   1330  OE1 GLU A 167      32.089  40.703  18.016  1.00 46.76           O  
-ATOM   1331  OE2 GLU A 167      30.126  39.790  17.632  1.00 47.13           O  
-ATOM   1332  N   THR A 168      35.587  37.025  20.425  1.00 26.45           N  
-ATOM   1333  CA  THR A 168      36.997  36.647  20.390  1.00 26.70           C  
-ATOM   1334  C   THR A 168      37.178  35.226  20.933  1.00 26.61           C  
-ATOM   1335  O   THR A 168      37.939  34.429  20.375  1.00 26.28           O  
-ATOM   1336  CB  THR A 168      37.857  37.631  21.217  1.00 27.84           C  
-ATOM   1337  OG1 THR A 168      37.706  38.954  20.689  1.00 27.99           O  
-ATOM   1338  CG2 THR A 168      39.329  37.245  21.155  1.00 29.34           C  
-ATOM   1339  N   ILE A 169      36.475  34.902  22.015  1.00 24.21           N  
-ATOM   1340  CA  ILE A 169      36.573  33.563  22.592  1.00 23.92           C  
-ATOM   1341  C   ILE A 169      35.950  32.540  21.643  1.00 25.04           C  
-ATOM   1342  O   ILE A 169      36.464  31.432  21.481  1.00 25.50           O  
-ATOM   1343  CB  ILE A 169      35.861  33.478  23.969  1.00 22.47           C  
-ATOM   1344  CG1 ILE A 169      36.582  34.369  24.989  1.00 21.38           C  
-ATOM   1345  CG2 ILE A 169      35.868  32.038  24.469  1.00 21.95           C  
-ATOM   1346  CD1 ILE A 169      35.806  34.587  26.292  1.00 23.25           C  
-ATOM   1347  N   LEU A 170      34.839  32.914  21.018  1.00 25.65           N  
-ATOM   1348  CA  LEU A 170      34.164  32.024  20.081  1.00 29.12           C  
-ATOM   1349  C   LEU A 170      35.121  31.641  18.949  1.00 30.45           C  
-ATOM   1350  O   LEU A 170      35.177  30.483  18.532  1.00 30.12           O  
-ATOM   1351  CB  LEU A 170      32.917  32.714  19.512  1.00 28.93           C  
-ATOM   1352  CG  LEU A 170      31.511  32.342  20.015  1.00 31.88           C  
-ATOM   1353  CD1 LEU A 170      31.568  31.461  21.241  1.00 30.39           C  
-ATOM   1354  CD2 LEU A 170      30.736  33.613  20.296  1.00 28.99           C  
-ATOM   1355  N   GLU A 171      35.889  32.614  18.469  1.00 31.81           N  
-ATOM   1356  CA  GLU A 171      36.833  32.362  17.385  1.00 35.15           C  
-ATOM   1357  C   GLU A 171      38.032  31.540  17.844  1.00 35.45           C  
-ATOM   1358  O   GLU A 171      38.769  30.995  17.023  1.00 36.35           O  
-ATOM   1359  CB  GLU A 171      37.306  33.684  16.777  1.00 35.78           C  
-ATOM   1360  CG  GLU A 171      36.166  34.543  16.262  1.00 41.82           C  
-ATOM   1361  CD  GLU A 171      36.638  35.697  15.399  1.00 44.39           C  
-ATOM   1362  OE1 GLU A 171      37.553  36.430  15.830  1.00 46.09           O  
-ATOM   1363  OE2 GLU A 171      36.087  35.876  14.292  1.00 46.70           O  
-ATOM   1364  N   LEU A 172      38.222  31.444  19.157  1.00 34.73           N  
-ATOM   1365  CA  LEU A 172      39.335  30.672  19.702  1.00 35.48           C  
-ATOM   1366  C   LEU A 172      39.040  29.176  19.622  1.00 35.63           C  
-ATOM   1367  O   LEU A 172      39.944  28.353  19.730  1.00 36.27           O  
-ATOM   1368  CB  LEU A 172      39.596  31.075  21.158  1.00 33.65           C  
-ATOM   1369  CG  LEU A 172      40.700  30.332  21.915  1.00 35.67           C  
-ATOM   1370  CD1 LEU A 172      42.043  30.516  21.214  1.00 35.46           C  
-ATOM   1371  CD2 LEU A 172      40.771  30.856  23.344  1.00 34.56           C  
-ATOM   1372  N   ILE A 173      37.771  28.827  19.432  1.00 37.30           N  
-ATOM   1373  CA  ILE A 173      37.372  27.426  19.341  1.00 39.57           C  
-ATOM   1374  C   ILE A 173      38.017  26.741  18.137  1.00 43.58           C  
-ATOM   1375  O   ILE A 173      37.965  27.253  17.019  1.00 43.99           O  
-ATOM   1376  CB  ILE A 173      35.836  27.288  19.229  1.00 38.32           C  
-ATOM   1377  CG1 ILE A 173      35.177  27.791  20.515  1.00 34.48           C  
-ATOM   1378  CG2 ILE A 173      35.458  25.836  18.960  1.00 36.76           C  
-ATOM   1379  CD1 ILE A 173      33.663  27.701  20.520  1.00 34.91           C  
-ATOM   1380  N   PRO A 174      38.642  25.571  18.355  1.00 45.78           N  
-ATOM   1381  CA  PRO A 174      39.298  24.817  17.280  1.00 47.76           C  
-ATOM   1382  C   PRO A 174      38.348  24.436  16.144  1.00 48.63           C  
-ATOM   1383  O   PRO A 174      37.128  24.631  16.306  1.00 49.27           O  
-ATOM   1384  CB  PRO A 174      39.845  23.592  18.007  1.00 48.45           C  
-ATOM   1385  CG  PRO A 174      40.154  24.132  19.372  1.00 47.91           C  
-ATOM   1386  CD  PRO A 174      38.926  24.963  19.667  1.00 47.20           C  
-TER    1387      PRO A 174                                                      
-ATOM   1388  N   MET B   1      62.796  45.380  67.475  1.00 53.50           N  
-ATOM   1389  CA  MET B   1      62.172  46.670  67.885  1.00 52.39           C  
-ATOM   1390  C   MET B   1      60.734  46.440  68.349  1.00 50.55           C  
-ATOM   1391  O   MET B   1      60.373  45.341  68.773  1.00 50.70           O  
-ATOM   1392  CB  MET B   1      62.187  47.652  66.709  1.00 54.46           C  
-ATOM   1393  CG  MET B   1      62.934  48.955  66.982  1.00 56.77           C  
-ATOM   1394  SD  MET B   1      62.120  50.029  68.189  1.00 59.10           S  
-ATOM   1395  CE  MET B   1      61.279  51.186  67.101  1.00 58.42           C  
-ATOM   1396  N   ARG B   2      59.919  47.485  68.270  1.00 47.23           N  
-ATOM   1397  CA  ARG B   2      58.524  47.390  68.672  1.00 44.95           C  
-ATOM   1398  C   ARG B   2      57.667  47.051  67.454  1.00 42.55           C  
-ATOM   1399  O   ARG B   2      57.884  47.584  66.366  1.00 41.03           O  
-ATOM   1400  CB  ARG B   2      58.056  48.719  69.272  1.00 43.86           C  
-ATOM   1401  CG  ARG B   2      58.881  49.196  70.459  1.00 44.42           C  
-ATOM   1402  CD  ARG B   2      59.400  50.598  70.211  1.00 44.03           C  
-ATOM   1403  NE  ARG B   2      58.319  51.573  70.136  1.00 44.25           N  
-ATOM   1404  CZ  ARG B   2      58.410  52.745  69.516  1.00 44.31           C  
-ATOM   1405  NH1 ARG B   2      59.534  53.097  68.907  1.00 44.35           N  
-ATOM   1406  NH2 ARG B   2      57.373  53.570  69.509  1.00 44.59           N  
-ATOM   1407  N   THR B   3      56.705  46.156  67.642  1.00 40.59           N  
-ATOM   1408  CA  THR B   3      55.804  45.762  66.563  1.00 38.73           C  
-ATOM   1409  C   THR B   3      54.371  45.944  67.051  1.00 37.86           C  
-ATOM   1410  O   THR B   3      54.150  46.344  68.195  1.00 36.46           O  
-ATOM   1411  CB  THR B   3      56.017  44.289  66.153  1.00 37.65           C  
-ATOM   1412  OG1 THR B   3      55.819  43.442  67.289  1.00 36.22           O  
-ATOM   1413  CG2 THR B   3      57.429  44.082  65.611  1.00 40.07           C  
-ATOM   1414  N   SER B   4      53.403  45.650  66.189  1.00 35.41           N  
-ATOM   1415  CA  SER B   4      52.000  45.797  66.554  1.00 35.22           C  
-ATOM   1416  C   SER B   4      51.192  44.554  66.198  1.00 35.00           C  
-ATOM   1417  O   SER B   4      51.721  43.584  65.658  1.00 34.83           O  
-ATOM   1418  CB  SER B   4      51.392  47.000  65.839  1.00 34.55           C  
-ATOM   1419  OG  SER B   4      51.151  46.696  64.475  1.00 34.61           O  
-ATOM   1420  N   LYS B   5      49.899  44.594  66.500  1.00 33.04           N  
-ATOM   1421  CA  LYS B   5      49.020  43.470  66.212  1.00 32.49           C  
-ATOM   1422  C   LYS B   5      48.241  43.703  64.920  1.00 31.23           C  
-ATOM   1423  O   LYS B   5      47.391  42.896  64.546  1.00 27.88           O  
-ATOM   1424  CB  LYS B   5      48.043  43.277  67.370  1.00 34.19           C  
-ATOM   1425  CG  LYS B   5      48.708  42.899  68.687  1.00 36.43           C  
-ATOM   1426  CD  LYS B   5      49.411  41.561  68.563  1.00 37.26           C  
-ATOM   1427  CE  LYS B   5      49.916  41.079  69.903  1.00 39.10           C  
-ATOM   1428  NZ  LYS B   5      50.515  39.728  69.805  1.00 38.24           N  
-ATOM   1429  N   LYS B   6      48.552  44.802  64.239  1.00 28.48           N  
-ATOM   1430  CA  LYS B   6      47.860  45.175  63.011  1.00 28.54           C  
-ATOM   1431  C   LYS B   6      47.751  44.101  61.927  1.00 28.43           C  
-ATOM   1432  O   LYS B   6      46.654  43.850  61.419  1.00 27.72           O  
-ATOM   1433  CB  LYS B   6      48.494  46.432  62.415  1.00 29.82           C  
-ATOM   1434  CG  LYS B   6      47.649  47.073  61.320  1.00 32.98           C  
-ATOM   1435  CD  LYS B   6      48.304  48.320  60.754  1.00 35.54           C  
-ATOM   1436  CE  LYS B   6      47.406  48.967  59.707  1.00 38.99           C  
-ATOM   1437  NZ  LYS B   6      48.009  50.195  59.109  1.00 41.01           N  
-ATOM   1438  N   GLU B   7      48.863  43.469  61.558  1.00 27.16           N  
-ATOM   1439  CA  GLU B   7      48.795  42.456  60.512  1.00 28.35           C  
-ATOM   1440  C   GLU B   7      47.980  41.250  60.956  1.00 27.26           C  
-ATOM   1441  O   GLU B   7      47.169  40.734  60.191  1.00 27.97           O  
-ATOM   1442  CB  GLU B   7      50.188  41.983  60.078  1.00 30.40           C  
-ATOM   1443  CG  GLU B   7      50.179  41.444  58.645  1.00 35.18           C  
-ATOM   1444  CD  GLU B   7      51.385  40.594  58.291  1.00 40.35           C  
-ATOM   1445  OE1 GLU B   7      52.514  40.943  58.699  1.00 43.02           O  
-ATOM   1446  OE2 GLU B   7      51.201  39.576  57.582  1.00 40.01           O  
-ATOM   1447  N   MET B   8      48.200  40.799  62.187  1.00 25.94           N  
-ATOM   1448  CA  MET B   8      47.465  39.650  62.713  1.00 25.44           C  
-ATOM   1449  C   MET B   8      45.969  39.949  62.719  1.00 24.99           C  
-ATOM   1450  O   MET B   8      45.147  39.072  62.437  1.00 23.31           O  
-ATOM   1451  CB  MET B   8      47.949  39.313  64.130  1.00 27.45           C  
-ATOM   1452  CG  MET B   8      47.186  38.183  64.820  1.00 30.81           C  
-ATOM   1453  SD  MET B   8      45.756  38.748  65.783  1.00 33.81           S  
-ATOM   1454  CE  MET B   8      46.457  38.827  67.420  1.00 35.58           C  
-ATOM   1455  N   ILE B   9      45.613  41.188  63.041  1.00 21.44           N  
-ATOM   1456  CA  ILE B   9      44.209  41.573  63.066  1.00 21.49           C  
-ATOM   1457  C   ILE B   9      43.617  41.401  61.665  1.00 22.64           C  
-ATOM   1458  O   ILE B   9      42.557  40.790  61.498  1.00 20.44           O  
-ATOM   1459  CB  ILE B   9      44.045  43.044  63.541  1.00 20.40           C  
-ATOM   1460  CG1 ILE B   9      44.430  43.151  65.024  1.00 22.41           C  
-ATOM   1461  CG2 ILE B   9      42.613  43.508  63.341  1.00 20.56           C  
-ATOM   1462  CD1 ILE B   9      44.531  44.586  65.543  1.00 24.02           C  
-ATOM   1463  N   LEU B  10      44.314  41.935  60.664  1.00 21.35           N  
-ATOM   1464  CA  LEU B  10      43.874  41.847  59.272  1.00 22.52           C  
-ATOM   1465  C   LEU B  10      43.781  40.400  58.774  1.00 21.69           C  
-ATOM   1466  O   LEU B  10      42.799  40.021  58.136  1.00 20.28           O  
-ATOM   1467  CB  LEU B  10      44.839  42.626  58.369  1.00 23.66           C  
-ATOM   1468  CG  LEU B  10      44.539  44.058  57.894  1.00 27.47           C  
-ATOM   1469  CD1 LEU B  10      43.305  44.625  58.551  1.00 26.14           C  
-ATOM   1470  CD2 LEU B  10      45.755  44.927  58.158  1.00 27.16           C  
-ATOM   1471  N   ARG B  11      44.808  39.603  59.049  1.00 20.51           N  
-ATOM   1472  CA  ARG B  11      44.815  38.206  58.612  1.00 21.82           C  
-ATOM   1473  C   ARG B  11      43.678  37.443  59.288  1.00 22.05           C  
-ATOM   1474  O   ARG B  11      43.040  36.588  58.678  1.00 23.35           O  
-ATOM   1475  CB  ARG B  11      46.150  37.537  58.960  1.00 21.93           C  
-ATOM   1476  CG  ARG B  11      47.378  38.162  58.308  1.00 23.43           C  
-ATOM   1477  CD  ARG B  11      47.399  37.977  56.795  1.00 23.52           C  
-ATOM   1478  NE  ARG B  11      48.591  38.586  56.201  1.00 23.07           N  
-ATOM   1479  CZ  ARG B  11      48.778  38.756  54.894  1.00 25.07           C  
-ATOM   1480  NH1 ARG B  11      47.852  38.361  54.029  1.00 23.53           N  
-ATOM   1481  NH2 ARG B  11      49.888  39.339  54.449  1.00 23.73           N  
-ATOM   1482  N   THR B  12      43.428  37.747  60.555  1.00 22.38           N  
-ATOM   1483  CA  THR B  12      42.359  37.067  61.280  1.00 21.80           C  
-ATOM   1484  C   THR B  12      40.991  37.449  60.716  1.00 21.90           C  
-ATOM   1485  O   THR B  12      40.104  36.597  60.580  1.00 20.63           O  
-ATOM   1486  CB  THR B  12      42.406  37.398  62.778  1.00 22.57           C  
-ATOM   1487  OG1 THR B  12      43.697  37.049  63.298  1.00 22.58           O  
-ATOM   1488  CG2 THR B  12      41.333  36.609  63.533  1.00 21.99           C  
-ATOM   1489  N   ALA B  13      40.828  38.727  60.382  1.00 18.77           N  
-ATOM   1490  CA  ALA B  13      39.577  39.223  59.818  1.00 19.97           C  
-ATOM   1491  C   ALA B  13      39.305  38.582  58.457  1.00 19.52           C  
-ATOM   1492  O   ALA B  13      38.158  38.265  58.122  1.00 19.66           O  
-ATOM   1493  CB  ALA B  13      39.637  40.747  59.671  1.00 18.90           C  
-ATOM   1494  N   ILE B  14      40.358  38.414  57.665  1.00 18.58           N  
-ATOM   1495  CA  ILE B  14      40.219  37.802  56.349  1.00 19.79           C  
-ATOM   1496  C   ILE B  14      39.791  36.335  56.517  1.00 20.89           C  
-ATOM   1497  O   ILE B  14      38.851  35.882  55.869  1.00 21.00           O  
-ATOM   1498  CB  ILE B  14      41.547  37.920  55.550  1.00 18.95           C  
-ATOM   1499  CG1 ILE B  14      41.798  39.395  55.209  1.00 19.49           C  
-ATOM   1500  CG2 ILE B  14      41.479  37.095  54.261  1.00 19.46           C  
-ATOM   1501  CD1 ILE B  14      43.170  39.676  54.620  1.00 22.07           C  
-ATOM   1502  N   ASP B  15      40.450  35.599  57.404  1.00 21.49           N  
-ATOM   1503  CA  ASP B  15      40.057  34.207  57.609  1.00 25.06           C  
-ATOM   1504  C   ASP B  15      38.641  34.085  58.171  1.00 23.40           C  
-ATOM   1505  O   ASP B  15      37.919  33.136  57.858  1.00 22.86           O  
-ATOM   1506  CB  ASP B  15      41.050  33.493  58.522  1.00 27.81           C  
-ATOM   1507  CG  ASP B  15      42.351  33.176  57.814  1.00 32.62           C  
-ATOM   1508  OD1 ASP B  15      42.318  33.013  56.573  1.00 36.24           O  
-ATOM   1509  OD2 ASP B  15      43.395  33.080  58.491  1.00 35.73           O  
-ATOM   1510  N   TYR B  16      38.245  35.056  58.988  1.00 21.05           N  
-ATOM   1511  CA  TYR B  16      36.912  35.075  59.575  1.00 20.74           C  
-ATOM   1512  C   TYR B  16      35.815  34.955  58.512  1.00 21.54           C  
-ATOM   1513  O   TYR B  16      34.859  34.199  58.679  1.00 20.08           O  
-ATOM   1514  CB  TYR B  16      36.696  36.380  60.361  1.00 21.08           C  
-ATOM   1515  CG  TYR B  16      35.318  36.484  60.979  1.00 20.46           C  
-ATOM   1516  CD1 TYR B  16      35.060  35.957  62.246  1.00 19.13           C  
-ATOM   1517  CD2 TYR B  16      34.258  37.067  60.278  1.00 18.43           C  
-ATOM   1518  CE1 TYR B  16      33.785  36.005  62.800  1.00 18.84           C  
-ATOM   1519  CE2 TYR B  16      32.973  37.118  60.825  1.00 17.67           C  
-ATOM   1520  CZ  TYR B  16      32.747  36.582  62.085  1.00 18.85           C  
-ATOM   1521  OH  TYR B  16      31.483  36.598  62.626  1.00 19.74           O  
-ATOM   1522  N   ILE B  17      35.948  35.697  57.418  1.00 22.40           N  
-ATOM   1523  CA  ILE B  17      34.918  35.662  56.380  1.00 24.68           C  
-ATOM   1524  C   ILE B  17      34.797  34.307  55.669  1.00 23.03           C  
-ATOM   1525  O   ILE B  17      33.757  33.996  55.085  1.00 22.50           O  
-ATOM   1526  CB  ILE B  17      35.132  36.799  55.342  1.00 27.82           C  
-ATOM   1527  CG1 ILE B  17      36.331  36.500  54.449  1.00 29.59           C  
-ATOM   1528  CG2 ILE B  17      35.366  38.118  56.059  1.00 26.46           C  
-ATOM   1529  CD1 ILE B  17      36.012  35.579  53.317  1.00 35.54           C  
-ATOM   1530  N   GLY B  18      35.850  33.500  55.718  1.00 23.83           N  
-ATOM   1531  CA  GLY B  18      35.793  32.192  55.085  1.00 23.48           C  
-ATOM   1532  C   GLY B  18      35.044  31.211  55.968  1.00 25.92           C  
-ATOM   1533  O   GLY B  18      34.412  30.264  55.494  1.00 23.86           O  
-ATOM   1534  N   GLU B  19      35.113  31.444  57.272  1.00 26.17           N  
-ATOM   1535  CA  GLU B  19      34.442  30.583  58.233  1.00 27.04           C  
-ATOM   1536  C   GLU B  19      33.044  31.099  58.538  1.00 25.82           C  
-ATOM   1537  O   GLU B  19      32.143  30.332  58.872  1.00 26.88           O  
-ATOM   1538  CB  GLU B  19      35.262  30.512  59.522  1.00 28.99           C  
-ATOM   1539  CG  GLU B  19      34.557  29.825  60.675  1.00 33.64           C  
-ATOM   1540  CD  GLU B  19      35.513  29.464  61.792  1.00 37.14           C  
-ATOM   1541  OE1 GLU B  19      36.388  30.295  62.126  1.00 40.10           O  
-ATOM   1542  OE2 GLU B  19      35.385  28.350  62.338  1.00 40.71           O  
-ATOM   1543  N   TYR B  20      32.868  32.408  58.424  1.00 22.53           N  
-ATOM   1544  CA  TYR B  20      31.581  33.023  58.695  1.00 21.00           C  
-ATOM   1545  C   TYR B  20      31.168  33.887  57.509  1.00 21.01           C  
-ATOM   1546  O   TYR B  20      30.773  33.362  56.465  1.00 20.21           O  
-ATOM   1547  CB  TYR B  20      31.676  33.841  59.987  1.00 22.91           C  
-ATOM   1548  CG  TYR B  20      31.920  32.964  61.198  1.00 23.29           C  
-ATOM   1549  CD1 TYR B  20      30.920  32.117  61.679  1.00 25.85           C  
-ATOM   1550  CD2 TYR B  20      33.164  32.936  61.828  1.00 24.59           C  
-ATOM   1551  CE1 TYR B  20      31.151  31.257  62.756  1.00 24.97           C  
-ATOM   1552  CE2 TYR B  20      33.408  32.078  62.911  1.00 28.19           C  
-ATOM   1553  CZ  TYR B  20      32.396  31.241  63.366  1.00 28.03           C  
-ATOM   1554  OH  TYR B  20      32.630  30.383  64.423  1.00 28.99           O  
-ATOM   1555  N   SER B  21      31.265  35.201  57.654  1.00 17.54           N  
-ATOM   1556  CA  SER B  21      30.893  36.083  56.559  1.00 17.81           C  
-ATOM   1557  C   SER B  21      31.368  37.496  56.811  1.00 19.43           C  
-ATOM   1558  O   SER B  21      31.732  37.854  57.930  1.00 18.56           O  
-ATOM   1559  CB  SER B  21      29.373  36.115  56.392  1.00 20.09           C  
-ATOM   1560  OG  SER B  21      28.753  36.668  57.549  1.00 17.87           O  
-ATOM   1561  N   LEU B  22      31.365  38.293  55.752  1.00 18.92           N  
-ATOM   1562  CA  LEU B  22      31.741  39.689  55.858  1.00 20.85           C  
-ATOM   1563  C   LEU B  22      30.591  40.331  56.644  1.00 21.06           C  
-ATOM   1564  O   LEU B  22      30.806  41.200  57.489  1.00 20.89           O  
-ATOM   1565  CB  LEU B  22      31.844  40.288  54.451  1.00 22.49           C  
-ATOM   1566  CG  LEU B  22      32.938  41.280  54.048  1.00 28.52           C  
-ATOM   1567  CD1 LEU B  22      34.260  40.986  54.739  1.00 25.98           C  
-ATOM   1568  CD2 LEU B  22      33.096  41.199  52.533  1.00 24.70           C  
-ATOM   1569  N   GLU B  23      29.367  39.880  56.376  1.00 19.43           N  
-ATOM   1570  CA  GLU B  23      28.191  40.421  57.057  1.00 20.74           C  
-ATOM   1571  C   GLU B  23      28.309  40.433  58.585  1.00 20.24           C  
-ATOM   1572  O   GLU B  23      27.981  41.438  59.223  1.00 20.12           O  
-ATOM   1573  CB  GLU B  23      26.917  39.650  56.664  1.00 19.42           C  
-ATOM   1574  CG  GLU B  23      25.668  40.181  57.379  1.00 22.65           C  
-ATOM   1575  CD  GLU B  23      24.401  39.374  57.119  1.00 26.03           C  
-ATOM   1576  OE1 GLU B  23      24.467  38.303  56.474  1.00 21.74           O  
-ATOM   1577  OE2 GLU B  23      23.330  39.817  57.581  1.00 25.42           O  
-ATOM   1578  N   THR B  24      28.767  39.332  59.179  1.00 19.67           N  
-ATOM   1579  CA  THR B  24      28.891  39.282  60.638  1.00 21.30           C  
-ATOM   1580  C   THR B  24      30.253  39.709  61.185  1.00 20.72           C  
-ATOM   1581  O   THR B  24      30.480  39.645  62.389  1.00 20.16           O  
-ATOM   1582  CB  THR B  24      28.558  37.884  61.207  1.00 21.44           C  
-ATOM   1583  OG1 THR B  24      29.543  36.940  60.778  1.00 18.98           O  
-ATOM   1584  CG2 THR B  24      27.179  37.434  60.733  1.00 20.94           C  
-ATOM   1585  N   LEU B  25      31.163  40.129  60.310  1.00 20.49           N  
-ATOM   1586  CA  LEU B  25      32.467  40.597  60.771  1.00 20.64           C  
-ATOM   1587  C   LEU B  25      32.209  41.948  61.447  1.00 21.41           C  
-ATOM   1588  O   LEU B  25      31.773  42.897  60.796  1.00 20.94           O  
-ATOM   1589  CB  LEU B  25      33.430  40.782  59.590  1.00 19.59           C  
-ATOM   1590  CG  LEU B  25      34.768  41.466  59.903  1.00 20.41           C  
-ATOM   1591  CD1 LEU B  25      35.572  40.614  60.861  1.00 17.59           C  
-ATOM   1592  CD2 LEU B  25      35.549  41.698  58.615  1.00 19.52           C  
-ATOM   1593  N   SER B  26      32.462  42.018  62.750  1.00 22.77           N  
-ATOM   1594  CA  SER B  26      32.248  43.243  63.523  1.00 24.07           C  
-ATOM   1595  C   SER B  26      33.352  43.352  64.562  1.00 23.51           C  
-ATOM   1596  O   SER B  26      34.179  42.454  64.681  1.00 21.51           O  
-ATOM   1597  CB  SER B  26      30.910  43.173  64.259  1.00 26.01           C  
-ATOM   1598  OG  SER B  26      30.953  42.163  65.259  1.00 26.84           O  
-ATOM   1599  N   TYR B  27      33.368  44.444  65.323  1.00 23.38           N  
-ATOM   1600  CA  TYR B  27      34.387  44.573  66.353  1.00 24.11           C  
-ATOM   1601  C   TYR B  27      34.217  43.472  67.390  1.00 23.71           C  
-ATOM   1602  O   TYR B  27      35.197  42.948  67.906  1.00 25.56           O  
-ATOM   1603  CB  TYR B  27      34.328  45.949  67.024  1.00 24.88           C  
-ATOM   1604  CG  TYR B  27      34.919  47.043  66.168  1.00 24.22           C  
-ATOM   1605  CD1 TYR B  27      34.133  47.755  65.266  1.00 26.39           C  
-ATOM   1606  CD2 TYR B  27      36.279  47.341  66.234  1.00 25.00           C  
-ATOM   1607  CE1 TYR B  27      34.690  48.743  64.449  1.00 28.46           C  
-ATOM   1608  CE2 TYR B  27      36.844  48.316  65.425  1.00 25.92           C  
-ATOM   1609  CZ  TYR B  27      36.047  49.016  64.538  1.00 27.80           C  
-ATOM   1610  OH  TYR B  27      36.602  50.000  63.754  1.00 30.45           O  
-ATOM   1611  N   ASP B  28      32.972  43.103  67.682  1.00 24.84           N  
-ATOM   1612  CA  ASP B  28      32.727  42.047  68.654  1.00 24.60           C  
-ATOM   1613  C   ASP B  28      33.234  40.692  68.174  1.00 23.70           C  
-ATOM   1614  O   ASP B  28      33.926  39.987  68.910  1.00 23.50           O  
-ATOM   1615  CB  ASP B  28      31.234  41.930  68.983  1.00 28.99           C  
-ATOM   1616  CG  ASP B  28      30.736  43.063  69.857  1.00 34.07           C  
-ATOM   1617  OD1 ASP B  28      31.472  43.476  70.775  1.00 36.11           O  
-ATOM   1618  OD2 ASP B  28      29.601  43.532  69.637  1.00 39.45           O  
-ATOM   1619  N   SER B  29      32.902  40.320  66.942  1.00 22.66           N  
-ATOM   1620  CA  SER B  29      33.336  39.022  66.437  1.00 22.04           C  
-ATOM   1621  C   SER B  29      34.834  38.983  66.171  1.00 20.47           C  
-ATOM   1622  O   SER B  29      35.462  37.939  66.325  1.00 21.11           O  
-ATOM   1623  CB  SER B  29      32.555  38.637  65.166  1.00 22.47           C  
-ATOM   1624  OG  SER B  29      32.736  39.572  64.118  1.00 24.06           O  
-ATOM   1625  N   LEU B  30      35.411  40.117  65.779  1.00 21.51           N  
-ATOM   1626  CA  LEU B  30      36.845  40.166  65.506  1.00 21.88           C  
-ATOM   1627  C   LEU B  30      37.612  40.154  66.826  1.00 21.58           C  
-ATOM   1628  O   LEU B  30      38.712  39.616  66.908  1.00 22.23           O  
-ATOM   1629  CB  LEU B  30      37.201  41.417  64.692  1.00 19.06           C  
-ATOM   1630  CG  LEU B  30      38.651  41.518  64.197  1.00 19.50           C  
-ATOM   1631  CD1 LEU B  30      39.043  40.265  63.414  1.00 19.70           C  
-ATOM   1632  CD2 LEU B  30      38.796  42.754  63.318  1.00 19.86           C  
-ATOM   1633  N   ALA B  31      37.024  40.743  67.861  1.00 23.27           N  
-ATOM   1634  CA  ALA B  31      37.663  40.754  69.172  1.00 24.34           C  
-ATOM   1635  C   ALA B  31      37.760  39.308  69.655  1.00 25.66           C  
-ATOM   1636  O   ALA B  31      38.798  38.872  70.156  1.00 25.93           O  
-ATOM   1637  CB  ALA B  31      36.843  41.585  70.152  1.00 22.91           C  
-ATOM   1638  N   GLU B  32      36.671  38.564  69.496  1.00 25.87           N  
-ATOM   1639  CA  GLU B  32      36.641  37.166  69.908  1.00 27.90           C  
-ATOM   1640  C   GLU B  32      37.641  36.357  69.082  1.00 27.11           C  
-ATOM   1641  O   GLU B  32      38.342  35.493  69.605  1.00 26.27           O  
-ATOM   1642  CB  GLU B  32      35.233  36.586  69.717  1.00 31.98           C  
-ATOM   1643  CG  GLU B  32      35.052  35.177  70.275  1.00 41.54           C  
-ATOM   1644  CD  GLU B  32      33.677  34.589  69.976  1.00 47.31           C  
-ATOM   1645  OE1 GLU B  32      32.663  35.282  70.214  1.00 50.98           O  
-ATOM   1646  OE2 GLU B  32      33.607  33.429  69.510  1.00 51.19           O  
-ATOM   1647  N   ALA B  33      37.712  36.650  67.788  1.00 26.15           N  
-ATOM   1648  CA  ALA B  33      38.611  35.927  66.895  1.00 26.05           C  
-ATOM   1649  C   ALA B  33      40.101  36.172  67.142  1.00 25.80           C  
-ATOM   1650  O   ALA B  33      40.903  35.245  67.052  1.00 23.79           O  
-ATOM   1651  CB  ALA B  33      38.270  36.256  65.445  1.00 26.05           C  
-ATOM   1652  N   THR B  34      40.470  37.414  67.441  1.00 24.43           N  
-ATOM   1653  CA  THR B  34      41.875  37.758  67.673  1.00 24.91           C  
-ATOM   1654  C   THR B  34      42.300  37.621  69.126  1.00 27.04           C  
-ATOM   1655  O   THR B  34      43.492  37.515  69.417  1.00 26.56           O  
-ATOM   1656  CB  THR B  34      42.178  39.212  67.279  1.00 24.72           C  
-ATOM   1657  OG1 THR B  34      41.382  40.087  68.087  1.00 24.74           O  
-ATOM   1658  CG2 THR B  34      41.881  39.451  65.805  1.00 22.77           C  
-ATOM   1659  N   GLY B  35      41.330  37.641  70.035  1.00 26.52           N  
-ATOM   1660  CA  GLY B  35      41.648  37.541  71.446  1.00 28.44           C  
-ATOM   1661  C   GLY B  35      42.065  38.898  71.989  1.00 28.66           C  
-ATOM   1662  O   GLY B  35      42.583  38.997  73.099  1.00 28.89           O  
-ATOM   1663  N   LEU B  36      41.835  39.942  71.196  1.00 26.63           N  
-ATOM   1664  CA  LEU B  36      42.170  41.314  71.571  1.00 27.07           C  
-ATOM   1665  C   LEU B  36      40.928  42.088  72.008  1.00 27.55           C  
-ATOM   1666  O   LEU B  36      39.801  41.700  71.697  1.00 26.75           O  
-ATOM   1667  CB  LEU B  36      42.817  42.037  70.384  1.00 28.20           C  
-ATOM   1668  CG  LEU B  36      44.321  41.867  70.138  1.00 30.44           C  
-ATOM   1669  CD1 LEU B  36      44.745  40.431  70.378  1.00 33.17           C  
-ATOM   1670  CD2 LEU B  36      44.651  42.314  68.714  1.00 27.70           C  
-ATOM   1671  N   SER B  37      41.133  43.188  72.726  1.00 26.92           N  
-ATOM   1672  CA  SER B  37      40.011  44.003  73.181  1.00 28.83           C  
-ATOM   1673  C   SER B  37      39.536  44.883  72.031  1.00 27.95           C  
-ATOM   1674  O   SER B  37      40.287  45.148  71.095  1.00 26.26           O  
-ATOM   1675  CB  SER B  37      40.433  44.883  74.363  1.00 27.90           C  
-ATOM   1676  OG  SER B  37      41.354  45.869  73.947  1.00 29.93           O  
-ATOM   1677  N   LYS B  38      38.289  45.334  72.091  1.00 28.56           N  
-ATOM   1678  CA  LYS B  38      37.774  46.187  71.032  1.00 30.74           C  
-ATOM   1679  C   LYS B  38      38.630  47.446  70.955  1.00 30.55           C  
-ATOM   1680  O   LYS B  38      38.821  48.015  69.883  1.00 28.42           O  
-ATOM   1681  CB  LYS B  38      36.308  46.542  71.295  1.00 34.05           C  
-ATOM   1682  CG  LYS B  38      35.379  45.327  71.248  1.00 37.87           C  
-ATOM   1683  CD  LYS B  38      33.932  45.676  71.594  1.00 42.61           C  
-ATOM   1684  CE  LYS B  38      33.253  46.475  70.491  1.00 44.09           C  
-ATOM   1685  NZ  LYS B  38      33.918  47.783  70.234  1.00 47.79           N  
-ATOM   1686  N   SER B  39      39.161  47.872  72.097  1.00 29.76           N  
-ATOM   1687  CA  SER B  39      40.006  49.057  72.125  1.00 28.73           C  
-ATOM   1688  C   SER B  39      41.282  48.761  71.342  1.00 27.15           C  
-ATOM   1689  O   SER B  39      41.810  49.626  70.640  1.00 27.39           O  
-ATOM   1690  CB  SER B  39      40.350  49.436  73.569  1.00 30.37           C  
-ATOM   1691  OG  SER B  39      41.171  50.590  73.603  1.00 32.53           O  
-ATOM   1692  N   GLY B  40      41.767  47.529  71.464  1.00 26.70           N  
-ATOM   1693  CA  GLY B  40      42.974  47.129  70.756  1.00 26.18           C  
-ATOM   1694  C   GLY B  40      42.784  47.096  69.247  1.00 25.54           C  
-ATOM   1695  O   GLY B  40      43.738  47.290  68.489  1.00 25.12           O  
-ATOM   1696  N   LEU B  41      41.554  46.835  68.810  1.00 24.95           N  
-ATOM   1697  CA  LEU B  41      41.224  46.793  67.381  1.00 24.54           C  
-ATOM   1698  C   LEU B  41      41.055  48.221  66.869  1.00 24.06           C  
-ATOM   1699  O   LEU B  41      41.566  48.584  65.808  1.00 22.94           O  
-ATOM   1700  CB  LEU B  41      39.914  46.025  67.159  1.00 23.82           C  
-ATOM   1701  CG  LEU B  41      39.918  44.493  67.245  1.00 26.97           C  
-ATOM   1702  CD1 LEU B  41      40.592  44.028  68.508  1.00 30.52           C  
-ATOM   1703  CD2 LEU B  41      38.476  43.990  67.189  1.00 24.05           C  
-ATOM   1704  N   ILE B  42      40.320  49.019  67.639  1.00 24.50           N  
-ATOM   1705  CA  ILE B  42      40.050  50.417  67.309  1.00 25.67           C  
-ATOM   1706  C   ILE B  42      41.346  51.202  67.159  1.00 25.74           C  
-ATOM   1707  O   ILE B  42      41.436  52.129  66.348  1.00 26.80           O  
-ATOM   1708  CB  ILE B  42      39.174  51.072  68.412  1.00 26.42           C  
-ATOM   1709  CG1 ILE B  42      37.769  50.461  68.379  1.00 27.55           C  
-ATOM   1710  CG2 ILE B  42      39.120  52.587  68.224  1.00 27.40           C  
-ATOM   1711  CD1 ILE B  42      36.865  50.881  69.536  1.00 28.00           C  
-ATOM   1712  N   TYR B  43      42.350  50.817  67.941  1.00 25.80           N  
-ATOM   1713  CA  TYR B  43      43.651  51.473  67.911  1.00 27.15           C  
-ATOM   1714  C   TYR B  43      44.193  51.548  66.485  1.00 28.66           C  
-ATOM   1715  O   TYR B  43      44.713  52.581  66.065  1.00 27.30           O  
-ATOM   1716  CB  TYR B  43      44.639  50.709  68.798  1.00 28.33           C  
-ATOM   1717  CG  TYR B  43      45.996  51.367  68.904  1.00 31.17           C  
-ATOM   1718  CD1 TYR B  43      46.204  52.453  69.759  1.00 32.51           C  
-ATOM   1719  CD2 TYR B  43      47.063  50.931  68.121  1.00 32.03           C  
-ATOM   1720  CE1 TYR B  43      47.447  53.090  69.828  1.00 32.28           C  
-ATOM   1721  CE2 TYR B  43      48.303  51.559  68.180  1.00 33.77           C  
-ATOM   1722  CZ  TYR B  43      48.488  52.637  69.035  1.00 34.10           C  
-ATOM   1723  OH  TYR B  43      49.714  53.262  69.080  1.00 36.60           O  
-ATOM   1724  N   HIS B  44      44.066  50.451  65.740  1.00 27.60           N  
-ATOM   1725  CA  HIS B  44      44.550  50.401  64.360  1.00 27.62           C  
-ATOM   1726  C   HIS B  44      43.457  50.698  63.328  1.00 27.55           C  
-ATOM   1727  O   HIS B  44      43.738  51.200  62.241  1.00 27.13           O  
-ATOM   1728  CB  HIS B  44      45.158  49.027  64.069  1.00 28.29           C  
-ATOM   1729  CG  HIS B  44      46.403  48.735  64.849  1.00 27.56           C  
-ATOM   1730  ND1 HIS B  44      47.574  49.438  64.672  1.00 29.71           N  
-ATOM   1731  CD2 HIS B  44      46.664  47.803  65.796  1.00 27.79           C  
-ATOM   1732  CE1 HIS B  44      48.505  48.951  65.472  1.00 26.97           C  
-ATOM   1733  NE2 HIS B  44      47.978  47.957  66.165  1.00 27.51           N  
-ATOM   1734  N   PHE B  45      42.212  50.396  63.672  1.00 25.67           N  
-ATOM   1735  CA  PHE B  45      41.094  50.620  62.756  1.00 27.00           C  
-ATOM   1736  C   PHE B  45      39.941  51.314  63.473  1.00 27.28           C  
-ATOM   1737  O   PHE B  45      39.114  50.665  64.110  1.00 27.19           O  
-ATOM   1738  CB  PHE B  45      40.656  49.268  62.186  1.00 25.25           C  
-ATOM   1739  CG  PHE B  45      41.788  48.487  61.585  1.00 24.16           C  
-ATOM   1740  CD1 PHE B  45      42.346  48.872  60.370  1.00 24.81           C  
-ATOM   1741  CD2 PHE B  45      42.336  47.400  62.261  1.00 23.56           C  
-ATOM   1742  CE1 PHE B  45      43.439  48.186  59.835  1.00 25.00           C  
-ATOM   1743  CE2 PHE B  45      43.426  46.707  61.738  1.00 24.95           C  
-ATOM   1744  CZ  PHE B  45      43.980  47.101  60.521  1.00 24.23           C  
-ATOM   1745  N   PRO B  46      39.873  52.655  63.370  1.00 28.70           N  
-ATOM   1746  CA  PRO B  46      38.840  53.481  64.001  1.00 29.69           C  
-ATOM   1747  C   PRO B  46      37.399  53.208  63.581  1.00 31.13           C  
-ATOM   1748  O   PRO B  46      36.471  53.486  64.341  1.00 31.31           O  
-ATOM   1749  CB  PRO B  46      39.289  54.908  63.674  1.00 30.67           C  
-ATOM   1750  CG  PRO B  46      39.980  54.753  62.370  1.00 32.24           C  
-ATOM   1751  CD  PRO B  46      40.791  53.490  62.575  1.00 29.78           C  
-ATOM   1752  N   SER B  47      37.212  52.671  62.378  1.00 29.13           N  
-ATOM   1753  CA  SER B  47      35.872  52.360  61.882  1.00 28.90           C  
-ATOM   1754  C   SER B  47      35.892  51.015  61.170  1.00 28.32           C  
-ATOM   1755  O   SER B  47      36.945  50.549  60.744  1.00 27.35           O  
-ATOM   1756  CB  SER B  47      35.404  53.423  60.895  1.00 28.10           C  
-ATOM   1757  OG  SER B  47      36.166  53.352  59.703  1.00 29.03           O  
-ATOM   1758  N   ARG B  48      34.727  50.392  61.040  1.00 28.67           N  
-ATOM   1759  CA  ARG B  48      34.651  49.109  60.357  1.00 28.43           C  
-ATOM   1760  C   ARG B  48      35.124  49.303  58.923  1.00 27.27           C  
-ATOM   1761  O   ARG B  48      35.833  48.461  58.370  1.00 27.74           O  
-ATOM   1762  CB  ARG B  48      33.216  48.583  60.371  1.00 30.34           C  
-ATOM   1763  CG  ARG B  48      33.052  47.210  59.727  1.00 28.38           C  
-ATOM   1764  CD  ARG B  48      31.675  46.644  60.025  1.00 29.27           C  
-ATOM   1765  NE  ARG B  48      31.471  45.318  59.443  1.00 28.53           N  
-ATOM   1766  CZ  ARG B  48      31.195  45.092  58.161  1.00 29.99           C  
-ATOM   1767  NH1 ARG B  48      31.086  46.104  57.309  1.00 25.28           N  
-ATOM   1768  NH2 ARG B  48      31.012  43.848  57.732  1.00 30.25           N  
-ATOM   1769  N   HIS B  49      34.744  50.430  58.325  1.00 26.58           N  
-ATOM   1770  CA  HIS B  49      35.146  50.721  56.954  1.00 26.03           C  
-ATOM   1771  C   HIS B  49      36.666  50.709  56.819  1.00 25.59           C  
-ATOM   1772  O   HIS B  49      37.206  50.189  55.841  1.00 25.84           O  
-ATOM   1773  CB  HIS B  49      34.606  52.082  56.510  1.00 27.27           C  
-ATOM   1774  CG  HIS B  49      34.908  52.406  55.081  1.00 27.29           C  
-ATOM   1775  ND1 HIS B  49      34.179  51.889  54.031  1.00 29.66           N  
-ATOM   1776  CD2 HIS B  49      35.890  53.153  54.524  1.00 26.54           C  
-ATOM   1777  CE1 HIS B  49      34.700  52.303  52.890  1.00 28.17           C  
-ATOM   1778  NE2 HIS B  49      35.740  53.071  53.161  1.00 28.04           N  
-ATOM   1779  N   ALA B  50      37.356  51.288  57.800  1.00 25.62           N  
-ATOM   1780  CA  ALA B  50      38.816  51.333  57.777  1.00 24.79           C  
-ATOM   1781  C   ALA B  50      39.384  49.921  57.855  1.00 24.24           C  
-ATOM   1782  O   ALA B  50      40.406  49.612  57.234  1.00 23.94           O  
-ATOM   1783  CB  ALA B  50      39.337  52.173  58.945  1.00 26.84           C  
-ATOM   1784  N   LEU B  51      38.730  49.068  58.634  1.00 22.91           N  
-ATOM   1785  CA  LEU B  51      39.176  47.683  58.765  1.00 23.04           C  
-ATOM   1786  C   LEU B  51      39.087  47.000  57.398  1.00 21.51           C  
-ATOM   1787  O   LEU B  51      40.066  46.427  56.914  1.00 22.32           O  
-ATOM   1788  CB  LEU B  51      38.300  46.938  59.775  1.00 22.00           C  
-ATOM   1789  CG  LEU B  51      38.506  45.420  59.862  1.00 23.84           C  
-ATOM   1790  CD1 LEU B  51      39.903  45.098  60.381  1.00 22.82           C  
-ATOM   1791  CD2 LEU B  51      37.444  44.831  60.780  1.00 23.29           C  
-ATOM   1792  N   LEU B  52      37.908  47.064  56.782  1.00 21.91           N  
-ATOM   1793  CA  LEU B  52      37.700  46.450  55.473  1.00 21.14           C  
-ATOM   1794  C   LEU B  52      38.686  46.991  54.445  1.00 21.67           C  
-ATOM   1795  O   LEU B  52      39.269  46.235  53.673  1.00 20.18           O  
-ATOM   1796  CB  LEU B  52      36.269  46.691  54.990  1.00 23.75           C  
-ATOM   1797  CG  LEU B  52      35.161  45.957  55.745  1.00 25.82           C  
-ATOM   1798  CD1 LEU B  52      33.817  46.252  55.092  1.00 27.00           C  
-ATOM   1799  CD2 LEU B  52      35.434  44.465  55.721  1.00 26.82           C  
-ATOM   1800  N   LEU B  53      38.873  48.306  54.429  1.00 21.25           N  
-ATOM   1801  CA  LEU B  53      39.808  48.909  53.491  1.00 21.23           C  
-ATOM   1802  C   LEU B  53      41.205  48.338  53.721  1.00 19.78           C  
-ATOM   1803  O   LEU B  53      41.923  48.019  52.774  1.00 19.94           O  
-ATOM   1804  CB  LEU B  53      39.834  50.429  53.674  1.00 23.45           C  
-ATOM   1805  CG  LEU B  53      40.836  51.202  52.814  1.00 25.52           C  
-ATOM   1806  CD1 LEU B  53      40.601  50.906  51.335  1.00 26.48           C  
-ATOM   1807  CD2 LEU B  53      40.687  52.691  53.098  1.00 28.13           C  
-ATOM   1808  N   GLY B  54      41.584  48.213  54.988  1.00 20.17           N  
-ATOM   1809  CA  GLY B  54      42.896  47.683  55.317  1.00 21.33           C  
-ATOM   1810  C   GLY B  54      43.082  46.249  54.846  1.00 21.61           C  
-ATOM   1811  O   GLY B  54      44.180  45.851  54.461  1.00 20.35           O  
-ATOM   1812  N   MET B  55      42.007  45.469  54.881  1.00 20.65           N  
-ATOM   1813  CA  MET B  55      42.061  44.077  54.439  1.00 20.86           C  
-ATOM   1814  C   MET B  55      42.320  44.021  52.934  1.00 20.10           C  
-ATOM   1815  O   MET B  55      43.145  43.239  52.466  1.00 20.13           O  
-ATOM   1816  CB  MET B  55      40.745  43.380  54.787  1.00 20.80           C  
-ATOM   1817  CG  MET B  55      40.529  43.253  56.297  1.00 21.29           C  
-ATOM   1818  SD  MET B  55      38.820  42.928  56.783  1.00 22.37           S  
-ATOM   1819  CE  MET B  55      38.519  41.305  55.982  1.00 19.21           C  
-ATOM   1820  N   HIS B  56      41.613  44.860  52.182  1.00 20.53           N  
-ATOM   1821  CA  HIS B  56      41.790  44.922  50.734  1.00 20.99           C  
-ATOM   1822  C   HIS B  56      43.199  45.396  50.379  1.00 22.20           C  
-ATOM   1823  O   HIS B  56      43.833  44.853  49.482  1.00 19.98           O  
-ATOM   1824  CB  HIS B  56      40.750  45.867  50.117  1.00 21.50           C  
-ATOM   1825  CG  HIS B  56      39.376  45.278  50.020  1.00 17.82           C  
-ATOM   1826  ND1 HIS B  56      38.981  44.484  48.965  1.00 19.52           N  
-ATOM   1827  CD2 HIS B  56      38.306  45.362  50.848  1.00 19.28           C  
-ATOM   1828  CE1 HIS B  56      37.728  44.105  49.145  1.00 18.47           C  
-ATOM   1829  NE2 HIS B  56      37.295  44.623  50.281  1.00 20.30           N  
-ATOM   1830  N   GLU B  57      43.692  46.416  51.081  1.00 23.35           N  
-ATOM   1831  CA  GLU B  57      45.033  46.926  50.808  1.00 23.37           C  
-ATOM   1832  C   GLU B  57      46.113  45.878  51.097  1.00 24.13           C  
-ATOM   1833  O   GLU B  57      47.095  45.774  50.363  1.00 26.16           O  
-ATOM   1834  CB  GLU B  57      45.301  48.194  51.634  1.00 26.08           C  
-ATOM   1835  CG  GLU B  57      44.313  49.329  51.358  1.00 27.45           C  
-ATOM   1836  CD  GLU B  57      44.630  50.591  52.147  1.00 30.55           C  
-ATOM   1837  OE1 GLU B  57      45.043  50.470  53.317  1.00 28.94           O  
-ATOM   1838  OE2 GLU B  57      44.454  51.700  51.600  1.00 30.11           O  
-ATOM   1839  N   LEU B  58      45.929  45.093  52.156  1.00 23.18           N  
-ATOM   1840  CA  LEU B  58      46.908  44.070  52.510  1.00 22.16           C  
-ATOM   1841  C   LEU B  58      47.052  43.045  51.387  1.00 21.46           C  
-ATOM   1842  O   LEU B  58      48.165  42.721  50.966  1.00 20.62           O  
-ATOM   1843  CB  LEU B  58      46.500  43.360  53.807  1.00 22.49           C  
-ATOM   1844  CG  LEU B  58      47.483  42.310  54.339  1.00 23.02           C  
-ATOM   1845  CD1 LEU B  58      48.839  42.970  54.612  1.00 24.62           C  
-ATOM   1846  CD2 LEU B  58      46.936  41.673  55.613  1.00 21.74           C  
-ATOM   1847  N   LEU B  59      45.922  42.532  50.909  1.00 20.97           N  
-ATOM   1848  CA  LEU B  59      45.921  41.550  49.830  1.00 19.82           C  
-ATOM   1849  C   LEU B  59      46.492  42.118  48.537  1.00 21.19           C  
-ATOM   1850  O   LEU B  59      47.229  41.437  47.830  1.00 19.07           O  
-ATOM   1851  CB  LEU B  59      44.494  41.052  49.581  1.00 23.78           C  
-ATOM   1852  CG  LEU B  59      44.074  39.765  50.295  1.00 26.52           C  
-ATOM   1853  CD1 LEU B  59      44.591  39.742  51.700  1.00 27.04           C  
-ATOM   1854  CD2 LEU B  59      42.558  39.626  50.247  1.00 26.39           C  
-ATOM   1855  N   ALA B  60      46.136  43.357  48.216  1.00 22.22           N  
-ATOM   1856  CA  ALA B  60      46.644  43.977  46.999  1.00 25.18           C  
-ATOM   1857  C   ALA B  60      48.158  44.118  47.109  1.00 26.46           C  
-ATOM   1858  O   ALA B  60      48.876  43.988  46.117  1.00 27.79           O  
-ATOM   1859  CB  ALA B  60      45.999  45.339  46.792  1.00 25.21           C  
-ATOM   1860  N   ASP B  61      48.641  44.380  48.322  1.00 28.73           N  
-ATOM   1861  CA  ASP B  61      50.077  44.525  48.552  1.00 28.65           C  
-ATOM   1862  C   ASP B  61      50.766  43.173  48.411  1.00 29.21           C  
-ATOM   1863  O   ASP B  61      51.844  43.082  47.820  1.00 29.06           O  
-ATOM   1864  CB  ASP B  61      50.352  45.096  49.945  1.00 30.34           C  
-ATOM   1865  CG  ASP B  61      51.829  45.375  50.175  1.00 34.14           C  
-ATOM   1866  OD1 ASP B  61      52.381  46.240  49.466  1.00 33.16           O  
-ATOM   1867  OD2 ASP B  61      52.438  44.725  51.054  1.00 35.51           O  
-ATOM   1868  N   ASP B  62      50.147  42.128  48.962  1.00 27.99           N  
-ATOM   1869  CA  ASP B  62      50.699  40.778  48.870  1.00 27.86           C  
-ATOM   1870  C   ASP B  62      50.968  40.444  47.406  1.00 27.60           C  
-ATOM   1871  O   ASP B  62      52.053  39.986  47.046  1.00 28.10           O  
-ATOM   1872  CB  ASP B  62      49.719  39.719  49.410  1.00 26.95           C  
-ATOM   1873  CG  ASP B  62      49.556  39.757  50.922  1.00 29.44           C  
-ATOM   1874  OD1 ASP B  62      50.466  40.246  51.627  1.00 26.81           O  
-ATOM   1875  OD2 ASP B  62      48.509  39.266  51.406  1.00 28.15           O  
-ATOM   1876  N   TRP B  63      49.965  40.668  46.565  1.00 26.86           N  
-ATOM   1877  CA  TRP B  63      50.090  40.360  45.145  1.00 28.06           C  
-ATOM   1878  C   TRP B  63      51.159  41.199  44.452  1.00 27.96           C  
-ATOM   1879  O   TRP B  63      51.956  40.676  43.679  1.00 28.65           O  
-ATOM   1880  CB  TRP B  63      48.747  40.551  44.439  1.00 27.83           C  
-ATOM   1881  CG  TRP B  63      48.649  39.752  43.162  1.00 29.35           C  
-ATOM   1882  CD1 TRP B  63      49.068  38.464  42.968  1.00 27.83           C  
-ATOM   1883  CD2 TRP B  63      48.071  40.175  41.928  1.00 28.38           C  
-ATOM   1884  NE1 TRP B  63      48.787  38.059  41.688  1.00 27.58           N  
-ATOM   1885  CE2 TRP B  63      48.172  39.089  41.026  1.00 29.63           C  
-ATOM   1886  CE3 TRP B  63      47.475  41.365  41.493  1.00 27.09           C  
-ATOM   1887  CZ2 TRP B  63      47.700  39.159  39.715  1.00 28.28           C  
-ATOM   1888  CZ3 TRP B  63      47.003  41.433  40.190  1.00 28.02           C  
-ATOM   1889  CH2 TRP B  63      47.119  40.336  39.315  1.00 29.41           C  
-ATOM   1890  N   ASP B  64      51.172  42.498  44.725  1.00 28.35           N  
-ATOM   1891  CA  ASP B  64      52.166  43.377  44.118  1.00 31.60           C  
-ATOM   1892  C   ASP B  64      53.575  42.860  44.411  1.00 32.88           C  
-ATOM   1893  O   ASP B  64      54.431  42.831  43.523  1.00 33.67           O  
-ATOM   1894  CB  ASP B  64      52.004  44.803  44.649  1.00 31.67           C  
-ATOM   1895  CG  ASP B  64      52.970  45.780  44.004  1.00 34.33           C  
-ATOM   1896  OD1 ASP B  64      52.997  45.862  42.757  1.00 35.16           O  
-ATOM   1897  OD2 ASP B  64      53.698  46.468  44.747  1.00 34.88           O  
-ATOM   1898  N   LYS B  65      53.814  42.439  45.651  1.00 33.90           N  
-ATOM   1899  CA  LYS B  65      55.127  41.924  46.028  1.00 36.45           C  
-ATOM   1900  C   LYS B  65      55.425  40.612  45.310  1.00 36.51           C  
-ATOM   1901  O   LYS B  65      56.564  40.352  44.921  1.00 37.36           O  
-ATOM   1902  CB  LYS B  65      55.216  41.718  47.546  1.00 38.31           C  
-ATOM   1903  CG  LYS B  65      55.135  43.008  48.354  1.00 41.16           C  
-ATOM   1904  CD  LYS B  65      55.424  42.769  49.835  1.00 43.92           C  
-ATOM   1905  CE  LYS B  65      54.455  41.767  50.456  1.00 46.04           C  
-ATOM   1906  NZ  LYS B  65      54.757  41.512  51.899  1.00 47.62           N  
-ATOM   1907  N   GLU B  66      54.402  39.783  45.133  1.00 35.81           N  
-ATOM   1908  CA  GLU B  66      54.584  38.512  44.445  1.00 37.23           C  
-ATOM   1909  C   GLU B  66      54.966  38.740  42.984  1.00 36.98           C  
-ATOM   1910  O   GLU B  66      55.857  38.071  42.458  1.00 36.87           O  
-ATOM   1911  CB  GLU B  66      53.303  37.675  44.525  1.00 39.30           C  
-ATOM   1912  CG  GLU B  66      53.097  36.988  45.867  1.00 43.32           C  
-ATOM   1913  CD  GLU B  66      51.680  36.469  46.058  1.00 45.95           C  
-ATOM   1914  OE1 GLU B  66      51.123  35.872  45.109  1.00 47.37           O  
-ATOM   1915  OE2 GLU B  66      51.128  36.655  47.164  1.00 48.38           O  
-ATOM   1916  N   LEU B  67      54.290  39.685  42.333  1.00 36.68           N  
-ATOM   1917  CA  LEU B  67      54.568  39.988  40.933  1.00 37.24           C  
-ATOM   1918  C   LEU B  67      55.968  40.560  40.739  1.00 38.77           C  
-ATOM   1919  O   LEU B  67      56.726  40.080  39.899  1.00 36.05           O  
-ATOM   1920  CB  LEU B  67      53.544  40.980  40.372  1.00 35.56           C  
-ATOM   1921  CG  LEU B  67      52.168  40.493  39.896  1.00 36.16           C  
-ATOM   1922  CD1 LEU B  67      52.332  39.273  38.995  1.00 33.84           C  
-ATOM   1923  CD2 LEU B  67      51.305  40.160  41.072  1.00 37.04           C  
-ATOM   1924  N   ARG B  68      56.304  41.589  41.514  1.00 41.23           N  
-ATOM   1925  CA  ARG B  68      57.615  42.224  41.412  1.00 45.24           C  
-ATOM   1926  C   ARG B  68      58.738  41.247  41.732  1.00 47.39           C  
-ATOM   1927  O   ARG B  68      59.866  41.398  41.263  1.00 47.44           O  
-ATOM   1928  CB  ARG B  68      57.691  43.435  42.347  1.00 45.17           C  
-ATOM   1929  CG  ARG B  68      56.685  44.516  42.001  1.00 48.35           C  
-ATOM   1930  CD  ARG B  68      56.871  45.778  42.823  1.00 50.92           C  
-ATOM   1931  NE  ARG B  68      55.875  46.786  42.466  1.00 53.46           N  
-ATOM   1932  CZ  ARG B  68      55.752  47.327  41.256  1.00 54.32           C  
-ATOM   1933  NH1 ARG B  68      56.568  46.966  40.272  1.00 54.27           N  
-ATOM   1934  NH2 ARG B  68      54.801  48.224  41.025  1.00 55.53           N  
-ATOM   1935  N   ASP B  69      58.419  40.236  42.528  1.00 50.57           N  
-ATOM   1936  CA  ASP B  69      59.394  39.227  42.908  1.00 54.17           C  
-ATOM   1937  C   ASP B  69      59.625  38.240  41.764  1.00 56.06           C  
-ATOM   1938  O   ASP B  69      60.702  37.657  41.644  1.00 55.89           O  
-ATOM   1939  CB  ASP B  69      58.901  38.489  44.154  1.00 56.26           C  
-ATOM   1940  CG  ASP B  69      59.862  37.417  44.619  1.00 58.64           C  
-ATOM   1941  OD1 ASP B  69      59.998  36.390  43.919  1.00 60.42           O  
-ATOM   1942  OD2 ASP B  69      60.483  37.604  45.686  1.00 60.54           O  
-ATOM   1943  N   ILE B  70      58.616  38.069  40.917  1.00 58.16           N  
-ATOM   1944  CA  ILE B  70      58.711  37.135  39.800  1.00 60.74           C  
-ATOM   1945  C   ILE B  70      58.857  37.835  38.449  1.00 62.80           C  
-ATOM   1946  O   ILE B  70      59.270  37.220  37.466  1.00 63.31           O  
-ATOM   1947  CB  ILE B  70      57.465  36.221  39.745  1.00 60.67           C  
-ATOM   1948  CG1 ILE B  70      57.707  35.052  38.789  1.00 61.44           C  
-ATOM   1949  CG2 ILE B  70      56.253  37.021  39.292  1.00 60.33           C  
-ATOM   1950  CD1 ILE B  70      58.777  34.081  39.259  1.00 61.80           C  
-ATOM   1951  N   THR B  71      58.521  39.119  38.401  1.00 65.05           N  
-ATOM   1952  CA  THR B  71      58.605  39.873  37.157  1.00 67.39           C  
-ATOM   1953  C   THR B  71      60.027  39.916  36.614  1.00 69.18           C  
-ATOM   1954  O   THR B  71      60.979  40.156  37.357  1.00 69.81           O  
-ATOM   1955  CB  THR B  71      58.102  41.318  37.342  1.00 67.30           C  
-ATOM   1956  OG1 THR B  71      58.069  41.976  36.070  1.00 67.77           O  
-ATOM   1957  CG2 THR B  71      59.018  42.089  38.286  1.00 66.36           C  
-ATOM   1958  N   ARG B  72      60.164  39.679  35.314  1.00 70.84           N  
-ATOM   1959  CA  ARG B  72      61.471  39.693  34.670  1.00 72.11           C  
-ATOM   1960  C   ARG B  72      61.813  41.105  34.202  1.00 72.82           C  
-ATOM   1961  O   ARG B  72      62.956  41.547  34.325  1.00 73.76           O  
-ATOM   1962  CB  ARG B  72      61.486  38.720  33.486  1.00 72.53           C  
-ATOM   1963  CG  ARG B  72      61.117  37.291  33.865  1.00 73.49           C  
-ATOM   1964  CD  ARG B  72      61.292  36.323  32.701  1.00 74.04           C  
-ATOM   1965  NE  ARG B  72      60.533  36.728  31.522  1.00 74.89           N  
-ATOM   1966  CZ  ARG B  72      60.448  36.016  30.402  1.00 75.37           C  
-ATOM   1967  NH1 ARG B  72      59.736  36.467  29.379  1.00 75.59           N  
-ATOM   1968  NH2 ARG B  72      61.071  34.849  30.305  1.00 75.23           N  
-ATOM   1969  N   ASP B  73      60.817  41.810  33.673  1.00 72.72           N  
-ATOM   1970  CA  ASP B  73      61.008  43.178  33.199  1.00 72.78           C  
-ATOM   1971  C   ASP B  73      59.721  43.980  33.375  1.00 72.01           C  
-ATOM   1972  O   ASP B  73      58.829  43.935  32.528  1.00 72.61           O  
-ATOM   1973  CB  ASP B  73      61.424  43.177  31.725  1.00 73.69           C  
-ATOM   1974  CG  ASP B  73      61.641  44.578  31.179  1.00 74.80           C  
-ATOM   1975  OD1 ASP B  73      60.651  45.328  31.038  1.00 75.02           O  
-ATOM   1976  OD2 ASP B  73      62.805  44.930  30.895  1.00 75.57           O  
-ATOM   1977  N   PRO B  74      59.615  44.731  34.482  1.00 70.83           N  
-ATOM   1978  CA  PRO B  74      58.435  45.547  34.783  1.00 69.60           C  
-ATOM   1979  C   PRO B  74      58.179  46.700  33.816  1.00 68.58           C  
-ATOM   1980  O   PRO B  74      57.302  47.529  34.057  1.00 68.59           O  
-ATOM   1981  CB  PRO B  74      58.712  46.031  36.203  1.00 69.66           C  
-ATOM   1982  CG  PRO B  74      60.200  46.164  36.214  1.00 70.18           C  
-ATOM   1983  CD  PRO B  74      60.639  44.891  35.530  1.00 70.60           C  
-ATOM   1984  N   GLU B  75      58.936  46.749  32.723  1.00 67.48           N  
-ATOM   1985  CA  GLU B  75      58.769  47.815  31.738  1.00 66.86           C  
-ATOM   1986  C   GLU B  75      57.868  47.397  30.578  1.00 64.60           C  
-ATOM   1987  O   GLU B  75      57.094  48.203  30.061  1.00 64.35           O  
-ATOM   1988  CB  GLU B  75      60.129  48.251  31.186  1.00 68.70           C  
-ATOM   1989  CG  GLU B  75      60.043  49.413  30.204  1.00 71.60           C  
-ATOM   1990  CD  GLU B  75      61.377  49.745  29.563  1.00 73.32           C  
-ATOM   1991  OE1 GLU B  75      61.925  48.881  28.843  1.00 74.06           O  
-ATOM   1992  OE2 GLU B  75      61.878  50.870  29.780  1.00 73.98           O  
-ATOM   1993  N   ASP B  76      57.973  46.136  30.173  1.00 62.02           N  
-ATOM   1994  CA  ASP B  76      57.171  45.618  29.071  1.00 58.88           C  
-ATOM   1995  C   ASP B  76      55.824  45.069  29.540  1.00 55.88           C  
-ATOM   1996  O   ASP B  76      55.767  44.160  30.367  1.00 55.52           O  
-ATOM   1997  CB  ASP B  76      57.952  44.532  28.327  1.00 60.28           C  
-ATOM   1998  CG  ASP B  76      57.119  43.833  27.273  1.00 61.69           C  
-ATOM   1999  OD1 ASP B  76      56.312  44.512  26.602  1.00 61.72           O  
-ATOM   2000  OD2 ASP B  76      57.278  42.604  27.108  1.00 63.08           O  
-ATOM   2001  N   PRO B  77      54.720  45.619  29.006  1.00 52.86           N  
-ATOM   2002  CA  PRO B  77      53.357  45.204  29.354  1.00 49.80           C  
-ATOM   2003  C   PRO B  77      53.134  43.696  29.235  1.00 47.05           C  
-ATOM   2004  O   PRO B  77      52.396  43.109  30.025  1.00 45.18           O  
-ATOM   2005  CB  PRO B  77      52.497  45.992  28.370  1.00 50.62           C  
-ATOM   2006  CG  PRO B  77      53.292  47.240  28.164  1.00 51.58           C  
-ATOM   2007  CD  PRO B  77      54.693  46.704  28.009  1.00 51.80           C  
-ATOM   2008  N   LEU B  78      53.766  43.076  28.245  1.00 43.89           N  
-ATOM   2009  CA  LEU B  78      53.622  41.639  28.047  1.00 41.66           C  
-ATOM   2010  C   LEU B  78      54.446  40.883  29.075  1.00 40.50           C  
-ATOM   2011  O   LEU B  78      54.194  39.708  29.350  1.00 38.37           O  
-ATOM   2012  CB  LEU B  78      54.057  41.238  26.633  1.00 41.59           C  
-ATOM   2013  CG  LEU B  78      53.170  41.704  25.475  1.00 41.78           C  
-ATOM   2014  CD1 LEU B  78      51.729  41.286  25.734  1.00 41.98           C  
-ATOM   2015  CD2 LEU B  78      53.256  43.212  25.334  1.00 44.29           C  
-ATOM   2016  N   GLU B  79      55.435  41.565  29.642  1.00 39.93           N  
-ATOM   2017  CA  GLU B  79      56.286  40.956  30.651  1.00 39.23           C  
-ATOM   2018  C   GLU B  79      55.542  40.986  31.985  1.00 37.01           C  
-ATOM   2019  O   GLU B  79      55.699  40.095  32.824  1.00 35.08           O  
-ATOM   2020  CB  GLU B  79      57.606  41.720  30.759  1.00 41.77           C  
-ATOM   2021  CG  GLU B  79      58.715  40.904  31.383  1.00 46.55           C  
-ATOM   2022  CD  GLU B  79      58.878  39.554  30.705  1.00 49.96           C  
-ATOM   2023  OE1 GLU B  79      59.050  39.522  29.468  1.00 51.50           O  
-ATOM   2024  OE2 GLU B  79      58.831  38.524  31.410  1.00 51.48           O  
-ATOM   2025  N   ARG B  80      54.731  42.022  32.174  1.00 34.65           N  
-ATOM   2026  CA  ARG B  80      53.944  42.149  33.392  1.00 34.04           C  
-ATOM   2027  C   ARG B  80      52.834  41.106  33.313  1.00 32.22           C  
-ATOM   2028  O   ARG B  80      52.468  40.497  34.317  1.00 30.35           O  
-ATOM   2029  CB  ARG B  80      53.323  43.542  33.490  1.00 35.06           C  
-ATOM   2030  CG  ARG B  80      54.319  44.689  33.464  1.00 39.93           C  
-ATOM   2031  CD  ARG B  80      53.584  46.011  33.315  1.00 42.77           C  
-ATOM   2032  NE  ARG B  80      54.436  47.051  32.753  1.00 49.12           N  
-ATOM   2033  CZ  ARG B  80      53.979  48.142  32.146  1.00 50.79           C  
-ATOM   2034  NH1 ARG B  80      52.673  48.339  32.023  1.00 51.28           N  
-ATOM   2035  NH2 ARG B  80      54.829  49.033  31.651  1.00 53.28           N  
-ATOM   2036  N   LEU B  81      52.304  40.911  32.107  1.00 30.49           N  
-ATOM   2037  CA  LEU B  81      51.237  39.942  31.888  1.00 29.56           C  
-ATOM   2038  C   LEU B  81      51.748  38.536  32.175  1.00 30.01           C  
-ATOM   2039  O   LEU B  81      51.050  37.729  32.787  1.00 28.58           O  
-ATOM   2040  CB  LEU B  81      50.717  40.035  30.447  1.00 29.63           C  
-ATOM   2041  CG  LEU B  81      49.612  39.051  30.030  1.00 28.86           C  
-ATOM   2042  CD1 LEU B  81      48.395  39.214  30.937  1.00 28.50           C  
-ATOM   2043  CD2 LEU B  81      49.229  39.297  28.572  1.00 27.13           C  
-ATOM   2044  N   ARG B  82      52.970  38.242  31.739  1.00 29.46           N  
-ATOM   2045  CA  ARG B  82      53.547  36.927  31.982  1.00 29.82           C  
-ATOM   2046  C   ARG B  82      53.631  36.686  33.487  1.00 28.11           C  
-ATOM   2047  O   ARG B  82      53.364  35.584  33.960  1.00 26.00           O  
-ATOM   2048  CB  ARG B  82      54.945  36.820  31.364  1.00 32.63           C  
-ATOM   2049  CG  ARG B  82      55.647  35.503  31.681  1.00 38.10           C  
-ATOM   2050  CD  ARG B  82      56.998  35.392  30.989  1.00 42.69           C  
-ATOM   2051  NE  ARG B  82      57.716  34.184  31.395  1.00 47.20           N  
-ATOM   2052  CZ  ARG B  82      58.234  33.995  32.605  1.00 49.99           C  
-ATOM   2053  NH1 ARG B  82      58.119  34.936  33.535  1.00 51.54           N  
-ATOM   2054  NH2 ARG B  82      58.867  32.865  32.889  1.00 51.91           N  
-ATOM   2055  N   ALA B  83      54.001  37.725  34.229  1.00 26.95           N  
-ATOM   2056  CA  ALA B  83      54.112  37.635  35.680  1.00 27.73           C  
-ATOM   2057  C   ALA B  83      52.746  37.274  36.262  1.00 26.79           C  
-ATOM   2058  O   ALA B  83      52.636  36.375  37.097  1.00 27.71           O  
-ATOM   2059  CB  ALA B  83      54.597  38.965  36.253  1.00 27.24           C  
-ATOM   2060  N   VAL B  84      51.710  37.978  35.817  1.00 25.89           N  
-ATOM   2061  CA  VAL B  84      50.349  37.713  36.279  1.00 26.33           C  
-ATOM   2062  C   VAL B  84      50.001  36.238  36.080  1.00 24.98           C  
-ATOM   2063  O   VAL B  84      49.491  35.581  36.989  1.00 24.74           O  
-ATOM   2064  CB  VAL B  84      49.314  38.569  35.510  1.00 26.56           C  
-ATOM   2065  CG1 VAL B  84      47.885  38.095  35.832  1.00 25.83           C  
-ATOM   2066  CG2 VAL B  84      49.474  40.030  35.887  1.00 26.28           C  
-ATOM   2067  N   VAL B  85      50.286  35.719  34.890  1.00 24.09           N  
-ATOM   2068  CA  VAL B  85      49.993  34.323  34.584  1.00 23.30           C  
-ATOM   2069  C   VAL B  85      50.806  33.380  35.470  1.00 25.35           C  
-ATOM   2070  O   VAL B  85      50.278  32.400  35.996  1.00 25.74           O  
-ATOM   2071  CB  VAL B  85      50.271  34.013  33.089  1.00 24.14           C  
-ATOM   2072  CG1 VAL B  85      50.006  32.536  32.788  1.00 22.95           C  
-ATOM   2073  CG2 VAL B  85      49.380  34.883  32.209  1.00 22.85           C  
-ATOM   2074  N   VAL B  86      52.089  33.676  35.648  1.00 24.62           N  
-ATOM   2075  CA  VAL B  86      52.939  32.830  36.479  1.00 26.50           C  
-ATOM   2076  C   VAL B  86      52.398  32.660  37.904  1.00 25.26           C  
-ATOM   2077  O   VAL B  86      52.515  31.581  38.489  1.00 25.90           O  
-ATOM   2078  CB  VAL B  86      54.386  33.388  36.543  1.00 27.60           C  
-ATOM   2079  CG1 VAL B  86      55.190  32.658  37.608  1.00 28.35           C  
-ATOM   2080  CG2 VAL B  86      55.059  33.224  35.187  1.00 29.34           C  
-ATOM   2081  N   THR B  87      51.799  33.712  38.454  1.00 24.83           N  
-ATOM   2082  CA  THR B  87      51.270  33.647  39.816  1.00 26.38           C  
-ATOM   2083  C   THR B  87      50.118  32.652  39.965  1.00 26.38           C  
-ATOM   2084  O   THR B  87      49.730  32.316  41.082  1.00 26.04           O  
-ATOM   2085  CB  THR B  87      50.792  35.035  40.316  1.00 27.62           C  
-ATOM   2086  OG1 THR B  87      49.663  35.470  39.547  1.00 29.54           O  
-ATOM   2087  CG2 THR B  87      51.908  36.063  40.187  1.00 27.82           C  
-ATOM   2088  N   LEU B  88      49.579  32.182  38.843  1.00 26.01           N  
-ATOM   2089  CA  LEU B  88      48.470  31.226  38.859  1.00 26.99           C  
-ATOM   2090  C   LEU B  88      48.886  29.823  39.300  1.00 25.51           C  
-ATOM   2091  O   LEU B  88      48.031  28.984  39.574  1.00 23.12           O  
-ATOM   2092  CB  LEU B  88      47.827  31.133  37.468  1.00 26.95           C  
-ATOM   2093  CG  LEU B  88      46.938  32.274  36.968  1.00 29.07           C  
-ATOM   2094  CD1 LEU B  88      47.543  33.602  37.323  1.00 34.15           C  
-ATOM   2095  CD2 LEU B  88      46.766  32.160  35.457  1.00 26.75           C  
-ATOM   2096  N   ALA B  89      50.192  29.571  39.363  1.00 25.34           N  
-ATOM   2097  CA  ALA B  89      50.702  28.256  39.751  1.00 26.49           C  
-ATOM   2098  C   ALA B  89      49.991  27.664  40.970  1.00 26.73           C  
-ATOM   2099  O   ALA B  89      49.688  26.473  40.997  1.00 27.92           O  
-ATOM   2100  CB  ALA B  89      52.208  28.331  40.005  1.00 29.01           C  
-ATOM   2101  N   GLU B  90      49.727  28.494  41.974  1.00 25.82           N  
-ATOM   2102  CA  GLU B  90      49.042  28.032  43.179  1.00 26.99           C  
-ATOM   2103  C   GLU B  90      47.720  28.767  43.360  1.00 25.18           C  
-ATOM   2104  O   GLU B  90      47.616  29.964  43.071  1.00 25.03           O  
-ATOM   2105  CB  GLU B  90      49.904  28.278  44.418  1.00 29.10           C  
-ATOM   2106  CG  GLU B  90      51.311  27.727  44.338  1.00 34.62           C  
-ATOM   2107  CD  GLU B  90      52.197  28.272  45.446  1.00 39.20           C  
-ATOM   2108  OE1 GLU B  90      52.186  27.712  46.565  1.00 40.14           O  
-ATOM   2109  OE2 GLU B  90      52.893  29.279  45.196  1.00 41.80           O  
-ATOM   2110  N   ASN B  91      46.709  28.051  43.841  1.00 23.79           N  
-ATOM   2111  CA  ASN B  91      45.402  28.657  44.083  1.00 23.29           C  
-ATOM   2112  C   ASN B  91      45.487  29.654  45.221  1.00 23.26           C  
-ATOM   2113  O   ASN B  91      46.308  29.493  46.129  1.00 23.33           O  
-ATOM   2114  CB  ASN B  91      44.376  27.592  44.480  1.00 22.79           C  
-ATOM   2115  CG  ASN B  91      43.682  26.981  43.293  1.00 22.22           C  
-ATOM   2116  OD1 ASN B  91      43.083  27.689  42.479  1.00 23.71           O  
-ATOM   2117  ND2 ASN B  91      43.750  25.658  43.184  1.00 21.98           N  
-ATOM   2118  N   VAL B  92      44.656  30.690  45.173  1.00 23.54           N  
-ATOM   2119  CA  VAL B  92      44.610  31.647  46.273  1.00 23.84           C  
-ATOM   2120  C   VAL B  92      43.695  30.967  47.275  1.00 21.49           C  
-ATOM   2121  O   VAL B  92      42.992  30.015  46.924  1.00 19.77           O  
-ATOM   2122  CB  VAL B  92      43.951  32.987  45.886  1.00 27.53           C  
-ATOM   2123  CG1 VAL B  92      44.918  33.832  45.087  1.00 31.88           C  
-ATOM   2124  CG2 VAL B  92      42.671  32.724  45.104  1.00 29.36           C  
-ATOM   2125  N   SER B  93      43.693  31.449  48.510  1.00 19.71           N  
-ATOM   2126  CA  SER B  93      42.842  30.866  49.538  1.00 21.21           C  
-ATOM   2127  C   SER B  93      41.404  31.315  49.316  1.00 20.25           C  
-ATOM   2128  O   SER B  93      41.151  32.385  48.754  1.00 18.03           O  
-ATOM   2129  CB  SER B  93      43.293  31.307  50.933  1.00 22.08           C  
-ATOM   2130  OG  SER B  93      42.788  32.593  51.244  1.00 23.02           O  
-ATOM   2131  N   ARG B  94      40.467  30.492  49.767  1.00 18.93           N  
-ATOM   2132  CA  ARG B  94      39.050  30.795  49.621  1.00 18.83           C  
-ATOM   2133  C   ARG B  94      38.667  32.126  50.286  1.00 17.61           C  
-ATOM   2134  O   ARG B  94      37.913  32.910  49.709  1.00 16.25           O  
-ATOM   2135  CB  ARG B  94      38.223  29.643  50.196  1.00 18.54           C  
-ATOM   2136  CG  ARG B  94      36.725  29.733  49.942  1.00 20.38           C  
-ATOM   2137  CD  ARG B  94      36.063  28.415  50.322  1.00 20.18           C  
-ATOM   2138  NE  ARG B  94      36.420  28.014  51.680  1.00 22.30           N  
-ATOM   2139  CZ  ARG B  94      35.832  28.474  52.780  1.00 24.10           C  
-ATOM   2140  NH1 ARG B  94      34.839  29.350  52.697  1.00 22.50           N  
-ATOM   2141  NH2 ARG B  94      36.258  28.077  53.967  1.00 25.39           N  
-ATOM   2142  N   PRO B  95      39.179  32.398  51.504  1.00 17.31           N  
-ATOM   2143  CA  PRO B  95      38.851  33.658  52.186  1.00 17.72           C  
-ATOM   2144  C   PRO B  95      39.328  34.876  51.398  1.00 16.67           C  
-ATOM   2145  O   PRO B  95      38.656  35.908  51.358  1.00 18.03           O  
-ATOM   2146  CB  PRO B  95      39.577  33.531  53.526  1.00 18.22           C  
-ATOM   2147  CG  PRO B  95      39.583  32.060  53.767  1.00 21.76           C  
-ATOM   2148  CD  PRO B  95      39.928  31.502  52.403  1.00 19.73           C  
-ATOM   2149  N   GLU B  96      40.496  34.750  50.778  1.00 16.12           N  
-ATOM   2150  CA  GLU B  96      41.050  35.844  49.991  1.00 18.06           C  
-ATOM   2151  C   GLU B  96      40.218  36.097  48.730  1.00 18.59           C  
-ATOM   2152  O   GLU B  96      39.982  37.247  48.354  1.00 16.68           O  
-ATOM   2153  CB  GLU B  96      42.513  35.549  49.663  1.00 20.60           C  
-ATOM   2154  CG  GLU B  96      43.416  35.771  50.888  1.00 21.93           C  
-ATOM   2155  CD  GLU B  96      44.843  35.285  50.701  1.00 28.29           C  
-ATOM   2156  OE1 GLU B  96      45.245  35.013  49.549  1.00 34.19           O  
-ATOM   2157  OE2 GLU B  96      45.567  35.180  51.717  1.00 28.48           O  
-ATOM   2158  N   LEU B  97      39.765  35.028  48.085  1.00 15.19           N  
-ATOM   2159  CA  LEU B  97      38.925  35.171  46.894  1.00 16.97           C  
-ATOM   2160  C   LEU B  97      37.604  35.816  47.319  1.00 15.57           C  
-ATOM   2161  O   LEU B  97      37.057  36.680  46.619  1.00 15.27           O  
-ATOM   2162  CB  LEU B  97      38.644  33.798  46.266  1.00 16.01           C  
-ATOM   2163  CG  LEU B  97      37.619  33.768  45.125  1.00 18.92           C  
-ATOM   2164  CD1 LEU B  97      38.105  34.640  43.956  1.00 17.95           C  
-ATOM   2165  CD2 LEU B  97      37.412  32.314  44.667  1.00 19.66           C  
-ATOM   2166  N   LEU B  98      37.097  35.387  48.472  1.00 15.30           N  
-ATOM   2167  CA  LEU B  98      35.846  35.916  49.009  1.00 17.43           C  
-ATOM   2168  C   LEU B  98      35.935  37.417  49.293  1.00 17.17           C  
-ATOM   2169  O   LEU B  98      34.979  38.158  49.059  1.00 18.02           O  
-ATOM   2170  CB  LEU B  98      35.460  35.156  50.286  1.00 18.71           C  
-ATOM   2171  CG  LEU B  98      34.329  34.111  50.279  1.00 22.73           C  
-ATOM   2172  CD1 LEU B  98      33.944  33.715  48.882  1.00 22.10           C  
-ATOM   2173  CD2 LEU B  98      34.747  32.896  51.108  1.00 20.71           C  
-ATOM   2174  N   LEU B  99      37.071  37.876  49.803  1.00 15.96           N  
-ATOM   2175  CA  LEU B  99      37.213  39.307  50.064  1.00 16.79           C  
-ATOM   2176  C   LEU B  99      37.280  40.070  48.741  1.00 16.85           C  
-ATOM   2177  O   LEU B  99      36.623  41.100  48.570  1.00 18.73           O  
-ATOM   2178  CB  LEU B  99      38.477  39.595  50.884  1.00 17.84           C  
-ATOM   2179  CG  LEU B  99      38.632  41.083  51.223  1.00 17.85           C  
-ATOM   2180  CD1 LEU B  99      37.483  41.522  52.130  1.00 16.46           C  
-ATOM   2181  CD2 LEU B  99      39.968  41.329  51.903  1.00 18.94           C  
-ATOM   2182  N   LEU B 100      38.076  39.559  47.805  1.00 18.48           N  
-ATOM   2183  CA  LEU B 100      38.230  40.192  46.492  1.00 17.88           C  
-ATOM   2184  C   LEU B 100      36.906  40.442  45.773  1.00 19.42           C  
-ATOM   2185  O   LEU B 100      36.672  41.531  45.242  1.00 17.20           O  
-ATOM   2186  CB  LEU B 100      39.121  39.335  45.585  1.00 19.02           C  
-ATOM   2187  CG  LEU B 100      39.165  39.757  44.105  1.00 19.95           C  
-ATOM   2188  CD1 LEU B 100      39.894  41.088  43.961  1.00 20.45           C  
-ATOM   2189  CD2 LEU B 100      39.869  38.693  43.292  1.00 19.50           C  
-ATOM   2190  N   ILE B 101      36.033  39.441  45.747  1.00 16.47           N  
-ATOM   2191  CA  ILE B 101      34.772  39.618  45.047  1.00 17.76           C  
-ATOM   2192  C   ILE B 101      33.821  40.601  45.714  1.00 19.17           C  
-ATOM   2193  O   ILE B 101      32.776  40.923  45.150  1.00 19.94           O  
-ATOM   2194  CB  ILE B 101      34.050  38.264  44.805  1.00 17.89           C  
-ATOM   2195  CG1 ILE B 101      33.663  37.608  46.131  1.00 19.54           C  
-ATOM   2196  CG2 ILE B 101      34.961  37.339  43.994  1.00 17.87           C  
-ATOM   2197  CD1 ILE B 101      32.885  36.301  45.944  1.00 22.77           C  
-ATOM   2198  N   ASP B 102      34.176  41.090  46.902  1.00 20.25           N  
-ATOM   2199  CA  ASP B 102      33.329  42.071  47.578  1.00 21.75           C  
-ATOM   2200  C   ASP B 102      33.845  43.493  47.337  1.00 22.18           C  
-ATOM   2201  O   ASP B 102      33.207  44.464  47.749  1.00 22.42           O  
-ATOM   2202  CB  ASP B 102      33.267  41.823  49.090  1.00 22.17           C  
-ATOM   2203  CG  ASP B 102      32.176  42.646  49.767  1.00 26.29           C  
-ATOM   2204  OD1 ASP B 102      30.990  42.428  49.450  1.00 25.76           O  
-ATOM   2205  OD2 ASP B 102      32.500  43.510  50.613  1.00 25.28           O  
-ATOM   2206  N   ALA B 103      34.990  43.609  46.672  1.00 21.82           N  
-ATOM   2207  CA  ALA B 103      35.577  44.918  46.385  1.00 23.26           C  
-ATOM   2208  C   ALA B 103      34.599  45.875  45.700  1.00 24.56           C  
-ATOM   2209  O   ALA B 103      34.592  47.070  45.994  1.00 26.64           O  
-ATOM   2210  CB  ALA B 103      36.842  44.754  45.534  1.00 21.83           C  
-ATOM   2211  N   PRO B 104      33.771  45.370  44.765  1.00 26.65           N  
-ATOM   2212  CA  PRO B 104      32.808  46.240  44.077  1.00 25.72           C  
-ATOM   2213  C   PRO B 104      31.780  46.887  45.010  1.00 27.79           C  
-ATOM   2214  O   PRO B 104      31.047  47.790  44.600  1.00 26.53           O  
-ATOM   2215  CB  PRO B 104      32.145  45.294  43.073  1.00 26.07           C  
-ATOM   2216  CG  PRO B 104      33.241  44.333  42.744  1.00 24.16           C  
-ATOM   2217  CD  PRO B 104      33.827  44.045  44.115  1.00 24.85           C  
-ATOM   2218  N   SER B 105      31.711  46.421  46.255  1.00 27.54           N  
-ATOM   2219  CA  SER B 105      30.749  46.969  47.213  1.00 28.38           C  
-ATOM   2220  C   SER B 105      31.036  48.423  47.598  1.00 28.89           C  
-ATOM   2221  O   SER B 105      30.172  49.104  48.153  1.00 29.58           O  
-ATOM   2222  CB  SER B 105      30.709  46.116  48.485  1.00 28.14           C  
-ATOM   2223  OG  SER B 105      31.914  46.242  49.220  1.00 30.92           O  
-ATOM   2224  N   HIS B 106      32.244  48.900  47.315  1.00 28.27           N  
-ATOM   2225  CA  HIS B 106      32.595  50.280  47.649  1.00 30.33           C  
-ATOM   2226  C   HIS B 106      33.758  50.786  46.804  1.00 29.43           C  
-ATOM   2227  O   HIS B 106      34.711  50.051  46.531  1.00 29.41           O  
-ATOM   2228  CB  HIS B 106      32.953  50.397  49.134  1.00 31.61           C  
-ATOM   2229  CG  HIS B 106      33.031  51.810  49.628  1.00 34.69           C  
-ATOM   2230  ND1 HIS B 106      32.002  52.417  50.317  1.00 35.78           N  
-ATOM   2231  CD2 HIS B 106      34.008  52.741  49.515  1.00 33.94           C  
-ATOM   2232  CE1 HIS B 106      32.342  53.660  50.609  1.00 35.44           C  
-ATOM   2233  NE2 HIS B 106      33.555  53.882  50.132  1.00 37.76           N  
-ATOM   2234  N   PRO B 107      33.698  52.059  46.377  1.00 29.54           N  
-ATOM   2235  CA  PRO B 107      34.764  52.640  45.556  1.00 28.56           C  
-ATOM   2236  C   PRO B 107      36.140  52.578  46.202  1.00 27.38           C  
-ATOM   2237  O   PRO B 107      37.142  52.387  45.516  1.00 29.92           O  
-ATOM   2238  CB  PRO B 107      34.292  54.078  45.341  1.00 29.44           C  
-ATOM   2239  CG  PRO B 107      32.807  53.944  45.360  1.00 30.95           C  
-ATOM   2240  CD  PRO B 107      32.578  53.006  46.524  1.00 28.69           C  
-ATOM   2241  N   ASP B 108      36.195  52.746  47.520  1.00 27.25           N  
-ATOM   2242  CA  ASP B 108      37.473  52.701  48.216  1.00 27.14           C  
-ATOM   2243  C   ASP B 108      38.140  51.337  48.089  1.00 26.03           C  
-ATOM   2244  O   ASP B 108      39.359  51.245  47.963  1.00 24.04           O  
-ATOM   2245  CB  ASP B 108      37.303  53.038  49.700  1.00 28.79           C  
-ATOM   2246  CG  ASP B 108      36.859  54.472  49.928  1.00 33.15           C  
-ATOM   2247  OD1 ASP B 108      37.215  55.336  49.100  1.00 32.71           O  
-ATOM   2248  OD2 ASP B 108      36.169  54.732  50.937  1.00 34.34           O  
-ATOM   2249  N   PHE B 109      37.341  50.276  48.128  1.00 26.23           N  
-ATOM   2250  CA  PHE B 109      37.902  48.933  48.022  1.00 25.68           C  
-ATOM   2251  C   PHE B 109      38.431  48.722  46.610  1.00 25.52           C  
-ATOM   2252  O   PHE B 109      39.544  48.235  46.418  1.00 25.87           O  
-ATOM   2253  CB  PHE B 109      36.843  47.887  48.380  1.00 25.33           C  
-ATOM   2254  CG  PHE B 109      36.210  48.108  49.729  1.00 25.64           C  
-ATOM   2255  CD1 PHE B 109      36.913  48.754  50.749  1.00 24.74           C  
-ATOM   2256  CD2 PHE B 109      34.917  47.666  49.986  1.00 24.91           C  
-ATOM   2257  CE1 PHE B 109      36.333  48.956  52.000  1.00 24.04           C  
-ATOM   2258  CE2 PHE B 109      34.325  47.861  51.236  1.00 24.99           C  
-ATOM   2259  CZ  PHE B 109      35.035  48.509  52.246  1.00 26.78           C  
-ATOM   2260  N   LEU B 110      37.631  49.102  45.622  1.00 27.30           N  
-ATOM   2261  CA  LEU B 110      38.039  48.988  44.230  1.00 29.83           C  
-ATOM   2262  C   LEU B 110      39.362  49.735  44.046  1.00 29.78           C  
-ATOM   2263  O   LEU B 110      40.303  49.225  43.441  1.00 30.27           O  
-ATOM   2264  CB  LEU B 110      36.966  49.604  43.328  1.00 31.06           C  
-ATOM   2265  CG  LEU B 110      36.008  48.704  42.535  1.00 33.12           C  
-ATOM   2266  CD1 LEU B 110      35.877  47.344  43.173  1.00 33.25           C  
-ATOM   2267  CD2 LEU B 110      34.655  49.395  42.421  1.00 31.78           C  
-ATOM   2268  N   ASN B 111      39.422  50.949  44.584  1.00 31.46           N  
-ATOM   2269  CA  ASN B 111      40.615  51.780  44.477  1.00 31.60           C  
-ATOM   2270  C   ASN B 111      41.861  51.100  45.047  1.00 30.54           C  
-ATOM   2271  O   ASN B 111      42.950  51.219  44.491  1.00 31.00           O  
-ATOM   2272  CB  ASN B 111      40.378  53.115  45.187  1.00 33.18           C  
-ATOM   2273  CG  ASN B 111      41.523  54.084  44.994  1.00 35.51           C  
-ATOM   2274  OD1 ASN B 111      41.852  54.455  43.868  1.00 36.43           O  
-ATOM   2275  ND2 ASN B 111      42.141  54.499  46.096  1.00 35.65           N  
-ATOM   2276  N   ALA B 112      41.699  50.381  46.154  1.00 30.04           N  
-ATOM   2277  CA  ALA B 112      42.824  49.688  46.772  1.00 28.94           C  
-ATOM   2278  C   ALA B 112      43.448  48.703  45.791  1.00 28.43           C  
-ATOM   2279  O   ALA B 112      44.659  48.475  45.808  1.00 27.92           O  
-ATOM   2280  CB  ALA B 112      42.364  48.952  48.028  1.00 28.93           C  
-ATOM   2281  N   TRP B 113      42.621  48.127  44.924  1.00 28.36           N  
-ATOM   2282  CA  TRP B 113      43.117  47.161  43.950  1.00 28.77           C  
-ATOM   2283  C   TRP B 113      43.663  47.765  42.657  1.00 31.37           C  
-ATOM   2284  O   TRP B 113      44.620  47.244  42.089  1.00 32.01           O  
-ATOM   2285  CB  TRP B 113      42.023  46.144  43.606  1.00 25.89           C  
-ATOM   2286  CG  TRP B 113      41.683  45.231  44.750  1.00 21.95           C  
-ATOM   2287  CD1 TRP B 113      40.660  45.375  45.647  1.00 22.45           C  
-ATOM   2288  CD2 TRP B 113      42.385  44.044  45.127  1.00 22.16           C  
-ATOM   2289  NE1 TRP B 113      40.684  44.345  46.563  1.00 21.27           N  
-ATOM   2290  CE2 TRP B 113      41.731  43.514  46.266  1.00 20.88           C  
-ATOM   2291  CE3 TRP B 113      43.502  43.375  44.616  1.00 21.79           C  
-ATOM   2292  CZ2 TRP B 113      42.160  42.345  46.899  1.00 21.75           C  
-ATOM   2293  CZ3 TRP B 113      43.930  42.209  45.249  1.00 23.53           C  
-ATOM   2294  CH2 TRP B 113      43.257  41.709  46.378  1.00 22.04           C  
-ATOM   2295  N   ARG B 114      43.063  48.852  42.187  1.00 35.86           N  
-ATOM   2296  CA  ARG B 114      43.529  49.468  40.944  1.00 39.58           C  
-ATOM   2297  C   ARG B 114      44.996  49.863  41.061  1.00 39.70           C  
-ATOM   2298  O   ARG B 114      45.769  49.722  40.114  1.00 39.25           O  
-ATOM   2299  CB  ARG B 114      42.704  50.709  40.604  1.00 41.95           C  
-ATOM   2300  CG  ARG B 114      43.017  51.916  41.473  1.00 47.79           C  
-ATOM   2301  CD  ARG B 114      42.627  53.213  40.780  1.00 51.02           C  
-ATOM   2302  NE  ARG B 114      42.929  54.382  41.603  1.00 55.04           N  
-ATOM   2303  CZ  ARG B 114      44.152  54.738  41.987  1.00 56.17           C  
-ATOM   2304  NH1 ARG B 114      45.205  54.018  41.621  1.00 56.97           N  
-ATOM   2305  NH2 ARG B 114      44.322  55.813  42.747  1.00 57.72           N  
-ATOM   2306  N   THR B 115      45.364  50.351  42.240  1.00 41.94           N  
-ATOM   2307  CA  THR B 115      46.724  50.789  42.524  1.00 44.81           C  
-ATOM   2308  C   THR B 115      47.769  49.766  42.101  1.00 46.00           C  
-ATOM   2309  O   THR B 115      48.883  50.130  41.720  1.00 45.72           O  
-ATOM   2310  CB  THR B 115      46.901  51.073  44.029  1.00 45.31           C  
-ATOM   2311  OG1 THR B 115      45.844  51.927  44.482  1.00 44.72           O  
-ATOM   2312  CG2 THR B 115      48.240  51.751  44.291  1.00 45.82           C  
-ATOM   2313  N   VAL B 116      47.408  48.487  42.176  1.00 47.02           N  
-ATOM   2314  CA  VAL B 116      48.322  47.413  41.806  1.00 47.69           C  
-ATOM   2315  C   VAL B 116      48.013  46.859  40.421  1.00 47.63           C  
-ATOM   2316  O   VAL B 116      48.927  46.590  39.640  1.00 50.01           O  
-ATOM   2317  CB  VAL B 116      48.272  46.244  42.829  1.00 48.69           C  
-ATOM   2318  CG1 VAL B 116      46.906  45.573  42.799  1.00 49.34           C  
-ATOM   2319  CG2 VAL B 116      49.362  45.235  42.519  1.00 48.39           C  
-ATOM   2320  N   ASN B 117      46.727  46.701  40.117  1.00 45.50           N  
-ATOM   2321  CA  ASN B 117      46.298  46.168  38.830  1.00 44.17           C  
-ATOM   2322  C   ASN B 117      46.717  47.021  37.640  1.00 45.14           C  
-ATOM   2323  O   ASN B 117      47.040  46.491  36.578  1.00 45.66           O  
-ATOM   2324  CB  ASN B 117      44.776  46.002  38.797  1.00 42.62           C  
-ATOM   2325  CG  ASN B 117      44.269  45.032  39.850  1.00 42.66           C  
-ATOM   2326  OD1 ASN B 117      44.994  44.134  40.287  1.00 41.59           O  
-ATOM   2327  ND2 ASN B 117      43.013  45.199  40.249  1.00 37.67           N  
-ATOM   2328  N   HIS B 118      46.693  48.339  37.810  1.00 44.92           N  
-ATOM   2329  CA  HIS B 118      47.067  49.242  36.728  1.00 44.64           C  
-ATOM   2330  C   HIS B 118      48.508  48.999  36.305  1.00 42.69           C  
-ATOM   2331  O   HIS B 118      48.888  49.281  35.170  1.00 43.79           O  
-ATOM   2332  CB  HIS B 118      46.890  50.699  37.164  1.00 47.51           C  
-ATOM   2333  CG  HIS B 118      47.224  51.694  36.096  1.00 51.69           C  
-ATOM   2334  ND1 HIS B 118      48.515  51.921  35.666  1.00 54.01           N  
-ATOM   2335  CD2 HIS B 118      46.433  52.504  35.351  1.00 53.45           C  
-ATOM   2336  CE1 HIS B 118      48.504  52.826  34.703  1.00 54.26           C  
-ATOM   2337  NE2 HIS B 118      47.254  53.196  34.492  1.00 53.94           N  
-ATOM   2338  N   GLN B 119      49.302  48.458  37.219  1.00 41.05           N  
-ATOM   2339  CA  GLN B 119      50.708  48.189  36.948  1.00 40.29           C  
-ATOM   2340  C   GLN B 119      50.969  46.802  36.363  1.00 39.23           C  
-ATOM   2341  O   GLN B 119      52.058  46.545  35.853  1.00 39.12           O  
-ATOM   2342  CB  GLN B 119      51.522  48.340  38.236  1.00 43.44           C  
-ATOM   2343  CG  GLN B 119      51.406  49.702  38.907  1.00 47.26           C  
-ATOM   2344  CD  GLN B 119      52.000  50.814  38.067  1.00 51.61           C  
-ATOM   2345  OE1 GLN B 119      53.178  50.774  37.705  1.00 53.87           O  
-ATOM   2346  NE2 GLN B 119      51.187  51.818  37.752  1.00 53.68           N  
-ATOM   2347  N   TRP B 120      49.983  45.909  36.419  1.00 35.78           N  
-ATOM   2348  CA  TRP B 120      50.200  44.556  35.917  1.00 32.30           C  
-ATOM   2349  C   TRP B 120      49.158  43.971  34.972  1.00 30.84           C  
-ATOM   2350  O   TRP B 120      49.508  43.280  34.020  1.00 28.36           O  
-ATOM   2351  CB  TRP B 120      50.376  43.595  37.092  1.00 31.63           C  
-ATOM   2352  CG  TRP B 120      51.457  43.998  38.036  1.00 32.01           C  
-ATOM   2353  CD1 TRP B 120      51.331  44.792  39.141  1.00 30.80           C  
-ATOM   2354  CD2 TRP B 120      52.835  43.628  37.961  1.00 32.34           C  
-ATOM   2355  NE1 TRP B 120      52.549  44.936  39.761  1.00 32.53           N  
-ATOM   2356  CE2 TRP B 120      53.491  44.231  39.058  1.00 33.59           C  
-ATOM   2357  CE3 TRP B 120      53.583  42.842  37.072  1.00 32.37           C  
-ATOM   2358  CZ2 TRP B 120      54.862  44.072  39.292  1.00 33.56           C  
-ATOM   2359  CZ3 TRP B 120      54.948  42.683  37.306  1.00 33.00           C  
-ATOM   2360  CH2 TRP B 120      55.571  43.296  38.409  1.00 33.38           C  
-ATOM   2361  N   ILE B 121      47.883  44.215  35.248  1.00 29.79           N  
-ATOM   2362  CA  ILE B 121      46.826  43.679  34.400  1.00 29.42           C  
-ATOM   2363  C   ILE B 121      46.587  44.592  33.200  1.00 29.52           C  
-ATOM   2364  O   ILE B 121      46.423  45.797  33.354  1.00 27.60           O  
-ATOM   2365  CB  ILE B 121      45.518  43.506  35.203  1.00 27.87           C  
-ATOM   2366  CG1 ILE B 121      45.723  42.435  36.280  1.00 26.31           C  
-ATOM   2367  CG2 ILE B 121      44.372  43.127  34.273  1.00 26.59           C  
-ATOM   2368  CD1 ILE B 121      44.536  42.255  37.212  1.00 25.24           C  
-ATOM   2369  N   PRO B 122      46.569  44.019  31.984  1.00 30.95           N  
-ATOM   2370  CA  PRO B 122      46.352  44.785  30.751  1.00 32.20           C  
-ATOM   2371  C   PRO B 122      45.070  45.597  30.812  1.00 32.70           C  
-ATOM   2372  O   PRO B 122      44.083  45.161  31.404  1.00 31.92           O  
-ATOM   2373  CB  PRO B 122      46.269  43.703  29.673  1.00 33.38           C  
-ATOM   2374  CG  PRO B 122      47.062  42.568  30.251  1.00 33.83           C  
-ATOM   2375  CD  PRO B 122      46.649  42.578  31.696  1.00 31.38           C  
-ATOM   2376  N   ASP B 123      45.086  46.780  30.207  1.00 32.47           N  
-ATOM   2377  CA  ASP B 123      43.897  47.613  30.184  1.00 32.66           C  
-ATOM   2378  C   ASP B 123      43.110  47.207  28.948  1.00 32.37           C  
-ATOM   2379  O   ASP B 123      43.577  46.398  28.149  1.00 33.41           O  
-ATOM   2380  CB  ASP B 123      44.274  49.095  30.117  1.00 34.22           C  
-ATOM   2381  CG  ASP B 123      45.109  49.428  28.899  1.00 35.52           C  
-ATOM   2382  OD1 ASP B 123      44.589  49.317  27.770  1.00 33.89           O  
-ATOM   2383  OD2 ASP B 123      46.289  49.794  29.075  1.00 37.48           O  
-ATOM   2384  N   THR B 124      41.916  47.759  28.792  1.00 32.88           N  
-ATOM   2385  CA  THR B 124      41.086  47.432  27.644  1.00 34.44           C  
-ATOM   2386  C   THR B 124      40.921  48.636  26.716  1.00 35.89           C  
-ATOM   2387  O   THR B 124      39.971  48.701  25.935  1.00 33.82           O  
-ATOM   2388  CB  THR B 124      39.697  46.975  28.097  1.00 33.70           C  
-ATOM   2389  OG1 THR B 124      38.925  46.578  26.958  1.00 40.18           O  
-ATOM   2390  CG2 THR B 124      38.989  48.104  28.807  1.00 28.41           C  
-ATOM   2391  N   ASP B 125      41.842  49.591  26.808  1.00 38.26           N  
-ATOM   2392  CA  ASP B 125      41.762  50.780  25.967  1.00 40.34           C  
-ATOM   2393  C   ASP B 125      41.822  50.415  24.491  1.00 39.70           C  
-ATOM   2394  O   ASP B 125      42.720  49.691  24.060  1.00 39.20           O  
-ATOM   2395  CB  ASP B 125      42.906  51.753  26.279  1.00 43.26           C  
-ATOM   2396  CG  ASP B 125      42.941  52.173  27.734  1.00 45.18           C  
-ATOM   2397  OD1 ASP B 125      41.861  52.339  28.340  1.00 47.43           O  
-ATOM   2398  OD2 ASP B 125      44.053  52.355  28.270  1.00 48.90           O  
-ATOM   2399  N   ASP B 126      40.853  50.912  23.727  1.00 39.94           N  
-ATOM   2400  CA  ASP B 126      40.798  50.680  22.286  1.00 40.50           C  
-ATOM   2401  C   ASP B 126      40.564  49.212  21.936  1.00 40.26           C  
-ATOM   2402  O   ASP B 126      40.902  48.766  20.837  1.00 38.67           O  
-ATOM   2403  CB  ASP B 126      42.106  51.162  21.646  1.00 42.69           C  
-ATOM   2404  CG  ASP B 126      41.901  51.748  20.262  1.00 44.85           C  
-ATOM   2405  OD1 ASP B 126      42.913  52.001  19.577  1.00 46.54           O  
-ATOM   2406  OD2 ASP B 126      40.736  51.963  19.862  1.00 45.89           O  
-ATOM   2407  N   LEU B 127      39.975  48.475  22.874  1.00 39.13           N  
-ATOM   2408  CA  LEU B 127      39.693  47.049  22.710  1.00 38.16           C  
-ATOM   2409  C   LEU B 127      38.990  46.688  21.400  1.00 36.91           C  
-ATOM   2410  O   LEU B 127      39.429  45.797  20.674  1.00 33.25           O  
-ATOM   2411  CB  LEU B 127      38.846  46.559  23.895  1.00 39.33           C  
-ATOM   2412  CG  LEU B 127      38.678  45.061  24.185  1.00 40.81           C  
-ATOM   2413  CD1 LEU B 127      37.970  44.366  23.038  1.00 41.66           C  
-ATOM   2414  CD2 LEU B 127      40.038  44.440  24.438  1.00 41.08           C  
-ATOM   2415  N   GLU B 128      37.893  47.374  21.103  1.00 37.63           N  
-ATOM   2416  CA  GLU B 128      37.133  47.087  19.891  1.00 39.62           C  
-ATOM   2417  C   GLU B 128      37.809  47.529  18.590  1.00 39.15           C  
-ATOM   2418  O   GLU B 128      37.322  47.217  17.506  1.00 39.05           O  
-ATOM   2419  CB  GLU B 128      35.748  47.735  19.973  1.00 40.61           C  
-ATOM   2420  CG  GLU B 128      34.999  47.478  21.272  1.00 42.92           C  
-ATOM   2421  CD  GLU B 128      35.239  48.561  22.310  1.00 44.54           C  
-ATOM   2422  OE1 GLU B 128      36.408  48.782  22.696  1.00 46.12           O  
-ATOM   2423  OE2 GLU B 128      34.252  49.195  22.739  1.00 43.60           O  
-ATOM   2424  N   ASN B 129      38.932  48.235  18.692  1.00 39.37           N  
-ATOM   2425  CA  ASN B 129      39.624  48.723  17.498  1.00 39.40           C  
-ATOM   2426  C   ASN B 129      41.029  48.168  17.312  1.00 39.14           C  
-ATOM   2427  O   ASN B 129      41.691  48.462  16.315  1.00 38.54           O  
-ATOM   2428  CB  ASN B 129      39.708  50.248  17.538  1.00 40.16           C  
-ATOM   2429  CG  ASN B 129      38.369  50.892  17.798  1.00 42.21           C  
-ATOM   2430  OD1 ASN B 129      37.409  50.668  17.060  1.00 42.41           O  
-ATOM   2431  ND2 ASN B 129      38.293  51.695  18.853  1.00 42.83           N  
-ATOM   2432  N   ASP B 130      41.485  47.373  18.272  1.00 36.69           N  
-ATOM   2433  CA  ASP B 130      42.821  46.801  18.207  1.00 35.63           C  
-ATOM   2434  C   ASP B 130      42.717  45.289  18.368  1.00 35.89           C  
-ATOM   2435  O   ASP B 130      42.434  44.788  19.460  1.00 36.20           O  
-ATOM   2436  CB  ASP B 130      43.685  47.399  19.320  1.00 33.99           C  
-ATOM   2437  CG  ASP B 130      45.148  47.033  19.189  1.00 34.78           C  
-ATOM   2438  OD1 ASP B 130      45.450  45.876  18.831  1.00 35.52           O  
-ATOM   2439  OD2 ASP B 130      46.003  47.902  19.463  1.00 35.94           O  
-ATOM   2440  N   ALA B 131      42.935  44.566  17.274  1.00 34.26           N  
-ATOM   2441  CA  ALA B 131      42.858  43.111  17.289  1.00 33.65           C  
-ATOM   2442  C   ALA B 131      43.924  42.537  18.213  1.00 32.88           C  
-ATOM   2443  O   ALA B 131      43.734  41.482  18.825  1.00 31.31           O  
-ATOM   2444  CB  ALA B 131      43.032  42.565  15.874  1.00 33.64           C  
-ATOM   2445  N   HIS B 132      45.049  43.237  18.307  1.00 31.31           N  
-ATOM   2446  CA  HIS B 132      46.144  42.812  19.166  1.00 31.21           C  
-ATOM   2447  C   HIS B 132      45.715  42.994  20.619  1.00 31.00           C  
-ATOM   2448  O   HIS B 132      46.031  42.171  21.476  1.00 30.44           O  
-ATOM   2449  CB  HIS B 132      47.398  43.637  18.856  1.00 30.15           C  
-ATOM   2450  CG  HIS B 132      48.536  43.401  19.799  1.00 28.66           C  
-ATOM   2451  ND1 HIS B 132      48.753  44.185  20.912  1.00 28.87           N  
-ATOM   2452  CD2 HIS B 132      49.521  42.473  19.795  1.00 28.52           C  
-ATOM   2453  CE1 HIS B 132      49.825  43.751  21.551  1.00 28.27           C  
-ATOM   2454  NE2 HIS B 132      50.310  42.713  20.894  1.00 30.03           N  
-ATOM   2455  N   LYS B 133      44.980  44.070  20.881  1.00 31.25           N  
-ATOM   2456  CA  LYS B 133      44.490  44.358  22.225  1.00 31.12           C  
-ATOM   2457  C   LYS B 133      43.537  43.259  22.690  1.00 30.32           C  
-ATOM   2458  O   LYS B 133      43.539  42.879  23.864  1.00 27.24           O  
-ATOM   2459  CB  LYS B 133      43.774  45.713  22.249  1.00 32.47           C  
-ATOM   2460  CG  LYS B 133      42.994  45.999  23.530  1.00 36.45           C  
-ATOM   2461  CD  LYS B 133      43.874  45.975  24.773  1.00 38.79           C  
-ATOM   2462  CE  LYS B 133      44.885  47.110  24.786  1.00 40.90           C  
-ATOM   2463  NZ  LYS B 133      45.752  47.043  26.001  1.00 42.04           N  
-ATOM   2464  N   ARG B 134      42.721  42.754  21.769  1.00 28.98           N  
-ATOM   2465  CA  ARG B 134      41.781  41.692  22.103  1.00 28.78           C  
-ATOM   2466  C   ARG B 134      42.531  40.383  22.342  1.00 28.17           C  
-ATOM   2467  O   ARG B 134      42.160  39.596  23.218  1.00 27.65           O  
-ATOM   2468  CB  ARG B 134      40.744  41.517  20.984  1.00 30.08           C  
-ATOM   2469  CG  ARG B 134      39.829  42.731  20.794  1.00 31.07           C  
-ATOM   2470  CD  ARG B 134      38.651  42.417  19.877  1.00 30.77           C  
-ATOM   2471  NE  ARG B 134      39.060  42.200  18.491  1.00 30.84           N  
-ATOM   2472  CZ  ARG B 134      39.349  43.173  17.632  1.00 32.93           C  
-ATOM   2473  NH1 ARG B 134      39.276  44.445  18.008  1.00 29.56           N  
-ATOM   2474  NH2 ARG B 134      39.707  42.874  16.391  1.00 33.60           N  
-ATOM   2475  N   ALA B 135      43.588  40.155  21.568  1.00 26.46           N  
-ATOM   2476  CA  ALA B 135      44.395  38.948  21.712  1.00 26.33           C  
-ATOM   2477  C   ALA B 135      45.092  38.959  23.076  1.00 27.05           C  
-ATOM   2478  O   ALA B 135      45.259  37.912  23.712  1.00 25.03           O  
-ATOM   2479  CB  ALA B 135      45.431  38.874  20.591  1.00 28.01           C  
-ATOM   2480  N   VAL B 136      45.499  40.148  23.516  1.00 25.50           N  
-ATOM   2481  CA  VAL B 136      46.163  40.300  24.807  1.00 25.69           C  
-ATOM   2482  C   VAL B 136      45.161  40.108  25.947  1.00 25.64           C  
-ATOM   2483  O   VAL B 136      45.463  39.444  26.945  1.00 25.61           O  
-ATOM   2484  CB  VAL B 136      46.827  41.699  24.952  1.00 27.09           C  
-ATOM   2485  CG1 VAL B 136      47.274  41.926  26.402  1.00 24.73           C  
-ATOM   2486  CG2 VAL B 136      48.035  41.803  24.023  1.00 25.65           C  
-ATOM   2487  N   TYR B 137      43.966  40.671  25.801  1.00 22.27           N  
-ATOM   2488  CA  TYR B 137      42.974  40.529  26.857  1.00 24.64           C  
-ATOM   2489  C   TYR B 137      42.404  39.116  26.904  1.00 24.26           C  
-ATOM   2490  O   TYR B 137      41.852  38.696  27.929  1.00 23.27           O  
-ATOM   2491  CB  TYR B 137      41.841  41.544  26.697  1.00 24.42           C  
-ATOM   2492  CG  TYR B 137      41.314  42.006  28.032  1.00 25.31           C  
-ATOM   2493  CD1 TYR B 137      42.118  42.753  28.894  1.00 25.33           C  
-ATOM   2494  CD2 TYR B 137      40.040  41.643  28.466  1.00 26.09           C  
-ATOM   2495  CE1 TYR B 137      41.671  43.124  30.162  1.00 24.80           C  
-ATOM   2496  CE2 TYR B 137      39.581  42.009  29.734  1.00 25.77           C  
-ATOM   2497  CZ  TYR B 137      40.403  42.745  30.573  1.00 25.65           C  
-ATOM   2498  OH  TYR B 137      39.966  43.083  31.828  1.00 25.34           O  
-ATOM   2499  N   LEU B 138      42.535  38.386  25.798  1.00 22.40           N  
-ATOM   2500  CA  LEU B 138      42.059  37.006  25.741  1.00 23.19           C  
-ATOM   2501  C   LEU B 138      42.923  36.215  26.719  1.00 23.37           C  
-ATOM   2502  O   LEU B 138      42.444  35.312  27.412  1.00 21.62           O  
-ATOM   2503  CB  LEU B 138      42.213  36.432  24.327  1.00 23.81           C  
-ATOM   2504  CG  LEU B 138      41.837  34.956  24.159  1.00 24.22           C  
-ATOM   2505  CD1 LEU B 138      40.347  34.769  24.445  1.00 24.12           C  
-ATOM   2506  CD2 LEU B 138      42.177  34.493  22.744  1.00 24.94           C  
-ATOM   2507  N   VAL B 139      44.207  36.561  26.765  1.00 23.36           N  
-ATOM   2508  CA  VAL B 139      45.133  35.910  27.680  1.00 21.52           C  
-ATOM   2509  C   VAL B 139      44.679  36.211  29.103  1.00 21.84           C  
-ATOM   2510  O   VAL B 139      44.627  35.319  29.953  1.00 21.11           O  
-ATOM   2511  CB  VAL B 139      46.573  36.442  27.513  1.00 22.88           C  
-ATOM   2512  CG1 VAL B 139      47.486  35.788  28.545  1.00 22.10           C  
-ATOM   2513  CG2 VAL B 139      47.080  36.163  26.097  1.00 23.03           C  
-ATOM   2514  N   GLN B 140      44.352  37.475  29.361  1.00 22.66           N  
-ATOM   2515  CA  GLN B 140      43.910  37.886  30.689  1.00 23.19           C  
-ATOM   2516  C   GLN B 140      42.656  37.122  31.107  1.00 23.48           C  
-ATOM   2517  O   GLN B 140      42.535  36.687  32.254  1.00 22.33           O  
-ATOM   2518  CB  GLN B 140      43.639  39.392  30.720  1.00 23.67           C  
-ATOM   2519  CG  GLN B 140      43.275  39.935  32.100  1.00 23.19           C  
-ATOM   2520  CD  GLN B 140      44.312  39.588  33.158  1.00 24.30           C  
-ATOM   2521  OE1 GLN B 140      45.510  39.808  32.969  1.00 22.72           O  
-ATOM   2522  NE2 GLN B 140      43.853  39.046  34.281  1.00 21.37           N  
-ATOM   2523  N   LEU B 141      41.728  36.957  30.168  1.00 21.79           N  
-ATOM   2524  CA  LEU B 141      40.488  36.239  30.435  1.00 21.72           C  
-ATOM   2525  C   LEU B 141      40.782  34.771  30.768  1.00 21.22           C  
-ATOM   2526  O   LEU B 141      40.159  34.191  31.665  1.00 21.03           O  
-ATOM   2527  CB  LEU B 141      39.557  36.352  29.221  1.00 23.79           C  
-ATOM   2528  CG  LEU B 141      38.216  37.088  29.372  1.00 27.03           C  
-ATOM   2529  CD1 LEU B 141      38.319  38.272  30.322  1.00 25.49           C  
-ATOM   2530  CD2 LEU B 141      37.738  37.533  27.997  1.00 23.73           C  
-ATOM   2531  N   ALA B 142      41.734  34.172  30.060  1.00 19.62           N  
-ATOM   2532  CA  ALA B 142      42.091  32.785  30.322  1.00 20.77           C  
-ATOM   2533  C   ALA B 142      42.732  32.709  31.706  1.00 20.23           C  
-ATOM   2534  O   ALA B 142      42.512  31.757  32.447  1.00 17.76           O  
-ATOM   2535  CB  ALA B 142      43.058  32.271  29.260  1.00 20.69           C  
-ATOM   2536  N   ALA B 143      43.518  33.726  32.053  1.00 19.86           N  
-ATOM   2537  CA  ALA B 143      44.162  33.767  33.362  1.00 20.23           C  
-ATOM   2538  C   ALA B 143      43.085  33.901  34.438  1.00 19.82           C  
-ATOM   2539  O   ALA B 143      43.153  33.243  35.476  1.00 20.12           O  
-ATOM   2540  CB  ALA B 143      45.141  34.940  33.439  1.00 20.98           C  
-ATOM   2541  N   ASP B 144      42.096  34.758  34.187  1.00 18.66           N  
-ATOM   2542  CA  ASP B 144      40.993  34.953  35.126  1.00 18.72           C  
-ATOM   2543  C   ASP B 144      40.319  33.601  35.379  1.00 19.33           C  
-ATOM   2544  O   ASP B 144      39.974  33.260  36.515  1.00 20.35           O  
-ATOM   2545  CB  ASP B 144      39.957  35.930  34.552  1.00 18.60           C  
-ATOM   2546  CG  ASP B 144      40.438  37.375  34.555  1.00 21.35           C  
-ATOM   2547  OD1 ASP B 144      41.468  37.663  35.199  1.00 18.42           O  
-ATOM   2548  OD2 ASP B 144      39.767  38.226  33.926  1.00 21.71           O  
-ATOM   2549  N   GLY B 145      40.140  32.837  34.307  1.00 18.75           N  
-ATOM   2550  CA  GLY B 145      39.518  31.529  34.417  1.00 20.27           C  
-ATOM   2551  C   GLY B 145      40.318  30.542  35.254  1.00 19.88           C  
-ATOM   2552  O   GLY B 145      39.761  29.868  36.124  1.00 19.30           O  
-ATOM   2553  N   LEU B 146      41.622  30.446  35.007  1.00 18.95           N  
-ATOM   2554  CA  LEU B 146      42.448  29.512  35.765  1.00 19.48           C  
-ATOM   2555  C   LEU B 146      42.460  29.902  37.237  1.00 19.40           C  
-ATOM   2556  O   LEU B 146      42.528  29.048  38.119  1.00 19.98           O  
-ATOM   2557  CB  LEU B 146      43.881  29.491  35.217  1.00 20.22           C  
-ATOM   2558  CG  LEU B 146      44.794  28.395  35.787  1.00 21.70           C  
-ATOM   2559  CD1 LEU B 146      44.129  27.039  35.628  1.00 21.49           C  
-ATOM   2560  CD2 LEU B 146      46.143  28.418  35.065  1.00 22.21           C  
-ATOM   2561  N   PHE B 147      42.393  31.206  37.486  1.00 19.03           N  
-ATOM   2562  CA  PHE B 147      42.385  31.759  38.836  1.00 20.34           C  
-ATOM   2563  C   PHE B 147      41.193  31.231  39.647  1.00 20.53           C  
-ATOM   2564  O   PHE B 147      41.351  30.827  40.799  1.00 22.69           O  
-ATOM   2565  CB  PHE B 147      42.343  33.293  38.745  1.00 20.57           C  
-ATOM   2566  CG  PHE B 147      42.093  33.983  40.056  1.00 22.70           C  
-ATOM   2567  CD1 PHE B 147      42.999  33.868  41.110  1.00 21.35           C  
-ATOM   2568  CD2 PHE B 147      40.954  34.761  40.233  1.00 20.45           C  
-ATOM   2569  CE1 PHE B 147      42.771  34.520  42.320  1.00 22.32           C  
-ATOM   2570  CE2 PHE B 147      40.716  35.418  41.442  1.00 22.86           C  
-ATOM   2571  CZ  PHE B 147      41.629  35.296  42.488  1.00 22.50           C  
-ATOM   2572  N   VAL B 148      40.005  31.214  39.046  1.00 21.59           N  
-ATOM   2573  CA  VAL B 148      38.816  30.737  39.758  1.00 21.36           C  
-ATOM   2574  C   VAL B 148      38.429  29.287  39.461  1.00 21.79           C  
-ATOM   2575  O   VAL B 148      37.531  28.740  40.106  1.00 19.44           O  
-ATOM   2576  CB  VAL B 148      37.579  31.610  39.441  1.00 22.69           C  
-ATOM   2577  CG1 VAL B 148      37.838  33.055  39.849  1.00 21.11           C  
-ATOM   2578  CG2 VAL B 148      37.229  31.515  37.948  1.00 20.94           C  
-ATOM   2579  N   HIS B 149      39.111  28.664  38.505  1.00 19.45           N  
-ATOM   2580  CA  HIS B 149      38.785  27.302  38.099  1.00 19.94           C  
-ATOM   2581  C   HIS B 149      38.415  26.302  39.191  1.00 21.17           C  
-ATOM   2582  O   HIS B 149      37.313  25.750  39.177  1.00 20.38           O  
-ATOM   2583  CB  HIS B 149      39.914  26.705  37.262  1.00 19.76           C  
-ATOM   2584  CG  HIS B 149      39.612  25.332  36.745  1.00 21.76           C  
-ATOM   2585  ND1 HIS B 149      39.678  24.205  37.537  1.00 21.52           N  
-ATOM   2586  CD2 HIS B 149      39.202  24.910  35.525  1.00 22.92           C  
-ATOM   2587  CE1 HIS B 149      39.319  23.149  36.828  1.00 21.13           C  
-ATOM   2588  NE2 HIS B 149      39.025  23.549  35.604  1.00 23.89           N  
-ATOM   2589  N   ASP B 150      39.327  26.066  40.129  1.00 20.52           N  
-ATOM   2590  CA  ASP B 150      39.082  25.087  41.186  1.00 21.37           C  
-ATOM   2591  C   ASP B 150      38.001  25.468  42.189  1.00 21.86           C  
-ATOM   2592  O   ASP B 150      37.662  24.678  43.070  1.00 18.36           O  
-ATOM   2593  CB  ASP B 150      40.390  24.760  41.909  1.00 21.63           C  
-ATOM   2594  CG  ASP B 150      41.409  24.098  40.989  1.00 24.98           C  
-ATOM   2595  OD1 ASP B 150      40.994  23.483  39.979  1.00 25.97           O  
-ATOM   2596  OD2 ASP B 150      42.617  24.185  41.279  1.00 26.01           O  
-ATOM   2597  N   TYR B 151      37.451  26.672  42.048  1.00 21.85           N  
-ATOM   2598  CA  TYR B 151      36.389  27.118  42.939  1.00 21.90           C  
-ATOM   2599  C   TYR B 151      35.017  27.067  42.263  1.00 22.71           C  
-ATOM   2600  O   TYR B 151      33.995  26.975  42.941  1.00 23.22           O  
-ATOM   2601  CB  TYR B 151      36.677  28.538  43.456  1.00 21.77           C  
-ATOM   2602  CG  TYR B 151      37.784  28.586  44.497  1.00 21.45           C  
-ATOM   2603  CD1 TYR B 151      37.604  28.023  45.763  1.00 20.83           C  
-ATOM   2604  CD2 TYR B 151      39.027  29.141  44.197  1.00 20.27           C  
-ATOM   2605  CE1 TYR B 151      38.640  28.008  46.704  1.00 20.63           C  
-ATOM   2606  CE2 TYR B 151      40.071  29.130  45.129  1.00 20.38           C  
-ATOM   2607  CZ  TYR B 151      39.869  28.558  46.381  1.00 20.50           C  
-ATOM   2608  OH  TYR B 151      40.907  28.520  47.291  1.00 20.55           O  
-ATOM   2609  N   ILE B 152      34.984  27.106  40.931  1.00 22.83           N  
-ATOM   2610  CA  ILE B 152      33.701  27.068  40.234  1.00 21.99           C  
-ATOM   2611  C   ILE B 152      33.409  25.767  39.493  1.00 22.20           C  
-ATOM   2612  O   ILE B 152      32.269  25.525  39.105  1.00 24.18           O  
-ATOM   2613  CB  ILE B 152      33.545  28.254  39.245  1.00 21.82           C  
-ATOM   2614  CG1 ILE B 152      34.556  28.137  38.102  1.00 22.46           C  
-ATOM   2615  CG2 ILE B 152      33.753  29.573  39.984  1.00 23.05           C  
-ATOM   2616  CD1 ILE B 152      34.341  29.172  36.999  1.00 25.87           C  
-ATOM   2617  N   HIS B 153      34.424  24.934  39.284  1.00 23.16           N  
-ATOM   2618  CA  HIS B 153      34.220  23.648  38.616  1.00 26.37           C  
-ATOM   2619  C   HIS B 153      34.329  22.531  39.660  1.00 29.08           C  
-ATOM   2620  O   HIS B 153      34.990  22.698  40.679  1.00 29.67           O  
-ATOM   2621  CB  HIS B 153      35.268  23.427  37.520  1.00 26.88           C  
-ATOM   2622  CG  HIS B 153      35.141  24.367  36.363  1.00 30.00           C  
-ATOM   2623  ND1 HIS B 153      33.959  24.548  35.676  1.00 32.22           N  
-ATOM   2624  CD2 HIS B 153      36.046  25.186  35.778  1.00 29.62           C  
-ATOM   2625  CE1 HIS B 153      34.142  25.441  34.719  1.00 32.51           C  
-ATOM   2626  NE2 HIS B 153      35.400  25.843  34.759  1.00 28.62           N  
-ATOM   2627  N   ASP B 154      33.694  21.391  39.419  1.00 30.57           N  
-ATOM   2628  CA  ASP B 154      33.770  20.322  40.407  1.00 34.23           C  
-ATOM   2629  C   ASP B 154      34.964  19.400  40.172  1.00 32.92           C  
-ATOM   2630  O   ASP B 154      35.399  18.701  41.085  1.00 32.94           O  
-ATOM   2631  CB  ASP B 154      32.477  19.510  40.420  1.00 39.11           C  
-ATOM   2632  CG  ASP B 154      32.474  18.420  39.386  1.00 41.97           C  
-ATOM   2633  OD1 ASP B 154      32.552  18.756  38.187  1.00 44.45           O  
-ATOM   2634  OD2 ASP B 154      32.404  17.230  39.779  1.00 43.37           O  
-ATOM   2635  N   ASP B 155      35.490  19.403  38.950  1.00 33.85           N  
-ATOM   2636  CA  ASP B 155      36.643  18.573  38.601  1.00 33.98           C  
-ATOM   2637  C   ASP B 155      37.917  19.424  38.683  1.00 33.28           C  
-ATOM   2638  O   ASP B 155      38.259  20.137  37.739  1.00 31.10           O  
-ATOM   2639  CB  ASP B 155      36.483  18.021  37.183  1.00 39.00           C  
-ATOM   2640  CG  ASP B 155      37.364  16.813  36.922  1.00 44.07           C  
-ATOM   2641  OD1 ASP B 155      38.587  16.894  37.175  1.00 46.31           O  
-ATOM   2642  OD2 ASP B 155      36.828  15.781  36.459  1.00 47.30           O  
-ATOM   2643  N   VAL B 156      38.609  19.339  39.818  1.00 32.32           N  
-ATOM   2644  CA  VAL B 156      39.838  20.097  40.063  1.00 29.70           C  
-ATOM   2645  C   VAL B 156      40.996  19.701  39.144  1.00 29.10           C  
-ATOM   2646  O   VAL B 156      41.178  18.523  38.829  1.00 25.30           O  
-ATOM   2647  CB  VAL B 156      40.300  19.915  41.531  1.00 30.21           C  
-ATOM   2648  CG1 VAL B 156      41.633  20.604  41.756  1.00 32.47           C  
-ATOM   2649  CG2 VAL B 156      39.242  20.467  42.481  1.00 31.29           C  
-ATOM   2650  N   LEU B 157      41.782  20.689  38.721  1.00 26.36           N  
-ATOM   2651  CA  LEU B 157      42.932  20.417  37.864  1.00 25.16           C  
-ATOM   2652  C   LEU B 157      44.094  19.919  38.716  1.00 25.10           C  
-ATOM   2653  O   LEU B 157      44.455  20.547  39.716  1.00 24.97           O  
-ATOM   2654  CB  LEU B 157      43.373  21.686  37.116  1.00 24.68           C  
-ATOM   2655  CG  LEU B 157      42.488  22.203  35.979  1.00 25.39           C  
-ATOM   2656  CD1 LEU B 157      42.964  23.583  35.533  1.00 25.95           C  
-ATOM   2657  CD2 LEU B 157      42.536  21.220  34.814  1.00 28.09           C  
-ATOM   2658  N   SER B 158      44.676  18.789  38.326  1.00 24.15           N  
-ATOM   2659  CA  SER B 158      45.819  18.254  39.055  1.00 24.79           C  
-ATOM   2660  C   SER B 158      46.963  19.244  38.884  1.00 26.59           C  
-ATOM   2661  O   SER B 158      46.911  20.126  38.019  1.00 26.24           O  
-ATOM   2662  CB  SER B 158      46.234  16.894  38.487  1.00 25.33           C  
-ATOM   2663  OG  SER B 158      46.707  17.022  37.156  1.00 25.28           O  
-ATOM   2664  N   LYS B 159      47.995  19.103  39.706  1.00 26.94           N  
-ATOM   2665  CA  LYS B 159      49.149  19.985  39.632  1.00 27.55           C  
-ATOM   2666  C   LYS B 159      49.734  19.993  38.216  1.00 27.96           C  
-ATOM   2667  O   LYS B 159      49.984  21.057  37.645  1.00 25.88           O  
-ATOM   2668  CB  LYS B 159      50.210  19.527  40.638  1.00 29.63           C  
-ATOM   2669  CG  LYS B 159      51.519  20.300  40.590  1.00 32.33           C  
-ATOM   2670  CD  LYS B 159      52.490  19.764  41.635  1.00 35.11           C  
-ATOM   2671  CE  LYS B 159      53.841  20.452  41.560  1.00 38.78           C  
-ATOM   2672  NZ  LYS B 159      53.727  21.925  41.736  1.00 40.55           N  
-ATOM   2673  N   SER B 160      49.934  18.808  37.647  1.00 27.84           N  
-ATOM   2674  CA  SER B 160      50.504  18.702  36.309  1.00 29.44           C  
-ATOM   2675  C   SER B 160      49.603  19.313  35.242  1.00 28.48           C  
-ATOM   2676  O   SER B 160      50.086  19.981  34.326  1.00 29.86           O  
-ATOM   2677  CB  SER B 160      50.806  17.236  35.966  1.00 29.45           C  
-ATOM   2678  OG  SER B 160      49.643  16.435  36.054  1.00 36.55           O  
-ATOM   2679  N   LYS B 161      48.296  19.099  35.354  1.00 28.13           N  
-ATOM   2680  CA  LYS B 161      47.380  19.659  34.370  1.00 26.96           C  
-ATOM   2681  C   LYS B 161      47.235  21.169  34.529  1.00 25.99           C  
-ATOM   2682  O   LYS B 161      47.010  21.882  33.548  1.00 26.28           O  
-ATOM   2683  CB  LYS B 161      46.018  18.969  34.455  1.00 28.97           C  
-ATOM   2684  CG  LYS B 161      46.057  17.523  33.979  1.00 30.31           C  
-ATOM   2685  CD  LYS B 161      44.676  16.888  33.951  1.00 31.70           C  
-ATOM   2686  CE  LYS B 161      44.753  15.465  33.406  1.00 32.38           C  
-ATOM   2687  NZ  LYS B 161      43.418  14.817  33.307  1.00 33.45           N  
-ATOM   2688  N   ARG B 162      47.371  21.660  35.757  1.00 24.57           N  
-ATOM   2689  CA  ARG B 162      47.271  23.095  36.000  1.00 24.43           C  
-ATOM   2690  C   ARG B 162      48.497  23.763  35.380  1.00 25.96           C  
-ATOM   2691  O   ARG B 162      48.391  24.799  34.726  1.00 25.47           O  
-ATOM   2692  CB  ARG B 162      47.238  23.398  37.498  1.00 23.48           C  
-ATOM   2693  CG  ARG B 162      46.986  24.864  37.805  1.00 21.85           C  
-ATOM   2694  CD  ARG B 162      47.090  25.189  39.291  1.00 22.23           C  
-ATOM   2695  NE  ARG B 162      46.630  26.557  39.547  1.00 22.38           N  
-ATOM   2696  CZ  ARG B 162      45.354  26.931  39.516  1.00 21.78           C  
-ATOM   2697  NH1 ARG B 162      44.402  26.040  39.255  1.00 19.71           N  
-ATOM   2698  NH2 ARG B 162      45.028  28.200  39.724  1.00 20.51           N  
-ATOM   2699  N   GLN B 163      49.662  23.160  35.594  1.00 26.59           N  
-ATOM   2700  CA  GLN B 163      50.898  23.701  35.046  1.00 29.26           C  
-ATOM   2701  C   GLN B 163      50.830  23.704  33.522  1.00 28.15           C  
-ATOM   2702  O   GLN B 163      51.277  24.653  32.876  1.00 28.01           O  
-ATOM   2703  CB  GLN B 163      52.096  22.876  35.519  1.00 31.14           C  
-ATOM   2704  CG  GLN B 163      53.439  23.409  35.039  1.00 36.53           C  
-ATOM   2705  CD  GLN B 163      53.641  24.875  35.374  1.00 39.37           C  
-ATOM   2706  OE1 GLN B 163      53.465  25.295  36.520  1.00 43.26           O  
-ATOM   2707  NE2 GLN B 163      54.018  25.664  34.374  1.00 42.51           N  
-ATOM   2708  N   ALA B 164      50.263  22.645  32.949  1.00 26.06           N  
-ATOM   2709  CA  ALA B 164      50.129  22.547  31.498  1.00 26.07           C  
-ATOM   2710  C   ALA B 164      49.242  23.663  30.938  1.00 26.05           C  
-ATOM   2711  O   ALA B 164      49.543  24.238  29.888  1.00 24.51           O  
-ATOM   2712  CB  ALA B 164      49.561  21.185  31.112  1.00 26.21           C  
-ATOM   2713  N   MET B 165      48.145  23.972  31.626  1.00 23.99           N  
-ATOM   2714  CA  MET B 165      47.265  25.033  31.148  1.00 24.59           C  
-ATOM   2715  C   MET B 165      47.922  26.393  31.363  1.00 25.06           C  
-ATOM   2716  O   MET B 165      47.714  27.324  30.583  1.00 25.25           O  
-ATOM   2717  CB  MET B 165      45.902  24.987  31.851  1.00 23.56           C  
-ATOM   2718  CG  MET B 165      45.036  23.794  31.463  1.00 24.57           C  
-ATOM   2719  SD  MET B 165      44.993  23.464  29.676  1.00 27.68           S  
-ATOM   2720  CE  MET B 165      44.265  24.987  29.040  1.00 22.10           C  
-ATOM   2721  N   LEU B 166      48.718  26.504  32.421  1.00 24.88           N  
-ATOM   2722  CA  LEU B 166      49.416  27.751  32.709  1.00 25.93           C  
-ATOM   2723  C   LEU B 166      50.345  28.052  31.529  1.00 26.37           C  
-ATOM   2724  O   LEU B 166      50.439  29.193  31.066  1.00 23.70           O  
-ATOM   2725  CB  LEU B 166      50.230  27.605  33.998  1.00 28.19           C  
-ATOM   2726  CG  LEU B 166      50.886  28.833  34.644  1.00 30.94           C  
-ATOM   2727  CD1 LEU B 166      52.024  29.370  33.785  1.00 31.69           C  
-ATOM   2728  CD2 LEU B 166      49.831  29.886  34.860  1.00 37.27           C  
-ATOM   2729  N   GLU B 167      51.027  27.019  31.044  1.00 25.23           N  
-ATOM   2730  CA  GLU B 167      51.943  27.176  29.918  1.00 28.77           C  
-ATOM   2731  C   GLU B 167      51.172  27.478  28.632  1.00 28.62           C  
-ATOM   2732  O   GLU B 167      51.634  28.248  27.786  1.00 30.26           O  
-ATOM   2733  CB  GLU B 167      52.788  25.911  29.752  1.00 30.41           C  
-ATOM   2734  CG  GLU B 167      53.518  25.516  31.029  1.00 35.06           C  
-ATOM   2735  CD  GLU B 167      54.316  24.232  30.889  1.00 38.65           C  
-ATOM   2736  OE1 GLU B 167      53.815  23.284  30.248  1.00 41.42           O  
-ATOM   2737  OE2 GLU B 167      55.436  24.165  31.439  1.00 42.32           O  
-ATOM   2738  N   THR B 168      49.992  26.882  28.498  1.00 27.26           N  
-ATOM   2739  CA  THR B 168      49.153  27.095  27.325  1.00 26.46           C  
-ATOM   2740  C   THR B 168      48.709  28.559  27.257  1.00 27.76           C  
-ATOM   2741  O   THR B 168      48.628  29.143  26.175  1.00 26.10           O  
-ATOM   2742  CB  THR B 168      47.921  26.168  27.367  1.00 28.63           C  
-ATOM   2743  OG1 THR B 168      48.365  24.805  27.344  1.00 28.32           O  
-ATOM   2744  CG2 THR B 168      47.002  26.422  26.172  1.00 25.72           C  
-ATOM   2745  N   ILE B 169      48.424  29.149  28.417  1.00 25.87           N  
-ATOM   2746  CA  ILE B 169      48.019  30.548  28.479  1.00 24.73           C  
-ATOM   2747  C   ILE B 169      49.215  31.418  28.086  1.00 26.71           C  
-ATOM   2748  O   ILE B 169      49.069  32.413  27.371  1.00 24.67           O  
-ATOM   2749  CB  ILE B 169      47.545  30.924  29.901  1.00 24.27           C  
-ATOM   2750  CG1 ILE B 169      46.249  30.174  30.218  1.00 23.07           C  
-ATOM   2751  CG2 ILE B 169      47.321  32.427  30.011  1.00 22.00           C  
-ATOM   2752  CD1 ILE B 169      45.765  30.352  31.637  1.00 22.55           C  
-ATOM   2753  N   LEU B 170      50.397  31.031  28.558  1.00 26.03           N  
-ATOM   2754  CA  LEU B 170      51.632  31.745  28.245  1.00 28.10           C  
-ATOM   2755  C   LEU B 170      51.855  31.715  26.730  1.00 27.98           C  
-ATOM   2756  O   LEU B 170      52.294  32.699  26.139  1.00 28.23           O  
-ATOM   2757  CB  LEU B 170      52.806  31.076  28.967  1.00 28.76           C  
-ATOM   2758  CG  LEU B 170      53.501  31.774  30.145  1.00 31.20           C  
-ATOM   2759  CD1 LEU B 170      52.590  32.766  30.833  1.00 30.83           C  
-ATOM   2760  CD2 LEU B 170      53.997  30.712  31.110  1.00 29.04           C  
-ATOM   2761  N   GLU B 171      51.544  30.580  26.111  1.00 29.76           N  
-ATOM   2762  CA  GLU B 171      51.694  30.414  24.663  1.00 32.60           C  
-ATOM   2763  C   GLU B 171      50.785  31.377  23.900  1.00 31.58           C  
-ATOM   2764  O   GLU B 171      51.101  31.798  22.787  1.00 29.95           O  
-ATOM   2765  CB  GLU B 171      51.336  28.983  24.253  1.00 35.33           C  
-ATOM   2766  CG  GLU B 171      52.363  27.918  24.605  1.00 41.21           C  
-ATOM   2767  CD  GLU B 171      51.783  26.511  24.523  1.00 44.15           C  
-ATOM   2768  OE1 GLU B 171      50.954  26.252  23.622  1.00 45.84           O  
-ATOM   2769  OE2 GLU B 171      52.158  25.661  25.357  1.00 48.78           O  
-ATOM   2770  N   LEU B 172      49.652  31.712  24.509  1.00 29.47           N  
-ATOM   2771  CA  LEU B 172      48.667  32.600  23.902  1.00 29.71           C  
-ATOM   2772  C   LEU B 172      49.116  34.061  23.817  1.00 29.44           C  
-ATOM   2773  O   LEU B 172      48.566  34.835  23.035  1.00 29.54           O  
-ATOM   2774  CB  LEU B 172      47.354  32.506  24.687  1.00 30.45           C  
-ATOM   2775  CG  LEU B 172      46.072  33.066  24.073  1.00 30.07           C  
-ATOM   2776  CD1 LEU B 172      45.779  32.349  22.760  1.00 30.02           C  
-ATOM   2777  CD2 LEU B 172      44.915  32.873  25.054  1.00 29.48           C  
-ATOM   2778  N   ILE B 173      50.099  34.444  24.626  1.00 29.24           N  
-ATOM   2779  CA  ILE B 173      50.592  35.817  24.611  1.00 30.04           C  
-ATOM   2780  C   ILE B 173      51.171  36.114  23.225  1.00 30.64           C  
-ATOM   2781  O   ILE B 173      51.998  35.360  22.720  1.00 28.63           O  
-ATOM   2782  CB  ILE B 173      51.692  36.032  25.679  1.00 30.38           C  
-ATOM   2783  CG1 ILE B 173      51.110  35.812  27.080  1.00 31.37           C  
-ATOM   2784  CG2 ILE B 173      52.260  37.443  25.576  1.00 31.53           C  
-ATOM   2785  CD1 ILE B 173      52.132  35.935  28.204  1.00 29.75           C  
-ATOM   2786  N   PRO B 174      50.727  37.210  22.590  1.00 30.67           N  
-ATOM   2787  CA  PRO B 174      51.216  37.586  21.256  1.00 32.08           C  
-ATOM   2788  C   PRO B 174      52.739  37.684  21.211  1.00 31.88           C  
-ATOM   2789  O   PRO B 174      53.365  38.227  22.121  1.00 32.94           O  
-ATOM   2790  CB  PRO B 174      50.538  38.930  21.009  1.00 31.70           C  
-ATOM   2791  CG  PRO B 174      49.230  38.773  21.739  1.00 31.19           C  
-ATOM   2792  CD  PRO B 174      49.672  38.136  23.042  1.00 31.61           C  
-ATOM   2793  N   SER B 175      53.327  37.150  20.148  1.00 34.44           N  
-ATOM   2794  CA  SER B 175      54.775  37.159  19.982  1.00 36.52           C  
-ATOM   2795  C   SER B 175      55.375  38.559  19.914  1.00 38.15           C  
-ATOM   2796  O   SER B 175      54.717  39.519  19.511  1.00 38.16           O  
-ATOM   2797  CB  SER B 175      55.158  36.392  18.715  1.00 37.91           C  
-ATOM   2798  OG  SER B 175      56.551  36.487  18.467  1.00 39.82           O  
-ATOM   2799  N   GLU B 176      56.633  38.664  20.323  1.00 39.70           N  
-ATOM   2800  CA  GLU B 176      57.357  39.926  20.279  1.00 42.92           C  
-ATOM   2801  C   GLU B 176      58.575  39.699  19.394  1.00 43.98           C  
-ATOM   2802  O   GLU B 176      59.461  40.546  19.302  1.00 44.43           O  
-ATOM   2803  CB  GLU B 176      57.812  40.342  21.679  1.00 44.22           C  
-ATOM   2804  CG  GLU B 176      56.708  40.879  22.568  1.00 46.92           C  
-ATOM   2805  CD  GLU B 176      57.236  41.371  23.902  1.00 49.13           C  
-ATOM   2806  OE1 GLU B 176      57.713  40.534  24.699  1.00 49.52           O  
-ATOM   2807  OE2 GLU B 176      57.181  42.595  24.150  1.00 49.33           O  
-ATOM   2808  N   LEU B 177      58.604  38.540  18.746  1.00 46.18           N  
-ATOM   2809  CA  LEU B 177      59.708  38.167  17.871  1.00 49.57           C  
-ATOM   2810  C   LEU B 177      59.358  38.319  16.399  1.00 51.10           C  
-ATOM   2811  O   LEU B 177      58.348  37.799  15.932  1.00 50.43           O  
-ATOM   2812  CB  LEU B 177      60.128  36.723  18.152  1.00 51.03           C  
-ATOM   2813  CG  LEU B 177      61.060  36.487  19.344  1.00 52.77           C  
-ATOM   2814  CD1 LEU B 177      60.578  37.255  20.564  1.00 53.46           C  
-ATOM   2815  CD2 LEU B 177      61.134  34.992  19.630  1.00 54.38           C  
-ATOM   2816  N   HIS B 178      60.204  39.037  15.672  1.00 54.27           N  
-ATOM   2817  CA  HIS B 178      59.987  39.252  14.251  1.00 58.00           C  
-ATOM   2818  C   HIS B 178      60.711  38.200  13.423  1.00 58.82           C  
-ATOM   2819  O   HIS B 178      61.871  37.884  13.679  1.00 58.68           O  
-ATOM   2820  CB  HIS B 178      60.447  40.659  13.856  1.00 60.96           C  
-ATOM   2821  CG  HIS B 178      61.552  41.198  14.711  1.00 64.41           C  
-ATOM   2822  ND1 HIS B 178      61.450  41.299  16.082  1.00 66.63           N  
-ATOM   2823  CD2 HIS B 178      62.774  41.685  14.388  1.00 66.32           C  
-ATOM   2824  CE1 HIS B 178      62.562  41.824  16.567  1.00 67.27           C  
-ATOM   2825  NE2 HIS B 178      63.381  42.068  15.560  1.00 67.34           N  
-ATOM   2826  N   HIS B 179      60.007  37.651  12.438  1.00 60.84           N  
-ATOM   2827  CA  HIS B 179      60.563  36.629  11.558  1.00 63.48           C  
-ATOM   2828  C   HIS B 179      61.286  37.288  10.390  1.00 64.80           C  
-ATOM   2829  O   HIS B 179      61.265  38.509  10.245  1.00 64.31           O  
-ATOM   2830  CB  HIS B 179      59.445  35.739  11.010  1.00 64.36           C  
-ATOM   2831  CG  HIS B 179      58.627  35.070  12.070  1.00 66.53           C  
-ATOM   2832  ND1 HIS B 179      57.481  34.358  11.785  1.00 66.84           N  
-ATOM   2833  CD2 HIS B 179      58.788  35.001  13.413  1.00 67.16           C  
-ATOM   2834  CE1 HIS B 179      56.972  33.880  12.906  1.00 67.49           C  
-ATOM   2835  NE2 HIS B 179      57.746  34.255  13.909  1.00 68.05           N  
-ATOM   2836  N   HIS B 180      61.923  36.473   9.557  1.00 66.78           N  
-ATOM   2837  CA  HIS B 180      62.636  36.985   8.396  1.00 69.53           C  
-ATOM   2838  C   HIS B 180      62.243  36.216   7.139  1.00 70.98           C  
-ATOM   2839  O   HIS B 180      62.859  35.205   6.796  1.00 71.75           O  
-ATOM   2840  CB  HIS B 180      64.148  36.908   8.623  1.00 69.91           C  
-ATOM   2841  CG  HIS B 180      64.646  37.853   9.673  1.00 70.79           C  
-ATOM   2842  ND1 HIS B 180      64.315  37.729  11.005  1.00 71.30           N  
-ATOM   2843  CD2 HIS B 180      65.427  38.956   9.581  1.00 70.97           C  
-ATOM   2844  CE1 HIS B 180      64.869  38.715  11.688  1.00 71.31           C  
-ATOM   2845  NE2 HIS B 180      65.549  39.474  10.848  1.00 71.12           N  
-ATOM   2846  N   HIS B 181      61.207  36.714   6.467  1.00 72.24           N  
-ATOM   2847  CA  HIS B 181      60.679  36.114   5.244  1.00 73.65           C  
-ATOM   2848  C   HIS B 181      60.684  34.588   5.307  1.00 74.77           C  
-ATOM   2849  O   HIS B 181      61.396  33.960   4.492  1.00 75.22           O  
-ATOM   2850  CB  HIS B 181      61.483  36.588   4.029  1.00 73.69           C  
-ATOM   2851  CG  HIS B 181      60.857  36.232   2.715  1.00 74.06           C  
-ATOM   2852  ND1 HIS B 181      61.480  36.461   1.507  1.00 74.00           N  
-ATOM   2853  CD2 HIS B 181      59.661  35.669   2.420  1.00 73.95           C  
-ATOM   2854  CE1 HIS B 181      60.696  36.054   0.525  1.00 74.12           C  
-ATOM   2855  NE2 HIS B 181      59.586  35.570   1.052  1.00 73.98           N  
-TER    2856      HIS B 181                                                      
-HETATM 2857  C1  GOL A 185      18.084  41.166  57.795  1.00 57.96           C  
-HETATM 2858  O1  GOL A 185      16.670  40.970  57.844  1.00 60.12           O  
-HETATM 2859  C2  GOL A 185      18.795  39.959  58.411  1.00 57.55           C  
-HETATM 2860  O2  GOL A 185      18.445  38.774  57.690  1.00 55.93           O  
-HETATM 2861  C3  GOL A 185      20.309  40.172  58.358  1.00 57.11           C  
-HETATM 2862  O3  GOL A 185      20.984  39.048  58.932  1.00 55.85           O  
-HETATM 2863  C1  GOL A 186      22.312  23.541  60.322  1.00 66.32           C  
-HETATM 2864  O1  GOL A 186      22.041  24.537  61.305  1.00 65.60           O  
-HETATM 2865  C2  GOL A 186      23.058  24.177  59.151  1.00 66.26           C  
-HETATM 2866  O2  GOL A 186      24.286  24.740  59.622  1.00 65.98           O  
-HETATM 2867  C3  GOL A 186      23.347  23.121  58.086  1.00 66.77           C  
-HETATM 2868  O3  GOL A 186      24.037  23.722  56.990  1.00 68.20           O  
-HETATM 2869  C1  GOL A 187      14.516  25.534  62.528  1.00 44.86           C  
-HETATM 2870  O1  GOL A 187      15.629  26.005  63.284  1.00 47.70           O  
-HETATM 2871  C2  GOL A 187      14.774  24.089  62.098  1.00 44.47           C  
-HETATM 2872  O2  GOL A 187      14.943  23.269  63.264  1.00 42.35           O  
-HETATM 2873  C3  GOL A 187      13.593  23.583  61.277  1.00 44.07           C  
-HETATM 2874  O3  GOL A 187      13.820  22.236  60.863  1.00 40.34           O  
-HETATM 2875  C1  GOL A 188      28.653  27.224  35.917  1.00 40.60           C  
-HETATM 2876  O1  GOL A 188      29.027  26.329  36.968  1.00 40.02           O  
-HETATM 2877  C2  GOL A 188      27.233  27.739  36.154  1.00 40.63           C  
-HETATM 2878  O2  GOL A 188      27.191  28.422  37.405  1.00 42.64           O  
-HETATM 2879  C3  GOL A 188      26.834  28.698  35.025  1.00 41.21           C  
-HETATM 2880  O3  GOL A 188      25.503  29.183  35.234  1.00 40.01           O  
-HETATM 2881  S   SO4 A 184      16.418  29.425  63.020  1.00 30.51           S  
-HETATM 2882  O1  SO4 A 184      16.829  28.664  61.774  1.00 27.70           O  
-HETATM 2883  O2  SO4 A 184      16.057  30.839  62.595  1.00 28.95           O  
-HETATM 2884  O3  SO4 A 184      15.233  28.822  63.511  1.00 34.07           O  
-HETATM 2885  O4  SO4 A 184      17.609  29.557  63.784  1.00 32.18           O  
-HETATM 2886  C1   ET B 184      44.296  36.981  38.364  1.00 23.84           C  
-HETATM 2887  C2   ET B 184      43.422  37.734  37.589  1.00 22.31           C  
-HETATM 2888  C3   ET B 184      42.648  38.765  38.172  1.00 21.43           C  
-HETATM 2889  C4   ET B 184      42.751  39.044  39.536  1.00 22.24           C  
-HETATM 2890  N5   ET B 184      43.751  38.554  41.762  1.00 25.71           N  
-HETATM 2891  C6   ET B 184      44.579  37.842  42.597  1.00 24.79           C  
-HETATM 2892  C7   ET B 184      46.316  35.977  42.873  1.00 27.38           C  
-HETATM 2893  C8   ET B 184      47.097  34.960  42.325  1.00 28.69           C  
-HETATM 2894  C9   ET B 184      47.025  34.664  40.939  1.00 26.88           C  
-HETATM 2895  C10  ET B 184      46.176  35.382  40.102  1.00 26.76           C  
-HETATM 2896  C11  ET B 184      45.430  36.743  42.046  1.00 27.01           C  
-HETATM 2897  C12  ET B 184      45.360  36.435  40.625  1.00 25.37           C  
-HETATM 2898  C13  ET B 184      44.430  37.232  39.770  1.00 24.73           C  
-HETATM 2899  C14  ET B 184      43.645  38.287  40.389  1.00 23.67           C  
-HETATM 2900  C15  ET B 184      44.666  38.108  44.091  1.00 27.13           C  
-HETATM 2901  C16  ET B 184      45.689  38.913  44.671  1.00 26.25           C  
-HETATM 2902  C17  ET B 184      45.722  39.100  46.069  1.00 27.12           C  
-HETATM 2903  C18  ET B 184      44.749  38.494  46.901  1.00 27.28           C  
-HETATM 2904  C19  ET B 184      43.730  37.697  46.340  1.00 26.58           C  
-HETATM 2905  C20  ET B 184      43.683  37.499  44.948  1.00 25.28           C  
-HETATM 2906  C21  ET B 184      42.918  39.663  42.326  1.00 25.81           C  
-HETATM 2907  C22  ET B 184      43.643  41.013  42.111  1.00 26.71           C  
-HETATM 2908  N23  ET B 184      41.774  39.517  37.382  1.00 21.68           N  
-HETATM 2909  N24  ET B 184      47.954  34.235  43.157  1.00 30.31           N  
-HETATM 2910  C1  GOL B 187      28.832  34.257  64.642  1.00 38.39           C  
-HETATM 2911  O1  GOL B 187      28.590  35.074  63.498  1.00 35.06           O  
-HETATM 2912  C2  GOL B 187      30.339  34.093  64.841  1.00 40.18           C  
-HETATM 2913  O2  GOL B 187      30.942  35.377  65.016  1.00 38.43           O  
-HETATM 2914  C3  GOL B 187      30.605  33.220  66.071  1.00 42.27           C  
-HETATM 2915  O3  GOL B 187      32.014  33.069  66.255  1.00 44.89           O  
-HETATM 2916  C1  GOL B 188      29.690  36.827  50.971  1.00 24.07           C  
-HETATM 2917  O1  GOL B 188      28.552  36.928  51.825  1.00 22.25           O  
-HETATM 2918  C2  GOL B 188      30.854  37.613  51.566  1.00 29.15           C  
-HETATM 2919  O2  GOL B 188      31.163  37.096  52.877  1.00 25.17           O  
-HETATM 2920  C3  GOL B 188      32.065  37.489  50.626  1.00 29.20           C  
-HETATM 2921  O3  GOL B 188      33.165  38.214  51.158  1.00 41.77           O  
-HETATM 2922  S   SO4 B 185      62.945  40.034   6.051  1.00 58.35           S  
-HETATM 2923  O1  SO4 B 185      63.778  38.766   5.897  1.00 58.42           O  
-HETATM 2924  O2  SO4 B 185      63.013  40.768   4.717  1.00 58.18           O  
-HETATM 2925  O3  SO4 B 185      61.599  39.636   6.239  1.00 56.69           O  
-HETATM 2926  O4  SO4 B 185      63.679  40.846   6.961  1.00 58.35           O  
-HETATM 2927  S   SO4 B 186      37.760  16.247  42.422  1.00 35.21           S  
-HETATM 2928  O1  SO4 B 186      38.571  16.868  41.289  1.00 32.98           O  
-HETATM 2929  O2  SO4 B 186      37.324  17.387  43.341  1.00 30.73           O  
-HETATM 2930  O3  SO4 B 186      36.582  15.698  41.846  1.00 35.67           O  
-HETATM 2931  O4  SO4 B 186      38.701  15.493  43.184  1.00 34.10           O  
-HETATM 2932  O   HOH A 189       2.718  29.955  56.456  1.00 13.64           O  
-HETATM 2933  O   HOH A 190      34.764  25.811  45.695  1.00 19.49           O  
-HETATM 2934  O   HOH A 191      31.917  39.092  34.560  1.00 20.69           O  
-HETATM 2935  O   HOH A 192      31.146  31.227  49.301  1.00 17.24           O  
-HETATM 2936  O   HOH A 193      15.107  38.235  55.625  1.00 22.02           O  
-HETATM 2937  O   HOH A 194      23.892  39.945  41.527  1.00 30.38           O  
-HETATM 2938  O   HOH A 195       9.905  18.171  55.012  1.00 25.11           O  
-HETATM 2939  O   HOH A 196      32.624  29.451  50.838  1.00 20.78           O  
-HETATM 2940  O   HOH A 197      22.512  28.582  37.146  1.00 22.41           O  
-HETATM 2941  O   HOH A 198      30.205  43.489  32.182  1.00 22.27           O  
-HETATM 2942  O   HOH A 199      26.623  25.597  50.366  1.00 19.38           O  
-HETATM 2943  O   HOH A 200      24.190  33.637  37.974  1.00 31.90           O  
-HETATM 2944  O   HOH A 201      30.888  43.657  40.049  1.00 27.95           O  
-HETATM 2945  O   HOH A 202       5.710  21.958  59.597  1.00 20.95           O  
-HETATM 2946  O   HOH A 203      41.109  43.235  41.066  1.00 26.34           O  
-HETATM 2947  O   HOH A 204      16.814  33.938  42.985  1.00 22.75           O  
-HETATM 2948  O   HOH A 205      18.466  29.816  66.522  1.00 25.25           O  
-HETATM 2949  O   HOH A 206      23.502  15.617  45.999  1.00 22.71           O  
-HETATM 2950  O   HOH A 207      36.913  43.204  42.466  1.00 23.85           O  
-HETATM 2951  O   HOH A 208      24.840  21.406  55.789  1.00 38.11           O  
-HETATM 2952  O   HOH A 209      26.995  41.804  41.146  1.00 33.01           O  
-HETATM 2953  O   HOH A 210      16.665  19.238  49.566  1.00 28.96           O  
-HETATM 2954  O   HOH A 211      28.444  26.271  54.409  1.00 41.02           O  
-HETATM 2955  O   HOH A 212      25.826  33.956  33.211  1.00 29.06           O  
-HETATM 2956  O   HOH A 213      35.289  51.162  28.931  1.00 37.20           O  
-HETATM 2957  O   HOH A 214      20.216  30.379  37.521  1.00 31.02           O  
-HETATM 2958  O   HOH A 215      33.062  24.059  43.579  1.00 26.27           O  
-HETATM 2959  O   HOH A 216      27.055  41.150  52.559  1.00 44.47           O  
-HETATM 2960  O   HOH A 217      18.971  27.596  60.617  1.00 29.28           O  
-HETATM 2961  O   HOH A 218      17.434  27.953  32.705  1.00 34.96           O  
-HETATM 2962  O   HOH A 219      15.882  22.312  43.702  1.00 27.65           O  
-HETATM 2963  O   HOH A 220      26.878  40.353  31.700  1.00 32.39           O  
-HETATM 2964  O   HOH A 221      44.439  12.267  32.075  1.00 38.10           O  
-HETATM 2965  O   HOH A 222      32.905  18.150  51.072  1.00 32.51           O  
-HETATM 2966  O   HOH A 223      28.646  43.868  35.960  1.00 31.25           O  
-HETATM 2967  O   HOH A 224      18.539  22.701  60.218  1.00 30.44           O  
-HETATM 2968  O   HOH A 225      30.241  30.193  53.306  1.00 30.63           O  
-HETATM 2969  O   HOH A 226      38.164  52.377  25.006  1.00 45.90           O  
-HETATM 2970  O   HOH A 227      27.376  31.483  62.404  1.00 31.24           O  
-HETATM 2971  O   HOH A 228      41.946  45.048  35.363  1.00 31.85           O  
-HETATM 2972  O   HOH A 229      28.035  49.572  28.906  1.00 44.57           O  
-HETATM 2973  O   HOH A 230      28.743  42.801  38.743  1.00 32.41           O  
-HETATM 2974  O   HOH A 231      24.563  30.809  32.900  1.00 31.76           O  
-HETATM 2975  O   HOH A 232      40.348  34.681  18.953  1.00 30.47           O  
-HETATM 2976  O   HOH A 233      15.413  37.459  49.392  1.00 27.16           O  
-HETATM 2977  O   HOH A 234      28.488  30.501  55.551  1.00 31.50           O  
-HETATM 2978  O   HOH A 235      26.570  28.528  55.496  1.00 32.06           O  
-HETATM 2979  O   HOH A 236      24.500  15.921  39.640  1.00 32.99           O  
-HETATM 2980  O   HOH A 237      35.335  16.441  26.241  1.00 39.71           O  
-HETATM 2981  O   HOH A 238      17.580  32.325  40.986  1.00 30.72           O  
-HETATM 2982  O   HOH A 239      34.184  19.963  36.090  1.00 34.65           O  
-HETATM 2983  O   HOH A 240      29.199  49.789  25.712  1.00 35.45           O  
-HETATM 2984  O   HOH A 241       6.722  35.081  58.019  1.00 32.56           O  
-HETATM 2985  O   HOH A 242      19.419  19.884  39.123  1.00 40.12           O  
-HETATM 2986  O   HOH A 243      15.317  24.971  36.963  1.00 35.61           O  
-HETATM 2987  O   HOH A 244      18.207  24.984  61.462  1.00 38.40           O  
-HETATM 2988  O   HOH A 245      21.158  34.108  41.315  1.00 34.60           O  
-HETATM 2989  O   HOH A 246      20.752  39.098  45.924  1.00 30.47           O  
-HETATM 2990  O   HOH A 247      28.161  39.926  25.233  1.00 33.11           O  
-HETATM 2991  O   HOH A 248      26.547  13.213  48.207  1.00 50.51           O  
-HETATM 2992  O   HOH A 249      41.946  27.179  21.444  1.00 35.82           O  
-HETATM 2993  O   HOH A 250       3.842  28.379  38.454  1.00 72.97           O  
-HETATM 2994  O   HOH A 251      13.527  19.345  51.018  1.00 39.19           O  
-HETATM 2995  O   HOH A 252      31.073  18.788  26.375  1.00 48.85           O  
-HETATM 2996  O   HOH A 253      39.742  36.404  17.016  1.00 46.67           O  
-HETATM 2997  O   HOH A 254       2.153  32.867  55.505  1.00 34.80           O  
-HETATM 2998  O   HOH A 255      27.590  42.525  26.090  1.00 40.64           O  
-HETATM 2999  O   HOH A 256      27.423  38.297  27.239  1.00 39.39           O  
-HETATM 3000  O   HOH A 257      17.870  32.545  63.892  1.00 36.82           O  
-HETATM 3001  O   HOH A 258      51.222  17.984  23.533  1.00 49.87           O  
-HETATM 3002  O   HOH A 259      11.154  35.680  60.791  1.00 40.01           O  
-HETATM 3003  O   HOH A 260      44.846  15.435  19.589  1.00 54.37           O  
-HETATM 3004  O   HOH A 261      16.644  39.033  51.021  1.00 38.94           O  
-HETATM 3005  O   HOH A 262      30.329  32.623  51.587  1.00 22.55           O  
-HETATM 3006  O   HOH A 263      20.798  21.328  58.530  1.00 27.35           O  
-HETATM 3007  O   HOH A 264      39.303  44.623  42.766  1.00 23.68           O  
-HETATM 3008  O   HOH A 265      41.967  45.038  37.852  1.00 41.57           O  
-HETATM 3009  O   HOH A 266      34.733  45.345  39.252  1.00 32.51           O  
-HETATM 3010  O   HOH A 267      19.793  32.476  39.709  1.00 33.39           O  
-HETATM 3011  O   HOH A 268      15.049  39.889  53.427  1.00 35.76           O  
-HETATM 3012  O   HOH A 269      29.358  43.146  42.219  1.00 28.74           O  
-HETATM 3013  O   HOH A 270      16.056  20.923  61.338  1.00 33.75           O  
-HETATM 3014  O   HOH A 271      25.819  39.980  29.064  1.00 33.15           O  
-HETATM 3015  O   HOH A 272      24.265  18.468  37.835  1.00 30.50           O  
-HETATM 3016  O   HOH A 273      21.151  29.887  66.139  1.00 38.96           O  
-HETATM 3017  O   HOH A 274      27.657  42.893  32.040  1.00 36.72           O  
-HETATM 3018  O   HOH A 275      15.995  18.763  47.135  1.00 42.83           O  
-HETATM 3019  O   HOH A 276      23.639  33.241  31.076  1.00 35.95           O  
-HETATM 3020  O   HOH A 277      25.756  25.649  20.009  1.00 41.63           O  
-HETATM 3021  O   HOH A 278      35.287  20.694  52.662  1.00 36.30           O  
-HETATM 3022  O   HOH A 279      39.461  19.648  26.458  1.00 32.12           O  
-HETATM 3023  O   HOH A 280      33.426  21.611  55.414  1.00 46.37           O  
-HETATM 3024  O   HOH A 281      34.977  48.473  30.279  1.00 40.72           O  
-HETATM 3025  O   HOH A 282       2.570  25.219  45.012  1.00 51.90           O  
-HETATM 3026  O   HOH A 283      23.717  14.147  53.847  1.00 43.02           O  
-HETATM 3027  O   HOH A 284       1.150  31.262  59.011  1.00 34.68           O  
-HETATM 3028  O   HOH A 285      21.379  18.327  40.426  1.00 39.48           O  
-HETATM 3029  O   HOH A 286      21.292  28.801  61.109  1.00 41.18           O  
-HETATM 3030  O   HOH A 287      25.019  29.711  59.881  1.00 34.60           O  
-HETATM 3031  O   HOH A 288      33.237  17.828  53.878  1.00 38.98           O  
-HETATM 3032  O   HOH A 289      18.605  17.092  56.660  1.00 37.82           O  
-HETATM 3033  O   HOH A 290      26.538  25.879  56.229  1.00 41.10           O  
-HETATM 3034  O   HOH A 291      40.634  17.355  35.203  1.00 39.05           O  
-HETATM 3035  O   HOH A 292      12.890  16.735  51.813  1.00 46.21           O  
-HETATM 3036  O   HOH A 293       1.224  31.290  51.621  1.00 39.49           O  
-HETATM 3037  O   HOH A 294      33.263  50.585  25.704  1.00 38.88           O  
-HETATM 3038  O   HOH A 295      21.883  30.948  60.112  1.00 36.91           O  
-HETATM 3039  O   HOH A 296      19.649  34.839  60.423  1.00 35.36           O  
-HETATM 3040  O   HOH A 297      32.131  33.221  28.123  1.00 29.34           O  
-HETATM 3041  O   HOH A 298      16.993  16.857  51.014  1.00 39.98           O  
-HETATM 3042  O   HOH A 299      47.085  12.944  32.401  1.00 44.12           O  
-HETATM 3043  O   HOH A 300      30.090  14.632  46.114  1.00 33.89           O  
-HETATM 3044  O   HOH A 301      31.281  22.741  41.955  1.00 34.63           O  
-HETATM 3045  O   HOH A 302      20.254  29.841  63.348  1.00 44.29           O  
-HETATM 3046  O   HOH A 303      39.798  46.570  35.268  1.00 43.01           O  
-HETATM 3047  O   HOH A 304      32.875  34.966  16.731  1.00 41.68           O  
-HETATM 3048  O   HOH A 305      22.511  13.966  48.045  1.00 44.91           O  
-HETATM 3049  O   HOH A 306      26.169  42.549  54.665  1.00 41.39           O  
-HETATM 3050  O   HOH A 307      15.676  42.611  53.486  1.00 38.19           O  
-HETATM 3051  O   HOH A 308      38.194  51.333  39.861  1.00 47.82           O  
-HETATM 3052  O   HOH A 309      21.533  29.291  34.084  1.00 44.53           O  
-HETATM 3053  O   HOH A 310      14.474  22.674  38.974  1.00 43.34           O  
-HETATM 3054  O   HOH A 311      17.471  31.937  67.632  1.00 50.57           O  
-HETATM 3055  O   HOH A 312       4.231  34.712  51.393  1.00 47.69           O  
-HETATM 3056  O   HOH A 313      47.109  23.699  22.491  1.00 36.61           O  
-HETATM 3057  O   HOH A 314      12.218  23.863  40.229  1.00 45.28           O  
-HETATM 3058  O   HOH A 315      28.008  36.514  19.340  1.00 53.50           O  
-HETATM 3059  O   HOH A 316      35.670  51.398  39.308  1.00 51.51           O  
-HETATM 3060  O   HOH A 317      40.982  49.180  35.454  1.00 47.74           O  
-HETATM 3061  O   HOH A 318      12.888  26.092  37.173  1.00 49.22           O  
-HETATM 3062  O   HOH A 319      41.814  32.637  18.073  1.00 45.52           O  
-HETATM 3063  O   HOH A 320      33.177  47.239  39.906  1.00 30.66           O  
-HETATM 3064  O   HOH A 321      37.375  47.339  31.025  1.00 52.39           O  
-HETATM 3065  O   HOH A 322      15.178  16.087  52.930  1.00 37.78           O  
-HETATM 3066  O   HOH A 323      38.100  18.036  24.736  1.00 38.70           O  
-HETATM 3067  O   HOH A 324      23.677  27.610  60.766  1.00 46.48           O  
-HETATM 3068  O   HOH A 325      24.102  35.105  35.550  1.00 40.58           O  
-HETATM 3069  O   HOH A 326      -0.944  30.845  50.168  1.00 51.70           O  
-HETATM 3070  O   HOH A 327       5.087  23.987  46.112  1.00 49.29           O  
-HETATM 3071  O   HOH A 328      25.864  42.472  28.066  1.00 40.73           O  
-HETATM 3072  O   HOH A 329      31.453  13.464  36.871  1.00 50.25           O  
-HETATM 3073  O   HOH A 330       2.083  31.078  61.353  1.00 43.17           O  
-HETATM 3074  O   HOH A 331       3.400  32.960  49.544  1.00 55.10           O  
-HETATM 3075  O   HOH A 332      14.476  20.706  46.126  1.00 48.68           O  
-HETATM 3076  O   HOH A 333      26.129  35.309  20.621  1.00 57.93           O  
-HETATM 3077  O   HOH A 334      12.957  23.254  42.869  1.00 49.79           O  
-HETATM 3078  O   HOH A 335      32.236  28.956  16.981  1.00 60.91           O  
-HETATM 3079  O   HOH A 336      17.354  18.454  40.763  1.00 51.85           O  
-HETATM 3080  O   HOH A 337      40.793  38.575  16.040  1.00 51.57           O  
-HETATM 3081  O   HOH A 338      27.083  28.491  58.746  1.00 47.66           O  
-HETATM 3082  O   HOH A 339      20.256  32.906  62.726  1.00 58.72           O  
-HETATM 3083  O   HOH A 340      26.159  35.892  26.285  1.00 44.40           O  
-HETATM 3084  O   HOH A 341      19.097  16.384  53.812  1.00 47.83           O  
-HETATM 3085  O   HOH A 342      24.497  39.379  37.598  1.00 53.58           O  
-HETATM 3086  O   HOH A 343      15.913  21.681  41.003  1.00 54.13           O  
-HETATM 3087  O   HOH A 344      49.802  17.093  21.221  1.00 53.32           O  
-HETATM 3088  O   HOH A 345      22.898  11.928  42.446  1.00 50.01           O  
-HETATM 3089  O   HOH A 346      31.112  18.543  55.272  1.00 45.13           O  
-HETATM 3090  O   HOH A 347       8.596  21.886  42.878  1.00 46.82           O  
-HETATM 3091  O   HOH A 348      15.372  27.215  34.626  1.00 55.81           O  
-HETATM 3092  O   HOH A 349       7.863  38.940  56.544  1.00 45.53           O  
-HETATM 3093  O   HOH A 350      18.181  37.240  61.043  1.00 54.53           O  
-HETATM 3094  O   HOH A 351      15.546  24.209  27.184  1.00 53.59           O  
-HETATM 3095  O   HOH A 352      33.250  50.093  32.248  1.00 56.78           O  
-HETATM 3096  O   HOH A 353      32.353  32.420  15.716  1.00 58.64           O  
-HETATM 3097  O   HOH A 354       9.786  17.897  52.358  1.00 45.05           O  
-HETATM 3098  O   HOH A 355       9.053  37.287  59.839  1.00 51.50           O  
-HETATM 3099  O   HOH A 356      26.372  23.424  55.502  1.00 56.14           O  
-HETATM 3100  O   HOH A 357      23.576  31.156  35.357  1.00 48.29           O  
-HETATM 3101  O   HOH A 358      35.647  18.728  23.343  1.00 49.24           O  
-HETATM 3102  O   HOH A 359      27.419  15.231  57.127  1.00 51.15           O  
-HETATM 3103  O   HOH A 360      30.554  50.080  31.797  1.00 55.16           O  
-HETATM 3104  O   HOH A 361      32.598  18.306  15.780  1.00 58.73           O  
-HETATM 3105  O   HOH A 362       0.196  34.689  56.129  1.00 45.75           O  
-HETATM 3106  O   HOH A 363      24.957  27.948  20.768  1.00 58.79           O  
-HETATM 3107  O   HOH A 364      26.265  13.580  55.470  1.00 56.10           O  
-HETATM 3108  O   HOH A 365      14.165  35.234  41.255  1.00 58.23           O  
-HETATM 3109  O   HOH A 366      36.684  20.548  35.093  1.00 44.66           O  
-HETATM 3110  O   HOH A 367      24.745  30.399  20.110  1.00 60.31           O  
-HETATM 3111  O   HOH A 368      15.943  19.829  43.652  1.00 49.97           O  
-HETATM 3112  O   HOH A 369      28.263  47.487  32.723  1.00 51.31           O  
-HETATM 3113  O   HOH A 370      36.889  18.032  20.397  1.00 49.09           O  
-HETATM 3114  O   HOH A 371      13.644  37.432  46.534  1.00 54.12           O  
-HETATM 3115  O   HOH A 372       0.515  21.095  49.792  1.00 50.22           O  
-HETATM 3116  O   HOH A 373      26.980  11.634  57.032  1.00 60.59           O  
-HETATM 3117  O   HOH A 374      12.090  28.229  35.842  1.00 58.89           O  
-HETATM 3118  O   HOH A 375       9.236  33.758  62.295  1.00 62.27           O  
-HETATM 3119  O   HOH A 376      33.481  20.176  24.026  1.00 53.73           O  
-HETATM 3120  O   HOH A 377      33.669  17.611  34.875  1.00 54.13           O  
-HETATM 3121  O   HOH A 378      21.767  15.750  39.269  1.00 54.87           O  
-HETATM 3122  O   HOH B 189      41.891  27.346  40.247  1.00 17.13           O  
-HETATM 3123  O   HOH B 190      28.070  34.293  52.189  1.00 21.10           O  
-HETATM 3124  O   HOH B 191      44.665  23.200  40.197  1.00 24.25           O  
-HETATM 3125  O   HOH B 192      31.804  34.519  53.299  1.00 24.27           O  
-HETATM 3126  O   HOH B 193      28.655  38.814  53.848  1.00 20.71           O  
-HETATM 3127  O   HOH B 194      30.578  39.912  48.619  1.00 27.76           O  
-HETATM 3128  O   HOH B 195      28.637  33.124  54.734  1.00 19.55           O  
-HETATM 3129  O   HOH B 196      26.662  38.025  50.417  1.00 23.42           O  
-HETATM 3130  O   HOH B 197      50.612  41.704  63.834  1.00 26.36           O  
-HETATM 3131  O   HOH B 198      41.915  52.374  70.836  1.00 25.27           O  
-HETATM 3132  O   HOH B 199      45.391  36.728  54.040  1.00 24.63           O  
-HETATM 3133  O   HOH B 200      30.599  45.493  67.131  1.00 32.31           O  
-HETATM 3134  O   HOH B 201      46.144  35.752  22.299  1.00 26.29           O  
-HETATM 3135  O   HOH B 202      30.260  41.905  44.604  1.00 27.69           O  
-HETATM 3136  O   HOH B 203      44.465  35.586  56.413  1.00 26.86           O  
-HETATM 3137  O   HOH B 204      43.221  30.510  42.609  1.00 25.93           O  
-HETATM 3138  O   HOH B 205      46.253  46.147  69.238  1.00 25.73           O  
-HETATM 3139  O   HOH B 206      35.677  22.626  43.015  1.00 25.44           O  
-HETATM 3140  O   HOH B 207      34.767  44.460  51.580  1.00 25.96           O  
-HETATM 3141  O   HOH B 208      31.233  46.560  63.744  1.00 29.78           O  
-HETATM 3142  O   HOH B 209      38.572  30.633  56.862  1.00 29.83           O  
-HETATM 3143  O   HOH B 210      34.633  35.288  66.238  1.00 27.48           O  
-HETATM 3144  O   HOH B 211      34.248  17.525  43.315  1.00 33.25           O  
-HETATM 3145  O   HOH B 212      37.611  47.386  74.751  1.00 30.49           O  
-HETATM 3146  O   HOH B 213      41.338  53.214  48.470  1.00 31.28           O  
-HETATM 3147  O   HOH B 214      45.715  31.065  41.160  1.00 30.08           O  
-HETATM 3148  O   HOH B 215      29.377  30.137  58.185  1.00 35.23           O  
-HETATM 3149  O   HOH B 216      43.756  52.332  48.981  1.00 38.67           O  
-HETATM 3150  O   HOH B 217      51.749  42.406  52.378  1.00 38.18           O  
-HETATM 3151  O   HOH B 218      57.966  36.429  21.576  1.00 44.35           O  
-HETATM 3152  O   HOH B 219      37.128  28.293  57.131  1.00 33.10           O  
-HETATM 3153  O   HOH B 220      42.771  16.887  36.765  1.00 39.21           O  
-HETATM 3154  O   HOH B 221      61.768  40.828   9.365  1.00 30.07           O  
-HETATM 3155  O   HOH B 222      48.663  35.912  46.658  1.00 48.11           O  
-HETATM 3156  O   HOH B 223      51.597  44.577  62.303  1.00 30.22           O  
-HETATM 3157  O   HOH B 224      38.531  39.666  73.208  1.00 30.21           O  
-HETATM 3158  O   HOH B 225      47.750  37.235  49.552  1.00 34.96           O  
-HETATM 3159  O   HOH B 226      28.664  42.910  50.726  1.00 41.86           O  
-HETATM 3160  O   HOH B 227      48.942  46.577  68.536  1.00 27.37           O  
-HETATM 3161  O   HOH B 228      28.948  39.774  64.476  1.00 31.41           O  
-HETATM 3162  O   HOH B 229      49.136  32.037  44.183  1.00 35.02           O  
-HETATM 3163  O   HOH B 230      46.607  47.125  55.174  1.00 28.95           O  
-HETATM 3164  O   HOH B 231      41.970  54.734  66.669  1.00 37.40           O  
-HETATM 3165  O   HOH B 232      37.115  33.025  62.543  1.00 36.62           O  
-HETATM 3166  O   HOH B 233      36.506  44.250  74.478  1.00 36.98           O  
-HETATM 3167  O   HOH B 234      48.129  28.250  23.541  1.00 32.73           O  
-HETATM 3168  O   HOH B 235      43.911  43.837  73.658  1.00 34.04           O  
-HETATM 3169  O   HOH B 236      50.546  23.545  39.130  1.00 34.72           O  
-HETATM 3170  O   HOH B 237      48.048  47.955  49.116  1.00 30.69           O  
-HETATM 3171  O   HOH B 238      51.734  33.869  43.522  1.00 37.75           O  
-HETATM 3172  O   HOH B 239      29.995  44.218  54.906  1.00 40.29           O  
-HETATM 3173  O   HOH B 240      31.270  24.523  35.975  1.00 39.30           O  
-HETATM 3174  O   HOH B 241      45.533  33.964  60.681  1.00 49.42           O  
-HETATM 3175  O   HOH B 242      52.572  19.725  33.372  1.00 31.37           O  
-HETATM 3176  O   HOH B 243      47.754  30.406  48.134  1.00 38.35           O  
-HETATM 3177  O   HOH B 244      47.864  47.150  28.933  1.00 36.96           O  
-HETATM 3178  O   HOH B 245      51.877  30.843  42.740  1.00 35.83           O  
-HETATM 3179  O   HOH B 246      53.887  31.324  40.993  1.00 33.07           O  
-HETATM 3180  O   HOH B 247      46.591  49.397  47.540  1.00 41.76           O  
-HETATM 3181  O   HOH B 248      39.460  34.178  61.903  1.00 30.54           O  
-HETATM 3182  O   HOH B 249      48.217  51.697  63.055  1.00 45.23           O  
-HETATM 3183  O   HOH B 250      42.236  39.193  18.358  1.00 34.39           O  
-HETATM 3184  O   HOH B 251      53.431  38.685  49.025  1.00 36.34           O  
-HETATM 3185  O   HOH B 252      52.059  22.628  27.964  1.00 52.07           O  
-HETATM 3186  O   HOH B 253      53.338  30.157  48.867  1.00 49.73           O  
-HETATM 3187  O   HOH B 254      28.729  43.032  61.500  1.00 36.32           O  
-HETATM 3188  O   HOH B 255      33.667  39.792  71.622  1.00 30.52           O  
-HETATM 3189  O   HOH B 256      44.112  35.252  65.326  1.00 44.86           O  
-HETATM 3190  O   HOH B 257      48.511  46.821  19.290  1.00 40.11           O  
-HETATM 3191  O   HOH B 258      48.935  34.457  20.203  1.00 43.41           O  
-HETATM 3192  O   HOH B 259      56.538  35.215  43.348  1.00 41.46           O  
-HETATM 3193  O   HOH B 260      53.690  41.764  66.738  1.00 33.41           O  
-HETATM 3194  O   HOH B 261      31.139  45.301  52.324  1.00 43.92           O  
-HETATM 3195  O   HOH B 262      43.480  13.677  36.593  1.00 40.46           O  
-HETATM 3196  O   HOH B 263      42.409  36.623  19.645  1.00 31.86           O  
-HETATM 3197  O   HOH B 264      44.860  35.118  20.017  1.00 31.68           O  
-HETATM 3198  O   HOH B 265      30.422  46.424  39.877  1.00 36.56           O  
-HETATM 3199  O   HOH B 266      36.228  33.210  65.176  1.00 37.62           O  
-HETATM 3200  O   HOH B 267      48.541  46.740  56.790  1.00 39.24           O  
-HETATM 3201  O   HOH B 268      32.303  50.009  54.518  1.00 38.51           O  
-HETATM 3202  O   HOH B 269      46.265  26.365  22.671  1.00 39.14           O  
-HETATM 3203  O   HOH B 270      42.927  52.174  59.696  1.00 34.55           O  
-HETATM 3204  O   HOH B 271      37.197  53.316  42.750  1.00 37.87           O  
-HETATM 3205  O   HOH B 272      62.346  43.263   4.179  1.00 40.33           O  
-HETATM 3206  O   HOH B 273      43.848  33.237  53.799  1.00 40.23           O  
-HETATM 3207  O   HOH B 274      42.480  51.455  56.984  1.00 44.44           O  
-HETATM 3208  O   HOH B 275      44.612  27.341  20.869  1.00 37.54           O  
-HETATM 3209  O   HOH B 276      35.606  49.364  15.927  1.00 45.95           O  
-HETATM 3210  O   HOH B 277      49.399  24.022  24.042  1.00 44.39           O  
-HETATM 3211  O   HOH B 278      57.378  38.175  33.514  1.00 45.92           O  
-HETATM 3212  O   HOH B 279      55.187  52.820  70.999  1.00 45.78           O  
-HETATM 3213  O   HOH B 280      64.130  35.205   4.226  1.00 83.79           O  
-HETATM 3214  O   HOH B 281      48.180  30.003  21.338  1.00 37.44           O  
-HETATM 3215  O   HOH B 282      39.606  43.119  13.113  1.00 45.87           O  
-HETATM 3216  O   HOH B 283      40.830  49.434  30.832  1.00 42.57           O  
-HETATM 3217  O   HOH B 284      27.034  43.815  58.473  1.00 41.28           O  
-HETATM 3218  O   HOH B 285      54.381  33.709  43.290  1.00 46.78           O  
-HETATM 3219  O   HOH B 286      51.475  45.998  60.100  1.00 44.25           O  
-HETATM 3220  O   HOH B 287      47.103  14.540  35.891  1.00 40.04           O  
-HETATM 3221  O   HOH B 288      31.427  15.313  42.465  1.00 43.32           O  
-HETATM 3222  O   HOH B 289      52.352  24.416  41.904  1.00 55.09           O  
-HETATM 3223  O   HOH B 290      43.979  46.668  34.169  1.00 39.97           O  
-HETATM 3224  O   HOH B 291      54.713  28.102  27.620  1.00 47.59           O  
-HETATM 3225  O   HOH B 292      63.397  38.111   1.514  1.00 50.60           O  
-HETATM 3226  O   HOH B 293      29.207  45.473  62.455  1.00 48.87           O  
-HETATM 3227  O   HOH B 294      37.893  55.795  59.849  1.00 46.91           O  
-HETATM 3228  O   HOH B 295      38.834  35.625  72.523  1.00 42.76           O  
-HETATM 3229  O   HOH B 296      23.011  42.475  58.346  1.00 42.18           O  
-HETATM 3230  O   HOH B 297      47.170  31.665  50.602  1.00 42.06           O  
-HETATM 3231  O   HOH B 298      39.523  56.216  67.592  1.00 49.70           O  
-HETATM 3232  O   HOH B 299      52.467  41.258  54.923  1.00 50.28           O  
-HETATM 3233  O   HOH B 300      47.278  49.399  53.964  1.00 40.71           O  
-HETATM 3234  O   HOH B 301      27.225  41.660  64.002  1.00 48.58           O  
-HETATM 3235  O   HOH B 302      30.769  49.188  63.305  1.00 48.11           O  
-HETATM 3236  O   HOH B 303      44.155  53.954  53.216  1.00 45.04           O  
-HETATM 3237  O   HOH B 304      50.005  44.244  31.317  1.00 42.62           O  
-HETATM 3238  O   HOH B 305      31.678  16.296  37.008  1.00 45.41           O  
-HETATM 3239  O   HOH B 306      47.537  33.520  46.557  1.00 55.66           O  
-HETATM 3240  O   HOH B 307      48.180  38.167  70.198  1.00 64.12           O  
-HETATM 3241  O   HOH B 308      44.710  32.554  19.173  1.00 38.44           O  
-HETATM 3242  O   HOH B 309      45.441  29.985  20.041  1.00 38.47           O  
-HETATM 3243  O   HOH B 310      49.817  44.985  58.218  1.00 40.12           O  
-HETATM 3244  O   HOH B 311      57.467  34.122  20.579  1.00 52.30           O  
-HETATM 3245  O   HOH B 312      40.246  15.982  39.393  1.00 50.28           O  
-HETATM 3246  O   HOH B 313      39.038  19.601  35.125  1.00 41.44           O  
-HETATM 3247  O   HOH B 314      54.585  25.898  26.204  1.00 57.00           O  
-HETATM 3248  O   HOH B 315      41.164  54.070  56.547  1.00 41.23           O  
-HETATM 3249  O   HOH B 316      38.065  55.719  46.560  1.00 54.00           O  
-HETATM 3250  O   HOH B 317      51.568  49.043  63.125  1.00 51.30           O  
-HETATM 3251  O   HOH B 318      49.684  46.506  53.391  1.00 52.28           O  
-HETATM 3252  O   HOH B 319      28.119  46.084  60.003  1.00 46.79           O  
-HETATM 3253  O   HOH B 320      64.902  42.787  12.782  1.00 61.16           O  
-HETATM 3254  O   HOH B 321      42.798  48.814  33.513  1.00 56.06           O  
-HETATM 3255  O   HOH B 322      53.909  50.369  29.305  1.00 57.43           O  
-HETATM 3256  O   HOH B 323      49.717  47.094  31.613  1.00 52.54           O  
-HETATM 3257  O   HOH B 324      50.338  49.011  57.491  1.00 51.87           O  
-HETATM 3258  O   HOH B 325      44.522  51.576  55.585  1.00 52.15           O  
-HETATM 3259  O   HOH B 326      38.943  40.633  15.441  1.00 53.72           O  
-HETATM 3260  O   HOH B 327      63.330  35.735  -1.109  1.00 60.29           O  
-HETATM 3261  O   HOH B 328      42.990  54.528  69.992  1.00 42.80           O  
-HETATM 3262  O   HOH B 329      53.079  42.454  62.890  1.00 54.96           O  
-HETATM 3263  O   HOH B 330      28.682  43.891  46.025  1.00 52.65           O  
-HETATM 3264  O   HOH B 331      31.265  36.799  67.894  1.00 48.79           O  
-HETATM 3265  O   HOH B 332      54.903  45.505  24.406  1.00 53.86           O  
-HETATM 3266  O   HOH B 333      62.317  45.112  64.798  1.00 51.53           O  
-HETATM 3267  O   HOH B 334      37.193  40.448  13.407  1.00 56.15           O  
-HETATM 3268  O   HOH B 335      55.231  28.622  48.029  1.00 59.17           O  
-HETATM 3269  O   HOH B 336      47.601  45.713  22.679  1.00 42.18           O  
-HETATM 3270  O   HOH B 337      41.345  55.407  58.974  1.00 47.72           O  
-HETATM 3271  O   HOH B 338      51.124  50.738  33.723  1.00 52.49           O  
-HETATM 3272  O   HOH B 339      29.992  48.141  42.038  1.00 45.58           O  
-HETATM 3273  O   HOH B 340      47.239  47.962  21.676  1.00 53.32           O  
-HETATM 3274  O   HOH B 341      55.331  48.310  24.764  1.00 49.64           O  
-HETATM 3275  O   HOH B 342      42.500  56.632  71.370  1.00 49.36           O  
-HETATM 3276  O   HOH B 343      45.424  55.324  67.236  1.00 62.25           O  
-HETATM 3277  O   HOH B 344      26.026  37.102  64.131  1.00 49.44           O  
-HETATM 3278  O   HOH B 345      46.224  51.702  61.177  1.00 49.95           O  
-HETATM 3279  O   HOH B 346      52.573  39.882  68.073  1.00 52.63           O  
-HETATM 3280  O   HOH B 347      32.792  27.442  62.520  1.00 58.56           O  
-HETATM 3281  O   HOH B 348      53.744  33.537  23.849  1.00 50.44           O  
-HETATM 3282  O   HOH B 349      45.681  53.603  56.999  1.00 60.65           O  
-HETATM 3283  O   HOH B 350      31.484  30.865  55.451  1.00 38.81           O  
-HETATM 3284  O   HOH B 351      51.053  53.128  66.811  1.00 57.19           O  
-HETATM 3285  O   HOH B 352      55.118  48.780  38.311  1.00 60.74           O  
-HETATM 3286  O   HOH B 353      47.749  54.680  65.980  1.00 60.99           O  
-HETATM 3287  O   HOH B 354      57.069  49.218  26.761  1.00 54.27           O  
-HETATM 3288  O   HOH B 355      62.437  33.598  10.870  1.00 55.11           O  
-CONECT 2857 2858 2859                                                           
-CONECT 2858 2857                                                                
-CONECT 2859 2857 2860 2861                                                      
-CONECT 2860 2859                                                                
-CONECT 2861 2859 2862                                                           
-CONECT 2862 2861                                                                
-CONECT 2863 2864 2865                                                           
-CONECT 2864 2863                                                                
-CONECT 2865 2863 2866 2867                                                      
-CONECT 2866 2865                                                                
-CONECT 2867 2865 2868                                                           
-CONECT 2868 2867                                                                
-CONECT 2869 2870 2871                                                           
-CONECT 2870 2869                                                                
-CONECT 2871 2869 2872 2873                                                      
-CONECT 2872 2871                                                                
-CONECT 2873 2871 2874                                                           
-CONECT 2874 2873                                                                
-CONECT 2875 2876 2877                                                           
-CONECT 2876 2875                                                                
-CONECT 2877 2875 2878 2879                                                      
-CONECT 2878 2877                                                                
-CONECT 2879 2877 2880                                                           
-CONECT 2880 2879                                                                
-CONECT 2881 2882 2883 2884 2885                                                 
-CONECT 2882 2881                                                                
-CONECT 2883 2881                                                                
-CONECT 2884 2881                                                                
-CONECT 2885 2881                                                                
-CONECT 2886 2887 2898                                                           
-CONECT 2887 2886 2888                                                           
-CONECT 2888 2887 2889 2908                                                      
-CONECT 2889 2888 2899                                                           
-CONECT 2890 2891 2899 2906                                                      
-CONECT 2891 2890 2896 2900                                                      
-CONECT 2892 2893 2896                                                           
-CONECT 2893 2892 2894 2909                                                      
-CONECT 2894 2893 2895                                                           
-CONECT 2895 2894 2897                                                           
-CONECT 2896 2891 2892 2897                                                      
-CONECT 2897 2895 2896 2898                                                      
-CONECT 2898 2886 2897 2899                                                      
-CONECT 2899 2889 2890 2898                                                      
-CONECT 2900 2891 2901 2905                                                      
-CONECT 2901 2900 2902                                                           
-CONECT 2902 2901 2903                                                           
-CONECT 2903 2902 2904                                                           
-CONECT 2904 2903 2905                                                           
-CONECT 2905 2900 2904                                                           
-CONECT 2906 2890 2907                                                           
-CONECT 2907 2906                                                                
-CONECT 2908 2888                                                                
-CONECT 2909 2893                                                                
-CONECT 2910 2911 2912                                                           
-CONECT 2911 2910                                                                
-CONECT 2912 2910 2913 2914                                                      
-CONECT 2913 2912                                                                
-CONECT 2914 2912 2915                                                           
-CONECT 2915 2914                                                                
-CONECT 2916 2917 2918                                                           
-CONECT 2917 2916                                                                
-CONECT 2918 2916 2919 2920                                                      
-CONECT 2919 2918                                                                
-CONECT 2920 2918 2921                                                           
-CONECT 2921 2920                                                                
-CONECT 2922 2923 2924 2925 2926                                                 
-CONECT 2923 2922                                                                
-CONECT 2924 2922                                                                
-CONECT 2925 2922                                                                
-CONECT 2926 2922                                                                
-CONECT 2927 2928 2929 2930 2931                                                 
-CONECT 2928 2927                                                                
-CONECT 2929 2927                                                                
-CONECT 2930 2927                                                                
-CONECT 2931 2927                                                                
-MASTER      341    0   10   22    0    0   17    6 3286    2   75   30          
-END                                                                             
diff --git a/plip/test/pdb/3o1h.pdb b/plip/test/pdb/3o1h.pdb
deleted file mode 100644
index 494b500..0000000
--- a/plip/test/pdb/3o1h.pdb
+++ /dev/null
@@ -1,5090 +0,0 @@
-HEADER    SIGNALING PROTEIN                       21-JUL-10   3O1H              
-TITLE     CRYSTAL STRUCTURE OF THE TORS SENSOR DOMAIN - TORT COMPLEX IN THE     
-TITLE    2 PRESENCE OF TMAO                                                     
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: SENSOR PROTEIN TORS;                                       
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 FRAGMENT: SENSOR DOMAIN (UNP RESIDUES 51-322);                       
-COMPND   5 EC: 2.7.13.3;                                                        
-COMPND   6 ENGINEERED: YES;                                                     
-COMPND   7 MOL_ID: 2;                                                           
-COMPND   8 MOLECULE: PERIPLASMIC PROTEIN TORT;                                  
-COMPND   9 CHAIN: B;                                                            
-COMPND  10 FRAGMENT: UNP RESIDUES 31-329;                                       
-COMPND  11 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO PARAHAEMOLYTICUS;                        
-SOURCE   3 ORGANISM_TAXID: 670;                                                 
-SOURCE   4 STRAIN: EB10;                                                        
-SOURCE   5 GENE: TORS, VPA0675;                                                 
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;                                  
-SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-T;                               
-SOURCE  11 MOL_ID: 2;                                                           
-SOURCE  12 ORGANISM_SCIENTIFIC: VIBRIO PARAHAEMOLYTICUS;                        
-SOURCE  13 ORGANISM_TAXID: 670;                                                 
-SOURCE  14 STRAIN: EB10;                                                        
-SOURCE  15 GENE: TORT, VPA0674;                                                 
-SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ORIGAMIB DE3 PLYSS;                        
-SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PETDUET-T                                 
-KEYWDS    TMAO BOUND, TWO COMPONENT SENSOR, PERIPLASMIC BINDING PROTEIN, TMAO   
-KEYWDS   2 BINDING, SIGNALING PROTEIN                                           
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    J.O.MOORE,W.A.HENDRICKSON                                             
-REVDAT   3   27-MAR-13 3O1H    1       REMARK                                   
-REVDAT   2   26-DEC-12 3O1H    1       JRNL                                     
-REVDAT   1   21-DEC-11 3O1H    0                                                
-JRNL        AUTH   J.O.MOORE,W.A.HENDRICKSON                                    
-JRNL        TITL   AN ASYMMETRY-TO-SYMMETRY SWITCH IN SIGNAL TRANSMISSION BY    
-JRNL        TITL 2 THE HISTIDINE KINASE RECEPTOR FOR TMAO.                      
-JRNL        REF    STRUCTURE                     V.  20   729 2012              
-JRNL        REFN                   ISSN 0969-2126                               
-JRNL        PMID   22483119                                                     
-JRNL        DOI    10.1016/J.STR.2012.02.021                                    
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS 1.2                                              
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2075670.080                    
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.4                           
-REMARK   3   NUMBER OF REFLECTIONS             : 27210                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.218                           
-REMARK   3   FREE R VALUE                     : 0.252                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1366                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.20                        
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3844                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.3460                       
-REMARK   3   BIN FREE R VALUE                    : 0.4140                       
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 203                          
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 4517                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 5                                       
-REMARK   3   SOLVENT ATOMS            : 71                                      
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.30                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 4.56000                                              
-REMARK   3    B22 (A**2) : -6.44000                                             
-REMARK   3    B33 (A**2) : 1.88000                                              
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.57                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.45                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.71                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.008                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.70                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : FLAT MODEL                                           
-REMARK   3   KSOL        : 0.30                                                 
-REMARK   3   BSOL        : 17.39                                                
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NULL                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
-REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
-REMARK   3  PARAMETER FILE  3  : TMEAMO.PARAM                                   
-REMARK   3  PARAMETER FILE  4  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
-REMARK   3  TOPOLOGY FILE  2   : TMEAMO.TOP                                     
-REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
-REMARK   3  TOPOLOGY FILE  4   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
-REMARK   4                                                                      
-REMARK   4 3O1H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-10.                  
-REMARK 100 THE RCSB ID CODE IS RCSB060545.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-07                          
-REMARK 200  TEMPERATURE           (KELVIN) : 110                                
-REMARK 200  PH                             : 6.0-6.5                            
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : APS                                
-REMARK 200  BEAMLINE                       : 1-BM-C                             
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90020                            
-REMARK 200  MONOCHROMATOR                  : BENT GE(111)                       
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27210                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
-REMARK 200  DATA REDUNDANCY                : 5.200                              
-REMARK 200  R MERGE                    (I) : 0.10500                            
-REMARK 200  R SYM                      (I) : 0.11200                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.29400                            
-REMARK 200  R SYM FOR SHELL            (I) : 0.35100                            
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2469.000                           
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: CNS                                                   
-REMARK 200 STARTING MODEL: ISOPROPANOL BOUND STRUCTURE                          
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 5.90                                      
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 79.14                    
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4-0.8M CAACETATE, 4-7% BUTANOL, 0.1M   
-REMARK 280  MES PH6.0-6.5, 2MM TMAO, VAPOR DIFFUSION, HANGING DROP,             
-REMARK 280  TEMPERATURE 277.15K                                                 
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,-Y,Z+1/2                                             
-REMARK 290       3555   -X,Y,-Z+1/2                                             
-REMARK 290       4555   X,-Y,-Z                                                 
-REMARK 290       5555   X+1/2,Y+1/2,Z                                           
-REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
-REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
-REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.34750            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.34750            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       64.02950            
-REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      153.49200            
-REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       64.02950            
-REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      153.49200            
-REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.34750            
-REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       64.02950            
-REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      153.49200            
-REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       39.34750            
-REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       64.02950            
-REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      153.49200            
-REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000     -128.05900            
-REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       39.34750            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     GLY A    47                                                      
-REMARK 465     SER A    48                                                      
-REMARK 465     GLY A    49                                                      
-REMARK 465     THR A   320                                                      
-REMARK 465     THR A   321                                                      
-REMARK 465     THR A   322                                                      
-REMARK 465     LYS A   323                                                      
-REMARK 465     GLY B    26                                                      
-REMARK 465     SER B    27                                                      
-REMARK 465     GLY B    28                                                      
-REMARK 465     SER B    29                                                      
-REMARK 465     THR B   172                                                      
-REMARK 465     ARG B   173                                                      
-REMARK 465     GLY B   174                                                      
-REMARK 465     GLY B   175                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
-REMARK 500    GLU A 184   CD    GLU A 184   OE2     0.087                       
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASN A  74       43.17    -74.25                                   
-REMARK 500    GLU A  78       36.62    -76.03                                   
-REMARK 500    GLN A  79      -51.75   -130.49                                   
-REMARK 500    GLU A  83      -72.09    -86.65                                   
-REMARK 500    GLU A 105        9.37    -68.21                                   
-REMARK 500    ALA A 185       11.02    -63.62                                   
-REMARK 500    VAL A 201      -57.45   -122.13                                   
-REMARK 500    GLU A 257       85.66    -66.81                                   
-REMARK 500    ASP A 258       88.33   -165.70                                   
-REMARK 500    PRO A 259      -97.26    -26.94                                   
-REMARK 500    SER A 308       -7.56    -57.55                                   
-REMARK 500    LYS A 312      -18.76    -49.97                                   
-REMARK 500    ASP A 315     -159.58    -90.10                                   
-REMARK 500    ASP A 316      -22.80     63.40                                   
-REMARK 500    LEU B  40       50.71   -150.89                                   
-REMARK 500    TYR B  44      -76.38    -51.46                                   
-REMARK 500    TYR B 102       -3.55     55.45                                   
-REMARK 500    LEU B 106      -49.25    -29.97                                   
-REMARK 500    VAL B 119      -67.40     52.78                                   
-REMARK 500    SER B 129        1.90    -62.85                                   
-REMARK 500    LEU B 132       87.87    -57.80                                   
-REMARK 500    LYS B 188      118.14    -35.08                                   
-REMARK 500    ASN B 189       53.71     71.58                                   
-REMARK 500    SER B 190       23.22   -142.86                                   
-REMARK 500    ASP B 191       18.68     48.53                                   
-REMARK 500    ALA B 200      161.85    179.96                                   
-REMARK 500    ASN B 202       42.18    -90.45                                   
-REMARK 500    ASP B 241        3.40     58.02                                   
-REMARK 500    HIS B 244       -4.04     73.20                                   
-REMARK 500    GLU B 323      -34.50     67.48                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMO B 1                   
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 3I9Y   RELATED DB: PDB                                   
-REMARK 900 E. COLI TORS MONOMER STRUCTURE                                       
-REMARK 900 RELATED ID: 3I9W   RELATED DB: PDB                                   
-REMARK 900 V. PARAHAEMOLYTICUS TORS MONOMER STRUCTURE                           
-REMARK 900 RELATED ID: 3O1I   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 3O1J   RELATED DB: PDB                                   
-DBREF  3O1H A   51   322  UNP    Q87ID1   Q87ID1_VIBPA    51    322             
-DBREF  3O1H B   31   329  UNP    Q87ID2   Q87ID2_VIBPA    31    329             
-SEQADV 3O1H GLY A   47  UNP  Q87ID1              EXPRESSION TAG                 
-SEQADV 3O1H SER A   48  UNP  Q87ID1              EXPRESSION TAG                 
-SEQADV 3O1H GLY A   49  UNP  Q87ID1              EXPRESSION TAG                 
-SEQADV 3O1H SER A   50  UNP  Q87ID1              EXPRESSION TAG                 
-SEQADV 3O1H LYS A  323  UNP  Q87ID1              EXPRESSION TAG                 
-SEQADV 3O1H GLY B   26  UNP  Q87ID2              EXPRESSION TAG                 
-SEQADV 3O1H SER B   27  UNP  Q87ID2              EXPRESSION TAG                 
-SEQADV 3O1H GLY B   28  UNP  Q87ID2              EXPRESSION TAG                 
-SEQADV 3O1H SER B   29  UNP  Q87ID2              EXPRESSION TAG                 
-SEQADV 3O1H ASP B   30  UNP  Q87ID2              EXPRESSION TAG                 
-SEQRES   1 A  277  GLY SER GLY SER ALA MET ILE GLU ALA ARG GLN VAL SER          
-SEQRES   2 A  277  GLU LEU SER THR ARG ILE ILE SER SER VAL GLN MET LEU          
-SEQRES   3 A  277  SER ASN ALA GLN ASN GLU GLN GLU ARG LYS GLU ALA GLY          
-SEQRES   4 A  277  ARG VAL LEU PHE GLU GLN LEU GLU SER LEU LEU THR HIS          
-SEQRES   5 A  277  ILE LYS GLU LEU GLY GLY GLU SER PHE ASP SER LYS LEU          
-SEQRES   6 A  277  LEU ASP ALA LEU GLU SER ASN VAL GLN ASN VAL ILE ASN          
-SEQRES   7 A  277  ASN LEU ALA GLU LEU GLY VAL THR VAL GLU ARG LYS LEU          
-SEQRES   8 A  277  TRP LEU ALA LYS GLU ILE ASP THR ARG VAL GLU GLU MET          
-SEQRES   9 A  277  ARG LEU LEU SER GLU GLU LEU GLU GLN LEU THR ARG THR          
-SEQRES  10 A  277  GLN VAL GLN ASN THR SER THR ILE ALA VAL ALA ASN VAL          
-SEQRES  11 A  277  THR HIS ILE TYR ASP LEU LEU GLU ALA ASN LYS LYS ASP          
-SEQRES  12 A  277  GLN VAL TYR GLN ALA LEU ASP ALA LEU VAL GLU VAL ASP          
-SEQRES  13 A  277  LEU ASP LEU THR GLU ARG LEU HIS GLU LEU HIS LEU LEU          
-SEQRES  14 A  277  ALA PHE LYS MET LEU ASN GLN ILE GLU GLU ALA ARG THR          
-SEQRES  15 A  277  LEU THR ASN VAL ASP ARG ILE GLN GLN ILE GLN THR ALA          
-SEQRES  16 A  277  PHE GLU ASN ASN LEU LYS ILE MET LYS ARG ARG VAL LEU          
-SEQRES  17 A  277  ALA VAL GLU ASP PRO THR ARG SER LYS GLN MET SER GLN          
-SEQRES  18 A  277  LEU LEU THR GLU LEU GLY LYS ARG GLN VAL VAL PHE THR          
-SEQRES  19 A  277  ILE LEU LEU GLN GLN TYR GLU ASN ASN GLU GLN SER GLN          
-SEQRES  20 A  277  GLN LEU MET GLN LYS THR LEU GLU LEU PHE SER GLU LEU          
-SEQRES  21 A  277  ASN SER THR VAL ASN LYS LEU VAL ASP ASP SER ASN LYS          
-SEQRES  22 A  277  THR THR THR LYS                                              
-SEQRES   1 B  304  GLY SER GLY SER ASP GLU LYS ILE CYS ALA ILE TYR PRO          
-SEQRES   2 B  304  HIS LEU LYS ASP SER TYR TRP LEU SER VAL ASN TYR GLY          
-SEQRES   3 B  304  MET VAL SER GLU ALA GLU LYS GLN GLY VAL ASN LEU ARG          
-SEQRES   4 B  304  VAL LEU GLU ALA GLY GLY TYR PRO ASN LYS SER ARG GLN          
-SEQRES   5 B  304  GLU GLN GLN LEU ALA LEU CYS THR GLN TRP GLY ALA ASN          
-SEQRES   6 B  304  ALA ILE ILE LEU GLY THR VAL ASP PRO HIS ALA TYR GLU          
-SEQRES   7 B  304  HIS ASN LEU LYS SER TRP VAL GLY ASN THR PRO VAL PHE          
-SEQRES   8 B  304  ALA THR VAL ASN GLN LEU ASP LEU ASP GLU GLU GLN SER          
-SEQRES   9 B  304  THR LEU LEU LYS GLY GLU VAL GLY VAL ASP TRP TYR TRP          
-SEQRES  10 B  304  MET GLY TYR GLU ALA GLY LYS TYR LEU ALA GLU ARG HIS          
-SEQRES  11 B  304  PRO LYS GLY SER GLY LYS THR ASN ILE ALA LEU LEU LEU          
-SEQRES  12 B  304  GLY PRO ARG THR ARG GLY GLY THR LYS PRO VAL THR THR          
-SEQRES  13 B  304  GLY PHE TYR GLU ALA ILE LYS ASN SER ASP ILE HIS ILE          
-SEQRES  14 B  304  VAL ASP SER PHE TRP ALA ASP ASN ASP LYS GLU LEU GLN          
-SEQRES  15 B  304  ARG ASN LEU VAL GLN ARG VAL ILE ASP MET GLY ASN ILE          
-SEQRES  16 B  304  ASP TYR ILE VAL GLY SER ALA VAL ALA ILE GLU ALA ALA          
-SEQRES  17 B  304  ILE SER GLU LEU ARG SER ALA ASP LYS THR HIS ASP ILE          
-SEQRES  18 B  304  GLY LEU VAL SER VAL TYR LEU SER HIS GLY VAL TYR ARG          
-SEQRES  19 B  304  GLY LEU LEU ARG ASN LYS VAL LEU PHE ALA PRO THR ASP          
-SEQRES  20 B  304  LYS MET VAL GLN GLN GLY ARG LEU SER VAL MET GLN ALA          
-SEQRES  21 B  304  ALA HIS TYR LEU ARG HIS GLN PRO TYR GLU LYS GLN ALA          
-SEQRES  22 B  304  SER PRO ILE ILE LYS PRO LEU THR PRO LYS THR LEU HIS          
-SEQRES  23 B  304  ASP ASP THR ILE GLU GLU SER LEU SER PRO SER GLU TYR          
-SEQRES  24 B  304  ARG PRO THR PHE SER                                          
-HET    TMO  B   1       5                                                       
-HETNAM     TMO TRIMETHYLAMINE OXIDE                                             
-FORMUL   3  TMO    C3 H9 N O                                                    
-FORMUL   4  HOH   *71(H2 O)                                                     
-HELIX    1   1 SER A   50  ASN A   74  1                                  25    
-HELIX    2   2 GLN A   79  LEU A  102  1                                  24    
-HELIX    3   3 ASP A  108  ALA A  185  1                                  78    
-HELIX    4   4 LYS A  187  VAL A  201  1                                  15    
-HELIX    5   5 VAL A  201  ARG A  227  1                                  27    
-HELIX    6   6 ASN A  231  VAL A  256  1                                  26    
-HELIX    7   7 ASP A  258  ARG A  275  1                                  18    
-HELIX    8   8 VAL A  277  ASP A  315  1                                  39    
-HELIX    9   9 ASP B   42  GLN B   59  1                                  18    
-HELIX   10  10 ASN B   73  TRP B   87  1                                  15    
-HELIX   11  11 LEU B  106  GLY B  111  1                                   6    
-HELIX   12  12 TRP B  140  HIS B  155  1                                  16    
-HELIX   13  13 LYS B  177  LYS B  188  1                                  12    
-HELIX   14  14 ASP B  203  MET B  217  1                                  15    
-HELIX   15  15 SER B  226  ALA B  240  1                                  15    
-HELIX   16  16 GLY B  256  ARG B  263  1                                   8    
-HELIX   17  17 LYS B  273  ARG B  290  1                                  18    
-HELIX   18  18 THR B  306  LEU B  310  5                                   5    
-HELIX   19  19 HIS B  311  GLU B  317  1                                   7    
-SHEET    1   A 6 ASN B  62  GLU B  67  0                                        
-SHEET    2   A 6 LYS B  32  TYR B  37  1  N  TYR B  37   O  LEU B  66           
-SHEET    3   A 6 ALA B  91  LEU B  94  1  O  ALA B  91   N  CYS B  34           
-SHEET    4   A 6 VAL B 115  ALA B 117  1  O  PHE B 116   N  LEU B  94           
-SHEET    5   A 6 LEU B 132  VAL B 136  1  O  GLY B 134   N  ALA B 117           
-SHEET    6   A 6 GLN B 297  ALA B 298  1  O  ALA B 298   N  GLU B 135           
-SHEET    1   B 4 ILE B 192  TRP B 199  0                                        
-SHEET    2   B 4 THR B 162  GLY B 169  1  N  THR B 162   O  HIS B 193           
-SHEET    3   B 4 TYR B 222  GLY B 225  1  O  VAL B 224   N  ALA B 165           
-SHEET    4   B 4 GLY B 247  SER B 250  1  O  GLY B 247   N  ILE B 223           
-SHEET    1   C 2 ALA B 269  THR B 271  0                                        
-SHEET    2   C 2 LYS B 303  LEU B 305 -1  O  LYS B 303   N  THR B 271           
-SSBOND   1 CYS B   34    CYS B   84                          1555   1555  2.04  
-SITE     1 AC1  5 HOH B   3  TYR B  44  TRP B  45  TYR B  71                    
-SITE     2 AC1  5 VAL B 119                                                     
-CRYST1  128.059  306.984   78.695  90.00  90.00  90.00 C 2 2 21      8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.007809  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.003257  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.012707        0.00000                         
-ATOM      1  N   SER A  50     -59.989 -27.233  12.815  1.00 95.02           N  
-ATOM      2  CA  SER A  50     -59.116 -26.161  12.251  1.00 95.80           C  
-ATOM      3  C   SER A  50     -59.911 -24.885  12.020  1.00 96.24           C  
-ATOM      4  O   SER A  50     -59.340 -23.830  11.750  1.00 96.16           O  
-ATOM      5  CB  SER A  50     -58.494 -26.621  10.928  1.00 95.77           C  
-ATOM      6  OG  SER A  50     -57.657 -25.618  10.377  1.00 95.51           O  
-ATOM      7  N   ALA A  51     -61.233 -24.988  12.118  1.00 96.70           N  
-ATOM      8  CA  ALA A  51     -62.103 -23.833  11.927  1.00 96.61           C  
-ATOM      9  C   ALA A  51     -62.033 -22.938  13.160  1.00 96.65           C  
-ATOM     10  O   ALA A  51     -62.246 -21.730  13.077  1.00 96.92           O  
-ATOM     11  CB  ALA A  51     -63.537 -24.291  11.688  1.00 96.63           C  
-ATOM     12  N   MET A  52     -61.739 -23.539  14.307  1.00 96.57           N  
-ATOM     13  CA  MET A  52     -61.625 -22.784  15.545  1.00 96.53           C  
-ATOM     14  C   MET A  52     -60.280 -22.065  15.518  1.00 95.46           C  
-ATOM     15  O   MET A  52     -60.100 -21.036  16.164  1.00 94.66           O  
-ATOM     16  CB  MET A  52     -61.690 -23.725  16.750  1.00 98.70           C  
-ATOM     17  CG  MET A  52     -61.539 -23.024  18.096  1.00101.51           C  
-ATOM     18  SD  MET A  52     -61.297 -24.163  19.494  1.00104.80           S  
-ATOM     19  CE  MET A  52     -59.477 -24.238  19.577  1.00102.56           C  
-ATOM     20  N   ILE A  53     -59.342 -22.622  14.756  1.00 94.81           N  
-ATOM     21  CA  ILE A  53     -58.000 -22.054  14.620  1.00 94.22           C  
-ATOM     22  C   ILE A  53     -58.043 -20.690  13.934  1.00 93.58           C  
-ATOM     23  O   ILE A  53     -57.255 -19.797  14.256  1.00 93.59           O  
-ATOM     24  CB  ILE A  53     -57.073 -22.983  13.786  1.00 94.44           C  
-ATOM     25  CG1 ILE A  53     -56.926 -24.342  14.481  1.00 94.28           C  
-ATOM     26  CG2 ILE A  53     -55.712 -22.316  13.577  1.00 93.55           C  
-ATOM     27  CD1 ILE A  53     -56.010 -25.315  13.754  1.00 94.27           C  
-ATOM     28  N   GLU A  54     -58.965 -20.545  12.984  1.00 92.52           N  
-ATOM     29  CA  GLU A  54     -59.124 -19.306  12.229  1.00 90.95           C  
-ATOM     30  C   GLU A  54     -60.119 -18.359  12.891  1.00 90.08           C  
-ATOM     31  O   GLU A  54     -59.903 -17.151  12.921  1.00 90.29           O  
-ATOM     32  CB  GLU A  54     -59.588 -19.616  10.801  1.00 90.42           C  
-ATOM     33  CG  GLU A  54     -58.582 -19.275   9.698  1.00 90.18           C  
-ATOM     34  CD  GLU A  54     -57.322 -20.125   9.742  1.00 90.13           C  
-ATOM     35  OE1 GLU A  54     -56.517 -20.055   8.784  1.00 89.80           O  
-ATOM     36  OE2 GLU A  54     -57.132 -20.859  10.734  1.00 90.72           O  
-ATOM     37  N   ALA A  55     -61.208 -18.908  13.418  1.00 89.41           N  
-ATOM     38  CA  ALA A  55     -62.232 -18.098  14.074  1.00 89.04           C  
-ATOM     39  C   ALA A  55     -61.625 -17.178  15.130  1.00 88.72           C  
-ATOM     40  O   ALA A  55     -61.839 -15.965  15.104  1.00 88.94           O  
-ATOM     41  CB  ALA A  55     -63.280 -18.998  14.707  1.00 89.15           C  
-ATOM     42  N   ARG A  56     -60.878 -17.762  16.065  1.00 88.15           N  
-ATOM     43  CA  ARG A  56     -60.229 -16.986  17.116  1.00 86.90           C  
-ATOM     44  C   ARG A  56     -59.234 -16.036  16.464  1.00 85.60           C  
-ATOM     45  O   ARG A  56     -59.089 -14.894  16.891  1.00 86.33           O  
-ATOM     46  CB  ARG A  56     -59.517 -17.916  18.108  1.00 87.44           C  
-ATOM     47  CG  ARG A  56     -60.450 -18.553  19.147  1.00 88.49           C  
-ATOM     48  CD  ARG A  56     -59.909 -19.870  19.736  1.00 88.62           C  
-ATOM     49  NE  ARG A  56     -58.700 -19.732  20.554  1.00 88.89           N  
-ATOM     50  CZ  ARG A  56     -57.479 -19.459  20.089  1.00 88.24           C  
-ATOM     51  NH1 ARG A  56     -57.268 -19.281  18.791  1.00 87.21           N  
-ATOM     52  NH2 ARG A  56     -56.455 -19.383  20.930  1.00 87.38           N  
-ATOM     53  N   GLN A  57     -58.558 -16.516  15.425  1.00 83.75           N  
-ATOM     54  CA  GLN A  57     -57.594 -15.708  14.683  1.00 81.84           C  
-ATOM     55  C   GLN A  57     -58.280 -14.453  14.135  1.00 80.97           C  
-ATOM     56  O   GLN A  57     -57.686 -13.378  14.077  1.00 80.44           O  
-ATOM     57  CB  GLN A  57     -57.028 -16.524  13.524  1.00 81.75           C  
-ATOM     58  CG  GLN A  57     -55.653 -17.103  13.754  1.00 81.23           C  
-ATOM     59  CD  GLN A  57     -54.574 -16.049  13.679  1.00 81.76           C  
-ATOM     60  OE1 GLN A  57     -53.415 -16.350  13.387  1.00 81.61           O  
-ATOM     61  NE2 GLN A  57     -54.945 -14.802  13.948  1.00 81.85           N  
-ATOM     62  N   VAL A  58     -59.533 -14.608  13.721  1.00 80.14           N  
-ATOM     63  CA  VAL A  58     -60.319 -13.505  13.186  1.00 79.36           C  
-ATOM     64  C   VAL A  58     -60.724 -12.568  14.318  1.00 79.35           C  
-ATOM     65  O   VAL A  58     -60.476 -11.366  14.242  1.00 79.56           O  
-ATOM     66  CB  VAL A  58     -61.586 -14.031  12.465  1.00 79.53           C  
-ATOM     67  CG1 VAL A  58     -62.606 -12.917  12.300  1.00 79.68           C  
-ATOM     68  CG2 VAL A  58     -61.205 -14.592  11.105  1.00 78.62           C  
-ATOM     69  N   SER A  59     -61.343 -13.129  15.359  1.00 79.30           N  
-ATOM     70  CA  SER A  59     -61.784 -12.372  16.540  1.00 78.82           C  
-ATOM     71  C   SER A  59     -60.617 -11.540  17.103  1.00 78.83           C  
-ATOM     72  O   SER A  59     -60.804 -10.425  17.590  1.00 77.75           O  
-ATOM     73  CB  SER A  59     -62.308 -13.349  17.611  1.00 78.16           C  
-ATOM     74  OG  SER A  59     -62.959 -12.686  18.686  1.00 76.42           O  
-ATOM     75  N   GLU A  60     -59.414 -12.102  17.015  1.00 79.74           N  
-ATOM     76  CA  GLU A  60     -58.184 -11.465  17.484  1.00 80.48           C  
-ATOM     77  C   GLU A  60     -57.794 -10.279  16.594  1.00 80.00           C  
-ATOM     78  O   GLU A  60     -57.515  -9.184  17.093  1.00 81.13           O  
-ATOM     79  CB  GLU A  60     -57.057 -12.507  17.502  1.00 82.34           C  
-ATOM     80  CG  GLU A  60     -55.679 -11.999  17.906  1.00 84.80           C  
-ATOM     81  CD  GLU A  60     -54.647 -13.122  17.946  1.00 86.59           C  
-ATOM     82  OE1 GLU A  60     -54.877 -14.114  18.677  1.00 87.09           O  
-ATOM     83  OE2 GLU A  60     -53.610 -13.014  17.249  1.00 86.53           O  
-ATOM     84  N   LEU A  61     -57.768 -10.502  15.280  1.00 78.23           N  
-ATOM     85  CA  LEU A  61     -57.427  -9.447  14.334  1.00 75.79           C  
-ATOM     86  C   LEU A  61     -58.538  -8.410  14.235  1.00 75.41           C  
-ATOM     87  O   LEU A  61     -58.295  -7.284  13.819  1.00 75.32           O  
-ATOM     88  CB  LEU A  61     -57.148 -10.028  12.947  1.00 74.57           C  
-ATOM     89  CG  LEU A  61     -55.750 -10.599  12.719  1.00 73.64           C  
-ATOM     90  CD1 LEU A  61     -55.642 -11.154  11.312  1.00 73.23           C  
-ATOM     91  CD2 LEU A  61     -54.722  -9.511  12.929  1.00 72.45           C  
-ATOM     92  N   SER A  62     -59.758  -8.788  14.607  1.00 75.18           N  
-ATOM     93  CA  SER A  62     -60.871  -7.848  14.565  1.00 75.51           C  
-ATOM     94  C   SER A  62     -60.573  -6.704  15.521  1.00 76.68           C  
-ATOM     95  O   SER A  62     -60.685  -5.531  15.157  1.00 77.70           O  
-ATOM     96  CB  SER A  62     -62.178  -8.520  14.990  1.00 74.93           C  
-ATOM     97  OG  SER A  62     -62.661  -9.391  13.989  1.00 75.11           O  
-ATOM     98  N   THR A  63     -60.188  -7.056  16.747  1.00 77.37           N  
-ATOM     99  CA  THR A  63     -59.873  -6.068  17.773  1.00 77.14           C  
-ATOM    100  C   THR A  63     -58.704  -5.166  17.371  1.00 77.20           C  
-ATOM    101  O   THR A  63     -58.781  -3.950  17.525  1.00 77.73           O  
-ATOM    102  CB  THR A  63     -59.562  -6.752  19.123  1.00 77.30           C  
-ATOM    103  OG1 THR A  63     -60.725  -7.455  19.581  1.00 76.99           O  
-ATOM    104  CG2 THR A  63     -59.173  -5.719  20.167  1.00 76.99           C  
-ATOM    105  N   ARG A  64     -57.628  -5.748  16.852  1.00 77.01           N  
-ATOM    106  CA  ARG A  64     -56.481  -4.946  16.433  1.00 77.64           C  
-ATOM    107  C   ARG A  64     -56.824  -4.004  15.267  1.00 76.72           C  
-ATOM    108  O   ARG A  64     -56.175  -2.971  15.093  1.00 76.18           O  
-ATOM    109  CB  ARG A  64     -55.312  -5.862  16.059  1.00 79.70           C  
-ATOM    110  CG  ARG A  64     -54.744  -6.617  17.255  1.00 83.76           C  
-ATOM    111  CD  ARG A  64     -54.250  -8.009  16.878  1.00 87.14           C  
-ATOM    112  NE  ARG A  64     -53.101  -7.986  15.973  1.00 90.05           N  
-ATOM    113  CZ  ARG A  64     -52.604  -9.066  15.373  1.00 91.21           C  
-ATOM    114  NH1 ARG A  64     -53.161 -10.255  15.584  1.00 91.31           N  
-ATOM    115  NH2 ARG A  64     -51.557  -8.961  14.560  1.00 91.34           N  
-ATOM    116  N   ILE A  65     -57.842  -4.359  14.478  1.00 75.93           N  
-ATOM    117  CA  ILE A  65     -58.282  -3.530  13.346  1.00 74.34           C  
-ATOM    118  C   ILE A  65     -58.959  -2.278  13.907  1.00 73.53           C  
-ATOM    119  O   ILE A  65     -58.592  -1.152  13.556  1.00 73.61           O  
-ATOM    120  CB  ILE A  65     -59.321  -4.270  12.423  1.00 73.91           C  
-ATOM    121  CG1 ILE A  65     -58.660  -5.433  11.670  1.00 72.78           C  
-ATOM    122  CG2 ILE A  65     -59.926  -3.286  11.415  1.00 72.74           C  
-ATOM    123  CD1 ILE A  65     -57.708  -5.015  10.572  1.00 71.76           C  
-ATOM    124  N   ILE A  66     -59.950  -2.490  14.774  1.00 71.66           N  
-ATOM    125  CA  ILE A  66     -60.689  -1.396  15.401  1.00 69.93           C  
-ATOM    126  C   ILE A  66     -59.721  -0.378  16.002  1.00 70.65           C  
-ATOM    127  O   ILE A  66     -59.794   0.816  15.713  1.00 70.07           O  
-ATOM    128  CB  ILE A  66     -61.623  -1.922  16.519  1.00 67.80           C  
-ATOM    129  CG1 ILE A  66     -62.685  -2.847  15.921  1.00 66.80           C  
-ATOM    130  CG2 ILE A  66     -62.275  -0.762  17.242  1.00 66.33           C  
-ATOM    131  CD1 ILE A  66     -63.707  -3.361  16.923  1.00 64.79           C  
-ATOM    132  N   SER A  67     -58.804  -0.858  16.833  1.00 71.62           N  
-ATOM    133  CA  SER A  67     -57.831   0.022  17.465  1.00 72.82           C  
-ATOM    134  C   SER A  67     -56.919   0.676  16.439  1.00 73.43           C  
-ATOM    135  O   SER A  67     -56.117   1.545  16.776  1.00 74.64           O  
-ATOM    136  CB  SER A  67     -56.997  -0.747  18.494  1.00 72.76           C  
-ATOM    137  OG  SER A  67     -57.769  -1.049  19.648  1.00 72.86           O  
-ATOM    138  N   SER A  68     -57.037   0.255  15.185  1.00 73.78           N  
-ATOM    139  CA  SER A  68     -56.223   0.834  14.127  1.00 73.93           C  
-ATOM    140  C   SER A  68     -57.031   1.889  13.399  1.00 74.68           C  
-ATOM    141  O   SER A  68     -56.463   2.809  12.809  1.00 74.71           O  
-ATOM    142  CB  SER A  68     -55.759  -0.242  13.148  1.00 73.27           C  
-ATOM    143  OG  SER A  68     -54.834  -1.110  13.772  1.00 72.77           O  
-ATOM    144  N   VAL A  69     -58.358   1.753  13.443  1.00 75.64           N  
-ATOM    145  CA  VAL A  69     -59.238   2.724  12.796  1.00 76.79           C  
-ATOM    146  C   VAL A  69     -59.332   3.935  13.721  1.00 77.55           C  
-ATOM    147  O   VAL A  69     -59.305   5.079  13.262  1.00 77.71           O  
-ATOM    148  CB  VAL A  69     -60.671   2.151  12.530  1.00 76.52           C  
-ATOM    149  CG1 VAL A  69     -60.571   0.751  11.943  1.00 76.60           C  
-ATOM    150  CG2 VAL A  69     -61.501   2.145  13.801  1.00 76.08           C  
-ATOM    151  N   GLN A  70     -59.428   3.671  15.025  1.00 78.41           N  
-ATOM    152  CA  GLN A  70     -59.500   4.730  16.031  1.00 78.47           C  
-ATOM    153  C   GLN A  70     -58.232   5.546  15.810  1.00 77.74           C  
-ATOM    154  O   GLN A  70     -58.271   6.762  15.640  1.00 77.29           O  
-ATOM    155  CB  GLN A  70     -59.496   4.126  17.440  1.00 79.35           C  
-ATOM    156  CG  GLN A  70     -60.106   5.006  18.529  1.00 80.84           C  
-ATOM    157  CD  GLN A  70     -61.605   4.786  18.705  1.00 82.29           C  
-ATOM    158  OE1 GLN A  70     -62.063   3.655  18.897  1.00 82.00           O  
-ATOM    159  NE2 GLN A  70     -62.374   5.872  18.652  1.00 83.15           N  
-ATOM    160  N   MET A  71     -57.106   4.848  15.797  1.00 77.23           N  
-ATOM    161  CA  MET A  71     -55.822   5.480  15.568  1.00 77.76           C  
-ATOM    162  C   MET A  71     -55.856   6.308  14.287  1.00 76.81           C  
-ATOM    163  O   MET A  71     -55.364   7.433  14.263  1.00 76.92           O  
-ATOM    164  CB  MET A  71     -54.739   4.411  15.465  1.00 80.44           C  
-ATOM    165  CG  MET A  71     -53.977   4.168  16.754  1.00 82.98           C  
-ATOM    166  SD  MET A  71     -52.643   5.364  16.941  1.00 86.28           S  
-ATOM    167  CE  MET A  71     -51.460   4.744  15.697  1.00 84.40           C  
-ATOM    168  N   LEU A  72     -56.431   5.745  13.226  1.00 75.80           N  
-ATOM    169  CA  LEU A  72     -56.529   6.440  11.940  1.00 74.53           C  
-ATOM    170  C   LEU A  72     -57.328   7.719  12.126  1.00 74.85           C  
-ATOM    171  O   LEU A  72     -56.947   8.790  11.649  1.00 74.37           O  
-ATOM    172  CB  LEU A  72     -57.239   5.568  10.901  1.00 72.38           C  
-ATOM    173  CG  LEU A  72     -57.460   6.231   9.538  1.00 69.92           C  
-ATOM    174  CD1 LEU A  72     -56.155   6.241   8.768  1.00 69.22           C  
-ATOM    175  CD2 LEU A  72     -58.523   5.488   8.764  1.00 68.50           C  
-ATOM    176  N   SER A  73     -58.451   7.583  12.819  1.00 75.50           N  
-ATOM    177  CA  SER A  73     -59.334   8.699  13.098  1.00 76.38           C  
-ATOM    178  C   SER A  73     -58.541   9.857  13.701  1.00 77.63           C  
-ATOM    179  O   SER A  73     -58.403  10.920  13.093  1.00 78.30           O  
-ATOM    180  CB  SER A  73     -60.423   8.251  14.068  1.00 75.04           C  
-ATOM    181  OG  SER A  73     -61.235   9.332  14.469  1.00 74.68           O  
-ATOM    182  N   ASN A  74     -58.000   9.640  14.892  1.00 78.47           N  
-ATOM    183  CA  ASN A  74     -57.242  10.671  15.576  1.00 78.81           C  
-ATOM    184  C   ASN A  74     -55.853  10.918  14.994  1.00 79.60           C  
-ATOM    185  O   ASN A  74     -54.885  11.066  15.731  1.00 79.55           O  
-ATOM    186  CB  ASN A  74     -57.137  10.318  17.060  1.00 78.57           C  
-ATOM    187  CG  ASN A  74     -58.499  10.095  17.699  1.00 79.30           C  
-ATOM    188  OD1 ASN A  74     -59.389  10.942  17.600  1.00 79.22           O  
-ATOM    189  ND2 ASN A  74     -58.670   8.945  18.350  1.00 78.83           N  
-ATOM    190  N   ALA A  75     -55.758  10.963  13.671  1.00 81.20           N  
-ATOM    191  CA  ALA A  75     -54.484  11.225  13.014  1.00 83.61           C  
-ATOM    192  C   ALA A  75     -54.506  12.701  12.668  1.00 85.40           C  
-ATOM    193  O   ALA A  75     -55.583  13.267  12.467  1.00 85.32           O  
-ATOM    194  CB  ALA A  75     -54.347  10.390  11.754  1.00 82.71           C  
-ATOM    195  N   GLN A  76     -53.337  13.333  12.586  1.00 87.43           N  
-ATOM    196  CA  GLN A  76     -53.318  14.761  12.293  1.00 89.31           C  
-ATOM    197  C   GLN A  76     -52.693  15.247  10.990  1.00 89.74           C  
-ATOM    198  O   GLN A  76     -53.358  15.945  10.234  1.00 90.41           O  
-ATOM    199  CB  GLN A  76     -52.745  15.511  13.492  1.00 90.18           C  
-ATOM    200  CG  GLN A  76     -53.812  15.722  14.560  1.00 92.83           C  
-ATOM    201  CD  GLN A  76     -53.254  16.231  15.868  1.00 95.25           C  
-ATOM    202  OE1 GLN A  76     -52.542  17.236  15.899  1.00 97.09           O  
-ATOM    203  NE2 GLN A  76     -53.581  15.545  16.963  1.00 95.59           N  
-ATOM    204  N   ASN A  77     -51.440  14.912  10.707  1.00 90.30           N  
-ATOM    205  CA  ASN A  77     -50.857  15.358   9.438  1.00 91.00           C  
-ATOM    206  C   ASN A  77     -51.040  14.266   8.386  1.00 91.09           C  
-ATOM    207  O   ASN A  77     -51.495  13.168   8.705  1.00 91.39           O  
-ATOM    208  CB  ASN A  77     -49.369  15.690   9.592  1.00 92.25           C  
-ATOM    209  CG  ASN A  77     -48.577  14.557  10.214  1.00 94.43           C  
-ATOM    210  OD1 ASN A  77     -48.830  13.382   9.939  1.00 96.55           O  
-ATOM    211  ND2 ASN A  77     -47.599  14.904  11.043  1.00 95.01           N  
-ATOM    212  N   GLU A  78     -50.699  14.562   7.135  1.00 91.19           N  
-ATOM    213  CA  GLU A  78     -50.837  13.575   6.065  1.00 91.36           C  
-ATOM    214  C   GLU A  78     -49.716  12.546   6.158  1.00 91.39           C  
-ATOM    215  O   GLU A  78     -49.194  12.080   5.146  1.00 90.70           O  
-ATOM    216  CB  GLU A  78     -50.814  14.263   4.694  1.00 92.14           C  
-ATOM    217  CG  GLU A  78     -52.065  14.026   3.837  1.00 93.97           C  
-ATOM    218  CD  GLU A  78     -52.119  12.635   3.212  1.00 95.46           C  
-ATOM    219  OE1 GLU A  78     -53.116  12.331   2.517  1.00 95.44           O  
-ATOM    220  OE2 GLU A  78     -51.168  11.846   3.409  1.00 96.28           O  
-ATOM    221  N   GLN A  79     -49.350  12.211   7.394  1.00 92.19           N  
-ATOM    222  CA  GLN A  79     -48.306  11.230   7.680  1.00 92.93           C  
-ATOM    223  C   GLN A  79     -48.822  10.230   8.695  1.00 92.56           C  
-ATOM    224  O   GLN A  79     -48.738   9.026   8.482  1.00 92.53           O  
-ATOM    225  CB  GLN A  79     -47.049  11.911   8.216  1.00 93.94           C  
-ATOM    226  CG  GLN A  79     -46.079  12.297   7.124  1.00 96.47           C  
-ATOM    227  CD  GLN A  79     -45.569  11.083   6.373  1.00 98.20           C  
-ATOM    228  OE1 GLN A  79     -44.881  10.233   6.945  1.00 98.86           O  
-ATOM    229  NE2 GLN A  79     -45.912  10.988   5.088  1.00 98.47           N  
-ATOM    230  N   GLU A  80     -49.352  10.727   9.805  1.00 92.72           N  
-ATOM    231  CA  GLU A  80     -49.918   9.844  10.811  1.00 93.79           C  
-ATOM    232  C   GLU A  80     -51.111   9.165  10.153  1.00 93.65           C  
-ATOM    233  O   GLU A  80     -51.594   8.137  10.623  1.00 93.93           O  
-ATOM    234  CB  GLU A  80     -50.422  10.636  12.009  1.00 94.98           C  
-ATOM    235  CG  GLU A  80     -49.402  11.496  12.693  1.00 96.18           C  
-ATOM    236  CD  GLU A  80     -50.050  12.362  13.741  1.00 97.36           C  
-ATOM    237  OE1 GLU A  80     -50.565  11.807  14.739  1.00 97.69           O  
-ATOM    238  OE2 GLU A  80     -50.057  13.597  13.556  1.00 97.87           O  
-ATOM    239  N   ARG A  81     -51.594   9.774   9.073  1.00 93.23           N  
-ATOM    240  CA  ARG A  81     -52.730   9.250   8.327  1.00 92.50           C  
-ATOM    241  C   ARG A  81     -52.213   8.145   7.434  1.00 92.56           C  
-ATOM    242  O   ARG A  81     -52.772   7.048   7.398  1.00 93.06           O  
-ATOM    243  CB  ARG A  81     -53.363  10.353   7.476  1.00 91.90           C  
-ATOM    244  CG  ARG A  81     -54.804  10.086   7.101  1.00 91.24           C  
-ATOM    245  CD  ARG A  81     -54.942   9.150   5.918  1.00 90.68           C  
-ATOM    246  NE  ARG A  81     -54.688   9.829   4.651  1.00 89.82           N  
-ATOM    247  CZ  ARG A  81     -55.172   9.418   3.484  1.00 89.98           C  
-ATOM    248  NH1 ARG A  81     -55.937   8.334   3.426  1.00 90.09           N  
-ATOM    249  NH2 ARG A  81     -54.894  10.089   2.376  1.00 89.04           N  
-ATOM    250  N   LYS A  82     -51.134   8.448   6.717  1.00 92.01           N  
-ATOM    251  CA  LYS A  82     -50.506   7.478   5.829  1.00 91.40           C  
-ATOM    252  C   LYS A  82     -50.079   6.238   6.619  1.00 90.87           C  
-ATOM    253  O   LYS A  82     -50.047   5.139   6.079  1.00 90.95           O  
-ATOM    254  CB  LYS A  82     -49.283   8.098   5.137  1.00 91.37           C  
-ATOM    255  CG  LYS A  82     -49.406   8.250   3.614  1.00 91.84           C  
-ATOM    256  CD  LYS A  82     -48.844   7.049   2.840  1.00 92.92           C  
-ATOM    257  CE  LYS A  82     -49.596   5.741   3.123  1.00 94.02           C  
-ATOM    258  NZ  LYS A  82     -51.038   5.743   2.707  1.00 93.91           N  
-ATOM    259  N   GLU A  83     -49.775   6.403   7.902  1.00 90.36           N  
-ATOM    260  CA  GLU A  83     -49.339   5.269   8.706  1.00 90.07           C  
-ATOM    261  C   GLU A  83     -50.452   4.456   9.343  1.00 89.16           C  
-ATOM    262  O   GLU A  83     -50.706   3.324   8.934  1.00 89.91           O  
-ATOM    263  CB  GLU A  83     -48.372   5.733   9.795  1.00 91.19           C  
-ATOM    264  CG  GLU A  83     -47.677   4.596  10.543  1.00 93.28           C  
-ATOM    265  CD  GLU A  83     -47.005   3.594   9.607  1.00 94.97           C  
-ATOM    266  OE1 GLU A  83     -46.476   4.021   8.556  1.00 95.31           O  
-ATOM    267  OE2 GLU A  83     -46.982   2.382   9.928  1.00 95.65           O  
-ATOM    268  N   ALA A  84     -51.101   5.019  10.358  1.00 88.02           N  
-ATOM    269  CA  ALA A  84     -52.181   4.319  11.061  1.00 86.67           C  
-ATOM    270  C   ALA A  84     -53.086   3.598  10.063  1.00 85.14           C  
-ATOM    271  O   ALA A  84     -53.764   2.624  10.408  1.00 84.78           O  
-ATOM    272  CB  ALA A  84     -52.995   5.309  11.914  1.00 87.32           C  
-ATOM    273  N   GLY A  85     -53.082   4.085   8.824  1.00 82.92           N  
-ATOM    274  CA  GLY A  85     -53.882   3.474   7.783  1.00 80.81           C  
-ATOM    275  C   GLY A  85     -53.129   2.374   7.060  1.00 79.16           C  
-ATOM    276  O   GLY A  85     -53.686   1.321   6.771  1.00 79.05           O  
-ATOM    277  N   ARG A  86     -51.856   2.611   6.765  1.00 78.24           N  
-ATOM    278  CA  ARG A  86     -51.052   1.619   6.058  1.00 76.86           C  
-ATOM    279  C   ARG A  86     -50.986   0.325   6.862  1.00 74.46           C  
-ATOM    280  O   ARG A  86     -50.940  -0.758   6.285  1.00 74.65           O  
-ATOM    281  CB  ARG A  86     -49.647   2.157   5.808  1.00 78.98           C  
-ATOM    282  CG  ARG A  86     -48.819   1.337   4.843  1.00 81.62           C  
-ATOM    283  CD  ARG A  86     -47.405   1.222   5.377  1.00 85.18           C  
-ATOM    284  NE  ARG A  86     -47.401   0.493   6.646  1.00 88.49           N  
-ATOM    285  CZ  ARG A  86     -46.319   0.270   7.388  1.00 89.74           C  
-ATOM    286  NH1 ARG A  86     -45.133   0.719   6.996  1.00 90.14           N  
-ATOM    287  NH2 ARG A  86     -46.429  -0.399   8.531  1.00 90.07           N  
-ATOM    288  N   VAL A  87     -50.975   0.435   8.188  1.00 71.53           N  
-ATOM    289  CA  VAL A  87     -50.963  -0.752   9.030  1.00 69.88           C  
-ATOM    290  C   VAL A  87     -52.396  -1.281   9.116  1.00 69.34           C  
-ATOM    291  O   VAL A  87     -52.617  -2.470   9.328  1.00 69.58           O  
-ATOM    292  CB  VAL A  87     -50.467  -0.449  10.462  1.00 69.75           C  
-ATOM    293  CG1 VAL A  87     -49.162   0.326  10.411  1.00 70.39           C  
-ATOM    294  CG2 VAL A  87     -51.541   0.289  11.249  1.00 69.55           C  
-ATOM    295  N   LEU A  88     -53.369  -0.386   8.961  1.00 68.51           N  
-ATOM    296  CA  LEU A  88     -54.767  -0.786   8.997  1.00 67.02           C  
-ATOM    297  C   LEU A  88     -54.941  -1.685   7.793  1.00 67.18           C  
-ATOM    298  O   LEU A  88     -55.681  -2.658   7.829  1.00 67.74           O  
-ATOM    299  CB  LEU A  88     -55.684   0.431   8.876  1.00 65.15           C  
-ATOM    300  CG  LEU A  88     -57.185   0.131   8.775  1.00 64.26           C  
-ATOM    301  CD1 LEU A  88     -57.683  -0.568  10.035  1.00 65.09           C  
-ATOM    302  CD2 LEU A  88     -57.938   1.425   8.564  1.00 63.97           C  
-ATOM    303  N   PHE A  89     -54.230  -1.350   6.725  1.00 67.80           N  
-ATOM    304  CA  PHE A  89     -54.281  -2.122   5.496  1.00 68.54           C  
-ATOM    305  C   PHE A  89     -53.768  -3.540   5.712  1.00 69.01           C  
-ATOM    306  O   PHE A  89     -54.501  -4.515   5.527  1.00 69.94           O  
-ATOM    307  CB  PHE A  89     -53.439  -1.444   4.421  1.00 68.97           C  
-ATOM    308  CG  PHE A  89     -53.323  -2.241   3.159  1.00 69.92           C  
-ATOM    309  CD1 PHE A  89     -54.460  -2.575   2.422  1.00 69.77           C  
-ATOM    310  CD2 PHE A  89     -52.076  -2.659   2.703  1.00 70.08           C  
-ATOM    311  CE1 PHE A  89     -54.355  -3.315   1.246  1.00 70.08           C  
-ATOM    312  CE2 PHE A  89     -51.960  -3.398   1.529  1.00 70.68           C  
-ATOM    313  CZ  PHE A  89     -53.102  -3.728   0.799  1.00 70.56           C  
-ATOM    314  N   GLU A  90     -52.503  -3.654   6.093  1.00 68.52           N  
-ATOM    315  CA  GLU A  90     -51.914  -4.959   6.323  1.00 68.23           C  
-ATOM    316  C   GLU A  90     -52.749  -5.814   7.264  1.00 66.68           C  
-ATOM    317  O   GLU A  90     -52.988  -6.988   6.990  1.00 67.24           O  
-ATOM    318  CB  GLU A  90     -50.499  -4.804   6.863  1.00 69.95           C  
-ATOM    319  CG  GLU A  90     -49.511  -4.353   5.807  1.00 73.89           C  
-ATOM    320  CD  GLU A  90     -48.085  -4.356   6.320  1.00 77.07           C  
-ATOM    321  OE1 GLU A  90     -47.785  -3.568   7.244  1.00 78.08           O  
-ATOM    322  OE2 GLU A  90     -47.265  -5.152   5.805  1.00 79.20           O  
-ATOM    323  N   GLN A  91     -53.201  -5.231   8.365  1.00 64.86           N  
-ATOM    324  CA  GLN A  91     -54.013  -5.973   9.317  1.00 63.94           C  
-ATOM    325  C   GLN A  91     -55.277  -6.484   8.648  1.00 63.13           C  
-ATOM    326  O   GLN A  91     -55.852  -7.485   9.068  1.00 63.41           O  
-ATOM    327  CB  GLN A  91     -54.402  -5.088  10.492  1.00 64.70           C  
-ATOM    328  CG  GLN A  91     -53.239  -4.609  11.313  1.00 67.82           C  
-ATOM    329  CD  GLN A  91     -53.677  -3.685  12.426  1.00 70.29           C  
-ATOM    330  OE1 GLN A  91     -54.414  -4.089  13.333  1.00 70.65           O  
-ATOM    331  NE2 GLN A  91     -53.232  -2.428  12.362  1.00 70.87           N  
-ATOM    332  N   LEU A  92     -55.715  -5.788   7.607  1.00 62.01           N  
-ATOM    333  CA  LEU A  92     -56.921  -6.185   6.899  1.00 60.96           C  
-ATOM    334  C   LEU A  92     -56.632  -7.346   5.960  1.00 61.42           C  
-ATOM    335  O   LEU A  92     -57.390  -8.314   5.916  1.00 61.10           O  
-ATOM    336  CB  LEU A  92     -57.486  -5.006   6.107  1.00 58.70           C  
-ATOM    337  CG  LEU A  92     -58.864  -5.234   5.492  1.00 56.86           C  
-ATOM    338  CD1 LEU A  92     -59.900  -5.410   6.587  1.00 56.39           C  
-ATOM    339  CD2 LEU A  92     -59.216  -4.062   4.625  1.00 55.29           C  
-ATOM    340  N   GLU A  93     -55.534  -7.250   5.211  1.00 62.26           N  
-ATOM    341  CA  GLU A  93     -55.163  -8.312   4.281  1.00 63.03           C  
-ATOM    342  C   GLU A  93     -54.992  -9.629   5.028  1.00 61.97           C  
-ATOM    343  O   GLU A  93     -54.998 -10.696   4.415  1.00 63.63           O  
-ATOM    344  CB  GLU A  93     -53.869  -7.967   3.529  1.00 65.02           C  
-ATOM    345  CG  GLU A  93     -54.027  -6.909   2.423  1.00 70.90           C  
-ATOM    346  CD  GLU A  93     -54.871  -7.377   1.219  1.00 74.17           C  
-ATOM    347  OE1 GLU A  93     -56.070  -7.702   1.397  1.00 75.17           O  
-ATOM    348  OE2 GLU A  93     -54.334  -7.411   0.086  1.00 74.83           O  
-ATOM    349  N   SER A  94     -54.840  -9.557   6.348  1.00 59.09           N  
-ATOM    350  CA  SER A  94     -54.691 -10.759   7.156  1.00 55.69           C  
-ATOM    351  C   SER A  94     -56.065 -11.245   7.570  1.00 53.67           C  
-ATOM    352  O   SER A  94     -56.356 -12.430   7.517  1.00 52.75           O  
-ATOM    353  CB  SER A  94     -53.838 -10.477   8.387  1.00 55.85           C  
-ATOM    354  OG  SER A  94     -52.504 -10.197   8.007  1.00 56.49           O  
-ATOM    355  N   LEU A  95     -56.919 -10.324   7.985  1.00 52.85           N  
-ATOM    356  CA  LEU A  95     -58.265 -10.698   8.371  1.00 51.95           C  
-ATOM    357  C   LEU A  95     -58.895 -11.411   7.188  1.00 53.09           C  
-ATOM    358  O   LEU A  95     -59.827 -12.193   7.352  1.00 53.83           O  
-ATOM    359  CB  LEU A  95     -59.097  -9.464   8.708  1.00 49.79           C  
-ATOM    360  CG  LEU A  95     -60.606  -9.712   8.769  1.00 47.07           C  
-ATOM    361  CD1 LEU A  95     -60.911 -10.685   9.879  1.00 47.17           C  
-ATOM    362  CD2 LEU A  95     -61.337  -8.413   9.001  1.00 47.06           C  
-ATOM    363  N   LEU A  96     -58.385 -11.132   5.991  1.00 54.09           N  
-ATOM    364  CA  LEU A  96     -58.915 -11.754   4.782  1.00 55.20           C  
-ATOM    365  C   LEU A  96     -58.362 -13.155   4.542  1.00 56.13           C  
-ATOM    366  O   LEU A  96     -59.133 -14.094   4.331  1.00 56.43           O  
-ATOM    367  CB  LEU A  96     -58.670 -10.862   3.555  1.00 54.47           C  
-ATOM    368  CG  LEU A  96     -59.611  -9.649   3.484  1.00 54.24           C  
-ATOM    369  CD1 LEU A  96     -59.216  -8.713   2.352  1.00 53.74           C  
-ATOM    370  CD2 LEU A  96     -61.034 -10.140   3.303  1.00 52.78           C  
-ATOM    371  N   THR A  97     -57.041 -13.318   4.579  1.00 56.35           N  
-ATOM    372  CA  THR A  97     -56.483 -14.647   4.367  1.00 56.68           C  
-ATOM    373  C   THR A  97     -57.197 -15.617   5.312  1.00 58.09           C  
-ATOM    374  O   THR A  97     -57.691 -16.658   4.882  1.00 58.92           O  
-ATOM    375  CB  THR A  97     -54.964 -14.696   4.637  1.00 55.22           C  
-ATOM    376  OG1 THR A  97     -54.721 -14.621   6.044  1.00 54.31           O  
-ATOM    377  CG2 THR A  97     -54.262 -13.547   3.933  1.00 54.14           C  
-ATOM    378  N   HIS A  98     -57.271 -15.260   6.591  1.00 59.33           N  
-ATOM    379  CA  HIS A  98     -57.937 -16.096   7.584  1.00 61.66           C  
-ATOM    380  C   HIS A  98     -59.429 -16.250   7.304  1.00 62.74           C  
-ATOM    381  O   HIS A  98     -59.967 -17.348   7.395  1.00 63.37           O  
-ATOM    382  CB  HIS A  98     -57.759 -15.510   8.984  1.00 63.65           C  
-ATOM    383  CG  HIS A  98     -56.339 -15.471   9.449  1.00 66.29           C  
-ATOM    384  ND1 HIS A  98     -55.660 -16.596   9.863  1.00 67.63           N  
-ATOM    385  CD2 HIS A  98     -55.465 -14.441   9.563  1.00 67.31           C  
-ATOM    386  CE1 HIS A  98     -54.430 -16.261  10.214  1.00 68.53           C  
-ATOM    387  NE2 HIS A  98     -54.286 -14.959  10.041  1.00 68.05           N  
-ATOM    388  N   ILE A  99     -60.106 -15.154   6.977  1.00 64.27           N  
-ATOM    389  CA  ILE A  99     -61.540 -15.223   6.700  1.00 65.82           C  
-ATOM    390  C   ILE A  99     -61.792 -16.087   5.458  1.00 67.97           C  
-ATOM    391  O   ILE A  99     -62.888 -16.617   5.267  1.00 68.88           O  
-ATOM    392  CB  ILE A  99     -62.149 -13.810   6.476  1.00 64.39           C  
-ATOM    393  CG1 ILE A  99     -63.674 -13.886   6.469  1.00 63.42           C  
-ATOM    394  CG2 ILE A  99     -61.697 -13.242   5.149  1.00 64.08           C  
-ATOM    395  CD1 ILE A  99     -64.269 -14.181   7.809  1.00 64.40           C  
-ATOM    396  N   LYS A 100     -60.766 -16.232   4.622  1.00 69.26           N  
-ATOM    397  CA  LYS A 100     -60.874 -17.029   3.405  1.00 69.79           C  
-ATOM    398  C   LYS A 100     -60.778 -18.515   3.733  1.00 70.14           C  
-ATOM    399  O   LYS A 100     -61.646 -19.297   3.356  1.00 69.36           O  
-ATOM    400  CB  LYS A 100     -59.770 -16.633   2.424  1.00 69.50           C  
-ATOM    401  CG  LYS A 100     -60.234 -16.518   0.981  1.00 71.37           C  
-ATOM    402  CD  LYS A 100     -61.238 -15.363   0.757  1.00 73.55           C  
-ATOM    403  CE  LYS A 100     -62.678 -15.704   1.221  1.00 74.94           C  
-ATOM    404  NZ  LYS A 100     -63.706 -14.643   0.907  1.00 72.79           N  
-ATOM    405  N   GLU A 101     -59.715 -18.894   4.438  1.00 71.22           N  
-ATOM    406  CA  GLU A 101     -59.511 -20.280   4.835  1.00 72.93           C  
-ATOM    407  C   GLU A 101     -60.735 -20.773   5.583  1.00 74.05           C  
-ATOM    408  O   GLU A 101     -61.289 -21.821   5.261  1.00 74.62           O  
-ATOM    409  CB  GLU A 101     -58.276 -20.402   5.727  1.00 73.37           C  
-ATOM    410  CG  GLU A 101     -56.968 -20.246   4.978  1.00 75.07           C  
-ATOM    411  CD  GLU A 101     -56.815 -21.278   3.877  1.00 76.28           C  
-ATOM    412  OE1 GLU A 101     -56.885 -22.490   4.184  1.00 77.83           O  
-ATOM    413  OE2 GLU A 101     -56.628 -20.882   2.706  1.00 75.80           O  
-ATOM    414  N   LEU A 102     -61.153 -20.010   6.588  1.00 75.27           N  
-ATOM    415  CA  LEU A 102     -62.334 -20.354   7.369  1.00 76.01           C  
-ATOM    416  C   LEU A 102     -63.522 -20.457   6.419  1.00 77.26           C  
-ATOM    417  O   LEU A 102     -64.544 -21.056   6.748  1.00 77.42           O  
-ATOM    418  CB  LEU A 102     -62.608 -19.275   8.424  1.00 75.00           C  
-ATOM    419  CG  LEU A 102     -64.011 -19.259   9.043  1.00 74.76           C  
-ATOM    420  CD1 LEU A 102     -64.289 -20.578   9.728  1.00 75.10           C  
-ATOM    421  CD2 LEU A 102     -64.129 -18.118  10.033  1.00 75.10           C  
-ATOM    422  N   GLY A 103     -63.378 -19.868   5.236  1.00 78.41           N  
-ATOM    423  CA  GLY A 103     -64.447 -19.905   4.256  1.00 79.93           C  
-ATOM    424  C   GLY A 103     -64.546 -21.248   3.561  1.00 81.12           C  
-ATOM    425  O   GLY A 103     -65.402 -21.456   2.700  1.00 81.62           O  
-ATOM    426  N   GLY A 104     -63.664 -22.168   3.934  1.00 81.80           N  
-ATOM    427  CA  GLY A 104     -63.684 -23.481   3.325  1.00 82.46           C  
-ATOM    428  C   GLY A 104     -64.293 -24.529   4.231  1.00 82.72           C  
-ATOM    429  O   GLY A 104     -64.835 -25.518   3.751  1.00 83.08           O  
-ATOM    430  N   GLU A 105     -64.218 -24.308   5.540  1.00 82.99           N  
-ATOM    431  CA  GLU A 105     -64.747 -25.258   6.516  1.00 83.81           C  
-ATOM    432  C   GLU A 105     -66.270 -25.382   6.521  1.00 83.32           C  
-ATOM    433  O   GLU A 105     -66.842 -26.011   7.415  1.00 83.38           O  
-ATOM    434  CB  GLU A 105     -64.268 -24.893   7.924  1.00 85.47           C  
-ATOM    435  CG  GLU A 105     -62.758 -24.721   8.060  1.00 87.91           C  
-ATOM    436  CD  GLU A 105     -61.979 -26.005   7.820  1.00 89.06           C  
-ATOM    437  OE1 GLU A 105     -62.053 -26.554   6.698  1.00 89.28           O  
-ATOM    438  OE2 GLU A 105     -61.288 -26.460   8.759  1.00 89.51           O  
-ATOM    439  N   SER A 106     -66.924 -24.778   5.533  1.00 82.89           N  
-ATOM    440  CA  SER A 106     -68.380 -24.854   5.426  1.00 82.96           C  
-ATOM    441  C   SER A 106     -68.856 -24.562   4.013  1.00 82.70           C  
-ATOM    442  O   SER A 106     -68.196 -23.840   3.261  1.00 82.25           O  
-ATOM    443  CB  SER A 106     -69.059 -23.879   6.391  1.00 83.12           C  
-ATOM    444  OG  SER A 106     -70.469 -23.917   6.222  1.00 82.65           O  
-ATOM    445  N   PHE A 107     -70.007 -25.128   3.659  1.00 82.58           N  
-ATOM    446  CA  PHE A 107     -70.572 -24.929   2.336  1.00 82.43           C  
-ATOM    447  C   PHE A 107     -72.047 -24.591   2.363  1.00 81.93           C  
-ATOM    448  O   PHE A 107     -72.761 -24.826   1.390  1.00 82.02           O  
-ATOM    449  CB  PHE A 107     -70.325 -26.160   1.466  1.00 82.34           C  
-ATOM    450  CG  PHE A 107     -68.893 -26.321   1.069  1.00 84.20           C  
-ATOM    451  CD1 PHE A 107     -68.239 -25.306   0.363  1.00 85.97           C  
-ATOM    452  CD2 PHE A 107     -68.178 -27.459   1.427  1.00 84.12           C  
-ATOM    453  CE1 PHE A 107     -66.886 -25.419   0.020  1.00 86.36           C  
-ATOM    454  CE2 PHE A 107     -66.826 -27.588   1.091  1.00 85.48           C  
-ATOM    455  CZ  PHE A 107     -66.178 -26.564   0.385  1.00 86.52           C  
-ATOM    456  N   ASP A 108     -72.503 -24.035   3.482  1.00 81.23           N  
-ATOM    457  CA  ASP A 108     -73.898 -23.641   3.601  1.00 80.95           C  
-ATOM    458  C   ASP A 108     -74.101 -22.360   2.799  1.00 81.26           C  
-ATOM    459  O   ASP A 108     -73.574 -21.302   3.151  1.00 81.58           O  
-ATOM    460  CB  ASP A 108     -74.275 -23.404   5.061  1.00 80.13           C  
-ATOM    461  CG  ASP A 108     -75.692 -22.900   5.212  1.00 79.61           C  
-ATOM    462  OD1 ASP A 108     -76.611 -23.529   4.648  1.00 78.86           O  
-ATOM    463  OD2 ASP A 108     -75.890 -21.873   5.892  1.00 80.62           O  
-ATOM    464  N   SER A 109     -74.867 -22.468   1.717  1.00 81.27           N  
-ATOM    465  CA  SER A 109     -75.138 -21.339   0.829  1.00 80.45           C  
-ATOM    466  C   SER A 109     -75.553 -20.079   1.593  1.00 79.95           C  
-ATOM    467  O   SER A 109     -74.993 -19.001   1.382  1.00 80.44           O  
-ATOM    468  CB  SER A 109     -76.228 -21.726  -0.181  1.00 80.03           C  
-ATOM    469  OG  SER A 109     -76.235 -20.853  -1.299  1.00 79.64           O  
-ATOM    470  N   LYS A 110     -76.526 -20.228   2.488  1.00 78.55           N  
-ATOM    471  CA  LYS A 110     -77.037 -19.111   3.280  1.00 76.30           C  
-ATOM    472  C   LYS A 110     -75.962 -18.404   4.119  1.00 73.90           C  
-ATOM    473  O   LYS A 110     -75.939 -17.174   4.197  1.00 72.80           O  
-ATOM    474  CB  LYS A 110     -78.175 -19.609   4.182  1.00 77.02           C  
-ATOM    475  CG  LYS A 110     -78.935 -18.513   4.903  1.00 78.08           C  
-ATOM    476  CD  LYS A 110     -80.110 -19.076   5.686  1.00 78.52           C  
-ATOM    477  CE  LYS A 110     -80.840 -17.971   6.438  1.00 78.85           C  
-ATOM    478  NZ  LYS A 110     -82.029 -18.470   7.179  1.00 78.50           N  
-ATOM    479  N   LEU A 111     -75.074 -19.179   4.737  1.00 71.79           N  
-ATOM    480  CA  LEU A 111     -74.015 -18.616   5.573  1.00 69.94           C  
-ATOM    481  C   LEU A 111     -72.804 -18.104   4.799  1.00 69.05           C  
-ATOM    482  O   LEU A 111     -72.289 -17.025   5.091  1.00 69.06           O  
-ATOM    483  CB  LEU A 111     -73.553 -19.639   6.616  1.00 68.60           C  
-ATOM    484  CG  LEU A 111     -74.040 -19.387   8.046  1.00 67.09           C  
-ATOM    485  CD1 LEU A 111     -75.560 -19.479   8.112  1.00 66.55           C  
-ATOM    486  CD2 LEU A 111     -73.396 -20.395   8.976  1.00 66.65           C  
-ATOM    487  N   LEU A 112     -72.337 -18.876   3.825  1.00 67.69           N  
-ATOM    488  CA  LEU A 112     -71.192 -18.448   3.037  1.00 65.87           C  
-ATOM    489  C   LEU A 112     -71.454 -17.104   2.363  1.00 66.18           C  
-ATOM    490  O   LEU A 112     -70.530 -16.318   2.165  1.00 66.12           O  
-ATOM    491  CB  LEU A 112     -70.843 -19.496   1.983  1.00 63.04           C  
-ATOM    492  CG  LEU A 112     -69.728 -20.449   2.395  1.00 60.87           C  
-ATOM    493  CD1 LEU A 112     -69.436 -21.431   1.272  1.00 61.06           C  
-ATOM    494  CD2 LEU A 112     -68.493 -19.645   2.722  1.00 59.68           C  
-ATOM    495  N   ASP A 113     -72.709 -16.839   2.008  1.00 66.42           N  
-ATOM    496  CA  ASP A 113     -73.045 -15.572   1.371  1.00 67.18           C  
-ATOM    497  C   ASP A 113     -73.147 -14.483   2.420  1.00 66.67           C  
-ATOM    498  O   ASP A 113     -72.676 -13.365   2.211  1.00 67.51           O  
-ATOM    499  CB  ASP A 113     -74.356 -15.676   0.582  1.00 69.46           C  
-ATOM    500  CG  ASP A 113     -74.156 -16.278  -0.812  1.00 72.77           C  
-ATOM    501  OD1 ASP A 113     -73.252 -15.811  -1.551  1.00 73.30           O  
-ATOM    502  OD2 ASP A 113     -74.907 -17.214  -1.173  1.00 73.96           O  
-ATOM    503  N   ALA A 114     -73.754 -14.810   3.557  1.00 65.68           N  
-ATOM    504  CA  ALA A 114     -73.883 -13.845   4.642  1.00 63.38           C  
-ATOM    505  C   ALA A 114     -72.491 -13.461   5.152  1.00 61.86           C  
-ATOM    506  O   ALA A 114     -72.324 -12.414   5.762  1.00 62.70           O  
-ATOM    507  CB  ALA A 114     -74.716 -14.425   5.771  1.00 63.23           C  
-ATOM    508  N   LEU A 115     -71.496 -14.310   4.910  1.00 59.51           N  
-ATOM    509  CA  LEU A 115     -70.136 -14.000   5.333  1.00 57.39           C  
-ATOM    510  C   LEU A 115     -69.509 -13.060   4.306  1.00 58.03           C  
-ATOM    511  O   LEU A 115     -68.954 -12.021   4.666  1.00 58.14           O  
-ATOM    512  CB  LEU A 115     -69.281 -15.267   5.441  1.00 55.08           C  
-ATOM    513  CG  LEU A 115     -67.814 -15.009   5.821  1.00 53.21           C  
-ATOM    514  CD1 LEU A 115     -67.735 -14.530   7.259  1.00 53.40           C  
-ATOM    515  CD2 LEU A 115     -66.986 -16.263   5.649  1.00 51.26           C  
-ATOM    516  N   GLU A 116     -69.597 -13.435   3.028  1.00 59.21           N  
-ATOM    517  CA  GLU A 116     -69.043 -12.630   1.935  1.00 59.28           C  
-ATOM    518  C   GLU A 116     -69.555 -11.211   2.075  1.00 57.58           C  
-ATOM    519  O   GLU A 116     -68.840 -10.242   1.795  1.00 57.15           O  
-ATOM    520  CB  GLU A 116     -69.485 -13.180   0.568  1.00 62.41           C  
-ATOM    521  CG  GLU A 116     -69.084 -12.294  -0.630  1.00 66.91           C  
-ATOM    522  CD  GLU A 116     -69.701 -12.731  -1.966  1.00 69.87           C  
-ATOM    523  OE1 GLU A 116     -69.399 -12.085  -2.997  1.00 70.90           O  
-ATOM    524  OE2 GLU A 116     -70.485 -13.710  -1.993  1.00 72.41           O  
-ATOM    525  N   SER A 117     -70.803 -11.112   2.523  1.00 54.75           N  
-ATOM    526  CA  SER A 117     -71.472  -9.836   2.697  1.00 52.30           C  
-ATOM    527  C   SER A 117     -70.938  -9.044   3.885  1.00 51.23           C  
-ATOM    528  O   SER A 117     -70.638  -7.859   3.760  1.00 50.77           O  
-ATOM    529  CB  SER A 117     -72.966 -10.074   2.854  1.00 51.64           C  
-ATOM    530  OG  SER A 117     -73.675  -8.873   2.649  1.00 54.13           O  
-ATOM    531  N   ASN A 118     -70.818  -9.704   5.034  1.00 50.56           N  
-ATOM    532  CA  ASN A 118     -70.321  -9.068   6.250  1.00 48.60           C  
-ATOM    533  C   ASN A 118     -68.910  -8.544   6.090  1.00 47.06           C  
-ATOM    534  O   ASN A 118     -68.545  -7.544   6.700  1.00 48.39           O  
-ATOM    535  CB  ASN A 118     -70.355 -10.048   7.422  1.00 49.31           C  
-ATOM    536  CG  ASN A 118     -71.765 -10.341   7.891  1.00 51.20           C  
-ATOM    537  OD1 ASN A 118     -71.971 -11.111   8.827  1.00 53.99           O  
-ATOM    538  ND2 ASN A 118     -72.747  -9.724   7.243  1.00 50.99           N  
-ATOM    539  N   VAL A 119     -68.115  -9.218   5.272  1.00 44.31           N  
-ATOM    540  CA  VAL A 119     -66.747  -8.789   5.064  1.00 42.38           C  
-ATOM    541  C   VAL A 119     -66.679  -7.567   4.160  1.00 42.22           C  
-ATOM    542  O   VAL A 119     -65.837  -6.692   4.359  1.00 41.38           O  
-ATOM    543  CB  VAL A 119     -65.897  -9.921   4.457  1.00 41.54           C  
-ATOM    544  CG1 VAL A 119     -64.466  -9.442   4.222  1.00 38.39           C  
-ATOM    545  CG2 VAL A 119     -65.911 -11.119   5.388  1.00 40.67           C  
-ATOM    546  N   GLN A 120     -67.564  -7.491   3.172  1.00 42.43           N  
-ATOM    547  CA  GLN A 120     -67.536  -6.345   2.268  1.00 42.65           C  
-ATOM    548  C   GLN A 120     -67.961  -5.088   3.005  1.00 42.80           C  
-ATOM    549  O   GLN A 120     -67.305  -4.048   2.891  1.00 43.57           O  
-ATOM    550  CB  GLN A 120     -68.442  -6.562   1.053  1.00 41.92           C  
-ATOM    551  CG  GLN A 120     -68.218  -5.529  -0.043  1.00 41.97           C  
-ATOM    552  CD  GLN A 120     -66.781  -5.514  -0.556  1.00 43.66           C  
-ATOM    553  OE1 GLN A 120     -66.196  -4.452  -0.765  1.00 44.28           O  
-ATOM    554  NE2 GLN A 120     -66.212  -6.696  -0.771  1.00 44.36           N  
-ATOM    555  N   ASN A 121     -69.057  -5.190   3.757  1.00 41.85           N  
-ATOM    556  CA  ASN A 121     -69.568  -4.069   4.532  1.00 40.86           C  
-ATOM    557  C   ASN A 121     -68.467  -3.550   5.444  1.00 40.81           C  
-ATOM    558  O   ASN A 121     -68.255  -2.337   5.541  1.00 42.03           O  
-ATOM    559  CB  ASN A 121     -70.775  -4.507   5.350  1.00 41.65           C  
-ATOM    560  CG  ASN A 121     -71.991  -4.746   4.487  1.00 44.00           C  
-ATOM    561  OD1 ASN A 121     -71.870  -5.212   3.356  1.00 46.11           O  
-ATOM    562  ND2 ASN A 121     -73.172  -4.436   5.013  1.00 45.07           N  
-ATOM    563  N   VAL A 122     -67.759  -4.465   6.104  1.00 38.35           N  
-ATOM    564  CA  VAL A 122     -66.670  -4.071   6.980  1.00 36.15           C  
-ATOM    565  C   VAL A 122     -65.572  -3.394   6.167  1.00 37.06           C  
-ATOM    566  O   VAL A 122     -64.899  -2.492   6.659  1.00 38.76           O  
-ATOM    567  CB  VAL A 122     -66.081  -5.282   7.729  1.00 34.88           C  
-ATOM    568  CG1 VAL A 122     -64.729  -4.927   8.343  1.00 32.86           C  
-ATOM    569  CG2 VAL A 122     -67.047  -5.723   8.818  1.00 34.55           C  
-ATOM    570  N   ILE A 123     -65.388  -3.813   4.920  1.00 37.40           N  
-ATOM    571  CA  ILE A 123     -64.354  -3.202   4.093  1.00 37.50           C  
-ATOM    572  C   ILE A 123     -64.768  -1.823   3.612  1.00 37.63           C  
-ATOM    573  O   ILE A 123     -63.981  -0.882   3.687  1.00 37.86           O  
-ATOM    574  CB  ILE A 123     -63.985  -4.087   2.883  1.00 37.39           C  
-ATOM    575  CG1 ILE A 123     -63.097  -5.237   3.353  1.00 37.66           C  
-ATOM    576  CG2 ILE A 123     -63.248  -3.272   1.832  1.00 34.80           C  
-ATOM    577  CD1 ILE A 123     -62.768  -6.249   2.274  1.00 39.09           C  
-ATOM    578  N   ASN A 124     -65.996  -1.693   3.124  1.00 38.03           N  
-ATOM    579  CA  ASN A 124     -66.465  -0.394   2.654  1.00 39.38           C  
-ATOM    580  C   ASN A 124     -66.427   0.616   3.780  1.00 40.76           C  
-ATOM    581  O   ASN A 124     -66.181   1.800   3.551  1.00 42.46           O  
-ATOM    582  CB  ASN A 124     -67.901  -0.460   2.150  1.00 38.55           C  
-ATOM    583  CG  ASN A 124     -68.073  -1.426   1.029  1.00 36.62           C  
-ATOM    584  OD1 ASN A 124     -67.121  -1.765   0.328  1.00 36.58           O  
-ATOM    585  ND2 ASN A 124     -69.298  -1.871   0.835  1.00 36.63           N  
-ATOM    586  N   ASN A 125     -66.690   0.149   4.996  1.00 40.90           N  
-ATOM    587  CA  ASN A 125     -66.688   1.033   6.149  1.00 39.83           C  
-ATOM    588  C   ASN A 125     -65.308   1.612   6.385  1.00 39.36           C  
-ATOM    589  O   ASN A 125     -65.121   2.822   6.332  1.00 39.01           O  
-ATOM    590  CB  ASN A 125     -67.138   0.292   7.385  1.00 39.32           C  
-ATOM    591  CG  ASN A 125     -67.783   1.200   8.367  1.00 39.15           C  
-ATOM    592  OD1 ASN A 125     -68.832   1.785   8.089  1.00 37.53           O  
-ATOM    593  ND2 ASN A 125     -67.162   1.347   9.526  1.00 40.87           N  
-ATOM    594  N   LEU A 126     -64.337   0.750   6.652  1.00 38.86           N  
-ATOM    595  CA  LEU A 126     -62.982   1.232   6.851  1.00 38.97           C  
-ATOM    596  C   LEU A 126     -62.590   2.131   5.690  1.00 38.42           C  
-ATOM    597  O   LEU A 126     -61.788   3.048   5.843  1.00 38.71           O  
-ATOM    598  CB  LEU A 126     -62.004   0.065   6.946  1.00 39.05           C  
-ATOM    599  CG  LEU A 126     -61.877  -0.531   8.340  1.00 39.44           C  
-ATOM    600  CD1 LEU A 126     -63.247  -0.949   8.835  1.00 40.36           C  
-ATOM    601  CD2 LEU A 126     -60.924  -1.705   8.305  1.00 41.28           C  
-ATOM    602  N   ALA A 127     -63.165   1.862   4.525  1.00 38.37           N  
-ATOM    603  CA  ALA A 127     -62.869   2.647   3.338  1.00 39.55           C  
-ATOM    604  C   ALA A 127     -63.455   4.044   3.465  1.00 40.59           C  
-ATOM    605  O   ALA A 127     -62.731   5.038   3.394  1.00 41.60           O  
-ATOM    606  CB  ALA A 127     -63.424   1.958   2.103  1.00 39.47           C  
-ATOM    607  N   GLU A 128     -64.770   4.116   3.649  1.00 41.13           N  
-ATOM    608  CA  GLU A 128     -65.455   5.396   3.788  1.00 41.54           C  
-ATOM    609  C   GLU A 128     -64.855   6.213   4.937  1.00 41.26           C  
-ATOM    610  O   GLU A 128     -64.728   7.433   4.859  1.00 41.05           O  
-ATOM    611  CB  GLU A 128     -66.951   5.159   4.013  1.00 41.14           C  
-ATOM    612  CG  GLU A 128     -67.728   6.409   4.331  1.00 44.07           C  
-ATOM    613  CD  GLU A 128     -69.222   6.232   4.146  1.00 47.06           C  
-ATOM    614  OE1 GLU A 128     -69.758   5.217   4.625  1.00 49.15           O  
-ATOM    615  OE2 GLU A 128     -69.868   7.111   3.529  1.00 49.33           O  
-ATOM    616  N   LEU A 129     -64.463   5.527   5.999  1.00 41.70           N  
-ATOM    617  CA  LEU A 129     -63.885   6.197   7.143  1.00 41.41           C  
-ATOM    618  C   LEU A 129     -62.496   6.710   6.811  1.00 41.81           C  
-ATOM    619  O   LEU A 129     -62.130   7.821   7.185  1.00 43.74           O  
-ATOM    620  CB  LEU A 129     -63.825   5.241   8.323  1.00 41.32           C  
-ATOM    621  CG  LEU A 129     -63.370   5.888   9.624  1.00 43.06           C  
-ATOM    622  CD1 LEU A 129     -64.142   5.270  10.780  1.00 43.64           C  
-ATOM    623  CD2 LEU A 129     -61.861   5.721   9.789  1.00 43.15           C  
-ATOM    624  N   GLY A 130     -61.719   5.901   6.106  1.00 41.69           N  
-ATOM    625  CA  GLY A 130     -60.376   6.313   5.745  1.00 41.18           C  
-ATOM    626  C   GLY A 130     -60.384   7.510   4.815  1.00 40.37           C  
-ATOM    627  O   GLY A 130     -59.392   8.232   4.717  1.00 39.64           O  
-ATOM    628  N   VAL A 131     -61.499   7.704   4.118  1.00 40.16           N  
-ATOM    629  CA  VAL A 131     -61.651   8.824   3.196  1.00 41.43           C  
-ATOM    630  C   VAL A 131     -62.036  10.048   4.008  1.00 42.65           C  
-ATOM    631  O   VAL A 131     -61.618  11.163   3.705  1.00 42.54           O  
-ATOM    632  CB  VAL A 131     -62.755   8.554   2.134  1.00 41.24           C  
-ATOM    633  CG1 VAL A 131     -63.212   9.859   1.494  1.00 38.93           C  
-ATOM    634  CG2 VAL A 131     -62.224   7.620   1.068  1.00 39.88           C  
-ATOM    635  N   THR A 132     -62.843   9.831   5.040  1.00 43.90           N  
-ATOM    636  CA  THR A 132     -63.265  10.915   5.910  1.00 44.87           C  
-ATOM    637  C   THR A 132     -62.048  11.564   6.560  1.00 46.17           C  
-ATOM    638  O   THR A 132     -61.909  12.787   6.531  1.00 47.62           O  
-ATOM    639  CB  THR A 132     -64.196  10.405   6.995  1.00 44.23           C  
-ATOM    640  OG1 THR A 132     -65.391   9.911   6.382  1.00 44.26           O  
-ATOM    641  CG2 THR A 132     -64.538  11.519   7.973  1.00 44.30           C  
-ATOM    642  N   VAL A 133     -61.173  10.749   7.146  1.00 46.72           N  
-ATOM    643  CA  VAL A 133     -59.958  11.262   7.776  1.00 48.98           C  
-ATOM    644  C   VAL A 133     -59.087  11.967   6.734  1.00 50.66           C  
-ATOM    645  O   VAL A 133     -58.246  12.802   7.055  1.00 50.32           O  
-ATOM    646  CB  VAL A 133     -59.148  10.123   8.417  1.00 49.35           C  
-ATOM    647  CG1 VAL A 133     -57.800  10.646   8.919  1.00 48.38           C  
-ATOM    648  CG2 VAL A 133     -59.952   9.511   9.561  1.00 50.97           C  
-ATOM    649  N   GLU A 134     -59.298  11.609   5.479  1.00 53.37           N  
-ATOM    650  CA  GLU A 134     -58.572  12.200   4.373  1.00 56.37           C  
-ATOM    651  C   GLU A 134     -59.178  13.581   4.115  1.00 57.45           C  
-ATOM    652  O   GLU A 134     -58.466  14.578   4.007  1.00 56.81           O  
-ATOM    653  CB  GLU A 134     -58.724  11.294   3.148  1.00 59.51           C  
-ATOM    654  CG  GLU A 134     -58.743  12.004   1.808  1.00 64.45           C  
-ATOM    655  CD  GLU A 134     -57.413  11.940   1.097  1.00 67.12           C  
-ATOM    656  OE1 GLU A 134     -56.956  10.807   0.806  1.00 67.77           O  
-ATOM    657  OE2 GLU A 134     -56.836  13.023   0.832  1.00 68.48           O  
-ATOM    658  N   ARG A 135     -60.505  13.629   4.026  1.00 59.43           N  
-ATOM    659  CA  ARG A 135     -61.223  14.878   3.789  1.00 60.46           C  
-ATOM    660  C   ARG A 135     -61.011  15.840   4.940  1.00 59.07           C  
-ATOM    661  O   ARG A 135     -60.977  17.047   4.737  1.00 60.09           O  
-ATOM    662  CB  ARG A 135     -62.720  14.623   3.643  1.00 63.83           C  
-ATOM    663  CG  ARG A 135     -63.126  13.749   2.459  1.00 71.59           C  
-ATOM    664  CD  ARG A 135     -64.656  13.569   2.363  1.00 74.95           C  
-ATOM    665  NE  ARG A 135     -65.327  14.854   2.209  1.00 79.73           N  
-ATOM    666  CZ  ARG A 135     -65.472  15.748   3.187  1.00 82.13           C  
-ATOM    667  NH1 ARG A 135     -65.002  15.491   4.402  1.00 82.96           N  
-ATOM    668  NH2 ARG A 135     -66.068  16.914   2.948  1.00 82.94           N  
-ATOM    669  N   LYS A 136     -60.883  15.309   6.152  1.00 57.11           N  
-ATOM    670  CA  LYS A 136     -60.672  16.152   7.321  1.00 55.25           C  
-ATOM    671  C   LYS A 136     -59.406  16.992   7.166  1.00 53.77           C  
-ATOM    672  O   LYS A 136     -59.448  18.218   7.264  1.00 54.05           O  
-ATOM    673  CB  LYS A 136     -60.555  15.306   8.585  1.00 54.74           C  
-ATOM    674  CG  LYS A 136     -60.387  16.145   9.835  1.00 55.15           C  
-ATOM    675  CD  LYS A 136     -60.113  15.292  11.052  1.00 55.14           C  
-ATOM    676  CE  LYS A 136     -58.767  14.601  10.955  1.00 55.15           C  
-ATOM    677  NZ  LYS A 136     -58.441  13.884  12.223  1.00 55.57           N  
-ATOM    678  N   LEU A 137     -58.283  16.320   6.933  1.00 51.71           N  
-ATOM    679  CA  LEU A 137     -56.998  16.986   6.758  1.00 49.78           C  
-ATOM    680  C   LEU A 137     -57.048  18.094   5.713  1.00 49.36           C  
-ATOM    681  O   LEU A 137     -56.333  19.087   5.816  1.00 48.83           O  
-ATOM    682  CB  LEU A 137     -55.932  15.966   6.357  1.00 48.11           C  
-ATOM    683  CG  LEU A 137     -55.032  15.415   7.462  1.00 46.99           C  
-ATOM    684  CD1 LEU A 137     -55.856  14.743   8.552  1.00 45.68           C  
-ATOM    685  CD2 LEU A 137     -54.036  14.450   6.838  1.00 46.54           C  
-ATOM    686  N   TRP A 138     -57.888  17.910   4.702  1.00 50.21           N  
-ATOM    687  CA  TRP A 138     -58.035  18.889   3.635  1.00 51.13           C  
-ATOM    688  C   TRP A 138     -58.805  20.101   4.147  1.00 51.16           C  
-ATOM    689  O   TRP A 138     -58.374  21.235   3.963  1.00 51.94           O  
-ATOM    690  CB  TRP A 138     -58.778  18.277   2.448  1.00 53.04           C  
-ATOM    691  CG  TRP A 138     -58.924  19.211   1.300  1.00 56.20           C  
-ATOM    692  CD1 TRP A 138     -57.939  19.630   0.456  1.00 58.01           C  
-ATOM    693  CD2 TRP A 138     -60.118  19.882   0.888  1.00 58.89           C  
-ATOM    694  NE1 TRP A 138     -58.444  20.524  -0.459  1.00 59.48           N  
-ATOM    695  CE2 TRP A 138     -59.781  20.697  -0.215  1.00 60.34           C  
-ATOM    696  CE3 TRP A 138     -61.443  19.876   1.345  1.00 60.99           C  
-ATOM    697  CZ2 TRP A 138     -60.722  21.502  -0.871  1.00 62.23           C  
-ATOM    698  CZ3 TRP A 138     -62.383  20.676   0.692  1.00 62.92           C  
-ATOM    699  CH2 TRP A 138     -62.015  21.478  -0.404  1.00 63.33           C  
-ATOM    700  N   LEU A 139     -59.948  19.862   4.783  1.00 50.47           N  
-ATOM    701  CA  LEU A 139     -60.747  20.954   5.324  1.00 49.26           C  
-ATOM    702  C   LEU A 139     -59.906  21.827   6.255  1.00 49.83           C  
-ATOM    703  O   LEU A 139     -59.937  23.050   6.155  1.00 50.73           O  
-ATOM    704  CB  LEU A 139     -61.957  20.412   6.082  1.00 46.74           C  
-ATOM    705  CG  LEU A 139     -63.020  19.718   5.236  1.00 44.30           C  
-ATOM    706  CD1 LEU A 139     -64.193  19.365   6.130  1.00 43.24           C  
-ATOM    707  CD2 LEU A 139     -63.469  20.625   4.097  1.00 42.83           C  
-ATOM    708  N   ALA A 140     -59.159  21.199   7.159  1.00 50.03           N  
-ATOM    709  CA  ALA A 140     -58.308  21.938   8.083  1.00 50.75           C  
-ATOM    710  C   ALA A 140     -57.328  22.814   7.298  1.00 51.87           C  
-ATOM    711  O   ALA A 140     -57.093  23.972   7.639  1.00 52.47           O  
-ATOM    712  CB  ALA A 140     -57.551  20.974   8.974  1.00 49.03           C  
-ATOM    713  N   LYS A 141     -56.761  22.251   6.240  1.00 53.63           N  
-ATOM    714  CA  LYS A 141     -55.811  22.965   5.393  1.00 55.09           C  
-ATOM    715  C   LYS A 141     -56.522  24.152   4.734  1.00 54.71           C  
-ATOM    716  O   LYS A 141     -56.004  25.261   4.702  1.00 54.12           O  
-ATOM    717  CB  LYS A 141     -55.274  22.013   4.311  1.00 57.31           C  
-ATOM    718  CG  LYS A 141     -53.953  22.408   3.654  1.00 59.95           C  
-ATOM    719  CD  LYS A 141     -52.757  21.838   4.428  1.00 63.57           C  
-ATOM    720  CE  LYS A 141     -51.426  22.049   3.683  1.00 64.82           C  
-ATOM    721  NZ  LYS A 141     -50.232  21.516   4.423  1.00 63.78           N  
-ATOM    722  N   GLU A 142     -57.718  23.906   4.213  1.00 55.64           N  
-ATOM    723  CA  GLU A 142     -58.490  24.945   3.544  1.00 56.67           C  
-ATOM    724  C   GLU A 142     -58.863  26.061   4.514  1.00 57.47           C  
-ATOM    725  O   GLU A 142     -58.490  27.212   4.309  1.00 59.03           O  
-ATOM    726  CB  GLU A 142     -59.758  24.349   2.930  1.00 56.60           C  
-ATOM    727  CG  GLU A 142     -60.398  25.223   1.877  1.00 58.51           C  
-ATOM    728  CD  GLU A 142     -59.554  25.324   0.621  1.00 61.27           C  
-ATOM    729  OE1 GLU A 142     -58.461  24.713   0.586  1.00 62.76           O  
-ATOM    730  OE2 GLU A 142     -59.981  26.010  -0.336  1.00 61.80           O  
-ATOM    731  N   ILE A 143     -59.599  25.716   5.568  1.00 57.85           N  
-ATOM    732  CA  ILE A 143     -60.023  26.685   6.579  1.00 56.67           C  
-ATOM    733  C   ILE A 143     -58.874  27.528   7.106  1.00 57.14           C  
-ATOM    734  O   ILE A 143     -58.902  28.748   6.998  1.00 57.34           O  
-ATOM    735  CB  ILE A 143     -60.712  25.981   7.764  1.00 55.71           C  
-ATOM    736  CG1 ILE A 143     -62.187  25.771   7.425  1.00 55.28           C  
-ATOM    737  CG2 ILE A 143     -60.520  26.778   9.050  1.00 53.66           C  
-ATOM    738  CD1 ILE A 143     -62.960  25.005   8.466  1.00 57.10           C  
-ATOM    739  N   ASP A 144     -57.864  26.880   7.672  1.00 57.84           N  
-ATOM    740  CA  ASP A 144     -56.729  27.613   8.206  1.00 59.03           C  
-ATOM    741  C   ASP A 144     -56.190  28.600   7.174  1.00 58.03           C  
-ATOM    742  O   ASP A 144     -55.792  29.712   7.521  1.00 59.24           O  
-ATOM    743  CB  ASP A 144     -55.622  26.652   8.639  1.00 62.38           C  
-ATOM    744  CG  ASP A 144     -54.961  27.078   9.942  1.00 66.85           C  
-ATOM    745  OD1 ASP A 144     -55.656  27.084  10.988  1.00 68.73           O  
-ATOM    746  OD2 ASP A 144     -53.752  27.413   9.921  1.00 69.44           O  
-ATOM    747  N   THR A 145     -56.189  28.201   5.907  1.00 56.38           N  
-ATOM    748  CA  THR A 145     -55.705  29.065   4.831  1.00 54.96           C  
-ATOM    749  C   THR A 145     -56.663  30.226   4.590  1.00 54.61           C  
-ATOM    750  O   THR A 145     -56.303  31.390   4.728  1.00 54.91           O  
-ATOM    751  CB  THR A 145     -55.556  28.281   3.499  1.00 53.90           C  
-ATOM    752  OG1 THR A 145     -54.444  27.386   3.594  1.00 54.71           O  
-ATOM    753  CG2 THR A 145     -55.336  29.228   2.330  1.00 52.40           C  
-ATOM    754  N   ARG A 146     -57.891  29.886   4.232  1.00 54.46           N  
-ATOM    755  CA  ARG A 146     -58.922  30.862   3.937  1.00 53.88           C  
-ATOM    756  C   ARG A 146     -59.142  31.878   5.059  1.00 52.98           C  
-ATOM    757  O   ARG A 146     -59.413  33.052   4.791  1.00 53.36           O  
-ATOM    758  CB  ARG A 146     -60.219  30.125   3.618  1.00 54.50           C  
-ATOM    759  CG  ARG A 146     -61.239  30.960   2.887  1.00 57.17           C  
-ATOM    760  CD  ARG A 146     -62.318  30.063   2.317  1.00 58.72           C  
-ATOM    761  NE  ARG A 146     -61.763  29.027   1.450  1.00 57.97           N  
-ATOM    762  CZ  ARG A 146     -62.117  28.860   0.180  1.00 58.90           C  
-ATOM    763  NH1 ARG A 146     -63.025  29.659  -0.369  1.00 57.76           N  
-ATOM    764  NH2 ARG A 146     -61.564  27.898  -0.544  1.00 59.40           N  
-ATOM    765  N   VAL A 147     -59.033  31.435   6.311  1.00 50.76           N  
-ATOM    766  CA  VAL A 147     -59.221  32.344   7.436  1.00 48.29           C  
-ATOM    767  C   VAL A 147     -58.125  33.396   7.407  1.00 48.58           C  
-ATOM    768  O   VAL A 147     -58.414  34.587   7.317  1.00 49.79           O  
-ATOM    769  CB  VAL A 147     -59.208  31.600   8.805  1.00 45.90           C  
-ATOM    770  CG1 VAL A 147     -58.906  32.561   9.936  1.00 43.62           C  
-ATOM    771  CG2 VAL A 147     -60.565  30.978   9.058  1.00 44.47           C  
-ATOM    772  N   GLU A 148     -56.872  32.958   7.463  1.00 48.15           N  
-ATOM    773  CA  GLU A 148     -55.743  33.884   7.436  1.00 47.25           C  
-ATOM    774  C   GLU A 148     -55.872  34.918   6.326  1.00 45.61           C  
-ATOM    775  O   GLU A 148     -55.493  36.069   6.497  1.00 45.13           O  
-ATOM    776  CB  GLU A 148     -54.431  33.117   7.279  1.00 48.79           C  
-ATOM    777  CG  GLU A 148     -53.577  33.138   8.529  1.00 51.61           C  
-ATOM    778  CD  GLU A 148     -52.970  34.504   8.795  1.00 53.55           C  
-ATOM    779  OE1 GLU A 148     -52.594  34.772   9.954  1.00 55.71           O  
-ATOM    780  OE2 GLU A 148     -52.855  35.308   7.847  1.00 54.23           O  
-ATOM    781  N   GLU A 149     -56.402  34.507   5.182  1.00 44.84           N  
-ATOM    782  CA  GLU A 149     -56.586  35.437   4.083  1.00 44.51           C  
-ATOM    783  C   GLU A 149     -57.476  36.557   4.584  1.00 42.77           C  
-ATOM    784  O   GLU A 149     -57.135  37.733   4.469  1.00 41.83           O  
-ATOM    785  CB  GLU A 149     -57.269  34.753   2.903  1.00 48.17           C  
-ATOM    786  CG  GLU A 149     -56.322  34.191   1.865  1.00 53.62           C  
-ATOM    787  CD  GLU A 149     -56.999  34.017   0.516  1.00 57.14           C  
-ATOM    788  OE1 GLU A 149     -56.282  33.768  -0.485  1.00 58.90           O  
-ATOM    789  OE2 GLU A 149     -58.249  34.131   0.466  1.00 57.72           O  
-ATOM    790  N   MET A 150     -58.619  36.162   5.145  1.00 41.86           N  
-ATOM    791  CA  MET A 150     -59.613  37.085   5.692  1.00 40.21           C  
-ATOM    792  C   MET A 150     -59.075  37.953   6.808  1.00 39.70           C  
-ATOM    793  O   MET A 150     -59.434  39.123   6.915  1.00 39.92           O  
-ATOM    794  CB  MET A 150     -60.813  36.319   6.224  1.00 39.12           C  
-ATOM    795  CG  MET A 150     -61.727  35.811   5.155  1.00 39.56           C  
-ATOM    796  SD  MET A 150     -63.228  35.226   5.913  1.00 39.45           S  
-ATOM    797  CE  MET A 150     -64.297  36.633   5.723  1.00 39.46           C  
-ATOM    798  N   ARG A 151     -58.231  37.371   7.651  1.00 38.62           N  
-ATOM    799  CA  ARG A 151     -57.645  38.105   8.752  1.00 38.03           C  
-ATOM    800  C   ARG A 151     -56.822  39.284   8.224  1.00 37.52           C  
-ATOM    801  O   ARG A 151     -57.021  40.425   8.646  1.00 38.70           O  
-ATOM    802  CB  ARG A 151     -56.760  37.187   9.580  1.00 38.94           C  
-ATOM    803  CG  ARG A 151     -56.764  37.515  11.058  1.00 41.48           C  
-ATOM    804  CD  ARG A 151     -55.439  37.156  11.658  1.00 43.46           C  
-ATOM    805  NE  ARG A 151     -54.399  37.961  11.035  1.00 48.02           N  
-ATOM    806  CZ  ARG A 151     -53.099  37.767  11.210  1.00 51.42           C  
-ATOM    807  NH1 ARG A 151     -52.681  36.782  11.995  1.00 54.12           N  
-ATOM    808  NH2 ARG A 151     -52.218  38.560  10.606  1.00 52.78           N  
-ATOM    809  N   LEU A 152     -55.910  39.017   7.293  1.00 35.69           N  
-ATOM    810  CA  LEU A 152     -55.079  40.080   6.735  1.00 34.27           C  
-ATOM    811  C   LEU A 152     -55.915  41.234   6.209  1.00 33.83           C  
-ATOM    812  O   LEU A 152     -55.507  42.393   6.291  1.00 34.21           O  
-ATOM    813  CB  LEU A 152     -54.194  39.551   5.607  1.00 33.53           C  
-ATOM    814  CG  LEU A 152     -53.157  38.497   5.991  1.00 32.76           C  
-ATOM    815  CD1 LEU A 152     -52.163  38.347   4.858  1.00 30.83           C  
-ATOM    816  CD2 LEU A 152     -52.441  38.906   7.268  1.00 32.80           C  
-ATOM    817  N   LEU A 153     -57.079  40.917   5.658  1.00 33.31           N  
-ATOM    818  CA  LEU A 153     -57.958  41.949   5.133  1.00 34.12           C  
-ATOM    819  C   LEU A 153     -58.642  42.705   6.267  1.00 35.09           C  
-ATOM    820  O   LEU A 153     -58.628  43.939   6.315  1.00 34.61           O  
-ATOM    821  CB  LEU A 153     -59.024  41.336   4.221  1.00 32.30           C  
-ATOM    822  CG  LEU A 153     -58.518  40.831   2.875  1.00 31.74           C  
-ATOM    823  CD1 LEU A 153     -59.680  40.364   2.011  1.00 31.31           C  
-ATOM    824  CD2 LEU A 153     -57.764  41.957   2.188  1.00 32.19           C  
-ATOM    825  N   SER A 154     -59.243  41.951   7.180  1.00 35.83           N  
-ATOM    826  CA  SER A 154     -59.947  42.543   8.299  1.00 35.62           C  
-ATOM    827  C   SER A 154     -58.995  43.395   9.097  1.00 35.01           C  
-ATOM    828  O   SER A 154     -59.363  44.454   9.594  1.00 37.33           O  
-ATOM    829  CB  SER A 154     -60.539  41.461   9.193  1.00 35.72           C  
-ATOM    830  OG  SER A 154     -61.244  42.062  10.262  1.00 39.26           O  
-ATOM    831  N   GLU A 155     -57.763  42.934   9.220  1.00 33.00           N  
-ATOM    832  CA  GLU A 155     -56.777  43.681   9.965  1.00 33.16           C  
-ATOM    833  C   GLU A 155     -56.443  44.972   9.226  1.00 31.93           C  
-ATOM    834  O   GLU A 155     -56.227  46.010   9.841  1.00 30.69           O  
-ATOM    835  CB  GLU A 155     -55.540  42.825  10.148  1.00 36.47           C  
-ATOM    836  CG  GLU A 155     -54.377  43.525  10.779  1.00 42.87           C  
-ATOM    837  CD  GLU A 155     -53.180  42.607  10.868  1.00 47.99           C  
-ATOM    838  OE1 GLU A 155     -53.227  41.653  11.684  1.00 51.10           O  
-ATOM    839  OE2 GLU A 155     -52.206  42.827  10.111  1.00 50.03           O  
-ATOM    840  N   GLU A 156     -56.403  44.914   7.901  1.00 31.86           N  
-ATOM    841  CA  GLU A 156     -56.116  46.116   7.138  1.00 31.47           C  
-ATOM    842  C   GLU A 156     -57.237  47.122   7.364  1.00 30.10           C  
-ATOM    843  O   GLU A 156     -56.976  48.300   7.605  1.00 30.90           O  
-ATOM    844  CB  GLU A 156     -55.995  45.817   5.641  1.00 33.66           C  
-ATOM    845  CG  GLU A 156     -55.745  47.088   4.821  1.00 37.40           C  
-ATOM    846  CD  GLU A 156     -55.447  46.841   3.346  1.00 38.68           C  
-ATOM    847  OE1 GLU A 156     -55.189  47.836   2.627  1.00 39.09           O  
-ATOM    848  OE2 GLU A 156     -55.468  45.668   2.906  1.00 40.73           O  
-ATOM    849  N   LEU A 157     -58.482  46.653   7.293  1.00 27.66           N  
-ATOM    850  CA  LEU A 157     -59.639  47.516   7.497  1.00 26.19           C  
-ATOM    851  C   LEU A 157     -59.686  48.136   8.905  1.00 26.58           C  
-ATOM    852  O   LEU A 157     -60.071  49.300   9.071  1.00 26.92           O  
-ATOM    853  CB  LEU A 157     -60.926  46.740   7.237  1.00 25.52           C  
-ATOM    854  CG  LEU A 157     -62.226  47.560   7.267  1.00 25.96           C  
-ATOM    855  CD1 LEU A 157     -62.226  48.601   6.164  1.00 24.70           C  
-ATOM    856  CD2 LEU A 157     -63.413  46.638   7.091  1.00 26.78           C  
-ATOM    857  N   GLU A 158     -59.304  47.363   9.917  1.00 25.36           N  
-ATOM    858  CA  GLU A 158     -59.295  47.860  11.286  1.00 24.30           C  
-ATOM    859  C   GLU A 158     -58.270  48.988  11.370  1.00 25.13           C  
-ATOM    860  O   GLU A 158     -58.520  50.029  11.977  1.00 25.71           O  
-ATOM    861  CB  GLU A 158     -58.923  46.729  12.244  1.00 23.43           C  
-ATOM    862  CG  GLU A 158     -58.957  47.073  13.734  1.00 27.38           C  
-ATOM    863  CD  GLU A 158     -57.754  47.896  14.218  1.00 30.11           C  
-ATOM    864  OE1 GLU A 158     -56.619  47.677  13.730  1.00 29.88           O  
-ATOM    865  OE2 GLU A 158     -57.945  48.752  15.111  1.00 30.49           O  
-ATOM    866  N   GLN A 159     -57.116  48.791  10.745  1.00 25.29           N  
-ATOM    867  CA  GLN A 159     -56.087  49.810  10.777  1.00 26.05           C  
-ATOM    868  C   GLN A 159     -56.502  51.005   9.921  1.00 26.13           C  
-ATOM    869  O   GLN A 159     -56.193  52.153  10.255  1.00 27.33           O  
-ATOM    870  CB  GLN A 159     -54.760  49.247  10.271  1.00 27.37           C  
-ATOM    871  CG  GLN A 159     -54.307  47.978  10.967  1.00 31.34           C  
-ATOM    872  CD  GLN A 159     -53.044  47.390  10.343  1.00 34.29           C  
-ATOM    873  OE1 GLN A 159     -52.823  47.517   9.127  1.00 35.44           O  
-ATOM    874  NE2 GLN A 159     -52.217  46.727  11.166  1.00 33.24           N  
-ATOM    875  N   LEU A 160     -57.200  50.753   8.819  1.00 23.76           N  
-ATOM    876  CA  LEU A 160     -57.603  51.863   7.976  1.00 22.65           C  
-ATOM    877  C   LEU A 160     -58.645  52.728   8.682  1.00 23.71           C  
-ATOM    878  O   LEU A 160     -58.686  53.937   8.472  1.00 23.52           O  
-ATOM    879  CB  LEU A 160     -58.135  51.371   6.626  1.00 19.04           C  
-ATOM    880  CG  LEU A 160     -58.566  52.450   5.613  1.00 16.04           C  
-ATOM    881  CD1 LEU A 160     -57.420  53.356   5.252  1.00 12.98           C  
-ATOM    882  CD2 LEU A 160     -59.088  51.780   4.368  1.00 15.72           C  
-ATOM    883  N   THR A 161     -59.487  52.126   9.519  1.00 24.89           N  
-ATOM    884  CA  THR A 161     -60.483  52.923  10.237  1.00 26.01           C  
-ATOM    885  C   THR A 161     -59.831  53.604  11.437  1.00 27.47           C  
-ATOM    886  O   THR A 161     -60.208  54.715  11.813  1.00 28.11           O  
-ATOM    887  CB  THR A 161     -61.686  52.088  10.719  1.00 23.92           C  
-ATOM    888  OG1 THR A 161     -61.222  50.922  11.398  1.00 25.16           O  
-ATOM    889  CG2 THR A 161     -62.545  51.687   9.553  1.00 24.46           C  
-ATOM    890  N   ARG A 162     -58.854  52.943  12.045  1.00 28.67           N  
-ATOM    891  CA  ARG A 162     -58.156  53.555  13.165  1.00 30.32           C  
-ATOM    892  C   ARG A 162     -57.456  54.792  12.600  1.00 30.40           C  
-ATOM    893  O   ARG A 162     -57.603  55.901  13.117  1.00 29.80           O  
-ATOM    894  CB  ARG A 162     -57.137  52.580  13.756  1.00 31.24           C  
-ATOM    895  CG  ARG A 162     -56.126  53.214  14.681  1.00 33.48           C  
-ATOM    896  CD  ARG A 162     -55.601  52.175  15.647  1.00 38.60           C  
-ATOM    897  NE  ARG A 162     -56.453  52.026  16.833  1.00 42.26           N  
-ATOM    898  CZ  ARG A 162     -56.722  50.864  17.432  1.00 43.84           C  
-ATOM    899  NH1 ARG A 162     -56.219  49.728  16.959  1.00 44.56           N  
-ATOM    900  NH2 ARG A 162     -57.475  50.836  18.525  1.00 44.54           N  
-ATOM    901  N   THR A 163     -56.720  54.591  11.513  1.00 30.34           N  
-ATOM    902  CA  THR A 163     -56.011  55.673  10.859  1.00 30.50           C  
-ATOM    903  C   THR A 163     -56.910  56.894  10.656  1.00 30.57           C  
-ATOM    904  O   THR A 163     -56.453  58.037  10.790  1.00 31.71           O  
-ATOM    905  CB  THR A 163     -55.465  55.223   9.490  1.00 32.20           C  
-ATOM    906  OG1 THR A 163     -54.472  54.206   9.682  1.00 34.13           O  
-ATOM    907  CG2 THR A 163     -54.857  56.409   8.731  1.00 32.01           C  
-ATOM    908  N   GLN A 164     -58.184  56.670  10.342  1.00 28.81           N  
-ATOM    909  CA  GLN A 164     -59.077  57.799  10.120  1.00 28.49           C  
-ATOM    910  C   GLN A 164     -59.483  58.467  11.424  1.00 28.38           C  
-ATOM    911  O   GLN A 164     -59.602  59.688  11.479  1.00 28.83           O  
-ATOM    912  CB  GLN A 164     -60.317  57.367   9.349  1.00 27.95           C  
-ATOM    913  CG  GLN A 164     -60.010  56.768   8.007  1.00 30.47           C  
-ATOM    914  CD  GLN A 164     -61.248  56.238   7.297  1.00 33.23           C  
-ATOM    915  OE1 GLN A 164     -62.115  57.009   6.883  1.00 34.65           O  
-ATOM    916  NE2 GLN A 164     -61.334  54.913   7.152  1.00 33.74           N  
-ATOM    917  N   VAL A 165     -59.693  57.679  12.476  1.00 28.19           N  
-ATOM    918  CA  VAL A 165     -60.075  58.255  13.762  1.00 27.47           C  
-ATOM    919  C   VAL A 165     -58.947  59.197  14.136  1.00 28.92           C  
-ATOM    920  O   VAL A 165     -59.175  60.345  14.540  1.00 29.14           O  
-ATOM    921  CB  VAL A 165     -60.215  57.187  14.862  1.00 25.35           C  
-ATOM    922  CG1 VAL A 165     -60.660  57.838  16.150  1.00 24.46           C  
-ATOM    923  CG2 VAL A 165     -61.221  56.131  14.448  1.00 24.77           C  
-ATOM    924  N   GLN A 166     -57.731  58.685  13.968  1.00 29.91           N  
-ATOM    925  CA  GLN A 166     -56.494  59.404  14.241  1.00 30.81           C  
-ATOM    926  C   GLN A 166     -56.480  60.765  13.567  1.00 31.12           C  
-ATOM    927  O   GLN A 166     -56.295  61.787  14.225  1.00 30.93           O  
-ATOM    928  CB  GLN A 166     -55.320  58.614  13.698  1.00 33.33           C  
-ATOM    929  CG  GLN A 166     -55.186  57.200  14.215  1.00 37.18           C  
-ATOM    930  CD  GLN A 166     -54.423  57.146  15.506  1.00 39.28           C  
-ATOM    931  OE1 GLN A 166     -53.770  56.145  15.809  1.00 40.57           O  
-ATOM    932  NE2 GLN A 166     -54.500  58.225  16.286  1.00 40.33           N  
-ATOM    933  N   ASN A 167     -56.650  60.766  12.244  1.00 31.04           N  
-ATOM    934  CA  ASN A 167     -56.653  62.006  11.472  1.00 30.97           C  
-ATOM    935  C   ASN A 167     -57.688  63.005  11.979  1.00 31.99           C  
-ATOM    936  O   ASN A 167     -57.390  64.191  12.113  1.00 33.21           O  
-ATOM    937  CB  ASN A 167     -56.936  61.741   9.990  1.00 29.25           C  
-ATOM    938  CG  ASN A 167     -55.889  60.880   9.339  1.00 29.04           C  
-ATOM    939  OD1 ASN A 167     -54.765  60.790   9.815  1.00 32.09           O  
-ATOM    940  ND2 ASN A 167     -56.246  60.255   8.224  1.00 29.64           N  
-ATOM    941  N   THR A 168     -58.900  62.539  12.267  1.00 32.16           N  
-ATOM    942  CA  THR A 168     -59.927  63.460  12.721  1.00 33.75           C  
-ATOM    943  C   THR A 168     -59.500  64.266  13.932  1.00 33.25           C  
-ATOM    944  O   THR A 168     -59.825  65.452  14.029  1.00 34.23           O  
-ATOM    945  CB  THR A 168     -61.233  62.753  13.044  1.00 35.13           C  
-ATOM    946  OG1 THR A 168     -61.533  61.818  12.003  1.00 38.57           O  
-ATOM    947  CG2 THR A 168     -62.372  63.779  13.094  1.00 37.36           C  
-ATOM    948  N   SER A 169     -58.773  63.636  14.847  1.00 31.45           N  
-ATOM    949  CA  SER A 169     -58.296  64.332  16.032  1.00 30.22           C  
-ATOM    950  C   SER A 169     -57.342  65.447  15.653  1.00 29.55           C  
-ATOM    951  O   SER A 169     -57.554  66.615  16.004  1.00 31.57           O  
-ATOM    952  CB  SER A 169     -57.569  63.373  16.954  1.00 31.27           C  
-ATOM    953  OG  SER A 169     -58.471  62.450  17.519  1.00 39.85           O  
-ATOM    954  N   THR A 170     -56.277  65.078  14.947  1.00 26.78           N  
-ATOM    955  CA  THR A 170     -55.275  66.034  14.516  1.00 22.72           C  
-ATOM    956  C   THR A 170     -55.979  67.215  13.886  1.00 21.96           C  
-ATOM    957  O   THR A 170     -55.768  68.359  14.295  1.00 22.92           O  
-ATOM    958  CB  THR A 170     -54.349  65.416  13.490  1.00 22.68           C  
-ATOM    959  OG1 THR A 170     -53.911  64.146  13.971  1.00 24.84           O  
-ATOM    960  CG2 THR A 170     -53.135  66.303  13.248  1.00 22.57           C  
-ATOM    961  N   ILE A 171     -56.838  66.950  12.909  1.00 19.24           N  
-ATOM    962  CA  ILE A 171     -57.544  68.042  12.259  1.00 19.13           C  
-ATOM    963  C   ILE A 171     -58.403  68.885  13.216  1.00 18.90           C  
-ATOM    964  O   ILE A 171     -58.453  70.108  13.084  1.00 18.56           O  
-ATOM    965  CB  ILE A 171     -58.390  67.531  11.105  1.00 18.60           C  
-ATOM    966  CG1 ILE A 171     -57.590  66.486  10.336  1.00 18.86           C  
-ATOM    967  CG2 ILE A 171     -58.691  68.676  10.140  1.00 18.41           C  
-ATOM    968  CD1 ILE A 171     -58.291  65.951   9.122  1.00 21.18           C  
-ATOM    969  N   ALA A 172     -59.075  68.253  14.175  1.00 17.40           N  
-ATOM    970  CA  ALA A 172     -59.863  69.018  15.131  1.00 16.68           C  
-ATOM    971  C   ALA A 172     -58.913  70.000  15.820  1.00 17.77           C  
-ATOM    972  O   ALA A 172     -59.212  71.190  15.945  1.00 18.42           O  
-ATOM    973  CB  ALA A 172     -60.480  68.107  16.154  1.00 15.03           C  
-ATOM    974  N   VAL A 173     -57.764  69.500  16.265  1.00 17.04           N  
-ATOM    975  CA  VAL A 173     -56.777  70.353  16.927  1.00 16.72           C  
-ATOM    976  C   VAL A 173     -56.293  71.457  15.980  1.00 17.56           C  
-ATOM    977  O   VAL A 173     -56.175  72.623  16.375  1.00 16.54           O  
-ATOM    978  CB  VAL A 173     -55.572  69.524  17.418  1.00 15.92           C  
-ATOM    979  CG1 VAL A 173     -54.421  70.430  17.857  1.00 11.45           C  
-ATOM    980  CG2 VAL A 173     -56.016  68.656  18.569  1.00 15.37           C  
-ATOM    981  N   ALA A 174     -56.018  71.090  14.731  1.00 16.97           N  
-ATOM    982  CA  ALA A 174     -55.577  72.068  13.748  1.00 17.30           C  
-ATOM    983  C   ALA A 174     -56.699  73.081  13.567  1.00 18.61           C  
-ATOM    984  O   ALA A 174     -56.466  74.287  13.497  1.00 18.48           O  
-ATOM    985  CB  ALA A 174     -55.281  71.386  12.436  1.00 16.82           C  
-ATOM    986  N   ASN A 175     -57.926  72.572  13.507  1.00 20.10           N  
-ATOM    987  CA  ASN A 175     -59.094  73.416  13.326  1.00 20.57           C  
-ATOM    988  C   ASN A 175     -59.323  74.377  14.468  1.00 21.65           C  
-ATOM    989  O   ASN A 175     -59.782  75.507  14.249  1.00 24.15           O  
-ATOM    990  CB  ASN A 175     -60.337  72.568  13.119  1.00 19.99           C  
-ATOM    991  CG  ASN A 175     -60.446  72.068  11.717  1.00 19.42           C  
-ATOM    992  OD1 ASN A 175     -60.032  72.750  10.785  1.00 18.05           O  
-ATOM    993  ND2 ASN A 175     -61.011  70.885  11.545  1.00 20.77           N  
-ATOM    994  N   VAL A 176     -59.032  73.935  15.688  1.00 20.18           N  
-ATOM    995  CA  VAL A 176     -59.202  74.816  16.827  1.00 19.42           C  
-ATOM    996  C   VAL A 176     -58.079  75.852  16.800  1.00 21.56           C  
-ATOM    997  O   VAL A 176     -58.322  77.033  17.052  1.00 23.10           O  
-ATOM    998  CB  VAL A 176     -59.176  74.043  18.163  1.00 16.32           C  
-ATOM    999  CG1 VAL A 176     -59.025  75.000  19.330  1.00 12.07           C  
-ATOM   1000  CG2 VAL A 176     -60.455  73.275  18.320  1.00 16.82           C  
-ATOM   1001  N   THR A 177     -56.859  75.427  16.470  1.00 22.03           N  
-ATOM   1002  CA  THR A 177     -55.740  76.366  16.439  1.00 22.94           C  
-ATOM   1003  C   THR A 177     -56.095  77.523  15.538  1.00 24.28           C  
-ATOM   1004  O   THR A 177     -55.822  78.682  15.850  1.00 24.88           O  
-ATOM   1005  CB  THR A 177     -54.469  75.763  15.855  1.00 22.10           C  
-ATOM   1006  OG1 THR A 177     -54.281  74.446  16.366  1.00 25.03           O  
-ATOM   1007  CG2 THR A 177     -53.277  76.618  16.222  1.00 19.67           C  
-ATOM   1008  N   HIS A 178     -56.705  77.199  14.405  1.00 24.64           N  
-ATOM   1009  CA  HIS A 178     -57.075  78.223  13.456  1.00 24.75           C  
-ATOM   1010  C   HIS A 178     -57.983  79.265  14.078  1.00 24.22           C  
-ATOM   1011  O   HIS A 178     -57.831  80.459  13.826  1.00 24.41           O  
-ATOM   1012  CB  HIS A 178     -57.753  77.600  12.254  1.00 26.51           C  
-ATOM   1013  CG  HIS A 178     -58.023  78.579  11.164  1.00 30.00           C  
-ATOM   1014  ND1 HIS A 178     -59.144  79.380  11.147  1.00 32.51           N  
-ATOM   1015  CD2 HIS A 178     -57.299  78.917  10.073  1.00 31.86           C  
-ATOM   1016  CE1 HIS A 178     -59.102  80.168  10.089  1.00 33.65           C  
-ATOM   1017  NE2 HIS A 178     -57.992  79.907   9.421  1.00 34.53           N  
-ATOM   1018  N   ILE A 179     -58.925  78.819  14.897  1.00 24.05           N  
-ATOM   1019  CA  ILE A 179     -59.838  79.746  15.542  1.00 24.12           C  
-ATOM   1020  C   ILE A 179     -59.100  80.788  16.379  1.00 25.39           C  
-ATOM   1021  O   ILE A 179     -59.533  81.932  16.462  1.00 26.95           O  
-ATOM   1022  CB  ILE A 179     -60.848  78.997  16.406  1.00 23.61           C  
-ATOM   1023  CG1 ILE A 179     -61.655  78.060  15.512  1.00 21.45           C  
-ATOM   1024  CG2 ILE A 179     -61.763  79.986  17.138  1.00 21.37           C  
-ATOM   1025  CD1 ILE A 179     -62.799  77.392  16.225  1.00 25.34           C  
-ATOM   1026  N   TYR A 180     -57.987  80.409  16.996  1.00 25.80           N  
-ATOM   1027  CA  TYR A 180     -57.223  81.371  17.783  1.00 26.71           C  
-ATOM   1028  C   TYR A 180     -56.840  82.574  16.921  1.00 28.73           C  
-ATOM   1029  O   TYR A 180     -56.871  83.707  17.383  1.00 28.16           O  
-ATOM   1030  CB  TYR A 180     -55.955  80.728  18.332  1.00 24.92           C  
-ATOM   1031  CG  TYR A 180     -56.188  79.753  19.451  1.00 23.23           C  
-ATOM   1032  CD1 TYR A 180     -55.720  78.449  19.364  1.00 23.55           C  
-ATOM   1033  CD2 TYR A 180     -56.847  80.142  20.613  1.00 22.75           C  
-ATOM   1034  CE1 TYR A 180     -55.896  77.555  20.403  1.00 25.12           C  
-ATOM   1035  CE2 TYR A 180     -57.032  79.258  21.664  1.00 23.16           C  
-ATOM   1036  CZ  TYR A 180     -56.552  77.964  21.557  1.00 25.23           C  
-ATOM   1037  OH  TYR A 180     -56.694  77.081  22.609  1.00 25.97           O  
-ATOM   1038  N   ASP A 181     -56.475  82.319  15.667  1.00 31.98           N  
-ATOM   1039  CA  ASP A 181     -56.094  83.386  14.749  1.00 35.40           C  
-ATOM   1040  C   ASP A 181     -57.311  84.215  14.436  1.00 36.49           C  
-ATOM   1041  O   ASP A 181     -57.302  85.432  14.582  1.00 38.44           O  
-ATOM   1042  CB  ASP A 181     -55.557  82.818  13.444  1.00 38.72           C  
-ATOM   1043  CG  ASP A 181     -54.312  81.988  13.641  1.00 43.64           C  
-ATOM   1044  OD1 ASP A 181     -53.964  81.233  12.703  1.00 47.23           O  
-ATOM   1045  OD2 ASP A 181     -53.681  82.092  14.722  1.00 44.91           O  
-ATOM   1046  N   LEU A 182     -58.363  83.553  13.985  1.00 37.11           N  
-ATOM   1047  CA  LEU A 182     -59.579  84.268  13.665  1.00 38.43           C  
-ATOM   1048  C   LEU A 182     -59.975  85.151  14.837  1.00 39.72           C  
-ATOM   1049  O   LEU A 182     -60.341  86.306  14.648  1.00 39.20           O  
-ATOM   1050  CB  LEU A 182     -60.701  83.280  13.342  1.00 38.38           C  
-ATOM   1051  CG  LEU A 182     -60.565  82.610  11.978  1.00 37.45           C  
-ATOM   1052  CD1 LEU A 182     -61.653  81.579  11.769  1.00 35.75           C  
-ATOM   1053  CD2 LEU A 182     -60.638  83.690  10.917  1.00 38.18           C  
-ATOM   1054  N   LEU A 183     -59.882  84.611  16.048  1.00 41.87           N  
-ATOM   1055  CA  LEU A 183     -60.250  85.360  17.245  1.00 44.61           C  
-ATOM   1056  C   LEU A 183     -59.372  86.595  17.432  1.00 47.17           C  
-ATOM   1057  O   LEU A 183     -59.868  87.668  17.788  1.00 48.28           O  
-ATOM   1058  CB  LEU A 183     -60.135  84.481  18.488  1.00 43.34           C  
-ATOM   1059  CG  LEU A 183     -61.262  84.645  19.507  1.00 43.44           C  
-ATOM   1060  CD1 LEU A 183     -60.699  84.363  20.880  1.00 43.53           C  
-ATOM   1061  CD2 LEU A 183     -61.857  86.043  19.458  1.00 42.35           C  
-ATOM   1062  N   GLU A 184     -58.069  86.434  17.203  1.00 48.24           N  
-ATOM   1063  CA  GLU A 184     -57.121  87.533  17.339  1.00 48.66           C  
-ATOM   1064  C   GLU A 184     -57.540  88.694  16.460  1.00 47.60           C  
-ATOM   1065  O   GLU A 184     -57.793  89.790  16.951  1.00 47.29           O  
-ATOM   1066  CB  GLU A 184     -55.714  87.092  16.931  1.00 52.40           C  
-ATOM   1067  CG  GLU A 184     -54.673  87.316  18.010  1.00 58.59           C  
-ATOM   1068  CD  GLU A 184     -54.913  88.608  18.772  1.00 63.07           C  
-ATOM   1069  OE1 GLU A 184     -54.954  89.685  18.176  1.00 66.35           O  
-ATOM   1070  OE2 GLU A 184     -55.081  88.507  20.097  1.00 63.36           O  
-ATOM   1071  N   ALA A 185     -57.611  88.442  15.156  1.00 46.78           N  
-ATOM   1072  CA  ALA A 185     -57.992  89.456  14.178  1.00 46.72           C  
-ATOM   1073  C   ALA A 185     -59.429  89.971  14.358  1.00 47.55           C  
-ATOM   1074  O   ALA A 185     -59.958  90.676  13.501  1.00 48.17           O  
-ATOM   1075  CB  ALA A 185     -57.809  88.897  12.773  1.00 44.06           C  
-ATOM   1076  N   ASN A 186     -60.052  89.621  15.476  1.00 48.38           N  
-ATOM   1077  CA  ASN A 186     -61.422  90.031  15.765  1.00 49.01           C  
-ATOM   1078  C   ASN A 186     -62.386  89.812  14.605  1.00 49.30           C  
-ATOM   1079  O   ASN A 186     -63.323  90.591  14.424  1.00 49.95           O  
-ATOM   1080  CB  ASN A 186     -61.465  91.495  16.192  1.00 49.68           C  
-ATOM   1081  CG  ASN A 186     -60.642  91.761  17.433  1.00 51.24           C  
-ATOM   1082  OD1 ASN A 186     -60.870  91.169  18.496  1.00 51.85           O  
-ATOM   1083  ND2 ASN A 186     -59.672  92.655  17.307  1.00 50.91           N  
-ATOM   1084  N   LYS A 187     -62.147  88.757  13.822  1.00 48.65           N  
-ATOM   1085  CA  LYS A 187     -63.010  88.396  12.695  1.00 47.04           C  
-ATOM   1086  C   LYS A 187     -64.142  87.533  13.272  1.00 46.26           C  
-ATOM   1087  O   LYS A 187     -64.385  86.410  12.834  1.00 46.06           O  
-ATOM   1088  CB  LYS A 187     -62.208  87.621  11.638  1.00 46.01           C  
-ATOM   1089  CG  LYS A 187     -61.000  88.396  11.116  1.00 47.28           C  
-ATOM   1090  CD  LYS A 187     -60.693  88.116   9.635  1.00 49.19           C  
-ATOM   1091  CE  LYS A 187     -59.838  86.871   9.412  1.00 50.38           C  
-ATOM   1092  NZ  LYS A 187     -58.414  87.031   9.854  1.00 51.22           N  
-ATOM   1093  N   LYS A 188     -64.820  88.104  14.266  1.00 45.46           N  
-ATOM   1094  CA  LYS A 188     -65.913  87.490  15.017  1.00 45.18           C  
-ATOM   1095  C   LYS A 188     -66.952  86.661  14.252  1.00 45.85           C  
-ATOM   1096  O   LYS A 188     -67.552  85.754  14.816  1.00 45.31           O  
-ATOM   1097  CB  LYS A 188     -66.594  88.585  15.841  1.00 43.92           C  
-ATOM   1098  CG  LYS A 188     -67.653  88.122  16.802  1.00 44.47           C  
-ATOM   1099  CD  LYS A 188     -68.057  89.271  17.715  1.00 46.68           C  
-ATOM   1100  CE  LYS A 188     -69.330  88.963  18.499  1.00 48.84           C  
-ATOM   1101  NZ  LYS A 188     -69.774  90.125  19.323  1.00 48.39           N  
-ATOM   1102  N   ASP A 189     -67.182  86.961  12.980  1.00 47.77           N  
-ATOM   1103  CA  ASP A 189     -68.143  86.176  12.206  1.00 48.77           C  
-ATOM   1104  C   ASP A 189     -67.526  84.827  11.903  1.00 47.41           C  
-ATOM   1105  O   ASP A 189     -68.074  83.790  12.256  1.00 47.80           O  
-ATOM   1106  CB  ASP A 189     -68.487  86.854  10.877  1.00 53.22           C  
-ATOM   1107  CG  ASP A 189     -69.785  87.652  10.934  1.00 56.92           C  
-ATOM   1108  OD1 ASP A 189     -70.266  88.062   9.852  1.00 58.11           O  
-ATOM   1109  OD2 ASP A 189     -70.320  87.874  12.047  1.00 58.99           O  
-ATOM   1110  N   GLN A 190     -66.375  84.854  11.240  1.00 45.73           N  
-ATOM   1111  CA  GLN A 190     -65.663  83.640  10.873  1.00 44.24           C  
-ATOM   1112  C   GLN A 190     -65.419  82.722  12.064  1.00 42.05           C  
-ATOM   1113  O   GLN A 190     -65.267  81.512  11.896  1.00 41.91           O  
-ATOM   1114  CB  GLN A 190     -64.348  84.011  10.209  1.00 46.33           C  
-ATOM   1115  CG  GLN A 190     -64.556  84.922   9.020  1.00 50.51           C  
-ATOM   1116  CD  GLN A 190     -63.258  85.359   8.371  1.00 53.24           C  
-ATOM   1117  OE1 GLN A 190     -62.442  84.527   7.953  1.00 52.59           O  
-ATOM   1118  NE2 GLN A 190     -63.062  86.677   8.273  1.00 54.43           N  
-ATOM   1119  N   VAL A 191     -65.379  83.303  13.262  1.00 39.60           N  
-ATOM   1120  CA  VAL A 191     -65.185  82.541  14.492  1.00 36.41           C  
-ATOM   1121  C   VAL A 191     -66.445  81.725  14.740  1.00 35.78           C  
-ATOM   1122  O   VAL A 191     -66.383  80.509  14.907  1.00 35.83           O  
-ATOM   1123  CB  VAL A 191     -64.932  83.477  15.689  1.00 35.26           C  
-ATOM   1124  CG1 VAL A 191     -64.922  82.690  16.995  1.00 32.42           C  
-ATOM   1125  CG2 VAL A 191     -63.608  84.181  15.493  1.00 34.61           C  
-ATOM   1126  N   TYR A 192     -67.587  82.406  14.763  1.00 34.73           N  
-ATOM   1127  CA  TYR A 192     -68.877  81.753  14.951  1.00 33.26           C  
-ATOM   1128  C   TYR A 192     -69.001  80.616  13.936  1.00 33.02           C  
-ATOM   1129  O   TYR A 192     -69.374  79.492  14.268  1.00 32.36           O  
-ATOM   1130  CB  TYR A 192     -70.011  82.740  14.702  1.00 32.77           C  
-ATOM   1131  CG  TYR A 192     -70.552  83.423  15.923  1.00 34.34           C  
-ATOM   1132  CD1 TYR A 192     -70.144  84.712  16.269  1.00 35.86           C  
-ATOM   1133  CD2 TYR A 192     -71.518  82.800  16.711  1.00 35.67           C  
-ATOM   1134  CE1 TYR A 192     -70.693  85.370  17.374  1.00 37.27           C  
-ATOM   1135  CE2 TYR A 192     -72.076  83.440  17.810  1.00 37.13           C  
-ATOM   1136  CZ  TYR A 192     -71.664  84.724  18.136  1.00 38.73           C  
-ATOM   1137  OH  TYR A 192     -72.251  85.361  19.207  1.00 40.44           O  
-ATOM   1138  N   GLN A 193     -68.689  80.930  12.686  1.00 32.80           N  
-ATOM   1139  CA  GLN A 193     -68.768  79.956  11.620  1.00 33.70           C  
-ATOM   1140  C   GLN A 193     -67.846  78.763  11.894  1.00 32.28           C  
-ATOM   1141  O   GLN A 193     -68.228  77.613  11.660  1.00 31.66           O  
-ATOM   1142  CB  GLN A 193     -68.410  80.631  10.297  1.00 38.59           C  
-ATOM   1143  CG  GLN A 193     -69.329  80.251   9.144  1.00 46.83           C  
-ATOM   1144  CD  GLN A 193     -70.800  80.440   9.497  1.00 52.30           C  
-ATOM   1145  OE1 GLN A 193     -71.220  81.547   9.865  1.00 53.94           O  
-ATOM   1146  NE2 GLN A 193     -71.592  79.355   9.395  1.00 54.02           N  
-ATOM   1147  N   ALA A 194     -66.640  79.044  12.394  1.00 29.96           N  
-ATOM   1148  CA  ALA A 194     -65.656  78.010  12.715  1.00 25.97           C  
-ATOM   1149  C   ALA A 194     -66.162  77.095  13.817  1.00 25.32           C  
-ATOM   1150  O   ALA A 194     -66.029  75.880  13.725  1.00 25.13           O  
-ATOM   1151  CB  ALA A 194     -64.372  78.645  13.147  1.00 24.11           C  
-ATOM   1152  N   LEU A 195     -66.731  77.685  14.867  1.00 24.72           N  
-ATOM   1153  CA  LEU A 195     -67.267  76.911  15.977  1.00 24.12           C  
-ATOM   1154  C   LEU A 195     -68.398  76.038  15.461  1.00 25.65           C  
-ATOM   1155  O   LEU A 195     -68.577  74.909  15.907  1.00 26.59           O  
-ATOM   1156  CB  LEU A 195     -67.778  77.833  17.086  1.00 22.06           C  
-ATOM   1157  CG  LEU A 195     -66.725  78.657  17.842  1.00 21.86           C  
-ATOM   1158  CD1 LEU A 195     -67.403  79.473  18.918  1.00 21.24           C  
-ATOM   1159  CD2 LEU A 195     -65.686  77.746  18.473  1.00 21.77           C  
-ATOM   1160  N   ASP A 196     -69.163  76.556  14.509  1.00 27.47           N  
-ATOM   1161  CA  ASP A 196     -70.260  75.789  13.937  1.00 28.82           C  
-ATOM   1162  C   ASP A 196     -69.710  74.515  13.336  1.00 29.46           C  
-ATOM   1163  O   ASP A 196     -70.163  73.417  13.665  1.00 29.04           O  
-ATOM   1164  CB  ASP A 196     -70.961  76.598  12.851  1.00 31.60           C  
-ATOM   1165  CG  ASP A 196     -72.017  77.522  13.413  1.00 34.56           C  
-ATOM   1166  OD1 ASP A 196     -72.382  78.506  12.717  1.00 32.52           O  
-ATOM   1167  OD2 ASP A 196     -72.484  77.241  14.550  1.00 35.78           O  
-ATOM   1168  N   ALA A 197     -68.722  74.678  12.456  1.00 30.34           N  
-ATOM   1169  CA  ALA A 197     -68.076  73.562  11.770  1.00 31.06           C  
-ATOM   1170  C   ALA A 197     -67.471  72.568  12.757  1.00 32.39           C  
-ATOM   1171  O   ALA A 197     -67.570  71.350  12.572  1.00 33.66           O  
-ATOM   1172  CB  ALA A 197     -67.003  74.083  10.847  1.00 30.45           C  
-ATOM   1173  N   LEU A 198     -66.847  73.095  13.807  1.00 31.94           N  
-ATOM   1174  CA  LEU A 198     -66.227  72.266  14.829  1.00 30.58           C  
-ATOM   1175  C   LEU A 198     -67.225  71.236  15.341  1.00 30.57           C  
-ATOM   1176  O   LEU A 198     -66.872  70.090  15.593  1.00 31.89           O  
-ATOM   1177  CB  LEU A 198     -65.764  73.141  15.987  1.00 30.02           C  
-ATOM   1178  CG  LEU A 198     -64.702  72.552  16.903  1.00 29.55           C  
-ATOM   1179  CD1 LEU A 198     -63.412  72.372  16.126  1.00 28.09           C  
-ATOM   1180  CD2 LEU A 198     -64.481  73.489  18.076  1.00 30.67           C  
-ATOM   1181  N   VAL A 199     -68.480  71.653  15.473  1.00 29.70           N  
-ATOM   1182  CA  VAL A 199     -69.538  70.786  15.972  1.00 28.43           C  
-ATOM   1183  C   VAL A 199     -70.264  70.011  14.886  1.00 28.76           C  
-ATOM   1184  O   VAL A 199     -70.368  68.788  14.948  1.00 29.44           O  
-ATOM   1185  CB  VAL A 199     -70.575  71.604  16.738  1.00 27.08           C  
-ATOM   1186  CG1 VAL A 199     -71.684  70.712  17.236  1.00 26.11           C  
-ATOM   1187  CG2 VAL A 199     -69.903  72.314  17.886  1.00 28.05           C  
-ATOM   1188  N   GLU A 200     -70.781  70.730  13.899  1.00 28.36           N  
-ATOM   1189  CA  GLU A 200     -71.519  70.117  12.810  1.00 28.22           C  
-ATOM   1190  C   GLU A 200     -70.695  69.174  11.942  1.00 28.37           C  
-ATOM   1191  O   GLU A 200     -71.242  68.321  11.232  1.00 27.93           O  
-ATOM   1192  CB  GLU A 200     -72.125  71.214  11.945  1.00 28.89           C  
-ATOM   1193  CG  GLU A 200     -73.435  71.750  12.478  1.00 31.56           C  
-ATOM   1194  CD  GLU A 200     -73.678  73.189  12.072  1.00 35.33           C  
-ATOM   1195  OE1 GLU A 200     -73.244  73.575  10.954  1.00 34.88           O  
-ATOM   1196  OE2 GLU A 200     -74.311  73.926  12.874  1.00 35.73           O  
-ATOM   1197  N   VAL A 201     -69.377  69.317  12.010  1.00 27.95           N  
-ATOM   1198  CA  VAL A 201     -68.498  68.497  11.194  1.00 27.35           C  
-ATOM   1199  C   VAL A 201     -67.457  67.648  11.941  1.00 28.25           C  
-ATOM   1200  O   VAL A 201     -67.441  66.429  11.793  1.00 28.46           O  
-ATOM   1201  CB  VAL A 201     -67.795  69.395  10.128  1.00 26.10           C  
-ATOM   1202  CG1 VAL A 201     -66.686  68.634   9.423  1.00 25.67           C  
-ATOM   1203  CG2 VAL A 201     -68.815  69.879   9.116  1.00 22.70           C  
-ATOM   1204  N   ASP A 202     -66.598  68.268  12.743  1.00 29.66           N  
-ATOM   1205  CA  ASP A 202     -65.565  67.514  13.448  1.00 31.78           C  
-ATOM   1206  C   ASP A 202     -66.036  66.619  14.575  1.00 31.30           C  
-ATOM   1207  O   ASP A 202     -65.775  65.412  14.577  1.00 30.59           O  
-ATOM   1208  CB  ASP A 202     -64.486  68.456  13.983  1.00 36.21           C  
-ATOM   1209  CG  ASP A 202     -63.589  68.988  12.882  1.00 42.65           C  
-ATOM   1210  OD1 ASP A 202     -63.894  70.078  12.336  1.00 44.89           O  
-ATOM   1211  OD2 ASP A 202     -62.586  68.297  12.551  1.00 46.79           O  
-ATOM   1212  N   LEU A 203     -66.714  67.218  15.546  1.00 31.02           N  
-ATOM   1213  CA  LEU A 203     -67.208  66.477  16.692  1.00 30.13           C  
-ATOM   1214  C   LEU A 203     -68.173  65.399  16.258  1.00 29.98           C  
-ATOM   1215  O   LEU A 203     -68.291  64.361  16.904  1.00 30.18           O  
-ATOM   1216  CB  LEU A 203     -67.887  67.426  17.675  1.00 30.03           C  
-ATOM   1217  CG  LEU A 203     -67.064  67.656  18.947  1.00 32.36           C  
-ATOM   1218  CD1 LEU A 203     -65.698  68.293  18.623  1.00 30.89           C  
-ATOM   1219  CD2 LEU A 203     -67.861  68.535  19.890  1.00 33.93           C  
-ATOM   1220  N   ASP A 204     -68.853  65.653  15.148  1.00 29.45           N  
-ATOM   1221  CA  ASP A 204     -69.827  64.724  14.606  1.00 29.16           C  
-ATOM   1222  C   ASP A 204     -69.143  63.596  13.877  1.00 29.23           C  
-ATOM   1223  O   ASP A 204     -69.603  62.463  13.899  1.00 30.93           O  
-ATOM   1224  CB  ASP A 204     -70.761  65.450  13.641  1.00 30.31           C  
-ATOM   1225  CG  ASP A 204     -71.786  64.523  13.017  1.00 31.13           C  
-ATOM   1226  OD1 ASP A 204     -72.561  63.896  13.783  1.00 32.06           O  
-ATOM   1227  OD2 ASP A 204     -71.814  64.428  11.767  1.00 30.32           O  
-ATOM   1228  N   LEU A 205     -68.040  63.915  13.218  1.00 30.26           N  
-ATOM   1229  CA  LEU A 205     -67.288  62.921  12.465  1.00 29.81           C  
-ATOM   1230  C   LEU A 205     -66.527  62.024  13.434  1.00 29.69           C  
-ATOM   1231  O   LEU A 205     -66.491  60.809  13.274  1.00 28.61           O  
-ATOM   1232  CB  LEU A 205     -66.322  63.624  11.518  1.00 28.94           C  
-ATOM   1233  CG  LEU A 205     -65.948  62.832  10.282  1.00 27.29           C  
-ATOM   1234  CD1 LEU A 205     -67.197  62.371   9.583  1.00 27.52           C  
-ATOM   1235  CD2 LEU A 205     -65.126  63.702   9.379  1.00 28.46           C  
-ATOM   1236  N   THR A 206     -65.927  62.640  14.446  1.00 30.19           N  
-ATOM   1237  CA  THR A 206     -65.186  61.907  15.458  1.00 31.55           C  
-ATOM   1238  C   THR A 206     -66.000  60.747  16.031  1.00 32.31           C  
-ATOM   1239  O   THR A 206     -65.440  59.711  16.407  1.00 33.30           O  
-ATOM   1240  CB  THR A 206     -64.767  62.842  16.614  1.00 31.60           C  
-ATOM   1241  OG1 THR A 206     -63.364  63.121  16.510  1.00 34.93           O  
-ATOM   1242  CG2 THR A 206     -65.071  62.204  17.980  1.00 30.48           C  
-ATOM   1243  N   GLU A 207     -67.318  60.926  16.104  1.00 33.08           N  
-ATOM   1244  CA  GLU A 207     -68.199  59.902  16.652  1.00 33.29           C  
-ATOM   1245  C   GLU A 207     -68.521  58.872  15.618  1.00 31.28           C  
-ATOM   1246  O   GLU A 207     -68.403  57.678  15.864  1.00 31.12           O  
-ATOM   1247  CB  GLU A 207     -69.493  60.520  17.194  1.00 37.10           C  
-ATOM   1248  CG  GLU A 207     -69.307  61.184  18.567  1.00 44.07           C  
-ATOM   1249  CD  GLU A 207     -68.655  60.244  19.601  1.00 48.35           C  
-ATOM   1250  OE1 GLU A 207     -67.834  60.743  20.412  1.00 49.02           O  
-ATOM   1251  OE2 GLU A 207     -68.965  59.019  19.603  1.00 49.62           O  
-ATOM   1252  N   ARG A 208     -68.919  59.341  14.448  1.00 30.34           N  
-ATOM   1253  CA  ARG A 208     -69.248  58.450  13.361  1.00 29.43           C  
-ATOM   1254  C   ARG A 208     -68.062  57.500  13.109  1.00 28.93           C  
-ATOM   1255  O   ARG A 208     -68.262  56.294  13.002  1.00 29.18           O  
-ATOM   1256  CB  ARG A 208     -69.591  59.280  12.122  1.00 30.38           C  
-ATOM   1257  CG  ARG A 208     -70.096  58.472  10.957  1.00 34.71           C  
-ATOM   1258  CD  ARG A 208     -71.460  58.947  10.504  1.00 38.45           C  
-ATOM   1259  NE  ARG A 208     -71.462  59.450   9.129  1.00 40.30           N  
-ATOM   1260  CZ  ARG A 208     -71.073  60.670   8.773  1.00 39.15           C  
-ATOM   1261  NH1 ARG A 208     -70.643  61.528   9.691  1.00 38.22           N  
-ATOM   1262  NH2 ARG A 208     -71.131  61.034   7.498  1.00 38.72           N  
-ATOM   1263  N   LEU A 209     -66.836  58.032  13.048  1.00 28.93           N  
-ATOM   1264  CA  LEU A 209     -65.642  57.208  12.815  1.00 28.11           C  
-ATOM   1265  C   LEU A 209     -65.312  56.280  13.966  1.00 29.03           C  
-ATOM   1266  O   LEU A 209     -64.859  55.167  13.740  1.00 27.37           O  
-ATOM   1267  CB  LEU A 209     -64.404  58.064  12.513  1.00 27.85           C  
-ATOM   1268  CG  LEU A 209     -64.181  58.602  11.090  1.00 27.03           C  
-ATOM   1269  CD1 LEU A 209     -64.247  57.463  10.092  1.00 25.77           C  
-ATOM   1270  CD2 LEU A 209     -65.233  59.632  10.758  1.00 27.16           C  
-ATOM   1271  N   HIS A 210     -65.504  56.724  15.204  1.00 33.15           N  
-ATOM   1272  CA  HIS A 210     -65.230  55.833  16.329  1.00 36.90           C  
-ATOM   1273  C   HIS A 210     -66.174  54.629  16.147  1.00 36.27           C  
-ATOM   1274  O   HIS A 210     -65.740  53.476  16.186  1.00 35.83           O  
-ATOM   1275  CB  HIS A 210     -65.448  56.558  17.676  1.00 41.95           C  
-ATOM   1276  CG  HIS A 210     -65.714  55.633  18.835  1.00 52.46           C  
-ATOM   1277  ND1 HIS A 210     -65.136  54.383  18.951  1.00 55.06           N  
-ATOM   1278  CD2 HIS A 210     -66.497  55.780  19.936  1.00 55.90           C  
-ATOM   1279  CE1 HIS A 210     -65.553  53.801  20.066  1.00 54.85           C  
-ATOM   1280  NE2 HIS A 210     -66.379  54.627  20.683  1.00 55.01           N  
-ATOM   1281  N   GLU A 211     -67.455  54.904  15.904  1.00 36.09           N  
-ATOM   1282  CA  GLU A 211     -68.455  53.855  15.687  1.00 36.51           C  
-ATOM   1283  C   GLU A 211     -68.042  52.868  14.589  1.00 34.84           C  
-ATOM   1284  O   GLU A 211     -68.154  51.650  14.752  1.00 33.88           O  
-ATOM   1285  CB  GLU A 211     -69.809  54.473  15.300  1.00 39.93           C  
-ATOM   1286  CG  GLU A 211     -70.806  54.570  16.437  1.00 45.22           C  
-ATOM   1287  CD  GLU A 211     -70.837  53.294  17.271  1.00 50.80           C  
-ATOM   1288  OE1 GLU A 211     -71.105  52.193  16.709  1.00 51.66           O  
-ATOM   1289  OE2 GLU A 211     -70.584  53.397  18.496  1.00 53.10           O  
-ATOM   1290  N   LEU A 212     -67.585  53.412  13.464  1.00 32.85           N  
-ATOM   1291  CA  LEU A 212     -67.156  52.611  12.326  1.00 31.16           C  
-ATOM   1292  C   LEU A 212     -65.965  51.734  12.699  1.00 31.07           C  
-ATOM   1293  O   LEU A 212     -65.928  50.554  12.368  1.00 32.15           O  
-ATOM   1294  CB  LEU A 212     -66.769  53.524  11.169  1.00 29.54           C  
-ATOM   1295  CG  LEU A 212     -66.705  52.876   9.793  1.00 29.88           C  
-ATOM   1296  CD1 LEU A 212     -68.114  52.779   9.236  1.00 30.12           C  
-ATOM   1297  CD2 LEU A 212     -65.849  53.715   8.862  1.00 30.63           C  
-ATOM   1298  N   HIS A 213     -64.992  52.319  13.390  1.00 30.27           N  
-ATOM   1299  CA  HIS A 213     -63.801  51.596  13.813  1.00 29.07           C  
-ATOM   1300  C   HIS A 213     -64.158  50.520  14.819  1.00 28.26           C  
-ATOM   1301  O   HIS A 213     -63.463  49.526  14.952  1.00 27.66           O  
-ATOM   1302  CB  HIS A 213     -62.798  52.561  14.452  1.00 30.89           C  
-ATOM   1303  CG  HIS A 213     -61.631  51.884  15.112  1.00 31.27           C  
-ATOM   1304  ND1 HIS A 213     -61.242  52.164  16.406  1.00 30.64           N  
-ATOM   1305  CD2 HIS A 213     -60.768  50.945  14.656  1.00 29.60           C  
-ATOM   1306  CE1 HIS A 213     -60.192  51.426  16.717  1.00 29.01           C  
-ATOM   1307  NE2 HIS A 213     -59.885  50.678  15.672  1.00 28.95           N  
-ATOM   1308  N   LEU A 214     -65.245  50.730  15.539  1.00 29.14           N  
-ATOM   1309  CA  LEU A 214     -65.670  49.771  16.544  1.00 30.61           C  
-ATOM   1310  C   LEU A 214     -66.158  48.490  15.844  1.00 31.20           C  
-ATOM   1311  O   LEU A 214     -65.871  47.379  16.298  1.00 30.67           O  
-ATOM   1312  CB  LEU A 214     -66.770  50.414  17.408  1.00 31.18           C  
-ATOM   1313  CG  LEU A 214     -66.937  50.061  18.893  1.00 30.80           C  
-ATOM   1314  CD1 LEU A 214     -67.593  48.703  19.027  1.00 33.27           C  
-ATOM   1315  CD2 LEU A 214     -65.596  50.088  19.595  1.00 29.55           C  
-ATOM   1316  N   LEU A 215     -66.872  48.660  14.729  1.00 32.42           N  
-ATOM   1317  CA  LEU A 215     -67.405  47.541  13.938  1.00 33.07           C  
-ATOM   1318  C   LEU A 215     -66.290  46.762  13.289  1.00 32.85           C  
-ATOM   1319  O   LEU A 215     -66.287  45.533  13.309  1.00 34.23           O  
-ATOM   1320  CB  LEU A 215     -68.318  48.043  12.820  1.00 33.86           C  
-ATOM   1321  CG  LEU A 215     -69.813  48.205  13.057  1.00 35.08           C  
-ATOM   1322  CD1 LEU A 215     -70.087  48.780  14.442  1.00 37.85           C  
-ATOM   1323  CD2 LEU A 215     -70.358  49.116  11.974  1.00 35.89           C  
-ATOM   1324  N   ALA A 216     -65.359  47.492  12.685  1.00 31.49           N  
-ATOM   1325  CA  ALA A 216     -64.230  46.876  12.018  1.00 31.48           C  
-ATOM   1326  C   ALA A 216     -63.445  46.068  13.039  1.00 31.64           C  
-ATOM   1327  O   ALA A 216     -62.835  45.048  12.717  1.00 30.28           O  
-ATOM   1328  CB  ALA A 216     -63.355  47.943  11.398  1.00 30.78           C  
-ATOM   1329  N   PHE A 217     -63.488  46.529  14.280  1.00 33.75           N  
-ATOM   1330  CA  PHE A 217     -62.790  45.868  15.367  1.00 36.12           C  
-ATOM   1331  C   PHE A 217     -63.524  44.595  15.716  1.00 36.93           C  
-ATOM   1332  O   PHE A 217     -62.914  43.552  15.932  1.00 37.02           O  
-ATOM   1333  CB  PHE A 217     -62.741  46.772  16.593  1.00 38.15           C  
-ATOM   1334  CG  PHE A 217     -61.791  46.303  17.646  1.00 40.85           C  
-ATOM   1335  CD1 PHE A 217     -60.424  46.290  17.404  1.00 42.64           C  
-ATOM   1336  CD2 PHE A 217     -62.260  45.879  18.887  1.00 42.36           C  
-ATOM   1337  CE1 PHE A 217     -59.534  45.862  18.387  1.00 45.97           C  
-ATOM   1338  CE2 PHE A 217     -61.379  45.446  19.883  1.00 43.85           C  
-ATOM   1339  CZ  PHE A 217     -60.015  45.437  19.636  1.00 44.98           C  
-ATOM   1340  N   LYS A 218     -64.845  44.684  15.781  1.00 37.96           N  
-ATOM   1341  CA  LYS A 218     -65.634  43.513  16.100  1.00 40.11           C  
-ATOM   1342  C   LYS A 218     -65.451  42.490  14.981  1.00 40.22           C  
-ATOM   1343  O   LYS A 218     -65.137  41.325  15.233  1.00 39.68           O  
-ATOM   1344  CB  LYS A 218     -67.112  43.890  16.250  1.00 42.15           C  
-ATOM   1345  CG  LYS A 218     -68.017  42.702  16.591  1.00 47.20           C  
-ATOM   1346  CD  LYS A 218     -67.545  41.953  17.857  1.00 49.39           C  
-ATOM   1347  CE  LYS A 218     -68.313  40.642  18.084  1.00 50.09           C  
-ATOM   1348  NZ  LYS A 218     -69.786  40.854  18.256  1.00 51.20           N  
-ATOM   1349  N   MET A 219     -65.627  42.942  13.742  1.00 40.81           N  
-ATOM   1350  CA  MET A 219     -65.489  42.079  12.577  1.00 41.09           C  
-ATOM   1351  C   MET A 219     -64.146  41.337  12.537  1.00 40.34           C  
-ATOM   1352  O   MET A 219     -64.054  40.233  11.990  1.00 40.34           O  
-ATOM   1353  CB  MET A 219     -65.669  42.900  11.304  1.00 42.34           C  
-ATOM   1354  CG  MET A 219     -65.570  42.081  10.030  1.00 47.13           C  
-ATOM   1355  SD  MET A 219     -66.004  43.055   8.560  1.00 54.18           S  
-ATOM   1356  CE  MET A 219     -67.738  43.497   8.954  1.00 51.04           C  
-ATOM   1357  N   LEU A 220     -63.106  41.942  13.106  1.00 38.16           N  
-ATOM   1358  CA  LEU A 220     -61.803  41.304  13.124  1.00 35.94           C  
-ATOM   1359  C   LEU A 220     -61.807  40.229  14.183  1.00 38.60           C  
-ATOM   1360  O   LEU A 220     -61.395  39.102  13.927  1.00 40.97           O  
-ATOM   1361  CB  LEU A 220     -60.697  42.308  13.435  1.00 31.88           C  
-ATOM   1362  CG  LEU A 220     -59.318  41.664  13.606  1.00 27.52           C  
-ATOM   1363  CD1 LEU A 220     -58.933  40.988  12.312  1.00 27.02           C  
-ATOM   1364  CD2 LEU A 220     -58.284  42.693  13.994  1.00 24.07           C  
-ATOM   1365  N   ASN A 221     -62.277  40.581  15.378  1.00 40.85           N  
-ATOM   1366  CA  ASN A 221     -62.335  39.636  16.493  1.00 41.69           C  
-ATOM   1367  C   ASN A 221     -63.062  38.370  16.084  1.00 40.96           C  
-ATOM   1368  O   ASN A 221     -62.727  37.284  16.541  1.00 41.74           O  
-ATOM   1369  CB  ASN A 221     -63.037  40.273  17.695  1.00 44.72           C  
-ATOM   1370  CG  ASN A 221     -62.130  41.222  18.468  1.00 49.83           C  
-ATOM   1371  OD1 ASN A 221     -62.603  42.153  19.125  1.00 52.57           O  
-ATOM   1372  ND2 ASN A 221     -60.818  40.982  18.405  1.00 51.18           N  
-ATOM   1373  N   GLN A 222     -64.063  38.513  15.222  1.00 40.16           N  
-ATOM   1374  CA  GLN A 222     -64.820  37.368  14.746  1.00 39.30           C  
-ATOM   1375  C   GLN A 222     -63.916  36.464  13.903  1.00 39.19           C  
-ATOM   1376  O   GLN A 222     -63.815  35.268  14.155  1.00 40.30           O  
-ATOM   1377  CB  GLN A 222     -66.023  37.850  13.937  1.00 39.42           C  
-ATOM   1378  CG  GLN A 222     -67.082  38.498  14.806  1.00 41.07           C  
-ATOM   1379  CD  GLN A 222     -68.295  38.984  14.027  1.00 42.39           C  
-ATOM   1380  OE1 GLN A 222     -69.413  38.984  14.552  1.00 42.15           O  
-ATOM   1381  NE2 GLN A 222     -68.082  39.415  12.781  1.00 41.04           N  
-ATOM   1382  N   ILE A 223     -63.244  37.039  12.914  1.00 38.02           N  
-ATOM   1383  CA  ILE A 223     -62.347  36.273  12.069  1.00 37.79           C  
-ATOM   1384  C   ILE A 223     -61.230  35.575  12.873  1.00 39.62           C  
-ATOM   1385  O   ILE A 223     -60.724  34.525  12.470  1.00 39.66           O  
-ATOM   1386  CB  ILE A 223     -61.739  37.188  10.997  1.00 37.01           C  
-ATOM   1387  CG1 ILE A 223     -62.828  37.594  10.014  1.00 36.28           C  
-ATOM   1388  CG2 ILE A 223     -60.613  36.490  10.264  1.00 37.55           C  
-ATOM   1389  CD1 ILE A 223     -62.308  38.372   8.829  1.00 38.12           C  
-ATOM   1390  N   GLU A 224     -60.849  36.143  14.010  1.00 40.61           N  
-ATOM   1391  CA  GLU A 224     -59.805  35.537  14.827  1.00 42.95           C  
-ATOM   1392  C   GLU A 224     -60.323  34.296  15.560  1.00 44.16           C  
-ATOM   1393  O   GLU A 224     -59.579  33.347  15.827  1.00 44.95           O  
-ATOM   1394  CB  GLU A 224     -59.290  36.540  15.852  1.00 44.99           C  
-ATOM   1395  CG  GLU A 224     -58.723  37.812  15.265  1.00 49.04           C  
-ATOM   1396  CD  GLU A 224     -58.167  38.739  16.333  1.00 52.13           C  
-ATOM   1397  OE1 GLU A 224     -57.648  39.819  15.977  1.00 53.00           O  
-ATOM   1398  OE2 GLU A 224     -58.249  38.386  17.532  1.00 54.09           O  
-ATOM   1399  N   GLU A 225     -61.604  34.310  15.894  1.00 44.63           N  
-ATOM   1400  CA  GLU A 225     -62.205  33.195  16.604  1.00 45.37           C  
-ATOM   1401  C   GLU A 225     -62.628  32.103  15.635  1.00 45.74           C  
-ATOM   1402  O   GLU A 225     -62.681  30.928  15.995  1.00 46.32           O  
-ATOM   1403  CB  GLU A 225     -63.429  33.672  17.391  1.00 45.65           C  
-ATOM   1404  CG  GLU A 225     -64.214  32.544  18.046  1.00 47.09           C  
-ATOM   1405  CD  GLU A 225     -65.608  32.957  18.477  1.00 47.75           C  
-ATOM   1406  OE1 GLU A 225     -66.345  33.489  17.627  1.00 49.75           O  
-ATOM   1407  OE2 GLU A 225     -65.976  32.741  19.652  1.00 47.14           O  
-ATOM   1408  N   ALA A 226     -62.917  32.496  14.401  1.00 45.75           N  
-ATOM   1409  CA  ALA A 226     -63.378  31.560  13.383  1.00 47.06           C  
-ATOM   1410  C   ALA A 226     -62.443  30.404  13.051  1.00 48.19           C  
-ATOM   1411  O   ALA A 226     -62.896  29.285  12.824  1.00 48.48           O  
-ATOM   1412  CB  ALA A 226     -63.719  32.318  12.112  1.00 45.89           C  
-ATOM   1413  N   ARG A 227     -61.142  30.657  13.030  1.00 49.96           N  
-ATOM   1414  CA  ARG A 227     -60.209  29.600  12.675  1.00 51.51           C  
-ATOM   1415  C   ARG A 227     -60.153  28.412  13.635  1.00 49.82           C  
-ATOM   1416  O   ARG A 227     -59.744  27.331  13.235  1.00 50.43           O  
-ATOM   1417  CB  ARG A 227     -58.812  30.190  12.428  1.00 55.57           C  
-ATOM   1418  CG  ARG A 227     -58.161  30.832  13.624  1.00 61.82           C  
-ATOM   1419  CD  ARG A 227     -57.430  29.785  14.423  1.00 67.58           C  
-ATOM   1420  NE  ARG A 227     -56.330  29.193  13.663  1.00 71.95           N  
-ATOM   1421  CZ  ARG A 227     -55.135  29.757  13.517  1.00 74.60           C  
-ATOM   1422  NH1 ARG A 227     -54.881  30.934  14.084  1.00 75.35           N  
-ATOM   1423  NH2 ARG A 227     -54.189  29.141  12.813  1.00 75.81           N  
-ATOM   1424  N   THR A 228     -60.557  28.590  14.889  1.00 48.01           N  
-ATOM   1425  CA  THR A 228     -60.557  27.466  15.824  1.00 46.74           C  
-ATOM   1426  C   THR A 228     -61.968  27.133  16.284  1.00 47.29           C  
-ATOM   1427  O   THR A 228     -62.162  26.561  17.355  1.00 47.94           O  
-ATOM   1428  CB  THR A 228     -59.695  27.720  17.079  1.00 45.48           C  
-ATOM   1429  OG1 THR A 228     -60.011  28.998  17.637  1.00 47.77           O  
-ATOM   1430  CG2 THR A 228     -58.231  27.655  16.738  1.00 44.44           C  
-ATOM   1431  N   LEU A 229     -62.953  27.493  15.470  1.00 47.90           N  
-ATOM   1432  CA  LEU A 229     -64.347  27.220  15.791  1.00 48.85           C  
-ATOM   1433  C   LEU A 229     -64.722  25.774  15.492  1.00 50.32           C  
-ATOM   1434  O   LEU A 229     -64.743  25.349  14.335  1.00 50.98           O  
-ATOM   1435  CB  LEU A 229     -65.272  28.147  14.997  1.00 48.14           C  
-ATOM   1436  CG  LEU A 229     -65.719  29.447  15.663  1.00 47.27           C  
-ATOM   1437  CD1 LEU A 229     -66.551  30.263  14.694  1.00 46.83           C  
-ATOM   1438  CD2 LEU A 229     -66.521  29.124  16.907  1.00 46.99           C  
-ATOM   1439  N   THR A 230     -65.020  25.022  16.546  1.00 51.86           N  
-ATOM   1440  CA  THR A 230     -65.417  23.624  16.414  1.00 51.70           C  
-ATOM   1441  C   THR A 230     -66.918  23.496  16.683  1.00 51.84           C  
-ATOM   1442  O   THR A 230     -67.601  22.714  16.029  1.00 53.04           O  
-ATOM   1443  CB  THR A 230     -64.664  22.735  17.415  1.00 51.47           C  
-ATOM   1444  OG1 THR A 230     -64.963  23.159  18.753  1.00 51.40           O  
-ATOM   1445  CG2 THR A 230     -63.163  22.824  17.176  1.00 51.71           C  
-ATOM   1446  N   ASN A 231     -67.417  24.273  17.645  1.00 51.24           N  
-ATOM   1447  CA  ASN A 231     -68.832  24.263  18.024  1.00 49.53           C  
-ATOM   1448  C   ASN A 231     -69.748  24.760  16.906  1.00 49.33           C  
-ATOM   1449  O   ASN A 231     -69.632  25.891  16.453  1.00 49.89           O  
-ATOM   1450  CB  ASN A 231     -69.046  25.124  19.272  1.00 47.67           C  
-ATOM   1451  CG  ASN A 231     -70.492  25.135  19.728  1.00 46.55           C  
-ATOM   1452  OD1 ASN A 231     -71.403  25.449  18.952  1.00 44.56           O  
-ATOM   1453  ND2 ASN A 231     -70.712  24.793  20.994  1.00 44.74           N  
-ATOM   1454  N   VAL A 232     -70.675  23.910  16.485  1.00 49.46           N  
-ATOM   1455  CA  VAL A 232     -71.602  24.240  15.413  1.00 49.81           C  
-ATOM   1456  C   VAL A 232     -72.499  25.445  15.680  1.00 51.50           C  
-ATOM   1457  O   VAL A 232     -72.692  26.279  14.797  1.00 52.16           O  
-ATOM   1458  CB  VAL A 232     -72.503  23.042  15.091  1.00 48.84           C  
-ATOM   1459  CG1 VAL A 232     -73.194  22.572  16.360  1.00 48.37           C  
-ATOM   1460  CG2 VAL A 232     -73.528  23.427  14.032  1.00 46.98           C  
-ATOM   1461  N   ASP A 233     -73.063  25.540  16.879  1.00 52.83           N  
-ATOM   1462  CA  ASP A 233     -73.943  26.666  17.182  1.00 53.91           C  
-ATOM   1463  C   ASP A 233     -73.233  28.008  17.111  1.00 53.01           C  
-ATOM   1464  O   ASP A 233     -73.802  28.995  16.645  1.00 53.63           O  
-ATOM   1465  CB  ASP A 233     -74.574  26.515  18.563  1.00 56.13           C  
-ATOM   1466  CG  ASP A 233     -75.726  25.542  18.568  1.00 58.41           C  
-ATOM   1467  OD1 ASP A 233     -76.511  25.537  17.588  1.00 59.47           O  
-ATOM   1468  OD2 ASP A 233     -75.849  24.796  19.562  1.00 59.94           O  
-ATOM   1469  N   ARG A 234     -71.996  28.049  17.588  1.00 50.57           N  
-ATOM   1470  CA  ARG A 234     -71.228  29.280  17.557  1.00 48.15           C  
-ATOM   1471  C   ARG A 234     -70.908  29.633  16.098  1.00 47.10           C  
-ATOM   1472  O   ARG A 234     -70.950  30.802  15.716  1.00 48.19           O  
-ATOM   1473  CB  ARG A 234     -69.951  29.107  18.381  1.00 47.13           C  
-ATOM   1474  CG  ARG A 234     -69.092  30.346  18.528  1.00 45.75           C  
-ATOM   1475  CD  ARG A 234     -69.838  31.503  19.162  1.00 45.71           C  
-ATOM   1476  NE  ARG A 234     -68.898  32.495  19.678  1.00 46.30           N  
-ATOM   1477  CZ  ARG A 234     -69.200  33.763  19.939  1.00 45.05           C  
-ATOM   1478  NH1 ARG A 234     -70.429  34.209  19.730  1.00 44.78           N  
-ATOM   1479  NH2 ARG A 234     -68.270  34.584  20.413  1.00 43.60           N  
-ATOM   1480  N   ILE A 235     -70.607  28.622  15.284  1.00 44.95           N  
-ATOM   1481  CA  ILE A 235     -70.297  28.839  13.870  1.00 43.53           C  
-ATOM   1482  C   ILE A 235     -71.521  29.446  13.207  1.00 43.79           C  
-ATOM   1483  O   ILE A 235     -71.412  30.301  12.330  1.00 43.62           O  
-ATOM   1484  CB  ILE A 235     -69.923  27.503  13.158  1.00 42.88           C  
-ATOM   1485  CG1 ILE A 235     -68.614  26.963  13.739  1.00 43.17           C  
-ATOM   1486  CG2 ILE A 235     -69.763  27.711  11.658  1.00 39.58           C  
-ATOM   1487  CD1 ILE A 235     -68.293  25.553  13.316  1.00 43.92           C  
-ATOM   1488  N   GLN A 236     -72.689  28.993  13.648  1.00 44.72           N  
-ATOM   1489  CA  GLN A 236     -73.977  29.468  13.140  1.00 45.88           C  
-ATOM   1490  C   GLN A 236     -74.125  30.960  13.448  1.00 44.70           C  
-ATOM   1491  O   GLN A 236     -74.423  31.787  12.574  1.00 43.33           O  
-ATOM   1492  CB  GLN A 236     -75.113  28.719  13.850  1.00 48.68           C  
-ATOM   1493  CG  GLN A 236     -75.173  27.211  13.628  1.00 51.19           C  
-ATOM   1494  CD  GLN A 236     -75.980  26.841  12.395  1.00 52.78           C  
-ATOM   1495  OE1 GLN A 236     -76.216  25.665  12.127  1.00 53.20           O  
-ATOM   1496  NE2 GLN A 236     -76.408  27.850  11.636  1.00 53.84           N  
-ATOM   1497  N   GLN A 237     -73.920  31.261  14.729  1.00 43.33           N  
-ATOM   1498  CA  GLN A 237     -74.017  32.595  15.300  1.00 41.52           C  
-ATOM   1499  C   GLN A 237     -73.061  33.587  14.655  1.00 40.61           C  
-ATOM   1500  O   GLN A 237     -73.489  34.606  14.116  1.00 40.68           O  
-ATOM   1501  CB  GLN A 237     -73.735  32.502  16.795  1.00 40.55           C  
-ATOM   1502  CG  GLN A 237     -74.085  33.727  17.588  1.00 41.58           C  
-ATOM   1503  CD  GLN A 237     -73.695  33.578  19.046  1.00 43.19           C  
-ATOM   1504  OE1 GLN A 237     -73.994  34.439  19.867  1.00 44.64           O  
-ATOM   1505  NE2 GLN A 237     -73.016  32.480  19.373  1.00 43.01           N  
-ATOM   1506  N   ILE A 238     -71.768  33.288  14.718  1.00 39.41           N  
-ATOM   1507  CA  ILE A 238     -70.754  34.157  14.141  1.00 38.45           C  
-ATOM   1508  C   ILE A 238     -71.002  34.390  12.663  1.00 39.54           C  
-ATOM   1509  O   ILE A 238     -70.831  35.501  12.171  1.00 41.01           O  
-ATOM   1510  CB  ILE A 238     -69.350  33.564  14.287  1.00 37.24           C  
-ATOM   1511  CG1 ILE A 238     -69.065  33.270  15.751  1.00 37.70           C  
-ATOM   1512  CG2 ILE A 238     -68.320  34.547  13.769  1.00 36.01           C  
-ATOM   1513  CD1 ILE A 238     -69.106  34.498  16.619  1.00 38.92           C  
-ATOM   1514  N   GLN A 239     -71.402  33.344  11.951  1.00 39.99           N  
-ATOM   1515  CA  GLN A 239     -71.653  33.459  10.520  1.00 40.31           C  
-ATOM   1516  C   GLN A 239     -72.678  34.532  10.176  1.00 39.42           C  
-ATOM   1517  O   GLN A 239     -72.413  35.394   9.344  1.00 39.00           O  
-ATOM   1518  CB  GLN A 239     -72.113  32.116   9.963  1.00 42.88           C  
-ATOM   1519  CG  GLN A 239     -72.483  32.143   8.493  1.00 44.87           C  
-ATOM   1520  CD  GLN A 239     -73.099  30.838   8.053  1.00 45.97           C  
-ATOM   1521  OE1 GLN A 239     -74.109  30.399   8.613  1.00 46.61           O  
-ATOM   1522  NE2 GLN A 239     -72.493  30.200   7.054  1.00 46.49           N  
-ATOM   1523  N   THR A 240     -73.850  34.479  10.804  1.00 39.68           N  
-ATOM   1524  CA  THR A 240     -74.885  35.476  10.529  1.00 40.43           C  
-ATOM   1525  C   THR A 240     -74.545  36.823  11.170  1.00 40.14           C  
-ATOM   1526  O   THR A 240     -74.999  37.865  10.707  1.00 40.63           O  
-ATOM   1527  CB  THR A 240     -76.274  35.016  11.025  1.00 40.47           C  
-ATOM   1528  OG1 THR A 240     -76.183  34.655  12.404  1.00 41.55           O  
-ATOM   1529  CG2 THR A 240     -76.778  33.816  10.206  1.00 40.16           C  
-ATOM   1530  N   ALA A 241     -73.745  36.801  12.234  1.00 39.70           N  
-ATOM   1531  CA  ALA A 241     -73.333  38.032  12.898  1.00 38.42           C  
-ATOM   1532  C   ALA A 241     -72.379  38.739  11.962  1.00 39.35           C  
-ATOM   1533  O   ALA A 241     -72.461  39.945  11.763  1.00 41.55           O  
-ATOM   1534  CB  ALA A 241     -72.633  37.722  14.194  1.00 36.05           C  
-ATOM   1535  N   PHE A 242     -71.466  37.968  11.388  1.00 40.08           N  
-ATOM   1536  CA  PHE A 242     -70.482  38.502  10.465  1.00 41.21           C  
-ATOM   1537  C   PHE A 242     -71.203  39.017   9.229  1.00 42.60           C  
-ATOM   1538  O   PHE A 242     -70.838  40.040   8.659  1.00 43.92           O  
-ATOM   1539  CB  PHE A 242     -69.500  37.406  10.056  1.00 40.28           C  
-ATOM   1540  CG  PHE A 242     -68.423  37.877   9.133  1.00 40.04           C  
-ATOM   1541  CD1 PHE A 242     -67.166  38.207   9.626  1.00 40.80           C  
-ATOM   1542  CD2 PHE A 242     -68.676  38.030   7.771  1.00 40.20           C  
-ATOM   1543  CE1 PHE A 242     -66.170  38.686   8.780  1.00 41.70           C  
-ATOM   1544  CE2 PHE A 242     -67.695  38.508   6.910  1.00 41.36           C  
-ATOM   1545  CZ  PHE A 242     -66.436  38.838   7.414  1.00 42.59           C  
-ATOM   1546  N   GLU A 243     -72.231  38.300   8.814  1.00 43.59           N  
-ATOM   1547  CA  GLU A 243     -72.971  38.696   7.636  1.00 46.31           C  
-ATOM   1548  C   GLU A 243     -73.747  39.984   7.873  1.00 46.52           C  
-ATOM   1549  O   GLU A 243     -73.809  40.845   7.000  1.00 47.39           O  
-ATOM   1550  CB  GLU A 243     -73.910  37.564   7.228  1.00 49.97           C  
-ATOM   1551  CG  GLU A 243     -74.885  37.881   6.108  1.00 54.91           C  
-ATOM   1552  CD  GLU A 243     -75.863  36.735   5.885  1.00 59.23           C  
-ATOM   1553  OE1 GLU A 243     -76.453  36.249   6.887  1.00 60.39           O  
-ATOM   1554  OE2 GLU A 243     -76.044  36.321   4.714  1.00 61.22           O  
-ATOM   1555  N   ASN A 244     -74.337  40.122   9.054  1.00 46.58           N  
-ATOM   1556  CA  ASN A 244     -75.107  41.322   9.358  1.00 47.17           C  
-ATOM   1557  C   ASN A 244     -74.193  42.510   9.565  1.00 46.53           C  
-ATOM   1558  O   ASN A 244     -74.432  43.590   9.035  1.00 45.92           O  
-ATOM   1559  CB  ASN A 244     -75.976  41.109  10.600  1.00 48.60           C  
-ATOM   1560  CG  ASN A 244     -77.235  40.317  10.298  1.00 50.96           C  
-ATOM   1561  OD1 ASN A 244     -77.453  39.874   9.161  1.00 52.77           O  
-ATOM   1562  ND2 ASN A 244     -78.074  40.133  11.313  1.00 51.11           N  
-ATOM   1563  N   ASN A 245     -73.141  42.309  10.343  1.00 46.50           N  
-ATOM   1564  CA  ASN A 245     -72.205  43.381  10.588  1.00 46.08           C  
-ATOM   1565  C   ASN A 245     -71.697  43.899   9.241  1.00 44.78           C  
-ATOM   1566  O   ASN A 245     -71.809  45.084   8.928  1.00 45.28           O  
-ATOM   1567  CB  ASN A 245     -71.040  42.876  11.423  1.00 48.02           C  
-ATOM   1568  CG  ASN A 245     -70.076  43.978  11.777  1.00 53.35           C  
-ATOM   1569  OD1 ASN A 245     -68.870  43.746  11.911  1.00 58.23           O  
-ATOM   1570  ND2 ASN A 245     -70.597  45.196  11.936  1.00 53.20           N  
-ATOM   1571  N   LEU A 246     -71.155  42.991   8.440  1.00 42.87           N  
-ATOM   1572  CA  LEU A 246     -70.618  43.321   7.128  1.00 41.01           C  
-ATOM   1573  C   LEU A 246     -71.535  44.224   6.328  1.00 40.79           C  
-ATOM   1574  O   LEU A 246     -71.090  45.128   5.634  1.00 39.84           O  
-ATOM   1575  CB  LEU A 246     -70.386  42.038   6.338  1.00 40.93           C  
-ATOM   1576  CG  LEU A 246     -69.643  42.153   5.009  1.00 40.39           C  
-ATOM   1577  CD1 LEU A 246     -68.255  42.717   5.254  1.00 40.98           C  
-ATOM   1578  CD2 LEU A 246     -69.540  40.778   4.372  1.00 41.40           C  
-ATOM   1579  N   LYS A 247     -72.828  43.960   6.435  1.00 42.59           N  
-ATOM   1580  CA  LYS A 247     -73.847  44.703   5.710  1.00 43.34           C  
-ATOM   1581  C   LYS A 247     -73.996  46.150   6.160  1.00 41.86           C  
-ATOM   1582  O   LYS A 247     -74.035  47.057   5.331  1.00 40.97           O  
-ATOM   1583  CB  LYS A 247     -75.184  43.982   5.855  1.00 46.65           C  
-ATOM   1584  CG  LYS A 247     -76.221  44.330   4.806  1.00 52.19           C  
-ATOM   1585  CD  LYS A 247     -77.423  43.376   4.889  1.00 57.44           C  
-ATOM   1586  CE  LYS A 247     -76.999  41.881   5.039  1.00 60.62           C  
-ATOM   1587  NZ  LYS A 247     -76.053  41.360   3.992  1.00 60.23           N  
-ATOM   1588  N   ILE A 248     -74.091  46.370   7.467  1.00 40.98           N  
-ATOM   1589  CA  ILE A 248     -74.252  47.728   7.963  1.00 40.11           C  
-ATOM   1590  C   ILE A 248     -72.944  48.464   7.735  1.00 39.97           C  
-ATOM   1591  O   ILE A 248     -72.932  49.635   7.375  1.00 41.29           O  
-ATOM   1592  CB  ILE A 248     -74.651  47.778   9.483  1.00 39.65           C  
-ATOM   1593  CG1 ILE A 248     -73.535  48.421  10.291  1.00 40.46           C  
-ATOM   1594  CG2 ILE A 248     -74.956  46.387  10.027  1.00 36.01           C  
-ATOM   1595  CD1 ILE A 248     -73.892  48.616  11.731  1.00 44.90           C  
-ATOM   1596  N   MET A 249     -71.840  47.760   7.939  1.00 39.38           N  
-ATOM   1597  CA  MET A 249     -70.522  48.329   7.735  1.00 38.65           C  
-ATOM   1598  C   MET A 249     -70.446  48.848   6.310  1.00 38.40           C  
-ATOM   1599  O   MET A 249     -70.059  49.979   6.074  1.00 37.08           O  
-ATOM   1600  CB  MET A 249     -69.478  47.250   7.933  1.00 40.80           C  
-ATOM   1601  CG  MET A 249     -68.081  47.690   7.646  1.00 42.91           C  
-ATOM   1602  SD  MET A 249     -67.289  48.123   9.166  1.00 48.13           S  
-ATOM   1603  CE  MET A 249     -66.945  46.484   9.826  1.00 45.03           C  
-ATOM   1604  N   LYS A 250     -70.827  47.998   5.363  1.00 41.18           N  
-ATOM   1605  CA  LYS A 250     -70.817  48.330   3.937  1.00 43.58           C  
-ATOM   1606  C   LYS A 250     -71.610  49.591   3.622  1.00 44.64           C  
-ATOM   1607  O   LYS A 250     -71.304  50.320   2.680  1.00 44.50           O  
-ATOM   1608  CB  LYS A 250     -71.393  47.163   3.129  1.00 43.43           C  
-ATOM   1609  CG  LYS A 250     -70.384  46.466   2.241  1.00 46.01           C  
-ATOM   1610  CD  LYS A 250     -70.984  45.239   1.566  1.00 48.44           C  
-ATOM   1611  CE  LYS A 250     -69.974  44.570   0.641  1.00 50.06           C  
-ATOM   1612  NZ  LYS A 250     -70.434  43.226   0.184  1.00 50.79           N  
-ATOM   1613  N   ARG A 251     -72.631  49.836   4.427  1.00 46.56           N  
-ATOM   1614  CA  ARG A 251     -73.495  50.984   4.255  1.00 48.54           C  
-ATOM   1615  C   ARG A 251     -72.932  52.216   4.939  1.00 48.02           C  
-ATOM   1616  O   ARG A 251     -72.941  53.295   4.365  1.00 48.76           O  
-ATOM   1617  CB  ARG A 251     -74.879  50.639   4.802  1.00 52.40           C  
-ATOM   1618  CG  ARG A 251     -75.847  51.793   4.940  1.00 58.67           C  
-ATOM   1619  CD  ARG A 251     -77.187  51.275   5.464  1.00 64.81           C  
-ATOM   1620  NE  ARG A 251     -77.012  50.317   6.561  1.00 69.66           N  
-ATOM   1621  CZ  ARG A 251     -77.998  49.612   7.115  1.00 71.45           C  
-ATOM   1622  NH1 ARG A 251     -79.247  49.753   6.681  1.00 71.96           N  
-ATOM   1623  NH2 ARG A 251     -77.732  48.753   8.095  1.00 71.77           N  
-ATOM   1624  N   ARG A 252     -72.437  52.060   6.160  1.00 47.91           N  
-ATOM   1625  CA  ARG A 252     -71.877  53.187   6.888  1.00 49.29           C  
-ATOM   1626  C   ARG A 252     -70.748  53.843   6.094  1.00 51.74           C  
-ATOM   1627  O   ARG A 252     -70.673  55.068   6.014  1.00 52.53           O  
-ATOM   1628  CB  ARG A 252     -71.343  52.737   8.244  1.00 48.26           C  
-ATOM   1629  CG  ARG A 252     -72.391  52.198   9.204  1.00 49.99           C  
-ATOM   1630  CD  ARG A 252     -72.997  53.293  10.077  1.00 51.76           C  
-ATOM   1631  NE  ARG A 252     -73.723  52.746  11.227  1.00 52.14           N  
-ATOM   1632  CZ  ARG A 252     -74.956  52.242  11.182  1.00 52.72           C  
-ATOM   1633  NH1 ARG A 252     -75.635  52.212  10.036  1.00 52.89           N  
-ATOM   1634  NH2 ARG A 252     -75.505  51.747  12.287  1.00 51.12           N  
-ATOM   1635  N   VAL A 253     -69.876  53.035   5.498  1.00 54.07           N  
-ATOM   1636  CA  VAL A 253     -68.757  53.579   4.730  1.00 56.45           C  
-ATOM   1637  C   VAL A 253     -69.172  54.381   3.496  1.00 59.79           C  
-ATOM   1638  O   VAL A 253     -68.605  55.441   3.232  1.00 60.13           O  
-ATOM   1639  CB  VAL A 253     -67.786  52.474   4.273  1.00 54.19           C  
-ATOM   1640  CG1 VAL A 253     -67.327  51.680   5.465  1.00 52.81           C  
-ATOM   1641  CG2 VAL A 253     -68.447  51.582   3.248  1.00 53.55           C  
-ATOM   1642  N   LEU A 254     -70.154  53.876   2.745  1.00 63.35           N  
-ATOM   1643  CA  LEU A 254     -70.632  54.548   1.535  1.00 66.28           C  
-ATOM   1644  C   LEU A 254     -71.098  55.970   1.788  1.00 69.09           C  
-ATOM   1645  O   LEU A 254     -70.981  56.834   0.914  1.00 69.88           O  
-ATOM   1646  CB  LEU A 254     -71.780  53.768   0.898  1.00 65.30           C  
-ATOM   1647  CG  LEU A 254     -71.420  52.419   0.280  1.00 66.86           C  
-ATOM   1648  CD1 LEU A 254     -72.646  51.853  -0.416  1.00 67.60           C  
-ATOM   1649  CD2 LEU A 254     -70.278  52.582  -0.712  1.00 66.73           C  
-ATOM   1650  N   ALA A 255     -71.629  56.210   2.984  1.00 72.13           N  
-ATOM   1651  CA  ALA A 255     -72.123  57.532   3.351  1.00 74.23           C  
-ATOM   1652  C   ALA A 255     -71.008  58.496   3.766  1.00 75.60           C  
-ATOM   1653  O   ALA A 255     -71.163  59.708   3.622  1.00 75.83           O  
-ATOM   1654  CB  ALA A 255     -73.163  57.407   4.470  1.00 73.70           C  
-ATOM   1655  N   VAL A 256     -69.893  57.963   4.274  1.00 77.28           N  
-ATOM   1656  CA  VAL A 256     -68.758  58.793   4.698  1.00 79.20           C  
-ATOM   1657  C   VAL A 256     -68.147  59.563   3.519  1.00 81.28           C  
-ATOM   1658  O   VAL A 256     -67.520  58.979   2.629  1.00 81.07           O  
-ATOM   1659  CB  VAL A 256     -67.656  57.935   5.405  1.00 78.42           C  
-ATOM   1660  CG1 VAL A 256     -66.272  58.552   5.225  1.00 76.31           C  
-ATOM   1661  CG2 VAL A 256     -67.976  57.841   6.890  1.00 77.32           C  
-ATOM   1662  N   GLU A 257     -68.344  60.881   3.526  1.00 83.31           N  
-ATOM   1663  CA  GLU A 257     -67.828  61.760   2.475  1.00 84.69           C  
-ATOM   1664  C   GLU A 257     -66.299  61.823   2.482  1.00 85.06           C  
-ATOM   1665  O   GLU A 257     -65.710  62.723   3.086  1.00 85.54           O  
-ATOM   1666  CB  GLU A 257     -68.394  63.179   2.637  1.00 85.74           C  
-ATOM   1667  CG  GLU A 257     -69.311  63.639   1.502  1.00 87.34           C  
-ATOM   1668  CD  GLU A 257     -70.778  63.335   1.761  1.00 88.60           C  
-ATOM   1669  OE1 GLU A 257     -71.592  63.514   0.826  1.00 88.08           O  
-ATOM   1670  OE2 GLU A 257     -71.116  62.932   2.901  1.00 88.37           O  
-ATOM   1671  N   ASP A 258     -65.660  60.870   1.805  1.00 84.41           N  
-ATOM   1672  CA  ASP A 258     -64.201  60.826   1.724  1.00 83.08           C  
-ATOM   1673  C   ASP A 258     -63.776  59.862   0.615  1.00 82.80           C  
-ATOM   1674  O   ASP A 258     -63.540  58.677   0.851  1.00 83.50           O  
-ATOM   1675  CB  ASP A 258     -63.615  60.388   3.058  1.00 82.40           C  
-ATOM   1676  CG  ASP A 258     -62.121  60.491   3.084  1.00 82.05           C  
-ATOM   1677  OD1 ASP A 258     -61.527  60.183   4.138  1.00 81.61           O  
-ATOM   1678  OD2 ASP A 258     -61.539  60.878   2.048  1.00 82.12           O  
-ATOM   1679  N   PRO A 259     -63.659  60.377  -0.618  1.00 81.82           N  
-ATOM   1680  CA  PRO A 259     -63.278  59.666  -1.844  1.00 79.83           C  
-ATOM   1681  C   PRO A 259     -62.398  58.424  -1.700  1.00 77.74           C  
-ATOM   1682  O   PRO A 259     -62.902  57.338  -1.430  1.00 77.63           O  
-ATOM   1683  CB  PRO A 259     -62.620  60.761  -2.669  1.00 80.37           C  
-ATOM   1684  CG  PRO A 259     -63.507  61.925  -2.353  1.00 82.19           C  
-ATOM   1685  CD  PRO A 259     -63.645  61.832  -0.851  1.00 81.61           C  
-ATOM   1686  N   THR A 260     -61.090  58.581  -1.881  1.00 75.73           N  
-ATOM   1687  CA  THR A 260     -60.152  57.456  -1.789  1.00 74.16           C  
-ATOM   1688  C   THR A 260     -60.441  56.462  -0.667  1.00 72.29           C  
-ATOM   1689  O   THR A 260     -60.366  55.250  -0.865  1.00 71.60           O  
-ATOM   1690  CB  THR A 260     -58.703  57.949  -1.590  1.00 74.40           C  
-ATOM   1691  OG1 THR A 260     -58.428  59.015  -2.505  1.00 74.68           O  
-ATOM   1692  CG2 THR A 260     -57.708  56.808  -1.832  1.00 73.54           C  
-ATOM   1693  N   ARG A 261     -60.761  56.986   0.511  1.00 70.57           N  
-ATOM   1694  CA  ARG A 261     -61.036  56.156   1.679  1.00 67.81           C  
-ATOM   1695  C   ARG A 261     -62.288  55.273   1.543  1.00 65.85           C  
-ATOM   1696  O   ARG A 261     -62.238  54.084   1.864  1.00 65.78           O  
-ATOM   1697  CB  ARG A 261     -61.130  57.039   2.940  1.00 66.98           C  
-ATOM   1698  CG  ARG A 261     -59.815  57.754   3.344  1.00 63.34           C  
-ATOM   1699  CD  ARG A 261     -58.720  56.766   3.727  1.00 61.30           C  
-ATOM   1700  NE  ARG A 261     -57.511  57.383   4.282  1.00 59.79           N  
-ATOM   1701  CZ  ARG A 261     -57.490  58.270   5.277  1.00 58.90           C  
-ATOM   1702  NH1 ARG A 261     -58.619  58.677   5.838  1.00 58.54           N  
-ATOM   1703  NH2 ARG A 261     -56.332  58.721   5.747  1.00 57.43           N  
-ATOM   1704  N   SER A 262     -63.401  55.833   1.068  1.00 62.99           N  
-ATOM   1705  CA  SER A 262     -64.621  55.043   0.902  1.00 60.95           C  
-ATOM   1706  C   SER A 262     -64.431  53.902  -0.090  1.00 60.65           C  
-ATOM   1707  O   SER A 262     -64.914  52.794   0.140  1.00 61.79           O  
-ATOM   1708  CB  SER A 262     -65.785  55.923   0.459  1.00 59.83           C  
-ATOM   1709  OG  SER A 262     -66.271  56.679   1.551  1.00 60.38           O  
-ATOM   1710  N   LYS A 263     -63.740  54.169  -1.195  1.00 59.18           N  
-ATOM   1711  CA  LYS A 263     -63.468  53.128  -2.184  1.00 57.19           C  
-ATOM   1712  C   LYS A 263     -62.620  52.048  -1.502  1.00 55.26           C  
-ATOM   1713  O   LYS A 263     -62.983  50.872  -1.505  1.00 55.02           O  
-ATOM   1714  CB  LYS A 263     -62.719  53.720  -3.389  1.00 58.98           C  
-ATOM   1715  CG  LYS A 263     -61.526  52.890  -3.921  1.00 61.61           C  
-ATOM   1716  CD  LYS A 263     -61.927  51.557  -4.566  1.00 62.75           C  
-ATOM   1717  CE  LYS A 263     -62.803  51.761  -5.792  1.00 63.82           C  
-ATOM   1718  NZ  LYS A 263     -62.146  52.634  -6.802  1.00 64.32           N  
-ATOM   1719  N   GLN A 264     -61.497  52.464  -0.915  1.00 52.69           N  
-ATOM   1720  CA  GLN A 264     -60.590  51.559  -0.214  1.00 49.79           C  
-ATOM   1721  C   GLN A 264     -61.344  50.586   0.668  1.00 47.67           C  
-ATOM   1722  O   GLN A 264     -61.131  49.374   0.617  1.00 46.47           O  
-ATOM   1723  CB  GLN A 264     -59.635  52.340   0.688  1.00 50.34           C  
-ATOM   1724  CG  GLN A 264     -58.533  53.080  -0.014  1.00 51.93           C  
-ATOM   1725  CD  GLN A 264     -57.326  53.229   0.878  1.00 52.76           C  
-ATOM   1726  OE1 GLN A 264     -56.787  52.234   1.360  1.00 52.46           O  
-ATOM   1727  NE2 GLN A 264     -56.894  54.469   1.111  1.00 53.93           N  
-ATOM   1728  N   MET A 265     -62.211  51.141   1.501  1.00 45.65           N  
-ATOM   1729  CA  MET A 265     -62.990  50.342   2.416  1.00 44.42           C  
-ATOM   1730  C   MET A 265     -64.050  49.511   1.709  1.00 45.20           C  
-ATOM   1731  O   MET A 265     -64.170  48.318   1.979  1.00 45.71           O  
-ATOM   1732  CB  MET A 265     -63.619  51.238   3.481  1.00 42.54           C  
-ATOM   1733  CG  MET A 265     -62.605  51.808   4.448  1.00 40.22           C  
-ATOM   1734  SD  MET A 265     -63.361  52.658   5.837  1.00 39.46           S  
-ATOM   1735  CE  MET A 265     -64.070  54.075   5.001  1.00 40.98           C  
-ATOM   1736  N   SER A 266     -64.819  50.122   0.809  1.00 45.60           N  
-ATOM   1737  CA  SER A 266     -65.846  49.371   0.089  1.00 46.61           C  
-ATOM   1738  C   SER A 266     -65.220  48.166  -0.607  1.00 46.95           C  
-ATOM   1739  O   SER A 266     -65.839  47.106  -0.718  1.00 47.46           O  
-ATOM   1740  CB  SER A 266     -66.556  50.255  -0.936  1.00 47.09           C  
-ATOM   1741  OG  SER A 266     -67.554  51.043  -0.313  1.00 49.38           O  
-ATOM   1742  N   GLN A 267     -63.990  48.339  -1.077  1.00 46.53           N  
-ATOM   1743  CA  GLN A 267     -63.269  47.262  -1.731  1.00 46.26           C  
-ATOM   1744  C   GLN A 267     -63.027  46.191  -0.662  1.00 43.65           C  
-ATOM   1745  O   GLN A 267     -63.568  45.091  -0.749  1.00 44.10           O  
-ATOM   1746  CB  GLN A 267     -61.939  47.785  -2.272  1.00 51.60           C  
-ATOM   1747  CG  GLN A 267     -61.194  46.829  -3.195  1.00 58.05           C  
-ATOM   1748  CD  GLN A 267     -61.905  46.638  -4.525  1.00 62.03           C  
-ATOM   1749  OE1 GLN A 267     -62.835  45.827  -4.644  1.00 63.00           O  
-ATOM   1750  NE2 GLN A 267     -61.478  47.401  -5.536  1.00 63.90           N  
-ATOM   1751  N   LEU A 268     -62.223  46.526   0.347  1.00 40.05           N  
-ATOM   1752  CA  LEU A 268     -61.924  45.612   1.451  1.00 36.28           C  
-ATOM   1753  C   LEU A 268     -63.176  44.860   1.921  1.00 36.86           C  
-ATOM   1754  O   LEU A 268     -63.134  43.653   2.174  1.00 36.12           O  
-ATOM   1755  CB  LEU A 268     -61.334  46.395   2.624  1.00 31.93           C  
-ATOM   1756  CG  LEU A 268     -59.842  46.732   2.624  1.00 28.25           C  
-ATOM   1757  CD1 LEU A 268     -59.555  47.823   3.639  1.00 26.97           C  
-ATOM   1758  CD2 LEU A 268     -59.044  45.490   2.955  1.00 26.00           C  
-ATOM   1759  N   LEU A 269     -64.288  45.582   2.041  1.00 37.83           N  
-ATOM   1760  CA  LEU A 269     -65.551  44.987   2.469  1.00 37.88           C  
-ATOM   1761  C   LEU A 269     -66.096  43.979   1.472  1.00 39.00           C  
-ATOM   1762  O   LEU A 269     -66.433  42.865   1.859  1.00 39.68           O  
-ATOM   1763  CB  LEU A 269     -66.605  46.064   2.726  1.00 35.34           C  
-ATOM   1764  CG  LEU A 269     -66.472  46.782   4.067  1.00 33.89           C  
-ATOM   1765  CD1 LEU A 269     -67.533  47.840   4.156  1.00 33.73           C  
-ATOM   1766  CD2 LEU A 269     -66.609  45.793   5.216  1.00 32.60           C  
-ATOM   1767  N   THR A 270     -66.189  44.353   0.195  1.00 40.35           N  
-ATOM   1768  CA  THR A 270     -66.698  43.410  -0.806  1.00 41.37           C  
-ATOM   1769  C   THR A 270     -65.774  42.196  -0.884  1.00 40.84           C  
-ATOM   1770  O   THR A 270     -66.230  41.072  -1.090  1.00 40.72           O  
-ATOM   1771  CB  THR A 270     -66.830  44.046  -2.213  1.00 40.64           C  
-ATOM   1772  OG1 THR A 270     -65.553  44.505  -2.648  1.00 40.62           O  
-ATOM   1773  CG2 THR A 270     -67.818  45.219  -2.188  1.00 41.78           C  
-ATOM   1774  N   GLU A 271     -64.478  42.420  -0.700  1.00 40.72           N  
-ATOM   1775  CA  GLU A 271     -63.533  41.319  -0.727  1.00 41.95           C  
-ATOM   1776  C   GLU A 271     -63.775  40.374   0.434  1.00 41.72           C  
-ATOM   1777  O   GLU A 271     -63.810  39.169   0.246  1.00 42.84           O  
-ATOM   1778  CB  GLU A 271     -62.098  41.831  -0.693  1.00 44.14           C  
-ATOM   1779  CG  GLU A 271     -61.563  42.130  -2.070  1.00 47.93           C  
-ATOM   1780  CD  GLU A 271     -61.729  40.941  -2.988  1.00 51.30           C  
-ATOM   1781  OE1 GLU A 271     -61.160  39.869  -2.678  1.00 52.61           O  
-ATOM   1782  OE2 GLU A 271     -62.438  41.075  -4.011  1.00 53.36           O  
-ATOM   1783  N   LEU A 272     -63.942  40.912   1.637  1.00 41.31           N  
-ATOM   1784  CA  LEU A 272     -64.208  40.068   2.792  1.00 39.51           C  
-ATOM   1785  C   LEU A 272     -65.543  39.364   2.572  1.00 40.36           C  
-ATOM   1786  O   LEU A 272     -65.674  38.172   2.832  1.00 41.32           O  
-ATOM   1787  CB  LEU A 272     -64.259  40.910   4.065  1.00 36.93           C  
-ATOM   1788  CG  LEU A 272     -62.902  41.345   4.609  1.00 35.70           C  
-ATOM   1789  CD1 LEU A 272     -63.086  42.327   5.740  1.00 36.65           C  
-ATOM   1790  CD2 LEU A 272     -62.146  40.134   5.092  1.00 35.82           C  
-ATOM   1791  N   GLY A 273     -66.526  40.110   2.076  1.00 40.87           N  
-ATOM   1792  CA  GLY A 273     -67.840  39.548   1.822  1.00 42.21           C  
-ATOM   1793  C   GLY A 273     -67.769  38.271   1.012  1.00 43.63           C  
-ATOM   1794  O   GLY A 273     -68.547  37.343   1.232  1.00 43.58           O  
-ATOM   1795  N   LYS A 274     -66.831  38.228   0.071  1.00 43.86           N  
-ATOM   1796  CA  LYS A 274     -66.642  37.058  -0.770  1.00 43.69           C  
-ATOM   1797  C   LYS A 274     -66.093  35.866   0.020  1.00 44.59           C  
-ATOM   1798  O   LYS A 274     -66.648  34.773  -0.068  1.00 46.79           O  
-ATOM   1799  CB  LYS A 274     -65.702  37.385  -1.926  1.00 42.61           C  
-ATOM   1800  CG  LYS A 274     -66.273  38.354  -2.939  1.00 43.57           C  
-ATOM   1801  CD  LYS A 274     -65.247  38.669  -4.023  1.00 45.21           C  
-ATOM   1802  CE  LYS A 274     -65.843  39.528  -5.133  1.00 47.55           C  
-ATOM   1803  NZ  LYS A 274     -64.849  39.799  -6.213  1.00 49.54           N  
-ATOM   1804  N   ARG A 275     -65.021  36.058   0.790  1.00 43.86           N  
-ATOM   1805  CA  ARG A 275     -64.455  34.948   1.565  1.00 44.52           C  
-ATOM   1806  C   ARG A 275     -65.363  34.559   2.726  1.00 45.06           C  
-ATOM   1807  O   ARG A 275     -64.959  33.814   3.624  1.00 45.48           O  
-ATOM   1808  CB  ARG A 275     -63.051  35.276   2.116  1.00 44.50           C  
-ATOM   1809  CG  ARG A 275     -61.998  35.612   1.065  1.00 43.37           C  
-ATOM   1810  CD  ARG A 275     -62.057  37.098   0.720  1.00 43.25           C  
-ATOM   1811  NE  ARG A 275     -61.403  37.452  -0.535  1.00 39.39           N  
-ATOM   1812  CZ  ARG A 275     -60.159  37.119  -0.845  1.00 40.42           C  
-ATOM   1813  NH1 ARG A 275     -59.428  36.412   0.007  1.00 39.47           N  
-ATOM   1814  NH2 ARG A 275     -59.643  37.508  -2.002  1.00 41.50           N  
-ATOM   1815  N   GLN A 276     -66.592  35.058   2.696  1.00 45.34           N  
-ATOM   1816  CA  GLN A 276     -67.576  34.775   3.735  1.00 46.42           C  
-ATOM   1817  C   GLN A 276     -67.928  33.278   3.781  1.00 46.25           C  
-ATOM   1818  O   GLN A 276     -68.317  32.744   4.823  1.00 45.91           O  
-ATOM   1819  CB  GLN A 276     -68.818  35.621   3.464  1.00 46.92           C  
-ATOM   1820  CG  GLN A 276     -69.843  35.655   4.569  1.00 48.58           C  
-ATOM   1821  CD  GLN A 276     -70.678  36.919   4.505  1.00 49.83           C  
-ATOM   1822  OE1 GLN A 276     -71.037  37.390   3.422  1.00 48.55           O  
-ATOM   1823  NE2 GLN A 276     -70.994  37.476   5.666  1.00 51.93           N  
-ATOM   1824  N   VAL A 277     -67.773  32.606   2.644  1.00 46.04           N  
-ATOM   1825  CA  VAL A 277     -68.059  31.178   2.537  1.00 45.11           C  
-ATOM   1826  C   VAL A 277     -67.244  30.335   3.522  1.00 44.49           C  
-ATOM   1827  O   VAL A 277     -67.629  29.212   3.845  1.00 44.87           O  
-ATOM   1828  CB  VAL A 277     -67.777  30.656   1.103  1.00 44.30           C  
-ATOM   1829  CG1 VAL A 277     -68.534  31.496   0.094  1.00 43.76           C  
-ATOM   1830  CG2 VAL A 277     -66.281  30.681   0.814  1.00 42.82           C  
-ATOM   1831  N   VAL A 278     -66.120  30.870   3.991  1.00 42.72           N  
-ATOM   1832  CA  VAL A 278     -65.272  30.148   4.935  1.00 41.40           C  
-ATOM   1833  C   VAL A 278     -66.128  29.563   6.057  1.00 41.37           C  
-ATOM   1834  O   VAL A 278     -65.754  28.583   6.694  1.00 40.75           O  
-ATOM   1835  CB  VAL A 278     -64.183  31.083   5.547  1.00 41.01           C  
-ATOM   1836  CG1 VAL A 278     -64.829  32.104   6.462  1.00 41.46           C  
-ATOM   1837  CG2 VAL A 278     -63.143  30.273   6.311  1.00 39.46           C  
-ATOM   1838  N   PHE A 279     -67.288  30.168   6.289  1.00 42.24           N  
-ATOM   1839  CA  PHE A 279     -68.183  29.700   7.338  1.00 42.89           C  
-ATOM   1840  C   PHE A 279     -68.870  28.400   6.947  1.00 42.97           C  
-ATOM   1841  O   PHE A 279     -69.013  27.495   7.771  1.00 41.85           O  
-ATOM   1842  CB  PHE A 279     -69.210  30.790   7.678  1.00 42.80           C  
-ATOM   1843  CG  PHE A 279     -68.645  31.890   8.532  1.00 41.98           C  
-ATOM   1844  CD1 PHE A 279     -68.188  31.615   9.821  1.00 41.45           C  
-ATOM   1845  CD2 PHE A 279     -68.490  33.174   8.027  1.00 41.75           C  
-ATOM   1846  CE1 PHE A 279     -67.578  32.600  10.591  1.00 40.62           C  
-ATOM   1847  CE2 PHE A 279     -67.880  34.167   8.791  1.00 41.36           C  
-ATOM   1848  CZ  PHE A 279     -67.422  33.877  10.075  1.00 39.87           C  
-ATOM   1849  N   THR A 280     -69.292  28.312   5.690  1.00 43.37           N  
-ATOM   1850  CA  THR A 280     -69.933  27.104   5.188  1.00 43.63           C  
-ATOM   1851  C   THR A 280     -68.950  25.955   5.367  1.00 43.45           C  
-ATOM   1852  O   THR A 280     -69.273  24.923   5.959  1.00 43.06           O  
-ATOM   1853  CB  THR A 280     -70.273  27.217   3.682  1.00 43.66           C  
-ATOM   1854  OG1 THR A 280     -71.371  28.122   3.498  1.00 44.21           O  
-ATOM   1855  CG2 THR A 280     -70.638  25.854   3.113  1.00 42.59           C  
-ATOM   1856  N   ILE A 281     -67.740  26.148   4.858  1.00 43.71           N  
-ATOM   1857  CA  ILE A 281     -66.721  25.119   4.960  1.00 44.88           C  
-ATOM   1858  C   ILE A 281     -66.308  24.876   6.420  1.00 45.89           C  
-ATOM   1859  O   ILE A 281     -65.719  23.845   6.750  1.00 45.63           O  
-ATOM   1860  CB  ILE A 281     -65.505  25.448   4.012  1.00 43.29           C  
-ATOM   1861  CG1 ILE A 281     -64.182  25.337   4.751  1.00 42.80           C  
-ATOM   1862  CG2 ILE A 281     -65.675  26.816   3.388  1.00 43.11           C  
-ATOM   1863  CD1 ILE A 281     -63.017  25.675   3.873  1.00 43.63           C  
-ATOM   1864  N   LEU A 282     -66.655  25.813   7.298  1.00 47.47           N  
-ATOM   1865  CA  LEU A 282     -66.349  25.674   8.721  1.00 48.28           C  
-ATOM   1866  C   LEU A 282     -67.369  24.667   9.276  1.00 48.77           C  
-ATOM   1867  O   LEU A 282     -67.098  23.954  10.251  1.00 47.42           O  
-ATOM   1868  CB  LEU A 282     -66.495  27.028   9.437  1.00 48.86           C  
-ATOM   1869  CG  LEU A 282     -65.491  27.409  10.534  1.00 48.04           C  
-ATOM   1870  CD1 LEU A 282     -65.199  26.220  11.435  1.00 48.45           C  
-ATOM   1871  CD2 LEU A 282     -64.213  27.868   9.892  1.00 48.58           C  
-ATOM   1872  N   LEU A 283     -68.545  24.627   8.644  1.00 49.74           N  
-ATOM   1873  CA  LEU A 283     -69.612  23.702   9.029  1.00 50.39           C  
-ATOM   1874  C   LEU A 283     -69.233  22.313   8.540  1.00 51.51           C  
-ATOM   1875  O   LEU A 283     -69.253  21.351   9.309  1.00 52.28           O  
-ATOM   1876  CB  LEU A 283     -70.960  24.085   8.394  1.00 49.70           C  
-ATOM   1877  CG  LEU A 283     -71.931  25.124   8.984  1.00 48.65           C  
-ATOM   1878  CD1 LEU A 283     -71.861  25.110  10.510  1.00 47.61           C  
-ATOM   1879  CD2 LEU A 283     -71.604  26.502   8.440  1.00 49.46           C  
-ATOM   1880  N   GLN A 284     -68.891  22.214   7.255  1.00 51.83           N  
-ATOM   1881  CA  GLN A 284     -68.497  20.938   6.667  1.00 52.27           C  
-ATOM   1882  C   GLN A 284     -67.471  20.273   7.570  1.00 52.69           C  
-ATOM   1883  O   GLN A 284     -67.484  19.059   7.743  1.00 53.12           O  
-ATOM   1884  CB  GLN A 284     -67.918  21.153   5.272  1.00 51.70           C  
-ATOM   1885  CG  GLN A 284     -68.868  21.905   4.368  1.00 53.73           C  
-ATOM   1886  CD  GLN A 284     -68.371  22.021   2.943  1.00 55.25           C  
-ATOM   1887  OE1 GLN A 284     -67.190  22.292   2.698  1.00 56.11           O  
-ATOM   1888  NE2 GLN A 284     -69.278  21.835   1.988  1.00 55.31           N  
-ATOM   1889  N   GLN A 285     -66.584  21.079   8.144  1.00 53.04           N  
-ATOM   1890  CA  GLN A 285     -65.574  20.583   9.068  1.00 53.09           C  
-ATOM   1891  C   GLN A 285     -66.312  19.775  10.132  1.00 52.99           C  
-ATOM   1892  O   GLN A 285     -66.064  18.589  10.324  1.00 52.85           O  
-ATOM   1893  CB  GLN A 285     -64.867  21.759   9.741  1.00 54.85           C  
-ATOM   1894  CG  GLN A 285     -63.856  21.364  10.792  1.00 55.92           C  
-ATOM   1895  CD  GLN A 285     -62.451  21.389  10.253  1.00 58.21           C  
-ATOM   1896  OE1 GLN A 285     -61.910  22.459   9.973  1.00 57.87           O  
-ATOM   1897  NE2 GLN A 285     -61.848  20.209  10.090  1.00 60.01           N  
-ATOM   1898  N   TYR A 286     -67.229  20.447  10.816  1.00 53.47           N  
-ATOM   1899  CA  TYR A 286     -68.039  19.853  11.871  1.00 54.09           C  
-ATOM   1900  C   TYR A 286     -68.869  18.688  11.350  1.00 55.29           C  
-ATOM   1901  O   TYR A 286     -68.884  17.602  11.934  1.00 55.67           O  
-ATOM   1902  CB  TYR A 286     -68.971  20.920  12.443  1.00 53.21           C  
-ATOM   1903  CG  TYR A 286     -70.112  20.378  13.267  1.00 50.79           C  
-ATOM   1904  CD1 TYR A 286     -69.927  20.045  14.606  1.00 49.87           C  
-ATOM   1905  CD2 TYR A 286     -71.373  20.170  12.694  1.00 48.92           C  
-ATOM   1906  CE1 TYR A 286     -70.963  19.518  15.361  1.00 50.18           C  
-ATOM   1907  CE2 TYR A 286     -72.417  19.642  13.434  1.00 48.69           C  
-ATOM   1908  CZ  TYR A 286     -72.207  19.316  14.772  1.00 49.99           C  
-ATOM   1909  OH  TYR A 286     -73.230  18.788  15.530  1.00 49.00           O  
-ATOM   1910  N   GLU A 287     -69.577  18.944  10.256  1.00 56.74           N  
-ATOM   1911  CA  GLU A 287     -70.433  17.956   9.614  1.00 58.04           C  
-ATOM   1912  C   GLU A 287     -69.660  16.671   9.324  1.00 56.59           C  
-ATOM   1913  O   GLU A 287     -70.177  15.570   9.487  1.00 54.35           O  
-ATOM   1914  CB  GLU A 287     -70.989  18.549   8.315  1.00 61.97           C  
-ATOM   1915  CG  GLU A 287     -72.016  17.685   7.626  1.00 69.16           C  
-ATOM   1916  CD  GLU A 287     -73.085  17.202   8.587  1.00 74.43           C  
-ATOM   1917  OE1 GLU A 287     -73.657  18.047   9.318  1.00 77.14           O  
-ATOM   1918  OE2 GLU A 287     -73.353  15.978   8.611  1.00 76.63           O  
-ATOM   1919  N   ASN A 288     -68.411  16.834   8.899  1.00 56.89           N  
-ATOM   1920  CA  ASN A 288     -67.534  15.720   8.573  1.00 56.76           C  
-ATOM   1921  C   ASN A 288     -67.018  15.008   9.811  1.00 57.07           C  
-ATOM   1922  O   ASN A 288     -66.914  13.789   9.825  1.00 58.23           O  
-ATOM   1923  CB  ASN A 288     -66.365  16.217   7.713  1.00 56.83           C  
-ATOM   1924  CG  ASN A 288     -65.178  15.269   7.719  1.00 57.65           C  
-ATOM   1925  OD1 ASN A 288     -64.344  15.308   8.629  1.00 58.55           O  
-ATOM   1926  ND2 ASN A 288     -65.096  14.410   6.703  1.00 55.61           N  
-ATOM   1927  N   ASN A 289     -66.688  15.752  10.855  1.00 57.74           N  
-ATOM   1928  CA  ASN A 289     -66.204  15.107  12.061  1.00 59.20           C  
-ATOM   1929  C   ASN A 289     -67.342  14.329  12.691  1.00 59.82           C  
-ATOM   1930  O   ASN A 289     -67.119  13.365  13.418  1.00 60.17           O  
-ATOM   1931  CB  ASN A 289     -65.655  16.141  13.031  1.00 60.85           C  
-ATOM   1932  CG  ASN A 289     -64.506  16.917  12.439  1.00 62.95           C  
-ATOM   1933  OD1 ASN A 289     -63.557  16.329  11.911  1.00 64.29           O  
-ATOM   1934  ND2 ASN A 289     -64.579  18.244  12.514  1.00 63.63           N  
-ATOM   1935  N   GLU A 290     -68.568  14.750  12.405  1.00 60.99           N  
-ATOM   1936  CA  GLU A 290     -69.742  14.061  12.921  1.00 62.48           C  
-ATOM   1937  C   GLU A 290     -69.799  12.700  12.255  1.00 62.69           C  
-ATOM   1938  O   GLU A 290     -69.966  11.680  12.920  1.00 62.87           O  
-ATOM   1939  CB  GLU A 290     -71.005  14.848  12.594  1.00 64.34           C  
-ATOM   1940  CG  GLU A 290     -71.340  15.905  13.614  1.00 66.88           C  
-ATOM   1941  CD  GLU A 290     -71.587  15.308  14.986  1.00 68.83           C  
-ATOM   1942  OE1 GLU A 290     -70.603  14.985  15.693  1.00 69.74           O  
-ATOM   1943  OE2 GLU A 290     -72.773  15.149  15.350  1.00 69.40           O  
-ATOM   1944  N   GLN A 291     -69.660  12.713  10.930  1.00 63.30           N  
-ATOM   1945  CA  GLN A 291     -69.650  11.514  10.094  1.00 62.99           C  
-ATOM   1946  C   GLN A 291     -68.597  10.583  10.681  1.00 61.80           C  
-ATOM   1947  O   GLN A 291     -68.898   9.493  11.156  1.00 61.54           O  
-ATOM   1948  CB  GLN A 291     -69.245  11.890   8.661  1.00 65.43           C  
-ATOM   1949  CG  GLN A 291     -69.446  10.812   7.610  1.00 69.19           C  
-ATOM   1950  CD  GLN A 291     -70.893  10.716   7.156  1.00 72.39           C  
-ATOM   1951  OE1 GLN A 291     -71.401  11.618   6.478  1.00 73.36           O  
-ATOM   1952  NE2 GLN A 291     -71.571   9.627   7.536  1.00 72.37           N  
-ATOM   1953  N   SER A 292     -67.355  11.044  10.649  1.00 61.35           N  
-ATOM   1954  CA  SER A 292     -66.227  10.292  11.167  1.00 61.93           C  
-ATOM   1955  C   SER A 292     -66.509   9.585  12.479  1.00 63.22           C  
-ATOM   1956  O   SER A 292     -65.900   8.564  12.782  1.00 64.35           O  
-ATOM   1957  CB  SER A 292     -65.030  11.217  11.353  1.00 61.24           C  
-ATOM   1958  OG  SER A 292     -63.993  10.559  12.055  1.00 60.71           O  
-ATOM   1959  N   GLN A 293     -67.425  10.115  13.274  1.00 64.86           N  
-ATOM   1960  CA  GLN A 293     -67.707   9.470  14.542  1.00 66.76           C  
-ATOM   1961  C   GLN A 293     -68.776   8.401  14.386  1.00 66.43           C  
-ATOM   1962  O   GLN A 293     -68.694   7.351  15.009  1.00 67.28           O  
-ATOM   1963  CB  GLN A 293     -68.124  10.504  15.585  1.00 69.46           C  
-ATOM   1964  CG  GLN A 293     -67.699  10.134  17.000  1.00 73.35           C  
-ATOM   1965  CD  GLN A 293     -67.915  11.267  17.990  1.00 76.46           C  
-ATOM   1966  OE1 GLN A 293     -69.053  11.673  18.256  1.00 78.03           O  
-ATOM   1967  NE2 GLN A 293     -66.817  11.790  18.538  1.00 77.11           N  
-ATOM   1968  N   GLN A 294     -69.775   8.663  13.550  1.00 65.94           N  
-ATOM   1969  CA  GLN A 294     -70.834   7.691  13.325  1.00 66.19           C  
-ATOM   1970  C   GLN A 294     -70.234   6.463  12.661  1.00 65.63           C  
-ATOM   1971  O   GLN A 294     -70.574   5.335  13.003  1.00 65.91           O  
-ATOM   1972  CB  GLN A 294     -71.908   8.279  12.423  1.00 68.14           C  
-ATOM   1973  CG  GLN A 294     -72.469   9.588  12.924  1.00 72.42           C  
-ATOM   1974  CD  GLN A 294     -73.348  10.267  11.895  1.00 75.46           C  
-ATOM   1975  OE1 GLN A 294     -73.768  11.416  12.077  1.00 77.07           O  
-ATOM   1976  NE2 GLN A 294     -73.633   9.561  10.801  1.00 76.35           N  
-ATOM   1977  N   LEU A 295     -69.342   6.689  11.703  1.00 65.08           N  
-ATOM   1978  CA  LEU A 295     -68.688   5.596  11.002  1.00 64.54           C  
-ATOM   1979  C   LEU A 295     -67.971   4.681  11.982  1.00 65.67           C  
-ATOM   1980  O   LEU A 295     -68.052   3.460  11.872  1.00 66.96           O  
-ATOM   1981  CB  LEU A 295     -67.687   6.138   9.982  1.00 62.25           C  
-ATOM   1982  CG  LEU A 295     -68.196   6.278   8.548  1.00 60.81           C  
-ATOM   1983  CD1 LEU A 295     -69.528   7.007   8.521  1.00 60.93           C  
-ATOM   1984  CD2 LEU A 295     -67.156   7.008   7.726  1.00 60.12           C  
-ATOM   1985  N   MET A 296     -67.274   5.275  12.943  1.00 66.54           N  
-ATOM   1986  CA  MET A 296     -66.540   4.512  13.947  1.00 67.69           C  
-ATOM   1987  C   MET A 296     -67.487   3.597  14.722  1.00 67.28           C  
-ATOM   1988  O   MET A 296     -67.178   2.432  14.978  1.00 66.75           O  
-ATOM   1989  CB  MET A 296     -65.868   5.467  14.925  1.00 70.65           C  
-ATOM   1990  CG  MET A 296     -64.555   4.973  15.498  1.00 74.39           C  
-ATOM   1991  SD  MET A 296     -63.170   5.472  14.443  1.00 80.85           S  
-ATOM   1992  CE  MET A 296     -63.406   7.264  14.378  1.00 76.54           C  
-ATOM   1993  N   GLN A 297     -68.640   4.142  15.098  1.00 67.00           N  
-ATOM   1994  CA  GLN A 297     -69.646   3.400  15.850  1.00 66.98           C  
-ATOM   1995  C   GLN A 297     -70.222   2.295  14.970  1.00 66.14           C  
-ATOM   1996  O   GLN A 297     -70.689   1.262  15.462  1.00 66.23           O  
-ATOM   1997  CB  GLN A 297     -70.760   4.351  16.307  1.00 68.37           C  
-ATOM   1998  CG  GLN A 297     -71.697   3.771  17.356  1.00 71.00           C  
-ATOM   1999  CD  GLN A 297     -70.958   3.325  18.607  1.00 72.61           C  
-ATOM   2000  OE1 GLN A 297     -70.241   4.110  19.230  1.00 73.52           O  
-ATOM   2001  NE2 GLN A 297     -71.128   2.060  18.979  1.00 72.77           N  
-ATOM   2002  N   LYS A 298     -70.185   2.530  13.661  1.00 65.11           N  
-ATOM   2003  CA  LYS A 298     -70.682   1.569  12.686  1.00 62.47           C  
-ATOM   2004  C   LYS A 298     -69.681   0.425  12.626  1.00 59.78           C  
-ATOM   2005  O   LYS A 298     -70.067  -0.736  12.637  1.00 59.00           O  
-ATOM   2006  CB  LYS A 298     -70.813   2.231  11.311  1.00 63.64           C  
-ATOM   2007  CG  LYS A 298     -71.720   1.490  10.337  1.00 65.92           C  
-ATOM   2008  CD  LYS A 298     -73.126   1.317  10.912  1.00 68.48           C  
-ATOM   2009  CE  LYS A 298     -73.754   2.661  11.298  1.00 69.70           C  
-ATOM   2010  NZ  LYS A 298     -75.132   2.513  11.861  1.00 69.67           N  
-ATOM   2011  N   THR A 299     -68.395   0.761  12.579  1.00 57.25           N  
-ATOM   2012  CA  THR A 299     -67.348  -0.247  12.531  1.00 56.79           C  
-ATOM   2013  C   THR A 299     -67.575  -1.318  13.589  1.00 58.70           C  
-ATOM   2014  O   THR A 299     -67.408  -2.509  13.325  1.00 60.31           O  
-ATOM   2015  CB  THR A 299     -65.954   0.359  12.767  1.00 54.83           C  
-ATOM   2016  OG1 THR A 299     -65.613   1.217  11.680  1.00 55.82           O  
-ATOM   2017  CG2 THR A 299     -64.909  -0.724  12.858  1.00 53.53           C  
-ATOM   2018  N   LEU A 300     -67.962  -0.905  14.790  1.00 59.51           N  
-ATOM   2019  CA  LEU A 300     -68.178  -1.874  15.856  1.00 59.35           C  
-ATOM   2020  C   LEU A 300     -69.343  -2.797  15.562  1.00 59.25           C  
-ATOM   2021  O   LEU A 300     -69.236  -4.004  15.744  1.00 59.95           O  
-ATOM   2022  CB  LEU A 300     -68.390  -1.166  17.192  1.00 58.92           C  
-ATOM   2023  CG  LEU A 300     -67.253  -0.215  17.578  1.00 59.00           C  
-ATOM   2024  CD1 LEU A 300     -67.466   0.228  19.012  1.00 59.68           C  
-ATOM   2025  CD2 LEU A 300     -65.892  -0.894  17.417  1.00 57.51           C  
-ATOM   2026  N   GLU A 301     -70.458  -2.243  15.108  1.00 60.11           N  
-ATOM   2027  CA  GLU A 301     -71.611  -3.077  14.794  1.00 61.67           C  
-ATOM   2028  C   GLU A 301     -71.282  -4.068  13.678  1.00 60.41           C  
-ATOM   2029  O   GLU A 301     -71.739  -5.210  13.695  1.00 61.07           O  
-ATOM   2030  CB  GLU A 301     -72.796  -2.217  14.361  1.00 64.82           C  
-ATOM   2031  CG  GLU A 301     -73.579  -1.578  15.489  1.00 69.86           C  
-ATOM   2032  CD  GLU A 301     -74.667  -0.651  14.962  1.00 73.70           C  
-ATOM   2033  OE1 GLU A 301     -75.607  -0.319  15.723  1.00 75.52           O  
-ATOM   2034  OE2 GLU A 301     -74.575  -0.244  13.780  1.00 76.02           O  
-ATOM   2035  N   LEU A 302     -70.485  -3.627  12.709  1.00 58.38           N  
-ATOM   2036  CA  LEU A 302     -70.120  -4.478  11.585  1.00 55.49           C  
-ATOM   2037  C   LEU A 302     -69.187  -5.597  11.993  1.00 55.34           C  
-ATOM   2038  O   LEU A 302     -69.335  -6.719  11.521  1.00 56.46           O  
-ATOM   2039  CB  LEU A 302     -69.476  -3.655  10.469  1.00 52.47           C  
-ATOM   2040  CG  LEU A 302     -70.333  -2.519   9.916  1.00 48.76           C  
-ATOM   2041  CD1 LEU A 302     -69.633  -1.928   8.716  1.00 46.34           C  
-ATOM   2042  CD2 LEU A 302     -71.718  -3.028   9.551  1.00 45.90           C  
-ATOM   2043  N   PHE A 303     -68.220  -5.300  12.855  1.00 54.86           N  
-ATOM   2044  CA  PHE A 303     -67.302  -6.337  13.307  1.00 54.79           C  
-ATOM   2045  C   PHE A 303     -68.024  -7.309  14.211  1.00 55.36           C  
-ATOM   2046  O   PHE A 303     -67.721  -8.498  14.232  1.00 55.18           O  
-ATOM   2047  CB  PHE A 303     -66.114  -5.737  14.039  1.00 53.14           C  
-ATOM   2048  CG  PHE A 303     -64.926  -5.557  13.170  1.00 52.36           C  
-ATOM   2049  CD1 PHE A 303     -64.427  -4.292  12.903  1.00 52.65           C  
-ATOM   2050  CD2 PHE A 303     -64.316  -6.659  12.593  1.00 52.82           C  
-ATOM   2051  CE1 PHE A 303     -63.329  -4.121  12.066  1.00 53.71           C  
-ATOM   2052  CE2 PHE A 303     -63.220  -6.508  11.755  1.00 54.30           C  
-ATOM   2053  CZ  PHE A 303     -62.722  -5.233  11.489  1.00 55.19           C  
-ATOM   2054  N   SER A 304     -68.989  -6.795  14.958  1.00 57.18           N  
-ATOM   2055  CA  SER A 304     -69.776  -7.631  15.845  1.00 59.67           C  
-ATOM   2056  C   SER A 304     -70.573  -8.574  14.943  1.00 60.17           C  
-ATOM   2057  O   SER A 304     -70.552  -9.793  15.118  1.00 60.87           O  
-ATOM   2058  CB  SER A 304     -70.723  -6.764  16.687  1.00 60.20           C  
-ATOM   2059  OG  SER A 304     -71.353  -7.516  17.714  1.00 61.71           O  
-ATOM   2060  N   GLU A 305     -71.256  -7.997  13.961  1.00 60.73           N  
-ATOM   2061  CA  GLU A 305     -72.059  -8.768  13.023  1.00 61.36           C  
-ATOM   2062  C   GLU A 305     -71.211  -9.797  12.268  1.00 60.47           C  
-ATOM   2063  O   GLU A 305     -71.655 -10.924  12.039  1.00 59.69           O  
-ATOM   2064  CB  GLU A 305     -72.742  -7.819  12.034  1.00 63.52           C  
-ATOM   2065  CG  GLU A 305     -73.696  -8.504  11.072  1.00 67.27           C  
-ATOM   2066  CD  GLU A 305     -74.830  -9.217  11.785  1.00 69.11           C  
-ATOM   2067  OE1 GLU A 305     -75.650  -8.528  12.438  1.00 69.58           O  
-ATOM   2068  OE2 GLU A 305     -74.892 -10.466  11.692  1.00 69.47           O  
-ATOM   2069  N   LEU A 306     -69.995  -9.404  11.883  1.00 59.81           N  
-ATOM   2070  CA  LEU A 306     -69.090 -10.296  11.160  1.00 58.70           C  
-ATOM   2071  C   LEU A 306     -68.809 -11.537  11.977  1.00 59.97           C  
-ATOM   2072  O   LEU A 306     -68.958 -12.644  11.473  1.00 61.46           O  
-ATOM   2073  CB  LEU A 306     -67.756  -9.612  10.839  1.00 55.99           C  
-ATOM   2074  CG  LEU A 306     -66.641 -10.579  10.413  1.00 53.34           C  
-ATOM   2075  CD1 LEU A 306     -67.030 -11.275   9.129  1.00 53.73           C  
-ATOM   2076  CD2 LEU A 306     -65.344  -9.838  10.222  1.00 51.36           C  
-ATOM   2077  N   ASN A 307     -68.396 -11.356  13.232  1.00 60.74           N  
-ATOM   2078  CA  ASN A 307     -68.098 -12.498  14.090  1.00 61.80           C  
-ATOM   2079  C   ASN A 307     -69.349 -13.272  14.487  1.00 62.04           C  
-ATOM   2080  O   ASN A 307     -69.329 -14.499  14.560  1.00 62.20           O  
-ATOM   2081  CB  ASN A 307     -67.317 -12.060  15.331  1.00 62.20           C  
-ATOM   2082  CG  ASN A 307     -65.893 -11.650  14.998  1.00 64.07           C  
-ATOM   2083  OD1 ASN A 307     -65.638 -10.508  14.608  1.00 64.76           O  
-ATOM   2084  ND2 ASN A 307     -64.956 -12.590  15.125  1.00 64.34           N  
-ATOM   2085  N   SER A 308     -70.445 -12.564  14.731  1.00 62.43           N  
-ATOM   2086  CA  SER A 308     -71.692 -13.235  15.080  1.00 63.18           C  
-ATOM   2087  C   SER A 308     -72.027 -14.197  13.939  1.00 63.14           C  
-ATOM   2088  O   SER A 308     -72.964 -14.990  14.029  1.00 64.57           O  
-ATOM   2089  CB  SER A 308     -72.823 -12.212  15.245  1.00 64.54           C  
-ATOM   2090  OG  SER A 308     -74.059 -12.845  15.546  1.00 65.81           O  
-ATOM   2091  N   THR A 309     -71.254 -14.109  12.861  1.00 61.82           N  
-ATOM   2092  CA  THR A 309     -71.445 -14.961  11.699  1.00 60.14           C  
-ATOM   2093  C   THR A 309     -70.269 -15.922  11.544  1.00 60.78           C  
-ATOM   2094  O   THR A 309     -70.455 -17.047  11.100  1.00 60.51           O  
-ATOM   2095  CB  THR A 309     -71.641 -14.109  10.409  1.00 58.34           C  
-ATOM   2096  OG1 THR A 309     -72.983 -13.605  10.377  1.00 55.31           O  
-ATOM   2097  CG2 THR A 309     -71.387 -14.930   9.156  1.00 56.65           C  
-ATOM   2098  N   VAL A 310     -69.062 -15.496  11.911  1.00 62.41           N  
-ATOM   2099  CA  VAL A 310     -67.915 -16.395  11.798  1.00 65.07           C  
-ATOM   2100  C   VAL A 310     -68.123 -17.505  12.818  1.00 66.74           C  
-ATOM   2101  O   VAL A 310     -67.595 -18.604  12.661  1.00 67.14           O  
-ATOM   2102  CB  VAL A 310     -66.539 -15.700  12.087  1.00 65.11           C  
-ATOM   2103  CG1 VAL A 310     -66.404 -14.430  11.264  1.00 65.84           C  
-ATOM   2104  CG2 VAL A 310     -66.382 -15.411  13.570  1.00 65.42           C  
-ATOM   2105  N   ASN A 311     -68.899 -17.206  13.863  1.00 68.67           N  
-ATOM   2106  CA  ASN A 311     -69.195 -18.184  14.908  1.00 69.16           C  
-ATOM   2107  C   ASN A 311     -70.221 -19.175  14.367  1.00 70.18           C  
-ATOM   2108  O   ASN A 311     -69.944 -20.369  14.313  1.00 70.61           O  
-ATOM   2109  CB  ASN A 311     -69.724 -17.503  16.185  1.00 68.34           C  
-ATOM   2110  CG  ASN A 311     -68.628 -16.749  16.964  1.00 67.83           C  
-ATOM   2111  OD1 ASN A 311     -67.455 -17.136  16.958  1.00 66.62           O  
-ATOM   2112  ND2 ASN A 311     -69.023 -15.684  17.656  1.00 67.15           N  
-ATOM   2113  N   LYS A 312     -71.392 -18.688  13.952  1.00 71.42           N  
-ATOM   2114  CA  LYS A 312     -72.423 -19.565  13.389  1.00 73.38           C  
-ATOM   2115  C   LYS A 312     -71.811 -20.448  12.309  1.00 75.41           C  
-ATOM   2116  O   LYS A 312     -72.365 -21.484  11.932  1.00 75.63           O  
-ATOM   2117  CB  LYS A 312     -73.550 -18.745  12.765  1.00 72.95           C  
-ATOM   2118  CG  LYS A 312     -74.515 -18.163  13.768  1.00 75.63           C  
-ATOM   2119  CD  LYS A 312     -75.922 -18.722  13.573  1.00 77.99           C  
-ATOM   2120  CE  LYS A 312     -76.572 -18.188  12.303  1.00 78.62           C  
-ATOM   2121  NZ  LYS A 312     -76.739 -16.706  12.369  1.00 79.26           N  
-ATOM   2122  N   LEU A 313     -70.653 -20.019  11.819  1.00 77.45           N  
-ATOM   2123  CA  LEU A 313     -69.938 -20.727  10.774  1.00 78.81           C  
-ATOM   2124  C   LEU A 313     -68.966 -21.745  11.352  1.00 80.98           C  
-ATOM   2125  O   LEU A 313     -68.754 -22.793  10.747  1.00 81.95           O  
-ATOM   2126  CB  LEU A 313     -69.170 -19.731   9.904  1.00 77.53           C  
-ATOM   2127  CG  LEU A 313     -68.772 -20.206   8.512  1.00 76.16           C  
-ATOM   2128  CD1 LEU A 313     -70.020 -20.381   7.669  1.00 75.64           C  
-ATOM   2129  CD2 LEU A 313     -67.846 -19.193   7.877  1.00 75.87           C  
-ATOM   2130  N   VAL A 314     -68.371 -21.443  12.508  1.00 83.20           N  
-ATOM   2131  CA  VAL A 314     -67.422 -22.373  13.130  1.00 85.21           C  
-ATOM   2132  C   VAL A 314     -68.140 -23.677  13.447  1.00 87.07           C  
-ATOM   2133  O   VAL A 314     -67.506 -24.688  13.748  1.00 88.11           O  
-ATOM   2134  CB  VAL A 314     -66.778 -21.801  14.422  1.00 84.71           C  
-ATOM   2135  CG1 VAL A 314     -65.806 -22.807  15.013  1.00 83.61           C  
-ATOM   2136  CG2 VAL A 314     -66.021 -20.529  14.104  1.00 85.31           C  
-ATOM   2137  N   ASP A 315     -69.468 -23.644  13.394  1.00 88.65           N  
-ATOM   2138  CA  ASP A 315     -70.259 -24.847  13.596  1.00 90.18           C  
-ATOM   2139  C   ASP A 315     -70.371 -25.372  12.168  1.00 92.55           C  
-ATOM   2140  O   ASP A 315     -69.561 -24.996  11.325  1.00 93.27           O  
-ATOM   2141  CB  ASP A 315     -71.627 -24.501  14.178  1.00 88.30           C  
-ATOM   2142  CG  ASP A 315     -71.526 -23.908  15.574  1.00 86.96           C  
-ATOM   2143  OD1 ASP A 315     -70.806 -24.484  16.418  1.00 85.40           O  
-ATOM   2144  OD2 ASP A 315     -72.171 -22.871  15.831  1.00 86.32           O  
-ATOM   2145  N   ASP A 316     -71.342 -26.222  11.862  1.00 95.34           N  
-ATOM   2146  CA  ASP A 316     -71.439 -26.729  10.489  1.00 98.68           C  
-ATOM   2147  C   ASP A 316     -70.208 -27.553  10.109  1.00100.64           C  
-ATOM   2148  O   ASP A 316     -70.251 -28.369   9.181  1.00100.92           O  
-ATOM   2149  CB  ASP A 316     -71.601 -25.569   9.506  1.00 97.93           C  
-ATOM   2150  CG  ASP A 316     -72.976 -24.967   9.558  1.00 98.19           C  
-ATOM   2151  OD1 ASP A 316     -73.830 -25.381   8.744  1.00 97.38           O  
-ATOM   2152  OD2 ASP A 316     -73.204 -24.095  10.425  1.00 98.73           O  
-ATOM   2153  N   SER A 317     -69.102 -27.310  10.807  1.00102.32           N  
-ATOM   2154  CA  SER A 317     -67.881 -28.067  10.589  1.00103.89           C  
-ATOM   2155  C   SER A 317     -67.889 -29.051  11.759  1.00105.07           C  
-ATOM   2156  O   SER A 317     -66.951 -29.828  11.951  1.00105.58           O  
-ATOM   2157  CB  SER A 317     -66.653 -27.159  10.645  1.00103.59           C  
-ATOM   2158  OG  SER A 317     -66.522 -26.556  11.917  1.00104.76           O  
-ATOM   2159  N   ASN A 318     -68.975 -28.980  12.537  1.00106.98           N  
-ATOM   2160  CA  ASN A 318     -69.229 -29.850  13.691  1.00108.08           C  
-ATOM   2161  C   ASN A 318     -70.432 -30.730  13.341  1.00108.89           C  
-ATOM   2162  O   ASN A 318     -71.124 -31.240  14.223  1.00108.76           O  
-ATOM   2163  CB  ASN A 318     -69.574 -29.038  14.952  1.00108.48           C  
-ATOM   2164  CG  ASN A 318     -68.417 -28.183  15.446  1.00108.95           C  
-ATOM   2165  OD1 ASN A 318     -67.247 -28.493  15.208  1.00108.90           O  
-ATOM   2166  ND2 ASN A 318     -68.742 -27.109  16.161  1.00108.83           N  
-ATOM   2167  N   LYS A 319     -70.679 -30.882  12.042  1.00109.32           N  
-ATOM   2168  CA  LYS A 319     -71.790 -31.689  11.542  1.00109.78           C  
-ATOM   2169  C   LYS A 319     -71.280 -32.713  10.521  1.00110.21           C  
-ATOM   2170  O   LYS A 319     -70.534 -32.304   9.600  1.00109.88           O  
-ATOM   2171  CB  LYS A 319     -72.841 -30.787  10.876  1.00108.72           C  
-ATOM   2172  CG  LYS A 319     -73.354 -29.651  11.748  1.00107.52           C  
-ATOM   2173  CD  LYS A 319     -74.074 -30.171  12.976  1.00107.06           C  
-ATOM   2174  CE  LYS A 319     -74.603 -29.029  13.823  1.00106.49           C  
-ATOM   2175  NZ  LYS A 319     -75.302 -29.525  15.039  1.00105.63           N  
-TER    2176      LYS A 319                                                      
-ATOM   2177  N   ASP B  30     -49.178  63.117 -18.457  1.00 53.46           N  
-ATOM   2178  CA  ASP B  30     -48.542  63.511 -17.168  1.00 53.55           C  
-ATOM   2179  C   ASP B  30     -47.830  62.352 -16.496  1.00 53.62           C  
-ATOM   2180  O   ASP B  30     -48.342  61.233 -16.445  1.00 53.83           O  
-ATOM   2181  CB  ASP B  30     -49.580  64.089 -16.216  1.00 54.28           C  
-ATOM   2182  CG  ASP B  30     -50.184  65.366 -16.739  1.00 56.81           C  
-ATOM   2183  OD1 ASP B  30     -49.418  66.209 -17.258  1.00 59.07           O  
-ATOM   2184  OD2 ASP B  30     -51.416  65.536 -16.631  1.00 58.65           O  
-ATOM   2185  N   GLU B  31     -46.641  62.636 -15.975  1.00 53.42           N  
-ATOM   2186  CA  GLU B  31     -45.826  61.628 -15.316  1.00 52.61           C  
-ATOM   2187  C   GLU B  31     -46.549  61.094 -14.095  1.00 52.12           C  
-ATOM   2188  O   GLU B  31     -47.221  61.838 -13.376  1.00 52.04           O  
-ATOM   2189  CB  GLU B  31     -44.473  62.215 -14.907  1.00 51.83           C  
-ATOM   2190  CG  GLU B  31     -43.740  62.913 -16.034  1.00 53.43           C  
-ATOM   2191  CD  GLU B  31     -44.192  64.359 -16.243  1.00 55.80           C  
-ATOM   2192  OE1 GLU B  31     -45.413  64.631 -16.281  1.00 56.06           O  
-ATOM   2193  OE2 GLU B  31     -43.313  65.235 -16.381  1.00 57.68           O  
-ATOM   2194  N   LYS B  32     -46.412  59.796 -13.868  1.00 51.03           N  
-ATOM   2195  CA  LYS B  32     -47.056  59.171 -12.735  1.00 50.38           C  
-ATOM   2196  C   LYS B  32     -46.069  58.933 -11.604  1.00 49.58           C  
-ATOM   2197  O   LYS B  32     -45.106  58.184 -11.749  1.00 49.21           O  
-ATOM   2198  CB  LYS B  32     -47.718  57.858 -13.172  1.00 51.37           C  
-ATOM   2199  CG  LYS B  32     -48.760  58.065 -14.280  1.00 52.26           C  
-ATOM   2200  CD  LYS B  32     -49.812  56.964 -14.334  1.00 51.82           C  
-ATOM   2201  CE  LYS B  32     -49.186  55.596 -14.536  1.00 53.46           C  
-ATOM   2202  NZ  LYS B  32     -50.222  54.535 -14.721  1.00 54.16           N  
-ATOM   2203  N   ILE B  33     -46.320  59.593 -10.478  1.00 49.20           N  
-ATOM   2204  CA  ILE B  33     -45.482  59.471  -9.290  1.00 48.45           C  
-ATOM   2205  C   ILE B  33     -46.309  58.824  -8.178  1.00 47.90           C  
-ATOM   2206  O   ILE B  33     -47.372  59.320  -7.799  1.00 48.57           O  
-ATOM   2207  CB  ILE B  33     -44.987  60.847  -8.849  1.00 48.14           C  
-ATOM   2208  CG1 ILE B  33     -44.279  61.523 -10.031  1.00 48.39           C  
-ATOM   2209  CG2 ILE B  33     -44.070  60.703  -7.649  1.00 47.37           C  
-ATOM   2210  CD1 ILE B  33     -44.003  62.998  -9.843  1.00 48.45           C  
-ATOM   2211  N   CYS B  34     -45.808  57.712  -7.662  1.00 46.48           N  
-ATOM   2212  CA  CYS B  34     -46.500  56.949  -6.634  1.00 45.57           C  
-ATOM   2213  C   CYS B  34     -45.729  57.029  -5.325  1.00 43.76           C  
-ATOM   2214  O   CYS B  34     -44.670  56.408  -5.188  1.00 43.68           O  
-ATOM   2215  CB  CYS B  34     -46.585  55.501  -7.114  1.00 49.56           C  
-ATOM   2216  SG  CYS B  34     -47.708  54.319  -6.294  1.00 55.79           S  
-ATOM   2217  N   ALA B  35     -46.254  57.794  -4.369  1.00 41.20           N  
-ATOM   2218  CA  ALA B  35     -45.603  57.950  -3.063  1.00 39.15           C  
-ATOM   2219  C   ALA B  35     -46.032  56.831  -2.110  1.00 37.76           C  
-ATOM   2220  O   ALA B  35     -47.118  56.290  -2.249  1.00 39.38           O  
-ATOM   2221  CB  ALA B  35     -45.951  59.301  -2.473  1.00 37.46           C  
-ATOM   2222  N   ILE B  36     -45.184  56.484  -1.148  1.00 35.43           N  
-ATOM   2223  CA  ILE B  36     -45.499  55.421  -0.196  1.00 34.25           C  
-ATOM   2224  C   ILE B  36     -44.994  55.751   1.202  1.00 34.43           C  
-ATOM   2225  O   ILE B  36     -43.781  55.843   1.435  1.00 35.04           O  
-ATOM   2226  CB  ILE B  36     -44.881  54.087  -0.649  1.00 34.56           C  
-ATOM   2227  CG1 ILE B  36     -45.670  53.555  -1.848  1.00 35.03           C  
-ATOM   2228  CG2 ILE B  36     -44.843  53.087   0.513  1.00 32.96           C  
-ATOM   2229  CD1 ILE B  36     -45.141  52.251  -2.415  1.00 36.42           C  
-ATOM   2230  N   TYR B  37     -45.928  55.909   2.138  1.00 32.84           N  
-ATOM   2231  CA  TYR B  37     -45.585  56.250   3.517  1.00 30.36           C  
-ATOM   2232  C   TYR B  37     -45.615  55.049   4.452  1.00 29.30           C  
-ATOM   2233  O   TYR B  37     -46.158  54.001   4.118  1.00 29.88           O  
-ATOM   2234  CB  TYR B  37     -46.582  57.257   4.065  1.00 29.36           C  
-ATOM   2235  CG  TYR B  37     -46.872  58.445   3.192  1.00 29.04           C  
-ATOM   2236  CD1 TYR B  37     -48.033  59.196   3.398  1.00 30.16           C  
-ATOM   2237  CD2 TYR B  37     -45.999  58.840   2.182  1.00 26.99           C  
-ATOM   2238  CE1 TYR B  37     -48.323  60.312   2.620  1.00 29.48           C  
-ATOM   2239  CE2 TYR B  37     -46.278  59.958   1.395  1.00 27.78           C  
-ATOM   2240  CZ  TYR B  37     -47.445  60.687   1.623  1.00 29.08           C  
-ATOM   2241  OH  TYR B  37     -47.750  61.790   0.863  1.00 30.33           O  
-ATOM   2242  N   PRO B  38     -45.031  55.193   5.648  1.00 29.12           N  
-ATOM   2243  CA  PRO B  38     -45.026  54.098   6.623  1.00 29.69           C  
-ATOM   2244  C   PRO B  38     -46.465  54.021   7.144  1.00 30.57           C  
-ATOM   2245  O   PRO B  38     -46.991  52.942   7.438  1.00 31.22           O  
-ATOM   2246  CB  PRO B  38     -44.078  54.594   7.708  1.00 28.16           C  
-ATOM   2247  CG  PRO B  38     -43.256  55.627   7.024  1.00 28.61           C  
-ATOM   2248  CD  PRO B  38     -44.219  56.319   6.128  1.00 28.50           C  
-ATOM   2249  N   HIS B  39     -47.080  55.201   7.252  1.00 30.02           N  
-ATOM   2250  CA  HIS B  39     -48.461  55.364   7.710  1.00 28.67           C  
-ATOM   2251  C   HIS B  39     -48.884  56.802   7.423  1.00 28.14           C  
-ATOM   2252  O   HIS B  39     -48.121  57.579   6.844  1.00 28.45           O  
-ATOM   2253  CB  HIS B  39     -48.557  55.153   9.213  1.00 27.81           C  
-ATOM   2254  CG  HIS B  39     -47.945  56.262  10.006  1.00 25.76           C  
-ATOM   2255  ND1 HIS B  39     -46.677  56.185  10.533  1.00 26.33           N  
-ATOM   2256  CD2 HIS B  39     -48.407  57.496  10.314  1.00 26.11           C  
-ATOM   2257  CE1 HIS B  39     -46.383  57.325  11.133  1.00 26.69           C  
-ATOM   2258  NE2 HIS B  39     -47.417  58.138  11.012  1.00 26.64           N  
-ATOM   2259  N   LEU B  40     -50.095  57.158   7.837  1.00 26.33           N  
-ATOM   2260  CA  LEU B  40     -50.572  58.524   7.664  1.00 24.54           C  
-ATOM   2261  C   LEU B  40     -51.560  58.828   8.789  1.00 24.89           C  
-ATOM   2262  O   LEU B  40     -52.661  59.317   8.557  1.00 24.82           O  
-ATOM   2263  CB  LEU B  40     -51.198  58.698   6.273  1.00 21.99           C  
-ATOM   2264  CG  LEU B  40     -51.834  60.036   5.859  1.00 22.36           C  
-ATOM   2265  CD1 LEU B  40     -51.004  61.218   6.305  1.00 22.01           C  
-ATOM   2266  CD2 LEU B  40     -51.999  60.047   4.354  1.00 21.80           C  
-ATOM   2267  N   LYS B  41     -51.131  58.552  10.020  1.00 25.91           N  
-ATOM   2268  CA  LYS B  41     -51.968  58.759  11.192  1.00 27.97           C  
-ATOM   2269  C   LYS B  41     -51.551  59.853  12.170  1.00 29.41           C  
-ATOM   2270  O   LYS B  41     -52.169  60.016  13.220  1.00 29.83           O  
-ATOM   2271  CB  LYS B  41     -52.134  57.435  11.947  1.00 29.62           C  
-ATOM   2272  CG  LYS B  41     -50.865  56.625  12.150  1.00 32.77           C  
-ATOM   2273  CD  LYS B  41     -51.174  55.232  12.715  1.00 36.17           C  
-ATOM   2274  CE  LYS B  41     -52.131  54.462  11.797  1.00 41.03           C  
-ATOM   2275  NZ  LYS B  41     -52.614  53.136  12.343  1.00 44.25           N  
-ATOM   2276  N   ASP B  42     -50.518  60.617  11.841  1.00 30.93           N  
-ATOM   2277  CA  ASP B  42     -50.094  61.681  12.742  1.00 29.96           C  
-ATOM   2278  C   ASP B  42     -49.913  63.038  12.075  1.00 29.18           C  
-ATOM   2279  O   ASP B  42     -49.944  63.162  10.850  1.00 27.67           O  
-ATOM   2280  CB  ASP B  42     -48.808  61.273  13.473  1.00 31.33           C  
-ATOM   2281  CG  ASP B  42     -47.593  61.255  12.572  1.00 32.36           C  
-ATOM   2282  OD1 ASP B  42     -47.721  61.546  11.363  1.00 34.03           O  
-ATOM   2283  OD2 ASP B  42     -46.496  60.948  13.090  1.00 33.27           O  
-ATOM   2284  N   SER B  43     -49.736  64.060  12.904  1.00 29.91           N  
-ATOM   2285  CA  SER B  43     -49.546  65.427  12.425  1.00 30.24           C  
-ATOM   2286  C   SER B  43     -48.428  65.476  11.377  1.00 29.68           C  
-ATOM   2287  O   SER B  43     -48.574  66.105  10.325  1.00 28.50           O  
-ATOM   2288  CB  SER B  43     -49.200  66.328  13.615  1.00 31.29           C  
-ATOM   2289  OG  SER B  43     -49.393  67.698  13.323  1.00 31.72           O  
-ATOM   2290  N   TYR B  44     -47.324  64.789  11.678  1.00 29.79           N  
-ATOM   2291  CA  TYR B  44     -46.143  64.718  10.814  1.00 29.47           C  
-ATOM   2292  C   TYR B  44     -46.446  64.318   9.371  1.00 28.93           C  
-ATOM   2293  O   TYR B  44     -46.441  65.163   8.462  1.00 29.38           O  
-ATOM   2294  CB  TYR B  44     -45.148  63.723  11.385  1.00 31.06           C  
-ATOM   2295  CG  TYR B  44     -43.740  63.910  10.880  1.00 34.09           C  
-ATOM   2296  CD1 TYR B  44     -42.865  64.782  11.517  1.00 35.10           C  
-ATOM   2297  CD2 TYR B  44     -43.274  63.202   9.773  1.00 36.50           C  
-ATOM   2298  CE1 TYR B  44     -41.552  64.946  11.070  1.00 37.01           C  
-ATOM   2299  CE2 TYR B  44     -41.961  63.357   9.314  1.00 37.81           C  
-ATOM   2300  CZ  TYR B  44     -41.104  64.230   9.968  1.00 37.76           C  
-ATOM   2301  OH  TYR B  44     -39.806  64.388   9.530  1.00 35.81           O  
-ATOM   2302  N   TRP B  45     -46.698  63.027   9.160  1.00 26.06           N  
-ATOM   2303  CA  TRP B  45     -46.994  62.537   7.823  1.00 24.03           C  
-ATOM   2304  C   TRP B  45     -48.227  63.139   7.177  1.00 23.53           C  
-ATOM   2305  O   TRP B  45     -48.332  63.145   5.955  1.00 23.51           O  
-ATOM   2306  CB  TRP B  45     -47.082  61.023   7.818  1.00 23.81           C  
-ATOM   2307  CG  TRP B  45     -45.748  60.420   8.037  1.00 25.52           C  
-ATOM   2308  CD1 TRP B  45     -45.168  60.120   9.234  1.00 26.67           C  
-ATOM   2309  CD2 TRP B  45     -44.784  60.095   7.032  1.00 26.08           C  
-ATOM   2310  NE1 TRP B  45     -43.897  59.624   9.039  1.00 26.65           N  
-ATOM   2311  CE2 TRP B  45     -43.637  59.598   7.696  1.00 26.22           C  
-ATOM   2312  CE3 TRP B  45     -44.776  60.176   5.634  1.00 25.56           C  
-ATOM   2313  CZ2 TRP B  45     -42.495  59.183   7.011  1.00 26.60           C  
-ATOM   2314  CZ3 TRP B  45     -43.643  59.765   4.953  1.00 26.57           C  
-ATOM   2315  CH2 TRP B  45     -42.513  59.273   5.643  1.00 27.40           C  
-ATOM   2316  N   LEU B  46     -49.169  63.638   7.974  1.00 23.61           N  
-ATOM   2317  CA  LEU B  46     -50.345  64.280   7.389  1.00 23.05           C  
-ATOM   2318  C   LEU B  46     -49.774  65.534   6.705  1.00 23.66           C  
-ATOM   2319  O   LEU B  46     -50.178  65.895   5.591  1.00 22.43           O  
-ATOM   2320  CB  LEU B  46     -51.364  64.649   8.484  1.00 21.22           C  
-ATOM   2321  CG  LEU B  46     -52.724  65.316   8.176  1.00 19.21           C  
-ATOM   2322  CD1 LEU B  46     -52.582  66.811   8.144  1.00 20.95           C  
-ATOM   2323  CD2 LEU B  46     -53.281  64.825   6.876  1.00 17.82           C  
-ATOM   2324  N   SER B  47     -48.801  66.163   7.373  1.00 23.64           N  
-ATOM   2325  CA  SER B  47     -48.143  67.362   6.857  1.00 23.35           C  
-ATOM   2326  C   SER B  47     -47.240  67.055   5.659  1.00 22.91           C  
-ATOM   2327  O   SER B  47     -47.214  67.813   4.692  1.00 22.42           O  
-ATOM   2328  CB  SER B  47     -47.348  68.044   7.966  1.00 22.85           C  
-ATOM   2329  OG  SER B  47     -48.225  68.763   8.811  1.00 23.90           O  
-ATOM   2330  N   VAL B  48     -46.489  65.960   5.724  1.00 21.59           N  
-ATOM   2331  CA  VAL B  48     -45.656  65.576   4.593  1.00 21.15           C  
-ATOM   2332  C   VAL B  48     -46.598  65.368   3.406  1.00 23.35           C  
-ATOM   2333  O   VAL B  48     -46.344  65.840   2.301  1.00 24.23           O  
-ATOM   2334  CB  VAL B  48     -44.947  64.243   4.834  1.00 19.38           C  
-ATOM   2335  CG1 VAL B  48     -44.389  63.731   3.532  1.00 17.37           C  
-ATOM   2336  CG2 VAL B  48     -43.862  64.402   5.874  1.00 18.62           C  
-ATOM   2337  N   ASN B  49     -47.686  64.642   3.654  1.00 25.04           N  
-ATOM   2338  CA  ASN B  49     -48.689  64.350   2.637  1.00 26.45           C  
-ATOM   2339  C   ASN B  49     -49.175  65.626   1.962  1.00 27.32           C  
-ATOM   2340  O   ASN B  49     -49.227  65.722   0.737  1.00 26.34           O  
-ATOM   2341  CB  ASN B  49     -49.882  63.617   3.273  1.00 27.43           C  
-ATOM   2342  CG  ASN B  49     -50.998  63.312   2.268  1.00 28.31           C  
-ATOM   2343  OD1 ASN B  49     -52.006  64.031   2.182  1.00 25.81           O  
-ATOM   2344  ND2 ASN B  49     -50.814  62.242   1.499  1.00 29.03           N  
-ATOM   2345  N   TYR B  50     -49.535  66.612   2.770  1.00 28.78           N  
-ATOM   2346  CA  TYR B  50     -50.031  67.858   2.221  1.00 30.11           C  
-ATOM   2347  C   TYR B  50     -49.067  68.469   1.215  1.00 30.73           C  
-ATOM   2348  O   TYR B  50     -49.483  68.940   0.158  1.00 31.39           O  
-ATOM   2349  CB  TYR B  50     -50.286  68.868   3.331  1.00 30.08           C  
-ATOM   2350  CG  TYR B  50     -50.608  70.232   2.782  1.00 30.94           C  
-ATOM   2351  CD1 TYR B  50     -51.790  70.455   2.097  1.00 30.29           C  
-ATOM   2352  CD2 TYR B  50     -49.717  71.293   2.928  1.00 32.24           C  
-ATOM   2353  CE1 TYR B  50     -52.084  71.703   1.572  1.00 32.60           C  
-ATOM   2354  CE2 TYR B  50     -50.000  72.547   2.405  1.00 32.96           C  
-ATOM   2355  CZ  TYR B  50     -51.189  72.745   1.729  1.00 32.64           C  
-ATOM   2356  OH  TYR B  50     -51.498  73.984   1.219  1.00 33.28           O  
-ATOM   2357  N   GLY B  51     -47.783  68.473   1.557  1.00 30.02           N  
-ATOM   2358  CA  GLY B  51     -46.792  69.056   0.678  1.00 29.09           C  
-ATOM   2359  C   GLY B  51     -46.625  68.222  -0.569  1.00 29.36           C  
-ATOM   2360  O   GLY B  51     -46.522  68.741  -1.683  1.00 30.54           O  
-ATOM   2361  N   MET B  52     -46.595  66.913  -0.389  1.00 28.16           N  
-ATOM   2362  CA  MET B  52     -46.435  66.036  -1.521  1.00 27.69           C  
-ATOM   2363  C   MET B  52     -47.626  66.239  -2.472  1.00 28.39           C  
-ATOM   2364  O   MET B  52     -47.452  66.338  -3.680  1.00 28.65           O  
-ATOM   2365  CB  MET B  52     -46.345  64.600  -1.023  1.00 26.14           C  
-ATOM   2366  CG  MET B  52     -45.566  63.708  -1.920  1.00 28.23           C  
-ATOM   2367  SD  MET B  52     -44.981  62.254  -1.051  1.00 32.44           S  
-ATOM   2368  CE  MET B  52     -43.717  62.955  -0.003  1.00 31.58           C  
-ATOM   2369  N   VAL B  53     -48.832  66.337  -1.922  1.00 29.70           N  
-ATOM   2370  CA  VAL B  53     -50.038  66.523  -2.734  1.00 30.44           C  
-ATOM   2371  C   VAL B  53     -50.074  67.909  -3.349  1.00 31.52           C  
-ATOM   2372  O   VAL B  53     -50.453  68.075  -4.498  1.00 32.77           O  
-ATOM   2373  CB  VAL B  53     -51.334  66.331  -1.892  1.00 29.46           C  
-ATOM   2374  CG1 VAL B  53     -52.555  66.774  -2.686  1.00 26.17           C  
-ATOM   2375  CG2 VAL B  53     -51.476  64.879  -1.477  1.00 29.30           C  
-ATOM   2376  N   SER B  54     -49.685  68.904  -2.568  1.00 33.05           N  
-ATOM   2377  CA  SER B  54     -49.680  70.283  -3.033  1.00 35.06           C  
-ATOM   2378  C   SER B  54     -48.702  70.475  -4.190  1.00 36.59           C  
-ATOM   2379  O   SER B  54     -49.097  70.925  -5.262  1.00 36.55           O  
-ATOM   2380  CB  SER B  54     -49.321  71.219  -1.878  1.00 34.27           C  
-ATOM   2381  OG  SER B  54     -49.376  72.567  -2.292  1.00 33.96           O  
-ATOM   2382  N   GLU B  55     -47.431  70.134  -3.972  1.00 38.31           N  
-ATOM   2383  CA  GLU B  55     -46.418  70.273  -5.016  1.00 39.51           C  
-ATOM   2384  C   GLU B  55     -46.820  69.433  -6.218  1.00 40.12           C  
-ATOM   2385  O   GLU B  55     -46.740  69.887  -7.348  1.00 41.58           O  
-ATOM   2386  CB  GLU B  55     -45.034  69.822  -4.523  1.00 39.66           C  
-ATOM   2387  CG  GLU B  55     -43.901  70.335  -5.400  1.00 40.31           C  
-ATOM   2388  CD  GLU B  55     -43.835  71.859  -5.409  1.00 42.80           C  
-ATOM   2389  OE1 GLU B  55     -43.388  72.458  -6.413  1.00 42.68           O  
-ATOM   2390  OE2 GLU B  55     -44.225  72.470  -4.395  1.00 45.89           O  
-ATOM   2391  N   ALA B  56     -47.259  68.208  -5.968  1.00 40.85           N  
-ATOM   2392  CA  ALA B  56     -47.679  67.318  -7.038  1.00 41.76           C  
-ATOM   2393  C   ALA B  56     -48.687  68.004  -7.954  1.00 42.28           C  
-ATOM   2394  O   ALA B  56     -48.816  67.669  -9.126  1.00 41.65           O  
-ATOM   2395  CB  ALA B  56     -48.287  66.068  -6.451  1.00 42.37           C  
-ATOM   2396  N   GLU B  57     -49.409  68.967  -7.416  1.00 44.07           N  
-ATOM   2397  CA  GLU B  57     -50.388  69.675  -8.217  1.00 47.53           C  
-ATOM   2398  C   GLU B  57     -49.647  70.750  -9.011  1.00 47.28           C  
-ATOM   2399  O   GLU B  57     -49.683  70.764 -10.236  1.00 46.91           O  
-ATOM   2400  CB  GLU B  57     -51.449  70.297  -7.299  1.00 51.67           C  
-ATOM   2401  CG  GLU B  57     -52.843  70.420  -7.912  1.00 56.63           C  
-ATOM   2402  CD  GLU B  57     -52.937  71.544  -8.930  1.00 60.56           C  
-ATOM   2403  OE1 GLU B  57     -54.010  71.687  -9.568  1.00 62.39           O  
-ATOM   2404  OE2 GLU B  57     -51.939  72.286  -9.087  1.00 62.05           O  
-ATOM   2405  N   LYS B  58     -48.968  71.636  -8.289  1.00 48.75           N  
-ATOM   2406  CA  LYS B  58     -48.190  72.736  -8.865  1.00 48.83           C  
-ATOM   2407  C   LYS B  58     -47.192  72.218  -9.906  1.00 48.13           C  
-ATOM   2408  O   LYS B  58     -47.006  72.810 -10.974  1.00 47.82           O  
-ATOM   2409  CB  LYS B  58     -47.429  73.454  -7.742  1.00 49.71           C  
-ATOM   2410  CG  LYS B  58     -46.736  74.746  -8.142  1.00 53.01           C  
-ATOM   2411  CD  LYS B  58     -45.597  75.082  -7.171  1.00 56.98           C  
-ATOM   2412  CE  LYS B  58     -46.072  75.219  -5.718  1.00 58.98           C  
-ATOM   2413  NZ  LYS B  58     -44.936  75.320  -4.737  1.00 58.62           N  
-ATOM   2414  N   GLN B  59     -46.554  71.102  -9.576  1.00 47.31           N  
-ATOM   2415  CA  GLN B  59     -45.564  70.485 -10.441  1.00 47.05           C  
-ATOM   2416  C   GLN B  59     -46.221  69.879 -11.675  1.00 47.26           C  
-ATOM   2417  O   GLN B  59     -45.537  69.504 -12.623  1.00 48.18           O  
-ATOM   2418  CB  GLN B  59     -44.812  69.402  -9.665  1.00 47.17           C  
-ATOM   2419  CG  GLN B  59     -43.417  69.109 -10.175  1.00 47.57           C  
-ATOM   2420  CD  GLN B  59     -42.558  70.358 -10.240  1.00 47.63           C  
-ATOM   2421  OE1 GLN B  59     -42.606  71.197  -9.341  1.00 44.90           O  
-ATOM   2422  NE2 GLN B  59     -41.759  70.483 -11.304  1.00 48.56           N  
-ATOM   2423  N   GLY B  60     -47.547  69.774 -11.653  1.00 46.73           N  
-ATOM   2424  CA  GLY B  60     -48.275  69.221 -12.785  1.00 45.29           C  
-ATOM   2425  C   GLY B  60     -48.020  67.755 -13.097  1.00 44.71           C  
-ATOM   2426  O   GLY B  60     -47.848  67.387 -14.260  1.00 44.90           O  
-ATOM   2427  N   VAL B  61     -47.992  66.913 -12.069  1.00 44.05           N  
-ATOM   2428  CA  VAL B  61     -47.771  65.484 -12.269  1.00 44.09           C  
-ATOM   2429  C   VAL B  61     -48.952  64.717 -11.682  1.00 44.62           C  
-ATOM   2430  O   VAL B  61     -49.705  65.262 -10.868  1.00 45.37           O  
-ATOM   2431  CB  VAL B  61     -46.464  65.008 -11.588  1.00 43.38           C  
-ATOM   2432  CG1 VAL B  61     -45.317  65.892 -12.012  1.00 44.53           C  
-ATOM   2433  CG2 VAL B  61     -46.612  65.020 -10.080  1.00 41.99           C  
-ATOM   2434  N   ASN B  62     -49.123  63.464 -12.096  1.00 44.01           N  
-ATOM   2435  CA  ASN B  62     -50.224  62.648 -11.591  1.00 44.05           C  
-ATOM   2436  C   ASN B  62     -49.803  61.843 -10.368  1.00 43.12           C  
-ATOM   2437  O   ASN B  62     -49.107  60.824 -10.481  1.00 42.08           O  
-ATOM   2438  CB  ASN B  62     -50.737  61.712 -12.682  1.00 46.63           C  
-ATOM   2439  CG  ASN B  62     -51.618  60.613 -12.134  1.00 48.20           C  
-ATOM   2440  OD1 ASN B  62     -52.534  60.870 -11.348  1.00 50.05           O  
-ATOM   2441  ND2 ASN B  62     -51.347  59.376 -12.545  1.00 48.45           N  
-ATOM   2442  N   LEU B  63     -50.248  62.297  -9.198  1.00 41.82           N  
-ATOM   2443  CA  LEU B  63     -49.881  61.645  -7.947  1.00 41.03           C  
-ATOM   2444  C   LEU B  63     -50.835  60.558  -7.490  1.00 40.65           C  
-ATOM   2445  O   LEU B  63     -52.024  60.567  -7.824  1.00 41.07           O  
-ATOM   2446  CB  LEU B  63     -49.735  62.694  -6.837  1.00 40.14           C  
-ATOM   2447  CG  LEU B  63     -49.254  62.248  -5.452  1.00 37.84           C  
-ATOM   2448  CD1 LEU B  63     -47.916  61.542  -5.564  1.00 36.57           C  
-ATOM   2449  CD2 LEU B  63     -49.148  63.463  -4.541  1.00 36.34           C  
-ATOM   2450  N   ARG B  64     -50.283  59.628  -6.716  1.00 39.41           N  
-ATOM   2451  CA  ARG B  64     -51.024  58.509  -6.154  1.00 40.02           C  
-ATOM   2452  C   ARG B  64     -50.258  58.123  -4.889  1.00 39.65           C  
-ATOM   2453  O   ARG B  64     -49.122  57.649  -4.981  1.00 41.45           O  
-ATOM   2454  CB  ARG B  64     -51.034  57.349  -7.152  1.00 41.21           C  
-ATOM   2455  CG  ARG B  64     -51.953  56.181  -6.808  1.00 45.73           C  
-ATOM   2456  CD  ARG B  64     -51.141  54.904  -6.652  1.00 49.89           C  
-ATOM   2457  NE  ARG B  64     -51.775  53.701  -7.210  1.00 54.08           N  
-ATOM   2458  CZ  ARG B  64     -52.820  53.065  -6.684  1.00 55.58           C  
-ATOM   2459  NH1 ARG B  64     -53.390  53.509  -5.568  1.00 57.57           N  
-ATOM   2460  NH2 ARG B  64     -53.274  51.958  -7.255  1.00 54.83           N  
-ATOM   2461  N   VAL B  65     -50.847  58.339  -3.712  1.00 37.66           N  
-ATOM   2462  CA  VAL B  65     -50.145  57.999  -2.470  1.00 37.05           C  
-ATOM   2463  C   VAL B  65     -50.692  56.758  -1.773  1.00 35.65           C  
-ATOM   2464  O   VAL B  65     -51.889  56.495  -1.789  1.00 36.14           O  
-ATOM   2465  CB  VAL B  65     -50.136  59.188  -1.458  1.00 36.79           C  
-ATOM   2466  CG1 VAL B  65     -49.506  60.398  -2.086  1.00 37.77           C  
-ATOM   2467  CG2 VAL B  65     -51.523  59.529  -1.029  1.00 38.24           C  
-ATOM   2468  N   LEU B  66     -49.798  55.995  -1.161  1.00 34.68           N  
-ATOM   2469  CA  LEU B  66     -50.176  54.776  -0.464  1.00 34.63           C  
-ATOM   2470  C   LEU B  66     -49.506  54.749   0.902  1.00 35.33           C  
-ATOM   2471  O   LEU B  66     -48.320  55.085   1.033  1.00 34.40           O  
-ATOM   2472  CB  LEU B  66     -49.742  53.536  -1.257  1.00 33.91           C  
-ATOM   2473  CG  LEU B  66     -50.197  53.341  -2.708  1.00 33.92           C  
-ATOM   2474  CD1 LEU B  66     -49.612  52.036  -3.227  1.00 34.88           C  
-ATOM   2475  CD2 LEU B  66     -51.708  53.318  -2.808  1.00 32.82           C  
-ATOM   2476  N   GLU B  67     -50.269  54.338   1.912  1.00 35.87           N  
-ATOM   2477  CA  GLU B  67     -49.757  54.267   3.271  1.00 36.25           C  
-ATOM   2478  C   GLU B  67     -49.816  52.861   3.835  1.00 37.20           C  
-ATOM   2479  O   GLU B  67     -50.855  52.205   3.774  1.00 38.71           O  
-ATOM   2480  CB  GLU B  67     -50.536  55.230   4.184  1.00 35.95           C  
-ATOM   2481  CG  GLU B  67     -52.057  55.041   4.257  1.00 35.87           C  
-ATOM   2482  CD  GLU B  67     -52.508  54.254   5.485  1.00 38.79           C  
-ATOM   2483  OE1 GLU B  67     -51.791  54.271   6.516  1.00 41.92           O  
-ATOM   2484  OE2 GLU B  67     -53.592  53.633   5.433  1.00 38.52           O  
-ATOM   2485  N   ALA B  68     -48.695  52.387   4.368  1.00 37.70           N  
-ATOM   2486  CA  ALA B  68     -48.658  51.059   4.976  1.00 38.54           C  
-ATOM   2487  C   ALA B  68     -49.569  51.105   6.208  1.00 39.35           C  
-ATOM   2488  O   ALA B  68     -50.072  52.170   6.588  1.00 40.42           O  
-ATOM   2489  CB  ALA B  68     -47.243  50.714   5.391  1.00 36.80           C  
-ATOM   2490  N   GLY B  69     -49.789  49.971   6.848  1.00 38.46           N  
-ATOM   2491  CA  GLY B  69     -50.648  50.021   8.015  1.00 38.80           C  
-ATOM   2492  C   GLY B  69     -50.061  50.874   9.132  1.00 37.93           C  
-ATOM   2493  O   GLY B  69     -50.778  51.540   9.866  1.00 36.75           O  
-ATOM   2494  N   GLY B  70     -48.737  50.840   9.240  1.00 38.70           N  
-ATOM   2495  CA  GLY B  70     -48.009  51.559  10.270  1.00 38.89           C  
-ATOM   2496  C   GLY B  70     -46.593  51.018  10.184  1.00 40.22           C  
-ATOM   2497  O   GLY B  70     -46.351  50.101   9.401  1.00 39.96           O  
-ATOM   2498  N   TYR B  71     -45.658  51.540  10.975  1.00 41.45           N  
-ATOM   2499  CA  TYR B  71     -44.272  51.074  10.887  1.00 42.88           C  
-ATOM   2500  C   TYR B  71     -44.014  49.566  10.993  1.00 44.37           C  
-ATOM   2501  O   TYR B  71     -43.058  49.046  10.405  1.00 45.60           O  
-ATOM   2502  CB  TYR B  71     -43.393  51.810  11.896  1.00 41.72           C  
-ATOM   2503  CG  TYR B  71     -42.938  53.168  11.422  1.00 40.22           C  
-ATOM   2504  CD1 TYR B  71     -43.499  54.325  11.939  1.00 40.83           C  
-ATOM   2505  CD2 TYR B  71     -41.947  53.294  10.452  1.00 40.45           C  
-ATOM   2506  CE1 TYR B  71     -43.085  55.586  11.506  1.00 41.14           C  
-ATOM   2507  CE2 TYR B  71     -41.523  54.551  10.010  1.00 40.16           C  
-ATOM   2508  CZ  TYR B  71     -42.100  55.693  10.543  1.00 40.62           C  
-ATOM   2509  OH  TYR B  71     -41.712  56.943  10.119  1.00 40.32           O  
-ATOM   2510  N   PRO B  72     -44.839  48.841  11.753  1.00 44.69           N  
-ATOM   2511  CA  PRO B  72     -44.556  47.406  11.820  1.00 44.85           C  
-ATOM   2512  C   PRO B  72     -45.047  46.593  10.613  1.00 45.21           C  
-ATOM   2513  O   PRO B  72     -44.757  45.406  10.511  1.00 46.49           O  
-ATOM   2514  CB  PRO B  72     -45.238  46.992  13.116  1.00 43.61           C  
-ATOM   2515  CG  PRO B  72     -46.388  47.927  13.186  1.00 44.42           C  
-ATOM   2516  CD  PRO B  72     -45.752  49.242  12.832  1.00 43.98           C  
-ATOM   2517  N   ASN B  73     -45.759  47.238   9.691  1.00 45.72           N  
-ATOM   2518  CA  ASN B  73     -46.318  46.570   8.503  1.00 46.10           C  
-ATOM   2519  C   ASN B  73     -45.389  46.371   7.292  1.00 46.77           C  
-ATOM   2520  O   ASN B  73     -45.710  46.804   6.183  1.00 45.29           O  
-ATOM   2521  CB  ASN B  73     -47.571  47.331   8.046  1.00 45.29           C  
-ATOM   2522  CG  ASN B  73     -48.753  47.132   8.980  1.00 43.54           C  
-ATOM   2523  OD1 ASN B  73     -48.597  47.041  10.201  1.00 43.26           O  
-ATOM   2524  ND2 ASN B  73     -49.947  47.078   8.407  1.00 43.49           N  
-ATOM   2525  N   LYS B  74     -44.263  45.688   7.502  1.00 49.15           N  
-ATOM   2526  CA  LYS B  74     -43.274  45.430   6.439  1.00 51.00           C  
-ATOM   2527  C   LYS B  74     -43.878  44.803   5.175  1.00 50.93           C  
-ATOM   2528  O   LYS B  74     -43.718  45.322   4.062  1.00 49.59           O  
-ATOM   2529  CB  LYS B  74     -42.165  44.502   6.952  1.00 52.64           C  
-ATOM   2530  CG  LYS B  74     -41.728  44.720   8.402  1.00 55.48           C  
-ATOM   2531  CD  LYS B  74     -41.150  46.108   8.630  1.00 58.62           C  
-ATOM   2532  CE  LYS B  74     -40.202  46.125   9.826  1.00 60.91           C  
-ATOM   2533  NZ  LYS B  74     -38.996  45.257   9.599  1.00 61.64           N  
-ATOM   2534  N   SER B  75     -44.560  43.676   5.354  1.00 50.91           N  
-ATOM   2535  CA  SER B  75     -45.170  42.984   4.235  1.00 51.24           C  
-ATOM   2536  C   SER B  75     -46.049  43.908   3.413  1.00 51.32           C  
-ATOM   2537  O   SER B  75     -45.900  43.998   2.198  1.00 51.14           O  
-ATOM   2538  CB  SER B  75     -46.011  41.809   4.728  1.00 51.63           C  
-ATOM   2539  OG  SER B  75     -46.767  41.267   3.654  1.00 52.13           O  
-ATOM   2540  N   ARG B  76     -46.965  44.593   4.087  1.00 51.92           N  
-ATOM   2541  CA  ARG B  76     -47.889  45.497   3.418  1.00 51.98           C  
-ATOM   2542  C   ARG B  76     -47.176  46.478   2.500  1.00 52.73           C  
-ATOM   2543  O   ARG B  76     -47.596  46.676   1.361  1.00 52.75           O  
-ATOM   2544  CB  ARG B  76     -48.707  46.277   4.447  1.00 51.54           C  
-ATOM   2545  CG  ARG B  76     -49.802  47.149   3.844  1.00 51.80           C  
-ATOM   2546  CD  ARG B  76     -51.090  46.368   3.671  1.00 52.40           C  
-ATOM   2547  NE  ARG B  76     -51.612  45.910   4.958  1.00 53.65           N  
-ATOM   2548  CZ  ARG B  76     -52.171  46.699   5.875  1.00 54.16           C  
-ATOM   2549  NH1 ARG B  76     -52.296  48.008   5.657  1.00 54.05           N  
-ATOM   2550  NH2 ARG B  76     -52.603  46.174   7.017  1.00 53.40           N  
-ATOM   2551  N   GLN B  77     -46.098  47.090   2.989  1.00 53.18           N  
-ATOM   2552  CA  GLN B  77     -45.376  48.064   2.180  1.00 52.99           C  
-ATOM   2553  C   GLN B  77     -44.710  47.419   0.974  1.00 52.94           C  
-ATOM   2554  O   GLN B  77     -44.621  48.030  -0.094  1.00 52.39           O  
-ATOM   2555  CB  GLN B  77     -44.337  48.814   3.019  1.00 52.83           C  
-ATOM   2556  CG  GLN B  77     -43.779  50.036   2.291  1.00 53.48           C  
-ATOM   2557  CD  GLN B  77     -42.981  50.963   3.187  1.00 53.81           C  
-ATOM   2558  OE1 GLN B  77     -41.972  50.569   3.776  1.00 53.32           O  
-ATOM   2559  NE2 GLN B  77     -43.431  52.213   3.289  1.00 53.86           N  
-ATOM   2560  N   GLU B  78     -44.247  46.183   1.141  1.00 52.75           N  
-ATOM   2561  CA  GLU B  78     -43.608  45.475   0.040  1.00 52.47           C  
-ATOM   2562  C   GLU B  78     -44.611  45.339  -1.092  1.00 52.51           C  
-ATOM   2563  O   GLU B  78     -44.305  45.628  -2.245  1.00 53.54           O  
-ATOM   2564  CB  GLU B  78     -43.133  44.093   0.491  1.00 51.00           C  
-ATOM   2565  CG  GLU B  78     -42.212  44.160   1.700  1.00 52.74           C  
-ATOM   2566  CD  GLU B  78     -41.635  42.813   2.099  1.00 52.69           C  
-ATOM   2567  OE1 GLU B  78     -42.387  41.813   2.077  1.00 53.22           O  
-ATOM   2568  OE2 GLU B  78     -40.435  42.760   2.451  1.00 51.02           O  
-ATOM   2569  N   GLN B  79     -45.823  44.928  -0.761  1.00 52.80           N  
-ATOM   2570  CA  GLN B  79     -46.838  44.758  -1.779  1.00 54.42           C  
-ATOM   2571  C   GLN B  79     -47.257  46.086  -2.372  1.00 54.27           C  
-ATOM   2572  O   GLN B  79     -47.630  46.150  -3.541  1.00 55.71           O  
-ATOM   2573  CB  GLN B  79     -48.048  44.051  -1.196  1.00 56.68           C  
-ATOM   2574  CG  GLN B  79     -47.679  42.835  -0.393  1.00 61.68           C  
-ATOM   2575  CD  GLN B  79     -48.876  42.206   0.269  1.00 64.56           C  
-ATOM   2576  OE1 GLN B  79     -49.664  42.885   0.931  1.00 65.88           O  
-ATOM   2577  NE2 GLN B  79     -49.021  40.897   0.102  1.00 67.36           N  
-ATOM   2578  N   GLN B  80     -47.210  47.149  -1.576  1.00 53.79           N  
-ATOM   2579  CA  GLN B  80     -47.595  48.468  -2.081  1.00 53.39           C  
-ATOM   2580  C   GLN B  80     -46.563  48.954  -3.082  1.00 53.09           C  
-ATOM   2581  O   GLN B  80     -46.892  49.629  -4.058  1.00 53.08           O  
-ATOM   2582  CB  GLN B  80     -47.711  49.476  -0.941  1.00 52.41           C  
-ATOM   2583  CG  GLN B  80     -49.026  49.425  -0.229  1.00 50.46           C  
-ATOM   2584  CD  GLN B  80     -49.034  50.297   0.988  1.00 50.30           C  
-ATOM   2585  OE1 GLN B  80     -48.340  50.025   1.964  1.00 49.42           O  
-ATOM   2586  NE2 GLN B  80     -49.814  51.364   0.941  1.00 52.27           N  
-ATOM   2587  N   LEU B  81     -45.308  48.611  -2.821  1.00 51.77           N  
-ATOM   2588  CA  LEU B  81     -44.219  48.986  -3.701  1.00 50.71           C  
-ATOM   2589  C   LEU B  81     -44.504  48.301  -5.033  1.00 51.15           C  
-ATOM   2590  O   LEU B  81     -44.458  48.918  -6.099  1.00 51.02           O  
-ATOM   2591  CB  LEU B  81     -42.902  48.495  -3.106  1.00 48.23           C  
-ATOM   2592  CG  LEU B  81     -41.762  49.506  -2.964  1.00 47.37           C  
-ATOM   2593  CD1 LEU B  81     -42.257  50.957  -2.992  1.00 44.64           C  
-ATOM   2594  CD2 LEU B  81     -41.057  49.197  -1.667  1.00 46.62           C  
-ATOM   2595  N   ALA B  82     -44.823  47.016  -4.950  1.00 51.66           N  
-ATOM   2596  CA  ALA B  82     -45.144  46.215  -6.122  1.00 52.07           C  
-ATOM   2597  C   ALA B  82     -46.407  46.736  -6.820  1.00 52.01           C  
-ATOM   2598  O   ALA B  82     -46.512  46.710  -8.050  1.00 51.79           O  
-ATOM   2599  CB  ALA B  82     -45.334  44.761  -5.704  1.00 51.45           C  
-ATOM   2600  N   LEU B  83     -47.363  47.209  -6.028  1.00 52.20           N  
-ATOM   2601  CA  LEU B  83     -48.612  47.730  -6.561  1.00 52.76           C  
-ATOM   2602  C   LEU B  83     -48.351  49.027  -7.329  1.00 53.64           C  
-ATOM   2603  O   LEU B  83     -48.980  49.291  -8.357  1.00 52.26           O  
-ATOM   2604  CB  LEU B  83     -49.601  47.967  -5.415  1.00 52.35           C  
-ATOM   2605  CG  LEU B  83     -51.093  47.970  -5.774  1.00 52.86           C  
-ATOM   2606  CD1 LEU B  83     -51.867  47.478  -4.568  1.00 52.10           C  
-ATOM   2607  CD2 LEU B  83     -51.572  49.356  -6.221  1.00 52.42           C  
-ATOM   2608  N   CYS B  84     -47.415  49.830  -6.822  1.00 55.61           N  
-ATOM   2609  CA  CYS B  84     -47.044  51.099  -7.455  1.00 56.33           C  
-ATOM   2610  C   CYS B  84     -46.506  50.823  -8.855  1.00 56.43           C  
-ATOM   2611  O   CYS B  84     -46.793  51.565  -9.797  1.00 55.71           O  
-ATOM   2612  CB  CYS B  84     -45.953  51.821  -6.643  1.00 56.82           C  
-ATOM   2613  SG  CYS B  84     -46.451  53.024  -5.350  1.00 57.89           S  
-ATOM   2614  N   THR B  85     -45.717  49.754  -8.975  1.00 56.95           N  
-ATOM   2615  CA  THR B  85     -45.122  49.361 -10.250  1.00 56.79           C  
-ATOM   2616  C   THR B  85     -46.212  48.914 -11.226  1.00 56.82           C  
-ATOM   2617  O   THR B  85     -46.253  49.379 -12.364  1.00 56.72           O  
-ATOM   2618  CB  THR B  85     -44.105  48.199 -10.081  1.00 56.70           C  
-ATOM   2619  OG1 THR B  85     -43.347  48.371  -8.875  1.00 55.64           O  
-ATOM   2620  CG2 THR B  85     -43.143  48.181 -11.257  1.00 56.65           C  
-ATOM   2621  N   GLN B  86     -47.090  48.015 -10.782  1.00 56.71           N  
-ATOM   2622  CA  GLN B  86     -48.184  47.526 -11.625  1.00 57.45           C  
-ATOM   2623  C   GLN B  86     -49.040  48.676 -12.128  1.00 55.80           C  
-ATOM   2624  O   GLN B  86     -49.644  48.597 -13.196  1.00 55.57           O  
-ATOM   2625  CB  GLN B  86     -49.078  46.573 -10.846  1.00 60.30           C  
-ATOM   2626  CG  GLN B  86     -48.451  45.240 -10.527  1.00 67.01           C  
-ATOM   2627  CD  GLN B  86     -49.247  44.485  -9.476  1.00 70.87           C  
-ATOM   2628  OE1 GLN B  86     -50.488  44.505  -9.485  1.00 72.08           O  
-ATOM   2629  NE2 GLN B  86     -48.541  43.811  -8.563  1.00 71.28           N  
-ATOM   2630  N   TRP B  87     -49.105  49.736 -11.330  1.00 54.19           N  
-ATOM   2631  CA  TRP B  87     -49.876  50.921 -11.675  1.00 51.55           C  
-ATOM   2632  C   TRP B  87     -49.152  51.629 -12.805  1.00 51.47           C  
-ATOM   2633  O   TRP B  87     -49.738  52.427 -13.533  1.00 49.50           O  
-ATOM   2634  CB  TRP B  87     -49.990  51.837 -10.453  1.00 49.62           C  
-ATOM   2635  CG  TRP B  87     -50.639  53.157 -10.734  1.00 48.05           C  
-ATOM   2636  CD1 TRP B  87     -51.866  53.371 -11.300  1.00 47.83           C  
-ATOM   2637  CD2 TRP B  87     -50.092  54.452 -10.465  1.00 46.99           C  
-ATOM   2638  NE1 TRP B  87     -52.117  54.721 -11.401  1.00 45.48           N  
-ATOM   2639  CE2 TRP B  87     -51.045  55.408 -10.897  1.00 45.70           C  
-ATOM   2640  CE3 TRP B  87     -48.889  54.900  -9.902  1.00 45.69           C  
-ATOM   2641  CZ2 TRP B  87     -50.832  56.781 -10.785  1.00 44.44           C  
-ATOM   2642  CZ3 TRP B  87     -48.677  56.264  -9.790  1.00 45.66           C  
-ATOM   2643  CH2 TRP B  87     -49.646  57.191 -10.232  1.00 45.49           C  
-ATOM   2644  N   GLY B  88     -47.867  51.312 -12.943  1.00 52.75           N  
-ATOM   2645  CA  GLY B  88     -47.045  51.910 -13.978  1.00 54.38           C  
-ATOM   2646  C   GLY B  88     -46.419  53.216 -13.532  1.00 55.68           C  
-ATOM   2647  O   GLY B  88     -46.364  54.186 -14.291  1.00 56.76           O  
-ATOM   2648  N   ALA B  89     -45.942  53.252 -12.295  1.00 55.84           N  
-ATOM   2649  CA  ALA B  89     -45.332  54.465 -11.781  1.00 55.43           C  
-ATOM   2650  C   ALA B  89     -44.091  54.808 -12.590  1.00 55.00           C  
-ATOM   2651  O   ALA B  89     -43.245  53.941 -12.829  1.00 55.54           O  
-ATOM   2652  CB  ALA B  89     -44.962  54.279 -10.317  1.00 55.52           C  
-ATOM   2653  N   ASN B  90     -43.995  56.063 -13.026  1.00 53.60           N  
-ATOM   2654  CA  ASN B  90     -42.824  56.521 -13.771  1.00 52.83           C  
-ATOM   2655  C   ASN B  90     -41.705  56.767 -12.738  1.00 52.38           C  
-ATOM   2656  O   ASN B  90     -40.512  56.625 -13.035  1.00 52.74           O  
-ATOM   2657  CB  ASN B  90     -43.132  57.817 -14.543  1.00 52.48           C  
-ATOM   2658  CG  ASN B  90     -44.145  57.613 -15.669  1.00 53.12           C  
-ATOM   2659  OD1 ASN B  90     -44.035  56.671 -16.453  1.00 54.06           O  
-ATOM   2660  ND2 ASN B  90     -45.125  58.509 -15.762  1.00 52.52           N  
-ATOM   2661  N   ALA B  91     -42.116  57.117 -11.518  1.00 50.81           N  
-ATOM   2662  CA  ALA B  91     -41.202  57.383 -10.405  1.00 47.99           C  
-ATOM   2663  C   ALA B  91     -41.893  57.047  -9.077  1.00 45.98           C  
-ATOM   2664  O   ALA B  91     -43.098  57.286  -8.909  1.00 45.00           O  
-ATOM   2665  CB  ALA B  91     -40.772  58.855 -10.416  1.00 48.73           C  
-ATOM   2666  N   ILE B  92     -41.121  56.506  -8.136  1.00 43.06           N  
-ATOM   2667  CA  ILE B  92     -41.647  56.122  -6.828  1.00 40.59           C  
-ATOM   2668  C   ILE B  92     -40.952  56.809  -5.653  1.00 39.35           C  
-ATOM   2669  O   ILE B  92     -39.744  56.655  -5.462  1.00 39.59           O  
-ATOM   2670  CB  ILE B  92     -41.522  54.587  -6.606  1.00 40.44           C  
-ATOM   2671  CG1 ILE B  92     -42.580  53.845  -7.418  1.00 40.43           C  
-ATOM   2672  CG2 ILE B  92     -41.664  54.246  -5.128  1.00 39.75           C  
-ATOM   2673  CD1 ILE B  92     -42.391  52.333  -7.405  1.00 40.09           C  
-ATOM   2674  N   ILE B  93     -41.711  57.569  -4.867  1.00 36.71           N  
-ATOM   2675  CA  ILE B  93     -41.149  58.203  -3.679  1.00 33.43           C  
-ATOM   2676  C   ILE B  93     -41.437  57.199  -2.551  1.00 32.78           C  
-ATOM   2677  O   ILE B  93     -42.541  56.671  -2.460  1.00 32.52           O  
-ATOM   2678  CB  ILE B  93     -41.825  59.534  -3.391  1.00 31.44           C  
-ATOM   2679  CG1 ILE B  93     -41.712  60.441  -4.615  1.00 31.52           C  
-ATOM   2680  CG2 ILE B  93     -41.161  60.189  -2.214  1.00 31.16           C  
-ATOM   2681  CD1 ILE B  93     -42.317  61.840  -4.427  1.00 32.74           C  
-ATOM   2682  N   LEU B  94     -40.458  56.924  -1.698  1.00 32.18           N  
-ATOM   2683  CA  LEU B  94     -40.656  55.931  -0.652  1.00 32.74           C  
-ATOM   2684  C   LEU B  94     -40.188  56.296   0.758  1.00 34.73           C  
-ATOM   2685  O   LEU B  94     -39.025  56.646   0.976  1.00 33.21           O  
-ATOM   2686  CB  LEU B  94     -39.987  54.623  -1.098  1.00 31.91           C  
-ATOM   2687  CG  LEU B  94     -39.882  53.361  -0.225  1.00 30.57           C  
-ATOM   2688  CD1 LEU B  94     -38.836  53.535   0.852  1.00 28.63           C  
-ATOM   2689  CD2 LEU B  94     -41.242  53.050   0.362  1.00 31.88           C  
-ATOM   2690  N   GLY B  95     -41.117  56.203   1.710  1.00 36.64           N  
-ATOM   2691  CA  GLY B  95     -40.814  56.472   3.105  1.00 38.37           C  
-ATOM   2692  C   GLY B  95     -40.708  55.119   3.786  1.00 40.01           C  
-ATOM   2693  O   GLY B  95     -41.711  54.574   4.238  1.00 40.37           O  
-ATOM   2694  N   THR B  96     -39.495  54.572   3.847  1.00 42.00           N  
-ATOM   2695  CA  THR B  96     -39.259  53.253   4.441  1.00 44.16           C  
-ATOM   2696  C   THR B  96     -39.894  53.027   5.784  1.00 44.74           C  
-ATOM   2697  O   THR B  96     -39.939  53.914   6.634  1.00 44.36           O  
-ATOM   2698  CB  THR B  96     -37.770  52.939   4.657  1.00 45.19           C  
-ATOM   2699  OG1 THR B  96     -36.963  53.856   3.911  1.00 46.90           O  
-ATOM   2700  CG2 THR B  96     -37.480  51.504   4.232  1.00 43.61           C  
-ATOM   2701  N   VAL B  97     -40.328  51.791   5.976  1.00 45.84           N  
-ATOM   2702  CA  VAL B  97     -40.972  51.367   7.201  1.00 46.77           C  
-ATOM   2703  C   VAL B  97     -39.888  50.808   8.132  1.00 49.06           C  
-ATOM   2704  O   VAL B  97     -40.122  50.533   9.309  1.00 48.24           O  
-ATOM   2705  CB  VAL B  97     -42.032  50.305   6.851  1.00 44.48           C  
-ATOM   2706  CG1 VAL B  97     -41.427  48.922   6.911  1.00 42.25           C  
-ATOM   2707  CG2 VAL B  97     -43.238  50.468   7.731  1.00 43.26           C  
-ATOM   2708  N   ASP B  98     -38.691  50.671   7.570  1.00 53.06           N  
-ATOM   2709  CA  ASP B  98     -37.506  50.157   8.259  1.00 56.37           C  
-ATOM   2710  C   ASP B  98     -36.308  50.418   7.344  1.00 57.35           C  
-ATOM   2711  O   ASP B  98     -36.274  49.940   6.210  1.00 56.63           O  
-ATOM   2712  CB  ASP B  98     -37.631  48.648   8.497  1.00 58.92           C  
-ATOM   2713  CG  ASP B  98     -36.289  47.989   8.829  1.00 61.61           C  
-ATOM   2714  OD1 ASP B  98     -36.162  46.763   8.608  1.00 62.61           O  
-ATOM   2715  OD2 ASP B  98     -35.367  48.688   9.314  1.00 62.40           O  
-ATOM   2716  N   PRO B  99     -35.303  51.164   7.832  1.00 58.27           N  
-ATOM   2717  CA  PRO B  99     -34.112  51.480   7.041  1.00 58.83           C  
-ATOM   2718  C   PRO B  99     -33.513  50.325   6.238  1.00 59.73           C  
-ATOM   2719  O   PRO B  99     -33.421  50.395   5.009  1.00 60.05           O  
-ATOM   2720  CB  PRO B  99     -33.141  52.013   8.091  1.00 57.61           C  
-ATOM   2721  CG  PRO B  99     -34.045  52.714   9.031  1.00 57.80           C  
-ATOM   2722  CD  PRO B  99     -35.167  51.705   9.196  1.00 58.26           C  
-ATOM   2723  N   HIS B 100     -33.122  49.259   6.930  1.00 60.74           N  
-ATOM   2724  CA  HIS B 100     -32.486  48.123   6.275  1.00 61.62           C  
-ATOM   2725  C   HIS B 100     -33.385  47.184   5.478  1.00 62.13           C  
-ATOM   2726  O   HIS B 100     -32.914  46.182   4.942  1.00 62.42           O  
-ATOM   2727  CB  HIS B 100     -31.659  47.338   7.299  1.00 62.11           C  
-ATOM   2728  CG  HIS B 100     -30.671  48.187   8.036  1.00 62.88           C  
-ATOM   2729  ND1 HIS B 100     -29.714  48.940   7.391  1.00 63.65           N  
-ATOM   2730  CD2 HIS B 100     -30.534  48.457   9.356  1.00 64.21           C  
-ATOM   2731  CE1 HIS B 100     -29.035  49.643   8.281  1.00 64.37           C  
-ATOM   2732  NE2 HIS B 100     -29.513  49.369   9.481  1.00 64.82           N  
-ATOM   2733  N   ALA B 101     -34.674  47.491   5.398  1.00 62.69           N  
-ATOM   2734  CA  ALA B 101     -35.573  46.664   4.602  1.00 63.70           C  
-ATOM   2735  C   ALA B 101     -35.248  47.029   3.152  1.00 65.46           C  
-ATOM   2736  O   ALA B 101     -34.603  48.055   2.895  1.00 66.85           O  
-ATOM   2737  CB  ALA B 101     -37.016  47.001   4.918  1.00 62.30           C  
-ATOM   2738  N   TYR B 102     -35.677  46.202   2.205  1.00 66.05           N  
-ATOM   2739  CA  TYR B 102     -35.414  46.465   0.781  1.00 67.21           C  
-ATOM   2740  C   TYR B 102     -33.929  46.654   0.409  1.00 67.57           C  
-ATOM   2741  O   TYR B 102     -33.604  46.815  -0.771  1.00 67.45           O  
-ATOM   2742  CB  TYR B 102     -36.168  47.715   0.302  1.00 66.28           C  
-ATOM   2743  CG  TYR B 102     -37.562  47.901   0.853  1.00 65.78           C  
-ATOM   2744  CD1 TYR B 102     -37.789  48.717   1.964  1.00 65.57           C  
-ATOM   2745  CD2 TYR B 102     -38.659  47.293   0.248  1.00 65.49           C  
-ATOM   2746  CE1 TYR B 102     -39.072  48.928   2.453  1.00 65.28           C  
-ATOM   2747  CE2 TYR B 102     -39.947  47.494   0.731  1.00 65.60           C  
-ATOM   2748  CZ  TYR B 102     -40.147  48.314   1.831  1.00 65.62           C  
-ATOM   2749  OH  TYR B 102     -41.422  48.523   2.300  1.00 65.45           O  
-ATOM   2750  N   GLU B 103     -33.041  46.636   1.404  1.00 67.80           N  
-ATOM   2751  CA  GLU B 103     -31.603  46.823   1.181  1.00 67.69           C  
-ATOM   2752  C   GLU B 103     -31.017  45.921   0.089  1.00 66.99           C  
-ATOM   2753  O   GLU B 103     -30.123  46.339  -0.651  1.00 66.47           O  
-ATOM   2754  CB  GLU B 103     -30.833  46.599   2.487  1.00 68.36           C  
-ATOM   2755  CG  GLU B 103     -29.442  47.224   2.502  1.00 70.01           C  
-ATOM   2756  CD  GLU B 103     -28.766  47.128   3.865  1.00 71.45           C  
-ATOM   2757  OE1 GLU B 103     -27.785  47.867   4.093  1.00 70.55           O  
-ATOM   2758  OE2 GLU B 103     -29.209  46.313   4.705  1.00 72.82           O  
-ATOM   2759  N   HIS B 104     -31.514  44.689  -0.004  1.00 66.02           N  
-ATOM   2760  CA  HIS B 104     -31.036  43.748  -1.015  1.00 64.77           C  
-ATOM   2761  C   HIS B 104     -32.203  43.214  -1.852  1.00 64.38           C  
-ATOM   2762  O   HIS B 104     -32.085  42.139  -2.454  1.00 64.43           O  
-ATOM   2763  CB  HIS B 104     -30.328  42.546  -0.367  1.00 64.38           C  
-ATOM   2764  CG  HIS B 104     -29.458  42.894   0.804  1.00 64.68           C  
-ATOM   2765  ND1 HIS B 104     -28.518  43.903   0.769  1.00 64.86           N  
-ATOM   2766  CD2 HIS B 104     -29.362  42.337   2.036  1.00 63.89           C  
-ATOM   2767  CE1 HIS B 104     -27.883  43.952   1.927  1.00 63.77           C  
-ATOM   2768  NE2 HIS B 104     -28.375  43.012   2.713  1.00 62.83           N  
-ATOM   2769  N   ASN B 105     -33.315  43.956  -1.903  1.00 63.21           N  
-ATOM   2770  CA  ASN B 105     -34.495  43.502  -2.645  1.00 62.25           C  
-ATOM   2771  C   ASN B 105     -35.209  44.551  -3.479  1.00 61.71           C  
-ATOM   2772  O   ASN B 105     -35.982  44.205  -4.371  1.00 61.34           O  
-ATOM   2773  CB  ASN B 105     -35.534  42.925  -1.684  1.00 62.48           C  
-ATOM   2774  CG  ASN B 105     -34.915  42.355  -0.435  1.00 64.92           C  
-ATOM   2775  OD1 ASN B 105     -34.257  43.066   0.331  1.00 65.78           O  
-ATOM   2776  ND2 ASN B 105     -35.118  41.062  -0.215  1.00 66.70           N  
-ATOM   2777  N   LEU B 106     -34.970  45.824  -3.187  1.00 60.61           N  
-ATOM   2778  CA  LEU B 106     -35.656  46.895  -3.895  1.00 59.98           C  
-ATOM   2779  C   LEU B 106     -36.056  46.597  -5.341  1.00 60.35           C  
-ATOM   2780  O   LEU B 106     -37.210  46.817  -5.714  1.00 60.15           O  
-ATOM   2781  CB  LEU B 106     -34.839  48.188  -3.828  1.00 58.44           C  
-ATOM   2782  CG  LEU B 106     -35.589  49.449  -4.276  1.00 57.51           C  
-ATOM   2783  CD1 LEU B 106     -37.005  49.472  -3.710  1.00 55.02           C  
-ATOM   2784  CD2 LEU B 106     -34.817  50.662  -3.826  1.00 56.52           C  
-ATOM   2785  N   LYS B 107     -35.128  46.089  -6.150  1.00 61.55           N  
-ATOM   2786  CA  LYS B 107     -35.429  45.781  -7.556  1.00 62.27           C  
-ATOM   2787  C   LYS B 107     -36.470  44.674  -7.746  1.00 61.98           C  
-ATOM   2788  O   LYS B 107     -37.222  44.679  -8.724  1.00 61.40           O  
-ATOM   2789  CB  LYS B 107     -34.145  45.415  -8.313  1.00 63.10           C  
-ATOM   2790  CG  LYS B 107     -33.251  46.614  -8.622  1.00 65.20           C  
-ATOM   2791  CD  LYS B 107     -31.936  46.202  -9.286  1.00 65.87           C  
-ATOM   2792  CE  LYS B 107     -31.030  47.411  -9.521  1.00 65.54           C  
-ATOM   2793  NZ  LYS B 107     -29.779  47.049 -10.240  1.00 65.40           N  
-ATOM   2794  N   SER B 108     -36.517  43.730  -6.811  1.00 61.83           N  
-ATOM   2795  CA  SER B 108     -37.477  42.633  -6.880  1.00 61.02           C  
-ATOM   2796  C   SER B 108     -38.878  43.103  -6.497  1.00 60.72           C  
-ATOM   2797  O   SER B 108     -39.807  42.303  -6.440  1.00 60.99           O  
-ATOM   2798  CB  SER B 108     -37.056  41.506  -5.942  1.00 60.67           C  
-ATOM   2799  OG  SER B 108     -37.052  41.953  -4.599  1.00 59.26           O  
-ATOM   2800  N   TRP B 109     -39.019  44.398  -6.224  1.00 60.42           N  
-ATOM   2801  CA  TRP B 109     -40.305  44.981  -5.848  1.00 59.76           C  
-ATOM   2802  C   TRP B 109     -40.707  46.060  -6.852  1.00 60.14           C  
-ATOM   2803  O   TRP B 109     -41.828  46.068  -7.366  1.00 60.31           O  
-ATOM   2804  CB  TRP B 109     -40.233  45.613  -4.448  1.00 58.50           C  
-ATOM   2805  CG  TRP B 109     -39.989  44.657  -3.303  1.00 56.71           C  
-ATOM   2806  CD1 TRP B 109     -38.965  44.707  -2.394  1.00 56.85           C  
-ATOM   2807  CD2 TRP B 109     -40.803  43.541  -2.921  1.00 56.14           C  
-ATOM   2808  NE1 TRP B 109     -39.092  43.693  -1.471  1.00 55.80           N  
-ATOM   2809  CE2 TRP B 109     -40.211  42.963  -1.772  1.00 55.96           C  
-ATOM   2810  CE3 TRP B 109     -41.974  42.973  -3.438  1.00 55.42           C  
-ATOM   2811  CZ2 TRP B 109     -40.753  41.846  -1.133  1.00 55.81           C  
-ATOM   2812  CZ3 TRP B 109     -42.512  41.861  -2.802  1.00 55.60           C  
-ATOM   2813  CH2 TRP B 109     -41.900  41.310  -1.661  1.00 55.95           C  
-ATOM   2814  N   VAL B 110     -39.785  46.977  -7.125  1.00 60.46           N  
-ATOM   2815  CA  VAL B 110     -40.056  48.063  -8.057  1.00 61.42           C  
-ATOM   2816  C   VAL B 110     -39.537  47.765  -9.457  1.00 61.67           C  
-ATOM   2817  O   VAL B 110     -39.962  48.394 -10.428  1.00 61.40           O  
-ATOM   2818  CB  VAL B 110     -39.429  49.399  -7.572  1.00 61.90           C  
-ATOM   2819  CG1 VAL B 110     -40.158  49.902  -6.339  1.00 61.62           C  
-ATOM   2820  CG2 VAL B 110     -37.948  49.210  -7.273  1.00 61.46           C  
-ATOM   2821  N   GLY B 111     -38.622  46.804  -9.555  1.00 61.95           N  
-ATOM   2822  CA  GLY B 111     -38.054  46.449 -10.844  1.00 62.27           C  
-ATOM   2823  C   GLY B 111     -36.907  47.365 -11.228  1.00 63.06           C  
-ATOM   2824  O   GLY B 111     -35.825  47.305 -10.638  1.00 62.88           O  
-ATOM   2825  N   ASN B 112     -37.145  48.219 -12.219  1.00 64.00           N  
-ATOM   2826  CA  ASN B 112     -36.137  49.164 -12.689  1.00 64.82           C  
-ATOM   2827  C   ASN B 112     -36.637  50.599 -12.521  1.00 64.87           C  
-ATOM   2828  O   ASN B 112     -36.049  51.528 -13.077  1.00 65.80           O  
-ATOM   2829  CB  ASN B 112     -35.828  48.913 -14.164  1.00 66.47           C  
-ATOM   2830  CG  ASN B 112     -37.000  49.268 -15.073  1.00 68.98           C  
-ATOM   2831  OD1 ASN B 112     -38.128  48.804 -14.864  1.00 70.29           O  
-ATOM   2832  ND2 ASN B 112     -36.739  50.093 -16.087  1.00 68.64           N  
-ATOM   2833  N   THR B 113     -37.729  50.777 -11.772  1.00 64.11           N  
-ATOM   2834  CA  THR B 113     -38.301  52.107 -11.533  1.00 61.87           C  
-ATOM   2835  C   THR B 113     -37.435  52.947 -10.578  1.00 59.44           C  
-ATOM   2836  O   THR B 113     -36.799  52.424  -9.657  1.00 59.25           O  
-ATOM   2837  CB  THR B 113     -39.757  52.017 -10.973  1.00 61.83           C  
-ATOM   2838  OG1 THR B 113     -39.842  50.952 -10.022  1.00 62.97           O  
-ATOM   2839  CG2 THR B 113     -40.760  51.763 -12.093  1.00 60.76           C  
-ATOM   2840  N   PRO B 114     -37.401  54.267 -10.798  1.00 57.06           N  
-ATOM   2841  CA  PRO B 114     -36.626  55.217  -9.994  1.00 56.15           C  
-ATOM   2842  C   PRO B 114     -37.235  55.467  -8.615  1.00 54.56           C  
-ATOM   2843  O   PRO B 114     -38.423  55.796  -8.509  1.00 55.53           O  
-ATOM   2844  CB  PRO B 114     -36.648  56.494 -10.843  1.00 56.52           C  
-ATOM   2845  CG  PRO B 114     -37.131  56.043 -12.204  1.00 56.41           C  
-ATOM   2846  CD  PRO B 114     -38.108  54.971 -11.875  1.00 56.35           C  
-ATOM   2847  N   VAL B 115     -36.432  55.328  -7.563  1.00 51.08           N  
-ATOM   2848  CA  VAL B 115     -36.951  55.569  -6.222  1.00 48.01           C  
-ATOM   2849  C   VAL B 115     -36.297  56.771  -5.531  1.00 47.13           C  
-ATOM   2850  O   VAL B 115     -35.087  56.988  -5.614  1.00 47.38           O  
-ATOM   2851  CB  VAL B 115     -36.812  54.317  -5.312  1.00 45.40           C  
-ATOM   2852  CG1 VAL B 115     -37.299  53.089  -6.049  1.00 44.40           C  
-ATOM   2853  CG2 VAL B 115     -35.389  54.147  -4.848  1.00 43.82           C  
-ATOM   2854  N   PHE B 116     -37.121  57.566  -4.862  1.00 44.94           N  
-ATOM   2855  CA  PHE B 116     -36.639  58.729  -4.146  1.00 42.58           C  
-ATOM   2856  C   PHE B 116     -37.043  58.549  -2.688  1.00 40.52           C  
-ATOM   2857  O   PHE B 116     -38.224  58.428  -2.383  1.00 41.90           O  
-ATOM   2858  CB  PHE B 116     -37.272  60.004  -4.712  1.00 43.18           C  
-ATOM   2859  CG  PHE B 116     -36.971  60.249  -6.174  1.00 44.69           C  
-ATOM   2860  CD1 PHE B 116     -37.353  59.330  -7.148  1.00 45.20           C  
-ATOM   2861  CD2 PHE B 116     -36.345  61.430  -6.583  1.00 45.91           C  
-ATOM   2862  CE1 PHE B 116     -37.122  59.585  -8.505  1.00 46.18           C  
-ATOM   2863  CE2 PHE B 116     -36.108  61.696  -7.938  1.00 45.40           C  
-ATOM   2864  CZ  PHE B 116     -36.500  60.772  -8.899  1.00 45.48           C  
-ATOM   2865  N   ALA B 117     -36.064  58.507  -1.792  1.00 37.50           N  
-ATOM   2866  CA  ALA B 117     -36.335  58.353  -0.371  1.00 35.21           C  
-ATOM   2867  C   ALA B 117     -36.833  59.681   0.221  1.00 34.93           C  
-ATOM   2868  O   ALA B 117     -36.478  60.760  -0.270  1.00 34.63           O  
-ATOM   2869  CB  ALA B 117     -35.074  57.895   0.344  1.00 33.99           C  
-ATOM   2870  N   THR B 118     -37.664  59.582   1.262  1.00 33.89           N  
-ATOM   2871  CA  THR B 118     -38.235  60.737   1.957  1.00 32.15           C  
-ATOM   2872  C   THR B 118     -38.247  60.494   3.443  1.00 32.95           C  
-ATOM   2873  O   THR B 118     -38.408  59.371   3.892  1.00 32.44           O  
-ATOM   2874  CB  THR B 118     -39.697  60.974   1.614  1.00 30.70           C  
-ATOM   2875  OG1 THR B 118     -40.141  59.955   0.719  1.00 32.11           O  
-ATOM   2876  CG2 THR B 118     -39.896  62.344   1.024  1.00 27.20           C  
-ATOM   2877  N   VAL B 119     -38.117  61.571   4.201  1.00 34.11           N  
-ATOM   2878  CA  VAL B 119     -38.138  61.498   5.649  1.00 34.82           C  
-ATOM   2879  C   VAL B 119     -37.154  60.495   6.235  1.00 36.71           C  
-ATOM   2880  O   VAL B 119     -36.185  60.875   6.888  1.00 37.03           O  
-ATOM   2881  CB  VAL B 119     -39.541  61.146   6.141  1.00 33.32           C  
-ATOM   2882  CG1 VAL B 119     -39.529  60.970   7.647  1.00 33.97           C  
-ATOM   2883  CG2 VAL B 119     -40.515  62.240   5.731  1.00 31.56           C  
-ATOM   2884  N   ASN B 120     -37.397  59.215   5.993  1.00 39.33           N  
-ATOM   2885  CA  ASN B 120     -36.550  58.168   6.541  1.00 42.88           C  
-ATOM   2886  C   ASN B 120     -35.410  57.710   5.655  1.00 45.73           C  
-ATOM   2887  O   ASN B 120     -35.548  57.622   4.435  1.00 45.76           O  
-ATOM   2888  CB  ASN B 120     -37.400  56.957   6.899  1.00 42.50           C  
-ATOM   2889  CG  ASN B 120     -38.600  57.325   7.732  1.00 42.40           C  
-ATOM   2890  OD1 ASN B 120     -39.719  56.925   7.419  1.00 42.43           O  
-ATOM   2891  ND2 ASN B 120     -38.379  58.096   8.799  1.00 41.56           N  
-ATOM   2892  N   GLN B 121     -34.290  57.401   6.304  1.00 49.18           N  
-ATOM   2893  CA  GLN B 121     -33.088  56.923   5.641  1.00 51.55           C  
-ATOM   2894  C   GLN B 121     -33.357  55.558   5.037  1.00 52.67           C  
-ATOM   2895  O   GLN B 121     -33.742  54.623   5.748  1.00 53.14           O  
-ATOM   2896  CB  GLN B 121     -31.945  56.827   6.658  1.00 52.33           C  
-ATOM   2897  CG  GLN B 121     -30.714  56.039   6.211  1.00 55.95           C  
-ATOM   2898  CD  GLN B 121     -30.024  56.615   4.976  1.00 58.21           C  
-ATOM   2899  OE1 GLN B 121     -29.647  57.793   4.943  1.00 59.65           O  
-ATOM   2900  NE2 GLN B 121     -29.847  55.776   3.956  1.00 58.12           N  
-ATOM   2901  N   LEU B 122     -33.166  55.460   3.721  1.00 53.73           N  
-ATOM   2902  CA  LEU B 122     -33.360  54.213   2.978  1.00 54.35           C  
-ATOM   2903  C   LEU B 122     -32.011  53.769   2.453  1.00 56.05           C  
-ATOM   2904  O   LEU B 122     -31.621  54.172   1.363  1.00 57.40           O  
-ATOM   2905  CB  LEU B 122     -34.297  54.431   1.779  1.00 51.08           C  
-ATOM   2906  CG  LEU B 122     -34.336  53.300   0.741  1.00 48.36           C  
-ATOM   2907  CD1 LEU B 122     -34.716  51.989   1.419  1.00 47.92           C  
-ATOM   2908  CD2 LEU B 122     -35.315  53.636  -0.362  1.00 46.60           C  
-ATOM   2909  N   ASP B 123     -31.281  52.956   3.204  1.00 57.60           N  
-ATOM   2910  CA  ASP B 123     -29.989  52.534   2.688  1.00 59.65           C  
-ATOM   2911  C   ASP B 123     -30.055  51.187   1.969  1.00 60.36           C  
-ATOM   2912  O   ASP B 123     -30.706  50.241   2.418  1.00 58.54           O  
-ATOM   2913  CB  ASP B 123     -28.911  52.565   3.793  1.00 59.55           C  
-ATOM   2914  CG  ASP B 123     -29.351  51.891   5.068  1.00 59.33           C  
-ATOM   2915  OD1 ASP B 123     -28.950  52.361   6.157  1.00 58.40           O  
-ATOM   2916  OD2 ASP B 123     -30.081  50.884   4.981  1.00 60.22           O  
-ATOM   2917  N   LEU B 124     -29.389  51.145   0.820  1.00 62.91           N  
-ATOM   2918  CA  LEU B 124     -29.358  49.972  -0.040  1.00 65.85           C  
-ATOM   2919  C   LEU B 124     -27.923  49.574  -0.386  1.00 68.62           C  
-ATOM   2920  O   LEU B 124     -27.003  50.407  -0.351  1.00 69.22           O  
-ATOM   2921  CB  LEU B 124     -30.115  50.280  -1.332  1.00 64.03           C  
-ATOM   2922  CG  LEU B 124     -31.454  50.996  -1.160  1.00 62.50           C  
-ATOM   2923  CD1 LEU B 124     -31.907  51.558  -2.487  1.00 60.31           C  
-ATOM   2924  CD2 LEU B 124     -32.479  50.032  -0.586  1.00 63.05           C  
-ATOM   2925  N   ASP B 125     -27.737  48.299  -0.725  1.00 70.91           N  
-ATOM   2926  CA  ASP B 125     -26.418  47.811  -1.093  1.00 72.56           C  
-ATOM   2927  C   ASP B 125     -26.070  48.418  -2.441  1.00 73.94           C  
-ATOM   2928  O   ASP B 125     -26.950  48.865  -3.179  1.00 73.74           O  
-ATOM   2929  CB  ASP B 125     -26.392  46.274  -1.182  1.00 71.97           C  
-ATOM   2930  CG  ASP B 125     -27.214  45.729  -2.343  1.00 72.18           C  
-ATOM   2931  OD1 ASP B 125     -27.026  46.195  -3.486  1.00 71.37           O  
-ATOM   2932  OD2 ASP B 125     -28.040  44.818  -2.113  1.00 71.79           O  
-ATOM   2933  N   GLU B 126     -24.779  48.435  -2.747  1.00 76.06           N  
-ATOM   2934  CA  GLU B 126     -24.260  48.985  -3.995  1.00 77.39           C  
-ATOM   2935  C   GLU B 126     -25.013  48.524  -5.248  1.00 75.95           C  
-ATOM   2936  O   GLU B 126     -25.173  49.295  -6.197  1.00 75.18           O  
-ATOM   2937  CB  GLU B 126     -22.768  48.639  -4.120  1.00 80.56           C  
-ATOM   2938  CG  GLU B 126     -22.429  47.135  -4.013  1.00 85.34           C  
-ATOM   2939  CD  GLU B 126     -22.751  46.516  -2.643  1.00 87.41           C  
-ATOM   2940  OE1 GLU B 126     -22.226  47.007  -1.617  1.00 87.92           O  
-ATOM   2941  OE2 GLU B 126     -23.527  45.530  -2.596  1.00 88.45           O  
-ATOM   2942  N   GLU B 127     -25.478  47.277  -5.242  1.00 74.63           N  
-ATOM   2943  CA  GLU B 127     -26.201  46.716  -6.383  1.00 74.29           C  
-ATOM   2944  C   GLU B 127     -27.598  47.324  -6.490  1.00 72.51           C  
-ATOM   2945  O   GLU B 127     -28.108  47.567  -7.587  1.00 71.70           O  
-ATOM   2946  CB  GLU B 127     -26.308  45.189  -6.237  1.00 76.60           C  
-ATOM   2947  CG  GLU B 127     -26.400  44.402  -7.558  1.00 80.12           C  
-ATOM   2948  CD  GLU B 127     -27.738  44.556  -8.274  1.00 82.06           C  
-ATOM   2949  OE1 GLU B 127     -27.878  44.047  -9.411  1.00 82.68           O  
-ATOM   2950  OE2 GLU B 127     -28.655  45.179  -7.702  1.00 83.81           O  
-ATOM   2951  N   GLN B 128     -28.209  47.576  -5.339  1.00 70.79           N  
-ATOM   2952  CA  GLN B 128     -29.551  48.138  -5.290  1.00 67.59           C  
-ATOM   2953  C   GLN B 128     -29.561  49.669  -5.361  1.00 65.67           C  
-ATOM   2954  O   GLN B 128     -30.565  50.270  -5.754  1.00 64.67           O  
-ATOM   2955  CB  GLN B 128     -30.240  47.674  -4.008  1.00 67.17           C  
-ATOM   2956  CG  GLN B 128     -31.669  47.208  -4.211  1.00 67.20           C  
-ATOM   2957  CD  GLN B 128     -31.757  45.864  -4.901  1.00 65.52           C  
-ATOM   2958  OE1 GLN B 128     -31.294  44.858  -4.375  1.00 65.87           O  
-ATOM   2959  NE2 GLN B 128     -32.354  45.841  -6.080  1.00 64.25           N  
-ATOM   2960  N   SER B 129     -28.443  50.292  -4.985  1.00 63.45           N  
-ATOM   2961  CA  SER B 129     -28.325  51.751  -4.993  1.00 61.38           C  
-ATOM   2962  C   SER B 129     -28.462  52.346  -6.397  1.00 60.24           C  
-ATOM   2963  O   SER B 129     -28.360  53.560  -6.586  1.00 59.82           O  
-ATOM   2964  CB  SER B 129     -26.986  52.183  -4.371  1.00 60.65           C  
-ATOM   2965  OG  SER B 129     -26.916  51.874  -2.986  1.00 58.63           O  
-ATOM   2966  N   THR B 130     -28.702  51.482  -7.376  1.00 58.98           N  
-ATOM   2967  CA  THR B 130     -28.860  51.901  -8.768  1.00 57.77           C  
-ATOM   2968  C   THR B 130     -30.080  52.779  -8.959  1.00 57.02           C  
-ATOM   2969  O   THR B 130     -30.070  53.700  -9.777  1.00 57.18           O  
-ATOM   2970  CB  THR B 130     -29.063  50.693  -9.692  1.00 57.45           C  
-ATOM   2971  OG1 THR B 130     -27.980  49.778  -9.520  1.00 58.25           O  
-ATOM   2972  CG2 THR B 130     -29.152  51.136 -11.147  1.00 55.79           C  
-ATOM   2973  N   LEU B 131     -31.128  52.470  -8.197  1.00 55.52           N  
-ATOM   2974  CA  LEU B 131     -32.413  53.157  -8.278  1.00 53.23           C  
-ATOM   2975  C   LEU B 131     -32.540  54.510  -7.560  1.00 52.07           C  
-ATOM   2976  O   LEU B 131     -33.343  55.353  -7.967  1.00 51.36           O  
-ATOM   2977  CB  LEU B 131     -33.495  52.196  -7.786  1.00 52.02           C  
-ATOM   2978  CG  LEU B 131     -33.459  50.823  -8.468  1.00 50.30           C  
-ATOM   2979  CD1 LEU B 131     -34.028  49.762  -7.545  1.00 49.72           C  
-ATOM   2980  CD2 LEU B 131     -34.227  50.883  -9.774  1.00 49.32           C  
-ATOM   2981  N   LEU B 132     -31.747  54.715  -6.510  1.00 50.08           N  
-ATOM   2982  CA  LEU B 132     -31.770  55.953  -5.725  1.00 48.57           C  
-ATOM   2983  C   LEU B 132     -31.495  57.225  -6.533  1.00 48.25           C  
-ATOM   2984  O   LEU B 132     -30.357  57.670  -6.615  1.00 50.32           O  
-ATOM   2985  CB  LEU B 132     -30.737  55.866  -4.593  1.00 47.22           C  
-ATOM   2986  CG  LEU B 132     -31.176  56.002  -3.133  1.00 45.81           C  
-ATOM   2987  CD1 LEU B 132     -31.926  57.297  -2.926  1.00 45.64           C  
-ATOM   2988  CD2 LEU B 132     -32.050  54.829  -2.769  1.00 46.54           C  
-ATOM   2989  N   LYS B 133     -32.519  57.835  -7.111  1.00 47.39           N  
-ATOM   2990  CA  LYS B 133     -32.283  59.052  -7.873  1.00 47.33           C  
-ATOM   2991  C   LYS B 133     -32.309  60.297  -6.991  1.00 47.02           C  
-ATOM   2992  O   LYS B 133     -31.935  61.383  -7.436  1.00 47.15           O  
-ATOM   2993  CB  LYS B 133     -33.308  59.191  -9.006  1.00 48.14           C  
-ATOM   2994  CG  LYS B 133     -33.350  57.990  -9.949  1.00 49.32           C  
-ATOM   2995  CD  LYS B 133     -31.951  57.530 -10.353  1.00 49.67           C  
-ATOM   2996  CE  LYS B 133     -31.988  56.257 -11.197  1.00 50.06           C  
-ATOM   2997  NZ  LYS B 133     -30.614  55.819 -11.584  1.00 50.88           N  
-ATOM   2998  N   GLY B 134     -32.744  60.140  -5.742  1.00 46.49           N  
-ATOM   2999  CA  GLY B 134     -32.798  61.276  -4.833  1.00 45.78           C  
-ATOM   3000  C   GLY B 134     -33.151  60.942  -3.392  1.00 45.36           C  
-ATOM   3001  O   GLY B 134     -33.694  59.878  -3.108  1.00 45.92           O  
-ATOM   3002  N   GLU B 135     -32.822  61.846  -2.473  1.00 44.72           N  
-ATOM   3003  CA  GLU B 135     -33.132  61.652  -1.061  1.00 43.98           C  
-ATOM   3004  C   GLU B 135     -33.484  62.977  -0.428  1.00 43.14           C  
-ATOM   3005  O   GLU B 135     -32.807  63.975  -0.651  1.00 44.24           O  
-ATOM   3006  CB  GLU B 135     -31.950  61.082  -0.296  1.00 44.21           C  
-ATOM   3007  CG  GLU B 135     -31.487  59.737  -0.762  1.00 51.07           C  
-ATOM   3008  CD  GLU B 135     -30.393  59.165   0.135  1.00 56.33           C  
-ATOM   3009  OE1 GLU B 135     -29.644  59.963   0.756  1.00 58.13           O  
-ATOM   3010  OE2 GLU B 135     -30.273  57.917   0.211  1.00 58.24           O  
-ATOM   3011  N   VAL B 136     -34.560  62.989   0.345  1.00 41.51           N  
-ATOM   3012  CA  VAL B 136     -34.973  64.184   1.061  1.00 39.67           C  
-ATOM   3013  C   VAL B 136     -35.079  63.726   2.501  1.00 40.72           C  
-ATOM   3014  O   VAL B 136     -35.663  62.682   2.775  1.00 40.98           O  
-ATOM   3015  CB  VAL B 136     -36.335  64.697   0.600  1.00 37.74           C  
-ATOM   3016  CG1 VAL B 136     -36.820  65.771   1.551  1.00 36.27           C  
-ATOM   3017  CG2 VAL B 136     -36.232  65.248  -0.806  1.00 35.53           C  
-ATOM   3018  N   GLY B 137     -34.495  64.485   3.417  1.00 41.39           N  
-ATOM   3019  CA  GLY B 137     -34.544  64.101   4.812  1.00 43.05           C  
-ATOM   3020  C   GLY B 137     -33.851  65.120   5.686  1.00 44.06           C  
-ATOM   3021  O   GLY B 137     -33.525  66.207   5.224  1.00 45.69           O  
-ATOM   3022  N   VAL B 138     -33.641  64.775   6.951  1.00 43.93           N  
-ATOM   3023  CA  VAL B 138     -32.976  65.650   7.906  1.00 43.28           C  
-ATOM   3024  C   VAL B 138     -32.299  64.735   8.889  1.00 44.78           C  
-ATOM   3025  O   VAL B 138     -32.806  63.656   9.180  1.00 46.90           O  
-ATOM   3026  CB  VAL B 138     -33.973  66.528   8.673  1.00 42.23           C  
-ATOM   3027  CG1 VAL B 138     -33.324  67.087   9.910  1.00 41.75           C  
-ATOM   3028  CG2 VAL B 138     -34.436  67.669   7.795  1.00 42.65           C  
-ATOM   3029  N   ASP B 139     -31.146  65.147   9.391  1.00 45.48           N  
-ATOM   3030  CA  ASP B 139     -30.426  64.331  10.350  1.00 45.53           C  
-ATOM   3031  C   ASP B 139     -31.068  64.575  11.697  1.00 45.36           C  
-ATOM   3032  O   ASP B 139     -30.883  65.640  12.276  1.00 46.84           O  
-ATOM   3033  CB  ASP B 139     -28.975  64.759  10.408  1.00 47.57           C  
-ATOM   3034  CG  ASP B 139     -28.121  63.765  11.129  1.00 50.97           C  
-ATOM   3035  OD1 ASP B 139     -28.522  63.320  12.228  1.00 52.16           O  
-ATOM   3036  OD2 ASP B 139     -27.046  63.427  10.594  1.00 54.79           O  
-ATOM   3037  N   TRP B 140     -31.808  63.601  12.215  1.00 45.00           N  
-ATOM   3038  CA  TRP B 140     -32.483  63.797  13.497  1.00 44.65           C  
-ATOM   3039  C   TRP B 140     -31.600  64.047  14.705  1.00 42.89           C  
-ATOM   3040  O   TRP B 140     -32.093  64.391  15.775  1.00 42.46           O  
-ATOM   3041  CB  TRP B 140     -33.452  62.651  13.765  1.00 47.55           C  
-ATOM   3042  CG  TRP B 140     -34.734  62.886  13.050  1.00 50.45           C  
-ATOM   3043  CD1 TRP B 140     -34.913  62.971  11.699  1.00 51.87           C  
-ATOM   3044  CD2 TRP B 140     -35.992  63.202  13.643  1.00 50.96           C  
-ATOM   3045  NE1 TRP B 140     -36.202  63.333  11.415  1.00 52.87           N  
-ATOM   3046  CE2 TRP B 140     -36.889  63.480  12.589  1.00 51.94           C  
-ATOM   3047  CE3 TRP B 140     -36.449  63.280  14.961  1.00 51.65           C  
-ATOM   3048  CZ2 TRP B 140     -38.217  63.832  12.814  1.00 51.36           C  
-ATOM   3049  CZ3 TRP B 140     -37.766  63.629  15.186  1.00 52.84           C  
-ATOM   3050  CH2 TRP B 140     -38.637  63.902  14.114  1.00 52.63           C  
-ATOM   3051  N   TYR B 141     -30.296  63.870  14.532  1.00 41.36           N  
-ATOM   3052  CA  TYR B 141     -29.348  64.140  15.596  1.00 39.20           C  
-ATOM   3053  C   TYR B 141     -29.518  65.636  15.886  1.00 38.80           C  
-ATOM   3054  O   TYR B 141     -29.606  66.052  17.044  1.00 39.00           O  
-ATOM   3055  CB  TYR B 141     -27.927  63.837  15.099  1.00 38.71           C  
-ATOM   3056  CG  TYR B 141     -26.804  64.508  15.872  1.00 40.03           C  
-ATOM   3057  CD1 TYR B 141     -26.109  63.829  16.876  1.00 39.86           C  
-ATOM   3058  CD2 TYR B 141     -26.435  65.828  15.593  1.00 40.79           C  
-ATOM   3059  CE1 TYR B 141     -25.069  64.451  17.583  1.00 41.11           C  
-ATOM   3060  CE2 TYR B 141     -25.405  66.461  16.292  1.00 42.05           C  
-ATOM   3061  CZ  TYR B 141     -24.721  65.770  17.283  1.00 43.01           C  
-ATOM   3062  OH  TYR B 141     -23.680  66.396  17.946  1.00 43.20           O  
-ATOM   3063  N   TRP B 142     -29.597  66.431  14.818  1.00 36.87           N  
-ATOM   3064  CA  TRP B 142     -29.741  67.877  14.921  1.00 36.18           C  
-ATOM   3065  C   TRP B 142     -31.059  68.340  15.503  1.00 35.73           C  
-ATOM   3066  O   TRP B 142     -31.161  69.461  16.001  1.00 36.35           O  
-ATOM   3067  CB  TRP B 142     -29.529  68.517  13.556  1.00 38.68           C  
-ATOM   3068  CG  TRP B 142     -28.111  68.423  13.121  1.00 42.82           C  
-ATOM   3069  CD1 TRP B 142     -27.613  67.713  12.061  1.00 44.38           C  
-ATOM   3070  CD2 TRP B 142     -26.983  69.020  13.769  1.00 44.42           C  
-ATOM   3071  NE1 TRP B 142     -26.240  67.831  12.013  1.00 44.00           N  
-ATOM   3072  CE2 TRP B 142     -25.830  68.628  13.051  1.00 43.76           C  
-ATOM   3073  CE3 TRP B 142     -26.833  69.847  14.891  1.00 45.72           C  
-ATOM   3074  CZ2 TRP B 142     -24.550  69.036  13.419  1.00 43.61           C  
-ATOM   3075  CZ3 TRP B 142     -25.556  70.251  15.255  1.00 45.25           C  
-ATOM   3076  CH2 TRP B 142     -24.433  69.844  14.520  1.00 44.41           C  
-ATOM   3077  N   MET B 143     -32.073  67.487  15.426  1.00 34.88           N  
-ATOM   3078  CA  MET B 143     -33.381  67.808  15.986  1.00 32.03           C  
-ATOM   3079  C   MET B 143     -33.236  67.768  17.498  1.00 29.79           C  
-ATOM   3080  O   MET B 143     -33.616  68.704  18.194  1.00 29.21           O  
-ATOM   3081  CB  MET B 143     -34.414  66.784  15.531  1.00 32.20           C  
-ATOM   3082  CG  MET B 143     -34.900  67.001  14.112  1.00 33.69           C  
-ATOM   3083  SD  MET B 143     -36.286  68.159  14.031  1.00 35.97           S  
-ATOM   3084  CE  MET B 143     -35.516  69.632  13.693  1.00 35.21           C  
-ATOM   3085  N   GLY B 144     -32.668  66.678  17.997  1.00 27.75           N  
-ATOM   3086  CA  GLY B 144     -32.463  66.546  19.422  1.00 27.33           C  
-ATOM   3087  C   GLY B 144     -31.454  67.562  19.912  1.00 27.48           C  
-ATOM   3088  O   GLY B 144     -31.576  68.096  21.012  1.00 28.11           O  
-ATOM   3089  N   TYR B 145     -30.450  67.836  19.091  1.00 27.94           N  
-ATOM   3090  CA  TYR B 145     -29.421  68.800  19.455  1.00 30.18           C  
-ATOM   3091  C   TYR B 145     -30.051  70.161  19.756  1.00 30.04           C  
-ATOM   3092  O   TYR B 145     -29.794  70.774  20.801  1.00 30.34           O  
-ATOM   3093  CB  TYR B 145     -28.409  68.936  18.308  1.00 33.36           C  
-ATOM   3094  CG  TYR B 145     -27.186  69.766  18.649  1.00 35.78           C  
-ATOM   3095  CD1 TYR B 145     -27.229  71.162  18.615  1.00 36.28           C  
-ATOM   3096  CD2 TYR B 145     -25.997  69.154  19.038  1.00 35.89           C  
-ATOM   3097  CE1 TYR B 145     -26.119  71.927  18.959  1.00 36.75           C  
-ATOM   3098  CE2 TYR B 145     -24.885  69.909  19.388  1.00 37.76           C  
-ATOM   3099  CZ  TYR B 145     -24.949  71.293  19.348  1.00 37.37           C  
-ATOM   3100  OH  TYR B 145     -23.847  72.038  19.708  1.00 37.34           O  
-ATOM   3101  N   GLU B 146     -30.878  70.618  18.821  1.00 28.87           N  
-ATOM   3102  CA  GLU B 146     -31.567  71.895  18.917  1.00 26.24           C  
-ATOM   3103  C   GLU B 146     -32.361  72.007  20.219  1.00 25.25           C  
-ATOM   3104  O   GLU B 146     -32.347  73.045  20.873  1.00 23.58           O  
-ATOM   3105  CB  GLU B 146     -32.489  72.039  17.712  1.00 25.65           C  
-ATOM   3106  CG  GLU B 146     -32.818  73.467  17.318  1.00 27.23           C  
-ATOM   3107  CD  GLU B 146     -31.639  74.193  16.714  1.00 26.47           C  
-ATOM   3108  OE1 GLU B 146     -30.920  73.571  15.908  1.00 26.26           O  
-ATOM   3109  OE2 GLU B 146     -31.441  75.387  17.031  1.00 27.19           O  
-ATOM   3110  N   ALA B 147     -33.056  70.933  20.588  1.00 25.97           N  
-ATOM   3111  CA  ALA B 147     -33.849  70.913  21.818  1.00 26.10           C  
-ATOM   3112  C   ALA B 147     -32.884  70.990  22.980  1.00 26.45           C  
-ATOM   3113  O   ALA B 147     -33.121  71.711  23.962  1.00 25.91           O  
-ATOM   3114  CB  ALA B 147     -34.667  69.635  21.908  1.00 24.38           C  
-ATOM   3115  N   GLY B 148     -31.795  70.231  22.854  1.00 25.34           N  
-ATOM   3116  CA  GLY B 148     -30.775  70.216  23.882  1.00 23.13           C  
-ATOM   3117  C   GLY B 148     -30.228  71.615  24.071  1.00 21.97           C  
-ATOM   3118  O   GLY B 148     -30.199  72.129  25.189  1.00 21.54           O  
-ATOM   3119  N   LYS B 149     -29.809  72.237  22.971  1.00 21.04           N  
-ATOM   3120  CA  LYS B 149     -29.257  73.583  23.022  1.00 21.04           C  
-ATOM   3121  C   LYS B 149     -30.206  74.559  23.730  1.00 21.27           C  
-ATOM   3122  O   LYS B 149     -29.770  75.419  24.502  1.00 19.98           O  
-ATOM   3123  CB  LYS B 149     -28.955  74.108  21.612  1.00 19.96           C  
-ATOM   3124  CG  LYS B 149     -28.255  75.458  21.651  1.00 20.64           C  
-ATOM   3125  CD  LYS B 149     -28.590  76.358  20.484  1.00 22.17           C  
-ATOM   3126  CE  LYS B 149     -28.067  75.812  19.169  1.00 25.92           C  
-ATOM   3127  NZ  LYS B 149     -28.306  76.786  18.052  1.00 27.71           N  
-ATOM   3128  N   TYR B 150     -31.502  74.437  23.468  1.00 21.87           N  
-ATOM   3129  CA  TYR B 150     -32.448  75.336  24.114  1.00 23.37           C  
-ATOM   3130  C   TYR B 150     -32.266  75.251  25.627  1.00 23.88           C  
-ATOM   3131  O   TYR B 150     -32.072  76.258  26.300  1.00 23.38           O  
-ATOM   3132  CB  TYR B 150     -33.897  74.976  23.763  1.00 22.42           C  
-ATOM   3133  CG  TYR B 150     -34.910  75.726  24.613  1.00 21.75           C  
-ATOM   3134  CD1 TYR B 150     -35.209  77.056  24.357  1.00 22.47           C  
-ATOM   3135  CD2 TYR B 150     -35.543  75.108  25.694  1.00 21.78           C  
-ATOM   3136  CE1 TYR B 150     -36.117  77.760  25.150  1.00 23.60           C  
-ATOM   3137  CE2 TYR B 150     -36.451  75.801  26.495  1.00 21.79           C  
-ATOM   3138  CZ  TYR B 150     -36.734  77.126  26.212  1.00 23.15           C  
-ATOM   3139  OH  TYR B 150     -37.650  77.817  26.966  1.00 23.63           O  
-ATOM   3140  N   LEU B 151     -32.333  74.036  26.153  1.00 24.22           N  
-ATOM   3141  CA  LEU B 151     -32.192  73.840  27.575  1.00 24.85           C  
-ATOM   3142  C   LEU B 151     -30.830  74.276  28.096  1.00 27.15           C  
-ATOM   3143  O   LEU B 151     -30.736  74.899  29.152  1.00 28.51           O  
-ATOM   3144  CB  LEU B 151     -32.462  72.381  27.914  1.00 23.78           C  
-ATOM   3145  CG  LEU B 151     -33.946  72.045  28.043  1.00 22.71           C  
-ATOM   3146  CD1 LEU B 151     -34.114  70.593  28.461  1.00 20.60           C  
-ATOM   3147  CD2 LEU B 151     -34.573  72.977  29.067  1.00 20.40           C  
-ATOM   3148  N   ALA B 152     -29.775  73.963  27.354  1.00 28.39           N  
-ATOM   3149  CA  ALA B 152     -28.430  74.334  27.765  1.00 29.16           C  
-ATOM   3150  C   ALA B 152     -28.278  75.846  27.980  1.00 31.31           C  
-ATOM   3151  O   ALA B 152     -27.763  76.284  29.007  1.00 33.04           O  
-ATOM   3152  CB  ALA B 152     -27.437  73.855  26.741  1.00 28.37           C  
-ATOM   3153  N   GLU B 153     -28.722  76.654  27.029  1.00 32.36           N  
-ATOM   3154  CA  GLU B 153     -28.583  78.094  27.191  1.00 34.24           C  
-ATOM   3155  C   GLU B 153     -29.499  78.605  28.288  1.00 35.42           C  
-ATOM   3156  O   GLU B 153     -29.303  79.690  28.825  1.00 36.47           O  
-ATOM   3157  CB  GLU B 153     -28.926  78.819  25.893  1.00 35.95           C  
-ATOM   3158  CG  GLU B 153     -28.374  78.161  24.657  1.00 40.19           C  
-ATOM   3159  CD  GLU B 153     -28.419  79.076  23.444  1.00 44.56           C  
-ATOM   3160  OE1 GLU B 153     -29.437  79.800  23.258  1.00 45.34           O  
-ATOM   3161  OE2 GLU B 153     -27.431  79.057  22.674  1.00 45.42           O  
-ATOM   3162  N   ARG B 154     -30.514  77.823  28.615  1.00 36.22           N  
-ATOM   3163  CA  ARG B 154     -31.467  78.231  29.629  1.00 36.50           C  
-ATOM   3164  C   ARG B 154     -30.825  77.992  30.982  1.00 36.63           C  
-ATOM   3165  O   ARG B 154     -31.134  78.675  31.953  1.00 36.60           O  
-ATOM   3166  CB  ARG B 154     -32.745  77.399  29.484  1.00 37.43           C  
-ATOM   3167  CG  ARG B 154     -33.964  77.870  30.272  1.00 37.81           C  
-ATOM   3168  CD  ARG B 154     -34.829  78.828  29.461  1.00 39.01           C  
-ATOM   3169  NE  ARG B 154     -36.264  78.526  29.553  1.00 39.19           N  
-ATOM   3170  CZ  ARG B 154     -36.966  78.480  30.683  1.00 37.97           C  
-ATOM   3171  NH1 ARG B 154     -36.377  78.710  31.845  1.00 40.04           N  
-ATOM   3172  NH2 ARG B 154     -38.266  78.222  30.654  1.00 36.73           N  
-ATOM   3173  N   HIS B 155     -29.910  77.029  31.032  1.00 36.29           N  
-ATOM   3174  CA  HIS B 155     -29.237  76.674  32.276  1.00 36.75           C  
-ATOM   3175  C   HIS B 155     -27.774  76.354  32.034  1.00 36.60           C  
-ATOM   3176  O   HIS B 155     -27.400  75.193  31.993  1.00 36.22           O  
-ATOM   3177  CB  HIS B 155     -29.904  75.439  32.894  1.00 37.59           C  
-ATOM   3178  CG  HIS B 155     -31.376  75.590  33.120  1.00 38.34           C  
-ATOM   3179  ND1 HIS B 155     -31.900  76.371  34.129  1.00 38.61           N  
-ATOM   3180  CD2 HIS B 155     -32.437  75.081  32.450  1.00 38.21           C  
-ATOM   3181  CE1 HIS B 155     -33.220  76.339  34.068  1.00 37.61           C  
-ATOM   3182  NE2 HIS B 155     -33.571  75.565  33.058  1.00 38.22           N  
-ATOM   3183  N   PRO B 156     -26.923  77.373  31.887  1.00 37.09           N  
-ATOM   3184  CA  PRO B 156     -25.495  77.132  31.648  1.00 38.76           C  
-ATOM   3185  C   PRO B 156     -24.793  76.509  32.864  1.00 41.19           C  
-ATOM   3186  O   PRO B 156     -25.387  76.398  33.936  1.00 41.93           O  
-ATOM   3187  CB  PRO B 156     -24.957  78.527  31.335  1.00 39.06           C  
-ATOM   3188  CG  PRO B 156     -26.178  79.318  30.934  1.00 38.15           C  
-ATOM   3189  CD  PRO B 156     -27.222  78.810  31.875  1.00 36.80           C  
-ATOM   3190  N   LYS B 157     -23.530  76.114  32.691  1.00 43.51           N  
-ATOM   3191  CA  LYS B 157     -22.722  75.512  33.768  1.00 45.35           C  
-ATOM   3192  C   LYS B 157     -22.605  76.424  34.992  1.00 45.68           C  
-ATOM   3193  O   LYS B 157     -22.144  77.568  34.887  1.00 47.26           O  
-ATOM   3194  CB  LYS B 157     -21.298  75.216  33.269  1.00 46.80           C  
-ATOM   3195  CG  LYS B 157     -20.796  73.789  33.464  1.00 48.27           C  
-ATOM   3196  CD  LYS B 157     -20.898  73.323  34.905  1.00 50.29           C  
-ATOM   3197  CE  LYS B 157     -20.240  71.953  35.086  1.00 52.10           C  
-ATOM   3198  NZ  LYS B 157     -20.699  70.933  34.093  1.00 52.26           N  
-ATOM   3199  N   GLY B 158     -23.019  75.917  36.150  1.00 44.94           N  
-ATOM   3200  CA  GLY B 158     -22.921  76.694  37.372  1.00 44.17           C  
-ATOM   3201  C   GLY B 158     -24.028  77.688  37.650  1.00 43.73           C  
-ATOM   3202  O   GLY B 158     -23.905  78.513  38.552  1.00 43.08           O  
-ATOM   3203  N   SER B 159     -25.109  77.617  36.885  1.00 44.01           N  
-ATOM   3204  CA  SER B 159     -26.232  78.527  37.084  1.00 43.97           C  
-ATOM   3205  C   SER B 159     -27.246  77.868  38.010  1.00 43.33           C  
-ATOM   3206  O   SER B 159     -28.189  78.507  38.471  1.00 41.67           O  
-ATOM   3207  CB  SER B 159     -26.894  78.860  35.743  1.00 44.50           C  
-ATOM   3208  OG  SER B 159     -27.487  77.711  35.161  1.00 45.45           O  
-ATOM   3209  N   GLY B 160     -27.039  76.581  38.275  1.00 43.62           N  
-ATOM   3210  CA  GLY B 160     -27.936  75.844  39.146  1.00 45.39           C  
-ATOM   3211  C   GLY B 160     -28.444  74.543  38.543  1.00 46.84           C  
-ATOM   3212  O   GLY B 160     -29.063  74.544  37.477  1.00 47.81           O  
-ATOM   3213  N   LYS B 161     -28.180  73.435  39.234  1.00 47.51           N  
-ATOM   3214  CA  LYS B 161     -28.599  72.102  38.800  1.00 47.35           C  
-ATOM   3215  C   LYS B 161     -30.068  72.110  38.399  1.00 46.33           C  
-ATOM   3216  O   LYS B 161     -30.895  72.717  39.077  1.00 45.91           O  
-ATOM   3217  CB  LYS B 161     -28.387  71.101  39.938  1.00 49.96           C  
-ATOM   3218  CG  LYS B 161     -27.346  70.014  39.680  1.00 53.73           C  
-ATOM   3219  CD  LYS B 161     -27.839  68.958  38.673  1.00 57.59           C  
-ATOM   3220  CE  LYS B 161     -29.204  68.324  39.059  1.00 58.89           C  
-ATOM   3221  NZ  LYS B 161     -29.262  67.582  40.363  1.00 57.13           N  
-ATOM   3222  N   THR B 162     -30.378  71.431  37.296  1.00 45.40           N  
-ATOM   3223  CA  THR B 162     -31.740  71.343  36.766  1.00 44.02           C  
-ATOM   3224  C   THR B 162     -32.036  69.895  36.333  1.00 43.96           C  
-ATOM   3225  O   THR B 162     -31.210  69.259  35.672  1.00 43.78           O  
-ATOM   3226  CB  THR B 162     -31.908  72.291  35.556  1.00 43.20           C  
-ATOM   3227  OG1 THR B 162     -31.580  73.630  35.945  1.00 42.59           O  
-ATOM   3228  CG2 THR B 162     -33.331  72.274  35.067  1.00 44.16           C  
-ATOM   3229  N   ASN B 163     -33.218  69.385  36.690  1.00 43.55           N  
-ATOM   3230  CA  ASN B 163     -33.595  67.998  36.373  1.00 42.31           C  
-ATOM   3231  C   ASN B 163     -34.529  67.766  35.182  1.00 40.09           C  
-ATOM   3232  O   ASN B 163     -35.571  68.407  35.044  1.00 39.80           O  
-ATOM   3233  CB  ASN B 163     -34.177  67.347  37.627  1.00 44.49           C  
-ATOM   3234  CG  ASN B 163     -33.189  67.346  38.785  1.00 45.03           C  
-ATOM   3235  OD1 ASN B 163     -32.191  66.606  38.775  1.00 43.45           O  
-ATOM   3236  ND2 ASN B 163     -33.450  68.194  39.783  1.00 44.31           N  
-ATOM   3237  N   ILE B 164     -34.143  66.803  34.352  1.00 37.36           N  
-ATOM   3238  CA  ILE B 164     -34.851  66.457  33.126  1.00 36.83           C  
-ATOM   3239  C   ILE B 164     -35.400  65.018  33.089  1.00 37.23           C  
-ATOM   3240  O   ILE B 164     -34.879  64.122  33.749  1.00 37.71           O  
-ATOM   3241  CB  ILE B 164     -33.879  66.686  31.911  1.00 35.94           C  
-ATOM   3242  CG1 ILE B 164     -34.010  68.113  31.401  1.00 37.83           C  
-ATOM   3243  CG2 ILE B 164     -34.131  65.709  30.789  1.00 36.31           C  
-ATOM   3244  CD1 ILE B 164     -33.647  69.171  32.414  1.00 39.70           C  
-ATOM   3245  N   ALA B 165     -36.468  64.812  32.323  1.00 36.33           N  
-ATOM   3246  CA  ALA B 165     -37.065  63.488  32.134  1.00 35.41           C  
-ATOM   3247  C   ALA B 165     -36.981  63.264  30.618  1.00 35.68           C  
-ATOM   3248  O   ALA B 165     -37.122  64.213  29.848  1.00 37.20           O  
-ATOM   3249  CB  ALA B 165     -38.516  63.483  32.599  1.00 33.05           C  
-ATOM   3250  N   LEU B 166     -36.752  62.041  30.164  1.00 34.15           N  
-ATOM   3251  CA  LEU B 166     -36.644  61.862  28.727  1.00 34.50           C  
-ATOM   3252  C   LEU B 166     -37.605  60.870  28.112  1.00 36.73           C  
-ATOM   3253  O   LEU B 166     -37.321  59.678  28.071  1.00 39.55           O  
-ATOM   3254  CB  LEU B 166     -35.215  61.472  28.356  1.00 32.60           C  
-ATOM   3255  CG  LEU B 166     -34.291  62.571  27.835  1.00 30.53           C  
-ATOM   3256  CD1 LEU B 166     -32.854  62.100  27.828  1.00 29.85           C  
-ATOM   3257  CD2 LEU B 166     -34.710  62.932  26.440  1.00 31.40           C  
-ATOM   3258  N   LEU B 167     -38.735  61.366  27.615  1.00 36.93           N  
-ATOM   3259  CA  LEU B 167     -39.728  60.515  26.973  1.00 36.65           C  
-ATOM   3260  C   LEU B 167     -39.527  60.625  25.472  1.00 38.08           C  
-ATOM   3261  O   LEU B 167     -40.256  61.342  24.796  1.00 38.60           O  
-ATOM   3262  CB  LEU B 167     -41.134  60.975  27.337  1.00 33.76           C  
-ATOM   3263  CG  LEU B 167     -41.590  60.680  28.760  1.00 32.21           C  
-ATOM   3264  CD1 LEU B 167     -40.541  61.139  29.747  1.00 33.32           C  
-ATOM   3265  CD2 LEU B 167     -42.913  61.374  29.014  1.00 30.16           C  
-ATOM   3266  N   LEU B 168     -38.542  59.911  24.946  1.00 39.81           N  
-ATOM   3267  CA  LEU B 168     -38.265  59.992  23.525  1.00 42.59           C  
-ATOM   3268  C   LEU B 168     -38.868  58.889  22.667  1.00 45.88           C  
-ATOM   3269  O   LEU B 168     -38.666  58.855  21.453  1.00 45.97           O  
-ATOM   3270  CB  LEU B 168     -36.755  60.077  23.305  1.00 41.90           C  
-ATOM   3271  CG  LEU B 168     -36.115  61.360  23.849  1.00 41.26           C  
-ATOM   3272  CD1 LEU B 168     -34.613  61.315  23.631  1.00 41.22           C  
-ATOM   3273  CD2 LEU B 168     -36.716  62.578  23.155  1.00 40.67           C  
-ATOM   3274  N   GLY B 169     -39.608  57.977  23.279  1.00 49.33           N  
-ATOM   3275  CA  GLY B 169     -40.228  56.944  22.475  1.00 53.41           C  
-ATOM   3276  C   GLY B 169     -39.600  55.571  22.505  1.00 56.64           C  
-ATOM   3277  O   GLY B 169     -39.064  55.157  23.528  1.00 56.28           O  
-ATOM   3278  N   PRO B 170     -39.671  54.833  21.382  1.00 59.99           N  
-ATOM   3279  CA  PRO B 170     -39.137  53.480  21.194  1.00 62.73           C  
-ATOM   3280  C   PRO B 170     -37.622  53.332  21.358  1.00 66.02           C  
-ATOM   3281  O   PRO B 170     -36.854  54.267  21.110  1.00 66.99           O  
-ATOM   3282  CB  PRO B 170     -39.595  53.125  19.781  1.00 61.26           C  
-ATOM   3283  CG  PRO B 170     -40.852  53.901  19.627  1.00 60.46           C  
-ATOM   3284  CD  PRO B 170     -40.438  55.238  20.193  1.00 60.60           C  
-ATOM   3285  N   ARG B 171     -37.211  52.133  21.763  1.00 68.41           N  
-ATOM   3286  CA  ARG B 171     -35.807  51.811  21.976  1.00 70.41           C  
-ATOM   3287  C   ARG B 171     -35.080  51.433  20.681  1.00 70.82           C  
-ATOM   3288  O   ARG B 171     -35.675  51.387  19.598  1.00 71.09           O  
-ATOM   3289  CB  ARG B 171     -35.694  50.663  22.976  1.00 71.38           C  
-ATOM   3290  CG  ARG B 171     -36.506  50.863  24.243  1.00 73.79           C  
-ATOM   3291  CD  ARG B 171     -35.797  50.274  25.458  1.00 76.42           C  
-ATOM   3292  NE  ARG B 171     -34.790  51.189  25.998  1.00 79.09           N  
-ATOM   3293  CZ  ARG B 171     -33.663  51.540  25.380  1.00 80.17           C  
-ATOM   3294  NH1 ARG B 171     -33.362  51.055  24.180  1.00 80.67           N  
-ATOM   3295  NH2 ARG B 171     -32.835  52.395  25.964  1.00 79.87           N  
-ATOM   3296  N   THR B 176     -28.292  53.380  20.647  1.00 69.14           N  
-ATOM   3297  CA  THR B 176     -28.030  54.692  20.060  1.00 69.71           C  
-ATOM   3298  C   THR B 176     -29.212  55.172  19.219  1.00 68.38           C  
-ATOM   3299  O   THR B 176     -29.832  54.382  18.507  1.00 70.33           O  
-ATOM   3300  CB  THR B 176     -26.762  54.671  19.152  1.00 70.84           C  
-ATOM   3301  OG1 THR B 176     -26.521  55.989  18.636  1.00 72.58           O  
-ATOM   3302  CG2 THR B 176     -26.951  53.709  17.972  1.00 70.69           C  
-ATOM   3303  N   LYS B 177     -29.520  56.463  19.308  1.00 64.66           N  
-ATOM   3304  CA  LYS B 177     -30.607  57.057  18.539  1.00 59.94           C  
-ATOM   3305  C   LYS B 177     -30.220  58.501  18.285  1.00 57.24           C  
-ATOM   3306  O   LYS B 177     -29.953  59.262  19.217  1.00 58.06           O  
-ATOM   3307  CB  LYS B 177     -31.924  56.991  19.310  1.00 59.58           C  
-ATOM   3308  CG  LYS B 177     -33.133  57.463  18.524  1.00 59.27           C  
-ATOM   3309  CD  LYS B 177     -34.389  57.084  19.273  1.00 60.66           C  
-ATOM   3310  CE  LYS B 177     -35.651  57.276  18.452  1.00 61.63           C  
-ATOM   3311  NZ  LYS B 177     -36.835  56.761  19.206  1.00 60.67           N  
-ATOM   3312  N   PRO B 178     -30.179  58.902  17.012  1.00 53.46           N  
-ATOM   3313  CA  PRO B 178     -29.812  60.273  16.657  1.00 50.98           C  
-ATOM   3314  C   PRO B 178     -30.364  61.345  17.607  1.00 49.37           C  
-ATOM   3315  O   PRO B 178     -29.598  62.086  18.227  1.00 48.50           O  
-ATOM   3316  CB  PRO B 178     -30.343  60.397  15.236  1.00 50.74           C  
-ATOM   3317  CG  PRO B 178     -30.129  59.018  14.704  1.00 49.95           C  
-ATOM   3318  CD  PRO B 178     -30.632  58.158  15.826  1.00 51.51           C  
-ATOM   3319  N   VAL B 179     -31.687  61.415  17.730  1.00 47.66           N  
-ATOM   3320  CA  VAL B 179     -32.328  62.396  18.603  1.00 45.33           C  
-ATOM   3321  C   VAL B 179     -31.658  62.406  19.968  1.00 43.16           C  
-ATOM   3322  O   VAL B 179     -31.313  63.457  20.490  1.00 42.86           O  
-ATOM   3323  CB  VAL B 179     -33.823  62.075  18.811  1.00 46.03           C  
-ATOM   3324  CG1 VAL B 179     -34.514  63.246  19.490  1.00 44.48           C  
-ATOM   3325  CG2 VAL B 179     -34.478  61.744  17.481  1.00 47.46           C  
-ATOM   3326  N   THR B 180     -31.485  61.224  20.542  1.00 41.25           N  
-ATOM   3327  CA  THR B 180     -30.858  61.098  21.843  1.00 39.75           C  
-ATOM   3328  C   THR B 180     -29.425  61.616  21.806  1.00 39.96           C  
-ATOM   3329  O   THR B 180     -29.079  62.545  22.535  1.00 39.59           O  
-ATOM   3330  CB  THR B 180     -30.844  59.635  22.306  1.00 39.31           C  
-ATOM   3331  OG1 THR B 180     -32.190  59.165  22.429  1.00 38.68           O  
-ATOM   3332  CG2 THR B 180     -30.139  59.505  23.642  1.00 38.16           C  
-ATOM   3333  N   THR B 181     -28.597  61.018  20.951  1.00 39.62           N  
-ATOM   3334  CA  THR B 181     -27.194  61.411  20.828  1.00 38.80           C  
-ATOM   3335  C   THR B 181     -27.008  62.918  20.749  1.00 38.60           C  
-ATOM   3336  O   THR B 181     -26.231  63.490  21.512  1.00 39.46           O  
-ATOM   3337  CB  THR B 181     -26.540  60.792  19.587  1.00 38.35           C  
-ATOM   3338  OG1 THR B 181     -26.746  59.376  19.589  1.00 41.21           O  
-ATOM   3339  CG2 THR B 181     -25.058  61.059  19.594  1.00 37.80           C  
-ATOM   3340  N   GLY B 182     -27.717  63.555  19.820  1.00 38.11           N  
-ATOM   3341  CA  GLY B 182     -27.619  64.996  19.664  1.00 37.45           C  
-ATOM   3342  C   GLY B 182     -28.069  65.758  20.896  1.00 37.93           C  
-ATOM   3343  O   GLY B 182     -27.497  66.795  21.244  1.00 37.77           O  
-ATOM   3344  N   PHE B 183     -29.102  65.254  21.562  1.00 37.56           N  
-ATOM   3345  CA  PHE B 183     -29.588  65.918  22.753  1.00 38.04           C  
-ATOM   3346  C   PHE B 183     -28.496  65.865  23.809  1.00 40.26           C  
-ATOM   3347  O   PHE B 183     -28.234  66.853  24.488  1.00 40.26           O  
-ATOM   3348  CB  PHE B 183     -30.849  65.246  23.288  1.00 36.15           C  
-ATOM   3349  CG  PHE B 183     -31.431  65.942  24.481  1.00 35.27           C  
-ATOM   3350  CD1 PHE B 183     -32.085  67.164  24.338  1.00 34.94           C  
-ATOM   3351  CD2 PHE B 183     -31.248  65.425  25.759  1.00 34.29           C  
-ATOM   3352  CE1 PHE B 183     -32.543  67.866  25.454  1.00 34.91           C  
-ATOM   3353  CE2 PHE B 183     -31.704  66.119  26.888  1.00 34.20           C  
-ATOM   3354  CZ  PHE B 183     -32.349  67.339  26.735  1.00 34.50           C  
-ATOM   3355  N   TYR B 184     -27.851  64.710  23.943  1.00 43.50           N  
-ATOM   3356  CA  TYR B 184     -26.777  64.552  24.920  1.00 44.74           C  
-ATOM   3357  C   TYR B 184     -25.597  65.447  24.596  1.00 44.25           C  
-ATOM   3358  O   TYR B 184     -25.024  66.058  25.488  1.00 44.97           O  
-ATOM   3359  CB  TYR B 184     -26.313  63.095  24.993  1.00 46.52           C  
-ATOM   3360  CG  TYR B 184     -27.200  62.214  25.845  1.00 49.19           C  
-ATOM   3361  CD1 TYR B 184     -28.523  61.969  25.488  1.00 50.69           C  
-ATOM   3362  CD2 TYR B 184     -26.722  61.641  27.024  1.00 50.51           C  
-ATOM   3363  CE1 TYR B 184     -29.354  61.175  26.286  1.00 52.43           C  
-ATOM   3364  CE2 TYR B 184     -27.544  60.844  27.831  1.00 51.74           C  
-ATOM   3365  CZ  TYR B 184     -28.860  60.617  27.455  1.00 52.66           C  
-ATOM   3366  OH  TYR B 184     -29.687  59.845  28.244  1.00 53.28           O  
-ATOM   3367  N   GLU B 185     -25.237  65.540  23.324  1.00 43.87           N  
-ATOM   3368  CA  GLU B 185     -24.112  66.379  22.946  1.00 45.20           C  
-ATOM   3369  C   GLU B 185     -24.311  67.851  23.264  1.00 45.16           C  
-ATOM   3370  O   GLU B 185     -23.359  68.542  23.607  1.00 44.70           O  
-ATOM   3371  CB  GLU B 185     -23.792  66.221  21.462  1.00 46.68           C  
-ATOM   3372  CG  GLU B 185     -22.555  65.366  21.197  1.00 51.07           C  
-ATOM   3373  CD  GLU B 185     -21.287  65.955  21.806  1.00 52.58           C  
-ATOM   3374  OE1 GLU B 185     -20.869  67.054  21.371  1.00 53.31           O  
-ATOM   3375  OE2 GLU B 185     -20.713  65.317  22.719  1.00 53.60           O  
-ATOM   3376  N   ALA B 186     -25.545  68.331  23.158  1.00 45.97           N  
-ATOM   3377  CA  ALA B 186     -25.837  69.735  23.423  1.00 45.52           C  
-ATOM   3378  C   ALA B 186     -25.972  70.016  24.917  1.00 45.94           C  
-ATOM   3379  O   ALA B 186     -25.952  71.165  25.342  1.00 44.82           O  
-ATOM   3380  CB  ALA B 186     -27.105  70.147  22.678  1.00 44.29           C  
-ATOM   3381  N   ILE B 187     -26.104  68.956  25.706  1.00 48.14           N  
-ATOM   3382  CA  ILE B 187     -26.234  69.072  27.156  1.00 50.85           C  
-ATOM   3383  C   ILE B 187     -24.847  69.115  27.791  1.00 53.34           C  
-ATOM   3384  O   ILE B 187     -24.614  69.830  28.763  1.00 52.65           O  
-ATOM   3385  CB  ILE B 187     -26.998  67.862  27.751  1.00 50.67           C  
-ATOM   3386  CG1 ILE B 187     -28.448  67.873  27.288  1.00 50.66           C  
-ATOM   3387  CG2 ILE B 187     -26.944  67.899  29.260  1.00 50.81           C  
-ATOM   3388  CD1 ILE B 187     -29.173  69.138  27.646  1.00 51.73           C  
-ATOM   3389  N   LYS B 188     -23.934  68.329  27.230  1.00 56.15           N  
-ATOM   3390  CA  LYS B 188     -22.559  68.245  27.711  1.00 58.95           C  
-ATOM   3391  C   LYS B 188     -22.069  69.610  28.225  1.00 59.55           C  
-ATOM   3392  O   LYS B 188     -22.013  70.584  27.473  1.00 59.26           O  
-ATOM   3393  CB  LYS B 188     -21.655  67.746  26.568  1.00 60.99           C  
-ATOM   3394  CG  LYS B 188     -20.578  66.725  26.956  1.00 64.27           C  
-ATOM   3395  CD  LYS B 188     -19.664  67.232  28.085  1.00 68.09           C  
-ATOM   3396  CE  LYS B 188     -18.957  68.550  27.731  1.00 68.87           C  
-ATOM   3397  NZ  LYS B 188     -18.211  69.125  28.892  1.00 67.82           N  
-ATOM   3398  N   ASN B 189     -21.731  69.679  29.511  1.00 60.61           N  
-ATOM   3399  CA  ASN B 189     -21.236  70.921  30.106  1.00 62.33           C  
-ATOM   3400  C   ASN B 189     -22.362  71.948  30.244  1.00 61.12           C  
-ATOM   3401  O   ASN B 189     -22.226  73.092  29.804  1.00 60.43           O  
-ATOM   3402  CB  ASN B 189     -20.106  71.494  29.229  1.00 64.91           C  
-ATOM   3403  CG  ASN B 189     -19.468  72.747  29.824  1.00 68.04           C  
-ATOM   3404  OD1 ASN B 189     -18.850  72.704  30.896  1.00 69.27           O  
-ATOM   3405  ND2 ASN B 189     -19.614  73.871  29.125  1.00 67.98           N  
-ATOM   3406  N   SER B 190     -23.460  71.561  30.888  1.00 60.02           N  
-ATOM   3407  CA  SER B 190     -24.579  72.481  30.991  1.00 59.37           C  
-ATOM   3408  C   SER B 190     -25.413  72.534  32.263  1.00 58.80           C  
-ATOM   3409  O   SER B 190     -26.564  72.952  32.204  1.00 60.64           O  
-ATOM   3410  CB  SER B 190     -25.535  72.237  29.824  1.00 58.88           C  
-ATOM   3411  OG  SER B 190     -26.170  70.979  29.968  1.00 57.50           O  
-ATOM   3412  N   ASP B 191     -24.889  72.121  33.404  1.00 56.77           N  
-ATOM   3413  CA  ASP B 191     -25.700  72.203  34.621  1.00 55.75           C  
-ATOM   3414  C   ASP B 191     -27.131  71.629  34.482  1.00 54.28           C  
-ATOM   3415  O   ASP B 191     -28.013  71.948  35.283  1.00 53.14           O  
-ATOM   3416  CB  ASP B 191     -25.783  73.666  35.081  1.00 55.97           C  
-ATOM   3417  CG  ASP B 191     -25.271  73.871  36.503  1.00 56.60           C  
-ATOM   3418  OD1 ASP B 191     -24.196  73.329  36.846  1.00 56.57           O  
-ATOM   3419  OD2 ASP B 191     -25.939  74.592  37.273  1.00 55.63           O  
-ATOM   3420  N   ILE B 192     -27.356  70.802  33.461  1.00 52.71           N  
-ATOM   3421  CA  ILE B 192     -28.652  70.159  33.241  1.00 51.63           C  
-ATOM   3422  C   ILE B 192     -28.450  68.673  33.487  1.00 52.37           C  
-ATOM   3423  O   ILE B 192     -27.552  68.057  32.921  1.00 52.88           O  
-ATOM   3424  CB  ILE B 192     -29.183  70.388  31.791  1.00 50.94           C  
-ATOM   3425  CG1 ILE B 192     -30.092  71.616  31.771  1.00 51.50           C  
-ATOM   3426  CG2 ILE B 192     -29.969  69.177  31.291  1.00 48.87           C  
-ATOM   3427  CD1 ILE B 192     -30.621  71.963  30.413  1.00 49.75           C  
-ATOM   3428  N   HIS B 193     -29.286  68.093  34.335  1.00 53.14           N  
-ATOM   3429  CA  HIS B 193     -29.157  66.682  34.665  1.00 53.39           C  
-ATOM   3430  C   HIS B 193     -30.350  65.824  34.231  1.00 51.61           C  
-ATOM   3431  O   HIS B 193     -31.494  66.118  34.580  1.00 51.12           O  
-ATOM   3432  CB  HIS B 193     -28.941  66.555  36.175  1.00 56.55           C  
-ATOM   3433  CG  HIS B 193     -28.873  65.144  36.662  1.00 60.42           C  
-ATOM   3434  ND1 HIS B 193     -29.201  64.789  37.953  1.00 62.09           N  
-ATOM   3435  CD2 HIS B 193     -28.549  63.992  36.025  1.00 61.79           C  
-ATOM   3436  CE1 HIS B 193     -29.089  63.479  38.090  1.00 63.24           C  
-ATOM   3437  NE2 HIS B 193     -28.697  62.971  36.934  1.00 63.28           N  
-ATOM   3438  N   ILE B 194     -30.071  64.762  33.477  1.00 49.85           N  
-ATOM   3439  CA  ILE B 194     -31.106  63.838  33.016  1.00 49.67           C  
-ATOM   3440  C   ILE B 194     -31.408  62.795  34.101  1.00 51.43           C  
-ATOM   3441  O   ILE B 194     -30.863  61.694  34.066  1.00 52.49           O  
-ATOM   3442  CB  ILE B 194     -30.659  63.054  31.762  1.00 47.88           C  
-ATOM   3443  CG1 ILE B 194     -30.301  64.006  30.625  1.00 46.47           C  
-ATOM   3444  CG2 ILE B 194     -31.765  62.110  31.327  1.00 47.12           C  
-ATOM   3445  CD1 ILE B 194     -29.891  63.284  29.360  1.00 43.07           C  
-ATOM   3446  N   VAL B 195     -32.277  63.136  35.050  1.00 53.04           N  
-ATOM   3447  CA  VAL B 195     -32.648  62.241  36.151  1.00 54.27           C  
-ATOM   3448  C   VAL B 195     -32.982  60.800  35.758  1.00 56.23           C  
-ATOM   3449  O   VAL B 195     -32.385  59.852  36.268  1.00 58.52           O  
-ATOM   3450  CB  VAL B 195     -33.843  62.799  36.921  1.00 53.95           C  
-ATOM   3451  CG1 VAL B 195     -34.308  61.794  37.961  1.00 53.92           C  
-ATOM   3452  CG2 VAL B 195     -33.455  64.115  37.570  1.00 54.55           C  
-ATOM   3453  N   ASP B 196     -33.957  60.627  34.879  1.00 57.24           N  
-ATOM   3454  CA  ASP B 196     -34.324  59.289  34.441  1.00 58.76           C  
-ATOM   3455  C   ASP B 196     -34.694  59.392  32.973  1.00 58.89           C  
-ATOM   3456  O   ASP B 196     -34.816  60.491  32.433  1.00 59.26           O  
-ATOM   3457  CB  ASP B 196     -35.520  58.760  35.246  1.00 60.79           C  
-ATOM   3458  CG  ASP B 196     -35.498  57.238  35.412  1.00 62.07           C  
-ATOM   3459  OD1 ASP B 196     -35.272  56.518  34.409  1.00 61.73           O  
-ATOM   3460  OD2 ASP B 196     -35.719  56.767  36.554  1.00 61.79           O  
-ATOM   3461  N   SER B 197     -34.862  58.247  32.328  1.00 58.90           N  
-ATOM   3462  CA  SER B 197     -35.227  58.224  30.921  1.00 58.98           C  
-ATOM   3463  C   SER B 197     -36.188  57.061  30.695  1.00 59.60           C  
-ATOM   3464  O   SER B 197     -35.875  55.918  31.018  1.00 61.35           O  
-ATOM   3465  CB  SER B 197     -33.973  58.067  30.060  1.00 57.37           C  
-ATOM   3466  OG  SER B 197     -34.307  58.092  28.690  1.00 55.69           O  
-ATOM   3467  N   PHE B 198     -37.365  57.357  30.155  1.00 59.99           N  
-ATOM   3468  CA  PHE B 198     -38.364  56.325  29.911  1.00 59.93           C  
-ATOM   3469  C   PHE B 198     -38.660  56.137  28.428  1.00 59.36           C  
-ATOM   3470  O   PHE B 198     -38.791  57.099  27.671  1.00 59.66           O  
-ATOM   3471  CB  PHE B 198     -39.652  56.663  30.665  1.00 60.95           C  
-ATOM   3472  CG  PHE B 198     -39.427  57.027  32.110  1.00 62.78           C  
-ATOM   3473  CD1 PHE B 198     -38.998  58.305  32.462  1.00 64.08           C  
-ATOM   3474  CD2 PHE B 198     -39.620  56.087  33.119  1.00 63.39           C  
-ATOM   3475  CE1 PHE B 198     -38.764  58.644  33.798  1.00 63.65           C  
-ATOM   3476  CE2 PHE B 198     -39.388  56.414  34.456  1.00 63.47           C  
-ATOM   3477  CZ  PHE B 198     -38.959  57.695  34.795  1.00 63.89           C  
-ATOM   3478  N   TRP B 199     -38.750  54.886  28.010  1.00 58.59           N  
-ATOM   3479  CA  TRP B 199     -39.035  54.588  26.621  1.00 58.91           C  
-ATOM   3480  C   TRP B 199     -40.315  53.769  26.549  1.00 57.04           C  
-ATOM   3481  O   TRP B 199     -40.710  53.129  27.522  1.00 56.81           O  
-ATOM   3482  CB  TRP B 199     -37.854  53.834  25.993  1.00 62.86           C  
-ATOM   3483  CG  TRP B 199     -36.643  54.714  25.748  1.00 68.25           C  
-ATOM   3484  CD1 TRP B 199     -36.416  55.534  24.666  1.00 70.61           C  
-ATOM   3485  CD2 TRP B 199     -35.525  54.900  26.623  1.00 70.07           C  
-ATOM   3486  NE1 TRP B 199     -35.227  56.216  24.819  1.00 70.01           N  
-ATOM   3487  CE2 TRP B 199     -34.660  55.847  26.009  1.00 70.57           C  
-ATOM   3488  CE3 TRP B 199     -35.168  54.362  27.867  1.00 70.61           C  
-ATOM   3489  CZ2 TRP B 199     -33.465  56.262  26.597  1.00 71.25           C  
-ATOM   3490  CZ3 TRP B 199     -33.978  54.777  28.454  1.00 72.42           C  
-ATOM   3491  CH2 TRP B 199     -33.139  55.720  27.816  1.00 72.81           C  
-ATOM   3492  N   ALA B 200     -40.969  53.815  25.399  1.00 54.99           N  
-ATOM   3493  CA  ALA B 200     -42.212  53.092  25.179  1.00 53.49           C  
-ATOM   3494  C   ALA B 200     -42.616  53.414  23.760  1.00 52.98           C  
-ATOM   3495  O   ALA B 200     -42.119  54.377  23.195  1.00 52.28           O  
-ATOM   3496  CB  ALA B 200     -43.270  53.575  26.138  1.00 53.38           C  
-ATOM   3497  N   ASP B 201     -43.499  52.618  23.169  1.00 53.52           N  
-ATOM   3498  CA  ASP B 201     -43.917  52.910  21.804  1.00 53.92           C  
-ATOM   3499  C   ASP B 201     -44.385  54.350  21.730  1.00 52.85           C  
-ATOM   3500  O   ASP B 201     -44.602  55.002  22.754  1.00 51.50           O  
-ATOM   3501  CB  ASP B 201     -45.037  51.974  21.360  1.00 56.31           C  
-ATOM   3502  CG  ASP B 201     -44.514  50.655  20.861  1.00 58.83           C  
-ATOM   3503  OD1 ASP B 201     -43.673  50.054  21.566  1.00 60.47           O  
-ATOM   3504  OD2 ASP B 201     -44.944  50.220  19.767  1.00 60.50           O  
-ATOM   3505  N   ASN B 202     -44.553  54.849  20.516  1.00 52.23           N  
-ATOM   3506  CA  ASN B 202     -44.961  56.229  20.359  1.00 52.34           C  
-ATOM   3507  C   ASN B 202     -46.461  56.452  20.302  1.00 52.09           C  
-ATOM   3508  O   ASN B 202     -46.955  57.239  19.495  1.00 51.50           O  
-ATOM   3509  CB  ASN B 202     -44.303  56.816  19.125  1.00 53.02           C  
-ATOM   3510  CG  ASN B 202     -43.939  58.248  19.317  1.00 53.78           C  
-ATOM   3511  OD1 ASN B 202     -43.353  58.615  20.341  1.00 54.57           O  
-ATOM   3512  ND2 ASN B 202     -44.278  59.079  18.343  1.00 55.80           N  
-ATOM   3513  N   ASP B 203     -47.182  55.752  21.168  1.00 52.14           N  
-ATOM   3514  CA  ASP B 203     -48.622  55.882  21.238  1.00 51.73           C  
-ATOM   3515  C   ASP B 203     -48.963  56.855  22.361  1.00 49.19           C  
-ATOM   3516  O   ASP B 203     -48.293  56.888  23.399  1.00 47.45           O  
-ATOM   3517  CB  ASP B 203     -49.261  54.516  21.497  1.00 57.05           C  
-ATOM   3518  CG  ASP B 203     -50.628  54.625  22.173  1.00 64.04           C  
-ATOM   3519  OD1 ASP B 203     -51.508  55.358  21.647  1.00 67.74           O  
-ATOM   3520  OD2 ASP B 203     -50.820  53.977  23.235  1.00 65.97           O  
-ATOM   3521  N   LYS B 204     -50.006  57.647  22.139  1.00 46.44           N  
-ATOM   3522  CA  LYS B 204     -50.463  58.639  23.105  1.00 45.09           C  
-ATOM   3523  C   LYS B 204     -50.694  58.083  24.504  1.00 44.89           C  
-ATOM   3524  O   LYS B 204     -50.156  58.595  25.493  1.00 44.13           O  
-ATOM   3525  CB  LYS B 204     -51.758  59.269  22.612  1.00 44.43           C  
-ATOM   3526  CG  LYS B 204     -51.665  60.746  22.288  1.00 43.47           C  
-ATOM   3527  CD  LYS B 204     -51.943  61.616  23.493  1.00 41.38           C  
-ATOM   3528  CE  LYS B 204     -52.127  63.062  23.056  1.00 40.76           C  
-ATOM   3529  NZ  LYS B 204     -53.193  63.189  22.022  1.00 39.85           N  
-ATOM   3530  N   GLU B 205     -51.505  57.036  24.588  1.00 44.23           N  
-ATOM   3531  CA  GLU B 205     -51.821  56.448  25.878  1.00 43.90           C  
-ATOM   3532  C   GLU B 205     -50.617  55.844  26.584  1.00 43.17           C  
-ATOM   3533  O   GLU B 205     -50.589  55.737  27.816  1.00 42.08           O  
-ATOM   3534  CB  GLU B 205     -52.949  55.429  25.714  1.00 44.31           C  
-ATOM   3535  CG  GLU B 205     -54.236  56.085  25.228  1.00 44.71           C  
-ATOM   3536  CD  GLU B 205     -54.565  57.358  26.016  1.00 45.35           C  
-ATOM   3537  OE1 GLU B 205     -55.035  58.343  25.392  1.00 45.25           O  
-ATOM   3538  OE2 GLU B 205     -54.353  57.372  27.255  1.00 42.81           O  
-ATOM   3539  N   LEU B 206     -49.611  55.470  25.807  1.00 42.46           N  
-ATOM   3540  CA  LEU B 206     -48.404  54.906  26.388  1.00 42.75           C  
-ATOM   3541  C   LEU B 206     -47.556  56.036  26.971  1.00 41.35           C  
-ATOM   3542  O   LEU B 206     -47.097  55.955  28.116  1.00 39.73           O  
-ATOM   3543  CB  LEU B 206     -47.624  54.117  25.326  1.00 43.97           C  
-ATOM   3544  CG  LEU B 206     -48.311  52.818  24.875  1.00 43.10           C  
-ATOM   3545  CD1 LEU B 206     -47.600  52.221  23.673  1.00 41.92           C  
-ATOM   3546  CD2 LEU B 206     -48.327  51.837  26.035  1.00 42.54           C  
-ATOM   3547  N   GLN B 207     -47.365  57.096  26.188  1.00 40.19           N  
-ATOM   3548  CA  GLN B 207     -46.582  58.231  26.660  1.00 39.06           C  
-ATOM   3549  C   GLN B 207     -47.279  58.870  27.847  1.00 38.40           C  
-ATOM   3550  O   GLN B 207     -46.642  59.188  28.849  1.00 37.68           O  
-ATOM   3551  CB  GLN B 207     -46.404  59.286  25.564  1.00 38.00           C  
-ATOM   3552  CG  GLN B 207     -45.585  58.846  24.369  1.00 37.66           C  
-ATOM   3553  CD  GLN B 207     -44.289  58.138  24.742  1.00 37.49           C  
-ATOM   3554  OE1 GLN B 207     -43.740  58.322  25.832  1.00 36.47           O  
-ATOM   3555  NE2 GLN B 207     -43.786  57.333  23.817  1.00 38.11           N  
-ATOM   3556  N   ARG B 208     -48.590  59.063  27.729  1.00 38.62           N  
-ATOM   3557  CA  ARG B 208     -49.352  59.670  28.807  1.00 39.15           C  
-ATOM   3558  C   ARG B 208     -49.021  58.976  30.123  1.00 40.64           C  
-ATOM   3559  O   ARG B 208     -48.775  59.624  31.140  1.00 39.67           O  
-ATOM   3560  CB  ARG B 208     -50.851  59.571  28.535  1.00 37.79           C  
-ATOM   3561  CG  ARG B 208     -51.681  59.852  29.783  1.00 38.63           C  
-ATOM   3562  CD  ARG B 208     -53.160  59.920  29.500  1.00 37.65           C  
-ATOM   3563  NE  ARG B 208     -53.535  61.238  29.009  1.00 38.34           N  
-ATOM   3564  CZ  ARG B 208     -54.075  61.466  27.817  1.00 39.19           C  
-ATOM   3565  NH1 ARG B 208     -54.310  60.464  26.977  1.00 39.12           N  
-ATOM   3566  NH2 ARG B 208     -54.386  62.702  27.468  1.00 40.23           N  
-ATOM   3567  N   ASN B 209     -49.009  57.649  30.085  1.00 42.82           N  
-ATOM   3568  CA  ASN B 209     -48.706  56.841  31.256  1.00 44.09           C  
-ATOM   3569  C   ASN B 209     -47.356  57.251  31.860  1.00 43.39           C  
-ATOM   3570  O   ASN B 209     -47.250  57.528  33.062  1.00 41.72           O  
-ATOM   3571  CB  ASN B 209     -48.688  55.373  30.838  1.00 47.72           C  
-ATOM   3572  CG  ASN B 209     -48.627  54.433  32.015  1.00 50.97           C  
-ATOM   3573  OD1 ASN B 209     -47.561  53.900  32.345  1.00 52.79           O  
-ATOM   3574  ND2 ASN B 209     -49.775  54.223  32.667  1.00 52.15           N  
-ATOM   3575  N   LEU B 210     -46.332  57.294  31.009  1.00 42.90           N  
-ATOM   3576  CA  LEU B 210     -44.986  57.677  31.423  1.00 42.18           C  
-ATOM   3577  C   LEU B 210     -44.986  59.085  32.013  1.00 42.05           C  
-ATOM   3578  O   LEU B 210     -44.424  59.320  33.082  1.00 42.59           O  
-ATOM   3579  CB  LEU B 210     -44.038  57.619  30.224  1.00 41.83           C  
-ATOM   3580  CG  LEU B 210     -44.015  56.286  29.466  1.00 42.40           C  
-ATOM   3581  CD1 LEU B 210     -43.142  56.386  28.223  1.00 40.43           C  
-ATOM   3582  CD2 LEU B 210     -43.502  55.200  30.388  1.00 43.04           C  
-ATOM   3583  N   VAL B 211     -45.620  60.016  31.308  1.00 41.73           N  
-ATOM   3584  CA  VAL B 211     -45.706  61.402  31.755  1.00 41.68           C  
-ATOM   3585  C   VAL B 211     -46.215  61.470  33.188  1.00 42.47           C  
-ATOM   3586  O   VAL B 211     -45.710  62.247  34.005  1.00 39.97           O  
-ATOM   3587  CB  VAL B 211     -46.658  62.206  30.848  1.00 41.22           C  
-ATOM   3588  CG1 VAL B 211     -46.804  63.632  31.359  1.00 40.88           C  
-ATOM   3589  CG2 VAL B 211     -46.136  62.196  29.434  1.00 40.96           C  
-ATOM   3590  N   GLN B 212     -47.221  60.647  33.479  1.00 44.92           N  
-ATOM   3591  CA  GLN B 212     -47.811  60.596  34.810  1.00 46.85           C  
-ATOM   3592  C   GLN B 212     -46.767  60.050  35.769  1.00 48.63           C  
-ATOM   3593  O   GLN B 212     -46.646  60.540  36.891  1.00 49.16           O  
-ATOM   3594  CB  GLN B 212     -49.045  59.693  34.823  1.00 47.08           C  
-ATOM   3595  CG  GLN B 212     -49.916  59.822  33.574  1.00 49.72           C  
-ATOM   3596  CD  GLN B 212     -51.215  59.029  33.651  1.00 50.77           C  
-ATOM   3597  OE1 GLN B 212     -52.184  59.463  34.283  1.00 51.35           O  
-ATOM   3598  NE2 GLN B 212     -51.243  57.863  33.003  1.00 50.41           N  
-ATOM   3599  N   ARG B 213     -46.006  59.046  35.325  1.00 49.76           N  
-ATOM   3600  CA  ARG B 213     -44.965  58.449  36.167  1.00 50.59           C  
-ATOM   3601  C   ARG B 213     -43.957  59.521  36.579  1.00 50.58           C  
-ATOM   3602  O   ARG B 213     -43.472  59.538  37.716  1.00 50.33           O  
-ATOM   3603  CB  ARG B 213     -44.233  57.321  35.427  1.00 51.55           C  
-ATOM   3604  CG  ARG B 213     -43.535  56.337  36.371  1.00 55.88           C  
-ATOM   3605  CD  ARG B 213     -42.265  55.705  35.784  1.00 59.58           C  
-ATOM   3606  NE  ARG B 213     -42.484  54.955  34.544  1.00 63.35           N  
-ATOM   3607  CZ  ARG B 213     -43.161  53.812  34.451  1.00 65.40           C  
-ATOM   3608  NH1 ARG B 213     -43.703  53.261  35.530  1.00 66.94           N  
-ATOM   3609  NH2 ARG B 213     -43.292  53.212  33.272  1.00 65.08           N  
-ATOM   3610  N   VAL B 214     -43.659  60.420  35.644  1.00 51.03           N  
-ATOM   3611  CA  VAL B 214     -42.710  61.506  35.875  1.00 51.22           C  
-ATOM   3612  C   VAL B 214     -43.263  62.543  36.843  1.00 53.02           C  
-ATOM   3613  O   VAL B 214     -42.544  63.064  37.695  1.00 52.65           O  
-ATOM   3614  CB  VAL B 214     -42.367  62.223  34.562  1.00 49.46           C  
-ATOM   3615  CG1 VAL B 214     -41.292  63.264  34.805  1.00 46.67           C  
-ATOM   3616  CG2 VAL B 214     -41.930  61.218  33.519  1.00 48.77           C  
-ATOM   3617  N   ILE B 215     -44.547  62.845  36.702  1.00 54.96           N  
-ATOM   3618  CA  ILE B 215     -45.193  63.831  37.556  1.00 56.95           C  
-ATOM   3619  C   ILE B 215     -45.175  63.410  39.021  1.00 59.22           C  
-ATOM   3620  O   ILE B 215     -45.153  64.255  39.923  1.00 58.57           O  
-ATOM   3621  CB  ILE B 215     -46.657  64.065  37.100  1.00 55.72           C  
-ATOM   3622  CG1 ILE B 215     -46.669  64.492  35.625  1.00 55.27           C  
-ATOM   3623  CG2 ILE B 215     -47.324  65.121  37.971  1.00 54.21           C  
-ATOM   3624  CD1 ILE B 215     -48.029  64.859  35.081  1.00 54.11           C  
-ATOM   3625  N   ASP B 216     -45.160  62.098  39.248  1.00 62.12           N  
-ATOM   3626  CA  ASP B 216     -45.165  61.543  40.598  1.00 64.33           C  
-ATOM   3627  C   ASP B 216     -43.818  61.619  41.306  1.00 65.91           C  
-ATOM   3628  O   ASP B 216     -43.784  61.763  42.531  1.00 67.39           O  
-ATOM   3629  CB  ASP B 216     -45.668  60.096  40.571  1.00 64.90           C  
-ATOM   3630  CG  ASP B 216     -47.087  59.982  40.019  1.00 66.31           C  
-ATOM   3631  OD1 ASP B 216     -47.937  60.815  40.401  1.00 67.33           O  
-ATOM   3632  OD2 ASP B 216     -47.360  59.064  39.214  1.00 65.86           O  
-ATOM   3633  N   MET B 217     -42.714  61.522  40.563  1.00 66.34           N  
-ATOM   3634  CA  MET B 217     -41.399  61.623  41.195  1.00 67.33           C  
-ATOM   3635  C   MET B 217     -41.100  63.083  41.551  1.00 67.14           C  
-ATOM   3636  O   MET B 217     -40.064  63.396  42.124  1.00 67.25           O  
-ATOM   3637  CB  MET B 217     -40.303  61.035  40.292  1.00 68.71           C  
-ATOM   3638  CG  MET B 217     -40.466  61.305  38.803  1.00 70.60           C  
-ATOM   3639  SD  MET B 217     -39.281  60.369  37.785  1.00 71.81           S  
-ATOM   3640  CE  MET B 217     -40.049  58.713  37.850  1.00 71.63           C  
-ATOM   3641  N   GLY B 218     -42.047  63.948  41.197  1.00 67.62           N  
-ATOM   3642  CA  GLY B 218     -42.009  65.382  41.459  1.00 68.10           C  
-ATOM   3643  C   GLY B 218     -40.767  66.216  41.755  1.00 67.95           C  
-ATOM   3644  O   GLY B 218     -40.858  67.230  42.464  1.00 67.92           O  
-ATOM   3645  N   ASN B 219     -39.615  65.832  41.226  1.00 67.27           N  
-ATOM   3646  CA  ASN B 219     -38.416  66.620  41.463  1.00 67.12           C  
-ATOM   3647  C   ASN B 219     -37.825  67.020  40.112  1.00 65.75           C  
-ATOM   3648  O   ASN B 219     -36.639  67.346  40.012  1.00 67.15           O  
-ATOM   3649  CB  ASN B 219     -37.392  65.824  42.289  1.00 69.72           C  
-ATOM   3650  CG  ASN B 219     -36.908  64.559  41.581  1.00 72.85           C  
-ATOM   3651  OD1 ASN B 219     -37.694  63.656  41.270  1.00 75.08           O  
-ATOM   3652  ND2 ASN B 219     -35.602  64.489  41.328  1.00 72.58           N  
-ATOM   3653  N   ILE B 220     -38.665  67.001  39.077  1.00 61.91           N  
-ATOM   3654  CA  ILE B 220     -38.247  67.355  37.726  1.00 57.35           C  
-ATOM   3655  C   ILE B 220     -38.719  68.739  37.308  1.00 54.79           C  
-ATOM   3656  O   ILE B 220     -39.763  69.203  37.762  1.00 55.04           O  
-ATOM   3657  CB  ILE B 220     -38.756  66.321  36.742  1.00 56.79           C  
-ATOM   3658  CG1 ILE B 220     -38.026  65.013  37.015  1.00 57.36           C  
-ATOM   3659  CG2 ILE B 220     -38.553  66.796  35.320  1.00 57.03           C  
-ATOM   3660  CD1 ILE B 220     -38.274  63.964  35.999  1.00 60.22           C  
-ATOM   3661  N   ASP B 221     -37.943  69.399  36.447  1.00 51.88           N  
-ATOM   3662  CA  ASP B 221     -38.288  70.747  35.985  1.00 49.03           C  
-ATOM   3663  C   ASP B 221     -38.642  70.817  34.502  1.00 45.26           C  
-ATOM   3664  O   ASP B 221     -39.230  71.801  34.045  1.00 43.16           O  
-ATOM   3665  CB  ASP B 221     -37.138  71.726  36.246  1.00 51.71           C  
-ATOM   3666  CG  ASP B 221     -36.523  71.563  37.622  1.00 54.58           C  
-ATOM   3667  OD1 ASP B 221     -35.585  70.740  37.753  1.00 56.04           O  
-ATOM   3668  OD2 ASP B 221     -36.979  72.253  38.568  1.00 55.16           O  
-ATOM   3669  N   TYR B 222     -38.269  69.787  33.748  1.00 41.13           N  
-ATOM   3670  CA  TYR B 222     -38.554  69.759  32.319  1.00 37.57           C  
-ATOM   3671  C   TYR B 222     -38.766  68.358  31.786  1.00 35.64           C  
-ATOM   3672  O   TYR B 222     -38.185  67.395  32.289  1.00 35.81           O  
-ATOM   3673  CB  TYR B 222     -37.408  70.381  31.510  1.00 35.78           C  
-ATOM   3674  CG  TYR B 222     -37.134  71.835  31.783  1.00 34.01           C  
-ATOM   3675  CD1 TYR B 222     -36.152  72.214  32.688  1.00 33.44           C  
-ATOM   3676  CD2 TYR B 222     -37.849  72.836  31.125  1.00 32.68           C  
-ATOM   3677  CE1 TYR B 222     -35.879  73.552  32.935  1.00 33.13           C  
-ATOM   3678  CE2 TYR B 222     -37.586  74.179  31.365  1.00 33.27           C  
-ATOM   3679  CZ  TYR B 222     -36.596  74.530  32.272  1.00 33.60           C  
-ATOM   3680  OH  TYR B 222     -36.317  75.856  32.526  1.00 34.73           O  
-ATOM   3681  N   ILE B 223     -39.593  68.250  30.754  1.00 32.89           N  
-ATOM   3682  CA  ILE B 223     -39.821  66.963  30.128  1.00 30.79           C  
-ATOM   3683  C   ILE B 223     -39.516  67.081  28.644  1.00 31.90           C  
-ATOM   3684  O   ILE B 223     -40.289  67.661  27.880  1.00 34.13           O  
-ATOM   3685  CB  ILE B 223     -41.260  66.481  30.280  1.00 27.85           C  
-ATOM   3686  CG1 ILE B 223     -41.604  66.317  31.755  1.00 27.88           C  
-ATOM   3687  CG2 ILE B 223     -41.422  65.166  29.565  1.00 25.02           C  
-ATOM   3688  CD1 ILE B 223     -42.953  65.683  31.998  1.00 27.86           C  
-ATOM   3689  N   VAL B 224     -38.366  66.559  28.241  1.00 30.45           N  
-ATOM   3690  CA  VAL B 224     -37.982  66.577  26.839  1.00 28.77           C  
-ATOM   3691  C   VAL B 224     -38.580  65.302  26.256  1.00 28.74           C  
-ATOM   3692  O   VAL B 224     -38.242  64.208  26.707  1.00 30.58           O  
-ATOM   3693  CB  VAL B 224     -36.449  66.534  26.693  1.00 27.35           C  
-ATOM   3694  CG1 VAL B 224     -36.060  66.416  25.222  1.00 25.07           C  
-ATOM   3695  CG2 VAL B 224     -35.847  67.775  27.323  1.00 25.75           C  
-ATOM   3696  N   GLY B 225     -39.470  65.417  25.278  1.00 26.55           N  
-ATOM   3697  CA  GLY B 225     -40.047  64.200  24.733  1.00 26.90           C  
-ATOM   3698  C   GLY B 225     -40.489  64.294  23.291  1.00 26.73           C  
-ATOM   3699  O   GLY B 225     -40.257  65.315  22.650  1.00 29.00           O  
-ATOM   3700  N   SER B 226     -41.112  63.239  22.768  1.00 25.01           N  
-ATOM   3701  CA  SER B 226     -41.585  63.285  21.391  1.00 25.15           C  
-ATOM   3702  C   SER B 226     -42.835  64.154  21.375  1.00 23.93           C  
-ATOM   3703  O   SER B 226     -43.443  64.400  22.418  1.00 23.79           O  
-ATOM   3704  CB  SER B 226     -41.924  61.887  20.875  1.00 26.17           C  
-ATOM   3705  OG  SER B 226     -43.045  61.354  21.554  1.00 28.99           O  
-ATOM   3706  N   ALA B 227     -43.223  64.614  20.194  1.00 23.09           N  
-ATOM   3707  CA  ALA B 227     -44.397  65.471  20.074  1.00 22.36           C  
-ATOM   3708  C   ALA B 227     -45.613  64.835  20.738  1.00 22.09           C  
-ATOM   3709  O   ALA B 227     -46.385  65.512  21.429  1.00 20.36           O  
-ATOM   3710  CB  ALA B 227     -44.685  65.778  18.597  1.00 18.87           C  
-ATOM   3711  N   VAL B 228     -45.769  63.528  20.547  1.00 22.91           N  
-ATOM   3712  CA  VAL B 228     -46.912  62.835  21.130  1.00 23.57           C  
-ATOM   3713  C   VAL B 228     -46.855  62.849  22.657  1.00 23.01           C  
-ATOM   3714  O   VAL B 228     -47.886  62.932  23.324  1.00 22.64           O  
-ATOM   3715  CB  VAL B 228     -46.997  61.373  20.643  1.00 22.56           C  
-ATOM   3716  CG1 VAL B 228     -45.748  60.630  21.041  1.00 24.20           C  
-ATOM   3717  CG2 VAL B 228     -48.225  60.699  21.238  1.00 19.75           C  
-ATOM   3718  N   ALA B 229     -45.652  62.767  23.208  1.00 21.85           N  
-ATOM   3719  CA  ALA B 229     -45.505  62.777  24.648  1.00 21.33           C  
-ATOM   3720  C   ALA B 229     -45.757  64.188  25.193  1.00 20.97           C  
-ATOM   3721  O   ALA B 229     -46.443  64.359  26.202  1.00 18.65           O  
-ATOM   3722  CB  ALA B 229     -44.118  62.294  25.029  1.00 20.85           C  
-ATOM   3723  N   ILE B 230     -45.210  65.203  24.530  1.00 21.39           N  
-ATOM   3724  CA  ILE B 230     -45.431  66.563  25.001  1.00 23.03           C  
-ATOM   3725  C   ILE B 230     -46.930  66.859  24.937  1.00 24.85           C  
-ATOM   3726  O   ILE B 230     -47.497  67.447  25.868  1.00 24.99           O  
-ATOM   3727  CB  ILE B 230     -44.610  67.598  24.173  1.00 21.41           C  
-ATOM   3728  CG1 ILE B 230     -43.328  67.939  24.921  1.00 20.49           C  
-ATOM   3729  CG2 ILE B 230     -45.373  68.895  23.999  1.00 21.80           C  
-ATOM   3730  CD1 ILE B 230     -42.493  66.741  25.257  1.00 22.45           C  
-ATOM   3731  N   GLU B 231     -47.566  66.436  23.846  1.00 25.94           N  
-ATOM   3732  CA  GLU B 231     -48.999  66.628  23.662  1.00 27.20           C  
-ATOM   3733  C   GLU B 231     -49.688  66.058  24.917  1.00 28.24           C  
-ATOM   3734  O   GLU B 231     -50.467  66.736  25.585  1.00 30.33           O  
-ATOM   3735  CB  GLU B 231     -49.450  65.876  22.404  1.00 29.01           C  
-ATOM   3736  CG  GLU B 231     -50.176  66.713  21.344  1.00 34.05           C  
-ATOM   3737  CD  GLU B 231     -49.719  66.389  19.902  1.00 38.55           C  
-ATOM   3738  OE1 GLU B 231     -49.538  65.189  19.570  1.00 38.94           O  
-ATOM   3739  OE2 GLU B 231     -49.547  67.340  19.093  1.00 39.63           O  
-ATOM   3740  N   ALA B 232     -49.378  64.814  25.253  1.00 27.75           N  
-ATOM   3741  CA  ALA B 232     -49.965  64.178  26.423  1.00 26.88           C  
-ATOM   3742  C   ALA B 232     -49.679  64.965  27.700  1.00 27.68           C  
-ATOM   3743  O   ALA B 232     -50.576  65.197  28.516  1.00 28.80           O  
-ATOM   3744  CB  ALA B 232     -49.428  62.775  26.558  1.00 26.84           C  
-ATOM   3745  N   ALA B 233     -48.421  65.365  27.870  1.00 27.85           N  
-ATOM   3746  CA  ALA B 233     -47.994  66.119  29.052  1.00 26.20           C  
-ATOM   3747  C   ALA B 233     -48.762  67.426  29.221  1.00 25.36           C  
-ATOM   3748  O   ALA B 233     -48.987  67.874  30.349  1.00 23.56           O  
-ATOM   3749  CB  ALA B 233     -46.495  66.404  28.975  1.00 24.76           C  
-ATOM   3750  N   ILE B 234     -49.162  68.037  28.105  1.00 24.87           N  
-ATOM   3751  CA  ILE B 234     -49.890  69.294  28.169  1.00 24.65           C  
-ATOM   3752  C   ILE B 234     -51.168  69.098  28.960  1.00 26.55           C  
-ATOM   3753  O   ILE B 234     -51.453  69.866  29.882  1.00 25.99           O  
-ATOM   3754  CB  ILE B 234     -50.220  69.838  26.767  1.00 22.76           C  
-ATOM   3755  CG1 ILE B 234     -48.915  70.150  26.030  1.00 23.26           C  
-ATOM   3756  CG2 ILE B 234     -51.088  71.097  26.875  1.00 20.23           C  
-ATOM   3757  CD1 ILE B 234     -49.095  70.769  24.649  1.00 22.74           C  
-ATOM   3758  N   SER B 235     -51.928  68.063  28.610  1.00 29.10           N  
-ATOM   3759  CA  SER B 235     -53.182  67.769  29.306  1.00 31.56           C  
-ATOM   3760  C   SER B 235     -52.883  67.264  30.725  1.00 33.51           C  
-ATOM   3761  O   SER B 235     -53.421  67.775  31.717  1.00 34.01           O  
-ATOM   3762  CB  SER B 235     -53.991  66.706  28.545  1.00 30.02           C  
-ATOM   3763  OG  SER B 235     -54.230  67.089  27.205  1.00 29.26           O  
-ATOM   3764  N   GLU B 236     -52.014  66.265  30.821  1.00 34.05           N  
-ATOM   3765  CA  GLU B 236     -51.677  65.712  32.115  1.00 35.41           C  
-ATOM   3766  C   GLU B 236     -51.200  66.771  33.105  1.00 36.11           C  
-ATOM   3767  O   GLU B 236     -51.512  66.699  34.291  1.00 36.84           O  
-ATOM   3768  CB  GLU B 236     -50.619  64.629  31.956  1.00 36.91           C  
-ATOM   3769  CG  GLU B 236     -50.954  63.398  32.759  1.00 39.21           C  
-ATOM   3770  CD  GLU B 236     -52.348  62.893  32.450  1.00 40.07           C  
-ATOM   3771  OE1 GLU B 236     -52.616  62.584  31.261  1.00 40.24           O  
-ATOM   3772  OE2 GLU B 236     -53.168  62.816  33.396  1.00 39.31           O  
-ATOM   3773  N   LEU B 237     -50.442  67.753  32.628  1.00 36.64           N  
-ATOM   3774  CA  LEU B 237     -49.952  68.803  33.511  1.00 37.08           C  
-ATOM   3775  C   LEU B 237     -51.042  69.787  33.906  1.00 38.69           C  
-ATOM   3776  O   LEU B 237     -50.920  70.474  34.915  1.00 39.33           O  
-ATOM   3777  CB  LEU B 237     -48.798  69.567  32.865  1.00 35.59           C  
-ATOM   3778  CG  LEU B 237     -47.402  68.961  32.984  1.00 34.02           C  
-ATOM   3779  CD1 LEU B 237     -46.393  69.971  32.479  1.00 33.78           C  
-ATOM   3780  CD2 LEU B 237     -47.100  68.605  34.431  1.00 32.08           C  
-ATOM   3781  N   ARG B 238     -52.097  69.875  33.101  1.00 40.62           N  
-ATOM   3782  CA  ARG B 238     -53.207  70.773  33.408  1.00 41.73           C  
-ATOM   3783  C   ARG B 238     -54.043  70.085  34.460  1.00 44.40           C  
-ATOM   3784  O   ARG B 238     -54.411  70.681  35.473  1.00 44.71           O  
-ATOM   3785  CB  ARG B 238     -54.076  71.011  32.177  1.00 39.39           C  
-ATOM   3786  CG  ARG B 238     -55.450  71.556  32.501  1.00 36.42           C  
-ATOM   3787  CD  ARG B 238     -56.368  71.377  31.320  1.00 37.16           C  
-ATOM   3788  NE  ARG B 238     -56.552  72.603  30.551  1.00 36.83           N  
-ATOM   3789  CZ  ARG B 238     -57.468  73.523  30.833  1.00 36.44           C  
-ATOM   3790  NH1 ARG B 238     -58.282  73.353  31.866  1.00 34.92           N  
-ATOM   3791  NH2 ARG B 238     -57.574  74.609  30.077  1.00 36.29           N  
-ATOM   3792  N   SER B 239     -54.330  68.815  34.191  1.00 47.37           N  
-ATOM   3793  CA  SER B 239     -55.129  67.976  35.066  1.00 50.03           C  
-ATOM   3794  C   SER B 239     -54.521  67.924  36.453  1.00 52.12           C  
-ATOM   3795  O   SER B 239     -55.226  68.051  37.450  1.00 53.39           O  
-ATOM   3796  CB  SER B 239     -55.219  66.568  34.482  1.00 50.78           C  
-ATOM   3797  OG  SER B 239     -56.057  65.741  35.267  1.00 54.51           O  
-ATOM   3798  N   ALA B 240     -53.207  67.744  36.513  1.00 54.95           N  
-ATOM   3799  CA  ALA B 240     -52.500  67.674  37.784  1.00 57.40           C  
-ATOM   3800  C   ALA B 240     -52.162  69.069  38.304  1.00 59.63           C  
-ATOM   3801  O   ALA B 240     -51.490  69.210  39.322  1.00 60.07           O  
-ATOM   3802  CB  ALA B 240     -51.230  66.849  37.624  1.00 56.44           C  
-ATOM   3803  N   ASP B 241     -52.629  70.094  37.594  1.00 62.62           N  
-ATOM   3804  CA  ASP B 241     -52.390  71.492  37.957  1.00 65.03           C  
-ATOM   3805  C   ASP B 241     -50.899  71.846  38.045  1.00 65.57           C  
-ATOM   3806  O   ASP B 241     -50.534  72.971  38.396  1.00 65.41           O  
-ATOM   3807  CB  ASP B 241     -53.067  71.808  39.290  1.00 67.20           C  
-ATOM   3808  CG  ASP B 241     -53.319  73.289  39.472  1.00 70.44           C  
-ATOM   3809  OD1 ASP B 241     -54.225  73.817  38.788  1.00 72.15           O  
-ATOM   3810  OD2 ASP B 241     -52.609  73.926  40.285  1.00 71.82           O  
-ATOM   3811  N   LYS B 242     -50.048  70.879  37.718  1.00 66.10           N  
-ATOM   3812  CA  LYS B 242     -48.604  71.057  37.754  1.00 66.67           C  
-ATOM   3813  C   LYS B 242     -48.063  71.954  36.641  1.00 67.03           C  
-ATOM   3814  O   LYS B 242     -46.853  72.007  36.422  1.00 67.39           O  
-ATOM   3815  CB  LYS B 242     -47.910  69.697  37.681  1.00 67.62           C  
-ATOM   3816  CG  LYS B 242     -47.922  68.887  38.969  1.00 68.96           C  
-ATOM   3817  CD  LYS B 242     -46.901  69.418  39.964  1.00 70.83           C  
-ATOM   3818  CE  LYS B 242     -46.507  68.351  40.985  1.00 72.42           C  
-ATOM   3819  NZ  LYS B 242     -45.778  67.188  40.373  1.00 72.03           N  
-ATOM   3820  N   THR B 243     -48.944  72.642  35.921  1.00 67.42           N  
-ATOM   3821  CA  THR B 243     -48.481  73.542  34.870  1.00 67.27           C  
-ATOM   3822  C   THR B 243     -47.686  74.594  35.627  1.00 68.17           C  
-ATOM   3823  O   THR B 243     -47.923  74.796  36.819  1.00 69.81           O  
-ATOM   3824  CB  THR B 243     -49.653  74.232  34.146  1.00 66.67           C  
-ATOM   3825  OG1 THR B 243     -50.549  73.242  33.627  1.00 65.60           O  
-ATOM   3826  CG2 THR B 243     -49.133  75.087  33.000  1.00 65.18           C  
-ATOM   3827  N   HIS B 244     -46.752  75.262  34.957  1.00 67.60           N  
-ATOM   3828  CA  HIS B 244     -45.926  76.281  35.614  1.00 66.91           C  
-ATOM   3829  C   HIS B 244     -44.903  75.618  36.538  1.00 64.52           C  
-ATOM   3830  O   HIS B 244     -44.070  76.299  37.138  1.00 65.50           O  
-ATOM   3831  CB  HIS B 244     -46.771  77.240  36.471  1.00 69.39           C  
-ATOM   3832  CG  HIS B 244     -47.873  77.930  35.729  1.00 72.62           C  
-ATOM   3833  ND1 HIS B 244     -47.670  78.607  34.544  1.00 74.17           N  
-ATOM   3834  CD2 HIS B 244     -49.184  78.091  36.033  1.00 73.26           C  
-ATOM   3835  CE1 HIS B 244     -48.806  79.156  34.152  1.00 74.48           C  
-ATOM   3836  NE2 HIS B 244     -49.740  78.859  35.038  1.00 75.02           N  
-ATOM   3837  N   ASP B 245     -44.974  74.296  36.663  1.00 60.80           N  
-ATOM   3838  CA  ASP B 245     -44.055  73.568  37.531  1.00 56.88           C  
-ATOM   3839  C   ASP B 245     -43.123  72.654  36.752  1.00 52.55           C  
-ATOM   3840  O   ASP B 245     -42.037  72.323  37.230  1.00 53.89           O  
-ATOM   3841  CB  ASP B 245     -44.838  72.755  38.561  1.00 60.39           C  
-ATOM   3842  CG  ASP B 245     -45.636  73.633  39.515  1.00 63.99           C  
-ATOM   3843  OD1 ASP B 245     -46.427  73.074  40.310  1.00 66.39           O  
-ATOM   3844  OD2 ASP B 245     -45.472  74.876  39.475  1.00 65.05           O  
-ATOM   3845  N   ILE B 246     -43.551  72.244  35.560  1.00 46.08           N  
-ATOM   3846  CA  ILE B 246     -42.742  71.388  34.696  1.00 38.80           C  
-ATOM   3847  C   ILE B 246     -42.778  71.917  33.264  1.00 35.85           C  
-ATOM   3848  O   ILE B 246     -43.845  72.017  32.660  1.00 35.22           O  
-ATOM   3849  CB  ILE B 246     -43.253  69.952  34.694  1.00 37.24           C  
-ATOM   3850  CG1 ILE B 246     -43.283  69.414  36.115  1.00 36.24           C  
-ATOM   3851  CG2 ILE B 246     -42.350  69.077  33.849  1.00 36.31           C  
-ATOM   3852  CD1 ILE B 246     -43.746  67.978  36.192  1.00 37.76           C  
-ATOM   3853  N   GLY B 247     -41.609  72.261  32.731  1.00 33.08           N  
-ATOM   3854  CA  GLY B 247     -41.530  72.780  31.376  1.00 30.49           C  
-ATOM   3855  C   GLY B 247     -41.555  71.679  30.336  1.00 29.58           C  
-ATOM   3856  O   GLY B 247     -41.065  70.564  30.560  1.00 29.32           O  
-ATOM   3857  N   LEU B 248     -42.127  71.977  29.179  1.00 28.01           N  
-ATOM   3858  CA  LEU B 248     -42.195  70.970  28.136  1.00 26.24           C  
-ATOM   3859  C   LEU B 248     -41.361  71.332  26.922  1.00 25.07           C  
-ATOM   3860  O   LEU B 248     -41.507  72.413  26.361  1.00 25.57           O  
-ATOM   3861  CB  LEU B 248     -43.642  70.750  27.706  1.00 25.43           C  
-ATOM   3862  CG  LEU B 248     -44.608  70.392  28.830  1.00 24.85           C  
-ATOM   3863  CD1 LEU B 248     -45.975  70.082  28.237  1.00 25.39           C  
-ATOM   3864  CD2 LEU B 248     -44.069  69.205  29.606  1.00 24.63           C  
-ATOM   3865  N   VAL B 249     -40.472  70.425  26.536  1.00 23.52           N  
-ATOM   3866  CA  VAL B 249     -39.641  70.627  25.361  1.00 22.01           C  
-ATOM   3867  C   VAL B 249     -39.883  69.470  24.390  1.00 22.61           C  
-ATOM   3868  O   VAL B 249     -39.718  68.293  24.736  1.00 23.84           O  
-ATOM   3869  CB  VAL B 249     -38.153  70.672  25.710  1.00 19.27           C  
-ATOM   3870  CG1 VAL B 249     -37.344  70.780  24.439  1.00 18.97           C  
-ATOM   3871  CG2 VAL B 249     -37.870  71.852  26.604  1.00 18.01           C  
-ATOM   3872  N   SER B 250     -40.299  69.798  23.177  1.00 21.11           N  
-ATOM   3873  CA  SER B 250     -40.541  68.760  22.206  1.00 20.73           C  
-ATOM   3874  C   SER B 250     -39.305  68.582  21.355  1.00 20.81           C  
-ATOM   3875  O   SER B 250     -38.549  69.511  21.123  1.00 21.61           O  
-ATOM   3876  CB  SER B 250     -41.731  69.113  21.320  1.00 21.67           C  
-ATOM   3877  OG  SER B 250     -42.099  67.996  20.530  1.00 20.09           O  
-ATOM   3878  N   VAL B 251     -39.119  67.370  20.877  1.00 21.66           N  
-ATOM   3879  CA  VAL B 251     -37.985  67.038  20.058  1.00 21.57           C  
-ATOM   3880  C   VAL B 251     -38.329  67.161  18.554  1.00 23.55           C  
-ATOM   3881  O   VAL B 251     -37.470  66.958  17.688  1.00 24.18           O  
-ATOM   3882  CB  VAL B 251     -37.495  65.637  20.480  1.00 21.37           C  
-ATOM   3883  CG1 VAL B 251     -37.573  64.652  19.337  1.00 23.16           C  
-ATOM   3884  CG2 VAL B 251     -36.113  65.754  21.050  1.00 20.11           C  
-ATOM   3885  N   TYR B 252     -39.591  67.487  18.257  1.00 23.70           N  
-ATOM   3886  CA  TYR B 252     -40.052  67.717  16.883  1.00 24.30           C  
-ATOM   3887  C   TYR B 252     -41.459  68.328  16.873  1.00 24.69           C  
-ATOM   3888  O   TYR B 252     -42.135  68.353  17.898  1.00 24.13           O  
-ATOM   3889  CB  TYR B 252     -39.958  66.450  16.015  1.00 24.07           C  
-ATOM   3890  CG  TYR B 252     -40.967  65.375  16.286  1.00 26.34           C  
-ATOM   3891  CD1 TYR B 252     -42.214  65.383  15.656  1.00 27.86           C  
-ATOM   3892  CD2 TYR B 252     -40.683  64.346  17.177  1.00 28.10           C  
-ATOM   3893  CE1 TYR B 252     -43.160  64.387  15.914  1.00 28.64           C  
-ATOM   3894  CE2 TYR B 252     -41.618  63.346  17.445  1.00 30.70           C  
-ATOM   3895  CZ  TYR B 252     -42.855  63.374  16.815  1.00 30.37           C  
-ATOM   3896  OH  TYR B 252     -43.789  62.415  17.134  1.00 32.09           O  
-ATOM   3897  N   LEU B 253     -41.892  68.828  15.715  1.00 25.41           N  
-ATOM   3898  CA  LEU B 253     -43.171  69.526  15.598  1.00 24.98           C  
-ATOM   3899  C   LEU B 253     -44.398  68.758  15.140  1.00 26.93           C  
-ATOM   3900  O   LEU B 253     -44.295  67.704  14.507  1.00 28.45           O  
-ATOM   3901  CB  LEU B 253     -42.991  70.738  14.681  1.00 22.73           C  
-ATOM   3902  CG  LEU B 253     -44.184  71.684  14.568  1.00 22.33           C  
-ATOM   3903  CD1 LEU B 253     -44.550  72.183  15.960  1.00 22.08           C  
-ATOM   3904  CD2 LEU B 253     -43.853  72.851  13.646  1.00 21.56           C  
-ATOM   3905  N   SER B 254     -45.566  69.316  15.465  1.00 27.33           N  
-ATOM   3906  CA  SER B 254     -46.861  68.743  15.091  1.00 26.73           C  
-ATOM   3907  C   SER B 254     -47.972  69.715  15.500  1.00 27.87           C  
-ATOM   3908  O   SER B 254     -47.752  70.574  16.364  1.00 28.64           O  
-ATOM   3909  CB  SER B 254     -47.083  67.412  15.802  1.00 23.23           C  
-ATOM   3910  OG  SER B 254     -47.371  67.632  17.169  1.00 21.34           O  
-ATOM   3911  N   HIS B 255     -49.149  69.612  14.870  1.00 27.84           N  
-ATOM   3912  CA  HIS B 255     -50.249  70.482  15.268  1.00 26.66           C  
-ATOM   3913  C   HIS B 255     -50.457  69.941  16.661  1.00 27.09           C  
-ATOM   3914  O   HIS B 255     -50.414  68.714  16.863  1.00 28.67           O  
-ATOM   3915  CB  HIS B 255     -51.537  70.213  14.499  1.00 26.82           C  
-ATOM   3916  CG  HIS B 255     -51.375  70.083  13.022  1.00 25.70           C  
-ATOM   3917  ND1 HIS B 255     -51.099  68.882  12.412  1.00 27.09           N  
-ATOM   3918  CD2 HIS B 255     -51.553  70.980  12.025  1.00 26.58           C  
-ATOM   3919  CE1 HIS B 255     -51.120  69.041  11.101  1.00 27.94           C  
-ATOM   3920  NE2 HIS B 255     -51.394  70.306  10.840  1.00 28.09           N  
-ATOM   3921  N   GLY B 256     -50.703  70.805  17.628  1.00 24.25           N  
-ATOM   3922  CA  GLY B 256     -50.868  70.267  18.965  1.00 22.78           C  
-ATOM   3923  C   GLY B 256     -49.659  70.729  19.729  1.00 20.43           C  
-ATOM   3924  O   GLY B 256     -49.806  71.503  20.674  1.00 20.40           O  
-ATOM   3925  N   VAL B 257     -48.475  70.252  19.344  1.00 18.51           N  
-ATOM   3926  CA  VAL B 257     -47.253  70.740  19.975  1.00 19.18           C  
-ATOM   3927  C   VAL B 257     -47.175  72.215  19.522  1.00 20.75           C  
-ATOM   3928  O   VAL B 257     -46.810  73.114  20.292  1.00 19.93           O  
-ATOM   3929  CB  VAL B 257     -45.998  69.974  19.489  1.00 18.40           C  
-ATOM   3930  CG1 VAL B 257     -44.797  70.904  19.449  1.00 18.71           C  
-ATOM   3931  CG2 VAL B 257     -45.695  68.829  20.440  1.00 17.73           C  
-ATOM   3932  N   TYR B 258     -47.546  72.454  18.265  1.00 21.81           N  
-ATOM   3933  CA  TYR B 258     -47.552  73.803  17.721  1.00 21.51           C  
-ATOM   3934  C   TYR B 258     -48.564  74.643  18.484  1.00 20.87           C  
-ATOM   3935  O   TYR B 258     -48.221  75.670  19.063  1.00 20.90           O  
-ATOM   3936  CB  TYR B 258     -47.942  73.810  16.238  1.00 23.05           C  
-ATOM   3937  CG  TYR B 258     -48.186  75.217  15.709  1.00 24.55           C  
-ATOM   3938  CD1 TYR B 258     -47.141  76.136  15.611  1.00 26.83           C  
-ATOM   3939  CD2 TYR B 258     -49.460  75.638  15.343  1.00 23.39           C  
-ATOM   3940  CE1 TYR B 258     -47.358  77.441  15.161  1.00 28.46           C  
-ATOM   3941  CE2 TYR B 258     -49.690  76.934  14.896  1.00 25.80           C  
-ATOM   3942  CZ  TYR B 258     -48.636  77.835  14.804  1.00 28.74           C  
-ATOM   3943  OH  TYR B 258     -48.852  79.128  14.355  1.00 29.81           O  
-ATOM   3944  N   ARG B 259     -49.818  74.207  18.468  1.00 20.33           N  
-ATOM   3945  CA  ARG B 259     -50.861  74.946  19.150  1.00 19.79           C  
-ATOM   3946  C   ARG B 259     -50.459  75.101  20.615  1.00 19.69           C  
-ATOM   3947  O   ARG B 259     -50.781  76.109  21.247  1.00 18.33           O  
-ATOM   3948  CB  ARG B 259     -52.214  74.234  18.944  1.00 20.42           C  
-ATOM   3949  CG  ARG B 259     -52.941  73.724  20.163  1.00 21.55           C  
-ATOM   3950  CD  ARG B 259     -54.039  74.654  20.596  1.00 21.98           C  
-ATOM   3951  NE  ARG B 259     -54.432  74.485  22.004  1.00 28.39           N  
-ATOM   3952  CZ  ARG B 259     -53.866  73.667  22.900  1.00 29.17           C  
-ATOM   3953  NH1 ARG B 259     -52.847  72.880  22.588  1.00 30.25           N  
-ATOM   3954  NH2 ARG B 259     -54.310  73.659  24.144  1.00 30.05           N  
-ATOM   3955  N   GLY B 260     -49.709  74.126  21.134  1.00 20.00           N  
-ATOM   3956  CA  GLY B 260     -49.241  74.191  22.515  1.00 21.31           C  
-ATOM   3957  C   GLY B 260     -48.284  75.363  22.692  1.00 23.25           C  
-ATOM   3958  O   GLY B 260     -48.313  76.066  23.706  1.00 22.84           O  
-ATOM   3959  N   LEU B 261     -47.421  75.568  21.697  1.00 24.17           N  
-ATOM   3960  CA  LEU B 261     -46.470  76.680  21.702  1.00 23.36           C  
-ATOM   3961  C   LEU B 261     -47.276  77.971  21.629  1.00 24.14           C  
-ATOM   3962  O   LEU B 261     -47.154  78.853  22.472  1.00 24.78           O  
-ATOM   3963  CB  LEU B 261     -45.550  76.601  20.478  1.00 21.01           C  
-ATOM   3964  CG  LEU B 261     -44.412  75.587  20.546  1.00 20.86           C  
-ATOM   3965  CD1 LEU B 261     -43.886  75.207  19.158  1.00 17.71           C  
-ATOM   3966  CD2 LEU B 261     -43.321  76.194  21.405  1.00 21.89           C  
-ATOM   3967  N   LEU B 262     -48.111  78.063  20.602  1.00 25.55           N  
-ATOM   3968  CA  LEU B 262     -48.938  79.242  20.379  1.00 25.27           C  
-ATOM   3969  C   LEU B 262     -49.615  79.737  21.642  1.00 24.85           C  
-ATOM   3970  O   LEU B 262     -49.808  80.935  21.814  1.00 24.36           O  
-ATOM   3971  CB  LEU B 262     -50.018  78.947  19.332  1.00 23.65           C  
-ATOM   3972  CG  LEU B 262     -50.902  80.161  19.065  1.00 21.69           C  
-ATOM   3973  CD1 LEU B 262     -50.128  81.124  18.221  1.00 20.52           C  
-ATOM   3974  CD2 LEU B 262     -52.174  79.761  18.362  1.00 23.36           C  
-ATOM   3975  N   ARG B 263     -49.972  78.810  22.522  1.00 24.51           N  
-ATOM   3976  CA  ARG B 263     -50.673  79.162  23.743  1.00 25.28           C  
-ATOM   3977  C   ARG B 263     -49.835  79.023  24.997  1.00 26.84           C  
-ATOM   3978  O   ARG B 263     -50.363  78.766  26.073  1.00 28.20           O  
-ATOM   3979  CB  ARG B 263     -51.920  78.301  23.856  1.00 24.87           C  
-ATOM   3980  CG  ARG B 263     -52.836  78.421  22.650  1.00 23.76           C  
-ATOM   3981  CD  ARG B 263     -53.499  79.755  22.675  1.00 22.02           C  
-ATOM   3982  NE  ARG B 263     -54.219  79.908  23.930  1.00 21.82           N  
-ATOM   3983  CZ  ARG B 263     -54.265  81.033  24.628  1.00 22.47           C  
-ATOM   3984  NH1 ARG B 263     -53.630  82.108  24.193  1.00 21.71           N  
-ATOM   3985  NH2 ARG B 263     -54.950  81.081  25.762  1.00 24.37           N  
-ATOM   3986  N   ASN B 264     -48.528  79.207  24.842  1.00 28.99           N  
-ATOM   3987  CA  ASN B 264     -47.556  79.118  25.929  1.00 29.43           C  
-ATOM   3988  C   ASN B 264     -47.712  77.921  26.826  1.00 28.24           C  
-ATOM   3989  O   ASN B 264     -47.530  78.028  28.034  1.00 28.79           O  
-ATOM   3990  CB  ASN B 264     -47.582  80.374  26.792  1.00 32.70           C  
-ATOM   3991  CG  ASN B 264     -47.129  81.596  26.037  1.00 37.64           C  
-ATOM   3992  OD1 ASN B 264     -47.940  82.273  25.395  1.00 39.61           O  
-ATOM   3993  ND2 ASN B 264     -45.820  81.882  26.086  1.00 39.00           N  
-ATOM   3994  N   LYS B 265     -48.055  76.780  26.246  1.00 26.83           N  
-ATOM   3995  CA  LYS B 265     -48.206  75.573  27.033  1.00 25.47           C  
-ATOM   3996  C   LYS B 265     -46.991  74.693  26.762  1.00 26.31           C  
-ATOM   3997  O   LYS B 265     -46.825  73.631  27.362  1.00 27.91           O  
-ATOM   3998  CB  LYS B 265     -49.505  74.857  26.670  1.00 23.05           C  
-ATOM   3999  CG  LYS B 265     -50.774  75.642  27.029  1.00 22.93           C  
-ATOM   4000  CD  LYS B 265     -50.774  76.079  28.495  1.00 24.76           C  
-ATOM   4001  CE  LYS B 265     -52.130  75.841  29.164  1.00 24.96           C  
-ATOM   4002  NZ  LYS B 265     -53.222  76.571  28.465  1.00 28.63           N  
-ATOM   4003  N   VAL B 266     -46.139  75.165  25.855  1.00 25.68           N  
-ATOM   4004  CA  VAL B 266     -44.910  74.474  25.481  1.00 24.06           C  
-ATOM   4005  C   VAL B 266     -43.806  75.522  25.419  1.00 25.23           C  
-ATOM   4006  O   VAL B 266     -44.070  76.692  25.120  1.00 27.31           O  
-ATOM   4007  CB  VAL B 266     -45.045  73.785  24.114  1.00 21.63           C  
-ATOM   4008  CG1 VAL B 266     -43.706  73.234  23.677  1.00 19.08           C  
-ATOM   4009  CG2 VAL B 266     -46.074  72.661  24.208  1.00 21.56           C  
-ATOM   4010  N   LEU B 267     -42.575  75.110  25.708  1.00 23.54           N  
-ATOM   4011  CA  LEU B 267     -41.452  76.033  25.705  1.00 21.65           C  
-ATOM   4012  C   LEU B 267     -40.636  76.042  24.435  1.00 22.18           C  
-ATOM   4013  O   LEU B 267     -40.171  77.098  23.997  1.00 23.77           O  
-ATOM   4014  CB  LEU B 267     -40.507  75.727  26.861  1.00 20.87           C  
-ATOM   4015  CG  LEU B 267     -40.977  76.107  28.257  1.00 20.76           C  
-ATOM   4016  CD1 LEU B 267     -39.923  75.711  29.273  1.00 21.14           C  
-ATOM   4017  CD2 LEU B 267     -41.247  77.591  28.303  1.00 19.59           C  
-ATOM   4018  N   PHE B 268     -40.458  74.876  23.832  1.00 21.22           N  
-ATOM   4019  CA  PHE B 268     -39.626  74.805  22.647  1.00 20.61           C  
-ATOM   4020  C   PHE B 268     -39.871  73.572  21.801  1.00 20.64           C  
-ATOM   4021  O   PHE B 268     -40.290  72.532  22.299  1.00 22.81           O  
-ATOM   4022  CB  PHE B 268     -38.150  74.827  23.088  1.00 18.34           C  
-ATOM   4023  CG  PHE B 268     -37.165  74.598  21.967  1.00 15.87           C  
-ATOM   4024  CD1 PHE B 268     -36.614  75.680  21.274  1.00 12.04           C  
-ATOM   4025  CD2 PHE B 268     -36.809  73.296  21.585  1.00 13.35           C  
-ATOM   4026  CE1 PHE B 268     -35.731  75.473  20.225  1.00  9.86           C  
-ATOM   4027  CE2 PHE B 268     -35.925  73.081  20.533  1.00 11.00           C  
-ATOM   4028  CZ  PHE B 268     -35.385  74.171  19.853  1.00 10.53           C  
-ATOM   4029  N   ALA B 269     -39.580  73.699  20.514  1.00 19.91           N  
-ATOM   4030  CA  ALA B 269     -39.708  72.598  19.586  1.00 19.37           C  
-ATOM   4031  C   ALA B 269     -39.015  72.980  18.286  1.00 20.07           C  
-ATOM   4032  O   ALA B 269     -39.115  74.120  17.826  1.00 19.74           O  
-ATOM   4033  CB  ALA B 269     -41.165  72.292  19.337  1.00 21.24           C  
-ATOM   4034  N   PRO B 270     -38.266  72.041  17.694  1.00 21.31           N  
-ATOM   4035  CA  PRO B 270     -37.572  72.323  16.437  1.00 21.31           C  
-ATOM   4036  C   PRO B 270     -38.497  71.846  15.334  1.00 21.62           C  
-ATOM   4037  O   PRO B 270     -39.352  71.010  15.592  1.00 21.27           O  
-ATOM   4038  CB  PRO B 270     -36.338  71.449  16.545  1.00 21.51           C  
-ATOM   4039  CG  PRO B 270     -36.911  70.207  17.160  1.00 20.53           C  
-ATOM   4040  CD  PRO B 270     -37.808  70.757  18.262  1.00 21.54           C  
-ATOM   4041  N   THR B 271     -38.351  72.378  14.126  1.00 22.43           N  
-ATOM   4042  CA  THR B 271     -39.186  71.930  13.012  1.00 24.78           C  
-ATOM   4043  C   THR B 271     -38.303  71.463  11.903  1.00 25.99           C  
-ATOM   4044  O   THR B 271     -37.348  72.151  11.563  1.00 27.23           O  
-ATOM   4045  CB  THR B 271     -39.982  73.017  12.376  1.00 24.88           C  
-ATOM   4046  OG1 THR B 271     -40.723  73.710  13.375  1.00 31.09           O  
-ATOM   4047  CG2 THR B 271     -40.921  72.409  11.359  1.00 24.36           C  
-ATOM   4048  N   ASP B 272     -38.613  70.314  11.319  1.00 26.28           N  
-ATOM   4049  CA  ASP B 272     -37.792  69.862  10.224  1.00 27.72           C  
-ATOM   4050  C   ASP B 272     -38.579  70.007   8.921  1.00 28.19           C  
-ATOM   4051  O   ASP B 272     -38.397  69.245   7.971  1.00 28.72           O  
-ATOM   4052  CB  ASP B 272     -37.283  68.433  10.469  1.00 27.77           C  
-ATOM   4053  CG  ASP B 272     -38.357  67.389  10.335  1.00 29.95           C  
-ATOM   4054  OD1 ASP B 272     -38.035  66.201  10.560  1.00 30.00           O  
-ATOM   4055  OD2 ASP B 272     -39.510  67.740  10.002  1.00 32.26           O  
-ATOM   4056  N   LYS B 273     -39.458  71.011   8.906  1.00 28.15           N  
-ATOM   4057  CA  LYS B 273     -40.280  71.355   7.743  1.00 28.78           C  
-ATOM   4058  C   LYS B 273     -40.959  70.162   7.052  1.00 29.60           C  
-ATOM   4059  O   LYS B 273     -40.679  69.875   5.879  1.00 30.36           O  
-ATOM   4060  CB  LYS B 273     -39.402  72.090   6.733  1.00 27.93           C  
-ATOM   4061  CG  LYS B 273     -38.590  73.220   7.323  1.00 26.40           C  
-ATOM   4062  CD  LYS B 273     -39.361  74.525   7.286  1.00 27.13           C  
-ATOM   4063  CE  LYS B 273     -38.566  75.622   6.576  1.00 27.86           C  
-ATOM   4064  NZ  LYS B 273     -37.221  75.860   7.195  1.00 29.59           N  
-ATOM   4065  N   MET B 274     -41.863  69.485   7.759  1.00 29.35           N  
-ATOM   4066  CA  MET B 274     -42.538  68.317   7.199  1.00 28.20           C  
-ATOM   4067  C   MET B 274     -43.204  68.570   5.849  1.00 27.65           C  
-ATOM   4068  O   MET B 274     -43.153  67.722   4.952  1.00 28.21           O  
-ATOM   4069  CB  MET B 274     -43.583  67.779   8.173  1.00 29.15           C  
-ATOM   4070  CG  MET B 274     -43.034  67.304   9.494  1.00 28.95           C  
-ATOM   4071  SD  MET B 274     -42.757  68.659  10.633  1.00 30.38           S  
-ATOM   4072  CE  MET B 274     -44.461  69.073  11.089  1.00 27.78           C  
-ATOM   4073  N   VAL B 275     -43.844  69.725   5.707  1.00 25.68           N  
-ATOM   4074  CA  VAL B 275     -44.503  70.056   4.455  1.00 23.56           C  
-ATOM   4075  C   VAL B 275     -43.464  70.200   3.350  1.00 24.76           C  
-ATOM   4076  O   VAL B 275     -43.616  69.648   2.259  1.00 23.99           O  
-ATOM   4077  CB  VAL B 275     -45.320  71.363   4.588  1.00 21.70           C  
-ATOM   4078  CG1 VAL B 275     -45.592  71.959   3.221  1.00 21.16           C  
-ATOM   4079  CG2 VAL B 275     -46.637  71.075   5.312  1.00 18.98           C  
-ATOM   4080  N   GLN B 276     -42.391  70.921   3.647  1.00 26.78           N  
-ATOM   4081  CA  GLN B 276     -41.344  71.145   2.666  1.00 27.53           C  
-ATOM   4082  C   GLN B 276     -40.695  69.848   2.225  1.00 27.56           C  
-ATOM   4083  O   GLN B 276     -40.455  69.661   1.034  1.00 27.95           O  
-ATOM   4084  CB  GLN B 276     -40.289  72.100   3.223  1.00 29.41           C  
-ATOM   4085  CG  GLN B 276     -39.316  72.634   2.173  1.00 31.75           C  
-ATOM   4086  CD  GLN B 276     -38.657  73.930   2.611  1.00 33.01           C  
-ATOM   4087  OE1 GLN B 276     -37.853  73.949   3.545  1.00 32.44           O  
-ATOM   4088  NE2 GLN B 276     -39.011  75.028   1.945  1.00 34.13           N  
-ATOM   4089  N   GLN B 277     -40.405  68.948   3.162  1.00 27.88           N  
-ATOM   4090  CA  GLN B 277     -39.783  67.680   2.774  1.00 28.82           C  
-ATOM   4091  C   GLN B 277     -40.658  66.991   1.727  1.00 30.36           C  
-ATOM   4092  O   GLN B 277     -40.151  66.365   0.787  1.00 30.48           O  
-ATOM   4093  CB  GLN B 277     -39.611  66.751   3.971  1.00 26.77           C  
-ATOM   4094  CG  GLN B 277     -38.789  67.316   5.094  1.00 27.30           C  
-ATOM   4095  CD  GLN B 277     -38.217  66.231   5.998  1.00 29.78           C  
-ATOM   4096  OE1 GLN B 277     -37.829  66.499   7.135  1.00 31.88           O  
-ATOM   4097  NE2 GLN B 277     -38.151  65.000   5.490  1.00 29.77           N  
-ATOM   4098  N   GLY B 278     -41.975  67.122   1.902  1.00 31.01           N  
-ATOM   4099  CA  GLY B 278     -42.925  66.529   0.975  1.00 30.24           C  
-ATOM   4100  C   GLY B 278     -42.792  67.127  -0.411  1.00 29.88           C  
-ATOM   4101  O   GLY B 278     -42.789  66.400  -1.403  1.00 29.78           O  
-ATOM   4102  N   ARG B 279     -42.685  68.450  -0.485  1.00 29.68           N  
-ATOM   4103  CA  ARG B 279     -42.532  69.121  -1.769  1.00 31.27           C  
-ATOM   4104  C   ARG B 279     -41.231  68.679  -2.415  1.00 33.08           C  
-ATOM   4105  O   ARG B 279     -41.231  68.071  -3.489  1.00 34.58           O  
-ATOM   4106  CB  ARG B 279     -42.488  70.630  -1.591  1.00 29.19           C  
-ATOM   4107  CG  ARG B 279     -43.731  71.213  -1.018  1.00 29.93           C  
-ATOM   4108  CD  ARG B 279     -43.456  72.632  -0.620  1.00 33.58           C  
-ATOM   4109  NE  ARG B 279     -44.666  73.342  -0.232  1.00 34.90           N  
-ATOM   4110  CZ  ARG B 279     -45.727  73.464  -1.014  1.00 35.31           C  
-ATOM   4111  NH1 ARG B 279     -45.728  72.916  -2.223  1.00 34.37           N  
-ATOM   4112  NH2 ARG B 279     -46.779  74.146  -0.590  1.00 37.87           N  
-ATOM   4113  N   LEU B 280     -40.121  68.989  -1.753  1.00 33.56           N  
-ATOM   4114  CA  LEU B 280     -38.813  68.634  -2.270  1.00 34.67           C  
-ATOM   4115  C   LEU B 280     -38.821  67.266  -2.937  1.00 35.63           C  
-ATOM   4116  O   LEU B 280     -38.404  67.134  -4.088  1.00 37.40           O  
-ATOM   4117  CB  LEU B 280     -37.762  68.667  -1.155  1.00 34.68           C  
-ATOM   4118  CG  LEU B 280     -37.437  70.030  -0.532  1.00 34.09           C  
-ATOM   4119  CD1 LEU B 280     -36.273  69.881   0.443  1.00 32.05           C  
-ATOM   4120  CD2 LEU B 280     -37.095  71.028  -1.625  1.00 33.09           C  
-ATOM   4121  N   SER B 281     -39.310  66.249  -2.239  1.00 35.63           N  
-ATOM   4122  CA  SER B 281     -39.331  64.918  -2.829  1.00 35.97           C  
-ATOM   4123  C   SER B 281     -40.074  64.859  -4.165  1.00 36.34           C  
-ATOM   4124  O   SER B 281     -39.615  64.208  -5.105  1.00 36.18           O  
-ATOM   4125  CB  SER B 281     -39.921  63.912  -1.852  1.00 35.10           C  
-ATOM   4126  OG  SER B 281     -38.952  62.919  -1.575  1.00 35.50           O  
-ATOM   4127  N   VAL B 282     -41.216  65.531  -4.258  1.00 36.47           N  
-ATOM   4128  CA  VAL B 282     -41.966  65.544  -5.508  1.00 36.97           C  
-ATOM   4129  C   VAL B 282     -41.135  66.284  -6.545  1.00 36.12           C  
-ATOM   4130  O   VAL B 282     -40.977  65.819  -7.672  1.00 36.05           O  
-ATOM   4131  CB  VAL B 282     -43.330  66.239  -5.339  1.00 38.26           C  
-ATOM   4132  CG1 VAL B 282     -44.047  66.350  -6.680  1.00 36.78           C  
-ATOM   4133  CG2 VAL B 282     -44.171  65.447  -4.364  1.00 38.13           C  
-ATOM   4134  N   MET B 283     -40.592  67.432  -6.156  1.00 36.07           N  
-ATOM   4135  CA  MET B 283     -39.750  68.217  -7.058  1.00 37.38           C  
-ATOM   4136  C   MET B 283     -38.626  67.356  -7.629  1.00 38.27           C  
-ATOM   4137  O   MET B 283     -38.409  67.344  -8.842  1.00 39.10           O  
-ATOM   4138  CB  MET B 283     -39.155  69.419  -6.327  1.00 34.96           C  
-ATOM   4139  CG  MET B 283     -40.216  70.336  -5.800  1.00 35.77           C  
-ATOM   4140  SD  MET B 283     -39.562  71.640  -4.802  1.00 37.01           S  
-ATOM   4141  CE  MET B 283     -40.569  73.073  -5.326  1.00 34.37           C  
-ATOM   4142  N   GLN B 284     -37.906  66.642  -6.765  1.00 37.95           N  
-ATOM   4143  CA  GLN B 284     -36.841  65.787  -7.257  1.00 38.48           C  
-ATOM   4144  C   GLN B 284     -37.418  64.929  -8.377  1.00 39.98           C  
-ATOM   4145  O   GLN B 284     -37.099  65.117  -9.553  1.00 39.80           O  
-ATOM   4146  CB  GLN B 284     -36.317  64.868  -6.160  1.00 37.25           C  
-ATOM   4147  CG  GLN B 284     -35.679  65.567  -4.991  1.00 38.48           C  
-ATOM   4148  CD  GLN B 284     -35.003  64.583  -4.051  1.00 40.25           C  
-ATOM   4149  OE1 GLN B 284     -35.545  63.510  -3.762  1.00 42.63           O  
-ATOM   4150  NE2 GLN B 284     -33.821  64.945  -3.559  1.00 38.14           N  
-ATOM   4151  N   ALA B 285     -38.293  64.003  -7.992  1.00 41.41           N  
-ATOM   4152  CA  ALA B 285     -38.929  63.078  -8.921  1.00 41.51           C  
-ATOM   4153  C   ALA B 285     -39.385  63.726 -10.227  1.00 41.17           C  
-ATOM   4154  O   ALA B 285     -39.125  63.186 -11.302  1.00 42.15           O  
-ATOM   4155  CB  ALA B 285     -40.105  62.373  -8.232  1.00 41.43           C  
-ATOM   4156  N   ALA B 286     -40.056  64.873 -10.151  1.00 39.50           N  
-ATOM   4157  CA  ALA B 286     -40.518  65.533 -11.375  1.00 39.24           C  
-ATOM   4158  C   ALA B 286     -39.335  65.957 -12.223  1.00 38.92           C  
-ATOM   4159  O   ALA B 286     -39.261  65.633 -13.405  1.00 38.63           O  
-ATOM   4160  CB  ALA B 286     -41.374  66.747 -11.051  1.00 38.70           C  
-ATOM   4161  N   HIS B 287     -38.405  66.682 -11.607  1.00 39.30           N  
-ATOM   4162  CA  HIS B 287     -37.224  67.152 -12.311  1.00 38.30           C  
-ATOM   4163  C   HIS B 287     -36.481  66.013 -12.970  1.00 38.78           C  
-ATOM   4164  O   HIS B 287     -36.236  66.056 -14.165  1.00 39.52           O  
-ATOM   4165  CB  HIS B 287     -36.305  67.924 -11.365  1.00 35.56           C  
-ATOM   4166  CG  HIS B 287     -36.788  69.308 -11.073  1.00 34.25           C  
-ATOM   4167  ND1 HIS B 287     -35.940  70.335 -10.722  1.00 34.30           N  
-ATOM   4168  CD2 HIS B 287     -38.033  69.841 -11.101  1.00 34.94           C  
-ATOM   4169  CE1 HIS B 287     -36.641  71.443 -10.550  1.00 35.13           C  
-ATOM   4170  NE2 HIS B 287     -37.914  71.171 -10.774  1.00 35.12           N  
-ATOM   4171  N   TYR B 288     -36.131  64.991 -12.203  1.00 39.96           N  
-ATOM   4172  CA  TYR B 288     -35.438  63.843 -12.768  1.00 41.84           C  
-ATOM   4173  C   TYR B 288     -36.095  63.385 -14.078  1.00 42.74           C  
-ATOM   4174  O   TYR B 288     -35.455  63.360 -15.131  1.00 43.81           O  
-ATOM   4175  CB  TYR B 288     -35.457  62.694 -11.777  1.00 42.83           C  
-ATOM   4176  CG  TYR B 288     -34.857  61.422 -12.309  1.00 44.48           C  
-ATOM   4177  CD1 TYR B 288     -33.479  61.236 -12.329  1.00 44.96           C  
-ATOM   4178  CD2 TYR B 288     -35.671  60.383 -12.758  1.00 45.29           C  
-ATOM   4179  CE1 TYR B 288     -32.921  60.037 -12.773  1.00 46.02           C  
-ATOM   4180  CE2 TYR B 288     -35.123  59.182 -13.205  1.00 45.97           C  
-ATOM   4181  CZ  TYR B 288     -33.748  59.015 -13.208  1.00 45.53           C  
-ATOM   4182  OH  TYR B 288     -33.200  57.827 -13.634  1.00 44.89           O  
-ATOM   4183  N   LEU B 289     -37.374  63.030 -14.013  1.00 42.70           N  
-ATOM   4184  CA  LEU B 289     -38.096  62.566 -15.193  1.00 41.87           C  
-ATOM   4185  C   LEU B 289     -38.133  63.590 -16.326  1.00 42.58           C  
-ATOM   4186  O   LEU B 289     -38.098  63.221 -17.494  1.00 43.23           O  
-ATOM   4187  CB  LEU B 289     -39.521  62.161 -14.812  1.00 39.58           C  
-ATOM   4188  CG  LEU B 289     -39.630  61.049 -13.766  1.00 38.91           C  
-ATOM   4189  CD1 LEU B 289     -41.073  60.585 -13.670  1.00 38.10           C  
-ATOM   4190  CD2 LEU B 289     -38.729  59.886 -14.141  1.00 35.98           C  
-ATOM   4191  N   ARG B 290     -38.206  64.872 -15.983  1.00 43.39           N  
-ATOM   4192  CA  ARG B 290     -38.239  65.933 -16.986  1.00 44.11           C  
-ATOM   4193  C   ARG B 290     -36.836  66.426 -17.333  1.00 46.33           C  
-ATOM   4194  O   ARG B 290     -36.670  67.498 -17.932  1.00 45.76           O  
-ATOM   4195  CB  ARG B 290     -39.062  67.107 -16.481  1.00 42.70           C  
-ATOM   4196  CG  ARG B 290     -40.500  66.765 -16.240  1.00 43.67           C  
-ATOM   4197  CD  ARG B 290     -41.238  67.946 -15.674  1.00 44.64           C  
-ATOM   4198  NE  ARG B 290     -42.627  67.613 -15.402  1.00 45.23           N  
-ATOM   4199  CZ  ARG B 290     -43.460  68.398 -14.733  1.00 46.92           C  
-ATOM   4200  NH1 ARG B 290     -43.038  69.569 -14.263  1.00 48.22           N  
-ATOM   4201  NH2 ARG B 290     -44.714  68.011 -14.536  1.00 46.52           N  
-ATOM   4202  N   HIS B 291     -35.833  65.639 -16.948  1.00 47.80           N  
-ATOM   4203  CA  HIS B 291     -34.440  65.981 -17.199  1.00 48.54           C  
-ATOM   4204  C   HIS B 291     -34.160  67.449 -16.843  1.00 48.66           C  
-ATOM   4205  O   HIS B 291     -33.877  68.271 -17.714  1.00 49.46           O  
-ATOM   4206  CB  HIS B 291     -34.102  65.714 -18.670  1.00 49.90           C  
-ATOM   4207  CG  HIS B 291     -34.259  64.280 -19.079  1.00 51.05           C  
-ATOM   4208  ND1 HIS B 291     -33.467  63.268 -18.575  1.00 52.02           N  
-ATOM   4209  CD2 HIS B 291     -35.113  63.691 -19.950  1.00 50.67           C  
-ATOM   4210  CE1 HIS B 291     -33.825  62.118 -19.119  1.00 51.56           C  
-ATOM   4211  NE2 HIS B 291     -34.822  62.347 -19.957  1.00 52.07           N  
-ATOM   4212  N   GLN B 292     -34.260  67.769 -15.555  1.00 47.63           N  
-ATOM   4213  CA  GLN B 292     -34.002  69.117 -15.056  1.00 46.31           C  
-ATOM   4214  C   GLN B 292     -32.997  68.959 -13.910  1.00 47.44           C  
-ATOM   4215  O   GLN B 292     -32.770  67.836 -13.436  1.00 47.07           O  
-ATOM   4216  CB  GLN B 292     -35.303  69.756 -14.548  1.00 43.83           C  
-ATOM   4217  CG  GLN B 292     -36.401  69.814 -15.594  1.00 43.01           C  
-ATOM   4218  CD  GLN B 292     -37.642  70.572 -15.141  1.00 42.08           C  
-ATOM   4219  OE1 GLN B 292     -38.413  70.095 -14.311  1.00 43.99           O  
-ATOM   4220  NE2 GLN B 292     -37.840  71.760 -15.693  1.00 39.91           N  
-ATOM   4221  N   PRO B 293     -32.378  70.070 -13.456  1.00 47.81           N  
-ATOM   4222  CA  PRO B 293     -31.392  70.060 -12.362  1.00 47.17           C  
-ATOM   4223  C   PRO B 293     -32.081  69.945 -10.999  1.00 47.04           C  
-ATOM   4224  O   PRO B 293     -33.131  70.554 -10.779  1.00 47.41           O  
-ATOM   4225  CB  PRO B 293     -30.684  71.414 -12.498  1.00 47.49           C  
-ATOM   4226  CG  PRO B 293     -31.215  72.021 -13.798  1.00 49.36           C  
-ATOM   4227  CD  PRO B 293     -32.587  71.441 -13.947  1.00 48.88           C  
-ATOM   4228  N   TYR B 294     -31.493  69.183 -10.080  1.00 46.02           N  
-ATOM   4229  CA  TYR B 294     -32.079  69.033  -8.748  1.00 44.30           C  
-ATOM   4230  C   TYR B 294     -31.067  68.460  -7.763  1.00 43.99           C  
-ATOM   4231  O   TYR B 294     -30.271  67.601  -8.132  1.00 44.19           O  
-ATOM   4232  CB  TYR B 294     -33.316  68.130  -8.824  1.00 41.98           C  
-ATOM   4233  CG  TYR B 294     -33.028  66.661  -9.036  1.00 37.82           C  
-ATOM   4234  CD1 TYR B 294     -32.589  65.861  -7.987  1.00 36.37           C  
-ATOM   4235  CD2 TYR B 294     -33.212  66.067 -10.280  1.00 36.86           C  
-ATOM   4236  CE1 TYR B 294     -32.339  64.505  -8.167  1.00 35.98           C  
-ATOM   4237  CE2 TYR B 294     -32.968  64.708 -10.471  1.00 36.23           C  
-ATOM   4238  CZ  TYR B 294     -32.530  63.935  -9.407  1.00 35.61           C  
-ATOM   4239  OH  TYR B 294     -32.280  62.593  -9.576  1.00 34.65           O  
-ATOM   4240  N   GLU B 295     -31.091  68.925  -6.516  1.00 43.99           N  
-ATOM   4241  CA  GLU B 295     -30.140  68.414  -5.534  1.00 45.60           C  
-ATOM   4242  C   GLU B 295     -30.424  66.946  -5.256  1.00 45.12           C  
-ATOM   4243  O   GLU B 295     -31.518  66.599  -4.833  1.00 45.82           O  
-ATOM   4244  CB  GLU B 295     -30.207  69.213  -4.230  1.00 46.90           C  
-ATOM   4245  CG  GLU B 295     -29.070  68.843  -3.284  1.00 54.29           C  
-ATOM   4246  CD  GLU B 295     -28.992  69.713  -2.036  1.00 58.08           C  
-ATOM   4247  OE1 GLU B 295     -28.059  69.488  -1.221  1.00 58.73           O  
-ATOM   4248  OE2 GLU B 295     -29.855  70.610  -1.871  1.00 59.70           O  
-ATOM   4249  N   LYS B 296     -29.444  66.080  -5.498  1.00 45.53           N  
-ATOM   4250  CA  LYS B 296     -29.641  64.648  -5.278  1.00 45.57           C  
-ATOM   4251  C   LYS B 296     -29.912  64.312  -3.820  1.00 44.11           C  
-ATOM   4252  O   LYS B 296     -30.573  63.321  -3.515  1.00 42.80           O  
-ATOM   4253  CB  LYS B 296     -28.435  63.851  -5.789  1.00 48.09           C  
-ATOM   4254  CG  LYS B 296     -28.414  63.650  -7.308  1.00 52.19           C  
-ATOM   4255  CD  LYS B 296     -27.128  62.945  -7.786  1.00 56.22           C  
-ATOM   4256  CE  LYS B 296     -27.091  61.441  -7.461  1.00 58.26           C  
-ATOM   4257  NZ  LYS B 296     -27.912  60.613  -8.400  1.00 58.69           N  
-ATOM   4258  N   GLN B 297     -29.401  65.142  -2.921  1.00 43.46           N  
-ATOM   4259  CA  GLN B 297     -29.607  64.929  -1.499  1.00 43.48           C  
-ATOM   4260  C   GLN B 297     -30.035  66.207  -0.842  1.00 42.64           C  
-ATOM   4261  O   GLN B 297     -29.238  66.865  -0.181  1.00 43.55           O  
-ATOM   4262  CB  GLN B 297     -28.340  64.444  -0.821  1.00 45.56           C  
-ATOM   4263  CG  GLN B 297     -27.984  63.018  -1.128  1.00 51.19           C  
-ATOM   4264  CD  GLN B 297     -26.961  62.484  -0.155  1.00 54.89           C  
-ATOM   4265  OE1 GLN B 297     -25.878  63.060   0.001  1.00 57.13           O  
-ATOM   4266  NE2 GLN B 297     -27.297  61.380   0.516  1.00 56.52           N  
-ATOM   4267  N   ALA B 298     -31.298  66.560  -1.031  1.00 42.17           N  
-ATOM   4268  CA  ALA B 298     -31.840  67.772  -0.446  1.00 41.01           C  
-ATOM   4269  C   ALA B 298     -32.289  67.502   0.980  1.00 40.77           C  
-ATOM   4270  O   ALA B 298     -32.533  66.359   1.371  1.00 39.57           O  
-ATOM   4271  CB  ALA B 298     -33.002  68.273  -1.272  1.00 41.70           C  
-ATOM   4272  N   SER B 299     -32.387  68.571   1.756  1.00 40.71           N  
-ATOM   4273  CA  SER B 299     -32.803  68.474   3.145  1.00 40.92           C  
-ATOM   4274  C   SER B 299     -33.136  69.878   3.617  1.00 39.43           C  
-ATOM   4275  O   SER B 299     -32.323  70.795   3.490  1.00 40.36           O  
-ATOM   4276  CB  SER B 299     -31.677  67.885   4.000  1.00 41.39           C  
-ATOM   4277  OG  SER B 299     -30.596  68.790   4.108  1.00 44.14           O  
-ATOM   4278  N   PRO B 300     -34.343  70.070   4.158  1.00 38.03           N  
-ATOM   4279  CA  PRO B 300     -34.703  71.404   4.620  1.00 37.49           C  
-ATOM   4280  C   PRO B 300     -33.753  71.827   5.720  1.00 36.88           C  
-ATOM   4281  O   PRO B 300     -32.861  71.068   6.109  1.00 36.43           O  
-ATOM   4282  CB  PRO B 300     -36.135  71.220   5.109  1.00 37.76           C  
-ATOM   4283  CG  PRO B 300     -36.110  69.839   5.650  1.00 37.80           C  
-ATOM   4284  CD  PRO B 300     -35.350  69.085   4.579  1.00 38.12           C  
-ATOM   4285  N   ILE B 301     -33.948  73.044   6.209  1.00 36.63           N  
-ATOM   4286  CA  ILE B 301     -33.115  73.585   7.269  1.00 36.13           C  
-ATOM   4287  C   ILE B 301     -33.909  73.652   8.560  1.00 35.24           C  
-ATOM   4288  O   ILE B 301     -34.884  74.409   8.668  1.00 34.84           O  
-ATOM   4289  CB  ILE B 301     -32.604  75.000   6.912  1.00 36.51           C  
-ATOM   4290  CG1 ILE B 301     -31.662  74.916   5.714  1.00 36.94           C  
-ATOM   4291  CG2 ILE B 301     -31.883  75.617   8.095  1.00 33.70           C  
-ATOM   4292  CD1 ILE B 301     -31.277  76.268   5.165  1.00 40.73           C  
-ATOM   4293  N   ILE B 302     -33.480  72.844   9.528  1.00 33.78           N  
-ATOM   4294  CA  ILE B 302     -34.112  72.788  10.832  1.00 32.18           C  
-ATOM   4295  C   ILE B 302     -34.216  74.193  11.387  1.00 32.86           C  
-ATOM   4296  O   ILE B 302     -33.312  74.995  11.209  1.00 35.08           O  
-ATOM   4297  CB  ILE B 302     -33.299  71.948  11.790  1.00 30.01           C  
-ATOM   4298  CG1 ILE B 302     -33.320  70.484  11.326  1.00 29.64           C  
-ATOM   4299  CG2 ILE B 302     -33.822  72.156  13.196  1.00 29.60           C  
-ATOM   4300  CD1 ILE B 302     -32.471  69.534  12.164  1.00 27.03           C  
-ATOM   4301  N   LYS B 303     -35.314  74.493  12.061  1.00 32.67           N  
-ATOM   4302  CA  LYS B 303     -35.506  75.823  12.603  1.00 32.93           C  
-ATOM   4303  C   LYS B 303     -36.094  75.700  14.011  1.00 32.10           C  
-ATOM   4304  O   LYS B 303     -37.010  74.912  14.246  1.00 33.58           O  
-ATOM   4305  CB  LYS B 303     -36.437  76.595  11.667  1.00 35.37           C  
-ATOM   4306  CG  LYS B 303     -36.557  78.074  11.945  1.00 40.25           C  
-ATOM   4307  CD  LYS B 303     -35.948  78.899  10.809  1.00 44.51           C  
-ATOM   4308  CE  LYS B 303     -36.118  80.406  11.069  1.00 46.38           C  
-ATOM   4309  NZ  LYS B 303     -35.410  81.259  10.069  1.00 47.89           N  
-ATOM   4310  N   PRO B 304     -35.554  76.454  14.979  1.00 30.34           N  
-ATOM   4311  CA  PRO B 304     -36.075  76.375  16.341  1.00 28.62           C  
-ATOM   4312  C   PRO B 304     -37.341  77.195  16.522  1.00 27.33           C  
-ATOM   4313  O   PRO B 304     -37.476  78.279  15.949  1.00 28.00           O  
-ATOM   4314  CB  PRO B 304     -34.922  76.911  17.168  1.00 27.46           C  
-ATOM   4315  CG  PRO B 304     -34.393  77.965  16.300  1.00 27.91           C  
-ATOM   4316  CD  PRO B 304     -34.344  77.291  14.950  1.00 29.92           C  
-ATOM   4317  N   LEU B 305     -38.261  76.670  17.325  1.00 24.85           N  
-ATOM   4318  CA  LEU B 305     -39.520  77.347  17.595  1.00 23.93           C  
-ATOM   4319  C   LEU B 305     -39.806  77.580  19.088  1.00 24.40           C  
-ATOM   4320  O   LEU B 305     -39.669  76.672  19.926  1.00 24.20           O  
-ATOM   4321  CB  LEU B 305     -40.681  76.554  16.983  1.00 23.24           C  
-ATOM   4322  CG  LEU B 305     -40.889  76.585  15.474  1.00 21.50           C  
-ATOM   4323  CD1 LEU B 305     -42.077  75.726  15.118  1.00 21.31           C  
-ATOM   4324  CD2 LEU B 305     -41.136  78.006  15.022  1.00 22.33           C  
-ATOM   4325  N   THR B 306     -40.202  78.806  19.415  1.00 23.90           N  
-ATOM   4326  CA  THR B 306     -40.554  79.158  20.785  1.00 25.18           C  
-ATOM   4327  C   THR B 306     -41.829  79.979  20.654  1.00 26.14           C  
-ATOM   4328  O   THR B 306     -42.068  80.589  19.624  1.00 26.02           O  
-ATOM   4329  CB  THR B 306     -39.480  80.013  21.459  1.00 23.90           C  
-ATOM   4330  OG1 THR B 306     -39.594  81.364  21.005  1.00 25.57           O  
-ATOM   4331  CG2 THR B 306     -38.110  79.494  21.116  1.00 23.36           C  
-ATOM   4332  N   PRO B 307     -42.663  80.011  21.694  1.00 27.09           N  
-ATOM   4333  CA  PRO B 307     -43.898  80.788  21.587  1.00 28.25           C  
-ATOM   4334  C   PRO B 307     -43.772  82.162  20.934  1.00 29.83           C  
-ATOM   4335  O   PRO B 307     -44.556  82.505  20.048  1.00 30.87           O  
-ATOM   4336  CB  PRO B 307     -44.391  80.857  23.030  1.00 28.05           C  
-ATOM   4337  CG  PRO B 307     -43.135  80.671  23.832  1.00 30.55           C  
-ATOM   4338  CD  PRO B 307     -42.432  79.584  23.078  1.00 27.43           C  
-ATOM   4339  N   LYS B 308     -42.786  82.948  21.338  1.00 32.18           N  
-ATOM   4340  CA  LYS B 308     -42.646  84.277  20.756  1.00 34.14           C  
-ATOM   4341  C   LYS B 308     -41.970  84.303  19.395  1.00 34.72           C  
-ATOM   4342  O   LYS B 308     -41.702  85.374  18.868  1.00 35.60           O  
-ATOM   4343  CB  LYS B 308     -41.877  85.202  21.699  1.00 35.96           C  
-ATOM   4344  CG  LYS B 308     -42.615  85.619  22.960  1.00 39.85           C  
-ATOM   4345  CD  LYS B 308     -41.784  86.655  23.723  1.00 45.34           C  
-ATOM   4346  CE  LYS B 308     -42.396  87.026  25.071  1.00 48.82           C  
-ATOM   4347  NZ  LYS B 308     -42.432  85.863  26.026  1.00 52.36           N  
-ATOM   4348  N   THR B 309     -41.706  83.148  18.802  1.00 35.60           N  
-ATOM   4349  CA  THR B 309     -41.028  83.154  17.512  1.00 36.28           C  
-ATOM   4350  C   THR B 309     -41.620  82.246  16.422  1.00 37.32           C  
-ATOM   4351  O   THR B 309     -40.879  81.678  15.611  1.00 36.84           O  
-ATOM   4352  CB  THR B 309     -39.525  82.825  17.710  1.00 36.40           C  
-ATOM   4353  OG1 THR B 309     -39.336  81.416  17.895  1.00 37.84           O  
-ATOM   4354  CG2 THR B 309     -39.012  83.523  18.943  1.00 35.70           C  
-ATOM   4355  N   LEU B 310     -42.947  82.123  16.394  1.00 38.31           N  
-ATOM   4356  CA  LEU B 310     -43.623  81.298  15.388  1.00 40.93           C  
-ATOM   4357  C   LEU B 310     -43.835  82.101  14.091  1.00 44.77           C  
-ATOM   4358  O   LEU B 310     -44.865  82.758  13.913  1.00 45.16           O  
-ATOM   4359  CB  LEU B 310     -44.981  80.838  15.921  1.00 38.85           C  
-ATOM   4360  CG  LEU B 310     -45.081  80.206  17.309  1.00 36.98           C  
-ATOM   4361  CD1 LEU B 310     -46.532  79.903  17.608  1.00 35.17           C  
-ATOM   4362  CD2 LEU B 310     -44.258  78.930  17.375  1.00 37.79           C  
-ATOM   4363  N   HIS B 311     -42.872  82.048  13.177  1.00 49.09           N  
-ATOM   4364  CA  HIS B 311     -42.987  82.809  11.934  1.00 52.78           C  
-ATOM   4365  C   HIS B 311     -43.861  82.124  10.902  1.00 54.01           C  
-ATOM   4366  O   HIS B 311     -43.588  80.996  10.508  1.00 54.40           O  
-ATOM   4367  CB  HIS B 311     -41.601  83.074  11.343  1.00 54.45           C  
-ATOM   4368  CG  HIS B 311     -40.693  83.821  12.269  1.00 56.83           C  
-ATOM   4369  ND1 HIS B 311     -41.100  84.941  12.964  1.00 56.99           N  
-ATOM   4370  CD2 HIS B 311     -39.407  83.599  12.631  1.00 57.08           C  
-ATOM   4371  CE1 HIS B 311     -40.105  85.374  13.717  1.00 58.11           C  
-ATOM   4372  NE2 HIS B 311     -39.067  84.577  13.534  1.00 58.44           N  
-ATOM   4373  N   ASP B 312     -44.909  82.819  10.466  1.00 55.44           N  
-ATOM   4374  CA  ASP B 312     -45.834  82.274   9.484  1.00 57.42           C  
-ATOM   4375  C   ASP B 312     -45.152  81.448   8.406  1.00 57.55           C  
-ATOM   4376  O   ASP B 312     -45.383  80.247   8.312  1.00 57.23           O  
-ATOM   4377  CB  ASP B 312     -46.655  83.391   8.839  1.00 59.87           C  
-ATOM   4378  CG  ASP B 312     -47.734  83.928   9.766  1.00 62.71           C  
-ATOM   4379  OD1 ASP B 312     -48.489  83.105  10.327  1.00 65.03           O  
-ATOM   4380  OD2 ASP B 312     -47.834  85.165   9.931  1.00 63.65           O  
-ATOM   4381  N   ASP B 313     -44.299  82.069   7.602  1.00 58.59           N  
-ATOM   4382  CA  ASP B 313     -43.629  81.318   6.548  1.00 60.02           C  
-ATOM   4383  C   ASP B 313     -42.889  80.074   7.058  1.00 58.50           C  
-ATOM   4384  O   ASP B 313     -42.716  79.114   6.308  1.00 58.97           O  
-ATOM   4385  CB  ASP B 313     -42.681  82.225   5.720  1.00 63.34           C  
-ATOM   4386  CG  ASP B 313     -41.538  82.825   6.542  1.00 66.64           C  
-ATOM   4387  OD1 ASP B 313     -41.817  83.559   7.518  1.00 69.27           O  
-ATOM   4388  OD2 ASP B 313     -40.355  82.575   6.200  1.00 67.11           O  
-ATOM   4389  N   THR B 314     -42.474  80.069   8.325  1.00 56.59           N  
-ATOM   4390  CA  THR B 314     -41.759  78.908   8.872  1.00 54.19           C  
-ATOM   4391  C   THR B 314     -42.699  77.734   9.138  1.00 52.07           C  
-ATOM   4392  O   THR B 314     -42.337  76.584   8.898  1.00 51.68           O  
-ATOM   4393  CB  THR B 314     -40.997  79.238  10.190  1.00 54.15           C  
-ATOM   4394  OG1 THR B 314     -40.061  80.297   9.959  1.00 55.04           O  
-ATOM   4395  CG2 THR B 314     -40.222  78.022  10.672  1.00 52.33           C  
-ATOM   4396  N   ILE B 315     -43.903  78.010   9.632  1.00 49.63           N  
-ATOM   4397  CA  ILE B 315     -44.833  76.923   9.888  1.00 46.97           C  
-ATOM   4398  C   ILE B 315     -45.542  76.488   8.602  1.00 46.38           C  
-ATOM   4399  O   ILE B 315     -45.856  75.313   8.450  1.00 46.73           O  
-ATOM   4400  CB  ILE B 315     -45.863  77.289  10.976  1.00 44.78           C  
-ATOM   4401  CG1 ILE B 315     -46.766  78.400  10.482  1.00 46.63           C  
-ATOM   4402  CG2 ILE B 315     -45.153  77.743  12.237  1.00 42.58           C  
-ATOM   4403  CD1 ILE B 315     -47.804  78.817  11.502  1.00 50.84           C  
-ATOM   4404  N   GLU B 316     -45.766  77.414   7.669  1.00 45.92           N  
-ATOM   4405  CA  GLU B 316     -46.419  77.080   6.397  1.00 46.06           C  
-ATOM   4406  C   GLU B 316     -45.657  75.961   5.677  1.00 43.85           C  
-ATOM   4407  O   GLU B 316     -46.215  75.256   4.836  1.00 43.07           O  
-ATOM   4408  CB  GLU B 316     -46.448  78.286   5.460  1.00 50.89           C  
-ATOM   4409  CG  GLU B 316     -46.713  79.624   6.120  1.00 59.42           C  
-ATOM   4410  CD  GLU B 316     -48.180  80.034   6.106  1.00 64.38           C  
-ATOM   4411  OE1 GLU B 316     -48.756  80.149   4.994  1.00 65.21           O  
-ATOM   4412  OE2 GLU B 316     -48.750  80.253   7.206  1.00 66.75           O  
-ATOM   4413  N   GLU B 317     -44.373  75.818   5.986  1.00 41.46           N  
-ATOM   4414  CA  GLU B 317     -43.560  74.783   5.359  1.00 39.79           C  
-ATOM   4415  C   GLU B 317     -43.384  73.589   6.296  1.00 37.77           C  
-ATOM   4416  O   GLU B 317     -42.622  72.661   6.002  1.00 37.63           O  
-ATOM   4417  CB  GLU B 317     -42.170  75.324   4.989  1.00 42.17           C  
-ATOM   4418  CG  GLU B 317     -42.007  76.840   5.029  1.00 44.55           C  
-ATOM   4419  CD  GLU B 317     -40.641  77.294   4.508  1.00 47.45           C  
-ATOM   4420  OE1 GLU B 317     -40.388  77.148   3.290  1.00 49.04           O  
-ATOM   4421  OE2 GLU B 317     -39.815  77.789   5.310  1.00 47.74           O  
-ATOM   4422  N   SER B 318     -44.084  73.612   7.427  1.00 34.13           N  
-ATOM   4423  CA  SER B 318     -43.975  72.529   8.394  1.00 31.07           C  
-ATOM   4424  C   SER B 318     -45.270  71.737   8.578  1.00 29.57           C  
-ATOM   4425  O   SER B 318     -45.274  70.507   8.454  1.00 28.64           O  
-ATOM   4426  CB  SER B 318     -43.532  73.095   9.739  1.00 30.47           C  
-ATOM   4427  OG  SER B 318     -42.420  73.950   9.572  1.00 28.28           O  
-ATOM   4428  N   LEU B 319     -46.361  72.450   8.858  1.00 26.51           N  
-ATOM   4429  CA  LEU B 319     -47.660  71.832   9.097  1.00 25.12           C  
-ATOM   4430  C   LEU B 319     -48.709  72.071   8.016  1.00 26.71           C  
-ATOM   4431  O   LEU B 319     -48.770  73.146   7.422  1.00 27.87           O  
-ATOM   4432  CB  LEU B 319     -48.214  72.331  10.433  1.00 21.36           C  
-ATOM   4433  CG  LEU B 319     -47.392  71.967  11.670  1.00 20.78           C  
-ATOM   4434  CD1 LEU B 319     -47.840  72.790  12.881  1.00 16.71           C  
-ATOM   4435  CD2 LEU B 319     -47.523  70.463  11.924  1.00 17.65           C  
-ATOM   4436  N   SER B 320     -49.546  71.062   7.776  1.00 26.97           N  
-ATOM   4437  CA  SER B 320     -50.625  71.171   6.798  1.00 25.60           C  
-ATOM   4438  C   SER B 320     -51.603  72.228   7.309  1.00 26.59           C  
-ATOM   4439  O   SER B 320     -51.703  72.454   8.518  1.00 26.60           O  
-ATOM   4440  CB  SER B 320     -51.355  69.837   6.680  1.00 26.22           C  
-ATOM   4441  OG  SER B 320     -52.077  69.541   7.865  1.00 23.99           O  
-ATOM   4442  N   PRO B 321     -52.340  72.891   6.402  1.00 27.82           N  
-ATOM   4443  CA  PRO B 321     -53.309  73.926   6.794  1.00 27.81           C  
-ATOM   4444  C   PRO B 321     -54.462  73.281   7.539  1.00 31.06           C  
-ATOM   4445  O   PRO B 321     -54.636  72.062   7.471  1.00 33.42           O  
-ATOM   4446  CB  PRO B 321     -53.763  74.501   5.467  1.00 25.78           C  
-ATOM   4447  CG  PRO B 321     -52.626  74.180   4.539  1.00 27.79           C  
-ATOM   4448  CD  PRO B 321     -52.253  72.790   4.940  1.00 26.75           C  
-ATOM   4449  N   SER B 322     -55.253  74.078   8.249  1.00 33.35           N  
-ATOM   4450  CA  SER B 322     -56.374  73.516   8.989  1.00 35.12           C  
-ATOM   4451  C   SER B 322     -57.410  73.076   7.984  1.00 37.81           C  
-ATOM   4452  O   SER B 322     -57.397  73.502   6.833  1.00 37.66           O  
-ATOM   4453  CB  SER B 322     -56.996  74.544   9.925  1.00 34.25           C  
-ATOM   4454  OG  SER B 322     -57.824  75.434   9.203  1.00 33.78           O  
-ATOM   4455  N   GLU B 323     -58.320  72.228   8.433  1.00 41.90           N  
-ATOM   4456  CA  GLU B 323     -59.374  71.698   7.579  1.00 46.11           C  
-ATOM   4457  C   GLU B 323     -58.835  70.768   6.487  1.00 45.95           C  
-ATOM   4458  O   GLU B 323     -59.517  69.797   6.141  1.00 48.83           O  
-ATOM   4459  CB  GLU B 323     -60.219  72.827   6.956  1.00 49.98           C  
-ATOM   4460  CG  GLU B 323     -61.325  73.437   7.866  1.00 55.14           C  
-ATOM   4461  CD  GLU B 323     -62.378  72.417   8.361  1.00 60.36           C  
-ATOM   4462  OE1 GLU B 323     -63.459  72.857   8.834  1.00 60.85           O  
-ATOM   4463  OE2 GLU B 323     -62.127  71.183   8.297  1.00 62.20           O  
-ATOM   4464  N   TYR B 324     -57.637  71.043   5.953  1.00 43.09           N  
-ATOM   4465  CA  TYR B 324     -57.042  70.168   4.931  1.00 40.72           C  
-ATOM   4466  C   TYR B 324     -57.140  68.723   5.408  1.00 40.97           C  
-ATOM   4467  O   TYR B 324     -56.715  68.396   6.519  1.00 41.35           O  
-ATOM   4468  CB  TYR B 324     -55.561  70.477   4.702  1.00 39.14           C  
-ATOM   4469  CG  TYR B 324     -54.856  69.410   3.863  1.00 37.58           C  
-ATOM   4470  CD1 TYR B 324     -54.998  69.377   2.474  1.00 36.42           C  
-ATOM   4471  CD2 TYR B 324     -54.094  68.403   4.465  1.00 36.73           C  
-ATOM   4472  CE1 TYR B 324     -54.408  68.370   1.702  1.00 35.15           C  
-ATOM   4473  CE2 TYR B 324     -53.500  67.388   3.703  1.00 35.38           C  
-ATOM   4474  CZ  TYR B 324     -53.666  67.376   2.319  1.00 35.59           C  
-ATOM   4475  OH  TYR B 324     -53.135  66.351   1.555  1.00 32.89           O  
-ATOM   4476  N   ARG B 325     -57.679  67.858   4.561  1.00 40.28           N  
-ATOM   4477  CA  ARG B 325     -57.843  66.467   4.922  1.00 40.91           C  
-ATOM   4478  C   ARG B 325     -56.955  65.615   4.005  1.00 40.46           C  
-ATOM   4479  O   ARG B 325     -56.655  66.027   2.884  1.00 40.74           O  
-ATOM   4480  CB  ARG B 325     -59.326  66.113   4.799  1.00 42.76           C  
-ATOM   4481  CG  ARG B 325     -59.868  65.312   5.967  1.00 49.00           C  
-ATOM   4482  CD  ARG B 325     -61.351  65.554   6.171  1.00 53.80           C  
-ATOM   4483  NE  ARG B 325     -61.602  66.891   6.709  1.00 59.83           N  
-ATOM   4484  CZ  ARG B 325     -61.730  67.175   8.004  1.00 62.66           C  
-ATOM   4485  NH1 ARG B 325     -61.638  66.206   8.917  1.00 63.57           N  
-ATOM   4486  NH2 ARG B 325     -61.949  68.432   8.391  1.00 62.88           N  
-ATOM   4487  N   PRO B 326     -56.511  64.425   4.473  1.00 39.58           N  
-ATOM   4488  CA  PRO B 326     -55.648  63.522   3.699  1.00 39.38           C  
-ATOM   4489  C   PRO B 326     -56.106  63.294   2.273  1.00 41.53           C  
-ATOM   4490  O   PRO B 326     -57.205  62.782   2.040  1.00 42.99           O  
-ATOM   4491  CB  PRO B 326     -55.683  62.236   4.503  1.00 37.68           C  
-ATOM   4492  CG  PRO B 326     -55.848  62.719   5.878  1.00 38.73           C  
-ATOM   4493  CD  PRO B 326     -56.896  63.788   5.741  1.00 38.30           C  
-ATOM   4494  N   THR B 327     -55.254  63.671   1.323  1.00 42.24           N  
-ATOM   4495  CA  THR B 327     -55.551  63.504  -0.097  1.00 41.77           C  
-ATOM   4496  C   THR B 327     -54.619  62.456  -0.711  1.00 41.86           C  
-ATOM   4497  O   THR B 327     -53.429  62.417  -0.389  1.00 40.47           O  
-ATOM   4498  CB  THR B 327     -55.390  64.827  -0.823  1.00 42.17           C  
-ATOM   4499  OG1 THR B 327     -56.332  65.767  -0.288  1.00 41.42           O  
-ATOM   4500  CG2 THR B 327     -55.608  64.643  -2.324  1.00 42.50           C  
-ATOM   4501  N   PHE B 328     -55.158  61.615  -1.597  1.00 42.66           N  
-ATOM   4502  CA  PHE B 328     -54.368  60.545  -2.201  1.00 44.18           C  
-ATOM   4503  C   PHE B 328     -54.127  60.581  -3.704  1.00 46.30           C  
-ATOM   4504  O   PHE B 328     -53.691  59.589  -4.292  1.00 46.27           O  
-ATOM   4505  CB  PHE B 328     -54.962  59.197  -1.809  1.00 42.92           C  
-ATOM   4506  CG  PHE B 328     -54.989  58.977  -0.335  1.00 43.88           C  
-ATOM   4507  CD1 PHE B 328     -55.956  59.601   0.454  1.00 44.56           C  
-ATOM   4508  CD2 PHE B 328     -53.995  58.222   0.284  1.00 42.89           C  
-ATOM   4509  CE1 PHE B 328     -55.924  59.483   1.837  1.00 45.09           C  
-ATOM   4510  CE2 PHE B 328     -53.950  58.096   1.663  1.00 43.06           C  
-ATOM   4511  CZ  PHE B 328     -54.913  58.726   2.445  1.00 44.99           C  
-ATOM   4512  N   SER B 329     -54.398  61.725  -4.322  1.00 48.73           N  
-ATOM   4513  CA  SER B 329     -54.179  61.891  -5.751  1.00 51.60           C  
-ATOM   4514  C   SER B 329     -54.106  63.379  -6.081  1.00 53.75           C  
-ATOM   4515  O   SER B 329     -55.113  63.927  -6.588  1.00 56.15           O  
-ATOM   4516  CB  SER B 329     -55.294  61.210  -6.552  1.00 51.53           C  
-ATOM   4517  OG  SER B 329     -56.566  61.715  -6.197  1.00 51.90           O  
-ATOM   4518  OXT SER B 329     -53.043  63.983  -5.806  1.00 54.83           O  
-TER    4519      SER B 329                                                      
-HETATM 4520  CAA TMO B   1     -40.295  60.583  11.229  1.00 56.64           C  
-HETATM 4521  NAC TMO B   1     -41.391  60.028  12.080  1.00 56.91           N  
-HETATM 4522  CAD TMO B   1     -42.171  61.167  12.709  1.00 54.82           C  
-HETATM 4523  CAB TMO B   1     -40.800  59.166  13.166  1.00 55.74           C  
-HETATM 4524  OAE TMO B   1     -42.258  59.245  11.285  1.00 56.46           O  
-HETATM 4525  O   HOH A   6     -70.951 -13.559  -4.653  1.00 24.10           O  
-HETATM 4526  O   HOH A  11     -58.137  14.775  -0.781  1.00 28.46           O  
-HETATM 4527  O   HOH A  14     -70.021  64.303   9.882  1.00 38.51           O  
-HETATM 4528  O   HOH A  18     -55.083  56.210   4.412  1.00 25.45           O  
-HETATM 4529  O   HOH A  25     -70.090  42.160  21.020  1.00 28.26           O  
-HETATM 4530  O   HOH A  26     -59.918  60.703   0.034  1.00 36.44           O  
-HETATM 4531  O   HOH A  28     -72.362  52.640  13.286  1.00 24.91           O  
-HETATM 4532  O   HOH A  31     -61.713  60.213   6.691  1.00 24.03           O  
-HETATM 4533  O   HOH A  41     -65.657  88.593   9.890  1.00 42.73           O  
-HETATM 4534  O   HOH A  42     -72.703  83.471  11.691  1.00 22.41           O  
-HETATM 4535  O   HOH A 324     -54.557  50.281   6.876  1.00 38.52           O  
-HETATM 4536  O   HOH A 325     -60.861  63.877  18.703  1.00 42.67           O  
-HETATM 4537  O   HOH A 326     -78.971  35.526   5.222  1.00 35.70           O  
-HETATM 4538  O   HOH A 327     -54.191  49.680  14.387  1.00 41.60           O  
-HETATM 4539  O   HOH A 328     -55.991 -24.893   4.942  1.00 47.15           O  
-HETATM 4540  O   HOH A 329     -68.024   9.012   1.534  1.00 35.57           O  
-HETATM 4541  O   HOH A 330     -54.499  43.447   3.732  1.00 29.90           O  
-HETATM 4542  O   HOH A 331     -68.358  61.961   6.171  1.00 36.93           O  
-HETATM 4543  O   HOH A 332     -75.414  46.967   3.102  1.00 35.58           O  
-HETATM 4544  O   HOH A 333     -54.390  23.815  10.844  1.00 46.14           O  
-HETATM 4545  O   HOH A 334     -55.349  29.560  16.658  1.00 29.89           O  
-HETATM 4546  O   HOH B   2     -37.465  56.451   3.132  1.00 34.50           O  
-HETATM 4547  O   HOH B   3     -44.563  58.899  12.648  1.00 22.61           O  
-HETATM 4548  O   HOH B   7     -38.873  60.011  18.589  1.00 11.84           O  
-HETATM 4549  O   HOH B   8     -38.272  80.550  12.889  1.00 38.27           O  
-HETATM 4550  O   HOH B  12     -55.939  62.128  21.465  1.00 28.28           O  
-HETATM 4551  O   HOH B  13     -53.248  55.757  29.079  1.00 24.17           O  
-HETATM 4552  O   HOH B  15     -39.930  82.989  23.327  1.00 28.38           O  
-HETATM 4553  O   HOH B  19     -30.132  77.502  15.547  1.00 25.36           O  
-HETATM 4554  O   HOH B  21     -52.243  70.342  21.910  1.00 25.56           O  
-HETATM 4555  O   HOH B  22     -23.299  62.483  21.870  1.00 29.56           O  
-HETATM 4556  O   HOH B  23     -58.055  72.954   4.476  1.00 32.95           O  
-HETATM 4557  O   HOH B 330     -25.674  52.590  -0.947  1.00 24.19           O  
-HETATM 4558  O   HOH B 331     -29.417  67.090   8.639  1.00 24.40           O  
-HETATM 4559  O   HOH B 332     -49.094  61.155 -20.192  1.00 49.55           O  
-HETATM 4560  O   HOH B 333     -34.661  60.026   2.748  1.00 32.72           O  
-HETATM 4561  O   HOH B 334     -45.731  57.494 -18.268  1.00 36.61           O  
-HETATM 4562  O   HOH B 335     -57.990  61.841  -1.869  1.00 33.56           O  
-HETATM 4563  O   HOH B 336     -40.126  49.986 -15.569  1.00 32.86           O  
-HETATM 4564  O   HOH B 337     -46.443  66.403 -18.602  1.00 38.06           O  
-HETATM 4565  O   HOH B 338     -39.967  79.659  25.556  1.00 20.84           O  
-HETATM 4566  O   HOH B 339     -34.652  56.650   9.185  1.00 31.44           O  
-HETATM 4567  O   HOH B 340     -59.370  76.796  30.298  1.00 31.52           O  
-HETATM 4568  O   HOH B 341     -47.280  78.312  31.830  1.00 26.52           O  
-HETATM 4569  O   HOH B 342     -30.336  78.780  18.518  1.00 27.49           O  
-HETATM 4570  O   HOH B 343     -29.321  70.061   1.623  1.00 45.00           O  
-HETATM 4571  O   HOH B 344     -54.290  52.379   3.168  1.00 29.69           O  
-HETATM 4572  O   HOH B 345     -34.940  55.831 -14.707  1.00 27.07           O  
-HETATM 4573  O   HOH B 346     -48.190  43.995   6.466  1.00 33.12           O  
-HETATM 4574  O   HOH B 347     -31.993  75.866  19.770  1.00 23.84           O  
-HETATM 4575  O   HOH B 348     -61.208  63.644   8.463  1.00 27.82           O  
-HETATM 4576  O   HOH B 349     -30.270  59.130  38.153  1.00 27.71           O  
-HETATM 4577  O   HOH B 350     -43.600  74.029  28.789  1.00 42.81           O  
-HETATM 4578  O   HOH B 351     -51.630  65.643  16.510  1.00 46.78           O  
-HETATM 4579  O   HOH B 352     -28.850  65.866  -9.425  1.00 32.08           O  
-HETATM 4580  O   HOH B 353     -48.961  74.461   5.012  1.00 27.40           O  
-HETATM 4581  O   HOH B 354     -44.913  77.180  -2.038  1.00 20.41           O  
-HETATM 4582  O   HOH B 355     -21.701  64.272  18.372  1.00 33.99           O  
-HETATM 4583  O   HOH B 356     -40.457  78.792   0.864  1.00 32.18           O  
-HETATM 4584  O   HOH B 357     -47.153  86.774   7.221  1.00 26.70           O  
-HETATM 4585  O   HOH B 358     -32.391  61.318   7.128  1.00 38.88           O  
-HETATM 4586  O   HOH B 359     -31.268  69.498 -18.110  1.00 31.80           O  
-HETATM 4587  O   HOH B 360     -50.559  81.119   2.836  1.00 31.44           O  
-HETATM 4588  O   HOH B 361     -50.887  60.505 -15.695  1.00 37.16           O  
-HETATM 4589  O   HOH B 362     -41.423  76.023  38.275  1.00 42.34           O  
-HETATM 4590  O   HOH B 363     -52.132  43.488   5.896  1.00 37.41           O  
-HETATM 4591  O   HOH B 364     -25.931  70.372  10.201  1.00 28.91           O  
-HETATM 4592  O   HOH B 365     -49.188  68.871 -17.356  1.00 44.60           O  
-HETATM 4593  O   HOH B 366     -46.707  63.938  14.940  1.00 25.18           O  
-HETATM 4594  O   HOH B 367     -30.076  69.537  42.234  1.00 53.52           O  
-HETATM 4595  O   HOH B 368     -44.824  76.819  29.167  1.00 28.55           O  
-CONECT 2216 2613                                                                
-CONECT 2613 2216                                                                
-CONECT 4520 4521                                                                
-CONECT 4521 4520 4522 4523 4524                                                 
-CONECT 4522 4521                                                                
-CONECT 4523 4521                                                                
-CONECT 4524 4521                                                                
-MASTER      335    0    1   19   12    0    2    6 4593    2    7   46          
-END                                                                             
diff --git a/plip/test/pdb/3og7.pdb b/plip/test/pdb/3og7.pdb
deleted file mode 100644
index cbca312..0000000
--- a/plip/test/pdb/3og7.pdb
+++ /dev/null
@@ -1,8757 +0,0 @@
-HEADER    TRANSFERASE                             16-AUG-10   3OG7              
-TITLE     B-RAF KINASE V600E ONCOGENIC MUTANT IN COMPLEX WITH PLX4032           
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: AKAP9-BRAF FUSION PROTEIN;                                 
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 1175-1446);                    
-COMPND   5 SYNONYM: PROTO-ONCOGENE B-RAF, P94, V-RAF MURINE SARCOMA VIRAL       
-COMPND   6 ONCOGENE HOMOLOG B1;                                                 
-COMPND   7 EC: 2.7.11.1;                                                        
-COMPND   8 ENGINEERED: YES;                                                     
-COMPND   9 MUTATION: YES                                                        
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: BRAF, BRAF1, RAFB1;                                            
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
-KEYWDS    B-RAF, BRAF, PROTO-ONCOGENE, V600E, KINASE, TRANSFERASE               
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    Y.ZHANG,K.Y.ZHANG,C.ZHANG                                             
-REVDAT   2   06-OCT-10 3OG7    1       JRNL                                     
-REVDAT   1   22-SEP-10 3OG7    0                                                
-JRNL        AUTH   G.BOLLAG,P.HIRTH,J.TSAI,J.ZHANG,P.N.IBRAHIM,H.CHO,W.SPEVAK,  
-JRNL        AUTH 2 C.ZHANG,Y.ZHANG,G.HABETS,E.A.BURTON,B.WONG,G.TSANG,B.L.WEST, 
-JRNL        AUTH 3 B.POWELL,R.SHELLOOE,A.MARIMUTHU,H.NGUYEN,K.Y.ZHANG,          
-JRNL        AUTH 4 D.R.ARTIS,J.SCHLESSINGER,F.SU,B.HIGGINS,R.IYER,K.D'ANDREA,   
-JRNL        AUTH 5 A.KOEHLER,M.STUMM,P.S.LIN,R.J.LEE,J.GRIPPO,I.PUZANOV,        
-JRNL        AUTH 6 K.B.KIM,A.RIBAS,G.A.MCARTHUR,J.A.SOSMAN,P.B.CHAPMAN,         
-JRNL        AUTH 7 K.T.FLAHERTY,X.XU,K.L.NATHANSON,K.NOLOP                      
-JRNL        TITL   CLINICAL EFFICACY OF A RAF INHIBITOR NEEDS BROAD TARGET      
-JRNL        TITL 2 BLOCKADE IN BRAF-MUTANT MELANOMA.                            
-JRNL        REF    NATURE                        V. 467   596 2010              
-JRNL        REFN                   ISSN 0028-0836                               
-JRNL        PMID   20823850                                                     
-JRNL        DOI    10.1038/NATURE09454                                          
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.30                          
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
-REMARK   3   NUMBER OF REFLECTIONS             : 21223                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
-REMARK   3   R VALUE            (WORKING SET) : 0.212                           
-REMARK   3   FREE R VALUE                     : 0.258                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.190                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1146                            
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 21.2756 -  4.8839    0.94     2744   156  0.1766 0.2014        
-REMARK   3     2  4.8839 -  3.8842    0.95     2646   129  0.1679 0.2228        
-REMARK   3     3  3.8842 -  3.3955    0.95     2639   130  0.2012 0.2405        
-REMARK   3     4  3.3955 -  3.0861    0.95     2615   142  0.2319 0.2977        
-REMARK   3     5  3.0861 -  2.8654    0.95     2581   142  0.2690 0.3498        
-REMARK   3     6  2.8654 -  2.6968    0.95     2581   137  0.2837 0.3466        
-REMARK   3     7  2.6968 -  2.5620    0.95     2602   129  0.3023 0.3415        
-REMARK   3     8  2.5620 -  2.4507    0.94     2570   142  0.3323 0.3173        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.11                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
-REMARK   3   K_SOL              : 0.33                                          
-REMARK   3   B_SOL              : 47.40                                         
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.220           
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.23                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 24.09380                                             
-REMARK   3    B22 (A**2) : -6.25230                                             
-REMARK   3    B33 (A**2) : -17.84150                                            
-REMARK   3    B12 (A**2) : -0.00000                                             
-REMARK   3    B13 (A**2) : -0.00000                                             
-REMARK   3    B23 (A**2) : -0.00000                                             
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: 0.0860                                                   
-REMARK   3   OPERATOR: -H,L,K                                                   
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.003           4119                                  
-REMARK   3   ANGLE     :  0.649           5553                                  
-REMARK   3   CHIRALITY :  0.048            600                                  
-REMARK   3   PLANARITY :  0.004            707                                  
-REMARK   3   DIHEDRAL  : 16.634           1535                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
-REMARK   3   TLS GROUP : 1                                                      
-REMARK   3    SELECTION: CHAIN A                                                
-REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3512 -12.8290 -19.0118              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2830 T22:   0.1799                                     
-REMARK   3      T33:   0.1414 T12:   0.0279                                     
-REMARK   3      T13:   0.0065 T23:  -0.0149                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.4271 L22:   0.5813                                     
-REMARK   3      L33:   0.3905 L12:   0.2092                                     
-REMARK   3      L13:   0.1909 L23:   0.5345                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0295 S12:   0.1294 S13:   0.0517                       
-REMARK   3      S21:   0.4450 S22:   0.0815 S23:   0.0308                       
-REMARK   3      S31:   0.2817 S32:   0.0987 S33:  -0.0896                       
-REMARK   3   TLS GROUP : 2                                                      
-REMARK   3    SELECTION: CHAIN B                                                
-REMARK   3    ORIGIN FOR THE GROUP (A):   1.4917   8.6212   6.0490              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:  -0.0793 T22:   0.1906                                     
-REMARK   3      T33:   0.0369 T12:   0.0770                                     
-REMARK   3      T13:   0.1264 T23:  -0.0440                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.9070 L22:  -0.0294                                     
-REMARK   3      L33:   1.4032 L12:   0.0673                                     
-REMARK   3      L13:  -0.0545 L23:   0.1136                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0650 S12:  -0.0999 S13:   0.5313                       
-REMARK   3      S21:   0.1643 S22:  -0.0917 S23:  -0.0431                       
-REMARK   3      S31:   0.6296 S32:   0.1890 S33:   0.1035                       
-REMARK   3   TLS GROUP : 3                                                      
-REMARK   3    SELECTION: CHAIN L AND RESSEQ 1:1                                 
-REMARK   3    ORIGIN FOR THE GROUP (A):   1.8508  -2.7808 -20.0870              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2232 T22:   0.2843                                     
-REMARK   3      T33:   0.2448 T12:   0.0830                                     
-REMARK   3      T13:   0.0676 T23:   0.0568                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.3324 L22:   0.2201                                     
-REMARK   3      L33:   0.0130 L12:   0.0881                                     
-REMARK   3      L13:   0.0256 L23:   0.0536                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0039 S12:  -0.0108 S13:   0.0148                       
-REMARK   3      S21:  -0.0181 S22:  -0.0394 S23:   0.0296                       
-REMARK   3      S31:   0.0173 S32:   0.0067 S33:   0.0485                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 3OG7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.                  
-REMARK 100 THE RCSB ID CODE IS RCSB061075.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-08                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 6.0                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ALS                                
-REMARK 200  BEAMLINE                       : 8.3.1                              
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
-REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22230                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 110.128                            
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
-REMARK 200  DATA REDUNDANCY                : 4.500                              
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : 0.07200                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.52400                            
-REMARK 200  R SYM FOR SHELL            (I) : 0.52400                            
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: MOLREP                                                
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 47.71                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BISTRIS AT PH 6.0, 12.5% 2,5-      
-REMARK 280  HEXANEDIOL, AND 12% PEG3350, VAPOR DIFFUSION, SITTING DROP,         
-REMARK 280  TEMPERATURE 277K                                                    
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.38500            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.06400            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.21200            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.06400            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.38500            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.21200            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2                                                    
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A   432                                                      
-REMARK 465     LYS A   433                                                      
-REMARK 465     LYS A   434                                                      
-REMARK 465     GLY A   435                                                      
-REMARK 465     HIS A   436                                                      
-REMARK 465     HIS A   437                                                      
-REMARK 465     HIS A   438                                                      
-REMARK 465     HIS A   439                                                      
-REMARK 465     HIS A   440                                                      
-REMARK 465     HIS A   441                                                      
-REMARK 465     GLY A   442                                                      
-REMARK 465     SER A   443                                                      
-REMARK 465     ARG A   444                                                      
-REMARK 465     ASP A   445                                                      
-REMARK 465     ALA A   446                                                      
-REMARK 465     ALA A   447                                                      
-REMARK 465     ASP A   448                                                      
-REMARK 465     GLU A   545                                                      
-REMARK 465     THR A   546                                                      
-REMARK 465     LYS A   547                                                      
-REMARK 465     LEU A   597                                                      
-REMARK 465     ALA A   598                                                      
-REMARK 465     THR A   599                                                      
-REMARK 465     GLU A   600                                                      
-REMARK 465     LYS A   601                                                      
-REMARK 465     SER A   602                                                      
-REMARK 465     ARG A   603                                                      
-REMARK 465     TRP A   604                                                      
-REMARK 465     SER A   605                                                      
-REMARK 465     GLY A   606                                                      
-REMARK 465     SER A   607                                                      
-REMARK 465     HIS A   608                                                      
-REMARK 465     GLN A   609                                                      
-REMARK 465     PHE A   610                                                      
-REMARK 465     GLU A   611                                                      
-REMARK 465     GLN A   612                                                      
-REMARK 465     LEU A   613                                                      
-REMARK 465     SER A   614                                                      
-REMARK 465     MET A   627                                                      
-REMARK 465     GLN A   628                                                      
-REMARK 465     ASP A   629                                                      
-REMARK 465     SER A   630                                                      
-REMARK 465     MET B   432                                                      
-REMARK 465     LYS B   433                                                      
-REMARK 465     LYS B   434                                                      
-REMARK 465     GLY B   435                                                      
-REMARK 465     HIS B   436                                                      
-REMARK 465     HIS B   437                                                      
-REMARK 465     HIS B   438                                                      
-REMARK 465     HIS B   439                                                      
-REMARK 465     HIS B   440                                                      
-REMARK 465     HIS B   441                                                      
-REMARK 465     GLY B   442                                                      
-REMARK 465     SER B   443                                                      
-REMARK 465     ARG B   444                                                      
-REMARK 465     ASP B   445                                                      
-REMARK 465     ALA B   446                                                      
-REMARK 465     ALA B   447                                                      
-REMARK 465     ASP B   448                                                      
-REMARK 465     LYS B   601                                                      
-REMARK 465     SER B   602                                                      
-REMARK 465     ARG B   603                                                      
-REMARK 465     TRP B   604                                                      
-REMARK 465     SER B   605                                                      
-REMARK 465     GLY B   606                                                      
-REMARK 465     SER B   607                                                      
-REMARK 465     HIS B   608                                                      
-REMARK 465     GLN B   609                                                      
-REMARK 465     PHE B   610                                                      
-REMARK 465     GLU B   611                                                      
-REMARK 465     GLN B   612                                                      
-REMARK 465     LEU B   613                                                      
-REMARK 465     SER B   614                                                      
-REMARK 465     MET B   627                                                      
-REMARK 465     GLN B   628                                                      
-REMARK 465     ASP B   629                                                      
-REMARK 465     SER B   630                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    PRO A 453      151.21    -47.95                                   
-REMARK 500    ARG A 575      -15.01     78.91                                   
-REMARK 500    ASP A 576       55.71   -154.93                                   
-REMARK 500    ASN A 660       56.53    -91.77                                   
-REMARK 500    ASN A 684       36.26    -75.66                                   
-REMARK 500    TRP B 476       92.18   -160.90                                   
-REMARK 500    THR B 521      -59.15   -129.61                                   
-REMARK 500    ALA B 522       21.78    -74.49                                   
-REMARK 500    PRO B 523      -87.45   -114.92                                   
-REMARK 500    ALA B 543       30.14    -91.55                                   
-REMARK 500    ASP B 576       38.22   -154.00                                   
-REMARK 500    ASP B 587      -15.42     76.91                                   
-REMARK 500    PHE B 595      -84.66    -52.94                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
-REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
-REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
-REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
-REMARK 500                                 MODEL     OMEGA                      
-REMARK 500 ALA B  522     PRO B  523                  143.03                    
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 032 A 1                   
-DBREF  3OG7 A  449   720  UNP    Q5IBP5   Q5IBP5_HUMAN  1175   1446             
-DBREF  3OG7 B  449   720  UNP    Q5IBP5   Q5IBP5_HUMAN  1175   1446             
-SEQADV 3OG7 MET A  432  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 LYS A  433  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 LYS A  434  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 GLY A  435  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS A  436  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS A  437  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS A  438  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS A  439  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS A  440  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS A  441  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 GLY A  442  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 SER A  443  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ARG A  444  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ASP A  445  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ALA A  446  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ALA A  447  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ASP A  448  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ALA A  522  UNP  Q5IBP5    LYS  1248 ENGINEERED MUTATION            
-SEQADV 3OG7 ALA A  543  UNP  Q5IBP5    ILE  1269 ENGINEERED MUTATION            
-SEQADV 3OG7 SER A  544  UNP  Q5IBP5    ILE  1270 ENGINEERED MUTATION            
-SEQADV 3OG7 LYS A  551  UNP  Q5IBP5    ILE  1277 ENGINEERED MUTATION            
-SEQADV 3OG7 ARG A  562  UNP  Q5IBP5    GLN  1288 ENGINEERED MUTATION            
-SEQADV 3OG7 ASN A  588  UNP  Q5IBP5    LEU  1314 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU A  600  UNP  Q5IBP5    VAL  1326 VARIANT                        
-SEQADV 3OG7 SER A  630  UNP  Q5IBP5    LYS  1356 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU A  667  UNP  Q5IBP5    PHE  1393 ENGINEERED MUTATION            
-SEQADV 3OG7 SER A  673  UNP  Q5IBP5    TYR  1399 ENGINEERED MUTATION            
-SEQADV 3OG7 ARG A  688  UNP  Q5IBP5    ALA  1414 ENGINEERED MUTATION            
-SEQADV 3OG7 SER A  706  UNP  Q5IBP5    LEU  1432 ENGINEERED MUTATION            
-SEQADV 3OG7 ARG A  709  UNP  Q5IBP5    GLN  1435 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU A  713  UNP  Q5IBP5    SER  1439 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU A  716  UNP  Q5IBP5    LEU  1442 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU A  720  UNP  Q5IBP5    SER  1446 ENGINEERED MUTATION            
-SEQADV 3OG7 MET B  432  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 LYS B  433  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 LYS B  434  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 GLY B  435  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS B  436  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS B  437  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS B  438  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS B  439  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS B  440  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 HIS B  441  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 GLY B  442  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 SER B  443  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ARG B  444  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ASP B  445  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ALA B  446  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ALA B  447  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ASP B  448  UNP  Q5IBP5              EXPRESSION TAG                 
-SEQADV 3OG7 ALA B  522  UNP  Q5IBP5    LYS  1248 ENGINEERED MUTATION            
-SEQADV 3OG7 ALA B  543  UNP  Q5IBP5    ILE  1269 ENGINEERED MUTATION            
-SEQADV 3OG7 SER B  544  UNP  Q5IBP5    ILE  1270 ENGINEERED MUTATION            
-SEQADV 3OG7 LYS B  551  UNP  Q5IBP5    ILE  1277 ENGINEERED MUTATION            
-SEQADV 3OG7 ARG B  562  UNP  Q5IBP5    GLN  1288 ENGINEERED MUTATION            
-SEQADV 3OG7 ASN B  588  UNP  Q5IBP5    LEU  1314 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU B  600  UNP  Q5IBP5    VAL  1326 VARIANT                        
-SEQADV 3OG7 SER B  630  UNP  Q5IBP5    LYS  1356 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU B  667  UNP  Q5IBP5    PHE  1393 ENGINEERED MUTATION            
-SEQADV 3OG7 SER B  673  UNP  Q5IBP5    TYR  1399 ENGINEERED MUTATION            
-SEQADV 3OG7 ARG B  688  UNP  Q5IBP5    ALA  1414 ENGINEERED MUTATION            
-SEQADV 3OG7 SER B  706  UNP  Q5IBP5    LEU  1432 ENGINEERED MUTATION            
-SEQADV 3OG7 ARG B  709  UNP  Q5IBP5    GLN  1435 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU B  713  UNP  Q5IBP5    SER  1439 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU B  716  UNP  Q5IBP5    LEU  1442 ENGINEERED MUTATION            
-SEQADV 3OG7 GLU B  720  UNP  Q5IBP5    SER  1446 ENGINEERED MUTATION            
-SEQRES   1 A  289  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG          
-SEQRES   2 A  289  ASP ALA ALA ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE          
-SEQRES   3 A  289  THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR          
-SEQRES   4 A  289  VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS          
-SEQRES   5 A  289  MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN          
-SEQRES   6 A  289  ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG          
-SEQRES   7 A  289  HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR ALA          
-SEQRES   8 A  289  PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER          
-SEQRES   9 A  289  SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE          
-SEQRES  10 A  289  GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA          
-SEQRES  11 A  289  ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS          
-SEQRES  12 A  289  ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP          
-SEQRES  13 A  289  ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR GLU          
-SEQRES  14 A  289  LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU          
-SEQRES  15 A  289  SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG          
-SEQRES  16 A  289  MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL          
-SEQRES  17 A  289  TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY          
-SEQRES  18 A  289  GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE          
-SEQRES  19 A  289  ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU          
-SEQRES  20 A  289  SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG          
-SEQRES  21 A  289  LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG          
-SEQRES  22 A  289  PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU          
-SEQRES  23 A  289  ALA ARG GLU                                                  
-SEQRES   1 B  289  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG          
-SEQRES   2 B  289  ASP ALA ALA ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE          
-SEQRES   3 B  289  THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR          
-SEQRES   4 B  289  VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS          
-SEQRES   5 B  289  MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN          
-SEQRES   6 B  289  ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG          
-SEQRES   7 B  289  HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR ALA          
-SEQRES   8 B  289  PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER          
-SEQRES   9 B  289  SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE          
-SEQRES  10 B  289  GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA          
-SEQRES  11 B  289  ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS          
-SEQRES  12 B  289  ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP          
-SEQRES  13 B  289  ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR GLU          
-SEQRES  14 B  289  LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU          
-SEQRES  15 B  289  SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG          
-SEQRES  16 B  289  MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL          
-SEQRES  17 B  289  TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY          
-SEQRES  18 B  289  GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE          
-SEQRES  19 B  289  ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU          
-SEQRES  20 B  289  SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG          
-SEQRES  21 B  289  LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG          
-SEQRES  22 B  289  PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU          
-SEQRES  23 B  289  ALA ARG GLU                                                  
-HET    032  A   1      33                                                       
-HETNAM     032 N-(3-{[5-(4-CHLOROPHENYL)-1H-PYRROLO[2,3-B]PYRIDIN-3-            
-HETNAM   2 032  YL]CARBONYL}-2,4-DIFLUOROPHENYL)PROPANE-1-SULFONAMIDE           
-HETSYN     032 PLX4032                                                          
-FORMUL   3  032    C23 H18 CL F2 N3 O3 S                                        
-FORMUL   4  HOH   *65(H2 O)                                                     
-HELIX    1   1 THR A  491  ARG A  506  1                                  16    
-HELIX    2   2 LEU A  537  HIS A  542  1                                   6    
-HELIX    3   3 GLU A  549  LYS A  570  1                                  22    
-HELIX    4   4 ALA A  621  ARG A  626  1                                   6    
-HELIX    5   5 SER A  634  GLY A  652  1                                  19    
-HELIX    6   6 ASN A  661  ARG A  671  1                                  11    
-HELIX    7   7 PRO A  686  LEU A  697  1                                  12    
-HELIX    8   8 LYS A  700  ARG A  704  5                                   5    
-HELIX    9   9 SER A  706  LEU A  717  1                                  12    
-HELIX   10  10 THR B  491  ARG B  506  1                                  16    
-HELIX   11  11 SER B  536  HIS B  542  1                                   7    
-HELIX   12  12 GLU B  549  LYS B  570  1                                  22    
-HELIX   13  13 GLU B  586  ASN B  588  5                                   3    
-HELIX   14  14 GLY B  615  MET B  620  5                                   6    
-HELIX   15  15 ALA B  621  ARG B  626  1                                   6    
-HELIX   16  16 SER B  634  GLY B  652  1                                  19    
-HELIX   17  17 ASN B  661  GLY B  672  1                                  12    
-HELIX   18  18 ASP B  677  VAL B  681  5                                   5    
-HELIX   19  19 PRO B  686  LEU B  697  1                                  12    
-HELIX   20  20 LYS B  700  ARG B  704  5                                   5    
-HELIX   21  21 SER B  706  GLU B  720  1                                  15    
-SHEET    1   A 5 THR A 458  SER A 465  0                                        
-SHEET    2   A 5 GLY A 469  LYS A 475 -1  O  VAL A 471   N  ILE A 463           
-SHEET    3   A 5 ASP A 479  LEU A 485 -1  O  VAL A 480   N  GLY A 474           
-SHEET    4   A 5 ALA A 526  GLN A 530 -1  O  ILE A 527   N  LYS A 483           
-SHEET    5   A 5 PHE A 516  SER A 520 -1  N  GLY A 518   O  VAL A 528           
-SHEET    1   B 3 GLY A 534  SER A 536  0                                        
-SHEET    2   B 3 ILE A 582  HIS A 585 -1  O  LEU A 584   N  SER A 535           
-SHEET    3   B 3 THR A 589  ILE A 592 -1  O  LYS A 591   N  PHE A 583           
-SHEET    1   C 5 THR B 458  SER B 465  0                                        
-SHEET    2   C 5 THR B 470  LYS B 475 -1  O  LYS B 473   N  GLY B 460           
-SHEET    3   C 5 ASP B 479  LEU B 485 -1  O  MET B 484   N  THR B 470           
-SHEET    4   C 5 LEU B 525  GLN B 530 -1  O  THR B 529   N  ALA B 481           
-SHEET    5   C 5 PHE B 516  SER B 520 -1  N  GLY B 518   O  VAL B 528           
-SHEET    1   D 2 ILE B 582  HIS B 585  0                                        
-SHEET    2   D 2 THR B 589  ILE B 592 -1  O  THR B 589   N  HIS B 585           
-CISPEP   1 ALA A  522    PRO A  523          0        -0.27                     
-SITE     1 AC1 13 VAL A 471  ALA A 481  LYS A 483  LEU A 505                    
-SITE     2 AC1 13 LEU A 514  THR A 529  GLN A 530  TRP A 531                    
-SITE     3 AC1 13 CYS A 532  PHE A 583  ASP A 594  PHE A 595                    
-SITE     4 AC1 13 GLY A 596                                                     
-CRYST1   50.770  104.424  110.128  90.00  90.00  90.00 P 21 21 21    8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.019697  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.009576  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.009080        0.00000                         
-ATOM      1  N   ASP A 449     -15.047   9.355 -11.670  1.00 80.04           N  
-ANISOU    1  N   ASP A 449     9855   9321  11236   -452   1214    -11       N  
-ATOM      2  CA  ASP A 449     -14.538   9.164 -13.021  1.00 83.30           C  
-ANISOU    2  CA  ASP A 449    10196   9808  11648   -424   1132     64       C  
-ATOM      3  C   ASP A 449     -13.017   9.130 -12.998  1.00 76.40           C  
-ANISOU    3  C   ASP A 449     9369   8972  10687   -374   1053     98       C  
-ATOM      4  O   ASP A 449     -12.381   9.818 -12.197  1.00 67.69           O  
-ANISOU    4  O   ASP A 449     8292   7844   9583   -357   1041     80       O  
-ATOM      5  CB  ASP A 449     -15.032  10.281 -13.944  1.00 82.63           C  
-ANISOU    5  CB  ASP A 449     9947   9738  11710   -431   1094    102       C  
-ATOM      6  CG  ASP A 449     -15.551   9.755 -15.271  1.00 81.08           C  
-ANISOU    6  CG  ASP A 449     9679   9593  11535   -439   1071    147       C  
-ATOM      7  OD1 ASP A 449     -15.391   8.545 -15.536  1.00 78.75           O  
-ANISOU    7  OD1 ASP A 449     9454   9328  11139   -435   1078    152       O  
-ATOM      8  OD2 ASP A 449     -16.121  10.550 -16.050  1.00 79.01           O  
-ANISOU    8  OD2 ASP A 449     9291   9338  11392   -449   1043    175       O  
-ATOM      9  N   TRP A 450     -12.436   8.326 -13.881  1.00 63.98           N  
-ANISOU    9  N   TRP A 450     7803   7462   9043   -351   1001    142       N  
-ATOM     10  CA  TRP A 450     -10.992   8.142 -13.891  1.00 51.35           C  
-ANISOU   10  CA  TRP A 450     6249   5904   7356   -304    927    163       C  
-ATOM     11  C   TRP A 450     -10.334   8.695 -15.147  1.00 42.87           C  
-ANISOU   11  C   TRP A 450     5057   4907   6327   -286    842    231       C  
-ATOM     12  O   TRP A 450      -9.221   8.302 -15.494  1.00 39.13           O  
-ANISOU   12  O   TRP A 450     4605   4486   5777   -252    780    250       O  
-ATOM     13  CB  TRP A 450     -10.640   6.665 -13.711  1.00 46.89           C  
-ANISOU   13  CB  TRP A 450     5814   5348   6655   -288    931    145       C  
-ATOM     14  CG  TRP A 450     -10.991   6.139 -12.353  1.00 47.22           C  
-ANISOU   14  CG  TRP A 450     5998   5313   6629   -303   1002     81       C  
-ATOM     15  CD1 TRP A 450     -12.177   5.584 -11.970  1.00 51.48           C  
-ANISOU   15  CD1 TRP A 450     6586   5804   7169   -350   1092     44       C  
-ATOM     16  CD2 TRP A 450     -10.148   6.126 -11.193  1.00 43.12           C  
-ANISOU   16  CD2 TRP A 450     5597   4757   6031   -275    991     45       C  
-ATOM     17  NE1 TRP A 450     -12.124   5.223 -10.646  1.00 56.25           N  
-ANISOU   17  NE1 TRP A 450     7335   6344   7693   -358   1139    -10       N  
-ATOM     18  CE2 TRP A 450     -10.890   5.544 -10.145  1.00 43.95           C  
-ANISOU   18  CE2 TRP A 450     5823   4791   6084   -311   1076     -9       C  
-ATOM     19  CE3 TRP A 450      -8.839   6.547 -10.939  1.00 30.98           C  
-ANISOU   19  CE3 TRP A 450     4074   3240   4459   -226    918     50       C  
-ATOM     20  CZ2 TRP A 450     -10.368   5.373  -8.867  1.00 41.72           C  
-ANISOU   20  CZ2 TRP A 450     5682   4457   5714   -298   1086    -52       C  
-ATOM     21  CZ3 TRP A 450      -8.322   6.376  -9.670  1.00 41.75           C  
-ANISOU   21  CZ3 TRP A 450     5570   4552   5740   -208    925      3       C  
-ATOM     22  CH2 TRP A 450      -9.085   5.793  -8.648  1.00 48.88           C  
-ANISOU   22  CH2 TRP A 450     6599   5384   6589   -243   1007    -45       C  
-ATOM     23  N   GLU A 451     -11.019   9.609 -15.823  1.00 40.93           N  
-ANISOU   23  N   GLU A 451     4685   4664   6201   -311    838    263       N  
-ATOM     24  CA  GLU A 451     -10.452  10.250 -17.000  1.00 44.36           C  
-ANISOU   24  CA  GLU A 451     5009   5166   6681   -303    759    331       C  
-ATOM     25  C   GLU A 451      -9.395  11.261 -16.588  1.00 35.04           C  
-ANISOU   25  C   GLU A 451     3813   3984   5516   -280    713    338       C  
-ATOM     26  O   GLU A 451      -9.611  12.062 -15.682  1.00 40.90           O  
-ANISOU   26  O   GLU A 451     4560   4665   6314   -285    742    305       O  
-ATOM     27  CB  GLU A 451     -11.537  10.937 -17.828  1.00 54.84           C  
-ANISOU   27  CB  GLU A 451     6215   6489   8134   -337    763    366       C  
-ATOM     28  CG  GLU A 451     -10.984  11.748 -18.985  1.00 63.51           C  
-ANISOU   28  CG  GLU A 451     7204   7646   9282   -336    681    440       C  
-ATOM     29  CD  GLU A 451     -12.061  12.228 -19.934  1.00 65.27           C  
-ANISOU   29  CD  GLU A 451     7318   7869   9614   -366    673    479       C  
-ATOM     30  OE1 GLU A 451     -13.218  11.781 -19.796  1.00 70.08           O  
-ANISOU   30  OE1 GLU A 451     7931   8441  10253   -385    730    445       O  
-ATOM     31  OE2 GLU A 451     -11.746  13.049 -20.821  1.00 62.98           O  
-ANISOU   31  OE2 GLU A 451     6939   7613   9377   -373    607    542       O  
-ATOM     32  N   ILE A 452      -8.249  11.212 -17.257  1.00 32.41           N  
-ANISOU   32  N   ILE A 452     3459   3721   5134   -258    643    374       N  
-ATOM     33  CA  ILE A 452      -7.156  12.130 -16.979  1.00 23.88           C  
-ANISOU   33  CA  ILE A 452     2358   2650   4065   -238    595    379       C  
-ATOM     34  C   ILE A 452      -7.138  13.237 -18.028  1.00 40.15           C  
-ANISOU   34  C   ILE A 452     4287   4744   6223   -261    545    447       C  
-ATOM     35  O   ILE A 452      -6.853  12.984 -19.199  1.00 51.35           O  
-ANISOU   35  O   ILE A 452     5654   6235   7623   -270    501    496       O  
-ATOM     36  CB  ILE A 452      -5.805  11.393 -16.961  1.00 27.36           C  
-ANISOU   36  CB  ILE A 452     2863   3145   4387   -199    548    364       C  
-ATOM     37  CG1 ILE A 452      -5.820  10.291 -15.898  1.00 15.82           C  
-ANISOU   37  CG1 ILE A 452     1544   1642   2826   -175    588    301       C  
-ATOM     38  CG2 ILE A 452      -4.668  12.367 -16.707  1.00 30.19           C  
-ANISOU   38  CG2 ILE A 452     3193   3516   4763   -180    499    364       C  
-ATOM     39  CD1 ILE A 452      -4.645   9.338 -15.976  1.00 22.15           C  
-ANISOU   39  CD1 ILE A 452     2412   2494   3509   -133    537    281       C  
-ATOM     40  N   PRO A 453      -7.455  14.472 -17.608  1.00 41.73           N  
-ANISOU   40  N   PRO A 453     4437   4890   6528   -273    552    448       N  
-ATOM     41  CA  PRO A 453      -7.568  15.633 -18.501  1.00 36.64           C  
-ANISOU   41  CA  PRO A 453     3675   4259   5989   -299    505    512       C  
-ATOM     42  C   PRO A 453      -6.383  15.771 -19.455  1.00 44.11           C  
-ANISOU   42  C   PRO A 453     4579   5289   6892   -298    433    563       C  
-ATOM     43  O   PRO A 453      -5.273  15.352 -19.127  1.00 40.43           O  
-ANISOU   43  O   PRO A 453     4168   4858   6337   -270    416    536       O  
-ATOM     44  CB  PRO A 453      -7.605  16.813 -17.527  1.00 29.14           C  
-ANISOU   44  CB  PRO A 453     2711   3236   5124   -296    518    483       C  
-ATOM     45  CG  PRO A 453      -8.222  16.249 -16.297  1.00 29.97           C  
-ANISOU   45  CG  PRO A 453     2906   3279   5202   -287    593    407       C  
-ATOM     46  CD  PRO A 453      -7.734  14.828 -16.206  1.00 29.84           C  
-ANISOU   46  CD  PRO A 453     2990   3304   5046   -265    604    384       C  
-ATOM     47  N   ASP A 454      -6.630  16.357 -20.623  1.00 52.80           N  
-ANISOU   47  N   ASP A 454     5586   6421   8056   -330    392    634       N  
-ATOM     48  CA  ASP A 454      -5.603  16.529 -21.648  1.00 51.35           C  
-ANISOU   48  CA  ASP A 454     5355   6321   7833   -342    328    687       C  
-ATOM     49  C   ASP A 454      -4.440  17.392 -21.161  1.00 47.70           C  
-ANISOU   49  C   ASP A 454     4891   5859   7376   -332    299    676       C  
-ATOM     50  O   ASP A 454      -4.644  18.477 -20.617  1.00 47.05           O  
-ANISOU   50  O   ASP A 454     4781   5713   7384   -336    301    675       O  
-ATOM     51  CB  ASP A 454      -6.221  17.142 -22.911  1.00 63.62           C  
-ANISOU   51  CB  ASP A 454     6815   7894   9465   -385    290    768       C  
-ATOM     52  CG  ASP A 454      -5.210  17.329 -24.033  1.00 73.69           C  
-ANISOU   52  CG  ASP A 454     8043   9259  10695   -410    229    825       C  
-ATOM     53  OD1 ASP A 454      -4.080  16.807 -23.925  1.00 77.79           O  
-ANISOU   53  OD1 ASP A 454     8599   9836  11121   -392    219    796       O  
-ATOM     54  OD2 ASP A 454      -5.553  17.999 -25.031  1.00 68.59           O  
-ANISOU   54  OD2 ASP A 454     7325   8627  10110   -449    189    897       O  
-ATOM     55  N   GLY A 455      -3.220  16.899 -21.358  1.00 45.78           N  
-ANISOU   55  N   GLY A 455     4670   5686   7036   -317    271    662       N  
-ATOM     56  CA  GLY A 455      -2.027  17.657 -21.026  1.00 42.94           C  
-ANISOU   56  CA  GLY A 455     4301   5339   6676   -309    239    649       C  
-ATOM     57  C   GLY A 455      -1.349  17.250 -19.730  1.00 52.32           C  
-ANISOU   57  C   GLY A 455     5577   6500   7802   -259    260    565       C  
-ATOM     58  O   GLY A 455      -0.195  17.608 -19.493  1.00 50.12           O  
-ANISOU   58  O   GLY A 455     5298   6248   7498   -244    230    541       O  
-ATOM     59  N   GLN A 456      -2.056  16.503 -18.888  1.00 49.33           N  
-ANISOU   59  N   GLN A 456     5277   6070   7397   -233    309    519       N  
-ATOM     60  CA  GLN A 456      -1.517  16.112 -17.588  1.00 35.14           C  
-ANISOU   60  CA  GLN A 456     3576   4236   5538   -187    328    441       C  
-ATOM     61  C   GLN A 456      -0.395  15.079 -17.692  1.00 36.13           C  
-ANISOU   61  C   GLN A 456     3755   4429   5543   -152    295    405       C  
-ATOM     62  O   GLN A 456       0.510  15.049 -16.858  1.00 36.99           O  
-ANISOU   62  O   GLN A 456     3919   4529   5606   -114    280    348       O  
-ATOM     63  CB  GLN A 456      -2.629  15.597 -16.670  1.00 35.87           C  
-ANISOU   63  CB  GLN A 456     3744   4253   5632   -179    393    403       C  
-ATOM     64  CG  GLN A 456      -3.615  16.667 -16.223  1.00 39.85           C  
-ANISOU   64  CG  GLN A 456     4205   4680   6258   -203    429    410       C  
-ATOM     65  CD  GLN A 456      -4.411  16.247 -15.001  1.00 38.41           C  
-ANISOU   65  CD  GLN A 456     4111   4421   6063   -193    497    348       C  
-ATOM     66  OE1 GLN A 456      -4.175  15.184 -14.428  1.00 42.30           O  
-ANISOU   66  OE1 GLN A 456     4707   4914   6452   -167    516    303       O  
-ATOM     67  NE2 GLN A 456      -5.355  17.087 -14.593  1.00 35.26           N  
-ANISOU   67  NE2 GLN A 456     3672   3955   5770   -215    534    343       N  
-ATOM     68  N   ILE A 457      -0.454  14.237 -18.718  1.00 35.99           N  
-ANISOU   68  N   ILE A 457     3720   4477   5476   -164    279    433       N  
-ATOM     69  CA  ILE A 457       0.531  13.174 -18.881  1.00 33.89           C  
-ANISOU   69  CA  ILE A 457     3500   4275   5100   -131    246    393       C  
-ATOM     70  C   ILE A 457       1.624  13.542 -19.880  1.00 41.19           C  
-ANISOU   70  C   ILE A 457     4342   5292   6015   -148    190    414       C  
-ATOM     71  O   ILE A 457       1.342  13.906 -21.024  1.00 37.76           O  
-ANISOU   71  O   ILE A 457     3823   4905   5620   -196    178    479       O  
-ATOM     72  CB  ILE A 457      -0.131  11.860 -19.334  1.00 34.08           C  
-ANISOU   72  CB  ILE A 457     3565   4319   5065   -130    265    396       C  
-ATOM     73  CG1 ILE A 457      -1.301  11.508 -18.416  1.00 46.25           C  
-ANISOU   73  CG1 ILE A 457     5184   5770   6617   -126    328    376       C  
-ATOM     74  CG2 ILE A 457       0.887  10.733 -19.358  1.00 23.74           C  
-ANISOU   74  CG2 ILE A 457     2312   3064   3644    -89    227    344       C  
-ATOM     75  CD1 ILE A 457      -2.090  10.303 -18.877  1.00 48.99           C  
-ANISOU   75  CD1 ILE A 457     5565   6130   6920   -133    354    383       C  
-ATOM     76  N   THR A 458       2.873  13.443 -19.440  1.00 40.82           N  
-ANISOU   76  N   THR A 458     4323   5272   5915   -111    155    356       N  
-ATOM     77  CA  THR A 458       4.009  13.669 -20.319  1.00 35.47           C  
-ANISOU   77  CA  THR A 458     3572   4687   5217   -127    105    358       C  
-ATOM     78  C   THR A 458       4.480  12.338 -20.891  1.00 44.63           C  
-ANISOU   78  C   THR A 458     4756   5921   6281   -107     80    325       C  
-ATOM     79  O   THR A 458       5.099  11.538 -20.190  1.00 42.62           O  
-ANISOU   79  O   THR A 458     4578   5659   5955    -51     62    252       O  
-ATOM     80  CB  THR A 458       5.174  14.346 -19.579  1.00 30.07           C  
-ANISOU   80  CB  THR A 458     2891   3997   4536   -100     78    302       C  
-ATOM     81  OG1 THR A 458       4.712  15.550 -18.953  1.00 26.25           O  
-ANISOU   81  OG1 THR A 458     2392   3439   4145   -114    103    326       O  
-ATOM     82  CG2 THR A 458       6.302  14.678 -20.550  1.00 28.76           C  
-ANISOU   82  CG2 THR A 458     2639   3929   4358   -128     34    304       C  
-ATOM     83  N   VAL A 459       4.176  12.101 -22.163  1.00 41.08           N  
-ANISOU   83  N   VAL A 459     4240   5539   5829   -152     75    379       N  
-ATOM     84  CA  VAL A 459       4.559  10.857 -22.821  1.00 35.09           C  
-ANISOU   84  CA  VAL A 459     3492   4857   4986   -138     51    350       C  
-ATOM     85  C   VAL A 459       6.036  10.889 -23.200  1.00 44.19           C  
-ANISOU   85  C   VAL A 459     4599   6094   6095   -132      1    299       C  
-ATOM     86  O   VAL A 459       6.534  11.897 -23.700  1.00 54.84           O  
-ANISOU   86  O   VAL A 459     5868   7482   7486   -175    -12    326       O  
-ATOM     87  CB  VAL A 459       3.709  10.604 -24.072  1.00 38.94           C  
-ANISOU   87  CB  VAL A 459     3920   5391   5486   -190     64    421       C  
-ATOM     88  CG1 VAL A 459       4.017   9.237 -24.659  1.00 36.62           C  
-ANISOU   88  CG1 VAL A 459     3642   5167   5105   -172     43    385       C  
-ATOM     89  CG2 VAL A 459       2.236  10.717 -23.731  1.00 36.69           C  
-ANISOU   89  CG2 VAL A 459     3663   5020   5257   -200    113    467       C  
-ATOM     90  N   GLY A 460       6.733   9.783 -22.960  1.00 45.65           N  
-ANISOU   90  N   GLY A 460     4838   6309   6200    -80    -29    222       N  
-ATOM     91  CA  GLY A 460       8.162   9.723 -23.208  1.00 43.47           C  
-ANISOU   91  CA  GLY A 460     4522   6110   5884    -66    -79    154       C  
-ATOM     92  C   GLY A 460       8.567   8.599 -24.140  1.00 55.80           C  
-ANISOU   92  C   GLY A 460     6060   7765   7377    -65   -108    122       C  
-ATOM     93  O   GLY A 460       8.028   8.464 -25.239  1.00 64.78           O  
-ANISOU   93  O   GLY A 460     7139   8957   8518   -118    -94    181       O  
-ATOM     94  N   GLN A 461       9.520   7.788 -23.693  1.00 57.20           N  
-ANISOU   94  N   GLN A 461     6282   7961   7493     -4   -152     25       N  
-ATOM     95  CA  GLN A 461      10.065   6.706 -24.507  1.00 56.72           C  
-ANISOU   95  CA  GLN A 461     6194   7989   7368      5   -188    -24       C  
-ATOM     96  C   GLN A 461       8.996   5.744 -25.014  1.00 47.12           C  
-ANISOU   96  C   GLN A 461     5006   6770   6128     -4   -164     20       C  
-ATOM     97  O   GLN A 461       8.163   5.267 -24.246  1.00 48.16           O  
-ANISOU   97  O   GLN A 461     5232   6812   6253     29   -140     32       O  
-ATOM     98  CB  GLN A 461      11.120   5.927 -23.717  1.00 89.08           C  
-ANISOU   98  CB  GLN A 461    10357  12080  11410     87   -244   -142       C  
-ATOM     99  CG  GLN A 461      12.397   6.704 -23.443  1.00111.66           C  
-ANISOU   99  CG  GLN A 461    13170  14972  14285     97   -279   -208       C  
-ATOM    100  CD  GLN A 461      13.397   5.907 -22.627  1.00124.11           C  
-ANISOU  100  CD  GLN A 461    14814  16534  15809    185   -343   -328       C  
-ATOM    101  OE1 GLN A 461      13.035   4.947 -21.947  1.00127.05           O  
-ANISOU  101  OE1 GLN A 461    15294  16840  16138    245   -357   -352       O  
-ATOM    102  NE2 GLN A 461      14.663   6.303 -22.689  1.00123.80           N  
-ANISOU  102  NE2 GLN A 461    14712  16554  15772    193   -383   -407       N  
-ATOM    103  N   ARG A 462       9.027   5.464 -26.313  1.00 49.68           N  
-ANISOU  103  N   ARG A 462     5245   7193   6437    -53   -168     42       N  
-ATOM    104  CA  ARG A 462       8.182   4.432 -26.896  1.00 49.61           C  
-ANISOU  104  CA  ARG A 462     5253   7197   6399    -58   -153     69       C  
-ATOM    105  C   ARG A 462       8.757   3.084 -26.493  1.00 58.57           C  
-ANISOU  105  C   ARG A 462     6457   8334   7464     15   -197    -28       C  
-ATOM    106  O   ARG A 462       9.936   2.818 -26.715  1.00 69.68           O  
-ANISOU  106  O   ARG A 462     7827   9809   8837     35   -247   -109       O  
-ATOM    107  CB  ARG A 462       8.173   4.548 -28.422  1.00 46.21           C  
-ANISOU  107  CB  ARG A 462     4709   6880   5968   -132   -150    113       C  
-ATOM    108  CG  ARG A 462       6.974   3.890 -29.096  1.00 53.04           C  
-ANISOU  108  CG  ARG A 462     5575   7748   6829   -156   -120    174       C  
-ATOM    109  CD  ARG A 462       7.196   3.697 -30.596  1.00 61.93           C  
-ANISOU  109  CD  ARG A 462     6599   9001   7932   -217   -131    191       C  
-ATOM    110  NE  ARG A 462       7.763   2.385 -30.898  1.00 67.67           N  
-ANISOU  110  NE  ARG A 462     7332   9788   8592   -179   -165    107       N  
-ATOM    111  CZ  ARG A 462       7.059   1.345 -31.336  1.00 71.66           C  
-ANISOU  111  CZ  ARG A 462     7855  10304   9070   -172   -157    115       C  
-ATOM    112  NH1 ARG A 462       5.753   1.460 -31.539  1.00 75.34           N  
-ANISOU  112  NH1 ARG A 462     8331  10726   9569   -201   -113    201       N  
-ATOM    113  NH2 ARG A 462       7.664   0.189 -31.578  1.00 69.00           N  
-ANISOU  113  NH2 ARG A 462     7521  10020   8676   -136   -194     32       N  
-ATOM    114  N   ILE A 463       7.931   2.231 -25.902  1.00 54.81           N  
-ANISOU  114  N   ILE A 463     6080   7778   6965     52   -180    -23       N  
-ATOM    115  CA  ILE A 463       8.418   0.959 -25.384  1.00 47.52           C  
-ANISOU  115  CA  ILE A 463     5243   6837   5977    125   -226   -111       C  
-ATOM    116  C   ILE A 463       8.243  -0.185 -26.378  1.00 51.42           C  
-ANISOU  116  C   ILE A 463     5707   7400   6431    118   -239   -122       C  
-ATOM    117  O   ILE A 463       9.179  -0.935 -26.647  1.00 51.75           O  
-ANISOU  117  O   ILE A 463     5734   7500   6428    153   -296   -206       O  
-ATOM    118  CB  ILE A 463       7.733   0.605 -24.054  1.00 50.81           C  
-ANISOU  118  CB  ILE A 463     5803   7121   6381    173   -206   -110       C  
-ATOM    119  CG1 ILE A 463       8.166   1.585 -22.961  1.00 50.65           C  
-ANISOU  119  CG1 ILE A 463     5819   7037   6387    195   -209   -125       C  
-ATOM    120  CG2 ILE A 463       8.064  -0.813 -23.640  1.00 60.87           C  
-ANISOU  120  CG2 ILE A 463     7174   8370   7584    241   -254   -186       C  
-ATOM    121  CD1 ILE A 463       9.667   1.708 -22.805  1.00 54.09           C  
-ANISOU  121  CD1 ILE A 463     6228   7522   6803    236   -277   -216       C  
-ATOM    122  N   GLY A 464       7.039  -0.313 -26.922  1.00 40.85           N  
-ANISOU  122  N   GLY A 464     4357   6054   5111     74   -188    -44       N  
-ATOM    123  CA  GLY A 464       6.741  -1.393 -27.842  1.00 45.13           C  
-ANISOU  123  CA  GLY A 464     4873   6656   5618     65   -193    -50       C  
-ATOM    124  C   GLY A 464       5.355  -1.255 -28.429  1.00 64.84           C  
-ANISOU  124  C   GLY A 464     7345   9142   8150      9   -131     46       C  
-ATOM    125  O   GLY A 464       4.610  -0.342 -28.077  1.00 61.84           O  
-ANISOU  125  O   GLY A 464     6971   8703   7823    -20    -86    113       O  
-ATOM    126  N   SER A 465       5.005  -2.170 -29.326  1.00 92.31           N  
-ANISOU  126  N   SER A 465    10793  12678  11602     -5   -132     46       N  
-ATOM    127  CA  SER A 465       3.726  -2.098 -30.017  1.00 92.81           C  
-ANISOU  127  CA  SER A 465    10821  12744  11699    -58    -80    130       C  
-ATOM    128  C   SER A 465       2.973  -3.415 -29.920  1.00 95.38           C  
-ANISOU  128  C   SER A 465    11218  13030  11991    -30    -65    114       C  
-ATOM    129  O   SER A 465       3.510  -4.422 -29.466  1.00 96.59           O  
-ANISOU  129  O   SER A 465    11441  13166  12093     26   -103     39       O  
-ATOM    130  CB  SER A 465       3.939  -1.740 -31.491  1.00 91.40           C  
-ANISOU  130  CB  SER A 465    10509  12692  11527   -122    -88    163       C  
-ATOM    131  OG  SER A 465       5.085  -0.921 -31.659  1.00 97.94           O  
-ANISOU  131  OG  SER A 465    11275  13582  12357   -138   -120    139       O  
-ATOM    132  N   GLY A 466       1.720  -3.392 -30.353  1.00 87.55           N  
-ANISOU  132  N   GLY A 466    10209  12023  11033    -71    -14    182       N  
-ATOM    133  CA  GLY A 466       0.892  -4.581 -30.398  1.00 97.97           C  
-ANISOU  133  CA  GLY A 466    11583  13311  12329    -57      8    173       C  
-ATOM    134  C   GLY A 466      -0.296  -4.270 -31.279  1.00115.10           C  
-ANISOU  134  C   GLY A 466    13682  15505  14546   -117     55    252       C  
-ATOM    135  O   GLY A 466      -0.459  -3.130 -31.706  1.00120.18           O  
-ANISOU  135  O   GLY A 466    14250  16174  15239   -162     67    312       O  
-ATOM    136  N   SER A 467      -1.126  -5.266 -31.562  1.00165.47           N  
-ANISOU  136  N   SER A 467    20085  21874  20913   -116     80    250       N  
-ATOM    137  CA  SER A 467      -2.311  -5.030 -32.378  1.00167.27           C  
-ANISOU  137  CA  SER A 467    20247  22120  21187   -168    122    318       C  
-ATOM    138  C   SER A 467      -3.161  -3.912 -31.779  1.00157.19           C  
-ANISOU  138  C   SER A 467    18982  20761  19982   -193    170    377       C  
-ATOM    139  O   SER A 467      -3.636  -3.024 -32.487  1.00159.99           O  
-ANISOU  139  O   SER A 467    19251  21148  20390   -240    180    441       O  
-ATOM    140  CB  SER A 467      -3.140  -6.308 -32.506  1.00140.50           C  
-ANISOU  140  CB  SER A 467    16901  18708  17775   -158    149    298       C  
-ATOM    141  OG  SER A 467      -4.359  -6.056 -33.184  1.00143.05           O  
-ANISOU  141  OG  SER A 467    17166  19038  18150   -204    192    359       O  
-ATOM    142  N   PHE A 468      -3.332  -3.966 -30.463  1.00 94.45           N  
-ANISOU  142  N   PHE A 468    11145  12706  12036   -160    196    351       N  
-ATOM    143  CA  PHE A 468      -4.162  -3.015 -29.733  1.00 82.14           C  
-ANISOU  143  CA  PHE A 468     9608  11058  10544   -178    245    391       C  
-ATOM    144  C   PHE A 468      -3.701  -1.564 -29.877  1.00 78.20           C  
-ANISOU  144  C   PHE A 468     9036  10582  10094   -202    226    434       C  
-ATOM    145  O   PHE A 468      -4.471  -0.701 -30.299  1.00 79.69           O  
-ANISOU  145  O   PHE A 468     9160  10767  10352   -244    248    495       O  
-ATOM    146  CB  PHE A 468      -4.203  -3.405 -28.257  1.00 89.46           C  
-ANISOU  146  CB  PHE A 468    10673  11874  11444   -138    271    345       C  
-ATOM    147  CG  PHE A 468      -2.943  -4.063 -27.775  1.00 92.61           C  
-ANISOU  147  CG  PHE A 468    11139  12282  11766    -84    216    279       C  
-ATOM    148  CD1 PHE A 468      -1.818  -3.310 -27.487  1.00 95.00           C  
-ANISOU  148  CD1 PHE A 468    11426  12605  12065    -66    171    263       C  
-ATOM    149  CD2 PHE A 468      -2.882  -5.437 -27.618  1.00 93.70           C  
-ANISOU  149  CD2 PHE A 468    11356  12405  11840    -51    205    228       C  
-ATOM    150  CE1 PHE A 468      -0.656  -3.913 -27.048  1.00 93.37           C  
-ANISOU  150  CE1 PHE A 468    11277  12406  11793    -13    115    194       C  
-ATOM    151  CE2 PHE A 468      -1.723  -6.047 -27.178  1.00 94.73           C  
-ANISOU  151  CE2 PHE A 468    11549  12540  11905      3    145    163       C  
-ATOM    152  CZ  PHE A 468      -0.608  -5.284 -26.892  1.00 96.14           C  
-ANISOU  152  CZ  PHE A 468    11706  12740  12081     24     99    144       C  
-ATOM    153  N   GLY A 469      -2.448  -1.301 -29.515  1.00 71.26           N  
-ANISOU  153  N   GLY A 469     8170   9725   9182   -176    181    399       N  
-ATOM    154  CA  GLY A 469      -1.895   0.041 -29.579  1.00 61.24           C  
-ANISOU  154  CA  GLY A 469     6840   8475   7956   -198    162    432       C  
-ATOM    155  C   GLY A 469      -0.412   0.082 -29.258  1.00 53.63           C  
-ANISOU  155  C   GLY A 469     5888   7546   6943   -164    110    375       C  
-ATOM    156  O   GLY A 469       0.254  -0.953 -29.228  1.00 57.80           O  
-ANISOU  156  O   GLY A 469     6453   8103   7404   -126     78    312       O  
-ATOM    157  N   THR A 470       0.106   1.284 -29.016  1.00 48.27           N  
-ANISOU  157  N   THR A 470     5174   6863   6302   -177     98    394       N  
-ATOM    158  CA  THR A 470       1.522   1.466 -28.707  1.00 43.91           C  
-ANISOU  158  CA  THR A 470     4625   6345   5714   -149     50    338       C  
-ATOM    159  C   THR A 470       1.726   1.857 -27.244  1.00 47.95           C  
-ANISOU  159  C   THR A 470     5228   6756   6236   -106     58    306       C  
-ATOM    160  O   THR A 470       0.988   2.680 -26.702  1.00 31.29           O  
-ANISOU  160  O   THR A 470     3131   4572   4186   -122     98    348       O  
-ATOM    161  CB  THR A 470       2.165   2.537 -29.608  1.00 44.14           C  
-ANISOU  161  CB  THR A 470     4540   6460   5771   -200     25    375       C  
-ATOM    162  OG1 THR A 470       1.953   2.199 -30.985  1.00 49.36           O  
-ANISOU  162  OG1 THR A 470     5119   7217   6418   -246     18    408       O  
-ATOM    163  CG2 THR A 470       3.659   2.635 -29.340  1.00 29.03           C  
-ANISOU  163  CG2 THR A 470     2622   4590   3819   -172    -23    304       C  
-ATOM    164  N   VAL A 471       2.736   1.265 -26.613  1.00 43.44           N  
-ANISOU  164  N   VAL A 471     4718   6181   5606    -50     18    227       N  
-ATOM    165  CA  VAL A 471       3.006   1.509 -25.202  1.00 36.99           C  
-ANISOU  165  CA  VAL A 471     3999   5271   4786     -4     19    188       C  
-ATOM    166  C   VAL A 471       4.186   2.453 -25.003  1.00 40.59           C  
-ANISOU  166  C   VAL A 471     4410   5756   5254      3    -20    162       C  
-ATOM    167  O   VAL A 471       5.283   2.201 -25.500  1.00 37.34           O  
-ANISOU  167  O   VAL A 471     3954   5427   4807     15    -71    112       O  
-ATOM    168  CB  VAL A 471       3.282   0.194 -24.449  1.00 47.16           C  
-ANISOU  168  CB  VAL A 471     5406   6514   5998     60     -5    115       C  
-ATOM    169  CG1 VAL A 471       3.670   0.477 -23.006  1.00 52.79           C  
-ANISOU  169  CG1 VAL A 471     6223   7137   6700    107    -12     73       C  
-ATOM    170  CG2 VAL A 471       2.068  -0.716 -24.509  1.00 41.19           C  
-ANISOU  170  CG2 VAL A 471     4705   5715   5230     51     40    139       C  
-ATOM    171  N   TYR A 472       3.948   3.541 -24.275  1.00 44.67           N  
-ANISOU  171  N   TYR A 472     4938   6208   5827     -7      7    189       N  
-ATOM    172  CA  TYR A 472       4.997   4.494 -23.933  1.00 37.85           C  
-ANISOU  172  CA  TYR A 472     4042   5358   4982      1    -24    163       C  
-ATOM    173  C   TYR A 472       5.157   4.563 -22.422  1.00 41.84           C  
-ANISOU  173  C   TYR A 472     4658   5763   5477     56    -22    116       C  
-ATOM    174  O   TYR A 472       4.266   4.159 -21.678  1.00 45.40           O  
-ANISOU  174  O   TYR A 472     5200   6128   5921     70     17    124       O  
-ATOM    175  CB  TYR A 472       4.648   5.893 -24.444  1.00 38.30           C  
-ANISOU  175  CB  TYR A 472     4003   5428   5121    -63      1    240       C  
-ATOM    176  CG  TYR A 472       4.415   5.991 -25.932  1.00 35.94           C  
-ANISOU  176  CG  TYR A 472     3598   5221   4836   -125      0    298       C  
-ATOM    177  CD1 TYR A 472       3.240   5.523 -26.500  1.00 48.96           C  
-ANISOU  177  CD1 TYR A 472     5242   6866   6496   -151     33    351       C  
-ATOM    178  CD2 TYR A 472       5.359   6.575 -26.766  1.00 48.62           C  
-ANISOU  178  CD2 TYR A 472     5110   6921   6444   -161    -32    299       C  
-ATOM    179  CE1 TYR A 472       3.016   5.617 -27.858  1.00 57.05           C  
-ANISOU  179  CE1 TYR A 472     6172   7974   7529   -208     29    404       C  
-ATOM    180  CE2 TYR A 472       5.145   6.675 -28.128  1.00 58.72           C  
-ANISOU  180  CE2 TYR A 472     6298   8285   7727   -224    -33    354       C  
-ATOM    181  CZ  TYR A 472       3.971   6.194 -28.668  1.00 69.08           C  
-ANISOU  181  CZ  TYR A 472     7610   9590   9048   -245     -5    408       C  
-ATOM    182  OH  TYR A 472       3.747   6.290 -30.021  1.00 90.27           O  
-ANISOU  182  OH  TYR A 472    10207  12358  11734   -307     -9    464       O  
-ATOM    183  N   LYS A 473       6.296   5.081 -21.975  1.00 49.09           N  
-ANISOU  183  N   LYS A 473     5569   6694   6391     83    -62     65       N  
-ATOM    184  CA  LYS A 473       6.494   5.398 -20.567  1.00 44.03           C  
-ANISOU  184  CA  LYS A 473     5019   5961   5748    129    -62     25       C  
-ATOM    185  C   LYS A 473       6.099   6.855 -20.365  1.00 47.85           C  
-ANISOU  185  C   LYS A 473     5450   6411   6319     86    -23     81       C  
-ATOM    186  O   LYS A 473       6.333   7.687 -21.240  1.00 40.62           O  
-ANISOU  186  O   LYS A 473     4424   5560   5452     38    -27    121       O  
-ATOM    187  CB  LYS A 473       7.954   5.175 -20.167  1.00 40.56           C  
-ANISOU  187  CB  LYS A 473     4597   5550   5261    186   -132    -68       C  
-ATOM    188  CG  LYS A 473       8.261   5.472 -18.708  1.00 36.67           C  
-ANISOU  188  CG  LYS A 473     4204   4969   4762    238   -141   -115       C  
-ATOM    189  CD  LYS A 473       9.694   5.094 -18.366  1.00 41.26           C  
-ANISOU  189  CD  LYS A 473     4805   5580   5292    302   -219   -215       C  
-ATOM    190  CE  LYS A 473      10.036   5.439 -16.925  1.00 43.21           C  
-ANISOU  190  CE  LYS A 473     5149   5739   5530    354   -233   -262       C  
-ATOM    191  NZ  LYS A 473      11.428   5.038 -16.570  1.00 49.15           N  
-ANISOU  191  NZ  LYS A 473     5924   6518   6235    422   -317   -367       N  
-ATOM    192  N   GLY A 474       5.494   7.167 -19.223  1.00 49.42           N  
-ANISOU  192  N   GLY A 474     5729   6511   6538    101     13     83       N  
-ATOM    193  CA  GLY A 474       4.974   8.504 -19.000  1.00 38.50           C  
-ANISOU  193  CA  GLY A 474     4297   5087   5244     62     53    133       C  
-ATOM    194  C   GLY A 474       5.197   9.078 -17.615  1.00 29.10           C  
-ANISOU  194  C   GLY A 474     3178   3814   4066     97     60     93       C  
-ATOM    195  O   GLY A 474       5.704   8.407 -16.714  1.00 31.67           O  
-ANISOU  195  O   GLY A 474     3605   4105   4324    154     35     26       O  
-ATOM    196  N   LYS A 475       4.806  10.338 -17.452  1.00 38.64           N  
-ANISOU  196  N   LYS A 475     4331   4990   5361     62     90    134       N  
-ATOM    197  CA  LYS A 475       4.944  11.041 -16.185  1.00 38.95           C  
-ANISOU  197  CA  LYS A 475     4423   4953   5425     87    102    100       C  
-ATOM    198  C   LYS A 475       3.592  11.563 -15.713  1.00 35.72           C  
-ANISOU  198  C   LYS A 475     4027   4462   5082     55    170    142       C  
-ATOM    199  O   LYS A 475       2.995  12.432 -16.348  1.00 37.81           O  
-ANISOU  199  O   LYS A 475     4199   4733   5433      4    192    205       O  
-ATOM    200  CB  LYS A 475       5.934  12.200 -16.327  1.00 46.69           C  
-ANISOU  200  CB  LYS A 475     5316   5969   6454     80     69     92       C  
-ATOM    201  CG  LYS A 475       7.347  11.773 -16.699  1.00 51.81           C  
-ANISOU  201  CG  LYS A 475     5945   6699   7044    112      3     34       C  
-ATOM    202  CD  LYS A 475       8.255  11.720 -15.479  1.00 67.39           C  
-ANISOU  202  CD  LYS A 475     7997   8632   8976    178    -31    -53       C  
-ATOM    203  CE  LYS A 475       7.768  10.709 -14.452  1.00 73.43           C  
-ANISOU  203  CE  LYS A 475     8907   9321   9671    225    -19    -88       C  
-ATOM    204  NZ  LYS A 475       8.595  10.733 -13.213  1.00 71.61           N  
-ANISOU  204  NZ  LYS A 475     8761   9046   9402    288    -54   -169       N  
-ATOM    205  N   TRP A 476       3.113  11.021 -14.599  1.00 33.46           N  
-ANISOU  205  N   TRP A 476     3858   4099   4755     82    202    105       N  
-ATOM    206  CA  TRP A 476       1.849  11.446 -14.008  1.00 47.11           C  
-ANISOU  206  CA  TRP A 476     5609   5748   6542     52    272    128       C  
-ATOM    207  C   TRP A 476       1.856  11.136 -12.516  1.00 53.56           C  
-ANISOU  207  C   TRP A 476     6560   6486   7306     89    293     65       C  
-ATOM    208  O   TRP A 476       1.572  10.009 -12.107  1.00 68.18           O  
-ANISOU  208  O   TRP A 476     8521   8309   9076    107    306     39       O  
-ATOM    209  CB  TRP A 476       0.675  10.743 -14.693  1.00 36.85           C  
-ANISOU  209  CB  TRP A 476     4304   4451   5245     16    314    171       C  
-ATOM    210  CG  TRP A 476      -0.648  11.369 -14.392  1.00 34.34           C  
-ANISOU  210  CG  TRP A 476     3968   4068   5013    -25    382    198       C  
-ATOM    211  CD1 TRP A 476      -1.093  12.585 -14.823  1.00 31.45           C  
-ANISOU  211  CD1 TRP A 476     3492   3698   4759    -63    392    245       C  
-ATOM    212  CD2 TRP A 476      -1.704  10.813 -13.599  1.00 36.82           C  
-ANISOU  212  CD2 TRP A 476     4373   4309   5309    -34    448    176       C  
-ATOM    213  NE1 TRP A 476      -2.359  12.823 -14.346  1.00 37.83           N  
-ANISOU  213  NE1 TRP A 476     4312   4436   5626    -91    458    247       N  
-ATOM    214  CE2 TRP A 476      -2.758  11.750 -13.592  1.00 40.69           C  
-ANISOU  214  CE2 TRP A 476     4795   4758   5909    -77    498    203       C  
-ATOM    215  CE3 TRP A 476      -1.861   9.616 -12.894  1.00 27.20           C  
-ANISOU  215  CE3 TRP A 476     3289   3055   3992    -13    470    133       C  
-ATOM    216  CZ2 TRP A 476      -3.953  11.526 -12.908  1.00 25.85           C  
-ANISOU  216  CZ2 TRP A 476     2970   2808   4045   -101    572    183       C  
-ATOM    217  CZ3 TRP A 476      -3.048   9.395 -12.215  1.00 25.46           C  
-ANISOU  217  CZ3 TRP A 476     3130   2762   3780    -41    547    119       C  
-ATOM    218  CH2 TRP A 476      -4.078  10.345 -12.227  1.00 20.42           C  
-ANISOU  218  CH2 TRP A 476     2414   2089   3254    -86    600    140       C  
-ATOM    219  N   HIS A 477       2.178  12.141 -11.706  1.00 50.57           N  
-ANISOU  219  N   HIS A 477     6175   6068   6971     98    295     41       N  
-ATOM    220  CA  HIS A 477       2.384  11.937 -10.277  1.00 42.88           C  
-ANISOU  220  CA  HIS A 477     5326   5025   5939    135    304    -23       C  
-ATOM    221  C   HIS A 477       3.378  10.802 -10.086  1.00 43.64           C  
-ANISOU  221  C   HIS A 477     5517   5145   5918    193    243    -73       C  
-ATOM    222  O   HIS A 477       3.172   9.910  -9.263  1.00 40.89           O  
-ANISOU  222  O   HIS A 477     5303   4745   5487    216    254   -109       O  
-ATOM    223  CB  HIS A 477       1.070  11.602  -9.573  1.00 30.90           C  
-ANISOU  223  CB  HIS A 477     3891   3432   4420    107    383    -24       C  
-ATOM    224  CG  HIS A 477      -0.044  12.548  -9.890  1.00 26.09           C  
-ANISOU  224  CG  HIS A 477     3184   2801   3929     50    441     21       C  
-ATOM    225  ND1 HIS A 477       0.039  13.903  -9.654  1.00 30.99           N  
-ANISOU  225  ND1 HIS A 477     3724   3404   4645     38    445     25       N  
-ATOM    226  CD2 HIS A 477      -1.274  12.333 -10.415  1.00 28.04           C  
-ANISOU  226  CD2 HIS A 477     3400   3037   4217      5    495     60       C  
-ATOM    227  CE1 HIS A 477      -1.087  14.484 -10.027  1.00 30.98           C  
-ANISOU  227  CE1 HIS A 477     3649   3382   4742    -10    493     65       C  
-ATOM    228  NE2 HIS A 477      -1.901  13.552 -10.491  1.00 20.93           N  
-ANISOU  228  NE2 HIS A 477     2401   2112   3437    -31    524     85       N  
-ATOM    229  N   GLY A 478       4.455  10.841 -10.863  1.00 33.77           N  
-ANISOU  229  N   GLY A 478     4195   3973   4663    214    176    -78       N  
-ATOM    230  CA  GLY A 478       5.419   9.760 -10.889  1.00 39.71           C  
-ANISOU  230  CA  GLY A 478     5014   4759   5316    269    109   -129       C  
-ATOM    231  C   GLY A 478       5.301   8.994 -12.191  1.00 47.16           C  
-ANISOU  231  C   GLY A 478     5902   5775   6243    250     95    -93       C  
-ATOM    232  O   GLY A 478       4.593   9.418 -13.102  1.00 55.39           O  
-ANISOU  232  O   GLY A 478     6846   6847   7352    196    130    -29       O  
-ATOM    233  N   ASP A 479       5.984   7.859 -12.278  1.00 55.93           N  
-ANISOU  233  N   ASP A 479     7076   6911   7265    296     39   -138       N  
-ATOM    234  CA  ASP A 479       6.000   7.071 -13.506  1.00 53.69           C  
-ANISOU  234  CA  ASP A 479     6738   6701   6959    284     18   -116       C  
-ATOM    235  C   ASP A 479       4.654   6.411 -13.807  1.00 45.74           C  
-ANISOU  235  C   ASP A 479     5763   5666   5948    244     80    -65       C  
-ATOM    236  O   ASP A 479       3.986   5.899 -12.909  1.00 39.96           O  
-ANISOU  236  O   ASP A 479     5151   4856   5178    251    117    -76       O  
-ATOM    237  CB  ASP A 479       7.096   6.006 -13.436  1.00 45.60           C  
-ANISOU  237  CB  ASP A 479     5776   5705   5845    349    -62   -188       C  
-ATOM    238  CG  ASP A 479       8.479   6.605 -13.299  1.00 43.87           C  
-ANISOU  238  CG  ASP A 479     5507   5527   5633    387   -128   -247       C  
-ATOM    239  OD1 ASP A 479       8.648   7.795 -13.637  1.00 58.40           O  
-ANISOU  239  OD1 ASP A 479     7238   7400   7551    352   -113   -220       O  
-ATOM    240  OD2 ASP A 479       9.399   5.885 -12.858  1.00 44.35           O  
-ANISOU  240  OD2 ASP A 479     5640   5587   5625    452   -197   -322       O  
-ATOM    241  N   VAL A 480       4.265   6.431 -15.079  1.00 38.67           N  
-ANISOU  241  N   VAL A 480     4761   4839   5094    200     92    -11       N  
-ATOM    242  CA  VAL A 480       3.081   5.712 -15.536  1.00 28.34           C  
-ANISOU  242  CA  VAL A 480     3470   3518   3780    166    142     32       C  
-ATOM    243  C   VAL A 480       3.368   5.018 -16.860  1.00 37.94           C  
-ANISOU  243  C   VAL A 480     4614   4828   4974    159    107     46       C  
-ATOM    244  O   VAL A 480       4.391   5.267 -17.496  1.00 38.76           O  
-ANISOU  244  O   VAL A 480     4639   5009   5079    168     52     30       O  
-ATOM    245  CB  VAL A 480       1.861   6.640 -15.722  1.00 22.61           C  
-ANISOU  245  CB  VAL A 480     2677   2764   3151    105    215     96       C  
-ATOM    246  CG1 VAL A 480       1.454   7.270 -14.402  1.00 25.48           C  
-ANISOU  246  CG1 VAL A 480     3110   3033   3537    107    258     77       C  
-ATOM    247  CG2 VAL A 480       2.156   7.709 -16.766  1.00 17.70           C  
-ANISOU  247  CG2 VAL A 480     1903   2213   2608     69    196    144       C  
-ATOM    248  N   ALA A 481       2.457   4.143 -17.268  1.00 33.45           N  
-ANISOU  248  N   ALA A 481     4072   4253   4386    139    140     71       N  
-ATOM    249  CA  ALA A 481       2.539   3.509 -18.574  1.00 31.89           C  
-ANISOU  249  CA  ALA A 481     3800   4143   4174    124    116     90       C  
-ATOM    250  C   ALA A 481       1.317   3.905 -19.390  1.00 39.31           C  
-ANISOU  250  C   ALA A 481     4657   5095   5184     60    174    165       C  
-ATOM    251  O   ALA A 481       0.186   3.780 -18.920  1.00 36.69           O  
-ANISOU  251  O   ALA A 481     4377   4693   4870     40    236    183       O  
-ATOM    252  CB  ALA A 481       2.626   2.006 -18.432  1.00 44.43           C  
-ANISOU  252  CB  ALA A 481     5489   5720   5671    163     93     46       C  
-ATOM    253  N   VAL A 482       1.546   4.382 -20.610  1.00 40.05           N  
-ANISOU  253  N   VAL A 482     4623   5276   5317     26    154    205       N  
-ATOM    254  CA  VAL A 482       0.461   4.865 -21.457  1.00 34.13           C  
-ANISOU  254  CA  VAL A 482     3787   4541   4638    -33    196    279       C  
-ATOM    255  C   VAL A 482       0.325   4.034 -22.730  1.00 35.52           C  
-ANISOU  255  C   VAL A 482     3909   4801   4786    -52    181    299       C  
-ATOM    256  O   VAL A 482       1.240   3.992 -23.551  1.00 34.97           O  
-ANISOU  256  O   VAL A 482     3773   4822   4694    -53    131    291       O  
-ATOM    257  CB  VAL A 482       0.681   6.334 -21.857  1.00 35.28           C  
-ANISOU  257  CB  VAL A 482     3826   4713   4867    -70    188    325       C  
-ATOM    258  CG1 VAL A 482      -0.602   6.924 -22.420  1.00 32.20           C  
-ANISOU  258  CG1 VAL A 482     3370   4305   4559   -124    232    397       C  
-ATOM    259  CG2 VAL A 482       1.167   7.143 -20.663  1.00 22.59           C  
-ANISOU  259  CG2 VAL A 482     2262   3042   3279    -44    187    292       C  
-ATOM    260  N   LYS A 483      -0.819   3.376 -22.890  1.00 36.14           N  
-ANISOU  260  N   LYS A 483     4014   4851   4868    -69    226    319       N  
-ATOM    261  CA  LYS A 483      -1.088   2.613 -24.103  1.00 31.16           C  
-ANISOU  261  CA  LYS A 483     3328   4295   4217    -90    217    341       C  
-ATOM    262  C   LYS A 483      -1.955   3.419 -25.063  1.00 41.75           C  
-ANISOU  262  C   LYS A 483     4560   5664   5639   -148    240    417       C  
-ATOM    263  O   LYS A 483      -3.173   3.490 -24.904  1.00 52.40           O  
-ANISOU  263  O   LYS A 483     5919   6956   7035   -170    292    444       O  
-ATOM    264  CB  LYS A 483      -1.762   1.274 -23.781  1.00 30.76           C  
-ANISOU  264  CB  LYS A 483     3373   4202   4113    -71    246    312       C  
-ATOM    265  CG  LYS A 483      -1.991   0.395 -25.010  1.00 33.57           C  
-ANISOU  265  CG  LYS A 483     3674   4637   4445    -87    234    326       C  
-ATOM    266  CD  LYS A 483      -2.928  -0.775 -24.725  1.00 28.54           C  
-ANISOU  266  CD  LYS A 483     3122   3947   3776    -82    277    308       C  
-ATOM    267  CE  LYS A 483      -2.167  -2.050 -24.392  1.00 32.71           C  
-ANISOU  267  CE  LYS A 483     3742   4477   4210    -30    237    243       C  
-ATOM    268  NZ  LYS A 483      -3.084  -3.214 -24.206  1.00 32.44           N  
-ANISOU  268  NZ  LYS A 483     3789   4393   4144    -31    279    230       N  
-ATOM    269  N   MET A 484      -1.316   4.032 -26.053  1.00 45.24           N  
-ANISOU  269  N   MET A 484     4900   6192   6096   -175    199    449       N  
-ATOM    270  CA  MET A 484      -2.027   4.770 -27.087  1.00 43.97           C  
-ANISOU  270  CA  MET A 484     4638   6066   6004   -232    206    525       C  
-ATOM    271  C   MET A 484      -2.779   3.795 -27.983  1.00 52.03           C  
-ANISOU  271  C   MET A 484     5639   7127   7002   -248    219    541       C  
-ATOM    272  O   MET A 484      -2.164   3.013 -28.708  1.00 48.46           O  
-ANISOU  272  O   MET A 484     5166   6758   6487   -243    186    520       O  
-ATOM    273  CB  MET A 484      -1.044   5.574 -27.937  1.00 41.09           C  
-ANISOU  273  CB  MET A 484     4181   5787   5644   -261    157    552       C  
-ATOM    274  CG  MET A 484      -0.078   6.436 -27.146  1.00 34.22           C  
-ANISOU  274  CG  MET A 484     3324   4893   4784   -243    138    526       C  
-ATOM    275  SD  MET A 484      -0.908   7.708 -26.184  1.00 53.62           S  
-ANISOU  275  SD  MET A 484     5795   7235   7343   -253    178    560       S  
-ATOM    276  CE  MET A 484       0.480   8.754 -25.763  1.00108.04           C  
-ANISOU  276  CE  MET A 484    12665  14141  14242   -245    139    537       C  
-ATOM    277  N   LEU A 485      -4.106   3.833 -27.935  1.00 51.35           N  
-ANISOU  277  N   LEU A 485     5555   6985   6971   -267    266    571       N  
-ATOM    278  CA  LEU A 485      -4.900   2.963 -28.792  1.00 50.67           C  
-ANISOU  278  CA  LEU A 485     5445   6935   6873   -284    280    585       C  
-ATOM    279  C   LEU A 485      -4.709   3.348 -30.252  1.00 65.91           C  
-ANISOU  279  C   LEU A 485     7262   8966   8813   -327    239    642       C  
-ATOM    280  O   LEU A 485      -4.552   4.526 -30.578  1.00 57.21           O  
-ANISOU  280  O   LEU A 485     6097   7875   7763   -358    218    691       O  
-ATOM    281  CB  LEU A 485      -6.382   3.008 -28.414  1.00 38.04           C  
-ANISOU  281  CB  LEU A 485     3864   5252   5338   -298    340    599       C  
-ATOM    282  CG  LEU A 485      -6.741   2.481 -27.025  1.00 41.86           C  
-ANISOU  282  CG  LEU A 485     4466   5636   5803   -266    391    542       C  
-ATOM    283  CD1 LEU A 485      -8.169   1.972 -27.014  1.00 45.83           C  
-ANISOU  283  CD1 LEU A 485     4982   6091   6340   -285    451    542       C  
-ATOM    284  CD2 LEU A 485      -5.788   1.374 -26.614  1.00 42.81           C  
-ANISOU  284  CD2 LEU A 485     4671   5773   5820   -222    369    483       C  
-ATOM    285  N   ASN A 486      -4.715   2.347 -31.125  1.00 76.57           N  
-ANISOU  285  N   ASN A 486     8592  10390  10112   -331    227    633       N  
-ATOM    286  CA  ASN A 486      -4.555   2.575 -32.555  1.00 81.69           C  
-ANISOU  286  CA  ASN A 486     9140  11142  10758   -376    191    683       C  
-ATOM    287  C   ASN A 486      -5.810   3.210 -33.150  1.00 70.37           C  
-ANISOU  287  C   ASN A 486     7647   9686   9404   -416    207    752       C  
-ATOM    288  O   ASN A 486      -6.490   2.611 -33.982  1.00 71.83           O  
-ANISOU  288  O   ASN A 486     7798   9910   9584   -433    211    768       O  
-ATOM    289  CB  ASN A 486      -4.227   1.259 -33.264  1.00113.06           C  
-ANISOU  289  CB  ASN A 486    13108  15198  14651   -366    176    645       C  
-ATOM    290  CG  ASN A 486      -3.659   1.467 -34.655  1.00117.89           C  
-ANISOU  290  CG  ASN A 486    13623  15933  15238   -411    132    679       C  
-ATOM    291  OD1 ASN A 486      -2.535   1.944 -34.817  1.00122.61           O  
-ANISOU  291  OD1 ASN A 486    14192  16584  15809   -421     97    671       O  
-ATOM    292  ND2 ASN A 486      -4.430   1.094 -35.668  1.00111.65           N  
-ANISOU  292  ND2 ASN A 486    12781  15188  14452   -440    135    714       N  
-ATOM    293  N   VAL A 487      -6.111   4.427 -32.708  1.00 59.80           N  
-ANISOU  293  N   VAL A 487     6296   8283   8143   -430    212    789       N  
-ATOM    294  CA  VAL A 487      -7.285   5.160 -33.166  1.00 58.57           C  
-ANISOU  294  CA  VAL A 487     6086   8093   8076   -463    218    850       C  
-ATOM    295  C   VAL A 487      -6.971   6.649 -33.314  1.00 78.44           C  
-ANISOU  295  C   VAL A 487     8552  10599  10653   -494    184    908       C  
-ATOM    296  O   VAL A 487      -6.868   7.370 -32.321  1.00 80.16           O  
-ANISOU  296  O   VAL A 487     8801  10741  10914   -478    198    895       O  
-ATOM    297  CB  VAL A 487      -8.478   4.968 -32.199  1.00 51.38           C  
-ANISOU  297  CB  VAL A 487     5228   7073   7222   -441    278    821       C  
-ATOM    298  CG1 VAL A 487      -9.558   6.012 -32.450  1.00 38.44           C  
-ANISOU  298  CG1 VAL A 487     3530   5383   5694   -470    278    874       C  
-ATOM    299  CG2 VAL A 487      -9.044   3.561 -32.327  1.00 53.66           C  
-ANISOU  299  CG2 VAL A 487     5551   7374   7464   -425    311    780       C  
-ATOM    300  N   THR A 488      -6.808   7.096 -34.558  1.00114.89           N  
-ANISOU  300  N   THR A 488    13094  15293  15268   -540    139    970       N  
-ATOM    301  CA  THR A 488      -6.555   8.505 -34.850  1.00114.80           C  
-ANISOU  301  CA  THR A 488    13034  15273  15312   -578    101   1034       C  
-ATOM    302  C   THR A 488      -7.637   9.382 -34.230  1.00111.40           C  
-ANISOU  302  C   THR A 488    12603  14730  14995   -573    118   1057       C  
-ATOM    303  O   THR A 488      -7.388  10.123 -33.277  1.00108.52           O  
-ANISOU  303  O   THR A 488    12263  14296  14672   -558    128   1042       O  
-ATOM    304  CB  THR A 488      -6.534   8.782 -36.372  1.00 96.39           C  
-ANISOU  304  CB  THR A 488    10627  13031  12965   -636     52   1107       C  
-ATOM    305  OG1 THR A 488      -7.778   8.375 -36.956  1.00 95.48           O  
-ANISOU  305  OG1 THR A 488    10488  12908  12883   -642     58   1130       O  
-ATOM    306  CG2 THR A 488      -5.401   8.034 -37.048  1.00 92.33           C  
-ANISOU  306  CG2 THR A 488    10101  12637  12342   -650     35   1082       C  
-ATOM    307  N   ALA A 489      -8.839   9.289 -34.789  1.00 85.22           N  
-ANISOU  307  N   ALA A 489     9253  11396  11730   -585    119   1087       N  
-ATOM    308  CA  ALA A 489      -9.990  10.035 -34.300  1.00 89.99           C  
-ANISOU  308  CA  ALA A 489     9847  11897  12449   -581    133   1099       C  
-ATOM    309  C   ALA A 489     -11.098   9.068 -33.898  1.00 85.87           C  
-ANISOU  309  C   ALA A 489     9353  11332  11942   -553    188   1046       C  
-ATOM    310  O   ALA A 489     -11.404   8.131 -34.633  1.00 87.48           O  
-ANISOU  310  O   ALA A 489     9545  11594  12100   -558    191   1043       O  
-ATOM    311  CB  ALA A 489     -10.483  11.000 -35.366  1.00124.82           C  
-ANISOU  311  CB  ALA A 489    14185  16316  16926   -624     74   1184       C  
-ATOM    312  N   PRO A 490     -11.699   9.294 -32.721  1.00 83.92           N  
-ANISOU  312  N   PRO A 490     9143  10984  11757   -528    236   1000       N  
-ATOM    313  CA  PRO A 490     -12.731   8.424 -32.150  1.00 80.01           C  
-ANISOU  313  CA  PRO A 490     8685  10438  11278   -507    301    939       C  
-ATOM    314  C   PRO A 490     -14.145   8.902 -32.465  1.00 76.07           C  
-ANISOU  314  C   PRO A 490     8127   9885  10891   -521    301    955       C  
-ATOM    315  O   PRO A 490     -14.460  10.065 -32.222  1.00 68.93           O  
-ANISOU  315  O   PRO A 490     7190   8920  10082   -528    281    978       O  
-ATOM    316  CB  PRO A 490     -12.494   8.556 -30.638  1.00 76.21           C  
-ANISOU  316  CB  PRO A 490     8278   9876  10801   -479    351    879       C  
-ATOM    317  CG  PRO A 490     -11.459   9.677 -30.464  1.00 77.25           C  
-ANISOU  317  CG  PRO A 490     8398  10011  10943   -484    307    913       C  
-ATOM    318  CD  PRO A 490     -11.325  10.361 -31.784  1.00 81.29           C  
-ANISOU  318  CD  PRO A 490     8826  10582  11477   -520    237    996       C  
-ATOM    319  N   THR A 491     -14.988   8.016 -32.987  1.00 90.34           N  
-ANISOU  319  N   THR A 491     9920  11712  12692   -523    322    939       N  
-ATOM    320  CA  THR A 491     -16.397   8.338 -33.177  1.00 96.80           C  
-ANISOU  320  CA  THR A 491    10686  12475  13620   -530    329    935       C  
-ATOM    321  C   THR A 491     -17.145   8.176 -31.865  1.00 99.78           C  
-ANISOU  321  C   THR A 491    11110  12756  14047   -513    410    854       C  
-ATOM    322  O   THR A 491     -16.712   7.423 -30.993  1.00104.47           O  
-ANISOU  322  O   THR A 491    11786  13341  14569   -497    465    801       O  
-ATOM    323  CB  THR A 491     -17.057   7.434 -34.226  1.00 85.30           C  
-ANISOU  323  CB  THR A 491     9193  11077  12141   -539    324    941       C  
-ATOM    324  OG1 THR A 491     -16.877   6.061 -33.857  1.00 75.67           O  
-ANISOU  324  OG1 THR A 491     8039   9884  10830   -524    383    883       O  
-ATOM    325  CG2 THR A 491     -16.441   7.680 -35.583  1.00 88.91           C  
-ANISOU  325  CG2 THR A 491     9597  11629  12555   -564    243   1022       C  
-ATOM    326  N   PRO A 492     -18.271   8.888 -31.717  1.00 87.82           N  
-ANISOU  326  N   PRO A 492     9545  11168  12655   -518    415    841       N  
-ATOM    327  CA  PRO A 492     -19.104   8.753 -30.520  1.00 85.23           C  
-ANISOU  327  CA  PRO A 492     9253  10751  12381   -510    497    757       C  
-ATOM    328  C   PRO A 492     -19.391   7.287 -30.214  1.00 81.77           C  
-ANISOU  328  C   PRO A 492     8878  10327  11864   -506    572    694       C  
-ATOM    329  O   PRO A 492     -19.469   6.914 -29.044  1.00 92.13           O  
-ANISOU  329  O   PRO A 492    10265  11585  13156   -501    646    628       O  
-ATOM    330  CB  PRO A 492     -20.394   9.474 -30.914  1.00 77.95           C  
-ANISOU  330  CB  PRO A 492     8241   9778  11597   -520    476    755       C  
-ATOM    331  CG  PRO A 492     -19.950  10.506 -31.892  1.00 78.39           C  
-ANISOU  331  CG  PRO A 492     8233   9866  11687   -528    374    848       C  
-ATOM    332  CD  PRO A 492     -18.805   9.894 -32.653  1.00 76.33           C  
-ANISOU  332  CD  PRO A 492     7998   9709  11296   -534    340    903       C  
-ATOM    333  N   GLN A 493     -19.537   6.471 -31.255  1.00 56.37           N  
-ANISOU  333  N   GLN A 493     5635   7181   8602   -511    552    716       N  
-ATOM    334  CA  GLN A 493     -19.777   5.040 -31.081  1.00 73.95           C  
-ANISOU  334  CA  GLN A 493     7920   9425  10752   -509    617    661       C  
-ATOM    335  C   GLN A 493     -18.520   4.313 -30.598  1.00 62.30           C  
-ANISOU  335  C   GLN A 493     6539   7985   9147   -492    628    654       C  
-ATOM    336  O   GLN A 493     -18.603   3.361 -29.820  1.00 58.59           O  
-ANISOU  336  O   GLN A 493     6153   7487   8621   -486    695    594       O  
-ATOM    337  CB  GLN A 493     -20.292   4.407 -32.379  1.00160.88           C  
-ANISOU  337  CB  GLN A 493    18868  20503  21755   -518    588    685       C  
-ATOM    338  CG  GLN A 493     -21.688   4.850 -32.801  1.00180.89           C  
-ANISOU  338  CG  GLN A 493    21318  23000  24414   -529    585    672       C  
-ATOM    339  CD  GLN A 493     -22.146   4.183 -34.087  1.00194.82           C  
-ANISOU  339  CD  GLN A 493    23024  24835  26164   -536    554    694       C  
-ATOM    340  OE1 GLN A 493     -21.330   3.734 -34.892  1.00196.55           O  
-ANISOU  340  OE1 GLN A 493    23245  25142  26293   -536    510    742       O  
-ATOM    341  NE2 GLN A 493     -23.458   4.117 -34.286  1.00200.76           N  
-ANISOU  341  NE2 GLN A 493    23721  25552  27006   -542    576    653       N  
-ATOM    342  N   GLN A 494     -17.359   4.761 -31.071  1.00 75.93           N  
-ANISOU  342  N   GLN A 494     8252   9770  10827   -487    560    714       N  
-ATOM    343  CA  GLN A 494     -16.081   4.241 -30.594  1.00 78.71           C  
-ANISOU  343  CA  GLN A 494     8685  10153  11068   -468    559    703       C  
-ATOM    344  C   GLN A 494     -15.832   4.682 -29.152  1.00 79.35           C  
-ANISOU  344  C   GLN A 494     8839  10151  11159   -455    601    661       C  
-ATOM    345  O   GLN A 494     -15.166   3.988 -28.383  1.00 77.04           O  
-ANISOU  345  O   GLN A 494     8640   9851  10782   -435    628    622       O  
-ATOM    346  CB  GLN A 494     -14.932   4.717 -31.492  1.00 70.27           C  
-ANISOU  346  CB  GLN A 494     7572   9170   9957   -471    477    771       C  
-ATOM    347  CG  GLN A 494     -14.786   3.953 -32.804  1.00 64.31           C  
-ANISOU  347  CG  GLN A 494     6774   8516   9145   -482    440    801       C  
-ATOM    348  CD  GLN A 494     -13.687   4.518 -33.691  1.00 55.96           C  
-ANISOU  348  CD  GLN A 494     5669   7544   8049   -495    364    865       C  
-ATOM    349  OE1 GLN A 494     -13.432   5.724 -33.693  1.00 44.74           O  
-ANISOU  349  OE1 GLN A 494     4214   6104   6681   -508    327    908       O  
-ATOM    350  NE2 GLN A 494     -13.034   3.647 -34.453  1.00 53.40           N  
-ANISOU  350  NE2 GLN A 494     5342   7313   7633   -496    341    867       N  
-ATOM    351  N   LEU A 495     -16.377   5.840 -28.793  1.00 76.05           N  
-ANISOU  351  N   LEU A 495     8379   9670  10848   -464    602    667       N  
-ATOM    352  CA  LEU A 495     -16.180   6.407 -27.465  1.00 67.39           C  
-ANISOU  352  CA  LEU A 495     7339   8496   9772   -455    638    628       C  
-ATOM    353  C   LEU A 495     -16.838   5.541 -26.395  1.00 65.37           C  
-ANISOU  353  C   LEU A 495     7170   8175   9491   -455    731    547       C  
-ATOM    354  O   LEU A 495     -16.260   5.299 -25.336  1.00 70.56           O  
-ANISOU  354  O   LEU A 495     7922   8799  10089   -441    763    509       O  
-ATOM    355  CB  LEU A 495     -16.728   7.835 -27.410  1.00 65.00           C  
-ANISOU  355  CB  LEU A 495     6960   8139   9599   -467    616    649       C  
-ATOM    356  CG  LEU A 495     -15.883   8.838 -26.626  1.00 72.34           C  
-ANISOU  356  CG  LEU A 495     7909   9034  10541   -456    598    656       C  
-ATOM    357  CD1 LEU A 495     -14.436   8.774 -27.085  1.00 76.71           C  
-ANISOU  357  CD1 LEU A 495     8478   9666  11002   -444    538    703       C  
-ATOM    358  CD2 LEU A 495     -16.435  10.246 -26.780  1.00 78.47           C  
-ANISOU  358  CD2 LEU A 495     8599   9764  11452   -468    563    685       C  
-ATOM    359  N   GLN A 496     -18.050   5.075 -26.681  1.00 56.29           N  
-ANISOU  359  N   GLN A 496     5991   7009   8388   -473    773    519       N  
-ATOM    360  CA  GLN A 496     -18.762   4.186 -25.771  1.00 57.69           C  
-ANISOU  360  CA  GLN A 496     6249   7129   8541   -483    866    441       C  
-ATOM    361  C   GLN A 496     -18.076   2.827 -25.721  1.00 64.96           C  
-ANISOU  361  C   GLN A 496     7265   8089   9327   -469    878    428       C  
-ATOM    362  O   GLN A 496     -17.937   2.227 -24.657  1.00 71.39           O  
-ANISOU  362  O   GLN A 496     8189   8856  10078   -467    934    377       O  
-ATOM    363  CB  GLN A 496     -20.220   4.026 -26.203  1.00 59.76           C  
-ANISOU  363  CB  GLN A 496     6444   7371   8891   -508    905    411       C  
-ATOM    364  CG  GLN A 496     -21.069   3.240 -25.218  1.00 69.61           C  
-ANISOU  364  CG  GLN A 496     7769   8553  10127   -530   1011    324       C  
-ATOM    365  CD  GLN A 496     -21.079   3.865 -23.835  1.00 75.89           C  
-ANISOU  365  CD  GLN A 496     8622   9267  10946   -537   1063    275       C  
-ATOM    366  OE1 GLN A 496     -20.352   3.434 -22.941  1.00 74.42           O  
-ANISOU  366  OE1 GLN A 496     8548   9061  10666   -529   1089    256       O  
-ATOM    367  NE2 GLN A 496     -21.903   4.892 -23.656  1.00 75.58           N  
-ANISOU  367  NE2 GLN A 496     8505   9179  11034   -552   1074    253       N  
-ATOM    368  N   ALA A 497     -17.648   2.346 -26.883  1.00 83.32           N  
-ANISOU  368  N   ALA A 497     9549  10501  11609   -461    821    474       N  
-ATOM    369  CA  ALA A 497     -16.910   1.094 -26.962  1.00 82.42           C  
-ANISOU  369  CA  ALA A 497     9512  10431  11372   -443    817    463       C  
-ATOM    370  C   ALA A 497     -15.687   1.142 -26.051  1.00 82.83           C  
-ANISOU  370  C   ALA A 497     9657  10468  11347   -416    803    454       C  
-ATOM    371  O   ALA A 497     -15.313   0.139 -25.444  1.00 87.58           O  
-ANISOU  371  O   ALA A 497    10365  11054  11857   -402    828    415       O  
-ATOM    372  CB  ALA A 497     -16.495   0.815 -28.395  1.00 47.45           C  
-ANISOU  372  CB  ALA A 497     5007   6105   6916   -439    748    517       C  
-ATOM    373  N   PHE A 498     -15.071   2.317 -25.961  1.00 65.89           N  
-ANISOU  373  N   PHE A 498     7471   8324   9239   -409    757    488       N  
-ATOM    374  CA  PHE A 498     -13.889   2.510 -25.129  1.00 55.10           C  
-ANISOU  374  CA  PHE A 498     6179   6946   7811   -382    737    478       C  
-ATOM    375  C   PHE A 498     -14.258   2.462 -23.651  1.00 56.42           C  
-ANISOU  375  C   PHE A 498     6448   7015   7974   -384    809    417       C  
-ATOM    376  O   PHE A 498     -13.652   1.724 -22.873  1.00 62.66           O  
-ANISOU  376  O   PHE A 498     7352   7785   8671   -363    822    381       O  
-ATOM    377  CB  PHE A 498     -13.217   3.844 -25.468  1.00 47.58           C  
-ANISOU  377  CB  PHE A 498     5148   6020   6911   -379    673    530       C  
-ATOM    378  CG  PHE A 498     -11.924   4.079 -24.737  1.00 41.86           C  
-ANISOU  378  CG  PHE A 498     4487   5293   6125   -350    644    519       C  
-ATOM    379  CD1 PHE A 498     -10.870   3.191 -24.867  1.00 37.86           C  
-ANISOU  379  CD1 PHE A 498     4034   4841   5511   -322    610    507       C  
-ATOM    380  CD2 PHE A 498     -11.757   5.198 -23.938  1.00 33.31           C  
-ANISOU  380  CD2 PHE A 498     3404   4157   5098   -348    647    516       C  
-ATOM    381  CE1 PHE A 498      -9.678   3.407 -24.202  1.00 34.08           C  
-ANISOU  381  CE1 PHE A 498     3609   4360   4980   -292    579    490       C  
-ATOM    382  CE2 PHE A 498     -10.566   5.421 -23.272  1.00 30.83           C  
-ANISOU  382  CE2 PHE A 498     3144   3841   4729   -320    619    502       C  
-ATOM    383  CZ  PHE A 498      -9.525   4.524 -23.404  1.00 28.01           C  
-ANISOU  383  CZ  PHE A 498     2841   3538   4265   -291    584    488       C  
-ATOM    384  N   LYS A 499     -15.260   3.248 -23.275  1.00 42.85           N  
-ANISOU  384  N   LYS A 499     4689   5236   6357   -409    854    403       N  
-ATOM    385  CA  LYS A 499     -15.724   3.305 -21.894  1.00 58.95           C  
-ANISOU  385  CA  LYS A 499     6814   7184   8401   -421    930    341       C  
-ATOM    386  C   LYS A 499     -16.095   1.926 -21.355  1.00 73.59           C  
-ANISOU  386  C   LYS A 499     8782   9008  10170   -430    996    288       C  
-ATOM    387  O   LYS A 499     -15.852   1.623 -20.187  1.00 86.64           O  
-ANISOU  387  O   LYS A 499    10553  10605  11762   -427   1036    245       O  
-ATOM    388  CB  LYS A 499     -16.917   4.255 -21.769  1.00 70.78           C  
-ANISOU  388  CB  LYS A 499     8231   8631  10032   -452    970    325       C  
-ATOM    389  CG  LYS A 499     -16.583   5.704 -22.078  1.00 78.32           C  
-ANISOU  389  CG  LYS A 499     9089   9594  11077   -444    908    372       C  
-ATOM    390  CD  LYS A 499     -17.806   6.593 -21.940  1.00 88.84           C  
-ANISOU  390  CD  LYS A 499    10342  10869  12546   -471    943    348       C  
-ATOM    391  CE  LYS A 499     -17.469   8.040 -22.252  1.00 93.87           C  
-ANISOU  391  CE  LYS A 499    10887  11507  13274   -463    875    397       C  
-ATOM    392  NZ  LYS A 499     -18.670   8.912 -22.154  1.00100.85           N  
-ANISOU  392  NZ  LYS A 499    11687  12331  14299   -485    899    369       N  
-ATOM    393  N   ASN A 500     -16.688   1.096 -22.208  1.00 78.59           N  
-ANISOU  393  N   ASN A 500     9385   9677  10797   -442   1005    292       N  
-ATOM    394  CA  ASN A 500     -17.090  -0.248 -21.808  1.00 83.44           C  
-ANISOU  394  CA  ASN A 500    10103  10265  11335   -455   1066    245       C  
-ATOM    395  C   ASN A 500     -15.892  -1.109 -21.423  1.00 85.66           C  
-ANISOU  395  C   ASN A 500    10503  10559  11486   -420   1032    242       C  
-ATOM    396  O   ASN A 500     -15.963  -1.903 -20.485  1.00 89.30           O  
-ANISOU  396  O   ASN A 500    11094  10963  11874   -427   1082    197       O  
-ATOM    397  CB  ASN A 500     -17.896  -0.926 -22.919  1.00 89.46           C  
-ANISOU  397  CB  ASN A 500    10796  11072  12123   -472   1074    253       C  
-ATOM    398  CG  ASN A 500     -19.212  -0.224 -23.201  1.00 81.66           C  
-ANISOU  398  CG  ASN A 500     9703  10059  11263   -506   1114    240       C  
-ATOM    399  OD1 ASN A 500     -19.416   0.923 -22.804  1.00 79.26           O  
-ANISOU  399  OD1 ASN A 500     9354   9720  11042   -513   1116    239       O  
-ATOM    400  ND2 ASN A 500     -20.112  -0.913 -23.892  1.00 77.81           N  
-ANISOU  400  ND2 ASN A 500     9175   9591  10798   -527   1143    226       N  
-ATOM    401  N   GLU A 501     -14.793  -0.946 -22.154  1.00 90.19           N  
-ANISOU  401  N   GLU A 501    11031  11207  12031   -384    943    288       N  
-ATOM    402  CA  GLU A 501     -13.563  -1.676 -21.868  1.00 95.27           C  
-ANISOU  402  CA  GLU A 501    11770  11869  12560   -344    896    281       C  
-ATOM    403  C   GLU A 501     -12.885  -1.143 -20.608  1.00 91.45           C  
-ANISOU  403  C   GLU A 501    11374  11327  12047   -326    896    259       C  
-ATOM    404  O   GLU A 501     -12.290  -1.903 -19.845  1.00 94.53           O  
-ANISOU  404  O   GLU A 501    11891  11685  12341   -303    892    227       O  
-ATOM    405  CB  GLU A 501     -12.604  -1.609 -23.060  1.00106.17           C  
-ANISOU  405  CB  GLU A 501    13064  13352  13925   -317    804    328       C  
-ATOM    406  CG  GLU A 501     -13.100  -2.336 -24.302  1.00108.92           C  
-ANISOU  406  CG  GLU A 501    13341  13765  14278   -330    796    346       C  
-ATOM    407  CD  GLU A 501     -12.148  -2.207 -25.477  1.00115.64           C  
-ANISOU  407  CD  GLU A 501    14105  14722  15113   -310    710    390       C  
-ATOM    408  OE1 GLU A 501     -11.204  -1.394 -25.395  1.00120.02           O  
-ANISOU  408  OE1 GLU A 501    14636  15299  15668   -292    659    410       O  
-ATOM    409  OE2 GLU A 501     -12.348  -2.916 -26.485  1.00116.17           O  
-ANISOU  409  OE2 GLU A 501    14124  14851  15164   -315    695    401       O  
-ATOM    410  N   VAL A 502     -12.978   0.167 -20.395  1.00 82.41           N  
-ANISOU  410  N   VAL A 502    10160  10165  10985   -335    895    274       N  
-ATOM    411  CA  VAL A 502     -12.426   0.787 -19.193  1.00 69.64           C  
-ANISOU  411  CA  VAL A 502     8615   8492   9352   -320    900    250       C  
-ATOM    412  C   VAL A 502     -13.242   0.399 -17.966  1.00 71.45           C  
-ANISOU  412  C   VAL A 502     8959   8628   9561   -350    992    193       C  
-ATOM    413  O   VAL A 502     -12.690   0.154 -16.894  1.00 70.00           O  
-ANISOU  413  O   VAL A 502     8898   8396   9302   -334    998    161       O  
-ATOM    414  CB  VAL A 502     -12.383   2.323 -19.308  1.00 49.22           C  
-ANISOU  414  CB  VAL A 502     5919   5911   6870   -325    878    280       C  
-ATOM    415  CG1 VAL A 502     -12.027   2.947 -17.968  1.00 42.52           C  
-ANISOU  415  CG1 VAL A 502     5146   4994   6014   -317    898    245       C  
-ATOM    416  CG2 VAL A 502     -11.388   2.746 -20.374  1.00 44.26           C  
-ANISOU  416  CG2 VAL A 502     5198   5371   6246   -300    786    334       C  
-ATOM    417  N   GLY A 503     -14.560   0.344 -18.133  1.00 76.74           N  
-ANISOU  417  N   GLY A 503     9588   9273  10297   -395   1063    177       N  
-ATOM    418  CA  GLY A 503     -15.452  -0.057 -17.061  1.00 73.78           C  
-ANISOU  418  CA  GLY A 503     9313   8814   9906   -435   1161    118       C  
-ATOM    419  C   GLY A 503     -15.149  -1.456 -16.560  1.00 74.09           C  
-ANISOU  419  C   GLY A 503     9508   8828   9814   -429   1176     91       C  
-ATOM    420  O   GLY A 503     -15.485  -1.806 -15.429  1.00 79.77           O  
-ANISOU  420  O   GLY A 503    10351   9473  10485   -455   1243     44       O  
-ATOM    421  N   VAL A 504     -14.514  -2.259 -17.409  1.00 67.53           N  
-ANISOU  421  N   VAL A 504     8673   8058   8927   -396   1112    120       N  
-ATOM    422  CA  VAL A 504     -14.113  -3.613 -17.038  1.00 62.72           C  
-ANISOU  422  CA  VAL A 504     8208   7427   8195   -382   1108     98       C  
-ATOM    423  C   VAL A 504     -12.778  -3.617 -16.294  1.00 58.02           C  
-ANISOU  423  C   VAL A 504     7713   6818   7513   -332   1043     93       C  
-ATOM    424  O   VAL A 504     -12.592  -4.374 -15.343  1.00 55.44           O  
-ANISOU  424  O   VAL A 504     7543   6429   7092   -331   1062     60       O  
-ATOM    425  CB  VAL A 504     -14.045  -4.542 -18.267  1.00 52.25           C  
-ANISOU  425  CB  VAL A 504     6833   6171   6849   -368   1068    121       C  
-ATOM    426  CG1 VAL A 504     -13.110  -5.715 -18.005  1.00 46.48           C  
-ANISOU  426  CG1 VAL A 504     6232   5434   5993   -329   1018    108       C  
-ATOM    427  CG2 VAL A 504     -15.437  -5.032 -18.637  1.00 50.12           C  
-ANISOU  427  CG2 VAL A 504     6532   5886   6624   -421   1149    104       C  
-ATOM    428  N   LEU A 505     -11.853  -2.769 -16.732  1.00 41.49           N  
-ANISOU  428  N   LEU A 505     5531   4781   5451   -293    966    125       N  
-ATOM    429  CA  LEU A 505     -10.589  -2.592 -16.030  1.00 38.00           C  
-ANISOU  429  CA  LEU A 505     5166   4329   4944   -245    903    115       C  
-ATOM    430  C   LEU A 505     -10.851  -1.925 -14.686  1.00 46.72           C  
-ANISOU  430  C   LEU A 505     6345   5350   6054   -265    959     83       C  
-ATOM    431  O   LEU A 505     -10.072  -2.055 -13.743  1.00 45.11           O  
-ANISOU  431  O   LEU A 505     6258   5107   5774   -235    932     59       O  
-ATOM    432  CB  LEU A 505      -9.636  -1.720 -16.849  1.00 32.36           C  
-ANISOU  432  CB  LEU A 505     4323   3697   4275   -209    818    153       C  
-ATOM    433  CG  LEU A 505      -9.174  -2.229 -18.213  1.00 34.41           C  
-ANISOU  433  CG  LEU A 505     4496   4051   4526   -188    753    184       C  
-ATOM    434  CD1 LEU A 505      -8.315  -1.180 -18.904  1.00 33.70           C  
-ANISOU  434  CD1 LEU A 505     4281   4035   4487   -167    684    219       C  
-ATOM    435  CD2 LEU A 505      -8.413  -3.533 -18.068  1.00 31.76           C  
-ANISOU  435  CD2 LEU A 505     4274   3716   4077   -148    707    155       C  
-ATOM    436  N   ARG A 506     -11.966  -1.209 -14.615  1.00 51.40           N  
-ANISOU  436  N   ARG A 506     6870   5919   6741   -315   1034     80       N  
-ATOM    437  CA  ARG A 506     -12.305  -0.401 -13.453  1.00 50.16           C  
-ANISOU  437  CA  ARG A 506     6753   5692   6611   -340   1091     47       C  
-ATOM    438  C   ARG A 506     -12.495  -1.253 -12.202  1.00 51.79           C  
-ANISOU  438  C   ARG A 506     7147   5817   6714   -360   1148     -2       C  
-ATOM    439  O   ARG A 506     -12.362  -0.764 -11.080  1.00 60.30           O  
-ANISOU  439  O   ARG A 506     8299   6839   7773   -367   1174    -32       O  
-ATOM    440  CB  ARG A 506     -13.578   0.394 -13.742  1.00 54.27           C  
-ANISOU  440  CB  ARG A 506     7156   6206   7259   -392   1161     44       C  
-ATOM    441  CG  ARG A 506     -13.690   1.705 -12.999  1.00 58.09           C  
-ANISOU  441  CG  ARG A 506     7602   6653   7818   -403   1185     27       C  
-ATOM    442  CD  ARG A 506     -15.014   2.379 -13.311  1.00 69.64           C  
-ANISOU  442  CD  ARG A 506     8948   8104   9409   -453   1250     16       C  
-ATOM    443  NE  ARG A 506     -15.208   3.586 -12.516  1.00 79.87           N  
-ANISOU  443  NE  ARG A 506    10212   9355  10778   -467   1279    -12       N  
-ATOM    444  CZ  ARG A 506     -15.550   3.584 -11.231  1.00 70.43           C  
-ANISOU  444  CZ  ARG A 506     9121   8089   9551   -498   1353    -71       C  
-ATOM    445  NH1 ARG A 506     -15.732   2.439 -10.590  1.00 66.24           N  
-ANISOU  445  NH1 ARG A 506     8739   7520   8911   -521   1405   -105       N  
-ATOM    446  NH2 ARG A 506     -15.705   4.728 -10.584  1.00 66.00           N  
-ANISOU  446  NH2 ARG A 506     8516   7495   9065   -509   1375    -97       N  
-ATOM    447  N   LYS A 507     -12.803  -2.530 -12.400  1.00 52.87           N  
-ANISOU  447  N   LYS A 507     7364   5944   6781   -373   1167    -10       N  
-ATOM    448  CA  LYS A 507     -13.107  -3.417 -11.282  1.00 60.87           C  
-ANISOU  448  CA  LYS A 507     8561   6874   7693   -403   1226    -52       C  
-ATOM    449  C   LYS A 507     -11.965  -4.367 -10.956  1.00 55.14           C  
-ANISOU  449  C   LYS A 507     7976   6136   6837   -349   1147    -52       C  
-ATOM    450  O   LYS A 507     -12.189  -5.468 -10.461  1.00 55.30           O  
-ANISOU  450  O   LYS A 507     8144   6103   6764   -369   1176    -74       O  
-ATOM    451  CB  LYS A 507     -14.381  -4.212 -11.563  1.00 88.87           C  
-ANISOU  451  CB  LYS A 507    12117  10400  11250   -465   1315    -70       C  
-ATOM    452  CG  LYS A 507     -14.444  -4.813 -12.949  1.00 97.15           C  
-ANISOU  452  CG  LYS A 507    13069  11520  12323   -447   1274    -36       C  
-ATOM    453  CD  LYS A 507     -15.832  -5.342 -13.242  1.00102.47           C  
-ANISOU  453  CD  LYS A 507    13723  12177  13035   -513   1371    -59       C  
-ATOM    454  CE  LYS A 507     -16.890  -4.277 -12.985  1.00110.08           C  
-ANISOU  454  CE  LYS A 507    14593  13119  14112   -565   1454    -84       C  
-ATOM    455  NZ  LYS A 507     -18.154  -4.578 -13.715  1.00114.39           N  
-ANISOU  455  NZ  LYS A 507    15052  13679  14731   -613   1521    -99       N  
-ATOM    456  N   THR A 508     -10.741  -3.933 -11.234  1.00 61.79           N  
-ANISOU  456  N   THR A 508     8775   7028   7676   -283   1046    -31       N  
-ATOM    457  CA  THR A 508      -9.559  -4.732 -10.924  1.00 60.10           C  
-ANISOU  457  CA  THR A 508     8682   6805   7349   -223    958    -38       C  
-ATOM    458  C   THR A 508      -8.683  -4.088  -9.848  1.00 58.68           C  
-ANISOU  458  C   THR A 508     8577   6588   7131   -189    920    -59       C  
-ATOM    459  O   THR A 508      -7.902  -3.181 -10.129  1.00 65.15           O  
-ANISOU  459  O   THR A 508     9296   7457   8000   -149    859    -46       O  
-ATOM    460  CB  THR A 508      -8.709  -5.023 -12.184  1.00 44.57           C  
-ANISOU  460  CB  THR A 508     6614   4930   5391   -167    859     -9       C  
-ATOM    461  OG1 THR A 508      -8.409  -3.797 -12.861  1.00 38.07           O  
-ANISOU  461  OG1 THR A 508     5620   4177   4668   -154    829     19       O  
-ATOM    462  CG2 THR A 508      -9.458  -5.947 -13.131  1.00 39.40           C  
-ANISOU  462  CG2 THR A 508     5923   4303   4745   -194    887      4       C  
-ATOM    463  N   ARG A 509      -8.826  -4.566  -8.614  1.00 47.77           N  
-ANISOU  463  N   ARG A 509     7373   5117   5658   -208    956    -93       N  
-ATOM    464  CA  ARG A 509      -7.993  -4.110  -7.506  1.00 34.97           C  
-ANISOU  464  CA  ARG A 509     5848   3454   3984   -175    917   -117       C  
-ATOM    465  C   ARG A 509      -7.283  -5.286  -6.846  1.00 39.72           C  
-ANISOU  465  C   ARG A 509     6646   4001   4444   -137    857   -137       C  
-ATOM    466  O   ARG A 509      -7.791  -5.876  -5.890  1.00 38.10           O  
-ANISOU  466  O   ARG A 509     6605   3712   4158   -179    913   -159       O  
-ATOM    467  CB  ARG A 509      -8.826  -3.354  -6.470  1.00 36.32           C  
-ANISOU  467  CB  ARG A 509     6054   3564   4180   -237   1020   -143       C  
-ATOM    468  CG  ARG A 509      -9.217  -1.950  -6.889  1.00 32.24           C  
-ANISOU  468  CG  ARG A 509     5352   3094   3805   -255   1053   -131       C  
-ATOM    469  CD  ARG A 509      -9.997  -1.244  -5.794  1.00 33.83           C  
-ANISOU  469  CD  ARG A 509     5593   3232   4029   -315   1151   -167       C  
-ATOM    470  NE  ARG A 509     -10.228   0.164  -6.107  1.00 34.95           N  
-ANISOU  470  NE  ARG A 509     5563   3410   4306   -322   1166   -160       N  
-ATOM    471  CZ  ARG A 509      -9.400   1.151  -5.775  1.00 39.21           C  
-ANISOU  471  CZ  ARG A 509     6061   3962   4875   -281   1114   -161       C  
-ATOM    472  NH1 ARG A 509      -8.279   0.889  -5.115  1.00 40.89           N  
-ANISOU  472  NH1 ARG A 509     6389   4157   4991   -228   1042   -174       N  
-ATOM    473  NH2 ARG A 509      -9.693   2.403  -6.103  1.00 31.35           N  
-ANISOU  473  NH2 ARG A 509     4909   2994   4006   -292   1130   -152       N  
-ATOM    474  N   HIS A 510      -6.103  -5.615  -7.362  1.00 45.32           N  
-ANISOU  474  N   HIS A 510     7338   4756   5126    -60    739   -132       N  
-ATOM    475  CA  HIS A 510      -5.337  -6.758  -6.884  1.00 41.83           C  
-ANISOU  475  CA  HIS A 510     7067   4266   4559    -12    660   -153       C  
-ATOM    476  C   HIS A 510      -3.845  -6.516  -7.110  1.00 51.88           C  
-ANISOU  476  C   HIS A 510     8299   5589   5825     80    529   -165       C  
-ATOM    477  O   HIS A 510      -3.455  -5.847  -8.068  1.00 58.62           O  
-ANISOU  477  O   HIS A 510     8977   6532   6765    103    496   -149       O  
-ATOM    478  CB  HIS A 510      -5.786  -8.022  -7.618  1.00 40.76           C  
-ANISOU  478  CB  HIS A 510     6958   4135   4393    -26    665   -141       C  
-ATOM    479  CG  HIS A 510      -5.335  -9.294  -6.972  1.00 45.06           C  
-ANISOU  479  CG  HIS A 510     7709   4605   4807      3    608   -163       C  
-ATOM    480  ND1 HIS A 510      -4.052  -9.779  -7.100  1.00 55.88           N  
-ANISOU  480  ND1 HIS A 510     9116   5991   6126     90    475   -181       N  
-ATOM    481  CD2 HIS A 510      -6.003 -10.189  -6.207  1.00 47.67           C  
-ANISOU  481  CD2 HIS A 510     8221   4842   5048    -46    663   -172       C  
-ATOM    482  CE1 HIS A 510      -3.946 -10.915  -6.433  1.00 54.84           C  
-ANISOU  482  CE1 HIS A 510     9182   5774   5880     99    444   -197       C  
-ATOM    483  NE2 HIS A 510      -5.115 -11.187  -5.883  1.00 41.73           N  
-ANISOU  483  NE2 HIS A 510     7618   4047   4193     14    558   -189       N  
-ATOM    484  N   VAL A 511      -3.016  -7.066  -6.228  1.00 46.78           N  
-ANISOU  484  N   VAL A 511     7816   4883   5074    129    454   -197       N  
-ATOM    485  CA  VAL A 511      -1.574  -6.832  -6.270  1.00 41.52           C  
-ANISOU  485  CA  VAL A 511     7124   4254   4397    218    329   -223       C  
-ATOM    486  C   VAL A 511      -0.897  -7.555  -7.436  1.00 44.17           C  
-ANISOU  486  C   VAL A 511     7382   4661   4739    271    239   -224       C  
-ATOM    487  O   VAL A 511       0.185  -7.164  -7.880  1.00 45.63           O  
-ANISOU  487  O   VAL A 511     7473   4912   4953    333    150   -243       O  
-ATOM    488  CB  VAL A 511      -0.906  -7.245  -4.945  1.00 39.56           C  
-ANISOU  488  CB  VAL A 511     7082   3914   4033    259    268   -261       C  
-ATOM    489  CG1 VAL A 511      -1.136  -8.724  -4.675  1.00 34.82           C  
-ANISOU  489  CG1 VAL A 511     6663   3241   3325    256    250   -266       C  
-ATOM    490  CG2 VAL A 511       0.580  -6.920  -4.966  1.00 46.86           C  
-ANISOU  490  CG2 VAL A 511     7970   4880   4956    353    139   -297       C  
-ATOM    491  N   ASN A 512      -1.540  -8.606  -7.935  1.00 50.35           N  
-ANISOU  491  N   ASN A 512     8200   5433   5496    244    265   -209       N  
-ATOM    492  CA  ASN A 512      -0.985  -9.389  -9.036  1.00 51.27           C  
-ANISOU  492  CA  ASN A 512     8248   5615   5615    289    185   -215       C  
-ATOM    493  C   ASN A 512      -1.589  -9.020 -10.389  1.00 45.47           C  
-ANISOU  493  C   ASN A 512     7314   4978   4983    249    238   -177       C  
-ATOM    494  O   ASN A 512      -1.179  -9.537 -11.428  1.00 38.42           O  
-ANISOU  494  O   ASN A 512     6338   4156   4105    279    181   -180       O  
-ATOM    495  CB  ASN A 512      -1.149 -10.885  -8.764  1.00 47.33           C  
-ANISOU  495  CB  ASN A 512     7923   5044   5018    296    160   -228       C  
-ATOM    496  CG  ASN A 512      -0.372 -11.340  -7.543  1.00 47.43           C  
-ANISOU  496  CG  ASN A 512     8134   4963   4923    348     79   -267       C  
-ATOM    497  OD1 ASN A 512      -0.907 -12.025  -6.670  1.00 50.90           O  
-ANISOU  497  OD1 ASN A 512     8760   5302   5278    316    114   -266       O  
-ATOM    498  ND2 ASN A 512       0.897 -10.954  -7.472  1.00 42.22           N  
-ANISOU  498  ND2 ASN A 512     7440   4337   4264    427    -29   -303       N  
-ATOM    499  N   ILE A 513      -2.569  -8.123 -10.362  1.00 41.20           N  
-ANISOU  499  N   ILE A 513     6700   4441   4514    182    344   -145       N  
-ATOM    500  CA  ILE A 513      -3.153  -7.584 -11.579  1.00 35.79           C  
-ANISOU  500  CA  ILE A 513     5823   3843   3933    144    391   -107       C  
-ATOM    501  C   ILE A 513      -2.616  -6.177 -11.811  1.00 34.07           C  
-ANISOU  501  C   ILE A 513     5461   3688   3797    158    373    -96       C  
-ATOM    502  O   ILE A 513      -2.737  -5.311 -10.944  1.00 40.19           O  
-ANISOU  502  O   ILE A 513     6263   4421   4589    143    409   -100       O  
-ATOM    503  CB  ILE A 513      -4.689  -7.538 -11.495  1.00 34.12           C  
-ANISOU  503  CB  ILE A 513     5615   3594   3758     59    519    -81       C  
-ATOM    504  CG1 ILE A 513      -5.252  -8.938 -11.257  1.00 32.21           C  
-ANISOU  504  CG1 ILE A 513     5518   3286   3432     39    544    -92       C  
-ATOM    505  CG2 ILE A 513      -5.276  -6.946 -12.764  1.00 40.91           C  
-ANISOU  505  CG2 ILE A 513     6276   4542   4727     25    557    -42       C  
-ATOM    506  CD1 ILE A 513      -4.938  -9.910 -12.367  1.00 27.21           C  
-ANISOU  506  CD1 ILE A 513     4837   2712   2789     70    484    -89       C  
-ATOM    507  N   LEU A 514      -2.011  -5.958 -12.975  1.00 49.76           N  
-ANISOU  507  N   LEU A 514     7298   5777   5833    183    316    -85       N  
-ATOM    508  CA  LEU A 514      -1.473  -4.648 -13.329  1.00 46.86           C  
-ANISOU  508  CA  LEU A 514     6787   5474   5545    190    296    -72       C  
-ATOM    509  C   LEU A 514      -2.427  -3.542 -12.886  1.00 49.02           C  
-ANISOU  509  C   LEU A 514     7022   5713   5890    132    391    -44       C  
-ATOM    510  O   LEU A 514      -3.631  -3.623 -13.128  1.00 55.05           O  
-ANISOU  510  O   LEU A 514     7765   6462   6691     74    475    -17       O  
-ATOM    511  CB  LEU A 514      -1.239  -4.561 -14.837  1.00 44.15           C  
-ANISOU  511  CB  LEU A 514     6272   5244   5257    189    265    -47       C  
-ATOM    512  CG  LEU A 514      -0.621  -3.265 -15.360  1.00 42.69           C  
-ANISOU  512  CG  LEU A 514     5936   5135   5150    191    238    -31       C  
-ATOM    513  CD1 LEU A 514       0.834  -3.161 -14.929  1.00 43.31           C  
-ANISOU  513  CD1 LEU A 514     6044   5225   5186    259    144    -82       C  
-ATOM    514  CD2 LEU A 514      -0.741  -3.188 -16.873  1.00 35.26           C  
-ANISOU  514  CD2 LEU A 514     4835   4297   4265    167    232      6       C  
-ATOM    515  N   LEU A 515      -1.889  -2.512 -12.239  1.00 32.24           N  
-ANISOU  515  N   LEU A 515     4885   3576   3790    148    377    -55       N  
-ATOM    516  CA  LEU A 515      -2.718  -1.443 -11.690  1.00 30.60           C  
-ANISOU  516  CA  LEU A 515     4649   3328   3649     99    460    -38       C  
-ATOM    517  C   LEU A 515      -3.226  -0.471 -12.754  1.00 36.90           C  
-ANISOU  517  C   LEU A 515     5260   4194   4565     59    491     10       C  
-ATOM    518  O   LEU A 515      -2.456   0.305 -13.318  1.00 30.10           O  
-ANISOU  518  O   LEU A 515     4286   3399   3752     80    439     22       O  
-ATOM    519  CB  LEU A 515      -1.960  -0.673 -10.603  1.00 40.33           C  
-ANISOU  519  CB  LEU A 515     5934   4522   4867    131    432    -71       C  
-ATOM    520  CG  LEU A 515      -2.721   0.507  -9.988  1.00 44.17           C  
-ANISOU  520  CG  LEU A 515     6385   4968   5428     84    513    -61       C  
-ATOM    521  CD1 LEU A 515      -3.992   0.027  -9.300  1.00 36.59           C  
-ANISOU  521  CD1 LEU A 515     5530   3929   4444     27    611    -67       C  
-ATOM    522  CD2 LEU A 515      -1.844   1.290  -9.021  1.00 36.86           C  
-ANISOU  522  CD2 LEU A 515     5497   4015   4491    121    475    -94       C  
-ATOM    523  N   PHE A 516      -4.528  -0.523 -13.020  1.00 35.64           N  
-ANISOU  523  N   PHE A 516     5072   4018   4453      1    575     35       N  
-ATOM    524  CA  PHE A 516      -5.177   0.453 -13.884  1.00 28.07           C  
-ANISOU  524  CA  PHE A 516     3950   3105   3610    -40    609     79       C  
-ATOM    525  C   PHE A 516      -5.291   1.775 -13.139  1.00 42.21           C  
-ANISOU  525  C   PHE A 516     5712   4858   5468    -54    639     76       C  
-ATOM    526  O   PHE A 516      -5.853   1.827 -12.046  1.00 59.59           O  
-ANISOU  526  O   PHE A 516     8007   6981   7654    -76    700     47       O  
-ATOM    527  CB  PHE A 516      -6.562  -0.043 -14.296  1.00 37.86           C  
-ANISOU  527  CB  PHE A 516     5176   4330   4880    -94    687     96       C  
-ATOM    528  CG  PHE A 516      -7.486   1.048 -14.758  1.00 44.58           C  
-ANISOU  528  CG  PHE A 516     5893   5192   5853   -141    738    129       C  
-ATOM    529  CD1 PHE A 516      -7.362   1.592 -16.026  1.00 43.05           C  
-ANISOU  529  CD1 PHE A 516     5546   5080   5731   -145    699    176       C  
-ATOM    530  CD2 PHE A 516      -8.491   1.518 -13.927  1.00 46.83           C  
-ANISOU  530  CD2 PHE A 516     6206   5404   6182   -184    823    109       C  
-ATOM    531  CE1 PHE A 516      -8.217   2.591 -16.452  1.00 43.82           C  
-ANISOU  531  CE1 PHE A 516     5526   5180   5942   -185    736    207       C  
-ATOM    532  CE2 PHE A 516      -9.349   2.516 -14.346  1.00 43.27           C  
-ANISOU  532  CE2 PHE A 516     5630   4959   5851   -223    863    132       C  
-ATOM    533  CZ  PHE A 516      -9.213   3.054 -15.611  1.00 37.89           C  
-ANISOU  533  CZ  PHE A 516     4801   4354   5242   -221    815    183       C  
-ATOM    534  N   MET A 517      -4.758   2.843 -13.726  1.00 29.33           N  
-ANISOU  534  N   MET A 517     3951   3283   3910    -46    598    103       N  
-ATOM    535  CA  MET A 517      -4.708   4.133 -13.042  1.00 21.17           C  
-ANISOU  535  CA  MET A 517     2885   2216   2942    -53    614     98       C  
-ATOM    536  C   MET A 517      -5.648   5.189 -13.621  1.00 23.54           C  
-ANISOU  536  C   MET A 517     3048   2525   3370   -101    658    138       C  
-ATOM    537  O   MET A 517      -6.176   6.023 -12.885  1.00 36.57           O  
-ANISOU  537  O   MET A 517     4695   4121   5079   -124    707    124       O  
-ATOM    538  CB  MET A 517      -3.272   4.666 -12.998  1.00 23.85           C  
-ANISOU  538  CB  MET A 517     3199   2595   3267     -3    531     87       C  
-ATOM    539  CG  MET A 517      -2.344   3.867 -12.095  1.00 23.13           C  
-ANISOU  539  CG  MET A 517     3254   2474   3062     51    486     34       C  
-ATOM    540  SD  MET A 517      -0.730   4.640 -11.870  1.00 39.06           S  
-ANISOU  540  SD  MET A 517     5237   4528   5075    108    396      7       S  
-ATOM    541  CE  MET A 517      -1.202   6.212 -11.154  1.00 24.48           C  
-ANISOU  541  CE  MET A 517     3337   2633   3329     76    450     13       C  
-ATOM    542  N   GLY A 518      -5.851   5.159 -14.934  1.00 35.49           N  
-ANISOU  542  N   GLY A 518     4451   4107   4927   -117    637    185       N  
-ATOM    543  CA  GLY A 518      -6.711   6.133 -15.581  1.00 33.55           C  
-ANISOU  543  CA  GLY A 518     4075   3870   4802   -159    665    227       C  
-ATOM    544  C   GLY A 518      -6.836   5.905 -17.072  1.00 35.70           C  
-ANISOU  544  C   GLY A 518     4243   4223   5099   -172    632    279       C  
-ATOM    545  O   GLY A 518      -6.265   4.960 -17.616  1.00 40.48           O  
-ANISOU  545  O   GLY A 518     4871   4880   5628   -150    592    279       O  
-ATOM    546  N   TYR A 519      -7.591   6.772 -17.737  1.00 29.92           N  
-ANISOU  546  N   TYR A 519     3395   3500   4475   -208    645    320       N  
-ATOM    547  CA  TYR A 519      -7.767   6.675 -19.179  1.00 32.48           C  
-ANISOU  547  CA  TYR A 519     3614   3898   4827   -225    612    374       C  
-ATOM    548  C   TYR A 519      -7.835   8.058 -19.810  1.00 40.99           C  
-ANISOU  548  C   TYR A 519     4566   4995   6014   -247    583    426       C  
-ATOM    549  O   TYR A 519      -8.267   9.021 -19.179  1.00 37.24           O  
-ANISOU  549  O   TYR A 519     4072   4460   5617   -259    610    419       O  
-ATOM    550  CB  TYR A 519      -9.026   5.875 -19.526  1.00 43.27           C  
-ANISOU  550  CB  TYR A 519     4987   5251   6204   -254    667    372       C  
-ATOM    551  CG  TYR A 519     -10.325   6.608 -19.271  1.00 41.48           C  
-ANISOU  551  CG  TYR A 519     4713   4963   6086   -291    727    370       C  
-ATOM    552  CD1 TYR A 519     -10.891   7.418 -20.247  1.00 34.61           C  
-ANISOU  552  CD1 TYR A 519     3714   4117   5317   -317    707    420       C  
-ATOM    553  CD2 TYR A 519     -10.992   6.477 -18.060  1.00 50.51           C  
-ANISOU  553  CD2 TYR A 519     5941   6022   7228   -302    801    314       C  
-ATOM    554  CE1 TYR A 519     -12.080   8.085 -20.021  1.00 45.28           C  
-ANISOU  554  CE1 TYR A 519     5018   5411   6776   -346    754    410       C  
-ATOM    555  CE2 TYR A 519     -12.182   7.139 -17.825  1.00 56.63           C  
-ANISOU  555  CE2 TYR A 519     6666   6744   8108   -337    857    300       C  
-ATOM    556  CZ  TYR A 519     -12.722   7.941 -18.808  1.00 57.41           C  
-ANISOU  556  CZ  TYR A 519     6631   6867   8314   -356    830    346       C  
-ATOM    557  OH  TYR A 519     -13.906   8.600 -18.574  1.00 60.01           O  
-ANISOU  557  OH  TYR A 519     6907   7140   8754   -387    879    325       O  
-ATOM    558  N   SER A 520      -7.406   8.145 -21.062  1.00 56.94           N  
-ANISOU  558  N   SER A 520     6501   7098   8037   -255    527    477       N  
-ATOM    559  CA  SER A 520      -7.408   9.407 -21.779  1.00 53.82           C  
-ANISOU  559  CA  SER A 520     5990   6724   7734   -280    491    535       C  
-ATOM    560  C   SER A 520      -8.347   9.384 -22.969  1.00 52.99           C  
-ANISOU  560  C   SER A 520     5799   6650   7683   -315    487    586       C  
-ATOM    561  O   SER A 520      -8.518   8.359 -23.622  1.00 44.37           O  
-ANISOU  561  O   SER A 520     4715   5605   6536   -316    488    589       O  
-ATOM    562  CB  SER A 520      -5.998   9.754 -22.245  1.00 59.23           C  
-ANISOU  562  CB  SER A 520     6645   7481   8381   -268    422    555       C  
-ATOM    563  OG  SER A 520      -5.246  10.303 -21.183  1.00 64.29           O  
-ANISOU  563  OG  SER A 520     7331   8081   9015   -242    419    518       O  
-ATOM    564  N   THR A 521      -8.952  10.532 -23.244  1.00 72.79           N  
-ANISOU  564  N   THR A 521     8226   9130  10302   -341    480    624       N  
-ATOM    565  CA  THR A 521      -9.800  10.696 -24.412  1.00 76.31           C  
-ANISOU  565  CA  THR A 521     8582   9602  10809   -372    462    678       C  
-ATOM    566  C   THR A 521      -9.145  11.695 -25.353  1.00 81.92           C  
-ANISOU  566  C   THR A 521     9207  10364  11554   -392    391    748       C  
-ATOM    567  O   THR A 521      -9.364  11.665 -26.561  1.00 89.12           O  
-ANISOU  567  O   THR A 521    10054  11332  12474   -417    355    802       O  
-ATOM    568  CB  THR A 521     -11.198  11.194 -24.026  1.00 72.80           C  
-ANISOU  568  CB  THR A 521     8111   9075  10475   -389    508    663       C  
-ATOM    569  OG1 THR A 521     -12.123  10.100 -24.060  1.00 68.41           O  
-ANISOU  569  OG1 THR A 521     7587   8512   9895   -393    559    630       O  
-ATOM    570  CG2 THR A 521     -11.664  12.267 -24.991  1.00 72.05           C  
-ANISOU  570  CG2 THR A 521     7905   8985  10485   -416    457    730       C  
-ATOM    571  N   ALA A 522      -8.338  12.583 -24.784  1.00 67.22           N  
-ANISOU  571  N   ALA A 522     7349   8482   9709   -384    371    746       N  
-ATOM    572  CA  ALA A 522      -7.611  13.571 -25.564  1.00 59.61           C  
-ANISOU  572  CA  ALA A 522     6314   7563   8773   -408    307    808       C  
-ATOM    573  C   ALA A 522      -6.194  13.671 -25.027  1.00 64.45           C  
-ANISOU  573  C   ALA A 522     6965   8202   9319   -386    289    780       C  
-ATOM    574  O   ALA A 522      -5.989  13.606 -23.820  1.00 65.36           O  
-ANISOU  574  O   ALA A 522     7148   8264   9422   -355    322    721       O  
-ATOM    575  CB  ALA A 522      -8.297  14.909 -25.475  1.00 43.28           C  
-ANISOU  575  CB  ALA A 522     4186   5425   6835   -428    296    841       C  
-ATOM    576  N   PRO A 523      -5.204  13.831 -25.917  1.00 76.95           N  
-ANISOU  576  N   PRO A 523     8508   9870  10861   -404    237    818       N  
-ATOM    577  CA  PRO A 523      -5.321  13.918 -27.377  1.00 83.87           C  
-ANISOU  577  CA  PRO A 523     9311  10818  11739   -447    195    889       C  
-ATOM    578  C   PRO A 523      -5.997  12.702 -28.001  1.00 92.50           C  
-ANISOU  578  C   PRO A 523    10412  11950  12785   -447    212    886       C  
-ATOM    579  O   PRO A 523      -7.031  12.852 -28.644  1.00102.22           O  
-ANISOU  579  O   PRO A 523    11598  13168  14074   -470    209    928       O  
-ATOM    580  CB  PRO A 523      -3.862  14.001 -27.845  1.00 49.22           C  
-ANISOU  580  CB  PRO A 523     4906   6515   7279   -458    153    894       C  
-ATOM    581  CG  PRO A 523      -3.040  13.641 -26.671  1.00 43.87           C  
-ANISOU  581  CG  PRO A 523     4302   5818   6550   -411    172    816       C  
-ATOM    582  CD  PRO A 523      -3.817  14.021 -25.473  1.00 42.32           C  
-ANISOU  582  CD  PRO A 523     4147   5513   6421   -386    215    786       C  
-ATOM    583  N   GLN A 524      -5.422  11.519 -27.824  1.00 64.98           N  
-ANISOU  583  N   GLN A 524     6983   8510   9198   -418    225    835       N  
-ATOM    584  CA  GLN A 524      -6.025  10.305 -28.361  1.00 60.54           C  
-ANISOU  584  CA  GLN A 524     6432   7982   8587   -416    243    826       C  
-ATOM    585  C   GLN A 524      -6.420   9.357 -27.241  1.00 60.76           C  
-ANISOU  585  C   GLN A 524     6555   7950   8582   -375    299    754       C  
-ATOM    586  O   GLN A 524      -6.079   9.580 -26.083  1.00 64.25           O  
-ANISOU  586  O   GLN A 524     7056   8334   9022   -347    320    710       O  
-ATOM    587  CB  GLN A 524      -5.055   9.607 -29.307  1.00 64.67           C  
-ANISOU  587  CB  GLN A 524     6936   8619   9016   -424    205    830       C  
-ATOM    588  CG  GLN A 524      -3.629   9.645 -28.819  1.00 64.61           C  
-ANISOU  588  CG  GLN A 524     6959   8642   8948   -401    184    787       C  
-ATOM    589  CD  GLN A 524      -2.712   8.796 -29.660  1.00 69.12           C  
-ANISOU  589  CD  GLN A 524     7514   9323   9425   -405    152    770       C  
-ATOM    590  OE1 GLN A 524      -3.151   7.850 -30.314  1.00 65.04           O  
-ANISOU  590  OE1 GLN A 524     6992   8848   8870   -408    157    771       O  
-ATOM    591  NE2 GLN A 524      -1.426   9.125 -29.648  1.00 75.35           N  
-ANISOU  591  NE2 GLN A 524     8292  10161  10178   -404    119    749       N  
-ATOM    592  N   LEU A 525      -7.139   8.296 -27.592  1.00 60.62           N  
-ANISOU  592  N   LEU A 525     6553   7947   8535   -373    325    742       N  
-ATOM    593  CA  LEU A 525      -7.558   7.310 -26.605  1.00 47.60           C  
-ANISOU  593  CA  LEU A 525     4999   6240   6845   -342    380    677       C  
-ATOM    594  C   LEU A 525      -6.350   6.586 -26.025  1.00 37.87           C  
-ANISOU  594  C   LEU A 525     3846   5031   5511   -303    366    624       C  
-ATOM    595  O   LEU A 525      -5.459   6.159 -26.759  1.00 33.21           O  
-ANISOU  595  O   LEU A 525     3233   4527   4858   -300    322    627       O  
-ATOM    596  CB  LEU A 525      -8.528   6.301 -27.221  1.00 42.71           C  
-ANISOU  596  CB  LEU A 525     4375   5638   6214   -353    407    677       C  
-ATOM    597  CG  LEU A 525      -9.853   6.850 -27.744  1.00 42.28           C  
-ANISOU  597  CG  LEU A 525     4250   5555   6261   -386    423    716       C  
-ATOM    598  CD1 LEU A 525     -10.821   5.710 -28.005  1.00 32.84           C  
-ANISOU  598  CD1 LEU A 525     3073   4359   5047   -388    464    693       C  
-ATOM    599  CD2 LEU A 525     -10.443   7.830 -26.749  1.00 51.88           C  
-ANISOU  599  CD2 LEU A 525     5474   6672   7568   -387    456    702       C  
-ATOM    600  N   ALA A 526      -6.320   6.448 -24.705  1.00 37.01           N  
-ANISOU  600  N   ALA A 526     3829   4845   5386   -273    401    570       N  
-ATOM    601  CA  ALA A 526      -5.210   5.771 -24.050  1.00 36.68           C  
-ANISOU  601  CA  ALA A 526     3873   4814   5251   -230    382    515       C  
-ATOM    602  C   ALA A 526      -5.620   5.156 -22.721  1.00 43.61           C  
-ANISOU  602  C   ALA A 526     4872   5601   6096   -205    434    457       C  
-ATOM    603  O   ALA A 526      -6.535   5.636 -22.052  1.00 35.94           O  
-ANISOU  603  O   ALA A 526     3917   4553   5186   -221    487    454       O  
-ATOM    604  CB  ALA A 526      -4.037   6.723 -23.858  1.00 24.96           C  
-ANISOU  604  CB  ALA A 526     2360   3350   3773   -220    336    516       C  
-ATOM    605  N   ILE A 527      -4.932   4.081 -22.356  1.00 49.96           N  
-ANISOU  605  N   ILE A 527     5764   6415   6802   -167    418    409       N  
-ATOM    606  CA  ILE A 527      -5.101   3.453 -21.058  1.00 38.77           C  
-ANISOU  606  CA  ILE A 527     4482   4915   5335   -141    457    353       C  
-ATOM    607  C   ILE A 527      -3.866   3.743 -20.215  1.00 39.85           C  
-ANISOU  607  C   ILE A 527     4674   5038   5427    -99    415    314       C  
-ATOM    608  O   ILE A 527      -2.745   3.450 -20.629  1.00 37.11           O  
-ANISOU  608  O   ILE A 527     4314   4757   5030    -71    352    300       O  
-ATOM    609  CB  ILE A 527      -5.281   1.930 -21.190  1.00 44.66           C  
-ANISOU  609  CB  ILE A 527     5303   5667   5998   -127    464    325       C  
-ATOM    610  CG1 ILE A 527      -6.530   1.609 -22.012  1.00 48.67           C  
-ANISOU  610  CG1 ILE A 527     5755   6187   6550   -168    507    358       C  
-ATOM    611  CG2 ILE A 527      -5.363   1.279 -19.819  1.00 44.80           C  
-ANISOU  611  CG2 ILE A 527     5474   5595   5953   -103    498    270       C  
-ATOM    612  CD1 ILE A 527      -7.807   2.168 -21.421  1.00 56.79           C  
-ANISOU  612  CD1 ILE A 527     6787   7135   7654   -203    583    362       C  
-ATOM    613  N   VAL A 528      -4.074   4.330 -19.041  1.00 44.22           N  
-ANISOU  613  N   VAL A 528     5285   5510   6004    -95    450    292       N  
-ATOM    614  CA  VAL A 528      -2.974   4.652 -18.139  1.00 41.34           C  
-ANISOU  614  CA  VAL A 528     4979   5126   5602    -54    413    251       C  
-ATOM    615  C   VAL A 528      -2.897   3.642 -16.998  1.00 44.19           C  
-ANISOU  615  C   VAL A 528     5499   5420   5871    -21    428    193       C  
-ATOM    616  O   VAL A 528      -3.896   3.370 -16.333  1.00 44.29           O  
-ANISOU  616  O   VAL A 528     5583   5361   5885    -42    495    183       O  
-ATOM    617  CB  VAL A 528      -3.123   6.066 -17.555  1.00 29.26           C  
-ANISOU  617  CB  VAL A 528     3408   3553   4157    -70    434    263       C  
-ATOM    618  CG1 VAL A 528      -1.915   6.418 -16.703  1.00 26.53           C  
-ANISOU  618  CG1 VAL A 528     3112   3194   3774    -26    391    219       C  
-ATOM    619  CG2 VAL A 528      -3.298   7.077 -18.670  1.00 34.33           C  
-ANISOU  619  CG2 VAL A 528     3902   4249   4892   -108    419    325       C  
-ATOM    620  N   THR A 529      -1.712   3.082 -16.779  1.00 35.18           N  
-ANISOU  620  N   THR A 529     4416   4302   4651     30    363    152       N  
-ATOM    621  CA  THR A 529      -1.504   2.127 -15.698  1.00 34.91           C  
-ANISOU  621  CA  THR A 529     4541   4201   4522     68    361     98       C  
-ATOM    622  C   THR A 529      -0.229   2.452 -14.937  1.00 35.06           C  
-ANISOU  622  C   THR A 529     4605   4212   4502    121    299     52       C  
-ATOM    623  O   THR A 529       0.398   3.483 -15.171  1.00 34.43           O  
-ANISOU  623  O   THR A 529     4434   4173   4477    123    270     61       O  
-ATOM    624  CB  THR A 529      -1.401   0.682 -16.224  1.00 31.83           C  
-ANISOU  624  CB  THR A 529     4200   3839   4054     87    333     84       C  
-ATOM    625  OG1 THR A 529      -0.142   0.500 -16.884  1.00 35.96           O  
-ANISOU  625  OG1 THR A 529     4671   4443   4549    127    246     64       O  
-ATOM    626  CG2 THR A 529      -2.532   0.380 -17.191  1.00 31.03           C  
-ANISOU  626  CG2 THR A 529     4030   3765   3995     37    383    129       C  
-ATOM    627  N   GLN A 530       0.150   1.564 -14.027  1.00 38.07           N  
-ANISOU  627  N   GLN A 530     5134   4540   4791    162    276      1       N  
-ATOM    628  CA  GLN A 530       1.396   1.713 -13.292  1.00 34.77           C  
-ANISOU  628  CA  GLN A 530     4771   4112   4328    221    207    -51       C  
-ATOM    629  C   GLN A 530       2.570   1.392 -14.205  1.00 32.47           C  
-ANISOU  629  C   GLN A 530     4407   3913   4017    260    119    -72       C  
-ATOM    630  O   GLN A 530       2.397   0.790 -15.265  1.00 40.47           O  
-ANISOU  630  O   GLN A 530     5361   4986   5029    246    111    -51       O  
-ATOM    631  CB  GLN A 530       1.419   0.773 -12.090  1.00 36.31           C  
-ANISOU  631  CB  GLN A 530     5154   4218   4423    254    201    -98       C  
-ATOM    632  CG  GLN A 530       1.367  -0.697 -12.469  1.00 41.92           C  
-ANISOU  632  CG  GLN A 530     5937   4932   5058    272    174   -110       C  
-ATOM    633  CD  GLN A 530       1.586  -1.618 -11.286  1.00 40.98           C  
-ANISOU  633  CD  GLN A 530     6013   4725   4834    310    149   -157       C  
-ATOM    634  OE1 GLN A 530       0.711  -2.405 -10.929  1.00 45.52           O  
-ANISOU  634  OE1 GLN A 530     6694   5238   5364    283    200   -149       O  
-ATOM    635  NE2 GLN A 530       2.757  -1.522 -10.670  1.00 44.60           N  
-ANISOU  635  NE2 GLN A 530     6521   5174   5250    373     69   -208       N  
-ATOM    636  N   TRP A 531       3.767   1.791 -13.790  1.00 33.91           N  
-ANISOU  636  N   TRP A 531     4591   4108   4185    308     53   -119       N  
-ATOM    637  CA  TRP A 531       4.976   1.447 -14.526  1.00 20.67           C  
-ANISOU  637  CA  TRP A 531     2854   2516   2485    348    -33   -157       C  
-ATOM    638  C   TRP A 531       5.691   0.266 -13.876  1.00 35.11           C  
-ANISOU  638  C   TRP A 531     4818   4307   4214    418   -104   -227       C  
-ATOM    639  O   TRP A 531       6.065   0.323 -12.705  1.00 39.27           O  
-ANISOU  639  O   TRP A 531     5454   4764   4701    457   -126   -269       O  
-ATOM    640  CB  TRP A 531       5.917   2.646 -14.618  1.00 31.26           C  
-ANISOU  640  CB  TRP A 531     4091   3905   3880    355    -65   -172       C  
-ATOM    641  CG  TRP A 531       7.171   2.327 -15.357  1.00 45.66           C  
-ANISOU  641  CG  TRP A 531     5848   5819   5682    391   -148   -221       C  
-ATOM    642  CD1 TRP A 531       8.436   2.273 -14.847  1.00 55.21           C  
-ANISOU  642  CD1 TRP A 531     7086   7034   6856    454   -226   -300       C  
-ATOM    643  CD2 TRP A 531       7.281   1.988 -16.742  1.00 47.52           C  
-ANISOU  643  CD2 TRP A 531     5973   6153   5930    365   -162   -203       C  
-ATOM    644  NE1 TRP A 531       9.328   1.933 -15.834  1.00 58.12           N  
-ANISOU  644  NE1 TRP A 531     7365   7501   7218    467   -285   -336       N  
-ATOM    645  CE2 TRP A 531       8.643   1.752 -17.007  1.00 55.62           C  
-ANISOU  645  CE2 TRP A 531     6963   7244   6928    411   -246   -276       C  
-ATOM    646  CE3 TRP A 531       6.359   1.867 -17.786  1.00 50.77           C  
-ANISOU  646  CE3 TRP A 531     6311   6606   6373    306   -113   -135       C  
-ATOM    647  CZ2 TRP A 531       9.107   1.402 -18.274  1.00 66.32           C  
-ANISOU  647  CZ2 TRP A 531     8210   8705   8283    396   -276   -286       C  
-ATOM    648  CZ3 TRP A 531       6.820   1.520 -19.040  1.00 62.50           C  
-ANISOU  648  CZ3 TRP A 531     7695   8196   7856    293   -146   -139       C  
-ATOM    649  CH2 TRP A 531       8.181   1.291 -19.275  1.00 68.08           C  
-ANISOU  649  CH2 TRP A 531     8368   8968   8533    336   -225   -214       C  
-ATOM    650  N   CYS A 532       5.878  -0.804 -14.644  1.00 58.01           N  
-ANISOU  650  N   CYS A 532     7712   7253   7075    433   -143   -242       N  
-ATOM    651  CA  CYS A 532       6.542  -2.005 -14.145  1.00 53.71           C  
-ANISOU  651  CA  CYS A 532     7293   6673   6440    501   -220   -309       C  
-ATOM    652  C   CYS A 532       8.019  -2.029 -14.517  1.00 55.19           C  
-ANISOU  652  C   CYS A 532     7416   6934   6620    558   -320   -381       C  
-ATOM    653  O   CYS A 532       8.371  -2.128 -15.693  1.00 66.28           O  
-ANISOU  653  O   CYS A 532     8697   8437   8050    545   -341   -383       O  
-ATOM    654  CB  CYS A 532       5.862  -3.263 -14.687  1.00 44.95           C  
-ANISOU  654  CB  CYS A 532     6227   5561   5291    489   -207   -293       C  
-ATOM    655  SG  CYS A 532       4.158  -3.491 -14.142  1.00 51.16           S  
-ANISOU  655  SG  CYS A 532     7114   6253   6073    427    -93   -228       S  
-ATOM    656  N   GLU A 533       8.877  -1.942 -13.506  1.00 40.92           N  
-ANISOU  656  N   GLU A 533     5693   5080   4776    619   -382   -444       N  
-ATOM    657  CA  GLU A 533      10.317  -2.025 -13.710  1.00 49.52           C  
-ANISOU  657  CA  GLU A 533     6733   6228   5856    681   -483   -528       C  
-ATOM    658  C   GLU A 533      10.698  -3.463 -14.042  1.00 60.99           C  
-ANISOU  658  C   GLU A 533     8241   7689   7244    730   -558   -580       C  
-ATOM    659  O   GLU A 533       9.938  -4.392 -13.768  1.00 60.94           O  
-ANISOU  659  O   GLU A 533     8351   7616   7188    728   -539   -557       O  
-ATOM    660  CB  GLU A 533      11.058  -1.558 -12.458  1.00 70.56           C  
-ANISOU  660  CB  GLU A 533     9482   8830   8499    736   -530   -584       C  
-ATOM    661  CG  GLU A 533      10.437  -0.334 -11.801  1.00 91.12           C  
-ANISOU  661  CG  GLU A 533    12082  11390  11150    691   -449   -531       C  
-ATOM    662  CD  GLU A 533      11.325   0.892 -11.876  1.00111.58           C  
-ANISOU  662  CD  GLU A 533    14555  14036  13804    695   -468   -559       C  
-ATOM    663  OE1 GLU A 533      10.852   1.940 -12.364  1.00117.27           O  
-ANISOU  663  OE1 GLU A 533    15163  14794  14601    631   -399   -499       O  
-ATOM    664  OE2 GLU A 533      12.495   0.810 -11.443  1.00122.10           O  
-ANISOU  664  OE2 GLU A 533    15909  15373  15110    763   -555   -644       O  
-ATOM    665  N   GLY A 534      11.873  -3.647 -14.634  1.00 74.02           N  
-ANISOU  665  N   GLY A 534     9807   9419   8898    772   -641   -655       N  
-ATOM    666  CA  GLY A 534      12.311  -4.968 -15.040  1.00 75.72           C  
-ANISOU  666  CA  GLY A 534    10055   9651   9064    820   -719   -714       C  
-ATOM    667  C   GLY A 534      11.809  -5.325 -16.425  1.00 73.73           C  
-ANISOU  667  C   GLY A 534     9686   9488   8839    765   -679   -673       C  
-ATOM    668  O   GLY A 534      11.926  -4.532 -17.359  1.00 64.82           O  
-ANISOU  668  O   GLY A 534     8401   8458   7771    715   -644   -649       O  
-ATOM    669  N   SER A 535      11.240  -6.517 -16.560  1.00 84.78           N  
-ANISOU  669  N   SER A 535    11167  10852  10193    772   -683   -664       N  
-ATOM    670  CA  SER A 535      10.781  -6.991 -17.859  1.00 86.17           C  
-ANISOU  670  CA  SER A 535    11241  11111  10389    727   -653   -633       C  
-ATOM    671  C   SER A 535       9.642  -7.996 -17.727  1.00 96.50           C  
-ANISOU  671  C   SER A 535    12662  12347  11657    710   -611   -586       C  
-ATOM    672  O   SER A 535       9.206  -8.313 -16.622  1.00106.63           O  
-ANISOU  672  O   SER A 535    14105  13514  12894    729   -603   -575       O  
-ATOM    673  CB  SER A 535      11.945  -7.617 -18.627  1.00 67.85           C  
-ANISOU  673  CB  SER A 535     8839   8880   8061    773   -748   -728       C  
-ATOM    674  OG  SER A 535      12.648  -8.533 -17.807  1.00 68.92           O  
-ANISOU  674  OG  SER A 535     9105   8945   8138    862   -850   -813       O  
-ATOM    675  N   SER A 536       9.164  -8.490 -18.865  1.00 87.00           N  
-ANISOU  675  N   SER A 536    11374  11212  10469    671   -583   -559       N  
-ATOM    676  CA  SER A 536       8.092  -9.480 -18.884  1.00 71.99           C  
-ANISOU  676  CA  SER A 536     9563   9254   8535    651   -542   -518       C  
-ATOM    677  C   SER A 536       8.611 -10.846 -18.454  1.00 64.70           C  
-ANISOU  677  C   SER A 536     8767   8273   7542    726   -636   -592       C  
-ATOM    678  O   SER A 536       9.819 -11.080 -18.432  1.00 68.05           O  
-ANISOU  678  O   SER A 536     9176   8727   7953    791   -737   -679       O  
-ATOM    679  CB  SER A 536       7.475  -9.572 -20.282  1.00 60.08           C  
-ANISOU  679  CB  SER A 536     7917   7844   7068    589   -489   -472       C  
-ATOM    680  OG  SER A 536       8.456  -9.875 -21.258  1.00 54.57           O  
-ANISOU  680  OG  SER A 536     7102   7256   6377    612   -559   -536       O  
-ATOM    681  N   LEU A 537       7.694 -11.744 -18.107  1.00 55.21           N  
-ANISOU  681  N   LEU A 537     7691   6987   6298    715   -604   -560       N  
-ATOM    682  CA  LEU A 537       8.063 -13.110 -17.752  1.00 58.30           C  
-ANISOU  682  CA  LEU A 537     8212   7315   6623    779   -692   -621       C  
-ATOM    683  C   LEU A 537       8.652 -13.822 -18.964  1.00 53.70           C  
-ANISOU  683  C   LEU A 537     7512   6836   6055    801   -754   -676       C  
-ATOM    684  O   LEU A 537       9.430 -14.767 -18.828  1.00 51.79           O  
-ANISOU  684  O   LEU A 537     7330   6574   5776    872   -859   -756       O  
-ATOM    685  CB  LEU A 537       6.851 -13.881 -17.226  1.00 59.30           C  
-ANISOU  685  CB  LEU A 537     8491   7336   6706    748   -630   -567       C  
-ATOM    686  CG  LEU A 537       7.109 -15.340 -16.841  1.00 48.23           C  
-ANISOU  686  CG  LEU A 537     7239   5854   5232    807   -716   -619       C  
-ATOM    687  CD1 LEU A 537       8.236 -15.421 -15.829  1.00 55.84           C  
-ANISOU  687  CD1 LEU A 537     8313   6754   6149    892   -830   -692       C  
-ATOM    688  CD2 LEU A 537       5.851 -15.993 -16.294  1.00 46.65           C  
-ANISOU  688  CD2 LEU A 537     7191   5547   4988    762   -640   -561       C  
-ATOM    689  N   TYR A 538       8.270 -13.357 -20.149  1.00 66.70           N  
-ANISOU  689  N   TYR A 538     8992   8593   7759    739   -690   -635       N  
-ATOM    690  CA  TYR A 538       8.774 -13.909 -21.400  1.00 73.20           C  
-ANISOU  690  CA  TYR A 538     9685   9530   8599    745   -735   -684       C  
-ATOM    691  C   TYR A 538      10.259 -13.604 -21.558  1.00 69.74           C  
-ANISOU  691  C   TYR A 538     9163   9164   8173    800   -831   -780       C  
-ATOM    692  O   TYR A 538      11.047 -14.481 -21.912  1.00 68.91           O  
-ANISOU  692  O   TYR A 538     9042   9090   8050    854   -922   -868       O  
-ATOM    693  CB  TYR A 538       7.991 -13.331 -22.581  1.00 79.53           C  
-ANISOU  693  CB  TYR A 538    10332  10431   9455    659   -640   -610       C  
-ATOM    694  CG  TYR A 538       8.294 -13.978 -23.916  1.00 76.47           C  
-ANISOU  694  CG  TYR A 538     9816  10159   9079    653   -670   -650       C  
-ATOM    695  CD1 TYR A 538       7.510 -15.016 -24.399  1.00 68.17           C  
-ANISOU  695  CD1 TYR A 538     8790   9098   8013    637   -648   -632       C  
-ATOM    696  CD2 TYR A 538       9.356 -13.543 -24.697  1.00 79.68           C  
-ANISOU  696  CD2 TYR A 538    10075  10687   9512    658   -717   -709       C  
-ATOM    697  CE1 TYR A 538       7.776 -15.607 -25.618  1.00 74.19           C  
-ANISOU  697  CE1 TYR A 538     9435   9969   8787    631   -675   -671       C  
-ATOM    698  CE2 TYR A 538       9.632 -14.128 -25.918  1.00 82.86           C  
-ANISOU  698  CE2 TYR A 538    10359  11200   9924    647   -741   -750       C  
-ATOM    699  CZ  TYR A 538       8.840 -15.159 -26.374  1.00 83.21           C  
-ANISOU  699  CZ  TYR A 538    10431  11233   9953    635   -721   -730       C  
-ATOM    700  OH  TYR A 538       9.112 -15.742 -27.589  1.00 90.64           O  
-ANISOU  700  OH  TYR A 538    11252  12286  10902    624   -745   -774       O  
-ATOM    701  N   HIS A 539      10.636 -12.357 -21.291  1.00 63.99           N  
-ANISOU  701  N   HIS A 539     8377   8459   7476    784   -810   -767       N  
-ATOM    702  CA  HIS A 539      12.022 -11.929 -21.435  1.00 57.31           C  
-ANISOU  702  CA  HIS A 539     7442   7685   6647    827   -889   -858       C  
-ATOM    703  C   HIS A 539      12.949 -12.667 -20.476  1.00 61.63           C  
-ANISOU  703  C   HIS A 539     8117   8154   7148    928  -1009   -957       C  
-ATOM    704  O   HIS A 539      14.108 -12.921 -20.795  1.00 76.15           O  
-ANISOU  704  O   HIS A 539     9888  10053   8992    979  -1101  -1062       O  
-ATOM    705  CB  HIS A 539      12.150 -10.419 -21.226  1.00 60.05           C  
-ANISOU  705  CB  HIS A 539     7719   8059   7038    788   -837   -818       C  
-ATOM    706  CG  HIS A 539      13.559  -9.919 -21.297  1.00 79.54           C  
-ANISOU  706  CG  HIS A 539    10099  10597   9525    827   -912   -913       C  
-ATOM    707  ND1 HIS A 539      14.426  -9.975 -20.225  1.00 86.89           N  
-ANISOU  707  ND1 HIS A 539    11126  11459  10431    907   -996   -990       N  
-ATOM    708  CD2 HIS A 539      14.255  -9.350 -22.310  1.00 88.86           C  
-ANISOU  708  CD2 HIS A 539    11106  11909  10747    794   -914   -948       C  
-ATOM    709  CE1 HIS A 539      15.591  -9.465 -20.575  1.00 90.64           C  
-ANISOU  709  CE1 HIS A 539    11483  12021  10935    924  -1047  -1072       C  
-ATOM    710  NE2 HIS A 539      15.515  -9.078 -21.838  1.00 91.45           N  
-ANISOU  710  NE2 HIS A 539    11422  12247  11077    854   -995  -1048       N  
-ATOM    711  N   HIS A 540      12.439 -13.004 -19.297  1.00 58.03           N  
-ANISOU  711  N   HIS A 540     7845   7560   6645    954  -1009   -927       N  
-ATOM    712  CA  HIS A 540      13.230 -13.738 -18.317  1.00 61.33           C  
-ANISOU  712  CA  HIS A 540     8406   7886   7010   1049  -1126  -1012       C  
-ATOM    713  C   HIS A 540      13.376 -15.204 -18.711  1.00 60.37           C  
-ANISOU  713  C   HIS A 540     8327   7753   6856   1095  -1204  -1070       C  
-ATOM    714  O   HIS A 540      14.477 -15.754 -18.700  1.00 63.50           O  
-ANISOU  714  O   HIS A 540     8719   8162   7245   1173  -1324  -1180       O  
-ATOM    715  CB  HIS A 540      12.605 -13.631 -16.923  1.00 71.26           C  
-ANISOU  715  CB  HIS A 540     9857   8999   8219   1055  -1098   -958       C  
-ATOM    716  CG  HIS A 540      12.872 -12.327 -16.238  1.00 74.21           C  
-ANISOU  716  CG  HIS A 540    10216   9364   8615   1046  -1070   -942       C  
-ATOM    717  ND1 HIS A 540      14.141 -11.913 -15.897  1.00 85.37           N  
-ANISOU  717  ND1 HIS A 540    11598  10800  10038   1110  -1160  -1032       N  
-ATOM    718  CD2 HIS A 540      12.031 -11.354 -15.812  1.00 77.78           C  
-ANISOU  718  CD2 HIS A 540    10681   9786   9086    983   -963   -853       C  
-ATOM    719  CE1 HIS A 540      14.072 -10.735 -15.301  1.00 91.63           C  
-ANISOU  719  CE1 HIS A 540    12385  11578  10853   1085  -1108   -995       C  
-ATOM    720  NE2 HIS A 540      12.804 -10.375 -15.236  1.00 89.07           N  
-ANISOU  720  NE2 HIS A 540    12087  11221  10534   1009   -989   -887       N  
-ATOM    721  N   LEU A 541      12.258 -15.827 -19.065  1.00 61.49           N  
-ANISOU  721  N   LEU A 541     8507   7872   6986   1047  -1136   -999       N  
-ATOM    722  CA  LEU A 541      12.241 -17.247 -19.405  1.00 63.14           C  
-ANISOU  722  CA  LEU A 541     8768   8058   7164   1083  -1200  -1043       C  
-ATOM    723  C   LEU A 541      12.943 -17.586 -20.724  1.00 66.98           C  
-ANISOU  723  C   LEU A 541     9076   8683   7691   1092  -1246  -1120       C  
-ATOM    724  O   LEU A 541      13.490 -18.681 -20.871  1.00 74.60           O  
-ANISOU  724  O   LEU A 541    10070   9636   8637   1155  -1347  -1204       O  
-ATOM    725  CB  LEU A 541      10.801 -17.782 -19.412  1.00 64.49           C  
-ANISOU  725  CB  LEU A 541     9026   8166   7313   1023  -1105   -946       C  
-ATOM    726  CG  LEU A 541      10.250 -18.388 -18.116  1.00 67.39           C  
-ANISOU  726  CG  LEU A 541     9629   8367   7609   1043  -1112   -916       C  
-ATOM    727  CD1 LEU A 541      10.661 -17.563 -16.914  1.00 69.59           C  
-ANISOU  727  CD1 LEU A 541     9998   8576   7867   1070  -1129   -917       C  
-ATOM    728  CD2 LEU A 541       8.734 -18.537 -18.169  1.00 62.24           C  
-ANISOU  728  CD2 LEU A 541     9028   7671   6949    960   -985   -812       C  
-ATOM    729  N   HIS A 542      12.942 -16.650 -21.671  1.00 68.55           N  
-ANISOU  729  N   HIS A 542     9091   9010   7944   1028  -1177  -1093       N  
-ATOM    730  CA  HIS A 542      13.378 -16.950 -23.038  1.00 62.98           C  
-ANISOU  730  CA  HIS A 542     8212   8444   7273   1013  -1195  -1148       C  
-ATOM    731  C   HIS A 542      14.392 -15.953 -23.624  1.00 73.47           C  
-ANISOU  731  C   HIS A 542     9367   9901   8647   1000  -1207  -1204       C  
-ATOM    732  O   HIS A 542      15.198 -16.313 -24.477  1.00 91.57           O  
-ANISOU  732  O   HIS A 542    11539  12296  10958   1016  -1264  -1296       O  
-ATOM    733  CB  HIS A 542      12.155 -17.067 -23.960  1.00 56.75           C  
-ANISOU  733  CB  HIS A 542     7362   7702   6499    927  -1086  -1054       C  
-ATOM    734  CG  HIS A 542      11.031 -17.869 -23.377  1.00 58.68           C  
-ANISOU  734  CG  HIS A 542     7770   7823   6704    922  -1050   -988       C  
-ATOM    735  ND1 HIS A 542      11.175 -19.186 -22.994  1.00 69.49           N  
-ANISOU  735  ND1 HIS A 542     9264   9109   8030    986  -1134  -1044       N  
-ATOM    736  CD2 HIS A 542       9.741 -17.544 -23.120  1.00 55.58           C  
-ANISOU  736  CD2 HIS A 542     7435   7374   6309    857   -939   -876       C  
-ATOM    737  CE1 HIS A 542      10.026 -19.635 -22.521  1.00 69.23           C  
-ANISOU  737  CE1 HIS A 542     9362   8975   7966    957  -1072   -965       C  
-ATOM    738  NE2 HIS A 542       9.139 -18.658 -22.586  1.00 57.62           N  
-ANISOU  738  NE2 HIS A 542     7850   7520   6521    878   -952   -866       N  
-ATOM    739  N   ALA A 543      14.350 -14.706 -23.163  1.00 62.13           N  
-ANISOU  739  N   ALA A 543     7919   8459   7230    968  -1152  -1152       N  
-ATOM    740  CA  ALA A 543      15.216 -13.659 -23.707  1.00 76.72           C  
-ANISOU  740  CA  ALA A 543     9605  10423   9121    943  -1150  -1191       C  
-ATOM    741  C   ALA A 543      16.570 -13.575 -23.001  1.00 69.22           C  
-ANISOU  741  C   ALA A 543     8676   9456   8168   1028  -1260  -1312       C  
-ATOM    742  O   ALA A 543      17.613 -13.555 -23.650  1.00 74.39           O  
-ANISOU  742  O   ALA A 543     9204  10215   8847   1043  -1315  -1415       O  
-ATOM    743  CB  ALA A 543      14.515 -12.319 -23.697  1.00131.35           C  
-ANISOU  743  CB  ALA A 543    16482  17354  16071    862  -1037  -1078       C  
-ATOM    744  N   SER A 544      16.554 -13.503 -21.675  1.00 83.33           N  
-ANISOU  744  N   SER A 544    10622  11114   9925   1080  -1291  -1303       N  
-ATOM    745  CA  SER A 544      17.797 -13.398 -20.912  1.00 88.90           C  
-ANISOU  745  CA  SER A 544    11358  11792  10626   1165  -1399  -1416       C  
-ATOM    746  C   SER A 544      18.141 -14.693 -20.184  1.00 84.72           C  
-ANISOU  746  C   SER A 544    10984  11157  10048   1265  -1520  -1493       C  
-ATOM    747  O   SER A 544      19.312 -15.010 -19.985  1.00 79.88           O  
-ANISOU  747  O   SER A 544    10359  10553   9438   1345  -1638  -1621       O  
-ATOM    748  CB  SER A 544      17.741 -12.229 -19.920  1.00104.37           C  
-ANISOU  748  CB  SER A 544    13372  13692  12590   1156  -1359  -1366       C  
-ATOM    749  OG  SER A 544      16.781 -12.459 -18.903  1.00107.21           O  
-ANISOU  749  OG  SER A 544    13916  13914  12906   1160  -1326  -1281       O  
-ATOM    750  N   PHE A 548      15.921 -18.528 -12.677  1.00 64.72           N  
-ANISOU  750  N   PHE A 548     9861   7647   7081   1532  -1778  -1341       N  
-ATOM    751  CA  PHE A 548      15.268 -18.477 -11.374  1.00 81.02           C  
-ANISOU  751  CA  PHE A 548    12141   9571   9072   1519  -1747  -1271       C  
-ATOM    752  C   PHE A 548      15.419 -19.798 -10.633  1.00 84.30           C  
-ANISOU  752  C   PHE A 548    12777   9849   9406   1589  -1868  -1306       C  
-ATOM    753  O   PHE A 548      15.573 -20.852 -11.248  1.00 86.69           O  
-ANISOU  753  O   PHE A 548    13071  10158   9711   1620  -1935  -1349       O  
-ATOM    754  CB  PHE A 548      13.777 -18.162 -11.521  1.00123.18           C  
-ANISOU  754  CB  PHE A 548    17490  14904  14409   1404  -1574  -1140       C  
-ATOM    755  CG  PHE A 548      13.492 -16.834 -12.159  1.00138.10           C  
-ANISOU  755  CG  PHE A 548    19185  16911  16375   1330  -1453  -1093       C  
-ATOM    756  CD1 PHE A 548      12.478 -16.708 -13.093  1.00143.09           C  
-ANISOU  756  CD1 PHE A 548    19710  17611  17047   1241  -1328  -1015       C  
-ATOM    757  CD2 PHE A 548      14.231 -15.714 -11.823  1.00146.24           C  
-ANISOU  757  CD2 PHE A 548    20144  17982  17438   1351  -1467  -1125       C  
-ATOM    758  CE1 PHE A 548      12.205 -15.491 -13.681  1.00147.10           C  
-ANISOU  758  CE1 PHE A 548    20047  18220  17624   1174  -1224   -968       C  
-ATOM    759  CE2 PHE A 548      13.964 -14.492 -12.410  1.00151.09           C  
-ANISOU  759  CE2 PHE A 548    20587  18698  18123   1281  -1359  -1078       C  
-ATOM    760  CZ  PHE A 548      12.949 -14.381 -13.340  1.00151.07           C  
-ANISOU  760  CZ  PHE A 548    20484  18758  18158   1193  -1240   -998       C  
-ATOM    761  N   GLU A 549      15.364 -19.736  -9.308  1.00 92.47           N  
-ANISOU  761  N   GLU A 549    14011  10756  10367   1610  -1896  -1285       N  
-ATOM    762  CA  GLU A 549      15.386 -20.935  -8.486  1.00 90.73           C  
-ANISOU  762  CA  GLU A 549    14029  10388  10058   1665  -2003  -1301       C  
-ATOM    763  C   GLU A 549      14.001 -21.571  -8.529  1.00 71.23           C  
-ANISOU  763  C   GLU A 549    11666   7855   7544   1578  -1892  -1197       C  
-ATOM    764  O   GLU A 549      13.006 -20.874  -8.720  1.00 64.40           O  
-ANISOU  764  O   GLU A 549    10741   7028   6699   1479  -1732  -1107       O  
-ATOM    765  CB  GLU A 549      15.767 -20.573  -7.052  1.00125.18           C  
-ANISOU  765  CB  GLU A 549    18571  14641  14352   1709  -2062  -1310       C  
-ATOM    766  CG  GLU A 549      16.362 -21.712  -6.252  1.00132.04           C  
-ANISOU  766  CG  GLU A 549    19654  15373  15140   1804  -2234  -1371       C  
-ATOM    767  CD  GLU A 549      17.380 -21.224  -5.243  1.00134.66           C  
-ANISOU  767  CD  GLU A 549    20060  15657  15445   1888  -2349  -1440       C  
-ATOM    768  OE1 GLU A 549      18.134 -20.283  -5.571  1.00134.72           O  
-ANISOU  768  OE1 GLU A 549    19890  15773  15527   1913  -2355  -1498       O  
-ATOM    769  OE2 GLU A 549      17.429 -21.780  -4.126  1.00133.15           O  
-ANISOU  769  OE2 GLU A 549    20109  15322  15160   1928  -2433  -1437       O  
-ATOM    770  N   MET A 550      13.931 -22.888  -8.366  1.00 72.51           N  
-ANISOU  770  N   MET A 550    11981   7920   7649   1613  -1977  -1212       N  
-ATOM    771  CA  MET A 550      12.647 -23.580  -8.445  1.00 78.54           C  
-ANISOU  771  CA  MET A 550    12846   8623   8372   1531  -1876  -1122       C  
-ATOM    772  C   MET A 550      11.627 -22.962  -7.494  1.00 79.74           C  
-ANISOU  772  C   MET A 550    13128   8701   8467   1444  -1743  -1021       C  
-ATOM    773  O   MET A 550      10.431 -22.933  -7.785  1.00 62.94           O  
-ANISOU  773  O   MET A 550    10989   6582   6344   1345  -1597   -937       O  
-ATOM    774  CB  MET A 550      12.809 -25.077  -8.168  1.00 92.63           C  
-ANISOU  774  CB  MET A 550    14815  10288  10090   1589  -2003  -1156       C  
-ATOM    775  CG  MET A 550      11.501 -25.860  -8.172  1.00101.04           C  
-ANISOU  775  CG  MET A 550    16004  11279  11107   1503  -1903  -1066       C  
-ATOM    776  SD  MET A 550      10.465 -25.548  -9.618  1.00 78.60           S  
-ANISOU  776  SD  MET A 550    12926   8583   8356   1398  -1726  -1006       S  
-ATOM    777  CE  MET A 550      11.596 -25.916 -10.959  1.00 67.49           C  
-ANISOU  777  CE  MET A 550    11295   7310   7040   1483  -1846  -1120       C  
-ATOM    778  N   LYS A 551      12.109 -22.461  -6.361  1.00 94.05           N  
-ANISOU  778  N   LYS A 551    15060  10445  10230   1480  -1793  -1036       N  
-ATOM    779  CA  LYS A 551      11.250 -21.800  -5.387  1.00 96.14           C  
-ANISOU  779  CA  LYS A 551    15445  10643  10441   1401  -1673   -953       C  
-ATOM    780  C   LYS A 551      10.609 -20.558  -5.992  1.00 82.48           C  
-ANISOU  780  C   LYS A 551    13511   9033   8795   1315  -1509   -899       C  
-ATOM    781  O   LYS A 551       9.409 -20.328  -5.839  1.00 73.32           O  
-ANISOU  781  O   LYS A 551    12386   7851   7622   1215  -1362   -815       O  
-ATOM    782  CB  LYS A 551      12.054 -21.413  -4.148  1.00113.98           C  
-ANISOU  782  CB  LYS A 551    17841  12824  12641   1467  -1771   -994       C  
-ATOM    783  CG  LYS A 551      11.252 -20.663  -3.102  1.00111.32           C  
-ANISOU  783  CG  LYS A 551    17623  12424  12249   1388  -1651   -919       C  
-ATOM    784  CD  LYS A 551      12.137 -20.233  -1.948  1.00106.88           C  
-ANISOU  784  CD  LYS A 551    17177  11798  11634   1459  -1755   -966       C  
-ATOM    785  CE  LYS A 551      11.358 -19.422  -0.931  1.00105.16           C  
-ANISOU  785  CE  LYS A 551    17062  11527  11365   1378  -1631   -898       C  
-ATOM    786  NZ  LYS A 551      12.233 -18.953   0.177  1.00108.46           N  
-ANISOU  786  NZ  LYS A 551    17586  11890  11733   1447  -1731   -946       N  
-ATOM    787  N   LYS A 552      11.424 -19.762  -6.676  1.00 79.69           N  
-ANISOU  787  N   LYS A 552    12946   8804   8529   1354  -1537   -951       N  
-ATOM    788  CA  LYS A 552      10.962 -18.538  -7.320  1.00 78.79           C  
-ANISOU  788  CA  LYS A 552    12627   8808   8501   1281  -1399   -906       C  
-ATOM    789  C   LYS A 552       9.960 -18.836  -8.432  1.00 78.21           C  
-ANISOU  789  C   LYS A 552    12442   8800   8475   1202  -1288   -849       C  
-ATOM    790  O   LYS A 552       8.920 -18.185  -8.535  1.00 74.59           O  
-ANISOU  790  O   LYS A 552    11935   8363   8041   1109  -1140   -771       O  
-ATOM    791  CB  LYS A 552      12.150 -17.749  -7.873  1.00 87.63           C  
-ANISOU  791  CB  LYS A 552    13551  10045   9700   1342  -1468   -982       C  
-ATOM    792  CG  LYS A 552      13.134 -17.290  -6.807  1.00104.20           C  
-ANISOU  792  CG  LYS A 552    15736  12091  11764   1417  -1568  -1042       C  
-ATOM    793  CD  LYS A 552      14.236 -16.427  -7.400  1.00113.38           C  
-ANISOU  793  CD  LYS A 552    16690  13378  13013   1464  -1617  -1117       C  
-ATOM    794  CE  LYS A 552      15.193 -15.930  -6.325  1.00121.72           C  
-ANISOU  794  CE  LYS A 552    17826  14383  14039   1538  -1714  -1180       C  
-ATOM    795  NZ  LYS A 552      16.259 -15.057  -6.891  1.00124.73           N  
-ANISOU  795  NZ  LYS A 552    18001  14886  14506   1578  -1754  -1257       N  
-ATOM    796  N   LEU A 553      10.284 -19.824  -9.260  1.00 82.38           N  
-ANISOU  796  N   LEU A 553    12927   9359   9016   1241  -1363   -892       N  
-ATOM    797  CA  LEU A 553       9.398 -20.252 -10.337  1.00 71.54           C  
-ANISOU  797  CA  LEU A 553    11455   8044   7682   1175  -1273   -847       C  
-ATOM    798  C   LEU A 553       8.003 -20.572  -9.812  1.00 62.44           C  
-ANISOU  798  C   LEU A 553    10451   6797   6477   1087  -1153   -758       C  
-ATOM    799  O   LEU A 553       7.001 -20.208 -10.425  1.00 66.53           O  
-ANISOU  799  O   LEU A 553    10868   7371   7041   1001  -1018   -695       O  
-ATOM    800  CB  LEU A 553       9.981 -21.470 -11.058  1.00 65.70           C  
-ANISOU  800  CB  LEU A 553    10698   7319   6945   1240  -1391   -916       C  
-ATOM    801  CG  LEU A 553      11.317 -21.250 -11.771  1.00 57.33           C  
-ANISOU  801  CG  LEU A 553     9466   6369   5946   1320  -1503  -1015       C  
-ATOM    802  CD1 LEU A 553      11.845 -22.559 -12.343  1.00 51.86           C  
-ANISOU  802  CD1 LEU A 553     8782   5672   5249   1386  -1624  -1090       C  
-ATOM    803  CD2 LEU A 553      11.187 -20.187 -12.858  1.00 55.53           C  
-ANISOU  803  CD2 LEU A 553     8987   6299   5812   1263  -1403   -993       C  
-ATOM    804  N   ILE A 554       7.946 -21.259  -8.676  1.00 60.96           N  
-ANISOU  804  N   ILE A 554    10505   6466   6191   1106  -1203   -756       N  
-ATOM    805  CA  ILE A 554       6.671 -21.582  -8.049  1.00 71.12           C  
-ANISOU  805  CA  ILE A 554    11953   7654   7416   1018  -1090   -680       C  
-ATOM    806  C   ILE A 554       5.970 -20.313  -7.588  1.00 74.62           C  
-ANISOU  806  C   ILE A 554    12358   8114   7880    940   -950   -621       C  
-ATOM    807  O   ILE A 554       4.757 -20.182  -7.729  1.00 86.01           O  
-ANISOU  807  O   ILE A 554    13790   9555   9335    845   -809   -557       O  
-ATOM    808  CB  ILE A 554       6.849 -22.528  -6.846  1.00 80.76           C  
-ANISOU  808  CB  ILE A 554    13455   8713   8518   1054  -1180   -692       C  
-ATOM    809  CG1 ILE A 554       7.407 -23.875  -7.309  1.00 79.27           C  
-ANISOU  809  CG1 ILE A 554    13314   8494   8310   1126  -1316   -746       C  
-ATOM    810  CG2 ILE A 554       5.526 -22.719  -6.113  1.00 80.92           C  
-ANISOU  810  CG2 ILE A 554    13643   8633   8470    950  -1048   -613       C  
-ATOM    811  CD1 ILE A 554       7.608 -24.861  -6.188  1.00 85.52           C  
-ANISOU  811  CD1 ILE A 554    14387   9120   8985   1164  -1419   -757       C  
-ATOM    812  N   ASP A 555       6.739 -19.379  -7.038  1.00 67.07           N  
-ANISOU  812  N   ASP A 555    11378   7173   6933    982   -992   -650       N  
-ATOM    813  CA  ASP A 555       6.181 -18.109  -6.589  1.00 67.64           C  
-ANISOU  813  CA  ASP A 555    11404   7263   7031    916   -871   -604       C  
-ATOM    814  C   ASP A 555       5.522 -17.382  -7.754  1.00 62.38           C  
-ANISOU  814  C   ASP A 555    10507   6723   6473    850   -753   -563       C  
-ATOM    815  O   ASP A 555       4.374 -16.948  -7.661  1.00 70.11           O  
-ANISOU  815  O   ASP A 555    11478   7694   7468    759   -613   -501       O  
-ATOM    816  CB  ASP A 555       7.267 -17.226  -5.974  1.00 72.40           C  
-ANISOU  816  CB  ASP A 555    11991   7879   7640    983   -950   -652       C  
-ATOM    817  CG  ASP A 555       6.701 -15.975  -5.332  1.00 74.86           C  
-ANISOU  817  CG  ASP A 555    12285   8189   7969    918   -833   -608       C  
-ATOM    818  OD1 ASP A 555       5.542 -16.021  -4.868  1.00 79.77           O  
-ANISOU  818  OD1 ASP A 555    13003   8750   8557    832   -716   -549       O  
-ATOM    819  OD2 ASP A 555       7.412 -14.948  -5.289  1.00 70.75           O  
-ANISOU  819  OD2 ASP A 555    11655   7729   7499    952   -858   -636       O  
-ATOM    820  N   ILE A 556       6.264 -17.252  -8.849  1.00 44.18           N  
-ANISOU  820  N   ILE A 556     8013   4533   4241    896   -812   -602       N  
-ATOM    821  CA  ILE A 556       5.755 -16.618 -10.058  1.00 39.16           C  
-ANISOU  821  CA  ILE A 556     7154   4022   3704    840   -718   -567       C  
-ATOM    822  C   ILE A 556       4.499 -17.330 -10.542  1.00 41.94           C  
-ANISOU  822  C   ILE A 556     7526   4357   4053    765   -621   -513       C  
-ATOM    823  O   ILE A 556       3.519 -16.696 -10.925  1.00 50.66           O  
-ANISOU  823  O   ILE A 556     8535   5503   5211    685   -494   -456       O  
-ATOM    824  CB  ILE A 556       6.810 -16.639 -11.174  1.00 48.34           C  
-ANISOU  824  CB  ILE A 556     8138   5304   4927    902   -811   -627       C  
-ATOM    825  CG1 ILE A 556       8.033 -15.818 -10.758  1.00 46.41           C  
-ANISOU  825  CG1 ILE A 556     7851   5087   4697    968   -896   -684       C  
-ATOM    826  CG2 ILE A 556       6.222 -16.107 -12.467  1.00 61.35           C  
-ANISOU  826  CG2 ILE A 556     9571   7074   6664    838   -716   -585       C  
-ATOM    827  CD1 ILE A 556       9.209 -15.942 -11.704  1.00 52.22           C  
-ANISOU  827  CD1 ILE A 556     8434   5928   5480   1036  -1002   -762       C  
-ATOM    828  N   ALA A 557       4.539 -18.657 -10.517  1.00 55.02           N  
-ANISOU  828  N   ALA A 557     9306   5950   5650    794   -686   -535       N  
-ATOM    829  CA  ALA A 557       3.388 -19.469 -10.889  1.00 50.15           C  
-ANISOU  829  CA  ALA A 557     8729   5303   5021    727   -602   -491       C  
-ATOM    830  C   ALA A 557       2.256 -19.283  -9.885  1.00 51.39           C  
-ANISOU  830  C   ALA A 557     9034   5360   5129    644   -482   -435       C  
-ATOM    831  O   ALA A 557       1.080 -19.364 -10.235  1.00 45.66           O  
-ANISOU  831  O   ALA A 557     8281   4640   4428    562   -362   -388       O  
-ATOM    832  CB  ALA A 557       3.783 -20.929 -10.970  1.00 51.07           C  
-ANISOU  832  CB  ALA A 557     8963   5363   5081    782   -710   -533       C  
-ATOM    833  N   ARG A 558       2.627 -19.039  -8.633  1.00 66.66           N  
-ANISOU  833  N   ARG A 558    11126   7205   6996    666   -517   -446       N  
-ATOM    834  CA  ARG A 558       1.666 -18.892  -7.549  1.00 66.38           C  
-ANISOU  834  CA  ARG A 558    11251   7069   6901    590   -413   -403       C  
-ATOM    835  C   ARG A 558       0.909 -17.575  -7.663  1.00 64.89           C  
-ANISOU  835  C   ARG A 558    10924   6942   6791    516   -276   -362       C  
-ATOM    836  O   ARG A 558      -0.317 -17.541  -7.563  1.00 73.99           O  
-ANISOU  836  O   ARG A 558    12098   8068   7948    425   -146   -320       O  
-ATOM    837  CB  ARG A 558       2.382 -18.961  -6.199  1.00 75.36           C  
-ANISOU  837  CB  ARG A 558    12591   8100   7943    639   -500   -431       C  
-ATOM    838  CG  ARG A 558       1.464 -19.163  -5.003  1.00 85.78           C  
-ANISOU  838  CG  ARG A 558    14126   9295   9172    562   -412   -395       C  
-ATOM    839  CD  ARG A 558       1.834 -18.222  -3.867  1.00 86.16           C  
-ANISOU  839  CD  ARG A 558    14246   9306   9187    571   -416   -403       C  
-ATOM    840  NE  ARG A 558       3.280 -18.108  -3.696  1.00 89.03           N  
-ANISOU  840  NE  ARG A 558    14605   9681   9540    685   -575   -460       N  
-ATOM    841  CZ  ARG A 558       3.970 -18.694  -2.722  1.00102.51           C  
-ANISOU  841  CZ  ARG A 558    16518  11285  11146    743   -690   -491       C  
-ATOM    842  NH1 ARG A 558       3.349 -19.438  -1.817  1.00107.46           N  
-ANISOU  842  NH1 ARG A 558    17380  11785  11664    694   -661   -466       N  
-ATOM    843  NH2 ARG A 558       5.285 -18.530  -2.651  1.00108.73           N  
-ANISOU  843  NH2 ARG A 558    17279  12094  11939    849   -834   -551       N  
-ATOM    844  N   GLN A 559       1.650 -16.491  -7.869  1.00 47.52           N  
-ANISOU  844  N   GLN A 559     8580   4823   4654    555   -309   -379       N  
-ATOM    845  CA  GLN A 559       1.055 -15.166  -7.980  1.00 37.03           C  
-ANISOU  845  CA  GLN A 559     7113   3552   3405    495   -196   -344       C  
-ATOM    846  C   GLN A 559       0.118 -15.078  -9.181  1.00 43.35           C  
-ANISOU  846  C   GLN A 559     7745   4435   4290    432    -99   -305       C  
-ATOM    847  O   GLN A 559      -0.941 -14.454  -9.108  1.00 48.52           O  
-ANISOU  847  O   GLN A 559     8359   5091   4987    353     27   -265       O  
-ATOM    848  CB  GLN A 559       2.143 -14.093  -8.076  1.00 43.64           C  
-ANISOU  848  CB  GLN A 559     7823   4463   4295    555   -263   -373       C  
-ATOM    849  CG  GLN A 559       3.097 -14.061  -6.891  1.00 44.15           C  
-ANISOU  849  CG  GLN A 559     8040   4452   4283    621   -360   -417       C  
-ATOM    850  CD  GLN A 559       4.052 -12.883  -6.942  1.00 49.07           C  
-ANISOU  850  CD  GLN A 559     8529   5147   4966    668   -407   -446       C  
-ATOM    851  OE1 GLN A 559       3.651 -11.757  -7.232  1.00 46.38           O  
-ANISOU  851  OE1 GLN A 559     8048   4869   4707    622   -322   -415       O  
-ATOM    852  NE2 GLN A 559       5.323 -13.138  -6.653  1.00 57.18           N  
-ANISOU  852  NE2 GLN A 559     9602   6166   5958    762   -546   -508       N  
-ATOM    853  N   THR A 560       0.509 -15.708 -10.284  1.00 58.54           N  
-ANISOU  853  N   THR A 560     9571   6429   6242    469   -161   -320       N  
-ATOM    854  CA  THR A 560      -0.306 -15.694 -11.495  1.00 56.37           C  
-ANISOU  854  CA  THR A 560     9136   6238   6045    416    -83   -287       C  
-ATOM    855  C   THR A 560      -1.674 -16.327 -11.246  1.00 49.10           C  
-ANISOU  855  C   THR A 560     8316   5245   5095    334     28   -252       C  
-ATOM    856  O   THR A 560      -2.686 -15.863 -11.766  1.00 50.10           O  
-ANISOU  856  O   THR A 560     8335   5413   5290    265    138   -216       O  
-ATOM    857  CB  THR A 560       0.392 -16.419 -12.664  1.00 47.49           C  
-ANISOU  857  CB  THR A 560     7908   5194   4940    471   -176   -317       C  
-ATOM    858  OG1 THR A 560       1.674 -15.826 -12.903  1.00 37.75           O  
-ANISOU  858  OG1 THR A 560     6576   4032   3734    541   -275   -358       O  
-ATOM    859  CG2 THR A 560      -0.448 -16.322 -13.928  1.00 37.95           C  
-ANISOU  859  CG2 THR A 560     6530   4078   3811    414    -95   -281       C  
-ATOM    860  N   ALA A 561      -1.699 -17.386 -10.445  1.00 43.88           N  
-ANISOU  860  N   ALA A 561     7865   4474   4335    342     -3   -267       N  
-ATOM    861  CA  ALA A 561      -2.953 -18.048 -10.106  1.00 40.67           C  
-ANISOU  861  CA  ALA A 561     7574   3988   3890    260    103   -241       C  
-ATOM    862  C   ALA A 561      -3.807 -17.143  -9.226  1.00 58.56           C  
-ANISOU  862  C   ALA A 561     9880   6209   6161    184    225   -216       C  
-ATOM    863  O   ALA A 561      -5.029 -17.100  -9.365  1.00 63.96           O  
-ANISOU  863  O   ALA A 561    10541   6887   6876    100    349   -190       O  
-ATOM    864  CB  ALA A 561      -2.690 -19.372  -9.419  1.00 39.01           C  
-ANISOU  864  CB  ALA A 561     7589   3664   3566    287     32   -262       C  
-ATOM    865  N   ARG A 562      -3.154 -16.428  -8.315  1.00 65.58           N  
-ANISOU  865  N   ARG A 562    10827   7068   7022    215    187   -229       N  
-ATOM    866  CA  ARG A 562      -3.838 -15.446  -7.483  1.00 57.59           C  
-ANISOU  866  CA  ARG A 562     9836   6023   6022    150    294   -213       C  
-ATOM    867  C   ARG A 562      -4.533 -14.420  -8.367  1.00 46.94           C  
-ANISOU  867  C   ARG A 562     8263   4772   4799    103    386   -187       C  
-ATOM    868  O   ARG A 562      -5.720 -14.143  -8.196  1.00 54.57           O  
-ANISOU  868  O   ARG A 562     9223   5718   5794     18    513   -168       O  
-ATOM    869  CB  ARG A 562      -2.853 -14.757  -6.533  1.00 56.19           C  
-ANISOU  869  CB  ARG A 562     9724   5818   5808    204    222   -237       C  
-ATOM    870  CG  ARG A 562      -2.403 -15.629  -5.370  1.00 62.46           C  
-ANISOU  870  CG  ARG A 562    10772   6491   6468    232    153   -259       C  
-ATOM    871  CD  ARG A 562      -1.368 -14.931  -4.504  1.00 71.87           C  
-ANISOU  871  CD  ARG A 562    12014   7664   7629    294     71   -287       C  
-ATOM    872  NE  ARG A 562      -1.071 -15.699  -3.297  1.00 77.15           N  
-ANISOU  872  NE  ARG A 562    12940   8208   8164    309     15   -304       N  
-ATOM    873  CZ  ARG A 562      -0.023 -15.483  -2.507  1.00 77.96           C  
-ANISOU  873  CZ  ARG A 562    13133   8275   8214    381    -91   -336       C  
-ATOM    874  NH1 ARG A 562       0.844 -14.523  -2.796  1.00 71.59           N  
-ANISOU  874  NH1 ARG A 562    12175   7550   7478    442   -148   -358       N  
-ATOM    875  NH2 ARG A 562       0.162 -16.235  -1.431  1.00 83.44           N  
-ANISOU  875  NH2 ARG A 562    14071   8851   8782    389   -142   -347       N  
-ATOM    876  N   GLY A 563      -3.788 -13.869  -9.320  1.00 38.19           N  
-ANISOU  876  N   GLY A 563     6974   3770   3766    158    320   -188       N  
-ATOM    877  CA  GLY A 563      -4.332 -12.902 -10.255  1.00 34.30           C  
-ANISOU  877  CA  GLY A 563     6267   3374   3392    121    388   -159       C  
-ATOM    878  C   GLY A 563      -5.442 -13.478 -11.115  1.00 50.62           C  
-ANISOU  878  C   GLY A 563     8272   5464   5497     62    467   -136       C  
-ATOM    879  O   GLY A 563      -6.483 -12.846 -11.302  1.00 62.70           O  
-ANISOU  879  O   GLY A 563     9716   7010   7097     -5    575   -114       O  
-ATOM    880  N   MET A 564      -5.224 -14.681 -11.637  1.00 39.74           N  
-ANISOU  880  N   MET A 564     6936   4088   4078     90    412   -147       N  
-ATOM    881  CA  MET A 564      -6.205 -15.328 -12.503  1.00 40.59           C  
-ANISOU  881  CA  MET A 564     6984   4220   4218     40    477   -131       C  
-ATOM    882  C   MET A 564      -7.479 -15.704 -11.756  1.00 39.67           C  
-ANISOU  882  C   MET A 564     6995   4009   4067    -46    599   -125       C  
-ATOM    883  O   MET A 564      -8.581 -15.554 -12.282  1.00 43.81           O  
-ANISOU  883  O   MET A 564     7428   4560   4656   -111    698   -109       O  
-ATOM    884  CB  MET A 564      -5.606 -16.563 -13.173  1.00 47.34           C  
-ANISOU  884  CB  MET A 564     7861   5093   5032     93    383   -150       C  
-ATOM    885  CG  MET A 564      -4.565 -16.246 -14.228  1.00 47.56           C  
-ANISOU  885  CG  MET A 564     7721   5237   5111    161    284   -160       C  
-ATOM    886  SD  MET A 564      -5.162 -15.037 -15.424  1.00 44.64           S  
-ANISOU  886  SD  MET A 564     7096   4993   4874    117    356   -120       S  
-ATOM    887  CE  MET A 564      -6.641 -15.851 -16.025  1.00 30.59           C  
-ANISOU  887  CE  MET A 564     5304   3202   3115     43    461   -100       C  
-ATOM    888  N   ASP A 565      -7.323 -16.199 -10.532  1.00 48.40           N  
-ANISOU  888  N   ASP A 565     8313   5006   5071    -48    589   -142       N  
-ATOM    889  CA  ASP A 565      -8.473 -16.552  -9.711  1.00 51.93           C  
-ANISOU  889  CA  ASP A 565     8899   5360   5474   -137    707   -141       C  
-ATOM    890  C   ASP A 565      -9.282 -15.311  -9.350  1.00 50.67           C  
-ANISOU  890  C   ASP A 565     8659   5209   5383   -202    821   -134       C  
-ATOM    891  O   ASP A 565     -10.511 -15.354  -9.307  1.00 52.23           O  
-ANISOU  891  O   ASP A 565     8853   5384   5608   -286    942   -133       O  
-ATOM    892  CB  ASP A 565      -8.032 -17.277  -8.439  1.00 61.71           C  
-ANISOU  892  CB  ASP A 565    10390   6478   6578   -126    664   -159       C  
-ATOM    893  CG  ASP A 565      -9.205 -17.723  -7.588  1.00 67.56           C  
-ANISOU  893  CG  ASP A 565    11288   7121   7262   -226    788   -161       C  
-ATOM    894  OD1 ASP A 565     -10.321 -17.862  -8.132  1.00 63.24           O  
-ANISOU  894  OD1 ASP A 565    10665   6594   6770   -296    893   -154       O  
-ATOM    895  OD2 ASP A 565      -9.010 -17.936  -6.374  1.00 75.07           O  
-ANISOU  895  OD2 ASP A 565    12438   7974   8112   -238    781   -171       O  
-ATOM    896  N   TYR A 566      -8.588 -14.206  -9.088  1.00 45.55           N  
-ANISOU  896  N   TYR A 566     7946   4593   4767   -162    780   -133       N  
-ATOM    897  CA  TYR A 566      -9.254 -12.945  -8.788  1.00 37.59           C  
-ANISOU  897  CA  TYR A 566     6848   3599   3836   -215    875   -129       C  
-ATOM    898  C   TYR A 566     -10.070 -12.477  -9.984  1.00 53.30           C  
-ANISOU  898  C   TYR A 566     8627   5675   5949   -248    936   -109       C  
-ATOM    899  O   TYR A 566     -11.224 -12.071  -9.839  1.00 62.88           O  
-ANISOU  899  O   TYR A 566     9805   6873   7215   -324   1052   -112       O  
-ATOM    900  CB  TYR A 566      -8.241 -11.866  -8.399  1.00 38.50           C  
-ANISOU  900  CB  TYR A 566     6921   3740   3969   -157    805   -132       C  
-ATOM    901  CG  TYR A 566      -8.856 -10.495  -8.202  1.00 47.98           C  
-ANISOU  901  CG  TYR A 566     8006   4961   5261   -203    891   -127       C  
-ATOM    902  CD1 TYR A 566      -9.421 -10.132  -6.984  1.00 51.63           C  
-ANISOU  902  CD1 TYR A 566     8581   5345   5691   -260    975   -148       C  
-ATOM    903  CD2 TYR A 566      -8.873  -9.565  -9.233  1.00 45.14           C  
-ANISOU  903  CD2 TYR A 566     7430   4699   5023   -191    886   -105       C  
-ATOM    904  CE1 TYR A 566      -9.986  -8.881  -6.800  1.00 39.67           C  
-ANISOU  904  CE1 TYR A 566     6958   3849   4267   -301   1051   -150       C  
-ATOM    905  CE2 TYR A 566      -9.435  -8.313  -9.058  1.00 42.95           C  
-ANISOU  905  CE2 TYR A 566     7050   4435   4835   -230    957   -102       C  
-ATOM    906  CZ  TYR A 566      -9.990  -7.976  -7.840  1.00 40.82           C  
-ANISOU  906  CZ  TYR A 566     6887   4087   4537   -283   1039   -127       C  
-ATOM    907  OH  TYR A 566     -10.549  -6.731  -7.663  1.00 45.75           O  
-ANISOU  907  OH  TYR A 566     7403   4722   5256   -320   1106   -131       O  
-ATOM    908  N   LEU A 567      -9.460 -12.535 -11.165  1.00 55.54           N  
-ANISOU  908  N   LEU A 567     8774   6050   6279   -192    854    -92       N  
-ATOM    909  CA  LEU A 567     -10.124 -12.109 -12.392  1.00 48.74           C  
-ANISOU  909  CA  LEU A 567     7713   5277   5529   -217    895    -69       C  
-ATOM    910  C   LEU A 567     -11.416 -12.885 -12.625  1.00 40.39           C  
-ANISOU  910  C   LEU A 567     6679   4190   4478   -288    994    -74       C  
-ATOM    911  O   LEU A 567     -12.457 -12.297 -12.913  1.00 47.85           O  
-ANISOU  911  O   LEU A 567     7520   5154   5508   -346   1086    -70       O  
-ATOM    912  CB  LEU A 567      -9.192 -12.259 -13.600  1.00 42.84           C  
-ANISOU  912  CB  LEU A 567     6841   4629   4808   -148    787    -55       C  
-ATOM    913  CG  LEU A 567      -7.979 -11.328 -13.684  1.00 44.89           C  
-ANISOU  913  CG  LEU A 567     7022   4945   5091    -83    695    -50       C  
-ATOM    914  CD1 LEU A 567      -7.189 -11.582 -14.961  1.00 35.99           C  
-ANISOU  914  CD1 LEU A 567     5767   3920   3987    -30    603    -42       C  
-ATOM    915  CD2 LEU A 567      -8.407  -9.871 -13.602  1.00 38.68           C  
-ANISOU  915  CD2 LEU A 567     6117   4181   4397   -116    753    -32       C  
-ATOM    916  N   HIS A 568     -11.343 -14.205 -12.491  1.00 46.97           N  
-ANISOU  916  N   HIS A 568     7649   4974   5223   -284    973    -87       N  
-ATOM    917  CA  HIS A 568     -12.501 -15.063 -12.720  1.00 52.41           C  
-ANISOU  917  CA  HIS A 568     8370   5633   5910   -351   1063    -95       C  
-ATOM    918  C   HIS A 568     -13.557 -14.917 -11.628  1.00 61.62           C  
-ANISOU  918  C   HIS A 568     9646   6710   7056   -439   1190   -117       C  
-ATOM    919  O   HIS A 568     -14.749 -15.084 -11.884  1.00 62.65           O  
-ANISOU  919  O   HIS A 568     9737   6836   7233   -509   1294   -128       O  
-ATOM    920  CB  HIS A 568     -12.069 -16.523 -12.856  1.00 46.11           C  
-ANISOU  920  CB  HIS A 568     7694   4802   5021   -320    999   -104       C  
-ATOM    921  CG  HIS A 568     -11.301 -16.808 -14.109  1.00 37.59           C  
-ANISOU  921  CG  HIS A 568     6488   3821   3975   -250    896    -92       C  
-ATOM    922  ND1 HIS A 568     -10.561 -17.957 -14.282  1.00 40.71           N  
-ANISOU  922  ND1 HIS A 568     6971   4201   4297   -198    803   -104       N  
-ATOM    923  CD2 HIS A 568     -11.160 -16.094 -15.250  1.00 35.97           C  
-ANISOU  923  CD2 HIS A 568     6074   3728   3866   -227    870    -72       C  
-ATOM    924  CE1 HIS A 568      -9.998 -17.939 -15.478  1.00 49.81           C  
-ANISOU  924  CE1 HIS A 568     7969   5457   5500   -147    729    -97       C  
-ATOM    925  NE2 HIS A 568     -10.346 -16.819 -16.085  1.00 43.06           N  
-ANISOU  925  NE2 HIS A 568     6935   4681   4743   -166    770    -75       N  
-ATOM    926  N   ALA A 569     -13.115 -14.616 -10.411  1.00 59.26           N  
-ANISOU  926  N   ALA A 569     9485   6343   6690   -436   1183   -129       N  
-ATOM    927  CA  ALA A 569     -14.039 -14.299  -9.329  1.00 50.33           C  
-ANISOU  927  CA  ALA A 569     8446   5134   5541   -522   1304   -154       C  
-ATOM    928  C   ALA A 569     -14.805 -13.038  -9.707  1.00 54.58           C  
-ANISOU  928  C   ALA A 569     8796   5729   6213   -558   1380   -155       C  
-ATOM    929  O   ALA A 569     -15.964 -12.860  -9.333  1.00 50.68           O  
-ANISOU  929  O   ALA A 569     8305   5200   5750   -642   1502   -182       O  
-ATOM    930  CB  ALA A 569     -13.289 -14.101  -8.028  1.00 52.96           C  
-ANISOU  930  CB  ALA A 569     8947   5395   5779   -503   1267   -164       C  
-ATOM    931  N   LYS A 570     -14.137 -12.166 -10.455  1.00 63.44           N  
-ANISOU  931  N   LYS A 570     9754   6937   7413   -495   1304   -129       N  
-ATOM    932  CA  LYS A 570     -14.761 -10.972 -11.005  1.00 58.91           C  
-ANISOU  932  CA  LYS A 570     8987   6424   6973   -517   1352   -123       C  
-ATOM    933  C   LYS A 570     -15.380 -11.294 -12.361  1.00 64.60           C  
-ANISOU  933  C   LYS A 570     9560   7215   7772   -525   1363   -108       C  
-ATOM    934  O   LYS A 570     -15.747 -10.394 -13.118  1.00 58.73           O  
-ANISOU  934  O   LYS A 570     8637   6536   7141   -527   1373    -93       O  
-ATOM    935  CB  LYS A 570     -13.727  -9.856 -11.157  1.00 56.21           C  
-ANISOU  935  CB  LYS A 570     8545   6137   6674   -450   1263    -99       C  
-ATOM    936  CG  LYS A 570     -13.172  -9.329  -9.843  1.00 60.28           C  
-ANISOU  936  CG  LYS A 570     9180   6590   7132   -441   1256   -117       C  
-ATOM    937  CD  LYS A 570     -14.172  -8.433  -9.135  1.00 61.05           C  
-ANISOU  937  CD  LYS A 570     9256   6651   7290   -513   1371   -145       C  
-ATOM    938  CE  LYS A 570     -13.504  -7.662  -8.009  1.00 64.13           C  
-ANISOU  938  CE  LYS A 570     9721   7001   7643   -495   1350   -159       C  
-ATOM    939  NZ  LYS A 570     -14.385  -6.602  -7.451  1.00 73.65           N  
-ANISOU  939  NZ  LYS A 570    10869   8186   8929   -556   1450   -187       N  
-ATOM    940  N   SER A 571     -15.486 -12.588 -12.656  1.00 66.45           N  
-ANISOU  940  N   SER A 571     9874   7433   7942   -529   1357   -112       N  
-ATOM    941  CA  SER A 571     -16.028 -13.071 -13.926  1.00 73.17           C  
-ANISOU  941  CA  SER A 571    10601   8347   8852   -535   1363   -101       C  
-ATOM    942  C   SER A 571     -15.375 -12.402 -15.135  1.00 74.39           C  
-ANISOU  942  C   SER A 571    10568   8613   9085   -473   1273    -63       C  
-ATOM    943  O   SER A 571     -16.052 -12.039 -16.097  1.00 78.42           O  
-ANISOU  943  O   SER A 571    10920   9186   9692   -491   1300    -52       O  
-ATOM    944  CB  SER A 571     -17.551 -12.899 -13.970  1.00116.67           C  
-ANISOU  944  CB  SER A 571    16053  13840  14437   -621   1495   -129       C  
-ATOM    945  OG  SER A 571     -17.916 -11.529 -13.909  1.00130.12           O  
-ANISOU  945  OG  SER A 571    17631  15566  16241   -636   1529   -130       O  
-ATOM    946  N   ILE A 572     -14.056 -12.250 -15.080  1.00 64.70           N  
-ANISOU  946  N   ILE A 572     9360   7410   7813   -401   1165    -46       N  
-ATOM    947  CA  ILE A 572     -13.309 -11.641 -16.174  1.00 45.23           C  
-ANISOU  947  CA  ILE A 572     6729   5049   5407   -345   1076    -12       C  
-ATOM    948  C   ILE A 572     -12.401 -12.654 -16.864  1.00 43.85           C  
-ANISOU  948  C   ILE A 572     6571   4918   5172   -287    978     -8       C  
-ATOM    949  O   ILE A 572     -11.472 -13.187 -16.258  1.00 40.59           O  
-ANISOU  949  O   ILE A 572     6286   4466   4670   -242    912    -22       O  
-ATOM    950  CB  ILE A 572     -12.463 -10.448 -15.688  1.00 48.65           C  
-ANISOU  950  CB  ILE A 572     7135   5493   5859   -309   1028     -1       C  
-ATOM    951  CG1 ILE A 572     -13.367  -9.342 -15.143  1.00 49.99           C  
-ANISOU  951  CG1 ILE A 572     7259   5629   6105   -364   1120     -7       C  
-ATOM    952  CG2 ILE A 572     -11.589  -9.917 -16.816  1.00 32.13           C  
-ANISOU  952  CG2 ILE A 572     4885   3507   3814   -255    934     31       C  
-ATOM    953  CD1 ILE A 572     -12.618  -8.138 -14.610  1.00 40.33           C  
-ANISOU  953  CD1 ILE A 572     6009   4409   4904   -334   1081      1       C  
-ATOM    954  N   ILE A 573     -12.682 -12.919 -18.135  1.00 58.20           N  
-ANISOU  954  N   ILE A 573     8258   6815   7041   -286    967      8       N  
-ATOM    955  CA  ILE A 573     -11.855 -13.818 -18.927  1.00 54.52           C  
-ANISOU  955  CA  ILE A 573     7780   6404   6531   -233    875      7       C  
-ATOM    956  C   ILE A 573     -10.711 -13.033 -19.558  1.00 63.01           C  
-ANISOU  956  C   ILE A 573     8736   7571   7635   -177    778     28       C  
-ATOM    957  O   ILE A 573     -10.942 -12.140 -20.374  1.00 72.21           O  
-ANISOU  957  O   ILE A 573     9742   8811   8886   -189    785     58       O  
-ATOM    958  CB  ILE A 573     -12.673 -14.490 -20.044  1.00 45.11           C  
-ANISOU  958  CB  ILE A 573     6499   5262   5379   -261    907     11       C  
-ATOM    959  CG1 ILE A 573     -13.990 -15.035 -19.487  1.00 38.19           C  
-ANISOU  959  CG1 ILE A 573     5710   4302   4498   -331   1023    -11       C  
-ATOM    960  CG2 ILE A 573     -11.865 -15.596 -20.708  1.00 43.16           C  
-ANISOU  960  CG2 ILE A 573     6266   5057   5075   -210    819      0       C  
-ATOM    961  CD1 ILE A 573     -14.915 -15.598 -20.546  1.00 43.39           C  
-ANISOU  961  CD1 ILE A 573     6272   5008   5207   -364   1065    -11       C  
-ATOM    962  N   HIS A 574      -9.480 -13.359 -19.179  1.00 46.60           N  
-ANISOU  962  N   HIS A 574     6738   5485   5485   -116    687     10       N  
-ATOM    963  CA  HIS A 574      -8.323 -12.667 -19.735  1.00 42.74           C  
-ANISOU  963  CA  HIS A 574     6140   5081   5017    -64    596     20       C  
-ATOM    964  C   HIS A 574      -8.312 -12.783 -21.255  1.00 39.32           C  
-ANISOU  964  C   HIS A 574     5543   4764   4633    -62    566     38       C  
-ATOM    965  O   HIS A 574      -8.099 -11.798 -21.960  1.00 46.55           O  
-ANISOU  965  O   HIS A 574     6314   5759   5613    -64    549     67       O  
-ATOM    966  CB  HIS A 574      -7.019 -13.219 -19.160  1.00 34.40           C  
-ANISOU  966  CB  HIS A 574     5197   3999   3874      5    497    -16       C  
-ATOM    967  CG  HIS A 574      -5.818 -12.393 -19.501  1.00 38.95           C  
-ANISOU  967  CG  HIS A 574     5676   4652   4472     53    413    -16       C  
-ATOM    968  ND1 HIS A 574      -5.332 -12.280 -20.785  1.00 38.31           N  
-ANISOU  968  ND1 HIS A 574     5440   4687   4428     69    361     -8       N  
-ATOM    969  CD2 HIS A 574      -5.006 -11.637 -18.723  1.00 37.26           C  
-ANISOU  969  CD2 HIS A 574     5497   4416   4245     85    374    -27       C  
-ATOM    970  CE1 HIS A 574      -4.272 -11.489 -20.785  1.00 33.88           C  
-ANISOU  970  CE1 HIS A 574     4823   4172   3877    106    297    -14       C  
-ATOM    971  NE2 HIS A 574      -4.054 -11.087 -19.547  1.00 31.08           N  
-ANISOU  971  NE2 HIS A 574     4579   3734   3494    119    302    -26       N  
-ATOM    972  N   ARG A 575      -8.536 -14.002 -21.742  1.00 52.34           N  
-ANISOU  972  N   ARG A 575     7220   6418   6247    -60    560     20       N  
-ATOM    973  CA  ARG A 575      -8.629 -14.296 -23.176  1.00 44.49           C  
-ANISOU  973  CA  ARG A 575     6084   5530   5292    -62    538     32       C  
-ATOM    974  C   ARG A 575      -7.287 -14.398 -23.900  1.00 35.22           C  
-ANISOU  974  C   ARG A 575     4838   4448   4097     -5    429     16       C  
-ATOM    975  O   ARG A 575      -7.225 -14.903 -25.019  1.00 28.88           O  
-ANISOU  975  O   ARG A 575     3942   3728   3304     -1    401     13       O  
-ATOM    976  CB  ARG A 575      -9.546 -13.298 -23.892  1.00 40.42           C  
-ANISOU  976  CB  ARG A 575     5418   5067   4873   -113    600     76       C  
-ATOM    977  CG  ARG A 575     -11.022 -13.525 -23.629  1.00 40.47           C  
-ANISOU  977  CG  ARG A 575     5456   5009   4910   -173    708     78       C  
-ATOM    978  CD  ARG A 575     -11.895 -12.583 -24.443  1.00 38.39           C  
-ANISOU  978  CD  ARG A 575     5035   4801   4748   -216    754    116       C  
-ATOM    979  NE  ARG A 575     -13.314 -12.801 -24.179  1.00 54.08           N  
-ANISOU  979  NE  ARG A 575     7047   6728   6772   -272    857    107       N  
-ATOM    980  CZ  ARG A 575     -13.962 -12.309 -23.127  1.00 69.49           C  
-ANISOU  980  CZ  ARG A 575     9069   8593   8741   -307    931     97       C  
-ATOM    981  NH1 ARG A 575     -13.317 -11.571 -22.233  1.00 67.95           N  
-ANISOU  981  NH1 ARG A 575     8928   8360   8529   -288    912     99       N  
-ATOM    982  NH2 ARG A 575     -15.255 -12.558 -22.964  1.00 77.59           N  
-ANISOU  982  NH2 ARG A 575    10107   9571   9802   -362   1026     80       N  
-ATOM    983  N   ASP A 576      -6.220 -13.921 -23.267  1.00 45.09           N  
-ANISOU  983  N   ASP A 576     6130   5686   5318     39    368      0       N  
-ATOM    984  CA  ASP A 576      -4.894 -13.988 -23.875  1.00 48.34           C  
-ANISOU  984  CA  ASP A 576     6474   6183   5711     92    265    -26       C  
-ATOM    985  C   ASP A 576      -3.793 -13.978 -22.821  1.00 37.16           C  
-ANISOU  985  C   ASP A 576     5173   4710   4237    149    196    -66       C  
-ATOM    986  O   ASP A 576      -2.904 -13.129 -22.848  1.00 40.42           O  
-ANISOU  986  O   ASP A 576     5523   5171   4666    174    149    -70       O  
-ATOM    987  CB  ASP A 576      -4.694 -12.836 -24.866  1.00 50.01           C  
-ANISOU  987  CB  ASP A 576     6504   6506   5992     72    258     11       C  
-ATOM    988  CG  ASP A 576      -3.429 -12.989 -25.697  1.00 50.47           C  
-ANISOU  988  CG  ASP A 576     6475   6669   6033    113    163    -21       C  
-ATOM    989  OD1 ASP A 576      -3.187 -12.138 -26.579  1.00 64.09           O  
-ANISOU  989  OD1 ASP A 576     8056   8491   7805     93    154      6       O  
-ATOM    990  OD2 ASP A 576      -2.675 -13.958 -25.474  1.00 50.57           O  
-ANISOU  990  OD2 ASP A 576     6563   6666   5985    165     97    -77       O  
-ATOM    991  N   LEU A 577      -3.858 -14.920 -21.887  1.00 34.52           N  
-ANISOU  991  N   LEU A 577     5010   4273   3834    169    190    -96       N  
-ATOM    992  CA  LEU A 577      -2.804 -15.063 -20.894  1.00 33.06           C  
-ANISOU  992  CA  LEU A 577     4947   4029   3586    230    113   -138       C  
-ATOM    993  C   LEU A 577      -1.588 -15.738 -21.514  1.00 37.04           C  
-ANISOU  993  C   LEU A 577     5413   4599   4062    295     -2   -193       C  
-ATOM    994  O   LEU A 577      -1.683 -16.836 -22.065  1.00 34.56           O  
-ANISOU  994  O   LEU A 577     5106   4298   3726    305    -25   -215       O  
-ATOM    995  CB  LEU A 577      -3.289 -15.866 -19.685  1.00 33.69           C  
-ANISOU  995  CB  LEU A 577     5234   3971   3596    226    141   -150       C  
-ATOM    996  CG  LEU A 577      -2.233 -16.066 -18.591  1.00 34.04           C  
-ANISOU  996  CG  LEU A 577     5422   3943   3568    290     55   -194       C  
-ATOM    997  CD1 LEU A 577      -1.856 -14.734 -17.960  1.00 27.83           C  
-ANISOU  997  CD1 LEU A 577     4612   3155   2808    293     62   -182       C  
-ATOM    998  CD2 LEU A 577      -2.709 -17.050 -17.532  1.00 27.80           C  
-ANISOU  998  CD2 LEU A 577     4846   3019   2698    283     73   -204       C  
-ATOM    999  N   LYS A 578      -0.450 -15.060 -21.430  1.00 46.90           N  
-ANISOU  999  N   LYS A 578     6613   5891   5315    338    -72   -218       N  
-ATOM   1000  CA  LYS A 578       0.821 -15.598 -21.899  1.00 41.77           C  
-ANISOU 1000  CA  LYS A 578     5926   5302   4641    404   -185   -284       C  
-ATOM   1001  C   LYS A 578       1.959 -14.920 -21.143  1.00 43.46           C  
-ANISOU 1001  C   LYS A 578     6170   5503   4841    455   -253   -320       C  
-ATOM   1002  O   LYS A 578       1.745 -13.909 -20.475  1.00 48.11           O  
-ANISOU 1002  O   LYS A 578     6774   6056   5449    433   -207   -286       O  
-ATOM   1003  CB  LYS A 578       0.971 -15.410 -23.412  1.00 36.32           C  
-ANISOU 1003  CB  LYS A 578     5040   4756   4003    383   -191   -279       C  
-ATOM   1004  CG  LYS A 578       0.444 -14.086 -23.937  1.00 43.85           C  
-ANISOU 1004  CG  LYS A 578     5859   5775   5029    321   -117   -213       C  
-ATOM   1005  CD  LYS A 578       0.702 -13.939 -25.430  1.00 52.39           C  
-ANISOU 1005  CD  LYS A 578     6759   6999   6150    300   -133   -211       C  
-ATOM   1006  CE  LYS A 578       0.275 -12.564 -25.925  1.00 59.49           C  
-ANISOU 1006  CE  LYS A 578     7532   7957   7117    241    -73   -144       C  
-ATOM   1007  NZ  LYS A 578       0.840 -12.249 -27.270  1.00 61.36           N  
-ANISOU 1007  NZ  LYS A 578     7599   8335   7380    225   -104   -147       N  
-ATOM   1008  N   SER A 579       3.163 -15.474 -21.247  1.00 42.58           N  
-ANISOU 1008  N   SER A 579     6061   5418   4699    524   -364   -394       N  
-ATOM   1009  CA  SER A 579       4.289 -15.010 -20.436  1.00 44.37           C  
-ANISOU 1009  CA  SER A 579     6335   5620   4905    583   -441   -443       C  
-ATOM   1010  C   SER A 579       4.683 -13.556 -20.697  1.00 54.00           C  
-ANISOU 1010  C   SER A 579     7418   6918   6183    560   -419   -423       C  
-ATOM   1011  O   SER A 579       5.289 -12.914 -19.840  1.00 58.15           O  
-ANISOU 1011  O   SER A 579     7990   7405   6700    591   -448   -442       O  
-ATOM   1012  CB  SER A 579       5.505 -15.922 -20.615  1.00 46.83           C  
-ANISOU 1012  CB  SER A 579     6659   5953   5181    663   -569   -537       C  
-ATOM   1013  OG  SER A 579       6.105 -15.729 -21.883  1.00 56.40           O  
-ANISOU 1013  OG  SER A 579     7686   7307   6438    660   -598   -566       O  
-ATOM   1014  N   ASN A 580       4.345 -13.040 -21.875  1.00 48.06           N  
-ANISOU 1014  N   ASN A 580     6499   6273   5489    507   -371   -384       N  
-ATOM   1015  CA  ASN A 580       4.670 -11.654 -22.207  1.00 41.16           C  
-ANISOU 1015  CA  ASN A 580     5494   5474   4672    477   -349   -358       C  
-ATOM   1016  C   ASN A 580       3.594 -10.661 -21.772  1.00 45.61           C  
-ANISOU 1016  C   ASN A 580     6066   5989   5276    416   -246   -275       C  
-ATOM   1017  O   ASN A 580       3.787  -9.448 -21.860  1.00 43.63           O  
-ANISOU 1017  O   ASN A 580     5728   5777   5073    392   -225   -249       O  
-ATOM   1018  CB  ASN A 580       5.002 -11.495 -23.696  1.00 60.25           C  
-ANISOU 1018  CB  ASN A 580     7728   8037   7129    450   -359   -361       C  
-ATOM   1019  CG  ASN A 580       4.355 -12.560 -24.559  1.00 80.20           C  
-ANISOU 1019  CG  ASN A 580    10234  10594   9646    431   -344   -355       C  
-ATOM   1020  OD1 ASN A 580       4.876 -13.666 -24.699  1.00 87.65           O  
-ANISOU 1020  OD1 ASN A 580    11213  11541  10550    479   -413   -420       O  
-ATOM   1021  ND2 ASN A 580       3.219 -12.225 -25.155  1.00 88.15           N  
-ANISOU 1021  ND2 ASN A 580    11178  11623  10693    362   -256   -279       N  
-ATOM   1022  N   ASN A 581       2.464 -11.182 -21.304  1.00 42.76           N  
-ANISOU 1022  N   ASN A 581     5809   5540   4896    390   -181   -240       N  
-ATOM   1023  CA  ASN A 581       1.432 -10.349 -20.695  1.00 45.33           C  
-ANISOU 1023  CA  ASN A 581     6164   5803   5255    338    -86   -177       C  
-ATOM   1024  C   ASN A 581       1.472 -10.490 -19.177  1.00 49.25           C  
-ANISOU 1024  C   ASN A 581     6842   6174   5699    367    -90   -198       C  
-ATOM   1025  O   ASN A 581       0.509 -10.180 -18.476  1.00 46.96           O  
-ANISOU 1025  O   ASN A 581     6621   5807   5415    326     -8   -160       O  
-ATOM   1026  CB  ASN A 581       0.047 -10.684 -21.254  1.00 47.07           C  
-ANISOU 1026  CB  ASN A 581     6360   6021   5503    276      2   -124       C  
-ATOM   1027  CG  ASN A 581      -0.184 -10.088 -22.633  1.00 53.25           C  
-ANISOU 1027  CG  ASN A 581     6957   6921   6353    232     24    -83       C  
-ATOM   1028  OD1 ASN A 581       0.609  -9.278 -23.113  1.00 53.67           O  
-ANISOU 1028  OD1 ASN A 581     6902   7054   6438    236    -13    -86       O  
-ATOM   1029  ND2 ASN A 581      -1.278 -10.485 -23.273  1.00 61.81           N  
-ANISOU 1029  ND2 ASN A 581     8008   8017   7462    186     85    -47       N  
-ATOM   1030  N   ILE A 582       2.614 -10.969 -18.692  1.00 43.11           N  
-ANISOU 1030  N   ILE A 582     6137   5377   4866    438   -187   -264       N  
-ATOM   1031  CA  ILE A 582       2.896 -11.083 -17.270  1.00 27.88           C  
-ANISOU 1031  CA  ILE A 582     4380   3336   2879    477   -213   -292       C  
-ATOM   1032  C   ILE A 582       4.189 -10.331 -16.982  1.00 43.13           C  
-ANISOU 1032  C   ILE A 582     6270   5300   4817    529   -291   -338       C  
-ATOM   1033  O   ILE A 582       5.265 -10.752 -17.407  1.00 49.74           O  
-ANISOU 1033  O   ILE A 582     7068   6192   5640    584   -386   -399       O  
-ATOM   1034  CB  ILE A 582       3.077 -12.552 -16.856  1.00 39.62           C  
-ANISOU 1034  CB  ILE A 582     6022   4750   4283    523   -275   -336       C  
-ATOM   1035  CG1 ILE A 582       1.767 -13.322 -17.033  1.00 40.95           C  
-ANISOU 1035  CG1 ILE A 582     6245   4875   4440    468   -193   -294       C  
-ATOM   1036  CG2 ILE A 582       3.568 -12.647 -15.420  1.00 39.54           C  
-ANISOU 1036  CG2 ILE A 582     6190   4630   4205    570   -323   -371       C  
-ATOM   1037  CD1 ILE A 582       1.905 -14.814 -16.830  1.00 30.92           C  
-ANISOU 1037  CD1 ILE A 582     5111   3543   3095    507   -253   -333       C  
-ATOM   1038  N   PHE A 583       4.082  -9.214 -16.270  1.00 52.23           N  
-ANISOU 1038  N   PHE A 583     7427   6420   5996    511   -249   -314       N  
-ATOM   1039  CA  PHE A 583       5.238  -8.359 -16.018  1.00 57.81           C  
-ANISOU 1039  CA  PHE A 583     8083   7163   6721    552   -311   -355       C  
-ATOM   1040  C   PHE A 583       5.777  -8.540 -14.604  1.00 64.55           C  
-ANISOU 1040  C   PHE A 583     9105   7913   7508    609   -364   -401       C  
-ATOM   1041  O   PHE A 583       5.042  -8.408 -13.626  1.00 64.82           O  
-ANISOU 1041  O   PHE A 583     9260   7853   7518    584   -305   -371       O  
-ATOM   1042  CB  PHE A 583       4.874  -6.894 -16.270  1.00 62.02           C  
-ANISOU 1042  CB  PHE A 583     8489   7740   7336    496   -238   -300       C  
-ATOM   1043  CG  PHE A 583       4.099  -6.678 -17.539  1.00 70.19           C  
-ANISOU 1043  CG  PHE A 583     9380   8856   8432    431   -175   -242       C  
-ATOM   1044  CD1 PHE A 583       2.715  -6.603 -17.517  1.00 63.85           C  
-ANISOU 1044  CD1 PHE A 583     8594   8011   7654    369    -76   -179       C  
-ATOM   1045  CD2 PHE A 583       4.751  -6.573 -18.756  1.00 71.76           C  
-ANISOU 1045  CD2 PHE A 583     9429   9174   8663    432   -216   -254       C  
-ATOM   1046  CE1 PHE A 583       1.997  -6.416 -18.684  1.00 54.12           C  
-ANISOU 1046  CE1 PHE A 583     7232   6851   6479    313    -25   -127       C  
-ATOM   1047  CE2 PHE A 583       4.039  -6.385 -19.927  1.00 66.81           C  
-ANISOU 1047  CE2 PHE A 583     8677   8620   8087    371   -163   -199       C  
-ATOM   1048  CZ  PHE A 583       2.660  -6.307 -19.890  1.00 55.36           C  
-ANISOU 1048  CZ  PHE A 583     7246   7124   6662    315    -71   -134       C  
-ATOM   1049  N   LEU A 584       7.066  -8.852 -14.504  1.00 62.51           N  
-ANISOU 1049  N   LEU A 584     8857   7674   7220    685   -477   -477       N  
-ATOM   1050  CA  LEU A 584       7.716  -9.004 -13.209  1.00 60.66           C  
-ANISOU 1050  CA  LEU A 584     8777   7347   6923    747   -545   -528       C  
-ATOM   1051  C   LEU A 584       8.199  -7.661 -12.683  1.00 70.65           C  
-ANISOU 1051  C   LEU A 584     9991   8623   8228    750   -537   -534       C  
-ATOM   1052  O   LEU A 584       9.359  -7.292 -12.875  1.00 74.13           O  
-ANISOU 1052  O   LEU A 584    10355   9123   8690    798   -614   -593       O  
-ATOM   1053  CB  LEU A 584       8.892  -9.979 -13.299  1.00 66.22           C  
-ANISOU 1053  CB  LEU A 584     9519   8060   7582    835   -680   -618       C  
-ATOM   1054  CG  LEU A 584       8.551 -11.463 -13.427  1.00 79.53           C  
-ANISOU 1054  CG  LEU A 584    11312   9698   9208    851   -713   -627       C  
-ATOM   1055  CD1 LEU A 584       9.808 -12.315 -13.324  1.00 79.10           C  
-ANISOU 1055  CD1 LEU A 584    11305   9637   9111    948   -860   -726       C  
-ATOM   1056  CD2 LEU A 584       7.549 -11.865 -12.359  1.00 86.11           C  
-ANISOU 1056  CD2 LEU A 584    12339  10400   9978    822   -654   -581       C  
-ATOM   1057  N   HIS A 585       7.307  -6.931 -12.019  1.00 73.69           N  
-ANISOU 1057  N   HIS A 585    10418   8953   8629    697   -443   -477       N  
-ATOM   1058  CA  HIS A 585       7.657  -5.635 -11.450  1.00 73.41           C  
-ANISOU 1058  CA  HIS A 585    10341   8918   8634    696   -428   -479       C  
-ATOM   1059  C   HIS A 585       8.661  -5.779 -10.313  1.00 76.53           C  
-ANISOU 1059  C   HIS A 585    10862   9249   8967    774   -522   -551       C  
-ATOM   1060  O   HIS A 585       8.411  -6.487  -9.338  1.00 75.95           O  
-ANISOU 1060  O   HIS A 585    10971   9072   8814    794   -536   -560       O  
-ATOM   1061  CB  HIS A 585       6.414  -4.897 -10.954  1.00 66.75           C  
-ANISOU 1061  CB  HIS A 585     9520   8023   7820    622   -306   -409       C  
-ATOM   1062  CG  HIS A 585       6.724  -3.665 -10.164  1.00 58.24           C  
-ANISOU 1062  CG  HIS A 585     8429   6925   6774    624   -293   -416       C  
-ATOM   1063  ND1 HIS A 585       7.500  -2.641 -10.661  1.00 54.40           N  
-ANISOU 1063  ND1 HIS A 585     7791   6520   6357    632   -318   -430       N  
-ATOM   1064  CD2 HIS A 585       6.365  -3.293  -8.913  1.00 60.57           C  
-ANISOU 1064  CD2 HIS A 585     8844   7130   7041    616   -256   -413       C  
-ATOM   1065  CE1 HIS A 585       7.608  -1.691  -9.750  1.00 55.63           C  
-ANISOU 1065  CE1 HIS A 585     7972   6635   6530    633   -298   -436       C  
-ATOM   1066  NE2 HIS A 585       6.927  -2.062  -8.680  1.00 58.31           N  
-ANISOU 1066  NE2 HIS A 585     8473   6871   6810    624   -261   -427       N  
-ATOM   1067  N   GLU A 586       9.794  -5.096 -10.447  1.00 75.48           N  
-ANISOU 1067  N   GLU A 586    10633   9176   8869    816   -586   -603       N  
-ATOM   1068  CA  GLU A 586      10.874  -5.189  -9.474  1.00 83.25           C  
-ANISOU 1068  CA  GLU A 586    11716  10112   9804    898   -688   -683       C  
-ATOM   1069  C   GLU A 586      11.462  -6.599  -9.477  1.00 84.43           C  
-ANISOU 1069  C   GLU A 586    11964  10234   9880    969   -797   -745       C  
-ATOM   1070  O   GLU A 586      12.310  -6.934  -8.649  1.00 80.72           O  
-ANISOU 1070  O   GLU A 586    11603   9709   9357   1045   -896   -814       O  
-ATOM   1071  CB  GLU A 586      10.376  -4.810  -8.077  1.00107.05           C  
-ANISOU 1071  CB  GLU A 586    14880  13016  12777    888   -646   -662       C  
-ATOM   1072  CG  GLU A 586      11.471  -4.660  -7.035  1.00119.50           C  
-ANISOU 1072  CG  GLU A 586    16545  14547  14311    968   -744   -739       C  
-ATOM   1073  CD  GLU A 586      10.922  -4.279  -5.677  1.00126.14           C  
-ANISOU 1073  CD  GLU A 586    17534  15283  15108    951   -695   -717       C  
-ATOM   1074  OE1 GLU A 586       9.716  -3.968  -5.592  1.00126.77           O  
-ANISOU 1074  OE1 GLU A 586    17624  15338  15205    872   -578   -644       O  
-ATOM   1075  OE2 GLU A 586      11.695  -4.288  -4.696  1.00128.89           O  
-ANISOU 1075  OE2 GLU A 586    17989  15578  15406   1015   -775   -776       O  
-ATOM   1076  N   ASP A 587      11.002  -7.415 -10.422  1.00 99.83           N  
-ANISOU 1076  N   ASP A 587    13876  12221  11832    944   -782   -721       N  
-ATOM   1077  CA  ASP A 587      11.488  -8.782 -10.598  1.00 95.84           C  
-ANISOU 1077  CA  ASP A 587    13446  11697  11270   1006   -882   -778       C  
-ATOM   1078  C   ASP A 587      11.031  -9.714  -9.477  1.00 80.77           C  
-ANISOU 1078  C   ASP A 587    11773   9651   9265   1026   -902   -771       C  
-ATOM   1079  O   ASP A 587      11.506 -10.844  -9.367  1.00 79.22           O  
-ANISOU 1079  O   ASP A 587    11674   9414   9011   1088  -1001   -823       O  
-ATOM   1080  CB  ASP A 587      13.015  -8.810 -10.729  1.00 98.14           C  
-ANISOU 1080  CB  ASP A 587    13679  12041  11570   1092  -1012   -885       C  
-ATOM   1081  CG  ASP A 587      13.524  -7.915 -11.844  1.00 93.37           C  
-ANISOU 1081  CG  ASP A 587    12846  11575  11054   1065   -992   -898       C  
-ATOM   1082  OD1 ASP A 587      13.095  -6.745 -11.911  1.00 98.37           O  
-ANISOU 1082  OD1 ASP A 587    13395  12238  11742   1004   -902   -840       O  
-ATOM   1083  OD2 ASP A 587      14.359  -8.380 -12.648  1.00 85.34           O  
-ANISOU 1083  OD2 ASP A 587    11737  10636  10053   1103  -1068   -968       O  
-ATOM   1084  N   ASN A 588      10.106  -9.233  -8.653  1.00 68.40           N  
-ANISOU 1084  N   ASN A 588    10297   8012   7680    972   -808   -708       N  
-ATOM   1085  CA  ASN A 588       9.552 -10.032  -7.567  1.00 77.27           C  
-ANISOU 1085  CA  ASN A 588    11648   9003   8708    973   -807   -693       C  
-ATOM   1086  C   ASN A 588       8.050 -10.251  -7.713  1.00 66.34           C  
-ANISOU 1086  C   ASN A 588    10297   7587   7320    879   -675   -608       C  
-ATOM   1087  O   ASN A 588       7.560 -11.369  -7.570  1.00 64.37           O  
-ANISOU 1087  O   ASN A 588    10179   7271   7007    873   -680   -597       O  
-ATOM   1088  CB  ASN A 588       9.851  -9.383  -6.211  1.00104.02           C  
-ANISOU 1088  CB  ASN A 588    15153  12315  12057    995   -821   -711       C  
-ATOM   1089  CG  ASN A 588      11.318  -9.453  -5.836  1.00115.59           C  
-ANISOU 1089  CG  ASN A 588    16638  13781  13501   1099   -969   -805       C  
-ATOM   1090  OD1 ASN A 588      12.072 -10.266  -6.369  1.00128.57           O  
-ANISOU 1090  OD1 ASN A 588    18263  15451  15136   1162  -1074   -863       O  
-ATOM   1091  ND2 ASN A 588      11.729  -8.597  -4.907  1.00107.65           N  
-ANISOU 1091  ND2 ASN A 588    15668  12745  12490   1120   -980   -826       N  
-ATOM   1092  N   THR A 589       7.325  -9.176  -8.003  1.00 50.52           N  
-ANISOU 1092  N   THR A 589     8173   5630   5390    806   -560   -553       N  
-ATOM   1093  CA  THR A 589       5.870  -9.236  -8.076  1.00 44.62           C  
-ANISOU 1093  CA  THR A 589     7448   4853   4651    716   -429   -479       C  
-ATOM   1094  C   THR A 589       5.373  -9.447  -9.506  1.00 45.58           C  
-ANISOU 1094  C   THR A 589     7412   5068   4838    676   -385   -445       C  
-ATOM   1095  O   THR A 589       5.933  -8.902 -10.458  1.00 63.73           O  
-ANISOU 1095  O   THR A 589     9535   7473   7208    687   -410   -456       O  
-ATOM   1096  CB  THR A 589       5.223  -7.964  -7.487  1.00 56.47           C  
-ANISOU 1096  CB  THR A 589     8921   6339   6196    656   -324   -440       C  
-ATOM   1097  OG1 THR A 589       5.945  -7.554  -6.319  1.00 67.71           O  
-ANISOU 1097  OG1 THR A 589    10446   7705   7575    703   -379   -482       O  
-ATOM   1098  CG2 THR A 589       3.770  -8.222  -7.117  1.00 46.00           C  
-ANISOU 1098  CG2 THR A 589     7685   4946   4849    572   -202   -385       C  
-ATOM   1099  N   VAL A 590       4.317 -10.244  -9.644  1.00 41.21           N  
-ANISOU 1099  N   VAL A 590     6926   4473   4258    625   -320   -407       N  
-ATOM   1100  CA  VAL A 590       3.716 -10.530 -10.942  1.00 43.26           C  
-ANISOU 1100  CA  VAL A 590     7053   4812   4573    584   -273   -373       C  
-ATOM   1101  C   VAL A 590       2.583  -9.559 -11.262  1.00 44.87           C  
-ANISOU 1101  C   VAL A 590     7148   5045   4855    497   -142   -308       C  
-ATOM   1102  O   VAL A 590       1.690  -9.345 -10.443  1.00 38.86           O  
-ANISOU 1102  O   VAL A 590     6481   4208   4078    447    -56   -280       O  
-ATOM   1103  CB  VAL A 590       3.176 -11.975 -11.003  1.00 57.27           C  
-ANISOU 1103  CB  VAL A 590     8951   6528   6282    577   -276   -371       C  
-ATOM   1104  CG1 VAL A 590       2.093 -12.103 -12.067  1.00 60.37           C  
-ANISOU 1104  CG1 VAL A 590     9230   6976   6731    507   -183   -320       C  
-ATOM   1105  CG2 VAL A 590       4.307 -12.956 -11.261  1.00 56.17           C  
-ANISOU 1105  CG2 VAL A 590     8845   6399   6098    663   -415   -435       C  
-ATOM   1106  N   LYS A 591       2.626  -8.978 -12.457  1.00 46.37           N  
-ANISOU 1106  N   LYS A 591     7143   5346   5131    479   -128   -287       N  
-ATOM   1107  CA  LYS A 591       1.590  -8.050 -12.899  1.00 49.20           C  
-ANISOU 1107  CA  LYS A 591     7383   5738   5571    403    -17   -227       C  
-ATOM   1108  C   LYS A 591       0.960  -8.528 -14.202  1.00 48.22           C  
-ANISOU 1108  C   LYS A 591     7150   5685   5488    366     16   -195       C  
-ATOM   1109  O   LYS A 591       1.578  -8.454 -15.265  1.00 51.48           O  
-ANISOU 1109  O   LYS A 591     7427   6197   5936    385    -34   -203       O  
-ATOM   1110  CB  LYS A 591       2.169  -6.646 -13.083  1.00 46.01           C  
-ANISOU 1110  CB  LYS A 591     6841   5399   5242    406    -25   -223       C  
-ATOM   1111  CG  LYS A 591       2.820  -6.068 -11.835  1.00 37.31           C  
-ANISOU 1111  CG  LYS A 591     5831   4235   4109    443    -57   -257       C  
-ATOM   1112  CD  LYS A 591       1.812  -5.885 -10.711  1.00 33.66           C  
-ANISOU 1112  CD  LYS A 591     5494   3670   3624    396     32   -235       C  
-ATOM   1113  CE  LYS A 591       2.463  -5.272  -9.481  1.00 33.85           C  
-ANISOU 1113  CE  LYS A 591     5606   3637   3617    432      1   -270       C  
-ATOM   1114  NZ  LYS A 591       1.458  -4.868  -8.458  1.00 40.01           N  
-ANISOU 1114  NZ  LYS A 591     6479   4332   4389    375    100   -249       N  
-ATOM   1115  N   ILE A 592      -0.272  -9.021 -14.115  1.00 38.30           N  
-ANISOU 1115  N   ILE A 592     5952   4378   4223    310    102   -163       N  
-ATOM   1116  CA  ILE A 592      -0.985  -9.517 -15.286  1.00 39.64           C  
-ANISOU 1116  CA  ILE A 592     6027   4606   4429    273    139   -134       C  
-ATOM   1117  C   ILE A 592      -1.764  -8.401 -15.976  1.00 40.22           C  
-ANISOU 1117  C   ILE A 592     5939   4738   4603    212    219    -82       C  
-ATOM   1118  O   ILE A 592      -2.631  -7.772 -15.369  1.00 35.56           O  
-ANISOU 1118  O   ILE A 592     5373   4095   4044    164    303    -58       O  
-ATOM   1119  CB  ILE A 592      -1.962 -10.644 -14.910  1.00 44.30           C  
-ANISOU 1119  CB  ILE A 592     6754   5113   4964    241    193   -130       C  
-ATOM   1120  CG1 ILE A 592      -1.200 -11.853 -14.367  1.00 29.05           C  
-ANISOU 1120  CG1 ILE A 592     4982   3123   2933    302    104   -179       C  
-ATOM   1121  CG2 ILE A 592      -2.806 -11.042 -16.111  1.00 58.87           C  
-ANISOU 1121  CG2 ILE A 592     8491   7021   6858    197    242   -100       C  
-ATOM   1122  CD1 ILE A 592      -2.103 -12.954 -13.856  1.00 29.18           C  
-ANISOU 1122  CD1 ILE A 592     5157   3045   2886    267    155   -175       C  
-ATOM   1123  N   GLY A 593      -1.453  -8.161 -17.245  1.00 58.81           N  
-ANISOU 1123  N   GLY A 593     8133   7203   7011    213    189    -67       N  
-ATOM   1124  CA  GLY A 593      -2.113  -7.114 -18.003  1.00 59.77           C  
-ANISOU 1124  CA  GLY A 593     8099   7383   7227    159    249    -14       C  
-ATOM   1125  C   GLY A 593      -2.473  -7.529 -19.416  1.00 63.34           C  
-ANISOU 1125  C   GLY A 593     8430   7923   7712    135    252     10       C  
-ATOM   1126  O   GLY A 593      -2.231  -8.666 -19.822  1.00 69.03           O  
-ANISOU 1126  O   GLY A 593     9183   8662   8383    160    212    -16       O  
-ATOM   1127  N   ASP A 594      -3.062  -6.596 -20.158  1.00 49.21           N  
-ANISOU 1127  N   ASP A 594     6504   6188   6007     88    297     60       N  
-ATOM   1128  CA  ASP A 594      -3.430  -6.799 -21.559  1.00 34.54           C  
-ANISOU 1128  CA  ASP A 594     4517   4421   4187     60    300     90       C  
-ATOM   1129  C   ASP A 594      -4.695  -7.644 -21.715  1.00 30.31           C  
-ANISOU 1129  C   ASP A 594     4020   3847   3650     23    369    101       C  
-ATOM   1130  O   ASP A 594      -4.966  -8.184 -22.788  1.00 44.21           O  
-ANISOU 1130  O   ASP A 594     5705   5673   5419     10    364    112       O  
-ATOM   1131  CB  ASP A 594      -2.264  -7.398 -22.353  1.00 53.71           C  
-ANISOU 1131  CB  ASP A 594     6897   6937   6574    103    209     56       C  
-ATOM   1132  CG  ASP A 594      -2.298  -7.013 -23.820  1.00 76.59           C  
-ANISOU 1132  CG  ASP A 594     9625   9951   9523     72    201     93       C  
-ATOM   1133  OD1 ASP A 594      -3.341  -6.502 -24.280  1.00 83.04           O  
-ANISOU 1133  OD1 ASP A 594    10373  10775  10403     19    263    145       O  
-ATOM   1134  OD2 ASP A 594      -1.279  -7.218 -24.513  1.00 80.76           O  
-ANISOU 1134  OD2 ASP A 594    10091  10565  10031     98    131     65       O  
-ATOM   1135  N   PHE A 595      -5.468  -7.748 -20.638  1.00 47.08           N  
-ANISOU 1135  N   PHE A 595     6260   5867   5760      4    435     95       N  
-ATOM   1136  CA  PHE A 595      -6.761  -8.419 -20.684  1.00 55.10           C  
-ANISOU 1136  CA  PHE A 595     7312   6840   6783    -41    514    102       C  
-ATOM   1137  C   PHE A 595      -7.856  -7.422 -21.053  1.00 62.24           C  
-ANISOU 1137  C   PHE A 595     8107   7755   7787    -98    587    144       C  
-ATOM   1138  O   PHE A 595      -8.986  -7.807 -21.355  1.00 66.01           O  
-ANISOU 1138  O   PHE A 595     8570   8218   8292   -140    652    152       O  
-ATOM   1139  CB  PHE A 595      -7.075  -9.084 -19.339  1.00 48.76           C  
-ANISOU 1139  CB  PHE A 595     6697   5919   5912    -42    553     68       C  
-ATOM   1140  CG  PHE A 595      -6.995  -8.150 -18.162  1.00 47.87           C  
-ANISOU 1140  CG  PHE A 595     6644   5739   5806    -46    578     64       C  
-ATOM   1141  CD1 PHE A 595      -5.789  -7.927 -17.520  1.00 43.58           C  
-ANISOU 1141  CD1 PHE A 595     6160   5184   5215      8    505     39       C  
-ATOM   1142  CD2 PHE A 595      -8.127  -7.501 -17.696  1.00 52.64           C  
-ANISOU 1142  CD2 PHE A 595     7244   6292   6466   -102    674     77       C  
-ATOM   1143  CE1 PHE A 595      -5.711  -7.071 -16.438  1.00 38.05           C  
-ANISOU 1143  CE1 PHE A 595     5514   4424   4521      5    528     33       C  
-ATOM   1144  CE2 PHE A 595      -8.056  -6.643 -16.615  1.00 41.78           C  
-ANISOU 1144  CE2 PHE A 595     5919   4857   5097   -107    699     68       C  
-ATOM   1145  CZ  PHE A 595      -6.846  -6.428 -15.985  1.00 34.81           C  
-ANISOU 1145  CZ  PHE A 595     5097   3965   4165    -54    626     48       C  
-ATOM   1146  N   GLY A 596      -7.500  -6.140 -21.035  1.00 62.49           N  
-ANISOU 1146  N   GLY A 596     8058   7810   7874    -98    572    168       N  
-ATOM   1147  CA  GLY A 596      -8.440  -5.059 -21.282  1.00 61.37           C  
-ANISOU 1147  CA  GLY A 596     7817   7670   7833   -146    630    205       C  
-ATOM   1148  C   GLY A 596      -9.400  -5.313 -22.426  1.00 61.41           C  
-ANISOU 1148  C   GLY A 596     7720   7724   7889   -183    660    233       C  
-ATOM   1149  O   GLY A 596      -9.387  -4.598 -23.429  1.00 58.98           O  
-ANISOU 1149  O   GLY A 596     7276   7491   7644   -195    634    274       O  
-ATOM   1150  N   GLY A 615      -2.203 -14.091 -33.910  1.00 61.85           N  
-ANISOU 1150  N   GLY A 615     7109   8853   7538     13     10    -31       N  
-ATOM   1151  CA  GLY A 615      -1.047 -13.702 -33.124  1.00 67.49           C  
-ANISOU 1151  CA  GLY A 615     7870   9544   8229     55    -41    -70       C  
-ATOM   1152  C   GLY A 615      -0.407 -14.870 -32.397  1.00 70.90           C  
-ANISOU 1152  C   GLY A 615     8416   9916   8608    123    -96   -152       C  
-ATOM   1153  O   GLY A 615       0.113 -15.793 -33.023  1.00 68.78           O  
-ANISOU 1153  O   GLY A 615     8112   9709   8310    146   -146   -212       O  
-ATOM   1154  N   SER A 616      -0.443 -14.827 -31.068  1.00 97.53           N  
-ANISOU 1154  N   SER A 616    11925  13166  11965    154    -90   -156       N  
-ATOM   1155  CA  SER A 616       0.139 -15.884 -30.245  1.00 91.96           C  
-ANISOU 1155  CA  SER A 616    11350  12386  11207    221   -147   -228       C  
-ATOM   1156  C   SER A 616      -0.808 -17.075 -30.108  1.00 81.37           C  
-ANISOU 1156  C   SER A 616    10097  10974   9846    220   -115   -230       C  
-ATOM   1157  O   SER A 616      -1.874 -16.968 -29.501  1.00 75.49           O  
-ANISOU 1157  O   SER A 616     9429  10139   9113    191    -41   -182       O  
-ATOM   1158  CB  SER A 616       0.514 -15.344 -28.865  1.00 71.41           C  
-ANISOU 1158  CB  SER A 616     8865   9679   8588    253   -157   -232       C  
-ATOM   1159  OG  SER A 616      -0.591 -14.705 -28.251  1.00 67.33           O  
-ANISOU 1159  OG  SER A 616     8400   9084   8101    211    -71   -162       O  
-ATOM   1160  N   ILE A 617      -0.403 -18.210 -30.669  1.00 52.21           N  
-ANISOU 1160  N   ILE A 617     6391   7321   6124    251   -169   -290       N  
-ATOM   1161  CA  ILE A 617      -1.244 -19.400 -30.705  1.00 43.99           C  
-ANISOU 1161  CA  ILE A 617     5420   6227   5068    248   -142   -296       C  
-ATOM   1162  C   ILE A 617      -0.748 -20.490 -29.761  1.00 41.05           C  
-ANISOU 1162  C   ILE A 617     5207   5750   4639    312   -205   -359       C  
-ATOM   1163  O   ILE A 617      -1.396 -21.525 -29.606  1.00 35.83           O  
-ANISOU 1163  O   ILE A 617     4631   5024   3958    313   -187   -367       O  
-ATOM   1164  CB  ILE A 617      -1.297 -19.992 -32.124  1.00 50.80           C  
-ANISOU 1164  CB  ILE A 617     6149   7209   5943    231   -155   -317       C  
-ATOM   1165  CG1 ILE A 617       0.121 -20.181 -32.661  1.00 55.61           C  
-ANISOU 1165  CG1 ILE A 617     6680   7915   6534    274   -253   -394       C  
-ATOM   1166  CG2 ILE A 617      -2.093 -19.092 -33.052  1.00 45.53           C  
-ANISOU 1166  CG2 ILE A 617     5346   6625   5327    160    -84   -244       C  
-ATOM   1167  CD1 ILE A 617       0.213 -21.127 -33.831  1.00 69.30           C  
-ANISOU 1167  CD1 ILE A 617     8321   9745   8265    274   -281   -441       C  
-ATOM   1168  N   LEU A 618       0.403 -20.260 -29.139  1.00 42.50           N  
-ANISOU 1168  N   LEU A 618     5432   5917   4798    366   -282   -406       N  
-ATOM   1169  CA  LEU A 618       1.017 -21.269 -28.281  1.00 39.74           C  
-ANISOU 1169  CA  LEU A 618     5233   5474   4395    436   -361   -472       C  
-ATOM   1170  C   LEU A 618       0.240 -21.518 -26.988  1.00 36.54           C  
-ANISOU 1170  C   LEU A 618     5018   4910   3956    430   -314   -437       C  
-ATOM   1171  O   LEU A 618       0.355 -22.587 -26.388  1.00 43.49           O  
-ANISOU 1171  O   LEU A 618     6038   5699   4789    471   -361   -476       O  
-ATOM   1172  CB  LEU A 618       2.468 -20.900 -27.966  1.00 46.75           C  
-ANISOU 1172  CB  LEU A 618     6107   6387   5268    497   -459   -536       C  
-ATOM   1173  CG  LEU A 618       3.451 -21.036 -29.128  1.00 40.24           C  
-ANISOU 1173  CG  LEU A 618     5123   5705   4460    516   -528   -604       C  
-ATOM   1174  CD1 LEU A 618       4.848 -20.604 -28.714  1.00 34.30           C  
-ANISOU 1174  CD1 LEU A 618     4363   4972   3698    573   -618   -672       C  
-ATOM   1175  CD2 LEU A 618       3.467 -22.467 -29.634  1.00 50.02           C  
-ANISOU 1175  CD2 LEU A 618     6375   6949   5680    545   -577   -663       C  
-ATOM   1176  N   TRP A 619      -0.550 -20.535 -26.566  1.00 46.12           N  
-ANISOU 1176  N   TRP A 619     6237   6091   5194    378   -224   -366       N  
-ATOM   1177  CA  TRP A 619      -1.299 -20.641 -25.315  1.00 51.24           C  
-ANISOU 1177  CA  TRP A 619     7060   6596   5811    362   -169   -334       C  
-ATOM   1178  C   TRP A 619      -2.778 -20.939 -25.543  1.00 46.37           C  
-ANISOU 1178  C   TRP A 619     6452   5950   5216    294    -60   -284       C  
-ATOM   1179  O   TRP A 619      -3.565 -20.982 -24.595  1.00 34.12           O  
-ANISOU 1179  O   TRP A 619     5032   4288   3645    265      5   -257       O  
-ATOM   1180  CB  TRP A 619      -1.150 -19.359 -24.493  1.00 55.29           C  
-ANISOU 1180  CB  TRP A 619     7592   7078   6336    353   -142   -301       C  
-ATOM   1181  CG  TRP A 619       0.255 -19.088 -24.055  1.00 58.89           C  
-ANISOU 1181  CG  TRP A 619     8066   7543   6767    421   -245   -355       C  
-ATOM   1182  CD1 TRP A 619       0.819 -19.423 -22.859  1.00 52.95           C  
-ANISOU 1182  CD1 TRP A 619     7478   6684   5957    473   -304   -390       C  
-ATOM   1183  CD2 TRP A 619       1.278 -18.426 -24.810  1.00 58.50           C  
-ANISOU 1183  CD2 TRP A 619     7864   7615   6750    442   -302   -383       C  
-ATOM   1184  NE1 TRP A 619       2.128 -19.012 -22.822  1.00 52.52           N  
-ANISOU 1184  NE1 TRP A 619     7378   6677   5901    530   -396   -442       N  
-ATOM   1185  CE2 TRP A 619       2.435 -18.397 -24.007  1.00 61.87           C  
-ANISOU 1185  CE2 TRP A 619     8366   8001   7140    510   -394   -440       C  
-ATOM   1186  CE3 TRP A 619       1.328 -17.856 -26.085  1.00 55.82           C  
-ANISOU 1186  CE3 TRP A 619     7334   7412   6463    407   -285   -366       C  
-ATOM   1187  CZ2 TRP A 619       3.629 -17.819 -24.438  1.00 60.15           C  
-ANISOU 1187  CZ2 TRP A 619     8034   7878   6942    543   -463   -487       C  
-ATOM   1188  CZ3 TRP A 619       2.513 -17.283 -26.510  1.00 53.07           C  
-ANISOU 1188  CZ3 TRP A 619     6879   7157   6128    435   -352   -408       C  
-ATOM   1189  CH2 TRP A 619       3.647 -17.269 -25.689  1.00 47.30           C  
-ANISOU 1189  CH2 TRP A 619     6222   6386   5365    502   -438   -470       C  
-ATOM   1190  N   MET A 620      -3.145 -21.154 -26.803  1.00 50.82           N  
-ANISOU 1190  N   MET A 620     6875   6614   5818    268    -41   -278       N  
-ATOM   1191  CA  MET A 620      -4.543 -21.333 -27.187  1.00 51.67           C  
-ANISOU 1191  CA  MET A 620     6960   6713   5959    203     61   -234       C  
-ATOM   1192  C   MET A 620      -5.048 -22.763 -27.008  1.00 59.18           C  
-ANISOU 1192  C   MET A 620     8027   7588   6870    206     66   -262       C  
-ATOM   1193  O   MET A 620      -4.462 -23.712 -27.529  1.00 56.36           O  
-ANISOU 1193  O   MET A 620     7657   7264   6492    247     -8   -313       O  
-ATOM   1194  CB  MET A 620      -4.756 -20.883 -28.635  1.00 38.33           C  
-ANISOU 1194  CB  MET A 620     5069   5166   4329    170     78   -212       C  
-ATOM   1195  CG  MET A 620      -4.622 -19.384 -28.837  1.00 37.02           C  
-ANISOU 1195  CG  MET A 620     4793   5063   4211    145     99   -166       C  
-ATOM   1196  SD  MET A 620      -4.761 -18.895 -30.563  1.00 59.10           S  
-ANISOU 1196  SD  MET A 620     7365   8026   7064    106    106   -140       S  
-ATOM   1197  CE  MET A 620      -6.214 -19.814 -31.057  1.00 57.26           C  
-ANISOU 1197  CE  MET A 620     7135   7772   6851     62    183   -125       C  
-ATOM   1198  N   ALA A 621      -6.149 -22.903 -26.275  1.00 62.89           N  
-ANISOU 1198  N   ALA A 621     8607   7956   7334    159    156   -232       N  
-ATOM   1199  CA  ALA A 621      -6.785 -24.198 -26.073  1.00 54.69           C  
-ANISOU 1199  CA  ALA A 621     7683   6838   6261    148    179   -251       C  
-ATOM   1200  C   ALA A 621      -7.319 -24.747 -27.389  1.00 54.88           C  
-ANISOU 1200  C   ALA A 621     7574   6953   6326    125    199   -256       C  
-ATOM   1201  O   ALA A 621      -7.687 -23.984 -28.281  1.00 51.93           O  
-ANISOU 1201  O   ALA A 621     7039   6680   6013     93    238   -225       O  
-ATOM   1202  CB  ALA A 621      -7.905 -24.084 -25.056  1.00 36.46           C  
-ANISOU 1202  CB  ALA A 621     5503   4411   3940     89    285   -218       C  
-ATOM   1203  N   PRO A 622      -7.366 -26.082 -27.508  1.00 45.25           N  
-ANISOU 1203  N   PRO A 622     6425   5695   5073    142    170   -296       N  
-ATOM   1204  CA  PRO A 622      -7.840 -26.744 -28.726  1.00 44.84           C  
-ANISOU 1204  CA  PRO A 622     6258   5725   5055    125    184   -309       C  
-ATOM   1205  C   PRO A 622      -9.192 -26.211 -29.182  1.00 51.61           C  
-ANISOU 1205  C   PRO A 622     7026   6611   5973     50    303   -261       C  
-ATOM   1206  O   PRO A 622      -9.358 -25.931 -30.368  1.00 39.01           O  
-ANISOU 1206  O   PRO A 622     5261   5133   4426     36    309   -252       O  
-ATOM   1207  CB  PRO A 622      -7.969 -28.205 -28.295  1.00 40.55           C  
-ANISOU 1207  CB  PRO A 622     5866   5080   4460    142    162   -348       C  
-ATOM   1208  CG  PRO A 622      -6.953 -28.358 -27.226  1.00 33.28           C  
-ANISOU 1208  CG  PRO A 622     5095   4072   3476    199     76   -374       C  
-ATOM   1209  CD  PRO A 622      -6.935 -27.053 -26.487  1.00 31.27           C  
-ANISOU 1209  CD  PRO A 622     4855   3799   3229    182    115   -331       C  
-ATOM   1210  N   GLU A 623     -10.136 -26.070 -28.255  1.00 53.67           N  
-ANISOU 1210  N   GLU A 623     7400   6765   6229      2    394   -234       N  
-ATOM   1211  CA  GLU A 623     -11.468 -25.572 -28.590  1.00 51.80           C  
-ANISOU 1211  CA  GLU A 623     7086   6544   6054    -69    508   -199       C  
-ATOM   1212  C   GLU A 623     -11.422 -24.123 -29.071  1.00 51.98           C  
-ANISOU 1212  C   GLU A 623     6956   6658   6137    -81    520   -157       C  
-ATOM   1213  O   GLU A 623     -12.323 -23.662 -29.772  1.00 51.12           O  
-ANISOU 1213  O   GLU A 623     6729   6603   6091   -126    584   -131       O  
-ATOM   1214  CB  GLU A 623     -12.422 -25.709 -27.398  1.00 39.66           C  
-ANISOU 1214  CB  GLU A 623     5706   4868   4495   -120    604   -190       C  
-ATOM   1215  CG  GLU A 623     -12.150 -24.749 -26.249  1.00 47.39           C  
-ANISOU 1215  CG  GLU A 623     6771   5782   5455   -121    616   -167       C  
-ATOM   1216  CD  GLU A 623     -11.109 -25.268 -25.276  1.00 43.38           C  
-ANISOU 1216  CD  GLU A 623     6431   5190   4861    -68    533   -192       C  
-ATOM   1217  OE1 GLU A 623     -10.479 -26.305 -25.568  1.00 45.67           O  
-ANISOU 1217  OE1 GLU A 623     6758   5483   5113    -22    453   -228       O  
-ATOM   1218  OE2 GLU A 623     -10.923 -24.637 -24.215  1.00 39.75           O  
-ANISOU 1218  OE2 GLU A 623     6067   4661   4374    -70    545   -178       O  
-ATOM   1219  N   VAL A 624     -10.366 -23.412 -28.690  1.00 51.85           N  
-ANISOU 1219  N   VAL A 624     6945   6655   6101    -41    454   -152       N  
-ATOM   1220  CA  VAL A 624     -10.171 -22.031 -29.118  1.00 50.63           C  
-ANISOU 1220  CA  VAL A 624     6655   6585   5999    -50    454   -112       C  
-ATOM   1221  C   VAL A 624      -9.639 -21.968 -30.547  1.00 60.59           C  
-ANISOU 1221  C   VAL A 624     7743   7993   7287    -33    395   -116       C  
-ATOM   1222  O   VAL A 624     -10.037 -21.105 -31.329  1.00 71.58           O  
-ANISOU 1222  O   VAL A 624     8996   9466   8736    -66    423    -78       O  
-ATOM   1223  CB  VAL A 624      -9.204 -21.281 -28.181  1.00 34.70           C  
-ANISOU 1223  CB  VAL A 624     4705   4528   3950    -15    407   -110       C  
-ATOM   1224  CG1 VAL A 624      -8.801 -19.945 -28.784  1.00 34.78           C  
-ANISOU 1224  CG1 VAL A 624     4565   4639   4012    -18    389    -74       C  
-ATOM   1225  CG2 VAL A 624      -9.837 -21.084 -26.819  1.00 36.09           C  
-ANISOU 1225  CG2 VAL A 624     5032   4571   4108    -44    478    -97       C  
-ATOM   1226  N   ILE A 625      -8.741 -22.889 -30.884  1.00 60.96           N  
-ANISOU 1226  N   ILE A 625     7800   8071   7290     15    311   -165       N  
-ATOM   1227  CA  ILE A 625      -8.150 -22.936 -32.219  1.00 50.51           C  
-ANISOU 1227  CA  ILE A 625     6318   6889   5983     30    253   -181       C  
-ATOM   1228  C   ILE A 625      -9.190 -23.233 -33.300  1.00 69.18           C  
-ANISOU 1228  C   ILE A 625     8575   9318   8392    -15    308   -166       C  
-ATOM   1229  O   ILE A 625      -9.309 -22.493 -34.279  1.00 82.27           O  
-ANISOU 1229  O   ILE A 625    10083  11083  10092    -41    314   -135       O  
-ATOM   1230  CB  ILE A 625      -7.000 -23.961 -32.298  1.00 35.84           C  
-ANISOU 1230  CB  ILE A 625     4499   5045   4072     94    151   -250       C  
-ATOM   1231  CG1 ILE A 625      -5.772 -23.441 -31.544  1.00 22.96           C  
-ANISOU 1231  CG1 ILE A 625     2923   3393   2408    143     78   -269       C  
-ATOM   1232  CG2 ILE A 625      -6.642 -24.248 -33.744  1.00 39.95           C  
-ANISOU 1232  CG2 ILE A 625     4859   5710   4610     97    108   -275       C  
-ATOM   1233  CD1 ILE A 625      -4.551 -24.339 -31.643  1.00 24.11           C  
-ANISOU 1233  CD1 ILE A 625     3092   3558   2510    210    -33   -346       C  
-ATOM   1234  N   ARG A 626      -9.939 -24.317 -33.121  1.00 66.80           N  
-ANISOU 1234  N   ARG A 626     8353   8949   8079    -26    347   -188       N  
-ATOM   1235  CA  ARG A 626     -11.009 -24.671 -34.049  1.00 68.44           C  
-ANISOU 1235  CA  ARG A 626     8470   9205   8330    -68    405   -180       C  
-ATOM   1236  C   ARG A 626     -12.251 -23.812 -33.825  1.00 67.25           C  
-ANISOU 1236  C   ARG A 626     8298   9018   8235   -127    505   -129       C  
-ATOM   1237  O   ARG A 626     -12.429 -22.778 -34.468  1.00 65.87           O  
-ANISOU 1237  O   ARG A 626     7996   8922   8108   -150    515    -88       O  
-ATOM   1238  CB  ARG A 626     -11.359 -26.159 -33.932  1.00 64.43           C  
-ANISOU 1238  CB  ARG A 626     8053   8635   7791    -60    411   -228       C  
-ATOM   1239  CG  ARG A 626     -11.218 -26.728 -32.528  1.00 60.34           C  
-ANISOU 1239  CG  ARG A 626     7739   7969   7219    -42    412   -247       C  
-ATOM   1240  CD  ARG A 626     -11.646 -28.188 -32.478  1.00 50.81           C  
-ANISOU 1240  CD  ARG A 626     6622   6698   5986    -42    422   -289       C  
-ATOM   1241  NE  ARG A 626     -11.251 -28.837 -31.230  1.00 59.38           N  
-ANISOU 1241  NE  ARG A 626     7907   7649   7006    -16    395   -312       N  
-ATOM   1242  CZ  ARG A 626     -11.985 -28.850 -30.121  1.00 54.61           C  
-ANISOU 1242  CZ  ARG A 626     7449   6917   6382    -54    470   -294       C  
-ATOM   1243  NH1 ARG A 626     -13.164 -28.241 -30.090  1.00 61.73           N  
-ANISOU 1243  NH1 ARG A 626     8313   7810   7332   -119    580   -260       N  
-ATOM   1244  NH2 ARG A 626     -11.538 -29.471 -29.038  1.00 51.35           N  
-ANISOU 1244  NH2 ARG A 626     7223   6386   5901    -28    434   -314       N  
-ATOM   1245  N   ASN A 631     -19.380 -20.852 -27.145  1.00103.54           N  
-ANISOU 1245  N   ASN A 631    13410  12920  13011   -480   1204    -87       N  
-ATOM   1246  CA  ASN A 631     -18.563 -20.280 -26.081  1.00104.19           C  
-ANISOU 1246  CA  ASN A 631    13595  12948  13045   -458   1176    -73       C  
-ATOM   1247  C   ASN A 631     -17.101 -20.715 -26.159  1.00 98.42           C  
-ANISOU 1247  C   ASN A 631    12912  12245  12239   -388   1059    -66       C  
-ATOM   1248  O   ASN A 631     -16.600 -21.382 -25.254  1.00 99.10           O  
-ANISOU 1248  O   ASN A 631    13161  12249  12242   -374   1041    -84       O  
-ATOM   1249  CB  ASN A 631     -19.157 -20.629 -24.712  1.00114.71           C  
-ANISOU 1249  CB  ASN A 631    15101  14149  14333   -508   1265   -103       C  
-ATOM   1250  CG  ASN A 631     -20.464 -19.907 -24.443  1.00121.88           C  
-ANISOU 1250  CG  ASN A 631    15959  15028  15322   -576   1378   -117       C  
-ATOM   1251  OD1 ASN A 631     -20.731 -18.851 -25.018  1.00128.92           O  
-ANISOU 1251  OD1 ASN A 631    16700  15983  16299   -576   1376    -95       O  
-ATOM   1252  ND2 ASN A 631     -21.284 -20.471 -23.563  1.00119.18           N  
-ANISOU 1252  ND2 ASN A 631    15743  14588  14952   -637   1477   -156       N  
-ATOM   1253  N   PRO A 632     -16.411 -20.337 -27.249  1.00 84.27           N  
-ANISOU 1253  N   PRO A 632    10977  10569  10474   -346    977    -42       N  
-ATOM   1254  CA  PRO A 632     -15.006 -20.711 -27.449  1.00 77.65           C  
-ANISOU 1254  CA  PRO A 632    10158   9771   9573   -280    864    -46       C  
-ATOM   1255  C   PRO A 632     -14.096 -20.186 -26.341  1.00 75.05           C  
-ANISOU 1255  C   PRO A 632     9937   9384   9195   -250    825    -41       C  
-ATOM   1256  O   PRO A 632     -13.291 -20.947 -25.806  1.00 73.42           O  
-ANISOU 1256  O   PRO A 632     9854   9130   8911   -210    767    -65       O  
-ATOM   1257  CB  PRO A 632     -14.655 -20.050 -28.785  1.00 73.11           C  
-ANISOU 1257  CB  PRO A 632     9391   9334   9054   -262    809    -18       C  
-ATOM   1258  CG  PRO A 632     -15.963 -19.879 -29.481  1.00 75.16           C  
-ANISOU 1258  CG  PRO A 632     9545   9622   9390   -313    885     -8       C  
-ATOM   1259  CD  PRO A 632     -16.945 -19.575 -28.391  1.00 77.75           C  
-ANISOU 1259  CD  PRO A 632     9962   9841   9738   -363    986    -16       C  
-ATOM   1260  N   TYR A 633     -14.221 -18.905 -26.006  1.00 68.21           N  
-ANISOU 1260  N   TYR A 633     9023   8518   8375   -265    851    -12       N  
-ATOM   1261  CA  TYR A 633     -13.415 -18.314 -24.939  1.00 48.37           C  
-ANISOU 1261  CA  TYR A 633     6606   5952   5822   -239    820     -9       C  
-ATOM   1262  C   TYR A 633     -14.083 -18.445 -23.574  1.00 47.74           C  
-ANISOU 1262  C   TYR A 633     6687   5741   5709   -280    903    -25       C  
-ATOM   1263  O   TYR A 633     -15.183 -17.936 -23.357  1.00 56.10           O  
-ANISOU 1263  O   TYR A 633     7720   6772   6824   -338    998    -21       O  
-ATOM   1264  CB  TYR A 633     -13.102 -16.848 -25.237  1.00 44.15           C  
-ANISOU 1264  CB  TYR A 633     5942   5483   5351   -233    799     29       C  
-ATOM   1265  CG  TYR A 633     -11.956 -16.666 -26.205  1.00 42.61           C  
-ANISOU 1265  CG  TYR A 633     5638   5399   5154   -183    696     39       C  
-ATOM   1266  CD1 TYR A 633     -12.178 -16.217 -27.499  1.00 47.88           C  
-ANISOU 1266  CD1 TYR A 633     6132   6176   5885   -195    686     67       C  
-ATOM   1267  CD2 TYR A 633     -10.654 -16.955 -25.825  1.00 40.83           C  
-ANISOU 1267  CD2 TYR A 633     5483   5170   4861   -125    608     18       C  
-ATOM   1268  CE1 TYR A 633     -11.132 -16.052 -28.386  1.00 40.52           C  
-ANISOU 1268  CE1 TYR A 633     5102   5349   4946   -158    597     74       C  
-ATOM   1269  CE2 TYR A 633      -9.602 -16.796 -26.702  1.00 45.91           C  
-ANISOU 1269  CE2 TYR A 633     6022   5919   5503    -84    518     18       C  
-ATOM   1270  CZ  TYR A 633      -9.846 -16.344 -27.982  1.00 46.02           C  
-ANISOU 1270  CZ  TYR A 633     5866   6042   5577   -104    517     46       C  
-ATOM   1271  OH  TYR A 633      -8.799 -16.183 -28.860  1.00 54.92           O  
-ANISOU 1271  OH  TYR A 633     6892   7278   6699    -72    434     43       O  
-ATOM   1272  N   SER A 634     -13.404 -19.121 -22.653  1.00 42.82           N  
-ANISOU 1272  N   SER A 634     6233   5041   4996   -252    864    -47       N  
-ATOM   1273  CA  SER A 634     -13.977 -19.426 -21.348  1.00 50.22           C  
-ANISOU 1273  CA  SER A 634     7346   5851   5883   -295    939    -64       C  
-ATOM   1274  C   SER A 634     -12.940 -19.341 -20.236  1.00 49.12           C  
-ANISOU 1274  C   SER A 634     7353   5646   5664   -253    877    -71       C  
-ATOM   1275  O   SER A 634     -11.756 -19.121 -20.489  1.00 68.04           O  
-ANISOU 1275  O   SER A 634     9713   8094   8045   -186    773    -68       O  
-ATOM   1276  CB  SER A 634     -14.581 -20.830 -21.362  1.00 54.07           C  
-ANISOU 1276  CB  SER A 634     7933   6285   6327   -323    976    -91       C  
-ATOM   1277  OG  SER A 634     -13.578 -21.805 -21.590  1.00 60.61           O  
-ANISOU 1277  OG  SER A 634     8820   7119   7089   -261    871   -107       O  
-ATOM   1278  N   PHE A 635     -13.396 -19.522 -19.002  1.00 44.60           N  
-ANISOU 1278  N   PHE A 635     6947   4960   5039   -294    942    -84       N  
-ATOM   1279  CA  PHE A 635     -12.496 -19.591 -17.863  1.00 49.86           C  
-ANISOU 1279  CA  PHE A 635     7777   5549   5617   -258    885    -93       C  
-ATOM   1280  C   PHE A 635     -11.558 -20.777 -18.049  1.00 46.27           C  
-ANISOU 1280  C   PHE A 635     7408   5085   5089   -195    776   -112       C  
-ATOM   1281  O   PHE A 635     -10.402 -20.743 -17.629  1.00 44.23           O  
-ANISOU 1281  O   PHE A 635     7211   4814   4779   -130    677   -121       O  
-ATOM   1282  CB  PHE A 635     -13.290 -19.751 -16.562  1.00 65.09           C  
-ANISOU 1282  CB  PHE A 635     9881   7356   7494   -326    983   -106       C  
-ATOM   1283  CG  PHE A 635     -14.275 -18.641 -16.303  1.00 77.01           C  
-ANISOU 1283  CG  PHE A 635    11313   8867   9079   -392   1095   -100       C  
-ATOM   1284  CD1 PHE A 635     -15.577 -18.723 -16.772  1.00 83.10           C  
-ANISOU 1284  CD1 PHE A 635    12009   9650   9916   -461   1202   -107       C  
-ATOM   1285  CD2 PHE A 635     -13.902 -17.522 -15.581  1.00 77.15           C  
-ANISOU 1285  CD2 PHE A 635    11334   8874   9107   -383   1092    -92       C  
-ATOM   1286  CE1 PHE A 635     -16.483 -17.704 -16.528  1.00 80.91           C  
-ANISOU 1286  CE1 PHE A 635    11656   9372   9714   -518   1299   -110       C  
-ATOM   1287  CE2 PHE A 635     -14.801 -16.501 -15.334  1.00 72.87           C  
-ANISOU 1287  CE2 PHE A 635    10717   8331   8638   -441   1191    -92       C  
-ATOM   1288  CZ  PHE A 635     -16.093 -16.593 -15.808  1.00 75.83           C  
-ANISOU 1288  CZ  PHE A 635    11015   8716   9081   -508   1293   -103       C  
-ATOM   1289  N   GLN A 636     -12.068 -21.821 -18.697  1.00 53.08           N  
-ANISOU 1289  N   GLN A 636     8265   5953   5949   -212    792   -124       N  
-ATOM   1290  CA  GLN A 636     -11.321 -23.058 -18.907  1.00 58.63           C  
-ANISOU 1290  CA  GLN A 636     9049   6639   6588   -157    695   -147       C  
-ATOM   1291  C   GLN A 636     -10.234 -22.915 -19.972  1.00 57.76           C  
-ANISOU 1291  C   GLN A 636     8789   6647   6511    -80    580   -153       C  
-ATOM   1292  O   GLN A 636      -9.208 -23.595 -19.917  1.00 47.43           O  
-ANISOU 1292  O   GLN A 636     7547   5326   5148    -14    470   -179       O  
-ATOM   1293  CB  GLN A 636     -12.272 -24.197 -19.282  1.00 64.55           C  
-ANISOU 1293  CB  GLN A 636     9835   7359   7333   -205    756   -160       C  
-ATOM   1294  CG  GLN A 636     -13.417 -24.403 -18.302  1.00 76.48           C  
-ANISOU 1294  CG  GLN A 636    11488   8758   8813   -293    881   -161       C  
-ATOM   1295  CD  GLN A 636     -14.753 -23.941 -18.854  1.00 83.43           C  
-ANISOU 1295  CD  GLN A 636    12235   9682   9783   -368   1007   -155       C  
-ATOM   1296  OE1 GLN A 636     -15.378 -24.633 -19.658  1.00 88.66           O  
-ANISOU 1296  OE1 GLN A 636    12837  10374  10476   -391   1039   -166       O  
-ATOM   1297  NE2 GLN A 636     -15.201 -22.768 -18.419  1.00 80.04           N  
-ANISOU 1297  NE2 GLN A 636    11758   9255   9398   -406   1077   -143       N  
-ATOM   1298  N   SER A 637     -10.464 -22.039 -20.946  1.00 68.94           N  
-ANISOU 1298  N   SER A 637    10003   8174   8015    -91    604   -131       N  
-ATOM   1299  CA  SER A 637      -9.457 -21.757 -21.963  1.00 55.83           C  
-ANISOU 1299  CA  SER A 637     8193   6634   6387    -30    505   -135       C  
-ATOM   1300  C   SER A 637      -8.365 -20.874 -21.370  1.00 59.06           C  
-ANISOU 1300  C   SER A 637     8615   7046   6779     19    437   -135       C  
-ATOM   1301  O   SER A 637      -7.214 -20.914 -21.808  1.00 66.70           O  
-ANISOU 1301  O   SER A 637     9529   8076   7738     83    331   -156       O  
-ATOM   1302  CB  SER A 637     -10.083 -21.087 -23.186  1.00 37.60           C  
-ANISOU 1302  CB  SER A 637     5674   4439   4172    -63    553   -108       C  
-ATOM   1303  OG  SER A 637     -10.620 -19.823 -22.855  1.00 52.89           O  
-ANISOU 1303  OG  SER A 637     7559   6375   6162   -104    624    -75       O  
-ATOM   1304  N   ASP A 638      -8.738 -20.076 -20.372  1.00 47.22           N  
-ANISOU 1304  N   ASP A 638     7184   5480   5278    -14    499   -116       N  
-ATOM   1305  CA  ASP A 638      -7.775 -19.302 -19.597  1.00 37.03           C  
-ANISOU 1305  CA  ASP A 638     5936   4172   3964     28    441   -119       C  
-ATOM   1306  C   ASP A 638      -6.906 -20.247 -18.778  1.00 35.00           C  
-ANISOU 1306  C   ASP A 638     5861   3829   3608     84    352   -156       C  
-ATOM   1307  O   ASP A 638      -5.706 -20.024 -18.619  1.00 37.77           O  
-ANISOU 1307  O   ASP A 638     6214   4200   3936    151    251   -178       O  
-ATOM   1308  CB  ASP A 638      -8.494 -18.320 -18.667  1.00 46.57           C  
-ANISOU 1308  CB  ASP A 638     7184   5319   5190    -26    536    -95       C  
-ATOM   1309  CG  ASP A 638      -8.617 -16.927 -19.260  1.00 45.72           C  
-ANISOU 1309  CG  ASP A 638     6892   5302   5177    -42    564    -63       C  
-ATOM   1310  OD1 ASP A 638      -7.840 -16.593 -20.177  1.00 50.80           O  
-ANISOU 1310  OD1 ASP A 638     7400   6047   5854     -1    491    -60       O  
-ATOM   1311  OD2 ASP A 638      -9.487 -16.160 -18.797  1.00 43.64           O  
-ANISOU 1311  OD2 ASP A 638     6622   5006   4955    -97    657    -44       O  
-ATOM   1312  N   VAL A 639      -7.527 -21.303 -18.259  1.00 36.38           N  
-ANISOU 1312  N   VAL A 639     6190   3907   3725     54    388   -165       N  
-ATOM   1313  CA  VAL A 639      -6.820 -22.314 -17.479  1.00 40.95           C  
-ANISOU 1313  CA  VAL A 639     6960   4391   4207    102    303   -198       C  
-ATOM   1314  C   VAL A 639      -5.757 -23.011 -18.324  1.00 48.70           C  
-ANISOU 1314  C   VAL A 639     7880   5439   5185    181    175   -235       C  
-ATOM   1315  O   VAL A 639      -4.650 -23.276 -17.852  1.00 53.42           O  
-ANISOU 1315  O   VAL A 639     8562   6005   5732    252     63   -268       O  
-ATOM   1316  CB  VAL A 639      -7.789 -23.365 -16.902  1.00 49.22           C  
-ANISOU 1316  CB  VAL A 639     8179   5326   5198     45    374   -197       C  
-ATOM   1317  CG1 VAL A 639      -7.024 -24.444 -16.156  1.00 59.31           C  
-ANISOU 1317  CG1 VAL A 639     9659   6503   6375     97    272   -227       C  
-ATOM   1318  CG2 VAL A 639      -8.803 -22.705 -15.983  1.00 44.49           C  
-ANISOU 1318  CG2 VAL A 639     7650   4659   4597    -37    502   -171       C  
-ATOM   1319  N   TYR A 640      -6.100 -23.306 -19.575  1.00 44.36           N  
-ANISOU 1319  N   TYR A 640     7181   4981   4692    169    190   -234       N  
-ATOM   1320  CA  TYR A 640      -5.158 -23.916 -20.506  1.00 48.57           C  
-ANISOU 1320  CA  TYR A 640     7629   5593   5231    237     78   -274       C  
-ATOM   1321  C   TYR A 640      -3.960 -23.002 -20.741  1.00 46.66           C  
-ANISOU 1321  C   TYR A 640     7277   5438   5016    295     -5   -291       C  
-ATOM   1322  O   TYR A 640      -2.811 -23.441 -20.697  1.00 43.20           O  
-ANISOU 1322  O   TYR A 640     6867   5003   4544    369   -124   -340       O  
-ATOM   1323  CB  TYR A 640      -5.841 -24.230 -21.837  1.00 55.55           C  
-ANISOU 1323  CB  TYR A 640     8357   6573   6178    203    125   -266       C  
-ATOM   1324  CG  TYR A 640      -4.929 -24.902 -22.839  1.00 62.96           C  
-ANISOU 1324  CG  TYR A 640     9202   7597   7123    265     17   -314       C  
-ATOM   1325  CD1 TYR A 640      -4.880 -26.285 -22.943  1.00 61.95           C  
-ANISOU 1325  CD1 TYR A 640     9161   7422   6955    289    -31   -351       C  
-ATOM   1326  CD2 TYR A 640      -4.110 -24.153 -23.674  1.00 67.30           C  
-ANISOU 1326  CD2 TYR A 640     9577   8276   7719    297    -37   -324       C  
-ATOM   1327  CE1 TYR A 640      -4.046 -26.905 -23.855  1.00 61.14           C  
-ANISOU 1327  CE1 TYR A 640     8968   7400   6863    346   -130   -402       C  
-ATOM   1328  CE2 TYR A 640      -3.271 -24.762 -24.588  1.00 62.89           C  
-ANISOU 1328  CE2 TYR A 640     8928   7801   7166    349   -131   -376       C  
-ATOM   1329  CZ  TYR A 640      -3.244 -26.139 -24.675  1.00 57.29           C  
-ANISOU 1329  CZ  TYR A 640     8303   7045   6421    375   -178   -417       C  
-ATOM   1330  OH  TYR A 640      -2.412 -26.753 -25.582  1.00 47.45           O  
-ANISOU 1330  OH  TYR A 640     6962   5883   5185    427   -272   -476       O  
-ATOM   1331  N   ALA A 641      -4.239 -21.728 -20.998  1.00 45.56           N  
-ANISOU 1331  N   ALA A 641     7008   5366   4938    259     57   -253       N  
-ATOM   1332  CA  ALA A 641      -3.190 -20.734 -21.188  1.00 41.41           C  
-ANISOU 1332  CA  ALA A 641     6376   4919   4440    301     -7   -263       C  
-ATOM   1333  C   ALA A 641      -2.260 -20.692 -19.980  1.00 41.65           C  
-ANISOU 1333  C   ALA A 641     6554   4864   4406    358    -84   -293       C  
-ATOM   1334  O   ALA A 641      -1.061 -20.445 -20.113  1.00 35.97           O  
-ANISOU 1334  O   ALA A 641     5785   4194   3686    421   -182   -333       O  
-ATOM   1335  CB  ALA A 641      -3.796 -19.366 -21.441  1.00 42.04           C  
-ANISOU 1335  CB  ALA A 641     6327   5054   4590    246     82   -209       C  
-ATOM   1336  N   PHE A 642      -2.822 -20.925 -18.799  1.00 59.75           N  
-ANISOU 1336  N   PHE A 642     9029   7029   6645    332    -38   -278       N  
-ATOM   1337  CA  PHE A 642      -2.029 -20.979 -17.578  1.00 62.64           C  
-ANISOU 1337  CA  PHE A 642     9560   7301   6940    383   -110   -306       C  
-ATOM   1338  C   PHE A 642      -1.136 -22.216 -17.590  1.00 57.63           C  
-ANISOU 1338  C   PHE A 642     9015   6634   6249    458   -238   -364       C  
-ATOM   1339  O   PHE A 642       0.027 -22.156 -17.192  1.00 47.61           O  
-ANISOU 1339  O   PHE A 642     7782   5356   4952    531   -348   -409       O  
-ATOM   1340  CB  PHE A 642      -2.937 -20.982 -16.345  1.00 60.49           C  
-ANISOU 1340  CB  PHE A 642     9466   6899   6617    326    -22   -274       C  
-ATOM   1341  CG  PHE A 642      -2.191 -20.969 -15.040  1.00 65.81           C  
-ANISOU 1341  CG  PHE A 642    10317   7474   7213    372    -90   -297       C  
-ATOM   1342  CD1 PHE A 642      -1.533 -19.826 -14.616  1.00 61.50           C  
-ANISOU 1342  CD1 PHE A 642     9727   6954   6686    398   -113   -300       C  
-ATOM   1343  CD2 PHE A 642      -2.154 -22.097 -14.235  1.00 71.22           C  
-ANISOU 1343  CD2 PHE A 642    11217   8038   7806    387   -134   -316       C  
-ATOM   1344  CE1 PHE A 642      -0.848 -19.809 -13.415  1.00 64.03           C  
-ANISOU 1344  CE1 PHE A 642    10210   7185   6935    441   -179   -323       C  
-ATOM   1345  CE2 PHE A 642      -1.470 -22.087 -13.032  1.00 72.13           C  
-ANISOU 1345  CE2 PHE A 642    11502   8059   7846    430   -203   -335       C  
-ATOM   1346  CZ  PHE A 642      -0.816 -20.941 -12.623  1.00 69.97           C  
-ANISOU 1346  CZ  PHE A 642    11177   7817   7592    458   -226   -341       C  
-ATOM   1347  N   GLY A 643      -1.686 -23.333 -18.058  1.00 47.47           N  
-ANISOU 1347  N   GLY A 643     7759   5329   4950    441   -226   -368       N  
-ATOM   1348  CA  GLY A 643      -0.934 -24.570 -18.169  1.00 43.88           C  
-ANISOU 1348  CA  GLY A 643     7379   4843   4450    510   -346   -425       C  
-ATOM   1349  C   GLY A 643       0.303 -24.414 -19.032  1.00 52.76           C  
-ANISOU 1349  C   GLY A 643     8347   6083   5614    583   -457   -482       C  
-ATOM   1350  O   GLY A 643       1.367 -24.945 -18.711  1.00 57.01           O  
-ANISOU 1350  O   GLY A 643     8956   6589   6114    663   -585   -542       O  
-ATOM   1351  N   ILE A 644       0.163 -23.686 -20.136  1.00 50.32           N  
-ANISOU 1351  N   ILE A 644     7827   5910   5382    553   -410   -465       N  
-ATOM   1352  CA  ILE A 644       1.295 -23.406 -21.010  1.00 48.82           C  
-ANISOU 1352  CA  ILE A 644     7474   5844   5232    608   -499   -517       C  
-ATOM   1353  C   ILE A 644       2.314 -22.548 -20.274  1.00 51.03           C  
-ANISOU 1353  C   ILE A 644     7773   6114   5500    656   -562   -541       C  
-ATOM   1354  O   ILE A 644       3.521 -22.762 -20.388  1.00 51.43           O  
-ANISOU 1354  O   ILE A 644     7799   6197   5544    731   -680   -613       O  
-ATOM   1355  CB  ILE A 644       0.857 -22.679 -22.294  1.00 42.17           C  
-ANISOU 1355  CB  ILE A 644     6410   5144   4468    554   -424   -483       C  
-ATOM   1356  CG1 ILE A 644      -0.196 -23.500 -23.041  1.00 34.99           C  
-ANISOU 1356  CG1 ILE A 644     5476   4247   3574    505   -359   -460       C  
-ATOM   1357  CG2 ILE A 644       2.058 -22.405 -23.190  1.00 36.75           C  
-ANISOU 1357  CG2 ILE A 644     5560   4587   3815    602   -513   -541       C  
-ATOM   1358  CD1 ILE A 644       0.318 -24.823 -23.543  1.00 35.00           C  
-ANISOU 1358  CD1 ILE A 644     5490   4255   3552    557   -452   -526       C  
-ATOM   1359  N   VAL A 645       1.817 -21.572 -19.519  1.00 54.17           N  
-ANISOU 1359  N   VAL A 645     8212   6469   5899    614   -482   -487       N  
-ATOM   1360  CA  VAL A 645       2.676 -20.722 -18.708  1.00 43.71           C  
-ANISOU 1360  CA  VAL A 645     6919   5126   4563    654   -531   -506       C  
-ATOM   1361  C   VAL A 645       3.438 -21.576 -17.702  1.00 42.45           C  
-ANISOU 1361  C   VAL A 645     6952   4854   4325    729   -646   -562       C  
-ATOM   1362  O   VAL A 645       4.643 -21.407 -17.517  1.00 47.68           O  
-ANISOU 1362  O   VAL A 645     7600   5535   4982    802   -754   -623       O  
-ATOM   1363  CB  VAL A 645       1.868 -19.636 -17.977  1.00 45.34           C  
-ANISOU 1363  CB  VAL A 645     7157   5290   4780    591   -419   -438       C  
-ATOM   1364  CG1 VAL A 645       2.768 -18.842 -17.043  1.00 45.31           C  
-ANISOU 1364  CG1 VAL A 645     7203   5255   4758    636   -475   -462       C  
-ATOM   1365  CG2 VAL A 645       1.192 -18.716 -18.983  1.00 35.38           C  
-ANISOU 1365  CG2 VAL A 645     5702   4140   3603    524   -322   -386       C  
-ATOM   1366  N   LEU A 646       2.729 -22.502 -17.062  1.00 39.28           N  
-ANISOU 1366  N   LEU A 646     6729   4333   3863    710   -623   -542       N  
-ATOM   1367  CA  LEU A 646       3.361 -23.464 -16.169  1.00 43.37           C  
-ANISOU 1367  CA  LEU A 646     7443   4733   4301    778   -737   -590       C  
-ATOM   1368  C   LEU A 646       4.477 -24.180 -16.913  1.00 58.12           C  
-ANISOU 1368  C   LEU A 646     9236   6662   6184    862   -874   -675       C  
-ATOM   1369  O   LEU A 646       5.577 -24.353 -16.390  1.00 67.76           O  
-ANISOU 1369  O   LEU A 646    10523   7849   7376    945  -1000   -739       O  
-ATOM   1370  CB  LEU A 646       2.344 -24.490 -15.664  1.00 49.20           C  
-ANISOU 1370  CB  LEU A 646     8364   5350   4979    734   -686   -555       C  
-ATOM   1371  CG  LEU A 646       1.174 -23.981 -14.820  1.00 53.53           C  
-ANISOU 1371  CG  LEU A 646     9016   5822   5502    646   -549   -482       C  
-ATOM   1372  CD1 LEU A 646       0.286 -25.136 -14.375  1.00 39.51           C  
-ANISOU 1372  CD1 LEU A 646     7423   3928   3661    603   -510   -460       C  
-ATOM   1373  CD2 LEU A 646       1.684 -23.203 -13.618  1.00 65.97           C  
-ANISOU 1373  CD2 LEU A 646    10695   7335   7037    669   -575   -484       C  
-ATOM   1374  N   TYR A 647       4.179 -24.593 -18.141  1.00 56.57           N  
-ANISOU 1374  N   TYR A 647     8898   6559   6036    840   -850   -679       N  
-ATOM   1375  CA  TYR A 647       5.140 -25.292 -18.982  1.00 57.43           C  
-ANISOU 1375  CA  TYR A 647     8914   6740   6168    910   -967   -764       C  
-ATOM   1376  C   TYR A 647       6.375 -24.436 -19.240  1.00 56.29           C  
-ANISOU 1376  C   TYR A 647     8633   6694   6062    962  -1041   -822       C  
-ATOM   1377  O   TYR A 647       7.502 -24.929 -19.198  1.00 57.08           O  
-ANISOU 1377  O   TYR A 647     8743   6793   6152   1047  -1176   -912       O  
-ATOM   1378  CB  TYR A 647       4.489 -25.689 -20.307  1.00 60.79           C  
-ANISOU 1378  CB  TYR A 647     9191   7263   6643    862   -906   -749       C  
-ATOM   1379  CG  TYR A 647       5.426 -26.385 -21.268  1.00 62.63           C  
-ANISOU 1379  CG  TYR A 647     9310   7584   6904    924  -1016   -840       C  
-ATOM   1380  CD1 TYR A 647       5.523 -27.769 -21.293  1.00 51.58           C  
-ANISOU 1380  CD1 TYR A 647     8006   6118   5474    967  -1095   -887       C  
-ATOM   1381  CD2 TYR A 647       6.212 -25.656 -22.150  1.00 60.08           C  
-ANISOU 1381  CD2 TYR A 647     8783   7407   6638    937  -1040   -881       C  
-ATOM   1382  CE1 TYR A 647       6.376 -28.409 -22.168  1.00 43.11           C  
-ANISOU 1382  CE1 TYR A 647     6823   5126   4431   1024  -1197   -978       C  
-ATOM   1383  CE2 TYR A 647       7.068 -26.286 -23.029  1.00 53.49           C  
-ANISOU 1383  CE2 TYR A 647     7838   6656   5828    989  -1136   -972       C  
-ATOM   1384  CZ  TYR A 647       7.146 -27.662 -23.035  1.00 51.26           C  
-ANISOU 1384  CZ  TYR A 647     7648   6309   5519   1035  -1215  -1023       C  
-ATOM   1385  OH  TYR A 647       7.999 -28.289 -23.911  1.00 59.55           O  
-ANISOU 1385  OH  TYR A 647     8583   7444   6598   1087  -1312  -1122       O  
-ATOM   1386  N   GLU A 648       6.156 -23.154 -19.512  1.00 55.21           N  
-ANISOU 1386  N   GLU A 648     8365   6640   5972    910   -952   -776       N  
-ATOM   1387  CA  GLU A 648       7.257 -22.224 -19.728  1.00 57.84           C  
-ANISOU 1387  CA  GLU A 648     8569   7066   6344    947  -1006   -824       C  
-ATOM   1388  C   GLU A 648       8.161 -22.185 -18.508  1.00 63.51           C  
-ANISOU 1388  C   GLU A 648     9430   7688   7012   1023  -1108   -874       C  
-ATOM   1389  O   GLU A 648       9.381 -22.272 -18.624  1.00 64.45           O  
-ANISOU 1389  O   GLU A 648     9500   7847   7141   1098  -1225   -965       O  
-ATOM   1390  CB  GLU A 648       6.731 -20.815 -20.001  1.00 58.05           C  
-ANISOU 1390  CB  GLU A 648     8469   7167   6420    873   -887   -751       C  
-ATOM   1391  CG  GLU A 648       5.905 -20.677 -21.261  1.00 50.82           C  
-ANISOU 1391  CG  GLU A 648     7395   6356   5558    799   -792   -702       C  
-ATOM   1392  CD  GLU A 648       5.624 -19.229 -21.602  1.00 57.19           C  
-ANISOU 1392  CD  GLU A 648     8065   7245   6421    738   -702   -642       C  
-ATOM   1393  OE1 GLU A 648       6.589 -18.484 -21.871  1.00 51.65           O  
-ANISOU 1393  OE1 GLU A 648     7252   6624   5748    762   -747   -682       O  
-ATOM   1394  OE2 GLU A 648       4.440 -18.833 -21.599  1.00 64.40           O  
-ANISOU 1394  OE2 GLU A 648     8980   8139   7352    665   -587   -560       O  
-ATOM   1395  N   LEU A 649       7.549 -22.047 -17.337  1.00 74.42           N  
-ANISOU 1395  N   LEU A 649    10988   8946   8343   1002  -1063   -818       N  
-ATOM   1396  CA  LEU A 649       8.288 -21.946 -16.085  1.00 74.17           C  
-ANISOU 1396  CA  LEU A 649    11108   8815   8258   1066  -1150   -855       C  
-ATOM   1397  C   LEU A 649       9.050 -23.228 -15.765  1.00 80.36           C  
-ANISOU 1397  C   LEU A 649    12020   9520   8991   1156  -1301   -936       C  
-ATOM   1398  O   LEU A 649      10.212 -23.184 -15.364  1.00 83.81           O  
-ANISOU 1398  O   LEU A 649    12476   9948   9420   1240  -1424  -1015       O  
-ATOM   1399  CB  LEU A 649       7.341 -21.597 -14.932  1.00 51.14           C  
-ANISOU 1399  CB  LEU A 649     8360   5782   5291   1011  -1058   -774       C  
-ATOM   1400  CG  LEU A 649       6.626 -20.243 -14.984  1.00 44.71           C  
-ANISOU 1400  CG  LEU A 649     7444   5020   4523    930   -919   -699       C  
-ATOM   1401  CD1 LEU A 649       5.457 -20.214 -14.013  1.00 36.77           C  
-ANISOU 1401  CD1 LEU A 649     6605   3899   3468    864   -815   -624       C  
-ATOM   1402  CD2 LEU A 649       7.590 -19.099 -14.701  1.00 50.64           C  
-ANISOU 1402  CD2 LEU A 649     8118   5821   5303    968   -960   -733       C  
-ATOM   1403  N   MET A 650       8.396 -24.370 -15.950  1.00 77.42           N  
-ANISOU 1403  N   MET A 650    11735   9092   8591   1141  -1295   -920       N  
-ATOM   1404  CA  MET A 650       8.971 -25.648 -15.536  1.00 77.61           C  
-ANISOU 1404  CA  MET A 650    11910   9016   8561   1221  -1435   -986       C  
-ATOM   1405  C   MET A 650       9.951 -26.259 -16.536  1.00 77.47           C  
-ANISOU 1405  C   MET A 650    11755   9090   8591   1291  -1552  -1089       C  
-ATOM   1406  O   MET A 650      10.716 -27.159 -16.189  1.00 86.84           O  
-ANISOU 1406  O   MET A 650    13043  10207   9747   1377  -1696  -1167       O  
-ATOM   1407  CB  MET A 650       7.863 -26.642 -15.189  1.00 65.47           C  
-ANISOU 1407  CB  MET A 650    10547   7363   6967   1173  -1383   -926       C  
-ATOM   1408  CG  MET A 650       7.040 -26.205 -13.987  1.00 69.83           C  
-ANISOU 1408  CG  MET A 650    11275   7802   7456   1115  -1292   -844       C  
-ATOM   1409  SD  MET A 650       8.087 -25.714 -12.597  1.00 98.36           S  
-ANISOU 1409  SD  MET A 650    15035  11326  11012   1192  -1404   -884       S  
-ATOM   1410  CE  MET A 650       6.898 -24.924 -11.511  1.00 69.32           C  
-ANISOU 1410  CE  MET A 650    11490   7564   7283   1092  -1247   -778       C  
-ATOM   1411  N   THR A 651       9.932 -25.767 -17.770  1.00 65.69           N  
-ANISOU 1411  N   THR A 651    10033   7753   7173   1254  -1492  -1094       N  
-ATOM   1412  CA  THR A 651      10.836 -26.270 -18.797  1.00 71.09           C  
-ANISOU 1412  CA  THR A 651    10566   8540   7905   1309  -1588  -1195       C  
-ATOM   1413  C   THR A 651      11.828 -25.199 -19.235  1.00 77.51           C  
-ANISOU 1413  C   THR A 651    11194   9483   8774   1329  -1611  -1252       C  
-ATOM   1414  O   THR A 651      12.912 -25.508 -19.725  1.00 81.89           O  
-ANISOU 1414  O   THR A 651    11654  10103   9358   1396  -1722  -1363       O  
-ATOM   1415  CB  THR A 651      10.068 -26.765 -20.036  1.00 60.22           C  
-ANISOU 1415  CB  THR A 651     9067   7248   6566   1249  -1512  -1169       C  
-ATOM   1416  OG1 THR A 651       9.595 -25.641 -20.787  1.00 65.46           O  
-ANISOU 1416  OG1 THR A 651     9553   8038   7282   1168  -1384  -1108       O  
-ATOM   1417  CG2 THR A 651       8.893 -27.641 -19.623  1.00 55.89           C  
-ANISOU 1417  CG2 THR A 651     8689   6578   5967   1208  -1455  -1097       C  
-ATOM   1418  N   GLY A 652      11.451 -23.938 -19.058  1.00 80.68           N  
-ANISOU 1418  N   GLY A 652    11542   9920   9191   1268  -1504  -1180       N  
-ATOM   1419  CA  GLY A 652      12.302 -22.834 -19.460  1.00 78.47           C  
-ANISOU 1419  CA  GLY A 652    11091   9761   8963   1274  -1510  -1222       C  
-ATOM   1420  C   GLY A 652      12.261 -22.603 -20.957  1.00 74.70           C  
-ANISOU 1420  C   GLY A 652    10384   9449   8550   1223  -1456  -1230       C  
-ATOM   1421  O   GLY A 652      13.104 -21.897 -21.511  1.00 73.86           O  
-ANISOU 1421  O   GLY A 652    10118   9458   8489   1230  -1476  -1286       O  
-ATOM   1422  N   GLN A 653      11.272 -23.199 -21.615  1.00 73.42           N  
-ANISOU 1422  N   GLN A 653    10208   9299   8391   1168  -1384  -1175       N  
-ATOM   1423  CA  GLN A 653      11.131 -23.062 -23.059  1.00 71.17           C  
-ANISOU 1423  CA  GLN A 653     9716   9167   8160   1116  -1330  -1177       C  
-ATOM   1424  C   GLN A 653       9.680 -23.193 -23.504  1.00 62.06           C  
-ANISOU 1424  C   GLN A 653     8562   8010   7009   1029  -1201  -1070       C  
-ATOM   1425  O   GLN A 653       8.844 -23.747 -22.790  1.00 53.72           O  
-ANISOU 1425  O   GLN A 653     7671   6830   5911   1019  -1171  -1016       O  
-ATOM   1426  CB  GLN A 653      11.994 -24.099 -23.776  1.00 64.06           C  
-ANISOU 1426  CB  GLN A 653     8746   8321   7271   1178  -1445  -1297       C  
-ATOM   1427  CG  GLN A 653      11.665 -25.529 -23.404  1.00 64.40           C  
-ANISOU 1427  CG  GLN A 653     8949   8247   7274   1222  -1507  -1314       C  
-ATOM   1428  CD  GLN A 653      12.768 -26.488 -23.790  1.00 72.82           C  
-ANISOU 1428  CD  GLN A 653     9974   9341   8352   1308  -1654  -1453       C  
-ATOM   1429  OE1 GLN A 653      13.898 -26.076 -24.049  1.00 83.48           O  
-ANISOU 1429  OE1 GLN A 653    11211  10775   9733   1349  -1724  -1547       O  
-ATOM   1430  NE2 GLN A 653      12.449 -27.775 -23.826  1.00 71.44           N  
-ANISOU 1430  NE2 GLN A 653     9893   9095   8156   1336  -1702  -1473       N  
-ATOM   1431  N   LEU A 654       9.396 -22.681 -24.696  1.00 54.49           N  
-ANISOU 1431  N   LEU A 654     7417   7188   6098    964  -1127  -1042       N  
-ATOM   1432  CA  LEU A 654       8.051 -22.710 -25.256  1.00 53.80           C  
-ANISOU 1432  CA  LEU A 654     7302   7115   6023    881  -1006   -947       C  
-ATOM   1433  C   LEU A 654       7.710 -24.085 -25.820  1.00 56.34           C  
-ANISOU 1433  C   LEU A 654     7643   7429   6335    893  -1033   -978       C  
-ATOM   1434  O   LEU A 654       8.602 -24.855 -26.175  1.00 73.95           O  
-ANISOU 1434  O   LEU A 654     9840   9691   8565    954  -1139  -1079       O  
-ATOM   1435  CB  LEU A 654       7.914 -21.647 -26.348  1.00 50.89           C  
-ANISOU 1435  CB  LEU A 654     6731   6897   5709    810   -927   -908       C  
-ATOM   1436  CG  LEU A 654       7.986 -20.190 -25.891  1.00 52.65           C  
-ANISOU 1436  CG  LEU A 654     6925   7128   5950    779   -875   -855       C  
-ATOM   1437  CD1 LEU A 654       8.244 -19.254 -27.066  1.00 43.41           C  
-ANISOU 1437  CD1 LEU A 654     5547   6118   4831    725   -836   -846       C  
-ATOM   1438  CD2 LEU A 654       6.710 -19.804 -25.157  1.00 57.37           C  
-ANISOU 1438  CD2 LEU A 654     7633   7625   6539    727   -770   -748       C  
-ATOM   1439  N   PRO A 655       6.409 -24.400 -25.894  1.00 45.52           N  
-ANISOU 1439  N   PRO A 655     6323   6014   4958    833   -937   -897       N  
-ATOM   1440  CA  PRO A 655       5.953 -25.662 -26.482  1.00 48.41           C  
-ANISOU 1440  CA  PRO A 655     6700   6374   5318    834   -948   -917       C  
-ATOM   1441  C   PRO A 655       6.219 -25.697 -27.981  1.00 52.99           C  
-ANISOU 1441  C   PRO A 655     7069   7120   5945    813   -948   -956       C  
-ATOM   1442  O   PRO A 655       6.303 -24.647 -28.619  1.00 55.51           O  
-ANISOU 1442  O   PRO A 655     7240   7552   6300    767   -897   -929       O  
-ATOM   1443  CB  PRO A 655       4.441 -25.644 -26.226  1.00 46.13           C  
-ANISOU 1443  CB  PRO A 655     6490   6015   5023    760   -821   -812       C  
-ATOM   1444  CG  PRO A 655       4.241 -24.659 -25.123  1.00 52.12           C  
-ANISOU 1444  CG  PRO A 655     7343   6695   5764    744   -775   -754       C  
-ATOM   1445  CD  PRO A 655       5.298 -23.623 -25.323  1.00 52.94           C  
-ANISOU 1445  CD  PRO A 655     7325   6893   5896    766   -817   -788       C  
-ATOM   1446  N   TYR A 656       6.359 -26.898 -28.529  1.00 52.47           N  
-ANISOU 1446  N   TYR A 656     6993   7067   5877    844  -1007  -1021       N  
-ATOM   1447  CA  TYR A 656       6.498 -27.074 -29.969  1.00 49.00           C  
-ANISOU 1447  CA  TYR A 656     6362   6781   5476    818  -1001  -1059       C  
-ATOM   1448  C   TYR A 656       7.685 -26.301 -30.545  1.00 47.41           C  
-ANISOU 1448  C   TYR A 656     6000   6714   5301    831  -1050  -1125       C  
-ATOM   1449  O   TYR A 656       7.628 -25.816 -31.674  1.00 42.87           O  
-ANISOU 1449  O   TYR A 656     5251   6279   4756    776  -1001  -1115       O  
-ATOM   1450  CB  TYR A 656       5.206 -26.654 -30.676  1.00 57.83           C  
-ANISOU 1450  CB  TYR A 656     7404   7952   6618    724   -867   -957       C  
-ATOM   1451  CG  TYR A 656       3.951 -26.912 -29.867  1.00 60.29           C  
-ANISOU 1451  CG  TYR A 656     7875   8126   6906    693   -788   -872       C  
-ATOM   1452  CD1 TYR A 656       3.633 -28.190 -29.430  1.00 55.80           C  
-ANISOU 1452  CD1 TYR A 656     7449   7447   6307    725   -823   -895       C  
-ATOM   1453  CD2 TYR A 656       3.079 -25.876 -29.550  1.00 58.20           C  
-ANISOU 1453  CD2 TYR A 656     7620   7842   6653    628   -679   -771       C  
-ATOM   1454  CE1 TYR A 656       2.488 -28.430 -28.694  1.00 54.08           C  
-ANISOU 1454  CE1 TYR A 656     7378   7106   6065    688   -745   -822       C  
-ATOM   1455  CE2 TYR A 656       1.930 -26.107 -28.815  1.00 49.30           C  
-ANISOU 1455  CE2 TYR A 656     6632   6594   5507    594   -602   -703       C  
-ATOM   1456  CZ  TYR A 656       1.640 -27.386 -28.391  1.00 49.22           C  
-ANISOU 1456  CZ  TYR A 656     6762   6478   5461    621   -632   -729       C  
-ATOM   1457  OH  TYR A 656       0.500 -27.625 -27.660  1.00 47.45           O  
-ANISOU 1457  OH  TYR A 656     6679   6135   5215    580   -550   -665       O  
-ATOM   1458  N   SER A 657       8.757 -26.188 -29.767  1.00 71.23           N  
-ANISOU 1458  N   SER A 657     9076   9686   8304    902  -1145  -1194       N  
-ATOM   1459  CA  SER A 657       9.965 -25.516 -30.234  1.00 76.81           C  
-ANISOU 1459  CA  SER A 657     9637  10511   9035    919  -1197  -1272       C  
-ATOM   1460  C   SER A 657      10.583 -26.279 -31.400  1.00 79.48           C  
-ANISOU 1460  C   SER A 657     9832  10970   9395    934  -1257  -1378       C  
-ATOM   1461  O   SER A 657      11.036 -25.682 -32.376  1.00 80.32           O  
-ANISOU 1461  O   SER A 657     9762  11228   9530    894  -1237  -1406       O  
-ATOM   1462  CB  SER A 657      10.979 -25.368 -29.099  1.00 79.38           C  
-ANISOU 1462  CB  SER A 657    10066  10752   9341   1000  -1297  -1337       C  
-ATOM   1463  OG  SER A 657      10.504 -24.475 -28.108  1.00 77.50           O  
-ANISOU 1463  OG  SER A 657     9933  10426   9086    978  -1236  -1244       O  
-ATOM   1464  N   ASN A 658      10.595 -27.603 -31.290  1.00 69.44           N  
-ANISOU 1464  N   ASN A 658     8641   9632   8111    990  -1330  -1438       N  
-ATOM   1465  CA  ASN A 658      11.093 -28.454 -32.361  1.00 68.49           C  
-ANISOU 1465  CA  ASN A 658     8395   9615   8013   1007  -1388  -1542       C  
-ATOM   1466  C   ASN A 658      10.288 -28.249 -33.642  1.00 76.62           C  
-ANISOU 1466  C   ASN A 658     9275  10773   9063    915  -1281  -1483       C  
-ATOM   1467  O   ASN A 658      10.836 -28.282 -34.744  1.00 85.94           O  
-ANISOU 1467  O   ASN A 658    10285  12100  10267    897  -1296  -1555       O  
-ATOM   1468  CB  ASN A 658      11.048 -29.923 -31.937  1.00 79.71           C  
-ANISOU 1468  CB  ASN A 658     9950  10919   9418   1079  -1477  -1598       C  
-ATOM   1469  CG  ASN A 658      12.272 -30.695 -32.383  1.00 90.16           C  
-ANISOU 1469  CG  ASN A 658    11192  12301  10763   1153  -1610  -1760       C  
-ATOM   1470  OD1 ASN A 658      13.368 -30.142 -32.479  1.00 90.49           O  
-ANISOU 1470  OD1 ASN A 658    11140  12420  10823   1179  -1665  -1844       O  
-ATOM   1471  ND2 ASN A 658      12.094 -31.984 -32.649  1.00 93.15           N  
-ANISOU 1471  ND2 ASN A 658    11604  12643  11144   1188  -1664  -1811       N  
-ATOM   1472  N   ILE A 659       8.986 -28.032 -33.487  1.00 88.19           N  
-ANISOU 1472  N   ILE A 659    10806  12183  10520    856  -1174  -1356       N  
-ATOM   1473  CA  ILE A 659       8.098 -27.799 -34.621  1.00 81.27           C  
-ANISOU 1473  CA  ILE A 659     9804  11414   9662    769  -1071  -1289       C  
-ATOM   1474  C   ILE A 659       7.896 -26.304 -34.854  1.00 93.81           C  
-ANISOU 1474  C   ILE A 659    11304  13077  11263    696   -982  -1204       C  
-ATOM   1475  O   ILE A 659       7.008 -25.696 -34.256  1.00102.93           O  
-ANISOU 1475  O   ILE A 659    12541  14153  12413    660   -903  -1095       O  
-ATOM   1476  CB  ILE A 659       6.715 -28.441 -34.385  1.00 51.46           C  
-ANISOU 1476  CB  ILE A 659     6140   7537   5875    742  -1001  -1204       C  
-ATOM   1477  CG1 ILE A 659       6.857 -29.926 -34.044  1.00 48.72           C  
-ANISOU 1477  CG1 ILE A 659     5904   7096   5513    812  -1089  -1279       C  
-ATOM   1478  CG2 ILE A 659       5.819 -28.246 -35.599  1.00 40.02           C  
-ANISOU 1478  CG2 ILE A 659     4555   6201   4448    658   -904  -1145       C  
-ATOM   1479  CD1 ILE A 659       5.540 -30.607 -33.727  1.00 52.67           C  
-ANISOU 1479  CD1 ILE A 659     6528   7486   6000    785  -1023  -1203       C  
-ATOM   1480  N   ASN A 660       8.712 -25.710 -35.719  1.00 80.02           N  
-ANISOU 1480  N   ASN A 660     9392  11479   9534    672   -995  -1255       N  
-ATOM   1481  CA  ASN A 660       8.594 -24.281 -36.001  1.00 65.24           C  
-ANISOU 1481  CA  ASN A 660     7433   9681   7674    601   -918  -1176       C  
-ATOM   1482  C   ASN A 660       7.679 -23.980 -37.185  1.00 58.82           C  
-ANISOU 1482  C   ASN A 660     6501   8973   6875    510   -824  -1100       C  
-ATOM   1483  O   ASN A 660       8.087 -23.339 -38.153  1.00 62.63           O  
-ANISOU 1483  O   ASN A 660     6831   9598   7367    458   -806  -1110       O  
-ATOM   1484  CB  ASN A 660       9.970 -23.646 -36.221  1.00 60.25           C  
-ANISOU 1484  CB  ASN A 660     6695   9147   7049    614   -976  -1264       C  
-ATOM   1485  CG  ASN A 660       9.890 -22.145 -36.447  1.00 61.90           C  
-ANISOU 1485  CG  ASN A 660     6826   9423   7271    540   -901  -1183       C  
-ATOM   1486  OD1 ASN A 660       8.907 -21.501 -36.077  1.00 73.55           O  
-ANISOU 1486  OD1 ASN A 660     8359  10835   8749    499   -820  -1063       O  
-ATOM   1487  ND2 ASN A 660      10.925 -21.581 -37.059  1.00 51.29           N  
-ANISOU 1487  ND2 ASN A 660     5348   8205   5935    521   -927  -1251       N  
-ATOM   1488  N   ASN A 661       6.440 -24.451 -37.101  1.00 42.10           N  
-ANISOU 1488  N   ASN A 661     4455   6783   4756    490   -765  -1025       N  
-ATOM   1489  CA  ASN A 661       5.444 -24.162 -38.123  1.00 43.46           C  
-ANISOU 1489  CA  ASN A 661     4530   7038   4944    408   -676   -945       C  
-ATOM   1490  C   ASN A 661       4.083 -23.851 -37.519  1.00 49.14           C  
-ANISOU 1490  C   ASN A 661     5354   7648   5671    376   -587   -826       C  
-ATOM   1491  O   ASN A 661       3.427 -24.717 -36.941  1.00 47.37           O  
-ANISOU 1491  O   ASN A 661     5249   7311   5437    403   -581   -818       O  
-ATOM   1492  CB  ASN A 661       5.329 -25.311 -39.121  1.00 57.46           C  
-ANISOU 1492  CB  ASN A 661     6231   8886   6718    409   -697  -1007       C  
-ATOM   1493  CG  ASN A 661       4.372 -25.001 -40.260  1.00 66.22           C  
-ANISOU 1493  CG  ASN A 661     7228  10091   7840    325   -612   -932       C  
-ATOM   1494  OD1 ASN A 661       3.302 -24.425 -40.055  1.00 71.29           O  
-ANISOU 1494  OD1 ASN A 661     7909  10683   8495    281   -531   -824       O  
-ATOM   1495  ND2 ASN A 661       4.755 -25.387 -41.470  1.00 62.70           N  
-ANISOU 1495  ND2 ASN A 661     6641   9786   7394    302   -632   -995       N  
-ATOM   1496  N   ARG A 662       3.669 -22.601 -37.672  1.00 63.81           N  
-ANISOU 1496  N   ARG A 662     7160   9538   7546    315   -518   -736       N  
-ATOM   1497  CA  ARG A 662       2.405 -22.128 -37.136  1.00 66.94           C  
-ANISOU 1497  CA  ARG A 662     7636   9841   7959    279   -431   -627       C  
-ATOM   1498  C   ARG A 662       1.232 -22.989 -37.598  1.00 65.37           C  
-ANISOU 1498  C   ARG A 662     7446   9625   7767    255   -382   -600       C  
-ATOM   1499  O   ARG A 662       0.573 -23.635 -36.786  1.00 68.88           O  
-ANISOU 1499  O   ARG A 662     8025   9943   8204    278   -364   -587       O  
-ATOM   1500  CB  ARG A 662       2.193 -20.675 -37.547  1.00 66.98           C  
-ANISOU 1500  CB  ARG A 662     7547   9914   7989    212   -374   -546       C  
-ATOM   1501  CG  ARG A 662       1.041 -19.997 -36.860  1.00 74.90           C  
-ANISOU 1501  CG  ARG A 662     8628  10816   9015    181   -293   -443       C  
-ATOM   1502  CD  ARG A 662       1.397 -18.566 -36.527  1.00 83.67           C  
-ANISOU 1502  CD  ARG A 662     9715  11935  10143    157   -279   -395       C  
-ATOM   1503  NE  ARG A 662       0.201 -17.771 -36.280  1.00 92.14           N  
-ANISOU 1503  NE  ARG A 662    10809  12950  11250    109   -194   -293       N  
-ATOM   1504  CZ  ARG A 662       0.212 -16.496 -35.911  1.00 98.35           C  
-ANISOU 1504  CZ  ARG A 662    11586  13722  12061     84   -168   -236       C  
-ATOM   1505  NH1 ARG A 662       1.363 -15.863 -35.736  1.00 98.97           N  
-ANISOU 1505  NH1 ARG A 662    11636  13838  12130    100   -216   -269       N  
-ATOM   1506  NH2 ARG A 662      -0.931 -15.855 -35.713  1.00 99.67           N  
-ANISOU 1506  NH2 ARG A 662    11769  13835  12265     42    -94   -152       N  
-ATOM   1507  N   ASP A 663       0.980 -22.997 -38.904  1.00 58.20           N  
-ANISOU 1507  N   ASP A 663     6397   8845   6872    207   -360   -593       N  
-ATOM   1508  CA  ASP A 663      -0.113 -23.781 -39.471  1.00 51.52           C  
-ANISOU 1508  CA  ASP A 663     5540   7998   6036    181   -314   -571       C  
-ATOM   1509  C   ASP A 663      -0.070 -25.238 -39.027  1.00 44.92           C  
-ANISOU 1509  C   ASP A 663     4806   7081   5181    241   -358   -643       C  
-ATOM   1510  O   ASP A 663      -1.107 -25.877 -38.860  1.00 48.20           O  
-ANISOU 1510  O   ASP A 663     5288   7423   5603    231   -311   -614       O  
-ATOM   1511  CB  ASP A 663      -0.109 -23.698 -40.998  1.00 63.49           C  
-ANISOU 1511  CB  ASP A 663     6884   9679   7560    130   -306   -576       C  
-ATOM   1512  CG  ASP A 663      -0.738 -22.421 -41.512  1.00 66.54           C  
-ANISOU 1512  CG  ASP A 663     7190  10120   7971     58   -240   -477       C  
-ATOM   1513  OD1 ASP A 663      -0.539 -21.363 -40.880  1.00 69.27           O  
-ANISOU 1513  OD1 ASP A 663     7567  10427   8325     51   -228   -431       O  
-ATOM   1514  OD2 ASP A 663      -1.434 -22.479 -42.547  1.00 59.47           O  
-ANISOU 1514  OD2 ASP A 663     6203   9305   7089      9   -203   -445       O  
-ATOM   1515  N   GLN A 664       1.133 -25.760 -38.836  1.00 47.78           N  
-ANISOU 1515  N   GLN A 664     5180   7454   5521    301   -451   -739       N  
-ATOM   1516  CA  GLN A 664       1.296 -27.129 -38.380  1.00 51.09           C  
-ANISOU 1516  CA  GLN A 664     5701   7789   5922    363   -509   -812       C  
-ATOM   1517  C   GLN A 664       0.775 -27.266 -36.948  1.00 51.90           C  
-ANISOU 1517  C   GLN A 664     5998   7711   6010    390   -489   -771       C  
-ATOM   1518  O   GLN A 664      -0.033 -28.144 -36.649  1.00 53.95           O  
-ANISOU 1518  O   GLN A 664     6354   7882   6265    393   -464   -761       O  
-ATOM   1519  CB  GLN A 664       2.767 -27.531 -38.470  1.00 51.22           C  
-ANISOU 1519  CB  GLN A 664     5681   7857   5925    425   -620   -930       C  
-ATOM   1520  CG  GLN A 664       2.997 -28.968 -38.892  1.00 61.35           C  
-ANISOU 1520  CG  GLN A 664     6959   9149   7203    468   -684  -1024       C  
-ATOM   1521  CD  GLN A 664       4.423 -29.224 -39.348  1.00 64.15           C  
-ANISOU 1521  CD  GLN A 664     7218   9599   7555    513   -785  -1147       C  
-ATOM   1522  OE1 GLN A 664       5.384 -28.837 -38.681  1.00 55.90           O  
-ANISOU 1522  OE1 GLN A 664     6211   8528   6501    557   -846  -1190       O  
-ATOM   1523  NE2 GLN A 664       4.564 -29.884 -40.491  1.00 63.83           N  
-ANISOU 1523  NE2 GLN A 664     7053   9675   7524    501   -803  -1212       N  
-ATOM   1524  N   ILE A 665       1.231 -26.377 -36.071  1.00 48.60           N  
-ANISOU 1524  N   ILE A 665     5640   7243   5584    403   -498   -747       N  
-ATOM   1525  CA  ILE A 665       0.801 -26.371 -34.675  1.00 46.39           C  
-ANISOU 1525  CA  ILE A 665     5544   6798   5284    423   -478   -707       C  
-ATOM   1526  C   ILE A 665      -0.700 -26.102 -34.542  1.00 43.87           C  
-ANISOU 1526  C   ILE A 665     5262   6423   4983    359   -362   -611       C  
-ATOM   1527  O   ILE A 665      -1.389 -26.749 -33.753  1.00 48.17           O  
-ANISOU 1527  O   ILE A 665     5951   6841   5510    364   -335   -595       O  
-ATOM   1528  CB  ILE A 665       1.582 -25.321 -33.855  1.00 41.11           C  
-ANISOU 1528  CB  ILE A 665     4909   6103   4607    444   -504   -700       C  
-ATOM   1529  CG1 ILE A 665       3.069 -25.681 -33.799  1.00 41.77           C  
-ANISOU 1529  CG1 ILE A 665     4978   6220   4673    516   -625   -808       C  
-ATOM   1530  CG2 ILE A 665       1.016 -25.210 -32.450  1.00 35.44           C  
-ANISOU 1530  CG2 ILE A 665     4376   5221   3867    452   -469   -650       C  
-ATOM   1531  CD1 ILE A 665       3.943 -24.571 -33.246  1.00 42.53           C  
-ANISOU 1531  CD1 ILE A 665     5068   6324   4769    532   -652   -811       C  
-ATOM   1532  N   ILE A 666      -1.196 -25.141 -35.316  1.00 38.32           N  
-ANISOU 1532  N   ILE A 666     4430   5814   4314    296   -296   -549       N  
-ATOM   1533  CA  ILE A 666      -2.618 -24.812 -35.325  1.00 40.15           C  
-ANISOU 1533  CA  ILE A 666     4672   6008   4574    235   -189   -464       C  
-ATOM   1534  C   ILE A 666      -3.460 -26.013 -35.750  1.00 42.31           C  
-ANISOU 1534  C   ILE A 666     4963   6264   4850    225   -162   -480       C  
-ATOM   1535  O   ILE A 666      -4.500 -26.299 -35.158  1.00 44.08           O  
-ANISOU 1535  O   ILE A 666     5288   6384   5077    202    -96   -443       O  
-ATOM   1536  CB  ILE A 666      -2.915 -23.638 -36.276  1.00 45.85           C  
-ANISOU 1536  CB  ILE A 666     5236   6850   5336    174   -141   -404       C  
-ATOM   1537  CG1 ILE A 666      -2.111 -22.404 -35.873  1.00 41.99           C  
-ANISOU 1537  CG1 ILE A 666     4728   6378   4849    179   -163   -386       C  
-ATOM   1538  CG2 ILE A 666      -4.403 -23.324 -36.291  1.00 51.25           C  
-ANISOU 1538  CG2 ILE A 666     5926   7491   6056    116    -38   -326       C  
-ATOM   1539  CD1 ILE A 666      -2.330 -21.214 -36.781  1.00 40.93           C  
-ANISOU 1539  CD1 ILE A 666     4447   6355   4751    118   -124   -324       C  
-ATOM   1540  N   GLU A 667      -3.002 -26.713 -36.782  1.00 33.57           N  
-ANISOU 1540  N   GLU A 667     3754   5259   3742    239   -213   -540       N  
-ATOM   1541  CA  GLU A 667      -3.709 -27.882 -37.293  1.00 49.60           C  
-ANISOU 1541  CA  GLU A 667     5785   7284   5776    232   -195   -563       C  
-ATOM   1542  C   GLU A 667      -3.642 -29.064 -36.329  1.00 53.13           C  
-ANISOU 1542  C   GLU A 667     6405   7592   6190    282   -232   -610       C  
-ATOM   1543  O   GLU A 667      -4.643 -29.738 -36.090  1.00 52.29           O  
-ANISOU 1543  O   GLU A 667     6377   7405   6086    261   -177   -591       O  
-ATOM   1544  CB  GLU A 667      -3.141 -28.291 -38.656  1.00 60.02           C  
-ANISOU 1544  CB  GLU A 667     6945   8757   7104    234   -244   -622       C  
-ATOM   1545  CG  GLU A 667      -3.608 -29.654 -39.152  1.00 75.96           C  
-ANISOU 1545  CG  GLU A 667     8967  10771   9123    243   -248   -669       C  
-ATOM   1546  CD  GLU A 667      -5.068 -29.665 -39.562  1.00 89.23           C  
-ANISOU 1546  CD  GLU A 667    10622  12446  10834    182   -148   -606       C  
-ATOM   1547  OE1 GLU A 667      -5.538 -28.656 -40.128  1.00 88.92           O  
-ANISOU 1547  OE1 GLU A 667    10482  12483  10823    130    -93   -543       O  
-ATOM   1548  OE2 GLU A 667      -5.743 -30.690 -39.328  1.00 97.57           O  
-ANISOU 1548  OE2 GLU A 667    11760  13422  11889    186   -126   -622       O  
-ATOM   1549  N   MET A 668      -2.459 -29.308 -35.774  1.00 53.91           N  
-ANISOU 1549  N   MET A 668     6565   7660   6258    347   -328   -671       N  
-ATOM   1550  CA  MET A 668      -2.224 -30.503 -34.968  1.00 36.10           C  
-ANISOU 1550  CA  MET A 668     4468   5280   3968    402   -388   -725       C  
-ATOM   1551  C   MET A 668      -2.753 -30.396 -33.536  1.00 39.21           C  
-ANISOU 1551  C   MET A 668     5058   5507   4333    399   -348   -675       C  
-ATOM   1552  O   MET A 668      -3.203 -31.387 -32.960  1.00 54.09           O  
-ANISOU 1552  O   MET A 668     7082   7275   6193    409   -347   -686       O  
-ATOM   1553  CB  MET A 668      -0.736 -30.870 -34.982  1.00 26.49           C  
-ANISOU 1553  CB  MET A 668     3236   4098   2733    477   -518   -821       C  
-ATOM   1554  CG  MET A 668      -0.192 -31.115 -36.387  1.00 30.16           C  
-ANISOU 1554  CG  MET A 668     3512   4726   3221    478   -558   -885       C  
-ATOM   1555  SD  MET A 668       1.391 -31.982 -36.448  1.00 52.40           S  
-ANISOU 1555  SD  MET A 668     6318   7567   6023    571   -713  -1024       S  
-ATOM   1556  CE  MET A 668       2.517 -30.744 -35.809  1.00 84.27           C  
-ANISOU 1556  CE  MET A 668    10352  11619  10050    597   -758  -1029       C  
-ATOM   1557  N   VAL A 669      -2.702 -29.199 -32.963  1.00 37.38           N  
-ANISOU 1557  N   VAL A 669     4838   5261   4102    381   -314   -622       N  
-ATOM   1558  CA  VAL A 669      -3.236 -28.983 -31.622  1.00 41.66           C  
-ANISOU 1558  CA  VAL A 669     5556   5655   4618    370   -267   -574       C  
-ATOM   1559  C   VAL A 669      -4.762 -28.898 -31.652  1.00 51.08           C  
-ANISOU 1559  C   VAL A 669     6763   6812   5835    295   -140   -507       C  
-ATOM   1560  O   VAL A 669      -5.439 -29.327 -30.716  1.00 49.55           O  
-ANISOU 1560  O   VAL A 669     6728   6486   5615    279    -95   -487       O  
-ATOM   1561  CB  VAL A 669      -2.657 -27.713 -30.974  1.00 38.71           C  
-ANISOU 1561  CB  VAL A 669     5188   5280   4242    377   -275   -546       C  
-ATOM   1562  CG1 VAL A 669      -3.434 -27.353 -29.718  1.00 33.85           C  
-ANISOU 1562  CG1 VAL A 669     4730   4526   3605    347   -201   -488       C  
-ATOM   1563  CG2 VAL A 669      -1.181 -27.904 -30.660  1.00 39.36           C  
-ANISOU 1563  CG2 VAL A 669     5296   5364   4294    457   -402   -621       C  
-ATOM   1564  N   GLY A 670      -5.295 -28.346 -32.737  1.00 48.76           N  
-ANISOU 1564  N   GLY A 670     6302   6635   5591    247    -84   -475       N  
-ATOM   1565  CA  GLY A 670      -6.730 -28.197 -32.896  1.00 42.52           C  
-ANISOU 1565  CA  GLY A 670     5497   5825   4834    178     32   -419       C  
-ATOM   1566  C   GLY A 670      -7.461 -29.517 -33.050  1.00 44.26           C  
-ANISOU 1566  C   GLY A 670     5777   5992   5046    168     56   -445       C  
-ATOM   1567  O   GLY A 670      -8.626 -29.634 -32.668  1.00 46.92           O  
-ANISOU 1567  O   GLY A 670     6179   6254   5394    118    149   -411       O  
-ATOM   1568  N   ARG A 671      -6.778 -30.512 -33.610  1.00 45.51           N  
-ANISOU 1568  N   ARG A 671     5910   6192   5191    214    -27   -511       N  
-ATOM   1569  CA  ARG A 671      -7.372 -31.830 -33.828  1.00 50.04           C  
-ANISOU 1569  CA  ARG A 671     6533   6720   5759    209    -16   -544       C  
-ATOM   1570  C   ARG A 671      -7.066 -32.787 -32.678  1.00 62.29           C  
-ANISOU 1570  C   ARG A 671     8294   8119   7255    249    -65   -576       C  
-ATOM   1571  O   ARG A 671      -7.692 -33.840 -32.552  1.00 65.90           O  
-ANISOU 1571  O   ARG A 671     8838   8500   7701    236    -42   -591       O  
-ATOM   1572  CB  ARG A 671      -6.893 -32.424 -35.156  1.00 48.71           C  
-ANISOU 1572  CB  ARG A 671     6213   6684   5611    232    -76   -601       C  
-ATOM   1573  CG  ARG A 671      -5.397 -32.694 -35.224  1.00 53.89           C  
-ANISOU 1573  CG  ARG A 671     6854   7380   6242    306   -205   -672       C  
-ATOM   1574  CD  ARG A 671      -4.963 -33.027 -36.645  1.00 49.10           C  
-ANISOU 1574  CD  ARG A 671     6066   6930   5662    315   -249   -726       C  
-ATOM   1575  NE  ARG A 671      -3.550 -33.387 -36.724  1.00 49.04           N  
-ANISOU 1575  NE  ARG A 671     6040   6959   5635    386   -373   -810       N  
-ATOM   1576  CZ  ARG A 671      -2.905 -33.646 -37.857  1.00 51.47           C  
-ANISOU 1576  CZ  ARG A 671     6193   7404   5959    401   -428   -873       C  
-ATOM   1577  NH1 ARG A 671      -3.542 -33.581 -39.017  1.00 48.15           N  
-ANISOU 1577  NH1 ARG A 671     5627   7097   5569    351   -371   -857       N  
-ATOM   1578  NH2 ARG A 671      -1.620 -33.968 -37.831  1.00 61.61           N  
-ANISOU 1578  NH2 ARG A 671     7468   8714   7229    466   -540   -958       N  
-ATOM   1579  N   GLY A 672      -6.099 -32.417 -31.844  1.00 69.77           N  
-ANISOU 1579  N   GLY A 672     9326   9019   8166    297   -135   -586       N  
-ATOM   1580  CA  GLY A 672      -5.766 -33.198 -30.666  1.00 56.72           C  
-ANISOU 1580  CA  GLY A 672     7883   7213   6454    336   -189   -611       C  
-ATOM   1581  C   GLY A 672      -4.617 -34.169 -30.855  1.00 55.05           C  
-ANISOU 1581  C   GLY A 672     7689   7005   6221    416   -328   -695       C  
-ATOM   1582  O   GLY A 672      -4.439 -35.090 -30.059  1.00 64.03           O  
-ANISOU 1582  O   GLY A 672     9001   8015   7313    450   -381   -722       O  
-ATOM   1583  N   SER A 673      -3.831 -33.966 -31.905  1.00 55.91           N  
-ANISOU 1583  N   SER A 673     7621   7260   6362    447   -388   -740       N  
-ATOM   1584  CA  SER A 673      -2.702 -34.846 -32.185  1.00 51.89           C  
-ANISOU 1584  CA  SER A 673     7103   6769   5842    524   -521   -833       C  
-ATOM   1585  C   SER A 673      -1.417 -34.319 -31.556  1.00 57.49           C  
-ANISOU 1585  C   SER A 673     7846   7468   6528    588   -621   -868       C  
-ATOM   1586  O   SER A 673      -0.408 -35.021 -31.502  1.00 63.38           O  
-ANISOU 1586  O   SER A 673     8619   8201   7261    662   -743   -951       O  
-ATOM   1587  CB  SER A 673      -2.513 -35.019 -33.693  1.00 32.98           C  
-ANISOU 1587  CB  SER A 673     4495   4542   3494    520   -535   -878       C  
-ATOM   1588  OG  SER A 673      -2.056 -33.816 -34.288  1.00 39.31           O  
-ANISOU 1588  OG  SER A 673     5136   5478   4320    505   -524   -864       O  
-ATOM   1589  N   LEU A 674      -1.458 -33.083 -31.073  1.00 49.58           N  
-ANISOU 1589  N   LEU A 674     6842   6472   5525    562   -570   -809       N  
-ATOM   1590  CA  LEU A 674      -0.269 -32.458 -30.514  1.00 46.08           C  
-ANISOU 1590  CA  LEU A 674     6416   6029   5064    618   -655   -840       C  
-ATOM   1591  C   LEU A 674      -0.520 -31.853 -29.136  1.00 48.11           C  
-ANISOU 1591  C   LEU A 674     6840   6156   5282    608   -619   -781       C  
-ATOM   1592  O   LEU A 674      -1.568 -31.257 -28.882  1.00 52.73           O  
-ANISOU 1592  O   LEU A 674     7446   6714   5874    539   -502   -701       O  
-ATOM   1593  CB  LEU A 674       0.276 -31.397 -31.472  1.00 34.92           C  
-ANISOU 1593  CB  LEU A 674     4791   4786   3693    604   -650   -846       C  
-ATOM   1594  CG  LEU A 674       1.606 -30.749 -31.095  1.00 37.40           C  
-ANISOU 1594  CG  LEU A 674     5087   5125   3997    661   -741   -893       C  
-ATOM   1595  CD1 LEU A 674       2.662 -31.808 -30.870  1.00 39.81           C  
-ANISOU 1595  CD1 LEU A 674     5456   5388   4280    750   -882   -999       C  
-ATOM   1596  CD2 LEU A 674       2.058 -29.774 -32.169  1.00 32.10           C  
-ANISOU 1596  CD2 LEU A 674     4201   4629   3366    634   -726   -898       C  
-ATOM   1597  N   SER A 675       0.456 -32.022 -28.252  1.00 44.55           N  
-ANISOU 1597  N   SER A 675     6508   5627   4792    678   -724   -826       N  
-ATOM   1598  CA  SER A 675       0.401 -31.468 -26.906  1.00 39.64           C  
-ANISOU 1598  CA  SER A 675     6049   4885   4127    677   -708   -781       C  
-ATOM   1599  C   SER A 675       1.823 -31.201 -26.426  1.00 46.38           C  
-ANISOU 1599  C   SER A 675     6922   5736   4962    760   -835   -846       C  
-ATOM   1600  O   SER A 675       2.763 -31.847 -26.885  1.00 51.50           O  
-ANISOU 1600  O   SER A 675     7522   6427   5620    825   -949   -934       O  
-ATOM   1601  CB  SER A 675      -0.302 -32.437 -25.956  1.00 41.24           C  
-ANISOU 1601  CB  SER A 675     6476   4919   4275    667   -692   -760       C  
-ATOM   1602  OG  SER A 675       0.438 -33.636 -25.810  1.00 48.22           O  
-ANISOU 1602  OG  SER A 675     7450   5740   5130    741   -822   -836       O  
-ATOM   1603  N   PRO A 676       1.987 -30.244 -25.502  1.00 70.98           N  
-ANISOU 1603  N   PRO A 676    10106   8805   8057    757   -817   -808       N  
-ATOM   1604  CA  PRO A 676       3.324 -29.892 -25.008  1.00 70.97           C  
-ANISOU 1604  CA  PRO A 676    10120   8803   8042    834   -933   -870       C  
-ATOM   1605  C   PRO A 676       4.113 -31.110 -24.521  1.00 62.82           C  
-ANISOU 1605  C   PRO A 676     9224   7675   6970    922  -1077   -952       C  
-ATOM   1606  O   PRO A 676       3.538 -32.023 -23.928  1.00 49.30           O  
-ANISOU 1606  O   PRO A 676     7684   5834   5213    918  -1077   -934       O  
-ATOM   1607  CB  PRO A 676       3.025 -28.940 -23.848  1.00 51.79           C  
-ANISOU 1607  CB  PRO A 676     7804   6291   5583    808   -875   -803       C  
-ATOM   1608  CG  PRO A 676       1.711 -28.326 -24.204  1.00 42.80           C  
-ANISOU 1608  CG  PRO A 676     6602   5187   4475    710   -718   -712       C  
-ATOM   1609  CD  PRO A 676       0.933 -29.407 -24.901  1.00 52.63           C  
-ANISOU 1609  CD  PRO A 676     7837   6432   5727    681   -686   -713       C  
-ATOM   1610  N   ASP A 677       5.418 -31.112 -24.781  1.00 52.97           N  
-ANISOU 1610  N   ASP A 677     7898   6490   5739    998  -1200  -1046       N  
-ATOM   1611  CA  ASP A 677       6.295 -32.216 -24.396  1.00 59.39           C  
-ANISOU 1611  CA  ASP A 677     8819   7222   6525   1092  -1354  -1138       C  
-ATOM   1612  C   ASP A 677       6.745 -32.082 -22.944  1.00 65.47           C  
-ANISOU 1612  C   ASP A 677     9792   7849   7235   1141  -1422  -1136       C  
-ATOM   1613  O   ASP A 677       7.583 -31.241 -22.618  1.00 71.71           O  
-ANISOU 1613  O   ASP A 677    10543   8672   8031   1176  -1466  -1165       O  
-ATOM   1614  CB  ASP A 677       7.515 -32.266 -25.321  1.00 91.24           C  
-ANISOU 1614  CB  ASP A 677    12670  11388  10607   1152  -1458  -1252       C  
-ATOM   1615  CG  ASP A 677       8.425 -33.445 -25.029  1.00103.38           C  
-ANISOU 1615  CG  ASP A 677    14301  12850  12129   1253  -1625  -1360       C  
-ATOM   1616  OD1 ASP A 677       8.036 -34.323 -24.230  1.00 99.57           O  
-ANISOU 1616  OD1 ASP A 677    14022  12212  11597   1272  -1658  -1340       O  
-ATOM   1617  OD2 ASP A 677       9.532 -33.495 -25.606  1.00113.04           O  
-ANISOU 1617  OD2 ASP A 677    15393  14167  13391   1313  -1723  -1468       O  
-ATOM   1618  N   LEU A 678       6.192 -32.924 -22.078  1.00 72.77           N  
-ANISOU 1618  N   LEU A 678    10936   8614   8100   1141  -1432  -1104       N  
-ATOM   1619  CA  LEU A 678       6.446 -32.829 -20.644  1.00 70.55           C  
-ANISOU 1619  CA  LEU A 678    10870   8185   7750   1174  -1483  -1088       C  
-ATOM   1620  C   LEU A 678       7.724 -33.548 -20.210  1.00 68.44           C  
-ANISOU 1620  C   LEU A 678    10688   7854   7462   1291  -1675  -1193       C  
-ATOM   1621  O   LEU A 678       7.990 -33.690 -19.017  1.00 74.04           O  
-ANISOU 1621  O   LEU A 678    11598   8426   8107   1329  -1743  -1189       O  
-ATOM   1622  CB  LEU A 678       5.241 -33.351 -19.857  1.00 63.71           C  
-ANISOU 1622  CB  LEU A 678    10213   7174   6821   1111  -1399  -1002       C  
-ATOM   1623  CG  LEU A 678       3.901 -32.704 -20.211  1.00 56.21           C  
-ANISOU 1623  CG  LEU A 678     9190   6274   5893    996  -1210   -904       C  
-ATOM   1624  CD1 LEU A 678       2.775 -33.277 -19.368  1.00 60.74           C  
-ANISOU 1624  CD1 LEU A 678     9978   6699   6402    933  -1132   -833       C  
-ATOM   1625  CD2 LEU A 678       3.973 -31.196 -20.047  1.00 48.10           C  
-ANISOU 1625  CD2 LEU A 678     8065   5320   4889    966  -1138   -864       C  
-ATOM   1626  N   SER A 679       8.513 -33.999 -21.180  1.00 66.07           N  
-ANISOU 1626  N   SER A 679    10235   7652   7216   1346  -1766  -1292       N  
-ATOM   1627  CA  SER A 679       9.804 -34.607 -20.880  1.00 62.92           C  
-ANISOU 1627  CA  SER A 679     9884   7210   6814   1462  -1954  -1409       C  
-ATOM   1628  C   SER A 679      10.863 -33.518 -20.768  1.00 68.26           C  
-ANISOU 1628  C   SER A 679    10450   7969   7516   1505  -2000  -1461       C  
-ATOM   1629  O   SER A 679      12.037 -33.798 -20.527  1.00 64.74           O  
-ANISOU 1629  O   SER A 679    10017   7506   7076   1603  -2154  -1568       O  
-ATOM   1630  CB  SER A 679      10.200 -35.613 -21.962  1.00 63.20           C  
-ANISOU 1630  CB  SER A 679     9799   7313   6900   1504  -2034  -1504       C  
-ATOM   1631  OG  SER A 679      10.497 -34.962 -23.184  1.00 62.24           O  
-ANISOU 1631  OG  SER A 679     9413   7385   6850   1479  -1986  -1542       O  
-ATOM   1632  N   LYS A 680      10.434 -32.272 -20.945  1.00 82.26           N  
-ANISOU 1632  N   LYS A 680    12116   9830   9308   1431  -1866  -1389       N  
-ATOM   1633  CA  LYS A 680      11.341 -31.133 -20.895  1.00 85.57           C  
-ANISOU 1633  CA  LYS A 680    12421  10337   9756   1457  -1889  -1429       C  
-ATOM   1634  C   LYS A 680      11.434 -30.545 -19.490  1.00 98.10           C  
-ANISOU 1634  C   LYS A 680    14184  11804  11285   1473  -1900  -1387       C  
-ATOM   1635  O   LYS A 680      12.432 -29.914 -19.139  1.00100.72           O  
-ANISOU 1635  O   LYS A 680    14482  12160  11626   1528  -1974  -1447       O  
-ATOM   1636  CB  LYS A 680      10.904 -30.057 -21.890  1.00 74.37           C  
-ANISOU 1636  CB  LYS A 680    10783   9082   8393   1369  -1747  -1378       C  
-ATOM   1637  CG  LYS A 680      10.872 -30.524 -23.338  1.00 77.91           C  
-ANISOU 1637  CG  LYS A 680    11040   9666   8898   1349  -1734  -1422       C  
-ATOM   1638  CD  LYS A 680      12.252 -30.934 -23.825  1.00 79.51           C  
-ANISOU 1638  CD  LYS A 680    11136   9938   9136   1438  -1882  -1571       C  
-ATOM   1639  CE  LYS A 680      12.239 -31.240 -25.313  1.00 76.18           C  
-ANISOU 1639  CE  LYS A 680    10504   9670   8770   1408  -1855  -1616       C  
-ATOM   1640  NZ  LYS A 680      13.588 -31.618 -25.813  1.00 85.32           N  
-ANISOU 1640  NZ  LYS A 680    11546  10904   9967   1489  -1994  -1771       N  
-ATOM   1641  N   VAL A 681      10.392 -30.751 -18.689  1.00 99.72           N  
-ANISOU 1641  N   VAL A 681    14577  11883  11429   1421  -1825  -1288       N  
-ATOM   1642  CA  VAL A 681      10.395 -30.274 -17.313  1.00 91.88           C  
-ANISOU 1642  CA  VAL A 681    13769  10768  10371   1430  -1831  -1245       C  
-ATOM   1643  C   VAL A 681      11.596 -30.870 -16.588  1.00 97.37           C  
-ANISOU 1643  C   VAL A 681    14588  11374  11035   1548  -2023  -1345       C  
-ATOM   1644  O   VAL A 681      11.961 -32.024 -16.818  1.00101.80           O  
-ANISOU 1644  O   VAL A 681    15193  11893  11595   1608  -2137  -1413       O  
-ATOM   1645  CB  VAL A 681       9.093 -30.650 -16.568  1.00 72.27           C  
-ANISOU 1645  CB  VAL A 681    11487   8152   7819   1356  -1731  -1137       C  
-ATOM   1646  CG1 VAL A 681       7.925 -30.734 -17.541  1.00 69.21           C  
-ANISOU 1646  CG1 VAL A 681    10987   7839   7470   1260  -1585  -1072       C  
-ATOM   1647  CG2 VAL A 681       9.259 -31.965 -15.829  1.00 70.97           C  
-ANISOU 1647  CG2 VAL A 681    11554   7825   7586   1414  -1854  -1167       C  
-ATOM   1648  N   ARG A 682      12.222 -30.078 -15.725  1.00 83.52           N  
-ANISOU 1648  N   ARG A 682    12885   9590   9260   1585  -2064  -1358       N  
-ATOM   1649  CA  ARG A 682      13.408 -30.536 -15.014  1.00 92.78           C  
-ANISOU 1649  CA  ARG A 682    14166  10681  10406   1702  -2252  -1458       C  
-ATOM   1650  C   ARG A 682      13.041 -31.450 -13.852  1.00 92.28           C  
-ANISOU 1650  C   ARG A 682    14397  10419  10246   1721  -2313  -1420       C  
-ATOM   1651  O   ARG A 682      11.928 -31.391 -13.329  1.00 88.83           O  
-ANISOU 1651  O   ARG A 682    14091   9907   9754   1637  -2194  -1310       O  
-ATOM   1652  CB  ARG A 682      14.233 -29.348 -14.518  1.00126.33           C  
-ANISOU 1652  CB  ARG A 682    18359  14972  14667   1735  -2276  -1490       C  
-ATOM   1653  CG  ARG A 682      14.819 -28.499 -15.631  1.00138.08           C  
-ANISOU 1653  CG  ARG A 682    19565  16651  16248   1727  -2243  -1546       C  
-ATOM   1654  CD  ARG A 682      15.672 -27.377 -15.069  1.00148.98           C  
-ANISOU 1654  CD  ARG A 682    20906  18061  17640   1763  -2275  -1583       C  
-ATOM   1655  NE  ARG A 682      16.278 -26.568 -16.122  1.00158.66           N  
-ANISOU 1655  NE  ARG A 682    21867  19466  18950   1751  -2245  -1640       N  
-ATOM   1656  CZ  ARG A 682      17.039 -25.503 -15.897  1.00167.12           C  
-ANISOU 1656  CZ  ARG A 682    22853  20596  20049   1771  -2257  -1679       C  
-ATOM   1657  NH1 ARG A 682      17.290 -25.116 -14.654  1.00169.66           N  
-ANISOU 1657  NH1 ARG A 682    23328  20814  20322   1808  -2299  -1669       N  
-ATOM   1658  NH2 ARG A 682      17.551 -24.824 -16.915  1.00169.44           N  
-ANISOU 1658  NH2 ARG A 682    22910  21054  20417   1751  -2225  -1729       N  
-ATOM   1659  N   SER A 683      13.985 -32.302 -13.463  1.00109.11           N  
-ANISOU 1659  N   SER A 683    16633  12467  12358   1830  -2500  -1516       N  
-ATOM   1660  CA  SER A 683      13.793 -33.210 -12.340  1.00109.17           C  
-ANISOU 1660  CA  SER A 683    16931  12279  12270   1859  -2585  -1490       C  
-ATOM   1661  C   SER A 683      13.428 -32.428 -11.085  1.00111.08           C  
-ANISOU 1661  C   SER A 683    17339  12433  12435   1820  -2523  -1407       C  
-ATOM   1662  O   SER A 683      12.593 -32.863 -10.292  1.00107.55           O  
-ANISOU 1662  O   SER A 683    17112  11851  11902   1769  -2478  -1323       O  
-ATOM   1663  CB  SER A 683      15.059 -34.034 -12.096  1.00 98.27           C  
-ANISOU 1663  CB  SER A 683    15616  10832  10891   1997  -2815  -1619       C  
-ATOM   1664  OG  SER A 683      15.392 -34.809 -13.234  1.00103.39           O  
-ANISOU 1664  OG  SER A 683    16114  11558  11610   2033  -2876  -1703       O  
-ATOM   1665  N   ASN A 684      14.057 -31.268 -10.916  1.00 99.62           N  
-ANISOU 1665  N   ASN A 684    15779  11059  11013   1840  -2517  -1434       N  
-ATOM   1666  CA  ASN A 684      13.789 -30.414  -9.766  1.00 93.17           C  
-ANISOU 1666  CA  ASN A 684    15094  10175  10133   1806  -2457  -1365       C  
-ATOM   1667  C   ASN A 684      12.467 -29.668  -9.887  1.00 85.78           C  
-ANISOU 1667  C   ASN A 684    14117   9281   9195   1671  -2237  -1242       C  
-ATOM   1668  O   ASN A 684      12.359 -28.515  -9.472  1.00 83.68           O  
-ANISOU 1668  O   ASN A 684    13814   9049   8930   1634  -2154  -1203       O  
-ATOM   1669  CB  ASN A 684      14.932 -29.417  -9.553  1.00100.04           C  
-ANISOU 1669  CB  ASN A 684    15856  11115  11041   1875  -2528  -1442       C  
-ATOM   1670  CG  ASN A 684      15.135 -28.491 -10.739  1.00104.03           C  
-ANISOU 1670  CG  ASN A 684    16058  11815  11652   1845  -2442  -1468       C  
-ATOM   1671  OD1 ASN A 684      14.228 -28.275 -11.541  1.00108.57           O  
-ANISOU 1671  OD1 ASN A 684    16515  12472  12263   1752  -2294  -1399       O  
-ATOM   1672  ND2 ASN A 684      16.335 -27.934 -10.850  1.00102.96           N  
-ANISOU 1672  ND2 ASN A 684    15798  11756  11568   1921  -2537  -1570       N  
-ATOM   1673  N   CYS A 685      11.469 -30.327 -10.467  1.00100.11           N  
-ANISOU 1673  N   CYS A 685    15933  11094  11012   1600  -2147  -1185       N  
-ATOM   1674  CA  CYS A 685      10.135 -29.750 -10.588  1.00108.60           C  
-ANISOU 1674  CA  CYS A 685    16979  12198  12086   1472  -1942  -1074       C  
-ATOM   1675  C   CYS A 685       9.161 -30.494  -9.682  1.00112.21           C  
-ANISOU 1675  C   CYS A 685    17700  12493  12443   1414  -1897   -996       C  
-ATOM   1676  O   CYS A 685       8.945 -31.691  -9.865  1.00111.51           O  
-ANISOU 1676  O   CYS A 685    17706  12334  12329   1424  -1948  -1004       O  
-ATOM   1677  CB  CYS A 685       9.644 -29.810 -12.037  1.00 98.67           C  
-ANISOU 1677  CB  CYS A 685    15496  11079  10916   1422  -1851  -1067       C  
-ATOM   1678  SG  CYS A 685       7.960 -29.175 -12.265  1.00 77.37           S  
-ANISOU 1678  SG  CYS A 685    12755   8417   8227   1270  -1608   -938       S  
-ATOM   1679  N   PRO A 686       8.580 -29.792  -8.695  1.00108.68           N  
-ANISOU 1679  N   PRO A 686    17372  11984  11937   1351  -1802   -924       N  
-ATOM   1680  CA  PRO A 686       7.604 -30.453  -7.825  1.00106.92           C  
-ANISOU 1680  CA  PRO A 686    17400  11611  11614   1281  -1743   -851       C  
-ATOM   1681  C   PRO A 686       6.614 -31.269  -8.626  1.00111.87           C  
-ANISOU 1681  C   PRO A 686    17998  12247  12261   1212  -1656   -813       C  
-ATOM   1682  O   PRO A 686       5.779 -30.714  -9.324  1.00115.45           O  
-ANISOU 1682  O   PRO A 686    18294  12799  12773   1129  -1502   -767       O  
-ATOM   1683  CB  PRO A 686       6.869 -29.284  -7.197  1.00 94.43           C  
-ANISOU 1683  CB  PRO A 686    15826  10039  10015   1191  -1587   -777       C  
-ATOM   1684  CG  PRO A 686       7.896 -28.218  -7.104  1.00 94.51           C  
-ANISOU 1684  CG  PRO A 686    15713  10129  10069   1258  -1648   -828       C  
-ATOM   1685  CD  PRO A 686       8.827 -28.397  -8.286  1.00 92.38           C  
-ANISOU 1685  CD  PRO A 686    15229   9978   9892   1341  -1748   -913       C  
-ATOM   1686  N   LYS A 687       6.682 -32.582  -8.493  1.00117.11           N  
-ANISOU 1686  N   LYS A 687    18821  12802  12874   1245  -1754   -833       N  
-ATOM   1687  CA  LYS A 687       5.820 -33.444  -9.275  1.00122.04           C  
-ANISOU 1687  CA  LYS A 687    19419  13432  13520   1187  -1685   -807       C  
-ATOM   1688  C   LYS A 687       4.359 -33.379  -8.807  1.00123.08           C  
-ANISOU 1688  C   LYS A 687    19665  13501  13599   1053  -1501   -708       C  
-ATOM   1689  O   LYS A 687       3.511 -34.149  -9.267  1.00125.39           O  
-ANISOU 1689  O   LYS A 687    19976  13774  13893    993  -1433   -680       O  
-ATOM   1690  CB  LYS A 687       6.380 -34.867  -9.320  1.00128.32           C  
-ANISOU 1690  CB  LYS A 687    20339  14131  14286   1267  -1853   -864       C  
-ATOM   1691  CG  LYS A 687       7.744 -34.943 -10.022  1.00126.69           C  
-ANISOU 1691  CG  LYS A 687    19970  14012  14154   1394  -2019   -976       C  
-ATOM   1692  CD  LYS A 687       8.294 -36.364 -10.033  1.00124.18           C  
-ANISOU 1692  CD  LYS A 687    19779  13592  13812   1477  -2193  -1039       C  
-ATOM   1693  CE  LYS A 687       9.684 -36.463 -10.640  1.00123.10           C  
-ANISOU 1693  CE  LYS A 687    19491  13534  13748   1606  -2366  -1162       C  
-ATOM   1694  NZ  LYS A 687      10.108 -37.880 -10.491  1.00125.69           N  
-ANISOU 1694  NZ  LYS A 687    19977  13736  14044   1681  -2535  -1217       N  
-ATOM   1695  N   ARG A 688       4.069 -32.435  -7.914  1.00107.16           N  
-ANISOU 1695  N   ARG A 688    17716  11461  11541   1003  -1419   -662       N  
-ATOM   1696  CA  ARG A 688       2.691 -32.073  -7.624  1.00 96.62           C  
-ANISOU 1696  CA  ARG A 688    16423  10107  10182    870  -1223   -579       C  
-ATOM   1697  C   ARG A 688       2.240 -31.013  -8.618  1.00 86.31           C  
-ANISOU 1697  C   ARG A 688    14836   8969   8988    823  -1089   -563       C  
-ATOM   1698  O   ARG A 688       1.046 -30.853  -8.867  1.00 68.44           O  
-ANISOU 1698  O   ARG A 688    12533   6728   6743    719   -928   -509       O  
-ATOM   1699  CB  ARG A 688       2.555 -31.538  -6.199  1.00103.53           C  
-ANISOU 1699  CB  ARG A 688    17497  10878  10960    834  -1193   -541       C  
-ATOM   1700  CG  ARG A 688       2.934 -32.540  -5.138  1.00108.38           C  
-ANISOU 1700  CG  ARG A 688    18410  11317  11452    871  -1320   -548       C  
-ATOM   1701  CD  ARG A 688       1.771 -32.832  -4.215  1.00115.93           C  
-ANISOU 1701  CD  ARG A 688    19592  12151  12307    749  -1194   -476       C  
-ATOM   1702  NE  ARG A 688       1.773 -31.916  -3.084  1.00117.50           N  
-ANISOU 1702  NE  ARG A 688    19892  12310  12442    719  -1151   -452       N  
-ATOM   1703  CZ  ARG A 688       0.682 -31.395  -2.536  1.00119.47           C  
-ANISOU 1703  CZ  ARG A 688    20196  12540  12657    597   -976   -394       C  
-ATOM   1704  NH1 ARG A 688      -0.516 -31.696  -3.016  1.00118.29           N  
-ANISOU 1704  NH1 ARG A 688    20010  12405  12531    492   -826   -356       N  
-ATOM   1705  NH2 ARG A 688       0.797 -30.568  -1.507  1.00123.66           N  
-ANISOU 1705  NH2 ARG A 688    20815  13037  13132    580   -953   -381       N  
-ATOM   1706  N   MET A 689       3.215 -30.287  -9.161  1.00102.42           N  
-ANISOU 1706  N   MET A 689    16687  11127  11102    900  -1161   -613       N  
-ATOM   1707  CA  MET A 689       3.003 -29.254 -10.169  1.00 97.85           C  
-ANISOU 1707  CA  MET A 689    15834  10713  10631    870  -1063   -605       C  
-ATOM   1708  C   MET A 689       2.626 -29.872 -11.507  1.00 93.86           C  
-ANISOU 1708  C   MET A 689    15173  10294  10196    855  -1035   -615       C  
-ATOM   1709  O   MET A 689       1.624 -29.502 -12.111  1.00 93.27           O  
-ANISOU 1709  O   MET A 689    14979  10287  10171    770   -890   -568       O  
-ATOM   1710  CB  MET A 689       4.297 -28.450 -10.340  1.00 90.15           C  
-ANISOU 1710  CB  MET A 689    14723   9827   9704    963  -1169   -665       C  
-ATOM   1711  CG  MET A 689       4.208 -27.278 -11.298  1.00 85.43           C  
-ANISOU 1711  CG  MET A 689    13853   9395   9211    934  -1079   -656       C  
-ATOM   1712  SD  MET A 689       3.186 -25.938 -10.668  1.00 99.67           S  
-ANISOU 1712  SD  MET A 689    15651  11202  11017    828   -898   -574       S  
-ATOM   1713  CE  MET A 689       4.046 -25.517  -9.160  1.00126.71           C  
-ANISOU 1713  CE  MET A 689    19262  14523  14360    886   -991   -596       C  
-ATOM   1714  N   LYS A 690       3.437 -30.823 -11.961  1.00 79.25           N  
-ANISOU 1714  N   LYS A 690    13322   8440   8351    940  -1180   -680       N  
-ATOM   1715  CA  LYS A 690       3.244 -31.429 -13.274  1.00 70.75           C  
-ANISOU 1715  CA  LYS A 690    12085   7453   7343    939  -1172   -703       C  
-ATOM   1716  C   LYS A 690       1.865 -32.065 -13.395  1.00 65.69           C  
-ANISOU 1716  C   LYS A 690    11514   6761   6684    840  -1043   -643       C  
-ATOM   1717  O   LYS A 690       1.223 -31.971 -14.440  1.00 73.45           O  
-ANISOU 1717  O   LYS A 690    12324   7847   7737    790   -950   -627       O  
-ATOM   1718  CB  LYS A 690       4.336 -32.457 -13.570  1.00 87.13           C  
-ANISOU 1718  CB  LYS A 690    14180   9507   9417   1048  -1358   -791       C  
-ATOM   1719  CG  LYS A 690       4.233 -33.072 -14.956  1.00103.56           C  
-ANISOU 1719  CG  LYS A 690    16085  11691  11572   1052  -1358   -825       C  
-ATOM   1720  CD  LYS A 690       5.394 -34.011 -15.250  1.00115.37           C  
-ANISOU 1720  CD  LYS A 690    17584  13174  13076   1166  -1548   -925       C  
-ATOM   1721  CE  LYS A 690       5.243 -34.657 -16.622  1.00124.93           C  
-ANISOU 1721  CE  LYS A 690    18623  14488  14359   1164  -1543   -961       C  
-ATOM   1722  NZ  LYS A 690       6.363 -35.582 -16.966  1.00128.44           N  
-ANISOU 1722  NZ  LYS A 690    19055  14926  14819   1274  -1726  -1069       N  
-ATOM   1723  N   ARG A 691       1.414 -32.711 -12.325  1.00 61.96           N  
-ANISOU 1723  N   ARG A 691    11297   6129   6115    808  -1039   -611       N  
-ATOM   1724  CA  ARG A 691       0.058 -33.239 -12.284  1.00 74.79           C  
-ANISOU 1724  CA  ARG A 691    13007   7696   7715    702   -903   -553       C  
-ATOM   1725  C   ARG A 691      -0.930 -32.110 -12.537  1.00 70.74           C  
-ANISOU 1725  C   ARG A 691    12353   7272   7255    606   -720   -497       C  
-ATOM   1726  O   ARG A 691      -1.874 -32.255 -13.312  1.00 63.48           O  
-ANISOU 1726  O   ARG A 691    11329   6407   6385    538   -609   -473       O  
-ATOM   1727  CB  ARG A 691      -0.239 -33.872 -10.927  1.00118.48           C  
-ANISOU 1727  CB  ARG A 691    18847  13044  13126    672   -914   -523       C  
-ATOM   1728  CG  ARG A 691      -1.585 -34.576 -10.867  1.00138.01           C  
-ANISOU 1728  CG  ARG A 691    21424  15446  15568    562   -783   -473       C  
-ATOM   1729  CD  ARG A 691      -2.040 -34.781  -9.434  1.00154.08           C  
-ANISOU 1729  CD  ARG A 691    23743  17318  17482    501   -747   -430       C  
-ATOM   1730  NE  ARG A 691      -0.912 -34.791  -8.508  1.00166.68           N  
-ANISOU 1730  NE  ARG A 691    25493  18830  19006    589   -903   -457       N  
-ATOM   1731  CZ  ARG A 691      -0.079 -35.815  -8.355  1.00173.65           C  
-ANISOU 1731  CZ  ARG A 691    26505  19629  19847    676  -1076   -499       C  
-ATOM   1732  NH1 ARG A 691      -0.240 -36.916  -9.076  1.00173.75           N  
-ANISOU 1732  NH1 ARG A 691    26508  19628  19881    687  -1112   -519       N  
-ATOM   1733  NH2 ARG A 691       0.920 -35.733  -7.488  1.00177.66           N  
-ANISOU 1733  NH2 ARG A 691    27147  20062  20292    756  -1216   -525       N  
-ATOM   1734  N   LEU A 692      -0.701 -30.981 -11.874  1.00 74.50           N  
-ANISOU 1734  N   LEU A 692    12826   7759   7723    602   -694   -481       N  
-ATOM   1735  CA  LEU A 692      -1.557 -29.812 -12.024  1.00 75.69           C  
-ANISOU 1735  CA  LEU A 692    12846   7986   7926    518   -533   -433       C  
-ATOM   1736  C   LEU A 692      -1.400 -29.203 -13.413  1.00 64.56           C  
-ANISOU 1736  C   LEU A 692    11147   6750   6632    535   -516   -448       C  
-ATOM   1737  O   LEU A 692      -2.381 -28.812 -14.045  1.00 59.17           O  
-ANISOU 1737  O   LEU A 692    10337   6136   6008    459   -384   -412       O  
-ATOM   1738  CB  LEU A 692      -1.233 -28.774 -10.948  1.00 75.11           C  
-ANISOU 1738  CB  LEU A 692    12843   7879   7815    520   -527   -419       C  
-ATOM   1739  CG  LEU A 692      -2.075 -27.498 -10.949  1.00 66.67           C  
-ANISOU 1739  CG  LEU A 692    11655   6877   6800    437   -368   -373       C  
-ATOM   1740  CD1 LEU A 692      -3.555 -27.821 -10.821  1.00 65.35           C  
-ANISOU 1740  CD1 LEU A 692    11554   6659   6618    320   -211   -327       C  
-ATOM   1741  CD2 LEU A 692      -1.632 -26.579  -9.830  1.00 63.14           C  
-ANISOU 1741  CD2 LEU A 692    11293   6388   6311    450   -381   -368       C  
-ATOM   1742  N   MET A 693      -0.158 -29.126 -13.880  1.00 48.22           N  
-ANISOU 1742  N   MET A 693     8977   4750   4594    633   -650   -504       N  
-ATOM   1743  CA  MET A 693       0.134 -28.626 -15.217  1.00 41.92           C  
-ANISOU 1743  CA  MET A 693     7914   4118   3896    652   -649   -525       C  
-ATOM   1744  C   MET A 693      -0.630 -29.430 -16.260  1.00 51.10           C  
-ANISOU 1744  C   MET A 693     8995   5324   5098    612   -596   -520       C  
-ATOM   1745  O   MET A 693      -1.358 -28.874 -17.080  1.00 50.03           O  
-ANISOU 1745  O   MET A 693     8692   5287   5030    552   -487   -488       O  
-ATOM   1746  CB  MET A 693       1.635 -28.713 -15.494  1.00 44.28           C  
-ANISOU 1746  CB  MET A 693     8150   4465   4208    765   -816   -602       C  
-ATOM   1747  CG  MET A 693       2.036 -28.244 -16.880  1.00 42.01           C  
-ANISOU 1747  CG  MET A 693     7595   4352   4017    782   -822   -631       C  
-ATOM   1748  SD  MET A 693       3.790 -28.490 -17.212  1.00 54.25           S  
-ANISOU 1748  SD  MET A 693     9074   5956   5581    910  -1017   -739       S  
-ATOM   1749  CE  MET A 693       4.508 -27.697 -15.777  1.00 37.93           C  
-ANISOU 1749  CE  MET A 693     7149   3804   3459    952  -1072   -742       C  
-ATOM   1750  N   ALA A 694      -0.457 -30.747 -16.217  1.00 54.19           N  
-ANISOU 1750  N   ALA A 694     9508   5636   5445    646   -678   -552       N  
-ATOM   1751  CA  ALA A 694      -1.138 -31.643 -17.142  1.00 59.93           C  
-ANISOU 1751  CA  ALA A 694    10176   6391   6203    613   -639   -554       C  
-ATOM   1752  C   ALA A 694      -2.651 -31.534 -16.990  1.00 65.96           C  
-ANISOU 1752  C   ALA A 694    10976   7120   6965    498   -466   -487       C  
-ATOM   1753  O   ALA A 694      -3.397 -31.729 -17.950  1.00 64.74           O  
-ANISOU 1753  O   ALA A 694    10694   7038   6867    452   -388   -476       O  
-ATOM   1754  CB  ALA A 694      -0.680 -33.072 -16.927  1.00 45.18           C  
-ANISOU 1754  CB  ALA A 694     8464   4420   4281    671   -763   -600       C  
-ATOM   1755  N   GLU A 695      -3.097 -31.229 -15.775  1.00 75.92           N  
-ANISOU 1755  N   GLU A 695    12413   8272   8162    451   -406   -447       N  
-ATOM   1756  CA  GLU A 695      -4.519 -31.061 -15.495  1.00 74.01           C  
-ANISOU 1756  CA  GLU A 695    12214   7992   7916    337   -238   -392       C  
-ATOM   1757  C   GLU A 695      -5.089 -29.828 -16.191  1.00 73.18           C  
-ANISOU 1757  C   GLU A 695    11888   8016   7902    288   -123   -362       C  
-ATOM   1758  O   GLU A 695      -6.246 -29.822 -16.613  1.00 73.44           O  
-ANISOU 1758  O   GLU A 695    11860   8072   7973    208      3   -334       O  
-ATOM   1759  CB  GLU A 695      -4.765 -30.975 -13.987  1.00 66.94           C  
-ANISOU 1759  CB  GLU A 695    11558   6952   6924    299   -207   -364       C  
-ATOM   1760  CG  GLU A 695      -4.934 -32.322 -13.307  1.00 67.97           C  
-ANISOU 1760  CG  GLU A 695    11935   6930   6960    289   -246   -368       C  
-ATOM   1761  CD  GLU A 695      -6.199 -33.036 -13.744  1.00 78.34           C  
-ANISOU 1761  CD  GLU A 695    13254   8225   8288    199   -127   -349       C  
-ATOM   1762  OE1 GLU A 695      -6.122 -34.239 -14.069  1.00 85.63           O  
-ANISOU 1762  OE1 GLU A 695    14242   9104   9192    221   -189   -371       O  
-ATOM   1763  OE2 GLU A 695      -7.269 -32.390 -13.769  1.00 76.75           O  
-ANISOU 1763  OE2 GLU A 695    12988   8054   8120    107     28   -315       O  
-ATOM   1764  N   CYS A 696      -4.272 -28.786 -16.303  1.00 67.49           N  
-ANISOU 1764  N   CYS A 696    11049   7377   7217    337   -171   -371       N  
-ATOM   1765  CA  CYS A 696      -4.680 -27.557 -16.974  1.00 58.42           C  
-ANISOU 1765  CA  CYS A 696     9689   6350   6155    298    -80   -342       C  
-ATOM   1766  C   CYS A 696      -4.484 -27.666 -18.484  1.00 47.12           C  
-ANISOU 1766  C   CYS A 696     8038   5061   4804    323   -107   -363       C  
-ATOM   1767  O   CYS A 696      -5.141 -26.970 -19.256  1.00 40.03           O  
-ANISOU 1767  O   CYS A 696     6972   4258   3980    274    -17   -334       O  
-ATOM   1768  CB  CYS A 696      -3.892 -26.361 -16.431  1.00 54.84           C  
-ANISOU 1768  CB  CYS A 696     9208   5922   5707    335   -117   -341       C  
-ATOM   1769  SG  CYS A 696      -4.111 -26.046 -14.663  1.00 59.29           S  
-ANISOU 1769  SG  CYS A 696    10012   6334   6179    302    -79   -318       S  
-ATOM   1770  N   LEU A 697      -3.577 -28.548 -18.894  1.00 48.53           N  
-ANISOU 1770  N   LEU A 697     8221   5251   4968    398   -235   -415       N  
-ATOM   1771  CA  LEU A 697      -3.266 -28.737 -20.308  1.00 49.34           C  
-ANISOU 1771  CA  LEU A 697     8122   5487   5137    426   -273   -445       C  
-ATOM   1772  C   LEU A 697      -4.166 -29.778 -20.969  1.00 50.11           C  
-ANISOU 1772  C   LEU A 697     8214   5580   5247    384   -221   -444       C  
-ATOM   1773  O   LEU A 697      -3.876 -30.248 -22.069  1.00 56.56           O  
-ANISOU 1773  O   LEU A 697     8898   6487   6103    413   -267   -479       O  
-ATOM   1774  CB  LEU A 697      -1.798 -29.135 -20.486  1.00 48.06           C  
-ANISOU 1774  CB  LEU A 697     7946   5353   4962    530   -437   -515       C  
-ATOM   1775  CG  LEU A 697      -0.751 -28.041 -20.292  1.00 42.08           C  
-ANISOU 1775  CG  LEU A 697     7114   4654   4220    579   -497   -532       C  
-ATOM   1776  CD1 LEU A 697       0.649 -28.595 -20.502  1.00 28.29           C  
-ANISOU 1776  CD1 LEU A 697     5356   2931   2464    680   -661   -616       C  
-ATOM   1777  CD2 LEU A 697      -1.018 -26.897 -21.249  1.00 47.10           C  
-ANISOU 1777  CD2 LEU A 697     7523   5435   4937    537   -419   -502       C  
-ATOM   1778  N   LYS A 698      -5.255 -30.135 -20.296  1.00 50.78           N  
-ANISOU 1778  N   LYS A 698     8440   5558   5296    313   -122   -408       N  
-ATOM   1779  CA  LYS A 698      -6.193 -31.124 -20.822  1.00 55.06           C  
-ANISOU 1779  CA  LYS A 698     8991   6083   5847    266    -63   -407       C  
-ATOM   1780  C   LYS A 698      -6.767 -30.700 -22.173  1.00 53.00           C  
-ANISOU 1780  C   LYS A 698     8493   5967   5678    231      8   -396       C  
-ATOM   1781  O   LYS A 698      -7.215 -29.565 -22.338  1.00 50.01           O  
-ANISOU 1781  O   LYS A 698     8002   5652   5347    189     90   -358       O  
-ATOM   1782  CB  LYS A 698      -7.328 -31.365 -19.822  1.00 53.09           C  
-ANISOU 1782  CB  LYS A 698     8922   5702   5548    182     51   -369       C  
-ATOM   1783  CG  LYS A 698      -6.953 -32.256 -18.647  1.00 51.98           C  
-ANISOU 1783  CG  LYS A 698     9043   5403   5306    205    -18   -382       C  
-ATOM   1784  CD  LYS A 698      -7.343 -33.701 -18.912  1.00 66.64           C  
-ANISOU 1784  CD  LYS A 698    10986   7195   7137    194    -31   -403       C  
-ATOM   1785  CE  LYS A 698      -6.821 -34.634 -17.832  1.00 76.44           C  
-ANISOU 1785  CE  LYS A 698    12487   8280   8277    228   -126   -418       C  
-ATOM   1786  NZ  LYS A 698      -5.346 -34.813 -17.923  1.00 82.89           N  
-ANISOU 1786  NZ  LYS A 698    13294   9116   9084    345   -304   -467       N  
-ATOM   1787  N   LYS A 699      -6.749 -31.617 -23.138  1.00 45.86           N  
-ANISOU 1787  N   LYS A 699     7515   5112   4796    250    -29   -429       N  
-ATOM   1788  CA  LYS A 699      -7.334 -31.351 -24.448  1.00 47.52           C  
-ANISOU 1788  CA  LYS A 699     7513   5455   5087    216     33   -421       C  
-ATOM   1789  C   LYS A 699      -8.810 -31.026 -24.277  1.00 46.55           C  
-ANISOU 1789  C   LYS A 699     7397   5302   4988    119    189   -373       C  
-ATOM   1790  O   LYS A 699      -9.346 -30.132 -24.934  1.00 47.09           O  
-ANISOU 1790  O   LYS A 699     7303   5465   5122     80    262   -344       O  
-ATOM   1791  CB  LYS A 699      -7.187 -32.564 -25.373  1.00 70.36           C  
-ANISOU 1791  CB  LYS A 699    10358   8385   7991    245    -25   -469       C  
-ATOM   1792  CG  LYS A 699      -5.756 -33.031 -25.623  1.00 81.01           C  
-ANISOU 1792  CG  LYS A 699    11692   9766   9324    342   -183   -532       C  
-ATOM   1793  CD  LYS A 699      -5.741 -34.292 -26.487  1.00 74.08           C  
-ANISOU 1793  CD  LYS A 699    10774   8913   8458    364   -231   -583       C  
-ATOM   1794  CE  LYS A 699      -4.332 -34.832 -26.693  1.00 65.34           C  
-ANISOU 1794  CE  LYS A 699     9658   7831   7339    462   -392   -658       C  
-ATOM   1795  NZ  LYS A 699      -3.480 -33.908 -27.490  1.00 68.54           N  
-ANISOU 1795  NZ  LYS A 699     9862   8389   7789    495   -436   -679       N  
-ATOM   1796  N   LYS A 700      -9.458 -31.762 -23.381  1.00 56.09           N  
-ANISOU 1796  N   LYS A 700     8797   6372   6141     78    238   -367       N  
-ATOM   1797  CA  LYS A 700     -10.886 -31.618 -23.143  1.00 56.79           C  
-ANISOU 1797  CA  LYS A 700     8911   6420   6248    -18    388   -335       C  
-ATOM   1798  C   LYS A 700     -11.170 -30.528 -22.117  1.00 61.93           C  
-ANISOU 1798  C   LYS A 700     9625   7020   6884    -58    458   -298       C  
-ATOM   1799  O   LYS A 700     -10.662 -30.558 -20.997  1.00 55.93           O  
-ANISOU 1799  O   LYS A 700     9037   6161   6053    -39    418   -297       O  
-ATOM   1800  CB  LYS A 700     -11.480 -32.950 -22.690  1.00 48.70           C  
-ANISOU 1800  CB  LYS A 700     8062   5273   5170    -53    416   -350       C  
-ATOM   1801  CG  LYS A 700     -10.956 -34.134 -23.487  1.00 54.73           C  
-ANISOU 1801  CG  LYS A 700     8800   6062   5932      3    318   -394       C  
-ATOM   1802  CD  LYS A 700     -11.655 -35.427 -23.106  1.00 60.67           C  
-ANISOU 1802  CD  LYS A 700     9718   6695   6640    -40    355   -407       C  
-ATOM   1803  CE  LYS A 700     -11.086 -36.602 -23.889  1.00 67.17           C  
-ANISOU 1803  CE  LYS A 700    10515   7540   7466     20    249   -455       C  
-ATOM   1804  NZ  LYS A 700     -11.785 -37.884 -23.588  1.00 71.14           N  
-ANISOU 1804  NZ  LYS A 700    11172   7926   7930    -24    285   -466       N  
-ATOM   1805  N   ARG A 701     -11.994 -29.572 -22.526  1.00 69.27           N  
-ANISOU 1805  N   ARG A 701    10415   8019   7886   -112    560   -271       N  
-ATOM   1806  CA  ARG A 701     -12.327 -28.399 -21.729  1.00 64.36           C  
-ANISOU 1806  CA  ARG A 701     9811   7370   7271   -152    632   -239       C  
-ATOM   1807  C   ARG A 701     -12.760 -28.706 -20.294  1.00 74.19           C  
-ANISOU 1807  C   ARG A 701    11288   8464   8438   -201    690   -236       C  
-ATOM   1808  O   ARG A 701     -12.230 -28.134 -19.340  1.00 68.37           O  
-ANISOU 1808  O   ARG A 701    10646   7675   7657   -184    664   -226       O  
-ATOM   1809  CB  ARG A 701     -13.431 -27.614 -22.436  1.00 61.92           C  
-ANISOU 1809  CB  ARG A 701     9331   7142   7056   -214    745   -219       C  
-ATOM   1810  CG  ARG A 701     -14.247 -26.746 -21.511  1.00 70.92           C  
-ANISOU 1810  CG  ARG A 701    10523   8221   8204   -283    856   -198       C  
-ATOM   1811  CD  ARG A 701     -15.541 -26.321 -22.165  1.00 73.99           C  
-ANISOU 1811  CD  ARG A 701    10770   8661   8681   -351    973   -191       C  
-ATOM   1812  NE  ARG A 701     -15.314 -25.392 -23.264  1.00 78.93           N  
-ANISOU 1812  NE  ARG A 701    11177   9423   9391   -322    941   -172       N  
-ATOM   1813  CZ  ARG A 701     -16.280 -24.720 -23.878  1.00 80.12           C  
-ANISOU 1813  CZ  ARG A 701    11181   9632   9629   -368   1021   -160       C  
-ATOM   1814  NH1 ARG A 701     -17.540 -24.875 -23.497  1.00 78.05           N  
-ANISOU 1814  NH1 ARG A 701    10961   9309   9387   -445   1141   -173       N  
-ATOM   1815  NH2 ARG A 701     -15.986 -23.893 -24.870  1.00 80.64           N  
-ANISOU 1815  NH2 ARG A 701    11061   9817   9762   -340    980   -138       N  
-ATOM   1816  N   ASP A 702     -13.727 -29.608 -20.153  1.00 87.96           N  
-ANISOU 1816  N   ASP A 702    13121  10136  10162   -264    770   -246       N  
-ATOM   1817  CA  ASP A 702     -14.374 -29.863 -18.867  1.00 91.81           C  
-ANISOU 1817  CA  ASP A 702    13818  10486  10580   -335    853   -242       C  
-ATOM   1818  C   ASP A 702     -13.523 -30.697 -17.913  1.00 85.85           C  
-ANISOU 1818  C   ASP A 702    13293   9613   9713   -294    757   -251       C  
-ATOM   1819  O   ASP A 702     -13.866 -30.852 -16.741  1.00 89.44           O  
-ANISOU 1819  O   ASP A 702    13941   9949  10094   -347    809   -244       O  
-ATOM   1820  CB  ASP A 702     -15.738 -30.527 -19.079  1.00104.10           C  
-ANISOU 1820  CB  ASP A 702    15387  12010  12158   -424    979   -254       C  
-ATOM   1821  CG  ASP A 702     -16.746 -29.590 -19.712  1.00112.43           C  
-ANISOU 1821  CG  ASP A 702    16249  13153  13317   -478   1091   -247       C  
-ATOM   1822  OD1 ASP A 702     -16.422 -28.395 -19.870  1.00117.39           O  
-ANISOU 1822  OD1 ASP A 702    16753  13855  13994   -452   1075   -228       O  
-ATOM   1823  OD2 ASP A 702     -17.859 -30.046 -20.047  1.00113.58           O  
-ANISOU 1823  OD2 ASP A 702    16368  13292  13497   -546   1190   -264       O  
-ATOM   1824  N   GLU A 703     -12.414 -31.228 -18.419  1.00 72.64           N  
-ANISOU 1824  N   GLU A 703    11599   7974   8028   -202    615   -268       N  
-ATOM   1825  CA  GLU A 703     -11.501 -32.019 -17.601  1.00 68.22           C  
-ANISOU 1825  CA  GLU A 703    11245   7307   7370   -148    501   -282       C  
-ATOM   1826  C   GLU A 703     -10.459 -31.148 -16.896  1.00 53.93           C  
-ANISOU 1826  C   GLU A 703     9469   5492   5528    -89    420   -275       C  
-ATOM   1827  O   GLU A 703      -9.491 -31.660 -16.331  1.00 57.32           O  
-ANISOU 1827  O   GLU A 703    10039   5853   5888    -24    299   -291       O  
-ATOM   1828  CB  GLU A 703     -10.804 -33.089 -18.450  1.00 90.43           C  
-ANISOU 1828  CB  GLU A 703    14024  10150  10187    -75    380   -316       C  
-ATOM   1829  CG  GLU A 703     -11.725 -34.202 -18.932  1.00 95.73           C  
-ANISOU 1829  CG  GLU A 703    14717  10791  10867   -128    442   -328       C  
-ATOM   1830  CD  GLU A 703     -10.988 -35.306 -19.675  1.00 94.28           C  
-ANISOU 1830  CD  GLU A 703    14515  10625  10683    -52    315   -367       C  
-ATOM   1831  OE1 GLU A 703     -11.644 -36.287 -20.080  1.00 93.26           O  
-ANISOU 1831  OE1 GLU A 703    14407  10469  10559    -88    352   -380       O  
-ATOM   1832  OE2 GLU A 703      -9.756 -35.197 -19.854  1.00 91.28           O  
-ANISOU 1832  OE2 GLU A 703    14096  10287  10301     42    179   -389       O  
-ATOM   1833  N   ARG A 704     -10.667 -29.833 -16.934  1.00 49.66           N  
-ANISOU 1833  N   ARG A 704     8800   5024   5045   -110    484   -254       N  
-ATOM   1834  CA  ARG A 704      -9.743 -28.881 -16.323  1.00 50.62           C  
-ANISOU 1834  CA  ARG A 704     8931   5154   5149    -59    419   -248       C  
-ATOM   1835  C   ARG A 704     -10.267 -28.372 -14.985  1.00 61.74           C  
-ANISOU 1835  C   ARG A 704    10497   6460   6501   -125    506   -226       C  
-ATOM   1836  O   ARG A 704     -11.463 -28.119 -14.832  1.00 55.67           O  
-ANISOU 1836  O   ARG A 704     9720   5676   5756   -218    647   -212       O  
-ATOM   1837  CB  ARG A 704      -9.493 -27.697 -17.257  1.00 39.16           C  
-ANISOU 1837  CB  ARG A 704     7231   3852   3798    -33    419   -239       C  
-ATOM   1838  CG  ARG A 704      -8.923 -28.071 -18.609  1.00 35.44           C  
-ANISOU 1838  CG  ARG A 704     6591   3495   3381     27    335   -262       C  
-ATOM   1839  CD  ARG A 704      -8.553 -26.820 -19.381  1.00 41.44           C  
-ANISOU 1839  CD  ARG A 704     7130   4392   4223     50    328   -250       C  
-ATOM   1840  NE  ARG A 704      -8.030 -27.115 -20.710  1.00 54.49           N  
-ANISOU 1840  NE  ARG A 704     8614   6163   5926     99    256   -273       N  
-ATOM   1841  CZ  ARG A 704      -8.626 -26.758 -21.843  1.00 56.05           C  
-ANISOU 1841  CZ  ARG A 704     8622   6471   6204     67    314   -258       C  
-ATOM   1842  NH1 ARG A 704      -9.769 -26.088 -21.812  1.00 61.82           N  
-ANISOU 1842  NH1 ARG A 704     9303   7205   6980    -10    440   -223       N  
-ATOM   1843  NH2 ARG A 704      -8.075 -27.066 -23.008  1.00 43.58           N  
-ANISOU 1843  NH2 ARG A 704     6901   4999   4659    110    243   -283       N  
-ATOM   1844  N   PRO A 705      -9.365 -28.233 -14.005  1.00 53.70           N  
-ANISOU 1844  N   PRO A 705     9621   5374   5409    -77    421   -230       N  
-ATOM   1845  CA  PRO A 705      -9.709 -27.747 -12.666  1.00 50.96           C  
-ANISOU 1845  CA  PRO A 705     9435   4930   4998   -133    489   -214       C  
-ATOM   1846  C   PRO A 705      -9.851 -26.231 -12.650  1.00 61.88           C  
-ANISOU 1846  C   PRO A 705    10669   6391   6451   -149    553   -198       C  
-ATOM   1847  O   PRO A 705      -9.077 -25.544 -13.314  1.00 63.64           O  
-ANISOU 1847  O   PRO A 705    10728   6717   6736    -81    481   -201       O  
-ATOM   1848  CB  PRO A 705      -8.499 -28.169 -11.818  1.00 73.48           C  
-ANISOU 1848  CB  PRO A 705    12468   7697   7753    -54    345   -228       C  
-ATOM   1849  CG  PRO A 705      -7.755 -29.171 -12.652  1.00 75.60           C  
-ANISOU 1849  CG  PRO A 705    12704   7992   8027     27    216   -256       C  
-ATOM   1850  CD  PRO A 705      -7.991 -28.751 -14.060  1.00 69.97           C  
-ANISOU 1850  CD  PRO A 705    11726   7429   7431     31    249   -258       C  
-ATOM   1851  N   SER A 706     -10.831 -25.718 -11.912  1.00 71.17           N  
-ANISOU 1851  N   SER A 706    11902   7520   7621   -241    686   -184       N  
-ATOM   1852  CA  SER A 706     -11.011 -24.274 -11.803  1.00 62.82           C  
-ANISOU 1852  CA  SER A 706    10715   6524   6630   -259    748   -172       C  
-ATOM   1853  C   SER A 706      -9.816 -23.638 -11.098  1.00 57.39           C  
-ANISOU 1853  C   SER A 706    10080   5824   5902   -187    645   -174       C  
-ATOM   1854  O   SER A 706      -9.007 -24.332 -10.482  1.00 51.88           O  
-ANISOU 1854  O   SER A 706     9551   5050   5113   -136    543   -186       O  
-ATOM   1855  CB  SER A 706     -12.314 -23.935 -11.071  1.00105.18           C  
-ANISOU 1855  CB  SER A 706    16141  11830  11991   -374    911   -168       C  
-ATOM   1856  OG  SER A 706     -12.290 -24.388  -9.728  1.00113.62           O  
-ANISOU 1856  OG  SER A 706    17462  12768  12941   -408    920   -172       O  
-ATOM   1857  N   PHE A 707      -9.706 -22.318 -11.199  1.00 67.43           N  
-ANISOU 1857  N   PHE A 707    11205   7169   7245   -180    668   -165       N  
-ATOM   1858  CA  PHE A 707      -8.588 -21.598 -10.597  1.00 67.75           C  
-ANISOU 1858  CA  PHE A 707    11271   7210   7261   -112    576   -170       C  
-ATOM   1859  C   PHE A 707      -8.574 -21.635  -9.067  1.00 76.76           C  
-ANISOU 1859  C   PHE A 707    12644   8226   8296   -141    593   -174       C  
-ATOM   1860  O   PHE A 707      -7.503 -21.661  -8.464  1.00 87.99           O  
-ANISOU 1860  O   PHE A 707    14165   9611   9655    -71    481   -186       O  
-ATOM   1861  CB  PHE A 707      -8.521 -20.154 -11.103  1.00 55.18           C  
-ANISOU 1861  CB  PHE A 707     9464   5725   5775   -104    602   -158       C  
-ATOM   1862  CG  PHE A 707      -7.587 -19.965 -12.266  1.00 48.69           C  
-ANISOU 1862  CG  PHE A 707     8464   5020   5017    -22    497   -163       C  
-ATOM   1863  CD1 PHE A 707      -6.220 -20.124 -12.103  1.00 45.35           C  
-ANISOU 1863  CD1 PHE A 707     8082   4599   4551     71    356   -186       C  
-ATOM   1864  CD2 PHE A 707      -8.072 -19.622 -13.517  1.00 43.74           C  
-ANISOU 1864  CD2 PHE A 707     7627   4501   4492    -40    539   -148       C  
-ATOM   1865  CE1 PHE A 707      -5.354 -19.951 -13.169  1.00 40.49           C  
-ANISOU 1865  CE1 PHE A 707     7299   4093   3992    140    264   -198       C  
-ATOM   1866  CE2 PHE A 707      -7.210 -19.445 -14.587  1.00 47.10           C  
-ANISOU 1866  CE2 PHE A 707     7892   5036   4969     27    446   -153       C  
-ATOM   1867  CZ  PHE A 707      -5.851 -19.610 -14.412  1.00 45.22           C  
-ANISOU 1867  CZ  PHE A 707     7694   4801   4687    115    312   -180       C  
-ATOM   1868  N   PRO A 708      -9.759 -21.623  -8.430  1.00 71.49           N  
-ANISOU 1868  N   PRO A 708    12061   7494   7607   -245    733   -168       N  
-ATOM   1869  CA  PRO A 708      -9.747 -21.815  -6.977  1.00 68.18           C  
-ANISOU 1869  CA  PRO A 708    11882   6951   7071   -279    747   -172       C  
-ATOM   1870  C   PRO A 708      -8.988 -23.090  -6.624  1.00 62.41           C  
-ANISOU 1870  C   PRO A 708    11351   6132   6229   -226    626   -180       C  
-ATOM   1871  O   PRO A 708      -8.154 -23.086  -5.717  1.00 49.82           O  
-ANISOU 1871  O   PRO A 708     9905   4474   4552   -180    539   -186       O  
-ATOM   1872  CB  PRO A 708     -11.231 -21.964  -6.635  1.00 52.30           C  
-ANISOU 1872  CB  PRO A 708     9923   4891   5056   -407    918   -172       C  
-ATOM   1873  CG  PRO A 708     -11.932 -21.181  -7.691  1.00 49.45           C  
-ANISOU 1873  CG  PRO A 708     9309   4644   4835   -431    998   -168       C  
-ATOM   1874  CD  PRO A 708     -11.114 -21.354  -8.943  1.00 52.70           C  
-ANISOU 1874  CD  PRO A 708     9562   5152   5307   -336    881   -161       C  
-ATOM   1875  N   ARG A 709      -9.273 -24.166  -7.352  1.00 63.46           N  
-ANISOU 1875  N   ARG A 709    11484   6263   6363   -230    615   -180       N  
-ATOM   1876  CA  ARG A 709      -8.571 -25.430  -7.171  1.00 74.31           C  
-ANISOU 1876  CA  ARG A 709    13029   7558   7646   -175    492   -189       C  
-ATOM   1877  C   ARG A 709      -7.083 -25.268  -7.473  1.00 71.74           C  
-ANISOU 1877  C   ARG A 709    12644   7281   7332    -44    319   -208       C  
-ATOM   1878  O   ARG A 709      -6.233 -25.705  -6.699  1.00 73.34           O  
-ANISOU 1878  O   ARG A 709    13021   7401   7443     11    206   -221       O  
-ATOM   1879  CB  ARG A 709      -9.166 -26.506  -8.081  1.00 90.90           C  
-ANISOU 1879  CB  ARG A 709    15098   9668   9772   -200    516   -190       C  
-ATOM   1880  CG  ARG A 709     -10.673 -26.699  -7.951  1.00101.20           C  
-ANISOU 1880  CG  ARG A 709    16434  10938  11081   -329    691   -181       C  
-ATOM   1881  CD  ARG A 709     -11.053 -27.469  -6.693  1.00108.05           C  
-ANISOU 1881  CD  ARG A 709    17589  11652  11814   -399    729   -176       C  
-ATOM   1882  NE  ARG A 709     -12.338 -28.149  -6.846  1.00113.59           N  
-ANISOU 1882  NE  ARG A 709    18327  12316  12514   -507    863   -176       N  
-ATOM   1883  CZ  ARG A 709     -12.472 -29.423  -7.205  1.00116.40           C  
-ANISOU 1883  CZ  ARG A 709    18767  12623  12836   -511    833   -179       C  
-ATOM   1884  NH1 ARG A 709     -11.397 -30.164  -7.443  1.00112.26           N  
-ANISOU 1884  NH1 ARG A 709    18298  12079  12277   -409    669   -183       N  
-ATOM   1885  NH2 ARG A 709     -13.679 -29.959  -7.324  1.00117.21           N  
-ANISOU 1885  NH2 ARG A 709    18896  12696  12943   -615    966   -182       N  
-ATOM   1886  N   ILE A 710      -6.778 -24.640  -8.604  1.00 70.37           N  
-ANISOU 1886  N   ILE A 710    12224   7242   7270      2    298   -213       N  
-ATOM   1887  CA  ILE A 710      -5.397 -24.419  -9.017  1.00 69.74           C  
-ANISOU 1887  CA  ILE A 710    12057   7226   7214    118    145   -239       C  
-ATOM   1888  C   ILE A 710      -4.635 -23.591  -7.987  1.00 76.75           C  
-ANISOU 1888  C   ILE A 710    13020   8081   8060    156     94   -246       C  
-ATOM   1889  O   ILE A 710      -3.462 -23.845  -7.716  1.00 74.96           O  
-ANISOU 1889  O   ILE A 710    12860   7832   7791    247    -51   -275       O  
-ATOM   1890  CB  ILE A 710      -5.331 -23.694 -10.373  1.00 57.44           C  
-ANISOU 1890  CB  ILE A 710    10215   5824   5784    139    157   -238       C  
-ATOM   1891  CG1 ILE A 710      -6.289 -24.341 -11.374  1.00 52.52           C  
-ANISOU 1891  CG1 ILE A 710     9503   5240   5210     87    233   -228       C  
-ATOM   1892  CG2 ILE A 710      -3.908 -23.687 -10.907  1.00 62.99           C  
-ANISOU 1892  CG2 ILE A 710    10831   6594   6507    254     -2   -274       C  
-ATOM   1893  CD1 ILE A 710      -6.258 -23.705 -12.741  1.00 47.96           C  
-ANISOU 1893  CD1 ILE A 710     8657   4814   4751    104    242   -225       C  
-ATOM   1894  N   LEU A 711      -5.309 -22.594  -7.421  1.00 74.49           N  
-ANISOU 1894  N   LEU A 711    12718   7794   7791     86    212   -226       N  
-ATOM   1895  CA  LEU A 711      -4.705 -21.730  -6.413  1.00 72.63           C  
-ANISOU 1895  CA  LEU A 711    12547   7528   7520    111    181   -232       C  
-ATOM   1896  C   LEU A 711      -4.454 -22.515  -5.131  1.00 71.10           C  
-ANISOU 1896  C   LEU A 711    12641   7190   7186    113    128   -239       C  
-ATOM   1897  O   LEU A 711      -3.331 -22.567  -4.631  1.00 67.11           O  
-ANISOU 1897  O   LEU A 711    12219   6651   6629    198     -6   -263       O  
-ATOM   1898  CB  LEU A 711      -5.603 -20.522  -6.131  1.00 75.62           C  
-ANISOU 1898  CB  LEU A 711    12840   7938   7955     28    328   -212       C  
-ATOM   1899  CG  LEU A 711      -5.085 -19.496  -5.121  1.00 76.82           C  
-ANISOU 1899  CG  LEU A 711    13037   8069   8083     46    314   -220       C  
-ATOM   1900  CD1 LEU A 711      -3.726 -18.958  -5.545  1.00 77.64           C  
-ANISOU 1900  CD1 LEU A 711    13020   8250   8230    157    177   -242       C  
-ATOM   1901  CD2 LEU A 711      -6.084 -18.360  -4.938  1.00 74.58           C  
-ANISOU 1901  CD2 LEU A 711    12654   7816   7865    -42    466   -204       C  
-ATOM   1902  N   ALA A 712      -5.509 -23.129  -4.606  1.00 75.72           N  
-ANISOU 1902  N   ALA A 712    13377   7686   7707     16    232   -220       N  
-ATOM   1903  CA  ALA A 712      -5.396 -23.966  -3.420  1.00 72.82           C  
-ANISOU 1903  CA  ALA A 712    13299   7173   7198      1    192   -219       C  
-ATOM   1904  C   ALA A 712      -4.292 -24.998  -3.599  1.00 70.73           C  
-ANISOU 1904  C   ALA A 712    13123   6868   6884    107     10   -242       C  
-ATOM   1905  O   ALA A 712      -3.453 -25.182  -2.719  1.00 75.70           O  
-ANISOU 1905  O   ALA A 712    13920   7419   7425    164   -101   -256       O  
-ATOM   1906  CB  ALA A 712      -6.718 -24.652  -3.128  1.00 47.68           C  
-ANISOU 1906  CB  ALA A 712    10239   3913   3966   -121    330   -198       C  
-ATOM   1907  N   GLU A 713      -4.297 -25.671  -4.744  1.00 59.88           N  
-ANISOU 1907  N   GLU A 713    11634   5549   5568    135    -21   -249       N  
-ATOM   1908  CA  GLU A 713      -3.290 -26.683  -5.033  1.00 66.20           C  
-ANISOU 1908  CA  GLU A 713    12497   6320   6336    236   -193   -278       C  
-ATOM   1909  C   GLU A 713      -1.878 -26.125  -4.910  1.00 69.63           C  
-ANISOU 1909  C   GLU A 713    12881   6792   6782    354   -342   -315       C  
-ATOM   1910  O   GLU A 713      -1.092 -26.596  -4.093  1.00 77.83           O  
-ANISOU 1910  O   GLU A 713    14105   7736   7731    414   -467   -335       O  
-ATOM   1911  CB  GLU A 713      -3.511 -27.283  -6.421  1.00101.89           C  
-ANISOU 1911  CB  GLU A 713    16852  10922  10940    248   -193   -286       C  
-ATOM   1912  CG  GLU A 713      -4.776 -28.110  -6.521  1.00118.10           C  
-ANISOU 1912  CG  GLU A 713    18984  12919  12969    145    -73   -259       C  
-ATOM   1913  CD  GLU A 713      -4.781 -29.265  -5.546  1.00127.47           C  
-ANISOU 1913  CD  GLU A 713    20468  13943  14022    129   -124   -254       C  
-ATOM   1914  OE1 GLU A 713      -3.700 -29.847  -5.317  1.00125.13           O  
-ANISOU 1914  OE1 GLU A 713    20273  13595  13676    226   -291   -280       O  
-ATOM   1915  OE2 GLU A 713      -5.861 -29.593  -5.012  1.00133.12           O  
-ANISOU 1915  OE2 GLU A 713    21316  14581  14683     19      1   -226       O  
-ATOM   1916  N   ILE A 714      -1.561 -25.117  -5.715  1.00 79.50           N  
-ANISOU 1916  N   ILE A 714    13883   8180   8143    386   -332   -327       N  
-ATOM   1917  CA  ILE A 714      -0.227 -24.526  -5.701  1.00 79.06           C  
-ANISOU 1917  CA  ILE A 714    13753   8174   8111    493   -464   -368       C  
-ATOM   1918  C   ILE A 714       0.138 -23.973  -4.324  1.00 77.70           C  
-ANISOU 1918  C   ILE A 714    13744   7920   7859    500   -487   -369       C  
-ATOM   1919  O   ILE A 714       1.284 -24.081  -3.885  1.00 80.97           O  
-ANISOU 1919  O   ILE A 714    14231   8302   8233    595   -635   -409       O  
-ATOM   1920  CB  ILE A 714      -0.088 -23.419  -6.763  1.00 71.79           C  
-ANISOU 1920  CB  ILE A 714    12541   7414   7321    505   -424   -372       C  
-ATOM   1921  CG1 ILE A 714      -0.425 -23.975  -8.148  1.00 58.40           C  
-ANISOU 1921  CG1 ILE A 714    10685   5804   5700    498   -406   -373       C  
-ATOM   1922  CG2 ILE A 714       1.316 -22.841  -6.750  1.00 73.28           C  
-ANISOU 1922  CG2 ILE A 714    12655   7655   7534    612   -560   -421       C  
-ATOM   1923  CD1 ILE A 714      -0.101 -23.034  -9.283  1.00 58.48           C  
-ANISOU 1923  CD1 ILE A 714    10418   5972   5830    522   -396   -382       C  
-ATOM   1924  N   GLU A 715      -0.843 -23.389  -3.645  1.00 73.42           N  
-ANISOU 1924  N   GLU A 715    13258   7344   7294    400   -342   -330       N  
-ATOM   1925  CA  GLU A 715      -0.632 -22.817  -2.321  1.00 81.55           C  
-ANISOU 1925  CA  GLU A 715    14440   8300   8247    392   -343   -329       C  
-ATOM   1926  C   GLU A 715      -0.316 -23.924  -1.322  1.00 87.69           C  
-ANISOU 1926  C   GLU A 715    15510   8925   8882    412   -440   -335       C  
-ATOM   1927  O   GLU A 715       0.572 -23.787  -0.479  1.00 97.77           O  
-ANISOU 1927  O   GLU A 715    16907  10147  10094    477   -550   -359       O  
-ATOM   1928  CB  GLU A 715      -1.877 -22.049  -1.874  1.00 90.14           C  
-ANISOU 1928  CB  GLU A 715    15520   9385   9344    268   -155   -291       C  
-ATOM   1929  CG  GLU A 715      -1.617 -20.968  -0.835  1.00 94.80           C  
-ANISOU 1929  CG  GLU A 715    16154   9959   9909    264   -137   -297       C  
-ATOM   1930  CD  GLU A 715      -1.371 -19.605  -1.457  1.00 89.81           C  
-ANISOU 1930  CD  GLU A 715    15262   9458   9403    288   -107   -305       C  
-ATOM   1931  OE1 GLU A 715      -0.199 -19.281  -1.743  1.00 90.69           O  
-ANISOU 1931  OE1 GLU A 715    15285   9624   9550    390   -232   -338       O  
-ATOM   1932  OE2 GLU A 715      -2.350 -18.856  -1.658  1.00 83.14           O  
-ANISOU 1932  OE2 GLU A 715    14302   8661   8625    203     41   -281       O  
-ATOM   1933  N   GLU A 716      -1.053 -25.025  -1.427  1.00 85.10           N  
-ANISOU 1933  N   GLU A 716    15299   8528   8506    355   -401   -312       N  
-ATOM   1934  CA  GLU A 716      -0.825 -26.184  -0.575  1.00 93.70           C  
-ANISOU 1934  CA  GLU A 716    16673   9467   9460    367   -494   -312       C  
-ATOM   1935  C   GLU A 716       0.494 -26.889  -0.893  1.00 93.25           C  
-ANISOU 1935  C   GLU A 716    16634   9399   9399    504   -705   -359       C  
-ATOM   1936  O   GLU A 716       1.217 -27.287   0.017  1.00101.91           O  
-ANISOU 1936  O   GLU A 716    17934  10391  10398    560   -831   -376       O  
-ATOM   1937  CB  GLU A 716      -1.997 -27.165  -0.663  1.00 97.24           C  
-ANISOU 1937  CB  GLU A 716    17233   9847   9865    263   -389   -277       C  
-ATOM   1938  CG  GLU A 716      -3.229 -26.746   0.132  1.00 96.45           C  
-ANISOU 1938  CG  GLU A 716    17228   9702   9718    122   -204   -239       C  
-ATOM   1939  CD  GLU A 716      -4.414 -27.656  -0.124  1.00 91.48           C  
-ANISOU 1939  CD  GLU A 716    16668   9024   9066     17    -89   -212       C  
-ATOM   1940  OE1 GLU A 716      -4.480 -28.242  -1.225  1.00 83.32           O  
-ANISOU 1940  OE1 GLU A 716    15511   8043   8102     43   -110   -219       O  
-ATOM   1941  OE2 GLU A 716      -5.277 -27.784   0.771  1.00 89.28           O  
-ANISOU 1941  OE2 GLU A 716    16565   8658   8700    -94     24   -188       O  
-ATOM   1942  N   LEU A 717       0.818 -27.046  -2.172  1.00 83.74           N  
-ANISOU 1942  N   LEU A 717    15220   8300   8299    560   -747   -385       N  
-ATOM   1943  CA  LEU A 717       2.094 -27.662  -2.527  1.00 80.59           C  
-ANISOU 1943  CA  LEU A 717    14813   7900   7908    691   -946   -443       C  
-ATOM   1944  C   LEU A 717       3.238 -26.665  -2.377  1.00 83.46           C  
-ANISOU 1944  C   LEU A 717    15070   8331   8312    784  -1038   -488       C  
-ATOM   1945  O   LEU A 717       4.384 -26.967  -2.706  1.00 90.28           O  
-ANISOU 1945  O   LEU A 717    15890   9215   9197    898  -1200   -549       O  
-ATOM   1946  CB  LEU A 717       2.063 -28.232  -3.947  1.00 75.82           C  
-ANISOU 1946  CB  LEU A 717    14025   7387   7398    716   -960   -462       C  
-ATOM   1947  CG  LEU A 717       1.829 -27.242  -5.089  1.00 63.55           C  
-ANISOU 1947  CG  LEU A 717    12164   6004   5978    696   -863   -460       C  
-ATOM   1948  CD1 LEU A 717       3.141 -26.853  -5.766  1.00 58.18           C  
-ANISOU 1948  CD1 LEU A 717    11305   5428   5374    814   -998   -526       C  
-ATOM   1949  CD2 LEU A 717       0.856 -27.846  -6.089  1.00 65.19           C  
-ANISOU 1949  CD2 LEU A 717    12281   6253   6235    630   -765   -435       C  
-ATOM   1950  N   ALA A 718       2.920 -25.479  -1.868  1.00 68.17           N  
-ANISOU 1950  N   ALA A 718    13089   6427   6385    733   -934   -465       N  
-ATOM   1951  CA  ALA A 718       3.912 -24.422  -1.724  1.00 75.01           C  
-ANISOU 1951  CA  ALA A 718    13843   7362   7297    808  -1002   -505       C  
-ATOM   1952  C   ALA A 718       4.562 -24.403  -0.342  1.00 98.12           C  
-ANISOU 1952  C   ALA A 718    16995  10173  10112    852  -1100   -522       C  
-ATOM   1953  O   ALA A 718       5.775 -24.234  -0.230  1.00103.28           O  
-ANISOU 1953  O   ALA A 718    17625  10840  10775    962  -1249   -581       O  
-ATOM   1954  CB  ALA A 718       3.295 -23.071  -2.037  1.00 73.52           C  
-ANISOU 1954  CB  ALA A 718    13456   7283   7197    738   -845   -475       C  
-ATOM   1955  N   ARG A 719       3.756 -24.575   0.703  1.00113.87           N  
-ANISOU 1955  N   ARG A 719    19205  12056  12002    764  -1018   -475       N  
-ATOM   1956  CA  ARG A 719       4.231 -24.456   2.086  1.00113.34           C  
-ANISOU 1956  CA  ARG A 719    19361  11881  11822    788  -1090   -483       C  
-ATOM   1957  C   ARG A 719       5.662 -24.955   2.297  1.00107.55           C  
-ANISOU 1957  C   ARG A 719    18703  11105  11058    931  -1316   -548       C  
-ATOM   1958  O   ARG A 719       6.440 -24.337   3.024  1.00100.11           O  
-ANISOU 1958  O   ARG A 719    17799  10148  10089    990  -1393   -581       O  
-ATOM   1959  CB  ARG A 719       3.279 -25.165   3.057  1.00120.17           C  
-ANISOU 1959  CB  ARG A 719    20502  12604  12552    685  -1015   -431       C  
-ATOM   1960  CG  ARG A 719       1.924 -24.496   3.210  1.00122.92           C  
-ANISOU 1960  CG  ARG A 719    20810  12980  12915    541   -792   -379       C  
-ATOM   1961  CD  ARG A 719       1.086 -25.182   4.279  1.00130.05           C  
-ANISOU 1961  CD  ARG A 719    22001  13738  13673    438   -724   -336       C  
-ATOM   1962  NE  ARG A 719      -0.199 -24.520   4.493  1.00135.42           N  
-ANISOU 1962  NE  ARG A 719    22643  14443  14366    299   -509   -298       N  
-ATOM   1963  CZ  ARG A 719      -1.115 -24.939   5.361  1.00139.56           C  
-ANISOU 1963  CZ  ARG A 719    23384  14863  14778    183   -408   -264       C  
-ATOM   1964  NH1 ARG A 719      -0.887 -26.019   6.094  1.00141.90           N  
-ANISOU 1964  NH1 ARG A 719    23959  15020  14938    189   -503   -254       N  
-ATOM   1965  NH2 ARG A 719      -2.258 -24.281   5.496  1.00140.45           N  
-ANISOU 1965  NH2 ARG A 719    23437  15010  14918     60   -213   -242       N  
-ATOM   1966  N   GLU A 720       5.999 -26.072   1.662  1.00105.75           N  
-ANISOU 1966  N   GLU A 720    18491  10854  10836    988  -1424   -573       N  
-ATOM   1967  CA  GLU A 720       7.333 -26.651   1.776  1.00106.33           C  
-ANISOU 1967  CA  GLU A 720    18628  10884  10889   1127  -1646   -644       C  
-ATOM   1968  C   GLU A 720       8.428 -25.606   1.568  1.00107.96           C  
-ANISOU 1968  C   GLU A 720    18642  11197  11179   1220  -1720   -709       C  
-ATOM   1969  O   GLU A 720       9.088 -25.576   0.529  1.00108.06           O  
-ANISOU 1969  O   GLU A 720    18448  11314  11295   1291  -1784   -764       O  
-ATOM   1970  CB  GLU A 720       7.503 -27.804   0.782  1.00113.46           C  
-ANISOU 1970  CB  GLU A 720    19486  11793  11832   1173  -1729   -670       C  
-ATOM   1971  CG  GLU A 720       6.517 -28.949   0.978  1.00121.28           C  
-ANISOU 1971  CG  GLU A 720    20675  12667  12738   1090  -1676   -612       C  
-ATOM   1972  CD  GLU A 720       5.091 -28.568   0.619  1.00127.43           C  
-ANISOU 1972  CD  GLU A 720    21371  13500  13548    946  -1446   -542       C  
-ATOM   1973  OE1 GLU A 720       4.906 -27.597  -0.145  1.00129.36           O  
-ANISOU 1973  OE1 GLU A 720    21361  13886  13903    926  -1346   -542       O  
-ATOM   1974  OE2 GLU A 720       4.154 -29.242   1.095  1.00129.80           O  
-ANISOU 1974  OE2 GLU A 720    21860  13696  13761    853  -1367   -488       O  
-TER    1975      GLU A 720                                                      
-ATOM   1976  N   ASP B 449     -19.744  -2.620  -7.379  1.00 84.65           N  
-ANISOU 1976  N   ASP B 449    11150  11526   9486  -1909   1102   -808       N  
-ATOM   1977  CA  ASP B 449     -19.689  -2.892  -5.948  1.00 82.57           C  
-ANISOU 1977  CA  ASP B 449    10987  11169   9215  -1963   1142   -855       C  
-ATOM   1978  C   ASP B 449     -18.336  -3.454  -5.526  1.00 66.83           C  
-ANISOU 1978  C   ASP B 449     9132   9015   7244  -1818   1179   -773       C  
-ATOM   1979  O   ASP B 449     -17.879  -4.468  -6.053  1.00 60.47           O  
-ANISOU 1979  O   ASP B 449     8494   8109   6372  -1807   1239   -728       O  
-ATOM   1980  CB  ASP B 449     -20.802  -3.864  -5.538  1.00 89.16           C  
-ANISOU 1980  CB  ASP B 449    11973  11985   9920  -2217   1221   -949       C  
-ATOM   1981  CG  ASP B 449     -22.188  -3.276  -5.717  1.00 92.57           C  
-ANISOU 1981  CG  ASP B 449    12261  12593  10318  -2367   1184  -1043       C  
-ATOM   1982  OD1 ASP B 449     -22.898  -3.109  -4.703  1.00 88.89           O  
-ANISOU 1982  OD1 ASP B 449    11781  12164   9831  -2486   1192  -1126       O  
-ATOM   1983  OD2 ASP B 449     -22.566  -2.979  -6.868  1.00 95.98           O  
-ANISOU 1983  OD2 ASP B 449    12592  13138  10739  -2360   1146  -1031       O  
-ATOM   1984  N   TRP B 450     -17.697  -2.781  -4.577  1.00 51.73           N  
-ANISOU 1984  N   TRP B 450     7154   7084   5417  -1703   1145   -756       N  
-ATOM   1985  CA  TRP B 450     -16.477  -3.294  -3.973  1.00 57.82           C  
-ANISOU 1985  CA  TRP B 450     8057   7718   6195  -1572   1180   -687       C  
-ATOM   1986  C   TRP B 450     -16.833  -4.055  -2.706  1.00 52.61           C  
-ANISOU 1986  C   TRP B 450     7572   6967   5451  -1701   1252   -742       C  
-ATOM   1987  O   TRP B 450     -15.964  -4.414  -1.911  1.00 39.21           O  
-ANISOU 1987  O   TRP B 450     5986   5167   3745  -1605   1279   -699       O  
-ATOM   1988  CB  TRP B 450     -15.502  -2.158  -3.669  1.00 63.98           C  
-ANISOU 1988  CB  TRP B 450     8668   8537   7105  -1372   1104   -630       C  
-ATOM   1989  CG  TRP B 450     -15.007  -1.489  -4.903  1.00 54.96           C  
-ANISOU 1989  CG  TRP B 450     7381   7469   6033  -1233   1040   -553       C  
-ATOM   1990  CD1 TRP B 450     -15.390  -0.273  -5.389  1.00 63.15           C  
-ANISOU 1990  CD1 TRP B 450     8216   8635   7144  -1200    958   -557       C  
-ATOM   1991  CD2 TRP B 450     -14.052  -2.010  -5.832  1.00 59.28           C  
-ANISOU 1991  CD2 TRP B 450     7985   7968   6569  -1104   1054   -457       C  
-ATOM   1992  NE1 TRP B 450     -14.723   0.000  -6.557  1.00 73.80           N  
-ANISOU 1992  NE1 TRP B 450     9490  10018   8532  -1065    921   -459       N  
-ATOM   1993  CE2 TRP B 450     -13.896  -1.051  -6.851  1.00 72.05           C  
-ANISOU 1993  CE2 TRP B 450     9414   9697   8263  -1007    978   -400       C  
-ATOM   1994  CE3 TRP B 450     -13.310  -3.192  -5.897  1.00 65.25           C  
-ANISOU 1994  CE3 TRP B 450     8946   8598   7249  -1053   1126   -410       C  
-ATOM   1995  CZ2 TRP B 450     -13.026  -1.239  -7.925  1.00 68.29           C  
-ANISOU 1995  CZ2 TRP B 450     8926   9223   7798   -874    970   -300       C  
-ATOM   1996  CZ3 TRP B 450     -12.449  -3.377  -6.962  1.00 58.90           C  
-ANISOU 1996  CZ3 TRP B 450     8133   7794   6453   -911   1119   -320       C  
-ATOM   1997  CH2 TRP B 450     -12.314  -2.407  -7.961  1.00 61.85           C  
-ANISOU 1997  CH2 TRP B 450     8296   8293   6912   -829   1041   -266       C  
-ATOM   1998  N   GLU B 451     -18.129  -4.291  -2.529  1.00 59.11           N  
-ANISOU 1998  N   GLU B 451     8416   7839   6203  -1920   1280   -836       N  
-ATOM   1999  CA  GLU B 451     -18.624  -5.060  -1.398  1.00 64.63           C  
-ANISOU 1999  CA  GLU B 451     9286   8464   6805  -2075   1352   -890       C  
-ATOM   2000  C   GLU B 451     -18.249  -6.528  -1.544  1.00 68.46           C  
-ANISOU 2000  C   GLU B 451    10072   8780   7161  -2101   1445   -849       C  
-ATOM   2001  O   GLU B 451     -18.811  -7.242  -2.374  1.00 74.83           O  
-ANISOU 2001  O   GLU B 451    10982   9571   7880  -2221   1488   -869       O  
-ATOM   2002  CB  GLU B 451     -20.144  -4.919  -1.272  1.00 68.43           C  
-ANISOU 2002  CB  GLU B 451     9701   9062   7236  -2311   1358  -1002       C  
-ATOM   2003  CG  GLU B 451     -20.751  -5.800  -0.189  1.00 76.89           C  
-ANISOU 2003  CG  GLU B 451    10959  10066   8189  -2500   1440  -1056       C  
-ATOM   2004  CD  GLU B 451     -22.227  -5.530   0.037  1.00 79.06           C  
-ANISOU 2004  CD  GLU B 451    11134  10484   8421  -2727   1439  -1169       C  
-ATOM   2005  OE1 GLU B 451     -22.743  -5.924   1.105  1.00 77.13           O  
-ANISOU 2005  OE1 GLU B 451    10977  10224   8104  -2871   1489  -1219       O  
-ATOM   2006  OE2 GLU B 451     -22.869  -4.923  -0.847  1.00 79.40           O  
-ANISOU 2006  OE2 GLU B 451    11013  10664   8492  -2757   1387  -1207       O  
-ATOM   2007  N   ILE B 452     -17.288  -6.971  -0.742  1.00 69.35           N  
-ANISOU 2007  N   ILE B 452    10331   8767   7251  -1981   1474   -794       N  
-ATOM   2008  CA  ILE B 452     -16.898  -8.374  -0.719  1.00 65.63           C  
-ANISOU 2008  CA  ILE B 452    10177   8119   6639  -1987   1561   -757       C  
-ATOM   2009  C   ILE B 452     -17.885  -9.160   0.134  1.00 79.73           C  
-ANISOU 2009  C   ILE B 452    12147   9855   8293  -2220   1634   -830       C  
-ATOM   2010  O   ILE B 452     -17.989  -8.929   1.339  1.00 90.09           O  
-ANISOU 2010  O   ILE B 452    13445  11178   9607  -2248   1633   -855       O  
-ATOM   2011  CB  ILE B 452     -15.479  -8.557  -0.151  1.00 48.47           C  
-ANISOU 2011  CB  ILE B 452     8102   5840   4475  -1753   1559   -671       C  
-ATOM   2012  CG1 ILE B 452     -14.472  -7.714  -0.939  1.00 50.64           C  
-ANISOU 2012  CG1 ILE B 452     8178   6182   4881  -1528   1485   -598       C  
-ATOM   2013  CG2 ILE B 452     -15.080 -10.027  -0.163  1.00 44.91           C  
-ANISOU 2013  CG2 ILE B 452     8001   5201   3863  -1742   1646   -636       C  
-ATOM   2014  CD1 ILE B 452     -13.050  -7.805  -0.415  1.00 51.72           C  
-ANISOU 2014  CD1 ILE B 452     8381   6243   5028  -1292   1475   -515       C  
-ATOM   2015  N   PRO B 453     -18.620 -10.091  -0.491  1.00 78.51           N  
-ANISOU 2015  N   PRO B 453    12163   9651   8015  -2395   1698   -865       N  
-ATOM   2016  CA  PRO B 453     -19.603 -10.901   0.234  1.00 78.42           C  
-ANISOU 2016  CA  PRO B 453    12341   9593   7862  -2639   1773   -933       C  
-ATOM   2017  C   PRO B 453     -18.939 -11.632   1.393  1.00 86.59           C  
-ANISOU 2017  C   PRO B 453    13622  10471   8808  -2574   1821   -895       C  
-ATOM   2018  O   PRO B 453     -17.980 -12.374   1.182  1.00 86.31           O  
-ANISOU 2018  O   PRO B 453    13797  10284   8715  -2424   1851   -824       O  
-ATOM   2019  CB  PRO B 453     -20.079 -11.906  -0.821  1.00 66.46           C  
-ANISOU 2019  CB  PRO B 453    11013   8014   6225  -2774   1837   -949       C  
-ATOM   2020  CG  PRO B 453     -19.781 -11.257  -2.128  1.00 65.56           C  
-ANISOU 2020  CG  PRO B 453    10696   7995   6219  -2655   1776   -919       C  
-ATOM   2021  CD  PRO B 453     -18.521 -10.482  -1.907  1.00 68.90           C  
-ANISOU 2021  CD  PRO B 453    10984   8418   6777  -2375   1709   -839       C  
-ATOM   2022  N   ASP B 454     -19.438 -11.416   2.605  1.00 95.95           N  
-ANISOU 2022  N   ASP B 454    14781  11700   9977  -2677   1825   -942       N  
-ATOM   2023  CA  ASP B 454     -18.834 -12.018   3.785  1.00 94.14           C  
-ANISOU 2023  CA  ASP B 454    14764  11342   9661  -2612   1862   -908       C  
-ATOM   2024  C   ASP B 454     -18.813 -13.538   3.670  1.00 88.84           C  
-ANISOU 2024  C   ASP B 454    14484  10474   8798  -2687   1955   -891       C  
-ATOM   2025  O   ASP B 454     -19.776 -14.149   3.206  1.00 86.12           O  
-ANISOU 2025  O   ASP B 454    14250  10119   8354  -2910   2009   -945       O  
-ATOM   2026  CB  ASP B 454     -19.581 -11.597   5.048  1.00 96.99           C  
-ANISOU 2026  CB  ASP B 454    15032  11802  10017  -2755   1859   -974       C  
-ATOM   2027  CG  ASP B 454     -18.706 -11.653   6.281  1.00 95.75           C  
-ANISOU 2027  CG  ASP B 454    14957  11579   9844  -2606   1855   -931       C  
-ATOM   2028  OD1 ASP B 454     -17.701 -10.912   6.328  1.00 83.17           O  
-ANISOU 2028  OD1 ASP B 454    13211  10018   8373  -2375   1792   -877       O  
-ATOM   2029  OD2 ASP B 454     -19.028 -12.425   7.208  1.00 96.70           O  
-ANISOU 2029  OD2 ASP B 454    15292  11625   9824  -2723   1913   -952       O  
-ATOM   2030  N   GLY B 455     -17.707 -14.141   4.091  1.00 76.64           N  
-ANISOU 2030  N   GLY B 455    13152   8775   7193  -2497   1973   -818       N  
-ATOM   2031  CA  GLY B 455     -17.561 -15.584   4.039  1.00 69.71           C  
-ANISOU 2031  CA  GLY B 455    12670   7691   6124  -2534   2060   -797       C  
-ATOM   2032  C   GLY B 455     -16.543 -16.017   3.004  1.00 76.27           C  
-ANISOU 2032  C   GLY B 455    13612   8414   6952  -2325   2063   -723       C  
-ATOM   2033  O   GLY B 455     -16.166 -17.186   2.938  1.00 85.74           O  
-ANISOU 2033  O   GLY B 455    15150   9428   7999  -2293   2129   -693       O  
-ATOM   2034  N   GLN B 456     -16.098 -15.068   2.188  1.00 73.46           N  
-ANISOU 2034  N   GLN B 456    12973   8177   6759  -2182   1992   -695       N  
-ATOM   2035  CA  GLN B 456     -15.098 -15.346   1.168  1.00 64.86           C  
-ANISOU 2035  CA  GLN B 456    11943   7018   5682  -1973   1988   -624       C  
-ATOM   2036  C   GLN B 456     -13.702 -15.064   1.704  1.00 58.38           C  
-ANISOU 2036  C   GLN B 456    11100   6169   4911  -1676   1943   -544       C  
-ATOM   2037  O   GLN B 456     -12.702 -15.422   1.082  1.00 63.68           O  
-ANISOU 2037  O   GLN B 456    11862   6767   5566  -1472   1944   -477       O  
-ATOM   2038  CB  GLN B 456     -15.357 -14.498  -0.078  1.00 68.48           C  
-ANISOU 2038  CB  GLN B 456    12110   7629   6278  -1980   1935   -634       C  
-ATOM   2039  CG  GLN B 456     -16.695 -14.766  -0.738  1.00 76.08           C  
-ANISOU 2039  CG  GLN B 456    13079   8641   7188  -2259   1974   -714       C  
-ATOM   2040  CD  GLN B 456     -16.988 -13.805  -1.872  1.00 80.32           C  
-ANISOU 2040  CD  GLN B 456    13302   9353   7864  -2259   1910   -727       C  
-ATOM   2041  OE1 GLN B 456     -16.180 -12.930  -2.187  1.00 79.42           O  
-ANISOU 2041  OE1 GLN B 456    12970   9318   7889  -2052   1837   -674       O  
-ATOM   2042  NE2 GLN B 456     -18.151 -13.963  -2.493  1.00 80.84           N  
-ANISOU 2042  NE2 GLN B 456    13344   9487   7885  -2493   1936   -799       N  
-ATOM   2043  N   ILE B 457     -13.640 -14.424   2.866  1.00 53.89           N  
-ANISOU 2043  N   ILE B 457    10408   5670   4397  -1655   1904   -553       N  
-ATOM   2044  CA  ILE B 457     -12.363 -14.021   3.439  1.00 61.75           C  
-ANISOU 2044  CA  ILE B 457    11342   6672   5448  -1387   1854   -485       C  
-ATOM   2045  C   ILE B 457     -11.984 -14.863   4.655  1.00 64.14           C  
-ANISOU 2045  C   ILE B 457    11927   6842   5603  -1340   1897   -469       C  
-ATOM   2046  O   ILE B 457     -12.714 -14.905   5.643  1.00 55.60           O  
-ANISOU 2046  O   ILE B 457    10879   5774   4474  -1503   1916   -521       O  
-ATOM   2047  CB  ILE B 457     -12.386 -12.540   3.850  1.00 54.70           C  
-ANISOU 2047  CB  ILE B 457    10074   5973   4737  -1359   1768   -502       C  
-ATOM   2048  CG1 ILE B 457     -13.325 -11.747   2.938  1.00 51.54           C  
-ANISOU 2048  CG1 ILE B 457     9420   5712   4453  -1511   1738   -554       C  
-ATOM   2049  CG2 ILE B 457     -10.979 -11.966   3.830  1.00 56.27           C  
-ANISOU 2049  CG2 ILE B 457    10146   6210   5024  -1068   1706   -424       C  
-ATOM   2050  CD1 ILE B 457     -13.494 -10.298   3.347  1.00 43.38           C  
-ANISOU 2050  CD1 ILE B 457     8037   4861   3586  -1506   1658   -582       C  
-ATOM   2051  N   THR B 458     -10.839 -15.534   4.573  1.00 67.93           N  
-ANISOU 2051  N   THR B 458    12606   7201   6003  -1111   1910   -398       N  
-ATOM   2052  CA  THR B 458     -10.323 -16.311   5.696  1.00 71.18           C  
-ANISOU 2052  CA  THR B 458    13285   7490   6270  -1021   1942   -374       C  
-ATOM   2053  C   THR B 458      -9.379 -15.459   6.535  1.00 78.45           C  
-ANISOU 2053  C   THR B 458    14007   8518   7283   -815   1869   -337       C  
-ATOM   2054  O   THR B 458      -8.276 -15.129   6.103  1.00 82.12           O  
-ANISOU 2054  O   THR B 458    14374   9018   7810   -574   1825   -275       O  
-ATOM   2055  CB  THR B 458      -9.599 -17.587   5.221  1.00 82.53           C  
-ANISOU 2055  CB  THR B 458    15080   8731   7545   -876   2001   -320       C  
-ATOM   2056  OG1 THR B 458     -10.561 -18.625   4.994  1.00 87.98           O  
-ANISOU 2056  OG1 THR B 458    16055   9285   8089  -1104   2087   -365       O  
-ATOM   2057  CG2 THR B 458      -8.594 -18.061   6.265  1.00 76.18           C  
-ANISOU 2057  CG2 THR B 458    14464   7846   6636   -663   2001   -270       C  
-ATOM   2058  N   VAL B 459      -9.825 -15.102   7.736  1.00 89.58           N  
-ANISOU 2058  N   VAL B 459    15352   9990   8694   -916   1858   -380       N  
-ATOM   2059  CA  VAL B 459      -9.054 -14.230   8.615  1.00 79.37           C  
-ANISOU 2059  CA  VAL B 459    13852   8817   7487   -753   1790   -360       C  
-ATOM   2060  C   VAL B 459      -8.035 -14.994   9.454  1.00 70.16           C  
-ANISOU 2060  C   VAL B 459    12931   7548   6181   -549   1804   -308       C  
-ATOM   2061  O   VAL B 459      -8.363 -15.992  10.093  1.00 72.19           O  
-ANISOU 2061  O   VAL B 459    13485   7673   6269   -628   1865   -320       O  
-ATOM   2062  CB  VAL B 459      -9.971 -13.396   9.530  1.00 74.24           C  
-ANISOU 2062  CB  VAL B 459    12991   8306   6912   -945   1766   -434       C  
-ATOM   2063  CG1 VAL B 459     -10.489 -12.190   8.781  1.00 66.44           C  
-ANISOU 2063  CG1 VAL B 459    11655   7477   6113  -1028   1714   -468       C  
-ATOM   2064  CG2 VAL B 459     -11.127 -14.240  10.050  1.00 75.02           C  
-ANISOU 2064  CG2 VAL B 459    13318   8318   6867  -1201   1839   -493       C  
-ATOM   2065  N   GLY B 460      -6.796 -14.511   9.443  1.00 71.56           N  
-ANISOU 2065  N   GLY B 460    12979   7791   6420   -287   1747   -250       N  
-ATOM   2066  CA  GLY B 460      -5.713 -15.143  10.172  1.00 73.84           C  
-ANISOU 2066  CA  GLY B 460    13467   8008   6581    -59   1751   -197       C  
-ATOM   2067  C   GLY B 460      -5.281 -14.353  11.393  1.00 84.28           C  
-ANISOU 2067  C   GLY B 460    14599   9470   7953     16   1693   -208       C  
-ATOM   2068  O   GLY B 460      -6.102 -13.708  12.047  1.00 92.97           O  
-ANISOU 2068  O   GLY B 460    15537  10667   9119   -167   1679   -272       O  
-ATOM   2069  N   GLN B 461      -3.986 -14.392  11.694  1.00 96.40           N  
-ANISOU 2069  N   GLN B 461    16150  11026   9454    288   1661   -150       N  
-ATOM   2070  CA  GLN B 461      -3.460 -13.801  12.926  1.00110.41           C  
-ANISOU 2070  CA  GLN B 461    17785  12923  11241    379   1611   -159       C  
-ATOM   2071  C   GLN B 461      -3.594 -12.280  13.001  1.00119.85           C  
-ANISOU 2071  C   GLN B 461    18569  14327  12640    322   1537   -198       C  
-ATOM   2072  O   GLN B 461      -3.644 -11.594  11.980  1.00134.13           O  
-ANISOU 2072  O   GLN B 461    20177  16199  14589    307   1506   -190       O  
-ATOM   2073  CB  GLN B 461      -1.999 -14.206  13.138  1.00102.28           C  
-ANISOU 2073  CB  GLN B 461    16860  11881  10120    694   1592    -88       C  
-ATOM   2074  CG  GLN B 461      -1.066 -13.787  12.016  1.00100.57           C  
-ANISOU 2074  CG  GLN B 461    16493  11724   9996    886   1551    -31       C  
-ATOM   2075  CD  GLN B 461       0.180 -13.090  12.528  1.00100.78           C  
-ANISOU 2075  CD  GLN B 461    16323  11908  10061   1119   1480      1       C  
-ATOM   2076  OE1 GLN B 461       0.106 -12.225  13.402  1.00 93.33           O  
-ANISOU 2076  OE1 GLN B 461    15165  11104   9192   1068   1434    -40       O  
-ATOM   2077  NE2 GLN B 461       1.332 -13.459  11.981  1.00108.36           N  
-ANISOU 2077  NE2 GLN B 461    17350  12856  10966   1374   1471     70       N  
-ATOM   2078  N   ARG B 462      -3.635 -11.767  14.229  1.00104.05           N  
-ANISOU 2078  N   ARG B 462    16454  12431  10648    294   1508   -240       N  
-ATOM   2079  CA  ARG B 462      -3.785 -10.337  14.486  1.00 99.60           C  
-ANISOU 2079  CA  ARG B 462    15521  12061  10261    234   1441   -289       C  
-ATOM   2080  C   ARG B 462      -2.477  -9.573  14.292  1.00 98.19           C  
-ANISOU 2080  C   ARG B 462    15137  12005  10167    472   1369   -243       C  
-ATOM   2081  O   ARG B 462      -1.391 -10.111  14.513  1.00 94.21           O  
-ANISOU 2081  O   ARG B 462    14762  11473   9560    694   1365   -186       O  
-ATOM   2082  CB  ARG B 462      -4.308 -10.112  15.908  1.00103.92           C  
-ANISOU 2082  CB  ARG B 462    16031  12681  10774    116   1440   -360       C  
-ATOM   2083  CG  ARG B 462      -4.538  -8.652  16.274  1.00104.55           C  
-ANISOU 2083  CG  ARG B 462    15742  12955  11026     43   1376   -426       C  
-ATOM   2084  CD  ARG B 462      -4.742  -8.473  17.773  1.00100.38           C  
-ANISOU 2084  CD  ARG B 462    15182  12513  10446    -14   1371   -491       C  
-ATOM   2085  NE  ARG B 462      -5.868  -9.255  18.277  1.00103.33           N  
-ANISOU 2085  NE  ARG B 462    15756  12798  10705   -221   1437   -533       N  
-ATOM   2086  CZ  ARG B 462      -5.751 -10.442  18.865  1.00106.77           C  
-ANISOU 2086  CZ  ARG B 462    16505  13112  10952   -191   1488   -505       C  
-ATOM   2087  NH1 ARG B 462      -4.555 -10.990  19.029  1.00108.20           N  
-ANISOU 2087  NH1 ARG B 462    16832  13243  11035     53   1480   -436       N  
-ATOM   2088  NH2 ARG B 462      -6.832 -11.081  19.291  1.00107.42           N  
-ANISOU 2088  NH2 ARG B 462    16756  13123  10934   -404   1547   -548       N  
-ATOM   2089  N   ILE B 463      -2.594  -8.313  13.881  1.00120.37           N  
-ANISOU 2089  N   ILE B 463    17626  14953  13156    422   1313   -269       N  
-ATOM   2090  CA  ILE B 463      -1.438  -7.440  13.710  1.00109.34           C  
-ANISOU 2090  CA  ILE B 463    16004  13690  11849    612   1240   -235       C  
-ATOM   2091  C   ILE B 463      -1.545  -6.236  14.643  1.00110.58           C  
-ANISOU 2091  C   ILE B 463    15888  14018  12111    547   1185   -309       C  
-ATOM   2092  O   ILE B 463      -0.542  -5.607  14.981  1.00110.28           O  
-ANISOU 2092  O   ILE B 463    15696  14100  12106    699   1128   -298       O  
-ATOM   2093  CB  ILE B 463      -1.297  -6.955  12.250  1.00 66.88           C  
-ANISOU 2093  CB  ILE B 463    10490   8330   6592    635   1217   -192       C  
-ATOM   2094  CG1 ILE B 463      -0.971  -8.128  11.322  1.00 68.88           C  
-ANISOU 2094  CG1 ILE B 463    11003   8431   6738    739   1267   -120       C  
-ATOM   2095  CG2 ILE B 463      -0.218  -5.888  12.134  1.00 47.66           C  
-ANISOU 2095  CG2 ILE B 463     7792   6055   4261    791   1138   -166       C  
-ATOM   2096  CD1 ILE B 463      -2.155  -9.012  11.004  1.00 65.86           C  
-ANISOU 2096  CD1 ILE B 463    10843   7895   6288    547   1341   -147       C  
-ATOM   2097  N   GLY B 464      -2.766  -5.923  15.062  1.00 80.93           N  
-ANISOU 2097  N   GLY B 464    12073  10278   8400    319   1203   -390       N  
-ATOM   2098  CA  GLY B 464      -2.989  -4.831  15.992  1.00 86.86           C  
-ANISOU 2098  CA  GLY B 464    12579  11182   9243    244   1158   -476       C  
-ATOM   2099  C   GLY B 464      -4.357  -4.198  15.842  1.00 99.56           C  
-ANISOU 2099  C   GLY B 464    14046  12823  10958     -1   1167   -556       C  
-ATOM   2100  O   GLY B 464      -5.271  -4.796  15.274  1.00 91.90           O  
-ANISOU 2100  O   GLY B 464    13208  11752   9957   -139   1219   -554       O  
-ATOM   2101  N   SER B 465      -4.506  -2.983  16.356  1.00162.81           N  
-ANISOU 2101  N   SER B 465    21788  20980  19091    -54   1117   -634       N  
-ATOM   2102  CA  SER B 465      -5.784  -2.294  16.272  1.00167.73           C  
-ANISOU 2102  CA  SER B 465    22259  21653  19819   -271   1121   -720       C  
-ATOM   2103  C   SER B 465      -5.592  -0.832  15.894  1.00171.32           C  
-ANISOU 2103  C   SER B 465    22408  22231  20456   -257   1050   -759       C  
-ATOM   2104  O   SER B 465      -4.973  -0.065  16.629  1.00177.30           O  
-ANISOU 2104  O   SER B 465    23008  23097  21261   -185   1001   -804       O  
-ATOM   2105  CB  SER B 465      -6.571  -2.426  17.580  1.00100.44           C  
-ANISOU 2105  CB  SER B 465    13759  13171  11231   -411   1151   -811       C  
-ATOM   2106  OG  SER B 465      -5.993  -1.665  18.627  1.00 90.59           O  
-ANISOU 2106  OG  SER B 465    12346  12055  10019   -340   1103   -872       O  
-ATOM   2107  N   GLY B 466      -6.124  -0.454  14.739  1.00103.18           N  
-ANISOU 2107  N   GLY B 466    13699  13581  11923   -328   1044   -745       N  
-ATOM   2108  CA  GLY B 466      -5.931   0.887  14.227  1.00 89.91           C  
-ANISOU 2108  CA  GLY B 466    11759  11995  10409   -311    976   -772       C  
-ATOM   2109  C   GLY B 466      -7.153   1.769  14.369  1.00 87.28           C  
-ANISOU 2109  C   GLY B 466    11253  11729  10182   -496    966   -884       C  
-ATOM   2110  O   GLY B 466      -7.626   2.028  15.476  1.00 93.27           O  
-ANISOU 2110  O   GLY B 466    11950  12553  10934   -579    972   -980       O  
-ATOM   2111  N   SER B 467      -7.666   2.228  13.234  1.00 84.11           N  
-ANISOU 2111  N   SER B 467    10771  11314   9871   -553    949   -875       N  
-ATOM   2112  CA  SER B 467      -8.788   3.157  13.212  1.00 81.81           C  
-ANISOU 2112  CA  SER B 467    10309  11088   9686   -707    929   -982       C  
-ATOM   2113  C   SER B 467     -10.123   2.496  13.550  1.00 96.73           C  
-ANISOU 2113  C   SER B 467    12292  12962  11500   -893    995  -1036       C  
-ATOM   2114  O   SER B 467     -10.793   2.889  14.505  1.00 99.63           O  
-ANISOU 2114  O   SER B 467    12570  13406  11880   -997   1001  -1142       O  
-ATOM   2115  CB  SER B 467      -8.878   3.844  11.848  1.00 66.32           C  
-ANISOU 2115  CB  SER B 467     8251   9117   7831   -693    883   -952       C  
-ATOM   2116  OG  SER B 467     -10.002   4.701  11.783  1.00 64.97           O  
-ANISOU 2116  OG  SER B 467     7943   8998   7747   -828    859  -1061       O  
-ATOM   2117  N   PHE B 468     -10.512   1.501  12.761  1.00132.66           N  
-ANISOU 2117  N   PHE B 468    17020  17418  15968   -941   1046   -970       N  
-ATOM   2118  CA  PHE B 468     -11.811   0.862  12.942  1.00145.66           C  
-ANISOU 2118  CA  PHE B 468    18762  19048  17536  -1135   1109  -1021       C  
-ATOM   2119  C   PHE B 468     -11.761  -0.318  13.905  1.00149.51           C  
-ANISOU 2119  C   PHE B 468    19474  19473  17860  -1161   1175  -1006       C  
-ATOM   2120  O   PHE B 468     -12.719  -1.078  14.014  1.00150.64           O  
-ANISOU 2120  O   PHE B 468    19750  19578  17907  -1320   1235  -1031       O  
-ATOM   2121  CB  PHE B 468     -12.382   0.400  11.600  1.00140.17           C  
-ANISOU 2121  CB  PHE B 468    18147  18285  16829  -1201   1130   -978       C  
-ATOM   2122  CG  PHE B 468     -13.022   1.499  10.796  1.00141.17           C  
-ANISOU 2122  CG  PHE B 468    18066  18487  17085  -1253   1074  -1031       C  
-ATOM   2123  CD1 PHE B 468     -12.874   1.541   9.419  1.00142.10           C  
-ANISOU 2123  CD1 PHE B 468    18184  18566  17241  -1201   1050   -969       C  
-ATOM   2124  CD2 PHE B 468     -13.775   2.481  11.411  1.00141.17           C  
-ANISOU 2124  CD2 PHE B 468    17879  18597  17160  -1345   1043  -1150       C  
-ATOM   2125  CE1 PHE B 468     -13.465   2.541   8.670  1.00143.29           C  
-ANISOU 2125  CE1 PHE B 468    18169  18782  17493  -1235    992  -1020       C  
-ATOM   2126  CE2 PHE B 468     -14.367   3.485  10.668  1.00141.76           C  
-ANISOU 2126  CE2 PHE B 468    17795  18730  17337  -1375    984  -1209       C  
-ATOM   2127  CZ  PHE B 468     -14.207   3.514   9.296  1.00141.90           C  
-ANISOU 2127  CZ  PHE B 468    17832  18703  17381  -1317    957  -1142       C  
-ATOM   2128  N   GLY B 469     -10.645  -0.477  14.602  1.00136.79           N  
-ANISOU 2128  N   GLY B 469    17912  17852  16208  -1006   1161   -969       N  
-ATOM   2129  CA  GLY B 469     -10.510  -1.587  15.522  1.00133.43           C  
-ANISOU 2129  CA  GLY B 469    17716  17362  15619  -1008   1214   -952       C  
-ATOM   2130  C   GLY B 469      -9.378  -2.512  15.136  1.00124.82           C  
-ANISOU 2130  C   GLY B 469    16840  16151  14436   -829   1225   -838       C  
-ATOM   2131  O   GLY B 469      -8.259  -2.067  14.900  1.00123.74           O  
-ANISOU 2131  O   GLY B 469    16621  16040  14356   -648   1174   -789       O  
-ATOM   2132  N   THR B 470      -9.673  -3.802  15.050  1.00108.31           N  
-ANISOU 2132  N   THR B 470    15027  13928  12196   -881   1291   -800       N  
-ATOM   2133  CA  THR B 470      -8.627  -4.802  14.891  1.00 95.22           C  
-ANISOU 2133  CA  THR B 470    13608  12148  10424   -706   1309   -704       C  
-ATOM   2134  C   THR B 470      -8.377  -5.225  13.442  1.00 81.30           C  
-ANISOU 2134  C   THR B 470    11933  10285   8672   -645   1319   -625       C  
-ATOM   2135  O   THR B 470      -9.305  -5.325  12.637  1.00 61.51           O  
-ANISOU 2135  O   THR B 470     9432   7750   6191   -794   1345   -643       O  
-ATOM   2136  CB  THR B 470      -8.905  -6.018  15.785  1.00 85.10           C  
-ANISOU 2136  CB  THR B 470    12612  10769   8955   -767   1374   -708       C  
-ATOM   2137  OG1 THR B 470     -10.183  -6.575  15.457  1.00 85.88           O  
-ANISOU 2137  OG1 THR B 470    12825  10806   9002   -992   1433   -743       O  
-ATOM   2138  CG2 THR B 470      -8.924  -5.575  17.229  1.00 80.33           C  
-ANISOU 2138  CG2 THR B 470    11908  10277   8335   -788   1356   -778       C  
-ATOM   2139  N   VAL B 471      -7.106  -5.461  13.123  1.00 75.11           N  
-ANISOU 2139  N   VAL B 471    11210   9462   7866   -422   1297   -542       N  
-ATOM   2140  CA  VAL B 471      -6.704  -5.872  11.783  1.00 78.39           C  
-ANISOU 2140  CA  VAL B 471    11706   9794   8286   -334   1304   -465       C  
-ATOM   2141  C   VAL B 471      -6.046  -7.251  11.784  1.00 85.99           C  
-ANISOU 2141  C   VAL B 471    12992  10603   9077   -206   1354   -397       C  
-ATOM   2142  O   VAL B 471      -5.164  -7.531  12.595  1.00 87.41           O  
-ANISOU 2142  O   VAL B 471    13253  10782   9178    -53   1345   -371       O  
-ATOM   2143  CB  VAL B 471      -5.758  -4.839  11.125  1.00 73.70           C  
-ANISOU 2143  CB  VAL B 471    10871   9301   7829   -173   1230   -423       C  
-ATOM   2144  CG1 VAL B 471      -6.358  -3.445  11.204  1.00 68.05           C  
-ANISOU 2144  CG1 VAL B 471     9852   8729   7277   -287   1178   -495       C  
-ATOM   2145  CG2 VAL B 471      -4.381  -4.869  11.780  1.00 68.29           C  
-ANISOU 2145  CG2 VAL B 471    10201   8649   7096     53   1198   -376       C  
-ATOM   2146  N   TYR B 472      -6.487  -8.111  10.872  1.00 81.63           N  
-ANISOU 2146  N   TYR B 472    12629   9924   8462   -270   1407   -373       N  
-ATOM   2147  CA  TYR B 472      -5.928  -9.449  10.755  1.00 76.59           C  
-ANISOU 2147  CA  TYR B 472    12319   9124   7659   -154   1460   -315       C  
-ATOM   2148  C   TYR B 472      -5.502  -9.745   9.322  1.00 65.59           C  
-ANISOU 2148  C   TYR B 472    10968   7671   6284    -57   1465   -253       C  
-ATOM   2149  O   TYR B 472      -6.202  -9.394   8.371  1.00 56.26           O  
-ANISOU 2149  O   TYR B 472     9674   6512   5189   -182   1464   -273       O  
-ATOM   2150  CB  TYR B 472      -6.943 -10.502  11.207  1.00 92.28           C  
-ANISOU 2150  CB  TYR B 472    14578  10984   9501   -347   1538   -356       C  
-ATOM   2151  CG  TYR B 472      -7.565 -10.245  12.560  1.00105.52           C  
-ANISOU 2151  CG  TYR B 472    16212  12727  11154   -482   1540   -425       C  
-ATOM   2152  CD1 TYR B 472      -8.774  -9.568  12.674  1.00108.26           C  
-ANISOU 2152  CD1 TYR B 472    16379  13168  11587   -715   1537   -506       C  
-ATOM   2153  CD2 TYR B 472      -6.952 -10.691  13.727  1.00107.98           C  
-ANISOU 2153  CD2 TYR B 472    16662  13016  11349   -373   1544   -413       C  
-ATOM   2154  CE1 TYR B 472      -9.347  -9.338  13.910  1.00113.17           C  
-ANISOU 2154  CE1 TYR B 472    16956  13862  12182   -837   1541   -573       C  
-ATOM   2155  CE2 TYR B 472      -7.525 -10.459  14.964  1.00106.48           C  
-ANISOU 2155  CE2 TYR B 472    16427  12898  11134   -499   1546   -479       C  
-ATOM   2156  CZ  TYR B 472      -8.718  -9.785  15.049  1.00108.99           C  
-ANISOU 2156  CZ  TYR B 472    16562  13310  11539   -731   1546   -560       C  
-ATOM   2157  OH  TYR B 472      -9.286  -9.558  16.286  1.00109.21           O  
-ANISOU 2157  OH  TYR B 472    16538  13419  11536   -854   1549   -629       O  
-ATOM   2158  N   LYS B 473      -4.349 -10.389   9.174  1.00 69.11           N  
-ANISOU 2158  N   LYS B 473    11570   8049   6641    173   1470   -181       N  
-ATOM   2159  CA  LYS B 473      -3.920 -10.896   7.880  1.00 64.48           C  
-ANISOU 2159  CA  LYS B 473    11075   7388   6035    274   1487   -125       C  
-ATOM   2160  C   LYS B 473      -4.894 -11.984   7.459  1.00 61.70           C  
-ANISOU 2160  C   LYS B 473    10994   6876   5573    101   1569   -151       C  
-ATOM   2161  O   LYS B 473      -5.152 -12.914   8.218  1.00 68.47           O  
-ANISOU 2161  O   LYS B 473    12119   7614   6281     53   1623   -167       O  
-ATOM   2162  CB  LYS B 473      -2.508 -11.469   7.982  1.00 54.58           C  
-ANISOU 2162  CB  LYS B 473     9962   6095   4683    561   1482    -50       C  
-ATOM   2163  CG  LYS B 473      -1.944 -12.003   6.675  1.00 50.65           C  
-ANISOU 2163  CG  LYS B 473     9557   5532   4156    693   1500      9       C  
-ATOM   2164  CD  LYS B 473      -0.489 -12.404   6.852  1.00 47.84           C  
-ANISOU 2164  CD  LYS B 473     9293   5174   3711    993   1484     79       C  
-ATOM   2165  CE  LYS B 473       0.143 -12.823   5.538  1.00 47.47           C  
-ANISOU 2165  CE  LYS B 473     9302   5092   3645   1140   1496    136       C  
-ATOM   2166  NZ  LYS B 473       1.609 -13.042   5.693  1.00 52.14           N  
-ANISOU 2166  NZ  LYS B 473     9929   5721   4162   1444   1471    202       N  
-ATOM   2167  N   GLY B 474      -5.441 -11.867   6.255  1.00 57.92           N  
-ANISOU 2167  N   GLY B 474    10448   6398   5160      1   1578   -159       N  
-ATOM   2168  CA  GLY B 474      -6.418 -12.827   5.778  1.00 41.64           C  
-ANISOU 2168  CA  GLY B 474     8621   4202   2998   -185   1653   -193       C  
-ATOM   2169  C   GLY B 474      -6.052 -13.490   4.465  1.00 53.18           C  
-ANISOU 2169  C   GLY B 474    10212   5579   4416    -99   1683   -149       C  
-ATOM   2170  O   GLY B 474      -4.931 -13.356   3.971  1.00 55.77           O  
-ANISOU 2170  O   GLY B 474    10484   5937   4769    132   1651    -84       O  
-ATOM   2171  N   LYS B 475      -7.013 -14.216   3.903  1.00 59.06           N  
-ANISOU 2171  N   LYS B 475    11129   6225   5088   -291   1747   -187       N  
-ATOM   2172  CA  LYS B 475      -6.841 -14.872   2.616  1.00 52.82           C  
-ANISOU 2172  CA  LYS B 475    10464   5355   4249   -247   1783   -160       C  
-ATOM   2173  C   LYS B 475      -8.049 -14.612   1.727  1.00 56.47           C  
-ANISOU 2173  C   LYS B 475    10813   5868   4776   -491   1796   -217       C  
-ATOM   2174  O   LYS B 475      -9.183 -14.907   2.101  1.00 70.00           O  
-ANISOU 2174  O   LYS B 475    12615   7546   6438   -733   1838   -283       O  
-ATOM   2175  CB  LYS B 475      -6.645 -16.377   2.798  1.00 63.19           C  
-ANISOU 2175  CB  LYS B 475    12203   6457   5349   -208   1865   -144       C  
-ATOM   2176  CG  LYS B 475      -5.258 -16.776   3.268  1.00 67.07           C  
-ANISOU 2176  CG  LYS B 475    12828   6895   5759     92   1854    -74       C  
-ATOM   2177  CD  LYS B 475      -4.203 -16.388   2.245  1.00 66.50           C  
-ANISOU 2177  CD  LYS B 475    12598   6904   5764    321   1810    -11       C  
-ATOM   2178  CE  LYS B 475      -3.148 -17.473   2.106  1.00 63.32           C  
-ANISOU 2178  CE  LYS B 475    12493   6367   5199    565   1848     47       C  
-ATOM   2179  NZ  LYS B 475      -2.024 -17.049   1.224  1.00 57.36           N  
-ANISOU 2179  NZ  LYS B 475    11565   5715   4514    806   1799    111       N  
-ATOM   2180  N   TRP B 476      -7.794 -14.055   0.549  1.00 50.73           N  
-ANISOU 2180  N   TRP B 476     9885   5234   4156   -427   1758   -192       N  
-ATOM   2181  CA  TRP B 476      -8.847 -13.775  -0.416  1.00 51.02           C  
-ANISOU 2181  CA  TRP B 476     9797   5335   4252   -631   1763   -241       C  
-ATOM   2182  C   TRP B 476      -8.230 -13.596  -1.798  1.00 60.34           C  
-ANISOU 2182  C   TRP B 476    10868   6569   5491   -494   1740   -191       C  
-ATOM   2183  O   TRP B 476      -7.826 -12.493  -2.171  1.00 57.41           O  
-ANISOU 2183  O   TRP B 476    10195   6348   5268   -400   1665   -162       O  
-ATOM   2184  CB  TRP B 476      -9.621 -12.523  -0.008  1.00 54.72           C  
-ANISOU 2184  CB  TRP B 476     9953   5968   4870   -772   1704   -293       C  
-ATOM   2185  CG  TRP B 476     -10.840 -12.272  -0.838  1.00 63.05           C  
-ANISOU 2185  CG  TRP B 476    10894   7095   5968   -998   1710   -356       C  
-ATOM   2186  CD1 TRP B 476     -12.007 -12.980  -0.816  1.00 62.57           C  
-ANISOU 2186  CD1 TRP B 476    10999   6972   5803  -1245   1775   -425       C  
-ATOM   2187  CD2 TRP B 476     -11.020 -11.232  -1.806  1.00 62.57           C  
-ANISOU 2187  CD2 TRP B 476    10527   7193   6054   -999   1646   -356       C  
-ATOM   2188  NE1 TRP B 476     -12.899 -12.450  -1.714  1.00 61.95           N  
-ANISOU 2188  NE1 TRP B 476    10729   7012   5797  -1395   1754   -471       N  
-ATOM   2189  CE2 TRP B 476     -12.318 -11.375  -2.335  1.00 64.60           C  
-ANISOU 2189  CE2 TRP B 476    10777   7482   6287  -1243   1674   -429       C  
-ATOM   2190  CE3 TRP B 476     -10.208 -10.196  -2.279  1.00 51.57           C  
-ANISOU 2190  CE3 TRP B 476     8870   5923   4803   -819   1567   -301       C  
-ATOM   2191  CZ2 TRP B 476     -12.824 -10.521  -3.313  1.00 63.80           C  
-ANISOU 2191  CZ2 TRP B 476    10415   7531   6295  -1299   1622   -448       C  
-ATOM   2192  CZ3 TRP B 476     -10.711  -9.349  -3.249  1.00 45.96           C  
-ANISOU 2192  CZ3 TRP B 476     7909   5350   4202   -880   1518   -316       C  
-ATOM   2193  CH2 TRP B 476     -12.007  -9.516  -3.756  1.00 54.36           C  
-ANISOU 2193  CH2 TRP B 476     8973   6443   5236  -1112   1544   -389       C  
-ATOM   2194  N   HIS B 477      -8.158 -14.690  -2.549  1.00 73.04           N  
-ANISOU 2194  N   HIS B 477    12728   8053   6971   -486   1805   -180       N  
-ATOM   2195  CA  HIS B 477      -7.469 -14.702  -3.833  1.00 66.77           C  
-ANISOU 2195  CA  HIS B 477    11872   7297   6202   -338   1792   -127       C  
-ATOM   2196  C   HIS B 477      -6.007 -14.327  -3.620  1.00 72.63           C  
-ANISOU 2196  C   HIS B 477    12528   8083   6986    -38   1740    -46       C  
-ATOM   2197  O   HIS B 477      -5.393 -13.664  -4.457  1.00 74.28           O  
-ANISOU 2197  O   HIS B 477    12516   8414   7295     90   1688      0       O  
-ATOM   2198  CB  HIS B 477      -8.135 -13.741  -4.820  1.00 40.56           C  
-ANISOU 2198  CB  HIS B 477     8242   4144   3024   -456   1744   -152       C  
-ATOM   2199  CG  HIS B 477      -9.624 -13.874  -4.880  1.00 50.43           C  
-ANISOU 2199  CG  HIS B 477     9514   5397   4252   -756   1779   -239       C  
-ATOM   2200  ND1 HIS B 477     -10.253 -14.981  -5.409  1.00 57.18           N  
-ANISOU 2200  ND1 HIS B 477    10624   6137   4965   -903   1861   -276       N  
-ATOM   2201  CD2 HIS B 477     -10.612 -13.036  -4.483  1.00 57.09           C  
-ANISOU 2201  CD2 HIS B 477    10154   6351   5186   -937   1744   -300       C  
-ATOM   2202  CE1 HIS B 477     -11.562 -14.821  -5.331  1.00 57.00           C  
-ANISOU 2202  CE1 HIS B 477    10548   6162   4948  -1167   1874   -356       C  
-ATOM   2203  NE2 HIS B 477     -11.806 -13.648  -4.774  1.00 58.18           N  
-ANISOU 2203  NE2 HIS B 477    10418   6450   5237  -1186   1802   -372       N  
-ATOM   2204  N   GLY B 478      -5.459 -14.761  -2.489  1.00 49.24           N  
-ANISOU 2204  N   GLY B 478     9740   5029   3939     68   1754    -29       N  
-ATOM   2205  CA  GLY B 478      -4.095 -14.437  -2.115  1.00 43.49           C  
-ANISOU 2205  CA  GLY B 478     8940   4351   3234    345   1705     40       C  
-ATOM   2206  C   GLY B 478      -4.045 -13.770  -0.753  1.00 46.79           C  
-ANISOU 2206  C   GLY B 478     9248   4823   3706    343   1663     27       C  
-ATOM   2207  O   GLY B 478      -5.033 -13.772  -0.020  1.00 52.79           O  
-ANISOU 2207  O   GLY B 478    10048   5554   4457    139   1683    -34       O  
-ATOM   2208  N   ASP B 479      -2.897 -13.197  -0.413  1.00 49.56           N  
-ANISOU 2208  N   ASP B 479     9456   5266   4108    566   1605     83       N  
-ATOM   2209  CA  ASP B 479      -2.737 -12.513   0.865  1.00 61.73           C  
-ANISOU 2209  CA  ASP B 479    10878   6877   5702    581   1560     72       C  
-ATOM   2210  C   ASP B 479      -3.505 -11.195   0.900  1.00 67.46           C  
-ANISOU 2210  C   ASP B 479    11276   7751   6603    412   1504     29       C  
-ATOM   2211  O   ASP B 479      -3.502 -10.441  -0.071  1.00 63.71           O  
-ANISOU 2211  O   ASP B 479    10573   7386   6247    411   1462     45       O  
-ATOM   2212  CB  ASP B 479      -1.256 -12.263   1.155  1.00 71.23           C  
-ANISOU 2212  CB  ASP B 479    12012   8150   6901    868   1513    141       C  
-ATOM   2213  CG  ASP B 479      -0.519 -13.525   1.547  1.00 78.64           C  
-ANISOU 2213  CG  ASP B 479    13286   8943   7649   1044   1564    174       C  
-ATOM   2214  OD1 ASP B 479      -1.188 -14.499   1.947  1.00 82.43           O  
-ANISOU 2214  OD1 ASP B 479    14054   9263   8002    929   1632    138       O  
-ATOM   2215  OD2 ASP B 479       0.727 -13.540   1.461  1.00 83.10           O  
-ANISOU 2215  OD2 ASP B 479    13830   9557   8185   1298   1536    234       O  
-ATOM   2216  N   VAL B 480      -4.167 -10.926   2.023  1.00 81.81           N  
-ANISOU 2216  N   VAL B 480    13077   9575   8430    274   1502    -26       N  
-ATOM   2217  CA  VAL B 480      -4.868  -9.662   2.219  1.00 69.49           C  
-ANISOU 2217  CA  VAL B 480    11219   8158   7028    129   1448    -72       C  
-ATOM   2218  C   VAL B 480      -4.733  -9.192   3.664  1.00 65.79           C  
-ANISOU 2218  C   VAL B 480    10690   7737   6571    136   1420    -96       C  
-ATOM   2219  O   VAL B 480      -4.407  -9.978   4.550  1.00 73.91           O  
-ANISOU 2219  O   VAL B 480    11938   8673   7472    197   1454    -91       O  
-ATOM   2220  CB  VAL B 480      -6.368  -9.766   1.865  1.00 55.90           C  
-ANISOU 2220  CB  VAL B 480     9511   6414   5315   -146   1484   -147       C  
-ATOM   2221  CG1 VAL B 480      -6.548 -10.237   0.431  1.00 48.55           C  
-ANISOU 2221  CG1 VAL B 480     8635   5445   4365   -166   1512   -130       C  
-ATOM   2222  CG2 VAL B 480      -7.087 -10.697   2.834  1.00 54.72           C  
-ANISOU 2222  CG2 VAL B 480     9625   6139   5026   -292   1551   -198       C  
-ATOM   2223  N   ALA B 481      -4.976  -7.906   3.890  1.00 54.58           N  
-ANISOU 2223  N   ALA B 481     8975   6463   5299     78   1356   -125       N  
-ATOM   2224  CA  ALA B 481      -5.005  -7.353   5.239  1.00 46.41           C  
-ANISOU 2224  CA  ALA B 481     7856   5492   4288     53   1330   -164       C  
-ATOM   2225  C   ALA B 481      -6.399  -6.809   5.521  1.00 49.48           C  
-ANISOU 2225  C   ALA B 481     8129   5930   4743   -200   1332   -252       C  
-ATOM   2226  O   ALA B 481      -6.938  -6.029   4.737  1.00 53.39           O  
-ANISOU 2226  O   ALA B 481     8427   6506   5354   -285   1299   -272       O  
-ATOM   2227  CB  ALA B 481      -3.959  -6.266   5.398  1.00 56.10           C  
-ANISOU 2227  CB  ALA B 481     8837   6857   5621    220   1251   -125       C  
-ATOM   2228  N   VAL B 482      -6.983  -7.225   6.640  1.00 57.97           N  
-ANISOU 2228  N   VAL B 482     9327   6962   5736   -315   1369   -306       N  
-ATOM   2229  CA  VAL B 482      -8.357  -6.855   6.960  1.00 67.90           C  
-ANISOU 2229  CA  VAL B 482    10501   8266   7030   -561   1380   -395       C  
-ATOM   2230  C   VAL B 482      -8.433  -5.949   8.184  1.00 77.97           C  
-ANISOU 2230  C   VAL B 482    11598   9658   8370   -587   1340   -447       C  
-ATOM   2231  O   VAL B 482      -7.751  -6.178   9.179  1.00 82.64           O  
-ANISOU 2231  O   VAL B 482    12265  10237   8897   -482   1339   -433       O  
-ATOM   2232  CB  VAL B 482      -9.225  -8.103   7.214  1.00 62.75           C  
-ANISOU 2232  CB  VAL B 482    10139   7481   6222   -726   1465   -429       C  
-ATOM   2233  CG1 VAL B 482     -10.691  -7.717   7.323  1.00 65.85           C  
-ANISOU 2233  CG1 VAL B 482    10426   7942   6654   -988   1477   -520       C  
-ATOM   2234  CG2 VAL B 482      -9.026  -9.128   6.109  1.00 51.43           C  
-ANISOU 2234  CG2 VAL B 482     8921   5916   4702   -684   1512   -380       C  
-ATOM   2235  N   LYS B 483      -9.266  -4.917   8.100  1.00 78.16           N  
-ANISOU 2235  N   LYS B 483    11385   9798   8516   -722   1305   -512       N  
-ATOM   2236  CA  LYS B 483      -9.559  -4.059   9.242  1.00 81.05           C  
-ANISOU 2236  CA  LYS B 483    11580  10274   8940   -781   1274   -583       C  
-ATOM   2237  C   LYS B 483     -11.014  -4.258   9.639  1.00 79.25           C  
-ANISOU 2237  C   LYS B 483    11382  10057   8672  -1029   1318   -672       C  
-ATOM   2238  O   LYS B 483     -11.919  -3.888   8.891  1.00 79.37           O  
-ANISOU 2238  O   LYS B 483    11294  10116   8748  -1160   1313   -712       O  
-ATOM   2239  CB  LYS B 483      -9.318  -2.591   8.887  1.00 90.38           C  
-ANISOU 2239  CB  LYS B 483    12453  11591  10295   -728   1193   -597       C  
-ATOM   2240  CG  LYS B 483      -9.971  -1.610   9.851  1.00 96.98           C  
-ANISOU 2240  CG  LYS B 483    13094  12546  11207   -838   1164   -697       C  
-ATOM   2241  CD  LYS B 483     -10.072  -0.210   9.255  1.00102.65           C  
-ANISOU 2241  CD  LYS B 483    13538  13372  12091   -830   1090   -726       C  
-ATOM   2242  CE  LYS B 483      -8.722   0.490   9.195  1.00 99.54           C  
-ANISOU 2242  CE  LYS B 483    13029  13020  11771   -630   1027   -670       C  
-ATOM   2243  NZ  LYS B 483      -8.856   1.891   8.702  1.00 94.13           N  
-ANISOU 2243  NZ  LYS B 483    12101  12427  11238   -635    952   -708       N  
-ATOM   2244  N   MET B 484     -11.241  -4.837  10.814  1.00 63.04           N  
-ANISOU 2244  N   MET B 484     9468   7976   6510  -1093   1360   -705       N  
-ATOM   2245  CA  MET B 484     -12.595  -5.188  11.234  1.00 67.56           C  
-ANISOU 2245  CA  MET B 484    10099   8555   7015  -1335   1410   -785       C  
-ATOM   2246  C   MET B 484     -13.042  -4.516  12.532  1.00 74.36           C  
-ANISOU 2246  C   MET B 484    10813   9538   7902  -1416   1396   -869       C  
-ATOM   2247  O   MET B 484     -12.388  -4.627  13.570  1.00 73.98           O  
-ANISOU 2247  O   MET B 484    10811   9492   7804  -1324   1392   -863       O  
-ATOM   2248  CB  MET B 484     -12.735  -6.706  11.351  1.00 83.97           C  
-ANISOU 2248  CB  MET B 484    12525  10473   8908  -1392   1490   -756       C  
-ATOM   2249  CG  MET B 484     -11.421  -7.455  11.208  1.00 89.76           C  
-ANISOU 2249  CG  MET B 484    13458  11082   9565  -1168   1496   -660       C  
-ATOM   2250  SD  MET B 484     -11.641  -9.232  11.388  1.00192.94           S  
-ANISOU 2250  SD  MET B 484    26959  23947  22404  -1239   1591   -636       S  
-ATOM   2251  CE  MET B 484     -13.003  -9.490  10.257  1.00 57.21           C  
-ANISOU 2251  CE  MET B 484     9785   6738   5214  -1486   1633   -683       C  
-ATOM   2252  N   LEU B 485     -14.173  -3.825  12.457  1.00103.00           N  
-ANISOU 2252  N   LEU B 485    14261  13274  11601  -1587   1388   -954       N  
-ATOM   2253  CA  LEU B 485     -14.763  -3.177  13.615  1.00105.18           C  
-ANISOU 2253  CA  LEU B 485    14385  13677  11900  -1685   1381  -1049       C  
-ATOM   2254  C   LEU B 485     -15.645  -4.164  14.372  1.00105.05           C  
-ANISOU 2254  C   LEU B 485    14564  13625  11724  -1872   1456  -1089       C  
-ATOM   2255  O   LEU B 485     -16.775  -4.437  13.965  1.00105.69           O  
-ANISOU 2255  O   LEU B 485    14671  13719  11768  -2064   1492  -1133       O  
-ATOM   2256  CB  LEU B 485     -15.590  -1.975  13.165  1.00 83.01           C  
-ANISOU 2256  CB  LEU B 485    11299  11006   9236  -1773   1336  -1128       C  
-ATOM   2257  CG  LEU B 485     -16.344  -1.206  14.244  1.00 80.34           C  
-ANISOU 2257  CG  LEU B 485    10777  10814   8934  -1883   1328  -1243       C  
-ATOM   2258  CD1 LEU B 485     -15.420  -0.210  14.924  1.00 81.35           C  
-ANISOU 2258  CD1 LEU B 485    10727  11015   9166  -1722   1267  -1260       C  
-ATOM   2259  CD2 LEU B 485     -17.540  -0.500  13.631  1.00 74.85           C  
-ANISOU 2259  CD2 LEU B 485     9904  10221   8316  -2027   1311  -1324       C  
-ATOM   2260  N   ASN B 486     -15.123  -4.700  15.471  1.00 86.64           N  
-ANISOU 2260  N   ASN B 486    12374  11257   9290  -1818   1476  -1076       N  
-ATOM   2261  CA  ASN B 486     -15.851  -5.694  16.254  1.00 81.34           C  
-ANISOU 2261  CA  ASN B 486    11915  10542   8449  -1986   1545  -1107       C  
-ATOM   2262  C   ASN B 486     -16.802  -5.095  17.290  1.00 69.11           C  
-ANISOU 2262  C   ASN B 486    10195   9153   6910  -2146   1549  -1218       C  
-ATOM   2263  O   ASN B 486     -16.658  -5.335  18.488  1.00 61.88           O  
-ANISOU 2263  O   ASN B 486     9340   8262   5910  -2148   1563  -1242       O  
-ATOM   2264  CB  ASN B 486     -14.881  -6.675  16.923  1.00 84.60           C  
-ANISOU 2264  CB  ASN B 486    12594  10829   8722  -1854   1568  -1039       C  
-ATOM   2265  CG  ASN B 486     -13.847  -5.979  17.785  1.00 88.56           C  
-ANISOU 2265  CG  ASN B 486    12957  11410   9283  -1665   1511  -1037       C  
-ATOM   2266  OD1 ASN B 486     -12.814  -5.524  17.293  1.00 94.39           O  
-ANISOU 2266  OD1 ASN B 486    13611  12143  10112  -1467   1461   -982       O  
-ATOM   2267  ND2 ASN B 486     -14.118  -5.896  19.082  1.00 88.69           N  
-ANISOU 2267  ND2 ASN B 486    12946  11510   9241  -1729   1519  -1102       N  
-ATOM   2268  N   VAL B 487     -17.775  -4.318  16.824  1.00 76.42           N  
-ANISOU 2268  N   VAL B 487    10906  10196   7933  -2275   1536  -1289       N  
-ATOM   2269  CA  VAL B 487     -18.808  -3.783  17.705  1.00 77.24           C  
-ANISOU 2269  CA  VAL B 487    10846  10461   8039  -2439   1547  -1402       C  
-ATOM   2270  C   VAL B 487     -20.169  -4.398  17.365  1.00 88.47           C  
-ANISOU 2270  C   VAL B 487    12356  11894   9365  -2692   1607  -1446       C  
-ATOM   2271  O   VAL B 487     -20.589  -4.388  16.208  1.00102.02           O  
-ANISOU 2271  O   VAL B 487    14054  13588  11121  -2742   1604  -1435       O  
-ATOM   2272  CB  VAL B 487     -18.870  -2.237  17.645  1.00 65.26           C  
-ANISOU 2272  CB  VAL B 487     8980   9103   6714  -2379   1479  -1473       C  
-ATOM   2273  CG1 VAL B 487     -17.507  -1.638  17.970  1.00 66.00           C  
-ANISOU 2273  CG1 VAL B 487     8991   9189   6896  -2143   1419  -1435       C  
-ATOM   2274  CG2 VAL B 487     -19.355  -1.761  16.285  1.00 58.64           C  
-ANISOU 2274  CG2 VAL B 487     8027   8276   5976  -2410   1452  -1473       C  
-ATOM   2275  N   THR B 488     -20.845  -4.947  18.372  1.00 87.67           N  
-ANISOU 2275  N   THR B 488    12351  11832   9128  -2853   1658  -1498       N  
-ATOM   2276  CA  THR B 488     -22.112  -5.651  18.157  1.00 84.73           C  
-ANISOU 2276  CA  THR B 488    12089  11470   8636  -3110   1721  -1540       C  
-ATOM   2277  C   THR B 488     -23.044  -4.881  17.228  1.00 92.97           C  
-ANISOU 2277  C   THR B 488    12905  12633   9786  -3207   1699  -1600       C  
-ATOM   2278  O   THR B 488     -23.474  -5.400  16.198  1.00100.02           O  
-ANISOU 2278  O   THR B 488    13900  13461  10643  -3296   1721  -1578       O  
-ATOM   2279  CB  THR B 488     -22.839  -5.956  19.486  1.00 73.23           C  
-ANISOU 2279  CB  THR B 488    10666  10108   7049  -3279   1766  -1615       C  
-ATOM   2280  OG1 THR B 488     -22.013  -6.792  20.305  1.00 73.95           O  
-ANISOU 2280  OG1 THR B 488    11002  10077   7019  -3196   1785  -1557       O  
-ATOM   2281  CG2 THR B 488     -24.161  -6.664  19.223  1.00 65.22           C  
-ANISOU 2281  CG2 THR B 488     9758   9117   5906  -3557   1830  -1661       C  
-ATOM   2282  N   ALA B 489     -23.345  -3.640  17.597  1.00 81.34           N  
-ANISOU 2282  N   ALA B 489    11128  11336   8440  -3184   1655  -1682       N  
-ATOM   2283  CA  ALA B 489     -24.182  -2.772  16.778  1.00 86.08           C  
-ANISOU 2283  CA  ALA B 489    11496  12063   9149  -3248   1621  -1747       C  
-ATOM   2284  C   ALA B 489     -23.523  -1.410  16.603  1.00 79.38           C  
-ANISOU 2284  C   ALA B 489    10387  11277   8497  -3048   1537  -1761       C  
-ATOM   2285  O   ALA B 489     -23.460  -0.621  17.546  1.00 70.93           O  
-ANISOU 2285  O   ALA B 489     9143  10320   7487  -3004   1516  -1829       O  
-ATOM   2286  CB  ALA B 489     -25.556  -2.619  17.401  1.00129.83           C  
-ANISOU 2286  CB  ALA B 489    16922  17783  14625  -3471   1657  -1864       C  
-ATOM   2287  N   PRO B 490     -23.027  -1.132  15.390  1.00 81.67           N  
-ANISOU 2287  N   PRO B 490    10656  11492   8882  -2929   1489  -1702       N  
-ATOM   2288  CA  PRO B 490     -22.310   0.111  15.084  1.00 77.72           C  
-ANISOU 2288  CA  PRO B 490     9943  11026   8561  -2736   1403  -1706       C  
-ATOM   2289  C   PRO B 490     -23.155   1.368  15.261  1.00 76.64           C  
-ANISOU 2289  C   PRO B 490     9569  11084   8465  -2688   1376  -1818       C  
-ATOM   2290  O   PRO B 490     -24.276   1.446  14.755  1.00 72.20           O  
-ANISOU 2290  O   PRO B 490     8976  10615   7843  -2773   1395  -1867       O  
-ATOM   2291  CB  PRO B 490     -21.938  -0.056  13.608  1.00105.73           C  
-ANISOU 2291  CB  PRO B 490    13558  14468  12147  -2659   1373  -1626       C  
-ATOM   2292  CG  PRO B 490     -21.930  -1.522  13.382  1.00107.55           C  
-ANISOU 2292  CG  PRO B 490    14081  14562  12221  -2742   1448  -1551       C  
-ATOM   2293  CD  PRO B 490     -23.027  -2.060  14.247  1.00108.20           C  
-ANISOU 2293  CD  PRO B 490    14218  14719  12173  -2965   1515  -1625       C  
-ATOM   2294  N   THR B 491     -22.605   2.348  15.969  1.00 80.73           N  
-ANISOU 2294  N   THR B 491     9932  11661   9082  -2547   1334  -1861       N  
-ATOM   2295  CA  THR B 491     -23.261   3.635  16.145  1.00 84.57           C  
-ANISOU 2295  CA  THR B 491    10213  12297   9621  -2468   1307  -1971       C  
-ATOM   2296  C   THR B 491     -23.258   4.386  14.819  1.00 90.69           C  
-ANISOU 2296  C   THR B 491    10932  13053  10474  -2335   1254  -1947       C  
-ATOM   2297  O   THR B 491     -22.512   4.027  13.907  1.00 87.34           O  
-ANISOU 2297  O   THR B 491    10597  12507  10082  -2273   1226  -1845       O  
-ATOM   2298  CB  THR B 491     -22.532   4.491  17.203  1.00 81.21           C  
-ANISOU 2298  CB  THR B 491     9658  11910   9289  -2341   1274  -2027       C  
-ATOM   2299  OG1 THR B 491     -21.257   4.902  16.694  1.00 67.06           O  
-ANISOU 2299  OG1 THR B 491     7859  10010   7612  -2162   1210  -1953       O  
-ATOM   2300  CG2 THR B 491     -22.334   3.706  18.494  1.00 89.39           C  
-ANISOU 2300  CG2 THR B 491    10756  12955  10252  -2460   1320  -2035       C  
-ATOM   2301  N   PRO B 492     -24.098   5.426  14.701  1.00115.99           N  
-ANISOU 2301  N   PRO B 492    13991  16376  13704  -2293   1240  -2042       N  
-ATOM   2302  CA  PRO B 492     -24.111   6.250  13.488  1.00111.63           C  
-ANISOU 2302  CA  PRO B 492    13384  15803  13226  -2164   1188  -2025       C  
-ATOM   2303  C   PRO B 492     -22.733   6.842  13.195  1.00108.69           C  
-ANISOU 2303  C   PRO B 492    12998  15315  12986  -1971   1122  -1962       C  
-ATOM   2304  O   PRO B 492     -22.425   7.137  12.041  1.00115.95           O  
-ANISOU 2304  O   PRO B 492    13930  16170  13954  -1880   1080  -1901       O  
-ATOM   2305  CB  PRO B 492     -25.105   7.361  13.833  1.00 87.43           C  
-ANISOU 2305  CB  PRO B 492    10164  12877  10180  -2144   1189  -2159       C  
-ATOM   2306  CG  PRO B 492     -26.003   6.760  14.856  1.00 87.44           C  
-ANISOU 2306  CG  PRO B 492    10163  12996  10065  -2323   1254  -2234       C  
-ATOM   2307  CD  PRO B 492     -25.136   5.838  15.663  1.00 91.50           C  
-ANISOU 2307  CD  PRO B 492    10780  13431  10554  -2375   1276  -2174       C  
-ATOM   2308  N   GLN B 493     -21.917   7.003  14.232  1.00 74.71           N  
-ANISOU 2308  N   GLN B 493     8663  10991   8732  -1918   1114  -1978       N  
-ATOM   2309  CA  GLN B 493     -20.584   7.581  14.079  1.00 74.75           C  
-ANISOU 2309  CA  GLN B 493     8646  10900   8856  -1748   1052  -1930       C  
-ATOM   2310  C   GLN B 493     -19.619   6.631  13.369  1.00 79.39           C  
-ANISOU 2310  C   GLN B 493     9369  11363   9432  -1737   1037  -1790       C  
-ATOM   2311  O   GLN B 493     -18.990   7.001  12.376  1.00 87.74           O  
-ANISOU 2311  O   GLN B 493    10433  12348  10557  -1622    986  -1726       O  
-ATOM   2312  CB  GLN B 493     -20.016   8.003  15.438  1.00 95.62           C  
-ANISOU 2312  CB  GLN B 493    11210  13574  11546  -1705   1047  -1999       C  
-ATOM   2313  CG  GLN B 493     -20.925   8.939  16.220  1.00100.63           C  
-ANISOU 2313  CG  GLN B 493    11710  14328  12198  -1713   1064  -2152       C  
-ATOM   2314  CD  GLN B 493     -20.182   9.731  17.279  1.00104.18           C  
-ANISOU 2314  CD  GLN B 493    12059  14786  12738  -1616   1036  -2230       C  
-ATOM   2315  OE1 GLN B 493     -19.299   9.209  17.961  1.00 96.14           O  
-ANISOU 2315  OE1 GLN B 493    11073  13745  11711  -1616   1031  -2191       O  
-ATOM   2316  NE2 GLN B 493     -20.540  11.003  17.422  1.00111.38           N  
-ANISOU 2316  NE2 GLN B 493    12851  15727  13740  -1537   1018  -2348       N  
-ATOM   2317  N   GLN B 494     -19.504   5.409  13.881  1.00 86.63           N  
-ANISOU 2317  N   GLN B 494    10402  12250  10265  -1861   1083  -1747       N  
-ATOM   2318  CA  GLN B 494     -18.639   4.401  13.276  1.00 79.97           C  
-ANISOU 2318  CA  GLN B 494     9707  11272   9405  -1867   1081  -1625       C  
-ATOM   2319  C   GLN B 494     -19.096   4.096  11.855  1.00 70.82           C  
-ANISOU 2319  C   GLN B 494     8616  10074   8218  -1889   1079  -1572       C  
-ATOM   2320  O   GLN B 494     -18.302   3.695  11.007  1.00 59.57           O  
-ANISOU 2320  O   GLN B 494     7272   8541   6819  -1832   1053  -1479       O  
-ATOM   2321  CB  GLN B 494     -18.657   3.120  14.110  1.00 76.78           C  
-ANISOU 2321  CB  GLN B 494     9447  10823   8902  -2026   1148  -1602       C  
-ATOM   2322  CG  GLN B 494     -18.526   3.347  15.604  1.00 75.87           C  
-ANISOU 2322  CG  GLN B 494     9258  10783   8785  -2043   1162  -1672       C  
-ATOM   2323  CD  GLN B 494     -18.858   2.108  16.412  1.00 73.88           C  
-ANISOU 2323  CD  GLN B 494     9199  10509   8365  -2160   1252  -1649       C  
-ATOM   2324  OE1 GLN B 494     -17.967   1.416  16.901  1.00 71.97           O  
-ANISOU 2324  OE1 GLN B 494     9113  10185   8048  -2072   1275  -1577       O  
-ATOM   2325  NE2 GLN B 494     -20.144   1.819  16.548  1.00 72.85           N  
-ANISOU 2325  NE2 GLN B 494     9069  10450   8163  -2357   1299  -1717       N  
-ATOM   2326  N   LEU B 495     -20.387   4.293  11.609  1.00 79.81           N  
-ANISOU 2326  N   LEU B 495     9714  11309   9300  -1975   1106  -1639       N  
-ATOM   2327  CA  LEU B 495     -20.977   4.048  10.300  1.00 71.19           C  
-ANISOU 2327  CA  LEU B 495     8668  10210   8169  -2010   1104  -1606       C  
-ATOM   2328  C   LEU B 495     -20.477   5.055   9.269  1.00 73.65           C  
-ANISOU 2328  C   LEU B 495     8898  10503   8584  -1833   1030  -1575       C  
-ATOM   2329  O   LEU B 495     -19.969   4.676   8.215  1.00 80.63           O  
-ANISOU 2329  O   LEU B 495     9852  11306   9478  -1794   1004  -1491       O  
-ATOM   2330  CB  LEU B 495     -22.501   4.120  10.395  1.00 47.34           C  
-ANISOU 2330  CB  LEU B 495     5602   7324   5060  -2145   1148  -1697       C  
-ATOM   2331  CG  LEU B 495     -23.291   3.760   9.138  1.00 57.28           C  
-ANISOU 2331  CG  LEU B 495     6906   8603   6254  -2217   1155  -1678       C  
-ATOM   2332  CD1 LEU B 495     -23.369   2.250   8.977  1.00 52.73           C  
-ANISOU 2332  CD1 LEU B 495     6522   7943   5571  -2385   1213  -1627       C  
-ATOM   2333  CD2 LEU B 495     -24.683   4.365   9.203  1.00 66.10           C  
-ANISOU 2333  CD2 LEU B 495     7911   9884   7321  -2286   1172  -1781       C  
-ATOM   2334  N   GLN B 496     -20.630   6.340   9.579  1.00 65.72           N  
-ANISOU 2334  N   GLN B 496     7753   9564   7653  -1732    998  -1648       N  
-ATOM   2335  CA  GLN B 496     -20.196   7.409   8.682  1.00 71.15           C  
-ANISOU 2335  CA  GLN B 496     8376  10221   8439  -1574    933  -1628       C  
-ATOM   2336  C   GLN B 496     -18.683   7.418   8.517  1.00 65.09           C  
-ANISOU 2336  C   GLN B 496     7641   9341   7750  -1450    884  -1542       C  
-ATOM   2337  O   GLN B 496     -18.168   7.751   7.450  1.00 68.22           O  
-ANISOU 2337  O   GLN B 496     8046   9682   8193  -1355    835  -1480       O  
-ATOM   2338  CB  GLN B 496     -20.680   8.770   9.188  1.00 88.86           C  
-ANISOU 2338  CB  GLN B 496    10484  12530  10749  -1507    922  -1740       C  
-ATOM   2339  CG  GLN B 496     -22.157   9.039   8.936  1.00101.03           C  
-ANISOU 2339  CG  GLN B 496    11973  14186  12228  -1592    951  -1820       C  
-ATOM   2340  CD  GLN B 496     -22.457   9.357   7.481  1.00 96.34           C  
-ANISOU 2340  CD  GLN B 496    11385  13583  11636  -1549    918  -1776       C  
-ATOM   2341  OE1 GLN B 496     -23.495   8.962   6.948  1.00 85.87           O  
-ANISOU 2341  OE1 GLN B 496    10070  12341  10218  -1653    941  -1789       O  
-ATOM   2342  NE2 GLN B 496     -21.547  10.075   6.832  1.00 94.61           N  
-ANISOU 2342  NE2 GLN B 496    11159  13270  11518  -1404    862  -1726       N  
-ATOM   2343  N   ALA B 497     -17.975   7.060   9.582  1.00 55.19           N  
-ANISOU 2343  N   ALA B 497     6402   8063   6504  -1456    895  -1541       N  
-ATOM   2344  CA  ALA B 497     -16.527   6.927   9.519  1.00 57.00           C  
-ANISOU 2344  CA  ALA B 497     6665   8201   6793  -1355    851  -1461       C  
-ATOM   2345  C   ALA B 497     -16.164   5.826   8.532  1.00 64.12           C  
-ANISOU 2345  C   ALA B 497     7695   9020   7649  -1390    854  -1353       C  
-ATOM   2346  O   ALA B 497     -15.151   5.905   7.836  1.00 57.06           O  
-ANISOU 2346  O   ALA B 497     6818   8060   6802  -1273    813  -1268       O  
-ATOM   2347  CB  ALA B 497     -15.962   6.616  10.890  1.00 38.37           C  
-ANISOU 2347  CB  ALA B 497     4300   5847   4430  -1377    869  -1485       C  
-ATOM   2348  N   PHE B 498     -17.003   4.797   8.482  1.00 69.20           N  
-ANISOU 2348  N   PHE B 498     8433   9667   8193  -1542    916  -1354       N  
-ATOM   2349  CA  PHE B 498     -16.808   3.687   7.561  1.00 62.55           C  
-ANISOU 2349  CA  PHE B 498     7736   8736   7293  -1577    945  -1259       C  
-ATOM   2350  C   PHE B 498     -17.041   4.128   6.120  1.00 67.68           C  
-ANISOU 2350  C   PHE B 498     8350   9398   7967  -1525    897  -1237       C  
-ATOM   2351  O   PHE B 498     -16.215   3.872   5.244  1.00 66.77           O  
-ANISOU 2351  O   PHE B 498     8285   9220   7866  -1411    890  -1127       O  
-ATOM   2352  CB  PHE B 498     -17.729   2.521   7.926  1.00 41.51           C  
-ANISOU 2352  CB  PHE B 498     5203   6063   4505  -1770   1032  -1282       C  
-ATOM   2353  CG  PHE B 498     -17.508   1.291   7.094  1.00 47.91           C  
-ANISOU 2353  CG  PHE B 498     6209   6768   5228  -1781   1088  -1183       C  
-ATOM   2354  CD1 PHE B 498     -16.293   0.629   7.127  1.00 48.28           C  
-ANISOU 2354  CD1 PHE B 498     6389   6704   5250  -1647   1114  -1075       C  
-ATOM   2355  CD2 PHE B 498     -18.518   0.791   6.288  1.00 56.18           C  
-ANISOU 2355  CD2 PHE B 498     7311   7829   6206  -1921   1113  -1209       C  
-ATOM   2356  CE1 PHE B 498     -16.084  -0.505   6.366  1.00 39.90           C  
-ANISOU 2356  CE1 PHE B 498     5523   5536   4100  -1647   1165   -997       C  
-ATOM   2357  CE2 PHE B 498     -18.316  -0.345   5.525  1.00 54.09           C  
-ANISOU 2357  CE2 PHE B 498     7234   7461   5857  -1935   1166  -1132       C  
-ATOM   2358  CZ  PHE B 498     -17.097  -0.993   5.565  1.00 51.53           C  
-ANISOU 2358  CZ  PHE B 498     7053   7015   5511  -1795   1193  -1028       C  
-ATOM   2359  N   LYS B 499     -18.165   4.798   5.881  1.00 64.93           N  
-ANISOU 2359  N   LYS B 499     7918   9151   7602  -1563    892  -1311       N  
-ATOM   2360  CA  LYS B 499     -18.496   5.289   4.546  1.00 72.42           C  
-ANISOU 2360  CA  LYS B 499     8830  10128   8560  -1511    850  -1291       C  
-ATOM   2361  C   LYS B 499     -17.444   6.270   4.030  1.00 67.99           C  
-ANISOU 2361  C   LYS B 499     8206   9524   8102  -1328    776  -1241       C  
-ATOM   2362  O   LYS B 499     -17.018   6.188   2.877  1.00 67.15           O  
-ANISOU 2362  O   LYS B 499     8117   9390   8007  -1243    764  -1137       O  
-ATOM   2363  CB  LYS B 499     -19.882   5.944   4.539  1.00 83.62           C  
-ANISOU 2363  CB  LYS B 499    10162  11669   9940  -1568    867  -1379       C  
-ATOM   2364  CG  LYS B 499     -21.032   4.963   4.721  1.00 85.76           C  
-ANISOU 2364  CG  LYS B 499    10496  11999  10089  -1761    938  -1420       C  
-ATOM   2365  CD  LYS B 499     -22.388   5.662   4.698  1.00 86.16           C  
-ANISOU 2365  CD  LYS B 499    10447  12189  10099  -1813    950  -1510       C  
-ATOM   2366  CE  LYS B 499     -22.952   5.845   6.101  1.00 87.62           C  
-ANISOU 2366  CE  LYS B 499    10582  12445  10263  -1882    996  -1604       C  
-ATOM   2367  NZ  LYS B 499     -24.354   6.356   6.081  1.00 88.20           N  
-ANISOU 2367  NZ  LYS B 499    10567  12665  10280  -1955   1016  -1698       N  
-ATOM   2368  N   ASN B 500     -17.031   7.195   4.891  1.00 64.66           N  
-ANISOU 2368  N   ASN B 500     7708   9106   7756  -1249    756  -1289       N  
-ATOM   2369  CA  ASN B 500     -16.030   8.189   4.527  1.00 61.69           C  
-ANISOU 2369  CA  ASN B 500     7272   8683   7483  -1070    716  -1223       C  
-ATOM   2370  C   ASN B 500     -14.709   7.567   4.086  1.00 58.57           C  
-ANISOU 2370  C   ASN B 500     6934   8217   7104   -976    711  -1080       C  
-ATOM   2371  O   ASN B 500     -14.181   7.904   3.026  1.00 55.46           O  
-ANISOU 2371  O   ASN B 500     6522   7799   6750   -866    690   -974       O  
-ATOM   2372  CB  ASN B 500     -15.795   9.165   5.682  1.00 63.32           C  
-ANISOU 2372  CB  ASN B 500     7402   8893   7766  -1027    705  -1318       C  
-ATOM   2373  CG  ASN B 500     -16.993  10.056   5.944  1.00 66.32           C  
-ANISOU 2373  CG  ASN B 500     7709   9336   8154  -1067    717  -1448       C  
-ATOM   2374  OD1 ASN B 500     -18.038   9.915   5.309  1.00 66.00           O  
-ANISOU 2374  OD1 ASN B 500     7671   9354   8051  -1131    734  -1461       O  
-ATOM   2375  ND2 ASN B 500     -16.846  10.982   6.885  1.00 64.10           N  
-ANISOU 2375  ND2 ASN B 500     7350   9049   7955  -1019    718  -1534       N  
-ATOM   2376  N   GLU B 501     -14.178   6.660   4.900  1.00 57.24           N  
-ANISOU 2376  N   GLU B 501     6830   8017   6901  -1014    738  -1066       N  
-ATOM   2377  CA  GLU B 501     -12.912   6.010   4.580  1.00 55.97           C  
-ANISOU 2377  CA  GLU B 501     6733   7795   6739   -908    747   -933       C  
-ATOM   2378  C   GLU B 501     -13.045   5.094   3.367  1.00 57.42           C  
-ANISOU 2378  C   GLU B 501     7009   7948   6862   -920    774   -846       C  
-ATOM   2379  O   GLU B 501     -12.099   4.923   2.601  1.00 59.08           O  
-ANISOU 2379  O   GLU B 501     7239   8123   7086   -799    763   -732       O  
-ATOM   2380  CB  GLU B 501     -12.370   5.229   5.780  1.00 80.45           C  
-ANISOU 2380  CB  GLU B 501     9901  10868   9797   -926    790   -931       C  
-ATOM   2381  CG  GLU B 501     -10.998   4.619   5.530  1.00 88.51           C  
-ANISOU 2381  CG  GLU B 501    10998  11832  10800   -784    802   -799       C  
-ATOM   2382  CD  GLU B 501     -10.421   3.927   6.751  1.00100.22           C  
-ANISOU 2382  CD  GLU B 501    12562  13293  12223   -767    846   -794       C  
-ATOM   2383  OE1 GLU B 501      -9.284   3.418   6.657  1.00100.56           O  
-ANISOU 2383  OE1 GLU B 501    12681  13297  12232   -633    856   -697       O  
-ATOM   2384  OE2 GLU B 501     -11.098   3.891   7.800  1.00103.57           O  
-ANISOU 2384  OE2 GLU B 501    12981  13748  12625   -878    871   -888       O  
-ATOM   2385  N   VAL B 502     -14.224   4.506   3.196  1.00 73.22           N  
-ANISOU 2385  N   VAL B 502     9062   9967   8790  -1072    810   -906       N  
-ATOM   2386  CA  VAL B 502     -14.483   3.652   2.044  1.00 72.05           C  
-ANISOU 2386  CA  VAL B 502     9002   9795   8580  -1104    839   -846       C  
-ATOM   2387  C   VAL B 502     -14.565   4.482   0.768  1.00 74.98           C  
-ANISOU 2387  C   VAL B 502     9278  10216   8997  -1021    783   -803       C  
-ATOM   2388  O   VAL B 502     -14.091   4.066  -0.289  1.00 80.97           O  
-ANISOU 2388  O   VAL B 502    10070  10950   9745   -955    784   -706       O  
-ATOM   2389  CB  VAL B 502     -15.777   2.833   2.223  1.00 56.16           C  
-ANISOU 2389  CB  VAL B 502     7072   7796   6468  -1309    895   -929       C  
-ATOM   2390  CG1 VAL B 502     -16.636   2.895   0.968  1.00 48.92           C  
-ANISOU 2390  CG1 VAL B 502     6129   6937   5520  -1362    879   -938       C  
-ATOM   2391  CG2 VAL B 502     -15.444   1.395   2.583  1.00 49.39           C  
-ANISOU 2391  CG2 VAL B 502     6411   6836   5521  -1359    981   -884       C  
-ATOM   2392  N   GLY B 503     -15.163   5.662   0.877  1.00 59.40           N  
-ANISOU 2392  N   GLY B 503     7192   8308   7070  -1015    743   -869       N  
-ATOM   2393  CA  GLY B 503     -15.308   6.550  -0.260  1.00 58.24           C  
-ANISOU 2393  CA  GLY B 503     6963   8201   6965   -928    706   -812       C  
-ATOM   2394  C   GLY B 503     -13.994   7.164  -0.700  1.00 63.60           C  
-ANISOU 2394  C   GLY B 503     7596   8835   7735   -754    672   -687       C  
-ATOM   2395  O   GLY B 503     -13.798   7.439  -1.883  1.00 74.18           O  
-ANISOU 2395  O   GLY B 503     8902  10186   9097   -680    653   -585       O  
-ATOM   2396  N   VAL B 504     -13.090   7.380   0.251  1.00 53.37           N  
-ANISOU 2396  N   VAL B 504     6294   7495   6487   -695    666   -690       N  
-ATOM   2397  CA  VAL B 504     -11.800   7.996  -0.050  1.00 50.40           C  
-ANISOU 2397  CA  VAL B 504     5873   7083   6194   -545    636   -578       C  
-ATOM   2398  C   VAL B 504     -10.816   6.980  -0.626  1.00 50.76           C  
-ANISOU 2398  C   VAL B 504     5988   7103   6196   -481    643   -465       C  
-ATOM   2399  O   VAL B 504      -9.956   7.323  -1.438  1.00 52.62           O  
-ANISOU 2399  O   VAL B 504     6188   7332   6473   -367    617   -346       O  
-ATOM   2400  CB  VAL B 504     -11.181   8.674   1.193  1.00 39.27           C  
-ANISOU 2400  CB  VAL B 504     4422   5649   4852   -509    626   -632       C  
-ATOM   2401  CG1 VAL B 504     -10.935   7.657   2.287  1.00 53.76           C  
-ANISOU 2401  CG1 VAL B 504     6331   7478   6619   -566    651   -685       C  
-ATOM   2402  CG2 VAL B 504      -9.885   9.376   0.828  1.00 44.46           C  
-ANISOU 2402  CG2 VAL B 504     5027   6271   5594   -373    598   -517       C  
-ATOM   2403  N   LEU B 505     -10.952   5.728  -0.205  1.00 45.78           N  
-ANISOU 2403  N   LEU B 505     5463   6449   5483   -554    688   -498       N  
-ATOM   2404  CA  LEU B 505     -10.084   4.659  -0.683  1.00 40.81           C  
-ANISOU 2404  CA  LEU B 505     4926   5777   4804   -486    717   -401       C  
-ATOM   2405  C   LEU B 505     -10.374   4.311  -2.140  1.00 43.62           C  
-ANISOU 2405  C   LEU B 505     5292   6150   5132   -482    718   -337       C  
-ATOM   2406  O   LEU B 505      -9.456   4.114  -2.935  1.00 49.94           O  
-ANISOU 2406  O   LEU B 505     6093   6944   5938   -366    708   -228       O  
-ATOM   2407  CB  LEU B 505     -10.241   3.414   0.193  1.00 46.41           C  
-ANISOU 2407  CB  LEU B 505     5780   6428   5425   -566    788   -448       C  
-ATOM   2408  CG  LEU B 505      -9.640   3.472   1.598  1.00 43.77           C  
-ANISOU 2408  CG  LEU B 505     5456   6077   5095   -537    796   -477       C  
-ATOM   2409  CD1 LEU B 505     -10.148   2.318   2.444  1.00 43.15           C  
-ANISOU 2409  CD1 LEU B 505     5535   5942   4917   -647    874   -529       C  
-ATOM   2410  CD2 LEU B 505      -8.121   3.468   1.536  1.00 40.42           C  
-ANISOU 2410  CD2 LEU B 505     5031   5642   4685   -359    779   -369       C  
-ATOM   2411  N   ARG B 506     -11.656   4.240  -2.484  1.00 50.84           N  
-ANISOU 2411  N   ARG B 506     6208   7098   6011   -610    728   -410       N  
-ATOM   2412  CA  ARG B 506     -12.070   3.831  -3.822  1.00 53.59           C  
-ANISOU 2412  CA  ARG B 506     6567   7474   6319   -629    733   -366       C  
-ATOM   2413  C   ARG B 506     -11.631   4.835  -4.885  1.00 54.67           C  
-ANISOU 2413  C   ARG B 506     6583   7663   6525   -507    673   -259       C  
-ATOM   2414  O   ARG B 506     -11.627   4.529  -6.078  1.00 57.84           O  
-ANISOU 2414  O   ARG B 506     6980   8095   6904   -484    670   -190       O  
-ATOM   2415  CB  ARG B 506     -13.586   3.630  -3.876  1.00 51.21           C  
-ANISOU 2415  CB  ARG B 506     6283   7219   5957   -802    754   -473       C  
-ATOM   2416  CG  ARG B 506     -14.391   4.918  -3.907  1.00 56.20           C  
-ANISOU 2416  CG  ARG B 506     6789   7933   6633   -812    707   -516       C  
-ATOM   2417  CD  ARG B 506     -15.875   4.625  -4.043  1.00 71.43           C  
-ANISOU 2417  CD  ARG B 506     8733   9927   8480   -979    729   -617       C  
-ATOM   2418  NE  ARG B 506     -16.130   3.555  -5.004  1.00 83.62           N  
-ANISOU 2418  NE  ARG B 506    10354  11474   9945  -1048    762   -592       N  
-ATOM   2419  CZ  ARG B 506     -16.215   3.731  -6.319  1.00 89.94           C  
-ANISOU 2419  CZ  ARG B 506    11099  12333  10741  -1003    737   -518       C  
-ATOM   2420  NH1 ARG B 506     -16.063   4.941  -6.841  1.00 96.69           N  
-ANISOU 2420  NH1 ARG B 506    11830  13241  11668   -886    684   -444       N  
-ATOM   2421  NH2 ARG B 506     -16.450   2.696  -7.114  1.00 85.26           N  
-ANISOU 2421  NH2 ARG B 506    10584  11740  10072  -1079    775   -510       N  
-ATOM   2422  N   LYS B 507     -11.255   6.031  -4.446  1.00 39.49           N  
-ANISOU 2422  N   LYS B 507     4572   5745   4688   -434    634   -241       N  
-ATOM   2423  CA  LYS B 507     -10.822   7.078  -5.363  1.00 42.63           C  
-ANISOU 2423  CA  LYS B 507     4871   6167   5160   -328    591   -123       C  
-ATOM   2424  C   LYS B 507      -9.315   7.079  -5.568  1.00 44.39           C  
-ANISOU 2424  C   LYS B 507     5087   6364   5416   -194    573     -2       C  
-ATOM   2425  O   LYS B 507      -8.772   7.982  -6.204  1.00 47.35           O  
-ANISOU 2425  O   LYS B 507     5387   6746   5859   -112    543    107       O  
-ATOM   2426  CB  LYS B 507     -11.279   8.445  -4.862  1.00 54.93           C  
-ANISOU 2426  CB  LYS B 507     6347   7720   6803   -332    577   -161       C  
-ATOM   2427  CG  LYS B 507     -12.782   8.599  -4.849  1.00 68.89           C  
-ANISOU 2427  CG  LYS B 507     8101   9538   8537   -443    592   -262       C  
-ATOM   2428  CD  LYS B 507     -13.203   9.999  -4.455  1.00 83.00           C  
-ANISOU 2428  CD  LYS B 507     9799  11310  10427   -426    589   -288       C  
-ATOM   2429  CE  LYS B 507     -14.719  10.123  -4.463  1.00 96.77           C  
-ANISOU 2429  CE  LYS B 507    11523  13121  12124   -529    608   -386       C  
-ATOM   2430  NZ  LYS B 507     -15.176  11.530  -4.271  1.00106.68           N  
-ANISOU 2430  NZ  LYS B 507    12678  14357  13498   -499    612   -395       N  
-ATOM   2431  N   THR B 508      -8.642   6.066  -5.032  1.00 42.76           N  
-ANISOU 2431  N   THR B 508     4964   6125   5159   -175    600    -15       N  
-ATOM   2432  CA  THR B 508      -7.190   5.984  -5.136  1.00 46.94           C  
-ANISOU 2432  CA  THR B 508     5490   6645   5701    -42    587     93       C  
-ATOM   2433  C   THR B 508      -6.716   4.784  -5.952  1.00 41.57           C  
-ANISOU 2433  C   THR B 508     4880   5965   4950     11    616    154       C  
-ATOM   2434  O   THR B 508      -7.121   3.647  -5.710  1.00 41.50           O  
-ANISOU 2434  O   THR B 508     4985   5914   4870    -51    674     88       O  
-ATOM   2435  CB  THR B 508      -6.519   5.946  -3.746  1.00 56.11           C  
-ANISOU 2435  CB  THR B 508     6682   7772   6866    -19    597     46       C  
-ATOM   2436  OG1 THR B 508      -6.857   4.723  -3.078  1.00 55.74           O  
-ANISOU 2436  OG1 THR B 508     6754   7684   6740    -80    654    -33       O  
-ATOM   2437  CG2 THR B 508      -6.974   7.126  -2.904  1.00 56.17           C  
-ANISOU 2437  CG2 THR B 508     6620   7774   6948    -73    576    -32       C  
-ATOM   2438  N   ARG B 509      -5.854   5.062  -6.925  1.00 39.12           N  
-ANISOU 2438  N   ARG B 509     4512   5694   4657    121    584    283       N  
-ATOM   2439  CA  ARG B 509      -5.196   4.032  -7.717  1.00 35.22           C  
-ANISOU 2439  CA  ARG B 509     4071   5208   4103    201    611    349       C  
-ATOM   2440  C   ARG B 509      -3.775   4.473  -8.040  1.00 23.84           C  
-ANISOU 2440  C   ARG B 509     2569   3809   2681    349    574    481       C  
-ATOM   2441  O   ARG B 509      -3.500   4.962  -9.135  1.00 25.95           O  
-ANISOU 2441  O   ARG B 509     2759   4134   2968    393    538    587       O  
-ATOM   2442  CB  ARG B 509      -5.968   3.756  -9.008  1.00 41.81           C  
-ANISOU 2442  CB  ARG B 509     4888   6082   4915    150    615    363       C  
-ATOM   2443  CG  ARG B 509      -7.214   2.910  -8.820  1.00 35.75           C  
-ANISOU 2443  CG  ARG B 509     4219   5277   4088      3    671    238       C  
-ATOM   2444  CD  ARG B 509      -7.937   2.688 -10.136  1.00 30.76           C  
-ANISOU 2444  CD  ARG B 509     3560   4702   3425    -51    671    255       C  
-ATOM   2445  NE  ARG B 509      -9.031   1.732  -9.997  1.00 38.14           N  
-ANISOU 2445  NE  ARG B 509     4612   5598   4282   -204    735    139       N  
-ATOM   2446  CZ  ARG B 509      -8.891   0.416 -10.110  1.00 35.02           C  
-ANISOU 2446  CZ  ARG B 509     4372   5133   3801   -225    811    115       C  
-ATOM   2447  NH1 ARG B 509      -7.700  -0.109 -10.367  1.00 35.13           N  
-ANISOU 2447  NH1 ARG B 509     4436   5116   3796    -84    833    192       N  
-ATOM   2448  NH2 ARG B 509      -9.943  -0.379  -9.965  1.00 31.56           N  
-ANISOU 2448  NH2 ARG B 509     4054   4651   3284   -387    870     15       N  
-ATOM   2449  N   HIS B 510      -2.879   4.304  -7.072  1.00 32.42           N  
-ANISOU 2449  N   HIS B 510     3693   4874   3750    418    583    478       N  
-ATOM   2450  CA  HIS B 510      -1.491   4.724  -7.219  1.00 30.12           C  
-ANISOU 2450  CA  HIS B 510     3352   4636   3457    546    550    594       C  
-ATOM   2451  C   HIS B 510      -0.578   3.681  -6.590  1.00 31.98           C  
-ANISOU 2451  C   HIS B 510     3683   4855   3613    657    590    588       C  
-ATOM   2452  O   HIS B 510      -0.936   3.058  -5.592  1.00 35.83           O  
-ANISOU 2452  O   HIS B 510     4269   5276   4070    621    635    491       O  
-ATOM   2453  CB  HIS B 510      -1.274   6.081  -6.546  1.00 25.55           C  
-ANISOU 2453  CB  HIS B 510     2698   4063   2948    509    513    600       C  
-ATOM   2454  CG  HIS B 510       0.013   6.748  -6.921  1.00 12.44           C  
-ANISOU 2454  CG  HIS B 510      978   2461   1287    594    488    727       C  
-ATOM   2455  ND1 HIS B 510       1.205   6.478  -6.283  1.00 21.18           N  
-ANISOU 2455  ND1 HIS B 510     2108   3604   2336    688    491    750       N  
-ATOM   2456  CD2 HIS B 510       0.290   7.678  -7.862  1.00 14.31           C  
-ANISOU 2456  CD2 HIS B 510     1138   2730   1570    591    469    838       C  
-ATOM   2457  CE1 HIS B 510       2.162   7.213  -6.821  1.00 29.66           C  
-ANISOU 2457  CE1 HIS B 510     3118   4738   3413    727    477    862       C  
-ATOM   2458  NE2 HIS B 510       1.636   7.950  -7.780  1.00 26.97           N  
-ANISOU 2458  NE2 HIS B 510     2718   4388   3142    666    468    920       N  
-ATOM   2459  N   VAL B 511       0.602   3.495  -7.170  1.00 40.15           N  
-ANISOU 2459  N   VAL B 511     4700   5950   4605    796    578    695       N  
-ATOM   2460  CA  VAL B 511       1.526   2.470  -6.694  1.00 40.09           C  
-ANISOU 2460  CA  VAL B 511     4794   5929   4508    935    620    698       C  
-ATOM   2461  C   VAL B 511       2.117   2.811  -5.324  1.00 41.64           C  
-ANISOU 2461  C   VAL B 511     4998   6132   4689    961    606    668       C  
-ATOM   2462  O   VAL B 511       2.629   1.937  -4.625  1.00 46.58           O  
-ANISOU 2462  O   VAL B 511     5736   6726   5237   1058    647    641       O  
-ATOM   2463  CB  VAL B 511       2.665   2.214  -7.706  1.00 49.43           C  
-ANISOU 2463  CB  VAL B 511     5946   7197   5640   1089    607    819       C  
-ATOM   2464  CG1 VAL B 511       3.750   3.268  -7.568  1.00 51.50           C  
-ANISOU 2464  CG1 VAL B 511     6106   7564   5897   1135    543    917       C  
-ATOM   2465  CG2 VAL B 511       3.249   0.831  -7.500  1.00 67.60           C  
-ANISOU 2465  CG2 VAL B 511     8397   9450   7838   1232    676    796       C  
-ATOM   2466  N   ASN B 512       2.044   4.082  -4.942  1.00 44.40           N  
-ANISOU 2466  N   ASN B 512     5245   6517   5107    875    557    667       N  
-ATOM   2467  CA  ASN B 512       2.544   4.515  -3.639  1.00 38.03           C  
-ANISOU 2467  CA  ASN B 512     4431   5725   4293    878    546    621       C  
-ATOM   2468  C   ASN B 512       1.427   4.744  -2.627  1.00 25.78           C  
-ANISOU 2468  C   ASN B 512     2894   4103   2799    741    559    488       C  
-ATOM   2469  O   ASN B 512       1.640   5.354  -1.581  1.00 29.98           O  
-ANISOU 2469  O   ASN B 512     3390   4648   3352    711    545    432       O  
-ATOM   2470  CB  ASN B 512       3.398   5.776  -3.776  1.00 40.43           C  
-ANISOU 2470  CB  ASN B 512     4625   6109   4626    873    506    691       C  
-ATOM   2471  CG  ASN B 512       4.696   5.521  -4.511  1.00 39.71           C  
-ANISOU 2471  CG  ASN B 512     4527   6116   4446   1011    499    815       C  
-ATOM   2472  OD1 ASN B 512       5.060   6.257  -5.428  1.00 35.61           O  
-ANISOU 2472  OD1 ASN B 512     3934   5647   3949    991    488    907       O  
-ATOM   2473  ND2 ASN B 512       5.402   4.467  -4.115  1.00 39.58           N  
-ANISOU 2473  ND2 ASN B 512     4591   6121   4325   1158    513    818       N  
-ATOM   2474  N   ILE B 513       0.237   4.254  -2.951  1.00 28.26           N  
-ANISOU 2474  N   ILE B 513     3257   4350   3131    651    590    431       N  
-ATOM   2475  CA  ILE B 513      -0.900   4.326  -2.045  1.00 27.73           C  
-ANISOU 2475  CA  ILE B 513     3216   4224   3096    514    610    303       C  
-ATOM   2476  C   ILE B 513      -1.350   2.912  -1.707  1.00 38.55           C  
-ANISOU 2476  C   ILE B 513     4751   5516   4381    506    685    248       C  
-ATOM   2477  O   ILE B 513      -1.530   2.086  -2.602  1.00 46.03           O  
-ANISOU 2477  O   ILE B 513     5776   6429   5284    526    722    278       O  
-ATOM   2478  CB  ILE B 513      -2.080   5.096  -2.673  1.00 26.94           C  
-ANISOU 2478  CB  ILE B 513     3043   4114   3077    384    589    270       C  
-ATOM   2479  CG1 ILE B 513      -1.664   6.525  -3.027  1.00 22.10           C  
-ANISOU 2479  CG1 ILE B 513     2309   3541   2547    388    538    331       C  
-ATOM   2480  CG2 ILE B 513      -3.278   5.105  -1.734  1.00 27.35           C  
-ANISOU 2480  CG2 ILE B 513     3124   4122   3148    245    612    131       C  
-ATOM   2481  CD1 ILE B 513      -1.256   7.354  -1.833  1.00 36.84           C  
-ANISOU 2481  CD1 ILE B 513     4130   5410   4459    372    525    271       C  
-ATOM   2482  N   LEU B 514      -1.510   2.631  -0.416  1.00 62.90           N  
-ANISOU 2482  N   LEU B 514     7902   8564   7432    472    712    168       N  
-ATOM   2483  CA  LEU B 514      -2.003   1.334   0.038  1.00 64.98           C  
-ANISOU 2483  CA  LEU B 514     8359   8731   7599    440    791    116       C  
-ATOM   2484  C   LEU B 514      -3.165   0.893  -0.847  1.00 62.17           C  
-ANISOU 2484  C   LEU B 514     8056   8324   7242    315    826     86       C  
-ATOM   2485  O   LEU B 514      -4.117   1.647  -1.043  1.00 72.83           O  
-ANISOU 2485  O   LEU B 514     9302   9704   8668    186    797     35       O  
-ATOM   2486  CB  LEU B 514      -2.458   1.421   1.497  1.00 76.30           C  
-ANISOU 2486  CB  LEU B 514     9821  10146   9023    353    804     19       C  
-ATOM   2487  CG  LEU B 514      -2.943   0.135   2.170  1.00 83.31           C  
-ANISOU 2487  CG  LEU B 514    10932  10928   9796    306    885    -29       C  
-ATOM   2488  CD1 LEU B 514      -1.777  -0.800   2.463  1.00 88.61           C  
-ANISOU 2488  CD1 LEU B 514    11758  11559  10351    488    914     34       C  
-ATOM   2489  CD2 LEU B 514      -3.705   0.457   3.448  1.00 77.55           C  
-ANISOU 2489  CD2 LEU B 514    10183  10203   9080    174    890   -133       C  
-ATOM   2490  N   LEU B 515      -3.085  -0.323  -1.383  1.00 36.62           N  
-ANISOU 2490  N   LEU B 515     4992   5012   3911    356    888    112       N  
-ATOM   2491  CA  LEU B 515      -4.095  -0.806  -2.324  1.00 34.24           C  
-ANISOU 2491  CA  LEU B 515     4746   4670   3593    239    924     84       C  
-ATOM   2492  C   LEU B 515      -5.382  -1.274  -1.645  1.00 44.96           C  
-ANISOU 2492  C   LEU B 515     6216   5957   4908     49    974    -22       C  
-ATOM   2493  O   LEU B 515      -5.433  -2.355  -1.058  1.00 46.17           O  
-ANISOU 2493  O   LEU B 515     6582   6009   4953     34   1041    -46       O  
-ATOM   2494  CB  LEU B 515      -3.530  -1.925  -3.205  1.00 47.66           C  
-ANISOU 2494  CB  LEU B 515     6596   6312   5199    345    974    145       C  
-ATOM   2495  CG  LEU B 515      -4.471  -2.478  -4.280  1.00 37.62           C  
-ANISOU 2495  CG  LEU B 515     5386   5008   3900    229   1012    120       C  
-ATOM   2496  CD1 LEU B 515      -4.970  -1.357  -5.176  1.00 30.81           C  
-ANISOU 2496  CD1 LEU B 515     4297   4259   3150    170    943    132       C  
-ATOM   2497  CD2 LEU B 515      -3.788  -3.559  -5.103  1.00 43.73           C  
-ANISOU 2497  CD2 LEU B 515     6314   5725   4577    348   1062    177       C  
-ATOM   2498  N   PHE B 516      -6.416  -0.445  -1.740  1.00 44.42           N  
-ANISOU 2498  N   PHE B 516     6013   5948   4918    -93    939    -84       N  
-ATOM   2499  CA  PHE B 516      -7.752  -0.797  -1.276  1.00 40.12           C  
-ANISOU 2499  CA  PHE B 516     5544   5365   4334   -290    980   -187       C  
-ATOM   2500  C   PHE B 516      -8.355  -1.855  -2.197  1.00 43.35           C  
-ANISOU 2500  C   PHE B 516     6103   5711   4657   -369   1040   -193       C  
-ATOM   2501  O   PHE B 516      -8.370  -1.684  -3.414  1.00 45.21           O  
-ANISOU 2501  O   PHE B 516     6265   5994   4921   -344   1017   -153       O  
-ATOM   2502  CB  PHE B 516      -8.631   0.456  -1.239  1.00 44.65           C  
-ANISOU 2502  CB  PHE B 516     5921   6034   5008   -393    917   -251       C  
-ATOM   2503  CG  PHE B 516     -10.106   0.181  -1.357  1.00 58.19           C  
-ANISOU 2503  CG  PHE B 516     7675   7750   6686   -591    947   -345       C  
-ATOM   2504  CD1 PHE B 516     -10.863  -0.127  -0.238  1.00 67.30           C  
-ANISOU 2504  CD1 PHE B 516     8902   8875   7793   -729    987   -435       C  
-ATOM   2505  CD2 PHE B 516     -10.741   0.261  -2.587  1.00 58.38           C  
-ANISOU 2505  CD2 PHE B 516     7650   7818   6713   -642    932   -341       C  
-ATOM   2506  CE1 PHE B 516     -12.222  -0.369  -0.348  1.00 61.55           C  
-ANISOU 2506  CE1 PHE B 516     8202   8164   7022   -919   1013   -522       C  
-ATOM   2507  CE2 PHE B 516     -12.098   0.021  -2.702  1.00 53.72           C  
-ANISOU 2507  CE2 PHE B 516     7087   7247   6076   -826    957   -430       C  
-ATOM   2508  CZ  PHE B 516     -12.839  -0.294  -1.582  1.00 44.51           C  
-ANISOU 2508  CZ  PHE B 516     5995   6053   4863   -968    997   -522       C  
-ATOM   2509  N   MET B 517      -8.847  -2.946  -1.617  1.00 40.03           N  
-ANISOU 2509  N   MET B 517     5898   5188   4124   -470   1116   -241       N  
-ATOM   2510  CA  MET B 517      -9.352  -4.062  -2.412  1.00 44.76           C  
-ANISOU 2510  CA  MET B 517     6677   5709   4620   -551   1182   -249       C  
-ATOM   2511  C   MET B 517     -10.850  -4.332  -2.247  1.00 53.84           C  
-ANISOU 2511  C   MET B 517     7879   6854   5725   -794   1218   -349       C  
-ATOM   2512  O   MET B 517     -11.450  -5.012  -3.081  1.00 58.80           O  
-ANISOU 2512  O   MET B 517     8602   7453   6285   -892   1258   -367       O  
-ATOM   2513  CB  MET B 517      -8.548  -5.332  -2.116  1.00 39.61           C  
-ANISOU 2513  CB  MET B 517     6292   4917   3841   -449   1250   -205       C  
-ATOM   2514  CG  MET B 517      -7.087  -5.244  -2.520  1.00 36.06           C  
-ANISOU 2514  CG  MET B 517     5809   4482   3411   -206   1222   -105       C  
-ATOM   2515  SD  MET B 517      -6.213  -6.803  -2.292  1.00 56.32           S  
-ANISOU 2515  SD  MET B 517     8711   6882   5805    -71   1302    -61       S  
-ATOM   2516  CE  MET B 517      -7.179  -7.889  -3.339  1.00 68.66           C  
-ANISOU 2516  CE  MET B 517    10467   8356   7267   -230   1376    -98       C  
-ATOM   2517  N   GLY B 518     -11.448  -3.809  -1.178  1.00 57.99           N  
-ANISOU 2517  N   GLY B 518     8337   7417   6280   -894   1203   -418       N  
-ATOM   2518  CA  GLY B 518     -12.870  -3.995  -0.935  1.00 60.79           C  
-ANISOU 2518  CA  GLY B 518     8720   7789   6589  -1125   1234   -517       C  
-ATOM   2519  C   GLY B 518     -13.290  -3.773   0.505  1.00 63.43           C  
-ANISOU 2519  C   GLY B 518     9052   8132   6918  -1214   1242   -582       C  
-ATOM   2520  O   GLY B 518     -12.457  -3.515   1.376  1.00 59.45           O  
-ANISOU 2520  O   GLY B 518     8533   7614   6441  -1094   1226   -552       O  
-ATOM   2521  N   TYR B 519     -14.593  -3.878   0.748  1.00 72.76           N  
-ANISOU 2521  N   TYR B 519    10240   9349   8057  -1427   1266   -674       N  
-ATOM   2522  CA  TYR B 519     -15.151  -3.672   2.075  1.00 72.46           C  
-ANISOU 2522  CA  TYR B 519    10185   9338   8007  -1535   1278   -746       C  
-ATOM   2523  C   TYR B 519     -16.245  -4.696   2.387  1.00 72.75           C  
-ANISOU 2523  C   TYR B 519    10409   9326   7907  -1761   1358   -810       C  
-ATOM   2524  O   TYR B 519     -16.533  -5.574   1.565  1.00 73.78           O  
-ANISOU 2524  O   TYR B 519    10690   9391   7951  -1832   1405   -800       O  
-ATOM   2525  CB  TYR B 519     -15.714  -2.262   2.191  1.00 60.09           C  
-ANISOU 2525  CB  TYR B 519     8347   7925   6561  -1562   1199   -811       C  
-ATOM   2526  CG  TYR B 519     -16.991  -2.038   1.420  1.00 61.05           C  
-ANISOU 2526  CG  TYR B 519     8387   8139   6671  -1720   1186   -883       C  
-ATOM   2527  CD1 TYR B 519     -18.229  -2.331   1.987  1.00 53.67           C  
-ANISOU 2527  CD1 TYR B 519     7485   7245   5662  -1936   1225   -979       C  
-ATOM   2528  CD2 TYR B 519     -16.960  -1.513   0.136  1.00 63.91           C  
-ANISOU 2528  CD2 TYR B 519     8634   8562   7088  -1649   1131   -854       C  
-ATOM   2529  CE1 TYR B 519     -19.390  -2.119   1.298  1.00 55.82           C  
-ANISOU 2529  CE1 TYR B 519     7678   7620   5912  -2074   1209  -1049       C  
-ATOM   2530  CE2 TYR B 519     -18.116  -1.296  -0.562  1.00 61.06           C  
-ANISOU 2530  CE2 TYR B 519     8198   8299   6701  -1779   1114   -919       C  
-ATOM   2531  CZ  TYR B 519     -19.330  -1.602   0.027  1.00 60.97           C  
-ANISOU 2531  CZ  TYR B 519     8221   8332   6613  -1991   1153  -1019       C  
-ATOM   2532  OH  TYR B 519     -20.499  -1.388  -0.656  1.00 61.13           O  
-ANISOU 2532  OH  TYR B 519     8164   8469   6594  -2119   1134  -1088       O  
-ATOM   2533  N   SER B 520     -16.852  -4.577   3.570  1.00 72.33           N  
-ANISOU 2533  N   SER B 520    10345   9309   7830  -1880   1375   -877       N  
-ATOM   2534  CA  SER B 520     -17.937  -5.473   3.996  1.00 75.17           C  
-ANISOU 2534  CA  SER B 520    10870   9639   8054  -2112   1450   -942       C  
-ATOM   2535  C   SER B 520     -18.753  -4.834   5.133  1.00 74.04           C  
-ANISOU 2535  C   SER B 520    10590   9610   7931  -2239   1439  -1032       C  
-ATOM   2536  O   SER B 520     -18.216  -4.050   5.910  1.00 71.32           O  
-ANISOU 2536  O   SER B 520    10114   9312   7671  -2128   1397  -1030       O  
-ATOM   2537  CB  SER B 520     -17.361  -6.827   4.433  1.00 70.09           C  
-ANISOU 2537  CB  SER B 520    10546   8817   7269  -2090   1529   -889       C  
-ATOM   2538  OG  SER B 520     -18.373  -7.815   4.521  1.00 72.35           O  
-ANISOU 2538  OG  SER B 520    11025   9054   7409  -2318   1605   -941       O  
-ATOM   2539  N   THR B 521     -20.045  -5.159   5.224  1.00 67.96           N  
-ANISOU 2539  N   THR B 521     9847   8895   7080  -2472   1478  -1115       N  
-ATOM   2540  CA  THR B 521     -20.925  -4.546   6.229  1.00 72.36           C  
-ANISOU 2540  CA  THR B 521    10260   9584   7651  -2603   1470  -1209       C  
-ATOM   2541  C   THR B 521     -21.737  -5.560   7.047  1.00 79.89           C  
-ANISOU 2541  C   THR B 521    11407  10504   8444  -2822   1557  -1255       C  
-ATOM   2542  O   THR B 521     -21.608  -5.617   8.272  1.00 88.46           O  
-ANISOU 2542  O   THR B 521    12526  11587   9498  -2831   1578  -1267       O  
-ATOM   2543  CB  THR B 521     -21.924  -3.530   5.607  1.00 92.83           C  
-ANISOU 2543  CB  THR B 521    12603  12351  10319  -2681   1408  -1293       C  
-ATOM   2544  OG1 THR B 521     -22.971  -4.235   4.927  1.00 94.99           O  
-ANISOU 2544  OG1 THR B 521    12965  12645  10484  -2881   1451  -1336       O  
-ATOM   2545  CG2 THR B 521     -21.219  -2.588   4.639  1.00 94.78           C  
-ANISOU 2545  CG2 THR B 521    12686  12625  10700  -2479   1320  -1249       C  
-ATOM   2546  N   ALA B 522     -22.555  -6.371   6.372  1.00 87.09           N  
-ANISOU 2546  N   ALA B 522    12450  11393   9246  -3001   1607  -1281       N  
-ATOM   2547  CA  ALA B 522     -23.580  -7.174   7.063  1.00 91.74           C  
-ANISOU 2547  CA  ALA B 522    13184  11991   9683  -3252   1683  -1345       C  
-ATOM   2548  C   ALA B 522     -23.138  -8.419   7.866  1.00100.60           C  
-ANISOU 2548  C   ALA B 522    14630  12939  10656  -3278   1763  -1299       C  
-ATOM   2549  O   ALA B 522     -23.932  -9.338   8.098  1.00111.56           O  
-ANISOU 2549  O   ALA B 522    16205  14294  11889  -3494   1834  -1338       O  
-ATOM   2550  CB  ALA B 522     -24.765  -7.493   6.128  1.00 79.64           C  
-ANISOU 2550  CB  ALA B 522    11651  10531   8079  -3464   1705  -1408       C  
-ATOM   2551  N   PRO B 523     -21.861  -8.457   8.266  1.00 93.61           N  
-ANISOU 2551  N   PRO B 523    13818  11944   9805  -3055   1747  -1218       N  
-ATOM   2552  CA  PRO B 523     -21.527  -9.028   9.571  1.00 93.53           C  
-ANISOU 2552  CA  PRO B 523    13984  11858   9696  -3054   1788  -1204       C  
-ATOM   2553  C   PRO B 523     -20.970  -7.893  10.422  1.00 91.20           C  
-ANISOU 2553  C   PRO B 523    13452  11669   9532  -2899   1724  -1208       C  
-ATOM   2554  O   PRO B 523     -21.734  -7.245  11.142  1.00 76.51           O  
-ANISOU 2554  O   PRO B 523    11413   9959   7699  -3012   1713  -1288       O  
-ATOM   2555  CB  PRO B 523     -20.417 -10.025   9.247  1.00 65.30           C  
-ANISOU 2555  CB  PRO B 523    10696   8071   6044  -2897   1819  -1107       C  
-ATOM   2556  CG  PRO B 523     -19.800  -9.512   7.930  1.00 60.87           C  
-ANISOU 2556  CG  PRO B 523    10004   7511   5612  -2730   1765  -1057       C  
-ATOM   2557  CD  PRO B 523     -20.685  -8.411   7.382  1.00 65.48           C  
-ANISOU 2557  CD  PRO B 523    10276   8285   6318  -2821   1713  -1127       C  
-ATOM   2558  N   GLN B 524     -19.659  -7.660  10.327  1.00 93.62           N  
-ANISOU 2558  N   GLN B 524    13754  11905   9913  -2648   1684  -1127       N  
-ATOM   2559  CA  GLN B 524     -19.000  -6.530  10.982  1.00 83.59           C  
-ANISOU 2559  CA  GLN B 524    12251  10733   8776  -2485   1617  -1127       C  
-ATOM   2560  C   GLN B 524     -18.689  -5.507   9.905  1.00 70.96           C  
-ANISOU 2560  C   GLN B 524    10417   9200   7343  -2361   1543  -1111       C  
-ATOM   2561  O   GLN B 524     -18.933  -5.753   8.724  1.00 75.17           O  
-ANISOU 2561  O   GLN B 524    10982   9702   7877  -2392   1546  -1095       O  
-ATOM   2562  CB  GLN B 524     -17.678  -6.955  11.628  1.00 86.79           C  
-ANISOU 2562  CB  GLN B 524    12810  11025   9140  -2281   1617  -1048       C  
-ATOM   2563  CG  GLN B 524     -17.747  -8.164  12.544  1.00 89.83           C  
-ANISOU 2563  CG  GLN B 524    13495  11298   9338  -2360   1687  -1042       C  
-ATOM   2564  CD  GLN B 524     -17.683  -7.796  14.010  1.00 89.48           C  
-ANISOU 2564  CD  GLN B 524    13379  11340   9280  -2356   1677  -1083       C  
-ATOM   2565  OE1 GLN B 524     -18.530  -7.061  14.517  1.00 92.47           O  
-ANISOU 2565  OE1 GLN B 524    13552  11873   9708  -2486   1666  -1168       O  
-ATOM   2566  NE2 GLN B 524     -16.680  -8.315  14.705  1.00 88.25           N  
-ANISOU 2566  NE2 GLN B 524    13391  11091   9048  -2203   1682  -1026       N  
-ATOM   2567  N   LEU B 525     -18.152  -4.359  10.301  1.00 54.97           N  
-ANISOU 2567  N   LEU B 525     8162   7272   5454  -2225   1476  -1118       N  
-ATOM   2568  CA  LEU B 525     -17.663  -3.408   9.312  1.00 55.31           C  
-ANISOU 2568  CA  LEU B 525     8010   7359   5645  -2082   1402  -1091       C  
-ATOM   2569  C   LEU B 525     -16.212  -3.765   8.981  1.00 66.17           C  
-ANISOU 2569  C   LEU B 525     9501   8616   7025  -1856   1391   -979       C  
-ATOM   2570  O   LEU B 525     -15.391  -3.946   9.886  1.00 71.88           O  
-ANISOU 2570  O   LEU B 525    10294   9301   7716  -1746   1396   -947       O  
-ATOM   2571  CB  LEU B 525     -17.820  -1.957   9.779  1.00 53.41           C  
-ANISOU 2571  CB  LEU B 525     7473   7273   5546  -2052   1332  -1161       C  
-ATOM   2572  CG  LEU B 525     -19.237  -1.498  10.099  1.00 48.44           C  
-ANISOU 2572  CG  LEU B 525     6708   6780   4918  -2254   1336  -1280       C  
-ATOM   2573  CD1 LEU B 525     -19.354   0.010  10.119  1.00 36.17           C  
-ANISOU 2573  CD1 LEU B 525     4867   5359   3515  -2192   1251  -1349       C  
-ATOM   2574  CD2 LEU B 525     -20.225  -2.072   9.115  1.00 59.40           C  
-ANISOU 2574  CD2 LEU B 525     8171   8163   6236  -2413   1365  -1299       C  
-ATOM   2575  N   ALA B 526     -15.909  -3.897   7.688  1.00 60.70           N  
-ANISOU 2575  N   ALA B 526     8828   7875   6360  -1786   1376   -924       N  
-ATOM   2576  CA  ALA B 526     -14.600  -4.382   7.247  1.00 57.64           C  
-ANISOU 2576  CA  ALA B 526     8568   7376   5957  -1581   1375   -818       C  
-ATOM   2577  C   ALA B 526     -13.993  -3.526   6.139  1.00 55.05           C  
-ANISOU 2577  C   ALA B 526     8058   7098   5761  -1435   1305   -772       C  
-ATOM   2578  O   ALA B 526     -14.689  -3.085   5.225  1.00 47.65           O  
-ANISOU 2578  O   ALA B 526     7003   6224   4878  -1511   1279   -803       O  
-ATOM   2579  CB  ALA B 526     -14.705  -5.830   6.789  1.00 60.59           C  
-ANISOU 2579  CB  ALA B 526     9243   7599   6178  -1637   1452   -783       C  
-ATOM   2580  N   ILE B 527     -12.687  -3.306   6.237  1.00 65.27           N  
-ANISOU 2580  N   ILE B 527     9334   8371   7095  -1223   1272   -698       N  
-ATOM   2581  CA  ILE B 527     -11.916  -2.652   5.189  1.00 63.03           C  
-ANISOU 2581  CA  ILE B 527     8914   8121   6915  -1067   1211   -635       C  
-ATOM   2582  C   ILE B 527     -10.768  -3.565   4.773  1.00 68.52           C  
-ANISOU 2582  C   ILE B 527     9796   8704   7535   -897   1239   -534       C  
-ATOM   2583  O   ILE B 527      -9.778  -3.713   5.494  1.00 68.13           O  
-ANISOU 2583  O   ILE B 527     9802   8627   7456   -754   1235   -492       O  
-ATOM   2584  CB  ILE B 527     -11.374  -1.282   5.644  1.00 62.41           C  
-ANISOU 2584  CB  ILE B 527     8590   8154   6970   -965   1132   -646       C  
-ATOM   2585  CG1 ILE B 527     -12.451  -0.210   5.473  1.00 70.19           C  
-ANISOU 2585  CG1 ILE B 527     9367   9251   8051  -1094   1086   -737       C  
-ATOM   2586  CG2 ILE B 527     -10.133  -0.901   4.856  1.00 54.50           C  
-ANISOU 2586  CG2 ILE B 527     7519   7156   6032   -760   1083   -551       C  
-ATOM   2587  CD1 ILE B 527     -11.958   1.195   5.723  1.00 68.14           C  
-ANISOU 2587  CD1 ILE B 527     8881   9084   7923   -996   1003   -755       C  
-ATOM   2588  N   VAL B 528     -10.923  -4.193   3.612  1.00 73.08           N  
-ANISOU 2588  N   VAL B 528    10472   9223   8073   -912   1266   -503       N  
-ATOM   2589  CA  VAL B 528      -9.935  -5.130   3.096  1.00 63.53           C  
-ANISOU 2589  CA  VAL B 528     9453   7905   6782   -757   1298   -417       C  
-ATOM   2590  C   VAL B 528      -8.960  -4.420   2.167  1.00 55.83           C  
-ANISOU 2590  C   VAL B 528     8310   6995   5908   -574   1235   -342       C  
-ATOM   2591  O   VAL B 528      -9.368  -3.651   1.298  1.00 52.32           O  
-ANISOU 2591  O   VAL B 528     7683   6636   5559   -614   1191   -352       O  
-ATOM   2592  CB  VAL B 528     -10.607  -6.271   2.314  1.00 56.81           C  
-ANISOU 2592  CB  VAL B 528     8815   6950   5818   -876   1368   -427       C  
-ATOM   2593  CG1 VAL B 528      -9.623  -7.406   2.087  1.00 62.12           C  
-ANISOU 2593  CG1 VAL B 528     9741   7486   6375   -721   1414   -353       C  
-ATOM   2594  CG2 VAL B 528     -11.835  -6.770   3.056  1.00 52.76           C  
-ANISOU 2594  CG2 VAL B 528     8420   6406   5221  -1108   1422   -512       C  
-ATOM   2595  N   THR B 529      -7.671  -4.675   2.359  1.00 38.98           N  
-ANISOU 2595  N   THR B 529     6240   4827   3744   -371   1229   -268       N  
-ATOM   2596  CA  THR B 529      -6.643  -4.102   1.501  1.00 38.24           C  
-ANISOU 2596  CA  THR B 529     6003   4797   3727   -191   1175   -188       C  
-ATOM   2597  C   THR B 529      -5.563  -5.137   1.224  1.00 40.54           C  
-ANISOU 2597  C   THR B 529     6497   4997   3910    -10   1212   -112       C  
-ATOM   2598  O   THR B 529      -5.607  -6.247   1.754  1.00 40.01           O  
-ANISOU 2598  O   THR B 529     6685   4808   3709    -19   1275   -121       O  
-ATOM   2599  CB  THR B 529      -5.989  -2.859   2.137  1.00 45.64           C  
-ANISOU 2599  CB  THR B 529     6715   5852   4775   -101   1099   -179       C  
-ATOM   2600  OG1 THR B 529      -5.130  -3.261   3.211  1.00 49.76           O  
-ANISOU 2600  OG1 THR B 529     7344   6341   5223     18   1111   -159       O  
-ATOM   2601  CG2 THR B 529      -7.048  -1.902   2.661  1.00 46.12           C  
-ANISOU 2601  CG2 THR B 529     6609   5990   4924   -271   1068   -270       C  
-ATOM   2602  N   GLN B 530      -4.595  -4.768   0.393  1.00 38.06           N  
-ANISOU 2602  N   GLN B 530     6072   4743   3647    157   1171    -35       N  
-ATOM   2603  CA  GLN B 530      -3.486  -5.657   0.080  1.00 47.49           C  
-ANISOU 2603  CA  GLN B 530     7432   5871   4740    352   1199     38       C  
-ATOM   2604  C   GLN B 530      -2.689  -5.969   1.338  1.00 40.03           C  
-ANISOU 2604  C   GLN B 530     6595   4896   3718    476   1203     49       C  
-ATOM   2605  O   GLN B 530      -2.714  -5.206   2.303  1.00 42.89           O  
-ANISOU 2605  O   GLN B 530     6828   5329   4138    447   1164     18       O  
-ATOM   2606  CB  GLN B 530      -2.570  -5.025  -0.969  1.00 48.44           C  
-ANISOU 2606  CB  GLN B 530     7369   6096   4938    505   1145    117       C  
-ATOM   2607  CG  GLN B 530      -2.036  -3.657  -0.572  1.00 49.40           C  
-ANISOU 2607  CG  GLN B 530     7226   6360   5183    560   1061    137       C  
-ATOM   2608  CD  GLN B 530      -0.878  -3.207  -1.440  1.00 46.97           C  
-ANISOU 2608  CD  GLN B 530     6781   6149   4916    738   1013    232       C  
-ATOM   2609  OE1 GLN B 530      -0.791  -2.040  -1.823  1.00 50.90           O  
-ANISOU 2609  OE1 GLN B 530     7048   6762   5532    725    945    257       O  
-ATOM   2610  NE2 GLN B 530       0.019  -4.134  -1.756  1.00 40.98           N  
-ANISOU 2610  NE2 GLN B 530     6175   5344   4052    907   1047    287       N  
-ATOM   2611  N   TRP B 531      -1.988  -7.096   1.330  1.00 59.53           N  
-ANISOU 2611  N   TRP B 531     9305   7264   6051    618   1249     90       N  
-ATOM   2612  CA  TRP B 531      -1.089  -7.430   2.426  1.00 73.03           C  
-ANISOU 2612  CA  TRP B 531    11120   8954   7673    773   1248    110       C  
-ATOM   2613  C   TRP B 531       0.303  -6.876   2.146  1.00 67.07           C  
-ANISOU 2613  C   TRP B 531    10209   8319   6957   1003   1189    186       C  
-ATOM   2614  O   TRP B 531       0.859  -7.085   1.068  1.00 67.56           O  
-ANISOU 2614  O   TRP B 531    10266   8392   7012   1115   1189    242       O  
-ATOM   2615  CB  TRP B 531      -1.031  -8.943   2.647  1.00 79.42           C  
-ANISOU 2615  CB  TRP B 531    12288   9589   8298    821   1326    114       C  
-ATOM   2616  CG  TRP B 531       0.081  -9.353   3.561  1.00 78.67           C  
-ANISOU 2616  CG  TRP B 531    12308   9483   8100   1031   1321    150       C  
-ATOM   2617  CD1 TRP B 531       1.214 -10.032   3.219  1.00 84.02           C  
-ANISOU 2617  CD1 TRP B 531    13118  10130   8678   1268   1331    215       C  
-ATOM   2618  CD2 TRP B 531       0.179  -9.090   4.965  1.00 79.62           C  
-ANISOU 2618  CD2 TRP B 531    12413   9637   8203   1031   1301    121       C  
-ATOM   2619  NE1 TRP B 531       2.006 -10.217   4.325  1.00 90.10           N  
-ANISOU 2619  NE1 TRP B 531    13957  10912   9364   1418   1318    228       N  
-ATOM   2620  CE2 TRP B 531       1.395  -9.646   5.410  1.00 87.40           C  
-ANISOU 2620  CE2 TRP B 531    13526  10611   9072   1274   1300    171       C  
-ATOM   2621  CE3 TRP B 531      -0.644  -8.440   5.890  1.00 89.96           C  
-ANISOU 2621  CE3 TRP B 531    13610  10995   9577    852   1286     52       C  
-ATOM   2622  CZ2 TRP B 531       1.806  -9.575   6.739  1.00100.63           C  
-ANISOU 2622  CZ2 TRP B 531    15218  12324  10695   1341   1282    157       C  
-ATOM   2623  CZ3 TRP B 531      -0.234  -8.370   7.208  1.00 99.45           C  
-ANISOU 2623  CZ3 TRP B 531    14827  12231  10729    915   1269     37       C  
-ATOM   2624  CH2 TRP B 531       0.980  -8.934   7.621  1.00103.68           C  
-ANISOU 2624  CH2 TRP B 531    15489  12756  11149   1155   1267     89       C  
-ATOM   2625  N   CYS B 532       0.864  -6.167   3.120  1.00 64.97           N  
-ANISOU 2625  N   CYS B 532     9812   8150   6726   1066   1138    183       N  
-ATOM   2626  CA  CYS B 532       2.160  -5.522   2.940  1.00 66.96           C  
-ANISOU 2626  CA  CYS B 532     9891   8537   7013   1262   1076    249       C  
-ATOM   2627  C   CYS B 532       3.298  -6.230   3.665  1.00 73.22           C  
-ANISOU 2627  C   CYS B 532    10837   9316   7669   1481   1085    284       C  
-ATOM   2628  O   CYS B 532       3.232  -6.466   4.872  1.00 80.92           O  
-ANISOU 2628  O   CYS B 532    11904  10261   8579   1473   1095    245       O  
-ATOM   2629  CB  CYS B 532       2.100  -4.059   3.383  1.00 67.66           C  
-ANISOU 2629  CB  CYS B 532     9690   8773   7244   1184   1002    225       C  
-ATOM   2630  SG  CYS B 532       1.760  -2.902   2.045  1.00 76.68           S  
-ANISOU 2630  SG  CYS B 532    10567  10014   8552   1093    950    252       S  
-ATOM   2631  N   GLU B 533       4.344  -6.557   2.913  1.00 61.56           N  
-ANISOU 2631  N   GLU B 533     9377   7871   6140   1683   1079    356       N  
-ATOM   2632  CA  GLU B 533       5.558  -7.122   3.484  1.00 73.33           C  
-ANISOU 2632  CA  GLU B 533    10979   9380   7502   1922   1077    395       C  
-ATOM   2633  C   GLU B 533       6.376  -6.019   4.145  1.00 75.19           C  
-ANISOU 2633  C   GLU B 533    10968   9801   7800   1993    998    406       C  
-ATOM   2634  O   GLU B 533       6.096  -4.835   3.960  1.00 76.21           O  
-ANISOU 2634  O   GLU B 533    10848  10037   8072   1872    945    395       O  
-ATOM   2635  CB  GLU B 533       6.390  -7.807   2.398  1.00 99.20           C  
-ANISOU 2635  CB  GLU B 533    14345  12646  10703   2114   1097    464       C  
-ATOM   2636  CG  GLU B 533       5.704  -8.990   1.732  1.00112.40           C  
-ANISOU 2636  CG  GLU B 533    16286  14132  12288   2062   1177    451       C  
-ATOM   2637  CD  GLU B 533       5.458 -10.137   2.692  1.00120.08           C  
-ANISOU 2637  CD  GLU B 533    17581  14940  13105   2076   1238    418       C  
-ATOM   2638  OE1 GLU B 533       4.331 -10.244   3.214  1.00117.25           O  
-ANISOU 2638  OE1 GLU B 533    17303  14488  12759   1866   1269    358       O  
-ATOM   2639  OE2 GLU B 533       6.393 -10.931   2.926  1.00126.59           O  
-ANISOU 2639  OE2 GLU B 533    18580  15732  13786   2298   1256    454       O  
-ATOM   2640  N   GLY B 534       7.384  -6.410   4.918  1.00 85.26           N  
-ANISOU 2640  N   GLY B 534    12320  11115   8960   2188    989    425       N  
-ATOM   2641  CA  GLY B 534       8.269  -5.453   5.560  1.00 83.41           C  
-ANISOU 2641  CA  GLY B 534    11866  11066   8760   2268    915    434       C  
-ATOM   2642  C   GLY B 534       7.612  -4.662   6.675  1.00 83.42           C  
-ANISOU 2642  C   GLY B 534    11754  11106   8837   2094    888    356       C  
-ATOM   2643  O   GLY B 534       6.467  -4.921   7.047  1.00 76.59           O  
-ANISOU 2643  O   GLY B 534    10991  10122   7987   1920    930    297       O  
-ATOM   2644  N   SER B 535       8.344  -3.690   7.211  1.00 95.04           N  
-ANISOU 2644  N   SER B 535    13013  12750  10348   2137    818    353       N  
-ATOM   2645  CA  SER B 535       7.843  -2.863   8.302  1.00 90.33           C  
-ANISOU 2645  CA  SER B 535    12291  12209   9820   1987    788    270       C  
-ATOM   2646  C   SER B 535       7.670  -1.414   7.858  1.00 80.01           C  
-ANISOU 2646  C   SER B 535    10706  11020   8676   1849    724    257       C  
-ATOM   2647  O   SER B 535       8.070  -1.045   6.754  1.00 76.39           O  
-ANISOU 2647  O   SER B 535    10148  10615   8262   1883    697    325       O  
-ATOM   2648  CB  SER B 535       8.786  -2.937   9.507  1.00 86.71           C  
-ANISOU 2648  CB  SER B 535    11837  11850   9259   2136    763    252       C  
-ATOM   2649  OG  SER B 535       8.857  -4.255  10.023  1.00 88.64           O  
-ANISOU 2649  OG  SER B 535    12358  11975   9348   2252    823    259       O  
-ATOM   2650  N   SER B 536       7.073  -0.597   8.722  1.00 70.21           N  
-ANISOU 2650  N   SER B 536     9346   9816   7514   1692    700    168       N  
-ATOM   2651  CA  SER B 536       6.855   0.813   8.415  1.00 64.93           C  
-ANISOU 2651  CA  SER B 536     8436   9241   6994   1550    642    140       C  
-ATOM   2652  C   SER B 536       8.174   1.573   8.394  1.00 63.77           C  
-ANISOU 2652  C   SER B 536     8132   9264   6833   1662    574    175       C  
-ATOM   2653  O   SER B 536       9.206   1.060   8.829  1.00 60.87           O  
-ANISOU 2653  O   SER B 536     7820   8962   6344   1845    568    206       O  
-ATOM   2654  CB  SER B 536       5.908   1.454   9.433  1.00 46.69           C  
-ANISOU 2654  CB  SER B 536     6052   6924   4764   1366    638     19       C  
-ATOM   2655  OG  SER B 536       6.572   1.706  10.660  1.00 54.13           O  
-ANISOU 2655  OG  SER B 536     6943   7966   5659   1429    609    -37       O  
-ATOM   2656  N   LEU B 537       8.133   2.799   7.887  1.00 53.85           N  
-ANISOU 2656  N   LEU B 537     6692   8076   5693   1544    528    167       N  
-ATOM   2657  CA  LEU B 537       9.316   3.645   7.841  1.00 51.37           C  
-ANISOU 2657  CA  LEU B 537     6234   7917   5367   1603    473    187       C  
-ATOM   2658  C   LEU B 537       9.740   4.006   9.257  1.00 53.84           C  
-ANISOU 2658  C   LEU B 537     6486   8316   5655   1618    448     89       C  
-ATOM   2659  O   LEU B 537      10.904   4.311   9.514  1.00 61.60           O  
-ANISOU 2659  O   LEU B 537     7398   9434   6573   1721    415     99       O  
-ATOM   2660  CB  LEU B 537       9.033   4.911   7.034  1.00 52.61           C  
-ANISOU 2660  CB  LEU B 537     6242   8086   5663   1443    448    184       C  
-ATOM   2661  CG  LEU B 537      10.250   5.764   6.686  1.00 46.14           C  
-ANISOU 2661  CG  LEU B 537     5297   7399   4834   1482    415    219       C  
-ATOM   2662  CD1 LEU B 537      11.263   4.936   5.918  1.00 42.86           C  
-ANISOU 2662  CD1 LEU B 537     4955   7058   4272   1673    419    347       C  
-ATOM   2663  CD2 LEU B 537       9.832   6.983   5.883  1.00 43.36           C  
-ANISOU 2663  CD2 LEU B 537     4828   7008   4640   1314    412    215       C  
-ATOM   2664  N   TYR B 538       8.777   3.968  10.172  1.00 61.42           N  
-ANISOU 2664  N   TYR B 538     7471   9204   6660   1509    468    -10       N  
-ATOM   2665  CA  TYR B 538       9.034   4.226  11.581  1.00 60.86           C  
-ANISOU 2665  CA  TYR B 538     7350   9207   6566   1516    450   -113       C  
-ATOM   2666  C   TYR B 538       9.964   3.160  12.141  1.00 59.60           C  
-ANISOU 2666  C   TYR B 538     7315   9098   6232   1735    462    -65       C  
-ATOM   2667  O   TYR B 538      10.994   3.468  12.739  1.00 65.43           O  
-ANISOU 2667  O   TYR B 538     7973   9977   6911   1833    425    -86       O  
-ATOM   2668  CB  TYR B 538       7.717   4.230  12.359  1.00 55.73           C  
-ANISOU 2668  CB  TYR B 538     6725   8465   5983   1357    479   -219       C  
-ATOM   2669  CG  TYR B 538       7.835   4.769  13.764  1.00 63.32           C  
-ANISOU 2669  CG  TYR B 538     7593   9511   6956   1322    454   -345       C  
-ATOM   2670  CD1 TYR B 538       7.747   6.132  14.011  1.00 65.31           C  
-ANISOU 2670  CD1 TYR B 538     7658   9814   7344   1192    412   -449       C  
-ATOM   2671  CD2 TYR B 538       8.029   3.917  14.843  1.00 72.39           C  
-ANISOU 2671  CD2 TYR B 538     8851  10676   7978   1420    478   -366       C  
-ATOM   2672  CE1 TYR B 538       7.853   6.632  15.293  1.00 75.36           C  
-ANISOU 2672  CE1 TYR B 538     8839  11162   8631   1160    389   -577       C  
-ATOM   2673  CE2 TYR B 538       8.136   4.408  16.130  1.00 74.51           C  
-ANISOU 2673  CE2 TYR B 538     9024  11034   8251   1389    454   -485       C  
-ATOM   2674  CZ  TYR B 538       8.047   5.768  16.349  1.00 74.26           C  
-ANISOU 2674  CZ  TYR B 538     8791  11062   8361   1258    409   -593       C  
-ATOM   2675  OH  TYR B 538       8.152   6.268  17.626  1.00 73.96           O  
-ANISOU 2675  OH  TYR B 538     8654  11113   8333   1226    386   -723       O  
-ATOM   2676  N   HIS B 539       9.591   1.902  11.935  1.00 61.26           N  
-ANISOU 2676  N   HIS B 539     7733   9185   6358   1811    519     -7       N  
-ATOM   2677  CA  HIS B 539      10.384   0.770  12.396  1.00 67.43           C  
-ANISOU 2677  CA  HIS B 539     8677   9974   6969   2029    543     40       C  
-ATOM   2678  C   HIS B 539      11.799   0.809  11.824  1.00 59.41           C  
-ANISOU 2678  C   HIS B 539     7604   9095   5875   2221    504    127       C  
-ATOM   2679  O   HIS B 539      12.776   0.635  12.550  1.00 57.96           O  
-ANISOU 2679  O   HIS B 539     7413   9029   5581   2376    483    123       O  
-ATOM   2680  CB  HIS B 539       9.700  -0.542  12.004  1.00 80.66           C  
-ANISOU 2680  CB  HIS B 539    10608  11460   8580   2057    620     88       C  
-ATOM   2681  CG  HIS B 539      10.414  -1.768  12.484  1.00 82.48           C  
-ANISOU 2681  CG  HIS B 539    11046  11662   8630   2276    655    130       C  
-ATOM   2682  ND1 HIS B 539      11.669  -2.122  12.035  1.00 78.17           N  
-ANISOU 2682  ND1 HIS B 539    10515  11202   7985   2505    637    212       N  
-ATOM   2683  CD2 HIS B 539      10.041  -2.730  13.358  1.00 86.18           C  
-ANISOU 2683  CD2 HIS B 539    11728  12027   8991   2302    708    102       C  
-ATOM   2684  CE1 HIS B 539      12.041  -3.245  12.621  1.00 88.16           C  
-ANISOU 2684  CE1 HIS B 539    11993  12411   9093   2673    678    229       C  
-ATOM   2685  NE2 HIS B 539      11.073  -3.637  13.428  1.00 91.58           N  
-ANISOU 2685  NE2 HIS B 539    12556  12725   9516   2551    721    166       N  
-ATOM   2686  N   HIS B 540      11.900   1.038  10.518  1.00 60.47           N  
-ANISOU 2686  N   HIS B 540     7694   9224   6056   2209    494    205       N  
-ATOM   2687  CA  HIS B 540      13.190   1.015   9.835  1.00 67.56           C  
-ANISOU 2687  CA  HIS B 540     8548  10253   6867   2382    462    296       C  
-ATOM   2688  C   HIS B 540      14.099   2.175  10.233  1.00 78.19           C  
-ANISOU 2688  C   HIS B 540     9688  11800   8219   2358    399    255       C  
-ATOM   2689  O   HIS B 540      15.323   2.043  10.227  1.00 85.29           O  
-ANISOU 2689  O   HIS B 540    10562  12846   8999   2528    375    301       O  
-ATOM   2690  CB  HIS B 540      12.995   0.996   8.317  1.00 66.44           C  
-ANISOU 2690  CB  HIS B 540     8410  10060   6774   2353    471    387       C  
-ATOM   2691  CG  HIS B 540      12.506  -0.315   7.787  1.00 68.90           C  
-ANISOU 2691  CG  HIS B 540     8940  10199   7041   2440    538    436       C  
-ATOM   2692  ND1 HIS B 540      13.349  -1.376   7.534  1.00 70.52           N  
-ANISOU 2692  ND1 HIS B 540     9285  10404   7107   2681    563    504       N  
-ATOM   2693  CD2 HIS B 540      11.262  -0.737   7.455  1.00 73.41           C  
-ANISOU 2693  CD2 HIS B 540     9621  10589   7681   2312    593    414       C  
-ATOM   2694  CE1 HIS B 540      12.646  -2.395   7.073  1.00 77.83           C  
-ANISOU 2694  CE1 HIS B 540    10411  11141   8019   2691    634    516       C  
-ATOM   2695  NE2 HIS B 540      11.376  -2.033   7.015  1.00 74.78           N  
-ANISOU 2695  NE2 HIS B 540    10011  10649   7755   2462    652    464       N  
-ATOM   2696  N   LEU B 541      13.499   3.309  10.576  1.00 90.06           N  
-ANISOU 2696  N   LEU B 541    11052  13305   9863   2146    380    159       N  
-ATOM   2697  CA  LEU B 541      14.267   4.488  10.955  1.00 84.94           C  
-ANISOU 2697  CA  LEU B 541    10216  12809   9248   2093    338     95       C  
-ATOM   2698  C   LEU B 541      14.590   4.512  12.444  1.00 83.47           C  
-ANISOU 2698  C   LEU B 541     9996  12706   9011   2141    320     -6       C  
-ATOM   2699  O   LEU B 541      15.677   4.930  12.845  1.00 80.19           O  
-ANISOU 2699  O   LEU B 541     9479  12454   8535   2217    290    -29       O  
-ATOM   2700  CB  LEU B 541      13.515   5.763  10.569  1.00 58.01           C  
-ANISOU 2700  CB  LEU B 541     6674   9335   6033   1852    333     31       C  
-ATOM   2701  CG  LEU B 541      13.901   6.409   9.239  1.00 62.04           C  
-ANISOU 2701  CG  LEU B 541     7111   9864   6598   1804    335    109       C  
-ATOM   2702  CD1 LEU B 541      14.074   5.361   8.149  1.00 69.82           C  
-ANISOU 2702  CD1 LEU B 541     8227  10831   7470   1936    356    251       C  
-ATOM   2703  CD2 LEU B 541      12.873   7.454   8.835  1.00 57.06           C  
-ANISOU 2703  CD2 LEU B 541     6397   9111   6171   1579    342     56       C  
-ATOM   2704  N   HIS B 542      13.647   4.054  13.260  1.00 69.67           N  
-ANISOU 2704  N   HIS B 542     8334  10854   7284   2092    344    -68       N  
-ATOM   2705  CA  HIS B 542      13.759   4.210  14.707  1.00 77.21           C  
-ANISOU 2705  CA  HIS B 542     9241  11882   8213   2097    331   -179       C  
-ATOM   2706  C   HIS B 542      14.004   2.901  15.459  1.00 86.39           C  
-ANISOU 2706  C   HIS B 542    10579  13035   9209   2288    361   -147       C  
-ATOM   2707  O   HIS B 542      14.957   2.791  16.229  1.00 82.55           O  
-ANISOU 2707  O   HIS B 542    10060  12692   8612   2429    339   -165       O  
-ATOM   2708  CB  HIS B 542      12.516   4.915  15.259  1.00 74.63           C  
-ANISOU 2708  CB  HIS B 542     8849  11465   8041   1869    336   -304       C  
-ATOM   2709  CG  HIS B 542      12.175   6.186  14.534  1.00 71.70           C  
-ANISOU 2709  CG  HIS B 542     8331  11066   7845   1686    316   -342       C  
-ATOM   2710  ND1 HIS B 542      13.130   7.064  14.089  1.00 64.90           N  
-ANISOU 2710  ND1 HIS B 542     7338  10306   7016   1690    286   -335       N  
-ATOM   2711  CD2 HIS B 542      10.975   6.717  14.194  1.00 62.79           C  
-ANISOU 2711  CD2 HIS B 542     7178   9811   6869   1495    330   -388       C  
-ATOM   2712  CE1 HIS B 542      12.538   8.092  13.494  1.00 54.47           C  
-ANISOU 2712  CE1 HIS B 542     5927   8900   5870   1513    286   -372       C  
-ATOM   2713  NE2 HIS B 542      11.236   7.903  13.546  1.00 57.47           N  
-ANISOU 2713  NE2 HIS B 542     6367   9147   6320   1399    308   -405       N  
-ATOM   2714  N   ALA B 543      13.140   1.915  15.239  1.00104.06           N  
-ANISOU 2714  N   ALA B 543    13012  15099  11429   2288    418   -103       N  
-ATOM   2715  CA  ALA B 543      13.221   0.654  15.970  1.00 90.66           C  
-ANISOU 2715  CA  ALA B 543    11521  13346   9580   2442    464    -82       C  
-ATOM   2716  C   ALA B 543      14.074  -0.372  15.236  1.00 91.68           C  
-ANISOU 2716  C   ALA B 543    11800  13461   9572   2680    484     43       C  
-ATOM   2717  O   ALA B 543      13.845  -1.578  15.349  1.00101.74           O  
-ANISOU 2717  O   ALA B 543    13312  14602  10743   2781    544     82       O  
-ATOM   2718  CB  ALA B 543      11.829   0.101  16.228  1.00 47.45           C  
-ANISOU 2718  CB  ALA B 543     6205   7680   4143   2299    525   -117       C  
-ATOM   2719  N   SER B 544      15.058   0.109  14.486  1.00 66.21           N  
-ANISOU 2719  N   SER B 544     8446  10372   6339   2764    438    100       N  
-ATOM   2720  CA  SER B 544      15.916  -0.780  13.717  1.00 75.31           C  
-ANISOU 2720  CA  SER B 544     9716  11533   7367   2996    452    215       C  
-ATOM   2721  C   SER B 544      17.378  -0.351  13.749  1.00 87.02           C  
-ANISOU 2721  C   SER B 544    11050  13257   8757   3153    393    242       C  
-ATOM   2722  O   SER B 544      17.698   0.818  13.973  1.00 82.54           O  
-ANISOU 2722  O   SER B 544    10273  12839   8251   3038    341    182       O  
-ATOM   2723  CB  SER B 544      15.428  -0.885  12.271  1.00 84.42           C  
-ANISOU 2723  CB  SER B 544    10910  12568   8598   2933    473    290       C  
-ATOM   2724  OG  SER B 544      16.241  -1.770  11.522  1.00 85.08           O  
-ANISOU 2724  OG  SER B 544    11107  12656   8563   3163    490    391       O  
-ATOM   2725  N   GLU B 545      18.256  -1.321  13.524  1.00125.06           N  
-ANISOU 2725  N   GLU B 545    15990  18106  13422   3413    410    323       N  
-ATOM   2726  CA  GLU B 545      19.692  -1.095  13.492  1.00146.54           C  
-ANISOU 2726  CA  GLU B 545    18590  21064  16023   3591    359    360       C  
-ATOM   2727  C   GLU B 545      20.177  -1.117  12.046  1.00146.25           C  
-ANISOU 2727  C   GLU B 545    18535  21061  15973   3652    348    465       C  
-ATOM   2728  O   GLU B 545      21.366  -0.954  11.771  1.00150.05           O  
-ANISOU 2728  O   GLU B 545    18926  21735  16351   3771    339    488       O  
-ATOM   2729  CB  GLU B 545      20.412  -2.161  14.326  1.00173.35           C  
-ANISOU 2729  CB  GLU B 545    22127  24498  19239   3864    385    373       C  
-ATOM   2730  CG  GLU B 545      20.137  -2.072  15.826  1.00183.23           C  
-ANISOU 2730  CG  GLU B 545    23376  25771  20473   3818    388    273       C  
-ATOM   2731  CD  GLU B 545      20.811  -3.177  16.627  1.00197.81           C  
-ANISOU 2731  CD  GLU B 545    25387  27646  22127   4088    421    292       C  
-ATOM   2732  OE1 GLU B 545      21.352  -4.123  16.017  1.00205.71           O  
-ANISOU 2732  OE1 GLU B 545    26538  28606  23015   4310    453    378       O  
-ATOM   2733  OE2 GLU B 545      20.795  -3.098  17.874  1.00201.43           O  
-ANISOU 2733  OE2 GLU B 545    25826  28167  22541   4079    417    217       O  
-ATOM   2734  N   THR B 546      19.240  -1.330  11.127  1.00153.86           N  
-ANISOU 2734  N   THR B 546    19585  21836  17041   3541    385    500       N  
-ATOM   2735  CA  THR B 546      19.524  -1.267   9.699  1.00145.45           C  
-ANISOU 2735  CA  THR B 546    18492  20783  15989   3533    410    564       C  
-ATOM   2736  C   THR B 546      19.334   0.160   9.202  1.00136.62           C  
-ANISOU 2736  C   THR B 546    17167  19751  14993   3282    369    542       C  
-ATOM   2737  O   THR B 546      18.215   0.673   9.153  1.00131.13           O  
-ANISOU 2737  O   THR B 546    16452  18937  14435   3077    350    519       O  
-ATOM   2738  CB  THR B 546      18.615  -2.214   8.893  1.00 95.93           C  
-ANISOU 2738  CB  THR B 546    12416  14269   9764   3541    471    610       C  
-ATOM   2739  OG1 THR B 546      18.937  -3.573   9.214  1.00 92.79           O  
-ANISOU 2739  OG1 THR B 546    12242  13784   9230   3793    519    635       O  
-ATOM   2740  CG2 THR B 546      18.802  -1.993   7.398  1.00 89.46           C  
-ANISOU 2740  CG2 THR B 546    11536  13474   8980   3488    501    659       C  
-ATOM   2741  N   LYS B 547      20.440   0.800   8.840  1.00123.23           N  
-ANISOU 2741  N   LYS B 547    15325  18259  13236   3305    358    551       N  
-ATOM   2742  CA  LYS B 547      20.412   2.192   8.420  1.00110.37           C  
-ANISOU 2742  CA  LYS B 547    13518  16716  11700   3083    324    532       C  
-ATOM   2743  C   LYS B 547      20.538   2.315   6.905  1.00109.37           C  
-ANISOU 2743  C   LYS B 547    13366  16580  11607   3041    366    607       C  
-ATOM   2744  O   LYS B 547      21.383   1.669   6.284  1.00116.70           O  
-ANISOU 2744  O   LYS B 547    14325  17583  12433   3215    405    660       O  
-ATOM   2745  CB  LYS B 547      21.519   2.978   9.127  1.00 81.77           C  
-ANISOU 2745  CB  LYS B 547     9745  13331   7993   3108    279    484       C  
-ATOM   2746  CG  LYS B 547      21.371   3.025  10.643  1.00 85.92           C  
-ANISOU 2746  CG  LYS B 547    10251  13867   8529   3114    255    378       C  
-ATOM   2747  CD  LYS B 547      22.551   3.732  11.292  1.00 90.52           C  
-ANISOU 2747  CD  LYS B 547    10665  14681   9046   3152    233    313       C  
-ATOM   2748  CE  LYS B 547      22.445   3.722  12.810  1.00 91.38           C  
-ANISOU 2748  CE  LYS B 547    10753  14819   9148   3172    208    208       C  
-ATOM   2749  NZ  LYS B 547      23.631   4.353  13.454  1.00 93.92           N  
-ANISOU 2749  NZ  LYS B 547    10907  15379   9400   3222    184    144       N  
-ATOM   2750  N   PHE B 548      19.683   3.143   6.315  1.00 82.40           N  
-ANISOU 2750  N   PHE B 548     9897  13079   8333   2814    356    611       N  
-ATOM   2751  CA  PHE B 548      19.680   3.332   4.871  1.00 71.41           C  
-ANISOU 2751  CA  PHE B 548     8475  11672   6987   2754    395    685       C  
-ATOM   2752  C   PHE B 548      20.760   4.309   4.436  1.00 75.29           C  
-ANISOU 2752  C   PHE B 548     8809  12362   7435   2723    385    711       C  
-ATOM   2753  O   PHE B 548      21.244   5.114   5.231  1.00 73.98           O  
-ANISOU 2753  O   PHE B 548     8513  12287   7307   2674    364    634       O  
-ATOM   2754  CB  PHE B 548      18.316   3.835   4.396  1.00 73.49           C  
-ANISOU 2754  CB  PHE B 548     8745  11764   7413   2532    390    687       C  
-ATOM   2755  CG  PHE B 548      17.211   2.838   4.567  1.00 76.08           C  
-ANISOU 2755  CG  PHE B 548     9227  11892   7787   2554    410    676       C  
-ATOM   2756  CD1 PHE B 548      16.175   3.075   5.454  1.00 81.68           C  
-ANISOU 2756  CD1 PHE B 548     9956  12491   8586   2431    381    606       C  
-ATOM   2757  CD2 PHE B 548      17.212   1.658   3.844  1.00 78.99           C  
-ANISOU 2757  CD2 PHE B 548     9721  12180   8112   2697    466    725       C  
-ATOM   2758  CE1 PHE B 548      15.156   2.155   5.612  1.00 87.77           C  
-ANISOU 2758  CE1 PHE B 548    10874  13081   9395   2449    403    602       C  
-ATOM   2759  CE2 PHE B 548      16.198   0.735   3.997  1.00 85.29           C  
-ANISOU 2759  CE2 PHE B 548    10677  12782   8946   2716    490    715       C  
-ATOM   2760  CZ  PHE B 548      15.168   0.983   4.883  1.00 90.04           C  
-ANISOU 2760  CZ  PHE B 548    11300  13280   9631   2593    455    661       C  
-ATOM   2761  N   GLU B 549      21.137   4.229   3.166  1.00 86.63           N  
-ANISOU 2761  N   GLU B 549    10219  13834   8862   2746    426    791       N  
-ATOM   2762  CA  GLU B 549      22.052   5.197   2.587  1.00 78.46           C  
-ANISOU 2762  CA  GLU B 549     9029  12964   7818   2693    427    828       C  
-ATOM   2763  C   GLU B 549      21.236   6.278   1.901  1.00 69.93           C  
-ANISOU 2763  C   GLU B 549     7849  11750   6972   2448    437    831       C  
-ATOM   2764  O   GLU B 549      20.022   6.141   1.748  1.00 69.05           O  
-ANISOU 2764  O   GLU B 549     7819  11461   6956   2343    440    827       O  
-ATOM   2765  CB  GLU B 549      23.006   4.520   1.604  1.00 74.89           C  
-ANISOU 2765  CB  GLU B 549     8577  12634   7242   2868    469    906       C  
-ATOM   2766  CG  GLU B 549      23.779   3.365   2.218  1.00 82.20           C  
-ANISOU 2766  CG  GLU B 549     9582  13639   8013   3133    479    881       C  
-ATOM   2767  CD  GLU B 549      25.109   3.119   1.537  1.00 97.69           C  
-ANISOU 2767  CD  GLU B 549    11475  15807   9835   3302    505    935       C  
-ATOM   2768  OE1 GLU B 549      25.266   3.531   0.369  1.00111.24           O  
-ANISOU 2768  OE1 GLU B 549    13117  17566  11583   3230    527   1003       O  
-ATOM   2769  OE2 GLU B 549      25.997   2.513   2.173  1.00 96.25           O  
-ANISOU 2769  OE2 GLU B 549    11312  15752   9507   3513    502    912       O  
-ATOM   2770  N   MET B 550      21.899   7.353   1.494  1.00 70.17           N  
-ANISOU 2770  N   MET B 550     7703  11861   7098   2363    437    845       N  
-ATOM   2771  CA  MET B 550      21.204   8.486   0.897  1.00 69.48           C  
-ANISOU 2771  CA  MET B 550     7515  11638   7245   2143    438    855       C  
-ATOM   2772  C   MET B 550      20.333   8.108  -0.295  1.00 70.56           C  
-ANISOU 2772  C   MET B 550     7741  11661   7406   2089    469    942       C  
-ATOM   2773  O   MET B 550      19.171   8.507  -0.367  1.00 73.77           O  
-ANISOU 2773  O   MET B 550     8165  11893   7973   1936    467    919       O  
-ATOM   2774  CB  MET B 550      22.196   9.581   0.506  1.00 64.80           C  
-ANISOU 2774  CB  MET B 550     6730  11157   6732   2092    429    885       C  
-ATOM   2775  CG  MET B 550      22.254  10.701   1.517  1.00 65.59           C  
-ANISOU 2775  CG  MET B 550     6701  11224   6996   1979    391    779       C  
-ATOM   2776  SD  MET B 550      20.610  11.391   1.767  1.00 67.79           S  
-ANISOU 2776  SD  MET B 550     7008  11227   7524   1763    383    710       S  
-ATOM   2777  CE  MET B 550      20.818  12.214   3.341  1.00 50.61           C  
-ANISOU 2777  CE  MET B 550     4725   9055   5447   1711    341    551       C  
-ATOM   2778  N   LYS B 551      20.889   7.338  -1.224  1.00 68.24           N  
-ANISOU 2778  N   LYS B 551     7500  11475   6951   2221    499   1038       N  
-ATOM   2779  CA  LYS B 551      20.171   6.998  -2.447  1.00 65.12           C  
-ANISOU 2779  CA  LYS B 551     7174  10997   6572   2177    529   1125       C  
-ATOM   2780  C   LYS B 551      18.765   6.481  -2.150  1.00 55.65           C  
-ANISOU 2780  C   LYS B 551     6113   9606   5424   2115    522   1087       C  
-ATOM   2781  O   LYS B 551      17.815   6.801  -2.862  1.00 59.60           O  
-ANISOU 2781  O   LYS B 551     6614   9981   6051   1979    530   1119       O  
-ATOM   2782  CB  LYS B 551      20.942   5.970  -3.278  1.00 68.48           C  
-ANISOU 2782  CB  LYS B 551     7650  11550   6819   2366    564   1195       C  
-ATOM   2783  CG  LYS B 551      20.619   6.047  -4.763  1.00 78.45           C  
-ANISOU 2783  CG  LYS B 551     8880  12779   8147   2300    596   1286       C  
-ATOM   2784  CD  LYS B 551      20.745   4.701  -5.458  1.00 76.67           C  
-ANISOU 2784  CD  LYS B 551     8732  12551   7846   2474    634   1290       C  
-ATOM   2785  CE  LYS B 551      20.332   4.810  -6.920  1.00 65.34           C  
-ANISOU 2785  CE  LYS B 551     7258  11086   6483   2396    660   1371       C  
-ATOM   2786  NZ  LYS B 551      20.228   3.480  -7.583  1.00 59.27           N  
-ANISOU 2786  NZ  LYS B 551     6583  10282   5654   2550    695   1363       N  
-ATOM   2787  N   LYS B 552      18.638   5.687  -1.093  1.00 43.34           N  
-ANISOU 2787  N   LYS B 552     4660   8021   3787   2219    505   1015       N  
-ATOM   2788  CA  LYS B 552      17.349   5.110  -0.728  1.00 52.71           C  
-ANISOU 2788  CA  LYS B 552     5958   9017   5052   2174    500    964       C  
-ATOM   2789  C   LYS B 552      16.492   6.101   0.054  1.00 64.66           C  
-ANISOU 2789  C   LYS B 552     7420  10429   6721   1984    470    886       C  
-ATOM   2790  O   LYS B 552      15.277   6.162  -0.131  1.00 67.58           O  
-ANISOU 2790  O   LYS B 552     7827  10646   7205   1862    470    872       O  
-ATOM   2791  CB  LYS B 552      17.545   3.822   0.075  1.00 60.21           C  
-ANISOU 2791  CB  LYS B 552     7030   9945   5902   2368    509    910       C  
-ATOM   2792  CG  LYS B 552      16.273   3.020   0.276  1.00 59.98           C  
-ANISOU 2792  CG  LYS B 552     7135   9715   5940   2347    518    875       C  
-ATOM   2793  CD  LYS B 552      16.594   1.575   0.605  1.00 59.93           C  
-ANISOU 2793  CD  LYS B 552     7279   9672   5821   2574    550    862       C  
-ATOM   2794  CE  LYS B 552      15.361   0.700   0.495  1.00 71.78           C  
-ANISOU 2794  CE  LYS B 552     8929  10962   7384   2557    575    847       C  
-ATOM   2795  NZ  LYS B 552      15.695  -0.746   0.629  1.00 81.74           N  
-ANISOU 2795  NZ  LYS B 552    10371  12159   8526   2787    619    848       N  
-ATOM   2796  N   LEU B 553      17.133   6.872   0.927  1.00 71.67           N  
-ANISOU 2796  N   LEU B 553     8195  11388   7650   1962    452    813       N  
-ATOM   2797  CA  LEU B 553      16.446   7.900   1.702  1.00 52.84           C  
-ANISOU 2797  CA  LEU B 553     5724   8896   5459   1789    433    708       C  
-ATOM   2798  C   LEU B 553      15.773   8.909   0.781  1.00 55.12           C  
-ANISOU 2798  C   LEU B 553     5928   9072   5942   1609    444    741       C  
-ATOM   2799  O   LEU B 553      14.613   9.269   0.979  1.00 61.59           O  
-ANISOU 2799  O   LEU B 553     6759   9742   6900   1476    439    687       O  
-ATOM   2800  CB  LEU B 553      17.428   8.613   2.631  1.00 37.32           C  
-ANISOU 2800  CB  LEU B 553     3632   7041   3506   1809    409    633       C  
-ATOM   2801  CG  LEU B 553      18.045   7.744   3.728  1.00 46.60           C  
-ANISOU 2801  CG  LEU B 553     4877   8327   4503   1982    392    586       C  
-ATOM   2802  CD1 LEU B 553      19.009   8.555   4.580  1.00 43.96           C  
-ANISOU 2802  CD1 LEU B 553     4396   8113   4192   1988    366    510       C  
-ATOM   2803  CD2 LEU B 553      16.958   7.120   4.592  1.00 46.81           C  
-ANISOU 2803  CD2 LEU B 553     5024   8228   4534   1967    381    516       C  
-ATOM   2804  N   ILE B 554      16.515   9.362  -0.225  1.00 43.89           N  
-ANISOU 2804  N   ILE B 554     4420   7728   4528   1613    457    835       N  
-ATOM   2805  CA  ILE B 554      15.983  10.280  -1.222  1.00 37.78           C  
-ANISOU 2805  CA  ILE B 554     3570   6855   3929   1467    466    894       C  
-ATOM   2806  C   ILE B 554      14.856   9.605  -1.995  1.00 49.78           C  
-ANISOU 2806  C   ILE B 554     5207   8273   5435   1436    485    944       C  
-ATOM   2807  O   ILE B 554      13.830  10.221  -2.279  1.00 65.14           O  
-ANISOU 2807  O   ILE B 554     7133  10077   7540   1297    484    934       O  
-ATOM   2808  CB  ILE B 554      17.068  10.720  -2.220  1.00 54.66           C  
-ANISOU 2808  CB  ILE B 554     5602   9117   6051   1499    476   1003       C  
-ATOM   2809  CG1 ILE B 554      18.338  11.164  -1.490  1.00 58.46           C  
-ANISOU 2809  CG1 ILE B 554     5973   9737   6501   1563    455    961       C  
-ATOM   2810  CG2 ILE B 554      16.542  11.827  -3.122  1.00 52.21           C  
-ANISOU 2810  CG2 ILE B 554     5200   8692   5944   1346    476   1065       C  
-ATOM   2811  CD1 ILE B 554      18.234  12.524  -0.837  1.00 58.97           C  
-ANISOU 2811  CD1 ILE B 554     5908   9716   6784   1428    423    882       C  
-ATOM   2812  N   ASP B 555      15.059   8.335  -2.332  1.00 51.59           N  
-ANISOU 2812  N   ASP B 555     5556   8572   5473   1577    501    996       N  
-ATOM   2813  CA  ASP B 555      14.067   7.558  -3.069  1.00 45.87           C  
-ANISOU 2813  CA  ASP B 555     4947   7761   4722   1569    513   1044       C  
-ATOM   2814  C   ASP B 555      12.766   7.435  -2.278  1.00 35.20           C  
-ANISOU 2814  C   ASP B 555     3660   6254   3459   1482    496    948       C  
-ATOM   2815  O   ASP B 555      11.686   7.701  -2.803  1.00 38.53           O  
-ANISOU 2815  O   ASP B 555     4086   6561   3994   1364    498    955       O  
-ATOM   2816  CB  ASP B 555      14.621   6.170  -3.405  1.00 61.13           C  
-ANISOU 2816  CB  ASP B 555     6988   9777   6461   1764    528   1091       C  
-ATOM   2817  CG  ASP B 555      13.697   5.371  -4.307  1.00 67.66           C  
-ANISOU 2817  CG  ASP B 555     7879  10489   7341   1759    554   1102       C  
-ATOM   2818  OD1 ASP B 555      13.331   5.876  -5.389  1.00 73.89           O  
-ANISOU 2818  OD1 ASP B 555     8610  11259   8205   1662    563   1169       O  
-ATOM   2819  OD2 ASP B 555      13.346   4.232  -3.937  1.00 67.76           O  
-ANISOU 2819  OD2 ASP B 555     8002  10429   7316   1858    567   1047       O  
-ATOM   2820  N   ILE B 556      12.877   7.031  -1.015  1.00 33.53           N  
-ANISOU 2820  N   ILE B 556     3496   6050   3194   1543    479    858       N  
-ATOM   2821  CA  ILE B 556      11.719   6.932  -0.131  1.00 42.95           C  
-ANISOU 2821  CA  ILE B 556     4739   7113   4468   1460    466    756       C  
-ATOM   2822  C   ILE B 556      10.985   8.265  -0.041  1.00 41.74           C  
-ANISOU 2822  C   ILE B 556     4475   6863   4521   1267    463    693       C  
-ATOM   2823  O   ILE B 556       9.756   8.309  -0.033  1.00 39.22           O  
-ANISOU 2823  O   ILE B 556     4187   6423   4291   1164    464    651       O  
-ATOM   2824  CB  ILE B 556      12.123   6.485   1.288  1.00 42.94           C  
-ANISOU 2824  CB  ILE B 556     4777   7153   4384   1553    449    669       C  
-ATOM   2825  CG1 ILE B 556      12.607   5.034   1.273  1.00 39.70           C  
-ANISOU 2825  CG1 ILE B 556     4507   6786   3790   1763    449    729       C  
-ATOM   2826  CG2 ILE B 556      10.956   6.641   2.249  1.00 37.86           C  
-ANISOU 2826  CG2 ILE B 556     4150   6389   3847   1437    442    552       C  
-ATOM   2827  CD1 ILE B 556      13.032   4.519   2.633  1.00 36.62           C  
-ANISOU 2827  CD1 ILE B 556     4168   6432   3314   1879    434    659       C  
-ATOM   2828  N   ALA B 557      11.749   9.350   0.027  1.00 48.42           N  
-ANISOU 2828  N   ALA B 557     5191   7757   5450   1230    457    687       N  
-ATOM   2829  CA  ALA B 557      11.176  10.690   0.059  1.00 38.91           C  
-ANISOU 2829  CA  ALA B 557     3880   6444   4461   1073    449    638       C  
-ATOM   2830  C   ALA B 557      10.470  10.996  -1.255  1.00 40.39           C  
-ANISOU 2830  C   ALA B 557     4063   6552   4734    995    464    731       C  
-ATOM   2831  O   ALA B 557       9.406  11.617  -1.272  1.00 48.94           O  
-ANISOU 2831  O   ALA B 557     5127   7505   5962    878    461    688       O  
-ATOM   2832  CB  ALA B 557      12.257  11.719   0.330  1.00 28.97           C  
-ANISOU 2832  CB  ALA B 557     2483   5248   3276   1070    434    626       C  
-ATOM   2833  N   ARG B 558      11.075  10.557  -2.354  1.00 33.92           N  
-ANISOU 2833  N   ARG B 558     3256   5816   3815   1068    480    857       N  
-ATOM   2834  CA  ARG B 558      10.522  10.773  -3.684  1.00 28.20           C  
-ANISOU 2834  CA  ARG B 558     2523   5042   3150   1011    493    960       C  
-ATOM   2835  C   ARG B 558       9.215  10.019  -3.879  1.00 28.03           C  
-ANISOU 2835  C   ARG B 558     2610   4931   3108    980    495    941       C  
-ATOM   2836  O   ARG B 558       8.257  10.555  -4.435  1.00 36.52           O  
-ANISOU 2836  O   ARG B 558     3665   5908   4304    880    494    954       O  
-ATOM   2837  CB  ARG B 558      11.524  10.345  -4.760  1.00 49.00           C  
-ANISOU 2837  CB  ARG B 558     5149   7810   5658   1109    510   1092       C  
-ATOM   2838  CG  ARG B 558      10.947  10.335  -6.170  1.00 51.85           C  
-ANISOU 2838  CG  ARG B 558     5516   8139   6045   1069    522   1203       C  
-ATOM   2839  CD  ARG B 558      12.038  10.204  -7.221  1.00 54.50           C  
-ANISOU 2839  CD  ARG B 558     5807   8616   6284   1148    541   1331       C  
-ATOM   2840  NE  ARG B 558      12.586   8.853  -7.308  1.00 61.42           N  
-ANISOU 2840  NE  ARG B 558     6786   9608   6943   1301    554   1352       N  
-ATOM   2841  CZ  ARG B 558      13.650   8.528  -8.037  1.00 68.82           C  
-ANISOU 2841  CZ  ARG B 558     7700  10696   7754   1404    574   1441       C  
-ATOM   2842  NH1 ARG B 558      14.286   9.460  -8.733  1.00 63.68           N  
-ANISOU 2842  NH1 ARG B 558     6917  10102   7175   1358    582   1521       N  
-ATOM   2843  NH2 ARG B 558      14.083   7.276  -8.065  1.00 72.07           N  
-ANISOU 2843  NH2 ARG B 558     8170  11170   8044   1556    595   1400       N  
-ATOM   2844  N   GLN B 559       9.183   8.770  -3.429  1.00 24.11           N  
-ANISOU 2844  N   GLN B 559     2228   4468   2464   1077    494    912       N  
-ATOM   2845  CA  GLN B 559       7.997   7.941  -3.591  1.00 29.90           C  
-ANISOU 2845  CA  GLN B 559     3060   5117   3183   1060    491    890       C  
-ATOM   2846  C   GLN B 559       6.836   8.472  -2.757  1.00 39.02           C  
-ANISOU 2846  C   GLN B 559     4205   6154   4468    930    484    767       C  
-ATOM   2847  O   GLN B 559       5.683   8.434  -3.188  1.00 35.70           O  
-ANISOU 2847  O   GLN B 559     3806   5649   4109    853    484    754       O  
-ATOM   2848  CB  GLN B 559       8.298   6.487  -3.222  1.00 20.31           C  
-ANISOU 2848  CB  GLN B 559     1967   3939   1812   1212    489    888       C  
-ATOM   2849  CG  GLN B 559       9.430   5.865  -4.021  1.00 30.37           C  
-ANISOU 2849  CG  GLN B 559     3262   5331   2947   1365    496    998       C  
-ATOM   2850  CD  GLN B 559       9.498   4.359  -3.860  1.00 41.10           C  
-ANISOU 2850  CD  GLN B 559     4729   6659   4229   1516    526    958       C  
-ATOM   2851  OE1 GLN B 559       8.473   3.681  -3.819  1.00 45.52           O  
-ANISOU 2851  OE1 GLN B 559     5369   7101   4827   1500    530    918       O  
-ATOM   2852  NE2 GLN B 559      10.711   3.827  -3.775  1.00 42.66           N  
-ANISOU 2852  NE2 GLN B 559     4940   6955   4314   1673    549    972       N  
-ATOM   2853  N   THR B 560       7.147   8.969  -1.565  1.00 42.65           N  
-ANISOU 2853  N   THR B 560     4624   6618   4965    911    476    671       N  
-ATOM   2854  CA  THR B 560       6.123   9.515  -0.682  1.00 40.48           C  
-ANISOU 2854  CA  THR B 560     4329   6244   4808    795    470    543       C  
-ATOM   2855  C   THR B 560       5.525  10.781  -1.288  1.00 41.27           C  
-ANISOU 2855  C   THR B 560     4339   6256   5084    679    470    553       C  
-ATOM   2856  O   THR B 560       4.316  10.999  -1.224  1.00 52.00           O  
-ANISOU 2856  O   THR B 560     5710   7525   6524    591    471    491       O  
-ATOM   2857  CB  THR B 560       6.684   9.822   0.722  1.00 40.43           C  
-ANISOU 2857  CB  THR B 560     4286   6272   4805    809    458    436       C  
-ATOM   2858  OG1 THR B 560       7.409   8.687   1.210  1.00 35.37           O  
-ANISOU 2858  OG1 THR B 560     3725   5720   3993    946    457    450       O  
-ATOM   2859  CG2 THR B 560       5.557  10.144   1.690  1.00 27.07           C  
-ANISOU 2859  CG2 THR B 560     2591   4489   3205    702    453    295       C  
-ATOM   2860  N   ALA B 561       6.378  11.609  -1.880  1.00 33.76           N  
-ANISOU 2860  N   ALA B 561     3298   5335   4195    688    469    633       N  
-ATOM   2861  CA  ALA B 561       5.927  12.832  -2.533  1.00 32.55           C  
-ANISOU 2861  CA  ALA B 561     3057   5090   4221    601    468    667       C  
-ATOM   2862  C   ALA B 561       4.995  12.522  -3.702  1.00 33.69           C  
-ANISOU 2862  C   ALA B 561     3245   5195   4358    575    476    746       C  
-ATOM   2863  O   ALA B 561       4.069  13.283  -3.979  1.00 28.67           O  
-ANISOU 2863  O   ALA B 561     2574   4463   3857    497    474    732       O  
-ATOM   2864  CB  ALA B 561       7.115  13.654  -3.000  1.00 30.57           C  
-ANISOU 2864  CB  ALA B 561     2700   4885   4029    625    464    755       C  
-ATOM   2865  N   ARG B 562       5.249  11.409  -4.385  1.00 35.33           N  
-ANISOU 2865  N   ARG B 562     3529   5484   4411    650    483    826       N  
-ATOM   2866  CA  ARG B 562       4.415  10.982  -5.505  1.00 26.42           C  
-ANISOU 2866  CA  ARG B 562     2442   4336   3261    637    484    895       C  
-ATOM   2867  C   ARG B 562       3.030  10.585  -5.016  1.00 31.34           C  
-ANISOU 2867  C   ARG B 562     3126   4881   3899    575    480    783       C  
-ATOM   2868  O   ARG B 562       2.019  10.975  -5.599  1.00 50.94           O  
-ANISOU 2868  O   ARG B 562     5592   7304   6458    510    478    788       O  
-ATOM   2869  CB  ARG B 562       5.054   9.802  -6.240  1.00 31.68           C  
-ANISOU 2869  CB  ARG B 562     3173   5105   3760    746    488    988       C  
-ATOM   2870  CG  ARG B 562       6.357  10.125  -6.955  1.00 35.13           C  
-ANISOU 2870  CG  ARG B 562     3547   5642   4161    807    497   1110       C  
-ATOM   2871  CD  ARG B 562       6.869   8.913  -7.721  1.00 44.74           C  
-ANISOU 2871  CD  ARG B 562     4833   6960   5208    925    501   1194       C  
-ATOM   2872  NE  ARG B 562       8.141   9.174  -8.389  1.00 55.35           N  
-ANISOU 2872  NE  ARG B 562     6114   8420   6497    986    516   1305       N  
-ATOM   2873  CZ  ARG B 562       8.786   8.287  -9.141  1.00 60.23           C  
-ANISOU 2873  CZ  ARG B 562     6755   9140   6991   1094    531   1364       C  
-ATOM   2874  NH1 ARG B 562       8.277   7.078  -9.326  1.00 60.72           N  
-ANISOU 2874  NH1 ARG B 562     6883   9175   7012   1153    541   1299       N  
-ATOM   2875  NH2 ARG B 562       9.938   8.611  -9.709  1.00 63.82           N  
-ANISOU 2875  NH2 ARG B 562     7135   9711   7404   1140    550   1451       N  
-ATOM   2876  N   GLY B 563       2.993   9.797  -3.946  1.00 23.31           N  
-ANISOU 2876  N   GLY B 563     2176   3874   2806    599    481    684       N  
-ATOM   2877  CA  GLY B 563       1.740   9.391  -3.339  1.00 21.67           C  
-ANISOU 2877  CA  GLY B 563     2022   3603   2610    532    483    566       C  
-ATOM   2878  C   GLY B 563       0.945  10.576  -2.822  1.00 32.50           C  
-ANISOU 2878  C   GLY B 563     3327   4892   4127    426    482    475       C  
-ATOM   2879  O   GLY B 563      -0.253  10.685  -3.076  1.00 41.52           O  
-ANISOU 2879  O   GLY B 563     4477   5983   5314    356    485    432       O  
-ATOM   2880  N   MET B 564       1.614  11.468  -2.096  1.00 35.64           N  
-ANISOU 2880  N   MET B 564     3655   5282   4604    420    478    439       N  
-ATOM   2881  CA  MET B 564       0.964  12.657  -1.549  1.00 34.23           C  
-ANISOU 2881  CA  MET B 564     3404   5016   4587    337    476    345       C  
-ATOM   2882  C   MET B 564       0.544  13.631  -2.642  1.00 30.88           C  
-ANISOU 2882  C   MET B 564     2912   4529   4292    305    477    430       C  
-ATOM   2883  O   MET B 564      -0.504  14.270  -2.547  1.00 39.92           O  
-ANISOU 2883  O   MET B 564     4029   5598   5542    242    480    366       O  
-ATOM   2884  CB  MET B 564       1.876  13.364  -0.545  1.00 29.80           C  
-ANISOU 2884  CB  MET B 564     2773   4459   4091    348    467    283       C  
-ATOM   2885  CG  MET B 564       2.054  12.618   0.761  1.00 29.90           C  
-ANISOU 2885  CG  MET B 564     2836   4522   4002    366    464    172       C  
-ATOM   2886  SD  MET B 564       0.474  12.208   1.525  1.00 37.86           S  
-ANISOU 2886  SD  MET B 564     3903   5480   5002    278    474     25       S  
-ATOM   2887  CE  MET B 564      -0.268  13.832   1.681  1.00 23.73           C  
-ANISOU 2887  CE  MET B 564     2007   3580   3430    195    472    -56       C  
-ATOM   2888  N   ASP B 565       1.372  13.748  -3.674  1.00 36.25           N  
-ANISOU 2888  N   ASP B 565     3562   5249   4963    353    475    576       N  
-ATOM   2889  CA  ASP B 565       1.054  14.597  -4.814  1.00 39.92           C  
-ANISOU 2889  CA  ASP B 565     3961   5666   5541    331    475    683       C  
-ATOM   2890  C   ASP B 565      -0.194  14.074  -5.509  1.00 33.20           C  
-ANISOU 2890  C   ASP B 565     3164   4809   4642    306    478    690       C  
-ATOM   2891  O   ASP B 565      -1.030  14.846  -5.977  1.00 39.01           O  
-ANISOU 2891  O   ASP B 565     3851   5482   5490    265    479    705       O  
-ATOM   2892  CB  ASP B 565       2.221  14.626  -5.800  1.00 35.77           C  
-ANISOU 2892  CB  ASP B 565     3398   5209   4982    388    474    842       C  
-ATOM   2893  CG  ASP B 565       1.965  15.540  -6.977  1.00 35.00           C  
-ANISOU 2893  CG  ASP B 565     3224   5068   5008    366    472    966       C  
-ATOM   2894  OD1 ASP B 565       1.491  16.673  -6.753  1.00 44.02           O  
-ANISOU 2894  OD1 ASP B 565     4290   6109   6326    317    468    934       O  
-ATOM   2895  OD2 ASP B 565       2.243  15.128  -8.123  1.00 40.24           O  
-ANISOU 2895  OD2 ASP B 565     3896   5800   5592    402    474   1097       O  
-ATOM   2896  N   TYR B 566      -0.307  12.751  -5.573  1.00 28.78           N  
-ANISOU 2896  N   TYR B 566     2700   4316   3919    336    479    678       N  
-ATOM   2897  CA  TYR B 566      -1.458  12.105  -6.184  1.00 30.09           C  
-ANISOU 2897  CA  TYR B 566     2916   4489   4028    311    478    667       C  
-ATOM   2898  C   TYR B 566      -2.720  12.385  -5.379  1.00 34.93           C  
-ANISOU 2898  C   TYR B 566     3534   5041   4696    232    485    521       C  
-ATOM   2899  O   TYR B 566      -3.766  12.711  -5.940  1.00 34.03           O  
-ANISOU 2899  O   TYR B 566     3399   4907   4625    190    486    520       O  
-ATOM   2900  CB  TYR B 566      -1.230  10.595  -6.294  1.00 24.91           C  
-ANISOU 2900  CB  TYR B 566     2353   3903   3208    364    475    668       C  
-ATOM   2901  CG  TYR B 566      -2.445   9.828  -6.771  1.00 38.92           C  
-ANISOU 2901  CG  TYR B 566     4175   5682   4930    326    475    623       C  
-ATOM   2902  CD1 TYR B 566      -2.772   9.775  -8.121  1.00 37.34           C  
-ANISOU 2902  CD1 TYR B 566     3951   5515   4719    336    465    719       C  
-ATOM   2903  CD2 TYR B 566      -3.265   9.157  -5.872  1.00 34.89           C  
-ANISOU 2903  CD2 TYR B 566     3726   5150   4381    270    488    481       C  
-ATOM   2904  CE1 TYR B 566      -3.882   9.076  -8.562  1.00 27.89           C  
-ANISOU 2904  CE1 TYR B 566     2787   4334   3475    292    467    664       C  
-ATOM   2905  CE2 TYR B 566      -4.377   8.456  -6.304  1.00 36.11           C  
-ANISOU 2905  CE2 TYR B 566     3918   5312   4489    215    497    428       C  
-ATOM   2906  CZ  TYR B 566      -4.680   8.419  -7.650  1.00 37.71           C  
-ANISOU 2906  CZ  TYR B 566     4094   5552   4684    227    486    515       C  
-ATOM   2907  OH  TYR B 566      -5.784   7.723  -8.085  1.00 43.06           O  
-ANISOU 2907  OH  TYR B 566     4803   6247   5312    161    498    452       O  
-ATOM   2908  N   LEU B 567      -2.610  12.257  -4.060  1.00 40.54           N  
-ANISOU 2908  N   LEU B 567     4267   5738   5399    213    490    397       N  
-ATOM   2909  CA  LEU B 567      -3.738  12.479  -3.163  1.00 22.53           C  
-ANISOU 2909  CA  LEU B 567     1990   3414   3158    136    499    246       C  
-ATOM   2910  C   LEU B 567      -4.222  13.923  -3.227  1.00 34.33           C  
-ANISOU 2910  C   LEU B 567     3388   4832   4826    102    502    234       C  
-ATOM   2911  O   LEU B 567      -5.418  14.180  -3.356  1.00 42.52           O  
-ANISOU 2911  O   LEU B 567     4414   5848   5895     53    510    181       O  
-ATOM   2912  CB  LEU B 567      -3.358  12.112  -1.729  1.00 21.27           C  
-ANISOU 2912  CB  LEU B 567     1861   3264   2958    129    502    128       C  
-ATOM   2913  CG  LEU B 567      -2.962  10.651  -1.502  1.00 26.10           C  
-ANISOU 2913  CG  LEU B 567     2568   3938   3413    166    504    132       C  
-ATOM   2914  CD1 LEU B 567      -2.391  10.450  -0.109  1.00 23.15           C  
-ANISOU 2914  CD1 LEU B 567     2207   3580   3011    175    505     42       C  
-ATOM   2915  CD2 LEU B 567      -4.148   9.729  -1.736  1.00 32.99           C  
-ANISOU 2915  CD2 LEU B 567     3509   4816   4210    108    518     79       C  
-ATOM   2916  N   HIS B 568      -3.289  14.863  -3.136  1.00 39.19           N  
-ANISOU 2916  N   HIS B 568     3927   5406   5558    130    495    283       N  
-ATOM   2917  CA  HIS B 568      -3.626  16.280  -3.214  1.00 36.20           C  
-ANISOU 2917  CA  HIS B 568     3445   4937   5374    107    495    283       C  
-ATOM   2918  C   HIS B 568      -4.233  16.631  -4.572  1.00 42.38           C  
-ANISOU 2918  C   HIS B 568     4194   5709   6199    108    495    406       C  
-ATOM   2919  O   HIS B 568      -5.064  17.531  -4.676  1.00 47.74           O  
-ANISOU 2919  O   HIS B 568     4808   6324   7007     80    499    386       O  
-ATOM   2920  CB  HIS B 568      -2.391  17.142  -2.935  1.00 35.42           C  
-ANISOU 2920  CB  HIS B 568     3266   4799   5392    134    483    320       C  
-ATOM   2921  CG  HIS B 568      -1.989  17.172  -1.492  1.00 30.71           C  
-ANISOU 2921  CG  HIS B 568     2667   4199   4802    124    480    175       C  
-ATOM   2922  ND1 HIS B 568      -1.173  18.152  -0.968  1.00 32.95           N  
-ANISOU 2922  ND1 HIS B 568     2861   4435   5225    131    468    153       N  
-ATOM   2923  CD2 HIS B 568      -2.299  16.351  -0.462  1.00 33.31           C  
-ANISOU 2923  CD2 HIS B 568     3067   4573   5016    105    485     45       C  
-ATOM   2924  CE1 HIS B 568      -0.991  17.929   0.322  1.00 34.36           C  
-ANISOU 2924  CE1 HIS B 568     3054   4634   5367    121    464     11       C  
-ATOM   2925  NE2 HIS B 568      -1.666  16.841   0.654  1.00 36.15           N  
-ANISOU 2925  NE2 HIS B 568     3378   4918   5439    105    475    -52       N  
-ATOM   2926  N   ALA B 569      -3.815  15.911  -5.609  1.00 39.63           N  
-ANISOU 2926  N   ALA B 569     3886   5431   5741    146    490    534       N  
-ATOM   2927  CA  ALA B 569      -4.353  16.116  -6.951  1.00 33.34           C  
-ANISOU 2927  CA  ALA B 569     3060   4648   4961    151    488    658       C  
-ATOM   2928  C   ALA B 569      -5.794  15.626  -7.045  1.00 37.20           C  
-ANISOU 2928  C   ALA B 569     3590   5165   5380    109    495    578       C  
-ATOM   2929  O   ALA B 569      -6.562  16.081  -7.894  1.00 29.16           O  
-ANISOU 2929  O   ALA B 569     2525   4146   4410     97    495    640       O  
-ATOM   2930  CB  ALA B 569      -3.488  15.419  -7.983  1.00 17.57           C  
-ANISOU 2930  CB  ALA B 569     1091   2731   2854    205    479    802       C  
-ATOM   2931  N   LYS B 570      -6.148  14.686  -6.174  1.00 44.71           N  
-ANISOU 2931  N   LYS B 570     4624   6150   6215     82    501    443       N  
-ATOM   2932  CA  LYS B 570      -7.502  14.151  -6.122  1.00 46.97           C  
-ANISOU 2932  CA  LYS B 570     4949   6473   6424     25    510    346       C  
-ATOM   2933  C   LYS B 570      -8.319  14.886  -5.064  1.00 51.83           C  
-ANISOU 2933  C   LYS B 570     5528   7035   7130    -28    526    202       C  
-ATOM   2934  O   LYS B 570      -9.450  14.503  -4.763  1.00 65.58           O  
-ANISOU 2934  O   LYS B 570     7298   8812   8806    -87    539     94       O  
-ATOM   2935  CB  LYS B 570      -7.475  12.650  -5.815  1.00 46.71           C  
-ANISOU 2935  CB  LYS B 570     5024   6507   6218     14    511    281       C  
-ATOM   2936  CG  LYS B 570      -6.720  11.810  -6.837  1.00 44.21           C  
-ANISOU 2936  CG  LYS B 570     4742   6248   5810     73    496    406       C  
-ATOM   2937  CD  LYS B 570      -7.564  11.502  -8.070  1.00 42.36           C  
-ANISOU 2937  CD  LYS B 570     4500   6070   5526     56    490    460       C  
-ATOM   2938  CE  LYS B 570      -8.621  10.444  -7.777  1.00 49.81           C  
-ANISOU 2938  CE  LYS B 570     5513   7056   6359    -21    502    328       C  
-ATOM   2939  NZ  LYS B 570      -9.256   9.915  -9.020  1.00 57.89           N  
-ANISOU 2939  NZ  LYS B 570     6532   8150   7312    -38    495    376       N  
-ATOM   2940  N   SER B 571      -7.736  15.944  -4.505  1.00 35.05           N  
-ANISOU 2940  N   SER B 571     3332   4828   5157    -11    524    195       N  
-ATOM   2941  CA  SER B 571      -8.386  16.726  -3.459  1.00 30.52           C  
-ANISOU 2941  CA  SER B 571     2710   4197   4690    -52    536     53       C  
-ATOM   2942  C   SER B 571      -8.581  15.905  -2.186  1.00 44.29           C  
-ANISOU 2942  C   SER B 571     4528   5980   6321    -93    545   -110       C  
-ATOM   2943  O   SER B 571      -9.597  16.034  -1.502  1.00 42.84           O  
-ANISOU 2943  O   SER B 571     4337   5802   6139   -147    560   -244       O  
-ATOM   2944  CB  SER B 571      -9.726  17.273  -3.950  1.00 43.37           C  
-ANISOU 2944  CB  SER B 571     4284   5823   6370    -84    547     42       C  
-ATOM   2945  OG  SER B 571      -9.554  18.036  -5.131  1.00 66.31           O  
-ANISOU 2945  OG  SER B 571     7116   8695   9383    -47    537    204       O  
-ATOM   2946  N   ILE B 572      -7.598  15.062  -1.880  1.00 54.56           N  
-ANISOU 2946  N   ILE B 572     5893   7314   7522    -68    536    -94       N  
-ATOM   2947  CA  ILE B 572      -7.629  14.226  -0.682  1.00 41.34           C  
-ANISOU 2947  CA  ILE B 572     4287   5678   5742   -104    543   -228       C  
-ATOM   2948  C   ILE B 572      -6.544  14.627   0.315  1.00 43.08           C  
-ANISOU 2948  C   ILE B 572     4476   5869   6023    -76    533   -268       C  
-ATOM   2949  O   ILE B 572      -5.354  14.601  -0.002  1.00 39.77           O  
-ANISOU 2949  O   ILE B 572     4051   5453   5606    -17    519   -165       O  
-ATOM   2950  CB  ILE B 572      -7.453  12.733  -1.029  1.00 35.25           C  
-ANISOU 2950  CB  ILE B 572     3619   4979   4794   -101    541   -188       C  
-ATOM   2951  CG1 ILE B 572      -8.667  12.210  -1.798  1.00 34.42           C  
-ANISOU 2951  CG1 ILE B 572     3547   4915   4614   -153    551   -193       C  
-ATOM   2952  CG2 ILE B 572      -7.246  11.913   0.234  1.00 27.17           C  
-ANISOU 2952  CG2 ILE B 572     2657   3984   3682   -131    546   -297       C  
-ATOM   2953  CD1 ILE B 572      -8.532  10.767  -2.245  1.00 34.70           C  
-ANISOU 2953  CD1 ILE B 572     3675   5005   4505   -156    551   -156       C  
-ATOM   2954  N   ILE B 573      -6.966  14.996   1.522  1.00 49.08           N  
-ANISOU 2954  N   ILE B 573     5210   6612   6824   -119    539   -422       N  
-ATOM   2955  CA  ILE B 573      -6.040  15.337   2.597  1.00 40.42           C  
-ANISOU 2955  CA  ILE B 573     4080   5503   5776   -101    528   -487       C  
-ATOM   2956  C   ILE B 573      -5.877  14.137   3.526  1.00 40.63           C  
-ANISOU 2956  C   ILE B 573     4189   5606   5643   -122    529   -560       C  
-ATOM   2957  O   ILE B 573      -6.864  13.589   4.014  1.00 50.89           O  
-ANISOU 2957  O   ILE B 573     5531   6938   6865   -190    544   -660       O  
-ATOM   2958  CB  ILE B 573      -6.549  16.538   3.417  1.00 47.29           C  
-ANISOU 2958  CB  ILE B 573     4856   6308   6803   -131    531   -620       C  
-ATOM   2959  CG1 ILE B 573      -7.042  17.651   2.491  1.00 45.28           C  
-ANISOU 2959  CG1 ILE B 573     4522   5974   6711   -120    534   -552       C  
-ATOM   2960  CG2 ILE B 573      -5.463  17.052   4.349  1.00 51.94           C  
-ANISOU 2960  CG2 ILE B 573     5390   6878   7465   -104    513   -673       C  
-ATOM   2961  CD1 ILE B 573      -7.609  18.849   3.220  1.00 42.91           C  
-ANISOU 2961  CD1 ILE B 573     4121   5601   6581   -143    537   -679       C  
-ATOM   2962  N   HIS B 574      -4.635  13.728   3.766  1.00 37.85           N  
-ANISOU 2962  N   HIS B 574     3852   5288   5240    -66    514   -505       N  
-ATOM   2963  CA  HIS B 574      -4.364  12.570   4.615  1.00 34.43           C  
-ANISOU 2963  CA  HIS B 574     3490   4927   4664    -71    514   -549       C  
-ATOM   2964  C   HIS B 574      -4.606  12.893   6.086  1.00 38.57           C  
-ANISOU 2964  C   HIS B 574     3977   5463   5214   -119    512   -714       C  
-ATOM   2965  O   HIS B 574      -5.258  12.128   6.799  1.00 43.56           O  
-ANISOU 2965  O   HIS B 574     4658   6137   5756   -180    524   -797       O  
-ATOM   2966  CB  HIS B 574      -2.931  12.081   4.410  1.00 43.28           C  
-ANISOU 2966  CB  HIS B 574     4630   6094   5721     23    500   -433       C  
-ATOM   2967  CG  HIS B 574      -2.682  10.704   4.940  1.00 38.49           C  
-ANISOU 2967  CG  HIS B 574     4111   5553   4961     45    507   -428       C  
-ATOM   2968  ND1 HIS B 574      -2.237  10.468   6.222  1.00 38.46           N  
-ANISOU 2968  ND1 HIS B 574     4103   5595   4917     55    503   -507       N  
-ATOM   2969  CD2 HIS B 574      -2.812   9.488   4.359  1.00 42.95           C  
-ANISOU 2969  CD2 HIS B 574     4769   6134   5414     66    525   -349       C  
-ATOM   2970  CE1 HIS B 574      -2.104   9.168   6.409  1.00 30.62           C  
-ANISOU 2970  CE1 HIS B 574     3203   4638   3795     89    522   -465       C  
-ATOM   2971  NE2 HIS B 574      -2.448   8.550   5.292  1.00 37.21           N  
-ANISOU 2971  NE2 HIS B 574     4101   5446   4590     95    539   -372       N  
-ATOM   2972  N   ARG B 575      -4.063  14.022   6.534  1.00 45.26           N  
-ANISOU 2972  N   ARG B 575     4732   6274   6192    -97    499   -762       N  
-ATOM   2973  CA  ARG B 575      -4.310  14.531   7.883  1.00 39.24           C  
-ANISOU 2973  CA  ARG B 575     3914   5516   5479   -138    495   -932       C  
-ATOM   2974  C   ARG B 575      -3.602  13.747   8.981  1.00 47.76           C  
-ANISOU 2974  C   ARG B 575     5017   6685   6444   -122    482   -974       C  
-ATOM   2975  O   ARG B 575      -3.748  14.061  10.162  1.00 60.48           O  
-ANISOU 2975  O   ARG B 575     6582   8319   8078   -156    477  -1115       O  
-ATOM   2976  CB  ARG B 575      -5.811  14.571   8.179  1.00 32.81           C  
-ANISOU 2976  CB  ARG B 575     3108   4693   4664   -225    517  -1050       C  
-ATOM   2977  CG  ARG B 575      -6.568  15.667   7.462  1.00 43.33           C  
-ANISOU 2977  CG  ARG B 575     4380   5940   6145   -232    529  -1052       C  
-ATOM   2978  CD  ARG B 575      -8.027  15.292   7.331  1.00 64.35           C  
-ANISOU 2978  CD  ARG B 575     7083   8626   8742   -305    555  -1113       C  
-ATOM   2979  NE  ARG B 575      -8.644  15.031   8.627  1.00 75.70           N  
-ANISOU 2979  NE  ARG B 575     8522  10121  10121   -376    564  -1281       N  
-ATOM   2980  CZ  ARG B 575      -9.472  15.869   9.241  1.00 80.31           C  
-ANISOU 2980  CZ  ARG B 575     9035  10688  10790   -410    576  -1424       C  
-ATOM   2981  NH1 ARG B 575      -9.792  17.026   8.673  1.00 82.84           N  
-ANISOU 2981  NH1 ARG B 575     9276  10926  11274   -378    581  -1412       N  
-ATOM   2982  NH2 ARG B 575      -9.985  15.547  10.420  1.00 77.40           N  
-ANISOU 2982  NH2 ARG B 575     8669  10388  10351   -478    584  -1573       N  
-ATOM   2983  N   ASP B 576      -2.846  12.726   8.602  1.00 44.36           N  
-ANISOU 2983  N   ASP B 576     4655   6308   5890    -63    480   -851       N  
-ATOM   2984  CA  ASP B 576      -2.135  11.928   9.592  1.00 53.46           C  
-ANISOU 2984  CA  ASP B 576     5833   7548   6932    -24    472   -868       C  
-ATOM   2985  C   ASP B 576      -0.898  11.278   8.988  1.00 46.49           C  
-ANISOU 2985  C   ASP B 576     4994   6709   5962     92    465   -714       C  
-ATOM   2986  O   ASP B 576      -0.568  10.135   9.305  1.00 54.97           O  
-ANISOU 2986  O   ASP B 576     6145   7839   6904    145    477   -667       O  
-ATOM   2987  CB  ASP B 576      -3.059  10.864  10.194  1.00 72.57           C  
-ANISOU 2987  CB  ASP B 576     8326  10003   9246    -94    497   -917       C  
-ATOM   2988  CG  ASP B 576      -2.518  10.286  11.492  1.00 75.62           C  
-ANISOU 2988  CG  ASP B 576     8716  10469   9548    -64    496   -964       C  
-ATOM   2989  OD1 ASP B 576      -2.873   9.136  11.828  1.00 74.81           O  
-ANISOU 2989  OD1 ASP B 576     8702  10388   9336    -79    532   -937       O  
-ATOM   2990  OD2 ASP B 576      -1.737  10.982  12.176  1.00 68.52           O  
-ANISOU 2990  OD2 ASP B 576     7737   9604   8693    -22    467  -1024       O  
-ATOM   2991  N   LEU B 577      -0.215  12.012   8.116  1.00 39.59           N  
-ANISOU 2991  N   LEU B 577     4073   5805   5166    139    453   -633       N  
-ATOM   2992  CA  LEU B 577       1.010  11.512   7.507  1.00 46.71           C  
-ANISOU 2992  CA  LEU B 577     5003   6761   5985    251    446   -492       C  
-ATOM   2993  C   LEU B 577       2.153  11.493   8.518  1.00 47.99           C  
-ANISOU 2993  C   LEU B 577     5128   7010   6097    326    426   -529       C  
-ATOM   2994  O   LEU B 577       2.402  12.480   9.214  1.00 45.12           O  
-ANISOU 2994  O   LEU B 577     4669   6641   5834    299    408   -630       O  
-ATOM   2995  CB  LEU B 577       1.400  12.348   6.287  1.00 39.54           C  
-ANISOU 2995  CB  LEU B 577     4043   5803   5176    266    442   -391       C  
-ATOM   2996  CG  LEU B 577       2.660  11.861   5.565  1.00 32.80           C  
-ANISOU 2996  CG  LEU B 577     3211   5020   4231    378    437   -244       C  
-ATOM   2997  CD1 LEU B 577       2.436  10.480   4.962  1.00 27.59           C  
-ANISOU 2997  CD1 LEU B 577     2671   4388   3425    428    455   -150       C  
-ATOM   2998  CD2 LEU B 577       3.090  12.849   4.498  1.00 40.78           C  
-ANISOU 2998  CD2 LEU B 577     4148   5987   5358    378    434   -153       C  
-ATOM   2999  N   LYS B 578       2.840  10.358   8.590  1.00 44.99           N  
-ANISOU 2999  N   LYS B 578     4825   6706   5561    431    430   -449       N  
-ATOM   3000  CA  LYS B 578       3.974  10.181   9.490  1.00 48.25           C  
-ANISOU 3000  CA  LYS B 578     5217   7219   5896    529    412   -468       C  
-ATOM   3001  C   LYS B 578       4.704   8.898   9.113  1.00 55.43           C  
-ANISOU 3001  C   LYS B 578     6237   8188   6638    674    425   -338       C  
-ATOM   3002  O   LYS B 578       4.152   8.055   8.405  1.00 63.05           O  
-ANISOU 3002  O   LYS B 578     7302   9102   7553    681    453   -262       O  
-ATOM   3003  CB  LYS B 578       3.502  10.121  10.944  1.00 52.03           C  
-ANISOU 3003  CB  LYS B 578     5679   7722   6366    481    409   -613       C  
-ATOM   3004  CG  LYS B 578       2.693   8.880  11.285  1.00 49.81           C  
-ANISOU 3004  CG  LYS B 578     5518   7426   5980    473    445   -605       C  
-ATOM   3005  CD  LYS B 578       2.230   8.888  12.735  1.00 44.09           C  
-ANISOU 3005  CD  LYS B 578     4767   6734   5250    416    447   -746       C  
-ATOM   3006  CE  LYS B 578       0.749   9.212  12.840  1.00 46.99           C  
-ANISOU 3006  CE  LYS B 578     5117   7033   5703    254    464   -843       C  
-ATOM   3007  NZ  LYS B 578       0.237   9.018  14.225  1.00 54.22           N  
-ANISOU 3007  NZ  LYS B 578     6021   7990   6589    198    476   -966       N  
-ATOM   3008  N   SER B 579       5.942   8.752   9.579  1.00 52.99           N  
-ANISOU 3008  N   SER B 579     5911   7980   6244    798    407   -318       N  
-ATOM   3009  CA  SER B 579       6.749   7.581   9.253  1.00 50.02           C  
-ANISOU 3009  CA  SER B 579     5643   7659   5705    965    418   -198       C  
-ATOM   3010  C   SER B 579       6.026   6.303   9.669  1.00 57.26           C  
-ANISOU 3010  C   SER B 579     6710   8516   6531    993    458   -194       C  
-ATOM   3011  O   SER B 579       6.277   5.230   9.122  1.00 64.36           O  
-ANISOU 3011  O   SER B 579     7738   9392   7326   1109    485    -92       O  
-ATOM   3012  CB  SER B 579       8.117   7.659   9.932  1.00 36.83           C  
-ANISOU 3012  CB  SER B 579     3926   6119   3949   1095    391   -204       C  
-ATOM   3013  OG  SER B 579       7.985   7.591  11.338  1.00 41.49           O  
-ANISOU 3013  OG  SER B 579     4505   6742   4518   1089    384   -318       O  
-ATOM   3014  N   ASN B 580       5.119   6.430  10.633  1.00 47.84           N  
-ANISOU 3014  N   ASN B 580     5506   7288   5383    883    469   -312       N  
-ATOM   3015  CA  ASN B 580       4.326   5.301  11.109  1.00 50.99           C  
-ANISOU 3015  CA  ASN B 580     6054   7615   5705    875    522   -322       C  
-ATOM   3016  C   ASN B 580       3.298   4.831  10.073  1.00 41.81           C  
-ANISOU 3016  C   ASN B 580     4977   6338   4571    794    563   -271       C  
-ATOM   3017  O   ASN B 580       3.023   3.635   9.953  1.00 51.87           O  
-ANISOU 3017  O   ASN B 580     6424   7534   5749    839    617   -223       O  
-ATOM   3018  CB  ASN B 580       3.634   5.658  12.428  1.00 84.25           C  
-ANISOU 3018  CB  ASN B 580    10216  11839   9956    764    523   -466       C  
-ATOM   3019  CG  ASN B 580       2.927   4.473  13.052  1.00 98.89           C  
-ANISOU 3019  CG  ASN B 580    12241  13624  11709    752    586   -475       C  
-ATOM   3020  OD1 ASN B 580       3.568   3.558  13.570  1.00101.08           O  
-ANISOU 3020  OD1 ASN B 580    12646  13910  11851    887    608   -434       O  
-ATOM   3021  ND2 ASN B 580       1.600   4.482  13.007  1.00104.71           N  
-ANISOU 3021  ND2 ASN B 580    12994  14287  12504    589    618   -530       N  
-ATOM   3022  N   ASN B 581       2.740   5.778   9.321  1.00 44.74           N  
-ANISOU 3022  N   ASN B 581     5240   6690   5070    676    540   -287       N  
-ATOM   3023  CA  ASN B 581       1.749   5.463   8.292  1.00 47.89           C  
-ANISOU 3023  CA  ASN B 581     5696   6998   5503    594    571   -247       C  
-ATOM   3024  C   ASN B 581       2.321   5.199   6.896  1.00 49.21           C  
-ANISOU 3024  C   ASN B 581     5891   7159   5647    686    568   -112       C  
-ATOM   3025  O   ASN B 581       1.577   5.159   5.910  1.00 44.53           O  
-ANISOU 3025  O   ASN B 581     5313   6508   5100    617    582    -80       O  
-ATOM   3026  CB  ASN B 581       0.688   6.566   8.213  1.00 46.44           C  
-ANISOU 3026  CB  ASN B 581     5396   6788   5460    422    552   -342       C  
-ATOM   3027  CG  ASN B 581      -0.183   6.635   9.444  1.00 43.96           C  
-ANISOU 3027  CG  ASN B 581     5071   6470   5162    312    567   -478       C  
-ATOM   3028  OD1 ASN B 581      -1.097   7.453   9.518  1.00 43.77           O  
-ANISOU 3028  OD1 ASN B 581     4966   6425   5240    183    555   -571       O  
-ATOM   3029  ND2 ASN B 581       0.089   5.785  10.414  1.00 42.80           N  
-ANISOU 3029  ND2 ASN B 581     5013   6342   4909    369    596   -490       N  
-ATOM   3030  N   ILE B 582       3.635   5.009   6.825  1.00 49.38           N  
-ANISOU 3030  N   ILE B 582     5918   7252   5593    844    548    -36       N  
-ATOM   3031  CA  ILE B 582       4.303   4.751   5.553  1.00 27.94           C  
-ANISOU 3031  CA  ILE B 582     3222   4552   2842    945    544     92       C  
-ATOM   3032  C   ILE B 582       4.925   3.363   5.547  1.00 39.57           C  
-ANISOU 3032  C   ILE B 582     4858   6006   4170   1120    581    161       C  
-ATOM   3033  O   ILE B 582       6.014   3.167   6.085  1.00 50.26           O  
-ANISOU 3033  O   ILE B 582     6222   7438   5436   1262    565    182       O  
-ATOM   3034  CB  ILE B 582       5.406   5.797   5.252  1.00 24.32           C  
-ANISOU 3034  CB  ILE B 582     2629   4198   2412    984    494    131       C  
-ATOM   3035  CG1 ILE B 582       4.826   7.206   5.257  1.00 34.53           C  
-ANISOU 3035  CG1 ILE B 582     3790   5469   3862    820    472     55       C  
-ATOM   3036  CG2 ILE B 582       6.089   5.512   3.909  1.00 29.04           C  
-ANISOU 3036  CG2 ILE B 582     3246   4827   2960   1082    493    270       C  
-ATOM   3037  CD1 ILE B 582       5.856   8.298   5.084  1.00 38.61           C  
-ANISOU 3037  CD1 ILE B 582     4187   6052   4430    836    444     73       C  
-ATOM   3038  N   PHE B 583       4.260   2.417   4.916  1.00 43.35           N  
-ANISOU 3038  N   PHE B 583     5474   6376   4622   1112    635    189       N  
-ATOM   3039  CA  PHE B 583       4.730   1.053   4.865  1.00 51.58           C  
-ANISOU 3039  CA  PHE B 583     6710   7359   5530   1273    685    241       C  
-ATOM   3040  C   PHE B 583       5.811   0.821   3.807  1.00 48.93           C  
-ANISOU 3040  C   PHE B 583     6351   7089   5151   1435    663    355       C  
-ATOM   3041  O   PHE B 583       5.604   1.074   2.663  1.00 56.01           O  
-ANISOU 3041  O   PHE B 583     7169   7998   6114   1390    648    407       O  
-ATOM   3042  CB  PHE B 583       3.544   0.154   4.612  1.00 93.46           C  
-ANISOU 3042  CB  PHE B 583    12190  12509  10813   1185    759    216       C  
-ATOM   3043  CG  PHE B 583       3.365  -0.918   5.630  1.00118.87           C  
-ANISOU 3043  CG  PHE B 583    15467  15662  14035   1035    790    112       C  
-ATOM   3044  CD1 PHE B 583       4.042  -2.113   5.520  1.00124.80           C  
-ANISOU 3044  CD1 PHE B 583    16391  16360  14666   1096    830     83       C  
-ATOM   3045  CD2 PHE B 583       2.507  -0.739   6.693  1.00132.59           C  
-ANISOU 3045  CD2 PHE B 583    17094  17395  15887    836    780     43       C  
-ATOM   3046  CE1 PHE B 583       3.875  -3.097   6.465  1.00135.76           C  
-ANISOU 3046  CE1 PHE B 583    17833  17699  16049    950    859     -7       C  
-ATOM   3047  CE2 PHE B 583       2.341  -1.718   7.643  1.00137.62           C  
-ANISOU 3047  CE2 PHE B 583    17778  17990  16522    696    810    -54       C  
-ATOM   3048  CZ  PHE B 583       3.020  -2.896   7.532  1.00141.31           C  
-ANISOU 3048  CZ  PHE B 583    18412  18411  16870    748    849    -77       C  
-ATOM   3049  N   LEU B 584       6.977   0.351   4.203  1.00 51.81           N  
-ANISOU 3049  N   LEU B 584     6782   7505   5398   1629    661    393       N  
-ATOM   3050  CA  LEU B 584       8.048   0.066   3.257  1.00 54.65           C  
-ANISOU 3050  CA  LEU B 584     7137   7933   5694   1803    647    497       C  
-ATOM   3051  C   LEU B 584       7.914  -1.353   2.711  1.00 66.74           C  
-ANISOU 3051  C   LEU B 584     8889   9330   7138   1910    721    523       C  
-ATOM   3052  O   LEU B 584       8.688  -2.241   3.066  1.00 73.40           O  
-ANISOU 3052  O   LEU B 584     9874  10161   7854   2095    746    543       O  
-ATOM   3053  CB  LEU B 584       9.422   0.263   3.903  1.00 49.57           C  
-ANISOU 3053  CB  LEU B 584     6439   7436   4958   1965    601    523       C  
-ATOM   3054  CG  LEU B 584      10.045   1.657   3.817  1.00 50.59           C  
-ANISOU 3054  CG  LEU B 584     6353   7734   5136   1899    528    539       C  
-ATOM   3055  CD1 LEU B 584      11.500   1.619   4.261  1.00 51.36           C  
-ANISOU 3055  CD1 LEU B 584     6424   7985   5105   2080    495    572       C  
-ATOM   3056  CD2 LEU B 584       9.941   2.189   2.399  1.00 51.55           C  
-ANISOU 3056  CD2 LEU B 584     6389   7879   5320   1829    514    617       C  
-ATOM   3057  N   HIS B 585       6.923  -1.557   1.846  1.00 65.17           N  
-ANISOU 3057  N   HIS B 585     8729   9031   7002   1789    758    517       N  
-ATOM   3058  CA  HIS B 585       6.655  -2.874   1.272  1.00 65.20           C  
-ANISOU 3058  CA  HIS B 585     8958   8894   6922   1849    835    524       C  
-ATOM   3059  C   HIS B 585       7.905  -3.461   0.626  1.00 71.18           C  
-ANISOU 3059  C   HIS B 585     9761   9704   7579   2087    836    606       C  
-ATOM   3060  O   HIS B 585       8.484  -2.865  -0.283  1.00 61.97           O  
-ANISOU 3060  O   HIS B 585     8430   8659   6459   2135    791    675       O  
-ATOM   3061  CB  HIS B 585       5.523  -2.790   0.246  1.00 77.05           C  
-ANISOU 3061  CB  HIS B 585    10439  10325   8512   1679    859    511       C  
-ATOM   3062  CG  HIS B 585       5.047  -4.121  -0.249  1.00 91.84           C  
-ANISOU 3062  CG  HIS B 585    12561  12041  10293   1688    942    497       C  
-ATOM   3063  ND1 HIS B 585       5.766  -5.284  -0.071  1.00 99.04           N  
-ANISOU 3063  ND1 HIS B 585    13694  12884  11053   1871    988    517       N  
-ATOM   3064  CD2 HIS B 585       3.927  -4.471  -0.924  1.00 97.75           C  
-ANISOU 3064  CD2 HIS B 585    13382  12690  11068   1534    987    462       C  
-ATOM   3065  CE1 HIS B 585       5.106  -6.293  -0.611  1.00103.87           C  
-ANISOU 3065  CE1 HIS B 585    14516  13348  11601   1820   1058    496       C  
-ATOM   3066  NE2 HIS B 585       3.987  -5.828  -1.136  1.00101.83           N  
-ANISOU 3066  NE2 HIS B 585    14167  13075  11449   1612   1059    461       N  
-ATOM   3067  N   GLU B 586       8.315  -4.632   1.106  1.00 90.43           N  
-ANISOU 3067  N   GLU B 586    12431  12055   9872   2237    888    598       N  
-ATOM   3068  CA  GLU B 586       9.495  -5.313   0.584  1.00 89.54           C  
-ANISOU 3068  CA  GLU B 586    12391  11985   9646   2484    897    664       C  
-ATOM   3069  C   GLU B 586      10.739  -4.431   0.668  1.00 78.85           C  
-ANISOU 3069  C   GLU B 586    10812  10846   8300   2613    816    723       C  
-ATOM   3070  O   GLU B 586      11.699  -4.624  -0.079  1.00 71.64           O  
-ANISOU 3070  O   GLU B 586     9866  10024   7332   2786    805    791       O  
-ATOM   3071  CB  GLU B 586       9.259  -5.779  -0.855  1.00113.53           C  
-ANISOU 3071  CB  GLU B 586    15473  14971  12691   2486    935    697       C  
-ATOM   3072  CG  GLU B 586       8.259  -6.922  -0.981  1.00120.94           C  
-ANISOU 3072  CG  GLU B 586    16689  15696  13566   2399   1021    645       C  
-ATOM   3073  CD  GLU B 586       7.800  -7.137  -2.409  1.00123.01           C  
-ANISOU 3073  CD  GLU B 586    16947  15925  13864   2339   1050    664       C  
-ATOM   3074  OE1 GLU B 586       8.437  -6.577  -3.325  1.00118.31           O  
-ANISOU 3074  OE1 GLU B 586    16161  15471  13321   2414   1009    726       O  
-ATOM   3075  OE2 GLU B 586       6.804  -7.862  -2.617  1.00124.44           O  
-ANISOU 3075  OE2 GLU B 586    17316  15949  14016   2210   1112    616       O  
-ATOM   3076  N   ASP B 587      10.705  -3.462   1.580  1.00 81.11           N  
-ANISOU 3076  N   ASP B 587    10950  11221   8646   2516    761    694       N  
-ATOM   3077  CA  ASP B 587      11.839  -2.579   1.850  1.00 85.18           C  
-ANISOU 3077  CA  ASP B 587    11272  11945   9147   2601    680    739       C  
-ATOM   3078  C   ASP B 587      12.051  -1.478   0.812  1.00 92.00           C  
-ANISOU 3078  C   ASP B 587    11916  12950  10091   2490    639    785       C  
-ATOM   3079  O   ASP B 587      12.770  -0.514   1.071  1.00100.00           O  
-ANISOU 3079  O   ASP B 587    12770  14129  11097   2451    597    786       O  
-ATOM   3080  CB  ASP B 587      13.133  -3.384   2.027  1.00 93.47           C  
-ANISOU 3080  CB  ASP B 587    12416  13063  10035   2873    692    774       C  
-ATOM   3081  CG  ASP B 587      13.226  -4.050   3.384  1.00 99.44           C  
-ANISOU 3081  CG  ASP B 587    13335  13754  10693   2964    716    721       C  
-ATOM   3082  OD1 ASP B 587      12.194  -4.559   3.871  1.00 97.95           O  
-ANISOU 3082  OD1 ASP B 587    13309  13393  10516   2848    771    657       O  
-ATOM   3083  OD2 ASP B 587      14.332  -4.066   3.963  1.00103.32           O  
-ANISOU 3083  OD2 ASP B 587    13795  14379  11084   3140    683    740       O  
-ATOM   3084  N   ASN B 588      11.425  -1.608  -0.353  1.00 85.43           N  
-ANISOU 3084  N   ASN B 588    11086  12049   9325   2418    666    811       N  
-ATOM   3085  CA  ASN B 588      11.718  -0.698  -1.459  1.00 78.48           C  
-ANISOU 3085  CA  ASN B 588    10024  11298   8496   2320    652    855       C  
-ATOM   3086  C   ASN B 588      10.541   0.120  -1.992  1.00 70.96           C  
-ANISOU 3086  C   ASN B 588     8977  10291   7693   2096    627    854       C  
-ATOM   3087  O   ASN B 588      10.742   1.176  -2.589  1.00 76.08           O  
-ANISOU 3087  O   ASN B 588     9471  11044   8393   1984    603    888       O  
-ATOM   3088  CB  ASN B 588      12.386  -1.459  -2.608  1.00 95.05           C  
-ANISOU 3088  CB  ASN B 588    12169  13432  10514   2464    700    903       C  
-ATOM   3089  CG  ASN B 588      13.742  -2.018  -2.224  1.00101.08           C  
-ANISOU 3089  CG  ASN B 588    12984  14301  11120   2686    716    912       C  
-ATOM   3090  OD1 ASN B 588      14.748  -1.308  -2.248  1.00 99.41           O  
-ANISOU 3090  OD1 ASN B 588    12632  14272  10867   2703    693    935       O  
-ATOM   3091  ND2 ASN B 588      13.775  -3.297  -1.868  1.00103.07           N  
-ANISOU 3091  ND2 ASN B 588    13452  14432  11276   2861    756    897       N  
-ATOM   3092  N   THR B 589       9.320  -0.359  -1.781  1.00 58.76           N  
-ANISOU 3092  N   THR B 589     7536   8577   6212   2036    637    820       N  
-ATOM   3093  CA  THR B 589       8.154   0.320  -2.338  1.00 59.96           C  
-ANISOU 3093  CA  THR B 589     7606   8681   6495   1829    626    804       C  
-ATOM   3094  C   THR B 589       7.309   1.018  -1.275  1.00 61.20           C  
-ANISOU 3094  C   THR B 589     7727   8797   6729   1651    614    712       C  
-ATOM   3095  O   THR B 589       6.643   0.371  -0.467  1.00 62.19           O  
-ANISOU 3095  O   THR B 589     7980   8809   6840   1617    663    627       O  
-ATOM   3096  CB  THR B 589       7.279  -0.642  -3.156  1.00 63.46           C  
-ANISOU 3096  CB  THR B 589     8173   8988   6951   1805    697    779       C  
-ATOM   3097  OG1 THR B 589       8.103  -1.371  -4.074  1.00 68.22           O  
-ANISOU 3097  OG1 THR B 589     8821   9624   7474   1984    718    847       O  
-ATOM   3098  CG2 THR B 589       6.219   0.128  -3.934  1.00 57.52           C  
-ANISOU 3098  CG2 THR B 589     7306   8225   6324   1612    677    776       C  
-ATOM   3099  N   VAL B 590       7.341   2.348  -1.287  1.00 62.91           N  
-ANISOU 3099  N   VAL B 590     7786   9102   7015   1530    557    725       N  
-ATOM   3100  CA  VAL B 590       6.556   3.142  -0.343  1.00 50.36           C  
-ANISOU 3100  CA  VAL B 590     6144   7478   5512   1363    547    626       C  
-ATOM   3101  C   VAL B 590       5.061   2.933  -0.538  1.00 52.97           C  
-ANISOU 3101  C   VAL B 590     6516   7682   5928   1218    581    559       C  
-ATOM   3102  O   VAL B 590       4.544   3.024  -1.652  1.00 55.70           O  
-ANISOU 3102  O   VAL B 590     6834   8007   6323   1165    582    599       O  
-ATOM   3103  CB  VAL B 590       6.856   4.651  -0.460  1.00 38.23           C  
-ANISOU 3103  CB  VAL B 590     4452   6028   4047   1253    504    638       C  
-ATOM   3104  CG1 VAL B 590       5.795   5.468   0.262  1.00 36.04           C  
-ANISOU 3104  CG1 VAL B 590     4121   5681   3891   1075    501    525       C  
-ATOM   3105  CG2 VAL B 590       8.232   4.965   0.097  1.00 35.52           C  
-ANISOU 3105  CG2 VAL B 590     4064   5811   3620   1352    485    656       C  
-ATOM   3106  N   LYS B 591       4.370   2.655   0.562  1.00 55.15           N  
-ANISOU 3106  N   LYS B 591     6859   7886   6209   1150    610    455       N  
-ATOM   3107  CA  LYS B 591       2.919   2.493   0.552  1.00 45.71           C  
-ANISOU 3107  CA  LYS B 591     5706   6586   5075    991    645    376       C  
-ATOM   3108  C   LYS B 591       2.267   3.427   1.589  1.00 43.02           C  
-ANISOU 3108  C   LYS B 591     5280   6252   4813    845    622    273       C  
-ATOM   3109  O   LYS B 591       2.313   3.160   2.791  1.00 49.04           O  
-ANISOU 3109  O   LYS B 591     6094   7006   5535    852    637    206       O  
-ATOM   3110  CB  LYS B 591       2.546   1.022   0.807  1.00 33.21           C  
-ANISOU 3110  CB  LYS B 591     4337   4886   3395   1028    725    343       C  
-ATOM   3111  CG  LYS B 591       2.880   0.067  -0.349  1.00 37.09           C  
-ANISOU 3111  CG  LYS B 591     4933   5339   3823   1138    764    416       C  
-ATOM   3112  CD  LYS B 591       1.791   0.099  -1.434  1.00 38.69           C  
-ANISOU 3112  CD  LYS B 591     5114   5496   4091   1004    780    405       C  
-ATOM   3113  CE  LYS B 591       2.287  -0.527  -2.743  1.00 40.45           C  
-ANISOU 3113  CE  LYS B 591     5376   5723   4270   1117    800    485       C  
-ATOM   3114  NZ  LYS B 591       1.249  -0.533  -3.818  1.00 49.85           N  
-ANISOU 3114  NZ  LYS B 591     6544   6884   5513    990    814    471       N  
-ATOM   3115  N   ILE B 592       1.680   4.528   1.123  1.00 40.32           N  
-ANISOU 3115  N   ILE B 592     4816   5923   4581    723    586    258       N  
-ATOM   3116  CA  ILE B 592       1.022   5.478   2.023  1.00 40.19           C  
-ANISOU 3116  CA  ILE B 592     4721   5902   4649    591    567    148       C  
-ATOM   3117  C   ILE B 592      -0.395   5.056   2.388  1.00 46.46           C  
-ANISOU 3117  C   ILE B 592     5574   6619   5458    459    606     49       C  
-ATOM   3118  O   ILE B 592      -1.229   4.848   1.503  1.00 40.97           O  
-ANISOU 3118  O   ILE B 592     4901   5883   4783    394    621     59       O  
-ATOM   3119  CB  ILE B 592       0.987   6.898   1.441  1.00 43.66           C  
-ANISOU 3119  CB  ILE B 592     5028   6359   5201    524    527    163       C  
-ATOM   3120  CG1 ILE B 592       2.378   7.513   1.472  1.00 34.23           C  
-ANISOU 3120  CG1 ILE B 592     3767   5240   4000    613    501    224       C  
-ATOM   3121  CG2 ILE B 592       0.020   7.799   2.220  1.00 41.70           C  
-ANISOU 3121  CG2 ILE B 592     4719   6070   5055    387    520     31       C  
-ATOM   3122  CD1 ILE B 592       2.411   8.943   0.971  1.00 27.44           C  
-ANISOU 3122  CD1 ILE B 592     2794   4363   3269    544    483    238       C  
-ATOM   3123  N   GLY B 593      -0.681   4.932   3.684  1.00 59.64           N  
-ANISOU 3123  N   GLY B 593     7269   8281   7110    412    622    -49       N  
-ATOM   3124  CA  GLY B 593      -1.997   4.456   4.106  1.00 63.41           C  
-ANISOU 3124  CA  GLY B 593     7816   8696   7580    276    667   -141       C  
-ATOM   3125  C   GLY B 593      -2.315   4.649   5.588  1.00 65.77           C  
-ANISOU 3125  C   GLY B 593     8101   9011   7880    208    672   -255       C  
-ATOM   3126  O   GLY B 593      -1.995   5.705   6.140  1.00 45.39           O  
-ANISOU 3126  O   GLY B 593     5394   6484   5369    201    625   -307       O  
-ATOM   3127  N   ASP B 594      -2.918   3.645   6.237  1.00102.07           N  
-ANISOU 3127  N   ASP B 594    12835  13554  12394    155    734   -298       N  
-ATOM   3128  CA  ASP B 594      -3.568   3.840   7.535  1.00110.17           C  
-ANISOU 3128  CA  ASP B 594    13839  14596  13423     48    745   -415       C  
-ATOM   3129  C   ASP B 594      -4.280   5.170   7.406  1.00114.57           C  
-ANISOU 3129  C   ASP B 594    14226  15192  14112    -61    695   -499       C  
-ATOM   3130  O   ASP B 594      -4.082   6.066   8.227  1.00121.23           O  
-ANISOU 3130  O   ASP B 594    14958  16088  15017    -72    657   -577       O  
-ATOM   3131  CB  ASP B 594      -2.559   3.847   8.704  1.00 77.57           C  
-ANISOU 3131  CB  ASP B 594     9705  10520   9247    153    731   -429       C  
-ATOM   3132  CG  ASP B 594      -3.181   3.388  10.015  1.00 92.41           C  
-ANISOU 3132  CG  ASP B 594    11654  12391  11066     69    772   -519       C  
-ATOM   3133  OD1 ASP B 594      -4.386   3.599  10.163  1.00 99.09           O  
-ANISOU 3133  OD1 ASP B 594    12470  13227  11953    -91    789   -600       O  
-ATOM   3134  OD2 ASP B 594      -2.497   2.836  10.903  1.00 89.36           O  
-ANISOU 3134  OD2 ASP B 594    11351  12016  10586    162    786   -511       O  
-ATOM   3135  N   PHE B 595      -5.070   5.313   6.341  1.00110.91           N  
-ANISOU 3135  N   PHE B 595    13753  14699  13689   -131    694   -486       N  
-ATOM   3136  CA  PHE B 595      -5.789   6.562   6.109  1.00123.69           C  
-ANISOU 3136  CA  PHE B 595    15243  16336  15418   -213    651   -563       C  
-ATOM   3137  C   PHE B 595      -6.598   6.964   7.336  1.00131.28           C  
-ANISOU 3137  C   PHE B 595    16155  17322  16402   -327    654   -710       C  
-ATOM   3138  O   PHE B 595      -6.133   7.778   8.119  1.00136.06           O  
-ANISOU 3138  O   PHE B 595    16673  17960  17063   -300    621   -773       O  
-ATOM   3139  CB  PHE B 595      -6.718   6.486   4.886  1.00108.82           C  
-ANISOU 3139  CB  PHE B 595    13378  14423  13543   -276    658   -540       C  
-ATOM   3140  CG  PHE B 595      -6.014   6.578   3.542  1.00 94.72           C  
-ANISOU 3140  CG  PHE B 595    11586  12630  11774   -170    635   -408       C  
-ATOM   3141  CD1 PHE B 595      -5.715   5.419   2.820  1.00 84.38           C  
-ANISOU 3141  CD1 PHE B 595    10384  11293  10383   -118    671   -316       C  
-ATOM   3142  CD2 PHE B 595      -5.700   7.821   2.980  1.00 81.29           C  
-ANISOU 3142  CD2 PHE B 595     9782  10937  10168   -125    590   -378       C  
-ATOM   3143  CE1 PHE B 595      -5.091   5.492   1.578  1.00 68.66           C  
-ANISOU 3143  CE1 PHE B 595     8375   9309   8404    -23    649   -199       C  
-ATOM   3144  CE2 PHE B 595      -5.072   7.906   1.736  1.00 68.14           C  
-ANISOU 3144  CE2 PHE B 595     8107   9272   8513    -38    573   -247       C  
-ATOM   3145  CZ  PHE B 595      -4.770   6.741   1.036  1.00 61.86           C  
-ANISOU 3145  CZ  PHE B 595     7398   8475   7632     13    596   -160       C  
-ATOM   3146  N   GLY B 596      -7.812   6.428   7.473  1.00130.86           N  
-ANISOU 3146  N   GLY B 596    16155  17258  16307   -458    695   -772       N  
-ATOM   3147  CA  GLY B 596      -8.580   6.560   8.702  1.00129.65           C  
-ANISOU 3147  CA  GLY B 596    15969  17141  16150   -572    710   -903       C  
-ATOM   3148  C   GLY B 596      -9.079   7.959   9.010  1.00125.50           C  
-ANISOU 3148  C   GLY B 596    15309  16647  15729   -611    661  -1030       C  
-ATOM   3149  O   GLY B 596     -10.239   8.140   9.362  1.00123.40           O  
-ANISOU 3149  O   GLY B 596    15019  16406  15462   -730    673  -1141       O  
-ATOM   3150  N   LEU B 597      -8.202   8.947   8.885  1.00150.40           N  
-ANISOU 3150  N   LEU B 597    18386  19792  18966   -506    616  -1018       N  
-ATOM   3151  CA  LEU B 597      -8.554  10.334   9.138  1.00145.83           C  
-ANISOU 3151  CA  LEU B 597    17708  19204  18497   -514    590  -1133       C  
-ATOM   3152  C   LEU B 597      -8.634  11.109   7.830  1.00136.04           C  
-ANISOU 3152  C   LEU B 597    16446  17906  17335   -458    581  -1064       C  
-ATOM   3153  O   LEU B 597      -8.896  12.313   7.826  1.00128.76           O  
-ANISOU 3153  O   LEU B 597    15447  16947  16528   -442    577  -1126       O  
-ATOM   3154  CB  LEU B 597      -7.504  10.967  10.043  1.00101.05           C  
-ANISOU 3154  CB  LEU B 597    11966  13546  12883   -444    563  -1174       C  
-ATOM   3155  CG  LEU B 597      -7.292  10.312  11.402  1.00 97.53           C  
-ANISOU 3155  CG  LEU B 597    11522  13169  12366   -477    570  -1233       C  
-ATOM   3156  CD1 LEU B 597      -6.095  10.925  12.106  1.00 95.13           C  
-ANISOU 3156  CD1 LEU B 597    11148  12887  12109   -388    537  -1258       C  
-ATOM   3157  CD2 LEU B 597      -8.542  10.448  12.258  1.00 92.01           C  
-ANISOU 3157  CD2 LEU B 597    10789  12507  11663   -608    585  -1388       C  
-ATOM   3158  N   ALA B 598      -8.372  10.421   6.724  1.00 81.88           N  
-ANISOU 3158  N   ALA B 598     9651  11035  10425   -421    586   -926       N  
-ATOM   3159  CA  ALA B 598      -8.385  11.054   5.408  1.00 85.42           C  
-ANISOU 3159  CA  ALA B 598    10075  11440  10939   -366    578   -834       C  
-ATOM   3160  C   ALA B 598      -9.727  11.709   5.120  1.00 96.57           C  
-ANISOU 3160  C   ALA B 598    11453  12844  12395   -429    593   -912       C  
-ATOM   3161  O   ALA B 598     -10.762  11.269   5.616  1.00 93.60           O  
-ANISOU 3161  O   ALA B 598    11104  12509  11950   -529    612  -1016       O  
-ATOM   3162  CB  ALA B 598      -8.048  10.043   4.322  1.00106.42           C  
-ANISOU 3162  CB  ALA B 598    12813  14106  13517   -331    582   -692       C  
-ATOM   3163  N   THR B 599      -9.699  12.754   4.300  1.00106.08           N  
-ANISOU 3163  N   THR B 599    12591  13997  13716   -371    588   -852       N  
-ATOM   3164  CA  THR B 599     -10.906  13.477   3.923  1.00131.35           C  
-ANISOU 3164  CA  THR B 599    15744  17190  16975   -406    605   -902       C  
-ATOM   3165  C   THR B 599     -10.799  13.971   2.492  1.00115.49           C  
-ANISOU 3165  C   THR B 599    13702  15142  15035   -345    598   -752       C  
-ATOM   3166  O   THR B 599      -9.771  13.799   1.838  1.00113.78           O  
-ANISOU 3166  O   THR B 599    13501  14907  14825   -279    581   -620       O  
-ATOM   3167  CB  THR B 599     -11.143  14.698   4.828  1.00192.99           C  
-ANISOU 3167  CB  THR B 599    23453  24956  24919   -406    609  -1025       C  
-ATOM   3168  OG1 THR B 599     -12.335  15.377   4.412  1.00190.13           O  
-ANISOU 3168  OG1 THR B 599    23036  24589  24615   -430    627  -1061       O  
-ATOM   3169  CG2 THR B 599      -9.971  15.665   4.732  1.00195.49           C  
-ANISOU 3169  CG2 THR B 599    23697  25189  25393   -320    587   -955       C  
-ATOM   3170  N   GLU B 600     -11.864  14.603   2.014  1.00100.98           N  
-ANISOU 3170  N   GLU B 600    11813  13303  13251   -367    612   -771       N  
-ATOM   3171  CA  GLU B 600     -11.876  15.162   0.672  1.00102.95           C  
-ANISOU 3171  CA  GLU B 600    12018  13521  13579   -316    604   -626       C  
-ATOM   3172  C   GLU B 600     -13.005  16.170   0.507  1.00100.19           C  
-ANISOU 3172  C   GLU B 600    11579  13157  13333   -335    619   -671       C  
-ATOM   3173  O   GLU B 600     -13.104  16.838  -0.520  1.00104.43           O  
-ANISOU 3173  O   GLU B 600    12055  13660  13962   -297    612   -555       O  
-ATOM   3174  CB  GLU B 600     -12.028  14.048  -0.356  1.00104.01           C  
-ANISOU 3174  CB  GLU B 600    12231  13721  13566   -328    602   -534       C  
-ATOM   3175  CG  GLU B 600     -13.260  13.207  -0.133  1.00107.36           C  
-ANISOU 3175  CG  GLU B 600    12711  14231  13849   -429    621   -643       C  
-ATOM   3176  CD  GLU B 600     -13.677  12.456  -1.370  1.00111.79           C  
-ANISOU 3176  CD  GLU B 600    13315  14851  14310   -446    618   -556       C  
-ATOM   3177  OE1 GLU B 600     -14.744  12.798  -1.919  1.00115.08           O  
-ANISOU 3177  OE1 GLU B 600    13690  15312  14725   -481    629   -566       O  
-ATOM   3178  OE2 GLU B 600     -12.944  11.535  -1.795  1.00113.04           O  
-ANISOU 3178  OE2 GLU B 600    13539  15015  14394   -425    606   -481       O  
-ATOM   3179  N   GLY B 615       0.377  10.504  19.667  1.00116.94           N  
-ANISOU 3179  N   GLY B 615    13633  16241  14557     94    411  -1528       N  
-ATOM   3180  CA  GLY B 615       1.607  10.149  18.984  1.00114.26           C  
-ANISOU 3180  CA  GLY B 615    13347  15913  14153    240    400  -1387       C  
-ATOM   3181  C   GLY B 615       1.817  10.993  17.743  1.00102.83           C  
-ANISOU 3181  C   GLY B 615    11862  14385  12825    230    378  -1343       C  
-ATOM   3182  O   GLY B 615       2.949  11.296  17.369  1.00102.45           O  
-ANISOU 3182  O   GLY B 615    11784  14364  12777    324    353  -1286       O  
-ATOM   3183  N   SER B 616       0.713  11.381  17.112  1.00 72.19           N  
-ANISOU 3183  N   SER B 616     7982  10407   9041    116    392  -1367       N  
-ATOM   3184  CA  SER B 616       0.747  12.178  15.892  1.00 66.44           C  
-ANISOU 3184  CA  SER B 616     7233   9583   8428    105    384  -1318       C  
-ATOM   3185  C   SER B 616       1.245  13.595  16.156  1.00 57.51           C  
-ANISOU 3185  C   SER B 616     5978   8427   7446     97    356  -1426       C  
-ATOM   3186  O   SER B 616       1.493  14.360  15.225  1.00 62.26           O  
-ANISOU 3186  O   SER B 616     6552   8946   8160    106    355  -1376       O  
-ATOM   3187  CB  SER B 616      -0.649  12.239  15.270  1.00 83.11           C  
-ANISOU 3187  CB  SER B 616     9379  11602  10597     -7    410  -1332       C  
-ATOM   3188  OG  SER B 616      -1.246  10.956  15.228  1.00 85.63           O  
-ANISOU 3188  OG  SER B 616     9805  11939  10792    -25    445  -1262       O  
-ATOM   3189  N   ILE B 617       1.384  13.938  17.432  1.00 56.61           N  
-ANISOU 3189  N   ILE B 617     5788   8382   7339     83    339  -1571       N  
-ATOM   3190  CA  ILE B 617       1.742  15.294  17.837  1.00 60.73           C  
-ANISOU 3190  CA  ILE B 617     6188   8871   8015     67    321  -1700       C  
-ATOM   3191  C   ILE B 617       2.991  15.837  17.137  1.00 45.47           C  
-ANISOU 3191  C   ILE B 617     4213   6922   6139    148    306  -1609       C  
-ATOM   3192  O   ILE B 617       3.038  17.009  16.760  1.00 37.01           O  
-ANISOU 3192  O   ILE B 617     3066   5753   5244    122    306  -1646       O  
-ATOM   3193  CB  ILE B 617       1.917  15.395  19.371  1.00 71.85           C  
-ANISOU 3193  CB  ILE B 617     7523  10388   9389     59    303  -1860       C  
-ATOM   3194  CG1 ILE B 617       2.475  16.766  19.761  1.00 76.73           C  
-ANISOU 3194  CG1 ILE B 617     8012  10974  10166     58    286  -1986       C  
-ATOM   3195  CG2 ILE B 617       2.818  14.281  19.884  1.00 66.78           C  
-ANISOU 3195  CG2 ILE B 617     6924   9891   8559    159    292  -1779       C  
-ATOM   3196  CD1 ILE B 617       1.569  17.925  19.398  1.00 79.74           C  
-ANISOU 3196  CD1 ILE B 617     8345  11203  10749    -18    304  -2076       C  
-ATOM   3197  N   LEU B 618       3.996  14.986  16.960  1.00 28.74           N  
-ANISOU 3197  N   LEU B 618     2142   4902   3875    250    297  -1485       N  
-ATOM   3198  CA  LEU B 618       5.256  15.417  16.363  1.00 38.10           C  
-ANISOU 3198  CA  LEU B 618     3282   6104   5091    328    283  -1399       C  
-ATOM   3199  C   LEU B 618       5.086  15.917  14.931  1.00 47.92           C  
-ANISOU 3199  C   LEU B 618     4538   7222   6449    306    298  -1285       C  
-ATOM   3200  O   LEU B 618       5.824  16.790  14.476  1.00 34.16           O  
-ANISOU 3200  O   LEU B 618     2716   5446   4817    322    289  -1258       O  
-ATOM   3201  CB  LEU B 618       6.284  14.287  16.406  1.00 43.39           C  
-ANISOU 3201  CB  LEU B 618     4014   6912   5560    458    275  -1283       C  
-ATOM   3202  CG  LEU B 618       6.776  13.876  17.792  1.00 43.55           C  
-ANISOU 3202  CG  LEU B 618     4007   7076   5465    514    256  -1373       C  
-ATOM   3203  CD1 LEU B 618       7.772  12.734  17.685  1.00 40.49           C  
-ANISOU 3203  CD1 LEU B 618     3696   6808   4879    669    254  -1237       C  
-ATOM   3204  CD2 LEU B 618       7.399  15.064  18.507  1.00 42.87           C  
-ANISOU 3204  CD2 LEU B 618     3775   7021   5493    493    233  -1512       C  
-ATOM   3205  N   TRP B 619       4.111  15.361  14.221  1.00 55.21           N  
-ANISOU 3205  N   TRP B 619     5554   8080   7344    267    321  -1217       N  
-ATOM   3206  CA  TRP B 619       3.896  15.712  12.823  1.00 40.84           C  
-ANISOU 3206  CA  TRP B 619     3752   6153   5612    252    336  -1098       C  
-ATOM   3207  C   TRP B 619       2.812  16.767  12.659  1.00 52.08           C  
-ANISOU 3207  C   TRP B 619     5127   7438   7225    157    348  -1185       C  
-ATOM   3208  O   TRP B 619       2.316  16.990  11.554  1.00 55.27           O  
-ANISOU 3208  O   TRP B 619     5554   7748   7696    136    364  -1095       O  
-ATOM   3209  CB  TRP B 619       3.541  14.467  12.012  1.00 39.16           C  
-ANISOU 3209  CB  TRP B 619     3668   5957   5253    279    355   -960       C  
-ATOM   3210  CG  TRP B 619       4.655  13.472  11.937  1.00 37.13           C  
-ANISOU 3210  CG  TRP B 619     3465   5820   4825    400    348   -848       C  
-ATOM   3211  CD1 TRP B 619       5.607  13.382  10.966  1.00 35.27           C  
-ANISOU 3211  CD1 TRP B 619     3235   5610   4555    480    346   -707       C  
-ATOM   3212  CD2 TRP B 619       4.936  12.427  12.875  1.00 46.92           C  
-ANISOU 3212  CD2 TRP B 619     4759   7169   5900    467    344   -866       C  
-ATOM   3213  NE1 TRP B 619       6.462  12.345  11.238  1.00 37.32           N  
-ANISOU 3213  NE1 TRP B 619     3554   5992   4635    601    341   -642       N  
-ATOM   3214  CE2 TRP B 619       6.073  11.742  12.405  1.00 42.65           C  
-ANISOU 3214  CE2 TRP B 619     4263   6712   5231    602    340   -733       C  
-ATOM   3215  CE3 TRP B 619       4.337  12.004  14.064  1.00 55.64           C  
-ANISOU 3215  CE3 TRP B 619     5878   8310   6952    433    346   -977       C  
-ATOM   3216  CZ2 TRP B 619       6.624  10.655  13.084  1.00 43.75           C  
-ANISOU 3216  CZ2 TRP B 619     4470   6956   5196    718    339   -706       C  
-ATOM   3217  CZ3 TRP B 619       4.884  10.927  14.736  1.00 55.53           C  
-ANISOU 3217  CZ3 TRP B 619     5929   8399   6771    538    347   -942       C  
-ATOM   3218  CH2 TRP B 619       6.016  10.264  14.244  1.00 49.43           C  
-ANISOU 3218  CH2 TRP B 619     5210   7694   5876    687    345   -807       C  
-ATOM   3219  N   MET B 620       2.450  17.416  13.761  1.00 54.81           N  
-ANISOU 3219  N   MET B 620     5401   7774   7652    110    341  -1360       N  
-ATOM   3220  CA  MET B 620       1.396  18.422  13.734  1.00 48.64           C  
-ANISOU 3220  CA  MET B 620     4568   6866   7047     36    355  -1459       C  
-ATOM   3221  C   MET B 620       1.952  19.804  13.432  1.00 53.37           C  
-ANISOU 3221  C   MET B 620     5051   7370   7859     45    345  -1467       C  
-ATOM   3222  O   MET B 620       2.973  20.209  13.986  1.00 57.25           O  
-ANISOU 3222  O   MET B 620     5464   7910   8377     78    324  -1509       O  
-ATOM   3223  CB  MET B 620       0.633  18.447  15.059  1.00 43.35           C  
-ANISOU 3223  CB  MET B 620     3875   6233   6364    -19    357  -1651       C  
-ATOM   3224  CG  MET B 620      -0.042  17.134  15.399  1.00 42.61           C  
-ANISOU 3224  CG  MET B 620     3885   6226   6079    -46    367  -1646       C  
-ATOM   3225  SD  MET B 620      -1.636  17.370  16.203  1.00 89.41           S  
-ANISOU 3225  SD  MET B 620     9800  12130  12042   -149    387  -1831       S  
-ATOM   3226  CE  MET B 620      -2.145  15.667  16.432  1.00 81.78           C  
-ANISOU 3226  CE  MET B 620     8953  11277  10843   -181    396  -1771       C  
-ATOM   3227  N   ALA B 621       1.273  20.518  12.542  1.00 69.63           N  
-ANISOU 3227  N   ALA B 621     7092   9297  10068     17    359  -1422       N  
-ATOM   3228  CA  ALA B 621       1.636  21.890  12.226  1.00 69.70           C  
-ANISOU 3228  CA  ALA B 621     6984   9195  10306     18    350  -1425       C  
-ATOM   3229  C   ALA B 621       1.194  22.801  13.357  1.00 73.08           C  
-ANISOU 3229  C   ALA B 621     7316   9580  10873    -18    347  -1631       C  
-ATOM   3230  O   ALA B 621       0.243  22.488  14.074  1.00 84.69           O  
-ANISOU 3230  O   ALA B 621     8817  11075  12287    -56    359  -1754       O  
-ATOM   3231  CB  ALA B 621       0.995  22.321  10.923  1.00 39.18           C  
-ANISOU 3231  CB  ALA B 621     3127   5207   6553      7    365  -1303       C  
-ATOM   3232  N   PRO B 622       1.884  23.936  13.520  1.00 60.26           N  
-ANISOU 3232  N   PRO B 622     5569   7897   9431    -10    330  -1673       N  
-ATOM   3233  CA  PRO B 622       1.504  24.904  14.551  1.00 64.77           C  
-ANISOU 3233  CA  PRO B 622     6034   8418  10157    -40    326  -1873       C  
-ATOM   3234  C   PRO B 622       0.015  25.218  14.472  1.00 70.77           C  
-ANISOU 3234  C   PRO B 622     6805   9085  11001    -80    349  -1943       C  
-ATOM   3235  O   PRO B 622      -0.644  25.341  15.502  1.00 81.57           O  
-ANISOU 3235  O   PRO B 622     8146  10475  12371   -109    356  -2121       O  
-ATOM   3236  CB  PRO B 622       2.328  26.139  14.182  1.00 48.41           C  
-ANISOU 3236  CB  PRO B 622     3836   6252   8306    -27    309  -1842       C  
-ATOM   3237  CG  PRO B 622       3.529  25.588  13.491  1.00 42.65           C  
-ANISOU 3237  CG  PRO B 622     3140   5601   7464     16    296  -1671       C  
-ATOM   3238  CD  PRO B 622       3.053  24.379  12.741  1.00 38.36           C  
-ANISOU 3238  CD  PRO B 622     2742   5105   6730     26    313  -1537       C  
-ATOM   3239  N   GLU B 623      -0.501  25.331  13.252  1.00 61.42           N  
-ANISOU 3239  N   GLU B 623     5653   7809   9875    -80    361  -1801       N  
-ATOM   3240  CA  GLU B 623      -1.912  25.612  13.021  1.00 52.43           C  
-ANISOU 3240  CA  GLU B 623     4521   6591   8808   -110    382  -1844       C  
-ATOM   3241  C   GLU B 623      -2.794  24.477  13.527  1.00 50.88           C  
-ANISOU 3241  C   GLU B 623     4432   6502   8398   -139    403  -1910       C  
-ATOM   3242  O   GLU B 623      -3.875  24.709  14.068  1.00 54.01           O  
-ANISOU 3242  O   GLU B 623     4809   6886   8826   -172    419  -2045       O  
-ATOM   3243  CB  GLU B 623      -2.155  25.823  11.530  1.00 60.91           C  
-ANISOU 3243  CB  GLU B 623     5614   7572   9956    -97    389  -1654       C  
-ATOM   3244  CG  GLU B 623      -0.905  25.646  10.689  1.00 68.07           C  
-ANISOU 3244  CG  GLU B 623     6533   8495  10837    -61    373  -1473       C  
-ATOM   3245  CD  GLU B 623      -1.201  25.044   9.334  1.00 85.89           C  
-ANISOU 3245  CD  GLU B 623     8877  10746  13010    -50    386  -1279       C  
-ATOM   3246  OE1 GLU B 623      -0.469  25.351   8.376  1.00 89.97           O  
-ANISOU 3246  OE1 GLU B 623     9367  11225  13591    -25    376  -1122       O  
-ATOM   3247  OE2 GLU B 623      -2.168  24.262   9.225  1.00 95.74           O  
-ANISOU 3247  OE2 GLU B 623    10216  12034  14126    -69    408  -1285       O  
-ATOM   3248  N   VAL B 624      -2.331  23.247  13.338  1.00 76.52           N  
-ANISOU 3248  N   VAL B 624     7788   9858  11429   -127    403  -1811       N  
-ATOM   3249  CA  VAL B 624      -3.064  22.076  13.804  1.00 88.76           C  
-ANISOU 3249  CA  VAL B 624     9440  11514  12770   -160    419  -1857       C  
-ATOM   3250  C   VAL B 624      -3.086  22.042  15.326  1.00 96.69           C  
-ANISOU 3250  C   VAL B 624    10406  12603  13729   -184    413  -2054       C  
-ATOM   3251  O   VAL B 624      -4.089  21.675  15.939  1.00108.10           O  
-ANISOU 3251  O   VAL B 624    11879  14097  15098   -230    431  -2166       O  
-ATOM   3252  CB  VAL B 624      -2.435  20.771  13.283  1.00 70.31           C  
-ANISOU 3252  CB  VAL B 624     7218   9271  10225   -135    416  -1702       C  
-ATOM   3253  CG1 VAL B 624      -3.113  19.567  13.912  1.00 70.67           C  
-ANISOU 3253  CG1 VAL B 624     7356   9428  10067   -175    428  -1758       C  
-ATOM   3254  CG2 VAL B 624      -2.525  20.706  11.767  1.00 65.69           C  
-ANISOU 3254  CG2 VAL B 624     6678   8619   9664   -115    425  -1513       C  
-ATOM   3255  N   ILE B 625      -1.969  22.433  15.928  1.00 80.01           N  
-ANISOU 3255  N   ILE B 625     8222  10519  11659   -154    389  -2098       N  
-ATOM   3256  CA  ILE B 625      -1.823  22.426  17.377  1.00 69.03           C  
-ANISOU 3256  CA  ILE B 625     6783   9223  10223   -170    379  -2280       C  
-ATOM   3257  C   ILE B 625      -2.602  23.565  18.038  1.00 65.12           C  
-ANISOU 3257  C   ILE B 625     6180   8653   9909   -200    389  -2469       C  
-ATOM   3258  O   ILE B 625      -3.230  23.378  19.081  1.00 66.43           O  
-ANISOU 3258  O   ILE B 625     6337   8894  10011   -237    397  -2629       O  
-ATOM   3259  CB  ILE B 625      -0.335  22.491  17.775  1.00 54.33           C  
-ANISOU 3259  CB  ILE B 625     4870   7428   8343   -123    350  -2264       C  
-ATOM   3260  CG1 ILE B 625       0.309  21.110  17.621  1.00 29.60           C  
-ANISOU 3260  CG1 ILE B 625     1845   4427   4977    -90    341  -2133       C  
-ATOM   3261  CG2 ILE B 625      -0.180  23.000  19.198  1.00 69.29           C  
-ANISOU 3261  CG2 ILE B 625     6668   9384  10277   -137    340  -2474       C  
-ATOM   3262  CD1 ILE B 625       1.815  21.115  17.751  1.00 35.94           C  
-ANISOU 3262  CD1 ILE B 625     2603   5304   5747    -28    314  -2079       C  
-ATOM   3263  N   ARG B 626      -2.562  24.741  17.420  1.00 61.13           N  
-ANISOU 3263  N   ARG B 626     5589   8005   9633   -184    386  -2446       N  
-ATOM   3264  CA  ARG B 626      -3.277  25.906  17.928  1.00 61.39           C  
-ANISOU 3264  CA  ARG B 626     5509   7951   9866   -203    392  -2613       C  
-ATOM   3265  C   ARG B 626      -4.785  25.759  17.736  1.00 64.94           C  
-ANISOU 3265  C   ARG B 626     5998   8380  10297   -237    421  -2651       C  
-ATOM   3266  O   ARG B 626      -5.576  26.344  18.479  1.00 71.36           O  
-ANISOU 3266  O   ARG B 626     6738   9182  11192   -259    431  -2827       O  
-ATOM   3267  CB  ARG B 626      -2.796  27.179  17.230  1.00 60.31           C  
-ANISOU 3267  CB  ARG B 626     5266   7659   9989   -177    378  -2556       C  
-ATOM   3268  CG  ARG B 626      -1.387  27.612  17.591  1.00 68.69           C  
-ANISOU 3268  CG  ARG B 626     6250   8738  11112   -151    351  -2566       C  
-ATOM   3269  CD  ARG B 626      -1.109  29.017  17.068  1.00 84.72           C  
-ANISOU 3269  CD  ARG B 626     8154  10607  13430   -140    339  -2547       C  
-ATOM   3270  NE  ARG B 626      -0.531  29.025  15.725  1.00 93.32           N  
-ANISOU 3270  NE  ARG B 626     9271  11631  14555   -117    331  -2321       N  
-ATOM   3271  CZ  ARG B 626      -1.235  28.970  14.598  1.00 84.37           C  
-ANISOU 3271  CZ  ARG B 626     8188  10417  13450   -116    343  -2181       C  
-ATOM   3272  NH1 ARG B 626      -2.558  28.888  14.638  1.00 75.45           N  
-ANISOU 3272  NH1 ARG B 626     7088   9265  12315   -137    364  -2242       N  
-ATOM   3273  NH2 ARG B 626      -0.612  28.990  13.427  1.00 84.28           N  
-ANISOU 3273  NH2 ARG B 626     8194  10362  13466    -94    335  -1979       N  
-ATOM   3274  N   ASN B 631     -11.322  25.041  10.819  1.00 84.23           N  
-ANISOU 3274  N   ASN B 631     8698  10596  12710   -285    551  -1982       N  
-ATOM   3275  CA  ASN B 631     -10.651  23.761  10.622  1.00 80.91           C  
-ANISOU 3275  CA  ASN B 631     8407  10261  12074   -292    553  -1884       C  
-ATOM   3276  C   ASN B 631      -9.178  23.970  10.280  1.00 71.34           C  
-ANISOU 3276  C   ASN B 631     7186   8985  10933   -247    524  -1765       C  
-ATOM   3277  O   ASN B 631      -8.855  24.649   9.305  1.00 66.19           O  
-ANISOU 3277  O   ASN B 631     6488   8236  10427   -213    512  -1632       O  
-ATOM   3278  CB  ASN B 631     -11.351  22.952   9.524  1.00 82.79           C  
-ANISOU 3278  CB  ASN B 631     8736  10548  12173   -306    573  -1752       C  
-ATOM   3279  CG  ASN B 631     -11.027  21.467   9.590  1.00 83.92           C  
-ANISOU 3279  CG  ASN B 631     9016  10804  12066   -332    581  -1707       C  
-ATOM   3280  OD1 ASN B 631     -10.655  20.945  10.641  1.00 89.72           O  
-ANISOU 3280  OD1 ASN B 631     9780  11606  12702   -354    577  -1807       O  
-ATOM   3281  ND2 ASN B 631     -11.180  20.778   8.464  1.00 73.74           N  
-ANISOU 3281  ND2 ASN B 631     7805   9537  10675   -330    588  -1555       N  
-ATOM   3282  N   PRO B 632      -8.280  23.395  11.093  1.00 72.62           N  
-ANISOU 3282  N   PRO B 632     7388   9216  10991   -248    513  -1812       N  
-ATOM   3283  CA  PRO B 632      -6.830  23.568  10.934  1.00 76.46           C  
-ANISOU 3283  CA  PRO B 632     7856   9670  11526   -207    486  -1722       C  
-ATOM   3284  C   PRO B 632      -6.251  22.806   9.744  1.00 81.21           C  
-ANISOU 3284  C   PRO B 632     8547  10290  12021   -181    484  -1510       C  
-ATOM   3285  O   PRO B 632      -5.331  23.296   9.089  1.00 76.54           O  
-ANISOU 3285  O   PRO B 632     7914   9636  11530   -144    466  -1390       O  
-ATOM   3286  CB  PRO B 632      -6.269  22.991  12.236  1.00 58.14           C  
-ANISOU 3286  CB  PRO B 632     5557   7452   9082   -220    478  -1848       C  
-ATOM   3287  CG  PRO B 632      -7.294  22.006  12.682  1.00 52.03           C  
-ANISOU 3287  CG  PRO B 632     4867   6782   8119   -271    502  -1924       C  
-ATOM   3288  CD  PRO B 632      -8.615  22.593  12.282  1.00 52.06           C  
-ANISOU 3288  CD  PRO B 632     4832   6733   8216   -291    524  -1963       C  
-ATOM   3289  N   TYR B 633      -6.789  21.620   9.476  1.00 79.86           N  
-ANISOU 3289  N   TYR B 633     8488  10207  11647   -204    502  -1469       N  
-ATOM   3290  CA  TYR B 633      -6.245  20.736   8.449  1.00 63.90           C  
-ANISOU 3290  CA  TYR B 633     6559   8222   9500   -180    500  -1285       C  
-ATOM   3291  C   TYR B 633      -6.418  21.254   7.024  1.00 60.21           C  
-ANISOU 3291  C   TYR B 633     6067   7673   9136   -155    502  -1125       C  
-ATOM   3292  O   TYR B 633      -7.485  21.735   6.646  1.00 56.22           O  
-ANISOU 3292  O   TYR B 633     5530   7126   8707   -172    517  -1141       O  
-ATOM   3293  CB  TYR B 633      -6.862  19.344   8.573  1.00 50.74           C  
-ANISOU 3293  CB  TYR B 633     5012   6665   7602   -218    518  -1297       C  
-ATOM   3294  CG  TYR B 633      -6.518  18.648   9.868  1.00 56.92           C  
-ANISOU 3294  CG  TYR B 633     5827   7542   8260   -241    512  -1414       C  
-ATOM   3295  CD1 TYR B 633      -7.281  18.849  11.011  1.00 64.06           C  
-ANISOU 3295  CD1 TYR B 633     6696   8476   9167   -291    522  -1600       C  
-ATOM   3296  CD2 TYR B 633      -5.430  17.790   9.948  1.00 52.55           C  
-ANISOU 3296  CD2 TYR B 633     5330   7055   7583   -210    495  -1335       C  
-ATOM   3297  CE1 TYR B 633      -6.970  18.215  12.198  1.00 67.90           C  
-ANISOU 3297  CE1 TYR B 633     7205   9057   9537   -316    513  -1699       C  
-ATOM   3298  CE2 TYR B 633      -5.111  17.150  11.129  1.00 55.10           C  
-ANISOU 3298  CE2 TYR B 633     5673   7470   7793   -228    485  -1429       C  
-ATOM   3299  CZ  TYR B 633      -5.884  17.366  12.251  1.00 62.71           C  
-ANISOU 3299  CZ  TYR B 633     6601   8462   8763   -284    493  -1609       C  
-ATOM   3300  OH  TYR B 633      -5.573  16.733  13.432  1.00 55.90           O  
-ANISOU 3300  OH  TYR B 633     5750   7700   7788   -306    481  -1695       O  
-ATOM   3301  N   SER B 634      -5.351  21.138   6.241  1.00 68.78           N  
-ANISOU 3301  N   SER B 634     7164   8751  10218   -113    487   -969       N  
-ATOM   3302  CA  SER B 634      -5.358  21.510   4.833  1.00 68.14           C  
-ANISOU 3302  CA  SER B 634     7066   8612  10213    -88    487   -795       C  
-ATOM   3303  C   SER B 634      -4.245  20.750   4.133  1.00 51.52           C  
-ANISOU 3303  C   SER B 634     5021   6564   7989    -50    478   -639       C  
-ATOM   3304  O   SER B 634      -3.523  19.978   4.764  1.00 48.36           O  
-ANISOU 3304  O   SER B 634     4673   6243   7458    -39    471   -670       O  
-ATOM   3305  CB  SER B 634      -5.137  23.015   4.673  1.00 67.89           C  
-ANISOU 3305  CB  SER B 634     6899   8455  10441    -75    472   -786       C  
-ATOM   3306  OG  SER B 634      -3.885  23.406   5.214  1.00 66.80           O  
-ANISOU 3306  OG  SER B 634     6708   8304  10368    -55    450   -804       O  
-ATOM   3307  N   PHE B 635      -4.104  20.964   2.830  1.00 45.71           N  
-ANISOU 3307  N   PHE B 635     4274   5796   7297    -26    476   -471       N  
-ATOM   3308  CA  PHE B 635      -2.973  20.407   2.106  1.00 45.52           C  
-ANISOU 3308  CA  PHE B 635     4288   5825   7182     16    467   -319       C  
-ATOM   3309  C   PHE B 635      -1.696  20.944   2.737  1.00 50.94           C  
-ANISOU 3309  C   PHE B 635     4906   6504   7947     38    446   -344       C  
-ATOM   3310  O   PHE B 635      -0.660  20.281   2.739  1.00 53.39           O  
-ANISOU 3310  O   PHE B 635     5253   6895   8137     72    439   -288       O  
-ATOM   3311  CB  PHE B 635      -3.029  20.790   0.628  1.00 50.52           C  
-ANISOU 3311  CB  PHE B 635     4893   6420   7883     34    468   -139       C  
-ATOM   3312  CG  PHE B 635      -4.265  20.312  -0.078  1.00 56.77           C  
-ANISOU 3312  CG  PHE B 635     5740   7231   8599     16    485   -109       C  
-ATOM   3313  CD1 PHE B 635      -5.189  21.216  -0.576  1.00 64.18           C  
-ANISOU 3313  CD1 PHE B 635     6608   8093   9684      0    490    -92       C  
-ATOM   3314  CD2 PHE B 635      -4.505  18.957  -0.243  1.00 52.75           C  
-ANISOU 3314  CD2 PHE B 635     5348   6821   7875     15    496   -100       C  
-ATOM   3315  CE1 PHE B 635      -6.326  20.778  -1.228  1.00 61.36           C  
-ANISOU 3315  CE1 PHE B 635     6294   7773   9248    -16    506    -67       C  
-ATOM   3316  CE2 PHE B 635      -5.641  18.513  -0.893  1.00 50.09           C  
-ANISOU 3316  CE2 PHE B 635     5055   6512   7466     -7    510    -81       C  
-ATOM   3317  CZ  PHE B 635      -6.552  19.425  -1.386  1.00 53.47           C  
-ANISOU 3317  CZ  PHE B 635     5410   6878   8028    -22    515    -66       C  
-ATOM   3318  N   GLN B 636      -1.791  22.153   3.282  1.00 57.78           N  
-ANISOU 3318  N   GLN B 636     5664   7275   9014     22    437   -433       N  
-ATOM   3319  CA  GLN B 636      -0.662  22.810   3.927  1.00 60.28           C  
-ANISOU 3319  CA  GLN B 636     5897   7578   9429     36    415   -475       C  
-ATOM   3320  C   GLN B 636      -0.176  22.026   5.142  1.00 54.33           C  
-ANISOU 3320  C   GLN B 636     5192   6927   8524     41    411   -598       C  
-ATOM   3321  O   GLN B 636       1.024  21.942   5.396  1.00 59.87           O  
-ANISOU 3321  O   GLN B 636     5871   7687   9190     71    395   -576       O  
-ATOM   3322  CB  GLN B 636      -1.050  24.228   4.347  1.00 75.80           C  
-ANISOU 3322  CB  GLN B 636     7739   9416  11646     13    406   -571       C  
-ATOM   3323  CG  GLN B 636      -1.811  25.000   3.281  1.00 79.93           C  
-ANISOU 3323  CG  GLN B 636     8211   9835  12323      7    412   -469       C  
-ATOM   3324  CD  GLN B 636      -0.998  25.225   2.021  1.00 80.13           C  
-ANISOU 3324  CD  GLN B 636     8208   9848  12390     33    402   -261       C  
-ATOM   3325  OE1 GLN B 636       0.224  25.068   2.017  1.00 74.55           O  
-ANISOU 3325  OE1 GLN B 636     7492   9194  11639     55    388   -207       O  
-ATOM   3326  NE2 GLN B 636      -1.675  25.601   0.943  1.00 87.26           N  
-ANISOU 3326  NE2 GLN B 636     9091  10693  13371     32    408   -143       N  
-ATOM   3327  N   SER B 637      -1.116  21.460   5.894  1.00 39.43           N  
-ANISOU 3327  N   SER B 637     3364   5072   6544     10    424   -726       N  
-ATOM   3328  CA  SER B 637      -0.784  20.652   7.059  1.00 35.35           C  
-ANISOU 3328  CA  SER B 637     2895   4660   5876     10    420   -838       C  
-ATOM   3329  C   SER B 637      -0.036  19.410   6.602  1.00 39.48           C  
-ANISOU 3329  C   SER B 637     3513   5294   6193     52    420   -715       C  
-ATOM   3330  O   SER B 637       0.982  19.032   7.186  1.00 43.52           O  
-ANISOU 3330  O   SER B 637     4024   5891   6621     88    405   -727       O  
-ATOM   3331  CB  SER B 637      -2.054  20.248   7.804  1.00 44.16           C  
-ANISOU 3331  CB  SER B 637     4058   5793   6929    -40    438   -981       C  
-ATOM   3332  OG  SER B 637      -3.064  21.229   7.656  1.00 53.97           O  
-ANISOU 3332  OG  SER B 637     5236   6932   8340    -70    448  -1037       O  
-ATOM   3333  N   ASP B 638      -0.554  18.781   5.552  1.00 41.67           N  
-ANISOU 3333  N   ASP B 638     3867   5576   6391     53    435   -597       N  
-ATOM   3334  CA  ASP B 638       0.078  17.610   4.955  1.00 36.77           C  
-ANISOU 3334  CA  ASP B 638     3334   5051   5587    100    437   -470       C  
-ATOM   3335  C   ASP B 638       1.504  17.921   4.515  1.00 32.59           C  
-ANISOU 3335  C   ASP B 638     2751   4550   5081    157    421   -360       C  
-ATOM   3336  O   ASP B 638       2.404  17.091   4.656  1.00 41.61           O  
-ANISOU 3336  O   ASP B 638     3936   5798   6076    211    415   -316       O  
-ATOM   3337  CB  ASP B 638      -0.739  17.109   3.762  1.00 37.48           C  
-ANISOU 3337  CB  ASP B 638     3492   5125   5623     90    455   -362       C  
-ATOM   3338  CG  ASP B 638      -1.957  16.311   4.182  1.00 44.20           C  
-ANISOU 3338  CG  ASP B 638     4425   6001   6371     41    471   -455       C  
-ATOM   3339  OD1 ASP B 638      -2.203  16.189   5.401  1.00 43.82           O  
-ANISOU 3339  OD1 ASP B 638     4376   5976   6296     11    470   -600       O  
-ATOM   3340  OD2 ASP B 638      -2.665  15.800   3.289  1.00 49.21           O  
-ANISOU 3340  OD2 ASP B 638     5117   6637   6945     30    484   -383       O  
-ATOM   3341  N   VAL B 639       1.701  19.122   3.980  1.00 17.19           N  
-ANISOU 3341  N   VAL B 639      703   2510   3319    149    414   -313       N  
-ATOM   3342  CA  VAL B 639       3.027  19.567   3.566  1.00 32.50           C  
-ANISOU 3342  CA  VAL B 639     2572   4474   5301    192    399   -215       C  
-ATOM   3343  C   VAL B 639       3.988  19.602   4.753  1.00 39.92           C  
-ANISOU 3343  C   VAL B 639     3470   5486   6213    216    381   -319       C  
-ATOM   3344  O   VAL B 639       5.140  19.182   4.639  1.00 51.17           O  
-ANISOU 3344  O   VAL B 639     4893   7013   7535    273    372   -248       O  
-ATOM   3345  CB  VAL B 639       2.975  20.953   2.887  1.00 44.93           C  
-ANISOU 3345  CB  VAL B 639     4035   5926   7110    169    392   -157       C  
-ATOM   3346  CG1 VAL B 639       4.380  21.492   2.656  1.00 37.14           C  
-ANISOU 3346  CG1 VAL B 639     2960   4972   6180    202    374    -78       C  
-ATOM   3347  CG2 VAL B 639       2.206  20.872   1.575  1.00 43.97           C  
-ANISOU 3347  CG2 VAL B 639     3949   5759   6998    160    408    -23       C  
-ATOM   3348  N   TYR B 640       3.505  20.096   5.892  1.00 39.85           N  
-ANISOU 3348  N   TYR B 640     3419   5434   6286    177    375   -489       N  
-ATOM   3349  CA  TYR B 640       4.317  20.167   7.106  1.00 30.23           C  
-ANISOU 3349  CA  TYR B 640     2153   4289   5042    196    356   -606       C  
-ATOM   3350  C   TYR B 640       4.694  18.776   7.599  1.00 33.17           C  
-ANISOU 3350  C   TYR B 640     2623   4810   5172    244    357   -607       C  
-ATOM   3351  O   TYR B 640       5.859  18.503   7.879  1.00 40.64           O  
-ANISOU 3351  O   TYR B 640     3548   5862   6030    304    343   -583       O  
-ATOM   3352  CB  TYR B 640       3.584  20.932   8.213  1.00 34.99           C  
-ANISOU 3352  CB  TYR B 640     2697   4821   5778    142    353   -797       C  
-ATOM   3353  CG  TYR B 640       4.357  21.010   9.516  1.00 29.01           C  
-ANISOU 3353  CG  TYR B 640     1884   4148   4991    159    333   -930       C  
-ATOM   3354  CD1 TYR B 640       5.216  22.071   9.775  1.00 28.10           C  
-ANISOU 3354  CD1 TYR B 640     1643   4009   5026    164    313   -966       C  
-ATOM   3355  CD2 TYR B 640       4.229  20.022  10.483  1.00 23.20           C  
-ANISOU 3355  CD2 TYR B 640     1217   3522   4078    168    333  -1018       C  
-ATOM   3356  CE1 TYR B 640       5.924  22.145  10.961  1.00 35.11           C  
-ANISOU 3356  CE1 TYR B 640     2474   4986   5881    179    295  -1093       C  
-ATOM   3357  CE2 TYR B 640       4.932  20.088  11.672  1.00 26.96           C  
-ANISOU 3357  CE2 TYR B 640     1637   4087   4519    188    314  -1136       C  
-ATOM   3358  CZ  TYR B 640       5.779  21.152  11.905  1.00 38.83           C  
-ANISOU 3358  CZ  TYR B 640     3015   5572   6168    194    296  -1177       C  
-ATOM   3359  OH  TYR B 640       6.483  21.224  13.085  1.00 51.19           O  
-ANISOU 3359  OH  TYR B 640     4518   7238   7693    214    276  -1300       O  
-ATOM   3360  N   ALA B 641       3.697  17.904   7.706  1.00 34.99           N  
-ANISOU 3360  N   ALA B 641     2954   5047   5293    221    373   -632       N  
-ATOM   3361  CA  ALA B 641       3.921  16.529   8.138  1.00 30.36           C  
-ANISOU 3361  CA  ALA B 641     2465   4585   4486    267    375   -623       C  
-ATOM   3362  C   ALA B 641       4.958  15.851   7.250  1.00 42.30           C  
-ANISOU 3362  C   ALA B 641     4016   6181   5874    354    375   -456       C  
-ATOM   3363  O   ALA B 641       5.800  15.092   7.730  1.00 48.22           O  
-ANISOU 3363  O   ALA B 641     4794   7052   6476    430    366   -445       O  
-ATOM   3364  CB  ALA B 641       2.619  15.751   8.130  1.00 26.22           C  
-ANISOU 3364  CB  ALA B 641     2037   4038   3885    219    394   -650       C  
-ATOM   3365  N   PHE B 642       4.883  16.128   5.953  1.00 33.03           N  
-ANISOU 3365  N   PHE B 642     2841   4950   4759    349    386   -327       N  
-ATOM   3366  CA  PHE B 642       5.849  15.605   4.998  1.00 22.55           C  
-ANISOU 3366  CA  PHE B 642     1538   3702   3328    427    388   -168       C  
-ATOM   3367  C   PHE B 642       7.240  16.139   5.314  1.00 29.48           C  
-ANISOU 3367  C   PHE B 642     2320   4653   4226    479    369   -163       C  
-ATOM   3368  O   PHE B 642       8.234  15.418   5.206  1.00 24.34           O  
-ANISOU 3368  O   PHE B 642     1696   4127   3424    571    367    -92       O  
-ATOM   3369  CB  PHE B 642       5.453  15.988   3.572  1.00 39.77           C  
-ANISOU 3369  CB  PHE B 642     3714   5804   5592    400    402    -39       C  
-ATOM   3370  CG  PHE B 642       6.381  15.451   2.524  1.00 39.12           C  
-ANISOU 3370  CG  PHE B 642     3655   5810   5401    476    408    123       C  
-ATOM   3371  CD1 PHE B 642       6.287  14.132   2.109  1.00 35.13           C  
-ANISOU 3371  CD1 PHE B 642     3263   5375   4710    532    422    192       C  
-ATOM   3372  CD2 PHE B 642       7.350  16.262   1.954  1.00 38.82           C  
-ANISOU 3372  CD2 PHE B 642     3518   5784   5447    493    399    207       C  
-ATOM   3373  CE1 PHE B 642       7.142  13.629   1.146  1.00 41.15           C  
-ANISOU 3373  CE1 PHE B 642     4044   6225   5367    611    429    334       C  
-ATOM   3374  CE2 PHE B 642       8.209  15.766   0.990  1.00 43.05           C  
-ANISOU 3374  CE2 PHE B 642     4069   6416   5874    563    407    352       C  
-ATOM   3375  CZ  PHE B 642       8.104  14.446   0.584  1.00 45.77           C  
-ANISOU 3375  CZ  PHE B 642     4529   6835   6027    625    423    413       C  
-ATOM   3376  N   GLY B 643       7.303  17.408   5.703  1.00 33.52           N  
-ANISOU 3376  N   GLY B 643     2719   5089   4928    426    355   -241       N  
-ATOM   3377  CA  GLY B 643       8.559  18.024   6.085  1.00 31.16           C  
-ANISOU 3377  CA  GLY B 643     2314   4856   4670    462    334   -256       C  
-ATOM   3378  C   GLY B 643       9.195  17.292   7.250  1.00 44.99           C  
-ANISOU 3378  C   GLY B 643     4086   6746   6261    527    321   -342       C  
-ATOM   3379  O   GLY B 643      10.413  17.116   7.296  1.00 51.05           O  
-ANISOU 3379  O   GLY B 643     4818   7639   6941    605    310   -297       O  
-ATOM   3380  N   ILE B 644       8.365  16.860   8.194  1.00 51.63           N  
-ANISOU 3380  N   ILE B 644     4982   7576   7059    499    323   -462       N  
-ATOM   3381  CA  ILE B 644       8.847  16.128   9.360  1.00 42.75           C  
-ANISOU 3381  CA  ILE B 644     3880   6582   5781    562    310   -543       C  
-ATOM   3382  C   ILE B 644       9.360  14.745   8.965  1.00 35.20           C  
-ANISOU 3382  C   ILE B 644     3032   5746   4598    674    318   -423       C  
-ATOM   3383  O   ILE B 644      10.376  14.281   9.482  1.00 30.80           O  
-ANISOU 3383  O   ILE B 644     2468   5326   3910    774    305   -419       O  
-ATOM   3384  CB  ILE B 644       7.753  15.987  10.440  1.00 52.51           C  
-ANISOU 3384  CB  ILE B 644     5146   7778   7027    498    311   -695       C  
-ATOM   3385  CG1 ILE B 644       7.322  17.364  10.953  1.00 45.72           C  
-ANISOU 3385  CG1 ILE B 644     4175   6810   6387    407    303   -833       C  
-ATOM   3386  CG2 ILE B 644       8.253  15.132  11.592  1.00 56.38           C  
-ANISOU 3386  CG2 ILE B 644     5665   8411   7345    573    297   -758       C  
-ATOM   3387  CD1 ILE B 644       8.398  18.096  11.734  1.00 46.07           C  
-ANISOU 3387  CD1 ILE B 644     4098   6922   6485    433    278   -914       C  
-ATOM   3388  N   VAL B 645       8.653  14.093   8.047  1.00 41.84           N  
-ANISOU 3388  N   VAL B 645     3972   6534   5392    666    340   -326       N  
-ATOM   3389  CA  VAL B 645       9.078  12.792   7.541  1.00 38.44           C  
-ANISOU 3389  CA  VAL B 645     3648   6195   4761    778    352   -206       C  
-ATOM   3390  C   VAL B 645      10.449  12.908   6.877  1.00 46.84           C  
-ANISOU 3390  C   VAL B 645     4663   7360   5774    870    347    -97       C  
-ATOM   3391  O   VAL B 645      11.319  12.060   7.079  1.00 57.49           O  
-ANISOU 3391  O   VAL B 645     6056   8839   6949   1001    344    -54       O  
-ATOM   3392  CB  VAL B 645       8.057  12.201   6.548  1.00 30.66           C  
-ANISOU 3392  CB  VAL B 645     2763   5127   3761    742    377   -123       C  
-ATOM   3393  CG1 VAL B 645       8.579  10.904   5.955  1.00 31.76           C  
-ANISOU 3393  CG1 VAL B 645     3009   5352   3707    871    389      3       C  
-ATOM   3394  CG2 VAL B 645       6.719  11.972   7.234  1.00 16.74           C  
-ANISOU 3394  CG2 VAL B 645     1048   3286   2026    655    383   -231       C  
-ATOM   3395  N   LEU B 646      10.635  13.962   6.087  1.00 38.58           N  
-ANISOU 3395  N   LEU B 646     3524   6254   4879    809    348    -51       N  
-ATOM   3396  CA  LEU B 646      11.940  14.259   5.504  1.00 34.29           C  
-ANISOU 3396  CA  LEU B 646     2908   5809   4313    877    342     42       C  
-ATOM   3397  C   LEU B 646      12.993  14.340   6.603  1.00 39.23           C  
-ANISOU 3397  C   LEU B 646     3465   6565   4874    948    318    -40       C  
-ATOM   3398  O   LEU B 646      14.059  13.731   6.505  1.00 39.11           O  
-ANISOU 3398  O   LEU B 646     3460   6700   4700   1071    317     24       O  
-ATOM   3399  CB  LEU B 646      11.903  15.578   4.728  1.00 30.41           C  
-ANISOU 3399  CB  LEU B 646     2306   5215   4034    784    341     81       C  
-ATOM   3400  CG  LEU B 646      11.132  15.611   3.407  1.00 32.55           C  
-ANISOU 3400  CG  LEU B 646     2620   5385   4363    733    363    196       C  
-ATOM   3401  CD1 LEU B 646      11.158  17.006   2.798  1.00 34.77           C  
-ANISOU 3401  CD1 LEU B 646     2781   5563   4868    653    355    233       C  
-ATOM   3402  CD2 LEU B 646      11.696  14.591   2.432  1.00 21.30           C  
-ANISOU 3402  CD2 LEU B 646     1268   4070   2757    830    381    341       C  
-ATOM   3403  N   TYR B 647      12.679  15.098   7.649  1.00 47.89           N  
-ANISOU 3403  N   TYR B 647     4492   7611   6093    874    301   -186       N  
-ATOM   3404  CA  TYR B 647      13.568  15.261   8.792  1.00 38.90           C  
-ANISOU 3404  CA  TYR B 647     3278   6594   4909    928    276   -285       C  
-ATOM   3405  C   TYR B 647      13.960  13.914   9.396  1.00 45.64           C  
-ANISOU 3405  C   TYR B 647     4230   7591   5520   1065    274   -277       C  
-ATOM   3406  O   TYR B 647      15.086  13.738   9.862  1.00 49.35           O  
-ANISOU 3406  O   TYR B 647     4655   8216   5879   1169    259   -281       O  
-ATOM   3407  CB  TYR B 647      12.906  16.142   9.855  1.00 38.47           C  
-ANISOU 3407  CB  TYR B 647     3154   6448   5015    822    262   -456       C  
-ATOM   3408  CG  TYR B 647      13.766  16.385  11.074  1.00 52.04           C  
-ANISOU 3408  CG  TYR B 647     4783   8293   6697    866    236   -572       C  
-ATOM   3409  CD1 TYR B 647      14.635  17.466  11.129  1.00 60.99           C  
-ANISOU 3409  CD1 TYR B 647     5770   9454   7949    845    218   -601       C  
-ATOM   3410  CD2 TYR B 647      13.709  15.532  12.169  1.00 46.94           C  
-ANISOU 3410  CD2 TYR B 647     4194   7743   5896    930    228   -649       C  
-ATOM   3411  CE1 TYR B 647      15.426  17.691  12.240  1.00 62.52           C  
-ANISOU 3411  CE1 TYR B 647     5875   9776   8106    882    195   -711       C  
-ATOM   3412  CE2 TYR B 647      14.496  15.749  13.284  1.00 57.00           C  
-ANISOU 3412  CE2 TYR B 647     5382   9146   7129    974    204   -754       C  
-ATOM   3413  CZ  TYR B 647      15.352  16.830  13.314  1.00 59.76           C  
-ANISOU 3413  CZ  TYR B 647     5583   9528   7595    948    188   -789       C  
-ATOM   3414  OH  TYR B 647      16.136  17.051  14.422  1.00 63.57           O  
-ANISOU 3414  OH  TYR B 647     5971  10150   8032    989    164   -899       O  
-ATOM   3415  N   GLU B 648      13.026  12.968   9.387  1.00 40.26           N  
-ANISOU 3415  N   GLU B 648     3682   6857   4758   1071    290   -262       N  
-ATOM   3416  CA  GLU B 648      13.279  11.638   9.930  1.00 40.15           C  
-ANISOU 3416  CA  GLU B 648     3780   6950   4527   1210    290   -241       C  
-ATOM   3417  C   GLU B 648      14.263  10.859   9.066  1.00 45.48           C  
-ANISOU 3417  C   GLU B 648     4508   7735   5037   1361    300    -94       C  
-ATOM   3418  O   GLU B 648      15.015  10.025   9.568  1.00 45.88           O  
-ANISOU 3418  O   GLU B 648     4608   7915   4909   1516    292    -76       O  
-ATOM   3419  CB  GLU B 648      11.977  10.844  10.042  1.00 45.26           C  
-ANISOU 3419  CB  GLU B 648     4554   7493   5150   1170    307   -252       C  
-ATOM   3420  CG  GLU B 648      10.950  11.432  10.987  1.00 54.82           C  
-ANISOU 3420  CG  GLU B 648     5723   8615   6490   1035    300   -404       C  
-ATOM   3421  CD  GLU B 648       9.744  10.528  11.157  1.00 56.34           C  
-ANISOU 3421  CD  GLU B 648     6040   8732   6635   1006    320   -410       C  
-ATOM   3422  OE1 GLU B 648       9.913   9.394  11.653  1.00 60.27           O  
-ANISOU 3422  OE1 GLU B 648     6636   9289   6973   1120    325   -382       O  
-ATOM   3423  OE2 GLU B 648       8.629  10.952  10.792  1.00 47.99           O  
-ANISOU 3423  OE2 GLU B 648     4982   7550   5703    875    333   -441       O  
-ATOM   3424  N   LEU B 649      14.243  11.128   7.765  1.00 49.75           N  
-ANISOU 3424  N   LEU B 649     5042   8227   5636   1323    318     12       N  
-ATOM   3425  CA  LEU B 649      15.082  10.410   6.814  1.00 50.01           C  
-ANISOU 3425  CA  LEU B 649     5124   8360   5517   1457    332    152       C  
-ATOM   3426  C   LEU B 649      16.499  10.970   6.782  1.00 50.55           C  
-ANISOU 3426  C   LEU B 649     5068   8578   5559   1521    319    170       C  
-ATOM   3427  O   LEU B 649      17.476  10.220   6.778  1.00 53.22           O  
-ANISOU 3427  O   LEU B 649     5440   9068   5711   1686    319    225       O  
-ATOM   3428  CB  LEU B 649      14.470  10.472   5.413  1.00 43.23           C  
-ANISOU 3428  CB  LEU B 649     4299   7399   4726   1386    358    258       C  
-ATOM   3429  CG  LEU B 649      13.095   9.834   5.217  1.00 28.73           C  
-ANISOU 3429  CG  LEU B 649     2586   5429   2903   1329    374    259       C  
-ATOM   3430  CD1 LEU B 649      12.499  10.243   3.881  1.00 25.07           C  
-ANISOU 3430  CD1 LEU B 649     2112   4869   2546   1232    394    345       C  
-ATOM   3431  CD2 LEU B 649      13.179   8.322   5.329  1.00 23.16           C  
-ANISOU 3431  CD2 LEU B 649     2034   4772   1993   1487    381    311       C  
-ATOM   3432  N   MET B 650      16.603  12.295   6.761  1.00 46.60           N  
-ANISOU 3432  N   MET B 650     4424   8032   5250   1398    307    124       N  
-ATOM   3433  CA  MET B 650      17.892  12.962   6.620  1.00 52.04           C  
-ANISOU 3433  CA  MET B 650     4976   8850   5945   1434    293    147       C  
-ATOM   3434  C   MET B 650      18.684  13.013   7.929  1.00 65.79           C  
-ANISOU 3434  C   MET B 650     6651  10730   7615   1506    265     38       C  
-ATOM   3435  O   MET B 650      19.883  13.290   7.920  1.00 64.73           O  
-ANISOU 3435  O   MET B 650     6416  10748   7428   1574    253     58       O  
-ATOM   3436  CB  MET B 650      17.704  14.377   6.067  1.00 40.15           C  
-ANISOU 3436  CB  MET B 650     3344   7228   4684   1280    288    149       C  
-ATOM   3437  CG  MET B 650      16.887  14.454   4.782  1.00 38.19           C  
-ANISOU 3437  CG  MET B 650     3146   6843   4522   1203    314    255       C  
-ATOM   3438  SD  MET B 650      17.670  13.693   3.342  1.00 63.82           S  
-ANISOU 3438  SD  MET B 650     6433  10212   7603   1316    340    441       S  
-ATOM   3439  CE  MET B 650      16.828  12.113   3.279  1.00 64.14           C  
-ANISOU 3439  CE  MET B 650     6680  10229   7461   1400    365    465       C  
-ATOM   3440  N   THR B 651      18.014  12.752   9.048  1.00 80.29           N  
-ANISOU 3440  N   THR B 651     8536  12523   9446   1490    254    -76       N  
-ATOM   3441  CA  THR B 651      18.685  12.727  10.346  1.00 73.98           C  
-ANISOU 3441  CA  THR B 651     7680  11861   8568   1561    228   -182       C  
-ATOM   3442  C   THR B 651      18.612  11.345  10.984  1.00 71.25           C  
-ANISOU 3442  C   THR B 651     7477  11588   8005   1713    229   -175       C  
-ATOM   3443  O   THR B 651      19.555  10.902  11.639  1.00 71.48           O  
-ANISOU 3443  O   THR B 651     7491  11789   7877   1857    213   -188       O  
-ATOM   3444  CB  THR B 651      18.086  13.758  11.329  1.00 53.37           C  
-ANISOU 3444  CB  THR B 651     4976   9158   6146   1415    209   -344       C  
-ATOM   3445  OG1 THR B 651      16.790  13.323  11.760  1.00 39.53           O  
-ANISOU 3445  OG1 THR B 651     3329   7277   4415   1357    218   -400       O  
-ATOM   3446  CG2 THR B 651      17.972  15.123  10.673  1.00 56.00           C  
-ANISOU 3446  CG2 THR B 651     5188   9372   6716   1269    209   -346       C  
-ATOM   3447  N   GLY B 652      17.486  10.668  10.787  1.00 64.65           N  
-ANISOU 3447  N   GLY B 652     6780  10620   7165   1684    247   -151       N  
-ATOM   3448  CA  GLY B 652      17.268   9.368  11.391  1.00 60.71           C  
-ANISOU 3448  CA  GLY B 652     6427  10151   6490   1818    248   -139       C  
-ATOM   3449  C   GLY B 652      16.580   9.492  12.736  1.00 67.08           C  
-ANISOU 3449  C   GLY B 652     7223  10919   7345   1753    233   -280       C  
-ATOM   3450  O   GLY B 652      16.112   8.503  13.299  1.00 69.24           O  
-ANISOU 3450  O   GLY B 652     7620  11173   7516   1827    237   -279       O  
-ATOM   3451  N   GLN B 653      16.514  10.716  13.250  1.00 72.43           N  
-ANISOU 3451  N   GLN B 653     7753  11579   8186   1615    217   -401       N  
-ATOM   3452  CA  GLN B 653      15.922  10.968  14.560  1.00 72.92           C  
-ANISOU 3452  CA  GLN B 653     7782  11622   8301   1545    203   -552       C  
-ATOM   3453  C   GLN B 653      14.552  11.632  14.460  1.00 72.73           C  
-ANISOU 3453  C   GLN B 653     7750  11408   8474   1351    214   -625       C  
-ATOM   3454  O   GLN B 653      14.222  12.257  13.451  1.00 76.28           O  
-ANISOU 3454  O   GLN B 653     8176  11748   9060   1255    227   -579       O  
-ATOM   3455  CB  GLN B 653      16.849  11.840  15.412  1.00 65.73           C  
-ANISOU 3455  CB  GLN B 653     6708  10842   7423   1545    175   -662       C  
-ATOM   3456  CG  GLN B 653      18.192  11.206  15.739  1.00 67.01           C  
-ANISOU 3456  CG  GLN B 653     6863  11219   7377   1742    160   -614       C  
-ATOM   3457  CD  GLN B 653      18.989  12.021  16.740  1.00 81.60           C  
-ANISOU 3457  CD  GLN B 653     8547  13206   9253   1732    133   -741       C  
-ATOM   3458  OE1 GLN B 653      19.994  11.556  17.278  1.00 93.73           O  
-ANISOU 3458  OE1 GLN B 653    10061  14933  10619   1886    118   -733       O  
-ATOM   3459  NE2 GLN B 653      18.538  13.243  17.000  1.00 85.51           N  
-ANISOU 3459  NE2 GLN B 653     8924  13606   9961   1557    126   -862       N  
-ATOM   3460  N   LEU B 654      13.762  11.486  15.519  1.00 61.56           N  
-ANISOU 3460  N   LEU B 654     6354   9964   7070   1301    210   -738       N  
-ATOM   3461  CA  LEU B 654      12.486  12.178  15.635  1.00 52.83           C  
-ANISOU 3461  CA  LEU B 654     5224   8704   6144   1123    219   -836       C  
-ATOM   3462  C   LEU B 654      12.727  13.607  16.102  1.00 57.13           C  
-ANISOU 3462  C   LEU B 654     5604   9238   6864   1022    200   -971       C  
-ATOM   3463  O   LEU B 654      13.728  13.887  16.765  1.00 58.82           O  
-ANISOU 3463  O   LEU B 654     5726   9585   7036   1083    179  -1024       O  
-ATOM   3464  CB  LEU B 654      11.566  11.450  16.618  1.00 45.10           C  
-ANISOU 3464  CB  LEU B 654     4323   7712   5102   1108    226   -908       C  
-ATOM   3465  CG  LEU B 654      10.957  10.131  16.140  1.00 46.44           C  
-ANISOU 3465  CG  LEU B 654     4665   7827   5152   1169    254   -788       C  
-ATOM   3466  CD1 LEU B 654      10.328   9.365  17.297  1.00 51.23           C  
-ANISOU 3466  CD1 LEU B 654     5340   8448   5677   1180    266   -854       C  
-ATOM   3467  CD2 LEU B 654       9.936  10.377  15.040  1.00 32.10           C  
-ANISOU 3467  CD2 LEU B 654     2885   5853   3458   1046    277   -742       C  
-ATOM   3468  N   PRO B 655      11.810  14.521  15.755  1.00 48.76           N  
-ANISOU 3468  N   PRO B 655     4506   8017   6004    874    210  -1027       N  
-ATOM   3469  CA  PRO B 655      11.967  15.929  16.128  1.00 51.55           C  
-ANISOU 3469  CA  PRO B 655     4711   8326   6550    783    197  -1153       C  
-ATOM   3470  C   PRO B 655      11.941  16.101  17.639  1.00 71.33           C  
-ANISOU 3470  C   PRO B 655     7151  10913   9040    770    179  -1328       C  
-ATOM   3471  O   PRO B 655      11.331  15.292  18.338  1.00 74.08           O  
-ANISOU 3471  O   PRO B 655     7573  11294   9279    782    182  -1366       O  
-ATOM   3472  CB  PRO B 655      10.731  16.596  15.512  1.00 28.68           C  
-ANISOU 3472  CB  PRO B 655     1827   5229   3843    651    216  -1171       C  
-ATOM   3473  CG  PRO B 655      10.248  15.643  14.468  1.00 33.02           C  
-ANISOU 3473  CG  PRO B 655     2512   5735   4299    678    238  -1017       C  
-ATOM   3474  CD  PRO B 655      10.569  14.285  15.001  1.00 28.43           C  
-ANISOU 3474  CD  PRO B 655     2024   5291   3486    793    235   -978       C  
-ATOM   3475  N   TYR B 656      12.603  17.141  18.133  1.00 75.93           N  
-ANISOU 3475  N   TYR B 656     7591  11530   9730    745    162  -1431       N  
-ATOM   3476  CA  TYR B 656      12.528  17.495  19.544  1.00 60.10           C  
-ANISOU 3476  CA  TYR B 656     5504   9592   7738    714    147  -1617       C  
-ATOM   3477  C   TYR B 656      12.971  16.350  20.454  1.00 62.57           C  
-ANISOU 3477  C   TYR B 656     5866  10094   7814    830    135  -1616       C  
-ATOM   3478  O   TYR B 656      12.177  15.823  21.233  1.00 64.27           O  
-ANISOU 3478  O   TYR B 656     6134  10318   7970    809    139  -1685       O  
-ATOM   3479  CB  TYR B 656      11.102  17.930  19.893  1.00 42.74           C  
-ANISOU 3479  CB  TYR B 656     3318   7245   5677    588    161  -1739       C  
-ATOM   3480  CG  TYR B 656      10.407  18.677  18.774  1.00 44.06           C  
-ANISOU 3480  CG  TYR B 656     3493   7210   6037    502    180  -1688       C  
-ATOM   3481  CD1 TYR B 656      10.969  19.821  18.224  1.00 43.29           C  
-ANISOU 3481  CD1 TYR B 656     3291   7042   6117    475    176  -1680       C  
-ATOM   3482  CD2 TYR B 656       9.189  18.238  18.268  1.00 47.28           C  
-ANISOU 3482  CD2 TYR B 656     4009   7503   6451    450    202  -1645       C  
-ATOM   3483  CE1 TYR B 656      10.340  20.506  17.201  1.00 44.64           C  
-ANISOU 3483  CE1 TYR B 656     3466   7029   6466    408    192  -1622       C  
-ATOM   3484  CE2 TYR B 656       8.552  18.916  17.246  1.00 37.14           C  
-ANISOU 3484  CE2 TYR B 656     2729   6046   5337    383    219  -1596       C  
-ATOM   3485  CZ  TYR B 656       9.132  20.050  16.716  1.00 40.16           C  
-ANISOU 3485  CZ  TYR B 656     3009   6357   5895    367    213  -1581       C  
-ATOM   3486  OH  TYR B 656       8.507  20.732  15.699  1.00 38.35           O  
-ANISOU 3486  OH  TYR B 656     2778   5956   5836    310    229  -1520       O  
-ATOM   3487  N   SER B 657      14.241  15.969  20.351  1.00 58.23           N  
-ANISOU 3487  N   SER B 657     5296   9700   7129    958    122  -1533       N  
-ATOM   3488  CA  SER B 657      14.802  14.930  21.210  1.00 55.21           C  
-ANISOU 3488  CA  SER B 657     4952   9506   6520   1095    110  -1524       C  
-ATOM   3489  C   SER B 657      15.026  15.438  22.632  1.00 73.80           C  
-ANISOU 3489  C   SER B 657     7184  11974   8882   1071     90  -1708       C  
-ATOM   3490  O   SER B 657      14.947  14.671  23.592  1.00 77.75           O  
-ANISOU 3490  O   SER B 657     7722  12586   9236   1137     85  -1744       O  
-ATOM   3491  CB  SER B 657      16.115  14.393  20.633  1.00 49.68           C  
-ANISOU 3491  CB  SER B 657     4264   8947   5666   1253    103  -1380       C  
-ATOM   3492  OG  SER B 657      15.889  13.270  19.797  1.00 49.35           O  
-ANISOU 3492  OG  SER B 657     4382   8866   5503   1341    121  -1215       O  
-ATOM   3493  N   ASN B 658      15.305  16.732  22.757  1.00106.41           N  
-ANISOU 3493  N   ASN B 658    11168  16075  13189    979     82  -1821       N  
-ATOM   3494  CA  ASN B 658      15.553  17.350  24.058  1.00108.51           C  
-ANISOU 3494  CA  ASN B 658    11301  16445  13481    946     66  -2010       C  
-ATOM   3495  C   ASN B 658      14.278  17.624  24.854  1.00115.43           C  
-ANISOU 3495  C   ASN B 658    12181  17226  14452    828     74  -2165       C  
-ATOM   3496  O   ASN B 658      14.336  18.117  25.982  1.00128.47           O  
-ANISOU 3496  O   ASN B 658    13727  18959  16127    792     64  -2336       O  
-ATOM   3497  CB  ASN B 658      16.349  18.649  23.897  1.00 81.46           C  
-ANISOU 3497  CB  ASN B 658     7713  13019  10217    893     57  -2076       C  
-ATOM   3498  CG  ASN B 658      17.815  18.404  23.587  1.00 90.59           C  
-ANISOU 3498  CG  ASN B 658     8820  14357  11242   1018     42  -1973       C  
-ATOM   3499  OD1 ASN B 658      18.231  17.274  23.333  1.00 94.57           O  
-ANISOU 3499  OD1 ASN B 658     9422  14968  11541   1154     41  -1838       O  
-ATOM   3500  ND2 ASN B 658      18.607  19.470  23.610  1.00100.35           N  
-ANISOU 3500  ND2 ASN B 658     9901  15632  12597    975     32  -2039       N  
-ATOM   3501  N   ILE B 659      13.129  17.308  24.266  1.00 64.68           N  
-ANISOU 3501  N   ILE B 659     5868  10635   8072    767     94  -2111       N  
-ATOM   3502  CA  ILE B 659      11.847  17.537  24.924  1.00 57.70           C  
-ANISOU 3502  CA  ILE B 659     4991   9662   7272    654    104  -2250       C  
-ATOM   3503  C   ILE B 659      11.098  16.223  25.128  1.00 67.11           C  
-ANISOU 3503  C   ILE B 659     6322  10878   8299    689    114  -2178       C  
-ATOM   3504  O   ILE B 659      10.866  15.476  24.177  1.00 68.93           O  
-ANISOU 3504  O   ILE B 659     6676  11042   8473    726    128  -2015       O  
-ATOM   3505  CB  ILE B 659      10.972  18.529  24.131  1.00 72.40           C  
-ANISOU 3505  CB  ILE B 659     6842  11296   9371    530    123  -2279       C  
-ATOM   3506  CG1 ILE B 659      11.656  19.899  24.054  1.00 79.94           C  
-ANISOU 3506  CG1 ILE B 659     7649  12211  10513    492    116  -2361       C  
-ATOM   3507  CG2 ILE B 659       9.599  18.660  24.769  1.00 77.39           C  
-ANISOU 3507  CG2 ILE B 659     7491  11848  10068    425    136  -2416       C  
-ATOM   3508  CD1 ILE B 659      10.841  20.961  23.339  1.00 89.16           C  
-ANISOU 3508  CD1 ILE B 659     8795  13151  11930    388    135  -2391       C  
-ATOM   3509  N   ASN B 660      10.729  15.947  26.376  1.00 91.34           N  
-ANISOU 3509  N   ASN B 660     9365  14044  11294    675    108  -2299       N  
-ATOM   3510  CA  ASN B 660      10.065  14.698  26.733  1.00 92.61           C  
-ANISOU 3510  CA  ASN B 660     9646  14241  11302    709    122  -2233       C  
-ATOM   3511  C   ASN B 660       8.664  14.946  27.275  1.00 80.19           C  
-ANISOU 3511  C   ASN B 660     8066  12586   9817    566    135  -2365       C  
-ATOM   3512  O   ASN B 660       8.005  14.031  27.773  1.00 73.95           O  
-ANISOU 3512  O   ASN B 660     7350  11830   8918    568    151  -2340       O  
-ATOM   3513  CB  ASN B 660      10.894  13.932  27.765  1.00110.90           C  
-ANISOU 3513  CB  ASN B 660    11952  16767  13418    842    109  -2230       C  
-ATOM   3514  CG  ASN B 660      12.323  13.706  27.312  1.00115.63           C  
-ANISOU 3514  CG  ASN B 660    12546  17472  13915    994     94  -2114       C  
-ATOM   3515  OD1 ASN B 660      12.989  14.623  26.831  1.00117.38           O  
-ANISOU 3515  OD1 ASN B 660    12673  17681  14243    973     81  -2137       O  
-ATOM   3516  ND2 ASN B 660      12.804  12.478  27.466  1.00113.48           N  
-ANISOU 3516  ND2 ASN B 660    12377  17302  13437   1154    101  -1986       N  
-ATOM   3517  N   ASN B 661       8.219  16.195  27.177  1.00 70.72           N  
-ANISOU 3517  N   ASN B 661     6777  11275   8817    449    135  -2501       N  
-ATOM   3518  CA  ASN B 661       6.893  16.584  27.636  1.00 81.43           C  
-ANISOU 3518  CA  ASN B 661     8115  12551  10271    317    148  -2642       C  
-ATOM   3519  C   ASN B 661       6.000  17.034  26.484  1.00 87.26           C  
-ANISOU 3519  C   ASN B 661     8909  13083  11163    235    169  -2599       C  
-ATOM   3520  O   ASN B 661       6.361  17.927  25.716  1.00 90.17           O  
-ANISOU 3520  O   ASN B 661     9238  13343  11679    229    172  -2586       O  
-ATOM   3521  CB  ASN B 661       6.994  17.691  28.684  1.00 93.22           C  
-ANISOU 3521  CB  ASN B 661     9458  14092  11870    260    137  -2872       C  
-ATOM   3522  CG  ASN B 661       5.640  18.118  29.210  1.00 98.65           C  
-ANISOU 3522  CG  ASN B 661    10122  14710  12650    135    152  -3032       C  
-ATOM   3523  OD1 ASN B 661       5.091  17.498  30.120  1.00 99.01           O  
-ANISOU 3523  OD1 ASN B 661    10172  14861  12587    108    150  -3087       O  
-ATOM   3524  ND2 ASN B 661       5.094  19.185  28.639  1.00104.41           N  
-ANISOU 3524  ND2 ASN B 661    10823  15264  13584     65    169  -3103       N  
-ATOM   3525  N   ARG B 662       4.834  16.404  26.379  1.00 91.61           N  
-ANISOU 3525  N   ARG B 662     9544  13586  11679    172    188  -2570       N  
-ATOM   3526  CA  ARG B 662       3.863  16.701  25.332  1.00 91.94           C  
-ANISOU 3526  CA  ARG B 662     9643  13449  11839     97    211  -2528       C  
-ATOM   3527  C   ARG B 662       3.451  18.169  25.317  1.00 81.79           C  
-ANISOU 3527  C   ARG B 662     8263  12039  10775     23    219  -2687       C  
-ATOM   3528  O   ARG B 662       3.369  18.793  24.257  1.00 82.51           O  
-ANISOU 3528  O   ARG B 662     8365  11981  11004     15    232  -2626       O  
-ATOM   3529  CB  ARG B 662       2.615  15.842  25.529  1.00110.12           C  
-ANISOU 3529  CB  ARG B 662    12022  15755  14063     26    231  -2514       C  
-ATOM   3530  CG  ARG B 662       2.848  14.347  25.438  1.00122.89           C  
-ANISOU 3530  CG  ARG B 662    13750  17454  15487    103    244  -2336       C  
-ATOM   3531  CD  ARG B 662       1.556  13.605  25.718  1.00139.52           C  
-ANISOU 3531  CD  ARG B 662    15914  19555  17542     15    278  -2333       C  
-ATOM   3532  NE  ARG B 662       1.710  12.156  25.669  1.00156.45           N  
-ANISOU 3532  NE  ARG B 662    18190  21743  19512     96    314  -2163       N  
-ATOM   3533  CZ  ARG B 662       0.737  11.301  25.965  1.00168.94           C  
-ANISOU 3533  CZ  ARG B 662    19849  23320  21019     38    364  -2132       C  
-ATOM   3534  NH1 ARG B 662      -0.452  11.758  26.332  1.00170.13           N  
-ANISOU 3534  NH1 ARG B 662    19932  23457  21253   -106    374  -2259       N  
-ATOM   3535  NH2 ARG B 662       0.949   9.994  25.898  1.00175.19           N  
-ANISOU 3535  NH2 ARG B 662    20801  24114  21649    126    411  -1980       N  
-ATOM   3536  N   ASP B 663       3.185  18.710  26.501  1.00 77.60           N  
-ANISOU 3536  N   ASP B 663     7637  11568  10280    -23    214  -2888       N  
-ATOM   3537  CA  ASP B 663       2.637  20.058  26.635  1.00 79.33           C  
-ANISOU 3537  CA  ASP B 663     7765  11666  10710    -85    229  -3059       C  
-ATOM   3538  C   ASP B 663       3.616  21.161  26.229  1.00 66.45           C  
-ANISOU 3538  C   ASP B 663     6043   9959   9245    -43    224  -3066       C  
-ATOM   3539  O   ASP B 663       3.198  22.237  25.799  1.00 57.56           O  
-ANISOU 3539  O   ASP B 663     4866   8678   8327    -76    241  -3124       O  
-ATOM   3540  CB  ASP B 663       2.131  20.290  28.062  1.00 96.65           C  
-ANISOU 3540  CB  ASP B 663     9877  13960  12885   -138    228  -3278       C  
-ATOM   3541  CG  ASP B 663       0.932  19.423  28.402  1.00102.11           C  
-ANISOU 3541  CG  ASP B 663    10637  14700  13460   -209    237  -3287       C  
-ATOM   3542  OD1 ASP B 663      -0.135  19.612  27.779  1.00 98.38           O  
-ANISOU 3542  OD1 ASP B 663    10212  14103  13064   -265    263  -3284       O  
-ATOM   3543  OD2 ASP B 663       1.055  18.557  29.294  1.00104.75           O  
-ANISOU 3543  OD2 ASP B 663    10969  15204  13629   -208    219  -3290       O  
-ATOM   3544  N   GLN B 664       4.912  20.901  26.376  1.00 68.40           N  
-ANISOU 3544  N   GLN B 664     6261  10324   9404     32    200  -3003       N  
-ATOM   3545  CA  GLN B 664       5.920  21.837  25.893  1.00 75.66           C  
-ANISOU 3545  CA  GLN B 664     7094  11187  10465     67    193  -2982       C  
-ATOM   3546  C   GLN B 664       5.736  21.999  24.392  1.00 74.00           C  
-ANISOU 3546  C   GLN B 664     6951  10809  10356     68    206  -2812       C  
-ATOM   3547  O   GLN B 664       5.328  23.054  23.912  1.00 68.20           O  
-ANISOU 3547  O   GLN B 664     6165   9912   9837     28    220  -2851       O  
-ATOM   3548  CB  GLN B 664       7.334  21.323  26.173  1.00 96.31           C  
-ANISOU 3548  CB  GLN B 664     9684  13980  12929    156    166  -2913       C  
-ATOM   3549  CG  GLN B 664       7.668  21.082  27.636  1.00110.06           C  
-ANISOU 3549  CG  GLN B 664    11355  15915  14547    171    150  -3060       C  
-ATOM   3550  CD  GLN B 664       9.140  20.761  27.842  1.00120.59           C  
-ANISOU 3550  CD  GLN B 664    12644  17422  15754    270    126  -2996       C  
-ATOM   3551  OE1 GLN B 664      10.015  21.438  27.299  1.00121.15           O  
-ANISOU 3551  OE1 GLN B 664    12647  17462  15922    293    120  -2957       O  
-ATOM   3552  NE2 GLN B 664       9.419  19.726  28.627  1.00125.09           N  
-ANISOU 3552  NE2 GLN B 664    13244  18179  16104    332    111  -2980       N  
-ATOM   3553  N   ILE B 665       6.039  20.929  23.664  1.00 93.59           N  
-ANISOU 3553  N   ILE B 665     9544  13335  12681    121    202  -2620       N  
-ATOM   3554  CA  ILE B 665       5.890  20.886  22.215  1.00 91.25           C  
-ANISOU 3554  CA  ILE B 665     9322  12906  12442    127    215  -2443       C  
-ATOM   3555  C   ILE B 665       4.617  21.583  21.748  1.00 92.13           C  
-ANISOU 3555  C   ILE B 665     9441  12836  12729     50    240  -2491       C  
-ATOM   3556  O   ILE B 665       4.663  22.475  20.906  1.00 99.63           O  
-ANISOU 3556  O   ILE B 665    10349  13646  13861     41    247  -2445       O  
-ATOM   3557  CB  ILE B 665       5.879  19.432  21.709  1.00 67.47           C  
-ANISOU 3557  CB  ILE B 665     6452   9968   9215    177    217  -2269       C  
-ATOM   3558  CG1 ILE B 665       7.182  18.728  22.096  1.00 47.57           C  
-ANISOU 3558  CG1 ILE B 665     3926   7629   6520    280    193  -2205       C  
-ATOM   3559  CG2 ILE B 665       5.670  19.389  20.204  1.00 78.02           C  
-ANISOU 3559  CG2 ILE B 665     7862  11174  10607    178    233  -2095       C  
-ATOM   3560  CD1 ILE B 665       7.227  17.270  21.699  1.00 47.21           C  
-ANISOU 3560  CD1 ILE B 665     4016   7658   6265    350    196  -2039       C  
-ATOM   3561  N   ILE B 666       3.480  21.169  22.299  1.00 74.49           N  
-ANISOU 3561  N   ILE B 666     7253  10613  10438     -3    254  -2580       N  
-ATOM   3562  CA  ILE B 666       2.200  21.780  21.959  1.00 66.71           C  
-ANISOU 3562  CA  ILE B 666     6271   9479   9598    -69    280  -2640       C  
-ATOM   3563  C   ILE B 666       2.239  23.293  22.156  1.00 64.53           C  
-ANISOU 3563  C   ILE B 666     5859   9090   9570    -86    282  -2773       C  
-ATOM   3564  O   ILE B 666       1.863  24.057  21.266  1.00 60.59           O  
-ANISOU 3564  O   ILE B 666     5341   8433   9248    -96    294  -2724       O  
-ATOM   3565  CB  ILE B 666       1.050  21.180  22.792  1.00 51.03           C  
-ANISOU 3565  CB  ILE B 666     4328   7557   7504   -128    293  -2754       C  
-ATOM   3566  CG1 ILE B 666       0.853  19.702  22.439  1.00 40.16           C  
-ANISOU 3566  CG1 ILE B 666     3086   6262   5912   -122    293  -2604       C  
-ATOM   3567  CG2 ILE B 666      -0.236  21.967  22.580  1.00 30.70           C  
-ANISOU 3567  CG2 ILE B 666     1731   4845   5088   -185    321  -2848       C  
-ATOM   3568  CD1 ILE B 666      -0.331  19.059  23.123  1.00 42.77           C  
-ANISOU 3568  CD1 ILE B 666     3458   6653   6139   -195    305  -2690       C  
-ATOM   3569  N   GLU B 667       2.697  23.720  23.328  1.00 70.54           N  
-ANISOU 3569  N   GLU B 667     6518   9938  10347    -86    269  -2940       N  
-ATOM   3570  CA  GLU B 667       2.814  25.140  23.634  1.00 77.62           C  
-ANISOU 3570  CA  GLU B 667     7273  10740  11481   -100    270  -3081       C  
-ATOM   3571  C   GLU B 667       3.863  25.789  22.745  1.00 66.76           C  
-ANISOU 3571  C   GLU B 667     5844   9287  10236    -65    256  -2958       C  
-ATOM   3572  O   GLU B 667       3.647  26.865  22.194  1.00 58.06           O  
-ANISOU 3572  O   GLU B 667     4673   8025   9363    -80    261  -2963       O  
-ATOM   3573  CB  GLU B 667       3.197  25.340  25.101  1.00107.44           C  
-ANISOU 3573  CB  GLU B 667    10951  14652  15218   -106    259  -3282       C  
-ATOM   3574  CG  GLU B 667       3.220  26.794  25.544  1.00120.97           C  
-ANISOU 3574  CG  GLU B 667    12510  16274  17180   -127    262  -3455       C  
-ATOM   3575  CD  GLU B 667       1.831  27.400  25.613  1.00132.31           C  
-ANISOU 3575  CD  GLU B 667    13928  17585  18758   -170    287  -3573       C  
-ATOM   3576  OE1 GLU B 667       1.727  28.642  25.698  1.00135.20           O  
-ANISOU 3576  OE1 GLU B 667    14173  17834  19361   -181    290  -3684       O  
-ATOM   3577  OE2 GLU B 667       0.844  26.635  25.584  1.00135.89           O  
-ANISOU 3577  OE2 GLU B 667    14482  18063  19087   -193    303  -3556       O  
-ATOM   3578  N   MET B 668       4.998  25.114  22.607  1.00 75.40           N  
-ANISOU 3578  N   MET B 668     6965  10503  11179    -15    237  -2843       N  
-ATOM   3579  CA  MET B 668       6.146  25.659  21.894  1.00 82.40           C  
-ANISOU 3579  CA  MET B 668     7789  11360  12159     19    222  -2734       C  
-ATOM   3580  C   MET B 668       5.959  25.695  20.378  1.00 83.29           C  
-ANISOU 3580  C   MET B 668     7968  11335  12344     25    230  -2534       C  
-ATOM   3581  O   MET B 668       6.145  26.738  19.754  1.00 90.53           O  
-ANISOU 3581  O   MET B 668     8804  12121  13473     13    229  -2504       O  
-ATOM   3582  CB  MET B 668       7.418  24.886  22.259  1.00 88.44           C  
-ANISOU 3582  CB  MET B 668     8558  12324  12722     80    200  -2679       C  
-ATOM   3583  CG  MET B 668       7.713  24.865  23.752  1.00 90.44           C  
-ANISOU 3583  CG  MET B 668     8734  12732  12896     79    188  -2869       C  
-ATOM   3584  SD  MET B 668       9.467  24.709  24.145  1.00202.48           S  
-ANISOU 3584  SD  MET B 668    22841  27125  26968    150    160  -2841       S  
-ATOM   3585  CE  MET B 668      10.070  26.332  23.683  1.00102.01           C  
-ANISOU 3585  CE  MET B 668     9958  14265  14535    115    156  -2876       C  
-ATOM   3586  N   VAL B 669       5.594  24.560  19.788  1.00 74.02           N  
-ANISOU 3586  N   VAL B 669     6933  10194  10996     43    239  -2396       N  
-ATOM   3587  CA  VAL B 669       5.406  24.480  18.341  1.00 71.76           C  
-ANISOU 3587  CA  VAL B 669     6714   9798  10752     50    249  -2202       C  
-ATOM   3588  C   VAL B 669       4.249  25.359  17.872  1.00 73.98           C  
-ANISOU 3588  C   VAL B 669     6973   9893  11244      1    268  -2237       C  
-ATOM   3589  O   VAL B 669       4.362  26.062  16.867  1.00 75.32           O  
-ANISOU 3589  O   VAL B 669     7107   9938  11572      1    268  -2131       O  
-ATOM   3590  CB  VAL B 669       5.193  23.029  17.869  1.00 63.51           C  
-ANISOU 3590  CB  VAL B 669     5822   8835   9472     78    257  -2062       C  
-ATOM   3591  CG1 VAL B 669       4.890  22.990  16.378  1.00 53.40           C  
-ANISOU 3591  CG1 VAL B 669     4607   7443   8242     80    271  -1877       C  
-ATOM   3592  CG2 VAL B 669       6.421  22.198  18.181  1.00 60.44           C  
-ANISOU 3592  CG2 VAL B 669     5450   8627   8889    148    237  -2002       C  
-ATOM   3593  N   GLY B 670       3.141  25.317  18.605  1.00 66.67           N  
-ANISOU 3593  N   GLY B 670     6062   8957  10315    -39    283  -2383       N  
-ATOM   3594  CA  GLY B 670       2.005  26.173  18.314  1.00 60.93           C  
-ANISOU 3594  CA  GLY B 670     5299   8070   9780    -77    300  -2441       C  
-ATOM   3595  C   GLY B 670       2.336  27.638  18.531  1.00 67.37           C  
-ANISOU 3595  C   GLY B 670     5959   8779  10859    -84    289  -2539       C  
-ATOM   3596  O   GLY B 670       1.829  28.510  17.826  1.00 59.61           O  
-ANISOU 3596  O   GLY B 670     4931   7640  10081    -94    295  -2505       O  
-ATOM   3597  N   ARG B 671       3.194  27.907  19.511  1.00100.73           N  
-ANISOU 3597  N   ARG B 671    10097  13094  15082    -77    273  -2661       N  
-ATOM   3598  CA  ARG B 671       3.610  29.270  19.823  1.00100.34           C  
-ANISOU 3598  CA  ARG B 671     9889  12957  15277    -88    262  -2769       C  
-ATOM   3599  C   ARG B 671       4.496  29.843  18.722  1.00110.70           C  
-ANISOU 3599  C   ARG B 671    11155  14186  16719    -70    248  -2600       C  
-ATOM   3600  O   ARG B 671       4.448  31.039  18.431  1.00111.50           O  
-ANISOU 3600  O   ARG B 671    11147  14143  17074    -86    243  -2623       O  
-ATOM   3601  CB  ARG B 671       4.355  29.303  21.160  1.00 61.64           C  
-ANISOU 3601  CB  ARG B 671     4909   8201  10311    -87    249  -2940       C  
-ATOM   3602  CG  ARG B 671       4.757  30.689  21.625  1.00 74.90           C  
-ANISOU 3602  CG  ARG B 671     6417   9805  12239   -105    240  -3081       C  
-ATOM   3603  CD  ARG B 671       5.261  30.667  23.063  1.00 90.54           C  
-ANISOU 3603  CD  ARG B 671     8321  11942  14139   -110    233  -3280       C  
-ATOM   3604  NE  ARG B 671       6.712  30.515  23.154  1.00104.23           N  
-ANISOU 3604  NE  ARG B 671    10009  13803  15789    -85    211  -3225       N  
-ATOM   3605  CZ  ARG B 671       7.570  31.530  23.109  1.00108.46           C  
-ANISOU 3605  CZ  ARG B 671    10407  14300  16503    -95    198  -3253       C  
-ATOM   3606  NH1 ARG B 671       7.125  32.772  22.965  1.00113.51           N  
-ANISOU 3606  NH1 ARG B 671    10943  14763  17423   -128    202  -3330       N  
-ATOM   3607  NH2 ARG B 671       8.874  31.306  23.204  1.00103.43           N  
-ANISOU 3607  NH2 ARG B 671     9730  13805  15763    -72    179  -3202       N  
-ATOM   3608  N   GLY B 672       5.301  28.980  18.109  1.00103.28           N  
-ANISOU 3608  N   GLY B 672    10294  13343  15606    -37    240  -2429       N  
-ATOM   3609  CA  GLY B 672       6.258  29.404  17.105  1.00 97.60           C  
-ANISOU 3609  CA  GLY B 672     9530  12581  14973    -19    226  -2264       C  
-ATOM   3610  C   GLY B 672       7.646  29.517  17.702  1.00 96.67           C  
-ANISOU 3610  C   GLY B 672     9324  12597  14809     -1    204  -2305       C  
-ATOM   3611  O   GLY B 672       8.560  30.072  17.089  1.00 98.49           O  
-ANISOU 3611  O   GLY B 672     9479  12807  15135      4    190  -2208       O  
-ATOM   3612  N   SER B 673       7.796  28.983  18.910  1.00 89.70           N  
-ANISOU 3612  N   SER B 673     8445  11864  13772      6    202  -2449       N  
-ATOM   3613  CA  SER B 673       9.063  29.028  19.627  1.00 90.93           C  
-ANISOU 3613  CA  SER B 673     8513  12176  13860     26    182  -2510       C  
-ATOM   3614  C   SER B 673       9.969  27.868  19.241  1.00 90.67           C  
-ANISOU 3614  C   SER B 673     8564  12310  13575     87    172  -2351       C  
-ATOM   3615  O   SER B 673      11.189  27.962  19.358  1.00 96.36           O  
-ANISOU 3615  O   SER B 673     9209  13149  14253    114    155  -2329       O  
-ATOM   3616  CB  SER B 673       8.815  28.994  21.141  1.00 85.10           C  
-ANISOU 3616  CB  SER B 673     7731  11537  13067     11    183  -2741       C  
-ATOM   3617  OG  SER B 673       8.256  27.742  21.528  1.00 79.88           O  
-ANISOU 3617  OG  SER B 673     7201  10980  12169     31    191  -2738       O  
-ATOM   3618  N   LEU B 674       9.371  26.777  18.775  1.00 81.37           N  
-ANISOU 3618  N   LEU B 674     7537  11147  12232    110    185  -2242       N  
-ATOM   3619  CA  LEU B 674      10.126  25.554  18.533  1.00 76.48           C  
-ANISOU 3619  CA  LEU B 674     7005  10695  11358    178    177  -2108       C  
-ATOM   3620  C   LEU B 674      10.011  25.032  17.104  1.00 76.80           C  
-ANISOU 3620  C   LEU B 674     7149  10675  11355    202    187  -1886       C  
-ATOM   3621  O   LEU B 674       8.925  25.002  16.523  1.00 83.96           O  
-ANISOU 3621  O   LEU B 674     8129  11449  12323    168    206  -1846       O  
-ATOM   3622  CB  LEU B 674       9.687  24.464  19.513  1.00 68.34           C  
-ANISOU 3622  CB  LEU B 674     6060   9794  10113    198    179  -2190       C  
-ATOM   3623  CG  LEU B 674      10.404  23.116  19.435  1.00 68.81           C  
-ANISOU 3623  CG  LEU B 674     6210  10034   9899    283    171  -2067       C  
-ATOM   3624  CD1 LEU B 674      11.864  23.275  19.817  1.00 59.72           C  
-ANISOU 3624  CD1 LEU B 674     4957   9044   8690    339    148  -2073       C  
-ATOM   3625  CD2 LEU B 674       9.721  22.093  20.329  1.00 76.92           C  
-ANISOU 3625  CD2 LEU B 674     7327  11153  10747    290    174  -2139       C  
-ATOM   3626  N   SER B 675      11.148  24.616  16.552  1.00 63.34           N  
-ANISOU 3626  N   SER B 675     5446   9083   9539    261    176  -1747       N  
-ATOM   3627  CA  SER B 675      11.196  23.992  15.234  1.00 63.00           C  
-ANISOU 3627  CA  SER B 675     5499   9020   9419    295    186  -1536       C  
-ATOM   3628  C   SER B 675      12.306  22.941  15.197  1.00 49.92           C  
-ANISOU 3628  C   SER B 675     3883   7567   7518    389    175  -1438       C  
-ATOM   3629  O   SER B 675      13.294  23.054  15.923  1.00 51.91           O  
-ANISOU 3629  O   SER B 675     4048   7960   7714    425    157  -1504       O  
-ATOM   3630  CB  SER B 675      11.418  25.047  14.149  1.00117.63           C  
-ANISOU 3630  CB  SER B 675    12340  15804  16550    262    185  -1435       C  
-ATOM   3631  OG  SER B 675      12.644  25.729  14.340  1.00128.40           O  
-ANISOU 3631  OG  SER B 675    13569  17244  17973    272    164  -1451       O  
-ATOM   3632  N   PRO B 676      12.144  21.910  14.352  1.00 46.03           N  
-ANISOU 3632  N   PRO B 676     3517   7097   6875    436    189  -1282       N  
-ATOM   3633  CA  PRO B 676      13.121  20.816  14.296  1.00 47.01           C  
-ANISOU 3633  CA  PRO B 676     3692   7414   6757    543    182  -1185       C  
-ATOM   3634  C   PRO B 676      14.546  21.315  14.061  1.00 47.93           C  
-ANISOU 3634  C   PRO B 676     3691   7638   6883    586    164  -1135       C  
-ATOM   3635  O   PRO B 676      14.749  22.285  13.330  1.00 45.34           O  
-ANISOU 3635  O   PRO B 676     3281   7214   6733    537    163  -1084       O  
-ATOM   3636  CB  PRO B 676      12.646  19.984  13.102  1.00 48.43           C  
-ANISOU 3636  CB  PRO B 676     4004   7545   6851    567    203  -1014       C  
-ATOM   3637  CG  PRO B 676      11.191  20.267  13.003  1.00 50.65           C  
-ANISOU 3637  CG  PRO B 676     4334   7649   7260    475    220  -1067       C  
-ATOM   3638  CD  PRO B 676      11.033  21.706  13.407  1.00 47.26           C  
-ANISOU 3638  CD  PRO B 676     3774   7107   7076    396    212  -1192       C  
-ATOM   3639  N   ASP B 677      15.517  20.650  14.679  1.00 60.40           N  
-ANISOU 3639  N   ASP B 677     5258   9422   8270    681    150  -1145       N  
-ATOM   3640  CA  ASP B 677      16.920  21.024  14.538  1.00 57.08           C  
-ANISOU 3640  CA  ASP B 677     4720   9141   7826    731    133  -1104       C  
-ATOM   3641  C   ASP B 677      17.458  20.604  13.176  1.00 58.15           C  
-ANISOU 3641  C   ASP B 677     4900   9308   7888    788    143   -900       C  
-ATOM   3642  O   ASP B 677      17.757  19.430  12.953  1.00 56.40           O  
-ANISOU 3642  O   ASP B 677     4778   9205   7448    895    149   -808       O  
-ATOM   3643  CB  ASP B 677      17.755  20.380  15.645  1.00 40.04           C  
-ANISOU 3643  CB  ASP B 677     2538   7210   5467    828    115  -1178       C  
-ATOM   3644  CG  ASP B 677      19.192  20.849  15.638  1.00 38.53           C  
-ANISOU 3644  CG  ASP B 677     2205   7180   5253    872     97  -1161       C  
-ATOM   3645  OD1 ASP B 677      19.490  21.844  14.944  1.00 36.61           O  
-ANISOU 3645  OD1 ASP B 677     1866   6860   5185    804     94  -1120       O  
-ATOM   3646  OD2 ASP B 677      20.023  20.226  16.331  1.00 53.79           O  
-ANISOU 3646  OD2 ASP B 677     4120   9325   6993    977     83  -1185       O  
-ATOM   3647  N   LEU B 678      17.585  21.567  12.270  1.00 45.02           N  
-ANISOU 3647  N   LEU B 678     3159   7538   6407    721    144   -830       N  
-ATOM   3648  CA  LEU B 678      18.037  21.278  10.914  1.00 45.96           C  
-ANISOU 3648  CA  LEU B 678     3309   7680   6475    761    154   -637       C  
-ATOM   3649  C   LEU B 678      19.529  20.965  10.844  1.00 43.77           C  
-ANISOU 3649  C   LEU B 678     2961   7633   6035    863    141   -574       C  
-ATOM   3650  O   LEU B 678      19.994  20.356   9.882  1.00 44.52           O  
-ANISOU 3650  O   LEU B 678     3103   7804   6008    934    152   -421       O  
-ATOM   3651  CB  LEU B 678      17.690  22.429   9.968  1.00 60.51           C  
-ANISOU 3651  CB  LEU B 678     5084   9340   8567    659    157   -574       C  
-ATOM   3652  CG  LEU B 678      16.219  22.536   9.568  1.00 61.71           C  
-ANISOU 3652  CG  LEU B 678     5328   9275   8843    585    177   -571       C  
-ATOM   3653  CD1 LEU B 678      16.018  23.651   8.557  1.00 64.34           C  
-ANISOU 3653  CD1 LEU B 678     5588   9449   9410    508    177   -485       C  
-ATOM   3654  CD2 LEU B 678      15.726  21.212   9.007  1.00 56.20           C  
-ANISOU 3654  CD2 LEU B 678     4795   8605   7951    646    200   -469       C  
-ATOM   3655  N   SER B 679      20.276  21.378  11.863  1.00 60.60           N  
-ANISOU 3655  N   SER B 679     4976   9887   8161    873    119   -695       N  
-ATOM   3656  CA  SER B 679      21.711  21.115  11.892  1.00 62.53           C  
-ANISOU 3656  CA  SER B 679     5140  10373   8245    973    104   -649       C  
-ATOM   3657  C   SER B 679      21.994  19.644  12.192  1.00 60.78           C  
-ANISOU 3657  C   SER B 679     5037  10324   7733   1127    110   -612       C  
-ATOM   3658  O   SER B 679      23.151  19.227  12.255  1.00 59.50           O  
-ANISOU 3658  O   SER B 679     4827  10381   7399   1240    101   -571       O  
-ATOM   3659  CB  SER B 679      22.415  22.018  12.911  1.00 45.07           C  
-ANISOU 3659  CB  SER B 679     2759   8252   6113    934     79   -796       C  
-ATOM   3660  OG  SER B 679      22.123  21.627  14.241  1.00 40.49           O  
-ANISOU 3660  OG  SER B 679     2205   7729   5451    960     72   -950       O  
-ATOM   3661  N   LYS B 680      20.933  18.862  12.370  1.00 50.58           N  
-ANISOU 3661  N   LYS B 680     3897   8934   6387   1136    126   -624       N  
-ATOM   3662  CA  LYS B 680      21.071  17.436  12.656  1.00 48.99           C  
-ANISOU 3662  CA  LYS B 680     3823   8867   5925   1285    132   -585       C  
-ATOM   3663  C   LYS B 680      21.024  16.566  11.400  1.00 54.09           C  
-ANISOU 3663  C   LYS B 680     4590   9505   6457   1358    157   -408       C  
-ATOM   3664  O   LYS B 680      21.187  15.348  11.477  1.00 50.99           O  
-ANISOU 3664  O   LYS B 680     4311   9214   5847   1497    165   -355       O  
-ATOM   3665  CB  LYS B 680      20.010  16.972  13.658  1.00 50.21           C  
-ANISOU 3665  CB  LYS B 680     4072   8946   6062   1264    134   -700       C  
-ATOM   3666  CG  LYS B 680      20.347  17.283  15.108  1.00 52.34           C  
-ANISOU 3666  CG  LYS B 680     4246   9324   6317   1267    110   -867       C  
-ATOM   3667  CD  LYS B 680      19.645  16.320  16.056  1.00 52.25           C  
-ANISOU 3667  CD  LYS B 680     4351   9327   6175   1318    110   -933       C  
-ATOM   3668  CE  LYS B 680      18.476  16.981  16.770  1.00 62.88           C  
-ANISOU 3668  CE  LYS B 680     5681  10512   7698   1172    111  -1084       C  
-ATOM   3669  NZ  LYS B 680      17.752  16.017  17.649  1.00 70.60           N  
-ANISOU 3669  NZ  LYS B 680     6770  11509   8547   1214    112  -1138       N  
-ATOM   3670  N   VAL B 681      20.798  17.190  10.247  1.00 60.87           N  
-ANISOU 3670  N   VAL B 681     5424  10240   7463   1271    170   -316       N  
-ATOM   3671  CA  VAL B 681      20.795  16.460   8.985  1.00 64.67           C  
-ANISOU 3671  CA  VAL B 681     6003  10721   7846   1331    195   -149       C  
-ATOM   3672  C   VAL B 681      22.152  15.800   8.770  1.00 67.96           C  
-ANISOU 3672  C   VAL B 681     6398  11379   8044   1494    193    -68       C  
-ATOM   3673  O   VAL B 681      23.153  16.221   9.350  1.00 67.52           O  
-ANISOU 3673  O   VAL B 681     6215  11477   7962   1529    170   -122       O  
-ATOM   3674  CB  VAL B 681      20.467  17.379   7.791  1.00 52.18           C  
-ANISOU 3674  CB  VAL B 681     4371   8990   6466   1211    205    -61       C  
-ATOM   3675  CG1 VAL B 681      19.040  17.893   7.891  1.00 52.53           C  
-ANISOU 3675  CG1 VAL B 681     4458   8796   6705   1074    212   -127       C  
-ATOM   3676  CG2 VAL B 681      21.452  18.535   7.724  1.00 45.80           C  
-ANISOU 3676  CG2 VAL B 681     3378   8245   5777   1166    183    -67       C  
-ATOM   3677  N   ARG B 682      22.183  14.761   7.942  1.00 62.63           N  
-ANISOU 3677  N   ARG B 682     5843  10745   7209   1599    218     56       N  
-ATOM   3678  CA  ARG B 682      23.422  14.040   7.673  1.00 72.46           C  
-ANISOU 3678  CA  ARG B 682     7082  12219   8231   1774    221    137       C  
-ATOM   3679  C   ARG B 682      24.409  14.883   6.873  1.00 80.44           C  
-ANISOU 3679  C   ARG B 682     7936  13322   9304   1744    215    210       C  
-ATOM   3680  O   ARG B 682      24.022  15.815   6.167  1.00 69.24           O  
-ANISOU 3680  O   ARG B 682     6456  11764   8087   1601    217    246       O  
-ATOM   3681  CB  ARG B 682      23.140  12.736   6.925  1.00 69.30           C  
-ANISOU 3681  CB  ARG B 682     6855  11820   7654   1893    252    248       C  
-ATOM   3682  CG  ARG B 682      22.440  11.666   7.744  1.00 71.73           C  
-ANISOU 3682  CG  ARG B 682     7323  12089   7843   1972    255    196       C  
-ATOM   3683  CD  ARG B 682      22.375  10.362   6.966  1.00 82.10           C  
-ANISOU 3683  CD  ARG B 682     8801  13423   8969   2115    284    313       C  
-ATOM   3684  NE  ARG B 682      21.663   9.311   7.685  1.00 92.72           N  
-ANISOU 3684  NE  ARG B 682    10309  14711  10210   2193    285    279       N  
-ATOM   3685  CZ  ARG B 682      21.561   8.057   7.258  1.00 98.11           C  
-ANISOU 3685  CZ  ARG B 682    11158  15398  10722   2339    304    364       C  
-ATOM   3686  NH1 ARG B 682      22.132   7.697   6.116  1.00 96.44           N  
-ANISOU 3686  NH1 ARG B 682    10966  15258  10416   2423    329    480       N  
-ATOM   3687  NH2 ARG B 682      20.893   7.161   7.972  1.00100.02           N  
-ANISOU 3687  NH2 ARG B 682    11543  15570  10891   2404    298    335       N  
-ATOM   3688  N   SER B 683      25.689  14.545   6.991  1.00105.07           N  
-ANISOU 3688  N   SER B 683    10993  16683  12247   1886    207    236       N  
-ATOM   3689  CA  SER B 683      26.734  15.189   6.208  1.00102.83           C  
-ANISOU 3689  CA  SER B 683    10561  16526  11982   1878    202    316       C  
-ATOM   3690  C   SER B 683      26.509  14.923   4.727  1.00105.75           C  
-ANISOU 3690  C   SER B 683    10992  16838  12349   1873    234    469       C  
-ATOM   3691  O   SER B 683      26.919  15.707   3.871  1.00107.13           O  
-ANISOU 3691  O   SER B 683    11053  17024  12628   1797    231    547       O  
-ATOM   3692  CB  SER B 683      28.106  14.659   6.622  1.00 78.30           C  
-ANISOU 3692  CB  SER B 683     7392  13713   8644   2059    192    316       C  
-ATOM   3693  OG  SER B 683      29.117  15.132   5.751  1.00 76.33           O  
-ANISOU 3693  OG  SER B 683     7009  13607   8385   2065    190    409       O  
-ATOM   3694  N   ASN B 684      25.852  13.806   4.433  1.00 96.24           N  
-ANISOU 3694  N   ASN B 684     9966  15576  11024   1952    262    512       N  
-ATOM   3695  CA  ASN B 684      25.598  13.405   3.057  1.00 89.86           C  
-ANISOU 3695  CA  ASN B 684     9229  14724  10189   1960    296    649       C  
-ATOM   3696  C   ASN B 684      24.398  14.123   2.445  1.00 90.82           C  
-ANISOU 3696  C   ASN B 684     9366  14595  10546   1771    304    672       C  
-ATOM   3697  O   ASN B 684      24.314  14.273   1.226  1.00 94.05           O  
-ANISOU 3697  O   ASN B 684     9767  14971  10997   1731    323    789       O  
-ATOM   3698  CB  ASN B 684      25.422  11.884   2.953  1.00 87.19           C  
-ANISOU 3698  CB  ASN B 684     9077  14431   9619   2132    326    686       C  
-ATOM   3699  CG  ASN B 684      25.331  11.203   4.311  1.00 85.29           C  
-ANISOU 3699  CG  ASN B 684     8919  14224   9263   2233    310    578       C  
-ATOM   3700  OD1 ASN B 684      24.340  10.542   4.620  1.00 88.13           O  
-ANISOU 3700  OD1 ASN B 684     9428  14449   9608   2234    319    550       O  
-ATOM   3701  ND2 ASN B 684      26.372  11.353   5.124  1.00 81.04           N  
-ANISOU 3701  ND2 ASN B 684     8280  13874   8639   2321    285    520       N  
-ATOM   3702  N   CYS B 685      23.477  14.570   3.294  1.00 90.65           N  
-ANISOU 3702  N   CYS B 685     9363  14408  10674   1662    288    560       N  
-ATOM   3703  CA  CYS B 685      22.256  15.223   2.829  1.00 87.42           C  
-ANISOU 3703  CA  CYS B 685     8975  13758  10481   1497    295    568       C  
-ATOM   3704  C   CYS B 685      22.546  16.415   1.927  1.00 79.32           C  
-ANISOU 3704  C   CYS B 685     7810  12689   9638   1387    287    649       C  
-ATOM   3705  O   CYS B 685      23.278  17.327   2.311  1.00 84.18           O  
-ANISOU 3705  O   CYS B 685     8278  13364  10345   1348    259    609       O  
-ATOM   3706  CB  CYS B 685      21.394  15.668   4.013  1.00 89.26           C  
-ANISOU 3706  CB  CYS B 685     9217  13848  10850   1403    275    416       C  
-ATOM   3707  SG  CYS B 685      19.807  16.400   3.536  1.00 74.50           S  
-ANISOU 3707  SG  CYS B 685     7384  11689   9232   1221    285    413       S  
-ATOM   3708  N   PRO B 686      21.968  16.405   0.717  1.00 61.83           N  
-ANISOU 3708  N   PRO B 686     5640  10376   7477   1336    310    765       N  
-ATOM   3709  CA  PRO B 686      22.106  17.510  -0.237  1.00 57.71           C  
-ANISOU 3709  CA  PRO B 686     4998   9793   7135   1232    303    861       C  
-ATOM   3710  C   PRO B 686      21.458  18.778   0.303  1.00 52.12           C  
-ANISOU 3710  C   PRO B 686     4214   8893   6695   1085    278    774       C  
-ATOM   3711  O   PRO B 686      20.390  18.704   0.909  1.00 55.05           O  
-ANISOU 3711  O   PRO B 686     4669   9115   7135   1036    280    680       O  
-ATOM   3712  CB  PRO B 686      21.335  17.013  -1.465  1.00 60.04           C  
-ANISOU 3712  CB  PRO B 686     5396  10006   7411   1218    336    982       C  
-ATOM   3713  CG  PRO B 686      21.266  15.525  -1.308  1.00 58.97           C  
-ANISOU 3713  CG  PRO B 686     5412   9963   7031   1353    363    972       C  
-ATOM   3714  CD  PRO B 686      21.185  15.288   0.164  1.00 56.34           C  
-ANISOU 3714  CD  PRO B 686     5111   9633   6661   1386    345    819       C  
-ATOM   3715  N   LYS B 687      22.099  19.924   0.087  1.00 53.01           N  
-ANISOU 3715  N   LYS B 687     4169   9016   6959   1019    254    804       N  
-ATOM   3716  CA  LYS B 687      21.559  21.199   0.546  1.00 50.79           C  
-ANISOU 3716  CA  LYS B 687     3804   8550   6945    889    230    726       C  
-ATOM   3717  C   LYS B 687      20.212  21.482  -0.107  1.00 48.72           C  
-ANISOU 3717  C   LYS B 687     3616   8059   6839    801    245    771       C  
-ATOM   3718  O   LYS B 687      19.472  22.356   0.337  1.00 57.88           O  
-ANISOU 3718  O   LYS B 687     4744   9039   8208    708    232    690       O  
-ATOM   3719  CB  LYS B 687      22.530  22.347   0.253  1.00 69.69           C  
-ANISOU 3719  CB  LYS B 687     6013  10998   9469    837    202    775       C  
-ATOM   3720  CG  LYS B 687      23.897  22.221   0.917  1.00 85.54           C  
-ANISOU 3720  CG  LYS B 687     7921  13245  11338    913    184    724       C  
-ATOM   3721  CD  LYS B 687      24.775  23.423   0.580  1.00 97.92           C  
-ANISOU 3721  CD  LYS B 687     9297  14856  13053    842    155    776       C  
-ATOM   3722  CE  LYS B 687      26.253  23.160   0.859  1.00101.57           C  
-ANISOU 3722  CE  LYS B 687     9655  15604  13333    931    141    774       C  
-ATOM   3723  NZ  LYS B 687      26.585  23.121   2.311  1.00 99.13           N  
-ANISOU 3723  NZ  LYS B 687     9313  15375  12976    960    124    598       N  
-ATOM   3724  N   ARG B 688      19.900  20.743  -1.167  1.00 53.03           N  
-ANISOU 3724  N   ARG B 688     4253   8618   7277    836    273    897       N  
-ATOM   3725  CA  ARG B 688      18.618  20.893  -1.844  1.00 67.06           C  
-ANISOU 3725  CA  ARG B 688     6103  10202   9173    763    289    946       C  
-ATOM   3726  C   ARG B 688      17.485  20.288  -1.022  1.00 58.68           C  
-ANISOU 3726  C   ARG B 688     5175   9037   8083    757    301    820       C  
-ATOM   3727  O   ARG B 688      16.379  20.827  -0.984  1.00 54.79           O  
-ANISOU 3727  O   ARG B 688     4703   8359   7757    673    301    783       O  
-ATOM   3728  CB  ARG B 688      18.658  20.257  -3.233  1.00122.92           C  
-ANISOU 3728  CB  ARG B 688    13230  17342  16131    803    316   1115       C  
-ATOM   3729  CG  ARG B 688      19.566  20.973  -4.213  1.00145.75           C  
-ANISOU 3729  CG  ARG B 688    15987  20311  19081    787    304   1258       C  
-ATOM   3730  CD  ARG B 688      19.397  20.415  -5.609  1.00162.94           C  
-ANISOU 3730  CD  ARG B 688    18216  22529  21164    812    332   1419       C  
-ATOM   3731  NE  ARG B 688      19.735  18.998  -5.662  1.00183.59           N  
-ANISOU 3731  NE  ARG B 688    20940  25308  23508    932    362   1421       N  
-ATOM   3732  CZ  ARG B 688      20.965  18.534  -5.843  1.00198.77           C  
-ANISOU 3732  CZ  ARG B 688    22816  27449  25257   1030    366   1466       C  
-ATOM   3733  NH1 ARG B 688      21.976  19.379  -5.988  1.00202.54           N  
-ANISOU 3733  NH1 ARG B 688    23137  28016  25801   1011    340   1512       N  
-ATOM   3734  NH2 ARG B 688      21.185  17.226  -5.880  1.00203.78           N  
-ANISOU 3734  NH2 ARG B 688    23558  28216  25652   1151    395   1463       N  
-ATOM   3735  N   MET B 689      17.764  19.166  -0.365  1.00 47.22           N  
-ANISOU 3735  N   MET B 689     3810   7714   6417    852    310    757       N  
-ATOM   3736  CA  MET B 689      16.768  18.513   0.475  1.00 45.53           C  
-ANISOU 3736  CA  MET B 689     3719   7425   6157    850    319    639       C  
-ATOM   3737  C   MET B 689      16.572  19.290   1.771  1.00 43.81           C  
-ANISOU 3737  C   MET B 689     3437   7131   6079    792    293    474       C  
-ATOM   3738  O   MET B 689      15.446  19.493   2.223  1.00 50.91           O  
-ANISOU 3738  O   MET B 689     4382   7879   7082    724    295    386       O  
-ATOM   3739  CB  MET B 689      17.178  17.074   0.783  1.00 52.86           C  
-ANISOU 3739  CB  MET B 689     4756   8514   6814    980    334    633       C  
-ATOM   3740  CG  MET B 689      16.106  16.277   1.506  1.00 57.06           C  
-ANISOU 3740  CG  MET B 689     5424   8972   7285    981    344    537       C  
-ATOM   3741  SD  MET B 689      14.636  16.017   0.493  1.00 69.13           S  
-ANISOU 3741  SD  MET B 689     7060  10337   8871    906    371    609       S  
-ATOM   3742  CE  MET B 689      15.279  14.906  -0.756  1.00 46.91           C  
-ANISOU 3742  CE  MET B 689     4314   7671   5840   1021    400    773       C  
-ATOM   3743  N   LYS B 690      17.680  19.716   2.368  1.00 45.85           N  
-ANISOU 3743  N   LYS B 690     3583   7505   6332    821    270    427       N  
-ATOM   3744  CA  LYS B 690      17.641  20.562   3.554  1.00 43.29           C  
-ANISOU 3744  CA  LYS B 690     3174   7125   6150    765    245    270       C  
-ATOM   3745  C   LYS B 690      16.946  21.872   3.202  1.00 44.00           C  
-ANISOU 3745  C   LYS B 690     3188   7009   6520    645    237    270       C  
-ATOM   3746  O   LYS B 690      16.219  22.443   4.013  1.00 40.34           O  
-ANISOU 3746  O   LYS B 690     2710   6417   6199    581    229    136       O  
-ATOM   3747  CB  LYS B 690      19.061  20.822   4.055  1.00 42.86           C  
-ANISOU 3747  CB  LYS B 690     2996   7252   6037    818    222    242       C  
-ATOM   3748  CG  LYS B 690      19.153  21.546   5.387  1.00 59.16           C  
-ANISOU 3748  CG  LYS B 690     4971   9298   8208    775    196     66       C  
-ATOM   3749  CD  LYS B 690      20.556  21.398   5.961  1.00 75.22           C  
-ANISOU 3749  CD  LYS B 690     6913  11563  10104    857    177     36       C  
-ATOM   3750  CE  LYS B 690      21.219  22.743   6.209  1.00 80.34           C  
-ANISOU 3750  CE  LYS B 690     7379  12206  10942    781    150    -12       C  
-ATOM   3751  NZ  LYS B 690      22.707  22.640   6.128  1.00 75.56           N  
-ANISOU 3751  NZ  LYS B 690     6669  11841  10199    857    136     37       N  
-ATOM   3752  N   ARG B 691      17.177  22.336   1.980  1.00 50.50           N  
-ANISOU 3752  N   ARG B 691     3961   7806   7421    621    240    423       N  
-ATOM   3753  CA  ARG B 691      16.488  23.504   1.451  1.00 52.30           C  
-ANISOU 3753  CA  ARG B 691     4126   7838   7908    524    233    457       C  
-ATOM   3754  C   ARG B 691      14.988  23.273   1.476  1.00 47.56           C  
-ANISOU 3754  C   ARG B 691     3639   7074   7357    484    252    413       C  
-ATOM   3755  O   ARG B 691      14.233  24.038   2.075  1.00 47.71           O  
-ANISOU 3755  O   ARG B 691     3628   6943   7556    420    244    303       O  
-ATOM   3756  CB  ARG B 691      16.921  23.752   0.008  1.00 79.85           C  
-ANISOU 3756  CB  ARG B 691     7568  11351  11420    521    237    654       C  
-ATOM   3757  CG  ARG B 691      17.576  25.095  -0.225  1.00 93.93           C  
-ANISOU 3757  CG  ARG B 691     9181  13097  13410    463    208    695       C  
-ATOM   3758  CD  ARG B 691      18.056  25.219  -1.660  1.00100.32           C  
-ANISOU 3758  CD  ARG B 691     9946  13958  14213    467    211    900       C  
-ATOM   3759  NE  ARG B 691      19.507  25.358  -1.730  1.00110.20           N  
-ANISOU 3759  NE  ARG B 691    11082  15399  15390    500    194    947       N  
-ATOM   3760  CZ  ARG B 691      20.279  24.713  -2.598  1.00118.46           C  
-ANISOU 3760  CZ  ARG B 691    12131  16618  16258    562    205   1082       C  
-ATOM   3761  NH1 ARG B 691      19.741  23.878  -3.477  1.00123.77           N  
-ANISOU 3761  NH1 ARG B 691    12920  17293  16812    597    235   1182       N  
-ATOM   3762  NH2 ARG B 691      21.591  24.903  -2.589  1.00117.06           N  
-ANISOU 3762  NH2 ARG B 691    11837  16623  16018    590    187   1112       N  
-ATOM   3763  N   LEU B 692      14.571  22.207   0.802  1.00 58.30           N  
-ANISOU 3763  N   LEU B 692     5125   8473   8552    525    278    498       N  
-ATOM   3764  CA  LEU B 692      13.166  21.849   0.678  1.00 50.44           C  
-ANISOU 3764  CA  LEU B 692     4242   7350   7572    491    298    475       C  
-ATOM   3765  C   LEU B 692      12.524  21.643   2.043  1.00 48.31           C  
-ANISOU 3765  C   LEU B 692     4020   7041   7295    477    295    287       C  
-ATOM   3766  O   LEU B 692      11.481  22.223   2.345  1.00 43.44           O  
-ANISOU 3766  O   LEU B 692     3403   6272   6832    412    295    207       O  
-ATOM   3767  CB  LEU B 692      13.038  20.575  -0.156  1.00 33.70           C  
-ANISOU 3767  CB  LEU B 692     2246   5320   5239    550    325    586       C  
-ATOM   3768  CG  LEU B 692      11.644  19.992  -0.353  1.00 29.72           C  
-ANISOU 3768  CG  LEU B 692     1866   4718   4708    522    347    572       C  
-ATOM   3769  CD1 LEU B 692      10.744  20.988  -1.068  1.00 36.53           C  
-ANISOU 3769  CD1 LEU B 692     2684   5411   5786    444    346    623       C  
-ATOM   3770  CD2 LEU B 692      11.738  18.695  -1.133  1.00 18.71           C  
-ANISOU 3770  CD2 LEU B 692      581   3436   3090    590    371    677       C  
-ATOM   3771  N   MET B 693      13.158  20.809   2.860  1.00 45.97           N  
-ANISOU 3771  N   MET B 693     3760   6892   6813    544    292    218       N  
-ATOM   3772  CA  MET B 693      12.680  20.510   4.202  1.00 29.88           C  
-ANISOU 3772  CA  MET B 693     1765   4850   4740    540    287     45       C  
-ATOM   3773  C   MET B 693      12.209  21.771   4.916  1.00 32.32           C  
-ANISOU 3773  C   MET B 693     1976   5018   5286    457    271    -86       C  
-ATOM   3774  O   MET B 693      11.084  21.833   5.406  1.00 39.72           O  
-ANISOU 3774  O   MET B 693     2959   5848   6286    409    278   -187       O  
-ATOM   3775  CB  MET B 693      13.796  19.848   5.009  1.00 36.08           C  
-ANISOU 3775  CB  MET B 693     2541   5826   5340    628    276     -2       C  
-ATOM   3776  CG  MET B 693      13.332  18.754   5.947  1.00 33.37           C  
-ANISOU 3776  CG  MET B 693     2312   5539   4828    671    282    -98       C  
-ATOM   3777  SD  MET B 693      14.695  18.107   6.929  1.00 65.37           S  
-ANISOU 3777  SD  MET B 693     6338   9821   8679    790    264   -149       S  
-ATOM   3778  CE  MET B 693      15.943  17.845   5.667  1.00 17.86           C  
-ANISOU 3778  CE  MET B 693      291   3940   2554    876    270     39       C  
-ATOM   3779  N   ALA B 694      13.076  22.777   4.966  1.00 42.07           N  
-ANISOU 3779  N   ALA B 694     3073   6260   6654    442    250    -87       N  
-ATOM   3780  CA  ALA B 694      12.774  24.024   5.663  1.00 46.39           C  
-ANISOU 3780  CA  ALA B 694     3513   6680   7435    372    234   -216       C  
-ATOM   3781  C   ALA B 694      11.498  24.681   5.145  1.00 46.93           C  
-ANISOU 3781  C   ALA B 694     3593   6544   7694    305    244   -204       C  
-ATOM   3782  O   ALA B 694      10.710  25.220   5.922  1.00 51.61           O  
-ANISOU 3782  O   ALA B 694     4165   7028   8415    260    243   -347       O  
-ATOM   3783  CB  ALA B 694      13.943  24.986   5.558  1.00 50.96           C  
-ANISOU 3783  CB  ALA B 694     3937   7297   8129    364    210   -187       C  
-ATOM   3784  N   GLU B 695      11.305  24.639   3.831  1.00 48.97           N  
-ANISOU 3784  N   GLU B 695     3879   6762   7967    304    256    -32       N  
-ATOM   3785  CA  GLU B 695      10.124  25.229   3.210  1.00 54.96           C  
-ANISOU 3785  CA  GLU B 695     4644   7343   8893    252    266      3       C  
-ATOM   3786  C   GLU B 695       8.843  24.510   3.631  1.00 45.01           C  
-ANISOU 3786  C   GLU B 695     3507   6043   7552    241    286    -87       C  
-ATOM   3787  O   GLU B 695       7.791  25.134   3.772  1.00 38.66           O  
-ANISOU 3787  O   GLU B 695     2689   5098   6902    196    291   -154       O  
-ATOM   3788  CB  GLU B 695      10.259  25.219   1.685  1.00 63.75           C  
-ANISOU 3788  CB  GLU B 695     5762   8452  10008    261    273    215       C  
-ATOM   3789  CG  GLU B 695      11.455  25.997   1.160  1.00 65.20           C  
-ANISOU 3789  CG  GLU B 695     5814   8673  10284    262    252    319       C  
-ATOM   3790  CD  GLU B 695      11.419  27.460   1.558  1.00 70.14           C  
-ANISOU 3790  CD  GLU B 695     6300   9159  11190    207    229    248       C  
-ATOM   3791  OE1 GLU B 695      12.412  27.939   2.145  1.00 65.27           O  
-ANISOU 3791  OE1 GLU B 695     5581   8604  10615    206    208    190       O  
-ATOM   3792  OE2 GLU B 695      10.398  28.128   1.289  1.00 77.83           O  
-ANISOU 3792  OE2 GLU B 695     7261   9969  12342    168    232    247       O  
-ATOM   3793  N   CYS B 696       8.939  23.199   3.829  1.00 41.41           N  
-ANISOU 3793  N   CYS B 696     3165   5715   6852    286    299    -87       N  
-ATOM   3794  CA  CYS B 696       7.789  22.395   4.233  1.00 34.41           C  
-ANISOU 3794  CA  CYS B 696     2397   4811   5867    274    318   -165       C  
-ATOM   3795  C   CYS B 696       7.465  22.575   5.714  1.00 35.40           C  
-ANISOU 3795  C   CYS B 696     2503   4926   6021    251    309   -372       C  
-ATOM   3796  O   CYS B 696       6.335  22.347   6.140  1.00 31.01           O  
-ANISOU 3796  O   CYS B 696     2006   4315   5460    219    322   -464       O  
-ATOM   3797  CB  CYS B 696       8.035  20.914   3.932  1.00 35.08           C  
-ANISOU 3797  CB  CYS B 696     2606   5036   5688    333    332    -89       C  
-ATOM   3798  SG  CYS B 696       8.296  20.525   2.184  1.00 50.67           S  
-ANISOU 3798  SG  CYS B 696     4617   7039   7597    364    348    143       S  
-ATOM   3799  N   LEU B 697       8.460  22.981   6.495  1.00 52.53           N  
-ANISOU 3799  N   LEU B 697     4584   7160   8214    268    288   -447       N  
-ATOM   3800  CA  LEU B 697       8.285  23.152   7.935  1.00 48.63           C  
-ANISOU 3800  CA  LEU B 697     4061   6678   7738    250    279   -646       C  
-ATOM   3801  C   LEU B 697       8.032  24.612   8.303  1.00 44.90           C  
-ANISOU 3801  C   LEU B 697     3460   6067   7533    195    267   -748       C  
-ATOM   3802  O   LEU B 697       7.988  24.969   9.481  1.00 46.60           O  
-ANISOU 3802  O   LEU B 697     3623   6287   7795    178    258   -921       O  
-ATOM   3803  CB  LEU B 697       9.509  22.625   8.686  1.00 36.53           C  
-ANISOU 3803  CB  LEU B 697     2509   5322   6048    309    263   -682       C  
-ATOM   3804  CG  LEU B 697       9.848  21.152   8.454  1.00 32.49           C  
-ANISOU 3804  CG  LEU B 697     2118   4959   5268    381    272   -592       C  
-ATOM   3805  CD1 LEU B 697      11.208  20.806   9.040  1.00 28.91           C  
-ANISOU 3805  CD1 LEU B 697     1621   4684   4681    456    254   -605       C  
-ATOM   3806  CD2 LEU B 697       8.764  20.253   9.028  1.00 30.94           C  
-ANISOU 3806  CD2 LEU B 697     2038   4760   4957    369    287   -670       C  
-ATOM   3807  N   LYS B 698       7.864  25.449   7.285  1.00 39.32           N  
-ANISOU 3807  N   LYS B 698     2699   5238   7003    172    268   -639       N  
-ATOM   3808  CA  LYS B 698       7.645  26.877   7.482  1.00 39.96           C  
-ANISOU 3808  CA  LYS B 698     2651   5174   7358    128    256   -713       C  
-ATOM   3809  C   LYS B 698       6.575  27.128   8.538  1.00 59.86           C  
-ANISOU 3809  C   LYS B 698     5173   7623   9947     93    263   -909       C  
-ATOM   3810  O   LYS B 698       5.541  26.466   8.551  1.00 71.15           O  
-ANISOU 3810  O   LYS B 698     6705   9044  11285     86    282   -931       O  
-ATOM   3811  CB  LYS B 698       7.230  27.522   6.162  1.00 31.35           C  
-ANISOU 3811  CB  LYS B 698     1533   3953   6424    111    260   -555       C  
-ATOM   3812  CG  LYS B 698       7.843  28.884   5.908  1.00 33.90           C  
-ANISOU 3812  CG  LYS B 698     1701   4185   6994     89    237   -525       C  
-ATOM   3813  CD  LYS B 698       9.360  28.825   5.933  1.00 34.71           C  
-ANISOU 3813  CD  LYS B 698     1743   4422   7026    113    219   -475       C  
-ATOM   3814  CE  LYS B 698       9.955  29.923   5.063  1.00 50.52           C  
-ANISOU 3814  CE  LYS B 698     3616   6347   9231     93    200   -347       C  
-ATOM   3815  NZ  LYS B 698      11.353  30.259   5.461  1.00 54.89           N  
-ANISOU 3815  NZ  LYS B 698     4063   7009   9785     97    177   -367       N  
-ATOM   3816  N   LYS B 699       6.829  28.087   9.423  1.00 53.85           N  
-ANISOU 3816  N   LYS B 699     4294   6820   9348     72    247  -1056       N  
-ATOM   3817  CA  LYS B 699       5.881  28.419  10.480  1.00 49.03           C  
-ANISOU 3817  CA  LYS B 699     3667   6150   8814     41    254  -1256       C  
-ATOM   3818  C   LYS B 699       4.535  28.843   9.890  1.00 51.97           C  
-ANISOU 3818  C   LYS B 699     4056   6369   9320     16    270  -1235       C  
-ATOM   3819  O   LYS B 699       3.487  28.327  10.280  1.00 54.88           O  
-ANISOU 3819  O   LYS B 699     4502   6743   9607      3    288  -1318       O  
-ATOM   3820  CB  LYS B 699       6.444  29.528  11.372  1.00 58.70           C  
-ANISOU 3820  CB  LYS B 699     4740   7342  10220     22    234  -1405       C  
-ATOM   3821  CG  LYS B 699       6.383  29.235  12.868  1.00 58.29           C  
-ANISOU 3821  CG  LYS B 699     4685   7385  10077     17    234  -1620       C  
-ATOM   3822  CD  LYS B 699       7.684  28.624  13.375  1.00 57.02           C  
-ANISOU 3822  CD  LYS B 699     4519   7409   9737     51    219  -1621       C  
-ATOM   3823  CE  LYS B 699       7.581  27.117  13.527  1.00 59.43           C  
-ANISOU 3823  CE  LYS B 699     4971   7860   9750     86    229  -1582       C  
-ATOM   3824  NZ  LYS B 699       6.729  26.733  14.688  1.00 62.36           N  
-ANISOU 3824  NZ  LYS B 699     5381   8265  10048     67    239  -1762       N  
-ATOM   3825  N   LYS B 700       4.572  29.780   8.946  1.00 66.98           N  
-ANISOU 3825  N   LYS B 700     5880   8146  11424      8    263  -1121       N  
-ATOM   3826  CA  LYS B 700       3.361  30.253   8.279  1.00 77.54           C  
-ANISOU 3826  CA  LYS B 700     7219   9344  12899     -8    275  -1080       C  
-ATOM   3827  C   LYS B 700       2.894  29.261   7.214  1.00 82.14           C  
-ANISOU 3827  C   LYS B 700     7931   9969  13308      7    294   -913       C  
-ATOM   3828  O   LYS B 700       3.654  28.899   6.316  1.00 94.58           O  
-ANISOU 3828  O   LYS B 700     9533  11597  14807     28    290   -742       O  
-ATOM   3829  CB  LYS B 700       3.591  31.634   7.660  1.00 82.61           C  
-ANISOU 3829  CB  LYS B 700     7722   9839  13829    -20    258  -1010       C  
-ATOM   3830  CG  LYS B 700       4.146  32.663   8.637  1.00 94.81           C  
-ANISOU 3830  CG  LYS B 700     9125  11339  15559    -37    238  -1168       C  
-ATOM   3831  CD  LYS B 700       4.119  34.067   8.050  1.00 97.83           C  
-ANISOU 3831  CD  LYS B 700     9368  11552  16252    -53    221  -1110       C  
-ATOM   3832  CE  LYS B 700       4.827  35.064   8.956  1.00 92.33           C  
-ANISOU 3832  CE  LYS B 700     8523  10820  15737    -73    200  -1257       C  
-ATOM   3833  NZ  LYS B 700       6.295  34.821   9.016  1.00 84.11           N  
-ANISOU 3833  NZ  LYS B 700     7456   9907  14596    -69    184  -1206       N  
-ATOM   3834  N   ARG B 701       1.639  28.832   7.318  1.00 61.00           N  
-ANISOU 3834  N   ARG B 701     5329   7277  10570     -6    316   -969       N  
-ATOM   3835  CA  ARG B 701       1.096  27.784   6.453  1.00 50.79           C  
-ANISOU 3835  CA  ARG B 701     4165   6040   9093      4    336   -841       C  
-ATOM   3836  C   ARG B 701       1.188  28.076   4.956  1.00 49.53           C  
-ANISOU 3836  C   ARG B 701     3992   5823   9005     15    336   -624       C  
-ATOM   3837  O   ARG B 701       1.466  27.179   4.161  1.00 55.10           O  
-ANISOU 3837  O   ARG B 701     4785   6611   9539     35    344   -483       O  
-ATOM   3838  CB  ARG B 701      -0.356  27.473   6.830  1.00 59.08           C  
-ANISOU 3838  CB  ARG B 701     5272   7075  10099    -19    358   -950       C  
-ATOM   3839  CG  ARG B 701      -1.260  28.686   6.947  1.00 67.58           C  
-ANISOU 3839  CG  ARG B 701     6245   8011  11421    -38    358  -1031       C  
-ATOM   3840  CD  ARG B 701      -2.621  28.299   7.500  1.00 59.82           C  
-ANISOU 3840  CD  ARG B 701     5315   7049  10365    -60    380  -1164       C  
-ATOM   3841  NE  ARG B 701      -3.383  27.482   6.561  1.00 68.81           N  
-ANISOU 3841  NE  ARG B 701     6557   8228  11360    -60    401  -1043       N  
-ATOM   3842  CZ  ARG B 701      -4.566  26.942   6.832  1.00 83.16           C  
-ANISOU 3842  CZ  ARG B 701     8437  10090  13073    -82    424  -1126       C  
-ATOM   3843  NH1 ARG B 701      -5.122  27.127   8.022  1.00 91.76           N  
-ANISOU 3843  NH1 ARG B 701     9496  11190  14180   -104    428  -1327       N  
-ATOM   3844  NH2 ARG B 701      -5.192  26.215   5.917  1.00 78.97           N  
-ANISOU 3844  NH2 ARG B 701     7992   9600  12413    -82    442  -1010       N  
-ATOM   3845  N   ASP B 702       0.947  29.323   4.570  1.00 50.87           N  
-ANISOU 3845  N   ASP B 702     4046   5854   9428      5    325   -596       N  
-ATOM   3846  CA  ASP B 702       0.903  29.667   3.153  1.00 49.59           C  
-ANISOU 3846  CA  ASP B 702     3861   5634   9346     13    324   -389       C  
-ATOM   3847  C   ASP B 702       2.270  30.023   2.575  1.00 50.96           C  
-ANISOU 3847  C   ASP B 702     3969   5825   9571     25    303   -252       C  
-ATOM   3848  O   ASP B 702       2.369  30.503   1.446  1.00 51.96           O  
-ANISOU 3848  O   ASP B 702     4048   5897   9797     29    297    -80       O  
-ATOM   3849  CB  ASP B 702      -0.112  30.784   2.897  1.00 74.93           C  
-ANISOU 3849  CB  ASP B 702     6979   8692  12798     -3    323   -403       C  
-ATOM   3850  CG  ASP B 702      -1.546  30.314   3.064  1.00 84.80           C  
-ANISOU 3850  CG  ASP B 702     8302   9950  13967    -12    347   -483       C  
-ATOM   3851  OD1 ASP B 702      -1.785  29.090   2.976  1.00 76.63           O  
-ANISOU 3851  OD1 ASP B 702     7396   9030  12688     -8    366   -467       O  
-ATOM   3852  OD2 ASP B 702      -2.434  31.165   3.281  1.00 88.39           O  
-ANISOU 3852  OD2 ASP B 702     8680  10301  14602    -23    347   -562       O  
-ATOM   3853  N   GLU B 703       3.322  29.785   3.353  1.00 53.72           N  
-ANISOU 3853  N   GLU B 703     4308   6259   9845     33    291   -326       N  
-ATOM   3854  CA  GLU B 703       4.684  29.915   2.846  1.00 56.68           C  
-ANISOU 3854  CA  GLU B 703     4631   6692  10215     47    273   -200       C  
-ATOM   3855  C   GLU B 703       5.223  28.538   2.489  1.00 54.04           C  
-ANISOU 3855  C   GLU B 703     4418   6523   9593     79    285   -112       C  
-ATOM   3856  O   GLU B 703       6.332  28.405   1.965  1.00 53.66           O  
-ANISOU 3856  O   GLU B 703     4345   6556   9487     99    275      7       O  
-ATOM   3857  CB  GLU B 703       5.597  30.582   3.874  1.00 70.49           C  
-ANISOU 3857  CB  GLU B 703     6272   8446  12065     38    250   -331       C  
-ATOM   3858  CG  GLU B 703       5.325  32.057   4.095  1.00 80.26           C  
-ANISOU 3858  CG  GLU B 703     7365   9518  13613      8    234   -395       C  
-ATOM   3859  CD  GLU B 703       6.409  32.727   4.917  1.00 86.63           C  
-ANISOU 3859  CD  GLU B 703     8054  10343  14519     -4    210   -496       C  
-ATOM   3860  OE1 GLU B 703       6.067  33.444   5.879  1.00 86.94           O  
-ANISOU 3860  OE1 GLU B 703     8019  10304  14711    -24    204   -674       O  
-ATOM   3861  OE2 GLU B 703       7.603  32.531   4.605  1.00 85.52           O  
-ANISOU 3861  OE2 GLU B 703     7890  10306  14299      7    197   -401       O  
-ATOM   3862  N   ARG B 704       4.427  27.515   2.782  1.00 49.91           N  
-ANISOU 3862  N   ARG B 704     4019   6053   8890     85    307   -173       N  
-ATOM   3863  CA  ARG B 704       4.796  26.139   2.481  1.00 52.54           C  
-ANISOU 3863  CA  ARG B 704     4475   6535   8953    118    320   -100       C  
-ATOM   3864  C   ARG B 704       4.495  25.810   1.028  1.00 51.50           C  
-ANISOU 3864  C   ARG B 704     4391   6403   8774    128    333     95       C  
-ATOM   3865  O   ARG B 704       3.470  26.231   0.491  1.00 53.60           O  
-ANISOU 3865  O   ARG B 704     4650   6570   9146    107    342    128       O  
-ATOM   3866  CB  ARG B 704       4.048  25.172   3.397  1.00 55.56           C  
-ANISOU 3866  CB  ARG B 704     4966   6973   9170    114    336   -243       C  
-ATOM   3867  CG  ARG B 704       4.161  25.513   4.868  1.00 52.04           C  
-ANISOU 3867  CG  ARG B 704     4472   6528   8773    100    325   -447       C  
-ATOM   3868  CD  ARG B 704       4.223  24.255   5.704  1.00 55.45           C  
-ANISOU 3868  CD  ARG B 704     5009   7095   8963    118    333   -534       C  
-ATOM   3869  NE  ARG B 704       2.963  23.952   6.375  1.00 65.03           N  
-ANISOU 3869  NE  ARG B 704     6281   8281  10146     86    348   -668       N  
-ATOM   3870  CZ  ARG B 704       2.705  24.257   7.642  1.00 70.62           C  
-ANISOU 3870  CZ  ARG B 704     6951   8984  10898     64    343   -857       C  
-ATOM   3871  NH1 ARG B 704       3.618  24.877   8.374  1.00 74.77           N  
-ANISOU 3871  NH1 ARG B 704     7380   9525  11503     71    323   -936       N  
-ATOM   3872  NH2 ARG B 704       1.539  23.940   8.180  1.00 75.54           N  
-ANISOU 3872  NH2 ARG B 704     7626   9596  11480     34    359   -970       N  
-ATOM   3873  N   PRO B 705       5.393  25.050   0.388  1.00 53.50           N  
-ANISOU 3873  N   PRO B 705     4686   6779   8862    164    335    222       N  
-ATOM   3874  CA  PRO B 705       5.251  24.666  -1.019  1.00 49.78           C  
-ANISOU 3874  CA  PRO B 705     4257   6332   8325    179    347    410       C  
-ATOM   3875  C   PRO B 705       4.079  23.713  -1.220  1.00 47.41           C  
-ANISOU 3875  C   PRO B 705     4082   6046   7884    176    372    395       C  
-ATOM   3876  O   PRO B 705       3.435  23.311  -0.251  1.00 52.42           O  
-ANISOU 3876  O   PRO B 705     4774   6680   8465    163    379    243       O  
-ATOM   3877  CB  PRO B 705       6.565  23.933  -1.317  1.00 43.15           C  
-ANISOU 3877  CB  PRO B 705     3437   5648   7311    225    345    500       C  
-ATOM   3878  CG  PRO B 705       7.504  24.339  -0.227  1.00 44.39           C  
-ANISOU 3878  CG  PRO B 705     3520   5837   7510    230    325    386       C  
-ATOM   3879  CD  PRO B 705       6.643  24.540   0.973  1.00 46.03           C  
-ANISOU 3879  CD  PRO B 705     3740   5968   7782    199    325    192       C  
-ATOM   3880  N   SER B 706       3.807  23.363  -2.472  1.00 37.15           N  
-ANISOU 3880  N   SER B 706     2820   4768   6526    187    383    551       N  
-ATOM   3881  CA  SER B 706       2.803  22.357  -2.784  1.00 36.83           C  
-ANISOU 3881  CA  SER B 706     2899   4763   6332    188    405    550       C  
-ATOM   3882  C   SER B 706       3.494  21.135  -3.370  1.00 31.22           C  
-ANISOU 3882  C   SER B 706     2273   4195   5393    234    414    649       C  
-ATOM   3883  O   SER B 706       4.610  21.233  -3.876  1.00 31.29           O  
-ANISOU 3883  O   SER B 706     2237   4267   5387    263    407    757       O  
-ATOM   3884  CB  SER B 706       1.764  22.911  -3.758  1.00 59.07           C  
-ANISOU 3884  CB  SER B 706     5689   7495   9262    166    411    638       C  
-ATOM   3885  OG  SER B 706       1.024  23.964  -3.166  1.00 58.81           O  
-ANISOU 3885  OG  SER B 706     5581   7334   9431    132    405    535       O  
-ATOM   3886  N   PHE B 707       2.830  19.986  -3.306  1.00 29.58           N  
-ANISOU 3886  N   PHE B 707     2185   4045   5011    241    430    611       N  
-ATOM   3887  CA  PHE B 707       3.455  18.723  -3.700  1.00 26.85           C  
-ANISOU 3887  CA  PHE B 707     1925   3832   4443    293    439    680       C  
-ATOM   3888  C   PHE B 707       3.882  18.610  -5.166  1.00 32.30           C  
-ANISOU 3888  C   PHE B 707     2602   4576   5094    322    444    871       C  
-ATOM   3889  O   PHE B 707       4.770  17.822  -5.488  1.00 52.69           O  
-ANISOU 3889  O   PHE B 707     5220   7275   7523    375    449    938       O  
-ATOM   3890  CB  PHE B 707       2.595  17.529  -3.280  1.00 18.37           C  
-ANISOU 3890  CB  PHE B 707      976   2796   3208    292    452    593       C  
-ATOM   3891  CG  PHE B 707       2.881  17.049  -1.886  1.00 23.48           C  
-ANISOU 3891  CG  PHE B 707     1659   3482   3780    299    448    447       C  
-ATOM   3892  CD1 PHE B 707       3.925  16.173  -1.645  1.00 18.63           C  
-ANISOU 3892  CD1 PHE B 707     1087   2985   3005    363    447    468       C  
-ATOM   3893  CD2 PHE B 707       2.123  17.490  -0.815  1.00 39.21           C  
-ANISOU 3893  CD2 PHE B 707     3636   5402   5859    250    445    289       C  
-ATOM   3894  CE1 PHE B 707       4.199  15.737  -0.361  1.00 16.36           C  
-ANISOU 3894  CE1 PHE B 707      828   2743   2647    378    442    342       C  
-ATOM   3895  CE2 PHE B 707       2.394  17.056   0.470  1.00 31.24           C  
-ANISOU 3895  CE2 PHE B 707     2654   4439   4778    256    440    158       C  
-ATOM   3896  CZ  PHE B 707       3.433  16.179   0.696  1.00 19.27           C  
-ANISOU 3896  CZ  PHE B 707     1180   3040   3103    321    437    189       C  
-ATOM   3897  N   PRO B 708       3.250  19.381  -6.062  1.00 25.42           N  
-ANISOU 3897  N   PRO B 708     1676   3627   4354    293    442    959       N  
-ATOM   3898  CA  PRO B 708       3.798  19.417  -7.420  1.00 24.28           C  
-ANISOU 3898  CA  PRO B 708     1498   3541   4187    318    443   1145       C  
-ATOM   3899  C   PRO B 708       5.214  19.983  -7.418  1.00 26.36           C  
-ANISOU 3899  C   PRO B 708     1669   3845   4503    338    432   1207       C  
-ATOM   3900  O   PRO B 708       6.108  19.427  -8.058  1.00 33.80           O  
-ANISOU 3900  O   PRO B 708     2620   4907   5317    383    438   1310       O  
-ATOM   3901  CB  PRO B 708       2.859  20.378  -8.146  1.00 24.54           C  
-ANISOU 3901  CB  PRO B 708     1465   3469   4391    279    439   1212       C  
-ATOM   3902  CG  PRO B 708       1.576  20.274  -7.410  1.00 21.15           C  
-ANISOU 3902  CG  PRO B 708     1087   2969   3981    247    444   1066       C  
-ATOM   3903  CD  PRO B 708       1.943  20.053  -5.975  1.00 20.56           C  
-ANISOU 3903  CD  PRO B 708     1039   2894   3879    244    442    902       C  
-ATOM   3904  N   ARG B 709       5.404  21.084  -6.699  1.00 30.48           N  
-ANISOU 3904  N   ARG B 709     2097   4273   5212    307    415   1140       N  
-ATOM   3905  CA  ARG B 709       6.709  21.726  -6.583  1.00 41.04           C  
-ANISOU 3905  CA  ARG B 709     3332   5644   6617    319    399   1180       C  
-ATOM   3906  C   ARG B 709       7.645  20.864  -5.737  1.00 42.73           C  
-ANISOU 3906  C   ARG B 709     3594   5982   6659    365    401   1098       C  
-ATOM   3907  O   ARG B 709       8.833  20.735  -6.037  1.00 42.25           O  
-ANISOU 3907  O   ARG B 709     3492   6033   6526    405    398   1175       O  
-ATOM   3908  CB  ARG B 709       6.550  23.124  -5.971  1.00 61.36           C  
-ANISOU 3908  CB  ARG B 709     5792   8074   9447    272    377   1112       C  
-ATOM   3909  CG  ARG B 709       7.804  23.997  -5.987  1.00 81.21           C  
-ANISOU 3909  CG  ARG B 709     8178  10604  12074    273    355   1167       C  
-ATOM   3910  CD  ARG B 709       8.740  23.669  -4.829  1.00 97.36           C  
-ANISOU 3910  CD  ARG B 709    10224  12734  14035    298    347   1042       C  
-ATOM   3911  NE  ARG B 709       9.847  24.617  -4.714  1.00101.59           N  
-ANISOU 3911  NE  ARG B 709    10622  13278  14698    290    321   1070       N  
-ATOM   3912  CZ  ARG B 709       9.938  25.556  -3.776  1.00100.91           C  
-ANISOU 3912  CZ  ARG B 709    10450  13102  14788    258    300    951       C  
-ATOM   3913  NH1 ARG B 709       8.988  25.678  -2.859  1.00 90.79           N  
-ANISOU 3913  NH1 ARG B 709     9204  11718  13573    233    303    794       N  
-ATOM   3914  NH2 ARG B 709      10.983  26.372  -3.751  1.00109.55           N  
-ANISOU 3914  NH2 ARG B 709    11416  14216  15990    250    276    985       N  
-ATOM   3915  N   ILE B 710       7.098  20.272  -4.681  1.00 42.93           N  
-ANISOU 3915  N   ILE B 710     3702   5998   6613    364    407    944       N  
-ATOM   3916  CA  ILE B 710       7.866  19.397  -3.803  1.00 38.79           C  
-ANISOU 3916  CA  ILE B 710     3228   5591   5919    414    408    862       C  
-ATOM   3917  C   ILE B 710       8.408  18.186  -4.555  1.00 40.62           C  
-ANISOU 3917  C   ILE B 710     3538   5970   5927    484    426    966       C  
-ATOM   3918  O   ILE B 710       9.596  17.878  -4.475  1.00 45.81           O  
-ANISOU 3918  O   ILE B 710     4171   6751   6482    543    425    996       O  
-ATOM   3919  CB  ILE B 710       7.020  18.918  -2.605  1.00 34.21           C  
-ANISOU 3919  CB  ILE B 710     2727   4972   5298    396    411    689       C  
-ATOM   3920  CG1 ILE B 710       6.720  20.084  -1.662  1.00 25.39           C  
-ANISOU 3920  CG1 ILE B 710     1523   3736   4387    342    394    561       C  
-ATOM   3921  CG2 ILE B 710       7.731  17.799  -1.859  1.00 25.23           C  
-ANISOU 3921  CG2 ILE B 710     1660   3972   3956    462    414    631       C  
-ATOM   3922  CD1 ILE B 710       5.850  19.702  -0.484  1.00 19.76           C  
-ANISOU 3922  CD1 ILE B 710      876   2991   3642    318    397    387       C  
-ATOM   3923  N   LEU B 711       7.533  17.499  -5.284  1.00 49.41           N  
-ANISOU 3923  N   LEU B 711     4738   7075   6961    482    443   1017       N  
-ATOM   3924  CA  LEU B 711       7.940  16.334  -6.063  1.00 52.89           C  
-ANISOU 3924  CA  LEU B 711     5254   7646   7197    551    460   1112       C  
-ATOM   3925  C   LEU B 711       8.931  16.715  -7.159  1.00 54.96           C  
-ANISOU 3925  C   LEU B 711     5432   7985   7464    578    461   1271       C  
-ATOM   3926  O   LEU B 711       9.840  15.953  -7.478  1.00 63.21           O  
-ANISOU 3926  O   LEU B 711     6499   9173   8345    653    473   1329       O  
-ATOM   3927  CB  LEU B 711       6.723  15.637  -6.675  1.00 41.64           C  
-ANISOU 3927  CB  LEU B 711     3924   6186   5711    535    471   1130       C  
-ATOM   3928  CG  LEU B 711       7.020  14.476  -7.627  1.00 38.95           C  
-ANISOU 3928  CG  LEU B 711     3656   5965   5177    605    486   1233       C  
-ATOM   3929  CD1 LEU B 711       7.930  13.457  -6.963  1.00 31.44           C  
-ANISOU 3929  CD1 LEU B 711     2765   5133   4047    695    493   1189       C  
-ATOM   3930  CD2 LEU B 711       5.734  13.819  -8.106  1.00 44.71           C  
-ANISOU 3930  CD2 LEU B 711     4473   6653   5862    584    488   1226       C  
-ATOM   3931  N   ALA B 712       8.747  17.900  -7.731  1.00 48.93           N  
-ANISOU 3931  N   ALA B 712     4568   7133   6889    521    450   1343       N  
-ATOM   3932  CA  ALA B 712       9.619  18.383  -8.796  1.00 52.14           C  
-ANISOU 3932  CA  ALA B 712     4881   7607   7322    534    447   1502       C  
-ATOM   3933  C   ALA B 712      11.048  18.589  -8.298  1.00 58.61           C  
-ANISOU 3933  C   ALA B 712     5625   8529   8115    574    438   1492       C  
-ATOM   3934  O   ALA B 712      12.012  18.220  -8.972  1.00 55.92           O  
-ANISOU 3934  O   ALA B 712     5259   8332   7657    629    447   1594       O  
-ATOM   3935  CB  ALA B 712       9.070  19.667  -9.378  1.00 70.02           C  
-ANISOU 3935  CB  ALA B 712     7051   9741   9814    466    432   1575       C  
-ATOM   3936  N   GLU B 713      11.172  19.192  -7.119  1.00 54.93           N  
-ANISOU 3936  N   GLU B 713     5115   7999   7756    548    419   1365       N  
-ATOM   3937  CA  GLU B 713      12.471  19.397  -6.484  1.00 48.88           C  
-ANISOU 3937  CA  GLU B 713     4274   7333   6966    586    404   1331       C  
-ATOM   3938  C   GLU B 713      13.142  18.071  -6.139  1.00 57.48           C  
-ANISOU 3938  C   GLU B 713     5449   8591   7801    683    422   1298       C  
-ATOM   3939  O   GLU B 713      14.272  17.811  -6.552  1.00 69.05           O  
-ANISOU 3939  O   GLU B 713     6871  10209   9154    748    426   1375       O  
-ATOM   3940  CB  GLU B 713      12.321  20.249  -5.221  1.00 32.85           C  
-ANISOU 3940  CB  GLU B 713     2188   5196   5099    538    380   1181       C  
-ATOM   3941  CG  GLU B 713      12.608  21.731  -5.421  1.00 52.43           C  
-ANISOU 3941  CG  GLU B 713     4518   7584   7819    478    354   1225       C  
-ATOM   3942  CD  GLU B 713      14.086  22.018  -5.614  1.00 68.35           C  
-ANISOU 3942  CD  GLU B 713     6425   9740   9805    512    339   1295       C  
-ATOM   3943  OE1 GLU B 713      14.481  23.201  -5.536  1.00 78.00           O  
-ANISOU 3943  OE1 GLU B 713     7517  10902  11218    466    312   1307       O  
-ATOM   3944  OE2 GLU B 713      14.856  21.060  -5.838  1.00 70.03           O  
-ANISOU 3944  OE2 GLU B 713     6678  10126   9803    588    354   1336       O  
-ATOM   3945  N   ILE B 714      12.439  17.238  -5.378  1.00 49.43           N  
-ANISOU 3945  N   ILE B 714     4545   7546   6689    699    431   1186       N  
-ATOM   3946  CA  ILE B 714      12.950  15.928  -4.983  1.00 46.06           C  
-ANISOU 3946  CA  ILE B 714     4211   7262   6026    802    446   1152       C  
-ATOM   3947  C   ILE B 714      13.356  15.080  -6.190  1.00 68.14           C  
-ANISOU 3947  C   ILE B 714     7051  10183   8657    874    472   1289       C  
-ATOM   3948  O   ILE B 714      14.423  14.465  -6.196  1.00 77.79           O  
-ANISOU 3948  O   ILE B 714     8273  11566   9718    976    481   1315       O  
-ATOM   3949  CB  ILE B 714      11.917  15.150  -4.138  1.00 34.63           C  
-ANISOU 3949  CB  ILE B 714     2890   5749   4520    797    451   1030       C  
-ATOM   3950  CG1 ILE B 714      11.725  15.813  -2.771  1.00 42.37           C  
-ANISOU 3950  CG1 ILE B 714     3828   6651   5620    748    428    876       C  
-ATOM   3951  CG2 ILE B 714      12.354  13.709  -3.958  1.00 35.18           C  
-ANISOU 3951  CG2 ILE B 714     3067   5954   4345    915    467   1027       C  
-ATOM   3952  CD1 ILE B 714      10.666  15.152  -1.908  1.00 30.61           C  
-ANISOU 3952  CD1 ILE B 714     2447   5097   4086    730    431    755       C  
-ATOM   3953  N   GLU B 715      12.500  15.049  -7.208  1.00 80.06           N  
-ANISOU 3953  N   GLU B 715     8593  11623  10202    830    483   1372       N  
-ATOM   3954  CA  GLU B 715      12.759  14.260  -8.409  1.00 73.41           C  
-ANISOU 3954  CA  GLU B 715     7790  10892   9210    892    508   1497       C  
-ATOM   3955  C   GLU B 715      14.003  14.760  -9.135  1.00 75.14           C  
-ANISOU 3955  C   GLU B 715     7891  11235   9424    923    508   1613       C  
-ATOM   3956  O   GLU B 715      14.834  13.969  -9.583  1.00 80.25           O  
-ANISOU 3956  O   GLU B 715     8557  12044   9891   1022    528   1669       O  
-ATOM   3957  CB  GLU B 715      11.559  14.316  -9.356  1.00 54.81           C  
-ANISOU 3957  CB  GLU B 715     5471   8435   6919    827    512   1562       C  
-ATOM   3958  CG  GLU B 715      11.577  13.261 -10.449  1.00 62.36           C  
-ANISOU 3958  CG  GLU B 715     6497   9495   7701    895    535   1658       C  
-ATOM   3959  CD  GLU B 715      10.817  12.007 -10.059  1.00 68.55           C  
-ANISOU 3959  CD  GLU B 715     7428  10263   8354    938    541   1578       C  
-ATOM   3960  OE1 GLU B 715       9.627  12.120  -9.696  1.00 62.29           O  
-ANISOU 3960  OE1 GLU B 715     6679   9339   7649    868    529   1506       O  
-ATOM   3961  OE2 GLU B 715      11.407  10.909 -10.124  1.00 77.22           O  
-ANISOU 3961  OE2 GLU B 715     8596  11480   9264   1049    556   1587       O  
-ATOM   3962  N   GLU B 716      14.119  16.078  -9.250  1.00 58.99           N  
-ANISOU 3962  N   GLU B 716     5722   9115   7578    842    485   1649       N  
-ATOM   3963  CA  GLU B 716      15.244  16.690  -9.942  1.00 68.86           C  
-ANISOU 3963  CA  GLU B 716     6843  10472   8848    855    479   1765       C  
-ATOM   3964  C   GLU B 716      16.565  16.319  -9.274  1.00 69.13           C  
-ANISOU 3964  C   GLU B 716     6844  10674   8748    948    477   1717       C  
-ATOM   3965  O   GLU B 716      17.494  15.859  -9.935  1.00 66.94           O  
-ANISOU 3965  O   GLU B 716     6541  10570   8325   1027    493   1802       O  
-ATOM   3966  CB  GLU B 716      15.077  18.213  -9.991  1.00113.00           C  
-ANISOU 3966  CB  GLU B 716    12308  15929  14699    752    447   1796       C  
-ATOM   3967  CG  GLU B 716      15.915  18.913 -11.056  1.00133.80           C  
-ANISOU 3967  CG  GLU B 716    14810  18646  17383    742    439   1956       C  
-ATOM   3968  CD  GLU B 716      17.359  19.125 -10.637  1.00152.19           C  
-ANISOU 3968  CD  GLU B 716    17039  21125  19663    789    425   1947       C  
-ATOM   3969  OE1 GLU B 716      18.141  19.658 -11.452  1.00159.22           O  
-ANISOU 3969  OE1 GLU B 716    17813  22104  20578    783    415   2075       O  
-ATOM   3970  OE2 GLU B 716      17.714  18.767  -9.495  1.00157.78           O  
-ANISOU 3970  OE2 GLU B 716    17776  21870  20303    833    420   1815       O  
-ATOM   3971  N   LEU B 717      16.640  16.512  -7.960  1.00 93.24           N  
-ANISOU 3971  N   LEU B 717     9897  13687  11843    944    458   1579       N  
-ATOM   3972  CA  LEU B 717      17.887  16.300  -7.227  1.00 90.51           C  
-ANISOU 3972  CA  LEU B 717     9504  13500  11385   1031    450   1526       C  
-ATOM   3973  C   LEU B 717      18.344  14.842  -7.231  1.00 97.93           C  
-ANISOU 3973  C   LEU B 717    10551  14603  12056   1173    479   1521       C  
-ATOM   3974  O   LEU B 717      19.541  14.560  -7.243  1.00107.62           O  
-ANISOU 3974  O   LEU B 717    11728  16013  13149   1272    482   1545       O  
-ATOM   3975  CB  LEU B 717      17.780  16.834  -5.793  1.00 58.29           C  
-ANISOU 3975  CB  LEU B 717     5399   9337   7412    993    421   1372       C  
-ATOM   3976  CG  LEU B 717      16.898  16.133  -4.762  1.00 55.48           C  
-ANISOU 3976  CG  LEU B 717     5171   8901   7007   1002    426   1235       C  
-ATOM   3977  CD1 LEU B 717      17.597  14.910  -4.194  1.00 54.42           C  
-ANISOU 3977  CD1 LEU B 717     5115   8934   6629   1144    438   1189       C  
-ATOM   3978  CD2 LEU B 717      16.552  17.098  -3.642  1.00 48.95           C  
-ANISOU 3978  CD2 LEU B 717     4286   7947   6367    919    395   1106       C  
-ATOM   3979  N   ALA B 718      17.388  13.919  -7.219  1.00 88.55           N  
-ANISOU 3979  N   ALA B 718     9508  13348  10789   1191    500   1489       N  
-ATOM   3980  CA  ALA B 718      17.707  12.496  -7.251  1.00 88.51           C  
-ANISOU 3980  CA  ALA B 718     9619  13473  10538   1333    528   1486       C  
-ATOM   3981  C   ALA B 718      18.510  12.148  -8.502  1.00101.20           C  
-ANISOU 3981  C   ALA B 718    11190  15240  12020   1409    554   1619       C  
-ATOM   3982  O   ALA B 718      19.447  11.349  -8.449  1.00 96.19           O  
-ANISOU 3982  O   ALA B 718    10579  14778  11192   1553    570   1623       O  
-ATOM   3983  CB  ALA B 718      16.440  11.665  -7.181  1.00 58.01           C  
-ANISOU 3983  CB  ALA B 718     5908   9493   6641   1321    541   1445       C  
-ATOM   3984  N   ARG B 719      18.130  12.748  -9.627  1.00123.94           N  
-ANISOU 3984  N   ARG B 719    14014  18068  15009   1320    557   1729       N  
-ATOM   3985  CA  ARG B 719      18.857  12.573 -10.879  1.00118.75           C  
-ANISOU 3985  CA  ARG B 719    13303  17563  14255   1374    579   1862       C  
-ATOM   3986  C   ARG B 719      20.140  13.395 -10.875  1.00114.53           C  
-ANISOU 3986  C   ARG B 719    12607  17158  13753   1383    560   1904       C  
-ATOM   3987  O   ARG B 719      21.201  12.910 -11.270  1.00111.50           O  
-ANISOU 3987  O   ARG B 719    12188  16973  13203   1496    577   1952       O  
-ATOM   3988  CB  ARG B 719      17.992  12.992 -12.071  1.00 88.38           C  
-ANISOU 3988  CB  ARG B 719     9442  13620  10519   1272    583   1971       C  
-ATOM   3989  CG  ARG B 719      16.921  11.993 -12.475  1.00 76.66           C  
-ANISOU 3989  CG  ARG B 719     8103  12073   8950   1288    606   1965       C  
-ATOM   3990  CD  ARG B 719      16.062  12.571 -13.587  1.00 79.23           C  
-ANISOU 3990  CD  ARG B 719     8396  12305   9402   1182    601   2069       C  
-ATOM   3991  NE  ARG B 719      15.391  13.792 -13.150  1.00 82.85           N  
-ANISOU 3991  NE  ARG B 719     8794  12585  10099   1053    569   2043       N  
-ATOM   3992  CZ  ARG B 719      14.957  14.747 -13.967  1.00 81.55           C  
-ANISOU 3992  CZ  ARG B 719     8549  12342  10093    961    554   2145       C  
-ATOM   3993  NH1 ARG B 719      15.128  14.633 -15.277  1.00 76.90           N  
-ANISOU 3993  NH1 ARG B 719     7926  11846   9447    974    568   2283       N  
-ATOM   3994  NH2 ARG B 719      14.358  15.821 -13.470  1.00 78.27           N  
-ANISOU 3994  NH2 ARG B 719     8086  11760   9893    863    527   2108       N  
-ATOM   3995  N   GLU B 720      20.029  14.644 -10.431  1.00 99.89           N  
-ANISOU 3995  N   GLU B 720    10652  15190  12112   1268    523   1884       N  
-ATOM   3996  CA  GLU B 720      21.161  15.565 -10.395  1.00108.70           C  
-ANISOU 3996  CA  GLU B 720    11603  16406  13290   1256    496   1923       C  
-ATOM   3997  C   GLU B 720      22.374  14.937  -9.715  1.00114.81           C  
-ANISOU 3997  C   GLU B 720    12363  17386  13874   1395    499   1862       C  
-ATOM   3998  O   GLU B 720      23.442  14.823 -10.315  1.00123.59           O  
-ANISOU 3998  O   GLU B 720    13394  18694  14871   1469    506   1941       O  
-ATOM   3999  CB  GLU B 720      20.774  16.868  -9.686  1.00120.72           C  
-ANISOU 3999  CB  GLU B 720    13045  17754  15067   1128    455   1867       C  
-ATOM   4000  CG  GLU B 720      21.895  17.900  -9.629  1.00130.23           C  
-ANISOU 4000  CG  GLU B 720    14072  19049  16360   1102    422   1904       C  
-ATOM   4001  CD  GLU B 720      21.468  19.208  -8.983  1.00140.10           C  
-ANISOU 4001  CD  GLU B 720    15244  20113  17876    977    383   1848       C  
-ATOM   4002  OE1 GLU B 720      20.284  19.337  -8.606  1.00144.19           O  
-ANISOU 4002  OE1 GLU B 720    15842  20435  18510    914    383   1781       O  
-ATOM   4003  OE2 GLU B 720      22.321  20.111  -8.852  1.00144.28           O  
-ANISOU 4003  OE2 GLU B 720    15625  20697  18496    946    352   1867       O  
-TER    4004      GLU B 720                                                      
-HETATM 4005  C10 032 A   1       9.454  -4.176 -21.735  1.00 58.37           C  
-ANISOU 4005  C10 032 A   1     7138   7748   7295    865    706    658       C  
-HETATM 4006  C15 032 A   1       1.934  -1.231 -18.357  1.00 37.50           C  
-ANISOU 4006  C15 032 A   1     4454   5094   4699    815    677    559       C  
-HETATM 4007  C17 032 A   1       1.516  -2.316 -20.597  1.00 34.06           C  
-ANISOU 4007  C17 032 A   1     4037   4645   4259    832    670    564       C  
-HETATM 4008  C20 032 A   1      -0.845  -3.053 -20.418  1.00 26.22           C  
-ANISOU 4008  C20 032 A   1     3040   3640   3283    825    667    533       C  
-HETATM 4009  C21 032 A   1      -2.207  -2.778 -20.374  1.00 27.30           C  
-ANISOU 4009  C21 032 A   1     3169   3768   3436    820    661    513       C  
-HETATM 4010  C22 032 A   1      -2.658  -1.461 -20.469  1.00 29.56           C  
-ANISOU 4010  C22 032 A   1     3444   4049   3738    818    650    505       C  
-HETATM 4011  C24 032 A   1      -0.387  -0.720 -20.649  1.00 34.82           C  
-ANISOU 4011  C24 032 A   1     4117   4729   4385    825    652    536       C  
-HETATM 4012  C01 032 A   1       6.130  -2.562 -19.577  1.00 50.16           C  
-ANISOU 4012  C01 032 A   1     6081   6709   6270    839    690    620       C  
-HETATM 4013  C02 032 A   1       6.309  -1.953 -18.333  1.00 46.22           C  
-ANISOU 4013  C02 032 A   1     5572   6217   5773    830    690    618       C  
-HETATM 4014  N03 032 A   1       5.354  -1.393 -17.558  1.00 44.65           N  
-ANISOU 4014  N03 032 A   1     5364   6020   5580    820    688    602       N  
-HETATM 4015  C04 032 A   1       4.825  -2.607 -20.089  1.00 44.14           C  
-ANISOU 4015  C04 032 A   1     5319   5939   5512    839    685    605       C  
-HETATM 4016  N14 032 A   1       2.999  -0.988 -17.535  1.00 34.94           N  
-ANISOU 4016  N14 032 A   1     4127   4781   4368    811    682    569       N  
-HETATM 4017  C16 032 A   1       2.365  -1.886 -19.491  1.00 37.77           C  
-ANISOU 4017  C16 032 A   1     4501   5125   4726    826    676    571       C  
-HETATM 4018  C05 032 A   1       3.781  -2.044 -19.335  1.00 42.71           C  
-ANISOU 4018  C05 032 A   1     5130   5758   5341    829    681    589       C  
-HETATM 4019  C06 032 A   1       4.133  -1.474 -18.114  1.00 40.72           C  
-ANISOU 4019  C06 032 A   1     4868   5514   5090    820    684    588       C  
-HETATM 4020  C07 032 A   1       7.269  -3.124 -20.317  1.00 54.29           C  
-ANISOU 4020  C07 032 A   1     6611   7232   6787    848    694    635       C  
-HETATM 4021  C18 032 A   1       0.073  -2.029 -20.549  1.00 35.44           C  
-ANISOU 4021  C18 032 A   1     4206   4813   4449    827    663    544       C  
-HETATM 4022  C23 032 A   1      -1.742  -0.420 -20.608  1.00 24.63           C  
-ANISOU 4022  C23 032 A   1     2818   3429   3112    821    646    517       C  
-HETATM 4023  F25 032 A   1       0.477   0.287 -20.782  1.00 32.98           F  
-ANISOU 4023  F25 032 A   1     3880   4499   4152    828    649    548       F  
-HETATM 4024  F26 032 A   1      -0.426  -4.317 -20.325  1.00 41.15           F  
-ANISOU 4024  F26 032 A   1     4939   5534   5164    827    676    541       F  
-HETATM 4025  N27 032 A   1      -3.116  -3.877 -20.230  1.00 36.57           N  
-ANISOU 4025  N27 032 A   1     4345   4937   4614    817    666    502       N  
-HETATM 4026  S28 032 A   1      -4.803  -3.571 -20.163  1.00 52.02           S  
-ANISOU 4026  S28 032 A   1     6290   6882   6594    811    660    476       S  
-HETATM 4027  O29 032 A   1      -5.510  -4.828 -20.031  1.00 58.84           O  
-ANISOU 4027  O29 032 A   1     7157   7741   7459    809    667    468       O  
-HETATM 4028  O30 032 A   1      -5.206  -2.598 -21.157  1.00 46.68           O  
-ANISOU 4028  O30 032 A   1     5610   6196   5928    818    642    472       O  
-HETATM 4029  C31 032 A   1      -4.997  -2.774 -18.571  1.00 50.34           C  
-ANISOU 4029  C31 032 A   1     6061   6676   6388    796    669    464       C  
-HETATM 4030  C32 032 A   1      -5.016  -3.720 -17.378  1.00 45.84           C  
-ANISOU 4030  C32 032 A   1     5493   6116   5810    784    686    463       C  
-HETATM 4031  C33 032 A   1      -4.277  -3.096 -16.205  1.00 36.76           C  
-ANISOU 4031  C33 032 A   1     4336   4981   4651    774    694    467       C  
-HETATM 4032  C08 032 A   1       7.146  -4.319 -21.047  1.00 58.69           C  
-ANISOU 4032  C08 032 A   1     7177   7784   7340    854    699    634       C  
-HETATM 4033  C09 032 A   1       8.232  -4.846 -21.751  1.00 62.06           C  
-ANISOU 4033  C09 032 A   1     7608   8210   7763    863    704    646       C  
-HETATM 4034  C11 032 A   1       9.603  -2.986 -21.024  1.00 48.54           C  
-ANISOU 4034  C11 032 A   1     5884   6507   6053    859    701    660       C  
-HETATM 4035  C12 032 A   1       8.514  -2.465 -20.323  1.00 48.21           C  
-ANISOU 4035  C12 032 A   1     5838   6466   6016    851    695    648       C  
-HETATM 4036 CL13 032 A   1      10.795  -4.820 -22.601  1.00 67.34          CL  
-ANISOU 4036 CL13 032 A   1     8277   8881   8427    874    716    670      CL  
-HETATM 4037  O19 032 A   1       1.942  -2.898 -21.592  1.00 44.03           O  
-ANISOU 4037  O19 032 A   1     5310   5906   5513    841    669    573       O  
-HETATM 4038  O   HOH A   2       0.360  16.940 -13.833  1.00 40.98           O  
-HETATM 4039  O   HOH A   3       2.005  15.274 -12.586  1.00 30.57           O  
-HETATM 4040  O   HOH A   4     -13.511 -22.832 -23.981  1.00 39.87           O  
-HETATM 4041  O   HOH A   6       0.867 -11.911  -3.812  1.00 44.63           O  
-HETATM 4042  O   HOH A   8      -5.183 -34.159 -22.465  1.00 38.38           O  
-HETATM 4043  O   HOH A   9       3.930  14.572 -24.093  1.00 40.22           O  
-HETATM 4044  O   HOH A  10       1.828  -2.294  -7.449  1.00 37.13           O  
-HETATM 4045  O   HOH A  11      -4.005  14.772 -11.681  1.00 32.36           O  
-HETATM 4046  O   HOH A  12       6.390 -29.427 -26.758  1.00 41.79           O  
-HETATM 4047  O   HOH A  14      -6.101  -2.762 -12.175  1.00 39.53           O  
-HETATM 4048  O   HOH A  16      -1.879  -3.895  -8.749  1.00 30.41           O  
-HETATM 4049  O   HOH A  18      -8.548  -2.696 -26.046  1.00 47.49           O  
-HETATM 4050  O   HOH A  20      -3.785  -9.253 -25.705  1.00 46.01           O  
-HETATM 4051  O   HOH A  21      16.340 -31.115 -12.651  1.00 41.06           O  
-HETATM 4052  O   HOH A  22      -5.509  11.875 -32.293  1.00 46.72           O  
-HETATM 4053  O   HOH A  24       5.197   6.147  -9.813  1.00 29.78           O  
-HETATM 4054  O   HOH A  27      -7.854 -34.790 -22.552  1.00 42.30           O  
-HETATM 4055  O   HOH A  30      -5.696 -16.885 -22.039  1.00 48.97           O  
-HETATM 4056  O   HOH A  31       7.673 -36.608 -19.395  1.00 50.79           O  
-HETATM 4057  O   HOH A  33       5.170  15.557 -14.306  1.00 47.62           O  
-HETATM 4058  O   HOH A  34       4.998 -31.492 -28.256  1.00 42.34           O  
-HETATM 4059  O   HOH A  35      15.920 -32.753 -24.273  1.00 40.77           O  
-HETATM 4060  O   HOH A  36       9.546 -24.321 -40.057  1.00 46.22           O  
-HETATM 4061  O   HOH A  37      -2.526  17.771 -25.929  1.00 54.56           O  
-HETATM 4062  O   HOH A  38      -9.772  -5.366 -25.824  1.00 45.12           O  
-HETATM 4063  O   HOH A  39       5.492  13.472 -12.162  1.00 42.35           O  
-HETATM 4064  O   HOH A  41     -14.092  -6.655  -4.439  1.00 53.07           O  
-HETATM 4065  O   HOH A  42     -12.352 -27.678 -10.451  1.00 49.39           O  
-HETATM 4066  O   HOH A  43      -4.036  13.051 -21.132  1.00 52.40           O  
-HETATM 4067  O   HOH A  44      -0.199  -4.656 -23.816  1.00 50.79           O  
-HETATM 4068  O   HOH A  45       5.160  -4.881  -5.594  1.00 47.83           O  
-HETATM 4069  O   HOH A  48      -0.633 -25.278 -27.127  1.00 39.34           O  
-HETATM 4070  O   HOH A  50     -11.830 -28.620 -25.249  1.00 52.78           O  
-HETATM 4071  O   HOH A  51      -7.910 -17.735 -23.546  1.00 45.58           O  
-HETATM 4072  O   HOH A  52     -10.338  -6.242  -5.139  1.00 50.32           O  
-HETATM 4073  O   HOH A  54      -0.578 -12.778 -35.991  1.00 50.01           O  
-HETATM 4074  O   HOH A  55      16.952 -16.829  -9.137  1.00 53.43           O  
-HETATM 4075  O   HOH A  60     -15.980   7.136 -10.552  1.00 47.31           O  
-HETATM 4076  O   HOH A  62      -2.852 -33.094 -23.100  1.00 48.62           O  
-HETATM 4077  O   HOH A  63       2.512   7.223 -10.680  1.00 46.70           O  
-HETATM 4078  O   HOH A  65      11.955 -25.800  -0.711  1.00 54.40           O  
-HETATM 4079  O   HOH B   1      14.536  18.696  16.878  1.00 23.21           O  
-HETATM 4080  O   HOH B   5      -0.877  14.664   7.294  1.00 44.41           O  
-HETATM 4081  O   HOH B   7      -5.962   2.219  -3.236  1.00 30.07           O  
-HETATM 4082  O   HOH B  13       6.789   4.962  -7.425  1.00 46.59           O  
-HETATM 4083  O   HOH B  15       1.834   4.767  -9.677  1.00 42.68           O  
-HETATM 4084  O   HOH B  17      -0.216  20.113  -2.800  1.00 45.19           O  
-HETATM 4085  O   HOH B  19       8.272  -6.177  -5.901  1.00 42.15           O  
-HETATM 4086  O   HOH B  23      22.940  -0.393  13.996  1.00 47.25           O  
-HETATM 4087  O   HOH B  25       0.950  28.083  10.877  1.00 49.80           O  
-HETATM 4088  O   HOH B  26      -1.376  -9.028  -1.082  1.00 36.26           O  
-HETATM 4089  O   HOH B  28      -4.064  24.988  -0.861  1.00 48.71           O  
-HETATM 4090  O   HOH B  29      -8.586  -1.448  19.578  1.00 44.20           O  
-HETATM 4091  O   HOH B  32      13.291  24.361  11.853  1.00 39.32           O  
-HETATM 4092  O   HOH B  40      -5.555 -16.168   6.791  1.00 33.45           O  
-HETATM 4093  O   HOH B  46       7.558  15.859 -11.119  1.00 42.89           O  
-HETATM 4094  O   HOH B  47       7.719  23.926  13.673  1.00 53.06           O  
-HETATM 4095  O   HOH B  49      -2.476  17.278   7.928  1.00 52.96           O  
-HETATM 4096  O   HOH B  53     -25.538   3.505   5.568  1.00 48.24           O  
-HETATM 4097  O   HOH B  56       5.525  17.424 -10.280  1.00 48.83           O  
-HETATM 4098  O   HOH B  57      -5.917   0.403   6.784  1.00 30.36           O  
-HETATM 4099  O   HOH B  58      -6.808   3.070   5.455  1.00 29.95           O  
-HETATM 4100  O   HOH B  59       6.684  19.126  14.868  1.00 50.57           O  
-HETATM 4101  O   HOH B  61      -3.939  -1.249   7.650  1.00 55.05           O  
-HETATM 4102  O   HOH B  64      -3.259   2.234  -4.675  1.00 50.29           O  
-CONECT 4005 4033 4034 4036                                                      
-CONECT 4006 4016 4017                                                           
-CONECT 4007 4017 4021 4037                                                      
-CONECT 4008 4009 4021 4024                                                      
-CONECT 4009 4008 4010 4025                                                      
-CONECT 4010 4009 4022                                                           
-CONECT 4011 4021 4022 4023                                                      
-CONECT 4012 4013 4015 4020                                                      
-CONECT 4013 4012 4014                                                           
-CONECT 4014 4013 4019                                                           
-CONECT 4015 4012 4018                                                           
-CONECT 4016 4006 4019                                                           
-CONECT 4017 4006 4007 4018                                                      
-CONECT 4018 4015 4017 4019                                                      
-CONECT 4019 4014 4016 4018                                                      
-CONECT 4020 4012 4032 4035                                                      
-CONECT 4021 4007 4008 4011                                                      
-CONECT 4022 4010 4011                                                           
-CONECT 4023 4011                                                                
-CONECT 4024 4008                                                                
-CONECT 4025 4009 4026                                                           
-CONECT 4026 4025 4027 4028 4029                                                 
-CONECT 4027 4026                                                                
-CONECT 4028 4026                                                                
-CONECT 4029 4026 4030                                                           
-CONECT 4030 4029 4031                                                           
-CONECT 4031 4030                                                                
-CONECT 4032 4020 4033                                                           
-CONECT 4033 4005 4032                                                           
-CONECT 4034 4005 4035                                                           
-CONECT 4035 4020 4034                                                           
-CONECT 4036 4005                                                                
-CONECT 4037 4007                                                                
-MASTER      381    0    1   21   15    0    4    6 4100    2   33   46          
-END                                                                             
diff --git a/plip/test/pdb/3pxf.pdb b/plip/test/pdb/3pxf.pdb
deleted file mode 100644
index 5ec1434..0000000
--- a/plip/test/pdb/3pxf.pdb
+++ /dev/null
@@ -1,3215 +0,0 @@
-HEADER    TRANSFERASE                             09-DEC-10   3PXF              
-TITLE     CDK2 IN COMPLEX WITH TWO MOLECULES OF 8-ANILINO-1-NAPHTHALENE         
-TITLE    2 SULFONATE                                                            
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 SYNONYM: CDK2, P33 PROTEIN KINASE;                                   
-COMPND   5 EC: 2.7.11.22;                                                       
-COMPND   6 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: CDK2;                                                          
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TUNER(DE3);                                
-SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1                                  
-KEYWDS    PROTEIN KINASE, ALLOSTERIC LIGAND, TRANSFERASE                        
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    S.BETZI,R.ALAM,E.SCHONBRUNN                                           
-REVDAT   2   01-JUN-11 3PXF    1       JRNL                                     
-REVDAT   1   16-FEB-11 3PXF    0                                                
-JRNL        AUTH   S.BETZI,R.ALAM,M.MARTIN,D.J.LUBBERS,H.HAN,S.R.JAKKARAJ,      
-JRNL        AUTH 2 G.I.GEORG,E.SCHONBRUNN                                       
-JRNL        TITL   DISCOVERY OF A POTENTIAL ALLOSTERIC LIGAND BINDING SITE IN   
-JRNL        TITL 2 CDK2.                                                        
-JRNL        REF    ACS CHEM.BIOL.                V.   6   492 2011              
-JRNL        REFN                   ISSN 1554-8929                               
-JRNL        PMID   21291269                                                     
-JRNL        DOI    10.1021/CB100410M                                            
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : CNS 1.2                                              
-REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
-REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
-REMARK   3               : READ,RICE,SIMONSON,WARREN                            
-REMARK   3                                                                      
-REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.50                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
-REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1409332.320                    
-REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
-REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.4                           
-REMARK   3   NUMBER OF REFLECTIONS             : 24998                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE            (WORKING SET) : 0.198                           
-REMARK   3   FREE R VALUE                     : 0.229                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1100                            
-REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.10                        
-REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3839                         
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
-REMARK   3   BIN FREE R VALUE                    : 0.2490                       
-REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.40                         
-REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 176                          
-REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 2431                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 62                                      
-REMARK   3   SOLVENT ATOMS            : 192                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 17.10                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.80                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -3.32000                                             
-REMARK   3    B22 (A**2) : 4.19000                                              
-REMARK   3    B33 (A**2) : -0.87000                                             
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED COORDINATE ERROR.                                         
-REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
-REMARK   3   ESD FROM SIGMAA              (A) : 0.10                            
-REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
-REMARK   3                                                                      
-REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
-REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
-REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.12                            
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
-REMARK   3   BOND LENGTHS                 (A) : 0.010                           
-REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
-REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.70                           
-REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84                            
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
-REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.310 ; 1.500                
-REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.180 ; 2.000                
-REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.750 ; 2.000                
-REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.640 ; 2.500                
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELING.                                              
-REMARK   3   METHOD USED : FLAT MODEL                                           
-REMARK   3   KSOL        : 0.40                                                 
-REMARK   3   BSOL        : 48.34                                                
-REMARK   3                                                                      
-REMARK   3  NCS MODEL : NONE                                                    
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
-REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
-REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
-REMARK   3                                                                      
-REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
-REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
-REMARK   3  PARAMETER FILE  3  : EDO.PAR                                        
-REMARK   3  PARAMETER FILE  4  : INH.PAR                                        
-REMARK   3  PARAMETER FILE  5  : NULL                                           
-REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
-REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
-REMARK   3  TOPOLOGY FILE  3   : EDO.TOP                                        
-REMARK   3  TOPOLOGY FILE  4   : INH.TOP                                        
-REMARK   3  TOPOLOGY FILE  5   : NULL                                           
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
-REMARK   4                                                                      
-REMARK   4 3PXF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-10.                  
-REMARK 100 THE RCSB ID CODE IS RCSB062930.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-10                          
-REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
-REMARK 200  PH                             : 7.5                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : N                                  
-REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
-REMARK 200  MONOCHROMATOR                  : MIRRORS                            
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD SATURN 944+                    
-REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
-REMARK 200  DATA SCALING SOFTWARE          : XDS                                
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24998                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
-REMARK 200  DATA REDUNDANCY                : 3.300                              
-REMARK 200  R MERGE                    (I) : 0.19900                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.0000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.03500                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: CNS 1.2                                               
-REMARK 200 STARTING MODEL: 1PW2                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 36.34                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MG/ML CDK2, 5 MM ANS, 15% (V/V)        
-REMARK 280  JEFFAMINE ED-2001, 50 MM HEPES, PH 7.5, VAPOR DIFFUSION, HANGING    
-REMARK 280  DROP, TEMPERATURE 291K                                              
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.50500            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.14500            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.72500            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.14500            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.50500            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.72500            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     GLY A    -7                                                      
-REMARK 465     PRO A    -6                                                      
-REMARK 465     LEU A    -5                                                      
-REMARK 465     GLY A    -4                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    VAL A   7      -60.50   -103.65                                   
-REMARK 500    GLU A  12       69.41   -159.66                                   
-REMARK 500    THR A  41      -77.83    -88.52                                   
-REMARK 500    GLU A  42      -26.63   -163.25                                   
-REMARK 500    GLU A  73       79.11     28.65                                   
-REMARK 500    ASN A  74       16.41     58.70                                   
-REMARK 500    LEU A  83      -36.57   -135.15                                   
-REMARK 500    HIS A  84      -21.12     46.44                                   
-REMARK 500    ARG A 126      -16.11     79.99                                   
-REMARK 500    ASP A 127       45.97   -140.42                                   
-REMARK 500    TYR A 159       60.59     60.10                                   
-REMARK 500    GLU A 162     -147.45    166.53                                   
-REMARK 500    VAL A 164       11.71   -179.55                                   
-REMARK 500    ARG A 297       75.47   -108.98                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
-REMARK 500                                                                      
-REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
-REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
-REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
-REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
-REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
-REMARK 500    HIS A  84        23.8      L          L   OUTSIDE RANGE           
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A 499        DISTANCE =  5.55 ANGSTROMS                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 299                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 300                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 301                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 302                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 303                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2AN A 304                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2AN A 305                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 3PXQ   RELATED DB: PDB                                   
-REMARK 900 CDK2/ANS/ANS/ANS COMPLEX                                             
-REMARK 900 RELATED ID: 3PXR   RELATED DB: PDB                                   
-REMARK 900 CDK2                                                                 
-REMARK 900 RELATED ID: 3PXY   RELATED DB: PDB                                   
-REMARK 900 CDK2/JWS648 COMPLEX                                                  
-REMARK 900 RELATED ID: 3PXZ   RELATED DB: PDB                                   
-REMARK 900 CDK2/JWS648/ANS/ANS COMPLEX                                          
-REMARK 900 RELATED ID: 3PY0   RELATED DB: PDB                                   
-REMARK 900 CDK2/SU9516 COMPLEX                                                  
-REMARK 900 RELATED ID: 3PY1   RELATED DB: PDB                                   
-REMARK 900 CDK2/SU9516/ANS/ANS COMPLEX                                          
-DBREF  3PXF A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
-SEQADV 3PXF GLY A   -7  UNP  P24941              EXPRESSION TAG                 
-SEQADV 3PXF PRO A   -6  UNP  P24941              EXPRESSION TAG                 
-SEQADV 3PXF LEU A   -5  UNP  P24941              EXPRESSION TAG                 
-SEQADV 3PXF GLY A   -4  UNP  P24941              EXPRESSION TAG                 
-SEQADV 3PXF SER A   -3  UNP  P24941              EXPRESSION TAG                 
-SEQADV 3PXF PRO A   -2  UNP  P24941              EXPRESSION TAG                 
-SEQADV 3PXF GLU A   -1  UNP  P24941              EXPRESSION TAG                 
-SEQADV 3PXF PHE A    0  UNP  P24941              EXPRESSION TAG                 
-SEQRES   1 A  306  GLY PRO LEU GLY SER PRO GLU PHE MET GLU ASN PHE GLN          
-SEQRES   2 A  306  LYS VAL GLU LYS ILE GLY GLU GLY THR TYR GLY VAL VAL          
-SEQRES   3 A  306  TYR LYS ALA ARG ASN LYS LEU THR GLY GLU VAL VAL ALA          
-SEQRES   4 A  306  LEU LYS LYS ILE ARG LEU ASP THR GLU THR GLU GLY VAL          
-SEQRES   5 A  306  PRO SER THR ALA ILE ARG GLU ILE SER LEU LEU LYS GLU          
-SEQRES   6 A  306  LEU ASN HIS PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE          
-SEQRES   7 A  306  HIS THR GLU ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU          
-SEQRES   8 A  306  HIS GLN ASP LEU LYS LYS PHE MET ASP ALA SER ALA LEU          
-SEQRES   9 A  306  THR GLY ILE PRO LEU PRO LEU ILE LYS SER TYR LEU PHE          
-SEQRES  10 A  306  GLN LEU LEU GLN GLY LEU ALA PHE CYS HIS SER HIS ARG          
-SEQRES  11 A  306  VAL LEU HIS ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE          
-SEQRES  12 A  306  ASN THR GLU GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU          
-SEQRES  13 A  306  ALA ARG ALA PHE GLY VAL PRO VAL ARG THR TYR THR HIS          
-SEQRES  14 A  306  GLU VAL VAL THR LEU TRP TYR ARG ALA PRO GLU ILE LEU          
-SEQRES  15 A  306  LEU GLY CYS LYS TYR TYR SER THR ALA VAL ASP ILE TRP          
-SEQRES  16 A  306  SER LEU GLY CYS ILE PHE ALA GLU MET VAL THR ARG ARG          
-SEQRES  17 A  306  ALA LEU PHE PRO GLY ASP SER GLU ILE ASP GLN LEU PHE          
-SEQRES  18 A  306  ARG ILE PHE ARG THR LEU GLY THR PRO ASP GLU VAL VAL          
-SEQRES  19 A  306  TRP PRO GLY VAL THR SER MET PRO ASP TYR LYS PRO SER          
-SEQRES  20 A  306  PHE PRO LYS TRP ALA ARG GLN ASP PHE SER LYS VAL VAL          
-SEQRES  21 A  306  PRO PRO LEU ASP GLU ASP GLY ARG SER LEU LEU SER GLN          
-SEQRES  22 A  306  MET LEU HIS TYR ASP PRO ASN LYS ARG ILE SER ALA LYS          
-SEQRES  23 A  306  ALA ALA LEU ALA HIS PRO PHE PHE GLN ASP VAL THR LYS          
-SEQRES  24 A  306  PRO VAL PRO HIS LEU ARG LEU                                  
-HET    EDO  A 299       4                                                       
-HET    EDO  A 300       4                                                       
-HET    EDO  A 301       4                                                       
-HET    EDO  A 302       4                                                       
-HET    EDO  A 303       4                                                       
-HET    2AN  A 304      21                                                       
-HET    2AN  A 305      21                                                       
-HETNAM     EDO 1,2-ETHANEDIOL                                                   
-HETNAM     2AN 8-ANILINO-1-NAPHTHALENE SULFONATE                                
-HETSYN     EDO ETHYLENE GLYCOL                                                  
-FORMUL   2  EDO    5(C2 H6 O2)                                                  
-FORMUL   7  2AN    2(C16 H13 N O3 S)                                            
-FORMUL   9  HOH   *192(H2 O)                                                    
-HELIX    1   1 PHE A    0  GLU A    2  5                                   3    
-HELIX    2   2 PRO A   45  LEU A   58  1                                  14    
-HELIX    3   3 LEU A   87  SER A   94  1                                   8    
-HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
-HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
-HELIX    6   6 GLY A  147  PHE A  152  1                                   6    
-HELIX    7   7 VAL A  164  ARG A  169  5                                   6    
-HELIX    8   8 ALA A  170  LEU A  175  1                                   6    
-HELIX    9   9 THR A  182  ARG A  199  1                                  18    
-HELIX   10  10 SER A  207  GLY A  220  1                                  14    
-HELIX   11  11 GLY A  229  MET A  233  5                                   5    
-HELIX   12  12 ASP A  247  VAL A  252  1                                   6    
-HELIX   13  13 ASP A  256  LEU A  267  1                                  12    
-HELIX   14  14 SER A  276  ALA A  282  1                                   7    
-HELIX   15  15 HIS A  283  GLN A  287  5                                   5    
-SHEET    1   A 5 PHE A   4  GLY A  11  0                                        
-SHEET    2   A 5 VAL A  18  ASN A  23 -1  O  LYS A  20   N  GLU A   8           
-SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  LEU A  32   N  TYR A  19           
-SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
-SHEET    5   A 5 LEU A  66  THR A  72 -1  N  ASP A  68   O  VAL A  79           
-SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
-SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
-SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
-SITE     1 AC1  5 LYS A  88  MET A  91  GLU A 195  ARG A 199                    
-SITE     2 AC1  5 HOH A 358                                                     
-SITE     1 AC2  5 GLU A  -1  PRO A  -2  ASP A  68  VAL A  69                    
-SITE     2 AC2  5 HOH A 351                                                     
-SITE     1 AC3  5 ASP A 210  PHE A 213  ARG A 217  TRP A 243                    
-SITE     2 AC3  5 HOH A 380                                                     
-SITE     1 AC4  4 MET A   1  GLU A   2  THR A  72  HOH A 503                    
-SITE     1 AC5  5 PRO A 253  PRO A 254  LEU A 255  ASP A 256                    
-SITE     2 AC5  5 ARG A 260                                                     
-SITE     1 AC6  7 LEU A  37  ILE A  52  LYS A  56  HIS A  71                    
-SITE     2 AC6  7 LEU A  76  LEU A  78  2AN A 305                               
-SITE     1 AC7 13 TYR A  15  LYS A  33  ILE A  35  LEU A  55                    
-SITE     2 AC7 13 LYS A  56  VAL A  64  LEU A  78  PHE A  80                    
-SITE     3 AC7 13 ALA A 144  ASP A 145  PHE A 146  2AN A 304                    
-SITE     4 AC7 13 HOH A 496                                                     
-CRYST1   53.010   69.450   72.290  90.00  90.00  90.00 P 21 21 21    4          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.018864  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.014399  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.013833        0.00000                         
-ATOM      1  N   SER A  -3     117.854 144.104  81.523  1.00 29.01           N  
-ATOM      2  CA  SER A  -3     118.435 142.910  82.214  1.00 30.05           C  
-ATOM      3  C   SER A  -3     118.348 141.664  81.328  1.00 27.62           C  
-ATOM      4  O   SER A  -3     117.296 141.376  80.746  1.00 27.75           O  
-ATOM      5  CB  SER A  -3     117.700 142.689  83.537  1.00 32.13           C  
-ATOM      6  OG  SER A  -3     116.294 142.803  83.347  1.00 38.03           O  
-ATOM      7  N   PRO A  -2     119.451 140.901  81.207  1.00 26.07           N  
-ATOM      8  CA  PRO A  -2     119.343 139.718  80.341  1.00 23.89           C  
-ATOM      9  C   PRO A  -2     118.278 138.710  80.740  1.00 22.64           C  
-ATOM     10  O   PRO A  -2     117.990 138.513  81.922  1.00 21.88           O  
-ATOM     11  CB  PRO A  -2     120.745 139.103  80.392  1.00 25.04           C  
-ATOM     12  CG  PRO A  -2     121.288 139.585  81.718  1.00 25.88           C  
-ATOM     13  CD  PRO A  -2     120.788 140.997  81.817  1.00 25.50           C  
-ATOM     14  N   GLU A  -1     117.685 138.079  79.736  1.00 21.26           N  
-ATOM     15  CA  GLU A  -1     116.702 137.054  79.994  1.00 21.91           C  
-ATOM     16  C   GLU A  -1     117.457 135.734  79.955  1.00 21.88           C  
-ATOM     17  O   GLU A  -1     118.458 135.592  79.232  1.00 22.67           O  
-ATOM     18  CB  GLU A  -1     115.608 137.065  78.929  1.00 21.16           C  
-ATOM     19  CG  GLU A  -1     114.874 138.369  78.887  1.00 24.15           C  
-ATOM     20  CD  GLU A  -1     113.658 138.284  78.030  1.00 24.40           C  
-ATOM     21  OE1 GLU A  -1     113.819 138.198  76.790  1.00 23.50           O  
-ATOM     22  OE2 GLU A  -1     112.548 138.290  78.606  1.00 26.44           O  
-ATOM     23  N   PHE A   0     116.987 134.785  80.754  1.00 22.83           N  
-ATOM     24  CA  PHE A   0     117.581 133.465  80.838  1.00 23.06           C  
-ATOM     25  C   PHE A   0     116.479 132.449  80.630  1.00 24.94           C  
-ATOM     26  O   PHE A   0     115.329 132.701  80.986  1.00 24.25           O  
-ATOM     27  CB  PHE A   0     118.229 133.257  82.211  1.00 22.54           C  
-ATOM     28  CG  PHE A   0     119.457 134.105  82.439  1.00 22.16           C  
-ATOM     29  CD1 PHE A   0     119.378 135.286  83.169  1.00 21.51           C  
-ATOM     30  CD2 PHE A   0     120.695 133.714  81.920  1.00 21.74           C  
-ATOM     31  CE1 PHE A   0     120.514 136.071  83.384  1.00 21.89           C  
-ATOM     32  CE2 PHE A   0     121.843 134.502  82.131  1.00 21.85           C  
-ATOM     33  CZ  PHE A   0     121.744 135.681  82.866  1.00 20.95           C  
-ATOM     34  N   MET A   1     116.825 131.300  80.058  1.00 25.89           N  
-ATOM     35  CA  MET A   1     115.832 130.268  79.804  1.00 26.77           C  
-ATOM     36  C   MET A   1     115.117 129.819  81.072  1.00 27.64           C  
-ATOM     37  O   MET A   1     113.971 129.357  81.020  1.00 27.31           O  
-ATOM     38  CB  MET A   1     116.486 129.082  79.103  1.00 27.85           C  
-ATOM     39  CG  MET A   1     116.939 129.411  77.703  1.00 28.67           C  
-ATOM     40  SD  MET A   1     115.705 130.408  76.827  1.00 32.30           S  
-ATOM     41  CE  MET A   1     114.367 129.197  76.674  1.00 29.00           C  
-ATOM     42  N   GLU A   2     115.787 129.968  82.212  1.00 27.99           N  
-ATOM     43  CA  GLU A   2     115.202 129.603  83.500  1.00 28.57           C  
-ATOM     44  C   GLU A   2     114.000 130.510  83.801  1.00 28.68           C  
-ATOM     45  O   GLU A   2     113.109 130.142  84.573  1.00 28.32           O  
-ATOM     46  CB  GLU A   2     116.237 129.760  84.620  1.00 30.66           C  
-ATOM     47  CG  GLU A   2     117.372 128.746  84.617  1.00 33.32           C  
-ATOM     48  CD  GLU A   2     118.155 128.688  83.312  1.00 35.83           C  
-ATOM     49  OE1 GLU A   2     118.451 129.749  82.711  1.00 34.67           O  
-ATOM     50  OE2 GLU A   2     118.499 127.561  82.898  1.00 37.77           O  
-ATOM     51  N   ASN A   3     114.003 131.700  83.198  1.00 26.77           N  
-ATOM     52  CA  ASN A   3     112.944 132.685  83.379  1.00 26.88           C  
-ATOM     53  C   ASN A   3     111.634 132.286  82.709  1.00 26.30           C  
-ATOM     54  O   ASN A   3     110.598 132.895  82.970  1.00 26.11           O  
-ATOM     55  CB  ASN A   3     113.346 134.024  82.770  1.00 26.98           C  
-ATOM     56  CG  ASN A   3     114.535 134.649  83.449  1.00 28.59           C  
-ATOM     57  OD1 ASN A   3     115.095 135.623  82.947  1.00 28.89           O  
-ATOM     58  ND2 ASN A   3     114.925 134.107  84.597  1.00 26.02           N  
-ATOM     59  N   PHE A   4     111.686 131.277  81.846  1.00 25.26           N  
-ATOM     60  CA  PHE A   4     110.506 130.867  81.105  1.00 26.93           C  
-ATOM     61  C   PHE A   4     109.964 129.508  81.473  1.00 28.14           C  
-ATOM     62  O   PHE A   4     110.711 128.549  81.656  1.00 27.93           O  
-ATOM     63  CB  PHE A   4     110.800 130.865  79.606  1.00 26.37           C  
-ATOM     64  CG  PHE A   4     111.127 132.214  79.047  1.00 26.06           C  
-ATOM     65  CD1 PHE A   4     110.111 133.111  78.711  1.00 26.75           C  
-ATOM     66  CD2 PHE A   4     112.452 132.597  78.862  1.00 25.45           C  
-ATOM     67  CE1 PHE A   4     110.409 134.372  78.199  1.00 25.07           C  
-ATOM     68  CE2 PHE A   4     112.765 133.856  78.351  1.00 25.91           C  
-ATOM     69  CZ  PHE A   4     111.736 134.748  78.018  1.00 26.16           C  
-ATOM     70  N   GLN A   5     108.643 129.440  81.551  1.00 29.68           N  
-ATOM     71  CA  GLN A   5     107.954 128.209  81.855  1.00 31.79           C  
-ATOM     72  C   GLN A   5     107.299 127.739  80.558  1.00 32.38           C  
-ATOM     73  O   GLN A   5     106.522 128.476  79.953  1.00 30.96           O  
-ATOM     74  CB  GLN A   5     106.886 128.470  82.920  1.00 33.22           C  
-ATOM     75  CG  GLN A   5     105.911 127.320  83.093  1.00 37.25           C  
-ATOM     76  CD  GLN A   5     106.599 126.050  83.529  1.00 39.11           C  
-ATOM     77  OE1 GLN A   5     107.168 125.985  84.622  1.00 41.62           O  
-ATOM     78  NE2 GLN A   5     106.560 125.030  82.675  1.00 40.88           N  
-ATOM     79  N   LYS A   6     107.631 126.531  80.115  1.00 33.28           N  
-ATOM     80  CA  LYS A   6     107.030 126.002  78.906  1.00 35.09           C  
-ATOM     81  C   LYS A   6     105.566 125.720  79.216  1.00 35.56           C  
-ATOM     82  O   LYS A   6     105.226 125.197  80.284  1.00 35.05           O  
-ATOM     83  CB  LYS A   6     107.713 124.704  78.481  1.00 37.64           C  
-ATOM     84  CG  LYS A   6     107.790 123.681  79.603  1.00 41.09           C  
-ATOM     85  CD  LYS A   6     108.264 122.321  79.114  1.00 43.64           C  
-ATOM     86  CE  LYS A   6     108.341 121.333  80.274  1.00 44.58           C  
-ATOM     87  NZ  LYS A   6     108.664 119.951  79.829  1.00 45.95           N  
-ATOM     88  N   VAL A   7     104.696 126.087  78.292  1.00 35.39           N  
-ATOM     89  CA  VAL A   7     103.278 125.845  78.483  1.00 36.01           C  
-ATOM     90  C   VAL A   7     102.879 124.660  77.626  1.00 36.41           C  
-ATOM     91  O   VAL A   7     102.435 123.630  78.134  1.00 36.22           O  
-ATOM     92  CB  VAL A   7     102.443 127.058  78.070  1.00 35.88           C  
-ATOM     93  CG1 VAL A   7     100.955 126.760  78.251  1.00 35.91           C  
-ATOM     94  CG2 VAL A   7     102.846 128.249  78.894  1.00 36.47           C  
-ATOM     95  N   GLU A   8     103.067 124.807  76.321  1.00 36.17           N  
-ATOM     96  CA  GLU A   8     102.708 123.758  75.382  1.00 37.69           C  
-ATOM     97  C   GLU A   8     103.432 123.960  74.060  1.00 37.65           C  
-ATOM     98  O   GLU A   8     103.944 125.040  73.781  1.00 37.20           O  
-ATOM     99  CB  GLU A   8     101.196 123.791  75.143  1.00 38.23           C  
-ATOM    100  CG  GLU A   8     100.700 125.172  74.732  1.00 39.78           C  
-ATOM    101  CD  GLU A   8      99.195 125.348  74.879  1.00 41.03           C  
-ATOM    102  OE1 GLU A   8      98.653 125.015  75.956  1.00 41.19           O  
-ATOM    103  OE2 GLU A   8      98.556 125.836  73.920  1.00 41.33           O  
-ATOM    104  N   LYS A   9     103.481 122.905  73.259  1.00 38.19           N  
-ATOM    105  CA  LYS A   9     104.091 122.963  71.942  1.00 38.62           C  
-ATOM    106  C   LYS A   9     103.024 123.605  71.056  1.00 39.09           C  
-ATOM    107  O   LYS A   9     101.867 123.199  71.104  1.00 38.07           O  
-ATOM    108  CB  LYS A   9     104.397 121.543  71.458  1.00 39.95           C  
-ATOM    109  CG  LYS A   9     104.817 121.464  70.011  1.00 40.95           C  
-ATOM    110  CD  LYS A   9     105.063 120.021  69.572  1.00 42.29           C  
-ATOM    111  CE  LYS A   9     105.510 119.976  68.114  1.00 43.19           C  
-ATOM    112  NZ  LYS A   9     104.524 120.637  67.207  1.00 44.12           N  
-ATOM    113  N   ILE A  10     103.389 124.615  70.268  1.00 39.75           N  
-ATOM    114  CA  ILE A  10     102.401 125.268  69.405  1.00 41.79           C  
-ATOM    115  C   ILE A  10     102.688 125.074  67.922  1.00 43.32           C  
-ATOM    116  O   ILE A  10     102.065 125.706  67.066  1.00 44.51           O  
-ATOM    117  CB  ILE A  10     102.296 126.784  69.704  1.00 41.14           C  
-ATOM    118  CG1 ILE A  10     103.667 127.446  69.563  1.00 40.65           C  
-ATOM    119  CG2 ILE A  10     101.731 127.000  71.099  1.00 40.88           C  
-ATOM    120  CD1 ILE A  10     103.692 128.910  69.981  1.00 40.03           C  
-ATOM    121  N   GLY A  11     103.630 124.190  67.620  1.00 44.58           N  
-ATOM    122  CA  GLY A  11     103.977 123.929  66.238  1.00 46.10           C  
-ATOM    123  C   GLY A  11     105.400 123.432  66.111  1.00 47.18           C  
-ATOM    124  O   GLY A  11     106.047 123.129  67.110  1.00 46.96           O  
-ATOM    125  N   GLU A  12     105.890 123.352  64.879  1.00 48.21           N  
-ATOM    126  CA  GLU A  12     107.248 122.889  64.634  1.00 48.97           C  
-ATOM    127  C   GLU A  12     107.756 123.336  63.270  1.00 48.38           C  
-ATOM    128  O   GLU A  12     107.946 122.523  62.373  1.00 49.46           O  
-ATOM    129  CB  GLU A  12     107.312 121.362  64.756  1.00 49.89           C  
-ATOM    130  CG  GLU A  12     106.284 120.617  63.921  1.00 51.56           C  
-ATOM    131  CD  GLU A  12     106.199 119.152  64.297  1.00 52.86           C  
-ATOM    132  OE1 GLU A  12     107.253 118.481  64.301  1.00 54.35           O  
-ATOM    133  OE2 GLU A  12     105.085 118.670  64.590  1.00 53.44           O  
-ATOM    134  N   GLY A  13     107.986 124.638  63.134  1.00 48.01           N  
-ATOM    135  CA  GLY A  13     108.466 125.195  61.883  1.00 47.06           C  
-ATOM    136  C   GLY A  13     109.701 124.522  61.314  1.00 46.61           C  
-ATOM    137  O   GLY A  13     110.056 123.404  61.701  1.00 45.86           O  
-ATOM    138  N   THR A  14     110.374 125.208  60.394  1.00 46.00           N  
-ATOM    139  CA  THR A  14     111.560 124.640  59.767  1.00 45.30           C  
-ATOM    140  C   THR A  14     112.741 124.555  60.729  1.00 44.61           C  
-ATOM    141  O   THR A  14     113.803 124.074  60.356  1.00 44.17           O  
-ATOM    142  CB  THR A  14     111.985 125.447  58.511  1.00 45.80           C  
-ATOM    143  OG1 THR A  14     112.753 126.588  58.899  1.00 46.96           O  
-ATOM    144  CG2 THR A  14     110.760 125.919  57.747  1.00 45.06           C  
-ATOM    145  N   TYR A  15     112.555 125.007  61.968  1.00 44.13           N  
-ATOM    146  CA  TYR A  15     113.637 124.960  62.958  1.00 43.65           C  
-ATOM    147  C   TYR A  15     113.270 124.164  64.192  1.00 44.16           C  
-ATOM    148  O   TYR A  15     113.610 124.552  65.311  1.00 44.60           O  
-ATOM    149  CB  TYR A  15     114.045 126.363  63.391  1.00 42.42           C  
-ATOM    150  CG  TYR A  15     114.511 127.221  62.247  1.00 41.54           C  
-ATOM    151  CD1 TYR A  15     115.686 126.923  61.562  1.00 40.81           C  
-ATOM    152  CD2 TYR A  15     113.754 128.315  61.823  1.00 41.59           C  
-ATOM    153  CE1 TYR A  15     116.096 127.693  60.476  1.00 40.38           C  
-ATOM    154  CE2 TYR A  15     114.151 129.089  60.746  1.00 40.74           C  
-ATOM    155  CZ  TYR A  15     115.321 128.775  60.075  1.00 39.88           C  
-ATOM    156  OH  TYR A  15     115.702 129.538  59.002  1.00 39.32           O  
-ATOM    157  N   GLY A  16     112.578 123.050  63.981  1.00 44.29           N  
-ATOM    158  CA  GLY A  16     112.183 122.205  65.091  1.00 43.76           C  
-ATOM    159  C   GLY A  16     110.847 122.606  65.676  1.00 43.01           C  
-ATOM    160  O   GLY A  16     109.986 123.143  64.977  1.00 43.14           O  
-ATOM    161  N   VAL A  17     110.683 122.359  66.971  1.00 41.68           N  
-ATOM    162  CA  VAL A  17     109.445 122.687  67.660  1.00 40.42           C  
-ATOM    163  C   VAL A  17     109.393 124.146  68.120  1.00 38.27           C  
-ATOM    164  O   VAL A  17     110.423 124.775  68.372  1.00 39.18           O  
-ATOM    165  CB  VAL A  17     109.267 121.784  68.893  1.00 41.53           C  
-ATOM    166  CG1 VAL A  17     110.342 122.105  69.917  1.00 42.11           C  
-ATOM    167  CG2 VAL A  17     107.890 121.976  69.490  1.00 42.36           C  
-ATOM    168  N   VAL A  18     108.184 124.692  68.193  1.00 35.38           N  
-ATOM    169  CA  VAL A  18     107.982 126.058  68.676  1.00 31.11           C  
-ATOM    170  C   VAL A  18     107.115 125.889  69.919  1.00 28.97           C  
-ATOM    171  O   VAL A  18     106.084 125.220  69.871  1.00 28.74           O  
-ATOM    172  CB  VAL A  18     107.225 126.947  67.661  1.00 30.76           C  
-ATOM    173  CG1 VAL A  18     107.007 128.343  68.262  1.00 28.42           C  
-ATOM    174  CG2 VAL A  18     108.022 127.050  66.365  1.00 30.89           C  
-ATOM    175  N   TYR A  19     107.530 126.493  71.030  1.00 27.90           N  
-ATOM    176  CA  TYR A  19     106.788 126.361  72.275  1.00 26.46           C  
-ATOM    177  C   TYR A  19     106.146 127.643  72.789  1.00 24.92           C  
-ATOM    178  O   TYR A  19     106.717 128.728  72.685  1.00 24.02           O  
-ATOM    179  CB  TYR A  19     107.711 125.829  73.379  1.00 29.43           C  
-ATOM    180  CG  TYR A  19     107.827 124.322  73.457  1.00 31.77           C  
-ATOM    181  CD1 TYR A  19     106.841 123.562  74.089  1.00 34.59           C  
-ATOM    182  CD2 TYR A  19     108.917 123.654  72.899  1.00 34.12           C  
-ATOM    183  CE1 TYR A  19     106.937 122.164  74.165  1.00 36.41           C  
-ATOM    184  CE2 TYR A  19     109.023 122.261  72.965  1.00 35.77           C  
-ATOM    185  CZ  TYR A  19     108.031 121.522  73.599  1.00 36.92           C  
-ATOM    186  OH  TYR A  19     108.123 120.143  73.664  1.00 38.34           O  
-ATOM    187  N   LYS A  20     104.938 127.513  73.325  1.00 22.06           N  
-ATOM    188  CA  LYS A  20     104.301 128.646  73.956  1.00 21.33           C  
-ATOM    189  C   LYS A  20     104.959 128.608  75.333  1.00 20.85           C  
-ATOM    190  O   LYS A  20     105.076 127.535  75.947  1.00 21.50           O  
-ATOM    191  CB  LYS A  20     102.787 128.426  74.093  1.00 21.26           C  
-ATOM    192  CG  LYS A  20     102.101 129.461  74.951  1.00 20.95           C  
-ATOM    193  CD  LYS A  20     100.579 129.265  75.032  1.00 22.77           C  
-ATOM    194  CE  LYS A  20      99.951 130.440  75.800  1.00 25.11           C  
-ATOM    195  NZ  LYS A  20      98.468 130.521  75.713  1.00 24.07           N  
-ATOM    196  N   ALA A  21     105.403 129.755  75.823  1.00 20.76           N  
-ATOM    197  CA  ALA A  21     106.031 129.810  77.129  1.00 21.17           C  
-ATOM    198  C   ALA A  21     105.557 131.036  77.886  1.00 22.08           C  
-ATOM    199  O   ALA A  21     105.039 131.983  77.287  1.00 22.46           O  
-ATOM    200  CB  ALA A  21     107.544 129.840  76.988  1.00 20.31           C  
-ATOM    201  N   ARG A  22     105.733 131.019  79.201  1.00 23.81           N  
-ATOM    202  CA  ARG A  22     105.327 132.148  80.027  1.00 26.89           C  
-ATOM    203  C   ARG A  22     106.550 132.718  80.730  1.00 27.33           C  
-ATOM    204  O   ARG A  22     107.314 131.980  81.344  1.00 26.38           O  
-ATOM    205  CB  ARG A  22     104.314 131.716  81.094  1.00 28.91           C  
-ATOM    206  CG  ARG A  22     103.239 130.759  80.618  1.00 33.16           C  
-ATOM    207  CD  ARG A  22     102.209 130.509  81.716  1.00 34.77           C  
-ATOM    208  NE  ARG A  22     101.482 131.732  82.052  1.00 37.97           N  
-ATOM    209  CZ  ARG A  22     100.506 132.247  81.313  1.00 37.20           C  
-ATOM    210  NH1 ARG A  22     100.129 131.647  80.194  1.00 39.25           N  
-ATOM    211  NH2 ARG A  22      99.914 133.366  81.692  1.00 39.45           N  
-ATOM    212  N   ASN A  23     106.743 134.026  80.612  1.00 29.13           N  
-ATOM    213  CA  ASN A  23     107.854 134.698  81.269  1.00 31.44           C  
-ATOM    214  C   ASN A  23     107.464 134.774  82.742  1.00 32.62           C  
-ATOM    215  O   ASN A  23     106.500 135.452  83.093  1.00 33.48           O  
-ATOM    216  CB  ASN A  23     108.023 136.109  80.694  1.00 30.89           C  
-ATOM    217  CG  ASN A  23     109.215 136.849  81.269  1.00 31.63           C  
-ATOM    218  OD1 ASN A  23     109.369 136.954  82.486  1.00 30.77           O  
-ATOM    219  ND2 ASN A  23     110.063 137.389  80.388  1.00 31.06           N  
-ATOM    220  N   LYS A  24     108.209 134.076  83.598  1.00 34.07           N  
-ATOM    221  CA  LYS A  24     107.927 134.051  85.036  1.00 34.47           C  
-ATOM    222  C   LYS A  24     108.027 135.399  85.750  1.00 35.38           C  
-ATOM    223  O   LYS A  24     107.420 135.584  86.807  1.00 34.53           O  
-ATOM    224  CB  LYS A  24     108.869 133.072  85.744  1.00 35.31           C  
-ATOM    225  CG  LYS A  24     108.710 131.632  85.330  1.00 35.03           C  
-ATOM    226  CD  LYS A  24     109.846 130.779  85.858  1.00 35.95           C  
-ATOM    227  CE  LYS A  24     109.798 129.351  85.306  1.00 35.38           C  
-ATOM    228  NZ  LYS A  24     111.012 128.594  85.777  1.00 38.24           N  
-ATOM    229  N   LEU A  25     108.791 136.327  85.177  1.00 36.49           N  
-ATOM    230  CA  LEU A  25     109.008 137.648  85.773  1.00 37.22           C  
-ATOM    231  C   LEU A  25     107.984 138.716  85.390  1.00 37.84           C  
-ATOM    232  O   LEU A  25     107.736 139.644  86.166  1.00 38.16           O  
-ATOM    233  CB  LEU A  25     110.407 138.170  85.413  1.00 37.65           C  
-ATOM    234  CG  LEU A  25     111.617 137.336  85.845  1.00 38.41           C  
-ATOM    235  CD1 LEU A  25     112.904 138.023  85.408  1.00 38.21           C  
-ATOM    236  CD2 LEU A  25     111.598 137.159  87.353  1.00 38.43           C  
-ATOM    237  N   THR A  26     107.410 138.599  84.196  1.00 37.78           N  
-ATOM    238  CA  THR A  26     106.426 139.574  83.728  1.00 37.96           C  
-ATOM    239  C   THR A  26     105.063 138.922  83.534  1.00 37.10           C  
-ATOM    240  O   THR A  26     104.038 139.597  83.550  1.00 38.15           O  
-ATOM    241  CB  THR A  26     106.853 140.224  82.382  1.00 38.62           C  
-ATOM    242  OG1 THR A  26     106.757 139.262  81.324  1.00 39.29           O  
-ATOM    243  CG2 THR A  26     108.287 140.731  82.459  1.00 38.05           C  
-ATOM    244  N   GLY A  27     105.057 137.607  83.360  1.00 35.79           N  
-ATOM    245  CA  GLY A  27     103.809 136.895  83.151  1.00 35.68           C  
-ATOM    246  C   GLY A  27     103.416 136.878  81.685  1.00 34.65           C  
-ATOM    247  O   GLY A  27     102.424 136.261  81.304  1.00 35.45           O  
-ATOM    248  N   GLU A  28     104.199 137.563  80.860  1.00 33.81           N  
-ATOM    249  CA  GLU A  28     103.927 137.626  79.432  1.00 33.59           C  
-ATOM    250  C   GLU A  28     104.125 136.256  78.786  1.00 32.65           C  
-ATOM    251  O   GLU A  28     105.060 135.517  79.132  1.00 32.18           O  
-ATOM    252  CB  GLU A  28     104.847 138.667  78.765  1.00 34.79           C  
-ATOM    253  CG  GLU A  28     104.819 138.637  77.227  1.00 37.84           C  
-ATOM    254  CD  GLU A  28     105.607 139.765  76.566  1.00 39.49           C  
-ATOM    255  OE1 GLU A  28     106.685 140.141  77.076  1.00 39.99           O  
-ATOM    256  OE2 GLU A  28     105.154 140.263  75.510  1.00 41.14           O  
-ATOM    257  N   VAL A  29     103.218 135.895  77.880  1.00 30.34           N  
-ATOM    258  CA  VAL A  29     103.360 134.636  77.175  1.00 27.72           C  
-ATOM    259  C   VAL A  29     104.036 135.010  75.865  1.00 26.39           C  
-ATOM    260  O   VAL A  29     103.778 136.079  75.301  1.00 25.22           O  
-ATOM    261  CB  VAL A  29     101.999 133.935  76.912  1.00 29.29           C  
-ATOM    262  CG1 VAL A  29     101.151 134.736  75.952  1.00 29.37           C  
-ATOM    263  CG2 VAL A  29     102.253 132.563  76.362  1.00 30.20           C  
-ATOM    264  N   VAL A  30     104.933 134.141  75.419  1.00 22.48           N  
-ATOM    265  CA  VAL A  30     105.705 134.339  74.206  1.00 22.16           C  
-ATOM    266  C   VAL A  30     105.763 133.029  73.447  1.00 20.74           C  
-ATOM    267  O   VAL A  30     105.281 132.006  73.923  1.00 22.15           O  
-ATOM    268  CB  VAL A  30     107.172 134.741  74.532  1.00 21.97           C  
-ATOM    269  CG1 VAL A  30     107.207 136.077  75.258  1.00 22.40           C  
-ATOM    270  CG2 VAL A  30     107.818 133.663  75.414  1.00 21.14           C  
-ATOM    271  N   ALA A  31     106.346 133.082  72.255  1.00 20.83           N  
-ATOM    272  CA  ALA A  31     106.550 131.902  71.444  1.00 18.53           C  
-ATOM    273  C   ALA A  31     108.073 131.768  71.406  1.00 20.08           C  
-ATOM    274  O   ALA A  31     108.761 132.732  71.064  1.00 18.60           O  
-ATOM    275  CB  ALA A  31     106.016 132.110  70.039  1.00 20.40           C  
-ATOM    276  N   LEU A  32     108.588 130.601  71.791  1.00 18.56           N  
-ATOM    277  CA  LEU A  32     110.033 130.359  71.782  1.00 21.02           C  
-ATOM    278  C   LEU A  32     110.429 129.355  70.738  1.00 22.03           C  
-ATOM    279  O   LEU A  32     109.833 128.280  70.622  1.00 23.74           O  
-ATOM    280  CB  LEU A  32     110.531 129.842  73.134  1.00 21.67           C  
-ATOM    281  CG  LEU A  32     110.393 130.697  74.385  1.00 22.93           C  
-ATOM    282  CD1 LEU A  32     110.883 129.876  75.583  1.00 22.28           C  
-ATOM    283  CD2 LEU A  32     111.221 131.963  74.254  1.00 24.14           C  
-ATOM    284  N   LYS A  33     111.463 129.703  69.988  1.00 22.78           N  
-ATOM    285  CA  LYS A  33     111.981 128.839  68.943  1.00 24.26           C  
-ATOM    286  C   LYS A  33     113.413 128.457  69.332  1.00 25.37           C  
-ATOM    287  O   LYS A  33     114.248 129.324  69.599  1.00 25.12           O  
-ATOM    288  CB  LYS A  33     111.939 129.591  67.606  1.00 24.13           C  
-ATOM    289  CG  LYS A  33     112.386 128.798  66.403  1.00 26.43           C  
-ATOM    290  CD  LYS A  33     112.081 129.564  65.117  1.00 26.19           C  
-ATOM    291  CE  LYS A  33     110.587 129.797  64.946  1.00 27.30           C  
-ATOM    292  NZ  LYS A  33     110.297 130.385  63.596  1.00 28.80           N  
-ATOM    293  N   LYS A  34     113.689 127.157  69.381  1.00 27.06           N  
-ATOM    294  CA  LYS A  34     115.010 126.675  69.757  1.00 29.30           C  
-ATOM    295  C   LYS A  34     115.861 126.394  68.524  1.00 31.15           C  
-ATOM    296  O   LYS A  34     115.459 125.673  67.614  1.00 31.02           O  
-ATOM    297  CB  LYS A  34     114.879 125.415  70.623  1.00 30.81           C  
-ATOM    298  CG  LYS A  34     116.181 124.937  71.250  1.00 32.65           C  
-ATOM    299  CD  LYS A  34     115.920 123.869  72.307  1.00 35.73           C  
-ATOM    300  CE  LYS A  34     115.296 122.629  71.691  1.00 36.73           C  
-ATOM    301  NZ  LYS A  34     116.229 121.992  70.728  1.00 38.98           N  
-ATOM    302  N   ILE A  35     117.049 126.976  68.500  1.00 33.03           N  
-ATOM    303  CA  ILE A  35     117.947 126.795  67.376  1.00 35.00           C  
-ATOM    304  C   ILE A  35     119.255 126.157  67.823  1.00 37.34           C  
-ATOM    305  O   ILE A  35     119.977 126.709  68.655  1.00 35.94           O  
-ATOM    306  CB  ILE A  35     118.232 128.153  66.710  1.00 34.67           C  
-ATOM    307  CG1 ILE A  35     116.925 128.734  66.175  1.00 35.12           C  
-ATOM    308  CG2 ILE A  35     119.260 128.001  65.602  1.00 34.35           C  
-ATOM    309  CD1 ILE A  35     116.978 130.212  65.975  1.00 36.87           C  
-ATOM    310  N   ARG A  36     119.551 124.984  67.271  1.00 41.02           N  
-ATOM    311  CA  ARG A  36     120.784 124.285  67.596  1.00 44.71           C  
-ATOM    312  C   ARG A  36     121.840 124.744  66.601  1.00 46.86           C  
-ATOM    313  O   ARG A  36     121.703 124.539  65.398  1.00 46.63           O  
-ATOM    314  CB  ARG A  36     120.591 122.766  67.503  1.00 46.42           C  
-ATOM    315  CG  ARG A  36     119.492 122.214  68.412  1.00 48.54           C  
-ATOM    316  CD  ARG A  36     119.799 120.785  68.854  1.00 50.25           C  
-ATOM    317  NE  ARG A  36     121.003 120.727  69.684  1.00 51.84           N  
-ATOM    318  CZ  ARG A  36     121.459 119.629  70.282  1.00 51.75           C  
-ATOM    319  NH1 ARG A  36     120.814 118.477  70.148  1.00 52.07           N  
-ATOM    320  NH2 ARG A  36     122.559 119.688  71.024  1.00 51.84           N  
-ATOM    321  N   LEU A  37     122.887 125.377  67.113  1.00 49.88           N  
-ATOM    322  CA  LEU A  37     123.965 125.898  66.283  1.00 53.84           C  
-ATOM    323  C   LEU A  37     124.900 124.802  65.783  1.00 56.51           C  
-ATOM    324  O   LEU A  37     124.727 123.630  66.115  1.00 56.75           O  
-ATOM    325  CB  LEU A  37     124.769 126.936  67.068  1.00 53.61           C  
-ATOM    326  CG  LEU A  37     124.059 128.220  67.506  1.00 53.58           C  
-ATOM    327  CD1 LEU A  37     122.820 127.904  68.322  1.00 54.21           C  
-ATOM    328  CD2 LEU A  37     125.024 129.048  68.328  1.00 53.91           C  
-ATOM    329  N   ASP A  38     125.896 125.199  64.992  1.00 59.97           N  
-ATOM    330  CA  ASP A  38     126.864 124.255  64.436  1.00 63.27           C  
-ATOM    331  C   ASP A  38     128.270 124.818  64.258  1.00 65.41           C  
-ATOM    332  O   ASP A  38     128.556 125.492  63.266  1.00 65.94           O  
-ATOM    333  CB  ASP A  38     126.383 123.736  63.081  1.00 63.36           C  
-ATOM    334  CG  ASP A  38     125.177 122.836  63.198  1.00 63.97           C  
-ATOM    335  OD1 ASP A  38     125.292 121.773  63.841  1.00 64.02           O  
-ATOM    336  OD2 ASP A  38     124.116 123.192  62.644  1.00 64.43           O  
-ATOM    337  N   THR A  39     129.145 124.536  65.218  1.00 67.80           N  
-ATOM    338  CA  THR A  39     130.531 124.979  65.127  1.00 70.08           C  
-ATOM    339  C   THR A  39     131.273 123.844  64.413  1.00 71.49           C  
-ATOM    340  O   THR A  39     132.473 123.629  64.608  1.00 71.83           O  
-ATOM    341  CB  THR A  39     131.150 125.225  66.526  1.00 70.38           C  
-ATOM    342  OG1 THR A  39     132.472 125.754  66.374  1.00 70.77           O  
-ATOM    343  CG2 THR A  39     131.215 123.927  67.331  1.00 70.59           C  
-ATOM    344  N   GLU A  40     130.517 123.121  63.589  1.00 72.81           N  
-ATOM    345  CA  GLU A  40     131.010 121.992  62.804  1.00 73.98           C  
-ATOM    346  C   GLU A  40     132.219 122.393  61.965  1.00 74.31           C  
-ATOM    347  O   GLU A  40     133.255 121.726  61.987  1.00 74.43           O  
-ATOM    348  CB  GLU A  40     129.893 121.489  61.884  1.00 74.62           C  
-ATOM    349  CG  GLU A  40     129.349 122.568  60.946  1.00 75.52           C  
-ATOM    350  CD  GLU A  40     128.109 122.132  60.187  1.00 76.30           C  
-ATOM    351  OE1 GLU A  40     128.157 121.079  59.515  1.00 76.58           O  
-ATOM    352  OE2 GLU A  40     127.086 122.849  60.258  1.00 76.64           O  
-ATOM    353  N   THR A  41     132.067 123.481  61.215  1.00 74.42           N  
-ATOM    354  CA  THR A  41     133.136 123.997  60.367  1.00 74.45           C  
-ATOM    355  C   THR A  41     133.989 124.960  61.181  1.00 73.93           C  
-ATOM    356  O   THR A  41     135.079 124.610  61.639  1.00 74.13           O  
-ATOM    357  CB  THR A  41     132.570 124.752  59.133  1.00 74.92           C  
-ATOM    358  OG1 THR A  41     131.609 125.728  59.562  1.00 75.12           O  
-ATOM    359  CG2 THR A  41     131.910 123.778  58.161  1.00 75.22           C  
-ATOM    360  N   GLU A  42     133.479 126.173  61.364  1.00 73.12           N  
-ATOM    361  CA  GLU A  42     134.182 127.192  62.127  1.00 71.93           C  
-ATOM    362  C   GLU A  42     133.201 128.297  62.513  1.00 70.54           C  
-ATOM    363  O   GLU A  42     133.384 128.985  63.520  1.00 70.64           O  
-ATOM    364  CB  GLU A  42     135.328 127.771  61.293  1.00 72.82           C  
-ATOM    365  CG  GLU A  42     136.379 128.496  62.115  1.00 73.89           C  
-ATOM    366  CD  GLU A  42     137.053 127.583  63.127  1.00 74.43           C  
-ATOM    367  OE1 GLU A  42     137.771 126.647  62.704  1.00 74.32           O  
-ATOM    368  OE2 GLU A  42     136.857 127.798  64.344  1.00 74.83           O  
-ATOM    369  N   GLY A  43     132.154 128.456  61.706  1.00 68.53           N  
-ATOM    370  CA  GLY A  43     131.159 129.473  61.984  1.00 65.63           C  
-ATOM    371  C   GLY A  43     130.074 129.577  60.930  1.00 63.59           C  
-ATOM    372  O   GLY A  43     129.910 128.687  60.091  1.00 63.39           O  
-ATOM    373  N   VAL A  44     129.322 130.671  60.982  1.00 61.41           N  
-ATOM    374  CA  VAL A  44     128.244 130.914  60.032  1.00 58.79           C  
-ATOM    375  C   VAL A  44     128.800 131.742  58.882  1.00 56.76           C  
-ATOM    376  O   VAL A  44     129.600 132.652  59.098  1.00 56.43           O  
-ATOM    377  CB  VAL A  44     127.082 131.701  60.686  1.00 59.09           C  
-ATOM    378  CG1 VAL A  44     125.940 131.870  59.695  1.00 58.67           C  
-ATOM    379  CG2 VAL A  44     126.606 130.985  61.942  1.00 58.91           C  
-ATOM    380  N   PRO A  45     128.392 131.430  57.642  1.00 54.98           N  
-ATOM    381  CA  PRO A  45     128.888 132.193  56.489  1.00 53.23           C  
-ATOM    382  C   PRO A  45     128.611 133.689  56.632  1.00 51.21           C  
-ATOM    383  O   PRO A  45     127.495 134.100  56.958  1.00 50.62           O  
-ATOM    384  CB  PRO A  45     128.157 131.555  55.303  1.00 53.86           C  
-ATOM    385  CG  PRO A  45     126.941 130.911  55.927  1.00 54.73           C  
-ATOM    386  CD  PRO A  45     127.473 130.361  57.216  1.00 54.57           C  
-ATOM    387  N   SER A  46     129.644 134.493  56.395  1.00 48.95           N  
-ATOM    388  CA  SER A  46     129.542 135.941  56.514  1.00 46.64           C  
-ATOM    389  C   SER A  46     128.308 136.487  55.806  1.00 44.84           C  
-ATOM    390  O   SER A  46     127.607 137.341  56.349  1.00 44.60           O  
-ATOM    391  CB  SER A  46     130.802 136.611  55.957  1.00 46.69           C  
-ATOM    392  OG  SER A  46     130.924 136.377  54.566  1.00 46.73           O  
-ATOM    393  N   THR A  47     128.029 136.003  54.600  1.00 42.50           N  
-ATOM    394  CA  THR A  47     126.851 136.488  53.888  1.00 40.07           C  
-ATOM    395  C   THR A  47     125.592 136.134  54.676  1.00 38.07           C  
-ATOM    396  O   THR A  47     124.617 136.893  54.677  1.00 36.94           O  
-ATOM    397  CB  THR A  47     126.728 135.874  52.492  1.00 40.62           C  
-ATOM    398  OG1 THR A  47     125.609 136.463  51.817  1.00 40.35           O  
-ATOM    399  CG2 THR A  47     126.529 134.363  52.589  1.00 40.16           C  
-ATOM    400  N   ALA A  48     125.624 134.976  55.335  1.00 35.61           N  
-ATOM    401  CA  ALA A  48     124.496 134.502  56.144  1.00 33.46           C  
-ATOM    402  C   ALA A  48     124.303 135.424  57.337  1.00 32.42           C  
-ATOM    403  O   ALA A  48     123.176 135.807  57.676  1.00 30.55           O  
-ATOM    404  CB  ALA A  48     124.756 133.086  56.637  1.00 33.86           C  
-ATOM    405  N   ILE A  49     125.411 135.767  57.984  1.00 30.04           N  
-ATOM    406  CA  ILE A  49     125.349 136.650  59.133  1.00 29.60           C  
-ATOM    407  C   ILE A  49     124.742 137.983  58.737  1.00 27.75           C  
-ATOM    408  O   ILE A  49     123.998 138.585  59.511  1.00 27.58           O  
-ATOM    409  CB  ILE A  49     126.743 136.892  59.727  1.00 31.06           C  
-ATOM    410  CG1 ILE A  49     127.232 135.607  60.390  1.00 32.52           C  
-ATOM    411  CG2 ILE A  49     126.692 138.023  60.747  1.00 31.04           C  
-ATOM    412  CD1 ILE A  49     126.239 135.011  61.394  1.00 33.87           C  
-ATOM    413  N   ARG A  50     125.050 138.428  57.525  1.00 26.16           N  
-ATOM    414  CA  ARG A  50     124.533 139.698  57.029  1.00 26.16           C  
-ATOM    415  C   ARG A  50     123.034 139.589  56.782  1.00 23.37           C  
-ATOM    416  O   ARG A  50     122.293 140.498  57.112  1.00 23.05           O  
-ATOM    417  CB  ARG A  50     125.267 140.105  55.739  1.00 28.04           C  
-ATOM    418  CG  ARG A  50     124.751 141.381  55.059  1.00 33.11           C  
-ATOM    419  CD  ARG A  50     125.745 141.881  54.001  1.00 37.13           C  
-ATOM    420  NE  ARG A  50     125.166 142.817  53.028  1.00 40.54           N  
-ATOM    421  CZ  ARG A  50     125.886 143.547  52.169  1.00 42.08           C  
-ATOM    422  NH1 ARG A  50     127.214 143.456  52.164  1.00 41.91           N  
-ATOM    423  NH2 ARG A  50     125.284 144.361  51.303  1.00 42.57           N  
-ATOM    424  N   GLU A  51     122.589 138.467  56.224  1.00 21.57           N  
-ATOM    425  CA  GLU A  51     121.169 138.280  55.947  1.00 20.68           C  
-ATOM    426  C   GLU A  51     120.356 138.160  57.231  1.00 18.78           C  
-ATOM    427  O   GLU A  51     119.216 138.608  57.284  1.00 18.16           O  
-ATOM    428  CB  GLU A  51     120.939 137.039  55.094  1.00 22.14           C  
-ATOM    429  CG  GLU A  51     121.417 137.159  53.649  1.00 24.90           C  
-ATOM    430  CD  GLU A  51     120.582 138.130  52.819  1.00 25.51           C  
-ATOM    431  OE1 GLU A  51     119.337 138.131  52.961  1.00 28.21           O  
-ATOM    432  OE2 GLU A  51     121.162 138.875  51.998  1.00 24.95           O  
-ATOM    433  N   ILE A  52     120.929 137.540  58.257  1.00 16.71           N  
-ATOM    434  CA  ILE A  52     120.222 137.416  59.534  1.00 16.73           C  
-ATOM    435  C   ILE A  52     120.123 138.831  60.113  1.00 16.46           C  
-ATOM    436  O   ILE A  52     119.112 139.216  60.697  1.00 14.96           O  
-ATOM    437  CB  ILE A  52     120.995 136.519  60.531  1.00 18.25           C  
-ATOM    438  CG1 ILE A  52     120.978 135.064  60.047  1.00 20.18           C  
-ATOM    439  CG2 ILE A  52     120.388 136.639  61.932  1.00 19.20           C  
-ATOM    440  CD1 ILE A  52     122.037 134.206  60.721  1.00 23.56           C  
-ATOM    441  N   SER A  53     121.190 139.602  59.942  1.00 16.50           N  
-ATOM    442  CA  SER A  53     121.204 140.965  60.441  1.00 17.12           C  
-ATOM    443  C   SER A  53     120.136 141.773  59.737  1.00 16.73           C  
-ATOM    444  O   SER A  53     119.437 142.564  60.373  1.00 16.31           O  
-ATOM    445  CB  SER A  53     122.576 141.605  60.230  1.00 18.35           C  
-ATOM    446  OG  SER A  53     123.518 141.010  61.100  1.00 20.48           O  
-ATOM    447  N   LEU A  54     120.009 141.572  58.430  1.00 16.05           N  
-ATOM    448  CA  LEU A  54     118.993 142.289  57.671  1.00 17.56           C  
-ATOM    449  C   LEU A  54     117.600 141.962  58.189  1.00 17.03           C  
-ATOM    450  O   LEU A  54     116.779 142.853  58.348  1.00 18.55           O  
-ATOM    451  CB  LEU A  54     119.069 141.937  56.181  1.00 19.16           C  
-ATOM    452  CG  LEU A  54     120.180 142.582  55.346  1.00 21.53           C  
-ATOM    453  CD1 LEU A  54     120.027 142.177  53.873  1.00 21.28           C  
-ATOM    454  CD2 LEU A  54     120.108 144.093  55.485  1.00 22.11           C  
-ATOM    455  N   LEU A  55     117.326 140.682  58.434  1.00 17.04           N  
-ATOM    456  CA  LEU A  55     116.006 140.286  58.929  1.00 17.63           C  
-ATOM    457  C   LEU A  55     115.738 140.905  60.303  1.00 17.42           C  
-ATOM    458  O   LEU A  55     114.655 141.437  60.561  1.00 17.22           O  
-ATOM    459  CB  LEU A  55     115.905 138.757  59.009  1.00 17.85           C  
-ATOM    460  CG  LEU A  55     114.510 138.180  59.300  1.00 19.31           C  
-ATOM    461  CD1 LEU A  55     113.458 138.833  58.405  1.00 19.39           C  
-ATOM    462  CD2 LEU A  55     114.544 136.663  59.062  1.00 20.27           C  
-ATOM    463  N   LYS A  56     116.731 140.850  61.186  1.00 16.36           N  
-ATOM    464  CA  LYS A  56     116.575 141.421  62.522  1.00 18.89           C  
-ATOM    465  C   LYS A  56     116.232 142.914  62.534  1.00 19.26           C  
-ATOM    466  O   LYS A  56     115.561 143.399  63.456  1.00 21.18           O  
-ATOM    467  CB  LYS A  56     117.859 141.201  63.335  1.00 19.71           C  
-ATOM    468  CG  LYS A  56     118.088 139.766  63.754  1.00 21.72           C  
-ATOM    469  CD  LYS A  56     119.428 139.593  64.462  1.00 24.19           C  
-ATOM    470  CE  LYS A  56     119.500 140.404  65.733  1.00 25.93           C  
-ATOM    471  NZ  LYS A  56     120.830 140.234  66.384  1.00 28.33           N  
-ATOM    472  N   GLU A  57     116.688 143.635  61.516  1.00 20.87           N  
-ATOM    473  CA  GLU A  57     116.467 145.087  61.405  1.00 22.57           C  
-ATOM    474  C   GLU A  57     115.020 145.457  61.120  1.00 21.99           C  
-ATOM    475  O   GLU A  57     114.578 146.564  61.436  1.00 21.26           O  
-ATOM    476  CB  GLU A  57     117.320 145.678  60.270  1.00 25.69           C  
-ATOM    477  CG  GLU A  57     118.818 145.767  60.520  1.00 28.94           C  
-ATOM    478  CD  GLU A  57     119.592 146.254  59.291  1.00 31.17           C  
-ATOM    479  OE1 GLU A  57     118.968 146.807  58.358  1.00 30.82           O  
-ATOM    480  OE2 GLU A  57     120.835 146.098  59.263  1.00 33.14           O  
-ATOM    481  N   LEU A  58     114.285 144.534  60.509  1.00 20.35           N  
-ATOM    482  CA  LEU A  58     112.903 144.811  60.134  1.00 20.48           C  
-ATOM    483  C   LEU A  58     111.913 144.894  61.286  1.00 19.67           C  
-ATOM    484  O   LEU A  58     111.840 144.010  62.136  1.00 20.91           O  
-ATOM    485  CB  LEU A  58     112.416 143.766  59.124  1.00 20.02           C  
-ATOM    486  CG  LEU A  58     113.279 143.619  57.864  1.00 20.02           C  
-ATOM    487  CD1 LEU A  58     112.633 142.568  56.955  1.00 21.05           C  
-ATOM    488  CD2 LEU A  58     113.434 144.959  57.140  1.00 21.48           C  
-ATOM    489  N   ASN A  59     111.157 145.985  61.296  1.00 17.95           N  
-ATOM    490  CA  ASN A  59     110.129 146.216  62.292  1.00 18.18           C  
-ATOM    491  C   ASN A  59     108.895 146.580  61.476  1.00 15.84           C  
-ATOM    492  O   ASN A  59     108.858 147.642  60.872  1.00 14.86           O  
-ATOM    493  CB  ASN A  59     110.516 147.393  63.194  1.00 20.01           C  
-ATOM    494  CG  ASN A  59     111.844 147.172  63.883  1.00 24.83           C  
-ATOM    495  OD1 ASN A  59     112.064 146.115  64.481  1.00 25.82           O  
-ATOM    496  ND2 ASN A  59     112.738 148.168  63.808  1.00 25.29           N  
-ATOM    497  N   HIS A  60     107.885 145.719  61.475  1.00 14.55           N  
-ATOM    498  CA  HIS A  60     106.695 145.984  60.671  1.00 13.10           C  
-ATOM    499  C   HIS A  60     105.508 145.256  61.250  1.00 13.85           C  
-ATOM    500  O   HIS A  60     105.651 144.156  61.771  1.00 13.03           O  
-ATOM    501  CB  HIS A  60     106.967 145.507  59.232  1.00 14.28           C  
-ATOM    502  CG  HIS A  60     105.915 145.909  58.239  1.00 13.01           C  
-ATOM    503  ND1 HIS A  60     104.734 145.219  58.080  1.00 13.20           N  
-ATOM    504  CD2 HIS A  60     105.859 146.951  57.375  1.00 14.73           C  
-ATOM    505  CE1 HIS A  60     103.990 145.825  57.172  1.00 11.98           C  
-ATOM    506  NE2 HIS A  60     104.650 146.882  56.728  1.00 13.45           N  
-ATOM    507  N   PRO A  61     104.297 145.837  61.133  1.00 13.52           N  
-ATOM    508  CA  PRO A  61     103.134 145.151  61.692  1.00 12.54           C  
-ATOM    509  C   PRO A  61     102.846 143.777  61.091  1.00 12.77           C  
-ATOM    510  O   PRO A  61     102.187 142.968  61.726  1.00 12.47           O  
-ATOM    511  CB  PRO A  61     101.982 146.129  61.451  1.00 14.91           C  
-ATOM    512  CG  PRO A  61     102.446 146.994  60.360  1.00 16.74           C  
-ATOM    513  CD  PRO A  61     103.935 147.153  60.589  1.00 14.14           C  
-ATOM    514  N   ASN A  62     103.337 143.540  59.872  1.00 10.92           N  
-ATOM    515  CA  ASN A  62     103.113 142.267  59.183  1.00 12.12           C  
-ATOM    516  C   ASN A  62     104.312 141.317  59.124  1.00 11.65           C  
-ATOM    517  O   ASN A  62     104.430 140.475  58.234  1.00 12.48           O  
-ATOM    518  CB  ASN A  62     102.541 142.551  57.785  1.00 12.27           C  
-ATOM    519  CG  ASN A  62     101.266 143.329  57.881  1.00 14.19           C  
-ATOM    520  OD1 ASN A  62     101.201 144.496  57.488  1.00 15.99           O  
-ATOM    521  ND2 ASN A  62     100.248 142.711  58.462  1.00 14.02           N  
-ATOM    522  N   ILE A  63     105.194 141.457  60.103  1.00 11.62           N  
-ATOM    523  CA  ILE A  63     106.347 140.564  60.241  1.00 11.49           C  
-ATOM    524  C   ILE A  63     106.336 140.193  61.728  1.00 11.74           C  
-ATOM    525  O   ILE A  63     106.278 141.084  62.579  1.00 13.34           O  
-ATOM    526  CB  ILE A  63     107.683 141.270  59.897  1.00 13.35           C  
-ATOM    527  CG1 ILE A  63     107.686 141.674  58.421  1.00 13.95           C  
-ATOM    528  CG2 ILE A  63     108.881 140.303  60.180  1.00 13.19           C  
-ATOM    529  CD1 ILE A  63     108.901 142.508  58.006  1.00 17.28           C  
-ATOM    530  N   VAL A  64     106.346 138.900  62.049  1.00 12.27           N  
-ATOM    531  CA  VAL A  64     106.324 138.482  63.441  1.00 13.06           C  
-ATOM    532  C   VAL A  64     107.454 139.181  64.206  1.00 13.77           C  
-ATOM    533  O   VAL A  64     108.603 139.287  63.740  1.00 13.06           O  
-ATOM    534  CB  VAL A  64     106.432 136.947  63.577  1.00 12.04           C  
-ATOM    535  CG1 VAL A  64     107.826 136.470  63.144  1.00 12.41           C  
-ATOM    536  CG2 VAL A  64     106.119 136.531  64.991  1.00 12.41           C  
-ATOM    537  N   LYS A  65     107.108 139.678  65.382  1.00 15.85           N  
-ATOM    538  CA  LYS A  65     108.071 140.417  66.175  1.00 16.77           C  
-ATOM    539  C   LYS A  65     109.021 139.574  67.000  1.00 16.30           C  
-ATOM    540  O   LYS A  65     108.595 138.740  67.809  1.00 15.34           O  
-ATOM    541  CB  LYS A  65     107.319 141.409  67.082  1.00 19.75           C  
-ATOM    542  CG  LYS A  65     108.234 142.330  67.875  1.00 25.06           C  
-ATOM    543  CD  LYS A  65     107.453 143.432  68.586  1.00 28.90           C  
-ATOM    544  CE  LYS A  65     108.399 144.419  69.269  1.00 30.87           C  
-ATOM    545  NZ  LYS A  65     107.654 145.490  70.002  1.00 35.36           N  
-ATOM    546  N   LEU A  66     110.318 139.779  66.771  1.00 17.49           N  
-ATOM    547  CA  LEU A  66     111.350 139.096  67.539  1.00 17.67           C  
-ATOM    548  C   LEU A  66     111.630 140.027  68.715  1.00 18.98           C  
-ATOM    549  O   LEU A  66     112.012 141.179  68.515  1.00 20.60           O  
-ATOM    550  CB  LEU A  66     112.618 138.919  66.701  1.00 18.26           C  
-ATOM    551  CG  LEU A  66     113.783 138.233  67.428  1.00 18.40           C  
-ATOM    552  CD1 LEU A  66     113.440 136.794  67.784  1.00 18.21           C  
-ATOM    553  CD2 LEU A  66     115.001 138.285  66.517  1.00 19.19           C  
-ATOM    554  N   LEU A  67     111.443 139.528  69.930  1.00 17.54           N  
-ATOM    555  CA  LEU A  67     111.624 140.328  71.133  1.00 18.26           C  
-ATOM    556  C   LEU A  67     113.016 140.245  71.742  1.00 17.97           C  
-ATOM    557  O   LEU A  67     113.510 141.237  72.302  1.00 17.04           O  
-ATOM    558  CB  LEU A  67     110.610 139.891  72.191  1.00 17.93           C  
-ATOM    559  CG  LEU A  67     109.144 140.029  71.749  1.00 19.16           C  
-ATOM    560  CD1 LEU A  67     108.239 139.342  72.747  1.00 18.34           C  
-ATOM    561  CD2 LEU A  67     108.800 141.508  71.595  1.00 20.26           C  
-ATOM    562  N   ASP A  68     113.638 139.072  71.629  1.00 17.73           N  
-ATOM    563  CA  ASP A  68     114.955 138.837  72.239  1.00 17.60           C  
-ATOM    564  C   ASP A  68     115.543 137.541  71.676  1.00 18.04           C  
-ATOM    565  O   ASP A  68     114.827 136.725  71.090  1.00 17.13           O  
-ATOM    566  CB  ASP A  68     114.768 138.718  73.775  1.00 18.39           C  
-ATOM    567  CG  ASP A  68     116.068 138.892  74.568  1.00 18.92           C  
-ATOM    568  OD1 ASP A  68     117.082 139.353  73.988  1.00 18.18           O  
-ATOM    569  OD2 ASP A  68     116.047 138.579  75.779  1.00 19.18           O  
-ATOM    570  N   VAL A  69     116.854 137.376  71.854  1.00 16.73           N  
-ATOM    571  CA  VAL A  69     117.590 136.209  71.398  1.00 17.32           C  
-ATOM    572  C   VAL A  69     118.465 135.869  72.596  1.00 17.67           C  
-ATOM    573  O   VAL A  69     119.281 136.694  73.033  1.00 17.56           O  
-ATOM    574  CB  VAL A  69     118.488 136.546  70.180  1.00 17.73           C  
-ATOM    575  CG1 VAL A  69     119.278 135.296  69.737  1.00 17.71           C  
-ATOM    576  CG2 VAL A  69     117.623 137.074  69.025  1.00 16.86           C  
-ATOM    577  N   ILE A  70     118.258 134.677  73.140  1.00 17.60           N  
-ATOM    578  CA  ILE A  70     118.995 134.203  74.313  1.00 18.78           C  
-ATOM    579  C   ILE A  70     120.037 133.175  73.868  1.00 20.08           C  
-ATOM    580  O   ILE A  70     119.711 132.220  73.177  1.00 20.09           O  
-ATOM    581  CB  ILE A  70     118.016 133.557  75.338  1.00 18.33           C  
-ATOM    582  CG1 ILE A  70     117.018 134.609  75.833  1.00 19.28           C  
-ATOM    583  CG2 ILE A  70     118.788 132.988  76.552  1.00 18.02           C  
-ATOM    584  CD1 ILE A  70     115.803 134.010  76.565  1.00 20.30           C  
-ATOM    585  N   HIS A  71     121.292 133.388  74.259  1.00 22.07           N  
-ATOM    586  CA  HIS A  71     122.374 132.480  73.891  1.00 24.28           C  
-ATOM    587  C   HIS A  71     122.786 131.617  75.068  1.00 27.44           C  
-ATOM    588  O   HIS A  71     122.994 132.121  76.165  1.00 26.43           O  
-ATOM    589  CB  HIS A  71     123.614 133.247  73.432  1.00 24.42           C  
-ATOM    590  CG  HIS A  71     123.464 133.916  72.105  1.00 21.77           C  
-ATOM    591  ND1 HIS A  71     122.698 135.046  71.920  1.00 22.81           N  
-ATOM    592  CD2 HIS A  71     123.997 133.619  70.899  1.00 19.97           C  
-ATOM    593  CE1 HIS A  71     122.772 135.421  70.655  1.00 19.74           C  
-ATOM    594  NE2 HIS A  71     123.553 134.570  70.014  1.00 22.61           N  
-ATOM    595  N   THR A  72     122.913 130.317  74.834  1.00 31.28           N  
-ATOM    596  CA  THR A  72     123.333 129.414  75.893  1.00 35.83           C  
-ATOM    597  C   THR A  72     123.857 128.102  75.319  1.00 38.33           C  
-ATOM    598  O   THR A  72     123.211 127.463  74.484  1.00 38.39           O  
-ATOM    599  CB  THR A  72     122.178 129.134  76.887  1.00 36.42           C  
-ATOM    600  OG1 THR A  72     122.659 128.312  77.956  1.00 39.91           O  
-ATOM    601  CG2 THR A  72     121.030 128.431  76.199  1.00 36.43           C  
-ATOM    602  N   GLU A  73     125.057 127.734  75.760  1.00 40.90           N  
-ATOM    603  CA  GLU A  73     125.717 126.500  75.343  1.00 43.72           C  
-ATOM    604  C   GLU A  73     125.386 125.956  73.957  1.00 43.92           C  
-ATOM    605  O   GLU A  73     124.600 125.016  73.824  1.00 44.89           O  
-ATOM    606  CB  GLU A  73     125.454 125.405  76.384  1.00 45.70           C  
-ATOM    607  CG  GLU A  73     126.216 125.598  77.684  1.00 48.96           C  
-ATOM    608  CD  GLU A  73     127.722 125.522  77.488  1.00 50.86           C  
-ATOM    609  OE1 GLU A  73     128.284 126.399  76.790  1.00 51.93           O  
-ATOM    610  OE2 GLU A  73     128.341 124.579  78.028  1.00 51.70           O  
-ATOM    611  N   ASN A  74     125.992 126.536  72.927  1.00 44.02           N  
-ATOM    612  CA  ASN A  74     125.774 126.064  71.562  1.00 43.78           C  
-ATOM    613  C   ASN A  74     124.311 126.111  71.125  1.00 42.57           C  
-ATOM    614  O   ASN A  74     123.933 125.468  70.143  1.00 42.52           O  
-ATOM    615  CB  ASN A  74     126.276 124.617  71.410  1.00 45.70           C  
-ATOM    616  CG  ASN A  74     127.669 124.406  71.991  1.00 47.15           C  
-ATOM    617  OD1 ASN A  74     128.598 125.169  71.708  1.00 48.30           O  
-ATOM    618  ND2 ASN A  74     127.822 123.355  72.798  1.00 47.20           N  
-ATOM    619  N   LYS A  75     123.484 126.855  71.851  1.00 40.65           N  
-ATOM    620  CA  LYS A  75     122.073 126.953  71.499  1.00 37.93           C  
-ATOM    621  C   LYS A  75     121.589 128.396  71.488  1.00 35.21           C  
-ATOM    622  O   LYS A  75     122.142 129.247  72.177  1.00 34.49           O  
-ATOM    623  CB  LYS A  75     121.218 126.137  72.476  1.00 40.18           C  
-ATOM    624  CG  LYS A  75     121.560 124.648  72.484  1.00 42.89           C  
-ATOM    625  CD  LYS A  75     120.669 123.851  73.423  1.00 45.01           C  
-ATOM    626  CE  LYS A  75     121.086 122.377  73.433  1.00 46.03           C  
-ATOM    627  NZ  LYS A  75     120.162 121.523  74.238  1.00 47.05           N  
-ATOM    628  N   LEU A  76     120.570 128.659  70.679  1.00 31.62           N  
-ATOM    629  CA  LEU A  76     119.966 129.982  70.592  1.00 29.72           C  
-ATOM    630  C   LEU A  76     118.473 129.834  70.779  1.00 27.52           C  
-ATOM    631  O   LEU A  76     117.855 128.968  70.158  1.00 27.97           O  
-ATOM    632  CB  LEU A  76     120.203 130.610  69.219  1.00 30.52           C  
-ATOM    633  CG  LEU A  76     121.196 131.761  69.159  1.00 32.12           C  
-ATOM    634  CD1 LEU A  76     122.559 131.276  69.572  1.00 32.81           C  
-ATOM    635  CD2 LEU A  76     121.230 132.310  67.755  1.00 32.24           C  
-ATOM    636  N   TYR A  77     117.892 130.663  71.634  1.00 24.85           N  
-ATOM    637  CA  TYR A  77     116.450 130.636  71.839  1.00 23.63           C  
-ATOM    638  C   TYR A  77     115.907 131.962  71.338  1.00 21.76           C  
-ATOM    639  O   TYR A  77     116.270 133.010  71.850  1.00 22.23           O  
-ATOM    640  CB  TYR A  77     116.120 130.486  73.314  1.00 26.15           C  
-ATOM    641  CG  TYR A  77     116.425 129.110  73.844  1.00 30.43           C  
-ATOM    642  CD1 TYR A  77     115.499 128.076  73.722  1.00 30.36           C  
-ATOM    643  CD2 TYR A  77     117.646 128.842  74.455  1.00 31.51           C  
-ATOM    644  CE1 TYR A  77     115.783 126.803  74.203  1.00 33.56           C  
-ATOM    645  CE2 TYR A  77     117.940 127.577  74.935  1.00 33.17           C  
-ATOM    646  CZ  TYR A  77     117.005 126.565  74.808  1.00 32.93           C  
-ATOM    647  OH  TYR A  77     117.300 125.316  75.298  1.00 35.64           O  
-ATOM    648  N   LEU A  78     115.058 131.923  70.324  1.00 19.33           N  
-ATOM    649  CA  LEU A  78     114.485 133.152  69.793  1.00 18.68           C  
-ATOM    650  C   LEU A  78     113.190 133.417  70.536  1.00 17.52           C  
-ATOM    651  O   LEU A  78     112.324 132.559  70.552  1.00 18.29           O  
-ATOM    652  CB  LEU A  78     114.186 132.999  68.298  1.00 18.55           C  
-ATOM    653  CG  LEU A  78     115.374 132.624  67.407  1.00 21.44           C  
-ATOM    654  CD1 LEU A  78     114.988 132.805  65.923  1.00 20.13           C  
-ATOM    655  CD2 LEU A  78     116.559 133.511  67.755  1.00 21.50           C  
-ATOM    656  N   VAL A  79     113.051 134.593  71.144  1.00 15.45           N  
-ATOM    657  CA  VAL A  79     111.832 134.910  71.873  1.00 14.04           C  
-ATOM    658  C   VAL A  79     110.957 135.800  70.986  1.00 15.05           C  
-ATOM    659  O   VAL A  79     111.341 136.914  70.658  1.00 12.75           O  
-ATOM    660  CB  VAL A  79     112.131 135.657  73.193  1.00 15.42           C  
-ATOM    661  CG1 VAL A  79     110.840 135.862  73.982  1.00 15.85           C  
-ATOM    662  CG2 VAL A  79     113.161 134.860  74.037  1.00 15.71           C  
-ATOM    663  N   PHE A  80     109.791 135.286  70.598  1.00 13.88           N  
-ATOM    664  CA  PHE A  80     108.873 136.026  69.735  1.00 15.60           C  
-ATOM    665  C   PHE A  80     107.588 136.341  70.448  1.00 16.04           C  
-ATOM    666  O   PHE A  80     107.257 135.711  71.444  1.00 16.27           O  
-ATOM    667  CB  PHE A  80     108.449 135.188  68.527  1.00 14.04           C  
-ATOM    668  CG  PHE A  80     109.526 134.952  67.527  1.00 15.03           C  
-ATOM    669  CD1 PHE A  80     109.777 135.900  66.535  1.00 14.34           C  
-ATOM    670  CD2 PHE A  80     110.252 133.760  67.535  1.00 15.01           C  
-ATOM    671  CE1 PHE A  80     110.733 135.668  65.554  1.00 16.40           C  
-ATOM    672  CE2 PHE A  80     111.219 133.514  66.550  1.00 16.78           C  
-ATOM    673  CZ  PHE A  80     111.451 134.483  65.553  1.00 15.78           C  
-ATOM    674  N   GLU A  81     106.844 137.287  69.882  1.00 17.12           N  
-ATOM    675  CA  GLU A  81     105.530 137.628  70.413  1.00 17.51           C  
-ATOM    676  C   GLU A  81     104.743 136.322  70.229  1.00 17.87           C  
-ATOM    677  O   GLU A  81     105.024 135.544  69.311  1.00 16.44           O  
-ATOM    678  CB  GLU A  81     104.898 138.739  69.575  1.00 18.93           C  
-ATOM    679  CG  GLU A  81     104.753 138.376  68.081  1.00 19.23           C  
-ATOM    680  CD  GLU A  81     103.932 139.382  67.289  1.00 20.00           C  
-ATOM    681  OE1 GLU A  81     102.805 139.699  67.729  1.00 22.90           O  
-ATOM    682  OE2 GLU A  81     104.399 139.848  66.227  1.00 20.11           O  
-ATOM    683  N   PHE A  82     103.758 136.092  71.089  1.00 18.66           N  
-ATOM    684  CA  PHE A  82     102.946 134.878  71.026  1.00 19.01           C  
-ATOM    685  C   PHE A  82     101.782 135.026  70.044  1.00 19.86           C  
-ATOM    686  O   PHE A  82     101.066 136.030  70.094  1.00 16.58           O  
-ATOM    687  CB  PHE A  82     102.392 134.570  72.407  1.00 19.31           C  
-ATOM    688  CG  PHE A  82     101.406 133.448  72.416  1.00 21.05           C  
-ATOM    689  CD1 PHE A  82     100.072 133.689  72.723  1.00 20.83           C  
-ATOM    690  CD2 PHE A  82     101.801 132.158  72.088  1.00 20.97           C  
-ATOM    691  CE1 PHE A  82      99.133 132.647  72.702  1.00 22.67           C  
-ATOM    692  CE2 PHE A  82     100.872 131.106  72.061  1.00 21.15           C  
-ATOM    693  CZ  PHE A  82      99.541 131.354  72.369  1.00 21.89           C  
-ATOM    694  N   LEU A  83     101.584 134.037  69.166  1.00 21.59           N  
-ATOM    695  CA  LEU A  83     100.485 134.103  68.193  1.00 25.48           C  
-ATOM    696  C   LEU A  83      99.611 132.841  67.968  1.00 27.91           C  
-ATOM    697  O   LEU A  83      98.388 132.956  67.751  1.00 30.00           O  
-ATOM    698  CB  LEU A  83     101.035 134.593  66.857  1.00 24.92           C  
-ATOM    699  CG  LEU A  83     101.386 136.083  66.854  1.00 25.28           C  
-ATOM    700  CD1 LEU A  83     102.057 136.438  65.552  1.00 23.93           C  
-ATOM    701  CD2 LEU A  83     100.126 136.917  67.055  1.00 23.98           C  
-ATOM    702  N   HIS A  84     100.261 131.679  68.020  1.00 30.34           N  
-ATOM    703  CA  HIS A  84      99.716 130.308  67.849  1.00 31.43           C  
-ATOM    704  C   HIS A  84      98.757 129.895  66.717  1.00 31.27           C  
-ATOM    705  O   HIS A  84      98.661 128.701  66.413  1.00 33.55           O  
-ATOM    706  CB  HIS A  84      99.144 129.778  69.179  1.00 34.22           C  
-ATOM    707  CG  HIS A  84      97.772 130.279  69.520  1.00 36.95           C  
-ATOM    708  ND1 HIS A  84      97.522 131.581  69.900  1.00 38.76           N  
-ATOM    709  CD2 HIS A  84      96.586 129.629  69.610  1.00 38.12           C  
-ATOM    710  CE1 HIS A  84      96.245 131.711  70.215  1.00 38.98           C  
-ATOM    711  NE2 HIS A  84      95.654 130.541  70.048  1.00 39.22           N  
-ATOM    712  N   GLN A  85      98.055 130.839  66.100  1.00 28.58           N  
-ATOM    713  CA  GLN A  85      97.142 130.514  64.999  1.00 27.29           C  
-ATOM    714  C   GLN A  85      97.825 130.828  63.647  1.00 24.02           C  
-ATOM    715  O   GLN A  85      98.523 131.819  63.533  1.00 21.03           O  
-ATOM    716  CB  GLN A  85      95.882 131.370  65.146  1.00 29.57           C  
-ATOM    717  CG  GLN A  85      94.741 131.014  64.243  1.00 35.04           C  
-ATOM    718  CD  GLN A  85      94.197 129.627  64.494  1.00 37.21           C  
-ATOM    719  OE1 GLN A  85      94.072 129.186  65.648  1.00 39.12           O  
-ATOM    720  NE2 GLN A  85      93.848 128.935  63.418  1.00 37.57           N  
-ATOM    721  N   ASP A  86      97.627 129.991  62.630  1.00 24.18           N  
-ATOM    722  CA  ASP A  86      98.234 130.276  61.329  1.00 23.13           C  
-ATOM    723  C   ASP A  86      97.223 130.096  60.207  1.00 22.73           C  
-ATOM    724  O   ASP A  86      96.142 129.528  60.412  1.00 20.86           O  
-ATOM    725  CB  ASP A  86      99.500 129.431  61.079  1.00 24.58           C  
-ATOM    726  CG  ASP A  86      99.222 127.948  60.966  1.00 27.64           C  
-ATOM    727  OD1 ASP A  86      98.387 127.557  60.133  1.00 27.53           O  
-ATOM    728  OD2 ASP A  86      99.860 127.166  61.709  1.00 30.71           O  
-ATOM    729  N   LEU A  87      97.573 130.589  59.024  1.00 20.35           N  
-ATOM    730  CA  LEU A  87      96.651 130.509  57.908  1.00 19.93           C  
-ATOM    731  C   LEU A  87      96.263 129.087  57.538  1.00 19.56           C  
-ATOM    732  O   LEU A  87      95.107 128.834  57.181  1.00 19.98           O  
-ATOM    733  CB  LEU A  87      97.231 131.238  56.694  1.00 18.01           C  
-ATOM    734  CG  LEU A  87      96.272 131.525  55.534  1.00 18.95           C  
-ATOM    735  CD1 LEU A  87      95.091 132.346  56.031  1.00 19.52           C  
-ATOM    736  CD2 LEU A  87      97.014 132.274  54.420  1.00 18.14           C  
-ATOM    737  N   LYS A  88      97.207 128.159  57.623  1.00 19.95           N  
-ATOM    738  CA  LYS A  88      96.905 126.773  57.280  1.00 21.18           C  
-ATOM    739  C   LYS A  88      95.828 126.231  58.232  1.00 21.80           C  
-ATOM    740  O   LYS A  88      94.788 125.731  57.799  1.00 21.98           O  
-ATOM    741  CB  LYS A  88      98.179 125.919  57.349  1.00 20.90           C  
-ATOM    742  CG  LYS A  88      97.957 124.437  57.027  1.00 22.49           C  
-ATOM    743  CD  LYS A  88      97.104 124.259  55.779  1.00 25.57           C  
-ATOM    744  CE  LYS A  88      96.613 122.828  55.669  1.00 27.30           C  
-ATOM    745  NZ  LYS A  88      95.990 122.550  54.358  1.00 29.16           N  
-ATOM    746  N   LYS A  89      96.067 126.365  59.533  1.00 22.09           N  
-ATOM    747  CA  LYS A  89      95.100 125.890  60.517  1.00 23.48           C  
-ATOM    748  C   LYS A  89      93.755 126.565  60.314  1.00 24.25           C  
-ATOM    749  O   LYS A  89      92.709 125.915  60.366  1.00 23.67           O  
-ATOM    750  CB  LYS A  89      95.588 126.170  61.941  1.00 25.36           C  
-ATOM    751  CG  LYS A  89      96.713 125.299  62.409  1.00 28.12           C  
-ATOM    752  CD  LYS A  89      97.075 125.674  63.835  1.00 31.10           C  
-ATOM    753  CE  LYS A  89      98.269 124.879  64.324  1.00 32.89           C  
-ATOM    754  NZ  LYS A  89      99.472 125.180  63.501  1.00 35.81           N  
-ATOM    755  N   PHE A  90      93.785 127.872  60.093  1.00 23.23           N  
-ATOM    756  CA  PHE A  90      92.567 128.633  59.877  1.00 25.09           C  
-ATOM    757  C   PHE A  90      91.809 128.161  58.635  1.00 25.13           C  
-ATOM    758  O   PHE A  90      90.583 128.049  58.658  1.00 25.40           O  
-ATOM    759  CB  PHE A  90      92.893 130.121  59.739  1.00 25.22           C  
-ATOM    760  CG  PHE A  90      91.683 130.998  59.605  1.00 26.54           C  
-ATOM    761  CD1 PHE A  90      90.669 130.963  60.561  1.00 28.71           C  
-ATOM    762  CD2 PHE A  90      91.570 131.887  58.546  1.00 27.16           C  
-ATOM    763  CE1 PHE A  90      89.566 131.812  60.458  1.00 29.03           C  
-ATOM    764  CE2 PHE A  90      90.483 132.733  58.432  1.00 27.16           C  
-ATOM    765  CZ  PHE A  90      89.476 132.701  59.389  1.00 28.76           C  
-ATOM    766  N   MET A  91      92.526 127.904  57.545  1.00 25.10           N  
-ATOM    767  CA  MET A  91      91.859 127.441  56.331  1.00 25.46           C  
-ATOM    768  C   MET A  91      91.235 126.071  56.582  1.00 26.94           C  
-ATOM    769  O   MET A  91      90.107 125.798  56.155  1.00 27.27           O  
-ATOM    770  CB  MET A  91      92.839 127.376  55.150  1.00 24.67           C  
-ATOM    771  CG  MET A  91      93.113 128.728  54.519  1.00 22.66           C  
-ATOM    772  SD  MET A  91      93.911 128.640  52.905  1.00 25.91           S  
-ATOM    773  CE  MET A  91      95.460 127.803  53.398  1.00 18.99           C  
-ATOM    774  N   ASP A  92      91.955 125.208  57.285  1.00 27.66           N  
-ATOM    775  CA  ASP A  92      91.412 123.888  57.577  1.00 29.61           C  
-ATOM    776  C   ASP A  92      90.151 123.997  58.420  1.00 31.05           C  
-ATOM    777  O   ASP A  92      89.234 123.203  58.257  1.00 31.53           O  
-ATOM    778  CB  ASP A  92      92.443 123.025  58.295  1.00 29.30           C  
-ATOM    779  CG  ASP A  92      93.590 122.637  57.394  1.00 29.61           C  
-ATOM    780  OD1 ASP A  92      93.462 122.822  56.167  1.00 29.72           O  
-ATOM    781  OD2 ASP A  92      94.610 122.145  57.907  1.00 30.48           O  
-ATOM    782  N   ALA A  93      90.104 124.979  59.317  1.00 32.43           N  
-ATOM    783  CA  ALA A  93      88.931 125.171  60.171  1.00 34.55           C  
-ATOM    784  C   ALA A  93      87.790 125.857  59.423  1.00 35.57           C  
-ATOM    785  O   ALA A  93      86.635 125.815  59.856  1.00 36.97           O  
-ATOM    786  CB  ALA A  93      89.304 125.982  61.398  1.00 33.92           C  
-ATOM    787  N   SER A  94      88.116 126.493  58.304  1.00 36.55           N  
-ATOM    788  CA  SER A  94      87.116 127.180  57.493  1.00 37.51           C  
-ATOM    789  C   SER A  94      86.829 126.354  56.240  1.00 38.46           C  
-ATOM    790  O   SER A  94      86.211 126.840  55.287  1.00 38.47           O  
-ATOM    791  CB  SER A  94      87.628 128.566  57.081  1.00 37.72           C  
-ATOM    792  OG  SER A  94      87.863 129.392  58.211  1.00 37.03           O  
-ATOM    793  N   ALA A  95      87.285 125.105  56.250  1.00 38.42           N  
-ATOM    794  CA  ALA A  95      87.114 124.209  55.112  1.00 39.44           C  
-ATOM    795  C   ALA A  95      85.686 124.134  54.576  1.00 40.01           C  
-ATOM    796  O   ALA A  95      85.453 124.280  53.376  1.00 39.51           O  
-ATOM    797  CB  ALA A  95      87.584 122.817  55.487  1.00 39.71           C  
-ATOM    798  N   LEU A  96      84.736 123.904  55.479  1.00 40.43           N  
-ATOM    799  CA  LEU A  96      83.331 123.762  55.111  1.00 39.88           C  
-ATOM    800  C   LEU A  96      82.685 124.941  54.402  1.00 38.31           C  
-ATOM    801  O   LEU A  96      81.837 124.761  53.534  1.00 38.10           O  
-ATOM    802  CB  LEU A  96      82.503 123.415  56.358  1.00 41.34           C  
-ATOM    803  CG  LEU A  96      82.761 122.042  56.996  1.00 42.33           C  
-ATOM    804  CD1 LEU A  96      81.833 121.857  58.196  1.00 42.46           C  
-ATOM    805  CD2 LEU A  96      82.524 120.930  55.963  1.00 41.68           C  
-ATOM    806  N   THR A  97      83.100 126.149  54.755  1.00 37.01           N  
-ATOM    807  CA  THR A  97      82.498 127.339  54.182  1.00 35.24           C  
-ATOM    808  C   THR A  97      83.460 128.231  53.426  1.00 33.64           C  
-ATOM    809  O   THR A  97      83.041 129.032  52.587  1.00 34.05           O  
-ATOM    810  CB  THR A  97      81.876 128.173  55.297  1.00 36.16           C  
-ATOM    811  OG1 THR A  97      82.867 128.397  56.309  1.00 37.02           O  
-ATOM    812  CG2 THR A  97      80.700 127.434  55.922  1.00 36.76           C  
-ATOM    813  N   GLY A  98      84.743 128.093  53.743  1.00 31.33           N  
-ATOM    814  CA  GLY A  98      85.765 128.910  53.125  1.00 28.97           C  
-ATOM    815  C   GLY A  98      85.932 130.214  53.889  1.00 27.24           C  
-ATOM    816  O   GLY A  98      85.025 130.660  54.574  1.00 24.75           O  
-ATOM    817  N   ILE A  99      87.108 130.816  53.793  1.00 26.53           N  
-ATOM    818  CA  ILE A  99      87.349 132.090  54.456  1.00 24.90           C  
-ATOM    819  C   ILE A  99      86.572 133.109  53.630  1.00 25.26           C  
-ATOM    820  O   ILE A  99      86.608 133.068  52.406  1.00 25.25           O  
-ATOM    821  CB  ILE A  99      88.851 132.444  54.425  1.00 26.18           C  
-ATOM    822  CG1 ILE A  99      89.641 131.390  55.212  1.00 25.84           C  
-ATOM    823  CG2 ILE A  99      89.071 133.847  54.985  1.00 25.95           C  
-ATOM    824  CD1 ILE A  99      91.145 131.467  55.016  1.00 27.43           C  
-ATOM    825  N   PRO A 100      85.837 134.023  54.284  1.00 24.63           N  
-ATOM    826  CA  PRO A 100      85.056 135.048  53.574  1.00 24.06           C  
-ATOM    827  C   PRO A 100      85.967 135.961  52.748  1.00 23.50           C  
-ATOM    828  O   PRO A 100      87.078 136.284  53.184  1.00 21.59           O  
-ATOM    829  CB  PRO A 100      84.382 135.824  54.709  1.00 24.92           C  
-ATOM    830  CG  PRO A 100      84.340 134.831  55.850  1.00 26.11           C  
-ATOM    831  CD  PRO A 100      85.676 134.144  55.743  1.00 25.68           C  
-ATOM    832  N   LEU A 101      85.482 136.400  51.587  1.00 22.67           N  
-ATOM    833  CA  LEU A 101      86.255 137.252  50.696  1.00 22.74           C  
-ATOM    834  C   LEU A 101      86.824 138.492  51.353  1.00 20.70           C  
-ATOM    835  O   LEU A 101      87.954 138.875  51.058  1.00 20.68           O  
-ATOM    836  CB  LEU A 101      85.438 137.681  49.470  1.00 22.91           C  
-ATOM    837  CG  LEU A 101      86.235 138.548  48.476  1.00 24.50           C  
-ATOM    838  CD1 LEU A 101      87.291 137.701  47.797  1.00 23.23           C  
-ATOM    839  CD2 LEU A 101      85.308 139.165  47.426  1.00 23.76           C  
-ATOM    840  N   PRO A 102      86.060 139.145  52.251  1.00 20.82           N  
-ATOM    841  CA  PRO A 102      86.650 140.335  52.862  1.00 19.33           C  
-ATOM    842  C   PRO A 102      87.925 140.005  53.649  1.00 17.63           C  
-ATOM    843  O   PRO A 102      88.862 140.804  53.670  1.00 18.49           O  
-ATOM    844  CB  PRO A 102      85.523 140.868  53.758  1.00 20.88           C  
-ATOM    845  CG  PRO A 102      84.271 140.381  53.037  1.00 21.92           C  
-ATOM    846  CD  PRO A 102      84.658 138.971  52.677  1.00 21.45           C  
-ATOM    847  N   LEU A 103      87.956 138.844  54.298  1.00 17.95           N  
-ATOM    848  CA  LEU A 103      89.130 138.426  55.067  1.00 18.53           C  
-ATOM    849  C   LEU A 103      90.259 138.021  54.129  1.00 17.68           C  
-ATOM    850  O   LEU A 103      91.430 138.283  54.396  1.00 16.42           O  
-ATOM    851  CB  LEU A 103      88.807 137.236  55.975  1.00 20.95           C  
-ATOM    852  CG  LEU A 103      88.904 137.464  57.488  1.00 24.75           C  
-ATOM    853  CD1 LEU A 103      88.946 136.109  58.196  1.00 25.88           C  
-ATOM    854  CD2 LEU A 103      90.143 138.271  57.836  1.00 23.24           C  
-ATOM    855  N   ILE A 104      89.903 137.342  53.043  1.00 16.53           N  
-ATOM    856  CA  ILE A 104      90.904 136.928  52.046  1.00 15.97           C  
-ATOM    857  C   ILE A 104      91.594 138.190  51.532  1.00 16.89           C  
-ATOM    858  O   ILE A 104      92.814 138.257  51.460  1.00 16.53           O  
-ATOM    859  CB  ILE A 104      90.245 136.187  50.825  1.00 15.03           C  
-ATOM    860  CG1 ILE A 104      89.736 134.812  51.267  1.00 14.41           C  
-ATOM    861  CG2 ILE A 104      91.268 136.080  49.652  1.00 15.79           C  
-ATOM    862  CD1 ILE A 104      89.017 134.027  50.175  1.00 16.41           C  
-ATOM    863  N   LYS A 105      90.796 139.188  51.163  1.00 15.71           N  
-ATOM    864  CA  LYS A 105      91.328 140.435  50.670  1.00 15.39           C  
-ATOM    865  C   LYS A 105      92.223 141.121  51.717  1.00 13.95           C  
-ATOM    866  O   LYS A 105      93.310 141.578  51.401  1.00 11.79           O  
-ATOM    867  CB  LYS A 105      90.166 141.342  50.268  1.00 16.72           C  
-ATOM    868  CG  LYS A 105      90.526 142.529  49.458  1.00 21.17           C  
-ATOM    869  CD  LYS A 105      89.270 143.116  48.786  1.00 22.28           C  
-ATOM    870  CE  LYS A 105      88.587 142.081  47.875  1.00 23.63           C  
-ATOM    871  NZ  LYS A 105      87.633 142.680  46.888  1.00 23.98           N  
-ATOM    872  N   SER A 106      91.757 141.180  52.957  1.00 14.18           N  
-ATOM    873  CA  SER A 106      92.543 141.810  54.021  1.00 14.01           C  
-ATOM    874  C   SER A 106      93.889 141.096  54.227  1.00 13.46           C  
-ATOM    875  O   SER A 106      94.941 141.731  54.295  1.00 13.86           O  
-ATOM    876  CB  SER A 106      91.761 141.781  55.329  1.00 15.97           C  
-ATOM    877  OG  SER A 106      92.563 142.310  56.374  1.00 17.41           O  
-ATOM    878  N   TYR A 107      93.852 139.773  54.326  1.00 12.30           N  
-ATOM    879  CA  TYR A 107      95.085 139.005  54.532  1.00 13.21           C  
-ATOM    880  C   TYR A 107      96.054 139.168  53.362  1.00 12.50           C  
-ATOM    881  O   TYR A 107      97.266 139.306  53.558  1.00 12.88           O  
-ATOM    882  CB  TYR A 107      94.770 137.520  54.709  1.00 13.27           C  
-ATOM    883  CG  TYR A 107      94.168 137.148  56.052  1.00 14.78           C  
-ATOM    884  CD1 TYR A 107      94.235 138.032  57.145  1.00 13.49           C  
-ATOM    885  CD2 TYR A 107      93.619 135.888  56.262  1.00 15.35           C  
-ATOM    886  CE1 TYR A 107      93.777 137.656  58.393  1.00 15.46           C  
-ATOM    887  CE2 TYR A 107      93.159 135.504  57.514  1.00 16.99           C  
-ATOM    888  CZ  TYR A 107      93.244 136.397  58.579  1.00 17.86           C  
-ATOM    889  OH  TYR A 107      92.827 136.019  59.840  1.00 18.64           O  
-ATOM    890  N   LEU A 108      95.529 139.131  52.140  1.00 13.33           N  
-ATOM    891  CA  LEU A 108      96.393 139.261  50.973  1.00 12.88           C  
-ATOM    892  C   LEU A 108      97.022 140.640  50.958  1.00 12.96           C  
-ATOM    893  O   LEU A 108      98.218 140.764  50.719  1.00 12.75           O  
-ATOM    894  CB  LEU A 108      95.597 139.000  49.676  1.00 14.25           C  
-ATOM    895  CG  LEU A 108      96.384 138.998  48.358  1.00 14.99           C  
-ATOM    896  CD1 LEU A 108      97.401 137.847  48.351  1.00 15.59           C  
-ATOM    897  CD2 LEU A 108      95.404 138.839  47.176  1.00 13.74           C  
-ATOM    898  N   PHE A 109      96.209 141.670  51.227  1.00 12.52           N  
-ATOM    899  CA  PHE A 109      96.687 143.054  51.252  1.00 11.74           C  
-ATOM    900  C   PHE A 109      97.810 143.197  52.285  1.00 11.43           C  
-ATOM    901  O   PHE A 109      98.865 143.749  51.997  1.00 12.52           O  
-ATOM    902  CB  PHE A 109      95.535 144.017  51.605  1.00 14.45           C  
-ATOM    903  CG  PHE A 109      95.866 145.490  51.408  1.00 15.53           C  
-ATOM    904  CD1 PHE A 109      95.917 146.052  50.135  1.00 17.22           C  
-ATOM    905  CD2 PHE A 109      96.111 146.312  52.497  1.00 18.70           C  
-ATOM    906  CE1 PHE A 109      96.206 147.416  49.948  1.00 18.12           C  
-ATOM    907  CE2 PHE A 109      96.403 147.682  52.318  1.00 19.04           C  
-ATOM    908  CZ  PHE A 109      96.449 148.226  51.046  1.00 18.43           C  
-ATOM    909  N   GLN A 110      97.577 142.692  53.487  1.00 11.83           N  
-ATOM    910  CA  GLN A 110      98.585 142.793  54.533  1.00 10.48           C  
-ATOM    911  C   GLN A 110      99.865 142.040  54.206  1.00 11.16           C  
-ATOM    912  O   GLN A 110     100.954 142.493  54.549  1.00  9.91           O  
-ATOM    913  CB  GLN A 110      98.043 142.259  55.850  1.00 11.08           C  
-ATOM    914  CG  GLN A 110      96.928 143.094  56.469  1.00 12.36           C  
-ATOM    915  CD  GLN A 110      96.475 142.466  57.774  1.00 14.04           C  
-ATOM    916  OE1 GLN A 110      97.253 142.403  58.732  1.00 14.21           O  
-ATOM    917  NE2 GLN A 110      95.224 141.973  57.816  1.00 12.12           N  
-ATOM    918  N   LEU A 111      99.729 140.854  53.617  1.00 11.22           N  
-ATOM    919  CA  LEU A 111     100.920 140.093  53.248  1.00 10.55           C  
-ATOM    920  C   LEU A 111     101.703 140.845  52.183  1.00 11.46           C  
-ATOM    921  O   LEU A 111     102.938 140.807  52.190  1.00 11.60           O  
-ATOM    922  CB  LEU A 111     100.536 138.689  52.754  1.00 12.15           C  
-ATOM    923  CG  LEU A 111      99.960 137.797  53.863  1.00 13.34           C  
-ATOM    924  CD1 LEU A 111      99.404 136.513  53.260  1.00 15.37           C  
-ATOM    925  CD2 LEU A 111     101.071 137.500  54.869  1.00 17.54           C  
-ATOM    926  N   LEU A 112     101.001 141.529  51.271  1.00 11.48           N  
-ATOM    927  CA  LEU A 112     101.679 142.315  50.247  1.00 11.02           C  
-ATOM    928  C   LEU A 112     102.417 143.491  50.919  1.00 12.55           C  
-ATOM    929  O   LEU A 112     103.525 143.836  50.511  1.00 12.19           O  
-ATOM    930  CB  LEU A 112     100.679 142.823  49.183  1.00 11.35           C  
-ATOM    931  CG  LEU A 112     100.250 141.719  48.203  1.00 12.95           C  
-ATOM    932  CD1 LEU A 112      99.013 142.137  47.397  1.00 12.33           C  
-ATOM    933  CD2 LEU A 112     101.445 141.404  47.279  1.00 12.82           C  
-ATOM    934  N   GLN A 113     101.809 144.086  51.951  1.00 12.59           N  
-ATOM    935  CA  GLN A 113     102.456 145.192  52.667  1.00 14.79           C  
-ATOM    936  C   GLN A 113     103.732 144.683  53.337  1.00 13.03           C  
-ATOM    937  O   GLN A 113     104.769 145.340  53.275  1.00 13.18           O  
-ATOM    938  CB  GLN A 113     101.539 145.785  53.738  1.00 15.01           C  
-ATOM    939  CG  GLN A 113     100.307 146.496  53.163  1.00 18.38           C  
-ATOM    940  CD  GLN A 113      99.412 147.069  54.244  1.00 18.78           C  
-ATOM    941  OE1 GLN A 113      99.387 148.278  54.454  1.00 24.33           O  
-ATOM    942  NE2 GLN A 113      98.680 146.213  54.935  1.00 18.19           N  
-ATOM    943  N   GLY A 114     103.636 143.513  53.964  1.00 13.02           N  
-ATOM    944  CA  GLY A 114     104.795 142.929  54.616  1.00 12.47           C  
-ATOM    945  C   GLY A 114     105.893 142.630  53.617  1.00 11.36           C  
-ATOM    946  O   GLY A 114     107.075 142.933  53.847  1.00 11.44           O  
-ATOM    947  N   LEU A 115     105.517 142.050  52.485  1.00 11.89           N  
-ATOM    948  CA  LEU A 115     106.514 141.716  51.461  1.00 11.78           C  
-ATOM    949  C   LEU A 115     107.104 142.949  50.822  1.00 11.63           C  
-ATOM    950  O   LEU A 115     108.297 142.992  50.541  1.00 11.30           O  
-ATOM    951  CB  LEU A 115     105.896 140.822  50.375  1.00 12.32           C  
-ATOM    952  CG  LEU A 115     105.560 139.385  50.789  1.00 14.17           C  
-ATOM    953  CD1 LEU A 115     104.830 138.728  49.596  1.00 14.76           C  
-ATOM    954  CD2 LEU A 115     106.849 138.568  51.156  1.00 15.16           C  
-ATOM    955  N   ALA A 116     106.283 143.961  50.587  1.00 11.94           N  
-ATOM    956  CA  ALA A 116     106.795 145.185  49.989  1.00 12.79           C  
-ATOM    957  C   ALA A 116     107.904 145.763  50.881  1.00 12.70           C  
-ATOM    958  O   ALA A 116     108.955 146.219  50.393  1.00 11.96           O  
-ATOM    959  CB  ALA A 116     105.667 146.203  49.808  1.00 13.08           C  
-ATOM    960  N   PHE A 117     107.656 145.742  52.181  1.00 12.25           N  
-ATOM    961  CA  PHE A 117     108.617 146.246  53.159  1.00 13.37           C  
-ATOM    962  C   PHE A 117     109.908 145.440  53.132  1.00 13.84           C  
-ATOM    963  O   PHE A 117     111.001 146.007  53.057  1.00 14.06           O  
-ATOM    964  CB  PHE A 117     108.009 146.188  54.564  1.00 15.29           C  
-ATOM    965  CG  PHE A 117     108.812 146.918  55.602  1.00 16.57           C  
-ATOM    966  CD1 PHE A 117     108.850 148.310  55.621  1.00 17.97           C  
-ATOM    967  CD2 PHE A 117     109.539 146.215  56.550  1.00 18.85           C  
-ATOM    968  CE1 PHE A 117     109.609 148.981  56.581  1.00 19.83           C  
-ATOM    969  CE2 PHE A 117     110.296 146.883  57.502  1.00 19.66           C  
-ATOM    970  CZ  PHE A 117     110.329 148.263  57.520  1.00 18.91           C  
-ATOM    971  N   CYS A 118     109.782 144.114  53.190  1.00 12.98           N  
-ATOM    972  CA  CYS A 118     110.954 143.254  53.170  1.00 13.98           C  
-ATOM    973  C   CYS A 118     111.755 143.513  51.914  1.00 13.24           C  
-ATOM    974  O   CYS A 118     112.967 143.766  51.969  1.00 12.69           O  
-ATOM    975  CB  CYS A 118     110.547 141.771  53.183  1.00 13.55           C  
-ATOM    976  SG  CYS A 118     109.823 141.198  54.707  1.00 16.83           S  
-ATOM    977  N   HIS A 119     111.070 143.441  50.777  1.00 12.16           N  
-ATOM    978  CA  HIS A 119     111.741 143.621  49.488  1.00 13.23           C  
-ATOM    979  C   HIS A 119     112.446 144.962  49.344  1.00 14.62           C  
-ATOM    980  O   HIS A 119     113.520 145.021  48.743  1.00 16.09           O  
-ATOM    981  CB  HIS A 119     110.744 143.419  48.340  1.00 12.66           C  
-ATOM    982  CG  HIS A 119     110.203 142.020  48.266  1.00 12.91           C  
-ATOM    983  ND1 HIS A 119     109.164 141.657  47.433  1.00 11.20           N  
-ATOM    984  CD2 HIS A 119     110.590 140.890  48.903  1.00 11.54           C  
-ATOM    985  CE1 HIS A 119     108.939 140.361  47.559  1.00 14.20           C  
-ATOM    986  NE2 HIS A 119     109.791 139.870  48.444  1.00 10.90           N  
-ATOM    987  N   SER A 120     111.868 146.027  49.892  1.00 14.97           N  
-ATOM    988  CA  SER A 120     112.519 147.341  49.788  1.00 17.01           C  
-ATOM    989  C   SER A 120     113.765 147.392  50.669  1.00 17.28           C  
-ATOM    990  O   SER A 120     114.651 148.233  50.468  1.00 17.96           O  
-ATOM    991  CB  SER A 120     111.538 148.478  50.152  1.00 16.47           C  
-ATOM    992  OG  SER A 120     111.148 148.412  51.508  1.00 17.83           O  
-ATOM    993  N   HIS A 121     113.843 146.485  51.639  1.00 16.82           N  
-ATOM    994  CA  HIS A 121     114.987 146.393  52.534  1.00 17.79           C  
-ATOM    995  C   HIS A 121     115.933 145.248  52.140  1.00 16.68           C  
-ATOM    996  O   HIS A 121     116.787 144.854  52.926  1.00 16.71           O  
-ATOM    997  CB  HIS A 121     114.512 146.204  53.983  1.00 20.84           C  
-ATOM    998  CG  HIS A 121     113.886 147.431  54.572  1.00 23.53           C  
-ATOM    999  ND1 HIS A 121     112.718 147.979  54.088  1.00 27.14           N  
-ATOM   1000  CD2 HIS A 121     114.295 148.248  55.571  1.00 27.75           C  
-ATOM   1001  CE1 HIS A 121     112.435 149.082  54.759  1.00 27.33           C  
-ATOM   1002  NE2 HIS A 121     113.377 149.268  55.664  1.00 27.10           N  
-ATOM   1003  N   ARG A 122     115.750 144.723  50.924  1.00 15.32           N  
-ATOM   1004  CA  ARG A 122     116.561 143.632  50.372  1.00 16.86           C  
-ATOM   1005  C   ARG A 122     116.418 142.282  51.060  1.00 16.61           C  
-ATOM   1006  O   ARG A 122     117.327 141.441  51.024  1.00 17.51           O  
-ATOM   1007  CB  ARG A 122     118.034 144.047  50.342  1.00 18.79           C  
-ATOM   1008  CG  ARG A 122     118.242 145.392  49.648  1.00 23.48           C  
-ATOM   1009  CD  ARG A 122     119.713 145.646  49.360  1.00 25.16           C  
-ATOM   1010  NE  ARG A 122     120.532 145.597  50.566  1.00 30.09           N  
-ATOM   1011  CZ  ARG A 122     120.641 146.592  51.439  1.00 31.09           C  
-ATOM   1012  NH1 ARG A 122     121.415 146.451  52.513  1.00 32.56           N  
-ATOM   1013  NH2 ARG A 122     119.988 147.732  51.236  1.00 33.45           N  
-ATOM   1014  N   VAL A 123     115.260 142.062  51.671  1.00 14.96           N  
-ATOM   1015  CA  VAL A 123     114.984 140.823  52.356  1.00 14.49           C  
-ATOM   1016  C   VAL A 123     113.903 140.072  51.581  1.00 15.55           C  
-ATOM   1017  O   VAL A 123     112.894 140.671  51.206  1.00 15.85           O  
-ATOM   1018  CB  VAL A 123     114.456 141.090  53.783  1.00 15.31           C  
-ATOM   1019  CG1 VAL A 123     113.914 139.801  54.394  1.00 15.87           C  
-ATOM   1020  CG2 VAL A 123     115.569 141.677  54.645  1.00 15.82           C  
-ATOM   1021  N   LEU A 124     114.136 138.781  51.336  1.00 15.07           N  
-ATOM   1022  CA  LEU A 124     113.160 137.932  50.654  1.00 15.24           C  
-ATOM   1023  C   LEU A 124     112.706 136.915  51.658  1.00 14.77           C  
-ATOM   1024  O   LEU A 124     113.456 136.577  52.580  1.00 14.66           O  
-ATOM   1025  CB  LEU A 124     113.770 137.189  49.460  1.00 15.97           C  
-ATOM   1026  CG  LEU A 124     113.813 137.973  48.147  1.00 17.93           C  
-ATOM   1027  CD1 LEU A 124     114.825 139.106  48.246  1.00 18.63           C  
-ATOM   1028  CD2 LEU A 124     114.185 137.024  47.015  1.00 19.11           C  
-ATOM   1029  N   HIS A 125     111.487 136.405  51.508  1.00 13.52           N  
-ATOM   1030  CA  HIS A 125     111.049 135.398  52.451  1.00 12.31           C  
-ATOM   1031  C   HIS A 125     111.594 134.041  51.993  1.00 13.08           C  
-ATOM   1032  O   HIS A 125     112.227 133.298  52.764  1.00 12.71           O  
-ATOM   1033  CB  HIS A 125     109.527 135.332  52.545  1.00 12.29           C  
-ATOM   1034  CG  HIS A 125     109.053 134.331  53.551  1.00 11.32           C  
-ATOM   1035  ND1 HIS A 125     108.646 134.682  54.821  1.00 14.21           N  
-ATOM   1036  CD2 HIS A 125     108.970 132.982  53.491  1.00 11.88           C  
-ATOM   1037  CE1 HIS A 125     108.329 133.592  55.496  1.00 11.36           C  
-ATOM   1038  NE2 HIS A 125     108.519 132.547  54.711  1.00 15.04           N  
-ATOM   1039  N   ARG A 126     111.300 133.721  50.737  1.00 13.27           N  
-ATOM   1040  CA  ARG A 126     111.759 132.495  50.079  1.00 16.01           C  
-ATOM   1041  C   ARG A 126     111.016 131.208  50.362  1.00 16.38           C  
-ATOM   1042  O   ARG A 126     111.191 130.242  49.616  1.00 18.58           O  
-ATOM   1043  CB  ARG A 126     113.249 132.228  50.353  1.00 16.56           C  
-ATOM   1044  CG  ARG A 126     114.192 133.348  49.964  1.00 19.26           C  
-ATOM   1045  CD  ARG A 126     115.655 132.971  50.208  1.00 20.53           C  
-ATOM   1046  NE  ARG A 126     116.522 134.043  49.730  1.00 22.06           N  
-ATOM   1047  CZ  ARG A 126     116.745 135.175  50.385  1.00 22.21           C  
-ATOM   1048  NH1 ARG A 126     116.184 135.383  51.567  1.00 23.74           N  
-ATOM   1049  NH2 ARG A 126     117.487 136.128  49.830  1.00 22.56           N  
-ATOM   1050  N   ASP A 127     110.209 131.164  51.414  1.00 15.39           N  
-ATOM   1051  CA  ASP A 127     109.494 129.933  51.703  1.00 16.03           C  
-ATOM   1052  C   ASP A 127     108.075 130.211  52.167  1.00 14.88           C  
-ATOM   1053  O   ASP A 127     107.617 129.654  53.152  1.00 14.89           O  
-ATOM   1054  CB  ASP A 127     110.255 129.116  52.750  1.00 17.27           C  
-ATOM   1055  CG  ASP A 127     109.608 127.758  53.019  1.00 20.03           C  
-ATOM   1056  OD1 ASP A 127     109.020 127.175  52.076  1.00 21.70           O  
-ATOM   1057  OD2 ASP A 127     109.707 127.278  54.165  1.00 20.95           O  
-ATOM   1058  N   LEU A 128     107.386 131.098  51.460  1.00 13.33           N  
-ATOM   1059  CA  LEU A 128     106.012 131.430  51.812  1.00 14.93           C  
-ATOM   1060  C   LEU A 128     105.060 130.269  51.616  1.00 16.04           C  
-ATOM   1061  O   LEU A 128     105.015 129.666  50.548  1.00 16.68           O  
-ATOM   1062  CB  LEU A 128     105.513 132.600  50.971  1.00 16.96           C  
-ATOM   1063  CG  LEU A 128     106.072 133.961  51.328  1.00 18.17           C  
-ATOM   1064  CD1 LEU A 128     105.679 134.948  50.232  1.00 19.25           C  
-ATOM   1065  CD2 LEU A 128     105.527 134.395  52.693  1.00 19.16           C  
-ATOM   1066  N   LYS A 129     104.313 129.953  52.661  1.00 15.92           N  
-ATOM   1067  CA  LYS A 129     103.323 128.898  52.612  1.00 16.68           C  
-ATOM   1068  C   LYS A 129     102.354 129.187  53.741  1.00 16.63           C  
-ATOM   1069  O   LYS A 129     102.719 129.812  54.729  1.00 17.16           O  
-ATOM   1070  CB  LYS A 129     103.959 127.522  52.767  1.00 19.43           C  
-ATOM   1071  CG  LYS A 129     104.795 127.331  53.992  1.00 24.17           C  
-ATOM   1072  CD  LYS A 129     105.396 125.929  53.986  1.00 28.45           C  
-ATOM   1073  CE  LYS A 129     106.209 125.669  55.223  1.00 31.34           C  
-ATOM   1074  NZ  LYS A 129     107.462 126.458  55.212  1.00 33.45           N  
-ATOM   1075  N   PRO A 130     101.101 128.728  53.611  1.00 17.06           N  
-ATOM   1076  CA  PRO A 130     100.087 128.968  54.642  1.00 16.76           C  
-ATOM   1077  C   PRO A 130     100.562 128.729  56.073  1.00 17.88           C  
-ATOM   1078  O   PRO A 130     100.224 129.484  56.969  1.00 16.49           O  
-ATOM   1079  CB  PRO A 130      98.959 128.011  54.249  1.00 18.40           C  
-ATOM   1080  CG  PRO A 130      99.107 127.890  52.782  1.00 17.36           C  
-ATOM   1081  CD  PRO A 130     100.597 127.798  52.586  1.00 16.77           C  
-ATOM   1082  N   GLN A 131     101.304 127.645  56.267  1.00 19.58           N  
-ATOM   1083  CA  GLN A 131     101.841 127.261  57.562  1.00 22.71           C  
-ATOM   1084  C   GLN A 131     102.693 128.347  58.220  1.00 22.71           C  
-ATOM   1085  O   GLN A 131     102.698 128.478  59.449  1.00 25.01           O  
-ATOM   1086  CB  GLN A 131     102.687 125.991  57.404  1.00 25.39           C  
-ATOM   1087  CG  GLN A 131     103.480 125.622  58.639  1.00 33.08           C  
-ATOM   1088  CD  GLN A 131     104.303 124.350  58.482  1.00 35.01           C  
-ATOM   1089  OE1 GLN A 131     103.793 123.312  58.041  1.00 37.69           O  
-ATOM   1090  NE2 GLN A 131     105.581 124.420  58.863  1.00 35.99           N  
-ATOM   1091  N   ASN A 132     103.410 129.117  57.407  1.00 21.49           N  
-ATOM   1092  CA  ASN A 132     104.303 130.160  57.919  1.00 22.40           C  
-ATOM   1093  C   ASN A 132     103.668 131.542  58.124  1.00 21.04           C  
-ATOM   1094  O   ASN A 132     104.383 132.511  58.403  1.00 22.43           O  
-ATOM   1095  CB  ASN A 132     105.521 130.296  56.987  1.00 24.02           C  
-ATOM   1096  CG  ASN A 132     106.275 128.984  56.828  1.00 28.17           C  
-ATOM   1097  OD1 ASN A 132     106.112 128.069  57.640  1.00 29.65           O  
-ATOM   1098  ND2 ASN A 132     107.109 128.885  55.792  1.00 28.10           N  
-ATOM   1099  N   LEU A 133     102.346 131.640  58.013  1.00 17.36           N  
-ATOM   1100  CA  LEU A 133     101.693 132.943  58.147  1.00 15.14           C  
-ATOM   1101  C   LEU A 133     100.810 132.952  59.394  1.00 15.96           C  
-ATOM   1102  O   LEU A 133      99.767 132.299  59.468  1.00 18.02           O  
-ATOM   1103  CB  LEU A 133     100.901 133.253  56.876  1.00 15.04           C  
-ATOM   1104  CG  LEU A 133     101.743 133.091  55.592  1.00 15.31           C  
-ATOM   1105  CD1 LEU A 133     100.835 133.205  54.371  1.00 14.43           C  
-ATOM   1106  CD2 LEU A 133     102.872 134.147  55.562  1.00 16.78           C  
-ATOM   1107  N   LEU A 134     101.241 133.728  60.372  1.00 13.34           N  
-ATOM   1108  CA  LEU A 134     100.571 133.772  61.662  1.00 12.91           C  
-ATOM   1109  C   LEU A 134      99.490 134.817  61.771  1.00 12.49           C  
-ATOM   1110  O   LEU A 134      99.676 135.939  61.321  1.00 13.86           O  
-ATOM   1111  CB  LEU A 134     101.616 134.048  62.724  1.00 13.45           C  
-ATOM   1112  CG  LEU A 134     102.801 133.092  62.586  1.00 16.55           C  
-ATOM   1113  CD1 LEU A 134     103.913 133.534  63.503  1.00 16.87           C  
-ATOM   1114  CD2 LEU A 134     102.346 131.686  62.877  1.00 18.39           C  
-ATOM   1115  N   ILE A 135      98.392 134.465  62.430  1.00 13.34           N  
-ATOM   1116  CA  ILE A 135      97.300 135.407  62.592  1.00 14.11           C  
-ATOM   1117  C   ILE A 135      96.941 135.681  64.058  1.00 14.90           C  
-ATOM   1118  O   ILE A 135      97.138 134.840  64.937  1.00 14.81           O  
-ATOM   1119  CB  ILE A 135      96.046 134.896  61.856  1.00 14.65           C  
-ATOM   1120  CG1 ILE A 135      95.618 133.556  62.446  1.00 15.86           C  
-ATOM   1121  CG2 ILE A 135      96.358 134.701  60.373  1.00 15.07           C  
-ATOM   1122  CD1 ILE A 135      94.396 132.947  61.742  1.00 20.73           C  
-ATOM   1123  N   ASN A 136      96.404 136.864  64.324  1.00 15.32           N  
-ATOM   1124  CA  ASN A 136      96.003 137.162  65.697  1.00 16.89           C  
-ATOM   1125  C   ASN A 136      94.504 137.471  65.789  1.00 18.35           C  
-ATOM   1126  O   ASN A 136      93.789 137.521  64.785  1.00 17.79           O  
-ATOM   1127  CB  ASN A 136      96.862 138.295  66.293  1.00 18.38           C  
-ATOM   1128  CG  ASN A 136      96.651 139.641  65.609  1.00 18.94           C  
-ATOM   1129  OD1 ASN A 136      95.662 139.851  64.908  1.00 20.11           O  
-ATOM   1130  ND2 ASN A 136      97.583 140.577  65.838  1.00 18.53           N  
-ATOM   1131  N   THR A 137      94.021 137.643  67.010  1.00 20.02           N  
-ATOM   1132  CA  THR A 137      92.607 137.905  67.231  1.00 20.89           C  
-ATOM   1133  C   THR A 137      92.092 139.166  66.553  1.00 20.52           C  
-ATOM   1134  O   THR A 137      90.926 139.220  66.145  1.00 21.17           O  
-ATOM   1135  CB  THR A 137      92.335 138.032  68.740  1.00 22.22           C  
-ATOM   1136  OG1 THR A 137      93.218 139.012  69.289  1.00 29.01           O  
-ATOM   1137  CG2 THR A 137      92.603 136.745  69.434  1.00 21.08           C  
-ATOM   1138  N   GLU A 138      92.945 140.179  66.451  1.00 19.44           N  
-ATOM   1139  CA  GLU A 138      92.539 141.446  65.871  1.00 20.93           C  
-ATOM   1140  C   GLU A 138      92.530 141.548  64.344  1.00 19.52           C  
-ATOM   1141  O   GLU A 138      92.236 142.608  63.796  1.00 22.08           O  
-ATOM   1142  CB  GLU A 138      93.365 142.575  66.492  1.00 21.55           C  
-ATOM   1143  CG  GLU A 138      93.060 142.755  67.976  1.00 25.26           C  
-ATOM   1144  CD  GLU A 138      93.978 143.752  68.665  1.00 27.78           C  
-ATOM   1145  OE1 GLU A 138      93.668 144.965  68.640  1.00 26.28           O  
-ATOM   1146  OE2 GLU A 138      95.011 143.309  69.226  1.00 28.14           O  
-ATOM   1147  N   GLY A 139      92.835 140.456  63.660  1.00 18.43           N  
-ATOM   1148  CA  GLY A 139      92.798 140.493  62.208  1.00 17.11           C  
-ATOM   1149  C   GLY A 139      94.112 140.703  61.467  1.00 16.65           C  
-ATOM   1150  O   GLY A 139      94.108 140.837  60.245  1.00 15.88           O  
-ATOM   1151  N   ALA A 140      95.228 140.764  62.179  1.00 14.74           N  
-ATOM   1152  CA  ALA A 140      96.490 140.944  61.478  1.00 14.29           C  
-ATOM   1153  C   ALA A 140      96.969 139.568  61.023  1.00 14.24           C  
-ATOM   1154  O   ALA A 140      96.557 138.542  61.567  1.00 14.44           O  
-ATOM   1155  CB  ALA A 140      97.538 141.563  62.410  1.00 14.73           C  
-ATOM   1156  N   ILE A 141      97.829 139.554  60.012  1.00 14.00           N  
-ATOM   1157  CA  ILE A 141      98.453 138.320  59.548  1.00 12.53           C  
-ATOM   1158  C   ILE A 141      99.922 138.725  59.410  1.00 12.42           C  
-ATOM   1159  O   ILE A 141     100.233 139.863  59.032  1.00 12.55           O  
-ATOM   1160  CB  ILE A 141      97.839 137.796  58.217  1.00 11.73           C  
-ATOM   1161  CG1 ILE A 141      98.482 136.444  57.868  1.00 12.08           C  
-ATOM   1162  CG2 ILE A 141      98.005 138.834  57.120  1.00 10.05           C  
-ATOM   1163  CD1 ILE A 141      97.711 135.663  56.790  1.00 13.29           C  
-ATOM   1164  N   LYS A 142     100.831 137.824  59.762  1.00 11.66           N  
-ATOM   1165  CA  LYS A 142     102.249 138.173  59.761  1.00 11.83           C  
-ATOM   1166  C   LYS A 142     103.175 137.120  59.171  1.00 11.63           C  
-ATOM   1167  O   LYS A 142     102.982 135.934  59.392  1.00 11.17           O  
-ATOM   1168  CB  LYS A 142     102.708 138.419  61.215  1.00 13.02           C  
-ATOM   1169  CG  LYS A 142     101.783 139.347  62.031  1.00 13.56           C  
-ATOM   1170  CD  LYS A 142     102.490 139.816  63.320  1.00 17.14           C  
-ATOM   1171  CE  LYS A 142     101.652 140.853  64.090  1.00 17.24           C  
-ATOM   1172  NZ  LYS A 142     102.417 141.494  65.200  1.00 17.28           N  
-ATOM   1173  N   LEU A 143     104.209 137.598  58.481  1.00 10.81           N  
-ATOM   1174  CA  LEU A 143     105.243 136.753  57.886  1.00 11.69           C  
-ATOM   1175  C   LEU A 143     106.114 136.123  58.981  1.00 12.93           C  
-ATOM   1176  O   LEU A 143     106.478 136.784  59.945  1.00 12.78           O  
-ATOM   1177  CB  LEU A 143     106.144 137.603  56.988  1.00 10.88           C  
-ATOM   1178  CG  LEU A 143     105.425 138.276  55.824  1.00 12.59           C  
-ATOM   1179  CD1 LEU A 143     106.316 139.358  55.200  1.00 13.29           C  
-ATOM   1180  CD2 LEU A 143     105.046 137.187  54.792  1.00 12.64           C  
-ATOM   1181  N   ALA A 144     106.440 134.845  58.820  1.00 13.25           N  
-ATOM   1182  CA  ALA A 144     107.290 134.136  59.778  1.00 13.01           C  
-ATOM   1183  C   ALA A 144     107.924 132.959  59.067  1.00 13.12           C  
-ATOM   1184  O   ALA A 144     107.540 132.642  57.944  1.00 13.28           O  
-ATOM   1185  CB  ALA A 144     106.468 133.641  60.955  1.00 11.34           C  
-ATOM   1186  N   ASP A 145     108.891 132.331  59.730  1.00 14.96           N  
-ATOM   1187  CA  ASP A 145     109.573 131.170  59.175  1.00 16.27           C  
-ATOM   1188  C   ASP A 145     110.228 131.486  57.823  1.00 15.42           C  
-ATOM   1189  O   ASP A 145     110.070 130.756  56.841  1.00 15.28           O  
-ATOM   1190  CB  ASP A 145     108.579 130.019  59.045  1.00 20.61           C  
-ATOM   1191  CG  ASP A 145     109.252 128.704  58.770  1.00 24.67           C  
-ATOM   1192  OD1 ASP A 145     108.614 127.829  58.139  1.00 28.52           O  
-ATOM   1193  OD2 ASP A 145     110.413 128.544  59.193  1.00 27.02           O  
-ATOM   1194  N   PHE A 146     110.977 132.583  57.789  1.00 14.73           N  
-ATOM   1195  CA  PHE A 146     111.696 132.985  56.584  1.00 14.76           C  
-ATOM   1196  C   PHE A 146     112.664 131.849  56.175  1.00 17.41           C  
-ATOM   1197  O   PHE A 146     113.191 131.146  57.042  1.00 16.16           O  
-ATOM   1198  CB  PHE A 146     112.481 134.256  56.875  1.00 14.01           C  
-ATOM   1199  CG  PHE A 146     111.616 135.489  56.987  1.00 13.83           C  
-ATOM   1200  CD1 PHE A 146     111.609 136.429  55.968  1.00 13.75           C  
-ATOM   1201  CD2 PHE A 146     110.783 135.687  58.084  1.00 13.66           C  
-ATOM   1202  CE1 PHE A 146     110.780 137.565  56.026  1.00 14.82           C  
-ATOM   1203  CE2 PHE A 146     109.953 136.822  58.139  1.00 13.13           C  
-ATOM   1204  CZ  PHE A 146     109.961 137.750  57.107  1.00 12.28           C  
-ATOM   1205  N   GLY A 147     112.898 131.693  54.871  1.00 17.54           N  
-ATOM   1206  CA  GLY A 147     113.775 130.631  54.383  1.00 21.17           C  
-ATOM   1207  C   GLY A 147     115.261 130.952  54.365  1.00 24.59           C  
-ATOM   1208  O   GLY A 147     116.018 130.449  53.534  1.00 25.74           O  
-ATOM   1209  N   LEU A 148     115.685 131.749  55.329  1.00 26.35           N  
-ATOM   1210  CA  LEU A 148     117.062 132.202  55.431  1.00 29.37           C  
-ATOM   1211  C   LEU A 148     118.155 131.139  55.593  1.00 30.57           C  
-ATOM   1212  O   LEU A 148     119.141 131.165  54.864  1.00 30.52           O  
-ATOM   1213  CB  LEU A 148     117.160 133.210  56.578  1.00 29.20           C  
-ATOM   1214  CG  LEU A 148     118.206 134.318  56.444  1.00 29.69           C  
-ATOM   1215  CD1 LEU A 148     117.998 135.081  55.152  1.00 30.54           C  
-ATOM   1216  CD2 LEU A 148     118.074 135.265  57.640  1.00 29.00           C  
-ATOM   1217  N   ALA A 149     117.975 130.228  56.549  1.00 31.87           N  
-ATOM   1218  CA  ALA A 149     118.947 129.168  56.844  1.00 34.49           C  
-ATOM   1219  C   ALA A 149     119.328 128.262  55.672  1.00 36.54           C  
-ATOM   1220  O   ALA A 149     120.506 127.947  55.478  1.00 37.01           O  
-ATOM   1221  CB  ALA A 149     118.436 128.308  57.998  1.00 34.18           C  
-ATOM   1222  N   ARG A 150     118.337 127.832  54.900  1.00 38.36           N  
-ATOM   1223  CA  ARG A 150     118.602 126.958  53.764  1.00 40.80           C  
-ATOM   1224  C   ARG A 150     119.096 127.750  52.548  1.00 41.25           C  
-ATOM   1225  O   ARG A 150     119.779 127.210  51.675  1.00 40.79           O  
-ATOM   1226  CB  ARG A 150     117.335 126.170  53.408  1.00 43.10           C  
-ATOM   1227  CG  ARG A 150     117.554 125.061  52.378  1.00 47.16           C  
-ATOM   1228  CD  ARG A 150     116.317 124.175  52.226  1.00 49.60           C  
-ATOM   1229  NE  ARG A 150     115.177 124.899  51.662  1.00 52.34           N  
-ATOM   1230  CZ  ARG A 150     115.136 125.401  50.429  1.00 54.25           C  
-ATOM   1231  NH1 ARG A 150     116.178 125.263  49.611  1.00 55.10           N  
-ATOM   1232  NH2 ARG A 150     114.046 126.039  50.007  1.00 54.81           N  
-ATOM   1233  N   ALA A 151     118.757 129.038  52.510  1.00 41.64           N  
-ATOM   1234  CA  ALA A 151     119.143 129.912  51.406  1.00 42.09           C  
-ATOM   1235  C   ALA A 151     120.605 130.342  51.445  1.00 42.22           C  
-ATOM   1236  O   ALA A 151     121.241 130.483  50.400  1.00 42.79           O  
-ATOM   1237  CB  ALA A 151     118.248 131.145  51.391  1.00 41.46           C  
-ATOM   1238  N   PHE A 152     121.136 130.550  52.646  1.00 42.49           N  
-ATOM   1239  CA  PHE A 152     122.517 130.987  52.798  1.00 42.99           C  
-ATOM   1240  C   PHE A 152     123.371 129.998  53.592  1.00 43.92           C  
-ATOM   1241  O   PHE A 152     124.430 130.354  54.114  1.00 44.21           O  
-ATOM   1242  CB  PHE A 152     122.531 132.371  53.452  1.00 42.35           C  
-ATOM   1243  CG  PHE A 152     121.773 133.403  52.667  1.00 41.80           C  
-ATOM   1244  CD1 PHE A 152     122.293 133.907  51.478  1.00 42.19           C  
-ATOM   1245  CD2 PHE A 152     120.514 133.823  53.080  1.00 42.51           C  
-ATOM   1246  CE1 PHE A 152     121.570 134.814  50.705  1.00 42.30           C  
-ATOM   1247  CE2 PHE A 152     119.773 134.731  52.316  1.00 42.04           C  
-ATOM   1248  CZ  PHE A 152     120.303 135.228  51.123  1.00 42.48           C  
-ATOM   1249  N   GLY A 153     122.896 128.758  53.675  1.00 44.69           N  
-ATOM   1250  CA  GLY A 153     123.621 127.716  54.382  1.00 46.21           C  
-ATOM   1251  C   GLY A 153     123.985 128.000  55.830  1.00 47.57           C  
-ATOM   1252  O   GLY A 153     125.142 127.835  56.222  1.00 47.12           O  
-ATOM   1253  N   VAL A 154     123.016 128.431  56.632  1.00 48.76           N  
-ATOM   1254  CA  VAL A 154     123.285 128.696  58.042  1.00 50.12           C  
-ATOM   1255  C   VAL A 154     123.520 127.359  58.741  1.00 51.52           C  
-ATOM   1256  O   VAL A 154     122.798 126.386  58.501  1.00 50.64           O  
-ATOM   1257  CB  VAL A 154     122.106 129.428  58.726  1.00 49.83           C  
-ATOM   1258  CG1 VAL A 154     122.297 129.436  60.242  1.00 49.33           C  
-ATOM   1259  CG2 VAL A 154     122.019 130.854  58.210  1.00 49.79           C  
-ATOM   1260  N   PRO A 155     124.545 127.293  59.608  1.00 52.82           N  
-ATOM   1261  CA  PRO A 155     124.863 126.061  60.333  1.00 54.13           C  
-ATOM   1262  C   PRO A 155     123.815 125.715  61.391  1.00 55.21           C  
-ATOM   1263  O   PRO A 155     124.006 125.973  62.583  1.00 55.45           O  
-ATOM   1264  CB  PRO A 155     126.234 126.365  60.934  1.00 53.99           C  
-ATOM   1265  CG  PRO A 155     126.145 127.826  61.211  1.00 53.86           C  
-ATOM   1266  CD  PRO A 155     125.493 128.367  59.957  1.00 53.20           C  
-ATOM   1267  N   VAL A 156     122.707 125.135  60.935  1.00 55.71           N  
-ATOM   1268  CA  VAL A 156     121.614 124.737  61.811  1.00 56.42           C  
-ATOM   1269  C   VAL A 156     120.723 123.764  61.042  1.00 56.70           C  
-ATOM   1270  O   VAL A 156     120.619 123.852  59.822  1.00 56.76           O  
-ATOM   1271  CB  VAL A 156     120.790 125.969  62.270  1.00 56.92           C  
-ATOM   1272  CG1 VAL A 156     120.103 126.626  61.079  1.00 56.74           C  
-ATOM   1273  CG2 VAL A 156     119.777 125.550  63.321  1.00 57.65           C  
-ATOM   1274  N   ARG A 157     120.093 122.832  61.750  1.00 57.29           N  
-ATOM   1275  CA  ARG A 157     119.229 121.835  61.115  1.00 57.98           C  
-ATOM   1276  C   ARG A 157     117.852 122.405  60.775  1.00 57.36           C  
-ATOM   1277  O   ARG A 157     117.427 123.396  61.370  1.00 57.66           O  
-ATOM   1278  CB  ARG A 157     119.074 120.627  62.041  1.00 59.33           C  
-ATOM   1279  CG  ARG A 157     118.270 119.475  61.458  1.00 60.96           C  
-ATOM   1280  CD  ARG A 157     118.994 118.789  60.303  1.00 62.24           C  
-ATOM   1281  NE  ARG A 157     118.450 117.452  60.068  1.00 62.68           N  
-ATOM   1282  CZ  ARG A 157     118.969 116.560  59.233  1.00 62.77           C  
-ATOM   1283  NH1 ARG A 157     120.057 116.854  58.533  1.00 62.80           N  
-ATOM   1284  NH2 ARG A 157     118.406 115.367  59.112  1.00 62.30           N  
-ATOM   1285  N   THR A 158     117.156 121.774  59.829  1.00 56.81           N  
-ATOM   1286  CA  THR A 158     115.830 122.239  59.420  1.00 56.85           C  
-ATOM   1287  C   THR A 158     114.847 121.138  58.988  1.00 57.48           C  
-ATOM   1288  O   THR A 158     115.248 120.013  58.687  1.00 56.84           O  
-ATOM   1289  CB  THR A 158     115.946 123.272  58.277  1.00 56.16           C  
-ATOM   1290  OG1 THR A 158     116.719 122.716  57.208  1.00 55.18           O  
-ATOM   1291  CG2 THR A 158     116.618 124.550  58.774  1.00 55.49           C  
-ATOM   1292  N   TYR A 159     113.561 121.498  58.957  1.00 57.97           N  
-ATOM   1293  CA  TYR A 159     112.444 120.611  58.591  1.00 58.52           C  
-ATOM   1294  C   TYR A 159     112.323 119.398  59.506  1.00 60.22           C  
-ATOM   1295  O   TYR A 159     112.411 118.251  59.059  1.00 60.80           O  
-ATOM   1296  CB  TYR A 159     112.551 120.138  57.132  1.00 56.96           C  
-ATOM   1297  CG  TYR A 159     112.545 121.255  56.114  1.00 54.78           C  
-ATOM   1298  CD1 TYR A 159     111.427 122.075  55.947  1.00 53.20           C  
-ATOM   1299  CD2 TYR A 159     113.678 121.508  55.335  1.00 53.64           C  
-ATOM   1300  CE1 TYR A 159     111.439 123.128  55.033  1.00 52.87           C  
-ATOM   1301  CE2 TYR A 159     113.705 122.562  54.418  1.00 53.22           C  
-ATOM   1302  CZ  TYR A 159     112.586 123.370  54.278  1.00 53.23           C  
-ATOM   1303  OH  TYR A 159     112.632 124.462  53.427  1.00 53.83           O  
-ATOM   1304  N   THR A 160     112.108 119.672  60.790  1.00 62.01           N  
-ATOM   1305  CA  THR A 160     111.963 118.641  61.820  1.00 63.34           C  
-ATOM   1306  C   THR A 160     110.814 117.658  61.565  1.00 64.22           C  
-ATOM   1307  O   THR A 160     110.845 116.518  62.042  1.00 64.10           O  
-ATOM   1308  CB  THR A 160     111.733 119.290  63.206  1.00 63.08           C  
-ATOM   1309  OG1 THR A 160     111.507 118.269  64.187  1.00 62.95           O  
-ATOM   1310  CG2 THR A 160     110.522 120.221  63.161  1.00 62.66           C  
-ATOM   1311  N   HIS A 161     109.802 118.101  60.822  1.00 65.41           N  
-ATOM   1312  CA  HIS A 161     108.646 117.258  60.533  1.00 66.59           C  
-ATOM   1313  C   HIS A 161     108.635 116.660  59.126  1.00 66.29           C  
-ATOM   1314  O   HIS A 161     108.365 115.469  58.963  1.00 66.44           O  
-ATOM   1315  CB  HIS A 161     107.346 118.037  60.796  1.00 68.35           C  
-ATOM   1316  CG  HIS A 161     107.281 119.375  60.122  1.00 70.27           C  
-ATOM   1317  ND1 HIS A 161     108.299 120.302  60.200  1.00 71.02           N  
-ATOM   1318  CD2 HIS A 161     106.298 119.958  59.394  1.00 70.95           C  
-ATOM   1319  CE1 HIS A 161     107.946 121.397  59.550  1.00 71.45           C  
-ATOM   1320  NE2 HIS A 161     106.736 121.214  59.052  1.00 71.37           N  
-ATOM   1321  N   GLU A 162     108.919 117.482  58.118  1.00 65.72           N  
-ATOM   1322  CA  GLU A 162     108.957 117.025  56.727  1.00 64.82           C  
-ATOM   1323  C   GLU A 162     108.976 118.187  55.738  1.00 63.10           C  
-ATOM   1324  O   GLU A 162     109.537 119.246  56.028  1.00 63.62           O  
-ATOM   1325  CB  GLU A 162     107.775 116.088  56.423  1.00 66.12           C  
-ATOM   1326  CG  GLU A 162     106.387 116.630  56.764  1.00 67.58           C  
-ATOM   1327  CD  GLU A 162     105.301 115.556  56.668  1.00 68.51           C  
-ATOM   1328  OE1 GLU A 162     105.157 114.944  55.587  1.00 68.35           O  
-ATOM   1329  OE2 GLU A 162     104.592 115.323  57.674  1.00 68.67           O  
-ATOM   1330  N   VAL A 163     108.367 117.990  54.571  1.00 60.68           N  
-ATOM   1331  CA  VAL A 163     108.342 119.029  53.547  1.00 57.14           C  
-ATOM   1332  C   VAL A 163     107.037 119.053  52.742  1.00 55.01           C  
-ATOM   1333  O   VAL A 163     106.231 118.121  52.812  1.00 54.70           O  
-ATOM   1334  CB  VAL A 163     109.556 118.864  52.588  1.00 57.07           C  
-ATOM   1335  CG1 VAL A 163     109.574 117.465  52.017  1.00 56.54           C  
-ATOM   1336  CG2 VAL A 163     109.515 119.916  51.479  1.00 56.23           C  
-ATOM   1337  N   VAL A 164     106.849 120.140  51.990  1.00 51.74           N  
-ATOM   1338  CA  VAL A 164     105.673 120.382  51.149  1.00 47.32           C  
-ATOM   1339  C   VAL A 164     105.957 121.744  50.500  1.00 43.85           C  
-ATOM   1340  O   VAL A 164     105.092 122.379  49.886  1.00 42.81           O  
-ATOM   1341  CB  VAL A 164     104.401 120.504  52.009  1.00 48.09           C  
-ATOM   1342  CG1 VAL A 164     104.325 121.888  52.646  1.00 48.32           C  
-ATOM   1343  CG2 VAL A 164     103.183 120.230  51.173  1.00 49.38           C  
-ATOM   1344  N   THR A 165     107.202 122.170  50.660  1.00 39.35           N  
-ATOM   1345  CA  THR A 165     107.693 123.451  50.166  1.00 34.73           C  
-ATOM   1346  C   THR A 165     107.606 123.645  48.658  1.00 30.85           C  
-ATOM   1347  O   THR A 165     107.520 124.795  48.161  1.00 29.53           O  
-ATOM   1348  CB  THR A 165     109.147 123.635  50.623  1.00 37.19           C  
-ATOM   1349  OG1 THR A 165     109.216 123.414  52.038  1.00 38.36           O  
-ATOM   1350  CG2 THR A 165     109.644 125.032  50.304  1.00 36.32           C  
-ATOM   1351  N   LEU A 166     107.602 122.533  47.927  1.00 25.17           N  
-ATOM   1352  CA  LEU A 166     107.545 122.613  46.481  1.00 20.57           C  
-ATOM   1353  C   LEU A 166     106.304 123.290  45.930  1.00 17.33           C  
-ATOM   1354  O   LEU A 166     106.380 123.930  44.892  1.00 14.32           O  
-ATOM   1355  CB  LEU A 166     107.634 121.224  45.847  1.00 22.16           C  
-ATOM   1356  CG  LEU A 166     108.916 120.428  46.084  1.00 23.92           C  
-ATOM   1357  CD1 LEU A 166     108.792 119.048  45.432  1.00 26.96           C  
-ATOM   1358  CD2 LEU A 166     110.087 121.204  45.523  1.00 24.53           C  
-ATOM   1359  N   TRP A 167     105.167 123.137  46.615  1.00 13.26           N  
-ATOM   1360  CA  TRP A 167     103.909 123.669  46.103  1.00 13.17           C  
-ATOM   1361  C   TRP A 167     103.886 125.159  45.820  1.00 11.64           C  
-ATOM   1362  O   TRP A 167     103.118 125.620  44.979  1.00 13.26           O  
-ATOM   1363  CB  TRP A 167     102.761 123.360  47.060  1.00 13.79           C  
-ATOM   1364  CG  TRP A 167     102.576 121.907  47.403  1.00 15.68           C  
-ATOM   1365  CD1 TRP A 167     103.282 120.829  46.913  1.00 15.71           C  
-ATOM   1366  CD2 TRP A 167     101.588 121.373  48.293  1.00 17.29           C  
-ATOM   1367  NE1 TRP A 167     102.778 119.655  47.450  1.00 15.79           N  
-ATOM   1368  CE2 TRP A 167     101.740 119.965  48.297  1.00 17.53           C  
-ATOM   1369  CE3 TRP A 167     100.578 121.951  49.082  1.00 16.66           C  
-ATOM   1370  CZ2 TRP A 167     100.909 119.122  49.071  1.00 18.63           C  
-ATOM   1371  CZ3 TRP A 167      99.755 121.117  49.844  1.00 18.13           C  
-ATOM   1372  CH2 TRP A 167      99.927 119.721  49.829  1.00 18.11           C  
-ATOM   1373  N   TYR A 168     104.709 125.913  46.535  1.00 10.39           N  
-ATOM   1374  CA  TYR A 168     104.710 127.361  46.360  1.00 11.42           C  
-ATOM   1375  C   TYR A 168     105.950 127.905  45.661  1.00 11.51           C  
-ATOM   1376  O   TYR A 168     106.108 129.122  45.564  1.00 11.10           O  
-ATOM   1377  CB  TYR A 168     104.564 128.001  47.745  1.00 11.57           C  
-ATOM   1378  CG  TYR A 168     103.360 127.456  48.465  1.00 11.14           C  
-ATOM   1379  CD1 TYR A 168     102.087 127.973  48.234  1.00 12.13           C  
-ATOM   1380  CD2 TYR A 168     103.483 126.361  49.312  1.00 13.40           C  
-ATOM   1381  CE1 TYR A 168     100.949 127.387  48.835  1.00 11.92           C  
-ATOM   1382  CE2 TYR A 168     102.367 125.784  49.905  1.00 13.29           C  
-ATOM   1383  CZ  TYR A 168     101.119 126.297  49.662  1.00 12.62           C  
-ATOM   1384  OH  TYR A 168     100.063 125.699  50.275  1.00 14.59           O  
-ATOM   1385  N   ARG A 169     106.815 127.009  45.179  1.00 12.31           N  
-ATOM   1386  CA  ARG A 169     108.081 127.410  44.536  1.00 12.35           C  
-ATOM   1387  C   ARG A 169     107.910 127.967  43.125  1.00 12.05           C  
-ATOM   1388  O   ARG A 169     107.273 127.343  42.282  1.00 11.70           O  
-ATOM   1389  CB  ARG A 169     109.052 126.214  44.518  1.00 13.39           C  
-ATOM   1390  CG  ARG A 169     110.397 126.486  43.907  1.00 17.50           C  
-ATOM   1391  CD  ARG A 169     111.347 125.308  44.128  1.00 19.76           C  
-ATOM   1392  NE  ARG A 169     111.636 125.102  45.543  1.00 24.94           N  
-ATOM   1393  CZ  ARG A 169     112.510 124.213  46.015  1.00 28.87           C  
-ATOM   1394  NH1 ARG A 169     113.196 123.432  45.182  1.00 29.39           N  
-ATOM   1395  NH2 ARG A 169     112.703 124.104  47.325  1.00 29.91           N  
-ATOM   1396  N   ALA A 170     108.497 129.145  42.885  1.00 10.87           N  
-ATOM   1397  CA  ALA A 170     108.430 129.813  41.577  1.00 11.10           C  
-ATOM   1398  C   ALA A 170     109.082 128.974  40.475  1.00 10.44           C  
-ATOM   1399  O   ALA A 170     110.072 128.284  40.698  1.00 10.03           O  
-ATOM   1400  CB  ALA A 170     109.094 131.190  41.649  1.00 12.23           C  
-ATOM   1401  N   PRO A 171     108.532 129.047  39.261  1.00 11.10           N  
-ATOM   1402  CA  PRO A 171     109.071 128.268  38.139  1.00 11.95           C  
-ATOM   1403  C   PRO A 171     110.503 128.569  37.759  1.00 11.11           C  
-ATOM   1404  O   PRO A 171     111.216 127.667  37.302  1.00 11.69           O  
-ATOM   1405  CB  PRO A 171     108.056 128.526  37.016  1.00 11.53           C  
-ATOM   1406  CG  PRO A 171     107.547 129.927  37.337  1.00 13.28           C  
-ATOM   1407  CD  PRO A 171     107.376 129.859  38.845  1.00 11.08           C  
-ATOM   1408  N   GLU A 172     110.948 129.814  37.936  1.00 11.31           N  
-ATOM   1409  CA  GLU A 172     112.344 130.118  37.616  1.00 11.31           C  
-ATOM   1410  C   GLU A 172     113.307 129.342  38.543  1.00 12.79           C  
-ATOM   1411  O   GLU A 172     114.422 129.018  38.142  1.00 13.52           O  
-ATOM   1412  CB  GLU A 172     112.619 131.629  37.667  1.00 12.16           C  
-ATOM   1413  CG  GLU A 172     112.331 132.308  39.020  1.00 11.39           C  
-ATOM   1414  CD  GLU A 172     110.927 132.894  39.131  1.00 12.13           C  
-ATOM   1415  OE1 GLU A 172     109.973 132.292  38.573  1.00 11.62           O  
-ATOM   1416  OE2 GLU A 172     110.784 133.967  39.794  1.00 12.99           O  
-ATOM   1417  N   ILE A 173     112.881 129.040  39.770  1.00 13.18           N  
-ATOM   1418  CA  ILE A 173     113.720 128.271  40.701  1.00 12.62           C  
-ATOM   1419  C   ILE A 173     113.705 126.806  40.249  1.00 13.63           C  
-ATOM   1420  O   ILE A 173     114.752 126.126  40.223  1.00 12.22           O  
-ATOM   1421  CB  ILE A 173     113.186 128.351  42.170  1.00 15.45           C  
-ATOM   1422  CG1 ILE A 173     113.256 129.790  42.692  1.00 16.30           C  
-ATOM   1423  CG2 ILE A 173     114.021 127.451  43.091  1.00 14.92           C  
-ATOM   1424  CD1 ILE A 173     112.539 129.943  44.034  1.00 19.59           C  
-ATOM   1425  N   LEU A 174     112.520 126.312  39.895  1.00 12.70           N  
-ATOM   1426  CA  LEU A 174     112.400 124.922  39.441  1.00 13.33           C  
-ATOM   1427  C   LEU A 174     113.216 124.685  38.163  1.00 13.58           C  
-ATOM   1428  O   LEU A 174     113.660 123.566  37.906  1.00 13.91           O  
-ATOM   1429  CB  LEU A 174     110.936 124.565  39.166  1.00 13.27           C  
-ATOM   1430  CG  LEU A 174     110.051 124.559  40.415  1.00 13.72           C  
-ATOM   1431  CD1 LEU A 174     108.567 124.544  39.999  1.00 14.70           C  
-ATOM   1432  CD2 LEU A 174     110.423 123.352  41.288  1.00 14.08           C  
-ATOM   1433  N   LEU A 175     113.412 125.737  37.373  1.00 12.56           N  
-ATOM   1434  CA  LEU A 175     114.150 125.628  36.111  1.00 13.09           C  
-ATOM   1435  C   LEU A 175     115.639 125.937  36.239  1.00 14.66           C  
-ATOM   1436  O   LEU A 175     116.354 126.018  35.230  1.00 15.47           O  
-ATOM   1437  CB  LEU A 175     113.515 126.521  35.048  1.00 13.05           C  
-ATOM   1438  CG  LEU A 175     112.155 126.068  34.521  1.00 12.00           C  
-ATOM   1439  CD1 LEU A 175     111.561 127.097  33.562  1.00 13.58           C  
-ATOM   1440  CD2 LEU A 175     112.339 124.727  33.804  1.00 13.70           C  
-ATOM   1441  N   GLY A 176     116.080 126.128  37.479  1.00 16.25           N  
-ATOM   1442  CA  GLY A 176     117.487 126.353  37.778  1.00 18.46           C  
-ATOM   1443  C   GLY A 176     118.109 127.714  37.529  1.00 19.93           C  
-ATOM   1444  O   GLY A 176     119.321 127.783  37.317  1.00 20.67           O  
-ATOM   1445  N   CYS A 177     117.318 128.785  37.570  1.00 19.53           N  
-ATOM   1446  CA  CYS A 177     117.842 130.141  37.339  1.00 21.22           C  
-ATOM   1447  C   CYS A 177     119.096 130.369  38.168  1.00 21.78           C  
-ATOM   1448  O   CYS A 177     119.173 129.925  39.303  1.00 22.12           O  
-ATOM   1449  CB  CYS A 177     116.798 131.198  37.720  1.00 21.19           C  
-ATOM   1450  SG  CYS A 177     116.223 131.122  39.455  1.00 24.65           S  
-ATOM   1451  N   LYS A 178     120.077 131.058  37.589  1.00 23.57           N  
-ATOM   1452  CA  LYS A 178     121.318 131.335  38.283  1.00 23.95           C  
-ATOM   1453  C   LYS A 178     121.036 132.212  39.500  1.00 23.02           C  
-ATOM   1454  O   LYS A 178     121.502 131.939  40.609  1.00 22.14           O  
-ATOM   1455  CB  LYS A 178     122.292 132.044  37.350  1.00 26.53           C  
-ATOM   1456  CG  LYS A 178     123.627 132.369  38.004  1.00 29.15           C  
-ATOM   1457  CD  LYS A 178     124.528 133.110  37.038  1.00 32.15           C  
-ATOM   1458  CE  LYS A 178     125.927 133.313  37.598  1.00 32.61           C  
-ATOM   1459  NZ  LYS A 178     126.726 134.185  36.678  1.00 31.93           N  
-ATOM   1460  N   TYR A 179     120.243 133.249  39.270  1.00 21.95           N  
-ATOM   1461  CA  TYR A 179     119.850 134.201  40.299  1.00 21.25           C  
-ATOM   1462  C   TYR A 179     118.344 134.374  40.239  1.00 20.76           C  
-ATOM   1463  O   TYR A 179     117.789 134.592  39.161  1.00 21.71           O  
-ATOM   1464  CB  TYR A 179     120.475 135.575  40.043  1.00 21.16           C  
-ATOM   1465  CG  TYR A 179     121.958 135.658  40.284  1.00 21.24           C  
-ATOM   1466  CD1 TYR A 179     122.467 135.659  41.578  1.00 23.33           C  
-ATOM   1467  CD2 TYR A 179     122.854 135.735  39.214  1.00 23.96           C  
-ATOM   1468  CE1 TYR A 179     123.834 135.729  41.809  1.00 24.64           C  
-ATOM   1469  CE2 TYR A 179     124.226 135.812  39.432  1.00 23.91           C  
-ATOM   1470  CZ  TYR A 179     124.707 135.807  40.727  1.00 25.41           C  
-ATOM   1471  OH  TYR A 179     126.064 135.884  40.957  1.00 26.85           O  
-ATOM   1472  N   TYR A 180     117.680 134.253  41.380  1.00 21.70           N  
-ATOM   1473  CA  TYR A 180     116.238 134.475  41.404  1.00 20.74           C  
-ATOM   1474  C   TYR A 180     116.071 135.888  41.952  1.00 19.55           C  
-ATOM   1475  O   TYR A 180     117.066 136.516  42.330  1.00 18.95           O  
-ATOM   1476  CB  TYR A 180     115.524 133.438  42.274  1.00 22.82           C  
-ATOM   1477  CG  TYR A 180     116.086 133.254  43.661  1.00 24.47           C  
-ATOM   1478  CD1 TYR A 180     115.573 133.958  44.749  1.00 24.60           C  
-ATOM   1479  CD2 TYR A 180     117.092 132.326  43.896  1.00 24.71           C  
-ATOM   1480  CE1 TYR A 180     116.048 133.725  46.045  1.00 24.78           C  
-ATOM   1481  CE2 TYR A 180     117.577 132.090  45.170  1.00 27.01           C  
-ATOM   1482  CZ  TYR A 180     117.049 132.785  46.247  1.00 26.04           C  
-ATOM   1483  OH  TYR A 180     117.502 132.492  47.514  1.00 26.82           O  
-ATOM   1484  N   SER A 181     114.830 136.378  42.015  1.00 17.09           N  
-ATOM   1485  CA  SER A 181     114.563 137.754  42.458  1.00 15.46           C  
-ATOM   1486  C   SER A 181     113.421 137.828  43.470  1.00 14.59           C  
-ATOM   1487  O   SER A 181     112.866 136.815  43.856  1.00 15.24           O  
-ATOM   1488  CB  SER A 181     114.177 138.611  41.259  1.00 15.26           C  
-ATOM   1489  OG  SER A 181     112.859 138.240  40.793  1.00 17.04           O  
-ATOM   1490  N   THR A 182     113.080 139.039  43.903  1.00 12.39           N  
-ATOM   1491  CA  THR A 182     111.969 139.199  44.850  1.00 12.87           C  
-ATOM   1492  C   THR A 182     110.676 138.642  44.269  1.00 11.25           C  
-ATOM   1493  O   THR A 182     109.728 138.366  45.017  1.00 12.74           O  
-ATOM   1494  CB  THR A 182     111.713 140.681  45.178  1.00 12.59           C  
-ATOM   1495  OG1 THR A 182     111.588 141.416  43.955  1.00 13.55           O  
-ATOM   1496  CG2 THR A 182     112.875 141.250  46.010  1.00 14.21           C  
-ATOM   1497  N   ALA A 183     110.620 138.494  42.944  1.00 10.63           N  
-ATOM   1498  CA  ALA A 183     109.408 137.962  42.293  1.00 11.30           C  
-ATOM   1499  C   ALA A 183     109.037 136.565  42.773  1.00 10.15           C  
-ATOM   1500  O   ALA A 183     107.878 136.144  42.642  1.00 10.73           O  
-ATOM   1501  CB  ALA A 183     109.591 137.944  40.768  1.00 13.09           C  
-ATOM   1502  N   VAL A 184     110.006 135.814  43.304  1.00 10.53           N  
-ATOM   1503  CA  VAL A 184     109.663 134.466  43.754  1.00  9.22           C  
-ATOM   1504  C   VAL A 184     108.639 134.501  44.878  1.00  9.10           C  
-ATOM   1505  O   VAL A 184     107.819 133.592  44.989  1.00 10.05           O  
-ATOM   1506  CB  VAL A 184     110.907 133.611  44.229  1.00  8.70           C  
-ATOM   1507  CG1 VAL A 184     111.941 133.472  43.074  1.00  9.22           C  
-ATOM   1508  CG2 VAL A 184     111.562 134.228  45.456  1.00  9.83           C  
-ATOM   1509  N   ASP A 185     108.677 135.541  45.719  1.00  9.46           N  
-ATOM   1510  CA  ASP A 185     107.715 135.628  46.821  1.00  9.81           C  
-ATOM   1511  C   ASP A 185     106.317 135.967  46.305  1.00  9.27           C  
-ATOM   1512  O   ASP A 185     105.301 135.534  46.875  1.00  9.93           O  
-ATOM   1513  CB  ASP A 185     108.141 136.691  47.853  1.00  9.71           C  
-ATOM   1514  CG  ASP A 185     109.320 136.252  48.709  1.00 12.63           C  
-ATOM   1515  OD1 ASP A 185     109.533 135.019  48.898  1.00 12.15           O  
-ATOM   1516  OD2 ASP A 185     110.013 137.162  49.222  1.00 13.31           O  
-ATOM   1517  N   ILE A 186     106.248 136.736  45.226  1.00 10.47           N  
-ATOM   1518  CA  ILE A 186     104.944 137.114  44.667  1.00  9.65           C  
-ATOM   1519  C   ILE A 186     104.267 135.863  44.076  1.00 11.12           C  
-ATOM   1520  O   ILE A 186     103.047 135.683  44.189  1.00  9.29           O  
-ATOM   1521  CB  ILE A 186     105.092 138.187  43.573  1.00 12.11           C  
-ATOM   1522  CG1 ILE A 186     105.750 139.443  44.165  1.00 13.03           C  
-ATOM   1523  CG2 ILE A 186     103.721 138.502  42.958  1.00 12.41           C  
-ATOM   1524  CD1 ILE A 186     105.007 140.038  45.339  1.00 13.96           C  
-ATOM   1525  N   TRP A 187     105.062 135.020  43.425  1.00  9.89           N  
-ATOM   1526  CA  TRP A 187     104.531 133.769  42.888  1.00 10.37           C  
-ATOM   1527  C   TRP A 187     103.931 132.961  44.038  1.00 11.19           C  
-ATOM   1528  O   TRP A 187     102.787 132.520  43.969  1.00 10.11           O  
-ATOM   1529  CB  TRP A 187     105.642 132.942  42.215  1.00 10.46           C  
-ATOM   1530  CG  TRP A 187     105.157 131.571  41.786  1.00  9.84           C  
-ATOM   1531  CD1 TRP A 187     105.053 130.437  42.558  1.00 11.46           C  
-ATOM   1532  CD2 TRP A 187     104.683 131.223  40.487  1.00 10.84           C  
-ATOM   1533  NE1 TRP A 187     104.534 129.398  41.797  1.00 11.34           N  
-ATOM   1534  CE2 TRP A 187     104.303 129.859  40.526  1.00 10.13           C  
-ATOM   1535  CE3 TRP A 187     104.545 131.941  39.278  1.00 11.63           C  
-ATOM   1536  CZ2 TRP A 187     103.790 129.191  39.399  1.00 11.11           C  
-ATOM   1537  CZ3 TRP A 187     104.040 131.280  38.154  1.00 11.89           C  
-ATOM   1538  CH2 TRP A 187     103.666 129.913  38.227  1.00 11.63           C  
-ATOM   1539  N   SER A 188     104.708 132.756  45.100  1.00  9.19           N  
-ATOM   1540  CA  SER A 188     104.215 132.002  46.251  1.00 10.38           C  
-ATOM   1541  C   SER A 188     102.911 132.579  46.788  1.00 10.08           C  
-ATOM   1542  O   SER A 188     101.957 131.847  47.105  1.00 11.08           O  
-ATOM   1543  CB  SER A 188     105.251 132.005  47.382  1.00  9.96           C  
-ATOM   1544  OG  SER A 188     106.488 131.484  46.940  1.00 10.48           O  
-ATOM   1545  N   LEU A 189     102.863 133.897  46.911  1.00 10.57           N  
-ATOM   1546  CA  LEU A 189     101.654 134.515  47.444  1.00 11.18           C  
-ATOM   1547  C   LEU A 189     100.477 134.340  46.495  1.00 11.17           C  
-ATOM   1548  O   LEU A 189      99.340 134.170  46.948  1.00 11.38           O  
-ATOM   1549  CB  LEU A 189     101.902 136.001  47.726  1.00 13.19           C  
-ATOM   1550  CG  LEU A 189     100.758 136.707  48.449  1.00 13.07           C  
-ATOM   1551  CD1 LEU A 189     100.376 135.934  49.695  1.00 13.34           C  
-ATOM   1552  CD2 LEU A 189     101.227 138.131  48.810  1.00 15.02           C  
-ATOM   1553  N   GLY A 190     100.737 134.386  45.189  1.00 10.92           N  
-ATOM   1554  CA  GLY A 190      99.662 134.182  44.230  1.00 11.56           C  
-ATOM   1555  C   GLY A 190      99.092 132.772  44.430  1.00 12.22           C  
-ATOM   1556  O   GLY A 190      97.886 132.578  44.331  1.00 11.29           O  
-ATOM   1557  N   CYS A 191      99.956 131.782  44.707  1.00 10.47           N  
-ATOM   1558  CA  CYS A 191      99.483 130.415  44.927  1.00 11.26           C  
-ATOM   1559  C   CYS A 191      98.631 130.369  46.189  1.00 11.67           C  
-ATOM   1560  O   CYS A 191      97.601 129.664  46.257  1.00 11.84           O  
-ATOM   1561  CB  CYS A 191     100.641 129.430  45.107  1.00 11.60           C  
-ATOM   1562  SG  CYS A 191     101.642 129.169  43.623  1.00 11.88           S  
-ATOM   1563  N   ILE A 192      99.047 131.139  47.184  1.00 10.05           N  
-ATOM   1564  CA  ILE A 192      98.321 131.171  48.452  1.00 11.75           C  
-ATOM   1565  C   ILE A 192      96.962 131.854  48.263  1.00 10.67           C  
-ATOM   1566  O   ILE A 192      95.969 131.402  48.834  1.00 10.28           O  
-ATOM   1567  CB  ILE A 192      99.181 131.870  49.575  1.00 11.11           C  
-ATOM   1568  CG1 ILE A 192     100.391 130.987  49.896  1.00 11.86           C  
-ATOM   1569  CG2 ILE A 192      98.352 132.048  50.857  1.00 14.08           C  
-ATOM   1570  CD1 ILE A 192     101.406 131.588  50.871  1.00 14.33           C  
-ATOM   1571  N   PHE A 193      96.923 132.907  47.438  1.00 11.16           N  
-ATOM   1572  CA  PHE A 193      95.676 133.633  47.123  1.00 11.87           C  
-ATOM   1573  C   PHE A 193      94.667 132.627  46.516  1.00 11.81           C  
-ATOM   1574  O   PHE A 193      93.517 132.485  46.979  1.00 10.91           O  
-ATOM   1575  CB  PHE A 193      96.043 134.773  46.138  1.00 10.57           C  
-ATOM   1576  CG  PHE A 193      94.881 135.566  45.593  1.00 12.34           C  
-ATOM   1577  CD1 PHE A 193      93.652 135.600  46.240  1.00 13.06           C  
-ATOM   1578  CD2 PHE A 193      95.045 136.317  44.438  1.00 13.82           C  
-ATOM   1579  CE1 PHE A 193      92.606 136.370  45.741  1.00 14.11           C  
-ATOM   1580  CE2 PHE A 193      94.007 137.097  43.925  1.00 13.90           C  
-ATOM   1581  CZ  PHE A 193      92.779 137.117  44.588  1.00 15.06           C  
-ATOM   1582  N   ALA A 194      95.119 131.894  45.503  1.00 11.82           N  
-ATOM   1583  CA  ALA A 194      94.274 130.903  44.844  1.00 13.71           C  
-ATOM   1584  C   ALA A 194      93.773 129.827  45.830  1.00 12.75           C  
-ATOM   1585  O   ALA A 194      92.644 129.376  45.742  1.00 13.16           O  
-ATOM   1586  CB  ALA A 194      95.064 130.229  43.712  1.00 13.91           C  
-ATOM   1587  N   GLU A 195      94.631 129.430  46.762  1.00 12.41           N  
-ATOM   1588  CA  GLU A 195      94.308 128.393  47.734  1.00 12.56           C  
-ATOM   1589  C   GLU A 195      93.240 128.868  48.709  1.00 12.99           C  
-ATOM   1590  O   GLU A 195      92.318 128.111  49.077  1.00 11.87           O  
-ATOM   1591  CB  GLU A 195      95.585 127.985  48.479  1.00 12.06           C  
-ATOM   1592  CG  GLU A 195      95.417 126.828  49.457  1.00 13.89           C  
-ATOM   1593  CD  GLU A 195      96.741 126.311  49.987  1.00 14.49           C  
-ATOM   1594  OE1 GLU A 195      97.802 126.622  49.378  1.00 13.23           O  
-ATOM   1595  OE2 GLU A 195      96.722 125.581  51.007  1.00 14.79           O  
-ATOM   1596  N   MET A 196      93.361 130.112  49.150  1.00 12.50           N  
-ATOM   1597  CA  MET A 196      92.354 130.640  50.057  1.00 13.91           C  
-ATOM   1598  C   MET A 196      90.988 130.660  49.367  1.00 14.35           C  
-ATOM   1599  O   MET A 196      89.966 130.326  49.976  1.00 14.98           O  
-ATOM   1600  CB  MET A 196      92.717 132.059  50.497  1.00 13.90           C  
-ATOM   1601  CG  MET A 196      93.856 132.116  51.509  1.00 14.91           C  
-ATOM   1602  SD  MET A 196      93.973 133.771  52.267  1.00 16.62           S  
-ATOM   1603  CE  MET A 196      94.829 134.663  51.011  1.00 16.48           C  
-ATOM   1604  N   VAL A 197      90.980 131.048  48.095  1.00 14.11           N  
-ATOM   1605  CA  VAL A 197      89.736 131.146  47.326  1.00 14.87           C  
-ATOM   1606  C   VAL A 197      89.078 129.804  47.000  1.00 16.08           C  
-ATOM   1607  O   VAL A 197      87.855 129.645  47.135  1.00 15.82           O  
-ATOM   1608  CB  VAL A 197      89.982 131.891  45.987  1.00 15.80           C  
-ATOM   1609  CG1 VAL A 197      88.724 131.834  45.097  1.00 16.67           C  
-ATOM   1610  CG2 VAL A 197      90.348 133.347  46.278  1.00 17.74           C  
-ATOM   1611  N   THR A 198      89.887 128.841  46.584  1.00 15.18           N  
-ATOM   1612  CA  THR A 198      89.364 127.536  46.198  1.00 16.20           C  
-ATOM   1613  C   THR A 198      89.334 126.503  47.305  1.00 16.54           C  
-ATOM   1614  O   THR A 198      88.678 125.479  47.173  1.00 16.50           O  
-ATOM   1615  CB  THR A 198      90.175 126.936  45.049  1.00 15.29           C  
-ATOM   1616  OG1 THR A 198      91.515 126.709  45.494  1.00 14.58           O  
-ATOM   1617  CG2 THR A 198      90.192 127.877  43.838  1.00 16.26           C  
-ATOM   1618  N   ARG A 199      90.069 126.776  48.379  1.00 15.48           N  
-ATOM   1619  CA  ARG A 199      90.164 125.900  49.519  1.00 16.05           C  
-ATOM   1620  C   ARG A 199      90.988 124.659  49.239  1.00 16.16           C  
-ATOM   1621  O   ARG A 199      90.825 123.643  49.901  1.00 13.69           O  
-ATOM   1622  CB  ARG A 199      88.765 125.499  50.032  1.00 18.36           C  
-ATOM   1623  CG  ARG A 199      87.840 126.672  50.295  1.00 21.44           C  
-ATOM   1624  CD  ARG A 199      86.422 126.178  50.642  1.00 24.42           C  
-ATOM   1625  NE  ARG A 199      85.405 127.041  50.055  1.00 27.90           N  
-ATOM   1626  CZ  ARG A 199      84.101 126.804  50.118  1.00 28.52           C  
-ATOM   1627  NH1 ARG A 199      83.658 125.728  50.749  1.00 29.61           N  
-ATOM   1628  NH2 ARG A 199      83.241 127.641  49.544  1.00 31.51           N  
-ATOM   1629  N   ARG A 200      91.889 124.744  48.263  1.00 13.42           N  
-ATOM   1630  CA  ARG A 200      92.764 123.619  47.977  1.00 14.56           C  
-ATOM   1631  C   ARG A 200      94.041 124.185  47.363  1.00 13.32           C  
-ATOM   1632  O   ARG A 200      93.990 125.186  46.660  1.00 13.14           O  
-ATOM   1633  CB  ARG A 200      92.106 122.645  46.989  1.00 15.54           C  
-ATOM   1634  CG  ARG A 200      92.925 121.391  46.723  1.00 16.89           C  
-ATOM   1635  CD  ARG A 200      92.275 120.510  45.640  1.00 17.62           C  
-ATOM   1636  NE  ARG A 200      93.037 119.279  45.427  1.00 18.44           N  
-ATOM   1637  CZ  ARG A 200      92.795 118.419  44.447  1.00 19.93           C  
-ATOM   1638  NH1 ARG A 200      91.801 118.654  43.598  1.00 16.73           N  
-ATOM   1639  NH2 ARG A 200      93.570 117.349  44.291  1.00 20.63           N  
-ATOM   1640  N   ALA A 201      95.172 123.549  47.640  1.00 12.86           N  
-ATOM   1641  CA  ALA A 201      96.443 124.017  47.092  1.00 13.20           C  
-ATOM   1642  C   ALA A 201      96.338 123.986  45.581  1.00 14.37           C  
-ATOM   1643  O   ALA A 201      95.716 123.090  44.998  1.00 16.37           O  
-ATOM   1644  CB  ALA A 201      97.600 123.132  47.560  1.00 14.19           C  
-ATOM   1645  N   LEU A 202      96.974 124.961  44.950  1.00 14.57           N  
-ATOM   1646  CA  LEU A 202      96.930 125.106  43.506  1.00 13.94           C  
-ATOM   1647  C   LEU A 202      97.792 124.123  42.738  1.00 14.17           C  
-ATOM   1648  O   LEU A 202      97.331 123.543  41.757  1.00 14.65           O  
-ATOM   1649  CB  LEU A 202      97.321 126.540  43.150  1.00 14.18           C  
-ATOM   1650  CG  LEU A 202      97.216 127.006  41.699  1.00 14.28           C  
-ATOM   1651  CD1 LEU A 202      95.783 126.856  41.212  1.00 13.78           C  
-ATOM   1652  CD2 LEU A 202      97.655 128.482  41.606  1.00 16.68           C  
-ATOM   1653  N   PHE A 203      99.038 123.943  43.170  1.00 13.06           N  
-ATOM   1654  CA  PHE A 203      99.987 123.037  42.484  1.00 13.75           C  
-ATOM   1655  C   PHE A 203     100.644 122.110  43.518  1.00 13.22           C  
-ATOM   1656  O   PHE A 203     101.799 122.284  43.901  1.00 13.20           O  
-ATOM   1657  CB  PHE A 203     101.073 123.854  41.767  1.00 12.91           C  
-ATOM   1658  CG  PHE A 203     100.540 124.926  40.819  1.00 14.19           C  
-ATOM   1659  CD1 PHE A 203      99.744 124.593  39.718  1.00 13.68           C  
-ATOM   1660  CD2 PHE A 203     100.889 126.268  41.009  1.00 14.40           C  
-ATOM   1661  CE1 PHE A 203      99.306 125.585  38.813  1.00 14.53           C  
-ATOM   1662  CE2 PHE A 203     100.467 127.255  40.123  1.00 14.48           C  
-ATOM   1663  CZ  PHE A 203      99.672 126.918  39.014  1.00 13.75           C  
-ATOM   1664  N   PRO A 204      99.909 121.097  43.978  1.00 14.69           N  
-ATOM   1665  CA  PRO A 204     100.459 120.176  44.979  1.00 15.40           C  
-ATOM   1666  C   PRO A 204     101.370 119.093  44.400  1.00 17.01           C  
-ATOM   1667  O   PRO A 204     100.991 117.924  44.369  1.00 17.21           O  
-ATOM   1668  CB  PRO A 204      99.200 119.593  45.629  1.00 16.17           C  
-ATOM   1669  CG  PRO A 204      98.231 119.550  44.500  1.00 15.97           C  
-ATOM   1670  CD  PRO A 204      98.473 120.846  43.740  1.00 16.31           C  
-ATOM   1671  N   GLY A 205     102.563 119.482  43.959  1.00 16.49           N  
-ATOM   1672  CA  GLY A 205     103.479 118.513  43.373  1.00 18.05           C  
-ATOM   1673  C   GLY A 205     104.200 117.660  44.395  1.00 19.04           C  
-ATOM   1674  O   GLY A 205     104.200 117.977  45.592  1.00 19.23           O  
-ATOM   1675  N   ASP A 206     104.821 116.577  43.927  1.00 18.55           N  
-ATOM   1676  CA  ASP A 206     105.559 115.678  44.795  1.00 21.07           C  
-ATOM   1677  C   ASP A 206     107.048 115.562  44.426  1.00 20.88           C  
-ATOM   1678  O   ASP A 206     107.770 114.746  44.994  1.00 21.74           O  
-ATOM   1679  CB  ASP A 206     104.911 114.281  44.807  1.00 23.20           C  
-ATOM   1680  CG  ASP A 206     104.776 113.681  43.425  1.00 25.82           C  
-ATOM   1681  OD1 ASP A 206     105.573 114.030  42.533  1.00 25.61           O  
-ATOM   1682  OD2 ASP A 206     103.874 112.831  43.230  1.00 30.04           O  
-ATOM   1683  N   SER A 207     107.483 116.357  43.453  1.00 19.07           N  
-ATOM   1684  CA  SER A 207     108.880 116.406  43.036  1.00 17.31           C  
-ATOM   1685  C   SER A 207     109.052 117.662  42.193  1.00 16.95           C  
-ATOM   1686  O   SER A 207     108.074 118.237  41.751  1.00 14.39           O  
-ATOM   1687  CB  SER A 207     109.265 115.189  42.194  1.00 17.68           C  
-ATOM   1688  OG  SER A 207     108.616 115.191  40.940  1.00 15.78           O  
-ATOM   1689  N   GLU A 208     110.290 118.091  41.965  1.00 17.14           N  
-ATOM   1690  CA  GLU A 208     110.486 119.290  41.141  1.00 17.56           C  
-ATOM   1691  C   GLU A 208     109.864 119.131  39.767  1.00 15.50           C  
-ATOM   1692  O   GLU A 208     109.139 120.016  39.298  1.00 14.97           O  
-ATOM   1693  CB  GLU A 208     111.976 119.598  40.978  1.00 18.35           C  
-ATOM   1694  CG  GLU A 208     112.665 120.029  42.268  1.00 24.11           C  
-ATOM   1695  CD  GLU A 208     114.167 120.071  42.098  1.00 26.41           C  
-ATOM   1696  OE1 GLU A 208     114.779 118.989  41.971  1.00 32.31           O  
-ATOM   1697  OE2 GLU A 208     114.727 121.175  42.062  1.00 29.47           O  
-ATOM   1698  N   ILE A 209     110.138 118.011  39.099  1.00 14.75           N  
-ATOM   1699  CA  ILE A 209     109.567 117.832  37.764  1.00 13.99           C  
-ATOM   1700  C   ILE A 209     108.036 117.749  37.813  1.00 12.92           C  
-ATOM   1701  O   ILE A 209     107.351 118.284  36.948  1.00 11.81           O  
-ATOM   1702  CB  ILE A 209     110.180 116.581  37.039  1.00 15.48           C  
-ATOM   1703  CG1 ILE A 209     109.836 116.603  35.540  1.00 17.76           C  
-ATOM   1704  CG2 ILE A 209     109.607 115.290  37.637  1.00 15.64           C  
-ATOM   1705  CD1 ILE A 209     110.416 117.792  34.749  1.00 16.84           C  
-ATOM   1706  N   ASP A 210     107.487 117.115  38.846  1.00 12.02           N  
-ATOM   1707  CA  ASP A 210     106.032 117.005  38.938  1.00 12.69           C  
-ATOM   1708  C   ASP A 210     105.437 118.390  39.198  1.00 12.14           C  
-ATOM   1709  O   ASP A 210     104.367 118.729  38.713  1.00 11.43           O  
-ATOM   1710  CB  ASP A 210     105.653 116.049  40.075  1.00 13.82           C  
-ATOM   1711  CG  ASP A 210     104.168 115.866  40.212  1.00 15.64           C  
-ATOM   1712  OD1 ASP A 210     103.534 115.345  39.270  1.00 19.65           O  
-ATOM   1713  OD2 ASP A 210     103.639 116.244  41.271  1.00 16.67           O  
-ATOM   1714  N   GLN A 211     106.157 119.186  39.968  1.00 12.29           N  
-ATOM   1715  CA  GLN A 211     105.698 120.529  40.301  1.00 13.02           C  
-ATOM   1716  C   GLN A 211     105.663 121.351  39.024  1.00 13.03           C  
-ATOM   1717  O   GLN A 211     104.700 122.051  38.737  1.00 11.68           O  
-ATOM   1718  CB  GLN A 211     106.649 121.150  41.319  1.00 14.42           C  
-ATOM   1719  CG  GLN A 211     106.195 122.493  41.845  1.00 15.69           C  
-ATOM   1720  CD  GLN A 211     104.934 122.394  42.672  1.00 16.31           C  
-ATOM   1721  OE1 GLN A 211     104.735 121.412  43.398  1.00 17.21           O  
-ATOM   1722  NE2 GLN A 211     104.088 123.423  42.593  1.00 17.65           N  
-ATOM   1723  N   LEU A 212     106.736 121.266  38.253  1.00 13.23           N  
-ATOM   1724  CA  LEU A 212     106.796 121.991  37.008  1.00 14.77           C  
-ATOM   1725  C   LEU A 212     105.667 121.583  36.068  1.00 13.94           C  
-ATOM   1726  O   LEU A 212     105.039 122.430  35.478  1.00 13.46           O  
-ATOM   1727  CB  LEU A 212     108.140 121.745  36.329  1.00 16.01           C  
-ATOM   1728  CG  LEU A 212     108.509 122.767  35.265  1.00 20.76           C  
-ATOM   1729  CD1 LEU A 212     108.926 124.090  35.933  1.00 17.68           C  
-ATOM   1730  CD2 LEU A 212     109.693 122.204  34.443  1.00 21.31           C  
-ATOM   1731  N   PHE A 213     105.410 120.281  35.934  1.00 13.02           N  
-ATOM   1732  CA  PHE A 213     104.360 119.820  35.046  1.00 12.82           C  
-ATOM   1733  C   PHE A 213     102.954 120.216  35.487  1.00 13.49           C  
-ATOM   1734  O   PHE A 213     102.091 120.496  34.648  1.00 11.82           O  
-ATOM   1735  CB  PHE A 213     104.470 118.303  34.841  1.00 15.33           C  
-ATOM   1736  CG  PHE A 213     105.623 117.906  33.952  1.00 18.77           C  
-ATOM   1737  CD1 PHE A 213     106.458 118.879  33.399  1.00 19.90           C  
-ATOM   1738  CD2 PHE A 213     105.882 116.571  33.681  1.00 20.61           C  
-ATOM   1739  CE1 PHE A 213     107.537 118.524  32.592  1.00 22.39           C  
-ATOM   1740  CE2 PHE A 213     106.959 116.211  32.874  1.00 22.40           C  
-ATOM   1741  CZ  PHE A 213     107.784 117.188  32.332  1.00 20.22           C  
-ATOM   1742  N   ARG A 214     102.739 120.280  36.799  1.00 13.47           N  
-ATOM   1743  CA  ARG A 214     101.436 120.694  37.316  1.00 12.88           C  
-ATOM   1744  C   ARG A 214     101.232 122.173  36.949  1.00 11.50           C  
-ATOM   1745  O   ARG A 214     100.140 122.579  36.535  1.00 11.07           O  
-ATOM   1746  CB  ARG A 214     101.378 120.495  38.835  1.00 12.19           C  
-ATOM   1747  CG  ARG A 214     101.046 119.049  39.216  1.00 14.97           C  
-ATOM   1748  CD  ARG A 214     101.269 118.803  40.690  1.00 13.91           C  
-ATOM   1749  NE  ARG A 214     101.023 117.414  41.104  1.00 15.47           N  
-ATOM   1750  CZ  ARG A 214      99.824 116.932  41.434  1.00 20.18           C  
-ATOM   1751  NH1 ARG A 214      98.754 117.713  41.393  1.00 20.21           N  
-ATOM   1752  NH2 ARG A 214      99.707 115.677  41.842  1.00 21.01           N  
-ATOM   1753  N   ILE A 215     102.288 122.964  37.082  1.00 11.76           N  
-ATOM   1754  CA  ILE A 215     102.200 124.371  36.712  1.00 11.24           C  
-ATOM   1755  C   ILE A 215     101.937 124.481  35.205  1.00 11.91           C  
-ATOM   1756  O   ILE A 215     101.046 125.224  34.795  1.00 11.56           O  
-ATOM   1757  CB  ILE A 215     103.496 125.136  37.070  1.00 12.10           C  
-ATOM   1758  CG1 ILE A 215     103.659 125.198  38.598  1.00 10.59           C  
-ATOM   1759  CG2 ILE A 215     103.439 126.572  36.503  1.00 12.54           C  
-ATOM   1760  CD1 ILE A 215     105.052 125.577  39.053  1.00 13.56           C  
-ATOM   1761  N   PHE A 216     102.690 123.730  34.391  1.00 12.48           N  
-ATOM   1762  CA  PHE A 216     102.536 123.793  32.938  1.00 12.76           C  
-ATOM   1763  C   PHE A 216     101.132 123.403  32.471  1.00 12.43           C  
-ATOM   1764  O   PHE A 216     100.581 123.998  31.548  1.00 12.45           O  
-ATOM   1765  CB  PHE A 216     103.547 122.861  32.214  1.00 10.61           C  
-ATOM   1766  CG  PHE A 216     104.995 123.298  32.287  1.00 12.57           C  
-ATOM   1767  CD1 PHE A 216     105.370 124.500  32.885  1.00 12.81           C  
-ATOM   1768  CD2 PHE A 216     105.990 122.475  31.760  1.00 13.05           C  
-ATOM   1769  CE1 PHE A 216     106.736 124.882  32.959  1.00 14.73           C  
-ATOM   1770  CE2 PHE A 216     107.347 122.843  31.824  1.00 15.46           C  
-ATOM   1771  CZ  PHE A 216     107.716 124.041  32.420  1.00 15.62           C  
-ATOM   1772  N   ARG A 217     100.575 122.368  33.094  1.00 14.85           N  
-ATOM   1773  CA  ARG A 217      99.258 121.858  32.735  1.00 17.20           C  
-ATOM   1774  C   ARG A 217      98.146 122.873  33.013  1.00 17.59           C  
-ATOM   1775  O   ARG A 217      97.067 122.810  32.422  1.00 16.92           O  
-ATOM   1776  CB  ARG A 217      98.966 120.575  33.523  1.00 20.74           C  
-ATOM   1777  CG  ARG A 217      97.702 119.851  33.090  1.00 28.07           C  
-ATOM   1778  CD  ARG A 217      97.257 118.840  34.134  1.00 31.73           C  
-ATOM   1779  NE  ARG A 217      96.281 117.891  33.593  1.00 37.56           N  
-ATOM   1780  CZ  ARG A 217      95.915 116.767  34.205  1.00 38.14           C  
-ATOM   1781  NH1 ARG A 217      96.445 116.447  35.381  1.00 40.75           N  
-ATOM   1782  NH2 ARG A 217      95.026 115.959  33.641  1.00 39.35           N  
-ATOM   1783  N   THR A 218      98.398 123.787  33.937  1.00 15.73           N  
-ATOM   1784  CA  THR A 218      97.398 124.794  34.274  1.00 15.47           C  
-ATOM   1785  C   THR A 218      97.605 126.119  33.528  1.00 14.60           C  
-ATOM   1786  O   THR A 218      96.679 126.662  32.917  1.00 16.53           O  
-ATOM   1787  CB  THR A 218      97.421 125.077  35.803  1.00 17.38           C  
-ATOM   1788  OG1 THR A 218      97.062 123.882  36.514  1.00 22.23           O  
-ATOM   1789  CG2 THR A 218      96.439 126.186  36.161  1.00 18.52           C  
-ATOM   1790  N   LEU A 219      98.829 126.635  33.576  1.00 13.31           N  
-ATOM   1791  CA  LEU A 219      99.137 127.905  32.951  1.00 12.80           C  
-ATOM   1792  C   LEU A 219      99.675 127.783  31.530  1.00 13.14           C  
-ATOM   1793  O   LEU A 219      99.902 128.803  30.866  1.00 15.27           O  
-ATOM   1794  CB  LEU A 219     100.149 128.668  33.826  1.00 14.54           C  
-ATOM   1795  CG  LEU A 219      99.703 128.830  35.281  1.00 15.86           C  
-ATOM   1796  CD1 LEU A 219     100.864 129.349  36.134  1.00 16.41           C  
-ATOM   1797  CD2 LEU A 219      98.510 129.763  35.316  1.00 17.37           C  
-ATOM   1798  N   GLY A 220      99.856 126.548  31.064  1.00 12.02           N  
-ATOM   1799  CA  GLY A 220     100.390 126.324  29.729  1.00 13.29           C  
-ATOM   1800  C   GLY A 220     101.904 126.204  29.792  1.00 13.95           C  
-ATOM   1801  O   GLY A 220     102.554 126.828  30.654  1.00 13.81           O  
-ATOM   1802  N   THR A 221     102.484 125.396  28.906  1.00 13.41           N  
-ATOM   1803  CA  THR A 221     103.934 125.254  28.891  1.00 14.31           C  
-ATOM   1804  C   THR A 221     104.470 126.565  28.329  1.00 14.31           C  
-ATOM   1805  O   THR A 221     104.085 127.002  27.237  1.00 13.46           O  
-ATOM   1806  CB  THR A 221     104.384 124.085  28.024  1.00 14.93           C  
-ATOM   1807  OG1 THR A 221     103.749 122.885  28.483  1.00 16.57           O  
-ATOM   1808  CG2 THR A 221     105.887 123.910  28.135  1.00 15.01           C  
-ATOM   1809  N   PRO A 222     105.361 127.218  29.076  1.00 15.36           N  
-ATOM   1810  CA  PRO A 222     105.900 128.493  28.599  1.00 16.71           C  
-ATOM   1811  C   PRO A 222     106.807 128.326  27.407  1.00 16.94           C  
-ATOM   1812  O   PRO A 222     107.454 127.300  27.271  1.00 16.56           O  
-ATOM   1813  CB  PRO A 222     106.652 129.033  29.817  1.00 16.11           C  
-ATOM   1814  CG  PRO A 222     107.095 127.803  30.517  1.00 15.88           C  
-ATOM   1815  CD  PRO A 222     105.922 126.859  30.387  1.00 14.47           C  
-ATOM   1816  N   ASP A 223     106.814 129.331  26.536  1.00 17.59           N  
-ATOM   1817  CA  ASP A 223     107.706 129.341  25.370  1.00 16.93           C  
-ATOM   1818  C   ASP A 223     108.385 130.715  25.359  1.00 16.73           C  
-ATOM   1819  O   ASP A 223     108.148 131.537  26.247  1.00 16.84           O  
-ATOM   1820  CB  ASP A 223     106.940 129.116  24.054  1.00 19.87           C  
-ATOM   1821  CG  ASP A 223     105.788 130.082  23.857  1.00 23.73           C  
-ATOM   1822  OD1 ASP A 223     105.774 131.170  24.457  1.00 25.09           O  
-ATOM   1823  OD2 ASP A 223     104.877 129.742  23.070  1.00 27.32           O  
-ATOM   1824  N   GLU A 224     109.215 130.984  24.357  1.00 17.46           N  
-ATOM   1825  CA  GLU A 224     109.921 132.261  24.300  1.00 17.58           C  
-ATOM   1826  C   GLU A 224     109.023 133.486  24.171  1.00 19.34           C  
-ATOM   1827  O   GLU A 224     109.382 134.583  24.599  1.00 19.10           O  
-ATOM   1828  CB  GLU A 224     110.940 132.231  23.150  1.00 18.94           C  
-ATOM   1829  CG  GLU A 224     112.128 131.267  23.405  1.00 18.69           C  
-ATOM   1830  CD  GLU A 224     113.126 131.788  24.438  1.00 20.73           C  
-ATOM   1831  OE1 GLU A 224     113.273 133.022  24.540  1.00 21.30           O  
-ATOM   1832  OE2 GLU A 224     113.787 130.970  25.145  1.00 20.37           O  
-ATOM   1833  N   VAL A 225     107.854 133.303  23.574  1.00 19.04           N  
-ATOM   1834  CA  VAL A 225     106.928 134.409  23.420  1.00 20.77           C  
-ATOM   1835  C   VAL A 225     106.434 134.893  24.787  1.00 21.06           C  
-ATOM   1836  O   VAL A 225     106.503 136.078  25.106  1.00 22.57           O  
-ATOM   1837  CB  VAL A 225     105.721 133.986  22.554  1.00 22.07           C  
-ATOM   1838  CG1 VAL A 225     104.770 135.171  22.362  1.00 24.57           C  
-ATOM   1839  CG2 VAL A 225     106.211 133.479  21.197  1.00 24.71           C  
-ATOM   1840  N   VAL A 226     105.974 133.960  25.609  1.00 19.95           N  
-ATOM   1841  CA  VAL A 226     105.450 134.283  26.926  1.00 18.21           C  
-ATOM   1842  C   VAL A 226     106.539 134.577  27.966  1.00 17.32           C  
-ATOM   1843  O   VAL A 226     106.367 135.436  28.842  1.00 16.17           O  
-ATOM   1844  CB AVAL A 226     104.539 133.138  27.428  0.50 18.99           C  
-ATOM   1845  CB BVAL A 226     104.553 133.138  27.448  0.50 19.28           C  
-ATOM   1846  CG1AVAL A 226     104.329 133.233  28.930  0.50 17.64           C  
-ATOM   1847  CG1BVAL A 226     103.512 132.764  26.390  0.50 19.93           C  
-ATOM   1848  CG2AVAL A 226     103.187 133.213  26.708  0.50 19.35           C  
-ATOM   1849  CG2BVAL A 226     105.390 131.935  27.794  0.50 18.58           C  
-ATOM   1850  N   TRP A 227     107.663 133.881  27.857  1.00 14.74           N  
-ATOM   1851  CA  TRP A 227     108.762 134.033  28.804  1.00 14.02           C  
-ATOM   1852  C   TRP A 227     110.107 134.019  28.072  1.00 14.54           C  
-ATOM   1853  O   TRP A 227     110.762 132.964  27.954  1.00 12.91           O  
-ATOM   1854  CB  TRP A 227     108.718 132.889  29.813  1.00 12.40           C  
-ATOM   1855  CG  TRP A 227     109.703 132.986  30.949  1.00 13.31           C  
-ATOM   1856  CD1 TRP A 227     110.661 133.949  31.140  1.00 14.45           C  
-ATOM   1857  CD2 TRP A 227     109.813 132.080  32.057  1.00 13.34           C  
-ATOM   1858  NE1 TRP A 227     111.358 133.693  32.305  1.00 15.57           N  
-ATOM   1859  CE2 TRP A 227     110.853 132.555  32.885  1.00 15.06           C  
-ATOM   1860  CE3 TRP A 227     109.132 130.915  32.428  1.00 13.60           C  
-ATOM   1861  CZ2 TRP A 227     111.225 131.905  34.073  1.00 15.38           C  
-ATOM   1862  CZ3 TRP A 227     109.505 130.264  33.614  1.00 15.37           C  
-ATOM   1863  CH2 TRP A 227     110.537 130.764  34.418  1.00 14.59           C  
-ATOM   1864  N   PRO A 228     110.550 135.196  27.596  1.00 15.14           N  
-ATOM   1865  CA  PRO A 228     111.822 135.260  26.878  1.00 14.83           C  
-ATOM   1866  C   PRO A 228     112.936 134.681  27.723  1.00 14.76           C  
-ATOM   1867  O   PRO A 228     113.085 135.023  28.908  1.00 15.50           O  
-ATOM   1868  CB  PRO A 228     111.993 136.762  26.604  1.00 16.47           C  
-ATOM   1869  CG  PRO A 228     110.556 137.236  26.473  1.00 16.16           C  
-ATOM   1870  CD  PRO A 228     109.909 136.526  27.653  1.00 15.40           C  
-ATOM   1871  N   GLY A 229     113.696 133.780  27.110  1.00 13.15           N  
-ATOM   1872  CA  GLY A 229     114.803 133.146  27.789  1.00 13.89           C  
-ATOM   1873  C   GLY A 229     114.484 131.818  28.450  1.00 14.18           C  
-ATOM   1874  O   GLY A 229     115.400 131.116  28.864  1.00 15.28           O  
-ATOM   1875  N   VAL A 230     113.210 131.457  28.548  1.00 12.32           N  
-ATOM   1876  CA  VAL A 230     112.878 130.214  29.235  1.00 13.41           C  
-ATOM   1877  C   VAL A 230     113.533 128.962  28.638  1.00 14.41           C  
-ATOM   1878  O   VAL A 230     114.015 128.116  29.389  1.00 13.38           O  
-ATOM   1879  CB  VAL A 230     111.325 130.011  29.345  1.00 13.80           C  
-ATOM   1880  CG1 VAL A 230     110.689 129.835  27.980  1.00 11.20           C  
-ATOM   1881  CG2 VAL A 230     111.028 128.809  30.250  1.00 13.10           C  
-ATOM   1882  N   THR A 231     113.597 128.861  27.307  1.00 15.08           N  
-ATOM   1883  CA  THR A 231     114.166 127.669  26.682  1.00 15.83           C  
-ATOM   1884  C   THR A 231     115.679 127.502  26.861  1.00 17.92           C  
-ATOM   1885  O   THR A 231     116.241 126.467  26.491  1.00 19.81           O  
-ATOM   1886  CB  THR A 231     113.788 127.573  25.164  1.00 16.95           C  
-ATOM   1887  OG1 THR A 231     114.465 128.584  24.415  1.00 16.62           O  
-ATOM   1888  CG2 THR A 231     112.273 127.736  24.984  1.00 19.59           C  
-ATOM   1889  N   SER A 232     116.332 128.499  27.450  1.00 16.92           N  
-ATOM   1890  CA  SER A 232     117.766 128.412  27.693  1.00 17.33           C  
-ATOM   1891  C   SER A 232     118.080 128.279  29.174  1.00 17.42           C  
-ATOM   1892  O   SER A 232     119.242 128.224  29.561  1.00 15.46           O  
-ATOM   1893  CB  SER A 232     118.469 129.639  27.123  1.00 18.89           C  
-ATOM   1894  OG  SER A 232     118.306 129.670  25.715  1.00 24.10           O  
-ATOM   1895  N   MET A 233     117.045 128.243  30.015  1.00 17.89           N  
-ATOM   1896  CA  MET A 233     117.269 128.120  31.454  1.00 17.45           C  
-ATOM   1897  C   MET A 233     117.978 126.803  31.736  1.00 17.16           C  
-ATOM   1898  O   MET A 233     117.737 125.811  31.047  1.00 17.28           O  
-ATOM   1899  CB AMET A 233     115.947 128.267  32.194  0.50 16.65           C  
-ATOM   1900  CB BMET A 233     115.923 128.110  32.185  0.50 18.85           C  
-ATOM   1901  CG AMET A 233     115.423 129.682  32.001  0.50 16.77           C  
-ATOM   1902  CG BMET A 233     115.168 129.415  32.122  0.50 21.48           C  
-ATOM   1903  SD AMET A 233     114.004 130.083  32.980  0.50 15.10           S  
-ATOM   1904  SD BMET A 233     115.955 130.627  33.166  0.50 24.01           S  
-ATOM   1905  CE AMET A 233     114.766 130.362  34.574  0.50 15.33           C  
-ATOM   1906  CE BMET A 233     115.387 130.099  34.776  0.50 22.38           C  
-ATOM   1907  N   PRO A 234     118.852 126.775  32.757  1.00 18.06           N  
-ATOM   1908  CA  PRO A 234     119.611 125.571  33.109  1.00 17.82           C  
-ATOM   1909  C   PRO A 234     118.911 124.225  33.026  1.00 17.28           C  
-ATOM   1910  O   PRO A 234     119.445 123.296  32.424  1.00 17.81           O  
-ATOM   1911  CB  PRO A 234     120.128 125.890  34.507  1.00 18.79           C  
-ATOM   1912  CG  PRO A 234     120.408 127.363  34.397  1.00 19.41           C  
-ATOM   1913  CD  PRO A 234     119.141 127.862  33.710  1.00 18.47           C  
-ATOM   1914  N   ASP A 235     117.738 124.099  33.642  1.00 14.84           N  
-ATOM   1915  CA  ASP A 235     117.035 122.831  33.612  1.00 15.81           C  
-ATOM   1916  C   ASP A 235     115.878 122.717  32.623  1.00 14.02           C  
-ATOM   1917  O   ASP A 235     115.090 121.789  32.688  1.00 13.73           O  
-ATOM   1918  CB  ASP A 235     116.581 122.462  35.022  1.00 16.28           C  
-ATOM   1919  CG  ASP A 235     117.738 122.391  35.983  1.00 20.17           C  
-ATOM   1920  OD1 ASP A 235     118.759 121.782  35.609  1.00 22.32           O  
-ATOM   1921  OD2 ASP A 235     117.638 122.947  37.094  1.00 22.29           O  
-ATOM   1922  N   TYR A 236     115.775 123.656  31.691  1.00 12.91           N  
-ATOM   1923  CA  TYR A 236     114.723 123.561  30.711  1.00 13.88           C  
-ATOM   1924  C   TYR A 236     115.068 122.410  29.743  1.00 14.14           C  
-ATOM   1925  O   TYR A 236     116.235 122.242  29.354  1.00 14.77           O  
-ATOM   1926  CB  TYR A 236     114.601 124.868  29.913  1.00 15.56           C  
-ATOM   1927  CG  TYR A 236     113.589 124.746  28.813  1.00 17.15           C  
-ATOM   1928  CD1 TYR A 236     112.252 125.068  29.038  1.00 18.46           C  
-ATOM   1929  CD2 TYR A 236     113.954 124.271  27.552  1.00 17.55           C  
-ATOM   1930  CE1 TYR A 236     111.292 124.919  28.025  1.00 18.77           C  
-ATOM   1931  CE2 TYR A 236     113.002 124.119  26.539  1.00 17.87           C  
-ATOM   1932  CZ  TYR A 236     111.682 124.442  26.787  1.00 18.35           C  
-ATOM   1933  OH  TYR A 236     110.735 124.274  25.805  1.00 19.33           O  
-ATOM   1934  N   LYS A 237     114.059 121.626  29.369  1.00 14.71           N  
-ATOM   1935  CA  LYS A 237     114.234 120.511  28.426  1.00 15.86           C  
-ATOM   1936  C   LYS A 237     113.197 120.624  27.311  1.00 16.11           C  
-ATOM   1937  O   LYS A 237     112.001 120.671  27.585  1.00 16.60           O  
-ATOM   1938  CB  LYS A 237     114.029 119.164  29.118  1.00 15.43           C  
-ATOM   1939  CG  LYS A 237     114.794 118.996  30.419  1.00 15.90           C  
-ATOM   1940  CD  LYS A 237     116.266 118.775  30.173  1.00 16.27           C  
-ATOM   1941  CE  LYS A 237     117.038 118.826  31.482  1.00 18.33           C  
-ATOM   1942  NZ  LYS A 237     118.447 118.462  31.213  1.00 18.92           N  
-ATOM   1943  N   PRO A 238     113.639 120.659  26.044  1.00 17.09           N  
-ATOM   1944  CA  PRO A 238     112.680 120.764  24.942  1.00 17.62           C  
-ATOM   1945  C   PRO A 238     111.706 119.593  24.933  1.00 17.89           C  
-ATOM   1946  O   PRO A 238     110.651 119.680  24.321  1.00 18.98           O  
-ATOM   1947  CB  PRO A 238     113.576 120.792  23.694  1.00 18.10           C  
-ATOM   1948  CG  PRO A 238     114.815 121.428  24.180  1.00 17.36           C  
-ATOM   1949  CD  PRO A 238     115.024 120.803  25.547  1.00 16.61           C  
-ATOM   1950  N   SER A 239     112.059 118.506  25.623  1.00 17.88           N  
-ATOM   1951  CA  SER A 239     111.200 117.328  25.681  1.00 18.68           C  
-ATOM   1952  C   SER A 239     109.958 117.531  26.543  1.00 18.45           C  
-ATOM   1953  O   SER A 239     109.083 116.666  26.604  1.00 18.03           O  
-ATOM   1954  CB  SER A 239     111.981 116.117  26.206  1.00 18.98           C  
-ATOM   1955  OG  SER A 239     112.595 116.395  27.451  1.00 18.13           O  
-ATOM   1956  N   PHE A 240     109.887 118.660  27.234  1.00 19.00           N  
-ATOM   1957  CA  PHE A 240     108.720 118.944  28.080  1.00 18.37           C  
-ATOM   1958  C   PHE A 240     107.424 118.887  27.276  1.00 18.04           C  
-ATOM   1959  O   PHE A 240     107.346 119.417  26.172  1.00 17.26           O  
-ATOM   1960  CB  PHE A 240     108.775 120.364  28.664  1.00 17.12           C  
-ATOM   1961  CG  PHE A 240     109.794 120.569  29.754  1.00 16.74           C  
-ATOM   1962  CD1 PHE A 240     110.287 119.512  30.498  1.00 16.81           C  
-ATOM   1963  CD2 PHE A 240     110.216 121.870  30.066  1.00 15.33           C  
-ATOM   1964  CE1 PHE A 240     111.200 119.750  31.562  1.00 16.62           C  
-ATOM   1965  CE2 PHE A 240     111.103 122.107  31.099  1.00 14.08           C  
-ATOM   1966  CZ  PHE A 240     111.598 121.051  31.851  1.00 16.07           C  
-ATOM   1967  N   PRO A 241     106.377 118.264  27.835  1.00 19.62           N  
-ATOM   1968  CA  PRO A 241     105.111 118.212  27.098  1.00 20.98           C  
-ATOM   1969  C   PRO A 241     104.625 119.646  26.903  1.00 22.11           C  
-ATOM   1970  O   PRO A 241     104.953 120.545  27.704  1.00 20.55           O  
-ATOM   1971  CB  PRO A 241     104.199 117.425  28.032  1.00 21.23           C  
-ATOM   1972  CG  PRO A 241     105.162 116.480  28.704  1.00 21.67           C  
-ATOM   1973  CD  PRO A 241     106.324 117.413  29.033  1.00 20.70           C  
-ATOM   1974  N   LYS A 242     103.846 119.859  25.844  1.00 22.68           N  
-ATOM   1975  CA  LYS A 242     103.316 121.179  25.542  1.00 23.25           C  
-ATOM   1976  C   LYS A 242     101.822 121.158  25.890  1.00 23.26           C  
-ATOM   1977  O   LYS A 242     101.012 120.474  25.236  1.00 23.31           O  
-ATOM   1978  CB  LYS A 242     103.523 121.500  24.054  1.00 26.66           C  
-ATOM   1979  CG  LYS A 242     103.398 122.982  23.699  1.00 29.73           C  
-ATOM   1980  CD  LYS A 242     102.030 123.533  24.067  1.00 34.08           C  
-ATOM   1981  CE  LYS A 242     101.895 125.002  23.688  1.00 35.72           C  
-ATOM   1982  NZ  LYS A 242     100.602 125.569  24.149  1.00 36.81           N  
-ATOM   1983  N   TRP A 243     101.476 121.884  26.948  1.00 20.67           N  
-ATOM   1984  CA  TRP A 243     100.104 121.992  27.424  1.00 19.58           C  
-ATOM   1985  C   TRP A 243      99.599 123.383  27.101  1.00 18.77           C  
-ATOM   1986  O   TRP A 243     100.378 124.345  27.070  1.00 17.06           O  
-ATOM   1987  CB  TRP A 243     100.034 121.807  28.947  1.00 21.25           C  
-ATOM   1988  CG  TRP A 243     100.079 120.381  29.420  1.00 21.79           C  
-ATOM   1989  CD1 TRP A 243      99.071 119.465  29.347  1.00 22.96           C  
-ATOM   1990  CD2 TRP A 243     101.186 119.716  30.036  1.00 22.38           C  
-ATOM   1991  NE1 TRP A 243      99.484 118.264  29.881  1.00 24.06           N  
-ATOM   1992  CE2 TRP A 243     100.779 118.394  30.313  1.00 23.75           C  
-ATOM   1993  CE3 TRP A 243     102.483 120.107  30.381  1.00 21.98           C  
-ATOM   1994  CZ2 TRP A 243     101.625 117.459  30.926  1.00 23.43           C  
-ATOM   1995  CZ3 TRP A 243     103.328 119.174  30.994  1.00 21.82           C  
-ATOM   1996  CH2 TRP A 243     102.890 117.868  31.258  1.00 24.03           C  
-ATOM   1997  N   ALA A 244      98.296 123.493  26.877  1.00 18.20           N  
-ATOM   1998  CA  ALA A 244      97.689 124.788  26.594  1.00 19.55           C  
-ATOM   1999  C   ALA A 244      97.220 125.371  27.922  1.00 19.95           C  
-ATOM   2000  O   ALA A 244      96.870 124.626  28.845  1.00 20.57           O  
-ATOM   2001  CB  ALA A 244      96.508 124.624  25.646  1.00 21.43           C  
-ATOM   2002  N   ARG A 245      97.228 126.698  28.034  1.00 19.15           N  
-ATOM   2003  CA  ARG A 245      96.793 127.367  29.258  1.00 20.11           C  
-ATOM   2004  C   ARG A 245      95.302 127.157  29.535  1.00 20.60           C  
-ATOM   2005  O   ARG A 245      94.487 127.173  28.610  1.00 19.09           O  
-ATOM   2006  CB  ARG A 245      97.084 128.870  29.167  1.00 21.85           C  
-ATOM   2007  CG  ARG A 245      96.503 129.680  30.308  1.00 25.07           C  
-ATOM   2008  CD  ARG A 245      96.827 131.169  30.159  1.00 28.69           C  
-ATOM   2009  NE  ARG A 245      96.337 131.932  31.303  1.00 31.21           N  
-ATOM   2010  CZ  ARG A 245      95.048 132.075  31.613  1.00 34.20           C  
-ATOM   2011  NH1 ARG A 245      94.108 131.512  30.863  1.00 35.26           N  
-ATOM   2012  NH2 ARG A 245      94.696 132.770  32.687  1.00 34.94           N  
-ATOM   2013  N   GLN A 246      94.951 126.954  30.807  1.00 20.02           N  
-ATOM   2014  CA  GLN A 246      93.551 126.765  31.213  1.00 20.71           C  
-ATOM   2015  C   GLN A 246      92.905 128.096  31.595  1.00 22.36           C  
-ATOM   2016  O   GLN A 246      93.604 129.017  32.001  1.00 22.80           O  
-ATOM   2017  CB  GLN A 246      93.472 125.811  32.413  1.00 22.14           C  
-ATOM   2018  CG  GLN A 246      94.035 124.432  32.123  1.00 23.21           C  
-ATOM   2019  CD  GLN A 246      93.379 123.813  30.909  1.00 28.93           C  
-ATOM   2020  OE1 GLN A 246      92.162 123.585  30.895  1.00 29.67           O  
-ATOM   2021  NE2 GLN A 246      94.173 123.548  29.870  1.00 30.23           N  
-ATOM   2022  N   ASP A 247      91.573 128.193  31.481  1.00 22.51           N  
-ATOM   2023  CA  ASP A 247      90.883 129.426  31.854  1.00 22.60           C  
-ATOM   2024  C   ASP A 247      90.732 129.521  33.372  1.00 21.32           C  
-ATOM   2025  O   ASP A 247      90.444 128.525  34.021  1.00 18.48           O  
-ATOM   2026  CB  ASP A 247      89.483 129.482  31.229  1.00 27.42           C  
-ATOM   2027  CG  ASP A 247      89.519 129.652  29.727  1.00 31.14           C  
-ATOM   2028  OD1 ASP A 247      90.389 130.410  29.246  1.00 32.88           O  
-ATOM   2029  OD2 ASP A 247      88.670 129.038  29.040  1.00 34.14           O  
-ATOM   2030  N   PHE A 248      90.914 130.717  33.930  1.00 19.41           N  
-ATOM   2031  CA  PHE A 248      90.752 130.900  35.367  1.00 19.93           C  
-ATOM   2032  C   PHE A 248      89.337 130.672  35.826  1.00 18.32           C  
-ATOM   2033  O   PHE A 248      89.114 130.425  37.005  1.00 18.17           O  
-ATOM   2034  CB  PHE A 248      91.188 132.298  35.805  1.00 21.86           C  
-ATOM   2035  CG  PHE A 248      92.661 132.448  35.921  1.00 25.63           C  
-ATOM   2036  CD1 PHE A 248      93.503 131.401  35.566  1.00 26.90           C  
-ATOM   2037  CD2 PHE A 248      93.215 133.624  36.406  1.00 27.49           C  
-ATOM   2038  CE1 PHE A 248      94.884 131.519  35.696  1.00 29.09           C  
-ATOM   2039  CE2 PHE A 248      94.595 133.750  36.539  1.00 29.05           C  
-ATOM   2040  CZ  PHE A 248      95.428 132.698  36.186  1.00 28.51           C  
-ATOM   2041  N   SER A 249      88.368 130.741  34.918  1.00 17.35           N  
-ATOM   2042  CA  SER A 249      86.993 130.498  35.349  1.00 18.29           C  
-ATOM   2043  C   SER A 249      86.929 129.063  35.844  1.00 17.72           C  
-ATOM   2044  O   SER A 249      86.038 128.686  36.616  1.00 18.74           O  
-ATOM   2045  CB  SER A 249      86.013 130.702  34.189  1.00 18.32           C  
-ATOM   2046  OG  SER A 249      86.256 129.792  33.135  1.00 20.00           O  
-ATOM   2047  N   LYS A 250      87.889 128.266  35.387  1.00 16.72           N  
-ATOM   2048  CA  LYS A 250      87.989 126.867  35.751  1.00 18.23           C  
-ATOM   2049  C   LYS A 250      88.983 126.670  36.905  1.00 17.04           C  
-ATOM   2050  O   LYS A 250      88.704 125.916  37.840  1.00 16.95           O  
-ATOM   2051  CB  LYS A 250      88.422 126.070  34.508  1.00 19.90           C  
-ATOM   2052  CG  LYS A 250      88.796 124.611  34.704  1.00 23.85           C  
-ATOM   2053  CD  LYS A 250      89.393 124.085  33.373  1.00 26.02           C  
-ATOM   2054  CE  LYS A 250      89.664 122.610  33.397  1.00 28.38           C  
-ATOM   2055  NZ  LYS A 250      88.408 121.864  33.697  1.00 29.43           N  
-ATOM   2056  N   VAL A 251      90.119 127.371  36.850  1.00 16.75           N  
-ATOM   2057  CA  VAL A 251      91.163 127.255  37.882  1.00 17.48           C  
-ATOM   2058  C   VAL A 251      90.809 127.863  39.242  1.00 16.95           C  
-ATOM   2059  O   VAL A 251      91.136 127.294  40.284  1.00 16.02           O  
-ATOM   2060  CB  VAL A 251      92.480 127.889  37.407  1.00 17.99           C  
-ATOM   2061  CG1 VAL A 251      93.564 127.688  38.469  1.00 21.69           C  
-ATOM   2062  CG2 VAL A 251      92.898 127.277  36.069  1.00 20.88           C  
-ATOM   2063  N   VAL A 252      90.139 129.008  39.224  1.00 16.42           N  
-ATOM   2064  CA  VAL A 252      89.714 129.689  40.448  1.00 17.27           C  
-ATOM   2065  C   VAL A 252      88.307 130.203  40.171  1.00 16.64           C  
-ATOM   2066  O   VAL A 252      88.067 131.408  40.046  1.00 17.57           O  
-ATOM   2067  CB  VAL A 252      90.672 130.856  40.801  1.00 17.78           C  
-ATOM   2068  CG1 VAL A 252      92.060 130.306  41.110  1.00 20.17           C  
-ATOM   2069  CG2 VAL A 252      90.764 131.833  39.642  1.00 21.74           C  
-ATOM   2070  N   PRO A 253      87.338 129.274  40.097  1.00 15.97           N  
-ATOM   2071  CA  PRO A 253      85.939 129.606  39.814  1.00 16.54           C  
-ATOM   2072  C   PRO A 253      85.307 130.820  40.514  1.00 17.37           C  
-ATOM   2073  O   PRO A 253      84.683 131.653  39.861  1.00 17.71           O  
-ATOM   2074  CB  PRO A 253      85.200 128.290  40.113  1.00 16.01           C  
-ATOM   2075  CG  PRO A 253      86.225 127.228  39.760  1.00 17.47           C  
-ATOM   2076  CD  PRO A 253      87.504 127.830  40.365  1.00 16.59           C  
-ATOM   2077  N   PRO A 254      85.452 130.937  41.844  1.00 18.61           N  
-ATOM   2078  CA  PRO A 254      84.847 132.083  42.548  1.00 19.66           C  
-ATOM   2079  C   PRO A 254      85.310 133.505  42.162  1.00 20.06           C  
-ATOM   2080  O   PRO A 254      84.564 134.471  42.334  1.00 18.84           O  
-ATOM   2081  CB  PRO A 254      85.134 131.779  44.032  1.00 21.69           C  
-ATOM   2082  CG  PRO A 254      85.268 130.284  44.070  1.00 20.37           C  
-ATOM   2083  CD  PRO A 254      86.052 129.987  42.796  1.00 18.13           C  
-ATOM   2084  N   LEU A 255      86.515 133.652  41.622  1.00 19.66           N  
-ATOM   2085  CA  LEU A 255      87.016 134.996  41.293  1.00 20.84           C  
-ATOM   2086  C   LEU A 255      86.389 135.723  40.107  1.00 20.92           C  
-ATOM   2087  O   LEU A 255      86.010 135.095  39.116  1.00 21.76           O  
-ATOM   2088  CB  LEU A 255      88.548 134.945  41.084  1.00 21.61           C  
-ATOM   2089  CG  LEU A 255      89.429 134.618  42.295  1.00 23.20           C  
-ATOM   2090  CD1 LEU A 255      90.907 134.590  41.862  1.00 24.08           C  
-ATOM   2091  CD2 LEU A 255      89.231 135.672  43.391  1.00 23.56           C  
-ATOM   2092  N   ASP A 256      86.261 137.051  40.206  1.00 19.98           N  
-ATOM   2093  CA  ASP A 256      85.739 137.827  39.083  1.00 21.46           C  
-ATOM   2094  C   ASP A 256      86.933 138.420  38.329  1.00 20.28           C  
-ATOM   2095  O   ASP A 256      88.085 138.105  38.648  1.00 19.37           O  
-ATOM   2096  CB  ASP A 256      84.803 138.953  39.547  1.00 23.23           C  
-ATOM   2097  CG  ASP A 256      85.431 139.842  40.602  1.00 25.38           C  
-ATOM   2098  OD1 ASP A 256      86.588 140.281  40.417  1.00 26.18           O  
-ATOM   2099  OD2 ASP A 256      84.750 140.109  41.617  1.00 26.98           O  
-ATOM   2100  N   GLU A 257      86.670 139.292  37.360  1.00 18.86           N  
-ATOM   2101  CA  GLU A 257      87.761 139.859  36.565  1.00 18.86           C  
-ATOM   2102  C   GLU A 257      88.830 140.615  37.369  1.00 18.30           C  
-ATOM   2103  O   GLU A 257      89.996 140.632  36.970  1.00 18.46           O  
-ATOM   2104  CB  GLU A 257      87.199 140.747  35.438  1.00 18.28           C  
-ATOM   2105  CG  GLU A 257      88.265 141.500  34.626  1.00 21.47           C  
-ATOM   2106  CD  GLU A 257      89.143 140.590  33.757  1.00 23.54           C  
-ATOM   2107  OE1 GLU A 257      88.871 139.369  33.701  1.00 23.37           O  
-ATOM   2108  OE2 GLU A 257      90.102 141.113  33.126  1.00 23.83           O  
-ATOM   2109  N   ASP A 258      88.452 141.261  38.472  1.00 18.03           N  
-ATOM   2110  CA  ASP A 258      89.455 141.970  39.281  1.00 17.50           C  
-ATOM   2111  C   ASP A 258      90.375 140.969  39.960  1.00 16.99           C  
-ATOM   2112  O   ASP A 258      91.603 141.150  39.993  1.00 16.09           O  
-ATOM   2113  CB  ASP A 258      88.790 142.856  40.348  1.00 21.33           C  
-ATOM   2114  CG  ASP A 258      88.509 144.261  39.840  1.00 20.86           C  
-ATOM   2115  OD1 ASP A 258      88.927 144.564  38.711  1.00 23.30           O  
-ATOM   2116  OD2 ASP A 258      87.895 145.065  40.569  1.00 22.83           O  
-ATOM   2117  N   GLY A 259      89.776 139.920  40.511  1.00 17.00           N  
-ATOM   2118  CA  GLY A 259      90.555 138.881  41.159  1.00 17.31           C  
-ATOM   2119  C   GLY A 259      91.419 138.151  40.141  1.00 16.97           C  
-ATOM   2120  O   GLY A 259      92.593 137.877  40.385  1.00 16.00           O  
-ATOM   2121  N   ARG A 260      90.845 137.838  38.984  1.00 16.88           N  
-ATOM   2122  CA  ARG A 260      91.589 137.127  37.950  1.00 18.16           C  
-ATOM   2123  C   ARG A 260      92.724 137.972  37.406  1.00 16.10           C  
-ATOM   2124  O   ARG A 260      93.805 137.452  37.093  1.00 16.85           O  
-ATOM   2125  CB  ARG A 260      90.651 136.707  36.813  1.00 19.99           C  
-ATOM   2126  CG  ARG A 260      89.628 135.676  37.258  1.00 26.17           C  
-ATOM   2127  CD  ARG A 260      88.966 134.956  36.087  1.00 30.99           C  
-ATOM   2128  NE  ARG A 260      87.935 135.759  35.448  1.00 34.57           N  
-ATOM   2129  CZ  ARG A 260      86.676 135.360  35.282  1.00 36.19           C  
-ATOM   2130  NH1 ARG A 260      86.287 134.164  35.709  1.00 37.50           N  
-ATOM   2131  NH2 ARG A 260      85.802 136.161  34.690  1.00 36.86           N  
-ATOM   2132  N   SER A 261      92.487 139.275  37.291  1.00 13.93           N  
-ATOM   2133  CA  SER A 261      93.510 140.182  36.791  1.00 14.51           C  
-ATOM   2134  C   SER A 261      94.699 140.167  37.731  1.00 14.69           C  
-ATOM   2135  O   SER A 261      95.856 140.045  37.311  1.00 14.29           O  
-ATOM   2136  CB  SER A 261      92.990 141.624  36.710  1.00 16.34           C  
-ATOM   2137  OG  SER A 261      94.086 142.523  36.511  1.00 16.35           O  
-ATOM   2138  N   LEU A 262      94.413 140.310  39.019  1.00 13.15           N  
-ATOM   2139  CA  LEU A 262      95.499 140.305  39.983  1.00 11.59           C  
-ATOM   2140  C   LEU A 262      96.183 138.935  40.036  1.00 10.81           C  
-ATOM   2141  O   LEU A 262      97.414 138.854  40.076  1.00 10.45           O  
-ATOM   2142  CB  LEU A 262      94.981 140.661  41.379  1.00 12.36           C  
-ATOM   2143  CG  LEU A 262      96.021 140.562  42.507  1.00 11.77           C  
-ATOM   2144  CD1 LEU A 262      97.169 141.511  42.243  1.00 12.90           C  
-ATOM   2145  CD2 LEU A 262      95.371 140.900  43.842  1.00 14.33           C  
-ATOM   2146  N   LEU A 263      95.410 137.862  40.046  1.00 11.58           N  
-ATOM   2147  CA  LEU A 263      96.049 136.550  40.146  1.00 13.54           C  
-ATOM   2148  C   LEU A 263      96.972 136.289  38.963  1.00 13.29           C  
-ATOM   2149  O   LEU A 263      98.085 135.759  39.129  1.00 12.05           O  
-ATOM   2150  CB  LEU A 263      95.007 135.435  40.236  1.00 13.78           C  
-ATOM   2151  CG  LEU A 263      95.579 134.027  40.446  1.00 14.31           C  
-ATOM   2152  CD1 LEU A 263      96.432 133.909  41.708  1.00 14.98           C  
-ATOM   2153  CD2 LEU A 263      94.394 133.094  40.546  1.00 15.63           C  
-ATOM   2154  N   SER A 264      96.504 136.642  37.768  1.00 14.23           N  
-ATOM   2155  CA  SER A 264      97.302 136.436  36.564  1.00 15.36           C  
-ATOM   2156  C   SER A 264      98.597 137.253  36.610  1.00 14.88           C  
-ATOM   2157  O   SER A 264      99.636 136.823  36.105  1.00 14.49           O  
-ATOM   2158  CB  SER A 264      96.473 136.768  35.304  1.00 18.41           C  
-ATOM   2159  OG  SER A 264      96.167 138.149  35.206  1.00 24.84           O  
-ATOM   2160  N   GLN A 265      98.556 138.422  37.236  1.00 12.86           N  
-ATOM   2161  CA  GLN A 265      99.762 139.230  37.327  1.00 13.18           C  
-ATOM   2162  C   GLN A 265     100.739 138.657  38.344  1.00 12.19           C  
-ATOM   2163  O   GLN A 265     101.947 138.806  38.187  1.00 12.14           O  
-ATOM   2164  CB  GLN A 265      99.391 140.680  37.656  1.00 16.11           C  
-ATOM   2165  CG  GLN A 265      98.650 141.324  36.467  1.00 17.88           C  
-ATOM   2166  CD  GLN A 265      98.291 142.770  36.702  1.00 22.72           C  
-ATOM   2167  OE1 GLN A 265      99.176 143.630  36.855  1.00 23.57           O  
-ATOM   2168  NE2 GLN A 265      96.994 143.059  36.722  1.00 24.96           N  
-ATOM   2169  N   MET A 266     100.219 137.962  39.357  1.00 10.71           N  
-ATOM   2170  CA  MET A 266     101.080 137.364  40.382  1.00 11.30           C  
-ATOM   2171  C   MET A 266     101.681 136.039  39.913  1.00 11.15           C  
-ATOM   2172  O   MET A 266     102.746 135.655  40.364  1.00 11.38           O  
-ATOM   2173  CB  MET A 266     100.285 137.135  41.680  1.00 11.34           C  
-ATOM   2174  CG  MET A 266      99.817 138.450  42.327  1.00 13.18           C  
-ATOM   2175  SD  MET A 266      98.861 138.132  43.827  1.00 14.40           S  
-ATOM   2176  CE  MET A 266     100.218 137.807  44.993  1.00 15.83           C  
-ATOM   2177  N   LEU A 267     101.000 135.367  38.986  1.00 11.15           N  
-ATOM   2178  CA  LEU A 267     101.472 134.093  38.455  1.00 11.65           C  
-ATOM   2179  C   LEU A 267     102.060 134.203  37.041  1.00 12.13           C  
-ATOM   2180  O   LEU A 267     102.141 133.229  36.300  1.00 12.33           O  
-ATOM   2181  CB  LEU A 267     100.336 133.054  38.505  1.00 11.22           C  
-ATOM   2182  CG  LEU A 267      99.828 132.691  39.919  1.00 11.74           C  
-ATOM   2183  CD1 LEU A 267      98.713 131.662  39.822  1.00 12.17           C  
-ATOM   2184  CD2 LEU A 267     100.964 132.145  40.792  1.00 12.05           C  
-ATOM   2185  N   HIS A 268     102.496 135.392  36.660  1.00 12.25           N  
-ATOM   2186  CA  HIS A 268     103.075 135.534  35.347  1.00 13.52           C  
-ATOM   2187  C   HIS A 268     104.367 134.697  35.334  1.00 13.60           C  
-ATOM   2188  O   HIS A 268     105.115 134.690  36.305  1.00 12.62           O  
-ATOM   2189  CB  HIS A 268     103.370 137.004  35.095  1.00 16.71           C  
-ATOM   2190  CG  HIS A 268     103.626 137.330  33.667  1.00 20.44           C  
-ATOM   2191  ND1 HIS A 268     104.757 136.902  33.005  1.00 21.52           N  
-ATOM   2192  CD2 HIS A 268     102.918 138.064  32.777  1.00 21.12           C  
-ATOM   2193  CE1 HIS A 268     104.737 137.366  31.766  1.00 24.26           C  
-ATOM   2194  NE2 HIS A 268     103.633 138.075  31.603  1.00 24.17           N  
-ATOM   2195  N   TYR A 269     104.625 133.979  34.250  1.00 12.34           N  
-ATOM   2196  CA  TYR A 269     105.838 133.156  34.185  1.00 12.11           C  
-ATOM   2197  C   TYR A 269     107.114 133.960  34.280  1.00 12.16           C  
-ATOM   2198  O   TYR A 269     108.042 133.603  35.000  1.00 13.94           O  
-ATOM   2199  CB  TYR A 269     105.886 132.373  32.868  1.00 12.38           C  
-ATOM   2200  CG  TYR A 269     105.174 131.030  32.921  1.00 12.20           C  
-ATOM   2201  CD1 TYR A 269     105.626 130.029  33.770  1.00 11.74           C  
-ATOM   2202  CD2 TYR A 269     104.075 130.759  32.106  1.00 12.87           C  
-ATOM   2203  CE1 TYR A 269     105.002 128.775  33.811  1.00 13.00           C  
-ATOM   2204  CE2 TYR A 269     103.436 129.501  32.137  1.00 13.25           C  
-ATOM   2205  CZ  TYR A 269     103.916 128.517  33.003  1.00 14.22           C  
-ATOM   2206  OH  TYR A 269     103.316 127.273  33.092  1.00 14.81           O  
-ATOM   2207  N   ASP A 270     107.173 135.032  33.505  1.00 13.63           N  
-ATOM   2208  CA  ASP A 270     108.378 135.859  33.470  1.00 14.32           C  
-ATOM   2209  C   ASP A 270     108.534 136.714  34.731  1.00 14.84           C  
-ATOM   2210  O   ASP A 270     107.734 137.631  34.986  1.00 14.21           O  
-ATOM   2211  CB  ASP A 270     108.304 136.731  32.220  1.00 13.66           C  
-ATOM   2212  CG  ASP A 270     109.563 137.523  31.971  1.00 15.37           C  
-ATOM   2213  OD1 ASP A 270     110.432 137.586  32.860  1.00 13.36           O  
-ATOM   2214  OD2 ASP A 270     109.662 138.098  30.864  1.00 19.25           O  
-ATOM   2215  N   PRO A 271     109.581 136.437  35.530  1.00 16.97           N  
-ATOM   2216  CA  PRO A 271     109.869 137.164  36.771  1.00 17.82           C  
-ATOM   2217  C   PRO A 271     109.901 138.670  36.537  1.00 19.22           C  
-ATOM   2218  O   PRO A 271     109.474 139.430  37.396  1.00 19.78           O  
-ATOM   2219  CB  PRO A 271     111.241 136.643  37.176  1.00 18.11           C  
-ATOM   2220  CG  PRO A 271     111.296 135.302  36.594  1.00 19.89           C  
-ATOM   2221  CD  PRO A 271     110.622 135.438  35.263  1.00 16.65           C  
-ATOM   2222  N   ASN A 272     110.405 139.083  35.370  1.00 18.97           N  
-ATOM   2223  CA  ASN A 272     110.510 140.504  35.016  1.00 21.15           C  
-ATOM   2224  C   ASN A 272     109.180 141.166  34.663  1.00 21.43           C  
-ATOM   2225  O   ASN A 272     109.111 142.387  34.528  1.00 22.76           O  
-ATOM   2226  CB  ASN A 272     111.474 140.696  33.833  1.00 22.89           C  
-ATOM   2227  CG  ASN A 272     112.904 140.377  34.186  1.00 24.42           C  
-ATOM   2228  OD1 ASN A 272     113.708 140.059  33.307  1.00 27.53           O  
-ATOM   2229  ND2 ASN A 272     113.243 140.469  35.467  1.00 23.57           N  
-ATOM   2230  N   LYS A 273     108.129 140.366  34.507  1.00 19.03           N  
-ATOM   2231  CA  LYS A 273     106.811 140.882  34.191  1.00 18.59           C  
-ATOM   2232  C   LYS A 273     105.837 140.657  35.351  1.00 17.40           C  
-ATOM   2233  O   LYS A 273     104.771 141.265  35.409  1.00 17.53           O  
-ATOM   2234  CB  LYS A 273     106.267 140.218  32.926  1.00 20.22           C  
-ATOM   2235  CG  LYS A 273     107.007 140.646  31.654  1.00 25.07           C  
-ATOM   2236  CD  LYS A 273     107.085 142.171  31.574  1.00 26.69           C  
-ATOM   2237  CE  LYS A 273     108.116 142.649  30.543  1.00 30.51           C  
-ATOM   2238  NZ  LYS A 273     108.434 144.106  30.736  1.00 31.43           N  
-ATOM   2239  N   ARG A 274     106.210 139.780  36.273  1.00 14.62           N  
-ATOM   2240  CA  ARG A 274     105.357 139.464  37.424  1.00 13.62           C  
-ATOM   2241  C   ARG A 274     105.158 140.735  38.241  1.00 12.37           C  
-ATOM   2242  O   ARG A 274     106.102 141.498  38.443  1.00 12.21           O  
-ATOM   2243  CB  ARG A 274     106.031 138.371  38.254  1.00 13.12           C  
-ATOM   2244  CG  ARG A 274     105.114 137.678  39.259  1.00 14.59           C  
-ATOM   2245  CD  ARG A 274     105.787 136.446  39.870  1.00 14.39           C  
-ATOM   2246  NE  ARG A 274     106.217 135.493  38.845  1.00 12.20           N  
-ATOM   2247  CZ  ARG A 274     107.293 134.717  38.943  1.00 13.33           C  
-ATOM   2248  NH1 ARG A 274     108.058 134.767  40.026  1.00 10.86           N  
-ATOM   2249  NH2 ARG A 274     107.627 133.903  37.940  1.00 12.23           N  
-ATOM   2250  N   ILE A 275     103.939 140.977  38.710  1.00 11.59           N  
-ATOM   2251  CA  ILE A 275     103.685 142.206  39.462  1.00 11.77           C  
-ATOM   2252  C   ILE A 275     104.533 142.284  40.750  1.00 12.30           C  
-ATOM   2253  O   ILE A 275     104.813 141.264  41.370  1.00 12.12           O  
-ATOM   2254  CB  ILE A 275     102.170 142.318  39.775  1.00 10.93           C  
-ATOM   2255  CG1 ILE A 275     101.827 143.737  40.241  1.00 11.48           C  
-ATOM   2256  CG2 ILE A 275     101.772 141.277  40.801  1.00 11.98           C  
-ATOM   2257  CD1 ILE A 275     100.348 144.038  40.226  1.00 14.40           C  
-ATOM   2258  N   SER A 276     104.970 143.484  41.142  1.00 11.85           N  
-ATOM   2259  CA  SER A 276     105.745 143.628  42.383  1.00 11.64           C  
-ATOM   2260  C   SER A 276     104.740 143.726  43.541  1.00 11.32           C  
-ATOM   2261  O   SER A 276     103.552 143.961  43.308  1.00 13.47           O  
-ATOM   2262  CB  SER A 276     106.590 144.915  42.354  1.00 13.91           C  
-ATOM   2263  OG  SER A 276     105.741 146.062  42.329  1.00 15.77           O  
-ATOM   2264  N   ALA A 277     105.196 143.560  44.781  1.00 10.61           N  
-ATOM   2265  CA  ALA A 277     104.299 143.677  45.925  1.00 12.51           C  
-ATOM   2266  C   ALA A 277     103.760 145.132  45.994  1.00 13.60           C  
-ATOM   2267  O   ALA A 277     102.571 145.365  46.185  1.00 14.02           O  
-ATOM   2268  CB  ALA A 277     105.049 143.324  47.230  1.00 14.48           C  
-ATOM   2269  N   LYS A 278     104.629 146.111  45.798  1.00 14.67           N  
-ATOM   2270  CA  LYS A 278     104.180 147.514  45.855  1.00 17.50           C  
-ATOM   2271  C   LYS A 278     103.078 147.804  44.822  1.00 17.71           C  
-ATOM   2272  O   LYS A 278     102.051 148.420  45.146  1.00 17.23           O  
-ATOM   2273  CB  LYS A 278     105.388 148.447  45.641  1.00 20.86           C  
-ATOM   2274  CG  LYS A 278     105.063 149.933  45.680  1.00 26.75           C  
-ATOM   2275  CD  LYS A 278     106.296 150.787  45.365  1.00 29.85           C  
-ATOM   2276  CE  LYS A 278     107.497 150.395  46.232  1.00 32.08           C  
-ATOM   2277  NZ  LYS A 278     108.684 151.298  46.013  1.00 35.05           N  
-ATOM   2278  N   ALA A 279     103.269 147.357  43.580  1.00 17.19           N  
-ATOM   2279  CA  ALA A 279     102.267 147.610  42.541  1.00 17.85           C  
-ATOM   2280  C   ALA A 279     100.957 146.850  42.780  1.00 16.43           C  
-ATOM   2281  O   ALA A 279      99.884 147.324  42.408  1.00 16.66           O  
-ATOM   2282  CB  ALA A 279     102.838 147.273  41.145  1.00 16.69           C  
-ATOM   2283  N   ALA A 280     101.043 145.665  43.389  1.00 14.52           N  
-ATOM   2284  CA  ALA A 280      99.847 144.887  43.665  1.00 14.79           C  
-ATOM   2285  C   ALA A 280      98.943 145.614  44.645  1.00 14.53           C  
-ATOM   2286  O   ALA A 280      97.723 145.525  44.543  1.00 14.42           O  
-ATOM   2287  CB  ALA A 280     100.213 143.493  44.228  1.00 13.05           C  
-ATOM   2288  N   LEU A 281      99.545 146.326  45.598  1.00 14.73           N  
-ATOM   2289  CA  LEU A 281      98.759 147.071  46.578  1.00 16.98           C  
-ATOM   2290  C   LEU A 281      97.813 148.084  45.920  1.00 17.66           C  
-ATOM   2291  O   LEU A 281      96.751 148.389  46.458  1.00 19.14           O  
-ATOM   2292  CB  LEU A 281      99.700 147.787  47.558  1.00 17.51           C  
-ATOM   2293  CG  LEU A 281     100.453 146.786  48.434  1.00 16.41           C  
-ATOM   2294  CD1 LEU A 281     101.608 147.479  49.175  1.00 21.08           C  
-ATOM   2295  CD2 LEU A 281      99.469 146.135  49.415  1.00 16.97           C  
-ATOM   2296  N   ALA A 282      98.192 148.590  44.755  1.00 18.80           N  
-ATOM   2297  CA  ALA A 282      97.360 149.567  44.031  1.00 19.05           C  
-ATOM   2298  C   ALA A 282      96.356 148.922  43.079  1.00 19.30           C  
-ATOM   2299  O   ALA A 282      95.622 149.629  42.375  1.00 19.46           O  
-ATOM   2300  CB  ALA A 282      98.257 150.542  43.238  1.00 19.87           C  
-ATOM   2301  N   HIS A 283      96.304 147.593  43.056  1.00 17.43           N  
-ATOM   2302  CA  HIS A 283      95.384 146.905  42.154  1.00 17.20           C  
-ATOM   2303  C   HIS A 283      93.926 147.164  42.529  1.00 17.80           C  
-ATOM   2304  O   HIS A 283      93.577 147.247  43.697  1.00 15.61           O  
-ATOM   2305  CB  HIS A 283      95.666 145.392  42.156  1.00 16.68           C  
-ATOM   2306  CG  HIS A 283      95.001 144.654  41.032  1.00 15.87           C  
-ATOM   2307  ND1 HIS A 283      93.664 144.319  41.048  1.00 14.83           N  
-ATOM   2308  CD2 HIS A 283      95.477 144.251  39.826  1.00 15.78           C  
-ATOM   2309  CE1 HIS A 283      93.340 143.749  39.898  1.00 16.82           C  
-ATOM   2310  NE2 HIS A 283      94.421 143.697  39.138  1.00 14.73           N  
-ATOM   2311  N   PRO A 284      93.051 147.304  41.525  1.00 18.29           N  
-ATOM   2312  CA  PRO A 284      91.625 147.549  41.777  1.00 18.86           C  
-ATOM   2313  C   PRO A 284      90.970 146.520  42.711  1.00 18.06           C  
-ATOM   2314  O   PRO A 284      89.951 146.799  43.347  1.00 19.75           O  
-ATOM   2315  CB  PRO A 284      91.029 147.524  40.370  1.00 18.78           C  
-ATOM   2316  CG  PRO A 284      92.130 148.104  39.550  1.00 21.17           C  
-ATOM   2317  CD  PRO A 284      93.354 147.391  40.084  1.00 18.70           C  
-ATOM   2318  N   PHE A 285      91.549 145.330  42.799  1.00 18.22           N  
-ATOM   2319  CA  PHE A 285      91.006 144.280  43.665  1.00 17.94           C  
-ATOM   2320  C   PHE A 285      90.920 144.746  45.122  1.00 18.03           C  
-ATOM   2321  O   PHE A 285      90.072 144.283  45.893  1.00 18.10           O  
-ATOM   2322  CB  PHE A 285      91.893 143.023  43.598  1.00 17.89           C  
-ATOM   2323  CG  PHE A 285      91.350 141.844  44.367  1.00 18.38           C  
-ATOM   2324  CD1 PHE A 285      90.142 141.238  44.000  1.00 18.21           C  
-ATOM   2325  CD2 PHE A 285      92.060 141.316  45.440  1.00 18.13           C  
-ATOM   2326  CE1 PHE A 285      89.664 140.126  44.693  1.00 18.32           C  
-ATOM   2327  CE2 PHE A 285      91.591 140.210  46.136  1.00 18.64           C  
-ATOM   2328  CZ  PHE A 285      90.387 139.612  45.762  1.00 17.90           C  
-ATOM   2329  N   PHE A 286      91.796 145.668  45.484  1.00 17.72           N  
-ATOM   2330  CA  PHE A 286      91.857 146.161  46.852  1.00 18.49           C  
-ATOM   2331  C   PHE A 286      91.100 147.460  47.125  1.00 20.40           C  
-ATOM   2332  O   PHE A 286      91.246 148.033  48.198  1.00 19.17           O  
-ATOM   2333  CB  PHE A 286      93.328 146.330  47.248  1.00 16.10           C  
-ATOM   2334  CG  PHE A 286      94.094 145.037  47.265  1.00 16.21           C  
-ATOM   2335  CD1 PHE A 286      93.694 143.994  48.090  1.00 14.72           C  
-ATOM   2336  CD2 PHE A 286      95.191 144.849  46.426  1.00 16.18           C  
-ATOM   2337  CE1 PHE A 286      94.370 142.771  48.082  1.00 16.03           C  
-ATOM   2338  CE2 PHE A 286      95.877 143.634  46.408  1.00 15.29           C  
-ATOM   2339  CZ  PHE A 286      95.467 142.590  47.238  1.00 13.82           C  
-ATOM   2340  N   GLN A 287      90.293 147.910  46.168  1.00 21.26           N  
-ATOM   2341  CA  GLN A 287      89.544 149.151  46.338  1.00 25.16           C  
-ATOM   2342  C   GLN A 287      88.732 149.206  47.622  1.00 25.21           C  
-ATOM   2343  O   GLN A 287      88.686 150.236  48.293  1.00 26.69           O  
-ATOM   2344  CB  GLN A 287      88.580 149.366  45.170  1.00 26.88           C  
-ATOM   2345  CG  GLN A 287      89.253 149.563  43.842  1.00 32.77           C  
-ATOM   2346  CD  GLN A 287      88.253 149.775  42.714  1.00 33.77           C  
-ATOM   2347  OE1 GLN A 287      87.355 148.955  42.490  1.00 35.73           O  
-ATOM   2348  NE2 GLN A 287      88.412 150.872  41.996  1.00 35.68           N  
-ATOM   2349  N   ASP A 288      88.084 148.094  47.942  1.00 25.77           N  
-ATOM   2350  CA  ASP A 288      87.217 147.995  49.112  1.00 26.92           C  
-ATOM   2351  C   ASP A 288      87.806 147.163  50.244  1.00 25.98           C  
-ATOM   2352  O   ASP A 288      87.056 146.535  51.009  1.00 26.16           O  
-ATOM   2353  CB  ASP A 288      85.903 147.347  48.692  1.00 28.01           C  
-ATOM   2354  CG  ASP A 288      86.085 145.891  48.324  1.00 30.30           C  
-ATOM   2355  OD1 ASP A 288      87.159 145.567  47.759  1.00 31.38           O  
-ATOM   2356  OD2 ASP A 288      85.170 145.079  48.586  1.00 30.97           O  
-ATOM   2357  N   VAL A 289      89.128 147.133  50.364  1.00 25.02           N  
-ATOM   2358  CA  VAL A 289      89.707 146.327  51.432  1.00 24.77           C  
-ATOM   2359  C   VAL A 289      89.443 146.898  52.826  1.00 25.02           C  
-ATOM   2360  O   VAL A 289      89.484 148.105  53.023  1.00 24.84           O  
-ATOM   2361  CB  VAL A 289      91.226 146.148  51.257  1.00 25.08           C  
-ATOM   2362  CG1 VAL A 289      91.954 147.472  51.422  1.00 24.73           C  
-ATOM   2363  CG2 VAL A 289      91.721 145.137  52.256  1.00 25.26           C  
-ATOM   2364  N   THR A 290      89.178 146.008  53.782  1.00 25.89           N  
-ATOM   2365  CA  THR A 290      88.929 146.385  55.170  1.00 28.43           C  
-ATOM   2366  C   THR A 290      89.741 145.455  56.061  1.00 29.42           C  
-ATOM   2367  O   THR A 290      90.569 144.687  55.568  1.00 29.23           O  
-ATOM   2368  CB  THR A 290      87.445 146.225  55.549  1.00 29.28           C  
-ATOM   2369  OG1 THR A 290      87.062 144.843  55.445  1.00 29.79           O  
-ATOM   2370  CG2 THR A 290      86.577 147.069  54.637  1.00 30.15           C  
-ATOM   2371  N   LYS A 291      89.511 145.525  57.372  1.00 30.34           N  
-ATOM   2372  CA  LYS A 291      90.224 144.648  58.294  1.00 31.87           C  
-ATOM   2373  C   LYS A 291      89.253 143.845  59.167  1.00 33.03           C  
-ATOM   2374  O   LYS A 291      89.004 144.187  60.329  1.00 33.36           O  
-ATOM   2375  CB  LYS A 291      91.182 145.449  59.178  1.00 32.31           C  
-ATOM   2376  CG  LYS A 291      92.194 144.556  59.902  1.00 33.24           C  
-ATOM   2377  CD  LYS A 291      93.126 145.342  60.812  1.00 34.59           C  
-ATOM   2378  CE  LYS A 291      94.094 144.395  61.512  1.00 35.00           C  
-ATOM   2379  NZ  LYS A 291      94.888 145.050  62.592  1.00 36.80           N  
-ATOM   2380  N   PRO A 292      88.684 142.763  58.609  1.00 33.94           N  
-ATOM   2381  CA  PRO A 292      87.741 141.908  59.331  1.00 34.59           C  
-ATOM   2382  C   PRO A 292      88.497 141.158  60.418  1.00 35.89           C  
-ATOM   2383  O   PRO A 292      89.711 141.001  60.326  1.00 34.92           O  
-ATOM   2384  CB  PRO A 292      87.239 140.942  58.252  1.00 34.59           C  
-ATOM   2385  CG  PRO A 292      87.570 141.628  56.953  1.00 34.23           C  
-ATOM   2386  CD  PRO A 292      88.890 142.261  57.240  1.00 33.85           C  
-ATOM   2387  N   VAL A 293      87.785 140.717  61.450  1.00 37.19           N  
-ATOM   2388  CA  VAL A 293      88.412 139.942  62.512  1.00 38.69           C  
-ATOM   2389  C   VAL A 293      88.012 138.497  62.262  1.00 39.83           C  
-ATOM   2390  O   VAL A 293      86.869 138.214  61.917  1.00 40.41           O  
-ATOM   2391  CB  VAL A 293      87.935 140.379  63.915  1.00 38.12           C  
-ATOM   2392  CG1 VAL A 293      88.567 141.720  64.284  1.00 37.12           C  
-ATOM   2393  CG2 VAL A 293      86.417 140.477  63.945  1.00 37.53           C  
-ATOM   2394  N   PRO A 294      88.955 137.560  62.413  1.00 41.65           N  
-ATOM   2395  CA  PRO A 294      88.626 136.151  62.179  1.00 43.09           C  
-ATOM   2396  C   PRO A 294      87.819 135.494  63.290  1.00 45.75           C  
-ATOM   2397  O   PRO A 294      87.866 135.915  64.447  1.00 44.54           O  
-ATOM   2398  CB  PRO A 294      89.995 135.507  62.035  1.00 42.47           C  
-ATOM   2399  CG  PRO A 294      90.822 136.308  63.004  1.00 41.79           C  
-ATOM   2400  CD  PRO A 294      90.392 137.725  62.702  1.00 41.01           C  
-ATOM   2401  N   HIS A 295      87.066 134.462  62.927  1.00 48.74           N  
-ATOM   2402  CA  HIS A 295      86.309 133.721  63.919  1.00 52.33           C  
-ATOM   2403  C   HIS A 295      87.220 132.572  64.324  1.00 53.88           C  
-ATOM   2404  O   HIS A 295      87.395 131.616  63.569  1.00 54.22           O  
-ATOM   2405  CB  HIS A 295      85.013 133.160  63.337  1.00 53.22           C  
-ATOM   2406  CG  HIS A 295      84.248 132.318  64.308  1.00 54.52           C  
-ATOM   2407  ND1 HIS A 295      83.766 132.813  65.501  1.00 54.77           N  
-ATOM   2408  CD2 HIS A 295      83.927 131.002  64.290  1.00 54.96           C  
-ATOM   2409  CE1 HIS A 295      83.184 131.839  66.177  1.00 55.54           C  
-ATOM   2410  NE2 HIS A 295      83.268 130.729  65.465  1.00 55.32           N  
-ATOM   2411  N   LEU A 296      87.817 132.680  65.505  1.00 56.22           N  
-ATOM   2412  CA  LEU A 296      88.727 131.650  65.999  1.00 58.89           C  
-ATOM   2413  C   LEU A 296      88.142 130.954  67.228  1.00 61.07           C  
-ATOM   2414  O   LEU A 296      88.096 131.532  68.317  1.00 61.10           O  
-ATOM   2415  CB  LEU A 296      90.076 132.278  66.365  1.00 58.03           C  
-ATOM   2416  CG  LEU A 296      90.712 133.246  65.362  1.00 57.60           C  
-ATOM   2417  CD1 LEU A 296      91.948 133.882  65.979  1.00 57.19           C  
-ATOM   2418  CD2 LEU A 296      91.068 132.507  64.085  1.00 57.25           C  
-ATOM   2419  N   ARG A 297      87.693 129.714  67.054  1.00 63.95           N  
-ATOM   2420  CA  ARG A 297      87.123 128.955  68.162  1.00 66.62           C  
-ATOM   2421  C   ARG A 297      88.076 127.838  68.568  1.00 68.03           C  
-ATOM   2422  O   ARG A 297      87.842 126.667  68.260  1.00 68.52           O  
-ATOM   2423  CB  ARG A 297      85.770 128.359  67.763  1.00 67.64           C  
-ATOM   2424  CG  ARG A 297      85.083 127.588  68.882  1.00 69.12           C  
-ATOM   2425  CD  ARG A 297      83.696 127.113  68.470  1.00 70.43           C  
-ATOM   2426  NE  ARG A 297      82.997 126.460  69.575  1.00 71.48           N  
-ATOM   2427  CZ  ARG A 297      81.739 126.027  69.520  1.00 72.12           C  
-ATOM   2428  NH1 ARG A 297      81.026 126.174  68.410  1.00 72.22           N  
-ATOM   2429  NH2 ARG A 297      81.191 125.445  70.580  1.00 72.37           N  
-ATOM   2430  N   LEU A 298      89.150 128.207  69.264  1.00 69.24           N  
-ATOM   2431  CA  LEU A 298      90.152 127.236  69.706  1.00 70.34           C  
-ATOM   2432  C   LEU A 298      89.719 126.405  70.915  1.00 70.60           C  
-ATOM   2433  O   LEU A 298      88.650 126.697  71.494  1.00 70.83           O  
-ATOM   2434  CB  LEU A 298      91.473 127.955  70.019  1.00 70.73           C  
-ATOM   2435  CG  LEU A 298      91.465 129.116  71.022  1.00 71.13           C  
-ATOM   2436  CD1 LEU A 298      91.044 128.635  72.410  1.00 71.23           C  
-ATOM   2437  CD2 LEU A 298      92.858 129.728  71.076  1.00 71.24           C  
-ATOM   2438  OXT LEU A 298      90.468 125.470  71.274  1.00 70.95           O  
-TER    2439      LEU A 298                                                      
-HETATM 2440  C1  EDO A 299      92.593 125.409  52.127  1.00 33.54           C  
-HETATM 2441  O1  EDO A 299      91.690 124.614  52.899  1.00 33.53           O  
-HETATM 2442  C2  EDO A 299      93.672 124.510  51.518  1.00 32.37           C  
-HETATM 2443  O2  EDO A 299      94.710 124.327  52.464  1.00 32.49           O  
-HETATM 2444  C1  EDO A 300     120.491 138.689  75.941  1.00 29.67           C  
-HETATM 2445  O1  EDO A 300     121.086 137.855  74.927  1.00 32.32           O  
-HETATM 2446  C2  EDO A 300     119.177 138.056  76.416  1.00 28.08           C  
-HETATM 2447  O2  EDO A 300     118.468 138.970  77.255  1.00 26.09           O  
-HETATM 2448  C1  EDO A 301     101.623 116.112  35.718  1.00 48.44           C  
-HETATM 2449  O1  EDO A 301     102.201 116.202  37.023  1.00 48.77           O  
-HETATM 2450  C2  EDO A 301     100.479 117.116  35.601  1.00 48.25           C  
-HETATM 2451  O2  EDO A 301     100.114 117.254  34.228  1.00 48.13           O  
-HETATM 2452  C1  EDO A 302     118.682 126.154  78.825  1.00 52.48           C  
-HETATM 2453  O1  EDO A 302     117.515 126.206  79.651  1.00 53.56           O  
-HETATM 2454  C2  EDO A 302     119.923 126.010  79.706  1.00 52.82           C  
-HETATM 2455  O2  EDO A 302     120.917 126.949  79.291  1.00 51.97           O  
-HETATM 2456  C1  EDO A 303      83.125 134.417  38.117  1.00 50.96           C  
-HETATM 2457  O1  EDO A 303      83.529 135.683  37.585  1.00 50.33           O  
-HETATM 2458  C2  EDO A 303      82.714 134.578  39.579  1.00 50.60           C  
-HETATM 2459  O2  EDO A 303      81.766 133.563  39.918  1.00 51.33           O  
-HETATM 2460  C1  2AN A 304     122.806 133.739  64.752  1.00 25.13           C  
-HETATM 2461  C2  2AN A 304     123.169 132.548  64.039  1.00 25.61           C  
-HETATM 2462  C3  2AN A 304     122.196 131.726  63.446  1.00 25.81           C  
-HETATM 2463  C4  2AN A 304     120.837 132.057  63.531  1.00 24.93           C  
-HETATM 2464  C5  2AN A 304     120.399 133.220  64.213  1.00 24.15           C  
-HETATM 2465  C6  2AN A 304     119.011 133.529  64.276  1.00 23.35           C  
-HETATM 2466  C7  2AN A 304     118.546 134.670  64.942  1.00 21.88           C  
-HETATM 2467  C8  2AN A 304     119.453 135.537  65.567  1.00 23.70           C  
-HETATM 2468  N   2AN A 304     123.748 134.479  65.289  1.00 25.69           N  
-HETATM 2469  S   2AN A 304     121.864 136.476  66.395  1.00 24.26           S  
-HETATM 2470  C9  2AN A 304     120.846 135.287  65.542  1.00 23.61           C  
-HETATM 2471  C10 2AN A 304     121.381 134.111  64.855  1.00 24.11           C  
-HETATM 2472  C11 2AN A 304     124.691 134.093  66.135  1.00 26.62           C  
-HETATM 2473  C12 2AN A 304     124.623 132.874  66.908  1.00 27.75           C  
-HETATM 2474  C13 2AN A 304     125.675 132.527  67.810  1.00 28.95           C  
-HETATM 2475  C14 2AN A 304     126.800 133.392  67.949  1.00 29.00           C  
-HETATM 2476  C15 2AN A 304     126.872 134.592  67.190  1.00 29.19           C  
-HETATM 2477  C16 2AN A 304     125.824 134.940  66.291  1.00 28.29           C  
-HETATM 2478  O1  2AN A 304     122.793 137.072  65.461  1.00 22.37           O  
-HETATM 2479  O2  2AN A 304     122.548 135.772  67.465  1.00 24.82           O  
-HETATM 2480  O3  2AN A 304     120.901 137.633  67.054  1.00 24.58           O  
-HETATM 2481  C1  2AN A 305     114.777 134.792  62.228  1.00 20.23           C  
-HETATM 2482  C2  2AN A 305     116.053 135.437  62.457  1.00 19.23           C  
-HETATM 2483  C3  2AN A 305     116.162 136.815  62.691  1.00 17.49           C  
-HETATM 2484  C4  2AN A 305     115.019 137.627  62.703  1.00 18.08           C  
-HETATM 2485  C5  2AN A 305     113.723 137.077  62.485  1.00 17.35           C  
-HETATM 2486  C6  2AN A 305     112.591 137.932  62.503  1.00 17.18           C  
-HETATM 2487  C7  2AN A 305     111.293 137.434  62.298  1.00 18.26           C  
-HETATM 2488  C8  2AN A 305     111.088 136.060  62.073  1.00 17.42           C  
-HETATM 2489  N   2AN A 305     114.721 133.477  62.005  1.00 21.81           N  
-HETATM 2490  S   2AN A 305     111.719 133.444  61.760  1.00 17.30           S  
-HETATM 2491  C9  2AN A 305     112.176 135.144  62.041  1.00 16.95           C  
-HETATM 2492  C10 2AN A 305     113.560 135.620  62.243  1.00 17.32           C  
-HETATM 2493  C11 2AN A 305     115.764 132.668  61.797  1.00 21.69           C  
-HETATM 2494  C12 2AN A 305     115.949 131.545  62.651  1.00 22.12           C  
-HETATM 2495  C13 2AN A 305     117.046 130.652  62.461  1.00 21.92           C  
-HETATM 2496  C14 2AN A 305     117.980 130.871  61.407  1.00 20.78           C  
-HETATM 2497  C15 2AN A 305     117.816 131.984  60.541  1.00 21.81           C  
-HETATM 2498  C16 2AN A 305     116.718 132.882  60.725  1.00 21.91           C  
-HETATM 2499  O1  2AN A 305     112.340 132.560  62.767  1.00 17.60           O  
-HETATM 2500  O2  2AN A 305     112.173 133.041  60.430  1.00 13.89           O  
-HETATM 2501  O3  2AN A 305     110.106 133.344  61.880  1.00 18.61           O  
-HETATM 2502  O   HOH A 306     107.967 143.152  45.235  1.00 11.13           O  
-HETATM 2503  O   HOH A 307     112.940 135.618  40.105  1.00 16.13           O  
-HETATM 2504  O   HOH A 308     108.466 132.434  48.898  1.00 10.19           O  
-HETATM 2505  O   HOH A 309      98.309 126.991  46.720  1.00 13.40           O  
-HETATM 2506  O   HOH A 310     107.597 145.789  45.689  1.00 15.48           O  
-HETATM 2507  O   HOH A 311     107.579 140.586  41.319  1.00 15.56           O  
-HETATM 2508  O   HOH A 312     109.129 142.081  43.033  1.00 14.02           O  
-HETATM 2509  O   HOH A 313     104.302 126.608  42.606  1.00 14.41           O  
-HETATM 2510  O   HOH A 314      93.842 137.672  62.045  1.00 19.21           O  
-HETATM 2511  O   HOH A 315      91.873 141.361  58.852  1.00 17.82           O  
-HETATM 2512  O   HOH A 316     100.288 125.615  45.132  1.00 14.11           O  
-HETATM 2513  O   HOH A 317     108.953 130.866  45.217  1.00 14.46           O  
-HETATM 2514  O   HOH A 318     108.123 143.139  63.317  1.00 18.28           O  
-HETATM 2515  O   HOH A 319     100.887 132.724  33.872  1.00 22.05           O  
-HETATM 2516  O   HOH A 320     114.992 141.220  43.230  1.00 17.53           O  
-HETATM 2517  O   HOH A 321     103.824 138.113  73.301  1.00 20.42           O  
-HETATM 2518  O   HOH A 322     102.645 134.130  32.059  1.00 19.13           O  
-HETATM 2519  O   HOH A 323      88.445 143.536  53.009  1.00 23.33           O  
-HETATM 2520  O   HOH A 324      87.137 132.975  37.922  1.00 22.63           O  
-HETATM 2521  O   HOH A 325     117.063 138.185  51.626  1.00 21.74           O  
-HETATM 2522  O   HOH A 326     109.010 146.966  47.771  1.00 20.44           O  
-HETATM 2523  O   HOH A 327     112.667 141.626  62.600  1.00 20.98           O  
-HETATM 2524  O   HOH A 328     114.776 135.420  38.235  1.00 27.83           O  
-HETATM 2525  O   HOH A 329      94.732 123.229  40.847  1.00 23.64           O  
-HETATM 2526  O   HOH A 330     116.123 124.541  24.606  1.00 24.01           O  
-HETATM 2527  O   HOH A 331     104.933 145.716  38.993  1.00 16.75           O  
-HETATM 2528  O   HOH A 332     116.630 139.840  33.448  1.00 21.44           O  
-HETATM 2529  O   HOH A 333     100.002 124.082  52.715  1.00 25.41           O  
-HETATM 2530  O   HOH A 334     101.765 125.407  54.686  1.00 19.19           O  
-HETATM 2531  O   HOH A 335     108.974 141.295  39.133  1.00 23.43           O  
-HETATM 2532  O   HOH A 336     116.393 131.621  25.231  1.00 24.42           O  
-HETATM 2533  O   HOH A 337      93.487 145.148  56.017  1.00 26.75           O  
-HETATM 2534  O   HOH A 338     104.606 142.803  64.312  1.00 24.66           O  
-HETATM 2535  O   HOH A 339      87.172 123.512  38.155  1.00 23.82           O  
-HETATM 2536  O   HOH A 340     119.006 144.828  64.663  1.00 22.71           O  
-HETATM 2537  O   HOH A 341     103.922 149.055  55.015  1.00 27.10           O  
-HETATM 2538  O   HOH A 342     114.924 134.078  53.758  1.00 27.44           O  
-HETATM 2539  O   HOH A 343     115.266 136.223  54.685  1.00 23.93           O  
-HETATM 2540  O   HOH A 344      95.088 121.486  49.721  1.00 23.90           O  
-HETATM 2541  O   HOH A 345     121.850 123.573  30.877  1.00 23.95           O  
-HETATM 2542  O   HOH A 346      97.835 120.219  40.071  1.00 28.45           O  
-HETATM 2543  O   HOH A 347      95.990 116.714  42.037  1.00 23.43           O  
-HETATM 2544  O   HOH A 348     107.232 113.339  55.728  1.00 24.92           O  
-HETATM 2545  O   HOH A 349     119.661 119.447  33.633  1.00 36.93           O  
-HETATM 2546  O   HOH A 350     109.734 129.075  22.397  1.00 22.39           O  
-HETATM 2547  O   HOH A 351     122.085 135.682  75.830  1.00 20.70           O  
-HETATM 2548  O   HOH A 352     119.462 131.370  34.675  1.00 31.27           O  
-HETATM 2549  O   HOH A 353     108.046 111.845  43.962  1.00 26.53           O  
-HETATM 2550  O   HOH A 354      99.319 131.535  31.920  1.00 28.96           O  
-HETATM 2551  O   HOH A 355     121.011 135.356  78.650  1.00 23.76           O  
-HETATM 2552  O   HOH A 356     111.460 124.061  23.264  1.00 21.23           O  
-HETATM 2553  O   HOH A 357     119.654 130.779  79.542  1.00 24.61           O  
-HETATM 2554  O   HOH A 358      89.690 126.696  53.459  1.00 29.92           O  
-HETATM 2555  O   HOH A 359      93.093 124.657  43.864  1.00 23.33           O  
-HETATM 2556  O   HOH A 360      84.103 130.574  37.195  1.00 22.97           O  
-HETATM 2557  O   HOH A 361     117.533 132.000  30.131  1.00 24.11           O  
-HETATM 2558  O   HOH A 362     106.758 144.204  37.741  1.00 28.84           O  
-HETATM 2559  O   HOH A 363     120.591 143.695  62.734  1.00 18.64           O  
-HETATM 2560  O   HOH A 364     107.356 127.749  50.021  1.00 20.95           O  
-HETATM 2561  O   HOH A 365      88.558 132.618  32.774  1.00 28.42           O  
-HETATM 2562  O   HOH A 366     111.138 139.841  29.841  1.00 31.57           O  
-HETATM 2563  O   HOH A 367      95.071 140.461  68.557  1.00 33.74           O  
-HETATM 2564  O   HOH A 368      99.421 134.996  33.973  1.00 25.06           O  
-HETATM 2565  O   HOH A 369     101.410 130.287  29.073  1.00 24.34           O  
-HETATM 2566  O   HOH A 370     112.895 148.042  59.900  1.00 25.04           O  
-HETATM 2567  O   HOH A 371     103.453 117.678  24.149  1.00 30.89           O  
-HETATM 2568  O   HOH A 372      95.961 145.558  36.754  1.00 27.66           O  
-HETATM 2569  O   HOH A 373     117.565 138.345  55.053  1.00 26.29           O  
-HETATM 2570  O   HOH A 374     108.175 130.179  62.146  1.00 39.19           O  
-HETATM 2571  O   HOH A 375      94.717 121.118  43.232  1.00 26.20           O  
-HETATM 2572  O   HOH A 376      87.470 144.439  43.173  1.00 27.14           O  
-HETATM 2573  O   HOH A 377      84.035 139.034  36.259  1.00 29.87           O  
-HETATM 2574  O   HOH A 378     111.339 128.312  56.040  1.00 24.61           O  
-HETATM 2575  O   HOH A 379     112.358 116.725  43.331  1.00 26.77           O  
-HETATM 2576  O   HOH A 380     104.263 114.252  36.800  1.00 34.51           O  
-HETATM 2577  O   HOH A 381     114.127 124.806  22.523  1.00 25.59           O  
-HETATM 2578  O   HOH A 382     110.090 115.869  29.304  1.00 21.25           O  
-HETATM 2579  O   HOH A 383      96.415 122.031  29.941  1.00 26.24           O  
-HETATM 2580  O   HOH A 384     112.216 116.059  39.863  1.00 18.62           O  
-HETATM 2581  O   HOH A 386     102.693 136.797  85.773  1.00 39.37           O  
-HETATM 2582  O   HOH A 387     119.222 134.520  36.720  1.00 31.08           O  
-HETATM 2583  O   HOH A 388     121.787 132.750  78.668  1.00 21.57           O  
-HETATM 2584  O   HOH A 389     110.014 144.155  41.692  1.00 28.83           O  
-HETATM 2585  O   HOH A 390     113.530 127.141  54.720  1.00 33.41           O  
-HETATM 2586  O   HOH A 391      87.310 130.665  50.477  1.00 23.21           O  
-HETATM 2587  O   HOH A 392     109.863 150.359  60.765  1.00 31.84           O  
-HETATM 2588  O   HOH A 393     107.212 138.288  28.995  1.00 30.95           O  
-HETATM 2589  O   HOH A 394      89.404 129.225  52.576  1.00 27.92           O  
-HETATM 2590  O   HOH A 395     114.732 133.879  35.875  1.00 27.61           O  
-HETATM 2591  O   HOH A 396      86.816 137.829  32.781  1.00 30.80           O  
-HETATM 2592  O   HOH A 397      87.637 147.254  58.967  1.00 34.05           O  
-HETATM 2593  O   HOH A 398     107.795 138.343  24.200  1.00 34.43           O  
-HETATM 2594  O   HOH A 399     122.371 141.733  63.855  1.00 29.09           O  
-HETATM 2595  O   HOH A 400     117.401 124.414  64.474  1.00 28.53           O  
-HETATM 2596  O   HOH A 401     109.303 129.397  47.539  1.00 23.87           O  
-HETATM 2597  O   HOH A 402      97.900 121.348  37.471  1.00 29.36           O  
-HETATM 2598  O   HOH A 403     109.105 126.552  22.865  1.00 27.20           O  
-HETATM 2599  O   HOH A 404     110.347 136.355  22.820  1.00 35.10           O  
-HETATM 2600  O   HOH A 405     112.764 150.679  62.810  1.00 32.10           O  
-HETATM 2601  O   HOH A 406     110.407 141.206  63.679  1.00 34.56           O  
-HETATM 2602  O   HOH A 407      96.135 118.951  47.633  1.00 33.98           O  
-HETATM 2603  O   HOH A 408     117.563 133.448  34.874  1.00 31.23           O  
-HETATM 2604  O   HOH A 409     105.996 112.606  40.638  1.00 32.96           O  
-HETATM 2605  O   HOH A 410     119.815 140.728  50.430  1.00 25.73           O  
-HETATM 2606  O   HOH A 411     110.331 126.988  48.075  1.00 43.31           O  
-HETATM 2607  O   HOH A 412     108.513 125.833  25.491  1.00 26.86           O  
-HETATM 2608  O   HOH A 413      84.440 139.005  33.573  1.00 31.58           O  
-HETATM 2609  O   HOH A 415     108.383 121.401  24.567  1.00 36.77           O  
-HETATM 2610  O   HOH A 416      96.890 129.804  73.836  1.00 32.94           O  
-HETATM 2611  O   HOH A 417     112.383 141.040  39.047  1.00 41.83           O  
-HETATM 2612  O   HOH A 418     121.278 128.124  24.778  1.00 34.48           O  
-HETATM 2613  O   HOH A 419      96.287 116.029  44.641  1.00 27.05           O  
-HETATM 2614  O   HOH A 420     120.904 131.194  43.216  1.00 40.82           O  
-HETATM 2615  O   HOH A 421     108.130 128.001  63.314  1.00 38.37           O  
-HETATM 2616  O   HOH A 422      89.032 137.331  66.133  1.00 35.01           O  
-HETATM 2617  O   HOH A 423     116.901 135.132  86.556  1.00 28.17           O  
-HETATM 2618  O   HOH A 424     111.269 147.188  46.412  1.00 34.16           O  
-HETATM 2619  O   HOH A 425     110.596 111.740  43.476  1.00 33.95           O  
-HETATM 2620  O   HOH A 426     116.909 117.169  42.104  1.00 27.93           O  
-HETATM 2621  O   HOH A 427      99.296 146.312  57.783  1.00 29.62           O  
-HETATM 2622  O   HOH A 428     120.875 147.361  55.067  1.00 39.72           O  
-HETATM 2623  O   HOH A 429      97.541 113.859  41.965  1.00 34.36           O  
-HETATM 2624  O   HOH A 430     100.589 144.014  63.901  1.00 30.86           O  
-HETATM 2625  O   HOH A 431      86.435 142.286  44.067  1.00 43.11           O  
-HETATM 2626  O   HOH A 432     110.330 114.823  45.510  1.00 40.73           O  
-HETATM 2627  O   HOH A 433      97.472 144.627  60.167  1.00 37.30           O  
-HETATM 2628  O   HOH A 434     111.471 144.059  36.935  1.00 29.43           O  
-HETATM 2629  O   HOH A 435     109.442 143.932  39.274  1.00 31.44           O  
-HETATM 2630  O   HOH A 436     119.543 131.012  31.963  1.00 32.31           O  
-HETATM 2631  O   HOH A 437     117.465 127.890  41.296  1.00 32.14           O  
-HETATM 2632  O   HOH A 438     115.393 128.984  51.340  1.00 32.84           O  
-HETATM 2633  O   HOH A 439      83.691 137.638  42.733  1.00 38.97           O  
-HETATM 2634  O   HOH A 440     114.465 122.929  20.644  1.00 34.66           O  
-HETATM 2635  O   HOH A 441     100.097 133.211  29.165  1.00 35.32           O  
-HETATM 2636  O   HOH A 442     115.963 138.244  83.433  1.00 41.61           O  
-HETATM 2637  O   HOH A 443     128.271 134.685  38.625  1.00 43.30           O  
-HETATM 2638  O   HOH A 444     121.228 122.635  36.650  1.00 44.70           O  
-HETATM 2639  O   HOH A 445     123.516 131.806  80.319  1.00 32.53           O  
-HETATM 2640  O   HOH A 446     106.825 147.770  40.514  1.00 32.97           O  
-HETATM 2641  O   HOH A 447     100.244 124.465  60.352  1.00 40.07           O  
-HETATM 2642  O   HOH A 448     108.941 113.440  30.581  1.00 35.28           O  
-HETATM 2643  O   HOH A 449     114.476 145.130  65.358  1.00 40.68           O  
-HETATM 2644  O   HOH A 451     109.878 138.311  77.290  1.00 38.34           O  
-HETATM 2645  O   HOH A 452     113.655 142.439  40.532  1.00 30.37           O  
-HETATM 2646  O   HOH A 453      89.600 119.845  33.023  1.00 43.18           O  
-HETATM 2647  O   HOH A 454      92.427 123.830  62.088  1.00 32.98           O  
-HETATM 2648  O   HOH A 455      86.214 133.867  59.871  1.00 30.36           O  
-HETATM 2649  O   HOH A 456      91.534 145.126  36.796  1.00 40.86           O  
-HETATM 2650  O   HOH A 457      86.338 143.826  51.374  1.00 31.56           O  
-HETATM 2651  O   HOH A 458     112.976 135.204  23.091  1.00 30.60           O  
-HETATM 2652  O   HOH A 459      90.047 143.473  32.115  1.00 36.37           O  
-HETATM 2653  O   HOH A 460      85.209 136.099  44.724  1.00 41.34           O  
-HETATM 2654  O   HOH A 461      96.873 120.999  26.640  1.00 36.97           O  
-HETATM 2655  O   HOH A 462     118.460 124.327  23.198  1.00 32.64           O  
-HETATM 2656  O   HOH A 463     123.168 143.540  57.786  1.00 47.87           O  
-HETATM 2657  O   HOH A 464      87.355 137.994  42.443  1.00 28.94           O  
-HETATM 2658  O   HOH A 465      96.884 143.455  65.423  1.00 36.71           O  
-HETATM 2659  O   HOH A 467     109.330 124.875  55.142  1.00 40.45           O  
-HETATM 2660  O   HOH A 468      86.362 134.419  67.395  1.00 40.77           O  
-HETATM 2661  O   HOH A 469      96.087 113.589  45.592  1.00 33.57           O  
-HETATM 2662  O   HOH A 471      99.252 128.336  26.236  1.00 31.03           O  
-HETATM 2663  O   HOH A 473     108.046 132.347  64.256  1.00 36.51           O  
-HETATM 2664  O   HOH A 474     121.644 130.108  83.335  1.00 45.89           O  
-HETATM 2665  O   HOH A 476     101.922 143.369  36.127  1.00 36.13           O  
-HETATM 2666  O   HOH A 477      98.190 139.678  33.087  1.00 42.70           O  
-HETATM 2667  O   HOH A 478     114.125 142.164  65.506  1.00 38.88           O  
-HETATM 2668  O   HOH A 479      82.837 135.845  51.128  1.00 29.33           O  
-HETATM 2669  O   HOH A 480     116.090 139.829  85.381  1.00 44.67           O  
-HETATM 2670  O   HOH A 481     117.193 128.110  23.013  1.00 44.33           O  
-HETATM 2671  O   HOH A 482     118.935 143.690  79.610  1.00 24.10           O  
-HETATM 2672  O   HOH A 483     113.818 123.582  42.409  1.00 31.77           O  
-HETATM 2673  O   HOH A 484      84.422 143.293  56.615  1.00 32.72           O  
-HETATM 2674  O   HOH A 486     118.823 139.551  84.388  1.00 30.47           O  
-HETATM 2675  O   HOH A 487     105.355 128.515  20.523  1.00 43.00           O  
-HETATM 2676  O   HOH A 488     103.931 130.913  66.953  1.00 42.03           O  
-HETATM 2677  O   HOH A 489     104.545 133.495  67.258  1.00 33.49           O  
-HETATM 2678  O   HOH A 490     106.396 131.817  65.854  1.00 42.34           O  
-HETATM 2679  O   HOH A 493     117.320 146.672  64.520  1.00 42.98           O  
-HETATM 2680  O   HOH A 494      82.339 131.253  35.585  1.00 42.19           O  
-HETATM 2681  O   HOH A 496     114.029 131.499  59.382  1.00 43.57           O  
-HETATM 2682  O   HOH A 497     114.036 121.160  62.793  1.00 42.37           O  
-HETATM 2683  O   HOH A 498     102.882 129.410  27.260  1.00 43.40           O  
-HETATM 2684  O   HOH A 499      83.565 140.861  57.088  1.00 34.15           O  
-HETATM 2685  O   HOH A 500     102.424 113.022  40.548  1.00 36.20           O  
-HETATM 2686  O   HOH A 501      84.627 135.594  65.954  1.00 42.97           O  
-HETATM 2687  O   HOH A 502      90.665 128.291  64.049  1.00 36.99           O  
-HETATM 2688  O   HOH A 503     120.395 129.114  81.045  1.00 39.84           O  
-HETATM 2689  O   HOH A 504     112.691 125.369  67.563  1.00 32.00           O  
-HETATM 2690  O   HOH A 505      91.584 119.619  31.795  1.00 33.97           O  
-HETATM 2691  O   HOH A 506      98.717 136.081  31.677  1.00 39.35           O  
-HETATM 2692  O   HOH A 507     113.001 151.222  57.155  1.00 34.53           O  
-HETATM 2693  O   HOH A 508     112.866 127.622  84.729  1.00 48.79           O  
-CONECT 2440 2441 2442                                                           
-CONECT 2441 2440                                                                
-CONECT 2442 2440 2443                                                           
-CONECT 2443 2442                                                                
-CONECT 2444 2445 2446                                                           
-CONECT 2445 2444                                                                
-CONECT 2446 2444 2447                                                           
-CONECT 2447 2446                                                                
-CONECT 2448 2449 2450                                                           
-CONECT 2449 2448                                                                
-CONECT 2450 2448 2451                                                           
-CONECT 2451 2450                                                                
-CONECT 2452 2453 2454                                                           
-CONECT 2453 2452                                                                
-CONECT 2454 2452 2455                                                           
-CONECT 2455 2454                                                                
-CONECT 2456 2457 2458                                                           
-CONECT 2457 2456                                                                
-CONECT 2458 2456 2459                                                           
-CONECT 2459 2458                                                                
-CONECT 2460 2461 2468 2471                                                      
-CONECT 2461 2460 2462                                                           
-CONECT 2462 2461 2463                                                           
-CONECT 2463 2462 2464                                                           
-CONECT 2464 2463 2465 2471                                                      
-CONECT 2465 2464 2466                                                           
-CONECT 2466 2465 2467                                                           
-CONECT 2467 2466 2470                                                           
-CONECT 2468 2460 2472                                                           
-CONECT 2469 2470 2478 2479 2480                                                 
-CONECT 2470 2467 2469 2471                                                      
-CONECT 2471 2460 2464 2470                                                      
-CONECT 2472 2468 2473 2477                                                      
-CONECT 2473 2472 2474                                                           
-CONECT 2474 2473 2475                                                           
-CONECT 2475 2474 2476                                                           
-CONECT 2476 2475 2477                                                           
-CONECT 2477 2472 2476                                                           
-CONECT 2478 2469                                                                
-CONECT 2479 2469                                                                
-CONECT 2480 2469                                                                
-CONECT 2481 2482 2489 2492                                                      
-CONECT 2482 2481 2483                                                           
-CONECT 2483 2482 2484                                                           
-CONECT 2484 2483 2485                                                           
-CONECT 2485 2484 2486 2492                                                      
-CONECT 2486 2485 2487                                                           
-CONECT 2487 2486 2488                                                           
-CONECT 2488 2487 2491                                                           
-CONECT 2489 2481 2493                                                           
-CONECT 2490 2491 2499 2500 2501                                                 
-CONECT 2491 2488 2490 2492                                                      
-CONECT 2492 2481 2485 2491                                                      
-CONECT 2493 2489 2494 2498                                                      
-CONECT 2494 2493 2495                                                           
-CONECT 2495 2494 2496                                                           
-CONECT 2496 2495 2497                                                           
-CONECT 2497 2496 2498                                                           
-CONECT 2498 2493 2497                                                           
-CONECT 2499 2490                                                                
-CONECT 2500 2490                                                                
-CONECT 2501 2490                                                                
-MASTER      335    0    7   15    8    0   15    6 2685    1   62   24          
-END                                                                             
diff --git a/plip/test/pdb/3r0t.pdb b/plip/test/pdb/3r0t.pdb
deleted file mode 100644
index 5088b4f..0000000
--- a/plip/test/pdb/3r0t.pdb
+++ /dev/null
@@ -1,6723 +0,0 @@
-HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       09-MAR-11   3R0T              
-TITLE     CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT IN COMPLEX
-TITLE    2 WITH THE INHIBITOR CX-5279                                           
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 FRAGMENT: UNP RESIDUES 1-337;                                        
-COMPND   5 SYNONYM: CK II ALPHA;                                                
-COMPND   6 EC: 2.7.11.1;                                                        
-COMPND   7 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: CSNK2A1, CK2A1;                                                
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
-KEYWDS    KINASE, CK2-INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR      
-KEYWDS   2 COMPLEX                                                              
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    R.BATTISTUTTA,E.PAPINUTTO,G.LOLLI,F.PIERRE,M.HADDACH,D.M.RYCKMAN      
-REVDAT   2   29-OCT-14 3R0T    1       AUTHOR                                   
-REVDAT   1   07-DEC-11 3R0T    0                                                
-JRNL        AUTH   R.BATTISTUTTA,G.COZZA,F.PIERRE,E.PAPINUTTO,G.LOLLI,S.SARNO,  
-JRNL        AUTH 2 S.E.O'BRIEN,A.SIDDIQUI-JAIN,M.HADDACH,K.ANDERES,D.M.RYCKMAN, 
-JRNL        AUTH 3 F.MEGGIO,L.A.PINNA                                           
-JRNL        TITL   UNPRECEDENTED SELECTIVITY AND STRUCTURAL DETERMINANTS OF A   
-JRNL        TITL 2 NEW CLASS OF PROTEIN KINASE CK2 INHIBITORS IN CLINICAL       
-JRNL        TITL 3 TRIALS FOR THE TREATMENT OF CANCER.                          
-JRNL        REF    BIOCHEMISTRY                  V.  50  8478 2011              
-JRNL        REFN                   ISSN 0006-2960                               
-JRNL        PMID   21870818                                                     
-JRNL        DOI    10.1021/BI2008382                                            
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   G.COZZA,M.MAZZORANA,E.PAPINUTTO,J.BAIN,M.ELLIOTT,G.DI MAIRA, 
-REMARK   1  AUTH 2 A.GIANONCELLI,M.A.PAGANO,S.SARNO,M.RUZZENE,R.BATTISTUTTA,    
-REMARK   1  AUTH 3 F.MEGGIO,S.MORO,G.ZAGOTTO,L.A.PINNA                          
-REMARK   1  TITL   QUINALIZARIN AS A POTENT, SELECTIVE AND CELL-PERMEABLE       
-REMARK   1  TITL 2 INHIBITOR OF PROTEIN KINASE CK2.                             
-REMARK   1  REF    BIOCHEM.J.                    V. 421   387 2009              
-REMARK   1  REFN                   ISSN 0264-6021                               
-REMARK   1  PMID   19432557                                                     
-REMARK   1  DOI    10.1042/BJ20090069                                           
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : ML                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.18                          
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.4                           
-REMARK   3   NUMBER OF REFLECTIONS             : 28526                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
-REMARK   3   R VALUE            (WORKING SET) : 0.160                           
-REMARK   3   FREE R VALUE                     : 0.211                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1420                            
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 35.1842 -  3.7690    0.99     3103   165  0.1437 0.1687        
-REMARK   3     2  3.7690 -  2.9920    0.99     3026   162  0.1456 0.1894        
-REMARK   3     3  2.9920 -  2.6140    1.00     3033   153  0.1662 0.2429        
-REMARK   3     4  2.6140 -  2.3750    0.99     2975   179  0.1725 0.2541        
-REMARK   3     5  2.3750 -  2.2048    0.99     3009   152  0.1654 0.2217        
-REMARK   3     6  2.2048 -  2.0749    0.97     2927   145  0.1638 0.2257        
-REMARK   3     7  2.0749 -  1.9710    0.92     2782   140  0.1662 0.2278        
-REMARK   3     8  1.9710 -  1.8852    0.85     2580   129  0.1825 0.2350        
-REMARK   3     9  1.8852 -  1.8126    0.71     2123   113  0.2041 0.2279        
-REMARK   3    10  1.8126 -  1.7500    0.51     1548    82  0.2385 0.3005        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.10                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
-REMARK   3   K_SOL              : 0.37                                          
-REMARK   3   B_SOL              : 38.79                                         
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.080           
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 17.83                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.07                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -6.30980                                             
-REMARK   3    B22 (A**2) : 3.47990                                              
-REMARK   3    B33 (A**2) : 2.82990                                              
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : -1.16510                                             
-REMARK   3    B23 (A**2) : -0.00000                                             
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.007           2946                                  
-REMARK   3   ANGLE     :  1.036           3976                                  
-REMARK   3   CHIRALITY :  0.075            406                                  
-REMARK   3   PLANARITY :  0.005            501                                  
-REMARK   3   DIHEDRAL  : 13.608           1109                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
-REMARK   3   TLS GROUP : 1                                                      
-REMARK   3    SELECTION: (chain A and resid 3:13)                               
-REMARK   3    ORIGIN FOR THE GROUP (A):   1.4641 -55.6146  14.6268              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1667 T22:   0.1553                                     
-REMARK   3      T33:   0.2001 T12:  -0.0541                                     
-REMARK   3      T13:   0.0353 T23:  -0.0565                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0564 L22:   0.0078                                     
-REMARK   3      L33:   0.0150 L12:   0.0243                                     
-REMARK   3      L13:   0.0083 L23:  -0.0003                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0120 S12:   0.0526 S13:  -0.0471                       
-REMARK   3      S21:  -0.0062 S22:   0.0860 S23:  -0.0703                       
-REMARK   3      S31:  -0.0106 S32:  -0.0466 S33:   0.0000                       
-REMARK   3   TLS GROUP : 2                                                      
-REMARK   3    SELECTION: (chain A and resid 14:32)                              
-REMARK   3    ORIGIN FOR THE GROUP (A):  20.9593 -56.5547   8.8193              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2184 T22:   0.1470                                     
-REMARK   3      T33:   0.3446 T12:   0.0235                                     
-REMARK   3      T13:   0.0536 T23:  -0.0858                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0139 L22:   0.0999                                     
-REMARK   3      L33:   0.0686 L12:  -0.0127                                     
-REMARK   3      L13:   0.0311 L23:  -0.0074                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.2488 S12:   0.1931 S13:  -0.1999                       
-REMARK   3      S21:  -0.0211 S22:   0.0957 S23:  -0.1243                       
-REMARK   3      S31:   0.1808 S32:   0.1616 S33:  -0.0000                       
-REMARK   3   TLS GROUP : 3                                                      
-REMARK   3    SELECTION: (chain A and resid 33:51)                              
-REMARK   3    ORIGIN FOR THE GROUP (A):  33.0192 -34.0681  15.6464              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1317 T22:   0.2292                                     
-REMARK   3      T33:   0.2319 T12:  -0.0256                                     
-REMARK   3      T13:   0.0088 T23:  -0.0750                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0751 L22:   0.1045                                     
-REMARK   3      L33:   0.1087 L12:  -0.0117                                     
-REMARK   3      L13:   0.0879 L23:   0.0255                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0732 S12:   0.0348 S13:  -0.0756                       
-REMARK   3      S21:  -0.0804 S22:  -0.1905 S23:   0.2135                       
-REMARK   3      S31:  -0.0276 S32:   0.0701 S33:  -0.0001                       
-REMARK   3   TLS GROUP : 4                                                      
-REMARK   3    SELECTION: (chain A and resid 52:71)                              
-REMARK   3    ORIGIN FOR THE GROUP (A):  32.1118 -31.5914  11.3104              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1156 T22:   0.2072                                     
-REMARK   3      T33:   0.1295 T12:  -0.0180                                     
-REMARK   3      T13:  -0.0353 T23:  -0.0043                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0728 L22:   0.0127                                     
-REMARK   3      L33:   0.0385 L12:  -0.0320                                     
-REMARK   3      L13:  -0.0050 L23:   0.0035                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0461 S12:   0.1432 S13:   0.2397                       
-REMARK   3      S21:  -0.1383 S22:   0.0626 S23:   0.0589                       
-REMARK   3      S31:   0.0279 S32:  -0.0798 S33:   0.0007                       
-REMARK   3   TLS GROUP : 5                                                      
-REMARK   3    SELECTION: (chain A and resid 72:102)                             
-REMARK   3    ORIGIN FOR THE GROUP (A):  24.7116 -44.4796  11.8194              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1217 T22:   0.1772                                     
-REMARK   3      T33:   0.1597 T12:   0.0066                                     
-REMARK   3      T13:  -0.0140 T23:  -0.0266                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.1791 L22:   0.2326                                     
-REMARK   3      L33:   0.1170 L12:   0.1641                                     
-REMARK   3      L13:   0.0026 L23:   0.1089                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0039 S12:  -0.1009 S13:  -0.1852                       
-REMARK   3      S21:   0.0915 S22:   0.0280 S23:  -0.1044                       
-REMARK   3      S31:   0.0618 S32:   0.0149 S33:  -0.0000                       
-REMARK   3   TLS GROUP : 6                                                      
-REMARK   3    SELECTION: (chain A and resid 103:139)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  15.9998 -29.1819  10.8388              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1312 T22:   0.1502                                     
-REMARK   3      T33:   0.1780 T12:   0.0178                                     
-REMARK   3      T13:  -0.0068 T23:  -0.0057                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0500 L22:   0.0814                                     
-REMARK   3      L33:   0.2482 L12:  -0.0064                                     
-REMARK   3      L13:  -0.0006 L23:  -0.1427                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0048 S12:   0.0020 S13:   0.2493                       
-REMARK   3      S21:   0.0802 S22:   0.0149 S23:  -0.1391                       
-REMARK   3      S31:  -0.0785 S32:  -0.0440 S33:   0.0000                       
-REMARK   3   TLS GROUP : 7                                                      
-REMARK   3    SELECTION: (chain A and resid 140:224)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   9.9353 -41.3947  15.1453              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.0934 T22:   0.0745                                     
-REMARK   3      T33:   0.1054 T12:  -0.0020                                     
-REMARK   3      T13:  -0.0027 T23:  -0.0197                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.5752 L22:   0.4700                                     
-REMARK   3      L33:   0.2096 L12:   0.0653                                     
-REMARK   3      L13:  -0.1833 L23:  -0.2846                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0428 S12:   0.1121 S13:  -0.0482                       
-REMARK   3      S21:   0.0253 S22:   0.0386 S23:  -0.1052                       
-REMARK   3      S31:   0.0006 S32:  -0.0174 S33:   0.0000                       
-REMARK   3   TLS GROUP : 8                                                      
-REMARK   3    SELECTION: (chain A and resid 225:247)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   0.7560 -31.9870  26.3692              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1549 T22:   0.0805                                     
-REMARK   3      T33:   0.1055 T12:   0.0151                                     
-REMARK   3      T13:  -0.0151 T23:   0.0012                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.1356 L22:   0.0378                                     
-REMARK   3      L33:   0.0555 L12:  -0.0798                                     
-REMARK   3      L13:   0.0674 L23:  -0.0466                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0772 S12:   0.0027 S13:   0.1597                       
-REMARK   3      S21:   0.1155 S22:   0.0023 S23:  -0.1846                       
-REMARK   3      S31:  -0.0997 S32:  -0.0487 S33:  -0.0003                       
-REMARK   3   TLS GROUP : 9                                                      
-REMARK   3    SELECTION: (chain A and resid 248:329)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9085 -37.9654  18.3039              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.0920 T22:   0.1009                                     
-REMARK   3      T33:   0.0675 T12:  -0.0082                                     
-REMARK   3      T13:  -0.0036 T23:   0.0107                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.4401 L22:   0.2274                                     
-REMARK   3      L33:   0.3372 L12:  -0.1399                                     
-REMARK   3      L13:  -0.2005 L23:  -0.0276                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0103 S12:   0.1025 S13:  -0.0126                       
-REMARK   3      S21:   0.0164 S22:   0.0378 S23:  -0.0172                       
-REMARK   3      S31:   0.0227 S32:  -0.1320 S33:   0.0000                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 3R0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-11.                  
-REMARK 100 THE RCSB ID CODE IS RCSB064346.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-10                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 8.5                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ELETTRA                            
-REMARK 200  BEAMLINE                       : 5.2R                               
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
-REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI111               
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : PIXEL                              
-REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
-REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28551                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 46.180                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.6                               
-REMARK 200  DATA REDUNDANCY                : 2.800                              
-REMARK 200  R MERGE                    (I) : 0.08300                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 57.4                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.46200                            
-REMARK 200  R SYM FOR SHELL            (I) : 0.46200                            
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASER                                                
-REMARK 200 STARTING MODEL: PDB ENTRY 2PVR                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 37.63                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 4000, 0.2M LI2SO4, 0.1M TRIS     
-REMARK 280  PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K             
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,Y+1/2,-Z                                             
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       23.09200            
-REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     SER A     2                                                      
-REMARK 465     ASP A   330                                                      
-REMARK 465     GLN A   331                                                      
-REMARK 465     ALA A   332                                                      
-REMARK 465     ARG A   333                                                      
-REMARK 465     MET A   334                                                      
-REMARK 465     GLY A   335                                                      
-REMARK 465     SER A   336                                                      
-REMARK 465     SER A   337                                                      
-REMARK 480                                                                      
-REMARK 480 ZERO OCCUPANCY ATOM                                                  
-REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
-REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
-REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
-REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
-REMARK 480   M RES C SSEQI ATOMS                                                
-REMARK 480     VAL A   66   CA   CB   CG1  CG2                                  
-REMARK 480     MET A  137   CA   CB   CG   SD   CE                              
-REMARK 480     MET A  150   CA   CB   CG   SD   CE                              
-REMARK 480     SER A  194   CA   CB   OG                                        
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    PRO A  72        7.31    -63.10                                   
-REMARK 500    LYS A  74      171.94     77.25                                   
-REMARK 500    LYS A  75      -94.80   -122.48                                   
-REMARK 500    ASP A 156       41.13   -151.35                                   
-REMARK 500    ASP A 175       76.09     53.05                                   
-REMARK 500    ALA A 193      155.33     68.87                                   
-REMARK 500    MET A 208       54.56    -92.13                                   
-REMARK 500    HIS A 234       73.11   -103.07                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A 630        DISTANCE =  5.37 ANGSTROMS                       
-REMARK 525    HOH A 658        DISTANCE =  5.17 ANGSTROMS                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU9 A 338                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 339                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 340                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 341                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 342                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 343                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 344                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 345                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 346                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 347                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 348                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 349                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 350                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 351                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 352                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 3PE1   RELATED DB: PDB                                   
-REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT          
-REMARK 900 IN COMPLEX WITH THE INHIBITOR CX-4945                                
-REMARK 900 RELATED ID: 3PE2   RELATED DB: PDB                                   
-REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT          
-REMARK 900 IN COMPLEX WITH THE INHIBITOR CX-5011                                
-DBREF  3R0T A    1   337  UNP    P68400   CSK21_HUMAN      1    337             
-SEQRES   1 A  337  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
-SEQRES   2 A  337  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
-SEQRES   3 A  337  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
-SEQRES   4 A  337  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
-SEQRES   5 A  337  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
-SEQRES   6 A  337  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
-SEQRES   7 A  337  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
-SEQRES   8 A  337  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
-SEQRES   9 A  337  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
-SEQRES  10 A  337  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
-SEQRES  11 A  337  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
-SEQRES  12 A  337  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
-SEQRES  13 A  337  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
-SEQRES  14 A  337  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
-SEQRES  15 A  337  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
-SEQRES  16 A  337  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
-SEQRES  17 A  337  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
-SEQRES  18 A  337  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
-SEQRES  19 A  337  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
-SEQRES  20 A  337  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
-SEQRES  21 A  337  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
-SEQRES  22 A  337  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
-SEQRES  23 A  337  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
-SEQRES  24 A  337  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
-SEQRES  25 A  337  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
-SEQRES  26 A  337  THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER SER              
-HET    FU9  A 338      32                                                       
-HET    SO4  A 339       5                                                       
-HET    SO4  A 340       5                                                       
-HET    SO4  A 341       5                                                       
-HET    SO4  A 342       5                                                       
-HET    PEG  A 343       7                                                       
-HET    EDO  A 344       4                                                       
-HET    EDO  A 345       4                                                       
-HET    EDO  A 346       4                                                       
-HET    EDO  A 347       4                                                       
-HET    EDO  A 348       4                                                       
-HET    EDO  A 349       4                                                       
-HET    EDO  A 350       4                                                       
-HET    EDO  A 351       4                                                       
-HET    EDO  A 352       4                                                       
-HETNAM     FU9 3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)                     
-HETNAM   2 FU9  PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC              
-HETNAM   3 FU9  ACID                                                            
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
-HETNAM     EDO 1,2-ETHANEDIOL                                                   
-HETSYN     FU9 CX-5279                                                          
-HETSYN     EDO ETHYLENE GLYCOL                                                  
-FORMUL   2  FU9    C22 H16 F3 N5 O2                                             
-FORMUL   3  SO4    4(O4 S 2-)                                                   
-FORMUL   7  PEG    C4 H10 O3                                                    
-FORMUL   8  EDO    9(C2 H6 O2)                                                  
-FORMUL  17  HOH   *334(H2 O)                                                    
-HELIX    1   1 PRO A   20  ASP A   25  1                                   6    
-HELIX    2   2 TYR A   26  HIS A   29  5                                   4    
-HELIX    3   3 ASN A   35  ASP A   37  5                                   3    
-HELIX    4   4 LYS A   76  ARG A   89  1                                  14    
-HELIX    5   5 ASP A  120  TYR A  125  1                                   6    
-HELIX    6   6 THR A  129  MET A  150  1                                  22    
-HELIX    7   7 LYS A  158  HIS A  160  5                                   3    
-HELIX    8   8 ASP A  175  ALA A  179  5                                   5    
-HELIX    9   9 SER A  194  LYS A  198  5                                   5    
-HELIX   10  10 GLY A  199  VAL A  204  1                                   6    
-HELIX   11  11 TYR A  211  ARG A  228  1                                  18    
-HELIX   12  12 ASP A  237  GLY A  250  1                                  14    
-HELIX   13  13 GLY A  250  TYR A  261  1                                  12    
-HELIX   14  14 ASP A  266  ILE A  272  5                                   7    
-HELIX   15  15 ARG A  280  VAL A  285  5                                   6    
-HELIX   16  16 ASN A  289  VAL A  293  5                                   5    
-HELIX   17  17 SER A  294  LEU A  305  1                                  12    
-HELIX   18  18 ASP A  308  ARG A  312  5                                   5    
-HELIX   19  19 THR A  314  GLU A  320  1                                   7    
-HELIX   20  20 HIS A  321  TYR A  325  5                                   5    
-SHEET    1   A 5 TYR A  39  ARG A  47  0                                        
-SHEET    2   A 5 SER A  51  ASN A  58 -1  O  VAL A  53   N  LEU A  45           
-SHEET    3   A 5 LYS A  64  LEU A  70 -1  O  VAL A  65   N  ALA A  56           
-SHEET    4   A 5 THR A 108  GLU A 114 -1  O  LEU A 111   N  LYS A  68           
-SHEET    5   A 5 LEU A  97  ASP A 103 -1  N  VAL A 101   O  ALA A 110           
-SHEET    1   B 2 ILE A 152  MET A 153  0                                        
-SHEET    2   B 2 GLU A 180  PHE A 181 -1  O  GLU A 180   N  MET A 153           
-SHEET    1   C 2 VAL A 162  ASP A 165  0                                        
-SHEET    2   C 2 LYS A 170  LEU A 173 -1  O  LYS A 170   N  ASP A 165           
-CISPEP   1 GLU A  230    PRO A  231          0         1.13                     
-SITE     1 AC1 20 LEU A  45  GLY A  46  ARG A  47  VAL A  53                    
-SITE     2 AC1 20 VAL A  66  LYS A  68  PHE A 113  GLU A 114                    
-SITE     3 AC1 20 HIS A 115  VAL A 116  ASN A 118  MET A 163                    
-SITE     4 AC1 20 ILE A 174  ASP A 175  EDO A 345  EDO A 351                    
-SITE     5 AC1 20 HOH A 370  HOH A 381  HOH A 616  HOH A 636                    
-SITE     1 AC2  6 ARG A  80  ARG A 155  ASN A 189  VAL A 192                    
-SITE     2 AC2  6 HOH A 369  HOH A 677                                          
-SITE     1 AC3  4 ARG A 191  LYS A 198  ASN A 238  PEG A 343                    
-SITE     1 AC4  8 ASP A 253  ARG A 278  ARG A 306  TYR A 307                    
-SITE     2 AC4  8 ASP A 308  HOH A 397  HOH A 442  HOH A 465                    
-SITE     1 AC5  5 LYS A 170  ARG A 172  HOH A 428  HOH A 463                    
-SITE     2 AC5  5 HOH A 649                                                     
-SITE     1 AC6  6 SER A 194  ARG A 195  TYR A 196  SO4 A 340                    
-SITE     2 AC6  6 HOH A 433  HOH A 619                                          
-SITE     1 AC7  6 GLN A  36  TYR A  39  VAL A 101  ASP A 103                    
-SITE     2 AC7  6 PRO A 104  ARG A 280                                          
-SITE     1 AC8  6 ASN A 118  ASP A 120  HIS A 160  FU9 A 338                    
-SITE     2 AC8  6 EDO A 348  EDO A 351                                          
-SITE     1 AC9  4 ASP A  37  PRO A 295  HIS A 321  HOH A 620                    
-SITE     1 BC1  5 PHE A 232  HOH A 372  HOH A 573  HOH A 621                    
-SITE     2 BC1  5 HOH A 668                                                     
-SITE     1 BC2  9 ASN A 118  THR A 119  ASP A 120  PHE A 121                    
-SITE     2 BC2  9 PRO A 159  VAL A 162  MET A 163  ILE A 164                    
-SITE     3 BC2  9 EDO A 345                                                     
-SITE     1 BC3  6 LYS A 158  HIS A 160  SER A 194  EDO A 350                    
-SITE     2 BC3  6 HOH A 618  HOH A 619                                          
-SITE     1 BC4  5 PRO A 159  PHE A 197  GLU A 230  EDO A 349                    
-SITE     2 BC4  5 HOH A 618                                                     
-SITE     1 BC5  5 ASN A 118  FU9 A 338  EDO A 345  HOH A 455                    
-SITE     2 BC5  5 HOH A 575                                                     
-SITE     1 BC6  7 PRO A 104  ARG A 278  LYS A 279  ASP A 302                    
-SITE     2 BC6  7 HOH A 531  HOH A 642  HOH A 679                               
-CRYST1   58.352   46.184   63.300  90.00 111.51  90.00 P 1 21 1      2          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.017137  0.000000  0.006753        0.00000                         
-SCALE2      0.000000  0.021653  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.016980        0.00000                         
-ATOM      1  N   GLY A   3      -1.502 -62.453  29.985  1.00 40.82           N  
-ANISOU    1  N   GLY A   3     5111   4857   5540   -349     80   -403       N  
-ATOM      2  CA  GLY A   3      -0.651 -61.305  29.715  1.00 44.52           C  
-ANISOU    2  CA  GLY A   3     5587   5318   6013   -345     98   -421       C  
-ATOM      3  C   GLY A   3      -1.188 -60.418  28.604  1.00 39.81           C  
-ANISOU    3  C   GLY A   3     4994   4745   5387   -353    122   -411       C  
-ATOM      4  O   GLY A   3      -2.322 -60.588  28.164  1.00 36.32           O  
-ANISOU    4  O   GLY A   3     4552   4328   4919   -359    125   -385       O  
-ATOM      5  N   PRO A   4      -0.368 -59.467  28.133  1.00 38.43           N  
-ANISOU    5  N   PRO A   4     4823   4562   5216   -353    140   -431       N  
-ATOM      6  CA  PRO A   4      -0.839 -58.542  27.100  1.00 28.04           C  
-ANISOU    6  CA  PRO A   4     3512   3269   3872   -360    164   -421       C  
-ATOM      7  C   PRO A   4      -1.077 -59.249  25.772  1.00 26.24           C  
-ANISOU    7  C   PRO A   4     3274   3054   3640   -386    172   -431       C  
-ATOM      8  O   PRO A   4      -0.480 -60.287  25.482  1.00 29.56           O  
-ANISOU    8  O   PRO A   4     3684   3461   4086   -400    164   -457       O  
-ATOM      9  CB  PRO A   4       0.313 -57.540  26.978  1.00 34.55           C  
-ANISOU    9  CB  PRO A   4     4342   4077   4709   -355    178   -446       C  
-ATOM     10  CG  PRO A   4       1.524 -58.326  27.371  1.00 39.33           C  
-ANISOU   10  CG  PRO A   4     4939   4652   5354   -358    165   -481       C  
-ATOM     11  CD  PRO A   4       1.055 -59.258  28.461  1.00 39.89           C  
-ANISOU   11  CD  PRO A   4     5007   4717   5431   -349    140   -465       C  
-ATOM     12  N   VAL A   5      -1.971 -58.679  24.977  1.00 21.32           N  
-ANISOU   12  N   VAL A   5     2656   2459   2987   -392    188   -409       N  
-ATOM     13  CA  VAL A   5      -2.286 -59.191  23.656  1.00 25.36           C  
-ANISOU   13  CA  VAL A   5     3158   2986   3490   -416    198   -415       C  
-ATOM     14  C   VAL A   5      -1.179 -58.723  22.726  1.00 20.62           C  
-ANISOU   14  C   VAL A   5     2556   2376   2904   -429    216   -450       C  
-ATOM     15  O   VAL A   5      -0.725 -57.591  22.846  1.00 22.01           O  
-ANISOU   15  O   VAL A   5     2740   2547   3076   -418    228   -453       O  
-ATOM     16  CB  VAL A   5      -3.629 -58.612  23.180  1.00 14.07           C  
-ANISOU   16  CB  VAL A   5     1735   1590   2021   -416    209   -378       C  
-ATOM     17  CG1 VAL A   5      -3.854 -58.886  21.709  1.00 17.54           C  
-ANISOU   17  CG1 VAL A   5     2167   2047   2450   -442    224   -386       C  
-ATOM     18  CG2 VAL A   5      -4.773 -59.147  24.037  1.00 23.46           C  
-ANISOU   18  CG2 VAL A   5     2926   2792   3196   -405    192   -344       C  
-ATOM     19  N   PRO A   6      -0.720 -59.591  21.809  1.00 19.05           N  
-ANISOU   19  N   PRO A   6     2345   2173   2721   -451    218   -477       N  
-ATOM     20  CA  PRO A   6       0.332 -59.161  20.879  1.00 22.26           C  
-ANISOU   20  CA  PRO A   6     2749   2571   3140   -464    235   -511       C  
-ATOM     21  C   PRO A   6      -0.180 -58.203  19.796  1.00 19.43           C  
-ANISOU   21  C   PRO A   6     2395   2237   2751   -473    259   -498       C  
-ATOM     22  O   PRO A   6      -1.380 -58.098  19.579  1.00 23.70           O  
-ANISOU   22  O   PRO A   6     2938   2804   3262   -474    262   -466       O  
-ATOM     23  CB  PRO A   6       0.816 -60.479  20.258  1.00 22.71           C  
-ANISOU   23  CB  PRO A   6     2791   2618   3221   -486    229   -541       C  
-ATOM     24  CG  PRO A   6      -0.334 -61.414  20.398  1.00 24.95           C  
-ANISOU   24  CG  PRO A   6     3071   2918   3492   -490    215   -515       C  
-ATOM     25  CD  PRO A   6      -1.050 -61.022  21.661  1.00 24.62           C  
-ANISOU   25  CD  PRO A   6     3039   2879   3436   -465    203   -481       C  
-ATOM     26  N   SER A   7       0.745 -57.506  19.142  1.00 17.65           N  
-ANISOU   26  N   SER A   7     2170   2004   2534   -480    276   -524       N  
-ATOM     27  CA  SER A   7       0.417 -56.544  18.097  1.00 16.35           C  
-ANISOU   27  CA  SER A   7     2008   1861   2343   -488    300   -515       C  
-ATOM     28  C   SER A   7       1.444 -56.657  16.984  1.00 20.63           C  
-ANISOU   28  C   SER A   7     2542   2394   2901   -510    313   -554       C  
-ATOM     29  O   SER A   7       2.597 -57.000  17.244  1.00 20.28           O  
-ANISOU   29  O   SER A   7     2493   2324   2888   -510    307   -587       O  
-ATOM     30  CB  SER A   7       0.466 -55.121  18.661  1.00 17.57           C  
-ANISOU   30  CB  SER A   7     2177   2015   2485   -467    308   -500       C  
-ATOM     31  OG  SER A   7       0.286 -54.152  17.636  1.00 19.00           O  
-ANISOU   31  OG  SER A   7     2361   2214   2643   -476    331   -495       O  
-ATOM     32  N   ARG A   8       1.025 -56.363  15.754  1.00 20.45           N  
-ANISOU   32  N   ARG A   8     2517   2395   2857   -527    331   -550       N  
-ATOM     33  CA  ARG A   8       1.917 -56.328  14.585  1.00 21.97           C  
-ANISOU   33  CA  ARG A   8     2703   2585   3062   -548    347   -584       C  
-ATOM     34  C   ARG A   8       1.691 -55.027  13.836  1.00 21.54           C  
-ANISOU   34  C   ARG A   8     2655   2548   2981   -550    370   -572       C  
-ATOM     35  O   ARG A   8       0.571 -54.501  13.838  1.00 18.25           O  
-ANISOU   35  O   ARG A   8     2246   2155   2534   -544    374   -536       O  
-ATOM     36  CB  ARG A   8       1.572 -57.455  13.608  1.00 29.94           C  
-ANISOU   36  CB  ARG A   8     3698   3606   4070   -574    346   -593       C  
-ATOM     37  CG  ARG A   8       1.835 -58.846  14.104  1.00 37.53           C  
-ANISOU   37  CG  ARG A   8     4651   4551   5059   -577    325   -610       C  
-ATOM     38  CD  ARG A   8       3.325 -59.102  14.202  1.00 40.04           C  
-ANISOU   38  CD  ARG A   8     4963   4838   5414   -580    323   -653       C  
-ATOM     39  NE  ARG A   8       3.601 -60.471  14.624  1.00 40.22           N  
-ANISOU   39  NE  ARG A   8     4975   4844   5464   -584    303   -669       N  
-ATOM     40  CZ  ARG A   8       3.575 -60.878  15.889  1.00 42.42           C  
-ANISOU   40  CZ  ARG A   8     5256   5106   5755   -566    282   -661       C  
-ATOM     41  NH1 ARG A   8       3.283 -60.018  16.864  1.00 33.21           N  
-ANISOU   41  NH1 ARG A   8     4102   3938   4577   -542    279   -636       N  
-ATOM     42  NH2 ARG A   8       3.841 -62.146  16.180  1.00 45.87           N  
-ANISOU   42  NH2 ARG A   8     5683   5528   6218   -572    264   -677       N  
-ATOM     43  N   ALA A   9       2.731 -54.532  13.165  1.00 15.62           N  
-ANISOU   43  N   ALA A   9     1904   1789   2243   -560    384   -602       N  
-ATOM     44  CA  ALA A   9       2.572 -53.402  12.257  1.00 18.46           C  
-ANISOU   44  CA  ALA A   9     2267   2166   2579   -566    407   -594       C  
-ATOM     45  C   ALA A   9       1.606 -53.796  11.137  1.00 21.46           C  
-ANISOU   45  C   ALA A   9     2642   2578   2936   -587    416   -580       C  
-ATOM     46  O   ALA A   9       1.625 -54.930  10.662  1.00 21.38           O  
-ANISOU   46  O   ALA A   9     2621   2568   2936   -605    409   -595       O  
-ATOM     47  CB  ALA A   9       3.914 -52.996  11.673  1.00 14.16           C  
-ANISOU   47  CB  ALA A   9     1720   1606   2055   -576    420   -633       C  
-ATOM     48  N   ARG A  10       0.762 -52.862  10.709  1.00 13.86           N  
-ANISOU   48  N   ARG A  10     1687   1639   1940   -586    429   -550       N  
-ATOM     49  CA  ARG A  10      -0.195 -53.164   9.653  1.00 16.17           C  
-ANISOU   49  CA  ARG A  10     1974   1962   2208   -605    438   -534       C  
-ATOM     50  C   ARG A  10       0.395 -52.974   8.263  1.00 16.19           C  
-ANISOU   50  C   ARG A  10     1970   1972   2210   -630    457   -560       C  
-ATOM     51  O   ARG A  10      -0.245 -53.311   7.260  1.00 20.93           O  
-ANISOU   51  O   ARG A  10     2563   2595   2793   -649    465   -553       O  
-ATOM     52  CB  ARG A  10      -1.463 -52.325   9.813  1.00 20.15           C  
-ANISOU   52  CB  ARG A  10     2489   2491   2677   -593    443   -489       C  
-ATOM     53  CG  ARG A  10      -2.278 -52.639  11.048  1.00 33.68           C  
-ANISOU   53  CG  ARG A  10     4208   4204   4385   -572    424   -460       C  
-ATOM     54  CD  ARG A  10      -3.552 -51.806  11.037  1.00 41.52           C  
-ANISOU   54  CD  ARG A  10     5211   5224   5342   -563    431   -416       C  
-ATOM     55  NE  ARG A  10      -3.245 -50.409  10.738  1.00 55.14           N  
-ANISOU   55  NE  ARG A  10     6944   6952   7056   -557    450   -413       N  
-ATOM     56  CZ  ARG A  10      -4.138 -49.512  10.325  1.00 57.27           C  
-ANISOU   56  CZ  ARG A  10     7221   7246   7295   -555    463   -382       C  
-ATOM     57  NH1 ARG A  10      -5.406 -49.859  10.157  1.00 51.33           N  
-ANISOU   57  NH1 ARG A  10     6468   6519   6518   -558    460   -351       N  
-ATOM     58  NH2 ARG A  10      -3.756 -48.265  10.082  1.00 58.40           N  
-ANISOU   58  NH2 ARG A  10     7370   7388   7430   -550    479   -382       N  
-ATOM     59  N   VAL A  11       1.614 -52.434   8.208  1.00 17.69           N  
-ANISOU   59  N   VAL A  11     2160   2142   2420   -629    465   -589       N  
-ATOM     60  CA  VAL A  11       2.346 -52.276   6.954  1.00 18.09           C  
-ANISOU   60  CA  VAL A  11     2203   2196   2474   -652    483   -618       C  
-ATOM     61  C   VAL A  11       3.819 -52.578   7.179  1.00 22.01           C  
-ANISOU   61  C   VAL A  11     2695   2661   3008   -653    479   -661       C  
-ATOM     62  O   VAL A  11       4.294 -52.538   8.311  1.00 20.68           O  
-ANISOU   62  O   VAL A  11     2531   2469   2858   -633    466   -665       O  
-ATOM     63  CB  VAL A  11       2.206 -50.858   6.352  1.00 17.11           C  
-ANISOU   63  CB  VAL A  11     2088   2088   2327   -652    504   -604       C  
-ATOM     64  CG1 VAL A  11       0.766 -50.601   5.959  1.00 21.02           C  
-ANISOU   64  CG1 VAL A  11     2586   2615   2785   -654    509   -563       C  
-ATOM     65  CG2 VAL A  11       2.716 -49.791   7.320  1.00 21.76           C  
-ANISOU   65  CG2 VAL A  11     2689   2658   2922   -626    504   -600       C  
-ATOM     66  N   TYR A  12       4.526 -52.889   6.097  1.00 17.12           N  
-ANISOU   66  N   TYR A  12     2064   2041   2398   -677    490   -693       N  
-ATOM     67  CA  TYR A  12       5.951 -53.168   6.155  1.00 19.55           C  
-ANISOU   67  CA  TYR A  12     2367   2322   2741   -681    488   -736       C  
-ATOM     68  C   TYR A  12       6.273 -54.144   7.269  1.00 21.70           C  
-ANISOU   68  C   TYR A  12     2636   2568   3041   -668    465   -747       C  
-ATOM     69  O   TYR A  12       7.320 -54.030   7.919  1.00 22.08           O  
-ANISOU   69  O   TYR A  12     2686   2589   3115   -658    459   -770       O  
-ATOM     70  CB  TYR A  12       6.708 -51.872   6.405  1.00 15.19           C  
-ANISOU   70  CB  TYR A  12     1824   1757   2191   -668    499   -742       C  
-ATOM     71  CG  TYR A  12       6.436 -50.806   5.380  1.00 18.71           C  
-ANISOU   71  CG  TYR A  12     2273   2225   2610   -678    522   -731       C  
-ATOM     72  CD1 TYR A  12       6.473 -51.100   4.028  1.00 19.73           C  
-ANISOU   72  CD1 TYR A  12     2393   2372   2733   -706    535   -746       C  
-ATOM     73  CD2 TYR A  12       6.138 -49.507   5.764  1.00 17.74           C  
-ANISOU   73  CD2 TYR A  12     2163   2107   2469   -660    529   -705       C  
-ATOM     74  CE1 TYR A  12       6.241 -50.128   3.081  1.00 18.96           C  
-ANISOU   74  CE1 TYR A  12     2298   2296   2611   -716    556   -735       C  
-ATOM     75  CE2 TYR A  12       5.887 -48.528   4.829  1.00 21.09           C  
-ANISOU   75  CE2 TYR A  12     2591   2553   2869   -670    550   -694       C  
-ATOM     76  CZ  TYR A  12       5.938 -48.849   3.485  1.00 16.76           C  
-ANISOU   76  CZ  TYR A  12     2033   2022   2315   -697    563   -709       C  
-ATOM     77  OH  TYR A  12       5.705 -47.877   2.541  1.00 22.86           O  
-ANISOU   77  OH  TYR A  12     2808   2815   3064   -707    583   -699       O  
-ATOM     78  N   THR A  13       5.373 -55.095   7.495  1.00 19.83           N  
-ANISOU   78  N   THR A  13     2396   2342   2799   -670    451   -729       N  
-ATOM     79  CA  THR A  13       5.482 -55.969   8.655  1.00 22.60           C  
-ANISOU   79  CA  THR A  13     2745   2671   3172   -656    428   -732       C  
-ATOM     80  C   THR A  13       6.719 -56.847   8.586  1.00 25.56           C  
-ANISOU   80  C   THR A  13     3108   3019   3583   -666    421   -776       C  
-ATOM     81  O   THR A  13       7.417 -57.034   9.587  1.00 24.25           O  
-ANISOU   81  O   THR A  13     2944   2827   3443   -651    408   -789       O  
-ATOM     82  CB  THR A  13       4.245 -56.876   8.814  1.00 20.97           C  
-ANISOU   82  CB  THR A  13     2535   2481   2950   -658    415   -704       C  
-ATOM     83  OG1 THR A  13       3.054 -56.090   8.692  1.00 26.40           O  
-ANISOU   83  OG1 THR A  13     3232   3196   3601   -652    423   -664       O  
-ATOM     84  CG2 THR A  13       4.268 -57.546  10.168  1.00 18.64           C  
-ANISOU   84  CG2 THR A  13     2241   2165   2674   -639    391   -700       C  
-ATOM     85  N   ASP A  14       7.000 -57.363   7.393  1.00 25.50           N  
-ANISOU   85  N   ASP A  14     3469   2039   4180   -271    566  -1070       N  
-ATOM     86  CA  ASP A  14       8.052 -58.358   7.223  1.00 28.16           C  
-ANISOU   86  CA  ASP A  14     3792   2362   4546   -223    643  -1099       C  
-ATOM     87  C   ASP A  14       9.233 -57.872   6.392  1.00 23.39           C  
-ANISOU   87  C   ASP A  14     3131   1840   3917   -248    629  -1101       C  
-ATOM     88  O   ASP A  14       9.986 -58.690   5.854  1.00 20.94           O  
-ANISOU   88  O   ASP A  14     2805   1531   3619   -234    699  -1140       O  
-ATOM     89  CB  ASP A  14       7.484 -59.634   6.594  1.00 38.57           C  
-ANISOU   89  CB  ASP A  14     5141   3635   5878   -246    740  -1168       C  
-ATOM     90  CG  ASP A  14       6.515 -60.358   7.517  1.00 43.55           C  
-ANISOU   90  CG  ASP A  14     5828   4175   6545   -204    770  -1167       C  
-ATOM     91  OD1 ASP A  14       6.987 -61.012   8.472  1.00 44.76           O  
-ANISOU   91  OD1 ASP A  14     5996   4269   6740   -114    800  -1150       O  
-ATOM     92  OD2 ASP A  14       5.290 -60.274   7.284  1.00 38.57           O  
-ANISOU   92  OD2 ASP A  14     5227   3530   5899   -259    763  -1184       O  
-ATOM     93  N   VAL A  15       9.409 -56.558   6.296  1.00 22.43           N  
-ANISOU   93  N   VAL A  15     2978   1785   3760   -282    540  -1060       N  
-ATOM     94  CA  VAL A  15      10.496 -56.020   5.487  1.00 22.29           C  
-ANISOU   94  CA  VAL A  15     2906   1849   3715   -310    522  -1060       C  
-ATOM     95  C   VAL A  15      11.853 -56.585   5.890  1.00 24.88           C  
-ANISOU   95  C   VAL A  15     3210   2167   4078   -228    560  -1052       C  
-ATOM     96  O   VAL A  15      12.652 -56.938   5.027  1.00 26.13           O  
-ANISOU   96  O   VAL A  15     3337   2362   4230   -245    605  -1086       O  
-ATOM     97  CB  VAL A  15      10.549 -54.476   5.535  1.00 24.94           C  
-ANISOU   97  CB  VAL A  15     3212   2252   4012   -347    413  -1007       C  
-ATOM     98  CG1 VAL A  15       9.453 -53.872   4.667  1.00 18.51           C  
-ANISOU   98  CG1 VAL A  15     2406   1475   3153   -449    382  -1029       C  
-ATOM     99  CG2 VAL A  15      10.416 -54.002   6.957  1.00 35.48           C  
-ANISOU   99  CG2 VAL A  15     4565   3547   5369   -277    353   -943       C  
-ATOM    100  N   ASN A  16      12.122 -56.667   7.190  1.00 24.52           N  
-ANISOU  100  N   ASN A  16     3178   2070   4069   -139    543  -1006       N  
-ATOM    101  CA  ASN A  16      13.408 -57.186   7.659  1.00 27.34           C  
-ANISOU  101  CA  ASN A  16     3513   2413   4461    -57    575   -994       C  
-ATOM    102  C   ASN A  16      13.463 -58.705   7.613  1.00 29.82           C  
-ANISOU  102  C   ASN A  16     3853   2662   4813    -17    682  -1045       C  
-ATOM    103  O   ASN A  16      14.539 -59.292   7.465  1.00 31.81           O  
-ANISOU  103  O   ASN A  16     4082   2919   5086     24    730  -1060       O  
-ATOM    104  CB  ASN A  16      13.731 -56.692   9.072  1.00 23.17           C  
-ANISOU  104  CB  ASN A  16     2990   1856   3958     25    514   -925       C  
-ATOM    105  CG  ASN A  16      14.065 -55.224   9.109  1.00 22.63           C  
-ANISOU  105  CG  ASN A  16     2885   1858   3854     -1    412   -872       C  
-ATOM    106  OD1 ASN A  16      14.844 -54.740   8.294  1.00 24.80           O  
-ANISOU  106  OD1 ASN A  16     3113   2207   4104    -39    397   -877       O  
-ATOM    107  ND2 ASN A  16      13.463 -54.498  10.043  1.00 17.96           N  
-ANISOU  107  ND2 ASN A  16     2315   1246   3262     17    340   -821       N  
-ATOM    108  N   THR A  17      12.298 -59.332   7.744  1.00 34.34           N  
-ANISOU  108  N   THR A  17     4476   3175   5396    -30    718  -1072       N  
-ATOM    109  CA  THR A  17      12.194 -60.784   7.694  1.00 33.88           C  
-ANISOU  109  CA  THR A  17     4448   3050   5373      2    819  -1123       C  
-ATOM    110  C   THR A  17      12.802 -61.307   6.399  1.00 34.28           C  
-ANISOU  110  C   THR A  17     4470   3144   5409    -42    883  -1180       C  
-ATOM    111  O   THR A  17      13.375 -62.394   6.363  1.00 41.50           O  
-ANISOU  111  O   THR A  17     5388   4024   6355      4    961  -1212       O  
-ATOM    112  CB  THR A  17      10.718 -61.231   7.783  1.00 30.25           C  
-ANISOU  112  CB  THR A  17     4043   2534   4916    -29    843  -1148       C  
-ATOM    113  OG1 THR A  17      10.090 -60.625   8.924  1.00 39.37           O  
-ANISOU  113  OG1 THR A  17     5224   3655   6079      3    777  -1093       O  
-ATOM    114  CG2 THR A  17      10.617 -62.750   7.882  1.00 31.13           C  
-ANISOU  114  CG2 THR A  17     4189   2569   5068     14    945  -1195       C  
-ATOM    115  N   HIS A  18      12.694 -60.512   5.342  1.00 32.28           N  
-ANISOU  115  N   HIS A  18     4187   2968   5108   -129    847  -1193       N  
-ATOM    116  CA  HIS A  18      13.097 -60.948   4.008  1.00 36.98           C  
-ANISOU  116  CA  HIS A  18     4759   3608   5684   -184    905  -1250       C  
-ATOM    117  C   HIS A  18      14.301 -60.203   3.431  1.00 35.82           C  
-ANISOU  117  C   HIS A  18     4552   3547   5513   -200    871  -1235       C  
-ATOM    118  O   HIS A  18      14.665 -60.401   2.272  1.00 33.08           O  
-ANISOU  118  O   HIS A  18     4179   3246   5143   -251    909  -1279       O  
-ATOM    119  CB  HIS A  18      11.904 -60.867   3.061  1.00 37.24           C  
-ANISOU  119  CB  HIS A  18     4813   3656   5682   -282    911  -1292       C  
-ATOM    120  CG  HIS A  18      10.808 -61.825   3.409  1.00 38.02           C  
-ANISOU  120  CG  HIS A  18     4968   3670   5806   -271    964  -1322       C  
-ATOM    121  ND1 HIS A  18       9.590 -61.419   3.913  1.00 34.86           N  
-ANISOU  121  ND1 HIS A  18     4605   3241   5401   -292    921  -1302       N  
-ATOM    122  CD2 HIS A  18      10.758 -63.177   3.347  1.00 35.48           C  
-ANISOU  122  CD2 HIS A  18     4674   3288   5517   -240   1058  -1369       C  
-ATOM    123  CE1 HIS A  18       8.830 -62.480   4.128  1.00 35.92           C  
-ANISOU  123  CE1 HIS A  18     4785   3301   5563   -276    986  -1336       C  
-ATOM    124  NE2 HIS A  18       9.516 -63.558   3.791  1.00 35.59           N  
-ANISOU  124  NE2 HIS A  18     4740   3239   5545   -245   1069  -1377       N  
-ATOM    125  N   ARG A  19      14.903 -59.344   4.247  1.00 36.48           N  
-ANISOU  125  N   ARG A  19     4611   3649   5600   -155    799  -1171       N  
-ATOM    126  CA  ARG A  19      16.174 -58.707   3.911  1.00 32.17           C  
-ANISOU  126  CA  ARG A  19     4007   3175   5040   -152    768  -1150       C  
-ATOM    127  C   ARG A  19      17.295 -59.661   4.277  1.00 34.10           C  
-ANISOU  127  C   ARG A  19     4240   3388   5327    -67    832  -1158       C  
-ATOM    128  O   ARG A  19      17.129 -60.485   5.172  1.00 32.12           O  
-ANISOU  128  O   ARG A  19     4025   3059   5119      4    870  -1155       O  
-ATOM    129  CB  ARG A  19      16.353 -57.415   4.714  1.00 27.42           C  
-ANISOU  129  CB  ARG A  19     3388   2603   4428   -134    663  -1076       C  
-ATOM    130  CG  ARG A  19      15.479 -56.258   4.275  1.00 33.58           C  
-ANISOU  130  CG  ARG A  19     4167   3432   5159   -220    586  -1062       C  
-ATOM    131  CD  ARG A  19      16.222 -55.352   3.330  1.00 38.85           C  
-ANISOU  131  CD  ARG A  19     4780   4196   5786   -278    546  -1057       C  
-ATOM    132  NE  ARG A  19      15.389 -54.281   2.794  1.00 42.19           N  
-ANISOU  132  NE  ARG A  19     5201   4668   6159   -366    477  -1049       N  
-ATOM    133  CZ  ARG A  19      15.812 -53.412   1.882  1.00 44.31           C  
-ANISOU  133  CZ  ARG A  19     5427   5023   6385   -431    437  -1047       C  
-ATOM    134  NH1 ARG A  19      17.053 -53.494   1.411  1.00 41.81           N  
-ANISOU  134  NH1 ARG A  19     5065   4751   6069   -419    459  -1053       N  
-ATOM    135  NH2 ARG A  19      15.001 -52.469   1.432  1.00 40.28           N  
-ANISOU  135  NH2 ARG A  19     4919   4553   5832   -510    375  -1040       N  
-ATOM    136  N   PRO A  20      18.455 -59.541   3.603  1.00 34.02           N  
-ANISOU  136  N   PRO A  20     4181   3439   5308    -73    844  -1166       N  
-ATOM    137  CA  PRO A  20      19.609 -60.329   4.042  1.00 34.71           C  
-ANISOU  137  CA  PRO A  20     4252   3500   5436     12    896  -1166       C  
-ATOM    138  C   PRO A  20      19.906 -60.020   5.504  1.00 37.28           C  
-ANISOU  138  C   PRO A  20     4585   3786   5795    100    845  -1101       C  
-ATOM    139  O   PRO A  20      19.670 -58.899   5.955  1.00 30.21           O  
-ANISOU  139  O   PRO A  20     3682   2916   4880     88    756  -1050       O  
-ATOM    140  CB  PRO A  20      20.755 -59.812   3.162  1.00 33.68           C  
-ANISOU  140  CB  PRO A  20     4059   3457   5281    -17    885  -1168       C  
-ATOM    141  CG  PRO A  20      20.107 -59.121   2.020  1.00 36.39           C  
-ANISOU  141  CG  PRO A  20     4394   3863   5571   -126    857  -1191       C  
-ATOM    142  CD  PRO A  20      18.797 -58.598   2.524  1.00 31.96           C  
-ANISOU  142  CD  PRO A  20     3873   3273   4998   -153    803  -1169       C  
-ATOM    143  N   ARG A  21      20.419 -61.005   6.230  1.00 37.42           N  
-ANISOU  143  N   ARG A  21     4617   3741   5861    188    900  -1104       N  
-ATOM    144  CA  ARG A  21      20.750 -60.838   7.641  1.00 36.04           C  
-ANISOU  144  CA  ARG A  21     4451   3521   5720    278    859  -1046       C  
-ATOM    145  C   ARG A  21      21.672 -59.640   7.898  1.00 32.18           C  
-ANISOU  145  C   ARG A  21     3912   3097   5217    289    775   -987       C  
-ATOM    146  O   ARG A  21      21.509 -58.937   8.888  1.00 30.57           O  
-ANISOU  146  O   ARG A  21     3718   2879   5019    323    703   -930       O  
-ATOM    147  CB  ARG A  21      21.373 -62.126   8.183  1.00 40.30           C  
-ANISOU  147  CB  ARG A  21     5005   3995   6313    367    939  -1064       C  
-ATOM    148  CG  ARG A  21      21.677 -62.128   9.669  1.00 42.05           C  
-ANISOU  148  CG  ARG A  21     5242   4160   6574    466    909  -1009       C  
-ATOM    149  CD  ARG A  21      21.910 -63.551  10.157  1.00 50.92           C  
-ANISOU  149  CD  ARG A  21     6395   5203   7747    543    997  -1038       C  
-ATOM    150  NE  ARG A  21      22.545 -63.597  11.472  1.00 59.73           N  
-ANISOU  150  NE  ARG A  21     7516   6276   8904    643    974   -987       N  
-ATOM    151  CZ  ARG A  21      21.925 -63.936  12.599  1.00 65.53           C  
-ANISOU  151  CZ  ARG A  21     8299   6932   9668    700    971   -965       C  
-ATOM    152  NH1 ARG A  21      20.638 -64.264  12.586  1.00 68.26           N  
-ANISOU  152  NH1 ARG A  21     8693   7234  10008    666    990   -988       N  
-ATOM    153  NH2 ARG A  21      22.597 -63.951  13.743  1.00 65.89           N  
-ANISOU  153  NH2 ARG A  21     8344   6943   9748    791    948   -919       N  
-ATOM    154  N   GLU A  22      22.639 -59.413   7.011  1.00 26.59           N  
-ANISOU  154  N   GLU A  22     3152   2459   4491    261    782  -1001       N  
-ATOM    155  CA  GLU A  22      23.559 -58.283   7.140  1.00 27.88           C  
-ANISOU  155  CA  GLU A  22     3264   2689   4639    266    705   -949       C  
-ATOM    156  C   GLU A  22      22.824 -56.942   7.224  1.00 26.97           C  
-ANISOU  156  C   GLU A  22     3149   2613   4484    209    606   -908       C  
-ATOM    157  O   GLU A  22      23.340 -55.981   7.798  1.00 29.49           O  
-ANISOU  157  O   GLU A  22     3443   2962   4799    232    528   -850       O  
-ATOM    158  CB  GLU A  22      24.540 -58.252   5.963  1.00 29.37           C  
-ANISOU  158  CB  GLU A  22     3399   2953   4807    226    733   -979       C  
-ATOM    159  CG  GLU A  22      23.853 -58.257   4.602  1.00 47.78           C  
-ANISOU  159  CG  GLU A  22     5732   5326   7096    123    761  -1034       C  
-ATOM    160  CD  GLU A  22      24.822 -58.191   3.430  1.00 62.08           C  
-ANISOU  160  CD  GLU A  22     7489   7212   8885     82    788  -1062       C  
-ATOM    161  OE1 GLU A  22      26.051 -58.129   3.664  1.00 61.20           O  
-ANISOU  161  OE1 GLU A  22     7337   7123   8791    134    785  -1039       O  
-ATOM    162  OE2 GLU A  22      24.347 -58.200   2.270  1.00 65.47           O  
-ANISOU  162  OE2 GLU A  22     7917   7678   9278     -2    812  -1108       O  
-ATOM    163  N   TYR A  23      21.627 -56.875   6.644  1.00 24.08           N  
-ANISOU  163  N   TYR A  23     2814   2247   4090    134    609   -938       N  
-ATOM    164  CA  TYR A  23      20.863 -55.632   6.635  1.00 18.77           C  
-ANISOU  164  CA  TYR A  23     2143   1612   3378     74    518   -904       C  
-ATOM    165  C   TYR A  23      20.475 -55.171   8.042  1.00 22.62           C  
-ANISOU  165  C   TYR A  23     2658   2051   3884    134    454   -843       C  
-ATOM    166  O   TYR A  23      20.655 -54.005   8.389  1.00 21.90           O  
-ANISOU  166  O   TYR A  23     2546   2000   3774    127    365   -790       O  
-ATOM    167  CB  TYR A  23      19.615 -55.749   5.751  1.00 19.50           C  
-ANISOU  167  CB  TYR A  23     2264   1707   3438    -15    540   -951       C  
-ATOM    168  CG  TYR A  23      18.807 -54.468   5.689  1.00 20.47           C  
-ANISOU  168  CG  TYR A  23     2389   1870   3518    -80    448   -919       C  
-ATOM    169  CD1 TYR A  23      19.171 -53.446   4.831  1.00 24.15           C  
-ANISOU  169  CD1 TYR A  23     2811   2426   3940   -149    396   -911       C  
-ATOM    170  CD2 TYR A  23      17.690 -54.278   6.500  1.00 19.19           C  
-ANISOU  170  CD2 TYR A  23     2273   1656   3361    -71    412   -895       C  
-ATOM    171  CE1 TYR A  23      18.454 -52.260   4.772  1.00 18.81           C  
-ANISOU  171  CE1 TYR A  23     2136   1786   3224   -208    310   -880       C  
-ATOM    172  CE2 TYR A  23      16.961 -53.090   6.454  1.00 17.09           C  
-ANISOU  172  CE2 TYR A  23     2008   1427   3057   -129    326   -865       C  
-ATOM    173  CZ  TYR A  23      17.351 -52.083   5.582  1.00 17.84           C  
-ANISOU  173  CZ  TYR A  23     2059   1612   3108   -198    275   -857       C  
-ATOM    174  OH  TYR A  23      16.655 -50.893   5.497  1.00 17.48           O  
-ANISOU  174  OH  TYR A  23     2013   1606   3022   -257    189   -828       O  
-ATOM    175  N   TRP A  24      19.940 -56.087   8.844  1.00 21.93           N  
-ANISOU  175  N   TRP A  24     2620   1877   3835    191    499   -852       N  
-ATOM    176  CA  TRP A  24      19.401 -55.725  10.162  1.00 21.58           C  
-ANISOU  176  CA  TRP A  24     2610   1780   3809    243    444   -799       C  
-ATOM    177  C   TRP A  24      20.253 -56.195  11.353  1.00 22.11           C  
-ANISOU  177  C   TRP A  24     2679   1795   3925    355    454   -765       C  
-ATOM    178  O   TRP A  24      20.078 -55.721  12.479  1.00 19.22           O  
-ANISOU  178  O   TRP A  24     2332   1398   3573    404    396   -711       O  
-ATOM    179  CB  TRP A  24      17.965 -56.241  10.304  1.00 20.96           C  
-ANISOU  179  CB  TRP A  24     2590   1640   3734    221    472   -825       C  
-ATOM    180  CG  TRP A  24      17.844 -57.693  10.030  1.00 20.25           C  
-ANISOU  180  CG  TRP A  24     2526   1494   3673    240    579   -885       C  
-ATOM    181  CD1 TRP A  24      17.385 -58.281   8.882  1.00 27.80           C  
-ANISOU  181  CD1 TRP A  24     3489   2463   4612    173    642   -949       C  
-ATOM    182  CD2 TRP A  24      18.205 -58.760  10.910  1.00 21.59           C  
-ANISOU  182  CD2 TRP A  24     2721   1587   3894    334    637   -886       C  
-ATOM    183  NE1 TRP A  24      17.437 -59.651   9.000  1.00 28.10           N  
-ANISOU  183  NE1 TRP A  24     3553   2435   4688    219    736   -990       N  
-ATOM    184  CE2 TRP A  24      17.932 -59.969  10.238  1.00 25.70           C  
-ANISOU  184  CE2 TRP A  24     3262   2077   4427    318    734   -952       C  
-ATOM    185  CE3 TRP A  24      18.724 -58.812  12.205  1.00 21.98           C  
-ANISOU  185  CE3 TRP A  24     2779   1592   3982    430    615   -837       C  
-ATOM    186  CZ2 TRP A  24      18.166 -61.215  10.819  1.00 32.78           C  
-ANISOU  186  CZ2 TRP A  24     4186   2898   5372    395    809   -971       C  
-ATOM    187  CZ3 TRP A  24      18.957 -60.051  12.780  1.00 23.29           C  
-ANISOU  187  CZ3 TRP A  24     2972   1683   4195    506    690   -856       C  
-ATOM    188  CH2 TRP A  24      18.673 -61.234  12.088  1.00 32.48           C  
-ANISOU  188  CH2 TRP A  24     4155   2817   5370    488    786   -922       C  
-ATOM    189  N   ASP A  25      21.167 -57.130  11.108  1.00 25.51           N  
-ANISOU  189  N   ASP A  25     3094   2216   4384    395    528   -795       N  
-ATOM    190  CA  ASP A  25      22.022 -57.664  12.168  1.00 23.59           C  
-ANISOU  190  CA  ASP A  25     2852   1924   4189    501    544   -768       C  
-ATOM    191  C   ASP A  25      23.178 -56.701  12.412  1.00 21.98           C  
-ANISOU  191  C   ASP A  25     2595   1778   3979    525    474   -716       C  
-ATOM    192  O   ASP A  25      24.328 -56.996  12.075  1.00 25.57           O  
-ANISOU  192  O   ASP A  25     3010   2260   4445    549    506   -726       O  
-ATOM    193  CB  ASP A  25      22.538 -59.051  11.778  1.00 26.72           C  
-ANISOU  193  CB  ASP A  25     3250   2287   4617    533    651   -823       C  
-ATOM    194  CG  ASP A  25      23.374 -59.709  12.871  1.00 29.58           C  
-ANISOU  194  CG  ASP A  25     3618   2591   5031    644    675   -799       C  
-ATOM    195  OD1 ASP A  25      23.339 -59.260  14.035  1.00 34.11           O  
-ANISOU  195  OD1 ASP A  25     4207   3134   5621    700    618   -744       O  
-ATOM    196  OD2 ASP A  25      24.069 -60.696  12.560  1.00 39.64           O  
-ANISOU  196  OD2 ASP A  25     4882   3851   6330    676    753   -837       O  
-ATOM    197  N   TYR A  26      22.863 -55.547  12.991  1.00 19.11           N  
-ANISOU  197  N   TYR A  26     2232   1433   3597    518    379   -660       N  
-ATOM    198  CA  TYR A  26      23.839 -54.474  13.156  1.00 24.13           C  
-ANISOU  198  CA  TYR A  26     2819   2131   4220    528    302   -608       C  
-ATOM    199  C   TYR A  26      24.998 -54.829  14.081  1.00 26.18           C  
-ANISOU  199  C   TYR A  26     3063   2361   4524    630    309   -576       C  
-ATOM    200  O   TYR A  26      26.073 -54.239  13.984  1.00 25.78           O  
-ANISOU  200  O   TYR A  26     2962   2365   4468    640    271   -548       O  
-ATOM    201  CB  TYR A  26      23.165 -53.187  13.635  1.00 25.24           C  
-ANISOU  201  CB  TYR A  26     2968   2291   4331    499    199   -555       C  
-ATOM    202  CG  TYR A  26      22.463 -53.309  14.971  1.00 29.33           C  
-ANISOU  202  CG  TYR A  26     3537   2730   4875    562    176   -520       C  
-ATOM    203  CD1 TYR A  26      23.164 -53.170  16.161  1.00 25.55           C  
-ANISOU  203  CD1 TYR A  26     3057   2221   4429    653    141   -467       C  
-ATOM    204  CD2 TYR A  26      21.096 -53.553  15.039  1.00 28.83           C  
-ANISOU  204  CD2 TYR A  26     3526   2622   4806    531    189   -539       C  
-ATOM    205  CE1 TYR A  26      22.523 -53.272  17.385  1.00 30.86           C  
-ANISOU  205  CE1 TYR A  26     3779   2821   5126    711    120   -434       C  
-ATOM    206  CE2 TYR A  26      20.447 -53.655  16.261  1.00 31.11           C  
-ANISOU  206  CE2 TYR A  26     3862   2839   5119    589    169   -507       C  
-ATOM    207  CZ  TYR A  26      21.169 -53.517  17.427  1.00 32.80           C  
-ANISOU  207  CZ  TYR A  26     4074   3024   5363    678    135   -454       C  
-ATOM    208  OH  TYR A  26      20.534 -53.616  18.640  1.00 46.14           O  
-ANISOU  208  OH  TYR A  26     5813   4643   7077    736    115   -422       O  
-ATOM    209  N   GLU A  27      24.781 -55.787  14.975  1.00 30.09           N  
-ANISOU  209  N   GLU A  27     3601   2769   5062    704    355   -580       N  
-ATOM    210  CA  GLU A  27      25.817 -56.172  15.926  1.00 33.50           C  
-ANISOU  210  CA  GLU A  27     4024   3166   5539    805    362   -549       C  
-ATOM    211  C   GLU A  27      27.064 -56.717  15.227  1.00 34.74           C  
-ANISOU  211  C   GLU A  27     4134   3359   5708    818    419   -579       C  
-ATOM    212  O   GLU A  27      28.171 -56.640  15.770  1.00 31.43           O  
-ANISOU  212  O   GLU A  27     3686   2944   5314    883    403   -547       O  
-ATOM    213  CB  GLU A  27      25.273 -57.172  16.952  1.00 39.01           C  
-ANISOU  213  CB  GLU A  27     4781   3763   6280    879    409   -553       C  
-ATOM    214  CG  GLU A  27      24.503 -56.523  18.096  1.00 41.96           C  
-ANISOU  214  CG  GLU A  27     5192   4096   6653    906    336   -499       C  
-ATOM    215  CD  GLU A  27      23.580 -57.496  18.817  1.00 51.75           C  
-ANISOU  215  CD  GLU A  27     6497   5241   7924    948    387   -515       C  
-ATOM    216  OE1 GLU A  27      22.369 -57.520  18.497  1.00 59.76           O  
-ANISOU  216  OE1 GLU A  27     7545   6242   8918    891    395   -539       O  
-ATOM    217  OE2 GLU A  27      24.059 -58.232  19.705  1.00 53.70           O  
-ANISOU  217  OE2 GLU A  27     6761   5427   8216   1037    419   -504       O  
-ATOM    218  N   SER A  28      26.886 -57.236  14.014  1.00 30.96           N  
-ANISOU  218  N   SER A  28     3646   2906   5211    754    484   -641       N  
-ATOM    219  CA  SER A  28      27.990 -57.828  13.269  1.00 36.58           C  
-ANISOU  219  CA  SER A  28     4316   3650   5933    761    546   -676       C  
-ATOM    220  C   SER A  28      28.534 -56.868  12.216  1.00 30.71           C  
-ANISOU  220  C   SER A  28     3514   3008   5146    687    505   -674       C  
-ATOM    221  O   SER A  28      29.439 -57.215  11.458  1.00 32.55           O  
-ANISOU  221  O   SER A  28     3707   3280   5380    680    550   -703       O  
-ATOM    222  CB  SER A  28      27.553 -59.137  12.608  1.00 44.54           C  
-ANISOU  222  CB  SER A  28     5352   4619   6952    746    652   -748       C  
-ATOM    223  OG  SER A  28      26.789 -58.886  11.439  1.00 53.21           O  
-ANISOU  223  OG  SER A  28     6449   5761   8006    644    660   -788       O  
-ATOM    224  N   HIS A  29      27.977 -55.663  12.173  1.00 25.16           N  
-ANISOU  224  N   HIS A  29     2807   2347   4404    631    419   -640       N  
-ATOM    225  CA  HIS A  29      28.439 -54.637  11.241  1.00 21.69           C  
-ANISOU  225  CA  HIS A  29     2315   2004   3922    559    370   -632       C  
-ATOM    226  C   HIS A  29      29.912 -54.280  11.461  1.00 26.62           C  
-ANISOU  226  C   HIS A  29     2884   2669   4561    608    344   -597       C  
-ATOM    227  O   HIS A  29      30.346 -54.020  12.583  1.00 27.29           O  
-ANISOU  227  O   HIS A  29     2971   2726   4674    681    299   -545       O  
-ATOM    228  CB  HIS A  29      27.585 -53.373  11.353  1.00 23.44           C  
-ANISOU  228  CB  HIS A  29     2546   2256   4104    502    276   -594       C  
-ATOM    229  CG  HIS A  29      27.979 -52.301  10.384  1.00 27.70           C  
-ANISOU  229  CG  HIS A  29     3034   2894   4598    424    224   -587       C  
-ATOM    230  ND1 HIS A  29      27.807 -52.433   9.024  1.00 25.50           N  
-ANISOU  230  ND1 HIS A  29     2739   2665   4285    341    265   -640       N  
-ATOM    231  CD2 HIS A  29      28.567 -51.096  10.575  1.00 29.49           C  
-ANISOU  231  CD2 HIS A  29     3222   3178   4805    418    135   -532       C  
-ATOM    232  CE1 HIS A  29      28.260 -51.350   8.417  1.00 32.65           C  
-ANISOU  232  CE1 HIS A  29     3598   3655   5154    286    204   -618       C  
-ATOM    233  NE2 HIS A  29      28.725 -50.521   9.336  1.00 30.23           N  
-ANISOU  233  NE2 HIS A  29     3277   3354   4855    331    125   -553       N  
-ATOM    234  N   VAL A  30      30.679 -54.267  10.380  1.00 25.27           N  
-ANISOU  234  N   VAL A  30     2664   2564   4373    566    372   -626       N  
-ATOM    235  CA  VAL A  30      32.069 -53.837  10.449  1.00 27.58           C  
-ANISOU  235  CA  VAL A  30     2899   2905   4675    600    344   -594       C  
-ATOM    236  C   VAL A  30      32.195 -52.409   9.928  1.00 31.06           C  
-ANISOU  236  C   VAL A  30     3299   3434   5068    529    256   -560       C  
-ATOM    237  O   VAL A  30      31.979 -52.142   8.742  1.00 31.42           O  
-ANISOU  237  O   VAL A  30     3326   3538   5074    443    266   -594       O  
-ATOM    238  CB  VAL A  30      32.991 -54.763   9.647  1.00 32.05           C  
-ANISOU  238  CB  VAL A  30     3433   3488   5256    609    433   -643       C  
-ATOM    239  CG1 VAL A  30      34.410 -54.192   9.598  1.00 37.88           C  
-ANISOU  239  CG1 VAL A  30     4107   4288   5999    632    399   -610       C  
-ATOM    240  CG2 VAL A  30      32.992 -56.153  10.259  1.00 36.74           C  
-ANISOU  240  CG2 VAL A  30     4064   3994   5900    688    516   -671       C  
-ATOM    241  N   VAL A  31      32.548 -51.492  10.821  1.00 26.69           N  
-ANISOU  241  N   VAL A  31     2733   2889   4519    566    169   -494       N  
-ATOM    242  CA  VAL A  31      32.630 -50.086  10.462  1.00 29.93           C  
-ANISOU  242  CA  VAL A  31     3109   3377   4885    504     78   -457       C  
-ATOM    243  C   VAL A  31      33.782 -49.805   9.501  1.00 29.17           C  
-ANISOU  243  C   VAL A  31     2946   3363   4773    472     86   -467       C  
-ATOM    244  O   VAL A  31      34.892 -50.299   9.690  1.00 32.69           O  
-ANISOU  244  O   VAL A  31     3363   3807   5253    532    120   -465       O  
-ATOM    245  CB  VAL A  31      32.763 -49.203  11.714  1.00 29.72           C  
-ANISOU  245  CB  VAL A  31     3086   3336   4869    557    -17   -382       C  
-ATOM    246  CG1 VAL A  31      33.047 -47.759  11.324  1.00 31.63           C  
-ANISOU  246  CG1 VAL A  31     3285   3664   5068    498   -110   -342       C  
-ATOM    247  CG2 VAL A  31      31.494 -49.294  12.554  1.00 31.17           C  
-ANISOU  247  CG2 VAL A  31     3336   3449   5059    573    -35   -370       C  
-ATOM    248  N   GLU A  32      33.506 -49.022   8.463  1.00 30.99           N  
-ANISOU  248  N   GLU A  32     3154   3667   4954    377     56   -478       N  
-ATOM    249  CA  GLU A  32      34.537 -48.569   7.534  1.00 35.78           C  
-ANISOU  249  CA  GLU A  32     3697   4359   5539    337     51   -482       C  
-ATOM    250  C   GLU A  32      34.983 -47.149   7.904  1.00 36.55           C  
-ANISOU  250  C   GLU A  32     3760   4511   5616    329    -59   -415       C  
-ATOM    251  O   GLU A  32      34.229 -46.180   7.732  1.00 28.88           O  
-ANISOU  251  O   GLU A  32     2798   3569   4605    266   -128   -395       O  
-ATOM    252  CB  GLU A  32      34.016 -48.616   6.095  1.00 44.73           C  
-ANISOU  252  CB  GLU A  32     4826   5541   6630    236     90   -539       C  
-ATOM    253  CG  GLU A  32      35.001 -48.118   5.044  1.00 58.64           C  
-ANISOU  253  CG  GLU A  32     6522   7393   8364    187     86   -546       C  
-ATOM    254  CD  GLU A  32      34.422 -48.158   3.636  1.00 68.68           C  
-ANISOU  254  CD  GLU A  32     7793   8710   9591     86    123   -602       C  
-ATOM    255  OE1 GLU A  32      33.430 -48.891   3.422  1.00 69.49           O  
-ANISOU  255  OE1 GLU A  32     7943   8767   9693     66    176   -646       O  
-ATOM    256  OE2 GLU A  32      34.954 -47.454   2.748  1.00 71.27           O  
-ANISOU  256  OE2 GLU A  32     8074   9121   9885     26     98   -601       O  
-ATOM    257  N   TRP A  33      36.207 -47.033   8.415  1.00 28.21           N  
-ANISOU  257  N   TRP A  33     2892   3925   3902     74    582   -704       N  
-ATOM    258  CA  TRP A  33      36.697 -45.766   8.962  1.00 29.78           C  
-ANISOU  258  CA  TRP A  33     3106   4157   4053     41    544   -647       C  
-ATOM    259  C   TRP A  33      37.291 -44.837   7.913  1.00 27.70           C  
-ANISOU  259  C   TRP A  33     2878   3930   3717     50    466   -611       C  
-ATOM    260  O   TRP A  33      38.052 -45.266   7.039  1.00 25.31           O  
-ANISOU  260  O   TRP A  33     2593   3660   3365     77    469   -570       O  
-ATOM    261  CB  TRP A  33      37.739 -46.023  10.055  1.00 27.02           C  
-ANISOU  261  CB  TRP A  33     2751   3849   3664     18    613   -554       C  
-ATOM    262  CG  TRP A  33      37.227 -46.906  11.145  1.00 27.32           C  
-ANISOU  262  CG  TRP A  33     2756   3855   3768      5    690   -582       C  
-ATOM    263  CD1 TRP A  33      37.440 -48.251  11.282  1.00 28.91           C  
-ANISOU  263  CD1 TRP A  33     2944   4052   3990     22    767   -575       C  
-ATOM    264  CD2 TRP A  33      36.401 -46.516  12.243  1.00 28.69           C  
-ANISOU  264  CD2 TRP A  33     2908   3995   3998    -26    698   -624       C  
-ATOM    265  NE1 TRP A  33      36.798 -48.717  12.404  1.00 28.81           N  
-ANISOU  265  NE1 TRP A  33     2902   4005   4041      2    822   -609       N  
-ATOM    266  CE2 TRP A  33      36.150 -47.673  13.011  1.00 31.32           C  
-ANISOU  266  CE2 TRP A  33     3214   4305   4383    -28    783   -639       C  
-ATOM    267  CE3 TRP A  33      35.839 -45.301  12.650  1.00 27.14           C  
-ANISOU  267  CE3 TRP A  33     2712   3786   3814    -52    642   -651       C  
-ATOM    268  CZ2 TRP A  33      35.365 -47.649  14.163  1.00 37.21           C  
-ANISOU  268  CZ2 TRP A  33     3932   5017   5190    -55    813   -680       C  
-ATOM    269  CZ3 TRP A  33      35.060 -45.281  13.801  1.00 31.89           C  
-ANISOU  269  CZ3 TRP A  33     3286   4354   4477    -78    673   -692       C  
-ATOM    270  CH2 TRP A  33      34.834 -46.446  14.543  1.00 36.40           C  
-ANISOU  270  CH2 TRP A  33     3830   4904   5097    -80    758   -705       C  
-ATOM    271  N   GLY A  34      36.958 -43.557   8.018  1.00 19.32           N  
-ANISOU  271  N   GLY A  34     1826   2865   2648     29    397   -623       N  
-ATOM    272  CA  GLY A  34      37.572 -42.551   7.175  1.00 20.89           C  
-ANISOU  272  CA  GLY A  34     2061   3102   2776     31    323   -580       C  
-ATOM    273  C   GLY A  34      38.796 -41.952   7.849  1.00 20.68           C  
-ANISOU  273  C   GLY A  34     2047   3134   2675      2    334   -470       C  
-ATOM    274  O   GLY A  34      39.281 -42.471   8.855  1.00 19.71           O  
-ANISOU  274  O   GLY A  34     1909   3027   2552    -13    406   -423       O  
-ATOM    275  N   ASN A  35      39.285 -40.850   7.297  1.00 21.08           N  
-ANISOU  275  N   ASN A  35     2129   3217   2665     -5    263   -430       N  
-ATOM    276  CA  ASN A  35      40.481 -40.203   7.827  1.00 21.01           C  
-ANISOU  276  CA  ASN A  35     2135   3266   2581    -31    266   -325       C  
-ATOM    277  C   ASN A  35      40.111 -39.067   8.755  1.00 19.67           C  
-ANISOU  277  C   ASN A  35     1964   3086   2425    -69    230   -329       C  
-ATOM    278  O   ASN A  35      39.546 -38.064   8.329  1.00 19.55           O  
-ANISOU  278  O   ASN A  35     1963   3053   2414    -74    150   -369       O  
-ATOM    279  CB  ASN A  35      41.362 -39.685   6.696  1.00 31.70           C  
-ANISOU  279  CB  ASN A  35     3524   4667   3853    -18    212   -268       C  
-ATOM    280  CG  ASN A  35      41.922 -40.801   5.852  1.00 45.33           C  
-ANISOU  280  CG  ASN A  35     5254   6415   5556     18    253   -249       C  
-ATOM    281  OD1 ASN A  35      42.064 -41.930   6.320  1.00 43.96           O  
-ANISOU  281  OD1 ASN A  35     5058   6237   5406     27    332   -243       O  
-ATOM    282  ND2 ASN A  35      42.243 -40.498   4.598  1.00 56.99           N  
-ANISOU  282  ND2 ASN A  35     6758   7913   6985     39    198   -239       N  
-ATOM    283  N   GLN A  36      40.437 -39.226  10.032  1.00 19.13           N  
-ANISOU  283  N   GLN A  36     1878   3028   2362    -95    289   -287       N  
-ATOM    284  CA  GLN A  36      40.078 -38.230  11.033  1.00 15.71           C  
-ANISOU  284  CA  GLN A  36     1441   2584   1945   -132    263   -292       C  
-ATOM    285  C   GLN A  36      40.659 -36.855  10.698  1.00 19.46           C  
-ANISOU  285  C   GLN A  36     1948   3095   2353   -149    183   -239       C  
-ATOM    286  O   GLN A  36      40.077 -35.830  11.049  1.00 17.88           O  
-ANISOU  286  O   GLN A  36     1750   2873   2170   -170    128   -270       O  
-ATOM    287  CB  GLN A  36      40.530 -38.708  12.416  1.00 21.17           C  
-ANISOU  287  CB  GLN A  36     2112   3289   2642   -155    345   -242       C  
-ATOM    288  CG  GLN A  36      40.075 -37.832  13.577  1.00 21.47           C  
-ANISOU  288  CG  GLN A  36     2141   3311   2706   -192    330   -253       C  
-ATOM    289  CD  GLN A  36      41.051 -36.700  13.877  1.00 21.25           C  
-ANISOU  289  CD  GLN A  36     2137   3332   2603   -219    291   -164       C  
-ATOM    290  OE1 GLN A  36      42.212 -36.745  13.473  1.00 23.76           O  
-ANISOU  290  OE1 GLN A  36     2475   3702   2851   -215    296    -80       O  
-ATOM    291  NE2 GLN A  36      40.574 -35.676  14.584  1.00 19.55           N  
-ANISOU  291  NE2 GLN A  36     1921   3102   2405   -247    250   -183       N  
-ATOM    292  N   ASP A  37      41.806 -36.835  10.021  1.00 18.94           N  
-ANISOU  292  N   ASP A  37     1906   3082   2209   -140    176   -159       N  
-ATOM    293  CA  ASP A  37      42.446 -35.578   9.656  1.00 17.14           C  
-ANISOU  293  CA  ASP A  37     1709   2891   1912   -156    102   -102       C  
-ATOM    294  C   ASP A  37      41.708 -34.792   8.571  1.00 23.36           C  
-ANISOU  294  C   ASP A  37     2517   3652   2707   -144      8   -166       C  
-ATOM    295  O   ASP A  37      42.053 -33.642   8.309  1.00 24.20           O  
-ANISOU  295  O   ASP A  37     2649   3780   2765   -160    -62   -130       O  
-ATOM    296  CB  ASP A  37      43.906 -35.808   9.250  1.00 25.11           C  
-ANISOU  296  CB  ASP A  37     2738   3967   2836   -151    125      4       C  
-ATOM    297  CG  ASP A  37      44.052 -36.918   8.238  1.00 40.71           C  
-ANISOU  297  CG  ASP A  37     4713   5946   4809   -111    155    -10       C  
-ATOM    298  OD1 ASP A  37      43.788 -38.085   8.603  1.00 45.25           O  
-ANISOU  298  OD1 ASP A  37     5263   6501   5430    -97    229    -38       O  
-ATOM    299  OD2 ASP A  37      44.420 -36.624   7.078  1.00 50.04           O  
-ANISOU  299  OD2 ASP A  37     5919   7151   5942    -94    106      6       O  
-ATOM    300  N   ASP A  38      40.684 -35.392   7.957  1.00 18.40           N  
-ANISOU  300  N   ASP A  38     1876   2975   2140   -116      4   -260       N  
-ATOM    301  CA  ASP A  38      39.933 -34.694   6.916  1.00 17.82           C  
-ANISOU  301  CA  ASP A  38     1821   2874   2077   -102    -85   -325       C  
-ATOM    302  C   ASP A  38      39.051 -33.588   7.483  1.00 19.39           C  
-ANISOU  302  C   ASP A  38     2017   3036   2313   -127   -144   -376       C  
-ATOM    303  O   ASP A  38      38.601 -32.706   6.745  1.00 20.59           O  
-ANISOU  303  O   ASP A  38     2190   3174   2461   -124   -229   -413       O  
-ATOM    304  CB  ASP A  38      39.047 -35.657   6.124  1.00 21.36           C  
-ANISOU  304  CB  ASP A  38     2255   3277   2582    -65    -72   -414       C  
-ATOM    305  CG  ASP A  38      39.822 -36.499   5.148  1.00 20.81           C  
-ANISOU  305  CG  ASP A  38     2198   3241   2468    -33    -46   -375       C  
-ATOM    306  OD1 ASP A  38      41.054 -36.289   5.012  1.00 19.37           O  
-ANISOU  306  OD1 ASP A  38     2035   3118   2207    -40    -41   -279       O  
-ATOM    307  OD2 ASP A  38      39.193 -37.374   4.512  1.00 22.14           O  
-ANISOU  307  OD2 ASP A  38     2356   3376   2680     -2    -29   -442       O  
-ATOM    308  N   TYR A  39      38.792 -33.639   8.788  1.00 17.12           N  
-ANISOU  308  N   TYR A  39     1705   2735   2064   -152    -99   -380       N  
-ATOM    309  CA  TYR A  39      37.806 -32.746   9.401  1.00 21.33           C  
-ANISOU  309  CA  TYR A  39     2230   3228   2646   -173   -145   -442       C  
-ATOM    310  C   TYR A  39      38.407 -31.895  10.505  1.00 25.65           C  
-ANISOU  310  C   TYR A  39     2783   3805   3160   -211   -147   -373       C  
-ATOM    311  O   TYR A  39      39.029 -32.407  11.441  1.00 26.89           O  
-ANISOU  311  O   TYR A  39     2925   3985   3306   -226    -73   -317       O  
-ATOM    312  CB  TYR A  39      36.600 -33.553   9.906  1.00 17.99           C  
-ANISOU  312  CB  TYR A  39     1769   2747   2318   -164    -99   -538       C  
-ATOM    313  CG  TYR A  39      36.103 -34.481   8.839  1.00 22.60           C  
-ANISOU  313  CG  TYR A  39     2349   3305   2933   -125    -91   -599       C  
-ATOM    314  CD1 TYR A  39      35.264 -34.016   7.829  1.00 17.51           C  
-ANISOU  314  CD1 TYR A  39     1715   2625   2311   -107   -169   -675       C  
-ATOM    315  CD2 TYR A  39      36.515 -35.808   8.797  1.00 22.55           C  
-ANISOU  315  CD2 TYR A  39     2329   3310   2931   -106    -10   -578       C  
-ATOM    316  CE1 TYR A  39      34.838 -34.852   6.825  1.00 18.86           C  
-ANISOU  316  CE1 TYR A  39     1884   2773   2508    -71   -164   -729       C  
-ATOM    317  CE2 TYR A  39      36.089 -36.654   7.794  1.00 17.79           C  
-ANISOU  317  CE2 TYR A  39     1723   2684   2354    -70     -5   -633       C  
-ATOM    318  CZ  TYR A  39      35.244 -36.168   6.815  1.00 19.20           C  
-ANISOU  318  CZ  TYR A  39     1912   2828   2555    -53    -82   -708       C  
-ATOM    319  OH  TYR A  39      34.814 -37.000   5.816  1.00 19.34           O  
-ANISOU  319  OH  TYR A  39     1927   2821   2599    -16    -78   -763       O  
-ATOM    320  N   GLN A  40      38.242 -30.585  10.364  1.00 20.44           N  
-ANISOU  320  N   GLN A  40     2144   3143   2480   -228   -233   -377       N  
-ATOM    321  CA  GLN A  40      38.687 -29.645  11.379  1.00 23.33           C  
-ANISOU  321  CA  GLN A  40     2516   3531   2818   -265   -246   -321       C  
-ATOM    322  C   GLN A  40      37.490 -29.054  12.116  1.00 25.44           C  
-ANISOU  322  C   GLN A  40     2765   3747   3153   -280   -275   -403       C  
-ATOM    323  O   GLN A  40      36.630 -28.428  11.501  1.00 18.67           O  
-ANISOU  323  O   GLN A  40     1916   2855   2322   -271   -349   -474       O  
-ATOM    324  CB  GLN A  40      39.509 -28.527  10.738  1.00 34.83           C  
-ANISOU  324  CB  GLN A  40     4012   5028   4194   -275   -324   -253       C  
-ATOM    325  CG  GLN A  40      40.746 -29.031  10.015  1.00 50.56           C  
-ANISOU  325  CG  GLN A  40     6023   7075   6114   -262   -298   -167       C  
-ATOM    326  CD  GLN A  40      41.760 -27.934   9.734  1.00 59.10           C  
-ANISOU  326  CD  GLN A  40     7140   8206   7111   -282   -358    -79       C  
-ATOM    327  OE1 GLN A  40      42.964 -28.138   9.879  1.00 55.16           O  
-ANISOU  327  OE1 GLN A  40     6648   7760   6550   -290   -321     16       O  
-ATOM    328  NE2 GLN A  40      41.275 -26.766   9.325  1.00 65.49           N  
-ANISOU  328  NE2 GLN A  40     7970   8997   7917   -291   -452   -111       N  
-ATOM    329  N   LEU A  41      37.441 -29.246  13.431  1.00 23.57           N  
-ANISOU  329  N   LEU A  41     2504   3507   2943   -301   -217   -393       N  
-ATOM    330  CA  LEU A  41      36.349 -28.700  14.241  1.00 20.98           C  
-ANISOU  330  CA  LEU A  41     2158   3135   2679   -317   -238   -466       C  
-ATOM    331  C   LEU A  41      36.390 -27.164  14.297  1.00 19.58           C  
-ANISOU  331  C   LEU A  41     2006   2964   2469   -340   -330   -451       C  
-ATOM    332  O   LEU A  41      37.447 -26.569  14.485  1.00 19.99           O  
-ANISOU  332  O   LEU A  41     2081   3062   2451   -359   -344   -359       O  
-ATOM    333  CB  LEU A  41      36.379 -29.295  15.648  1.00 22.01           C  
-ANISOU  333  CB  LEU A  41     2258   3265   2840   -336   -150   -451       C  
-ATOM    334  CG  LEU A  41      36.328 -30.822  15.735  1.00 16.83           C  
-ANISOU  334  CG  LEU A  41     1575   2601   2219   -317    -55   -465       C  
-ATOM    335  CD1 LEU A  41      36.442 -31.290  17.182  1.00 21.71           C  
-ANISOU  335  CD1 LEU A  41     2167   3222   2860   -340     27   -441       C  
-ATOM    336  CD2 LEU A  41      35.065 -31.354  15.093  1.00 21.48           C  
-ANISOU  336  CD2 LEU A  41     2145   3134   2882   -290    -64   -577       C  
-ATOM    337  N   VAL A  42      35.236 -26.533  14.102  1.00 19.54           N  
-ANISOU  337  N   VAL A  42     1998   2912   2514   -336   -394   -542       N  
-ATOM    338  CA  VAL A  42      35.135 -25.075  14.052  1.00 20.83           C  
-ANISOU  338  CA  VAL A  42     2187   3075   2654   -354   -489   -541       C  
-ATOM    339  C   VAL A  42      34.472 -24.500  15.310  1.00 21.04           C  
-ANISOU  339  C   VAL A  42     2194   3076   2725   -379   -490   -577       C  
-ATOM    340  O   VAL A  42      34.941 -23.519  15.876  1.00 23.99           O  
-ANISOU  340  O   VAL A  42     2584   3472   3060   -405   -525   -526       O  
-ATOM    341  CB  VAL A  42      34.335 -24.623  12.808  1.00 23.88           C  
-ANISOU  341  CB  VAL A  42     2589   3427   3058   -331   -575   -617       C  
-ATOM    342  CG1 VAL A  42      34.177 -23.108  12.793  1.00 31.16           C  
-ANISOU  342  CG1 VAL A  42     3537   4345   3959   -350   -675   -619       C  
-ATOM    343  CG2 VAL A  42      35.024 -25.100  11.544  1.00 26.27           C  
-ANISOU  343  CG2 VAL A  42     2913   3757   3311   -307   -580   -578       C  
-ATOM    344  N   ARG A  43      33.359 -25.094  15.729  1.00 22.92           N  
-ANISOU  344  N   ARG A  43     2396   3267   3044   -370   -453   -667       N  
-ATOM    345  CA  ARG A  43      32.715 -24.661  16.959  1.00 24.76           C  
-ANISOU  345  CA  ARG A  43     2608   3477   3322   -392   -445   -704       C  
-ATOM    346  C   ARG A  43      31.737 -25.689  17.493  1.00 21.65           C  
-ANISOU  346  C   ARG A  43     2171   3044   3012   -383   -373   -783       C  
-ATOM    347  O   ARG A  43      31.151 -26.448  16.732  1.00 22.81           O  
-ANISOU  347  O   ARG A  43     2306   3163   3198   -356   -362   -844       O  
-ATOM    348  CB  ARG A  43      32.010 -23.318  16.766  1.00 27.32           C  
-ANISOU  348  CB  ARG A  43     2947   3775   3657   -399   -548   -756       C  
-ATOM    349  CG  ARG A  43      30.981 -23.300  15.662  1.00 34.69           C  
-ANISOU  349  CG  ARG A  43     3881   4665   4635   -371   -606   -852       C  
-ATOM    350  CD  ARG A  43      30.017 -22.147  15.890  1.00 42.48           C  
-ANISOU  350  CD  ARG A  43     4868   5614   5657   -380   -687   -924       C  
-ATOM    351  NE  ARG A  43      29.701 -21.445  14.653  1.00 56.71           N  
-ANISOU  351  NE  ARG A  43     6699   7401   7447   -363   -784   -959       N  
-ATOM    352  CZ  ARG A  43      28.484 -21.368  14.124  1.00 63.47           C  
-ANISOU  352  CZ  ARG A  43     7544   8207   8366   -344   -828  -1066       C  
-ATOM    353  NH1 ARG A  43      27.453 -21.950  14.728  1.00 58.93           N  
-ANISOU  353  NH1 ARG A  43     6929   7593   7871   -339   -783  -1148       N  
-ATOM    354  NH2 ARG A  43      28.296 -20.702  12.993  1.00 69.65           N  
-ANISOU  354  NH2 ARG A  43     8356   8979   9130   -330   -918  -1090       N  
-ATOM    355  N   LYS A  44      31.572 -25.709  18.812  1.00 17.42           N  
-ANISOU  355  N   LYS A  44     1612   2504   2502   -405   -325   -782       N  
-ATOM    356  CA  LYS A  44      30.643 -26.631  19.444  1.00 21.28           C  
-ANISOU  356  CA  LYS A  44     2059   2956   3071   -400   -255   -855       C  
-ATOM    357  C   LYS A  44      29.227 -26.110  19.235  1.00 21.78           C  
-ANISOU  357  C   LYS A  44     2108   2964   3202   -392   -315   -971       C  
-ATOM    358  O   LYS A  44      28.940 -24.967  19.552  1.00 23.47           O  
-ANISOU  358  O   LYS A  44     2332   3172   3414   -407   -380   -986       O  
-ATOM    359  CB  LYS A  44      30.944 -26.746  20.947  1.00 21.45           C  
-ANISOU  359  CB  LYS A  44     2062   2992   3095   -429   -187   -813       C  
-ATOM    360  CG  LYS A  44      30.318 -27.960  21.615  1.00 21.19           C  
-ANISOU  360  CG  LYS A  44     1988   2934   3130   -425    -94   -861       C  
-ATOM    361  CD  LYS A  44      30.501 -27.949  23.131  1.00 35.38           C  
-ANISOU  361  CD  LYS A  44     3768   4742   4933   -454    -35   -828       C  
-ATOM    362  CE  LYS A  44      31.946 -28.202  23.520  1.00 45.21           C  
-ANISOU  362  CE  LYS A  44     5030   6042   6105   -468     13   -708       C  
-ATOM    363  NZ  LYS A  44      32.201 -28.024  24.985  1.00 48.12           N  
-ANISOU  363  NZ  LYS A  44     5387   6425   6471   -498     59   -669       N  
-ATOM    364  N   LEU A  45      28.342 -26.939  18.695  1.00 18.06           N  
-ANISOU  364  N   LEU A  45     1614   2454   2792   -367   -295  -1053       N  
-ATOM    365  CA  LEU A  45      26.960 -26.503  18.506  1.00 21.60           C  
-ANISOU  365  CA  LEU A  45     2047   2850   3311   -358   -349  -1166       C  
-ATOM    366  C   LEU A  45      26.112 -26.868  19.720  1.00 23.72           C  
-ANISOU  366  C   LEU A  45     2273   3091   3650   -371   -290  -1223       C  
-ATOM    367  O   LEU A  45      25.174 -26.149  20.086  1.00 26.91           O  
-ANISOU  367  O   LEU A  45     2664   3463   4097   -378   -334  -1294       O  
-ATOM    368  CB  LEU A  45      26.374 -27.107  17.242  1.00 18.66           C  
-ANISOU  368  CB  LEU A  45     1672   2448   2970   -324   -369  -1232       C  
-ATOM    369  CG  LEU A  45      27.060 -26.735  15.927  1.00 21.04           C  
-ANISOU  369  CG  LEU A  45     2015   2773   3208   -308   -434  -1189       C  
-ATOM    370  CD1 LEU A  45      26.280 -27.303  14.759  1.00 25.65           C  
-ANISOU  370  CD1 LEU A  45     2593   3319   3834   -274   -455  -1270       C  
-ATOM    371  CD2 LEU A  45      27.182 -25.232  15.792  1.00 25.51           C  
-ANISOU  371  CD2 LEU A  45     2612   3347   3734   -322   -533  -1174       C  
-ATOM    372  N   GLY A  46      26.450 -27.981  20.357  1.00 25.86           N  
-ANISOU  372  N   GLY A  46     2522   3373   3930   -376   -191  -1192       N  
-ATOM    373  CA  GLY A  46      25.697 -28.415  21.512  1.00 29.67           C  
-ANISOU  373  CA  GLY A  46     2964   3831   4477   -390   -128  -1240       C  
-ATOM    374  C   GLY A  46      26.109 -29.772  22.036  1.00 27.87           C  
-ANISOU  374  C   GLY A  46     2716   3615   4259   -391    -17  -1204       C  
-ATOM    375  O   GLY A  46      26.994 -30.427  21.499  1.00 24.72           O  
-ANISOU  375  O   GLY A  46     2332   3243   3816   -380     13  -1141       O  
-ATOM    376  N   ARG A  47      25.423 -30.196  23.088  1.00 29.31           N  
-ANISOU  376  N   ARG A  47     2862   3775   4501   -404     42  -1248       N  
-ATOM    377  CA  ARG A  47      25.749 -31.420  23.783  1.00 33.06           C  
-ANISOU  377  CA  ARG A  47     3314   4259   4987   -410    148  -1215       C  
-ATOM    378  C   ARG A  47      24.461 -32.132  24.150  1.00 36.27           C  
-ANISOU  378  C   ARG A  47     3677   4617   5486   -406    191  -1316       C  
-ATOM    379  O   ARG A  47      23.528 -31.508  24.652  1.00 37.40           O  
-ANISOU  379  O   ARG A  47     3802   4732   5675   -416    163  -1384       O  
-ATOM    380  CB  ARG A  47      26.542 -31.090  25.050  1.00 32.66           C  
-ANISOU  380  CB  ARG A  47     3268   4244   4896   -442    187  -1134       C  
-ATOM    381  CG  ARG A  47      26.839 -32.287  25.915  1.00 41.28           C  
-ANISOU  381  CG  ARG A  47     4337   5345   6004   -451    297  -1102       C  
-ATOM    382  CD  ARG A  47      28.247 -32.213  26.464  1.00 50.96           C  
-ANISOU  382  CD  ARG A  47     5586   6625   7152   -469    329   -982       C  
-ATOM    383  NE  ARG A  47      28.286 -31.582  27.774  1.00 57.17           N  
-ANISOU  383  NE  ARG A  47     6366   7422   7935   -499    342   -960       N  
-ATOM    384  CZ  ARG A  47      29.381 -31.070  28.330  1.00 55.87           C  
-ANISOU  384  CZ  ARG A  47     6225   7301   7703   -519    344   -864       C  
-ATOM    385  NH1 ARG A  47      30.544 -31.094  27.688  1.00 47.52           N  
-ANISOU  385  NH1 ARG A  47     5199   6283   6575   -512    332   -779       N  
-ATOM    386  NH2 ARG A  47      29.307 -30.525  29.533  1.00 60.60           N  
-ANISOU  386  NH2 ARG A  47     6816   7904   8304   -545    355   -854       N  
-ATOM    387  N   GLY A  48      24.407 -33.430  23.879  1.00 36.61           N  
-ANISOU  387  N   GLY A  48     3704   4649   5558   -391    258  -1327       N  
-ATOM    388  CA  GLY A  48      23.269 -34.246  24.253  1.00 43.19           C  
-ANISOU  388  CA  GLY A  48     4495   5439   6478   -388    309  -1414       C  
-ATOM    389  C   GLY A  48      23.695 -35.271  25.280  1.00 43.23           C  
-ANISOU  389  C   GLY A  48     4480   5458   6487   -404    417  -1368       C  
-ATOM    390  O   GLY A  48      24.866 -35.337  25.638  1.00 43.65           O  
-ANISOU  390  O   GLY A  48     4553   5554   6477   -415    448  -1269       O  
-ATOM    391  N   LYS A  49      22.750 -36.074  25.756  1.00 47.80           N  
-ANISOU  391  N   LYS A  49     5020   6000   7142   -406    473  -1438       N  
-ATOM    392  CA  LYS A  49      23.079 -37.111  26.722  1.00 45.40           C  
-ANISOU  392  CA  LYS A  49     4697   5706   6848   -421    577  -1399       C  
-ATOM    393  C   LYS A  49      24.058 -38.100  26.109  1.00 35.92           C  
-ANISOU  393  C   LYS A  49     3512   4528   5606   -404    619  -1331       C  
-ATOM    394  O   LYS A  49      24.841 -38.728  26.817  1.00 41.93           O  
-ANISOU  394  O   LYS A  49     4275   5316   6341   -418    692  -1260       O  
-ATOM    395  CB  LYS A  49      21.813 -37.830  27.215  1.00 51.88           C  
-ANISOU  395  CB  LYS A  49     5472   6480   7761   -424    626  -1493       C  
-ATOM    396  CG  LYS A  49      20.568 -37.561  26.373  1.00 54.96           C  
-ANISOU  396  CG  LYS A  49     5847   6824   8212   -404    563  -1604       C  
-ATOM    397  CD  LYS A  49      19.284 -38.049  27.060  1.00 63.39           C  
-ANISOU  397  CD  LYS A  49     6868   7849   9370   -413    606  -1697       C  
-ATOM    398  CE  LYS A  49      19.201 -39.569  27.129  1.00 66.56           C  
-ANISOU  398  CE  LYS A  49     7247   8235   9810   -407    696  -1702       C  
-ATOM    399  NZ  LYS A  49      17.842 -40.044  27.535  1.00 67.59           N  
-ANISOU  399  NZ  LYS A  49     7330   8317  10032   -411    727  -1804       N  
-ATOM    400  N   TYR A  50      24.038 -38.206  24.784  1.00 34.83           N  
-ANISOU  400  N   TYR A  50     3390   4382   5461   -375    572  -1352       N  
-ATOM    401  CA  TYR A  50      24.788 -39.255  24.100  1.00 35.43           C  
-ANISOU  401  CA  TYR A  50     3478   4473   5510   -355    613  -1304       C  
-ATOM    402  C   TYR A  50      25.979 -38.786  23.272  1.00 28.57           C  
-ANISOU  402  C   TYR A  50     2652   3648   4554   -343    566  -1221       C  
-ATOM    403  O   TYR A  50      26.767 -39.608  22.816  1.00 28.32           O  
-ANISOU  403  O   TYR A  50     2633   3638   4490   -329    604  -1168       O  
-ATOM    404  CB  TYR A  50      23.855 -40.049  23.191  1.00 43.16           C  
-ANISOU  404  CB  TYR A  50     4438   5407   6552   -327    611  -1393       C  
-ATOM    405  CG  TYR A  50      22.747 -40.756  23.925  1.00 54.97           C  
-ANISOU  405  CG  TYR A  50     5890   6861   8134   -336    668  -1470       C  
-ATOM    406  CD1 TYR A  50      23.027 -41.750  24.852  1.00 56.71           C  
-ANISOU  406  CD1 TYR A  50     6093   7087   8367   -351    765  -1436       C  
-ATOM    407  CD2 TYR A  50      21.416 -40.437  23.682  1.00 61.84           C  
-ANISOU  407  CD2 TYR A  50     6737   7684   9074   -330    626  -1579       C  
-ATOM    408  CE1 TYR A  50      22.012 -42.403  25.522  1.00 64.71           C  
-ANISOU  408  CE1 TYR A  50     7066   8062   9459   -361    818  -1506       C  
-ATOM    409  CE2 TYR A  50      20.395 -41.085  24.347  1.00 66.52           C  
-ANISOU  409  CE2 TYR A  50     7289   8240   9747   -339    679  -1650       C  
-ATOM    410  CZ  TYR A  50      20.698 -42.068  25.265  1.00 69.94           C  
-ANISOU  410  CZ  TYR A  50     7704   8680  10190   -355    775  -1613       C  
-ATOM    411  OH  TYR A  50      19.681 -42.716  25.929  1.00 76.85           O  
-ANISOU  411  OH  TYR A  50     8539   9518  11144   -365    829  -1682       O  
-ATOM    412  N   SER A  51      26.097 -37.481  23.062  1.00 26.64           N  
-ANISOU  412  N   SER A  51     2430   3417   4273   -349    484  -1212       N  
-ATOM    413  CA  SER A  51      27.116 -36.963  22.159  1.00 21.41           C  
-ANISOU  413  CA  SER A  51     1809   2793   3533   -338    430  -1142       C  
-ATOM    414  C   SER A  51      27.318 -35.465  22.302  1.00 20.30           C  
-ANISOU  414  C   SER A  51     1692   2671   3351   -354    351  -1120       C  
-ATOM    415  O   SER A  51      26.550 -34.772  22.982  1.00 24.16           O  
-ANISOU  415  O   SER A  51     2165   3138   3875   -371    328  -1170       O  
-ATOM    416  CB  SER A  51      26.716 -37.240  20.715  1.00 32.43           C  
-ANISOU  416  CB  SER A  51     3213   4167   4944   -303    385  -1195       C  
-ATOM    417  OG  SER A  51      25.740 -36.300  20.289  1.00 34.14           O  
-ANISOU  417  OG  SER A  51     3429   4351   5193   -299    301  -1276       O  
-ATOM    418  N   GLU A  52      28.372 -34.982  21.655  1.00 16.13           N  
-ANISOU  418  N   GLU A  52     1581   2569   1979    -40   -314   -497       N  
-ATOM    419  CA  GLU A  52      28.588 -33.560  21.444  1.00 23.57           C  
-ANISOU  419  CA  GLU A  52     2481   3477   2996    -23   -320   -459       C  
-ATOM    420  C   GLU A  52      28.637 -33.333  19.949  1.00 20.74           C  
-ANISOU  420  C   GLU A  52     2140   3135   2604    -51   -336   -394       C  
-ATOM    421  O   GLU A  52      29.212 -34.133  19.223  1.00 18.50           O  
-ANISOU  421  O   GLU A  52     1906   2875   2249    -74   -325   -391       O  
-ATOM    422  CB  GLU A  52      29.909 -33.105  22.062  1.00 28.68           C  
-ANISOU  422  CB  GLU A  52     3125   4090   3683      3   -285   -494       C  
-ATOM    423  CG  GLU A  52      29.905 -33.045  23.568  1.00 38.23           C  
-ANISOU  423  CG  GLU A  52     4307   5276   4942     36   -270   -555       C  
-ATOM    424  CD  GLU A  52      31.054 -32.226  24.100  1.00 38.03           C  
-ANISOU  424  CD  GLU A  52     4263   5210   4976     65   -242   -576       C  
-ATOM    425  OE1 GLU A  52      32.138 -32.267  23.489  1.00 34.57           O  
-ANISOU  425  OE1 GLU A  52     3854   4769   4512     56   -223   -568       O  
-ATOM    426  OE2 GLU A  52      30.868 -31.529  25.113  1.00 41.69           O  
-ANISOU  426  OE2 GLU A  52     4683   5645   5513     95   -241   -600       O  
-ATOM    427  N   VAL A  53      28.049 -32.235  19.495  1.00 13.76           N  
-ANISOU  427  N   VAL A  53     1217   2239   1773    -47   -362   -341       N  
-ATOM    428  CA  VAL A  53      27.943 -31.958  18.074  1.00 13.64           C  
-ANISOU  428  CA  VAL A  53     1213   2240   1730    -73   -381   -274       C  
-ATOM    429  C   VAL A  53      28.707 -30.679  17.736  1.00 16.95           C  
-ANISOU  429  C   VAL A  53     1607   2624   2210    -58   -373   -241       C  
-ATOM    430  O   VAL A  53      28.517 -29.641  18.380  1.00 22.10           O  
-ANISOU  430  O   VAL A  53     2210   3243   2944    -31   -377   -241       O  
-ATOM    431  CB  VAL A  53      26.460 -31.816  17.660  1.00 18.78           C  
-ANISOU  431  CB  VAL A  53     1842   2912   2382    -87   -421   -232       C  
-ATOM    432  CG1 VAL A  53      26.342 -31.425  16.200  1.00 21.71           C  
-ANISOU  432  CG1 VAL A  53     2220   3297   2730   -111   -442   -161       C  
-ATOM    433  CG2 VAL A  53      25.710 -33.115  17.919  1.00 17.35           C  
-ANISOU  433  CG2 VAL A  53     1688   2768   2138   -104   -429   -263       C  
-ATOM    434  N   PHE A  54      29.553 -30.761  16.711  1.00 15.01           N  
-ANISOU  434  N   PHE A  54     1395   2387   1923    -75   -363   -212       N  
-ATOM    435  CA  PHE A  54      30.391 -29.648  16.297  1.00 17.97           C  
-ANISOU  435  CA  PHE A  54     1751   2729   2346    -64   -354   -180       C  
-ATOM    436  C   PHE A  54      30.131 -29.255  14.846  1.00 24.44           C  
-ANISOU  436  C   PHE A  54     2576   3566   3145    -88   -377   -106       C  
-ATOM    437  O   PHE A  54      29.832 -30.102  14.000  1.00 25.40           O  
-ANISOU  437  O   PHE A  54     2735   3726   3189   -118   -388    -87       O  
-ATOM    438  CB  PHE A  54      31.869 -30.031  16.448  1.00 18.44           C  
-ANISOU  438  CB  PHE A  54     1845   2779   2382    -59   -315   -217       C  
-ATOM    439  CG  PHE A  54      32.284 -30.353  17.857  1.00 19.95           C  
-ANISOU  439  CG  PHE A  54     2031   2951   2597    -34   -289   -290       C  
-ATOM    440  CD1 PHE A  54      32.931 -29.402  18.634  1.00 18.78           C  
-ANISOU  440  CD1 PHE A  54     1848   2760   2528     -2   -271   -310       C  
-ATOM    441  CD2 PHE A  54      32.055 -31.607  18.399  1.00 18.57           C  
-ANISOU  441  CD2 PHE A  54     1887   2802   2366    -41   -281   -339       C  
-ATOM    442  CE1 PHE A  54      33.339 -29.687  19.936  1.00 24.13           C  
-ANISOU  442  CE1 PHE A  54     2521   3420   3227     23   -246   -378       C  
-ATOM    443  CE2 PHE A  54      32.464 -31.908  19.707  1.00 17.56           C  
-ANISOU  443  CE2 PHE A  54     1756   2657   2260    -16   -256   -406       C  
-ATOM    444  CZ  PHE A  54      33.104 -30.942  20.475  1.00 23.65           C  
-ANISOU  444  CZ  PHE A  54     2491   3386   3110     16   -239   -426       C  
-ATOM    445  N   GLU A  55      30.227 -27.968  14.548  1.00 22.30           N  
-ANISOU  445  N   GLU A  55     2266   3266   2939    -76   -385    -63       N  
-ATOM    446  CA  GLU A  55      30.323 -27.556  13.158  1.00 20.33           C  
-ANISOU  446  CA  GLU A  55     2027   3028   2669    -96   -398      4       C  
-ATOM    447  C   GLU A  55      31.766 -27.797  12.768  1.00 22.63           C  
-ANISOU  447  C   GLU A  55     2355   3314   2927   -101   -366     -5       C  
-ATOM    448  O   GLU A  55      32.651 -27.626  13.588  1.00 19.13           O  
-ANISOU  448  O   GLU A  55     1907   2843   2518    -79   -338    -48       O  
-ATOM    449  CB  GLU A  55      29.979 -26.083  13.007  1.00 20.72           C  
-ANISOU  449  CB  GLU A  55     2023   3046   2803    -80   -416     52       C  
-ATOM    450  CG  GLU A  55      30.209 -25.530  11.613  1.00 27.79           C  
-ANISOU  450  CG  GLU A  55     2925   3949   3686    -98   -427    122       C  
-ATOM    451  CD  GLU A  55      29.842 -24.061  11.504  1.00 33.49           C  
-ANISOU  451  CD  GLU A  55     3592   4638   4493    -80   -444    169       C  
-ATOM    452  OE1 GLU A  55      28.641 -23.745  11.593  1.00 46.55           O  
-ANISOU  452  OE1 GLU A  55     5216   6299   6174    -79   -474    189       O  
-ATOM    453  OE2 GLU A  55      30.749 -23.229  11.322  1.00 43.53           O  
-ANISOU  453  OE2 GLU A  55     4853   5880   5807    -68   -428    185       O  
-ATOM    454  N   ALA A  56      32.013 -28.205  11.531  1.00 21.27           N  
-ANISOU  454  N   ALA A  56     2221   3171   2690   -129   -370     34       N  
-ATOM    455  CA  ALA A  56      33.384 -28.450  11.106  1.00 19.79           C  
-ANISOU  455  CA  ALA A  56     2070   2981   2469   -134   -340     27       C  
-ATOM    456  C   ALA A  56      33.534 -28.207   9.623  1.00 17.35           C  
-ANISOU  456  C   ALA A  56     1778   2690   2125   -158   -352     94       C  
-ATOM    457  O   ALA A  56      32.558 -27.981   8.923  1.00 19.31           O  
-ANISOU  457  O   ALA A  56     2014   2956   2367   -172   -384    143       O  
-ATOM    458  CB  ALA A  56      33.823 -29.867  11.462  1.00 17.19           C  
-ANISOU  458  CB  ALA A  56     1792   2677   2065   -145   -319    -30       C  
-ATOM    459  N   ILE A  57      34.773 -28.241   9.154  1.00 14.84           N  
-ANISOU  459  N   ILE A  57     1488   2366   1784   -162   -327     97       N  
-ATOM    460  CA  ILE A  57      35.046 -28.091   7.739  1.00 18.59           C  
-ANISOU  460  CA  ILE A  57     1984   2860   2220   -184   -335    157       C  
-ATOM    461  C   ILE A  57      35.735 -29.359   7.265  1.00 21.03           C  
-ANISOU  461  C   ILE A  57     2354   3201   2434   -207   -317    136       C  
-ATOM    462  O   ILE A  57      36.643 -29.877   7.920  1.00 20.95           O  
-ANISOU  462  O   ILE A  57     2367   3183   2411   -198   -286     82       O  
-ATOM    463  CB  ILE A  57      35.917 -26.844   7.456  1.00 25.09           C  
-ANISOU  463  CB  ILE A  57     2781   3645   3105   -169   -322    190       C  
-ATOM    464  CG1 ILE A  57      36.276 -26.768   5.974  1.00 30.10           C  
-ANISOU  464  CG1 ILE A  57     3441   4301   3693   -193   -328    251       C  
-ATOM    465  CG2 ILE A  57      37.184 -26.883   8.282  1.00 33.95           C  
-ANISOU  465  CG2 ILE A  57     3912   4740   4248   -149   -283    136       C  
-ATOM    466  CD1 ILE A  57      37.222 -25.638   5.630  1.00 39.51           C  
-ANISOU  466  CD1 ILE A  57     4614   5459   4939   -180   -313    283       C  
-ATOM    467  N   ASN A  58      35.261 -29.891   6.152  1.00 18.95           N  
-ANISOU  467  N   ASN A  58     2119   2978   2104   -237   -337    176       N  
-ATOM    468  CA  ASN A  58      35.931 -30.997   5.501  1.00 19.65           C  
-ANISOU  468  CA  ASN A  58     2266   3099   2102   -260   -322    165       C  
-ATOM    469  C   ASN A  58      37.007 -30.377   4.627  1.00 20.12           C  
-ANISOU  469  C   ASN A  58     2334   3147   2163   -262   -308    204       C  
-ATOM    470  O   ASN A  58      36.698 -29.790   3.598  1.00 24.45           O  
-ANISOU  470  O   ASN A  58     2873   3704   2714   -274   -328    268       O  
-ATOM    471  CB  ASN A  58      34.920 -31.765   4.643  1.00 20.67           C  
-ANISOU  471  CB  ASN A  58     2418   3274   2160   -291   -352    195       C  
-ATOM    472  CG  ASN A  58      35.549 -32.901   3.851  1.00 26.18           C  
-ANISOU  472  CG  ASN A  58     3177   4008   2761   -317   -340    190       C  
-ATOM    473  OD1 ASN A  58      36.765 -32.968   3.688  1.00 20.69           O  
-ANISOU  473  OD1 ASN A  58     2506   3304   2050   -315   -312    179       O  
-ATOM    474  ND2 ASN A  58      34.705 -33.791   3.333  1.00 25.62           N  
-ANISOU  474  ND2 ASN A  58     3131   3980   2624   -343   -362    199       N  
-ATOM    475  N   ILE A  59      38.267 -30.492   5.030  1.00 23.02           N  
-ANISOU  475  N   ILE A  59     2718   3495   2532   -251   -272    168       N  
-ATOM    476  CA  ILE A  59      39.337 -29.794   4.321  1.00 18.90           C  
-ANISOU  476  CA  ILE A  59     2199   2957   2023   -249   -256    202       C  
-ATOM    477  C   ILE A  59      39.719 -30.421   2.976  1.00 25.46           C  
-ANISOU  477  C   ILE A  59     3078   3825   2769   -279   -258    238       C  
-ATOM    478  O   ILE A  59      40.600 -29.913   2.289  1.00 28.14           O  
-ANISOU  478  O   ILE A  59     3423   4155   3112   -280   -245    270       O  
-ATOM    479  CB  ILE A  59      40.601 -29.638   5.194  1.00 19.71           C  
-ANISOU  479  CB  ILE A  59     2304   3026   2160   -226   -218    152       C  
-ATOM    480  CG1 ILE A  59      41.247 -30.989   5.474  1.00 23.83           C  
-ANISOU  480  CG1 ILE A  59     2877   3569   2606   -235   -193     96       C  
-ATOM    481  CG2 ILE A  59      40.274 -28.943   6.495  1.00 24.78           C  
-ANISOU  481  CG2 ILE A  59     2896   3629   2889   -195   -216    118       C  
-ATOM    482  CD1 ILE A  59      42.601 -30.869   6.181  1.00 27.74           C  
-ANISOU  482  CD1 ILE A  59     3379   4035   3127   -215   -154     50       C  
-ATOM    483  N   THR A  60      39.070 -31.520   2.602  1.00 23.15           N  
-ANISOU  483  N   THR A  60     2820   3576   2402   -303   -272    233       N  
-ATOM    484  CA  THR A  60      39.301 -32.108   1.281  1.00 28.27           C  
-ANISOU  484  CA  THR A  60     3511   4262   2968   -333   -278    270       C  
-ATOM    485  C   THR A  60      38.400 -31.484   0.206  1.00 33.71           C  
-ANISOU  485  C   THR A  60     4180   4966   3661   -347   -313    345       C  
-ATOM    486  O   THR A  60      38.637 -31.673  -0.991  1.00 35.69           O  
-ANISOU  486  O   THR A  60     4458   5244   3858   -368   -318    387       O  
-ATOM    487  CB  THR A  60      39.124 -33.643   1.272  1.00 28.82           C  
-ANISOU  487  CB  THR A  60     3632   4373   2947   -354   -276    231       C  
-ATOM    488  OG1 THR A  60      37.726 -33.972   1.282  1.00 33.21           O  
-ANISOU  488  OG1 THR A  60     4177   4951   3490   -365   -308    240       O  
-ATOM    489  CG2 THR A  60      39.824 -34.272   2.470  1.00 34.17           C  
-ANISOU  489  CG2 THR A  60     4324   5033   3624   -338   -244    155       C  
-ATOM    490  N   ASN A  61      37.372 -30.750   0.632  1.00 32.24           N  
-ANISOU  490  N   ASN A  61     3946   4765   3538   -335   -337    360       N  
-ATOM    491  CA  ASN A  61      36.517 -30.011  -0.301  1.00 23.44           C  
-ANISOU  491  CA  ASN A  61     2807   3660   2439   -344   -370    431       C  
-ATOM    492  C   ASN A  61      36.170 -28.609   0.202  1.00 26.12           C  
-ANISOU  492  C   ASN A  61     3085   3958   2881   -318   -379    452       C  
-ATOM    493  O   ASN A  61      35.462 -27.857  -0.460  1.00 32.10           O  
-ANISOU  493  O   ASN A  61     3815   4717   3664   -322   -406    510       O  
-ATOM    494  CB  ASN A  61      35.249 -30.802  -0.648  1.00 24.84           C  
-ANISOU  494  CB  ASN A  61     2997   3880   2563   -367   -402    440       C  
-ATOM    495  CG  ASN A  61      34.439 -31.177   0.578  1.00 24.36           C  
-ANISOU  495  CG  ASN A  61     2918   3812   2525   -355   -408    388       C  
-ATOM    496  OD1 ASN A  61      34.612 -30.603   1.655  1.00 21.81           O  
-ANISOU  496  OD1 ASN A  61     2562   3452   2273   -328   -395    356       O  
-ATOM    497  ND2 ASN A  61      33.533 -32.135   0.417  1.00 28.38           N  
-ANISOU  497  ND2 ASN A  61     3447   4359   2976   -376   -428    380       N  
-ATOM    498  N   ASN A  62      36.702 -28.257   1.367  1.00 28.34           N  
-ANISOU  498  N   ASN A  62     3345   4200   3222   -292   -356    405       N  
-ATOM    499  CA  ASN A  62      36.363 -27.004   2.041  1.00 21.69           C  
-ANISOU  499  CA  ASN A  62     2444   3316   2479   -265   -363    414       C  
-ATOM    500  C   ASN A  62      34.861 -26.833   2.269  1.00 26.87           C  
-ANISOU  500  C   ASN A  62     3068   3981   3160   -265   -398    428       C  
-ATOM    501  O   ASN A  62      34.375 -25.710   2.369  1.00 36.30           O  
-ANISOU  501  O   ASN A  62     4214   5150   4427   -250   -414    461       O  
-ATOM    502  CB  ASN A  62      36.946 -25.785   1.305  1.00 24.88           C  
-ANISOU  502  CB  ASN A  62     2826   3696   2930   -258   -361    471       C  
-ATOM    503  CG  ASN A  62      38.452 -25.672   1.464  1.00 36.50           C  
-ANISOU  503  CG  ASN A  62     4315   5144   4409   -248   -323    448       C  
-ATOM    504  OD1 ASN A  62      39.053 -26.363   2.291  1.00 36.83           O  
-ANISOU  504  OD1 ASN A  62     4377   5181   4434   -240   -297    385       O  
-ATOM    505  ND2 ASN A  62      39.071 -24.797   0.676  1.00 36.86           N  
-ANISOU  505  ND2 ASN A  62     4352   5176   4479   -247   -318    498       N  
-ATOM    506  N   GLU A  63      34.137 -27.947   2.364  1.00 20.47           N  
-ANISOU  506  N   GLU A  63     2283   3206   2288   -282   -411    404       N  
-ATOM    507  CA  GLU A  63      32.700 -27.902   2.646  1.00 27.40           C  
-ANISOU  507  CA  GLU A  63     3132   4094   3184   -282   -443    412       C  
-ATOM    508  C   GLU A  63      32.417 -27.958   4.145  1.00 26.20           C  
-ANISOU  508  C   GLU A  63     2955   3918   3081   -258   -435    350       C  
-ATOM    509  O   GLU A  63      33.075 -28.670   4.900  1.00 25.93           O  
-ANISOU  509  O   GLU A  63     2945   3880   3027   -252   -408    290       O  
-ATOM    510  CB  GLU A  63      31.973 -29.062   1.966  1.00 28.11           C  
-ANISOU  510  CB  GLU A  63     3261   4236   3184   -313   -463    419       C  
-ATOM    511  CG  GLU A  63      32.280 -29.215   0.497  1.00 42.84           C  
-ANISOU  511  CG  GLU A  63     5158   6131   4989   -339   -470    473       C  
-ATOM    512  CD  GLU A  63      31.424 -28.342  -0.383  1.00 58.90           C  
-ANISOU  512  CD  GLU A  63     7160   8171   7047   -345   -503    545       C  
-ATOM    513  OE1 GLU A  63      30.940 -27.294   0.099  1.00 64.41           O  
-ANISOU  513  OE1 GLU A  63     7808   8839   7827   -325   -514    559       O  
-ATOM    514  OE2 GLU A  63      31.233 -28.715  -1.561  1.00 60.51           O  
-ANISOU  514  OE2 GLU A  63     7391   8411   7189   -371   -518    587       O  
-ATOM    515  N   LYS A  64      31.414 -27.208   4.570  1.00 26.31           N  
-ANISOU  515  N   LYS A  64     2921   3917   3158   -245   -459    365       N  
-ATOM    516  CA  LYS A  64      30.963 -27.268   5.942  1.00 26.31           C  
-ANISOU  516  CA  LYS A  64     2895   3898   3202   -223   -456    311       C  
-ATOM    517  C   LYS A  64      30.304 -28.625   6.204  1.00 22.12           C  
-ANISOU  517  C   LYS A  64     2397   3405   2602   -241   -463    273       C  
-ATOM    518  O   LYS A  64      29.598 -29.153   5.355  1.00 20.96           O  
-ANISOU  518  O   LYS A  64     2270   3297   2399   -266   -486    304       O  
-ATOM    519  CB  LYS A  64      29.981 -26.130   6.190  1.00 37.02           C  
-ANISOU  519  CB  LYS A  64     4194   5233   4639   -207   -482    343       C  
-ATOM    520  CG  LYS A  64      29.812 -25.747   7.630  1.00 47.84           C  
-ANISOU  520  CG  LYS A  64     5527   6570   6082   -176   -474    293       C  
-ATOM    521  CD  LYS A  64      29.031 -24.452   7.729  1.00 54.69           C  
-ANISOU  521  CD  LYS A  64     6336   7411   7033   -159   -498    333       C  
-ATOM    522  CE  LYS A  64      29.715 -23.340   6.953  1.00 52.07           C  
-ANISOU  522  CE  LYS A  64     5988   7055   6739   -154   -494    386       C  
-ATOM    523  NZ  LYS A  64      28.918 -22.082   7.015  1.00 50.83           N  
-ANISOU  523  NZ  LYS A  64     5775   6874   6663   -138   -519    427       N  
-ATOM    524  N   VAL A  65      30.565 -29.195   7.373  1.00 18.69           N  
-ANISOU  524  N   VAL A  65     1969   2961   2173   -226   -442    205       N  
-ATOM    525  CA  VAL A  65      29.913 -30.418   7.802  1.00 21.64           C  
-ANISOU  525  CA  VAL A  65     2366   3364   2490   -239   -448    164       C  
-ATOM    526  C   VAL A  65      29.625 -30.341   9.292  1.00 17.68           C  
-ANISOU  526  C   VAL A  65     1836   2838   2045   -212   -440    107       C  
-ATOM    527  O   VAL A  65      29.958 -29.361   9.950  1.00 18.67           O  
-ANISOU  527  O   VAL A  65     1923   2923   2248   -184   -430    100       O  
-ATOM    528  CB  VAL A  65      30.784 -31.672   7.542  1.00 13.04           C  
-ANISOU  528  CB  VAL A  65     1339   2301   1316   -257   -423    131       C  
-ATOM    529  CG1 VAL A  65      31.057 -31.825   6.059  1.00 21.10           C  
-ANISOU  529  CG1 VAL A  65     2391   3349   2276   -285   -431    185       C  
-ATOM    530  CG2 VAL A  65      32.090 -31.603   8.344  1.00 15.99           C  
-ANISOU  530  CG2 VAL A  65     1719   2643   1714   -235   -384     81       C  
-ATOM    531  N   VAL A  66      29.005 -31.385   9.820  1.00 16.59           N  
-ANISOU  531  N   VAL A  66     1715   2724   1866   -220   -444     67       N  
-ATOM    532  CA AVAL A  66      28.745 -31.475  11.250  1.00 14.78           C  
-ANISOU  532  CA AVAL A  66     1462   2475   1679   -196   -435      9       C  
-ATOM    533  CA BVAL A  66      28.758 -31.463  11.250  0.00 18.02           C  
-ANISOU  533  CA BVAL A  66     1872   2884   2089   -195   -435      9       C  
-ATOM    534  C   VAL A  66      29.320 -32.773  11.792  1.00 20.05           C  
-ANISOU  534  C   VAL A  66     2175   3158   2286   -201   -409    -54       C  
-ATOM    535  O   VAL A  66      29.225 -33.822  11.148  1.00 20.95           O  
-ANISOU  535  O   VAL A  66     2333   3308   2317   -229   -413    -52       O  
-ATOM    536  CB AVAL A  66      27.225 -31.384  11.528  1.00 20.20           C  
-ANISOU  536  CB AVAL A  66     2116   3173   2386   -197   -470     21       C  
-ATOM    537  CB BVAL A  66      27.258 -31.332  11.580  0.00 20.85           C  
-ANISOU  537  CB BVAL A  66     2197   3253   2474   -195   -469     19       C  
-ATOM    538  CG1AVAL A  66      26.895 -31.928  12.903  1.00 25.84           C  
-ANISOU  538  CG1AVAL A  66     2823   3881   3116   -180   -460    -45       C  
-ATOM    539  CG1BVAL A  66      26.533 -32.634  11.299  0.00 20.48           C  
-ANISOU  539  CG1BVAL A  66     2186   3251   2344   -222   -482      8       C  
-ATOM    540  CG2AVAL A  66      26.771 -29.942  11.392  1.00 22.92           C  
-ANISOU  540  CG2AVAL A  66     2406   3490   2812   -180   -489     69       C  
-ATOM    541  CG2BVAL A  66      27.069 -30.918  13.024  0.00 23.51           C  
-ANISOU  541  CG2BVAL A  66     2493   3557   2882   -162   -460    -28       C  
-ATOM    542  N   VAL A  67      29.937 -32.703  12.969  1.00 16.83           N  
-ANISOU  542  N   VAL A  67     1757   2720   1917   -174   -382   -109       N  
-ATOM    543  CA  VAL A  67      30.561 -33.870  13.556  1.00 14.61           C  
-ANISOU  543  CA  VAL A  67     1517   2450   1584   -176   -355   -171       C  
-ATOM    544  C   VAL A  67      29.936 -34.202  14.892  1.00 14.30           C  
-ANISOU  544  C   VAL A  67     1457   2404   1571   -158   -354   -225       C  
-ATOM    545  O   VAL A  67      29.940 -33.386  15.812  1.00 15.49           O  
-ANISOU  545  O   VAL A  67     1566   2521   1800   -129   -348   -243       O  
-ATOM    546  CB  VAL A  67      32.074 -33.641  13.773  1.00 15.21           C  
-ANISOU  546  CB  VAL A  67     1606   2499   1673   -161   -317   -195       C  
-ATOM    547  CG1 VAL A  67      32.709 -34.844  14.458  1.00 21.55           C  
-ANISOU  547  CG1 VAL A  67     2451   3313   2426   -161   -288   -262       C  
-ATOM    548  CG2 VAL A  67      32.750 -33.332  12.450  1.00 16.51           C  
-ANISOU  548  CG2 VAL A  67     1792   2671   1810   -179   -317   -142       C  
-ATOM    549  N   LYS A  68      29.420 -35.421  15.000  1.00 12.79           N  
-ANISOU  549  N   LYS A  68     1297   2246   1315   -176   -358   -252       N  
-ATOM    550  CA  LYS A  68      28.808 -35.906  16.223  1.00 12.64           C  
-ANISOU  550  CA  LYS A  68     1266   2226   1311   -162   -357   -304       C  
-ATOM    551  C   LYS A  68      29.741 -36.897  16.913  1.00 15.60           C  
-ANISOU  551  C   LYS A  68     1679   2602   1646   -157   -321   -369       C  
-ATOM    552  O   LYS A  68      29.842 -38.066  16.509  1.00 15.67           O  
-ANISOU  552  O   LYS A  68     1737   2644   1575   -181   -316   -382       O  
-ATOM    553  CB  LYS A  68      27.469 -36.574  15.880  1.00 12.17           C  
-ANISOU  553  CB  LYS A  68     1212   2203   1208   -186   -389   -288       C  
-ATOM    554  CG  LYS A  68      26.699 -37.135  17.048  1.00 11.49           C  
-ANISOU  554  CG  LYS A  68     1114   2121   1131   -175   -391   -337       C  
-ATOM    555  CD  LYS A  68      25.333 -37.603  16.526  1.00 15.60           C  
-ANISOU  555  CD  LYS A  68     1635   2677   1615   -200   -426   -308       C  
-ATOM    556  CE  LYS A  68      24.525 -38.341  17.552  1.00 20.22           C  
-ANISOU  556  CE  LYS A  68     2216   3273   2196   -194   -430   -355       C  
-ATOM    557  NZ  LYS A  68      23.236 -38.802  16.909  1.00 15.69           N  
-ANISOU  557  NZ  LYS A  68     1645   2735   1582   -222   -465   -323       N  
-ATOM    558  N   ILE A  69      30.439 -36.419  17.942  1.00 14.89           N  
-ANISOU  558  N   ILE A  69     1567   2476   1612   -126   -296   -410       N  
-ATOM    559  CA  ILE A  69      31.349 -37.253  18.713  1.00 15.90           C  
-ANISOU  559  CA  ILE A  69     1727   2602   1712   -117   -261   -474       C  
-ATOM    560  C   ILE A  69      30.558 -37.973  19.790  1.00 21.50           C  
-ANISOU  560  C   ILE A  69     2432   3321   2418   -109   -264   -522       C  
-ATOM    561  O   ILE A  69      30.034 -37.349  20.720  1.00 21.01           O  
-ANISOU  561  O   ILE A  69     2324   3236   2423    -84   -270   -538       O  
-ATOM    562  CB  ILE A  69      32.492 -36.413  19.323  1.00 16.71           C  
-ANISOU  562  CB  ILE A  69     1810   2663   1877    -86   -232   -495       C  
-ATOM    563  CG1 ILE A  69      33.206 -35.654  18.198  1.00 19.76           C  
-ANISOU  563  CG1 ILE A  69     2200   3040   2268    -95   -232   -442       C  
-ATOM    564  CG2 ILE A  69      33.432 -37.300  20.123  1.00 20.64           C  
-ANISOU  564  CG2 ILE A  69     2341   3159   2343    -76   -196   -562       C  
-ATOM    565  CD1 ILE A  69      34.332 -34.779  18.649  1.00 24.56           C  
-ANISOU  565  CD1 ILE A  69     2788   3608   2936    -68   -206   -456       C  
-ATOM    566  N   LEU A  70      30.444 -39.289  19.641  1.00 20.37           N  
-ANISOU  566  N   LEU A  70     2333   3211   2195   -131   -260   -545       N  
-ATOM    567  CA  LEU A  70      29.596 -40.076  20.519  1.00 23.96           C  
-ANISOU  567  CA  LEU A  70     2787   3680   2637   -129   -265   -586       C  
-ATOM    568  C   LEU A  70      30.206 -40.202  21.906  1.00 30.96           C  
-ANISOU  568  C   LEU A  70     3665   4542   3555    -98   -234   -653       C  
-ATOM    569  O   LEU A  70      31.381 -40.549  22.052  1.00 33.58           O  
-ANISOU  569  O   LEU A  70     4027   4867   3866    -93   -203   -684       O  
-ATOM    570  CB  LEU A  70      29.350 -41.464  19.925  1.00 25.15           C  
-ANISOU  570  CB  LEU A  70     2991   3874   2692   -162   -269   -591       C  
-ATOM    571  CG  LEU A  70      28.742 -41.467  18.522  1.00 22.89           C  
-ANISOU  571  CG  LEU A  70     2716   3615   2364   -195   -299   -527       C  
-ATOM    572  CD1 LEU A  70      28.592 -42.887  17.996  1.00 31.22           C  
-ANISOU  572  CD1 LEU A  70     3826   4711   3323   -227   -300   -538       C  
-ATOM    573  CD2 LEU A  70      27.395 -40.752  18.544  1.00 29.44           C  
-ANISOU  573  CD2 LEU A  70     3499   4445   3243   -193   -335   -492       C  
-ATOM    574  N   LYS A  71      29.411 -39.913  22.930  1.00 37.86           N  
-ANISOU  574  N   LYS A  71     4499   5404   4482    -77   -244   -675       N  
-ATOM    575  CA  LYS A  71      29.855 -40.160  24.294  1.00 38.35           C  
-ANISOU  575  CA  LYS A  71     4555   5448   4569    -48   -216   -742       C  
-ATOM    576  C   LYS A  71      29.957 -41.665  24.456  1.00 43.80           C  
-ANISOU  576  C   LYS A  71     5296   6168   5178    -65   -202   -783       C  
-ATOM    577  O   LYS A  71      29.251 -42.411  23.770  1.00 43.64           O  
-ANISOU  577  O   LYS A  71     5301   6181   5099    -95   -221   -762       O  
-ATOM    578  CB  LYS A  71      28.876 -39.583  25.320  1.00 35.82           C  
-ANISOU  578  CB  LYS A  71     4181   5111   4318    -24   -232   -755       C  
-ATOM    579  CG  LYS A  71      28.901 -38.067  25.439  1.00 37.30           C  
-ANISOU  579  CG  LYS A  71     4315   5262   4596      0   -240   -727       C  
-ATOM    580  CD  LYS A  71      28.454 -37.637  26.827  1.00 44.12           C  
-ANISOU  580  CD  LYS A  71     5132   6102   5528     34   -238   -767       C  
-ATOM    581  CE  LYS A  71      28.532 -36.129  27.001  1.00 47.17           C  
-ANISOU  581  CE  LYS A  71     5466   6451   6007     60   -245   -742       C  
-ATOM    582  NZ  LYS A  71      27.389 -35.452  26.344  1.00 49.58           N  
-ANISOU  582  NZ  LYS A  71     5740   6763   6337     48   -283   -684       N  
-ATOM    583  N   PRO A  72      30.854 -42.122  25.342  1.00 59.77           N  
-ANISOU  583  N   PRO A  72     7350   8035   7326    133   -514     86       N  
-ATOM    584  CA  PRO A  72      31.000 -43.556  25.608  1.00 66.40           C  
-ANISOU  584  CA  PRO A  72     8186   8830   8212    140   -541    130       C  
-ATOM    585  C   PRO A  72      29.719 -44.126  26.201  1.00 74.42           C  
-ANISOU  585  C   PRO A  72     9234   9848   9195    119   -528    172       C  
-ATOM    586  O   PRO A  72      29.688 -45.283  26.621  1.00 77.36           O  
-ANISOU  586  O   PRO A  72     9611  10188   9593    120   -551    217       O  
-ATOM    587  CB  PRO A  72      32.137 -43.608  26.634  1.00 63.60           C  
-ANISOU  587  CB  PRO A  72     7829   8481   7855    151   -594    160       C  
-ATOM    588  CG  PRO A  72      32.902 -42.343  26.418  1.00 62.79           C  
-ANISOU  588  CG  PRO A  72     7713   8412   7734    157   -592    115       C  
-ATOM    589  CD  PRO A  72      31.867 -41.322  26.051  1.00 60.90           C  
-ANISOU  589  CD  PRO A  72     7490   8208   7443    139   -544     83       C  
-ATOM    590  N   VAL A  73      28.672 -43.308  26.235  1.00 80.09           N  
-ANISOU  590  N   VAL A  73     9972  10603   9857     99   -492    158       N  
-ATOM    591  CA  VAL A  73      27.368 -43.753  26.698  1.00 85.73           C  
-ANISOU  591  CA  VAL A  73    10714  11321  10538     77   -473    190       C  
-ATOM    592  C   VAL A  73      26.847 -44.868  25.792  1.00 85.27           C  
-ANISOU  592  C   VAL A  73    10646  11216  10537     80   -454    190       C  
-ATOM    593  O   VAL A  73      26.482 -44.634  24.636  1.00 81.60           O  
-ANISOU  593  O   VAL A  73    10167  10743  10094     82   -419    147       O  
-ATOM    594  CB  VAL A  73      26.351 -42.588  26.752  1.00 87.64           C  
-ANISOU  594  CB  VAL A  73    10974  11609  10716     58   -433    165       C  
-ATOM    595  CG1 VAL A  73      25.018 -43.066  27.310  1.00 88.21           C  
-ANISOU  595  CG1 VAL A  73    11074  11687  10754     33   -414    198       C  
-ATOM    596  CG2 VAL A  73      26.900 -41.440  27.590  1.00 86.39           C  
-ANISOU  596  CG2 VAL A  73    10823  11497  10503     55   -450    160       C  
-ATOM    597  N   LYS A  74      26.846 -46.084  26.328  1.00 85.27           N  
-ANISOU  597  N   LYS A  74    10654  11185  10561     80   -478    239       N  
-ATOM    598  CA  LYS A  74      26.312 -47.260  25.640  1.00 80.27           C  
-ANISOU  598  CA  LYS A  74    10015  10505   9979     81   -463    247       C  
-ATOM    599  C   LYS A  74      27.237 -47.829  24.560  1.00 74.78           C  
-ANISOU  599  C   LYS A  74     9283   9764   9365    105   -471    219       C  
-ATOM    600  O   LYS A  74      28.262 -47.236  24.224  1.00 69.76           O  
-ANISOU  600  O   LYS A  74     8625   9134   8746    121   -484    188       O  
-ATOM    601  CB  LYS A  74      24.892 -47.010  25.124  1.00 78.26           C  
-ANISOU  601  CB  LYS A  74     9773  10265   9698     61   -413    227       C  
-ATOM    602  CG  LYS A  74      23.899 -46.635  26.227  1.00 75.70           C  
-ANISOU  602  CG  LYS A  74     9484   9980   9299     35   -403    256       C  
-ATOM    603  CD  LYS A  74      23.861 -47.672  27.352  1.00 78.20           C  
-ANISOU  603  CD  LYS A  74     9822  10280   9609     25   -435    321       C  
-ATOM    604  CE  LYS A  74      24.887 -47.391  28.456  1.00 81.00           C  
-ANISOU  604  CE  LYS A  74    10184  10652   9939     31   -482    350       C  
-ATOM    605  NZ  LYS A  74      24.695 -46.065  29.108  1.00 80.63           N  
-ANISOU  605  NZ  LYS A  74    10153  10664   9820     16   -473    336       N  
-ATOM    606  N   LYS A  75      26.861 -48.990  24.032  1.00 72.99           N  
-ANISOU  606  N   LYS A  75     9051   9494   9188    106   -462    231       N  
-ATOM    607  CA  LYS A  75      27.791 -49.848  23.306  1.00 70.54           C  
-ANISOU  607  CA  LYS A  75     8708   9132   8960    128   -479    220       C  
-ATOM    608  C   LYS A  75      27.358 -50.162  21.875  1.00 62.81           C  
-ANISOU  608  C   LYS A  75     7711   8127   8028    129   -438    177       C  
-ATOM    609  O   LYS A  75      27.637 -49.396  20.953  1.00 63.31           O  
-ANISOU  609  O   LYS A  75     7755   8201   8099    133   -416    125       O  
-ATOM    610  CB  LYS A  75      27.980 -51.147  24.090  1.00 78.55           C  
-ANISOU  610  CB  LYS A  75     9732  10110  10004    132   -516    280       C  
-ATOM    611  CG  LYS A  75      26.970 -51.333  25.220  1.00 82.31           C  
-ANISOU  611  CG  LYS A  75    10248  10606  10418    108   -517    331       C  
-ATOM    612  CD  LYS A  75      27.632 -51.236  26.591  1.00 84.14           C  
-ANISOU  612  CD  LYS A  75    10497  10855  10617    109   -567    377       C  
-ATOM    613  CE  LYS A  75      28.239 -49.860  26.835  1.00 85.27           C  
-ANISOU  613  CE  LYS A  75    10636  11046  10717    113   -573    349       C  
-ATOM    614  NZ  LYS A  75      27.428 -49.015  27.763  1.00 83.83           N  
-ANISOU  614  NZ  LYS A  75    10488  10918  10447     87   -561    363       N  
-ATOM    615  N   LYS A  76      26.689 -51.299  21.695  1.00 55.57           N  
-ANISOU  615  N   LYS A  76     6799   7174   7141    122   -428    201       N  
-ATOM    616  CA  LYS A  76      26.199 -51.711  20.378  1.00 48.97           C  
-ANISOU  616  CA  LYS A  76     5946   6311   6348    120   -389    164       C  
-ATOM    617  C   LYS A  76      25.136 -50.752  19.843  1.00 37.27           C  
-ANISOU  617  C   LYS A  76     4477   4868   4818    101   -343    129       C  
-ATOM    618  O   LYS A  76      24.669 -50.886  18.709  1.00 35.16           O  
-ANISOU  618  O   LYS A  76     4198   4586   4577     96   -309     94       O  
-ATOM    619  CB  LYS A  76      25.621 -53.126  20.432  1.00 50.58           C  
-ANISOU  619  CB  LYS A  76     6158   6472   6589    114   -388    201       C  
-ATOM    620  CG  LYS A  76      24.477 -53.287  21.420  1.00 52.97           C  
-ANISOU  620  CG  LYS A  76     6498   6795   6834     92   -382    247       C  
-ATOM    621  CD  LYS A  76      23.565 -54.439  21.020  1.00 58.69           C  
-ANISOU  621  CD  LYS A  76     7227   7483   7589     80   -359    262       C  
-ATOM    622  CE  LYS A  76      22.619 -54.808  22.149  1.00 62.81           C  
-ANISOU  622  CE  LYS A  76     7786   8017   8060     59   -363    315       C  
-ATOM    623  NZ  LYS A  76      23.363 -55.336  23.330  1.00 64.57           N  
-ANISOU  623  NZ  LYS A  76     8021   8227   8284     66   -414    370       N  
-ATOM    624  N   LYS A  77      24.733 -49.800  20.673  1.00 33.14           N  
-ANISOU  624  N   LYS A  77     3977   4393   4223     90   -344    140       N  
-ATOM    625  CA  LYS A  77      23.899 -48.711  20.196  1.00 35.10           C  
-ANISOU  625  CA  LYS A  77     4232   4679   4425     76   -306    103       C  
-ATOM    626  C   LYS A  77      24.641 -47.953  19.092  1.00 28.18           C  
-ANISOU  626  C   LYS A  77     3330   3804   3573     88   -296     45       C  
-ATOM    627  O   LYS A  77      24.024 -47.397  18.181  1.00 23.31           O  
-ANISOU  627  O   LYS A  77     2710   3198   2947     79   -260      5       O  
-ATOM    628  CB  LYS A  77      23.535 -47.763  21.341  1.00 43.08           C  
-ANISOU  628  CB  LYS A  77     5269   5741   5359     64   -312    122       C  
-ATOM    629  CG  LYS A  77      23.018 -46.413  20.860  1.00 52.46           C  
-ANISOU  629  CG  LYS A  77     6460   6969   6503     56   -281     77       C  
-ATOM    630  CD  LYS A  77      22.330 -45.622  21.958  1.00 51.14           C  
-ANISOU  630  CD  LYS A  77     6320   6849   6260     39   -278     96       C  
-ATOM    631  CE  LYS A  77      21.900 -44.270  21.421  1.00 55.61           C  
-ANISOU  631  CE  LYS A  77     6886   7453   6791     34   -249     49       C  
-ATOM    632  NZ  LYS A  77      21.019 -43.540  22.368  1.00 60.18           N  
-ANISOU  632  NZ  LYS A  77     7490   8075   7300     15   -238     63       N  
-ATOM    633  N   ILE A  78      25.971 -47.935  19.174  1.00 21.48           N  
-ANISOU  633  N   ILE A  78     2462   2945   2755    107   -327     39       N  
-ATOM    634  CA  ILE A  78      26.763 -47.212  18.190  1.00 18.93           C  
-ANISOU  634  CA  ILE A  78     2115   2624   2455    117   -318    -16       C  
-ATOM    635  C   ILE A  78      26.637 -47.851  16.817  1.00 20.90           C  
-ANISOU  635  C   ILE A  78     2344   2835   2763    116   -291    -49       C  
-ATOM    636  O   ILE A  78      26.399 -47.163  15.826  1.00 19.77           O  
-ANISOU  636  O   ILE A  78     2195   2703   2614    109   -261    -96       O  
-ATOM    637  CB  ILE A  78      28.245 -47.140  18.591  1.00 25.23           C  
-ANISOU  637  CB  ILE A  78     2895   3416   3277    137   -358    -14       C  
-ATOM    638  CG1 ILE A  78      28.405 -46.317  19.867  1.00 31.47           C  
-ANISOU  638  CG1 ILE A  78     3705   4250   4004    135   -382     12       C  
-ATOM    639  CG2 ILE A  78      29.061 -46.532  17.467  1.00 31.51           C  
-ANISOU  639  CG2 ILE A  78     3663   4207   4103    145   -345    -74       C  
-ATOM    640  CD1 ILE A  78      29.842 -46.246  20.373  1.00 36.61           C  
-ANISOU  640  CD1 ILE A  78     4338   4896   4675    155   -425     17       C  
-ATOM    641  N   LYS A  79      26.811 -49.168  16.753  1.00 21.64           N  
-ANISOU  641  N   LYS A  79     2427   2883   2913    123   -302    -26       N  
-ATOM    642  CA  LYS A  79      26.642 -49.882  15.495  1.00 22.44           C  
-ANISOU  642  CA  LYS A  79     2509   2945   3071    121   -275    -56       C  
-ATOM    643  C   LYS A  79      25.212 -49.773  14.965  1.00 16.37           C  
-ANISOU  643  C   LYS A  79     1757   2189   2274     99   -234    -65       C  
-ATOM    644  O   LYS A  79      25.000 -49.703  13.758  1.00 17.17           O  
-ANISOU  644  O   LYS A  79     1847   2280   2398     92   -204   -108       O  
-ATOM    645  CB  LYS A  79      27.017 -51.352  15.654  1.00 21.41           C  
-ANISOU  645  CB  LYS A  79     2367   2764   3006    131   -296    -25       C  
-ATOM    646  CG  LYS A  79      28.496 -51.580  15.905  1.00 27.16           C  
-ANISOU  646  CG  LYS A  79     3070   3470   3779    154   -334    -24       C  
-ATOM    647  CD  LYS A  79      28.923 -52.933  15.393  1.00 33.52           C  
-ANISOU  647  CD  LYS A  79     3851   4216   4668    164   -340    -22       C  
-ATOM    648  CE  LYS A  79      30.415 -53.148  15.565  1.00 38.03           C  
-ANISOU  648  CE  LYS A  79     4394   4765   5291    188   -378    -26       C  
-ATOM    649  NZ  LYS A  79      30.792 -54.506  15.089  1.00 37.33           N  
-ANISOU  649  NZ  LYS A  79     4281   4616   5287    199   -383    -23       N  
-ATOM    650  N   ARG A  80      24.229 -49.789  15.859  1.00 17.21           N  
-ANISOU  650  N   ARG A  80     1891   2316   2331     87   -233    -26       N  
-ATOM    651  CA  ARG A  80      22.837 -49.686  15.435  1.00 20.64           C  
-ANISOU  651  CA  ARG A  80     2340   2763   2737     67   -196    -34       C  
-ATOM    652  C   ARG A  80      22.621 -48.387  14.681  1.00 19.09           C  
-ANISOU  652  C   ARG A  80     2143   2600   2509     61   -171    -84       C  
-ATOM    653  O   ARG A  80      22.065 -48.391  13.586  1.00 13.78           O  
-ANISOU  653  O   ARG A  80     1464   1920   1851     51   -140   -116       O  
-ATOM    654  CB  ARG A  80      21.897 -49.749  16.638  1.00 17.29           C  
-ANISOU  654  CB  ARG A  80     1947   2363   2261     55   -199     13       C  
-ATOM    655  CG  ARG A  80      20.432 -49.773  16.279  1.00 18.45           C  
-ANISOU  655  CG  ARG A  80     2108   2519   2384     34   -162      8       C  
-ATOM    656  CD  ARG A  80      19.594 -49.895  17.542  1.00 18.00           C  
-ANISOU  656  CD  ARG A  80     2080   2484   2277     21   -167     55       C  
-ATOM    657  NE  ARG A  80      19.612 -48.661  18.322  1.00 20.32           N  
-ANISOU  657  NE  ARG A  80     2387   2826   2507     18   -175     54       N  
-ATOM    658  CZ  ARG A  80      19.137 -48.553  19.562  1.00 27.70           C  
-ANISOU  658  CZ  ARG A  80     3347   3786   3392      7   -184     93       C  
-ATOM    659  NH1 ARG A  80      18.636 -49.614  20.177  1.00 28.92           N  
-ANISOU  659  NH1 ARG A  80     3516   3922   3552     -3   -188    136       N  
-ATOM    660  NH2 ARG A  80      19.174 -47.385  20.192  1.00 24.51           N  
-ANISOU  660  NH2 ARG A  80     2954   3427   2932      4   -188     87       N  
-ATOM    661  N   GLU A  81      23.067 -47.271  15.258  1.00 17.61           N  
-ANISOU  661  N   GLU A  81     1963   2451   2278     65   -185    -89       N  
-ATOM    662  CA  GLU A  81      22.856 -45.980  14.616  1.00 14.79           C  
-ANISOU  662  CA  GLU A  81     1607   2126   1887     59   -164   -133       C  
-ATOM    663  C   GLU A  81      23.611 -45.938  13.288  1.00 15.07           C  
-ANISOU  663  C   GLU A  81     1617   2138   1970     64   -153   -182       C  
-ATOM    664  O   GLU A  81      23.076 -45.504  12.277  1.00 12.64           O  
-ANISOU  664  O   GLU A  81     1309   1835   1659     53   -125   -219       O  
-ATOM    665  CB  GLU A  81      23.263 -44.819  15.530  1.00 13.15           C  
-ANISOU  665  CB  GLU A  81     1411   1962   1625     63   -182   -129       C  
-ATOM    666  CG  GLU A  81      23.170 -43.451  14.858  1.00 16.14           C  
-ANISOU  666  CG  GLU A  81     1790   2370   1972     58   -162   -176       C  
-ATOM    667  CD  GLU A  81      23.466 -42.292  15.800  1.00 15.49           C  
-ANISOU  667  CD  GLU A  81     1720   2331   1833     61   -178   -172       C  
-ATOM    668  OE1 GLU A  81      23.835 -42.538  16.966  1.00 17.69           O  
-ANISOU  668  OE1 GLU A  81     2006   2617   2098     66   -205   -133       O  
-ATOM    669  OE2 GLU A  81      23.326 -41.132  15.373  1.00 17.23           O  
-ANISOU  669  OE2 GLU A  81     1944   2579   2024     56   -163   -207       O  
-ATOM    670  N   ILE A  82      24.860 -46.399  13.293  1.00 14.70           N  
-ANISOU  670  N   ILE A  82     1550   2066   1969     80   -177   -184       N  
-ATOM    671  CA  ILE A  82      25.650 -46.429  12.065  1.00 16.94           C  
-ANISOU  671  CA  ILE A  82     1809   2327   2303     83   -167   -232       C  
-ATOM    672  C   ILE A  82      25.022 -47.246  10.945  1.00 14.45           C  
-ANISOU  672  C   ILE A  82     1484   1978   2027     72   -137   -249       C  
-ATOM    673  O   ILE A  82      24.960 -46.791   9.808  1.00 17.47           O  
-ANISOU  673  O   ILE A  82     1861   2362   2416     62   -113   -295       O  
-ATOM    674  CB  ILE A  82      27.076 -46.943  12.315  1.00 17.93           C  
-ANISOU  674  CB  ILE A  82     1910   2425   2477    103   -199   -228       C  
-ATOM    675  CG1 ILE A  82      27.860 -45.916  13.140  1.00 19.47           C  
-ANISOU  675  CG1 ILE A  82     2109   2656   2634    113   -224   -226       C  
-ATOM    676  CG2 ILE A  82      27.736 -47.211  10.986  1.00 18.58           C  
-ANISOU  676  CG2 ILE A  82     1965   2476   2617    103   -182   -277       C  
-ATOM    677  CD1 ILE A  82      29.275 -46.375  13.546  1.00 19.46           C  
-ANISOU  677  CD1 ILE A  82     2085   2632   2678    134   -261   -219       C  
-ATOM    678  N   LYS A  83      24.574 -48.461  11.257  1.00 16.91           N  
-ANISOU  678  N   LYS A  83     1798   2261   2367     72   -140   -214       N  
-ATOM    679  CA  LYS A  83      23.957 -49.340  10.267  1.00 15.88           C  
-ANISOU  679  CA  LYS A  83     1660   2098   2277     60   -112   -227       C  
-ATOM    680  C   LYS A  83      22.671 -48.732   9.705  1.00 15.01           C  
-ANISOU  680  C   LYS A  83     1566   2012   2123     40    -79   -245       C  
-ATOM    681  O   LYS A  83      22.418 -48.753   8.494  1.00 14.41           O  
-ANISOU  681  O   LYS A  83     1482   1926   2069     28    -53   -283       O  
-ATOM    682  CB  LYS A  83      23.666 -50.715  10.880  1.00 15.92           C  
-ANISOU  682  CB  LYS A  83     1667   2069   2312     63   -124   -180       C  
-ATOM    683  CG  LYS A  83      23.158 -51.746   9.891  1.00 20.59           C  
-ANISOU  683  CG  LYS A  83     2248   2623   2953     53    -97   -193       C  
-ATOM    684  CD  LYS A  83      24.091 -51.880   8.710  1.00 28.36           C  
-ANISOU  684  CD  LYS A  83     3203   3579   3993     56    -88   -242       C  
-ATOM    685  CE  LYS A  83      23.485 -52.752   7.630  1.00 29.59           C  
-ANISOU  685  CE  LYS A  83     3350   3703   4190     41    -56   -261       C  
-ATOM    686  NZ  LYS A  83      24.445 -52.981   6.521  1.00 31.14           N  
-ANISOU  686  NZ  LYS A  83     3517   3870   4445     42    -47   -309       N  
-ATOM    687  N   ILE A  84      21.862 -48.174  10.593  1.00 13.52           N  
-ANISOU  687  N   ILE A  84     1402   1859   1876     35    -82   -218       N  
-ATOM    688  CA  ILE A  84      20.628 -47.524  10.169  1.00 14.53           C  
-ANISOU  688  CA  ILE A  84     1545   2013   1963     17    -53   -233       C  
-ATOM    689  C   ILE A  84      20.924 -46.357   9.222  1.00 14.65           C  
-ANISOU  689  C   ILE A  84     1556   2048   1964     13    -41   -285       C  
-ATOM    690  O   ILE A  84      20.294 -46.227   8.174  1.00 17.01           O  
-ANISOU  690  O   ILE A  84     1854   2344   2267     -1    -15   -314       O  
-ATOM    691  CB  ILE A  84      19.787 -47.068  11.388  1.00 15.22           C  
-ANISOU  691  CB  ILE A  84     1657   2136   1990     13    -59   -197       C  
-ATOM    692  CG1 ILE A  84      19.137 -48.292  12.054  1.00 18.48           C  
-ANISOU  692  CG1 ILE A  84     2078   2528   2415      9    -61   -151       C  
-ATOM    693  CG2 ILE A  84      18.709 -46.077  10.968  1.00 16.82           C  
-ANISOU  693  CG2 ILE A  84     1872   2371   2146     -1    -34   -220       C  
-ATOM    694  CD1 ILE A  84      18.420 -47.998  13.358  1.00 20.30           C  
-ANISOU  694  CD1 ILE A  84     2333   2791   2590      4    -68   -112       C  
-ATOM    695  N   LEU A  85      21.880 -45.505   9.590  1.00 13.95           N  
-ANISOU  695  N   LEU A  85     1464   1978   1858     24    -60   -295       N  
-ATOM    696  CA  LEU A  85      22.262 -44.380   8.732  1.00 12.39           C  
-ANISOU  696  CA  LEU A  85     1263   1798   1646     20    -50   -343       C  
-ATOM    697  C   LEU A  85      22.742 -44.859   7.367  1.00 13.72           C  
-ANISOU  697  C   LEU A  85     1412   1933   1868     14    -34   -383       C  
-ATOM    698  O   LEU A  85      22.444 -44.247   6.344  1.00 15.24           O  
-ANISOU  698  O   LEU A  85     1607   2133   2051      0    -12   -421       O  
-ATOM    699  CB  LEU A  85      23.346 -43.523   9.403  1.00 11.31           C  
-ANISOU  699  CB  LEU A  85     1125   1684   1489     34    -74   -346       C  
-ATOM    700  CG  LEU A  85      22.857 -42.634  10.560  1.00 13.05           C  
-ANISOU  700  CG  LEU A  85     1368   1947   1645     35    -85   -321       C  
-ATOM    701  CD1 LEU A  85      24.032 -42.138  11.415  1.00 14.85           C  
-ANISOU  701  CD1 LEU A  85     1591   2190   1861     51   -114   -313       C  
-ATOM    702  CD2 LEU A  85      22.024 -41.465  10.033  1.00 13.00           C  
-ANISOU  702  CD2 LEU A  85     1374   1970   1593     22    -62   -349       C  
-ATOM    703  N   GLU A  86      23.509 -45.945   7.351  1.00 18.52           N  
-ANISOU  703  N   GLU A  86     2001   2504   2533     23    -44   -375       N  
-ATOM    704  CA  GLU A  86      23.985 -46.489   6.081  1.00 20.17           C  
-ANISOU  704  CA  GLU A  86     2189   2679   2797     16    -27   -413       C  
-ATOM    705  C   GLU A  86      22.861 -47.113   5.255  1.00 19.39           C  
-ANISOU  705  C   GLU A  86     2094   2564   2710     -3      2   -419       C  
-ATOM    706  O   GLU A  86      22.788 -46.897   4.047  1.00 16.08           O  
-ANISOU  706  O   GLU A  86     1670   2139   2302    -18     24   -461       O  
-ATOM    707  CB  GLU A  86      25.144 -47.460   6.291  1.00 16.99           C  
-ANISOU  707  CB  GLU A  86     1761   2239   2455     32    -47   -406       C  
-ATOM    708  CG  GLU A  86      26.458 -46.722   6.514  1.00 19.51           C  
-ANISOU  708  CG  GLU A  86     2068   2570   2773     46    -68   -426       C  
-ATOM    709  CD  GLU A  86      27.627 -47.636   6.802  1.00 28.89           C  
-ANISOU  709  CD  GLU A  86     3230   3723   4023     64    -91   -417       C  
-ATOM    710  OE1 GLU A  86      27.481 -48.876   6.684  1.00 29.59           O  
-ANISOU  710  OE1 GLU A  86     3309   3773   4161     66    -89   -401       O  
-ATOM    711  OE2 GLU A  86      28.694 -47.095   7.168  1.00 29.86           O  
-ANISOU  711  OE2 GLU A  86     3343   3856   4146     77   -112   -427       O  
-ATOM    712  N   ASN A  87      21.985 -47.874   5.905  1.00 19.41           N  
-ANISOU  712  N   ASN A  87     2106   2560   2709     -3      1   -377       N  
-ATOM    713  CA  ASN A  87      20.816 -48.424   5.213  1.00 20.98           C  
-ANISOU  713  CA  ASN A  87     2310   2748   2914    -21     29   -380       C  
-ATOM    714  C   ASN A  87      19.945 -47.357   4.556  1.00 19.21           C  
-ANISOU  714  C   ASN A  87     2100   2554   2643    -38     49   -408       C  
-ATOM    715  O   ASN A  87      19.450 -47.546   3.449  1.00 17.41           O  
-ANISOU  715  O   ASN A  87     1870   2315   2431    -55     73   -435       O  
-ATOM    716  CB  ASN A  87      19.955 -49.263   6.160  1.00 19.87           C  
-ANISOU  716  CB  ASN A  87     2181   2602   2768    -19     24   -330       C  
-ATOM    717  CG  ASN A  87      20.600 -50.577   6.524  1.00 21.93           C  
-ANISOU  717  CG  ASN A  87     2427   2821   3085     -7     10   -304       C  
-ATOM    718  OD1 ASN A  87      21.596 -50.980   5.920  1.00 21.18           O  
-ANISOU  718  OD1 ASN A  87     2310   2697   3040     -2      7   -328       O  
-ATOM    719  ND2 ASN A  87      20.030 -51.261   7.518  1.00 17.18           N  
-ANISOU  719  ND2 ASN A  87     1838   2216   2476     -4      0   -255       N  
-ATOM    720  N   LEU A  88      19.778 -46.228   5.233  1.00 15.95           N  
-ANISOU  720  N   LEU A  88     1703   2181   2176    -33     39   -401       N  
-ATOM    721  CA  LEU A  88      18.824 -45.208   4.808  1.00 12.77           C  
-ANISOU  721  CA  LEU A  88     1317   1809   1727    -47     54   -420       C  
-ATOM    722  C   LEU A  88      19.453 -44.119   3.939  1.00 15.70           C  
-ANISOU  722  C   LEU A  88     1686   2193   2087    -52     58   -466       C  
-ATOM    723  O   LEU A  88      18.756 -43.245   3.430  1.00 15.46           O  
-ANISOU  723  O   LEU A  88     1668   2184   2022    -64     70   -486       O  
-ATOM    724  CB  LEU A  88      18.159 -44.556   6.029  1.00 17.62           C  
-ANISOU  724  CB  LEU A  88     1949   2459   2286    -41     44   -387       C  
-ATOM    725  CG  LEU A  88      17.305 -45.438   6.947  1.00 18.61           C  
-ANISOU  725  CG  LEU A  88     2082   2580   2408    -41     43   -342       C  
-ATOM    726  CD1 LEU A  88      16.814 -44.645   8.155  1.00 19.32           C  
-ANISOU  726  CD1 LEU A  88     2191   2709   2441    -37     33   -316       C  
-ATOM    727  CD2 LEU A  88      16.123 -46.027   6.190  1.00 16.43           C  
-ANISOU  727  CD2 LEU A  88     1808   2292   2145    -58     69   -347       C  
-ATOM    728  N   ARG A  89      20.764 -44.185   3.750  1.00 14.49           N  
-ANISOU  728  N   ARG A  89     1518   2025   1964    -44     47   -484       N  
-ATOM    729  CA  ARG A  89      21.484 -43.102   3.091  1.00 17.92           C  
-ANISOU  729  CA  ARG A  89     1951   2473   2383    -48     48   -525       C  
-ATOM    730  C   ARG A  89      21.001 -42.898   1.665  1.00 20.43           C  
-ANISOU  730  C   ARG A  89     2273   2785   2706    -72     74   -565       C  
-ATOM    731  O   ARG A  89      20.855 -43.854   0.903  1.00 15.60           O  
-ANISOU  731  O   ARG A  89     1649   2142   2135    -83     89   -575       O  
-ATOM    732  CB  ARG A  89      22.997 -43.363   3.132  1.00 20.16           C  
-ANISOU  732  CB  ARG A  89     2215   2738   2707    -36     34   -539       C  
-ATOM    733  CG  ARG A  89      23.854 -42.207   2.630  1.00 24.12           C  
-ANISOU  733  CG  ARG A  89     2717   3257   3192    -39     33   -580       C  
-ATOM    734  CD  ARG A  89      25.283 -42.291   3.187  1.00 21.61           C  
-ANISOU  734  CD  ARG A  89     2381   2932   2898    -21     11   -581       C  
-ATOM    735  NE  ARG A  89      25.871 -43.608   2.952  1.00 17.86           N  
-ANISOU  735  NE  ARG A  89     1882   2415   2489    -16     10   -579       N  
-ATOM    736  CZ  ARG A  89      26.865 -44.131   3.664  1.00 29.70           C  
-ANISOU  736  CZ  ARG A  89     3364   3900   4022      4    -13   -564       C  
-ATOM    737  NH1 ARG A  89      27.404 -43.449   4.672  1.00 28.08           N  
-ANISOU  737  NH1 ARG A  89     3163   3721   3787     20    -38   -547       N  
-ATOM    738  NH2 ARG A  89      27.324 -45.343   3.365  1.00 27.34           N  
-ANISOU  738  NH2 ARG A  89     3041   3560   3786      7    -12   -565       N  
-ATOM    739  N   GLY A  90      20.750 -41.643   1.313  1.00 18.08           N  
-ANISOU  739  N   GLY A  90     1990   2515   2365    -80     77   -587       N  
-ATOM    740  CA  GLY A  90      20.262 -41.307  -0.013  1.00 15.39           C  
-ANISOU  740  CA  GLY A  90     1655   2172   2021   -104     97   -623       C  
-ATOM    741  C   GLY A  90      18.742 -41.294  -0.103  1.00 20.97           C  
-ANISOU  741  C   GLY A  90     2376   2890   2703   -114    108   -608       C  
-ATOM    742  O   GLY A  90      18.181 -40.884  -1.117  1.00 23.78           O  
-ANISOU  742  O   GLY A  90     2740   3248   3048   -133    122   -634       O  
-ATOM    743  N   GLY A  91      18.073 -41.754   0.950  1.00 18.29           N  
-ANISOU  743  N   GLY A  91     2039   2556   2355   -102    102   -567       N  
-ATOM    744  CA  GLY A  91      16.612 -41.768   0.975  1.00 15.75           C  
-ANISOU  744  CA  GLY A  91     1728   2245   2010   -111    113   -552       C  
-ATOM    745  C   GLY A  91      16.058 -40.359   1.088  1.00 16.34           C  
-ANISOU  745  C   GLY A  91     1821   2355   2032   -112    109   -561       C  
-ATOM    746  O   GLY A  91      16.758 -39.454   1.522  1.00 15.24           O  
-ANISOU  746  O   GLY A  91     1686   2235   1869   -102     95   -567       O  
-ATOM    747  N   PRO A  92      14.797 -40.152   0.677  1.00 13.63           N  
-ANISOU  747  N   PRO A  92     1487   2021   1671   -125    120   -563       N  
-ATOM    748  CA  PRO A  92      14.239 -38.790   0.685  1.00 10.85           C  
-ANISOU  748  CA  PRO A  92     1150   1701   1273   -126    116   -575       C  
-ATOM    749  C   PRO A  92      14.276 -38.131   2.061  1.00 12.49           C  
-ANISOU  749  C   PRO A  92     1364   1936   1445   -108    102   -550       C  
-ATOM    750  O   PRO A  92      13.742 -38.676   3.018  1.00 14.51           O  
-ANISOU  750  O   PRO A  92     1619   2196   1697   -101    101   -517       O  
-ATOM    751  CB  PRO A  92      12.789 -38.992   0.213  1.00 15.75           C  
-ANISOU  751  CB  PRO A  92     1774   2321   1889   -140    130   -573       C  
-ATOM    752  CG  PRO A  92      12.524 -40.431   0.318  1.00 22.20           C  
-ANISOU  752  CG  PRO A  92     2580   3113   2742   -142    140   -552       C  
-ATOM    753  CD  PRO A  92      13.825 -41.155   0.223  1.00 18.05           C  
-ANISOU  753  CD  PRO A  92     2041   2562   2254   -137    136   -556       C  
-ATOM    754  N   ASN A  93      14.931 -36.974   2.156  1.00 15.60           N  
-ANISOU  754  N   ASN A  93     1766   2349   1813   -102     91   -567       N  
-ATOM    755  CA  ASN A  93      14.928 -36.189   3.391  1.00 16.13           C  
-ANISOU  755  CA  ASN A  93     1841   2447   1842    -88     79   -548       C  
-ATOM    756  C   ASN A  93      15.581 -36.863   4.605  1.00 17.10           C  
-ANISOU  756  C   ASN A  93     1957   2568   1973    -72     67   -515       C  
-ATOM    757  O   ASN A  93      15.361 -36.460   5.735  1.00 15.52           O  
-ANISOU  757  O   ASN A  93     1763   2391   1742    -63     59   -493       O  
-ATOM    758  CB  ASN A  93      13.493 -35.719   3.694  1.00 16.21           C  
-ANISOU  758  CB  ASN A  93     1860   2477   1822    -91     85   -539       C  
-ATOM    759  CG  ASN A  93      12.975 -34.770   2.630  1.00 19.04           C  
-ANISOU  759  CG  ASN A  93     2228   2842   2166   -103     90   -571       C  
-ATOM    760  OD1 ASN A  93      13.764 -34.182   1.890  1.00 15.66           O  
-ANISOU  760  OD1 ASN A  93     1802   2409   1737   -108     86   -599       O  
-ATOM    761  ND2 ASN A  93      11.648 -34.609   2.550  1.00 15.29           N  
-ANISOU  761  ND2 ASN A  93     1756   2375   1678   -110     98   -568       N  
-ATOM    762  N   ILE A  94      16.389 -37.889   4.370  1.00 14.72           N  
-ANISOU  762  N   ILE A  94     1642   2238   1713    -70     65   -513       N  
-ATOM    763  CA  ILE A  94      17.151 -38.512   5.458  1.00 11.60           C  
-ANISOU  763  CA  ILE A  94     1239   1838   1329    -55     50   -482       C  
-ATOM    764  C   ILE A  94      18.513 -37.817   5.534  1.00 11.64           C  
-ANISOU  764  C   ILE A  94     1241   1851   1331    -46     35   -501       C  
-ATOM    765  O   ILE A  94      19.142 -37.618   4.517  1.00 11.72           O  
-ANISOU  765  O   ILE A  94     1246   1848   1360    -52     40   -535       O  
-ATOM    766  CB  ILE A  94      17.398 -40.017   5.164  1.00 17.52           C  
-ANISOU  766  CB  ILE A  94     1974   2550   2132    -56     54   -470       C  
-ATOM    767  CG1 ILE A  94      16.071 -40.746   4.877  1.00 15.03           C  
-ANISOU  767  CG1 ILE A  94     1661   2225   1824    -68     72   -458       C  
-ATOM    768  CG2 ILE A  94      18.211 -40.673   6.287  1.00 18.80           C  
-ANISOU  768  CG2 ILE A  94     2130   2706   2309    -39     34   -437       C  
-ATOM    769  CD1 ILE A  94      15.070 -40.683   6.012  1.00 15.09           C  
-ANISOU  769  CD1 ILE A  94     1681   2256   1798    -65     71   -424       C  
-ATOM    770  N   ILE A  95      18.963 -37.449   6.729  1.00 11.55           N  
-ANISOU  770  N   ILE A  95     1234   1860   1296    -32     17   -479       N  
-ATOM    771  CA  ILE A  95      20.273 -36.826   6.849  1.00 11.13           C  
-ANISOU  771  CA  ILE A  95     1176   1814   1240    -23      2   -496       C  
-ATOM    772  C   ILE A  95      21.332 -37.781   6.289  1.00 12.75           C  
-ANISOU  772  C   ILE A  95     1361   1984   1500    -20     -1   -506       C  
-ATOM    773  O   ILE A  95      21.238 -39.009   6.461  1.00 12.96           O  
-ANISOU  773  O   ILE A  95     1378   1985   1561    -17     -2   -482       O  
-ATOM    774  CB  ILE A  95      20.597 -36.440   8.316  1.00 11.01           C  
-ANISOU  774  CB  ILE A  95     1166   1824   1192     -8    -18   -466       C  
-ATOM    775  CG1 ILE A  95      21.732 -35.409   8.345  1.00 12.93           C  
-ANISOU  775  CG1 ILE A  95     1408   2083   1420     -2    -29   -491       C  
-ATOM    776  CG2 ILE A  95      20.946 -37.676   9.154  1.00 12.19           C  
-ANISOU  776  CG2 ILE A  95     1306   1955   1369      2    -32   -427       C  
-ATOM    777  CD1 ILE A  95      21.335 -34.035   7.849  1.00 14.05           C  
-ANISOU  777  CD1 ILE A  95     1564   2249   1524    -11    -19   -522       C  
-ATOM    778  N   THR A  96      22.320 -37.220   5.597  1.00 15.31           N  
-ANISOU  778  N   THR A  96     1679   2304   1832    -22     -2   -543       N  
-ATOM    779  CA  THR A  96      23.376 -38.007   4.991  1.00 11.90           C  
-ANISOU  779  CA  THR A  96     1227   1841   1454    -21     -3   -560       C  
-ATOM    780  C   THR A  96      24.583 -38.136   5.907  1.00 14.24           C  
-ANISOU  780  C   THR A  96     1511   2138   1761     -2    -27   -546       C  
-ATOM    781  O   THR A  96      25.209 -37.147   6.294  1.00 18.06           O  
-ANISOU  781  O   THR A  96     1999   2646   2216      4    -39   -557       O  
-ATOM    782  CB  THR A  96      23.843 -37.402   3.650  1.00 16.26           C  
-ANISOU  782  CB  THR A  96     1777   2387   2013    -36     12   -612       C  
-ATOM    783  OG1 THR A  96      22.788 -37.499   2.694  1.00 18.45           O  
-ANISOU  783  OG1 THR A  96     2064   2658   2290    -55     33   -624       O  
-ATOM    784  CG2 THR A  96      25.057 -38.150   3.111  1.00 21.88           C  
-ANISOU  784  CG2 THR A  96     2466   3068   2780    -35     11   -633       C  
-ATOM    785  N   LEU A  97      24.894 -39.373   6.244  1.00 14.79           N  
-ANISOU  785  N   LEU A  97     1565   2180   1873      7    -36   -522       N  
-ATOM    786  CA  LEU A  97      26.129 -39.680   6.941  1.00 16.95           C  
-ANISOU  786  CA  LEU A  97     1823   2446   2171     25    -61   -512       C  
-ATOM    787  C   LEU A  97      27.234 -39.676   5.910  1.00 15.10           C  
-ANISOU  787  C   LEU A  97     1569   2192   1977     21    -55   -558       C  
-ATOM    788  O   LEU A  97      27.267 -40.522   5.022  1.00 16.78           O  
-ANISOU  788  O   LEU A  97     1768   2372   2236     13    -41   -574       O  
-ATOM    789  CB  LEU A  97      26.042 -41.055   7.595  1.00 19.71           C  
-ANISOU  789  CB  LEU A  97     2164   2770   2557     36    -74   -470       C  
-ATOM    790  CG  LEU A  97      27.300 -41.519   8.340  1.00 15.61           C  
-ANISOU  790  CG  LEU A  97     1626   2238   2068     55   -103   -455       C  
-ATOM    791  CD1 LEU A  97      27.589 -40.640   9.545  1.00 14.71           C  
-ANISOU  791  CD1 LEU A  97     1523   2160   1904     66   -127   -434       C  
-ATOM    792  CD2 LEU A  97      27.125 -42.960   8.777  1.00 16.73           C  
-ANISOU  792  CD2 LEU A  97     1760   2347   2251     63   -113   -416       C  
-ATOM    793  N   ALA A  98      28.141 -38.717   6.022  1.00 13.74           N  
-ANISOU  793  N   ALA A  98     1395   2038   1786     25    -65   -581       N  
-ATOM    794  CA  ALA A  98      29.205 -38.567   5.038  1.00 17.45           C  
-ANISOU  794  CA  ALA A  98     1848   2493   2289     19    -57   -630       C  
-ATOM    795  C   ALA A  98      30.426 -39.427   5.344  1.00 16.81           C  
-ANISOU  795  C   ALA A  98     1739   2386   2264     35    -76   -627       C  
-ATOM    796  O   ALA A  98      31.154 -39.845   4.436  1.00 17.32           O  
-ANISOU  796  O   ALA A  98     1781   2422   2375     29    -65   -663       O  
-ATOM    797  CB  ALA A  98      29.607 -37.117   4.930  1.00 19.68           C  
-ANISOU  797  CB  ALA A  98     2142   2808   2528     13    -56   -659       C  
-ATOM    798  N   ASP A  99      30.661 -39.699   6.621  1.00 14.01           N  
-ANISOU  798  N   ASP A  99     1381   2038   1904     55   -104   -585       N  
-ATOM    799  CA  ASP A  99      31.871 -40.404   7.001  1.00 16.23           C  
-ANISOU  799  CA  ASP A  99     1635   2296   2235     72   -128   -581       C  
-ATOM    800  C   ASP A  99      31.774 -40.806   8.464  1.00 18.17           C  
-ANISOU  800  C   ASP A  99     1886   2550   2469     91   -159   -524       C  
-ATOM    801  O   ASP A  99      30.901 -40.337   9.193  1.00 15.16           O  
-ANISOU  801  O   ASP A  99     1529   2197   2033     89   -162   -494       O  
-ATOM    802  CB  ASP A  99      33.071 -39.476   6.802  1.00 18.00           C  
-ANISOU  802  CB  ASP A  99     1848   2534   2456     74   -133   -622       C  
-ATOM    803  CG  ASP A  99      34.365 -40.223   6.489  1.00 17.41           C  
-ANISOU  803  CG  ASP A  99     1738   2426   2450     83   -143   -644       C  
-ATOM    804  OD1 ASP A  99      34.409 -41.468   6.574  1.00 18.50           O  
-ANISOU  804  OD1 ASP A  99     1860   2530   2641     93   -151   -624       O  
-ATOM    805  OD2 ASP A  99      35.345 -39.540   6.140  1.00 19.56           O  
-ANISOU  805  OD2 ASP A  99     1999   2706   2726     81   -143   -685       O  
-ATOM    806  N   ILE A 100      32.673 -41.688   8.887  1.00 17.05           N  
-ANISOU  806  N   ILE A 100     1720   2381   2377    108   -184   -510       N  
-ATOM    807  CA  ILE A 100      32.795 -42.056  10.288  1.00 13.66           C  
-ANISOU  807  CA  ILE A 100     1294   1958   1938    126   -219   -457       C  
-ATOM    808  C   ILE A 100      34.291 -42.111  10.553  1.00 14.50           C  
-ANISOU  808  C   ILE A 100     1373   2054   2082    143   -247   -470       C  
-ATOM    809  O   ILE A 100      35.022 -42.741   9.793  1.00 18.43           O  
-ANISOU  809  O   ILE A 100     1843   2518   2642    146   -242   -499       O  
-ATOM    810  CB  ILE A 100      32.230 -43.455  10.560  1.00 17.79           C  
-ANISOU  810  CB  ILE A 100     1815   2447   2496    131   -225   -415       C  
-ATOM    811  CG1 ILE A 100      30.811 -43.592  10.009  1.00 21.92           C  
-ANISOU  811  CG1 ILE A 100     2358   2970   2998    112   -192   -412       C  
-ATOM    812  CG2 ILE A 100      32.272 -43.743  12.057  1.00 18.94           C  
-ANISOU  812  CG2 ILE A 100     1971   2603   2623    146   -261   -358       C  
-ATOM    813  CD1 ILE A 100      30.397 -45.041   9.730  1.00 22.93           C  
-ANISOU  813  CD1 ILE A 100     2477   3055   3180    112   -186   -392       C  
-ATOM    814  N   VAL A 101      34.743 -41.435  11.601  1.00 12.67           N  
-ANISOU  814  N   VAL A 101     1148   1853   1812    154   -274   -451       N  
-ATOM    815  CA  VAL A 101      36.164 -41.418  11.940  1.00 12.95           C  
-ANISOU  815  CA  VAL A 101     1158   1883   1880    170   -303   -462       C  
-ATOM    816  C   VAL A 101      36.305 -41.701  13.429  1.00 19.18           C  
-ANISOU  816  C   VAL A 101     1954   2682   2652    186   -345   -405       C  
-ATOM    817  O   VAL A 101      35.346 -41.553  14.190  1.00 19.93           O  
-ANISOU  817  O   VAL A 101     2078   2800   2695    181   -346   -366       O  
-ATOM    818  CB  VAL A 101      36.833 -40.062  11.632  1.00 17.75           C  
-ANISOU  818  CB  VAL A 101     1765   2523   2457    164   -295   -509       C  
-ATOM    819  CG1 VAL A 101      36.673 -39.683  10.143  1.00 17.91           C  
-ANISOU  819  CG1 VAL A 101     1783   2536   2487    145   -254   -566       C  
-ATOM    820  CG2 VAL A 101      36.281 -38.968  12.545  1.00 18.27           C  
-ANISOU  820  CG2 VAL A 101     1861   2638   2442    160   -301   -486       C  
-ATOM    821  N   LYS A 102      37.501 -42.114  13.840  1.00 16.87           N  
-ANISOU  821  N   LYS A 102     1635   2373   2402    205   -378   -402       N  
-ATOM    822  CA  LYS A 102      37.788 -42.335  15.250  1.00 16.94           C  
-ANISOU  822  CA  LYS A 102     1650   2392   2395    220   -422   -349       C  
-ATOM    823  C   LYS A 102      38.310 -41.036  15.830  1.00 21.09           C  
-ANISOU  823  C   LYS A 102     2183   2964   2867    220   -434   -361       C  
-ATOM    824  O   LYS A 102      39.368 -40.550  15.421  1.00 22.12           O  
-ANISOU  824  O   LYS A 102     2290   3096   3018    225   -437   -404       O  
-ATOM    825  CB  LYS A 102      38.858 -43.425  15.418  1.00 19.34           C  
-ANISOU  825  CB  LYS A 102     1919   2654   2775    241   -457   -339       C  
-ATOM    826  CG  LYS A 102      38.492 -44.754  14.770  1.00 29.98           C  
-ANISOU  826  CG  LYS A 102     3254   3950   4186    242   -445   -333       C  
-ATOM    827  CD  LYS A 102      39.469 -45.859  15.165  1.00 44.03           C  
-ANISOU  827  CD  LYS A 102     5003   5688   6038    265   -485   -312       C  
-ATOM    828  CE  LYS A 102      39.078 -47.185  14.531  1.00 45.45           C  
-ANISOU  828  CE  LYS A 102     5171   5816   6281    266   -472   -306       C  
-ATOM    829  NZ  LYS A 102      39.629 -48.348  15.281  1.00 50.62           N  
-ANISOU  829  NZ  LYS A 102     5809   6433   6990    288   -517   -262       N  
-ATOM    830  N   ASP A 103      37.599 -40.469  16.791  1.00 15.74           N  
-ANISOU  830  N   ASP A 103     1638   1947   2394    -55   -449   -203       N  
-ATOM    831  CA  ASP A 103      38.127 -39.275  17.428  1.00 16.68           C  
-ANISOU  831  CA  ASP A 103     1733   2018   2587    -73   -484   -223       C  
-ATOM    832  C   ASP A 103      39.247 -39.661  18.407  1.00 19.33           C  
-ANISOU  832  C   ASP A 103     2059   2352   2932    -86   -522   -247       C  
-ATOM    833  O   ASP A 103      39.066 -40.527  19.260  1.00 19.43           O  
-ANISOU  833  O   ASP A 103     2103   2390   2888    -81   -538   -286       O  
-ATOM    834  CB  ASP A 103      37.035 -38.463  18.117  1.00 13.90           C  
-ANISOU  834  CB  ASP A 103     1406   1643   2234    -74   -499   -269       C  
-ATOM    835  CG  ASP A 103      37.561 -37.160  18.663  1.00 22.96           C  
-ANISOU  835  CG  ASP A 103     2529   2735   3459    -93   -532   -286       C  
-ATOM    836  OD1 ASP A 103      37.670 -36.192  17.884  1.00 23.60           O  
-ANISOU  836  OD1 ASP A 103     2582   2786   3598    -99   -519   -252       O  
-ATOM    837  OD2 ASP A 103      37.881 -37.098  19.867  1.00 24.50           O  
-ANISOU  837  OD2 ASP A 103     2735   2917   3657   -104   -572   -333       O  
-ATOM    838  N   PRO A 104      40.417 -39.021  18.279  1.00 21.38           N  
-ANISOU  838  N   PRO A 104     2275   2584   3264   -102   -538   -224       N  
-ATOM    839  CA  PRO A 104      41.566 -39.448  19.084  1.00 20.53           C  
-ANISOU  839  CA  PRO A 104     2154   2479   3166   -114   -571   -238       C  
-ATOM    840  C   PRO A 104      41.509 -38.921  20.523  1.00 20.26           C  
-ANISOU  840  C   PRO A 104     2137   2418   3145   -130   -620   -300       C  
-ATOM    841  O   PRO A 104      42.218 -39.426  21.399  1.00 23.15           O  
-ANISOU  841  O   PRO A 104     2502   2793   3500   -138   -650   -324       O  
-ATOM    842  CB  PRO A 104      42.746 -38.820  18.338  1.00 22.97           C  
-ANISOU  842  CB  PRO A 104     2409   2766   3551   -127   -569   -185       C  
-ATOM    843  CG  PRO A 104      42.186 -37.543  17.813  1.00 21.03           C  
-ANISOU  843  CG  PRO A 104     2152   2481   3356   -134   -560   -174       C  
-ATOM    844  CD  PRO A 104      40.742 -37.862  17.425  1.00 16.97           C  
-ANISOU  844  CD  PRO A 104     1677   1988   2781   -112   -527   -183       C  
-ATOM    845  N   VAL A 105      40.686 -37.905  20.756  1.00 14.93           N  
-ANISOU  845  N   VAL A 105     1474   1710   2490   -134   -627   -326       N  
-ATOM    846  CA  VAL A 105      40.521 -37.351  22.096  1.00 14.93           C  
-ANISOU  846  CA  VAL A 105     1493   1681   2499   -148   -671   -386       C  
-ATOM    847  C   VAL A 105      39.449 -38.097  22.887  1.00 19.26           C  
-ANISOU  847  C   VAL A 105     2093   2258   2968   -132   -673   -436       C  
-ATOM    848  O   VAL A 105      39.673 -38.473  24.034  1.00 21.24           O  
-ANISOU  848  O   VAL A 105     2360   2513   3196   -138   -707   -481       O  
-ATOM    849  CB  VAL A 105      40.196 -35.831  22.062  1.00 18.21           C  
-ANISOU  849  CB  VAL A 105     1899   2042   2978   -160   -681   -392       C  
-ATOM    850  CG1 VAL A 105      39.957 -35.311  23.474  1.00 18.50           C  
-ANISOU  850  CG1 VAL A 105     1963   2050   3017   -171   -725   -458       C  
-ATOM    851  CG2 VAL A 105      41.335 -35.052  21.407  1.00 18.80           C  
-ANISOU  851  CG2 VAL A 105     1924   2086   3135   -179   -684   -346       C  
-ATOM    852  N   SER A 106      38.283 -38.316  22.279  1.00 20.03           N  
-ANISOU  852  N   SER A 106     2214   2376   3022   -112   -638   -428       N  
-ATOM    853  CA  SER A 106      37.201 -38.978  22.995  1.00 20.51           C  
-ANISOU  853  CA  SER A 106     2322   2464   3007    -98   -639   -473       C  
-ATOM    854  C   SER A 106      37.412 -40.488  23.038  1.00 26.82           C  
-ANISOU  854  C   SER A 106     3137   3315   3739    -87   -630   -470       C  
-ATOM    855  O   SER A 106      36.862 -41.174  23.908  1.00 27.67           O  
-ANISOU  855  O   SER A 106     3280   3445   3786    -80   -643   -513       O  
-ATOM    856  CB  SER A 106      35.854 -38.684  22.337  1.00 15.10           C  
-ANISOU  856  CB  SER A 106     1655   1784   2297    -81   -606   -463       C  
-ATOM    857  OG  SER A 106      35.819 -39.254  21.046  1.00 15.77           O  
-ANISOU  857  OG  SER A 106     1729   1898   2365    -70   -563   -408       O  
-ATOM    858  N   ARG A 107      38.199 -40.999  22.089  1.00 20.61           N  
-ANISOU  858  N   ARG A 107     2323   2545   2962    -85   -607   -417       N  
-ATOM    859  CA  ARG A 107      38.417 -42.435  21.952  1.00 22.22           C  
-ANISOU  859  CA  ARG A 107     2543   2797   3102    -73   -593   -406       C  
-ATOM    860  C   ARG A 107      37.098 -43.122  21.613  1.00 27.32           C  
-ANISOU  860  C   ARG A 107     3229   3478   3672    -55   -562   -410       C  
-ATOM    861  O   ARG A 107      36.841 -44.248  22.036  1.00 31.57           O  
-ANISOU  861  O   ARG A 107     3799   4053   4141    -46   -563   -430       O  
-ATOM    862  CB  ARG A 107      39.023 -43.010  23.240  1.00 27.91           C  
-ANISOU  862  CB  ARG A 107     3274   3526   3803    -81   -632   -450       C  
-ATOM    863  CG  ARG A 107      40.292 -42.276  23.706  1.00 33.68           C  
-ANISOU  863  CG  ARG A 107     3967   4222   4609   -103   -668   -451       C  
-ATOM    864  CD  ARG A 107      40.730 -42.707  25.107  1.00 35.10           C  
-ANISOU  864  CD  ARG A 107     4161   4406   4769   -112   -710   -502       C  
-ATOM    865  NE  ARG A 107      41.056 -44.130  25.149  1.00 27.37           N  
-ANISOU  865  NE  ARG A 107     3196   3474   3730    -99   -701   -495       N  
-ATOM    866  CZ  ARG A 107      42.144 -44.646  24.603  1.00 29.03           C  
-ANISOU  866  CZ  ARG A 107     3377   3699   3954    -98   -691   -452       C  
-ATOM    867  NH1 ARG A 107      43.000 -43.850  23.983  1.00 30.32           N  
-ANISOU  867  NH1 ARG A 107     3493   3835   4190   -110   -690   -412       N  
-ATOM    868  NH2 ARG A 107      42.375 -45.948  24.673  1.00 28.45           N  
-ANISOU  868  NH2 ARG A 107     3320   3666   3822    -84   -681   -448       N  
-ATOM    869  N   THR A 108      36.265 -42.426  20.844  1.00 22.72           N  
-ANISOU  869  N   THR A 108     2646   2885   3104    -50   -537   -390       N  
-ATOM    870  CA  THR A 108      34.984 -42.957  20.399  1.00 19.54           C  
-ANISOU  870  CA  THR A 108     2276   2514   2633    -34   -506   -387       C  
-ATOM    871  C   THR A 108      34.765 -42.583  18.938  1.00 20.95           C  
-ANISOU  871  C   THR A 108     2435   2691   2835    -28   -465   -329       C  
-ATOM    872  O   THR A 108      35.482 -41.740  18.393  1.00 17.29           O  
-ANISOU  872  O   THR A 108     1932   2196   2443    -37   -463   -298       O  
-ATOM    873  CB  THR A 108      33.813 -42.387  21.226  1.00 21.06           C  
-ANISOU  873  CB  THR A 108     2498   2696   2810    -32   -522   -436       C  
-ATOM    874  OG1 THR A 108      33.752 -40.969  21.050  1.00 19.03           O  
-ANISOU  874  OG1 THR A 108     2217   2393   2623    -39   -526   -431       O  
-ATOM    875  CG2 THR A 108      33.996 -42.696  22.701  1.00 26.62           C  
-ANISOU  875  CG2 THR A 108     3222   3400   3491    -37   -564   -495       C  
-ATOM    876  N   PRO A 109      33.764 -43.197  18.300  1.00 21.75           N  
-ANISOU  876  N   PRO A 109     2562   2826   2876    -15   -432   -313       N  
-ATOM    877  CA  PRO A 109      33.491 -42.855  16.903  1.00 18.62           C  
-ANISOU  877  CA  PRO A 109     2148   2429   2497    -10   -393   -258       C  
-ATOM    878  C   PRO A 109      32.887 -41.470  16.793  1.00 16.15           C  
-ANISOU  878  C   PRO A 109     1821   2080   2236    -13   -393   -261       C  
-ATOM    879  O   PRO A 109      32.127 -41.038  17.676  1.00 20.30           O  
-ANISOU  879  O   PRO A 109     2367   2596   2751    -13   -413   -305       O  
-ATOM    880  CB  PRO A 109      32.468 -43.915  16.470  1.00 18.07           C  
-ANISOU  880  CB  PRO A 109     2118   2408   2341      3   -364   -250       C  
-ATOM    881  CG  PRO A 109      32.593 -45.009  17.486  1.00 23.41           C  
-ANISOU  881  CG  PRO A 109     2826   3111   2957      4   -386   -290       C  
-ATOM    882  CD  PRO A 109      32.919 -44.307  18.769  1.00 17.86           C  
-ANISOU  882  CD  PRO A 109     2116   2376   2293     -6   -430   -341       C  
-ATOM    883  N   ALA A 110      33.225 -40.789  15.705  1.00 14.15           N  
-ANISOU  883  N   ALA A 110     1533   1807   2037    -15   -370   -212       N  
-ATOM    884  CA  ALA A 110      32.703 -39.468  15.404  1.00 13.72           C  
-ANISOU  884  CA  ALA A 110     1462   1717   2034    -17   -365   -205       C  
-ATOM    885  C   ALA A 110      31.998 -39.555  14.059  1.00 18.00           C  
-ANISOU  885  C   ALA A 110     2002   2279   2557     -6   -319   -155       C  
-ATOM    886  O   ALA A 110      32.630 -39.800  13.039  1.00 14.93           O  
-ANISOU  886  O   ALA A 110     1591   1897   2184     -6   -295   -106       O  
-ATOM    887  CB  ALA A 110      33.820 -38.443  15.352  1.00 15.53           C  
-ANISOU  887  CB  ALA A 110     1648   1899   2354    -31   -382   -191       C  
-ATOM    888  N   LEU A 111      30.683 -39.369  14.063  1.00 16.18           N  
-ANISOU  888  N   LEU A 111     1797   2061   2291      3   -307   -167       N  
-ATOM    889  CA  LEU A 111      29.911 -39.402  12.827  1.00 17.34           C  
-ANISOU  889  CA  LEU A 111     1943   2228   2418     12   -264   -121       C  
-ATOM    890  C   LEU A 111      29.906 -38.036  12.157  1.00 18.10           C  
-ANISOU  890  C   LEU A 111     2005   2284   2589     10   -253    -93       C  
-ATOM    891  O   LEU A 111      29.638 -37.012  12.804  1.00 17.83           O  
-ANISOU  891  O   LEU A 111     1968   2214   2594      7   -273   -122       O  
-ATOM    892  CB  LEU A 111      28.462 -39.835  13.092  1.00 16.33           C  
-ANISOU  892  CB  LEU A 111     1855   2134   2215     22   -255   -142       C  
-ATOM    893  CG  LEU A 111      28.202 -41.069  13.959  1.00 17.60           C  
-ANISOU  893  CG  LEU A 111     2057   2334   2297     24   -270   -180       C  
-ATOM    894  CD1 LEU A 111      26.707 -41.375  13.972  1.00 14.61           C  
-ANISOU  894  CD1 LEU A 111     1713   1989   1850     33   -255   -189       C  
-ATOM    895  CD2 LEU A 111      28.984 -42.265  13.487  1.00 19.53           C  
-ANISOU  895  CD2 LEU A 111     2304   2606   2509     23   -259   -155       C  
-ATOM    896  N   VAL A 112      30.169 -38.024  10.853  1.00 13.13           N  
-ANISOU  896  N   VAL A 112     1352   1660   1978     11   -220    -35       N  
-ATOM    897  CA  VAL A 112      30.215 -36.786  10.081  1.00 15.18           C  
-ANISOU  897  CA  VAL A 112     1577   1883   2309      9   -205     -1       C  
-ATOM    898  C   VAL A 112      28.989 -36.714   9.183  1.00 15.06           C  
-ANISOU  898  C   VAL A 112     1571   1890   2260     20   -168     28       C  
-ATOM    899  O   VAL A 112      28.768 -37.600   8.355  1.00 16.67           O  
-ANISOU  899  O   VAL A 112     1785   2132   2415     25   -139     61       O  
-ATOM    900  CB  VAL A 112      31.479 -36.734   9.217  1.00 14.05           C  
-ANISOU  900  CB  VAL A 112     1394   1727   2218      2   -195     46       C  
-ATOM    901  CG1 VAL A 112      31.563 -35.402   8.457  1.00 18.45           C  
-ANISOU  901  CG1 VAL A 112     1914   2244   2852     -1   -182     80       C  
-ATOM    902  CG2 VAL A 112      32.707 -36.953  10.085  1.00 12.94           C  
-ANISOU  902  CG2 VAL A 112     1244   1572   2103     -9   -231     21       C  
-ATOM    903  N   PHE A 113      28.193 -35.667   9.358  1.00 12.23           N  
-ANISOU  903  N   PHE A 113     1213   1508   1927     24   -169     16       N  
-ATOM    904  CA  PHE A 113      26.921 -35.514   8.624  1.00 13.54           C  
-ANISOU  904  CA  PHE A 113     1388   1695   2060     35   -137     40       C  
-ATOM    905  C   PHE A 113      26.944 -34.299   7.712  1.00 19.03           C  
-ANISOU  905  C   PHE A 113     2048   2356   2825     36   -117     80       C  
-ATOM    906  O   PHE A 113      27.703 -33.339   7.932  1.00 13.98           O  
-ANISOU  906  O   PHE A 113     1382   1669   2261     28   -135     75       O  
-ATOM    907  CB  PHE A 113      25.746 -35.309   9.586  1.00 13.58           C  
-ANISOU  907  CB  PHE A 113     1425   1707   2028     44   -150     -7       C  
-ATOM    908  CG  PHE A 113      25.487 -36.461  10.493  1.00 14.71           C  
-ANISOU  908  CG  PHE A 113     1606   1886   2096     45   -168    -47       C  
-ATOM    909  CD1 PHE A 113      24.661 -37.501  10.092  1.00 16.37           C  
-ANISOU  909  CD1 PHE A 113     1845   2150   2227     51   -145    -33       C  
-ATOM    910  CD2 PHE A 113      26.023 -36.485  11.769  1.00 16.63           C  
-ANISOU  910  CD2 PHE A 113     1860   2111   2349     39   -207    -99       C  
-ATOM    911  CE1 PHE A 113      24.390 -38.552  10.943  1.00 17.88           C  
-ANISOU  911  CE1 PHE A 113     2071   2374   2347     51   -162    -71       C  
-ATOM    912  CE2 PHE A 113      25.770 -37.542  12.622  1.00 12.89           C  
-ANISOU  912  CE2 PHE A 113     1421   1671   1806     41   -224   -137       C  
-ATOM    913  CZ  PHE A 113      24.953 -38.577  12.209  1.00 16.56           C  
-ANISOU  913  CZ  PHE A 113     1913   2189   2191     47   -201   -122       C  
-ATOM    914  N   GLU A 114      26.082 -34.324   6.704  1.00 13.90           N  
-ANISOU  914  N   GLU A 114     1400   1731   2151     44    -81    119       N  
-ATOM    915  CA  GLU A 114      25.899 -33.160   5.865  1.00 16.51           C  
-ANISOU  915  CA  GLU A 114     1700   2032   2540     47    -60    155       C  
-ATOM    916  C   GLU A 114      25.475 -31.998   6.758  1.00 18.96           C  
-ANISOU  916  C   GLU A 114     2013   2302   2890     50    -83    116       C  
-ATOM    917  O   GLU A 114      24.819 -32.187   7.791  1.00 18.28           O  
-ANISOU  917  O   GLU A 114     1958   2225   2763     56   -102     69       O  
-ATOM    918  CB  GLU A 114      24.819 -33.440   4.803  1.00 24.79           C  
-ANISOU  918  CB  GLU A 114     2756   3120   3543     56    -19    197       C  
-ATOM    919  CG  GLU A 114      23.413 -33.146   5.268  1.00 20.07           C  
-ANISOU  919  CG  GLU A 114     2183   2535   2907     68    -17    173       C  
-ATOM    920  CD  GLU A 114      22.336 -33.527   4.250  1.00 25.31           C  
-ANISOU  920  CD  GLU A 114     2855   3243   3518     75     21    214       C  
-ATOM    921  OE1 GLU A 114      21.939 -32.672   3.433  1.00 30.42           O  
-ANISOU  921  OE1 GLU A 114     3480   3877   4201     81     45    250       O  
-ATOM    922  OE2 GLU A 114      21.859 -34.678   4.296  1.00 18.47           O  
-ANISOU  922  OE2 GLU A 114     2019   2425   2574     75     27    210       O  
-ATOM    923  N   HIS A 115      25.849 -30.790   6.370  1.00 18.34           N  
-ANISOU  923  N   HIS A 115     1902   2177   2888     47    -81    136       N  
-ATOM    924  CA  HIS A 115      25.497 -29.610   7.140  1.00 20.92           C  
-ANISOU  924  CA  HIS A 115     2232   2459   3256     51   -101    102       C  
-ATOM    925  C   HIS A 115      24.212 -29.019   6.579  1.00 16.44           C  
-ANISOU  925  C   HIS A 115     1668   1900   2677     67    -71    123       C  
-ATOM    926  O   HIS A 115      24.087 -28.840   5.365  1.00 20.12           O  
-ANISOU  926  O   HIS A 115     2112   2374   3157     69    -38    175       O  
-ATOM    927  CB  HIS A 115      26.632 -28.588   7.052  1.00 24.21           C  
-ANISOU  927  CB  HIS A 115     2614   2819   3766     37   -117    112       C  
-ATOM    928  CG  HIS A 115      26.359 -27.307   7.776  1.00 25.64           C  
-ANISOU  928  CG  HIS A 115     2798   2949   3995     40   -137     80       C  
-ATOM    929  ND1 HIS A 115      25.636 -26.276   7.212  1.00 21.34           N  
-ANISOU  929  ND1 HIS A 115     2245   2383   3480     51   -115    102       N  
-ATOM    930  CD2 HIS A 115      26.727 -26.879   9.007  1.00 24.97           C  
-ANISOU  930  CD2 HIS A 115     2727   2828   3933     33   -177     28       C  
-ATOM    931  CE1 HIS A 115      25.561 -25.273   8.068  1.00 21.73           C  
-ANISOU  931  CE1 HIS A 115     2303   2385   3568     51   -140     65       C  
-ATOM    932  NE2 HIS A 115      26.204 -25.617   9.170  1.00 21.36           N  
-ANISOU  932  NE2 HIS A 115     2271   2329   3518     40   -178     19       N  
-ATOM    933  N   VAL A 116      23.257 -28.731   7.461  1.00 16.11           N  
-ANISOU  933  N   VAL A 116     1654   1858   2608     79    -82     82       N  
-ATOM    934  CA  VAL A 116      22.003 -28.097   7.069  1.00 18.56           C  
-ANISOU  934  CA  VAL A 116     1970   2175   2908     97    -56     98       C  
-ATOM    935  C   VAL A 116      21.928 -26.671   7.612  1.00 22.46           C  
-ANISOU  935  C   VAL A 116     2460   2611   3465    103    -71     75       C  
-ATOM    936  O   VAL A 116      21.982 -26.449   8.819  1.00 26.60           O  
-ANISOU  936  O   VAL A 116     3005   3112   3991    103   -104     22       O  
-ATOM    937  CB  VAL A 116      20.777 -28.902   7.567  1.00 21.44           C  
-ANISOU  937  CB  VAL A 116     2371   2591   3183    110    -51     75       C  
-ATOM    938  CG1 VAL A 116      19.478 -28.216   7.149  1.00 22.86           C  
-ANISOU  938  CG1 VAL A 116     2553   2780   3353    129    -24     95       C  
-ATOM    939  CG2 VAL A 116      20.815 -30.314   7.019  1.00 23.08           C  
-ANISOU  939  CG2 VAL A 116     2587   2856   3326    103    -36     97       C  
-ATOM    940  N   ASN A 117      21.828 -25.699   6.718  1.00 22.55           N  
-ANISOU  940  N   ASN A 117     2445   2596   3529    107    -48    115       N  
-ATOM    941  CA  ASN A 117      21.680 -24.314   7.146  1.00 19.94           C  
-ANISOU  941  CA  ASN A 117     2112   2208   3256    114    -59     98       C  
-ATOM    942  C   ASN A 117      20.259 -24.063   7.631  1.00 24.70           C  
-ANISOU  942  C   ASN A 117     2744   2828   3815    138    -50     76       C  
-ATOM    943  O   ASN A 117      19.460 -23.442   6.932  1.00 26.34           O  
-ANISOU  943  O   ASN A 117     2942   3036   4029    153    -21    109       O  
-ATOM    944  CB  ASN A 117      22.031 -23.366   6.001  1.00 28.30           C  
-ANISOU  944  CB  ASN A 117     3133   3234   4385    110    -37    150       C  
-ATOM    945  CG  ASN A 117      21.966 -21.913   6.414  1.00 36.42           C  
-ANISOU  945  CG  ASN A 117     4160   4200   5477    116    -49    133       C  
-ATOM    946  OD1 ASN A 117      22.095 -21.589   7.596  1.00 43.08           O  
-ANISOU  946  OD1 ASN A 117     5026   5013   6329    116    -82     80       O  
-ATOM    947  ND2 ASN A 117      21.762 -21.025   5.444  1.00 41.10           N  
-ANISOU  947  ND2 ASN A 117     4729   4772   6115    122    -21    177       N  
-ATOM    948  N   ASN A 118      19.935 -24.553   8.825  1.00 20.82           N  
-ANISOU  948  N   ASN A 118     2285   2349   3275    143    -75     23       N  
-ATOM    949  CA  ASN A 118      18.545 -24.502   9.284  1.00 30.46           C  
-ANISOU  949  CA  ASN A 118     3534   3596   4443    167    -65      5       C  
-ATOM    950  C   ASN A 118      18.199 -23.254  10.089  1.00 31.03           C  
-ANISOU  950  C   ASN A 118     3620   3617   4553    182    -80    -29       C  
-ATOM    951  O   ASN A 118      19.075 -22.466  10.452  1.00 30.53           O  
-ANISOU  951  O   ASN A 118     3549   3494   4556    171   -104    -47       O  
-ATOM    952  CB  ASN A 118      18.182 -25.756  10.090  1.00 23.22           C  
-ANISOU  952  CB  ASN A 118     2648   2730   3444    167    -80    -30       C  
-ATOM    953  CG  ASN A 118      18.701 -25.700  11.503  1.00 25.83           C  
-ANISOU  953  CG  ASN A 118     3001   3030   3782    163   -123    -94       C  
-ATOM    954  OD1 ASN A 118      19.862 -25.363  11.731  1.00 26.50           O  
-ANISOU  954  OD1 ASN A 118     3074   3072   3924    145   -147   -106       O  
-ATOM    955  ND2 ASN A 118      17.838 -26.003  12.468  1.00 26.57           N  
-ANISOU  955  ND2 ASN A 118     3128   3147   3819    178   -133   -134       N  
-ATOM    956  N   THR A 119      16.904 -23.081  10.346  1.00 25.53           N  
-ANISOU  956  N   THR A 119     2945   2943   3814    207    -65    -37       N  
-ATOM    957  CA  THR A 119      16.417 -22.084  11.282  1.00 23.06           C  
-ANISOU  957  CA  THR A 119     2654   2590   3520    226    -79    -76       C  
-ATOM    958  C   THR A 119      15.829 -22.852  12.459  1.00 23.83           C  
-ANISOU  958  C   THR A 119     2788   2722   3546    236    -98   -126       C  
-ATOM    959  O   THR A 119      14.883 -23.628  12.279  1.00 30.50           O  
-ANISOU  959  O   THR A 119     3642   3627   4321    247    -79   -114       O  
-ATOM    960  CB  THR A 119      15.299 -21.213  10.648  1.00 37.02           C  
-ANISOU  960  CB  THR A 119     4415   4357   5293    253    -43    -43       C  
-ATOM    961  OG1 THR A 119      15.808 -20.513   9.502  1.00 31.49           O  
-ANISOU  961  OG1 THR A 119     3680   3628   4658    244    -23      7       O  
-ATOM    962  CG2 THR A 119      14.760 -20.211  11.660  1.00 34.55           C  
-ANISOU  962  CG2 THR A 119     4129   4003   4994    276    -57    -85       C  
-ATOM    963  N   ASP A 120      16.379 -22.658  13.655  1.00 23.65           N  
-ANISOU  963  N   ASP A 120     2786   2662   3539    231   -137   -182       N  
-ATOM    964  CA  ASP A 120      15.913 -23.410  14.820  1.00 26.93           C  
-ANISOU  964  CA  ASP A 120     3236   3109   3889    238   -158   -231       C  
-ATOM    965  C   ASP A 120      14.393 -23.348  14.945  1.00 26.22           C  
-ANISOU  965  C   ASP A 120     3165   3056   3743    270   -134   -229       C  
-ATOM    966  O   ASP A 120      13.772 -22.328  14.645  1.00 30.45           O  
-ANISOU  966  O   ASP A 120     3696   3568   4304    290   -114   -212       O  
-ATOM    967  CB  ASP A 120      16.557 -22.922  16.117  1.00 28.82           C  
-ANISOU  967  CB  ASP A 120     3497   3295   4158    234   -201   -292       C  
-ATOM    968  CG  ASP A 120      16.245 -23.838  17.296  1.00 33.04           C  
-ANISOU  968  CG  ASP A 120     4064   3864   4624    237   -224   -343       C  
-ATOM    969  OD1 ASP A 120      16.764 -24.977  17.315  1.00 33.53           O  
-ANISOU  969  OD1 ASP A 120     4125   3962   4655    219   -235   -345       O  
-ATOM    970  OD2 ASP A 120      15.483 -23.424  18.198  1.00 34.32           O  
-ANISOU  970  OD2 ASP A 120     4256   4018   4766    260   -232   -379       O  
-ATOM    971  N   PHE A 121      13.797 -24.444  15.399  1.00 24.15           N  
-ANISOU  971  N   PHE A 121     2923   2852   3402    273   -136   -245       N  
-ATOM    972  CA  PHE A 121      12.345 -24.525  15.436  1.00 21.75           C  
-ANISOU  972  CA  PHE A 121     2633   2593   3038    301   -113   -237       C  
-ATOM    973  C   PHE A 121      11.775 -23.470  16.378  1.00 23.66           C  
-ANISOU  973  C   PHE A 121     2898   2797   3295    328   -122   -274       C  
-ATOM    974  O   PHE A 121      10.662 -22.990  16.179  1.00 27.82           O  
-ANISOU  974  O   PHE A 121     3428   3339   3804    355    -96   -256       O  
-ATOM    975  CB  PHE A 121      11.876 -25.931  15.814  1.00 23.07           C  
-ANISOU  975  CB  PHE A 121     2819   2829   3118    297   -117   -249       C  
-ATOM    976  CG  PHE A 121      12.101 -26.289  17.254  1.00 25.13           C  
-ANISOU  976  CG  PHE A 121     3111   3083   3355    296   -155   -314       C  
-ATOM    977  CD1 PHE A 121      11.094 -26.106  18.194  1.00 23.30           C  
-ANISOU  977  CD1 PHE A 121     2908   2864   3082    323   -160   -347       C  
-ATOM    978  CD2 PHE A 121      13.311 -26.830  17.670  1.00 28.69           C  
-ANISOU  978  CD2 PHE A 121     3563   3517   3822    270   -187   -341       C  
-ATOM    979  CE1 PHE A 121      11.296 -26.439  19.526  1.00 23.90           C  
-ANISOU  979  CE1 PHE A 121     3012   2934   3133    323   -195   -407       C  
-ATOM    980  CE2 PHE A 121      13.513 -27.167  19.002  1.00 26.79           C  
-ANISOU  980  CE2 PHE A 121     3351   3271   3558    270   -222   -400       C  
-ATOM    981  CZ  PHE A 121      12.498 -26.967  19.927  1.00 25.78           C  
-ANISOU  981  CZ  PHE A 121     3252   3155   3389    296   -226   -434       C  
-ATOM    982  N   LYS A 122      12.555 -23.088  17.383  1.00 30.38           N  
-ANISOU  982  N   LYS A 122     3766   3597   4181    321   -159   -325       N  
-ATOM    983  CA  LYS A 122      12.132 -22.049  18.319  1.00 32.67           C  
-ANISOU  983  CA  LYS A 122     4082   3843   4490    346   -170   -364       C  
-ATOM    984  C   LYS A 122      11.921 -20.682  17.664  1.00 41.90           C  
-ANISOU  984  C   LYS A 122     5236   4964   5719    362   -147   -334       C  
-ATOM    985  O   LYS A 122      11.182 -19.851  18.194  1.00 45.71           O  
-ANISOU  985  O   LYS A 122     5740   5424   6202    392   -143   -352       O  
-ATOM    986  CB  LYS A 122      13.126 -21.926  19.467  1.00 37.99           C  
-ANISOU  986  CB  LYS A 122     4775   4468   5191    331   -216   -423       C  
-ATOM    987  CG  LYS A 122      13.076 -23.079  20.447  1.00 44.58           C  
-ANISOU  987  CG  LYS A 122     5634   5345   5960    326   -241   -465       C  
-ATOM    988  CD  LYS A 122      11.936 -22.923  21.438  1.00 55.39           C  
-ANISOU  988  CD  LYS A 122     7038   6729   7279    359   -242   -500       C  
-ATOM    989  CE  LYS A 122      12.174 -23.821  22.635  1.00 61.85           C  
-ANISOU  989  CE  LYS A 122     7883   7568   8050    350   -276   -554       C  
-ATOM    990  NZ  LYS A 122      13.628 -23.838  22.973  1.00 63.05           N  
-ANISOU  990  NZ  LYS A 122     8030   7674   8252    319   -313   -580       N  
-ATOM    991  N   GLN A 123      12.574 -20.442  16.528  1.00 40.19           N  
-ANISOU  991  N   GLN A 123     4986   4732   5554    344   -133   -289       N  
-ATOM    992  CA  GLN A 123      12.338 -19.217  15.756  1.00 42.13           C  
-ANISOU  992  CA  GLN A 123     5215   4937   5855    358   -107   -253       C  
-ATOM    993  C   GLN A 123      11.438 -19.467  14.549  1.00 34.13           C  
-ANISOU  993  C   GLN A 123     4178   3978   4812    369    -62   -191       C  
-ATOM    994  O   GLN A 123      10.647 -18.611  14.166  1.00 41.66           O  
-ANISOU  994  O   GLN A 123     5129   4922   5778    395    -35   -167       O  
-ATOM    995  CB  GLN A 123      13.657 -18.592  15.287  1.00 53.75           C  
-ANISOU  995  CB  GLN A 123     6663   6348   7411    331   -120   -241       C  
-ATOM    996  CG  GLN A 123      13.475 -17.520  14.203  1.00 64.11           C  
-ANISOU  996  CG  GLN A 123     7950   7630   8778    340    -89   -191       C  
-ATOM    997  CD  GLN A 123      14.786 -16.886  13.747  1.00 71.16           C  
-ANISOU  997  CD  GLN A 123     8819   8462   9755    312   -103   -179       C  
-ATOM    998  OE1 GLN A 123      15.835 -17.076  14.370  1.00 74.87           O  
-ANISOU  998  OE1 GLN A 123     9294   8904  10248    288   -139   -212       O  
-ATOM    999  NE2 GLN A 123      14.729 -16.127  12.653  1.00 65.45           N  
-ANISOU  999  NE2 GLN A 123     8069   7720   9078    316    -74   -129       N  
-ATOM   1000  N   LEU A 124      11.559 -20.650  13.953  1.00 26.63           N  
-ANISOU 1000  N   LEU A 124     3213   3085   3821    350    -54   -165       N  
-ATOM   1001  CA  LEU A 124      10.862 -20.961  12.710  1.00 22.62           C  
-ANISOU 1001  CA  LEU A 124     2680   2626   3287    355    -13   -104       C  
-ATOM   1002  C   LEU A 124       9.352 -21.164  12.855  1.00 24.56           C  
-ANISOU 1002  C   LEU A 124     2942   2927   3464    384     10    -96       C  
-ATOM   1003  O   LEU A 124       8.578 -20.676  12.037  1.00 25.63           O  
-ANISOU 1003  O   LEU A 124     3062   3077   3601    401     45    -51       O  
-ATOM   1004  CB  LEU A 124      11.475 -22.198  12.058  1.00 22.93           C  
-ANISOU 1004  CB  LEU A 124     2704   2708   3301    325    -12    -80       C  
-ATOM   1005  CG  LEU A 124      10.905 -22.567  10.690  1.00 25.19           C  
-ANISOU 1005  CG  LEU A 124     2965   3044   3563    324     28    -15       C  
-ATOM   1006  CD1 LEU A 124      11.267 -21.499   9.679  1.00 25.67           C  
-ANISOU 1006  CD1 LEU A 124     2994   3060   3698    323     49     28       C  
-ATOM   1007  CD2 LEU A 124      11.437 -23.922  10.244  1.00 27.28           C  
-ANISOU 1007  CD2 LEU A 124     3222   3353   3789    296     25      0       C  
-ATOM   1008  N   TYR A 125       8.931 -21.888  13.884  1.00 25.83           N  
-ANISOU 1008  N   TYR A 125     3131   3120   3562    390     -8   -137       N  
-ATOM   1009  CA  TYR A 125       7.527 -22.269  13.993  1.00 24.24           C  
-ANISOU 1009  CA  TYR A 125     2942   2981   3288    415     13   -126       C  
-ATOM   1010  C   TYR A 125       6.575 -21.076  14.050  1.00 28.43           C  
-ANISOU 1010  C   TYR A 125     3477   3491   3835    452     34   -118       C  
-ATOM   1011  O   TYR A 125       5.461 -21.146  13.539  1.00 26.99           O  
-ANISOU 1011  O   TYR A 125     3286   3357   3611    470     65    -80       O  
-ATOM   1012  CB  TYR A 125       7.299 -23.210  15.177  1.00 28.48           C  
-ANISOU 1012  CB  TYR A 125     3511   3553   3759    414    -14   -176       C  
-ATOM   1013  CG  TYR A 125       7.733 -24.638  14.914  1.00 24.19           C  
-ANISOU 1013  CG  TYR A 125     2963   3057   3169    384    -22   -169       C  
-ATOM   1014  CD1 TYR A 125       8.639 -24.937  13.905  1.00 29.65           C  
-ANISOU 1014  CD1 TYR A 125     3629   3743   3894    356    -16   -135       C  
-ATOM   1015  CD2 TYR A 125       7.214 -25.685  15.664  1.00 22.39           C  
-ANISOU 1015  CD2 TYR A 125     2759   2883   2865    384    -35   -196       C  
-ATOM   1016  CE1 TYR A 125       9.033 -26.246  13.663  1.00 26.87           C  
-ANISOU 1016  CE1 TYR A 125     3276   3434   3498    330    -22   -128       C  
-ATOM   1017  CE2 TYR A 125       7.593 -26.992  15.431  1.00 22.20           C  
-ANISOU 1017  CE2 TYR A 125     2736   2903   2798    357    -42   -189       C  
-ATOM   1018  CZ  TYR A 125       8.506 -27.268  14.431  1.00 21.99           C  
-ANISOU 1018  CZ  TYR A 125     2684   2867   2804    331    -35   -156       C  
-ATOM   1019  OH  TYR A 125       8.884 -28.571  14.196  1.00 26.49           O  
-ANISOU 1019  OH  TYR A 125     3256   3478   3329    306    -41   -150       O  
-ATOM   1020  N   GLN A 126       7.001 -19.974  14.651  1.00 26.10           N  
-ANISOU 1020  N   GLN A 126     3194   3126   3599    463     18   -150       N  
-ATOM   1021  CA  GLN A 126       6.097 -18.830  14.741  1.00 33.26           C  
-ANISOU 1021  CA  GLN A 126     4108   4011   4520    502     39   -143       C  
-ATOM   1022  C   GLN A 126       6.057 -17.980  13.469  1.00 29.17           C  
-ANISOU 1022  C   GLN A 126     3557   3471   4054    505     73    -85       C  
-ATOM   1023  O   GLN A 126       5.333 -16.989  13.401  1.00 29.39           O  
-ANISOU 1023  O   GLN A 126     3588   3481   4098    537     94    -72       O  
-ATOM   1024  CB  GLN A 126       6.431 -17.966  15.950  1.00 44.05           C  
-ANISOU 1024  CB  GLN A 126     5505   5311   5921    516     11   -202       C  
-ATOM   1025  CG  GLN A 126       7.863 -17.509  15.994  1.00 47.35           C  
-ANISOU 1025  CG  GLN A 126     5919   5658   6415    488    -17   -221       C  
-ATOM   1026  CD  GLN A 126       8.249 -17.032  17.371  1.00 53.71           C  
-ANISOU 1026  CD  GLN A 126     6761   6410   7236    494    -54   -288       C  
-ATOM   1027  OE1 GLN A 126       7.478 -17.178  18.322  1.00 58.27           O  
-ANISOU 1027  OE1 GLN A 126     7368   7008   7764    519    -60   -322       O  
-ATOM   1028  NE2 GLN A 126       9.439 -16.455  17.492  1.00 49.81           N  
-ANISOU 1028  NE2 GLN A 126     6266   5849   6813    472    -80   -307       N  
-ATOM   1029  N   THR A 127       6.831 -18.369  12.462  1.00 30.64           N  
-ANISOU 1029  N   THR A 127     3714   3662   4267    474     78    -50       N  
-ATOM   1030  CA  THR A 127       6.793 -17.687  11.174  1.00 34.89           C  
-ANISOU 1030  CA  THR A 127     4219   4188   4850    475    111      9       C  
-ATOM   1031  C   THR A 127       6.149 -18.541  10.069  1.00 33.67           C  
-ANISOU 1031  C   THR A 127     4041   4108   4645    469    143     67       C  
-ATOM   1032  O   THR A 127       5.854 -18.034   8.989  1.00 36.13           O  
-ANISOU 1032  O   THR A 127     4326   4421   4981    474    175    119       O  
-ATOM   1033  CB  THR A 127       8.199 -17.225  10.733  1.00 41.61           C  
-ANISOU 1033  CB  THR A 127     5051   4975   5782    447     96     13       C  
-ATOM   1034  OG1 THR A 127       8.992 -18.360  10.359  1.00 44.49           O  
-ANISOU 1034  OG1 THR A 127     5402   5370   6131    412     85     20       O  
-ATOM   1035  CG2 THR A 127       8.889 -16.482  11.867  1.00 40.35           C  
-ANISOU 1035  CG2 THR A 127     4917   4744   5669    448     60    -46       C  
-ATOM   1036  N   LEU A 128       5.910 -19.824  10.341  1.00 27.96           N  
-ANISOU 1036  N   LEU A 128     3328   3446   3851    456    134     57       N  
-ATOM   1037  CA  LEU A 128       5.367 -20.718   9.316  1.00 25.47           C  
-ANISOU 1037  CA  LEU A 128     2993   3201   3484    445    161    109       C  
-ATOM   1038  C   LEU A 128       3.936 -20.357   8.941  1.00 23.54           C  
-ANISOU 1038  C   LEU A 128     2744   2998   3204    476    197    147       C  
-ATOM   1039  O   LEU A 128       3.091 -20.105   9.799  1.00 18.72           O  
-ANISOU 1039  O   LEU A 128     2154   2396   2561    504    195    121       O  
-ATOM   1040  CB  LEU A 128       5.424 -22.184   9.746  1.00 25.58           C  
-ANISOU 1040  CB  LEU A 128     3023   3270   3427    424    143     89       C  
-ATOM   1041  CG  LEU A 128       6.786 -22.867   9.916  1.00 27.72           C  
-ANISOU 1041  CG  LEU A 128     3295   3520   3718    390    113     63       C  
-ATOM   1042  CD1 LEU A 128       6.568 -24.314  10.316  1.00 31.40           C  
-ANISOU 1042  CD1 LEU A 128     3780   4048   4103    376    100     48       C  
-ATOM   1043  CD2 LEU A 128       7.636 -22.779   8.646  1.00 22.75           C  
-ANISOU 1043  CD2 LEU A 128     2632   2872   3139    367    128    109       C  
-ATOM   1044  N   THR A 129       3.672 -20.329   7.642  1.00 20.65           N  
-ANISOU 1044  N   THR A 129     2348   2656   2843    470    229    209       N  
-ATOM   1045  CA  THR A 129       2.322 -20.082   7.171  1.00 19.47           C  
-ANISOU 1045  CA  THR A 129     2190   2553   2656    496    264    251       C  
-ATOM   1046  C   THR A 129       1.583 -21.408   7.075  1.00 14.21           C  
-ANISOU 1046  C   THR A 129     1528   1971   1898    484    269    266       C  
-ATOM   1047  O   THR A 129       2.178 -22.475   7.260  1.00 21.10           O  
-ANISOU 1047  O   THR A 129     2411   2863   2742    456    247    247       O  
-ATOM   1048  CB  THR A 129       2.327 -19.442   5.779  1.00 19.10           C  
-ANISOU 1048  CB  THR A 129     2107   2496   2654    494    297    314       C  
-ATOM   1049  OG1 THR A 129       2.928 -20.354   4.863  1.00 18.37           O  
-ANISOU 1049  OG1 THR A 129     1997   2430   2551    459    301    344       O  
-ATOM   1050  CG2 THR A 129       3.098 -18.121   5.779  1.00 18.42           C  
-ANISOU 1050  CG2 THR A 129     2014   2324   2661    503    293    303       C  
-ATOM   1051  N   ASP A 130       0.280 -21.333   6.805  1.00 15.32           N  
-ANISOU 1051  N   ASP A 130     1665   2164   1993    506    296    301       N  
-ATOM   1052  CA  ASP A 130      -0.526 -22.526   6.555  1.00 15.53           C  
-ANISOU 1052  CA  ASP A 130     1693   2275   1933    494    305    326       C  
-ATOM   1053  C   ASP A 130       0.128 -23.367   5.463  1.00 19.62           C  
-ANISOU 1053  C   ASP A 130     2195   2814   2448    455    310    361       C  
-ATOM   1054  O   ASP A 130       0.277 -24.588   5.598  1.00 17.26           O  
-ANISOU 1054  O   ASP A 130     1909   2555   2094    431    295    351       O  
-ATOM   1055  CB  ASP A 130      -1.955 -22.139   6.156  1.00 18.05           C  
-ANISOU 1055  CB  ASP A 130     2000   2641   2216    522    339    371       C  
-ATOM   1056  CG  ASP A 130      -2.829 -23.349   5.827  1.00 28.92           C  
-ANISOU 1056  CG  ASP A 130     3379   4108   3503    507    348    402       C  
-ATOM   1057  OD1 ASP A 130      -2.609 -24.435   6.409  1.00 22.80           O  
-ANISOU 1057  OD1 ASP A 130     2624   3359   2678    486    323    371       O  
-ATOM   1058  OD2 ASP A 130      -3.757 -23.205   4.997  1.00 27.70           O  
-ANISOU 1058  OD2 ASP A 130     3204   3997   3325    515    380    458       O  
-ATOM   1059  N   TYR A 131       0.535 -22.713   4.382  1.00 14.64           N  
-ANISOU 1059  N   TYR A 131     1535   2153   1875    451    331    402       N  
-ATOM   1060  CA  TYR A 131       1.156 -23.441   3.282  1.00 13.86           C  
-ANISOU 1060  CA  TYR A 131     1419   2071   1775    417    339    439       C  
-ATOM   1061  C   TYR A 131       2.455 -24.118   3.740  1.00 15.86           C  
-ANISOU 1061  C   TYR A 131     1687   2297   2044    390    306    396       C  
-ATOM   1062  O   TYR A 131       2.677 -25.311   3.472  1.00 14.57           O  
-ANISOU 1062  O   TYR A 131     1531   2174   1833    363    300    403       O  
-ATOM   1063  CB  TYR A 131       1.384 -22.536   2.071  1.00 15.37           C  
-ANISOU 1063  CB  TYR A 131     1576   2233   2031    419    368    490       C  
-ATOM   1064  CG  TYR A 131       1.843 -23.309   0.861  1.00 21.42           C  
-ANISOU 1064  CG  TYR A 131     2325   3026   2787    387    380    534       C  
-ATOM   1065  CD1 TYR A 131       0.934 -23.957   0.044  1.00 19.87           C  
-ANISOU 1065  CD1 TYR A 131     2122   2900   2529    379    405    584       C  
-ATOM   1066  CD2 TYR A 131       3.200 -23.422   0.557  1.00 22.65           C  
-ANISOU 1066  CD2 TYR A 131     2474   3139   2995    363    367    526       C  
-ATOM   1067  CE1 TYR A 131       1.356 -24.680  -1.065  1.00 24.62           C  
-ANISOU 1067  CE1 TYR A 131     2710   3524   3119    350    417    624       C  
-ATOM   1068  CE2 TYR A 131       3.631 -24.146  -0.538  1.00 26.18           C  
-ANISOU 1068  CE2 TYR A 131     2906   3610   3430    336    380    566       C  
-ATOM   1069  CZ  TYR A 131       2.704 -24.773  -1.345  1.00 28.95           C  
-ANISOU 1069  CZ  TYR A 131     3253   4029   3719    329    405    615       C  
-ATOM   1070  OH  TYR A 131       3.120 -25.493  -2.437  1.00 28.68           O  
-ANISOU 1070  OH  TYR A 131     3208   4017   3672    303    418    654       O  
-ATOM   1071  N   ASP A 132       3.310 -23.369   4.433  1.00 15.64           N  
-ANISOU 1071  N   ASP A 132     1664   2199   2080    396    284    353       N  
-ATOM   1072  CA  ASP A 132       4.568 -23.953   4.912  1.00 16.36           C  
-ANISOU 1072  CA  ASP A 132     1766   2261   2188    371    251    313       C  
-ATOM   1073  C   ASP A 132       4.327 -25.233   5.736  1.00 16.52           C  
-ANISOU 1073  C   ASP A 132     1817   2331   2130    361    229    278       C  
-ATOM   1074  O   ASP A 132       5.054 -26.225   5.588  1.00 17.77           O  
-ANISOU 1074  O   ASP A 132     1980   2503   2270    333    216    274       O  
-ATOM   1075  CB  ASP A 132       5.359 -22.964   5.774  1.00 16.16           C  
-ANISOU 1075  CB  ASP A 132     1747   2158   2234    382    226    265       C  
-ATOM   1076  CG  ASP A 132       5.853 -21.751   5.005  1.00 24.34           C  
-ANISOU 1076  CG  ASP A 132     2756   3137   3356    387    242    294       C  
-ATOM   1077  OD1 ASP A 132       6.131 -21.847   3.786  1.00 19.87           O  
-ANISOU 1077  OD1 ASP A 132     2163   2580   2808    371    264    344       O  
-ATOM   1078  OD2 ASP A 132       5.980 -20.686   5.651  1.00 32.84           O  
-ANISOU 1078  OD2 ASP A 132     3839   4157   4482    406    232    265       O  
-ATOM   1079  N   ILE A 133       3.324 -25.208   6.613  1.00 15.85           N  
-ANISOU 1079  N   ILE A 133     1752   2272   1998    383    225    255       N  
-ATOM   1080  CA  ILE A 133       3.093 -26.341   7.508  1.00 15.83           C  
-ANISOU 1080  CA  ILE A 133     1778   2312   1923    375    202    218       C  
-ATOM   1081  C   ILE A 133       2.749 -27.580   6.693  1.00 18.20           C  
-ANISOU 1081  C   ILE A 133     2077   2682   2156    351    216    258       C  
-ATOM   1082  O   ILE A 133       3.313 -28.648   6.906  1.00 16.34           O  
-ANISOU 1082  O   ILE A 133     1858   2463   1889    327    197    239       O  
-ATOM   1083  CB  ILE A 133       1.996 -26.064   8.554  1.00 18.98           C  
-ANISOU 1083  CB  ILE A 133     2199   2731   2283    406    198    190       C  
-ATOM   1084  CG1 ILE A 133       2.408 -24.933   9.494  1.00 19.17           C  
-ANISOU 1084  CG1 ILE A 133     2232   2684   2368    428    180    143       C  
-ATOM   1085  CG2 ILE A 133       1.692 -27.329   9.374  1.00 19.15           C  
-ANISOU 1085  CG2 ILE A 133     2249   2805   2223    395    176    159       C  
-ATOM   1086  CD1 ILE A 133       1.238 -24.411  10.344  1.00 19.40           C  
-ANISOU 1086  CD1 ILE A 133     2278   2728   2367    466    184    126       C  
-ATOM   1087  N   ARG A 134       1.842 -27.434   5.733  1.00 18.06           N  
-ANISOU 1087  N   ARG A 134     2042   2703   2118    356    249    315       N  
-ATOM   1088  CA  ARG A 134       1.459 -28.566   4.900  1.00 19.42           C  
-ANISOU 1088  CA  ARG A 134     2213   2940   2225    332    263    356       C  
-ATOM   1089  C   ARG A 134       2.666 -29.056   4.105  1.00 14.78           C  
-ANISOU 1089  C   ARG A 134     1616   2332   1666    302    261    370       C  
-ATOM   1090  O   ARG A 134       2.908 -30.260   3.988  1.00 13.62           O  
-ANISOU 1090  O   ARG A 134     1486   2221   1470    277    252    369       O  
-ATOM   1091  CB  ARG A 134       0.338 -28.158   3.955  1.00 18.51           C  
-ANISOU 1091  CB  ARG A 134     2077   2864   2092    343    300    417       C  
-ATOM   1092  CG  ARG A 134      -0.812 -27.440   4.653  1.00 11.47           C  
-ANISOU 1092  CG  ARG A 134     1189   1985   1185    379    307    409       C  
-ATOM   1093  CD  ARG A 134      -2.009 -27.410   3.747  1.00 17.63           C  
-ANISOU 1093  CD  ARG A 134     1951   2823   1925    384    341    471       C  
-ATOM   1094  NE  ARG A 134      -3.040 -26.491   4.228  1.00 14.71           N  
-ANISOU 1094  NE  ARG A 134     1578   2457   1555    422    353    473       N  
-ATOM   1095  CZ  ARG A 134      -4.331 -26.635   3.950  1.00 19.25           C  
-ANISOU 1095  CZ  ARG A 134     2146   3096   2072    432    375    512       C  
-ATOM   1096  NH1 ARG A 134      -4.736 -27.673   3.227  1.00 18.04           N  
-ANISOU 1096  NH1 ARG A 134     1992   3006   1856    404    383    551       N  
-ATOM   1097  NH2 ARG A 134      -5.207 -25.754   4.404  1.00 16.76           N  
-ANISOU 1097  NH2 ARG A 134     1827   2781   1761    470    387    513       N  
-ATOM   1098  N   PHE A 135       3.409 -28.112   3.540  1.00 17.70           N  
-ANISOU 1098  N   PHE A 135     1962   2647   2118    305    270    384       N  
-ATOM   1099  CA  PHE A 135       4.584 -28.444   2.737  1.00 14.43           C  
-ANISOU 1099  CA  PHE A 135     1534   2210   1739    280    270    401       C  
-ATOM   1100  C   PHE A 135       5.599 -29.274   3.531  1.00 13.48           C  
-ANISOU 1100  C   PHE A 135     1436   2075   1612    262    236    352       C  
-ATOM   1101  O   PHE A 135       6.045 -30.343   3.091  1.00 17.50           O  
-ANISOU 1101  O   PHE A 135     1952   2610   2086    238    234    363       O  
-ATOM   1102  CB  PHE A 135       5.235 -27.171   2.205  1.00 13.99           C  
-ANISOU 1102  CB  PHE A 135     1449   2090   1778    289    281    417       C  
-ATOM   1103  CG  PHE A 135       6.443 -27.427   1.347  1.00 23.47           C  
-ANISOU 1103  CG  PHE A 135     2632   3267   3019    265    283    439       C  
-ATOM   1104  CD1 PHE A 135       6.326 -27.524  -0.034  1.00 21.84           C  
-ANISOU 1104  CD1 PHE A 135     2404   3083   2812    255    314    500       C  
-ATOM   1105  CD2 PHE A 135       7.700 -27.584   1.925  1.00 22.43           C  
-ANISOU 1105  CD2 PHE A 135     2507   3092   2924    253    254    398       C  
-ATOM   1106  CE1 PHE A 135       7.454 -27.765  -0.823  1.00 20.28           C  
-ANISOU 1106  CE1 PHE A 135     2191   2864   2652    235    317    520       C  
-ATOM   1107  CE2 PHE A 135       8.813 -27.823   1.146  1.00 23.94           C  
-ANISOU 1107  CE2 PHE A 135     2681   3264   3152    233    257    420       C  
-ATOM   1108  CZ  PHE A 135       8.690 -27.914  -0.229  1.00 22.75           C  
-ANISOU 1108  CZ  PHE A 135     2508   3134   3000    225    289    481       C  
-ATOM   1109  N   TYR A 136       5.956 -28.785   4.710  1.00 13.25           N  
-ANISOU 1109  N   TYR A 136     1419   2004   1612    275    209    297       N  
-ATOM   1110  CA  TYR A 136       6.996 -29.432   5.496  1.00 14.94           C  
-ANISOU 1110  CA  TYR A 136     1651   2197   1828    259    175    249       C  
-ATOM   1111  C   TYR A 136       6.495 -30.735   6.113  1.00 15.14           C  
-ANISOU 1111  C   TYR A 136     1708   2281   1764    250    161    227       C  
-ATOM   1112  O   TYR A 136       7.247 -31.697   6.250  1.00 17.40           O  
-ANISOU 1112  O   TYR A 136     2008   2575   2030    230    144    211       O  
-ATOM   1113  CB  TYR A 136       7.576 -28.465   6.538  1.00 17.09           C  
-ANISOU 1113  CB  TYR A 136     1926   2404   2163    274    149    198       C  
-ATOM   1114  CG  TYR A 136       8.453 -27.364   5.957  1.00 16.63           C  
-ANISOU 1114  CG  TYR A 136     1838   2281   2198    274    155    214       C  
-ATOM   1115  CD1 TYR A 136       9.543 -27.667   5.139  1.00 19.48           C  
-ANISOU 1115  CD1 TYR A 136     2180   2626   2593    251    158    238       C  
-ATOM   1116  CD2 TYR A 136       8.193 -26.026   6.226  1.00 18.56           C  
-ANISOU 1116  CD2 TYR A 136     2075   2481   2497    297    159    207       C  
-ATOM   1117  CE1 TYR A 136      10.350 -26.666   4.622  1.00 21.51           C  
-ANISOU 1117  CE1 TYR A 136     2411   2827   2936    250    162    255       C  
-ATOM   1118  CE2 TYR A 136       8.990 -25.014   5.703  1.00 16.97           C  
-ANISOU 1118  CE2 TYR A 136     1848   2220   2381    296    163    222       C  
-ATOM   1119  CZ  TYR A 136      10.065 -25.337   4.903  1.00 14.72           C  
-ANISOU 1119  CZ  TYR A 136     1543   1922   2128    272    165    247       C  
-ATOM   1120  OH  TYR A 136      10.874 -24.355   4.378  1.00 22.04           O  
-ANISOU 1120  OH  TYR A 136     2443   2791   3139    269    169    264       O  
-ATOM   1121  N   MET A 137       5.215 -30.781   6.477  1.00 16.57           N  
-ANISOU 1121  N   MET A 137     1901   2505   1890    266    168    228       N  
-ATOM   1122  CA AMET A 137       4.618 -32.029   6.940  1.00 15.26           C  
-ANISOU 1122  CA AMET A 137     1765   2401   1635    256    158    215       C  
-ATOM   1123  CA BMET A 137       4.612 -32.026   6.941  0.00 15.30           C  
-ANISOU 1123  CA BMET A 137     1769   2405   1639    256    158    215       C  
-ATOM   1124  C   MET A 137       4.739 -33.107   5.868  1.00 15.98           C  
-ANISOU 1124  C   MET A 137     1855   2533   1682    228    174    258       C  
-ATOM   1125  O   MET A 137       5.108 -34.241   6.155  1.00 16.30           O  
-ANISOU 1125  O   MET A 137     1919   2597   1678    209    157    239       O  
-ATOM   1126  CB AMET A 137       3.148 -31.814   7.328  1.00 13.48           C  
-ANISOU 1126  CB AMET A 137     1547   2218   1359    277    169    220       C  
-ATOM   1127  CB BMET A 137       3.143 -31.811   7.320  0.00 14.47           C  
-ANISOU 1127  CB BMET A 137     1671   2343   1484    277    169    221       C  
-ATOM   1128  CG AMET A 137       2.971 -31.251   8.723  1.00 14.23           C  
-ANISOU 1128  CG AMET A 137     1657   2286   1464    302    146    164       C  
-ATOM   1129  CG BMET A 137       2.937 -31.528   8.800  0.00 14.00           C  
-ANISOU 1129  CG BMET A 137     1633   2268   1420    298    143    161       C  
-ATOM   1130  SD AMET A 137       3.362 -32.472  10.003  1.00 20.34           S  
-ANISOU 1130  SD AMET A 137     2468   3077   2182    287    106    102       S  
-ATOM   1131  SD BMET A 137       3.329 -32.976   9.799  0.00 21.63           S  
-ANISOU 1131  SD BMET A 137     2635   3261   2321    277    107    111       S  
-ATOM   1132  CE AMET A 137       1.836 -33.425  10.069  1.00 46.14           C  
-ANISOU 1132  CE AMET A 137     5753   6435   5341    287    117    123       C  
-ATOM   1133  CE BMET A 137       3.564 -32.239  11.415  0.00 20.62           C  
-ANISOU 1133  CE BMET A 137     2524   3084   2225    302     75     39       C  
-ATOM   1134  N   TYR A 138       4.445 -32.743   4.627  1.00 12.97           N  
-ANISOU 1134  N   TYR A 138     1449   2162   1316    226    206    316       N  
-ATOM   1135  CA  TYR A 138       4.554 -33.690   3.530  1.00 11.88           C  
-ANISOU 1135  CA  TYR A 138     1311   2061   1140    201    222    360       C  
-ATOM   1136  C   TYR A 138       6.006 -34.147   3.401  1.00 11.80           C  
-ANISOU 1136  C   TYR A 138     1303   2016   1164    183    208    345       C  
-ATOM   1137  O   TYR A 138       6.280 -35.316   3.161  1.00 15.91           O  
-ANISOU 1137  O   TYR A 138     1842   2567   1635    162    204    350       O  
-ATOM   1138  CB  TYR A 138       4.108 -33.040   2.234  1.00 15.92           C  
-ANISOU 1138  CB  TYR A 138     1793   2579   1675    204    258    422       C  
-ATOM   1139  CG  TYR A 138       3.774 -34.023   1.140  1.00 17.92           C  
-ANISOU 1139  CG  TYR A 138     2052   2887   1870    181    278    472       C  
-ATOM   1140  CD1 TYR A 138       2.588 -34.748   1.169  1.00 16.94           C  
-ANISOU 1140  CD1 TYR A 138     1946   2830   1660    175    284    488       C  
-ATOM   1141  CD2 TYR A 138       4.631 -34.205   0.068  1.00 22.10           C  
-ANISOU 1141  CD2 TYR A 138     2567   3400   2429    164    292    505       C  
-ATOM   1142  CE1 TYR A 138       2.277 -35.645   0.158  1.00 21.08           C  
-ANISOU 1142  CE1 TYR A 138     2477   3403   2129    151    302    534       C  
-ATOM   1143  CE2 TYR A 138       4.334 -35.086  -0.939  1.00 27.38           C  
-ANISOU 1143  CE2 TYR A 138     3244   4116   3043    143    311    550       C  
-ATOM   1144  CZ  TYR A 138       3.160 -35.807  -0.894  1.00 19.30           C  
-ANISOU 1144  CZ  TYR A 138     2241   3158   1935    136    315    564       C  
-ATOM   1145  OH  TYR A 138       2.881 -36.684  -1.920  1.00 22.96           O  
-ANISOU 1145  OH  TYR A 138     2714   3667   2344    112    333    609       O  
-ATOM   1146  N   GLU A 139       6.937 -33.223   3.573  1.00 14.75           N  
-ANISOU 1146  N   GLU A 139     1658   2326   1621    191    199    327       N  
-ATOM   1147  CA  GLU A 139       8.349 -33.573   3.478  1.00 16.15           C  
-ANISOU 1147  CA  GLU A 139     1832   2469   1836    175    185    314       C  
-ATOM   1148  C   GLU A 139       8.779 -34.534   4.591  1.00 13.10           C  
-ANISOU 1148  C   GLU A 139     1478   2090   1409    167    152    261       C  
-ATOM   1149  O   GLU A 139       9.571 -35.448   4.356  1.00 13.07           O  
-ANISOU 1149  O   GLU A 139     1484   2093   1390    148    145    262       O  
-ATOM   1150  CB  GLU A 139       9.216 -32.311   3.454  1.00 14.66           C  
-ANISOU 1150  CB  GLU A 139     1615   2210   1747    185    182    308       C  
-ATOM   1151  CG  GLU A 139       8.999 -31.461   2.196  1.00 13.28           C  
-ANISOU 1151  CG  GLU A 139     1407   2024   1615    190    216    366       C  
-ATOM   1152  CD  GLU A 139       9.424 -32.176   0.931  1.00 20.95           C  
-ANISOU 1152  CD  GLU A 139     2369   3018   2573    170    237    415       C  
-ATOM   1153  OE1 GLU A 139      10.524 -32.754   0.908  1.00 22.45           O  
-ANISOU 1153  OE1 GLU A 139     2562   3192   2774    155    224    404       O  
-ATOM   1154  OE2 GLU A 139       8.672 -32.160  -0.053  1.00 20.40           O  
-ANISOU 1154  OE2 GLU A 139     2289   2981   2480    170    267    465       O  
-ATOM   1155  N   ILE A 140       8.270 -34.331   5.806  1.00 12.25           N  
-ANISOU 1155  N   ILE A 140     1393   1793   1470   -117     97      1       N  
-ATOM   1156  CA  ILE A 140       8.551 -35.271   6.901  1.00 14.01           C  
-ANISOU 1156  CA  ILE A 140     1643   1958   1720   -108     82    -41       C  
-ATOM   1157  C   ILE A 140       7.971 -36.656   6.577  1.00 17.14           C  
-ANISOU 1157  C   ILE A 140     2045   2381   2089   -128     89    -81       C  
-ATOM   1158  O   ILE A 140       8.593 -37.693   6.817  1.00 12.90           O  
-ANISOU 1158  O   ILE A 140     1515   1814   1571   -130     92   -126       O  
-ATOM   1159  CB  ILE A 140       7.958 -34.780   8.242  1.00 13.59           C  
-ANISOU 1159  CB  ILE A 140     1618   1858   1687    -85     62    -20       C  
-ATOM   1160  CG1 ILE A 140       8.579 -33.438   8.639  1.00 18.92           C  
-ANISOU 1160  CG1 ILE A 140     2293   2500   2394    -68     55     12       C  
-ATOM   1161  CG2 ILE A 140       8.198 -35.806   9.345  1.00 14.03           C  
-ANISOU 1161  CG2 ILE A 140     1702   1863   1767    -76     47    -59       C  
-ATOM   1162  CD1 ILE A 140       7.880 -32.761   9.816  1.00 13.79           C  
-ANISOU 1162  CD1 ILE A 140     1674   1811   1757    -47     41     36       C  
-ATOM   1163  N   LEU A 141       6.765 -36.666   6.025  1.00 13.18           N  
-ANISOU 1163  N   LEU A 141     1536   1930   1542   -143     91    -63       N  
-ATOM   1164  CA  LEU A 141       6.122 -37.916   5.672  1.00 11.84           C  
-ANISOU 1164  CA  LEU A 141     1370   1787   1343   -166     95   -101       C  
-ATOM   1165  C   LEU A 141       6.939 -38.706   4.646  1.00 12.40           C  
-ANISOU 1165  C   LEU A 141     1429   1882   1401   -189    118   -146       C  
-ATOM   1166  O   LEU A 141       6.977 -39.930   4.705  1.00 14.53           O  
-ANISOU 1166  O   LEU A 141     1708   2138   1674   -201    124   -195       O  
-ATOM   1167  CB  LEU A 141       4.708 -37.647   5.158  1.00 12.23           C  
-ANISOU 1167  CB  LEU A 141     1407   1893   1345   -182     92    -65       C  
-ATOM   1168  CG  LEU A 141       3.670 -37.372   6.248  1.00 16.86           C  
-ANISOU 1168  CG  LEU A 141     2010   2451   1944   -162     75    -33       C  
-ATOM   1169  CD1 LEU A 141       2.324 -36.944   5.621  1.00 13.42           C  
-ANISOU 1169  CD1 LEU A 141     1555   2078   1467   -178     73     14       C  
-ATOM   1170  CD2 LEU A 141       3.480 -38.596   7.132  1.00 16.36           C  
-ANISOU 1170  CD2 LEU A 141     1971   2345   1900   -159     67    -75       C  
-ATOM   1171  N   LYS A 142       7.602 -38.016   3.718  1.00 17.86           N  
-ANISOU 1171  N   LYS A 142     2098   2606   2080   -194    133   -131       N  
-ATOM   1172  CA  LYS A 142       8.466 -38.709   2.757  1.00 13.81           C  
-ANISOU 1172  CA  LYS A 142     1575   2114   1556   -213    160   -174       C  
-ATOM   1173  C   LYS A 142       9.566 -39.452   3.502  1.00 20.53           C  
-ANISOU 1173  C   LYS A 142     2440   2897   2466   -197    165   -213       C  
-ATOM   1174  O   LYS A 142       9.814 -40.631   3.254  1.00 16.81           O  
-ANISOU 1174  O   LYS A 142     1974   2418   1995   -210    182   -265       O  
-ATOM   1175  CB  LYS A 142       9.093 -37.735   1.760  1.00 18.22           C  
-ANISOU 1175  CB  LYS A 142     2108   2714   2099   -215    177   -142       C  
-ATOM   1176  CG  LYS A 142       8.122 -37.187   0.729  1.00 24.39           C  
-ANISOU 1176  CG  LYS A 142     2872   3578   2817   -237    178   -106       C  
-ATOM   1177  CD  LYS A 142       8.860 -36.236  -0.209  1.00 26.64           C  
-ANISOU 1177  CD  LYS A 142     3129   3899   3092   -236    198    -72       C  
-ATOM   1178  CE  LYS A 142       7.892 -35.483  -1.100  1.00 28.97           C  
-ANISOU 1178  CE  LYS A 142     3403   4275   3331   -253    195    -20       C  
-ATOM   1179  NZ  LYS A 142       8.615 -34.486  -1.930  1.00 31.54           N  
-ANISOU 1179  NZ  LYS A 142     3700   4633   3653   -247    215     21       N  
-ATOM   1180  N   ALA A 143      10.214 -38.750   4.426  1.00 13.04           N  
-ANISOU 1180  N   ALA A 143     1493   1895   1566   -169    149   -188       N  
-ATOM   1181  CA  ALA A 143      11.256 -39.342   5.252  1.00 13.66           C  
-ANISOU 1181  CA  ALA A 143     1580   1908   1703   -152    147   -215       C  
-ATOM   1182  C   ALA A 143      10.717 -40.512   6.079  1.00 14.94           C  
-ANISOU 1182  C   ALA A 143     1763   2037   1875   -152    137   -248       C  
-ATOM   1183  O   ALA A 143      11.360 -41.556   6.172  1.00 10.45           O  
-ANISOU 1183  O   ALA A 143     1196   1439   1335   -153    152   -287       O  
-ATOM   1184  CB  ALA A 143      11.864 -38.281   6.165  1.00 11.33           C  
-ANISOU 1184  CB  ALA A 143     1286   1568   1451   -127    124   -177       C  
-ATOM   1185  N   LEU A 144       9.536 -40.350   6.681  1.00 12.32           N  
-ANISOU 1185  N   LEU A 144     1448   1709   1525   -149    116   -228       N  
-ATOM   1186  CA  LEU A 144       8.990 -41.416   7.518  1.00 11.38           C  
-ANISOU 1186  CA  LEU A 144     1349   1558   1419   -146    107   -254       C  
-ATOM   1187  C   LEU A 144       8.525 -42.629   6.704  1.00 16.13           C  
-ANISOU 1187  C   LEU A 144     1946   2189   1993   -175    129   -298       C  
-ATOM   1188  O   LEU A 144       8.819 -43.773   7.056  1.00 14.52           O  
-ANISOU 1188  O   LEU A 144     1749   1949   1818   -175    138   -337       O  
-ATOM   1189  CB  LEU A 144       7.879 -40.906   8.440  1.00 10.75           C  
-ANISOU 1189  CB  LEU A 144     1286   1469   1329   -132     82   -218       C  
-ATOM   1190  CG  LEU A 144       8.342 -39.991   9.582  1.00 11.83           C  
-ANISOU 1190  CG  LEU A 144     1437   1559   1500   -103     60   -188       C  
-ATOM   1191  CD1 LEU A 144       7.128 -39.512  10.385  1.00 14.17           C  
-ANISOU 1191  CD1 LEU A 144     1754   1851   1781    -90     43   -155       C  
-ATOM   1192  CD2 LEU A 144       9.362 -40.705  10.486  1.00 13.43           C  
-ANISOU 1192  CD2 LEU A 144     1648   1702   1752    -88     52   -212       C  
-ATOM   1193  N   ASP A 145       7.819 -42.406   5.606  1.00 13.85           N  
-ANISOU 1193  N   ASP A 145     1647   1966   1650   -201    138   -294       N  
-ATOM   1194  CA  ASP A 145       7.465 -43.553   4.785  1.00 18.17           C  
-ANISOU 1194  CA  ASP A 145     2193   2541   2168   -233    158   -343       C  
-ATOM   1195  C   ASP A 145       8.721 -44.283   4.316  1.00 19.38           C  
-ANISOU 1195  C   ASP A 145     2343   2673   2349   -237    190   -390       C  
-ATOM   1196  O   ASP A 145       8.752 -45.516   4.275  1.00 15.27           O  
-ANISOU 1196  O   ASP A 145     1829   2132   1842   -249    208   -439       O  
-ATOM   1197  CB  ASP A 145       6.656 -43.160   3.568  1.00 15.59           C  
-ANISOU 1197  CB  ASP A 145     1854   2295   1774   -264    161   -331       C  
-ATOM   1198  CG  ASP A 145       6.184 -44.376   2.800  1.00 27.73           C  
-ANISOU 1198  CG  ASP A 145     3396   3861   3280   -303    177   -386       C  
-ATOM   1199  OD1 ASP A 145       5.660 -45.311   3.449  1.00 22.16           O  
-ANISOU 1199  OD1 ASP A 145     2703   3122   2595   -305    171   -410       O  
-ATOM   1200  OD2 ASP A 145       6.373 -44.413   1.570  1.00 27.69           O  
-ANISOU 1200  OD2 ASP A 145     3382   3909   3230   -330    198   -406       O  
-ATOM   1201  N   TYR A 146       9.754 -43.528   3.944  1.00 16.75           N  
-ANISOU 1201  N   TYR A 146     1996   2343   2027   -226    201   -373       N  
-ATOM   1202  CA  TYR A 146      10.993 -44.173   3.526  1.00 15.93           C  
-ANISOU 1202  CA  TYR A 146     1885   2215   1954   -225    236   -411       C  
-ATOM   1203  C   TYR A 146      11.571 -45.081   4.617  1.00 15.23           C  
-ANISOU 1203  C   TYR A 146     1804   2051   1933   -205    235   -433       C  
-ATOM   1204  O   TYR A 146      11.769 -46.276   4.388  1.00 15.96           O  
-ANISOU 1204  O   TYR A 146     1899   2125   2040   -217    263   -482       O  
-ATOM   1205  CB  TYR A 146      12.038 -43.165   3.034  1.00 13.74           C  
-ANISOU 1205  CB  TYR A 146     1587   1948   1685   -213    247   -382       C  
-ATOM   1206  CG  TYR A 146      13.252 -43.866   2.464  1.00 13.07           C  
-ANISOU 1206  CG  TYR A 146     1492   1844   1628   -215    289   -421       C  
-ATOM   1207  CD1 TYR A 146      13.171 -44.535   1.243  1.00 19.16           C  
-ANISOU 1207  CD1 TYR A 146     2265   2659   2356   -244    327   -465       C  
-ATOM   1208  CD2 TYR A 146      14.465 -43.884   3.144  1.00 14.64           C  
-ANISOU 1208  CD2 TYR A 146     1681   1983   1897   -188    291   -413       C  
-ATOM   1209  CE1 TYR A 146      14.263 -45.194   0.711  1.00 21.98           C  
-ANISOU 1209  CE1 TYR A 146     2615   2996   2740   -243    373   -501       C  
-ATOM   1210  CE2 TYR A 146      15.573 -44.544   2.610  1.00 18.44           C  
-ANISOU 1210  CE2 TYR A 146     2151   2445   2411   -187    334   -443       C  
-ATOM   1211  CZ  TYR A 146      15.457 -45.195   1.390  1.00 22.28           C  
-ANISOU 1211  CZ  TYR A 146     2641   2972   2854   -214    378   -488       C  
-ATOM   1212  OH  TYR A 146      16.522 -45.857   0.828  1.00 22.86           O  
-ANISOU 1212  OH  TYR A 146     2704   3025   2958   -212    428   -521       O  
-ATOM   1213  N   CYS A 147      11.832 -44.546   5.808  1.00 16.57           N  
-ANISOU 1213  N   CYS A 147     1977   2177   2144   -176    204   -397       N  
-ATOM   1214  CA  CYS A 147      12.454 -45.388   6.826  1.00 15.40           C  
-ANISOU 1214  CA  CYS A 147     1832   1961   2058   -157    202   -411       C  
-ATOM   1215  C   CYS A 147      11.556 -46.558   7.244  1.00 15.69           C  
-ANISOU 1215  C   CYS A 147     1884   1982   2095   -166    202   -441       C  
-ATOM   1216  O   CYS A 147      12.034 -47.682   7.390  1.00 14.85           O  
-ANISOU 1216  O   CYS A 147     1775   1838   2029   -165    225   -475       O  
-ATOM   1217  CB  CYS A 147      13.008 -44.592   8.018  1.00 16.91           C  
-ANISOU 1217  CB  CYS A 147     2025   2110   2290   -128    167   -368       C  
-ATOM   1218  SG  CYS A 147      11.806 -43.821   9.129  1.00 14.85           S  
-ANISOU 1218  SG  CYS A 147     1788   1848   2006   -115    122   -328       S  
-ATOM   1219  N   HIS A 148      10.253 -46.313   7.380  1.00 11.14           N  
-ANISOU 1219  N   HIS A 148     1321   1436   1477   -175    181   -427       N  
-ATOM   1220  CA  HIS A 148       9.321 -47.409   7.652  1.00 12.23           C  
-ANISOU 1220  CA  HIS A 148     1470   1565   1613   -187    182   -453       C  
-ATOM   1221  C   HIS A 148       9.364 -48.475   6.543  1.00 12.35           C  
-ANISOU 1221  C   HIS A 148     1480   1597   1615   -219    221   -512       C  
-ATOM   1222  O   HIS A 148       9.404 -49.674   6.823  1.00 18.03           O  
-ANISOU 1222  O   HIS A 148     2202   2278   2370   -222    238   -547       O  
-ATOM   1223  CB  HIS A 148       7.896 -46.880   7.835  1.00 12.31           C  
-ANISOU 1223  CB  HIS A 148     1490   1610   1579   -193    155   -423       C  
-ATOM   1224  CG  HIS A 148       7.739 -45.949   8.997  1.00 12.14           C  
-ANISOU 1224  CG  HIS A 148     1479   1565   1571   -162    122   -372       C  
-ATOM   1225  ND1 HIS A 148       6.604 -45.192   9.194  1.00 12.53           N  
-ANISOU 1225  ND1 HIS A 148     1535   1642   1584   -161    102   -334       N  
-ATOM   1226  CD2 HIS A 148       8.572 -45.655  10.026  1.00 13.72           C  
-ANISOU 1226  CD2 HIS A 148     1683   1715   1814   -133    108   -353       C  
-ATOM   1227  CE1 HIS A 148       6.743 -44.475  10.296  1.00 17.68           C  
-ANISOU 1227  CE1 HIS A 148     2200   2262   2258   -131     79   -298       C  
-ATOM   1228  NE2 HIS A 148       7.933 -44.726  10.810  1.00 16.70           N  
-ANISOU 1228  NE2 HIS A 148     2075   2092   2178   -115     80   -310       N  
-ATOM   1229  N   SER A 149       9.385 -48.047   5.285  1.00 17.95           N  
-ANISOU 1229  N   SER A 149     2182   2363   2274   -243    238   -522       N  
-ATOM   1230  CA  SER A 149       9.414 -48.999   4.167  1.00 14.90           C  
-ANISOU 1230  CA  SER A 149     1797   1999   1866   -277    277   -582       C  
-ATOM   1231  C   SER A 149      10.722 -49.777   4.188  1.00 14.78           C  
-ANISOU 1231  C   SER A 149     1775   1930   1910   -264    315   -616       C  
-ATOM   1232  O   SER A 149      10.831 -50.864   3.608  1.00 14.99           O  
-ANISOU 1232  O   SER A 149     1806   1947   1942   -285    353   -672       O  
-ATOM   1233  CB  SER A 149       9.262 -48.279   2.821  1.00 19.65           C  
-ANISOU 1233  CB  SER A 149     2392   2677   2396   -303    287   -580       C  
-ATOM   1234  OG  SER A 149      10.431 -47.536   2.487  1.00 18.10           O  
-ANISOU 1234  OG  SER A 149     2182   2482   2213   -286    302   -562       O  
-ATOM   1235  N   MET A 150      11.709 -49.215   4.875  1.00 15.91           N  
-ANISOU 1235  N   MET A 150     1908   2037   2101   -230    306   -581       N  
-ATOM   1236  CA AMET A 150      13.019 -49.846   4.968  1.00 16.51           C  
-ANISOU 1236  CA AMET A 150     1972   2060   2241   -214    340   -600       C  
-ATOM   1237  CA BMET A 150      13.028 -49.828   4.985  0.00 17.16           C  
-ANISOU 1237  CA BMET A 150     2054   2142   2324   -214    340   -599       C  
-ATOM   1238  C   MET A 150      13.207 -50.571   6.303  1.00 20.08           C  
-ANISOU 1238  C   MET A 150     2424   2442   2763   -189    327   -592       C  
-ATOM   1239  O   MET A 150      14.330 -50.894   6.690  1.00 20.12           O  
-ANISOU 1239  O   MET A 150     2415   2400   2831   -168    343   -588       O  
-ATOM   1240  CB AMET A 150      14.111 -48.788   4.739  1.00 15.94           C  
-ANISOU 1240  CB AMET A 150     1883   1995   2180   -197    341   -565       C  
-ATOM   1241  CB BMET A 150      14.120 -48.767   4.829  0.00 16.51           C  
-ANISOU 1241  CB BMET A 150     1955   2064   2255   -195    339   -562       C  
-ATOM   1242  CG AMET A 150      14.020 -48.152   3.335  1.00 17.08           C  
-ANISOU 1242  CG AMET A 150     2023   2208   2257   -220    362   -572       C  
-ATOM   1243  CG BMET A 150      14.348 -48.356   3.385  0.00 16.72           C  
-ANISOU 1243  CG BMET A 150     1974   2147   2230   -216    371   -578       C  
-ATOM   1244  SD AMET A 150      14.813 -49.218   2.078  1.00 22.26           S  
-ANISOU 1244  SD AMET A 150     2676   2865   2916   -240    435   -639       S  
-ATOM   1245  SD BMET A 150      14.886 -49.761   2.393  0.00 22.35           S  
-ANISOU 1245  SD BMET A 150     2690   2848   2954   -236    441   -652       S  
-ATOM   1246  CE AMET A 150      16.541 -48.929   2.507  1.00 20.02           C  
-ANISOU 1246  CE AMET A 150     2365   2525   2715   -202    451   -608       C  
-ATOM   1247  CE BMET A 150      14.897 -49.055   0.749  0.00 22.77           C  
-ANISOU 1247  CE BMET A 150     2742   2985   2926   -263    469   -662       C  
-ATOM   1248  N   GLY A 151      12.099 -50.832   6.992  1.00 16.45           N  
-ANISOU 1248  N   GLY A 151     1978   1980   2292   -192    299   -586       N  
-ATOM   1249  CA  GLY A 151      12.109 -51.622   8.215  1.00 16.97           C  
-ANISOU 1249  CA  GLY A 151     2045   1985   2416   -171    288   -579       C  
-ATOM   1250  C   GLY A 151      12.600 -50.939   9.481  1.00 17.90           C  
-ANISOU 1250  C   GLY A 151     2160   2071   2568   -136    249   -524       C  
-ATOM   1251  O   GLY A 151      13.004 -51.595  10.436  1.00 15.22           O  
-ANISOU 1251  O   GLY A 151     1817   1680   2287   -116    245   -516       O  
-ATOM   1252  N   ILE A 152      12.548 -49.617   9.502  1.00 15.74           N  
-ANISOU 1252  N   ILE A 152     1891   1830   2261   -130    220   -487       N  
-ATOM   1253  CA  ILE A 152      13.138 -48.868  10.603  1.00  9.20           C  
-ANISOU 1253  CA  ILE A 152     1062    972   1461   -102    183   -440       C  
-ATOM   1254  C   ILE A 152      12.165 -47.861  11.186  1.00 15.13           C  
-ANISOU 1254  C   ILE A 152     1833   1746   2170    -96    143   -404       C  
-ATOM   1255  O   ILE A 152      11.490 -47.139  10.455  1.00 15.32           O  
-ANISOU 1255  O   ILE A 152     1861   1819   2140   -111    142   -399       O  
-ATOM   1256  CB  ILE A 152      14.417 -48.150  10.118  1.00 15.76           C  
-ANISOU 1256  CB  ILE A 152     1873   1804   2310    -96    192   -428       C  
-ATOM   1257  CG1 ILE A 152      15.510 -49.191   9.804  1.00 15.32           C  
-ANISOU 1257  CG1 ILE A 152     1796   1713   2314    -94    233   -455       C  
-ATOM   1258  CG2 ILE A 152      14.858 -47.078  11.129  1.00 12.81           C  
-ANISOU 1258  CG2 ILE A 152     1502   1413   1951    -74    147   -378       C  
-ATOM   1259  CD1 ILE A 152      16.546 -48.713   8.811  1.00 21.51           C  
-ANISOU 1259  CD1 ILE A 152     2559   2511   3102    -98    261   -457       C  
-ATOM   1260  N   MET A 153      12.094 -47.818  12.514  1.00 10.93           N  
-ANISOU 1260  N   MET A 153     1313   1179   1661    -73    111   -376       N  
-ATOM   1261  CA  MET A 153      11.347 -46.769  13.187  1.00 13.52           C  
-ANISOU 1261  CA  MET A 153     1662   1520   1954    -63     76   -340       C  
-ATOM   1262  C   MET A 153      12.308 -45.759  13.812  1.00 14.47           C  
-ANISOU 1262  C   MET A 153     1782   1620   2094    -46     48   -308       C  
-ATOM   1263  O   MET A 153      13.354 -46.128  14.353  1.00 13.67           O  
-ANISOU 1263  O   MET A 153     1671   1482   2042    -34     43   -304       O  
-ATOM   1264  CB  MET A 153      10.367 -47.338  14.220  1.00 22.03           C  
-ANISOU 1264  CB  MET A 153     2760   2579   3032    -52     61   -331       C  
-ATOM   1265  CG  MET A 153      10.887 -48.463  15.062  1.00 22.27           C  
-ANISOU 1265  CG  MET A 153     2785   2560   3116    -38     63   -338       C  
-ATOM   1266  SD  MET A 153       9.599 -49.211  16.102  1.00 19.07           S  
-ANISOU 1266  SD  MET A 153     2399   2139   2707    -27     52   -328       S  
-ATOM   1267  CE  MET A 153      10.502 -50.655  16.656  1.00 16.75           C  
-ANISOU 1267  CE  MET A 153     2087   1791   2486    -16     67   -341       C  
-ATOM   1268  N   HIS A 154      11.954 -44.482  13.720  1.00 11.92           N  
-ANISOU 1268  N   HIS A 154     1470   1323   1736    -45     32   -282       N  
-ATOM   1269  CA  HIS A 154      12.844 -43.426  14.182  1.00 12.51           C  
-ANISOU 1269  CA  HIS A 154     1545   1381   1828    -34      7   -255       C  
-ATOM   1270  C   HIS A 154      12.829 -43.338  15.711  1.00 17.35           C  
-ANISOU 1270  C   HIS A 154     2182   1955   2455    -15    -30   -235       C  
-ATOM   1271  O   HIS A 154      13.884 -43.313  16.342  1.00 14.50           O  
-ANISOU 1271  O   HIS A 154     1815   1562   2132     -6    -49   -225       O  
-ATOM   1272  CB  HIS A 154      12.468 -42.089  13.536  1.00 13.29           C  
-ANISOU 1272  CB  HIS A 154     1645   1515   1888    -41      5   -235       C  
-ATOM   1273  CG  HIS A 154      13.413 -40.975  13.865  1.00 13.72           C  
-ANISOU 1273  CG  HIS A 154     1697   1553   1964    -33    -17   -210       C  
-ATOM   1274  ND1 HIS A 154      13.393 -40.326  15.079  1.00 12.40           N  
-ANISOU 1274  ND1 HIS A 154     1555   1355   1801    -19    -52   -189       N  
-ATOM   1275  CD2 HIS A 154      14.407 -40.398  13.146  1.00 14.06           C  
-ANISOU 1275  CD2 HIS A 154     1715   1601   2025    -39     -9   -204       C  
-ATOM   1276  CE1 HIS A 154      14.334 -39.397  15.096  1.00 10.88           C  
-ANISOU 1276  CE1 HIS A 154     1353   1150   1630    -19    -67   -172       C  
-ATOM   1277  NE2 HIS A 154      14.963 -39.417  13.936  1.00  9.44           N  
-ANISOU 1277  NE2 HIS A 154     1138    989   1459    -30    -41   -179       N  
-ATOM   1278  N   ARG A 155      11.624 -43.304  16.285  1.00 14.40           N  
-ANISOU 1278  N   ARG A 155     1835   1587   2050     -8    -38   -226       N  
-ATOM   1279  CA  ARG A 155      11.394 -43.304  17.744  1.00 11.74           C  
-ANISOU 1279  CA  ARG A 155     1526   1217   1715     11    -67   -208       C  
-ATOM   1280  C   ARG A 155      11.813 -42.032  18.495  1.00 11.12           C  
-ANISOU 1280  C   ARG A 155     1469   1124   1632     20   -100   -183       C  
-ATOM   1281  O   ARG A 155      11.818 -42.007  19.724  1.00 14.32           O  
-ANISOU 1281  O   ARG A 155     1899   1502   2038     34   -126   -171       O  
-ATOM   1282  CB  ARG A 155      11.978 -44.553  18.438  1.00  9.72           C  
-ANISOU 1282  CB  ARG A 155     1263    928   1503     20    -71   -216       C  
-ATOM   1283  CG  ARG A 155      11.563 -45.892  17.800  1.00 12.71           C  
-ANISOU 1283  CG  ARG A 155     1623   1312   1893     11    -37   -244       C  
-ATOM   1284  CD  ARG A 155      11.858 -47.089  18.722  1.00 10.60           C  
-ANISOU 1284  CD  ARG A 155     1353   1008   1669     24    -40   -243       C  
-ATOM   1285  NE  ARG A 155      13.268 -47.150  19.119  1.00 12.13           N  
-ANISOU 1285  NE  ARG A 155     1528   1172   1908     30    -56   -233       N  
-ATOM   1286  CZ  ARG A 155      13.792 -48.056  19.948  1.00 16.69           C  
-ANISOU 1286  CZ  ARG A 155     2096   1716   2529     42    -63   -223       C  
-ATOM   1287  NH1 ARG A 155      13.029 -48.995  20.501  1.00 12.23           N  
-ANISOU 1287  NH1 ARG A 155     1539   1140   1968     51    -56   -223       N  
-ATOM   1288  NH2 ARG A 155      15.096 -48.012  20.239  1.00 13.85           N  
-ANISOU 1288  NH2 ARG A 155     1716   1335   2212     46    -79   -208       N  
-ATOM   1289  N   ASP A 156      12.134 -40.970  17.771  1.00 13.28           N  
-ANISOU 1289  N   ASP A 156     1734   1415   1898     12    -97   -177       N  
-ATOM   1290  CA  ASP A 156      12.465 -39.714  18.440  1.00  8.89           C  
-ANISOU 1290  CA  ASP A 156     1198    841   1339     17   -125   -156       C  
-ATOM   1291  C   ASP A 156      12.108 -38.554  17.536  1.00 11.31           C  
-ANISOU 1291  C   ASP A 156     1499   1176   1623     10   -111   -144       C  
-ATOM   1292  O   ASP A 156      12.850 -37.582  17.427  1.00 13.86           O  
-ANISOU 1292  O   ASP A 156     1815   1490   1960      6   -122   -133       O  
-ATOM   1293  CB  ASP A 156      13.953 -39.679  18.823  1.00 10.43           C  
-ANISOU 1293  CB  ASP A 156     1378   1007   1578     15   -150   -154       C  
-ATOM   1294  CG  ASP A 156      14.268 -38.609  19.858  1.00 16.50           C  
-ANISOU 1294  CG  ASP A 156     2176   1749   2343     19   -188   -138       C  
-ATOM   1295  OD1 ASP A 156      13.337 -38.125  20.552  1.00 13.46           O  
-ANISOU 1295  OD1 ASP A 156     1830   1361   1923     29   -194   -131       O  
-ATOM   1296  OD2 ASP A 156      15.461 -38.269  19.990  1.00 17.62           O  
-ANISOU 1296  OD2 ASP A 156     2303   1873   2518     12   -211   -132       O  
-ATOM   1297  N   VAL A 157      10.956 -38.668  16.877  1.00 12.85           N  
-ANISOU 1297  N   VAL A 157     1693   1406   1785      7    -85   -143       N  
-ATOM   1298  CA  VAL A 157      10.463 -37.579  16.050  1.00 11.54           C  
-ANISOU 1298  CA  VAL A 157     1520   1271   1596      1    -71   -124       C  
-ATOM   1299  C   VAL A 157      10.029 -36.429  16.970  1.00 16.56           C  
-ANISOU 1299  C   VAL A 157     2189   1883   2220     15    -87   -101       C  
-ATOM   1300  O   VAL A 157       9.233 -36.625  17.894  1.00 14.25           O  
-ANISOU 1300  O   VAL A 157     1928   1575   1912     29    -92    -97       O  
-ATOM   1301  CB  VAL A 157       9.280 -38.042  15.153  1.00 13.30           C  
-ANISOU 1301  CB  VAL A 157     1731   1539   1784     -8    -43   -125       C  
-ATOM   1302  CG1 VAL A 157       8.639 -36.848  14.452  1.00 12.02           C  
-ANISOU 1302  CG1 VAL A 157     1562   1409   1597    -11    -31    -95       C  
-ATOM   1303  CG2 VAL A 157       9.743 -39.081  14.133  1.00 14.95           C  
-ANISOU 1303  CG2 VAL A 157     1908   1771   2000    -26    -24   -154       C  
-ATOM   1304  N   LYS A 158      10.572 -35.242  16.722  1.00 10.05           N  
-ANISOU 1304  N   LYS A 158     1359   1053   1406     12    -91    -85       N  
-ATOM   1305  CA  LYS A 158      10.285 -34.036  17.497  1.00 11.22           C  
-ANISOU 1305  CA  LYS A 158     1539   1175   1550     23   -102    -66       C  
-ATOM   1306  C   LYS A 158      10.892 -32.866  16.729  1.00 15.25           C  
-ANISOU 1306  C   LYS A 158     2026   1690   2077     14    -96    -49       C  
-ATOM   1307  O   LYS A 158      11.758 -33.074  15.870  1.00 10.97           O  
-ANISOU 1307  O   LYS A 158     1449   1164   1555      2    -92    -55       O  
-ATOM   1308  CB  LYS A 158      10.896 -34.128  18.910  1.00 10.10           C  
-ANISOU 1308  CB  LYS A 158     1432    986   1422     30   -136    -79       C  
-ATOM   1309  CG  LYS A 158      12.418 -34.210  18.932  1.00 14.66           C  
-ANISOU 1309  CG  LYS A 158     1989   1543   2038     19   -161    -89       C  
-ATOM   1310  CD  LYS A 158      12.933 -34.388  20.350  1.00 13.63           C  
-ANISOU 1310  CD  LYS A 158     1890   1372   1915     23   -199    -98       C  
-ATOM   1311  CE  LYS A 158      14.451 -34.454  20.379  1.00 13.01           C  
-ANISOU 1311  CE  LYS A 158     1788   1276   1880     10   -227   -103       C  
-ATOM   1312  NZ  LYS A 158      14.956 -34.412  21.806  1.00 20.64           N  
-ANISOU 1312  NZ  LYS A 158     2787   2205   2848     10   -270   -107       N  
-ATOM   1313  N   PRO A 159      10.437 -31.633  17.014  1.00 14.30           N  
-ANISOU 1313  N   PRO A 159     1926   1556   1953     22    -92    -27       N  
-ATOM   1314  CA  PRO A 159      10.897 -30.457  16.271  1.00 14.87           C  
-ANISOU 1314  CA  PRO A 159     1975   1632   2045     15    -83     -5       C  
-ATOM   1315  C   PRO A 159      12.424 -30.373  16.146  1.00 15.21           C  
-ANISOU 1315  C   PRO A 159     1996   1656   2127      2   -104    -16       C  
-ATOM   1316  O   PRO A 159      12.932 -30.092  15.064  1.00 13.78           O  
-ANISOU 1316  O   PRO A 159     1775   1500   1961     -7    -89     -4       O  
-ATOM   1317  CB  PRO A 159      10.351 -29.296  17.099  1.00 17.02           C  
-ANISOU 1317  CB  PRO A 159     2284   1869   2315     27    -83     10       C  
-ATOM   1318  CG  PRO A 159       9.043 -29.840  17.639  1.00 14.16           C  
-ANISOU 1318  CG  PRO A 159     1949   1513   1917     42    -71     11       C  
-ATOM   1319  CD  PRO A 159       9.361 -31.287  17.972  1.00 15.38           C  
-ANISOU 1319  CD  PRO A 159     2105   1672   2066     39    -89    -19       C  
-ATOM   1320  N   HIS A 160      13.145 -30.617  17.232  1.00 15.98           N  
-ANISOU 1320  N   HIS A 160     2117   1713   2242      2   -138    -36       N  
-ATOM   1321  CA  HIS A 160      14.604 -30.509  17.168  1.00 15.65           C  
-ANISOU 1321  CA  HIS A 160     2052   1652   2243    -11   -161    -41       C  
-ATOM   1322  C   HIS A 160      15.214 -31.430  16.119  1.00 16.29           C  
-ANISOU 1322  C   HIS A 160     2087   1765   2338    -19   -145    -46       C  
-ATOM   1323  O   HIS A 160      16.220 -31.087  15.495  1.00 19.06           O  
-ANISOU 1323  O   HIS A 160     2404   2116   2723    -28   -145    -37       O  
-ATOM   1324  CB  HIS A 160      15.234 -30.779  18.525  1.00 12.87           C  
-ANISOU 1324  CB  HIS A 160     1730   1256   1903    -13   -204    -59       C  
-ATOM   1325  CG  HIS A 160      16.734 -30.748  18.499  1.00 21.38           C  
-ANISOU 1325  CG  HIS A 160     2780   2315   3028    -27   -231    -59       C  
-ATOM   1326  ND1 HIS A 160      17.465 -29.655  18.913  1.00 27.93           N  
-ANISOU 1326  ND1 HIS A 160     3616   3111   3886    -38   -257    -52       N  
-ATOM   1327  CD2 HIS A 160      17.636 -31.672  18.094  1.00 23.52           C  
-ANISOU 1327  CD2 HIS A 160     3014   2595   3327    -33   -234    -64       C  
-ATOM   1328  CE1 HIS A 160      18.754 -29.911  18.774  1.00 28.54           C  
-ANISOU 1328  CE1 HIS A 160     3660   3179   4007    -51   -278    -50       C  
-ATOM   1329  NE2 HIS A 160      18.886 -31.129  18.282  1.00 25.70           N  
-ANISOU 1329  NE2 HIS A 160     3272   2843   3648    -46   -263    -56       N  
-ATOM   1330  N   ASN A 161      14.605 -32.593  15.903  1.00 15.14           N  
-ANISOU 1330  N   ASN A 161     1941   1646   2168    -15   -130    -61       N  
-ATOM   1331  CA  ASN A 161      15.190 -33.579  14.979  1.00 13.20           C  
-ANISOU 1331  CA  ASN A 161     1656   1425   1934    -22   -112    -73       C  
-ATOM   1332  C   ASN A 161      14.753 -33.427  13.523  1.00 14.47           C  
-ANISOU 1332  C   ASN A 161     1787   1637   2073    -29    -73    -63       C  
-ATOM   1333  O   ASN A 161      15.113 -34.228  12.663  1.00 14.47           O  
-ANISOU 1333  O   ASN A 161     1760   1663   2075    -36    -52    -77       O  
-ATOM   1334  CB  ASN A 161      14.914 -34.997  15.473  1.00  9.02           C  
-ANISOU 1334  CB  ASN A 161     1139    893   1397    -18   -114    -98       C  
-ATOM   1335  CG  ASN A 161      15.740 -35.340  16.688  1.00 11.33           C  
-ANISOU 1335  CG  ASN A 161     1446   1141   1720    -15   -151   -105       C  
-ATOM   1336  OD1 ASN A 161      16.776 -34.708  16.932  1.00 14.17           O  
-ANISOU 1336  OD1 ASN A 161     1796   1476   2113    -20   -175    -95       O  
-ATOM   1337  ND2 ASN A 161      15.303 -36.329  17.455  1.00 12.48           N  
-ANISOU 1337  ND2 ASN A 161     1611   1277   1854     -7   -159   -118       N  
-ATOM   1338  N   VAL A 162      13.958 -32.406  13.244  1.00 12.18           N  
-ANISOU 1338  N   VAL A 162     1503   1363   1761    -27    -62    -39       N  
-ATOM   1339  CA  VAL A 162      13.563 -32.140  11.866  1.00 13.50           C  
-ANISOU 1339  CA  VAL A 162     1640   1584   1906    -34    -29    -21       C  
-ATOM   1340  C   VAL A 162      14.177 -30.822  11.454  1.00 20.08           C  
-ANISOU 1340  C   VAL A 162     2453   2412   2765    -36    -26     10       C  
-ATOM   1341  O   VAL A 162      13.610 -29.757  11.727  1.00 25.06           O  
-ANISOU 1341  O   VAL A 162     3097   3032   3393    -29    -27     35       O  
-ATOM   1342  CB  VAL A 162      12.022 -32.045  11.726  1.00 17.56           C  
-ANISOU 1342  CB  VAL A 162     2168   2130   2373    -30    -14     -7       C  
-ATOM   1343  CG1 VAL A 162      11.635 -31.684  10.289  1.00 15.46           C  
-ANISOU 1343  CG1 VAL A 162     1868   1925   2082    -41     16     17       C  
-ATOM   1344  CG2 VAL A 162      11.378 -33.355  12.126  1.00 15.58           C  
-ANISOU 1344  CG2 VAL A 162     1935   1884   2100    -30    -16    -36       C  
-ATOM   1345  N   MET A 163      15.332 -30.891  10.796  1.00 13.91           N  
-ANISOU 1345  N   MET A 163     1637   1633   2013    -43    -20      9       N  
-ATOM   1346  CA  MET A 163      16.071 -29.698  10.415  1.00 11.33           C  
-ANISOU 1346  CA  MET A 163     1287   1298   1721    -45    -18     39       C  
-ATOM   1347  C   MET A 163      15.541 -29.122   9.116  1.00 16.36           C  
-ANISOU 1347  C   MET A 163     1894   1989   2331    -48     17     71       C  
-ATOM   1348  O   MET A 163      15.379 -29.836   8.129  1.00 18.29           O  
-ANISOU 1348  O   MET A 163     2120   2284   2546    -55     42     63       O  
-ATOM   1349  CB  MET A 163      17.565 -29.991  10.292  1.00 15.54           C  
-ANISOU 1349  CB  MET A 163     1793   1809   2302    -50    -26     31       C  
-ATOM   1350  CG  MET A 163      18.112 -30.646  11.532  1.00 19.96           C  
-ANISOU 1350  CG  MET A 163     2376   2320   2887    -49    -62      5       C  
-ATOM   1351  SD  MET A 163      19.863 -30.348  11.670  1.00 25.32           S  
-ANISOU 1351  SD  MET A 163     3024   2960   3638    -56    -83     15       S  
-ATOM   1352  CE  MET A 163      19.861 -28.569  11.719  1.00 19.94           C  
-ANISOU 1352  CE  MET A 163     2342   2259   2976    -58    -92     51       C  
-ATOM   1353  N   ILE A 164      15.275 -27.821   9.125  1.00 17.72           N  
-ANISOU 1353  N   ILE A 164     2065   2153   2515    -43     19    107       N  
-ATOM   1354  CA  ILE A 164      14.683 -27.161   7.971  1.00 19.38           C  
-ANISOU 1354  CA  ILE A 164     2246   2416   2701    -45     50    147       C  
-ATOM   1355  C   ILE A 164      15.505 -25.963   7.518  1.00 23.77           C  
-ANISOU 1355  C   ILE A 164     2770   2959   3301    -44     58    184       C  
-ATOM   1356  O   ILE A 164      15.735 -25.021   8.284  1.00 23.42           O  
-ANISOU 1356  O   ILE A 164     2739   2862   3296    -40     41    196       O  
-ATOM   1357  CB  ILE A 164      13.259 -26.675   8.287  1.00 18.16           C  
-ANISOU 1357  CB  ILE A 164     2113   2269   2516    -36     55    168       C  
-ATOM   1358  CG1 ILE A 164      12.343 -27.858   8.580  1.00 17.33           C  
-ANISOU 1358  CG1 ILE A 164     2034   2185   2367    -38     51    138       C  
-ATOM   1359  CG2 ILE A 164      12.705 -25.841   7.146  1.00 23.44           C  
-ANISOU 1359  CG2 ILE A 164     2747   2990   3168    -37     85    220       C  
-ATOM   1360  CD1 ILE A 164      10.974 -27.438   9.130  1.00 23.01           C  
-ANISOU 1360  CD1 ILE A 164     2778   2901   3064    -27     53    158       C  
-ATOM   1361  N   ASP A 165      15.961 -26.022   6.273  1.00 17.35           N  
-ANISOU 1361  N   ASP A 165     1917   2194   2483    -51     84    202       N  
-ATOM   1362  CA  ASP A 165      16.530 -24.869   5.607  1.00 22.07           C  
-ANISOU 1362  CA  ASP A 165     2477   2794   3114    -49    100    248       C  
-ATOM   1363  C   ASP A 165      15.374 -24.153   4.926  1.00 25.66           C  
-ANISOU 1363  C   ASP A 165     2920   3297   3535    -46    125    293       C  
-ATOM   1364  O   ASP A 165      14.928 -24.542   3.851  1.00 25.26           O  
-ANISOU 1364  O   ASP A 165     2847   3315   3435    -52    149    305       O  
-ATOM   1365  CB  ASP A 165      17.592 -25.289   4.585  1.00 25.30           C  
-ANISOU 1365  CB  ASP A 165     2847   3233   3532    -56    121    248       C  
-ATOM   1366  CG  ASP A 165      18.216 -24.103   3.872  1.00 29.53           C  
-ANISOU 1366  CG  ASP A 165     3340   3772   4106    -53    139    300       C  
-ATOM   1367  OD1 ASP A 165      17.567 -23.037   3.798  1.00 31.11           O  
-ANISOU 1367  OD1 ASP A 165     3535   3975   4309    -48    146    341       O  
-ATOM   1368  OD2 ASP A 165      19.356 -24.237   3.389  1.00 31.96           O  
-ANISOU 1368  OD2 ASP A 165     3619   4079   4445    -56    149    302       O  
-ATOM   1369  N   HIS A 166      14.895 -23.104   5.574  1.00 23.93           N  
-ANISOU 1369  N   HIS A 166     2714   3040   3340    -37    118    319       N  
-ATOM   1370  CA  HIS A 166      13.725 -22.377   5.107  1.00 21.26           C  
-ANISOU 1370  CA  HIS A 166     2364   2736   2977    -31    141    367       C  
-ATOM   1371  C   HIS A 166      14.007 -21.559   3.843  1.00 26.37           C  
-ANISOU 1371  C   HIS A 166     2958   3428   3633    -31    171    425       C  
-ATOM   1372  O   HIS A 166      13.080 -21.183   3.127  1.00 29.81           O  
-ANISOU 1372  O   HIS A 166     3374   3917   4037    -30    193    470       O  
-ATOM   1373  CB  HIS A 166      13.202 -21.477   6.233  1.00 18.53           C  
-ANISOU 1373  CB  HIS A 166     2051   2327   2663    -18    130    377       C  
-ATOM   1374  CG  HIS A 166      11.777 -21.053   6.060  1.00 22.64           C  
-ANISOU 1374  CG  HIS A 166     2571   2877   3153     -9    151    416       C  
-ATOM   1375  ND1 HIS A 166      10.802 -21.896   5.571  1.00 23.89           N  
-ANISOU 1375  ND1 HIS A 166     2729   3099   3251    -14    157    416       N  
-ATOM   1376  CD2 HIS A 166      11.157 -19.880   6.334  1.00 25.06           C  
-ANISOU 1376  CD2 HIS A 166     2878   3155   3487      4    166    460       C  
-ATOM   1377  CE1 HIS A 166       9.645 -21.260   5.548  1.00 24.81           C  
-ANISOU 1377  CE1 HIS A 166     2841   3227   3357     -4    174    461       C  
-ATOM   1378  NE2 HIS A 166       9.832 -20.034   6.001  1.00 26.08           N  
-ANISOU 1378  NE2 HIS A 166     3004   3333   3573      8    183    489       N  
-ATOM   1379  N   GLU A 167      15.278 -21.282   3.567  1.00 25.68           N  
-ANISOU 1379  N   GLU A 167     2846   3321   3590    -34    172    428       N  
-ATOM   1380  CA  GLU A 167      15.637 -20.567   2.344  1.00 27.70           C  
-ANISOU 1380  CA  GLU A 167     3049   3620   3854    -34    203    484       C  
-ATOM   1381  C   GLU A 167      15.410 -21.417   1.098  1.00 31.17           C  
-ANISOU 1381  C   GLU A 167     3466   4150   4226    -44    225    485       C  
-ATOM   1382  O   GLU A 167      14.751 -20.984   0.152  1.00 31.17           O  
-ANISOU 1382  O   GLU A 167     3437   4212   4193    -44    250    535       O  
-ATOM   1383  CB  GLU A 167      17.088 -20.072   2.396  1.00 34.72           C  
-ANISOU 1383  CB  GLU A 167     3915   4462   4813    -34    199    488       C  
-ATOM   1384  CG  GLU A 167      17.542 -19.360   1.126  1.00 45.22           C  
-ANISOU 1384  CG  GLU A 167     5189   5837   6156    -32    233    548       C  
-ATOM   1385  CD  GLU A 167      18.980 -18.868   1.207  1.00 55.68           C  
-ANISOU 1385  CD  GLU A 167     6489   7112   7556    -32    229    555       C  
-ATOM   1386  OE1 GLU A 167      19.626 -19.064   2.259  1.00 55.80           O  
-ANISOU 1386  OE1 GLU A 167     6530   7058   7613    -36    196    514       O  
-ATOM   1387  OE2 GLU A 167      19.465 -18.282   0.216  1.00 61.72           O  
-ANISOU 1387  OE2 GLU A 167     7206   7907   8339    -29    258    605       O  
-ATOM   1388  N   HIS A 168      15.945 -22.633   1.099  1.00 32.98           N  
-ANISOU 1388  N   HIS A 168     3709   4385   4435    -52    218    430       N  
-ATOM   1389  CA  HIS A 168      15.806 -23.523  -0.051  1.00 31.81           C  
-ANISOU 1389  CA  HIS A 168     3547   4318   4223    -64    241    419       C  
-ATOM   1390  C   HIS A 168      14.678 -24.531   0.122  1.00 29.42           C  
-ANISOU 1390  C   HIS A 168     3276   4047   3856    -74    231    383       C  
-ATOM   1391  O   HIS A 168      14.554 -25.464  -0.668  1.00 28.61           O  
-ANISOU 1391  O   HIS A 168     3171   4002   3698    -88    245    359       O  
-ATOM   1392  CB  HIS A 168      17.111 -24.266  -0.307  1.00 31.94           C  
-ANISOU 1392  CB  HIS A 168     3554   4323   4257    -68    248    383       C  
-ATOM   1393  CG  HIS A 168      18.295 -23.362  -0.463  1.00 35.89           C  
-ANISOU 1393  CG  HIS A 168     4020   4790   4826    -60    257    418       C  
-ATOM   1394  ND1 HIS A 168      18.507 -22.604  -1.594  1.00 36.99           N  
-ANISOU 1394  ND1 HIS A 168     4115   4977   4964    -58    289    475       N  
-ATOM   1395  CD2 HIS A 168      19.326 -23.092   0.372  1.00 38.98           C  
-ANISOU 1395  CD2 HIS A 168     4413   5106   5291    -55    236    408       C  
-ATOM   1396  CE1 HIS A 168      19.622 -21.908  -1.451  1.00 42.46           C  
-ANISOU 1396  CE1 HIS A 168     4783   5622   5729    -50    289    498       C  
-ATOM   1397  NE2 HIS A 168      20.139 -22.186  -0.267  1.00 42.60           N  
-ANISOU 1397  NE2 HIS A 168     4828   5565   5794    -50    256    457       N  
-ATOM   1398  N   ARG A 169      13.870 -24.345   1.162  1.00 22.57           N  
-ANISOU 1398  N   ARG A 169     2440   3140   2996    -67    208    379       N  
-ATOM   1399  CA  ARG A 169      12.726 -25.212   1.413  1.00 24.39           C  
-ANISOU 1399  CA  ARG A 169     2698   3395   3173    -74    198    351       C  
-ATOM   1400  C   ARG A 169      13.147 -26.674   1.487  1.00 25.91           C  
-ANISOU 1400  C   ARG A 169     2912   3589   3344    -86    192    283       C  
-ATOM   1401  O   ARG A 169      12.495 -27.546   0.911  1.00 30.85           O  
-ANISOU 1401  O   ARG A 169     3542   4270   3911   -101    199    263       O  
-ATOM   1402  CB  ARG A 169      11.678 -25.043   0.307  1.00 28.73           C  
-ANISOU 1402  CB  ARG A 169     3223   4032   3662    -85    217    395       C  
-ATOM   1403  CG  ARG A 169      11.495 -23.610  -0.180  1.00 36.09           C  
-ANISOU 1403  CG  ARG A 169     4118   4978   4615    -75    234    473       C  
-ATOM   1404  CD  ARG A 169      10.464 -22.862   0.632  1.00 41.23           C  
-ANISOU 1404  CD  ARG A 169     4782   5596   5285    -61    226    505       C  
-ATOM   1405  NE  ARG A 169       9.157 -23.518   0.621  1.00 45.50           N  
-ANISOU 1405  NE  ARG A 169     5338   6181   5770    -70    219    501       N  
-ATOM   1406  CZ  ARG A 169       8.135 -23.140   1.385  1.00 42.51           C  
-ANISOU 1406  CZ  ARG A 169     4976   5775   5401    -58    213    522       C  
-ATOM   1407  NH1 ARG A 169       8.278 -22.109   2.209  1.00 43.44           N  
-ANISOU 1407  NH1 ARG A 169     5104   5823   5580    -37    215    543       N  
-ATOM   1408  NH2 ARG A 169       6.980 -23.787   1.337  1.00 35.17           N  
-ANISOU 1408  NH2 ARG A 169     4055   4886   4422    -67    207    520       N  
-ATOM   1409  N   LYS A 170      14.229 -26.933   2.213  1.00 22.91           N  
-ANISOU 1409  N   LYS A 170     2544   3146   3014    -79    178    250       N  
-ATOM   1410  CA  LYS A 170      14.824 -28.261   2.299  1.00 28.35           C  
-ANISOU 1410  CA  LYS A 170     3247   3828   3698    -87    177    191       C  
-ATOM   1411  C   LYS A 170      14.737 -28.810   3.729  1.00 24.85           C  
-ANISOU 1411  C   LYS A 170     2844   3319   3279    -80    144    152       C  
-ATOM   1412  O   LYS A 170      14.959 -28.085   4.699  1.00 22.26           O  
-ANISOU 1412  O   LYS A 170     2529   2933   2995    -68    122    164       O  
-ATOM   1413  CB  LYS A 170      16.286 -28.186   1.844  1.00 29.58           C  
-ANISOU 1413  CB  LYS A 170     3375   3970   3896    -85    192    191       C  
-ATOM   1414  CG  LYS A 170      17.041 -29.505   1.885  1.00 39.56           C  
-ANISOU 1414  CG  LYS A 170     4647   5220   5165    -90    197    136       C  
-ATOM   1415  CD  LYS A 170      18.475 -29.358   1.350  1.00 45.79           C  
-ANISOU 1415  CD  LYS A 170     5403   5998   5998    -87    217    145       C  
-ATOM   1416  CE  LYS A 170      19.434 -28.787   2.395  1.00 43.65           C  
-ANISOU 1416  CE  LYS A 170     5129   5648   5805    -75    188    155       C  
-ATOM   1417  NZ  LYS A 170      20.823 -28.675   1.862  1.00 45.77           N  
-ANISOU 1417  NZ  LYS A 170     5362   5907   6122    -72    208    168       N  
-ATOM   1418  N   LEU A 171      14.432 -30.095   3.857  1.00 16.14           N  
-ANISOU 1418  N   LEU A 171     1760   2224   2146    -88    142    105       N  
-ATOM   1419  CA  LEU A 171      14.193 -30.683   5.171  1.00 17.78           C  
-ANISOU 1419  CA  LEU A 171     2006   2380   2370    -81    114     73       C  
-ATOM   1420  C   LEU A 171      14.986 -31.973   5.361  1.00 19.01           C  
-ANISOU 1420  C   LEU A 171     2168   2514   2542    -85    114     22       C  
-ATOM   1421  O   LEU A 171      15.107 -32.769   4.428  1.00 17.55           O  
-ANISOU 1421  O   LEU A 171     1969   2369   2329    -97    140      0       O  
-ATOM   1422  CB  LEU A 171      12.689 -30.964   5.327  1.00 14.16           C  
-ANISOU 1422  CB  LEU A 171     1568   1949   1862    -84    110     73       C  
-ATOM   1423  CG  LEU A 171      12.188 -31.498   6.668  1.00 21.01           C  
-ANISOU 1423  CG  LEU A 171     2476   2769   2738    -75     84     47       C  
-ATOM   1424  CD1 LEU A 171      10.774 -30.977   6.939  1.00 18.92           C  
-ANISOU 1424  CD1 LEU A 171     2225   2520   2445    -70     81     77       C  
-ATOM   1425  CD2 LEU A 171      12.236 -33.022   6.671  1.00 17.94           C  
-ANISOU 1425  CD2 LEU A 171     2097   2384   2334    -84     86     -4       C  
-ATOM   1426  N   ARG A 172      15.530 -32.175   6.565  1.00 15.49           N  
-ANISOU 1426  N   ARG A 172     1741   2005   2140    -75     86      5       N  
-ATOM   1427  CA  ARG A 172      16.263 -33.398   6.882  1.00  8.69           C  
-ANISOU 1427  CA  ARG A 172      884   1117   1301    -76     85    -36       C  
-ATOM   1428  C   ARG A 172      15.857 -33.940   8.252  1.00  9.85           C  
-ANISOU 1428  C   ARG A 172     1067   1219   1456    -68     53    -57       C  
-ATOM   1429  O   ARG A 172      15.859 -33.202   9.249  1.00 14.38           O  
-ANISOU 1429  O   ARG A 172     1659   1754   2052    -59     24    -40       O  
-ATOM   1430  CB  ARG A 172      17.791 -33.164   6.859  1.00 12.87           C  
-ANISOU 1430  CB  ARG A 172     1387   1613   1890    -72     85    -28       C  
-ATOM   1431  CG  ARG A 172      18.349 -32.738   5.490  1.00 12.76           C  
-ANISOU 1431  CG  ARG A 172     1335   1641   1872    -78    121     -8       C  
-ATOM   1432  CD  ARG A 172      18.351 -33.886   4.507  1.00 16.06           C  
-ANISOU 1432  CD  ARG A 172     1744   2100   2257    -88    159    -41       C  
-ATOM   1433  NE  ARG A 172      18.917 -33.507   3.211  1.00 17.01           N  
-ANISOU 1433  NE  ARG A 172     1831   2262   2370    -92    196    -22       N  
-ATOM   1434  CZ  ARG A 172      18.201 -33.106   2.164  1.00 24.72           C  
-ANISOU 1434  CZ  ARG A 172     2799   3304   3291   -102    218     -5       C  
-ATOM   1435  NH1 ARG A 172      16.877 -33.016   2.241  1.00 20.57           N  
-ANISOU 1435  NH1 ARG A 172     2293   2809   2715   -109    206     -2       N  
-ATOM   1436  NH2 ARG A 172      18.808 -32.791   1.031  1.00 28.67           N  
-ANISOU 1436  NH2 ARG A 172     3268   3841   3785   -105    253     13       N  
-ATOM   1437  N   LEU A 173      15.525 -35.229   8.306  1.00 10.07           N  
-ANISOU 1437  N   LEU A 173     1106   1253   1468    -72     61    -93       N  
-ATOM   1438  CA  LEU A 173      15.258 -35.898   9.578  1.00 10.24           C  
-ANISOU 1438  CA  LEU A 173     1157   1232   1501    -64     35   -112       C  
-ATOM   1439  C   LEU A 173      16.592 -36.409  10.147  1.00 13.44           C  
-ANISOU 1439  C   LEU A 173     1552   1590   1963    -58     22   -124       C  
-ATOM   1440  O   LEU A 173      17.284 -37.206   9.507  1.00 15.81           O  
-ANISOU 1440  O   LEU A 173     1831   1896   2280    -63     48   -143       O  
-ATOM   1441  CB  LEU A 173      14.293 -37.065   9.377  1.00 10.25           C  
-ANISOU 1441  CB  LEU A 173     1170   1258   1465    -71     49   -142       C  
-ATOM   1442  CG  LEU A 173      13.771 -37.860  10.581  1.00 16.27           C  
-ANISOU 1442  CG  LEU A 173     1963   1986   2232    -62     28   -159       C  
-ATOM   1443  CD1 LEU A 173      13.079 -36.961  11.620  1.00 16.89           C  
-ANISOU 1443  CD1 LEU A 173     2070   2045   2303    -49     -1   -132       C  
-ATOM   1444  CD2 LEU A 173      12.817 -38.962  10.116  1.00 16.63           C  
-ANISOU 1444  CD2 LEU A 173     2013   2063   2243    -74     48   -187       C  
-ATOM   1445  N   ILE A 174      16.933 -35.962  11.350  1.00 13.88           N  
-ANISOU 1445  N   ILE A 174     1625   1600   2048    -49    -15   -112       N  
-ATOM   1446  CA  ILE A 174      18.231 -36.271  11.936  1.00 16.84           C  
-ANISOU 1446  CA  ILE A 174     1987   1932   2479    -46    -34   -114       C  
-ATOM   1447  C   ILE A 174      18.133 -37.093  13.221  1.00 16.21           C  
-ANISOU 1447  C   ILE A 174     1933   1816   2410    -38    -62   -128       C  
-ATOM   1448  O   ILE A 174      17.030 -37.453  13.662  1.00 15.92           O  
-ANISOU 1448  O   ILE A 174     1925   1786   2338    -34    -65   -138       O  
-ATOM   1449  CB  ILE A 174      18.991 -34.981  12.265  1.00 15.01           C  
-ANISOU 1449  CB  ILE A 174     1748   1675   2279    -46    -60    -84       C  
-ATOM   1450  CG1 ILE A 174      18.254 -34.179  13.346  1.00 13.87           C  
-ANISOU 1450  CG1 ILE A 174     1644   1510   2116    -41    -94    -74       C  
-ATOM   1451  CG2 ILE A 174      19.207 -34.142  10.997  1.00 14.38           C  
-ANISOU 1451  CG2 ILE A 174     1638   1629   2196    -52    -31    -63       C  
-ATOM   1452  CD1 ILE A 174      19.139 -33.101  14.005  1.00 17.54           C  
-ANISOU 1452  CD1 ILE A 174     2109   1935   2620    -44   -129    -54       C  
-ATOM   1453  N   ASP A 175      19.303 -37.373  13.799  1.00 13.87           N  
-ANISOU 1453  N   ASP A 175     1621   1482   2165    -36    -83   -123       N  
-ATOM   1454  CA  ASP A 175      19.466 -38.091  15.068  1.00 15.55           C  
-ANISOU 1454  CA  ASP A 175     1851   1659   2397    -29   -115   -128       C  
-ATOM   1455  C   ASP A 175      18.743 -39.432  15.112  1.00 11.90           C  
-ANISOU 1455  C   ASP A 175     1399   1205   1918    -24    -94   -154       C  
-ATOM   1456  O   ASP A 175      17.702 -39.577  15.760  1.00 14.24           O  
-ANISOU 1456  O   ASP A 175     1728   1503   2179    -18   -104   -159       O  
-ATOM   1457  CB  ASP A 175      19.065 -37.238  16.271  1.00 13.77           C  
-ANISOU 1457  CB  ASP A 175     1665   1414   2155    -26   -159   -116       C  
-ATOM   1458  CG  ASP A 175      19.668 -37.758  17.577  1.00 18.09           C  
-ANISOU 1458  CG  ASP A 175     2222   1923   2729    -22   -200   -112       C  
-ATOM   1459  OD1 ASP A 175      19.685 -37.009  18.566  1.00 25.06           O  
-ANISOU 1459  OD1 ASP A 175     3132   2784   3604    -24   -240   -102       O  
-ATOM   1460  OD2 ASP A 175      20.138 -38.913  17.612  1.00 17.02           O  
-ANISOU 1460  OD2 ASP A 175     2066   1779   2624    -19   -191   -118       O  
-ATOM   1461  N   TRP A 176      19.340 -40.404  14.436  1.00 10.44           N  
-ANISOU 1461  N   TRP A 176     1183   1021   1762    -26    -62   -168       N  
-ATOM   1462  CA  TRP A 176      18.835 -41.764  14.373  1.00 12.13           C  
-ANISOU 1462  CA  TRP A 176     1400   1236   1972    -23    -36   -195       C  
-ATOM   1463  C   TRP A 176      19.374 -42.616  15.510  1.00 14.74           C  
-ANISOU 1463  C   TRP A 176     1729   1526   2347    -13    -59   -189       C  
-ATOM   1464  O   TRP A 176      19.362 -43.848  15.441  1.00 16.33           O  
-ANISOU 1464  O   TRP A 176     1920   1716   2568     -9    -34   -207       O  
-ATOM   1465  CB  TRP A 176      19.167 -42.350  12.996  1.00  9.25           C  
-ANISOU 1465  CB  TRP A 176     1006    893   1616    -31     17   -217       C  
-ATOM   1466  CG  TRP A 176      18.482 -41.546  11.946  1.00 14.39           C  
-ANISOU 1466  CG  TRP A 176     1661   1592   2215    -42     36   -220       C  
-ATOM   1467  CD1 TRP A 176      18.866 -40.318  11.460  1.00 17.23           C  
-ANISOU 1467  CD1 TRP A 176     2010   1968   2571    -46     31   -196       C  
-ATOM   1468  CD2 TRP A 176      17.227 -41.849  11.323  1.00 15.90           C  
-ANISOU 1468  CD2 TRP A 176     1868   1822   2350    -52     58   -242       C  
-ATOM   1469  NE1 TRP A 176      17.936 -39.867  10.542  1.00 14.24           N  
-ANISOU 1469  NE1 TRP A 176     1636   1637   2136    -56     52   -200       N  
-ATOM   1470  CE2 TRP A 176      16.926 -40.788  10.441  1.00 14.83           C  
-ANISOU 1470  CE2 TRP A 176     1728   1728   2178    -61     67   -228       C  
-ATOM   1471  CE3 TRP A 176      16.346 -42.931  11.400  1.00 14.06           C  
-ANISOU 1471  CE3 TRP A 176     1650   1594   2099    -56     72   -270       C  
-ATOM   1472  CZ2 TRP A 176      15.770 -40.775   9.649  1.00 13.45           C  
-ANISOU 1472  CZ2 TRP A 176     1562   1602   1944    -74     86   -239       C  
-ATOM   1473  CZ3 TRP A 176      15.193 -42.915  10.614  1.00 18.70           C  
-ANISOU 1473  CZ3 TRP A 176     2247   2227   2629    -70     89   -284       C  
-ATOM   1474  CH2 TRP A 176      14.921 -41.848   9.750  1.00 17.10           C  
-ANISOU 1474  CH2 TRP A 176     2039   2069   2388    -80     95   -268       C  
-ATOM   1475  N   GLY A 177      19.826 -41.949  16.570  1.00 17.31           N  
-ANISOU 1475  N   GLY A 177     2065   1827   2685     -9   -107   -163       N  
-ATOM   1476  CA  GLY A 177      20.432 -42.618  17.708  1.00 16.98           C  
-ANISOU 1476  CA  GLY A 177     2019   1750   2683     -1   -137   -148       C  
-ATOM   1477  C   GLY A 177      19.475 -43.454  18.545  1.00 18.84           C  
-ANISOU 1477  C   GLY A 177     2283   1980   2896      9   -143   -157       C  
-ATOM   1478  O   GLY A 177      19.911 -44.324  19.301  1.00 18.10           O  
-ANISOU 1478  O   GLY A 177     2179   1861   2837     18   -155   -147       O  
-ATOM   1479  N   LEU A 178      18.176 -43.188  18.429  1.00 17.53           N  
-ANISOU 1479  N   LEU A 178     2149   1837   2673      9   -134   -171       N  
-ATOM   1480  CA  LEU A 178      17.176 -44.027  19.082  1.00 14.17           C  
-ANISOU 1480  CA  LEU A 178     1747   1409   2228     19   -132   -178       C  
-ATOM   1481  C   LEU A 178      16.451 -44.951  18.098  1.00 16.85           C  
-ANISOU 1481  C   LEU A 178     2077   1767   2559     14    -83   -208       C  
-ATOM   1482  O   LEU A 178      15.591 -45.722  18.500  1.00 16.89           O  
-ANISOU 1482  O   LEU A 178     2096   1769   2551     20    -76   -216       O  
-ATOM   1483  CB  LEU A 178      16.140 -43.183  19.843  1.00 12.31           C  
-ANISOU 1483  CB  LEU A 178     1557   1181   1938     24   -158   -169       C  
-ATOM   1484  CG  LEU A 178      16.645 -42.387  21.050  1.00 20.05           C  
-ANISOU 1484  CG  LEU A 178     2560   2140   2918     28   -208   -146       C  
-ATOM   1485  CD1 LEU A 178      15.481 -41.717  21.790  1.00 20.05           C  
-ANISOU 1485  CD1 LEU A 178     2609   2146   2864     36   -222   -141       C  
-ATOM   1486  CD2 LEU A 178      17.422 -43.291  21.978  1.00 26.37           C  
-ANISOU 1486  CD2 LEU A 178     3347   2913   3759     35   -231   -132       C  
-ATOM   1487  N   ALA A 179      16.798 -44.873  16.817  1.00 17.60           N  
-ANISOU 1487  N   ALA A 179     2148   1882   2659      2    -49   -225       N  
-ATOM   1488  CA  ALA A 179      16.089 -45.653  15.801  1.00 14.08           C  
-ANISOU 1488  CA  ALA A 179     1696   1460   2196     -8     -4   -258       C  
-ATOM   1489  C   ALA A 179      16.336 -47.147  15.967  1.00 18.29           C  
-ANISOU 1489  C   ALA A 179     2213   1963   2773     -3     19   -275       C  
-ATOM   1490  O   ALA A 179      17.405 -47.553  16.434  1.00 16.14           O  
-ANISOU 1490  O   ALA A 179     1919   1658   2556      6     13   -261       O  
-ATOM   1491  CB  ALA A 179      16.472 -45.189  14.394  1.00 12.10           C  
-ANISOU 1491  CB  ALA A 179     1424   1238   1935    -23     26   -271       C  
-ATOM   1492  N   GLU A 180      15.346 -47.962  15.602  1.00 12.77           N  
-ANISOU 1492  N   GLU A 180     1522   1276   2054    -10     46   -303       N  
-ATOM   1493  CA  GLU A 180      15.467 -49.428  15.702  1.00 16.10           C  
-ANISOU 1493  CA  GLU A 180     1929   1668   2521     -7     74   -322       C  
-ATOM   1494  C   GLU A 180      14.892 -50.126  14.483  1.00 16.88           C  
-ANISOU 1494  C   GLU A 180     2023   1787   2602    -28    121   -368       C  
-ATOM   1495  O   GLU A 180      14.079 -49.555  13.758  1.00 20.07           O  
-ANISOU 1495  O   GLU A 180     2441   2235   2951    -44    124   -380       O  
-ATOM   1496  CB  GLU A 180      14.714 -49.965  16.919  1.00 17.20           C  
-ANISOU 1496  CB  GLU A 180     2087   1786   2661      7     51   -307       C  
-ATOM   1497  CG  GLU A 180      15.579 -50.424  18.072  1.00 20.57           C  
-ANISOU 1497  CG  GLU A 180     2502   2172   3143     26     30   -277       C  
-ATOM   1498  CD  GLU A 180      16.343 -51.715  17.797  1.00 22.60           C  
-ANISOU 1498  CD  GLU A 180     2724   2394   3468     29     68   -291       C  
-ATOM   1499  OE1 GLU A 180      16.844 -52.301  18.774  1.00 27.51           O  
-ANISOU 1499  OE1 GLU A 180     3334   2982   4137     45     54   -263       O  
-ATOM   1500  OE2 GLU A 180      16.467 -52.142  16.629  1.00 21.15           O  
-ANISOU 1500  OE2 GLU A 180     2526   2217   3293     14    114   -327       O  
-ATOM   1501  N   PHE A 181      15.294 -51.378  14.284  1.00 15.58           N  
-ANISOU 1501  N   PHE A 181     1840   1592   2487    -28    158   -392       N  
-ATOM   1502  CA  PHE A 181      14.721 -52.217  13.242  1.00 14.19           C  
-ANISOU 1502  CA  PHE A 181     1663   1429   2298    -50    203   -442       C  
-ATOM   1503  C   PHE A 181      13.410 -52.827  13.748  1.00 14.12           C  
-ANISOU 1503  C   PHE A 181     1673   1420   2271    -54    195   -449       C  
-ATOM   1504  O   PHE A 181      13.343 -53.300  14.885  1.00 18.49           O  
-ANISOU 1504  O   PHE A 181     2228   1939   2858    -34    177   -425       O  
-ATOM   1505  CB  PHE A 181      15.702 -53.333  12.877  1.00 20.31           C  
-ANISOU 1505  CB  PHE A 181     2412   2165   3141    -48    251   -467       C  
-ATOM   1506  CG  PHE A 181      16.925 -52.851  12.149  1.00 15.72           C  
-ANISOU 1506  CG  PHE A 181     1810   1587   2578    -48    271   -465       C  
-ATOM   1507  CD1 PHE A 181      16.944 -52.809  10.760  1.00 14.82           C  
-ANISOU 1507  CD1 PHE A 181     1694   1503   2432    -70    313   -505       C  
-ATOM   1508  CD2 PHE A 181      18.051 -52.441  12.851  1.00 16.40           C  
-ANISOU 1508  CD2 PHE A 181     1875   1645   2711    -27    248   -422       C  
-ATOM   1509  CE1 PHE A 181      18.073 -52.365  10.077  1.00 18.59           C  
-ANISOU 1509  CE1 PHE A 181     2151   1985   2928    -68    335   -501       C  
-ATOM   1510  CE2 PHE A 181      19.184 -51.995  12.181  1.00 19.46           C  
-ANISOU 1510  CE2 PHE A 181     2239   2034   3120    -26    267   -416       C  
-ATOM   1511  CZ  PHE A 181      19.190 -51.964  10.783  1.00 17.85           C  
-ANISOU 1511  CZ  PHE A 181     2034   1860   2886    -45    313   -455       C  
-ATOM   1512  N   TYR A 182      12.377 -52.812  12.909  1.00 15.91           N  
-ANISOU 1512  N   TYR A 182     1913   1686   2445    -79    207   -479       N  
-ATOM   1513  CA  TYR A 182      11.121 -53.453  13.270  1.00 15.25           C  
-ANISOU 1513  CA  TYR A 182     1844   1602   2349    -85    203   -486       C  
-ATOM   1514  C   TYR A 182      11.122 -54.933  12.900  1.00 17.20           C  
-ANISOU 1514  C   TYR A 182     2078   1817   2639    -98    247   -531       C  
-ATOM   1515  O   TYR A 182      11.323 -55.307  11.737  1.00 16.00           O  
-ANISOU 1515  O   TYR A 182     1921   1678   2480   -123    285   -577       O  
-ATOM   1516  CB  TYR A 182       9.887 -52.753  12.672  1.00 18.00           C  
-ANISOU 1516  CB  TYR A 182     2209   2007   2623   -107    189   -489       C  
-ATOM   1517  CG  TYR A 182       8.618 -53.520  13.013  1.00 16.76           C  
-ANISOU 1517  CG  TYR A 182     2061   1846   2461   -115    187   -496       C  
-ATOM   1518  CD1 TYR A 182       8.076 -53.478  14.293  1.00 18.70           C  
-ANISOU 1518  CD1 TYR A 182     2317   2071   2716    -90    158   -456       C  
-ATOM   1519  CD2 TYR A 182       8.008 -54.340  12.076  1.00 19.91           C  
-ANISOU 1519  CD2 TYR A 182     2457   2260   2847   -148    216   -543       C  
-ATOM   1520  CE1 TYR A 182       6.926 -54.212  14.616  1.00 18.94           C  
-ANISOU 1520  CE1 TYR A 182     2353   2096   2748    -96    159   -459       C  
-ATOM   1521  CE2 TYR A 182       6.873 -55.068  12.388  1.00 19.00           C  
-ANISOU 1521  CE2 TYR A 182     2347   2139   2734   -157    213   -549       C  
-ATOM   1522  CZ  TYR A 182       6.342 -55.009  13.656  1.00 15.86           C  
-ANISOU 1522  CZ  TYR A 182     1956   1719   2350   -130    186   -505       C  
-ATOM   1523  OH  TYR A 182       5.210 -55.755  13.948  1.00 16.36           O  
-ANISOU 1523  OH  TYR A 182     2022   1775   2420   -139    186   -507       O  
-ATOM   1524  N   HIS A 183      10.895 -55.764  13.913  1.00 13.33           N  
-ANISOU 1524  N   HIS A 183     1586   1284   2194    -81    242   -517       N  
-ATOM   1525  CA  HIS A 183      10.777 -57.203  13.740  1.00 16.68           C  
-ANISOU 1525  CA  HIS A 183     1999   1671   2668    -91    282   -554       C  
-ATOM   1526  C   HIS A 183       9.438 -57.638  14.349  1.00 17.75           C  
-ANISOU 1526  C   HIS A 183     2146   1805   2792    -93    266   -545       C  
-ATOM   1527  O   HIS A 183       9.170 -57.366  15.526  1.00 19.91           O  
-ANISOU 1527  O   HIS A 183     2427   2068   3070    -67    232   -497       O  
-ATOM   1528  CB  HIS A 183      11.932 -57.925  14.429  1.00 19.80           C  
-ANISOU 1528  CB  HIS A 183     2371   2007   3147    -64    299   -537       C  
-ATOM   1529  CG  HIS A 183      13.278 -57.644  13.826  1.00 23.30           C  
-ANISOU 1529  CG  HIS A 183     2796   2444   3612    -61    321   -544       C  
-ATOM   1530  ND1 HIS A 183      13.671 -58.154  12.606  1.00 26.13           N  
-ANISOU 1530  ND1 HIS A 183     3148   2802   3980    -83    374   -598       N  
-ATOM   1531  CD2 HIS A 183      14.328 -56.924  14.288  1.00 23.44           C  
-ANISOU 1531  CD2 HIS A 183     2802   2455   3648    -39    299   -503       C  
-ATOM   1532  CE1 HIS A 183      14.900 -57.750  12.338  1.00 26.26           C  
-ANISOU 1532  CE1 HIS A 183     3147   2811   4020    -72    386   -586       C  
-ATOM   1533  NE2 HIS A 183      15.323 -57.004  13.343  1.00 23.62           N  
-ANISOU 1533  NE2 HIS A 183     2807   2473   3693    -46    339   -529       N  
-ATOM   1534  N   PRO A 184       8.596 -58.312  13.555  1.00 18.36           N  
-ANISOU 1534  N   PRO A 184     2228   1894   2855   -126    290   -591       N  
-ATOM   1535  CA  PRO A 184       7.261 -58.658  14.067  1.00 20.60           C  
-ANISOU 1535  CA  PRO A 184     2519   2180   3127   -130    273   -579       C  
-ATOM   1536  C   PRO A 184       7.382 -59.436  15.373  1.00 19.16           C  
-ANISOU 1536  C   PRO A 184     2327   1942   3011    -98    270   -545       C  
-ATOM   1537  O   PRO A 184       8.157 -60.394  15.429  1.00 17.53           O  
-ANISOU 1537  O   PRO A 184     2102   1687   2872    -92    304   -562       O  
-ATOM   1538  CB  PRO A 184       6.688 -59.564  12.972  1.00 21.55           C  
-ANISOU 1538  CB  PRO A 184     2638   2306   3243   -173    308   -643       C  
-ATOM   1539  CG  PRO A 184       7.460 -59.235  11.744  1.00 27.23           C  
-ANISOU 1539  CG  PRO A 184     3358   3052   3937   -194    333   -683       C  
-ATOM   1540  CD  PRO A 184       8.839 -58.861  12.209  1.00 20.53           C  
-ANISOU 1540  CD  PRO A 184     2498   2176   3126   -160    335   -655       C  
-ATOM   1541  N   GLY A 185       6.657 -59.016  16.406  1.00 20.23           N  
-ANISOU 1541  N   GLY A 185     2474   2084   3130    -77    234   -496       N  
-ATOM   1542  CA  GLY A 185       6.621 -59.738  17.664  1.00 22.19           C  
-ANISOU 1542  CA  GLY A 185     2714   2285   3432    -47    230   -460       C  
-ATOM   1543  C   GLY A 185       7.681 -59.319  18.661  1.00 23.51           C  
-ANISOU 1543  C   GLY A 185     2877   2432   3622    -11    209   -414       C  
-ATOM   1544  O   GLY A 185       7.686 -59.763  19.807  1.00 21.28           O  
-ANISOU 1544  O   GLY A 185     2591   2120   3376     17    199   -374       O  
-ATOM   1545  N   GLN A 186       8.587 -58.453  18.232  1.00 18.73           N  
-ANISOU 1545  N   GLN A 186     2274   1846   2995    -11    201   -416       N  
-ATOM   1546  CA  GLN A 186       9.681 -58.035  19.095  1.00 19.73           C  
-ANISOU 1546  CA  GLN A 186     2395   1956   3145     18    178   -375       C  
-ATOM   1547  C   GLN A 186       9.188 -57.026  20.131  1.00 21.94           C  
-ANISOU 1547  C   GLN A 186     2701   2257   3376     38    130   -326       C  
-ATOM   1548  O   GLN A 186       8.395 -56.136  19.816  1.00 21.24           O  
-ANISOU 1548  O   GLN A 186     2635   2210   3226     28    114   -328       O  
-ATOM   1549  CB  GLN A 186      10.816 -57.448  18.254  1.00 19.54           C  
-ANISOU 1549  CB  GLN A 186     2361   1943   3119      8    186   -393       C  
-ATOM   1550  CG  GLN A 186      12.121 -57.280  19.003  1.00 28.53           C  
-ANISOU 1550  CG  GLN A 186     3484   3055   4300     33    170   -355       C  
-ATOM   1551  CD  GLN A 186      13.309 -57.145  18.062  1.00 33.03           C  
-ANISOU 1551  CD  GLN A 186     4033   3623   4894     24    196   -378       C  
-ATOM   1552  OE1 GLN A 186      13.556 -58.021  17.227  1.00 36.94           O  
-ANISOU 1552  OE1 GLN A 186     4511   4098   5426     10    244   -419       O  
-ATOM   1553  NE2 GLN A 186      14.039 -56.042  18.182  1.00 31.62           N  
-ANISOU 1553  NE2 GLN A 186     3858   3463   4695     30    165   -354       N  
-ATOM   1554  N   GLU A 187       9.638 -57.182  21.371  1.00 18.90           N  
-ANISOU 1554  N   GLU A 187     2313   1846   3020     67    108   -282       N  
-ATOM   1555  CA  GLU A 187       9.313 -56.226  22.420  1.00 20.08           C  
-ANISOU 1555  CA  GLU A 187     2492   2014   3124     86     64   -239       C  
-ATOM   1556  C   GLU A 187      10.428 -55.194  22.529  1.00 21.68           C  
-ANISOU 1556  C   GLU A 187     2698   2225   3313     91     36   -224       C  
-ATOM   1557  O   GLU A 187      11.603 -55.555  22.590  1.00 23.77           O  
-ANISOU 1557  O   GLU A 187     2937   2466   3627     95     39   -218       O  
-ATOM   1558  CB  GLU A 187       9.109 -56.943  23.754  1.00 20.03           C  
-ANISOU 1558  CB  GLU A 187     2484   1978   3147    113     54   -197       C  
-ATOM   1559  CG  GLU A 187       7.947 -57.944  23.721  1.00 24.92           C  
-ANISOU 1559  CG  GLU A 187     3099   2586   3784    110     81   -206       C  
-ATOM   1560  CD  GLU A 187       7.559 -58.446  25.099  1.00 37.68           C  
-ANISOU 1560  CD  GLU A 187     4719   4181   5415    139     68   -157       C  
-ATOM   1561  OE1 GLU A 187       8.460 -58.672  25.935  1.00 39.16           O  
-ANISOU 1561  OE1 GLU A 187     4895   4348   5634    159     54   -124       O  
-ATOM   1562  OE2 GLU A 187       6.348 -58.617  25.345  1.00 41.74           O  
-ANISOU 1562  OE2 GLU A 187     5246   4702   5910    142     73   -149       O  
-ATOM   1563  N   TYR A 188      10.058 -53.914  22.539  1.00 15.11           N  
-ANISOU 1563  N   TYR A 188     1895   1427   2419     88      9   -217       N  
-ATOM   1564  CA  TYR A 188      11.038 -52.823  22.537  1.00 16.20           C  
-ANISOU 1564  CA  TYR A 188     2038   1575   2543     88    -18   -207       C  
-ATOM   1565  C   TYR A 188      11.037 -52.054  23.843  1.00 20.21           C  
-ANISOU 1565  C   TYR A 188     2575   2083   3020    107    -62   -167       C  
-ATOM   1566  O   TYR A 188      10.068 -52.094  24.586  1.00 20.21           O  
-ANISOU 1566  O   TYR A 188     2599   2086   2993    120    -70   -149       O  
-ATOM   1567  CB  TYR A 188      10.774 -51.860  21.379  1.00 20.55           C  
-ANISOU 1567  CB  TYR A 188     2596   2163   3049     67    -11   -233       C  
-ATOM   1568  CG  TYR A 188      10.938 -52.538  20.054  1.00 17.41           C  
-ANISOU 1568  CG  TYR A 188     2172   1769   2675     45     31   -275       C  
-ATOM   1569  CD1 TYR A 188      12.189 -52.652  19.486  1.00 20.03           C  
-ANISOU 1569  CD1 TYR A 188     2478   2088   3045     39     45   -288       C  
-ATOM   1570  CD2 TYR A 188       9.851 -53.117  19.397  1.00 14.15           C  
-ANISOU 1570  CD2 TYR A 188     1760   1369   2247     29     58   -303       C  
-ATOM   1571  CE1 TYR A 188      12.374 -53.289  18.296  1.00 22.63           C  
-ANISOU 1571  CE1 TYR A 188     2786   2418   3393     20     88   -329       C  
-ATOM   1572  CE2 TYR A 188      10.026 -53.767  18.182  1.00 16.03           C  
-ANISOU 1572  CE2 TYR A 188     1978   1611   2503      5     97   -347       C  
-ATOM   1573  CZ  TYR A 188      11.306 -53.845  17.646  1.00 16.47           C  
-ANISOU 1573  CZ  TYR A 188     2011   1654   2593      2    114   -361       C  
-ATOM   1574  OH  TYR A 188      11.541 -54.479  16.454  1.00 20.28           O  
-ANISOU 1574  OH  TYR A 188     2477   2138   3091    -20    157   -407       O  
-ATOM   1575  N   ASN A 189      12.133 -51.353  24.109  1.00 17.19           N  
-ANISOU 1575  N   ASN A 189     2191   1699   2643    108    -91   -152       N  
-ATOM   1576  CA  ASN A 189      12.237 -50.467  25.263  1.00 16.32           C  
-ANISOU 1576  CA  ASN A 189     2113   1591   2498    121   -136   -121       C  
-ATOM   1577  C   ASN A 189      11.219 -49.337  25.126  1.00 13.85           C  
-ANISOU 1577  C   ASN A 189     1837   1305   2119    118   -141   -127       C  
-ATOM   1578  O   ASN A 189      11.091 -48.747  24.054  1.00 19.45           O  
-ANISOU 1578  O   ASN A 189     2543   2035   2813    102   -125   -150       O  
-ATOM   1579  CB  ASN A 189      13.664 -49.901  25.305  1.00 21.42           C  
-ANISOU 1579  CB  ASN A 189     2742   2229   3165    114   -163   -111       C  
-ATOM   1580  CG  ASN A 189      13.932 -49.018  26.518  1.00 29.77           C  
-ANISOU 1580  CG  ASN A 189     3833   3289   4191    122   -214    -82       C  
-ATOM   1581  OD1 ASN A 189      13.101 -48.873  27.414  1.00 21.50           O  
-ANISOU 1581  OD1 ASN A 189     2821   2244   3102    135   -227    -68       O  
-ATOM   1582  ND2 ASN A 189      15.126 -48.436  26.556  1.00 36.70           N  
-ANISOU 1582  ND2 ASN A 189     4697   4161   5085    112   -243    -73       N  
-ATOM   1583  N   VAL A 190      10.485 -49.029  26.191  1.00 16.54           N  
-ANISOU 1583  N   VAL A 190     2215   1647   2423    134   -159   -105       N  
-ATOM   1584  CA  VAL A 190       9.501 -47.942  26.108  1.00 12.06           C  
-ANISOU 1584  CA  VAL A 190     1684   1101   1799    135   -158   -106       C  
-ATOM   1585  C   VAL A 190      10.115 -46.579  26.443  1.00 15.38           C  
-ANISOU 1585  C   VAL A 190     2130   1524   2191    131   -191   -100       C  
-ATOM   1586  O   VAL A 190       9.466 -45.544  26.304  1.00 20.86           O  
-ANISOU 1586  O   VAL A 190     2851   2232   2844    131   -189   -102       O  
-ATOM   1587  CB  VAL A 190       8.233 -48.208  26.976  1.00 15.67           C  
-ANISOU 1587  CB  VAL A 190     2170   1557   2226    155   -152    -87       C  
-ATOM   1588  CG1 VAL A 190       7.517 -49.486  26.524  1.00 17.61           C  
-ANISOU 1588  CG1 VAL A 190     2390   1800   2502    154   -118    -95       C  
-ATOM   1589  CG2 VAL A 190       8.596 -48.271  28.458  1.00 16.86           C  
-ANISOU 1589  CG2 VAL A 190     2345   1691   2369    174   -183    -58       C  
-ATOM   1590  N   ARG A 191      11.381 -46.586  26.864  1.00 16.73           N  
-ANISOU 1590  N   ARG A 191     2288   1680   2389    128   -221    -92       N  
-ATOM   1591  CA  ARG A 191      12.080 -45.351  27.209  1.00 22.31           C  
-ANISOU 1591  CA  ARG A 191     3016   2386   3075    121   -256    -88       C  
-ATOM   1592  C   ARG A 191      12.767 -44.729  25.995  1.00 21.88           C  
-ANISOU 1592  C   ARG A 191     2934   2340   3039    101   -248   -106       C  
-ATOM   1593  O   ARG A 191      14.004 -44.608  25.941  1.00 20.27           O  
-ANISOU 1593  O   ARG A 191     2707   2126   2868     91   -269   -102       O  
-ATOM   1594  CB  ARG A 191      13.085 -45.591  28.343  1.00 23.22           C  
-ANISOU 1594  CB  ARG A 191     3132   2484   3206    124   -298    -65       C  
-ATOM   1595  CG  ARG A 191      12.454 -46.138  29.620  1.00 29.76           C  
-ANISOU 1595  CG  ARG A 191     3990   3307   4011    144   -308    -43       C  
-ATOM   1596  CD  ARG A 191      13.455 -46.172  30.759  1.00 41.24           C  
-ANISOU 1596  CD  ARG A 191     5450   4752   5470    144   -356    -18       C  
-ATOM   1597  NE  ARG A 191      13.795 -44.826  31.209  1.00 51.04           N  
-ANISOU 1597  NE  ARG A 191     6728   5994   6671    133   -392    -22       N  
-ATOM   1598  CZ  ARG A 191      14.845 -44.533  31.970  1.00 59.55           C  
-ANISOU 1598  CZ  ARG A 191     7809   7066   7751    122   -442     -7       C  
-ATOM   1599  NH1 ARG A 191      15.671 -45.493  32.365  1.00 59.53           N  
-ANISOU 1599  NH1 ARG A 191     7771   7058   7790    123   -460     19       N  
-ATOM   1600  NH2 ARG A 191      15.075 -43.278  32.330  1.00 62.27           N  
-ANISOU 1600  NH2 ARG A 191     8191   7410   8058    108   -472    -17       N  
-ATOM   1601  N   VAL A 192      11.943 -44.335  25.029  1.00 17.93           N  
-ANISOU 1601  N   VAL A 192     2435   1860   2518     95   -217   -121       N  
-ATOM   1602  CA  VAL A 192      12.375 -43.648  23.830  1.00 17.11           C  
-ANISOU 1602  CA  VAL A 192     2309   1770   2421     78   -205   -136       C  
-ATOM   1603  C   VAL A 192      11.491 -42.413  23.645  1.00 19.79           C  
-ANISOU 1603  C   VAL A 192     2679   2127   2714     78   -200   -134       C  
-ATOM   1604  O   VAL A 192      10.457 -42.270  24.326  1.00 16.33           O  
-ANISOU 1604  O   VAL A 192     2275   1688   2242     92   -198   -124       O  
-ATOM   1605  CB  VAL A 192      12.229 -44.550  22.583  1.00 13.70           C  
-ANISOU 1605  CB  VAL A 192     1839   1353   2012     69   -165   -156       C  
-ATOM   1606  CG1 VAL A 192      13.139 -45.794  22.691  1.00 12.50           C  
-ANISOU 1606  CG1 VAL A 192     1654   1179   1915     70   -162   -159       C  
-ATOM   1607  CG2 VAL A 192      10.759 -44.966  22.400  1.00 16.11           C  
-ANISOU 1607  CG2 VAL A 192     2158   1676   2289     73   -138   -162       C  
-ATOM   1608  N   ALA A 193      11.899 -41.536  22.725  1.00 19.02           N  
-ANISOU 1608  N   ALA A 193     2566   2041   2618     64   -195   -139       N  
-ATOM   1609  CA  ALA A 193      11.188 -40.292  22.418  1.00 16.89           C  
-ANISOU 1609  CA  ALA A 193     2317   1785   2313     63   -187   -133       C  
-ATOM   1610  C   ALA A 193      11.255 -39.273  23.554  1.00 15.43           C  
-ANISOU 1610  C   ALA A 193     2176   1578   2109     71   -217   -121       C  
-ATOM   1611  O   ALA A 193      11.463 -39.619  24.724  1.00 19.31           O  
-ANISOU 1611  O   ALA A 193     2691   2049   2597     80   -242   -117       O  
-ATOM   1612  CB  ALA A 193       9.720 -40.582  22.037  1.00 18.06           C  
-ANISOU 1612  CB  ALA A 193     2472   1957   2432     69   -155   -131       C  
-ATOM   1613  N   SER A 194      11.107 -38.003  23.210  1.00 13.79           N  
-ANISOU 1613  N   SER A 194     1979   1374   1886     66   -213   -117       N  
-ATOM   1614  CA ASER A 194      11.015 -36.968  24.220  1.00 15.19           C  
-ANISOU 1614  CA ASER A 194     2202   1528   2041     72   -234   -110       C  
-ATOM   1615  CA BSER A 194      11.012 -36.959  24.217  0.00 17.17           C  
-ANISOU 1615  CA BSER A 194     2453   1779   2293     72   -234   -110       C  
-ATOM   1616  C   SER A 194       9.630 -37.015  24.851  1.00 17.31           C  
-ANISOU 1616  C   SER A 194     2508   1797   2271     92   -215   -102       C  
-ATOM   1617  O   SER A 194       8.655 -37.342  24.182  1.00 14.94           O  
-ANISOU 1617  O   SER A 194     2194   1521   1962     97   -183    -96       O  
-ATOM   1618  CB ASER A 194      11.242 -35.596  23.593  1.00 19.69           C  
-ANISOU 1618  CB ASER A 194     2769   2098   2615     62   -229   -106       C  
-ATOM   1619  CB BSER A 194      11.247 -35.583  23.594  0.00 19.96           C  
-ANISOU 1619  CB BSER A 194     2803   2132   2649     62   -229   -106       C  
-ATOM   1620  OG ASER A 194      10.557 -34.596  24.333  1.00 27.84           O  
-ANISOU 1620  OG ASER A 194     3849   3112   3618     72   -228   -100       O  
-ATOM   1621  OG BSER A 194      12.605 -35.405  23.235  0.00 19.92           O  
-ANISOU 1621  OG BSER A 194     2768   2119   2681     45   -251   -111       O  
-ATOM   1622  N   ARG A 195       9.553 -36.690  26.139  1.00 16.00           N  
-ANISOU 1622  N   ARG A 195     2390   1608   2083    103   -235   -100       N  
-ATOM   1623  CA  ARG A 195       8.296 -36.756  26.887  1.00 18.85           C  
-ANISOU 1623  CA  ARG A 195     2790   1965   2407    125   -216    -90       C  
-ATOM   1624  C   ARG A 195       7.057 -36.308  26.103  1.00 13.43           C  
-ANISOU 1624  C   ARG A 195     2098   1297   1708    133   -174    -76       C  
-ATOM   1625  O   ARG A 195       6.065 -37.027  26.056  1.00 13.56           O  
-ANISOU 1625  O   ARG A 195     2110   1327   1714    145   -151    -66       O  
-ATOM   1626  CB  ARG A 195       8.384 -35.945  28.184  1.00 19.55           C  
-ANISOU 1626  CB  ARG A 195     2937   2025   2467    131   -237    -93       C  
-ATOM   1627  CG  ARG A 195       7.106 -35.990  29.023  1.00 19.35           C  
-ANISOU 1627  CG  ARG A 195     2955   1993   2403    157   -213    -81       C  
-ATOM   1628  CD  ARG A 195       7.168 -34.972  30.155  1.00 23.67           C  
-ANISOU 1628  CD  ARG A 195     3565   2512   2918    161   -226    -89       C  
-ATOM   1629  NE  ARG A 195       8.430 -35.070  30.875  1.00 28.80           N  
-ANISOU 1629  NE  ARG A 195     4224   3148   3569    145   -277   -103       N  
-ATOM   1630  CZ  ARG A 195       9.040 -34.049  31.465  1.00 28.67           C  
-ANISOU 1630  CZ  ARG A 195     4245   3108   3541    131   -302   -119       C  
-ATOM   1631  NH1 ARG A 195       8.502 -32.833  31.440  1.00 23.38           N  
-ANISOU 1631  NH1 ARG A 195     3608   2420   2856    135   -277   -124       N  
-ATOM   1632  NH2 ARG A 195      10.188 -34.251  32.091  1.00 34.26           N  
-ANISOU 1632  NH2 ARG A 195     4956   3809   4252    113   -353   -128       N  
-ATOM   1633  N   TYR A 196       7.109 -35.119  25.508  1.00 16.27           N  
-ANISOU 1633  N   TYR A 196     2455   1657   2071    125   -164    -73       N  
-ATOM   1634  CA  TYR A 196       5.908 -34.519  24.903  1.00 15.08           C  
-ANISOU 1634  CA  TYR A 196     2302   1522   1908    135   -125    -52       C  
-ATOM   1635  C   TYR A 196       5.446 -35.275  23.656  1.00 14.31           C  
-ANISOU 1635  C   TYR A 196     2154   1464   1819    126   -104    -44       C  
-ATOM   1636  O   TYR A 196       4.301 -35.118  23.204  1.00 12.73           O  
-ANISOU 1636  O   TYR A 196     1946   1284   1606    134    -74    -23       O  
-ATOM   1637  CB  TYR A 196       6.151 -33.048  24.575  1.00 17.38           C  
-ANISOU 1637  CB  TYR A 196     2599   1799   2204    129   -119    -46       C  
-ATOM   1638  CG  TYR A 196       6.797 -32.313  25.717  1.00 21.19           C  
-ANISOU 1638  CG  TYR A 196     3129   2240   2680    129   -144    -62       C  
-ATOM   1639  CD1 TYR A 196       6.242 -32.350  26.990  1.00 20.98           C  
-ANISOU 1639  CD1 TYR A 196     3157   2191   2623    147   -144    -64       C  
-ATOM   1640  CD2 TYR A 196       7.989 -31.624  25.537  1.00 28.95           C  
-ANISOU 1640  CD2 TYR A 196     4105   3209   3687    109   -170    -74       C  
-ATOM   1641  CE1 TYR A 196       6.841 -31.693  28.048  1.00 24.20           C  
-ANISOU 1641  CE1 TYR A 196     3613   2564   3019    143   -169    -82       C  
-ATOM   1642  CE2 TYR A 196       8.600 -30.965  26.592  1.00 30.64           C  
-ANISOU 1642  CE2 TYR A 196     4363   3385   3893    104   -198    -91       C  
-ATOM   1643  CZ  TYR A 196       8.019 -31.003  27.843  1.00 30.86           C  
-ANISOU 1643  CZ  TYR A 196     4447   3392   3885    120   -198    -97       C  
-ATOM   1644  OH  TYR A 196       8.622 -30.349  28.895  1.00 32.91           O  
-ANISOU 1644  OH  TYR A 196     4756   3618   4132    112   -227   -117       O  
-ATOM   1645  N   PHE A 197       6.313 -36.145  23.150  1.00  9.74           N  
-ANISOU 1645  N   PHE A 197     1541    897   1262    111   -119    -62       N  
-ATOM   1646  CA  PHE A 197       6.071 -36.815  21.877  1.00 16.08           C  
-ANISOU 1646  CA  PHE A 197     2298   1739   2073     97   -101    -64       C  
-ATOM   1647  C   PHE A 197       5.928 -38.330  22.044  1.00 13.97           C  
-ANISOU 1647  C   PHE A 197     2020   1477   1813     98   -101    -76       C  
-ATOM   1648  O   PHE A 197       5.819 -39.057  21.064  1.00 11.77           O  
-ANISOU 1648  O   PHE A 197     1705   1225   1543     84    -87    -85       O  
-ATOM   1649  CB  PHE A 197       7.192 -36.445  20.897  1.00 15.93           C  
-ANISOU 1649  CB  PHE A 197     2245   1731   2077     77   -107    -74       C  
-ATOM   1650  CG  PHE A 197       7.339 -34.967  20.720  1.00 14.48           C  
-ANISOU 1650  CG  PHE A 197     2069   1540   1893     76   -105    -59       C  
-ATOM   1651  CD1 PHE A 197       6.569 -34.297  19.791  1.00 10.51           C  
-ANISOU 1651  CD1 PHE A 197     1549   1066   1379     74    -78    -36       C  
-ATOM   1652  CD2 PHE A 197       8.198 -34.234  21.536  1.00 14.96           C  
-ANISOU 1652  CD2 PHE A 197     2156   1563   1964     77   -131    -65       C  
-ATOM   1653  CE1 PHE A 197       6.665 -32.923  19.640  1.00 16.33           C  
-ANISOU 1653  CE1 PHE A 197     2291   1793   2121     75    -72    -18       C  
-ATOM   1654  CE2 PHE A 197       8.307 -32.865  21.398  1.00 14.59           C  
-ANISOU 1654  CE2 PHE A 197     2117   1504   1922     75   -127    -53       C  
-ATOM   1655  CZ  PHE A 197       7.528 -32.205  20.445  1.00 12.99           C  
-ANISOU 1655  CZ  PHE A 197     1895   1328   1712     76    -95    -28       C  
-ATOM   1656  N   LYS A 198       5.924 -38.797  23.296  1.00 13.64           N  
-ANISOU 1656  N   LYS A 198     2008   1407   1768    114   -116    -77       N  
-ATOM   1657  CA  LYS A 198       5.833 -40.229  23.578  1.00 13.40           C  
-ANISOU 1657  CA  LYS A 198     1966   1375   1750    117   -117    -85       C  
-ATOM   1658  C   LYS A 198       4.433 -40.683  23.244  1.00 16.42           C  
-ANISOU 1658  C   LYS A 198     2343   1779   2118    122    -88    -72       C  
-ATOM   1659  O   LYS A 198       3.488 -40.016  23.642  1.00 13.01           O  
-ANISOU 1659  O   LYS A 198     1936   1346   1663    137    -76    -50       O  
-ATOM   1660  CB  LYS A 198       6.083 -40.501  25.068  1.00 13.19           C  
-ANISOU 1660  CB  LYS A 198     1976   1317   1718    134   -139    -81       C  
-ATOM   1661  CG  LYS A 198       7.565 -40.506  25.478  1.00 10.01           C  
-ANISOU 1661  CG  LYS A 198     1571    895   1339    126   -174    -93       C  
-ATOM   1662  CD  LYS A 198       7.681 -40.482  26.992  1.00  8.55           C  
-ANISOU 1662  CD  LYS A 198     1429    684   1135    142   -199    -84       C  
-ATOM   1663  CE  LYS A 198       9.133 -40.252  27.434  1.00 10.62           C  
-ANISOU 1663  CE  LYS A 198     1690    929   1415    129   -240    -92       C  
-ATOM   1664  NZ  LYS A 198       9.975 -41.450  27.150  1.00 14.76           N  
-ANISOU 1664  NZ  LYS A 198     2171   1454   1982    122   -248    -96       N  
-ATOM   1665  N   GLY A 199       4.302 -41.803  22.530  1.00 12.98           N  
-ANISOU 1665  N   GLY A 199     1873   1361   1699    109    -77    -86       N  
-ATOM   1666  CA  GLY A 199       2.982 -42.349  22.208  1.00 11.79           C  
-ANISOU 1666  CA  GLY A 199     1712   1230   1538    109    -54    -74       C  
-ATOM   1667  C   GLY A 199       2.319 -42.946  23.440  1.00 14.45           C  
-ANISOU 1667  C   GLY A 199     2075   1543   1872    133    -54    -58       C  
-ATOM   1668  O   GLY A 199       2.987 -43.298  24.399  1.00 16.53           O  
-ANISOU 1668  O   GLY A 199     2356   1780   2146    145    -71    -62       O  
-ATOM   1669  N   PRO A 200       0.980 -43.048  23.433  1.00 10.74           N  
-ANISOU 1669  N   PRO A 200     1606   1086   1388    141    -34    -35       N  
-ATOM   1670  CA  PRO A 200       0.311 -43.720  24.549  1.00 12.28           C  
-ANISOU 1670  CA  PRO A 200     1821   1260   1583    165    -29    -17       C  
-ATOM   1671  C   PRO A 200       0.882 -45.125  24.802  1.00 13.89           C  
-ANISOU 1671  C   PRO A 200     2009   1449   1821    161    -37    -36       C  
-ATOM   1672  O   PRO A 200       0.897 -45.581  25.950  1.00 15.84           O  
-ANISOU 1672  O   PRO A 200     2277   1672   2071    183    -43    -24       O  
-ATOM   1673  CB  PRO A 200      -1.144 -43.797  24.074  1.00  8.24           C  
-ANISOU 1673  CB  PRO A 200     1296    772   1064    164     -5      7       C  
-ATOM   1674  CG  PRO A 200      -1.313 -42.571  23.242  1.00 14.32           C  
-ANISOU 1674  CG  PRO A 200     2060   1567   1815    153      2     17       C  
-ATOM   1675  CD  PRO A 200       0.028 -42.401  22.518  1.00 15.01           C  
-ANISOU 1675  CD  PRO A 200     2132   1660   1912    131    -15    -17       C  
-ATOM   1676  N   GLU A 201       1.371 -45.795  23.758  1.00 10.11           N  
-ANISOU 1676  N   GLU A 201     1493    984   1366    135    -35    -65       N  
-ATOM   1677  CA  GLU A 201       1.900 -47.140  23.944  1.00 12.28           C  
-ANISOU 1677  CA  GLU A 201     1749   1239   1679    132    -36    -82       C  
-ATOM   1678  C   GLU A 201       3.086 -47.133  24.921  1.00 14.93           C  
-ANISOU 1678  C   GLU A 201     2101   1545   2026    146    -60    -82       C  
-ATOM   1679  O   GLU A 201       3.215 -48.024  25.770  1.00 13.14           O  
-ANISOU 1679  O   GLU A 201     1876   1296   1821    161    -64    -73       O  
-ATOM   1680  CB  GLU A 201       2.281 -47.803  22.605  1.00 15.02           C  
-ANISOU 1680  CB  GLU A 201     2056   1602   2048    100    -25   -118       C  
-ATOM   1681  CG  GLU A 201       3.278 -47.031  21.735  1.00 12.17           C  
-ANISOU 1681  CG  GLU A 201     1686   1257   1682     82    -31   -138       C  
-ATOM   1682  CD  GLU A 201       2.589 -46.095  20.760  1.00 16.55           C  
-ANISOU 1682  CD  GLU A 201     2235   1850   2202     67    -23   -132       C  
-ATOM   1683  OE1 GLU A 201       1.789 -45.257  21.212  1.00 13.16           O  
-ANISOU 1683  OE1 GLU A 201     1828   1427   1746     82    -23   -101       O  
-ATOM   1684  OE2 GLU A 201       2.846 -46.196  19.545  1.00 13.80           O  
-ANISOU 1684  OE2 GLU A 201     1861   1528   1854     41    -13   -156       O  
-ATOM   1685  N   LEU A 202       3.943 -46.123  24.803  1.00 14.58           N  
-ANISOU 1685  N   LEU A 202     2066   1503   1970    142    -77    -88       N  
-ATOM   1686  CA  LEU A 202       5.064 -45.991  25.714  1.00 14.40           C  
-ANISOU 1686  CA  LEU A 202     2059   1456   1955    151   -105    -86       C  
-ATOM   1687  C   LEU A 202       4.571 -45.641  27.113  1.00 13.86           C  
-ANISOU 1687  C   LEU A 202     2035   1373   1858    178   -116    -58       C  
-ATOM   1688  O   LEU A 202       5.108 -46.120  28.111  1.00 14.22           O  
-ANISOU 1688  O   LEU A 202     2091   1400   1912    190   -135    -49       O  
-ATOM   1689  CB  LEU A 202       6.035 -44.909  25.226  1.00 14.75           C  
-ANISOU 1689  CB  LEU A 202     2103   1506   1995    137   -122    -97       C  
-ATOM   1690  CG  LEU A 202       6.452 -44.972  23.756  1.00 11.63           C  
-ANISOU 1690  CG  LEU A 202     1670   1131   1619    112   -107   -122       C  
-ATOM   1691  CD1 LEU A 202       7.373 -43.803  23.446  1.00 13.79           C  
-ANISOU 1691  CD1 LEU A 202     1945   1407   1887    103   -124   -126       C  
-ATOM   1692  CD2 LEU A 202       7.136 -46.309  23.442  1.00 14.66           C  
-ANISOU 1692  CD2 LEU A 202     2018   1504   2048    103   -100   -140       C  
-ATOM   1693  N   LEU A 203       3.552 -44.789  27.180  1.00 10.65           N  
-ANISOU 1693  N   LEU A 203     1654    976   1415    187   -102    -44       N  
-ATOM   1694  CA  LEU A 203       3.105 -44.252  28.458  1.00 11.46           C  
-ANISOU 1694  CA  LEU A 203     1806   1065   1485    212   -107    -22       C  
-ATOM   1695  C   LEU A 203       2.335 -45.294  29.267  1.00 14.34           C  
-ANISOU 1695  C   LEU A 203     2175   1421   1853    233    -95      0       C  
-ATOM   1696  O   LEU A 203       2.190 -45.172  30.482  1.00 13.07           O  
-ANISOU 1696  O   LEU A 203     2052   1246   1668    256   -102     18       O  
-ATOM   1697  CB  LEU A 203       2.260 -42.997  28.224  1.00 10.73           C  
-ANISOU 1697  CB  LEU A 203     1737    982   1359    217    -90    -11       C  
-ATOM   1698  CG  LEU A 203       3.019 -41.862  27.516  1.00 16.30           C  
-ANISOU 1698  CG  LEU A 203     2439   1693   2061    199   -101    -27       C  
-ATOM   1699  CD1 LEU A 203       2.074 -40.750  27.109  1.00 15.99           C  
-ANISOU 1699  CD1 LEU A 203     2413   1665   2000    203    -76    -12       C  
-ATOM   1700  CD2 LEU A 203       4.158 -41.327  28.381  1.00 16.19           C  
-ANISOU 1700  CD2 LEU A 203     2455   1657   2040    199   -135    -37       C  
-ATOM   1701  N   VAL A 204       1.835 -46.319  28.589  1.00 18.39           N  
-ANISOU 1701  N   VAL A 204     2650   1942   2396    225    -76     -2       N  
-ATOM   1702  CA  VAL A 204       1.150 -47.409  29.271  1.00 16.36           C  
-ANISOU 1702  CA  VAL A 204     2389   1673   2152    243    -63     19       C  
-ATOM   1703  C   VAL A 204       2.034 -48.646  29.348  1.00 18.17           C  
-ANISOU 1703  C   VAL A 204     2588   1888   2427    237    -73      9       C  
-ATOM   1704  O   VAL A 204       1.582 -49.712  29.772  1.00 17.81           O  
-ANISOU 1704  O   VAL A 204     2530   1832   2405    249    -61     24       O  
-ATOM   1705  CB  VAL A 204      -0.215 -47.756  28.610  1.00 10.98           C  
-ANISOU 1705  CB  VAL A 204     1687   1007   1476    240    -32     29       C  
-ATOM   1706  CG1 VAL A 204      -1.130 -46.542  28.617  1.00 16.54           C  
-ANISOU 1706  CG1 VAL A 204     2420   1724   2142    250    -18     48       C  
-ATOM   1707  CG2 VAL A 204      -0.022 -48.272  27.191  1.00 12.50           C  
-ANISOU 1707  CG2 VAL A 204     1834   1216   1699    207    -25     -1       C  
-ATOM   1708  N   ASP A 205       3.294 -48.494  28.938  1.00 14.79           N  
-ANISOU 1708  N   ASP A 205     2145   1458   2015    220    -94    -14       N  
-ATOM   1709  CA  ASP A 205       4.294 -49.546  29.095  1.00 15.82           C  
-ANISOU 1709  CA  ASP A 205     2248   1572   2192    217   -104    -19       C  
-ATOM   1710  C   ASP A 205       4.026 -50.758  28.190  1.00 22.82           C  
-ANISOU 1710  C   ASP A 205     3089   2455   3125    202    -76    -37       C  
-ATOM   1711  O   ASP A 205       4.309 -51.892  28.570  1.00 25.55           O  
-ANISOU 1711  O   ASP A 205     3414   2781   3513    209    -72    -29       O  
-ATOM   1712  CB  ASP A 205       4.357 -49.970  30.573  1.00 24.18           C  
-ANISOU 1712  CB  ASP A 205     3328   2613   3245    243   -119     14       C  
-ATOM   1713  CG  ASP A 205       5.636 -50.713  30.931  1.00 37.88           C  
-ANISOU 1713  CG  ASP A 205     5039   4333   5022    242   -139     18       C  
-ATOM   1714  OD1 ASP A 205       6.628 -50.624  30.171  1.00 36.53           O  
-ANISOU 1714  OD1 ASP A 205     4842   4160   4876    221   -148     -5       O  
-ATOM   1715  OD2 ASP A 205       5.647 -51.383  31.992  1.00 36.60           O  
-ANISOU 1715  OD2 ASP A 205     4882   4159   4867    262   -147     48       O  
-ATOM   1716  N   TYR A 206       3.491 -50.516  26.993  1.00 14.96           N  
-ANISOU 1716  N   TYR A 206     2079   1480   2124    181    -58    -59       N  
-ATOM   1717  CA  TYR A 206       3.277 -51.581  26.007  1.00 14.72           C  
-ANISOU 1717  CA  TYR A 206     2011   1450   2134    161    -33    -85       C  
-ATOM   1718  C   TYR A 206       4.460 -51.685  25.057  1.00 14.68           C  
-ANISOU 1718  C   TYR A 206     1978   1444   2154    138    -32   -119       C  
-ATOM   1719  O   TYR A 206       4.713 -50.761  24.293  1.00 15.31           O  
-ANISOU 1719  O   TYR A 206     2061   1546   2209    123    -37   -135       O  
-ATOM   1720  CB  TYR A 206       2.013 -51.320  25.182  1.00 15.52           C  
-ANISOU 1720  CB  TYR A 206     2108   1577   2210    146    -14    -90       C  
-ATOM   1721  CG  TYR A 206       1.659 -52.485  24.279  1.00 14.67           C  
-ANISOU 1721  CG  TYR A 206     1965   1469   2139    122     10   -117       C  
-ATOM   1722  CD1 TYR A 206       1.137 -53.666  24.806  1.00 18.65           C  
-ANISOU 1722  CD1 TYR A 206     2457   1950   2680    132     24   -105       C  
-ATOM   1723  CD2 TYR A 206       1.854 -52.412  22.905  1.00 15.70           C  
-ANISOU 1723  CD2 TYR A 206     2075   1622   2267     89     20   -154       C  
-ATOM   1724  CE1 TYR A 206       0.810 -54.738  23.983  1.00 16.60           C  
-ANISOU 1724  CE1 TYR A 206     2166   1685   2456    107     47   -134       C  
-ATOM   1725  CE2 TYR A 206       1.542 -53.477  22.078  1.00 13.49           C  
-ANISOU 1725  CE2 TYR A 206     1767   1342   2018     64     42   -185       C  
-ATOM   1726  CZ  TYR A 206       1.013 -54.634  22.621  1.00 15.11           C  
-ANISOU 1726  CZ  TYR A 206     1962   1520   2261     72     55   -176       C  
-ATOM   1727  OH  TYR A 206       0.697 -55.688  21.793  1.00 16.04           O  
-ANISOU 1727  OH  TYR A 206     2052   1632   2410     44     78   -210       O  
-ATOM   1728  N   GLN A 207       5.159 -52.820  25.077  1.00 15.08           N  
-ANISOU 1728  N   GLN A 207     2001   1469   2259    136    -23   -129       N  
-ATOM   1729  CA  GLN A 207       6.453 -52.926  24.396  1.00 18.49           C  
-ANISOU 1729  CA  GLN A 207     2408   1894   2722    121    -22   -155       C  
-ATOM   1730  C   GLN A 207       6.423 -53.393  22.943  1.00 18.69           C  
-ANISOU 1730  C   GLN A 207     2407   1930   2764     91      9   -199       C  
-ATOM   1731  O   GLN A 207       7.420 -53.232  22.225  1.00 16.10           O  
-ANISOU 1731  O   GLN A 207     2063   1603   2451     78     13   -221       O  
-ATOM   1732  CB  GLN A 207       7.391 -53.850  25.183  1.00 16.62           C  
-ANISOU 1732  CB  GLN A 207     2154   1622   2540    136    -27   -139       C  
-ATOM   1733  CG  GLN A 207       7.692 -53.387  26.591  1.00 18.90           C  
-ANISOU 1733  CG  GLN A 207     2468   1904   2810    162    -62    -97       C  
-ATOM   1734  CD  GLN A 207       8.671 -54.310  27.280  1.00 24.07           C  
-ANISOU 1734  CD  GLN A 207     3097   2527   3520    174    -68    -76       C  
-ATOM   1735  OE1 GLN A 207       8.278 -55.136  28.097  1.00 26.32           O  
-ANISOU 1735  OE1 GLN A 207     3379   2795   3825    192    -63    -49       O  
-ATOM   1736  NE2 GLN A 207       9.955 -54.196  26.928  1.00 20.65           N  
-ANISOU 1736  NE2 GLN A 207     2642   2087   3116    165    -77    -84       N  
-ATOM   1737  N   MET A 208       5.316 -53.989  22.503  1.00 15.20           N  
-ANISOU 1737  N   MET A 208     1960   1496   2321     79     30   -212       N  
-ATOM   1738  CA  MET A 208       5.269 -54.565  21.153  1.00 13.79           C  
-ANISOU 1738  CA  MET A 208     1757   1326   2156     47     60   -258       C  
-ATOM   1739  C   MET A 208       4.736 -53.552  20.140  1.00 14.19           C  
-ANISOU 1739  C   MET A 208     1817   1425   2151     25     57   -272       C  
-ATOM   1740  O   MET A 208       3.758 -53.813  19.417  1.00 15.06           O  
-ANISOU 1740  O   MET A 208     1922   1557   2245      2     71   -289       O  
-ATOM   1741  CB  MET A 208       4.452 -55.867  21.152  1.00 15.06           C  
-ANISOU 1741  CB  MET A 208     1903   1467   2353     40     84   -269       C  
-ATOM   1742  CG  MET A 208       4.778 -56.815  20.007  1.00 18.48           C  
-ANISOU 1742  CG  MET A 208     2310   1891   2821     10    118   -321       C  
-ATOM   1743  SD  MET A 208       3.933 -58.428  20.086  1.00 20.80           S  
-ANISOU 1743  SD  MET A 208     2584   2150   3168      1    148   -337       S  
-ATOM   1744  CE  MET A 208       4.650 -59.091  21.589  1.00 36.70           C  
-ANISOU 1744  CE  MET A 208     4590   4111   5243     43    143   -292       C  
-ATOM   1745  N   TYR A 209       5.378 -52.386  20.102  1.00 14.68           N  
-ANISOU 1745  N   TYR A 209     1890   1502   2185     30     38   -262       N  
-ATOM   1746  CA  TYR A 209       4.928 -51.287  19.249  1.00 15.47           C  
-ANISOU 1746  CA  TYR A 209     1998   1647   2233     14     34   -265       C  
-ATOM   1747  C   TYR A 209       5.668 -51.312  17.920  1.00 16.22           C  
-ANISOU 1747  C   TYR A 209     2072   1760   2331    -14     52   -304       C  
-ATOM   1748  O   TYR A 209       6.423 -52.245  17.657  1.00 13.40           O  
-ANISOU 1748  O   TYR A 209     1696   1378   2017    -20     72   -331       O  
-ATOM   1749  CB  TYR A 209       5.095 -49.934  19.959  1.00 11.07           C  
-ANISOU 1749  CB  TYR A 209     1466   1095   1644     34      6   -230       C  
-ATOM   1750  CG  TYR A 209       6.518 -49.567  20.373  1.00 13.55           C  
-ANISOU 1750  CG  TYR A 209     1781   1388   1980     45    -10   -226       C  
-ATOM   1751  CD1 TYR A 209       7.403 -49.025  19.461  1.00 14.76           C  
-ANISOU 1751  CD1 TYR A 209     1920   1556   2132     30     -7   -244       C  
-ATOM   1752  CD2 TYR A 209       6.945 -49.725  21.692  1.00 10.71           C  
-ANISOU 1752  CD2 TYR A 209     1434    996   1638     71    -31   -201       C  
-ATOM   1753  CE1 TYR A 209       8.693 -48.669  19.829  1.00 18.96           C  
-ANISOU 1753  CE1 TYR A 209     2448   2067   2687     39    -24   -237       C  
-ATOM   1754  CE2 TYR A 209       8.238 -49.362  22.079  1.00 16.38           C  
-ANISOU 1754  CE2 TYR A 209     2150   1697   2375     77    -52   -195       C  
-ATOM   1755  CZ  TYR A 209       9.109 -48.843  21.139  1.00 17.04           C  
-ANISOU 1755  CZ  TYR A 209     2217   1793   2463     61    -48   -213       C  
-ATOM   1756  OH  TYR A 209      10.390 -48.479  21.503  1.00 15.81           O  
-ANISOU 1756  OH  TYR A 209     2056   1620   2331     66    -70   -203       O  
-ATOM   1757  N   ASP A 210       5.446 -50.303  17.078  1.00 12.80           N  
-ANISOU 1757  N   ASP A 210     1641   1368   1853    -29     49   -304       N  
-ATOM   1758  CA  ASP A 210       5.954 -50.345  15.701  1.00 10.01           C  
-ANISOU 1758  CA  ASP A 210     1270   1042   1493    -58     70   -341       C  
-ATOM   1759  C   ASP A 210       6.120 -48.956  15.095  1.00 11.19           C  
-ANISOU 1759  C   ASP A 210     1422   1229   1600    -63     60   -326       C  
-ATOM   1760  O   ASP A 210       6.145 -47.958  15.816  1.00 12.61           O  
-ANISOU 1760  O   ASP A 210     1619   1406   1768    -42     37   -291       O  
-ATOM   1761  CB  ASP A 210       5.084 -51.258  14.813  1.00 10.75           C  
-ANISOU 1761  CB  ASP A 210     1352   1155   1577    -89     93   -375       C  
-ATOM   1762  CG  ASP A 210       3.615 -50.829  14.764  1.00 15.03           C  
-ANISOU 1762  CG  ASP A 210     1902   1732   2075    -97     81   -351       C  
-ATOM   1763  OD1 ASP A 210       3.333 -49.779  14.153  1.00 17.79           O  
-ANISOU 1763  OD1 ASP A 210     2253   2126   2381   -106     73   -336       O  
-ATOM   1764  OD2 ASP A 210       2.731 -51.551  15.298  1.00 15.69           O  
-ANISOU 1764  OD2 ASP A 210     1988   1802   2173    -94     81   -344       O  
-ATOM   1765  N   TYR A 211       6.242 -48.885  13.771  1.00 10.85           N  
-ANISOU 1765  N   TYR A 211     1364   1223   1535    -91     78   -353       N  
-ATOM   1766  CA  TYR A 211       6.354 -47.607  13.075  1.00 10.39           C  
-ANISOU 1766  CA  TYR A 211     1304   1206   1437    -97     72   -337       C  
-ATOM   1767  C   TYR A 211       5.315 -46.577  13.500  1.00 14.59           C  
-ANISOU 1767  C   TYR A 211     1850   1758   1933    -86     51   -292       C  
-ATOM   1768  O   TYR A 211       5.556 -45.372  13.441  1.00 10.36           O  
-ANISOU 1768  O   TYR A 211     1319   1237   1381    -78     41   -266       O  
-ATOM   1769  CB  TYR A 211       6.202 -47.816  11.562  1.00 11.86           C  
-ANISOU 1769  CB  TYR A 211     1474   1440   1593   -133     96   -369       C  
-ATOM   1770  CG  TYR A 211       6.921 -49.015  10.988  1.00  9.21           C  
-ANISOU 1770  CG  TYR A 211     1126   1086   1287   -149    126   -421       C  
-ATOM   1771  CD1 TYR A 211       8.311 -49.018  10.846  1.00 13.55           C  
-ANISOU 1771  CD1 TYR A 211     1665   1612   1870   -140    140   -433       C  
-ATOM   1772  CD2 TYR A 211       6.211 -50.139  10.560  1.00 11.36           C  
-ANISOU 1772  CD2 TYR A 211     1396   1364   1557   -174    144   -457       C  
-ATOM   1773  CE1 TYR A 211       8.967 -50.106  10.313  1.00 15.78           C  
-ANISOU 1773  CE1 TYR A 211     1937   1875   2184   -152    175   -479       C  
-ATOM   1774  CE2 TYR A 211       6.865 -51.238  10.017  1.00 14.27           C  
-ANISOU 1774  CE2 TYR A 211     1755   1711   1955   -189    177   -508       C  
-ATOM   1775  CZ  TYR A 211       8.247 -51.209   9.892  1.00 13.96           C  
-ANISOU 1775  CZ  TYR A 211     1707   1648   1950   -177    195   -518       C  
-ATOM   1776  OH  TYR A 211       8.917 -52.279   9.350  1.00 14.37           O  
-ANISOU 1776  OH  TYR A 211     1749   1675   2035   -189    234   -567       O  
-ATOM   1777  N   SER A 212       4.140 -47.054  13.888  1.00 11.20           N  
-ANISOU 1777  N   SER A 212     1428   1331   1496    -87     49   -283       N  
-ATOM   1778  CA  SER A 212       3.035 -46.160  14.224  1.00 12.21           C  
-ANISOU 1778  CA  SER A 212     1567   1479   1592    -77     36   -240       C  
-ATOM   1779  C   SER A 212       3.364 -45.212  15.393  1.00  8.63           C  
-ANISOU 1779  C   SER A 212     1138    995   1147    -43     18   -205       C  
-ATOM   1780  O   SER A 212       2.763 -44.149  15.512  1.00 11.13           O  
-ANISOU 1780  O   SER A 212     1464   1327   1438    -33     11   -170       O  
-ATOM   1781  CB  SER A 212       1.762 -46.964  14.481  1.00 12.26           C  
-ANISOU 1781  CB  SER A 212     1574   1488   1597    -83     38   -235       C  
-ATOM   1782  OG  SER A 212       1.961 -47.941  15.491  1.00 12.60           O  
-ANISOU 1782  OG  SER A 212     1626   1482   1680    -65     38   -245       O  
-ATOM   1783  N   LEU A 213       4.334 -45.573  16.233  1.00 11.37           N  
-ANISOU 1783  N   LEU A 213     1494   1296   1529    -25     10   -215       N  
-ATOM   1784  CA  LEU A 213       4.826 -44.625  17.252  1.00 10.76           C  
-ANISOU 1784  CA  LEU A 213     1441   1192   1455      2    -11   -188       C  
-ATOM   1785  C   LEU A 213       5.200 -43.272  16.632  1.00 14.81           C  
-ANISOU 1785  C   LEU A 213     1951   1728   1948     -3    -14   -175       C  
-ATOM   1786  O   LEU A 213       4.847 -42.213  17.162  1.00 11.80           O  
-ANISOU 1786  O   LEU A 213     1590   1343   1551     12    -23   -144       O  
-ATOM   1787  CB  LEU A 213       6.051 -45.190  17.975  1.00 11.77           C  
-ANISOU 1787  CB  LEU A 213     1571   1278   1625     13    -22   -202       C  
-ATOM   1788  CG  LEU A 213       6.723 -44.207  18.928  1.00 15.92           C  
-ANISOU 1788  CG  LEU A 213     2119   1779   2152     33    -47   -180       C  
-ATOM   1789  CD1 LEU A 213       5.835 -43.946  20.149  1.00 17.71           C  
-ANISOU 1789  CD1 LEU A 213     2379   1988   2360     56    -58   -153       C  
-ATOM   1790  CD2 LEU A 213       8.092 -44.747  19.354  1.00 14.74           C  
-ANISOU 1790  CD2 LEU A 213     1960   1596   2044     37    -59   -193       C  
-ATOM   1791  N   ASP A 214       5.927 -43.309  15.515  1.00 12.40           N  
-ANISOU 1791  N   ASP A 214     1620   1445   1646    -24     -3   -196       N  
-ATOM   1792  CA  ASP A 214       6.403 -42.087  14.861  1.00 13.58           C  
-ANISOU 1792  CA  ASP A 214     1761   1616   1782    -29     -4   -182       C  
-ATOM   1793  C   ASP A 214       5.228 -41.224  14.408  1.00 11.99           C  
-ANISOU 1793  C   ASP A 214     1560   1453   1541    -33      2   -151       C  
-ATOM   1794  O   ASP A 214       5.343 -40.003  14.304  1.00 11.26           O  
-ANISOU 1794  O   ASP A 214     1470   1368   1441    -27     -2   -124       O  
-ATOM   1795  CB  ASP A 214       7.278 -42.419  13.647  1.00 13.08           C  
-ANISOU 1795  CB  ASP A 214     1670   1575   1726    -51     14   -211       C  
-ATOM   1796  CG  ASP A 214       8.605 -43.068  14.031  1.00 15.36           C  
-ANISOU 1796  CG  ASP A 214     1953   1823   2060    -45     11   -233       C  
-ATOM   1797  OD1 ASP A 214       9.071 -42.892  15.179  1.00 14.00           O  
-ANISOU 1797  OD1 ASP A 214     1797   1610   1912    -25    -11   -220       O  
-ATOM   1798  OD2 ASP A 214       9.184 -43.755  13.163  1.00 14.88           O  
-ANISOU 1798  OD2 ASP A 214     1871   1773   2012    -61     33   -263       O  
-ATOM   1799  N   MET A 215       4.105 -41.866  14.120  1.00 11.39           N  
-ANISOU 1799  N   MET A 215     1479   1402   1447    -44     11   -151       N  
-ATOM   1800  CA  MET A 215       2.942 -41.139  13.630  1.00 10.59           C  
-ANISOU 1800  CA  MET A 215     1371   1341   1311    -49     16   -116       C  
-ATOM   1801  C   MET A 215       2.242 -40.373  14.764  1.00 11.69           C  
-ANISOU 1801  C   MET A 215     1537   1454   1449    -20      9    -77       C  
-ATOM   1802  O   MET A 215       1.737 -39.267  14.552  1.00 13.02           O  
-ANISOU 1802  O   MET A 215     1704   1641   1602    -15     13    -40       O  
-ATOM   1803  CB  MET A 215       1.988 -42.084  12.888  1.00 11.39           C  
-ANISOU 1803  CB  MET A 215     1454   1481   1392    -76     26   -129       C  
-ATOM   1804  CG  MET A 215       2.641 -42.790  11.694  1.00 16.78           C  
-ANISOU 1804  CG  MET A 215     2114   2191   2068   -107     37   -172       C  
-ATOM   1805  SD  MET A 215       3.507 -41.675  10.551  1.00 14.79           S  
-ANISOU 1805  SD  MET A 215     1844   1978   1798   -118     45   -164       S  
-ATOM   1806  CE  MET A 215       2.120 -40.845   9.765  1.00 15.01           C  
-ANISOU 1806  CE  MET A 215     1854   2071   1778   -133     45   -115       C  
-ATOM   1807  N   TRP A 216       2.221 -40.948  15.967  1.00 11.33           N  
-ANISOU 1807  N   TRP A 216     1517   1366   1424      0      1    -83       N  
-ATOM   1808  CA  TRP A 216       1.779 -40.193  17.130  1.00 11.21           C  
-ANISOU 1808  CA  TRP A 216     1533   1319   1407     29     -4    -52       C  
-ATOM   1809  C   TRP A 216       2.648 -38.945  17.312  1.00 12.59           C  
-ANISOU 1809  C   TRP A 216     1720   1476   1586     39    -12    -43       C  
-ATOM   1810  O   TRP A 216       2.144 -37.830  17.439  1.00 14.33           O  
-ANISOU 1810  O   TRP A 216     1951   1699   1796     51     -5    -11       O  
-ATOM   1811  CB  TRP A 216       1.812 -41.028  18.418  1.00  6.73           C  
-ANISOU 1811  CB  TRP A 216      992    709    857     49    -13    -62       C  
-ATOM   1812  CG  TRP A 216       1.405 -40.200  19.609  1.00 13.29           C  
-ANISOU 1812  CG  TRP A 216     1860   1509   1679     79    -16    -33       C  
-ATOM   1813  CD1 TRP A 216       2.226 -39.447  20.407  1.00  9.88           C  
-ANISOU 1813  CD1 TRP A 216     1457   1044   1252     94    -30    -34       C  
-ATOM   1814  CD2 TRP A 216       0.062 -39.969  20.087  1.00 13.28           C  
-ANISOU 1814  CD2 TRP A 216     1873   1509   1663     96     -1      2       C  
-ATOM   1815  NE1 TRP A 216       1.479 -38.794  21.368  1.00 14.93           N  
-ANISOU 1815  NE1 TRP A 216     2131   1663   1877    119    -24     -7       N  
-ATOM   1816  CE2 TRP A 216       0.153 -39.096  21.189  1.00 13.99           C  
-ANISOU 1816  CE2 TRP A 216     2004   1564   1748    123     -4     17       C  
-ATOM   1817  CE3 TRP A 216      -1.197 -40.434  19.701  1.00 11.54           C  
-ANISOU 1817  CE3 TRP A 216     1634   1316   1434     91     14     23       C  
-ATOM   1818  CZ2 TRP A 216      -0.972 -38.680  21.914  1.00 14.73           C  
-ANISOU 1818  CZ2 TRP A 216     2122   1647   1829    147     14     52       C  
-ATOM   1819  CZ3 TRP A 216      -2.320 -40.005  20.415  1.00 12.21           C  
-ANISOU 1819  CZ3 TRP A 216     1739   1391   1510    115     29     62       C  
-ATOM   1820  CH2 TRP A 216      -2.195 -39.146  21.511  1.00 16.29           C  
-ANISOU 1820  CH2 TRP A 216     2298   1870   2022    145     31     76       C  
-ATOM   1821  N   SER A 217       3.966 -39.147  17.330  1.00 10.21           N  
-ANISOU 1821  N   SER A 217     1417   1157   1307     34    -25    -71       N  
-ATOM   1822  CA  SER A 217       4.913 -38.038  17.478  1.00  8.02           C  
-ANISOU 1822  CA  SER A 217     1147    861   1040     39    -36    -66       C  
-ATOM   1823  C   SER A 217       4.679 -36.954  16.437  1.00 10.36           C  
-ANISOU 1823  C   SER A 217     1423   1192   1322     29    -22    -42       C  
-ATOM   1824  O   SER A 217       4.692 -35.769  16.758  1.00 10.59           O  
-ANISOU 1824  O   SER A 217     1466   1205   1352     40    -22    -19       O  
-ATOM   1825  CB  SER A 217       6.350 -38.561  17.383  1.00  7.89           C  
-ANISOU 1825  CB  SER A 217     1118    829   1052     29    -49    -97       C  
-ATOM   1826  OG  SER A 217       6.576 -39.521  18.396  1.00 12.32           O  
-ANISOU 1826  OG  SER A 217     1695   1357   1628     40    -63   -112       O  
-ATOM   1827  N   LEU A 218       4.455 -37.361  15.189  1.00 10.19           N  
-ANISOU 1827  N   LEU A 218     1367   1218   1287      7     -8    -47       N  
-ATOM   1828  CA  LEU A 218       4.193 -36.403  14.132  1.00  9.10           C  
-ANISOU 1828  CA  LEU A 218     1204   1120   1132     -4      6    -19       C  
-ATOM   1829  C   LEU A 218       2.903 -35.642  14.397  1.00 12.87           C  
-ANISOU 1829  C   LEU A 218     1691   1606   1593     10     16     26       C  
-ATOM   1830  O   LEU A 218       2.821 -34.441  14.126  1.00 12.97           O  
-ANISOU 1830  O   LEU A 218     1698   1625   1607     15     24     59       O  
-ATOM   1831  CB  LEU A 218       4.110 -37.091  12.767  1.00 11.20           C  
-ANISOU 1831  CB  LEU A 218     1436   1442   1379    -32     17    -33       C  
-ATOM   1832  CG  LEU A 218       3.924 -36.171  11.554  1.00 13.16           C  
-ANISOU 1832  CG  LEU A 218     1654   1741   1606    -46     31     -3       C  
-ATOM   1833  CD1 LEU A 218       5.199 -35.411  11.225  1.00 13.89           C  
-ANISOU 1833  CD1 LEU A 218     1736   1823   1719    -46     30     -4       C  
-ATOM   1834  CD2 LEU A 218       3.467 -36.973  10.342  1.00 11.86           C  
-ANISOU 1834  CD2 LEU A 218     1462   1636   1409    -77     41    -16       C  
-ATOM   1835  N   GLY A 219       1.898 -36.337  14.926  1.00 10.33           N  
-ANISOU 1835  N   GLY A 219     1381   1282   1263     17     18     30       N  
-ATOM   1836  CA  GLY A 219       0.635 -35.690  15.243  1.00 10.36           C  
-ANISOU 1836  CA  GLY A 219     1392   1288   1254     32     31     75       C  
-ATOM   1837  C   GLY A 219       0.850 -34.643  16.323  1.00 16.41           C  
-ANISOU 1837  C   GLY A 219     2195   2004   2036     60     32     90       C  
-ATOM   1838  O   GLY A 219       0.261 -33.563  16.273  1.00 15.04           O  
-ANISOU 1838  O   GLY A 219     2021   1832   1861     72     48    130       O  
-ATOM   1839  N   CYS A 220       1.695 -34.955  17.305  1.00 14.35           N  
-ANISOU 1839  N   CYS A 220     1965   1698   1790     70     14     57       N  
-ATOM   1840  CA  CYS A 220       2.011 -33.977  18.352  1.00 14.61           C  
-ANISOU 1840  CA  CYS A 220     2037   1682   1832     92     11     63       C  
-ATOM   1841  C   CYS A 220       2.660 -32.726  17.759  1.00 17.41           C  
-ANISOU 1841  C   CYS A 220     2379   2038   2199     86     15     76       C  
-ATOM   1842  O   CYS A 220       2.312 -31.603  18.148  1.00 12.24           O  
-ANISOU 1842  O   CYS A 220     1742   1360   1548    101     28    102       O  
-ATOM   1843  CB  CYS A 220       2.921 -34.577  19.430  1.00 12.75           C  
-ANISOU 1843  CB  CYS A 220     1832   1405   1607     98    -14     27       C  
-ATOM   1844  SG  CYS A 220       2.153 -35.883  20.408  1.00 14.03           S  
-ANISOU 1844  SG  CYS A 220     2016   1555   1759    112    -16     20       S  
-ATOM   1845  N   MET A 221       3.586 -32.925  16.816  1.00 11.13           N  
-ANISOU 1845  N   MET A 221     1551   1267   1412     64      6     59       N  
-ATOM   1846  CA  MET A 221       4.206 -31.805  16.102  1.00 12.81           C  
-ANISOU 1846  CA  MET A 221     1743   1486   1638     57     11     75       C  
-ATOM   1847  C   MET A 221       3.153 -30.992  15.338  1.00 15.26           C  
-ANISOU 1847  C   MET A 221     2030   1830   1936     59     38    125       C  
-ATOM   1848  O   MET A 221       3.132 -29.764  15.418  1.00 14.88           O  
-ANISOU 1848  O   MET A 221     1986   1763   1903     69     50    152       O  
-ATOM   1849  CB  MET A 221       5.305 -32.292  15.145  1.00 11.62           C  
-ANISOU 1849  CB  MET A 221     1559   1360   1496     34      2     51       C  
-ATOM   1850  CG  MET A 221       6.523 -32.873  15.863  1.00 12.35           C  
-ANISOU 1850  CG  MET A 221     1668   1414   1611     33    -24     12       C  
-ATOM   1851  SD  MET A 221       7.872 -33.232  14.701  1.00 18.58           S  
-ANISOU 1851  SD  MET A 221     2414   2228   2419     11    -27     -9       S  
-ATOM   1852  CE  MET A 221       8.013 -31.674  13.847  1.00 10.91           C  
-ANISOU 1852  CE  MET A 221     1419   1273   1455      8    -11     30       C  
-ATOM   1853  N   LEU A 222       2.299 -31.678  14.586  1.00 13.02           N  
-ANISOU 1853  N   LEU A 222     1720   1598   1630     48     47    137       N  
-ATOM   1854  CA  LEU A 222       1.253 -31.001  13.836  1.00 10.60           C  
-ANISOU 1854  CA  LEU A 222     1386   1330   1310     47     70    190       C  
-ATOM   1855  C   LEU A 222       0.375 -30.150  14.750  1.00 11.17           C  
-ANISOU 1855  C   LEU A 222     1486   1366   1393     76     88    225       C  
-ATOM   1856  O   LEU A 222       0.137 -28.973  14.469  1.00 14.19           O  
-ANISOU 1856  O   LEU A 222     1857   1747   1788     84    107    267       O  
-ATOM   1857  CB  LEU A 222       0.412 -31.998  13.039  1.00 13.21           C  
-ANISOU 1857  CB  LEU A 222     1688   1719   1611     28     71    194       C  
-ATOM   1858  CG  LEU A 222      -0.696 -31.382  12.184  1.00 10.03           C  
-ANISOU 1858  CG  LEU A 222     1251   1368   1194     23     90    254       C  
-ATOM   1859  CD1 LEU A 222      -0.140 -30.508  11.056  1.00 12.56           C  
-ANISOU 1859  CD1 LEU A 222     1535   1723   1513     10     97    278       C  
-ATOM   1860  CD2 LEU A 222      -1.555 -32.497  11.622  1.00 12.24           C  
-ANISOU 1860  CD2 LEU A 222     1509   1698   1444      1     84    251       C  
-ATOM   1861  N   ALA A 223      -0.100 -30.737  15.845  1.00 10.39           N  
-ANISOU 1861  N   ALA A 223     1423   1235   1290     92     85    210       N  
-ATOM   1862  CA  ALA A 223      -0.955 -30.004  16.772  1.00 11.50           C  
-ANISOU 1862  CA  ALA A 223     1594   1337   1437    121    107    241       C  
-ATOM   1863  C   ALA A 223      -0.255 -28.740  17.268  1.00 17.44           C  
-ANISOU 1863  C   ALA A 223     2372   2040   2213    133    113    240       C  
-ATOM   1864  O   ALA A 223      -0.869 -27.681  17.331  1.00 12.42           O  
-ANISOU 1864  O   ALA A 223     1739   1391   1591    149    141    281       O  
-ATOM   1865  CB  ALA A 223      -1.359 -30.880  17.938  1.00 11.81           C  
-ANISOU 1865  CB  ALA A 223     1672   1347   1468    136    101    219       C  
-ATOM   1866  N   SER A 224       1.032 -28.847  17.610  1.00 15.01           N  
-ANISOU 1866  N   SER A 224     2082   1705   1915    124     87    195       N  
-ATOM   1867  CA  SER A 224       1.777 -27.685  18.103  1.00 11.85           C  
-ANISOU 1867  CA  SER A 224     1707   1256   1539    131     87    190       C  
-ATOM   1868  C   SER A 224       1.906 -26.601  17.028  1.00 14.62           C  
-ANISOU 1868  C   SER A 224     2017   1627   1909    124    105    227       C  
-ATOM   1869  O   SER A 224       1.892 -25.410  17.334  1.00 19.99           O  
-ANISOU 1869  O   SER A 224     2713   2271   2613    136    124    246       O  
-ATOM   1870  CB  SER A 224       3.168 -28.090  18.637  1.00 14.67           C  
-ANISOU 1870  CB  SER A 224     2085   1585   1904    119     50    137       C  
-ATOM   1871  OG  SER A 224       4.081 -28.342  17.583  1.00 15.88           O  
-ANISOU 1871  OG  SER A 224     2195   1771   2066     96     35    128       O  
-ATOM   1872  N   MET A 225       2.008 -27.004  15.767  1.00 14.19           N  
-ANISOU 1872  N   MET A 225     1905   1453   2035     42     41    352       N  
-ATOM   1873  CA  MET A 225       2.169 -26.027  14.695  1.00 14.12           C  
-ANISOU 1873  CA  MET A 225     1863   1430   2072     35     49    392       C  
-ATOM   1874  C   MET A 225       0.835 -25.351  14.319  1.00 15.20           C  
-ANISOU 1874  C   MET A 225     2014   1593   2167     58     70    385       C  
-ATOM   1875  O   MET A 225       0.747 -24.119  14.290  1.00 17.67           O  
-ANISOU 1875  O   MET A 225     2331   1871   2513     66     40    391       O  
-ATOM   1876  CB  MET A 225       2.801 -26.675  13.457  1.00 14.89           C  
-ANISOU 1876  CB  MET A 225     1910   1555   2193     10     95    437       C  
-ATOM   1877  CG  MET A 225       4.240 -27.172  13.649  1.00 22.12           C  
-ANISOU 1877  CG  MET A 225     2804   2439   3162    -15     74    454       C  
-ATOM   1878  SD  MET A 225       4.731 -28.223  12.259  1.00 33.16           S  
-ANISOU 1878  SD  MET A 225     4149   3886   4564    -39    138    498       S  
-ATOM   1879  CE  MET A 225       6.376 -28.710  12.724  1.00 48.15           C  
-ANISOU 1879  CE  MET A 225     6030   5742   6524    -65    103    510       C  
-ATOM   1880  N   ILE A 226      -0.197 -26.141  14.042  1.00 15.33           N  
-ANISOU 1880  N   ILE A 226     2040   1672   2113     67    120    372       N  
-ATOM   1881  CA  ILE A 226      -1.472 -25.542  13.606  1.00 16.81           C  
-ANISOU 1881  CA  ILE A 226     2238   1888   2259     88    144    367       C  
-ATOM   1882  C   ILE A 226      -2.176 -24.755  14.713  1.00 16.32           C  
-ANISOU 1882  C   ILE A 226     2224   1802   2175    116    100    326       C  
-ATOM   1883  O   ILE A 226      -2.868 -23.782  14.427  1.00 20.69           O  
-ANISOU 1883  O   ILE A 226     2784   2352   2725    131     98    328       O  
-ATOM   1884  CB  ILE A 226      -2.440 -26.548  12.927  1.00 14.15           C  
-ANISOU 1884  CB  ILE A 226     1897   1626   1853     92    211    366       C  
-ATOM   1885  CG1 ILE A 226      -2.939 -27.603  13.922  1.00 14.27           C  
-ANISOU 1885  CG1 ILE A 226     1948   1669   1806    102    214    324       C  
-ATOM   1886  CG2 ILE A 226      -1.771 -27.188  11.710  1.00 15.37           C  
-ANISOU 1886  CG2 ILE A 226     2002   1805   2033     67    255    409       C  
-ATOM   1887  CD1 ILE A 226      -4.035 -28.491  13.350  1.00 13.53           C  
-ANISOU 1887  CD1 ILE A 226     1854   1647   1641    109    276    319       C  
-ATOM   1888  N   PHE A 227      -1.965 -25.153  15.966  1.00 13.74           N  
-ANISOU 1888  N   PHE A 227     1930   1458   1834    123     65    290       N  
-ATOM   1889  CA  PHE A 227      -2.565 -24.489  17.119  1.00 13.81           C  
-ANISOU 1889  CA  PHE A 227     1985   1443   1820    150     20    248       C  
-ATOM   1890  C   PHE A 227      -1.641 -23.462  17.771  1.00 19.51           C  
-ANISOU 1890  C   PHE A 227     2713   2090   2611    149    -49    247       C  
-ATOM   1891  O   PHE A 227      -2.064 -22.699  18.641  1.00 19.54           O  
-ANISOU 1891  O   PHE A 227     2751   2067   2605    173    -91    216       O  
-ATOM   1892  CB  PHE A 227      -2.999 -25.527  18.162  1.00 11.50           C  
-ANISOU 1892  CB  PHE A 227     1726   1177   1464    162     22    207       C  
-ATOM   1893  CG  PHE A 227      -4.121 -26.426  17.696  1.00 14.02           C  
-ANISOU 1893  CG  PHE A 227     2048   1569   1709    170     83    202       C  
-ATOM   1894  CD1 PHE A 227      -5.170 -25.916  16.952  1.00 13.31           C  
-ANISOU 1894  CD1 PHE A 227     1958   1511   1590    183    116    209       C  
-ATOM   1895  CD2 PHE A 227      -4.119 -27.778  18.001  1.00 12.26           C  
-ANISOU 1895  CD2 PHE A 227     1830   1382   1446    163    108    189       C  
-ATOM   1896  CE1 PHE A 227      -6.208 -26.746  16.519  1.00 14.19           C  
-ANISOU 1896  CE1 PHE A 227     2071   1688   1634    189    172    204       C  
-ATOM   1897  CE2 PHE A 227      -5.149 -28.608  17.578  1.00 14.53           C  
-ANISOU 1897  CE2 PHE A 227     2120   1735   1668    169    163    184       C  
-ATOM   1898  CZ  PHE A 227      -6.192 -28.086  16.837  1.00 16.01           C  
-ANISOU 1898  CZ  PHE A 227     2305   1953   1826    182    195    192       C  
-ATOM   1899  N   ARG A 228      -0.370 -23.464  17.385  1.00 20.12           N  
-ANISOU 1899  N   ARG A 228     2755   2133   2755    122    -61    279       N  
-ATOM   1900  CA  ARG A 228       0.575 -22.509  17.958  1.00 20.90           C  
-ANISOU 1900  CA  ARG A 228     2857   2161   2925    119   -127    280       C  
-ATOM   1901  C   ARG A 228       0.688 -22.704  19.461  1.00 17.92           C  
-ANISOU 1901  C   ARG A 228     2522   1758   2530    134   -176    234       C  
-ATOM   1902  O   ARG A 228       0.559 -21.758  20.242  1.00 21.09           O  
-ANISOU 1902  O   ARG A 228     2951   2118   2944    153   -227    210       O  
-ATOM   1903  CB  ARG A 228       0.147 -21.075  17.629  1.00 25.45           C  
-ANISOU 1903  CB  ARG A 228     3434   2709   3526    132   -148    289       C  
-ATOM   1904  CG  ARG A 228       0.269 -20.733  16.157  1.00 33.26           C  
-ANISOU 1904  CG  ARG A 228     4377   3711   4548    115   -109    340       C  
-ATOM   1905  CD  ARG A 228       1.722 -20.488  15.760  1.00 48.78           C  
-ANISOU 1905  CD  ARG A 228     6304   5631   6601     86   -132    380       C  
-ATOM   1906  NE  ARG A 228       1.849 -20.068  14.363  1.00 61.30           N  
-ANISOU 1906  NE  ARG A 228     7845   7227   8220     72    -97    431       N  
-ATOM   1907  CZ  ARG A 228       1.787 -18.804  13.947  1.00 62.73           C  
-ANISOU 1907  CZ  ARG A 228     8015   7375   8443     76   -118    451       C  
-ATOM   1908  NH1 ARG A 228       1.598 -17.820  14.819  1.00 64.73           N  
-ANISOU 1908  NH1 ARG A 228     8301   7582   8710     95   -174    423       N  
-ATOM   1909  NH2 ARG A 228       1.912 -18.521  12.656  1.00 57.33           N  
-ANISOU 1909  NH2 ARG A 228     7289   6707   7788     62    -83    498       N  
-ATOM   1910  N   LYS A 229       0.925 -23.947  19.862  1.00 17.11           N  
-ANISOU 1910  N   LYS A 229     2423   1681   2397    125   -159    221       N  
-ATOM   1911  CA  LYS A 229       1.167 -24.287  21.251  1.00 20.15           C  
-ANISOU 1911  CA  LYS A 229     2843   2045   2768    136   -202    181       C  
-ATOM   1912  C   LYS A 229       2.247 -25.366  21.267  1.00 22.32           C  
-ANISOU 1912  C   LYS A 229     3096   2320   3065    109   -194    194       C  
-ATOM   1913  O   LYS A 229       1.987 -26.513  20.920  1.00 18.46           O  
-ANISOU 1913  O   LYS A 229     2598   1882   2534    101   -145    197       O  
-ATOM   1914  CB  LYS A 229      -0.117 -24.779  21.925  1.00 20.49           C  
-ANISOU 1914  CB  LYS A 229     2927   2135   2724    164   -184    139       C  
-ATOM   1915  CG  LYS A 229       0.053 -25.099  23.410  1.00 21.54           C  
-ANISOU 1915  CG  LYS A 229     3099   2249   2838    179   -229     95       C  
-ATOM   1916  CD  LYS A 229      -1.237 -25.594  24.052  1.00 23.14           C  
-ANISOU 1916  CD  LYS A 229     3340   2501   2953    208   -210     57       C  
-ATOM   1917  CE  LYS A 229      -1.012 -25.933  25.523  1.00 27.67           C  
-ANISOU 1917  CE  LYS A 229     3949   3055   3508    222   -254     16       C  
-ATOM   1918  NZ  LYS A 229       0.195 -26.799  25.752  1.00 24.08           N  
-ANISOU 1918  NZ  LYS A 229     3478   2584   3088    196   -262     25       N  
-ATOM   1919  N   GLU A 230       3.467 -25.001  21.651  1.00 20.77           N  
-ANISOU 1919  N   GLU A 230     2890   2066   2937     95   -242    202       N  
-ATOM   1920  CA  GLU A 230       4.595 -25.935  21.553  1.00 23.03           C  
-ANISOU 1920  CA  GLU A 230     3150   2347   3252     67   -236    221       C  
-ATOM   1921  C   GLU A 230       5.279 -26.085  22.900  1.00 28.82           C  
-ANISOU 1921  C   GLU A 230     3910   3040   4000     71   -291    189       C  
-ATOM   1922  O   GLU A 230       5.840 -25.118  23.408  1.00 25.95           O  
-ANISOU 1922  O   GLU A 230     3554   2617   3687     74   -348    185       O  
-ATOM   1923  CB  GLU A 230       5.605 -25.452  20.496  1.00 30.20           C  
-ANISOU 1923  CB  GLU A 230     4009   3227   4237     40   -234    272       C  
-ATOM   1924  CG  GLU A 230       6.444 -26.562  19.819  1.00 30.77           C  
-ANISOU 1924  CG  GLU A 230     4043   3322   4325     10   -196    303       C  
-ATOM   1925  CD  GLU A 230       7.524 -27.142  20.731  1.00 30.89           C  
-ANISOU 1925  CD  GLU A 230     4064   3306   4367     -2   -233    291       C  
-ATOM   1926  OE1 GLU A 230       8.225 -26.363  21.408  1.00 33.35           O  
-ANISOU 1926  OE1 GLU A 230     4385   3557   4730     -2   -292    284       O  
-ATOM   1927  OE2 GLU A 230       7.673 -28.380  20.780  1.00 25.65           O  
-ANISOU 1927  OE2 GLU A 230     3397   2677   3673    -12   -203    286       O  
-ATOM   1928  N   PRO A 231       5.239 -27.302  23.481  1.00 27.48           N  
-ANISOU 1928  N   PRO A 231     3754   2901   3785     70   -275    167       N  
-ATOM   1929  CA  PRO A 231       4.599 -28.478  22.877  1.00 24.36           C  
-ANISOU 1929  CA  PRO A 231     3350   2575   3332     65   -209    172       C  
-ATOM   1930  C   PRO A 231       3.102 -28.487  23.165  1.00 20.10           C  
-ANISOU 1930  C   PRO A 231     2844   2078   2714     95   -188    141       C  
-ATOM   1931  O   PRO A 231       2.646 -27.744  24.036  1.00 20.97           O  
-ANISOU 1931  O   PRO A 231     2990   2166   2812    120   -229    110       O  
-ATOM   1932  CB  PRO A 231       5.279 -29.637  23.603  1.00 19.75           C  
-ANISOU 1932  CB  PRO A 231     2770   1993   2739     54   -215    158       C  
-ATOM   1933  CG  PRO A 231       5.509 -29.097  24.980  1.00 25.62           C  
-ANISOU 1933  CG  PRO A 231     3551   2689   3492     72   -281    121       C  
-ATOM   1934  CD  PRO A 231       5.831 -27.621  24.792  1.00 34.45           C  
-ANISOU 1934  CD  PRO A 231     4663   3753   4672     74   -323    135       C  
-ATOM   1935  N   PHE A 232       2.350 -29.324  22.453  1.00 14.29           N  
-ANISOU 1935  N   PHE A 232     2099   1405   1927     93   -127    149       N  
-ATOM   1936  CA  PHE A 232       0.908 -29.368  22.613  1.00 12.68           C  
-ANISOU 1936  CA  PHE A 232     1924   1247   1649    120   -102    124       C  
-ATOM   1937  C   PHE A 232       0.501 -30.085  23.912  1.00 16.65           C  
-ANISOU 1937  C   PHE A 232     2466   1764   2096    138   -117     79       C  
-ATOM   1938  O   PHE A 232      -0.226 -29.525  24.740  1.00 16.27           O  
-ANISOU 1938  O   PHE A 232     2455   1710   2017    166   -144     47       O  
-ATOM   1939  CB  PHE A 232       0.257 -30.016  21.377  1.00 14.34           C  
-ANISOU 1939  CB  PHE A 232     2107   1517   1824    111    -31    149       C  
-ATOM   1940  CG  PHE A 232      -1.254 -29.980  21.399  1.00 10.54           C  
-ANISOU 1940  CG  PHE A 232     1651   1083   1270    137     -3    127       C  
-ATOM   1941  CD1 PHE A 232      -1.927 -28.788  21.245  1.00 15.80           C  
-ANISOU 1941  CD1 PHE A 232     2329   1737   1937    156    -15    125       C  
-ATOM   1942  CD2 PHE A 232      -1.986 -31.137  21.582  1.00 15.46           C  
-ANISOU 1942  CD2 PHE A 232     2287   1761   1826    143     36    110       C  
-ATOM   1943  CE1 PHE A 232      -3.306 -28.746  21.277  1.00 14.01           C  
-ANISOU 1943  CE1 PHE A 232     2126   1553   1644    181     10    105       C  
-ATOM   1944  CE2 PHE A 232      -3.377 -31.101  21.613  1.00 21.47           C  
-ANISOU 1944  CE2 PHE A 232     3072   2566   2521    167     61     91       C  
-ATOM   1945  CZ  PHE A 232      -4.031 -29.904  21.464  1.00 20.03           C  
-ANISOU 1945  CZ  PHE A 232     2900   2371   2338    186     48     88       C  
-ATOM   1946  N   PHE A 233       0.969 -31.318  24.096  1.00 13.15           N  
-ANISOU 1946  N   PHE A 233     2016   1340   1642    122   -100     79       N  
-ATOM   1947  CA  PHE A 233       0.723 -32.031  25.340  1.00 10.24           C  
-ANISOU 1947  CA  PHE A 233     1681    982   1226    137   -116     40       C  
-ATOM   1948  C   PHE A 233       1.920 -31.792  26.249  1.00 17.59           C  
-ANISOU 1948  C   PHE A 233     2619   1854   2210    131   -176     30       C  
-ATOM   1949  O   PHE A 233       2.962 -32.425  26.099  1.00 15.32           O  
-ANISOU 1949  O   PHE A 233     2308   1554   1959    105   -175     47       O  
-ATOM   1950  CB  PHE A 233       0.546 -33.536  25.095  1.00  8.84           C  
-ANISOU 1950  CB  PHE A 233     1494    859   1005    124    -66     43       C  
-ATOM   1951  CG  PHE A 233      -0.637 -33.896  24.209  1.00 12.81           C  
-ANISOU 1951  CG  PHE A 233     1990   1423   1454    130     -5     52       C  
-ATOM   1952  CD1 PHE A 233      -1.951 -33.676  24.628  1.00 15.01           C  
-ANISOU 1952  CD1 PHE A 233     2301   1732   1670    159      2     25       C  
-ATOM   1953  CD2 PHE A 233      -0.426 -34.494  22.980  1.00  8.64           C  
-ANISOU 1953  CD2 PHE A 233     1423    924    937    106     44     86       C  
-ATOM   1954  CE1 PHE A 233      -3.034 -34.033  23.820  1.00 15.28           C  
-ANISOU 1954  CE1 PHE A 233     2328   1823   1655    164     57     33       C  
-ATOM   1955  CE2 PHE A 233      -1.495 -34.851  22.162  1.00 11.04           C  
-ANISOU 1955  CE2 PHE A 233     1720   1285   1191    112     99     94       C  
-ATOM   1956  CZ  PHE A 233      -2.807 -34.612  22.581  1.00 14.96           C  
-ANISOU 1956  CZ  PHE A 233     2249   1810   1627    140    106     67       C  
-ATOM   1957  N   HIS A 234       1.758 -30.871  27.191  1.00 19.36           N  
-ANISOU 1957  N   HIS A 234     2876   2041   2438    154   -228      2       N  
-ATOM   1958  CA  HIS A 234       2.869 -30.352  27.983  1.00 16.77           C  
-ANISOU 1958  CA  HIS A 234     2554   1650   2168    150   -291     -6       C  
-ATOM   1959  C   HIS A 234       2.868 -30.973  29.384  1.00 19.59           C  
-ANISOU 1959  C   HIS A 234     2948   2008   2490    166   -320    -47       C  
-ATOM   1960  O   HIS A 234       2.524 -30.311  30.368  1.00 20.42           O  
-ANISOU 1960  O   HIS A 234     3088   2090   2581    194   -364    -80       O  
-ATOM   1961  CB  HIS A 234       2.719 -28.831  28.068  1.00 25.39           C  
-ANISOU 1961  CB  HIS A 234     3657   2697   3292    167   -334    -11       C  
-ATOM   1962  CG  HIS A 234       3.993 -28.100  28.362  1.00 32.21           C  
-ANISOU 1962  CG  HIS A 234     4512   3491   4237    155   -391     -2       C  
-ATOM   1963  ND1 HIS A 234       5.040 -28.668  29.055  1.00 40.96           N  
-ANISOU 1963  ND1 HIS A 234     5620   4572   5372    141   -420     -8       N  
-ATOM   1964  CD2 HIS A 234       4.387 -26.841  28.053  1.00 35.70           C  
-ANISOU 1964  CD2 HIS A 234     4943   3882   4738    153   -426     14       C  
-ATOM   1965  CE1 HIS A 234       6.021 -27.789  29.167  1.00 38.12           C  
-ANISOU 1965  CE1 HIS A 234     5250   4149   5084    132   -470      2       C  
-ATOM   1966  NE2 HIS A 234       5.649 -26.672  28.568  1.00 36.86           N  
-ANISOU 1966  NE2 HIS A 234     5084   3974   4947    139   -475     16       N  
-ATOM   1967  N   GLY A 235       3.249 -32.246  29.476  1.00 16.45           N  
-ANISOU 1967  N   GLY A 235     2540   1635   2076    150   -295    -44       N  
-ATOM   1968  CA  GLY A 235       3.246 -32.942  30.750  1.00 14.75           C  
-ANISOU 1968  CA  GLY A 235     2356   1425   1825    163   -317    -80       C  
-ATOM   1969  C   GLY A 235       4.442 -32.601  31.621  1.00 16.45           C  
-ANISOU 1969  C   GLY A 235     2577   1578   2095    158   -379    -90       C  
-ATOM   1970  O   GLY A 235       5.509 -32.280  31.110  1.00 16.97           O  
-ANISOU 1970  O   GLY A 235     2613   1604   2229    134   -394    -62       O  
-ATOM   1971  N   HIS A 236       4.270 -32.701  32.934  1.00 15.67           N  
-ANISOU 1971  N   HIS A 236     2516   1473   1966    181   -416   -130       N  
-ATOM   1972  CA  HIS A 236       5.350 -32.390  33.873  1.00 22.36           C  
-ANISOU 1972  CA  HIS A 236     3373   2263   2861    180   -478   -144       C  
-ATOM   1973  C   HIS A 236       6.243 -33.596  34.155  1.00 22.53           C  
-ANISOU 1973  C   HIS A 236     3381   2287   2890    157   -471   -139       C  
-ATOM   1974  O   HIS A 236       7.393 -33.449  34.608  1.00 22.88           O  
-ANISOU 1974  O   HIS A 236     3421   2283   2989    145   -514   -139       O  
-ATOM   1975  CB  HIS A 236       4.771 -31.824  35.169  1.00 29.40           C  
-ANISOU 1975  CB  HIS A 236     4311   3141   3718    218   -524   -189       C  
-ATOM   1976  CG  HIS A 236       4.039 -30.531  34.974  1.00 51.58           C  
-ANISOU 1976  CG  HIS A 236     7134   5937   6528    241   -541   -195       C  
-ATOM   1977  ND1 HIS A 236       4.618 -29.435  34.370  1.00 62.08           N  
-ANISOU 1977  ND1 HIS A 236     8444   7217   7925    230   -566   -173       N  
-ATOM   1978  CD2 HIS A 236       2.774 -30.162  35.291  1.00 55.16           C  
-ANISOU 1978  CD2 HIS A 236     7617   6419   6922    275   -535   -220       C  
-ATOM   1979  CE1 HIS A 236       3.744 -28.444  34.328  1.00 61.33           C  
-ANISOU 1979  CE1 HIS A 236     8368   7122   7814    255   -576   -185       C  
-ATOM   1980  NE2 HIS A 236       2.618 -28.859  34.881  1.00 58.45           N  
-ANISOU 1980  NE2 HIS A 236     8033   6804   7372    283   -557   -214       N  
-ATOM   1981  N   ASP A 237       5.694 -34.782  33.894  1.00 17.22           N  
-ANISOU 1981  N   ASP A 237     2705   1674   2165    152   -418   -137       N  
-ATOM   1982  CA  ASP A 237       6.420 -36.047  33.944  1.00 20.94           C  
-ANISOU 1982  CA  ASP A 237     3159   2158   2639    128   -399   -128       C  
-ATOM   1983  C   ASP A 237       5.661 -37.052  33.071  1.00 16.97           C  
-ANISOU 1983  C   ASP A 237     2640   1721   2088    119   -329   -111       C  
-ATOM   1984  O   ASP A 237       4.667 -36.691  32.458  1.00 19.66           O  
-ANISOU 1984  O   ASP A 237     2980   2090   2397    130   -299   -106       O  
-ATOM   1985  CB  ASP A 237       6.572 -36.560  35.387  1.00 22.73           C  
-ANISOU 1985  CB  ASP A 237     3418   2379   2839    144   -434   -165       C  
-ATOM   1986  CG  ASP A 237       5.234 -36.767  36.090  1.00 28.60           C  
-ANISOU 1986  CG  ASP A 237     4199   3167   3502    178   -423   -198       C  
-ATOM   1987  OD1 ASP A 237       4.278 -37.248  35.447  1.00 22.27           O  
-ANISOU 1987  OD1 ASP A 237     3391   2418   2652    180   -370   -189       O  
-ATOM   1988  OD2 ASP A 237       5.143 -36.458  37.298  1.00 28.84           O  
-ANISOU 1988  OD2 ASP A 237     4264   3179   3516    204   -468   -232       O  
-ATOM   1989  N   ASN A 238       6.113 -38.303  33.021  1.00 13.50           N  
-ANISOU 1989  N   ASN A 238     2185   1304   1640     99   -303   -103       N  
-ATOM   1990  CA  ASN A 238       5.502 -39.277  32.106  1.00 16.39           C  
-ANISOU 1990  CA  ASN A 238     2532   1730   1968     87   -237    -85       C  
-ATOM   1991  C   ASN A 238       4.082 -39.683  32.496  1.00 14.78           C  
-ANISOU 1991  C   ASN A 238     2356   1578   1681    113   -211   -110       C  
-ATOM   1992  O   ASN A 238       3.308 -40.145  31.651  1.00 16.78           O  
-ANISOU 1992  O   ASN A 238     2596   1880   1899    110   -158    -96       O  
-ATOM   1993  CB  ASN A 238       6.392 -40.515  31.925  1.00 20.71           C  
-ANISOU 1993  CB  ASN A 238     3055   2285   2530     59   -217    -69       C  
-ATOM   1994  CG  ASN A 238       7.712 -40.188  31.236  1.00 18.83           C  
-ANISOU 1994  CG  ASN A 238     2781   2004   2370     30   -230    -36       C  
-ATOM   1995  OD1 ASN A 238       7.833 -39.172  30.551  1.00 20.39           O  
-ANISOU 1995  OD1 ASN A 238     2963   2177   2606     27   -237    -17       O  
-ATOM   1996  ND2 ASN A 238       8.710 -41.050  31.420  1.00 21.74           N  
-ANISOU 1996  ND2 ASN A 238     3135   2363   2763      9   -234    -29       N  
-ATOM   1997  N   TYR A 239       3.742 -39.518  33.770  1.00 17.18           N  
-ANISOU 1997  N   TYR A 239     2698   1875   1955    140   -247   -146       N  
-ATOM   1998  CA  TYR A 239       2.401 -39.842  34.241  1.00 16.32           C  
-ANISOU 1998  CA  TYR A 239     2618   1815   1768    167   -227   -171       C  
-ATOM   1999  C   TYR A 239       1.461 -38.710  33.863  1.00 15.05           C  
-ANISOU 1999  C   TYR A 239     2468   1657   1593    189   -225   -173       C  
-ATOM   2000  O   TYR A 239       0.414 -38.932  33.245  1.00 14.74           O  
-ANISOU 2000  O   TYR A 239     2426   1666   1509    195   -180   -167       O  
-ATOM   2001  CB  TYR A 239       2.409 -40.089  35.747  1.00 15.78           C  
-ANISOU 2001  CB  TYR A 239     2585   1739   1672    189   -266   -207       C  
-ATOM   2002  CG  TYR A 239       3.456 -41.106  36.118  1.00 27.93           C  
-ANISOU 2002  CG  TYR A 239     4112   3267   3232    167   -273   -204       C  
-ATOM   2003  CD1 TYR A 239       3.340 -42.421  35.703  1.00 29.10           C  
-ANISOU 2003  CD1 TYR A 239     4244   3460   3354    149   -225   -191       C  
-ATOM   2004  CD2 TYR A 239       4.581 -40.744  36.839  1.00 31.18           C  
-ANISOU 2004  CD2 TYR A 239     4529   3624   3694    163   -326   -213       C  
-ATOM   2005  CE1 TYR A 239       4.306 -43.359  36.015  1.00 32.55           C  
-ANISOU 2005  CE1 TYR A 239     4669   3888   3811    128   -230   -187       C  
-ATOM   2006  CE2 TYR A 239       5.554 -41.674  37.155  1.00 36.96           C  
-ANISOU 2006  CE2 TYR A 239     5250   4348   4447    142   -331   -208       C  
-ATOM   2007  CZ  TYR A 239       5.408 -42.983  36.740  1.00 36.84           C  
-ANISOU 2007  CZ  TYR A 239     5218   4378   4403    125   -282   -196       C  
-ATOM   2008  OH  TYR A 239       6.367 -43.924  37.048  1.00 35.98           O  
-ANISOU 2008  OH  TYR A 239     5097   4259   4313    104   -287   -192       O  
-ATOM   2009  N   ASP A 240       1.868 -37.489  34.192  1.00 14.82           N  
-ANISOU 2009  N   ASP A 240     2448   1576   1606    199   -275   -180       N  
-ATOM   2010  CA  ASP A 240       1.081 -36.325  33.845  1.00 12.58           C  
-ANISOU 2010  CA  ASP A 240     2174   1289   1316    219   -279   -182       C  
-ATOM   2011  C   ASP A 240       0.957 -36.226  32.324  1.00 12.39           C  
-ANISOU 2011  C   ASP A 240     2114   1282   1312    197   -232   -144       C  
-ATOM   2012  O   ASP A 240      -0.039 -35.736  31.814  1.00 16.24           O  
-ANISOU 2012  O   ASP A 240     2606   1795   1770    211   -209   -142       O  
-ATOM   2013  CB  ASP A 240       1.707 -35.058  34.429  1.00 16.75           C  
-ANISOU 2013  CB  ASP A 240     2717   1753   1896    230   -345   -195       C  
-ATOM   2014  CG  ASP A 240       0.847 -33.831  34.232  1.00 19.21           C  
-ANISOU 2014  CG  ASP A 240     3043   2058   2197    255   -355   -201       C  
-ATOM   2015  OD1 ASP A 240      -0.329 -33.830  34.655  1.00 19.42           O  
-ANISOU 2015  OD1 ASP A 240     3097   2122   2160    284   -343   -225       O  
-ATOM   2016  OD2 ASP A 240       1.344 -32.856  33.644  1.00 20.11           O  
-ANISOU 2016  OD2 ASP A 240     3141   2132   2369    245   -373   -183       O  
-ATOM   2017  N   GLN A 241       1.957 -36.710  31.602  1.00  8.86           N  
-ANISOU 2017  N   GLN A 241     1631    824    912    164   -217   -114       N  
-ATOM   2018  CA  GLN A 241       1.888 -36.689  30.144  1.00 11.71           C  
-ANISOU 2018  CA  GLN A 241     1956   1204   1291    144   -171    -76       C  
-ATOM   2019  C   GLN A 241       0.636 -37.455  29.689  1.00 15.44           C  
-ANISOU 2019  C   GLN A 241     2430   1745   1692    151   -112    -77       C  
-ATOM   2020  O   GLN A 241      -0.116 -36.980  28.842  1.00 16.94           O  
-ANISOU 2020  O   GLN A 241     2611   1956   1869    156    -83    -64       O  
-ATOM   2021  CB  GLN A 241       3.156 -37.281  29.527  1.00 11.55           C  
-ANISOU 2021  CB  GLN A 241     1897   1166   1325    108   -161    -45       C  
-ATOM   2022  CG  GLN A 241       3.224 -37.165  27.999  1.00 10.08           C  
-ANISOU 2022  CG  GLN A 241     1670    995   1164     87   -118     -4       C  
-ATOM   2023  CD  GLN A 241       3.294 -35.719  27.517  1.00 15.13           C  
-ANISOU 2023  CD  GLN A 241     2302   1596   1848     91   -141     10       C  
-ATOM   2024  OE1 GLN A 241       3.742 -34.843  28.238  1.00 14.33           O  
-ANISOU 2024  OE1 GLN A 241     2218   1445   1781    101   -195     -4       O  
-ATOM   2025  NE2 GLN A 241       2.866 -35.477  26.283  1.00 15.43           N  
-ANISOU 2025  NE2 GLN A 241     2315   1659   1888     85   -100     38       N  
-ATOM   2026  N   LEU A 242       0.400 -38.633  30.263  1.00 10.57           N  
-ANISOU 2026  N   LEU A 242     1825   1162   1030    153    -96    -93       N  
-ATOM   2027  CA  LEU A 242      -0.772 -39.412  29.856  1.00 11.92           C  
-ANISOU 2027  CA  LEU A 242     1998   1398   1135    159    -42    -94       C  
-ATOM   2028  C   LEU A 242      -2.058 -38.715  30.280  1.00 14.50           C  
-ANISOU 2028  C   LEU A 242     2356   1743   1409    194    -46   -118       C  
-ATOM   2029  O   LEU A 242      -3.060 -38.769  29.557  1.00 13.00           O  
-ANISOU 2029  O   LEU A 242     2162   1596   1182    199     -3   -110       O  
-ATOM   2030  CB  LEU A 242      -0.719 -40.847  30.377  1.00 13.43           C  
-ANISOU 2030  CB  LEU A 242     2193   1621   1291    152    -24   -104       C  
-ATOM   2031  CG  LEU A 242      -1.835 -41.758  29.846  1.00  9.80           C  
-ANISOU 2031  CG  LEU A 242     1728   1227    768    154     35   -100       C  
-ATOM   2032  CD1 LEU A 242      -1.836 -41.826  28.313  1.00 11.99           C  
-ANISOU 2032  CD1 LEU A 242     1968   1524   1065    133     81    -65       C  
-ATOM   2033  CD2 LEU A 242      -1.733 -43.158  30.455  1.00 12.60           C  
-ANISOU 2033  CD2 LEU A 242     2088   1608   1091    147     47   -111       C  
-ATOM   2034  N   VAL A 243      -2.046 -38.061  31.443  1.00 12.11           N  
-ANISOU 2034  N   VAL A 243     2087   1410   1105    217    -98   -147       N  
-ATOM   2035  CA  VAL A 243      -3.229 -37.316  31.884  1.00 11.31           C  
-ANISOU 2035  CA  VAL A 243     2017   1323    957    252   -106   -171       C  
-ATOM   2036  C   VAL A 243      -3.546 -36.177  30.914  1.00 14.80           C  
-ANISOU 2036  C   VAL A 243     2447   1754   1423    254    -99   -153       C  
-ATOM   2037  O   VAL A 243      -4.704 -35.967  30.553  1.00 15.92           O  
-ANISOU 2037  O   VAL A 243     2597   1933   1520    270    -70   -155       O  
-ATOM   2038  CB  VAL A 243      -3.102 -36.776  33.329  1.00 11.56           C  
-ANISOU 2038  CB  VAL A 243     2086   1321    984    279   -167   -207       C  
-ATOM   2039  CG1 VAL A 243      -4.403 -36.048  33.741  1.00 12.86           C  
-ANISOU 2039  CG1 VAL A 243     2284   1507   1095    317   -172   -231       C  
-ATOM   2040  CG2 VAL A 243      -2.769 -37.915  34.315  1.00 16.59           C  
-ANISOU 2040  CG2 VAL A 243     2736   1970   1597    278   -174   -225       C  
-ATOM   2041  N   ARG A 244      -2.517 -35.458  30.476  1.00 13.14           N  
-ANISOU 2041  N   ARG A 244     2215   1493   1285    236   -124   -133       N  
-ATOM   2042  CA  ARG A 244      -2.696 -34.367  29.511  1.00 15.63           C  
-ANISOU 2042  CA  ARG A 244     2516   1794   1631    235   -119   -112       C  
-ATOM   2043  C   ARG A 244      -3.362 -34.881  28.252  1.00 15.75           C  
-ANISOU 2043  C   ARG A 244     2504   1860   1620    223    -53    -85       C  
-ATOM   2044  O   ARG A 244      -4.261 -34.246  27.707  1.00 12.85           O  
-ANISOU 2044  O   ARG A 244     2139   1512   1232    236    -34    -82       O  
-ATOM   2045  CB  ARG A 244      -1.350 -33.747  29.119  1.00 14.77           C  
-ANISOU 2045  CB  ARG A 244     2380   1626   1607    212   -150    -88       C  
-ATOM   2046  CG  ARG A 244      -0.552 -33.194  30.276  1.00 22.38           C  
-ANISOU 2046  CG  ARG A 244     3366   2533   2606    221   -217   -111       C  
-ATOM   2047  CD  ARG A 244      -1.248 -32.014  30.900  1.00 25.82           C  
-ANISOU 2047  CD  ARG A 244     3835   2950   3027    255   -255   -137       C  
-ATOM   2048  NE  ARG A 244      -0.450 -31.397  31.960  1.00 28.99           N  
-ANISOU 2048  NE  ARG A 244     4256   3292   3467    264   -323   -159       N  
-ATOM   2049  CZ  ARG A 244      -0.382 -30.084  32.165  1.00 36.40           C  
-ANISOU 2049  CZ  ARG A 244     5207   4186   4439    279   -368   -167       C  
-ATOM   2050  NH1 ARG A 244      -1.042 -29.255  31.362  1.00 37.52           N  
-ANISOU 2050  NH1 ARG A 244     5342   4334   4582    286   -351   -153       N  
-ATOM   2051  NH2 ARG A 244       0.350 -29.596  33.158  1.00 34.32           N  
-ANISOU 2051  NH2 ARG A 244     4961   3869   4208    288   -430   -188       N  
-ATOM   2052  N   ILE A 245      -2.894 -36.026  27.778  1.00 11.77           N  
-ANISOU 2052  N   ILE A 245     1975   1379   1119    197    -19    -67       N  
-ATOM   2053  CA  ILE A 245      -3.462 -36.637  26.580  1.00 12.87           C  
-ANISOU 2053  CA  ILE A 245     2088   1569   1234    184     44    -43       C  
-ATOM   2054  C   ILE A 245      -4.917 -37.034  26.838  1.00 14.62           C  
-ANISOU 2054  C   ILE A 245     2335   1846   1375    208     74    -64       C  
-ATOM   2055  O   ILE A 245      -5.809 -36.724  26.046  1.00 13.51           O  
-ANISOU 2055  O   ILE A 245     2188   1735   1210    215    108    -53       O  
-ATOM   2056  CB  ILE A 245      -2.660 -37.873  26.148  1.00 11.09           C  
-ANISOU 2056  CB  ILE A 245     1833   1356   1024    154     71    -23       C  
-ATOM   2057  CG1 ILE A 245      -1.258 -37.443  25.660  1.00 11.82           C  
-ANISOU 2057  CG1 ILE A 245     1895   1398   1198    128     48      4       C  
-ATOM   2058  CG2 ILE A 245      -3.423 -38.636  25.069  1.00 11.12           C  
-ANISOU 2058  CG2 ILE A 245     1816   1419    990    146    136     -5       C  
-ATOM   2059  CD1 ILE A 245      -0.274 -38.585  25.437  1.00 12.57           C  
-ANISOU 2059  CD1 ILE A 245     1964   1497   1316    100     63     20       C  
-ATOM   2060  N   ALA A 246      -5.154 -37.697  27.963  1.00 12.06           N  
-ANISOU 2060  N   ALA A 246     2038   1534   1010    222     60    -92       N  
-ATOM   2061  CA  ALA A 246      -6.508 -38.149  28.310  1.00 15.56           C  
-ANISOU 2061  CA  ALA A 246     2504   2031   1376    245     87   -112       C  
-ATOM   2062  C   ALA A 246      -7.532 -37.007  28.470  1.00 15.93           C  
-ANISOU 2062  C   ALA A 246     2577   2081   1396    276     75   -127       C  
-ATOM   2063  O   ALA A 246      -8.740 -37.196  28.245  1.00 13.93           O  
-ANISOU 2063  O   ALA A 246     2333   1876   1086    291    110   -132       O  
-ATOM   2064  CB  ALA A 246      -6.471 -39.007  29.552  1.00 11.17           C  
-ANISOU 2064  CB  ALA A 246     1973   1484    786    254     69   -139       C  
-ATOM   2065  N   LYS A 247      -7.062 -35.827  28.849  1.00 11.66           N  
-ANISOU 2065  N   LYS A 247     2046   1487    896    286     26   -135       N  
-ATOM   2066  CA  LYS A 247      -7.934 -34.645  28.914  1.00 12.20           C  
-ANISOU 2066  CA  LYS A 247     2136   1552    947    314     12   -147       C  
-ATOM   2067  C   LYS A 247      -8.454 -34.169  27.543  1.00 16.76           C  
-ANISOU 2067  C   LYS A 247     2689   2148   1531    307     53   -119       C  
-ATOM   2068  O   LYS A 247      -9.404 -33.388  27.463  1.00 17.83           O  
-ANISOU 2068  O   LYS A 247     2841   2296   1639    330     55   -127       O  
-ATOM   2069  CB  LYS A 247      -7.256 -33.496  29.671  1.00 17.22           C  
-ANISOU 2069  CB  LYS A 247     2790   2125   1630    327    -54   -163       C  
-ATOM   2070  CG  LYS A 247      -7.139 -33.748  31.176  1.00 16.66           C  
-ANISOU 2070  CG  LYS A 247     2754   2042   1535    347    -96   -199       C  
-ATOM   2071  CD  LYS A 247      -6.543 -32.566  31.918  1.00 21.58           C  
-ANISOU 2071  CD  LYS A 247     3396   2603   2202    362   -163   -216       C  
-ATOM   2072  CE  LYS A 247      -6.719 -32.738  33.424  1.00 30.61           C  
-ANISOU 2072  CE  LYS A 247     4579   3744   3309    390   -201   -256       C  
-ATOM   2073  NZ  LYS A 247      -5.992 -31.700  34.203  1.00 36.89           N  
-ANISOU 2073  NZ  LYS A 247     5391   4476   4150    403   -269   -274       N  
-ATOM   2074  N   VAL A 248      -7.840 -34.656  26.475  1.00 12.09           N  
-ANISOU 2074  N   VAL A 248     1686   1563   1344     75    -38    181       N  
-ATOM   2075  CA  VAL A 248      -8.200 -34.271  25.123  1.00 12.93           C  
-ANISOU 2075  CA  VAL A 248     1765   1704   1445     66    -29    193       C  
-ATOM   2076  C   VAL A 248      -8.879 -35.426  24.401  1.00 14.51           C  
-ANISOU 2076  C   VAL A 248     1945   1939   1630     32    -27    192       C  
-ATOM   2077  O   VAL A 248      -9.956 -35.253  23.824  1.00 15.30           O  
-ANISOU 2077  O   VAL A 248     2019   2086   1709     28    -18    211       O  
-ATOM   2078  CB  VAL A 248      -6.965 -33.818  24.318  1.00 14.10           C  
-ANISOU 2078  CB  VAL A 248     1914   1829   1616     65    -34    179       C  
-ATOM   2079  CG1 VAL A 248      -7.336 -33.536  22.865  1.00 11.84           C  
-ANISOU 2079  CG1 VAL A 248     1599   1583   1319     57    -23    192       C  
-ATOM   2080  CG2 VAL A 248      -6.328 -32.579  24.956  1.00 13.22           C  
-ANISOU 2080  CG2 VAL A 248     1819   1683   1523     96    -34    177       C  
-ATOM   2081  N   LEU A 249      -8.252 -36.598  24.427  1.00 10.40           N  
-ANISOU 2081  N   LEU A 249     1435   1397   1120      7    -35    169       N  
-ATOM   2082  CA  LEU A 249      -8.800 -37.773  23.752  1.00 11.45           C  
-ANISOU 2082  CA  LEU A 249     1551   1557   1243    -29    -33    162       C  
-ATOM   2083  C   LEU A 249      -9.828 -38.490  24.616  1.00 13.95           C  
-ANISOU 2083  C   LEU A 249     1869   1883   1547    -37    -26    171       C  
-ATOM   2084  O   LEU A 249     -10.607 -39.311  24.124  1.00 11.89           O  
-ANISOU 2084  O   LEU A 249     1589   1652   1277    -67    -21    169       O  
-ATOM   2085  CB  LEU A 249      -7.681 -38.755  23.370  1.00 14.12           C  
-ANISOU 2085  CB  LEU A 249     1901   1864   1600    -52    -40    133       C  
-ATOM   2086  CG  LEU A 249      -6.827 -38.430  22.142  1.00 15.35           C  
-ANISOU 2086  CG  LEU A 249     2047   2021   1764    -56    -43    121       C  
-ATOM   2087  CD1 LEU A 249      -6.036 -37.140  22.301  1.00 16.15           C  
-ANISOU 2087  CD1 LEU A 249     2156   2100   1879    -25    -45    128       C  
-ATOM   2088  CD2 LEU A 249      -5.871 -39.576  21.829  1.00 16.02           C  
-ANISOU 2088  CD2 LEU A 249     2143   2078   1866    -80    -47     93       C  
-ATOM   2089  N   GLY A 250      -9.820 -38.185  25.903  1.00 11.25           N  
-ANISOU 2089  N   GLY A 250     1549   1518   1208    -11    -27    180       N  
-ATOM   2090  CA  GLY A 250     -10.807 -38.741  26.815  1.00 12.99           C  
-ANISOU 2090  CA  GLY A 250     1771   1747   1417    -13    -18    194       C  
-ATOM   2091  C   GLY A 250     -10.363 -40.033  27.466  1.00 15.00           C  
-ANISOU 2091  C   GLY A 250     2047   1968   1684    -29    -18    180       C  
-ATOM   2092  O   GLY A 250      -9.541 -40.782  26.919  1.00 14.67           O  
-ANISOU 2092  O   GLY A 250     2011   1906   1658    -50    -23    158       O  
-ATOM   2093  N   THR A 251     -10.913 -40.307  28.643  1.00 14.90           N  
-ANISOU 2093  N   THR A 251     2048   1949   1664    -16    -11    194       N  
-ATOM   2094  CA  THR A 251     -10.521 -41.503  29.371  1.00 13.15           C  
-ANISOU 2094  CA  THR A 251     1848   1695   1454    -25     -8    187       C  
-ATOM   2095  C   THR A 251     -11.213 -42.780  28.884  1.00  8.74           C  
-ANISOU 2095  C   THR A 251     1274   1147    899    -67      6    184       C  
-ATOM   2096  O   THR A 251     -10.643 -43.864  28.999  1.00 14.97           O  
-ANISOU 2096  O   THR A 251     2078   1904   1704    -84      9    170       O  
-ATOM   2097  CB  THR A 251     -10.739 -41.352  30.888  1.00 14.93           C  
-ANISOU 2097  CB  THR A 251     2097   1907   1670      9     -4    204       C  
-ATOM   2098  OG1 THR A 251     -12.054 -40.846  31.128  1.00 12.69           O  
-ANISOU 2098  OG1 THR A 251     1796   1660   1367     17      9    229       O  
-ATOM   2099  CG2 THR A 251      -9.721 -40.383  31.483  1.00 16.79           C  
-ANISOU 2099  CG2 THR A 251     2355   2118   1908     47    -20    196       C  
-ATOM   2100  N   GLU A 252     -12.441 -42.687  28.371  1.00 12.44           N  
-ANISOU 2100  N   GLU A 252     1712   1661   1354    -86     16    196       N  
-ATOM   2101  CA  GLU A 252     -13.116 -43.925  27.956  1.00 12.07           C  
-ANISOU 2101  CA  GLU A 252     1649   1624   1313   -130     29    189       C  
-ATOM   2102  C   GLU A 252     -12.375 -44.625  26.814  1.00 14.45           C  
-ANISOU 2102  C   GLU A 252     1946   1914   1629   -163     23    157       C  
-ATOM   2103  O   GLU A 252     -12.242 -45.855  26.799  1.00 15.38           O  
-ANISOU 2103  O   GLU A 252     2072   2007   1764   -192     33    142       O  
-ATOM   2104  CB  GLU A 252     -14.589 -43.683  27.611  1.00 16.76           C  
-ANISOU 2104  CB  GLU A 252     2206   2273   1889   -144     39    206       C  
-ATOM   2105  CG  GLU A 252     -15.444 -43.419  28.844  1.00 24.41           C  
-ANISOU 2105  CG  GLU A 252     3179   3248   2847   -119     52    237       C  
-ATOM   2106  CD  GLU A 252     -15.562 -44.640  29.737  1.00 37.97           C  
-ANISOU 2106  CD  GLU A 252     4915   4934   4579   -132     69    241       C  
-ATOM   2107  OE1 GLU A 252     -16.125 -45.661  29.284  1.00 46.30           O  
-ANISOU 2107  OE1 GLU A 252     5951   5996   5644   -175     81    232       O  
-ATOM   2108  OE2 GLU A 252     -15.084 -44.585  30.890  1.00 37.25           O  
-ANISOU 2108  OE2 GLU A 252     4855   4809   4488    -99     70    252       O  
-ATOM   2109  N   ASP A 253     -11.865 -43.848  25.867  1.00 12.71           N  
-ANISOU 2109  N   ASP A 253     1716   1709   1404   -158     10    147       N  
-ATOM   2110  CA  ASP A 253     -11.094 -44.438  24.779  1.00 14.01           C  
-ANISOU 2110  CA  ASP A 253     1878   1863   1580   -185      4    117       C  
-ATOM   2111  C   ASP A 253      -9.712 -44.927  25.211  1.00 13.90           C  
-ANISOU 2111  C   ASP A 253     1898   1792   1589   -174      0    102       C  
-ATOM   2112  O   ASP A 253      -9.160 -45.855  24.610  1.00 15.55           O  
-ANISOU 2112  O   ASP A 253     2112   1982   1813   -201      2     77       O  
-ATOM   2113  CB  ASP A 253     -11.026 -43.498  23.582  1.00 12.33           C  
-ANISOU 2113  CB  ASP A 253     1642   1689   1355   -182     -6    114       C  
-ATOM   2114  CG  ASP A 253     -12.383 -43.335  22.908  1.00 17.70           C  
-ANISOU 2114  CG  ASP A 253     2283   2431   2011   -201     -1    123       C  
-ATOM   2115  OD1 ASP A 253     -13.127 -44.333  22.818  1.00 21.86           O  
-ANISOU 2115  OD1 ASP A 253     2796   2970   2538   -237      8    114       O  
-ATOM   2116  OD2 ASP A 253     -12.707 -42.208  22.503  1.00 18.37           O  
-ANISOU 2116  OD2 ASP A 253     2350   2553   2078   -180     -5    140       O  
-ATOM   2117  N   LEU A 254      -9.172 -44.327  26.266  1.00 14.24           N  
-ANISOU 2117  N   LEU A 254     1965   1810   1635   -135     -7    115       N  
-ATOM   2118  CA  LEU A 254      -7.936 -44.831  26.858  1.00 17.65           C  
-ANISOU 2118  CA  LEU A 254     2428   2193   2086   -122    -11    104       C  
-ATOM   2119  C   LEU A 254      -8.210 -46.203  27.447  1.00 17.43           C  
-ANISOU 2119  C   LEU A 254     2413   2140   2069   -140      5    105       C  
-ATOM   2120  O   LEU A 254      -7.431 -47.139  27.248  1.00 17.70           O  
-ANISOU 2120  O   LEU A 254     2462   2141   2122   -153      9     87       O  
-ATOM   2121  CB  LEU A 254      -7.403 -43.889  27.936  1.00 13.92           C  
-ANISOU 2121  CB  LEU A 254     1975   1704   1610    -77    -23    117       C  
-ATOM   2122  CG  LEU A 254      -6.195 -44.374  28.745  1.00 16.16           C  
-ANISOU 2122  CG  LEU A 254     2289   1943   1910    -57    -30    109       C  
-ATOM   2123  CD1 LEU A 254      -5.041 -44.737  27.821  1.00 17.48           C  
-ANISOU 2123  CD1 LEU A 254     2456   2090   2096    -71    -37     83       C  
-ATOM   2124  CD2 LEU A 254      -5.801 -43.286  29.707  1.00 15.23           C  
-ANISOU 2124  CD2 LEU A 254     2183   1818   1784    -15    -44    117       C  
-ATOM   2125  N   TYR A 255      -9.322 -46.337  28.165  1.00 15.47           N  
-ANISOU 2125  N   TYR A 255     2161   1907   1810   -140     18    126       N  
-ATOM   2126  CA  TYR A 255      -9.672 -47.645  28.704  1.00 14.01           C  
-ANISOU 2126  CA  TYR A 255     1988   1699   1639   -159     39    130       C  
-ATOM   2127  C   TYR A 255      -9.949 -48.666  27.596  1.00 15.80           C  
-ANISOU 2127  C   TYR A 255     2198   1928   1878   -210     51    106       C  
-ATOM   2128  O   TYR A 255      -9.550 -49.825  27.714  1.00 17.25           O  
-ANISOU 2128  O   TYR A 255     2398   2073   2083   -226     65     96       O  
-ATOM   2129  CB  TYR A 255     -10.823 -47.563  29.713  1.00 11.64           C  
-ANISOU 2129  CB  TYR A 255     1684   1414   1324   -148     53    160       C  
-ATOM   2130  CG  TYR A 255     -10.342 -47.244  31.116  1.00 14.69           C  
-ANISOU 2130  CG  TYR A 255     2101   1777   1705   -100     50    180       C  
-ATOM   2131  CD1 TYR A 255      -9.822 -48.239  31.925  1.00 19.00           C  
-ANISOU 2131  CD1 TYR A 255     2674   2282   2264    -92     62    185       C  
-ATOM   2132  CD2 TYR A 255     -10.398 -45.949  31.629  1.00 21.03           C  
-ANISOU 2132  CD2 TYR A 255     2905   2599   2488    -62     36    193       C  
-ATOM   2133  CE1 TYR A 255      -9.373 -47.966  33.202  1.00 21.87           C  
-ANISOU 2133  CE1 TYR A 255     3064   2630   2618    -46     57    202       C  
-ATOM   2134  CE2 TYR A 255      -9.951 -45.669  32.916  1.00 19.68           C  
-ANISOU 2134  CE2 TYR A 255     2761   2409   2308    -20     32    206       C  
-ATOM   2135  CZ  TYR A 255      -9.441 -46.687  33.694  1.00 23.45           C  
-ANISOU 2135  CZ  TYR A 255     3263   2851   2796    -11     41    210       C  
-ATOM   2136  OH  TYR A 255      -8.991 -46.440  34.979  1.00 28.51           O  
-ANISOU 2136  OH  TYR A 255     3930   3478   3423     33     35    223       O  
-ATOM   2137  N   ASP A 256     -10.613 -48.245  26.519  1.00 14.06           N  
-ANISOU 2137  N   ASP A 256     1944   1752   1645   -234     46     97       N  
-ATOM   2138  CA  ASP A 256     -10.837 -49.147  25.387  1.00 12.60           C  
-ANISOU 2138  CA  ASP A 256     1743   1576   1470   -283     54     68       C  
-ATOM   2139  C   ASP A 256      -9.503 -49.667  24.829  1.00 15.19           C  
-ANISOU 2139  C   ASP A 256     2090   1866   1816   -287     49     41       C  
-ATOM   2140  O   ASP A 256      -9.389 -50.829  24.451  1.00 16.15           O  
-ANISOU 2140  O   ASP A 256     2217   1964   1957   -320     63     19       O  
-ATOM   2141  CB  ASP A 256     -11.585 -48.454  24.254  1.00 15.74           C  
-ANISOU 2141  CB  ASP A 256     2101   2034   1845   -301     44     62       C  
-ATOM   2142  CG  ASP A 256     -13.069 -48.238  24.549  1.00 19.83           C  
-ANISOU 2142  CG  ASP A 256     2592   2596   2348   -310     52     83       C  
-ATOM   2143  OD1 ASP A 256     -13.626 -48.836  25.501  1.00 17.04           O  
-ANISOU 2143  OD1 ASP A 256     2247   2225   2004   -314     69     99       O  
-ATOM   2144  OD2 ASP A 256     -13.683 -47.461  23.788  1.00 24.75           O  
-ANISOU 2144  OD2 ASP A 256     3183   3273   2948   -313     42     86       O  
-ATOM   2145  N   TYR A 257      -8.517 -48.774  24.752  1.00 15.49           N  
-ANISOU 2145  N   TYR A 257     2138   1898   1850   -254     31     42       N  
-ATOM   2146  CA  TYR A 257      -7.181 -49.080  24.248  1.00 16.94           C  
-ANISOU 2146  CA  TYR A 257     2337   2049   2050   -251     25     19       C  
-ATOM   2147  C   TYR A 257      -6.490 -50.118  25.116  1.00 16.68           C  
-ANISOU 2147  C   TYR A 257     2336   1960   2040   -243     37     20       C  
-ATOM   2148  O   TYR A 257      -6.088 -51.176  24.634  1.00 17.14           O  
-ANISOU 2148  O   TYR A 257     2403   1992   2117   -268     49     -2       O  
-ATOM   2149  CB  TYR A 257      -6.340 -47.803  24.199  1.00 15.96           C  
-ANISOU 2149  CB  TYR A 257     2215   1931   1919   -214      4     25       C  
-ATOM   2150  CG  TYR A 257      -4.899 -47.994  23.768  1.00 19.32           C  
-ANISOU 2150  CG  TYR A 257     2654   2323   2361   -207     -3      6       C  
-ATOM   2151  CD1 TYR A 257      -4.584 -48.768  22.650  1.00 15.97           C  
-ANISOU 2151  CD1 TYR A 257     2225   1896   1945   -238      4    -22       C  
-ATOM   2152  CD2 TYR A 257      -3.855 -47.373  24.451  1.00 16.61           C  
-ANISOU 2152  CD2 TYR A 257     2329   1957   2026   -168    -16     13       C  
-ATOM   2153  CE1 TYR A 257      -3.263 -48.936  22.234  1.00 17.06           C  
-ANISOU 2153  CE1 TYR A 257     2376   2007   2100   -229     -1    -39       C  
-ATOM   2154  CE2 TYR A 257      -2.520 -47.542  24.039  1.00 19.24           C  
-ANISOU 2154  CE2 TYR A 257     2672   2263   2377   -161    -22     -4       C  
-ATOM   2155  CZ  TYR A 257      -2.245 -48.326  22.923  1.00 20.90           C  
-ANISOU 2155  CZ  TYR A 257     2877   2470   2595   -191    -13    -29       C  
-ATOM   2156  OH  TYR A 257      -0.956 -48.510  22.463  1.00 17.11           O  
-ANISOU 2156  OH  TYR A 257     2405   1965   2132   -184    -17    -45       O  
-ATOM   2157  N   ILE A 258      -6.349 -49.829  26.403  1.00 14.21           N  
-ANISOU 2157  N   ILE A 258     2042   1631   1726   -207     35     45       N  
-ATOM   2158  CA  ILE A 258      -5.643 -50.769  27.263  1.00 10.14           C  
-ANISOU 2158  CA  ILE A 258     1557   1066   1229   -193     46     49       C  
-ATOM   2159  C   ILE A 258      -6.434 -52.077  27.368  1.00 18.57           C  
-ANISOU 2159  C   ILE A 258     2627   2117   2311   -227     75     49       C  
-ATOM   2160  O   ILE A 258      -5.855 -53.152  27.504  1.00 17.83           O  
-ANISOU 2160  O   ILE A 258     2554   1980   2239   -232     91     43       O  
-ATOM   2161  CB  ILE A 258      -5.315 -50.188  28.660  1.00 17.19           C  
-ANISOU 2161  CB  ILE A 258     2469   1949   2113   -144     37     76       C  
-ATOM   2162  CG1 ILE A 258      -6.582 -49.899  29.460  1.00 18.49           C  
-ANISOU 2162  CG1 ILE A 258     2627   2137   2260   -139     45    103       C  
-ATOM   2163  CG2 ILE A 258      -4.441 -48.930  28.538  1.00 16.83           C  
-ANISOU 2163  CG2 ILE A 258     2421   1914   2060   -114      9     71       C  
-ATOM   2164  CD1 ILE A 258      -6.303 -49.615  30.911  1.00 21.81           C  
-ANISOU 2164  CD1 ILE A 258     3071   2544   2671    -93     41    127       C  
-ATOM   2165  N   ASP A 259      -7.759 -51.985  27.293  1.00 14.49           N  
-ANISOU 2165  N   ASP A 259     2089   1634   1784   -250     84     58       N  
-ATOM   2166  CA  ASP A 259      -8.585 -53.190  27.362  1.00 10.77           C  
-ANISOU 2166  CA  ASP A 259     1616   1148   1329   -287    113     56       C  
-ATOM   2167  C   ASP A 259      -8.388 -54.069  26.135  1.00 15.75           C  
-ANISOU 2167  C   ASP A 259     2240   1767   1977   -333    122     18       C  
-ATOM   2168  O   ASP A 259      -8.349 -55.295  26.241  1.00 16.39           O  
-ANISOU 2168  O   ASP A 259     2336   1809   2084   -355    148     10       O  
-ATOM   2169  CB  ASP A 259     -10.071 -52.841  27.510  1.00 13.74           C  
-ANISOU 2169  CB  ASP A 259     1965   1567   1688   -304    119     72       C  
-ATOM   2170  CG  ASP A 259     -10.432 -52.398  28.912  1.00 17.44           C  
-ANISOU 2170  CG  ASP A 259     2446   2036   2146   -264    123    111       C  
-ATOM   2171  OD1 ASP A 259      -9.578 -52.489  29.819  1.00 17.27           O  
-ANISOU 2171  OD1 ASP A 259     2455   1979   2128   -227    122    125       O  
-ATOM   2172  OD2 ASP A 259     -11.594 -51.989  29.114  1.00 20.10           O  
-ANISOU 2172  OD2 ASP A 259     2761   2409   2467   -271    127    128       O  
-ATOM   2173  N   LYS A 260      -8.288 -53.441  24.970  1.00 16.45           N  
-ANISOU 2173  N   LYS A 260     2307   1893   2052   -346    103     -5       N  
-ATOM   2174  CA  LYS A 260      -8.050 -54.174  23.730  1.00 18.59           C  
-ANISOU 2174  CA  LYS A 260     2571   2159   2334   -386    109    -45       C  
-ATOM   2175  C   LYS A 260      -6.789 -55.020  23.795  1.00 18.35           C  
-ANISOU 2175  C   LYS A 260     2573   2070   2330   -377    119    -58       C  
-ATOM   2176  O   LYS A 260      -6.776 -56.145  23.307  1.00 20.25           O  
-ANISOU 2176  O   LYS A 260     2818   2283   2591   -411    140    -83       O  
-ATOM   2177  CB  LYS A 260      -7.973 -53.228  22.528  1.00 22.54           C  
-ANISOU 2177  CB  LYS A 260     3044   2709   2810   -391     85    -62       C  
-ATOM   2178  CG  LYS A 260      -7.436 -53.912  21.284  1.00 18.05           C  
-ANISOU 2178  CG  LYS A 260     2475   2133   2251   -422     89   -103       C  
-ATOM   2179  CD  LYS A 260      -7.580 -53.048  20.041  1.00 24.81           C  
-ANISOU 2179  CD  LYS A 260     3301   3047   3080   -429     69   -119       C  
-ATOM   2180  CE  LYS A 260      -6.770 -53.635  18.886  1.00 24.53           C  
-ANISOU 2180  CE  LYS A 260     3269   2999   3051   -449     71   -158       C  
-ATOM   2181  NZ  LYS A 260      -6.780 -52.754  17.696  1.00 25.15           N  
-ANISOU 2181  NZ  LYS A 260     3321   3134   3101   -449     53   -169       N  
-ATOM   2182  N   TYR A 261      -5.734 -54.476  24.401  1.00 15.81           N  
-ANISOU 2182  N   TYR A 261     2271   1730   2008   -330    105    -41       N  
-ATOM   2183  CA  TYR A 261      -4.447 -55.171  24.486  1.00 16.61           C  
-ANISOU 2183  CA  TYR A 261     2400   1780   2132   -314    112    -50       C  
-ATOM   2184  C   TYR A 261      -4.249 -55.887  25.819  1.00 18.36           C  
-ANISOU 2184  C   TYR A 261     2650   1956   2370   -289    131    -22       C  
-ATOM   2185  O   TYR A 261      -3.162 -56.416  26.104  1.00 18.74           O  
-ANISOU 2185  O   TYR A 261     2723   1963   2436   -266    137    -22       O  
-ATOM   2186  CB  TYR A 261      -3.311 -54.191  24.198  1.00 13.37           C  
-ANISOU 2186  CB  TYR A 261     1989   1378   1712   -280     85    -52       C  
-ATOM   2187  CG  TYR A 261      -3.402 -53.696  22.780  1.00 12.86           C  
-ANISOU 2187  CG  TYR A 261     1899   1353   1635   -305     73    -79       C  
-ATOM   2188  CD1 TYR A 261      -2.903 -54.460  21.727  1.00 16.26           C  
-ANISOU 2188  CD1 TYR A 261     2332   1769   2078   -331     83   -112       C  
-ATOM   2189  CD2 TYR A 261      -4.033 -52.488  22.482  1.00 13.21           C  
-ANISOU 2189  CD2 TYR A 261     1917   1449   1652   -302     55    -70       C  
-ATOM   2190  CE1 TYR A 261      -3.015 -54.031  20.421  1.00 17.30           C  
-ANISOU 2190  CE1 TYR A 261     2440   1940   2193   -353     74   -137       C  
-ATOM   2191  CE2 TYR A 261      -4.139 -52.044  21.176  1.00 14.91           C  
-ANISOU 2191  CE2 TYR A 261     2109   1704   1853   -321     46    -91       C  
-ATOM   2192  CZ  TYR A 261      -3.628 -52.818  20.150  1.00 18.46           C  
-ANISOU 2192  CZ  TYR A 261     2561   2141   2313   -347     54   -125       C  
-ATOM   2193  OH  TYR A 261      -3.734 -52.382  18.848  1.00 16.58           O  
-ANISOU 2193  OH  TYR A 261     2298   1945   2056   -364     46   -145       O  
-ATOM   2194  N   ASN A 262      -5.318 -55.924  26.614  1.00 20.95           N  
-ANISOU 2194  N   ASN A 262     2974   2293   2691   -292    142      2       N  
-ATOM   2195  CA  ASN A 262      -5.294 -56.560  27.925  1.00 20.67           C  
-ANISOU 2195  CA  ASN A 262     2965   2221   2668   -267    162     33       C  
-ATOM   2196  C   ASN A 262      -4.110 -56.040  28.749  1.00 22.84           C  
-ANISOU 2196  C   ASN A 262     3260   2482   2936   -210    144     51       C  
-ATOM   2197  O   ASN A 262      -3.388 -56.816  29.369  1.00 24.99           O  
-ANISOU 2197  O   ASN A 262     3559   2713   3225   -187    158     63       O  
-ATOM   2198  CB  ASN A 262      -5.244 -58.090  27.790  1.00 19.62           C  
-ANISOU 2198  CB  ASN A 262     2849   2036   2568   -295    199     22       C  
-ATOM   2199  CG  ASN A 262      -6.526 -58.687  27.205  1.00 24.72           C  
-ANISOU 2199  CG  ASN A 262     3475   2693   3224   -353    221      5       C  
-ATOM   2200  OD1 ASN A 262      -7.435 -57.976  26.769  1.00 31.16           O  
-ANISOU 2200  OD1 ASN A 262     4261   3560   4020   -374    207     -1       O  
-ATOM   2201  ND2 ASN A 262      -6.593 -60.010  27.190  1.00 30.97           N  
-ANISOU 2201  ND2 ASN A 262     4283   3437   4049   -379    257     -4       N  
-ATOM   2202  N   ILE A 263      -3.931 -54.717  28.717  1.00 24.17           N  
-ANISOU 2202  N   ILE A 263     3415   2688   3080   -187    112     53       N  
-ATOM   2203  CA  ILE A 263      -2.900 -53.986  29.450  1.00 21.22           C  
-ANISOU 2203  CA  ILE A 263     3054   2311   2696   -136     88     66       C  
-ATOM   2204  C   ILE A 263      -3.539 -53.438  30.719  1.00 25.67           C  
-ANISOU 2204  C   ILE A 263     3623   2892   3240   -106     85     98       C  
-ATOM   2205  O   ILE A 263      -4.717 -53.070  30.720  1.00 29.14           O  
-ANISOU 2205  O   ILE A 263     4046   3361   3666   -123     89    107       O  
-ATOM   2206  CB  ILE A 263      -2.423 -52.744  28.657  1.00 25.79           C  
-ANISOU 2206  CB  ILE A 263     3614   2923   3263   -132     57     48       C  
-ATOM   2207  CG1 ILE A 263      -1.774 -53.120  27.324  1.00 28.90           C  
-ANISOU 2207  CG1 ILE A 263     4000   3307   3672   -159     58     16       C  
-ATOM   2208  CG2 ILE A 263      -1.459 -51.899  29.479  1.00 29.30           C  
-ANISOU 2208  CG2 ILE A 263     4068   3366   3698    -83     32     59       C  
-ATOM   2209  CD1 ILE A 263      -1.470 -51.903  26.465  1.00 27.83           C  
-ANISOU 2209  CD1 ILE A 263     3843   3206   3524   -158     33      2       C  
-ATOM   2210  N   GLU A 264      -2.765 -53.361  31.793  1.00 17.83           N  
-ANISOU 2210  N   GLU A 264     2650   1883   2241    -60     77    116       N  
-ATOM   2211  CA  GLU A 264      -3.236 -52.734  33.013  1.00 24.93           C  
-ANISOU 2211  CA  GLU A 264     3555   2801   3116    -26     70    144       C  
-ATOM   2212  C   GLU A 264      -2.507 -51.410  33.238  1.00 24.75           C  
-ANISOU 2212  C   GLU A 264     3528   2800   3076      8     34    137       C  
-ATOM   2213  O   GLU A 264      -1.284 -51.359  33.152  1.00 25.73           O  
-ANISOU 2213  O   GLU A 264     3658   2909   3208     26     19    124       O  
-ATOM   2214  CB  GLU A 264      -2.981 -53.680  34.180  1.00 29.60           C  
-ANISOU 2214  CB  GLU A 264     4174   3361   3712      4     90    171       C  
-ATOM   2215  CG  GLU A 264      -3.625 -53.267  35.462  1.00 34.03           C  
-ANISOU 2215  CG  GLU A 264     4742   3940   4246     37     91    202       C  
-ATOM   2216  CD  GLU A 264      -3.897 -54.454  36.355  1.00 37.05           C  
-ANISOU 2216  CD  GLU A 264     5147   4293   4637     50    126    233       C  
-ATOM   2217  OE1 GLU A 264      -3.001 -55.323  36.490  1.00 36.76           O  
-ANISOU 2217  OE1 GLU A 264     5129   4222   4617     64    136    236       O  
-ATOM   2218  OE2 GLU A 264      -5.017 -54.520  36.902  1.00 38.19           O  
-ANISOU 2218  OE2 GLU A 264     5290   4450   4771     46    145    256       O  
-ATOM   2219  N   LEU A 265      -3.252 -50.339  33.509  1.00 21.44           N  
-ANISOU 2219  N   LEU A 265     3097   2415   2634     15     23    145       N  
-ATOM   2220  CA  LEU A 265      -2.634 -49.062  33.845  1.00 23.13           C  
-ANISOU 2220  CA  LEU A 265     3309   2646   2832     48     -8    138       C  
-ATOM   2221  C   LEU A 265      -1.882 -49.174  35.170  1.00 22.61           C  
-ANISOU 2221  C   LEU A 265     3266   2567   2756     95    -17    151       C  
-ATOM   2222  O   LEU A 265      -2.321 -49.869  36.080  1.00 28.20           O  
-ANISOU 2222  O   LEU A 265     3991   3268   3457    110      1    176       O  
-ATOM   2223  CB  LEU A 265      -3.680 -47.945  33.981  1.00 25.27           C  
-ANISOU 2223  CB  LEU A 265     3566   2953   3081     49    -14    146       C  
-ATOM   2224  CG  LEU A 265      -4.121 -47.107  32.785  1.00 21.23           C  
-ANISOU 2224  CG  LEU A 265     3028   2468   2570     21    -21    132       C  
-ATOM   2225  CD1 LEU A 265      -4.877 -45.903  33.296  1.00 22.47           C  
-ANISOU 2225  CD1 LEU A 265     3179   2656   2704     41    -28    144       C  
-ATOM   2226  CD2 LEU A 265      -2.928 -46.678  31.935  1.00 24.36           C  
-ANISOU 2226  CD2 LEU A 265     3418   2855   2981     19    -40    106       C  
-ATOM   2227  N   ASP A 266      -0.755 -48.481  35.268  1.00 20.39           N  
-ANISOU 2227  N   ASP A 266     2986   2286   2475    119    -45    135       N  
-ATOM   2228  CA  ASP A 266      -0.071 -48.294  36.542  1.00 23.03           C  
-ANISOU 2228  CA  ASP A 266     3337   2620   2793    167    -61    143       C  
-ATOM   2229  C   ASP A 266      -1.109 -47.812  37.556  1.00 24.91           C  
-ANISOU 2229  C   ASP A 266     3581   2880   3001    187    -57    164       C  
-ATOM   2230  O   ASP A 266      -1.856 -46.870  37.277  1.00 22.29           O  
-ANISOU 2230  O   ASP A 266     3237   2572   2661    176    -61    160       O  
-ATOM   2231  CB  ASP A 266       1.025 -47.243  36.367  1.00 22.24           C  
-ANISOU 2231  CB  ASP A 266     3228   2527   2696    181    -95    116       C  
-ATOM   2232  CG  ASP A 266       1.930 -47.117  37.573  1.00 23.26           C  
-ANISOU 2232  CG  ASP A 266     3371   2658   2811    227   -116    117       C  
-ATOM   2233  OD1 ASP A 266       1.467 -47.301  38.716  1.00 23.74           O  
-ANISOU 2233  OD1 ASP A 266     3447   2726   2846    256   -110    139       O  
-ATOM   2234  OD2 ASP A 266       3.114 -46.797  37.376  1.00 27.48           O  
-ANISOU 2234  OD2 ASP A 266     3898   3187   3356    236   -138     96       O  
-ATOM   2235  N   PRO A 267      -1.178 -48.462  38.733  1.00 22.66           N  
-ANISOU 2235  N   PRO A 267     3317   2591   2702    219    -46    189       N  
-ATOM   2236  CA  PRO A 267      -2.197 -48.064  39.712  1.00 21.53           C  
-ANISOU 2236  CA  PRO A 267     3182   2470   2529    239    -38    211       C  
-ATOM   2237  C   PRO A 267      -2.005 -46.636  40.219  1.00 24.28           C  
-ANISOU 2237  C   PRO A 267     3527   2843   2854    267    -68    196       C  
-ATOM   2238  O   PRO A 267      -2.919 -46.071  40.826  1.00 24.50           O  
-ANISOU 2238  O   PRO A 267     3558   2893   2859    280    -63    209       O  
-ATOM   2239  CB  PRO A 267      -2.010 -49.076  40.855  1.00 20.50           C  
-ANISOU 2239  CB  PRO A 267     3075   2328   2387    274    -23    240       C  
-ATOM   2240  CG  PRO A 267      -0.622 -49.587  40.685  1.00 23.66           C  
-ANISOU 2240  CG  PRO A 267     3480   2707   2804    285    -36    226       C  
-ATOM   2241  CD  PRO A 267      -0.386 -49.610  39.198  1.00 21.88           C  
-ANISOU 2241  CD  PRO A 267     3236   2467   2611    239    -37    201       C  
-ATOM   2242  N   ARG A 268      -0.839 -46.047  39.979  1.00 20.69           N  
-ANISOU 2242  N   ARG A 268     3067   2386   2407    274    -97    168       N  
-ATOM   2243  CA  ARG A 268      -0.633 -44.675  40.429  1.00 25.72           C  
-ANISOU 2243  CA  ARG A 268     3701   3042   3027    296   -124    149       C  
-ATOM   2244  C   ARG A 268      -1.552 -43.691  39.690  1.00 26.54           C  
-ANISOU 2244  C   ARG A 268     3789   3161   3134    271   -120    143       C  
-ATOM   2245  O   ARG A 268      -1.749 -42.565  40.143  1.00 27.62           O  
-ANISOU 2245  O   ARG A 268     3926   3313   3254    289   -132    135       O  
-ATOM   2246  CB  ARG A 268       0.836 -44.256  40.327  1.00 34.61           C  
-ANISOU 2246  CB  ARG A 268     4823   4162   4166    308   -156    118       C  
-ATOM   2247  CG  ARG A 268       1.291 -43.847  38.947  1.00 40.62           C  
-ANISOU 2247  CG  ARG A 268     5564   4913   4959    272   -162     95       C  
-ATOM   2248  CD  ARG A 268       2.733 -43.367  38.992  1.00 44.75           C  
-ANISOU 2248  CD  ARG A 268     6080   5430   5493    286   -193     66       C  
-ATOM   2249  NE  ARG A 268       3.676 -44.479  39.065  1.00 46.97           N  
-ANISOU 2249  NE  ARG A 268     6366   5695   5785    294   -194     69       N  
-ATOM   2250  CZ  ARG A 268       4.838 -44.428  39.704  1.00 47.02           C  
-ANISOU 2250  CZ  ARG A 268     6373   5704   5787    323   -219     56       C  
-ATOM   2251  NH1 ARG A 268       5.200 -43.322  40.345  1.00 46.62           N  
-ANISOU 2251  NH1 ARG A 268     6320   5670   5724    344   -246     34       N  
-ATOM   2252  NH2 ARG A 268       5.635 -45.487  39.710  1.00 45.27           N  
-ANISOU 2252  NH2 ARG A 268     6156   5469   5577    333   -216     63       N  
-ATOM   2253  N   PHE A 269      -2.116 -44.126  38.564  1.00 23.57           N  
-ANISOU 2253  N   PHE A 269     3398   2779   2777    230   -101    148       N  
-ATOM   2254  CA  PHE A 269      -3.081 -43.310  37.827  1.00 16.00           C  
-ANISOU 2254  CA  PHE A 269     2422   1838   1818    208    -93    148       C  
-ATOM   2255  C   PHE A 269      -4.441 -43.243  38.515  1.00 24.46           C  
-ANISOU 2255  C   PHE A 269     3498   2931   2866    217    -74    176       C  
-ATOM   2256  O   PHE A 269      -5.276 -42.417  38.153  1.00 27.65           O  
-ANISOU 2256  O   PHE A 269     3888   3354   3264    209    -69    179       O  
-ATOM   2257  CB  PHE A 269      -3.252 -43.815  36.394  1.00 20.28           C  
-ANISOU 2257  CB  PHE A 269     2946   2375   2386    162    -81    143       C  
-ATOM   2258  CG  PHE A 269      -2.112 -43.453  35.480  1.00 21.32           C  
-ANISOU 2258  CG  PHE A 269     3067   2494   2540    151    -99    116       C  
-ATOM   2259  CD1 PHE A 269      -2.002 -42.175  34.964  1.00 20.05           C  
-ANISOU 2259  CD1 PHE A 269     2892   2344   2382    149   -112    101       C  
-ATOM   2260  CD2 PHE A 269      -1.173 -44.403  35.110  1.00 20.43           C  
-ANISOU 2260  CD2 PHE A 269     2957   2358   2447    141   -100    107       C  
-ATOM   2261  CE1 PHE A 269      -0.964 -41.835  34.107  1.00 19.32           C  
-ANISOU 2261  CE1 PHE A 269     2789   2240   2312    138   -126     79       C  
-ATOM   2262  CE2 PHE A 269      -0.128 -44.074  34.254  1.00 22.16           C  
-ANISOU 2262  CE2 PHE A 269     3165   2566   2687    131   -115     83       C  
-ATOM   2263  CZ  PHE A 269      -0.026 -42.781  33.753  1.00 18.43           C  
-ANISOU 2263  CZ  PHE A 269     2679   2107   2218    129   -128     69       C  
-ATOM   2264  N   ASN A 270      -4.663 -44.102  39.506  1.00 22.09           N  
-ANISOU 2264  N   ASN A 270     3215   2626   2552    237    -60    198       N  
-ATOM   2265  CA  ASN A 270      -5.940 -44.125  40.223  1.00 22.61           C  
-ANISOU 2265  CA  ASN A 270     3286   2711   2595    248    -39    227       C  
-ATOM   2266  C   ASN A 270      -6.310 -42.791  40.865  1.00 29.10           C  
-ANISOU 2266  C   ASN A 270     4110   3556   3391    277    -50    224       C  
-ATOM   2267  O   ASN A 270      -7.489 -42.437  40.933  1.00 28.26           O  
-ANISOU 2267  O   ASN A 270     3995   3469   3272    275    -33    242       O  
-ATOM   2268  CB  ASN A 270      -5.948 -45.221  41.296  1.00 31.94           C  
-ANISOU 2268  CB  ASN A 270     4489   3883   3765    271    -22    252       C  
-ATOM   2269  CG  ASN A 270      -6.036 -46.623  40.710  1.00 36.06           C  
-ANISOU 2269  CG  ASN A 270     5008   4381   4313    238      2    263       C  
-ATOM   2270  OD1 ASN A 270      -6.577 -46.824  39.624  1.00 34.58           O  
-ANISOU 2270  OD1 ASN A 270     4801   4194   4145    195     14    259       O  
-ATOM   2271  ND2 ASN A 270      -5.509 -47.602  41.441  1.00 39.76           N  
-ANISOU 2271  ND2 ASN A 270     5496   4830   4780    260     11    278       N  
-ATOM   2272  N   ASP A 271      -5.307 -42.057  41.344  1.00 23.41           N  
-ANISOU 2272  N   ASP A 271     3399   2831   2663    305    -78    200       N  
-ATOM   2273  CA  ASP A 271      -5.547 -40.795  42.042  1.00 31.26           C  
-ANISOU 2273  CA  ASP A 271     4400   3843   3634    336    -89    192       C  
-ATOM   2274  C   ASP A 271      -5.306 -39.549  41.195  1.00 30.11           C  
-ANISOU 2274  C   ASP A 271     4239   3697   3504    322   -103    166       C  
-ATOM   2275  O   ASP A 271      -5.473 -38.429  41.685  1.00 32.25           O  
-ANISOU 2275  O   ASP A 271     4515   3978   3760    345   -111    156       O  
-ATOM   2276  CB  ASP A 271      -4.685 -40.708  43.303  1.00 44.70           C  
-ANISOU 2276  CB  ASP A 271     6125   5545   5314    379   -109    180       C  
-ATOM   2277  CG  ASP A 271      -5.034 -41.774  44.321  1.00 57.48           C  
-ANISOU 2277  CG  ASP A 271     7762   7169   6910    403    -92    211       C  
-ATOM   2278  OD1 ASP A 271      -6.134 -42.362  44.220  1.00 57.84           O  
-ANISOU 2278  OD1 ASP A 271     7804   7220   6955    389    -62    243       O  
-ATOM   2279  OD2 ASP A 271      -4.206 -42.019  45.224  1.00 65.78           O  
-ANISOU 2279  OD2 ASP A 271     8830   8220   7944    437   -108    206       O  
-ATOM   2280  N   ILE A 272      -4.902 -39.729  39.939  1.00 25.96           N  
-ANISOU 2280  N   ILE A 272     3695   3160   3009    286   -105    155       N  
-ATOM   2281  CA  ILE A 272      -4.565 -38.577  39.100  1.00 17.07           C  
-ANISOU 2281  CA  ILE A 272     2555   2031   1900    275   -117    132       C  
-ATOM   2282  C   ILE A 272      -5.295 -38.494  37.754  1.00 20.17           C  
-ANISOU 2282  C   ILE A 272     2923   2433   2308    239   -101    142       C  
-ATOM   2283  O   ILE A 272      -5.351 -37.417  37.153  1.00 19.32           O  
-ANISOU 2283  O   ILE A 272     2803   2329   2208    235   -104    134       O  
-ATOM   2284  CB  ILE A 272      -3.029 -38.463  38.847  1.00 19.50           C  
-ANISOU 2284  CB  ILE A 272     2862   2317   2229    274   -143    101       C  
-ATOM   2285  CG1 ILE A 272      -2.500 -39.706  38.128  1.00 16.43           C  
-ANISOU 2285  CG1 ILE A 272     2468   1915   1861    247   -140    103       C  
-ATOM   2286  CG2 ILE A 272      -2.294 -38.231  40.142  1.00 23.80           C  
-ANISOU 2286  CG2 ILE A 272     3427   2860   2756    311   -164     85       C  
-ATOM   2287  CD1 ILE A 272      -1.009 -39.619  37.744  1.00 20.48           C  
-ANISOU 2287  CD1 ILE A 272     2977   2408   2398    244   -163     74       C  
-ATOM   2288  N   LEU A 273      -5.855 -39.609  37.284  1.00 16.40           N  
-ANISOU 2288  N   LEU A 273     2438   1960   1835    213    -83    160       N  
-ATOM   2289  CA  LEU A 273      -6.372 -39.661  35.915  1.00 16.26           C  
-ANISOU 2289  CA  LEU A 273     2394   1952   1831    176    -72    164       C  
-ATOM   2290  C   LEU A 273      -7.742 -39.003  35.733  1.00 24.10           C  
-ANISOU 2290  C   LEU A 273     3371   2976   2809    175    -55    185       C  
-ATOM   2291  O   LEU A 273      -7.988 -38.357  34.716  1.00 26.12           O  
-ANISOU 2291  O   LEU A 273     3607   3245   3072    160    -54    183       O  
-ATOM   2292  CB  LEU A 273      -6.406 -41.099  35.399  1.00 22.71           C  
-ANISOU 2292  CB  LEU A 273     3207   2762   2661    144    -60    169       C  
-ATOM   2293  CG  LEU A 273      -6.874 -41.316  33.961  1.00 23.94           C  
-ANISOU 2293  CG  LEU A 273     3336   2931   2830    103    -50    167       C  
-ATOM   2294  CD1 LEU A 273      -6.095 -40.435  32.990  1.00 23.68           C  
-ANISOU 2294  CD1 LEU A 273     3290   2895   2811     98    -65    147       C  
-ATOM   2295  CD2 LEU A 273      -6.763 -42.787  33.566  1.00 26.06           C  
-ANISOU 2295  CD2 LEU A 273     3605   3185   3113     73    -39    166       C  
-ATOM   2296  N   GLY A 274      -8.637 -39.192  36.695  1.00 19.27           N  
-ANISOU 2296  N   GLY A 274     2769   2378   2176    193    -42    207       N  
-ATOM   2297  CA  GLY A 274      -9.977 -38.625  36.611  1.00 19.77           C  
-ANISOU 2297  CA  GLY A 274     2816   2471   2223    195    -24    230       C  
-ATOM   2298  C   GLY A 274     -10.826 -39.215  35.499  1.00 18.33           C  
-ANISOU 2298  C   GLY A 274     2605   2311   2049    155     -9    242       C  
-ATOM   2299  O   GLY A 274     -10.466 -40.235  34.914  1.00 19.30           O  
-ANISOU 2299  O   GLY A 274     2723   2423   2188    124     -8    233       O  
-ATOM   2300  N   ARG A 275     -11.973 -38.583  35.234  1.00 16.23           N  
-ANISOU 2300  N   ARG A 275     2319   2079   1770    156      5    261       N  
-ATOM   2301  CA  ARG A 275     -12.822 -38.918  34.090  1.00 15.31           C  
-ANISOU 2301  CA  ARG A 275     2168   1991   1656    120     16    270       C  
-ATOM   2302  C   ARG A 275     -12.916 -37.718  33.164  1.00 15.98           C  
-ANISOU 2302  C   ARG A 275     2234   2096   1742    124     11    269       C  
-ATOM   2303  O   ARG A 275     -13.203 -36.606  33.607  1.00 21.43           O  
-ANISOU 2303  O   ARG A 275     2928   2793   2420    156     14    278       O  
-ATOM   2304  CB  ARG A 275     -14.229 -39.337  34.542  1.00 18.34           C  
-ANISOU 2304  CB  ARG A 275     2538   2404   2025    116     39    299       C  
-ATOM   2305  CG  ARG A 275     -14.277 -40.674  35.268  1.00 23.99           C  
-ANISOU 2305  CG  ARG A 275     3268   3102   2745    105     50    305       C  
-ATOM   2306  CD  ARG A 275     -15.717 -41.203  35.330  1.00 24.86           C  
-ANISOU 2306  CD  ARG A 275     3355   3244   2847     87     75    332       C  
-ATOM   2307  NE  ARG A 275     -16.572 -40.403  36.204  1.00 20.86           N  
-ANISOU 2307  NE  ARG A 275     2849   2759   2317    123     86    358       N  
-ATOM   2308  CZ  ARG A 275     -17.884 -40.590  36.326  1.00 24.59           C  
-ANISOU 2308  CZ  ARG A 275     3299   3265   2781    115    108    384       C  
-ATOM   2309  NH1 ARG A 275     -18.472 -41.552  35.632  1.00 24.74           N  
-ANISOU 2309  NH1 ARG A 275     3290   3298   2812     70    119    386       N  
-ATOM   2310  NH2 ARG A 275     -18.605 -39.829  37.144  1.00 17.81           N  
-ANISOU 2310  NH2 ARG A 275     2442   2424   1899    152    119    408       N  
-ATOM   2311  N   HIS A 276     -12.696 -37.953  31.873  1.00 11.87           N  
-ANISOU 2311  N   HIS A 276     1692   1585   1233     92      7    257       N  
-ATOM   2312  CA  HIS A 276     -12.668 -36.889  30.885  1.00 12.28           C  
-ANISOU 2312  CA  HIS A 276     1725   1654   1285     96      4    257       C  
-ATOM   2313  C   HIS A 276     -13.342 -37.310  29.598  1.00 15.62           C  
-ANISOU 2313  C   HIS A 276     2113   2116   1706     61      9    262       C  
-ATOM   2314  O   HIS A 276     -13.107 -38.402  29.073  1.00 11.30           O  
-ANISOU 2314  O   HIS A 276     1560   1564   1168     26      7    247       O  
-ATOM   2315  CB  HIS A 276     -11.224 -36.498  30.577  1.00 16.69           C  
-ANISOU 2315  CB  HIS A 276     2300   2178   1864    101    -13    232       C  
-ATOM   2316  CG  HIS A 276     -10.451 -36.093  31.785  1.00 18.23           C  
-ANISOU 2316  CG  HIS A 276     2527   2337   2062    133    -23    221       C  
-ATOM   2317  ND1 HIS A 276     -10.579 -34.848  32.361  1.00 15.88           N  
-ANISOU 2317  ND1 HIS A 276     2240   2037   1758    168    -21    227       N  
-ATOM   2318  CD2 HIS A 276      -9.541 -36.764  32.529  1.00 19.78           C  
-ANISOU 2318  CD2 HIS A 276     2749   2501   2267    136    -35    204       C  
-ATOM   2319  CE1 HIS A 276      -9.777 -34.768  33.407  1.00 18.06           C  
-ANISOU 2319  CE1 HIS A 276     2543   2281   2036    189    -33    211       C  
-ATOM   2320  NE2 HIS A 276      -9.137 -35.918  33.530  1.00 23.89           N  
-ANISOU 2320  NE2 HIS A 276     3291   3003   2783    171    -42    198       N  
-ATOM   2321  N   SER A 277     -14.192 -36.431  29.092  1.00 11.47           N  
-ANISOU 2321  N   SER A 277     1563   1629   1165     72     18    282       N  
-ATOM   2322  CA  SER A 277     -14.809 -36.653  27.795  1.00 12.21           C  
-ANISOU 2322  CA  SER A 277     1620   1768   1253     43     21    286       C  
-ATOM   2323  C   SER A 277     -13.795 -36.429  26.685  1.00 16.92           C  
-ANISOU 2323  C   SER A 277     2213   2353   1861     33      9    266       C  
-ATOM   2324  O   SER A 277     -12.798 -35.710  26.871  1.00 17.78           O  
-ANISOU 2324  O   SER A 277     2344   2428   1983     55      2    258       O  
-ATOM   2325  CB  SER A 277     -15.974 -35.677  27.622  1.00 16.67           C  
-ANISOU 2325  CB  SER A 277     2159   2380   1797     65     33    317       C  
-ATOM   2326  OG  SER A 277     -15.486 -34.357  27.784  1.00 21.24           O  
-ANISOU 2326  OG  SER A 277     2753   2940   2379    104     33    323       O  
-ATOM   2327  N   ARG A 278     -14.032 -37.035  25.523  1.00 12.32           N  
-ANISOU 2327  N   ARG A 278     1604   1802   1274     -1      8    258       N  
-ATOM   2328  CA  ARG A 278     -13.207 -36.729  24.361  1.00 12.55           C  
-ANISOU 2328  CA  ARG A 278     1627   1832   1310     -7      0    244       C  
-ATOM   2329  C   ARG A 278     -13.596 -35.337  23.892  1.00 16.68           C  
-ANISOU 2329  C   ARG A 278     2134   2384   1821     24      7    270       C  
-ATOM   2330  O   ARG A 278     -14.783 -35.001  23.876  1.00 15.61           O  
-ANISOU 2330  O   ARG A 278     1973   2292   1664     33     17    295       O  
-ATOM   2331  CB  ARG A 278     -13.429 -37.754  23.248  1.00 15.01           C  
-ANISOU 2331  CB  ARG A 278     1913   2173   1616    -50     -3    228       C  
-ATOM   2332  CG  ARG A 278     -12.469 -37.612  22.065  1.00 15.25           C  
-ANISOU 2332  CG  ARG A 278     1940   2201   1653    -58    -10    210       C  
-ATOM   2333  CD  ARG A 278     -12.190 -38.990  21.457  1.00 15.79           C  
-ANISOU 2333  CD  ARG A 278     2005   2266   1727   -102    -15    179       C  
-ATOM   2334  NE  ARG A 278     -10.979 -39.019  20.633  1.00 22.77           N  
-ANISOU 2334  NE  ARG A 278     2897   3129   2624   -107    -22    158       N  
-ATOM   2335  CZ  ARG A 278     -10.279 -40.124  20.394  1.00 19.51           C  
-ANISOU 2335  CZ  ARG A 278     2496   2690   2226   -135    -25    129       C  
-ATOM   2336  NH1 ARG A 278     -10.669 -41.274  20.929  1.00 17.53           N  
-ANISOU 2336  NH1 ARG A 278     2252   2427   1981   -162    -22    117       N  
-ATOM   2337  NH2 ARG A 278      -9.193 -40.087  19.630  1.00 16.75           N  
-ANISOU 2337  NH2 ARG A 278     2153   2324   1887   -137    -30    112       N  
-ATOM   2338  N   LYS A 279     -12.614 -34.520  23.527  1.00 15.90           N  
-ANISOU 2338  N   LYS A 279     2046   2260   1736     42      4    265       N  
-ATOM   2339  CA  LYS A 279     -12.898 -33.142  23.113  1.00 19.66           C  
-ANISOU 2339  CA  LYS A 279     2509   2755   2204     75     15    292       C  
-ATOM   2340  C   LYS A 279     -12.930 -33.009  21.592  1.00 25.53           C  
-ANISOU 2340  C   LYS A 279     3224   3540   2937     65     17    296       C  
-ATOM   2341  O   LYS A 279     -12.280 -33.774  20.887  1.00 25.94           O  
-ANISOU 2341  O   LYS A 279     3273   3587   2994     36      7    273       O  
-ATOM   2342  CB  LYS A 279     -11.838 -32.188  23.666  1.00 12.05           C  
-ANISOU 2342  CB  LYS A 279     1576   1738   1266    104     15    286       C  
-ATOM   2343  CG  LYS A 279     -11.649 -32.222  25.171  1.00 11.59           C  
-ANISOU 2343  CG  LYS A 279     1549   1638   1216    119     11    277       C  
-ATOM   2344  CD  LYS A 279     -12.963 -32.139  25.954  1.00 16.74           C  
-ANISOU 2344  CD  LYS A 279     2195   2318   1846    133     22    301       C  
-ATOM   2345  CE  LYS A 279     -12.727 -32.098  27.472  1.00 17.42           C  
-ANISOU 2345  CE  LYS A 279     2315   2365   1939    153     19    293       C  
-ATOM   2346  NZ  LYS A 279     -12.103 -33.344  28.060  1.00 11.69           N  
-ANISOU 2346  NZ  LYS A 279     1609   1612   1222    130      5    268       N  
-ATOM   2347  N   ARG A 280     -13.671 -32.030  21.082  1.00 18.34           N  
-ANISOU 2347  N   ARG A 280     2290   2670   2009     90     29    328       N  
-ATOM   2348  CA  ARG A 280     -13.604 -31.723  19.654  1.00 17.01           C  
-ANISOU 2348  CA  ARG A 280     2095   2540   1828     89     33    337       C  
-ATOM   2349  C   ARG A 280     -12.442 -30.759  19.408  1.00 19.11           C  
-ANISOU 2349  C   ARG A 280     2380   2762   2118    112     39    338       C  
-ATOM   2350  O   ARG A 280     -12.166 -29.882  20.228  1.00 17.85           O  
-ANISOU 2350  O   ARG A 280     2243   2562   1977    141     47    346       O  
-ATOM   2351  CB  ARG A 280     -14.918 -31.132  19.154  1.00 19.93           C  
-ANISOU 2351  CB  ARG A 280     2429   2977   2166    108     45    374       C  
-ATOM   2352  CG  ARG A 280     -16.122 -32.016  19.469  1.00 19.67           C  
-ANISOU 2352  CG  ARG A 280     2374   2988   2111     85     40    374       C  
-ATOM   2353  CD  ARG A 280     -17.388 -31.493  18.852  1.00 21.61           C  
-ANISOU 2353  CD  ARG A 280     2578   3308   2324    101     50    409       C  
-ATOM   2354  NE  ARG A 280     -18.544 -32.185  19.405  1.00 22.34           N  
-ANISOU 2354  NE  ARG A 280     2651   3434   2401     84     48    412       N  
-ATOM   2355  CZ  ARG A 280     -19.076 -33.297  18.904  1.00 21.65           C  
-ANISOU 2355  CZ  ARG A 280     2537   3390   2300     41     37    394       C  
-ATOM   2356  NH1 ARG A 280     -20.130 -33.844  19.500  1.00 24.34           N  
-ANISOU 2356  NH1 ARG A 280     2861   3757   2632     26     39    399       N  
-ATOM   2357  NH2 ARG A 280     -18.557 -33.859  17.817  1.00 20.23           N  
-ANISOU 2357  NH2 ARG A 280     2346   3225   2114     13     26    369       N  
-ATOM   2358  N   TRP A 281     -11.771 -30.915  18.275  1.00 14.12           N  
-ANISOU 2358  N   TRP A 281     1739   2139   1488    100     36    328       N  
-ATOM   2359  CA  TRP A 281     -10.521 -30.183  18.049  1.00 16.44           C  
-ANISOU 2359  CA  TRP A 281     2050   2385   1810    115     42    324       C  
-ATOM   2360  C   TRP A 281     -10.728 -28.682  17.919  1.00 18.79           C  
-ANISOU 2360  C   TRP A 281     2345   2683   2111    158     64    361       C  
-ATOM   2361  O   TRP A 281      -9.796 -27.897  18.115  1.00 17.10           O  
-ANISOU 2361  O   TRP A 281     2150   2418   1928    175     72    359       O  
-ATOM   2362  CB  TRP A 281      -9.802 -30.721  16.814  1.00 17.65           C  
-ANISOU 2362  CB  TRP A 281     2193   2552   1962     93     37    308       C  
-ATOM   2363  CG  TRP A 281      -9.271 -32.078  17.027  1.00 17.73           C  
-ANISOU 2363  CG  TRP A 281     2215   2542   1980     55     19    269       C  
-ATOM   2364  CD1 TRP A 281      -9.752 -33.240  16.498  1.00 16.72           C  
-ANISOU 2364  CD1 TRP A 281     2070   2453   1830     22      9    252       C  
-ATOM   2365  CD2 TRP A 281      -8.169 -32.438  17.865  1.00 15.93           C  
-ANISOU 2365  CD2 TRP A 281     2018   2249   1784     47      9    242       C  
-ATOM   2366  NE1 TRP A 281      -9.002 -34.304  16.945  1.00 21.00           N  
-ANISOU 2366  NE1 TRP A 281     2634   2954   2392     -6     -3    217       N  
-ATOM   2367  CE2 TRP A 281      -8.022 -33.835  17.784  1.00 17.81           C  
-ANISOU 2367  CE2 TRP A 281     2259   2488   2020     11     -4    212       C  
-ATOM   2368  CE3 TRP A 281      -7.283 -31.710  18.673  1.00 20.27           C  
-ANISOU 2368  CE3 TRP A 281     2595   2742   2367     68     10    238       C  
-ATOM   2369  CZ2 TRP A 281      -7.029 -34.520  18.475  1.00 14.31           C  
-ANISOU 2369  CZ2 TRP A 281     1842   1992   1603     -2    -15    184       C  
-ATOM   2370  CZ3 TRP A 281      -6.299 -32.394  19.362  1.00 20.78           C  
-ANISOU 2370  CZ3 TRP A 281     2683   2757   2456     53     -4    207       C  
-ATOM   2371  CH2 TRP A 281      -6.183 -33.788  19.261  1.00 20.51           C  
-ANISOU 2371  CH2 TRP A 281     2650   2726   2416     21    -16    183       C  
-ATOM   2372  N   GLU A 282     -11.950 -28.294  17.577  1.00 17.72           N  
-ANISOU 2372  N   GLU A 282     2182   2605   1945    175     75    394       N  
-ATOM   2373  CA  GLU A 282     -12.283 -26.891  17.372  1.00 22.08           C  
-ANISOU 2373  CA  GLU A 282     2729   3163   2497    219    100    434       C  
-ATOM   2374  C   GLU A 282     -12.059 -26.035  18.619  1.00 18.02           C  
-ANISOU 2374  C   GLU A 282     2246   2590   2012    245    110    435       C  
-ATOM   2375  O   GLU A 282     -11.806 -24.835  18.523  1.00 21.37           O  
-ANISOU 2375  O   GLU A 282     2678   2989   2454    277    131    457       O  
-ATOM   2376  CB  GLU A 282     -13.731 -26.749  16.868  1.00 23.89           C  
-ANISOU 2376  CB  GLU A 282     2921   3470   2685    234    108    469       C  
-ATOM   2377  CG  GLU A 282     -13.923 -27.113  15.393  1.00 24.12           C  
-ANISOU 2377  CG  GLU A 282     2915   3564   2684    223    105    477       C  
-ATOM   2378  CD  GLU A 282     -14.131 -28.611  15.143  1.00 32.25           C  
-ANISOU 2378  CD  GLU A 282     3931   4627   3695    174     80    442       C  
-ATOM   2379  OE1 GLU A 282     -14.075 -29.414  16.104  1.00 26.65           O  
-ANISOU 2379  OE1 GLU A 282     3240   3886   2998    148     66    414       O  
-ATOM   2380  OE2 GLU A 282     -14.355 -28.988  13.967  1.00 35.47           O  
-ANISOU 2380  OE2 GLU A 282     4309   5092   4074    162     75    443       O  
-ATOM   2381  N   ARG A 283     -12.135 -26.635  19.794  1.00 18.51           N  
-ANISOU 2381  N   ARG A 283     2328   2627   2080    231     95    412       N  
-ATOM   2382  CA  ARG A 283     -11.917 -25.849  21.007  1.00 23.86           C  
-ANISOU 2382  CA  ARG A 283     3035   3250   2780    256    103    409       C  
-ATOM   2383  C   ARG A 283     -10.508 -25.245  21.094  1.00 19.13           C  
-ANISOU 2383  C   ARG A 283     2461   2585   2221    260    105    389       C  
-ATOM   2384  O   ARG A 283     -10.306 -24.280  21.810  1.00 17.24           O  
-ANISOU 2384  O   ARG A 283     2242   2305   2003    285    117    390       O  
-ATOM   2385  CB  ARG A 283     -12.217 -26.658  22.273  1.00 24.15           C  
-ANISOU 2385  CB  ARG A 283     3089   3274   2811    242     87    387       C  
-ATOM   2386  CG  ARG A 283     -11.326 -27.869  22.474  1.00 23.06           C  
-ANISOU 2386  CG  ARG A 283     2964   3112   2685    204     62    348       C  
-ATOM   2387  CD  ARG A 283     -10.992 -28.066  23.958  1.00 33.52           C  
-ANISOU 2387  CD  ARG A 283     4322   4390   4023    207     52    325       C  
-ATOM   2388  NE  ARG A 283     -12.183 -28.252  24.784  1.00 44.40           N  
-ANISOU 2388  NE  ARG A 283     5698   5794   5378    217     56    340       N  
-ATOM   2389  CZ  ARG A 283     -12.171 -28.318  26.114  1.00 40.28           C  
-ANISOU 2389  CZ  ARG A 283     5202   5243   4859    228     51    328       C  
-ATOM   2390  NH1 ARG A 283     -11.033 -28.203  26.788  1.00 40.36           N  
-ANISOU 2390  NH1 ARG A 283     5241   5200   4893    229     40    299       N  
-ATOM   2391  NH2 ARG A 283     -13.303 -28.493  26.770  1.00 38.76           N  
-ANISOU 2391  NH2 ARG A 283     5006   5079   4644    237     58    346       N  
-ATOM   2392  N   PHE A 284      -9.545 -25.808  20.370  1.00 18.17           N  
-ANISOU 2392  N   PHE A 284     2337   2454   2111    234     94    368       N  
-ATOM   2393  CA  PHE A 284      -8.174 -25.305  20.427  1.00 14.05           C  
-ANISOU 2393  CA  PHE A 284     1835   1874   1631    234     95    348       C  
-ATOM   2394  C   PHE A 284      -7.924 -24.208  19.401  1.00 16.47           C  
-ANISOU 2394  C   PHE A 284     2129   2179   1949    257    121    377       C  
-ATOM   2395  O   PHE A 284      -6.839 -23.639  19.340  1.00 20.06           O  
-ANISOU 2395  O   PHE A 284     2596   2585   2440    259    128    365       O  
-ATOM   2396  CB  PHE A 284      -7.194 -26.453  20.236  1.00 12.75           C  
-ANISOU 2396  CB  PHE A 284     1675   1695   1475    198     71    312       C  
-ATOM   2397  CG  PHE A 284      -7.348 -27.514  21.273  1.00 15.57           C  
-ANISOU 2397  CG  PHE A 284     2046   2045   1823    179     49    287       C  
-ATOM   2398  CD1 PHE A 284      -6.951 -27.273  22.581  1.00 19.39           C  
-ANISOU 2398  CD1 PHE A 284     2558   2484   2326    188     41    267       C  
-ATOM   2399  CD2 PHE A 284      -7.938 -28.723  20.966  1.00 14.48           C  
-ANISOU 2399  CD2 PHE A 284     1894   1949   1658    153     37    283       C  
-ATOM   2400  CE1 PHE A 284      -7.109 -28.233  23.553  1.00 17.92           C  
-ANISOU 2400  CE1 PHE A 284     2385   2294   2130    175     23    248       C  
-ATOM   2401  CE2 PHE A 284      -8.094 -29.693  21.936  1.00 20.28           C  
-ANISOU 2401  CE2 PHE A 284     2642   2675   2388    137     21    263       C  
-ATOM   2402  CZ  PHE A 284      -7.686 -29.449  23.232  1.00 19.51           C  
-ANISOU 2402  CZ  PHE A 284     2573   2533   2307    150     14    248       C  
-ATOM   2403  N   VAL A 285      -8.939 -23.919  18.598  1.00 17.01           N  
-ANISOU 2403  N   VAL A 285     2172   2304   1988    274    137    415       N  
-ATOM   2404  CA  VAL A 285      -8.831 -22.883  17.575  1.00 15.13           C  
-ANISOU 2404  CA  VAL A 285     1920   2073   1756    300    166    450       C  
-ATOM   2405  C   VAL A 285      -9.205 -21.525  18.144  1.00 19.44           C  
-ANISOU 2405  C   VAL A 285     2478   2590   2318    340    194    476       C  
-ATOM   2406  O   VAL A 285     -10.203 -21.396  18.843  1.00 25.56           O  
-ANISOU 2406  O   VAL A 285     3254   3382   3075    356    196    488       O  
-ATOM   2407  CB  VAL A 285      -9.760 -23.184  16.392  1.00 17.36           C  
-ANISOU 2407  CB  VAL A 285     2167   2436   1994    304    171    482       C  
-ATOM   2408  CG1 VAL A 285      -9.635 -22.095  15.331  1.00 15.97           C  
-ANISOU 2408  CG1 VAL A 285     1977   2269   1822    337    203    523       C  
-ATOM   2409  CG2 VAL A 285      -9.456 -24.549  15.821  1.00 15.22           C  
-ANISOU 2409  CG2 VAL A 285     1885   2194   1706    264    144    453       C  
-ATOM   2410  N   HIS A 286      -8.400 -20.510  17.848  1.00 15.71           N  
-ANISOU 2410  N   HIS A 286     2015   2072   1883    356    218    484       N  
-ATOM   2411  CA  HIS A 286      -8.680 -19.159  18.321  1.00 16.81           C  
-ANISOU 2411  CA  HIS A 286     2168   2177   2044    394    249    507       C  
-ATOM   2412  C   HIS A 286      -8.181 -18.144  17.297  1.00 18.14           C  
-ANISOU 2412  C   HIS A 286     2328   2328   2235    416    284    539       C  
-ATOM   2413  O   HIS A 286      -7.607 -18.528  16.274  1.00 21.26           O  
-ANISOU 2413  O   HIS A 286     2708   2741   2628    402    282    542       O  
-ATOM   2414  CB  HIS A 286      -8.066 -18.927  19.704  1.00 19.10           C  
-ANISOU 2414  CB  HIS A 286     2492   2398   2369    387    239    467       C  
-ATOM   2415  CG  HIS A 286      -6.617 -19.291  19.790  1.00 19.90           C  
-ANISOU 2415  CG  HIS A 286     2605   2450   2505    356    221    424       C  
-ATOM   2416  ND1 HIS A 286      -5.653 -18.681  19.021  1.00 15.99           N  
-ANISOU 2416  ND1 HIS A 286     2107   1923   2045    356    240    429       N  
-ATOM   2417  CD2 HIS A 286      -5.969 -20.191  20.568  1.00 15.79           C  
-ANISOU 2417  CD2 HIS A 286     2099   1909   1991    325    187    378       C  
-ATOM   2418  CE1 HIS A 286      -4.471 -19.201  19.306  1.00 15.81           C  
-ANISOU 2418  CE1 HIS A 286     2094   1863   2049    326    217    387       C  
-ATOM   2419  NE2 HIS A 286      -4.636 -20.116  20.244  1.00 19.04           N  
-ANISOU 2419  NE2 HIS A 286     2515   2280   2441    308    185    355       N  
-ATOM   2420  N   SER A 287      -8.404 -16.857  17.552  1.00 16.89           N  
-ANISOU 2420  N   SER A 287     2180   2136   2100    452    319    565       N  
-ATOM   2421  CA  SER A 287      -8.170 -15.850  16.518  1.00 20.35           C  
-ANISOU 2421  CA  SER A 287     2608   2567   2556    480    359    607       C  
-ATOM   2422  C   SER A 287      -6.711 -15.770  16.066  1.00 21.62           C  
-ANISOU 2422  C   SER A 287     2776   2678   2761    458    362    585       C  
-ATOM   2423  O   SER A 287      -6.420 -15.305  14.962  1.00 21.89           O  
-ANISOU 2423  O   SER A 287     2796   2721   2803    473    389    619       O  
-ATOM   2424  CB  SER A 287      -8.684 -14.483  16.969  1.00 32.23           C  
-ANISOU 2424  CB  SER A 287     4126   4037   4081    524    400    637       C  
-ATOM   2425  OG  SER A 287      -8.160 -14.143  18.238  1.00 46.24           O  
-ANISOU 2425  OG  SER A 287     5934   5740   5895    514    394    594       O  
-ATOM   2426  N   GLU A 288      -5.804 -16.247  16.911  1.00 17.86           N  
-ANISOU 2426  N   GLU A 288     2319   2155   2313    424    334    531       N  
-ATOM   2427  CA  GLU A 288      -4.370 -16.171  16.624  1.00 20.78           C  
-ANISOU 2427  CA  GLU A 288     2694   2473   2728    402    335    506       C  
-ATOM   2428  C   GLU A 288      -3.795 -17.389  15.907  1.00 22.45           C  
-ANISOU 2428  C   GLU A 288     2890   2720   2921    369    307    488       C  
-ATOM   2429  O   GLU A 288      -2.641 -17.354  15.475  1.00 25.72           O  
-ANISOU 2429  O   GLU A 288     3304   3101   3370    353    310    474       O  
-ATOM   2430  CB  GLU A 288      -3.574 -15.896  17.896  1.00 19.55           C  
-ANISOU 2430  CB  GLU A 288     2567   2245   2618    385    323    456       C  
-ATOM   2431  CG  GLU A 288      -3.702 -14.474  18.401  1.00 25.22           C  
-ANISOU 2431  CG  GLU A 288     3302   2909   3372    414    360    468       C  
-ATOM   2432  CD  GLU A 288      -5.077 -14.186  18.980  1.00 28.04           C  
-ANISOU 2432  CD  GLU A 288     3665   3294   3696    445    368    491       C  
-ATOM   2433  OE1 GLU A 288      -5.539 -14.977  19.839  1.00 28.20           O  
-ANISOU 2433  OE1 GLU A 288     3692   3335   3687    433    334    465       O  
-ATOM   2434  OE2 GLU A 288      -5.690 -13.170  18.577  1.00 32.21           O  
-ANISOU 2434  OE2 GLU A 288     4190   3821   4228    483    409    537       O  
-ATOM   2435  N   ASN A 289      -4.574 -18.463  15.789  1.00 17.01           N  
-ANISOU 2435  N   ASN A 289     2188   2093   2180    358    280    487       N  
-ATOM   2436  CA  ASN A 289      -4.109 -19.631  15.040  1.00 14.65           C  
-ANISOU 2436  CA  ASN A 289     1875   1829   1862    328    256    470       C  
-ATOM   2437  C   ASN A 289      -5.053 -20.086  13.921  1.00 17.87           C  
-ANISOU 2437  C   ASN A 289     2254   2320   2216    338    259    505       C  
-ATOM   2438  O   ASN A 289      -4.719 -20.995  13.165  1.00 20.11           O  
-ANISOU 2438  O   ASN A 289     2524   2636   2480    315    243    493       O  
-ATOM   2439  CB  ASN A 289      -3.796 -20.808  15.983  1.00 13.48           C  
-ANISOU 2439  CB  ASN A 289     1740   1670   1711    292    214    419       C  
-ATOM   2440  CG  ASN A 289      -5.048 -21.359  16.686  1.00 13.63           C  
-ANISOU 2440  CG  ASN A 289     1760   1730   1690    294    196    419       C  
-ATOM   2441  OD1 ASN A 289      -6.176 -21.196  16.210  1.00 14.95           O  
-ANISOU 2441  OD1 ASN A 289     1909   1951   1821    314    208    455       O  
-ATOM   2442  ND2 ASN A 289      -4.841 -22.036  17.816  1.00 14.30           N  
-ANISOU 2442  ND2 ASN A 289     1863   1790   1779    273    168    379       N  
-ATOM   2443  N   GLN A 290      -6.217 -19.447  13.798  1.00 16.88           N  
-ANISOU 2443  N   GLN A 290     2118   2232   2065    371    279    547       N  
-ATOM   2444  CA  GLN A 290      -7.253 -19.927  12.870  1.00 17.56           C  
-ANISOU 2444  CA  GLN A 290     2174   2405   2094    380    276    577       C  
-ATOM   2445  C   GLN A 290      -6.783 -19.966  11.405  1.00 19.52           C  
-ANISOU 2445  C   GLN A 290     2400   2685   2330    383    290    598       C  
-ATOM   2446  O   GLN A 290      -7.243 -20.786  10.606  1.00 20.97           O  
-ANISOU 2446  O   GLN A 290     2561   2939   2468    373    274    600       O  
-ATOM   2447  CB  GLN A 290      -8.534 -19.091  13.006  1.00 18.94           C  
-ANISOU 2447  CB  GLN A 290     2339   2612   2247    421    299    622       C  
-ATOM   2448  CG  GLN A 290      -8.395 -17.681  12.463  1.00 28.56           C  
-ANISOU 2448  CG  GLN A 290     3557   3806   3488    464    346    670       C  
-ATOM   2449  CD  GLN A 290      -9.456 -16.725  12.985  1.00 44.27           C  
-ANISOU 2449  CD  GLN A 290     5548   5799   5472    506    371    706       C  
-ATOM   2450  OE1 GLN A 290     -10.498 -17.144  13.491  1.00 48.16           O  
-ANISOU 2450  OE1 GLN A 290     6033   6333   5931    507    355    706       O  
-ATOM   2451  NE2 GLN A 290      -9.186 -15.424  12.871  1.00 46.74           N  
-ANISOU 2451  NE2 GLN A 290     5872   6066   5822    541    414    739       N  
-ATOM   2452  N   HIS A 291      -5.878 -19.069  11.049  1.00 22.27           N  
-ANISOU 2452  N   HIS A 291     2757   2986   2720    398    319    613       N  
-ATOM   2453  CA  HIS A 291      -5.339 -19.049   9.692  1.00 21.04           C  
-ANISOU 2453  CA  HIS A 291     2583   2855   2555    405    336    634       C  
-ATOM   2454  C   HIS A 291      -4.492 -20.299   9.375  1.00 22.80           C  
-ANISOU 2454  C   HIS A 291     2805   3084   2774    362    305    589       C  
-ATOM   2455  O   HIS A 291      -4.117 -20.524   8.221  1.00 21.85           O  
-ANISOU 2455  O   HIS A 291     2669   2996   2637    363    312    601       O  
-ATOM   2456  CB  HIS A 291      -4.511 -17.780   9.473  1.00 22.46           C  
-ANISOU 2456  CB  HIS A 291     2773   2972   2787    429    378    660       C  
-ATOM   2457  CG  HIS A 291      -3.267 -17.723  10.303  1.00 18.36           C  
-ANISOU 2457  CG  HIS A 291     2279   2367   2328    401    371    616       C  
-ATOM   2458  ND1 HIS A 291      -3.288 -17.477  11.659  1.00 20.87           N  
-ANISOU 2458  ND1 HIS A 291     2621   2633   2676    393    360    587       N  
-ATOM   2459  CD2 HIS A 291      -1.967 -17.912   9.976  1.00 23.04           C  
-ANISOU 2459  CD2 HIS A 291     2875   2922   2956    379    371    594       C  
-ATOM   2460  CE1 HIS A 291      -2.054 -17.500  12.128  1.00 25.00           C  
-ANISOU 2460  CE1 HIS A 291     3159   3090   3248    368    353    549       C  
-ATOM   2461  NE2 HIS A 291      -1.232 -17.765  11.126  1.00 24.33           N  
-ANISOU 2461  NE2 HIS A 291     3061   3013   3169    358    359    552       N  
-ATOM   2462  N   LEU A 292      -4.186 -21.097  10.396  1.00 18.11           N  
-ANISOU 2462  N   LEU A 292     2230   2458   2195    327    271    539       N  
-ATOM   2463  CA  LEU A 292      -3.398 -22.322  10.213  1.00 20.91           C  
-ANISOU 2463  CA  LEU A 292     2586   2812   2548    287    243    496       C  
-ATOM   2464  C   LEU A 292      -4.297 -23.557  10.264  1.00 22.19           C  
-ANISOU 2464  C   LEU A 292     2737   3034   2660    265    210    476       C  
-ATOM   2465  O   LEU A 292      -3.842 -24.690  10.064  1.00 18.70           O  
-ANISOU 2465  O   LEU A 292     2295   2600   2209    232    187    441       O  
-ATOM   2466  CB  LEU A 292      -2.331 -22.431  11.299  1.00 18.13           C  
-ANISOU 2466  CB  LEU A 292     2260   2382   2247    264    228    453       C  
-ATOM   2467  CG  LEU A 292      -1.379 -21.236  11.400  1.00 20.31           C  
-ANISOU 2467  CG  LEU A 292     2547   2592   2580    279    258    463       C  
-ATOM   2468  CD1 LEU A 292      -0.432 -21.394  12.571  1.00 16.41           C  
-ANISOU 2468  CD1 LEU A 292     2076   2029   2132    255    238    417       C  
-ATOM   2469  CD2 LEU A 292      -0.606 -21.064  10.098  1.00 21.98           C  
-ANISOU 2469  CD2 LEU A 292     2743   2811   2799    285    281    483       C  
-ATOM   2470  N   VAL A 293      -5.577 -23.332  10.528  1.00 17.53           N  
-ANISOU 2470  N   VAL A 293     2137   2484   2039    282    211    499       N  
-ATOM   2471  CA  VAL A 293      -6.515 -24.428  10.739  1.00 15.85           C  
-ANISOU 2471  CA  VAL A 293     1914   2324   1784    259    183    480       C  
-ATOM   2472  C   VAL A 293      -7.551 -24.489   9.629  1.00 17.89           C  
-ANISOU 2472  C   VAL A 293     2138   2671   1988    274    188    512       C  
-ATOM   2473  O   VAL A 293      -8.038 -23.473   9.146  1.00 25.60           O  
-ANISOU 2473  O   VAL A 293     3101   3672   2953    314    215    559       O  
-ATOM   2474  CB  VAL A 293      -7.238 -24.317  12.112  1.00 18.48           C  
-ANISOU 2474  CB  VAL A 293     2261   2636   2124    261    173    474       C  
-ATOM   2475  CG1 VAL A 293      -8.172 -25.501  12.336  1.00 25.32           C  
-ANISOU 2475  CG1 VAL A 293     3117   3554   2952    235    146    454       C  
-ATOM   2476  CG2 VAL A 293      -6.238 -24.232  13.244  1.00 19.51           C  
-ANISOU 2476  CG2 VAL A 293     2425   2684   2304    249    166    441       C  
-ATOM   2477  N   SER A 294      -7.879 -25.702   9.231  1.00 20.35           N  
-ANISOU 2477  N   SER A 294     2436   3032   2265    243    163    486       N  
-ATOM   2478  CA  SER A 294      -8.859 -25.933   8.198  1.00 21.02           C  
-ANISOU 2478  CA  SER A 294     2485   3208   2293    251    162    507       C  
-ATOM   2479  C   SER A 294      -9.530 -27.226   8.589  1.00 20.12           C  
-ANISOU 2479  C   SER A 294     2365   3125   2155    211    130    469       C  
-ATOM   2480  O   SER A 294      -8.993 -27.968   9.403  1.00 17.73           O  
-ANISOU 2480  O   SER A 294     2085   2772   1880    179    113    429       O  
-ATOM   2481  CB  SER A 294      -8.160 -26.082   6.841  1.00 21.16           C  
-ANISOU 2481  CB  SER A 294     2491   3253   2297    251    170    509       C  
-ATOM   2482  OG  SER A 294      -7.153 -27.082   6.890  1.00 18.82           O  
-ANISOU 2482  OG  SER A 294     2212   2920   2020    212    152    460       O  
-ATOM   2483  N   PRO A 295     -10.704 -27.511   8.017  1.00 21.46           N  
-ANISOU 2483  N   PRO A 295     2501   3379   2275    212    123    482       N  
-ATOM   2484  CA  PRO A 295     -11.323 -28.808   8.297  1.00 18.83           C  
-ANISOU 2484  CA  PRO A 295     2159   3076   1921    169     94    443       C  
-ATOM   2485  C   PRO A 295     -10.376 -29.955   7.936  1.00 20.45           C  
-ANISOU 2485  C   PRO A 295     2376   3259   2134    128     78    394       C  
-ATOM   2486  O   PRO A 295     -10.314 -30.946   8.660  1.00 14.43           O  
-ANISOU 2486  O   PRO A 295     1628   2469   1386     91     59    355       O  
-ATOM   2487  CB  PRO A 295     -12.551 -28.812   7.380  1.00 22.58           C  
-ANISOU 2487  CB  PRO A 295     2590   3652   2339    180     92    467       C  
-ATOM   2488  CG  PRO A 295     -12.860 -27.352   7.173  1.00 26.98           C  
-ANISOU 2488  CG  PRO A 295     3137   4221   2891    236    121    526       C  
-ATOM   2489  CD  PRO A 295     -11.528 -26.673   7.123  1.00 23.95           C  
-ANISOU 2489  CD  PRO A 295     2783   3765   2551    253    141    533       C  
-ATOM   2490  N   GLU A 296      -9.656 -29.816   6.826  1.00 18.47           N  
-ANISOU 2490  N   GLU A 296     2120   3023   1876    136     87    397       N  
-ATOM   2491  CA  GLU A 296      -8.674 -30.821   6.409  1.00 15.13           C  
-ANISOU 2491  CA  GLU A 296     1709   2577   1461    102     76    353       C  
-ATOM   2492  C   GLU A 296      -7.577 -31.050   7.450  1.00 13.28           C  
-ANISOU 2492  C   GLU A 296     1514   2250   1283     86     72    326       C  
-ATOM   2493  O   GLU A 296      -7.228 -32.197   7.727  1.00 16.78           O  
-ANISOU 2493  O   GLU A 296     1970   2672   1736     49     55    283       O  
-ATOM   2494  CB  GLU A 296      -8.040 -30.457   5.067  1.00 19.47           C  
-ANISOU 2494  CB  GLU A 296     2248   3155   1995    121     91    368       C  
-ATOM   2495  CG  GLU A 296      -8.990 -30.591   3.886  1.00 19.29           C  
-ANISOU 2495  CG  GLU A 296     2186   3235   1909    128     88    381       C  
-ATOM   2496  CD  GLU A 296      -9.898 -29.395   3.724  1.00 31.25           C  
-ANISOU 2496  CD  GLU A 296     3677   4794   3401    175    106    439       C  
-ATOM   2497  OE1 GLU A 296      -9.616 -28.335   4.327  1.00 25.80           O  
-ANISOU 2497  OE1 GLU A 296     3005   4052   2747    206    127    472       O  
-ATOM   2498  OE2 GLU A 296     -10.900 -29.522   2.985  1.00 30.89           O  
-ANISOU 2498  OE2 GLU A 296     3596   4837   3302    180     99    450       O  
-ATOM   2499  N   ALA A 297      -7.042 -29.972   8.027  1.00 16.22           N  
-ANISOU 2499  N   ALA A 297     1903   2566   1692    115     89    351       N  
-ATOM   2500  CA  ALA A 297      -6.010 -30.101   9.067  1.00 15.01           C  
-ANISOU 2500  CA  ALA A 297     1784   2328   1591    103     84    326       C  
-ATOM   2501  C   ALA A 297      -6.546 -30.827  10.295  1.00 16.97           C  
-ANISOU 2501  C   ALA A 297     2045   2558   1845     80     64    302       C  
-ATOM   2502  O   ALA A 297      -5.874 -31.700  10.841  1.00 14.90           O  
-ANISOU 2502  O   ALA A 297     1803   2253   1605     52     50    265       O  
-ATOM   2503  CB  ALA A 297      -5.459 -28.741   9.470  1.00 10.57           C  
-ANISOU 2503  CB  ALA A 297     1235   1715   1066    138    106    356       C  
-ATOM   2504  N   LEU A 298      -7.753 -30.467  10.734  1.00 17.46           N  
-ANISOU 2504  N   LEU A 298     2095   2652   1887     92     65    325       N  
-ATOM   2505  CA  LEU A 298      -8.337 -31.094  11.918  1.00 15.81           C  
-ANISOU 2505  CA  LEU A 298     1897   2428   1682     73     49    307       C  
-ATOM   2506  C   LEU A 298      -8.621 -32.578  11.694  1.00 20.87           C  
-ANISOU 2506  C   LEU A 298     2531   3096   2304     30     30    270       C  
-ATOM   2507  O   LEU A 298      -8.366 -33.406  12.573  1.00 18.70           O  
-ANISOU 2507  O   LEU A 298     2276   2780   2048      6     17    240       O  
-ATOM   2508  CB  LEU A 298      -9.582 -30.348  12.392  1.00 15.69           C  
-ANISOU 2508  CB  LEU A 298     1869   2444   1650     99     58    342       C  
-ATOM   2509  CG  LEU A 298      -9.293 -28.912  12.841  1.00 17.81           C  
-ANISOU 2509  CG  LEU A 298     2152   2673   1945    141     79    374       C  
-ATOM   2510  CD1 LEU A 298     -10.552 -28.260  13.397  1.00 17.28           C  
-ANISOU 2510  CD1 LEU A 298     2073   2633   1860    166     87    406       C  
-ATOM   2511  CD2 LEU A 298      -8.190 -28.912  13.876  1.00 21.82           C  
-ANISOU 2511  CD2 LEU A 298     2695   3098   2499    134     73    348       C  
-ATOM   2512  N   ASP A 299      -9.107 -32.930  10.512  1.00 15.45           N  
-ANISOU 2512  N   ASP A 299     1816   2476   1580     21     28    269       N  
-ATOM   2513  CA  ASP A 299      -9.361 -34.332  10.236  1.00 17.28           C  
-ANISOU 2513  CA  ASP A 299     2040   2732   1795    -23     12    230       C  
-ATOM   2514  C   ASP A 299      -8.050 -35.116  10.185  1.00 20.94           C  
-ANISOU 2514  C   ASP A 299     2530   3141   2287    -46      7    192       C  
-ATOM   2515  O   ASP A 299      -7.965 -36.223  10.689  1.00 16.04           O  
-ANISOU 2515  O   ASP A 299     1922   2495   1677    -78     -5    159       O  
-ATOM   2516  CB  ASP A 299     -10.146 -34.524   8.940  1.00 20.75           C  
-ANISOU 2516  CB  ASP A 299     2441   3258   2184    -29     10    233       C  
-ATOM   2517  CG  ASP A 299     -10.443 -35.986   8.665  1.00 24.08           C  
-ANISOU 2517  CG  ASP A 299     2856   3703   2592    -78     -7    187       C  
-ATOM   2518  OD1 ASP A 299     -11.171 -36.611   9.464  1.00 24.36           O  
-ANISOU 2518  OD1 ASP A 299     2890   3735   2631   -101    -15    175       O  
-ATOM   2519  OD2 ASP A 299      -9.942 -36.520   7.664  1.00 18.58           O  
-ANISOU 2519  OD2 ASP A 299     2153   3024   1881    -94     -9    163       O  
-ATOM   2520  N   PHE A 300      -7.029 -34.531   9.572  1.00 13.76           N  
-ANISOU 2520  N   PHE A 300     1626   2212   1390    -26     18    201       N  
-ATOM   2521  CA  PHE A 300      -5.727 -35.197   9.463  1.00 12.88           C  
-ANISOU 2521  CA  PHE A 300     1537   2051   1306    -43     15    168       C  
-ATOM   2522  C   PHE A 300      -5.151 -35.408  10.852  1.00 13.21           C  
-ANISOU 2522  C   PHE A 300     1610   2020   1390    -48      8    155       C  
-ATOM   2523  O   PHE A 300      -4.756 -36.511  11.189  1.00 12.95           O  
-ANISOU 2523  O   PHE A 300     1592   1958   1369    -76     -2    121       O  
-ATOM   2524  CB  PHE A 300      -4.785 -34.367   8.607  1.00 13.01           C  
-ANISOU 2524  CB  PHE A 300     1551   2061   1330    -18     31    186       C  
-ATOM   2525  CG  PHE A 300      -3.400 -34.936   8.494  1.00 14.47           C  
-ANISOU 2525  CG  PHE A 300     1757   2196   1546    -31     31    157       C  
-ATOM   2526  CD1 PHE A 300      -3.216 -36.289   8.269  1.00 13.16           C  
-ANISOU 2526  CD1 PHE A 300     1596   2030   1374    -66     19    116       C  
-ATOM   2527  CD2 PHE A 300      -2.289 -34.116   8.604  1.00 16.21           C  
-ANISOU 2527  CD2 PHE A 300     1990   2367   1802     -9     43    171       C  
-ATOM   2528  CE1 PHE A 300      -1.939 -36.818   8.150  1.00 18.29           C  
-ANISOU 2528  CE1 PHE A 300     2265   2635   2051    -75     20     91       C  
-ATOM   2529  CE2 PHE A 300      -1.004 -34.645   8.491  1.00 16.16           C  
-ANISOU 2529  CE2 PHE A 300     1999   2317   1824    -20     42    145       C  
-ATOM   2530  CZ  PHE A 300      -0.837 -35.988   8.272  1.00 15.65           C  
-ANISOU 2530  CZ  PHE A 300     1940   2256   1751    -51     31    107       C  
-ATOM   2531  N   LEU A 301      -5.119 -34.352  11.659  1.00 13.73           N  
-ANISOU 2531  N   LEU A 301     1686   2056   1477    -20     15    181       N  
-ATOM   2532  CA  LEU A 301      -4.614 -34.454  13.029  1.00 12.83           C  
-ANISOU 2532  CA  LEU A 301     1600   1878   1398    -21      7    169       C  
-ATOM   2533  C   LEU A 301      -5.380 -35.517  13.809  1.00 14.49           C  
-ANISOU 2533  C   LEU A 301     1816   2092   1599    -47     -6    150       C  
-ATOM   2534  O   LEU A 301      -4.781 -36.352  14.497  1.00 13.42           O  
-ANISOU 2534  O   LEU A 301     1701   1913   1485    -64    -15    124       O  
-ATOM   2535  CB  LEU A 301      -4.721 -33.109  13.746  1.00 13.19           C  
-ANISOU 2535  CB  LEU A 301     1651   1901   1459     14     16    199       C  
-ATOM   2536  CG  LEU A 301      -4.337 -33.111  15.227  1.00 15.24           C  
-ANISOU 2536  CG  LEU A 301     1938   2102   1749     16      7    187       C  
-ATOM   2537  CD1 LEU A 301      -2.839 -33.453  15.417  1.00 11.44           C  
-ANISOU 2537  CD1 LEU A 301     1477   1565   1304      8      1    160       C  
-ATOM   2538  CD2 LEU A 301      -4.686 -31.755  15.867  1.00 16.30           C  
-ANISOU 2538  CD2 LEU A 301     2077   2224   1893     50     18    216       C  
-ATOM   2539  N   ASP A 302      -6.709 -35.476  13.696  1.00 11.08           N  
-ANISOU 2539  N   ASP A 302     1361   1712   1135    -48     -6    166       N  
-ATOM   2540  CA  ASP A 302      -7.570 -36.438  14.370  1.00 12.93           C  
-ANISOU 2540  CA  ASP A 302     1596   1956   1360    -74    -15    152       C  
-ATOM   2541  C   ASP A 302      -7.205 -37.876  14.023  1.00 14.36           C  
-ANISOU 2541  C   ASP A 302     1783   2130   1543   -113    -22    112       C  
-ATOM   2542  O   ASP A 302      -7.375 -38.778  14.838  1.00 14.26           O  
-ANISOU 2542  O   ASP A 302     1784   2093   1541   -133    -28     95       O  
-ATOM   2543  CB  ASP A 302      -9.031 -36.198  13.981  1.00 16.89           C  
-ANISOU 2543  CB  ASP A 302     2065   2528   1824    -72    -12    173       C  
-ATOM   2544  CG  ASP A 302      -9.992 -36.992  14.840  1.00 23.97           C  
-ANISOU 2544  CG  ASP A 302     2961   3431   2715    -94    -18    166       C  
-ATOM   2545  OD1 ASP A 302      -9.848 -36.948  16.076  1.00 18.24           O  
-ANISOU 2545  OD1 ASP A 302     2259   2659   2011    -86    -19    168       O  
-ATOM   2546  OD2 ASP A 302     -10.873 -37.676  14.276  1.00 22.53           O  
-ANISOU 2546  OD2 ASP A 302     2753   3300   2507   -121    -22    156       O  
-ATOM   2547  N   LYS A 303      -6.727 -38.090  12.798  1.00 13.25           N  
-ANISOU 2547  N   LYS A 303     1631   2011   1392   -122    -20     99       N  
-ATOM   2548  CA  LYS A 303      -6.422 -39.432  12.327  1.00  7.65           C  
-ANISOU 2548  CA  LYS A 303      926   1298    682   -159    -25     60       C  
-ATOM   2549  C   LYS A 303      -4.999 -39.873  12.681  1.00 10.87           C  
-ANISOU 2549  C   LYS A 303     1364   1639   1127   -160    -26     39       C  
-ATOM   2550  O   LYS A 303      -4.669 -41.047  12.555  1.00 12.84           O  
-ANISOU 2550  O   LYS A 303     1624   1871   1383   -188    -28      7       O  
-ATOM   2551  CB  LYS A 303      -6.667 -39.535  10.817  1.00  9.15           C  
-ANISOU 2551  CB  LYS A 303     1089   1550    838   -169    -23     52       C  
-ATOM   2552  CG  LYS A 303      -8.162 -39.570  10.453  1.00 15.23           C  
-ANISOU 2552  CG  LYS A 303     1826   2394   1569   -180    -27     61       C  
-ATOM   2553  CD  LYS A 303      -8.372 -39.403   8.956  1.00 24.26           C  
-ANISOU 2553  CD  LYS A 303     2940   3605   2674   -180    -25     59       C  
-ATOM   2554  CE  LYS A 303      -9.761 -39.859   8.543  1.00 23.95           C  
-ANISOU 2554  CE  LYS A 303     2866   3638   2595   -204    -33     52       C  
-ATOM   2555  NZ  LYS A 303     -10.780 -39.395   9.526  1.00 25.12           N  
-ANISOU 2555  NZ  LYS A 303     3006   3794   2744   -193    -34     80       N  
-ATOM   2556  N   LEU A 304      -4.166 -38.936  13.132  1.00 14.49           N  
-ANISOU 2556  N   LEU A 304     1836   2059   1609   -130    -23     57       N  
-ATOM   2557  CA  LEU A 304      -2.828 -39.277  13.625  1.00 14.62           C  
-ANISOU 2557  CA  LEU A 304     1880   2014   1663   -128    -25     39       C  
-ATOM   2558  C   LEU A 304      -2.880 -39.565  15.129  1.00 15.95           C  
-ANISOU 2558  C   LEU A 304     2070   2139   1851   -126    -33     38       C  
-ATOM   2559  O   LEU A 304      -2.313 -40.546  15.612  1.00 11.66           O  
-ANISOU 2559  O   LEU A 304     1546   1558   1326   -140    -37     16       O  
-ATOM   2560  CB  LEU A 304      -1.850 -38.131  13.367  1.00 11.76           C  
-ANISOU 2560  CB  LEU A 304     1518   1631   1319    -99    -19     56       C  
-ATOM   2561  CG  LEU A 304      -1.496 -37.772  11.918  1.00 12.22           C  
-ANISOU 2561  CG  LEU A 304     1558   1723   1363    -94     -8     61       C  
-ATOM   2562  CD1 LEU A 304      -0.530 -36.593  11.885  1.00 14.93           C  
-ANISOU 2562  CD1 LEU A 304     1903   2035   1732    -64      1     81       C  
-ATOM   2563  CD2 LEU A 304      -0.901 -38.969  11.197  1.00 16.97           C  
-ANISOU 2563  CD2 LEU A 304     2164   2322   1963   -119     -9     27       C  
-ATOM   2564  N   LEU A 305      -3.570 -38.698  15.863  1.00  9.26           N  
-ANISOU 2564  N   LEU A 305     1220   1298    999   -106    -33     64       N  
-ATOM   2565  CA  LEU A 305      -3.639 -38.809  17.314  1.00  8.11           C  
-ANISOU 2565  CA  LEU A 305     1096   1117    869    -98    -40     65       C  
-ATOM   2566  C   LEU A 305      -4.734 -39.772  17.778  1.00 13.02           C  
-ANISOU 2566  C   LEU A 305     1717   1756   1475   -121    -41     61       C  
-ATOM   2567  O   LEU A 305      -5.809 -39.345  18.230  1.00 14.69           O  
-ANISOU 2567  O   LEU A 305     1918   1992   1670   -114    -39     81       O  
-ATOM   2568  CB  LEU A 305      -3.798 -37.424  17.948  1.00 13.54           C  
-ANISOU 2568  CB  LEU A 305     1785   1799   1561    -65    -38     92       C  
-ATOM   2569  CG  LEU A 305      -2.624 -36.455  17.713  1.00 13.78           C  
-ANISOU 2569  CG  LEU A 305     1820   1801   1616    -43    -36     95       C  
-ATOM   2570  CD1 LEU A 305      -2.843 -35.123  18.411  1.00 14.01           C  
-ANISOU 2570  CD1 LEU A 305     1852   1819   1651    -12    -32    118       C  
-ATOM   2571  CD2 LEU A 305      -1.271 -37.086  18.148  1.00 11.71           C  
-ANISOU 2571  CD2 LEU A 305     1578   1487   1383    -48    -45     69       C  
-ATOM   2572  N   ARG A 306      -4.460 -41.066  17.633  1.00 11.77           N  
-ANISOU 2572  N   ARG A 306     1567   1583   1324   -149    -41     34       N  
-ATOM   2573  CA  ARG A 306      -5.316 -42.134  18.165  1.00 16.22           C  
-ANISOU 2573  CA  ARG A 306     2132   2149   1880   -174    -39     26       C  
-ATOM   2574  C   ARG A 306      -4.569 -42.875  19.267  1.00 15.18           C  
-ANISOU 2574  C   ARG A 306     2032   1960   1776   -171    -41     16       C  
-ATOM   2575  O   ARG A 306      -3.367 -43.138  19.130  1.00 12.13           O  
-ANISOU 2575  O   ARG A 306     1660   1539   1409   -168    -43      1       O  
-ATOM   2576  CB  ARG A 306      -5.685 -43.156  17.079  1.00 16.18           C  
-ANISOU 2576  CB  ARG A 306     2113   2173   1863   -213    -34      1       C  
-ATOM   2577  CG  ARG A 306      -5.997 -42.602  15.698  1.00 20.67           C  
-ANISOU 2577  CG  ARG A 306     2652   2797   2405   -216    -34      3       C  
-ATOM   2578  CD  ARG A 306      -7.187 -41.648  15.685  1.00 14.86           C  
-ANISOU 2578  CD  ARG A 306     1891   2113   1643   -202    -34     33       C  
-ATOM   2579  NE  ARG A 306      -8.367 -42.186  16.360  1.00 16.74           N  
-ANISOU 2579  NE  ARG A 306     2121   2366   1873   -219    -32     36       N  
-ATOM   2580  CZ  ARG A 306      -9.517 -41.524  16.470  1.00 23.86           C  
-ANISOU 2580  CZ  ARG A 306     3001   3313   2753   -210    -31     62       C  
-ATOM   2581  NH1 ARG A 306      -9.652 -40.307  15.949  1.00 19.50           N  
-ANISOU 2581  NH1 ARG A 306     2431   2794   2183   -181    -31     87       N  
-ATOM   2582  NH2 ARG A 306     -10.539 -42.074  17.105  1.00 23.47           N  
-ANISOU 2582  NH2 ARG A 306     2945   3276   2699   -227    -28     65       N  
-ATOM   2583  N   TYR A 307      -5.257 -43.228  20.356  1.00 15.70           N  
-ANISOU 2583  N   TYR A 307     2107   2017   1841   -171    -38     26       N  
-ATOM   2584  CA  TYR A 307      -4.615 -44.043  21.391  1.00 13.78           C  
-ANISOU 2584  CA  TYR A 307     1893   1724   1619   -167    -38     19       C  
-ATOM   2585  C   TYR A 307      -4.084 -45.320  20.743  1.00 16.10           C  
-ANISOU 2585  C   TYR A 307     2193   1998   1926   -196    -31     -9       C  
-ATOM   2586  O   TYR A 307      -2.914 -45.666  20.883  1.00 14.00           O  
-ANISOU 2586  O   TYR A 307     1946   1694   1681   -188    -34    -21       O  
-ATOM   2587  CB  TYR A 307      -5.608 -44.448  22.482  1.00 14.89           C  
-ANISOU 2587  CB  TYR A 307     2040   1865   1754   -169    -32     34       C  
-ATOM   2588  CG  TYR A 307      -5.969 -43.379  23.492  1.00  9.87           C  
-ANISOU 2588  CG  TYR A 307     1407   1232   1109   -135    -37     60       C  
-ATOM   2589  CD1 TYR A 307      -4.993 -42.796  24.299  1.00  9.86           C  
-ANISOU 2589  CD1 TYR A 307     1427   1198   1121   -102    -47     63       C  
-ATOM   2590  CD2 TYR A 307      -7.291 -42.988  23.670  1.00 11.28           C  
-ANISOU 2590  CD2 TYR A 307     1570   1450   1268   -135    -31     80       C  
-ATOM   2591  CE1 TYR A 307      -5.319 -41.839  25.243  1.00 10.50           C  
-ANISOU 2591  CE1 TYR A 307     1514   1283   1194    -71    -52     82       C  
-ATOM   2592  CE2 TYR A 307      -7.634 -42.031  24.620  1.00 12.82           C  
-ANISOU 2592  CE2 TYR A 307     1770   1647   1454   -103    -34    103       C  
-ATOM   2593  CZ  TYR A 307      -6.642 -41.463  25.399  1.00 11.41           C  
-ANISOU 2593  CZ  TYR A 307     1614   1433   1287    -71    -44    102       C  
-ATOM   2594  OH  TYR A 307      -6.962 -40.519  26.329  1.00 14.50           O  
-ANISOU 2594  OH  TYR A 307     2013   1826   1670    -39    -46    121       O  
-ATOM   2595  N   ASP A 308      -4.967 -46.017  20.031  1.00 11.03           N  
-ANISOU 2595  N   ASP A 308     1534   1385   1271   -231    -22    -21       N  
-ATOM   2596  CA  ASP A 308      -4.633 -47.309  19.425  1.00  9.46           C  
-ANISOU 2596  CA  ASP A 308     1342   1168   1084   -263    -13    -51       C  
-ATOM   2597  C   ASP A 308      -3.653 -47.133  18.271  1.00 10.89           C  
-ANISOU 2597  C   ASP A 308     1519   1351   1267   -263    -16    -70       C  
-ATOM   2598  O   ASP A 308      -4.006 -46.597  17.222  1.00 14.36           O  
-ANISOU 2598  O   ASP A 308     1934   1836   1686   -270    -19    -73       O  
-ATOM   2599  CB  ASP A 308      -5.909 -48.009  18.928  1.00 11.30           C  
-ANISOU 2599  CB  ASP A 308     1554   1435   1303   -304     -3    -63       C  
-ATOM   2600  CG  ASP A 308      -5.679 -49.471  18.592  1.00 19.77           C  
-ANISOU 2600  CG  ASP A 308     2640   2479   2394   -339     11    -95       C  
-ATOM   2601  OD1 ASP A 308      -4.509 -49.861  18.416  1.00 16.78           O  
-ANISOU 2601  OD1 ASP A 308     2280   2063   2033   -331     13   -109       O  
-ATOM   2602  OD2 ASP A 308      -6.665 -50.237  18.523  1.00 17.40           O  
-ANISOU 2602  OD2 ASP A 308     2329   2193   2091   -373     22   -105       O  
-ATOM   2603  N   HIS A 309      -2.412 -47.571  18.477  1.00 13.38           N  
-ANISOU 2603  N   HIS A 309     1857   1620   1607   -252    -15    -81       N  
-ATOM   2604  CA  HIS A 309      -1.360 -47.394  17.481  1.00 11.12           C  
-ANISOU 2604  CA  HIS A 309     1568   1331   1326   -248    -17    -96       C  
-ATOM   2605  C   HIS A 309      -1.730 -48.055  16.154  1.00 11.53           C  
-ANISOU 2605  C   HIS A 309     1605   1412   1363   -283     -9   -124       C  
-ATOM   2606  O   HIS A 309      -1.319 -47.593  15.094  1.00 16.33           O  
-ANISOU 2606  O   HIS A 309     2200   2045   1961   -280    -10   -131       O  
-ATOM   2607  CB  HIS A 309      -0.036 -47.950  17.998  1.00 10.39           C  
-ANISOU 2607  CB  HIS A 309     1501   1184   1263   -232    -16   -104       C  
-ATOM   2608  CG  HIS A 309      -0.130 -49.357  18.522  1.00 13.59           C  
-ANISOU 2608  CG  HIS A 309     1927   1553   1683   -250     -2   -116       C  
-ATOM   2609  ND1 HIS A 309      -0.571 -49.655  19.796  1.00 12.91           N  
-ANISOU 2609  ND1 HIS A 309     1855   1447   1604   -242      0    -99       N  
-ATOM   2610  CD2 HIS A 309       0.165 -50.547  17.944  1.00 12.13           C  
-ANISOU 2610  CD2 HIS A 309     1751   1347   1510   -274     13   -143       C  
-ATOM   2611  CE1 HIS A 309      -0.528 -50.961  19.983  1.00 15.80           C  
-ANISOU 2611  CE1 HIS A 309     2238   1779   1985   -260     17   -113       C  
-ATOM   2612  NE2 HIS A 309      -0.077 -51.526  18.875  1.00 12.85           N  
-ANISOU 2612  NE2 HIS A 309     1863   1404   1617   -280     25   -141       N  
-ATOM   2613  N   GLN A 310      -2.534 -49.116  16.221  1.00 12.00           N  
-ANISOU 2613  N   GLN A 310     1666   1472   1422   -316      2   -140       N  
-ATOM   2614  CA  GLN A 310      -2.998 -49.806  15.021  1.00 13.71           C  
-ANISOU 2614  CA  GLN A 310     1868   1719   1624   -353      9   -171       C  
-ATOM   2615  C   GLN A 310      -4.025 -48.983  14.230  1.00 17.52           C  
-ANISOU 2615  C   GLN A 310     2316   2272   2070   -361      0   -164       C  
-ATOM   2616  O   GLN A 310      -4.256 -49.246  13.056  1.00 21.80           O  
-ANISOU 2616  O   GLN A 310     2840   2851   2592   -384      2   -189       O  
-ATOM   2617  CB  GLN A 310      -3.604 -51.169  15.378  1.00 16.55           C  
-ANISOU 2617  CB  GLN A 310     2238   2055   1997   -389     24   -192       C  
-ATOM   2618  CG  GLN A 310      -2.585 -52.221  15.828  1.00 16.02           C  
-ANISOU 2618  CG  GLN A 310     2204   1920   1964   -387     38   -205       C  
-ATOM   2619  CD  GLN A 310      -3.238 -53.565  16.137  1.00 22.15           C  
-ANISOU 2619  CD  GLN A 310     2990   2670   2755   -424     58   -224       C  
-ATOM   2620  OE1 GLN A 310      -4.403 -53.792  15.807  1.00 23.71           O  
-ANISOU 2620  OE1 GLN A 310     3168   2903   2939   -458     61   -235       O  
-ATOM   2621  NE2 GLN A 310      -2.486 -54.464  16.768  1.00 20.70           N  
-ANISOU 2621  NE2 GLN A 310     2837   2425   2603   -417     74   -227       N  
-ATOM   2622  N   SER A 311      -4.638 -47.996  14.871  1.00 16.22           N  
-ANISOU 2622  N   SER A 311     2141   2129   1895   -339     -8   -131       N  
-ATOM   2623  CA  SER A 311      -5.673 -47.184  14.217  1.00 17.81           C  
-ANISOU 2623  CA  SER A 311     2308   2398   2062   -341    -15   -118       C  
-ATOM   2624  C   SER A 311      -5.134 -45.910  13.556  1.00 15.40           C  
-ANISOU 2624  C   SER A 311     1991   2118   1743   -308    -22   -100       C  
-ATOM   2625  O   SER A 311      -5.857 -45.220  12.819  1.00 16.17           O  
-ANISOU 2625  O   SER A 311     2060   2275   1809   -306    -25    -88       O  
-ATOM   2626  CB  SER A 311      -6.769 -46.814  15.222  1.00 19.97           C  
-ANISOU 2626  CB  SER A 311     2574   2685   2330   -335    -17    -91       C  
-ATOM   2627  OG  SER A 311      -7.411 -47.976  15.708  1.00 20.18           O  
-ANISOU 2627  OG  SER A 311     2604   2695   2367   -369     -7   -106       O  
-ATOM   2628  N   ARG A 312      -3.875 -45.584  13.820  1.00 11.53           N  
-ANISOU 2628  N   ARG A 312     1521   1583   1275   -282    -22    -94       N  
-ATOM   2629  CA  ARG A 312      -3.304 -44.364  13.260  1.00 17.36           C  
-ANISOU 2629  CA  ARG A 312     2250   2338   2007   -252    -25    -75       C  
-ATOM   2630  C   ARG A 312      -3.084 -44.494  11.766  1.00 12.80           C  
-ANISOU 2630  C   ARG A 312     1657   1798   1410   -263    -21    -94       C  
-ATOM   2631  O   ARG A 312      -2.858 -45.599  11.272  1.00 15.63           O  
-ANISOU 2631  O   ARG A 312     2022   2148   1770   -290    -16   -128       O  
-ATOM   2632  CB  ARG A 312      -1.983 -44.033  13.953  1.00 12.82           C  
-ANISOU 2632  CB  ARG A 312     1700   1705   1466   -225    -27    -68       C  
-ATOM   2633  CG  ARG A 312      -2.184 -43.790  15.439  1.00 12.41           C  
-ANISOU 2633  CG  ARG A 312     1664   1622   1430   -209    -32    -49       C  
-ATOM   2634  CD  ARG A 312      -0.857 -43.645  16.168  1.00 13.88           C  
-ANISOU 2634  CD  ARG A 312     1873   1754   1649   -186    -36    -49       C  
-ATOM   2635  NE  ARG A 312      -1.078 -43.857  17.599  1.00 12.13           N  
-ANISOU 2635  NE  ARG A 312     1669   1501   1438   -177    -41    -40       N  
-ATOM   2636  CZ  ARG A 312      -0.173 -44.318  18.446  1.00 11.88           C  
-ANISOU 2636  CZ  ARG A 312     1660   1422   1431   -166    -44    -46       C  
-ATOM   2637  NH1 ARG A 312       1.061 -44.602  18.028  1.00  9.98           N  
-ANISOU 2637  NH1 ARG A 312     1427   1155   1210   -163    -43    -61       N  
-ATOM   2638  NH2 ARG A 312      -0.504 -44.481  19.718  1.00 11.43           N  
-ANISOU 2638  NH2 ARG A 312     1618   1346   1378   -156    -47    -35       N  
-ATOM   2639  N   LEU A 313      -3.175 -43.369  11.050  1.00 14.10           N  
-ANISOU 2639  N   LEU A 313     1800   2003   1553   -241    -22    -71       N  
-ATOM   2640  CA  LEU A 313      -2.753 -43.316   9.651  1.00 13.97           C  
-ANISOU 2640  CA  LEU A 313     1771   2020   1518   -242    -16    -83       C  
-ATOM   2641  C   LEU A 313      -1.297 -43.773   9.547  1.00 14.85           C  
-ANISOU 2641  C   LEU A 313     1905   2078   1659   -238    -11   -101       C  
-ATOM   2642  O   LEU A 313      -0.465 -43.434  10.398  1.00 14.51           O  
-ANISOU 2642  O   LEU A 313     1880   1984   1648   -218    -12    -89       O  
-ATOM   2643  CB  LEU A 313      -2.831 -41.886   9.106  1.00 13.10           C  
-ANISOU 2643  CB  LEU A 313     1641   1947   1390   -208    -14    -46       C  
-ATOM   2644  CG  LEU A 313      -4.215 -41.294   8.842  1.00 17.71           C  
-ANISOU 2644  CG  LEU A 313     2195   2597   1936   -205    -17    -24       C  
-ATOM   2645  CD1 LEU A 313      -4.074 -39.872   8.380  1.00 17.18           C  
-ANISOU 2645  CD1 LEU A 313     2115   2554   1860   -166    -10     15       C  
-ATOM   2646  CD2 LEU A 313      -4.961 -42.117   7.817  1.00 18.11           C  
-ANISOU 2646  CD2 LEU A 313     2224   2707   1950   -236    -20    -53       C  
-ATOM   2647  N   THR A 314      -0.998 -44.537   8.503  1.00 12.49           N  
-ANISOU 2647  N   THR A 314     1604   1794   1347   -257     -5   -132       N  
-ATOM   2648  CA  THR A 314       0.385 -44.839   8.167  1.00 15.26           C  
-ANISOU 2648  CA  THR A 314     1972   2106   1721   -249      3   -146       C  
-ATOM   2649  C   THR A 314       0.949 -43.624   7.446  1.00 16.88           C  
-ANISOU 2649  C   THR A 314     2163   2332   1919   -217      9   -119       C  
-ATOM   2650  O   THR A 314       0.201 -42.717   7.059  1.00 11.64           O  
-ANISOU 2650  O   THR A 314     1478   1718   1229   -204      8    -94       O  
-ATOM   2651  CB  THR A 314       0.529 -46.097   7.268  1.00 16.89           C  
-ANISOU 2651  CB  THR A 314     2182   2319   1915   -279     11   -191       C  
-ATOM   2652  OG1 THR A 314      -0.054 -45.862   5.979  1.00 15.50           O  
-ANISOU 2652  OG1 THR A 314     1980   2213   1695   -285     12   -197       O  
-ATOM   2653  CG2 THR A 314      -0.121 -47.312   7.914  1.00 12.26           C  
-ANISOU 2653  CG2 THR A 314     1608   1713   1338   -314      9   -218       C  
-ATOM   2654  N   ALA A 315       2.263 -43.597   7.262  1.00 14.41           N  
-ANISOU 2654  N   ALA A 315     1862   1982   1632   -203     17   -122       N  
-ATOM   2655  CA  ALA A 315       2.883 -42.479   6.577  1.00 11.71           C  
-ANISOU 2655  CA  ALA A 315     1507   1654   1288   -174     26    -96       C  
-ATOM   2656  C   ALA A 315       2.349 -42.389   5.148  1.00 13.77           C  
-ANISOU 2656  C   ALA A 315     1746   1985   1503   -176     33    -99       C  
-ATOM   2657  O   ALA A 315       2.072 -41.307   4.662  1.00 14.51           O  
-ANISOU 2657  O   ALA A 315     1820   2115   1578   -154     38    -67       O  
-ATOM   2658  CB  ALA A 315       4.406 -42.618   6.578  1.00 10.32           C  
-ANISOU 2658  CB  ALA A 315     1345   1428   1148   -162     34   -103       C  
-ATOM   2659  N   ARG A 316       2.217 -43.531   4.478  1.00 14.39           N  
-ANISOU 2659  N   ARG A 316     1826   2080   1561   -203     34   -138       N  
-ATOM   2660  CA  ARG A 316       1.766 -43.531   3.102  1.00 18.76           C  
-ANISOU 2660  CA  ARG A 316     2358   2702   2067   -207     39   -146       C  
-ATOM   2661  C   ARG A 316       0.317 -43.045   3.017  1.00 17.86           C  
-ANISOU 2661  C   ARG A 316     2220   2652   1915   -210     29   -129       C  
-ATOM   2662  O   ARG A 316       0.001 -42.189   2.195  1.00 16.65           O  
-ANISOU 2662  O   ARG A 316     2043   2553   1728   -188     33   -104       O  
-ATOM   2663  CB  ARG A 316       1.921 -44.913   2.482  1.00 25.06           C  
-ANISOU 2663  CB  ARG A 316     3167   3502   2854   -238     42   -197       C  
-ATOM   2664  CG  ARG A 316       1.825 -44.912   0.976  1.00 32.68           C  
-ANISOU 2664  CG  ARG A 316     4112   4532   3771   -236     49   -210       C  
-ATOM   2665  CD  ARG A 316       3.045 -44.242   0.368  1.00 33.59           C  
-ANISOU 2665  CD  ARG A 316     4229   4636   3897   -202     66   -188       C  
-ATOM   2666  NE  ARG A 316       2.842 -43.924  -1.040  1.00 37.24           N  
-ANISOU 2666  NE  ARG A 316     4671   5171   4309   -190     74   -186       N  
-ATOM   2667  CZ  ARG A 316       3.233 -44.702  -2.043  1.00 39.95           C  
-ANISOU 2667  CZ  ARG A 316     5017   5533   4629   -200     83   -222       C  
-ATOM   2668  NH1 ARG A 316       3.857 -45.844  -1.792  1.00 36.37           N  
-ANISOU 2668  NH1 ARG A 316     4588   5028   4202   -222     86   -263       N  
-ATOM   2669  NH2 ARG A 316       3.009 -44.330  -3.295  1.00 46.64           N  
-ANISOU 2669  NH2 ARG A 316     5843   6452   5426   -185     89   -217       N  
-ATOM   2670  N   GLU A 317      -0.552 -43.563   3.883  1.00 20.72           N  
-ANISOU 2670  N   GLU A 317     2586   3006   2282   -234     16   -140       N  
-ATOM   2671  CA  GLU A 317      -1.939 -43.089   3.938  1.00 19.64           C  
-ANISOU 2671  CA  GLU A 317     2423   2926   2113   -236      7   -122       C  
-ATOM   2672  C   GLU A 317      -2.000 -41.611   4.239  1.00 15.69           C  
-ANISOU 2672  C   GLU A 317     1914   2432   1617   -196     10    -69       C  
-ATOM   2673  O   GLU A 317      -2.847 -40.895   3.708  1.00 19.26           O  
-ANISOU 2673  O   GLU A 317     2339   2946   2032   -182     10    -44       O  
-ATOM   2674  CB  GLU A 317      -2.733 -43.789   5.037  1.00 19.38           C  
-ANISOU 2674  CB  GLU A 317     2398   2870   2094   -264     -4   -136       C  
-ATOM   2675  CG  GLU A 317      -2.967 -45.256   4.850  1.00 18.62           C  
-ANISOU 2675  CG  GLU A 317     2310   2770   1996   -308     -5   -187       C  
-ATOM   2676  CD  GLU A 317      -3.789 -45.824   5.983  1.00 24.97           C  
-ANISOU 2676  CD  GLU A 317     3119   3551   2817   -333    -12   -193       C  
-ATOM   2677  OE1 GLU A 317      -3.367 -45.717   7.160  1.00 16.99           O  
-ANISOU 2677  OE1 GLU A 317     2131   2480   1844   -321    -11   -176       O  
-ATOM   2678  OE2 GLU A 317      -4.874 -46.364   5.698  1.00 21.41           O  
-ANISOU 2678  OE2 GLU A 317     2649   3145   2341   -364    -18   -214       O  
-ATOM   2679  N   ALA A 318      -1.136 -41.153   5.142  1.00 13.91           N  
-ANISOU 2679  N   ALA A 318     1709   2140   1436   -178     14    -52       N  
-ATOM   2680  CA  ALA A 318      -1.126 -39.745   5.506  1.00 12.13           C  
-ANISOU 2680  CA  ALA A 318     1478   1911   1221   -141     19     -5       C  
-ATOM   2681  C   ALA A 318      -0.857 -38.898   4.258  1.00 16.66           C  
-ANISOU 2681  C   ALA A 318     2032   2528   1770   -114     34     20       C  
-ATOM   2682  O   ALA A 318      -1.473 -37.841   4.053  1.00 18.18           O  
-ANISOU 2682  O   ALA A 318     2206   2758   1944    -89     39     58       O  
-ATOM   2683  CB  ALA A 318      -0.082 -39.474   6.606  1.00 13.18           C  
-ANISOU 2683  CB  ALA A 318     1636   1965   1407   -129     20      2       C  
-ATOM   2684  N   MET A 319       0.042 -39.376   3.402  1.00 13.28           N  
-ANISOU 2684  N   MET A 319     1609   2097   1340   -118     42     -1       N  
-ATOM   2685  CA  MET A 319       0.398 -38.630   2.205  1.00 15.25           C  
-ANISOU 2685  CA  MET A 319     1842   2386   1568    -90     59     23       C  
-ATOM   2686  C   MET A 319      -0.755 -38.553   1.207  1.00 16.72           C  
-ANISOU 2686  C   MET A 319     1998   2662   1692    -89     57     28       C  
-ATOM   2687  O   MET A 319      -0.764 -37.683   0.340  1.00 17.25           O  
-ANISOU 2687  O   MET A 319     2048   2772   1735    -59     71     62       O  
-ATOM   2688  CB  MET A 319       1.658 -39.205   1.554  1.00 16.77           C  
-ANISOU 2688  CB  MET A 319     2046   2553   1773    -94     70     -1       C  
-ATOM   2689  CG  MET A 319       2.863 -39.060   2.459  1.00 19.83           C  
-ANISOU 2689  CG  MET A 319     2457   2859   2220    -87     74      1       C  
-ATOM   2690  SD  MET A 319       4.299 -39.836   1.733  1.00 21.15           S  
-ANISOU 2690  SD  MET A 319     2636   2997   2402    -92     87    -28       S  
-ATOM   2691  CE  MET A 319       4.618 -38.655   0.434  1.00 20.13           C  
-ANISOU 2691  CE  MET A 319     2485   2914   2251    -54    112     13       C  
-ATOM   2692  N   GLU A 320      -1.739 -39.434   1.360  1.00 18.27           N  
-ANISOU 2692  N   GLU A 320     2188   2888   1865   -122     39     -2       N  
-ATOM   2693  CA  GLU A 320      -2.947 -39.395   0.526  1.00 21.93           C  
-ANISOU 2693  CA  GLU A 320     2621   3443   2270   -124     32      0       C  
-ATOM   2694  C   GLU A 320      -4.002 -38.417   1.050  1.00 20.65           C  
-ANISOU 2694  C   GLU A 320     2439   3308   2097   -104     29     44       C  
-ATOM   2695  O   GLU A 320      -5.022 -38.195   0.394  1.00 22.25           O  
-ANISOU 2695  O   GLU A 320     2613   3591   2252    -98     24     55       O  
-ATOM   2696  CB  GLU A 320      -3.581 -40.791   0.410  1.00 19.95           C  
-ANISOU 2696  CB  GLU A 320     2367   3214   1999   -172     16    -55       C  
-ATOM   2697  CG  GLU A 320      -2.645 -41.900  -0.076  1.00 21.28           C  
-ANISOU 2697  CG  GLU A 320     2555   3354   2176   -196     20   -104       C  
-ATOM   2698  CD  GLU A 320      -2.428 -41.879  -1.574  1.00 25.98           C  
-ANISOU 2698  CD  GLU A 320     3135   4013   2725   -184     28   -112       C  
-ATOM   2699  OE1 GLU A 320      -3.383 -42.179  -2.317  1.00 26.11           O  
-ANISOU 2699  OE1 GLU A 320     3125   4106   2690   -198     17   -130       O  
-ATOM   2700  OE2 GLU A 320      -1.300 -41.574  -2.018  1.00 25.28           O  
-ANISOU 2700  OE2 GLU A 320     3057   3898   2650   -161     45   -101       O  
-ATOM   2701  N   HIS A 321      -3.790 -37.843   2.231  1.00 16.18           N  
-ANISOU 2701  N   HIS A 321     1891   2681   1576    -91     31     67       N  
-ATOM   2702  CA  HIS A 321      -4.855 -37.050   2.866  1.00 16.84           C  
-ANISOU 2702  CA  HIS A 321     1960   2786   1652    -75     28    103       C  
-ATOM   2703  C   HIS A 321      -5.165 -35.716   2.170  1.00 15.40           C  
-ANISOU 2703  C   HIS A 321     1755   2652   1444    -30     44    156       C  
-ATOM   2704  O   HIS A 321      -4.260 -35.033   1.703  1.00 17.60           O  
-ANISOU 2704  O   HIS A 321     2040   2912   1736     -2     63    179       O  
-ATOM   2705  CB  HIS A 321      -4.550 -36.815   4.355  1.00 20.12           C  
-ANISOU 2705  CB  HIS A 321     2402   3122   2120    -74     27    110       C  
-ATOM   2706  CG  HIS A 321      -5.740 -36.367   5.147  1.00 22.62           C  
-ANISOU 2706  CG  HIS A 321     2707   3457   2429    -68     20    134       C  
-ATOM   2707  ND1 HIS A 321      -6.159 -35.056   5.184  1.00 20.36           N  
-ANISOU 2707  ND1 HIS A 321     2408   3190   2136    -29     33    183       N  
-ATOM   2708  CD2 HIS A 321      -6.608 -37.059   5.924  1.00 15.63           C  
-ANISOU 2708  CD2 HIS A 321     1822   2575   1542    -95      6    116       C  
-ATOM   2709  CE1 HIS A 321      -7.231 -34.957   5.951  1.00 17.67           C  
-ANISOU 2709  CE1 HIS A 321     2060   2864   1789    -31     25    194       C  
-ATOM   2710  NE2 HIS A 321      -7.526 -36.159   6.410  1.00 16.05           N  
-ANISOU 2710  NE2 HIS A 321     1861   2651   1587    -72      8    154       N  
-ATOM   2711  N   PRO A 322      -6.464 -35.339   2.099  1.00 15.12           N  
-ANISOU 2711  N   PRO A 322     1692   2681   1372    -21     39    179       N  
-ATOM   2712  CA  PRO A 322      -6.861 -34.059   1.493  1.00 17.97           C  
-ANISOU 2712  CA  PRO A 322     2030   3091   1707     26     56    234       C  
-ATOM   2713  C   PRO A 322      -6.088 -32.819   1.991  1.00 16.23           C  
-ANISOU 2713  C   PRO A 322     1828   2806   1531     65     79    277       C  
-ATOM   2714  O   PRO A 322      -5.974 -31.831   1.255  1.00 16.40           O  
-ANISOU 2714  O   PRO A 322     1838   2855   1540    104    101    320       O  
-ATOM   2715  CB  PRO A 322      -8.358 -33.961   1.843  1.00 17.98           C  
-ANISOU 2715  CB  PRO A 322     2006   3148   1679     25     44    248       C  
-ATOM   2716  CG  PRO A 322      -8.810 -35.382   1.890  1.00 19.75           C  
-ANISOU 2716  CG  PRO A 322     2225   3391   1887    -27     20    192       C  
-ATOM   2717  CD  PRO A 322      -7.634 -36.159   2.471  1.00 19.58           C  
-ANISOU 2717  CD  PRO A 322     2242   3282   1915    -55     18    153       C  
-ATOM   2718  N   TYR A 323      -5.571 -32.863   3.215  1.00 16.49           N  
-ANISOU 2718  N   TYR A 323     1891   2758   1617     53     76    266       N  
-ATOM   2719  CA  TYR A 323      -4.765 -31.771   3.760  1.00 19.60           C  
-ANISOU 2719  CA  TYR A 323     2303   3086   2058     83     96    297       C  
-ATOM   2720  C   TYR A 323      -3.636 -31.382   2.793  1.00 14.72           C  
-ANISOU 2720  C   TYR A 323     1687   2458   1449    101    117    308       C  
-ATOM   2721  O   TYR A 323      -3.253 -30.216   2.691  1.00 20.48           O  
-ANISOU 2721  O   TYR A 323     2418   3167   2198    136    142    349       O  
-ATOM   2722  CB  TYR A 323      -4.192 -32.201   5.125  1.00 20.93           C  
-ANISOU 2722  CB  TYR A 323     2503   3172   2277     59     84    267       C  
-ATOM   2723  CG  TYR A 323      -3.380 -31.170   5.892  1.00 15.71           C  
-ANISOU 2723  CG  TYR A 323     1862   2438   1668     83     99    289       C  
-ATOM   2724  CD1 TYR A 323      -3.919 -29.938   6.247  1.00 17.09           C  
-ANISOU 2724  CD1 TYR A 323     2033   2613   1849    117    115    332       C  
-ATOM   2725  CD2 TYR A 323      -2.086 -31.461   6.319  1.00 13.12           C  
-ANISOU 2725  CD2 TYR A 323     1558   2042   1386     70     98    264       C  
-ATOM   2726  CE1 TYR A 323      -3.190 -29.012   6.976  1.00 11.61           C  
-ANISOU 2726  CE1 TYR A 323     1357   1849   1204    134    129    346       C  
-ATOM   2727  CE2 TYR A 323      -1.345 -30.546   7.037  1.00 14.16           C  
-ANISOU 2727  CE2 TYR A 323     1706   2110   1566     87    109    278       C  
-ATOM   2728  CZ  TYR A 323      -1.894 -29.330   7.362  1.00 14.72           C  
-ANISOU 2728  CZ  TYR A 323     1772   2179   1642    118    125    317       C  
-ATOM   2729  OH  TYR A 323      -1.155 -28.436   8.087  1.00 20.27           O  
-ANISOU 2729  OH  TYR A 323     2491   2815   2394    132    137    326       O  
-ATOM   2730  N   PHE A 324      -3.130 -32.357   2.053  1.00 16.82           N  
-ANISOU 2730  N   PHE A 324     1952   2739   1698     78    110    273       N  
-ATOM   2731  CA  PHE A 324      -1.978 -32.112   1.191  1.00 15.81           C  
-ANISOU 2731  CA  PHE A 324     1829   2599   1581     93    130    280       C  
-ATOM   2732  C   PHE A 324      -2.346 -31.802  -0.260  1.00 18.98           C  
-ANISOU 2732  C   PHE A 324     2203   3083   1927    118    144    305       C  
-ATOM   2733  O   PHE A 324      -1.474 -31.587  -1.091  1.00 16.21           O  
-ANISOU 2733  O   PHE A 324     1852   2730   1578    134    164    315       O  
-ATOM   2734  CB  PHE A 324      -1.002 -33.283   1.274  1.00 16.75           C  
-ANISOU 2734  CB  PHE A 324     1968   2676   1722     58    119    228       C  
-ATOM   2735  CG  PHE A 324      -0.463 -33.499   2.651  1.00 20.78           C  
-ANISOU 2735  CG  PHE A 324     2504   3104   2287     41    108    208       C  
-ATOM   2736  CD1 PHE A 324       0.399 -32.571   3.222  1.00 16.26           C  
-ANISOU 2736  CD1 PHE A 324     1945   2468   1765     61    123    231       C  
-ATOM   2737  CD2 PHE A 324      -0.835 -34.611   3.389  1.00 17.22           C  
-ANISOU 2737  CD2 PHE A 324     2065   2641   1838      5     84    168       C  
-ATOM   2738  CE1 PHE A 324       0.892 -32.759   4.513  1.00 16.20           C  
-ANISOU 2738  CE1 PHE A 324     1961   2390   1805     46    111    211       C  
-ATOM   2739  CE2 PHE A 324      -0.345 -34.809   4.679  1.00 18.85           C  
-ANISOU 2739  CE2 PHE A 324     2295   2775   2091     -8     74    152       C  
-ATOM   2740  CZ  PHE A 324       0.518 -33.880   5.239  1.00 14.78           C  
-ANISOU 2740  CZ  PHE A 324     1792   2201   1621     14     86    173       C  
-ATOM   2741  N   TYR A 325      -3.640 -31.739  -0.563  1.00 17.95           N  
-ANISOU 2741  N   TYR A 325     2046   3027   1746    125    136    319       N  
-ATOM   2742  CA  TYR A 325      -4.043 -31.424  -1.931  1.00 15.72           C  
-ANISOU 2742  CA  TYR A 325     1735   2831   1405    153    147    345       C  
-ATOM   2743  C   TYR A 325      -3.513 -30.063  -2.388  1.00 12.87           C  
-ANISOU 2743  C   TYR A 325     1373   2459   1059    203    184    405       C  
-ATOM   2744  O   TYR A 325      -3.205 -29.881  -3.565  1.00 16.53           O  
-ANISOU 2744  O   TYR A 325     1823   2967   1490    226    201    422       O  
-ATOM   2745  CB  TYR A 325      -5.573 -31.458  -2.087  1.00 14.31           C  
-ANISOU 2745  CB  TYR A 325     1526   2738   1173    155    131    354       C  
-ATOM   2746  CG  TYR A 325      -6.212 -32.828  -2.011  1.00 20.03           C  
-ANISOU 2746  CG  TYR A 325     2244   3497   1871    106     98    296       C  
-ATOM   2747  CD1 TYR A 325      -5.448 -33.994  -2.001  1.00 19.25           C  
-ANISOU 2747  CD1 TYR A 325     2165   3360   1788     65     86    239       C  
-ATOM   2748  CD2 TYR A 325      -7.596 -32.953  -1.962  1.00 22.59           C  
-ANISOU 2748  CD2 TYR A 325     2540   3890   2154    100     81    298       C  
-ATOM   2749  CE1 TYR A 325      -6.046 -35.240  -1.933  1.00 20.90           C  
-ANISOU 2749  CE1 TYR A 325     2369   3596   1976     19     60    186       C  
-ATOM   2750  CE2 TYR A 325      -8.199 -34.184  -1.891  1.00 27.87           C  
-ANISOU 2750  CE2 TYR A 325     3201   4588   2802     52     53    245       C  
-ATOM   2751  CZ  TYR A 325      -7.429 -35.321  -1.881  1.00 26.19           C  
-ANISOU 2751  CZ  TYR A 325     3010   4334   2608     12     44    188       C  
-ATOM   2752  OH  TYR A 325      -8.061 -36.536  -1.807  1.00 27.33           O  
-ANISOU 2752  OH  TYR A 325     3146   4503   2734    -37     19    135       O  
-ATOM   2753  N   THR A 326      -3.391 -29.112  -1.460  1.00 15.82           N  
-ANISOU 2753  N   THR A 326     1759   2771   1481    221    198    436       N  
-ATOM   2754  CA  THR A 326      -2.988 -27.758  -1.836  1.00 16.96           C  
-ANISOU 2754  CA  THR A 326     1901   2899   1642    269    237    495       C  
-ATOM   2755  C   THR A 326      -1.467 -27.636  -2.033  1.00 18.62           C  
-ANISOU 2755  C   THR A 326     2131   3045   1900    268    257    490       C  
-ATOM   2756  O   THR A 326      -0.991 -26.698  -2.669  1.00 21.52           O  
-ANISOU 2756  O   THR A 326     2492   3408   2275    305    292    536       O  
-ATOM   2757  CB  THR A 326      -3.486 -26.697  -0.831  1.00 29.18           C  
-ANISOU 2757  CB  THR A 326     3456   4409   3224    290    248    532       C  
-ATOM   2758  OG1 THR A 326      -3.153 -25.386  -1.308  1.00 35.24           O  
-ANISOU 2758  OG1 THR A 326     4219   5164   4006    338    289    591       O  
-ATOM   2759  CG2 THR A 326      -2.859 -26.906   0.515  1.00 29.96           C  
-ANISOU 2759  CG2 THR A 326     3584   4414   3386    261    236    498       C  
-ATOM   2760  N   VAL A 327      -0.729 -28.608  -1.516  1.00 15.81           N  
-ANISOU 2760  N   VAL A 327     1794   2639   1573    228    237    437       N  
-ATOM   2761  CA  VAL A 327       0.736 -28.637  -1.653  1.00 15.17           C  
-ANISOU 2761  CA  VAL A 327     1730   2498   1538    223    252    426       C  
-ATOM   2762  C   VAL A 327       1.175 -28.987  -3.077  1.00 17.69           C  
-ANISOU 2762  C   VAL A 327     2035   2869   1817    233    266    427       C  
-ATOM   2763  O   VAL A 327       0.740 -29.990  -3.643  1.00 20.21           O  
-ANISOU 2763  O   VAL A 327     2346   3246   2086    214    245    394       O  
-ATOM   2764  CB  VAL A 327       1.344 -29.628  -0.666  1.00 17.41           C  
-ANISOU 2764  CB  VAL A 327     2036   2718   1860    179    226    370       C  
-ATOM   2765  CG1 VAL A 327       2.856 -29.734  -0.874  1.00 19.37           C  
-ANISOU 2765  CG1 VAL A 327     2296   2912   2151    175    241    358       C  
-ATOM   2766  CG2 VAL A 327       1.035 -29.193   0.754  1.00 19.91           C  
-ANISOU 2766  CG2 VAL A 327     2366   2980   2217    174    216    372       C  
-ATOM   2767  N   VAL A 328       2.033 -28.154  -3.662  1.00 15.51           N  
-ANISOU 2767  N   VAL A 328     1758   2572   1563    263    302    465       N  
-ATOM   2768  CA  VAL A 328       2.514 -28.395  -5.019  1.00 20.21           C  
-ANISOU 2768  CA  VAL A 328     2342   3216   2122    278    319    471       C  
-ATOM   2769  C   VAL A 328       3.404 -29.626  -5.074  1.00 24.03           C  
-ANISOU 2769  C   VAL A 328     2840   3675   2617    242    303    413       C  
-ATOM   2770  O   VAL A 328       4.365 -29.737  -4.311  1.00 19.02           O  
-ANISOU 2770  O   VAL A 328     2223   2961   2042    223    302    393       O  
-ATOM   2771  CB  VAL A 328       3.305 -27.190  -5.582  1.00 25.81           C  
-ANISOU 2771  CB  VAL A 328     3047   3900   2860    319    367    528       C  
-ATOM   2772  CG1 VAL A 328       4.060 -27.595  -6.842  1.00 29.17           C  
-ANISOU 2772  CG1 VAL A 328     3465   4360   3257    329    384    526       C  
-ATOM   2773  CG2 VAL A 328       2.381 -26.013  -5.863  1.00 23.63           C  
-ANISOU 2773  CG2 VAL A 328     2754   3665   2560    364    390    591       C  
-ATOM   2774  N   LYS A 329       3.092 -30.536  -5.991  1.00 24.47           N  
-ANISOU 2774  N   LYS A 329     2886   3800   2612    233    290    385       N  
-ATOM   2775  CA  LYS A 329       3.924 -31.719  -6.204  1.00 36.96           C  
-ANISOU 2775  CA  LYS A 329     4481   5363   4199    202    279    332       C  
-ATOM   2776  C   LYS A 329       4.956 -31.494  -7.318  1.00 37.65           C  
-ANISOU 2776  C   LYS A 329     4564   5459   4282    228    313    351       C  
-ATOM   2777  O   LYS A 329       6.148 -31.770  -7.146  1.00 41.50           O  
-ANISOU 2777  O   LYS A 329     5066   5887   4816    217    322    333       O  
-ATOM   2778  CB  LYS A 329       3.054 -32.936  -6.528  1.00 43.00           C  
-ANISOU 2778  CB  LYS A 329     5240   6192   4905    173    248    282       C  
-ATOM   2779  CG  LYS A 329       1.943 -33.186  -5.519  1.00 44.23           C  
-ANISOU 2779  CG  LYS A 329     5397   6349   5060    148    217    265       C  
-ATOM   2780  CD  LYS A 329       2.471 -33.174  -4.088  1.00 41.48           C  
-ANISOU 2780  CD  LYS A 329     5072   5904   4783    128    208    253       C  
-ATOM   2781  CE  LYS A 329       1.384 -33.590  -3.102  1.00 39.67           C  
-ANISOU 2781  CE  LYS A 329     4845   5678   4551    101    178    232       C  
-ATOM   2782  NZ  LYS A 329       0.137 -32.776  -3.236  1.00 36.68           N  
-ANISOU 2782  NZ  LYS A 329     4443   5359   4134    126    179    273       N  
-TER    2783      LYS A 329                                                      
-HETATM 2784  N1  FU9 A 338      23.421 -29.478  10.420  1.00 19.97           N  
-HETATM 2785  C2  FU9 A 338      23.434 -28.488  11.339  1.00 19.82           C  
-HETATM 2786  N3  FU9 A 338      23.310 -28.750  12.649  1.00 16.65           N  
-HETATM 2787  C4  FU9 A 338      23.185 -30.006  13.072  1.00 14.99           C  
-HETATM 2788  C5  FU9 A 338      23.147 -31.045  12.151  1.00 13.79           C  
-HETATM 2789  C6  FU9 A 338      23.287 -30.744  10.797  1.00 17.01           C  
-HETATM 2790  OAA FU9 A 338      22.464 -36.547  15.342  1.00 13.61           O  
-HETATM 2791  OAB FU9 A 338      22.086 -37.214  13.268  1.00 16.32           O  
-HETATM 2792  FAC FU9 A 338      24.116 -31.123  20.289  1.00 37.04           F  
-HETATM 2793  FAD FU9 A 338      22.009 -30.950  20.696  1.00 39.25           F  
-HETATM 2794  FAE FU9 A 338      22.714 -32.258  19.128  1.00 40.80           F  
-HETATM 2795  CAF FU9 A 338      22.594 -27.556  18.409  1.00 18.66           C  
-HETATM 2796  CAG FU9 A 338      22.777 -27.761  17.049  1.00 19.72           C  
-HETATM 2797  CAH FU9 A 338      22.658 -28.643  19.269  1.00 16.31           C  
-HETATM 2798  CAI FU9 A 338      22.800 -34.725  12.202  1.00 10.51           C  
-HETATM 2799  CAJ FU9 A 338      22.968 -33.433  11.721  1.00 13.22           C  
-HETATM 2800  CAL FU9 A 338      22.973 -30.130  17.400  1.00 17.88           C  
-HETATM 2801  CAM FU9 A 338      22.708 -33.870  14.448  1.00 13.89           C  
-HETATM 2802  CAN FU9 A 338      23.500 -24.762  11.531  1.00 23.65           C  
-HETATM 2803  CAO FU9 A 338      24.834 -25.307  12.063  1.00 31.24           C  
-HETATM 2804  NAQ FU9 A 338      22.885 -31.520  14.849  1.00 14.98           N  
-HETATM 2805  NAS FU9 A 338      22.985 -29.154  15.196  1.00 14.12           N  
-HETATM 2806  NAT FU9 A 338      23.580 -27.216  10.980  1.00 21.94           N  
-HETATM 2807  CAU FU9 A 338      22.486 -36.365  14.101  1.00 15.99           C  
-HETATM 2808  CAV FU9 A 338      22.877 -29.044  16.527  1.00 14.02           C  
-HETATM 2809  CAW FU9 A 338      22.708 -34.950  13.574  1.00 15.52           C  
-HETATM 2810  CAX FU9 A 338      22.843 -29.925  18.771  1.00 18.91           C  
-HETATM 2811  CAZ FU9 A 338      23.093 -30.247  14.432  1.00 14.63           C  
-HETATM 2812  CBA FU9 A 338      22.874 -32.568  13.978  1.00 14.78           C  
-HETATM 2813  CBB FU9 A 338      22.996 -32.352  12.609  1.00 12.09           C  
-HETATM 2814  CBE FU9 A 338      23.598 -26.197  12.040  1.00 24.43           C  
-HETATM 2815  CBF FU9 A 338      22.914 -31.103  19.747  1.00 33.36           C  
-HETATM 2816  S   SO4 A 339      16.994 -48.427  23.467  1.00 56.37           S  
-HETATM 2817  O1  SO4 A 339      18.081 -47.592  22.948  1.00 54.07           O  
-HETATM 2818  O2  SO4 A 339      16.573 -49.386  22.452  1.00 44.10           O  
-HETATM 2819  O3  SO4 A 339      17.449 -49.155  24.652  1.00 62.33           O  
-HETATM 2820  O4  SO4 A 339      15.862 -47.573  23.827  1.00 55.64           O  
-HETATM 2821  S   SO4 A 340      12.335 -41.463  29.821  1.00 55.41           S  
-HETATM 2822  O1  SO4 A 340      12.524 -41.505  28.365  1.00 49.11           O  
-HETATM 2823  O2  SO4 A 340      11.605 -42.648  30.264  1.00 51.42           O  
-HETATM 2824  O3  SO4 A 340      13.642 -41.420  30.480  1.00 56.91           O  
-HETATM 2825  O4  SO4 A 340      11.578 -40.268  30.194  1.00 53.41           O  
-HETATM 2826  S   SO4 A 341      -8.673 -44.194  19.555  1.00 20.92           S  
-HETATM 2827  O1  SO4 A 341      -8.890 -44.407  18.118  1.00 26.24           O  
-HETATM 2828  O2  SO4 A 341      -9.987 -44.244  20.203  1.00 24.61           O  
-HETATM 2829  O3  SO4 A 341      -7.781 -45.264  20.045  1.00 17.72           O  
-HETATM 2830  O4  SO4 A 341      -8.117 -42.851  19.768  1.00 12.17           O  
-HETATM 2831  S   SO4 A 342      16.660 -32.532  -1.544  1.00 60.53           S  
-HETATM 2832  O1  SO4 A 342      18.092 -32.240  -1.608  1.00 60.37           O  
-HETATM 2833  O2  SO4 A 342      16.008 -31.860  -2.665  1.00 66.82           O  
-HETATM 2834  O3  SO4 A 342      16.445 -33.972  -1.635  1.00 60.76           O  
-HETATM 2835  O4  SO4 A 342      16.083 -32.057  -0.290  1.00 56.69           O  
-HETATM 2836  C1  PEG A 343      11.944 -32.966  28.991  1.00 56.31           C  
-HETATM 2837  O1  PEG A 343      11.298 -31.707  29.225  1.00 56.67           O  
-HETATM 2838  C2  PEG A 343      11.484 -33.531  27.650  1.00 53.96           C  
-HETATM 2839  O2  PEG A 343      12.178 -34.752  27.413  1.00 55.88           O  
-HETATM 2840  C3  PEG A 343      11.570 -35.803  28.154  1.00 52.84           C  
-HETATM 2841  C4  PEG A 343      12.333 -37.112  28.003  1.00 49.96           C  
-HETATM 2842  O4  PEG A 343      11.995 -37.950  29.120  1.00 53.07           O  
-HETATM 2843  C1  EDO A 344      36.720 -34.839  14.137  1.00 36.42           C  
-HETATM 2844  O1  EDO A 344      37.874 -34.042  13.843  1.00 41.78           O  
-HETATM 2845  C2  EDO A 344      37.172 -36.201  14.636  1.00 35.03           C  
-HETATM 2846  O2  EDO A 344      38.187 -36.015  15.626  1.00 42.78           O  
-HETATM 2847  C1  EDO A 345      19.415 -27.579  15.641  1.00 36.05           C  
-HETATM 2848  O1  EDO A 345      18.612 -26.416  15.884  1.00 36.30           O  
-HETATM 2849  C2  EDO A 345      18.554 -28.838  15.673  1.00 30.48           C  
-HETATM 2850  O2  EDO A 345      17.199 -28.530  15.316  1.00 26.54           O  
-HETATM 2851  C1  EDO A 346      46.096 -32.820   6.362  1.00 34.89           C  
-HETATM 2852  O1  EDO A 346      45.187 -33.876   6.713  1.00 41.33           O  
-HETATM 2853  C2  EDO A 346      46.688 -33.074   4.975  1.00 39.51           C  
-HETATM 2854  O2  EDO A 346      47.830 -33.946   5.050  1.00 29.68           O  
-HETATM 2855  C1  EDO A 347      -3.512 -28.782  24.927  1.00 31.45           C  
-HETATM 2856  O1  EDO A 347      -4.315 -28.235  25.980  1.00 34.75           O  
-HETATM 2857  C2  EDO A 347      -3.161 -30.226  25.258  1.00 23.02           C  
-HETATM 2858  O2  EDO A 347      -2.455 -30.258  26.501  1.00 28.27           O  
-HETATM 2859  C1  EDO A 348      13.925 -26.745  12.537  1.00 30.67           C  
-HETATM 2860  O1  EDO A 348      15.064 -26.455  11.710  1.00 27.06           O  
-HETATM 2861  C2  EDO A 348      14.326 -27.670  13.686  1.00 28.04           C  
-HETATM 2862  O2  EDO A 348      15.184 -26.970  14.593  1.00 34.93           O  
-HETATM 2863  C1  EDO A 349      13.940 -31.689  22.311  1.00 39.56           C  
-HETATM 2864  O1  EDO A 349      14.512 -30.521  21.707  1.00 45.99           O  
-HETATM 2865  C2  EDO A 349      13.327 -31.365  23.668  1.00 44.54           C  
-HETATM 2866  O2  EDO A 349      12.614 -32.504  24.166  1.00 44.84           O  
-HETATM 2867  C1  EDO A 350      10.835 -28.583  23.200  1.00 32.95           C  
-HETATM 2868  O1  EDO A 350       9.779 -27.664  23.502  1.00 33.08           O  
-HETATM 2869  C2  EDO A 350      10.240 -29.859  22.616  1.00 31.46           C  
-HETATM 2870  O2  EDO A 350       9.881 -29.645  21.243  1.00 32.80           O  
-HETATM 2871  C1  EDO A 351      20.986 -23.426  13.465  1.00 52.38           C  
-HETATM 2872  O1  EDO A 351      20.721 -22.062  13.812  1.00 57.95           O  
-HETATM 2873  C2  EDO A 351      20.228 -24.368  14.395  1.00 49.78           C  
-HETATM 2874  O2  EDO A 351      20.793 -24.356  15.712  1.00 46.66           O  
-HETATM 2875  C1  EDO A 352     -13.220 -35.583  18.281  1.00 37.90           C  
-HETATM 2876  O1  EDO A 352     -13.664 -35.017  17.031  1.00 39.89           O  
-HETATM 2877  C2  EDO A 352     -11.932 -36.382  18.091  1.00 40.36           C  
-HETATM 2878  O2  EDO A 352     -12.190 -37.673  17.506  1.00 34.29           O  
-HETATM 2879  O   HOH A 353       8.987 -40.871  17.285  1.00 11.54           O  
-HETATM 2880  O   HOH A 354      19.887 -46.447  16.454  1.00 14.49           O  
-HETATM 2881  O   HOH A 355       2.911 -32.739  22.505  1.00 12.91           O  
-HETATM 2882  O   HOH A 356      17.796 -55.912  14.153  1.00 18.39           O  
-HETATM 2883  O   HOH A 357       3.501 -48.348  17.810  1.00 12.78           O  
-HETATM 2884  O   HOH A 358       4.072 -45.639   8.010  1.00 15.13           O  
-HETATM 2885  O   HOH A 359       5.129 -56.420  16.508  1.00 14.96           O  
-HETATM 2886  O   HOH A 360       2.642 -49.571  11.395  1.00 16.54           O  
-HETATM 2887  O   HOH A 361       6.648 -54.967  18.038  1.00 14.45           O  
-HETATM 2888  O   HOH A 362       2.678 -37.208  23.829  1.00 13.76           O  
-HETATM 2889  O   HOH A 363     -12.542 -41.011  25.190  1.00 13.06           O  
-HETATM 2890  O   HOH A 364       3.806 -30.836  20.403  1.00 14.14           O  
-HETATM 2891  O   HOH A 365       3.656 -45.923   5.361  1.00 14.29           O  
-HETATM 2892  O   HOH A 366      22.685 -41.517   5.775  1.00 15.45           O  
-HETATM 2893  O   HOH A 367      10.733 -37.427  20.575  1.00 19.09           O  
-HETATM 2894  O   HOH A 368       2.780 -53.781  16.835  1.00 14.74           O  
-HETATM 2895  O   HOH A 369      14.426 -50.921  22.150  1.00 20.60           O  
-HETATM 2896  O   HOH A 370      21.855 -39.865  13.360  1.00 13.76           O  
-HETATM 2897  O   HOH A 371      42.009 -38.747  25.405  1.00 17.57           O  
-HETATM 2898  O   HOH A 372      -4.465 -31.544  28.119  1.00 19.13           O  
-HETATM 2899  O   HOH A 373       4.265 -54.914  26.848  1.00 23.39           O  
-HETATM 2900  O   HOH A 374      17.533 -39.711  18.780  1.00 16.97           O  
-HETATM 2901  O   HOH A 375       0.699 -45.713  11.723  1.00 17.36           O  
-HETATM 2902  O   HOH A 376       2.793 -46.915  10.393  1.00 16.79           O  
-HETATM 2903  O   HOH A 377     -14.155 -40.349  27.563  1.00 15.62           O  
-HETATM 2904  O   HOH A 378      20.975 -39.402   2.890  1.00 21.54           O  
-HETATM 2905  O   HOH A 379       9.134 -41.397   0.598  1.00 19.48           O  
-HETATM 2906  O   HOH A 380      -4.935 -25.756   7.552  1.00 18.32           O  
-HETATM 2907  O   HOH A 381      21.984 -35.285  17.697  1.00 18.29           O  
-HETATM 2908  O   HOH A 382       0.274 -51.267  14.343  1.00 18.60           O  
-HETATM 2909  O   HOH A 383      -1.149 -47.631  12.399  1.00 21.52           O  
-HETATM 2910  O   HOH A 384       0.018 -50.293  11.987  1.00 20.34           O  
-HETATM 2911  O   HOH A 385      39.348 -42.611  11.751  1.00 16.81           O  
-HETATM 2912  O   HOH A 386      -7.995 -37.924  17.848  1.00 14.71           O  
-HETATM 2913  O   HOH A 387      37.834 -39.677   5.231  1.00 20.11           O  
-HETATM 2914  O   HOH A 388      -6.813 -42.787  11.904  1.00 13.63           O  
-HETATM 2915  O   HOH A 389      11.369 -28.600  13.194  1.00 21.39           O  
-HETATM 2916  O   HOH A 390      -3.234 -56.930  17.914  1.00 24.53           O  
-HETATM 2917  O   HOH A 391      -1.347 -35.492  36.694  1.00 18.42           O  
-HETATM 2918  O   HOH A 392       1.543 -47.653   4.618  1.00 22.24           O  
-HETATM 2919  O   HOH A 393      22.234 -57.364  15.694  1.00 32.79           O  
-HETATM 2920  O   HOH A 394      16.303 -42.005  16.506  1.00 16.12           O  
-HETATM 2921  O   HOH A 395      14.367 -37.035  22.773  1.00 24.20           O  
-HETATM 2922  O   HOH A 396       5.423 -24.868  -3.326  1.00 20.38           O  
-HETATM 2923  O   HOH A 397      -9.125 -46.712  21.995  1.00 19.61           O  
-HETATM 2924  O   HOH A 398      -1.139 -18.620   6.435  1.00 21.33           O  
-HETATM 2925  O   HOH A 399     -11.422 -52.354  23.775  1.00 22.96           O  
-HETATM 2926  O   HOH A 400      -7.604 -26.782   3.277  1.00 21.94           O  
-HETATM 2927  O   HOH A 401     -13.582 -42.892  31.940  1.00 19.54           O  
-HETATM 2928  O   HOH A 402      21.093 -26.219   3.957  1.00 23.45           O  
-HETATM 2929  O   HOH A 403      43.640 -41.818  21.066  1.00 21.26           O  
-HETATM 2930  O   HOH A 404       6.222 -31.065   0.101  1.00 21.88           O  
-HETATM 2931  O   HOH A 405       5.926 -29.808  19.127  1.00 25.17           O  
-HETATM 2932  O   HOH A 406      10.860 -50.969  28.444  1.00 23.36           O  
-HETATM 2933  O   HOH A 407      23.244 -54.092   4.147  1.00 23.70           O  
-HETATM 2934  O   HOH A 408      26.114 -50.905   5.506  1.00 23.66           O  
-HETATM 2935  O   HOH A 409      -2.706 -21.923  21.212  1.00 21.27           O  
-HETATM 2936  O   HOH A 410       0.774 -42.278  -0.412  1.00 29.93           O  
-HETATM 2937  O   HOH A 411      23.379 -41.136  19.237  1.00 27.98           O  
-HETATM 2938  O   HOH A 412     -10.318 -16.170  19.802  1.00 21.17           O  
-HETATM 2939  O   HOH A 413      -7.632 -14.724  21.421  1.00 24.65           O  
-HETATM 2940  O   HOH A 414     -15.121 -30.129  22.991  1.00 31.12           O  
-HETATM 2941  O   HOH A 415       5.720 -44.137  32.363  1.00 32.89           O  
-HETATM 2942  O   HOH A 416      -1.666 -25.760   8.506  1.00 20.16           O  
-HETATM 2943  O   HOH A 417      17.143 -26.886  19.125  1.00 29.81           O  
-HETATM 2944  O   HOH A 418      -4.114 -29.928  30.383  1.00 26.31           O  
-HETATM 2945  O   HOH A 419       4.413 -46.642  34.675  1.00 32.14           O  
-HETATM 2946  O   HOH A 420      10.164 -56.549   9.469  1.00 21.53           O  
-HETATM 2947  O   HOH A 421      41.959 -41.303  14.987  1.00 24.00           O  
-HETATM 2948  O   HOH A 422      -5.506 -28.983   0.729  1.00 24.63           O  
-HETATM 2949  O   HOH A 423      -4.991 -46.372   9.146  1.00 30.81           O  
-HETATM 2950  O   HOH A 424      27.660 -30.729   4.215  1.00 29.30           O  
-HETATM 2951  O   HOH A 425     -21.404 -41.199  36.611  1.00 27.34           O  
-HETATM 2952  O   HOH A 426      -2.740 -35.777  -0.544  1.00 20.22           O  
-HETATM 2953  O   HOH A 427      -8.719 -49.412  21.249  1.00 29.92           O  
-HETATM 2954  O   HOH A 428      16.577 -35.947   0.068  1.00 21.27           O  
-HETATM 2955  O   HOH A 429       3.162 -42.870  31.959  1.00 22.42           O  
-HETATM 2956  O   HOH A 430      -8.147 -43.271   9.276  1.00 29.09           O  
-HETATM 2957  O   HOH A 431      31.321 -36.279  22.820  1.00 34.85           O  
-HETATM 2958  O   HOH A 432      23.663 -61.490   5.037  1.00 37.50           O  
-HETATM 2959  O   HOH A 433       9.789 -37.458  31.225  1.00 36.24           O  
-HETATM 2960  O   HOH A 434       2.995 -25.731  25.757  1.00 31.26           O  
-HETATM 2961  O   HOH A 435      -7.586 -40.501   5.760  1.00 22.37           O  
-HETATM 2962  O   HOH A 436     -13.460 -28.763   3.650  1.00 41.17           O  
-HETATM 2963  O   HOH A 437     -14.286 -47.573  28.134  1.00 28.78           O  
-HETATM 2964  O   HOH A 438       8.992 -23.871  21.291  1.00 31.83           O  
-HETATM 2965  O   HOH A 439     -11.063 -51.070  21.222  1.00 32.01           O  
-HETATM 2966  O   HOH A 440      40.192 -26.924  14.795  1.00 25.66           O  
-HETATM 2967  O   HOH A 441       8.846 -52.049  29.945  1.00 35.68           O  
-HETATM 2968  O   HOH A 442      -9.323 -46.912  17.430  1.00 22.12           O  
-HETATM 2969  O   HOH A 443      24.442 -44.374  18.580  1.00 28.11           O  
-HETATM 2970  O   HOH A 444      -4.785 -23.809  21.307  1.00 23.80           O  
-HETATM 2971  O   HOH A 445       0.403 -42.968  -3.612  1.00 25.15           O  
-HETATM 2972  O   HOH A 446      -7.421 -35.680  36.038  1.00 23.99           O  
-HETATM 2973  O   HOH A 447      30.472 -48.622   8.290  1.00 27.71           O  
-HETATM 2974  O   HOH A 448      24.588 -23.891  18.696  1.00 39.99           O  
-HETATM 2975  O   HOH A 449      -4.227 -19.079   5.923  1.00 25.82           O  
-HETATM 2976  O   HOH A 450     -16.376 -33.756  16.087  1.00 26.91           O  
-HETATM 2977  O   HOH A 451      -5.542 -40.836   3.692  1.00 26.34           O  
-HETATM 2978  O   HOH A 452     -13.062 -33.825  34.162  1.00 25.66           O  
-HETATM 2979  O   HOH A 453       2.877 -40.653  -2.024  1.00 36.34           O  
-HETATM 2980  O   HOH A 454       8.408 -43.660  28.127  1.00 26.95           O  
-HETATM 2981  O   HOH A 455      23.336 -24.450  16.087  1.00 23.85           O  
-HETATM 2982  O   HOH A 456      -6.877 -38.794  -1.320  1.00 29.85           O  
-HETATM 2983  O   HOH A 457       6.574 -42.217   0.161  1.00 32.59           O  
-HETATM 2984  O   HOH A 458       4.250 -56.808  24.850  1.00 29.79           O  
-HETATM 2985  O   HOH A 459      18.670 -36.527   1.628  1.00 41.68           O  
-HETATM 2986  O   HOH A 460       2.731 -37.384  38.612  1.00 40.20           O  
-HETATM 2987  O   HOH A 461      -8.272 -42.805   6.840  1.00 21.73           O  
-HETATM 2988  O   HOH A 462      29.512 -44.707   6.245  1.00 30.57           O  
-HETATM 2989  O   HOH A 463      13.783 -31.554   1.480  1.00 26.91           O  
-HETATM 2990  O   HOH A 464      19.473 -40.454  20.444  1.00 32.00           O  
-HETATM 2991  O   HOH A 465     -12.156 -44.554  18.915  1.00 26.17           O  
-HETATM 2992  O   HOH A 466      33.404 -34.346  22.535  1.00 40.28           O  
-HETATM 2993  O   HOH A 467      24.614 -42.885  20.996  1.00 27.93           O  
-HETATM 2994  O   HOH A 468       0.554 -47.234  33.162  1.00 31.37           O  
-HETATM 2995  O   HOH A 469      -9.790 -34.492  20.818  1.00 32.61           O  
-HETATM 2996  O   HOH A 470       2.873 -47.067  32.777  1.00 36.55           O  
-HETATM 2997  O   HOH A 471      -5.167 -15.793  12.654  1.00 33.66           O  
-HETATM 2998  O   HOH A 472      22.380 -51.519   3.454  1.00 30.05           O  
-HETATM 2999  O   HOH A 473      -4.059 -51.031  37.829  1.00 36.69           O  
-HETATM 3000  O   HOH A 474      -4.934 -46.758  37.318  1.00 29.20           O  
-HETATM 3001  O   HOH A 475      -3.943 -35.056  37.565  1.00 26.44           O  
-HETATM 3002  O   HOH A 476      42.444 -43.224  16.922  1.00 30.61           O  
-HETATM 3003  O   HOH A 477      -1.280 -39.304  -3.392  1.00 28.50           O  
-HETATM 3004  O   HOH A 478     -13.624 -53.509  28.381  1.00 31.89           O  
-HETATM 3005  O   HOH A 479      36.688 -36.539   3.451  1.00 40.64           O  
-HETATM 3006  O   HOH A 480     -11.940 -46.797  21.061  1.00 26.59           O  
-HETATM 3007  O   HOH A 481      39.690 -30.436  14.892  1.00 22.81           O  
-HETATM 3008  O   HOH A 482     -12.156 -35.922  36.712  1.00 31.35           O  
-HETATM 3009  O   HOH A 483      11.129 -59.699  22.041  1.00 28.91           O  
-HETATM 3010  O   HOH A 484     -12.156 -36.058  12.025  1.00 31.53           O  
-HETATM 3011  O   HOH A 485       0.691 -35.685  38.432  1.00 29.26           O  
-HETATM 3012  O   HOH A 486     -15.249 -28.824  25.276  1.00 33.35           O  
-HETATM 3013  O   HOH A 487     -17.117 -32.681  26.885  1.00 29.66           O  
-HETATM 3014  O   HOH A 488      16.588 -54.905  16.453  1.00 26.49           O  
-HETATM 3015  O   HOH A 489      25.439 -56.069   9.491  1.00 29.14           O  
-HETATM 3016  O   HOH A 490      45.408 -39.758   7.676  1.00 36.57           O  
-HETATM 3017  O   HOH A 491      31.016 -52.455   6.147  1.00 49.61           O  
-HETATM 3018  O   HOH A 492     -11.225 -39.951  12.195  1.00 30.54           O  
-HETATM 3019  O   HOH A 493      -8.669 -30.348  26.891  1.00 32.98           O  
-HETATM 3020  O   HOH A 494      -8.812 -56.960  28.616  1.00 38.66           O  
-HETATM 3021  O   HOH A 495       5.944 -56.460  28.158  1.00 42.20           O  
-HETATM 3022  O   HOH A 496      -6.596 -51.753   8.705  1.00 41.18           O  
-HETATM 3023  O   HOH A 497     -11.037 -26.208   3.618  1.00 44.65           O  
-HETATM 3024  O   HOH A 498      -3.234 -43.681  42.897  1.00 42.07           O  
-HETATM 3025  O   HOH A 499      42.432 -41.227  10.656  1.00 32.84           O  
-HETATM 3026  O   HOH A 500      31.718 -33.575   2.882  1.00 31.86           O  
-HETATM 3027  O   HOH A 501      -9.625 -34.728  37.096  1.00 31.70           O  
-HETATM 3028  O   HOH A 502       9.199 -52.110   1.314  1.00 40.53           O  
-HETATM 3029  O   HOH A 503      20.046 -49.891   1.955  1.00 31.41           O  
-HETATM 3030  O   HOH A 504      41.837 -42.981  12.600  1.00 27.78           O  
-HETATM 3031  O   HOH A 505      -7.323 -50.590  14.907  1.00 28.55           O  
-HETATM 3032  O   HOH A 506      -7.186 -53.302  30.877  1.00 26.87           O  
-HETATM 3033  O   HOH A 507       9.388 -39.697  -1.489  1.00 30.55           O  
-HETATM 3034  O   HOH A 508     -13.871 -42.218  18.577  1.00 29.56           O  
-HETATM 3035  O   HOH A 509      -1.937 -55.736  13.465  1.00 31.56           O  
-HETATM 3036  O   HOH A 510     -12.295 -43.120  34.267  1.00 42.79           O  
-HETATM 3037  O   HOH A 511      15.669 -52.821  21.172  1.00 28.09           O  
-HETATM 3038  O   HOH A 512      -3.645 -30.545  32.931  1.00 29.39           O  
-HETATM 3039  O   HOH A 513      10.723 -61.471  14.569  1.00 35.50           O  
-HETATM 3040  O   HOH A 514      43.133 -41.011  23.974  1.00 24.97           O  
-HETATM 3041  O   HOH A 515      12.327 -58.376  -0.032  1.00 33.37           O  
-HETATM 3042  O   HOH A 516      13.442 -35.011  -1.078  1.00 51.72           O  
-HETATM 3043  O   HOH A 517     -11.705 -27.740   1.000  1.00 36.49           O  
-HETATM 3044  O   HOH A 518      -5.860 -42.693  -1.803  1.00 34.88           O  
-HETATM 3045  O   HOH A 519      17.950 -53.316  22.670  1.00 34.24           O  
-HETATM 3046  O   HOH A 520      19.622 -57.566  15.677  1.00 37.57           O  
-HETATM 3047  O   HOH A 521      -8.882 -41.271  44.550  1.00 47.56           O  
-HETATM 3048  O   HOH A 522     -13.228 -50.239  28.060  1.00 33.31           O  
-HETATM 3049  O   HOH A 523       0.028 -51.910  36.102  1.00 34.92           O  
-HETATM 3050  O   HOH A 524      -1.579 -21.597  23.731  1.00 34.19           O  
-HETATM 3051  O   HOH A 525      11.834 -60.657  -0.713  1.00 33.81           O  
-HETATM 3052  O   HOH A 526      22.340 -29.992   3.535  1.00 33.35           O  
-HETATM 3053  O   HOH A 527      -6.869 -48.041   6.855  1.00 44.06           O  
-HETATM 3054  O   HOH A 528      25.428 -25.634   4.585  1.00 36.24           O  
-HETATM 3055  O   HOH A 529       5.592 -46.281  30.843  1.00 37.42           O  
-HETATM 3056  O   HOH A 530      34.118 -44.081   5.974  1.00 42.31           O  
-HETATM 3057  O   HOH A 531      -9.727 -36.677  19.920  1.00 29.57           O  
-HETATM 3058  O   HOH A 532      41.958 -44.391  20.994  1.00 32.80           O  
-HETATM 3059  O   HOH A 533      29.946 -25.609   2.803  1.00 31.26           O  
-HETATM 3060  O   HOH A 534     -16.297 -31.170  13.532  1.00 36.73           O  
-HETATM 3061  O   HOH A 535      20.135 -21.628   3.369  1.00 36.24           O  
-HETATM 3062  O   HOH A 536      -5.726 -12.160  15.693  1.00 35.86           O  
-HETATM 3063  O   HOH A 537      15.438 -64.473   6.272  1.00 47.94           O  
-HETATM 3064  O   HOH A 538      25.336 -60.721  15.449  1.00 44.65           O  
-HETATM 3065  O   HOH A 539      36.246 -51.381  12.114  1.00 43.19           O  
-HETATM 3066  O   HOH A 540     -10.406 -12.657  12.914  1.00 44.14           O  
-HETATM 3067  O   HOH A 541      -4.024 -57.459  32.035  1.00 29.96           O  
-HETATM 3068  O   HOH A 542      -9.628 -39.050   4.423  1.00 40.58           O  
-HETATM 3069  O   HOH A 543     -11.825 -18.407  15.845  1.00 43.15           O  
-HETATM 3070  O   HOH A 544      29.965 -49.690   5.661  1.00 36.88           O  
-HETATM 3071  O   HOH A 545       1.589 -17.726  10.004  1.00 34.66           O  
-HETATM 3072  O   HOH A 546      24.998 -45.095   0.252  1.00 45.15           O  
-HETATM 3073  O   HOH A 547      40.331 -25.921   4.480  1.00 43.50           O  
-HETATM 3074  O   HOH A 548      -9.017 -49.318  18.607  1.00 42.10           O  
-HETATM 3075  O   HOH A 549     -17.098 -27.192  24.175  1.00 24.07           O  
-HETATM 3076  O   HOH A 550     -11.582 -32.895  30.824  1.00 37.29           O  
-HETATM 3077  O   HOH A 551     -13.016 -49.345  20.451  1.00 33.16           O  
-HETATM 3078  O   HOH A 552      14.318 -55.182  21.070  1.00 30.29           O  
-HETATM 3079  O   HOH A 553      -2.595 -32.555  34.139  1.00 32.88           O  
-HETATM 3080  O   HOH A 554      11.397 -33.436  -1.627  1.00 36.25           O  
-HETATM 3081  O   HOH A 555      18.931 -45.870   1.296  1.00 29.31           O  
-HETATM 3082  O   HOH A 556      -8.316 -12.231  22.397  1.00 34.91           O  
-HETATM 3083  O   HOH A 557       4.166 -56.597   4.985  1.00 33.50           O  
-HETATM 3084  O   HOH A 558       0.796 -49.582  32.362  1.00 41.85           O  
-HETATM 3085  O   HOH A 559     -11.599 -18.937  20.443  1.00 44.26           O  
-HETATM 3086  O   HOH A 560       1.785 -52.390  30.681  1.00 27.95           O  
-HETATM 3087  O   HOH A 561       4.156 -23.647  16.847  1.00 36.00           O  
-HETATM 3088  O   HOH A 562      18.500 -51.548   0.573  1.00 33.29           O  
-HETATM 3089  O   HOH A 563     -14.599 -49.080  30.299  1.00 37.03           O  
-HETATM 3090  O   HOH A 564      33.863 -30.493  24.531  1.00 34.27           O  
-HETATM 3091  O   HOH A 565      19.680 -40.421  -3.506  1.00 41.55           O  
-HETATM 3092  O   HOH A 566      -7.157 -47.993  35.960  1.00 30.89           O  
-HETATM 3093  O   HOH A 567      -5.034 -24.078  23.853  1.00 41.10           O  
-HETATM 3094  O   HOH A 568      29.486 -55.523   7.750  1.00 38.26           O  
-HETATM 3095  O   HOH A 569      -7.865 -50.118  38.360  1.00 46.08           O  
-HETATM 3096  O   HOH A 570      25.449 -60.897   9.766  1.00 50.64           O  
-HETATM 3097  O   HOH A 571       5.339 -41.809  -1.955  1.00 41.56           O  
-HETATM 3098  O   HOH A 572      10.026 -51.195  32.720  1.00 36.14           O  
-HETATM 3099  O   HOH A 573      -3.816 -27.684  28.935  1.00 48.98           O  
-HETATM 3100  O   HOH A 574      -3.764 -62.391  26.213  1.00 54.21           O  
-HETATM 3101  O   HOH A 575      18.609 -20.792  13.803  1.00 29.57           O  
-HETATM 3102  O   HOH A 576      -5.911 -50.429  39.984  1.00 31.27           O  
-HETATM 3103  O   HOH A 577      10.886 -54.346   1.006  1.00 27.43           O  
-HETATM 3104  O   HOH A 578       7.886 -43.712  33.472  1.00 40.79           O  
-HETATM 3105  O   HOH A 579      21.565 -56.109   3.123  1.00 31.07           O  
-HETATM 3106  O   HOH A 580      26.921 -54.949   7.785  1.00 38.95           O  
-HETATM 3107  O   HOH A 581       5.219 -37.752  -3.409  1.00 31.63           O  
-HETATM 3108  O   HOH A 582      23.543 -26.288   2.871  1.00 38.05           O  
-HETATM 3109  O   HOH A 583      -3.752 -37.691  -3.065  1.00 35.09           O  
-HETATM 3110  O   HOH A 584      33.644 -52.199  13.564  1.00 32.43           O  
-HETATM 3111  O   HOH A 585      12.975 -52.583  28.329  1.00 38.29           O  
-HETATM 3112  O   HOH A 586      -7.329 -46.771   9.945  1.00 38.33           O  
-HETATM 3113  O   HOH A 587      15.709 -24.026  20.958  1.00 37.85           O  
-HETATM 3114  O   HOH A 588      -6.695 -29.987  28.212  1.00 41.24           O  
-HETATM 3115  O   HOH A 589       2.114 -60.305  23.873  1.00 41.47           O  
-HETATM 3116  O   HOH A 590     -12.107 -36.412  39.559  1.00 33.57           O  
-HETATM 3117  O   HOH A 591       0.659 -37.607  -2.181  1.00 38.27           O  
-HETATM 3118  O   HOH A 592      -7.474 -11.257  19.867  1.00 38.67           O  
-HETATM 3119  O   HOH A 593      -0.958 -57.855  30.505  1.00 37.24           O  
-HETATM 3120  O   HOH A 594       8.309 -39.434  34.616  1.00 28.39           O  
-HETATM 3121  O   HOH A 595       7.165 -48.266  31.823  1.00 40.15           O  
-HETATM 3122  O   HOH A 596       9.210 -44.839  30.298  1.00 42.43           O  
-HETATM 3123  O   HOH A 597      38.333 -41.802   3.751  1.00 44.38           O  
-HETATM 3124  O   HOH A 598      11.855 -49.430  30.513  1.00 44.09           O  
-HETATM 3125  O   HOH A 599     -13.199 -49.022  17.846  1.00 43.38           O  
-HETATM 3126  O   HOH A 600     -12.130 -33.036  13.150  1.00 41.24           O  
-HETATM 3127  O   HOH A 601       2.030 -54.408  28.689  1.00 33.15           O  
-HETATM 3128  O   HOH A 602      12.591 -52.701   2.190  1.00 31.39           O  
-HETATM 3129  O   HOH A 603     -22.838 -42.228  38.659  1.00 41.52           O  
-HETATM 3130  O   HOH A 604      43.553 -46.577  21.223  1.00 39.70           O  
-HETATM 3131  O   HOH A 605      21.818 -33.439   0.661  1.00 34.62           O  
-HETATM 3132  O   HOH A 606       6.823 -39.637  -2.417  1.00 38.12           O  
-HETATM 3133  O   HOH A 607      -2.702 -45.750  44.276  1.00 48.77           O  
-HETATM 3134  O   HOH A 608     -11.272 -31.729   1.446  1.00 39.82           O  
-HETATM 3135  O   HOH A 609      32.326 -24.884   9.038  1.00 38.28           O  
-HETATM 3136  O   HOH A 610      35.295 -25.089  -1.615  1.00 49.23           O  
-HETATM 3137  O   HOH A 611       7.698 -50.635  34.147  1.00 44.01           O  
-HETATM 3138  O   HOH A 612       9.908 -34.472  35.583  1.00 42.93           O  
-HETATM 3139  O   HOH A 613      37.928 -49.254   7.995  1.00 33.32           O  
-HETATM 3140  O   HOH A 614      23.152 -26.273  22.215  1.00 41.20           O  
-HETATM 3141  O   HOH A 615      41.285 -28.672  16.660  1.00 35.58           O  
-HETATM 3142  O   HOH A 616      20.942 -32.581  17.029  1.00 26.57           O  
-HETATM 3143  O   HOH A 617      22.035 -38.838  19.645  1.00 32.26           O  
-HETATM 3144  O   HOH A 618      12.202 -30.676  19.997  1.00 14.82           O  
-HETATM 3145  O   HOH A 619      14.373 -33.985  25.464  1.00 38.59           O  
-HETATM 3146  O   HOH A 620      43.061 -34.427   4.985  1.00 35.88           O  
-HETATM 3147  O   HOH A 621      -0.776 -29.421  28.143  1.00 20.64           O  
-HETATM 3148  O   HOH A 622       3.095 -22.818  13.914  1.00 27.75           O  
-HETATM 3149  O   HOH A 623       9.209 -20.408  16.731  1.00 38.23           O  
-HETATM 3150  O   HOH A 624       3.905 -62.107  18.929  1.00 27.78           O  
-HETATM 3151  O   HOH A 625      -0.182 -59.831  16.492  1.00 25.49           O  
-HETATM 3152  O   HOH A 626      19.234 -38.595   0.745  1.00 35.60           O  
-HETATM 3153  O   HOH A 627       9.452 -30.821  34.123  1.00 45.46           O  
-HETATM 3154  O   HOH A 628     -12.153 -25.558   0.203  1.00 36.58           O  
-HETATM 3155  O   HOH A 629      12.513 -56.905   2.268  1.00 32.28           O  
-HETATM 3156  O   HOH A 630      12.552 -43.701  -2.672  1.00 39.41           O  
-HETATM 3157  O   HOH A 631      24.894 -50.854   2.690  1.00 47.58           O  
-HETATM 3158  O   HOH A 632      16.843 -21.855   7.294  1.00 31.74           O  
-HETATM 3159  O   HOH A 633       6.043 -30.978  -2.727  1.00 40.43           O  
-HETATM 3160  O   HOH A 634      44.817 -28.772  11.400  1.00 34.20           O  
-HETATM 3161  O   HOH A 635      23.360 -38.250  -0.120  1.00 35.95           O  
-HETATM 3162  O   HOH A 636      23.070 -35.013  20.269  1.00 37.93           O  
-HETATM 3163  O   HOH A 637      -1.905 -57.581  15.499  1.00 37.08           O  
-HETATM 3164  O   HOH A 638      -7.143 -62.724  28.374  1.00 43.76           O  
-HETATM 3165  O   HOH A 639      -6.909 -22.965   3.883  1.00 36.99           O  
-HETATM 3166  O   HOH A 640      35.774 -34.414  23.348  1.00 45.32           O  
-HETATM 3167  O   HOH A 641     -12.621 -31.610  10.278  1.00 33.08           O  
-HETATM 3168  O   HOH A 642     -13.569 -36.962  14.949  1.00 39.45           O  
-HETATM 3169  O   HOH A 643      40.843 -44.553  18.615  1.00 34.61           O  
-HETATM 3170  O   HOH A 644      15.373 -14.592  15.843  1.00 43.78           O  
-HETATM 3171  O   HOH A 645      -6.338 -22.228   6.340  1.00 37.51           O  
-HETATM 3172  O   HOH A 646      -8.097 -20.886   7.364  1.00 46.49           O  
-HETATM 3173  O   HOH A 647      -1.390 -14.623  14.431  1.00 40.72           O  
-HETATM 3174  O   HOH A 648      12.668 -60.723  16.841  1.00 38.81           O  
-HETATM 3175  O   HOH A 649      19.780 -34.799  -1.808  1.00 38.64           O  
-HETATM 3176  O   HOH A 650       4.401 -40.543  40.978  1.00 43.07           O  
-HETATM 3177  O   HOH A 651       9.323 -46.983  31.784  1.00 53.17           O  
-HETATM 3178  O   HOH A 652     -17.525 -43.561  33.887  1.00 35.48           O  
-HETATM 3179  O   HOH A 653      25.803 -54.363   3.372  1.00 35.60           O  
-HETATM 3180  O   HOH A 654      42.827 -26.398   5.086  1.00 36.77           O  
-HETATM 3181  O   HOH A 655      15.340 -43.345  -2.787  1.00 43.07           O  
-HETATM 3182  O   HOH A 656      42.969 -31.562  10.198  1.00 36.97           O  
-HETATM 3183  O   HOH A 657      33.204 -51.226  16.085  1.00 54.54           O  
-HETATM 3184  O   HOH A 658      -5.037 -26.627  34.398  1.00 49.78           O  
-HETATM 3185  O   HOH A 659      -1.910 -34.521  -2.811  1.00 41.69           O  
-HETATM 3186  O   HOH A 660      32.752 -37.926  24.216  1.00 43.13           O  
-HETATM 3187  O   HOH A 661      17.955 -18.788  10.146  1.00 40.71           O  
-HETATM 3188  O   HOH A 662      41.125 -44.687   9.088  1.00 40.62           O  
-HETATM 3189  O   HOH A 663      14.143 -18.449   8.697  1.00 44.61           O  
-HETATM 3190  O   HOH A 664      32.632 -23.638   3.736  1.00 42.30           O  
-HETATM 3191  O   HOH A 665      43.601 -34.187  12.677  1.00 38.07           O  
-HETATM 3192  O   HOH A 666      44.029 -39.282  13.971  1.00 36.52           O  
-HETATM 3193  O   HOH A 667       4.442 -61.705   9.312  1.00 43.23           O  
-HETATM 3194  O   HOH A 668      -6.223 -27.476  27.565  1.00 57.32           O  
-HETATM 3195  O   HOH A 669      25.591 -23.039   3.959  1.00 49.88           O  
-HETATM 3196  O   HOH A 670      10.349 -47.112  -0.137  1.00 39.41           O  
-HETATM 3197  O   HOH A 671      16.192 -62.081   7.266  1.00 49.49           O  
-HETATM 3198  O   HOH A 672      11.988 -17.990  10.583  1.00 43.35           O  
-HETATM 3199  O   HOH A 673      33.949 -53.866  15.617  1.00 53.72           O  
-HETATM 3200  O   HOH A 674      -4.454 -28.624  36.023  1.00 55.78           O  
-HETATM 3201  O   HOH A 675     -13.092 -20.997  17.495  1.00 45.73           O  
-HETATM 3202  O   HOH A 676      38.424 -43.378  18.884  1.00 48.49           O  
-HETATM 3203  O   HOH A 677      17.663 -51.580  24.458  1.00 49.03           O  
-HETATM 3204  O   HOH A 678      -0.956 -26.433  28.785  1.00 40.13           O  
-HETATM 3205  O   HOH A 679     -12.680 -40.260  17.294  1.00 35.21           O  
-HETATM 3206  O   HOH A 680      11.973 -60.029  11.207  1.00 40.14           O  
-HETATM 3207  O   HOH A 681      10.583 -20.475   2.116  1.00 36.94           O  
-HETATM 3208  O   HOH A 682     -16.460 -32.838  24.455  1.00 31.74           O  
-HETATM 3209  O   HOH A 683      11.946 -31.462  32.508  1.00 41.88           O  
-HETATM 3210  O   HOH A 684      17.725 -33.871  21.326  1.00 31.82           O  
-HETATM 3211  O   HOH A 685      17.274 -36.842  20.894  1.00 39.21           O  
-HETATM 3212  O   HOH A 686      18.354 -35.010  19.012  1.00 27.88           O  
-CONECT 2784 2785 2789                                                           
-CONECT 2785 2784 2786 2806                                                      
-CONECT 2786 2785 2787                                                           
-CONECT 2787 2786 2788 2811                                                      
-CONECT 2788 2787 2789 2813                                                      
-CONECT 2789 2784 2788                                                           
-CONECT 2790 2807                                                                
-CONECT 2791 2807                                                                
-CONECT 2792 2815                                                                
-CONECT 2793 2815                                                                
-CONECT 2794 2815                                                                
-CONECT 2795 2796 2797                                                           
-CONECT 2796 2795 2808                                                           
-CONECT 2797 2795 2810                                                           
-CONECT 2798 2799 2809                                                           
-CONECT 2799 2798 2813                                                           
-CONECT 2800 2808 2810                                                           
-CONECT 2801 2809 2812                                                           
-CONECT 2802 2803 2814                                                           
-CONECT 2803 2802 2814                                                           
-CONECT 2804 2811 2812                                                           
-CONECT 2805 2808 2811                                                           
-CONECT 2806 2785 2814                                                           
-CONECT 2807 2790 2791 2809                                                      
-CONECT 2808 2796 2800 2805                                                      
-CONECT 2809 2798 2801 2807                                                      
-CONECT 2810 2797 2800 2815                                                      
-CONECT 2811 2787 2804 2805                                                      
-CONECT 2812 2801 2804 2813                                                      
-CONECT 2813 2788 2799 2812                                                      
-CONECT 2814 2802 2803 2806                                                      
-CONECT 2815 2792 2793 2794 2810                                                 
-CONECT 2816 2817 2818 2819 2820                                                 
-CONECT 2817 2816                                                                
-CONECT 2818 2816                                                                
-CONECT 2819 2816                                                                
-CONECT 2820 2816                                                                
-CONECT 2821 2822 2823 2824 2825                                                 
-CONECT 2822 2821                                                                
-CONECT 2823 2821                                                                
-CONECT 2824 2821                                                                
-CONECT 2825 2821                                                                
-CONECT 2826 2827 2828 2829 2830                                                 
-CONECT 2827 2826                                                                
-CONECT 2828 2826                                                                
-CONECT 2829 2826                                                                
-CONECT 2830 2826                                                                
-CONECT 2831 2832 2833 2834 2835                                                 
-CONECT 2832 2831                                                                
-CONECT 2833 2831                                                                
-CONECT 2834 2831                                                                
-CONECT 2835 2831                                                                
-CONECT 2836 2837 2838                                                           
-CONECT 2837 2836                                                                
-CONECT 2838 2836 2839                                                           
-CONECT 2839 2838 2840                                                           
-CONECT 2840 2839 2841                                                           
-CONECT 2841 2840 2842                                                           
-CONECT 2842 2841                                                                
-CONECT 2843 2844 2845                                                           
-CONECT 2844 2843                                                                
-CONECT 2845 2843 2846                                                           
-CONECT 2846 2845                                                                
-CONECT 2847 2848 2849                                                           
-CONECT 2848 2847                                                                
-CONECT 2849 2847 2850                                                           
-CONECT 2850 2849                                                                
-CONECT 2851 2852 2853                                                           
-CONECT 2852 2851                                                                
-CONECT 2853 2851 2854                                                           
-CONECT 2854 2853                                                                
-CONECT 2855 2856 2857                                                           
-CONECT 2856 2855                                                                
-CONECT 2857 2855 2858                                                           
-CONECT 2858 2857                                                                
-CONECT 2859 2860 2861                                                           
-CONECT 2860 2859                                                                
-CONECT 2861 2859 2862                                                           
-CONECT 2862 2861                                                                
-CONECT 2863 2864 2865                                                           
-CONECT 2864 2863                                                                
-CONECT 2865 2863 2866                                                           
-CONECT 2866 2865                                                                
-CONECT 2867 2868 2869                                                           
-CONECT 2868 2867                                                                
-CONECT 2869 2867 2870                                                           
-CONECT 2870 2869                                                                
-CONECT 2871 2872 2873                                                           
-CONECT 2872 2871                                                                
-CONECT 2873 2871 2874                                                           
-CONECT 2874 2873                                                                
-CONECT 2875 2876 2877                                                           
-CONECT 2876 2875                                                                
-CONECT 2877 2875 2878                                                           
-CONECT 2878 2877                                                                
-MASTER      473    0   15   20    9    0   32    6 3194    1   95   26          
-END                                                                             
diff --git a/plip/test/pdb/3shy.pdb b/plip/test/pdb/3shy.pdb
deleted file mode 100644
index 7afd93f..0000000
--- a/plip/test/pdb/3shy.pdb
+++ /dev/null
@@ -1,2872 +0,0 @@
-HEADER    HYDROLASE/HYDROLASE INHIBITOR           17-JUN-11   3SHY              
-TITLE     CRYSTAL STRUCTURE OF THE PDE5A1 CATALYTIC DOMAIN IN COMPLEX WITH NOVEL
-TITLE    2 INHIBITORS                                                           
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE;              
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 FRAGMENT: UNP RESIDUES 535-860;                                      
-COMPND   5 SYNONYM: PDE5A1, CGMP-BINDING CGMP-SPECIFIC PHOSPHODIESTERASE, CGB-  
-COMPND   6 PDE;                                                                 
-COMPND   7 EC: 3.1.4.35;                                                        
-COMPND   8 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: PDE5, PDE5A;                                                   
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
-SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
-KEYWDS    PDE5A INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    T.T.CHEN,T.CHEN,Y.C.XU                                                
-REVDAT   1   24-AUG-11 3SHY    0                                                
-JRNL        AUTH   Z.XU,Z.LIU,T.CHEN,T.T.CHEN,Z.WANG,G.TIAN,J.SHI,X.WANG,Y.LU,  
-JRNL        AUTH 2 X.YAN,G.WANG,H.JIANG,K.CHEN,S.WANG,Y.XU,J.SHEN,W.ZHU         
-JRNL        TITL   UTILIZATION OF HALOGEN BOND IN LEAD OPTIMIZATION: A CASE     
-JRNL        TITL 2 STUDY OF RATIONAL DESIGN OF POTENT PHOSPHODIESTERASE TYPE 5  
-JRNL        TITL 3 (PDE5) INHIBITORS.                                           
-JRNL        REF    J.MED.CHEM.                   V.  54  5607 2011              
-JRNL        REFN                   ISSN 0022-2623                               
-JRNL        PMID   21714539                                                     
-JRNL        DOI    10.1021/JM200644R                                            
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : MLHL                                          
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.33                          
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
-REMARK   3   NUMBER OF REFLECTIONS             : 12511                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
-REMARK   3   R VALUE            (WORKING SET) : 0.211                           
-REMARK   3   FREE R VALUE                     : 0.259                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 608                             
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 36.3344 -  4.1997    0.99     3137   162  0.2103 0.2522        
-REMARK   3     2  4.1997 -  3.3342    0.99     3040   162  0.1831 0.2501        
-REMARK   3     3  3.3342 -  2.9129    0.97     2927   150  0.2361 0.2686        
-REMARK   3     4  2.9129 -  2.6467    0.93     2799   134  0.2645 0.3097        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.20                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
-REMARK   3   K_SOL              : 0.31                                          
-REMARK   3   B_SOL              : 51.95                                         
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.470           
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 58.51                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.99                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 2.51540                                              
-REMARK   3    B22 (A**2) : 2.51540                                              
-REMARK   3    B33 (A**2) : -5.03080                                             
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : -0.00000                                             
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.009           2354                                  
-REMARK   3   ANGLE     :  1.191           3192                                  
-REMARK   3   CHIRALITY :  0.071            368                                  
-REMARK   3   PLANARITY :  0.005            403                                  
-REMARK   3   DIHEDRAL  : 14.740            827                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 3SHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-11.                  
-REMARK 100 THE RCSB ID CODE IS RCSB066224.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 15-APR-11                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 7.5                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : SSRF                               
-REMARK 200  BEAMLINE                       : BL17U                              
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
-REMARK 200  DATA SCALING SOFTWARE          : XDS                                
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12774                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.647                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 36.331                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASER                                                
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 53.29                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 19-20%(W/V) PEG 3350, 200MM MGSO4,       
-REMARK 280  100MM TRIS-HCL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,              
-REMARK 280  TEMPERATURE 293K                                                    
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -Y,X-Y,Z+1/3                                            
-REMARK 290       3555   -X+Y,-X,Z+2/3                                           
-REMARK 290       4555   Y,X,-Z                                                  
-REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
-REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.97533            
-REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       87.95067            
-REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       87.95067            
-REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.97533            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A   514                                                      
-REMARK 465     GLY A   515                                                      
-REMARK 465     SER A   516                                                      
-REMARK 465     SER A   517                                                      
-REMARK 465     HIS A   518                                                      
-REMARK 465     HIS A   519                                                      
-REMARK 465     HIS A   520                                                      
-REMARK 465     HIS A   521                                                      
-REMARK 465     HIS A   522                                                      
-REMARK 465     HIS A   523                                                      
-REMARK 465     SER A   524                                                      
-REMARK 465     SER A   525                                                      
-REMARK 465     GLY A   526                                                      
-REMARK 465     LEU A   527                                                      
-REMARK 465     VAL A   528                                                      
-REMARK 465     PRO A   529                                                      
-REMARK 465     ARG A   530                                                      
-REMARK 465     GLY A   531                                                      
-REMARK 465     SER A   532                                                      
-REMARK 465     HIS A   533                                                      
-REMARK 465     MET A   534                                                      
-REMARK 465     GLU A   535                                                      
-REMARK 465     HIS A   670                                                      
-REMARK 465     PRO A   671                                                      
-REMARK 465     LEU A   672                                                      
-REMARK 465     ALA A   673                                                      
-REMARK 465     GLN A   674                                                      
-REMARK 465     LEU A   675                                                      
-REMARK 465     TYR A   676                                                      
-REMARK 465     CYS A   677                                                      
-REMARK 465     GLY A   790                                                      
-REMARK 465     ASP A   791                                                      
-REMARK 465     ARG A   792                                                      
-REMARK 465     GLU A   793                                                      
-REMARK 465     ARG A   794                                                      
-REMARK 465     LYS A   795                                                      
-REMARK 465     GLU A   796                                                      
-REMARK 465     LEU A   797                                                      
-REMARK 465     ASN A   798                                                      
-REMARK 465     ILE A   799                                                      
-REMARK 465     GLU A   800                                                      
-REMARK 465     PRO A   801                                                      
-REMARK 465     THR A   802                                                      
-REMARK 465     ASP A   803                                                      
-REMARK 465     LEU A   804                                                      
-REMARK 465     MET A   805                                                      
-REMARK 465     ASN A   806                                                      
-REMARK 465     ARG A   807                                                      
-REMARK 465     GLU A   808                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     GLU A 536    CG   CD   OE1  OE2                                  
-REMARK 470     ARG A 538    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     LEU A 540    CG   CD1  CD2                                       
-REMARK 470     GLN A 541    CG   CD   OE1  NE2                                  
-REMARK 470     LEU A 543    CD1  CD2                                            
-REMARK 470     GLN A 589    OE1  NE2                                            
-REMARK 470     LYS A 591    CD   CE   NZ                                        
-REMARK 470     GLU A 593    CG   CD   OE1  OE2                                  
-REMARK 470     ARG A 597    CZ   NH1  NH2                                       
-REMARK 470     LYS A 604    CD   CE   NZ                                        
-REMARK 470     LYS A 608    CD   CE   NZ                                        
-REMARK 470     LYS A 633    CE   NZ                                             
-REMARK 470     ASN A 636    CG   OD1  ND2                                       
-REMARK 470     ASN A 662    OD1  ND2                                            
-REMARK 470     SER A 663    OG                                                  
-REMARK 470     TYR A 664    CG   CD1  CD2  CE1  CE2  CZ   OH                    
-REMARK 470     ILE A 665    CB   CG1  CG2  CD1                                  
-REMARK 470     GLN A 666    CB   CG   CD   OE1  NE2                             
-REMARK 470     ARG A 667    CB   CG   CD   NE   CZ   NH1  NH2                   
-REMARK 470     SER A 668    CB   OG                                             
-REMARK 470     GLU A 669    CB   CG   CD   OE1  OE2                             
-REMARK 470     ILE A 706    CD1                                                 
-REMARK 470     GLU A 707    CG   CD   OE1  OE2                                  
-REMARK 470     LYS A 714    CG   CD   CE   NZ                                   
-REMARK 470     LEU A 727    CD1  CD2                                            
-REMARK 470     LYS A 730    CD   CE   NZ                                        
-REMARK 470     LYS A 741    CG   CD   CE   NZ                                   
-REMARK 470     ASN A 742    CG   OD1  ND2                                       
-REMARK 470     GLN A 743    CD   OE1  NE2                                       
-REMARK 470     LEU A 746    CG   CD1  CD2                                       
-REMARK 470     GLU A 747    CG   CD   OE1  OE2                                  
-REMARK 470     LYS A 809    CG   CD   CE   NZ                                   
-REMARK 470     LYS A 810    CG   CD   CE   NZ                                   
-REMARK 470     ASN A 811    CG   OD1  ND2                                       
-REMARK 470     LYS A 812    CG   CD   CE   NZ                                   
-REMARK 470     ILE A 824    CD1                                                 
-REMARK 470     LEU A 826    CD1  CD2                                            
-REMARK 470     GLU A 837    CG   CD   OE1  OE2                                  
-REMARK 470     GLN A 851    CD   OE1  NE2                                       
-REMARK 470     GLN A 859    CG   CD   OE1  NE2                                  
-REMARK 470     GLN A 860    OE1  NE2                                            
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    PHE A 561      150.50    -44.58                                   
-REMARK 500    ASN A 583       17.35     84.25                                   
-REMARK 500    GLN A 586      -72.67    -54.16                                   
-REMARK 500    LYS A 630      -76.11    -85.87                                   
-REMARK 500    ASN A 661       32.30    -95.46                                   
-REMARK 500    ARG A 667     -114.55     41.45                                   
-REMARK 500    ILE A 700        1.56    -62.07                                   
-REMARK 500    ASN A 742       10.24     43.92                                   
-REMARK 500    PRO A 841      -19.52    -48.92                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 620                                                                      
-REMARK 620 METAL COORDINATION                                                   
-REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              ZN A 861  ZN                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 ASP A 654   OD2                                                    
-REMARK 620 2 ASP A 764   OD1 158.9                                              
-REMARK 620 3 HIS A 653   NE2  81.4  83.0                                        
-REMARK 620 4 HIS A 617   NE2  88.9  76.3  88.2                                  
-REMARK 620 N                    1     2     3                                   
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG A 862  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 HOH A  11   O                                                      
-REMARK 620 2 HOH A 864   O   150.4                                              
-REMARK 620 N                    1                                               
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5FO A 1                   
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 861                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 862                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3                    
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 1T9R   RELATED DB: PDB                                   
-REMARK 900 PDE5A CATALYTIC DOMAIN COMPLEX WITH INHIBITORS                       
-REMARK 900 RELATED ID: 3SHZ   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 3SIE   RELATED DB: PDB                                   
-DBREF  3SHY A  535   860  UNP    O76074   PDE5A_HUMAN    535    860             
-SEQADV 3SHY MET A  514  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY GLY A  515  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY SER A  516  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY SER A  517  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY HIS A  518  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY HIS A  519  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY HIS A  520  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY HIS A  521  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY HIS A  522  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY HIS A  523  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY SER A  524  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY SER A  525  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY GLY A  526  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY LEU A  527  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY VAL A  528  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY PRO A  529  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY ARG A  530  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY GLY A  531  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY SER A  532  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY HIS A  533  UNP  O76074              EXPRESSION TAG                 
-SEQADV 3SHY MET A  534  UNP  O76074              EXPRESSION TAG                 
-SEQRES   1 A  347  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
-SEQRES   2 A  347  LEU VAL PRO ARG GLY SER HIS MET GLU GLU THR ARG GLU          
-SEQRES   3 A  347  LEU GLN SER LEU ALA ALA ALA VAL VAL PRO SER ALA GLN          
-SEQRES   4 A  347  THR LEU LYS ILE THR ASP PHE SER PHE SER ASP PHE GLU          
-SEQRES   5 A  347  LEU SER ASP LEU GLU THR ALA LEU CYS THR ILE ARG MET          
-SEQRES   6 A  347  PHE THR ASP LEU ASN LEU VAL GLN ASN PHE GLN MET LYS          
-SEQRES   7 A  347  HIS GLU VAL LEU CYS ARG TRP ILE LEU SER VAL LYS LYS          
-SEQRES   8 A  347  ASN TYR ARG LYS ASN VAL ALA TYR HIS ASN TRP ARG HIS          
-SEQRES   9 A  347  ALA PHE ASN THR ALA GLN CYS MET PHE ALA ALA LEU LYS          
-SEQRES  10 A  347  ALA GLY LYS ILE GLN ASN LYS LEU THR ASP LEU GLU ILE          
-SEQRES  11 A  347  LEU ALA LEU LEU ILE ALA ALA LEU SER HIS ASP LEU ASP          
-SEQRES  12 A  347  HIS ARG GLY VAL ASN ASN SER TYR ILE GLN ARG SER GLU          
-SEQRES  13 A  347  HIS PRO LEU ALA GLN LEU TYR CYS HIS SER ILE MET GLU          
-SEQRES  14 A  347  HIS HIS HIS PHE ASP GLN CYS LEU MET ILE LEU ASN SER          
-SEQRES  15 A  347  PRO GLY ASN GLN ILE LEU SER GLY LEU SER ILE GLU GLU          
-SEQRES  16 A  347  TYR LYS THR THR LEU LYS ILE ILE LYS GLN ALA ILE LEU          
-SEQRES  17 A  347  ALA THR ASP LEU ALA LEU TYR ILE LYS ARG ARG GLY GLU          
-SEQRES  18 A  347  PHE PHE GLU LEU ILE ARG LYS ASN GLN PHE ASN LEU GLU          
-SEQRES  19 A  347  ASP PRO HIS GLN LYS GLU LEU PHE LEU ALA MET LEU MET          
-SEQRES  20 A  347  THR ALA CYS ASP LEU SER ALA ILE THR LYS PRO TRP PRO          
-SEQRES  21 A  347  ILE GLN GLN ARG ILE ALA GLU LEU VAL ALA THR GLU PHE          
-SEQRES  22 A  347  PHE ASP GLN GLY ASP ARG GLU ARG LYS GLU LEU ASN ILE          
-SEQRES  23 A  347  GLU PRO THR ASP LEU MET ASN ARG GLU LYS LYS ASN LYS          
-SEQRES  24 A  347  ILE PRO SER MET GLN VAL GLY PHE ILE ASP ALA ILE CYS          
-SEQRES  25 A  347  LEU GLN LEU TYR GLU ALA LEU THR HIS VAL SER GLU ASP          
-SEQRES  26 A  347  CYS PHE PRO LEU LEU ASP GLY CYS ARG LYS ASN ARG GLN          
-SEQRES  27 A  347  LYS TRP GLN ALA LEU ALA GLU GLN GLN                          
-HET    5FO  A   1      30                                                       
-HET     ZN  A 861       1                                                       
-HET     MG  A 862       1                                                       
-HET     MG  A   2       1                                                       
-HET     MG  A   3       1                                                       
-HETNAM     5FO 6-ETHYL-5-FLUORO-2-{5-[(4-METHYLPIPERAZIN-1-YL)                  
-HETNAM   2 5FO  SULFONYL]-2-PROPOXYPHENYL}PYRIMIDIN-4(3H)-ONE                   
-HETNAM      ZN ZINC ION                                                         
-HETNAM      MG MAGNESIUM ION                                                    
-FORMUL   2  5FO    C20 H27 F N4 O4 S                                            
-FORMUL   3   ZN    ZN 2+                                                        
-FORMUL   4   MG    3(MG 2+)                                                     
-FORMUL   7  HOH   *12(H2 O)                                                     
-HELIX    1   1 THR A  537  ALA A  546  1                                  10    
-HELIX    2   2 SER A  550  LYS A  555  1                                   6    
-HELIX    3   3 SER A  567  LEU A  582  1                                  16    
-HELIX    4   4 ASN A  583  GLN A  589  1                                   7    
-HELIX    5   5 LYS A  591  ASN A  605  1                                  15    
-HELIX    6   6 ASN A  614  LYS A  630  1                                  17    
-HELIX    7   7 ILE A  634  LEU A  638  5                                   5    
-HELIX    8   8 THR A  639  HIS A  653  1                                  15    
-HELIX    9   9 SER A  679  ASN A  694  1                                  16    
-HELIX   10  10 SER A  705  THR A  723  1                                  19    
-HELIX   11  11 ASP A  724  LYS A  741  1                                  18    
-HELIX   12  12 ASP A  748  LEU A  765  1                                  18    
-HELIX   13  13 SER A  766  LYS A  770  5                                   5    
-HELIX   14  14 PRO A  771  GLN A  789  1                                  19    
-HELIX   15  15 LYS A  812  ILE A  824  1                                  13    
-HELIX   16  16 ILE A  824  SER A  836  1                                  13    
-HELIX   17  17 CYS A  839  GLN A  860  1                                  22    
-LINK         OD2 ASP A 654                ZN    ZN A 861     1555   1555  2.21  
-LINK         OD1 ASP A 764                ZN    ZN A 861     1555   1555  2.27  
-LINK         NE2 HIS A 653                ZN    ZN A 861     1555   1555  2.38  
-LINK         NE2 HIS A 617                ZN    ZN A 861     1555   1555  2.40  
-LINK        MG    MG A 862                 O   HOH A  11     1555   1555  2.61  
-LINK        MG    MG A 862                 O   HOH A 864     1555   1555  2.64  
-SITE     1 AC1  8 SER A 668  ALA A 779  PHE A 786  ILE A 813                    
-SITE     2 AC1  8 MET A 816  GLN A 817  PHE A 820  HOH A 865                    
-SITE     1 AC2  6 HIS A 617  HIS A 653  ASP A 654  ASP A 764                    
-SITE     2 AC2  6  MG A 862  HOH A 864                                          
-SITE     1 AC3  5 HOH A  11  HIS A 613  ASP A 654   ZN A 861                    
-SITE     2 AC3  5 HOH A 864                                                     
-SITE     1 AC4  1 ASP A 568                                                     
-CRYST1   74.458   74.458  131.926  90.00  90.00 120.00 P 31 2 1      6          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.013430  0.007754  0.000000        0.00000                         
-SCALE2      0.000000  0.015508  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.007580        0.00000                         
-ATOM      1  N   GLU A 536     -55.723   3.872   4.784  1.00 86.68           N  
-ATOM      2  CA  GLU A 536     -55.565   5.219   5.337  1.00 91.35           C  
-ATOM      3  C   GLU A 536     -56.803   5.728   6.109  1.00 90.65           C  
-ATOM      4  O   GLU A 536     -57.944   5.376   5.803  1.00 85.92           O  
-ATOM      5  CB  GLU A 536     -55.168   6.216   4.235  1.00 79.93           C  
-ATOM      6  N   THR A 537     -56.558   6.557   7.118  1.00 90.64           N  
-ATOM      7  CA  THR A 537     -57.630   7.190   7.879  1.00 89.54           C  
-ATOM      8  C   THR A 537     -57.911   8.591   7.336  1.00 86.16           C  
-ATOM      9  O   THR A 537     -57.093   9.171   6.612  1.00 84.94           O  
-ATOM     10  CB  THR A 537     -57.284   7.272   9.402  1.00 90.58           C  
-ATOM     11  OG1 THR A 537     -58.240   8.103  10.074  1.00 94.75           O  
-ATOM     12  CG2 THR A 537     -55.890   7.858   9.627  1.00 84.42           C  
-ATOM     13  N   ARG A 538     -59.068   9.142   7.674  1.00 82.88           N  
-ATOM     14  CA  ARG A 538     -59.307  10.535   7.348  1.00 85.24           C  
-ATOM     15  C   ARG A 538     -58.118  11.346   7.860  1.00 86.64           C  
-ATOM     16  O   ARG A 538     -57.518  12.132   7.122  1.00 83.79           O  
-ATOM     17  CB  ARG A 538     -60.609  11.031   7.980  1.00 77.41           C  
-ATOM     18  N   GLU A 539     -57.764  11.108   9.124  1.00 89.81           N  
-ATOM     19  CA  GLU A 539     -56.752  11.895   9.835  1.00 85.93           C  
-ATOM     20  C   GLU A 539     -55.368  11.834   9.193  1.00 83.21           C  
-ATOM     21  O   GLU A 539     -54.631  12.835   9.183  1.00 76.53           O  
-ATOM     22  CB  GLU A 539     -56.672  11.457  11.299  1.00 82.59           C  
-ATOM     23  CG  GLU A 539     -55.842  12.385  12.160  1.00 85.52           C  
-ATOM     24  CD  GLU A 539     -55.895  12.033  13.644  1.00 88.19           C  
-ATOM     25  OE1 GLU A 539     -56.148  10.854  13.981  1.00 81.16           O  
-ATOM     26  OE2 GLU A 539     -55.686  12.945  14.476  1.00 84.64           O  
-ATOM     27  N   LEU A 540     -55.024  10.659   8.661  1.00 83.61           N  
-ATOM     28  CA  LEU A 540     -53.760  10.483   7.946  1.00 80.66           C  
-ATOM     29  C   LEU A 540     -53.720  11.366   6.714  1.00 76.97           C  
-ATOM     30  O   LEU A 540     -52.741  12.073   6.502  1.00 72.47           O  
-ATOM     31  CB  LEU A 540     -53.520   9.019   7.554  1.00 78.61           C  
-ATOM     32  N   GLN A 541     -54.786  11.324   5.911  1.00 79.86           N  
-ATOM     33  CA  GLN A 541     -54.858  12.128   4.690  1.00 79.87           C  
-ATOM     34  C   GLN A 541     -54.671  13.623   4.996  1.00 78.38           C  
-ATOM     35  O   GLN A 541     -53.884  14.308   4.335  1.00 75.00           O  
-ATOM     36  CB  GLN A 541     -56.172  11.874   3.937  1.00 73.29           C  
-ATOM     37  N   SER A 542     -55.376  14.114   6.013  1.00 75.51           N  
-ATOM     38  CA  SER A 542     -55.292  15.520   6.391  1.00 77.85           C  
-ATOM     39  C   SER A 542     -53.870  15.921   6.772  1.00 78.78           C  
-ATOM     40  O   SER A 542     -53.362  16.939   6.275  1.00 75.24           O  
-ATOM     41  CB  SER A 542     -56.244  15.845   7.552  1.00 80.98           C  
-ATOM     42  OG  SER A 542     -57.333  14.933   7.611  1.00 86.83           O  
-ATOM     43  N   LEU A 543     -53.234  15.142   7.659  1.00 75.94           N  
-ATOM     44  CA  LEU A 543     -51.899  15.507   8.149  1.00 70.55           C  
-ATOM     45  C   LEU A 543     -50.870  15.358   7.050  1.00 67.08           C  
-ATOM     46  O   LEU A 543     -49.948  16.165   6.937  1.00 68.12           O  
-ATOM     47  CB  LEU A 543     -51.483  14.705   9.388  1.00 73.81           C  
-ATOM     48  CG  LEU A 543     -50.117  15.094   9.997  1.00 61.14           C  
-ATOM     49  N   ALA A 544     -51.040  14.329   6.227  1.00 70.28           N  
-ATOM     50  CA  ALA A 544     -50.159  14.121   5.076  1.00 71.95           C  
-ATOM     51  C   ALA A 544     -50.229  15.293   4.101  1.00 70.51           C  
-ATOM     52  O   ALA A 544     -49.194  15.775   3.630  1.00 67.46           O  
-ATOM     53  CB  ALA A 544     -50.483  12.810   4.368  1.00 67.98           C  
-ATOM     54  N   ALA A 545     -51.447  15.760   3.829  1.00 67.85           N  
-ATOM     55  CA  ALA A 545     -51.663  16.843   2.870  1.00 69.92           C  
-ATOM     56  C   ALA A 545     -51.380  18.246   3.404  1.00 70.32           C  
-ATOM     57  O   ALA A 545     -51.389  19.204   2.643  1.00 69.56           O  
-ATOM     58  CB  ALA A 545     -53.072  16.782   2.312  1.00 70.51           C  
-ATOM     59  N   ALA A 546     -51.128  18.375   4.702  1.00 73.51           N  
-ATOM     60  CA  ALA A 546     -50.967  19.702   5.312  1.00 70.32           C  
-ATOM     61  C   ALA A 546     -49.655  20.410   4.961  1.00 71.22           C  
-ATOM     62  O   ALA A 546     -48.757  19.825   4.369  1.00 73.81           O  
-ATOM     63  CB  ALA A 546     -51.131  19.609   6.807  1.00 66.04           C  
-ATOM     64  N   VAL A 547     -49.559  21.689   5.305  1.00 79.30           N  
-ATOM     65  CA  VAL A 547     -48.293  22.414   5.183  1.00 75.26           C  
-ATOM     66  C   VAL A 547     -47.697  22.512   6.575  1.00 76.35           C  
-ATOM     67  O   VAL A 547     -48.434  22.610   7.571  1.00 74.80           O  
-ATOM     68  CB  VAL A 547     -48.483  23.852   4.657  1.00 73.27           C  
-ATOM     69  CG1 VAL A 547     -47.169  24.375   4.064  1.00 73.77           C  
-ATOM     70  CG2 VAL A 547     -49.603  23.902   3.634  1.00 75.35           C  
-ATOM     71  N   VAL A 548     -46.373  22.491   6.657  1.00 71.78           N  
-ATOM     72  CA  VAL A 548     -45.715  22.492   7.955  1.00 69.31           C  
-ATOM     73  C   VAL A 548     -45.088  23.859   8.213  1.00 67.69           C  
-ATOM     74  O   VAL A 548     -44.042  24.191   7.636  1.00 65.49           O  
-ATOM     75  CB  VAL A 548     -44.661  21.345   8.067  1.00 66.31           C  
-ATOM     76  CG1 VAL A 548     -43.973  21.352   9.436  1.00 61.36           C  
-ATOM     77  CG2 VAL A 548     -45.312  20.007   7.807  1.00 62.10           C  
-ATOM     78  N   PRO A 549     -45.736  24.658   9.081  1.00 66.70           N  
-ATOM     79  CA  PRO A 549     -45.258  26.000   9.428  1.00 60.36           C  
-ATOM     80  C   PRO A 549     -43.813  25.955   9.854  1.00 60.18           C  
-ATOM     81  O   PRO A 549     -43.291  24.885  10.114  1.00 64.10           O  
-ATOM     82  CB  PRO A 549     -46.142  26.384  10.617  1.00 62.02           C  
-ATOM     83  CG  PRO A 549     -47.431  25.646  10.364  1.00 59.71           C  
-ATOM     84  CD  PRO A 549     -47.007  24.327   9.761  1.00 64.19           C  
-ATOM     85  N   SER A 550     -43.179  27.112   9.933  1.00 63.69           N  
-ATOM     86  CA  SER A 550     -41.801  27.210  10.375  1.00 62.95           C  
-ATOM     87  C   SER A 550     -41.714  26.900  11.871  1.00 66.98           C  
-ATOM     88  O   SER A 550     -42.728  26.853  12.565  1.00 66.02           O  
-ATOM     89  CB  SER A 550     -41.287  28.625  10.104  1.00 62.76           C  
-ATOM     90  OG  SER A 550     -39.981  28.810  10.623  1.00 69.12           O  
-ATOM     91  N   ALA A 551     -40.501  26.700  12.369  1.00 66.92           N  
-ATOM     92  CA  ALA A 551     -40.317  26.500  13.793  1.00 59.67           C  
-ATOM     93  C   ALA A 551     -40.725  27.759  14.507  1.00 65.74           C  
-ATOM     94  O   ALA A 551     -41.323  27.702  15.581  1.00 70.50           O  
-ATOM     95  CB  ALA A 551     -38.875  26.170  14.108  1.00 59.00           C  
-ATOM     96  N   GLN A 552     -40.392  28.906  13.922  1.00 70.03           N  
-ATOM     97  CA  GLN A 552     -40.688  30.184  14.570  1.00 72.96           C  
-ATOM     98  C   GLN A 552     -42.190  30.379  14.682  1.00 66.70           C  
-ATOM     99  O   GLN A 552     -42.705  30.753  15.724  1.00 69.50           O  
-ATOM    100  CB  GLN A 552     -40.066  31.347  13.809  1.00 75.78           C  
-ATOM    101  CG  GLN A 552     -38.628  31.646  14.183  1.00 83.82           C  
-ATOM    102  CD  GLN A 552     -38.064  32.819  13.384  1.00 97.22           C  
-ATOM    103  OE1 GLN A 552     -38.434  33.977  13.621  1.00 89.22           O  
-ATOM    104  NE2 GLN A 552     -37.174  32.521  12.421  1.00 93.18           N  
-ATOM    105  N   THR A 553     -42.881  30.106  13.589  1.00 66.28           N  
-ATOM    106  CA  THR A 553     -44.330  30.217  13.521  1.00 65.41           C  
-ATOM    107  C   THR A 553     -44.989  29.306  14.556  1.00 69.12           C  
-ATOM    108  O   THR A 553     -46.068  29.619  15.085  1.00 67.20           O  
-ATOM    109  CB  THR A 553     -44.819  29.817  12.097  1.00 69.83           C  
-ATOM    110  OG1 THR A 553     -44.076  30.545  11.103  1.00 69.07           O  
-ATOM    111  CG2 THR A 553     -46.317  30.049  11.925  1.00 53.96           C  
-ATOM    112  N   LEU A 554     -44.326  28.180  14.836  1.00 67.34           N  
-ATOM    113  CA  LEU A 554     -44.857  27.168  15.738  1.00 62.10           C  
-ATOM    114  C   LEU A 554     -44.365  27.364  17.169  1.00 63.17           C  
-ATOM    115  O   LEU A 554     -44.946  26.827  18.120  1.00 60.19           O  
-ATOM    116  CB  LEU A 554     -44.557  25.770  15.220  1.00 59.74           C  
-ATOM    117  CG  LEU A 554     -45.363  25.442  13.966  1.00 60.96           C  
-ATOM    118  CD1 LEU A 554     -44.918  24.128  13.384  1.00 57.35           C  
-ATOM    119  CD2 LEU A 554     -46.864  25.432  14.243  1.00 52.74           C  
-ATOM    120  N   LYS A 555     -43.318  28.164  17.316  1.00 60.98           N  
-ATOM    121  CA  LYS A 555     -42.921  28.633  18.634  1.00 63.15           C  
-ATOM    122  C   LYS A 555     -42.254  27.539  19.435  1.00 61.38           C  
-ATOM    123  O   LYS A 555     -42.015  27.672  20.634  1.00 63.51           O  
-ATOM    124  CB  LYS A 555     -44.144  29.148  19.383  1.00 59.57           C  
-ATOM    125  CG  LYS A 555     -44.388  30.627  19.190  1.00 66.59           C  
-ATOM    126  CD  LYS A 555     -45.814  30.998  19.577  1.00 68.78           C  
-ATOM    127  CE  LYS A 555     -46.810  30.273  18.690  1.00 71.52           C  
-ATOM    128  NZ  LYS A 555     -48.209  30.658  19.026  1.00 77.61           N  
-ATOM    129  N   ILE A 556     -41.935  26.451  18.760  1.00 61.65           N  
-ATOM    130  CA  ILE A 556     -41.441  25.274  19.443  1.00 57.25           C  
-ATOM    131  C   ILE A 556     -39.973  25.407  19.821  1.00 58.73           C  
-ATOM    132  O   ILE A 556     -39.342  24.419  20.166  1.00 62.59           O  
-ATOM    133  CB  ILE A 556     -41.603  24.054  18.563  1.00 55.75           C  
-ATOM    134  CG1 ILE A 556     -40.765  24.248  17.298  1.00 61.08           C  
-ATOM    135  CG2 ILE A 556     -43.062  23.856  18.201  1.00 53.10           C  
-ATOM    136  CD1 ILE A 556     -40.855  23.108  16.318  1.00 62.88           C  
-ATOM    137  N   THR A 557     -39.423  26.617  19.767  1.00 62.21           N  
-ATOM    138  CA  THR A 557     -38.019  26.819  20.135  1.00 60.96           C  
-ATOM    139  C   THR A 557     -37.893  27.518  21.473  1.00 59.98           C  
-ATOM    140  O   THR A 557     -36.791  27.674  22.005  1.00 59.24           O  
-ATOM    141  CB  THR A 557     -37.236  27.648  19.085  1.00 60.53           C  
-ATOM    142  OG1 THR A 557     -37.463  27.107  17.782  1.00 65.44           O  
-ATOM    143  CG2 THR A 557     -35.737  27.584  19.378  1.00 62.56           C  
-ATOM    144  N   ASP A 558     -39.024  27.954  22.012  1.00 60.47           N  
-ATOM    145  CA  ASP A 558     -39.007  28.690  23.268  1.00 64.34           C  
-ATOM    146  C   ASP A 558     -39.182  27.723  24.423  1.00 59.28           C  
-ATOM    147  O   ASP A 558     -40.115  26.916  24.426  1.00 55.90           O  
-ATOM    148  CB  ASP A 558     -40.118  29.755  23.290  1.00 66.88           C  
-ATOM    149  CG  ASP A 558     -40.311  30.439  21.927  1.00 78.04           C  
-ATOM    150  OD1 ASP A 558     -39.302  30.870  21.298  1.00 79.94           O  
-ATOM    151  OD2 ASP A 558     -41.482  30.535  21.479  1.00 76.92           O  
-ATOM    152  N   PHE A 559     -38.289  27.801  25.404  1.00 54.86           N  
-ATOM    153  CA  PHE A 559     -38.446  26.986  26.595  1.00 55.50           C  
-ATOM    154  C   PHE A 559     -39.811  27.168  27.262  1.00 60.37           C  
-ATOM    155  O   PHE A 559     -40.272  26.294  27.998  1.00 64.64           O  
-ATOM    156  CB  PHE A 559     -37.333  27.258  27.593  1.00 57.95           C  
-ATOM    157  CG  PHE A 559     -36.010  26.692  27.186  1.00 61.44           C  
-ATOM    158  CD1 PHE A 559     -34.974  27.529  26.796  1.00 59.34           C  
-ATOM    159  CD2 PHE A 559     -35.797  25.314  27.191  1.00 60.65           C  
-ATOM    160  CE1 PHE A 559     -33.745  27.004  26.422  1.00 62.97           C  
-ATOM    161  CE2 PHE A 559     -34.577  24.778  26.825  1.00 57.47           C  
-ATOM    162  CZ  PHE A 559     -33.546  25.625  26.433  1.00 63.13           C  
-ATOM    163  N   SER A 560     -40.465  28.292  27.002  1.00 58.29           N  
-ATOM    164  CA  SER A 560     -41.729  28.591  27.666  1.00 58.85           C  
-ATOM    165  C   SER A 560     -42.913  28.166  26.819  1.00 54.68           C  
-ATOM    166  O   SER A 560     -44.064  28.487  27.120  1.00 55.63           O  
-ATOM    167  CB  SER A 560     -41.803  30.078  28.014  1.00 62.12           C  
-ATOM    168  OG  SER A 560     -41.304  30.847  26.933  1.00 71.52           O  
-ATOM    169  N   PHE A 561     -42.626  27.424  25.761  1.00 53.00           N  
-ATOM    170  CA  PHE A 561     -43.673  26.882  24.895  1.00 50.16           C  
-ATOM    171  C   PHE A 561     -44.861  26.268  25.647  1.00 51.78           C  
-ATOM    172  O   PHE A 561     -44.718  25.742  26.757  1.00 51.89           O  
-ATOM    173  CB  PHE A 561     -43.070  25.837  23.975  1.00 48.88           C  
-ATOM    174  CG  PHE A 561     -44.070  25.130  23.139  1.00 47.76           C  
-ATOM    175  CD1 PHE A 561     -44.404  25.614  21.884  1.00 48.43           C  
-ATOM    176  CD2 PHE A 561     -44.683  23.978  23.602  1.00 45.57           C  
-ATOM    177  CE1 PHE A 561     -45.334  24.959  21.101  1.00 48.60           C  
-ATOM    178  CE2 PHE A 561     -45.615  23.317  22.833  1.00 48.53           C  
-ATOM    179  CZ  PHE A 561     -45.941  23.808  21.569  1.00 51.55           C  
-ATOM    180  N   SER A 562     -46.034  26.322  25.028  1.00 51.12           N  
-ATOM    181  CA  SER A 562     -47.219  25.712  25.608  1.00 49.55           C  
-ATOM    182  C   SER A 562     -48.189  25.217  24.541  1.00 52.66           C  
-ATOM    183  O   SER A 562     -48.235  25.748  23.441  1.00 54.42           O  
-ATOM    184  CB  SER A 562     -47.924  26.674  26.558  1.00 48.15           C  
-ATOM    185  OG  SER A 562     -49.112  26.081  27.065  1.00 56.68           O  
-ATOM    186  N   ASP A 563     -48.977  24.203  24.887  1.00 53.81           N  
-ATOM    187  CA  ASP A 563     -49.765  23.482  23.902  1.00 53.21           C  
-ATOM    188  C   ASP A 563     -51.261  23.570  24.138  1.00 53.64           C  
-ATOM    189  O   ASP A 563     -52.021  22.932  23.421  1.00 53.50           O  
-ATOM    190  CB  ASP A 563     -49.386  22.009  23.955  1.00 49.54           C  
-ATOM    191  CG  ASP A 563     -49.920  21.324  25.206  1.00 55.58           C  
-ATOM    192  OD1 ASP A 563     -49.367  21.582  26.296  1.00 56.43           O  
-ATOM    193  OD2 ASP A 563     -50.911  20.548  25.110  1.00 56.28           O  
-ATOM    194  N   PHE A 564     -51.692  24.304  25.159  1.00 52.09           N  
-ATOM    195  CA  PHE A 564     -53.110  24.292  25.536  1.00 54.86           C  
-ATOM    196  C   PHE A 564     -54.042  24.724  24.392  1.00 58.35           C  
-ATOM    197  O   PHE A 564     -55.159  24.223  24.269  1.00 59.98           O  
-ATOM    198  CB  PHE A 564     -53.382  25.174  26.763  1.00 57.38           C  
-ATOM    199  CG  PHE A 564     -52.749  24.687  28.038  1.00 54.84           C  
-ATOM    200  CD1 PHE A 564     -52.369  25.592  29.021  1.00 55.45           C  
-ATOM    201  CD2 PHE A 564     -52.551  23.340  28.273  1.00 55.53           C  
-ATOM    202  CE1 PHE A 564     -51.786  25.160  30.219  1.00 55.71           C  
-ATOM    203  CE2 PHE A 564     -51.969  22.901  29.469  1.00 54.35           C  
-ATOM    204  CZ  PHE A 564     -51.590  23.812  30.441  1.00 51.85           C  
-ATOM    205  N   GLU A 565     -53.592  25.653  23.556  1.00 56.01           N  
-ATOM    206  CA  GLU A 565     -54.433  26.147  22.469  1.00 60.30           C  
-ATOM    207  C   GLU A 565     -54.329  25.324  21.184  1.00 61.53           C  
-ATOM    208  O   GLU A 565     -55.014  25.612  20.199  1.00 61.71           O  
-ATOM    209  CB  GLU A 565     -54.066  27.586  22.134  1.00 59.78           C  
-ATOM    210  CG  GLU A 565     -52.709  27.708  21.479  1.00 60.29           C  
-ATOM    211  CD  GLU A 565     -51.629  28.136  22.472  1.00 68.85           C  
-ATOM    212  OE1 GLU A 565     -51.701  27.744  23.678  1.00 59.23           O  
-ATOM    213  OE2 GLU A 565     -50.717  28.880  22.033  1.00 67.80           O  
-ATOM    214  N   LEU A 566     -53.466  24.316  21.185  1.00 57.91           N  
-ATOM    215  CA  LEU A 566     -53.222  23.533  19.988  1.00 54.74           C  
-ATOM    216  C   LEU A 566     -54.201  22.388  19.864  1.00 57.48           C  
-ATOM    217  O   LEU A 566     -54.621  21.803  20.864  1.00 54.20           O  
-ATOM    218  CB  LEU A 566     -51.798  22.994  19.985  1.00 52.15           C  
-ATOM    219  CG  LEU A 566     -50.739  24.078  20.102  1.00 56.39           C  
-ATOM    220  CD1 LEU A 566     -49.358  23.525  19.823  1.00 55.26           C  
-ATOM    221  CD2 LEU A 566     -51.064  25.161  19.116  1.00 62.76           C  
-ATOM    222  N   SER A 567     -54.560  22.084  18.617  1.00 62.18           N  
-ATOM    223  CA  SER A 567     -55.379  20.923  18.288  1.00 63.18           C  
-ATOM    224  C   SER A 567     -54.444  19.740  18.129  1.00 56.81           C  
-ATOM    225  O   SER A 567     -53.239  19.914  17.975  1.00 55.27           O  
-ATOM    226  CB  SER A 567     -56.138  21.151  16.971  1.00 61.90           C  
-ATOM    227  OG  SER A 567     -55.248  21.201  15.851  1.00 63.83           O  
-ATOM    228  N   ASP A 568     -54.999  18.539  18.141  1.00 57.30           N  
-ATOM    229  CA  ASP A 568     -54.184  17.363  17.876  1.00 59.33           C  
-ATOM    230  C   ASP A 568     -53.394  17.533  16.608  1.00 59.29           C  
-ATOM    231  O   ASP A 568     -52.180  17.339  16.606  1.00 61.58           O  
-ATOM    232  CB  ASP A 568     -55.029  16.105  17.821  1.00 57.19           C  
-ATOM    233  CG  ASP A 568     -55.494  15.676  19.201  1.00 65.32           C  
-ATOM    234  OD1 ASP A 568     -55.024  16.283  20.193  1.00 61.30           O  
-ATOM    235  OD2 ASP A 568     -56.310  14.735  19.300  1.00 69.62           O  
-ATOM    236  N   LEU A 569     -54.067  17.932  15.536  1.00 59.96           N  
-ATOM    237  CA  LEU A 569     -53.398  18.118  14.258  1.00 56.66           C  
-ATOM    238  C   LEU A 569     -52.187  19.054  14.384  1.00 55.95           C  
-ATOM    239  O   LEU A 569     -51.086  18.754  13.912  1.00 54.29           O  
-ATOM    240  CB  LEU A 569     -54.398  18.654  13.244  1.00 63.40           C  
-ATOM    241  CG  LEU A 569     -53.842  19.101  11.889  1.00 68.54           C  
-ATOM    242  CD1 LEU A 569     -53.372  17.898  11.062  1.00 65.26           C  
-ATOM    243  CD2 LEU A 569     -54.892  19.913  11.142  1.00 64.12           C  
-ATOM    244  N   GLU A 570     -52.378  20.183  15.045  1.00 57.27           N  
-ATOM    245  CA  GLU A 570     -51.274  21.119  15.205  1.00 60.96           C  
-ATOM    246  C   GLU A 570     -50.091  20.542  15.994  1.00 58.45           C  
-ATOM    247  O   GLU A 570     -48.943  20.965  15.818  1.00 57.56           O  
-ATOM    248  CB  GLU A 570     -51.760  22.410  15.854  1.00 61.49           C  
-ATOM    249  CG  GLU A 570     -52.911  23.077  15.109  1.00 64.62           C  
-ATOM    250  CD  GLU A 570     -53.566  24.181  15.931  1.00 72.19           C  
-ATOM    251  OE1 GLU A 570     -54.420  23.860  16.802  1.00 64.95           O  
-ATOM    252  OE2 GLU A 570     -53.208  25.362  15.712  1.00 68.48           O  
-ATOM    253  N   THR A 571     -50.355  19.585  16.871  1.00 50.80           N  
-ATOM    254  CA  THR A 571     -49.250  18.968  17.579  1.00 55.76           C  
-ATOM    255  C   THR A 571     -48.513  18.036  16.609  1.00 53.60           C  
-ATOM    256  O   THR A 571     -47.280  17.993  16.555  1.00 51.99           O  
-ATOM    257  CB  THR A 571     -49.720  18.268  18.877  1.00 56.79           C  
-ATOM    258  OG1 THR A 571     -50.482  17.098  18.562  1.00 55.68           O  
-ATOM    259  CG2 THR A 571     -50.586  19.224  19.692  1.00 54.17           C  
-ATOM    260  N   ALA A 572     -49.291  17.338  15.802  1.00 52.22           N  
-ATOM    261  CA  ALA A 572     -48.750  16.498  14.747  1.00 54.66           C  
-ATOM    262  C   ALA A 572     -47.784  17.255  13.854  1.00 54.61           C  
-ATOM    263  O   ALA A 572     -46.727  16.749  13.481  1.00 55.61           O  
-ATOM    264  CB  ALA A 572     -49.874  15.929  13.927  1.00 59.23           C  
-ATOM    265  N   LEU A 573     -48.153  18.475  13.509  1.00 55.13           N  
-ATOM    266  CA  LEU A 573     -47.334  19.275  12.620  1.00 54.11           C  
-ATOM    267  C   LEU A 573     -46.109  19.773  13.338  1.00 54.18           C  
-ATOM    268  O   LEU A 573     -45.014  19.818  12.777  1.00 53.67           O  
-ATOM    269  CB  LEU A 573     -48.157  20.444  12.103  1.00 60.73           C  
-ATOM    270  CG  LEU A 573     -49.240  19.974  11.134  1.00 60.92           C  
-ATOM    271  CD1 LEU A 573     -50.344  21.013  10.934  1.00 57.11           C  
-ATOM    272  CD2 LEU A 573     -48.581  19.558   9.811  1.00 59.92           C  
-ATOM    273  N   CYS A 574     -46.301  20.155  14.594  1.00 56.60           N  
-ATOM    274  CA  CYS A 574     -45.190  20.584  15.428  1.00 55.75           C  
-ATOM    275  C   CYS A 574     -44.176  19.475  15.512  1.00 54.05           C  
-ATOM    276  O   CYS A 574     -42.962  19.699  15.494  1.00 53.60           O  
-ATOM    277  CB  CYS A 574     -45.685  20.911  16.826  1.00 57.99           C  
-ATOM    278  SG  CYS A 574     -46.487  22.529  16.954  1.00 59.22           S  
-ATOM    279  N   THR A 575     -44.682  18.260  15.603  1.00 52.69           N  
-ATOM    280  CA  THR A 575     -43.794  17.129  15.710  1.00 54.09           C  
-ATOM    281  C   THR A 575     -43.029  16.901  14.407  1.00 56.68           C  
-ATOM    282  O   THR A 575     -41.805  16.711  14.426  1.00 56.31           O  
-ATOM    283  CB  THR A 575     -44.550  15.904  16.146  1.00 50.09           C  
-ATOM    284  OG1 THR A 575     -45.212  16.212  17.375  1.00 53.58           O  
-ATOM    285  CG2 THR A 575     -43.596  14.759  16.372  1.00 48.38           C  
-ATOM    286  N   ILE A 576     -43.727  16.949  13.277  1.00 51.54           N  
-ATOM    287  CA  ILE A 576     -43.026  16.844  12.017  1.00 50.07           C  
-ATOM    288  C   ILE A 576     -41.981  17.933  11.891  1.00 54.12           C  
-ATOM    289  O   ILE A 576     -40.879  17.703  11.398  1.00 54.38           O  
-ATOM    290  CB  ILE A 576     -43.947  16.973  10.836  1.00 55.94           C  
-ATOM    291  CG1 ILE A 576     -44.818  15.720  10.721  1.00 57.72           C  
-ATOM    292  CG2 ILE A 576     -43.112  17.173   9.580  1.00 49.52           C  
-ATOM    293  CD1 ILE A 576     -45.998  15.892   9.810  1.00 59.60           C  
-ATOM    294  N   ARG A 577     -42.327  19.130  12.336  1.00 53.29           N  
-ATOM    295  CA  ARG A 577     -41.386  20.225  12.240  1.00 52.33           C  
-ATOM    296  C   ARG A 577     -40.115  19.929  13.046  1.00 56.11           C  
-ATOM    297  O   ARG A 577     -39.008  20.349  12.671  1.00 57.64           O  
-ATOM    298  CB  ARG A 577     -42.052  21.543  12.649  1.00 49.50           C  
-ATOM    299  CG  ARG A 577     -41.089  22.701  12.842  1.00 52.92           C  
-ATOM    300  CD  ARG A 577     -40.229  22.955  11.602  1.00 60.19           C  
-ATOM    301  NE  ARG A 577     -41.041  23.136  10.394  1.00 65.82           N  
-ATOM    302  CZ  ARG A 577     -40.564  23.127   9.151  1.00 57.55           C  
-ATOM    303  NH1 ARG A 577     -39.272  22.935   8.934  1.00 52.30           N  
-ATOM    304  NH2 ARG A 577     -41.388  23.302   8.128  1.00 56.73           N  
-ATOM    305  N   MET A 578     -40.266  19.188  14.142  1.00 53.08           N  
-ATOM    306  CA  MET A 578     -39.128  18.896  14.997  1.00 53.87           C  
-ATOM    307  C   MET A 578     -38.148  17.948  14.322  1.00 57.64           C  
-ATOM    308  O   MET A 578     -36.919  18.132  14.375  1.00 57.90           O  
-ATOM    309  CB  MET A 578     -39.596  18.293  16.312  1.00 58.75           C  
-ATOM    310  CG  MET A 578     -40.321  19.268  17.213  1.00 59.92           C  
-ATOM    311  SD  MET A 578     -40.897  18.440  18.696  1.00 58.81           S  
-ATOM    312  CE  MET A 578     -42.392  19.374  19.014  1.00 51.30           C  
-ATOM    313  N   PHE A 579     -38.694  16.923  13.689  1.00 52.85           N  
-ATOM    314  CA  PHE A 579     -37.851  15.979  12.992  1.00 56.70           C  
-ATOM    315  C   PHE A 579     -37.160  16.684  11.855  1.00 58.81           C  
-ATOM    316  O   PHE A 579     -35.983  16.441  11.586  1.00 61.44           O  
-ATOM    317  CB  PHE A 579     -38.665  14.813  12.448  1.00 56.39           C  
-ATOM    318  CG  PHE A 579     -38.930  13.718  13.456  1.00 59.16           C  
-ATOM    319  CD1 PHE A 579     -40.037  13.775  14.293  1.00 58.33           C  
-ATOM    320  CD2 PHE A 579     -38.086  12.611  13.540  1.00 58.23           C  
-ATOM    321  CE1 PHE A 579     -40.296  12.755  15.198  1.00 57.49           C  
-ATOM    322  CE2 PHE A 579     -38.336  11.588  14.434  1.00 51.51           C  
-ATOM    323  CZ  PHE A 579     -39.441  11.663  15.271  1.00 56.74           C  
-ATOM    324  N   THR A 580     -37.894  17.567  11.189  1.00 57.15           N  
-ATOM    325  CA  THR A 580     -37.376  18.215  10.002  1.00 57.12           C  
-ATOM    326  C   THR A 580     -36.236  19.161  10.332  1.00 61.84           C  
-ATOM    327  O   THR A 580     -35.203  19.139   9.677  1.00 65.70           O  
-ATOM    328  CB  THR A 580     -38.465  18.963   9.258  1.00 61.37           C  
-ATOM    329  OG1 THR A 580     -39.542  18.063   8.979  1.00 59.46           O  
-ATOM    330  CG2 THR A 580     -37.920  19.538   7.949  1.00 59.89           C  
-ATOM    331  N   ASP A 581     -36.405  19.977  11.364  1.00 64.86           N  
-ATOM    332  CA  ASP A 581     -35.388  20.978  11.690  1.00 62.91           C  
-ATOM    333  C   ASP A 581     -34.174  20.410  12.386  1.00 61.22           C  
-ATOM    334  O   ASP A 581     -33.143  21.063  12.488  1.00 64.34           O  
-ATOM    335  CB  ASP A 581     -35.992  22.115  12.516  1.00 66.23           C  
-ATOM    336  CG  ASP A 581     -36.400  23.310  11.652  1.00 71.83           C  
-ATOM    337  OD1 ASP A 581     -37.044  23.103  10.586  1.00 63.24           O  
-ATOM    338  OD2 ASP A 581     -36.058  24.453  12.043  1.00 75.95           O  
-ATOM    339  N   LEU A 582     -34.308  19.192  12.884  1.00 65.50           N  
-ATOM    340  CA  LEU A 582     -33.192  18.509  13.520  1.00 66.23           C  
-ATOM    341  C   LEU A 582     -32.367  17.729  12.497  1.00 69.15           C  
-ATOM    342  O   LEU A 582     -31.315  17.179  12.835  1.00 70.18           O  
-ATOM    343  CB  LEU A 582     -33.700  17.587  14.620  1.00 62.65           C  
-ATOM    344  CG  LEU A 582     -33.920  18.325  15.936  1.00 62.44           C  
-ATOM    345  CD1 LEU A 582     -34.598  17.421  16.957  1.00 50.77           C  
-ATOM    346  CD2 LEU A 582     -32.597  18.895  16.457  1.00 58.01           C  
-ATOM    347  N   ASN A 583     -32.857  17.698  11.257  1.00 61.96           N  
-ATOM    348  CA  ASN A 583     -32.155  17.102  10.129  1.00 64.32           C  
-ATOM    349  C   ASN A 583     -32.387  15.627  10.057  1.00 68.97           C  
-ATOM    350  O   ASN A 583     -31.645  14.913   9.388  1.00 70.80           O  
-ATOM    351  CB  ASN A 583     -30.653  17.361  10.189  1.00 64.95           C  
-ATOM    352  CG  ASN A 583     -30.300  18.756   9.776  1.00 73.26           C  
-ATOM    353  OD1 ASN A 583     -30.880  19.291   8.823  1.00 73.72           O  
-ATOM    354  ND2 ASN A 583     -29.365  19.376  10.499  1.00 73.62           N  
-ATOM    355  N   LEU A 584     -33.421  15.173  10.750  1.00 69.52           N  
-ATOM    356  CA  LEU A 584     -33.691  13.749  10.849  1.00 65.46           C  
-ATOM    357  C   LEU A 584     -34.333  13.194   9.591  1.00 64.36           C  
-ATOM    358  O   LEU A 584     -34.030  12.074   9.196  1.00 69.22           O  
-ATOM    359  CB  LEU A 584     -34.555  13.452  12.068  1.00 62.81           C  
-ATOM    360  CG  LEU A 584     -33.975  14.011  13.367  1.00 63.91           C  
-ATOM    361  CD1 LEU A 584     -34.795  13.490  14.541  1.00 58.17           C  
-ATOM    362  CD2 LEU A 584     -32.485  13.650  13.502  1.00 57.27           C  
-ATOM    363  N   VAL A 585     -35.209  13.964   8.955  1.00 62.85           N  
-ATOM    364  CA  VAL A 585     -35.861  13.485   7.735  1.00 65.90           C  
-ATOM    365  C   VAL A 585     -34.833  13.378   6.610  1.00 62.04           C  
-ATOM    366  O   VAL A 585     -34.773  12.397   5.878  1.00 61.21           O  
-ATOM    367  CB  VAL A 585     -37.019  14.404   7.308  1.00 62.43           C  
-ATOM    368  CG1 VAL A 585     -37.571  13.976   5.949  1.00 58.06           C  
-ATOM    369  CG2 VAL A 585     -38.118  14.407   8.370  1.00 59.45           C  
-ATOM    370  N   GLN A 586     -34.015  14.411   6.513  1.00 65.09           N  
-ATOM    371  CA  GLN A 586     -32.885  14.459   5.605  1.00 66.66           C  
-ATOM    372  C   GLN A 586     -31.934  13.272   5.763  1.00 67.92           C  
-ATOM    373  O   GLN A 586     -31.894  12.379   4.910  1.00 67.47           O  
-ATOM    374  CB  GLN A 586     -32.116  15.758   5.839  1.00 66.93           C  
-ATOM    375  CG  GLN A 586     -30.777  15.828   5.141  1.00 70.36           C  
-ATOM    376  CD  GLN A 586     -30.882  15.539   3.652  1.00 73.52           C  
-ATOM    377  OE1 GLN A 586     -31.922  15.787   3.018  1.00 67.47           O  
-ATOM    378  NE2 GLN A 586     -29.807  14.989   3.089  1.00 71.41           N  
-ATOM    379  N   ASN A 587     -31.179  13.272   6.859  1.00 64.44           N  
-ATOM    380  CA  ASN A 587     -30.115  12.300   7.079  1.00 65.22           C  
-ATOM    381  C   ASN A 587     -30.521  10.829   7.140  1.00 64.75           C  
-ATOM    382  O   ASN A 587     -29.655   9.964   7.217  1.00 67.76           O  
-ATOM    383  CB  ASN A 587     -29.334  12.642   8.345  1.00 66.01           C  
-ATOM    384  CG  ASN A 587     -28.651  13.983   8.261  1.00 69.30           C  
-ATOM    385  OD1 ASN A 587     -28.526  14.561   7.185  1.00 73.55           O  
-ATOM    386  ND2 ASN A 587     -28.189  14.483   9.400  1.00 70.61           N  
-ATOM    387  N   PHE A 588     -31.814  10.539   7.120  1.00 59.14           N  
-ATOM    388  CA  PHE A 588     -32.261   9.163   7.282  1.00 61.32           C  
-ATOM    389  C   PHE A 588     -33.407   8.827   6.340  1.00 66.89           C  
-ATOM    390  O   PHE A 588     -34.073   7.789   6.488  1.00 63.84           O  
-ATOM    391  CB  PHE A 588     -32.636   8.873   8.745  1.00 59.74           C  
-ATOM    392  CG  PHE A 588     -31.537   9.191   9.710  1.00 65.77           C  
-ATOM    393  CD1 PHE A 588     -31.637  10.280  10.567  1.00 62.22           C  
-ATOM    394  CD2 PHE A 588     -30.372   8.430   9.727  1.00 60.99           C  
-ATOM    395  CE1 PHE A 588     -30.606  10.589  11.433  1.00 62.13           C  
-ATOM    396  CE2 PHE A 588     -29.344   8.737  10.593  1.00 59.13           C  
-ATOM    397  CZ  PHE A 588     -29.460   9.822  11.445  1.00 61.16           C  
-ATOM    398  N   GLN A 589     -33.635   9.724   5.386  1.00 64.65           N  
-ATOM    399  CA  GLN A 589     -34.516   9.450   4.261  1.00 64.16           C  
-ATOM    400  C   GLN A 589     -35.868   8.905   4.717  1.00 66.79           C  
-ATOM    401  O   GLN A 589     -36.260   7.796   4.337  1.00 65.00           O  
-ATOM    402  CB  GLN A 589     -33.831   8.463   3.311  1.00 61.86           C  
-ATOM    403  CG  GLN A 589     -32.321   8.739   3.108  1.00 65.80           C  
-ATOM    404  CD  GLN A 589     -31.478   7.466   3.047  1.00 67.58           C  
-ATOM    405  N   MET A 590     -36.578   9.681   5.534  1.00 64.72           N  
-ATOM    406  CA  MET A 590     -37.901   9.258   5.977  1.00 69.35           C  
-ATOM    407  C   MET A 590     -38.981   9.696   4.988  1.00 64.73           C  
-ATOM    408  O   MET A 590     -39.125  10.871   4.689  1.00 65.61           O  
-ATOM    409  CB  MET A 590     -38.226   9.777   7.388  1.00 65.04           C  
-ATOM    410  CG  MET A 590     -37.115   9.581   8.431  1.00 66.50           C  
-ATOM    411  SD  MET A 590     -37.532  10.247  10.083  1.00 64.51           S  
-ATOM    412  CE  MET A 590     -36.010  10.003  10.984  1.00 57.48           C  
-ATOM    413  N   LYS A 591     -39.734   8.733   4.481  1.00 62.26           N  
-ATOM    414  CA  LYS A 591     -40.887   9.038   3.661  1.00 65.57           C  
-ATOM    415  C   LYS A 591     -41.968   9.737   4.494  1.00 73.79           C  
-ATOM    416  O   LYS A 591     -42.385   9.259   5.559  1.00 71.10           O  
-ATOM    417  CB  LYS A 591     -41.439   7.769   2.994  1.00 73.28           C  
-ATOM    418  CG  LYS A 591     -40.492   7.124   1.957  1.00 73.49           C  
-ATOM    419  N   HIS A 592     -42.419  10.877   3.984  1.00 77.12           N  
-ATOM    420  CA  HIS A 592     -43.425  11.702   4.633  1.00 67.85           C  
-ATOM    421  C   HIS A 592     -44.624  10.910   5.171  1.00 64.72           C  
-ATOM    422  O   HIS A 592     -45.037  11.106   6.305  1.00 61.39           O  
-ATOM    423  CB  HIS A 592     -43.894  12.776   3.650  1.00 70.85           C  
-ATOM    424  CG  HIS A 592     -44.582  13.933   4.299  1.00 75.75           C  
-ATOM    425  ND1 HIS A 592     -43.902  14.897   5.014  1.00 75.82           N  
-ATOM    426  CD2 HIS A 592     -45.892  14.275   4.352  1.00 70.69           C  
-ATOM    427  CE1 HIS A 592     -44.765  15.784   5.482  1.00 74.46           C  
-ATOM    428  NE2 HIS A 592     -45.979  15.430   5.093  1.00 77.37           N  
-ATOM    429  N   GLU A 593     -45.192  10.028   4.359  1.00 65.73           N  
-ATOM    430  CA  GLU A 593     -46.362   9.261   4.791  1.00 68.60           C  
-ATOM    431  C   GLU A 593     -46.000   8.353   5.962  1.00 64.38           C  
-ATOM    432  O   GLU A 593     -46.836   8.060   6.830  1.00 60.78           O  
-ATOM    433  CB  GLU A 593     -46.935   8.413   3.637  1.00 64.38           C  
-ATOM    434  N   VAL A 594     -44.755   7.890   5.967  1.00 57.02           N  
-ATOM    435  CA  VAL A 594     -44.323   6.977   7.008  1.00 61.41           C  
-ATOM    436  C   VAL A 594     -44.182   7.742   8.317  1.00 59.11           C  
-ATOM    437  O   VAL A 594     -44.749   7.354   9.329  1.00 61.78           O  
-ATOM    438  CB  VAL A 594     -42.995   6.286   6.650  1.00 66.97           C  
-ATOM    439  CG1 VAL A 594     -42.633   5.246   7.701  1.00 60.81           C  
-ATOM    440  CG2 VAL A 594     -43.094   5.653   5.279  1.00 61.44           C  
-ATOM    441  N   LEU A 595     -43.432   8.834   8.292  1.00 55.23           N  
-ATOM    442  CA  LEU A 595     -43.344   9.699   9.452  1.00 55.28           C  
-ATOM    443  C   LEU A 595     -44.721  10.038  10.039  1.00 59.98           C  
-ATOM    444  O   LEU A 595     -44.958   9.853  11.242  1.00 58.55           O  
-ATOM    445  CB  LEU A 595     -42.597  10.973   9.096  1.00 53.97           C  
-ATOM    446  CG  LEU A 595     -42.442  11.936  10.266  1.00 55.72           C  
-ATOM    447  CD1 LEU A 595     -42.091  11.157  11.505  1.00 53.03           C  
-ATOM    448  CD2 LEU A 595     -41.394  13.013   9.977  1.00 56.31           C  
-ATOM    449  N   CYS A 596     -45.625  10.520   9.190  1.00 57.32           N  
-ATOM    450  CA  CYS A 596     -46.949  10.941   9.637  1.00 58.53           C  
-ATOM    451  C   CYS A 596     -47.691   9.791  10.288  1.00 59.04           C  
-ATOM    452  O   CYS A 596     -48.343   9.946  11.327  1.00 59.03           O  
-ATOM    453  CB  CYS A 596     -47.788  11.484   8.466  1.00 59.19           C  
-ATOM    454  SG  CYS A 596     -47.198  13.050   7.735  1.00 63.20           S  
-ATOM    455  N   ARG A 597     -47.608   8.634   9.653  1.00 56.93           N  
-ATOM    456  CA  ARG A 597     -48.322   7.463  10.135  1.00 61.03           C  
-ATOM    457  C   ARG A 597     -47.717   7.081  11.501  1.00 59.97           C  
-ATOM    458  O   ARG A 597     -48.426   6.719  12.455  1.00 54.91           O  
-ATOM    459  CB  ARG A 597     -48.208   6.338   9.092  1.00 61.11           C  
-ATOM    460  CG  ARG A 597     -49.289   5.260   9.153  1.00 68.08           C  
-ATOM    461  CD  ARG A 597     -49.085   4.179   8.067  1.00 73.77           C  
-ATOM    462  NE  ARG A 597     -49.154   4.703   6.697  1.00 67.89           N  
-ATOM    463  N   TRP A 598     -46.398   7.209  11.598  1.00 54.92           N  
-ATOM    464  CA  TRP A 598     -45.711   6.887  12.830  1.00 56.45           C  
-ATOM    465  C   TRP A 598     -46.214   7.750  13.972  1.00 54.78           C  
-ATOM    466  O   TRP A 598     -46.485   7.257  15.056  1.00 53.20           O  
-ATOM    467  CB  TRP A 598     -44.190   7.031  12.681  1.00 59.49           C  
-ATOM    468  CG  TRP A 598     -43.460   6.707  13.980  1.00 57.29           C  
-ATOM    469  CD1 TRP A 598     -43.183   5.469  14.473  1.00 53.72           C  
-ATOM    470  CD2 TRP A 598     -42.954   7.639  14.938  1.00 58.71           C  
-ATOM    471  NE1 TRP A 598     -42.527   5.564  15.656  1.00 54.37           N  
-ATOM    472  CE2 TRP A 598     -42.374   6.887  15.977  1.00 59.81           C  
-ATOM    473  CE3 TRP A 598     -42.933   9.040  15.020  1.00 56.43           C  
-ATOM    474  CZ2 TRP A 598     -41.781   7.488  17.100  1.00 56.90           C  
-ATOM    475  CZ3 TRP A 598     -42.341   9.633  16.127  1.00 56.74           C  
-ATOM    476  CH2 TRP A 598     -41.773   8.857  17.154  1.00 54.90           C  
-ATOM    477  N   ILE A 599     -46.331   9.043  13.709  1.00 57.15           N  
-ATOM    478  CA  ILE A 599     -46.842  10.001  14.677  1.00 54.11           C  
-ATOM    479  C   ILE A 599     -48.310   9.784  15.043  1.00 53.97           C  
-ATOM    480  O   ILE A 599     -48.686   9.834  16.216  1.00 57.36           O  
-ATOM    481  CB  ILE A 599     -46.697  11.412  14.146  1.00 56.46           C  
-ATOM    482  CG1 ILE A 599     -45.218  11.735  13.931  1.00 51.00           C  
-ATOM    483  CG2 ILE A 599     -47.401  12.416  15.081  1.00 54.39           C  
-ATOM    484  CD1 ILE A 599     -44.985  13.057  13.269  1.00 48.22           C  
-ATOM    485  N   LEU A 600     -49.158   9.549  14.059  1.00 52.28           N  
-ATOM    486  CA  LEU A 600     -50.540   9.269  14.407  1.00 56.65           C  
-ATOM    487  C   LEU A 600     -50.606   8.038  15.300  1.00 55.52           C  
-ATOM    488  O   LEU A 600     -51.449   7.935  16.184  1.00 55.04           O  
-ATOM    489  CB  LEU A 600     -51.402   9.100  13.161  1.00 58.37           C  
-ATOM    490  CG  LEU A 600     -51.579  10.417  12.399  1.00 68.69           C  
-ATOM    491  CD1 LEU A 600     -52.567  10.301  11.232  1.00 71.41           C  
-ATOM    492  CD2 LEU A 600     -52.017  11.514  13.356  1.00 61.88           C  
-ATOM    493  N   SER A 601     -49.689   7.113  15.074  1.00 54.19           N  
-ATOM    494  CA  SER A 601     -49.675   5.891  15.836  1.00 54.16           C  
-ATOM    495  C   SER A 601     -49.262   6.170  17.256  1.00 55.49           C  
-ATOM    496  O   SER A 601     -49.879   5.679  18.209  1.00 55.89           O  
-ATOM    497  CB  SER A 601     -48.702   4.888  15.221  1.00 56.67           C  
-ATOM    498  OG  SER A 601     -49.290   4.254  14.109  1.00 61.35           O  
-ATOM    499  N   VAL A 602     -48.195   6.941  17.404  1.00 49.86           N  
-ATOM    500  CA  VAL A 602     -47.695   7.184  18.730  1.00 49.08           C  
-ATOM    501  C   VAL A 602     -48.814   7.847  19.511  1.00 52.79           C  
-ATOM    502  O   VAL A 602     -49.184   7.410  20.599  1.00 54.32           O  
-ATOM    503  CB  VAL A 602     -46.462   8.071  18.712  1.00 53.06           C  
-ATOM    504  CG1 VAL A 602     -46.152   8.562  20.136  1.00 50.47           C  
-ATOM    505  CG2 VAL A 602     -45.273   7.323  18.100  1.00 49.86           C  
-ATOM    506  N   LYS A 603     -49.379   8.885  18.915  1.00 53.52           N  
-ATOM    507  CA  LYS A 603     -50.438   9.649  19.537  1.00 53.48           C  
-ATOM    508  C   LYS A 603     -51.631   8.771  19.919  1.00 53.80           C  
-ATOM    509  O   LYS A 603     -52.197   8.907  21.009  1.00 51.38           O  
-ATOM    510  CB  LYS A 603     -50.846  10.767  18.586  1.00 54.58           C  
-ATOM    511  CG  LYS A 603     -52.008  11.626  19.049  1.00 54.47           C  
-ATOM    512  CD  LYS A 603     -52.088  12.845  18.139  1.00 57.98           C  
-ATOM    513  CE  LYS A 603     -53.509  13.314  17.971  1.00 66.34           C  
-ATOM    514  NZ  LYS A 603     -54.353  12.331  17.258  1.00 67.79           N  
-ATOM    515  N   LYS A 604     -51.980   7.850  19.028  1.00 52.01           N  
-ATOM    516  CA  LYS A 604     -53.128   6.975  19.211  1.00 51.25           C  
-ATOM    517  C   LYS A 604     -52.937   6.080  20.422  1.00 56.47           C  
-ATOM    518  O   LYS A 604     -53.905   5.674  21.067  1.00 59.78           O  
-ATOM    519  CB  LYS A 604     -53.323   6.113  17.953  1.00 57.81           C  
-ATOM    520  CG  LYS A 604     -54.538   5.174  17.964  1.00 54.12           C  
-ATOM    521  N   ASN A 605     -51.682   5.763  20.720  1.00 55.05           N  
-ATOM    522  CA  ASN A 605     -51.371   4.832  21.792  1.00 54.09           C  
-ATOM    523  C   ASN A 605     -51.078   5.489  23.128  1.00 56.97           C  
-ATOM    524  O   ASN A 605     -50.519   4.870  24.020  1.00 60.43           O  
-ATOM    525  CB  ASN A 605     -50.231   3.899  21.393  1.00 56.88           C  
-ATOM    526  CG  ASN A 605     -50.717   2.746  20.560  1.00 67.88           C  
-ATOM    527  OD1 ASN A 605     -51.079   1.692  21.099  1.00 72.42           O  
-ATOM    528  ND2 ASN A 605     -50.777   2.946  19.234  1.00 63.89           N  
-ATOM    529  N   TYR A 606     -51.441   6.752  23.261  1.00 55.31           N  
-ATOM    530  CA  TYR A 606     -51.559   7.329  24.574  1.00 51.53           C  
-ATOM    531  C   TYR A 606     -53.044   7.305  24.878  1.00 54.84           C  
-ATOM    532  O   TYR A 606     -53.852   7.312  23.953  1.00 55.41           O  
-ATOM    533  CB  TYR A 606     -50.978   8.740  24.594  1.00 50.60           C  
-ATOM    534  CG  TYR A 606     -49.466   8.766  24.689  1.00 50.71           C  
-ATOM    535  CD1 TYR A 606     -48.828   8.671  25.928  1.00 46.26           C  
-ATOM    536  CD2 TYR A 606     -48.674   8.891  23.554  1.00 49.35           C  
-ATOM    537  CE1 TYR A 606     -47.464   8.701  26.035  1.00 43.38           C  
-ATOM    538  CE2 TYR A 606     -47.277   8.913  23.654  1.00 47.07           C  
-ATOM    539  CZ  TYR A 606     -46.688   8.809  24.901  1.00 47.34           C  
-ATOM    540  OH  TYR A 606     -45.321   8.826  25.030  1.00 46.95           O  
-ATOM    541  N   ARG A 607     -53.408   7.242  26.159  1.00 58.00           N  
-ATOM    542  CA  ARG A 607     -54.819   7.263  26.558  1.00 61.18           C  
-ATOM    543  C   ARG A 607     -55.320   8.675  26.890  1.00 69.32           C  
-ATOM    544  O   ARG A 607     -54.755   9.347  27.760  1.00 68.50           O  
-ATOM    545  CB  ARG A 607     -55.031   6.352  27.765  1.00 69.17           C  
-ATOM    546  CG  ARG A 607     -54.905   4.884  27.435  1.00 70.44           C  
-ATOM    547  CD  ARG A 607     -54.581   4.039  28.648  1.00 70.36           C  
-ATOM    548  NE  ARG A 607     -54.312   2.670  28.234  1.00 75.92           N  
-ATOM    549  CZ  ARG A 607     -55.239   1.836  27.764  1.00 81.81           C  
-ATOM    550  NH1 ARG A 607     -56.503   2.227  27.657  1.00 79.27           N  
-ATOM    551  NH2 ARG A 607     -54.901   0.606  27.404  1.00 85.44           N  
-ATOM    552  N   LYS A 608     -56.377   9.123  26.209  1.00 71.84           N  
-ATOM    553  CA  LYS A 608     -56.945  10.449  26.478  1.00 69.47           C  
-ATOM    554  C   LYS A 608     -57.557  10.517  27.885  1.00 72.04           C  
-ATOM    555  O   LYS A 608     -57.470  11.545  28.557  1.00 69.04           O  
-ATOM    556  CB  LYS A 608     -57.977  10.836  25.413  1.00 68.91           C  
-ATOM    557  CG  LYS A 608     -57.887  12.299  24.953  1.00 74.93           C  
-ATOM    558  N   ASN A 609     -58.144   9.405  28.327  1.00 68.63           N  
-ATOM    559  CA  ASN A 609     -58.760   9.305  29.650  1.00 71.45           C  
-ATOM    560  C   ASN A 609     -57.810   9.522  30.858  1.00 72.80           C  
-ATOM    561  O   ASN A 609     -58.254   9.609  32.006  1.00 69.82           O  
-ATOM    562  CB  ASN A 609     -59.541   7.978  29.778  1.00 76.77           C  
-ATOM    563  CG  ASN A 609     -58.720   6.748  29.343  1.00 82.34           C  
-ATOM    564  OD1 ASN A 609     -58.668   6.382  28.148  1.00 77.31           O  
-ATOM    565  ND2 ASN A 609     -58.094   6.093  30.323  1.00 77.35           N  
-ATOM    566  N   VAL A 610     -56.511   9.626  30.598  1.00 69.06           N  
-ATOM    567  CA  VAL A 610     -55.538   9.873  31.659  1.00 62.23           C  
-ATOM    568  C   VAL A 610     -55.160  11.350  31.686  1.00 61.37           C  
-ATOM    569  O   VAL A 610     -54.666  11.882  30.698  1.00 60.29           O  
-ATOM    570  CB  VAL A 610     -54.272   9.027  31.456  1.00 64.10           C  
-ATOM    571  CG1 VAL A 610     -53.268   9.266  32.588  1.00 62.57           C  
-ATOM    572  CG2 VAL A 610     -54.640   7.549  31.357  1.00 65.53           C  
-ATOM    573  N   ALA A 611     -55.383  12.005  32.822  1.00 59.74           N  
-ATOM    574  CA  ALA A 611     -55.323  13.463  32.898  1.00 55.47           C  
-ATOM    575  C   ALA A 611     -53.969  14.102  32.534  1.00 61.35           C  
-ATOM    576  O   ALA A 611     -53.911  15.069  31.770  1.00 57.43           O  
-ATOM    577  CB  ALA A 611     -55.782  13.934  34.265  1.00 59.96           C  
-ATOM    578  N   TYR A 612     -52.881  13.585  33.087  1.00 59.36           N  
-ATOM    579  CA  TYR A 612     -51.585  14.169  32.782  1.00 57.19           C  
-ATOM    580  C   TYR A 612     -50.782  13.343  31.786  1.00 55.80           C  
-ATOM    581  O   TYR A 612     -50.336  13.849  30.751  1.00 57.89           O  
-ATOM    582  CB  TYR A 612     -50.767  14.354  34.058  1.00 55.42           C  
-ATOM    583  CG  TYR A 612     -49.382  14.885  33.798  1.00 51.24           C  
-ATOM    584  CD1 TYR A 612     -49.189  16.154  33.266  1.00 46.86           C  
-ATOM    585  CD2 TYR A 612     -48.267  14.114  34.083  1.00 54.26           C  
-ATOM    586  CE1 TYR A 612     -47.925  16.641  33.032  1.00 47.44           C  
-ATOM    587  CE2 TYR A 612     -46.998  14.584  33.856  1.00 54.85           C  
-ATOM    588  CZ  TYR A 612     -46.826  15.843  33.329  1.00 58.18           C  
-ATOM    589  OH  TYR A 612     -45.537  16.292  33.127  1.00 65.99           O  
-ATOM    590  N   HIS A 613     -50.571  12.079  32.126  1.00 55.49           N  
-ATOM    591  CA  HIS A 613     -49.678  11.229  31.353  1.00 56.47           C  
-ATOM    592  C   HIS A 613     -50.355  10.781  30.059  1.00 54.99           C  
-ATOM    593  O   HIS A 613     -50.877   9.680  29.962  1.00 54.75           O  
-ATOM    594  CB  HIS A 613     -49.194  10.033  32.181  1.00 52.98           C  
-ATOM    595  CG  HIS A 613     -48.115  10.374  33.164  1.00 53.80           C  
-ATOM    596  ND1 HIS A 613     -48.328  10.404  34.525  1.00 55.27           N  
-ATOM    597  CD2 HIS A 613     -46.815  10.698  32.982  1.00 57.40           C  
-ATOM    598  CE1 HIS A 613     -47.210  10.744  35.139  1.00 56.94           C  
-ATOM    599  NE2 HIS A 613     -46.274  10.923  34.225  1.00 60.20           N  
-ATOM    600  N   ASN A 614     -50.323  11.653  29.059  1.00 53.01           N  
-ATOM    601  CA  ASN A 614     -50.961  11.382  27.790  1.00 48.44           C  
-ATOM    602  C   ASN A 614     -50.161  12.020  26.678  1.00 47.32           C  
-ATOM    603  O   ASN A 614     -49.105  12.598  26.922  1.00 46.92           O  
-ATOM    604  CB  ASN A 614     -52.365  11.951  27.813  1.00 49.59           C  
-ATOM    605  CG  ASN A 614     -52.389  13.360  28.340  1.00 51.11           C  
-ATOM    606  OD1 ASN A 614     -51.640  14.229  27.873  1.00 50.26           O  
-ATOM    607  ND2 ASN A 614     -53.214  13.589  29.350  1.00 51.46           N  
-ATOM    608  N   TRP A 615     -50.671  11.922  25.458  1.00 43.03           N  
-ATOM    609  CA  TRP A 615     -49.993  12.495  24.323  1.00 41.46           C  
-ATOM    610  C   TRP A 615     -49.468  13.909  24.575  1.00 46.69           C  
-ATOM    611  O   TRP A 615     -48.343  14.234  24.184  1.00 47.35           O  
-ATOM    612  CB  TRP A 615     -50.917  12.490  23.110  1.00 46.65           C  
-ATOM    613  CG  TRP A 615     -50.422  13.361  22.021  1.00 46.61           C  
-ATOM    614  CD1 TRP A 615     -51.005  14.496  21.550  1.00 45.61           C  
-ATOM    615  CD2 TRP A 615     -49.207  13.196  21.289  1.00 50.33           C  
-ATOM    616  NE1 TRP A 615     -50.237  15.041  20.557  1.00 48.39           N  
-ATOM    617  CE2 TRP A 615     -49.123  14.263  20.377  1.00 51.73           C  
-ATOM    618  CE3 TRP A 615     -48.182  12.240  21.307  1.00 51.65           C  
-ATOM    619  CZ2 TRP A 615     -48.053  14.402  19.478  1.00 56.43           C  
-ATOM    620  CZ3 TRP A 615     -47.114  12.382  20.413  1.00 52.26           C  
-ATOM    621  CH2 TRP A 615     -47.060  13.455  19.516  1.00 51.54           C  
-ATOM    622  N   ARG A 616     -50.262  14.761  25.220  1.00 44.82           N  
-ATOM    623  CA  ARG A 616     -49.823  16.141  25.378  1.00 45.69           C  
-ATOM    624  C   ARG A 616     -48.542  16.223  26.191  1.00 45.38           C  
-ATOM    625  O   ARG A 616     -47.665  17.051  25.919  1.00 45.87           O  
-ATOM    626  CB  ARG A 616     -50.918  17.015  25.971  1.00 45.48           C  
-ATOM    627  CG  ARG A 616     -52.129  17.196  25.069  1.00 47.79           C  
-ATOM    628  CD  ARG A 616     -51.721  17.707  23.672  1.00 53.30           C  
-ATOM    629  NE  ARG A 616     -52.867  17.856  22.770  1.00 58.90           N  
-ATOM    630  CZ  ARG A 616     -53.275  19.019  22.262  1.00 55.01           C  
-ATOM    631  NH1 ARG A 616     -52.627  20.136  22.562  1.00 51.29           N  
-ATOM    632  NH2 ARG A 616     -54.327  19.065  21.458  1.00 47.98           N  
-ATOM    633  N   HIS A 617     -48.415  15.337  27.172  1.00 46.60           N  
-ATOM    634  CA  HIS A 617     -47.213  15.312  28.002  1.00 42.84           C  
-ATOM    635  C   HIS A 617     -46.020  14.806  27.204  1.00 45.24           C  
-ATOM    636  O   HIS A 617     -44.911  15.327  27.318  1.00 41.83           O  
-ATOM    637  CB  HIS A 617     -47.430  14.450  29.242  1.00 48.44           C  
-ATOM    638  CG  HIS A 617     -46.158  14.038  29.902  1.00 49.12           C  
-ATOM    639  ND1 HIS A 617     -45.245  14.946  30.384  1.00 45.71           N  
-ATOM    640  CD2 HIS A 617     -45.624  12.818  30.121  1.00 52.08           C  
-ATOM    641  CE1 HIS A 617     -44.209  14.306  30.882  1.00 45.03           C  
-ATOM    642  NE2 HIS A 617     -44.417  13.012  30.743  1.00 51.85           N  
-ATOM    643  N   ALA A 618     -46.266  13.794  26.376  1.00 45.02           N  
-ATOM    644  CA  ALA A 618     -45.226  13.240  25.529  1.00 42.61           C  
-ATOM    645  C   ALA A 618     -44.789  14.275  24.525  1.00 42.58           C  
-ATOM    646  O   ALA A 618     -43.594  14.402  24.224  1.00 43.78           O  
-ATOM    647  CB  ALA A 618     -45.717  12.004  24.817  1.00 45.16           C  
-ATOM    648  N   PHE A 619     -45.770  15.011  24.012  1.00 43.20           N  
-ATOM    649  CA  PHE A 619     -45.514  16.048  23.032  1.00 44.60           C  
-ATOM    650  C   PHE A 619     -44.667  17.154  23.633  1.00 45.50           C  
-ATOM    651  O   PHE A 619     -43.713  17.610  23.014  1.00 45.24           O  
-ATOM    652  CB  PHE A 619     -46.820  16.613  22.489  1.00 47.08           C  
-ATOM    653  CG  PHE A 619     -46.630  17.801  21.601  1.00 50.05           C  
-ATOM    654  CD1 PHE A 619     -45.881  17.698  20.434  1.00 51.50           C  
-ATOM    655  CD2 PHE A 619     -47.195  19.028  21.927  1.00 47.62           C  
-ATOM    656  CE1 PHE A 619     -45.699  18.802  19.601  1.00 54.83           C  
-ATOM    657  CE2 PHE A 619     -47.012  20.139  21.097  1.00 52.35           C  
-ATOM    658  CZ  PHE A 619     -46.267  20.026  19.936  1.00 49.25           C  
-ATOM    659  N   ASN A 620     -45.000  17.551  24.859  1.00 44.24           N  
-ATOM    660  CA  ASN A 620     -44.221  18.548  25.574  1.00 42.52           C  
-ATOM    661  C   ASN A 620     -42.809  18.119  25.925  1.00 41.93           C  
-ATOM    662  O   ASN A 620     -41.856  18.892  25.816  1.00 43.98           O  
-ATOM    663  CB  ASN A 620     -44.991  19.006  26.803  1.00 42.93           C  
-ATOM    664  CG  ASN A 620     -45.996  20.093  26.460  1.00 46.20           C  
-ATOM    665  OD1 ASN A 620     -45.629  21.128  25.898  1.00 51.36           O  
-ATOM    666  ND2 ASN A 620     -47.257  19.843  26.729  1.00 38.94           N  
-ATOM    667  N   THR A 621     -42.672  16.871  26.336  1.00 42.23           N  
-ATOM    668  CA  THR A 621     -41.360  16.323  26.593  1.00 41.92           C  
-ATOM    669  C   THR A 621     -40.460  16.445  25.375  1.00 44.77           C  
-ATOM    670  O   THR A 621     -39.318  16.921  25.493  1.00 44.39           O  
-ATOM    671  CB  THR A 621     -41.452  14.884  27.044  1.00 41.74           C  
-ATOM    672  OG1 THR A 621     -42.405  14.810  28.105  1.00 47.24           O  
-ATOM    673  CG2 THR A 621     -40.104  14.398  27.546  1.00 39.81           C  
-ATOM    674  N   ALA A 622     -40.972  16.046  24.206  1.00 41.99           N  
-ATOM    675  CA  ALA A 622     -40.206  16.186  22.963  1.00 42.94           C  
-ATOM    676  C   ALA A 622     -39.911  17.642  22.576  1.00 47.31           C  
-ATOM    677  O   ALA A 622     -38.790  17.962  22.161  1.00 46.21           O  
-ATOM    678  CB  ALA A 622     -40.877  15.463  21.834  1.00 44.29           C  
-ATOM    679  N   GLN A 623     -40.903  18.522  22.719  1.00 43.79           N  
-ATOM    680  CA  GLN A 623     -40.695  19.931  22.434  1.00 43.64           C  
-ATOM    681  C   GLN A 623     -39.598  20.488  23.342  1.00 45.55           C  
-ATOM    682  O   GLN A 623     -38.713  21.224  22.907  1.00 43.42           O  
-ATOM    683  CB  GLN A 623     -42.000  20.705  22.605  1.00 47.33           C  
-ATOM    684  CG  GLN A 623     -41.920  22.202  22.303  1.00 46.28           C  
-ATOM    685  CD  GLN A 623     -41.255  23.008  23.403  1.00 45.65           C  
-ATOM    686  OE1 GLN A 623     -41.536  22.821  24.592  1.00 48.93           O  
-ATOM    687  NE2 GLN A 623     -40.378  23.923  23.011  1.00 45.91           N  
-ATOM    688  N   CYS A 624     -39.629  20.112  24.612  1.00 44.71           N  
-ATOM    689  CA  CYS A 624     -38.548  20.547  25.477  1.00 47.40           C  
-ATOM    690  C   CYS A 624     -37.192  19.969  25.066  1.00 47.80           C  
-ATOM    691  O   CYS A 624     -36.165  20.623  25.200  1.00 47.25           O  
-ATOM    692  CB  CYS A 624     -38.837  20.218  26.925  1.00 47.37           C  
-ATOM    693  SG  CYS A 624     -37.460  20.761  27.942  1.00 59.83           S  
-ATOM    694  N   MET A 625     -37.193  18.731  24.583  1.00 49.18           N  
-ATOM    695  CA  MET A 625     -35.979  18.142  24.028  1.00 51.71           C  
-ATOM    696  C   MET A 625     -35.473  19.017  22.884  1.00 49.52           C  
-ATOM    697  O   MET A 625     -34.314  19.439  22.841  1.00 50.31           O  
-ATOM    698  CB  MET A 625     -36.243  16.711  23.533  1.00 49.60           C  
-ATOM    699  CG  MET A 625     -34.982  15.989  23.004  1.00 49.19           C  
-ATOM    700  SD  MET A 625     -33.684  15.772  24.254  1.00 56.40           S  
-ATOM    701  CE  MET A 625     -34.507  14.691  25.423  1.00 50.64           C  
-ATOM    702  N   PHE A 626     -36.372  19.293  21.961  1.00 48.02           N  
-ATOM    703  CA  PHE A 626     -36.056  20.131  20.828  1.00 52.74           C  
-ATOM    704  C   PHE A 626     -35.434  21.460  21.264  1.00 56.48           C  
-ATOM    705  O   PHE A 626     -34.375  21.858  20.784  1.00 56.90           O  
-ATOM    706  CB  PHE A 626     -37.325  20.386  20.028  1.00 53.64           C  
-ATOM    707  CG  PHE A 626     -37.087  21.123  18.767  1.00 56.69           C  
-ATOM    708  CD1 PHE A 626     -36.689  20.446  17.626  1.00 55.94           C  
-ATOM    709  CD2 PHE A 626     -37.239  22.494  18.718  1.00 59.84           C  
-ATOM    710  CE1 PHE A 626     -36.444  21.115  16.457  1.00 60.59           C  
-ATOM    711  CE2 PHE A 626     -37.001  23.188  17.540  1.00 64.69           C  
-ATOM    712  CZ  PHE A 626     -36.603  22.499  16.405  1.00 64.38           C  
-ATOM    713  N   ALA A 627     -36.097  22.146  22.182  1.00 54.22           N  
-ATOM    714  CA  ALA A 627     -35.630  23.453  22.595  1.00 55.69           C  
-ATOM    715  C   ALA A 627     -34.255  23.344  23.224  1.00 55.53           C  
-ATOM    716  O   ALA A 627     -33.405  24.187  23.004  1.00 57.61           O  
-ATOM    717  CB  ALA A 627     -36.630  24.106  23.562  1.00 55.47           C  
-ATOM    718  N   ALA A 628     -34.036  22.293  24.005  1.00 55.80           N  
-ATOM    719  CA  ALA A 628     -32.742  22.100  24.648  1.00 58.49           C  
-ATOM    720  C   ALA A 628     -31.681  21.770  23.602  1.00 60.94           C  
-ATOM    721  O   ALA A 628     -30.499  22.012  23.809  1.00 62.39           O  
-ATOM    722  CB  ALA A 628     -32.813  21.010  25.730  1.00 51.32           C  
-ATOM    723  N   LEU A 629     -32.108  21.219  22.472  1.00 61.02           N  
-ATOM    724  CA  LEU A 629     -31.170  20.923  21.392  1.00 63.34           C  
-ATOM    725  C   LEU A 629     -30.806  22.166  20.590  1.00 64.81           C  
-ATOM    726  O   LEU A 629     -29.630  22.410  20.322  1.00 67.53           O  
-ATOM    727  CB  LEU A 629     -31.706  19.820  20.477  1.00 59.08           C  
-ATOM    728  CG  LEU A 629     -31.645  18.449  21.158  1.00 64.27           C  
-ATOM    729  CD1 LEU A 629     -32.256  17.346  20.291  1.00 61.07           C  
-ATOM    730  CD2 LEU A 629     -30.220  18.104  21.575  1.00 58.75           C  
-ATOM    731  N   LYS A 630     -31.816  22.948  20.221  1.00 62.71           N  
-ATOM    732  CA  LYS A 630     -31.616  24.156  19.426  1.00 63.39           C  
-ATOM    733  C   LYS A 630     -31.286  25.363  20.302  1.00 62.77           C  
-ATOM    734  O   LYS A 630     -30.140  25.786  20.384  1.00 66.20           O  
-ATOM    735  CB  LYS A 630     -32.850  24.443  18.567  1.00 65.62           C  
-ATOM    736  CG  LYS A 630     -33.147  23.391  17.498  1.00 64.23           C  
-ATOM    737  CD  LYS A 630     -32.035  23.302  16.466  1.00 66.62           C  
-ATOM    738  CE  LYS A 630     -32.535  22.652  15.160  1.00 72.78           C  
-ATOM    739  NZ  LYS A 630     -31.459  22.429  14.119  1.00 70.81           N  
-ATOM    740  N   ALA A 631     -32.291  25.917  20.965  1.00 67.46           N  
-ATOM    741  CA  ALA A 631     -32.069  27.063  21.846  1.00 64.71           C  
-ATOM    742  C   ALA A 631     -31.035  26.750  22.939  1.00 65.72           C  
-ATOM    743  O   ALA A 631     -30.186  27.579  23.262  1.00 68.30           O  
-ATOM    744  CB  ALA A 631     -33.403  27.543  22.453  1.00 63.08           C  
-ATOM    745  N   GLY A 632     -31.098  25.541  23.492  1.00 68.59           N  
-ATOM    746  CA  GLY A 632     -30.185  25.131  24.551  1.00 69.21           C  
-ATOM    747  C   GLY A 632     -28.793  24.781  24.053  1.00 69.64           C  
-ATOM    748  O   GLY A 632     -27.910  24.457  24.856  1.00 67.41           O  
-ATOM    749  N   LYS A 633     -28.608  24.843  22.731  1.00 66.28           N  
-ATOM    750  CA  LYS A 633     -27.315  24.596  22.096  1.00 70.06           C  
-ATOM    751  C   LYS A 633     -26.682  23.279  22.552  1.00 74.06           C  
-ATOM    752  O   LYS A 633     -25.511  23.252  22.946  1.00 78.98           O  
-ATOM    753  CB  LYS A 633     -26.353  25.769  22.345  1.00 70.52           C  
-ATOM    754  CG  LYS A 633     -26.688  27.032  21.544  1.00 74.12           C  
-ATOM    755  CD  LYS A 633     -25.789  28.213  21.912  1.00 74.75           C  
-ATOM    756  N   ILE A 634     -27.459  22.197  22.493  1.00 69.08           N  
-ATOM    757  CA  ILE A 634     -26.996  20.876  22.917  1.00 68.59           C  
-ATOM    758  C   ILE A 634     -26.811  19.958  21.701  1.00 70.65           C  
-ATOM    759  O   ILE A 634     -26.031  19.004  21.726  1.00 69.64           O  
-ATOM    760  CB  ILE A 634     -27.965  20.255  23.945  1.00 64.88           C  
-ATOM    761  CG1 ILE A 634     -27.800  20.958  25.293  1.00 67.94           C  
-ATOM    762  CG2 ILE A 634     -27.721  18.757  24.091  1.00 64.01           C  
-ATOM    763  CD1 ILE A 634     -28.806  20.554  26.338  1.00 63.42           C  
-ATOM    764  N   GLN A 635     -27.532  20.274  20.635  1.00 65.81           N  
-ATOM    765  CA  GLN A 635     -27.372  19.607  19.352  1.00 71.46           C  
-ATOM    766  C   GLN A 635     -25.910  19.334  18.990  1.00 75.55           C  
-ATOM    767  O   GLN A 635     -25.566  18.245  18.515  1.00 74.06           O  
-ATOM    768  CB  GLN A 635     -27.984  20.488  18.277  1.00 67.04           C  
-ATOM    769  CG  GLN A 635     -28.055  19.884  16.920  1.00 68.22           C  
-ATOM    770  CD  GLN A 635     -28.812  20.796  15.987  1.00 72.88           C  
-ATOM    771  OE1 GLN A 635     -28.863  22.013  16.210  1.00 74.03           O  
-ATOM    772  NE2 GLN A 635     -29.428  20.224  14.956  1.00 65.31           N  
-ATOM    773  N   ASN A 636     -25.058  20.334  19.205  1.00 74.47           N  
-ATOM    774  CA  ASN A 636     -23.674  20.278  18.743  1.00 75.94           C  
-ATOM    775  C   ASN A 636     -22.757  19.522  19.705  1.00 77.85           C  
-ATOM    776  O   ASN A 636     -21.543  19.469  19.514  1.00 84.27           O  
-ATOM    777  CB  ASN A 636     -23.135  21.689  18.456  1.00 72.38           C  
-ATOM    778  N   LYS A 637     -23.338  18.929  20.739  1.00 74.11           N  
-ATOM    779  CA  LYS A 637     -22.564  18.080  21.637  1.00 74.98           C  
-ATOM    780  C   LYS A 637     -22.852  16.598  21.381  1.00 73.86           C  
-ATOM    781  O   LYS A 637     -22.239  15.726  22.000  1.00 71.35           O  
-ATOM    782  CB  LYS A 637     -22.850  18.433  23.100  1.00 76.13           C  
-ATOM    783  CG  LYS A 637     -22.295  19.793  23.547  1.00 86.07           C  
-ATOM    784  CD  LYS A 637     -22.553  20.067  25.041  1.00 84.49           C  
-ATOM    785  CE  LYS A 637     -21.835  21.331  25.503  1.00 80.36           C  
-ATOM    786  NZ  LYS A 637     -22.204  22.507  24.655  1.00 80.80           N  
-ATOM    787  N   LEU A 638     -23.777  16.328  20.459  1.00 68.05           N  
-ATOM    788  CA  LEU A 638     -24.288  14.982  20.238  1.00 65.42           C  
-ATOM    789  C   LEU A 638     -24.250  14.548  18.764  1.00 67.25           C  
-ATOM    790  O   LEU A 638     -24.168  15.383  17.860  1.00 64.60           O  
-ATOM    791  CB  LEU A 638     -25.727  14.882  20.744  1.00 62.63           C  
-ATOM    792  CG  LEU A 638     -26.049  15.356  22.159  1.00 64.61           C  
-ATOM    793  CD1 LEU A 638     -27.515  15.123  22.461  1.00 57.65           C  
-ATOM    794  CD2 LEU A 638     -25.190  14.667  23.203  1.00 66.87           C  
-ATOM    795  N   THR A 639     -24.326  13.235  18.540  1.00 65.60           N  
-ATOM    796  CA  THR A 639     -24.366  12.670  17.194  1.00 64.52           C  
-ATOM    797  C   THR A 639     -25.793  12.658  16.683  1.00 64.82           C  
-ATOM    798  O   THR A 639     -26.737  12.593  17.472  1.00 64.77           O  
-ATOM    799  CB  THR A 639     -23.792  11.218  17.137  1.00 63.08           C  
-ATOM    800  OG1 THR A 639     -24.678  10.293  17.796  1.00 60.63           O  
-ATOM    801  CG2 THR A 639     -22.415  11.163  17.783  1.00 62.20           C  
-ATOM    802  N   ASP A 640     -25.942  12.735  15.365  1.00 63.67           N  
-ATOM    803  CA  ASP A 640     -27.237  12.575  14.729  1.00 65.31           C  
-ATOM    804  C   ASP A 640     -28.009  11.422  15.333  1.00 59.74           C  
-ATOM    805  O   ASP A 640     -29.202  11.535  15.589  1.00 61.46           O  
-ATOM    806  CB  ASP A 640     -27.077  12.315  13.227  1.00 73.19           C  
-ATOM    807  CG  ASP A 640     -26.799  13.580  12.436  1.00 77.52           C  
-ATOM    808  OD1 ASP A 640     -27.014  14.690  12.980  1.00 77.76           O  
-ATOM    809  OD2 ASP A 640     -26.380  13.456  11.264  1.00 77.17           O  
-ATOM    810  N   LEU A 641     -27.336  10.301  15.542  1.00 58.49           N  
-ATOM    811  CA  LEU A 641     -28.039   9.109  15.995  1.00 61.79           C  
-ATOM    812  C   LEU A 641     -28.565   9.280  17.406  1.00 57.54           C  
-ATOM    813  O   LEU A 641     -29.672   8.843  17.718  1.00 58.30           O  
-ATOM    814  CB  LEU A 641     -27.166   7.856  15.878  1.00 62.99           C  
-ATOM    815  CG  LEU A 641     -26.943   7.375  14.440  1.00 58.91           C  
-ATOM    816  CD1 LEU A 641     -26.087   6.134  14.415  1.00 58.68           C  
-ATOM    817  CD2 LEU A 641     -28.272   7.102  13.772  1.00 58.01           C  
-ATOM    818  N   GLU A 642     -27.774   9.917  18.258  1.00 57.04           N  
-ATOM    819  CA  GLU A 642     -28.229  10.221  19.607  1.00 57.73           C  
-ATOM    820  C   GLU A 642     -29.492  11.073  19.562  1.00 54.84           C  
-ATOM    821  O   GLU A 642     -30.459  10.832  20.277  1.00 56.46           O  
-ATOM    822  CB  GLU A 642     -27.121  10.917  20.393  1.00 57.68           C  
-ATOM    823  CG  GLU A 642     -26.114   9.927  20.945  1.00 64.12           C  
-ATOM    824  CD  GLU A 642     -24.716  10.500  21.132  1.00 68.72           C  
-ATOM    825  OE1 GLU A 642     -24.452  11.615  20.637  1.00 68.18           O  
-ATOM    826  OE2 GLU A 642     -23.878   9.818  21.769  1.00 69.09           O  
-ATOM    827  N   ILE A 643     -29.479  12.058  18.685  1.00 55.67           N  
-ATOM    828  CA  ILE A 643     -30.562  13.013  18.595  1.00 55.65           C  
-ATOM    829  C   ILE A 643     -31.832  12.336  18.117  1.00 53.59           C  
-ATOM    830  O   ILE A 643     -32.912  12.506  18.699  1.00 50.98           O  
-ATOM    831  CB  ILE A 643     -30.175  14.144  17.639  1.00 54.25           C  
-ATOM    832  CG1 ILE A 643     -29.186  15.077  18.337  1.00 57.29           C  
-ATOM    833  CG2 ILE A 643     -31.407  14.872  17.144  1.00 50.74           C  
-ATOM    834  CD1 ILE A 643     -28.282  15.816  17.397  1.00 62.34           C  
-ATOM    835  N   LEU A 644     -31.685  11.567  17.049  1.00 52.45           N  
-ATOM    836  CA  LEU A 644     -32.789  10.828  16.477  1.00 52.37           C  
-ATOM    837  C   LEU A 644     -33.431  10.008  17.591  1.00 50.60           C  
-ATOM    838  O   LEU A 644     -34.651  10.015  17.786  1.00 48.97           O  
-ATOM    839  CB  LEU A 644     -32.255   9.939  15.356  1.00 51.61           C  
-ATOM    840  CG  LEU A 644     -33.153   8.805  14.876  1.00 54.15           C  
-ATOM    841  CD1 LEU A 644     -34.500   9.335  14.433  1.00 50.53           C  
-ATOM    842  CD2 LEU A 644     -32.462   8.053  13.751  1.00 55.36           C  
-ATOM    843  N   ALA A 645     -32.570   9.350  18.354  1.00 50.41           N  
-ATOM    844  CA  ALA A 645     -32.971   8.467  19.427  1.00 49.09           C  
-ATOM    845  C   ALA A 645     -33.647   9.211  20.570  1.00 48.36           C  
-ATOM    846  O   ALA A 645     -34.662   8.768  21.092  1.00 48.42           O  
-ATOM    847  CB  ALA A 645     -31.764   7.720  19.924  1.00 53.22           C  
-ATOM    848  N   LEU A 646     -33.074  10.340  20.966  1.00 49.46           N  
-ATOM    849  CA  LEU A 646     -33.659  11.163  22.015  1.00 48.79           C  
-ATOM    850  C   LEU A 646     -35.043  11.677  21.639  1.00 49.23           C  
-ATOM    851  O   LEU A 646     -35.938  11.758  22.487  1.00 46.33           O  
-ATOM    852  CB  LEU A 646     -32.756  12.348  22.308  1.00 48.40           C  
-ATOM    853  CG  LEU A 646     -31.501  12.053  23.115  1.00 53.58           C  
-ATOM    854  CD1 LEU A 646     -30.643  13.319  23.211  1.00 49.85           C  
-ATOM    855  CD2 LEU A 646     -31.872  11.523  24.511  1.00 51.93           C  
-ATOM    856  N   LEU A 647     -35.224  12.033  20.372  1.00 43.34           N  
-ATOM    857  CA  LEU A 647     -36.492  12.588  19.981  1.00 44.72           C  
-ATOM    858  C   LEU A 647     -37.565  11.513  20.030  1.00 47.59           C  
-ATOM    859  O   LEU A 647     -38.665  11.739  20.535  1.00 46.61           O  
-ATOM    860  CB  LEU A 647     -36.422  13.217  18.591  1.00 49.63           C  
-ATOM    861  CG  LEU A 647     -37.706  14.010  18.305  1.00 53.90           C  
-ATOM    862  CD1 LEU A 647     -37.738  15.224  19.225  1.00 54.52           C  
-ATOM    863  CD2 LEU A 647     -37.862  14.447  16.848  1.00 53.72           C  
-ATOM    864  N   ILE A 648     -37.245  10.341  19.498  1.00 48.19           N  
-ATOM    865  CA  ILE A 648     -38.201   9.249  19.482  1.00 47.35           C  
-ATOM    866  C   ILE A 648     -38.455   8.780  20.898  1.00 43.67           C  
-ATOM    867  O   ILE A 648     -39.591   8.540  21.288  1.00 43.80           O  
-ATOM    868  CB  ILE A 648     -37.687   8.069  18.665  1.00 49.32           C  
-ATOM    869  CG1 ILE A 648     -37.805   8.362  17.182  1.00 47.55           C  
-ATOM    870  CG2 ILE A 648     -38.480   6.817  18.980  1.00 50.27           C  
-ATOM    871  CD1 ILE A 648     -36.675   7.764  16.375  1.00 48.05           C  
-ATOM    872  N   ALA A 649     -37.388   8.630  21.662  1.00 42.37           N  
-ATOM    873  CA  ALA A 649     -37.531   8.305  23.069  1.00 45.94           C  
-ATOM    874  C   ALA A 649     -38.457   9.318  23.748  1.00 44.84           C  
-ATOM    875  O   ALA A 649     -39.385   8.937  24.463  1.00 44.31           O  
-ATOM    876  CB  ALA A 649     -36.167   8.254  23.761  1.00 45.73           C  
-ATOM    877  N   ALA A 650     -38.217  10.605  23.522  1.00 41.63           N  
-ATOM    878  CA  ALA A 650     -39.024  11.636  24.189  1.00 43.86           C  
-ATOM    879  C   ALA A 650     -40.519  11.483  23.890  1.00 42.45           C  
-ATOM    880  O   ALA A 650     -41.357  11.505  24.799  1.00 41.21           O  
-ATOM    881  CB  ALA A 650     -38.523  13.033  23.844  1.00 41.13           C  
-ATOM    882  N   LEU A 651     -40.839  11.291  22.613  1.00 44.74           N  
-ATOM    883  CA  LEU A 651     -42.211  11.044  22.174  1.00 44.22           C  
-ATOM    884  C   LEU A 651     -42.825   9.733  22.681  1.00 44.46           C  
-ATOM    885  O   LEU A 651     -44.035   9.636  22.908  1.00 45.43           O  
-ATOM    886  CB  LEU A 651     -42.265  11.085  20.653  1.00 44.57           C  
-ATOM    887  CG  LEU A 651     -42.034  12.509  20.133  1.00 53.10           C  
-ATOM    888  CD1 LEU A 651     -41.645  12.502  18.655  1.00 53.89           C  
-ATOM    889  CD2 LEU A 651     -43.257  13.439  20.386  1.00 46.86           C  
-ATOM    890  N   SER A 652     -41.986   8.732  22.886  1.00 46.55           N  
-ATOM    891  CA  SER A 652     -42.478   7.402  23.185  1.00 44.83           C  
-ATOM    892  C   SER A 652     -42.453   7.017  24.666  1.00 43.91           C  
-ATOM    893  O   SER A 652     -43.152   6.082  25.041  1.00 43.92           O  
-ATOM    894  CB  SER A 652     -41.691   6.383  22.367  1.00 47.78           C  
-ATOM    895  OG  SER A 652     -41.646   6.755  20.992  1.00 49.06           O  
-ATOM    896  N   HIS A 653     -41.701   7.759  25.490  1.00 39.12           N  
-ATOM    897  CA  HIS A 653     -41.307   7.338  26.854  1.00 41.34           C  
-ATOM    898  C   HIS A 653     -42.406   7.047  27.872  1.00 42.77           C  
-ATOM    899  O   HIS A 653     -42.124   6.530  28.940  1.00 46.82           O  
-ATOM    900  CB  HIS A 653     -40.367   8.363  27.498  1.00 45.35           C  
-ATOM    901  CG  HIS A 653     -41.091   9.525  28.111  1.00 46.43           C  
-ATOM    902  ND1 HIS A 653     -41.388  10.672  27.407  1.00 47.42           N  
-ATOM    903  CD2 HIS A 653     -41.615   9.696  29.344  1.00 43.69           C  
-ATOM    904  CE1 HIS A 653     -42.058  11.501  28.188  1.00 49.58           C  
-ATOM    905  NE2 HIS A 653     -42.212  10.932  29.367  1.00 45.65           N  
-ATOM    906  N   ASP A 654     -43.647   7.399  27.577  1.00 47.05           N  
-ATOM    907  CA  ASP A 654     -44.739   7.014  28.451  1.00 44.30           C  
-ATOM    908  C   ASP A 654     -45.875   6.345  27.669  1.00 45.41           C  
-ATOM    909  O   ASP A 654     -47.010   6.380  28.110  1.00 47.56           O  
-ATOM    910  CB  ASP A 654     -45.293   8.239  29.172  1.00 46.10           C  
-ATOM    911  CG  ASP A 654     -44.545   8.589  30.448  1.00 51.04           C  
-ATOM    912  OD1 ASP A 654     -43.949   7.722  31.147  1.00 55.82           O  
-ATOM    913  OD2 ASP A 654     -44.589   9.783  30.779  1.00 50.61           O  
-ATOM    914  N   LEU A 655     -45.595   5.743  26.518  1.00 46.11           N  
-ATOM    915  CA  LEU A 655     -46.663   5.133  25.698  1.00 50.59           C  
-ATOM    916  C   LEU A 655     -47.607   4.198  26.463  1.00 52.27           C  
-ATOM    917  O   LEU A 655     -47.145   3.328  27.186  1.00 53.96           O  
-ATOM    918  CB  LEU A 655     -46.068   4.361  24.524  1.00 47.58           C  
-ATOM    919  CG  LEU A 655     -45.763   5.115  23.238  1.00 50.58           C  
-ATOM    920  CD1 LEU A 655     -44.696   4.415  22.362  1.00 49.47           C  
-ATOM    921  CD2 LEU A 655     -47.054   5.309  22.488  1.00 49.27           C  
-ATOM    922  N   ASP A 656     -48.918   4.383  26.292  1.00 53.20           N  
-ATOM    923  CA  ASP A 656     -49.943   3.497  26.857  1.00 54.27           C  
-ATOM    924  C   ASP A 656     -49.991   3.537  28.392  1.00 59.62           C  
-ATOM    925  O   ASP A 656     -50.516   2.635  29.040  1.00 62.85           O  
-ATOM    926  CB  ASP A 656     -49.725   2.065  26.352  1.00 62.43           C  
-ATOM    927  CG  ASP A 656     -50.897   1.130  26.656  1.00 66.62           C  
-ATOM    928  OD1 ASP A 656     -52.068   1.528  26.472  1.00 67.33           O  
-ATOM    929  OD2 ASP A 656     -50.632  -0.021  27.067  1.00 67.14           O  
-ATOM    930  N   HIS A 657     -49.441   4.600  28.964  1.00 58.54           N  
-ATOM    931  CA  HIS A 657     -49.482   4.843  30.405  1.00 57.85           C  
-ATOM    932  C   HIS A 657     -50.930   4.989  30.962  1.00 62.99           C  
-ATOM    933  O   HIS A 657     -51.792   5.621  30.362  1.00 62.72           O  
-ATOM    934  CB  HIS A 657     -48.637   6.081  30.701  1.00 53.49           C  
-ATOM    935  CG  HIS A 657     -48.377   6.316  32.155  1.00 55.67           C  
-ATOM    936  ND1 HIS A 657     -47.105   6.470  32.666  1.00 54.22           N  
-ATOM    937  CD2 HIS A 657     -49.224   6.457  33.201  1.00 52.67           C  
-ATOM    938  CE1 HIS A 657     -47.182   6.678  33.968  1.00 55.96           C  
-ATOM    939  NE2 HIS A 657     -48.456   6.681  34.315  1.00 52.50           N  
-ATOM    940  N   ARG A 658     -51.200   4.399  32.117  1.00 65.75           N  
-ATOM    941  CA  ARG A 658     -52.583   4.317  32.579  1.00 70.29           C  
-ATOM    942  C   ARG A 658     -52.892   5.225  33.765  1.00 70.70           C  
-ATOM    943  O   ARG A 658     -53.934   5.094  34.394  1.00 74.73           O  
-ATOM    944  CB  ARG A 658     -52.930   2.875  32.934  1.00 70.74           C  
-ATOM    945  CG  ARG A 658     -53.853   2.218  31.944  1.00 73.35           C  
-ATOM    946  CD  ARG A 658     -53.096   1.401  30.911  1.00 79.58           C  
-ATOM    947  NE  ARG A 658     -54.030   0.620  30.100  1.00 90.22           N  
-ATOM    948  CZ  ARG A 658     -54.372  -0.644  30.345  1.00 91.33           C  
-ATOM    949  NH1 ARG A 658     -53.837  -1.292  31.377  1.00 86.98           N  
-ATOM    950  NH2 ARG A 658     -55.246  -1.260  29.551  1.00 88.88           N  
-ATOM    951  N   GLY A 659     -51.992   6.152  34.057  1.00 68.89           N  
-ATOM    952  CA  GLY A 659     -52.113   6.971  35.243  1.00 67.72           C  
-ATOM    953  C   GLY A 659     -51.405   6.303  36.402  1.00 70.25           C  
-ATOM    954  O   GLY A 659     -51.533   5.092  36.593  1.00 72.68           O  
-ATOM    955  N   VAL A 660     -50.670   7.099  37.176  1.00 69.72           N  
-ATOM    956  CA  VAL A 660     -49.876   6.608  38.308  1.00 77.06           C  
-ATOM    957  C   VAL A 660     -50.611   5.682  39.294  1.00 83.21           C  
-ATOM    958  O   VAL A 660     -49.985   4.871  39.983  1.00 84.39           O  
-ATOM    959  CB  VAL A 660     -49.300   7.780  39.110  1.00 72.75           C  
-ATOM    960  CG1 VAL A 660     -48.232   8.505  38.295  1.00 69.76           C  
-ATOM    961  CG2 VAL A 660     -50.423   8.722  39.526  1.00 71.31           C  
-ATOM    962  N   ASN A 661     -51.930   5.812  39.370  1.00 81.60           N  
-ATOM    963  CA  ASN A 661     -52.715   4.995  40.284  1.00 84.51           C  
-ATOM    964  C   ASN A 661     -53.314   3.739  39.635  1.00 89.31           C  
-ATOM    965  O   ASN A 661     -54.398   3.296  40.016  1.00 91.08           O  
-ATOM    966  CB  ASN A 661     -53.835   5.836  40.922  1.00 85.88           C  
-ATOM    967  CG  ASN A 661     -53.308   6.894  41.887  1.00 86.19           C  
-ATOM    968  OD1 ASN A 661     -52.318   6.680  42.591  1.00 85.18           O  
-ATOM    969  ND2 ASN A 661     -53.982   8.041  41.930  1.00 81.38           N  
-ATOM    970  N   ASN A 662     -52.628   3.157  38.659  1.00 89.61           N  
-ATOM    971  CA  ASN A 662     -53.161   1.946  38.030  1.00 93.91           C  
-ATOM    972  C   ASN A 662     -52.107   0.845  37.815  1.00 98.40           C  
-ATOM    973  O   ASN A 662     -50.944   1.136  37.514  1.00 91.73           O  
-ATOM    974  CB  ASN A 662     -53.926   2.291  36.741  1.00 88.65           C  
-ATOM    975  CG  ASN A 662     -55.004   3.351  36.964  1.00 81.79           C  
-ATOM    976  N   SER A 663     -52.528  -0.413  37.977  1.00103.73           N  
-ATOM    977  CA  SER A 663     -51.598  -1.548  38.066  1.00111.04           C  
-ATOM    978  C   SER A 663     -51.611  -2.518  36.873  1.00115.67           C  
-ATOM    979  O   SER A 663     -52.665  -2.988  36.444  1.00111.82           O  
-ATOM    980  CB  SER A 663     -51.836  -2.328  39.365  1.00105.83           C  
-ATOM    981  N   TYR A 664     -50.420  -2.813  36.355  1.00121.47           N  
-ATOM    982  CA  TYR A 664     -50.234  -3.817  35.312  1.00117.26           C  
-ATOM    983  C   TYR A 664     -49.407  -4.977  35.881  1.00124.01           C  
-ATOM    984  O   TYR A 664     -48.223  -4.810  36.196  1.00116.49           O  
-ATOM    985  CB  TYR A 664     -49.537  -3.202  34.095  1.00103.73           C  
-ATOM    986  N   ILE A 665     -50.038  -6.145  36.012  1.00125.55           N  
-ATOM    987  CA  ILE A 665     -49.429  -7.298  36.678  1.00125.40           C  
-ATOM    988  C   ILE A 665     -48.783  -8.341  35.753  1.00127.64           C  
-ATOM    989  O   ILE A 665     -49.304  -8.657  34.680  1.00122.15           O  
-ATOM    990  N   GLN A 666     -47.646  -8.872  36.199  1.00127.12           N  
-ATOM    991  CA  GLN A 666     -46.907  -9.916  35.489  1.00120.91           C  
-ATOM    992  C   GLN A 666     -45.881 -10.555  36.442  1.00126.86           C  
-ATOM    993  O   GLN A 666     -45.069  -9.856  37.062  1.00120.50           O  
-ATOM    994  N   ARG A 667     -45.927 -11.880  36.566  1.00125.23           N  
-ATOM    995  CA  ARG A 667     -45.023 -12.599  37.465  1.00121.01           C  
-ATOM    996  C   ARG A 667     -44.823 -11.895  38.815  1.00115.04           C  
-ATOM    997  O   ARG A 667     -45.757 -11.772  39.614  1.00109.15           O  
-ATOM    998  N   SER A 668     -43.596 -11.443  39.061  1.00110.29           N  
-ATOM    999  CA  SER A 668     -43.263 -10.760  40.296  1.00105.66           C  
-ATOM   1000  C   SER A 668     -42.161  -9.736  40.106  1.00110.59           C  
-ATOM   1001  O   SER A 668     -41.182  -9.982  39.390  1.00103.54           O  
-ATOM   1002  N   GLU A 669     -42.328  -8.579  40.746  1.00111.04           N  
-ATOM   1003  CA  GLU A 669     -41.339  -7.518  40.695  1.00107.20           C  
-ATOM   1004  C   GLU A 669     -40.941  -7.056  42.084  1.00110.36           C  
-ATOM   1005  O   GLU A 669     -39.968  -7.546  42.663  1.00106.78           O  
-ATOM   1006  N   HIS A 678     -35.601  -3.376  37.273  1.00 95.97           N  
-ATOM   1007  CA  HIS A 678     -37.043  -3.606  37.269  1.00 98.50           C  
-ATOM   1008  C   HIS A 678     -37.800  -2.275  37.175  1.00100.24           C  
-ATOM   1009  O   HIS A 678     -38.555  -1.884  38.083  1.00 96.64           O  
-ATOM   1010  CB  HIS A 678     -37.482  -4.383  38.516  1.00101.07           C  
-ATOM   1011  CG  HIS A 678     -37.674  -3.519  39.725  1.00106.54           C  
-ATOM   1012  ND1 HIS A 678     -36.630  -2.874  40.358  1.00108.78           N  
-ATOM   1013  CD2 HIS A 678     -38.795  -3.174  40.403  1.00106.07           C  
-ATOM   1014  CE1 HIS A 678     -37.098  -2.175  41.376  1.00108.83           C  
-ATOM   1015  NE2 HIS A 678     -38.409  -2.339  41.425  1.00115.61           N  
-ATOM   1016  N   SER A 679     -37.578  -1.562  36.079  1.00 90.45           N  
-ATOM   1017  CA  SER A 679     -38.412  -0.424  35.764  1.00 74.67           C  
-ATOM   1018  C   SER A 679     -39.560  -0.991  34.956  1.00 70.67           C  
-ATOM   1019  O   SER A 679     -39.517  -1.009  33.726  1.00 71.45           O  
-ATOM   1020  CB  SER A 679     -37.624   0.589  34.952  1.00 73.47           C  
-ATOM   1021  OG  SER A 679     -36.431   0.948  35.627  1.00 76.03           O  
-ATOM   1022  N   ILE A 680     -40.566  -1.491  35.663  1.00 67.50           N  
-ATOM   1023  CA  ILE A 680     -41.656  -2.250  35.059  1.00 67.00           C  
-ATOM   1024  C   ILE A 680     -42.300  -1.475  33.945  1.00 65.76           C  
-ATOM   1025  O   ILE A 680     -42.358  -1.923  32.803  1.00 66.39           O  
-ATOM   1026  CB  ILE A 680     -42.803  -2.511  36.060  1.00 73.71           C  
-ATOM   1027  CG1 ILE A 680     -42.323  -2.395  37.520  1.00 83.12           C  
-ATOM   1028  CG2 ILE A 680     -43.519  -3.819  35.730  1.00 63.82           C  
-ATOM   1029  CD1 ILE A 680     -41.201  -3.346  37.901  1.00 88.67           C  
-ATOM   1030  N   MET A 681     -42.811  -0.306  34.313  1.00 66.75           N  
-ATOM   1031  CA  MET A 681     -43.511   0.584  33.403  1.00 62.10           C  
-ATOM   1032  C   MET A 681     -42.712   0.961  32.162  1.00 59.13           C  
-ATOM   1033  O   MET A 681     -43.204   0.859  31.036  1.00 54.35           O  
-ATOM   1034  CB  MET A 681     -43.880   1.853  34.153  1.00 62.35           C  
-ATOM   1035  CG  MET A 681     -45.054   1.682  35.062  1.00 62.57           C  
-ATOM   1036  SD  MET A 681     -46.439   1.087  34.099  1.00 76.04           S  
-ATOM   1037  CE  MET A 681     -46.287  -0.686  34.336  1.00 72.16           C  
-ATOM   1038  N   GLU A 682     -41.484   1.418  32.379  1.00 56.61           N  
-ATOM   1039  CA  GLU A 682     -40.692   1.920  31.288  1.00 53.15           C  
-ATOM   1040  C   GLU A 682     -40.303   0.786  30.330  1.00 59.82           C  
-ATOM   1041  O   GLU A 682     -40.179   0.994  29.113  1.00 58.13           O  
-ATOM   1042  CB  GLU A 682     -39.504   2.773  31.768  1.00 52.47           C  
-ATOM   1043  CG  GLU A 682     -39.227   2.798  33.290  1.00 67.97           C  
-ATOM   1044  CD  GLU A 682     -40.263   3.548  34.143  1.00 66.58           C  
-ATOM   1045  OE1 GLU A 682     -41.037   2.883  34.870  1.00 65.50           O  
-ATOM   1046  OE2 GLU A 682     -40.276   4.796  34.121  1.00 66.72           O  
-ATOM   1047  N   HIS A 683     -40.172  -0.428  30.851  1.00 59.09           N  
-ATOM   1048  CA  HIS A 683     -39.962  -1.559  29.960  1.00 55.92           C  
-ATOM   1049  C   HIS A 683     -41.155  -1.707  29.028  1.00 53.84           C  
-ATOM   1050  O   HIS A 683     -41.009  -1.971  27.829  1.00 57.17           O  
-ATOM   1051  CB  HIS A 683     -39.657  -2.844  30.739  1.00 56.52           C  
-ATOM   1052  CG  HIS A 683     -38.201  -3.014  31.047  1.00 57.19           C  
-ATOM   1053  ND1 HIS A 683     -37.293  -3.466  30.111  1.00 59.64           N  
-ATOM   1054  CD2 HIS A 683     -37.485  -2.740  32.165  1.00 61.41           C  
-ATOM   1055  CE1 HIS A 683     -36.082  -3.481  30.646  1.00 63.14           C  
-ATOM   1056  NE2 HIS A 683     -36.171  -3.042  31.890  1.00 63.10           N  
-ATOM   1057  N   HIS A 684     -42.338  -1.490  29.575  1.00 51.81           N  
-ATOM   1058  CA  HIS A 684     -43.549  -1.599  28.792  1.00 53.86           C  
-ATOM   1059  C   HIS A 684     -43.660  -0.470  27.759  1.00 57.55           C  
-ATOM   1060  O   HIS A 684     -44.105  -0.694  26.631  1.00 57.02           O  
-ATOM   1061  CB  HIS A 684     -44.763  -1.601  29.717  1.00 54.59           C  
-ATOM   1062  CG  HIS A 684     -46.070  -1.715  28.997  1.00 56.57           C  
-ATOM   1063  ND1 HIS A 684     -46.997  -0.695  28.970  1.00 61.43           N  
-ATOM   1064  CD2 HIS A 684     -46.602  -2.724  28.269  1.00 60.18           C  
-ATOM   1065  CE1 HIS A 684     -48.049  -1.074  28.265  1.00 62.47           C  
-ATOM   1066  NE2 HIS A 684     -47.833  -2.302  27.828  1.00 64.34           N  
-ATOM   1067  N   HIS A 685     -43.256   0.741  28.140  1.00 53.88           N  
-ATOM   1068  CA  HIS A 685     -43.344   1.875  27.222  1.00 54.67           C  
-ATOM   1069  C   HIS A 685     -42.443   1.628  26.038  1.00 53.20           C  
-ATOM   1070  O   HIS A 685     -42.812   1.906  24.900  1.00 51.93           O  
-ATOM   1071  CB  HIS A 685     -42.930   3.172  27.904  1.00 52.17           C  
-ATOM   1072  CG  HIS A 685     -43.814   3.555  29.043  1.00 51.39           C  
-ATOM   1073  ND1 HIS A 685     -45.179   3.380  29.007  1.00 52.60           N  
-ATOM   1074  CD2 HIS A 685     -43.531   4.080  30.256  1.00 46.56           C  
-ATOM   1075  CE1 HIS A 685     -45.701   3.789  30.149  1.00 50.09           C  
-ATOM   1076  NE2 HIS A 685     -44.722   4.225  30.921  1.00 49.88           N  
-ATOM   1077  N   PHE A 686     -41.254   1.106  26.324  1.00 54.25           N  
-ATOM   1078  CA  PHE A 686     -40.329   0.705  25.274  1.00 56.07           C  
-ATOM   1079  C   PHE A 686     -40.871  -0.389  24.345  1.00 55.42           C  
-ATOM   1080  O   PHE A 686     -40.690  -0.327  23.135  1.00 49.72           O  
-ATOM   1081  CB  PHE A 686     -38.995   0.247  25.838  1.00 48.08           C  
-ATOM   1082  CG  PHE A 686     -38.084  -0.247  24.785  1.00 56.79           C  
-ATOM   1083  CD1 PHE A 686     -37.520   0.639  23.878  1.00 57.30           C  
-ATOM   1084  CD2 PHE A 686     -37.840  -1.602  24.635  1.00 61.44           C  
-ATOM   1085  CE1 PHE A 686     -36.696   0.188  22.862  1.00 56.90           C  
-ATOM   1086  CE2 PHE A 686     -37.021  -2.060  23.626  1.00 58.59           C  
-ATOM   1087  CZ  PHE A 686     -36.445  -1.160  22.739  1.00 59.28           C  
-ATOM   1088  N   ASP A 687     -41.508  -1.404  24.913  1.00 56.61           N  
-ATOM   1089  CA  ASP A 687     -42.098  -2.433  24.076  1.00 59.85           C  
-ATOM   1090  C   ASP A 687     -43.042  -1.783  23.090  1.00 57.34           C  
-ATOM   1091  O   ASP A 687     -42.939  -1.964  21.868  1.00 56.82           O  
-ATOM   1092  CB  ASP A 687     -42.834  -3.459  24.929  1.00 60.30           C  
-ATOM   1093  CG  ASP A 687     -41.880  -4.414  25.609  1.00 75.80           C  
-ATOM   1094  OD1 ASP A 687     -42.026  -4.655  26.838  1.00 77.38           O  
-ATOM   1095  OD2 ASP A 687     -40.966  -4.909  24.901  1.00 78.68           O  
-ATOM   1096  N   GLN A 688     -43.961  -1.018  23.652  1.00 55.64           N  
-ATOM   1097  CA  GLN A 688     -44.926  -0.255  22.891  1.00 57.41           C  
-ATOM   1098  C   GLN A 688     -44.230   0.534  21.780  1.00 53.96           C  
-ATOM   1099  O   GLN A 688     -44.621   0.483  20.625  1.00 55.40           O  
-ATOM   1100  CB  GLN A 688     -45.674   0.666  23.851  1.00 56.70           C  
-ATOM   1101  CG  GLN A 688     -47.091   0.949  23.444  1.00 66.15           C  
-ATOM   1102  CD  GLN A 688     -47.996  -0.269  23.501  1.00 72.29           C  
-ATOM   1103  OE1 GLN A 688     -47.621  -1.329  24.018  1.00 67.51           O  
-ATOM   1104  NE2 GLN A 688     -49.212  -0.116  22.971  1.00 74.83           N  
-ATOM   1105  N   CYS A 689     -43.166   1.232  22.140  1.00 52.69           N  
-ATOM   1106  CA  CYS A 689     -42.400   2.013  21.187  1.00 51.97           C  
-ATOM   1107  C   CYS A 689     -41.893   1.180  20.006  1.00 55.49           C  
-ATOM   1108  O   CYS A 689     -42.063   1.550  18.831  1.00 54.66           O  
-ATOM   1109  CB  CYS A 689     -41.221   2.654  21.910  1.00 49.57           C  
-ATOM   1110  SG  CYS A 689     -40.058   3.520  20.829  1.00 56.90           S  
-ATOM   1111  N   LEU A 690     -41.249   0.065  20.340  1.00 53.31           N  
-ATOM   1112  CA  LEU A 690     -40.673  -0.839  19.365  1.00 52.74           C  
-ATOM   1113  C   LEU A 690     -41.757  -1.443  18.475  1.00 57.91           C  
-ATOM   1114  O   LEU A 690     -41.612  -1.518  17.246  1.00 54.52           O  
-ATOM   1115  CB  LEU A 690     -39.944  -1.956  20.086  1.00 54.57           C  
-ATOM   1116  CG  LEU A 690     -39.006  -2.774  19.209  1.00 55.08           C  
-ATOM   1117  CD1 LEU A 690     -38.159  -1.834  18.386  1.00 61.36           C  
-ATOM   1118  CD2 LEU A 690     -38.133  -3.657  20.049  1.00 52.50           C  
-ATOM   1119  N   MET A 691     -42.842  -1.885  19.101  1.00 51.46           N  
-ATOM   1120  CA  MET A 691     -43.959  -2.390  18.336  1.00 52.17           C  
-ATOM   1121  C   MET A 691     -44.271  -1.376  17.231  1.00 58.33           C  
-ATOM   1122  O   MET A 691     -44.213  -1.703  16.045  1.00 60.52           O  
-ATOM   1123  CB  MET A 691     -45.160  -2.672  19.250  1.00 56.67           C  
-ATOM   1124  CG  MET A 691     -46.440  -3.125  18.555  1.00 59.30           C  
-ATOM   1125  SD  MET A 691     -47.524  -1.765  18.028  1.00 89.00           S  
-ATOM   1126  CE  MET A 691     -48.321  -1.326  19.587  1.00 72.89           C  
-ATOM   1127  N   ILE A 692     -44.548  -0.136  17.618  1.00 57.90           N  
-ATOM   1128  CA  ILE A 692     -44.864   0.909  16.650  1.00 59.69           C  
-ATOM   1129  C   ILE A 692     -43.779   1.111  15.600  1.00 58.13           C  
-ATOM   1130  O   ILE A 692     -44.072   1.211  14.402  1.00 59.93           O  
-ATOM   1131  CB  ILE A 692     -45.155   2.255  17.330  1.00 58.80           C  
-ATOM   1132  CG1 ILE A 692     -46.499   2.202  18.043  1.00 58.99           C  
-ATOM   1133  CG2 ILE A 692     -45.168   3.388  16.310  1.00 54.44           C  
-ATOM   1134  CD1 ILE A 692     -46.692   3.336  19.014  1.00 57.77           C  
-ATOM   1135  N   LEU A 693     -42.531   1.183  16.041  1.00 54.05           N  
-ATOM   1136  CA  LEU A 693     -41.438   1.376  15.098  1.00 55.97           C  
-ATOM   1137  C   LEU A 693     -41.418   0.285  14.043  1.00 58.73           C  
-ATOM   1138  O   LEU A 693     -41.035   0.531  12.904  1.00 61.36           O  
-ATOM   1139  CB  LEU A 693     -40.109   1.384  15.828  1.00 56.88           C  
-ATOM   1140  CG  LEU A 693     -39.849   2.726  16.478  1.00 57.93           C  
-ATOM   1141  CD1 LEU A 693     -38.630   2.660  17.385  1.00 51.99           C  
-ATOM   1142  CD2 LEU A 693     -39.680   3.739  15.370  1.00 54.53           C  
-ATOM   1143  N   ASN A 694     -41.828  -0.918  14.447  1.00 60.74           N  
-ATOM   1144  CA  ASN A 694     -41.816  -2.105  13.599  1.00 60.83           C  
-ATOM   1145  C   ASN A 694     -43.111  -2.383  12.866  1.00 63.62           C  
-ATOM   1146  O   ASN A 694     -43.207  -3.395  12.178  1.00 66.48           O  
-ATOM   1147  CB  ASN A 694     -41.496  -3.334  14.432  1.00 55.46           C  
-ATOM   1148  CG  ASN A 694     -40.033  -3.496  14.661  1.00 62.12           C  
-ATOM   1149  OD1 ASN A 694     -39.220  -3.031  13.867  1.00 65.97           O  
-ATOM   1150  ND2 ASN A 694     -39.675  -4.141  15.761  1.00 61.54           N  
-ATOM   1151  N   SER A 695     -44.114  -1.525  13.037  1.00 56.33           N  
-ATOM   1152  CA  SER A 695     -45.363  -1.688  12.308  1.00 58.96           C  
-ATOM   1153  C   SER A 695     -45.221  -1.310  10.832  1.00 65.49           C  
-ATOM   1154  O   SER A 695     -44.488  -0.381  10.474  1.00 63.28           O  
-ATOM   1155  CB  SER A 695     -46.470  -0.877  12.957  1.00 60.24           C  
-ATOM   1156  OG  SER A 695     -46.642  -1.312  14.291  1.00 64.86           O  
-ATOM   1157  N   PRO A 696     -45.906  -2.062   9.962  1.00 69.26           N  
-ATOM   1158  CA  PRO A 696     -45.962  -1.742   8.532  1.00 67.45           C  
-ATOM   1159  C   PRO A 696     -46.438  -0.308   8.297  1.00 64.30           C  
-ATOM   1160  O   PRO A 696     -47.499   0.092   8.786  1.00 65.14           O  
-ATOM   1161  CB  PRO A 696     -46.994  -2.739   8.000  1.00 61.20           C  
-ATOM   1162  CG  PRO A 696     -46.881  -3.910   8.923  1.00 62.18           C  
-ATOM   1163  CD  PRO A 696     -46.551  -3.351  10.274  1.00 63.13           C  
-ATOM   1164  N   GLY A 697     -45.645   0.465   7.568  1.00 60.14           N  
-ATOM   1165  CA  GLY A 697     -46.047   1.808   7.207  1.00 62.19           C  
-ATOM   1166  C   GLY A 697     -45.516   2.840   8.161  1.00 66.75           C  
-ATOM   1167  O   GLY A 697     -45.507   4.035   7.854  1.00 69.32           O  
-ATOM   1168  N   ASN A 698     -45.054   2.366   9.315  1.00 67.03           N  
-ATOM   1169  CA  ASN A 698     -44.623   3.239  10.397  1.00 62.14           C  
-ATOM   1170  C   ASN A 698     -43.139   3.211  10.644  1.00 61.55           C  
-ATOM   1171  O   ASN A 698     -42.675   3.807  11.595  1.00 59.75           O  
-ATOM   1172  CB  ASN A 698     -45.319   2.843  11.690  1.00 58.44           C  
-ATOM   1173  CG  ASN A 698     -46.788   3.099  11.639  1.00 62.84           C  
-ATOM   1174  OD1 ASN A 698     -47.538   2.341  11.031  1.00 71.07           O  
-ATOM   1175  ND2 ASN A 698     -47.219   4.184  12.260  1.00 59.33           N  
-ATOM   1176  N   GLN A 699     -42.390   2.521   9.796  1.00 59.65           N  
-ATOM   1177  CA  GLN A 699     -40.990   2.262  10.102  1.00 60.82           C  
-ATOM   1178  C   GLN A 699     -40.009   3.379   9.776  1.00 57.73           C  
-ATOM   1179  O   GLN A 699     -39.174   3.233   8.894  1.00 56.88           O  
-ATOM   1180  CB  GLN A 699     -40.557   0.972   9.433  1.00 60.53           C  
-ATOM   1181  CG  GLN A 699     -41.429  -0.167   9.854  1.00 63.90           C  
-ATOM   1182  CD  GLN A 699     -41.042  -1.457   9.190  1.00 70.77           C  
-ATOM   1183  OE1 GLN A 699     -39.918  -1.605   8.676  1.00 62.72           O  
-ATOM   1184  NE2 GLN A 699     -41.975  -2.413   9.187  1.00 72.19           N  
-ATOM   1185  N   ILE A 700     -40.075   4.466  10.531  1.00 55.97           N  
-ATOM   1186  CA  ILE A 700     -39.208   5.609  10.289  1.00 55.58           C  
-ATOM   1187  C   ILE A 700     -37.721   5.310  10.444  1.00 57.40           C  
-ATOM   1188  O   ILE A 700     -36.896   6.209  10.298  1.00 53.44           O  
-ATOM   1189  CB  ILE A 700     -39.548   6.782  11.212  1.00 54.22           C  
-ATOM   1190  CG1 ILE A 700     -39.569   6.299  12.671  1.00 58.98           C  
-ATOM   1191  CG2 ILE A 700     -40.882   7.387  10.818  1.00 55.81           C  
-ATOM   1192  CD1 ILE A 700     -39.433   7.424  13.704  1.00 56.33           C  
-ATOM   1193  N   LEU A 701     -37.355   4.068  10.744  1.00 58.27           N  
-ATOM   1194  CA  LEU A 701     -35.922   3.770  10.845  1.00 58.57           C  
-ATOM   1195  C   LEU A 701     -35.408   2.917   9.688  1.00 60.49           C  
-ATOM   1196  O   LEU A 701     -34.208   2.644   9.590  1.00 62.17           O  
-ATOM   1197  CB  LEU A 701     -35.577   3.137  12.198  1.00 61.51           C  
-ATOM   1198  CG  LEU A 701     -35.895   3.960  13.457  1.00 57.40           C  
-ATOM   1199  CD1 LEU A 701     -35.451   3.213  14.708  1.00 52.35           C  
-ATOM   1200  CD2 LEU A 701     -35.228   5.319  13.393  1.00 53.32           C  
-ATOM   1201  N   SER A 702     -36.323   2.512   8.810  1.00 54.99           N  
-ATOM   1202  CA  SER A 702     -35.977   1.719   7.645  1.00 52.49           C  
-ATOM   1203  C   SER A 702     -34.704   2.208   6.962  1.00 56.53           C  
-ATOM   1204  O   SER A 702     -33.937   1.413   6.437  1.00 59.50           O  
-ATOM   1205  CB  SER A 702     -37.120   1.736   6.643  1.00 53.98           C  
-ATOM   1206  OG  SER A 702     -37.195   3.001   6.022  1.00 60.90           O  
-ATOM   1207  N   GLY A 703     -34.469   3.510   6.977  1.00 54.97           N  
-ATOM   1208  CA  GLY A 703     -33.332   4.067   6.273  1.00 54.24           C  
-ATOM   1209  C   GLY A 703     -31.961   3.913   6.900  1.00 59.09           C  
-ATOM   1210  O   GLY A 703     -30.972   4.368   6.326  1.00 60.25           O  
-ATOM   1211  N   LEU A 704     -31.883   3.288   8.072  1.00 58.73           N  
-ATOM   1212  CA  LEU A 704     -30.599   3.097   8.736  1.00 52.52           C  
-ATOM   1213  C   LEU A 704     -30.046   1.707   8.433  1.00 58.77           C  
-ATOM   1214  O   LEU A 704     -30.804   0.733   8.311  1.00 57.53           O  
-ATOM   1215  CB  LEU A 704     -30.759   3.233  10.247  1.00 59.53           C  
-ATOM   1216  CG  LEU A 704     -31.177   4.525  10.949  1.00 57.64           C  
-ATOM   1217  CD1 LEU A 704     -32.516   5.038  10.456  1.00 59.76           C  
-ATOM   1218  CD2 LEU A 704     -31.215   4.275  12.445  1.00 52.56           C  
-ATOM   1219  N   SER A 705     -28.724   1.608   8.331  1.00 56.69           N  
-ATOM   1220  CA  SER A 705     -28.054   0.311   8.264  1.00 56.90           C  
-ATOM   1221  C   SER A 705     -28.357  -0.471   9.545  1.00 62.17           C  
-ATOM   1222  O   SER A 705     -28.823   0.114  10.522  1.00 64.99           O  
-ATOM   1223  CB  SER A 705     -26.557   0.530   8.160  1.00 55.94           C  
-ATOM   1224  OG  SER A 705     -26.052   1.111   9.349  1.00 61.73           O  
-ATOM   1225  N   ILE A 706     -28.091  -1.774   9.575  1.00 62.27           N  
-ATOM   1226  CA  ILE A 706     -28.296  -2.518  10.831  1.00 63.68           C  
-ATOM   1227  C   ILE A 706     -27.431  -1.962  11.962  1.00 59.42           C  
-ATOM   1228  O   ILE A 706     -27.870  -1.899  13.107  1.00 60.10           O  
-ATOM   1229  CB  ILE A 706     -27.977  -4.043  10.727  1.00 63.23           C  
-ATOM   1230  CG1 ILE A 706     -27.920  -4.506   9.282  1.00 60.59           C  
-ATOM   1231  CG2 ILE A 706     -28.984  -4.867  11.542  1.00 59.45           C  
-ATOM   1232  N   GLU A 707     -26.197  -1.585  11.642  1.00 53.99           N  
-ATOM   1233  CA  GLU A 707     -25.277  -1.125  12.662  1.00 58.24           C  
-ATOM   1234  C   GLU A 707     -25.874   0.103  13.337  1.00 60.55           C  
-ATOM   1235  O   GLU A 707     -26.076   0.131  14.548  1.00 58.22           O  
-ATOM   1236  CB  GLU A 707     -23.909  -0.810  12.058  1.00 53.71           C  
-ATOM   1237  N   GLU A 708     -26.175   1.111  12.529  1.00 62.00           N  
-ATOM   1238  CA  GLU A 708     -26.856   2.303  13.008  1.00 61.90           C  
-ATOM   1239  C   GLU A 708     -28.130   1.956  13.771  1.00 56.91           C  
-ATOM   1240  O   GLU A 708     -28.367   2.451  14.871  1.00 60.09           O  
-ATOM   1241  CB  GLU A 708     -27.203   3.203  11.830  1.00 58.92           C  
-ATOM   1242  CG  GLU A 708     -26.005   3.840  11.165  1.00 58.85           C  
-ATOM   1243  CD  GLU A 708     -26.403   4.671   9.936  1.00 69.32           C  
-ATOM   1244  OE1 GLU A 708     -27.424   4.341   9.275  1.00 64.88           O  
-ATOM   1245  OE2 GLU A 708     -25.694   5.662   9.638  1.00 71.29           O  
-ATOM   1246  N   TYR A 709     -28.937   1.099  13.171  1.00 53.48           N  
-ATOM   1247  CA  TYR A 709     -30.213   0.721  13.727  1.00 56.33           C  
-ATOM   1248  C   TYR A 709     -30.089   0.126  15.132  1.00 62.63           C  
-ATOM   1249  O   TYR A 709     -30.852   0.463  16.049  1.00 61.01           O  
-ATOM   1250  CB  TYR A 709     -30.894  -0.260  12.796  1.00 54.80           C  
-ATOM   1251  CG  TYR A 709     -32.252  -0.637  13.279  1.00 57.69           C  
-ATOM   1252  CD1 TYR A 709     -33.285   0.287  13.273  1.00 59.08           C  
-ATOM   1253  CD2 TYR A 709     -32.506  -1.910  13.757  1.00 60.98           C  
-ATOM   1254  CE1 TYR A 709     -34.549  -0.049  13.722  1.00 58.41           C  
-ATOM   1255  CE2 TYR A 709     -33.757  -2.259  14.213  1.00 63.69           C  
-ATOM   1256  CZ  TYR A 709     -34.779  -1.323  14.197  1.00 65.55           C  
-ATOM   1257  OH  TYR A 709     -36.033  -1.669  14.657  1.00 70.34           O  
-ATOM   1258  N   LYS A 710     -29.117  -0.760  15.299  1.00 61.84           N  
-ATOM   1259  CA  LYS A 710     -28.903  -1.408  16.576  1.00 61.29           C  
-ATOM   1260  C   LYS A 710     -28.497  -0.372  17.611  1.00 60.57           C  
-ATOM   1261  O   LYS A 710     -28.989  -0.368  18.752  1.00 57.88           O  
-ATOM   1262  CB  LYS A 710     -27.796  -2.446  16.450  1.00 62.03           C  
-ATOM   1263  CG  LYS A 710     -28.226  -3.841  16.049  1.00 59.04           C  
-ATOM   1264  CD  LYS A 710     -26.950  -4.625  15.794  1.00 64.41           C  
-ATOM   1265  CE  LYS A 710     -27.186  -6.076  15.468  1.00 72.40           C  
-ATOM   1266  NZ  LYS A 710     -25.863  -6.770  15.319  1.00 73.70           N  
-ATOM   1267  N   THR A 711     -27.577   0.491  17.201  1.00 52.94           N  
-ATOM   1268  CA  THR A 711     -27.073   1.535  18.061  1.00 56.25           C  
-ATOM   1269  C   THR A 711     -28.232   2.403  18.538  1.00 60.69           C  
-ATOM   1270  O   THR A 711     -28.431   2.586  19.743  1.00 58.50           O  
-ATOM   1271  CB  THR A 711     -26.069   2.399  17.311  1.00 61.40           C  
-ATOM   1272  OG1 THR A 711     -24.967   1.585  16.893  1.00 65.72           O  
-ATOM   1273  CG2 THR A 711     -25.560   3.508  18.204  1.00 57.69           C  
-ATOM   1274  N   THR A 712     -29.015   2.894  17.578  1.00 59.19           N  
-ATOM   1275  CA  THR A 712     -30.176   3.739  17.852  1.00 58.57           C  
-ATOM   1276  C   THR A 712     -31.171   3.116  18.833  1.00 57.42           C  
-ATOM   1277  O   THR A 712     -31.628   3.770  19.771  1.00 55.06           O  
-ATOM   1278  CB  THR A 712     -30.889   4.122  16.540  1.00 54.57           C  
-ATOM   1279  OG1 THR A 712     -29.966   4.819  15.699  1.00 58.52           O  
-ATOM   1280  CG2 THR A 712     -32.078   5.024  16.803  1.00 50.76           C  
-ATOM   1281  N   LEU A 713     -31.497   1.853  18.614  1.00 57.07           N  
-ATOM   1282  CA  LEU A 713     -32.403   1.144  19.501  1.00 58.53           C  
-ATOM   1283  C   LEU A 713     -31.883   1.065  20.926  1.00 57.33           C  
-ATOM   1284  O   LEU A 713     -32.645   1.151  21.881  1.00 54.66           O  
-ATOM   1285  CB  LEU A 713     -32.622  -0.270  18.994  1.00 61.34           C  
-ATOM   1286  CG  LEU A 713     -33.823  -0.479  18.095  1.00 66.27           C  
-ATOM   1287  CD1 LEU A 713     -34.117  -1.970  18.056  1.00 64.88           C  
-ATOM   1288  CD2 LEU A 713     -35.012   0.295  18.644  1.00 62.73           C  
-ATOM   1289  N   LYS A 714     -30.583   0.859  21.067  1.00 58.06           N  
-ATOM   1290  CA  LYS A 714     -30.003   0.714  22.385  1.00 58.23           C  
-ATOM   1291  C   LYS A 714     -30.196   2.047  23.094  1.00 59.47           C  
-ATOM   1292  O   LYS A 714     -30.704   2.102  24.216  1.00 57.21           O  
-ATOM   1293  CB  LYS A 714     -28.513   0.362  22.287  1.00 59.51           C  
-ATOM   1294  N   ILE A 715     -29.816   3.123  22.413  1.00 54.16           N  
-ATOM   1295  CA  ILE A 715     -30.027   4.455  22.951  1.00 57.12           C  
-ATOM   1296  C   ILE A 715     -31.498   4.750  23.286  1.00 54.32           C  
-ATOM   1297  O   ILE A 715     -31.813   5.222  24.371  1.00 55.98           O  
-ATOM   1298  CB  ILE A 715     -29.492   5.534  22.014  1.00 57.25           C  
-ATOM   1299  CG1 ILE A 715     -28.006   5.304  21.731  1.00 50.78           C  
-ATOM   1300  CG2 ILE A 715     -29.717   6.919  22.628  1.00 54.45           C  
-ATOM   1301  CD1 ILE A 715     -27.498   6.105  20.542  1.00 54.17           C  
-ATOM   1302  N   ILE A 716     -32.398   4.466  22.365  1.00 53.33           N  
-ATOM   1303  CA  ILE A 716     -33.802   4.701  22.630  1.00 53.04           C  
-ATOM   1304  C   ILE A 716     -34.192   3.998  23.911  1.00 53.34           C  
-ATOM   1305  O   ILE A 716     -34.842   4.577  24.782  1.00 51.93           O  
-ATOM   1306  CB  ILE A 716     -34.687   4.192  21.479  1.00 53.86           C  
-ATOM   1307  CG1 ILE A 716     -34.512   5.070  20.238  1.00 52.45           C  
-ATOM   1308  CG2 ILE A 716     -36.148   4.176  21.880  1.00 50.52           C  
-ATOM   1309  CD1 ILE A 716     -35.176   4.498  19.010  1.00 50.78           C  
-ATOM   1310  N   LYS A 717     -33.766   2.749  24.039  1.00 55.58           N  
-ATOM   1311  CA  LYS A 717     -34.215   1.915  25.156  1.00 56.85           C  
-ATOM   1312  C   LYS A 717     -33.722   2.498  26.475  1.00 55.52           C  
-ATOM   1313  O   LYS A 717     -34.458   2.571  27.444  1.00 54.45           O  
-ATOM   1314  CB  LYS A 717     -33.724   0.471  24.986  1.00 55.40           C  
-ATOM   1315  CG  LYS A 717     -34.217  -0.481  26.057  1.00 58.82           C  
-ATOM   1316  CD  LYS A 717     -33.612  -1.874  25.920  1.00 61.14           C  
-ATOM   1317  CE  LYS A 717     -34.209  -2.842  26.942  1.00 61.14           C  
-ATOM   1318  NZ  LYS A 717     -34.217  -4.271  26.499  1.00 61.53           N  
-ATOM   1319  N   GLN A 718     -32.466   2.920  26.487  1.00 54.09           N  
-ATOM   1320  CA  GLN A 718     -31.858   3.462  27.675  1.00 54.11           C  
-ATOM   1321  C   GLN A 718     -32.509   4.781  28.026  1.00 55.25           C  
-ATOM   1322  O   GLN A 718     -32.777   5.052  29.195  1.00 52.77           O  
-ATOM   1323  CB  GLN A 718     -30.360   3.663  27.456  1.00 58.83           C  
-ATOM   1324  CG  GLN A 718     -29.536   2.382  27.495  1.00 66.47           C  
-ATOM   1325  CD  GLN A 718     -28.080   2.612  27.077  1.00 81.59           C  
-ATOM   1326  OE1 GLN A 718     -27.785   3.453  26.205  1.00 77.30           O  
-ATOM   1327  NE2 GLN A 718     -27.162   1.867  27.701  1.00 75.67           N  
-ATOM   1328  N   ALA A 719     -32.760   5.599  27.007  1.00 56.06           N  
-ATOM   1329  CA  ALA A 719     -33.467   6.866  27.198  1.00 52.90           C  
-ATOM   1330  C   ALA A 719     -34.787   6.628  27.907  1.00 47.86           C  
-ATOM   1331  O   ALA A 719     -35.059   7.214  28.947  1.00 47.08           O  
-ATOM   1332  CB  ALA A 719     -33.720   7.531  25.880  1.00 49.22           C  
-ATOM   1333  N   ILE A 720     -35.603   5.753  27.344  1.00 44.79           N  
-ATOM   1334  CA  ILE A 720     -36.915   5.540  27.911  1.00 47.94           C  
-ATOM   1335  C   ILE A 720     -36.801   5.024  29.346  1.00 51.30           C  
-ATOM   1336  O   ILE A 720     -37.641   5.321  30.192  1.00 48.54           O  
-ATOM   1337  CB  ILE A 720     -37.786   4.600  27.049  1.00 43.41           C  
-ATOM   1338  CG1 ILE A 720     -38.047   5.243  25.693  1.00 42.25           C  
-ATOM   1339  CG2 ILE A 720     -39.093   4.251  27.785  1.00 43.49           C  
-ATOM   1340  CD1 ILE A 720     -39.148   4.571  24.855  1.00 47.48           C  
-ATOM   1341  N   LEU A 721     -35.749   4.266  29.627  1.00 50.71           N  
-ATOM   1342  CA  LEU A 721     -35.631   3.672  30.947  1.00 54.72           C  
-ATOM   1343  C   LEU A 721     -35.124   4.703  31.931  1.00 52.87           C  
-ATOM   1344  O   LEU A 721     -35.346   4.589  33.126  1.00 57.38           O  
-ATOM   1345  CB  LEU A 721     -34.728   2.431  30.936  1.00 56.42           C  
-ATOM   1346  CG  LEU A 721     -35.242   1.143  30.266  1.00 57.58           C  
-ATOM   1347  CD1 LEU A 721     -34.184   0.071  30.384  1.00 61.47           C  
-ATOM   1348  CD2 LEU A 721     -36.550   0.642  30.827  1.00 55.24           C  
-ATOM   1349  N   ALA A 722     -34.447   5.717  31.417  1.00 50.93           N  
-ATOM   1350  CA  ALA A 722     -33.950   6.775  32.260  1.00 47.89           C  
-ATOM   1351  C   ALA A 722     -35.110   7.553  32.871  1.00 52.90           C  
-ATOM   1352  O   ALA A 722     -34.929   8.193  33.906  1.00 57.05           O  
-ATOM   1353  CB  ALA A 722     -33.020   7.689  31.479  1.00 45.00           C  
-ATOM   1354  N   THR A 723     -36.297   7.475  32.254  1.00 50.53           N  
-ATOM   1355  CA  THR A 723     -37.481   8.199  32.741  1.00 49.41           C  
-ATOM   1356  C   THR A 723     -38.125   7.576  33.989  1.00 53.68           C  
-ATOM   1357  O   THR A 723     -39.178   8.035  34.475  1.00 53.59           O  
-ATOM   1358  CB  THR A 723     -38.574   8.414  31.634  1.00 49.75           C  
-ATOM   1359  OG1 THR A 723     -39.263   7.179  31.345  1.00 50.40           O  
-ATOM   1360  CG2 THR A 723     -37.973   9.030  30.373  1.00 45.43           C  
-ATOM   1361  N   ASP A 724     -37.512   6.511  34.487  1.00 53.69           N  
-ATOM   1362  CA  ASP A 724     -37.865   5.992  35.794  1.00 57.93           C  
-ATOM   1363  C   ASP A 724     -37.184   6.913  36.796  1.00 58.66           C  
-ATOM   1364  O   ASP A 724     -35.958   7.069  36.779  1.00 57.06           O  
-ATOM   1365  CB  ASP A 724     -37.393   4.542  35.956  1.00 61.49           C  
-ATOM   1366  CG  ASP A 724     -37.753   3.952  37.314  1.00 67.75           C  
-ATOM   1367  OD1 ASP A 724     -38.465   4.627  38.099  1.00 67.49           O  
-ATOM   1368  OD2 ASP A 724     -37.340   2.799  37.593  1.00 69.27           O  
-ATOM   1369  N   LEU A 725     -37.969   7.565  37.646  1.00 56.68           N  
-ATOM   1370  CA  LEU A 725     -37.348   8.466  38.604  1.00 59.96           C  
-ATOM   1371  C   LEU A 725     -36.389   7.728  39.535  1.00 58.60           C  
-ATOM   1372  O   LEU A 725     -35.340   8.254  39.895  1.00 59.40           O  
-ATOM   1373  CB  LEU A 725     -38.391   9.270  39.366  1.00 63.85           C  
-ATOM   1374  CG  LEU A 725     -38.998  10.392  38.512  1.00 60.33           C  
-ATOM   1375  CD1 LEU A 725     -40.238  10.969  39.185  1.00 61.43           C  
-ATOM   1376  CD2 LEU A 725     -37.971  11.489  38.202  1.00 49.29           C  
-ATOM   1377  N   ALA A 726     -36.728   6.491  39.875  1.00 58.11           N  
-ATOM   1378  CA  ALA A 726     -35.811   5.623  40.626  1.00 62.45           C  
-ATOM   1379  C   ALA A 726     -34.425   5.491  39.978  1.00 59.58           C  
-ATOM   1380  O   ALA A 726     -33.404   5.613  40.659  1.00 62.11           O  
-ATOM   1381  CB  ALA A 726     -36.437   4.235  40.863  1.00 61.90           C  
-ATOM   1382  N   LEU A 727     -34.383   5.239  38.671  1.00 58.98           N  
-ATOM   1383  CA  LEU A 727     -33.102   5.214  37.957  1.00 60.02           C  
-ATOM   1384  C   LEU A 727     -32.392   6.560  38.052  1.00 60.17           C  
-ATOM   1385  O   LEU A 727     -31.167   6.633  38.176  1.00 61.28           O  
-ATOM   1386  CB  LEU A 727     -33.292   4.840  36.481  1.00 64.10           C  
-ATOM   1387  CG  LEU A 727     -33.170   3.373  36.063  1.00 63.54           C  
-ATOM   1388  N   TYR A 728     -33.164   7.635  37.990  1.00 60.36           N  
-ATOM   1389  CA  TYR A 728     -32.565   8.960  38.004  1.00 60.41           C  
-ATOM   1390  C   TYR A 728     -31.888   9.258  39.352  1.00 61.10           C  
-ATOM   1391  O   TYR A 728     -30.805   9.837  39.410  1.00 56.91           O  
-ATOM   1392  CB  TYR A 728     -33.609  10.021  37.640  1.00 59.01           C  
-ATOM   1393  CG  TYR A 728     -33.227  11.398  38.100  1.00 58.56           C  
-ATOM   1394  CD1 TYR A 728     -32.203  12.109  37.471  1.00 59.03           C  
-ATOM   1395  CD2 TYR A 728     -33.872  11.984  39.175  1.00 54.22           C  
-ATOM   1396  CE1 TYR A 728     -31.830  13.378  37.915  1.00 60.60           C  
-ATOM   1397  CE2 TYR A 728     -33.511  13.237  39.630  1.00 60.52           C  
-ATOM   1398  CZ  TYR A 728     -32.492  13.938  39.004  1.00 65.40           C  
-ATOM   1399  OH  TYR A 728     -32.157  15.200  39.472  1.00 64.41           O  
-ATOM   1400  N   ILE A 729     -32.526   8.839  40.435  1.00 61.44           N  
-ATOM   1401  CA  ILE A 729     -31.990   9.075  41.772  1.00 65.01           C  
-ATOM   1402  C   ILE A 729     -30.739   8.231  42.074  1.00 66.96           C  
-ATOM   1403  O   ILE A 729     -29.799   8.692  42.747  1.00 63.38           O  
-ATOM   1404  CB  ILE A 729     -33.070   8.828  42.822  1.00 63.61           C  
-ATOM   1405  CG1 ILE A 729     -34.084   9.972  42.770  1.00 62.37           C  
-ATOM   1406  CG2 ILE A 729     -32.457   8.712  44.207  1.00 66.82           C  
-ATOM   1407  CD1 ILE A 729     -35.476   9.561  43.146  1.00 57.36           C  
-ATOM   1408  N   LYS A 730     -30.739   6.999  41.572  1.00 62.23           N  
-ATOM   1409  CA  LYS A 730     -29.571   6.141  41.664  1.00 64.24           C  
-ATOM   1410  C   LYS A 730     -28.391   6.779  40.948  1.00 67.35           C  
-ATOM   1411  O   LYS A 730     -27.262   6.751  41.443  1.00 71.89           O  
-ATOM   1412  CB  LYS A 730     -29.850   4.772  41.032  1.00 70.56           C  
-ATOM   1413  CG  LYS A 730     -30.608   3.778  41.914  1.00 71.02           C  
-ATOM   1414  N   ARG A 731     -28.642   7.363  39.784  1.00 63.92           N  
-ATOM   1415  CA  ARG A 731     -27.535   7.701  38.891  1.00 64.21           C  
-ATOM   1416  C   ARG A 731     -27.057   9.149  38.943  1.00 64.77           C  
-ATOM   1417  O   ARG A 731     -25.991   9.478  38.423  1.00 65.80           O  
-ATOM   1418  CB  ARG A 731     -27.859   7.259  37.456  1.00 63.17           C  
-ATOM   1419  CG  ARG A 731     -28.112   5.754  37.369  1.00 68.76           C  
-ATOM   1420  CD  ARG A 731     -27.903   5.164  35.980  1.00 75.28           C  
-ATOM   1421  NE  ARG A 731     -26.526   5.265  35.495  1.00 74.12           N  
-ATOM   1422  CZ  ARG A 731     -26.197   5.695  34.274  1.00 82.10           C  
-ATOM   1423  NH1 ARG A 731     -27.146   6.076  33.415  1.00 75.08           N  
-ATOM   1424  NH2 ARG A 731     -24.919   5.756  33.908  1.00 82.36           N  
-ATOM   1425  N   ARG A 732     -27.831  10.013  39.585  1.00 65.91           N  
-ATOM   1426  CA  ARG A 732     -27.555  11.441  39.515  1.00 62.94           C  
-ATOM   1427  C   ARG A 732     -26.360  11.839  40.380  1.00 68.42           C  
-ATOM   1428  O   ARG A 732     -25.606  12.754  40.030  1.00 69.03           O  
-ATOM   1429  CB  ARG A 732     -28.795  12.242  39.900  1.00 65.72           C  
-ATOM   1430  CG  ARG A 732     -29.268  11.976  41.316  1.00 69.85           C  
-ATOM   1431  CD  ARG A 732     -30.249  13.021  41.741  1.00 68.42           C  
-ATOM   1432  NE  ARG A 732     -30.643  12.854  43.134  1.00 76.09           N  
-ATOM   1433  CZ  ARG A 732     -31.570  13.599  43.736  1.00 78.25           C  
-ATOM   1434  NH1 ARG A 732     -32.195  14.557  43.052  1.00 68.85           N  
-ATOM   1435  NH2 ARG A 732     -31.867  13.386  45.018  1.00 73.19           N  
-ATOM   1436  N   GLY A 733     -26.190  11.152  41.508  1.00 68.08           N  
-ATOM   1437  CA  GLY A 733     -25.043  11.384  42.367  1.00 70.83           C  
-ATOM   1438  C   GLY A 733     -23.758  11.462  41.563  1.00 75.16           C  
-ATOM   1439  O   GLY A 733     -23.036  12.469  41.609  1.00 72.50           O  
-ATOM   1440  N   GLU A 734     -23.491  10.398  40.805  1.00 74.73           N  
-ATOM   1441  CA  GLU A 734     -22.326  10.343  39.939  1.00 72.77           C  
-ATOM   1442  C   GLU A 734     -22.246  11.553  39.019  1.00 71.50           C  
-ATOM   1443  O   GLU A 734     -21.179  12.139  38.831  1.00 75.06           O  
-ATOM   1444  CB  GLU A 734     -22.341   9.070  39.106  1.00 75.63           C  
-ATOM   1445  CG  GLU A 734     -21.146   8.969  38.168  1.00 81.53           C  
-ATOM   1446  CD  GLU A 734     -21.137   7.694  37.350  1.00 86.81           C  
-ATOM   1447  OE1 GLU A 734     -22.017   6.827  37.577  1.00 85.68           O  
-ATOM   1448  OE2 GLU A 734     -20.244   7.565  36.481  1.00 87.81           O  
-ATOM   1449  N   PHE A 735     -23.380  11.923  38.445  1.00 70.60           N  
-ATOM   1450  CA  PHE A 735     -23.448  13.066  37.536  1.00 73.61           C  
-ATOM   1451  C   PHE A 735     -23.040  14.349  38.242  1.00 70.76           C  
-ATOM   1452  O   PHE A 735     -22.304  15.162  37.700  1.00 69.14           O  
-ATOM   1453  CB  PHE A 735     -24.871  13.196  36.975  1.00 70.75           C  
-ATOM   1454  CG  PHE A 735     -25.012  14.233  35.903  1.00 65.42           C  
-ATOM   1455  CD1 PHE A 735     -24.180  14.222  34.801  1.00 63.60           C  
-ATOM   1456  CD2 PHE A 735     -25.997  15.210  35.990  1.00 65.16           C  
-ATOM   1457  CE1 PHE A 735     -24.313  15.186  33.805  1.00 67.65           C  
-ATOM   1458  CE2 PHE A 735     -26.138  16.174  35.004  1.00 65.72           C  
-ATOM   1459  CZ  PHE A 735     -25.294  16.165  33.905  1.00 65.75           C  
-ATOM   1460  N   PHE A 736     -23.519  14.512  39.468  1.00 72.59           N  
-ATOM   1461  CA  PHE A 736     -23.235  15.707  40.254  1.00 74.99           C  
-ATOM   1462  C   PHE A 736     -21.780  15.779  40.703  1.00 76.09           C  
-ATOM   1463  O   PHE A 736     -21.149  16.831  40.591  1.00 76.17           O  
-ATOM   1464  CB  PHE A 736     -24.182  15.794  41.456  1.00 72.27           C  
-ATOM   1465  CG  PHE A 736     -25.631  15.913  41.072  1.00 70.33           C  
-ATOM   1466  CD1 PHE A 736     -26.630  15.483  41.930  1.00 65.80           C  
-ATOM   1467  CD2 PHE A 736     -25.991  16.446  39.836  1.00 69.49           C  
-ATOM   1468  CE1 PHE A 736     -27.965  15.585  41.572  1.00 65.88           C  
-ATOM   1469  CE2 PHE A 736     -27.318  16.546  39.470  1.00 67.54           C  
-ATOM   1470  CZ  PHE A 736     -28.310  16.115  40.348  1.00 68.34           C  
-ATOM   1471  N   GLU A 737     -21.251  14.668  41.214  1.00 76.39           N  
-ATOM   1472  CA  GLU A 737     -19.815  14.578  41.500  1.00 80.00           C  
-ATOM   1473  C   GLU A 737     -18.998  15.119  40.323  1.00 77.54           C  
-ATOM   1474  O   GLU A 737     -18.304  16.120  40.447  1.00 79.07           O  
-ATOM   1475  CB  GLU A 737     -19.401  13.131  41.799  1.00 77.45           C  
-ATOM   1476  CG  GLU A 737     -20.460  12.333  42.556  1.00 84.61           C  
-ATOM   1477  CD  GLU A 737     -19.986  10.949  43.015  1.00 89.61           C  
-ATOM   1478  OE1 GLU A 737     -18.819  10.587  42.729  1.00 87.42           O  
-ATOM   1479  OE2 GLU A 737     -20.787  10.233  43.672  1.00 84.14           O  
-ATOM   1480  N   LEU A 738     -19.105  14.458  39.176  1.00 76.04           N  
-ATOM   1481  CA  LEU A 738     -18.357  14.850  37.988  1.00 79.91           C  
-ATOM   1482  C   LEU A 738     -18.367  16.359  37.761  1.00 84.30           C  
-ATOM   1483  O   LEU A 738     -17.351  16.954  37.399  1.00 86.00           O  
-ATOM   1484  CB  LEU A 738     -18.908  14.141  36.750  1.00 83.00           C  
-ATOM   1485  CG  LEU A 738     -18.901  12.611  36.771  1.00 84.71           C  
-ATOM   1486  CD1 LEU A 738     -19.779  12.072  35.658  1.00 85.53           C  
-ATOM   1487  CD2 LEU A 738     -17.487  12.049  36.664  1.00 81.77           C  
-ATOM   1488  N   ILE A 739     -19.523  16.975  37.967  1.00 82.96           N  
-ATOM   1489  CA  ILE A 739     -19.662  18.409  37.762  1.00 82.07           C  
-ATOM   1490  C   ILE A 739     -18.860  19.236  38.771  1.00 84.53           C  
-ATOM   1491  O   ILE A 739     -18.064  20.101  38.389  1.00 82.41           O  
-ATOM   1492  CB  ILE A 739     -21.129  18.821  37.836  1.00 79.19           C  
-ATOM   1493  CG1 ILE A 739     -21.970  17.915  36.930  1.00 79.62           C  
-ATOM   1494  CG2 ILE A 739     -21.290  20.298  37.472  1.00 81.42           C  
-ATOM   1495  CD1 ILE A 739     -21.803  18.184  35.450  1.00 77.50           C  
-ATOM   1496  N   ARG A 740     -19.070  18.973  40.059  1.00 84.04           N  
-ATOM   1497  CA  ARG A 740     -18.445  19.792  41.089  1.00 83.35           C  
-ATOM   1498  C   ARG A 740     -16.939  19.611  41.087  1.00 88.58           C  
-ATOM   1499  O   ARG A 740     -16.198  20.513  41.491  1.00 91.40           O  
-ATOM   1500  CB  ARG A 740     -19.026  19.497  42.470  1.00 82.99           C  
-ATOM   1501  CG  ARG A 740     -18.890  18.062  42.922  1.00 84.72           C  
-ATOM   1502  CD  ARG A 740     -19.468  17.890  44.317  1.00 81.89           C  
-ATOM   1503  NE  ARG A 740     -19.416  16.503  44.760  1.00 82.03           N  
-ATOM   1504  CZ  ARG A 740     -20.480  15.714  44.879  1.00 83.23           C  
-ATOM   1505  NH1 ARG A 740     -20.326  14.460  45.291  1.00 81.11           N  
-ATOM   1506  NH2 ARG A 740     -21.695  16.179  44.598  1.00 78.75           N  
-ATOM   1507  N   LYS A 741     -16.490  18.448  40.620  1.00 88.59           N  
-ATOM   1508  CA  LYS A 741     -15.059  18.147  40.538  1.00 87.97           C  
-ATOM   1509  C   LYS A 741     -14.497  18.481  39.148  1.00 85.14           C  
-ATOM   1510  O   LYS A 741     -13.507  17.899  38.721  1.00 84.37           O  
-ATOM   1511  CB  LYS A 741     -14.778  16.684  40.933  1.00 78.85           C  
-ATOM   1512  N   ASN A 742     -15.139  19.431  38.465  1.00 85.29           N  
-ATOM   1513  CA  ASN A 742     -14.745  19.887  37.119  1.00 91.56           C  
-ATOM   1514  C   ASN A 742     -14.373  18.784  36.103  1.00 92.79           C  
-ATOM   1515  O   ASN A 742     -13.888  19.075  35.000  1.00 83.94           O  
-ATOM   1516  CB  ASN A 742     -13.645  20.951  37.200  1.00 87.07           C  
-ATOM   1517  N   GLN A 743     -14.649  17.532  36.478  1.00 90.89           N  
-ATOM   1518  CA  GLN A 743     -14.302  16.343  35.696  1.00 86.70           C  
-ATOM   1519  C   GLN A 743     -15.191  16.071  34.463  1.00 91.33           C  
-ATOM   1520  O   GLN A 743     -14.808  15.284  33.595  1.00 95.37           O  
-ATOM   1521  CB  GLN A 743     -14.311  15.092  36.601  1.00 89.13           C  
-ATOM   1522  CG  GLN A 743     -13.064  14.863  37.467  1.00 86.86           C  
-ATOM   1523  N   PHE A 744     -16.365  16.694  34.373  1.00 89.78           N  
-ATOM   1524  CA  PHE A 744     -17.319  16.312  33.320  1.00 90.05           C  
-ATOM   1525  C   PHE A 744     -16.758  16.343  31.889  1.00 90.73           C  
-ATOM   1526  O   PHE A 744     -16.196  17.346  31.439  1.00 93.22           O  
-ATOM   1527  CB  PHE A 744     -18.623  17.115  33.398  1.00 88.02           C  
-ATOM   1528  CG  PHE A 744     -19.693  16.603  32.468  1.00 87.51           C  
-ATOM   1529  CD1 PHE A 744     -20.318  15.382  32.716  1.00 84.31           C  
-ATOM   1530  CD2 PHE A 744     -20.061  17.326  31.336  1.00 87.42           C  
-ATOM   1531  CE1 PHE A 744     -21.298  14.893  31.862  1.00 77.45           C  
-ATOM   1532  CE2 PHE A 744     -21.043  16.847  30.476  1.00 84.46           C  
-ATOM   1533  CZ  PHE A 744     -21.663  15.624  30.743  1.00 78.43           C  
-ATOM   1534  N   ASN A 745     -16.939  15.237  31.177  1.00 86.27           N  
-ATOM   1535  CA  ASN A 745     -16.397  15.085  29.835  1.00 90.99           C  
-ATOM   1536  C   ASN A 745     -17.305  14.228  28.948  1.00 92.57           C  
-ATOM   1537  O   ASN A 745     -17.403  13.004  29.125  1.00 90.28           O  
-ATOM   1538  CB  ASN A 745     -14.990  14.481  29.909  1.00 91.42           C  
-ATOM   1539  CG  ASN A 745     -14.455  14.048  28.547  1.00 94.51           C  
-ATOM   1540  OD1 ASN A 745     -14.565  14.772  27.549  1.00 93.49           O  
-ATOM   1541  ND2 ASN A 745     -13.873  12.852  28.503  1.00 91.99           N  
-ATOM   1542  N   LEU A 746     -17.968  14.875  27.994  1.00 88.08           N  
-ATOM   1543  CA  LEU A 746     -18.934  14.185  27.147  1.00 87.40           C  
-ATOM   1544  C   LEU A 746     -18.268  13.186  26.193  1.00 88.95           C  
-ATOM   1545  O   LEU A 746     -18.928  12.294  25.672  1.00 88.53           O  
-ATOM   1546  CB  LEU A 746     -19.812  15.189  26.380  1.00 79.55           C  
-ATOM   1547  N   GLU A 747     -16.963  13.321  25.973  1.00 89.76           N  
-ATOM   1548  CA  GLU A 747     -16.279  12.443  25.023  1.00 88.50           C  
-ATOM   1549  C   GLU A 747     -16.133  11.023  25.569  1.00 86.08           C  
-ATOM   1550  O   GLU A 747     -15.761  10.106  24.843  1.00 84.67           O  
-ATOM   1551  CB  GLU A 747     -14.922  13.016  24.604  1.00 83.97           C  
-ATOM   1552  N   ASP A 748     -16.448  10.838  26.846  1.00 87.64           N  
-ATOM   1553  CA  ASP A 748     -16.430   9.500  27.442  1.00 87.08           C  
-ATOM   1554  C   ASP A 748     -17.755   8.759  27.236  1.00 83.82           C  
-ATOM   1555  O   ASP A 748     -18.814   9.248  27.610  1.00 85.58           O  
-ATOM   1556  CB  ASP A 748     -16.093   9.571  28.934  1.00 82.31           C  
-ATOM   1557  CG  ASP A 748     -16.208   8.225  29.621  1.00 86.58           C  
-ATOM   1558  OD1 ASP A 748     -15.984   7.192  28.955  1.00 89.06           O  
-ATOM   1559  OD2 ASP A 748     -16.526   8.192  30.828  1.00 89.63           O  
-ATOM   1560  N   PRO A 749     -17.696   7.571  26.631  1.00 85.79           N  
-ATOM   1561  CA  PRO A 749     -18.898   6.751  26.430  1.00 87.15           C  
-ATOM   1562  C   PRO A 749     -19.789   6.680  27.666  1.00 81.48           C  
-ATOM   1563  O   PRO A 749     -21.005   6.823  27.549  1.00 80.79           O  
-ATOM   1564  CB  PRO A 749     -18.324   5.361  26.130  1.00 79.63           C  
-ATOM   1565  CG  PRO A 749     -17.012   5.645  25.486  1.00 81.99           C  
-ATOM   1566  CD  PRO A 749     -16.490   6.943  26.064  1.00 82.60           C  
-ATOM   1567  N   HIS A 750     -19.194   6.454  28.833  1.00 84.34           N  
-ATOM   1568  CA  HIS A 750     -19.980   6.209  30.038  1.00 84.57           C  
-ATOM   1569  C   HIS A 750     -20.676   7.471  30.523  1.00 81.14           C  
-ATOM   1570  O   HIS A 750     -21.834   7.442  30.926  1.00 73.90           O  
-ATOM   1571  CB  HIS A 750     -19.115   5.637  31.154  1.00 81.18           C  
-ATOM   1572  CG  HIS A 750     -19.889   5.301  32.391  1.00 88.02           C  
-ATOM   1573  ND1 HIS A 750     -19.928   6.126  33.495  1.00 85.54           N  
-ATOM   1574  CD2 HIS A 750     -20.668   4.233  32.692  1.00 87.48           C  
-ATOM   1575  CE1 HIS A 750     -20.688   5.576  34.426  1.00 87.31           C  
-ATOM   1576  NE2 HIS A 750     -21.150   4.427  33.964  1.00 83.39           N  
-ATOM   1577  N   GLN A 751     -19.956   8.583  30.480  1.00 82.11           N  
-ATOM   1578  CA  GLN A 751     -20.525   9.856  30.885  1.00 82.19           C  
-ATOM   1579  C   GLN A 751     -21.572  10.350  29.895  1.00 77.71           C  
-ATOM   1580  O   GLN A 751     -22.579  10.943  30.298  1.00 75.67           O  
-ATOM   1581  CB  GLN A 751     -19.426  10.896  31.096  1.00 86.03           C  
-ATOM   1582  CG  GLN A 751     -18.602  10.644  32.347  1.00 81.59           C  
-ATOM   1583  CD  GLN A 751     -17.478  11.636  32.500  1.00 91.34           C  
-ATOM   1584  OE1 GLN A 751     -17.559  12.773  32.019  1.00 89.88           O  
-ATOM   1585  NE2 GLN A 751     -16.407  11.209  33.161  1.00 92.89           N  
-ATOM   1586  N   LYS A 752     -21.329  10.099  28.609  1.00 77.49           N  
-ATOM   1587  CA  LYS A 752     -22.293  10.392  27.551  1.00 76.41           C  
-ATOM   1588  C   LYS A 752     -23.646   9.742  27.823  1.00 72.31           C  
-ATOM   1589  O   LYS A 752     -24.679  10.400  27.869  1.00 66.87           O  
-ATOM   1590  CB  LYS A 752     -21.768   9.860  26.229  1.00 76.44           C  
-ATOM   1591  CG  LYS A 752     -21.553  10.921  25.201  1.00 80.13           C  
-ATOM   1592  CD  LYS A 752     -22.850  11.446  24.651  1.00 71.48           C  
-ATOM   1593  CE  LYS A 752     -22.549  12.306  23.442  1.00 71.72           C  
-ATOM   1594  NZ  LYS A 752     -21.732  11.540  22.450  1.00 71.51           N  
-ATOM   1595  N   GLU A 753     -23.626   8.433  27.994  1.00 69.80           N  
-ATOM   1596  CA  GLU A 753     -24.839   7.705  28.252  1.00 71.71           C  
-ATOM   1597  C   GLU A 753     -25.567   8.272  29.472  1.00 73.09           C  
-ATOM   1598  O   GLU A 753     -26.801   8.253  29.537  1.00 71.70           O  
-ATOM   1599  CB  GLU A 753     -24.515   6.234  28.454  1.00 71.09           C  
-ATOM   1600  CG  GLU A 753     -25.665   5.434  29.007  1.00 80.82           C  
-ATOM   1601  CD  GLU A 753     -25.327   3.964  29.103  1.00 89.52           C  
-ATOM   1602  OE1 GLU A 753     -26.013   3.234  29.863  1.00 91.17           O  
-ATOM   1603  OE2 GLU A 753     -24.364   3.547  28.414  1.00 85.85           O  
-ATOM   1604  N   LEU A 754     -24.800   8.787  30.428  1.00 71.06           N  
-ATOM   1605  CA  LEU A 754     -25.361   9.283  31.680  1.00 70.25           C  
-ATOM   1606  C   LEU A 754     -26.030  10.642  31.466  1.00 66.73           C  
-ATOM   1607  O   LEU A 754     -27.102  10.933  32.009  1.00 58.44           O  
-ATOM   1608  CB  LEU A 754     -24.268   9.381  32.742  1.00 68.82           C  
-ATOM   1609  CG  LEU A 754     -24.589   9.976  34.115  1.00 70.29           C  
-ATOM   1610  CD1 LEU A 754     -25.575   9.123  34.929  1.00 64.84           C  
-ATOM   1611  CD2 LEU A 754     -23.289  10.181  34.875  1.00 71.79           C  
-ATOM   1612  N   PHE A 755     -25.385  11.467  30.658  1.00 63.99           N  
-ATOM   1613  CA  PHE A 755     -25.914  12.770  30.346  1.00 59.29           C  
-ATOM   1614  C   PHE A 755     -27.235  12.601  29.607  1.00 62.31           C  
-ATOM   1615  O   PHE A 755     -28.219  13.276  29.912  1.00 61.65           O  
-ATOM   1616  CB  PHE A 755     -24.899  13.521  29.510  1.00 57.87           C  
-ATOM   1617  CG  PHE A 755     -25.406  14.787  28.932  1.00 60.91           C  
-ATOM   1618  CD1 PHE A 755     -25.771  15.845  29.753  1.00 64.14           C  
-ATOM   1619  CD2 PHE A 755     -25.487  14.946  27.557  1.00 62.05           C  
-ATOM   1620  CE1 PHE A 755     -26.227  17.044  29.210  1.00 62.35           C  
-ATOM   1621  CE2 PHE A 755     -25.945  16.143  27.004  1.00 65.53           C  
-ATOM   1622  CZ  PHE A 755     -26.318  17.190  27.832  1.00 63.88           C  
-ATOM   1623  N   LEU A 756     -27.267  11.675  28.653  1.00 63.43           N  
-ATOM   1624  CA  LEU A 756     -28.489  11.397  27.913  1.00 56.75           C  
-ATOM   1625  C   LEU A 756     -29.619  10.992  28.868  1.00 56.45           C  
-ATOM   1626  O   LEU A 756     -30.764  11.378  28.676  1.00 52.80           O  
-ATOM   1627  CB  LEU A 756     -28.245  10.321  26.860  1.00 59.13           C  
-ATOM   1628  CG  LEU A 756     -27.167  10.608  25.804  1.00 63.38           C  
-ATOM   1629  CD1 LEU A 756     -26.933   9.388  24.941  1.00 63.52           C  
-ATOM   1630  CD2 LEU A 756     -27.531  11.789  24.936  1.00 61.25           C  
-ATOM   1631  N   ALA A 757     -29.286  10.232  29.908  1.00 57.64           N  
-ATOM   1632  CA  ALA A 757     -30.267   9.839  30.913  1.00 55.76           C  
-ATOM   1633  C   ALA A 757     -30.770  11.064  31.672  1.00 56.52           C  
-ATOM   1634  O   ALA A 757     -31.964  11.195  31.968  1.00 53.34           O  
-ATOM   1635  CB  ALA A 757     -29.663   8.829  31.884  1.00 53.16           C  
-ATOM   1636  N   MET A 758     -29.833  11.946  31.997  1.00 55.94           N  
-ATOM   1637  CA  MET A 758     -30.127  13.154  32.741  1.00 56.90           C  
-ATOM   1638  C   MET A 758     -30.984  14.082  31.882  1.00 56.58           C  
-ATOM   1639  O   MET A 758     -32.018  14.587  32.326  1.00 52.08           O  
-ATOM   1640  CB  MET A 758     -28.817  13.832  33.149  1.00 57.83           C  
-ATOM   1641  CG  MET A 758     -27.968  12.980  34.063  1.00 57.97           C  
-ATOM   1642  SD  MET A 758     -28.841  12.623  35.588  1.00 61.66           S  
-ATOM   1643  CE  MET A 758     -28.840  10.837  35.729  1.00 56.31           C  
-ATOM   1644  N   LEU A 759     -30.543  14.277  30.643  1.00 55.24           N  
-ATOM   1645  CA  LEU A 759     -31.268  15.068  29.669  1.00 52.23           C  
-ATOM   1646  C   LEU A 759     -32.699  14.569  29.506  1.00 53.02           C  
-ATOM   1647  O   LEU A 759     -33.621  15.368  29.418  1.00 52.18           O  
-ATOM   1648  CB  LEU A 759     -30.533  15.048  28.331  1.00 54.57           C  
-ATOM   1649  CG  LEU A 759     -31.042  15.980  27.224  1.00 60.45           C  
-ATOM   1650  CD1 LEU A 759     -31.368  17.356  27.763  1.00 59.24           C  
-ATOM   1651  CD2 LEU A 759     -30.018  16.095  26.109  1.00 60.22           C  
-ATOM   1652  N   MET A 760     -32.892  13.253  29.476  1.00 52.50           N  
-ATOM   1653  CA  MET A 760     -34.241  12.707  29.366  1.00 48.98           C  
-ATOM   1654  C   MET A 760     -35.116  13.151  30.528  1.00 48.52           C  
-ATOM   1655  O   MET A 760     -36.231  13.607  30.317  1.00 46.46           O  
-ATOM   1656  CB  MET A 760     -34.243  11.179  29.271  1.00 48.30           C  
-ATOM   1657  CG  MET A 760     -33.932  10.615  27.882  1.00 52.23           C  
-ATOM   1658  SD  MET A 760     -35.018  11.069  26.492  1.00 51.79           S  
-ATOM   1659  CE  MET A 760     -36.617  10.420  26.985  1.00 41.06           C  
-ATOM   1660  N   THR A 761     -34.604  13.023  31.750  1.00 50.14           N  
-ATOM   1661  CA  THR A 761     -35.372  13.377  32.939  1.00 48.65           C  
-ATOM   1662  C   THR A 761     -35.689  14.874  32.975  1.00 48.67           C  
-ATOM   1663  O   THR A 761     -36.804  15.285  33.308  1.00 47.33           O  
-ATOM   1664  CB  THR A 761     -34.666  12.935  34.227  1.00 51.35           C  
-ATOM   1665  OG1 THR A 761     -34.528  11.506  34.235  1.00 51.73           O  
-ATOM   1666  CG2 THR A 761     -35.486  13.355  35.442  1.00 48.91           C  
-ATOM   1667  N   ALA A 762     -34.713  15.680  32.588  1.00 47.65           N  
-ATOM   1668  CA  ALA A 762     -34.905  17.119  32.488  1.00 48.55           C  
-ATOM   1669  C   ALA A 762     -36.085  17.526  31.588  1.00 49.63           C  
-ATOM   1670  O   ALA A 762     -36.843  18.441  31.932  1.00 48.06           O  
-ATOM   1671  CB  ALA A 762     -33.617  17.802  32.036  1.00 46.68           C  
-ATOM   1672  N   CYS A 763     -36.244  16.869  30.441  1.00 46.02           N  
-ATOM   1673  CA  CYS A 763     -37.335  17.238  29.540  1.00 48.86           C  
-ATOM   1674  C   CYS A 763     -38.655  16.741  30.089  1.00 50.35           C  
-ATOM   1675  O   CYS A 763     -39.674  17.420  30.002  1.00 47.57           O  
-ATOM   1676  CB  CYS A 763     -37.126  16.659  28.151  1.00 46.28           C  
-ATOM   1677  SG  CYS A 763     -35.643  17.254  27.384  1.00 56.39           S  
-ATOM   1678  N   ASP A 764     -38.609  15.536  30.644  1.00 50.27           N  
-ATOM   1679  CA  ASP A 764     -39.770  14.869  31.198  1.00 48.91           C  
-ATOM   1680  C   ASP A 764     -40.375  15.720  32.312  1.00 50.15           C  
-ATOM   1681  O   ASP A 764     -41.595  15.796  32.443  1.00 50.85           O  
-ATOM   1682  CB  ASP A 764     -39.354  13.482  31.731  1.00 49.96           C  
-ATOM   1683  CG  ASP A 764     -40.540  12.561  31.975  1.00 53.93           C  
-ATOM   1684  OD1 ASP A 764     -41.666  12.961  31.620  1.00 56.69           O  
-ATOM   1685  OD2 ASP A 764     -40.363  11.432  32.490  1.00 58.14           O  
-ATOM   1686  N   LEU A 765     -39.530  16.364  33.113  1.00 47.56           N  
-ATOM   1687  CA  LEU A 765     -40.034  17.155  34.243  1.00 51.90           C  
-ATOM   1688  C   LEU A 765     -40.184  18.637  33.919  1.00 53.14           C  
-ATOM   1689  O   LEU A 765     -40.446  19.436  34.819  1.00 52.80           O  
-ATOM   1690  CB  LEU A 765     -39.120  17.029  35.467  1.00 49.18           C  
-ATOM   1691  CG  LEU A 765     -38.748  15.616  35.932  1.00 50.13           C  
-ATOM   1692  CD1 LEU A 765     -37.694  15.686  37.004  1.00 45.32           C  
-ATOM   1693  CD2 LEU A 765     -39.951  14.800  36.390  1.00 43.91           C  
-ATOM   1694  N   SER A 766     -40.010  18.999  32.649  1.00 47.09           N  
-ATOM   1695  CA  SER A 766     -39.854  20.397  32.275  1.00 46.45           C  
-ATOM   1696  C   SER A 766     -41.099  21.243  32.520  1.00 47.83           C  
-ATOM   1697  O   SER A 766     -41.023  22.465  32.550  1.00 48.57           O  
-ATOM   1698  CB  SER A 766     -39.375  20.526  30.822  1.00 48.51           C  
-ATOM   1699  OG  SER A 766     -40.295  19.951  29.908  1.00 51.20           O  
-ATOM   1700  N   ALA A 767     -42.243  20.596  32.691  1.00 44.87           N  
-ATOM   1701  CA  ALA A 767     -43.454  21.313  33.038  1.00 45.45           C  
-ATOM   1702  C   ALA A 767     -43.217  22.228  34.255  1.00 52.17           C  
-ATOM   1703  O   ALA A 767     -43.788  23.317  34.352  1.00 51.65           O  
-ATOM   1704  CB  ALA A 767     -44.560  20.341  33.312  1.00 43.63           C  
-ATOM   1705  N   ILE A 768     -42.351  21.776  35.161  1.00 49.94           N  
-ATOM   1706  CA  ILE A 768     -42.016  22.491  36.380  1.00 49.97           C  
-ATOM   1707  C   ILE A 768     -41.264  23.797  36.101  1.00 54.15           C  
-ATOM   1708  O   ILE A 768     -41.075  24.647  37.000  1.00 53.50           O  
-ATOM   1709  CB  ILE A 768     -41.151  21.600  37.312  1.00 51.59           C  
-ATOM   1710  CG1 ILE A 768     -41.258  22.097  38.748  1.00 50.47           C  
-ATOM   1711  CG2 ILE A 768     -39.675  21.554  36.835  1.00 48.67           C  
-ATOM   1712  CD1 ILE A 768     -42.662  22.159  39.254  1.00 50.32           C  
-ATOM   1713  N   THR A 769     -40.825  23.962  34.859  1.00 48.42           N  
-ATOM   1714  CA  THR A 769     -39.990  25.109  34.535  1.00 52.81           C  
-ATOM   1715  C   THR A 769     -40.783  26.178  33.801  1.00 51.65           C  
-ATOM   1716  O   THR A 769     -40.243  27.227  33.420  1.00 47.37           O  
-ATOM   1717  CB  THR A 769     -38.767  24.701  33.691  1.00 51.96           C  
-ATOM   1718  OG1 THR A 769     -39.210  24.211  32.423  1.00 47.85           O  
-ATOM   1719  CG2 THR A 769     -37.973  23.634  34.400  1.00 49.43           C  
-ATOM   1720  N   LYS A 770     -42.071  25.906  33.619  1.00 49.19           N  
-ATOM   1721  CA  LYS A 770     -42.893  26.732  32.748  1.00 51.23           C  
-ATOM   1722  C   LYS A 770     -43.326  28.052  33.397  1.00 54.78           C  
-ATOM   1723  O   LYS A 770     -43.251  28.212  34.617  1.00 54.85           O  
-ATOM   1724  CB  LYS A 770     -44.105  25.938  32.257  1.00 50.37           C  
-ATOM   1725  CG  LYS A 770     -43.769  24.793  31.353  1.00 45.00           C  
-ATOM   1726  CD  LYS A 770     -43.264  25.275  30.011  1.00 49.61           C  
-ATOM   1727  CE  LYS A 770     -42.903  24.101  29.112  1.00 52.59           C  
-ATOM   1728  NZ  LYS A 770     -42.629  24.509  27.700  1.00 56.33           N  
-ATOM   1729  N   PRO A 771     -43.760  29.020  32.573  1.00 55.61           N  
-ATOM   1730  CA  PRO A 771     -44.307  30.241  33.166  1.00 50.65           C  
-ATOM   1731  C   PRO A 771     -45.459  29.903  34.108  1.00 54.30           C  
-ATOM   1732  O   PRO A 771     -46.236  28.977  33.854  1.00 54.39           O  
-ATOM   1733  CB  PRO A 771     -44.790  31.018  31.945  1.00 45.53           C  
-ATOM   1734  CG  PRO A 771     -43.890  30.571  30.865  1.00 48.80           C  
-ATOM   1735  CD  PRO A 771     -43.681  29.113  31.104  1.00 49.85           C  
-ATOM   1736  N   TRP A 772     -45.560  30.664  35.191  1.00 58.67           N  
-ATOM   1737  CA  TRP A 772     -46.453  30.340  36.298  1.00 58.97           C  
-ATOM   1738  C   TRP A 772     -47.898  30.013  35.896  1.00 56.83           C  
-ATOM   1739  O   TRP A 772     -48.458  29.008  36.342  1.00 57.64           O  
-ATOM   1740  CB  TRP A 772     -46.394  31.453  37.343  1.00 63.19           C  
-ATOM   1741  CG  TRP A 772     -47.359  31.305  38.484  1.00 65.42           C  
-ATOM   1742  CD1 TRP A 772     -48.372  32.160  38.820  1.00 62.71           C  
-ATOM   1743  CD2 TRP A 772     -47.397  30.243  39.441  1.00 65.12           C  
-ATOM   1744  NE1 TRP A 772     -49.034  31.696  39.925  1.00 64.27           N  
-ATOM   1745  CE2 TRP A 772     -48.458  30.518  40.326  1.00 67.38           C  
-ATOM   1746  CE3 TRP A 772     -46.635  29.088  39.638  1.00 65.34           C  
-ATOM   1747  CZ2 TRP A 772     -48.774  29.678  41.395  1.00 66.05           C  
-ATOM   1748  CZ3 TRP A 772     -46.952  28.252  40.701  1.00 64.27           C  
-ATOM   1749  CH2 TRP A 772     -48.010  28.552  41.564  1.00 66.49           C  
-ATOM   1750  N   PRO A 773     -48.505  30.851  35.054  1.00 54.56           N  
-ATOM   1751  CA  PRO A 773     -49.885  30.557  34.637  1.00 59.01           C  
-ATOM   1752  C   PRO A 773     -50.006  29.184  33.988  1.00 56.62           C  
-ATOM   1753  O   PRO A 773     -51.047  28.544  34.064  1.00 59.48           O  
-ATOM   1754  CB  PRO A 773     -50.188  31.653  33.613  1.00 57.21           C  
-ATOM   1755  CG  PRO A 773     -49.262  32.773  33.983  1.00 58.43           C  
-ATOM   1756  CD  PRO A 773     -48.014  32.125  34.509  1.00 55.86           C  
-ATOM   1757  N   ILE A 774     -48.931  28.722  33.373  1.00 52.77           N  
-ATOM   1758  CA  ILE A 774     -48.949  27.422  32.735  1.00 53.39           C  
-ATOM   1759  C   ILE A 774     -48.609  26.305  33.718  1.00 54.08           C  
-ATOM   1760  O   ILE A 774     -49.328  25.297  33.812  1.00 54.10           O  
-ATOM   1761  CB  ILE A 774     -48.042  27.424  31.488  1.00 56.74           C  
-ATOM   1762  CG1 ILE A 774     -48.706  28.275  30.401  1.00 52.48           C  
-ATOM   1763  CG2 ILE A 774     -47.793  26.015  30.981  1.00 50.81           C  
-ATOM   1764  CD1 ILE A 774     -47.943  28.332  29.164  1.00 56.91           C  
-ATOM   1765  N   GLN A 775     -47.531  26.495  34.470  1.00 50.46           N  
-ATOM   1766  CA  GLN A 775     -47.228  25.582  35.569  1.00 54.59           C  
-ATOM   1767  C   GLN A 775     -48.436  25.338  36.484  1.00 51.73           C  
-ATOM   1768  O   GLN A 775     -48.707  24.208  36.865  1.00 52.16           O  
-ATOM   1769  CB  GLN A 775     -45.997  26.046  36.363  1.00 55.23           C  
-ATOM   1770  CG  GLN A 775     -45.853  25.427  37.753  1.00 53.00           C  
-ATOM   1771  CD  GLN A 775     -45.798  23.904  37.772  1.00 49.66           C  
-ATOM   1772  OE1 GLN A 775     -45.426  23.250  36.792  1.00 49.21           O  
-ATOM   1773  NE2 GLN A 775     -46.182  23.331  38.902  1.00 50.17           N  
-ATOM   1774  N   GLN A 776     -49.192  26.375  36.803  1.00 53.85           N  
-ATOM   1775  CA  GLN A 776     -50.380  26.156  37.626  1.00 57.31           C  
-ATOM   1776  C   GLN A 776     -51.341  25.174  36.996  1.00 55.13           C  
-ATOM   1777  O   GLN A 776     -51.925  24.339  37.686  1.00 57.63           O  
-ATOM   1778  CB  GLN A 776     -51.120  27.452  37.884  1.00 58.32           C  
-ATOM   1779  CG  GLN A 776     -50.407  28.346  38.840  1.00 66.62           C  
-ATOM   1780  CD  GLN A 776     -51.280  29.481  39.316  1.00 73.79           C  
-ATOM   1781  OE1 GLN A 776     -51.957  29.366  40.349  1.00 75.04           O  
-ATOM   1782  NE2 GLN A 776     -51.278  30.591  38.565  1.00 69.04           N  
-ATOM   1783  N   ARG A 777     -51.513  25.280  35.686  1.00 53.04           N  
-ATOM   1784  CA  ARG A 777     -52.499  24.467  34.999  1.00 54.19           C  
-ATOM   1785  C   ARG A 777     -52.035  23.025  34.880  1.00 53.94           C  
-ATOM   1786  O   ARG A 777     -52.814  22.088  35.072  1.00 53.49           O  
-ATOM   1787  CB  ARG A 777     -52.809  25.062  33.627  1.00 59.43           C  
-ATOM   1788  CG  ARG A 777     -53.412  26.470  33.688  1.00 57.36           C  
-ATOM   1789  CD  ARG A 777     -54.891  26.476  34.109  1.00 58.43           C  
-ATOM   1790  NE  ARG A 777     -55.514  27.763  33.806  1.00 61.89           N  
-ATOM   1791  CZ  ARG A 777     -56.750  28.120  34.150  1.00 60.75           C  
-ATOM   1792  NH1 ARG A 777     -57.533  27.293  34.834  1.00 56.19           N  
-ATOM   1793  NH2 ARG A 777     -57.196  29.325  33.813  1.00 62.43           N  
-ATOM   1794  N   ILE A 778     -50.754  22.839  34.588  1.00 54.53           N  
-ATOM   1795  CA  ILE A 778     -50.204  21.487  34.581  1.00 53.55           C  
-ATOM   1796  C   ILE A 778     -50.306  20.865  35.980  1.00 51.99           C  
-ATOM   1797  O   ILE A 778     -50.834  19.772  36.129  1.00 52.14           O  
-ATOM   1798  CB  ILE A 778     -48.769  21.450  33.986  1.00 53.81           C  
-ATOM   1799  CG1 ILE A 778     -48.850  21.588  32.464  1.00 54.45           C  
-ATOM   1800  CG2 ILE A 778     -48.070  20.140  34.272  1.00 47.97           C  
-ATOM   1801  CD1 ILE A 778     -47.896  22.578  31.914  1.00 54.35           C  
-ATOM   1802  N   ALA A 779     -49.841  21.580  37.001  1.00 51.30           N  
-ATOM   1803  CA  ALA A 779     -49.971  21.113  38.376  1.00 51.54           C  
-ATOM   1804  C   ALA A 779     -51.393  20.652  38.630  1.00 53.64           C  
-ATOM   1805  O   ALA A 779     -51.645  19.689  39.344  1.00 56.77           O  
-ATOM   1806  CB  ALA A 779     -49.588  22.198  39.348  1.00 48.75           C  
-ATOM   1807  N   GLU A 780     -52.342  21.337  38.028  1.00 55.79           N  
-ATOM   1808  CA  GLU A 780     -53.726  20.947  38.206  1.00 57.16           C  
-ATOM   1809  C   GLU A 780     -54.062  19.623  37.497  1.00 60.31           C  
-ATOM   1810  O   GLU A 780     -54.776  18.791  38.046  1.00 60.76           O  
-ATOM   1811  CB  GLU A 780     -54.623  22.071  37.749  1.00 52.30           C  
-ATOM   1812  CG  GLU A 780     -56.060  21.748  37.821  1.00 63.28           C  
-ATOM   1813  CD  GLU A 780     -56.903  22.960  37.477  1.00 73.54           C  
-ATOM   1814  OE1 GLU A 780     -56.293  24.060  37.342  1.00 63.21           O  
-ATOM   1815  OE2 GLU A 780     -58.151  22.801  37.333  1.00 71.53           O  
-ATOM   1816  N   LEU A 781     -53.540  19.423  36.288  1.00 55.65           N  
-ATOM   1817  CA  LEU A 781     -53.650  18.119  35.638  1.00 55.72           C  
-ATOM   1818  C   LEU A 781     -53.000  16.994  36.446  1.00 57.28           C  
-ATOM   1819  O   LEU A 781     -53.567  15.913  36.590  1.00 53.80           O  
-ATOM   1820  CB  LEU A 781     -53.025  18.147  34.247  1.00 55.17           C  
-ATOM   1821  CG  LEU A 781     -53.687  19.032  33.196  1.00 57.64           C  
-ATOM   1822  CD1 LEU A 781     -52.816  19.100  31.957  1.00 51.51           C  
-ATOM   1823  CD2 LEU A 781     -55.090  18.545  32.867  1.00 54.07           C  
-ATOM   1824  N   VAL A 782     -51.793  17.246  36.940  1.00 55.28           N  
-ATOM   1825  CA  VAL A 782     -51.070  16.253  37.703  1.00 55.26           C  
-ATOM   1826  C   VAL A 782     -51.883  15.886  38.943  1.00 60.25           C  
-ATOM   1827  O   VAL A 782     -51.962  14.724  39.339  1.00 62.78           O  
-ATOM   1828  CB  VAL A 782     -49.688  16.785  38.118  1.00 58.33           C  
-ATOM   1829  CG1 VAL A 782     -49.026  15.851  39.107  1.00 62.63           C  
-ATOM   1830  CG2 VAL A 782     -48.804  17.016  36.905  1.00 52.92           C  
-ATOM   1831  N   ALA A 783     -52.504  16.887  39.547  1.00 62.63           N  
-ATOM   1832  CA  ALA A 783     -53.270  16.686  40.768  1.00 63.47           C  
-ATOM   1833  C   ALA A 783     -54.463  15.787  40.505  1.00 64.48           C  
-ATOM   1834  O   ALA A 783     -54.800  14.936  41.325  1.00 67.85           O  
-ATOM   1835  CB  ALA A 783     -53.725  18.024  41.318  1.00 60.76           C  
-ATOM   1836  N   THR A 784     -55.102  15.992  39.356  1.00 61.25           N  
-ATOM   1837  CA  THR A 784     -56.270  15.216  38.964  1.00 65.30           C  
-ATOM   1838  C   THR A 784     -55.932  13.740  38.790  1.00 67.30           C  
-ATOM   1839  O   THR A 784     -56.718  12.855  39.123  1.00 70.92           O  
-ATOM   1840  CB  THR A 784     -56.833  15.715  37.627  1.00 66.03           C  
-ATOM   1841  OG1 THR A 784     -57.351  17.035  37.787  1.00 65.12           O  
-ATOM   1842  CG2 THR A 784     -57.939  14.795  37.120  1.00 62.27           C  
-ATOM   1843  N   GLU A 785     -54.764  13.477  38.234  1.00 62.26           N  
-ATOM   1844  CA  GLU A 785     -54.360  12.111  38.012  1.00 64.08           C  
-ATOM   1845  C   GLU A 785     -53.964  11.478  39.337  1.00 65.04           C  
-ATOM   1846  O   GLU A 785     -54.303  10.333  39.604  1.00 67.77           O  
-ATOM   1847  CB  GLU A 785     -53.212  12.048  37.004  1.00 60.84           C  
-ATOM   1848  CG  GLU A 785     -52.752  10.642  36.692  1.00 63.07           C  
-ATOM   1849  CD  GLU A 785     -51.645  10.573  35.648  1.00 65.73           C  
-ATOM   1850  OE1 GLU A 785     -50.733   9.742  35.849  1.00 63.24           O  
-ATOM   1851  OE2 GLU A 785     -51.690  11.324  34.634  1.00 61.52           O  
-ATOM   1852  N   PHE A 786     -53.264  12.241  40.169  1.00 65.73           N  
-ATOM   1853  CA  PHE A 786     -52.779  11.750  41.461  1.00 68.91           C  
-ATOM   1854  C   PHE A 786     -53.872  11.380  42.446  1.00 70.25           C  
-ATOM   1855  O   PHE A 786     -53.728  10.428  43.202  1.00 72.95           O  
-ATOM   1856  CB  PHE A 786     -51.849  12.771  42.129  1.00 67.39           C  
-ATOM   1857  CG  PHE A 786     -50.438  12.747  41.599  1.00 74.03           C  
-ATOM   1858  CD1 PHE A 786     -50.180  12.387  40.281  1.00 71.37           C  
-ATOM   1859  CD2 PHE A 786     -49.366  13.064  42.423  1.00 77.28           C  
-ATOM   1860  CE1 PHE A 786     -48.886  12.353  39.794  1.00 70.76           C  
-ATOM   1861  CE2 PHE A 786     -48.067  13.031  41.941  1.00 77.13           C  
-ATOM   1862  CZ  PHE A 786     -47.827  12.678  40.624  1.00 75.93           C  
-ATOM   1863  N   PHE A 787     -54.964  12.130  42.432  1.00 71.30           N  
-ATOM   1864  CA  PHE A 787     -55.899  12.088  43.540  1.00 75.54           C  
-ATOM   1865  C   PHE A 787     -57.303  11.730  43.124  1.00 78.52           C  
-ATOM   1866  O   PHE A 787     -58.095  11.291  43.950  1.00 85.03           O  
-ATOM   1867  CB  PHE A 787     -55.921  13.441  44.249  1.00 71.44           C  
-ATOM   1868  CG  PHE A 787     -54.594  13.848  44.797  1.00 71.85           C  
-ATOM   1869  CD1 PHE A 787     -54.166  15.161  44.706  1.00 72.95           C  
-ATOM   1870  CD2 PHE A 787     -53.768  12.909  45.410  1.00 75.33           C  
-ATOM   1871  CE1 PHE A 787     -52.933  15.539  45.216  1.00 75.51           C  
-ATOM   1872  CE2 PHE A 787     -52.534  13.273  45.926  1.00 74.89           C  
-ATOM   1873  CZ  PHE A 787     -52.113  14.592  45.827  1.00 78.00           C  
-ATOM   1874  N   ASP A 788     -57.620  11.926  41.853  1.00 75.10           N  
-ATOM   1875  CA  ASP A 788     -59.001  11.765  41.417  1.00 79.64           C  
-ATOM   1876  C   ASP A 788     -59.185  10.639  40.420  1.00 79.58           C  
-ATOM   1877  O   ASP A 788     -60.268  10.483  39.856  1.00 85.25           O  
-ATOM   1878  CB  ASP A 788     -59.540  13.066  40.810  1.00 82.12           C  
-ATOM   1879  CG  ASP A 788     -59.448  14.242  41.767  1.00 89.12           C  
-ATOM   1880  OD1 ASP A 788     -58.444  14.328  42.517  1.00 90.81           O  
-ATOM   1881  OD2 ASP A 788     -60.380  15.077  41.770  1.00 90.10           O  
-ATOM   1882  N   GLN A 789     -58.134   9.865  40.185  1.00 75.98           N  
-ATOM   1883  CA  GLN A 789     -58.228   8.772  39.222  1.00 80.77           C  
-ATOM   1884  C   GLN A 789     -57.534   7.548  39.789  1.00 80.28           C  
-ATOM   1885  O   GLN A 789     -56.755   7.670  40.737  1.00 79.73           O  
-ATOM   1886  CB  GLN A 789     -57.626   9.173  37.862  1.00 76.50           C  
-ATOM   1887  CG  GLN A 789     -58.180  10.485  37.268  1.00 71.86           C  
-ATOM   1888  CD  GLN A 789     -57.737  10.749  35.809  1.00 74.70           C  
-ATOM   1889  OE1 GLN A 789     -58.519  11.260  34.996  1.00 73.22           O  
-ATOM   1890  NE2 GLN A 789     -56.482  10.413  35.483  1.00 68.46           N  
-ATOM   1891  N   LYS A 809     -56.922  17.718  50.693  1.00108.66           N  
-ATOM   1892  CA  LYS A 809     -57.319  18.953  50.015  1.00109.79           C  
-ATOM   1893  C   LYS A 809     -56.239  19.471  49.051  1.00101.35           C  
-ATOM   1894  O   LYS A 809     -55.122  18.932  48.987  1.00 92.83           O  
-ATOM   1895  CB  LYS A 809     -57.682  20.039  51.042  1.00 98.21           C  
-ATOM   1896  N   LYS A 810     -56.593  20.518  48.306  1.00 98.36           N  
-ATOM   1897  CA  LYS A 810     -55.649  21.227  47.442  1.00 95.32           C  
-ATOM   1898  C   LYS A 810     -54.759  22.171  48.272  1.00 90.86           C  
-ATOM   1899  O   LYS A 810     -53.985  22.965  47.728  1.00 81.34           O  
-ATOM   1900  CB  LYS A 810     -56.402  22.000  46.347  1.00 89.72           C  
-ATOM   1901  N   ASN A 811     -54.885  22.074  49.596  1.00 95.76           N  
-ATOM   1902  CA  ASN A 811     -54.082  22.867  50.521  1.00 89.48           C  
-ATOM   1903  C   ASN A 811     -52.674  22.295  50.671  1.00 82.47           C  
-ATOM   1904  O   ASN A 811     -51.715  23.035  50.891  1.00 80.45           O  
-ATOM   1905  CB  ASN A 811     -54.768  22.954  51.893  1.00 91.39           C  
-ATOM   1906  N   LYS A 812     -52.558  20.977  50.538  1.00 80.27           N  
-ATOM   1907  CA  LYS A 812     -51.281  20.298  50.725  1.00 78.91           C  
-ATOM   1908  C   LYS A 812     -50.409  20.390  49.483  1.00 73.78           C  
-ATOM   1909  O   LYS A 812     -49.214  20.095  49.535  1.00 73.18           O  
-ATOM   1910  CB  LYS A 812     -51.508  18.826  51.086  1.00 81.98           C  
-ATOM   1911  N   ILE A 813     -51.010  20.822  48.378  1.00 69.13           N  
-ATOM   1912  CA  ILE A 813     -50.359  20.799  47.078  1.00 62.26           C  
-ATOM   1913  C   ILE A 813     -49.201  21.780  46.892  1.00 62.60           C  
-ATOM   1914  O   ILE A 813     -48.181  21.424  46.316  1.00 66.73           O  
-ATOM   1915  CB  ILE A 813     -51.396  20.944  45.950  1.00 68.65           C  
-ATOM   1916  CG1 ILE A 813     -52.097  19.601  45.731  1.00 70.31           C  
-ATOM   1917  CG2 ILE A 813     -50.753  21.443  44.662  1.00 58.25           C  
-ATOM   1918  CD1 ILE A 813     -53.373  19.696  44.948  1.00 73.75           C  
-ATOM   1919  N   PRO A 814     -49.337  23.021  47.370  1.00 63.84           N  
-ATOM   1920  CA  PRO A 814     -48.174  23.878  47.111  1.00 62.30           C  
-ATOM   1921  C   PRO A 814     -46.953  23.362  47.849  1.00 64.07           C  
-ATOM   1922  O   PRO A 814     -45.812  23.620  47.458  1.00 63.30           O  
-ATOM   1923  CB  PRO A 814     -48.613  25.243  47.661  1.00 61.25           C  
-ATOM   1924  CG  PRO A 814     -50.112  25.209  47.593  1.00 58.54           C  
-ATOM   1925  CD  PRO A 814     -50.487  23.783  47.889  1.00 65.08           C  
-ATOM   1926  N   SER A 815     -47.212  22.625  48.921  1.00 68.16           N  
-ATOM   1927  CA  SER A 815     -46.166  22.078  49.767  1.00 66.50           C  
-ATOM   1928  C   SER A 815     -45.435  20.968  49.030  1.00 64.06           C  
-ATOM   1929  O   SER A 815     -44.208  20.973  48.907  1.00 61.47           O  
-ATOM   1930  CB  SER A 815     -46.789  21.533  51.047  1.00 69.49           C  
-ATOM   1931  OG  SER A 815     -45.880  20.691  51.734  1.00 78.91           O  
-ATOM   1932  N   MET A 816     -46.209  20.013  48.541  1.00 60.49           N  
-ATOM   1933  CA  MET A 816     -45.673  18.962  47.693  1.00 66.62           C  
-ATOM   1934  C   MET A 816     -44.868  19.525  46.517  1.00 63.88           C  
-ATOM   1935  O   MET A 816     -43.802  19.013  46.182  1.00 62.84           O  
-ATOM   1936  CB  MET A 816     -46.809  18.083  47.180  1.00 67.06           C  
-ATOM   1937  CG  MET A 816     -47.634  17.484  48.297  1.00 66.04           C  
-ATOM   1938  SD  MET A 816     -49.080  16.613  47.685  1.00 73.94           S  
-ATOM   1939  CE  MET A 816     -48.262  15.294  46.798  1.00 79.41           C  
-ATOM   1940  N   GLN A 817     -45.369  20.579  45.892  1.00 57.93           N  
-ATOM   1941  CA  GLN A 817     -44.655  21.140  44.756  1.00 61.70           C  
-ATOM   1942  C   GLN A 817     -43.256  21.610  45.145  1.00 61.92           C  
-ATOM   1943  O   GLN A 817     -42.290  21.390  44.399  1.00 58.16           O  
-ATOM   1944  CB  GLN A 817     -45.449  22.273  44.099  1.00 61.49           C  
-ATOM   1945  CG  GLN A 817     -46.627  21.809  43.266  1.00 60.08           C  
-ATOM   1946  CD  GLN A 817     -46.264  20.678  42.325  1.00 60.77           C  
-ATOM   1947  OE1 GLN A 817     -46.207  19.519  42.734  1.00 62.24           O  
-ATOM   1948  NE2 GLN A 817     -46.026  21.005  41.055  1.00 55.76           N  
-ATOM   1949  N   VAL A 818     -43.152  22.258  46.309  1.00 63.61           N  
-ATOM   1950  CA  VAL A 818     -41.866  22.768  46.793  1.00 62.22           C  
-ATOM   1951  C   VAL A 818     -40.944  21.594  47.114  1.00 60.10           C  
-ATOM   1952  O   VAL A 818     -39.745  21.623  46.797  1.00 56.77           O  
-ATOM   1953  CB  VAL A 818     -42.013  23.683  48.040  1.00 62.26           C  
-ATOM   1954  CG1 VAL A 818     -40.648  24.112  48.531  1.00 57.72           C  
-ATOM   1955  CG2 VAL A 818     -42.861  24.908  47.725  1.00 59.12           C  
-ATOM   1956  N   GLY A 819     -41.521  20.556  47.719  1.00 55.33           N  
-ATOM   1957  CA  GLY A 819     -40.804  19.323  47.985  1.00 56.67           C  
-ATOM   1958  C   GLY A 819     -40.257  18.687  46.724  1.00 59.12           C  
-ATOM   1959  O   GLY A 819     -39.094  18.301  46.650  1.00 57.74           O  
-ATOM   1960  N   PHE A 820     -41.109  18.598  45.714  1.00 60.74           N  
-ATOM   1961  CA  PHE A 820     -40.742  18.042  44.419  1.00 59.31           C  
-ATOM   1962  C   PHE A 820     -39.613  18.854  43.770  1.00 58.14           C  
-ATOM   1963  O   PHE A 820     -38.627  18.303  43.274  1.00 56.60           O  
-ATOM   1964  CB  PHE A 820     -42.013  17.982  43.567  1.00 61.67           C  
-ATOM   1965  CG  PHE A 820     -41.785  17.723  42.130  1.00 61.78           C  
-ATOM   1966  CD1 PHE A 820     -41.092  16.605  41.713  1.00 66.23           C  
-ATOM   1967  CD2 PHE A 820     -42.309  18.582  41.182  1.00 61.19           C  
-ATOM   1968  CE1 PHE A 820     -40.902  16.361  40.371  1.00 64.90           C  
-ATOM   1969  CE2 PHE A 820     -42.129  18.349  39.841  1.00 60.06           C  
-ATOM   1970  CZ  PHE A 820     -41.424  17.237  39.430  1.00 62.74           C  
-ATOM   1971  N   ILE A 821     -39.730  20.172  43.805  1.00 56.88           N  
-ATOM   1972  CA  ILE A 821     -38.689  21.010  43.220  1.00 58.49           C  
-ATOM   1973  C   ILE A 821     -37.362  20.843  43.947  1.00 60.27           C  
-ATOM   1974  O   ILE A 821     -36.312  20.693  43.309  1.00 59.62           O  
-ATOM   1975  CB  ILE A 821     -39.080  22.489  43.252  1.00 57.69           C  
-ATOM   1976  CG1 ILE A 821     -40.376  22.711  42.479  1.00 58.39           C  
-ATOM   1977  CG2 ILE A 821     -37.958  23.366  42.713  1.00 54.10           C  
-ATOM   1978  CD1 ILE A 821     -40.790  24.159  42.436  1.00 62.45           C  
-ATOM   1979  N   ASP A 822     -37.411  20.875  45.280  1.00 55.56           N  
-ATOM   1980  CA  ASP A 822     -36.205  20.712  46.093  1.00 59.35           C  
-ATOM   1981  C   ASP A 822     -35.512  19.371  45.917  1.00 58.84           C  
-ATOM   1982  O   ASP A 822     -34.302  19.312  45.714  1.00 58.93           O  
-ATOM   1983  CB  ASP A 822     -36.524  20.894  47.572  1.00 61.91           C  
-ATOM   1984  CG  ASP A 822     -36.660  22.347  47.953  1.00 69.29           C  
-ATOM   1985  OD1 ASP A 822     -36.300  23.203  47.099  1.00 62.91           O  
-ATOM   1986  OD2 ASP A 822     -37.118  22.622  49.094  1.00 70.70           O  
-ATOM   1987  N   ALA A 823     -36.299  18.306  46.007  1.00 53.63           N  
-ATOM   1988  CA  ALA A 823     -35.797  16.947  45.964  1.00 51.15           C  
-ATOM   1989  C   ALA A 823     -35.239  16.581  44.598  1.00 59.62           C  
-ATOM   1990  O   ALA A 823     -34.204  15.925  44.501  1.00 64.24           O  
-ATOM   1991  CB  ALA A 823     -36.906  15.978  46.338  1.00 51.17           C  
-ATOM   1992  N   ILE A 824     -35.921  17.014  43.545  1.00 55.32           N  
-ATOM   1993  CA  ILE A 824     -35.697  16.447  42.226  1.00 56.65           C  
-ATOM   1994  C   ILE A 824     -35.190  17.467  41.210  1.00 61.27           C  
-ATOM   1995  O   ILE A 824     -34.144  17.270  40.590  1.00 66.44           O  
-ATOM   1996  CB  ILE A 824     -37.008  15.797  41.686  1.00 58.92           C  
-ATOM   1997  CG1 ILE A 824     -37.487  14.680  42.617  1.00 55.61           C  
-ATOM   1998  CG2 ILE A 824     -36.826  15.286  40.272  1.00 53.53           C  
-ATOM   1999  N   CYS A 825     -35.920  18.564  41.053  1.00 56.20           N  
-ATOM   2000  CA  CYS A 825     -35.738  19.414  39.885  1.00 56.26           C  
-ATOM   2001  C   CYS A 825     -34.592  20.426  39.921  1.00 57.80           C  
-ATOM   2002  O   CYS A 825     -33.846  20.525  38.941  1.00 57.08           O  
-ATOM   2003  CB  CYS A 825     -37.048  20.115  39.543  1.00 60.02           C  
-ATOM   2004  SG  CYS A 825     -38.449  19.005  39.621  1.00 63.79           S  
-ATOM   2005  N   LEU A 826     -34.450  21.179  41.014  1.00 54.09           N  
-ATOM   2006  CA  LEU A 826     -33.452  22.257  41.042  1.00 57.88           C  
-ATOM   2007  C   LEU A 826     -32.030  21.782  40.735  1.00 61.33           C  
-ATOM   2008  O   LEU A 826     -31.355  22.352  39.870  1.00 57.98           O  
-ATOM   2009  CB  LEU A 826     -33.484  23.058  42.356  1.00 62.42           C  
-ATOM   2010  CG  LEU A 826     -34.257  24.390  42.381  1.00 55.00           C  
-ATOM   2011  N   GLN A 827     -31.577  20.738  41.425  1.00 61.64           N  
-ATOM   2012  CA  GLN A 827     -30.221  20.243  41.197  1.00 65.33           C  
-ATOM   2013  C   GLN A 827     -30.013  19.835  39.738  1.00 64.43           C  
-ATOM   2014  O   GLN A 827     -29.001  20.170  39.110  1.00 63.62           O  
-ATOM   2015  CB  GLN A 827     -29.902  19.080  42.129  1.00 68.27           C  
-ATOM   2016  CG  GLN A 827     -29.551  19.518  43.541  1.00 75.41           C  
-ATOM   2017  CD  GLN A 827     -29.294  18.341  44.475  1.00 84.15           C  
-ATOM   2018  OE1 GLN A 827     -30.217  17.582  44.812  1.00 82.86           O  
-ATOM   2019  NE2 GLN A 827     -28.033  18.177  44.892  1.00 74.78           N  
-ATOM   2020  N   LEU A 828     -30.986  19.121  39.196  1.00 59.16           N  
-ATOM   2021  CA  LEU A 828     -30.885  18.683  37.832  1.00 57.40           C  
-ATOM   2022  C   LEU A 828     -30.692  19.871  36.897  1.00 58.84           C  
-ATOM   2023  O   LEU A 828     -29.743  19.884  36.118  1.00 58.85           O  
-ATOM   2024  CB  LEU A 828     -32.114  17.869  37.441  1.00 61.57           C  
-ATOM   2025  CG  LEU A 828     -32.157  17.425  35.978  1.00 55.61           C  
-ATOM   2026  CD1 LEU A 828     -31.030  16.443  35.721  1.00 59.29           C  
-ATOM   2027  CD2 LEU A 828     -33.508  16.813  35.644  1.00 53.45           C  
-ATOM   2028  N   TYR A 829     -31.569  20.873  36.973  1.00 56.19           N  
-ATOM   2029  CA  TYR A 829     -31.468  21.997  36.042  1.00 55.92           C  
-ATOM   2030  C   TYR A 829     -30.247  22.883  36.295  1.00 60.01           C  
-ATOM   2031  O   TYR A 829     -29.759  23.567  35.396  1.00 59.54           O  
-ATOM   2032  CB  TYR A 829     -32.744  22.825  36.013  1.00 52.14           C  
-ATOM   2033  CG  TYR A 829     -33.929  22.057  35.502  1.00 53.81           C  
-ATOM   2034  CD1 TYR A 829     -34.974  21.714  36.350  1.00 47.22           C  
-ATOM   2035  CD2 TYR A 829     -34.000  21.655  34.161  1.00 51.57           C  
-ATOM   2036  CE1 TYR A 829     -36.060  21.006  35.882  1.00 52.30           C  
-ATOM   2037  CE2 TYR A 829     -35.091  20.941  33.680  1.00 45.50           C  
-ATOM   2038  CZ  TYR A 829     -36.120  20.620  34.542  1.00 48.41           C  
-ATOM   2039  OH  TYR A 829     -37.204  19.906  34.089  1.00 43.76           O  
-ATOM   2040  N   GLU A 830     -29.757  22.871  37.526  1.00 64.06           N  
-ATOM   2041  CA  GLU A 830     -28.461  23.462  37.811  1.00 65.43           C  
-ATOM   2042  C   GLU A 830     -27.388  22.709  37.025  1.00 66.57           C  
-ATOM   2043  O   GLU A 830     -26.687  23.294  36.200  1.00 66.72           O  
-ATOM   2044  CB  GLU A 830     -28.172  23.436  39.310  1.00 62.98           C  
-ATOM   2045  CG  GLU A 830     -28.356  24.791  39.969  1.00 68.69           C  
-ATOM   2046  CD  GLU A 830     -28.744  24.702  41.442  1.00 76.24           C  
-ATOM   2047  OE1 GLU A 830     -29.482  25.607  41.903  1.00 78.89           O  
-ATOM   2048  OE2 GLU A 830     -28.321  23.739  42.133  1.00 72.94           O  
-ATOM   2049  N   ALA A 831     -27.281  21.407  37.265  1.00 61.78           N  
-ATOM   2050  CA  ALA A 831     -26.335  20.578  36.527  1.00 63.23           C  
-ATOM   2051  C   ALA A 831     -26.406  20.805  35.015  1.00 64.68           C  
-ATOM   2052  O   ALA A 831     -25.401  21.131  34.384  1.00 64.05           O  
-ATOM   2053  CB  ALA A 831     -26.557  19.113  36.858  1.00 64.39           C  
-ATOM   2054  N   LEU A 832     -27.601  20.638  34.447  1.00 64.76           N  
-ATOM   2055  CA  LEU A 832     -27.824  20.842  33.016  1.00 64.68           C  
-ATOM   2056  C   LEU A 832     -27.344  22.217  32.553  1.00 65.62           C  
-ATOM   2057  O   LEU A 832     -26.916  22.403  31.410  1.00 68.31           O  
-ATOM   2058  CB  LEU A 832     -29.305  20.644  32.660  1.00 62.01           C  
-ATOM   2059  CG  LEU A 832     -29.738  21.137  31.264  1.00 65.09           C  
-ATOM   2060  CD1 LEU A 832     -28.987  20.401  30.166  1.00 63.95           C  
-ATOM   2061  CD2 LEU A 832     -31.244  21.027  31.028  1.00 55.92           C  
-ATOM   2062  N   THR A 833     -27.418  23.187  33.446  1.00 66.81           N  
-ATOM   2063  CA  THR A 833     -27.014  24.541  33.098  1.00 71.88           C  
-ATOM   2064  C   THR A 833     -25.490  24.672  33.044  1.00 70.69           C  
-ATOM   2065  O   THR A 833     -24.956  25.474  32.284  1.00 71.24           O  
-ATOM   2066  CB  THR A 833     -27.646  25.569  34.061  1.00 69.03           C  
-ATOM   2067  OG1 THR A 833     -28.989  25.839  33.636  1.00 68.92           O  
-ATOM   2068  CG2 THR A 833     -26.862  26.859  34.063  1.00 68.17           C  
-ATOM   2069  N   HIS A 834     -24.798  23.866  33.841  1.00 68.74           N  
-ATOM   2070  CA  HIS A 834     -23.347  23.814  33.786  1.00 72.71           C  
-ATOM   2071  C   HIS A 834     -22.887  23.208  32.468  1.00 74.87           C  
-ATOM   2072  O   HIS A 834     -22.029  23.757  31.789  1.00 78.13           O  
-ATOM   2073  CB  HIS A 834     -22.780  23.031  34.971  1.00 77.02           C  
-ATOM   2074  CG  HIS A 834     -22.751  23.816  36.247  1.00 88.60           C  
-ATOM   2075  ND1 HIS A 834     -21.817  24.801  36.494  1.00 94.34           N  
-ATOM   2076  CD2 HIS A 834     -23.548  23.772  37.343  1.00 89.33           C  
-ATOM   2077  CE1 HIS A 834     -22.036  25.323  37.689  1.00 98.31           C  
-ATOM   2078  NE2 HIS A 834     -23.080  24.716  38.225  1.00 94.69           N  
-ATOM   2079  N   VAL A 835     -23.463  22.075  32.100  1.00 73.74           N  
-ATOM   2080  CA  VAL A 835     -23.212  21.518  30.784  1.00 70.46           C  
-ATOM   2081  C   VAL A 835     -23.477  22.545  29.674  1.00 76.58           C  
-ATOM   2082  O   VAL A 835     -22.613  22.783  28.825  1.00 75.27           O  
-ATOM   2083  CB  VAL A 835     -24.060  20.272  30.563  1.00 70.90           C  
-ATOM   2084  CG1 VAL A 835     -23.956  19.800  29.124  1.00 73.32           C  
-ATOM   2085  CG2 VAL A 835     -23.606  19.195  31.513  1.00 73.20           C  
-ATOM   2086  N   SER A 836     -24.667  23.150  29.675  1.00 75.30           N  
-ATOM   2087  CA  SER A 836     -24.973  24.205  28.706  1.00 75.90           C  
-ATOM   2088  C   SER A 836     -25.604  25.445  29.335  1.00 76.09           C  
-ATOM   2089  O   SER A 836     -26.720  25.407  29.869  1.00 74.96           O  
-ATOM   2090  CB  SER A 836     -25.847  23.696  27.551  1.00 77.23           C  
-ATOM   2091  OG  SER A 836     -26.027  24.722  26.579  1.00 73.89           O  
-ATOM   2092  N   GLU A 837     -24.873  26.547  29.244  1.00 74.23           N  
-ATOM   2093  CA  GLU A 837     -25.317  27.817  29.783  1.00 74.30           C  
-ATOM   2094  C   GLU A 837     -26.620  28.289  29.155  1.00 72.62           C  
-ATOM   2095  O   GLU A 837     -27.274  29.185  29.683  1.00 71.50           O  
-ATOM   2096  CB  GLU A 837     -24.233  28.880  29.580  1.00 77.50           C  
-ATOM   2097  N   ASP A 838     -27.010  27.700  28.032  1.00 71.24           N  
-ATOM   2098  CA  ASP A 838     -28.203  28.198  27.352  1.00 70.37           C  
-ATOM   2099  C   ASP A 838     -29.484  27.496  27.780  1.00 71.32           C  
-ATOM   2100  O   ASP A 838     -30.558  27.815  27.284  1.00 67.94           O  
-ATOM   2101  CB  ASP A 838     -28.026  28.147  25.845  1.00 72.31           C  
-ATOM   2102  CG  ASP A 838     -26.807  28.930  25.387  1.00 83.08           C  
-ATOM   2103  OD1 ASP A 838     -26.988  29.998  24.748  1.00 82.34           O  
-ATOM   2104  OD2 ASP A 838     -25.671  28.484  25.691  1.00 82.86           O  
-ATOM   2105  N   CYS A 839     -29.358  26.547  28.707  1.00 71.26           N  
-ATOM   2106  CA  CYS A 839     -30.511  25.882  29.302  1.00 64.71           C  
-ATOM   2107  C   CYS A 839     -30.835  26.557  30.611  1.00 65.43           C  
-ATOM   2108  O   CYS A 839     -31.617  26.046  31.410  1.00 66.94           O  
-ATOM   2109  CB  CYS A 839     -30.214  24.405  29.561  1.00 63.99           C  
-ATOM   2110  SG  CYS A 839     -29.834  23.457  28.094  1.00 67.69           S  
-ATOM   2111  N   PHE A 840     -30.201  27.696  30.849  1.00 65.48           N  
-ATOM   2112  CA  PHE A 840     -30.452  28.442  32.066  1.00 65.70           C  
-ATOM   2113  C   PHE A 840     -31.933  28.793  32.210  1.00 63.59           C  
-ATOM   2114  O   PHE A 840     -32.490  28.716  33.301  1.00 62.54           O  
-ATOM   2115  CB  PHE A 840     -29.600  29.705  32.102  1.00 67.78           C  
-ATOM   2116  CG  PHE A 840     -30.014  30.662  33.162  1.00 68.20           C  
-ATOM   2117  CD1 PHE A 840     -29.672  30.432  34.493  1.00 68.31           C  
-ATOM   2118  CD2 PHE A 840     -30.771  31.782  32.842  1.00 68.57           C  
-ATOM   2119  CE1 PHE A 840     -30.075  31.308  35.496  1.00 64.32           C  
-ATOM   2120  CE2 PHE A 840     -31.174  32.663  33.832  1.00 71.12           C  
-ATOM   2121  CZ  PHE A 840     -30.827  32.423  35.164  1.00 67.38           C  
-ATOM   2122  N   PRO A 841     -32.576  29.177  31.099  1.00 60.55           N  
-ATOM   2123  CA  PRO A 841     -34.008  29.473  31.098  1.00 61.20           C  
-ATOM   2124  C   PRO A 841     -34.853  28.405  31.761  1.00 61.81           C  
-ATOM   2125  O   PRO A 841     -35.986  28.707  32.131  1.00 66.65           O  
-ATOM   2126  CB  PRO A 841     -34.343  29.537  29.614  1.00 62.63           C  
-ATOM   2127  CG  PRO A 841     -33.122  30.058  28.996  1.00 60.32           C  
-ATOM   2128  CD  PRO A 841     -31.964  29.493  29.801  1.00 63.62           C  
-ATOM   2129  N   LEU A 842     -34.334  27.192  31.907  1.00 59.85           N  
-ATOM   2130  CA  LEU A 842     -35.094  26.134  32.565  1.00 57.90           C  
-ATOM   2131  C   LEU A 842     -34.892  26.240  34.052  1.00 57.96           C  
-ATOM   2132  O   LEU A 842     -35.833  26.087  34.823  1.00 60.14           O  
-ATOM   2133  CB  LEU A 842     -34.683  24.746  32.073  1.00 54.94           C  
-ATOM   2134  CG  LEU A 842     -35.156  24.363  30.664  1.00 57.19           C  
-ATOM   2135  CD1 LEU A 842     -34.297  23.255  30.061  1.00 58.65           C  
-ATOM   2136  CD2 LEU A 842     -36.605  23.948  30.673  1.00 53.72           C  
-ATOM   2137  N   LEU A 843     -33.655  26.502  34.450  1.00 58.23           N  
-ATOM   2138  CA  LEU A 843     -33.319  26.668  35.850  1.00 57.41           C  
-ATOM   2139  C   LEU A 843     -34.066  27.876  36.387  1.00 62.70           C  
-ATOM   2140  O   LEU A 843     -34.652  27.843  37.474  1.00 60.05           O  
-ATOM   2141  CB  LEU A 843     -31.824  26.895  35.990  1.00 58.27           C  
-ATOM   2142  CG  LEU A 843     -31.316  27.216  37.396  1.00 62.45           C  
-ATOM   2143  CD1 LEU A 843     -31.801  26.205  38.436  1.00 57.45           C  
-ATOM   2144  CD2 LEU A 843     -29.796  27.291  37.378  1.00 62.64           C  
-ATOM   2145  N   ASP A 844     -34.039  28.940  35.596  1.00 60.76           N  
-ATOM   2146  CA  ASP A 844     -34.733  30.167  35.913  1.00 61.18           C  
-ATOM   2147  C   ASP A 844     -36.222  29.922  36.123  1.00 61.35           C  
-ATOM   2148  O   ASP A 844     -36.777  30.270  37.167  1.00 60.26           O  
-ATOM   2149  CB  ASP A 844     -34.515  31.174  34.783  1.00 67.85           C  
-ATOM   2150  CG  ASP A 844     -34.839  32.604  35.195  1.00 72.77           C  
-ATOM   2151  OD1 ASP A 844     -34.582  32.987  36.365  1.00 71.38           O  
-ATOM   2152  OD2 ASP A 844     -35.360  33.346  34.336  1.00 77.67           O  
-ATOM   2153  N   GLY A 845     -36.868  29.322  35.131  1.00 59.05           N  
-ATOM   2154  CA  GLY A 845     -38.282  29.020  35.234  1.00 56.15           C  
-ATOM   2155  C   GLY A 845     -38.614  28.248  36.493  1.00 56.61           C  
-ATOM   2156  O   GLY A 845     -39.600  28.526  37.174  1.00 57.02           O  
-ATOM   2157  N   CYS A 846     -37.776  27.270  36.801  1.00 56.22           N  
-ATOM   2158  CA  CYS A 846     -38.006  26.379  37.932  1.00 56.83           C  
-ATOM   2159  C   CYS A 846     -37.886  27.154  39.242  1.00 56.96           C  
-ATOM   2160  O   CYS A 846     -38.598  26.895  40.204  1.00 59.48           O  
-ATOM   2161  CB  CYS A 846     -37.000  25.212  37.882  1.00 54.54           C  
-ATOM   2162  SG  CYS A 846     -37.132  23.980  39.207  1.00 57.05           S  
-ATOM   2163  N   ARG A 847     -36.972  28.112  39.276  1.00 60.93           N  
-ATOM   2164  CA  ARG A 847     -36.790  28.942  40.464  1.00 60.59           C  
-ATOM   2165  C   ARG A 847     -37.977  29.852  40.683  1.00 58.52           C  
-ATOM   2166  O   ARG A 847     -38.521  29.903  41.781  1.00 60.89           O  
-ATOM   2167  CB  ARG A 847     -35.523  29.772  40.350  1.00 55.45           C  
-ATOM   2168  CG  ARG A 847     -34.298  28.979  40.663  1.00 57.97           C  
-ATOM   2169  CD  ARG A 847     -33.087  29.690  40.153  1.00 59.24           C  
-ATOM   2170  NE  ARG A 847     -31.852  29.107  40.664  1.00 65.29           N  
-ATOM   2171  CZ  ARG A 847     -30.645  29.543  40.319  1.00 65.48           C  
-ATOM   2172  NH1 ARG A 847     -30.544  30.557  39.458  1.00 52.17           N  
-ATOM   2173  NH2 ARG A 847     -29.555  28.961  40.817  1.00 61.55           N  
-ATOM   2174  N   LYS A 848     -38.376  30.574  39.641  1.00 56.54           N  
-ATOM   2175  CA  LYS A 848     -39.571  31.391  39.736  1.00 57.47           C  
-ATOM   2176  C   LYS A 848     -40.742  30.565  40.272  1.00 60.67           C  
-ATOM   2177  O   LYS A 848     -41.463  31.000  41.168  1.00 64.36           O  
-ATOM   2178  CB  LYS A 848     -39.905  32.053  38.397  1.00 55.29           C  
-ATOM   2179  CG  LYS A 848     -38.898  33.116  38.005  1.00 56.45           C  
-ATOM   2180  CD  LYS A 848     -39.134  33.693  36.619  1.00 60.46           C  
-ATOM   2181  CE  LYS A 848     -38.003  34.679  36.283  1.00 70.99           C  
-ATOM   2182  NZ  LYS A 848     -38.007  35.208  34.884  1.00 68.60           N  
-ATOM   2183  N   ASN A 849     -40.912  29.356  39.763  1.00 59.62           N  
-ATOM   2184  CA  ASN A 849     -42.036  28.548  40.213  1.00 61.07           C  
-ATOM   2185  C   ASN A 849     -41.927  28.141  41.656  1.00 58.80           C  
-ATOM   2186  O   ASN A 849     -42.935  27.885  42.299  1.00 60.44           O  
-ATOM   2187  CB  ASN A 849     -42.225  27.317  39.339  1.00 59.83           C  
-ATOM   2188  CG  ASN A 849     -42.932  27.637  38.054  1.00 60.33           C  
-ATOM   2189  OD1 ASN A 849     -43.832  28.481  38.034  1.00 61.42           O  
-ATOM   2190  ND2 ASN A 849     -42.529  26.975  36.964  1.00 56.43           N  
-ATOM   2191  N   ARG A 850     -40.706  28.056  42.163  1.00 59.47           N  
-ATOM   2192  CA  ARG A 850     -40.516  27.685  43.559  1.00 60.95           C  
-ATOM   2193  C   ARG A 850     -40.980  28.861  44.418  1.00 62.00           C  
-ATOM   2194  O   ARG A 850     -41.686  28.683  45.421  1.00 58.61           O  
-ATOM   2195  CB  ARG A 850     -39.053  27.325  43.850  1.00 56.82           C  
-ATOM   2196  CG  ARG A 850     -38.875  26.582  45.159  1.00 55.79           C  
-ATOM   2197  CD  ARG A 850     -37.448  26.660  45.721  1.00 55.69           C  
-ATOM   2198  NE  ARG A 850     -37.355  25.968  47.012  1.00 60.69           N  
-ATOM   2199  CZ  ARG A 850     -37.711  26.486  48.193  1.00 62.62           C  
-ATOM   2200  NH1 ARG A 850     -37.590  25.762  49.304  1.00 60.23           N  
-ATOM   2201  NH2 ARG A 850     -38.179  27.726  48.274  1.00 62.47           N  
-ATOM   2202  N   GLN A 851     -40.603  30.068  43.998  1.00 59.87           N  
-ATOM   2203  CA  GLN A 851     -41.066  31.271  44.675  1.00 61.87           C  
-ATOM   2204  C   GLN A 851     -42.600  31.270  44.762  1.00 62.75           C  
-ATOM   2205  O   GLN A 851     -43.173  31.365  45.846  1.00 64.55           O  
-ATOM   2206  CB  GLN A 851     -40.532  32.528  43.976  1.00 60.90           C  
-ATOM   2207  CG  GLN A 851     -40.999  33.836  44.618  1.00 66.95           C  
-ATOM   2208  N   LYS A 852     -43.253  31.127  43.616  1.00 60.00           N  
-ATOM   2209  CA  LYS A 852     -44.703  31.044  43.553  1.00 60.00           C  
-ATOM   2210  C   LYS A 852     -45.351  30.003  44.472  1.00 62.64           C  
-ATOM   2211  O   LYS A 852     -46.343  30.305  45.128  1.00 67.54           O  
-ATOM   2212  CB  LYS A 852     -45.143  30.792  42.114  1.00 63.61           C  
-ATOM   2213  CG  LYS A 852     -44.719  31.872  41.164  1.00 64.62           C  
-ATOM   2214  CD  LYS A 852     -45.373  33.187  41.546  1.00 69.12           C  
-ATOM   2215  CE  LYS A 852     -45.335  34.199  40.401  1.00 70.71           C  
-ATOM   2216  NZ  LYS A 852     -45.996  35.477  40.784  1.00 67.86           N  
-ATOM   2217  N   TRP A 853     -44.822  28.781  44.507  1.00 62.63           N  
-ATOM   2218  CA  TRP A 853     -45.451  27.713  45.283  1.00 61.07           C  
-ATOM   2219  C   TRP A 853     -45.216  27.861  46.782  1.00 62.93           C  
-ATOM   2220  O   TRP A 853     -46.092  27.549  47.595  1.00 61.68           O  
-ATOM   2221  CB  TRP A 853     -44.971  26.336  44.827  1.00 60.08           C  
-ATOM   2222  CG  TRP A 853     -45.584  25.834  43.545  1.00 61.29           C  
-ATOM   2223  CD1 TRP A 853     -44.924  25.547  42.387  1.00 60.73           C  
-ATOM   2224  CD2 TRP A 853     -46.970  25.542  43.294  1.00 62.56           C  
-ATOM   2225  NE1 TRP A 853     -45.807  25.099  41.431  1.00 60.19           N  
-ATOM   2226  CE2 TRP A 853     -47.069  25.087  41.960  1.00 59.95           C  
-ATOM   2227  CE3 TRP A 853     -48.136  25.624  44.064  1.00 62.14           C  
-ATOM   2228  CZ2 TRP A 853     -48.285  24.715  41.380  1.00 60.30           C  
-ATOM   2229  CZ3 TRP A 853     -49.345  25.252  43.484  1.00 63.75           C  
-ATOM   2230  CH2 TRP A 853     -49.408  24.802  42.156  1.00 60.59           C  
-ATOM   2231  N   GLN A 854     -44.017  28.321  47.131  1.00 66.11           N  
-ATOM   2232  CA  GLN A 854     -43.614  28.557  48.518  1.00 66.30           C  
-ATOM   2233  C   GLN A 854     -44.524  29.597  49.162  1.00 70.74           C  
-ATOM   2234  O   GLN A 854     -45.113  29.360  50.229  1.00 69.57           O  
-ATOM   2235  CB  GLN A 854     -42.150  29.027  48.552  1.00 59.99           C  
-ATOM   2236  CG  GLN A 854     -41.623  29.432  49.914  1.00 64.21           C  
-ATOM   2237  CD  GLN A 854     -41.791  28.353  50.982  1.00 71.40           C  
-ATOM   2238  OE1 GLN A 854     -41.962  27.168  50.686  1.00 65.10           O  
-ATOM   2239  NE2 GLN A 854     -41.742  28.773  52.244  1.00 76.07           N  
-ATOM   2240  N   ALA A 855     -44.631  30.744  48.490  1.00 68.14           N  
-ATOM   2241  CA  ALA A 855     -45.541  31.820  48.874  1.00 68.97           C  
-ATOM   2242  C   ALA A 855     -46.960  31.308  49.150  1.00 71.22           C  
-ATOM   2243  O   ALA A 855     -47.560  31.624  50.178  1.00 75.79           O  
-ATOM   2244  CB  ALA A 855     -45.562  32.873  47.804  1.00 55.27           C  
-ATOM   2245  N   LEU A 856     -47.494  30.521  48.227  1.00 65.07           N  
-ATOM   2246  CA  LEU A 856     -48.773  29.869  48.442  1.00 67.73           C  
-ATOM   2247  C   LEU A 856     -48.797  28.947  49.667  1.00 70.06           C  
-ATOM   2248  O   LEU A 856     -49.768  28.943  50.417  1.00 71.78           O  
-ATOM   2249  CB  LEU A 856     -49.172  29.079  47.196  1.00 66.97           C  
-ATOM   2250  CG  LEU A 856     -49.823  29.864  46.058  1.00 68.85           C  
-ATOM   2251  CD1 LEU A 856     -49.953  28.991  44.818  1.00 65.39           C  
-ATOM   2252  CD2 LEU A 856     -51.191  30.428  46.478  1.00 63.20           C  
-ATOM   2253  N   ALA A 857     -47.747  28.149  49.854  1.00 66.28           N  
-ATOM   2254  CA  ALA A 857     -47.731  27.173  50.938  1.00 72.56           C  
-ATOM   2255  C   ALA A 857     -47.698  27.880  52.293  1.00 78.66           C  
-ATOM   2256  O   ALA A 857     -48.047  27.306  53.332  1.00 78.19           O  
-ATOM   2257  CB  ALA A 857     -46.546  26.214  50.794  1.00 66.49           C  
-ATOM   2258  N   GLU A 858     -47.277  29.137  52.258  1.00 78.13           N  
-ATOM   2259  CA  GLU A 858     -47.183  29.967  53.447  1.00 82.10           C  
-ATOM   2260  C   GLU A 858     -48.505  30.670  53.750  1.00 81.81           C  
-ATOM   2261  O   GLU A 858     -48.804  30.975  54.908  1.00 84.67           O  
-ATOM   2262  CB  GLU A 858     -46.075  31.005  53.276  1.00 78.40           C  
-ATOM   2263  CG  GLU A 858     -44.671  30.466  53.438  1.00 71.63           C  
-ATOM   2264  CD  GLU A 858     -43.630  31.539  53.179  1.00 82.92           C  
-ATOM   2265  OE1 GLU A 858     -44.024  32.691  52.885  1.00 87.41           O  
-ATOM   2266  OE2 GLU A 858     -42.418  31.242  53.258  1.00 87.63           O  
-ATOM   2267  N   GLN A 859     -49.280  30.951  52.708  1.00 77.51           N  
-ATOM   2268  CA  GLN A 859     -50.626  31.463  52.901  1.00 78.90           C  
-ATOM   2269  C   GLN A 859     -51.478  30.345  53.516  1.00 81.25           C  
-ATOM   2270  O   GLN A 859     -52.569  30.589  54.024  1.00 84.26           O  
-ATOM   2271  CB  GLN A 859     -51.227  31.979  51.584  1.00 75.55           C  
-ATOM   2272  N   GLN A 860     -50.962  29.118  53.483  1.00 80.56           N  
-ATOM   2273  CA  GLN A 860     -51.645  27.986  54.111  1.00 84.49           C  
-ATOM   2274  C   GLN A 860     -51.225  27.850  55.579  1.00 91.44           C  
-ATOM   2275  O   GLN A 860     -51.038  28.850  56.286  1.00 88.17           O  
-ATOM   2276  CB  GLN A 860     -51.370  26.676  53.351  1.00 84.61           C  
-ATOM   2277  CG  GLN A 860     -52.199  26.472  52.062  1.00 86.72           C  
-ATOM   2278  CD  GLN A 860     -53.600  25.924  52.332  1.00 84.18           C  
-TER    2279      GLN A 860                                                      
-HETATM 2280  CAA 5FO A   1     -49.506  19.057  42.213  1.00 66.95           C  
-HETATM 2281  CAB 5FO A   1     -45.074  13.796  37.184  1.00 67.43           C  
-HETATM 2282  CAC 5FO A   1     -45.396  10.564  41.879  1.00 93.11           C  
-HETATM 2283  OAD 5FO A   1     -46.167  18.947  38.675  1.00 66.52           O  
-HETATM 2284  OAE 5FO A   1     -42.874  13.966  45.972  1.00 85.39           O  
-HETATM 2285  OAF 5FO A   1     -41.807  14.136  43.793  1.00 84.04           O  
-HETATM 2286  FAG 5FO A   1     -45.016  17.241  36.823  1.00 75.09           F  
-HETATM 2287  CAH 5FO A   1     -45.468  14.991  44.768  1.00 79.68           C  
-HETATM 2288  CAI 5FO A   1     -46.483  15.806  44.277  1.00 78.36           C  
-HETATM 2289  CAJ 5FO A   1     -44.405  15.074  42.632  1.00 74.46           C  
-HETATM 2290  CAK 5FO A   1     -49.823  17.563  42.315  1.00 67.43           C  
-HETATM 2291  CAL 5FO A   1     -43.965  14.677  37.776  1.00 69.43           C  
-HETATM 2292  CAM 5FO A   1     -48.748  16.815  43.114  1.00 72.55           C  
-HETATM 2293  CAN 5FO A   1     -43.146  10.255  42.539  1.00 99.60           C  
-HETATM 2294  CAO 5FO A   1     -44.813  10.114  44.247  1.00100.43           C  
-HETATM 2295  CAP 5FO A   1     -42.967  11.755  42.810  1.00 93.60           C  
-HETATM 2296  CAQ 5FO A   1     -44.658  11.615  44.526  1.00 99.24           C  
-HETATM 2297  NAR 5FO A   1     -44.731  15.454  39.953  1.00 73.74           N  
-HETATM 2298  NAS 5FO A   1     -45.843  17.469  40.354  1.00 71.29           N  
-HETATM 2299  OAT 5FO A   1     -47.459  17.037  42.465  1.00 73.84           O  
-HETATM 2300  CAU 5FO A   1     -44.389  14.681  43.951  1.00 79.25           C  
-HETATM 2301  CAV 5FO A   1     -46.452  16.264  42.961  1.00 74.44           C  
-HETATM 2302  CAW 5FO A   1     -44.625  15.745  38.646  1.00 72.83           C  
-HETATM 2303  CAX 5FO A   1     -45.123  16.953  38.149  1.00 72.30           C  
-HETATM 2304  CAY 5FO A   1     -45.353  15.958  42.164  1.00 72.94           C  
-HETATM 2305  CAZ 5FO A   1     -45.237  16.323  40.830  1.00 71.04           C  
-HETATM 2306  CBA 5FO A   1     -45.714  17.853  39.031  1.00 67.67           C  
-HETATM 2307  NBB 5FO A   1     -44.518   9.836  42.820  1.00101.84           N  
-HETATM 2308  NBC 5FO A   1     -43.273  12.051  44.225  1.00100.46           N  
-HETATM 2309  SBD 5FO A   1     -43.053  13.686  44.502  1.00 94.82           S  
-HETATM 2310 ZN    ZN A 861     -43.081  11.191  31.566  1.00 67.10          ZN  
-HETATM 2311 MG    MG A 862     -43.453   9.138  33.970  1.00 70.11          MG  
-HETATM 2312 MG    MG A   2     -43.733  -1.922   5.311  1.00 79.39          MG  
-HETATM 2313 MG    MG A   3     -58.501  18.457  18.617  1.00 78.02          MG  
-HETATM 2314  O   HOH A   4     -38.331  31.020  26.471  1.00 63.06           O  
-HETATM 2315  O   HOH A   5     -35.816   6.112   7.580  1.00 63.76           O  
-HETATM 2316  O   HOH A   6     -57.441  -1.700  27.298  1.00 81.78           O  
-HETATM 2317  O   HOH A   7     -57.345  17.863  15.513  1.00 68.22           O  
-HETATM 2318  O   HOH A  10     -43.018  20.357  29.070  1.00 59.00           O  
-HETATM 2319  O   HOH A  11     -42.076   7.003  33.358  1.00 65.79           O  
-HETATM 2320  O   HOH A  16     -34.802  17.105   7.419  1.00 61.81           O  
-HETATM 2321  O   HOH A  17     -44.385  29.270   8.400  1.00 58.70           O  
-HETATM 2322  O   HOH A  24     -49.129  35.861  41.365  1.00 68.89           O  
-HETATM 2323  O   HOH A 863     -32.320   9.726  34.439  1.00 58.32           O  
-HETATM 2324  O   HOH A 864     -43.636  11.763  34.214  1.00 57.93           O  
-HETATM 2325  O   HOH A 865     -46.655   9.441  46.275  1.00 92.45           O  
-CONECT  642 2310                                                                
-CONECT  905 2310                                                                
-CONECT  913 2310                                                                
-CONECT 1684 2310                                                                
-CONECT 2280 2290                                                                
-CONECT 2281 2291                                                                
-CONECT 2282 2307                                                                
-CONECT 2283 2306                                                                
-CONECT 2284 2309                                                                
-CONECT 2285 2309                                                                
-CONECT 2286 2303                                                                
-CONECT 2287 2288 2300                                                           
-CONECT 2288 2287 2301                                                           
-CONECT 2289 2300 2304                                                           
-CONECT 2290 2280 2292                                                           
-CONECT 2291 2281 2302                                                           
-CONECT 2292 2290 2299                                                           
-CONECT 2293 2295 2307                                                           
-CONECT 2294 2296 2307                                                           
-CONECT 2295 2293 2308                                                           
-CONECT 2296 2294 2308                                                           
-CONECT 2297 2302 2305                                                           
-CONECT 2298 2305 2306                                                           
-CONECT 2299 2292 2301                                                           
-CONECT 2300 2287 2289 2309                                                      
-CONECT 2301 2288 2299 2304                                                      
-CONECT 2302 2291 2297 2303                                                      
-CONECT 2303 2286 2302 2306                                                      
-CONECT 2304 2289 2301 2305                                                      
-CONECT 2305 2297 2298 2304                                                      
-CONECT 2306 2283 2298 2303                                                      
-CONECT 2307 2282 2293 2294                                                      
-CONECT 2308 2295 2296 2309                                                      
-CONECT 2309 2284 2285 2300 2308                                                 
-CONECT 2310  642  905  913 1684                                                 
-CONECT 2311 2319 2324                                                           
-CONECT 2319 2311                                                                
-CONECT 2324 2311                                                                
-MASTER      374    0    5   17    0    0    7    6 2324    1   38   27          
-END                                                                             
diff --git a/plip/test/pdb/3tah.pdb b/plip/test/pdb/3tah.pdb
deleted file mode 100644
index 49a8788..0000000
--- a/plip/test/pdb/3tah.pdb
+++ /dev/null
@@ -1,5381 +0,0 @@
-HEADER    METAL TRANSPORT                         04-AUG-11   3TAH              
-TITLE     CRYSTAL STRUCTURE OF AN S. THERMOPHILUS NFEOB N11A MUTANT BOUND TO    
-TITLE    2 MGDP                                                                 
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: FERROUS IRON UPTAKE TRANSPORTER PROTEIN B;                 
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 FRAGMENT: G-PROTEIN DOMAIN, UNP RESIDUES 1-270;                      
-COMPND   5 SYNONYM: FEOB;                                                       
-COMPND   6 ENGINEERED: YES;                                                     
-COMPND   7 MUTATION: YES                                                        
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS THERMOPHILUS;                     
-SOURCE   3 ORGANISM_TAXID: 264199;                                              
-SOURCE   4 STRAIN: LMG 18311;                                                   
-SOURCE   5 GENE: FEOB;                                                          
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
-SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1                                 
-KEYWDS    G-PROTEIN, GTPASE, IRON TRANSPORT, POTASSIUM BINDING, GTP BINDING,    
-KEYWDS   2 METAL TRANSPORT                                                      
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    M.R.ASH,M.J.MAHER,J.M.GUSS,M.JORMAKKA                                 
-REVDAT   2   02-MAY-12 3TAH    1       JRNL                                     
-REVDAT   1   14-DEC-11 3TAH    0                                                
-JRNL        AUTH   M.R.ASH,M.J.MAHER,J.M.GUSS,M.JORMAKKA                        
-JRNL        TITL   THE STRUCTURE OF AN N11A MUTANT OF THE G-PROTEIN DOMAIN OF   
-JRNL        TITL 2 FEOB                                                         
-JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  67  1511 2011              
-JRNL        REFN                   ESSN 1744-3091                               
-JRNL        PMID   22139154                                                     
-JRNL        DOI    10.1107/S1744309111042965                                    
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
-REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
-REMARK   3   NUMBER OF REFLECTIONS             : 43738                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
-REMARK   3   R VALUE            (WORKING SET) : 0.176                           
-REMARK   3   FREE R VALUE                     : 0.216                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 2197                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
-REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2890                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.78                        
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
-REMARK   3   BIN FREE R VALUE SET COUNT          : 130                          
-REMARK   3   BIN FREE R VALUE                    : 0.3570                       
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 4046                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 95                                      
-REMARK   3   SOLVENT ATOMS            : 416                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 23.00                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.33                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 0.43000                                              
-REMARK   3    B22 (A**2) : 0.15000                                              
-REMARK   3    B33 (A**2) : -0.59000                                             
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
-REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
-REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
-REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
-REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.831         
-REMARK   3                                                                      
-REMARK   3 CORRELATION COEFFICIENTS.                                            
-REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
-REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
-REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4404 ; 0.010 ; 0.022       
-REMARK   3   BOND LENGTHS OTHERS               (A):  2878 ; 0.001 ; 0.020       
-REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6022 ; 1.502 ; 2.001       
-REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7082 ; 1.013 ; 3.001       
-REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   567 ; 4.625 ; 5.000       
-REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   187 ;38.420 ;25.561       
-REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   777 ;11.030 ;15.000       
-REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;11.594 ;15.000       
-REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   710 ; 0.076 ; 0.200       
-REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4955 ; 0.006 ; 0.021       
-REMARK   3   GENERAL PLANES OTHERS             (A):   799 ; 0.001 ; 0.020       
-REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
-REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
-REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2744 ; 1.179 ; 2.000       
-REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1103 ; 0.297 ; 2.000       
-REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4485 ; 1.952 ; 3.000       
-REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1660 ; 2.085 ; 3.000       
-REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1539 ; 3.211 ; 4.000       
-REMARK   3                                                                      
-REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
-REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS STATISTICS                                           
-REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED : MASK                                                 
-REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
-REMARK   3   VDW PROBE RADIUS   : 1.20                                          
-REMARK   3   ION PROBE RADIUS   : 0.80                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
-REMARK   3  POSITIONS                                                           
-REMARK   4                                                                      
-REMARK   4 3TAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-AUG-11.                  
-REMARK 100 THE RCSB ID CODE IS RCSB067240.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 05-FEB-10                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 6.0                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : N                                  
-REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
-REMARK 200  BEAMLINE                       : NULL                               
-REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
-REMARK 200  MONOCHROMATOR                  : NI FILTER                          
-REMARK 200  OPTICS                         : OSMIC MIRRORS                      
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
-REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
-REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43892                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
-REMARK 200  DATA REDUNDANCY                : 6.200                              
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : 0.06800                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.9000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.37900                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASER                                                
-REMARK 200 STARTING MODEL: 3LX8                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 41.63                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LICL, 0.1M MES, 20% PEG 6000, PH    
-REMARK 280  6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X,-Y,Z+1/2                                             
-REMARK 290       3555   -X,Y,-Z+1/2                                             
-REMARK 290       4555   X,-Y,-Z                                                 
-REMARK 290       5555   X+1/2,Y+1/2,Z                                           
-REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
-REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
-REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      132.60000            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      132.60000            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.05000            
-REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.90000            
-REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.05000            
-REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.90000            
-REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      132.60000            
-REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.05000            
-REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       31.90000            
-REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      132.60000            
-REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.05000            
-REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       31.90000            
-REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2                                                    
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     GLY A    -1                                                      
-REMARK 465     SER A   260                                                      
-REMARK 465     HIS A   261                                                      
-REMARK 465     THR A   262                                                      
-REMARK 465     GLU A   263                                                      
-REMARK 465     ASP A   264                                                      
-REMARK 465     PHE A   265                                                      
-REMARK 465     ALA A   266                                                      
-REMARK 465     LEU A   267                                                      
-REMARK 465     THR A   268                                                      
-REMARK 465     LEU A   269                                                      
-REMARK 465     SER A   270                                                      
-REMARK 465     GLU B   263                                                      
-REMARK 465     ASP B   264                                                      
-REMARK 465     PHE B   265                                                      
-REMARK 465     ALA B   266                                                      
-REMARK 465     LEU B   267                                                      
-REMARK 465     THR B   268                                                      
-REMARK 465     LEU B   269                                                      
-REMARK 465     SER B   270                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     LYS A  44    CD   CE   NZ                                        
-REMARK 470     ARG A  78    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     ASP A 119    CG   OD1  OD2                                       
-REMARK 470     LYS A 123    CE   NZ                                             
-REMARK 470     LYS A 124    CG   CD   CE   NZ                                   
-REMARK 470     VAL A 186    CG1  CG2                                            
-REMARK 470     GLU A 240    CD   OE1  OE2                                       
-REMARK 470     HIS B  24    CG   ND1  CD2  CE1  NE2                             
-REMARK 470     ASN B  25    CG   OD1  ND2                                       
-REMARK 470     ARG B  93    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     VAL B 186    CG1  CG2                                            
-REMARK 470     THR B 262    OG1  CG2                                            
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    MET A  60       68.04   -102.47                                   
-REMARK 500    ASN A  90       52.05   -144.17                                   
-REMARK 500    ASN B  46       92.33   -166.95                                   
-REMARK 500    MET B  60       67.58   -115.78                                   
-REMARK 500    ASP B 215       67.23     39.79                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 620                                                                      
-REMARK 620 METAL COORDINATION                                                   
-REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG A 401  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 ASP A 128   OD1                                                    
-REMARK 620 2 ASN A 126   OD1  81.3                                              
-REMARK 620 3 HOH A 359   O   177.5 100.8                                        
-REMARK 620 4 HOH A 360   O    83.7  91.2  97.5                                  
-REMARK 620 5 HOH A 357   O    90.6  85.6  88.3 173.9                            
-REMARK 620 N                    1     2     3     4                             
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGO A 300                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 400                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGO B 300                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 400                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 401                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 3LX5   RELATED DB: PDB                                   
-REMARK 900 WILD-TYPE PROTEIN COMPLEXED WITH MGMPPNP                             
-REMARK 900 RELATED ID: 3LX8   RELATED DB: PDB                                   
-REMARK 900 WILD-TYPE PROTEIN COMPLEXED WITH GDP                                 
-REMARK 900 RELATED ID: 3SS8   RELATED DB: PDB                                   
-REMARK 900 WILD-TYPE PROTEIN COMPLEXED WITH GDP.ALF4- AND K+                    
-DBREF  3TAH A    1   270  UNP    Q5M586   Q5M586_STRT2     1    270             
-DBREF  3TAH B    1   270  UNP    Q5M586   Q5M586_STRT2     1    270             
-SEQADV 3TAH GLY A   -1  UNP  Q5M586              EXPRESSION TAG                 
-SEQADV 3TAH SER A    0  UNP  Q5M586              EXPRESSION TAG                 
-SEQADV 3TAH ALA A   11  UNP  Q5M586    ASN    11 ENGINEERED MUTATION            
-SEQADV 3TAH GLY B   -1  UNP  Q5M586              EXPRESSION TAG                 
-SEQADV 3TAH SER B    0  UNP  Q5M586              EXPRESSION TAG                 
-SEQADV 3TAH ALA B   11  UNP  Q5M586    ASN    11 ENGINEERED MUTATION            
-SEQRES   1 A  272  GLY SER MET THR GLU ILE ALA LEU ILE GLY ASN PRO ALA          
-SEQRES   2 A  272  SER GLY LYS THR SER LEU PHE ASN LEU ILE THR GLY HIS          
-SEQRES   3 A  272  ASN GLN ARG VAL GLY ASN TRP PRO GLY VAL THR VAL GLU          
-SEQRES   4 A  272  ARG LYS SER GLY LEU VAL LYS LYS ASN LYS ASP LEU GLU          
-SEQRES   5 A  272  ILE GLN ASP LEU PRO GLY ILE TYR SER MET SER PRO TYR          
-SEQRES   6 A  272  SER PRO GLU GLU LYS VAL ALA ARG ASP TYR LEU LEU SER          
-SEQRES   7 A  272  GLN ARG ALA ASP SER ILE LEU ASN VAL VAL ASP ALA THR          
-SEQRES   8 A  272  ASN LEU GLU ARG ASN LEU TYR LEU THR THR GLN LEU ILE          
-SEQRES   9 A  272  GLU THR GLY ILE PRO VAL THR ILE ALA LEU ASN MET ILE          
-SEQRES  10 A  272  ASP VAL LEU ASP GLY GLN GLY LYS LYS ILE ASN VAL ASP          
-SEQRES  11 A  272  LYS LEU SER TYR HIS LEU GLY VAL PRO VAL VAL ALA THR          
-SEQRES  12 A  272  SER ALA LEU LYS GLN THR GLY VAL ASP GLN VAL VAL LYS          
-SEQRES  13 A  272  LYS ALA ALA HIS THR THR THR SER THR VAL GLY ASP LEU          
-SEQRES  14 A  272  ALA PHE PRO ILE TYR ASP ASP ARG LEU GLU ALA ALA ILE          
-SEQRES  15 A  272  SER GLN ILE LEU GLU VAL LEU GLY ASN SER VAL PRO GLN          
-SEQRES  16 A  272  ARG SER ALA ARG PHE TYR ALA ILE LYS LEU PHE GLU GLN          
-SEQRES  17 A  272  ASP SER LEU VAL GLU ALA GLU LEU ASP LEU SER GLN PHE          
-SEQRES  18 A  272  GLN ARG LYS GLU ILE GLU ASP ILE ILE ARG ILE THR GLU          
-SEQRES  19 A  272  GLU ILE PHE THR GLU ASP ALA GLU SER ILE VAL ILE ASN          
-SEQRES  20 A  272  GLU ARG TYR ALA PHE ILE GLU ARG VAL CYS GLN MET ALA          
-SEQRES  21 A  272  GLU SER HIS THR GLU ASP PHE ALA LEU THR LEU SER              
-SEQRES   1 B  272  GLY SER MET THR GLU ILE ALA LEU ILE GLY ASN PRO ALA          
-SEQRES   2 B  272  SER GLY LYS THR SER LEU PHE ASN LEU ILE THR GLY HIS          
-SEQRES   3 B  272  ASN GLN ARG VAL GLY ASN TRP PRO GLY VAL THR VAL GLU          
-SEQRES   4 B  272  ARG LYS SER GLY LEU VAL LYS LYS ASN LYS ASP LEU GLU          
-SEQRES   5 B  272  ILE GLN ASP LEU PRO GLY ILE TYR SER MET SER PRO TYR          
-SEQRES   6 B  272  SER PRO GLU GLU LYS VAL ALA ARG ASP TYR LEU LEU SER          
-SEQRES   7 B  272  GLN ARG ALA ASP SER ILE LEU ASN VAL VAL ASP ALA THR          
-SEQRES   8 B  272  ASN LEU GLU ARG ASN LEU TYR LEU THR THR GLN LEU ILE          
-SEQRES   9 B  272  GLU THR GLY ILE PRO VAL THR ILE ALA LEU ASN MET ILE          
-SEQRES  10 B  272  ASP VAL LEU ASP GLY GLN GLY LYS LYS ILE ASN VAL ASP          
-SEQRES  11 B  272  LYS LEU SER TYR HIS LEU GLY VAL PRO VAL VAL ALA THR          
-SEQRES  12 B  272  SER ALA LEU LYS GLN THR GLY VAL ASP GLN VAL VAL LYS          
-SEQRES  13 B  272  LYS ALA ALA HIS THR THR THR SER THR VAL GLY ASP LEU          
-SEQRES  14 B  272  ALA PHE PRO ILE TYR ASP ASP ARG LEU GLU ALA ALA ILE          
-SEQRES  15 B  272  SER GLN ILE LEU GLU VAL LEU GLY ASN SER VAL PRO GLN          
-SEQRES  16 B  272  ARG SER ALA ARG PHE TYR ALA ILE LYS LEU PHE GLU GLN          
-SEQRES  17 B  272  ASP SER LEU VAL GLU ALA GLU LEU ASP LEU SER GLN PHE          
-SEQRES  18 B  272  GLN ARG LYS GLU ILE GLU ASP ILE ILE ARG ILE THR GLU          
-SEQRES  19 B  272  GLU ILE PHE THR GLU ASP ALA GLU SER ILE VAL ILE ASN          
-SEQRES  20 B  272  GLU ARG TYR ALA PHE ILE GLU ARG VAL CYS GLN MET ALA          
-SEQRES  21 B  272  GLU SER HIS THR GLU ASP PHE ALA LEU THR LEU SER              
-HET    BGO  A 300      38                                                       
-HET    GOL  A 400       6                                                       
-HET     MG  A 401       1                                                       
-HET    BGO  B 300      38                                                       
-HET    GOL  B 400       6                                                       
-HET    GOL  B 401       6                                                       
-HETNAM     BGO 3'-O-(N-METHYLANTHRANILOYL)GUANOSINE-5'-DIPHOSPHATE              
-HETNAM     GOL GLYCEROL                                                         
-HETNAM      MG MAGNESIUM ION                                                    
-HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
-FORMUL   3  BGO    2(C18 H22 N6 O12 P2)                                         
-FORMUL   4  GOL    3(C3 H8 O3)                                                  
-FORMUL   5   MG    MG 2+                                                        
-FORMUL   9  HOH   *416(H2 O)                                                    
-HELIX    1   1 GLY A   13  GLY A   23  1                                  11    
-HELIX    2   2 SER A   64  SER A   76  1                                  13    
-HELIX    3   3 ASN A   90  THR A  104  1                                  15    
-HELIX    4   4 MET A  114  GLN A  121  1                                   8    
-HELIX    5   5 ASN A  126  GLY A  135  1                                  10    
-HELIX    6   6 GLY A  148  HIS A  158  1                                  11    
-HELIX    7   7 ASP A  173  GLY A  188  1                                  16    
-HELIX    8   8 SER A  195  GLU A  205  1                                  11    
-HELIX    9   9 ASP A  207  LEU A  214  1                                   8    
-HELIX   10  10 SER A  217  THR A  236  1                                  20    
-HELIX   11  11 ASP A  238  ALA A  258  1                                  21    
-HELIX   12  12 GLY B   13  GLY B   23  1                                  11    
-HELIX   13  13 SER B   64  SER B   76  1                                  13    
-HELIX   14  14 ASN B   90  THR B  104  1                                  15    
-HELIX   15  15 MET B  114  GLN B  121  1                                   8    
-HELIX   16  16 ASN B  126  GLY B  135  1                                  10    
-HELIX   17  17 GLY B  148  HIS B  158  1                                  11    
-HELIX   18  18 ASP B  173  GLY B  188  1                                  16    
-HELIX   19  19 SER B  195  GLU B  205  1                                  11    
-HELIX   20  20 ASP B  207  ASP B  215  1                                   9    
-HELIX   21  21 SER B  217  THR B  236  1                                  20    
-HELIX   22  22 ASP B  238  ALA B  258  1                                  21    
-SHEET    1   A 7 GLN A  26  ASN A  30  0                                        
-SHEET    2   A 7 GLU A  37  VAL A  43 -1  O  SER A  40   N  ARG A  27           
-SHEET    3   A 7 ASN A  46  ASP A  53 -1  O  ILE A  51   N  GLY A  41           
-SHEET    4   A 7 THR A   2  GLY A   8  1  N  ILE A   4   O  GLU A  50           
-SHEET    5   A 7 SER A  81  ASP A  87  1  O  LEU A  83   N  ALA A   5           
-SHEET    6   A 7 VAL A 108  ASN A 113  1  O  THR A 109   N  ASN A  84           
-SHEET    7   A 7 VAL A 138  ALA A 140  1  O  VAL A 139   N  LEU A 112           
-SHEET    1   B 7 ARG B  27  ASN B  30  0                                        
-SHEET    2   B 7 GLU B  37  VAL B  43 -1  O  SER B  40   N  ARG B  27           
-SHEET    3   B 7 ASN B  46  ASP B  53 -1  O  ILE B  51   N  GLY B  41           
-SHEET    4   B 7 THR B   2  GLY B   8  1  N  ILE B   4   O  GLU B  50           
-SHEET    5   B 7 SER B  81  ASP B  87  1  O  SER B  81   N  ALA B   5           
-SHEET    6   B 7 VAL B 108  ASN B 113  1  O  ALA B 111   N  VAL B  86           
-SHEET    7   B 7 VAL B 138  ALA B 140  1  O  VAL B 139   N  LEU B 112           
-SHEET    1   C 2 LYS B 123  ILE B 125  0                                        
-SHEET    2   C 2 GLU B 259  HIS B 261 -1  O  SER B 260   N  LYS B 124           
-LINK         OD1 ASP A 128                MG    MG A 401     1555   1555  2.05  
-LINK         OD1 ASN A 126                MG    MG A 401     1555   1555  2.13  
-LINK        MG    MG A 401                 O   HOH A 359     1555   1555  2.04  
-LINK        MG    MG A 401                 O   HOH A 360     1555   1555  2.10  
-LINK        MG    MG A 401                 O   HOH A 357     1555   1555  2.20  
-SITE     1 AC1 25 ASN A   9  ALA A  11  SER A  12  GLY A  13                    
-SITE     2 AC1 25 LYS A  14  THR A  15  SER A  16  TYR A  58                    
-SITE     3 AC1 25 SER A  59  ARG A  93  TYR A  96  ASN A 113                    
-SITE     4 AC1 25 MET A 114  ASP A 116  VAL A 117  SER A 142                    
-SITE     5 AC1 25 ALA A 143  LEU A 144  TYR A 248  HOH A 302                    
-SITE     6 AC1 25 HOH A 379  HOH A 380  HOH A 381  HOH A 420                    
-SITE     7 AC1 25 HOH A 453                                                     
-SITE     1 AC2  5 THR A   2  ASP A  80  THR A 160  THR A 163                    
-SITE     2 AC2  5 HOH A 436                                                     
-SITE     1 AC3  6 ASN A 126  ASP A 128  GLU A 211  HOH A 357                    
-SITE     2 AC3  6 HOH A 359  HOH A 360                                          
-SITE     1 AC4 20 ASN B   9  ALA B  11  SER B  12  GLY B  13                    
-SITE     2 AC4 20 LYS B  14  THR B  15  SER B  16  TYR B  58                    
-SITE     3 AC4 20 TYR B  96  ASN B 113  MET B 114  ASP B 116                    
-SITE     4 AC4 20 VAL B 117  SER B 142  ALA B 143  LEU B 144                    
-SITE     5 AC4 20 TYR B 248  HOH B 411  HOH B 413  HOH B 414                    
-SITE     1 AC5  4 HIS B 133  PHE B 250  ARG B 253  HOH B 309                    
-SITE     1 AC6  8 ASN B   9  PRO B  10  TYR B  58  ASP B  87                    
-SITE     2 AC6  8 ASN B  90  ASN B  94  HOH B 405  HOH B 470                    
-CRYST1   60.100   63.800  265.200  90.00  90.00  90.00 C 2 2 21     16          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.016626  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.015679  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.003771        0.00000                         
-ATOM      1  N   SER A   0      -8.460  17.355 -27.331  1.00 39.25           N  
-ATOM      2  CA  SER A   0      -8.342  16.020 -26.683  1.00 39.42           C  
-ATOM      3  C   SER A   0      -7.301  16.029 -25.558  1.00 38.68           C  
-ATOM      4  O   SER A   0      -6.175  16.499 -25.738  1.00 38.34           O  
-ATOM      5  CB  SER A   0      -7.975  14.956 -27.719  1.00 40.05           C  
-ATOM      6  OG  SER A   0      -7.880  13.673 -27.128  1.00 40.75           O  
-ATOM      7  N   MET A   1      -7.693  15.498 -24.404  1.00 37.12           N  
-ATOM      8  CA  MET A   1      -6.819  15.397 -23.246  1.00 36.05           C  
-ATOM      9  C   MET A   1      -5.714  14.352 -23.488  1.00 32.70           C  
-ATOM     10  O   MET A   1      -5.993  13.292 -24.052  1.00 33.25           O  
-ATOM     11  CB  MET A   1      -7.652  14.960 -22.033  1.00 38.70           C  
-ATOM     12  CG  MET A   1      -6.981  15.138 -20.673  1.00 40.81           C  
-ATOM     13  SD  MET A   1      -7.337  16.738 -19.913  1.00 46.26           S  
-ATOM     14  CE  MET A   1      -9.061  16.525 -19.414  1.00 42.77           C  
-ATOM     15  N   THR A   2      -4.474  14.637 -23.081  1.00 27.53           N  
-ATOM     16  CA  THR A   2      -3.437  13.587 -23.059  1.00 22.55           C  
-ATOM     17  C   THR A   2      -3.601  12.843 -21.728  1.00 20.74           C  
-ATOM     18  O   THR A   2      -3.504  13.444 -20.666  1.00 19.67           O  
-ATOM     19  CB  THR A   2      -2.019  14.129 -23.249  1.00 22.59           C  
-ATOM     20  OG1 THR A   2      -1.913  14.743 -24.530  1.00 21.88           O  
-ATOM     21  CG2 THR A   2      -0.989  12.999 -23.218  1.00 21.08           C  
-ATOM     22  N   GLU A   3      -3.876  11.543 -21.797  1.00 19.32           N  
-ATOM     23  CA  GLU A   3      -4.106  10.722 -20.617  1.00 19.20           C  
-ATOM     24  C   GLU A   3      -2.825   9.982 -20.278  1.00 18.04           C  
-ATOM     25  O   GLU A   3      -2.353   9.172 -21.083  1.00 16.20           O  
-ATOM     26  CB  GLU A   3      -5.208   9.709 -20.892  1.00 20.32           C  
-ATOM     27  CG  GLU A   3      -5.808   9.114 -19.654  1.00 25.26           C  
-ATOM     28  CD  GLU A   3      -6.696  10.091 -18.907  1.00 28.81           C  
-ATOM     29  OE1 GLU A   3      -7.024   9.811 -17.743  1.00 33.68           O  
-ATOM     30  OE2 GLU A   3      -7.065  11.137 -19.484  1.00 34.52           O  
-ATOM     31  N   ILE A   4      -2.294  10.268 -19.096  1.00 17.05           N  
-ATOM     32  CA  ILE A   4      -1.043   9.707 -18.627  1.00 17.61           C  
-ATOM     33  C   ILE A   4      -1.335   8.766 -17.464  1.00 16.51           C  
-ATOM     34  O   ILE A   4      -1.759   9.217 -16.401  1.00 17.24           O  
-ATOM     35  CB  ILE A   4      -0.056  10.808 -18.190  1.00 17.97           C  
-ATOM     36  CG1 ILE A   4       0.219  11.778 -19.349  1.00 18.70           C  
-ATOM     37  CG2 ILE A   4       1.241  10.173 -17.683  1.00 19.96           C  
-ATOM     38  CD1 ILE A   4       1.146  12.941 -19.034  1.00 16.29           C  
-ATOM     39  N   ALA A   5      -1.093   7.468 -17.663  1.00 14.55           N  
-ATOM     40  CA  ALA A   5      -1.291   6.472 -16.612  1.00 15.23           C  
-ATOM     41  C   ALA A   5      -0.080   6.443 -15.675  1.00 14.57           C  
-ATOM     42  O   ALA A   5       1.016   6.129 -16.115  1.00 16.06           O  
-ATOM     43  CB  ALA A   5      -1.531   5.068 -17.216  1.00 15.73           C  
-ATOM     44  N   LEU A   6      -0.287   6.758 -14.401  1.00 13.30           N  
-ATOM     45  CA  LEU A   6       0.766   6.751 -13.379  1.00 13.56           C  
-ATOM     46  C   LEU A   6       0.735   5.414 -12.639  1.00 12.61           C  
-ATOM     47  O   LEU A   6      -0.285   5.052 -12.054  1.00 15.84           O  
-ATOM     48  CB  LEU A   6       0.543   7.913 -12.410  1.00 13.29           C  
-ATOM     49  CG  LEU A   6       1.621   8.207 -11.379  1.00 13.13           C  
-ATOM     50  CD1 LEU A   6       2.820   8.815 -12.066  1.00 13.45           C  
-ATOM     51  CD2 LEU A   6       1.095   9.139 -10.295  1.00 14.43           C  
-ATOM     52  N   ILE A   7       1.841   4.671 -12.660  1.00 12.84           N  
-ATOM     53  CA  ILE A   7       1.893   3.381 -11.999  1.00 12.90           C  
-ATOM     54  C   ILE A   7       3.305   3.032 -11.523  1.00 13.97           C  
-ATOM     55  O   ILE A   7       4.312   3.444 -12.101  1.00 15.08           O  
-ATOM     56  CB  ILE A   7       1.296   2.265 -12.920  1.00 15.07           C  
-ATOM     57  CG1 ILE A   7       1.160   0.933 -12.181  1.00 18.32           C  
-ATOM     58  CG2 ILE A   7       2.122   2.095 -14.177  1.00 17.72           C  
-ATOM     59  CD1 ILE A   7       0.293  -0.075 -12.938  1.00 17.92           C  
-ATOM     60  N   GLY A   8       3.363   2.267 -10.447  1.00 13.84           N  
-ATOM     61  CA  GLY A   8       4.629   1.798  -9.898  1.00 14.39           C  
-ATOM     62  C   GLY A   8       4.331   0.883  -8.730  1.00 15.49           C  
-ATOM     63  O   GLY A   8       3.159   0.650  -8.393  1.00 14.42           O  
-ATOM     64  N   ASN A   9       5.396   0.355  -8.131  1.00 14.19           N  
-ATOM     65  CA  ASN A   9       5.291  -0.480  -6.957  1.00 14.69           C  
-ATOM     66  C   ASN A   9       4.744   0.329  -5.774  1.00 15.40           C  
-ATOM     67  O   ASN A   9       4.911   1.554  -5.712  1.00 14.72           O  
-ATOM     68  CB  ASN A   9       6.660  -0.971  -6.500  1.00 15.32           C  
-ATOM     69  CG  ASN A   9       7.343  -1.960  -7.442  1.00 14.60           C  
-ATOM     70  OD1 ASN A   9       8.477  -2.331  -7.152  1.00 13.21           O  
-ATOM     71  ND2 ASN A   9       6.696  -2.396  -8.524  1.00 13.63           N  
-ATOM     72  N   PRO A  10       4.108  -0.365  -4.817  1.00 16.42           N  
-ATOM     73  CA  PRO A  10       3.848   0.241  -3.512  1.00 17.76           C  
-ATOM     74  C   PRO A  10       5.114   0.828  -2.921  1.00 17.77           C  
-ATOM     75  O   PRO A  10       6.203   0.252  -3.065  1.00 17.38           O  
-ATOM     76  CB  PRO A  10       3.386  -0.946  -2.664  1.00 17.84           C  
-ATOM     77  CG  PRO A  10       2.750  -1.854  -3.653  1.00 17.42           C  
-ATOM     78  CD  PRO A  10       3.603  -1.747  -4.874  1.00 17.09           C  
-ATOM     79  N   ALA A  11       4.960   1.976  -2.267  1.00 18.17           N  
-ATOM     80  CA  ALA A  11       6.054   2.660  -1.571  1.00 18.96           C  
-ATOM     81  C   ALA A  11       7.164   3.122  -2.512  1.00 18.78           C  
-ATOM     82  O   ALA A  11       8.306   3.255  -2.102  1.00 18.54           O  
-ATOM     83  CB  ALA A  11       6.624   1.772  -0.425  1.00 19.22           C  
-ATOM     84  N   SER A  12       6.835   3.361  -3.780  1.00 17.71           N  
-ATOM     85  CA  SER A  12       7.805   3.861  -4.737  1.00 17.13           C  
-ATOM     86  C   SER A  12       7.804   5.383  -4.780  1.00 17.03           C  
-ATOM     87  O   SER A  12       8.684   5.988  -5.388  1.00 15.35           O  
-ATOM     88  CB  SER A  12       7.529   3.291  -6.133  1.00 16.50           C  
-ATOM     89  OG  SER A  12       6.281   3.711  -6.634  1.00 13.94           O  
-ATOM     90  N   GLY A  13       6.815   5.994  -4.135  1.00 17.50           N  
-ATOM     91  CA  GLY A  13       6.627   7.445  -4.163  1.00 17.15           C  
-ATOM     92  C   GLY A  13       5.571   7.887  -5.162  1.00 17.04           C  
-ATOM     93  O   GLY A  13       5.499   9.070  -5.512  1.00 13.87           O  
-ATOM     94  N   LYS A  14       4.733   6.949  -5.615  1.00 17.26           N  
-ATOM     95  CA  LYS A  14       3.734   7.265  -6.632  1.00 18.82           C  
-ATOM     96  C   LYS A  14       2.711   8.281  -6.109  1.00 18.45           C  
-ATOM     97  O   LYS A  14       2.412   9.246  -6.803  1.00 18.50           O  
-ATOM     98  CB  LYS A  14       3.049   5.993  -7.151  1.00 19.06           C  
-ATOM     99  CG  LYS A  14       1.903   6.268  -8.124  1.00 19.95           C  
-ATOM    100  CD  LYS A  14       1.393   5.008  -8.776  1.00 21.61           C  
-ATOM    101  CE  LYS A  14       0.694   4.097  -7.802  1.00 21.43           C  
-ATOM    102  NZ  LYS A  14      -0.562   4.700  -7.257  1.00 22.02           N  
-ATOM    103  N   THR A  15       2.188   8.071  -4.900  1.00 20.35           N  
-ATOM    104  CA  THR A  15       1.230   9.002  -4.310  1.00 20.50           C  
-ATOM    105  C   THR A  15       1.855  10.375  -4.098  1.00 19.68           C  
-ATOM    106  O   THR A  15       1.225  11.396  -4.398  1.00 20.07           O  
-ATOM    107  CB  THR A  15       0.686   8.521  -2.943  1.00 22.62           C  
-ATOM    108  OG1 THR A  15       0.056   7.248  -3.100  1.00 24.74           O  
-ATOM    109  CG2 THR A  15      -0.322   9.508  -2.387  1.00 22.35           C  
-ATOM    110  N   SER A  16       3.085  10.392  -3.584  1.00 17.99           N  
-ATOM    111  CA  SER A  16       3.806  11.637  -3.358  1.00 17.33           C  
-ATOM    112  C   SER A  16       3.943  12.419  -4.652  1.00 17.22           C  
-ATOM    113  O   SER A  16       3.716  13.629  -4.654  1.00 17.17           O  
-ATOM    114  CB  SER A  16       5.189  11.391  -2.752  1.00 18.41           C  
-ATOM    115  OG  SER A  16       5.087  10.808  -1.462  1.00 17.35           O  
-ATOM    116  N   LEU A  17       4.315  11.740  -5.745  1.00 15.95           N  
-ATOM    117  CA  LEU A  17       4.418  12.409  -7.051  1.00 16.45           C  
-ATOM    118  C   LEU A  17       3.042  12.790  -7.589  1.00 16.36           C  
-ATOM    119  O   LEU A  17       2.869  13.875  -8.109  1.00 17.96           O  
-ATOM    120  CB  LEU A  17       5.150  11.550  -8.085  1.00 15.51           C  
-ATOM    121  CG  LEU A  17       6.636  11.338  -7.825  1.00 17.14           C  
-ATOM    122  CD1 LEU A  17       7.222  10.288  -8.772  1.00 17.84           C  
-ATOM    123  CD2 LEU A  17       7.417  12.631  -7.946  1.00 18.35           C  
-ATOM    124  N   PHE A  18       2.069  11.901  -7.466  1.00 17.20           N  
-ATOM    125  CA  PHE A  18       0.696  12.241  -7.855  1.00 18.28           C  
-ATOM    126  C   PHE A  18       0.242  13.559  -7.215  1.00 17.85           C  
-ATOM    127  O   PHE A  18      -0.288  14.454  -7.901  1.00 19.21           O  
-ATOM    128  CB  PHE A  18      -0.280  11.121  -7.483  1.00 18.24           C  
-ATOM    129  CG  PHE A  18      -1.686  11.395  -7.931  1.00 20.02           C  
-ATOM    130  CD1 PHE A  18      -2.054  11.185  -9.252  1.00 20.80           C  
-ATOM    131  CD2 PHE A  18      -2.636  11.888  -7.040  1.00 21.87           C  
-ATOM    132  CE1 PHE A  18      -3.360  11.450  -9.691  1.00 21.88           C  
-ATOM    133  CE2 PHE A  18      -3.950  12.150  -7.475  1.00 21.42           C  
-ATOM    134  CZ  PHE A  18      -4.301  11.922  -8.807  1.00 21.43           C  
-ATOM    135  N   ASN A  19       0.455  13.671  -5.906  1.00 18.03           N  
-ATOM    136  CA  ASN A  19       0.063  14.877  -5.153  1.00 18.90           C  
-ATOM    137  C   ASN A  19       0.807  16.121  -5.600  1.00 20.21           C  
-ATOM    138  O   ASN A  19       0.194  17.180  -5.721  1.00 21.60           O  
-ATOM    139  CB  ASN A  19       0.200  14.653  -3.638  1.00 20.45           C  
-ATOM    140  CG  ASN A  19      -0.795  13.639  -3.113  1.00 21.33           C  
-ATOM    141  OD1 ASN A  19      -1.831  13.398  -3.729  1.00 21.99           O  
-ATOM    142  ND2 ASN A  19      -0.490  13.034  -1.966  1.00 22.07           N  
-ATOM    143  N   LEU A  20       2.111  16.001  -5.868  1.00 20.10           N  
-ATOM    144  CA  LEU A  20       2.879  17.125  -6.410  1.00 21.09           C  
-ATOM    145  C   LEU A  20       2.403  17.561  -7.793  1.00 21.07           C  
-ATOM    146  O   LEU A  20       2.271  18.756  -8.067  1.00 21.34           O  
-ATOM    147  CB  LEU A  20       4.368  16.786  -6.501  1.00 21.73           C  
-ATOM    148  CG  LEU A  20       5.200  16.905  -5.235  1.00 23.19           C  
-ATOM    149  CD1 LEU A  20       6.598  16.355  -5.493  1.00 23.61           C  
-ATOM    150  CD2 LEU A  20       5.259  18.379  -4.801  1.00 24.68           C  
-ATOM    151  N   ILE A  21       2.149  16.588  -8.660  1.00 19.86           N  
-ATOM    152  CA  ILE A  21       1.799  16.853 -10.051  1.00 18.73           C  
-ATOM    153  C   ILE A  21       0.408  17.468 -10.193  1.00 19.51           C  
-ATOM    154  O   ILE A  21       0.224  18.352 -11.038  1.00 19.71           O  
-ATOM    155  CB  ILE A  21       1.871  15.563 -10.916  1.00 17.93           C  
-ATOM    156  CG1 ILE A  21       3.311  15.057 -11.022  1.00 19.09           C  
-ATOM    157  CG2 ILE A  21       1.344  15.827 -12.330  1.00 16.31           C  
-ATOM    158  CD1 ILE A  21       3.406  13.592 -11.409  1.00 17.83           C  
-ATOM    159  N   THR A  22      -0.538  16.984  -9.390  1.00 20.80           N  
-ATOM    160  CA  THR A  22      -1.937  17.419  -9.456  1.00 22.30           C  
-ATOM    161  C   THR A  22      -2.344  18.448  -8.398  1.00 26.03           C  
-ATOM    162  O   THR A  22      -3.383  19.105  -8.559  1.00 25.55           O  
-ATOM    163  CB  THR A  22      -2.922  16.233  -9.337  1.00 20.67           C  
-ATOM    164  OG1 THR A  22      -2.855  15.644  -8.026  1.00 20.98           O  
-ATOM    165  CG2 THR A  22      -2.635  15.198 -10.428  1.00 17.67           C  
-ATOM    166  N   GLY A  23      -1.553  18.583  -7.333  1.00 29.67           N  
-ATOM    167  CA  GLY A  23      -1.935  19.433  -6.208  1.00 32.49           C  
-ATOM    168  C   GLY A  23      -3.175  18.886  -5.525  1.00 35.27           C  
-ATOM    169  O   GLY A  23      -3.421  17.675  -5.529  1.00 35.59           O  
-ATOM    170  N   HIS A  24      -3.974  19.781  -4.954  1.00 37.91           N  
-ATOM    171  CA  HIS A  24      -5.189  19.380  -4.229  1.00 40.54           C  
-ATOM    172  C   HIS A  24      -6.398  19.090  -5.135  1.00 40.73           C  
-ATOM    173  O   HIS A  24      -7.429  18.643  -4.627  1.00 42.29           O  
-ATOM    174  CB  HIS A  24      -5.556  20.434  -3.173  1.00 41.45           C  
-ATOM    175  CG  HIS A  24      -4.441  20.740  -2.218  1.00 44.39           C  
-ATOM    176  ND1 HIS A  24      -4.273  20.067  -1.025  1.00 46.06           N  
-ATOM    177  CD2 HIS A  24      -3.436  21.647  -2.283  1.00 45.12           C  
-ATOM    178  CE1 HIS A  24      -3.212  20.546  -0.398  1.00 47.04           C  
-ATOM    179  NE2 HIS A  24      -2.686  21.506  -1.140  1.00 46.41           N  
-ATOM    180  N   ASN A  25      -6.282  19.331  -6.445  1.00 40.79           N  
-ATOM    181  CA  ASN A  25      -7.368  19.063  -7.407  1.00 41.09           C  
-ATOM    182  C   ASN A  25      -7.425  17.625  -7.914  1.00 38.73           C  
-ATOM    183  O   ASN A  25      -6.896  17.332  -8.991  1.00 40.62           O  
-ATOM    184  CB  ASN A  25      -7.271  19.984  -8.641  1.00 42.71           C  
-ATOM    185  CG  ASN A  25      -7.915  21.336  -8.431  1.00 44.54           C  
-ATOM    186  OD1 ASN A  25      -8.970  21.454  -7.798  1.00 48.06           O  
-ATOM    187  ND2 ASN A  25      -7.294  22.368  -8.988  1.00 46.08           N  
-ATOM    188  N   GLN A  26      -8.083  16.747  -7.161  1.00 34.69           N  
-ATOM    189  CA  GLN A  26      -8.244  15.351  -7.565  1.00 32.09           C  
-ATOM    190  C   GLN A  26      -9.698  14.888  -7.530  1.00 31.18           C  
-ATOM    191  O   GLN A  26     -10.544  15.499  -6.875  1.00 30.08           O  
-ATOM    192  CB  GLN A  26      -7.386  14.440  -6.687  1.00 32.05           C  
-ATOM    193  CG  GLN A  26      -7.723  14.478  -5.207  1.00 31.81           C  
-ATOM    194  CD  GLN A  26      -6.944  13.447  -4.423  1.00 32.70           C  
-ATOM    195  OE1 GLN A  26      -5.732  13.307  -4.605  1.00 30.89           O  
-ATOM    196  NE2 GLN A  26      -7.632  12.719  -3.544  1.00 30.91           N  
-ATOM    197  N   ARG A  27      -9.953  13.793  -8.238  1.00 28.55           N  
-ATOM    198  CA  ARG A  27     -11.253  13.151  -8.315  1.00 28.44           C  
-ATOM    199  C   ARG A  27     -11.075  11.711  -7.857  1.00 26.69           C  
-ATOM    200  O   ARG A  27     -10.211  11.013  -8.386  1.00 23.81           O  
-ATOM    201  CB  ARG A  27     -11.750  13.231  -9.757  1.00 29.62           C  
-ATOM    202  CG  ARG A  27     -13.070  12.592 -10.001  1.00 32.66           C  
-ATOM    203  CD  ARG A  27     -13.758  13.243 -11.182  1.00 34.86           C  
-ATOM    204  NE  ARG A  27     -12.905  13.358 -12.364  1.00 37.73           N  
-ATOM    205  CZ  ARG A  27     -12.750  12.428 -13.311  1.00 40.50           C  
-ATOM    206  NH1 ARG A  27     -13.378  11.252 -13.253  1.00 41.51           N  
-ATOM    207  NH2 ARG A  27     -11.943  12.675 -14.338  1.00 42.26           N  
-ATOM    208  N   VAL A  28     -11.873  11.273  -6.882  1.00 25.94           N  
-ATOM    209  CA  VAL A  28     -11.758   9.936  -6.302  1.00 26.10           C  
-ATOM    210  C   VAL A  28     -13.091   9.181  -6.341  1.00 26.82           C  
-ATOM    211  O   VAL A  28     -14.148   9.736  -6.042  1.00 25.65           O  
-ATOM    212  CB  VAL A  28     -11.242   9.987  -4.842  1.00 26.77           C  
-ATOM    213  CG1 VAL A  28     -11.120   8.584  -4.260  1.00 27.67           C  
-ATOM    214  CG2 VAL A  28      -9.902  10.673  -4.785  1.00 28.54           C  
-ATOM    215  N   GLY A  29     -13.023   7.912  -6.719  1.00 25.50           N  
-ATOM    216  CA  GLY A  29     -14.193   7.020  -6.752  1.00 26.62           C  
-ATOM    217  C   GLY A  29     -13.721   5.581  -6.682  1.00 25.52           C  
-ATOM    218  O   GLY A  29     -12.707   5.294  -6.053  1.00 25.24           O  
-ATOM    219  N   ASN A  30     -14.448   4.681  -7.323  1.00 26.07           N  
-ATOM    220  CA  ASN A  30     -14.039   3.290  -7.427  1.00 27.04           C  
-ATOM    221  C   ASN A  30     -14.066   2.850  -8.882  1.00 25.61           C  
-ATOM    222  O   ASN A  30     -14.781   3.436  -9.704  1.00 25.61           O  
-ATOM    223  CB  ASN A  30     -14.944   2.365  -6.600  1.00 28.65           C  
-ATOM    224  CG  ASN A  30     -16.372   2.325  -7.118  1.00 32.19           C  
-ATOM    225  OD1 ASN A  30     -17.129   3.284  -6.941  1.00 37.18           O  
-ATOM    226  ND2 ASN A  30     -16.753   1.218  -7.757  1.00 34.28           N  
-ATOM    227  N   TRP A  31     -13.292   1.819  -9.194  1.00 23.83           N  
-ATOM    228  CA  TRP A  31     -13.344   1.224 -10.525  1.00 24.23           C  
-ATOM    229  C   TRP A  31     -14.642   0.425 -10.626  1.00 25.19           C  
-ATOM    230  O   TRP A  31     -15.090  -0.157  -9.632  1.00 23.43           O  
-ATOM    231  CB  TRP A  31     -12.115   0.370 -10.822  1.00 24.23           C  
-ATOM    232  CG  TRP A  31     -10.892   1.207 -11.024  1.00 21.74           C  
-ATOM    233  CD1 TRP A  31      -9.987   1.560 -10.081  1.00 22.51           C  
-ATOM    234  CD2 TRP A  31     -10.446   1.800 -12.251  1.00 22.34           C  
-ATOM    235  NE1 TRP A  31      -8.998   2.343 -10.631  1.00 21.94           N  
-ATOM    236  CE2 TRP A  31      -9.256   2.504 -11.965  1.00 21.78           C  
-ATOM    237  CE3 TRP A  31     -10.944   1.815 -13.563  1.00 23.73           C  
-ATOM    238  CZ2 TRP A  31      -8.550   3.214 -12.939  1.00 24.11           C  
-ATOM    239  CZ3 TRP A  31     -10.240   2.529 -14.537  1.00 24.93           C  
-ATOM    240  CH2 TRP A  31      -9.055   3.214 -14.215  1.00 24.29           C  
-ATOM    241  N   PRO A  32     -15.263   0.409 -11.815  1.00 27.64           N  
-ATOM    242  CA  PRO A  32     -16.582  -0.221 -11.905  1.00 28.77           C  
-ATOM    243  C   PRO A  32     -16.605  -1.691 -11.479  1.00 29.69           C  
-ATOM    244  O   PRO A  32     -15.717  -2.468 -11.848  1.00 29.91           O  
-ATOM    245  CB  PRO A  32     -16.946  -0.090 -13.389  1.00 29.41           C  
-ATOM    246  CG  PRO A  32     -16.103   0.973 -13.907  1.00 29.77           C  
-ATOM    247  CD  PRO A  32     -14.860   1.029 -13.088  1.00 27.97           C  
-ATOM    248  N   GLY A  33     -17.618  -2.043 -10.692  1.00 30.97           N  
-ATOM    249  CA  GLY A  33     -17.818  -3.413 -10.215  1.00 31.13           C  
-ATOM    250  C   GLY A  33     -16.908  -3.901  -9.096  1.00 31.58           C  
-ATOM    251  O   GLY A  33     -17.061  -5.036  -8.649  1.00 31.81           O  
-ATOM    252  N   VAL A  34     -15.965  -3.067  -8.646  1.00 30.93           N  
-ATOM    253  CA  VAL A  34     -15.021  -3.426  -7.585  1.00 30.13           C  
-ATOM    254  C   VAL A  34     -14.860  -2.262  -6.607  1.00 29.92           C  
-ATOM    255  O   VAL A  34     -15.292  -1.136  -6.885  1.00 30.32           O  
-ATOM    256  CB  VAL A  34     -13.639  -3.830  -8.168  1.00 31.05           C  
-ATOM    257  CG1 VAL A  34     -13.762  -5.108  -8.996  1.00 30.81           C  
-ATOM    258  CG2 VAL A  34     -13.041  -2.701  -9.001  1.00 28.06           C  
-ATOM    259  N   THR A  35     -14.244  -2.533  -5.463  1.00 29.48           N  
-ATOM    260  CA  THR A  35     -13.998  -1.491  -4.461  1.00 30.03           C  
-ATOM    261  C   THR A  35     -12.597  -0.866  -4.549  1.00 28.94           C  
-ATOM    262  O   THR A  35     -12.209  -0.116  -3.657  1.00 30.65           O  
-ATOM    263  CB  THR A  35     -14.259  -2.025  -3.030  1.00 30.78           C  
-ATOM    264  OG1 THR A  35     -13.312  -3.048  -2.714  1.00 30.26           O  
-ATOM    265  CG2 THR A  35     -15.693  -2.569  -2.916  1.00 30.25           C  
-ATOM    266  N   VAL A  36     -11.844  -1.151  -5.611  1.00 26.06           N  
-ATOM    267  CA  VAL A  36     -10.519  -0.550  -5.787  1.00 24.92           C  
-ATOM    268  C   VAL A  36     -10.695   0.928  -6.113  1.00 23.90           C  
-ATOM    269  O   VAL A  36     -11.492   1.283  -6.991  1.00 22.63           O  
-ATOM    270  CB  VAL A  36      -9.713  -1.214  -6.915  1.00 23.84           C  
-ATOM    271  CG1 VAL A  36      -8.313  -0.608  -6.997  1.00 24.85           C  
-ATOM    272  CG2 VAL A  36      -9.620  -2.736  -6.714  1.00 23.73           C  
-ATOM    273  N   GLU A  37      -9.952   1.781  -5.414  1.00 23.65           N  
-ATOM    274  CA  GLU A  37     -10.028   3.227  -5.622  1.00 23.94           C  
-ATOM    275  C   GLU A  37      -9.689   3.603  -7.060  1.00 22.41           C  
-ATOM    276  O   GLU A  37      -8.728   3.086  -7.629  1.00 21.12           O  
-ATOM    277  CB  GLU A  37      -9.074   3.962  -4.669  1.00 25.22           C  
-ATOM    278  CG  GLU A  37      -8.864   5.444  -4.961  1.00 26.03           C  
-ATOM    279  CD  GLU A  37      -7.766   6.033  -4.105  1.00 28.85           C  
-ATOM    280  OE1 GLU A  37      -8.081   6.402  -2.955  1.00 27.46           O  
-ATOM    281  OE2 GLU A  37      -6.607   6.120  -4.588  1.00 28.55           O  
-ATOM    282  N   ARG A  38     -10.486   4.501  -7.631  1.00 19.61           N  
-ATOM    283  CA  ARG A  38     -10.189   5.113  -8.916  1.00 20.29           C  
-ATOM    284  C   ARG A  38      -9.926   6.580  -8.661  1.00 20.72           C  
-ATOM    285  O   ARG A  38     -10.826   7.300  -8.204  1.00 20.17           O  
-ATOM    286  CB  ARG A  38     -11.360   4.949  -9.869  1.00 22.35           C  
-ATOM    287  CG  ARG A  38     -11.151   5.500 -11.264  1.00 22.69           C  
-ATOM    288  CD  ARG A  38     -12.413   5.234 -12.067  1.00 27.26           C  
-ATOM    289  NE  ARG A  38     -12.277   5.531 -13.485  1.00 28.25           N  
-ATOM    290  CZ  ARG A  38     -13.247   5.345 -14.384  1.00 31.33           C  
-ATOM    291  NH1 ARG A  38     -14.446   4.875 -14.023  1.00 31.13           N  
-ATOM    292  NH2 ARG A  38     -13.020   5.647 -15.660  1.00 32.21           N  
-ATOM    293  N   LYS A  39      -8.703   7.022  -8.956  1.00 19.71           N  
-ATOM    294  CA  LYS A  39      -8.291   8.386  -8.675  1.00 19.70           C  
-ATOM    295  C   LYS A  39      -7.593   8.991  -9.878  1.00 19.54           C  
-ATOM    296  O   LYS A  39      -6.738   8.357 -10.491  1.00 18.03           O  
-ATOM    297  CB  LYS A  39      -7.354   8.428  -7.478  1.00 20.29           C  
-ATOM    298  CG  LYS A  39      -6.901   9.842  -7.079  1.00 23.13           C  
-ATOM    299  CD  LYS A  39      -6.199   9.842  -5.726  1.00 23.20           C  
-ATOM    300  CE  LYS A  39      -4.893   9.031  -5.741  1.00 23.98           C  
-ATOM    301  NZ  LYS A  39      -4.137   9.181  -4.455  1.00 25.50           N  
-ATOM    302  N   SER A  40      -7.958  10.229 -10.181  1.00 17.67           N  
-ATOM    303  CA  SER A  40      -7.323  10.982 -11.244  1.00 17.66           C  
-ATOM    304  C   SER A  40      -7.264  12.449 -10.876  1.00 17.46           C  
-ATOM    305  O   SER A  40      -7.951  12.898  -9.951  1.00 16.75           O  
-ATOM    306  CB  SER A  40      -8.084  10.810 -12.550  1.00 19.12           C  
-ATOM    307  OG  SER A  40      -9.390  11.359 -12.439  1.00 20.62           O  
-ATOM    308  N   GLY A  41      -6.435  13.170 -11.620  1.00 18.80           N  
-ATOM    309  CA  GLY A  41      -6.283  14.619 -11.469  1.00 19.17           C  
-ATOM    310  C   GLY A  41      -5.629  15.230 -12.682  1.00 18.84           C  
-ATOM    311  O   GLY A  41      -4.862  14.562 -13.379  1.00 20.13           O  
-ATOM    312  N   LEU A  42      -5.931  16.503 -12.948  1.00 17.91           N  
-ATOM    313  CA  LEU A  42      -5.293  17.242 -14.026  1.00 16.68           C  
-ATOM    314  C   LEU A  42      -3.918  17.729 -13.576  1.00 18.10           C  
-ATOM    315  O   LEU A  42      -3.716  18.018 -12.390  1.00 19.06           O  
-ATOM    316  CB  LEU A  42      -6.161  18.427 -14.457  1.00 17.77           C  
-ATOM    317  CG  LEU A  42      -7.563  18.058 -14.979  1.00 20.21           C  
-ATOM    318  CD1 LEU A  42      -8.316  19.326 -15.438  1.00 20.49           C  
-ATOM    319  CD2 LEU A  42      -7.510  17.022 -16.099  1.00 18.80           C  
-ATOM    320  N   VAL A  43      -2.975  17.825 -14.510  1.00 17.96           N  
-ATOM    321  CA  VAL A  43      -1.634  18.326 -14.164  1.00 19.58           C  
-ATOM    322  C   VAL A  43      -1.785  19.814 -13.803  1.00 21.22           C  
-ATOM    323  O   VAL A  43      -2.246  20.594 -14.621  1.00 21.36           O  
-ATOM    324  CB  VAL A  43      -0.625  18.111 -15.284  1.00 18.74           C  
-ATOM    325  CG1 VAL A  43       0.727  18.750 -14.951  1.00 21.10           C  
-ATOM    326  CG2 VAL A  43      -0.433  16.612 -15.531  1.00 18.38           C  
-ATOM    327  N   LYS A  44      -1.411  20.178 -12.577  1.00 23.44           N  
-ATOM    328  CA  LYS A  44      -1.579  21.558 -12.066  1.00 25.15           C  
-ATOM    329  C   LYS A  44      -1.006  22.602 -13.023  1.00 25.34           C  
-ATOM    330  O   LYS A  44      -1.637  23.634 -13.276  1.00 26.12           O  
-ATOM    331  CB  LYS A  44      -0.967  21.677 -10.654  1.00 25.14           C  
-ATOM    332  CG  LYS A  44      -1.153  23.027  -9.964  1.00 27.90           C  
-ATOM    333  N   LYS A  45       0.169  22.323 -13.584  1.00 26.59           N  
-ATOM    334  CA  LYS A  45       0.849  23.254 -14.505  1.00 25.77           C  
-ATOM    335  C   LYS A  45       0.515  23.085 -15.993  1.00 26.93           C  
-ATOM    336  O   LYS A  45       0.988  23.863 -16.825  1.00 26.89           O  
-ATOM    337  CB  LYS A  45       2.361  23.173 -14.277  1.00 26.14           C  
-ATOM    338  CG  LYS A  45       2.776  23.697 -12.917  1.00 27.97           C  
-ATOM    339  CD  LYS A  45       4.244  23.437 -12.651  1.00 28.23           C  
-ATOM    340  CE  LYS A  45       4.749  24.183 -11.441  1.00 29.18           C  
-ATOM    341  NZ  LYS A  45       6.245  24.149 -11.452  1.00 27.12           N  
-ATOM    342  N   ASN A  46      -0.302  22.086 -16.333  1.00 26.76           N  
-ATOM    343  CA  ASN A  46      -0.781  21.881 -17.699  1.00 26.60           C  
-ATOM    344  C   ASN A  46      -2.098  21.087 -17.677  1.00 26.69           C  
-ATOM    345  O   ASN A  46      -2.113  19.869 -17.730  1.00 24.91           O  
-ATOM    346  CB  ASN A  46       0.284  21.202 -18.564  1.00 26.53           C  
-ATOM    347  CG  ASN A  46      -0.111  21.123 -20.026  1.00 27.71           C  
-ATOM    348  OD1 ASN A  46      -1.249  21.408 -20.410  1.00 29.93           O  
-ATOM    349  ND2 ASN A  46       0.831  20.723 -20.855  1.00 29.27           N  
-ATOM    350  N   LYS A  47      -3.213  21.806 -17.620  1.00 26.05           N  
-ATOM    351  CA  LYS A  47      -4.526  21.190 -17.420  1.00 26.33           C  
-ATOM    352  C   LYS A  47      -5.038  20.413 -18.632  1.00 25.13           C  
-ATOM    353  O   LYS A  47      -6.045  19.718 -18.532  1.00 26.09           O  
-ATOM    354  CB  LYS A  47      -5.531  22.251 -16.959  1.00 26.47           C  
-ATOM    355  CG  LYS A  47      -5.181  22.928 -15.626  1.00 26.87           C  
-ATOM    356  CD  LYS A  47      -5.588  22.132 -14.398  1.00 27.17           C  
-ATOM    357  CE  LYS A  47      -5.376  22.951 -13.146  1.00 26.67           C  
-ATOM    358  NZ  LYS A  47      -5.852  22.279 -11.903  1.00 28.16           N  
-ATOM    359  N   ASP A  48      -4.354  20.526 -19.770  1.00 26.17           N  
-ATOM    360  CA  ASP A  48      -4.564  19.617 -20.911  1.00 26.41           C  
-ATOM    361  C   ASP A  48      -4.067  18.179 -20.666  1.00 24.51           C  
-ATOM    362  O   ASP A  48      -4.355  17.298 -21.470  1.00 25.36           O  
-ATOM    363  CB  ASP A  48      -3.887  20.161 -22.177  1.00 27.98           C  
-ATOM    364  CG  ASP A  48      -4.611  21.358 -22.765  1.00 31.73           C  
-ATOM    365  OD1 ASP A  48      -5.853  21.408 -22.666  1.00 34.08           O  
-ATOM    366  OD2 ASP A  48      -3.943  22.238 -23.347  1.00 35.62           O  
-ATOM    367  N   LEU A  49      -3.311  17.950 -19.589  1.00 21.76           N  
-ATOM    368  CA  LEU A  49      -2.806  16.626 -19.239  1.00 20.23           C  
-ATOM    369  C   LEU A  49      -3.578  16.063 -18.056  1.00 20.13           C  
-ATOM    370  O   LEU A  49      -3.718  16.733 -17.022  1.00 20.90           O  
-ATOM    371  CB  LEU A  49      -1.322  16.691 -18.869  1.00 19.22           C  
-ATOM    372  CG  LEU A  49      -0.355  17.405 -19.812  1.00 19.37           C  
-ATOM    373  CD1 LEU A  49       1.052  17.321 -19.228  1.00 21.36           C  
-ATOM    374  CD2 LEU A  49      -0.391  16.851 -21.224  1.00 20.41           C  
-ATOM    375  N   GLU A  50      -4.078  14.836 -18.189  1.00 18.70           N  
-ATOM    376  CA  GLU A  50      -4.743  14.177 -17.068  1.00 17.96           C  
-ATOM    377  C   GLU A  50      -3.923  12.986 -16.587  1.00 17.93           C  
-ATOM    378  O   GLU A  50      -3.471  12.174 -17.398  1.00 19.30           O  
-ATOM    379  CB  GLU A  50      -6.129  13.702 -17.464  1.00 18.77           C  
-ATOM    380  CG  GLU A  50      -6.915  13.089 -16.314  1.00 21.81           C  
-ATOM    381  CD  GLU A  50      -8.392  12.942 -16.640  1.00 23.90           C  
-ATOM    382  OE1 GLU A  50      -9.240  13.472 -15.893  1.00 27.71           O  
-ATOM    383  OE2 GLU A  50      -8.701  12.299 -17.654  1.00 27.08           O  
-ATOM    384  N   ILE A  51      -3.747  12.892 -15.276  1.00 16.87           N  
-ATOM    385  CA  ILE A  51      -3.053  11.775 -14.652  1.00 16.80           C  
-ATOM    386  C   ILE A  51      -4.110  10.787 -14.175  1.00 17.59           C  
-ATOM    387  O   ILE A  51      -4.969  11.122 -13.349  1.00 18.19           O  
-ATOM    388  CB  ILE A  51      -2.183  12.228 -13.463  1.00 15.23           C  
-ATOM    389  CG1 ILE A  51      -1.239  13.367 -13.886  1.00 15.38           C  
-ATOM    390  CG2 ILE A  51      -1.419  11.071 -12.876  1.00 13.99           C  
-ATOM    391  CD1 ILE A  51      -0.363  13.082 -15.067  1.00 14.67           C  
-ATOM    392  N   GLN A  52      -4.058   9.577 -14.718  1.00 17.58           N  
-ATOM    393  CA  GLN A  52      -4.868   8.487 -14.227  1.00 17.70           C  
-ATOM    394  C   GLN A  52      -3.984   7.723 -13.265  1.00 18.35           C  
-ATOM    395  O   GLN A  52      -3.057   7.016 -13.700  1.00 17.82           O  
-ATOM    396  CB  GLN A  52      -5.336   7.568 -15.368  1.00 17.99           C  
-ATOM    397  CG  GLN A  52      -6.186   6.387 -14.897  1.00 19.51           C  
-ATOM    398  CD  GLN A  52      -7.438   6.832 -14.185  1.00 21.04           C  
-ATOM    399  OE1 GLN A  52      -8.317   7.398 -14.807  1.00 22.39           O  
-ATOM    400  NE2 GLN A  52      -7.518   6.587 -12.874  1.00 19.60           N  
-ATOM    401  N   ASP A  53      -4.243   7.860 -11.967  1.00 17.71           N  
-ATOM    402  CA  ASP A  53      -3.538   7.045 -10.998  1.00 19.00           C  
-ATOM    403  C   ASP A  53      -4.009   5.604 -11.198  1.00 19.48           C  
-ATOM    404  O   ASP A  53      -5.163   5.348 -11.586  1.00 20.33           O  
-ATOM    405  CB  ASP A  53      -3.774   7.516  -9.561  1.00 20.02           C  
-ATOM    406  CG  ASP A  53      -2.819   6.883  -8.568  1.00 21.90           C  
-ATOM    407  OD1 ASP A  53      -1.606   6.798  -8.854  1.00 24.06           O  
-ATOM    408  OD2 ASP A  53      -3.288   6.470  -7.491  1.00 24.69           O  
-ATOM    409  N   LEU A  54      -3.091   4.675 -10.971  1.00 17.86           N  
-ATOM    410  CA  LEU A  54      -3.393   3.257 -11.001  1.00 17.41           C  
-ATOM    411  C   LEU A  54      -2.879   2.677  -9.695  1.00 18.39           C  
-ATOM    412  O   LEU A  54      -1.937   3.225  -9.119  1.00 17.22           O  
-ATOM    413  CB  LEU A  54      -2.751   2.591 -12.218  1.00 17.35           C  
-ATOM    414  CG  LEU A  54      -3.278   2.993 -13.592  1.00 17.80           C  
-ATOM    415  CD1 LEU A  54      -2.500   2.277 -14.704  1.00 17.42           C  
-ATOM    416  CD2 LEU A  54      -4.775   2.678 -13.734  1.00 18.23           C  
-ATOM    417  N   PRO A  55      -3.493   1.581  -9.210  1.00 19.75           N  
-ATOM    418  CA  PRO A  55      -3.068   0.999  -7.925  1.00 20.79           C  
-ATOM    419  C   PRO A  55      -1.600   0.602  -7.957  1.00 19.30           C  
-ATOM    420  O   PRO A  55      -1.110   0.161  -8.998  1.00 20.32           O  
-ATOM    421  CB  PRO A  55      -3.931  -0.261  -7.779  1.00 20.38           C  
-ATOM    422  CG  PRO A  55      -4.987  -0.167  -8.777  1.00 20.81           C  
-ATOM    423  CD  PRO A  55      -4.594   0.818  -9.830  1.00 21.03           C  
-ATOM    424  N   GLY A  56      -0.913   0.784  -6.838  1.00 18.27           N  
-ATOM    425  CA  GLY A  56       0.464   0.331  -6.709  1.00 18.39           C  
-ATOM    426  C   GLY A  56       0.502  -1.187  -6.799  1.00 16.85           C  
-ATOM    427  O   GLY A  56      -0.205  -1.876  -6.051  1.00 17.53           O  
-ATOM    428  N   ILE A  57       1.308  -1.715  -7.717  1.00 15.38           N  
-ATOM    429  CA  ILE A  57       1.447  -3.163  -7.903  1.00 15.49           C  
-ATOM    430  C   ILE A  57       2.893  -3.541  -8.201  1.00 14.29           C  
-ATOM    431  O   ILE A  57       3.694  -2.703  -8.630  1.00 14.13           O  
-ATOM    432  CB  ILE A  57       0.534  -3.689  -9.038  1.00 16.92           C  
-ATOM    433  CG1 ILE A  57       0.866  -3.033 -10.384  1.00 17.97           C  
-ATOM    434  CG2 ILE A  57      -0.937  -3.434  -8.718  1.00 17.35           C  
-ATOM    435  CD1 ILE A  57       0.065  -3.620 -11.546  1.00 17.94           C  
-ATOM    436  N   TYR A  58       3.216  -4.811  -7.982  1.00 14.64           N  
-ATOM    437  CA  TYR A  58       4.543  -5.374  -8.286  1.00 15.03           C  
-ATOM    438  C   TYR A  58       4.637  -6.102  -9.635  1.00 15.53           C  
-ATOM    439  O   TYR A  58       5.729  -6.290 -10.177  1.00 13.84           O  
-ATOM    440  CB  TYR A  58       4.938  -6.368  -7.186  1.00 16.42           C  
-ATOM    441  CG  TYR A  58       5.163  -5.686  -5.873  1.00 16.54           C  
-ATOM    442  CD1 TYR A  58       6.305  -4.919  -5.669  1.00 17.03           C  
-ATOM    443  CD2 TYR A  58       4.244  -5.786  -4.837  1.00 17.56           C  
-ATOM    444  CE1 TYR A  58       6.529  -4.269  -4.472  1.00 18.90           C  
-ATOM    445  CE2 TYR A  58       4.464  -5.134  -3.628  1.00 19.35           C  
-ATOM    446  CZ  TYR A  58       5.610  -4.381  -3.452  1.00 18.87           C  
-ATOM    447  OH  TYR A  58       5.841  -3.716  -2.258  1.00 22.46           O  
-ATOM    448  N  ASER A  59       3.494  -6.530 -10.165  0.30 15.26           N  
-ATOM    449  N  BSER A  59       3.487  -6.498 -10.164  0.70 14.10           N  
-ATOM    450  CA ASER A  59       3.443  -7.249 -11.431  0.30 15.76           C  
-ATOM    451  CA BSER A  59       3.425  -7.276 -11.389  0.70 14.27           C  
-ATOM    452  C  ASER A  59       2.002  -7.304 -11.876  0.30 15.76           C  
-ATOM    453  C  BSER A  59       2.018  -7.171 -11.926  0.70 15.23           C  
-ATOM    454  O  ASER A  59       1.106  -7.065 -11.067  0.30 15.97           O  
-ATOM    455  O  BSER A  59       1.164  -6.624 -11.246  0.70 16.55           O  
-ATOM    456  CB ASER A  59       3.954  -8.683 -11.280  0.30 15.97           C  
-ATOM    457  CB BSER A  59       3.775  -8.737 -11.093  0.70 13.62           C  
-ATOM    458  OG ASER A  59       2.990  -9.494 -10.633  0.30 16.73           O  
-ATOM    459  OG BSER A  59       3.898  -9.484 -12.287  0.70 10.95           O  
-ATOM    460  N   MET A  60       1.786  -7.643 -13.146  1.00 15.28           N  
-ATOM    461  CA  MET A  60       0.436  -7.708 -13.722  1.00 16.61           C  
-ATOM    462  C   MET A  60      -0.001  -9.178 -13.815  1.00 16.62           C  
-ATOM    463  O   MET A  60      -0.159  -9.748 -14.907  1.00 15.95           O  
-ATOM    464  CB  MET A  60       0.380  -6.976 -15.063  1.00 17.97           C  
-ATOM    465  CG  MET A  60       0.267  -5.473 -14.875  1.00 20.38           C  
-ATOM    466  SD  MET A  60      -0.054  -4.599 -16.416  1.00 27.03           S  
-ATOM    467  CE  MET A  60       1.507  -4.862 -17.139  1.00 10.20           C  
-ATOM    468  N   SER A  61      -0.202  -9.759 -12.639  1.00 17.03           N  
-ATOM    469  CA  SER A  61      -0.652 -11.140 -12.503  1.00 18.88           C  
-ATOM    470  C   SER A  61      -2.178 -11.171 -12.356  1.00 19.68           C  
-ATOM    471  O   SER A  61      -2.808 -10.137 -12.133  1.00 19.43           O  
-ATOM    472  CB  SER A  61       0.018 -11.808 -11.298  1.00 20.96           C  
-ATOM    473  OG  SER A  61      -0.784 -11.653 -10.134  1.00 25.17           O  
-ATOM    474  N   PRO A  62      -2.790 -12.363 -12.469  1.00 20.66           N  
-ATOM    475  CA  PRO A  62      -4.251 -12.421 -12.358  1.00 23.07           C  
-ATOM    476  C   PRO A  62      -4.792 -12.494 -10.917  1.00 26.12           C  
-ATOM    477  O   PRO A  62      -6.005 -12.598 -10.735  1.00 29.34           O  
-ATOM    478  CB  PRO A  62      -4.613 -13.695 -13.164  1.00 23.30           C  
-ATOM    479  CG  PRO A  62      -3.387 -14.537 -13.191  1.00 23.14           C  
-ATOM    480  CD  PRO A  62      -2.194 -13.670 -12.796  1.00 21.15           C  
-ATOM    481  N   TYR A  63      -3.918 -12.395  -9.917  1.00 26.55           N  
-ATOM    482  CA  TYR A  63      -4.233 -12.756  -8.536  1.00 28.88           C  
-ATOM    483  C   TYR A  63      -4.620 -11.635  -7.569  1.00 28.70           C  
-ATOM    484  O   TYR A  63      -4.806 -11.899  -6.377  1.00 31.13           O  
-ATOM    485  CB  TYR A  63      -3.044 -13.545  -7.972  1.00 30.25           C  
-ATOM    486  CG  TYR A  63      -2.684 -14.750  -8.833  1.00 33.68           C  
-ATOM    487  CD1 TYR A  63      -3.634 -15.731  -9.111  1.00 34.02           C  
-ATOM    488  CD2 TYR A  63      -1.399 -14.907  -9.366  1.00 34.53           C  
-ATOM    489  CE1 TYR A  63      -3.326 -16.836  -9.892  1.00 35.82           C  
-ATOM    490  CE2 TYR A  63      -1.078 -16.020 -10.155  1.00 35.91           C  
-ATOM    491  CZ  TYR A  63      -2.056 -16.977 -10.413  1.00 36.19           C  
-ATOM    492  OH  TYR A  63      -1.788 -18.085 -11.185  1.00 40.18           O  
-ATOM    493  N   SER A  64      -4.735 -10.394  -8.034  1.00 26.05           N  
-ATOM    494  CA  SER A  64      -5.316  -9.358  -7.177  1.00 24.84           C  
-ATOM    495  C   SER A  64      -6.205  -8.419  -7.974  1.00 23.66           C  
-ATOM    496  O   SER A  64      -5.944  -8.184  -9.164  1.00 21.53           O  
-ATOM    497  CB  SER A  64      -4.249  -8.577  -6.412  1.00 25.66           C  
-ATOM    498  OG  SER A  64      -3.655  -7.588  -7.212  1.00 23.68           O  
-ATOM    499  N   PRO A  65      -7.257  -7.881  -7.323  1.00 22.59           N  
-ATOM    500  CA  PRO A  65      -8.138  -6.916  -7.963  1.00 21.93           C  
-ATOM    501  C   PRO A  65      -7.405  -5.691  -8.497  1.00 18.65           C  
-ATOM    502  O   PRO A  65      -7.746  -5.195  -9.555  1.00 18.10           O  
-ATOM    503  CB  PRO A  65      -9.075  -6.508  -6.827  1.00 22.97           C  
-ATOM    504  CG  PRO A  65      -9.151  -7.744  -5.986  1.00 23.23           C  
-ATOM    505  CD  PRO A  65      -7.757  -8.238  -5.973  1.00 24.34           C  
-ATOM    506  N   GLU A  66      -6.414  -5.239  -7.738  1.00 19.12           N  
-ATOM    507  CA  GLU A  66      -5.580  -4.089  -8.084  1.00 18.84           C  
-ATOM    508  C   GLU A  66      -4.778  -4.332  -9.358  1.00 17.30           C  
-ATOM    509  O   GLU A  66      -4.733  -3.479 -10.233  1.00 16.48           O  
-ATOM    510  CB  GLU A  66      -4.637  -3.762  -6.930  1.00 19.82           C  
-ATOM    511  CG  GLU A  66      -5.335  -3.169  -5.714  1.00 21.72           C  
-ATOM    512  CD  GLU A  66      -5.991  -4.189  -4.791  1.00 24.22           C  
-ATOM    513  OE1 GLU A  66      -5.733  -5.414  -4.913  1.00 20.88           O  
-ATOM    514  OE2 GLU A  66      -6.784  -3.749  -3.932  1.00 24.44           O  
-ATOM    515  N  AGLU A  67      -4.146  -5.499  -9.451  0.50 18.06           N  
-ATOM    516  N  BGLU A  67      -4.148  -5.499  -9.457  0.50 18.27           N  
-ATOM    517  CA AGLU A  67      -3.424  -5.894 -10.658  0.50 17.84           C  
-ATOM    518  CA BGLU A  67      -3.411  -5.869 -10.665  0.50 18.22           C  
-ATOM    519  C  AGLU A  67      -4.349  -6.001 -11.869  0.50 18.08           C  
-ATOM    520  C  BGLU A  67      -4.340  -6.019 -11.875  0.50 18.28           C  
-ATOM    521  O  AGLU A  67      -3.979  -5.617 -12.979  0.50 16.41           O  
-ATOM    522  O  BGLU A  67      -3.962  -5.676 -12.996  0.50 16.59           O  
-ATOM    523  CB AGLU A  67      -2.745  -7.239 -10.443  0.50 17.79           C  
-ATOM    524  CB BGLU A  67      -2.618  -7.150 -10.428  0.50 18.42           C  
-ATOM    525  CG AGLU A  67      -1.552  -7.190  -9.526  0.50 17.45           C  
-ATOM    526  CG BGLU A  67      -1.486  -6.963  -9.436  0.50 18.61           C  
-ATOM    527  CD AGLU A  67      -1.115  -8.574  -9.137  0.50 17.65           C  
-ATOM    528  CD BGLU A  67      -0.779  -8.255  -9.119  0.50 19.78           C  
-ATOM    529  OE1AGLU A  67      -0.084  -9.048  -9.656  0.50 19.06           O  
-ATOM    530  OE1BGLU A  67      -0.606  -9.081 -10.035  0.50 20.38           O  
-ATOM    531  OE2AGLU A  67      -1.822  -9.192  -8.326  0.50 17.57           O  
-ATOM    532  OE2BGLU A  67      -0.389  -8.445  -7.955  0.50 20.42           O  
-ATOM    533  N   LYS A  68      -5.556  -6.518 -11.651  1.00 18.81           N  
-ATOM    534  CA  LYS A  68      -6.534  -6.651 -12.740  1.00 18.93           C  
-ATOM    535  C   LYS A  68      -6.997  -5.279 -13.234  1.00 16.64           C  
-ATOM    536  O   LYS A  68      -7.101  -5.052 -14.434  1.00 14.90           O  
-ATOM    537  CB  LYS A  68      -7.732  -7.526 -12.326  1.00 20.08           C  
-ATOM    538  CG  LYS A  68      -8.669  -7.818 -13.494  1.00 23.31           C  
-ATOM    539  CD  LYS A  68      -9.753  -8.849 -13.169  1.00 24.10           C  
-ATOM    540  CE  LYS A  68     -10.607  -9.138 -14.390  1.00 23.46           C  
-ATOM    541  NZ  LYS A  68     -11.396  -7.956 -14.828  1.00 21.58           N  
-ATOM    542  N   VAL A  69      -7.281  -4.367 -12.309  1.00 15.93           N  
-ATOM    543  CA  VAL A  69      -7.662  -3.006 -12.686  1.00 16.02           C  
-ATOM    544  C   VAL A  69      -6.573  -2.363 -13.548  1.00 15.41           C  
-ATOM    545  O   VAL A  69      -6.875  -1.784 -14.594  1.00 15.30           O  
-ATOM    546  CB  VAL A  69      -8.008  -2.138 -11.441  1.00 17.01           C  
-ATOM    547  CG1 VAL A  69      -7.810  -0.621 -11.690  1.00 17.13           C  
-ATOM    548  CG2 VAL A  69      -9.445  -2.457 -11.013  1.00 15.89           C  
-ATOM    549  N   ALA A  70      -5.321  -2.489 -13.125  1.00 14.53           N  
-ATOM    550  CA  ALA A  70      -4.213  -1.872 -13.868  1.00 15.53           C  
-ATOM    551  C   ALA A  70      -4.120  -2.465 -15.274  1.00 15.37           C  
-ATOM    552  O   ALA A  70      -4.053  -1.738 -16.271  1.00 13.77           O  
-ATOM    553  CB  ALA A  70      -2.903  -2.026 -13.124  1.00 14.25           C  
-ATOM    554  N   ARG A  71      -4.130  -3.792 -15.359  1.00 15.97           N  
-ATOM    555  CA  ARG A  71      -4.042  -4.469 -16.650  1.00 15.67           C  
-ATOM    556  C   ARG A  71      -5.166  -4.078 -17.612  1.00 16.00           C  
-ATOM    557  O   ARG A  71      -4.893  -3.684 -18.753  1.00 14.74           O  
-ATOM    558  CB  ARG A  71      -4.048  -5.985 -16.461  1.00 16.93           C  
-ATOM    559  CG  ARG A  71      -3.830  -6.744 -17.742  1.00 16.15           C  
-ATOM    560  CD  ARG A  71      -4.266  -8.174 -17.636  1.00 14.07           C  
-ATOM    561  NE  ARG A  71      -3.428  -8.963 -16.741  1.00 17.14           N  
-ATOM    562  CZ  ARG A  71      -3.368 -10.294 -16.731  1.00 16.24           C  
-ATOM    563  NH1 ARG A  71      -4.101 -11.017 -17.579  1.00 16.43           N  
-ATOM    564  NH2 ARG A  71      -2.570 -10.909 -15.867  1.00 15.38           N  
-ATOM    565  N   ASP A  72      -6.417  -4.202 -17.160  1.00 15.93           N  
-ATOM    566  CA  ASP A  72      -7.578  -3.901 -18.006  1.00 16.46           C  
-ATOM    567  C   ASP A  72      -7.515  -2.471 -18.525  1.00 15.79           C  
-ATOM    568  O   ASP A  72      -7.773  -2.212 -19.700  1.00 15.43           O  
-ATOM    569  CB  ASP A  72      -8.906  -4.115 -17.267  1.00 17.15           C  
-ATOM    570  CG  ASP A  72      -9.168  -5.577 -16.929  1.00 19.53           C  
-ATOM    571  OD1 ASP A  72      -8.495  -6.472 -17.496  1.00 19.81           O  
-ATOM    572  OD2 ASP A  72     -10.038  -5.851 -16.083  1.00 19.68           O  
-ATOM    573  N   TYR A  73      -7.162  -1.541 -17.651  1.00 15.61           N  
-ATOM    574  CA  TYR A  73      -7.049  -0.161 -18.066  1.00 14.70           C  
-ATOM    575  C   TYR A  73      -5.964   0.011 -19.125  1.00 14.98           C  
-ATOM    576  O   TYR A  73      -6.197   0.624 -20.172  1.00 14.93           O  
-ATOM    577  CB  TYR A  73      -6.752   0.743 -16.885  1.00 15.28           C  
-ATOM    578  CG  TYR A  73      -6.546   2.149 -17.347  1.00 18.18           C  
-ATOM    579  CD1 TYR A  73      -7.632   2.943 -17.708  1.00 19.25           C  
-ATOM    580  CD2 TYR A  73      -5.267   2.688 -17.451  1.00 18.54           C  
-ATOM    581  CE1 TYR A  73      -7.446   4.246 -18.151  1.00 19.86           C  
-ATOM    582  CE2 TYR A  73      -5.077   3.973 -17.885  1.00 21.00           C  
-ATOM    583  CZ  TYR A  73      -6.164   4.750 -18.232  1.00 23.80           C  
-ATOM    584  OH  TYR A  73      -5.958   6.038 -18.667  1.00 27.47           O  
-ATOM    585  N   LEU A  74      -4.778  -0.531 -18.867  1.00 15.02           N  
-ATOM    586  CA  LEU A  74      -3.678  -0.382 -19.834  1.00 14.43           C  
-ATOM    587  C   LEU A  74      -3.923  -1.076 -21.178  1.00 15.31           C  
-ATOM    588  O   LEU A  74      -3.489  -0.567 -22.208  1.00 15.77           O  
-ATOM    589  CB  LEU A  74      -2.348  -0.835 -19.222  1.00 14.96           C  
-ATOM    590  CG  LEU A  74      -1.888   0.037 -18.049  1.00 16.00           C  
-ATOM    591  CD1 LEU A  74      -0.649  -0.571 -17.422  1.00 16.40           C  
-ATOM    592  CD2 LEU A  74      -1.625   1.510 -18.501  1.00 12.61           C  
-ATOM    593  N  ALEU A  75      -4.595  -2.227 -21.157  0.50 16.15           N  
-ATOM    594  N  BLEU A  75      -4.598  -2.224 -21.170  0.50 15.65           N  
-ATOM    595  CA ALEU A  75      -4.951  -2.943 -22.387  0.50 17.08           C  
-ATOM    596  CA BLEU A  75      -4.926  -2.920 -22.418  0.50 16.21           C  
-ATOM    597  C  ALEU A  75      -6.149  -2.327 -23.123  0.50 18.05           C  
-ATOM    598  C  BLEU A  75      -6.182  -2.362 -23.111  0.50 17.58           C  
-ATOM    599  O  ALEU A  75      -6.390  -2.668 -24.273  0.50 18.55           O  
-ATOM    600  O  BLEU A  75      -6.505  -2.789 -24.212  0.50 18.09           O  
-ATOM    601  CB ALEU A  75      -5.223  -4.420 -22.099  0.50 17.76           C  
-ATOM    602  CB BLEU A  75      -5.060  -4.423 -22.179  0.50 16.24           C  
-ATOM    603  CG ALEU A  75      -3.994  -5.323 -22.211  0.50 18.61           C  
-ATOM    604  CG BLEU A  75      -3.713  -5.131 -22.031  0.50 16.26           C  
-ATOM    605  CD1ALEU A  75      -2.785  -4.702 -21.522  0.50 19.84           C  
-ATOM    606  CD1BLEU A  75      -2.842  -4.895 -23.270  0.50 15.15           C  
-ATOM    607  CD2ALEU A  75      -4.286  -6.721 -21.673  0.50 18.98           C  
-ATOM    608  CD2BLEU A  75      -2.981  -4.681 -20.781  0.50 17.21           C  
-ATOM    609  N   SER A  76      -6.888  -1.424 -22.479  1.00 18.91           N  
-ATOM    610  CA  SER A  76      -8.054  -0.760 -23.106  1.00 19.82           C  
-ATOM    611  C   SER A  76      -7.644   0.295 -24.138  1.00 22.44           C  
-ATOM    612  O   SER A  76      -8.491   0.816 -24.865  1.00 21.46           O  
-ATOM    613  CB  SER A  76      -8.950  -0.095 -22.050  1.00 21.01           C  
-ATOM    614  OG  SER A  76      -8.412   1.136 -21.570  1.00 20.45           O  
-ATOM    615  N   GLN A  77      -6.356   0.631 -24.182  1.00 22.91           N  
-ATOM    616  CA  GLN A  77      -5.821   1.627 -25.089  1.00 25.78           C  
-ATOM    617  C   GLN A  77      -6.444   3.033 -24.870  1.00 25.62           C  
-ATOM    618  O   GLN A  77      -6.551   3.806 -25.814  1.00 29.09           O  
-ATOM    619  CB  GLN A  77      -5.946   1.162 -26.557  1.00 27.26           C  
-ATOM    620  CG  GLN A  77      -5.550  -0.317 -26.796  1.00 28.50           C  
-ATOM    621  CD  GLN A  77      -5.329  -0.653 -28.268  1.00 29.24           C  
-ATOM    622  OE1 GLN A  77      -6.021  -1.512 -28.844  1.00 28.21           O  
-ATOM    623  NE2 GLN A  77      -4.370   0.031 -28.886  1.00 24.08           N  
-ATOM    624  N   ARG A  78      -6.843   3.352 -23.636  1.00 23.57           N  
-ATOM    625  CA  ARG A  78      -7.330   4.690 -23.275  1.00 22.79           C  
-ATOM    626  C   ARG A  78      -6.180   5.604 -22.833  1.00 21.77           C  
-ATOM    627  O   ARG A  78      -6.291   6.823 -22.933  1.00 23.77           O  
-ATOM    628  CB  ARG A  78      -8.367   4.629 -22.153  1.00 23.50           C  
-ATOM    629  N   ALA A  79      -5.090   5.026 -22.330  1.00 18.33           N  
-ATOM    630  CA  ALA A  79      -3.916   5.807 -21.959  1.00 18.33           C  
-ATOM    631  C   ALA A  79      -3.041   6.141 -23.170  1.00 18.69           C  
-ATOM    632  O   ALA A  79      -2.757   5.275 -24.000  1.00 18.77           O  
-ATOM    633  CB  ALA A  79      -3.093   5.045 -20.919  1.00 19.19           C  
-ATOM    634  N   ASP A  80      -2.612   7.395 -23.269  1.00 16.36           N  
-ATOM    635  CA  ASP A  80      -1.683   7.830 -24.288  1.00 16.76           C  
-ATOM    636  C   ASP A  80      -0.249   7.493 -23.909  1.00 14.75           C  
-ATOM    637  O   ASP A  80       0.547   7.225 -24.785  1.00 13.80           O  
-ATOM    638  CB  ASP A  80      -1.809   9.334 -24.516  1.00 17.88           C  
-ATOM    639  CG  ASP A  80      -3.192   9.722 -25.019  1.00 20.06           C  
-ATOM    640  OD1 ASP A  80      -3.521   9.354 -26.154  1.00 22.94           O  
-ATOM    641  OD2 ASP A  80      -3.938  10.379 -24.279  1.00 19.64           O  
-ATOM    642  N   SER A  81       0.050   7.525 -22.611  1.00 15.12           N  
-ATOM    643  CA  SER A  81       1.398   7.355 -22.065  1.00 15.01           C  
-ATOM    644  C   SER A  81       1.324   6.615 -20.740  1.00 14.33           C  
-ATOM    645  O   SER A  81       0.324   6.718 -20.034  1.00 14.77           O  
-ATOM    646  CB  SER A  81       2.016   8.744 -21.826  1.00 16.16           C  
-ATOM    647  OG  SER A  81       2.931   8.755 -20.735  1.00 19.04           O  
-ATOM    648  N   ILE A  82       2.370   5.856 -20.410  1.00 13.88           N  
-ATOM    649  CA  ILE A  82       2.534   5.305 -19.067  1.00 14.12           C  
-ATOM    650  C   ILE A  82       3.684   6.072 -18.415  1.00 13.93           C  
-ATOM    651  O   ILE A  82       4.765   6.125 -18.991  1.00 14.99           O  
-ATOM    652  CB  ILE A  82       2.885   3.808 -19.072  1.00 14.08           C  
-ATOM    653  CG1 ILE A  82       1.713   2.966 -19.573  1.00 13.28           C  
-ATOM    654  CG2 ILE A  82       3.247   3.328 -17.660  1.00 13.53           C  
-ATOM    655  CD1 ILE A  82       2.071   1.485 -19.732  1.00 14.06           C  
-ATOM    656  N   LEU A  83       3.443   6.651 -17.236  1.00 14.33           N  
-ATOM    657  CA  LEU A  83       4.486   7.280 -16.418  1.00 14.85           C  
-ATOM    658  C   LEU A  83       4.734   6.318 -15.256  1.00 13.47           C  
-ATOM    659  O   LEU A  83       3.911   6.171 -14.339  1.00 12.82           O  
-ATOM    660  CB  LEU A  83       4.069   8.676 -15.943  1.00 16.27           C  
-ATOM    661  CG  LEU A  83       5.089   9.450 -15.097  1.00 19.03           C  
-ATOM    662  CD1 LEU A  83       6.468   9.548 -15.725  1.00 22.35           C  
-ATOM    663  CD2 LEU A  83       4.541  10.853 -14.831  1.00 18.93           C  
-ATOM    664  N   ASN A  84       5.873   5.640 -15.335  1.00 12.55           N  
-ATOM    665  CA  ASN A  84       6.226   4.539 -14.449  1.00 11.70           C  
-ATOM    666  C   ASN A  84       7.124   5.095 -13.348  1.00 13.60           C  
-ATOM    667  O   ASN A  84       8.251   5.507 -13.627  1.00 11.52           O  
-ATOM    668  CB  ASN A  84       6.903   3.428 -15.288  1.00 12.90           C  
-ATOM    669  CG  ASN A  84       7.401   2.241 -14.473  1.00 12.42           C  
-ATOM    670  OD1 ASN A  84       8.328   1.536 -14.899  1.00 13.17           O  
-ATOM    671  ND2 ASN A  84       6.795   1.998 -13.317  1.00 12.60           N  
-ATOM    672  N   VAL A  85       6.613   5.105 -12.115  1.00 12.20           N  
-ATOM    673  CA  VAL A  85       7.375   5.550 -10.934  1.00 13.06           C  
-ATOM    674  C   VAL A  85       8.189   4.358 -10.424  1.00 12.82           C  
-ATOM    675  O   VAL A  85       7.630   3.313 -10.073  1.00 13.67           O  
-ATOM    676  CB  VAL A  85       6.451   6.104  -9.819  1.00 13.41           C  
-ATOM    677  CG1 VAL A  85       7.259   6.580  -8.608  1.00 14.46           C  
-ATOM    678  CG2 VAL A  85       5.583   7.227 -10.368  1.00 14.37           C  
-ATOM    679  N   VAL A  86       9.506   4.530 -10.412  1.00 14.42           N  
-ATOM    680  CA  VAL A  86      10.468   3.499 -10.024  1.00 15.27           C  
-ATOM    681  C   VAL A  86      11.330   3.991  -8.858  1.00 16.83           C  
-ATOM    682  O   VAL A  86      11.902   5.076  -8.922  1.00 17.27           O  
-ATOM    683  CB  VAL A  86      11.366   3.135 -11.235  1.00 16.37           C  
-ATOM    684  CG1 VAL A  86      12.592   2.279 -10.843  1.00 15.12           C  
-ATOM    685  CG2 VAL A  86      10.521   2.434 -12.316  1.00 13.61           C  
-ATOM    686  N   ASP A  87      11.407   3.172  -7.811  1.00 16.86           N  
-ATOM    687  CA  ASP A  87      12.253   3.409  -6.654  1.00 16.87           C  
-ATOM    688  C   ASP A  87      13.718   3.115  -6.977  1.00 14.61           C  
-ATOM    689  O   ASP A  87      14.138   1.941  -7.035  1.00 14.21           O  
-ATOM    690  CB  ASP A  87      11.782   2.518  -5.499  1.00 17.58           C  
-ATOM    691  CG  ASP A  87      12.593   2.707  -4.221  1.00 18.68           C  
-ATOM    692  OD1 ASP A  87      13.535   3.516  -4.177  1.00 16.97           O  
-ATOM    693  OD2 ASP A  87      12.270   2.020  -3.246  1.00 19.28           O  
-ATOM    694  N   ALA A  88      14.493   4.185  -7.150  1.00 14.75           N  
-ATOM    695  CA  ALA A  88      15.913   4.082  -7.498  1.00 16.38           C  
-ATOM    696  C   ALA A  88      16.730   3.250  -6.514  1.00 18.08           C  
-ATOM    697  O   ALA A  88      17.718   2.644  -6.919  1.00 18.87           O  
-ATOM    698  CB  ALA A  88      16.530   5.454  -7.626  1.00 14.83           C  
-ATOM    699  N   THR A  89      16.317   3.226  -5.242  1.00 18.59           N  
-ATOM    700  CA  THR A  89      17.039   2.494  -4.190  1.00 19.97           C  
-ATOM    701  C   THR A  89      16.721   0.994  -4.191  1.00 21.64           C  
-ATOM    702  O   THR A  89      17.282   0.241  -3.409  1.00 20.94           O  
-ATOM    703  CB  THR A  89      16.745   3.053  -2.776  1.00 19.65           C  
-ATOM    704  OG1 THR A  89      15.456   2.605  -2.331  1.00 18.42           O  
-ATOM    705  CG2 THR A  89      16.816   4.582  -2.750  1.00 21.04           C  
-ATOM    706  N   ASN A  90      15.812   0.567  -5.061  1.00 20.59           N  
-ATOM    707  CA  ASN A  90      15.438  -0.833  -5.187  1.00 21.13           C  
-ATOM    708  C   ASN A  90      15.158  -1.142  -6.651  1.00 18.16           C  
-ATOM    709  O   ASN A  90      14.104  -1.687  -7.011  1.00 15.94           O  
-ATOM    710  CB  ASN A  90      14.194  -1.022  -4.346  1.00 22.93           C  
-ATOM    711  CG  ASN A  90      13.793  -2.449  -4.196  1.00 26.44           C  
-ATOM    712  OD1 ASN A  90      12.607  -2.724  -4.056  1.00 29.94           O  
-ATOM    713  ND2 ASN A  90      14.748  -3.368  -4.226  1.00 30.02           N  
-ATOM    714  N   LEU A  91      16.123  -0.784  -7.482  1.00 17.71           N  
-ATOM    715  CA  LEU A  91      15.925  -0.709  -8.940  1.00 17.45           C  
-ATOM    716  C   LEU A  91      15.491  -2.021  -9.595  1.00 17.73           C  
-ATOM    717  O   LEU A  91      14.460  -2.061 -10.269  1.00 16.40           O  
-ATOM    718  CB  LEU A  91      17.199  -0.190  -9.616  1.00 17.67           C  
-ATOM    719  CG  LEU A  91      17.139   0.093 -11.119  1.00 17.13           C  
-ATOM    720  CD1 LEU A  91      16.007   1.068 -11.456  1.00 17.86           C  
-ATOM    721  CD2 LEU A  91      18.471   0.641 -11.580  1.00 19.47           C  
-ATOM    722  N   GLU A  92      16.262  -3.086  -9.401  1.00 18.62           N  
-ATOM    723  CA  GLU A  92      15.959  -4.355 -10.075  1.00 19.21           C  
-ATOM    724  C   GLU A  92      14.551  -4.876  -9.767  1.00 17.87           C  
-ATOM    725  O   GLU A  92      13.839  -5.296 -10.687  1.00 16.26           O  
-ATOM    726  CB  GLU A  92      17.042  -5.409  -9.794  1.00 20.82           C  
-ATOM    727  CG  GLU A  92      18.382  -5.020 -10.430  1.00 25.60           C  
-ATOM    728  CD  GLU A  92      19.412  -6.135 -10.471  1.00 30.25           C  
-ATOM    729  OE1 GLU A  92      19.098  -7.290 -10.103  1.00 34.65           O  
-ATOM    730  OE2 GLU A  92      20.555  -5.840 -10.888  1.00 35.91           O  
-ATOM    731  N   ARG A  93      14.157  -4.845  -8.494  1.00 17.57           N  
-ATOM    732  CA  ARG A  93      12.823  -5.280  -8.069  1.00 17.88           C  
-ATOM    733  C   ARG A  93      11.715  -4.449  -8.723  1.00 15.66           C  
-ATOM    734  O   ARG A  93      10.706  -5.008  -9.125  1.00 16.69           O  
-ATOM    735  CB  ARG A  93      12.655  -5.235  -6.539  1.00 19.28           C  
-ATOM    736  CG  ARG A  93      11.263  -5.707  -6.050  1.00 24.99           C  
-ATOM    737  CD  ARG A  93      11.167  -5.948  -4.524  1.00 28.31           C  
-ATOM    738  NE  ARG A  93      11.184  -4.704  -3.760  1.00 29.67           N  
-ATOM    739  CZ  ARG A  93      11.443  -4.594  -2.451  1.00 34.19           C  
-ATOM    740  NH1 ARG A  93      11.716  -5.651  -1.696  1.00 34.16           N  
-ATOM    741  NH2 ARG A  93      11.433  -3.386  -1.885  1.00 35.62           N  
-ATOM    742  N   ASN A  94      11.913  -3.135  -8.807  1.00 15.00           N  
-ATOM    743  CA  ASN A  94      10.940  -2.234  -9.429  1.00 13.67           C  
-ATOM    744  C   ASN A  94      10.814  -2.413 -10.955  1.00 14.19           C  
-ATOM    745  O   ASN A  94       9.720  -2.250 -11.507  1.00 13.48           O  
-ATOM    746  CB  ASN A  94      11.259  -0.769  -9.125  1.00 14.48           C  
-ATOM    747  CG  ASN A  94      10.827  -0.341  -7.731  1.00 14.03           C  
-ATOM    748  OD1 ASN A  94      10.012   0.583  -7.575  1.00 13.06           O  
-ATOM    749  ND2 ASN A  94      11.374  -0.986  -6.716  1.00 12.67           N  
-ATOM    750  N   LEU A  95      11.923  -2.742 -11.627  1.00 12.84           N  
-ATOM    751  CA  LEU A  95      11.909  -2.903 -13.092  1.00 11.94           C  
-ATOM    752  C   LEU A  95      11.195  -4.179 -13.556  1.00 12.59           C  
-ATOM    753  O   LEU A  95      10.909  -4.326 -14.740  1.00 11.24           O  
-ATOM    754  CB  LEU A  95      13.322  -2.837 -13.694  1.00 11.39           C  
-ATOM    755  CG  LEU A  95      14.057  -1.495 -13.581  1.00 12.43           C  
-ATOM    756  CD1 LEU A  95      15.485  -1.674 -14.038  1.00 13.29           C  
-ATOM    757  CD2 LEU A  95      13.347  -0.363 -14.385  1.00 13.80           C  
-ATOM    758  N   TYR A  96      10.913  -5.102 -12.640  1.00 14.17           N  
-ATOM    759  CA  TYR A  96      10.133  -6.289 -12.978  1.00 14.02           C  
-ATOM    760  C   TYR A  96       8.791  -5.884 -13.587  1.00 13.89           C  
-ATOM    761  O   TYR A  96       8.426  -6.322 -14.686  1.00 13.77           O  
-ATOM    762  CB  TYR A  96       9.958  -7.164 -11.741  1.00 14.21           C  
-ATOM    763  CG  TYR A  96       9.296  -8.485 -12.010  1.00 14.97           C  
-ATOM    764  CD1 TYR A  96      10.032  -9.579 -12.467  1.00 15.88           C  
-ATOM    765  CD2 TYR A  96       7.936  -8.656 -11.792  1.00 15.72           C  
-ATOM    766  CE1 TYR A  96       9.434 -10.783 -12.714  1.00 16.09           C  
-ATOM    767  CE2 TYR A  96       7.330  -9.873 -12.033  1.00 15.85           C  
-ATOM    768  CZ  TYR A  96       8.088 -10.923 -12.493  1.00 18.92           C  
-ATOM    769  OH  TYR A  96       7.494 -12.118 -12.732  1.00 21.06           O  
-ATOM    770  N   LEU A  97       8.078  -5.012 -12.890  1.00 12.66           N  
-ATOM    771  CA  LEU A  97       6.845  -4.443 -13.418  1.00 12.10           C  
-ATOM    772  C   LEU A  97       7.102  -3.662 -14.724  1.00 12.37           C  
-ATOM    773  O   LEU A  97       6.349  -3.787 -15.676  1.00 11.38           O  
-ATOM    774  CB  LEU A  97       6.197  -3.510 -12.389  1.00 12.13           C  
-ATOM    775  CG  LEU A  97       4.894  -2.814 -12.805  1.00 14.06           C  
-ATOM    776  CD1 LEU A  97       3.748  -3.810 -13.073  1.00 14.96           C  
-ATOM    777  CD2 LEU A  97       4.488  -1.787 -11.758  1.00 12.28           C  
-ATOM    778  N   THR A  98       8.169  -2.861 -14.753  1.00 12.18           N  
-ATOM    779  CA  THR A  98       8.477  -2.022 -15.892  1.00 12.12           C  
-ATOM    780  C   THR A  98       8.506  -2.835 -17.192  1.00 14.58           C  
-ATOM    781  O   THR A  98       7.943  -2.411 -18.215  1.00 12.90           O  
-ATOM    782  CB  THR A  98       9.827  -1.312 -15.685  1.00 13.10           C  
-ATOM    783  OG1 THR A  98       9.803  -0.578 -14.450  1.00 12.08           O  
-ATOM    784  CG2 THR A  98      10.126  -0.397 -16.870  1.00 12.90           C  
-ATOM    785  N   THR A  99       9.134  -4.013 -17.149  1.00 14.11           N  
-ATOM    786  CA  THR A  99       9.229  -4.843 -18.362  1.00 13.44           C  
-ATOM    787  C   THR A  99       7.836  -5.194 -18.893  1.00 14.11           C  
-ATOM    788  O   THR A  99       7.588  -5.201 -20.100  1.00 12.64           O  
-ATOM    789  CB  THR A  99      10.083  -6.127 -18.145  1.00 13.60           C  
-ATOM    790  OG1 THR A  99       9.479  -6.981 -17.163  1.00 14.21           O  
-ATOM    791  CG2 THR A  99      11.532  -5.790 -17.740  1.00 13.34           C  
-ATOM    792  N   GLN A 100       6.917  -5.470 -17.983  1.00 13.49           N  
-ATOM    793  CA  GLN A 100       5.548  -5.788 -18.346  1.00 13.86           C  
-ATOM    794  C   GLN A 100       4.771  -4.593 -18.877  1.00 13.47           C  
-ATOM    795  O   GLN A 100       3.958  -4.740 -19.789  1.00 13.52           O  
-ATOM    796  CB  GLN A 100       4.819  -6.389 -17.148  1.00 15.22           C  
-ATOM    797  CG  GLN A 100       5.430  -7.679 -16.631  1.00 15.86           C  
-ATOM    798  CD  GLN A 100       4.794  -8.107 -15.338  1.00 18.12           C  
-ATOM    799  OE1 GLN A 100       3.579  -8.269 -15.283  1.00 21.63           O  
-ATOM    800  NE2 GLN A 100       5.596  -8.274 -14.285  1.00 21.69           N  
-ATOM    801  N   LEU A 101       5.023  -3.420 -18.298  1.00 13.06           N  
-ATOM    802  CA  LEU A 101       4.426  -2.172 -18.785  1.00 12.98           C  
-ATOM    803  C   LEU A 101       4.846  -1.871 -20.230  1.00 14.26           C  
-ATOM    804  O   LEU A 101       3.999  -1.510 -21.055  1.00 15.03           O  
-ATOM    805  CB  LEU A 101       4.769  -1.004 -17.862  1.00 12.50           C  
-ATOM    806  CG  LEU A 101       4.259  -1.113 -16.415  1.00 12.09           C  
-ATOM    807  CD1 LEU A 101       4.859   0.005 -15.545  1.00 11.90           C  
-ATOM    808  CD2 LEU A 101       2.716  -1.111 -16.323  1.00 13.51           C  
-ATOM    809  N   ILE A 102       6.136  -2.037 -20.544  1.00 13.30           N  
-ATOM    810  CA  ILE A 102       6.629  -1.797 -21.904  1.00 13.32           C  
-ATOM    811  C   ILE A 102       5.877  -2.690 -22.890  1.00 11.79           C  
-ATOM    812  O   ILE A 102       5.501  -2.260 -23.977  1.00 13.27           O  
-ATOM    813  CB  ILE A 102       8.169  -2.011 -22.005  1.00 14.59           C  
-ATOM    814  CG1 ILE A 102       8.915  -0.962 -21.157  1.00 14.28           C  
-ATOM    815  CG2 ILE A 102       8.638  -1.933 -23.472  1.00 13.24           C  
-ATOM    816  CD1 ILE A 102      10.426  -1.211 -20.946  1.00 13.14           C  
-ATOM    817  N   GLU A 103       5.653  -3.939 -22.494  1.00 12.98           N  
-ATOM    818  CA  GLU A 103       5.019  -4.939 -23.351  1.00 13.48           C  
-ATOM    819  C   GLU A 103       3.550  -4.632 -23.697  1.00 14.66           C  
-ATOM    820  O   GLU A 103       3.031  -5.159 -24.680  1.00 16.28           O  
-ATOM    821  CB  GLU A 103       5.155  -6.315 -22.706  1.00 14.65           C  
-ATOM    822  CG  GLU A 103       6.618  -6.774 -22.725  1.00 12.73           C  
-ATOM    823  CD  GLU A 103       6.939  -7.899 -21.769  1.00 15.85           C  
-ATOM    824  OE1 GLU A 103       6.067  -8.308 -20.968  1.00 14.25           O  
-ATOM    825  OE2 GLU A 103       8.089  -8.380 -21.831  1.00 16.09           O  
-ATOM    826  N   THR A 104       2.892  -3.777 -22.917  1.00 14.13           N  
-ATOM    827  CA  THR A 104       1.520  -3.353 -23.238  1.00 13.65           C  
-ATOM    828  C   THR A 104       1.432  -2.571 -24.557  1.00 14.35           C  
-ATOM    829  O   THR A 104       0.353  -2.462 -25.164  1.00 14.06           O  
-ATOM    830  CB  THR A 104       0.897  -2.471 -22.125  1.00 13.78           C  
-ATOM    831  OG1 THR A 104       1.562  -1.201 -22.092  1.00 15.66           O  
-ATOM    832  CG2 THR A 104       0.940  -3.161 -20.746  1.00 12.91           C  
-ATOM    833  N   GLY A 105       2.559  -2.008 -24.993  1.00 14.33           N  
-ATOM    834  CA  GLY A 105       2.610  -1.196 -26.186  1.00 14.80           C  
-ATOM    835  C   GLY A 105       2.226   0.263 -26.008  1.00 15.55           C  
-ATOM    836  O   GLY A 105       2.215   0.991 -26.995  1.00 17.92           O  
-ATOM    837  N  AILE A 106       1.906   0.694 -24.786  0.50 16.11           N  
-ATOM    838  N  BILE A 106       1.890   0.679 -24.783  0.50 15.41           N  
-ATOM    839  CA AILE A 106       1.697   2.113 -24.501  0.50 16.41           C  
-ATOM    840  CA BILE A 106       1.714   2.091 -24.466  0.50 15.18           C  
-ATOM    841  C  AILE A 106       3.048   2.652 -24.041  0.50 15.68           C  
-ATOM    842  C  BILE A 106       3.126   2.558 -24.118  0.50 14.91           C  
-ATOM    843  O  AILE A 106       3.563   2.185 -23.022  0.50 15.23           O  
-ATOM    844  O  BILE A 106       3.774   1.935 -23.268  0.50 13.65           O  
-ATOM    845  CB AILE A 106       0.690   2.341 -23.398  0.50 16.69           C  
-ATOM    846  CB BILE A 106       0.806   2.332 -23.261  0.50 14.83           C  
-ATOM    847  CG1AILE A 106      -0.658   1.737 -23.777  0.50 17.94           C  
-ATOM    848  CG1BILE A 106      -0.499   1.530 -23.356  0.50 14.25           C  
-ATOM    849  CG2AILE A 106       0.546   3.833 -23.138  0.50 16.52           C  
-ATOM    850  CG2BILE A 106       0.517   3.821 -23.132  0.50 14.55           C  
-ATOM    851  CD1AILE A 106      -1.686   1.914 -22.714  0.50 17.15           C  
-ATOM    852  CD1BILE A 106      -1.419   1.962 -24.497  0.50 12.36           C  
-ATOM    853  N   PRO A 107       3.633   3.615 -24.778  1.00 14.95           N  
-ATOM    854  CA  PRO A 107       5.007   4.066 -24.462  1.00 15.40           C  
-ATOM    855  C   PRO A 107       5.215   4.462 -23.012  1.00 14.00           C  
-ATOM    856  O   PRO A 107       4.397   5.204 -22.452  1.00 15.06           O  
-ATOM    857  CB  PRO A 107       5.200   5.266 -25.388  1.00 15.08           C  
-ATOM    858  CG  PRO A 107       4.401   4.878 -26.556  1.00 15.80           C  
-ATOM    859  CD  PRO A 107       3.145   4.306 -25.990  1.00 16.52           C  
-ATOM    860  N   VAL A 108       6.293   3.942 -22.437  1.00 13.57           N  
-ATOM    861  CA  VAL A 108       6.646   4.150 -21.040  1.00 14.05           C  
-ATOM    862  C   VAL A 108       7.690   5.253 -20.897  1.00 13.75           C  
-ATOM    863  O   VAL A 108       8.625   5.317 -21.697  1.00 13.30           O  
-ATOM    864  CB  VAL A 108       7.182   2.824 -20.431  1.00 13.34           C  
-ATOM    865  CG1 VAL A 108       7.827   3.046 -19.079  1.00 13.06           C  
-ATOM    866  CG2 VAL A 108       6.040   1.799 -20.363  1.00 15.14           C  
-ATOM    867  N   THR A 109       7.498   6.120 -19.892  1.00 12.59           N  
-ATOM    868  CA  THR A 109       8.477   7.109 -19.443  1.00 12.78           C  
-ATOM    869  C   THR A 109       8.687   6.810 -17.945  1.00 14.31           C  
-ATOM    870  O   THR A 109       7.714   6.618 -17.217  1.00 14.08           O  
-ATOM    871  CB  THR A 109       7.970   8.543 -19.633  1.00 13.88           C  
-ATOM    872  OG1 THR A 109       7.851   8.832 -21.034  1.00 15.26           O  
-ATOM    873  CG2 THR A 109       8.915   9.553 -18.970  1.00 14.83           C  
-ATOM    874  N   ILE A 110       9.935   6.762 -17.483  1.00 13.68           N  
-ATOM    875  CA  ILE A 110      10.221   6.402 -16.085  1.00 12.76           C  
-ATOM    876  C   ILE A 110      10.566   7.632 -15.255  1.00 12.85           C  
-ATOM    877  O   ILE A 110      11.424   8.405 -15.672  1.00 14.51           O  
-ATOM    878  CB  ILE A 110      11.376   5.380 -15.973  1.00 13.12           C  
-ATOM    879  CG1 ILE A 110      10.960   4.005 -16.518  1.00 14.73           C  
-ATOM    880  CG2 ILE A 110      11.845   5.245 -14.519  1.00 10.85           C  
-ATOM    881  CD1 ILE A 110      12.133   2.971 -16.559  1.00 15.67           C  
-ATOM    882  N   ALA A 111       9.892   7.807 -14.108  1.00 13.48           N  
-ATOM    883  CA  ALA A 111      10.309   8.754 -13.071  1.00 13.11           C  
-ATOM    884  C   ALA A 111      11.147   7.890 -12.139  1.00 14.39           C  
-ATOM    885  O   ALA A 111      10.619   7.054 -11.415  1.00 14.11           O  
-ATOM    886  CB  ALA A 111       9.117   9.382 -12.325  1.00 14.36           C  
-ATOM    887  N   LEU A 112      12.459   8.100 -12.178  1.00 12.95           N  
-ATOM    888  CA  LEU A 112      13.404   7.344 -11.385  1.00 13.17           C  
-ATOM    889  C   LEU A 112      13.454   8.109 -10.074  1.00 14.36           C  
-ATOM    890  O   LEU A 112      14.282   9.019  -9.912  1.00 13.62           O  
-ATOM    891  CB  LEU A 112      14.763   7.262 -12.093  1.00 13.17           C  
-ATOM    892  CG  LEU A 112      15.876   6.504 -11.352  1.00 12.93           C  
-ATOM    893  CD1 LEU A 112      15.500   5.036 -11.220  1.00 14.28           C  
-ATOM    894  CD2 LEU A 112      17.236   6.634 -12.027  1.00 14.82           C  
-ATOM    895  N   ASN A 113      12.551   7.717  -9.167  1.00 14.25           N  
-ATOM    896  CA  ASN A 113      12.230   8.443  -7.938  1.00 15.98           C  
-ATOM    897  C   ASN A 113      13.123   8.000  -6.763  1.00 16.71           C  
-ATOM    898  O   ASN A 113      13.845   7.007  -6.868  1.00 16.96           O  
-ATOM    899  CB  ASN A 113      10.715   8.308  -7.650  1.00 16.59           C  
-ATOM    900  CG  ASN A 113      10.200   9.317  -6.627  1.00 16.88           C  
-ATOM    901  OD1 ASN A 113      10.456  10.516  -6.736  1.00 15.99           O  
-ATOM    902  ND2 ASN A 113       9.463   8.833  -5.630  1.00 17.25           N  
-ATOM    903  N  AMET A 114      13.089   8.731  -5.649  0.50 16.56           N  
-ATOM    904  N  BMET A 114      13.077   8.778  -5.681  0.50 17.71           N  
-ATOM    905  CA AMET A 114      13.953   8.462  -4.489  0.50 16.93           C  
-ATOM    906  CA BMET A 114      13.902   8.576  -4.491  0.50 18.95           C  
-ATOM    907  C  AMET A 114      15.421   8.715  -4.799  0.50 17.71           C  
-ATOM    908  C  BMET A 114      15.390   8.701  -4.818  0.50 18.91           C  
-ATOM    909  O  AMET A 114      16.294   8.164  -4.123  0.50 17.85           O  
-ATOM    910  O  BMET A 114      16.232   8.058  -4.184  0.50 19.18           O  
-ATOM    911  CB AMET A 114      13.829   7.023  -3.992  0.50 16.61           C  
-ATOM    912  CB BMET A 114      13.572   7.245  -3.820  0.50 19.81           C  
-ATOM    913  CG AMET A 114      12.427   6.603  -3.663  0.50 17.30           C  
-ATOM    914  CG BMET A 114      12.101   7.151  -3.447  0.50 22.52           C  
-ATOM    915  SD AMET A 114      12.032   7.077  -1.974  0.50 15.64           S  
-ATOM    916  SD BMET A 114      11.583   5.611  -2.668  0.50 23.71           S  
-ATOM    917  CE AMET A 114      10.328   6.546  -1.936  0.50 16.49           C  
-ATOM    918  CE BMET A 114       9.970   6.080  -2.059  0.50 24.67           C  
-ATOM    919  N   ILE A 115      15.695   9.545  -5.806  1.00 18.63           N  
-ATOM    920  CA  ILE A 115      17.067   9.779  -6.250  1.00 20.39           C  
-ATOM    921  C   ILE A 115      17.919  10.443  -5.143  1.00 21.97           C  
-ATOM    922  O   ILE A 115      19.140  10.233  -5.066  1.00 21.59           O  
-ATOM    923  CB  ILE A 115      17.095  10.565  -7.609  1.00 19.52           C  
-ATOM    924  CG1 ILE A 115      18.324  10.166  -8.426  1.00 21.77           C  
-ATOM    925  CG2 ILE A 115      17.004  12.087  -7.403  1.00 20.88           C  
-ATOM    926  CD1 ILE A 115      18.255   8.730  -8.963  1.00 20.17           C  
-ATOM    927  N   ASP A 116      17.271  11.225  -4.283  1.00 22.83           N  
-ATOM    928  CA  ASP A 116      17.966  11.864  -3.149  1.00 24.27           C  
-ATOM    929  C   ASP A 116      18.441  10.865  -2.078  1.00 26.27           C  
-ATOM    930  O   ASP A 116      19.421  11.127  -1.386  1.00 26.80           O  
-ATOM    931  CB  ASP A 116      17.062  12.911  -2.493  1.00 23.86           C  
-ATOM    932  CG  ASP A 116      15.786  12.307  -1.936  1.00 22.71           C  
-ATOM    933  OD1 ASP A 116      14.964  11.837  -2.744  1.00 20.41           O  
-ATOM    934  OD2 ASP A 116      15.592  12.286  -0.704  1.00 21.56           O  
-ATOM    935  N   VAL A 117      17.726   9.748  -1.943  1.00 28.37           N  
-ATOM    936  CA  VAL A 117      18.024   8.676  -0.985  1.00 30.70           C  
-ATOM    937  C   VAL A 117      19.230   7.871  -1.444  1.00 33.58           C  
-ATOM    938  O   VAL A 117      20.082   7.476  -0.642  1.00 31.94           O  
-ATOM    939  CB  VAL A 117      16.825   7.699  -0.831  1.00 29.60           C  
-ATOM    940  CG1 VAL A 117      17.112   6.607   0.210  1.00 31.44           C  
-ATOM    941  CG2 VAL A 117      15.562   8.449  -0.461  1.00 28.24           C  
-ATOM    942  N   LEU A 118      19.268   7.625  -2.752  1.00 36.31           N  
-ATOM    943  CA  LEU A 118      20.348   6.925  -3.423  1.00 38.53           C  
-ATOM    944  C   LEU A 118      21.676   7.628  -3.175  1.00 41.02           C  
-ATOM    945  O   LEU A 118      22.669   6.985  -2.834  1.00 40.40           O  
-ATOM    946  CB  LEU A 118      20.051   6.867  -4.927  1.00 38.82           C  
-ATOM    947  CG  LEU A 118      20.801   5.868  -5.792  1.00 38.32           C  
-ATOM    948  CD1 LEU A 118      20.436   4.448  -5.410  1.00 37.26           C  
-ATOM    949  CD2 LEU A 118      20.472   6.153  -7.251  1.00 38.73           C  
-ATOM    950  N   ASP A 119      21.674   8.950  -3.337  1.00 44.38           N  
-ATOM    951  CA  ASP A 119      22.843   9.784  -3.060  1.00 46.27           C  
-ATOM    952  C   ASP A 119      23.367   9.563  -1.630  1.00 47.76           C  
-ATOM    953  O   ASP A 119      24.577   9.464  -1.413  1.00 47.91           O  
-ATOM    954  CB  ASP A 119      22.498  11.259  -3.300  1.00 46.53           C  
-ATOM    955  N   GLY A 120      22.444   9.468  -0.672  1.00 48.66           N  
-ATOM    956  CA  GLY A 120      22.775   9.206   0.729  1.00 49.11           C  
-ATOM    957  C   GLY A 120      23.259   7.803   1.078  1.00 49.43           C  
-ATOM    958  O   GLY A 120      23.938   7.631   2.089  1.00 49.69           O  
-ATOM    959  N   GLN A 121      22.914   6.805   0.262  1.00 49.44           N  
-ATOM    960  CA  GLN A 121      23.357   5.414   0.453  1.00 49.44           C  
-ATOM    961  C   GLN A 121      24.727   5.120  -0.178  1.00 49.51           C  
-ATOM    962  O   GLN A 121      25.203   3.981  -0.110  1.00 50.28           O  
-ATOM    963  CB  GLN A 121      22.336   4.430  -0.145  1.00 49.62           C  
-ATOM    964  CG  GLN A 121      20.958   4.410   0.528  1.00 49.55           C  
-ATOM    965  CD  GLN A 121      19.943   3.535  -0.209  1.00 49.67           C  
-ATOM    966  OE1 GLN A 121      20.100   3.238  -1.396  1.00 50.81           O  
-ATOM    967  NE2 GLN A 121      18.894   3.124   0.496  1.00 47.78           N  
-ATOM    968  N   GLY A 122      25.360   6.121  -0.789  1.00 48.93           N  
-ATOM    969  CA  GLY A 122      26.612   5.906  -1.522  1.00 48.67           C  
-ATOM    970  C   GLY A 122      26.447   5.095  -2.807  1.00 47.76           C  
-ATOM    971  O   GLY A 122      27.398   4.449  -3.262  1.00 48.57           O  
-ATOM    972  N   LYS A 123      25.245   5.130  -3.390  1.00 45.73           N  
-ATOM    973  CA  LYS A 123      24.941   4.429  -4.638  1.00 43.20           C  
-ATOM    974  C   LYS A 123      24.819   5.436  -5.783  1.00 41.36           C  
-ATOM    975  O   LYS A 123      24.630   6.637  -5.550  1.00 41.17           O  
-ATOM    976  CB  LYS A 123      23.662   3.602  -4.501  1.00 43.39           C  
-ATOM    977  CG  LYS A 123      23.748   2.450  -3.492  1.00 43.36           C  
-ATOM    978  CD  LYS A 123      22.489   1.582  -3.523  1.00 44.17           C  
-ATOM    979  N   LYS A 124      24.951   4.933  -7.013  1.00 38.99           N  
-ATOM    980  CA  LYS A 124      24.835   5.744  -8.237  1.00 36.24           C  
-ATOM    981  C   LYS A 124      24.109   4.968  -9.339  1.00 32.66           C  
-ATOM    982  O   LYS A 124      24.208   3.734  -9.407  1.00 32.74           O  
-ATOM    983  CB  LYS A 124      26.218   6.181  -8.743  1.00 36.82           C  
-ATOM    984  N   ILE A 125      23.367   5.703 -10.172  1.00 27.71           N  
-ATOM    985  CA  ILE A 125      22.713   5.167 -11.365  1.00 25.45           C  
-ATOM    986  C   ILE A 125      23.020   6.137 -12.494  1.00 24.14           C  
-ATOM    987  O   ILE A 125      22.813   7.348 -12.349  1.00 24.05           O  
-ATOM    988  CB  ILE A 125      21.168   5.033 -11.203  1.00 24.98           C  
-ATOM    989  CG1 ILE A 125      20.835   3.969 -10.161  1.00 24.89           C  
-ATOM    990  CG2 ILE A 125      20.491   4.710 -12.558  1.00 23.65           C  
-ATOM    991  CD1 ILE A 125      19.346   3.774  -9.869  1.00 25.58           C  
-ATOM    992  N   ASN A 126      23.519   5.615 -13.611  1.00 21.95           N  
-ATOM    993  CA  ASN A 126      23.807   6.457 -14.760  1.00 21.84           C  
-ATOM    994  C   ASN A 126      22.522   6.553 -15.584  1.00 19.69           C  
-ATOM    995  O   ASN A 126      22.205   5.662 -16.371  1.00 18.26           O  
-ATOM    996  CB  ASN A 126      24.993   5.920 -15.553  1.00 22.80           C  
-ATOM    997  CG  ASN A 126      25.504   6.919 -16.564  1.00 25.02           C  
-ATOM    998  OD1 ASN A 126      24.746   7.759 -17.052  1.00 26.04           O  
-ATOM    999  ND2 ASN A 126      26.796   6.845 -16.884  1.00 25.30           N  
-ATOM   1000  N   VAL A 127      21.790   7.645 -15.394  1.00 17.51           N  
-ATOM   1001  CA  VAL A 127      20.440   7.788 -15.966  1.00 16.42           C  
-ATOM   1002  C   VAL A 127      20.368   7.590 -17.483  1.00 16.88           C  
-ATOM   1003  O   VAL A 127      19.535   6.805 -17.957  1.00 14.20           O  
-ATOM   1004  CB  VAL A 127      19.797   9.131 -15.550  1.00 16.26           C  
-ATOM   1005  CG1 VAL A 127      18.481   9.359 -16.267  1.00 14.18           C  
-ATOM   1006  CG2 VAL A 127      19.569   9.127 -14.061  1.00 18.10           C  
-ATOM   1007  N   ASP A 128      21.216   8.275 -18.256  1.00 17.53           N  
-ATOM   1008  CA  ASP A 128      21.105   8.150 -19.711  1.00 18.87           C  
-ATOM   1009  C   ASP A 128      21.436   6.726 -20.192  1.00 18.64           C  
-ATOM   1010  O   ASP A 128      20.826   6.268 -21.164  1.00 17.47           O  
-ATOM   1011  CB  ASP A 128      21.892   9.225 -20.479  1.00 20.80           C  
-ATOM   1012  CG  ASP A 128      23.338   8.916 -20.564  1.00 23.55           C  
-ATOM   1013  OD1 ASP A 128      23.918   8.656 -19.489  1.00 28.23           O  
-ATOM   1014  OD2 ASP A 128      23.884   8.929 -21.678  1.00 23.50           O  
-ATOM   1015  N  ALYS A 129      22.375   6.043 -19.531  0.70 18.74           N  
-ATOM   1016  N  BLYS A 129      22.368   6.049 -19.522  0.30 18.28           N  
-ATOM   1017  CA ALYS A 129      22.676   4.644 -19.866  0.70 19.54           C  
-ATOM   1018  CA BLYS A 129      22.699   4.662 -19.845  0.30 18.42           C  
-ATOM   1019  C  ALYS A 129      21.503   3.732 -19.518  0.70 18.05           C  
-ATOM   1020  C  BLYS A 129      21.552   3.712 -19.488  0.30 17.71           C  
-ATOM   1021  O  ALYS A 129      21.189   2.822 -20.272  0.70 17.68           O  
-ATOM   1022  O  BLYS A 129      21.304   2.751 -20.212  0.30 17.59           O  
-ATOM   1023  CB ALYS A 129      23.938   4.134 -19.168  0.70 20.25           C  
-ATOM   1024  CB BLYS A 129      23.992   4.241 -19.146  0.30 18.64           C  
-ATOM   1025  CG ALYS A 129      25.231   4.683 -19.754  0.70 22.22           C  
-ATOM   1026  CG BLYS A 129      25.208   5.047 -19.596  0.30 19.00           C  
-ATOM   1027  CD ALYS A 129      26.423   3.871 -19.286  0.70 23.64           C  
-ATOM   1028  CD BLYS A 129      26.500   4.456 -19.054  0.30 19.51           C  
-ATOM   1029  CE ALYS A 129      27.706   4.382 -19.920  0.70 24.61           C  
-ATOM   1030  CE BLYS A 129      27.718   5.242 -19.520  0.30 19.64           C  
-ATOM   1031  NZ ALYS A 129      28.897   3.827 -19.230  0.70 25.27           N  
-ATOM   1032  NZ BLYS A 129      27.762   5.372 -20.999  0.30 19.42           N  
-ATOM   1033  N   LEU A 130      20.864   3.974 -18.375  1.00 17.22           N  
-ATOM   1034  CA  LEU A 130      19.669   3.196 -17.999  1.00 16.56           C  
-ATOM   1035  C   LEU A 130      18.572   3.368 -19.049  1.00 16.50           C  
-ATOM   1036  O   LEU A 130      17.956   2.383 -19.475  1.00 18.75           O  
-ATOM   1037  CB  LEU A 130      19.141   3.601 -16.619  1.00 16.70           C  
-ATOM   1038  CG  LEU A 130      17.925   2.823 -16.099  1.00 17.04           C  
-ATOM   1039  CD1 LEU A 130      18.319   1.370 -15.917  1.00 16.92           C  
-ATOM   1040  CD2 LEU A 130      17.377   3.439 -14.801  1.00 17.41           C  
-ATOM   1041  N   SER A 131      18.341   4.616 -19.459  1.00 16.03           N  
-ATOM   1042  CA  SER A 131      17.382   4.952 -20.518  1.00 15.61           C  
-ATOM   1043  C   SER A 131      17.744   4.250 -21.822  1.00 16.96           C  
-ATOM   1044  O   SER A 131      16.888   3.621 -22.462  1.00 15.51           O  
-ATOM   1045  CB  SER A 131      17.320   6.467 -20.759  1.00 16.36           C  
-ATOM   1046  OG  SER A 131      16.420   6.800 -21.816  1.00 16.90           O  
-ATOM   1047  N   TYR A 132      19.015   4.341 -22.208  1.00 16.36           N  
-ATOM   1048  CA  TYR A 132      19.459   3.748 -23.471  1.00 18.30           C  
-ATOM   1049  C   TYR A 132      19.134   2.252 -23.526  1.00 15.69           C  
-ATOM   1050  O   TYR A 132      18.566   1.755 -24.503  1.00 17.55           O  
-ATOM   1051  CB  TYR A 132      20.967   3.959 -23.694  1.00 19.02           C  
-ATOM   1052  CG  TYR A 132      21.422   3.419 -25.034  1.00 21.58           C  
-ATOM   1053  CD1 TYR A 132      21.501   4.254 -26.141  1.00 25.20           C  
-ATOM   1054  CD2 TYR A 132      21.746   2.075 -25.201  1.00 25.25           C  
-ATOM   1055  CE1 TYR A 132      21.904   3.768 -27.385  1.00 25.91           C  
-ATOM   1056  CE2 TYR A 132      22.141   1.572 -26.449  1.00 26.47           C  
-ATOM   1057  CZ  TYR A 132      22.222   2.430 -27.529  1.00 24.59           C  
-ATOM   1058  OH  TYR A 132      22.609   1.967 -28.764  1.00 26.03           O  
-ATOM   1059  N   HIS A 133      19.509   1.536 -22.475  1.00 16.72           N  
-ATOM   1060  CA  HIS A 133      19.373   0.087 -22.453  1.00 16.83           C  
-ATOM   1061  C   HIS A 133      17.962  -0.412 -22.164  1.00 17.91           C  
-ATOM   1062  O   HIS A 133      17.611  -1.509 -22.603  1.00 15.38           O  
-ATOM   1063  CB  HIS A 133      20.436  -0.507 -21.539  1.00 18.61           C  
-ATOM   1064  CG  HIS A 133      21.802  -0.401 -22.130  1.00 20.64           C  
-ATOM   1065  ND1 HIS A 133      22.742   0.510 -21.698  1.00 23.85           N  
-ATOM   1066  CD2 HIS A 133      22.365  -1.064 -23.167  1.00 18.56           C  
-ATOM   1067  CE1 HIS A 133      23.839   0.379 -22.426  1.00 21.48           C  
-ATOM   1068  NE2 HIS A 133      23.637  -0.567 -23.323  1.00 24.40           N  
-ATOM   1069  N   LEU A 134      17.150   0.375 -21.459  1.00 16.23           N  
-ATOM   1070  CA  LEU A 134      15.722   0.032 -21.294  1.00 17.83           C  
-ATOM   1071  C   LEU A 134      14.864   0.383 -22.506  1.00 18.07           C  
-ATOM   1072  O   LEU A 134      13.756  -0.139 -22.631  1.00 17.96           O  
-ATOM   1073  CB  LEU A 134      15.115   0.710 -20.060  1.00 17.29           C  
-ATOM   1074  CG  LEU A 134      15.468   0.138 -18.699  1.00 17.03           C  
-ATOM   1075  CD1 LEU A 134      14.854   1.011 -17.599  1.00 17.32           C  
-ATOM   1076  CD2 LEU A 134      15.001  -1.328 -18.556  1.00 18.14           C  
-ATOM   1077  N   GLY A 135      15.362   1.264 -23.373  1.00 16.52           N  
-ATOM   1078  CA  GLY A 135      14.629   1.728 -24.542  1.00 16.38           C  
-ATOM   1079  C   GLY A 135      13.456   2.633 -24.187  1.00 16.62           C  
-ATOM   1080  O   GLY A 135      12.478   2.691 -24.927  1.00 15.93           O  
-ATOM   1081  N   VAL A 136      13.550   3.328 -23.053  1.00 14.69           N  
-ATOM   1082  CA  VAL A 136      12.523   4.275 -22.615  1.00 14.87           C  
-ATOM   1083  C   VAL A 136      13.173   5.525 -22.042  1.00 15.08           C  
-ATOM   1084  O   VAL A 136      14.276   5.452 -21.498  1.00 14.32           O  
-ATOM   1085  CB  VAL A 136      11.591   3.709 -21.534  1.00 13.71           C  
-ATOM   1086  CG1 VAL A 136      10.842   2.482 -22.072  1.00 14.19           C  
-ATOM   1087  CG2 VAL A 136      12.339   3.408 -20.219  1.00 16.10           C  
-ATOM   1088  N   PRO A 137      12.489   6.673 -22.152  1.00 15.21           N  
-ATOM   1089  CA  PRO A 137      12.999   7.857 -21.464  1.00 14.88           C  
-ATOM   1090  C   PRO A 137      13.040   7.628 -19.955  1.00 15.59           C  
-ATOM   1091  O   PRO A 137      12.150   6.972 -19.404  1.00 15.11           O  
-ATOM   1092  CB  PRO A 137      11.968   8.948 -21.804  1.00 15.37           C  
-ATOM   1093  CG  PRO A 137      11.199   8.435 -22.972  1.00 14.79           C  
-ATOM   1094  CD  PRO A 137      11.283   6.956 -22.947  1.00 15.87           C  
-ATOM   1095  N   VAL A 138      14.072   8.160 -19.304  1.00 15.84           N  
-ATOM   1096  CA  VAL A 138      14.190   8.106 -17.852  1.00 14.08           C  
-ATOM   1097  C   VAL A 138      14.563   9.501 -17.339  1.00 14.58           C  
-ATOM   1098  O   VAL A 138      15.489  10.122 -17.866  1.00 13.78           O  
-ATOM   1099  CB  VAL A 138      15.269   7.088 -17.393  1.00 12.91           C  
-ATOM   1100  CG1 VAL A 138      15.324   7.015 -15.866  1.00 11.85           C  
-ATOM   1101  CG2 VAL A 138      15.017   5.687 -17.976  1.00 12.06           C  
-ATOM   1102  N   VAL A 139      13.854   9.973 -16.319  1.00 14.74           N  
-ATOM   1103  CA  VAL A 139      14.132  11.248 -15.656  1.00 15.42           C  
-ATOM   1104  C   VAL A 139      14.252  11.023 -14.144  1.00 15.43           C  
-ATOM   1105  O   VAL A 139      13.340  10.474 -13.522  1.00 16.02           O  
-ATOM   1106  CB  VAL A 139      13.017  12.282 -15.937  1.00 14.73           C  
-ATOM   1107  CG1 VAL A 139      13.283  13.591 -15.169  1.00 15.15           C  
-ATOM   1108  CG2 VAL A 139      12.898  12.558 -17.427  1.00 16.54           C  
-ATOM   1109  N   ALA A 140      15.374  11.441 -13.554  1.00 15.95           N  
-ATOM   1110  CA  ALA A 140      15.593  11.317 -12.124  1.00 15.14           C  
-ATOM   1111  C   ALA A 140      14.662  12.293 -11.423  1.00 15.66           C  
-ATOM   1112  O   ALA A 140      14.593  13.467 -11.802  1.00 14.41           O  
-ATOM   1113  CB  ALA A 140      17.038  11.612 -11.750  1.00 15.46           C  
-ATOM   1114  N   THR A 141      13.934  11.801 -10.423  1.00 15.35           N  
-ATOM   1115  CA  THR A 141      13.052  12.644  -9.634  1.00 14.15           C  
-ATOM   1116  C   THR A 141      13.235  12.411  -8.132  1.00 15.33           C  
-ATOM   1117  O   THR A 141      13.730  11.367  -7.694  1.00 15.38           O  
-ATOM   1118  CB  THR A 141      11.538  12.413  -9.961  1.00 14.17           C  
-ATOM   1119  OG1 THR A 141      11.147  11.092  -9.573  1.00 13.75           O  
-ATOM   1120  CG2 THR A 141      11.245  12.608 -11.432  1.00 15.21           C  
-ATOM   1121  N   SER A 142      12.818  13.416  -7.367  1.00 17.34           N  
-ATOM   1122  CA  SER A 142      12.683  13.318  -5.915  1.00 18.23           C  
-ATOM   1123  C   SER A 142      11.376  13.998  -5.533  1.00 18.56           C  
-ATOM   1124  O   SER A 142      11.235  15.211  -5.705  1.00 17.67           O  
-ATOM   1125  CB  SER A 142      13.851  13.985  -5.183  1.00 19.02           C  
-ATOM   1126  OG  SER A 142      13.674  13.864  -3.782  1.00 19.74           O  
-ATOM   1127  N   ALA A 143      10.422  13.206  -5.044  1.00 18.08           N  
-ATOM   1128  CA  ALA A 143       9.162  13.742  -4.533  1.00 20.50           C  
-ATOM   1129  C   ALA A 143       9.415  14.566  -3.260  1.00 21.35           C  
-ATOM   1130  O   ALA A 143       8.738  15.567  -3.028  1.00 23.64           O  
-ATOM   1131  CB  ALA A 143       8.154  12.611  -4.284  1.00 18.98           C  
-ATOM   1132  N   LEU A 144      10.397  14.171  -2.450  1.00 22.80           N  
-ATOM   1133  CA  LEU A 144      10.731  14.904  -1.215  1.00 24.58           C  
-ATOM   1134  C   LEU A 144      11.325  16.282  -1.529  1.00 25.35           C  
-ATOM   1135  O   LEU A 144      10.785  17.326  -1.115  1.00 25.96           O  
-ATOM   1136  CB  LEU A 144      11.693  14.090  -0.335  1.00 25.22           C  
-ATOM   1137  CG  LEU A 144      12.204  14.777   0.948  1.00 26.65           C  
-ATOM   1138  CD1 LEU A 144      11.043  15.184   1.840  1.00 25.22           C  
-ATOM   1139  CD2 LEU A 144      13.159  13.861   1.686  1.00 25.92           C  
-ATOM   1140  N   LYS A 145      12.417  16.280  -2.286  1.00 24.71           N  
-ATOM   1141  CA  LYS A 145      13.117  17.507  -2.663  1.00 24.20           C  
-ATOM   1142  C   LYS A 145      12.389  18.310  -3.736  1.00 23.70           C  
-ATOM   1143  O   LYS A 145      12.764  19.447  -4.003  1.00 23.07           O  
-ATOM   1144  CB  LYS A 145      14.543  17.204  -3.139  1.00 25.76           C  
-ATOM   1145  CG  LYS A 145      15.394  16.373  -2.174  1.00 28.38           C  
-ATOM   1146  CD  LYS A 145      15.616  17.060  -0.827  1.00 33.20           C  
-ATOM   1147  CE  LYS A 145      16.244  16.112   0.189  1.00 34.42           C  
-ATOM   1148  NZ  LYS A 145      16.212  16.698   1.571  1.00 35.71           N  
-ATOM   1149  N   GLN A 146      11.373  17.715  -4.357  1.00 23.48           N  
-ATOM   1150  CA  GLN A 146      10.572  18.346  -5.404  1.00 24.37           C  
-ATOM   1151  C   GLN A 146      11.435  18.735  -6.615  1.00 23.69           C  
-ATOM   1152  O   GLN A 146      11.459  19.899  -7.032  1.00 24.36           O  
-ATOM   1153  CB  GLN A 146       9.759  19.524  -4.833  1.00 25.29           C  
-ATOM   1154  CG  GLN A 146       8.940  19.125  -3.594  1.00 26.65           C  
-ATOM   1155  CD  GLN A 146       7.969  20.192  -3.095  1.00 29.78           C  
-ATOM   1156  OE1 GLN A 146       7.710  21.186  -3.768  1.00 32.64           O  
-ATOM   1157  NE2 GLN A 146       7.420  19.973  -1.905  1.00 31.76           N  
-ATOM   1158  N   THR A 147      12.141  17.743  -7.162  1.00 20.81           N  
-ATOM   1159  CA  THR A 147      13.010  17.905  -8.330  1.00 20.48           C  
-ATOM   1160  C   THR A 147      12.655  16.907  -9.434  1.00 19.96           C  
-ATOM   1161  O   THR A 147      12.269  15.764  -9.150  1.00 18.44           O  
-ATOM   1162  CB  THR A 147      14.502  17.726  -7.973  1.00 21.03           C  
-ATOM   1163  OG1 THR A 147      14.734  16.436  -7.392  1.00 20.58           O  
-ATOM   1164  CG2 THR A 147      14.970  18.816  -7.001  1.00 22.27           C  
-ATOM   1165  N   GLY A 148      12.772  17.348 -10.683  1.00 19.07           N  
-ATOM   1166  CA  GLY A 148      12.541  16.479 -11.853  1.00 20.15           C  
-ATOM   1167  C   GLY A 148      11.089  16.222 -12.226  1.00 19.71           C  
-ATOM   1168  O   GLY A 148      10.804  15.583 -13.245  1.00 17.65           O  
-ATOM   1169  N   VAL A 149      10.165  16.737 -11.419  1.00 20.95           N  
-ATOM   1170  CA  VAL A 149       8.748  16.403 -11.558  1.00 21.42           C  
-ATOM   1171  C   VAL A 149       8.161  16.985 -12.845  1.00 21.84           C  
-ATOM   1172  O   VAL A 149       7.573  16.246 -13.647  1.00 22.72           O  
-ATOM   1173  CB  VAL A 149       7.941  16.834 -10.300  1.00 22.70           C  
-ATOM   1174  CG1 VAL A 149       6.468  16.505 -10.451  1.00 23.89           C  
-ATOM   1175  CG2 VAL A 149       8.484  16.152  -9.062  1.00 22.54           C  
-ATOM   1176  N   ASP A 150       8.330  18.290 -13.066  1.00 21.40           N  
-ATOM   1177  CA  ASP A 150       7.784  18.923 -14.270  1.00 21.73           C  
-ATOM   1178  C   ASP A 150       8.434  18.355 -15.535  1.00 19.68           C  
-ATOM   1179  O   ASP A 150       7.782  18.204 -16.581  1.00 19.38           O  
-ATOM   1180  CB  ASP A 150       7.979  20.447 -14.246  1.00 22.85           C  
-ATOM   1181  CG  ASP A 150       7.287  21.127 -13.069  1.00 25.64           C  
-ATOM   1182  OD1 ASP A 150       6.309  20.583 -12.508  1.00 24.71           O  
-ATOM   1183  OD2 ASP A 150       7.742  22.231 -12.697  1.00 28.95           O  
-ATOM   1184  N   GLN A 151       9.719  18.044 -15.414  1.00 18.87           N  
-ATOM   1185  CA  GLN A 151      10.521  17.449 -16.483  1.00 18.89           C  
-ATOM   1186  C   GLN A 151      10.006  16.069 -16.907  1.00 16.65           C  
-ATOM   1187  O   GLN A 151       9.868  15.803 -18.112  1.00 16.95           O  
-ATOM   1188  CB  GLN A 151      11.986  17.346 -16.073  1.00 20.14           C  
-ATOM   1189  CG  GLN A 151      12.675  18.703 -15.823  1.00 23.97           C  
-ATOM   1190  CD  GLN A 151      12.664  19.142 -14.368  1.00 26.46           C  
-ATOM   1191  OE1 GLN A 151      11.664  18.997 -13.653  1.00 25.27           O  
-ATOM   1192  NE2 GLN A 151      13.790  19.695 -13.921  1.00 29.57           N  
-ATOM   1193  N   VAL A 152       9.706  15.204 -15.939  1.00 15.75           N  
-ATOM   1194  CA  VAL A 152       9.219  13.853 -16.270  1.00 14.10           C  
-ATOM   1195  C   VAL A 152       7.806  13.940 -16.858  1.00 15.58           C  
-ATOM   1196  O   VAL A 152       7.498  13.223 -17.829  1.00 14.24           O  
-ATOM   1197  CB  VAL A 152       9.327  12.840 -15.087  1.00 14.47           C  
-ATOM   1198  CG1 VAL A 152       8.226  13.043 -14.026  1.00 14.12           C  
-ATOM   1199  CG2 VAL A 152       9.321  11.392 -15.621  1.00 15.37           C  
-ATOM   1200  N   VAL A 153       6.962  14.818 -16.309  1.00 16.39           N  
-ATOM   1201  CA  VAL A 153       5.602  14.989 -16.842  1.00 17.15           C  
-ATOM   1202  C   VAL A 153       5.653  15.463 -18.303  1.00 18.75           C  
-ATOM   1203  O   VAL A 153       4.908  14.943 -19.153  1.00 18.29           O  
-ATOM   1204  CB  VAL A 153       4.730  15.916 -15.947  1.00 18.32           C  
-ATOM   1205  CG1 VAL A 153       3.415  16.312 -16.655  1.00 19.99           C  
-ATOM   1206  CG2 VAL A 153       4.429  15.234 -14.626  1.00 16.31           C  
-ATOM   1207  N   LYS A 154       6.539  16.414 -18.609  1.00 19.41           N  
-ATOM   1208  CA  LYS A 154       6.730  16.894 -19.986  1.00 20.70           C  
-ATOM   1209  C   LYS A 154       7.166  15.793 -20.958  1.00 20.00           C  
-ATOM   1210  O   LYS A 154       6.662  15.688 -22.094  1.00 19.16           O  
-ATOM   1211  CB  LYS A 154       7.768  18.026 -20.023  1.00 21.96           C  
-ATOM   1212  CG  LYS A 154       7.924  18.699 -21.402  1.00 27.36           C  
-ATOM   1213  CD  LYS A 154       8.860  19.904 -21.343  1.00 29.27           C  
-ATOM   1214  CE  LYS A 154       9.061  20.516 -22.724  1.00 32.33           C  
-ATOM   1215  NZ  LYS A 154      10.060  21.627 -22.685  1.00 34.88           N  
-ATOM   1216  N   LYS A 155       8.119  14.985 -20.511  1.00 18.69           N  
-ATOM   1217  CA  LYS A 155       8.615  13.870 -21.296  1.00 18.01           C  
-ATOM   1218  C   LYS A 155       7.505  12.865 -21.573  1.00 16.90           C  
-ATOM   1219  O   LYS A 155       7.296  12.470 -22.735  1.00 15.11           O  
-ATOM   1220  CB  LYS A 155       9.789  13.203 -20.578  1.00 20.02           C  
-ATOM   1221  CG  LYS A 155      10.486  12.066 -21.315  1.00 21.71           C  
-ATOM   1222  CD  LYS A 155      10.970  12.447 -22.709  1.00 26.40           C  
-ATOM   1223  CE  LYS A 155      12.039  13.523 -22.661  1.00 27.06           C  
-ATOM   1224  NZ  LYS A 155      12.654  13.709 -24.010  1.00 28.80           N  
-ATOM   1225  N   ALA A 156       6.786  12.470 -20.519  1.00 17.18           N  
-ATOM   1226  CA  ALA A 156       5.676  11.531 -20.654  1.00 17.05           C  
-ATOM   1227  C   ALA A 156       4.637  12.084 -21.619  1.00 18.75           C  
-ATOM   1228  O   ALA A 156       4.149  11.351 -22.489  1.00 18.18           O  
-ATOM   1229  CB  ALA A 156       5.041  11.208 -19.293  1.00 18.37           C  
-ATOM   1230  N   ALA A 157       4.318  13.374 -21.480  1.00 17.09           N  
-ATOM   1231  CA  ALA A 157       3.334  14.025 -22.362  1.00 17.92           C  
-ATOM   1232  C   ALA A 157       3.706  14.005 -23.848  1.00 18.96           C  
-ATOM   1233  O   ALA A 157       2.793  14.029 -24.687  1.00 17.59           O  
-ATOM   1234  CB  ALA A 157       3.039  15.464 -21.899  1.00 16.41           C  
-ATOM   1235  N   HIS A 158       5.009  13.944 -24.162  1.00 20.38           N  
-ATOM   1236  CA  HIS A 158       5.518  13.900 -25.545  1.00 23.03           C  
-ATOM   1237  C   HIS A 158       6.012  12.523 -25.993  1.00 21.12           C  
-ATOM   1238  O   HIS A 158       6.642  12.407 -27.041  1.00 21.58           O  
-ATOM   1239  CB  HIS A 158       6.627  14.947 -25.722  1.00 25.29           C  
-ATOM   1240  CG  HIS A 158       6.108  16.348 -25.676  1.00 30.22           C  
-ATOM   1241  ND1 HIS A 158       6.047  17.079 -24.510  1.00 33.00           N  
-ATOM   1242  CD2 HIS A 158       5.594  17.142 -26.647  1.00 32.38           C  
-ATOM   1243  CE1 HIS A 158       5.531  18.269 -24.764  1.00 34.71           C  
-ATOM   1244  NE2 HIS A 158       5.243  18.332 -26.052  1.00 35.53           N  
-ATOM   1245  N   THR A 159       5.704  11.498 -25.200  1.00 19.13           N  
-ATOM   1246  CA  THR A 159       6.072  10.110 -25.450  1.00 18.06           C  
-ATOM   1247  C   THR A 159       4.783   9.280 -25.385  1.00 17.52           C  
-ATOM   1248  O   THR A 159       4.471   8.637 -24.372  1.00 16.52           O  
-ATOM   1249  CB  THR A 159       7.106   9.624 -24.425  1.00 17.12           C  
-ATOM   1250  OG1 THR A 159       8.209  10.537 -24.380  1.00 16.13           O  
-ATOM   1251  CG2 THR A 159       7.613   8.213 -24.785  1.00 17.04           C  
-ATOM   1252  N   THR A 160       4.033   9.312 -26.482  1.00 16.91           N  
-ATOM   1253  CA  THR A 160       2.694   8.739 -26.527  1.00 16.98           C  
-ATOM   1254  C   THR A 160       2.481   7.740 -27.656  1.00 16.45           C  
-ATOM   1255  O   THR A 160       3.333   7.579 -28.532  1.00 17.25           O  
-ATOM   1256  CB  THR A 160       1.633   9.854 -26.679  1.00 16.80           C  
-ATOM   1257  OG1 THR A 160       1.684  10.366 -28.021  1.00 17.85           O  
-ATOM   1258  CG2 THR A 160       1.852  10.977 -25.657  1.00 18.66           C  
-ATOM   1259  N   THR A 161       1.326   7.073 -27.617  1.00 17.86           N  
-ATOM   1260  CA  THR A 161       0.908   6.153 -28.675  1.00 19.30           C  
-ATOM   1261  C   THR A 161       0.832   6.881 -30.042  1.00 21.37           C  
-ATOM   1262  O   THR A 161       0.955   6.246 -31.090  1.00 22.53           O  
-ATOM   1263  CB  THR A 161      -0.450   5.490 -28.345  1.00 19.86           C  
-ATOM   1264  OG1 THR A 161      -1.441   6.505 -28.146  1.00 21.85           O  
-ATOM   1265  CG2 THR A 161      -0.363   4.624 -27.079  1.00 18.98           C  
-ATOM   1266  N   SER A 162       0.635   8.202 -30.029  1.00 21.41           N  
-ATOM   1267  CA  SER A 162       0.613   8.997 -31.266  1.00 22.79           C  
-ATOM   1268  C   SER A 162       2.017   9.374 -31.733  1.00 23.26           C  
-ATOM   1269  O   SER A 162       2.302   9.292 -32.929  1.00 25.65           O  
-ATOM   1270  CB  SER A 162      -0.257  10.251 -31.103  1.00 22.31           C  
-ATOM   1271  OG  SER A 162      -1.554   9.896 -30.668  1.00 22.35           O  
-ATOM   1272  N   THR A 163       2.894   9.764 -30.808  1.00 23.14           N  
-ATOM   1273  CA  THR A 163       4.226  10.275 -31.156  1.00 23.16           C  
-ATOM   1274  C   THR A 163       5.315   9.214 -31.378  1.00 23.92           C  
-ATOM   1275  O   THR A 163       6.259   9.445 -32.130  1.00 24.61           O  
-ATOM   1276  CB  THR A 163       4.724  11.297 -30.101  1.00 24.12           C  
-ATOM   1277  OG1 THR A 163       5.000  10.642 -28.853  1.00 23.57           O  
-ATOM   1278  CG2 THR A 163       3.682  12.389 -29.880  1.00 22.45           C  
-ATOM   1279  N   VAL A 164       5.190   8.055 -30.741  1.00 22.65           N  
-ATOM   1280  CA  VAL A 164       6.197   7.001 -30.829  1.00 22.22           C  
-ATOM   1281  C   VAL A 164       5.832   5.996 -31.923  1.00 24.00           C  
-ATOM   1282  O   VAL A 164       4.662   5.603 -32.049  1.00 24.07           O  
-ATOM   1283  CB  VAL A 164       6.357   6.301 -29.439  1.00 22.33           C  
-ATOM   1284  CG1 VAL A 164       7.309   5.086 -29.487  1.00 21.75           C  
-ATOM   1285  CG2 VAL A 164       6.840   7.300 -28.426  1.00 21.65           C  
-ATOM   1286  N   GLY A 165       6.838   5.589 -32.696  1.00 25.03           N  
-ATOM   1287  CA  GLY A 165       6.689   4.599 -33.760  1.00 26.18           C  
-ATOM   1288  C   GLY A 165       6.835   3.179 -33.246  1.00 27.24           C  
-ATOM   1289  O   GLY A 165       6.047   2.739 -32.399  1.00 27.56           O  
-ATOM   1290  N   ASP A 166       7.846   2.462 -33.735  1.00 28.42           N  
-ATOM   1291  CA  ASP A 166       8.039   1.048 -33.385  1.00 29.38           C  
-ATOM   1292  C   ASP A 166       8.242   0.819 -31.880  1.00 28.59           C  
-ATOM   1293  O   ASP A 166       8.826   1.654 -31.202  1.00 28.46           O  
-ATOM   1294  CB  ASP A 166       9.242   0.446 -34.139  1.00 31.20           C  
-ATOM   1295  CG  ASP A 166       8.988   0.264 -35.637  1.00 34.08           C  
-ATOM   1296  OD1 ASP A 166       7.855   0.488 -36.120  1.00 32.25           O  
-ATOM   1297  OD2 ASP A 166       9.953  -0.120 -36.336  1.00 38.04           O  
-ATOM   1298  N   LEU A 167       7.753  -0.319 -31.387  1.00 27.69           N  
-ATOM   1299  CA  LEU A 167       7.946  -0.716 -29.989  1.00 27.58           C  
-ATOM   1300  C   LEU A 167       9.379  -1.217 -29.780  1.00 24.59           C  
-ATOM   1301  O   LEU A 167       9.823  -2.098 -30.502  1.00 24.80           O  
-ATOM   1302  CB  LEU A 167       6.941  -1.819 -29.600  1.00 27.82           C  
-ATOM   1303  CG  LEU A 167       6.975  -2.387 -28.168  1.00 28.40           C  
-ATOM   1304  CD1 LEU A 167       6.750  -1.271 -27.152  1.00 25.92           C  
-ATOM   1305  CD2 LEU A 167       5.967  -3.561 -27.948  1.00 25.96           C  
-ATOM   1306  N   ALA A 168      10.102  -0.654 -28.813  1.00 22.58           N  
-ATOM   1307  CA  ALA A 168      11.393  -1.220 -28.388  1.00 22.33           C  
-ATOM   1308  C   ALA A 168      11.122  -2.042 -27.136  1.00 20.87           C  
-ATOM   1309  O   ALA A 168      11.113  -1.513 -26.024  1.00 21.22           O  
-ATOM   1310  CB  ALA A 168      12.420  -0.140 -28.122  1.00 23.49           C  
-ATOM   1311  N   PHE A 169      10.890  -3.341 -27.313  1.00 19.17           N  
-ATOM   1312  CA  PHE A 169      10.529  -4.216 -26.197  1.00 18.75           C  
-ATOM   1313  C   PHE A 169      11.751  -4.963 -25.658  1.00 18.07           C  
-ATOM   1314  O   PHE A 169      12.682  -5.242 -26.426  1.00 15.45           O  
-ATOM   1315  CB  PHE A 169       9.454  -5.221 -26.627  1.00 21.74           C  
-ATOM   1316  CG  PHE A 169       9.825  -6.037 -27.843  1.00 25.57           C  
-ATOM   1317  CD1 PHE A 169      10.659  -7.148 -27.735  1.00 27.41           C  
-ATOM   1318  CD2 PHE A 169       9.331  -5.691 -29.105  1.00 27.80           C  
-ATOM   1319  CE1 PHE A 169      10.998  -7.899 -28.853  1.00 28.03           C  
-ATOM   1320  CE2 PHE A 169       9.671  -6.440 -30.230  1.00 29.37           C  
-ATOM   1321  CZ  PHE A 169      10.504  -7.541 -30.105  1.00 28.61           C  
-ATOM   1322  N   PRO A 170      11.755  -5.296 -24.353  1.00 16.59           N  
-ATOM   1323  CA  PRO A 170      12.830  -6.146 -23.816  1.00 16.54           C  
-ATOM   1324  C   PRO A 170      12.977  -7.440 -24.616  1.00 16.02           C  
-ATOM   1325  O   PRO A 170      12.011  -8.171 -24.790  1.00 16.26           O  
-ATOM   1326  CB  PRO A 170      12.362  -6.460 -22.386  1.00 16.24           C  
-ATOM   1327  CG  PRO A 170      11.530  -5.280 -22.022  1.00 16.50           C  
-ATOM   1328  CD  PRO A 170      10.834  -4.859 -23.287  1.00 16.04           C  
-ATOM   1329  N   ILE A 171      14.180  -7.698 -25.116  1.00 16.56           N  
-ATOM   1330  CA  ILE A 171      14.449  -8.896 -25.903  1.00 16.69           C  
-ATOM   1331  C   ILE A 171      15.006  -9.941 -24.950  1.00 15.15           C  
-ATOM   1332  O   ILE A 171      15.996  -9.686 -24.258  1.00 14.18           O  
-ATOM   1333  CB  ILE A 171      15.436  -8.613 -27.070  1.00 18.81           C  
-ATOM   1334  CG1 ILE A 171      14.832  -7.618 -28.054  1.00 20.32           C  
-ATOM   1335  CG2 ILE A 171      15.813  -9.915 -27.806  1.00 18.82           C  
-ATOM   1336  CD1 ILE A 171      15.826  -7.127 -29.120  1.00 22.21           C  
-ATOM   1337  N   TYR A 172      14.362 -11.105 -24.905  1.00 13.67           N  
-ATOM   1338  CA  TYR A 172      14.742 -12.201 -24.015  1.00 13.90           C  
-ATOM   1339  C   TYR A 172      15.570 -13.246 -24.766  1.00 14.50           C  
-ATOM   1340  O   TYR A 172      15.912 -13.047 -25.935  1.00 15.18           O  
-ATOM   1341  CB  TYR A 172      13.483 -12.832 -23.409  1.00 13.50           C  
-ATOM   1342  CG  TYR A 172      12.634 -11.823 -22.683  1.00 10.67           C  
-ATOM   1343  CD1 TYR A 172      13.190 -11.022 -21.670  1.00 13.81           C  
-ATOM   1344  CD2 TYR A 172      11.304 -11.649 -22.986  1.00 13.14           C  
-ATOM   1345  CE1 TYR A 172      12.426 -10.073 -20.987  1.00 13.57           C  
-ATOM   1346  CE2 TYR A 172      10.530 -10.694 -22.314  1.00 12.32           C  
-ATOM   1347  CZ  TYR A 172      11.100  -9.918 -21.310  1.00 13.53           C  
-ATOM   1348  OH  TYR A 172      10.362  -8.982 -20.632  1.00 14.81           O  
-ATOM   1349  N   ASP A 173      15.897 -14.347 -24.096  1.00 14.31           N  
-ATOM   1350  CA  ASP A 173      16.668 -15.426 -24.714  1.00 16.31           C  
-ATOM   1351  C   ASP A 173      16.069 -15.859 -26.049  1.00 15.82           C  
-ATOM   1352  O   ASP A 173      14.836 -15.909 -26.192  1.00 14.82           O  
-ATOM   1353  CB  ASP A 173      16.727 -16.656 -23.809  1.00 17.62           C  
-ATOM   1354  CG  ASP A 173      17.646 -17.719 -24.377  1.00 21.76           C  
-ATOM   1355  OD1 ASP A 173      17.147 -18.713 -24.933  1.00 24.50           O  
-ATOM   1356  OD2 ASP A 173      18.869 -17.504 -24.315  1.00 27.98           O  
-ATOM   1357  N   ASP A 174      16.928 -16.164 -27.025  1.00 15.81           N  
-ATOM   1358  CA  ASP A 174      16.458 -16.696 -28.330  1.00 17.28           C  
-ATOM   1359  C   ASP A 174      15.396 -17.781 -28.251  1.00 16.61           C  
-ATOM   1360  O   ASP A 174      14.496 -17.825 -29.103  1.00 17.37           O  
-ATOM   1361  CB  ASP A 174      17.621 -17.273 -29.151  1.00 19.16           C  
-ATOM   1362  CG  ASP A 174      18.523 -16.209 -29.722  1.00 21.56           C  
-ATOM   1363  OD1 ASP A 174      18.129 -15.025 -29.762  1.00 22.34           O  
-ATOM   1364  OD2 ASP A 174      19.637 -16.566 -30.146  1.00 22.68           O  
-ATOM   1365  N   ARG A 175      15.500 -18.656 -27.258  1.00 15.93           N  
-ATOM   1366  CA  ARG A 175      14.542 -19.767 -27.108  1.00 17.36           C  
-ATOM   1367  C   ARG A 175      13.163 -19.284 -26.670  1.00 16.57           C  
-ATOM   1368  O   ARG A 175      12.150 -19.846 -27.096  1.00 17.55           O  
-ATOM   1369  CB  ARG A 175      15.039 -20.806 -26.117  1.00 20.09           C  
-ATOM   1370  CG  ARG A 175      16.267 -21.597 -26.559  1.00 22.75           C  
-ATOM   1371  CD  ARG A 175      16.831 -22.346 -25.365  1.00 24.74           C  
-ATOM   1372  NE  ARG A 175      17.422 -21.437 -24.387  1.00 24.90           N  
-ATOM   1373  CZ  ARG A 175      17.864 -21.787 -23.181  1.00 27.82           C  
-ATOM   1374  NH1 ARG A 175      17.818 -23.054 -22.769  1.00 29.51           N  
-ATOM   1375  NH2 ARG A 175      18.377 -20.866 -22.379  1.00 27.56           N  
-ATOM   1376  N   LEU A 176      13.121 -18.255 -25.827  1.00 14.17           N  
-ATOM   1377  CA  LEU A 176      11.831 -17.676 -25.461  1.00 13.93           C  
-ATOM   1378  C   LEU A 176      11.275 -16.846 -26.607  1.00 13.64           C  
-ATOM   1379  O   LEU A 176      10.079 -16.893 -26.858  1.00 13.98           O  
-ATOM   1380  CB  LEU A 176      11.904 -16.847 -24.170  1.00 13.23           C  
-ATOM   1381  CG  LEU A 176      10.569 -16.236 -23.715  1.00 11.42           C  
-ATOM   1382  CD1 LEU A 176       9.460 -17.302 -23.606  1.00 13.73           C  
-ATOM   1383  CD2 LEU A 176      10.746 -15.516 -22.391  1.00 12.14           C  
-ATOM   1384  N   GLU A 177      12.134 -16.087 -27.291  1.00 14.21           N  
-ATOM   1385  CA  GLU A 177      11.717 -15.299 -28.469  1.00 14.55           C  
-ATOM   1386  C   GLU A 177      11.116 -16.169 -29.578  1.00 16.03           C  
-ATOM   1387  O   GLU A 177      10.140 -15.765 -30.215  1.00 14.50           O  
-ATOM   1388  CB  GLU A 177      12.868 -14.445 -29.005  1.00 15.38           C  
-ATOM   1389  CG  GLU A 177      13.316 -13.330 -28.048  1.00 14.82           C  
-ATOM   1390  CD  GLU A 177      12.232 -12.324 -27.765  1.00 16.74           C  
-ATOM   1391  OE1 GLU A 177      11.372 -12.093 -28.645  1.00 16.20           O  
-ATOM   1392  OE2 GLU A 177      12.221 -11.757 -26.650  1.00 14.32           O  
-ATOM   1393  N   ALA A 178      11.669 -17.368 -29.781  1.00 15.85           N  
-ATOM   1394  CA  ALA A 178      11.118 -18.327 -30.742  1.00 17.13           C  
-ATOM   1395  C   ALA A 178       9.689 -18.709 -30.353  1.00 16.92           C  
-ATOM   1396  O   ALA A 178       8.784 -18.723 -31.201  1.00 15.58           O  
-ATOM   1397  CB  ALA A 178      12.016 -19.593 -30.831  1.00 18.65           C  
-ATOM   1398  N   ALA A 179       9.483 -18.996 -29.069  1.00 13.85           N  
-ATOM   1399  CA  ALA A 179       8.146 -19.312 -28.562  1.00 13.98           C  
-ATOM   1400  C   ALA A 179       7.165 -18.147 -28.735  1.00 13.24           C  
-ATOM   1401  O   ALA A 179       6.028 -18.340 -29.154  1.00 14.54           O  
-ATOM   1402  CB  ALA A 179       8.212 -19.726 -27.081  1.00 11.77           C  
-ATOM   1403  N   ILE A 180       7.599 -16.938 -28.391  1.00 13.73           N  
-ATOM   1404  CA  ILE A 180       6.744 -15.748 -28.530  1.00 12.05           C  
-ATOM   1405  C   ILE A 180       6.364 -15.517 -30.010  1.00 14.35           C  
-ATOM   1406  O   ILE A 180       5.185 -15.265 -30.328  1.00 14.65           O  
-ATOM   1407  CB  ILE A 180       7.422 -14.506 -27.940  1.00 11.58           C  
-ATOM   1408  CG1 ILE A 180       7.586 -14.659 -26.419  1.00 12.39           C  
-ATOM   1409  CG2 ILE A 180       6.627 -13.224 -28.283  1.00 12.22           C  
-ATOM   1410  CD1 ILE A 180       8.549 -13.639 -25.829  1.00 10.60           C  
-ATOM   1411  N  ASER A 181       7.357 -15.591 -30.893  0.70 16.21           N  
-ATOM   1412  N  BSER A 181       7.354 -15.615 -30.898  0.30 14.42           N  
-ATOM   1413  CA ASER A 181       7.122 -15.482 -32.341  0.70 17.40           C  
-ATOM   1414  CA BSER A 181       7.135 -15.484 -32.343  0.30 14.36           C  
-ATOM   1415  C  ASER A 181       6.084 -16.475 -32.878  0.70 17.01           C  
-ATOM   1416  C  BSER A 181       6.097 -16.474 -32.886  0.30 15.12           C  
-ATOM   1417  O  ASER A 181       5.241 -16.106 -33.691  0.70 17.34           O  
-ATOM   1418  O  BSER A 181       5.256 -16.097 -33.700  0.30 15.32           O  
-ATOM   1419  CB ASER A 181       8.429 -15.649 -33.119  0.70 18.49           C  
-ATOM   1420  CB BSER A 181       8.449 -15.668 -33.107  0.30 14.25           C  
-ATOM   1421  OG ASER A 181       9.193 -14.463 -33.029  0.70 21.87           O  
-ATOM   1422  OG BSER A 181       8.284 -15.360 -34.484  0.30 11.74           O  
-ATOM   1423  N   GLN A 182       6.170 -17.729 -32.446  1.00 15.29           N  
-ATOM   1424  CA  GLN A 182       5.218 -18.774 -32.883  1.00 15.37           C  
-ATOM   1425  C   GLN A 182       3.824 -18.565 -32.298  1.00 14.39           C  
-ATOM   1426  O   GLN A 182       2.821 -18.810 -32.976  1.00 14.38           O  
-ATOM   1427  CB  GLN A 182       5.772 -20.165 -32.592  1.00 15.70           C  
-ATOM   1428  CG  GLN A 182       6.953 -20.462 -33.505  1.00 18.43           C  
-ATOM   1429  CD  GLN A 182       7.747 -21.662 -33.065  1.00 20.37           C  
-ATOM   1430  OE1 GLN A 182       7.200 -22.586 -32.498  1.00 26.15           O  
-ATOM   1431  NE2 GLN A 182       9.045 -21.649 -33.338  1.00 20.88           N  
-ATOM   1432  N   ILE A 183       3.749 -18.085 -31.056  1.00 12.80           N  
-ATOM   1433  CA  ILE A 183       2.455 -17.750 -30.458  1.00 13.64           C  
-ATOM   1434  C   ILE A 183       1.831 -16.558 -31.206  1.00 15.35           C  
-ATOM   1435  O   ILE A 183       0.625 -16.564 -31.484  1.00 15.16           O  
-ATOM   1436  CB  ILE A 183       2.550 -17.506 -28.933  1.00 12.65           C  
-ATOM   1437  CG1 ILE A 183       2.856 -18.825 -28.223  1.00 13.75           C  
-ATOM   1438  CG2 ILE A 183       1.243 -16.921 -28.400  1.00  9.82           C  
-ATOM   1439  CD1 ILE A 183       3.267 -18.650 -26.767  1.00 11.57           C  
-ATOM   1440  N   LEU A 184       2.645 -15.562 -31.549  1.00 16.66           N  
-ATOM   1441  CA  LEU A 184       2.180 -14.441 -32.382  1.00 17.38           C  
-ATOM   1442  C   LEU A 184       1.622 -14.924 -33.725  1.00 18.70           C  
-ATOM   1443  O   LEU A 184       0.574 -14.441 -34.149  1.00 17.15           O  
-ATOM   1444  CB  LEU A 184       3.285 -13.405 -32.600  1.00 16.03           C  
-ATOM   1445  CG  LEU A 184       3.631 -12.532 -31.397  1.00 15.77           C  
-ATOM   1446  CD1 LEU A 184       4.937 -11.753 -31.659  1.00 18.14           C  
-ATOM   1447  CD2 LEU A 184       2.461 -11.580 -31.047  1.00 15.97           C  
-ATOM   1448  N   GLU A 185       2.307 -15.867 -34.377  1.00 19.26           N  
-ATOM   1449  CA  GLU A 185       1.811 -16.460 -35.635  1.00 22.66           C  
-ATOM   1450  C   GLU A 185       0.463 -17.137 -35.416  1.00 22.08           C  
-ATOM   1451  O   GLU A 185      -0.455 -16.943 -36.201  1.00 23.15           O  
-ATOM   1452  CB  GLU A 185       2.769 -17.520 -36.198  1.00 24.19           C  
-ATOM   1453  CG  GLU A 185       4.118 -17.021 -36.668  1.00 29.45           C  
-ATOM   1454  CD  GLU A 185       5.186 -18.134 -36.745  1.00 34.93           C  
-ATOM   1455  OE1 GLU A 185       4.839 -19.341 -36.818  1.00 39.77           O  
-ATOM   1456  OE2 GLU A 185       6.391 -17.802 -36.730  1.00 39.04           O  
-ATOM   1457  N   VAL A 186       0.342 -17.919 -34.346  1.00 20.17           N  
-ATOM   1458  CA  VAL A 186      -0.903 -18.597 -34.036  1.00 19.42           C  
-ATOM   1459  C   VAL A 186      -2.031 -17.599 -33.725  1.00 19.00           C  
-ATOM   1460  O   VAL A 186      -3.180 -17.819 -34.106  1.00 18.48           O  
-ATOM   1461  CB  VAL A 186      -0.756 -19.564 -32.855  1.00 20.13           C  
-ATOM   1462  N   LEU A 187      -1.692 -16.510 -33.038  1.00 17.41           N  
-ATOM   1463  CA  LEU A 187      -2.676 -15.483 -32.686  1.00 16.70           C  
-ATOM   1464  C   LEU A 187      -3.279 -14.766 -33.893  1.00 16.04           C  
-ATOM   1465  O   LEU A 187      -4.475 -14.440 -33.891  1.00 14.30           O  
-ATOM   1466  CB  LEU A 187      -2.059 -14.454 -31.732  1.00 16.33           C  
-ATOM   1467  CG  LEU A 187      -2.032 -14.907 -30.272  1.00 17.32           C  
-ATOM   1468  CD1 LEU A 187      -1.133 -13.986 -29.465  1.00 15.46           C  
-ATOM   1469  CD2 LEU A 187      -3.436 -14.920 -29.678  1.00 18.73           C  
-ATOM   1470  N   GLY A 188      -2.467 -14.523 -34.923  1.00 16.39           N  
-ATOM   1471  CA  GLY A 188      -2.953 -13.792 -36.103  1.00 16.52           C  
-ATOM   1472  C   GLY A 188      -3.507 -12.443 -35.667  1.00 16.45           C  
-ATOM   1473  O   GLY A 188      -2.821 -11.709 -34.945  1.00 16.22           O  
-ATOM   1474  N   ASN A 189      -4.742 -12.129 -36.075  1.00 15.60           N  
-ATOM   1475  CA  ASN A 189      -5.398 -10.857 -35.733  1.00 15.59           C  
-ATOM   1476  C   ASN A 189      -6.382 -10.956 -34.558  1.00 16.55           C  
-ATOM   1477  O   ASN A 189      -7.264 -10.105 -34.406  1.00 16.94           O  
-ATOM   1478  CB  ASN A 189      -6.085 -10.250 -36.968  1.00 14.99           C  
-ATOM   1479  CG  ASN A 189      -7.314 -11.027 -37.421  1.00 14.28           C  
-ATOM   1480  OD1 ASN A 189      -7.609 -12.118 -36.924  1.00 14.63           O  
-ATOM   1481  ND2 ASN A 189      -8.035 -10.464 -38.396  1.00 14.13           N  
-ATOM   1482  N   SER A 190      -6.222 -11.991 -33.731  1.00 16.83           N  
-ATOM   1483  CA  SER A 190      -7.083 -12.206 -32.566  1.00 17.40           C  
-ATOM   1484  C   SER A 190      -6.897 -11.162 -31.487  1.00 17.90           C  
-ATOM   1485  O   SER A 190      -7.781 -10.979 -30.653  1.00 18.46           O  
-ATOM   1486  CB  SER A 190      -6.852 -13.595 -31.957  1.00 17.22           C  
-ATOM   1487  OG  SER A 190      -7.367 -14.589 -32.819  1.00 19.22           O  
-ATOM   1488  N   VAL A 191      -5.752 -10.489 -31.507  1.00 18.03           N  
-ATOM   1489  CA  VAL A 191      -5.443  -9.398 -30.592  1.00 18.19           C  
-ATOM   1490  C   VAL A 191      -4.889  -8.223 -31.370  1.00 17.20           C  
-ATOM   1491  O   VAL A 191      -4.453  -8.396 -32.497  1.00 17.83           O  
-ATOM   1492  CB  VAL A 191      -4.424  -9.845 -29.530  1.00 17.59           C  
-ATOM   1493  CG1 VAL A 191      -5.015 -10.998 -28.698  1.00 20.24           C  
-ATOM   1494  CG2 VAL A 191      -3.109 -10.267 -30.155  1.00 17.71           C  
-ATOM   1495  N   PRO A 192      -4.897  -7.013 -30.784  1.00 18.25           N  
-ATOM   1496  CA  PRO A 192      -4.281  -5.880 -31.475  1.00 16.41           C  
-ATOM   1497  C   PRO A 192      -2.771  -6.053 -31.653  1.00 16.43           C  
-ATOM   1498  O   PRO A 192      -2.102  -6.627 -30.780  1.00 15.77           O  
-ATOM   1499  CB  PRO A 192      -4.571  -4.687 -30.553  1.00 17.47           C  
-ATOM   1500  CG  PRO A 192      -5.695  -5.143 -29.653  1.00 17.81           C  
-ATOM   1501  CD  PRO A 192      -5.498  -6.619 -29.500  1.00 18.40           C  
-ATOM   1502  N   GLN A 193      -2.246  -5.567 -32.778  1.00 15.50           N  
-ATOM   1503  CA  GLN A 193      -0.800  -5.578 -33.018  1.00 15.82           C  
-ATOM   1504  C   GLN A 193      -0.021  -4.895 -31.885  1.00 15.49           C  
-ATOM   1505  O   GLN A 193       1.015  -5.404 -31.466  1.00 16.16           O  
-ATOM   1506  CB  GLN A 193      -0.442  -4.965 -34.380  1.00 16.92           C  
-ATOM   1507  CG  GLN A 193      -0.756  -5.902 -35.568  1.00 15.46           C  
-ATOM   1508  CD  GLN A 193       0.260  -7.016 -35.706  1.00 18.24           C  
-ATOM   1509  OE1 GLN A 193       0.039  -8.172 -35.274  1.00 17.90           O  
-ATOM   1510  NE2 GLN A 193       1.395  -6.676 -36.293  1.00 15.48           N  
-ATOM   1511  N   ARG A 194      -0.520  -3.770 -31.372  1.00 15.16           N  
-ATOM   1512  CA  ARG A 194       0.217  -2.996 -30.365  1.00 15.41           C  
-ATOM   1513  C   ARG A 194       0.535  -3.785 -29.093  1.00 15.44           C  
-ATOM   1514  O   ARG A 194       1.628  -3.659 -28.536  1.00 16.12           O  
-ATOM   1515  CB  ARG A 194      -0.557  -1.727 -29.991  1.00 16.15           C  
-ATOM   1516  CG  ARG A 194       0.083  -0.875 -28.887  1.00 16.62           C  
-ATOM   1517  CD  ARG A 194      -0.688   0.441 -28.695  1.00 16.78           C  
-ATOM   1518  NE  ARG A 194      -0.648   1.278 -29.898  1.00 18.11           N  
-ATOM   1519  CZ  ARG A 194       0.365   2.051 -30.290  1.00 20.98           C  
-ATOM   1520  NH1 ARG A 194       1.498   2.145 -29.591  1.00 20.09           N  
-ATOM   1521  NH2 ARG A 194       0.239   2.749 -31.421  1.00 21.24           N  
-ATOM   1522  N   SER A 195      -0.438  -4.573 -28.642  1.00 16.31           N  
-ATOM   1523  CA  SER A 195      -0.359  -5.318 -27.398  1.00 16.92           C  
-ATOM   1524  C   SER A 195      -0.139  -6.807 -27.636  1.00 17.67           C  
-ATOM   1525  O   SER A 195      -0.183  -7.599 -26.682  1.00 17.20           O  
-ATOM   1526  CB  SER A 195      -1.637  -5.085 -26.574  1.00 18.63           C  
-ATOM   1527  OG  SER A 195      -2.814  -5.324 -27.334  1.00 15.13           O  
-ATOM   1528  N   ALA A 196       0.119  -7.193 -28.889  1.00 16.90           N  
-ATOM   1529  CA  ALA A 196       0.210  -8.612 -29.257  1.00 17.11           C  
-ATOM   1530  C   ALA A 196       1.245  -9.341 -28.417  1.00 15.51           C  
-ATOM   1531  O   ALA A 196       0.995 -10.458 -27.975  1.00 15.99           O  
-ATOM   1532  CB  ALA A 196       0.510  -8.801 -30.740  1.00 17.51           C  
-ATOM   1533  N   ARG A 197       2.387  -8.702 -28.183  1.00 14.99           N  
-ATOM   1534  CA  ARG A 197       3.461  -9.308 -27.391  1.00 16.09           C  
-ATOM   1535  C   ARG A 197       3.047  -9.553 -25.932  1.00 15.11           C  
-ATOM   1536  O   ARG A 197       3.394 -10.596 -25.365  1.00 13.67           O  
-ATOM   1537  CB  ARG A 197       4.727  -8.457 -27.473  1.00 16.85           C  
-ATOM   1538  CG  ARG A 197       5.939  -9.122 -26.892  1.00 18.63           C  
-ATOM   1539  CD  ARG A 197       7.192  -8.321 -27.213  1.00 18.44           C  
-ATOM   1540  NE  ARG A 197       8.315  -8.869 -26.476  1.00 15.57           N  
-ATOM   1541  CZ  ARG A 197       9.085  -9.885 -26.860  1.00 15.26           C  
-ATOM   1542  NH1 ARG A 197       8.908 -10.519 -28.018  1.00 17.60           N  
-ATOM   1543  NH2 ARG A 197      10.068 -10.282 -26.059  1.00 15.83           N  
-ATOM   1544  N   PHE A 198       2.307  -8.606 -25.345  1.00 14.33           N  
-ATOM   1545  CA  PHE A 198       1.766  -8.768 -23.996  1.00 15.62           C  
-ATOM   1546  C   PHE A 198       0.913 -10.029 -23.926  1.00 14.44           C  
-ATOM   1547  O   PHE A 198       1.053 -10.837 -23.011  1.00 14.15           O  
-ATOM   1548  CB  PHE A 198       0.902  -7.567 -23.577  1.00 17.69           C  
-ATOM   1549  CG  PHE A 198       0.279  -7.733 -22.230  1.00 17.85           C  
-ATOM   1550  CD1 PHE A 198       0.931  -7.276 -21.100  1.00 18.39           C  
-ATOM   1551  CD2 PHE A 198      -0.961  -8.343 -22.085  1.00 20.28           C  
-ATOM   1552  CE1 PHE A 198       0.372  -7.441 -19.849  1.00 19.66           C  
-ATOM   1553  CE2 PHE A 198      -1.518  -8.501 -20.822  1.00 19.77           C  
-ATOM   1554  CZ  PHE A 198      -0.847  -8.047 -19.718  1.00 18.50           C  
-ATOM   1555  N   TYR A 199       0.013 -10.174 -24.895  1.00 13.95           N  
-ATOM   1556  CA  TYR A 199      -0.872 -11.331 -24.932  1.00 13.29           C  
-ATOM   1557  C   TYR A 199      -0.103 -12.619 -25.213  1.00 12.79           C  
-ATOM   1558  O   TYR A 199      -0.397 -13.646 -24.610  1.00 12.74           O  
-ATOM   1559  CB  TYR A 199      -1.967 -11.140 -25.974  1.00 14.79           C  
-ATOM   1560  CG  TYR A 199      -3.022 -10.166 -25.548  1.00 13.59           C  
-ATOM   1561  CD1 TYR A 199      -3.929 -10.499 -24.543  1.00 17.58           C  
-ATOM   1562  CD2 TYR A 199      -3.136  -8.926 -26.146  1.00 14.48           C  
-ATOM   1563  CE1 TYR A 199      -4.908  -9.609 -24.141  1.00 17.12           C  
-ATOM   1564  CE2 TYR A 199      -4.113  -8.036 -25.752  1.00 16.00           C  
-ATOM   1565  CZ  TYR A 199      -4.997  -8.386 -24.755  1.00 18.23           C  
-ATOM   1566  OH  TYR A 199      -5.964  -7.494 -24.354  1.00 19.45           O  
-ATOM   1567  N   ALA A 200       0.875 -12.567 -26.115  1.00 12.88           N  
-ATOM   1568  CA  ALA A 200       1.651 -13.760 -26.442  1.00 12.91           C  
-ATOM   1569  C   ALA A 200       2.403 -14.287 -25.204  1.00 12.60           C  
-ATOM   1570  O   ALA A 200       2.424 -15.488 -24.945  1.00 13.00           O  
-ATOM   1571  CB  ALA A 200       2.609 -13.493 -27.597  1.00 11.33           C  
-ATOM   1572  N   ILE A 201       3.013 -13.388 -24.442  1.00 13.63           N  
-ATOM   1573  CA  ILE A 201       3.756 -13.772 -23.242  1.00 14.18           C  
-ATOM   1574  C   ILE A 201       2.805 -14.314 -22.180  1.00 14.25           C  
-ATOM   1575  O   ILE A 201       3.109 -15.316 -21.530  1.00 15.40           O  
-ATOM   1576  CB  ILE A 201       4.596 -12.610 -22.677  1.00 13.99           C  
-ATOM   1577  CG1 ILE A 201       5.721 -12.272 -23.646  1.00 16.94           C  
-ATOM   1578  CG2 ILE A 201       5.214 -13.005 -21.307  1.00 15.97           C  
-ATOM   1579  CD1 ILE A 201       6.397 -10.964 -23.379  1.00 15.46           C  
-ATOM   1580  N   LYS A 202       1.664 -13.651 -21.997  1.00 14.34           N  
-ATOM   1581  CA  LYS A 202       0.645 -14.139 -21.062  1.00 14.58           C  
-ATOM   1582  C   LYS A 202       0.132 -15.531 -21.408  1.00 14.25           C  
-ATOM   1583  O   LYS A 202      -0.074 -16.358 -20.527  1.00 12.97           O  
-ATOM   1584  CB  LYS A 202      -0.525 -13.161 -20.988  1.00 16.74           C  
-ATOM   1585  CG  LYS A 202      -0.185 -11.897 -20.230  1.00 17.67           C  
-ATOM   1586  CD  LYS A 202      -0.352 -12.093 -18.750  1.00 21.31           C  
-ATOM   1587  CE  LYS A 202       0.330 -11.012 -17.931  1.00 21.45           C  
-ATOM   1588  NZ  LYS A 202       1.810 -11.151 -17.993  1.00 22.67           N  
-ATOM   1589  N   LEU A 203      -0.080 -15.789 -22.693  1.00 14.07           N  
-ATOM   1590  CA  LEU A 203      -0.509 -17.108 -23.128  1.00 14.56           C  
-ATOM   1591  C   LEU A 203       0.559 -18.156 -22.860  1.00 13.84           C  
-ATOM   1592  O   LEU A 203       0.241 -19.277 -22.431  1.00 13.72           O  
-ATOM   1593  CB  LEU A 203      -0.866 -17.103 -24.613  1.00 14.45           C  
-ATOM   1594  CG  LEU A 203      -2.212 -16.418 -24.878  1.00 13.72           C  
-ATOM   1595  CD1 LEU A 203      -2.341 -16.076 -26.351  1.00 12.43           C  
-ATOM   1596  CD2 LEU A 203      -3.361 -17.294 -24.388  1.00 13.91           C  
-ATOM   1597  N   PHE A 204       1.813 -17.781 -23.105  1.00 12.05           N  
-ATOM   1598  CA  PHE A 204       2.925 -18.690 -22.883  1.00 11.77           C  
-ATOM   1599  C   PHE A 204       2.972 -19.128 -21.417  1.00 13.43           C  
-ATOM   1600  O   PHE A 204       3.142 -20.320 -21.120  1.00 16.13           O  
-ATOM   1601  CB  PHE A 204       4.261 -18.064 -23.283  1.00 12.28           C  
-ATOM   1602  CG  PHE A 204       5.440 -18.969 -23.032  1.00 11.94           C  
-ATOM   1603  CD1 PHE A 204       5.788 -19.952 -23.954  1.00 12.59           C  
-ATOM   1604  CD2 PHE A 204       6.194 -18.853 -21.870  1.00 12.87           C  
-ATOM   1605  CE1 PHE A 204       6.881 -20.800 -23.719  1.00 14.86           C  
-ATOM   1606  CE2 PHE A 204       7.288 -19.700 -21.622  1.00 15.30           C  
-ATOM   1607  CZ  PHE A 204       7.636 -20.671 -22.543  1.00 15.48           C  
-ATOM   1608  N   GLU A 205       2.792 -18.169 -20.514  1.00 14.14           N  
-ATOM   1609  CA  GLU A 205       2.828 -18.452 -19.074  1.00 16.37           C  
-ATOM   1610  C   GLU A 205       1.482 -18.943 -18.491  1.00 16.08           C  
-ATOM   1611  O   GLU A 205       1.325 -19.057 -17.265  1.00 16.88           O  
-ATOM   1612  CB  GLU A 205       3.362 -17.231 -18.321  1.00 18.23           C  
-ATOM   1613  CG  GLU A 205       2.383 -16.100 -18.222  1.00 19.93           C  
-ATOM   1614  CD  GLU A 205       3.000 -14.759 -17.841  1.00 23.14           C  
-ATOM   1615  OE1 GLU A 205       2.204 -13.809 -17.721  1.00 23.98           O  
-ATOM   1616  OE2 GLU A 205       4.228 -14.646 -17.650  1.00 19.70           O  
-ATOM   1617  N   GLN A 206       0.532 -19.235 -19.372  1.00 16.20           N  
-ATOM   1618  CA  GLN A 206      -0.799 -19.753 -19.036  1.00 17.35           C  
-ATOM   1619  C   GLN A 206      -1.589 -18.886 -18.062  1.00 16.09           C  
-ATOM   1620  O   GLN A 206      -2.226 -19.380 -17.130  1.00 14.52           O  
-ATOM   1621  CB  GLN A 206      -0.685 -21.182 -18.547  1.00 19.06           C  
-ATOM   1622  CG  GLN A 206      -0.225 -22.085 -19.671  1.00 21.91           C  
-ATOM   1623  CD  GLN A 206       0.636 -23.172 -19.173  1.00 26.74           C  
-ATOM   1624  OE1 GLN A 206       0.188 -24.299 -19.010  1.00 28.88           O  
-ATOM   1625  NE2 GLN A 206       1.897 -22.847 -18.915  1.00 32.25           N  
-ATOM   1626  N   ASP A 207      -1.544 -17.585 -18.319  1.00 15.34           N  
-ATOM   1627  CA  ASP A 207      -2.334 -16.623 -17.590  1.00 15.21           C  
-ATOM   1628  C   ASP A 207      -3.823 -16.937 -17.728  1.00 14.81           C  
-ATOM   1629  O   ASP A 207      -4.375 -16.920 -18.824  1.00 14.48           O  
-ATOM   1630  CB  ASP A 207      -2.050 -15.221 -18.113  1.00 15.04           C  
-ATOM   1631  CG  ASP A 207      -2.714 -14.162 -17.276  1.00 15.66           C  
-ATOM   1632  OD1 ASP A 207      -2.094 -13.720 -16.284  1.00 17.60           O  
-ATOM   1633  OD2 ASP A 207      -3.856 -13.777 -17.615  1.00 15.56           O  
-ATOM   1634  N   SER A 208      -4.468 -17.223 -16.611  1.00 16.63           N  
-ATOM   1635  CA  SER A 208      -5.858 -17.673 -16.620  1.00 17.18           C  
-ATOM   1636  C   SER A 208      -6.845 -16.601 -17.098  1.00 17.46           C  
-ATOM   1637  O   SER A 208      -7.860 -16.940 -17.682  1.00 17.40           O  
-ATOM   1638  CB  SER A 208      -6.240 -18.220 -15.236  1.00 17.68           C  
-ATOM   1639  OG  SER A 208      -6.018 -17.249 -14.247  1.00 19.03           O  
-ATOM   1640  N   LEU A 209      -6.549 -15.323 -16.864  1.00 17.21           N  
-ATOM   1641  CA  LEU A 209      -7.419 -14.232 -17.330  1.00 16.66           C  
-ATOM   1642  C   LEU A 209      -7.412 -14.074 -18.845  1.00 16.31           C  
-ATOM   1643  O   LEU A 209      -8.465 -13.925 -19.462  1.00 16.81           O  
-ATOM   1644  CB  LEU A 209      -7.038 -12.897 -16.687  1.00 17.59           C  
-ATOM   1645  CG  LEU A 209      -7.395 -12.656 -15.223  1.00 20.22           C  
-ATOM   1646  CD1 LEU A 209      -6.707 -11.384 -14.737  1.00 21.56           C  
-ATOM   1647  CD2 LEU A 209      -8.907 -12.565 -15.054  1.00 19.13           C  
-ATOM   1648  N   VAL A 210      -6.221 -14.100 -19.443  1.00 15.93           N  
-ATOM   1649  CA  VAL A 210      -6.097 -13.991 -20.901  1.00 15.24           C  
-ATOM   1650  C   VAL A 210      -6.737 -15.212 -21.553  1.00 15.07           C  
-ATOM   1651  O   VAL A 210      -7.464 -15.075 -22.545  1.00 15.41           O  
-ATOM   1652  CB  VAL A 210      -4.636 -13.766 -21.349  1.00 15.23           C  
-ATOM   1653  CG1 VAL A 210      -4.463 -14.004 -22.841  1.00 17.23           C  
-ATOM   1654  CG2 VAL A 210      -4.174 -12.341 -20.968  1.00 14.79           C  
-ATOM   1655  N   GLU A 211      -6.505 -16.396 -20.988  1.00 16.52           N  
-ATOM   1656  CA  GLU A 211      -7.084 -17.631 -21.557  1.00 18.08           C  
-ATOM   1657  C   GLU A 211      -8.611 -17.618 -21.551  1.00 18.95           C  
-ATOM   1658  O   GLU A 211      -9.252 -18.048 -22.508  1.00 19.41           O  
-ATOM   1659  CB  GLU A 211      -6.585 -18.853 -20.794  1.00 17.90           C  
-ATOM   1660  CG  GLU A 211      -5.127 -19.127 -21.053  1.00 16.05           C  
-ATOM   1661  CD  GLU A 211      -4.543 -20.202 -20.187  1.00 14.27           C  
-ATOM   1662  OE1 GLU A 211      -5.161 -20.593 -19.179  1.00 16.64           O  
-ATOM   1663  OE2 GLU A 211      -3.435 -20.665 -20.507  1.00 16.29           O  
-ATOM   1664  N   ALA A 212      -9.184 -17.122 -20.463  1.00 18.43           N  
-ATOM   1665  CA  ALA A 212     -10.635 -17.004 -20.347  1.00 18.58           C  
-ATOM   1666  C   ALA A 212     -11.206 -15.913 -21.252  1.00 20.05           C  
-ATOM   1667  O   ALA A 212     -12.317 -16.056 -21.731  1.00 24.08           O  
-ATOM   1668  CB  ALA A 212     -11.017 -16.747 -18.892  1.00 18.27           C  
-ATOM   1669  N   GLU A 213     -10.473 -14.827 -21.498  1.00 19.95           N  
-ATOM   1670  CA  GLU A 213     -11.030 -13.701 -22.243  1.00 21.94           C  
-ATOM   1671  C   GLU A 213     -10.911 -13.806 -23.766  1.00 21.20           C  
-ATOM   1672  O   GLU A 213     -11.775 -13.299 -24.467  1.00 20.40           O  
-ATOM   1673  CB  GLU A 213     -10.422 -12.355 -21.788  1.00 23.79           C  
-ATOM   1674  CG  GLU A 213      -9.136 -11.964 -22.482  1.00 27.79           C  
-ATOM   1675  CD  GLU A 213      -8.523 -10.655 -21.982  1.00 30.19           C  
-ATOM   1676  OE1 GLU A 213      -7.323 -10.642 -21.684  1.00 30.48           O  
-ATOM   1677  OE2 GLU A 213      -9.238  -9.649 -21.885  1.00 34.62           O  
-ATOM   1678  N  ALEU A 214      -9.847 -14.440 -24.259  0.50 21.84           N  
-ATOM   1679  N  BLEU A 214      -9.850 -14.435 -24.267  0.50 20.74           N  
-ATOM   1680  CA ALEU A 214      -9.598 -14.551 -25.697  0.50 22.68           C  
-ATOM   1681  CA BLEU A 214      -9.608 -14.502 -25.708  0.50 20.78           C  
-ATOM   1682  C  ALEU A 214     -10.454 -15.636 -26.340  0.50 23.36           C  
-ATOM   1683  C  BLEU A 214     -10.415 -15.628 -26.356  0.50 22.25           C  
-ATOM   1684  O  ALEU A 214     -10.620 -16.717 -25.784  0.50 23.60           O  
-ATOM   1685  O  BLEU A 214     -10.505 -16.728 -25.820  0.50 22.42           O  
-ATOM   1686  CB ALEU A 214      -8.123 -14.853 -25.978  0.50 23.46           C  
-ATOM   1687  CB BLEU A 214      -8.115 -14.675 -26.005  0.50 20.29           C  
-ATOM   1688  CG ALEU A 214      -7.151 -13.682 -26.109  0.50 23.75           C  
-ATOM   1689  CG BLEU A 214      -7.185 -13.497 -25.704  0.50 18.58           C  
-ATOM   1690  CD1ALEU A 214      -7.086 -12.893 -24.831  0.50 24.75           C  
-ATOM   1691  CD1BLEU A 214      -5.751 -13.837 -26.119  0.50 16.21           C  
-ATOM   1692  CD2ALEU A 214      -5.765 -14.177 -26.489  0.50 21.92           C  
-ATOM   1693  CD2BLEU A 214      -7.660 -12.218 -26.400  0.50 16.08           C  
-ATOM   1694  N   ASP A 215     -10.988 -15.336 -27.518  1.00 24.34           N  
-ATOM   1695  CA  ASP A 215     -11.808 -16.280 -28.266  1.00 26.79           C  
-ATOM   1696  C   ASP A 215     -10.850 -16.958 -29.221  1.00 27.03           C  
-ATOM   1697  O   ASP A 215     -10.708 -16.526 -30.376  1.00 28.50           O  
-ATOM   1698  CB  ASP A 215     -12.919 -15.538 -29.014  1.00 28.42           C  
-ATOM   1699  CG  ASP A 215     -13.761 -16.456 -29.897  1.00 31.10           C  
-ATOM   1700  OD1 ASP A 215     -14.065 -17.591 -29.490  1.00 33.52           O  
-ATOM   1701  OD2 ASP A 215     -14.129 -16.023 -31.006  1.00 36.66           O  
-ATOM   1702  N   LEU A 216     -10.180 -17.997 -28.721  1.00 25.22           N  
-ATOM   1703  CA  LEU A 216      -9.230 -18.784 -29.516  1.00 23.95           C  
-ATOM   1704  C   LEU A 216      -9.867 -20.065 -30.020  1.00 22.61           C  
-ATOM   1705  O   LEU A 216     -10.592 -20.737 -29.287  1.00 23.23           O  
-ATOM   1706  CB  LEU A 216      -7.968 -19.151 -28.720  1.00 22.29           C  
-ATOM   1707  CG  LEU A 216      -7.153 -17.959 -28.204  1.00 22.69           C  
-ATOM   1708  CD1 LEU A 216      -5.904 -18.426 -27.444  1.00 25.65           C  
-ATOM   1709  CD2 LEU A 216      -6.786 -16.989 -29.335  1.00 22.03           C  
-ATOM   1710  N   SER A 217      -9.573 -20.398 -31.270  1.00 22.06           N  
-ATOM   1711  CA  SER A 217     -10.046 -21.646 -31.856  1.00 21.35           C  
-ATOM   1712  C   SER A 217      -9.345 -22.828 -31.207  1.00 21.36           C  
-ATOM   1713  O   SER A 217      -8.276 -22.681 -30.568  1.00 20.08           O  
-ATOM   1714  CB  SER A 217      -9.786 -21.668 -33.359  1.00 21.79           C  
-ATOM   1715  OG  SER A 217      -8.397 -21.798 -33.635  1.00 19.75           O  
-ATOM   1716  N   GLN A 218      -9.940 -24.006 -31.380  1.00 19.88           N  
-ATOM   1717  CA  GLN A 218      -9.317 -25.242 -30.919  1.00 19.84           C  
-ATOM   1718  C   GLN A 218      -7.930 -25.373 -31.547  1.00 17.82           C  
-ATOM   1719  O   GLN A 218      -6.985 -25.755 -30.869  1.00 19.27           O  
-ATOM   1720  CB  GLN A 218     -10.175 -26.472 -31.263  1.00 21.05           C  
-ATOM   1721  CG  GLN A 218      -9.508 -27.798 -30.890  1.00 23.94           C  
-ATOM   1722  CD  GLN A 218     -10.373 -29.013 -31.147  1.00 25.34           C  
-ATOM   1723  OE1 GLN A 218     -11.441 -28.921 -31.749  1.00 25.71           O  
-ATOM   1724  NE2 GLN A 218      -9.908 -30.160 -30.692  1.00 24.43           N  
-ATOM   1725  N   PHE A 219      -7.801 -25.059 -32.834  1.00 16.41           N  
-ATOM   1726  CA  PHE A 219      -6.500 -25.197 -33.498  1.00 17.36           C  
-ATOM   1727  C   PHE A 219      -5.461 -24.238 -32.885  1.00 17.78           C  
-ATOM   1728  O   PHE A 219      -4.319 -24.624 -32.640  1.00 16.94           O  
-ATOM   1729  CB  PHE A 219      -6.621 -25.012 -35.018  1.00 17.46           C  
-ATOM   1730  CG  PHE A 219      -5.292 -25.031 -35.717  1.00 18.77           C  
-ATOM   1731  CD1 PHE A 219      -4.507 -26.177 -35.672  1.00 19.88           C  
-ATOM   1732  CD2 PHE A 219      -4.822 -23.914 -36.389  1.00 20.14           C  
-ATOM   1733  CE1 PHE A 219      -3.268 -26.218 -36.290  1.00 19.19           C  
-ATOM   1734  CE2 PHE A 219      -3.581 -23.944 -37.018  1.00 22.27           C  
-ATOM   1735  CZ  PHE A 219      -2.807 -25.113 -36.962  1.00 19.03           C  
-ATOM   1736  N   GLN A 220      -5.867 -22.990 -32.633  1.00 17.69           N  
-ATOM   1737  CA  GLN A 220      -4.988 -22.002 -31.998  1.00 16.85           C  
-ATOM   1738  C   GLN A 220      -4.487 -22.515 -30.651  1.00 16.85           C  
-ATOM   1739  O   GLN A 220      -3.294 -22.446 -30.360  1.00 16.34           O  
-ATOM   1740  CB  GLN A 220      -5.696 -20.646 -31.828  1.00 16.89           C  
-ATOM   1741  CG  GLN A 220      -5.723 -19.796 -33.083  1.00 16.18           C  
-ATOM   1742  CD  GLN A 220      -6.569 -18.538 -32.934  1.00 18.71           C  
-ATOM   1743  OE1 GLN A 220      -7.734 -18.616 -32.543  1.00 19.20           O  
-ATOM   1744  NE2 GLN A 220      -5.993 -17.381 -33.261  1.00 18.40           N  
-ATOM   1745  N   ARG A 221      -5.400 -23.048 -29.848  1.00 17.22           N  
-ATOM   1746  CA  ARG A 221      -5.064 -23.576 -28.525  1.00 19.65           C  
-ATOM   1747  C   ARG A 221      -4.096 -24.759 -28.615  1.00 18.72           C  
-ATOM   1748  O   ARG A 221      -3.165 -24.858 -27.814  1.00 16.51           O  
-ATOM   1749  CB  ARG A 221      -6.326 -23.954 -27.750  1.00 19.43           C  
-ATOM   1750  CG  ARG A 221      -7.199 -22.745 -27.409  1.00 22.94           C  
-ATOM   1751  CD  ARG A 221      -8.613 -23.123 -26.975  1.00 25.55           C  
-ATOM   1752  NE  ARG A 221      -8.680 -23.500 -25.566  1.00 29.37           N  
-ATOM   1753  CZ  ARG A 221      -9.764 -23.964 -24.937  1.00 32.19           C  
-ATOM   1754  NH1 ARG A 221     -10.916 -24.137 -25.586  1.00 33.10           N  
-ATOM   1755  NH2 ARG A 221      -9.698 -24.265 -23.635  1.00 31.68           N  
-ATOM   1756  N   LYS A 222      -4.299 -25.636 -29.599  1.00 18.27           N  
-ATOM   1757  CA  LYS A 222      -3.385 -26.766 -29.816  1.00 18.31           C  
-ATOM   1758  C   LYS A 222      -1.980 -26.289 -30.195  1.00 18.63           C  
-ATOM   1759  O   LYS A 222      -0.988 -26.803 -29.658  1.00 18.05           O  
-ATOM   1760  CB  LYS A 222      -3.913 -27.704 -30.901  1.00 19.37           C  
-ATOM   1761  CG  LYS A 222      -5.089 -28.533 -30.454  1.00 20.89           C  
-ATOM   1762  CD  LYS A 222      -5.695 -29.366 -31.580  1.00 22.92           C  
-ATOM   1763  CE  LYS A 222      -4.827 -30.538 -31.964  1.00 24.57           C  
-ATOM   1764  NZ  LYS A 222      -5.618 -31.587 -32.686  1.00 23.53           N  
-ATOM   1765  N   GLU A 223      -1.905 -25.323 -31.111  1.00 17.74           N  
-ATOM   1766  CA  GLU A 223      -0.619 -24.728 -31.536  1.00 18.07           C  
-ATOM   1767  C   GLU A 223       0.130 -24.160 -30.333  1.00 16.86           C  
-ATOM   1768  O   GLU A 223       1.333 -24.363 -30.176  1.00 15.67           O  
-ATOM   1769  CB  GLU A 223      -0.804 -23.571 -32.524  1.00 19.06           C  
-ATOM   1770  CG  GLU A 223      -1.303 -23.906 -33.905  1.00 21.95           C  
-ATOM   1771  CD  GLU A 223      -1.439 -22.669 -34.770  1.00 22.25           C  
-ATOM   1772  OE1 GLU A 223      -0.517 -22.398 -35.555  1.00 25.49           O  
-ATOM   1773  OE2 GLU A 223      -2.464 -21.961 -34.655  1.00 26.19           O  
-ATOM   1774  N   ILE A 224      -0.599 -23.420 -29.507  1.00 15.57           N  
-ATOM   1775  CA  ILE A 224      -0.032 -22.786 -28.311  1.00 16.21           C  
-ATOM   1776  C   ILE A 224       0.432 -23.821 -27.287  1.00 16.35           C  
-ATOM   1777  O   ILE A 224       1.525 -23.703 -26.750  1.00 15.67           O  
-ATOM   1778  CB  ILE A 224      -1.015 -21.777 -27.676  1.00 15.54           C  
-ATOM   1779  CG1 ILE A 224      -1.210 -20.594 -28.622  1.00 15.76           C  
-ATOM   1780  CG2 ILE A 224      -0.484 -21.333 -26.299  1.00 15.83           C  
-ATOM   1781  CD1 ILE A 224      -2.405 -19.663 -28.252  1.00 14.29           C  
-ATOM   1782  N  AGLU A 225      -0.397 -24.830 -27.020  0.50 17.36           N  
-ATOM   1783  N  BGLU A 225      -0.398 -24.828 -27.033  0.50 17.17           N  
-ATOM   1784  CA AGLU A 225      -0.018 -25.930 -26.127  0.50 17.87           C  
-ATOM   1785  CA BGLU A 225      -0.041 -25.917 -26.129  0.50 17.53           C  
-ATOM   1786  C  AGLU A 225       1.299 -26.578 -26.552  0.50 17.13           C  
-ATOM   1787  C  BGLU A 225       1.267 -26.610 -26.547  0.50 16.95           C  
-ATOM   1788  O  AGLU A 225       2.180 -26.810 -25.721  0.50 16.08           O  
-ATOM   1789  O  BGLU A 225       2.113 -26.906 -25.701  0.50 16.00           O  
-ATOM   1790  CB AGLU A 225      -1.090 -27.014 -26.095  0.50 18.71           C  
-ATOM   1791  CB BGLU A 225      -1.176 -26.935 -26.074  0.50 18.14           C  
-ATOM   1792  CG AGLU A 225      -0.587 -28.340 -25.520  0.50 20.19           C  
-ATOM   1793  CG BGLU A 225      -0.973 -28.027 -25.043  0.50 19.11           C  
-ATOM   1794  CD AGLU A 225      -0.304 -28.268 -24.028  0.50 22.20           C  
-ATOM   1795  CD BGLU A 225      -2.034 -29.112 -25.128  0.50 20.58           C  
-ATOM   1796  OE1AGLU A 225      -0.781 -27.310 -23.389  0.50 24.97           O  
-ATOM   1797  OE1BGLU A 225      -3.239 -28.782 -25.160  0.50 21.82           O  
-ATOM   1798  OE2AGLU A 225       0.388 -29.163 -23.485  0.50 22.24           O  
-ATOM   1799  OE2BGLU A 225      -1.656 -30.299 -25.162  0.50 21.22           O  
-ATOM   1800  N   ASP A 226       1.423 -26.858 -27.848  1.00 16.28           N  
-ATOM   1801  CA  ASP A 226       2.643 -27.470 -28.402  1.00 14.67           C  
-ATOM   1802  C   ASP A 226       3.884 -26.590 -28.162  1.00 14.03           C  
-ATOM   1803  O   ASP A 226       4.924 -27.078 -27.722  1.00 14.40           O  
-ATOM   1804  CB  ASP A 226       2.494 -27.684 -29.912  1.00 15.07           C  
-ATOM   1805  CG  ASP A 226       1.647 -28.899 -30.294  1.00 16.66           C  
-ATOM   1806  OD1 ASP A 226       1.301 -29.736 -29.432  1.00 20.14           O  
-ATOM   1807  OD2 ASP A 226       1.339 -29.019 -31.506  1.00 17.48           O  
-ATOM   1808  N   ILE A 227       3.765 -25.298 -28.447  1.00 13.32           N  
-ATOM   1809  CA  ILE A 227       4.882 -24.334 -28.270  1.00 14.59           C  
-ATOM   1810  C   ILE A 227       5.384 -24.316 -26.812  1.00 13.17           C  
-ATOM   1811  O   ILE A 227       6.596 -24.331 -26.544  1.00 13.60           O  
-ATOM   1812  CB  ILE A 227       4.462 -22.917 -28.703  1.00 14.91           C  
-ATOM   1813  CG1 ILE A 227       4.237 -22.870 -30.222  1.00 16.12           C  
-ATOM   1814  CG2 ILE A 227       5.520 -21.865 -28.298  1.00 16.30           C  
-ATOM   1815  CD1 ILE A 227       3.336 -21.740 -30.677  1.00 13.80           C  
-ATOM   1816  N   ILE A 228       4.439 -24.280 -25.882  1.00 12.15           N  
-ATOM   1817  CA  ILE A 228       4.752 -24.290 -24.441  1.00 13.17           C  
-ATOM   1818  C   ILE A 228       5.455 -25.577 -24.032  1.00 14.57           C  
-ATOM   1819  O   ILE A 228       6.457 -25.539 -23.297  1.00 14.94           O  
-ATOM   1820  CB  ILE A 228       3.489 -24.068 -23.570  1.00 13.23           C  
-ATOM   1821  CG1 ILE A 228       2.912 -22.666 -23.807  1.00 15.20           C  
-ATOM   1822  CG2 ILE A 228       3.803 -24.233 -22.074  1.00 14.71           C  
-ATOM   1823  CD1 ILE A 228       1.521 -22.481 -23.189  1.00 15.55           C  
-ATOM   1824  N   ARG A 229       4.951 -26.709 -24.521  1.00 15.66           N  
-ATOM   1825  CA  ARG A 229       5.488 -28.003 -24.124  1.00 17.41           C  
-ATOM   1826  C   ARG A 229       6.950 -28.124 -24.527  1.00 16.79           C  
-ATOM   1827  O   ARG A 229       7.799 -28.419 -23.676  1.00 16.20           O  
-ATOM   1828  CB  ARG A 229       4.672 -29.160 -24.710  1.00 18.80           C  
-ATOM   1829  CG  ARG A 229       5.092 -30.549 -24.210  1.00 21.17           C  
-ATOM   1830  CD  ARG A 229       4.339 -31.682 -24.911  1.00 22.49           C  
-ATOM   1831  NE  ARG A 229       4.556 -31.687 -26.365  1.00 24.22           N  
-ATOM   1832  CZ  ARG A 229       3.682 -31.298 -27.297  1.00 25.99           C  
-ATOM   1833  NH1 ARG A 229       2.463 -30.846 -26.987  1.00 28.52           N  
-ATOM   1834  NH2 ARG A 229       4.032 -31.363 -28.577  1.00 27.00           N  
-ATOM   1835  N   ILE A 230       7.242 -27.873 -25.800  1.00 15.27           N  
-ATOM   1836  CA  ILE A 230       8.604 -28.038 -26.307  1.00 16.00           C  
-ATOM   1837  C   ILE A 230       9.534 -27.005 -25.668  1.00 15.91           C  
-ATOM   1838  O   ILE A 230      10.689 -27.317 -25.380  1.00 14.27           O  
-ATOM   1839  CB  ILE A 230       8.693 -28.032 -27.887  1.00 14.25           C  
-ATOM   1840  CG1 ILE A 230      10.119 -28.340 -28.367  1.00 15.29           C  
-ATOM   1841  CG2 ILE A 230       8.149 -26.715 -28.505  1.00 14.22           C  
-ATOM   1842  CD1 ILE A 230      10.692 -29.704 -27.877  1.00 16.44           C  
-ATOM   1843  N   THR A 231       9.036 -25.786 -25.432  1.00 14.64           N  
-ATOM   1844  CA  THR A 231       9.864 -24.738 -24.812  1.00 13.25           C  
-ATOM   1845  C   THR A 231      10.217 -25.093 -23.362  1.00 13.42           C  
-ATOM   1846  O   THR A 231      11.373 -24.937 -22.952  1.00 14.10           O  
-ATOM   1847  CB  THR A 231       9.211 -23.353 -24.949  1.00 11.73           C  
-ATOM   1848  OG1 THR A 231       8.967 -23.121 -26.337  1.00 13.12           O  
-ATOM   1849  CG2 THR A 231      10.125 -22.256 -24.410  1.00 13.65           C  
-ATOM   1850  N   GLU A 232       9.250 -25.608 -22.609  1.00 14.41           N  
-ATOM   1851  CA  GLU A 232       9.503 -26.092 -21.253  1.00 15.10           C  
-ATOM   1852  C   GLU A 232      10.533 -27.224 -21.253  1.00 16.10           C  
-ATOM   1853  O   GLU A 232      11.379 -27.289 -20.369  1.00 16.30           O  
-ATOM   1854  CB  GLU A 232       8.226 -26.594 -20.588  1.00 15.00           C  
-ATOM   1855  CG  GLU A 232       7.281 -25.466 -20.138  1.00 14.57           C  
-ATOM   1856  CD  GLU A 232       6.041 -25.977 -19.456  1.00 18.58           C  
-ATOM   1857  OE1 GLU A 232       5.582 -27.086 -19.814  1.00 18.17           O  
-ATOM   1858  OE2 GLU A 232       5.516 -25.263 -18.573  1.00 16.84           O  
-ATOM   1859  N   GLU A 233      10.447 -28.103 -22.242  1.00 17.39           N  
-ATOM   1860  CA  GLU A 233      11.381 -29.227 -22.356  1.00 18.37           C  
-ATOM   1861  C   GLU A 233      12.811 -28.769 -22.562  1.00 18.83           C  
-ATOM   1862  O   GLU A 233      13.724 -29.311 -21.933  1.00 16.31           O  
-ATOM   1863  CB  GLU A 233      10.949 -30.181 -23.476  1.00 20.00           C  
-ATOM   1864  CG  GLU A 233       9.712 -30.958 -23.097  1.00 24.39           C  
-ATOM   1865  CD  GLU A 233       9.170 -31.863 -24.208  1.00 28.68           C  
-ATOM   1866  OE1 GLU A 233       9.834 -32.010 -25.257  1.00 30.48           O  
-ATOM   1867  OE2 GLU A 233       8.071 -32.428 -24.003  1.00 31.01           O  
-ATOM   1868  N   ILE A 234      13.006 -27.768 -23.422  1.00 17.71           N  
-ATOM   1869  CA  ILE A 234      14.361 -27.290 -23.721  1.00 18.55           C  
-ATOM   1870  C   ILE A 234      14.930 -26.411 -22.607  1.00 19.53           C  
-ATOM   1871  O   ILE A 234      16.144 -26.348 -22.464  1.00 20.32           O  
-ATOM   1872  CB  ILE A 234      14.495 -26.634 -25.135  1.00 19.50           C  
-ATOM   1873  CG1 ILE A 234      13.804 -25.271 -25.252  1.00 18.09           C  
-ATOM   1874  CG2 ILE A 234      13.980 -27.618 -26.211  1.00 17.96           C  
-ATOM   1875  CD1 ILE A 234      13.927 -24.644 -26.677  1.00 16.14           C  
-ATOM   1876  N   PHE A 235      14.088 -25.744 -21.822  1.00 18.18           N  
-ATOM   1877  CA  PHE A 235      14.582 -25.059 -20.607  1.00 18.30           C  
-ATOM   1878  C   PHE A 235      14.659 -25.950 -19.352  1.00 19.06           C  
-ATOM   1879  O   PHE A 235      15.338 -25.569 -18.376  1.00 18.83           O  
-ATOM   1880  CB  PHE A 235      13.695 -23.856 -20.250  1.00 18.68           C  
-ATOM   1881  CG  PHE A 235      13.942 -22.608 -21.060  1.00 18.04           C  
-ATOM   1882  CD1 PHE A 235      14.846 -21.643 -20.619  1.00 19.71           C  
-ATOM   1883  CD2 PHE A 235      13.236 -22.361 -22.231  1.00 17.53           C  
-ATOM   1884  CE1 PHE A 235      15.056 -20.477 -21.333  1.00 17.00           C  
-ATOM   1885  CE2 PHE A 235      13.442 -21.195 -22.955  1.00 17.92           C  
-ATOM   1886  CZ  PHE A 235      14.354 -20.249 -22.507  1.00 18.41           C  
-ATOM   1887  N  ATHR A 236      14.008 -27.121 -19.387  0.70 18.19           N  
-ATOM   1888  N  BTHR A 236      13.960 -27.087 -19.380  0.30 18.86           N  
-ATOM   1889  CA ATHR A 236      13.729 -27.978 -18.209  0.70 19.20           C  
-ATOM   1890  CA BTHR A 236      13.780 -27.957 -18.217  0.30 19.41           C  
-ATOM   1891  C  ATHR A 236      13.203 -27.155 -17.033  0.70 20.29           C  
-ATOM   1892  C  BTHR A 236      13.199 -27.165 -17.039  0.30 20.09           C  
-ATOM   1893  O  ATHR A 236      13.640 -27.298 -15.891  0.70 20.29           O  
-ATOM   1894  O  BTHR A 236      13.605 -27.354 -15.892  0.30 20.14           O  
-ATOM   1895  CB ATHR A 236      14.920 -28.910 -17.778  0.70 19.40           C  
-ATOM   1896  CB BTHR A 236      15.100 -28.644 -17.805  0.30 19.50           C  
-ATOM   1897  OG1ATHR A 236      16.071 -28.136 -17.423  0.70 18.08           O  
-ATOM   1898  OG1BTHR A 236      15.797 -29.094 -18.973  0.30 18.48           O  
-ATOM   1899  CG2ATHR A 236      15.278 -29.867 -18.891  0.70 19.25           C  
-ATOM   1900  CG2BTHR A 236      14.819 -29.816 -16.903  0.30 19.28           C  
-ATOM   1901  N   GLU A 237      12.243 -26.283 -17.343  1.00 20.13           N  
-ATOM   1902  CA  GLU A 237      11.653 -25.379 -16.368  1.00 21.05           C  
-ATOM   1903  C   GLU A 237      10.200 -25.145 -16.799  1.00 20.09           C  
-ATOM   1904  O   GLU A 237       9.890 -25.263 -17.987  1.00 15.93           O  
-ATOM   1905  CB  GLU A 237      12.462 -24.082 -16.404  1.00 23.54           C  
-ATOM   1906  CG  GLU A 237      12.284 -23.125 -15.243  1.00 29.38           C  
-ATOM   1907  CD  GLU A 237      13.279 -23.351 -14.091  1.00 32.95           C  
-ATOM   1908  OE1 GLU A 237      14.514 -23.196 -14.288  1.00 38.23           O  
-ATOM   1909  OE2 GLU A 237      12.821 -23.663 -12.982  1.00 33.49           O  
-ATOM   1910  N   ASP A 238       9.320 -24.829 -15.854  1.00 18.48           N  
-ATOM   1911  CA  ASP A 238       7.925 -24.518 -16.188  1.00 19.21           C  
-ATOM   1912  C   ASP A 238       7.840 -23.139 -16.839  1.00 17.59           C  
-ATOM   1913  O   ASP A 238       8.656 -22.253 -16.552  1.00 16.68           O  
-ATOM   1914  CB  ASP A 238       7.013 -24.590 -14.961  1.00 21.29           C  
-ATOM   1915  CG  ASP A 238       7.276 -23.482 -13.982  1.00 23.80           C  
-ATOM   1916  OD1 ASP A 238       8.209 -23.624 -13.175  1.00 28.73           O  
-ATOM   1917  OD2 ASP A 238       6.553 -22.467 -14.029  1.00 26.14           O  
-ATOM   1918  N   ALA A 239       6.849 -22.976 -17.717  1.00 16.18           N  
-ATOM   1919  CA  ALA A 239       6.657 -21.750 -18.505  1.00 17.01           C  
-ATOM   1920  C   ALA A 239       6.674 -20.453 -17.682  1.00 17.16           C  
-ATOM   1921  O   ALA A 239       7.357 -19.483 -18.040  1.00 16.88           O  
-ATOM   1922  CB  ALA A 239       5.334 -21.855 -19.308  1.00 16.20           C  
-ATOM   1923  N   GLU A 240       5.931 -20.425 -16.577  1.00 17.33           N  
-ATOM   1924  CA  GLU A 240       5.888 -19.217 -15.748  1.00 18.28           C  
-ATOM   1925  C   GLU A 240       7.273 -18.845 -15.214  1.00 18.59           C  
-ATOM   1926  O   GLU A 240       7.651 -17.670 -15.224  1.00 17.53           O  
-ATOM   1927  CB  GLU A 240       4.910 -19.352 -14.582  1.00 18.91           C  
-ATOM   1928  CG  GLU A 240       4.742 -18.041 -13.835  1.00 21.66           C  
-ATOM   1929  N   SER A 241       8.015 -19.846 -14.756  1.00 17.95           N  
-ATOM   1930  CA  SER A 241       9.376 -19.645 -14.244  1.00 17.79           C  
-ATOM   1931  C   SER A 241      10.349 -19.142 -15.312  1.00 16.27           C  
-ATOM   1932  O   SER A 241      11.192 -18.290 -15.031  1.00 16.65           O  
-ATOM   1933  CB  SER A 241       9.931 -20.934 -13.630  1.00 19.03           C  
-ATOM   1934  OG  SER A 241       9.228 -21.296 -12.457  1.00 19.94           O  
-ATOM   1935  N   ILE A 242      10.232 -19.677 -16.524  1.00 15.16           N  
-ATOM   1936  CA  ILE A 242      11.048 -19.265 -17.659  1.00 14.26           C  
-ATOM   1937  C   ILE A 242      10.902 -17.764 -17.861  1.00 14.18           C  
-ATOM   1938  O   ILE A 242      11.903 -17.043 -17.962  1.00 12.57           O  
-ATOM   1939  CB  ILE A 242      10.660 -20.031 -18.968  1.00 15.15           C  
-ATOM   1940  CG1 ILE A 242      11.052 -21.514 -18.910  1.00 14.76           C  
-ATOM   1941  CG2 ILE A 242      11.322 -19.377 -20.191  1.00 13.69           C  
-ATOM   1942  CD1 ILE A 242      10.391 -22.377 -20.011  1.00 13.87           C  
-ATOM   1943  N   VAL A 243       9.662 -17.287 -17.894  1.00 12.61           N  
-ATOM   1944  CA  VAL A 243       9.409 -15.850 -18.128  1.00 14.66           C  
-ATOM   1945  C   VAL A 243       9.949 -14.996 -16.977  1.00 13.99           C  
-ATOM   1946  O   VAL A 243      10.594 -13.978 -17.212  1.00 14.16           O  
-ATOM   1947  CB  VAL A 243       7.910 -15.571 -18.390  1.00 14.72           C  
-ATOM   1948  CG1 VAL A 243       7.659 -14.083 -18.575  1.00 15.55           C  
-ATOM   1949  CG2 VAL A 243       7.451 -16.331 -19.617  1.00 12.12           C  
-ATOM   1950  N   ILE A 244       9.702 -15.427 -15.744  1.00 14.30           N  
-ATOM   1951  CA  ILE A 244      10.250 -14.761 -14.562  1.00 13.96           C  
-ATOM   1952  C   ILE A 244      11.763 -14.638 -14.645  1.00 13.92           C  
-ATOM   1953  O   ILE A 244      12.315 -13.551 -14.454  1.00 12.46           O  
-ATOM   1954  CB  ILE A 244       9.889 -15.516 -13.254  1.00 14.28           C  
-ATOM   1955  CG1 ILE A 244       8.399 -15.392 -12.926  1.00 14.26           C  
-ATOM   1956  CG2 ILE A 244      10.700 -14.978 -12.103  1.00 14.54           C  
-ATOM   1957  CD1 ILE A 244       7.975 -16.263 -11.718  1.00 15.91           C  
-ATOM   1958  N   ASN A 245      12.428 -15.753 -14.955  1.00 13.50           N  
-ATOM   1959  CA  ASN A 245      13.888 -15.769 -15.042  1.00 15.30           C  
-ATOM   1960  C   ASN A 245      14.388 -14.858 -16.151  1.00 14.13           C  
-ATOM   1961  O   ASN A 245      15.377 -14.148 -15.966  1.00 13.73           O  
-ATOM   1962  CB  ASN A 245      14.410 -17.208 -15.241  1.00 17.67           C  
-ATOM   1963  CG  ASN A 245      14.155 -18.101 -14.040  1.00 21.72           C  
-ATOM   1964  OD1 ASN A 245      13.947 -17.616 -12.929  1.00 24.29           O  
-ATOM   1965  ND2 ASN A 245      14.180 -19.424 -14.256  1.00 22.71           N  
-ATOM   1966  N   GLU A 246      13.703 -14.876 -17.308  1.00 14.18           N  
-ATOM   1967  CA  GLU A 246      14.083 -14.010 -18.436  1.00 14.56           C  
-ATOM   1968  C   GLU A 246      13.908 -12.529 -18.111  1.00 12.06           C  
-ATOM   1969  O   GLU A 246      14.767 -11.731 -18.490  1.00 12.78           O  
-ATOM   1970  CB  GLU A 246      13.343 -14.379 -19.737  1.00 14.60           C  
-ATOM   1971  CG  GLU A 246      13.792 -15.701 -20.351  1.00 15.20           C  
-ATOM   1972  CD  GLU A 246      15.279 -15.756 -20.661  1.00 15.28           C  
-ATOM   1973  OE1 GLU A 246      15.836 -14.795 -21.208  1.00 14.96           O  
-ATOM   1974  OE2 GLU A 246      15.894 -16.787 -20.353  1.00 16.97           O  
-ATOM   1975  N   ARG A 247      12.824 -12.152 -17.425  1.00 14.02           N  
-ATOM   1976  CA  ARG A 247      12.647 -10.757 -16.996  1.00 13.27           C  
-ATOM   1977  C   ARG A 247      13.813 -10.290 -16.118  1.00 13.52           C  
-ATOM   1978  O   ARG A 247      14.434  -9.274 -16.386  1.00 14.69           O  
-ATOM   1979  CB  ARG A 247      11.314 -10.534 -16.261  1.00 12.38           C  
-ATOM   1980  CG  ARG A 247      10.073 -10.721 -17.094  1.00 13.26           C  
-ATOM   1981  CD  ARG A 247       8.787 -10.330 -16.340  1.00 13.65           C  
-ATOM   1982  NE  ARG A 247       7.612 -10.699 -17.131  1.00 12.01           N  
-ATOM   1983  CZ  ARG A 247       7.210 -10.052 -18.223  1.00 16.19           C  
-ATOM   1984  NH1 ARG A 247       7.859  -8.973 -18.659  1.00 15.92           N  
-ATOM   1985  NH2 ARG A 247       6.139 -10.483 -18.886  1.00 16.39           N  
-ATOM   1986  N   TYR A 248      14.117 -11.043 -15.069  1.00 15.28           N  
-ATOM   1987  CA  TYR A 248      15.238 -10.696 -14.190  1.00 15.60           C  
-ATOM   1988  C   TYR A 248      16.593 -10.724 -14.882  1.00 14.89           C  
-ATOM   1989  O   TYR A 248      17.426  -9.872 -14.595  1.00 14.89           O  
-ATOM   1990  CB  TYR A 248      15.249 -11.554 -12.909  1.00 15.63           C  
-ATOM   1991  CG  TYR A 248      14.181 -11.143 -11.926  1.00 18.12           C  
-ATOM   1992  CD1 TYR A 248      14.183  -9.874 -11.356  1.00 18.82           C  
-ATOM   1993  CD2 TYR A 248      13.163 -12.023 -11.550  1.00 17.02           C  
-ATOM   1994  CE1 TYR A 248      13.190  -9.485 -10.456  1.00 19.27           C  
-ATOM   1995  CE2 TYR A 248      12.176 -11.639 -10.651  1.00 18.21           C  
-ATOM   1996  CZ  TYR A 248      12.192 -10.370 -10.107  1.00 19.09           C  
-ATOM   1997  OH  TYR A 248      11.218  -9.984  -9.208  1.00 21.50           O  
-ATOM   1998  N   ALA A 249      16.816 -11.657 -15.806  1.00 15.97           N  
-ATOM   1999  CA  ALA A 249      18.085 -11.675 -16.556  1.00 16.18           C  
-ATOM   2000  C   ALA A 249      18.258 -10.388 -17.380  1.00 15.43           C  
-ATOM   2001  O   ALA A 249      19.331  -9.759 -17.357  1.00 14.40           O  
-ATOM   2002  CB  ALA A 249      18.199 -12.936 -17.411  1.00 15.30           C  
-ATOM   2003  N   PHE A 250      17.199  -9.993 -18.091  1.00 14.80           N  
-ATOM   2004  CA  PHE A 250      17.193  -8.756 -18.858  1.00 14.52           C  
-ATOM   2005  C   PHE A 250      17.500  -7.553 -17.970  1.00 13.00           C  
-ATOM   2006  O   PHE A 250      18.359  -6.721 -18.291  1.00 15.07           O  
-ATOM   2007  CB  PHE A 250      15.837  -8.562 -19.540  1.00 13.33           C  
-ATOM   2008  CG  PHE A 250      15.668  -7.201 -20.142  1.00 13.58           C  
-ATOM   2009  CD1 PHE A 250      16.194  -6.907 -21.401  1.00 15.11           C  
-ATOM   2010  CD2 PHE A 250      14.972  -6.208 -19.459  1.00 13.66           C  
-ATOM   2011  CE1 PHE A 250      16.041  -5.642 -21.953  1.00 14.74           C  
-ATOM   2012  CE2 PHE A 250      14.815  -4.948 -20.008  1.00 15.60           C  
-ATOM   2013  CZ  PHE A 250      15.347  -4.665 -21.255  1.00 16.83           C  
-ATOM   2014  N   ILE A 251      16.782  -7.473 -16.847  1.00 15.55           N  
-ATOM   2015  CA  ILE A 251      16.950  -6.398 -15.859  1.00 14.53           C  
-ATOM   2016  C   ILE A 251      18.390  -6.337 -15.337  1.00 16.13           C  
-ATOM   2017  O   ILE A 251      18.973  -5.254 -15.279  1.00 16.23           O  
-ATOM   2018  CB  ILE A 251      15.964  -6.545 -14.692  1.00 14.79           C  
-ATOM   2019  CG1 ILE A 251      14.535  -6.305 -15.170  1.00 13.52           C  
-ATOM   2020  CG2 ILE A 251      16.276  -5.558 -13.550  1.00 15.71           C  
-ATOM   2021  CD1 ILE A 251      13.504  -6.827 -14.193  1.00 16.07           C  
-ATOM   2022  N   GLU A 252      18.953  -7.485 -14.969  1.00 16.69           N  
-ATOM   2023  CA  GLU A 252      20.343  -7.513 -14.503  1.00 17.35           C  
-ATOM   2024  C   GLU A 252      21.331  -7.024 -15.562  1.00 17.75           C  
-ATOM   2025  O   GLU A 252      22.255  -6.249 -15.228  1.00 18.73           O  
-ATOM   2026  CB  GLU A 252      20.729  -8.913 -14.002  1.00 18.24           C  
-ATOM   2027  CG  GLU A 252      19.980  -9.318 -12.741  1.00 20.83           C  
-ATOM   2028  CD  GLU A 252      20.437 -10.629 -12.148  1.00 25.67           C  
-ATOM   2029  OE1 GLU A 252      21.608 -11.041 -12.353  1.00 27.62           O  
-ATOM   2030  OE2 GLU A 252      19.608 -11.244 -11.448  1.00 32.18           O  
-ATOM   2031  N   ARG A 253      21.140  -7.469 -16.810  1.00 17.83           N  
-ATOM   2032  CA  ARG A 253      21.975  -7.052 -17.945  1.00 19.36           C  
-ATOM   2033  C   ARG A 253      21.896  -5.547 -18.147  1.00 19.27           C  
-ATOM   2034  O   ARG A 253      22.920  -4.872 -18.251  1.00 20.25           O  
-ATOM   2035  CB  ARG A 253      21.569  -7.762 -19.247  1.00 20.32           C  
-ATOM   2036  CG  ARG A 253      21.935  -9.241 -19.352  1.00 22.73           C  
-ATOM   2037  CD  ARG A 253      21.803  -9.772 -20.797  1.00 24.35           C  
-ATOM   2038  NE  ARG A 253      20.444  -9.710 -21.366  1.00 23.56           N  
-ATOM   2039  CZ  ARG A 253      19.477 -10.619 -21.228  1.00 25.12           C  
-ATOM   2040  NH1 ARG A 253      19.648 -11.723 -20.508  1.00 26.31           N  
-ATOM   2041  NH2 ARG A 253      18.291 -10.414 -21.820  1.00 25.36           N  
-ATOM   2042  N   VAL A 254      20.677  -5.011 -18.167  1.00 19.63           N  
-ATOM   2043  CA  VAL A 254      20.481  -3.570 -18.303  1.00 19.88           C  
-ATOM   2044  C   VAL A 254      21.163  -2.805 -17.168  1.00 20.48           C  
-ATOM   2045  O   VAL A 254      21.909  -1.844 -17.429  1.00 22.83           O  
-ATOM   2046  CB  VAL A 254      18.979  -3.199 -18.345  1.00 19.28           C  
-ATOM   2047  CG1 VAL A 254      18.816  -1.681 -18.277  1.00 20.52           C  
-ATOM   2048  CG2 VAL A 254      18.324  -3.782 -19.603  1.00 18.05           C  
-ATOM   2049  N   CYS A 255      20.929  -3.221 -15.924  1.00 21.26           N  
-ATOM   2050  CA  CYS A 255      21.499  -2.507 -14.774  1.00 24.49           C  
-ATOM   2051  C   CYS A 255      23.030  -2.570 -14.758  1.00 27.09           C  
-ATOM   2052  O   CYS A 255      23.675  -1.587 -14.405  1.00 27.92           O  
-ATOM   2053  CB  CYS A 255      20.899  -2.987 -13.452  1.00 24.15           C  
-ATOM   2054  SG  CYS A 255      19.134  -2.594 -13.320  1.00 24.08           S  
-ATOM   2055  N   GLN A 256      23.604  -3.703 -15.157  1.00 29.18           N  
-ATOM   2056  CA  GLN A 256      25.064  -3.798 -15.337  1.00 32.41           C  
-ATOM   2057  C   GLN A 256      25.578  -2.845 -16.425  1.00 34.48           C  
-ATOM   2058  O   GLN A 256      26.525  -2.089 -16.192  1.00 34.77           O  
-ATOM   2059  CB  GLN A 256      25.484  -5.223 -15.707  1.00 32.29           C  
-ATOM   2060  CG  GLN A 256      26.991  -5.392 -15.967  1.00 35.09           C  
-ATOM   2061  CD  GLN A 256      27.308  -6.597 -16.822  1.00 38.72           C  
-ATOM   2062  OE1 GLN A 256      28.030  -7.483 -16.384  1.00 44.50           O  
-ATOM   2063  NE2 GLN A 256      26.769  -6.646 -18.038  1.00 40.51           N  
-ATOM   2064  N   MET A 257      24.976  -2.900 -17.614  1.00 37.30           N  
-ATOM   2065  CA  MET A 257      25.356  -2.010 -18.726  1.00 40.10           C  
-ATOM   2066  C   MET A 257      25.092  -0.528 -18.411  1.00 42.27           C  
-ATOM   2067  O   MET A 257      25.667   0.348 -19.068  1.00 42.39           O  
-ATOM   2068  CB  MET A 257      24.643  -2.391 -20.036  1.00 40.48           C  
-ATOM   2069  CG  MET A 257      25.063  -3.739 -20.632  1.00 41.98           C  
-ATOM   2070  SD  MET A 257      24.282  -4.156 -22.219  1.00 44.66           S  
-ATOM   2071  CE  MET A 257      22.545  -4.356 -21.796  1.00 45.22           C  
-ATOM   2072  N   ALA A 258      24.235  -0.257 -17.421  1.00 44.35           N  
-ATOM   2073  CA  ALA A 258      23.910   1.106 -16.981  1.00 46.68           C  
-ATOM   2074  C   ALA A 258      24.650   1.569 -15.717  1.00 49.10           C  
-ATOM   2075  O   ALA A 258      24.139   2.419 -14.973  1.00 49.71           O  
-ATOM   2076  CB  ALA A 258      22.398   1.237 -16.780  1.00 46.00           C  
-ATOM   2077  N   GLU A 259      25.840   1.021 -15.467  1.00 51.25           N  
-ATOM   2078  CA  GLU A 259      26.663   1.437 -14.316  1.00 52.94           C  
-ATOM   2079  C   GLU A 259      28.128   1.502 -14.719  1.00 53.60           C  
-ATOM   2080  O   GLU A 259      28.455   2.093 -15.750  1.00 54.56           O  
-ATOM   2081  CB  GLU A 259      26.451   0.510 -13.108  1.00 53.80           C  
-ATOM   2082  CG  GLU A 259      25.107   0.740 -12.383  1.00 55.08           C  
-ATOM   2083  CD  GLU A 259      24.852  -0.210 -11.211  1.00 56.02           C  
-ATOM   2084  OE1 GLU A 259      25.770  -0.963 -10.819  1.00 56.14           O  
-ATOM   2085  OE2 GLU A 259      23.716  -0.199 -10.683  1.00 56.84           O  
-TER    2086      GLU A 259                                                      
-ATOM   2087  N   GLY B  -1      11.027  13.982 -38.935  1.00 32.92           N  
-ATOM   2088  CA  GLY B  -1      11.890  12.881 -38.411  1.00 33.43           C  
-ATOM   2089  C   GLY B  -1      13.238  12.800 -39.106  1.00 33.69           C  
-ATOM   2090  O   GLY B  -1      13.750  13.804 -39.604  1.00 34.38           O  
-ATOM   2091  N   SER B   0      13.814  11.596 -39.134  1.00 34.05           N  
-ATOM   2092  CA  SER B   0      15.104  11.335 -39.775  1.00 33.83           C  
-ATOM   2093  C   SER B   0      14.942  10.293 -40.887  1.00 33.51           C  
-ATOM   2094  O   SER B   0      14.492   9.180 -40.636  1.00 33.45           O  
-ATOM   2095  CB  SER B   0      16.120  10.850 -38.733  1.00 33.70           C  
-ATOM   2096  OG  SER B   0      17.403  10.658 -39.309  1.00 35.15           O  
-ATOM   2097  N   MET B   1      15.300  10.663 -42.111  1.00 33.25           N  
-ATOM   2098  CA  MET B   1      15.260   9.745 -43.237  1.00 33.74           C  
-ATOM   2099  C   MET B   1      16.330   8.678 -42.986  1.00 31.71           C  
-ATOM   2100  O   MET B   1      17.447   9.028 -42.593  1.00 31.73           O  
-ATOM   2101  CB  MET B   1      15.569  10.488 -44.547  1.00 36.03           C  
-ATOM   2102  CG  MET B   1      15.041   9.836 -45.832  1.00 37.50           C  
-ATOM   2103  SD  MET B   1      13.577  10.628 -46.572  1.00 44.60           S  
-ATOM   2104  CE  MET B   1      14.339  12.146 -47.160  1.00 39.97           C  
-ATOM   2105  N   THR B   2      15.987   7.402 -43.180  1.00 27.72           N  
-ATOM   2106  CA  THR B   2      16.992   6.328 -43.188  1.00 25.75           C  
-ATOM   2107  C   THR B   2      17.722   6.391 -44.527  1.00 23.93           C  
-ATOM   2108  O   THR B   2      17.091   6.275 -45.586  1.00 25.07           O  
-ATOM   2109  CB  THR B   2      16.379   4.960 -43.009  1.00 24.97           C  
-ATOM   2110  OG1 THR B   2      15.634   4.940 -41.791  1.00 24.96           O  
-ATOM   2111  CG2 THR B   2      17.464   3.847 -42.979  1.00 22.84           C  
-ATOM   2112  N   GLU B   3      19.040   6.573 -44.474  1.00 22.94           N  
-ATOM   2113  CA  GLU B   3      19.867   6.776 -45.643  1.00 22.98           C  
-ATOM   2114  C   GLU B   3      20.561   5.467 -46.005  1.00 21.77           C  
-ATOM   2115  O   GLU B   3      21.385   4.962 -45.234  1.00 20.46           O  
-ATOM   2116  CB  GLU B   3      20.902   7.867 -45.366  1.00 25.03           C  
-ATOM   2117  CG  GLU B   3      21.525   8.451 -46.599  1.00 29.11           C  
-ATOM   2118  CD  GLU B   3      20.635   9.449 -47.321  1.00 32.58           C  
-ATOM   2119  OE1 GLU B   3      20.857   9.650 -48.531  1.00 36.61           O  
-ATOM   2120  OE2 GLU B   3      19.718  10.031 -46.700  1.00 39.09           O  
-ATOM   2121  N   ILE B   4      20.220   4.930 -47.170  1.00 19.95           N  
-ATOM   2122  CA  ILE B   4      20.746   3.638 -47.632  1.00 19.81           C  
-ATOM   2123  C   ILE B   4      21.677   3.887 -48.809  1.00 19.40           C  
-ATOM   2124  O   ILE B   4      21.243   4.407 -49.845  1.00 18.66           O  
-ATOM   2125  CB  ILE B   4      19.594   2.675 -48.031  1.00 20.31           C  
-ATOM   2126  CG1 ILE B   4      18.685   2.390 -46.841  1.00 20.01           C  
-ATOM   2127  CG2 ILE B   4      20.127   1.346 -48.579  1.00 17.92           C  
-ATOM   2128  CD1 ILE B   4      17.331   1.856 -47.249  1.00 19.24           C  
-ATOM   2129  N   ALA B   5      22.951   3.518 -48.643  1.00 17.50           N  
-ATOM   2130  CA  ALA B   5      23.967   3.690 -49.673  1.00 16.81           C  
-ATOM   2131  C   ALA B   5      23.948   2.504 -50.627  1.00 17.69           C  
-ATOM   2132  O   ALA B   5      24.218   1.378 -50.210  1.00 18.22           O  
-ATOM   2133  CB  ALA B   5      25.368   3.832 -49.027  1.00 16.16           C  
-ATOM   2134  N   LEU B   6      23.645   2.750 -51.900  1.00 16.89           N  
-ATOM   2135  CA  LEU B   6      23.561   1.697 -52.902  1.00 16.59           C  
-ATOM   2136  C   LEU B   6      24.865   1.670 -53.668  1.00 15.65           C  
-ATOM   2137  O   LEU B   6      25.270   2.677 -54.269  1.00 16.31           O  
-ATOM   2138  CB  LEU B   6      22.404   1.941 -53.877  1.00 16.54           C  
-ATOM   2139  CG  LEU B   6      21.976   0.779 -54.779  1.00 15.50           C  
-ATOM   2140  CD1 LEU B   6      21.279  -0.317 -54.014  1.00 16.00           C  
-ATOM   2141  CD2 LEU B   6      21.074   1.315 -55.900  1.00 15.30           C  
-ATOM   2142  N   ILE B   7      25.516   0.514 -53.676  1.00 13.81           N  
-ATOM   2143  CA  ILE B   7      26.833   0.425 -54.293  1.00 14.49           C  
-ATOM   2144  C   ILE B   7      27.120  -0.987 -54.744  1.00 13.98           C  
-ATOM   2145  O   ILE B   7      26.640  -1.939 -54.167  1.00 14.00           O  
-ATOM   2146  CB  ILE B   7      27.944   0.941 -53.324  1.00 15.98           C  
-ATOM   2147  CG1 ILE B   7      29.291   1.117 -54.044  1.00 17.03           C  
-ATOM   2148  CG2 ILE B   7      28.091   0.040 -52.115  1.00 15.34           C  
-ATOM   2149  CD1 ILE B   7      30.258   1.947 -53.270  1.00 18.35           C  
-ATOM   2150  N   GLY B   8      27.915  -1.094 -55.789  1.00 15.23           N  
-ATOM   2151  CA  GLY B   8      28.267  -2.387 -56.363  1.00 15.56           C  
-ATOM   2152  C   GLY B   8      29.204  -2.147 -57.521  1.00 16.16           C  
-ATOM   2153  O   GLY B   8      29.509  -0.988 -57.847  1.00 15.86           O  
-ATOM   2154  N   ASN B   9      29.692  -3.232 -58.119  1.00 16.20           N  
-ATOM   2155  CA  ASN B   9      30.526  -3.136 -59.299  1.00 15.39           C  
-ATOM   2156  C   ASN B   9      29.748  -2.548 -60.482  1.00 16.61           C  
-ATOM   2157  O   ASN B   9      28.507  -2.629 -60.529  1.00 16.04           O  
-ATOM   2158  CB  ASN B   9      31.009  -4.516 -59.779  1.00 14.17           C  
-ATOM   2159  CG  ASN B   9      31.913  -5.276 -58.801  1.00 14.13           C  
-ATOM   2160  OD1 ASN B   9      32.225  -6.439 -59.090  1.00 13.18           O  
-ATOM   2161  ND2 ASN B   9      32.350  -4.666 -57.691  1.00 13.59           N  
-ATOM   2162  N   PRO B  10      30.475  -1.970 -61.456  1.00 17.22           N  
-ATOM   2163  CA  PRO B  10      29.879  -1.665 -62.748  1.00 17.96           C  
-ATOM   2164  C   PRO B  10      29.244  -2.931 -63.326  1.00 17.40           C  
-ATOM   2165  O   PRO B  10      29.757  -4.026 -63.106  1.00 16.70           O  
-ATOM   2166  CB  PRO B  10      31.084  -1.210 -63.586  1.00 18.78           C  
-ATOM   2167  CG  PRO B  10      32.025  -0.643 -62.593  1.00 18.01           C  
-ATOM   2168  CD  PRO B  10      31.879  -1.523 -61.392  1.00 17.49           C  
-ATOM   2169  N   ALA B  11      28.125  -2.776 -64.031  1.00 17.66           N  
-ATOM   2170  CA  ALA B  11      27.420  -3.899 -64.657  1.00 17.23           C  
-ATOM   2171  C   ALA B  11      26.840  -4.948 -63.683  1.00 16.31           C  
-ATOM   2172  O   ALA B  11      26.553  -6.061 -64.090  1.00 17.10           O  
-ATOM   2173  CB  ALA B  11      28.331  -4.569 -65.693  1.00 19.50           C  
-ATOM   2174  N   SER B  12      26.641  -4.602 -62.410  1.00 15.83           N  
-ATOM   2175  CA  SER B  12      26.022  -5.512 -61.437  1.00 15.15           C  
-ATOM   2176  C   SER B  12      24.487  -5.407 -61.398  1.00 14.96           C  
-ATOM   2177  O   SER B  12      23.821  -6.215 -60.743  1.00 14.77           O  
-ATOM   2178  CB  SER B  12      26.580  -5.248 -60.037  1.00 15.51           C  
-ATOM   2179  OG  SER B  12      26.286  -3.918 -59.626  1.00 15.17           O  
-ATOM   2180  N   GLY B  13      23.924  -4.435 -62.108  1.00 14.54           N  
-ATOM   2181  CA  GLY B  13      22.488  -4.185 -62.078  1.00 15.12           C  
-ATOM   2182  C   GLY B  13      22.095  -3.087 -61.096  1.00 15.18           C  
-ATOM   2183  O   GLY B  13      20.919  -2.912 -60.802  1.00 14.05           O  
-ATOM   2184  N   LYS B  14      23.079  -2.343 -60.596  1.00 17.38           N  
-ATOM   2185  CA  LYS B  14      22.837  -1.287 -59.609  1.00 17.23           C  
-ATOM   2186  C   LYS B  14      21.854  -0.237 -60.132  1.00 18.21           C  
-ATOM   2187  O   LYS B  14      20.898   0.080 -59.431  1.00 16.85           O  
-ATOM   2188  CB  LYS B  14      24.161  -0.642 -59.152  1.00 17.42           C  
-ATOM   2189  CG  LYS B  14      23.993   0.517 -58.158  1.00 20.84           C  
-ATOM   2190  CD  LYS B  14      25.311   0.963 -57.538  1.00 21.74           C  
-ATOM   2191  CE  LYS B  14      26.194   1.658 -58.535  1.00 22.18           C  
-ATOM   2192  NZ  LYS B  14      25.600   2.910 -59.043  1.00 20.67           N  
-ATOM   2193  N   THR B  15      22.073   0.291 -61.341  1.00 18.65           N  
-ATOM   2194  CA  THR B  15      21.174   1.311 -61.898  1.00 20.85           C  
-ATOM   2195  C   THR B  15      19.785   0.742 -62.111  1.00 20.56           C  
-ATOM   2196  O   THR B  15      18.792   1.401 -61.799  1.00 20.80           O  
-ATOM   2197  CB  THR B  15      21.694   1.898 -63.243  1.00 21.99           C  
-ATOM   2198  OG1 THR B  15      22.975   2.480 -63.022  1.00 24.37           O  
-ATOM   2199  CG2 THR B  15      20.767   2.956 -63.792  1.00 24.62           C  
-ATOM   2200  N   SER B  16      19.713  -0.480 -62.644  1.00 19.68           N  
-ATOM   2201  CA  SER B  16      18.409  -1.125 -62.838  1.00 20.07           C  
-ATOM   2202  C   SER B  16      17.645  -1.224 -61.509  1.00 20.25           C  
-ATOM   2203  O   SER B  16      16.440  -0.935 -61.446  1.00 19.02           O  
-ATOM   2204  CB  SER B  16      18.550  -2.507 -63.478  1.00 19.38           C  
-ATOM   2205  OG  SER B  16      19.220  -2.442 -64.732  1.00 19.93           O  
-ATOM   2206  N   LEU B  17      18.343  -1.632 -60.447  1.00 18.65           N  
-ATOM   2207  CA  LEU B  17      17.714  -1.701 -59.124  1.00 18.37           C  
-ATOM   2208  C   LEU B  17      17.341  -0.331 -58.568  1.00 19.56           C  
-ATOM   2209  O   LEU B  17      16.252  -0.180 -58.001  1.00 20.09           O  
-ATOM   2210  CB  LEU B  17      18.585  -2.460 -58.119  1.00 17.95           C  
-ATOM   2211  CG  LEU B  17      18.658  -3.967 -58.364  1.00 15.50           C  
-ATOM   2212  CD1 LEU B  17      19.694  -4.597 -57.427  1.00 15.17           C  
-ATOM   2213  CD2 LEU B  17      17.318  -4.668 -58.157  1.00 15.16           C  
-ATOM   2214  N   PHE B  18      18.240   0.641 -58.725  1.00 18.73           N  
-ATOM   2215  CA  PHE B  18      17.974   2.014 -58.306  1.00 19.61           C  
-ATOM   2216  C   PHE B  18      16.661   2.530 -58.914  1.00 20.42           C  
-ATOM   2217  O   PHE B  18      15.813   3.079 -58.205  1.00 19.93           O  
-ATOM   2218  CB  PHE B  18      19.123   2.936 -58.699  1.00 19.51           C  
-ATOM   2219  CG  PHE B  18      18.918   4.351 -58.257  1.00 22.19           C  
-ATOM   2220  CD1 PHE B  18      19.173   4.723 -56.943  1.00 22.89           C  
-ATOM   2221  CD2 PHE B  18      18.443   5.306 -59.142  1.00 24.32           C  
-ATOM   2222  CE1 PHE B  18      18.973   6.023 -56.524  1.00 24.55           C  
-ATOM   2223  CE2 PHE B  18      18.241   6.613 -58.719  1.00 24.99           C  
-ATOM   2224  CZ  PHE B  18      18.513   6.964 -57.412  1.00 24.80           C  
-ATOM   2225  N   ASN B  19      16.509   2.323 -60.222  1.00 20.95           N  
-ATOM   2226  CA  ASN B  19      15.304   2.743 -60.952  1.00 21.92           C  
-ATOM   2227  C   ASN B  19      14.016   2.076 -60.494  1.00 22.12           C  
-ATOM   2228  O   ASN B  19      12.987   2.755 -60.377  1.00 24.05           O  
-ATOM   2229  CB  ASN B  19      15.508   2.570 -62.472  1.00 23.46           C  
-ATOM   2230  CG  ASN B  19      16.525   3.548 -63.043  1.00 26.03           C  
-ATOM   2231  OD1 ASN B  19      16.802   4.598 -62.450  1.00 30.26           O  
-ATOM   2232  ND2 ASN B  19      17.092   3.209 -64.198  1.00 28.08           N  
-ATOM   2233  N   LEU B  20      14.054   0.769 -60.229  1.00 21.00           N  
-ATOM   2234  CA  LEU B  20      12.891   0.043 -59.705  1.00 21.86           C  
-ATOM   2235  C   LEU B  20      12.502   0.499 -58.303  1.00 22.26           C  
-ATOM   2236  O   LEU B  20      11.317   0.597 -57.979  1.00 21.51           O  
-ATOM   2237  CB  LEU B  20      13.158  -1.464 -59.626  1.00 21.96           C  
-ATOM   2238  CG  LEU B  20      13.131  -2.272 -60.918  1.00 23.91           C  
-ATOM   2239  CD1 LEU B  20      13.697  -3.656 -60.667  1.00 21.40           C  
-ATOM   2240  CD2 LEU B  20      11.705  -2.361 -61.450  1.00 22.89           C  
-ATOM   2241  N   ILE B  21      13.513   0.756 -57.473  1.00 21.50           N  
-ATOM   2242  CA  ILE B  21      13.292   1.109 -56.079  1.00 21.00           C  
-ATOM   2243  C   ILE B  21      12.731   2.523 -55.940  1.00 22.56           C  
-ATOM   2244  O   ILE B  21      11.813   2.735 -55.144  1.00 24.99           O  
-ATOM   2245  CB  ILE B  21      14.605   0.987 -55.245  1.00 20.52           C  
-ATOM   2246  CG1 ILE B  21      15.020  -0.483 -55.077  1.00 19.47           C  
-ATOM   2247  CG2 ILE B  21      14.430   1.584 -53.854  1.00 16.31           C  
-ATOM   2248  CD1 ILE B  21      16.462  -0.623 -54.625  1.00 21.44           C  
-ATOM   2249  N   THR B  22      13.288   3.466 -56.699  1.00 23.66           N  
-ATOM   2250  CA  THR B  22      12.913   4.874 -56.601  1.00 24.42           C  
-ATOM   2251  C   THR B  22      11.830   5.289 -57.602  1.00 28.08           C  
-ATOM   2252  O   THR B  22      11.312   6.400 -57.518  1.00 28.72           O  
-ATOM   2253  CB  THR B  22      14.149   5.800 -56.768  1.00 23.94           C  
-ATOM   2254  OG1 THR B  22      14.686   5.703 -58.087  1.00 22.61           O  
-ATOM   2255  CG2 THR B  22      15.248   5.455 -55.760  1.00 24.87           C  
-ATOM   2256  N   GLY B  23      11.494   4.401 -58.539  1.00 31.01           N  
-ATOM   2257  CA  GLY B  23      10.615   4.740 -59.655  1.00 34.14           C  
-ATOM   2258  C   GLY B  23      11.208   5.888 -60.452  1.00 36.19           C  
-ATOM   2259  O   GLY B  23      12.430   6.025 -60.555  1.00 36.76           O  
-ATOM   2260  N   HIS B  24      10.343   6.730 -61.005  1.00 38.23           N  
-ATOM   2261  CA  HIS B  24      10.803   7.892 -61.763  1.00 39.86           C  
-ATOM   2262  C   HIS B  24      11.412   8.990 -60.876  1.00 40.53           C  
-ATOM   2263  O   HIS B  24      12.221   9.779 -61.361  1.00 42.48           O  
-ATOM   2264  CB  HIS B  24       9.646   8.466 -62.584  1.00 39.86           C  
-ATOM   2265  N   ASN B  25      11.039   9.040 -59.595  1.00 40.57           N  
-ATOM   2266  CA  ASN B  25      11.496  10.108 -58.688  1.00 39.81           C  
-ATOM   2267  C   ASN B  25      12.986   9.994 -58.313  1.00 39.18           C  
-ATOM   2268  O   ASN B  25      13.364   9.102 -57.545  1.00 41.14           O  
-ATOM   2269  CB  ASN B  25      10.644  10.124 -57.421  1.00 40.02           C  
-ATOM   2270  N  AGLN B  26      13.807  10.891 -58.862  0.50 37.53           N  
-ATOM   2271  N  BGLN B  26      13.812  10.883 -58.865  0.50 37.75           N  
-ATOM   2272  CA AGLN B  26      15.249  10.912 -58.632  0.50 35.81           C  
-ATOM   2273  CA BGLN B  26      15.243  10.922 -58.579  0.50 36.22           C  
-ATOM   2274  C  AGLN B  26      15.745  12.355 -58.666  0.50 35.40           C  
-ATOM   2275  C  BGLN B  26      15.737  12.359 -58.647  0.50 35.62           C  
-ATOM   2276  O  AGLN B  26      15.049  13.232 -59.180  0.50 34.82           O  
-ATOM   2277  O  BGLN B  26      15.040  13.232 -59.166  0.50 35.03           O  
-ATOM   2278  CB AGLN B  26      15.972  10.080 -59.698  0.50 35.36           C  
-ATOM   2279  CB BGLN B  26      16.032  10.059 -59.568  0.50 36.01           C  
-ATOM   2280  CG AGLN B  26      15.326   8.722 -59.940  0.50 34.09           C  
-ATOM   2281  CG BGLN B  26      16.245  10.692 -60.940  0.50 35.36           C  
-ATOM   2282  CD AGLN B  26      16.055   7.845 -60.928  0.50 33.08           C  
-ATOM   2283  CD BGLN B  26      17.158   9.865 -61.826  0.50 35.11           C  
-ATOM   2284  OE1AGLN B  26      17.045   8.248 -61.544  0.50 32.21           O  
-ATOM   2285  OE1BGLN B  26      17.208   8.635 -61.716  0.50 35.07           O  
-ATOM   2286  NE2AGLN B  26      15.569   6.623 -61.077  0.50 28.93           N  
-ATOM   2287  NE2BGLN B  26      17.890  10.533 -62.708  0.50 32.83           N  
-ATOM   2288  N   ARG B  27      16.935  12.587 -58.111  1.00 33.89           N  
-ATOM   2289  CA  ARG B  27      17.591  13.900 -58.130  1.00 33.98           C  
-ATOM   2290  C   ARG B  27      19.061  13.698 -58.485  1.00 32.03           C  
-ATOM   2291  O   ARG B  27      19.738  12.897 -57.847  1.00 29.94           O  
-ATOM   2292  CB  ARG B  27      17.465  14.615 -56.781  1.00 34.80           C  
-ATOM   2293  CG  ARG B  27      18.051  16.023 -56.794  1.00 36.78           C  
-ATOM   2294  CD  ARG B  27      17.810  16.784 -55.498  1.00 38.17           C  
-ATOM   2295  NE  ARG B  27      18.628  16.283 -54.391  1.00 39.91           N  
-ATOM   2296  CZ  ARG B  27      18.190  15.624 -53.316  1.00 41.32           C  
-ATOM   2297  NH1 ARG B  27      16.898  15.348 -53.128  1.00 43.49           N  
-ATOM   2298  NH2 ARG B  27      19.067  15.241 -52.393  1.00 41.47           N  
-ATOM   2299  N   VAL B  28      19.540  14.421 -59.495  1.00 31.84           N  
-ATOM   2300  CA  VAL B  28      20.898  14.281 -59.999  1.00 32.94           C  
-ATOM   2301  C   VAL B  28      21.672  15.587 -59.911  1.00 33.57           C  
-ATOM   2302  O   VAL B  28      21.147  16.659 -60.223  1.00 34.06           O  
-ATOM   2303  CB  VAL B  28      20.897  13.811 -61.472  1.00 33.97           C  
-ATOM   2304  CG1 VAL B  28      22.311  13.770 -62.035  1.00 34.66           C  
-ATOM   2305  CG2 VAL B  28      20.236  12.446 -61.589  1.00 34.29           C  
-ATOM   2306  N   GLY B  29      22.922  15.483 -59.481  1.00 31.96           N  
-ATOM   2307  CA  GLY B  29      23.854  16.599 -59.475  1.00 32.31           C  
-ATOM   2308  C   GLY B  29      25.250  16.029 -59.618  1.00 32.65           C  
-ATOM   2309  O   GLY B  29      25.440  14.997 -60.269  1.00 32.18           O  
-ATOM   2310  N   ASN B  30      26.226  16.695 -59.013  1.00 32.91           N  
-ATOM   2311  CA  ASN B  30      27.599  16.197 -58.967  1.00 33.46           C  
-ATOM   2312  C   ASN B  30      28.104  16.285 -57.531  1.00 31.81           C  
-ATOM   2313  O   ASN B  30      27.653  17.155 -56.793  1.00 29.84           O  
-ATOM   2314  CB  ASN B  30      28.506  16.977 -59.929  1.00 35.08           C  
-ATOM   2315  CG  ASN B  30      28.006  16.937 -61.370  1.00 38.77           C  
-ATOM   2316  OD1 ASN B  30      28.466  16.131 -62.184  1.00 40.78           O  
-ATOM   2317  ND2 ASN B  30      27.041  17.803 -61.685  1.00 42.58           N  
-ATOM   2318  N   TRP B  31      29.015  15.394 -57.127  1.00 30.08           N  
-ATOM   2319  CA  TRP B  31      29.614  15.486 -55.787  1.00 30.31           C  
-ATOM   2320  C   TRP B  31      30.477  16.745 -55.717  1.00 30.86           C  
-ATOM   2321  O   TRP B  31      31.018  17.156 -56.740  1.00 30.14           O  
-ATOM   2322  CB  TRP B  31      30.435  14.245 -55.412  1.00 29.61           C  
-ATOM   2323  CG  TRP B  31      29.565  13.038 -55.261  1.00 27.49           C  
-ATOM   2324  CD1 TRP B  31      29.186  12.187 -56.240  1.00 25.95           C  
-ATOM   2325  CD2 TRP B  31      28.948  12.568 -54.056  1.00 26.48           C  
-ATOM   2326  NE1 TRP B  31      28.377  11.203 -55.731  1.00 25.75           N  
-ATOM   2327  CE2 TRP B  31      28.210  11.412 -54.390  1.00 25.16           C  
-ATOM   2328  CE3 TRP B  31      28.947  13.012 -52.730  1.00 27.85           C  
-ATOM   2329  CZ2 TRP B  31      27.471  10.688 -53.445  1.00 26.32           C  
-ATOM   2330  CZ3 TRP B  31      28.213  12.292 -51.782  1.00 28.82           C  
-ATOM   2331  CH2 TRP B  31      27.487  11.140 -52.149  1.00 28.04           C  
-ATOM   2332  N   PRO B  32      30.609  17.355 -54.519  1.00 33.62           N  
-ATOM   2333  CA  PRO B  32      31.375  18.613 -54.368  1.00 34.52           C  
-ATOM   2334  C   PRO B  32      32.799  18.567 -54.910  1.00 35.10           C  
-ATOM   2335  O   PRO B  32      33.564  17.683 -54.540  1.00 35.62           O  
-ATOM   2336  CB  PRO B  32      31.424  18.817 -52.848  1.00 34.37           C  
-ATOM   2337  CG  PRO B  32      30.295  18.064 -52.322  1.00 34.25           C  
-ATOM   2338  CD  PRO B  32      30.061  16.899 -53.227  1.00 33.17           C  
-ATOM   2339  N   GLY B  33      33.140  19.510 -55.785  1.00 36.79           N  
-ATOM   2340  CA  GLY B  33      34.502  19.639 -56.308  1.00 36.88           C  
-ATOM   2341  C   GLY B  33      34.926  18.683 -57.411  1.00 37.69           C  
-ATOM   2342  O   GLY B  33      36.071  18.751 -57.863  1.00 38.37           O  
-ATOM   2343  N   VAL B  34      34.028  17.799 -57.852  1.00 36.71           N  
-ATOM   2344  CA  VAL B  34      34.336  16.842 -58.919  1.00 35.86           C  
-ATOM   2345  C   VAL B  34      33.165  16.748 -59.887  1.00 35.36           C  
-ATOM   2346  O   VAL B  34      32.071  17.245 -59.606  1.00 35.74           O  
-ATOM   2347  CB  VAL B  34      34.680  15.426 -58.346  1.00 36.23           C  
-ATOM   2348  CG1 VAL B  34      35.950  15.485 -57.521  1.00 35.41           C  
-ATOM   2349  CG2 VAL B  34      33.522  14.868 -57.515  1.00 35.20           C  
-ATOM   2350  N   THR B  35      33.403  16.118 -61.031  1.00 35.51           N  
-ATOM   2351  CA  THR B  35      32.364  15.915 -62.042  1.00 35.62           C  
-ATOM   2352  C   THR B  35      31.579  14.615 -61.843  1.00 34.57           C  
-ATOM   2353  O   THR B  35      30.629  14.354 -62.589  1.00 35.33           O  
-ATOM   2354  CB  THR B  35      32.968  15.932 -63.465  1.00 37.26           C  
-ATOM   2355  OG1 THR B  35      33.979  14.923 -63.575  1.00 38.03           O  
-ATOM   2356  CG2 THR B  35      33.590  17.293 -63.756  1.00 38.04           C  
-ATOM   2357  N   VAL B  36      31.962  13.810 -60.848  1.00 31.47           N  
-ATOM   2358  CA  VAL B  36      31.307  12.525 -60.580  1.00 29.13           C  
-ATOM   2359  C   VAL B  36      29.850  12.769 -60.241  1.00 27.65           C  
-ATOM   2360  O   VAL B  36      29.560  13.610 -59.394  1.00 26.58           O  
-ATOM   2361  CB  VAL B  36      31.968  11.771 -59.392  1.00 28.58           C  
-ATOM   2362  CG1 VAL B  36      31.278  10.419 -59.147  1.00 27.45           C  
-ATOM   2363  CG2 VAL B  36      33.473  11.575 -59.625  1.00 28.05           C  
-ATOM   2364  N   GLU B  37      28.950  12.040 -60.902  1.00 27.99           N  
-ATOM   2365  CA  GLU B  37      27.509  12.156 -60.686  1.00 27.54           C  
-ATOM   2366  C   GLU B  37      27.117  11.849 -59.239  1.00 26.45           C  
-ATOM   2367  O   GLU B  37      27.611  10.891 -58.642  1.00 24.63           O  
-ATOM   2368  CB  GLU B  37      26.711  11.236 -61.632  1.00 28.94           C  
-ATOM   2369  CG  GLU B  37      25.217  11.082 -61.261  1.00 30.24           C  
-ATOM   2370  CD  GLU B  37      24.484   9.991 -62.034  1.00 32.60           C  
-ATOM   2371  OE1 GLU B  37      24.053  10.262 -63.175  1.00 35.40           O  
-ATOM   2372  OE2 GLU B  37      24.314   8.871 -61.492  1.00 29.56           O  
-ATOM   2373  N   ARG B  38      26.221  12.677 -58.705  1.00 24.61           N  
-ATOM   2374  CA  ARG B  38      25.654  12.505 -57.371  1.00 25.39           C  
-ATOM   2375  C   ARG B  38      24.168  12.310 -57.571  1.00 25.79           C  
-ATOM   2376  O   ARG B  38      23.457  13.233 -57.988  1.00 26.68           O  
-ATOM   2377  CB  ARG B  38      25.938  13.710 -56.483  1.00 26.21           C  
-ATOM   2378  CG  ARG B  38      25.394  13.611 -55.077  1.00 26.77           C  
-ATOM   2379  CD  ARG B  38      25.811  14.855 -54.303  1.00 28.48           C  
-ATOM   2380  NE  ARG B  38      25.460  14.795 -52.889  1.00 29.92           N  
-ATOM   2381  CZ  ARG B  38      25.790  15.725 -51.993  1.00 29.59           C  
-ATOM   2382  NH1 ARG B  38      26.480  16.806 -52.348  1.00 28.60           N  
-ATOM   2383  NH2 ARG B  38      25.421  15.575 -50.729  1.00 31.78           N  
-ATOM   2384  N   LYS B  39      23.698  11.104 -57.286  1.00 25.09           N  
-ATOM   2385  CA  LYS B  39      22.311  10.751 -57.535  1.00 24.20           C  
-ATOM   2386  C   LYS B  39      21.669  10.114 -56.327  1.00 24.01           C  
-ATOM   2387  O   LYS B  39      22.235   9.205 -55.710  1.00 23.67           O  
-ATOM   2388  CB  LYS B  39      22.233   9.805 -58.729  1.00 24.80           C  
-ATOM   2389  CG  LYS B  39      20.804   9.366 -59.093  1.00 25.97           C  
-ATOM   2390  CD  LYS B  39      20.763   8.665 -60.463  1.00 27.23           C  
-ATOM   2391  CE  LYS B  39      21.474   7.320 -60.458  1.00 28.78           C  
-ATOM   2392  NZ  LYS B  39      21.289   6.567 -61.752  1.00 29.55           N  
-ATOM   2393  N   SER B  40      20.471  10.591 -56.003  1.00 22.38           N  
-ATOM   2394  CA  SER B  40      19.669  10.012 -54.944  1.00 22.23           C  
-ATOM   2395  C   SER B  40      18.211   9.974 -55.359  1.00 22.68           C  
-ATOM   2396  O   SER B  40      17.812  10.596 -56.350  1.00 22.94           O  
-ATOM   2397  CB  SER B  40      19.815  10.803 -53.638  1.00 23.25           C  
-ATOM   2398  OG  SER B  40      19.466  12.167 -53.822  1.00 25.06           O  
-ATOM   2399  N   GLY B  41      17.438   9.227 -54.590  1.00 22.80           N  
-ATOM   2400  CA  GLY B  41      16.011   9.080 -54.817  1.00 24.80           C  
-ATOM   2401  C   GLY B  41      15.380   8.478 -53.586  1.00 25.53           C  
-ATOM   2402  O   GLY B  41      16.035   7.731 -52.843  1.00 24.90           O  
-ATOM   2403  N   LEU B  42      14.113   8.812 -53.362  1.00 24.39           N  
-ATOM   2404  CA  LEU B  42      13.354   8.265 -52.259  1.00 25.53           C  
-ATOM   2405  C   LEU B  42      12.780   6.926 -52.693  1.00 25.60           C  
-ATOM   2406  O   LEU B  42      12.518   6.721 -53.880  1.00 27.62           O  
-ATOM   2407  CB  LEU B  42      12.243   9.239 -51.840  1.00 26.85           C  
-ATOM   2408  CG  LEU B  42      12.756  10.652 -51.488  1.00 28.29           C  
-ATOM   2409  CD1 LEU B  42      11.596  11.523 -50.988  1.00 28.67           C  
-ATOM   2410  CD2 LEU B  42      13.899  10.635 -50.470  1.00 29.13           C  
-ATOM   2411  N   VAL B  43      12.594   6.020 -51.740  1.00 24.86           N  
-ATOM   2412  CA  VAL B  43      12.053   4.698 -52.024  1.00 24.38           C  
-ATOM   2413  C   VAL B  43      10.573   4.865 -52.356  1.00 28.06           C  
-ATOM   2414  O   VAL B  43       9.799   5.289 -51.503  1.00 26.99           O  
-ATOM   2415  CB  VAL B  43      12.271   3.737 -50.854  1.00 24.51           C  
-ATOM   2416  CG1 VAL B  43      11.559   2.407 -51.085  1.00 21.37           C  
-ATOM   2417  CG2 VAL B  43      13.778   3.521 -50.634  1.00 21.16           C  
-ATOM   2418  N   LYS B  44      10.200   4.537 -53.595  1.00 30.87           N  
-ATOM   2419  CA  LYS B  44       8.821   4.690 -54.084  1.00 34.33           C  
-ATOM   2420  C   LYS B  44       7.763   4.209 -53.092  1.00 35.18           C  
-ATOM   2421  O   LYS B  44       6.777   4.913 -52.860  1.00 38.00           O  
-ATOM   2422  CB  LYS B  44       8.605   3.965 -55.430  1.00 35.85           C  
-ATOM   2423  CG  LYS B  44       7.346   4.433 -56.165  1.00 37.99           C  
-ATOM   2424  CD  LYS B  44       6.951   3.523 -57.308  1.00 40.87           C  
-ATOM   2425  CE  LYS B  44       5.678   4.046 -57.984  1.00 42.01           C  
-ATOM   2426  NZ  LYS B  44       5.106   3.101 -58.996  1.00 42.38           N  
-ATOM   2427  N   LYS B  45       7.965   3.029 -52.513  1.00 34.59           N  
-ATOM   2428  CA  LYS B  45       6.977   2.448 -51.600  1.00 34.93           C  
-ATOM   2429  C   LYS B  45       7.156   2.827 -50.127  1.00 34.98           C  
-ATOM   2430  O   LYS B  45       6.431   2.313 -49.283  1.00 36.06           O  
-ATOM   2431  CB  LYS B  45       6.964   0.928 -51.754  1.00 34.94           C  
-ATOM   2432  CG  LYS B  45       6.460   0.497 -53.117  1.00 35.45           C  
-ATOM   2433  CD  LYS B  45       6.407  -1.005 -53.230  1.00 34.64           C  
-ATOM   2434  CE  LYS B  45       6.048  -1.434 -54.642  1.00 33.80           C  
-ATOM   2435  NZ  LYS B  45       6.011  -2.915 -54.761  1.00 31.24           N  
-ATOM   2436  N   ASN B  46       8.108   3.713 -49.832  1.00 34.65           N  
-ATOM   2437  CA  ASN B  46       8.348   4.213 -48.473  1.00 35.21           C  
-ATOM   2438  C   ASN B  46       9.274   5.439 -48.526  1.00 35.10           C  
-ATOM   2439  O   ASN B  46      10.492   5.305 -48.498  1.00 33.61           O  
-ATOM   2440  CB  ASN B  46       8.920   3.101 -47.585  1.00 35.14           C  
-ATOM   2441  CG  ASN B  46       9.193   3.555 -46.165  1.00 34.47           C  
-ATOM   2442  OD1 ASN B  46       9.076   4.728 -45.837  1.00 36.64           O  
-ATOM   2443  ND2 ASN B  46       9.564   2.619 -45.320  1.00 34.07           N  
-ATOM   2444  N   LYS B  47       8.691   6.636 -48.593  1.00 35.15           N  
-ATOM   2445  CA  LYS B  47       9.474   7.866 -48.811  1.00 35.24           C  
-ATOM   2446  C   LYS B  47      10.275   8.345 -47.579  1.00 34.09           C  
-ATOM   2447  O   LYS B  47      11.008   9.327 -47.693  1.00 35.30           O  
-ATOM   2448  CB  LYS B  47       8.577   8.988 -49.364  1.00 36.08           C  
-ATOM   2449  CG  LYS B  47       7.920   8.710 -50.719  1.00 36.82           C  
-ATOM   2450  CD  LYS B  47       8.789   9.047 -51.923  1.00 36.82           C  
-ATOM   2451  CE  LYS B  47       8.041   8.751 -53.231  1.00 37.46           C  
-ATOM   2452  NZ  LYS B  47       8.511   9.526 -54.423  1.00 35.74           N  
-ATOM   2453  N   ASP B  48      10.121   7.673 -46.430  1.00 32.72           N  
-ATOM   2454  CA  ASP B  48      11.036   7.804 -45.261  1.00 31.87           C  
-ATOM   2455  C   ASP B  48      12.403   7.112 -45.452  1.00 29.98           C  
-ATOM   2456  O   ASP B  48      13.277   7.205 -44.576  1.00 28.93           O  
-ATOM   2457  CB  ASP B  48      10.415   7.200 -43.992  1.00 31.54           C  
-ATOM   2458  CG  ASP B  48       9.224   7.978 -43.467  1.00 33.20           C  
-ATOM   2459  OD1 ASP B  48       9.114   9.192 -43.711  1.00 34.58           O  
-ATOM   2460  OD2 ASP B  48       8.401   7.353 -42.776  1.00 36.05           O  
-ATOM   2461  N   LEU B  49      12.579   6.389 -46.558  1.00 28.14           N  
-ATOM   2462  CA  LEU B  49      13.867   5.773 -46.904  1.00 26.14           C  
-ATOM   2463  C   LEU B  49      14.383   6.505 -48.127  1.00 24.69           C  
-ATOM   2464  O   LEU B  49      13.627   6.705 -49.086  1.00 26.07           O  
-ATOM   2465  CB  LEU B  49      13.718   4.277 -47.209  1.00 25.33           C  
-ATOM   2466  CG  LEU B  49      12.948   3.360 -46.258  1.00 24.94           C  
-ATOM   2467  CD1 LEU B  49      12.839   1.946 -46.843  1.00 25.50           C  
-ATOM   2468  CD2 LEU B  49      13.560   3.306 -44.854  1.00 25.55           C  
-ATOM   2469  N   GLU B  50      15.653   6.912 -48.086  1.00 22.83           N  
-ATOM   2470  CA  GLU B  50      16.342   7.537 -49.202  1.00 23.08           C  
-ATOM   2471  C   GLU B  50      17.456   6.615 -49.670  1.00 21.99           C  
-ATOM   2472  O   GLU B  50      18.183   6.040 -48.846  1.00 21.52           O  
-ATOM   2473  CB  GLU B  50      16.957   8.885 -48.807  1.00 23.84           C  
-ATOM   2474  CG  GLU B  50      17.709   9.576 -49.951  1.00 27.74           C  
-ATOM   2475  CD  GLU B  50      17.804  11.088 -49.785  1.00 31.54           C  
-ATOM   2476  OE1 GLU B  50      17.197  11.814 -50.601  1.00 34.02           O  
-ATOM   2477  OE2 GLU B  50      18.473  11.556 -48.844  1.00 33.44           O  
-ATOM   2478  N   ILE B  51      17.573   6.472 -50.984  1.00 19.56           N  
-ATOM   2479  CA  ILE B  51      18.677   5.731 -51.575  1.00 20.06           C  
-ATOM   2480  C   ILE B  51      19.712   6.709 -52.078  1.00 20.15           C  
-ATOM   2481  O   ILE B  51      19.448   7.517 -52.997  1.00 20.12           O  
-ATOM   2482  CB  ILE B  51      18.274   4.837 -52.757  1.00 18.55           C  
-ATOM   2483  CG1 ILE B  51      17.092   3.933 -52.402  1.00 20.37           C  
-ATOM   2484  CG2 ILE B  51      19.477   4.009 -53.181  1.00 17.60           C  
-ATOM   2485  CD1 ILE B  51      17.307   3.020 -51.208  1.00 21.76           C  
-ATOM   2486  N   GLN B  52      20.899   6.638 -51.479  1.00 19.33           N  
-ATOM   2487  CA  GLN B  52      22.038   7.372 -51.994  1.00 20.72           C  
-ATOM   2488  C   GLN B  52      22.762   6.442 -52.944  1.00 20.94           C  
-ATOM   2489  O   GLN B  52      23.416   5.489 -52.503  1.00 21.15           O  
-ATOM   2490  CB  GLN B  52      22.980   7.816 -50.870  1.00 21.04           C  
-ATOM   2491  CG  GLN B  52      24.179   8.560 -51.356  1.00 21.55           C  
-ATOM   2492  CD  GLN B  52      23.795   9.884 -52.013  1.00 23.88           C  
-ATOM   2493  OE1 GLN B  52      23.206  10.745 -51.361  1.00 22.28           O  
-ATOM   2494  NE2 GLN B  52      24.114  10.040 -53.298  1.00 21.72           N  
-ATOM   2495  N   ASP B  53      22.664   6.711 -54.243  1.00 20.15           N  
-ATOM   2496  CA  ASP B  53      23.371   5.919 -55.218  1.00 21.25           C  
-ATOM   2497  C   ASP B  53      24.841   6.310 -55.065  1.00 21.78           C  
-ATOM   2498  O   ASP B  53      25.155   7.477 -54.767  1.00 23.28           O  
-ATOM   2499  CB  ASP B  53      22.864   6.177 -56.641  1.00 21.78           C  
-ATOM   2500  CG  ASP B  53      23.463   5.218 -57.671  1.00 23.15           C  
-ATOM   2501  OD1 ASP B  53      23.546   4.004 -57.397  1.00 25.33           O  
-ATOM   2502  OD2 ASP B  53      23.863   5.686 -58.758  1.00 26.51           O  
-ATOM   2503  N   LEU B  54      25.735   5.340 -55.215  1.00 18.86           N  
-ATOM   2504  CA  LEU B  54      27.161   5.639 -55.249  1.00 19.59           C  
-ATOM   2505  C   LEU B  54      27.691   5.131 -56.588  1.00 20.44           C  
-ATOM   2506  O   LEU B  54      27.112   4.221 -57.187  1.00 20.61           O  
-ATOM   2507  CB  LEU B  54      27.900   5.039 -54.042  1.00 19.45           C  
-ATOM   2508  CG  LEU B  54      27.525   5.640 -52.681  1.00 19.06           C  
-ATOM   2509  CD1 LEU B  54      28.121   4.811 -51.531  1.00 18.32           C  
-ATOM   2510  CD2 LEU B  54      27.946   7.122 -52.568  1.00 20.14           C  
-ATOM   2511  N   PRO B  55      28.788   5.721 -57.084  1.00 20.95           N  
-ATOM   2512  CA  PRO B  55      29.291   5.265 -58.366  1.00 21.26           C  
-ATOM   2513  C   PRO B  55      29.723   3.798 -58.320  1.00 19.62           C  
-ATOM   2514  O   PRO B  55      30.177   3.312 -57.273  1.00 20.03           O  
-ATOM   2515  CB  PRO B  55      30.487   6.177 -58.626  1.00 21.69           C  
-ATOM   2516  CG  PRO B  55      30.826   6.754 -57.358  1.00 21.52           C  
-ATOM   2517  CD  PRO B  55      29.591   6.830 -56.551  1.00 21.52           C  
-ATOM   2518  N   GLY B  56      29.549   3.115 -59.448  1.00 18.28           N  
-ATOM   2519  CA  GLY B  56      29.951   1.713 -59.576  1.00 17.72           C  
-ATOM   2520  C   GLY B  56      31.461   1.605 -59.427  1.00 16.98           C  
-ATOM   2521  O   GLY B  56      32.199   2.293 -60.130  1.00 16.02           O  
-ATOM   2522  N   ILE B  57      31.918   0.768 -58.496  1.00 14.61           N  
-ATOM   2523  CA  ILE B  57      33.355   0.530 -58.278  1.00 13.77           C  
-ATOM   2524  C   ILE B  57      33.675  -0.933 -58.008  1.00 12.99           C  
-ATOM   2525  O   ILE B  57      32.791  -1.683 -57.577  1.00 11.57           O  
-ATOM   2526  CB  ILE B  57      33.907   1.386 -57.115  1.00 13.90           C  
-ATOM   2527  CG1 ILE B  57      33.172   1.112 -55.802  1.00 15.08           C  
-ATOM   2528  CG2 ILE B  57      33.839   2.889 -57.488  1.00 14.74           C  
-ATOM   2529  CD1 ILE B  57      33.728   1.861 -54.644  1.00 13.52           C  
-ATOM   2530  N   TYR B  58      34.935  -1.321 -58.261  1.00 14.18           N  
-ATOM   2531  CA  TYR B  58      35.440  -2.666 -57.985  1.00 13.34           C  
-ATOM   2532  C   TYR B  58      36.166  -2.782 -56.632  1.00 14.34           C  
-ATOM   2533  O   TYR B  58      36.357  -3.885 -56.129  1.00 15.52           O  
-ATOM   2534  CB  TYR B  58      36.400  -3.116 -59.085  1.00 15.10           C  
-ATOM   2535  CG  TYR B  58      35.725  -3.320 -60.416  1.00 14.71           C  
-ATOM   2536  CD1 TYR B  58      34.944  -4.452 -60.645  1.00 18.04           C  
-ATOM   2537  CD2 TYR B  58      35.847  -2.379 -61.441  1.00 16.54           C  
-ATOM   2538  CE1 TYR B  58      34.304  -4.653 -61.852  1.00 18.35           C  
-ATOM   2539  CE2 TYR B  58      35.208  -2.571 -62.657  1.00 18.44           C  
-ATOM   2540  CZ  TYR B  58      34.443  -3.705 -62.856  1.00 17.72           C  
-ATOM   2541  OH  TYR B  58      33.810  -3.898 -64.058  1.00 19.34           O  
-ATOM   2542  N   SER B  59      36.594  -1.653 -56.066  1.00 14.03           N  
-ATOM   2543  CA  SER B  59      37.386  -1.643 -54.845  1.00 15.71           C  
-ATOM   2544  C   SER B  59      37.325  -0.233 -54.251  1.00 17.44           C  
-ATOM   2545  O   SER B  59      36.754   0.667 -54.870  1.00 19.80           O  
-ATOM   2546  CB  SER B  59      38.830  -2.022 -55.187  1.00 15.27           C  
-ATOM   2547  OG  SER B  59      39.590  -2.320 -54.027  1.00 16.29           O  
-ATOM   2548  N  AMET B  60      37.939  -0.009 -53.100  0.50 16.98           N  
-ATOM   2549  N  BMET B  60      37.856  -0.086 -53.034  0.50 17.45           N  
-ATOM   2550  CA AMET B  60      38.095   1.356 -52.618  0.50 16.37           C  
-ATOM   2551  CA BMET B  60      37.872   1.175 -52.279  0.50 17.18           C  
-ATOM   2552  C  AMET B  60      39.582   1.697 -52.568  0.50 16.51           C  
-ATOM   2553  C  BMET B  60      39.324   1.619 -52.099  0.50 17.99           C  
-ATOM   2554  O  AMET B  60      40.136   1.876 -51.475  0.50 15.82           O  
-ATOM   2555  O  BMET B  60      39.872   1.684 -50.995  0.50 16.33           O  
-ATOM   2556  CB AMET B  60      37.387   1.550 -51.268  0.50 16.32           C  
-ATOM   2557  CB BMET B  60      37.179   1.024 -50.924  0.50 17.02           C  
-ATOM   2558  CG AMET B  60      35.855   1.495 -51.396  0.50 15.83           C  
-ATOM   2559  CG BMET B  60      35.708   0.640 -51.030  0.50 16.13           C  
-ATOM   2560  SD AMET B  60      34.935   1.895 -49.893  0.50 16.38           S  
-ATOM   2561  SD BMET B  60      34.912   0.533 -49.421  0.50 14.74           S  
-ATOM   2562  CE AMET B  60      35.353   0.517 -48.834  0.50 13.57           C  
-ATOM   2563  CE BMET B  60      34.951   2.233 -48.872  0.50 15.79           C  
-ATOM   2564  N  ASER B  61      40.214   1.786 -53.746  0.60 17.58           N  
-ATOM   2565  N  BSER B  61      39.924   1.931 -53.254  0.40 18.54           N  
-ATOM   2566  CA ASER B  61      41.601   2.185 -53.828  0.60 18.03           C  
-ATOM   2567  CA BSER B  61      41.340   2.300 -53.411  0.40 19.46           C  
-ATOM   2568  C  ASER B  61      41.600   3.715 -53.867  0.60 19.54           C  
-ATOM   2569  C  BSER B  61      41.515   3.806 -53.678  0.40 20.45           C  
-ATOM   2570  O  ASER B  61      40.563   4.344 -54.082  0.60 18.60           O  
-ATOM   2571  O  BSER B  61      40.520   4.496 -53.905  0.40 19.69           O  
-ATOM   2572  CB ASER B  61      42.275   1.584 -55.071  0.60 18.17           C  
-ATOM   2573  CB BSER B  61      41.944   1.487 -54.563  0.40 20.46           C  
-ATOM   2574  OG ASER B  61      42.008   2.386 -56.193  0.60 16.69           O  
-ATOM   2575  OG BSER B  61      41.838   0.097 -54.317  0.40 19.93           O  
-ATOM   2576  N   PRO B  62      42.768   4.325 -53.663  1.00 20.84           N  
-ATOM   2577  CA  PRO B  62      42.897   5.774 -53.783  1.00 24.35           C  
-ATOM   2578  C   PRO B  62      43.064   6.285 -55.227  1.00 27.65           C  
-ATOM   2579  O   PRO B  62      43.297   7.479 -55.409  1.00 30.29           O  
-ATOM   2580  CB  PRO B  62      44.141   6.068 -52.921  1.00 24.22           C  
-ATOM   2581  CG  PRO B  62      44.952   4.853 -52.962  1.00 22.66           C  
-ATOM   2582  CD  PRO B  62      44.077   3.699 -53.385  1.00 22.40           C  
-ATOM   2583  N   TYR B  63      42.902   5.417 -56.228  1.00 29.63           N  
-ATOM   2584  CA  TYR B  63      43.288   5.717 -57.616  1.00 31.16           C  
-ATOM   2585  C   TYR B  63      42.199   6.195 -58.590  1.00 30.83           C  
-ATOM   2586  O   TYR B  63      42.504   6.393 -59.763  1.00 33.16           O  
-ATOM   2587  CB  TYR B  63      44.034   4.508 -58.199  1.00 32.42           C  
-ATOM   2588  CG  TYR B  63      45.232   4.137 -57.346  1.00 34.99           C  
-ATOM   2589  CD1 TYR B  63      46.238   5.076 -57.085  1.00 36.23           C  
-ATOM   2590  CD2 TYR B  63      45.360   2.857 -56.790  1.00 36.39           C  
-ATOM   2591  CE1 TYR B  63      47.338   4.756 -56.301  1.00 37.29           C  
-ATOM   2592  CE2 TYR B  63      46.465   2.530 -56.005  1.00 37.03           C  
-ATOM   2593  CZ  TYR B  63      47.445   3.485 -55.762  1.00 37.20           C  
-ATOM   2594  OH  TYR B  63      48.542   3.181 -54.983  1.00 38.92           O  
-ATOM   2595  N   SER B  64      40.954   6.371 -58.158  1.00 27.85           N  
-ATOM   2596  CA  SER B  64      39.969   6.981 -59.058  1.00 26.35           C  
-ATOM   2597  C   SER B  64      39.037   7.906 -58.302  1.00 25.45           C  
-ATOM   2598  O   SER B  64      38.811   7.708 -57.106  1.00 24.94           O  
-ATOM   2599  CB  SER B  64      39.183   5.937 -59.869  1.00 27.25           C  
-ATOM   2600  OG  SER B  64      38.094   5.382 -59.156  1.00 23.49           O  
-ATOM   2601  N   PRO B  65      38.492   8.923 -58.995  1.00 24.45           N  
-ATOM   2602  CA  PRO B  65      37.543   9.841 -58.354  1.00 24.63           C  
-ATOM   2603  C   PRO B  65      36.295   9.145 -57.830  1.00 23.07           C  
-ATOM   2604  O   PRO B  65      35.775   9.516 -56.781  1.00 22.17           O  
-ATOM   2605  CB  PRO B  65      37.172  10.814 -59.486  1.00 25.64           C  
-ATOM   2606  CG  PRO B  65      38.317  10.742 -60.428  1.00 25.55           C  
-ATOM   2607  CD  PRO B  65      38.737   9.304 -60.400  1.00 26.10           C  
-ATOM   2608  N   GLU B  66      35.836   8.128 -58.550  1.00 22.73           N  
-ATOM   2609  CA  GLU B  66      34.630   7.382 -58.144  1.00 21.90           C  
-ATOM   2610  C   GLU B  66      34.867   6.631 -56.826  1.00 19.67           C  
-ATOM   2611  O   GLU B  66      34.011   6.648 -55.927  1.00 18.65           O  
-ATOM   2612  CB  GLU B  66      34.184   6.410 -59.241  1.00 22.00           C  
-ATOM   2613  CG  GLU B  66      33.596   7.059 -60.501  1.00 24.98           C  
-ATOM   2614  CD  GLU B  66      34.621   7.697 -61.435  1.00 27.67           C  
-ATOM   2615  OE1 GLU B  66      35.840   7.446 -61.290  1.00 28.19           O  
-ATOM   2616  OE2 GLU B  66      34.200   8.466 -62.327  1.00 30.63           O  
-ATOM   2617  N  AGLU B  67      36.018   5.966 -56.727  0.50 18.97           N  
-ATOM   2618  N  BGLU B  67      36.018   5.972 -56.715  0.50 19.34           N  
-ATOM   2619  CA AGLU B  67      36.419   5.271 -55.505  0.50 18.65           C  
-ATOM   2620  CA BGLU B  67      36.376   5.262 -55.488  0.50 19.29           C  
-ATOM   2621  C  AGLU B  67      36.555   6.221 -54.314  0.50 19.20           C  
-ATOM   2622  C  BGLU B  67      36.588   6.206 -54.299  0.50 19.57           C  
-ATOM   2623  O  AGLU B  67      36.120   5.905 -53.201  0.50 17.29           O  
-ATOM   2624  O  BGLU B  67      36.232   5.869 -53.165  0.50 17.79           O  
-ATOM   2625  CB AGLU B  67      37.736   4.537 -55.729  0.50 18.69           C  
-ATOM   2626  CB BGLU B  67      37.591   4.370 -55.740  0.50 19.68           C  
-ATOM   2627  CG AGLU B  67      37.631   3.391 -56.716  0.50 18.54           C  
-ATOM   2628  CG BGLU B  67      37.269   3.290 -56.765  0.50 20.20           C  
-ATOM   2629  CD AGLU B  67      38.984   2.827 -57.078  0.50 19.04           C  
-ATOM   2630  CD BGLU B  67      38.438   2.391 -57.090  0.50 21.23           C  
-ATOM   2631  OE1AGLU B  67      39.360   1.789 -56.498  0.50 19.56           O  
-ATOM   2632  OE1BGLU B  67      39.371   2.284 -56.265  0.50 21.26           O  
-ATOM   2633  OE2AGLU B  67      39.680   3.428 -57.919  0.50 19.86           O  
-ATOM   2634  OE2BGLU B  67      38.415   1.783 -58.178  0.50 23.87           O  
-ATOM   2635  N   LYS B  68      37.147   7.390 -54.554  1.00 19.31           N  
-ATOM   2636  CA  LYS B  68      37.314   8.392 -53.491  1.00 19.54           C  
-ATOM   2637  C   LYS B  68      35.951   8.923 -53.001  1.00 18.46           C  
-ATOM   2638  O   LYS B  68      35.721   9.046 -51.789  1.00 17.07           O  
-ATOM   2639  CB  LYS B  68      38.226   9.541 -53.935  1.00 20.64           C  
-ATOM   2640  CG  LYS B  68      38.606  10.426 -52.764  1.00 23.60           C  
-ATOM   2641  CD  LYS B  68      39.641  11.500 -53.120  1.00 26.07           C  
-ATOM   2642  CE  LYS B  68      40.009  12.311 -51.896  1.00 27.14           C  
-ATOM   2643  NZ  LYS B  68      38.832  13.032 -51.330  1.00 26.48           N  
-ATOM   2644  N   VAL B  69      35.047   9.210 -53.935  1.00 18.86           N  
-ATOM   2645  CA  VAL B  69      33.678   9.631 -53.587  1.00 18.20           C  
-ATOM   2646  C   VAL B  69      33.014   8.599 -52.678  1.00 17.58           C  
-ATOM   2647  O   VAL B  69      32.438   8.940 -51.631  1.00 15.24           O  
-ATOM   2648  CB  VAL B  69      32.813   9.889 -54.860  1.00 19.62           C  
-ATOM   2649  CG1 VAL B  69      31.315   9.848 -54.553  1.00 18.63           C  
-ATOM   2650  CG2 VAL B  69      33.186  11.249 -55.472  1.00 18.97           C  
-ATOM   2651  N   ALA B  70      33.107   7.334 -53.074  1.00 17.31           N  
-ATOM   2652  CA  ALA B  70      32.418   6.269 -52.344  1.00 17.12           C  
-ATOM   2653  C   ALA B  70      32.999   6.111 -50.931  1.00 17.27           C  
-ATOM   2654  O   ALA B  70      32.267   6.058 -49.934  1.00 16.67           O  
-ATOM   2655  CB  ALA B  70      32.498   4.966 -53.126  1.00 17.73           C  
-ATOM   2656  N   ARG B  71      34.323   6.036 -50.847  1.00 16.48           N  
-ATOM   2657  CA  ARG B  71      34.997   5.936 -49.557  1.00 17.94           C  
-ATOM   2658  C   ARG B  71      34.688   7.116 -48.626  1.00 17.58           C  
-ATOM   2659  O   ARG B  71      34.351   6.914 -47.467  1.00 18.62           O  
-ATOM   2660  CB  ARG B  71      36.513   5.866 -49.749  1.00 18.68           C  
-ATOM   2661  CG  ARG B  71      37.266   5.702 -48.432  1.00 20.61           C  
-ATOM   2662  CD  ARG B  71      38.723   6.045 -48.566  1.00 20.32           C  
-ATOM   2663  NE  ARG B  71      39.460   5.129 -49.432  1.00 18.74           N  
-ATOM   2664  CZ  ARG B  71      40.791   5.063 -49.480  1.00 21.18           C  
-ATOM   2665  NH1 ARG B  71      41.540   5.847 -48.700  1.00 19.68           N  
-ATOM   2666  NH2 ARG B  71      41.382   4.194 -50.293  1.00 20.15           N  
-ATOM   2667  N   ASP B  72      34.830   8.338 -49.130  1.00 18.08           N  
-ATOM   2668  CA  ASP B  72      34.569   9.532 -48.312  1.00 18.84           C  
-ATOM   2669  C   ASP B  72      33.144   9.525 -47.758  1.00 18.31           C  
-ATOM   2670  O   ASP B  72      32.910   9.804 -46.568  1.00 18.10           O  
-ATOM   2671  CB  ASP B  72      34.863  10.820 -49.098  1.00 19.96           C  
-ATOM   2672  CG  ASP B  72      36.343  11.038 -49.338  1.00 21.70           C  
-ATOM   2673  OD1 ASP B  72      37.170  10.266 -48.816  1.00 22.07           O  
-ATOM   2674  OD2 ASP B  72      36.691  11.988 -50.064  1.00 24.27           O  
-ATOM   2675  N   TYR B  73      32.183   9.176 -48.602  1.00 18.40           N  
-ATOM   2676  CA  TYR B  73      30.807   9.113 -48.139  1.00 16.99           C  
-ATOM   2677  C   TYR B  73      30.595   8.046 -47.055  1.00 17.32           C  
-ATOM   2678  O   TYR B  73      29.985   8.327 -46.011  1.00 15.43           O  
-ATOM   2679  CB  TYR B  73      29.844   8.901 -49.306  1.00 19.27           C  
-ATOM   2680  CG  TYR B  73      28.432   8.782 -48.833  1.00 18.87           C  
-ATOM   2681  CD1 TYR B  73      27.693   9.915 -48.495  1.00 20.95           C  
-ATOM   2682  CD2 TYR B  73      27.842   7.537 -48.691  1.00 20.04           C  
-ATOM   2683  CE1 TYR B  73      26.398   9.805 -48.047  1.00 21.76           C  
-ATOM   2684  CE2 TYR B  73      26.544   7.412 -48.243  1.00 21.12           C  
-ATOM   2685  CZ  TYR B  73      25.830   8.541 -47.929  1.00 23.43           C  
-ATOM   2686  OH  TYR B  73      24.552   8.379 -47.490  1.00 26.68           O  
-ATOM   2687  N   LEU B  74      31.102   6.841 -47.298  1.00 16.30           N  
-ATOM   2688  CA  LEU B  74      30.926   5.734 -46.357  1.00 17.83           C  
-ATOM   2689  C   LEU B  74      31.633   5.956 -45.019  1.00 18.19           C  
-ATOM   2690  O   LEU B  74      31.114   5.527 -43.984  1.00 19.14           O  
-ATOM   2691  CB  LEU B  74      31.334   4.397 -47.002  1.00 17.64           C  
-ATOM   2692  CG  LEU B  74      30.424   3.906 -48.141  1.00 18.72           C  
-ATOM   2693  CD1 LEU B  74      30.960   2.610 -48.759  1.00 18.28           C  
-ATOM   2694  CD2 LEU B  74      28.978   3.725 -47.678  1.00 16.82           C  
-ATOM   2695  N  ALEU B  75      32.784   6.632 -45.039  0.70 18.50           N  
-ATOM   2696  N  BLEU B  75      32.793   6.614 -45.037  0.30 18.72           N  
-ATOM   2697  CA ALEU B  75      33.541   6.916 -43.810  0.70 18.96           C  
-ATOM   2698  CA BLEU B  75      33.541   6.910 -43.808  0.30 19.10           C  
-ATOM   2699  C  ALEU B  75      33.034   8.149 -43.058  0.70 20.32           C  
-ATOM   2700  C  BLEU B  75      33.049   8.159 -43.068  0.30 20.15           C  
-ATOM   2701  O  ALEU B  75      33.440   8.383 -41.910  0.70 20.52           O  
-ATOM   2702  O  BLEU B  75      33.492   8.421 -41.945  0.30 20.32           O  
-ATOM   2703  CB ALEU B  75      35.044   7.041 -44.102  0.70 19.54           C  
-ATOM   2704  CB BLEU B  75      35.041   7.014 -44.102  0.30 19.13           C  
-ATOM   2705  CG ALEU B  75      35.726   5.720 -44.465  0.70 19.34           C  
-ATOM   2706  CG BLEU B  75      35.724   5.644 -44.187  0.30 18.76           C  
-ATOM   2707  CD1ALEU B  75      37.163   5.991 -44.900  0.70 22.03           C  
-ATOM   2708  CD1BLEU B  75      35.034   4.752 -45.210  0.30 18.00           C  
-ATOM   2709  CD2ALEU B  75      35.689   4.729 -43.301  0.70 19.44           C  
-ATOM   2710  CD2BLEU B  75      37.209   5.792 -44.503  0.30 19.52           C  
-ATOM   2711  N   SER B  76      32.141   8.920 -43.684  1.00 20.81           N  
-ATOM   2712  CA  SER B  76      31.514  10.082 -43.040  1.00 22.21           C  
-ATOM   2713  C   SER B  76      30.463   9.683 -42.002  1.00 23.60           C  
-ATOM   2714  O   SER B  76      30.021  10.523 -41.225  1.00 26.00           O  
-ATOM   2715  CB  SER B  76      30.853  11.005 -44.074  1.00 22.71           C  
-ATOM   2716  OG  SER B  76      29.645  10.461 -44.600  1.00 22.41           O  
-ATOM   2717  N   GLN B  77      30.060   8.416 -42.012  1.00 22.76           N  
-ATOM   2718  CA  GLN B  77      29.049   7.853 -41.113  1.00 25.40           C  
-ATOM   2719  C   GLN B  77      27.634   8.451 -41.327  1.00 26.93           C  
-ATOM   2720  O   GLN B  77      26.763   8.321 -40.456  1.00 29.46           O  
-ATOM   2721  CB  GLN B  77      29.503   7.909 -39.634  1.00 24.80           C  
-ATOM   2722  CG  GLN B  77      30.948   7.414 -39.387  1.00 25.14           C  
-ATOM   2723  CD  GLN B  77      31.257   7.107 -37.920  1.00 24.15           C  
-ATOM   2724  OE1 GLN B  77      30.689   6.182 -37.337  1.00 21.58           O  
-ATOM   2725  NE2 GLN B  77      32.178   7.885 -37.322  1.00 23.22           N  
-ATOM   2726  N   ARG B  78      27.403   9.075 -42.486  1.00 25.38           N  
-ATOM   2727  CA  ARG B  78      26.079   9.604 -42.839  1.00 25.62           C  
-ATOM   2728  C   ARG B  78      25.127   8.503 -43.314  1.00 22.71           C  
-ATOM   2729  O   ARG B  78      23.913   8.599 -43.116  1.00 22.71           O  
-ATOM   2730  CB  ARG B  78      26.177  10.691 -43.893  1.00 27.95           C  
-ATOM   2731  CG  ARG B  78      26.701  11.998 -43.308  1.00 33.38           C  
-ATOM   2732  CD  ARG B  78      26.559  13.114 -44.312  1.00 37.46           C  
-ATOM   2733  NE  ARG B  78      27.430  12.861 -45.453  1.00 41.39           N  
-ATOM   2734  CZ  ARG B  78      28.645  13.378 -45.640  1.00 44.40           C  
-ATOM   2735  NH1 ARG B  78      29.198  14.224 -44.765  1.00 46.04           N  
-ATOM   2736  NH2 ARG B  78      29.319  13.042 -46.739  1.00 45.53           N  
-ATOM   2737  N   ALA B  79      25.669   7.461 -43.935  1.00 19.72           N  
-ATOM   2738  CA  ALA B  79      24.859   6.319 -44.329  1.00 18.21           C  
-ATOM   2739  C   ALA B  79      24.402   5.552 -43.094  1.00 17.78           C  
-ATOM   2740  O   ALA B  79      25.206   5.290 -42.190  1.00 18.24           O  
-ATOM   2741  CB  ALA B  79      25.660   5.391 -45.240  1.00 18.84           C  
-ATOM   2742  N   ASP B  80      23.120   5.201 -43.055  1.00 16.20           N  
-ATOM   2743  CA  ASP B  80      22.598   4.317 -42.026  1.00 17.32           C  
-ATOM   2744  C   ASP B  80      22.886   2.859 -42.388  1.00 17.04           C  
-ATOM   2745  O   ASP B  80      23.095   2.051 -41.502  1.00 18.14           O  
-ATOM   2746  CB  ASP B  80      21.094   4.508 -41.849  1.00 17.29           C  
-ATOM   2747  CG  ASP B  80      20.751   5.872 -41.285  1.00 21.85           C  
-ATOM   2748  OD1 ASP B  80      21.127   6.118 -40.121  1.00 25.84           O  
-ATOM   2749  OD2 ASP B  80      20.122   6.683 -42.006  1.00 21.50           O  
-ATOM   2750  N   SER B  81      22.911   2.556 -43.686  1.00 16.02           N  
-ATOM   2751  CA  SER B  81      23.007   1.184 -44.194  1.00 15.89           C  
-ATOM   2752  C   SER B  81      23.698   1.184 -45.536  1.00 15.28           C  
-ATOM   2753  O   SER B  81      23.642   2.167 -46.260  1.00 13.72           O  
-ATOM   2754  CB  SER B  81      21.594   0.597 -44.345  1.00 17.22           C  
-ATOM   2755  OG  SER B  81      21.512  -0.401 -45.362  1.00 17.51           O  
-ATOM   2756  N   ILE B  82      24.369   0.081 -45.857  1.00 14.96           N  
-ATOM   2757  CA  ILE B  82      24.886  -0.139 -47.199  1.00 14.06           C  
-ATOM   2758  C   ILE B  82      24.051  -1.270 -47.816  1.00 13.31           C  
-ATOM   2759  O   ILE B  82      23.926  -2.346 -47.229  1.00 13.58           O  
-ATOM   2760  CB  ILE B  82      26.355  -0.589 -47.172  1.00 13.86           C  
-ATOM   2761  CG1 ILE B  82      27.277   0.545 -46.707  1.00 14.57           C  
-ATOM   2762  CG2 ILE B  82      26.806  -1.095 -48.577  1.00 12.50           C  
-ATOM   2763  CD1 ILE B  82      28.729   0.085 -46.478  1.00 14.17           C  
-ATOM   2764  N   LEU B  83      23.502  -1.017 -49.000  1.00 13.88           N  
-ATOM   2765  CA  LEU B  83      22.805  -2.019 -49.787  1.00 12.95           C  
-ATOM   2766  C   LEU B  83      23.745  -2.324 -50.946  1.00 14.39           C  
-ATOM   2767  O   LEU B  83      23.840  -1.561 -51.913  1.00 13.94           O  
-ATOM   2768  CB  LEU B  83      21.436  -1.500 -50.255  1.00 13.67           C  
-ATOM   2769  CG  LEU B  83      20.575  -2.458 -51.089  1.00 15.59           C  
-ATOM   2770  CD1 LEU B  83      20.501  -3.836 -50.491  1.00 18.59           C  
-ATOM   2771  CD2 LEU B  83      19.156  -1.865 -51.281  1.00 13.99           C  
-ATOM   2772  N   ASN B  84      24.442  -3.455 -50.832  1.00 14.18           N  
-ATOM   2773  CA  ASN B  84      25.482  -3.882 -51.758  1.00 12.56           C  
-ATOM   2774  C   ASN B  84      24.875  -4.781 -52.833  1.00 13.03           C  
-ATOM   2775  O   ASN B  84      24.437  -5.893 -52.521  1.00 11.73           O  
-ATOM   2776  CB  ASN B  84      26.552  -4.622 -50.950  1.00 13.10           C  
-ATOM   2777  CG  ASN B  84      27.710  -5.180 -51.778  1.00 12.64           C  
-ATOM   2778  OD1 ASN B  84      28.359  -6.133 -51.340  1.00 12.34           O  
-ATOM   2779  ND2 ASN B  84      28.002  -4.591 -52.930  1.00 13.13           N  
-ATOM   2780  N   VAL B  85      24.855  -4.276 -54.065  1.00 12.98           N  
-ATOM   2781  CA  VAL B  85      24.365  -4.984 -55.245  1.00 12.73           C  
-ATOM   2782  C   VAL B  85      25.521  -5.850 -55.766  1.00 12.53           C  
-ATOM   2783  O   VAL B  85      26.568  -5.335 -56.141  1.00 12.73           O  
-ATOM   2784  CB  VAL B  85      23.898  -4.049 -56.369  1.00 13.74           C  
-ATOM   2785  CG1 VAL B  85      23.391  -4.853 -57.567  1.00 13.10           C  
-ATOM   2786  CG2 VAL B  85      22.797  -3.075 -55.879  1.00 11.94           C  
-ATOM   2787  N   VAL B  86      25.297  -7.161 -55.766  1.00 12.71           N  
-ATOM   2788  CA  VAL B  86      26.295  -8.180 -56.118  1.00 13.45           C  
-ATOM   2789  C   VAL B  86      25.789  -9.009 -57.296  1.00 14.92           C  
-ATOM   2790  O   VAL B  86      24.684  -9.582 -57.252  1.00 15.78           O  
-ATOM   2791  CB  VAL B  86      26.559  -9.087 -54.906  1.00 11.99           C  
-ATOM   2792  CG1 VAL B  86      27.401 -10.353 -55.254  1.00 12.79           C  
-ATOM   2793  CG2 VAL B  86      27.230  -8.286 -53.790  1.00 12.90           C  
-ATOM   2794  N   ASP B  87      26.594  -9.077 -58.356  1.00 13.63           N  
-ATOM   2795  CA  ASP B  87      26.276  -9.916 -59.527  1.00 13.94           C  
-ATOM   2796  C   ASP B  87      26.481 -11.413 -59.199  1.00 14.43           C  
-ATOM   2797  O   ASP B  87      27.617 -11.883 -59.074  1.00 14.85           O  
-ATOM   2798  CB  ASP B  87      27.118  -9.459 -60.718  1.00 14.63           C  
-ATOM   2799  CG  ASP B  87      26.904 -10.290 -61.972  1.00 15.78           C  
-ATOM   2800  OD1 ASP B  87      26.076 -11.234 -62.014  1.00 17.45           O  
-ATOM   2801  OD2 ASP B  87      27.620  -9.983 -62.936  1.00 16.22           O  
-ATOM   2802  N   ALA B  88      25.373 -12.140 -59.050  1.00 14.25           N  
-ATOM   2803  CA  ALA B  88      25.385 -13.575 -58.697  1.00 15.42           C  
-ATOM   2804  C   ALA B  88      26.174 -14.434 -59.675  1.00 16.55           C  
-ATOM   2805  O   ALA B  88      26.725 -15.458 -59.282  1.00 17.27           O  
-ATOM   2806  CB  ALA B  88      23.955 -14.103 -58.591  1.00 14.32           C  
-ATOM   2807  N   THR B  89      26.234 -14.012 -60.935  1.00 16.21           N  
-ATOM   2808  CA  THR B  89      26.948 -14.761 -61.979  1.00 17.38           C  
-ATOM   2809  C   THR B  89      28.475 -14.574 -61.965  1.00 18.25           C  
-ATOM   2810  O   THR B  89      29.202 -15.288 -62.674  1.00 18.21           O  
-ATOM   2811  CB  THR B  89      26.396 -14.410 -63.387  1.00 15.95           C  
-ATOM   2812  OG1 THR B  89      26.804 -13.096 -63.782  1.00 15.36           O  
-ATOM   2813  CG2 THR B  89      24.884 -14.475 -63.421  1.00 14.91           C  
-ATOM   2814  N   ASN B  90      28.953 -13.618 -61.168  1.00 16.83           N  
-ATOM   2815  CA  ASN B  90      30.374 -13.293 -61.054  1.00 16.76           C  
-ATOM   2816  C   ASN B  90      30.709 -13.059 -59.572  1.00 15.97           C  
-ATOM   2817  O   ASN B  90      31.296 -12.049 -59.193  1.00 15.20           O  
-ATOM   2818  CB  ASN B  90      30.648 -12.050 -61.894  1.00 17.49           C  
-ATOM   2819  CG  ASN B  90      32.121 -11.778 -62.093  1.00 18.08           C  
-ATOM   2820  OD1 ASN B  90      32.944 -12.687 -61.995  1.00 21.23           O  
-ATOM   2821  ND2 ASN B  90      32.469 -10.524 -62.376  1.00 19.36           N  
-ATOM   2822  N   LEU B  91      30.337 -14.020 -58.747  1.00 16.68           N  
-ATOM   2823  CA  LEU B  91      30.303 -13.823 -57.285  1.00 16.95           C  
-ATOM   2824  C   LEU B  91      31.644 -13.481 -56.636  1.00 16.33           C  
-ATOM   2825  O   LEU B  91      31.739 -12.480 -55.935  1.00 16.84           O  
-ATOM   2826  CB  LEU B  91      29.655 -15.039 -56.605  1.00 17.19           C  
-ATOM   2827  CG  LEU B  91      29.408 -14.915 -55.103  1.00 17.35           C  
-ATOM   2828  CD1 LEU B  91      28.508 -13.689 -54.750  1.00 15.68           C  
-ATOM   2829  CD2 LEU B  91      28.813 -16.208 -54.581  1.00 18.74           C  
-ATOM   2830  N   GLU B  92      32.679 -14.284 -56.851  1.00 16.90           N  
-ATOM   2831  CA  GLU B  92      33.973 -14.015 -56.206  1.00 18.89           C  
-ATOM   2832  C   GLU B  92      34.508 -12.626 -56.538  1.00 18.40           C  
-ATOM   2833  O   GLU B  92      34.965 -11.904 -55.655  1.00 18.48           O  
-ATOM   2834  CB  GLU B  92      35.012 -15.087 -56.585  1.00 20.80           C  
-ATOM   2835  CG  GLU B  92      36.478 -14.703 -56.280  1.00 25.11           C  
-ATOM   2836  CD  GLU B  92      37.465 -15.859 -56.463  1.00 30.08           C  
-ATOM   2837  OE1 GLU B  92      37.040 -16.968 -56.872  1.00 28.15           O  
-ATOM   2838  OE2 GLU B  92      38.675 -15.635 -56.196  1.00 34.13           O  
-ATOM   2839  N   ARG B  93      34.459 -12.258 -57.814  1.00 16.22           N  
-ATOM   2840  CA  ARG B  93      34.947 -10.959 -58.251  1.00 15.22           C  
-ATOM   2841  C   ARG B  93      34.180  -9.802 -57.612  1.00 14.01           C  
-ATOM   2842  O   ARG B  93      34.786  -8.820 -57.230  1.00 13.91           O  
-ATOM   2843  CB  ARG B  93      34.897 -10.836 -59.776  1.00 16.87           C  
-ATOM   2844  N   ASN B  94      32.865  -9.921 -57.496  1.00 13.92           N  
-ATOM   2845  CA  ASN B  94      32.047  -8.884 -56.861  1.00 13.33           C  
-ATOM   2846  C   ASN B  94      32.276  -8.774 -55.353  1.00 14.22           C  
-ATOM   2847  O   ASN B  94      32.234  -7.668 -54.798  1.00 13.17           O  
-ATOM   2848  CB  ASN B  94      30.542  -9.110 -57.126  1.00 13.83           C  
-ATOM   2849  CG  ASN B  94      30.113  -8.709 -58.516  1.00 14.36           C  
-ATOM   2850  OD1 ASN B  94      29.249  -7.848 -58.680  1.00 13.10           O  
-ATOM   2851  ND2 ASN B  94      30.693  -9.336 -59.526  1.00 13.99           N  
-ATOM   2852  N   LEU B  95      32.525  -9.908 -54.691  1.00 14.20           N  
-ATOM   2853  CA  LEU B  95      32.736  -9.912 -53.244  1.00 14.79           C  
-ATOM   2854  C   LEU B  95      34.057  -9.243 -52.793  1.00 14.09           C  
-ATOM   2855  O   LEU B  95      34.192  -8.942 -51.620  1.00 13.90           O  
-ATOM   2856  CB  LEU B  95      32.610 -11.321 -52.651  1.00 14.31           C  
-ATOM   2857  CG  LEU B  95      31.237 -12.003 -52.678  1.00 15.15           C  
-ATOM   2858  CD1 LEU B  95      31.362 -13.452 -52.200  1.00 15.24           C  
-ATOM   2859  CD2 LEU B  95      30.185 -11.258 -51.887  1.00 14.70           C  
-ATOM   2860  N   TYR B  96      35.012  -9.007 -53.695  1.00 13.41           N  
-ATOM   2861  CA  TYR B  96      36.209  -8.223 -53.352  1.00 13.03           C  
-ATOM   2862  C   TYR B  96      35.836  -6.862 -52.757  1.00 13.10           C  
-ATOM   2863  O   TYR B  96      36.319  -6.472 -51.682  1.00 12.13           O  
-ATOM   2864  CB  TYR B  96      37.087  -8.046 -54.581  1.00 12.27           C  
-ATOM   2865  CG  TYR B  96      38.457  -7.469 -54.327  1.00 14.06           C  
-ATOM   2866  CD1 TYR B  96      39.471  -8.248 -53.777  1.00 14.67           C  
-ATOM   2867  CD2 TYR B  96      38.762  -6.157 -54.667  1.00 13.17           C  
-ATOM   2868  CE1 TYR B  96      40.733  -7.731 -53.565  1.00 14.50           C  
-ATOM   2869  CE2 TYR B  96      40.027  -5.640 -54.444  1.00 15.02           C  
-ATOM   2870  CZ  TYR B  96      40.998  -6.425 -53.893  1.00 15.77           C  
-ATOM   2871  OH  TYR B  96      42.255  -5.891 -53.688  1.00 19.35           O  
-ATOM   2872  N   LEU B  97      34.947  -6.148 -53.442  1.00 12.05           N  
-ATOM   2873  CA  LEU B  97      34.420  -4.898 -52.898  1.00 12.39           C  
-ATOM   2874  C   LEU B  97      33.652  -5.139 -51.596  1.00 11.73           C  
-ATOM   2875  O   LEU B  97      33.819  -4.396 -50.636  1.00 11.52           O  
-ATOM   2876  CB  LEU B  97      33.523  -4.185 -53.916  1.00 13.01           C  
-ATOM   2877  CG  LEU B  97      32.825  -2.917 -53.419  1.00 13.36           C  
-ATOM   2878  CD1 LEU B  97      33.854  -1.811 -53.176  1.00 13.90           C  
-ATOM   2879  CD2 LEU B  97      31.727  -2.474 -54.424  1.00 14.57           C  
-ATOM   2880  N   THR B  98      32.811  -6.163 -51.577  1.00 11.73           N  
-ATOM   2881  CA  THR B  98      31.960  -6.462 -50.402  1.00 12.32           C  
-ATOM   2882  C   THR B  98      32.756  -6.541 -49.105  1.00 13.63           C  
-ATOM   2883  O   THR B  98      32.362  -5.967 -48.097  1.00 10.98           O  
-ATOM   2884  CB  THR B  98      31.161  -7.752 -50.620  1.00 13.02           C  
-ATOM   2885  OG1 THR B  98      30.441  -7.660 -51.856  1.00 12.90           O  
-ATOM   2886  CG2 THR B  98      30.184  -8.015 -49.461  1.00 13.16           C  
-ATOM   2887  N   THR B  99      33.888  -7.248 -49.118  1.00 12.69           N  
-ATOM   2888  CA  THR B  99      34.717  -7.336 -47.930  1.00 13.43           C  
-ATOM   2889  C   THR B  99      35.142  -5.960 -47.411  1.00 13.70           C  
-ATOM   2890  O   THR B  99      35.173  -5.735 -46.198  1.00 12.05           O  
-ATOM   2891  CB  THR B  99      35.975  -8.226 -48.158  1.00 13.91           C  
-ATOM   2892  OG1 THR B  99      36.822  -7.645 -49.177  1.00 14.82           O  
-ATOM   2893  CG2 THR B  99      35.539  -9.644 -48.537  1.00 14.36           C  
-ATOM   2894  N   GLN B 100      35.447  -5.034 -48.318  1.00 14.04           N  
-ATOM   2895  CA  GLN B 100      35.876  -3.693 -47.934  1.00 14.14           C  
-ATOM   2896  C   GLN B 100      34.706  -2.867 -47.387  1.00 14.52           C  
-ATOM   2897  O   GLN B 100      34.859  -2.086 -46.426  1.00 13.19           O  
-ATOM   2898  CB  GLN B 100      36.528  -2.983 -49.132  1.00 16.51           C  
-ATOM   2899  CG  GLN B 100      37.777  -3.690 -49.660  1.00 16.56           C  
-ATOM   2900  CD  GLN B 100      38.322  -3.080 -50.947  1.00 15.75           C  
-ATOM   2901  OE1 GLN B 100      38.666  -1.914 -50.976  1.00 20.25           O  
-ATOM   2902  NE2 GLN B 100      38.407  -3.876 -52.013  1.00 17.87           N  
-ATOM   2903  N   LEU B 101      33.538  -3.052 -48.000  1.00 11.50           N  
-ATOM   2904  CA  LEU B 101      32.329  -2.384 -47.535  1.00 13.14           C  
-ATOM   2905  C   LEU B 101      31.992  -2.780 -46.098  1.00 13.28           C  
-ATOM   2906  O   LEU B 101      31.677  -1.925 -45.272  1.00 12.55           O  
-ATOM   2907  CB  LEU B 101      31.153  -2.700 -48.449  1.00 11.52           C  
-ATOM   2908  CG  LEU B 101      31.222  -2.164 -49.874  1.00 11.67           C  
-ATOM   2909  CD1 LEU B 101      30.059  -2.739 -50.725  1.00  9.28           C  
-ATOM   2910  CD2 LEU B 101      31.233  -0.633 -49.860  1.00 13.27           C  
-ATOM   2911  N   ILE B 102      32.082  -4.077 -45.799  1.00 12.25           N  
-ATOM   2912  CA  ILE B 102      31.791  -4.566 -44.442  1.00 13.07           C  
-ATOM   2913  C   ILE B 102      32.730  -3.914 -43.426  1.00 13.57           C  
-ATOM   2914  O   ILE B 102      32.296  -3.507 -42.352  1.00 13.22           O  
-ATOM   2915  CB  ILE B 102      31.885  -6.108 -44.373  1.00 13.29           C  
-ATOM   2916  CG1 ILE B 102      30.775  -6.757 -45.218  1.00 14.12           C  
-ATOM   2917  CG2 ILE B 102      31.765  -6.622 -42.935  1.00 13.02           C  
-ATOM   2918  CD1 ILE B 102      30.953  -8.274 -45.417  1.00 10.00           C  
-ATOM   2919  N   GLU B 103      34.007  -3.809 -43.792  1.00 15.85           N  
-ATOM   2920  CA  GLU B 103      35.036  -3.197 -42.943  1.00 14.19           C  
-ATOM   2921  C   GLU B 103      34.805  -1.727 -42.606  1.00 14.43           C  
-ATOM   2922  O   GLU B 103      35.370  -1.254 -41.631  1.00 14.68           O  
-ATOM   2923  CB  GLU B 103      36.424  -3.413 -43.551  1.00 15.30           C  
-ATOM   2924  CG  GLU B 103      36.843  -4.881 -43.508  1.00 13.76           C  
-ATOM   2925  CD  GLU B 103      37.918  -5.254 -44.511  1.00 16.33           C  
-ATOM   2926  OE1 GLU B 103      38.385  -4.398 -45.287  1.00 16.72           O  
-ATOM   2927  OE2 GLU B 103      38.297  -6.438 -44.532  1.00 15.88           O  
-ATOM   2928  N   THR B 104      33.986  -1.004 -43.377  1.00 13.56           N  
-ATOM   2929  CA  THR B 104      33.620   0.368 -43.019  1.00 14.80           C  
-ATOM   2930  C   THR B 104      32.817   0.460 -41.719  1.00 15.20           C  
-ATOM   2931  O   THR B 104      32.714   1.536 -41.153  1.00 15.83           O  
-ATOM   2932  CB  THR B 104      32.759   1.077 -44.096  1.00 13.65           C  
-ATOM   2933  OG1 THR B 104      31.490   0.401 -44.210  1.00 13.54           O  
-ATOM   2934  CG2 THR B 104      33.466   1.118 -45.448  1.00 13.53           C  
-ATOM   2935  N   GLY B 105      32.219  -0.643 -41.278  1.00 14.94           N  
-ATOM   2936  CA  GLY B 105      31.384  -0.654 -40.085  1.00 15.61           C  
-ATOM   2937  C   GLY B 105      29.979  -0.092 -40.262  1.00 14.66           C  
-ATOM   2938  O   GLY B 105      29.250   0.022 -39.272  1.00 14.90           O  
-ATOM   2939  N   ILE B 106      29.605   0.284 -41.486  1.00 13.51           N  
-ATOM   2940  CA  ILE B 106      28.209   0.579 -41.823  1.00 14.66           C  
-ATOM   2941  C   ILE B 106      27.611  -0.781 -42.212  1.00 14.36           C  
-ATOM   2942  O   ILE B 106      28.125  -1.426 -43.135  1.00 12.20           O  
-ATOM   2943  CB  ILE B 106      28.061   1.582 -42.973  1.00 14.55           C  
-ATOM   2944  CG1 ILE B 106      28.840   2.878 -42.700  1.00 17.96           C  
-ATOM   2945  CG2 ILE B 106      26.547   1.914 -43.246  1.00 14.93           C  
-ATOM   2946  CD1 ILE B 106      28.437   3.619 -41.476  1.00 18.75           C  
-ATOM   2947  N   PRO B 107      26.551  -1.227 -41.519  1.00 14.41           N  
-ATOM   2948  CA  PRO B 107      26.044  -2.570 -41.821  1.00 15.01           C  
-ATOM   2949  C   PRO B 107      25.621  -2.769 -43.279  1.00 14.00           C  
-ATOM   2950  O   PRO B 107      24.902  -1.946 -43.830  1.00 12.99           O  
-ATOM   2951  CB  PRO B 107      24.848  -2.717 -40.878  1.00 14.90           C  
-ATOM   2952  CG  PRO B 107      25.210  -1.861 -39.714  1.00 14.67           C  
-ATOM   2953  CD  PRO B 107      25.841  -0.643 -40.361  1.00 15.05           C  
-ATOM   2954  N   VAL B 108      26.107  -3.859 -43.854  1.00 12.50           N  
-ATOM   2955  CA  VAL B 108      25.856  -4.250 -45.232  1.00 11.64           C  
-ATOM   2956  C   VAL B 108      24.689  -5.244 -45.327  1.00 12.26           C  
-ATOM   2957  O   VAL B 108      24.595  -6.160 -44.511  1.00 12.31           O  
-ATOM   2958  CB  VAL B 108      27.129  -4.923 -45.842  1.00 11.30           C  
-ATOM   2959  CG1 VAL B 108      26.817  -5.617 -47.171  1.00 12.82           C  
-ATOM   2960  CG2 VAL B 108      28.249  -3.903 -46.023  1.00 13.45           C  
-ATOM   2961  N   THR B 109      23.819  -5.016 -46.318  1.00 10.95           N  
-ATOM   2962  CA  THR B 109      22.793  -5.951 -46.768  1.00 12.15           C  
-ATOM   2963  C   THR B 109      23.108  -6.196 -48.243  1.00 11.30           C  
-ATOM   2964  O   THR B 109      23.382  -5.250 -48.985  1.00 12.23           O  
-ATOM   2965  CB  THR B 109      21.374  -5.372 -46.595  1.00 12.93           C  
-ATOM   2966  OG1 THR B 109      21.118  -5.149 -45.201  1.00 13.44           O  
-ATOM   2967  CG2 THR B 109      20.286  -6.290 -47.206  1.00 11.54           C  
-ATOM   2968  N   ILE B 110      23.093  -7.460 -48.663  1.00 11.55           N  
-ATOM   2969  CA  ILE B 110      23.416  -7.812 -50.051  1.00 10.47           C  
-ATOM   2970  C   ILE B 110      22.162  -8.060 -50.883  1.00 10.95           C  
-ATOM   2971  O   ILE B 110      21.305  -8.867 -50.498  1.00 13.27           O  
-ATOM   2972  CB  ILE B 110      24.347  -9.041 -50.135  1.00 10.61           C  
-ATOM   2973  CG1 ILE B 110      25.745  -8.657 -49.629  1.00 12.91           C  
-ATOM   2974  CG2 ILE B 110      24.423  -9.562 -51.582  1.00 12.92           C  
-ATOM   2975  CD1 ILE B 110      26.752  -9.785 -49.559  1.00 10.78           C  
-ATOM   2976  N   ALA B 111      22.067  -7.355 -52.008  1.00 12.73           N  
-ATOM   2977  CA  ALA B 111      21.110  -7.682 -53.059  1.00 13.68           C  
-ATOM   2978  C   ALA B 111      21.886  -8.593 -54.000  1.00 14.10           C  
-ATOM   2979  O   ALA B 111      22.756  -8.146 -54.746  1.00 14.97           O  
-ATOM   2980  CB  ALA B 111      20.645  -6.438 -53.786  1.00 14.00           C  
-ATOM   2981  N   LEU B 112      21.581  -9.884 -53.946  1.00 14.96           N  
-ATOM   2982  CA  LEU B 112      22.266 -10.881 -54.754  1.00 14.54           C  
-ATOM   2983  C   LEU B 112      21.533 -10.891 -56.101  1.00 14.60           C  
-ATOM   2984  O   LEU B 112      20.567 -11.642 -56.285  1.00 13.54           O  
-ATOM   2985  CB  LEU B 112      22.240 -12.239 -54.055  1.00 14.33           C  
-ATOM   2986  CG  LEU B 112      23.001 -13.367 -54.754  1.00 15.01           C  
-ATOM   2987  CD1 LEU B 112      24.457 -13.022 -54.872  1.00 15.74           C  
-ATOM   2988  CD2 LEU B 112      22.805 -14.654 -53.960  1.00 15.24           C  
-ATOM   2989  N   ASN B 113      21.998 -10.019 -57.000  1.00 14.25           N  
-ATOM   2990  CA  ASN B 113      21.277  -9.669 -58.243  1.00 15.11           C  
-ATOM   2991  C   ASN B 113      21.628 -10.597 -59.415  1.00 15.75           C  
-ATOM   2992  O   ASN B 113      22.553 -11.403 -59.301  1.00 15.01           O  
-ATOM   2993  CB  ASN B 113      21.470  -8.175 -58.572  1.00 15.95           C  
-ATOM   2994  CG  ASN B 113      20.433  -7.640 -59.569  1.00 15.64           C  
-ATOM   2995  OD1 ASN B 113      19.229  -7.821 -59.392  1.00 16.14           O  
-ATOM   2996  ND2 ASN B 113      20.912  -7.016 -60.648  1.00 15.75           N  
-ATOM   2997  N  AMET B 114      20.860 -10.471 -60.501  0.50 16.25           N  
-ATOM   2998  N  BMET B 114      20.894 -10.493 -60.525  0.50 15.93           N  
-ATOM   2999  CA AMET B 114      20.961 -11.321 -61.697  0.50 18.54           C  
-ATOM   3000  CA BMET B 114      21.068 -11.376 -61.696  0.50 17.94           C  
-ATOM   3001  C  AMET B 114      20.767 -12.798 -61.340  0.50 18.03           C  
-ATOM   3002  C  BMET B 114      20.737 -12.829 -61.369  0.50 17.62           C  
-ATOM   3003  O  AMET B 114      21.398 -13.676 -61.931  0.50 19.39           O  
-ATOM   3004  O  BMET B 114      21.251 -13.737 -62.025  0.50 18.90           O  
-ATOM   3005  CB AMET B 114      22.277 -11.065 -62.441  0.50 19.00           C  
-ATOM   3006  CB BMET B 114      22.498 -11.333 -62.231  0.50 17.98           C  
-ATOM   3007  CG AMET B 114      22.342  -9.663 -63.074  0.50 21.25           C  
-ATOM   3008  CG BMET B 114      23.012  -9.947 -62.512  0.50 19.45           C  
-ATOM   3009  SD AMET B 114      24.000  -9.102 -63.542  0.50 20.78           S  
-ATOM   3010  SD BMET B 114      22.587  -9.417 -64.184  0.50 18.28           S  
-ATOM   3011  CE AMET B 114      23.678  -7.412 -64.022  0.50 19.34           C  
-ATOM   3012  CE BMET B 114      23.339  -7.793 -64.135  0.50 17.92           C  
-ATOM   3013  N   ILE B 115      19.890 -13.051 -60.365  1.00 17.70           N  
-ATOM   3014  CA  ILE B 115      19.583 -14.419 -59.913  1.00 18.36           C  
-ATOM   3015  C   ILE B 115      18.891 -15.248 -61.011  1.00 18.44           C  
-ATOM   3016  O   ILE B 115      19.109 -16.452 -61.102  1.00 18.29           O  
-ATOM   3017  CB  ILE B 115      18.782 -14.436 -58.560  1.00 17.51           C  
-ATOM   3018  CG1 ILE B 115      19.079 -15.720 -57.774  1.00 18.35           C  
-ATOM   3019  CG2 ILE B 115      17.283 -14.197 -58.752  1.00 17.13           C  
-ATOM   3020  CD1 ILE B 115      20.392 -15.701 -57.059  1.00 19.13           C  
-ATOM   3021  N   ASP B 116      18.077 -14.596 -61.833  1.00 20.13           N  
-ATOM   3022  CA  ASP B 116      17.421 -15.245 -62.978  1.00 21.88           C  
-ATOM   3023  C   ASP B 116      18.400 -15.820 -64.013  1.00 23.69           C  
-ATOM   3024  O   ASP B 116      18.091 -16.809 -64.683  1.00 24.48           O  
-ATOM   3025  CB  ASP B 116      16.466 -14.276 -63.660  1.00 21.09           C  
-ATOM   3026  CG  ASP B 116      17.186 -13.072 -64.237  1.00 22.09           C  
-ATOM   3027  OD1 ASP B 116      17.693 -12.270 -63.423  1.00 19.15           O  
-ATOM   3028  OD2 ASP B 116      17.247 -12.923 -65.483  1.00 20.18           O  
-ATOM   3029  N   VAL B 117      19.567 -15.199 -64.142  1.00 25.55           N  
-ATOM   3030  CA  VAL B 117      20.606 -15.645 -65.073  1.00 27.24           C  
-ATOM   3031  C   VAL B 117      21.311 -16.913 -64.562  1.00 29.66           C  
-ATOM   3032  O   VAL B 117      21.761 -17.737 -65.365  1.00 27.51           O  
-ATOM   3033  CB  VAL B 117      21.654 -14.525 -65.336  1.00 26.68           C  
-ATOM   3034  CG1 VAL B 117      22.644 -14.933 -66.417  1.00 27.93           C  
-ATOM   3035  CG2 VAL B 117      20.970 -13.215 -65.722  1.00 26.03           C  
-ATOM   3036  N  ALEU B 118      21.388 -17.057 -63.239  0.50 30.15           N  
-ATOM   3037  N  BLEU B 118      21.410 -17.068 -63.238  0.50 30.73           N  
-ATOM   3038  CA ALEU B 118      22.040 -18.193 -62.595  0.50 31.07           C  
-ATOM   3039  CA BLEU B 118      22.059 -18.239 -62.635  0.50 32.07           C  
-ATOM   3040  C  ALEU B 118      21.488 -19.557 -63.048  0.50 32.74           C  
-ATOM   3041  C  BLEU B 118      21.489 -19.576 -63.097  0.50 33.29           C  
-ATOM   3042  O  ALEU B 118      22.267 -20.469 -63.316  0.50 32.46           O  
-ATOM   3043  O  BLEU B 118      22.253 -20.487 -63.410  0.50 32.85           O  
-ATOM   3044  CB ALEU B 118      21.928 -18.028 -61.076  0.50 30.74           C  
-ATOM   3045  CB BLEU B 118      21.986 -18.187 -61.110  0.50 32.57           C  
-ATOM   3046  CG ALEU B 118      23.086 -18.539 -60.221  0.50 29.84           C  
-ATOM   3047  CG BLEU B 118      22.916 -17.195 -60.432  0.50 32.78           C  
-ATOM   3048  CD1ALEU B 118      24.400 -17.916 -60.652  0.50 28.96           C  
-ATOM   3049  CD1BLEU B 118      22.656 -17.209 -58.937  0.50 33.62           C  
-ATOM   3050  CD2ALEU B 118      22.806 -18.260 -58.746  0.50 27.93           C  
-ATOM   3051  CD2BLEU B 118      24.358 -17.550 -60.736  0.50 33.17           C  
-ATOM   3052  N   ASP B 119      20.165 -19.702 -63.139  1.00 35.25           N  
-ATOM   3053  CA  ASP B 119      19.549 -20.966 -63.616  1.00 38.25           C  
-ATOM   3054  C   ASP B 119      20.044 -21.329 -65.017  1.00 38.72           C  
-ATOM   3055  O   ASP B 119      20.491 -22.454 -65.253  1.00 39.24           O  
-ATOM   3056  CB  ASP B 119      18.018 -20.921 -63.619  1.00 39.97           C  
-ATOM   3057  CG  ASP B 119      17.402 -22.128 -64.313  1.00 42.80           C  
-ATOM   3058  OD1 ASP B 119      17.654 -23.264 -63.858  1.00 44.36           O  
-ATOM   3059  OD2 ASP B 119      16.671 -21.945 -65.314  1.00 46.59           O  
-ATOM   3060  N   GLY B 120      19.996 -20.356 -65.926  1.00 39.49           N  
-ATOM   3061  CA  GLY B 120      20.461 -20.540 -67.301  1.00 39.63           C  
-ATOM   3062  C   GLY B 120      21.883 -21.051 -67.431  1.00 39.91           C  
-ATOM   3063  O   GLY B 120      22.222 -21.686 -68.433  1.00 41.32           O  
-ATOM   3064  N   GLN B 121      22.715 -20.771 -66.427  1.00 38.38           N  
-ATOM   3065  CA  GLN B 121      24.101 -21.234 -66.393  1.00 37.31           C  
-ATOM   3066  C   GLN B 121      24.272 -22.532 -65.600  1.00 37.00           C  
-ATOM   3067  O   GLN B 121      25.404 -22.977 -65.398  1.00 36.88           O  
-ATOM   3068  CB  GLN B 121      24.995 -20.148 -65.790  1.00 36.77           C  
-ATOM   3069  CG  GLN B 121      24.934 -18.819 -66.537  1.00 35.68           C  
-ATOM   3070  CD  GLN B 121      25.759 -17.738 -65.883  1.00 36.13           C  
-ATOM   3071  OE1 GLN B 121      26.093 -17.816 -64.697  1.00 35.31           O  
-ATOM   3072  NE2 GLN B 121      26.091 -16.714 -66.653  1.00 36.74           N  
-ATOM   3073  N   GLY B 122      23.164 -23.135 -65.163  1.00 36.72           N  
-ATOM   3074  CA  GLY B 122      23.192 -24.338 -64.321  1.00 36.74           C  
-ATOM   3075  C   GLY B 122      23.885 -24.141 -62.981  1.00 36.39           C  
-ATOM   3076  O   GLY B 122      24.646 -25.011 -62.533  1.00 38.06           O  
-ATOM   3077  N   LYS B 123      23.627 -23.003 -62.335  1.00 34.22           N  
-ATOM   3078  CA  LYS B 123      24.285 -22.672 -61.072  1.00 32.03           C  
-ATOM   3079  C   LYS B 123      23.300 -22.305 -59.975  1.00 29.10           C  
-ATOM   3080  O   LYS B 123      22.156 -21.916 -60.236  1.00 27.31           O  
-ATOM   3081  CB  LYS B 123      25.274 -21.528 -61.264  1.00 33.13           C  
-ATOM   3082  CG  LYS B 123      26.408 -21.831 -62.230  1.00 34.92           C  
-ATOM   3083  CD  LYS B 123      27.298 -20.621 -62.381  1.00 36.25           C  
-ATOM   3084  CE  LYS B 123      28.604 -20.948 -63.067  1.00 37.15           C  
-ATOM   3085  NZ  LYS B 123      29.533 -19.795 -62.923  1.00 36.99           N  
-ATOM   3086  N   LYS B 124      23.778 -22.453 -58.744  1.00 26.36           N  
-ATOM   3087  CA  LYS B 124      23.020 -22.154 -57.549  1.00 25.81           C  
-ATOM   3088  C   LYS B 124      23.940 -21.486 -56.542  1.00 22.66           C  
-ATOM   3089  O   LYS B 124      25.159 -21.711 -56.545  1.00 22.10           O  
-ATOM   3090  CB  LYS B 124      22.461 -23.420 -56.895  1.00 28.75           C  
-ATOM   3091  CG  LYS B 124      21.608 -24.300 -57.795  1.00 31.87           C  
-ATOM   3092  CD  LYS B 124      20.821 -25.368 -57.004  1.00 34.57           C  
-ATOM   3093  CE  LYS B 124      21.686 -26.208 -56.070  1.00 36.09           C  
-ATOM   3094  NZ  LYS B 124      20.971 -27.428 -55.583  1.00 37.00           N  
-ATOM   3095  N   ILE B 125      23.332 -20.660 -55.697  1.00 19.03           N  
-ATOM   3096  CA  ILE B 125      23.974 -20.072 -54.544  1.00 17.95           C  
-ATOM   3097  C   ILE B 125      23.040 -20.317 -53.356  1.00 17.87           C  
-ATOM   3098  O   ILE B 125      21.864 -19.960 -53.383  1.00 18.33           O  
-ATOM   3099  CB  ILE B 125      24.206 -18.564 -54.718  1.00 17.82           C  
-ATOM   3100  CG1 ILE B 125      25.169 -18.305 -55.885  1.00 17.38           C  
-ATOM   3101  CG2 ILE B 125      24.731 -17.976 -53.402  1.00 16.43           C  
-ATOM   3102  CD1 ILE B 125      25.312 -16.823 -56.297  1.00 16.95           C  
-ATOM   3103  N   ASN B 126      23.573 -20.939 -52.314  1.00 17.59           N  
-ATOM   3104  CA  ASN B 126      22.822 -21.162 -51.093  1.00 17.03           C  
-ATOM   3105  C   ASN B 126      22.858 -19.843 -50.315  1.00 16.86           C  
-ATOM   3106  O   ASN B 126      23.889 -19.472 -49.748  1.00 14.13           O  
-ATOM   3107  CB  ASN B 126      23.427 -22.328 -50.316  1.00 16.85           C  
-ATOM   3108  CG  ASN B 126      22.646 -22.658 -49.079  1.00 20.02           C  
-ATOM   3109  OD1 ASN B 126      22.304 -21.771 -48.284  1.00 19.16           O  
-ATOM   3110  ND2 ASN B 126      22.361 -23.940 -48.896  1.00 17.99           N  
-ATOM   3111  N   VAL B 127      21.732 -19.131 -50.297  1.00 16.41           N  
-ATOM   3112  CA  VAL B 127      21.705 -17.789 -49.718  1.00 16.87           C  
-ATOM   3113  C   VAL B 127      21.921 -17.802 -48.208  1.00 16.80           C  
-ATOM   3114  O   VAL B 127      22.585 -16.915 -47.679  1.00 15.06           O  
-ATOM   3115  CB  VAL B 127      20.398 -17.047 -50.088  1.00 17.78           C  
-ATOM   3116  CG1 VAL B 127      20.249 -15.785 -49.304  1.00 21.47           C  
-ATOM   3117  CG2 VAL B 127      20.383 -16.745 -51.581  1.00 18.69           C  
-ATOM   3118  N   ASP B 128      21.376 -18.804 -47.522  1.00 14.23           N  
-ATOM   3119  CA  ASP B 128      21.634 -18.958 -46.081  1.00 14.79           C  
-ATOM   3120  C   ASP B 128      23.117 -19.050 -45.745  1.00 15.22           C  
-ATOM   3121  O   ASP B 128      23.590 -18.359 -44.838  1.00 14.45           O  
-ATOM   3122  CB  ASP B 128      20.962 -20.214 -45.544  1.00 14.30           C  
-ATOM   3123  CG  ASP B 128      21.193 -20.396 -44.066  1.00 16.08           C  
-ATOM   3124  OD1 ASP B 128      20.856 -19.481 -43.295  1.00 15.02           O  
-ATOM   3125  OD2 ASP B 128      21.737 -21.449 -43.683  1.00 18.82           O  
-ATOM   3126  N  ALYS B 129      23.838 -19.901 -46.474  0.50 16.06           N  
-ATOM   3127  N  BLYS B 129      23.836 -19.897 -46.477  0.50 16.36           N  
-ATOM   3128  CA ALYS B 129      25.275 -20.089 -46.252  0.50 16.68           C  
-ATOM   3129  CA BLYS B 129      25.272 -20.087 -46.263  0.50 17.22           C  
-ATOM   3130  C  ALYS B 129      26.096 -18.857 -46.637  0.50 16.45           C  
-ATOM   3131  C  BLYS B 129      26.094 -18.855 -46.637  0.50 16.76           C  
-ATOM   3132  O  ALYS B 129      27.046 -18.516 -45.937  0.50 17.12           O  
-ATOM   3133  O  BLYS B 129      27.038 -18.514 -45.931  0.50 17.41           O  
-ATOM   3134  CB ALYS B 129      25.788 -21.329 -46.990  0.50 17.42           C  
-ATOM   3135  CB BLYS B 129      25.767 -21.311 -47.030  0.50 18.33           C  
-ATOM   3136  CG ALYS B 129      25.212 -22.632 -46.464  0.50 17.17           C  
-ATOM   3137  CG BLYS B 129      25.212 -22.603 -46.478  0.50 18.79           C  
-ATOM   3138  CD ALYS B 129      25.899 -23.850 -47.067  0.50 17.29           C  
-ATOM   3139  CD BLYS B 129      25.643 -23.807 -47.286  0.50 19.74           C  
-ATOM   3140  CE ALYS B 129      25.198 -25.151 -46.684  0.50 16.43           C  
-ATOM   3141  CE BLYS B 129      25.211 -25.097 -46.603  0.50 19.85           C  
-ATOM   3142  NZ ALYS B 129      25.044 -25.318 -45.213  0.50 15.91           N  
-ATOM   3143  NZ BLYS B 129      25.522 -26.291 -47.425  0.50 21.28           N  
-ATOM   3144  N   LEU B 130      25.746 -18.195 -47.740  1.00 17.04           N  
-ATOM   3145  CA  LEU B 130      26.433 -16.952 -48.133  1.00 16.53           C  
-ATOM   3146  C   LEU B 130      26.317 -15.920 -47.004  1.00 14.58           C  
-ATOM   3147  O   LEU B 130      27.309 -15.343 -46.582  1.00 15.04           O  
-ATOM   3148  CB  LEU B 130      25.887 -16.380 -49.454  1.00 15.19           C  
-ATOM   3149  CG  LEU B 130      26.622 -15.157 -50.036  1.00 15.09           C  
-ATOM   3150  CD1 LEU B 130      28.089 -15.461 -50.308  1.00 15.65           C  
-ATOM   3151  CD2 LEU B 130      25.946 -14.639 -51.326  1.00 15.31           C  
-ATOM   3152  N   SER B 131      25.091 -15.723 -46.513  1.00 14.21           N  
-ATOM   3153  CA  SER B 131      24.803 -14.797 -45.417  1.00 14.93           C  
-ATOM   3154  C   SER B 131      25.534 -15.179 -44.127  1.00 14.84           C  
-ATOM   3155  O   SER B 131      26.122 -14.326 -43.448  1.00 14.08           O  
-ATOM   3156  CB  SER B 131      23.296 -14.779 -45.153  1.00 14.46           C  
-ATOM   3157  OG  SER B 131      22.923 -13.981 -44.038  1.00 16.51           O  
-ATOM   3158  N   TYR B 132      25.487 -16.466 -43.796  1.00 15.34           N  
-ATOM   3159  CA  TYR B 132      26.109 -16.968 -42.569  1.00 16.37           C  
-ATOM   3160  C   TYR B 132      27.608 -16.692 -42.554  1.00 17.08           C  
-ATOM   3161  O   TYR B 132      28.131 -16.180 -41.566  1.00 17.52           O  
-ATOM   3162  CB  TYR B 132      25.824 -18.467 -42.396  1.00 17.68           C  
-ATOM   3163  CG  TYR B 132      26.545 -19.076 -41.236  1.00 18.57           C  
-ATOM   3164  CD1 TYR B 132      26.174 -18.772 -39.929  1.00 24.19           C  
-ATOM   3165  CD2 TYR B 132      27.607 -19.943 -41.433  1.00 23.46           C  
-ATOM   3166  CE1 TYR B 132      26.842 -19.322 -38.842  1.00 23.95           C  
-ATOM   3167  CE2 TYR B 132      28.283 -20.506 -40.350  1.00 25.94           C  
-ATOM   3168  CZ  TYR B 132      27.885 -20.186 -39.062  1.00 25.50           C  
-ATOM   3169  OH  TYR B 132      28.534 -20.729 -37.987  1.00 30.47           O  
-ATOM   3170  N   HIS B 133      28.291 -17.012 -43.648  1.00 17.56           N  
-ATOM   3171  CA  HIS B 133      29.747 -16.851 -43.714  1.00 17.57           C  
-ATOM   3172  C   HIS B 133      30.208 -15.412 -43.937  1.00 19.01           C  
-ATOM   3173  O   HIS B 133      31.302 -15.047 -43.498  1.00 19.97           O  
-ATOM   3174  CB  HIS B 133      30.338 -17.781 -44.760  1.00 19.23           C  
-ATOM   3175  CG  HIS B 133      30.308 -19.212 -44.341  1.00 20.26           C  
-ATOM   3176  ND1 HIS B 133      29.447 -20.131 -44.896  1.00 20.36           N  
-ATOM   3177  CD2 HIS B 133      31.020 -19.881 -43.404  1.00 20.50           C  
-ATOM   3178  CE1 HIS B 133      29.635 -21.302 -44.320  1.00 18.10           C  
-ATOM   3179  NE2 HIS B 133      30.587 -21.180 -43.415  1.00 21.08           N  
-ATOM   3180  N   LEU B 134      29.390 -14.607 -44.603  1.00 16.35           N  
-ATOM   3181  CA  LEU B 134      29.685 -13.174 -44.756  1.00 16.72           C  
-ATOM   3182  C   LEU B 134      29.265 -12.356 -43.532  1.00 16.74           C  
-ATOM   3183  O   LEU B 134      29.748 -11.236 -43.353  1.00 18.07           O  
-ATOM   3184  CB  LEU B 134      29.040 -12.612 -46.028  1.00 14.46           C  
-ATOM   3185  CG  LEU B 134      29.647 -13.049 -47.365  1.00 15.67           C  
-ATOM   3186  CD1 LEU B 134      28.853 -12.424 -48.521  1.00 16.03           C  
-ATOM   3187  CD2 LEU B 134      31.143 -12.675 -47.488  1.00 17.15           C  
-ATOM   3188  N   GLY B 135      28.389 -12.903 -42.691  1.00 15.07           N  
-ATOM   3189  CA  GLY B 135      27.827 -12.156 -41.558  1.00 16.57           C  
-ATOM   3190  C   GLY B 135      26.971 -10.958 -41.944  1.00 16.47           C  
-ATOM   3191  O   GLY B 135      26.938  -9.945 -41.224  1.00 16.45           O  
-ATOM   3192  N   VAL B 136      26.283 -11.056 -43.087  1.00 15.09           N  
-ATOM   3193  CA  VAL B 136      25.367 -10.016 -43.547  1.00 12.64           C  
-ATOM   3194  C   VAL B 136      24.070 -10.629 -44.082  1.00 13.27           C  
-ATOM   3195  O   VAL B 136      24.080 -11.757 -44.567  1.00 13.98           O  
-ATOM   3196  CB  VAL B 136      25.970  -9.163 -44.676  1.00 13.43           C  
-ATOM   3197  CG1 VAL B 136      27.278  -8.477 -44.211  1.00 11.41           C  
-ATOM   3198  CG2 VAL B 136      26.181 -10.001 -45.952  1.00 11.79           C  
-ATOM   3199  N   PRO B 137      22.958  -9.895 -43.990  1.00 14.03           N  
-ATOM   3200  CA  PRO B 137      21.733 -10.350 -44.658  1.00 14.58           C  
-ATOM   3201  C   PRO B 137      21.924 -10.425 -46.169  1.00 14.83           C  
-ATOM   3202  O   PRO B 137      22.590  -9.558 -46.723  1.00 14.48           O  
-ATOM   3203  CB  PRO B 137      20.735  -9.238 -44.350  1.00 14.47           C  
-ATOM   3204  CG  PRO B 137      21.255  -8.557 -43.140  1.00 15.85           C  
-ATOM   3205  CD  PRO B 137      22.725  -8.683 -43.180  1.00 13.55           C  
-ATOM   3206  N   VAL B 138      21.342 -11.439 -46.805  1.00 13.73           N  
-ATOM   3207  CA  VAL B 138      21.388 -11.610 -48.272  1.00 14.29           C  
-ATOM   3208  C   VAL B 138      19.985 -11.889 -48.785  1.00 14.29           C  
-ATOM   3209  O   VAL B 138      19.275 -12.737 -48.229  1.00 15.35           O  
-ATOM   3210  CB  VAL B 138      22.314 -12.773 -48.694  1.00 13.67           C  
-ATOM   3211  CG1 VAL B 138      22.287 -13.014 -50.238  1.00 14.77           C  
-ATOM   3212  CG2 VAL B 138      23.734 -12.526 -48.218  1.00 15.23           C  
-ATOM   3213  N   VAL B 139      19.580 -11.166 -49.822  1.00 15.82           N  
-ATOM   3214  CA  VAL B 139      18.285 -11.365 -50.481  1.00 14.76           C  
-ATOM   3215  C   VAL B 139      18.554 -11.523 -51.979  1.00 15.78           C  
-ATOM   3216  O   VAL B 139      19.216 -10.675 -52.582  1.00 14.77           O  
-ATOM   3217  CB  VAL B 139      17.312 -10.198 -50.228  1.00 15.09           C  
-ATOM   3218  CG1 VAL B 139      15.946 -10.453 -50.890  1.00 13.16           C  
-ATOM   3219  CG2 VAL B 139      17.122  -9.955 -48.741  1.00 13.71           C  
-ATOM   3220  N   ALA B 140      18.057 -12.609 -52.569  1.00 15.48           N  
-ATOM   3221  CA  ALA B 140      18.218 -12.831 -54.007  1.00 15.55           C  
-ATOM   3222  C   ALA B 140      17.279 -11.880 -54.739  1.00 15.03           C  
-ATOM   3223  O   ALA B 140      16.104 -11.781 -54.372  1.00 15.65           O  
-ATOM   3224  CB  ALA B 140      17.917 -14.283 -54.362  1.00 14.21           C  
-ATOM   3225  N   THR B 141      17.792 -11.168 -55.743  1.00 16.14           N  
-ATOM   3226  CA  THR B 141      16.988 -10.229 -56.526  1.00 15.48           C  
-ATOM   3227  C   THR B 141      17.167 -10.437 -58.034  1.00 16.46           C  
-ATOM   3228  O   THR B 141      18.163 -10.997 -58.498  1.00 14.51           O  
-ATOM   3229  CB  THR B 141      17.313  -8.740 -56.192  1.00 15.88           C  
-ATOM   3230  OG1 THR B 141      18.638  -8.421 -56.627  1.00 14.23           O  
-ATOM   3231  CG2 THR B 141      17.199  -8.432 -54.677  1.00 14.33           C  
-ATOM   3232  N   SER B 142      16.179  -9.979 -58.794  1.00 16.87           N  
-ATOM   3233  CA  SER B 142      16.304  -9.899 -60.241  1.00 17.95           C  
-ATOM   3234  C   SER B 142      15.695  -8.578 -60.645  1.00 17.02           C  
-ATOM   3235  O   SER B 142      14.492  -8.371 -60.452  1.00 18.12           O  
-ATOM   3236  CB  SER B 142      15.596 -11.040 -60.967  1.00 17.46           C  
-ATOM   3237  OG  SER B 142      15.681 -10.830 -62.377  1.00 17.95           O  
-ATOM   3238  N   ALA B 143      16.511  -7.677 -61.182  1.00 19.87           N  
-ATOM   3239  CA  ALA B 143      15.984  -6.412 -61.714  1.00 20.43           C  
-ATOM   3240  C   ALA B 143      15.122  -6.682 -62.955  1.00 22.99           C  
-ATOM   3241  O   ALA B 143      14.153  -5.963 -63.188  1.00 23.83           O  
-ATOM   3242  CB  ALA B 143      17.104  -5.429 -62.032  1.00 21.08           C  
-ATOM   3243  N   LEU B 144      15.458  -7.720 -63.729  1.00 22.85           N  
-ATOM   3244  CA  LEU B 144      14.694  -8.076 -64.951  1.00 24.60           C  
-ATOM   3245  C   LEU B 144      13.311  -8.621 -64.623  1.00 24.30           C  
-ATOM   3246  O   LEU B 144      12.306  -8.123 -65.127  1.00 25.21           O  
-ATOM   3247  CB  LEU B 144      15.453  -9.111 -65.804  1.00 24.29           C  
-ATOM   3248  CG  LEU B 144      14.744  -9.605 -67.079  1.00 26.06           C  
-ATOM   3249  CD1 LEU B 144      14.491  -8.447 -68.017  1.00 27.38           C  
-ATOM   3250  CD2 LEU B 144      15.530 -10.701 -67.787  1.00 26.52           C  
-ATOM   3251  N   LYS B 145      13.261  -9.651 -63.784  1.00 23.51           N  
-ATOM   3252  CA  LYS B 145      11.990 -10.255 -63.377  1.00 24.54           C  
-ATOM   3253  C   LYS B 145      11.260  -9.420 -62.315  1.00 23.98           C  
-ATOM   3254  O   LYS B 145      10.097  -9.679 -62.048  1.00 22.27           O  
-ATOM   3255  CB  LYS B 145      12.196 -11.671 -62.836  1.00 25.19           C  
-ATOM   3256  CG  LYS B 145      13.013 -12.611 -63.704  1.00 29.16           C  
-ATOM   3257  CD  LYS B 145      12.354 -12.903 -65.040  1.00 31.91           C  
-ATOM   3258  CE  LYS B 145      13.207 -13.876 -65.851  1.00 34.63           C  
-ATOM   3259  NZ  LYS B 145      12.585 -14.197 -67.178  1.00 37.40           N  
-ATOM   3260  N   GLN B 146      11.939  -8.437 -61.710  1.00 23.33           N  
-ATOM   3261  CA  GLN B 146      11.377  -7.583 -60.652  1.00 23.87           C  
-ATOM   3262  C   GLN B 146      10.959  -8.384 -59.406  1.00 23.19           C  
-ATOM   3263  O   GLN B 146       9.834  -8.258 -58.911  1.00 22.07           O  
-ATOM   3264  CB  GLN B 146      10.226  -6.698 -61.180  1.00 25.07           C  
-ATOM   3265  CG  GLN B 146      10.607  -5.918 -62.429  1.00 26.26           C  
-ATOM   3266  CD  GLN B 146       9.570  -4.894 -62.879  1.00 29.30           C  
-ATOM   3267  OE1 GLN B 146       8.567  -4.644 -62.208  1.00 30.20           O  
-ATOM   3268  NE2 GLN B 146       9.819  -4.298 -64.038  1.00 31.49           N  
-ATOM   3269  N   THR B 147      11.891  -9.207 -58.925  1.00 22.27           N  
-ATOM   3270  CA  THR B 147      11.713 -10.041 -57.745  1.00 21.89           C  
-ATOM   3271  C   THR B 147      12.754  -9.693 -56.675  1.00 22.87           C  
-ATOM   3272  O   THR B 147      13.893  -9.330 -56.999  1.00 19.27           O  
-ATOM   3273  CB  THR B 147      11.819 -11.546 -58.090  1.00 22.01           C  
-ATOM   3274  OG1 THR B 147      13.109 -11.839 -58.635  1.00 18.84           O  
-ATOM   3275  CG2 THR B 147      10.732 -11.958 -59.105  1.00 23.02           C  
-ATOM   3276  N   GLY B 148      12.339  -9.804 -55.409  1.00 22.62           N  
-ATOM   3277  CA  GLY B 148      13.215  -9.591 -54.254  1.00 23.36           C  
-ATOM   3278  C   GLY B 148      13.548  -8.153 -53.909  1.00 22.76           C  
-ATOM   3279  O   GLY B 148      14.230  -7.904 -52.900  1.00 21.48           O  
-ATOM   3280  N   VAL B 149      13.062  -7.201 -54.707  1.00 22.89           N  
-ATOM   3281  CA  VAL B 149      13.456  -5.802 -54.555  1.00 23.83           C  
-ATOM   3282  C   VAL B 149      12.918  -5.202 -53.246  1.00 22.81           C  
-ATOM   3283  O   VAL B 149      13.696  -4.715 -52.429  1.00 21.77           O  
-ATOM   3284  CB  VAL B 149      13.020  -4.949 -55.774  1.00 25.59           C  
-ATOM   3285  CG1 VAL B 149      13.451  -3.495 -55.602  1.00 26.54           C  
-ATOM   3286  CG2 VAL B 149      13.609  -5.513 -57.057  1.00 26.15           C  
-ATOM   3287  N   ASP B 150      11.599  -5.259 -53.035  1.00 22.51           N  
-ATOM   3288  CA  ASP B 150      11.005  -4.679 -51.834  1.00 22.77           C  
-ATOM   3289  C   ASP B 150      11.554  -5.347 -50.578  1.00 22.27           C  
-ATOM   3290  O   ASP B 150      11.766  -4.684 -49.562  1.00 22.78           O  
-ATOM   3291  CB  ASP B 150       9.477  -4.788 -51.819  1.00 23.86           C  
-ATOM   3292  CG  ASP B 150       8.808  -4.030 -52.947  1.00 25.35           C  
-ATOM   3293  OD1 ASP B 150       9.439  -3.156 -53.578  1.00 27.81           O  
-ATOM   3294  OD2 ASP B 150       7.619  -4.344 -53.212  1.00 28.73           O  
-ATOM   3295  N   GLN B 151      11.795  -6.651 -50.676  1.00 21.02           N  
-ATOM   3296  CA  GLN B 151      12.305  -7.457 -49.581  1.00 21.23           C  
-ATOM   3297  C   GLN B 151      13.717  -6.998 -49.175  1.00 20.27           C  
-ATOM   3298  O   GLN B 151      13.977  -6.784 -47.982  1.00 17.42           O  
-ATOM   3299  CB  GLN B 151      12.306  -8.941 -49.961  1.00 22.92           C  
-ATOM   3300  CG  GLN B 151      10.917  -9.554 -50.239  1.00 24.89           C  
-ATOM   3301  CD  GLN B 151      10.410  -9.436 -51.698  1.00 27.26           C  
-ATOM   3302  OE1 GLN B 151      10.628  -8.437 -52.390  1.00 23.79           O  
-ATOM   3303  NE2 GLN B 151       9.706 -10.475 -52.151  1.00 30.40           N  
-ATOM   3304  N   VAL B 152      14.612  -6.825 -50.149  1.00 18.31           N  
-ATOM   3305  CA  VAL B 152      15.994  -6.382 -49.825  1.00 18.01           C  
-ATOM   3306  C   VAL B 152      16.020  -4.947 -49.282  1.00 18.21           C  
-ATOM   3307  O   VAL B 152      16.819  -4.630 -48.385  1.00 18.79           O  
-ATOM   3308  CB  VAL B 152      16.990  -6.570 -50.999  1.00 18.52           C  
-ATOM   3309  CG1 VAL B 152      16.817  -5.512 -52.113  1.00 16.63           C  
-ATOM   3310  CG2 VAL B 152      18.426  -6.585 -50.466  1.00 19.24           C  
-ATOM   3311  N   VAL B 153      15.154  -4.084 -49.802  1.00 17.23           N  
-ATOM   3312  CA  VAL B 153      15.083  -2.698 -49.325  1.00 18.42           C  
-ATOM   3313  C   VAL B 153      14.642  -2.668 -47.849  1.00 18.09           C  
-ATOM   3314  O   VAL B 153      15.229  -1.957 -47.032  1.00 16.85           O  
-ATOM   3315  CB  VAL B 153      14.180  -1.811 -50.222  1.00 19.15           C  
-ATOM   3316  CG1 VAL B 153      13.888  -0.449 -49.562  1.00 20.90           C  
-ATOM   3317  CG2 VAL B 153      14.830  -1.574 -51.582  1.00 20.30           C  
-ATOM   3318  N   LYS B 154      13.616  -3.452 -47.528  1.00 18.70           N  
-ATOM   3319  CA  LYS B 154      13.111  -3.590 -46.163  1.00 20.11           C  
-ATOM   3320  C   LYS B 154      14.167  -4.137 -45.195  1.00 19.60           C  
-ATOM   3321  O   LYS B 154      14.296  -3.652 -44.069  1.00 19.49           O  
-ATOM   3322  CB  LYS B 154      11.884  -4.509 -46.132  1.00 21.28           C  
-ATOM   3323  CG  LYS B 154      11.384  -4.775 -44.715  1.00 24.32           C  
-ATOM   3324  CD  LYS B 154      10.007  -5.415 -44.662  1.00 28.76           C  
-ATOM   3325  CE  LYS B 154       9.662  -5.751 -43.217  1.00 31.18           C  
-ATOM   3326  NZ  LYS B 154       8.215  -6.053 -43.035  1.00 35.89           N  
-ATOM   3327  N   LYS B 155      14.901  -5.156 -45.630  1.00 18.98           N  
-ATOM   3328  CA  LYS B 155      15.977  -5.717 -44.828  1.00 19.64           C  
-ATOM   3329  C   LYS B 155      17.040  -4.646 -44.568  1.00 17.60           C  
-ATOM   3330  O   LYS B 155      17.402  -4.432 -43.409  1.00 17.62           O  
-ATOM   3331  CB  LYS B 155      16.596  -6.948 -45.491  1.00 20.11           C  
-ATOM   3332  CG  LYS B 155      17.682  -7.644 -44.668  1.00 21.70           C  
-ATOM   3333  CD  LYS B 155      17.259  -8.069 -43.250  1.00 22.77           C  
-ATOM   3334  CE  LYS B 155      16.174  -9.113 -43.256  1.00 24.59           C  
-ATOM   3335  NZ  LYS B 155      16.200  -9.915 -41.999  1.00 25.77           N  
-ATOM   3336  N   ALA B 156      17.513  -3.986 -45.629  1.00 16.81           N  
-ATOM   3337  CA  ALA B 156      18.501  -2.892 -45.512  1.00 16.83           C  
-ATOM   3338  C   ALA B 156      18.050  -1.817 -44.518  1.00 16.55           C  
-ATOM   3339  O   ALA B 156      18.830  -1.365 -43.674  1.00 14.88           O  
-ATOM   3340  CB  ALA B 156      18.785  -2.251 -46.885  1.00 16.97           C  
-ATOM   3341  N   ALA B 157      16.783  -1.421 -44.628  1.00 17.29           N  
-ATOM   3342  CA  ALA B 157      16.202  -0.405 -43.755  1.00 18.04           C  
-ATOM   3343  C   ALA B 157      16.187  -0.797 -42.275  1.00 19.12           C  
-ATOM   3344  O   ALA B 157      16.205   0.091 -41.424  1.00 21.61           O  
-ATOM   3345  CB  ALA B 157      14.775   0.018 -44.232  1.00 17.68           C  
-ATOM   3346  N   HIS B 158      16.156  -2.091 -41.978  1.00 19.11           N  
-ATOM   3347  CA  HIS B 158      16.199  -2.618 -40.607  1.00 21.07           C  
-ATOM   3348  C   HIS B 158      17.573  -3.141 -40.176  1.00 19.82           C  
-ATOM   3349  O   HIS B 158      17.699  -3.747 -39.108  1.00 20.97           O  
-ATOM   3350  CB  HIS B 158      15.137  -3.707 -40.460  1.00 23.10           C  
-ATOM   3351  CG  HIS B 158      13.754  -3.154 -40.514  1.00 26.76           C  
-ATOM   3352  ND1 HIS B 158      13.031  -3.068 -41.684  1.00 28.89           N  
-ATOM   3353  CD2 HIS B 158      12.977  -2.609 -39.548  1.00 29.22           C  
-ATOM   3354  CE1 HIS B 158      11.855  -2.521 -41.430  1.00 30.77           C  
-ATOM   3355  NE2 HIS B 158      11.800  -2.227 -40.143  1.00 29.83           N  
-ATOM   3356  N   THR B 159      18.589  -2.887 -40.999  1.00 17.87           N  
-ATOM   3357  CA  THR B 159      19.966  -3.344 -40.761  1.00 16.36           C  
-ATOM   3358  C   THR B 159      20.866  -2.107 -40.842  1.00 15.89           C  
-ATOM   3359  O   THR B 159      21.527  -1.856 -41.855  1.00 13.65           O  
-ATOM   3360  CB  THR B 159      20.338  -4.440 -41.784  1.00 16.36           C  
-ATOM   3361  OG1 THR B 159      19.308  -5.455 -41.792  1.00 14.66           O  
-ATOM   3362  CG2 THR B 159      21.686  -5.073 -41.443  1.00 13.99           C  
-ATOM   3363  N   THR B 160      20.877  -1.329 -39.757  1.00 15.92           N  
-ATOM   3364  CA  THR B 160      21.514  -0.012 -39.750  1.00 15.75           C  
-ATOM   3365  C   THR B 160      22.509   0.172 -38.611  1.00 14.51           C  
-ATOM   3366  O   THR B 160      22.602  -0.661 -37.717  1.00 14.53           O  
-ATOM   3367  CB  THR B 160      20.462   1.122 -39.616  1.00 17.19           C  
-ATOM   3368  OG1 THR B 160      19.918   1.118 -38.283  1.00 17.57           O  
-ATOM   3369  CG2 THR B 160      19.346   0.993 -40.663  1.00 15.15           C  
-ATOM   3370  N   THR B 161      23.248   1.281 -38.659  1.00 16.65           N  
-ATOM   3371  CA  THR B 161      24.181   1.637 -37.588  1.00 17.38           C  
-ATOM   3372  C   THR B 161      23.469   1.775 -36.224  1.00 18.42           C  
-ATOM   3373  O   THR B 161      24.112   1.675 -35.169  1.00 19.68           O  
-ATOM   3374  CB  THR B 161      24.945   2.937 -37.905  1.00 17.74           C  
-ATOM   3375  OG1 THR B 161      24.009   3.988 -38.153  1.00 18.61           O  
-ATOM   3376  CG2 THR B 161      25.855   2.772 -39.127  1.00 17.98           C  
-ATOM   3377  N   SER B 162      22.158   2.008 -36.237  1.00 17.88           N  
-ATOM   3378  CA  SER B 162      21.368   2.088 -35.012  1.00 20.79           C  
-ATOM   3379  C   SER B 162      20.849   0.727 -34.539  1.00 21.14           C  
-ATOM   3380  O   SER B 162      20.854   0.466 -33.340  1.00 22.93           O  
-ATOM   3381  CB  SER B 162      20.198   3.069 -35.212  1.00 20.25           C  
-ATOM   3382  OG  SER B 162      20.696   4.351 -35.564  1.00 21.19           O  
-ATOM   3383  N   THR B 163      20.410  -0.138 -35.455  1.00 20.80           N  
-ATOM   3384  CA  THR B 163      19.802  -1.433 -35.069  1.00 20.64           C  
-ATOM   3385  C   THR B 163      20.794  -2.566 -34.810  1.00 21.36           C  
-ATOM   3386  O   THR B 163      20.515  -3.472 -34.025  1.00 22.87           O  
-ATOM   3387  CB  THR B 163      18.760  -1.920 -36.114  1.00 21.03           C  
-ATOM   3388  OG1 THR B 163      19.408  -2.266 -37.353  1.00 19.14           O  
-ATOM   3389  CG2 THR B 163      17.700  -0.858 -36.343  1.00 22.19           C  
-ATOM   3390  N   VAL B 164      21.952  -2.517 -35.463  1.00 21.75           N  
-ATOM   3391  CA  VAL B 164      22.956  -3.578 -35.389  1.00 21.27           C  
-ATOM   3392  C   VAL B 164      23.983  -3.220 -34.321  1.00 22.49           C  
-ATOM   3393  O   VAL B 164      24.446  -2.081 -34.264  1.00 20.71           O  
-ATOM   3394  CB  VAL B 164      23.656  -3.767 -36.752  1.00 20.27           C  
-ATOM   3395  CG1 VAL B 164      24.755  -4.830 -36.676  1.00 20.05           C  
-ATOM   3396  CG2 VAL B 164      22.619  -4.131 -37.815  1.00 19.87           C  
-ATOM   3397  N   GLY B 165      24.315  -4.186 -33.471  1.00 24.42           N  
-ATOM   3398  CA  GLY B 165      25.310  -4.000 -32.412  1.00 26.83           C  
-ATOM   3399  C   GLY B 165      26.684  -4.355 -32.943  1.00 27.72           C  
-ATOM   3400  O   GLY B 165      27.211  -3.661 -33.819  1.00 27.37           O  
-ATOM   3401  N   ASP B 166      27.264  -5.438 -32.432  1.00 29.36           N  
-ATOM   3402  CA  ASP B 166      28.607  -5.841 -32.838  1.00 31.88           C  
-ATOM   3403  C   ASP B 166      28.539  -6.273 -34.297  1.00 31.43           C  
-ATOM   3404  O   ASP B 166      27.596  -6.958 -34.698  1.00 32.93           O  
-ATOM   3405  CB  ASP B 166      29.148  -7.006 -32.005  1.00 34.42           C  
-ATOM   3406  CG  ASP B 166      29.326  -6.660 -30.544  1.00 36.98           C  
-ATOM   3407  OD1 ASP B 166      29.976  -5.639 -30.234  1.00 39.07           O  
-ATOM   3408  OD2 ASP B 166      28.815  -7.434 -29.708  1.00 41.23           O  
-ATOM   3409  N   LEU B 167      29.528  -5.849 -35.072  1.00 30.86           N  
-ATOM   3410  CA  LEU B 167      29.614  -6.211 -36.483  1.00 31.43           C  
-ATOM   3411  C   LEU B 167      30.635  -7.332 -36.638  1.00 27.82           C  
-ATOM   3412  O   LEU B 167      31.666  -7.344 -35.966  1.00 28.29           O  
-ATOM   3413  CB  LEU B 167      29.986  -4.996 -37.335  1.00 32.03           C  
-ATOM   3414  CG  LEU B 167      28.870  -3.952 -37.516  1.00 34.28           C  
-ATOM   3415  CD1 LEU B 167      29.421  -2.524 -37.350  1.00 35.26           C  
-ATOM   3416  CD2 LEU B 167      28.113  -4.128 -38.849  1.00 30.73           C  
-ATOM   3417  N   ALA B 168      30.313  -8.275 -37.513  1.00 24.96           N  
-ATOM   3418  CA  ALA B 168      31.169  -9.401 -37.817  1.00 23.88           C  
-ATOM   3419  C   ALA B 168      31.919  -9.003 -39.076  1.00 21.44           C  
-ATOM   3420  O   ALA B 168      31.294  -8.760 -40.106  1.00 23.87           O  
-ATOM   3421  CB  ALA B 168      30.343 -10.648 -38.061  1.00 24.84           C  
-ATOM   3422  N  APHE B 169      33.242  -8.925 -38.997  0.50 20.11           N  
-ATOM   3423  N  BPHE B 169      33.246  -8.928 -38.979  0.50 20.35           N  
-ATOM   3424  CA APHE B 169      34.063  -8.572 -40.144  0.50 18.21           C  
-ATOM   3425  CA BPHE B 169      34.113  -8.583 -40.101  0.50 18.66           C  
-ATOM   3426  C  APHE B 169      34.732  -9.833 -40.671  0.50 18.47           C  
-ATOM   3427  C  BPHE B 169      34.738  -9.853 -40.667  0.50 18.71           C  
-ATOM   3428  O  APHE B 169      34.940 -10.774 -39.907  0.50 17.99           O  
-ATOM   3429  O  BPHE B 169      34.919 -10.819 -39.928  0.50 18.26           O  
-ATOM   3430  CB APHE B 169      35.109  -7.556 -39.722  0.50 18.09           C  
-ATOM   3431  CB BPHE B 169      35.214  -7.628 -39.637  0.50 18.77           C  
-ATOM   3432  CG APHE B 169      35.864  -7.961 -38.502  0.50 16.86           C  
-ATOM   3433  CG BPHE B 169      34.698  -6.327 -39.095  0.50 18.40           C  
-ATOM   3434  CD1APHE B 169      36.846  -8.930 -38.578  0.50 16.51           C  
-ATOM   3435  CD1BPHE B 169      34.251  -5.335 -39.949  0.50 18.21           C  
-ATOM   3436  CD2APHE B 169      35.589  -7.384 -37.274  0.50 17.75           C  
-ATOM   3437  CD2BPHE B 169      34.665  -6.087 -37.728  0.50 18.54           C  
-ATOM   3438  CE1APHE B 169      37.550  -9.306 -37.458  0.50 15.87           C  
-ATOM   3439  CE1BPHE B 169      33.772  -4.131 -39.454  0.50 17.04           C  
-ATOM   3440  CE2APHE B 169      36.295  -7.765 -36.144  0.50 17.53           C  
-ATOM   3441  CE2BPHE B 169      34.187  -4.877 -37.233  0.50 19.03           C  
-ATOM   3442  CZ APHE B 169      37.274  -8.728 -36.243  0.50 15.37           C  
-ATOM   3443  CZ BPHE B 169      33.740  -3.904 -38.101  0.50 17.09           C  
-ATOM   3444  N   PRO B 170      35.068  -9.869 -41.977  1.00 17.80           N  
-ATOM   3445  CA  PRO B 170      35.804 -11.013 -42.517  1.00 16.67           C  
-ATOM   3446  C   PRO B 170      37.122 -11.237 -41.735  1.00 17.04           C  
-ATOM   3447  O   PRO B 170      37.920 -10.295 -41.577  1.00 16.61           O  
-ATOM   3448  CB  PRO B 170      36.093 -10.592 -43.971  1.00 17.37           C  
-ATOM   3449  CG  PRO B 170      34.991  -9.634 -44.318  1.00 17.06           C  
-ATOM   3450  CD  PRO B 170      34.730  -8.890 -43.034  1.00 18.61           C  
-ATOM   3451  N  AILE B 171      37.330 -12.457 -41.242  0.50 16.78           N  
-ATOM   3452  N  BILE B 171      37.326 -12.458 -41.246  0.50 15.92           N  
-ATOM   3453  CA AILE B 171      38.525 -12.790 -40.469  0.50 16.76           C  
-ATOM   3454  CA BILE B 171      38.540 -12.790 -40.511  0.50 15.23           C  
-ATOM   3455  C  AILE B 171      39.560 -13.424 -41.410  0.50 16.30           C  
-ATOM   3456  C  BILE B 171      39.555 -13.405 -41.463  0.50 15.44           C  
-ATOM   3457  O  AILE B 171      39.262 -14.423 -42.068  0.50 16.02           O  
-ATOM   3458  O  BILE B 171      39.241 -14.359 -42.178  0.50 15.03           O  
-ATOM   3459  CB AILE B 171      38.175 -13.743 -39.314  0.50 16.91           C  
-ATOM   3460  CB BILE B 171      38.252 -13.755 -39.378  0.50 14.40           C  
-ATOM   3461  CG1AILE B 171      36.968 -13.217 -38.513  0.50 17.56           C  
-ATOM   3462  CG1BILE B 171      37.516 -13.008 -38.263  0.50 14.50           C  
-ATOM   3463  CG2AILE B 171      39.388 -13.968 -38.413  0.50 17.54           C  
-ATOM   3464  CG2BILE B 171      39.560 -14.395 -38.897  0.50 13.14           C  
-ATOM   3465  CD1AILE B 171      37.288 -12.170 -37.476  0.50 18.45           C  
-ATOM   3466  CD1BILE B 171      36.868 -13.913 -37.244  0.50 12.31           C  
-ATOM   3467  N   TYR B 172      40.761 -12.846 -41.473  1.00 14.90           N  
-ATOM   3468  CA  TYR B 172      41.833 -13.298 -42.362  1.00 14.47           C  
-ATOM   3469  C   TYR B 172      42.803 -14.216 -41.613  1.00 13.97           C  
-ATOM   3470  O   TYR B 172      42.588 -14.573 -40.451  1.00 15.07           O  
-ATOM   3471  CB  TYR B 172      42.546 -12.070 -42.982  1.00 13.33           C  
-ATOM   3472  CG  TYR B 172      41.569 -11.152 -43.705  1.00 13.00           C  
-ATOM   3473  CD1 TYR B 172      40.805 -11.633 -44.761  1.00 14.53           C  
-ATOM   3474  CD2 TYR B 172      41.382  -9.828 -43.321  1.00 14.31           C  
-ATOM   3475  CE1 TYR B 172      39.891 -10.823 -45.420  1.00 15.52           C  
-ATOM   3476  CE2 TYR B 172      40.470  -9.004 -43.983  1.00 14.29           C  
-ATOM   3477  CZ  TYR B 172      39.729  -9.507 -45.029  1.00 16.77           C  
-ATOM   3478  OH  TYR B 172      38.808  -8.729 -45.698  1.00 15.95           O  
-ATOM   3479  N   ASP B 173      43.870 -14.605 -42.286  1.00 14.50           N  
-ATOM   3480  CA  ASP B 173      44.891 -15.436 -41.651  1.00 17.45           C  
-ATOM   3481  C   ASP B 173      45.383 -14.820 -40.333  1.00 16.73           C  
-ATOM   3482  O   ASP B 173      45.515 -13.590 -40.223  1.00 15.25           O  
-ATOM   3483  CB  ASP B 173      46.074 -15.616 -42.587  1.00 17.58           C  
-ATOM   3484  CG  ASP B 173      47.079 -16.589 -42.035  1.00 22.54           C  
-ATOM   3485  OD1 ASP B 173      48.107 -16.127 -41.519  1.00 22.67           O  
-ATOM   3486  OD2 ASP B 173      46.783 -17.809 -42.087  1.00 29.22           O  
-ATOM   3487  N   ASP B 174      45.652 -15.677 -39.345  1.00 16.86           N  
-ATOM   3488  CA  ASP B 174      46.199 -15.253 -38.046  1.00 16.88           C  
-ATOM   3489  C   ASP B 174      47.352 -14.262 -38.157  1.00 16.34           C  
-ATOM   3490  O   ASP B 174      47.437 -13.344 -37.353  1.00 16.05           O  
-ATOM   3491  CB  ASP B 174      46.701 -16.454 -37.239  1.00 17.27           C  
-ATOM   3492  CG  ASP B 174      45.576 -17.299 -36.665  1.00 21.37           C  
-ATOM   3493  OD1 ASP B 174      44.411 -16.855 -36.656  1.00 20.60           O  
-ATOM   3494  OD2 ASP B 174      45.880 -18.416 -36.211  1.00 22.62           O  
-ATOM   3495  N   ARG B 175      48.227 -14.447 -39.140  1.00 17.27           N  
-ATOM   3496  CA  ARG B 175      49.381 -13.549 -39.290  1.00 18.27           C  
-ATOM   3497  C   ARG B 175      48.944 -12.128 -39.705  1.00 17.71           C  
-ATOM   3498  O   ARG B 175      49.506 -11.128 -39.233  1.00 17.52           O  
-ATOM   3499  CB  ARG B 175      50.400 -14.136 -40.260  1.00 20.99           C  
-ATOM   3500  CG  ARG B 175      50.992 -15.463 -39.794  1.00 22.95           C  
-ATOM   3501  CD  ARG B 175      51.766 -16.133 -40.913  1.00 26.94           C  
-ATOM   3502  NE  ARG B 175      50.950 -16.407 -42.093  1.00 29.32           N  
-ATOM   3503  CZ  ARG B 175      51.416 -16.880 -43.247  1.00 31.70           C  
-ATOM   3504  NH1 ARG B 175      52.711 -17.151 -43.413  1.00 32.62           N  
-ATOM   3505  NH2 ARG B 175      50.575 -17.081 -44.249  1.00 32.33           N  
-ATOM   3506  N   LEU B 176      47.934 -12.029 -40.565  1.00 15.59           N  
-ATOM   3507  CA  LEU B 176      47.404 -10.702 -40.902  1.00 15.41           C  
-ATOM   3508  C   LEU B 176      46.613 -10.126 -39.719  1.00 12.60           C  
-ATOM   3509  O   LEU B 176      46.709  -8.931 -39.422  1.00 13.25           O  
-ATOM   3510  CB  LEU B 176      46.574 -10.717 -42.193  1.00 14.15           C  
-ATOM   3511  CG  LEU B 176      46.030  -9.361 -42.647  1.00 13.76           C  
-ATOM   3512  CD1 LEU B 176      47.153  -8.343 -42.767  1.00 15.85           C  
-ATOM   3513  CD2 LEU B 176      45.257  -9.527 -43.973  1.00 11.67           C  
-ATOM   3514  N   GLU B 177      45.843 -10.971 -39.041  1.00 13.66           N  
-ATOM   3515  CA  GLU B 177      45.085 -10.534 -37.875  1.00 14.69           C  
-ATOM   3516  C   GLU B 177      45.993  -9.985 -36.770  1.00 15.20           C  
-ATOM   3517  O   GLU B 177      45.614  -9.028 -36.098  1.00 13.18           O  
-ATOM   3518  CB  GLU B 177      44.191 -11.657 -37.336  1.00 15.13           C  
-ATOM   3519  CG  GLU B 177      43.039 -12.022 -38.269  1.00 13.23           C  
-ATOM   3520  CD  GLU B 177      42.104 -10.853 -38.559  1.00 15.78           C  
-ATOM   3521  OE1 GLU B 177      41.909 -10.001 -37.678  1.00 15.43           O  
-ATOM   3522  OE2 GLU B 177      41.547 -10.775 -39.680  1.00 16.51           O  
-ATOM   3523  N   ALA B 178      47.176 -10.576 -36.588  1.00 14.68           N  
-ATOM   3524  CA  ALA B 178      48.123 -10.062 -35.592  1.00 14.91           C  
-ATOM   3525  C   ALA B 178      48.566  -8.640 -35.970  1.00 15.25           C  
-ATOM   3526  O   ALA B 178      48.638  -7.767 -35.107  1.00 14.54           O  
-ATOM   3527  CB  ALA B 178      49.345 -10.997 -35.425  1.00 13.98           C  
-ATOM   3528  N   ALA B 179      48.827  -8.424 -37.261  1.00 13.16           N  
-ATOM   3529  CA  ALA B 179      49.242  -7.122 -37.774  1.00 12.83           C  
-ATOM   3530  C   ALA B 179      48.150  -6.075 -37.583  1.00 11.68           C  
-ATOM   3531  O   ALA B 179      48.415  -4.975 -37.117  1.00 12.67           O  
-ATOM   3532  CB  ALA B 179      49.644  -7.218 -39.241  1.00 12.77           C  
-ATOM   3533  N   ILE B 180      46.923  -6.441 -37.916  1.00 13.16           N  
-ATOM   3534  CA  ILE B 180      45.774  -5.565 -37.757  1.00 13.66           C  
-ATOM   3535  C   ILE B 180      45.600  -5.167 -36.282  1.00 14.92           C  
-ATOM   3536  O   ILE B 180      45.438  -3.983 -35.980  1.00 12.35           O  
-ATOM   3537  CB  ILE B 180      44.482  -6.203 -38.358  1.00 13.45           C  
-ATOM   3538  CG1 ILE B 180      44.595  -6.343 -39.882  1.00 14.18           C  
-ATOM   3539  CG2 ILE B 180      43.261  -5.351 -38.003  1.00 12.50           C  
-ATOM   3540  CD1 ILE B 180      43.533  -7.321 -40.496  1.00 14.36           C  
-ATOM   3541  N  ASER B 181      45.634  -6.155 -35.386  0.50 15.51           N  
-ATOM   3542  N  BSER B 181      45.642  -6.152 -35.386  0.50 14.68           N  
-ATOM   3543  CA ASER B 181      45.515  -5.924 -33.946  0.50 16.54           C  
-ATOM   3544  CA BSER B 181      45.514  -5.915 -33.949  0.50 14.98           C  
-ATOM   3545  C  ASER B 181      46.533  -4.910 -33.416  0.50 16.24           C  
-ATOM   3546  C  BSER B 181      46.532  -4.903 -33.421  0.50 15.45           C  
-ATOM   3547  O  ASER B 181      46.180  -4.002 -32.661  0.50 15.78           O  
-ATOM   3548  O  BSER B 181      46.181  -3.990 -32.669  0.50 15.01           O  
-ATOM   3549  CB ASER B 181      45.680  -7.236 -33.175  0.50 17.34           C  
-ATOM   3550  CB BSER B 181      45.685  -7.219 -33.173  0.50 15.17           C  
-ATOM   3551  OG ASER B 181      44.543  -8.071 -33.330  0.50 18.23           O  
-ATOM   3552  OG BSER B 181      45.392  -7.019 -31.801  0.50 11.88           O  
-ATOM   3553  N   GLN B 182      47.786  -5.076 -33.823  1.00 14.55           N  
-ATOM   3554  CA  GLN B 182      48.871  -4.189 -33.403  1.00 14.81           C  
-ATOM   3555  C   GLN B 182      48.740  -2.795 -34.010  1.00 13.92           C  
-ATOM   3556  O   GLN B 182      49.020  -1.804 -33.323  1.00 13.91           O  
-ATOM   3557  CB  GLN B 182      50.230  -4.821 -33.699  1.00 15.48           C  
-ATOM   3558  CG  GLN B 182      50.501  -6.015 -32.816  1.00 17.41           C  
-ATOM   3559  CD  GLN B 182      51.661  -6.837 -33.320  1.00 21.37           C  
-ATOM   3560  OE1 GLN B 182      52.624  -6.289 -33.853  1.00 26.92           O  
-ATOM   3561  NE2 GLN B 182      51.577  -8.149 -33.165  1.00 19.20           N  
-ATOM   3562  N   ILE B 183      48.289  -2.701 -35.266  1.00 12.06           N  
-ATOM   3563  CA  ILE B 183      48.020  -1.398 -35.859  1.00 12.64           C  
-ATOM   3564  C   ILE B 183      46.861  -0.716 -35.088  1.00 13.72           C  
-ATOM   3565  O   ILE B 183      46.937   0.482 -34.790  1.00 14.29           O  
-ATOM   3566  CB  ILE B 183      47.740  -1.493 -37.396  1.00 11.99           C  
-ATOM   3567  CG1 ILE B 183      49.020  -1.914 -38.115  1.00 10.43           C  
-ATOM   3568  CG2 ILE B 183      47.232  -0.153 -37.960  1.00 11.88           C  
-ATOM   3569  CD1 ILE B 183      48.816  -2.304 -39.559  1.00 13.45           C  
-ATOM   3570  N   LEU B 184      45.811  -1.466 -34.755  1.00 14.48           N  
-ATOM   3571  CA  LEU B 184      44.724  -0.911 -33.928  1.00 15.57           C  
-ATOM   3572  C   LEU B 184      45.256  -0.368 -32.588  1.00 15.71           C  
-ATOM   3573  O   LEU B 184      44.871   0.735 -32.180  1.00 14.39           O  
-ATOM   3574  CB  LEU B 184      43.598  -1.921 -33.705  1.00 14.84           C  
-ATOM   3575  CG  LEU B 184      42.771  -2.268 -34.935  1.00 14.79           C  
-ATOM   3576  CD1 LEU B 184      41.882  -3.473 -34.714  1.00 17.29           C  
-ATOM   3577  CD2 LEU B 184      41.944  -1.028 -35.381  1.00 15.66           C  
-ATOM   3578  N   GLU B 185      46.151  -1.111 -31.937  1.00 17.46           N  
-ATOM   3579  CA  GLU B 185      46.741  -0.682 -30.665  1.00 20.11           C  
-ATOM   3580  C   GLU B 185      47.509   0.617 -30.884  1.00 19.50           C  
-ATOM   3581  O   GLU B 185      47.416   1.539 -30.077  1.00 19.67           O  
-ATOM   3582  CB  GLU B 185      47.743  -1.690 -30.101  1.00 22.84           C  
-ATOM   3583  CG  GLU B 185      47.226  -3.005 -29.594  1.00 27.66           C  
-ATOM   3584  CD  GLU B 185      48.359  -3.993 -29.272  1.00 33.79           C  
-ATOM   3585  OE1 GLU B 185      49.550  -3.732 -29.614  1.00 36.48           O  
-ATOM   3586  OE2 GLU B 185      48.055  -5.052 -28.674  1.00 36.94           O  
-ATOM   3587  N   VAL B 186      48.267   0.670 -31.977  1.00 18.41           N  
-ATOM   3588  CA  VAL B 186      49.071   1.852 -32.315  1.00 18.23           C  
-ATOM   3589  C   VAL B 186      48.193   3.077 -32.611  1.00 17.21           C  
-ATOM   3590  O   VAL B 186      48.570   4.199 -32.289  1.00 16.76           O  
-ATOM   3591  CB  VAL B 186      50.018   1.576 -33.507  1.00 19.18           C  
-ATOM   3592  N   LEU B 187      47.030   2.844 -33.213  1.00 16.71           N  
-ATOM   3593  CA  LEU B 187      46.073   3.898 -33.574  1.00 16.61           C  
-ATOM   3594  C   LEU B 187      45.354   4.505 -32.367  1.00 15.61           C  
-ATOM   3595  O   LEU B 187      45.054   5.705 -32.377  1.00 16.42           O  
-ATOM   3596  CB  LEU B 187      45.033   3.381 -34.593  1.00 14.83           C  
-ATOM   3597  CG  LEU B 187      45.455   3.228 -36.069  1.00 17.57           C  
-ATOM   3598  CD1 LEU B 187      44.368   2.619 -36.942  1.00 15.75           C  
-ATOM   3599  CD2 LEU B 187      45.851   4.580 -36.658  1.00 19.93           C  
-ATOM   3600  N   GLY B 188      45.076   3.695 -31.341  1.00 15.59           N  
-ATOM   3601  CA  GLY B 188      44.369   4.154 -30.136  1.00 15.99           C  
-ATOM   3602  C   GLY B 188      43.052   4.790 -30.541  1.00 14.43           C  
-ATOM   3603  O   GLY B 188      42.263   4.159 -31.235  1.00 15.74           O  
-ATOM   3604  N   ASN B 189      42.829   6.051 -30.162  1.00 14.97           N  
-ATOM   3605  CA  ASN B 189      41.595   6.764 -30.518  1.00 15.20           C  
-ATOM   3606  C   ASN B 189      41.717   7.712 -31.739  1.00 16.71           C  
-ATOM   3607  O   ASN B 189      40.867   8.591 -31.934  1.00 17.09           O  
-ATOM   3608  CB  ASN B 189      41.022   7.504 -29.283  1.00 14.92           C  
-ATOM   3609  CG  ASN B 189      41.814   8.747 -28.918  1.00 16.85           C  
-ATOM   3610  OD1 ASN B 189      42.917   8.967 -29.433  1.00 12.98           O  
-ATOM   3611  ND2 ASN B 189      41.254   9.571 -28.018  1.00 13.45           N  
-ATOM   3612  N   SER B 190      42.758   7.529 -32.554  1.00 15.85           N  
-ATOM   3613  CA  SER B 190      42.982   8.349 -33.752  1.00 18.40           C  
-ATOM   3614  C   SER B 190      41.937   8.114 -34.842  1.00 18.52           C  
-ATOM   3615  O   SER B 190      41.847   8.913 -35.771  1.00 20.00           O  
-ATOM   3616  CB  SER B 190      44.388   8.098 -34.332  1.00 18.79           C  
-ATOM   3617  OG  SER B 190      45.390   8.492 -33.390  1.00 20.51           O  
-ATOM   3618  N   VAL B 191      41.172   7.020 -34.737  1.00 16.91           N  
-ATOM   3619  CA  VAL B 191      40.087   6.701 -35.672  1.00 18.22           C  
-ATOM   3620  C   VAL B 191      38.840   6.278 -34.904  1.00 17.83           C  
-ATOM   3621  O   VAL B 191      38.945   5.883 -33.743  1.00 18.55           O  
-ATOM   3622  CB  VAL B 191      40.459   5.526 -36.607  1.00 17.85           C  
-ATOM   3623  CG1 VAL B 191      41.593   5.910 -37.541  1.00 20.78           C  
-ATOM   3624  CG2 VAL B 191      40.811   4.283 -35.799  1.00 17.98           C  
-ATOM   3625  N   PRO B 192      37.656   6.354 -35.540  1.00 17.95           N  
-ATOM   3626  CA  PRO B 192      36.481   5.841 -34.838  1.00 18.20           C  
-ATOM   3627  C   PRO B 192      36.530   4.327 -34.672  1.00 17.73           C  
-ATOM   3628  O   PRO B 192      37.060   3.612 -35.525  1.00 16.30           O  
-ATOM   3629  CB  PRO B 192      35.309   6.269 -35.730  1.00 18.64           C  
-ATOM   3630  CG  PRO B 192      35.878   7.305 -36.691  1.00 19.58           C  
-ATOM   3631  CD  PRO B 192      37.306   6.939 -36.849  1.00 18.14           C  
-ATOM   3632  N   GLN B 193      35.987   3.845 -33.561  1.00 17.52           N  
-ATOM   3633  CA  GLN B 193      35.941   2.410 -33.304  1.00 17.21           C  
-ATOM   3634  C   GLN B 193      35.188   1.671 -34.411  1.00 17.22           C  
-ATOM   3635  O   GLN B 193      35.617   0.592 -34.826  1.00 15.76           O  
-ATOM   3636  CB  GLN B 193      35.345   2.130 -31.926  1.00 17.15           C  
-ATOM   3637  CG  GLN B 193      36.322   2.499 -30.794  1.00 16.39           C  
-ATOM   3638  CD  GLN B 193      37.350   1.405 -30.591  1.00 19.28           C  
-ATOM   3639  OE1 GLN B 193      38.529   1.548 -30.952  1.00 20.83           O  
-ATOM   3640  NE2 GLN B 193      36.899   0.287 -30.034  1.00 15.46           N  
-ATOM   3641  N   ARG B 194      34.105   2.264 -34.913  1.00 17.29           N  
-ATOM   3642  CA  ARG B 194      33.260   1.606 -35.919  1.00 16.28           C  
-ATOM   3643  C   ARG B 194      34.040   1.226 -37.180  1.00 16.70           C  
-ATOM   3644  O   ARG B 194      33.896   0.123 -37.703  1.00 15.69           O  
-ATOM   3645  CB  ARG B 194      32.097   2.520 -36.302  1.00 16.90           C  
-ATOM   3646  CG  ARG B 194      31.162   1.960 -37.347  1.00 16.28           C  
-ATOM   3647  CD  ARG B 194      29.934   2.821 -37.515  1.00 15.71           C  
-ATOM   3648  NE  ARG B 194      29.113   2.737 -36.311  1.00 17.74           N  
-ATOM   3649  CZ  ARG B 194      28.260   1.753 -36.032  1.00 21.80           C  
-ATOM   3650  NH1 ARG B 194      28.053   0.746 -36.883  1.00 20.43           N  
-ATOM   3651  NH2 ARG B 194      27.585   1.786 -34.887  1.00 23.74           N  
-ATOM   3652  N   SER B 195      34.871   2.151 -37.634  1.00 17.19           N  
-ATOM   3653  CA  SER B 195      35.591   2.001 -38.895  1.00 16.91           C  
-ATOM   3654  C   SER B 195      37.066   1.683 -38.679  1.00 15.66           C  
-ATOM   3655  O   SER B 195      37.820   1.664 -39.637  1.00 14.69           O  
-ATOM   3656  CB  SER B 195      35.426   3.291 -39.707  1.00 16.78           C  
-ATOM   3657  OG  SER B 195      35.874   4.436 -38.990  1.00 16.36           O  
-ATOM   3658  N   ALA B 196      37.478   1.412 -37.440  1.00 15.08           N  
-ATOM   3659  CA  ALA B 196      38.916   1.251 -37.127  1.00 16.34           C  
-ATOM   3660  C   ALA B 196      39.618   0.181 -37.973  1.00 16.65           C  
-ATOM   3661  O   ALA B 196      40.771   0.341 -38.357  1.00 15.79           O  
-ATOM   3662  CB  ALA B 196      39.125   0.961 -35.625  1.00 16.23           C  
-ATOM   3663  N   ARG B 197      38.914  -0.909 -38.248  1.00 18.35           N  
-ATOM   3664  CA  ARG B 197      39.478  -1.996 -39.028  1.00 18.04           C  
-ATOM   3665  C   ARG B 197      39.715  -1.584 -40.487  1.00 16.35           C  
-ATOM   3666  O   ARG B 197      40.730  -1.954 -41.085  1.00 14.94           O  
-ATOM   3667  CB  ARG B 197      38.567  -3.202 -38.922  1.00 18.66           C  
-ATOM   3668  CG  ARG B 197      39.197  -4.445 -39.376  1.00 20.64           C  
-ATOM   3669  CD  ARG B 197      38.318  -5.622 -39.054  1.00 18.24           C  
-ATOM   3670  NE  ARG B 197      38.836  -6.745 -39.803  1.00 17.06           N  
-ATOM   3671  CZ  ARG B 197      39.769  -7.602 -39.389  1.00 17.12           C  
-ATOM   3672  NH1 ARG B 197      40.327  -7.543 -38.181  1.00 16.40           N  
-ATOM   3673  NH2 ARG B 197      40.126  -8.567 -40.213  1.00 18.43           N  
-ATOM   3674  N   PHE B 198      38.803  -0.804 -41.063  1.00 14.94           N  
-ATOM   3675  CA  PHE B 198      39.054  -0.245 -42.397  1.00 14.46           C  
-ATOM   3676  C   PHE B 198      40.345   0.549 -42.415  1.00 13.03           C  
-ATOM   3677  O   PHE B 198      41.189   0.358 -43.301  1.00 13.08           O  
-ATOM   3678  CB  PHE B 198      37.916   0.679 -42.828  1.00 15.68           C  
-ATOM   3679  CG  PHE B 198      38.102   1.264 -44.196  1.00 16.90           C  
-ATOM   3680  CD1 PHE B 198      37.750   0.535 -45.319  1.00 20.69           C  
-ATOM   3681  CD2 PHE B 198      38.611   2.534 -44.362  1.00 20.18           C  
-ATOM   3682  CE1 PHE B 198      37.914   1.066 -46.587  1.00 20.20           C  
-ATOM   3683  CE2 PHE B 198      38.775   3.077 -45.635  1.00 21.27           C  
-ATOM   3684  CZ  PHE B 198      38.425   2.336 -46.742  1.00 20.02           C  
-ATOM   3685  N   TYR B 199      40.496   1.443 -41.440  1.00 11.73           N  
-ATOM   3686  CA  TYR B 199      41.707   2.264 -41.349  1.00 12.88           C  
-ATOM   3687  C   TYR B 199      42.966   1.434 -41.127  1.00 13.63           C  
-ATOM   3688  O   TYR B 199      43.985   1.682 -41.776  1.00 13.58           O  
-ATOM   3689  CB  TYR B 199      41.575   3.329 -40.266  1.00 14.83           C  
-ATOM   3690  CG  TYR B 199      40.654   4.453 -40.660  1.00 14.72           C  
-ATOM   3691  CD1 TYR B 199      41.076   5.414 -41.555  1.00 16.01           C  
-ATOM   3692  CD2 TYR B 199      39.376   4.566 -40.127  1.00 15.86           C  
-ATOM   3693  CE1 TYR B 199      40.257   6.455 -41.936  1.00 19.50           C  
-ATOM   3694  CE2 TYR B 199      38.533   5.632 -40.502  1.00 16.54           C  
-ATOM   3695  CZ  TYR B 199      38.990   6.563 -41.405  1.00 16.74           C  
-ATOM   3696  OH  TYR B 199      38.194   7.613 -41.793  1.00 19.52           O  
-ATOM   3697  N   ALA B 200      42.894   0.448 -40.238  1.00 13.96           N  
-ATOM   3698  CA  ALA B 200      44.054  -0.375 -39.919  1.00 14.43           C  
-ATOM   3699  C   ALA B 200      44.538  -1.142 -41.150  1.00 13.48           C  
-ATOM   3700  O   ALA B 200      45.738  -1.225 -41.403  1.00 12.26           O  
-ATOM   3701  CB  ALA B 200      43.737  -1.362 -38.768  1.00 14.30           C  
-ATOM   3702  N   ILE B 201      43.610  -1.704 -41.914  1.00 13.67           N  
-ATOM   3703  CA  ILE B 201      43.984  -2.453 -43.116  1.00 13.39           C  
-ATOM   3704  C   ILE B 201      44.563  -1.504 -44.169  1.00 13.52           C  
-ATOM   3705  O   ILE B 201      45.591  -1.802 -44.802  1.00 13.98           O  
-ATOM   3706  CB  ILE B 201      42.801  -3.281 -43.684  1.00 13.77           C  
-ATOM   3707  CG1 ILE B 201      42.381  -4.376 -42.690  1.00 15.09           C  
-ATOM   3708  CG2 ILE B 201      43.190  -3.898 -45.040  1.00 14.83           C  
-ATOM   3709  CD1 ILE B 201      41.051  -5.048 -43.010  1.00 16.16           C  
-ATOM   3710  N   LYS B 202      43.923  -0.353 -44.361  1.00 14.48           N  
-ATOM   3711  CA  LYS B 202      44.447   0.634 -45.301  1.00 14.51           C  
-ATOM   3712  C   LYS B 202      45.860   1.091 -44.908  1.00 14.91           C  
-ATOM   3713  O   LYS B 202      46.716   1.268 -45.780  1.00 14.29           O  
-ATOM   3714  CB  LYS B 202      43.483   1.821 -45.464  1.00 16.80           C  
-ATOM   3715  CG  LYS B 202      42.174   1.425 -46.156  1.00 17.07           C  
-ATOM   3716  CD  LYS B 202      42.294   1.198 -47.675  1.00 21.89           C  
-ATOM   3717  CE  LYS B 202      41.413   0.019 -48.149  1.00 20.37           C  
-ATOM   3718  NZ  LYS B 202      41.555  -0.337 -49.589  1.00 24.08           N  
-ATOM   3719  N   LEU B 203      46.120   1.267 -43.615  1.00 13.57           N  
-ATOM   3720  CA  LEU B 203      47.476   1.628 -43.174  1.00 13.48           C  
-ATOM   3721  C   LEU B 203      48.487   0.518 -43.482  1.00 14.30           C  
-ATOM   3722  O   LEU B 203      49.615   0.824 -43.901  1.00 14.79           O  
-ATOM   3723  CB  LEU B 203      47.506   1.972 -41.692  1.00 13.22           C  
-ATOM   3724  CG  LEU B 203      46.894   3.322 -41.353  1.00 15.34           C  
-ATOM   3725  CD1 LEU B 203      46.619   3.401 -39.838  1.00 13.96           C  
-ATOM   3726  CD2 LEU B 203      47.796   4.479 -41.806  1.00 13.10           C  
-ATOM   3727  N   PHE B 204      48.065  -0.736 -43.289  1.00 14.39           N  
-ATOM   3728  CA  PHE B 204      48.898  -1.903 -43.598  1.00 14.86           C  
-ATOM   3729  C   PHE B 204      49.294  -1.918 -45.085  1.00 16.13           C  
-ATOM   3730  O   PHE B 204      50.458  -2.165 -45.398  1.00 16.74           O  
-ATOM   3731  CB  PHE B 204      48.211  -3.216 -43.198  1.00 12.87           C  
-ATOM   3732  CG  PHE B 204      49.081  -4.420 -43.412  1.00 15.68           C  
-ATOM   3733  CD1 PHE B 204      49.980  -4.827 -42.417  1.00 15.16           C  
-ATOM   3734  CD2 PHE B 204      49.025  -5.136 -44.608  1.00 13.92           C  
-ATOM   3735  CE1 PHE B 204      50.798  -5.943 -42.611  1.00 17.94           C  
-ATOM   3736  CE2 PHE B 204      49.849  -6.250 -44.822  1.00 15.41           C  
-ATOM   3737  CZ  PHE B 204      50.734  -6.655 -43.826  1.00 17.03           C  
-ATOM   3738  N  AGLU B 205      48.363  -1.646 -45.990  0.50 16.73           N  
-ATOM   3739  N  BGLU B 205      48.308  -1.638 -45.949  0.50 16.88           N  
-ATOM   3740  CA AGLU B 205      48.693  -1.625 -47.417  0.50 17.05           C  
-ATOM   3741  CA BGLU B 205      48.456  -1.524 -47.410  0.50 17.23           C  
-ATOM   3742  C  AGLU B 205      49.192  -0.245 -47.878  0.50 17.32           C  
-ATOM   3743  C  BGLU B 205      49.192  -0.254 -47.865  0.50 17.49           C  
-ATOM   3744  O  AGLU B 205      49.289   0.012 -49.085  0.50 16.54           O  
-ATOM   3745  O  BGLU B 205      49.455  -0.085 -49.062  0.50 17.08           O  
-ATOM   3746  CB AGLU B 205      47.496  -2.094 -48.235  0.50 16.85           C  
-ATOM   3747  CB BGLU B 205      47.078  -1.507 -48.101  0.50 17.05           C  
-ATOM   3748  CG AGLU B 205      46.385  -1.104 -48.263  0.50 16.33           C  
-ATOM   3749  CG BGLU B 205      46.187  -2.747 -47.959  0.50 17.37           C  
-ATOM   3750  CD AGLU B 205      45.063  -1.718 -48.639  0.50 16.24           C  
-ATOM   3751  CD BGLU B 205      44.913  -2.667 -48.818  0.50 18.29           C  
-ATOM   3752  OE1AGLU B 205      44.934  -2.962 -48.677  0.50 15.39           O  
-ATOM   3753  OE1BGLU B 205      43.807  -2.477 -48.272  0.50 20.08           O  
-ATOM   3754  OE2AGLU B 205      44.145  -0.928 -48.893  0.50 16.17           O  
-ATOM   3755  OE2BGLU B 205      45.004  -2.785 -50.057  0.50 19.72           O  
-ATOM   3756  N   GLN B 206      49.505   0.635 -46.921  1.00 16.99           N  
-ATOM   3757  CA  GLN B 206      50.149   1.922 -47.182  1.00 18.08           C  
-ATOM   3758  C   GLN B 206      49.347   2.822 -48.130  1.00 17.88           C  
-ATOM   3759  O   GLN B 206      49.882   3.452 -49.047  1.00 17.79           O  
-ATOM   3760  CB  GLN B 206      51.597   1.680 -47.618  1.00 20.29           C  
-ATOM   3761  CG  GLN B 206      52.354   0.859 -46.554  1.00 21.67           C  
-ATOM   3762  CD  GLN B 206      53.269  -0.168 -47.168  1.00 24.27           C  
-ATOM   3763  OE1 GLN B 206      54.202   0.182 -47.860  1.00 27.39           O  
-ATOM   3764  NE2 GLN B 206      53.004  -1.444 -46.908  1.00 27.58           N  
-ATOM   3765  N   ASP B 207      48.046   2.859 -47.861  1.00 16.71           N  
-ATOM   3766  CA  ASP B 207      47.093   3.693 -48.595  1.00 16.89           C  
-ATOM   3767  C   ASP B 207      47.441   5.161 -48.380  1.00 17.24           C  
-ATOM   3768  O   ASP B 207      47.367   5.655 -47.264  1.00 15.13           O  
-ATOM   3769  CB  ASP B 207      45.675   3.403 -48.094  1.00 14.96           C  
-ATOM   3770  CG  ASP B 207      44.611   4.132 -48.879  1.00 17.29           C  
-ATOM   3771  OD1 ASP B 207      44.003   3.495 -49.766  1.00 13.69           O  
-ATOM   3772  OD2 ASP B 207      44.369   5.329 -48.605  1.00 17.67           O  
-ATOM   3773  N   SER B 208      47.826   5.849 -49.454  1.00 17.67           N  
-ATOM   3774  CA  SER B 208      48.266   7.255 -49.379  1.00 19.20           C  
-ATOM   3775  C   SER B 208      47.201   8.229 -48.839  1.00 18.36           C  
-ATOM   3776  O   SER B 208      47.537   9.171 -48.121  1.00 18.13           O  
-ATOM   3777  CB  SER B 208      48.731   7.739 -50.758  1.00 19.66           C  
-ATOM   3778  OG  SER B 208      47.689   7.630 -51.719  1.00 21.94           O  
-ATOM   3779  N   LEU B 209      45.932   7.997 -49.167  1.00 18.54           N  
-ATOM   3780  CA  LEU B 209      44.853   8.879 -48.706  1.00 19.10           C  
-ATOM   3781  C   LEU B 209      44.580   8.756 -47.206  1.00 17.17           C  
-ATOM   3782  O   LEU B 209      44.389   9.766 -46.522  1.00 18.27           O  
-ATOM   3783  CB  LEU B 209      43.563   8.651 -49.493  1.00 20.04           C  
-ATOM   3784  CG  LEU B 209      43.524   9.108 -50.954  1.00 23.45           C  
-ATOM   3785  CD1 LEU B 209      42.136   8.782 -51.487  1.00 24.97           C  
-ATOM   3786  CD2 LEU B 209      43.828  10.610 -51.136  1.00 24.60           C  
-ATOM   3787  N   VAL B 210      44.569   7.524 -46.699  1.00 16.50           N  
-ATOM   3788  CA  VAL B 210      44.424   7.285 -45.271  1.00 15.62           C  
-ATOM   3789  C   VAL B 210      45.622   7.851 -44.486  1.00 15.51           C  
-ATOM   3790  O   VAL B 210      45.422   8.479 -43.455  1.00 16.97           O  
-ATOM   3791  CB  VAL B 210      44.182   5.790 -44.965  1.00 15.62           C  
-ATOM   3792  CG1 VAL B 210      44.354   5.477 -43.487  1.00 17.40           C  
-ATOM   3793  CG2 VAL B 210      42.760   5.402 -45.437  1.00 16.18           C  
-ATOM   3794  N   GLU B 211      46.848   7.627 -44.965  1.00 15.92           N  
-ATOM   3795  CA  GLU B 211      48.032   8.190 -44.301  1.00 15.84           C  
-ATOM   3796  C   GLU B 211      47.915   9.712 -44.174  1.00 16.84           C  
-ATOM   3797  O   GLU B 211      48.187  10.270 -43.117  1.00 16.51           O  
-ATOM   3798  CB  GLU B 211      49.309   7.798 -45.043  1.00 15.84           C  
-ATOM   3799  CG  GLU B 211      49.689   6.331 -44.839  1.00 16.50           C  
-ATOM   3800  CD  GLU B 211      50.849   5.867 -45.696  1.00 19.00           C  
-ATOM   3801  OE1 GLU B 211      51.463   6.693 -46.409  1.00 17.12           O  
-ATOM   3802  OE2 GLU B 211      51.148   4.658 -45.663  1.00 15.46           O  
-ATOM   3803  N   ALA B 212      47.494  10.361 -45.255  1.00 16.52           N  
-ATOM   3804  CA  ALA B 212      47.324  11.827 -45.301  1.00 18.29           C  
-ATOM   3805  C   ALA B 212      46.250  12.323 -44.349  1.00 18.29           C  
-ATOM   3806  O   ALA B 212      46.464  13.273 -43.594  1.00 19.37           O  
-ATOM   3807  CB  ALA B 212      47.027  12.291 -46.742  1.00 16.66           C  
-ATOM   3808  N   GLU B 213      45.106  11.652 -44.384  1.00 21.29           N  
-ATOM   3809  CA  GLU B 213      43.963  11.933 -43.516  1.00 21.84           C  
-ATOM   3810  C   GLU B 213      44.317  11.859 -42.026  1.00 22.13           C  
-ATOM   3811  O   GLU B 213      43.931  12.729 -41.243  1.00 20.18           O  
-ATOM   3812  CB  GLU B 213      42.873  10.910 -43.854  1.00 23.03           C  
-ATOM   3813  CG  GLU B 213      41.584  10.982 -43.089  1.00 27.96           C  
-ATOM   3814  CD  GLU B 213      40.571   9.961 -43.580  1.00 28.86           C  
-ATOM   3815  OE1 GLU B 213      40.908   9.077 -44.407  1.00 31.60           O  
-ATOM   3816  OE2 GLU B 213      39.425  10.038 -43.117  1.00 35.37           O  
-ATOM   3817  N   LEU B 214      45.075  10.834 -41.634  1.00 20.93           N  
-ATOM   3818  CA  LEU B 214      45.357  10.603 -40.212  1.00 21.71           C  
-ATOM   3819  C   LEU B 214      46.561  11.352 -39.636  1.00 21.62           C  
-ATOM   3820  O   LEU B 214      46.593  11.580 -38.442  1.00 22.92           O  
-ATOM   3821  CB  LEU B 214      45.508   9.105 -39.933  1.00 20.37           C  
-ATOM   3822  CG  LEU B 214      44.274   8.242 -40.233  1.00 19.67           C  
-ATOM   3823  CD1 LEU B 214      44.570   6.785 -39.909  1.00 18.32           C  
-ATOM   3824  CD2 LEU B 214      43.038   8.707 -39.483  1.00 21.15           C  
-ATOM   3825  N   ASP B 215      47.530  11.717 -40.472  1.00 21.89           N  
-ATOM   3826  CA  ASP B 215      48.735  12.464 -40.072  1.00 22.48           C  
-ATOM   3827  C   ASP B 215      49.290  11.992 -38.724  1.00 21.80           C  
-ATOM   3828  O   ASP B 215      49.265  12.707 -37.712  1.00 20.14           O  
-ATOM   3829  CB  ASP B 215      48.460  13.973 -40.068  1.00 23.44           C  
-ATOM   3830  CG  ASP B 215      49.734  14.799 -39.928  1.00 26.31           C  
-ATOM   3831  OD1 ASP B 215      50.835  14.312 -40.293  1.00 24.09           O  
-ATOM   3832  OD2 ASP B 215      49.626  15.952 -39.451  1.00 31.37           O  
-ATOM   3833  N   LEU B 216      49.785  10.762 -38.722  1.00 21.02           N  
-ATOM   3834  CA  LEU B 216      50.153  10.083 -37.476  1.00 19.37           C  
-ATOM   3835  C   LEU B 216      51.425  10.669 -36.873  1.00 19.25           C  
-ATOM   3836  O   LEU B 216      52.188  11.355 -37.549  1.00 18.04           O  
-ATOM   3837  CB  LEU B 216      50.285   8.571 -37.721  1.00 19.62           C  
-ATOM   3838  CG  LEU B 216      49.021   7.853 -38.219  1.00 18.08           C  
-ATOM   3839  CD1 LEU B 216      49.319   6.392 -38.656  1.00 16.29           C  
-ATOM   3840  CD2 LEU B 216      47.896   7.886 -37.187  1.00 16.52           C  
-ATOM   3841  N   SER B 217      51.633  10.419 -35.588  1.00 18.78           N  
-ATOM   3842  CA  SER B 217      52.848  10.848 -34.914  1.00 19.38           C  
-ATOM   3843  C   SER B 217      54.057  10.071 -35.428  1.00 20.33           C  
-ATOM   3844  O   SER B 217      53.915   9.016 -36.070  1.00 20.89           O  
-ATOM   3845  CB  SER B 217      52.704  10.664 -33.397  1.00 20.57           C  
-ATOM   3846  OG  SER B 217      52.726   9.289 -33.056  1.00 21.56           O  
-ATOM   3847  N   GLN B 218      55.249  10.592 -35.139  1.00 19.72           N  
-ATOM   3848  CA  GLN B 218      56.485   9.906 -35.457  1.00 20.62           C  
-ATOM   3849  C   GLN B 218      56.489   8.500 -34.863  1.00 19.84           C  
-ATOM   3850  O   GLN B 218      56.877   7.546 -35.537  1.00 19.68           O  
-ATOM   3851  CB  GLN B 218      57.699  10.674 -34.946  1.00 20.73           C  
-ATOM   3852  CG  GLN B 218      59.000   9.926 -35.166  1.00 21.99           C  
-ATOM   3853  CD  GLN B 218      60.227  10.795 -35.004  1.00 23.27           C  
-ATOM   3854  OE1 GLN B 218      60.218  11.757 -34.247  1.00 24.63           O  
-ATOM   3855  NE2 GLN B 218      61.292  10.450 -35.715  1.00 25.09           N  
-ATOM   3856  N   PHE B 219      56.071   8.389 -33.607  1.00 18.60           N  
-ATOM   3857  CA  PHE B 219      56.042   7.094 -32.934  1.00 18.56           C  
-ATOM   3858  C   PHE B 219      55.057   6.125 -33.601  1.00 17.97           C  
-ATOM   3859  O   PHE B 219      55.401   4.977 -33.830  1.00 17.66           O  
-ATOM   3860  CB  PHE B 219      55.725   7.230 -31.443  1.00 18.26           C  
-ATOM   3861  CG  PHE B 219      55.702   5.913 -30.729  1.00 18.13           C  
-ATOM   3862  CD1 PHE B 219      56.852   5.138 -30.677  1.00 21.97           C  
-ATOM   3863  CD2 PHE B 219      54.542   5.439 -30.138  1.00 18.86           C  
-ATOM   3864  CE1 PHE B 219      56.846   3.897 -30.034  1.00 21.80           C  
-ATOM   3865  CE2 PHE B 219      54.530   4.201 -29.483  1.00 21.72           C  
-ATOM   3866  CZ  PHE B 219      55.681   3.434 -29.436  1.00 19.07           C  
-ATOM   3867  N   GLN B 220      53.853   6.592 -33.911  1.00 18.50           N  
-ATOM   3868  CA  GLN B 220      52.857   5.775 -34.611  1.00 17.81           C  
-ATOM   3869  C   GLN B 220      53.377   5.292 -35.971  1.00 17.82           C  
-ATOM   3870  O   GLN B 220      53.191   4.115 -36.322  1.00 15.94           O  
-ATOM   3871  CB  GLN B 220      51.520   6.515 -34.758  1.00 17.64           C  
-ATOM   3872  CG  GLN B 220      50.672   6.593 -33.505  1.00 17.22           C  
-ATOM   3873  CD  GLN B 220      49.486   7.550 -33.632  1.00 19.80           C  
-ATOM   3874  OE1 GLN B 220      49.630   8.655 -34.160  1.00 20.56           O  
-ATOM   3875  NE2 GLN B 220      48.319   7.133 -33.148  1.00 17.76           N  
-ATOM   3876  N   ARG B 221      54.039   6.173 -36.727  1.00 17.71           N  
-ATOM   3877  CA  ARG B 221      54.618   5.794 -38.031  1.00 18.42           C  
-ATOM   3878  C   ARG B 221      55.648   4.673 -37.878  1.00 19.14           C  
-ATOM   3879  O   ARG B 221      55.644   3.718 -38.660  1.00 16.87           O  
-ATOM   3880  CB  ARG B 221      55.283   6.987 -38.738  1.00 18.54           C  
-ATOM   3881  CG  ARG B 221      54.305   8.074 -39.172  1.00 18.37           C  
-ATOM   3882  CD  ARG B 221      54.986   9.438 -39.388  1.00 20.01           C  
-ATOM   3883  NE  ARG B 221      53.942  10.437 -39.607  1.00 22.17           N  
-ATOM   3884  CZ  ARG B 221      53.485  10.846 -40.789  1.00 20.05           C  
-ATOM   3885  NH1 ARG B 221      53.977  10.376 -41.936  1.00 20.66           N  
-ATOM   3886  NH2 ARG B 221      52.507  11.739 -40.816  1.00 20.36           N  
-ATOM   3887  N   LYS B 222      56.528   4.798 -36.877  1.00 18.66           N  
-ATOM   3888  CA  LYS B 222      57.552   3.785 -36.622  1.00 18.40           C  
-ATOM   3889  C   LYS B 222      56.923   2.449 -36.241  1.00 16.68           C  
-ATOM   3890  O   LYS B 222      57.333   1.419 -36.762  1.00 15.44           O  
-ATOM   3891  CB  LYS B 222      58.538   4.236 -35.533  1.00 21.35           C  
-ATOM   3892  CG  LYS B 222      59.444   5.386 -35.995  1.00 24.62           C  
-ATOM   3893  CD  LYS B 222      60.207   6.086 -34.855  1.00 26.79           C  
-ATOM   3894  CE  LYS B 222      61.279   5.223 -34.247  1.00 29.47           C  
-ATOM   3895  NZ  LYS B 222      62.298   6.051 -33.513  1.00 28.58           N  
-ATOM   3896  N   GLU B 223      55.933   2.489 -35.350  1.00 17.26           N  
-ATOM   3897  CA  GLU B 223      55.223   1.283 -34.917  1.00 17.69           C  
-ATOM   3898  C   GLU B 223      54.605   0.530 -36.105  1.00 15.77           C  
-ATOM   3899  O   GLU B 223      54.740  -0.683 -36.219  1.00 15.43           O  
-ATOM   3900  CB  GLU B 223      54.088   1.616 -33.949  1.00 18.98           C  
-ATOM   3901  CG  GLU B 223      54.468   2.043 -32.525  1.00 22.82           C  
-ATOM   3902  CD  GLU B 223      53.206   2.300 -31.696  1.00 23.66           C  
-ATOM   3903  OE1 GLU B 223      52.539   3.344 -31.896  1.00 27.16           O  
-ATOM   3904  OE2 GLU B 223      52.880   1.458 -30.843  1.00 25.52           O  
-ATOM   3905  N   ILE B 224      53.920   1.269 -36.970  1.00 14.91           N  
-ATOM   3906  CA  ILE B 224      53.258   0.694 -38.151  1.00 14.69           C  
-ATOM   3907  C   ILE B 224      54.273   0.188 -39.177  1.00 13.34           C  
-ATOM   3908  O   ILE B 224      54.098  -0.893 -39.762  1.00 13.47           O  
-ATOM   3909  CB  ILE B 224      52.235   1.707 -38.755  1.00 14.89           C  
-ATOM   3910  CG1 ILE B 224      51.132   1.945 -37.722  1.00 15.95           C  
-ATOM   3911  CG2 ILE B 224      51.682   1.194 -40.096  1.00 15.81           C  
-ATOM   3912  CD1 ILE B 224      50.203   3.109 -38.025  1.00 14.67           C  
-ATOM   3913  N   GLU B 225      55.350   0.943 -39.400  1.00 13.42           N  
-ATOM   3914  CA  GLU B 225      56.418   0.487 -40.304  1.00 15.56           C  
-ATOM   3915  C   GLU B 225      56.980  -0.851 -39.843  1.00 14.58           C  
-ATOM   3916  O   GLU B 225      57.239  -1.743 -40.656  1.00 14.32           O  
-ATOM   3917  CB  GLU B 225      57.582   1.490 -40.379  1.00 17.32           C  
-ATOM   3918  CG  GLU B 225      57.329   2.705 -41.247  1.00 21.26           C  
-ATOM   3919  CD  GLU B 225      58.382   3.817 -41.070  1.00 26.82           C  
-ATOM   3920  OE1 GLU B 225      59.341   3.644 -40.283  1.00 27.86           O  
-ATOM   3921  OE2 GLU B 225      58.231   4.881 -41.704  1.00 27.50           O  
-ATOM   3922  N   ASP B 226      57.172  -0.976 -38.529  1.00 15.75           N  
-ATOM   3923  CA  ASP B 226      57.679  -2.211 -37.922  1.00 15.43           C  
-ATOM   3924  C   ASP B 226      56.735  -3.394 -38.165  1.00 13.42           C  
-ATOM   3925  O   ASP B 226      57.183  -4.479 -38.550  1.00 13.71           O  
-ATOM   3926  CB  ASP B 226      57.891  -2.036 -36.409  1.00 16.08           C  
-ATOM   3927  CG  ASP B 226      59.173  -1.272 -36.055  1.00 18.92           C  
-ATOM   3928  OD1 ASP B 226      60.022  -1.008 -36.936  1.00 19.70           O  
-ATOM   3929  OD2 ASP B 226      59.325  -0.942 -34.862  1.00 18.90           O  
-ATOM   3930  N   ILE B 227      55.444  -3.178 -37.924  1.00 12.91           N  
-ATOM   3931  CA  ILE B 227      54.426  -4.202 -38.152  1.00 12.59           C  
-ATOM   3932  C   ILE B 227      54.424  -4.625 -39.626  1.00 12.99           C  
-ATOM   3933  O   ILE B 227      54.451  -5.816 -39.935  1.00 13.33           O  
-ATOM   3934  CB  ILE B 227      53.021  -3.724 -37.718  1.00 12.66           C  
-ATOM   3935  CG1 ILE B 227      52.982  -3.484 -36.202  1.00 12.60           C  
-ATOM   3936  CG2 ILE B 227      51.955  -4.748 -38.151  1.00 12.50           C  
-ATOM   3937  CD1 ILE B 227      51.893  -2.545 -35.714  1.00 14.18           C  
-ATOM   3938  N   ILE B 228      54.401  -3.668 -40.542  1.00 15.23           N  
-ATOM   3939  CA  ILE B 228      54.419  -4.034 -41.978  1.00 15.51           C  
-ATOM   3940  C   ILE B 228      55.674  -4.853 -42.322  1.00 16.40           C  
-ATOM   3941  O   ILE B 228      55.567  -5.898 -42.959  1.00 15.18           O  
-ATOM   3942  CB  ILE B 228      54.297  -2.814 -42.884  1.00 15.62           C  
-ATOM   3943  CG1 ILE B 228      52.920  -2.154 -42.703  1.00 15.80           C  
-ATOM   3944  CG2 ILE B 228      54.514  -3.198 -44.348  1.00 16.81           C  
-ATOM   3945  CD1 ILE B 228      52.905  -0.688 -43.212  1.00 15.40           C  
-ATOM   3946  N   ARG B 229      56.842  -4.406 -41.858  1.00 16.74           N  
-ATOM   3947  CA  ARG B 229      58.115  -5.031 -42.219  1.00 17.42           C  
-ATOM   3948  C   ARG B 229      58.211  -6.500 -41.790  1.00 16.36           C  
-ATOM   3949  O   ARG B 229      58.523  -7.372 -42.617  1.00 14.57           O  
-ATOM   3950  CB  ARG B 229      59.285  -4.211 -41.637  1.00 20.17           C  
-ATOM   3951  CG  ARG B 229      60.680  -4.768 -41.968  1.00 23.33           C  
-ATOM   3952  CD  ARG B 229      61.812  -3.870 -41.422  1.00 25.37           C  
-ATOM   3953  NE  ARG B 229      61.570  -3.455 -40.038  1.00 30.45           N  
-ATOM   3954  CZ  ARG B 229      61.663  -4.249 -38.974  1.00 30.76           C  
-ATOM   3955  NH1 ARG B 229      61.997  -5.531 -39.113  1.00 34.96           N  
-ATOM   3956  NH2 ARG B 229      61.414  -3.759 -37.758  1.00 31.30           N  
-ATOM   3957  N   ILE B 230      57.951  -6.780 -40.510  1.00 15.32           N  
-ATOM   3958  CA  ILE B 230      57.967  -8.164 -40.017  1.00 14.38           C  
-ATOM   3959  C   ILE B 230      56.864  -9.027 -40.661  1.00 14.09           C  
-ATOM   3960  O   ILE B 230      57.088 -10.204 -40.952  1.00 13.73           O  
-ATOM   3961  CB  ILE B 230      57.958  -8.246 -38.448  1.00 14.31           C  
-ATOM   3962  CG1 ILE B 230      58.155  -9.680 -37.970  1.00 13.96           C  
-ATOM   3963  CG2 ILE B 230      56.677  -7.655 -37.835  1.00 14.71           C  
-ATOM   3964  CD1 ILE B 230      59.506 -10.286 -38.391  1.00 16.85           C  
-ATOM   3965  N   THR B 231      55.684  -8.451 -40.908  1.00 14.50           N  
-ATOM   3966  CA  THR B 231      54.602  -9.185 -41.544  1.00 13.41           C  
-ATOM   3967  C   THR B 231      54.971  -9.542 -43.006  1.00 13.86           C  
-ATOM   3968  O   THR B 231      54.799 -10.680 -43.423  1.00 15.52           O  
-ATOM   3969  CB  THR B 231      53.272  -8.403 -41.435  1.00 13.54           C  
-ATOM   3970  OG1 THR B 231      53.034  -8.122 -40.046  1.00 13.25           O  
-ATOM   3971  CG2 THR B 231      52.109  -9.224 -41.972  1.00 12.58           C  
-ATOM   3972  N   GLU B 232      55.490  -8.588 -43.770  1.00 13.71           N  
-ATOM   3973  CA  GLU B 232      55.986  -8.889 -45.125  1.00 15.01           C  
-ATOM   3974  C   GLU B 232      57.023 -10.027 -45.140  1.00 16.60           C  
-ATOM   3975  O   GLU B 232      56.990 -10.906 -46.018  1.00 15.20           O  
-ATOM   3976  CB  GLU B 232      56.557  -7.643 -45.783  1.00 16.24           C  
-ATOM   3977  CG  GLU B 232      55.489  -6.628 -46.186  1.00 16.60           C  
-ATOM   3978  CD  GLU B 232      56.079  -5.409 -46.859  1.00 18.93           C  
-ATOM   3979  OE1 GLU B 232      57.209  -5.009 -46.507  1.00 17.87           O  
-ATOM   3980  OE2 GLU B 232      55.408  -4.846 -47.735  1.00 17.58           O  
-ATOM   3981  N   GLU B 233      57.911 -10.019 -44.151  1.00 18.59           N  
-ATOM   3982  CA  GLU B 233      58.957 -11.052 -44.035  1.00 20.24           C  
-ATOM   3983  C   GLU B 233      58.385 -12.443 -43.773  1.00 19.90           C  
-ATOM   3984  O   GLU B 233      58.842 -13.423 -44.371  1.00 18.08           O  
-ATOM   3985  CB  GLU B 233      59.971 -10.668 -42.957  1.00 23.04           C  
-ATOM   3986  CG  GLU B 233      60.817  -9.453 -43.369  1.00 27.19           C  
-ATOM   3987  CD  GLU B 233      61.653  -8.839 -42.252  1.00 31.42           C  
-ATOM   3988  OE1 GLU B 233      61.505  -9.238 -41.078  1.00 33.73           O  
-ATOM   3989  OE2 GLU B 233      62.472  -7.938 -42.555  1.00 34.45           O  
-ATOM   3990  N   ILE B 234      57.382 -12.555 -42.906  1.00 18.21           N  
-ATOM   3991  CA  ILE B 234      56.811 -13.887 -42.627  1.00 18.80           C  
-ATOM   3992  C   ILE B 234      55.910 -14.430 -43.756  1.00 20.21           C  
-ATOM   3993  O   ILE B 234      55.785 -15.644 -43.893  1.00 21.54           O  
-ATOM   3994  CB  ILE B 234      56.124 -13.996 -41.245  1.00 18.45           C  
-ATOM   3995  CG1 ILE B 234      54.886 -13.099 -41.129  1.00 19.21           C  
-ATOM   3996  CG2 ILE B 234      57.151 -13.746 -40.138  1.00 19.63           C  
-ATOM   3997  CD1 ILE B 234      54.271 -13.089 -39.742  1.00 18.36           C  
-ATOM   3998  N   PHE B 235      55.297 -13.547 -44.545  1.00 18.93           N  
-ATOM   3999  CA  PHE B 235      54.553 -13.938 -45.750  1.00 19.49           C  
-ATOM   4000  C   PHE B 235      55.419 -14.053 -47.019  1.00 19.24           C  
-ATOM   4001  O   PHE B 235      54.983 -14.658 -48.004  1.00 19.39           O  
-ATOM   4002  CB  PHE B 235      53.468 -12.887 -46.060  1.00 19.52           C  
-ATOM   4003  CG  PHE B 235      52.189 -13.035 -45.279  1.00 18.33           C  
-ATOM   4004  CD1 PHE B 235      51.169 -13.836 -45.764  1.00 18.69           C  
-ATOM   4005  CD2 PHE B 235      51.989 -12.345 -44.081  1.00 16.99           C  
-ATOM   4006  CE1 PHE B 235      49.963 -13.967 -45.069  1.00 18.21           C  
-ATOM   4007  CE2 PHE B 235      50.791 -12.460 -43.379  1.00 18.21           C  
-ATOM   4008  CZ  PHE B 235      49.772 -13.284 -43.876  1.00 17.90           C  
-ATOM   4009  N  ATHR B 236      56.636 -13.498 -46.979  0.70 19.76           N  
-ATOM   4010  N  BTHR B 236      56.617 -13.466 -46.970  0.30 19.63           N  
-ATOM   4011  CA ATHR B 236      57.510 -13.274 -48.152  0.70 19.78           C  
-ATOM   4012  CA BTHR B 236      57.499 -13.261 -48.124  0.30 19.63           C  
-ATOM   4013  C  ATHR B 236      56.733 -12.647 -49.322  0.70 21.40           C  
-ATOM   4014  C  BTHR B 236      56.750 -12.637 -49.305  0.30 20.80           C  
-ATOM   4015  O  ATHR B 236      56.827 -13.089 -50.476  0.70 20.43           O  
-ATOM   4016  O  BTHR B 236      56.885 -13.077 -50.451  0.30 20.42           O  
-ATOM   4017  CB ATHR B 236      58.341 -14.527 -48.576  0.70 20.02           C  
-ATOM   4018  CB BTHR B 236      58.213 -14.539 -48.581  0.30 19.53           C  
-ATOM   4019  OG1ATHR B 236      57.475 -15.647 -48.792  0.70 19.85           O  
-ATOM   4020  OG1BTHR B 236      58.339 -15.454 -47.484  0.30 18.15           O  
-ATOM   4021  CG2ATHR B 236      59.369 -14.862 -47.492  0.70 19.99           C  
-ATOM   4022  CG2BTHR B 236      59.579 -14.163 -49.100  0.30 18.92           C  
-ATOM   4023  N   GLU B 237      55.965 -11.608 -48.995  1.00 21.14           N  
-ATOM   4024  CA  GLU B 237      55.145 -10.916 -49.960  1.00 21.94           C  
-ATOM   4025  C   GLU B 237      54.979  -9.468 -49.506  1.00 20.86           C  
-ATOM   4026  O   GLU B 237      54.998  -9.199 -48.307  1.00 20.83           O  
-ATOM   4027  CB  GLU B 237      53.783 -11.610 -50.030  1.00 22.51           C  
-ATOM   4028  CG  GLU B 237      52.839 -11.026 -51.041  1.00 27.05           C  
-ATOM   4029  CD  GLU B 237      53.369 -11.139 -52.467  1.00 26.93           C  
-ATOM   4030  OE1 GLU B 237      53.112 -12.182 -53.086  1.00 27.60           O  
-ATOM   4031  OE2 GLU B 237      54.037 -10.191 -52.949  1.00 28.69           O  
-ATOM   4032  N   ASP B 238      54.814  -8.555 -50.457  1.00 18.28           N  
-ATOM   4033  CA  ASP B 238      54.577  -7.152 -50.138  1.00 20.11           C  
-ATOM   4034  C   ASP B 238      53.187  -6.992 -49.521  1.00 18.45           C  
-ATOM   4035  O   ASP B 238      52.267  -7.774 -49.806  1.00 18.26           O  
-ATOM   4036  CB  ASP B 238      54.757  -6.242 -51.372  1.00 21.89           C  
-ATOM   4037  CG  ASP B 238      53.675  -6.429 -52.408  1.00 24.51           C  
-ATOM   4038  OD1 ASP B 238      53.889  -7.239 -53.328  1.00 33.22           O  
-ATOM   4039  OD2 ASP B 238      52.606  -5.796 -52.308  1.00 25.18           O  
-ATOM   4040  N   ALA B 239      53.054  -5.969 -48.680  1.00 18.99           N  
-ATOM   4041  CA  ALA B 239      51.846  -5.718 -47.891  1.00 16.73           C  
-ATOM   4042  C   ALA B 239      50.586  -5.623 -48.737  1.00 18.18           C  
-ATOM   4043  O   ALA B 239      49.586  -6.254 -48.401  1.00 16.86           O  
-ATOM   4044  CB  ALA B 239      52.003  -4.460 -47.075  1.00 15.31           C  
-ATOM   4045  N   GLU B 240      50.623  -4.861 -49.832  1.00 19.28           N  
-ATOM   4046  CA  GLU B 240      49.408  -4.744 -50.670  1.00 20.23           C  
-ATOM   4047  C   GLU B 240      48.944  -6.112 -51.179  1.00 19.02           C  
-ATOM   4048  O   GLU B 240      47.755  -6.416 -51.148  1.00 18.29           O  
-ATOM   4049  CB  GLU B 240      49.577  -3.784 -51.848  1.00 22.25           C  
-ATOM   4050  CG  GLU B 240      48.246  -3.635 -52.600  1.00 26.62           C  
-ATOM   4051  CD  GLU B 240      48.221  -2.536 -53.629  1.00 30.90           C  
-ATOM   4052  OE1 GLU B 240      49.301  -2.060 -54.051  1.00 34.91           O  
-ATOM   4053  OE2 GLU B 240      47.091  -2.166 -54.017  1.00 32.98           O  
-ATOM   4054  N   SER B 241      49.893  -6.925 -51.637  1.00 17.35           N  
-ATOM   4055  CA  SER B 241      49.601  -8.276 -52.119  1.00 17.23           C  
-ATOM   4056  C   SER B 241      49.094  -9.212 -51.028  1.00 16.21           C  
-ATOM   4057  O   SER B 241      48.233 -10.043 -51.289  1.00 15.49           O  
-ATOM   4058  CB  SER B 241      50.836  -8.875 -52.779  1.00 16.54           C  
-ATOM   4059  OG  SER B 241      51.178  -8.136 -53.933  1.00 20.50           O  
-ATOM   4060  N   ILE B 242      49.639  -9.097 -49.823  1.00 14.65           N  
-ATOM   4061  CA  ILE B 242      49.151  -9.890 -48.693  1.00 14.89           C  
-ATOM   4062  C   ILE B 242      47.640  -9.650 -48.503  1.00 14.73           C  
-ATOM   4063  O   ILE B 242      46.868 -10.600 -48.387  1.00 14.44           O  
-ATOM   4064  CB  ILE B 242      49.916  -9.557 -47.393  1.00 15.87           C  
-ATOM   4065  CG1 ILE B 242      51.344 -10.110 -47.446  1.00 14.96           C  
-ATOM   4066  CG2 ILE B 242      49.193 -10.142 -46.167  1.00 15.57           C  
-ATOM   4067  CD1 ILE B 242      52.229  -9.586 -46.344  1.00 14.42           C  
-ATOM   4068  N   VAL B 243      47.225  -8.386 -48.515  1.00 14.08           N  
-ATOM   4069  CA  VAL B 243      45.812  -8.072 -48.294  1.00 13.96           C  
-ATOM   4070  C   VAL B 243      44.937  -8.585 -49.440  1.00 12.68           C  
-ATOM   4071  O   VAL B 243      43.891  -9.192 -49.189  1.00 13.60           O  
-ATOM   4072  CB  VAL B 243      45.579  -6.580 -48.004  1.00 13.33           C  
-ATOM   4073  CG1 VAL B 243      44.087  -6.326 -47.772  1.00 13.64           C  
-ATOM   4074  CG2 VAL B 243      46.371  -6.160 -46.766  1.00 15.33           C  
-ATOM   4075  N   ILE B 244      45.375  -8.342 -50.679  1.00 15.57           N  
-ATOM   4076  CA  ILE B 244      44.674  -8.830 -51.880  1.00 15.27           C  
-ATOM   4077  C   ILE B 244      44.466 -10.340 -51.784  1.00 14.59           C  
-ATOM   4078  O   ILE B 244      43.339 -10.827 -51.924  1.00 14.79           O  
-ATOM   4079  CB  ILE B 244      45.441  -8.453 -53.193  1.00 15.67           C  
-ATOM   4080  CG1 ILE B 244      45.424  -6.941 -53.457  1.00 18.10           C  
-ATOM   4081  CG2 ILE B 244      44.855  -9.186 -54.398  1.00 17.85           C  
-ATOM   4082  CD1 ILE B 244      46.486  -6.481 -54.493  1.00 19.56           C  
-ATOM   4083  N   ASN B 245      45.555 -11.066 -51.510  1.00 14.49           N  
-ATOM   4084  CA  ASN B 245      45.523 -12.525 -51.369  1.00 14.85           C  
-ATOM   4085  C   ASN B 245      44.619 -12.993 -50.244  1.00 14.81           C  
-ATOM   4086  O   ASN B 245      43.857 -13.951 -50.421  1.00 13.78           O  
-ATOM   4087  CB  ASN B 245      46.943 -13.094 -51.199  1.00 16.61           C  
-ATOM   4088  CG  ASN B 245      47.808 -12.904 -52.446  1.00 19.39           C  
-ATOM   4089  OD1 ASN B 245      47.303 -12.608 -53.524  1.00 21.40           O  
-ATOM   4090  ND2 ASN B 245      49.121 -13.079 -52.297  1.00 21.08           N  
-ATOM   4091  N   GLU B 246      44.663 -12.314 -49.099  1.00 14.40           N  
-ATOM   4092  CA  GLU B 246      43.792 -12.686 -47.980  1.00 14.80           C  
-ATOM   4093  C   GLU B 246      42.301 -12.434 -48.250  1.00 14.69           C  
-ATOM   4094  O   GLU B 246      41.447 -13.228 -47.837  1.00 13.58           O  
-ATOM   4095  CB  GLU B 246      44.228 -11.996 -46.683  1.00 14.68           C  
-ATOM   4096  CG  GLU B 246      45.531 -12.545 -46.109  1.00 16.60           C  
-ATOM   4097  CD  GLU B 246      45.436 -14.008 -45.722  1.00 17.10           C  
-ATOM   4098  OE1 GLU B 246      44.426 -14.397 -45.108  1.00 16.33           O  
-ATOM   4099  OE2 GLU B 246      46.371 -14.771 -46.048  1.00 18.18           O  
-ATOM   4100  N   ARG B 247      41.996 -11.335 -48.936  1.00 14.92           N  
-ATOM   4101  CA  ARG B 247      40.629 -11.065 -49.342  1.00 14.29           C  
-ATOM   4102  C   ARG B 247      40.110 -12.188 -50.234  1.00 13.47           C  
-ATOM   4103  O   ARG B 247      39.027 -12.723 -49.984  1.00 13.73           O  
-ATOM   4104  CB  ARG B 247      40.510  -9.735 -50.078  1.00 14.38           C  
-ATOM   4105  CG  ARG B 247      40.635  -8.517 -49.211  1.00 14.77           C  
-ATOM   4106  CD  ARG B 247      40.255  -7.252 -49.970  1.00 15.33           C  
-ATOM   4107  NE  ARG B 247      40.710  -6.087 -49.234  1.00 15.29           N  
-ATOM   4108  CZ  ARG B 247      40.146  -5.638 -48.112  1.00 17.29           C  
-ATOM   4109  NH1 ARG B 247      39.075  -6.226 -47.598  1.00 16.58           N  
-ATOM   4110  NH2 ARG B 247      40.653  -4.582 -47.500  1.00 17.32           N  
-ATOM   4111  N   TYR B 248      40.882 -12.544 -51.262  1.00 16.14           N  
-ATOM   4112  CA  TYR B 248      40.444 -13.587 -52.191  1.00 16.20           C  
-ATOM   4113  C   TYR B 248      40.393 -14.964 -51.561  1.00 16.42           C  
-ATOM   4114  O   TYR B 248      39.504 -15.760 -51.912  1.00 14.84           O  
-ATOM   4115  CB  TYR B 248      41.267 -13.583 -53.489  1.00 17.62           C  
-ATOM   4116  CG  TYR B 248      40.831 -12.512 -54.461  1.00 18.59           C  
-ATOM   4117  CD1 TYR B 248      39.530 -12.495 -54.977  1.00 20.61           C  
-ATOM   4118  CD2 TYR B 248      41.708 -11.522 -54.876  1.00 18.04           C  
-ATOM   4119  CE1 TYR B 248      39.132 -11.506 -55.872  1.00 20.74           C  
-ATOM   4120  CE2 TYR B 248      41.322 -10.540 -55.775  1.00 19.57           C  
-ATOM   4121  CZ  TYR B 248      40.032 -10.536 -56.267  1.00 18.89           C  
-ATOM   4122  OH  TYR B 248      39.667  -9.549 -57.153  1.00 22.23           O  
-ATOM   4123  N   ALA B 249      41.306 -15.266 -50.630  1.00 16.60           N  
-ATOM   4124  CA  ALA B 249      41.241 -16.551 -49.923  1.00 15.79           C  
-ATOM   4125  C   ALA B 249      39.966 -16.662 -49.083  1.00 15.71           C  
-ATOM   4126  O   ALA B 249      39.288 -17.704 -49.087  1.00 17.59           O  
-ATOM   4127  CB  ALA B 249      42.482 -16.781 -49.064  1.00 15.12           C  
-ATOM   4128  N   PHE B 250      39.634 -15.591 -48.366  1.00 14.78           N  
-ATOM   4129  CA  PHE B 250      38.383 -15.522 -47.609  1.00 14.61           C  
-ATOM   4130  C   PHE B 250      37.185 -15.728 -48.536  1.00 13.95           C  
-ATOM   4131  O   PHE B 250      36.294 -16.550 -48.265  1.00 15.63           O  
-ATOM   4132  CB  PHE B 250      38.254 -14.164 -46.909  1.00 14.32           C  
-ATOM   4133  CG  PHE B 250      36.928 -13.945 -46.254  1.00 15.14           C  
-ATOM   4134  CD1 PHE B 250      36.680 -14.439 -44.988  1.00 15.47           C  
-ATOM   4135  CD2 PHE B 250      35.922 -13.235 -46.908  1.00 15.09           C  
-ATOM   4136  CE1 PHE B 250      35.454 -14.241 -44.384  1.00 16.71           C  
-ATOM   4137  CE2 PHE B 250      34.696 -13.034 -46.314  1.00 16.49           C  
-ATOM   4138  CZ  PHE B 250      34.457 -13.538 -45.049  1.00 18.40           C  
-ATOM   4139  N   ILE B 251      37.174 -14.979 -49.632  1.00 15.40           N  
-ATOM   4140  CA  ILE B 251      36.075 -15.037 -50.608  1.00 15.04           C  
-ATOM   4141  C   ILE B 251      35.946 -16.436 -51.198  1.00 15.42           C  
-ATOM   4142  O   ILE B 251      34.840 -16.974 -51.305  1.00 17.80           O  
-ATOM   4143  CB  ILE B 251      36.264 -13.981 -51.718  1.00 15.03           C  
-ATOM   4144  CG1 ILE B 251      36.082 -12.580 -51.139  1.00 13.22           C  
-ATOM   4145  CG2 ILE B 251      35.288 -14.205 -52.862  1.00 13.41           C  
-ATOM   4146  CD1 ILE B 251      36.601 -11.456 -52.035  1.00 13.82           C  
-ATOM   4147  N   GLU B 252      37.074 -17.030 -51.564  1.00 17.32           N  
-ATOM   4148  CA  GLU B 252      37.061 -18.372 -52.131  1.00 17.77           C  
-ATOM   4149  C   GLU B 252      36.512 -19.378 -51.137  1.00 18.49           C  
-ATOM   4150  O   GLU B 252      35.758 -20.272 -51.535  1.00 17.50           O  
-ATOM   4151  CB  GLU B 252      38.450 -18.763 -52.646  1.00 19.13           C  
-ATOM   4152  CG  GLU B 252      38.815 -18.038 -53.936  1.00 21.04           C  
-ATOM   4153  CD  GLU B 252      40.223 -18.327 -54.429  1.00 25.08           C  
-ATOM   4154  OE1 GLU B 252      40.729 -19.451 -54.199  1.00 30.64           O  
-ATOM   4155  OE2 GLU B 252      40.803 -17.429 -55.080  1.00 30.94           O  
-ATOM   4156  N   ARG B 253      36.869 -19.232 -49.861  1.00 19.22           N  
-ATOM   4157  CA  ARG B 253      36.346 -20.101 -48.799  1.00 20.87           C  
-ATOM   4158  C   ARG B 253      34.808 -19.991 -48.726  1.00 21.17           C  
-ATOM   4159  O   ARG B 253      34.121 -21.007 -48.685  1.00 20.19           O  
-ATOM   4160  CB  ARG B 253      37.005 -19.807 -47.434  1.00 22.55           C  
-ATOM   4161  CG  ARG B 253      38.495 -20.219 -47.296  1.00 26.26           C  
-ATOM   4162  CD  ARG B 253      39.099 -20.053 -45.881  1.00 29.18           C  
-ATOM   4163  NE  ARG B 253      39.110 -18.676 -45.357  1.00 30.00           N  
-ATOM   4164  CZ  ARG B 253      40.155 -17.838 -45.322  1.00 32.11           C  
-ATOM   4165  NH1 ARG B 253      41.359 -18.179 -45.797  1.00 31.61           N  
-ATOM   4166  NH2 ARG B 253      39.986 -16.618 -44.790  1.00 30.91           N  
-ATOM   4167  N   VAL B 254      34.288 -18.757 -48.732  1.00 19.20           N  
-ATOM   4168  CA  VAL B 254      32.853 -18.501 -48.677  1.00 18.56           C  
-ATOM   4169  C   VAL B 254      32.121 -19.069 -49.890  1.00 17.80           C  
-ATOM   4170  O   VAL B 254      31.082 -19.705 -49.728  1.00 19.72           O  
-ATOM   4171  CB  VAL B 254      32.566 -16.999 -48.560  1.00 17.66           C  
-ATOM   4172  CG1 VAL B 254      31.059 -16.712 -48.750  1.00 17.85           C  
-ATOM   4173  CG2 VAL B 254      33.098 -16.468 -47.214  1.00 16.69           C  
-ATOM   4174  N   CYS B 255      32.672 -18.864 -51.086  1.00 18.01           N  
-ATOM   4175  CA  CYS B 255      32.049 -19.312 -52.333  1.00 19.16           C  
-ATOM   4176  C   CYS B 255      32.024 -20.828 -52.470  1.00 19.95           C  
-ATOM   4177  O   CYS B 255      31.064 -21.368 -53.038  1.00 19.02           O  
-ATOM   4178  CB  CYS B 255      32.738 -18.696 -53.553  1.00 20.73           C  
-ATOM   4179  SG  CYS B 255      32.425 -16.906 -53.691  1.00 23.67           S  
-ATOM   4180  N   GLN B 256      33.061 -21.498 -51.966  1.00 20.70           N  
-ATOM   4181  CA  GLN B 256      33.113 -22.964 -51.980  1.00 22.14           C  
-ATOM   4182  C   GLN B 256      31.989 -23.548 -51.121  1.00 22.50           C  
-ATOM   4183  O   GLN B 256      31.398 -24.576 -51.473  1.00 19.24           O  
-ATOM   4184  CB  GLN B 256      34.475 -23.461 -51.491  1.00 24.40           C  
-ATOM   4185  CG  GLN B 256      34.723 -24.974 -51.643  1.00 28.40           C  
-ATOM   4186  CD  GLN B 256      34.161 -25.863 -50.520  1.00 33.29           C  
-ATOM   4187  OE1 GLN B 256      33.874 -25.404 -49.413  1.00 37.76           O  
-ATOM   4188  NE2 GLN B 256      34.015 -27.159 -50.813  1.00 37.37           N  
-ATOM   4189  N   MET B 257      31.705 -22.885 -50.003  1.00 22.79           N  
-ATOM   4190  CA  MET B 257      30.597 -23.266 -49.128  1.00 25.40           C  
-ATOM   4191  C   MET B 257      29.235 -22.958 -49.739  1.00 25.45           C  
-ATOM   4192  O   MET B 257      28.301 -23.752 -49.604  1.00 25.84           O  
-ATOM   4193  CB  MET B 257      30.659 -22.502 -47.801  1.00 27.16           C  
-ATOM   4194  CG  MET B 257      31.960 -22.584 -47.037  1.00 32.50           C  
-ATOM   4195  SD  MET B 257      31.922 -23.843 -45.787  1.00 39.46           S  
-ATOM   4196  CE  MET B 257      31.885 -25.305 -46.806  1.00 37.62           C  
-ATOM   4197  N   ALA B 258      29.121 -21.802 -50.397  1.00 24.75           N  
-ATOM   4198  CA  ALA B 258      27.811 -21.290 -50.841  1.00 24.14           C  
-ATOM   4199  C   ALA B 258      27.390 -21.689 -52.264  1.00 25.10           C  
-ATOM   4200  O   ALA B 258      26.199 -21.919 -52.506  1.00 23.39           O  
-ATOM   4201  CB  ALA B 258      27.770 -19.791 -50.678  1.00 23.29           C  
-ATOM   4202  N   GLU B 259      28.350 -21.777 -53.185  1.00 25.59           N  
-ATOM   4203  CA  GLU B 259      28.061 -22.068 -54.594  1.00 27.65           C  
-ATOM   4204  C   GLU B 259      28.054 -23.552 -54.930  1.00 29.99           C  
-ATOM   4205  O   GLU B 259      28.705 -24.354 -54.263  1.00 29.73           O  
-ATOM   4206  CB  GLU B 259      29.065 -21.381 -55.516  1.00 27.95           C  
-ATOM   4207  CG  GLU B 259      29.051 -19.876 -55.415  1.00 28.32           C  
-ATOM   4208  CD  GLU B 259      29.742 -19.229 -56.595  1.00 29.99           C  
-ATOM   4209  OE1 GLU B 259      30.986 -19.139 -56.585  1.00 29.37           O  
-ATOM   4210  OE2 GLU B 259      29.033 -18.821 -57.534  1.00 30.77           O  
-ATOM   4211  N   SER B 260      27.303 -23.895 -55.972  1.00 31.28           N  
-ATOM   4212  CA  SER B 260      27.302 -25.248 -56.520  1.00 33.81           C  
-ATOM   4213  C   SER B 260      26.767 -25.250 -57.958  1.00 37.68           C  
-ATOM   4214  O   SER B 260      26.120 -24.290 -58.400  1.00 36.12           O  
-ATOM   4215  CB  SER B 260      26.509 -26.216 -55.624  1.00 33.20           C  
-ATOM   4216  OG  SER B 260      25.179 -25.780 -55.391  1.00 32.47           O  
-ATOM   4217  N   HIS B 261      27.063 -26.332 -58.680  1.00 42.27           N  
-ATOM   4218  CA  HIS B 261      26.570 -26.541 -60.047  1.00 45.79           C  
-ATOM   4219  C   HIS B 261      25.301 -27.399 -60.000  1.00 47.73           C  
-ATOM   4220  O   HIS B 261      25.335 -28.531 -59.502  1.00 48.97           O  
-ATOM   4221  CB  HIS B 261      27.632 -27.215 -60.918  1.00 46.96           C  
-ATOM   4222  CG  HIS B 261      28.818 -26.348 -61.206  1.00 49.12           C  
-ATOM   4223  ND1 HIS B 261      28.729 -25.184 -61.941  1.00 50.46           N  
-ATOM   4224  CD2 HIS B 261      30.124 -26.481 -60.869  1.00 50.30           C  
-ATOM   4225  CE1 HIS B 261      29.927 -24.633 -62.037  1.00 50.94           C  
-ATOM   4226  NE2 HIS B 261      30.791 -25.401 -61.396  1.00 50.79           N  
-ATOM   4227  N   THR B 262      24.193 -26.853 -60.506  1.00 49.25           N  
-ATOM   4228  CA  THR B 262      22.900 -27.542 -60.497  1.00 49.94           C  
-ATOM   4229  C   THR B 262      21.881 -26.871 -61.410  1.00 50.07           C  
-ATOM   4230  O   THR B 262      21.330 -27.512 -62.304  1.00 49.94           O  
-ATOM   4231  CB  THR B 262      22.304 -27.599 -59.076  1.00 50.76           C  
-TER    4232      THR B 262                                                      
-HETATM 4233  C'  BGO A 300       6.585   8.618   4.329  1.00 19.71           C  
-HETATM 4234  N1  BGO A 300      12.503  10.811  -1.764  1.00 20.31           N  
-HETATM 4235  C2  BGO A 300      12.413  10.490  -0.391  1.00 21.64           C  
-HETATM 4236  N2  BGO A 300      13.459  10.678   0.403  1.00 22.35           N  
-HETATM 4237  N3  BGO A 300      11.269   9.988   0.101  1.00 18.99           N  
-HETATM 4238  C4  BGO A 300      10.212   9.808  -0.720  1.00 19.18           C  
-HETATM 4239  C5  BGO A 300      10.242  10.108  -2.088  1.00 19.27           C  
-HETATM 4240  C6  BGO A 300      11.418  10.629  -2.628  1.00 20.30           C  
-HETATM 4241  O6  BGO A 300      11.523  10.926  -3.825  1.00 17.09           O  
-HETATM 4242  N7  BGO A 300       9.039   9.807  -2.577  1.00 17.68           N  
-HETATM 4243  C8  BGO A 300       8.269   9.333  -1.595  1.00 19.04           C  
-HETATM 4244  N9  BGO A 300       8.999   9.347  -0.472  1.00 19.42           N  
-HETATM 4245  PA  BGO A 300       4.397   7.061  -1.229  1.00 22.32           P  
-HETATM 4246  PB  BGO A 300       3.262   5.016  -2.969  0.60 23.96           P  
-HETATM 4247  C1' BGO A 300       7.213   8.630   5.740  1.00 20.14           C  
-HETATM 4248  O1' BGO A 300       5.512   9.166   4.112  1.00 16.66           O  
-HETATM 4249  O1A BGO A 300       4.159   8.193  -2.129  1.00 20.70           O  
-HETATM 4250  C1B BGO A 300       8.673   8.927   0.857  1.00 19.04           C  
-HETATM 4251  O1B BGO A 300       3.931   4.470  -4.150  0.60 23.20           O  
-HETATM 4252  C2' BGO A 300       6.702   9.452   6.755  1.00 21.94           C  
-HETATM 4253  N2' BGO A 300       5.650  10.254   6.565  1.00 22.91           N  
-HETATM 4254  O2' BGO A 300       7.240  10.405   1.993  1.00 17.13           O  
-HETATM 4255  O2A BGO A 300       3.448   6.795  -0.098  1.00 27.10           O  
-HETATM 4256  C2B BGO A 300       7.340   9.141   1.368  1.00 19.07           C  
-HETATM 4257  O2B BGO A 300       2.258   6.029  -3.241  0.60 22.76           O  
-HETATM 4258  C3' BGO A 300       7.314   9.421   8.004  1.00 22.66           C  
-HETATM 4259  O3' BGO A 300       7.210   8.039   3.340  1.00 18.74           O  
-HETATM 4260  O3A BGO A 300       4.474   5.681  -2.085  1.00 21.96           O  
-HETATM 4261  C3B BGO A 300       6.536   8.140   2.071  1.00 19.09           C  
-HETATM 4262  O3B BGO A 300       2.793   3.957  -2.017  0.60 23.74           O  
-HETATM 4263  C4' BGO A 300       8.408   8.610   8.239  1.00 22.04           C  
-HETATM 4264  O4' BGO A 300       8.539   7.463   0.770  1.00 19.78           O  
-HETATM 4265  C4B BGO A 300       7.242   6.964   1.399  1.00 18.76           C  
-HETATM 4266  C5' BGO A 300       8.924   7.794   7.240  1.00 22.69           C  
-HETATM 4267  O5' BGO A 300       5.885   7.196  -0.628  1.00 20.34           O  
-HETATM 4268  C5B BGO A 300       6.430   6.249   0.304  1.00 19.96           C  
-HETATM 4269  C6' BGO A 300       8.318   7.807   5.978  1.00 21.17           C  
-HETATM 4270  CM' BGO A 300       4.791  10.730   7.665  1.00 25.83           C  
-HETATM 4271  C1  GOL A 400      -2.941  14.047 -28.309  1.00 49.49           C  
-HETATM 4272  O1  GOL A 400      -4.274  13.612 -28.132  1.00 51.06           O  
-HETATM 4273  C2  GOL A 400      -1.959  12.994 -27.794  1.00 48.60           C  
-HETATM 4274  O2  GOL A 400      -2.325  12.590 -26.494  1.00 48.25           O  
-HETATM 4275  C3  GOL A 400      -0.540  13.562 -27.743  1.00 47.50           C  
-HETATM 4276  O3  GOL A 400       0.396  12.680 -28.312  1.00 44.35           O  
-HETATM 4277 MG    MG A 401      25.039   9.612 -18.058  1.00 27.85          MG  
-HETATM 4278  C'  BGO B 300      21.458  -4.568 -70.692  1.00 17.25           C  
-HETATM 4279  N1  BGO B 300      18.769  -9.956 -64.442  1.00 18.07           N  
-HETATM 4280  C2  BGO B 300      19.105  -9.894 -65.808  1.00 19.19           C  
-HETATM 4281  N2  BGO B 300      18.823 -10.952 -66.580  1.00 17.32           N  
-HETATM 4282  N3  BGO B 300      19.685  -8.780 -66.295  1.00 17.31           N  
-HETATM 4283  C4  BGO B 300      19.930  -7.740 -65.464  1.00 19.47           C  
-HETATM 4284  C5  BGO B 300      19.620  -7.755 -64.102  1.00 16.99           C  
-HETATM 4285  C6  BGO B 300      19.024  -8.893 -63.585  1.00 18.59           C  
-HETATM 4286  O6  BGO B 300      18.731  -8.986 -62.393  1.00 18.42           O  
-HETATM 4287  N7  BGO B 300      20.000  -6.592 -63.567  1.00 18.35           N  
-HETATM 4288  C8  BGO B 300      20.533  -5.850 -64.546  1.00 20.61           C  
-HETATM 4289  N9  BGO B 300      20.471  -6.559 -65.684  1.00 19.66           N  
-HETATM 4290  PA  BGO B 300      22.930  -1.939 -65.105  1.00 21.30           P  
-HETATM 4291  PB  BGO B 300      24.966  -1.003 -63.367  0.60 21.13           P  
-HETATM 4292  C1' BGO B 300      21.623  -5.388 -71.983  1.00 18.56           C  
-HETATM 4293  O1' BGO B 300      20.840  -3.507 -70.654  1.00 16.64           O  
-HETATM 4294  O1A BGO B 300      21.738  -1.724 -64.275  1.00 18.59           O  
-HETATM 4295  C1B BGO B 300      20.932  -6.267 -67.019  1.00 19.52           C  
-HETATM 4296  O1B BGO B 300      25.490  -1.770 -62.227  0.60 20.95           O  
-HETATM 4297  C2' BGO B 300      20.859  -5.141 -73.142  1.00 22.00           C  
-HETATM 4298  N2' BGO B 300      19.951  -4.171 -73.203  1.00 23.48           N  
-HETATM 4299  O2' BGO B 300      19.569  -4.856 -68.334  1.00 18.13           O  
-HETATM 4300  O2A BGO B 300      23.255  -0.951 -66.163  1.00 24.62           O  
-HETATM 4301  C2B BGO B 300      20.834  -4.992 -67.660  1.00 18.65           C  
-HETATM 4302  O2B BGO B 300      24.083   0.090 -63.022  0.60 20.01           O  
-HETATM 4303  C3' BGO B 300      21.070  -5.946 -74.265  1.00 21.61           C  
-HETATM 4304  O3' BGO B 300      21.997  -5.069 -69.551  1.00 18.03           O  
-HETATM 4305  O3A BGO B 300      24.206  -2.172 -64.233  1.00 20.09           O  
-HETATM 4306  C3B BGO B 300      21.876  -4.262 -68.359  1.00 17.99           C  
-HETATM 4307  O3B BGO B 300      25.970  -0.653 -64.407  0.60 22.45           O  
-HETATM 4308  C4' BGO B 300      22.007  -6.963 -74.257  1.00 21.05           C  
-HETATM 4309  O4' BGO B 300      22.405  -6.156 -66.837  1.00 19.50           O  
-HETATM 4310  C4B BGO B 300      22.971  -4.954 -67.543  1.00 16.82           C  
-HETATM 4311  C5' BGO B 300      22.765  -7.218 -73.117  1.00 22.03           C  
-HETATM 4312  O5' BGO B 300      22.636  -3.371 -65.728  1.00 19.33           O  
-HETATM 4313  C5B BGO B 300      23.619  -4.117 -66.408  1.00 19.46           C  
-HETATM 4314  C6' BGO B 300      22.563  -6.424 -71.983  1.00 20.17           C  
-HETATM 4315  CM' BGO B 300      19.343  -3.740 -74.478  1.00 27.67           C  
-HETATM 4316  C1  GOL B 400      34.297 -18.803 -42.887  1.00 47.48           C  
-HETATM 4317  O1  GOL B 400      33.325 -17.812 -43.160  1.00 47.93           O  
-HETATM 4318  C2  GOL B 400      35.226 -18.921 -44.085  1.00 46.80           C  
-HETATM 4319  O2  GOL B 400      36.120 -19.998 -43.913  1.00 46.29           O  
-HETATM 4320  C3  GOL B 400      35.983 -17.611 -44.262  1.00 46.21           C  
-HETATM 4321  O3  GOL B 400      37.334 -17.759 -43.897  1.00 46.09           O  
-HETATM 4322  C1  GOL B 401      31.661  -7.008 -63.993  1.00 22.70           C  
-HETATM 4323  O1  GOL B 401      33.033  -6.727 -64.173  1.00 23.31           O  
-HETATM 4324  C2  GOL B 401      31.303  -6.821 -62.528  1.00 21.56           C  
-HETATM 4325  O2  GOL B 401      32.204  -7.533 -61.694  1.00 21.07           O  
-HETATM 4326  C3  GOL B 401      29.875  -7.278 -62.266  1.00 18.82           C  
-HETATM 4327  O3  GOL B 401      29.812  -8.682 -62.404  1.00 14.99           O  
-HETATM 4328  O   HOH A 271      -8.975 -14.142 -36.052  1.00 31.03           O  
-HETATM 4329  O   HOH A 272      16.455 -12.286 -20.714  1.00 13.87           O  
-HETATM 4330  O   HOH A 273       5.403   7.794 -21.936  1.00 16.48           O  
-HETATM 4331  O   HOH A 274       9.364  -7.821 -24.175  1.00 13.93           O  
-HETATM 4332  O   HOH A 275      -8.657 -19.495 -24.854  1.00 30.62           O  
-HETATM 4333  O   HOH A 276     -10.390  -5.775 -10.046  1.00 32.48           O  
-HETATM 4334  O   HOH A 277     -12.970 -26.951 -33.244  1.00 38.34           O  
-HETATM 4335  O   HOH A 278      -3.981  -4.639 -34.979  1.00 15.85           O  
-HETATM 4336  O   HOH A 279      -2.854  -8.038 -14.128  1.00 15.16           O  
-HETATM 4337  O   HOH A 280      16.909  15.954  -5.500  1.00 29.79           O  
-HETATM 4338  O   HOH A 281      -6.347 -14.808 -36.146  1.00 23.98           O  
-HETATM 4339  O   HOH A 282       8.788   4.761 -24.468  1.00 15.16           O  
-HETATM 4340  O   HOH A 283       5.471   0.428 -24.473  1.00 13.00           O  
-HETATM 4341  O   HOH A 284     -10.981  15.328 -16.689  1.00 32.33           O  
-HETATM 4342  O   HOH A 285      -8.976  -3.869 -21.473  1.00 30.14           O  
-HETATM 4343  O   HOH A 286      11.443  16.798 -20.107  1.00 23.53           O  
-HETATM 4344  O   HOH A 287      -9.982 -16.300 -14.681  1.00 28.30           O  
-HETATM 4345  O   HOH A 288      17.202  13.017 -15.361  1.00 16.72           O  
-HETATM 4346  O   HOH A 289       7.825  -0.353 -11.783  1.00 13.22           O  
-HETATM 4347  O   HOH A 290       7.891   0.901  -9.150  1.00 13.32           O  
-HETATM 4348  O   HOH A 291      18.531 -14.379 -21.021  1.00 26.12           O  
-HETATM 4349  O   HOH A 292       7.627 -24.793 -31.437  1.00 15.45           O  
-HETATM 4350  O   HOH A 293      -6.524 -20.894 -24.034  1.00 22.08           O  
-HETATM 4351  O   HOH A 294      -2.029 -20.597 -22.891  1.00 16.95           O  
-HETATM 4352  O   HOH A 295      10.580   8.148 -27.479  1.00 30.03           O  
-HETATM 4353  O   HOH A 296       3.293  -6.313 -29.963  1.00 25.91           O  
-HETATM 4354  O   HOH A 297      10.326   0.931 -25.089  1.00 18.64           O  
-HETATM 4355  O   HOH A 298     -12.535 -30.760 -33.658  1.00 35.13           O  
-HETATM 4356  O   HOH A 299      19.903   8.060   2.009  1.00 39.33           O  
-HETATM 4357  O   HOH A 301       7.868   1.999 -24.009  1.00 16.36           O  
-HETATM 4358  O   HOH A 302      11.897   7.975   2.169  1.00 28.87           O  
-HETATM 4359  O   HOH A 303      10.204 -13.048 -30.777  1.00 23.20           O  
-HETATM 4360  O   HOH A 304      18.010  -8.078 -24.354  1.00 28.38           O  
-HETATM 4361  O   HOH A 305       5.927  -9.292 -34.683  1.00 30.45           O  
-HETATM 4362  O   HOH A 306      15.773   9.938 -21.088  1.00 23.58           O  
-HETATM 4363  O   HOH A 307       9.433   6.232 -32.420  1.00 38.57           O  
-HETATM 4364  O   HOH A 308      -4.056  -3.189 -26.773  1.00 31.83           O  
-HETATM 4365  O   HOH A 309      -8.773 -19.495 -17.503  1.00 16.92           O  
-HETATM 4366  O   HOH A 310      -2.264   1.949  -4.509  1.00 43.10           O  
-HETATM 4367  O   HOH A 311      26.463   7.301 -12.794  1.00 38.16           O  
-HETATM 4368  O   HOH A 312     -12.501   5.430  -3.297  1.00 36.10           O  
-HETATM 4369  O   HOH A 313      15.970  -4.553  -6.157  1.00 17.59           O  
-HETATM 4370  O   HOH A 314      -4.400  20.071 -10.960  1.00 25.84           O  
-HETATM 4371  O   HOH A 315      10.833  -0.191  -3.797  1.00 17.06           O  
-HETATM 4372  O   HOH A 316      -1.696  -1.265  -3.942  1.00 28.71           O  
-HETATM 4373  O   HOH A 317      -2.660 -17.982 -14.361  1.00 19.55           O  
-HETATM 4374  O   HOH A 318      15.591 -12.049 -30.643  1.00 32.73           O  
-HETATM 4375  O   HOH A 319       2.064  14.013  -0.677  1.00 30.92           O  
-HETATM 4376  O   HOH A 320      -7.832  17.948 -11.400  1.00 29.43           O  
-HETATM 4377  O   HOH A 321      -1.776 -23.389 -23.227  1.00 18.05           O  
-HETATM 4378  O   HOH A 322     -13.068 -13.426 -19.545  1.00 36.89           O  
-HETATM 4379  O   HOH A 323      -6.937   4.708  -9.664  1.00 21.88           O  
-HETATM 4380  O   HOH A 324       8.024  -4.737  -9.841  1.00 15.96           O  
-HETATM 4381  O   HOH A 325       2.981 -27.599 -20.654  1.00 35.77           O  
-HETATM 4382  O   HOH A 326       9.717   3.691 -35.545  1.00 38.65           O  
-HETATM 4383  O   HOH A 327     -10.610 -20.279 -19.130  1.00 18.25           O  
-HETATM 4384  O   HOH A 328       1.977  20.212 -12.164  1.00 17.59           O  
-HETATM 4385  O   HOH A 329     -11.188  12.280 -18.737  1.00 31.95           O  
-HETATM 4386  O   HOH A 330       2.784 -25.067 -32.386  1.00 18.04           O  
-HETATM 4387  O   HOH A 331       1.119  -6.315  -6.686  1.00 23.01           O  
-HETATM 4388  O   HOH A 332      12.191 -16.426 -33.504  1.00 40.94           O  
-HETATM 4389  O   HOH A 333      13.751  20.042 -10.962  1.00 27.94           O  
-HETATM 4390  O   HOH A 334       4.999  -8.242 -31.335  1.00 28.58           O  
-HETATM 4391  O   HOH A 335     -11.722 -14.326 -16.187  1.00 28.12           O  
-HETATM 4392  O   HOH A 336      10.705   3.791 -28.470  1.00 28.06           O  
-HETATM 4393  O   HOH A 337       7.317 -11.817 -34.651  1.00 31.25           O  
-HETATM 4394  O   HOH A 338       1.746 -10.411 -34.757  1.00 18.99           O  
-HETATM 4395  O   HOH A 339       3.529  -8.888 -33.598  1.00 25.18           O  
-HETATM 4396  O   HOH A 340     -10.073 -18.955 -15.150  1.00 22.51           O  
-HETATM 4397  O   HOH A 341     -10.476  -9.477 -24.259  1.00 43.18           O  
-HETATM 4398  O   HOH A 342      -3.896 -21.029 -24.951  1.00 17.53           O  
-HETATM 4399  O   HOH A 343      10.396   8.513 -30.329  1.00 38.95           O  
-HETATM 4400  O   HOH A 344      -9.835  16.275 -11.658  1.00 30.78           O  
-HETATM 4401  O   HOH A 345      -3.931  11.654  -3.498  1.00 23.23           O  
-HETATM 4402  O   HOH A 346      -9.231  13.939 -13.158  1.00 31.36           O  
-HETATM 4403  O   HOH A 347      10.280   5.706 -26.513  1.00 29.43           O  
-HETATM 4404  O   HOH A 348       6.048  14.764  -1.419  1.00 37.55           O  
-HETATM 4405  O   HOH A 349      26.367   7.753 -21.403  1.00 23.36           O  
-HETATM 4406  O   HOH A 350      -1.856   7.932  -5.352  1.00 34.77           O  
-HETATM 4407  O   HOH A 351       2.309  17.486  -2.348  1.00 34.59           O  
-HETATM 4408  O   HOH A 352     -12.428   8.821  -9.947  1.00 36.32           O  
-HETATM 4409  O   HOH A 353      -9.825 -10.082  -9.004  1.00 34.30           O  
-HETATM 4410  O   HOH A 354     -11.086  -5.489 -12.550  1.00 42.51           O  
-HETATM 4411  O   HOH A 355     -11.286  -8.095  -9.186  1.00 26.07           O  
-HETATM 4412  O   HOH A 356      -1.962  -6.036  -5.429  1.00 48.28           O  
-HETATM 4413  O   HOH A 357      23.210  10.266 -17.028  1.00 20.40           O  
-HETATM 4414  O   HOH A 358      21.376  11.972 -12.873  1.00 25.53           O  
-HETATM 4415  O   HOH A 359      26.119  10.640 -16.662  1.00 21.08           O  
-HETATM 4416  O   HOH A 360      26.657   8.826 -19.131  1.00 27.45           O  
-HETATM 4417  O   HOH A 361       9.488  -2.388  -4.645  1.00 25.26           O  
-HETATM 4418  O   HOH A 362      -2.451  -9.015 -34.169  1.00 19.02           O  
-HETATM 4419  O   HOH A 363       4.180 -22.553 -15.260  1.00 23.97           O  
-HETATM 4420  O   HOH A 364      -3.506 -23.687 -25.345  1.00 17.43           O  
-HETATM 4421  O   HOH A 365      -4.033  14.915  -5.503  1.00 34.40           O  
-HETATM 4422  O   HOH A 366     -13.302  -8.821 -11.554  1.00 46.83           O  
-HETATM 4423  O   HOH A 367     -10.997   9.365 -11.877  1.00 39.38           O  
-HETATM 4424  O   HOH A 368       0.217   2.182  -3.788  1.00 46.03           O  
-HETATM 4425  O   HOH A 369       8.991 -11.861  -5.230  1.00 44.76           O  
-HETATM 4426  O   HOH A 370      11.388  -9.357  -4.608  1.00 32.05           O  
-HETATM 4427  O   HOH A 371      18.527  10.151 -21.657  1.00 43.13           O  
-HETATM 4428  O   HOH A 372      15.012  -3.048 -29.080  1.00 35.57           O  
-HETATM 4429  O   HOH A 373       6.475   1.994 -27.316  1.00 25.23           O  
-HETATM 4430  O   HOH A 374       6.299 -21.523 -11.552  1.00 38.57           O  
-HETATM 4431  O   HOH A 375       4.652 -15.007 -13.108  1.00 24.15           O  
-HETATM 4432  O   HOH A 376      23.109  -5.988 -12.751  1.00 34.06           O  
-HETATM 4433  O   HOH A 377      -5.702   5.180  -7.200  1.00 22.81           O  
-HETATM 4434  O   HOH A 378       9.778 -12.092  -8.400  1.00 27.72           O  
-HETATM 4435  O   HOH A 379       4.978  11.818   2.029  1.00 36.08           O  
-HETATM 4436  O   HOH A 380       2.116   8.991   0.929  1.00 45.16           O  
-HETATM 4437  O   HOH A 381       3.235   3.855   0.505  1.00 30.64           O  
-HETATM 4438  O   HOH A 382       5.503 -13.904 -35.525  1.00 22.85           O  
-HETATM 4439  O   HOH A 383      -8.165   0.815  -3.392  1.00 30.85           O  
-HETATM 4440  O   HOH A 384      -3.669   5.671 -26.940  1.00 26.70           O  
-HETATM 4441  O   HOH A 385       1.490 -31.375 -33.012  1.00 26.36           O  
-HETATM 4442  O   HOH A 386      10.368 -19.450 -34.019  1.00 35.82           O  
-HETATM 4443  O   HOH A 387       4.741 -12.062 -17.287  1.00 32.63           O  
-HETATM 4444  O   HOH A 388       4.000 -12.002 -11.352  1.00 40.00           O  
-HETATM 4445  O   HOH A 389      -7.813 -32.992 -31.599  1.00 37.81           O  
-HETATM 4446  O   HOH A 390      12.386  -8.731  -6.984  1.00 29.27           O  
-HETATM 4447  O   HOH A 391      -6.775  -5.618 -25.928  1.00 29.28           O  
-HETATM 4448  O   HOH A 392      -6.156   2.549  -6.993  1.00 24.63           O  
-HETATM 4449  O   HOH A 393      -0.531 -20.520 -37.197  1.00 39.65           O  
-HETATM 4450  O   HOH A 394     -10.728   7.907 -13.923  1.00 33.45           O  
-HETATM 4451  O   HOH A 395      12.887  -4.593 -29.053  1.00 28.63           O  
-HETATM 4452  O   HOH A 396     -12.533 -24.151 -32.585  1.00 36.50           O  
-HETATM 4453  O   HOH A 397       0.813 -31.324 -24.813  1.00 34.06           O  
-HETATM 4454  O   HOH A 398      -0.990 -28.343 -32.833  1.00 31.73           O  
-HETATM 4455  O   HOH A 399     -16.789   5.939  -8.861  1.00 40.98           O  
-HETATM 4456  O   HOH A 402       2.902  -5.737 -27.380  1.00 19.18           O  
-HETATM 4457  O   HOH A 403       7.523  19.675  -7.944  1.00 36.37           O  
-HETATM 4458  O   HOH A 404      13.398  -5.783 -31.415  1.00 39.13           O  
-HETATM 4459  O   HOH A 405       2.841 -20.804 -34.932  1.00 22.46           O  
-HETATM 4460  O   HOH A 406     -10.213 -12.070 -30.928  1.00 30.25           O  
-HETATM 4461  O   HOH A 407      -6.479 -10.014 -19.106  1.00 21.43           O  
-HETATM 4462  O   HOH A 408       3.701  15.135  -2.417  1.00 25.99           O  
-HETATM 4463  O   HOH A 409       3.910   7.675 -34.569  1.00 38.79           O  
-HETATM 4464  O   HOH A 410       5.768  20.969  -9.954  1.00 31.99           O  
-HETATM 4465  O   HOH A 411     -13.769  13.143  -5.890  1.00 37.24           O  
-HETATM 4466  O   HOH A 412     -10.640  -0.042 -17.503  1.00 24.51           O  
-HETATM 4467  O   HOH A 413      15.807   8.325   3.609  1.00 35.54           O  
-HETATM 4468  O   HOH A 414       8.167 -11.633 -32.094  1.00 29.25           O  
-HETATM 4469  O   HOH A 415       3.117  11.474   0.477  1.00 40.64           O  
-HETATM 4470  O   HOH A 416      -9.731   2.650 -27.191  1.00 40.92           O  
-HETATM 4471  O   HOH A 417      17.318  12.634   1.274  1.00 30.53           O  
-HETATM 4472  O   HOH A 418      15.787  -1.179 -26.878  1.00 38.50           O  
-HETATM 4473  O   HOH A 419      -0.088 -14.097 -37.865  1.00 34.74           O  
-HETATM 4474  O   HOH A 420       2.577   2.834  -5.512  1.00 32.46           O  
-HETATM 4475  O   HOH A 421      12.053 -18.733 -11.455  1.00 33.64           O  
-HETATM 4476  O   HOH A 422      -2.987 -32.738 -33.090  1.00 34.81           O  
-HETATM 4477  O   HOH A 423      -5.137 -17.482 -40.740  1.00 35.01           O  
-HETATM 4478  O   HOH A 424     -10.101 -14.124 -32.707  1.00 31.31           O  
-HETATM 4479  O   HOH A 425       9.273   1.685 -27.369  1.00 25.77           O  
-HETATM 4480  O   HOH A 426      17.495   2.767 -26.572  1.00 28.25           O  
-HETATM 4481  O   HOH A 427      13.157   3.074 -27.553  1.00 38.95           O  
-HETATM 4482  O   HOH A 428      -2.576  11.782  -0.523  1.00 40.42           O  
-HETATM 4483  O   HOH A 429     -10.420  13.932  -3.308  1.00 36.04           O  
-HETATM 4484  O   HOH A 430      17.004  12.264 -18.167  1.00 17.18           O  
-HETATM 4485  O   HOH A 431      15.566  13.848 -19.868  1.00 27.51           O  
-HETATM 4486  O   HOH A 432       7.166  21.555  -6.096  1.00 37.65           O  
-HETATM 4487  O   HOH A 433       8.678  18.125   0.311  1.00 44.16           O  
-HETATM 4488  O   HOH A 434      18.100  18.066  -4.159  1.00 43.64           O  
-HETATM 4489  O   HOH A 435       6.771  11.709 -33.441  1.00 36.38           O  
-HETATM 4490  O   HOH A 436       0.021  13.718 -30.838  1.00 36.07           O  
-HETATM 4491  O   HOH A 437      -5.802 -20.036 -37.011  1.00 28.03           O  
-HETATM 4492  O   HOH A 438      -5.795 -16.780 -37.842  1.00 35.39           O  
-HETATM 4493  O   HOH A 439      23.080  10.052 -14.281  1.00 19.39           O  
-HETATM 4494  O   HOH A 440      29.820   6.692 -22.022  1.00 31.87           O  
-HETATM 4495  O   HOH A 441       7.096 -32.205 -27.295  1.00 37.46           O  
-HETATM 4496  O   HOH A 442      -0.204 -31.908 -29.570  1.00 39.12           O  
-HETATM 4497  O   HOH A 443      -1.509 -29.518 -28.921  1.00 30.65           O  
-HETATM 4498  O   HOH A 444      -4.158 -29.254 -22.582  1.00 37.95           O  
-HETATM 4499  O   HOH A 445      -2.279  -1.587 -25.076  1.00 27.66           O  
-HETATM 4500  O   HOH A 446      16.122  -5.530 -25.436  1.00 24.39           O  
-HETATM 4501  O   HOH A 447      15.338  -2.900 -24.469  1.00 30.12           O  
-HETATM 4502  O   HOH A 448      10.358 -24.739 -13.292  1.00 36.06           O  
-HETATM 4503  O   HOH A 449      18.603  -3.210  -7.815  1.00 21.61           O  
-HETATM 4504  O   HOH A 450      18.741  -0.079  -6.380  1.00 32.74           O  
-HETATM 4505  O   HOH A 451      -4.692   2.159 -22.044  1.00 26.30           O  
-HETATM 4506  O   HOH A 452       0.433 -14.177 -15.643  1.00 20.64           O  
-HETATM 4507  O   HOH A 453      13.586  10.829   3.339  1.00 30.71           O  
-HETATM 4508  O   HOH A 454      -0.214 -11.929 -33.667  1.00 20.69           O  
-HETATM 4509  O   HOH A 455      12.848  -2.223 -23.954  1.00 21.36           O  
-HETATM 4510  O   HOH A 456      15.506  15.019  -9.600  1.00 21.31           O  
-HETATM 4511  O   HOH A 457       7.009 -12.794 -15.291  1.00 23.49           O  
-HETATM 4512  O   HOH A 458      15.008 -15.316 -11.525  1.00 29.95           O  
-HETATM 4513  O   HOH A 459       3.681  -7.667 -19.888  1.00 23.66           O  
-HETATM 4514  O   HOH A 460      16.032  15.021 -13.442  1.00 23.52           O  
-HETATM 4515  O   HOH A 461       5.623 -15.264 -15.630  1.00 27.65           O  
-HETATM 4516  O   HOH A 462      16.906 -13.019 -28.478  1.00 22.06           O  
-HETATM 4517  O   HOH A 463      -7.933 -20.933 -36.152  1.00 26.31           O  
-HETATM 4518  O   HOH A 464      -9.531  -1.214 -15.154  1.00 23.81           O  
-HETATM 4519  O   HOH A 465     -10.714 -13.154 -18.331  1.00 23.86           O  
-HETATM 4520  O   HOH A 466       3.574   3.943 -30.050  1.00 25.36           O  
-HETATM 4521  O   HOH A 467      19.173 -11.843 -27.538  1.00 30.67           O  
-HETATM 4522  O   HOH A 468     -10.870  -3.597 -14.381  1.00 32.21           O  
-HETATM 4523  O   HOH A 469       7.327  -9.563 -30.462  1.00 19.13           O  
-HETATM 4524  O   HOH A 470     -10.088 -25.019 -34.696  1.00 19.72           O  
-HETATM 4525  O   HOH A 471      -1.694   9.210 -28.171  1.00 21.31           O  
-HETATM 4526  O   HOH A 472       9.877  10.656 -26.443  1.00 26.63           O  
-HETATM 4527  O   HOH A 473       4.221  19.316 -13.757  1.00 26.78           O  
-HETATM 4528  O   HOH A 474     -10.004 -17.188 -33.064  1.00 33.31           O  
-HETATM 4529  O   HOH A 475     -10.870   1.832 -19.458  1.00 41.62           O  
-HETATM 4530  O   HOH A 476      -8.515  -9.225 -17.397  1.00 21.34           O  
-HETATM 4531  O   HOH A 477      -6.741  -7.185 -19.435  1.00 29.85           O  
-HETATM 4532  O   HOH A 478      -5.816  -6.689  -2.670  1.00 36.33           O  
-HETATM 4533  O   HOH A 479      17.211  -8.953 -10.271  1.00 34.64           O  
-HETATM 4534  O   HOH A 480      28.921   1.590 -20.842  1.00 33.76           O  
-HETATM 4535  O   HOH A 481       2.218 -13.151 -13.693  1.00 36.35           O  
-HETATM 4536  O   HOH A 482      14.588 -16.613 -31.636  1.00 19.83           O  
-HETATM 4537  O   HOH A 483     -10.823 -10.373 -18.009  1.00 25.64           O  
-HETATM 4538  O   HOH A 484       2.816 -10.089 -20.586  1.00 25.80           O  
-HETATM 4539  O   HOH A 485       2.524  -8.679 -17.545  1.00 26.55           O  
-HETATM 4540  O   HOH A 486      14.913 -20.324 -17.034  1.00 23.06           O  
-HETATM 4541  O   HOH A 487     -12.249 -12.555 -13.532  1.00 39.69           O  
-HETATM 4542  O   HOH B 271      28.998  -5.688 -57.061  1.00 12.25           O  
-HETATM 4543  O   HOH B 272      44.079  -4.191 -30.857  1.00 21.82           O  
-HETATM 4544  O   HOH B 273      39.510  -5.763 -35.772  1.00 23.22           O  
-HETATM 4545  O   HOH B 274      17.774   5.193 -39.419  1.00 31.75           O  
-HETATM 4546  O   HOH B 275      29.602  -3.428 -41.713  1.00 14.08           O  
-HETATM 4547  O   HOH B 276      54.729  -7.091 -35.001  1.00 15.84           O  
-HETATM 4548  O   HOH B 277      57.663  -1.974 -32.787  1.00 15.03           O  
-HETATM 4549  O   HOH B 278      40.317  -1.505 -45.556  1.00 27.69           O  
-HETATM 4550  O   HOH B 279      19.155  -7.238 -39.698  1.00 24.94           O  
-HETATM 4551  O   HOH B 280      22.258  -2.732 -44.312  1.00 14.26           O  
-HETATM 4552  O   HOH B 281      30.217  -5.690 -54.542  1.00 11.83           O  
-HETATM 4553  O   HOH B 282      31.798  11.627 -51.067  1.00 24.98           O  
-HETATM 4554  O   HOH B 283      45.047  10.198 -30.383  1.00 27.49           O  
-HETATM 4555  O   HOH B 284      30.110   5.026 -34.846  1.00 17.77           O  
-HETATM 4556  O   HOH B 285      54.202   4.131 -41.072  1.00 17.61           O  
-HETATM 4557  O   HOH B 286      34.732  -6.116 -56.477  1.00 11.38           O  
-HETATM 4558  O   HOH B 287      27.830   4.202 -61.474  1.00 34.12           O  
-HETATM 4559  O   HOH B 288      34.751  10.869 -44.847  1.00 27.21           O  
-HETATM 4560  O   HOH B 289      23.442  -6.941 -33.849  1.00 38.35           O  
-HETATM 4561  O   HOH B 290      36.652  12.136 -56.096  1.00 31.42           O  
-HETATM 4562  O   HOH B 291      25.183  -6.316 -41.684  1.00 15.24           O  
-HETATM 4563  O   HOH B 292      11.000 -14.901 -61.659  1.00 30.66           O  
-HETATM 4564  O   HOH B 293      38.510   4.602 -52.146  1.00 17.11           O  
-HETATM 4565  O   HOH B 294      24.567 -13.586 -41.167  1.00 30.63           O  
-HETATM 4566  O   HOH B 295      55.240  -2.265 -33.862  1.00 14.53           O  
-HETATM 4567  O   HOH B 296      36.646  -1.644 -36.135  1.00 31.58           O  
-HETATM 4568  O   HOH B 297      51.030   6.767 -29.378  1.00 26.95           O  
-HETATM 4569  O   HOH B 298      35.930  -1.387 -38.870  1.00 17.78           O  
-HETATM 4570  O   HOH B 299      37.777  -7.755 -42.163  1.00 16.41           O  
-HETATM 4571  O   HOH B 301       9.105   0.227 -56.193  1.00 30.75           O  
-HETATM 4572  O   HOH B 302      52.849   7.948 -44.507  1.00 20.08           O  
-HETATM 4573  O   HOH B 303      44.554 -16.091 -51.863  1.00 30.59           O  
-HETATM 4574  O   HOH B 304      35.292   5.629 -31.472  1.00 17.14           O  
-HETATM 4575  O   HOH B 305      41.512 -17.534 -41.943  1.00 40.61           O  
-HETATM 4576  O   HOH B 306      58.700   1.380 -33.347  1.00 27.75           O  
-HETATM 4577  O   HOH B 307      22.426 -16.976 -42.144  1.00 25.34           O  
-HETATM 4578  O   HOH B 308      51.157   2.998 -43.463  1.00 14.53           O  
-HETATM 4579  O   HOH B 309      37.387 -16.208 -41.829  1.00 33.74           O  
-HETATM 4580  O   HOH B 310      39.446   3.898 -32.053  1.00 20.10           O  
-HETATM 4581  O   HOH B 311      17.809  16.380 -60.570  1.00 43.40           O  
-HETATM 4582  O   HOH B 312      36.607   0.634 -59.516  1.00 19.69           O  
-HETATM 4583  O   HOH B 313      46.366 -13.501 -34.708  1.00 25.67           O  
-HETATM 4584  O   HOH B 314      41.834 -14.905 -45.698  1.00 17.18           O  
-HETATM 4585  O   HOH B 315      19.935 -22.241 -53.780  1.00 29.68           O  
-HETATM 4586  O   HOH B 316      32.171   4.345 -41.430  1.00 18.66           O  
-HETATM 4587  O   HOH B 317      38.482  -3.367 -35.115  1.00 32.58           O  
-HETATM 4588  O   HOH B 318      28.867  -7.982 -41.112  1.00 17.28           O  
-HETATM 4589  O   HOH B 319      21.301   4.242 -38.144  1.00 19.29           O  
-HETATM 4590  O   HOH B 320      33.987 -14.019 -59.970  1.00 19.73           O  
-HETATM 4591  O   HOH B 321      44.950 -13.225 -54.956  1.00 36.55           O  
-HETATM 4592  O   HOH B 322      20.082 -13.587 -45.094  1.00 23.97           O  
-HETATM 4593  O   HOH B 323      51.875  -0.650 -51.009  1.00 37.55           O  
-HETATM 4594  O   HOH B 324      59.666  -5.955 -45.972  1.00 41.40           O  
-HETATM 4595  O   HOH B 325      32.009 -10.484 -42.203  1.00 21.78           O  
-HETATM 4596  O   HOH B 326      51.409   7.214 -41.873  1.00 16.34           O  
-HETATM 4597  O   HOH B 327      51.996   5.066 -48.685  1.00 37.35           O  
-HETATM 4598  O   HOH B 328      61.549   1.355 -36.212  1.00 35.72           O  
-HETATM 4599  O   HOH B 329      34.911 -14.221 -40.852  1.00 22.85           O  
-HETATM 4600  O   HOH B 330      53.853   2.494 -43.306  1.00 20.44           O  
-HETATM 4601  O   HOH B 331      28.644 -13.305 -38.385  1.00 30.16           O  
-HETATM 4602  O   HOH B 332      32.532   4.322 -33.559  1.00 15.86           O  
-HETATM 4603  O   HOH B 333      31.218 -13.390 -39.484  1.00 34.00           O  
-HETATM 4604  O   HOH B 334      33.553   9.725 -39.013  1.00 34.27           O  
-HETATM 4605  O   HOH B 335      57.503  -0.888 -43.120  1.00 18.82           O  
-HETATM 4606  O   HOH B 336      32.500 -13.210 -41.711  1.00 23.42           O  
-HETATM 4607  O   HOH B 337       9.603 -10.746 -55.111  1.00 25.68           O  
-HETATM 4608  O   HOH B 338      24.974   6.124 -39.436  1.00 27.16           O  
-HETATM 4609  O   HOH B 339      26.240  -1.175 -36.199  1.00 21.64           O  
-HETATM 4610  O   HOH B 340      35.411  10.785 -42.345  1.00 35.25           O  
-HETATM 4611  O   HOH B 341      57.209   0.356 -31.479  1.00 19.35           O  
-HETATM 4612  O   HOH B 342      20.999 -12.192 -41.835  1.00 33.34           O  
-HETATM 4613  O   HOH B 343      50.049   9.479 -41.349  1.00 19.14           O  
-HETATM 4614  O   HOH B 344      16.395 -14.442 -51.167  1.00 20.36           O  
-HETATM 4615  O   HOH B 345      21.986 -23.962 -52.874  1.00 25.92           O  
-HETATM 4616  O   HOH B 346      51.508   4.517 -41.203  1.00 17.65           O  
-HETATM 4617  O   HOH B 347      25.840   9.359 -56.545  1.00 21.70           O  
-HETATM 4618  O   HOH B 348      55.866   0.846 -44.378  1.00 24.14           O  
-HETATM 4619  O   HOH B 349      24.315 -25.872 -50.235  1.00 31.64           O  
-HETATM 4620  O   HOH B 350      10.733  -1.129 -52.148  1.00 29.09           O  
-HETATM 4621  O   HOH B 351      27.986  -5.520 -42.241  1.00 15.24           O  
-HETATM 4622  O   HOH B 352      45.679   7.534 -30.244  1.00 24.62           O  
-HETATM 4623  O   HOH B 353      43.570  12.166 -47.565  1.00 19.74           O  
-HETATM 4624  O   HOH B 354      20.274 -20.033 -56.537  1.00 23.32           O  
-HETATM 4625  O   HOH B 355      50.658   4.325 -30.164  1.00 27.45           O  
-HETATM 4626  O   HOH B 356      63.372   3.046 -33.199  1.00 27.62           O  
-HETATM 4627  O   HOH B 357      19.336 -16.097 -45.895  1.00 24.67           O  
-HETATM 4628  O   HOH B 358      48.074 -10.555 -32.236  1.00 48.24           O  
-HETATM 4629  O   HOH B 359      14.543 -12.733 -56.640  1.00 20.80           O  
-HETATM 4630  O   HOH B 360      22.083 -14.607 -41.648  1.00 32.57           O  
-HETATM 4631  O   HOH B 361      25.236  -8.332 -34.797  1.00 40.68           O  
-HETATM 4632  O   HOH B 362      12.818  10.476 -55.270  1.00 30.75           O  
-HETATM 4633  O   HOH B 363      16.895  12.180 -53.136  1.00 36.23           O  
-HETATM 4634  O   HOH B 364      23.786 -10.825 -40.719  1.00 26.33           O  
-HETATM 4635  O   HOH B 365      56.018  10.544 -31.569  1.00 23.63           O  
-HETATM 4636  O   HOH B 366      28.437 -25.782 -45.558  1.00 35.22           O  
-HETATM 4637  O   HOH B 367       5.579  11.030 -54.613  1.00 30.71           O  
-HETATM 4638  O   HOH B 368      58.132  -2.599 -45.562  1.00 34.78           O  
-HETATM 4639  O   HOH B 369      30.795  21.865 -56.298  1.00 43.93           O  
-HETATM 4640  O   HOH B 370      15.124  -0.822 -63.731  1.00 28.03           O  
-HETATM 4641  O   HOH B 371      14.710  -3.405 -64.861  1.00 36.39           O  
-HETATM 4642  O   HOH B 372      28.450 -26.088 -48.086  1.00 30.35           O  
-HETATM 4643  O   HOH B 373      29.053 -16.763 -59.438  1.00 28.15           O  
-HETATM 4644  O   HOH B 374      28.329 -17.870 -63.799  1.00 34.92           O  
-HETATM 4645  O   HOH B 375      58.284  -9.343 -48.644  1.00 42.07           O  
-HETATM 4646  O   HOH B 376      43.608 -17.264 -45.373  1.00 29.42           O  
-HETATM 4647  O   HOH B 377      27.898   1.712 -62.462  1.00 39.44           O  
-HETATM 4648  O   HOH B 378      25.354   7.994 -59.092  1.00 33.61           O  
-HETATM 4649  O   HOH B 379      38.214 -11.605 -34.214  1.00 32.06           O  
-HETATM 4650  O   HOH B 380       6.027   7.361 -48.334  1.00 37.17           O  
-HETATM 4651  O   HOH B 381      16.121   0.714 -65.524  1.00 26.92           O  
-HETATM 4652  O   HOH B 382      38.848  13.025 -57.102  1.00 33.09           O  
-HETATM 4653  O   HOH B 383      33.209  14.046 -47.514  1.00 34.84           O  
-HETATM 4654  O   HOH B 384      35.810  13.436 -53.835  1.00 29.82           O  
-HETATM 4655  O   HOH B 385      29.868  14.953 -50.178  1.00 38.67           O  
-HETATM 4656  O   HOH B 386      30.880  12.717 -48.873  1.00 32.10           O  
-HETATM 4657  O   HOH B 387      17.821 -18.633 -61.805  1.00 43.70           O  
-HETATM 4658  O   HOH B 388      13.136 -14.002 -60.315  1.00 29.49           O  
-HETATM 4659  O   HOH B 389      24.556 -16.565 -69.080  1.00 44.69           O  
-HETATM 4660  O   HOH B 390      24.726 -23.913 -53.547  1.00 23.72           O  
-HETATM 4661  O   HOH B 391       6.568  -6.990 -52.838  1.00 44.05           O  
-HETATM 4662  O   HOH B 392       9.783  -7.022 -54.741  1.00 26.99           O  
-HETATM 4663  O   HOH B 393       8.912  -7.059 -48.356  1.00 41.66           O  
-HETATM 4664  O   HOH B 394      42.849  -8.746 -35.668  1.00 19.76           O  
-HETATM 4665  O   HOH B 395      45.689 -11.068 -33.313  1.00 36.03           O  
-HETATM 4666  O   HOH B 396      42.890  11.055 -36.163  1.00 36.33           O  
-HETATM 4667  O   HOH B 397      39.056  -2.028 -32.614  1.00 26.44           O  
-HETATM 4668  O   HOH B 398      34.815  -2.009 -31.363  1.00 37.24           O  
-HETATM 4669  O   HOH B 399      62.137 -11.646 -40.719  1.00 36.98           O  
-HETATM 4670  O   HOH B 402      60.221  -8.902 -46.827  1.00 34.85           O  
-HETATM 4671  O   HOH B 403      42.502 -15.595 -37.847  1.00 21.67           O  
-HETATM 4672  O   HOH B 404      19.053 -17.660 -43.587  1.00 21.57           O  
-HETATM 4673  O   HOH B 405      34.815  -8.731 -62.321  1.00 24.27           O  
-HETATM 4674  O   HOH B 406      16.842 -13.784 -48.333  1.00 20.76           O  
-HETATM 4675  O   HOH B 407      34.386 -10.745 -37.140  1.00 30.56           O  
-HETATM 4676  O   HOH B 408      21.510  -3.594 -31.134  1.00 43.79           O  
-HETATM 4677  O   HOH B 409      61.648  -1.499 -33.543  1.00 31.93           O  
-HETATM 4678  O   HOH B 410      25.756  -8.332 -37.464  1.00 30.07           O  
-HETATM 4679  O   HOH B 411      27.212  -0.268 -60.859  1.00 27.11           O  
-HETATM 4680  O   HOH B 412      36.100   8.459 -40.341  1.00 36.82           O  
-HETATM 4681  O   HOH B 413      18.652 -10.959 -69.463  1.00 39.33           O  
-HETATM 4682  O   HOH B 414      18.426  -2.579 -68.733  1.00 37.61           O  
-HETATM 4683  O   HOH B 415      10.630  -2.210 -49.141  1.00 33.12           O  
-HETATM 4684  O   HOH B 416      14.529  12.600 -55.042  1.00 33.28           O  
-HETATM 4685  O   HOH B 417      18.470  12.984 -40.409  1.00 37.05           O  
-HETATM 4686  O   HOH B 418      29.692  10.236 -62.810  1.00 40.92           O  
-HETATM 4687  O   HOH B 419      25.056  19.026 -57.426  1.00 38.20           O  
-HETATM 4688  O   HOH B 420      34.652  12.743 -51.716  1.00 37.52           O  
-HETATM 4689  O   HOH B 421      28.854 -22.453 -59.457  1.00 34.58           O  
-HETATM 4690  O   HOH B 422      11.028  -0.693 -44.427  1.00 29.96           O  
-HETATM 4691  O   HOH B 423      44.813  11.209 -33.027  1.00 37.06           O  
-HETATM 4692  O   HOH B 424      48.006 -15.164 -48.477  1.00 31.31           O  
-HETATM 4693  O   HOH B 425      53.092  15.450 -39.399  1.00 49.74           O  
-HETATM 4694  O   HOH B 426      58.096   8.222 -44.299  1.00 28.84           O  
-HETATM 4695  O   HOH B 427       4.039   1.344 -49.481  1.00 43.71           O  
-HETATM 4696  O   HOH B 428      10.361  -0.784 -46.906  1.00 46.39           O  
-HETATM 4697  O   HOH B 429      10.223  -8.650 -46.620  1.00 35.40           O  
-HETATM 4698  O   HOH B 430      44.910  13.732 -49.430  1.00 30.88           O  
-HETATM 4699  O   HOH B 431      16.748 -16.048 -47.170  1.00 32.38           O  
-HETATM 4700  O   HOH B 432      24.094  -7.917 -39.702  1.00 23.10           O  
-HETATM 4701  O   HOH B 433      21.787  -7.723 -38.940  1.00 28.60           O  
-HETATM 4702  O   HOH B 434      41.396 -14.114 -35.753  1.00 25.07           O  
-HETATM 4703  O   HOH B 435      40.344 -11.185 -35.704  1.00 40.68           O  
-HETATM 4704  O   HOH B 436      17.810   2.570 -37.972  1.00 20.96           O  
-HETATM 4705  O   HOH B 437      40.735   7.990 -47.167  1.00 21.74           O  
-HETATM 4706  O   HOH B 438       9.997   1.077 -53.692  1.00 21.36           O  
-HETATM 4707  O   HOH B 439      14.448 -13.210 -52.808  1.00 22.53           O  
-HETATM 4708  O   HOH B 440      19.391 -21.114 -48.705  1.00 19.22           O  
-HETATM 4709  O   HOH B 441      12.917  -8.521 -45.985  1.00 22.02           O  
-HETATM 4710  O   HOH B 442      40.742  -0.314 -31.404  1.00 21.05           O  
-HETATM 4711  O   HOH B 443      49.957 -13.581 -49.306  1.00 24.39           O  
-HETATM 4712  O   HOH B 444      48.501   4.407 -51.757  1.00 24.06           O  
-HETATM 4713  O   HOH B 445      26.834 -15.040 -39.485  1.00 24.42           O  
-HETATM 4714  O   HOH B 446      33.991   6.030 -39.921  1.00 25.75           O  
-HETATM 4715  O   HOH B 447      44.552   1.069 -50.796  1.00 29.46           O  
-HETATM 4716  O   HOH B 448      55.929   8.313 -42.579  1.00 23.67           O  
-HETATM 4717  O   HOH B 449      42.386   1.582 -32.558  1.00 24.00           O  
-HETATM 4718  O   HOH B 450      41.849  -6.773 -34.334  1.00 28.27           O  
-HETATM 4719  O   HOH B 451      14.449 -10.699 -45.989  1.00 34.42           O  
-HETATM 4720  O   HOH B 452      52.270 -15.117 -49.008  1.00 28.67           O  
-HETATM 4721  O   HOH B 453      16.877 -14.549 -67.424  1.00 28.33           O  
-HETATM 4722  O   HOH B 454      19.266 -20.334 -51.327  1.00 21.47           O  
-HETATM 4723  O   HOH B 455      18.720   6.438 -62.683  1.00 26.86           O  
-HETATM 4724  O   HOH B 456      52.822  -3.095 -50.889  1.00 21.29           O  
-HETATM 4725  O   HOH B 457      32.369 -16.897 -58.237  1.00 31.43           O  
-HETATM 4726  O   HOH B 458      14.778 -16.070 -60.891  1.00 31.27           O  
-HETATM 4727  O   HOH B 459      55.701   5.807 -42.631  1.00 31.37           O  
-HETATM 4728  O   HOH B 460      41.918  -8.081 -58.014  1.00 33.30           O  
-HETATM 4729  O   HOH B 461      51.727   8.909 -30.639  1.00 24.86           O  
-HETATM 4730  O   HOH B 462      43.488  -0.745 -52.526  1.00 42.54           O  
-HETATM 4731  O   HOH B 463      51.003  -2.165 -31.417  1.00 26.05           O  
-HETATM 4732  O   HOH B 464      42.821  -5.414 -51.087  1.00 22.93           O  
-HETATM 4733  O   HOH B 465      53.801   4.075 -45.673  1.00 24.64           O  
-HETATM 4734  O   HOH B 466      55.467  13.114 -34.089  1.00 34.39           O  
-HETATM 4735  O   HOH B 467      23.046   8.297 -39.147  1.00 35.47           O  
-HETATM 4736  O   HOH B 468      48.077  10.819 -34.190  1.00 29.02           O  
-HETATM 4737  O   HOH B 469      54.965  -2.597 -48.906  1.00 27.94           O  
-HETATM 4738  O   HOH B 470      26.217  -7.663 -66.138  1.00 24.08           O  
-HETATM 4739  O   HOH B 471      41.959  -5.832 -31.871  1.00 21.26           O  
-HETATM 4740  O   HOH B 472      28.402   6.860 -44.058  1.00 26.70           O  
-HETATM 4741  O   HOH B 473      34.242  -2.925 -34.268  1.00 36.35           O  
-HETATM 4742  O   HOH B 474      46.717  14.260 -36.556  1.00 35.71           O  
-HETATM 4743  O   HOH B 475      27.097 -20.752 -58.320  1.00 30.93           O  
-CONECT  998 4277                                                                
-CONECT 1013 4277                                                                
-CONECT 4233 4247 4248 4259                                                      
-CONECT 4234 4235 4240                                                           
-CONECT 4235 4234 4236 4237                                                      
-CONECT 4236 4235                                                                
-CONECT 4237 4235 4238                                                           
-CONECT 4238 4237 4239 4244                                                      
-CONECT 4239 4238 4240 4242                                                      
-CONECT 4240 4234 4239 4241                                                      
-CONECT 4241 4240                                                                
-CONECT 4242 4239 4243                                                           
-CONECT 4243 4242 4244                                                           
-CONECT 4244 4238 4243 4250                                                      
-CONECT 4245 4249 4255 4260 4267                                                 
-CONECT 4246 4251 4257 4260 4262                                                 
-CONECT 4247 4233 4252 4269                                                      
-CONECT 4248 4233                                                                
-CONECT 4249 4245                                                                
-CONECT 4250 4244 4256 4264                                                      
-CONECT 4251 4246                                                                
-CONECT 4252 4247 4253 4258                                                      
-CONECT 4253 4252 4270                                                           
-CONECT 4254 4256                                                                
-CONECT 4255 4245                                                                
-CONECT 4256 4250 4254 4261                                                      
-CONECT 4257 4246                                                                
-CONECT 4258 4252 4263                                                           
-CONECT 4259 4233 4261                                                           
-CONECT 4260 4245 4246                                                           
-CONECT 4261 4256 4259 4265                                                      
-CONECT 4262 4246                                                                
-CONECT 4263 4258 4266                                                           
-CONECT 4264 4250 4265                                                           
-CONECT 4265 4261 4264 4268                                                      
-CONECT 4266 4263 4269                                                           
-CONECT 4267 4245 4268                                                           
-CONECT 4268 4265 4267                                                           
-CONECT 4269 4247 4266                                                           
-CONECT 4270 4253                                                                
-CONECT 4271 4272 4273                                                           
-CONECT 4272 4271                                                                
-CONECT 4273 4271 4274 4275                                                      
-CONECT 4274 4273                                                                
-CONECT 4275 4273 4276                                                           
-CONECT 4276 4275                                                                
-CONECT 4277  998 1013 4413 4415                                                 
-CONECT 4277 4416                                                                
-CONECT 4278 4292 4293 4304                                                      
-CONECT 4279 4280 4285                                                           
-CONECT 4280 4279 4281 4282                                                      
-CONECT 4281 4280                                                                
-CONECT 4282 4280 4283                                                           
-CONECT 4283 4282 4284 4289                                                      
-CONECT 4284 4283 4285 4287                                                      
-CONECT 4285 4279 4284 4286                                                      
-CONECT 4286 4285                                                                
-CONECT 4287 4284 4288                                                           
-CONECT 4288 4287 4289                                                           
-CONECT 4289 4283 4288 4295                                                      
-CONECT 4290 4294 4300 4305 4312                                                 
-CONECT 4291 4296 4302 4305 4307                                                 
-CONECT 4292 4278 4297 4314                                                      
-CONECT 4293 4278                                                                
-CONECT 4294 4290                                                                
-CONECT 4295 4289 4301 4309                                                      
-CONECT 4296 4291                                                                
-CONECT 4297 4292 4298 4303                                                      
-CONECT 4298 4297 4315                                                           
-CONECT 4299 4301                                                                
-CONECT 4300 4290                                                                
-CONECT 4301 4295 4299 4306                                                      
-CONECT 4302 4291                                                                
-CONECT 4303 4297 4308                                                           
-CONECT 4304 4278 4306                                                           
-CONECT 4305 4290 4291                                                           
-CONECT 4306 4301 4304 4310                                                      
-CONECT 4307 4291                                                                
-CONECT 4308 4303 4311                                                           
-CONECT 4309 4295 4310                                                           
-CONECT 4310 4306 4309 4313                                                      
-CONECT 4311 4308 4314                                                           
-CONECT 4312 4290 4313                                                           
-CONECT 4313 4310 4312                                                           
-CONECT 4314 4292 4311                                                           
-CONECT 4315 4298                                                                
-CONECT 4316 4317 4318                                                           
-CONECT 4317 4316                                                                
-CONECT 4318 4316 4319 4320                                                      
-CONECT 4319 4318                                                                
-CONECT 4320 4318 4321                                                           
-CONECT 4321 4320                                                                
-CONECT 4322 4323 4324                                                           
-CONECT 4323 4322                                                                
-CONECT 4324 4322 4325 4326                                                      
-CONECT 4325 4324                                                                
-CONECT 4326 4324 4327                                                           
-CONECT 4327 4326                                                                
-CONECT 4413 4277                                                                
-CONECT 4415 4277                                                                
-CONECT 4416 4277                                                                
-MASTER      369    0    6   22   16    0   19    6 4557    2  101   42          
-END                                                                             
diff --git a/plip/test/pdb/3thy.pdb b/plip/test/pdb/3thy.pdb
deleted file mode 100644
index ad0c6a2..0000000
--- a/plip/test/pdb/3thy.pdb
+++ /dev/null
@@ -1,30958 +0,0 @@
-HEADER    DNA BINDING PROTEIN/DNA                 19-AUG-11   3THY              
-TITLE     HUMAN MUTSBETA COMPLEXED WITH AN IDL OF 2 BASES (LOOP2) AND ADP       
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: DNA MISMATCH REPAIR PROTEIN MSH2;                          
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 SYNONYM: HMSH2, MUTS PROTEIN HOMOLOG 2;                              
-COMPND   5 ENGINEERED: YES;                                                     
-COMPND   6 MOL_ID: 2;                                                           
-COMPND   7 MOLECULE: DNA MISMATCH REPAIR PROTEIN MSH3;                          
-COMPND   8 CHAIN: B;                                                            
-COMPND   9 FRAGMENT: UNP RESIDUES 219- 1134;                                    
-COMPND  10 SYNONYM: HMSH3, DIVERGENT UPSTREAM PROTEIN, DUP, MISMATCH REPAIR     
-COMPND  11 PROTEIN 1, MRP1;                                                     
-COMPND  12 ENGINEERED: YES;                                                     
-COMPND  13 MOL_ID: 3;                                                           
-COMPND  14 MOLECULE: DNA LOOP2 MINUS STRAND;                                    
-COMPND  15 CHAIN: D;                                                            
-COMPND  16 ENGINEERED: YES;                                                     
-COMPND  17 MOL_ID: 4;                                                           
-COMPND  18 MOLECULE: DNA LOOP2 PLUS STRAND;                                     
-COMPND  19 CHAIN: E;                                                            
-COMPND  20 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: MSH2;                                                          
-SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
-SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HI5;                                    
-SOURCE   9 MOL_ID: 2;                                                           
-SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
-SOURCE  12 ORGANISM_TAXID: 9606;                                                
-SOURCE  13 GENE: DUC1, DUG, MSH3;                                               
-SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
-SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7108;                                       
-SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: HI5;                                    
-SOURCE  17 MOL_ID: 3;                                                           
-SOURCE  18 SYNTHETIC: YES;                                                      
-SOURCE  19 OTHER_DETAILS: CHEMICALLY SYNTHESIZED DNA;                           
-SOURCE  20 MOL_ID: 4;                                                           
-SOURCE  21 SYNTHETIC: YES;                                                      
-SOURCE  22 OTHER_DETAILS: CHEMICALLY SYNTHESIZED DNA                            
-KEYWDS    ABC FAMILY ATPASE, MISMATCH RECOGNITION, MISMATCHED UNPAIRED IDL DNA, 
-KEYWDS   2 DNA BINDING PROTEIN-DNA COMPLEX                                      
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    W.YANG                                                                
-REVDAT   2   26-JUN-13 3THY    1       JRNL                                     
-REVDAT   1   21-DEC-11 3THY    0                                                
-JRNL        AUTH   S.GUPTA,M.GELLERT,W.YANG                                     
-JRNL        TITL   MECHANISM OF MISMATCH REPAIR REVEALED BY HUMAN MUTSBETA      
-JRNL        TITL 2 BOUND TO UNPAIRED DNA LOOPS                                  
-JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  19    72 2012              
-JRNL        REFN                   ISSN 1545-9993                               
-JRNL        PMID   22179786                                                     
-JRNL        DOI    10.1038/NSMB.2175                                            
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.89 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : ML                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.19                          
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.000                          
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.3                           
-REMARK   3   NUMBER OF REFLECTIONS             : 39845                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
-REMARK   3   R VALUE            (WORKING SET) : 0.194                           
-REMARK   3   FREE R VALUE                     : 0.274                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.820                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1125                            
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 44.1943 -  5.7844    0.98     5291   158  0.1627 0.2319        
-REMARK   3     2  5.7844 -  4.5928    0.99     5282   140  0.1776 0.2684        
-REMARK   3     3  4.5928 -  4.0127    0.98     5269   135  0.1641 0.2254        
-REMARK   3     4  4.0127 -  3.6460    0.97     5197   154  0.1943 0.2920        
-REMARK   3     5  3.6460 -  3.3848    0.95     5098   168  0.2195 0.2918        
-REMARK   3     6  3.3848 -  3.1853    0.92     4904   155  0.2554 0.3453        
-REMARK   3     7  3.1853 -  3.0258    0.83     4430   130  0.2744 0.3447        
-REMARK   3     8  3.0258 -  2.8941    0.61     3249    85  0.3124 0.3904        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.10                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
-REMARK   3   K_SOL              : 0.31                                          
-REMARK   3   B_SOL              : 53.72                                         
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.050           
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 12.95940                                             
-REMARK   3    B22 (A**2) : 3.34570                                              
-REMARK   3    B33 (A**2) : -16.30510                                            
-REMARK   3    B12 (A**2) : -2.57600                                             
-REMARK   3    B13 (A**2) : 13.76210                                             
-REMARK   3    B23 (A**2) : 3.33880                                              
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.003          15026                                  
-REMARK   3   ANGLE     :  0.682          20505                                  
-REMARK   3   CHIRALITY :  0.045           2358                                  
-REMARK   3   PLANARITY :  0.002           2468                                  
-REMARK   3   DIHEDRAL  : 17.413           5666                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : 51                                         
-REMARK   3   TLS GROUP : 1                                                      
-REMARK   3    SELECTION: (chain A and resid 12:117)                             
-REMARK   3    ORIGIN FOR THE GROUP (A):   1.0523  -1.4696  28.7427              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3400 T22:   0.3026                                     
-REMARK   3      T33:   0.3439 T12:   0.0110                                     
-REMARK   3      T13:  -0.1460 T23:  -0.0951                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.3115 L22:   2.9973                                     
-REMARK   3      L33:   1.2617 L12:  -0.9280                                     
-REMARK   3      L13:   1.5312 L23:  -0.3328                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0783 S12:  -0.3526 S13:   0.0723                       
-REMARK   3      S21:   0.2019 S22:  -0.0083 S23:  -0.4031                       
-REMARK   3      S31:   0.1335 S32:  -0.3189 S33:  -0.0001                       
-REMARK   3   TLS GROUP : 2                                                      
-REMARK   3    SELECTION: (chain A and resid 118:175)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   5.5775 -19.2949   9.1275              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2409 T22:   0.2999                                     
-REMARK   3      T33:   0.3540 T12:   0.0340                                     
-REMARK   3      T13:  -0.0624 T23:   0.0226                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.2492 L22:   1.3940                                     
-REMARK   3      L33:   1.1083 L12:  -1.0362                                     
-REMARK   3      L13:   0.8384 L23:  -1.7477                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0917 S12:   0.4588 S13:   0.2455                       
-REMARK   3      S21:   0.0138 S22:  -0.1391 S23:  -0.1642                       
-REMARK   3      S31:   0.5203 S32:  -0.2151 S33:  -0.0166                       
-REMARK   3   TLS GROUP : 3                                                      
-REMARK   3    SELECTION: (chain A and resid 176:231)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  15.9948 -14.8096   2.2256              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3906 T22:   0.4400                                     
-REMARK   3      T33:   0.4120 T12:  -0.0939                                     
-REMARK   3      T13:  -0.0668 T23:   0.1382                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.0522 L22:   1.2511                                     
-REMARK   3      L33:   1.7619 L12:  -0.5214                                     
-REMARK   3      L13:  -0.2609 L23:  -1.1762                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1545 S12:   0.0344 S13:   0.0811                       
-REMARK   3      S21:  -0.3158 S22:  -0.2779 S23:  -0.4376                       
-REMARK   3      S31:  -0.3927 S32:   0.6006 S33:  -0.0005                       
-REMARK   3   TLS GROUP : 4                                                      
-REMARK   3    SELECTION: (chain A and resid 232:260)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   9.7804 -36.3742  13.9073              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.0200 T22:   0.3855                                     
-REMARK   3      T33:   0.5943 T12:   0.1594                                     
-REMARK   3      T13:   0.0797 T23:   0.1467                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.3548 L22:   0.1707                                     
-REMARK   3      L33:   0.2648 L12:  -0.0160                                     
-REMARK   3      L13:  -0.0786 L23:   0.1702                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.2908 S12:  -0.4233 S13:   0.0188                       
-REMARK   3      S21:  -1.0729 S22:  -0.3890 S23:  -0.2529                       
-REMARK   3      S31:   1.3656 S32:   0.8490 S33:  -0.0012                       
-REMARK   3   TLS GROUP : 5                                                      
-REMARK   3    SELECTION: (chain A and resid 261:295)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   8.1342 -27.5641  11.8127              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.7543 T22:   0.2850                                     
-REMARK   3      T33:   0.4728 T12:  -0.0133                                     
-REMARK   3      T13:  -0.0018 T23:   0.0180                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.4964 L22:   0.5852                                     
-REMARK   3      L33:   1.3601 L12:  -0.5000                                     
-REMARK   3      L13:   0.7137 L23:  -1.0280                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.1642 S12:  -0.3845 S13:  -0.2434                       
-REMARK   3      S21:   0.4550 S22:  -0.4729 S23:  -0.0617                       
-REMARK   3      S31:   1.0270 S32:  -0.3866 S33:  -0.0103                       
-REMARK   3   TLS GROUP : 6                                                      
-REMARK   3    SELECTION: (chain A and resid 296:380)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  -8.6831 -19.6327  -8.7369              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4130 T22:   0.6958                                     
-REMARK   3      T33:   0.2179 T12:  -0.2199                                     
-REMARK   3      T13:  -0.0726 T23:   0.1132                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.8499 L22:   0.7959                                     
-REMARK   3      L33:   1.0019 L12:   0.8104                                     
-REMARK   3      L13:  -0.8571 L23:  -2.0131                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.2588 S12:   0.2440 S13:   0.4535                       
-REMARK   3      S21:  -0.1739 S22:   0.5886 S23:  -0.0788                       
-REMARK   3      S31:   0.2117 S32:  -0.7173 S33:   0.1113                       
-REMARK   3   TLS GROUP : 7                                                      
-REMARK   3    SELECTION: (chain A and resid 381:441)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -20.3581 -29.7203   4.5175              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5346 T22:   1.1109                                     
-REMARK   3      T33:   0.6518 T12:  -0.4470                                     
-REMARK   3      T13:  -0.1263 T23:   0.1156                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:  -0.2641 L22:   0.6934                                     
-REMARK   3      L33:   0.7846 L12:   0.1854                                     
-REMARK   3      L13:   0.2994 L23:   0.6556                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.2445 S12:   0.8503 S13:   0.5484                       
-REMARK   3      S21:   0.3487 S22:   0.6077 S23:   0.1366                       
-REMARK   3      S31:   0.2368 S32:   0.2655 S33:   0.0124                       
-REMARK   3   TLS GROUP : 8                                                      
-REMARK   3    SELECTION: (chain A and resid 442:470)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -26.9802 -31.8947  17.6261              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.8656 T22:   1.0602                                     
-REMARK   3      T33:   0.7386 T12:  -0.4407                                     
-REMARK   3      T13:   0.0322 T23:   0.1942                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.2897 L22:   0.2534                                     
-REMARK   3      L33:   0.1762 L12:   0.0625                                     
-REMARK   3      L13:   0.2682 L23:   0.2013                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1511 S12:   0.0142 S13:   0.5370                       
-REMARK   3      S21:   0.2369 S22:   0.4551 S23:  -0.3659                       
-REMARK   3      S31:   1.3583 S32:  -1.1419 S33:   0.0004                       
-REMARK   3   TLS GROUP : 9                                                      
-REMARK   3    SELECTION: (chain A and resid 471:482)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -32.4139 -35.5797  33.2660              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.3381 T22:   1.1221                                     
-REMARK   3      T33:   1.3139 T12:  -0.1535                                     
-REMARK   3      T13:   0.5260 T23:  -0.3775                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0020 L22:  -0.0086                                     
-REMARK   3      L33:   0.0772 L12:  -0.0085                                     
-REMARK   3      L13:   0.0603 L23:  -0.0576                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.4984 S12:   0.3725 S13:  -0.2509                       
-REMARK   3      S21:   1.0407 S22:   0.1510 S23:  -0.0043                       
-REMARK   3      S31:   0.8095 S32:  -0.6291 S33:   0.0003                       
-REMARK   3   TLS GROUP : 10                                                     
-REMARK   3    SELECTION: (chain A and resid 483:554)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -39.9470 -13.3383  50.8897              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.9532 T22:   0.9511                                     
-REMARK   3      T33:   0.9476 T12:  -0.1976                                     
-REMARK   3      T13:   0.4373 T23:  -0.2038                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.8048 L22:   0.2101                                     
-REMARK   3      L33:   2.8678 L12:  -0.5328                                     
-REMARK   3      L13:   2.9282 L23:  -0.1545                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.8093 S12:  -0.3929 S13:   0.1513                       
-REMARK   3      S21:   0.3071 S22:   0.1610 S23:   0.1820                       
-REMARK   3      S31:   0.0747 S32:  -0.0124 S33:  -3.2611                       
-REMARK   3   TLS GROUP : 11                                                     
-REMARK   3    SELECTION: (chain A and resid 555:580)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -28.2326 -28.2479  41.6447              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.4943 T22:   1.0151                                     
-REMARK   3      T33:   0.7761 T12:  -0.0078                                     
-REMARK   3      T13:   0.0264 T23:  -0.2082                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0774 L22:  -0.0434                                     
-REMARK   3      L33:   0.2177 L12:   0.0174                                     
-REMARK   3      L13:   0.1940 L23:  -0.0192                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.5332 S12:  -0.9489 S13:  -0.1759                       
-REMARK   3      S21:   0.2340 S22:  -0.4365 S23:  -0.4693                       
-REMARK   3      S31:  -0.7575 S32:   0.5396 S33:   0.0001                       
-REMARK   3   TLS GROUP : 12                                                     
-REMARK   3    SELECTION: (chain A and resid 581:645)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -11.2198 -22.0869  -9.3429              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2552 T22:   0.8607                                     
-REMARK   3      T33:   0.4063 T12:  -0.4229                                     
-REMARK   3      T13:  -0.1774 T23:   0.1275                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:  -0.0181 L22:   2.2697                                     
-REMARK   3      L33:   1.3002 L12:   0.5734                                     
-REMARK   3      L13:  -1.8916 L23:   0.0133                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0150 S12:   0.3651 S13:  -0.1165                       
-REMARK   3      S21:  -0.1892 S22:   0.1730 S23:   0.2105                       
-REMARK   3      S31:   0.5254 S32:  -0.3367 S33:  -0.0016                       
-REMARK   3   TLS GROUP : 13                                                     
-REMARK   3    SELECTION: (chain A and resid 646:650)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -14.8414  -0.0300 -19.9174              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.1737 T22:   0.9947                                     
-REMARK   3      T33:   0.9830 T12:  -0.2670                                     
-REMARK   3      T13:  -0.5495 T23:   0.3902                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0794 L22:   0.0030                                     
-REMARK   3      L33:   0.0597 L12:   0.0273                                     
-REMARK   3      L13:  -0.0674 L23:  -0.0275                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.5428 S12:   0.1128 S13:  -0.5462                       
-REMARK   3      S21:  -0.1002 S22:  -0.7352 S23:  -0.5949                       
-REMARK   3      S31:  -0.1516 S32:  -0.2179 S33:   0.0007                       
-REMARK   3   TLS GROUP : 14                                                     
-REMARK   3    SELECTION: (chain A and resid 651:749)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   4.3921 -10.7931 -21.6832              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3818 T22:   0.3912                                     
-REMARK   3      T33:   0.1717 T12:  -0.1251                                     
-REMARK   3      T13:  -0.0249 T23:   0.0148                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.0012 L22:   1.2107                                     
-REMARK   3      L33:   3.0202 L12:   0.4957                                     
-REMARK   3      L13:  -0.3368 L23:  -0.4335                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1367 S12:   0.3170 S13:   0.1536                       
-REMARK   3      S21:  -0.4389 S22:   0.1183 S23:  -0.1290                       
-REMARK   3      S31:   0.4479 S32:  -0.5111 S33:  -0.0003                       
-REMARK   3   TLS GROUP : 15                                                     
-REMARK   3    SELECTION: (chain A and resid 750:763)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  19.2638   3.7462 -23.9827              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5089 T22:   0.4017                                     
-REMARK   3      T33:   0.4377 T12:   0.1247                                     
-REMARK   3      T13:   0.0656 T23:   0.0774                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.1404 L22:   0.3426                                     
-REMARK   3      L33:   0.1775 L12:  -0.1277                                     
-REMARK   3      L13:   0.1533 L23:  -0.0269                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.3575 S12:   1.0754 S13:   0.9301                       
-REMARK   3      S21:  -0.3481 S22:   0.7301 S23:   0.6373                       
-REMARK   3      S31:  -0.2799 S32:   0.3567 S33:   0.0015                       
-REMARK   3   TLS GROUP : 16                                                     
-REMARK   3    SELECTION: (chain A and resid 764:825)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   6.8873  -1.5268 -31.3470              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4056 T22:   0.5682                                     
-REMARK   3      T33:   0.1799 T12:  -0.0817                                     
-REMARK   3      T13:  -0.0465 T23:   0.1063                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.9941 L22:   1.0525                                     
-REMARK   3      L33:   1.2651 L12:   0.2164                                     
-REMARK   3      L13:  -0.3475 L23:  -0.3275                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0313 S12:   0.2988 S13:  -0.1535                       
-REMARK   3      S21:  -0.4862 S22:   0.4004 S23:  -0.0734                       
-REMARK   3      S31:   0.2220 S32:  -0.3293 S33:   0.0467                       
-REMARK   3   TLS GROUP : 17                                                     
-REMARK   3    SELECTION: (chain A and resid 826:882)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  10.9367  16.9383 -37.0071              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.0618 T22:   0.8771                                     
-REMARK   3      T33:   0.6155 T12:   0.0169                                     
-REMARK   3      T13:  -0.0819 T23:   0.1807                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.1513 L22:   0.0870                                     
-REMARK   3      L33:   0.6851 L12:   0.2666                                     
-REMARK   3      L13:  -0.0701 L23:  -0.0782                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.2027 S12:   0.5417 S13:   0.2634                       
-REMARK   3      S21:  -0.7277 S22:   0.5718 S23:   0.3113                       
-REMARK   3      S31:  -0.4289 S32:  -0.8805 S33:   0.0004                       
-REMARK   3   TLS GROUP : 18                                                     
-REMARK   3    SELECTION: (chain A and resid 883:897)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  33.9474  19.8576 -52.4959              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.0132 T22:   0.7294                                     
-REMARK   3      T33:   0.8187 T12:   0.2891                                     
-REMARK   3      T13:   0.2291 T23:   0.1251                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0550 L22:   0.1390                                     
-REMARK   3      L33:   2.7109 L12:   0.1226                                     
-REMARK   3      L13:  -0.3673 L23:  -0.5824                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0799 S12:   0.2981 S13:   0.5935                       
-REMARK   3      S21:  -0.3005 S22:   0.2854 S23:  -0.5894                       
-REMARK   3      S31:   2.8950 S32:   0.8582 S33:   0.0203                       
-REMARK   3   TLS GROUP : 19                                                     
-REMARK   3    SELECTION: (chain A and resid 898:907)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  36.6765  31.4150 -58.6805              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.0824 T22:   1.3724                                     
-REMARK   3      T33:   0.9957 T12:  -0.2540                                     
-REMARK   3      T13:  -0.0007 T23:   0.0554                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0266 L22:   0.0773                                     
-REMARK   3      L33:   0.0194 L12:   0.0438                                     
-REMARK   3      L13:   0.0013 L23:   0.0711                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -1.1721 S12:   0.2245 S13:   0.9284                       
-REMARK   3      S21:  -0.4288 S22:   0.0752 S23:  -1.0785                       
-REMARK   3      S31:   0.2289 S32:   0.6153 S33:   0.0015                       
-REMARK   3   TLS GROUP : 20                                                     
-REMARK   3    SELECTION: (chain A and resid 908:930)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  20.5523  20.0923 -55.0910              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.7298 T22:   0.6520                                     
-REMARK   3      T33:   0.2029 T12:  -0.3262                                     
-REMARK   3      T13:  -0.0957 T23:   0.0596                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0131 L22:   0.4578                                     
-REMARK   3      L33:   0.2514 L12:  -0.0685                                     
-REMARK   3      L13:   0.0427 L23:   0.0003                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1581 S12:   0.6444 S13:   0.5127                       
-REMARK   3      S21:  -0.3967 S22:   0.6227 S23:   0.0060                       
-REMARK   3      S31:  -0.3593 S32:  -1.2637 S33:   0.0007                       
-REMARK   3   TLS GROUP : 21                                                     
-REMARK   3    SELECTION: (chain B and resid 226:301)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -26.0822   7.5883  21.0808              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1700 T22:   0.4776                                     
-REMARK   3      T33:   0.3780 T12:  -0.0167                                     
-REMARK   3      T13:  -0.0826 T23:  -0.0646                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.7478 L22:   0.6432                                     
-REMARK   3      L33:   0.8408 L12:   0.5904                                     
-REMARK   3      L13:  -0.4929 L23:   0.4527                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1053 S12:   0.1714 S13:   0.0335                       
-REMARK   3      S21:   0.2401 S22:  -0.0835 S23:  -0.0447                       
-REMARK   3      S31:   0.2634 S32:  -0.8401 S33:  -0.0001                       
-REMARK   3   TLS GROUP : 22                                                     
-REMARK   3    SELECTION: (chain B and resid 302:346)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -26.4720  19.0982  26.6675              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3614 T22:   0.4533                                     
-REMARK   3      T33:   0.4162 T12:   0.1923                                     
-REMARK   3      T13:  -0.0281 T23:   0.0088                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.7297 L22:   1.2594                                     
-REMARK   3      L33:   0.3687 L12:  -0.3180                                     
-REMARK   3      L13:   0.4851 L23:   0.3256                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.3934 S12:   0.1442 S13:   0.0813                       
-REMARK   3      S21:   0.0697 S22:  -0.1371 S23:  -0.0350                       
-REMARK   3      S31:  -0.4596 S32:  -0.3938 S33:   0.0003                       
-REMARK   3   TLS GROUP : 23                                                     
-REMARK   3    SELECTION: (chain B and resid 347:367)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8212  18.7476  20.1303              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.1353 T22:   0.3726                                     
-REMARK   3      T33:   0.4518 T12:   0.0144                                     
-REMARK   3      T13:   0.1980 T23:  -0.1980                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.5589 L22:   0.2458                                     
-REMARK   3      L33:   0.1130 L12:   0.3493                                     
-REMARK   3      L13:   0.0027 L23:  -0.2253                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.4124 S12:   0.3141 S13:   1.0032                       
-REMARK   3      S21:   0.4488 S22:  -0.3373 S23:   0.0164                       
-REMARK   3      S31:   1.3739 S32:  -0.3192 S33:   0.0400                       
-REMARK   3   TLS GROUP : 24                                                     
-REMARK   3    SELECTION: (chain B and resid 368:405)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -10.1015  30.0481   0.2611              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5015 T22:   0.7603                                     
-REMARK   3      T33:   0.5201 T12:   0.3550                                     
-REMARK   3      T13:   0.0531 T23:   0.1539                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.9632 L22:   0.6024                                     
-REMARK   3      L33:   0.2067 L12:  -0.2639                                     
-REMARK   3      L13:  -0.2832 L23:  -0.0906                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2743 S12:   0.4329 S13:   0.2425                       
-REMARK   3      S21:   0.1630 S22:  -0.0538 S23:   0.0992                       
-REMARK   3      S31:  -0.8443 S32:  -0.7890 S33:   0.0177                       
-REMARK   3   TLS GROUP : 25                                                     
-REMARK   3    SELECTION: (chain B and resid 406:455)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9593  19.0625  -2.9214              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3753 T22:   0.5446                                     
-REMARK   3      T33:   0.3239 T12:   0.2005                                     
-REMARK   3      T13:  -0.0069 T23:   0.0570                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.1152 L22:   1.4695                                     
-REMARK   3      L33:   0.6923 L12:   0.2750                                     
-REMARK   3      L13:  -0.8465 L23:   0.6664                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2419 S12:   0.4551 S13:  -0.0759                       
-REMARK   3      S21:  -0.0966 S22:  -0.1981 S23:  -0.2042                       
-REMARK   3      S31:   0.1220 S32:  -0.4541 S33:  -0.0001                       
-REMARK   3   TLS GROUP : 26                                                     
-REMARK   3    SELECTION: (chain B and resid 456:519)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -20.2798  33.9336   4.3542              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2837 T22:   0.5381                                     
-REMARK   3      T33:   0.5007 T12:   0.4276                                     
-REMARK   3      T13:   0.1054 T23:   0.1417                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.5124 L22:   1.8153                                     
-REMARK   3      L33:   1.8210 L12:   0.2280                                     
-REMARK   3      L13:  -0.0058 L23:   0.4169                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.6985 S12:   0.4141 S13:  -0.0049                       
-REMARK   3      S21:   0.1663 S22:  -0.2217 S23:   0.2676                       
-REMARK   3      S31:  -0.3974 S32:  -0.8913 S33:   0.2139                       
-REMARK   3   TLS GROUP : 27                                                     
-REMARK   3    SELECTION: (chain B and resid 520:577)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   5.2965  24.9832   5.8943              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3573 T22:   0.3009                                     
-REMARK   3      T33:   0.4148 T12:   0.0753                                     
-REMARK   3      T13:   0.0365 T23:   0.0767                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.7033 L22:   1.5366                                     
-REMARK   3      L33:   0.8606 L12:  -0.4559                                     
-REMARK   3      L13:  -0.9415 L23:   0.8223                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2281 S12:   0.1696 S13:  -0.0134                       
-REMARK   3      S21:  -0.1605 S22:   0.2261 S23:  -0.0531                       
-REMARK   3      S31:  -0.1047 S32:  -0.0103 S33:   0.0003                       
-REMARK   3   TLS GROUP : 28                                                     
-REMARK   3    SELECTION: (chain B and resid 578:588)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  10.0358  35.1478   3.7966              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5746 T22:   0.3385                                     
-REMARK   3      T33:   0.6249 T12:   0.0587                                     
-REMARK   3      T13:   0.2622 T23:  -0.0635                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.3935 L22:   0.9801                                     
-REMARK   3      L33:   2.9234 L12:  -1.0065                                     
-REMARK   3      L13:   1.8989 L23:  -1.0209                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   1.0453 S12:  -0.1015 S13:   0.2438                       
-REMARK   3      S21:   0.1447 S22:   0.5819 S23:  -0.0431                       
-REMARK   3      S31:  -1.0386 S32:  -1.0638 S33:   0.3099                       
-REMARK   3   TLS GROUP : 29                                                     
-REMARK   3    SELECTION: (chain B and resid 589:616)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  19.2294  34.5647  19.7087              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.6181 T22:   0.5163                                     
-REMARK   3      T33:   0.4863 T12:  -0.2058                                     
-REMARK   3      T13:   0.2206 T23:  -0.2243                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.1533 L22:   0.4433                                     
-REMARK   3      L33:   0.8029 L12:   0.1280                                     
-REMARK   3      L13:  -0.6449 L23:   0.1767                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.5908 S12:  -0.5580 S13:   0.2881                       
-REMARK   3      S21:  -0.3911 S22:   0.5896 S23:   0.0519                       
-REMARK   3      S31:  -0.8443 S32:   0.5146 S33:   0.0204                       
-REMARK   3   TLS GROUP : 30                                                     
-REMARK   3    SELECTION: (chain B and resid 617:638)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1311  28.4735  26.2482              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3941 T22:   0.2100                                     
-REMARK   3      T33:   0.3360 T12:   0.0646                                     
-REMARK   3      T13:  -0.0521 T23:   0.0214                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.2094 L22:   0.4804                                     
-REMARK   3      L33:   0.7879 L12:  -0.0610                                     
-REMARK   3      L13:  -0.1167 L23:  -0.8178                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.3711 S12:   0.2186 S13:  -0.3916                       
-REMARK   3      S21:  -0.2790 S22:   0.2203 S23:   0.3296                       
-REMARK   3      S31:   0.5866 S32:   0.0337 S33:   0.0002                       
-REMARK   3   TLS GROUP : 31                                                     
-REMARK   3    SELECTION: (chain B and resid 639:686)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   7.0727  39.8474  28.6311              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.6704 T22:   0.2951                                     
-REMARK   3      T33:   0.4840 T12:  -0.1169                                     
-REMARK   3      T13:   0.0091 T23:  -0.2643                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   3.0400 L22:   0.5814                                     
-REMARK   3      L33:   0.1729 L12:   0.4391                                     
-REMARK   3      L13:   0.4212 L23:   0.0803                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.3261 S12:  -0.9458 S13:   0.2344                       
-REMARK   3      S21:  -0.2934 S22:   0.2126 S23:  -0.0504                       
-REMARK   3      S31:  -0.2128 S32:   0.2132 S33:  -0.0200                       
-REMARK   3   TLS GROUP : 32                                                     
-REMARK   3    SELECTION: (chain B and resid 687:715)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -15.7315  33.2580  43.4913              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.8818 T22:   0.7843                                     
-REMARK   3      T33:   0.6407 T12:  -0.0902                                     
-REMARK   3      T13:   0.2002 T23:  -0.0966                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.1400 L22:   0.5519                                     
-REMARK   3      L33:   0.3661 L12:   0.2249                                     
-REMARK   3      L13:  -0.3183 L23:  -0.0645                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1092 S12:  -0.7241 S13:  -0.1749                       
-REMARK   3      S21:   0.1388 S22:   0.1247 S23:   0.1513                       
-REMARK   3      S31:  -0.6663 S32:   0.6708 S33:  -0.0004                       
-REMARK   3   TLS GROUP : 33                                                     
-REMARK   3    SELECTION: (chain B and resid 716:770)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -29.8741  14.4959  61.7947              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2994 T22:   0.5631                                     
-REMARK   3      T33:   0.5741 T12:   0.1098                                     
-REMARK   3      T13:   0.0226 T23:   0.1597                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.9372 L22:   0.5020                                     
-REMARK   3      L33:   1.7016 L12:  -0.6235                                     
-REMARK   3      L13:   0.2787 L23:   0.7301                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.1116 S12:  -0.9603 S13:  -0.3390                       
-REMARK   3      S21:   0.1274 S22:  -0.0660 S23:  -0.3908                       
-REMARK   3      S31:   0.0990 S32:   0.1371 S33:  -0.0001                       
-REMARK   3   TLS GROUP : 34                                                     
-REMARK   3    SELECTION: (chain B and resid 771:814)                            
-REMARK   3    ORIGIN FOR THE GROUP (A): -27.2866  22.1153  46.1156              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4843 T22:   0.4475                                     
-REMARK   3      T33:   0.5688 T12:   0.1205                                     
-REMARK   3      T13:   0.1103 T23:   0.0593                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.8782 L22:   0.2719                                     
-REMARK   3      L33:   1.4732 L12:   0.1077                                     
-REMARK   3      L13:  -1.0687 L23:   0.4101                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0970 S12:   0.1545 S13:  -0.2814                       
-REMARK   3      S21:   0.3006 S22:  -0.0021 S23:  -0.0145                       
-REMARK   3      S31:  -0.0889 S32:  -0.4451 S33:   0.0001                       
-REMARK   3   TLS GROUP : 35                                                     
-REMARK   3    SELECTION: (chain B and resid 815:849)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  10.0445  32.8054  16.9972              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4518 T22:   0.3019                                     
-REMARK   3      T33:   0.4713 T12:  -0.1130                                     
-REMARK   3      T13:   0.0678 T23:  -0.1075                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.6745 L22:   0.0726                                     
-REMARK   3      L33:   1.6208 L12:   0.3709                                     
-REMARK   3      L13:   1.0832 L23:   0.4231                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2872 S12:  -0.4978 S13:   0.4428                       
-REMARK   3      S21:  -0.0849 S22:   0.3046 S23:  -0.1948                       
-REMARK   3      S31:  -0.5923 S32:   0.5162 S33:   0.0005                       
-REMARK   3   TLS GROUP : 36                                                     
-REMARK   3    SELECTION: (chain B and resid 850:953)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):  21.3626  23.3538  -5.3257              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4167 T22:   0.3668                                     
-REMARK   3      T33:   0.5719 T12:   0.0445                                     
-REMARK   3      T13:   0.0878 T23:  -0.0618                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:  -0.3814 L22:  -0.2474                                     
-REMARK   3      L33:   3.1577 L12:   0.0676                                     
-REMARK   3      L13:  -1.6617 L23:   1.0292                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.4463 S12:   0.0812 S13:   0.1457                       
-REMARK   3      S21:  -0.3475 S22:   0.1244 S23:  -0.2509                       
-REMARK   3      S31:  -0.4027 S32:   0.3183 S33:   0.0002                       
-REMARK   3   TLS GROUP : 37                                                     
-REMARK   3    SELECTION: (chain B and resid 954:979)                            
-REMARK   3    ORIGIN FOR THE GROUP (A):   8.5291  23.5971 -16.4581              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5791 T22:   0.5068                                     
-REMARK   3      T33:   0.5224 T12:   0.3664                                     
-REMARK   3      T13:   0.1106 T23:   0.1499                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.4616 L22:   0.4973                                     
-REMARK   3      L33:   0.8176 L12:  -0.2100                                     
-REMARK   3      L13:  -0.3314 L23:  -0.0513                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2225 S12:   0.3499 S13:  -0.3893                       
-REMARK   3      S21:   0.0737 S22:   0.0085 S23:  -0.0704                       
-REMARK   3      S31:  -0.3530 S32:  -0.5640 S33:   0.0006                       
-REMARK   3   TLS GROUP : 38                                                     
-REMARK   3    SELECTION: (chain B and resid 980:1022)                           
-REMARK   3    ORIGIN FOR THE GROUP (A):  17.5825  22.3868 -24.6426              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.6976 T22:   0.3780                                     
-REMARK   3      T33:   0.4845 T12:   0.1686                                     
-REMARK   3      T13:   0.2425 T23:   0.1310                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.4407 L22:   0.4479                                     
-REMARK   3      L33:   0.8418 L12:  -0.2028                                     
-REMARK   3      L13:  -0.4088 L23:   0.1065                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.3547 S12:   0.3608 S13:   0.1337                       
-REMARK   3      S21:  -0.4094 S22:   0.2847 S23:  -0.4408                       
-REMARK   3      S31:  -0.9098 S32:  -0.1921 S33:  -0.0000                       
-REMARK   3   TLS GROUP : 39                                                     
-REMARK   3    SELECTION: (chain B and resid 1023:1070)                          
-REMARK   3    ORIGIN FOR THE GROUP (A):  29.8989  12.8239 -13.9883              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5291 T22:   0.5865                                     
-REMARK   3      T33:   0.8652 T12:  -0.0146                                     
-REMARK   3      T13:   0.1946 T23:  -0.1952                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.9528 L22:   0.6465                                     
-REMARK   3      L33:   0.6781 L12:  -0.0748                                     
-REMARK   3      L13:  -0.0245 L23:   0.7566                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1152 S12:  -0.1523 S13:  -0.2954                       
-REMARK   3      S21:  -0.2124 S22:   0.5675 S23:  -1.0288                       
-REMARK   3      S31:  -0.1705 S32:   0.0672 S33:  -0.0005                       
-REMARK   3   TLS GROUP : 40                                                     
-REMARK   3    SELECTION: (chain B and resid 1071:1129)                          
-REMARK   3    ORIGIN FOR THE GROUP (A):  28.3861  13.5665 -36.1559              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.7980 T22:   0.4908                                     
-REMARK   3      T33:   0.4491 T12:  -0.1410                                     
-REMARK   3      T13:  -0.0747 T23:  -0.0044                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:  -0.3821 L22:   0.9083                                     
-REMARK   3      L33:   0.0563 L12:   0.8695                                     
-REMARK   3      L13:  -1.4066 L23:  -1.2048                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1692 S12:  -0.0060 S13:  -0.0647                       
-REMARK   3      S21:   0.3081 S22:   0.1350 S23:  -0.4420                       
-REMARK   3      S31:  -0.4348 S32:   0.0559 S33:  -0.0001                       
-REMARK   3   TLS GROUP : 41                                                     
-REMARK   3    SELECTION: (chain D and resid 3:7)                                
-REMARK   3    ORIGIN FOR THE GROUP (A): -12.7848  -4.2712  64.1627              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   2.9084 T22:   2.2814                                     
-REMARK   3      T33:   2.8805 T12:   0.8150                                     
-REMARK   3      T13:   0.1451 T23:   0.7545                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:  -0.0023 L22:   0.0315                                     
-REMARK   3      L33:   0.0039 L12:  -0.0072                                     
-REMARK   3      L13:  -0.0068 L23:  -0.0342                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.6261 S12:  -0.2985 S13:  -0.1348                       
-REMARK   3      S21:  -0.1939 S22:   0.5121 S23:  -0.3240                       
-REMARK   3      S31:  -0.0603 S32:   0.3378 S33:   0.0008                       
-REMARK   3   TLS GROUP : 42                                                     
-REMARK   3    SELECTION: (chain D and resid 8:11)                               
-REMARK   3    ORIGIN FOR THE GROUP (A): -12.2892  -4.7707  47.3067              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.6338 T22:   1.4064                                     
-REMARK   3      T33:   1.0510 T12:   0.5698                                     
-REMARK   3      T13:  -0.3250 T23:   0.2884                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0691 L22:   0.1372                                     
-REMARK   3      L33:   0.1056 L12:  -0.0832                                     
-REMARK   3      L13:  -0.0589 L23:  -0.0140                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.6529 S12:   0.0851 S13:  -0.1406                       
-REMARK   3      S21:  -0.0476 S22:  -0.1835 S23:  -1.5410                       
-REMARK   3      S31:   0.1346 S32:  -0.0421 S33:  -0.0005                       
-REMARK   3   TLS GROUP : 43                                                     
-REMARK   3    SELECTION: (chain D and resid 12:15)                              
-REMARK   3    ORIGIN FOR THE GROUP (A): -24.3047   3.8872  41.4489              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3718 T22:   0.6681                                     
-REMARK   3      T33:   0.6549 T12:  -0.1142                                     
-REMARK   3      T13:  -0.1971 T23:   0.1783                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0582 L22:   0.0833                                     
-REMARK   3      L33:   0.1413 L12:  -0.0821                                     
-REMARK   3      L13:   0.1028 L23:   0.0254                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.5248 S12:  -0.5505 S13:  -0.2833                       
-REMARK   3      S21:   0.7381 S22:  -0.8645 S23:  -0.5665                       
-REMARK   3      S31:   0.0698 S32:  -1.2046 S33:  -0.0002                       
-REMARK   3   TLS GROUP : 44                                                     
-REMARK   3    SELECTION: (chain D and resid 16:19)                              
-REMARK   3    ORIGIN FOR THE GROUP (A): -36.4099   6.5611  33.7929              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2636 T22:   1.0858                                     
-REMARK   3      T33:   0.9975 T12:  -0.1994                                     
-REMARK   3      T13:   0.1423 T23:   0.0894                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.2086 L22:   0.2244                                     
-REMARK   3      L33:   0.3988 L12:  -0.1730                                     
-REMARK   3      L13:   0.0604 L23:  -0.1706                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -1.2194 S12:  -0.4079 S13:  -0.1313                       
-REMARK   3      S21:  -0.0414 S22:   0.0001 S23:   1.5894                       
-REMARK   3      S31:  -0.3639 S32:  -0.3406 S33:  -0.0044                       
-REMARK   3   TLS GROUP : 45                                                     
-REMARK   3    SELECTION: (chain D and resid 20:23)                              
-REMARK   3    ORIGIN FOR THE GROUP (A): -49.1833   2.6030  42.1947              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.7868 T22:   1.5011                                     
-REMARK   3      T33:   1.0476 T12:  -0.1851                                     
-REMARK   3      T13:   0.3357 T23:   0.0802                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.1224 L22:   0.1516                                     
-REMARK   3      L33:   0.2086 L12:  -0.1720                                     
-REMARK   3      L13:   0.1804 L23:  -0.2312                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.6069 S12:  -0.2581 S13:  -0.6853                       
-REMARK   3      S21:   1.0498 S22:  -0.0741 S23:   0.1565                       
-REMARK   3      S31:  -0.3010 S32:  -0.4961 S33:  -0.0002                       
-REMARK   3   TLS GROUP : 46                                                     
-REMARK   3    SELECTION: (chain E and resid 26:31)                              
-REMARK   3    ORIGIN FOR THE GROUP (A): -48.2921   9.8392  39.2938              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.0744 T22:   1.7281                                     
-REMARK   3      T33:   1.4380 T12:  -0.0094                                     
-REMARK   3      T13:  -0.0393 T23:  -0.2056                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0936 L22:   0.0487                                     
-REMARK   3      L33:   0.2093 L12:   0.0673                                     
-REMARK   3      L13:  -0.0434 L23:   0.0814                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -1.1348 S12:   0.4740 S13:   1.2106                       
-REMARK   3      S21:  -0.0134 S22:  -1.1395 S23:   1.1162                       
-REMARK   3      S31:   0.2808 S32:  -0.7514 S33:  -0.0035                       
-REMARK   3   TLS GROUP : 47                                                     
-REMARK   3    SELECTION: (chain E and resid 32:36)                              
-REMARK   3    ORIGIN FOR THE GROUP (A): -31.1909  -0.3985  37.1947              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.9489 T22:   0.8954                                     
-REMARK   3      T33:   1.1643 T12:  -0.0626                                     
-REMARK   3      T13:   0.2674 T23:   0.0746                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0853 L22:   0.1370                                     
-REMARK   3      L33:  -0.0199 L12:  -0.2158                                     
-REMARK   3      L13:   0.0048 L23:  -0.0469                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0849 S12:  -0.1951 S13:  -0.4961                       
-REMARK   3      S21:   0.7944 S22:  -0.0327 S23:  -0.2174                       
-REMARK   3      S31:   1.0230 S32:  -0.6563 S33:   0.0000                       
-REMARK   3   TLS GROUP : 48                                                     
-REMARK   3    SELECTION: (chain E and resid 37:40)                              
-REMARK   3    ORIGIN FOR THE GROUP (A): -15.9917   3.7589  35.3763              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.6804 T22:   0.8696                                     
-REMARK   3      T33:   0.5065 T12:  -0.0583                                     
-REMARK   3      T13:  -0.1654 T23:  -0.0446                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.1332 L22:   0.1522                                     
-REMARK   3      L33:   0.1706 L12:   0.0035                                     
-REMARK   3      L13:  -0.1788 L23:  -0.1218                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1425 S12:  -0.7487 S13:   0.3980                       
-REMARK   3      S21:   0.3312 S22:  -0.1940 S23:   0.8536                       
-REMARK   3      S31:   0.2135 S32:   0.1205 S33:  -0.0007                       
-REMARK   3   TLS GROUP : 49                                                     
-REMARK   3    SELECTION: (chain E and resid 41:45)                              
-REMARK   3    ORIGIN FOR THE GROUP (A): -17.8054  -1.3872  51.7166              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   1.6517 T22:   1.1033                                     
-REMARK   3      T33:   1.1283 T12:   0.7949                                     
-REMARK   3      T13:   0.1664 T23:   0.5917                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.3276 L22:   0.0657                                     
-REMARK   3      L33:   0.2153 L12:  -0.1486                                     
-REMARK   3      L13:   0.0227 L23:   0.0803                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0455 S12:  -0.7836 S13:  -0.8334                       
-REMARK   3      S21:   2.1758 S22:   0.5139 S23:   1.4508                       
-REMARK   3      S31:   0.7821 S32:   1.5549 S33:  -0.0000                       
-REMARK   3   TLS GROUP : 50                                                     
-REMARK   3    SELECTION: (chain E and resid 46:50)                              
-REMARK   3    ORIGIN FOR THE GROUP (A):  -8.2858  -8.8003  62.2217              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   3.3801 T22:   2.3747                                     
-REMARK   3      T33:   1.3034 T12:   0.7335                                     
-REMARK   3      T13:  -0.6075 T23:   0.0916                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0651 L22:   0.0213                                     
-REMARK   3      L33:   0.0080 L12:  -0.0625                                     
-REMARK   3      L13:  -0.0339 L23:   0.0220                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.1575 S12:  -0.5106 S13:  -1.0301                       
-REMARK   3      S21:   0.0040 S22:  -0.1898 S23:   0.5492                       
-REMARK   3      S31:  -0.4263 S32:  -0.1747 S33:  -0.0003                       
-REMARK   3   TLS GROUP : 51                                                     
-REMARK   3    SELECTION: (chain G and resid 1)                                  
-REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1489   1.8711 -21.9724              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.9704 T22:   1.2521                                     
-REMARK   3      T33:   0.8729 T12:   0.2238                                     
-REMARK   3      T13:   0.1017 T23:   0.3495                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.0137 L22:   0.0370                                     
-REMARK   3      L33:   0.0478 L12:   0.0319                                     
-REMARK   3      L13:  -0.0232 L23:  -0.0406                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.1432 S12:  -0.5800 S13:   0.6976                       
-REMARK   3      S21:   0.3365 S22:   0.2798 S23:   0.3526                       
-REMARK   3      S31:   0.5289 S32:  -0.7287 S33:   0.0022                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 3THY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-11.                  
-REMARK 100 THE RCSB ID CODE IS RCSB067499.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-10                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 6.5-7.5                            
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : APS                                
-REMARK 200  BEAMLINE                       : 23-ID-B                            
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
-REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
-REMARK 200  OPTICS                         : MIRROR                             
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
-REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39892                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.894                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
-REMARK 200  DATA REDUNDANCY                : 1.900                              
-REMARK 200  R MERGE                    (I) : 0.04600                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.5                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.24800                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: CNS                                                   
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 46.14                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 20-25% PEG3350    
-REMARK 280  (W/V) AND 0.1M MES PH 6.5-7.5, VAPOR DIFFUSION, HANGING DROP,       
-REMARK 280  TEMPERATURE 277K                                                    
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 14550 ANGSTROM**2                         
-REMARK 350 SURFACE AREA OF THE COMPLEX: 78230 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL                       
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E                            
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     ALA A     2                                                      
-REMARK 465     VAL A     3                                                      
-REMARK 465     GLN A     4                                                      
-REMARK 465     PRO A     5                                                      
-REMARK 465     LYS A     6                                                      
-REMARK 465     GLU A     7                                                      
-REMARK 465     THR A     8                                                      
-REMARK 465     LEU A     9                                                      
-REMARK 465     GLN A    10                                                      
-REMARK 465     LEU A    11                                                      
-REMARK 465     GLU A    12                                                      
-REMARK 465     GLY A   108                                                      
-REMARK 465     ASN A   109                                                      
-REMARK 465     LYS A   110                                                      
-REMARK 465     ALA A   111                                                      
-REMARK 465     ALA A   143                                                      
-REMARK 465     VAL A   317                                                      
-REMARK 465     GLU A   318                                                      
-REMARK 465     ASP A   319                                                      
-REMARK 465     THR A   320                                                      
-REMARK 465     THR A   321                                                      
-REMARK 465     GLY A   322                                                      
-REMARK 465     ALA A   714                                                      
-REMARK 465     GLY A   715                                                      
-REMARK 465     ASP A   716                                                      
-REMARK 465     SER A   717                                                      
-REMARK 465     GLN A   718                                                      
-REMARK 465     LEU A   719                                                      
-REMARK 465     LYS A   720                                                      
-REMARK 465     GLY A   721                                                      
-REMARK 465     VAL A   722                                                      
-REMARK 465     ILE A   857                                                      
-REMARK 465     GLY A   858                                                      
-REMARK 465     GLU A   859                                                      
-REMARK 465     SER A   860                                                      
-REMARK 465     GLN A   861                                                      
-REMARK 465     GLY A   862                                                      
-REMARK 465     TYR A   863                                                      
-REMARK 465     ASP A   864                                                      
-REMARK 465     ILE A   865                                                      
-REMARK 465     MET A   866                                                      
-REMARK 465     GLU A   867                                                      
-REMARK 465     PRO A   868                                                      
-REMARK 465     ALA A   869                                                      
-REMARK 465     ALA A   870                                                      
-REMARK 465     LYS A   871                                                      
-REMARK 465     LYS A   931                                                      
-REMARK 465     VAL A   932                                                      
-REMARK 465     THR A   933                                                      
-REMARK 465     THR A   934                                                      
-REMARK 465     GLY B   208                                                      
-REMARK 465     PRO B   209                                                      
-REMARK 465     LYS B   210                                                      
-REMARK 465     SER B   211                                                      
-REMARK 465     ALA B   212                                                      
-REMARK 465     ASN B   213                                                      
-REMARK 465     LYS B   214                                                      
-REMARK 465     ARG B   215                                                      
-REMARK 465     SER B   216                                                      
-REMARK 465     ASP B   342                                                      
-REMARK 465     ASP B   343                                                      
-REMARK 465     GLU B   367                                                      
-REMARK 465     ASN B   368                                                      
-REMARK 465     VAL B   369                                                      
-REMARK 465     ARG B   370                                                      
-REMARK 465     ASP B   371                                                      
-REMARK 465     LYS B   372                                                      
-REMARK 465     LYS B   373                                                      
-REMARK 465     LYS B   374                                                      
-REMARK 465     GLY B   375                                                      
-REMARK 465     ASP B   470                                                      
-REMARK 465     THR B   471                                                      
-REMARK 465     VAL B   472                                                      
-REMARK 465     ASP B   473                                                      
-REMARK 465     ILE B   474                                                      
-REMARK 465     LYS B   475                                                      
-REMARK 465     GLY B   476                                                      
-REMARK 465     SER B   477                                                      
-REMARK 465     GLN B   478                                                      
-REMARK 465     ILE B   479                                                      
-REMARK 465     ILE B   480                                                      
-REMARK 465     SER B   481                                                      
-REMARK 465     ALA B   933                                                      
-REMARK 465     ASP B   934                                                      
-REMARK 465     ASN B   935                                                      
-REMARK 465     ILE B   936                                                      
-REMARK 465     TYR B   937                                                      
-REMARK 465     LYS B   938                                                      
-REMARK 465     GLY B   939                                                      
-REMARK 465     ARG B   940                                                      
-REMARK 465     GLU B  1027                                                      
-REMARK 465     ASP B  1028                                                      
-REMARK 465     GLU B  1029                                                      
-REMARK 465     SER B  1030                                                      
-REMARK 465     LYS B  1031                                                      
-REMARK 465     LEU B  1032                                                      
-REMARK 465     ASP B  1033                                                      
-REMARK 465     PRO B  1034                                                      
-REMARK 465     GLY B  1035                                                      
-REMARK 465     ALA B  1036                                                      
-REMARK 465     ALA B  1037                                                      
-REMARK 465     GLU B  1038                                                      
-REMARK 465     GLN B  1039                                                      
-REMARK 465     VAL B  1040                                                      
-REMARK 465     PRO B  1041                                                      
-REMARK 465     ASP B  1042                                                      
-REMARK 465     GLU B  1121                                                      
-REMARK 465     THR B  1122                                                      
-REMARK 465     GLN B  1123                                                      
-REMARK 465     THR B  1124                                                      
-REMARK 465     SER B  1125                                                      
-REMARK 465      DC D     1                                                      
-REMARK 465      DC D     2                                                      
-REMARK 465      DG D    24                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     ASP A 140    CG   OD1  OD2                                       
-REMARK 470     GLU A 205    CG   CD   OE1  OE2                                  
-REMARK 470     GLN A 264    CG   CD   OE1  NE2                                  
-REMARK 470     SER A 316    OG                                                  
-REMARK 470     SER A 323    OG                                                  
-REMARK 470     GLN A 397    CG   CD   OE1  NE2                                  
-REMARK 470     LEU A 431    CG   CD1  CD2                                       
-REMARK 470     LYS A 509    CG   CD   CE   NZ                                   
-REMARK 470     GLN A 510    CG   CD   OE1  NE2                                  
-REMARK 470     LYS A 512    CG   CD   CE   NZ                                   
-REMARK 470     GLN A 518    CG   CD   OE1  NE2                                  
-REMARK 470     ARG A 524    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     THR A 526    OG1  CG2                                            
-REMARK 470     CYS A 527    SG                                                  
-REMARK 470     ASP A 543    CG   OD1  OD2                                       
-REMARK 470     ILE A 544    CG1  CG2  CD1                                       
-REMARK 470     LYS A 546    CG   CD   CE   NZ                                   
-REMARK 470     ASP A 646    CG   OD1  OD2                                       
-REMARK 470     GLU A 749    CG   CD   OE1  OE2                                  
-REMARK 470     ASN A 835    CG   OD1  ND2                                       
-REMARK 470     LYS A 838    CG   CD   CE   NZ                                   
-REMARK 470     TYR A 856    CG   CD1  CD2  CE1  CE2  CZ   OH                    
-REMARK 470     LYS A 872    CG   CD   CE   NZ                                   
-REMARK 470     CYS A 873    SG                                                  
-REMARK 470     TYR A 874    CG   CD1  CD2  CE1  CE2  CZ   OH                    
-REMARK 470     LEU A 875    CG   CD1  CD2                                       
-REMARK 470     GLU A 878    CG   CD   OE1  OE2                                  
-REMARK 470     LYS A 882    CG   CD   CE   NZ                                   
-REMARK 470     GLN A 893    CG   CD   OE1  NE2                                  
-REMARK 470     GLU A 902    CG   CD   OE1  OE2                                  
-REMARK 470     SER A 921    OG                                                  
-REMARK 470     LYS B 217    CG   CD   CE   NZ                                   
-REMARK 470     GLU B 252    CG   CD   OE1  OE2                                  
-REMARK 470     LEU B 341    CG   CD1  CD2                                       
-REMARK 470     SER B 355    OG                                                  
-REMARK 470     LYS B 366    CG   CD   CE   NZ                                   
-REMARK 470     GLN B 440    CG   CD   OE1  NE2                                  
-REMARK 470     LYS B 469    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 522    CG   CD   CE   NZ                                   
-REMARK 470     MET B 523    CG   SD   CE                                        
-REMARK 470     LYS B 608    CG   CD   CE   NZ                                   
-REMARK 470     GLU B 613    CB   CG   CD   OE1  OE2                             
-REMARK 470     GLU B 668    CG   CD   OE1  OE2                                  
-REMARK 470     GLN B 683    CG   CD   OE1  NE2                                  
-REMARK 470     PHE B 700    CG   CD1  CD2  CE1  CE2  CZ                         
-REMARK 470     ASP B 878    CG   OD1  OD2                                       
-REMARK 470     SER B 941    OG                                                  
-REMARK 470     SER B1026    OG                                                  
-REMARK 470     PHE B1043    CG   CD1  CD2  CE1  CE2  CZ                         
-REMARK 470     GLN B1111    CG   CD   OE1  NE2                                  
-REMARK 470      DT D   3    P    OP1  OP2                                       
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500     DT E  26   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
-REMARK 500     DA E  28   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASN A  74     -145.55   -142.90                                   
-REMARK 500    LEU A  75       79.75     57.17                                   
-REMARK 500    VAL A  95      -81.87   -106.58                                   
-REMARK 500    MET A 141       72.60     53.12                                   
-REMARK 500    VAL A 155      -78.43    -64.25                                   
-REMARK 500    CYS A 176      117.93   -168.82                                   
-REMARK 500    GLU A 205     -178.17    -43.40                                   
-REMARK 500    LYS A 235      -80.02    -48.71                                   
-REMARK 500    ASN A 311       72.79     40.48                                   
-REMARK 500    THR A 375       -7.26    -59.36                                   
-REMARK 500    GLU A 378       -1.40   -153.48                                   
-REMARK 500    ASP A 379      -52.74   -120.85                                   
-REMARK 500    ARG A 382       11.46    -69.01                                   
-REMARK 500    ASP A 386       91.88    -67.39                                   
-REMARK 500    ARG A 396       25.58    -79.95                                   
-REMARK 500    GLN A 397       28.17     45.84                                   
-REMARK 500    ALA A 398       69.55   -116.27                                   
-REMARK 500    MET A 453      -70.39    -40.43                                   
-REMARK 500    ASN A 465       30.20    -78.62                                   
-REMARK 500    PHE A 474      -68.28   -105.72                                   
-REMARK 500    ASP A 506      133.82    -35.46                                   
-REMARK 500    LYS A 509      -76.89    -45.69                                   
-REMARK 500    GLN A 510      -66.36    -99.40                                   
-REMARK 500    ASN A 535      -70.85    -73.62                                   
-REMARK 500    ASN A 536       62.53     15.30                                   
-REMARK 500    VAL A 542      -78.75   -108.56                                   
-REMARK 500    ILE A 544      101.88   -166.39                                   
-REMARK 500    ASN A 553      151.12    -47.33                                   
-REMARK 500    SER A 612      -75.56    -54.21                                   
-REMARK 500    ALA A 636       78.56     46.89                                   
-REMARK 500    GLN A 645      -93.71    -58.14                                   
-REMARK 500    ILE A 648     -176.31    -65.33                                   
-REMARK 500    LYS A 661      -61.80   -103.55                                   
-REMARK 500    PRO A 696       79.18    -67.00                                   
-REMARK 500    GLU A 749       81.80     47.80                                   
-REMARK 500    THR A 772      -67.68   -100.71                                   
-REMARK 500    GLU A 809       29.88   -149.78                                   
-REMARK 500    GLN A 824     -148.35   -145.52                                   
-REMARK 500    ALA A 834       24.85    -77.81                                   
-REMARK 500    PHE A 854       98.54    -41.72                                   
-REMARK 500    GLN A 893       40.57   -105.54                                   
-REMARK 500    PRO A 895       48.62    -81.82                                   
-REMARK 500    GLU A 898       39.44   -151.20                                   
-REMARK 500    HIS B 234       62.09   -154.63                                   
-REMARK 500    HIS B 269      -98.00     61.03                                   
-REMARK 500    ALA B 308        5.05    -68.03                                   
-REMARK 500    ASP B 311      -79.36    -58.05                                   
-REMARK 500    SER B 314       63.63   -112.22                                   
-REMARK 500    SER B 315     -163.65   -164.23                                   
-REMARK 500    ASP B 348      129.53    -36.32                                   
-REMARK 500                                                                      
-REMARK 500 THIS ENTRY HAS      88 RAMACHANDRAN OUTLIERS.                        
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 935                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 3THW   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 3THX   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 3THZ   RELATED DB: PDB                                   
-DBREF  3THY A    1   934  UNP    P43246   MSH2_HUMAN       1    934             
-DBREF1 3THY B  210  1125  GB                   EAW95862                         
-DBREF2 3THY B     119616268                         210        1125             
-DBREF  3THY D    1    24  PDB    3THY     3THY             1     24             
-DBREF  3THY E   26    49  PDB    3THY     3THY             1     24             
-SEQADV 3THY GLY B  208  GB   119616268           EXPRESSION TAG                 
-SEQADV 3THY PRO B  209  GB   119616268           EXPRESSION TAG                 
-SEQRES   1 A  934  MET ALA VAL GLN PRO LYS GLU THR LEU GLN LEU GLU SER          
-SEQRES   2 A  934  ALA ALA GLU VAL GLY PHE VAL ARG PHE PHE GLN GLY MET          
-SEQRES   3 A  934  PRO GLU LYS PRO THR THR THR VAL ARG LEU PHE ASP ARG          
-SEQRES   4 A  934  GLY ASP PHE TYR THR ALA HIS GLY GLU ASP ALA LEU LEU          
-SEQRES   5 A  934  ALA ALA ARG GLU VAL PHE LYS THR GLN GLY VAL ILE LYS          
-SEQRES   6 A  934  TYR MET GLY PRO ALA GLY ALA LYS ASN LEU GLN SER VAL          
-SEQRES   7 A  934  VAL LEU SER LYS MET ASN PHE GLU SER PHE VAL LYS ASP          
-SEQRES   8 A  934  LEU LEU LEU VAL ARG GLN TYR ARG VAL GLU VAL TYR LYS          
-SEQRES   9 A  934  ASN ARG ALA GLY ASN LYS ALA SER LYS GLU ASN ASP TRP          
-SEQRES  10 A  934  TYR LEU ALA TYR LYS ALA SER PRO GLY ASN LEU SER GLN          
-SEQRES  11 A  934  PHE GLU ASP ILE LEU PHE GLY ASN ASN ASP MET SER ALA          
-SEQRES  12 A  934  SER ILE GLY VAL VAL GLY VAL LYS MET SER ALA VAL ASP          
-SEQRES  13 A  934  GLY GLN ARG GLN VAL GLY VAL GLY TYR VAL ASP SER ILE          
-SEQRES  14 A  934  GLN ARG LYS LEU GLY LEU CYS GLU PHE PRO ASP ASN ASP          
-SEQRES  15 A  934  GLN PHE SER ASN LEU GLU ALA LEU LEU ILE GLN ILE GLY          
-SEQRES  16 A  934  PRO LYS GLU CYS VAL LEU PRO GLY GLY GLU THR ALA GLY          
-SEQRES  17 A  934  ASP MET GLY LYS LEU ARG GLN ILE ILE GLN ARG GLY GLY          
-SEQRES  18 A  934  ILE LEU ILE THR GLU ARG LYS LYS ALA ASP PHE SER THR          
-SEQRES  19 A  934  LYS ASP ILE TYR GLN ASP LEU ASN ARG LEU LEU LYS GLY          
-SEQRES  20 A  934  LYS LYS GLY GLU GLN MET ASN SER ALA VAL LEU PRO GLU          
-SEQRES  21 A  934  MET GLU ASN GLN VAL ALA VAL SER SER LEU SER ALA VAL          
-SEQRES  22 A  934  ILE LYS PHE LEU GLU LEU LEU SER ASP ASP SER ASN PHE          
-SEQRES  23 A  934  GLY GLN PHE GLU LEU THR THR PHE ASP PHE SER GLN TYR          
-SEQRES  24 A  934  MET LYS LEU ASP ILE ALA ALA VAL ARG ALA LEU ASN LEU          
-SEQRES  25 A  934  PHE GLN GLY SER VAL GLU ASP THR THR GLY SER GLN SER          
-SEQRES  26 A  934  LEU ALA ALA LEU LEU ASN LYS CYS LYS THR PRO GLN GLY          
-SEQRES  27 A  934  GLN ARG LEU VAL ASN GLN TRP ILE LYS GLN PRO LEU MET          
-SEQRES  28 A  934  ASP LYS ASN ARG ILE GLU GLU ARG LEU ASN LEU VAL GLU          
-SEQRES  29 A  934  ALA PHE VAL GLU ASP ALA GLU LEU ARG GLN THR LEU GLN          
-SEQRES  30 A  934  GLU ASP LEU LEU ARG ARG PHE PRO ASP LEU ASN ARG LEU          
-SEQRES  31 A  934  ALA LYS LYS PHE GLN ARG GLN ALA ALA ASN LEU GLN ASP          
-SEQRES  32 A  934  CYS TYR ARG LEU TYR GLN GLY ILE ASN GLN LEU PRO ASN          
-SEQRES  33 A  934  VAL ILE GLN ALA LEU GLU LYS HIS GLU GLY LYS HIS GLN          
-SEQRES  34 A  934  LYS LEU LEU LEU ALA VAL PHE VAL THR PRO LEU THR ASP          
-SEQRES  35 A  934  LEU ARG SER ASP PHE SER LYS PHE GLN GLU MET ILE GLU          
-SEQRES  36 A  934  THR THR LEU ASP MET ASP GLN VAL GLU ASN HIS GLU PHE          
-SEQRES  37 A  934  LEU VAL LYS PRO SER PHE ASP PRO ASN LEU SER GLU LEU          
-SEQRES  38 A  934  ARG GLU ILE MET ASN ASP LEU GLU LYS LYS MET GLN SER          
-SEQRES  39 A  934  THR LEU ILE SER ALA ALA ARG ASP LEU GLY LEU ASP PRO          
-SEQRES  40 A  934  GLY LYS GLN ILE LYS LEU ASP SER SER ALA GLN PHE GLY          
-SEQRES  41 A  934  TYR TYR PHE ARG VAL THR CYS LYS GLU GLU LYS VAL LEU          
-SEQRES  42 A  934  ARG ASN ASN LYS ASN PHE SER THR VAL ASP ILE GLN LYS          
-SEQRES  43 A  934  ASN GLY VAL LYS PHE THR ASN SER LYS LEU THR SER LEU          
-SEQRES  44 A  934  ASN GLU GLU TYR THR LYS ASN LYS THR GLU TYR GLU GLU          
-SEQRES  45 A  934  ALA GLN ASP ALA ILE VAL LYS GLU ILE VAL ASN ILE SER          
-SEQRES  46 A  934  SER GLY TYR VAL GLU PRO MET GLN THR LEU ASN ASP VAL          
-SEQRES  47 A  934  LEU ALA GLN LEU ASP ALA VAL VAL SER PHE ALA HIS VAL          
-SEQRES  48 A  934  SER ASN GLY ALA PRO VAL PRO TYR VAL ARG PRO ALA ILE          
-SEQRES  49 A  934  LEU GLU LYS GLY GLN GLY ARG ILE ILE LEU LYS ALA SER          
-SEQRES  50 A  934  ARG HIS ALA CYS VAL GLU VAL GLN ASP GLU ILE ALA PHE          
-SEQRES  51 A  934  ILE PRO ASN ASP VAL TYR PHE GLU LYS ASP LYS GLN MET          
-SEQRES  52 A  934  PHE HIS ILE ILE THR GLY PRO ASN MET GLY GLY LYS SER          
-SEQRES  53 A  934  THR TYR ILE ARG GLN THR GLY VAL ILE VAL LEU MET ALA          
-SEQRES  54 A  934  GLN ILE GLY CYS PHE VAL PRO CYS GLU SER ALA GLU VAL          
-SEQRES  55 A  934  SER ILE VAL ASP CYS ILE LEU ALA ARG VAL GLY ALA GLY          
-SEQRES  56 A  934  ASP SER GLN LEU LYS GLY VAL SER THR PHE MET ALA GLU          
-SEQRES  57 A  934  MET LEU GLU THR ALA SER ILE LEU ARG SER ALA THR LYS          
-SEQRES  58 A  934  ASP SER LEU ILE ILE ILE ASP GLU LEU GLY ARG GLY THR          
-SEQRES  59 A  934  SER THR TYR ASP GLY PHE GLY LEU ALA TRP ALA ILE SER          
-SEQRES  60 A  934  GLU TYR ILE ALA THR LYS ILE GLY ALA PHE CYS MET PHE          
-SEQRES  61 A  934  ALA THR HIS PHE HIS GLU LEU THR ALA LEU ALA ASN GLN          
-SEQRES  62 A  934  ILE PRO THR VAL ASN ASN LEU HIS VAL THR ALA LEU THR          
-SEQRES  63 A  934  THR GLU GLU THR LEU THR MET LEU TYR GLN VAL LYS LYS          
-SEQRES  64 A  934  GLY VAL CYS ASP GLN SER PHE GLY ILE HIS VAL ALA GLU          
-SEQRES  65 A  934  LEU ALA ASN PHE PRO LYS HIS VAL ILE GLU CYS ALA LYS          
-SEQRES  66 A  934  GLN LYS ALA LEU GLU LEU GLU GLU PHE GLN TYR ILE GLY          
-SEQRES  67 A  934  GLU SER GLN GLY TYR ASP ILE MET GLU PRO ALA ALA LYS          
-SEQRES  68 A  934  LYS CYS TYR LEU GLU ARG GLU GLN GLY GLU LYS ILE ILE          
-SEQRES  69 A  934  GLN GLU PHE LEU SER LYS VAL LYS GLN MET PRO PHE THR          
-SEQRES  70 A  934  GLU MET SER GLU GLU ASN ILE THR ILE LYS LEU LYS GLN          
-SEQRES  71 A  934  LEU LYS ALA GLU VAL ILE ALA LYS ASN ASN SER PHE VAL          
-SEQRES  72 A  934  ASN GLU ILE ILE SER ARG ILE LYS VAL THR THR                  
-SEQRES   1 B  918  GLY PRO LYS SER ALA ASN LYS ARG SER LYS SER ILE TYR          
-SEQRES   2 B  918  THR PRO LEU GLU LEU GLN TYR ILE GLU MET LYS GLN GLN          
-SEQRES   3 B  918  HIS LYS ASP ALA VAL LEU CYS VAL GLU CYS GLY TYR LYS          
-SEQRES   4 B  918  TYR ARG PHE PHE GLY GLU ASP ALA GLU ILE ALA ALA ARG          
-SEQRES   5 B  918  GLU LEU ASN ILE TYR CYS HIS LEU ASP HIS ASN PHE MET          
-SEQRES   6 B  918  THR ALA SER ILE PRO THR HIS ARG LEU PHE VAL HIS VAL          
-SEQRES   7 B  918  ARG ARG LEU VAL ALA LYS GLY TYR LYS VAL GLY VAL VAL          
-SEQRES   8 B  918  LYS GLN THR GLU THR ALA ALA LEU LYS ALA ILE GLY ASP          
-SEQRES   9 B  918  ASN ARG SER SER LEU PHE SER ARG LYS LEU THR ALA LEU          
-SEQRES  10 B  918  TYR THR LYS SER THR LEU ILE GLY GLU ASP VAL ASN PRO          
-SEQRES  11 B  918  LEU ILE LYS LEU ASP ASP ALA VAL ASN VAL ASP GLU ILE          
-SEQRES  12 B  918  MET THR ASP THR SER THR SER TYR LEU LEU CYS ILE SER          
-SEQRES  13 B  918  GLU ASN LYS GLU ASN VAL ARG ASP LYS LYS LYS GLY ASN          
-SEQRES  14 B  918  ILE PHE ILE GLY ILE VAL GLY VAL GLN PRO ALA THR GLY          
-SEQRES  15 B  918  GLU VAL VAL PHE ASP SER PHE GLN ASP SER ALA SER ARG          
-SEQRES  16 B  918  SER GLU LEU GLU THR ARG MET SER SER LEU GLN PRO VAL          
-SEQRES  17 B  918  GLU LEU LEU LEU PRO SER ALA LEU SER GLU GLN THR GLU          
-SEQRES  18 B  918  ALA LEU ILE HIS ARG ALA THR SER VAL SER VAL GLN ASP          
-SEQRES  19 B  918  ASP ARG ILE ARG VAL GLU ARG MET ASP ASN ILE TYR PHE          
-SEQRES  20 B  918  GLU TYR SER HIS ALA PHE GLN ALA VAL THR GLU PHE TYR          
-SEQRES  21 B  918  ALA LYS ASP THR VAL ASP ILE LYS GLY SER GLN ILE ILE          
-SEQRES  22 B  918  SER GLY ILE VAL ASN LEU GLU LYS PRO VAL ILE CYS SER          
-SEQRES  23 B  918  LEU ALA ALA ILE ILE LYS TYR LEU LYS GLU PHE ASN LEU          
-SEQRES  24 B  918  GLU LYS MET LEU SER LYS PRO GLU ASN PHE LYS GLN LEU          
-SEQRES  25 B  918  SER SER LYS MET GLU PHE MET THR ILE ASN GLY THR THR          
-SEQRES  26 B  918  LEU ARG ASN LEU GLU ILE LEU GLN ASN GLN THR ASP MET          
-SEQRES  27 B  918  LYS THR LYS GLY SER LEU LEU TRP VAL LEU ASP HIS THR          
-SEQRES  28 B  918  LYS THR SER PHE GLY ARG ARG LYS LEU LYS LYS TRP VAL          
-SEQRES  29 B  918  THR GLN PRO LEU LEU LYS LEU ARG GLU ILE ASN ALA ARG          
-SEQRES  30 B  918  LEU ASP ALA VAL SER GLU VAL LEU HIS SER GLU SER SER          
-SEQRES  31 B  918  VAL PHE GLY GLN ILE GLU ASN HIS LEU ARG LYS LEU PRO          
-SEQRES  32 B  918  ASP ILE GLU ARG GLY LEU CYS SER ILE TYR HIS LYS LYS          
-SEQRES  33 B  918  CYS SER THR GLN GLU PHE PHE LEU ILE VAL LYS THR LEU          
-SEQRES  34 B  918  TYR HIS LEU LYS SER GLU PHE GLN ALA ILE ILE PRO ALA          
-SEQRES  35 B  918  VAL ASN SER HIS ILE GLN SER ASP LEU LEU ARG THR VAL          
-SEQRES  36 B  918  ILE LEU GLU ILE PRO GLU LEU LEU SER PRO VAL GLU HIS          
-SEQRES  37 B  918  TYR LEU LYS ILE LEU ASN GLU GLN ALA ALA LYS VAL GLY          
-SEQRES  38 B  918  ASP LYS THR GLU LEU PHE LYS ASP LEU SER ASP PHE PRO          
-SEQRES  39 B  918  LEU ILE LYS LYS ARG LYS ASP GLU ILE GLN GLY VAL ILE          
-SEQRES  40 B  918  ASP GLU ILE ARG MET HIS LEU GLN GLU ILE ARG LYS ILE          
-SEQRES  41 B  918  LEU LYS ASN PRO SER ALA GLN TYR VAL THR VAL SER GLY          
-SEQRES  42 B  918  GLN GLU PHE MET ILE GLU ILE LYS ASN SER ALA VAL SER          
-SEQRES  43 B  918  CYS ILE PRO THR ASP TRP VAL LYS VAL GLY SER THR LYS          
-SEQRES  44 B  918  ALA VAL SER ARG PHE HIS SER PRO PHE ILE VAL GLU ASN          
-SEQRES  45 B  918  TYR ARG HIS LEU ASN GLN LEU ARG GLU GLN LEU VAL LEU          
-SEQRES  46 B  918  ASP CYS SER ALA GLU TRP LEU ASP PHE LEU GLU LYS PHE          
-SEQRES  47 B  918  SER GLU HIS TYR HIS SER LEU CYS LYS ALA VAL HIS HIS          
-SEQRES  48 B  918  LEU ALA THR VAL ASP CYS ILE PHE SER LEU ALA LYS VAL          
-SEQRES  49 B  918  ALA LYS GLN GLY ASP TYR CYS ARG PRO THR VAL GLN GLU          
-SEQRES  50 B  918  GLU ARG LYS ILE VAL ILE LYS ASN GLY ARG HIS PRO VAL          
-SEQRES  51 B  918  ILE ASP VAL LEU LEU GLY GLU GLN ASP GLN TYR VAL PRO          
-SEQRES  52 B  918  ASN ASN THR ASP LEU SER GLU ASP SER GLU ARG VAL MET          
-SEQRES  53 B  918  ILE ILE THR GLY PRO ASN MET GLY GLY LYS SER SER TYR          
-SEQRES  54 B  918  ILE LYS GLN VAL ALA LEU ILE THR ILE MET ALA GLN ILE          
-SEQRES  55 B  918  GLY SER TYR VAL PRO ALA GLU GLU ALA THR ILE GLY ILE          
-SEQRES  56 B  918  VAL ASP GLY ILE PHE THR ARG MET GLY ALA ALA ASP ASN          
-SEQRES  57 B  918  ILE TYR LYS GLY ARG SER THR PHE MET GLU GLU LEU THR          
-SEQRES  58 B  918  ASP THR ALA GLU ILE ILE ARG LYS ALA THR SER GLN SER          
-SEQRES  59 B  918  LEU VAL ILE LEU ASP GLU LEU GLY ARG GLY THR SER THR          
-SEQRES  60 B  918  HIS ASP GLY ILE ALA ILE ALA TYR ALA THR LEU GLU TYR          
-SEQRES  61 B  918  PHE ILE ARG ASP VAL LYS SER LEU THR LEU PHE VAL THR          
-SEQRES  62 B  918  HIS TYR PRO PRO VAL CYS GLU LEU GLU LYS ASN TYR SER          
-SEQRES  63 B  918  HIS GLN VAL GLY ASN TYR HIS MET GLY PHE LEU VAL SER          
-SEQRES  64 B  918  GLU ASP GLU SER LYS LEU ASP PRO GLY ALA ALA GLU GLN          
-SEQRES  65 B  918  VAL PRO ASP PHE VAL THR PHE LEU TYR GLN ILE THR ARG          
-SEQRES  66 B  918  GLY ILE ALA ALA ARG SER TYR GLY LEU ASN VAL ALA LYS          
-SEQRES  67 B  918  LEU ALA ASP VAL PRO GLY GLU ILE LEU LYS LYS ALA ALA          
-SEQRES  68 B  918  HIS LYS SER LYS GLU LEU GLU GLY LEU ILE ASN THR LYS          
-SEQRES  69 B  918  ARG LYS ARG LEU LYS TYR PHE ALA LYS LEU TRP THR MET          
-SEQRES  70 B  918  HIS ASN ALA GLN ASP LEU GLN LYS TRP THR GLU GLU PHE          
-SEQRES  71 B  918  ASN MET GLU GLU THR GLN THR SER                              
-SEQRES   1 D   24   DC  DC  DT  DC  DT  DA  DT  DC  DT  DG  DA  DA  DG          
-SEQRES   2 D   24   DC  DC  DG  DA  DT  DC  DG  DA  DT  DG  DG                  
-SEQRES   1 E   24   DT  DC  DA  DT  DC  DG  DA  DT  DC  DG  DC  DA  DG          
-SEQRES   2 E   24   DC  DT  DT  DC  DA  DG  DA  DT  DA  DG  DG                  
-HET    ADP  A 935      27                                                       
-HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
-FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
-FORMUL   6  HOH   *15(H2 O)                                                     
-HELIX    1   1 ALA A   14  MET A   26  1                                  13    
-HELIX    2   2 GLY A   47  VAL A   57  1                                  11    
-HELIX    3   3 PRO A   69  LYS A   73  5                                   5    
-HELIX    4   4 LYS A   82  VAL A   95  1                                  14    
-HELIX    5   5 PHE A  131  PHE A  136  1                                   6    
-HELIX    6   6 PHE A  184  GLY A  195  1                                  12    
-HELIX    7   7 ALA A  207  GLY A  221  1                                  15    
-HELIX    8   8 LYS A  228  SER A  233  5                                   6    
-HELIX    9   9 ASP A  236  LEU A  245  1                                  10    
-HELIX   10  10 LEU A  258  GLU A  262  5                                   5    
-HELIX   11  11 ASN A  263  GLU A  278  1                                  16    
-HELIX   12  12 LEU A  279  PHE A  286  5                                   8    
-HELIX   13  13 ASP A  295  TYR A  299  5                                   5    
-HELIX   14  14 ASP A  303  LEU A  310  1                                   8    
-HELIX   15  15 LEU A  326  ASN A  331  1                                   6    
-HELIX   16  16 THR A  335  GLN A  348  1                                  14    
-HELIX   17  17 ASP A  352  GLU A  368  1                                  17    
-HELIX   18  18 ASP A  369  GLU A  378  1                                  10    
-HELIX   19  19 LEU A  380  PHE A  384  5                                   5    
-HELIX   20  20 ASP A  386  PHE A  394  1                                   9    
-HELIX   21  21 ASN A  400  ASN A  412  1                                  13    
-HELIX   22  22 GLN A  413  GLU A  425  1                                  13    
-HELIX   23  23 GLN A  429  LEU A  458  1                                  30    
-HELIX   24  24 ASP A  475  MET A  492  1                                  18    
-HELIX   25  25 GLN A  493  LEU A  503  1                                  11    
-HELIX   26  26 THR A  526  LYS A  531  1                                   6    
-HELIX   27  27 VAL A  532  ASN A  535  5                                   4    
-HELIX   28  28 ASN A  553  THR A  564  1                                  12    
-HELIX   29  29 LYS A  567  SER A  586  1                                  20    
-HELIX   30  30 TYR A  588  GLY A  614  1                                  27    
-HELIX   31  31 GLY A  674  ILE A  691  1                                  18    
-HELIX   32  32 THR A  724  ALA A  739  1                                  16    
-HELIX   33  33 SER A  755  LYS A  773  1                                  19    
-HELIX   34  34 PHE A  784  THR A  788  5                                   5    
-HELIX   35  35 ALA A  789  ILE A  794  1                                   6    
-HELIX   36  36 PHE A  826  ALA A  834  1                                   9    
-HELIX   37  37 PRO A  837  LEU A  851  1                                  15    
-HELIX   38  38 TYR A  874  GLN A  893  1                                  20    
-HELIX   39  39 SER A  900  ALA A  917  1                                  18    
-HELIX   40  40 ASN A  920  ARG A  929  1                                  10    
-HELIX   41  41 THR B  221  GLN B  233  1                                  13    
-HELIX   42  42 GLY B  251  LEU B  261  1                                  11    
-HELIX   43  43 ARG B  280  LYS B  291  1                                  12    
-HELIX   44  44 THR B  303  ALA B  308  1                                   6    
-HELIX   45  45 GLU B  404  GLN B  413  1                                  10    
-HELIX   46  46 SER B  424  SER B  438  1                                  15    
-HELIX   47  47 ASP B  450  PHE B  454  5                                   5    
-HELIX   48  48 GLU B  455  TYR B  467  1                                  13    
-HELIX   49  49 GLU B  487  PHE B  504  1                                  18    
-HELIX   50  50 ASN B  505  LEU B  510  5                                   6    
-HELIX   51  51 LYS B  512  GLU B  514  5                                   3    
-HELIX   52  52 ASN B  529  LEU B  536  1                                   8    
-HELIX   53  53 SER B  550  ASP B  556  1                                   7    
-HELIX   54  54 THR B  560  GLN B  573  1                                  14    
-HELIX   55  55 LYS B  577  SER B  594  1                                  18    
-HELIX   56  56 SER B  597  ARG B  607  1                                  11    
-HELIX   57  57 ASP B  611  HIS B  621  1                                  11    
-HELIX   58  58 SER B  625  ILE B  654  1                                  30    
-HELIX   59  59 SER B  656  LEU B  664  1                                   9    
-HELIX   60  60 LEU B  664  LEU B  670  1                                   7    
-HELIX   61  61 PRO B  672  ILE B  679  1                                   8    
-HELIX   62  62 ASN B  681  LYS B  686  1                                   6    
-HELIX   63  63 ASP B  696  ASP B  699  5                                   4    
-HELIX   64  64 PHE B  700  HIS B  720  1                                  21    
-HELIX   65  65 HIS B  720  LYS B  729  1                                  10    
-HELIX   66  66 ALA B  751  ILE B  755  5                                   5    
-HELIX   67  67 SER B  773  GLU B  807  1                                  35    
-HELIX   68  68 HIS B  808  ALA B  832  1                                  25    
-HELIX   69  69 HIS B  855  LEU B  862  1                                   8    
-HELIX   70  70 MET B  890  ILE B  909  1                                  20    
-HELIX   71  71 THR B  942  ALA B  957  1                                  16    
-HELIX   72  72 SER B  973  ASP B  991  1                                  19    
-HELIX   73  73 TYR B 1002  GLU B 1007  1                                   6    
-HELIX   74  74 GLU B 1007  TYR B 1012  1                                   6    
-HELIX   75  75 GLY B 1060  LYS B 1065  1                                   6    
-HELIX   76  76 PRO B 1070  THR B 1103  1                                  34    
-HELIX   77  77 ASN B 1106  GLU B 1120  1                                  15    
-SHEET    1   A 6 LYS A  65  MET A  67  0                                        
-SHEET    2   A 6 ASN A  74  SER A  81 -1  O  SER A  77   N  LYS A  65           
-SHEET    3   A 6 PHE A  42  HIS A  46 -1  N  TYR A  43   O  LEU A  80           
-SHEET    4   A 6 THR A  33  ASP A  38 -1  N  PHE A  37   O  THR A  44           
-SHEET    5   A 6 ARG A  99  ASN A 105  1  O  TYR A 103   N  ASP A  38           
-SHEET    6   A 6 TRP A 117  ALA A 123 -1  O  ALA A 123   N  VAL A 100           
-SHEET    1   B 4 VAL A 148  MET A 152  0                                        
-SHEET    2   B 4 GLN A 160  ASP A 167 -1  O  GLY A 164   N  GLY A 149           
-SHEET    3   B 4 LYS A 172  PRO A 179 -1  O  PHE A 178   N  VAL A 161           
-SHEET    4   B 4 GLU A 290  THR A 293  1  O  THR A 292   N  LEU A 173           
-SHEET    1   C 2 GLU A 198  PRO A 202  0                                        
-SHEET    2   C 2 LEU A 223  ARG A 227  1  O  THR A 225   N  LEU A 201           
-SHEET    1   D 7 LYS A 301  LEU A 302  0                                        
-SHEET    2   D 7 CYS A 707  ARG A 711  1  O  ILE A 708   N  LYS A 301           
-SHEET    3   D 7 LEU A 744  ASP A 748  1  O  LEU A 744   N  CYS A 707           
-SHEET    4   D 7 PHE A 777  ALA A 781  1  O  MET A 779   N  ILE A 747           
-SHEET    5   D 7 PHE A 664  THR A 668  1  N  ILE A 667   O  PHE A 780           
-SHEET    6   D 7 ASN A 799  THR A 807  1  O  LEU A 800   N  ILE A 666           
-SHEET    7   D 7 THR A 810  LYS A 819 -1  O  THR A 810   N  THR A 807           
-SHEET    1   E 2 LYS A 512  SER A 516  0                                        
-SHEET    2   E 2 GLY A 520  ARG A 524 -1  O  TYR A 522   N  ASP A 514           
-SHEET    1   F 2 SER A 540  ILE A 544  0                                        
-SHEET    2   F 2 VAL A 549  THR A 552 -1  O  THR A 552   N  SER A 540           
-SHEET    1   G 4 ALA A 623  LEU A 625  0                                        
-SHEET    2   G 4 SER A 699  SER A 703  1  O  ALA A 700   N  ALA A 623           
-SHEET    3   G 4 ILE A 632  SER A 637 -1  N  ILE A 633   O  GLU A 701           
-SHEET    4   G 4 ASN A 653  PHE A 657 -1  O  VAL A 655   N  LEU A 634           
-SHEET    1   H 6 HIS B 266  ASP B 268  0                                        
-SHEET    2   H 6 PHE B 271  PRO B 277 -1  O  PHE B 271   N  ASP B 268           
-SHEET    3   H 6 LYS B 246  PHE B 250 -1  N  TYR B 247   O  ILE B 276           
-SHEET    4   H 6 VAL B 238  CYS B 243 -1  N  VAL B 241   O  ARG B 248           
-SHEET    5   H 6 VAL B 295  GLN B 300  1  O  GLY B 296   N  VAL B 238           
-SHEET    6   H 6 ARG B 319  TYR B 325 -1  O  TYR B 325   N  VAL B 295           
-SHEET    1   I 6 ARG B 445  MET B 449  0                                        
-SHEET    2   I 6 GLU B 416  PRO B 420  1  N  LEU B 417   O  GLU B 447           
-SHEET    3   I 6 LEU B 359  ASN B 365  1  N  LEU B 360   O  GLU B 416           
-SHEET    4   I 6 PHE B 378  VAL B 384 -1  O  VAL B 382   N  CYS B 361           
-SHEET    5   I 6 VAL B 391  GLN B 397 -1  O  VAL B 392   N  GLY B 383           
-SHEET    6   I 6 PHE B 516  GLN B 518  1  O  LYS B 517   N  PHE B 393           
-SHEET    1   J 7 THR B 527  ILE B 528  0                                        
-SHEET    2   J 7 GLY B 925  ARG B 929  1  O  ILE B 926   N  THR B 527           
-SHEET    3   J 7 LEU B 962  ASP B 966  1  O  ILE B 964   N  PHE B 927           
-SHEET    4   J 7 LEU B 995  VAL B 999  1  O  VAL B 999   N  LEU B 965           
-SHEET    5   J 7 VAL B 882  THR B 886  1  N  ILE B 885   O  PHE B 998           
-SHEET    6   J 7 VAL B1016  VAL B1025  1  O  TYR B1019   N  ILE B 884           
-SHEET    7   J 7 THR B1045  ARG B1052 -1  O  THR B1051   N  HIS B1020           
-SHEET    1   K 4 TYR B 735  VAL B 738  0                                        
-SHEET    2   K 4 GLN B 741  LYS B 748 -1  O  GLN B 741   N  VAL B 738           
-SHEET    3   K 4 VAL B 768  HIS B 772 -1  O  SER B 769   N  ILE B 747           
-SHEET    4   K 4 VAL B 760  SER B 764 -1  N  VAL B 760   O  HIS B 772           
-SHEET    1   L 4 THR B 841  GLN B 843  0                                        
-SHEET    2   L 4 GLU B 917  GLY B 921  1  O  ILE B 920   N  THR B 841           
-SHEET    3   L 4 LYS B 847  GLY B 853 -1  N  LYS B 847   O  GLY B 921           
-SHEET    4   L 4 ASN B 871  LEU B 875 -1  O  THR B 873   N  ILE B 850           
-SITE     1 AC1 15 ILE A 648  ALA A 649  PHE A 650  ILE A 651                    
-SITE     2 AC1 15 ASN A 653  PRO A 670  ASN A 671  MET A 672                    
-SITE     3 AC1 15 GLY A 673  GLY A 674  LYS A 675  SER A 676                    
-SITE     4 AC1 15 THR A 677  TYR A 815  HOH A 937                               
-CRYST1   66.270   91.106   95.628  67.82  86.98  73.35 P 1           1          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.015090 -0.004513  0.000987        0.00000                         
-SCALE2      0.000000  0.011457 -0.004689        0.00000                         
-SCALE3      0.000000  0.000000  0.011315        0.00000                         
-ATOM      1  N   SER A  13      -1.722   1.204  47.335  1.00125.29           N  
-ANISOU    1  N   SER A  13    17194  17892  12518   1711  -2442  -1627       N  
-ATOM      2  CA  SER A  13      -0.944   1.295  46.106  1.00122.92           C  
-ANISOU    2  CA  SER A  13    16773  17245  12685   1562  -2540  -1635       C  
-ATOM      3  C   SER A  13       0.443   0.686  46.287  1.00120.86           C  
-ANISOU    3  C   SER A  13    16615  16696  12610   1492  -2764  -1557       C  
-ATOM      4  O   SER A  13       1.384   1.040  45.577  1.00118.95           O  
-ANISOU    4  O   SER A  13    16308  16146  12740   1452  -2929  -1621       O  
-ATOM      5  CB  SER A  13      -0.827   2.753  45.654  1.00119.52           C  
-ANISOU    5  CB  SER A  13    16272  16693  12446   1712  -2692  -1901       C  
-ATOM      6  OG  SER A  13      -0.157   3.536  46.626  1.00117.66           O  
-ANISOU    6  OG  SER A  13    16195  16391  12120   1945  -2986  -2100       O  
-ATOM      7  N   ALA A  14       0.563  -0.226  47.247  1.00151.97           N  
-ANISOU    7  N   ALA A  14    20709  20738  16294   1480  -2769  -1408       N  
-ATOM      8  CA  ALA A  14       1.826  -0.910  47.499  1.00148.26           C  
-ANISOU    8  CA  ALA A  14    20343  20005  15984   1415  -2987  -1321       C  
-ATOM      9  C   ALA A  14       2.235  -1.703  46.268  1.00143.78           C  
-ANISOU    9  C   ALA A  14    19626  19209  15794   1168  -2906  -1168       C  
-ATOM     10  O   ALA A  14       3.421  -1.846  45.973  1.00141.69           O  
-ANISOU   10  O   ALA A  14    19357  18642  15837   1125  -3099  -1174       O  
-ATOM     11  CB  ALA A  14       1.708  -1.823  48.710  1.00148.51           C  
-ANISOU   11  CB  ALA A  14    20568  20215  15643   1431  -2978  -1158       C  
-ATOM     12  N   ALA A  15       1.239  -2.218  45.556  1.00110.03           N  
-ANISOU   12  N   ALA A  15    15225  15083  11497   1016  -2623  -1035       N  
-ATOM     13  CA  ALA A  15       1.474  -2.909  44.296  1.00105.51           C  
-ANISOU   13  CA  ALA A  15    14516  14317  11256    804  -2533   -915       C  
-ATOM     14  C   ALA A  15       1.664  -1.893  43.173  1.00101.22           C  
-ANISOU   14  C   ALA A  15    13825  13618  11016    829  -2548  -1079       C  
-ATOM     15  O   ALA A  15       2.449  -2.111  42.253  1.00100.68           O  
-ANISOU   15  O   ALA A  15    13678  13295  11280    731  -2590  -1053       O  
-ATOM     16  CB  ALA A  15       0.321  -3.847  43.981  1.00106.37           C  
-ANISOU   16  CB  ALA A  15    14556  14627  11233    638  -2262   -713       C  
-ATOM     17  N   GLU A  16       0.943  -0.777  43.262  1.00107.43           N  
-ANISOU   17  N   GLU A  16    14576  14562  11681    968  -2514  -1245       N  
-ATOM     18  CA  GLU A  16       1.077   0.307  42.293  1.00102.03           C  
-ANISOU   18  CA  GLU A  16    13766  13737  11265   1005  -2551  -1401       C  
-ATOM     19  C   GLU A  16       2.491   0.871  42.271  1.00 98.82           C  
-ANISOU   19  C   GLU A  16    13376  13021  11151   1071  -2826  -1502       C  
-ATOM     20  O   GLU A  16       2.788   1.787  41.506  1.00 96.77           O  
-ANISOU   20  O   GLU A  16    13011  12606  11150   1097  -2888  -1609       O  
-ATOM     21  CB  GLU A  16       0.083   1.436  42.585  1.00103.49           C  
-ANISOU   21  CB  GLU A  16    13929  14141  11253   1172  -2511  -1578       C  
-ATOM     22  CG  GLU A  16      -1.304   1.232  41.997  1.00102.83           C  
-ANISOU   22  CG  GLU A  16    13729  14285  11057   1087  -2231  -1511       C  
-ATOM     23  CD  GLU A  16      -2.101   2.528  41.915  1.00103.27           C  
-ANISOU   23  CD  GLU A  16    13718  14469  11051   1246  -2222  -1717       C  
-ATOM     24  OE1 GLU A  16      -1.824   3.453  42.714  1.00103.80           O  
-ANISOU   24  OE1 GLU A  16    13869  14546  11023   1455  -2409  -1906       O  
-ATOM     25  OE2 GLU A  16      -2.996   2.624  41.044  1.00102.25           O  
-ANISOU   25  OE2 GLU A  16    13457  14416  10978   1170  -2050  -1699       O  
-ATOM     26  N   VAL A  17       3.357   0.334  43.122  1.00101.49           N  
-ANISOU   26  N   VAL A  17    13839  13263  11459   1095  -3000  -1456       N  
-ATOM     27  CA  VAL A  17       4.754   0.742  43.137  1.00 97.62           C  
-ANISOU   27  CA  VAL A  17    13348  12461  11282   1144  -3274  -1530       C  
-ATOM     28  C   VAL A  17       5.636  -0.462  42.842  1.00 94.00           C  
-ANISOU   28  C   VAL A  17    12881  11815  11020    990  -3282  -1355       C  
-ATOM     29  O   VAL A  17       6.671  -0.343  42.187  1.00 94.55           O  
-ANISOU   29  O   VAL A  17    12851  11614  11460    948  -3381  -1355       O  
-ATOM     30  CB  VAL A  17       5.160   1.362  44.488  1.00100.55           C  
-ANISOU   30  CB  VAL A  17    13884  12835  11486   1354  -3560  -1681       C  
-ATOM     31  CG1 VAL A  17       6.569   1.932  44.403  1.00 99.54           C  
-ANISOU   31  CG1 VAL A  17    13717  12357  11746   1401  -3866  -1767       C  
-ATOM     32  CG2 VAL A  17       4.174   2.447  44.895  1.00101.09           C  
-ANISOU   32  CG2 VAL A  17    13982  13128  11300   1532  -3542  -1865       C  
-ATOM     33  N   GLY A  18       5.216  -1.625  43.325  1.00 75.22           N  
-ANISOU   33  N   GLY A  18    10598   9580   8401    908  -3175  -1197       N  
-ATOM     34  CA  GLY A  18       5.935  -2.853  43.052  1.00 71.99           C  
-ANISOU   34  CA  GLY A  18    10188   9004   8162    763  -3183  -1031       C  
-ATOM     35  C   GLY A  18       6.012  -3.117  41.564  1.00 67.12           C  
-ANISOU   35  C   GLY A  18     9399   8261   7843    623  -3014   -973       C  
-ATOM     36  O   GLY A  18       6.973  -3.711  41.072  1.00 66.70           O  
-ANISOU   36  O   GLY A  18     9297   7980   8067    551  -3070   -908       O  
-ATOM     37  N   PHE A  19       4.988  -2.666  40.846  1.00 91.45           N  
-ANISOU   37  N   PHE A  19    12394  11495  10858    599  -2812  -1003       N  
-ATOM     38  CA  PHE A  19       4.919  -2.833  39.401  1.00 84.91           C  
-ANISOU   38  CA  PHE A  19    11424  10575  10263    486  -2645   -961       C  
-ATOM     39  C   PHE A  19       5.898  -1.903  38.705  1.00 83.97           C  
-ANISOU   39  C   PHE A  19    11194  10225  10486    540  -2746  -1061       C  
-ATOM     40  O   PHE A  19       6.651  -2.319  37.820  1.00 80.10           O  
-ANISOU   40  O   PHE A  19    10618   9546  10269    467  -2712  -1000       O  
-ATOM     41  CB  PHE A  19       3.504  -2.547  38.903  1.00 80.39           C  
-ANISOU   41  CB  PHE A  19    10801  10231   9514    457  -2429   -972       C  
-ATOM     42  CG  PHE A  19       3.357  -2.646  37.416  1.00 74.36           C  
-ANISOU   42  CG  PHE A  19     9917   9380   8955    359  -2275   -941       C  
-ATOM     43  CD1 PHE A  19       2.988  -3.839  36.825  1.00 72.65           C  
-ANISOU   43  CD1 PHE A  19     9696   9171   8736    219  -2139   -802       C  
-ATOM     44  CD2 PHE A  19       3.594  -1.548  36.608  1.00 72.54           C  
-ANISOU   44  CD2 PHE A  19     9589   9052   8920    413  -2281  -1050       C  
-ATOM     45  CE1 PHE A  19       2.856  -3.936  35.454  1.00 72.48           C  
-ANISOU   45  CE1 PHE A  19     9591   9070   8879    151  -2012   -789       C  
-ATOM     46  CE2 PHE A  19       3.463  -1.638  35.237  1.00 71.34           C  
-ANISOU   46  CE2 PHE A  19     9349   8831   8925    336  -2137  -1015       C  
-ATOM     47  CZ  PHE A  19       3.093  -2.833  34.659  1.00 71.61           C  
-ANISOU   47  CZ  PHE A  19     9396   8882   8932    213  -2002   -894       C  
-ATOM     48  N   VAL A  20       5.876  -0.639  39.111  1.00 75.44           N  
-ANISOU   48  N   VAL A  20    10109   9161   9394    673  -2872  -1212       N  
-ATOM     49  CA  VAL A  20       6.750   0.362  38.521  1.00 75.92           C  
-ANISOU   49  CA  VAL A  20    10053   9001   9792    721  -2987  -1294       C  
-ATOM     50  C   VAL A  20       8.205  -0.062  38.629  1.00 79.37           C  
-ANISOU   50  C   VAL A  20    10462   9174  10520    706  -3152  -1243       C  
-ATOM     51  O   VAL A  20       8.996   0.161  37.714  1.00 79.79           O  
-ANISOU   51  O   VAL A  20    10374   9033  10908    669  -3136  -1213       O  
-ATOM     52  CB  VAL A  20       6.567   1.723  39.195  1.00 76.01           C  
-ANISOU   52  CB  VAL A  20    10092   9046   9743    882  -3168  -1473       C  
-ATOM     53  CG1 VAL A  20       7.562   2.737  38.639  1.00 75.28           C  
-ANISOU   53  CG1 VAL A  20     9867   8690  10046    917  -3323  -1531       C  
-ATOM     54  CG2 VAL A  20       5.147   2.200  38.999  1.00 73.25           C  
-ANISOU   54  CG2 VAL A  20     9742   8948   9142    907  -2999  -1535       C  
-ATOM     55  N   ARG A  21       8.553  -0.682  39.751  1.00102.77           N  
-ANISOU   55  N   ARG A  21    13556  12135  13356    739  -3309  -1224       N  
-ATOM     56  CA  ARG A  21       9.923  -1.122  39.969  1.00103.48           C  
-ANISOU   56  CA  ARG A  21    13625  11972  13722    734  -3496  -1182       C  
-ATOM     57  C   ARG A  21      10.281  -2.240  38.991  1.00102.33           C  
-ANISOU   57  C   ARG A  21    13394  11735  13750    599  -3321  -1038       C  
-ATOM     58  O   ARG A  21      11.383  -2.266  38.441  1.00102.25           O  
-ANISOU   58  O   ARG A  21    13257  11498  14095    584  -3371  -1012       O  
-ATOM     59  CB  ARG A  21      10.116  -1.580  41.415  1.00105.38           C  
-ANISOU   59  CB  ARG A  21    14052  12242  13746    804  -3712  -1190       C  
-ATOM     60  CG  ARG A  21      11.500  -1.284  41.985  1.00106.80           C  
-ANISOU   60  CG  ARG A  21    14221  12147  14212    885  -4037  -1245       C  
-ATOM     61  CD  ARG A  21      11.616   0.157  42.482  1.00107.88           C  
-ANISOU   61  CD  ARG A  21    14362  12235  14391   1039  -4264  -1423       C  
-ATOM     62  NE  ARG A  21      11.499   1.143  41.410  1.00106.62           N  
-ANISOU   62  NE  ARG A  21    14020  12027  14463   1022  -4156  -1467       N  
-ATOM     63  CZ  ARG A  21      11.414   2.454  41.608  1.00107.31           C  
-ANISOU   63  CZ  ARG A  21    14087  12081  14604   1139  -4316  -1617       C  
-ATOM     64  NH1 ARG A  21      11.309   3.277  40.571  1.00106.21           N  
-ANISOU   64  NH1 ARG A  21    13781  11888  14686   1105  -4211  -1627       N  
-ATOM     65  NH2 ARG A  21      11.430   2.941  42.842  1.00109.27           N  
-ANISOU   65  NH2 ARG A  21    14495  12345  14679   1297  -4593  -1757       N  
-ATOM     66  N   PHE A  22       9.339  -3.154  38.775  1.00 97.05           N  
-ANISOU   66  N   PHE A  22    12790  11244  12839    507  -3120   -948       N  
-ATOM     67  CA  PHE A  22       9.516  -4.246  37.821  1.00 91.51           C  
-ANISOU   67  CA  PHE A  22    12031  10471  12266    391  -2959   -831       C  
-ATOM     68  C   PHE A  22       9.664  -3.713  36.403  1.00 87.08           C  
-ANISOU   68  C   PHE A  22    11308   9836  11941    372  -2795   -847       C  
-ATOM     69  O   PHE A  22      10.680  -3.933  35.741  1.00 84.65           O  
-ANISOU   69  O   PHE A  22    10892   9337  11934    363  -2791   -814       O  
-ATOM     70  CB  PHE A  22       8.325  -5.202  37.872  1.00 92.68           C  
-ANISOU   70  CB  PHE A  22    12278  10826  12110    297  -2798   -736       C  
-ATOM     71  CG  PHE A  22       8.298  -6.188  36.742  1.00 92.00           C  
-ANISOU   71  CG  PHE A  22    12137  10676  12142    191  -2634   -645       C  
-ATOM     72  CD1 PHE A  22       8.893  -7.428  36.877  1.00 93.92           C  
-ANISOU   72  CD1 PHE A  22    12423  10792  12469    136  -2701   -551       C  
-ATOM     73  CD2 PHE A  22       7.687  -5.870  35.539  1.00 92.66           C  
-ANISOU   73  CD2 PHE A  22    12138  10816  12253    160  -2433   -664       C  
-ATOM     74  CE1 PHE A  22       8.875  -8.339  35.837  1.00 96.83           C  
-ANISOU   74  CE1 PHE A  22    12754  11093  12945     61  -2571   -490       C  
-ATOM     75  CE2 PHE A  22       7.667  -6.775  34.495  1.00 95.72           C  
-ANISOU   75  CE2 PHE A  22    12497  11140  12731     86  -2302   -599       C  
-ATOM     76  CZ  PHE A  22       8.261  -8.012  34.644  1.00 97.18           C  
-ANISOU   76  CZ  PHE A  22    12726  11199  12998     42  -2372   -519       C  
-ATOM     77  N   PHE A  23       8.630  -3.022  35.940  1.00 71.63           N  
-ANISOU   77  N   PHE A  23     9337   8043   9838    372  -2654   -893       N  
-ATOM     78  CA  PHE A  23       8.643  -2.417  34.622  1.00 67.24           C  
-ANISOU   78  CA  PHE A  23     8652   7438   9460    360  -2502   -903       C  
-ATOM     79  C   PHE A  23       9.934  -1.640  34.432  1.00 70.40           C  
-ANISOU   79  C   PHE A  23     8921   7615  10214    418  -2625   -928       C  
-ATOM     80  O   PHE A  23      10.494  -1.599  33.337  1.00 70.91           O  
-ANISOU   80  O   PHE A  23     8863   7568  10512    396  -2505   -878       O  
-ATOM     81  CB  PHE A  23       7.448  -1.479  34.471  1.00 59.57           C  
-ANISOU   81  CB  PHE A  23     7688   6650   8296    384  -2422   -978       C  
-ATOM     82  CG  PHE A  23       7.293  -0.910  33.091  1.00 49.85           C  
-ANISOU   82  CG  PHE A  23     6351   5388   7200    363  -2262   -975       C  
-ATOM     83  CD1 PHE A  23       6.557  -1.584  32.131  1.00 45.18           C  
-ANISOU   83  CD1 PHE A  23     5775   4880   6510    287  -2058   -917       C  
-ATOM     84  CD2 PHE A  23       7.875   0.302  32.756  1.00 45.95           C  
-ANISOU   84  CD2 PHE A  23     5750   4774   6935    421  -2331  -1021       C  
-ATOM     85  CE1 PHE A  23       6.407  -1.065  30.867  1.00 41.57           C  
-ANISOU   85  CE1 PHE A  23     5247   4399   6149    280  -1919   -913       C  
-ATOM     86  CE2 PHE A  23       7.732   0.825  31.488  1.00 41.51           C  
-ANISOU   86  CE2 PHE A  23     5102   4188   6481    400  -2180   -995       C  
-ATOM     87  CZ  PHE A  23       6.993   0.140  30.544  1.00 40.60           C  
-ANISOU   87  CZ  PHE A  23     5023   4170   6235    335  -1970   -944       C  
-ATOM     88  N   GLN A  24      10.402  -1.028  35.511  1.00 71.19           N  
-ANISOU   88  N   GLN A  24     9046   7651  10353    498  -2870  -1000       N  
-ATOM     89  CA  GLN A  24      11.602  -0.208  35.468  1.00 75.49           C  
-ANISOU   89  CA  GLN A  24     9455   7967  11260    552  -3034  -1024       C  
-ATOM     90  C   GLN A  24      12.821  -0.995  35.007  1.00 75.65           C  
-ANISOU   90  C   GLN A  24     9367   7791  11587    515  -3017   -927       C  
-ATOM     91  O   GLN A  24      13.733  -0.431  34.401  1.00 75.35           O  
-ANISOU   91  O   GLN A  24     9154   7580  11895    527  -3025   -896       O  
-ATOM     92  CB  GLN A  24      11.876   0.397  36.844  1.00 81.39           C  
-ANISOU   92  CB  GLN A  24    10284   8669  11973    654  -3345  -1130       C  
-ATOM     93  CG  GLN A  24      13.207   1.119  36.965  1.00 88.34           C  
-ANISOU   93  CG  GLN A  24    11023   9275  13266    706  -3577  -1148       C  
-ATOM     94  CD  GLN A  24      13.129   2.563  36.518  1.00 91.40           C  
-ANISOU   94  CD  GLN A  24    11298   9609  13821    745  -3620  -1208       C  
-ATOM     95  OE1 GLN A  24      13.730   3.445  37.133  1.00 93.85           O  
-ANISOU   95  OE1 GLN A  24    11572   9759  14326    825  -3902  -1286       O  
-ATOM     96  NE2 GLN A  24      12.385   2.815  35.446  1.00 92.89           N  
-ANISOU   96  NE2 GLN A  24    11436   9915  13942    691  -3364  -1171       N  
-ATOM     97  N   GLY A  25      12.833  -2.296  35.285  1.00 92.59           N  
-ANISOU   97  N   GLY A  25    11606   9959  13616    473  -2993   -872       N  
-ATOM     98  CA  GLY A  25      14.011  -3.110  35.035  1.00 90.70           C  
-ANISOU   98  CA  GLY A  25    11277   9527  13658    460  -3018   -801       C  
-ATOM     99  C   GLY A  25      13.927  -4.088  33.879  1.00 86.88           C  
-ANISOU   99  C   GLY A  25    10758   9064  13188    401  -2763   -722       C  
-ATOM    100  O   GLY A  25      14.887  -4.808  33.601  1.00 86.23           O  
-ANISOU  100  O   GLY A  25    10595   8830  13337    406  -2766   -674       O  
-ATOM    101  N   MET A  26      12.782  -4.124  33.207  1.00 70.35           N  
-ANISOU  101  N   MET A  26     8725   7152  10853    357  -2557   -720       N  
-ATOM    102  CA  MET A  26      12.605  -5.014  32.067  1.00 67.70           C  
-ANISOU  102  CA  MET A  26     8380   6837  10505    317  -2333   -664       C  
-ATOM    103  C   MET A  26      13.703  -4.784  31.038  1.00 68.38           C  
-ANISOU  103  C   MET A  26     8282   6772  10927    359  -2224   -628       C  
-ATOM    104  O   MET A  26      14.202  -3.666  30.900  1.00 68.26           O  
-ANISOU  104  O   MET A  26     8134   6689  11111    393  -2251   -631       O  
-ATOM    105  CB  MET A  26      11.243  -4.789  31.415  1.00 64.62           C  
-ANISOU  105  CB  MET A  26     8059   6643   9850    276  -2152   -678       C  
-ATOM    106  CG  MET A  26      10.072  -4.968  32.348  1.00 63.05           C  
-ANISOU  106  CG  MET A  26     8012   6621   9325    235  -2217   -699       C  
-ATOM    107  SD  MET A  26       8.534  -5.074  31.423  1.00 58.10           S  
-ANISOU  107  SD  MET A  26     7443   6192   8440    175  -1997   -696       S  
-ATOM    108  CE  MET A  26       8.805  -6.581  30.497  1.00 56.42           C  
-ANISOU  108  CE  MET A  26     7256   5888   8293    133  -1890   -629       C  
-ATOM    109  N   PRO A  27      14.078  -5.843  30.306  1.00 61.43           N  
-ANISOU  109  N   PRO A  27     7388   5839  10114    362  -2101   -589       N  
-ATOM    110  CA  PRO A  27      15.109  -5.720  29.273  1.00 63.61           C  
-ANISOU  110  CA  PRO A  27     7484   6000  10684    419  -1956   -546       C  
-ATOM    111  C   PRO A  27      14.696  -4.694  28.232  1.00 65.13           C  
-ANISOU  111  C   PRO A  27     7612   6279  10854    426  -1757   -528       C  
-ATOM    112  O   PRO A  27      13.513  -4.606  27.899  1.00 63.89           O  
-ANISOU  112  O   PRO A  27     7579   6277  10421    390  -1667   -554       O  
-ATOM    113  CB  PRO A  27      15.137  -7.114  28.638  1.00 62.69           C  
-ANISOU  113  CB  PRO A  27     7430   5873  10515    432  -1843   -538       C  
-ATOM    114  CG  PRO A  27      14.547  -8.020  29.658  1.00 61.27           C  
-ANISOU  114  CG  PRO A  27     7425   5722  10132    372  -2018   -556       C  
-ATOM    115  CD  PRO A  27      13.516  -7.202  30.367  1.00 59.87           C  
-ANISOU  115  CD  PRO A  27     7339   5691   9719    319  -2088   -579       C  
-ATOM    116  N   GLU A  28      15.658  -3.928  27.730  1.00 87.36           N  
-ANISOU  116  N   GLU A  28    10232   8992  13970    468  -1697   -471       N  
-ATOM    117  CA  GLU A  28      15.387  -2.970  26.669  1.00 88.84           C  
-ANISOU  117  CA  GLU A  28    10350   9244  14160    474  -1502   -425       C  
-ATOM    118  C   GLU A  28      14.523  -3.623  25.601  1.00 85.82           C  
-ANISOU  118  C   GLU A  28    10101   9002  13505    479  -1277   -435       C  
-ATOM    119  O   GLU A  28      14.726  -4.788  25.252  1.00 85.54           O  
-ANISOU  119  O   GLU A  28    10114   8952  13435    512  -1203   -445       O  
-ATOM    120  CB  GLU A  28      16.691  -2.475  26.041  1.00 97.37           C  
-ANISOU  120  CB  GLU A  28    11186  10191  15618    522  -1403   -321       C  
-ATOM    121  CG  GLU A  28      17.383  -3.497  25.148  1.00108.83           C  
-ANISOU  121  CG  GLU A  28    12579  11619  17151    591  -1194   -279       C  
-ATOM    122  CD  GLU A  28      18.489  -2.884  24.308  1.00117.89           C  
-ANISOU  122  CD  GLU A  28    13475  12689  18628    641  -1018   -151       C  
-ATOM    123  OE1 GLU A  28      19.095  -1.889  24.759  1.00123.83           O  
-ANISOU  123  OE1 GLU A  28    14055  13328  19665    613  -1145    -89       O  
-ATOM    124  OE2 GLU A  28      18.746  -3.391  23.194  1.00122.33           O  
-ANISOU  124  OE2 GLU A  28    14009  13303  19166    714   -754   -108       O  
-ATOM    125  N   LYS A  29      13.546  -2.880  25.094  1.00 76.44           N  
-ANISOU  125  N   LYS A  29     8978   7935  12130    453  -1193   -442       N  
-ATOM    126  CA  LYS A  29      12.725  -3.370  23.999  1.00 72.89           C  
-ANISOU  126  CA  LYS A  29     8653   7603  11438    465   -997   -453       C  
-ATOM    127  C   LYS A  29      12.806  -2.421  22.814  1.00 72.41           C  
-ANISOU  127  C   LYS A  29     8516   7570  11426    497   -802   -377       C  
-ATOM    128  O   LYS A  29      13.061  -1.231  22.982  1.00 73.69           O  
-ANISOU  128  O   LYS A  29     8562   7692  11746    479   -853   -329       O  
-ATOM    129  CB  LYS A  29      11.267  -3.527  24.430  1.00 67.61           C  
-ANISOU  129  CB  LYS A  29     8164   7069  10456    400  -1079   -531       C  
-ATOM    130  CG  LYS A  29      10.492  -2.225  24.466  1.00 62.00           C  
-ANISOU  130  CG  LYS A  29     7452   6439   9668    370  -1106   -545       C  
-ATOM    131  CD  LYS A  29       9.007  -2.474  24.643  1.00 55.04           C  
-ANISOU  131  CD  LYS A  29     6729   5707   8478    320  -1133   -615       C  
-ATOM    132  CE  LYS A  29       8.222  -1.168  24.625  1.00 51.54           C  
-ANISOU  132  CE  LYS A  29     6277   5342   7965    307  -1161   -644       C  
-ATOM    133  NZ  LYS A  29       8.279  -0.468  23.308  1.00 46.72           N  
-ANISOU  133  NZ  LYS A  29     5628   4723   7400    338   -999   -588       N  
-ATOM    134  N   PRO A  30      12.596  -2.950  21.603  1.00 80.56           N  
-ANISOU  134  N   PRO A  30     9623   8664  12323    552   -592   -364       N  
-ATOM    135  CA  PRO A  30      12.521  -2.093  20.419  1.00 80.24           C  
-ANISOU  135  CA  PRO A  30     9551   8673  12264    585   -398   -284       C  
-ATOM    136  C   PRO A  30      11.269  -1.236  20.501  1.00 78.27           C  
-ANISOU  136  C   PRO A  30     9400   8515  11824    519   -475   -323       C  
-ATOM    137  O   PRO A  30      10.344  -1.582  21.241  1.00 77.19           O  
-ANISOU  137  O   PRO A  30     9380   8435  11514    466   -621   -421       O  
-ATOM    138  CB  PRO A  30      12.377  -3.093  19.264  1.00 81.78           C  
-ANISOU  138  CB  PRO A  30     9869   8925  12277    673   -203   -304       C  
-ATOM    139  CG  PRO A  30      12.800  -4.417  19.819  1.00 81.22           C  
-ANISOU  139  CG  PRO A  30     9824   8791  12245    697   -284   -372       C  
-ATOM    140  CD  PRO A  30      12.458  -4.377  21.272  1.00 80.19           C  
-ANISOU  140  CD  PRO A  30     9701   8631  12136    595   -542   -423       C  
-ATOM    141  N   THR A  31      11.238  -0.133  19.762  1.00 66.26           N  
-ANISOU  141  N   THR A  31     7824   7008  10343    524   -379   -239       N  
-ATOM    142  CA  THR A  31      10.026   0.668  19.667  1.00 62.19           C  
-ANISOU  142  CA  THR A  31     7407   6575   9647    478   -442   -281       C  
-ATOM    143  C   THR A  31       8.960  -0.163  18.966  1.00 59.53           C  
-ANISOU  143  C   THR A  31     7275   6348   8997    497   -365   -357       C  
-ATOM    144  O   THR A  31       7.788  -0.138  19.336  1.00 58.59           O  
-ANISOU  144  O   THR A  31     7262   6305   8695    447   -477   -447       O  
-ATOM    145  CB  THR A  31      10.265   1.957  18.872  1.00 63.43           C  
-ANISOU  145  CB  THR A  31     7472   6708   9919    483   -350   -156       C  
-ATOM    146  OG1 THR A  31      11.276   2.740  19.520  1.00 62.54           O  
-ANISOU  146  OG1 THR A  31     7155   6468  10141    459   -448    -77       O  
-ATOM    147  CG2 THR A  31       8.981   2.765  18.767  1.00 62.59           C  
-ANISOU  147  CG2 THR A  31     7473   6677   9633    444   -436   -213       C  
-ATOM    148  N   THR A  32       9.393  -0.913  17.957  1.00 56.83           N  
-ANISOU  148  N   THR A  32     6979   6010   8604    577   -179   -322       N  
-ATOM    149  CA  THR A  32       8.508  -1.747  17.154  1.00 53.30           C  
-ANISOU  149  CA  THR A  32     6733   5639   7881    617   -118   -396       C  
-ATOM    150  C   THR A  32       7.930  -2.939  17.924  1.00 50.51           C  
-ANISOU  150  C   THR A  32     6478   5292   7422    575   -264   -511       C  
-ATOM    151  O   THR A  32       6.962  -3.559  17.486  1.00 49.30           O  
-ANISOU  151  O   THR A  32     6485   5189   7057    576   -283   -582       O  
-ATOM    152  CB  THR A  32       9.231  -2.248  15.896  1.00 54.09           C  
-ANISOU  152  CB  THR A  32     6863   5736   7951    744    113   -340       C  
-ATOM    153  OG1 THR A  32      10.640  -2.296  16.151  1.00 54.59           O  
-ANISOU  153  OG1 THR A  32     6739   5721   8283    783    189   -258       O  
-ATOM    154  CG2 THR A  32       8.975  -1.308  14.730  1.00 52.16           C  
-ANISOU  154  CG2 THR A  32     6663   5548   7608    784    261   -253       C  
-ATOM    155  N   THR A  33       8.528  -3.264  19.064  1.00 56.61           N  
-ANISOU  155  N   THR A  33     7154   6002   8352    537   -381   -518       N  
-ATOM    156  CA  THR A  33       7.944  -4.250  19.963  1.00 53.57           C  
-ANISOU  156  CA  THR A  33     6852   5627   7876    475   -538   -597       C  
-ATOM    157  C   THR A  33       7.079  -3.528  20.983  1.00 51.01           C  
-ANISOU  157  C   THR A  33     6517   5370   7496    381   -693   -628       C  
-ATOM    158  O   THR A  33       7.491  -2.515  21.548  1.00 50.30           O  
-ANISOU  158  O   THR A  33     6311   5257   7544    368   -747   -600       O  
-ATOM    159  CB  THR A  33       9.014  -5.056  20.719  1.00 55.05           C  
-ANISOU  159  CB  THR A  33     6963   5711   8242    488   -602   -588       C  
-ATOM    160  OG1 THR A  33       9.800  -5.812  19.789  1.00 55.14           O  
-ANISOU  160  OG1 THR A  33     6981   5666   8303    596   -458   -577       O  
-ATOM    161  CG2 THR A  33       8.357  -6.007  21.705  1.00 52.65           C  
-ANISOU  161  CG2 THR A  33     6750   5418   7835    410   -775   -642       C  
-ATOM    162  N   VAL A  34       5.878  -4.044  21.209  1.00 57.65           N  
-ANISOU  162  N   VAL A  34     7472   6290   8141    322   -767   -685       N  
-ATOM    163  CA  VAL A  34       4.957  -3.436  22.158  1.00 54.85           C  
-ANISOU  163  CA  VAL A  34     7108   6029   7705    249   -890   -721       C  
-ATOM    164  C   VAL A  34       4.542  -4.434  23.235  1.00 53.72           C  
-ANISOU  164  C   VAL A  34     7010   5915   7485    180  -1011   -737       C  
-ATOM    165  O   VAL A  34       4.046  -5.521  22.933  1.00 54.27           O  
-ANISOU  165  O   VAL A  34     7172   5986   7461    153  -1012   -743       O  
-ATOM    166  CB  VAL A  34       3.705  -2.892  21.451  1.00 54.02           C  
-ANISOU  166  CB  VAL A  34     7070   6019   7437    236   -858   -756       C  
-ATOM    167  CG1 VAL A  34       2.671  -2.454  22.472  1.00 53.23           C  
-ANISOU  167  CG1 VAL A  34     6955   6031   7239    172   -975   -804       C  
-ATOM    168  CG2 VAL A  34       4.075  -1.748  20.528  1.00 52.19           C  
-ANISOU  168  CG2 VAL A  34     6794   5759   7275    294   -760   -720       C  
-ATOM    169  N   ARG A  35       4.758  -4.056  24.491  1.00 47.77           N  
-ANISOU  169  N   ARG A  35     6195   5179   6775    155  -1126   -740       N  
-ATOM    170  CA  ARG A  35       4.418  -4.903  25.626  1.00 46.34           C  
-ANISOU  170  CA  ARG A  35     6059   5040   6509     91  -1238   -732       C  
-ATOM    171  C   ARG A  35       3.091  -4.482  26.246  1.00 44.83           C  
-ANISOU  171  C   ARG A  35     5887   5015   6132     41  -1280   -763       C  
-ATOM    172  O   ARG A  35       2.946  -3.359  26.721  1.00 43.20           O  
-ANISOU  172  O   ARG A  35     5628   4868   5918     71  -1319   -807       O  
-ATOM    173  CB  ARG A  35       5.526  -4.848  26.678  1.00 46.98           C  
-ANISOU  173  CB  ARG A  35     6080   5039   6732    113  -1348   -716       C  
-ATOM    174  CG  ARG A  35       6.903  -5.194  26.138  1.00 47.31           C  
-ANISOU  174  CG  ARG A  35     6065   4915   6995    171  -1307   -684       C  
-ATOM    175  CD  ARG A  35       7.920  -5.372  27.254  1.00 47.08           C  
-ANISOU  175  CD  ARG A  35     5987   4790   7112    181  -1452   -667       C  
-ATOM    176  NE  ARG A  35       9.152  -5.992  26.771  1.00 47.61           N  
-ANISOU  176  NE  ARG A  35     5996   4702   7392    232  -1414   -635       N  
-ATOM    177  CZ  ARG A  35      10.360  -5.450  26.884  1.00 48.71           C  
-ANISOU  177  CZ  ARG A  35     6004   4722   7783    286  -1442   -616       C  
-ATOM    178  NH1 ARG A  35      10.506  -4.271  27.474  1.00 49.47           N  
-ANISOU  178  NH1 ARG A  35     6027   4818   7953    294  -1533   -630       N  
-ATOM    179  NH2 ARG A  35      11.420  -6.091  26.410  1.00 48.67           N  
-ANISOU  179  NH2 ARG A  35     5933   4590   7970    340  -1389   -587       N  
-ATOM    180  N   LEU A  36       2.119  -5.387  26.224  1.00 43.55           N  
-ANISOU  180  N   LEU A  36     5792   4921   5834    -31  -1278   -740       N  
-ATOM    181  CA  LEU A  36       0.831  -5.160  26.868  1.00 45.06           C  
-ANISOU  181  CA  LEU A  36     5980   5283   5858    -85  -1302   -750       C  
-ATOM    182  C   LEU A  36       0.677  -6.107  28.048  1.00 46.88           C  
-ANISOU  182  C   LEU A  36     6240   5563   6010   -156  -1378   -678       C  
-ATOM    183  O   LEU A  36       1.016  -7.292  27.960  1.00 47.17           O  
-ANISOU  183  O   LEU A  36     6326   5503   6092   -203  -1407   -614       O  
-ATOM    184  CB  LEU A  36      -0.311  -5.391  25.887  1.00 45.09           C  
-ANISOU  184  CB  LEU A  36     6017   5334   5782   -124  -1242   -759       C  
-ATOM    185  CG  LEU A  36      -0.347  -4.487  24.661  1.00 44.71           C  
-ANISOU  185  CG  LEU A  36     5965   5252   5772    -58  -1170   -818       C  
-ATOM    186  CD1 LEU A  36      -1.322  -5.041  23.648  1.00 44.25           C  
-ANISOU  186  CD1 LEU A  36     5971   5196   5645    -93  -1145   -823       C  
-ATOM    187  CD2 LEU A  36      -0.720  -3.073  25.058  1.00 45.42           C  
-ANISOU  187  CD2 LEU A  36     5984   5440   5835    -17  -1183   -879       C  
-ATOM    188  N   PHE A  37       0.151  -5.584  29.148  1.00 41.25           N  
-ANISOU  188  N   PHE A  37     5500   5001   5172   -157  -1413   -687       N  
-ATOM    189  CA  PHE A  37       0.047  -6.356  30.375  1.00 43.84           C  
-ANISOU  189  CA  PHE A  37     5862   5396   5398   -213  -1477   -603       C  
-ATOM    190  C   PHE A  37      -1.385  -6.819  30.622  1.00 47.81           C  
-ANISOU  190  C   PHE A  37     6355   6070   5741   -304  -1429   -535       C  
-ATOM    191  O   PHE A  37      -2.305  -6.005  30.698  1.00 48.95           O  
-ANISOU  191  O   PHE A  37     6444   6371   5785   -279  -1375   -588       O  
-ATOM    192  CB  PHE A  37       0.586  -5.533  31.544  1.00 40.74           C  
-ANISOU  192  CB  PHE A  37     5462   5054   4963   -130  -1558   -651       C  
-ATOM    193  CG  PHE A  37       2.034  -5.130  31.381  1.00 37.80           C  
-ANISOU  193  CG  PHE A  37     5076   4494   4791    -53  -1630   -698       C  
-ATOM    194  CD1 PHE A  37       3.039  -5.812  32.051  1.00 36.85           C  
-ANISOU  194  CD1 PHE A  37     4996   4260   4746    -55  -1736   -646       C  
-ATOM    195  CD2 PHE A  37       2.390  -4.083  30.542  1.00 35.51           C  
-ANISOU  195  CD2 PHE A  37     4724   4135   4634     16  -1595   -779       C  
-ATOM    196  CE1 PHE A  37       4.365  -5.451  31.901  1.00 37.04           C  
-ANISOU  196  CE1 PHE A  37     4980   4106   4987     13  -1805   -682       C  
-ATOM    197  CE2 PHE A  37       3.718  -3.714  30.390  1.00 35.49           C  
-ANISOU  197  CE2 PHE A  37     4679   3959   4845     76  -1652   -796       C  
-ATOM    198  CZ  PHE A  37       4.707  -4.400  31.071  1.00 35.63           C  
-ANISOU  198  CZ  PHE A  37     4720   3866   4951     76  -1756   -752       C  
-ATOM    199  N   ASP A  38      -1.564  -8.136  30.714  1.00 53.52           N  
-ANISOU  199  N   ASP A  38     7119   6751   6466   -410  -1455   -413       N  
-ATOM    200  CA  ASP A  38      -2.862  -8.733  31.002  1.00 60.28           C  
-ANISOU  200  CA  ASP A  38     7946   7749   7208   -521  -1420   -308       C  
-ATOM    201  C   ASP A  38      -3.170  -8.583  32.486  1.00 63.97           C  
-ANISOU  201  C   ASP A  38     8402   8410   7492   -523  -1417   -240       C  
-ATOM    202  O   ASP A  38      -2.439  -9.095  33.336  1.00 66.97           O  
-ANISOU  202  O   ASP A  38     8847   8748   7849   -530  -1493   -169       O  
-ATOM    203  CB  ASP A  38      -2.857 -10.215  30.617  1.00 61.35           C  
-ANISOU  203  CB  ASP A  38     8131   7742   7438   -636  -1480   -190       C  
-ATOM    204  CG  ASP A  38      -4.213 -10.884  30.812  1.00 66.81           C  
-ANISOU  204  CG  ASP A  38     8771   8551   8064   -770  -1458    -57       C  
-ATOM    205  OD1 ASP A  38      -4.662 -11.609  29.894  1.00 66.72           O  
-ANISOU  205  OD1 ASP A  38     8765   8428   8157   -840  -1493    -32       O  
-ATOM    206  OD2 ASP A  38      -4.829 -10.694  31.883  1.00 68.22           O  
-ANISOU  206  OD2 ASP A  38     8899   8931   8089   -799  -1409     24       O  
-ATOM    207  N   ARG A  39      -4.250  -7.878  32.799  1.00 59.33           N  
-ANISOU  207  N   ARG A  39     7738   8038   6767   -505  -1330   -264       N  
-ATOM    208  CA  ARG A  39      -4.649  -7.695  34.187  1.00 60.90           C  
-ANISOU  208  CA  ARG A  39     7929   8458   6754   -482  -1300   -206       C  
-ATOM    209  C   ARG A  39      -6.036  -8.263  34.440  1.00 65.56           C  
-ANISOU  209  C   ARG A  39     8432   9233   7244   -597  -1201    -60       C  
-ATOM    210  O   ARG A  39      -6.849  -7.650  35.126  1.00 68.16           O  
-ANISOU  210  O   ARG A  39     8693   9804   7402   -546  -1108    -70       O  
-ATOM    211  CB  ARG A  39      -4.615  -6.217  34.561  1.00 58.36           C  
-ANISOU  211  CB  ARG A  39     7582   8254   6337   -319  -1286   -380       C  
-ATOM    212  CG  ARG A  39      -3.249  -5.591  34.435  1.00 52.05           C  
-ANISOU  212  CG  ARG A  39     6846   7272   5657   -212  -1397   -504       C  
-ATOM    213  CD  ARG A  39      -3.301  -4.124  34.802  1.00 49.92           C  
-ANISOU  213  CD  ARG A  39     6550   7103   5316    -54  -1415   -675       C  
-ATOM    214  NE  ARG A  39      -1.999  -3.477  34.669  1.00 47.00           N  
-ANISOU  214  NE  ARG A  39     6216   6540   5100     38  -1538   -780       N  
-ATOM    215  CZ  ARG A  39      -1.103  -3.385  35.646  1.00 45.31           C  
-ANISOU  215  CZ  ARG A  39     6076   6285   4856    109  -1663   -796       C  
-ATOM    216  NH1 ARG A  39      -1.364  -3.906  36.838  1.00 46.86           N  
-ANISOU  216  NH1 ARG A  39     6338   6630   4838    107  -1673   -715       N  
-ATOM    217  NH2 ARG A  39       0.055  -2.771  35.429  1.00 42.32           N  
-ANISOU  217  NH2 ARG A  39     5701   5713   4666    183  -1781   -884       N  
-ATOM    218  N   GLY A  40      -6.306  -9.436  33.880  1.00 50.50           N  
-ANISOU  218  N   GLY A  40     6520   7209   5459   -746  -1227     76       N  
-ATOM    219  CA  GLY A  40      -7.592 -10.079  34.064  1.00 58.29           C  
-ANISOU  219  CA  GLY A  40     7404   8336   6407   -879  -1153    244       C  
-ATOM    220  C   GLY A  40      -8.674  -9.528  33.158  1.00 63.96           C  
-ANISOU  220  C   GLY A  40     8001   9112   7190   -880  -1085    162       C  
-ATOM    221  O   GLY A  40      -8.877 -10.021  32.051  1.00 65.96           O  
-ANISOU  221  O   GLY A  40     8251   9196   7616   -951  -1144    157       O  
-ATOM    222  N   ASP A  41      -9.371  -8.497  33.624  1.00 92.85           N  
-ANISOU  222  N   ASP A  41    11567  13005  10707   -787   -977     85       N  
-ATOM    223  CA  ASP A  41     -10.523  -7.972  32.897  1.00 95.04           C  
-ANISOU  223  CA  ASP A  41    11710  13360  11042   -789   -915     18       C  
-ATOM    224  C   ASP A  41     -10.151  -6.902  31.879  1.00 88.24           C  
-ANISOU  224  C   ASP A  41    10884  12380  10264   -665   -960   -211       C  
-ATOM    225  O   ASP A  41     -11.011  -6.390  31.164  1.00 87.00           O  
-ANISOU  225  O   ASP A  41    10636  12254  10165   -653   -936   -288       O  
-ATOM    226  CB  ASP A  41     -11.563  -7.423  33.874  1.00108.18           C  
-ANISOU  226  CB  ASP A  41    13235  15345  12522   -744   -769     52       C  
-ATOM    227  CG  ASP A  41     -12.043  -8.470  34.855  1.00119.40           C  
-ANISOU  227  CG  ASP A  41    14604  16909  13852   -875   -697    315       C  
-ATOM    228  OD1 ASP A  41     -12.923  -9.274  34.480  1.00126.25           O  
-ANISOU  228  OD1 ASP A  41    15357  17763  14849  -1034   -682    474       O  
-ATOM    229  OD2 ASP A  41     -11.536  -8.494  35.997  1.00128.05           O  
-ANISOU  229  OD2 ASP A  41    15776  18122  14755   -822   -666    371       O  
-ATOM    230  N   PHE A  42      -8.869  -6.565  31.815  1.00 80.23           N  
-ANISOU  230  N   PHE A  42     9993  11223   9267   -577  -1029   -308       N  
-ATOM    231  CA  PHE A  42      -8.409  -5.530  30.903  1.00 71.73           C  
-ANISOU  231  CA  PHE A  42     8949  10032   8274   -465  -1066   -495       C  
-ATOM    232  C   PHE A  42      -6.902  -5.608  30.729  1.00 65.50           C  
-ANISOU  232  C   PHE A  42     8283   9040   7565   -419  -1146   -533       C  
-ATOM    233  O   PHE A  42      -6.251  -6.496  31.277  1.00 66.23           O  
-ANISOU  233  O   PHE A  42     8440   9071   7654   -473  -1186   -427       O  
-ATOM    234  CB  PHE A  42      -8.808  -4.148  31.422  1.00 72.49           C  
-ANISOU  234  CB  PHE A  42     8977  10309   8256   -324  -1023   -636       C  
-ATOM    235  CG  PHE A  42      -8.140  -3.765  32.713  1.00 74.68           C  
-ANISOU  235  CG  PHE A  42     9303  10685   8386   -226  -1036   -660       C  
-ATOM    236  CD1 PHE A  42      -8.579  -4.287  33.919  1.00 77.38           C  
-ANISOU  236  CD1 PHE A  42     9623  11227   8550   -254   -972   -538       C  
-ATOM    237  CD2 PHE A  42      -7.083  -2.871  32.723  1.00 74.24           C  
-ANISOU  237  CD2 PHE A  42     9317  10520   8372   -101  -1122   -798       C  
-ATOM    238  CE1 PHE A  42      -7.968  -3.933  35.110  1.00 77.92           C  
-ANISOU  238  CE1 PHE A  42     9763  11386   8457   -145  -1001   -570       C  
-ATOM    239  CE2 PHE A  42      -6.468  -2.513  33.907  1.00 75.41           C  
-ANISOU  239  CE2 PHE A  42     9520  10737   8394     -1  -1171   -835       C  
-ATOM    240  CZ  PHE A  42      -6.912  -3.044  35.104  1.00 77.18           C  
-ANISOU  240  CZ  PHE A  42     9748  11164   8413    -15  -1115   -730       C  
-ATOM    241  N   TYR A  43      -6.350  -4.677  29.961  1.00 62.13           N  
-ANISOU  241  N   TYR A  43     7880   8504   7222   -322  -1171   -672       N  
-ATOM    242  CA  TYR A  43      -4.916  -4.649  29.723  1.00 55.56           C  
-ANISOU  242  CA  TYR A  43     7132   7483   6496   -273  -1231   -703       C  
-ATOM    243  C   TYR A  43      -4.386  -3.246  29.935  1.00 53.13           C  
-ANISOU  243  C   TYR A  43     6808   7182   6196   -138  -1260   -838       C  
-ATOM    244  O   TYR A  43      -5.142  -2.282  29.886  1.00 52.59           O  
-ANISOU  244  O   TYR A  43     6678   7226   6077    -79  -1240   -929       O  
-ATOM    245  CB  TYR A  43      -4.609  -5.092  28.298  1.00 50.66           C  
-ANISOU  245  CB  TYR A  43     6560   6669   6018   -302  -1234   -706       C  
-ATOM    246  CG  TYR A  43      -5.079  -6.484  27.974  1.00 46.61           C  
-ANISOU  246  CG  TYR A  43     6075   6104   5529   -425  -1248   -593       C  
-ATOM    247  CD1 TYR A  43      -6.404  -6.732  27.653  1.00 44.63           C  
-ANISOU  247  CD1 TYR A  43     5767   5938   5251   -499  -1228   -561       C  
-ATOM    248  CD2 TYR A  43      -4.192  -7.553  27.983  1.00 44.47           C  
-ANISOU  248  CD2 TYR A  43     5881   5683   5334   -464  -1301   -521       C  
-ATOM    249  CE1 TYR A  43      -6.834  -8.005  27.354  1.00 44.59           C  
-ANISOU  249  CE1 TYR A  43     5783   5860   5301   -616  -1273   -453       C  
-ATOM    250  CE2 TYR A  43      -4.611  -8.830  27.685  1.00 42.94           C  
-ANISOU  250  CE2 TYR A  43     5718   5417   5182   -572  -1346   -423       C  
-ATOM    251  CZ  TYR A  43      -5.934  -9.051  27.370  1.00 43.73           C  
-ANISOU  251  CZ  TYR A  43     5763   5593   5261   -651  -1338   -386       C  
-ATOM    252  OH  TYR A  43      -6.362 -10.324  27.071  1.00 43.84           O  
-ANISOU  252  OH  TYR A  43     5801   5511   5347   -764  -1413   -285       O  
-ATOM    253  N   THR A  44      -3.085  -3.128  30.169  1.00 52.89           N  
-ANISOU  253  N   THR A  44     6825   7020   6252    -87  -1326   -852       N  
-ATOM    254  CA  THR A  44      -2.461  -1.816  30.275  1.00 49.35           C  
-ANISOU  254  CA  THR A  44     6355   6530   5866     32  -1385   -970       C  
-ATOM    255  C   THR A  44      -1.173  -1.747  29.465  1.00 46.93           C  
-ANISOU  255  C   THR A  44     6067   5999   5766     51  -1410   -966       C  
-ATOM    256  O   THR A  44      -0.527  -2.761  29.215  1.00 46.37           O  
-ANISOU  256  O   THR A  44     6037   5815   5766     -2  -1402   -885       O  
-ATOM    257  CB  THR A  44      -2.144  -1.434  31.739  1.00 50.26           C  
-ANISOU  257  CB  THR A  44     6485   6736   5876    110  -1472  -1008       C  
-ATOM    258  OG1 THR A  44      -1.257  -2.403  32.312  1.00 50.34           O  
-ANISOU  258  OG1 THR A  44     6559   6660   5908     68  -1524   -914       O  
-ATOM    259  CG2 THR A  44      -3.417  -1.350  32.568  1.00 49.42           C  
-ANISOU  259  CG2 THR A  44     6349   6884   5543    122  -1420  -1018       C  
-ATOM    260  N   ALA A  45      -0.817  -0.538  29.048  1.00 47.94           N  
-ANISOU  260  N   ALA A  45     6154   6062   5998    131  -1440  -1048       N  
-ATOM    261  CA  ALA A  45       0.472  -0.269  28.427  1.00 47.36           C  
-ANISOU  261  CA  ALA A  45     6067   5791   6136    160  -1458  -1031       C  
-ATOM    262  C   ALA A  45       1.180   0.786  29.271  1.00 48.83           C  
-ANISOU  262  C   ALA A  45     6212   5934   6407    250  -1595  -1101       C  
-ATOM    263  O   ALA A  45       0.535   1.501  30.031  1.00 48.31           O  
-ANISOU  263  O   ALA A  45     6139   5991   6227    308  -1662  -1190       O  
-ATOM    264  CB  ALA A  45       0.276   0.229  27.007  1.00 45.49           C  
-ANISOU  264  CB  ALA A  45     5816   5494   5975    163  -1375  -1035       C  
-ATOM    265  N   HIS A  46       2.498   0.895  29.150  1.00 44.05           N  
-ANISOU  265  N   HIS A  46     5575   5150   6011    271  -1645  -1068       N  
-ATOM    266  CA  HIS A  46       3.236   1.840  29.986  1.00 46.35           C  
-ANISOU  266  CA  HIS A  46     5825   5367   6418    353  -1814  -1132       C  
-ATOM    267  C   HIS A  46       4.424   2.484  29.279  1.00 48.09           C  
-ANISOU  267  C   HIS A  46     5955   5380   6936    373  -1839  -1091       C  
-ATOM    268  O   HIS A  46       5.029   1.892  28.392  1.00 48.26           O  
-ANISOU  268  O   HIS A  46     5953   5307   7075    330  -1722   -997       O  
-ATOM    269  CB  HIS A  46       3.687   1.162  31.279  1.00 47.77           C  
-ANISOU  269  CB  HIS A  46     6060   5560   6532    364  -1926  -1128       C  
-ATOM    270  CG  HIS A  46       2.579   0.480  32.011  1.00 48.08           C  
-ANISOU  270  CG  HIS A  46     6179   5810   6281    337  -1884  -1129       C  
-ATOM    271  ND1 HIS A  46       1.913   1.062  33.068  1.00 49.86           N  
-ANISOU  271  ND1 HIS A  46     6435   6193   6318    415  -1964  -1223       N  
-ATOM    272  CD2 HIS A  46       2.007  -0.735  31.831  1.00 48.90           C  
-ANISOU  272  CD2 HIS A  46     6328   5994   6258    242  -1769  -1039       C  
-ATOM    273  CE1 HIS A  46       0.983   0.235  33.509  1.00 49.86           C  
-ANISOU  273  CE1 HIS A  46     6484   6376   6084    364  -1875  -1174       C  
-ATOM    274  NE2 HIS A  46       1.018  -0.862  32.777  1.00 48.18           N  
-ANISOU  274  NE2 HIS A  46     6278   6109   5919    250  -1767  -1056       N  
-ATOM    275  N   GLY A  47       4.755   3.703  29.688  1.00 40.79           N  
-ANISOU  275  N   GLY A  47     4974   4384   6139    444  -1996  -1161       N  
-ATOM    276  CA  GLY A  47       5.803   4.464  29.041  1.00 47.27           C  
-ANISOU  276  CA  GLY A  47     5684   5008   7270    453  -2030  -1103       C  
-ATOM    277  C   GLY A  47       5.501   4.673  27.572  1.00 49.89           C  
-ANISOU  277  C   GLY A  47     5988   5335   7634    412  -1847  -1027       C  
-ATOM    278  O   GLY A  47       4.363   4.941  27.191  1.00 47.67           O  
-ANISOU  278  O   GLY A  47     5755   5177   7179    409  -1790  -1076       O  
-ATOM    279  N   GLU A  48       6.538   4.545  26.751  1.00 77.90           N  
-ANISOU  279  N   GLU A  48     9455   8740  11403    388  -1755   -905       N  
-ATOM    280  CA  GLU A  48       6.436   4.675  25.303  1.00 80.59           C  
-ANISOU  280  CA  GLU A  48     9781   9070  11768    362  -1565   -811       C  
-ATOM    281  C   GLU A  48       5.124   4.104  24.786  1.00 78.63           C  
-ANISOU  281  C   GLU A  48     9657   8988  11229    337  -1444   -853       C  
-ATOM    282  O   GLU A  48       4.347   4.797  24.130  1.00 78.34           O  
-ANISOU  282  O   GLU A  48     9642   8998  11126    340  -1416   -870       O  
-ATOM    283  CB  GLU A  48       7.599   3.932  24.643  1.00 87.43           C  
-ANISOU  283  CB  GLU A  48    10586   9833  12799    348  -1422   -683       C  
-ATOM    284  CG  GLU A  48       8.295   4.689  23.534  1.00 98.22           C  
-ANISOU  284  CG  GLU A  48    11845  11094  14382    352  -1313   -550       C  
-ATOM    285  CD  GLU A  48       9.254   3.811  22.752  1.00106.16           C  
-ANISOU  285  CD  GLU A  48    12805  12048  15484    359  -1116   -432       C  
-ATOM    286  OE1 GLU A  48       9.256   2.584  22.990  1.00111.22           O  
-ANISOU  286  OE1 GLU A  48    13519  12732  16009    361  -1075   -471       O  
-ATOM    287  OE2 GLU A  48      10.002   4.347  21.904  1.00111.15           O  
-ANISOU  287  OE2 GLU A  48    13325  12598  16310    367  -1001   -297       O  
-ATOM    288  N   ASP A  49       4.886   2.834  25.093  1.00 65.69           N  
-ANISOU  288  N   ASP A  49     8096   7424   9438    309  -1393   -864       N  
-ATOM    289  CA  ASP A  49       3.718   2.125  24.588  1.00 64.02           C  
-ANISOU  289  CA  ASP A  49     7991   7344   8989    275  -1292   -887       C  
-ATOM    290  C   ASP A  49       2.418   2.784  25.026  1.00 62.33           C  
-ANISOU  290  C   ASP A  49     7802   7267   8614    281  -1368   -988       C  
-ATOM    291  O   ASP A  49       1.465   2.865  24.256  1.00 62.62           O  
-ANISOU  291  O   ASP A  49     7884   7373   8536    267  -1301  -1003       O  
-ATOM    292  CB  ASP A  49       3.757   0.656  25.009  1.00 65.58           C  
-ANISOU  292  CB  ASP A  49     8253   7573   9091    236  -1266   -871       C  
-ATOM    293  CG  ASP A  49       4.870  -0.116  24.317  1.00 68.50           C  
-ANISOU  293  CG  ASP A  49     8610   7819   9596    245  -1165   -786       C  
-ATOM    294  OD1 ASP A  49       5.292   0.300  23.214  1.00 70.94           O  
-ANISOU  294  OD1 ASP A  49     8889   8066   9998    275  -1052   -731       O  
-ATOM    295  OD2 ASP A  49       5.318  -1.140  24.875  1.00 69.34           O  
-ANISOU  295  OD2 ASP A  49     8737   7895   9713    228  -1195   -771       O  
-ATOM    296  N   ALA A  50       2.385   3.264  26.263  1.00 60.23           N  
-ANISOU  296  N   ALA A  50     7508   7038   8340    316  -1516  -1065       N  
-ATOM    297  CA  ALA A  50       1.223   3.992  26.756  1.00 58.04           C  
-ANISOU  297  CA  ALA A  50     7237   6896   7919    351  -1590  -1177       C  
-ATOM    298  C   ALA A  50       0.883   5.145  25.816  1.00 55.89           C  
-ANISOU  298  C   ALA A  50     6932   6580   7723    376  -1591  -1194       C  
-ATOM    299  O   ALA A  50      -0.264   5.308  25.408  1.00 55.35           O  
-ANISOU  299  O   ALA A  50     6891   6616   7523    371  -1555  -1241       O  
-ATOM    300  CB  ALA A  50       1.479   4.510  28.154  1.00 58.80           C  
-ANISOU  300  CB  ALA A  50     7313   7012   8017    420  -1763  -1267       C  
-ATOM    301  N   LEU A  51       1.894   5.939  25.473  1.00 57.78           N  
-ANISOU  301  N   LEU A  51     7105   6655   8193    398  -1642  -1143       N  
-ATOM    302  CA  LEU A  51       1.711   7.059  24.562  1.00 55.32           C  
-ANISOU  302  CA  LEU A  51     6762   6276   7981    413  -1654  -1126       C  
-ATOM    303  C   LEU A  51       1.154   6.566  23.239  1.00 53.64           C  
-ANISOU  303  C   LEU A  51     6619   6102   7661    369  -1480  -1057       C  
-ATOM    304  O   LEU A  51       0.193   7.130  22.710  1.00 53.80           O  
-ANISOU  304  O   LEU A  51     6667   6172   7602    379  -1491  -1101       O  
-ATOM    305  CB  LEU A  51       3.035   7.782  24.320  1.00 56.72           C  
-ANISOU  305  CB  LEU A  51     6842   6256   8454    420  -1707  -1029       C  
-ATOM    306  CG  LEU A  51       3.802   8.246  25.556  1.00 58.14           C  
-ANISOU  306  CG  LEU A  51     6952   6346   8792    466  -1912  -1088       C  
-ATOM    307  CD1 LEU A  51       5.060   8.991  25.148  1.00 60.17           C  
-ANISOU  307  CD1 LEU A  51     7087   6390   9386    456  -1964   -965       C  
-ATOM    308  CD2 LEU A  51       2.923   9.116  26.435  1.00 59.45           C  
-ANISOU  308  CD2 LEU A  51     7137   6588   8865    544  -2102  -1262       C  
-ATOM    309  N   LEU A  52       1.763   5.509  22.710  1.00 45.04           N  
-ANISOU  309  N   LEU A  52     5563   4982   6569    333  -1335   -960       N  
-ATOM    310  CA  LEU A  52       1.346   4.945  21.430  1.00 42.79           C  
-ANISOU  310  CA  LEU A  52     5366   4720   6172    312  -1182   -903       C  
-ATOM    311  C   LEU A  52      -0.120   4.523  21.444  1.00 41.87           C  
-ANISOU  311  C   LEU A  52     5328   4745   5837    292  -1193   -994       C  
-ATOM    312  O   LEU A  52      -0.860   4.807  20.510  1.00 41.51           O  
-ANISOU  312  O   LEU A  52     5339   4716   5717    295  -1163   -998       O  
-ATOM    313  CB  LEU A  52       2.228   3.755  21.047  1.00 39.58           C  
-ANISOU  313  CB  LEU A  52     4988   4265   5786    299  -1048   -817       C  
-ATOM    314  CG  LEU A  52       1.767   2.998  19.799  1.00 37.24           C  
-ANISOU  314  CG  LEU A  52     4813   3996   5340    300   -910   -786       C  
-ATOM    315  CD1 LEU A  52       1.670   3.944  18.621  1.00 35.76           C  
-ANISOU  315  CD1 LEU A  52     4648   3770   5168    329   -854   -726       C  
-ATOM    316  CD2 LEU A  52       2.703   1.850  19.485  1.00 35.65           C  
-ANISOU  316  CD2 LEU A  52     4636   3740   5169    313   -793   -723       C  
-ATOM    317  N   ALA A  53      -0.534   3.839  22.506  1.00 60.84           N  
-ANISOU  317  N   ALA A  53     7729   7246   8143    270  -1238  -1057       N  
-ATOM    318  CA  ALA A  53      -1.929   3.445  22.664  1.00 60.87           C  
-ANISOU  318  CA  ALA A  53     7769   7392   7968    243  -1248  -1126       C  
-ATOM    319  C   ALA A  53      -2.841   4.659  22.772  1.00 62.35           C  
-ANISOU  319  C   ALA A  53     7913   7641   8137    285  -1339  -1221       C  
-ATOM    320  O   ALA A  53      -4.009   4.595  22.403  1.00 63.02           O  
-ANISOU  320  O   ALA A  53     8018   7809   8116    272  -1335  -1265       O  
-ATOM    321  CB  ALA A  53      -2.092   2.557  23.881  1.00 60.06           C  
-ANISOU  321  CB  ALA A  53     7656   7387   7778    210  -1270  -1144       C  
-ATOM    322  N   ALA A  54      -2.311   5.764  23.284  1.00 42.36           N  
-ANISOU  322  N   ALA A  54     5315   5055   5726    342  -1441  -1259       N  
-ATOM    323  CA  ALA A  54      -3.110   6.968  23.446  1.00 45.41           C  
-ANISOU  323  CA  ALA A  54     5659   5482   6113    401  -1555  -1366       C  
-ATOM    324  C   ALA A  54      -3.330   7.661  22.106  1.00 46.83           C  
-ANISOU  324  C   ALA A  54     5870   5573   6352    401  -1544  -1324       C  
-ATOM    325  O   ALA A  54      -4.315   8.368  21.922  1.00 48.71           O  
-ANISOU  325  O   ALA A  54     6097   5857   6553    433  -1617  -1407       O  
-ATOM    326  CB  ALA A  54      -2.464   7.911  24.437  1.00 47.69           C  
-ANISOU  326  CB  ALA A  54     5880   5719   6521    473  -1704  -1432       C  
-ATOM    327  N   ARG A  55      -2.418   7.450  21.167  1.00 61.35           N  
-ANISOU  327  N   ARG A  55     7747   7289   8274    372  -1450  -1192       N  
-ATOM    328  CA  ARG A  55      -2.557   8.042  19.842  1.00 63.96           C  
-ANISOU  328  CA  ARG A  55     8128   7540   8632    375  -1422  -1125       C  
-ATOM    329  C   ARG A  55      -3.348   7.143  18.894  1.00 63.03           C  
-ANISOU  329  C   ARG A  55     8125   7479   8343    347  -1323  -1112       C  
-ATOM    330  O   ARG A  55      -4.319   7.585  18.286  1.00 64.28           O  
-ANISOU  330  O   ARG A  55     8326   7657   8441    358  -1374  -1155       O  
-ATOM    331  CB  ARG A  55      -1.185   8.369  19.247  1.00 68.04           C  
-ANISOU  331  CB  ARG A  55     8624   7908   9321    371  -1355   -973       C  
-ATOM    332  CG  ARG A  55      -0.455   9.492  19.954  1.00 75.57           C  
-ANISOU  332  CG  ARG A  55     9460   8760  10495    397  -1496   -973       C  
-ATOM    333  CD  ARG A  55       0.878   9.778  19.287  1.00 83.79           C  
-ANISOU  333  CD  ARG A  55    10452   9652  11734    379  -1415   -791       C  
-ATOM    334  NE  ARG A  55       1.780   8.632  19.359  1.00 89.24           N  
-ANISOU  334  NE  ARG A  55    11138  10342  12427    360  -1269   -720       N  
-ATOM    335  CZ  ARG A  55       2.663   8.438  20.334  1.00 91.54           C  
-ANISOU  335  CZ  ARG A  55    11338  10585  12859    360  -1325   -726       C  
-ATOM    336  NH1 ARG A  55       2.763   9.319  21.321  1.00 93.25           N  
-ANISOU  336  NH1 ARG A  55    11471  10748  13211    384  -1528   -804       N  
-ATOM    337  NH2 ARG A  55       3.444   7.365  20.322  1.00 92.34           N  
-ANISOU  337  NH2 ARG A  55    11439  10680  12967    347  -1197   -663       N  
-ATOM    338  N   GLU A  56      -2.927   5.888  18.765  1.00 66.06           N  
-ANISOU  338  N   GLU A  56     8562   7872   8664    316  -1207  -1059       N  
-ATOM    339  CA  GLU A  56      -3.579   4.954  17.852  1.00 64.77           C  
-ANISOU  339  CA  GLU A  56     8519   7735   8354    299  -1140  -1052       C  
-ATOM    340  C   GLU A  56      -5.033   4.716  18.232  1.00 61.29           C  
-ANISOU  340  C   GLU A  56     8070   7408   7808    273  -1225  -1161       C  
-ATOM    341  O   GLU A  56      -5.933   4.881  17.414  1.00 62.88           O  
-ANISOU  341  O   GLU A  56     8336   7612   7944    280  -1262  -1189       O  
-ATOM    342  CB  GLU A  56      -2.843   3.615  17.827  1.00 69.05           C  
-ANISOU  342  CB  GLU A  56     9109   8258   8868    280  -1033   -997       C  
-ATOM    343  CG  GLU A  56      -1.439   3.692  17.274  1.00 77.94           C  
-ANISOU  343  CG  GLU A  56    10239   9280  10095    315   -919   -883       C  
-ATOM    344  CD  GLU A  56      -1.401   4.225  15.853  1.00 84.68           C  
-ANISOU  344  CD  GLU A  56    11187  10079  10910    361   -849   -811       C  
-ATOM    345  OE1 GLU A  56      -1.843   3.502  14.929  1.00 87.14           O  
-ANISOU  345  OE1 GLU A  56    11639  10397  11072    384   -801   -819       O  
-ATOM    346  OE2 GLU A  56      -0.937   5.373  15.665  1.00 88.19           O  
-ANISOU  346  OE2 GLU A  56    11571  10466  11471    377   -856   -743       O  
-ATOM    347  N   VAL A  57      -5.260   4.320  19.477  1.00 44.12           N  
-ANISOU  347  N   VAL A  57     5812   5332   5621    245  -1254  -1212       N  
-ATOM    348  CA  VAL A  57      -6.599   3.938  19.906  1.00 42.22           C  
-ANISOU  348  CA  VAL A  57     5537   5217   5288    213  -1301  -1287       C  
-ATOM    349  C   VAL A  57      -7.459   5.129  20.315  1.00 42.90           C  
-ANISOU  349  C   VAL A  57     5533   5377   5389    260  -1401  -1391       C  
-ATOM    350  O   VAL A  57      -8.464   5.429  19.674  1.00 45.31           O  
-ANISOU  350  O   VAL A  57     5851   5696   5669    267  -1452  -1436       O  
-ATOM    351  CB  VAL A  57      -6.566   2.955  21.089  1.00 38.55           C  
-ANISOU  351  CB  VAL A  57     5020   4848   4780    163  -1274  -1278       C  
-ATOM    352  CG1 VAL A  57      -7.980   2.653  21.544  1.00 37.15           C  
-ANISOU  352  CG1 VAL A  57     4777   4815   4524    126  -1305  -1329       C  
-ATOM    353  CG2 VAL A  57      -5.845   1.679  20.705  1.00 37.18           C  
-ANISOU  353  CG2 VAL A  57     4933   4595   4599    118  -1201  -1189       C  
-ATOM    354  N   PHE A  58      -7.059   5.806  21.383  1.00 52.74           N  
-ANISOU  354  N   PHE A  58     6693   6662   6682    306  -1446  -1440       N  
-ATOM    355  CA  PHE A  58      -7.936   6.773  22.018  1.00 54.67           C  
-ANISOU  355  CA  PHE A  58     6845   7006   6921    370  -1544  -1566       C  
-ATOM    356  C   PHE A  58      -7.871   8.176  21.422  1.00 54.30           C  
-ANISOU  356  C   PHE A  58     6797   6852   6981    436  -1652  -1608       C  
-ATOM    357  O   PHE A  58      -8.737   9.005  21.695  1.00 55.56           O  
-ANISOU  357  O   PHE A  58     6892   7074   7145    499  -1750  -1725       O  
-ATOM    358  CB  PHE A  58      -7.679   6.794  23.523  1.00 56.67           C  
-ANISOU  358  CB  PHE A  58     7024   7368   7141    409  -1562  -1622       C  
-ATOM    359  CG  PHE A  58      -7.880   5.456  24.187  1.00 58.74           C  
-ANISOU  359  CG  PHE A  58     7282   7749   7289    339  -1467  -1568       C  
-ATOM    360  CD1 PHE A  58      -9.154   5.005  24.494  1.00 59.43           C  
-ANISOU  360  CD1 PHE A  58     7306   7999   7275    313  -1434  -1596       C  
-ATOM    361  CD2 PHE A  58      -6.797   4.651  24.506  1.00 60.22           C  
-ANISOU  361  CD2 PHE A  58     7516   7876   7488    297  -1418  -1477       C  
-ATOM    362  CE1 PHE A  58      -9.343   3.778  25.103  1.00 60.90           C  
-ANISOU  362  CE1 PHE A  58     7481   8285   7374    235  -1353  -1517       C  
-ATOM    363  CE2 PHE A  58      -6.984   3.426  25.117  1.00 61.90           C  
-ANISOU  363  CE2 PHE A  58     7731   8181   7606    227  -1350  -1415       C  
-ATOM    364  CZ  PHE A  58      -8.256   2.991  25.414  1.00 62.52           C  
-ANISOU  364  CZ  PHE A  58     7751   8420   7584    191  -1318  -1426       C  
-ATOM    365  N   LYS A  59      -6.852   8.437  20.611  1.00 44.05           N  
-ANISOU  365  N   LYS A  59     5565   5394   5778    425  -1632  -1505       N  
-ATOM    366  CA  LYS A  59      -6.731   9.716  19.914  1.00 44.92           C  
-ANISOU  366  CA  LYS A  59     5683   5381   6002    468  -1730  -1500       C  
-ATOM    367  C   LYS A  59      -6.680  10.887  20.884  1.00 48.55           C  
-ANISOU  367  C   LYS A  59     6045   5838   6564    549  -1886  -1613       C  
-ATOM    368  O   LYS A  59      -7.043  12.013  20.532  1.00 49.89           O  
-ANISOU  368  O   LYS A  59     6199   5939   6817    598  -2016  -1662       O  
-ATOM    369  CB  LYS A  59      -7.886   9.897  18.927  1.00 43.43           C  
-ANISOU  369  CB  LYS A  59     5549   5200   5753    468  -1767  -1530       C  
-ATOM    370  CG  LYS A  59      -7.923   8.850  17.824  1.00 40.33           C  
-ANISOU  370  CG  LYS A  59     5282   4779   5261    410  -1652  -1431       C  
-ATOM    371  CD  LYS A  59      -6.733   9.004  16.896  1.00 40.58           C  
-ANISOU  371  CD  LYS A  59     5402   4669   5346    405  -1574  -1281       C  
-ATOM    372  CE  LYS A  59      -6.385   7.693  16.210  1.00 41.99           C  
-ANISOU  372  CE  LYS A  59     5696   4843   5417    369  -1429  -1196       C  
-ATOM    373  NZ  LYS A  59      -7.538   7.109  15.455  1.00 44.59           N  
-ANISOU  373  NZ  LYS A  59     6123   5204   5617    360  -1458  -1242       N  
-ATOM    374  N   THR A  60      -6.235  10.609  22.106  1.00 41.02           N  
-ANISOU  374  N   THR A  60     5037   4951   5599    571  -1890  -1660       N  
-ATOM    375  CA  THR A  60      -6.082  11.643  23.119  1.00 45.92           C  
-ANISOU  375  CA  THR A  60     5583   5562   6302    669  -2055  -1784       C  
-ATOM    376  C   THR A  60      -5.135  11.218  24.234  1.00 48.26           C  
-ANISOU  376  C   THR A  60     5859   5870   6607    681  -2054  -1781       C  
-ATOM    377  O   THR A  60      -4.968  10.031  24.511  1.00 48.47           O  
-ANISOU  377  O   THR A  60     5913   5977   6526    622  -1923  -1720       O  
-ATOM    378  CB  THR A  60      -7.434  12.057  23.731  1.00 44.96           C  
-ANISOU  378  CB  THR A  60     5404   5603   6075    757  -2131  -1966       C  
-ATOM    379  OG1 THR A  60      -7.199  12.871  24.887  1.00 46.25           O  
-ANISOU  379  OG1 THR A  60     5513   5779   6280    875  -2284  -2105       O  
-ATOM    380  CG2 THR A  60      -8.236  10.829  24.138  1.00 43.96           C  
-ANISOU  380  CG2 THR A  60     5268   5680   5754    713  -1983  -1971       C  
-ATOM    381  N   GLN A  61      -4.523  12.205  24.875  1.00 75.42           N  
-ANISOU  381  N   GLN A  61     9257   9213  10188    761  -2227  -1848       N  
-ATOM    382  CA  GLN A  61      -3.579  11.959  25.952  1.00 77.19           C  
-ANISOU  382  CA  GLN A  61     9468   9417  10442    788  -2277  -1860       C  
-ATOM    383  C   GLN A  61      -4.317  11.882  27.283  1.00 77.60           C  
-ANISOU  383  C   GLN A  61     9512   9669  10305    893  -2328  -2033       C  
-ATOM    384  O   GLN A  61      -3.781  11.394  28.279  1.00 78.30           O  
-ANISOU  384  O   GLN A  61     9617   9800  10333    917  -2340  -2047       O  
-ATOM    385  CB  GLN A  61      -2.552  13.087  26.006  1.00 81.53           C  
-ANISOU  385  CB  GLN A  61     9975   9746  11257    830  -2472  -1851       C  
-ATOM    386  CG  GLN A  61      -1.142  12.640  26.330  1.00 85.10           C  
-ANISOU  386  CG  GLN A  61    10413  10075  11848    786  -2468  -1740       C  
-ATOM    387  CD  GLN A  61      -0.403  12.145  25.109  1.00 86.68           C  
-ANISOU  387  CD  GLN A  61    10612  10163  12160    667  -2298  -1524       C  
-ATOM    388  OE1 GLN A  61      -0.928  11.347  24.334  1.00 88.19           O  
-ANISOU  388  OE1 GLN A  61    10858  10446  12204    603  -2109  -1458       O  
-ATOM    389  NE2 GLN A  61       0.822  12.622  24.927  1.00 89.53           N  
-ANISOU  389  NE2 GLN A  61    10907  10322  12787    644  -2368  -1413       N  
-ATOM    390  N   GLY A  62      -5.555  12.369  27.290  1.00 59.56           N  
-ANISOU  390  N   GLY A  62     7201   7509   7921    962  -2355  -2161       N  
-ATOM    391  CA  GLY A  62      -6.362  12.404  28.495  1.00 57.56           C  
-ANISOU  391  CA  GLY A  62     6924   7470   7476   1084  -2381  -2329       C  
-ATOM    392  C   GLY A  62      -6.457  11.064  29.191  1.00 58.59           C  
-ANISOU  392  C   GLY A  62     7079   7781   7401   1030  -2210  -2264       C  
-ATOM    393  O   GLY A  62      -6.574  10.999  30.415  1.00 62.19           O  
-ANISOU  393  O   GLY A  62     7541   8381   7707   1130  -2239  -2361       O  
-ATOM    394  N   VAL A  63      -6.397   9.992  28.408  1.00 53.11           N  
-ANISOU  394  N   VAL A  63     6409   7074   6698    878  -2042  -2097       N  
-ATOM    395  CA  VAL A  63      -6.543   8.642  28.938  1.00 53.01           C  
-ANISOU  395  CA  VAL A  63     6418   7209   6515    804  -1888  -2011       C  
-ATOM    396  C   VAL A  63      -5.308   8.183  29.694  1.00 54.22           C  
-ANISOU  396  C   VAL A  63     6623   7290   6687    798  -1924  -1955       C  
-ATOM    397  O   VAL A  63      -5.332   7.156  30.374  1.00 52.74           O  
-ANISOU  397  O   VAL A  63     6464   7222   6354    756  -1834  -1893       O  
-ATOM    398  CB  VAL A  63      -6.837   7.634  27.820  1.00 48.97           C  
-ANISOU  398  CB  VAL A  63     5925   6673   6009    653  -1735  -1863       C  
-ATOM    399  CG1 VAL A  63      -8.228   7.863  27.262  1.00 47.63           C  
-ANISOU  399  CG1 VAL A  63     5700   6608   5791    656  -1702  -1918       C  
-ATOM    400  CG2 VAL A  63      -5.786   7.738  26.724  1.00 46.92           C  
-ANISOU  400  CG2 VAL A  63     5714   6178   5936    591  -1747  -1760       C  
-ATOM    401  N   ILE A  64      -4.230   8.952  29.571  1.00 62.08           N  
-ANISOU  401  N   ILE A  64     7627   8082   7880    835  -2067  -1967       N  
-ATOM    402  CA  ILE A  64      -2.968   8.611  30.219  1.00 65.16           C  
-ANISOU  402  CA  ILE A  64     8053   8366   8339    833  -2133  -1917       C  
-ATOM    403  C   ILE A  64      -2.988   8.858  31.723  1.00 70.60           C  
-ANISOU  403  C   ILE A  64     8771   9169   8883    968  -2257  -2052       C  
-ATOM    404  O   ILE A  64      -3.183   9.988  32.180  1.00 70.16           O  
-ANISOU  404  O   ILE A  64     8702   9110   8847   1109  -2424  -2214       O  
-ATOM    405  CB  ILE A  64      -1.790   9.379  29.604  1.00 64.71           C  
-ANISOU  405  CB  ILE A  64     7968   8043   8576    825  -2254  -1871       C  
-ATOM    406  CG1 ILE A  64      -1.480   8.836  28.210  1.00 61.95           C  
-ANISOU  406  CG1 ILE A  64     7614   7589   8334    692  -2096  -1701       C  
-ATOM    407  CG2 ILE A  64      -0.569   9.274  30.495  1.00 63.76           C  
-ANISOU  407  CG2 ILE A  64     7864   7812   8551    858  -2383  -1864       C  
-ATOM    408  CD1 ILE A  64      -0.323   9.524  27.531  1.00 62.02           C  
-ANISOU  408  CD1 ILE A  64     7578   7357   8630    673  -2169  -1614       C  
-ATOM    409  N   LYS A  65      -2.778   7.789  32.484  1.00 71.77           N  
-ANISOU  409  N   LYS A  65     8972   9414   8882    934  -2186  -1985       N  
-ATOM    410  CA  LYS A  65      -2.707   7.872  33.935  1.00 81.38           C  
-ANISOU  410  CA  LYS A  65    10247  10746   9927   1063  -2292  -2089       C  
-ATOM    411  C   LYS A  65      -1.267   7.696  34.397  1.00 83.42           C  
-ANISOU  411  C   LYS A  65    10555  10812  10327   1062  -2437  -2046       C  
-ATOM    412  O   LYS A  65      -0.426   7.204  33.651  1.00 84.48           O  
-ANISOU  412  O   LYS A  65    10669  10772  10658    941  -2395  -1908       O  
-ATOM    413  CB  LYS A  65      -3.602   6.806  34.567  1.00 84.74           C  
-ANISOU  413  CB  LYS A  65    10699  11440  10059   1029  -2113  -2031       C  
-ATOM    414  CG  LYS A  65      -5.043   6.858  34.083  1.00 90.46           C  
-ANISOU  414  CG  LYS A  65    11347  12350  10673   1013  -1961  -2052       C  
-ATOM    415  CD  LYS A  65      -5.578   8.279  34.164  1.00 93.13           C  
-ANISOU  415  CD  LYS A  65    11641  12715  11030   1179  -2087  -2256       C  
-ATOM    416  CE  LYS A  65      -7.005   8.376  33.656  1.00 92.77           C  
-ANISOU  416  CE  LYS A  65    11503  12841  10905   1169  -1952  -2285       C  
-ATOM    417  NZ  LYS A  65      -7.439   9.798  33.578  1.00 92.96           N  
-ANISOU  417  NZ  LYS A  65    11482  12845  10993   1328  -2100  -2487       N  
-ATOM    418  N   TYR A  66      -0.985   8.103  35.628  1.00125.62           N  
-ANISOU  418  N   TYR A  66    15966  16189  15574   1210  -2614  -2172       N  
-ATOM    419  CA  TYR A  66       0.364   8.007  36.172  1.00136.93           C  
-ANISOU  419  CA  TYR A  66    17446  17427  17153   1227  -2796  -2150       C  
-ATOM    420  C   TYR A  66       0.374   7.245  37.489  1.00142.69           C  
-ANISOU  420  C   TYR A  66    18294  18313  17608   1286  -2812  -2156       C  
-ATOM    421  O   TYR A  66      -0.513   7.419  38.321  1.00142.54           O  
-ANISOU  421  O   TYR A  66    18331  18530  17298   1410  -2793  -2264       O  
-ATOM    422  CB  TYR A  66       0.953   9.400  36.373  1.00150.83           C  
-ANISOU  422  CB  TYR A  66    19187  18995  19127   1362  -3084  -2304       C  
-ATOM    423  CG  TYR A  66       0.930  10.239  35.124  1.00119.72           C  
-ANISOU  423  CG  TYR A  66    15135  14900  15455   1306  -3084  -2284       C  
-ATOM    424  CD1 TYR A  66       2.079  10.434  34.375  1.00 86.95           C  
-ANISOU  424  CD1 TYR A  66    10908  10473  11655   1215  -3151  -2168       C  
-ATOM    425  CD2 TYR A  66      -0.246  10.831  34.689  1.00124.43           C  
-ANISOU  425  CD2 TYR A  66    15696  15628  15954   1347  -3012  -2370       C  
-ATOM    426  CE1 TYR A  66       2.058  11.200  33.228  1.00 62.30           C  
-ANISOU  426  CE1 TYR A  66     7691   7219   8760   1162  -3139  -2123       C  
-ATOM    427  CE2 TYR A  66      -0.278  11.598  33.548  1.00 97.71           C  
-ANISOU  427  CE2 TYR A  66    12226  12097  12803   1296  -3025  -2341       C  
-ATOM    428  CZ  TYR A  66       0.875  11.780  32.820  1.00 67.44           C  
-ANISOU  428  CZ  TYR A  66     8331   7997   9296   1202  -3084  -2210       C  
-ATOM    429  OH  TYR A  66       0.835  12.544  31.678  1.00 46.69           O  
-ANISOU  429  OH  TYR A  66     5625   5233   6882   1149  -3086  -2156       O  
-ATOM    430  N   MET A  67       1.384   6.400  37.670  1.00122.03           N  
-ANISOU  430  N   MET A  67    15717  15568  15082   1204  -2843  -2033       N  
-ATOM    431  CA  MET A  67       1.515   5.600  38.881  1.00128.31           C  
-ANISOU  431  CA  MET A  67    16639  16481  15633   1245  -2875  -2008       C  
-ATOM    432  C   MET A  67       2.966   5.539  39.337  1.00149.20           C  
-ANISOU  432  C   MET A  67    19328  18876  18484   1265  -3112  -1998       C  
-ATOM    433  O   MET A  67       3.853   6.089  38.687  1.00155.21           O  
-ANISOU  433  O   MET A  67    20000  19381  19593   1238  -3231  -1996       O  
-ATOM    434  CB  MET A  67       0.967   4.188  38.651  1.00100.85           C  
-ANISOU  434  CB  MET A  67    13170  13156  11994   1085  -2616  -1820       C  
-ATOM    435  CG  MET A  67       1.470   3.521  37.376  1.00 88.82           C  
-ANISOU  435  CG  MET A  67    11561  11455  10733    903  -2499  -1663       C  
-ATOM    436  SD  MET A  67       0.593   2.002  36.942  1.00 63.48           S  
-ANISOU  436  SD  MET A  67     8351   8413   7356    725  -2221  -1472       S  
-ATOM    437  CE  MET A  67       1.387   0.804  38.014  1.00 67.74           C  
-ANISOU  437  CE  MET A  67     9012   8924   7802    693  -2302  -1356       C  
-ATOM    438  N   GLY A  68       3.201   4.875  40.462  1.00147.53           N  
-ANISOU  438  N   GLY A  68    19251  18740  18065   1313  -3184  -1980       N  
-ATOM    439  CA  GLY A  68       4.546   4.723  40.980  1.00163.94           C  
-ANISOU  439  CA  GLY A  68    21379  20583  20327   1335  -3427  -1969       C  
-ATOM    440  C   GLY A  68       4.722   5.286  42.372  1.00189.08           C  
-ANISOU  440  C   GLY A  68    24717  23801  23323   1546  -3698  -2138       C  
-ATOM    441  O   GLY A  68       3.753   5.428  43.117  1.00183.26           O  
-ANISOU  441  O   GLY A  68    24080  23333  22217   1668  -3641  -2225       O  
-ATOM    442  N   PRO A  69       5.970   5.613  42.732  1.00132.17           N  
-ANISOU  442  N   PRO A  69    17527  16320  16371   1601  -3999  -2187       N  
-ATOM    443  CA  PRO A  69       6.262   6.184  44.047  1.00154.17           C  
-ANISOU  443  CA  PRO A  69    20478  19095  19006   1818  -4313  -2365       C  
-ATOM    444  C   PRO A  69       5.631   7.564  44.161  1.00162.74           C  
-ANISOU  444  C   PRO A  69    21559  20237  20037   1999  -4427  -2591       C  
-ATOM    445  O   PRO A  69       5.663   8.331  43.196  1.00163.05           O  
-ANISOU  445  O   PRO A  69    21440  20137  20375   1949  -4424  -2613       O  
-ATOM    446  CB  PRO A  69       7.789   6.290  44.047  1.00178.16           C  
-ANISOU  446  CB  PRO A  69    23470  21763  22458   1796  -4608  -2347       C  
-ATOM    447  CG  PRO A  69       8.157   6.411  42.608  1.00148.52           C  
-ANISOU  447  CG  PRO A  69    19487  17832  19113   1621  -4467  -2228       C  
-ATOM    448  CD  PRO A  69       7.164   5.560  41.870  1.00130.55           C  
-ANISOU  448  CD  PRO A  69    17174  15796  16634   1475  -4069  -2086       C  
-ATOM    449  N   ALA A  70       5.049   7.864  45.318  1.00115.19           N  
-ANISOU  449  N   ALA A  70    15714  14422  13630   2213  -4522  -2754       N  
-ATOM    450  CA  ALA A  70       4.452   9.173  45.550  1.00125.14           C  
-ANISOU  450  CA  ALA A  70    16990  15741  14817   2422  -4661  -3002       C  
-ATOM    451  C   ALA A  70       5.467  10.269  45.248  1.00163.56           C  
-ANISOU  451  C   ALA A  70    21774  20227  20145   2468  -5023  -3117       C  
-ATOM    452  O   ALA A  70       5.110  11.344  44.764  1.00156.96           O  
-ANISOU  452  O   ALA A  70    20847  19334  19457   2531  -5091  -3244       O  
-ATOM    453  CB  ALA A  70       3.954   9.283  46.983  1.00119.65           C  
-ANISOU  453  CB  ALA A  70    16525  15289  13646   2680  -4764  -3171       C  
-ATOM    454  N   GLY A  71       6.735   9.980  45.529  1.00202.00           N  
-ANISOU  454  N   GLY A  71    26664  24826  25260   2431  -5262  -3060       N  
-ATOM    455  CA  GLY A  71       7.814  10.917  45.280  1.00180.58           C  
-ANISOU  455  CA  GLY A  71    23851  21727  23034   2452  -5619  -3131       C  
-ATOM    456  C   GLY A  71       7.752  11.537  43.897  1.00163.23           C  
-ANISOU  456  C   GLY A  71    21416  19395  21210   2306  -5498  -3054       C  
-ATOM    457  O   GLY A  71       8.029  12.723  43.727  1.00177.12           O  
-ANISOU  457  O   GLY A  71    23104  20940  23255   2385  -5764  -3179       O  
-ATOM    458  N   ALA A  72       7.384  10.732  42.906  1.00203.86           N  
-ANISOU  458  N   ALA A  72    26447  24657  26352   2095  -5111  -2845       N  
-ATOM    459  CA  ALA A  72       7.272  11.218  41.536  1.00178.65           C  
-ANISOU  459  CA  ALA A  72    23051  21365  23464   1953  -4960  -2750       C  
-ATOM    460  C   ALA A  72       6.334  10.347  40.707  1.00171.67           C  
-ANISOU  460  C   ALA A  72    22122  20735  22370   1797  -4519  -2596       C  
-ATOM    461  O   ALA A  72       6.739   9.317  40.171  1.00162.64           O  
-ANISOU  461  O   ALA A  72    20924  19569  21303   1625  -4321  -2397       O  
-ATOM    462  CB  ALA A  72       8.644  11.292  40.883  1.00167.87           C  
-ANISOU  462  CB  ALA A  72    21518  19645  22620   1819  -5086  -2605       C  
-ATOM    463  N   LYS A  73       5.079  10.768  40.607  1.00199.31           N  
-ANISOU  463  N   LYS A  73    25643  24468  25617   1867  -4384  -2698       N  
-ATOM    464  CA  LYS A  73       4.105  10.050  39.799  1.00178.89           C  
-ANISOU  464  CA  LYS A  73    23006  22108  22856   1727  -4000  -2567       C  
-ATOM    465  C   LYS A  73       4.368  10.283  38.321  1.00143.97           C  
-ANISOU  465  C   LYS A  73    18410  17513  18780   1561  -3881  -2429       C  
-ATOM    466  O   LYS A  73       4.124  11.369  37.799  1.00153.54           O  
-ANISOU  466  O   LYS A  73    19546  18640  20152   1601  -3966  -2508       O  
-ATOM    467  CB  LYS A  73       2.684  10.487  40.150  1.00121.59           C  
-ANISOU  467  CB  LYS A  73    15803  15143  15253   1863  -3906  -2723       C  
-ATOM    468  CG  LYS A  73       2.233  10.074  41.539  1.00113.90           C  
-ANISOU  468  CG  LYS A  73    15002  14418  13855   2020  -3925  -2821       C  
-ATOM    469  CD  LYS A  73       1.926   8.586  41.602  1.00 93.67           C  
-ANISOU  469  CD  LYS A  73    12476  12052  11062   1872  -3633  -2618       C  
-ATOM    470  CE  LYS A  73       1.403   8.179  42.976  1.00 94.61           C  
-ANISOU  470  CE  LYS A  73    12767  12446  10734   2024  -3623  -2683       C  
-ATOM    471  NZ  LYS A  73       0.796   6.816  42.962  1.00 78.34           N  
-ANISOU  471  NZ  LYS A  73    10716  10614   8435   1872  -3308  -2473       N  
-ATOM    472  N   ASN A  74       4.877   9.257  37.653  1.00173.20           N  
-ANISOU  472  N   ASN A  74    22057  21162  22591   1383  -3690  -2223       N  
-ATOM    473  CA  ASN A  74       5.100   9.320  36.218  1.00142.90           C  
-ANISOU  473  CA  ASN A  74    18073  17198  19024   1232  -3531  -2075       C  
-ATOM    474  C   ASN A  74       4.796   7.981  35.569  1.00119.88           C  
-ANISOU  474  C   ASN A  74    15159  14412  15979   1077  -3212  -1904       C  
-ATOM    475  O   ASN A  74       3.893   7.268  36.005  1.00110.59           O  
-ANISOU  475  O   ASN A  74    14071  13476  14473   1080  -3072  -1914       O  
-ATOM    476  CB  ASN A  74       6.528   9.761  35.915  1.00133.50           C  
-ANISOU  476  CB  ASN A  74    16770  15681  18272   1195  -3718  -2003       C  
-ATOM    477  CG  ASN A  74       6.832  11.145  36.452  1.00150.14           C  
-ANISOU  477  CG  ASN A  74    18863  17619  20564   1337  -4067  -2165       C  
-ATOM    478  OD1 ASN A  74       6.689  12.144  35.746  1.00166.81           O  
-ANISOU  478  OD1 ASN A  74    20881  19628  22873   1333  -4115  -2176       O  
-ATOM    479  ND2 ASN A  74       7.246  11.212  37.713  1.00150.59           N  
-ANISOU  479  ND2 ASN A  74    19025  17637  20557   1469  -4333  -2294       N  
-ATOM    480  N   LEU A  75       5.548   7.636  34.530  1.00115.24           N  
-ANISOU  480  N   LEU A  75    14469  13663  15655    949  -3102  -1743       N  
-ATOM    481  CA  LEU A  75       5.311   6.387  33.825  1.00 92.48           C  
-ANISOU  481  CA  LEU A  75    11593  10874  12672    817  -2826  -1596       C  
-ATOM    482  C   LEU A  75       3.876   6.350  33.320  1.00 89.03           C  
-ANISOU  482  C   LEU A  75    11183  10659  11987    795  -2633  -1620       C  
-ATOM    483  O   LEU A  75       3.007   5.730  33.936  1.00109.26           O  
-ANISOU  483  O   LEU A  75    13829  13434  14252    806  -2556  -1649       O  
-ATOM    484  CB  LEU A  75       5.567   5.195  34.749  1.00102.67           C  
-ANISOU  484  CB  LEU A  75    12982  12230  13799    805  -2832  -1559       C  
-ATOM    485  CG  LEU A  75       5.296   3.807  34.167  1.00 75.85           C  
-ANISOU  485  CG  LEU A  75     9607   8919  10293    676  -2587  -1417       C  
-ATOM    486  CD1 LEU A  75       6.255   3.524  33.029  1.00 41.70           C  
-ANISOU  486  CD1 LEU A  75     5178   4401   6267    591  -2495  -1291       C  
-ATOM    487  CD2 LEU A  75       5.414   2.742  35.239  1.00 86.26           C  
-ANISOU  487  CD2 LEU A  75    11037  10312  11427    673  -2629  -1387       C  
-ATOM    488  N   GLN A  76       3.632   7.030  32.206  1.00116.30           N  
-ANISOU  488  N   GLN A  76    14559  14056  15574    763  -2563  -1598       N  
-ATOM    489  CA  GLN A  76       2.314   7.049  31.595  1.00109.80           C  
-ANISOU  489  CA  GLN A  76    13749  13409  14560    739  -2401  -1620       C  
-ATOM    490  C   GLN A  76       1.783   5.629  31.502  1.00109.16           C  
-ANISOU  490  C   GLN A  76    13726  13480  14269    646  -2198  -1529       C  
-ATOM    491  O   GLN A  76       2.548   4.688  31.311  1.00 96.89           O  
-ANISOU  491  O   GLN A  76    12180  11843  12792    572  -2137  -1414       O  
-ATOM    492  CB  GLN A  76       2.382   7.661  30.197  1.00 84.06           C  
-ANISOU  492  CB  GLN A  76    10413  10029  11497    686  -2328  -1549       C  
-ATOM    493  CG  GLN A  76       3.253   8.894  30.086  1.00 80.75           C  
-ANISOU  493  CG  GLN A  76     9910   9391  11380    734  -2521  -1564       C  
-ATOM    494  CD  GLN A  76       4.715   8.557  29.874  1.00 68.95           C  
-ANISOU  494  CD  GLN A  76     8347   7693  10158    678  -2533  -1428       C  
-ATOM    495  OE1 GLN A  76       5.162   7.453  30.185  1.00 67.04           O  
-ANISOU  495  OE1 GLN A  76     8137   7471   9864    639  -2462  -1369       O  
-ATOM    496  NE2 GLN A  76       5.471   9.511  29.335  1.00 63.17           N  
-ANISOU  496  NE2 GLN A  76     7508   6758   9737    673  -2627  -1368       N  
-ATOM    497  N   SER A  77       0.475   5.467  31.647  1.00 55.10           N  
-ANISOU  497  N   SER A  77     6909   6849   7176    653  -2106  -1579       N  
-ATOM    498  CA  SER A  77      -0.123   4.147  31.503  1.00 54.07           C  
-ANISOU  498  CA  SER A  77     6819   6850   6876    551  -1929  -1480       C  
-ATOM    499  C   SER A  77      -1.610   4.216  31.159  1.00 47.87           C  
-ANISOU  499  C   SER A  77     6016   6254   5920    539  -1815  -1517       C  
-ATOM    500  O   SER A  77      -2.366   4.989  31.746  1.00 55.59           O  
-ANISOU  500  O   SER A  77     6977   7365   6781    637  -1870  -1641       O  
-ATOM    501  CB  SER A  77       0.119   3.290  32.751  1.00 63.60           C  
-ANISOU  501  CB  SER A  77     8095   8137   7932    557  -1967  -1453       C  
-ATOM    502  OG  SER A  77      -0.566   3.789  33.881  1.00 61.86           O  
-ANISOU  502  OG  SER A  77     7905   8098   7500    669  -2037  -1570       O  
-ATOM    503  N   VAL A  78      -2.019   3.385  30.208  1.00 71.25           N  
-ANISOU  503  N   VAL A  78     8980   9219   8874    427  -1668  -1416       N  
-ATOM    504  CA  VAL A  78      -3.378   3.412  29.686  1.00 64.05           C  
-ANISOU  504  CA  VAL A  78     8038   8446   7853    401  -1575  -1438       C  
-ATOM    505  C   VAL A  78      -4.124   2.126  30.035  1.00 55.17           C  
-ANISOU  505  C   VAL A  78     6929   7470   6563    310  -1465  -1348       C  
-ATOM    506  O   VAL A  78      -3.508   1.122  30.390  1.00 52.54           O  
-ANISOU  506  O   VAL A  78     6645   7096   6223    249  -1453  -1249       O  
-ATOM    507  CB  VAL A  78      -3.358   3.594  28.155  1.00 55.22           C  
-ANISOU  507  CB  VAL A  78     6914   7193   6873    352  -1521  -1399       C  
-ATOM    508  CG1 VAL A  78      -4.754   3.848  27.624  1.00 53.62           C  
-ANISOU  508  CG1 VAL A  78     6678   7109   6585    345  -1473  -1446       C  
-ATOM    509  CG2 VAL A  78      -2.431   4.734  27.776  1.00 55.19           C  
-ANISOU  509  CG2 VAL A  78     6888   7018   7065    416  -1619  -1434       C  
-ATOM    510  N   VAL A  79      -5.451   2.165  29.944  1.00 54.96           N  
-ANISOU  510  N   VAL A  79     6851   7607   6424    298  -1399  -1373       N  
-ATOM    511  CA  VAL A  79      -6.275   0.980  30.162  1.00 52.93           C  
-ANISOU  511  CA  VAL A  79     6582   7482   6048    194  -1297  -1265       C  
-ATOM    512  C   VAL A  79      -6.923   0.527  28.854  1.00 51.47           C  
-ANISOU  512  C   VAL A  79     6384   7233   5938    100  -1239  -1216       C  
-ATOM    513  O   VAL A  79      -7.360   1.349  28.048  1.00 53.91           O  
-ANISOU  513  O   VAL A  79     6664   7512   6308    140  -1257  -1296       O  
-ATOM    514  CB  VAL A  79      -7.374   1.234  31.214  1.00 59.92           C  
-ANISOU  514  CB  VAL A  79     7395   8628   6742    251  -1254  -1310       C  
-ATOM    515  CG1 VAL A  79      -8.372   0.079  31.247  1.00 63.68           C  
-ANISOU  515  CG1 VAL A  79     7822   9232   7140    123  -1140  -1172       C  
-ATOM    516  CG2 VAL A  79      -6.753   1.446  32.579  1.00 61.86           C  
-ANISOU  516  CG2 VAL A  79     7689   8949   6866    349  -1313  -1346       C  
-ATOM    517  N   LEU A  80      -6.980  -0.785  28.650  1.00 57.68           N  
-ANISOU  517  N   LEU A  80     7201   7988   6725    -20  -1193  -1087       N  
-ATOM    518  CA  LEU A  80      -7.535  -1.350  27.431  1.00 57.26           C  
-ANISOU  518  CA  LEU A  80     7160   7854   6744   -103  -1170  -1045       C  
-ATOM    519  C   LEU A  80      -8.508  -2.483  27.723  1.00 71.44           C  
-ANISOU  519  C   LEU A  80     8909   9751   8483   -221  -1129   -931       C  
-ATOM    520  O   LEU A  80      -8.118  -3.522  28.252  1.00 77.10           O  
-ANISOU  520  O   LEU A  80     9662  10450   9181   -296  -1126   -817       O  
-ATOM    521  CB  LEU A  80      -6.408  -1.860  26.540  1.00 46.88           C  
-ANISOU  521  CB  LEU A  80     5949   6320   5544   -123  -1187  -1005       C  
-ATOM    522  CG  LEU A  80      -5.628  -0.807  25.764  1.00 35.10           C  
-ANISOU  522  CG  LEU A  80     4487   4700   4150    -33  -1208  -1082       C  
-ATOM    523  CD1 LEU A  80      -4.254  -1.320  25.414  1.00 27.39           C  
-ANISOU  523  CD1 LEU A  80     3582   3552   3272    -32  -1202  -1027       C  
-ATOM    524  CD2 LEU A  80      -6.398  -0.445  24.511  1.00 30.11           C  
-ANISOU  524  CD2 LEU A  80     3866   4034   3541    -31  -1202  -1122       C  
-ATOM    525  N   SER A  81      -9.775  -2.280  27.375  1.00 38.35           N  
-ANISOU  525  N   SER A  81     4630   5656   4286   -243  -1109   -953       N  
-ATOM    526  CA  SER A  81     -10.778  -3.326  27.522  1.00 56.22           C  
-ANISOU  526  CA  SER A  81     6821   7996   6543   -368  -1080   -830       C  
-ATOM    527  C   SER A  81     -10.503  -4.422  26.508  1.00 64.08           C  
-ANISOU  527  C   SER A  81     7912   8784   7651   -463  -1140   -757       C  
-ATOM    528  O   SER A  81      -9.785  -4.201  25.538  1.00 52.22           O  
-ANISOU  528  O   SER A  81     6517   7113   6213   -413  -1181   -824       O  
-ATOM    529  CB  SER A  81     -12.187  -2.768  27.314  1.00 62.59           C  
-ANISOU  529  CB  SER A  81     7490   8937   7354   -359  -1059   -881       C  
-ATOM    530  OG  SER A  81     -12.425  -2.461  25.951  1.00 62.31           O  
-ANISOU  530  OG  SER A  81     7497   8752   7426   -348  -1129   -957       O  
-ATOM    531  N   LYS A  82     -11.071  -5.602  26.737  1.00 61.98           N  
-ANISOU  531  N   LYS A  82     7608   8532   7411   -594  -1148   -616       N  
-ATOM    532  CA  LYS A  82     -10.937  -6.699  25.790  1.00 75.02           C  
-ANISOU  532  CA  LYS A  82     9349   9979   9177   -677  -1237   -561       C  
-ATOM    533  C   LYS A  82     -11.149  -6.145  24.392  1.00 65.41           C  
-ANISOU  533  C   LYS A  82     8191   8641   8022   -613  -1291   -687       C  
-ATOM    534  O   LYS A  82     -10.319  -6.328  23.503  1.00 47.34           O  
-ANISOU  534  O   LYS A  82     6044   6175   5769   -566  -1333   -733       O  
-ATOM    535  CB  LYS A  82     -11.972  -7.790  26.075  1.00103.21           C  
-ANISOU  535  CB  LYS A  82    12822  13588  12805   -831  -1266   -405       C  
-ATOM    536  CG  LYS A  82     -11.865  -8.416  27.451  1.00122.91           C  
-ANISOU  536  CG  LYS A  82    15261  16212  15226   -909  -1208   -244       C  
-ATOM    537  CD  LYS A  82     -10.553  -9.161  27.625  1.00133.18           C  
-ANISOU  537  CD  LYS A  82    16708  17359  16535   -915  -1260   -200       C  
-ATOM    538  CE  LYS A  82     -10.449  -9.764  29.018  1.00150.29           C  
-ANISOU  538  CE  LYS A  82    18839  19651  18615   -990  -1217    -30       C  
-ATOM    539  NZ  LYS A  82      -9.152 -10.465  29.233  1.00155.78           N  
-ANISOU  539  NZ  LYS A  82    19673  20185  19330   -990  -1288      6       N  
-ATOM    540  N   MET A  83     -12.268  -5.451  24.219  1.00 98.59           N  
-ANISOU  540  N   MET A  83    12283  12948  12228   -600  -1286   -739       N  
-ATOM    541  CA  MET A  83     -12.614  -4.834  22.948  1.00 88.46           C  
-ANISOU  541  CA  MET A  83    11054  11566  10992   -538  -1351   -854       C  
-ATOM    542  C   MET A  83     -11.450  -4.011  22.403  1.00 66.21           C  
-ANISOU  542  C   MET A  83     8367   8653   8138   -414  -1332   -952       C  
-ATOM    543  O   MET A  83     -10.920  -4.313  21.339  1.00 50.36           O  
-ANISOU  543  O   MET A  83     6502   6475   6158   -385  -1376   -975       O  
-ATOM    544  CB  MET A  83     -13.850  -3.951  23.117  1.00 90.00           C  
-ANISOU  544  CB  MET A  83    11090  11917  11190   -517  -1339   -912       C  
-ATOM    545  CG  MET A  83     -15.068  -4.683  23.645  1.00104.27           C  
-ANISOU  545  CG  MET A  83    12727  13835  13054   -639  -1338   -798       C  
-ATOM    546  SD  MET A  83     -15.798  -5.751  22.399  1.00111.63           S  
-ANISOU  546  SD  MET A  83    13706  14559  14150   -744  -1508   -756       S  
-ATOM    547  CE  MET A  83     -16.342  -4.533  21.204  1.00104.28           C  
-ANISOU  547  CE  MET A  83    12810  13571  13241   -627  -1589   -933       C  
-ATOM    548  N   ASN A  84     -11.050  -2.978  23.135  1.00 83.12           N  
-ANISOU  548  N   ASN A  84    10456  10902  10222   -335  -1268  -1006       N  
-ATOM    549  CA  ASN A  84      -9.952  -2.125  22.697  1.00 64.69           C  
-ANISOU  549  CA  ASN A  84     8214   8476   7890   -230  -1256  -1076       C  
-ATOM    550  C   ASN A  84      -8.662  -2.895  22.475  1.00 56.03           C  
-ANISOU  550  C   ASN A  84     7236   7234   6817   -235  -1240  -1020       C  
-ATOM    551  O   ASN A  84      -8.038  -2.777  21.426  1.00 42.37           O  
-ANISOU  551  O   ASN A  84     5615   5367   5115   -181  -1241  -1045       O  
-ATOM    552  CB  ASN A  84      -9.716  -0.987  23.687  1.00 58.57           C  
-ANISOU  552  CB  ASN A  84     7356   7826   7072   -150  -1225  -1139       C  
-ATOM    553  CG  ASN A  84     -10.710   0.139  23.519  1.00 60.62           C  
-ANISOU  553  CG  ASN A  84     7530   8174   7330    -90  -1254  -1241       C  
-ATOM    554  OD1 ASN A  84     -11.282   0.317  22.441  1.00 61.95           O  
-ANISOU  554  OD1 ASN A  84     7730   8269   7541    -89  -1304  -1275       O  
-ATOM    555  ND2 ASN A  84     -10.921   0.911  24.581  1.00 59.96           N  
-ANISOU  555  ND2 ASN A  84     7346   8245   7192    -26  -1238  -1302       N  
-ATOM    556  N   PHE A  85      -8.269  -3.684  23.468  1.00 78.43           N  
-ANISOU  556  N   PHE A  85    10051  10109   9639   -291  -1222   -939       N  
-ATOM    557  CA  PHE A  85      -7.055  -4.479  23.373  1.00 64.28           C  
-ANISOU  557  CA  PHE A  85     8356   8180   7887   -293  -1220   -889       C  
-ATOM    558  C   PHE A  85      -6.986  -5.225  22.053  1.00 52.51           C  
-ANISOU  558  C   PHE A  85     6984   6527   6440   -295  -1256   -891       C  
-ATOM    559  O   PHE A  85      -5.987  -5.150  21.340  1.00 35.25           O  
-ANISOU  559  O   PHE A  85     4889   4221   4282   -220  -1227   -916       O  
-ATOM    560  CB  PHE A  85      -6.976  -5.485  24.514  1.00 72.12           C  
-ANISOU  560  CB  PHE A  85     9317   9225   8861   -381  -1230   -783       C  
-ATOM    561  CG  PHE A  85      -5.968  -6.570  24.286  1.00 54.52           C  
-ANISOU  561  CG  PHE A  85     7188   6833   6695   -399  -1260   -728       C  
-ATOM    562  CD1 PHE A  85      -4.629  -6.348  24.544  1.00 40.65           C  
-ANISOU  562  CD1 PHE A  85     5464   5006   4974   -331  -1239   -741       C  
-ATOM    563  CD2 PHE A  85      -6.359  -7.810  23.809  1.00 52.23           C  
-ANISOU  563  CD2 PHE A  85     6950   6447   6448   -479  -1327   -670       C  
-ATOM    564  CE1 PHE A  85      -3.697  -7.338  24.334  1.00 27.99           C  
-ANISOU  564  CE1 PHE A  85     3939   3254   3442   -334  -1267   -701       C  
-ATOM    565  CE2 PHE A  85      -5.433  -8.811  23.597  1.00 39.55           C  
-ANISOU  565  CE2 PHE A  85     5437   4683   4906   -479  -1369   -637       C  
-ATOM    566  CZ  PHE A  85      -4.097  -8.574  23.859  1.00 29.15           C  
-ANISOU  566  CZ  PHE A  85     4147   3312   3617   -402  -1331   -655       C  
-ATOM    567  N   GLU A  86      -8.046  -5.959  21.738  1.00 90.18           N  
-ANISOU  567  N   GLU A  86    11751  11292  11220   -374  -1323   -864       N  
-ATOM    568  CA  GLU A  86      -8.080  -6.726  20.504  1.00 82.86           C  
-ANISOU  568  CA  GLU A  86    10955  10202  10326   -363  -1394   -884       C  
-ATOM    569  C   GLU A  86      -7.851  -5.792  19.326  1.00 71.18           C  
-ANISOU  569  C   GLU A  86     9565   8669   8813   -246  -1366   -977       C  
-ATOM    570  O   GLU A  86      -6.976  -6.021  18.493  1.00 60.09           O  
-ANISOU  570  O   GLU A  86     8288   7144   7401   -165  -1342  -1000       O  
-ATOM    571  CB  GLU A  86      -9.419  -7.448  20.349  1.00102.00           C  
-ANISOU  571  CB  GLU A  86    13339  12626  12791   -466  -1503   -849       C  
-ATOM    572  CG  GLU A  86      -9.380  -8.612  19.371  1.00105.28           C  
-ANISOU  572  CG  GLU A  86    13897  12850  13256   -470  -1623   -856       C  
-ATOM    573  CD  GLU A  86      -8.654  -9.822  19.935  1.00111.99           C  
-ANISOU  573  CD  GLU A  86    14778  13617  14156   -525  -1654   -772       C  
-ATOM    574  OE1 GLU A  86      -8.403  -9.851  21.159  1.00124.17           O  
-ANISOU  574  OE1 GLU A  86    16219  15264  15695   -588  -1594   -686       O  
-ATOM    575  OE2 GLU A  86      -8.336 -10.747  19.158  1.00108.77           O  
-ANISOU  575  OE2 GLU A  86    14506  13037  13786   -494  -1750   -799       O  
-ATOM    576  N   SER A  87      -8.636  -4.724  19.277  1.00 62.93           N  
-ANISOU  576  N   SER A  87     8448   7718   7746   -230  -1365  -1026       N  
-ATOM    577  CA  SER A  87      -8.607  -3.795  18.155  1.00 59.77           C  
-ANISOU  577  CA  SER A  87     8130   7266   7312   -132  -1359  -1097       C  
-ATOM    578  C   SER A  87      -7.225  -3.169  17.951  1.00 56.09           C  
-ANISOU  578  C   SER A  87     7715   6755   6842    -39  -1255  -1094       C  
-ATOM    579  O   SER A  87      -6.768  -3.007  16.820  1.00 56.77           O  
-ANISOU  579  O   SER A  87     7928   6748   6895     43  -1228  -1110       O  
-ATOM    580  CB  SER A  87      -9.656  -2.706  18.362  1.00 60.33           C  
-ANISOU  580  CB  SER A  87     8090   7452   7382   -134  -1388  -1148       C  
-ATOM    581  OG  SER A  87      -9.821  -1.930  17.195  1.00 62.98           O  
-ANISOU  581  OG  SER A  87     8520   7720   7689    -55  -1419  -1206       O  
-ATOM    582  N   PHE A  88      -6.571  -2.823  19.055  1.00 52.93           N  
-ANISOU  582  N   PHE A  88     7214   6421   6477    -50  -1201  -1066       N  
-ATOM    583  CA  PHE A  88      -5.246  -2.203  19.043  1.00 47.57           C  
-ANISOU  583  CA  PHE A  88     6541   5693   5841     23  -1120  -1049       C  
-ATOM    584  C   PHE A  88      -4.192  -3.165  18.506  1.00 47.01           C  
-ANISOU  584  C   PHE A  88     6570   5503   5790     57  -1068  -1009       C  
-ATOM    585  O   PHE A  88      -3.354  -2.795  17.692  1.00 45.49           O  
-ANISOU  585  O   PHE A  88     6436   5239   5610    140   -989   -997       O  
-ATOM    586  CB  PHE A  88      -4.891  -1.772  20.470  1.00 44.40           C  
-ANISOU  586  CB  PHE A  88     6012   5379   5478      2  -1118  -1039       C  
-ATOM    587  CG  PHE A  88      -3.567  -1.067  20.601  1.00 40.86           C  
-ANISOU  587  CG  PHE A  88     5539   4868   5117     66  -1069  -1020       C  
-ATOM    588  CD1 PHE A  88      -3.213  -0.047  19.737  1.00 39.62           C  
-ANISOU  588  CD1 PHE A  88     5400   4654   5000    133  -1035  -1024       C  
-ATOM    589  CD2 PHE A  88      -2.695  -1.400  21.626  1.00 38.90           C  
-ANISOU  589  CD2 PHE A  88     5242   4614   4925     54  -1071   -986       C  
-ATOM    590  CE1 PHE A  88      -2.001   0.613  19.878  1.00 40.27           C  
-ANISOU  590  CE1 PHE A  88     5432   4669   5199    179   -997   -984       C  
-ATOM    591  CE2 PHE A  88      -1.485  -0.746  21.773  1.00 38.40           C  
-ANISOU  591  CE2 PHE A  88     5135   4477   4977    109  -1049   -966       C  
-ATOM    592  CZ  PHE A  88      -1.137   0.263  20.899  1.00 38.08           C  
-ANISOU  592  CZ  PHE A  88     5094   4377   4999    167  -1009   -960       C  
-ATOM    593  N   VAL A  89      -4.248  -4.407  18.971  1.00 43.04           N  
-ANISOU  593  N   VAL A  89     6081   4980   5294     -5  -1111   -982       N  
-ATOM    594  CA  VAL A  89      -3.303  -5.433  18.560  1.00 43.67           C  
-ANISOU  594  CA  VAL A  89     6250   4941   5401     33  -1086   -960       C  
-ATOM    595  C   VAL A  89      -3.444  -5.712  17.074  1.00 45.53           C  
-ANISOU  595  C   VAL A  89     6640   5090   5570    116  -1081  -1004       C  
-ATOM    596  O   VAL A  89      -2.452  -5.851  16.358  1.00 46.07           O  
-ANISOU  596  O   VAL A  89     6784   5083   5638    217   -994  -1004       O  
-ATOM    597  CB  VAL A  89      -3.517  -6.733  19.368  1.00 42.34           C  
-ANISOU  597  CB  VAL A  89     6069   4756   5261    -61  -1172   -919       C  
-ATOM    598  CG1 VAL A  89      -2.858  -7.908  18.682  1.00 42.97           C  
-ANISOU  598  CG1 VAL A  89     6270   4692   5365    -11  -1190   -927       C  
-ATOM    599  CG2 VAL A  89      -2.976  -6.563  20.767  1.00 40.82           C  
-ANISOU  599  CG2 VAL A  89     5763   4629   5116   -107  -1160   -868       C  
-ATOM    600  N   LYS A  90      -4.686  -5.789  16.617  1.00 50.81           N  
-ANISOU  600  N   LYS A  90     7353   5771   6180     82  -1176  -1044       N  
-ATOM    601  CA  LYS A  90      -4.969  -5.973  15.203  1.00 54.35           C  
-ANISOU  601  CA  LYS A  90     7969   6137   6543    169  -1204  -1099       C  
-ATOM    602  C   LYS A  90      -4.257  -4.902  14.367  1.00 54.44           C  
-ANISOU  602  C   LYS A  90     8032   6152   6501    286  -1073  -1096       C  
-ATOM    603  O   LYS A  90      -3.535  -5.218  13.423  1.00 54.81           O  
-ANISOU  603  O   LYS A  90     8209   6130   6488    401  -1000  -1104       O  
-ATOM    604  CB  LYS A  90      -6.480  -5.937  14.969  1.00 57.33           C  
-ANISOU  604  CB  LYS A  90     8351   6535   6895    106  -1345  -1139       C  
-ATOM    605  CG  LYS A  90      -6.905  -6.268  13.558  1.00 62.60           C  
-ANISOU  605  CG  LYS A  90     9213   7101   7472    194  -1428  -1208       C  
-ATOM    606  CD  LYS A  90      -8.413  -6.403  13.464  1.00 68.19           C  
-ANISOU  606  CD  LYS A  90     9898   7806   8204    113  -1604  -1242       C  
-ATOM    607  CE  LYS A  90      -8.854  -6.554  12.015  1.00 72.17           C  
-ANISOU  607  CE  LYS A  90    10613   8200   8608    218  -1713  -1324       C  
-ATOM    608  NZ  LYS A  90      -8.601  -5.310  11.236  1.00 74.97           N  
-ANISOU  608  NZ  LYS A  90    11041   8591   8853    324  -1617  -1337       N  
-ATOM    609  N   ASP A  91      -4.463  -3.640  14.735  1.00 58.24           N  
-ANISOU  609  N   ASP A  91     8406   6715   7007    262  -1043  -1078       N  
-ATOM    610  CA  ASP A  91      -3.796  -2.509  14.097  1.00 58.56           C  
-ANISOU  610  CA  ASP A  91     8462   6754   7034    346   -930  -1043       C  
-ATOM    611  C   ASP A  91      -2.279  -2.665  14.077  1.00 56.93           C  
-ANISOU  611  C   ASP A  91     8239   6505   6886    411   -783   -979       C  
-ATOM    612  O   ASP A  91      -1.645  -2.513  13.035  1.00 57.85           O  
-ANISOU  612  O   ASP A  91     8452   6584   6944    517   -671   -948       O  
-ATOM    613  CB  ASP A  91      -4.168  -1.210  14.821  1.00 60.22           C  
-ANISOU  613  CB  ASP A  91     8527   7043   7310    295   -956  -1036       C  
-ATOM    614  CG  ASP A  91      -3.281  -0.039  14.424  1.00 64.46           C  
-ANISOU  614  CG  ASP A  91     9039   7560   7893    359   -853   -971       C  
-ATOM    615  OD1 ASP A  91      -2.946   0.086  13.224  1.00 66.67           O  
-ANISOU  615  OD1 ASP A  91     9445   7791   8095    443   -775   -935       O  
-ATOM    616  OD2 ASP A  91      -2.908   0.752  15.319  1.00 64.47           O  
-ANISOU  616  OD2 ASP A  91     8897   7591   8009    327   -855   -949       O  
-ATOM    617  N   LEU A  92      -1.698  -2.956  15.235  1.00 54.74           N  
-ANISOU  617  N   LEU A  92     7834   6239   6724    354   -780   -954       N  
-ATOM    618  CA  LEU A  92      -0.251  -3.073  15.352  1.00 52.79           C  
-ANISOU  618  CA  LEU A  92     7537   5945   6576    408   -660   -894       C  
-ATOM    619  C   LEU A  92       0.317  -4.108  14.387  1.00 53.51           C  
-ANISOU  619  C   LEU A  92     7765   5965   6602    512   -586   -906       C  
-ATOM    620  O   LEU A  92       1.313  -3.852  13.709  1.00 54.64           O  
-ANISOU  620  O   LEU A  92     7917   6083   6761    612   -434   -854       O  
-ATOM    621  CB  LEU A  92       0.135  -3.434  16.786  1.00 51.42           C  
-ANISOU  621  CB  LEU A  92     7233   5781   6522    329   -716   -881       C  
-ATOM    622  CG  LEU A  92      -0.055  -2.336  17.835  1.00 48.53           C  
-ANISOU  622  CG  LEU A  92     6726   5483   6229    267   -770   -873       C  
-ATOM    623  CD1 LEU A  92       0.138  -2.871  19.244  1.00 46.51           C  
-ANISOU  623  CD1 LEU A  92     6387   5249   6037    198   -846   -871       C  
-ATOM    624  CD2 LEU A  92       0.915  -1.213  17.556  1.00 49.71           C  
-ANISOU  624  CD2 LEU A  92     6802   5596   6491    323   -682   -812       C  
-ATOM    625  N   LEU A  93      -0.320  -5.274  14.328  1.00 46.67           N  
-ANISOU  625  N   LEU A  93     6998   5063   5671    493   -696   -973       N  
-ATOM    626  CA  LEU A  93       0.193  -6.386  13.537  1.00 48.04           C  
-ANISOU  626  CA  LEU A  93     7308   5155   5790    603   -666  -1013       C  
-ATOM    627  C   LEU A  93      -0.050  -6.183  12.046  1.00 50.84           C  
-ANISOU  627  C   LEU A  93     7844   5500   5972    734   -610  -1049       C  
-ATOM    628  O   LEU A  93       0.884  -6.223  11.247  1.00 53.65           O  
-ANISOU  628  O   LEU A  93     8261   5842   6281    875   -455  -1030       O  
-ATOM    629  CB  LEU A  93      -0.440  -7.705  13.993  1.00 46.93           C  
-ANISOU  629  CB  LEU A  93     7216   4955   5661    534   -842  -1070       C  
-ATOM    630  CG  LEU A  93      -0.219  -8.135  15.450  1.00 43.93           C  
-ANISOU  630  CG  LEU A  93     6692   4579   5422    410   -909  -1024       C  
-ATOM    631  CD1 LEU A  93      -1.112  -9.309  15.809  1.00 40.47           C  
-ANISOU  631  CD1 LEU A  93     6302   4089   4987    317  -1094  -1050       C  
-ATOM    632  CD2 LEU A  93       1.240  -8.474  15.696  1.00 42.04           C  
-ANISOU  632  CD2 LEU A  93     6398   4284   5290    480   -811   -995       C  
-ATOM    633  N   LEU A  94      -1.305  -5.965  11.670  1.00 46.81           N  
-ANISOU  633  N   LEU A  94     7418   5002   5364    697   -736  -1097       N  
-ATOM    634  CA  LEU A  94      -1.665  -5.850  10.259  1.00 48.68           C  
-ANISOU  634  CA  LEU A  94     7859   5220   5416    824   -727  -1142       C  
-ATOM    635  C   LEU A  94      -1.186  -4.558   9.601  1.00 50.29           C  
-ANISOU  635  C   LEU A  94     8062   5484   5563    894   -555  -1056       C  
-ATOM    636  O   LEU A  94      -0.924  -4.535   8.396  1.00 53.93           O  
-ANISOU  636  O   LEU A  94     8692   5938   5861   1042   -464  -1059       O  
-ATOM    637  CB  LEU A  94      -3.177  -5.961  10.086  1.00 45.42           C  
-ANISOU  637  CB  LEU A  94     7524   4788   4947    755   -940  -1215       C  
-ATOM    638  CG  LEU A  94      -3.812  -7.238  10.620  1.00 43.48           C  
-ANISOU  638  CG  LEU A  94     7281   4469   4769    673  -1131  -1278       C  
-ATOM    639  CD1 LEU A  94      -5.312  -7.233  10.359  1.00 41.59           C  
-ANISOU  639  CD1 LEU A  94     7093   4208   4501    606  -1336  -1334       C  
-ATOM    640  CD2 LEU A  94      -3.153  -8.431   9.979  1.00 43.99           C  
-ANISOU  640  CD2 LEU A  94     7504   4433   4776    807  -1137  -1344       C  
-ATOM    641  N   VAL A  95      -1.079  -3.487  10.382  1.00 54.93           N  
-ANISOU  641  N   VAL A  95     8465   6126   6279    793   -520   -977       N  
-ATOM    642  CA  VAL A  95      -0.775  -2.172   9.821  1.00 56.73           C  
-ANISOU  642  CA  VAL A  95     8677   6392   6486    831   -401   -881       C  
-ATOM    643  C   VAL A  95       0.647  -1.695  10.096  1.00 57.69           C  
-ANISOU  643  C   VAL A  95     8649   6524   6747    855   -209   -759       C  
-ATOM    644  O   VAL A  95       1.515  -1.816   9.244  1.00 60.45           O  
-ANISOU  644  O   VAL A  95     9064   6873   7033    979    -32   -698       O  
-ATOM    645  CB  VAL A  95      -1.757  -1.112  10.325  1.00 55.18           C  
-ANISOU  645  CB  VAL A  95     8392   6230   6342    719   -529   -884       C  
-ATOM    646  CG1 VAL A  95      -1.457   0.229   9.677  1.00 55.10           C  
-ANISOU  646  CG1 VAL A  95     8380   6235   6321    757   -433   -777       C  
-ATOM    647  CG2 VAL A  95      -3.186  -1.551  10.041  1.00 56.46           C  
-ANISOU  647  CG2 VAL A  95     8674   6380   6398    692   -721   -995       C  
-ATOM    648  N   ARG A  96       0.881  -1.141  11.279  1.00 58.26           N  
-ANISOU  648  N   ARG A  96     8518   6606   7014    743   -246   -722       N  
-ATOM    649  CA  ARG A  96       2.205  -0.637  11.626  1.00 59.94           C  
-ANISOU  649  CA  ARG A  96     8565   6805   7406    752   -104   -605       C  
-ATOM    650  C   ARG A  96       3.240  -1.749  11.487  1.00 61.01           C  
-ANISOU  650  C   ARG A  96     8709   6909   7564    839     16   -605       C  
-ATOM    651  O   ARG A  96       4.444  -1.495  11.496  1.00 61.87           O  
-ANISOU  651  O   ARG A  96     8694   7002   7812    879    167   -502       O  
-ATOM    652  CB  ARG A  96       2.219  -0.084  13.054  1.00 61.34           C  
-ANISOU  652  CB  ARG A  96     8546   6981   7779    629   -219   -605       C  
-ATOM    653  CG  ARG A  96       0.889   0.490  13.524  1.00 64.55           C  
-ANISOU  653  CG  ARG A  96     8956   7430   8141    544   -396   -681       C  
-ATOM    654  CD  ARG A  96       0.523   1.774  12.795  1.00 66.60           C  
-ANISOU  654  CD  ARG A  96     9241   7694   8371    559   -391   -625       C  
-ATOM    655  NE  ARG A  96       0.657   2.948  13.654  1.00 65.79           N  
-ANISOU  655  NE  ARG A  96     8971   7583   8445    496   -467   -594       N  
-ATOM    656  CZ  ARG A  96       1.769   3.668  13.768  1.00 67.42           C  
-ANISOU  656  CZ  ARG A  96     9049   7735   8831    501   -391   -476       C  
-ATOM    657  NH1 ARG A  96       2.848   3.332  13.076  1.00 69.18           N  
-ANISOU  657  NH1 ARG A  96     9277   7929   9081    566   -206   -366       N  
-ATOM    658  NH2 ARG A  96       1.801   4.720  14.575  1.00 67.69           N  
-ANISOU  658  NH2 ARG A  96     8945   7743   9031    450   -506   -471       N  
-ATOM    659  N   GLN A  97       2.756  -2.981  11.356  1.00 43.67           N  
-ANISOU  659  N   GLN A  97     6649   4694   5250    870    -65   -720       N  
-ATOM    660  CA  GLN A  97       3.612  -4.157  11.251  1.00 45.35           C  
-ANISOU  660  CA  GLN A  97     6887   4863   5481    962      7   -752       C  
-ATOM    661  C   GLN A  97       4.541  -4.301  12.446  1.00 43.50           C  
-ANISOU  661  C   GLN A  97     6448   4595   5486    896      6   -711       C  
-ATOM    662  O   GLN A  97       5.731  -4.567  12.285  1.00 45.35           O  
-ANISOU  662  O   GLN A  97     6611   4802   5818    983    151   -662       O  
-ATOM    663  CB  GLN A  97       4.422  -4.130   9.959  1.00 50.15           C  
-ANISOU  663  CB  GLN A  97     7583   5490   5981   1140    232   -697       C  
-ATOM    664  CG  GLN A  97       3.633  -4.560   8.737  1.00 56.82           C  
-ANISOU  664  CG  GLN A  97     8693   6345   6550   1256    206   -785       C  
-ATOM    665  CD  GLN A  97       4.502  -5.228   7.698  1.00 63.38           C  
-ANISOU  665  CD  GLN A  97     9641   7185   7255   1468    394   -797       C  
-ATOM    666  OE1 GLN A  97       4.466  -6.450   7.541  1.00 66.76           O  
-ANISOU  666  OE1 GLN A  97    10190   7560   7617   1555    319   -927       O  
-ATOM    667  NE2 GLN A  97       5.296  -4.432   6.985  1.00 66.95           N  
-ANISOU  667  NE2 GLN A  97    10055   7703   7680   1559    639   -657       N  
-ATOM    668  N   TYR A  98       3.988  -4.131  13.643  1.00 52.35           N  
-ANISOU  668  N   TYR A  98     7476   5719   6695    753   -158   -733       N  
-ATOM    669  CA  TYR A  98       4.770  -4.222  14.871  1.00 50.77           C  
-ANISOU  669  CA  TYR A  98     7103   5483   6703    687   -198   -701       C  
-ATOM    670  C   TYR A  98       4.820  -5.640  15.427  1.00 50.79           C  
-ANISOU  670  C   TYR A  98     7147   5432   6719    674   -300   -772       C  
-ATOM    671  O   TYR A  98       4.196  -6.555  14.896  1.00 50.07           O  
-ANISOU  671  O   TYR A  98     7210   5322   6491    707   -356   -848       O  
-ATOM    672  CB  TYR A  98       4.208  -3.279  15.939  1.00 49.30           C  
-ANISOU  672  CB  TYR A  98     6807   5337   6587    561   -324   -691       C  
-ATOM    673  CG  TYR A  98       4.697  -1.850  15.838  1.00 48.93           C  
-ANISOU  673  CG  TYR A  98     6639   5295   6656    563   -253   -599       C  
-ATOM    674  CD1 TYR A  98       4.724  -1.029  16.958  1.00 48.58           C  
-ANISOU  674  CD1 TYR A  98     6457   5250   6750    482   -366   -588       C  
-ATOM    675  CD2 TYR A  98       5.122  -1.319  14.624  1.00 48.13           C  
-ANISOU  675  CD2 TYR A  98     6569   5194   6526    650    -85   -517       C  
-ATOM    676  CE1 TYR A  98       5.171   0.275  16.877  1.00 48.09           C  
-ANISOU  676  CE1 TYR A  98     6283   5165   6825    481   -337   -505       C  
-ATOM    677  CE2 TYR A  98       5.567  -0.012  14.533  1.00 47.71           C  
-ANISOU  677  CE2 TYR A  98     6395   5128   6603    636    -34   -408       C  
-ATOM    678  CZ  TYR A  98       5.590   0.780  15.663  1.00 47.90           C  
-ANISOU  678  CZ  TYR A  98     6275   5128   6795    548   -173   -405       C  
-ATOM    679  OH  TYR A  98       6.034   2.082  15.586  1.00 48.17           O  
-ANISOU  679  OH  TYR A  98     6188   5125   6991    533   -158   -299       O  
-ATOM    680  N   ARG A  99       5.575  -5.812  16.502  1.00 54.73           N  
-ANISOU  680  N   ARG A  99     7510   5889   7396    627   -346   -743       N  
-ATOM    681  CA  ARG A  99       5.542  -7.055  17.257  1.00 55.19           C  
-ANISOU  681  CA  ARG A  99     7596   5891   7482    584   -480   -790       C  
-ATOM    682  C   ARG A  99       4.842  -6.772  18.576  1.00 49.52           C  
-ANISOU  682  C   ARG A  99     6816   5220   6778    439   -637   -783       C  
-ATOM    683  O   ARG A  99       4.745  -5.616  18.992  1.00 46.91           O  
-ANISOU  683  O   ARG A  99     6395   4945   6485    399   -635   -752       O  
-ATOM    684  CB  ARG A  99       6.955  -7.598  17.479  1.00 65.05           C  
-ANISOU  684  CB  ARG A  99     8754   7049   8912    656   -426   -765       C  
-ATOM    685  CG  ARG A  99       7.553  -8.211  16.229  1.00 80.74           C  
-ANISOU  685  CG  ARG A  99    10822   9000  10855    820   -278   -796       C  
-ATOM    686  CD  ARG A  99       9.069  -8.250  16.258  1.00 95.01           C  
-ANISOU  686  CD  ARG A  99    12480  10748  12872    912   -154   -745       C  
-ATOM    687  NE  ARG A  99       9.596  -8.831  15.026  1.00108.81           N  
-ANISOU  687  NE  ARG A  99    14307  12486  14548   1095     11   -782       N  
-ATOM    688  CZ  ARG A  99      10.693  -8.411  14.404  1.00117.40           C  
-ANISOU  688  CZ  ARG A  99    15283  13588  15736   1216    233   -711       C  
-ATOM    689  NH1 ARG A  99      11.396  -7.401  14.896  1.00121.88           N  
-ANISOU  689  NH1 ARG A  99    15641  14156  16511   1157    294   -591       N  
-ATOM    690  NH2 ARG A  99      11.086  -9.003  13.286  1.00122.03           N  
-ANISOU  690  NH2 ARG A  99    15962  14187  16216   1402    389   -758       N  
-ATOM    691  N   VAL A 100       4.336  -7.821  19.217  1.00 47.35           N  
-ANISOU  691  N   VAL A 100     6595   4925   6470    367   -775   -809       N  
-ATOM    692  CA  VAL A 100       3.587  -7.668  20.456  1.00 44.11           C  
-ANISOU  692  CA  VAL A 100     6140   4585   6036    238   -905   -792       C  
-ATOM    693  C   VAL A 100       3.957  -8.738  21.468  1.00 43.30           C  
-ANISOU  693  C   VAL A 100     6029   4420   6004    183  -1023   -766       C  
-ATOM    694  O   VAL A 100       4.097  -9.910  21.123  1.00 43.28           O  
-ANISOU  694  O   VAL A 100     6107   4327   6011    204  -1064   -782       O  
-ATOM    695  CB  VAL A 100       2.066  -7.718  20.199  1.00 42.56           C  
-ANISOU  695  CB  VAL A 100     6022   4469   5681    170   -962   -821       C  
-ATOM    696  CG1 VAL A 100       1.317  -8.043  21.475  1.00 39.91           C  
-ANISOU  696  CG1 VAL A 100     5648   4201   5314     42  -1086   -789       C  
-ATOM    697  CG2 VAL A 100       1.589  -6.401  19.614  1.00 41.18           C  
-ANISOU  697  CG2 VAL A 100     5828   4372   5445    197   -888   -838       C  
-ATOM    698  N   GLU A 101       4.133  -8.318  22.715  1.00 47.10           N  
-ANISOU  698  N   GLU A 101     6424   4941   6531    122  -1092   -729       N  
-ATOM    699  CA  GLU A 101       4.345  -9.232  23.825  1.00 47.53           C  
-ANISOU  699  CA  GLU A 101     6482   4954   6622     55  -1222   -688       C  
-ATOM    700  C   GLU A 101       3.250  -8.977  24.842  1.00 48.57           C  
-ANISOU  700  C   GLU A 101     6606   5224   6623    -53  -1298   -657       C  
-ATOM    701  O   GLU A 101       2.976  -7.826  25.180  1.00 48.76           O  
-ANISOU  701  O   GLU A 101     6570   5349   6606    -47  -1272   -676       O  
-ATOM    702  CB  GLU A 101       5.692  -8.968  24.488  1.00 46.83           C  
-ANISOU  702  CB  GLU A 101     6302   4787   6704    102  -1245   -668       C  
-ATOM    703  CG  GLU A 101       6.891  -9.162  23.598  1.00 48.61           C  
-ANISOU  703  CG  GLU A 101     6493   4889   7088    217  -1150   -684       C  
-ATOM    704  CD  GLU A 101       8.170  -8.715  24.277  1.00 50.79           C  
-ANISOU  704  CD  GLU A 101     6643   5087   7569    255  -1182   -658       C  
-ATOM    705  OE1 GLU A 101       8.078  -8.186  25.407  1.00 50.91           O  
-ANISOU  705  OE1 GLU A 101     6620   5142   7581    200  -1291   -640       O  
-ATOM    706  OE2 GLU A 101       9.261  -8.885  23.686  1.00 52.95           O  
-ANISOU  706  OE2 GLU A 101     6852   5258   8007    350  -1102   -657       O  
-ATOM    707  N   VAL A 102       2.614 -10.039  25.324  1.00 38.40           N  
-ANISOU  707  N   VAL A 102     5375   3942   5275   -146  -1391   -605       N  
-ATOM    708  CA  VAL A 102       1.636  -9.901  26.396  1.00 40.00           C  
-ANISOU  708  CA  VAL A 102     5557   4291   5350   -246  -1443   -551       C  
-ATOM    709  C   VAL A 102       2.173 -10.556  27.661  1.00 41.64           C  
-ANISOU  709  C   VAL A 102     5773   4470   5580   -294  -1553   -471       C  
-ATOM    710  O   VAL A 102       2.603 -11.705  27.635  1.00 42.43           O  
-ANISOU  710  O   VAL A 102     5925   4440   5758   -318  -1631   -428       O  
-ATOM    711  CB  VAL A 102       0.293 -10.545  26.030  1.00 38.34           C  
-ANISOU  711  CB  VAL A 102     5387   4133   5049   -339  -1461   -517       C  
-ATOM    712  CG1 VAL A 102      -0.722 -10.285  27.126  1.00 38.07           C  
-ANISOU  712  CG1 VAL A 102     5300   4280   4883   -431  -1475   -450       C  
-ATOM    713  CG2 VAL A 102      -0.209 -10.002  24.712  1.00 38.99           C  
-ANISOU  713  CG2 VAL A 102     5486   4219   5109   -284  -1380   -600       C  
-ATOM    714  N   TYR A 103       2.161  -9.821  28.766  1.00 50.78           N  
-ANISOU  714  N   TYR A 103     6889   5741   6664   -294  -1576   -459       N  
-ATOM    715  CA  TYR A 103       2.634 -10.364  30.035  1.00 54.21           C  
-ANISOU  715  CA  TYR A 103     7351   6161   7087   -330  -1691   -381       C  
-ATOM    716  C   TYR A 103       1.474 -10.705  30.965  1.00 58.70           C  
-ANISOU  716  C   TYR A 103     7938   6899   7465   -435  -1710   -280       C  
-ATOM    717  O   TYR A 103       0.390 -10.131  30.854  1.00 58.39           O  
-ANISOU  717  O   TYR A 103     7859   7020   7306   -455  -1627   -295       O  
-ATOM    718  CB  TYR A 103       3.588  -9.381  30.715  1.00 52.71           C  
-ANISOU  718  CB  TYR A 103     7120   5959   6949   -237  -1733   -438       C  
-ATOM    719  CG  TYR A 103       4.931  -9.273  30.034  1.00 51.08           C  
-ANISOU  719  CG  TYR A 103     6872   5565   6971   -150  -1733   -492       C  
-ATOM    720  CD1 TYR A 103       6.057  -9.866  30.584  1.00 50.74           C  
-ANISOU  720  CD1 TYR A 103     6837   5376   7064   -129  -1851   -462       C  
-ATOM    721  CD2 TYR A 103       5.070  -8.587  28.835  1.00 48.77           C  
-ANISOU  721  CD2 TYR A 103     6525   5243   6761    -85  -1612   -561       C  
-ATOM    722  CE1 TYR A 103       7.284  -9.774  29.968  1.00 50.91           C  
-ANISOU  722  CE1 TYR A 103     6794   5234   7316    -44  -1837   -504       C  
-ATOM    723  CE2 TYR A 103       6.293  -8.490  28.209  1.00 49.26           C  
-ANISOU  723  CE2 TYR A 103     6531   5153   7031     -3  -1583   -587       C  
-ATOM    724  CZ  TYR A 103       7.398  -9.087  28.780  1.00 51.31           C  
-ANISOU  724  CZ  TYR A 103     6779   5276   7441     18  -1690   -561       C  
-ATOM    725  OH  TYR A 103       8.626  -8.996  28.163  1.00 54.07           O  
-ANISOU  725  OH  TYR A 103     7045   5481   8020    105  -1648   -581       O  
-ATOM    726  N   LYS A 104       1.703 -11.648  31.874  1.00 47.54           N  
-ANISOU  726  N   LYS A 104     6579   5452   6031   -501  -1815   -165       N  
-ATOM    727  CA  LYS A 104       0.712 -11.984  32.890  1.00 54.27           C  
-ANISOU  727  CA  LYS A 104     7446   6480   6696   -600  -1820    -34       C  
-ATOM    728  C   LYS A 104       1.342 -12.004  34.276  1.00 60.19           C  
-ANISOU  728  C   LYS A 104     8251   7258   7361   -578  -1920     24       C  
-ATOM    729  O   LYS A 104       2.541 -12.238  34.423  1.00 61.44           O  
-ANISOU  729  O   LYS A 104     8448   7246   7652   -527  -2031     -1       O  
-ATOM    730  CB  LYS A 104       0.050 -13.328  32.588  1.00 52.07           C  
-ANISOU  730  CB  LYS A 104     7192   6140   6451   -739  -1858    102       C  
-ATOM    731  CG  LYS A 104      -0.831 -13.317  31.354  1.00 49.20           C  
-ANISOU  731  CG  LYS A 104     6786   5775   6132   -767  -1781     54       C  
-ATOM    732  CD  LYS A 104      -1.300 -14.712  31.003  1.00 47.25           C  
-ANISOU  732  CD  LYS A 104     6572   5409   5971   -894  -1871    173       C  
-ATOM    733  CE  LYS A 104      -2.044 -14.732  29.673  1.00 44.76           C  
-ANISOU  733  CE  LYS A 104     6236   5049   5721   -899  -1835     99       C  
-ATOM    734  NZ  LYS A 104      -2.245 -16.129  29.153  1.00 44.03           N  
-ANISOU  734  NZ  LYS A 104     6198   4770   5762   -990  -1973    174       N  
-ATOM    735  N   ASN A 105       0.526 -11.747  35.292  1.00 80.59           N  
-ANISOU  735  N   ASN A 105    10839  10063   9719   -605  -1883    100       N  
-ATOM    736  CA  ASN A 105       1.015 -11.732  36.665  1.00 90.01           C  
-ANISOU  736  CA  ASN A 105    12110  11311  10779   -569  -1980    155       C  
-ATOM    737  C   ASN A 105       0.786 -13.062  37.363  1.00 97.58           C  
-ANISOU  737  C   ASN A 105    13141  12262  11673   -702  -2050    374       C  
-ATOM    738  O   ASN A 105      -0.297 -13.642  37.269  1.00 97.86           O  
-ANISOU  738  O   ASN A 105    13140  12400  11643   -825  -1971    510       O  
-ATOM    739  CB  ASN A 105       0.361 -10.607  37.468  1.00 89.67           C  
-ANISOU  739  CB  ASN A 105    12051  11527  10494   -483  -1902     99       C  
-ATOM    740  CG  ASN A 105       0.964 -10.458  38.847  1.00 90.98           C  
-ANISOU  740  CG  ASN A 105    12322  11740  10506   -406  -2022    119       C  
-ATOM    741  OD1 ASN A 105       2.093 -10.881  39.088  1.00 91.14           O  
-ANISOU  741  OD1 ASN A 105    12413  11566  10651   -388  -2180    126       O  
-ATOM    742  ND2 ASN A 105       0.213  -9.855  39.763  1.00 93.02           N  
-ANISOU  742  ND2 ASN A 105    12597  12258  10488   -347  -1954    123       N  
-ATOM    743  N   ARG A 106       1.810 -13.540  38.062  1.00 99.24           N  
-ANISOU  743  N   ARG A 106    13446  12338  11922   -682  -2212    417       N  
-ATOM    744  CA  ARG A 106       1.709 -14.790  38.805  1.00109.30           C  
-ANISOU  744  CA  ARG A 106    14805  13585  13139   -805  -2308    638       C  
-ATOM    745  C   ARG A 106       0.615 -14.697  39.868  1.00113.20           C  
-ANISOU  745  C   ARG A 106    15316  14373  13321   -855  -2208    793       C  
-ATOM    746  O   ARG A 106       0.809 -14.097  40.927  1.00115.54           O  
-ANISOU  746  O   ARG A 106    15685  14807  13408   -757  -2230    775       O  
-ATOM    747  CB  ARG A 106       3.054 -15.142  39.443  1.00116.79           C  
-ANISOU  747  CB  ARG A 106    15859  14342  14174   -749  -2516    635       C  
-ATOM    748  CG  ARG A 106       3.527 -16.558  39.154  1.00127.43           C  
-ANISOU  748  CG  ARG A 106    17251  15446  15722   -854  -2660    753       C  
-ATOM    749  CD  ARG A 106       3.064 -17.541  40.219  1.00137.77           C  
-ANISOU  749  CD  ARG A 106    18658  16821  16868   -985  -2737   1014       C  
-ATOM    750  NE  ARG A 106       3.677 -17.268  41.516  1.00147.04           N  
-ANISOU  750  NE  ARG A 106    19953  18045  17872   -907  -2854   1044       N  
-ATOM    751  CZ  ARG A 106       4.980 -17.365  41.763  1.00150.99           C  
-ANISOU  751  CZ  ARG A 106    20521  18330  18520   -822  -3054    965       C  
-ATOM    752  NH1 ARG A 106       5.818 -17.719  40.797  1.00155.21           N  
-ANISOU  752  NH1 ARG A 106    20997  18600  19374   -800  -3132    855       N  
-ATOM    753  NH2 ARG A 106       5.447 -17.098  42.974  1.00153.73           N  
-ANISOU  753  NH2 ARG A 106    20991  18728  18693   -748  -3178    993       N  
-ATOM    754  N   ALA A 107      -0.536 -15.291  39.570  1.00106.53           N  
-ANISOU  754  N   ALA A 107    14401  13623  12451   -998  -2101    944       N  
-ATOM    755  CA  ALA A 107      -1.686 -15.238  40.465  1.00109.56           C  
-ANISOU  755  CA  ALA A 107    14761  14306  12559  -1054  -1965   1114       C  
-ATOM    756  C   ALA A 107      -2.805 -16.160  39.986  1.00109.86           C  
-ANISOU  756  C   ALA A 107    14700  14366  12676  -1247  -1893   1313       C  
-ATOM    757  O   ALA A 107      -2.552 -17.214  39.403  1.00109.86           O  
-ANISOU  757  O   ALA A 107    14715  14127  12899  -1361  -2018   1392       O  
-ATOM    758  CB  ALA A 107      -2.194 -13.807  40.590  1.00111.02           C  
-ANISOU  758  CB  ALA A 107    14881  14734  12566   -908  -1810    941       C  
-ATOM    759  N   SER A 112      -3.669  -9.904  48.475  1.00142.37           N  
-ANISOU  759  N   SER A 112    19426  20428  14242     37  -1490    885       N  
-ATOM    760  CA  SER A 112      -2.285 -10.238  48.161  1.00140.18           C  
-ANISOU  760  CA  SER A 112    19252  19772  14238      6  -1771    818       C  
-ATOM    761  C   SER A 112      -1.981 -10.024  46.682  1.00134.52           C  
-ANISOU  761  C   SER A 112    18377  18786  13947    -69  -1806    664       C  
-ATOM    762  O   SER A 112      -2.323 -10.855  45.839  1.00134.04           O  
-ANISOU  762  O   SER A 112    18201  18622  14107   -268  -1736    807       O  
-ATOM    763  CB  SER A 112      -1.975 -11.683  48.557  1.00142.34           C  
-ANISOU  763  CB  SER A 112    19623  19936  14523   -179  -1851   1126       C  
-ATOM    764  OG  SER A 112      -2.073 -11.859  49.958  1.00144.58           O  
-ANISOU  764  OG  SER A 112    20089  20442  14402    -96  -1851   1270       O  
-ATOM    765  N   LYS A 113      -1.335  -8.905  46.374  1.00130.63           N  
-ANISOU  765  N   LYS A 113    17886  18177  13569     97  -1923    376       N  
-ATOM    766  CA  LYS A 113      -0.930  -8.612  45.006  1.00123.06           C  
-ANISOU  766  CA  LYS A 113    16795  16967  12995     49  -1958    230       C  
-ATOM    767  C   LYS A 113       0.570  -8.348  44.925  1.00119.87           C  
-ANISOU  767  C   LYS A 113    16474  16255  12817    130  -2222     82       C  
-ATOM    768  O   LYS A 113       1.041  -7.255  45.246  1.00118.52           O  
-ANISOU  768  O   LYS A 113    16346  16069  12618    314  -2339   -130       O  
-ATOM    769  CB  LYS A 113      -1.721  -7.426  44.448  1.00120.45           C  
-ANISOU  769  CB  LYS A 113    16326  16784  12655    147  -1816     38       C  
-ATOM    770  CG  LYS A 113      -1.341  -7.027  43.027  1.00113.52           C  
-ANISOU  770  CG  LYS A 113    15324  15666  12144    109  -1841   -105       C  
-ATOM    771  CD  LYS A 113      -1.347  -8.220  42.081  1.00109.15           C  
-ANISOU  771  CD  LYS A 113    14704  14941  11828   -106  -1802     63       C  
-ATOM    772  CE  LYS A 113      -2.701  -8.911  42.056  1.00107.81           C  
-ANISOU  772  CE  LYS A 113    14448  14983  11531   -247  -1600    261       C  
-ATOM    773  NZ  LYS A 113      -3.798  -7.973  41.703  1.00104.78           N  
-ANISOU  773  NZ  LYS A 113    13931  14810  11072   -183  -1431    148       N  
-ATOM    774  N   GLU A 114       1.316  -9.364  44.502  1.00126.25           N  
-ANISOU  774  N   GLU A 114    17296  16809  13866     -5  -2325    195       N  
-ATOM    775  CA  GLU A 114       2.755  -9.234  44.317  1.00122.92           C  
-ANISOU  775  CA  GLU A 114    16914  16078  13711     53  -2560     77       C  
-ATOM    776  C   GLU A 114       3.081  -9.245  42.833  1.00113.18           C  
-ANISOU  776  C   GLU A 114    15526  14629  12849    -22  -2516      5       C  
-ATOM    777  O   GLU A 114       2.483  -9.996  42.062  1.00112.91           O  
-ANISOU  777  O   GLU A 114    15413  14593  12894   -169  -2382    121       O  
-ATOM    778  CB  GLU A 114       3.503 -10.367  45.022  1.00132.82           C  
-ANISOU  778  CB  GLU A 114    18309  17190  14965    -13  -2737    244       C  
-ATOM    779  CG  GLU A 114       3.056 -10.614  46.450  1.00148.69           C  
-ANISOU  779  CG  GLU A 114    20489  19434  16571     29  -2751    380       C  
-ATOM    780  CD  GLU A 114       1.781 -11.428  46.524  1.00156.84           C  
-ANISOU  780  CD  GLU A 114    21484  20698  17409   -128  -2523    627       C  
-ATOM    781  OE1 GLU A 114       0.717 -10.845  46.821  1.00162.48           O  
-ANISOU  781  OE1 GLU A 114    22158  21715  17862    -72  -2329    618       O  
-ATOM    782  OE2 GLU A 114       1.843 -12.652  46.287  1.00160.84           O  
-ANISOU  782  OE2 GLU A 114    21991  21078  18044   -305  -2546    831       O  
-ATOM    783  N   ASN A 115       4.031  -8.407  42.435  1.00 97.96           N  
-ANISOU  783  N   ASN A 115    13555  12516  11148     85  -2636   -181       N  
-ATOM    784  CA  ASN A 115       4.391  -8.289  41.031  1.00 85.80           C  
-ANISOU  784  CA  ASN A 115    11872  10791   9938     40  -2577   -252       C  
-ATOM    785  C   ASN A 115       5.400  -9.339  40.588  1.00 80.65           C  
-ANISOU  785  C   ASN A 115    11220   9868   9555    -41  -2681   -173       C  
-ATOM    786  O   ASN A 115       6.592  -9.238  40.877  1.00 79.76           O  
-ANISOU  786  O   ASN A 115    11132   9560   9613     28  -2870   -230       O  
-ATOM    787  CB  ASN A 115       4.905  -6.882  40.725  1.00 82.09           C  
-ANISOU  787  CB  ASN A 115    11330  10250   9609    181  -2636   -461       C  
-ATOM    788  CG  ASN A 115       3.823  -5.831  40.852  1.00 78.69           C  
-ANISOU  788  CG  ASN A 115    10870  10065   8962    260  -2517   -561       C  
-ATOM    789  OD1 ASN A 115       2.991  -5.670  39.959  1.00 76.72           O  
-ANISOU  789  OD1 ASN A 115    10520   9901   8731    203  -2336   -566       O  
-ATOM    790  ND2 ASN A 115       3.825  -5.110  41.968  1.00 77.24           N  
-ANISOU  790  ND2 ASN A 115    10781   9993   8573    405  -2634   -652       N  
-ATOM    791  N   ASP A 116       4.904 -10.351  39.888  1.00 84.40           N  
-ANISOU  791  N   ASP A 116    11662  10326  10080   -181  -2569    -50       N  
-ATOM    792  CA  ASP A 116       5.746 -11.409  39.353  1.00 79.43           C  
-ANISOU  792  CA  ASP A 116    11029   9447   9705   -249  -2656     11       C  
-ATOM    793  C   ASP A 116       5.280 -11.733  37.940  1.00 73.56           C  
-ANISOU  793  C   ASP A 116    10184   8661   9106   -324  -2496      5       C  
-ATOM    794  O   ASP A 116       4.663 -12.773  37.696  1.00 72.50           O  
-ANISOU  794  O   ASP A 116    10069   8533   8943   -447  -2455    136       O  
-ATOM    795  CB  ASP A 116       5.674 -12.651  40.241  1.00 83.96           C  
-ANISOU  795  CB  ASP A 116    11728  10014  10160   -346  -2762    205       C  
-ATOM    796  CG  ASP A 116       6.789 -13.639  39.952  1.00 85.87           C  
-ANISOU  796  CG  ASP A 116    11985   9966  10675   -375  -2922    238       C  
-ATOM    797  OD1 ASP A 116       7.841 -13.211  39.431  1.00 88.29           O  
-ANISOU  797  OD1 ASP A 116    12218  10090  11238   -285  -2983    103       O  
-ATOM    798  OD2 ASP A 116       6.620 -14.842  40.255  1.00 88.42           O  
-ANISOU  798  OD2 ASP A 116    12384  10242  10970   -486  -2990    406       O  
-ATOM    799  N   TRP A 117       5.582 -10.820  37.019  1.00 67.13           N  
-ANISOU  799  N   TRP A 117     9266   7794   8446   -247  -2421   -142       N  
-ATOM    800  CA  TRP A 117       5.126 -10.902  35.632  1.00 60.04           C  
-ANISOU  800  CA  TRP A 117     8286   6874   7652   -286  -2265   -174       C  
-ATOM    801  C   TRP A 117       6.067 -11.706  34.736  1.00 57.16           C  
-ANISOU  801  C   TRP A 117     7898   6267   7555   -288  -2301   -180       C  
-ATOM    802  O   TRP A 117       7.281 -11.732  34.942  1.00 58.69           O  
-ANISOU  802  O   TRP A 117     8080   6293   7928   -222  -2419   -214       O  
-ATOM    803  CB  TRP A 117       4.955  -9.497  35.047  1.00 56.55           C  
-ANISOU  803  CB  TRP A 117     7754   6504   7229   -197  -2160   -315       C  
-ATOM    804  CG  TRP A 117       3.960  -8.642  35.771  1.00 54.41           C  
-ANISOU  804  CG  TRP A 117     7494   6475   6706   -172  -2113   -341       C  
-ATOM    805  CD1 TRP A 117       4.174  -7.916  36.909  1.00 53.91           C  
-ANISOU  805  CD1 TRP A 117     7474   6489   6519    -82  -2216   -391       C  
-ATOM    806  CD2 TRP A 117       2.594  -8.409  35.398  1.00 53.06           C  
-ANISOU  806  CD2 TRP A 117     7285   6496   6378   -219  -1960   -333       C  
-ATOM    807  NE1 TRP A 117       3.024  -7.255  37.271  1.00 53.44           N  
-ANISOU  807  NE1 TRP A 117     7409   6672   6222    -60  -2121   -419       N  
-ATOM    808  CE2 TRP A 117       2.040  -7.541  36.362  1.00 52.99           C  
-ANISOU  808  CE2 TRP A 117     7291   6689   6152   -148  -1960   -379       C  
-ATOM    809  CE3 TRP A 117       1.786  -8.853  34.346  1.00 52.01           C  
-ANISOU  809  CE3 TRP A 117     7111   6378   6273   -303  -1837   -300       C  
-ATOM    810  CZ2 TRP A 117       0.719  -7.108  36.303  1.00 52.44           C  
-ANISOU  810  CZ2 TRP A 117     7176   6843   5907   -161  -1824   -388       C  
-ATOM    811  CZ3 TRP A 117       0.473  -8.425  34.292  1.00 51.62           C  
-ANISOU  811  CZ3 TRP A 117     7018   6535   6062   -328  -1721   -302       C  
-ATOM    812  CH2 TRP A 117      -0.047  -7.558  35.262  1.00 52.85           C  
-ANISOU  812  CH2 TRP A 117     7168   6896   6015   -259  -1707   -344       C  
-ATOM    813  N   TYR A 118       5.493 -12.342  33.722  1.00 70.42           N  
-ANISOU  813  N   TYR A 118    11303   5886   9569   1681  -1917   -430       N  
-ATOM    814  CA  TYR A 118       6.261 -13.117  32.757  1.00 65.09           C  
-ANISOU  814  CA  TYR A 118    10404   5277   9050   1474  -1899   -436       C  
-ATOM    815  C   TYR A 118       5.668 -12.939  31.363  1.00 63.64           C  
-ANISOU  815  C   TYR A 118     9987   5234   8960   1425  -1766   -351       C  
-ATOM    816  O   TYR A 118       4.517 -12.523  31.219  1.00 61.53           O  
-ANISOU  816  O   TYR A 118     9716   5040   8623   1540  -1645   -290       O  
-ATOM    817  CB  TYR A 118       6.225 -14.589  33.136  1.00 59.26           C  
-ANISOU  817  CB  TYR A 118     9680   4589   8248   1398  -1776   -515       C  
-ATOM    818  CG  TYR A 118       4.825 -15.150  33.194  1.00 53.26           C  
-ANISOU  818  CG  TYR A 118     8927   3931   7378   1470  -1549   -505       C  
-ATOM    819  CD1 TYR A 118       4.360 -16.005  32.209  1.00 49.52           C  
-ANISOU  819  CD1 TYR A 118     8273   3583   6958   1353  -1387   -495       C  
-ATOM    820  CD2 TYR A 118       3.962 -14.814  34.231  1.00 52.70           C  
-ANISOU  820  CD2 TYR A 118     9051   3824   7149   1667  -1503   -494       C  
-ATOM    821  CE1 TYR A 118       3.082 -16.522  32.255  1.00 47.34           C  
-ANISOU  821  CE1 TYR A 118     7994   3387   6607   1414  -1201   -468       C  
-ATOM    822  CE2 TYR A 118       2.679 -15.324  34.287  1.00 50.59           C  
-ANISOU  822  CE2 TYR A 118     8768   3652   6801   1748  -1294   -452       C  
-ATOM    823  CZ  TYR A 118       2.245 -16.181  33.294  1.00 48.04           C  
-ANISOU  823  CZ  TYR A 118     8247   3447   6559   1613  -1151   -434       C  
-ATOM    824  OH  TYR A 118       0.969 -16.698  33.340  1.00 46.09           O  
-ANISOU  824  OH  TYR A 118     7970   3289   6253   1689   -964   -367       O  
-ATOM    825  N   LEU A 119       6.450 -13.254  30.336  1.00 64.09           N  
-ANISOU  825  N   LEU A 119     9849   5334   9170   1270  -1785   -330       N  
-ATOM    826  CA  LEU A 119       5.954 -13.165  28.969  1.00 61.61           C  
-ANISOU  826  CA  LEU A 119     9317   5152   8940   1225  -1665   -248       C  
-ATOM    827  C   LEU A 119       5.039 -14.352  28.688  1.00 58.50           C  
-ANISOU  827  C   LEU A 119     8886   4866   8474   1187  -1453   -282       C  
-ATOM    828  O   LEU A 119       5.489 -15.492  28.626  1.00 57.48           O  
-ANISOU  828  O   LEU A 119     8747   4744   8347   1067  -1415   -360       O  
-ATOM    829  CB  LEU A 119       7.116 -13.112  27.974  1.00 66.23           C  
-ANISOU  829  CB  LEU A 119     9721   5741   9701   1098  -1753   -201       C  
-ATOM    830  CG  LEU A 119       6.802 -12.773  26.512  1.00 68.44           C  
-ANISOU  830  CG  LEU A 119     9772   6151  10082   1073  -1671    -90       C  
-ATOM    831  CD1 LEU A 119       5.522 -11.965  26.393  1.00 73.00           C  
-ANISOU  831  CD1 LEU A 119    10325   6839  10573   1185  -1592    -23       C  
-ATOM    832  CD2 LEU A 119       7.966 -12.031  25.872  1.00 70.83           C  
-ANISOU  832  CD2 LEU A 119     9934   6419  10559   1023  -1826      1       C  
-ATOM    833  N   ALA A 120       3.747 -14.078  28.539  1.00 38.68           N  
-ANISOU  833  N   ALA A 120     6328   2509   5860   1257  -1323   -219       N  
-ATOM    834  CA  ALA A 120       2.759 -15.131  28.327  1.00 37.47           C  
-ANISOU  834  CA  ALA A 120     6083   2582   5572   1162  -1139   -233       C  
-ATOM    835  C   ALA A 120       2.717 -15.618  26.876  1.00 37.08           C  
-ANISOU  835  C   ALA A 120     5777   2770   5543    970  -1066   -206       C  
-ATOM    836  O   ALA A 120       2.522 -16.809  26.629  1.00 36.75           O  
-ANISOU  836  O   ALA A 120     5692   2829   5441    839   -984   -259       O  
-ATOM    837  CB  ALA A 120       1.382 -14.664  28.775  1.00 37.87           C  
-ANISOU  837  CB  ALA A 120     6156   2754   5478   1296  -1029   -147       C  
-ATOM    838  N   TYR A 121       2.891 -14.701  25.925  1.00 47.51           N  
-ANISOU  838  N   TYR A 121     6938   4172   6941    961  -1103   -123       N  
-ATOM    839  CA  TYR A 121       2.898 -15.056  24.505  1.00 48.62           C  
-ANISOU  839  CA  TYR A 121     6848   4528   7099    807  -1041    -91       C  
-ATOM    840  C   TYR A 121       3.238 -13.869  23.610  1.00 49.06           C  
-ANISOU  840  C   TYR A 121     6746   4632   7263    833  -1103      7       C  
-ATOM    841  O   TYR A 121       3.208 -12.718  24.047  1.00 49.10           O  
-ANISOU  841  O   TYR A 121     6806   4540   7311    964  -1182     63       O  
-ATOM    842  CB  TYR A 121       1.559 -15.664  24.081  1.00 49.08           C  
-ANISOU  842  CB  TYR A 121     6797   4840   7011    722   -887    -58       C  
-ATOM    843  CG  TYR A 121       0.382 -14.742  24.269  1.00 51.17           C  
-ANISOU  843  CG  TYR A 121     7020   5219   7202    827   -820     52       C  
-ATOM    844  CD1 TYR A 121      -0.371 -14.773  25.433  1.00 52.51           C  
-ANISOU  844  CD1 TYR A 121     7339   5340   7273    947   -771     65       C  
-ATOM    845  CD2 TYR A 121       0.021 -13.838  23.281  1.00 53.50           C  
-ANISOU  845  CD2 TYR A 121     7129   5677   7521    820   -798    152       C  
-ATOM    846  CE1 TYR A 121      -1.450 -13.928  25.607  1.00 53.97           C  
-ANISOU  846  CE1 TYR A 121     7491   5638   7377   1066   -698    186       C  
-ATOM    847  CE2 TYR A 121      -1.060 -12.988  23.452  1.00 53.64           C  
-ANISOU  847  CE2 TYR A 121     7111   5805   7465    922   -730    260       C  
-ATOM    848  CZ  TYR A 121      -1.785 -13.040  24.616  1.00 53.56           C  
-ANISOU  848  CZ  TYR A 121     7256   5745   7350   1049   -678    281       C  
-ATOM    849  OH  TYR A 121      -2.854 -12.203  24.788  1.00 54.27           O  
-ANISOU  849  OH  TYR A 121     7316   5951   7354   1172   -597    406       O  
-ATOM    850  N   LYS A 122       3.557 -14.163  22.352  1.00 51.85           N  
-ANISOU  850  N   LYS A 122     6912   5133   7654    719  -1071     32       N  
-ATOM    851  CA  LYS A 122       3.973 -13.145  21.394  1.00 51.15           C  
-ANISOU  851  CA  LYS A 122     6648   5106   7680    736  -1122    134       C  
-ATOM    852  C   LYS A 122       3.054 -13.125  20.179  1.00 51.91           C  
-ANISOU  852  C   LYS A 122     6532   5492   7699    658   -998    194       C  
-ATOM    853  O   LYS A 122       2.202 -13.997  20.016  1.00 51.90           O  
-ANISOU  853  O   LYS A 122     6520   5633   7566    571   -889    161       O  
-ATOM    854  CB  LYS A 122       5.402 -13.418  20.921  1.00 50.36           C  
-ANISOU  854  CB  LYS A 122     6510   4906   7720    700  -1208    137       C  
-ATOM    855  CG  LYS A 122       6.450 -13.501  22.016  1.00 49.59           C  
-ANISOU  855  CG  LYS A 122     6606   4514   7722    755  -1346     91       C  
-ATOM    856  CD  LYS A 122       7.807 -13.870  21.421  1.00 51.02           C  
-ANISOU  856  CD  LYS A 122     6716   4636   8035    711  -1406    126       C  
-ATOM    857  CE  LYS A 122       8.964 -13.584  22.378  1.00 52.57           C  
-ANISOU  857  CE  LYS A 122     7061   4529   8384    771  -1583    137       C  
-ATOM    858  NZ  LYS A 122       9.053 -14.534  23.520  1.00 52.76           N  
-ANISOU  858  NZ  LYS A 122     7316   4393   8338    761  -1582      0       N  
-ATOM    859  N   ALA A 123       3.245 -12.125  19.325  1.00 49.88           N  
-ANISOU  859  N   ALA A 123     6105   5315   7533    684  -1027    293       N  
-ATOM    860  CA  ALA A 123       2.559 -12.047  18.039  1.00 51.84           C  
-ANISOU  860  CA  ALA A 123     6139   5828   7730    611   -923    355       C  
-ATOM    861  C   ALA A 123       3.275 -11.047  17.135  1.00 52.53           C  
-ANISOU  861  C   ALA A 123     6049   5945   7964    651   -987    456       C  
-ATOM    862  O   ALA A 123       3.684  -9.977  17.582  1.00 54.00           O  
-ANISOU  862  O   ALA A 123     6256   5998   8264    749  -1098    513       O  
-ATOM    863  CB  ALA A 123       1.098 -11.656  18.225  1.00 51.47           C  
-ANISOU  863  CB  ALA A 123     6065   5928   7563    624   -828    397       C  
-ATOM    864  N   SER A 124       3.444 -11.407  15.869  1.00 61.67           N  
-ANISOU  864  N   SER A 124     7043   7268   9120    583   -927    485       N  
-ATOM    865  CA  SER A 124       4.056 -10.509  14.899  1.00 62.22           C  
-ANISOU  865  CA  SER A 124     6916   7400   9324    625   -966    600       C  
-ATOM    866  C   SER A 124       3.350 -10.697  13.562  1.00 61.80           C  
-ANISOU  866  C   SER A 124     6684   7615   9183    558   -844    631       C  
-ATOM    867  O   SER A 124       2.467 -11.543  13.449  1.00 60.79           O  
-ANISOU  867  O   SER A 124     6600   7596   8901    472   -754    567       O  
-ATOM    868  CB  SER A 124       5.551 -10.794  14.776  1.00 63.31           C  
-ANISOU  868  CB  SER A 124     7059   7398   9598    654  -1054    627       C  
-ATOM    869  OG  SER A 124       5.781 -12.100  14.286  1.00 64.99           O  
-ANISOU  869  OG  SER A 124     7307   7670   9715    589   -978    560       O  
-ATOM    870  N   PRO A 125       3.720  -9.905  12.545  1.00 53.54           N  
-ANISOU  870  N   PRO A 125     5435   6670   8237    597   -851    740       N  
-ATOM    871  CA  PRO A 125       3.041 -10.038  11.252  1.00 54.11           C  
-ANISOU  871  CA  PRO A 125     5346   6992   8223    544   -740    770       C  
-ATOM    872  C   PRO A 125       2.973 -11.485  10.782  1.00 54.30           C  
-ANISOU  872  C   PRO A 125     5451   7074   8105    463   -674    683       C  
-ATOM    873  O   PRO A 125       1.984 -11.894  10.175  1.00 55.35           O  
-ANISOU  873  O   PRO A 125     5551   7374   8106    382   -595    663       O  
-ATOM    874  CB  PRO A 125       3.933  -9.231  10.312  1.00 54.51           C  
-ANISOU  874  CB  PRO A 125     5197   7088   8428    622   -776    897       C  
-ATOM    875  CG  PRO A 125       4.527  -8.187  11.181  1.00 53.41           C  
-ANISOU  875  CG  PRO A 125     5076   6764   8455    701   -910    959       C  
-ATOM    876  CD  PRO A 125       4.714  -8.818  12.535  1.00 53.39           C  
-ANISOU  876  CD  PRO A 125     5322   6544   8418    691   -971    854       C  
-ATOM    877  N   GLY A 126       4.025 -12.248  11.065  1.00 45.45           N  
-ANISOU  877  N   GLY A 126     4446   5810   7013    485   -720    641       N  
-ATOM    878  CA  GLY A 126       4.113 -13.629  10.625  1.00 46.93           C  
-ANISOU  878  CA  GLY A 126     4737   6031   7065    427   -674    558       C  
-ATOM    879  C   GLY A 126       3.627 -14.648  11.643  1.00 47.02           C  
-ANISOU  879  C   GLY A 126     4960   5944   6961    342   -678    430       C  
-ATOM    880  O   GLY A 126       3.659 -15.852  11.400  1.00 47.14           O  
-ANISOU  880  O   GLY A 126     5088   5966   6857    285   -659    352       O  
-ATOM    881  N   ASN A 127       3.167 -14.168  12.790  1.00 64.40           N  
-ANISOU  881  N   ASN A 127     7224   8052   9192    345   -706    414       N  
-ATOM    882  CA  ASN A 127       2.728 -15.063  13.848  1.00 64.56           C  
-ANISOU  882  CA  ASN A 127     7436   7975   9117    283   -707    309       C  
-ATOM    883  C   ASN A 127       1.452 -14.577  14.519  1.00 64.11           C  
-ANISOU  883  C   ASN A 127     7380   7971   9007    266   -671    330       C  
-ATOM    884  O   ASN A 127       1.498 -13.808  15.482  1.00 64.19           O  
-ANISOU  884  O   ASN A 127     7443   7862   9085    349   -711    347       O  
-ATOM    885  CB  ASN A 127       3.832 -15.231  14.885  1.00 67.98           C  
-ANISOU  885  CB  ASN A 127     8018   8168   9643    344   -789    260       C  
-ATOM    886  CG  ASN A 127       3.475 -16.234  15.946  1.00 69.32           C  
-ANISOU  886  CG  ASN A 127     8385   8237   9716    287   -785    147       C  
-ATOM    887  OD1 ASN A 127       2.526 -17.002  15.794  1.00 70.56           O  
-ANISOU  887  OD1 ASN A 127     8569   8504   9736    191   -728    109       O  
-ATOM    888  ND2 ASN A 127       4.239 -16.242  17.029  1.00 73.82           N  
-ANISOU  888  ND2 ASN A 127     9094   8590  10363    343   -856    102       N  
-ATOM    889  N   LEU A 128       0.316 -15.034  14.007  1.00 43.37           N  
-ANISOU  889  N   LEU A 128     4704   5518   6256    166   -601    342       N  
-ATOM    890  CA  LEU A 128      -0.975 -14.601  14.516  1.00 42.79           C  
-ANISOU  890  CA  LEU A 128     4603   5529   6126    152   -548    400       C  
-ATOM    891  C   LEU A 128      -1.647 -15.697  15.330  1.00 44.95           C  
-ANISOU  891  C   LEU A 128     5018   5770   6290     74   -531    349       C  
-ATOM    892  O   LEU A 128      -2.829 -15.601  15.648  1.00 47.64           O  
-ANISOU  892  O   LEU A 128     5326   6211   6564     45   -474    420       O  
-ATOM    893  CB  LEU A 128      -1.872 -14.183  13.353  1.00 37.54           C  
-ANISOU  893  CB  LEU A 128     3748   5096   5420     93   -486    493       C  
-ATOM    894  CG  LEU A 128      -1.252 -13.154  12.410  1.00 32.15           C  
-ANISOU  894  CG  LEU A 128     2901   4471   4842    164   -495    551       C  
-ATOM    895  CD1 LEU A 128      -2.273 -12.664  11.401  1.00 27.94           C  
-ANISOU  895  CD1 LEU A 128     2185   4166   4264    110   -426    644       C  
-ATOM    896  CD2 LEU A 128      -0.689 -11.999  13.213  1.00 28.35           C  
-ANISOU  896  CD2 LEU A 128     2433   3852   4487    299   -547    581       C  
-ATOM    897  N   SER A 129      -0.883 -16.734  15.663  1.00 54.41           N  
-ANISOU  897  N   SER A 129     6365   6834   7476     44   -578    241       N  
-ATOM    898  CA  SER A 129      -1.402 -17.898  16.384  1.00 55.91           C  
-ANISOU  898  CA  SER A 129     6690   6985   7569    -39   -574    186       C  
-ATOM    899  C   SER A 129      -2.247 -17.527  17.599  1.00 56.45           C  
-ANISOU  899  C   SER A 129     6803   7029   7618     19   -534    238       C  
-ATOM    900  O   SER A 129      -3.346 -18.045  17.787  1.00 56.90           O  
-ANISOU  900  O   SER A 129     6845   7186   7588    -59   -491    295       O  
-ATOM    901  CB  SER A 129      -0.255 -18.809  16.830  1.00 55.05           C  
-ANISOU  901  CB  SER A 129     6750   6692   7474    -36   -633     58       C  
-ATOM    902  OG  SER A 129       0.158 -19.672  15.787  1.00 55.45           O  
-ANISOU  902  OG  SER A 129     6806   6791   7470   -116   -654     11       O  
-ATOM    903  N   GLN A 130      -1.724 -16.619  18.414  1.00 64.96           N  
-ANISOU  903  N   GLN A 130     7938   7968   8776    166   -556    233       N  
-ATOM    904  CA  GLN A 130      -2.355 -16.257  19.672  1.00 65.10           C  
-ANISOU  904  CA  GLN A 130     8047   7924   8763    268   -524    272       C  
-ATOM    905  C   GLN A 130      -3.541 -15.326  19.477  1.00 64.99           C  
-ANISOU  905  C   GLN A 130     7898   8085   8709    311   -444    420       C  
-ATOM    906  O   GLN A 130      -4.043 -14.750  20.436  1.00 65.30           O  
-ANISOU  906  O   GLN A 130     8006   8084   8720    443   -410    477       O  
-ATOM    907  CB  GLN A 130      -1.329 -15.602  20.592  1.00 66.58           C  
-ANISOU  907  CB  GLN A 130     8378   7877   9043    420   -603    212       C  
-ATOM    908  CG  GLN A 130       0.001 -16.334  20.622  1.00 69.16           C  
-ANISOU  908  CG  GLN A 130     8806   8036   9436    382   -686     89       C  
-ATOM    909  CD  GLN A 130      -0.134 -17.745  21.142  1.00 70.87           C  
-ANISOU  909  CD  GLN A 130     9144   8213   9570    294   -669      3       C  
-ATOM    910  OE1 GLN A 130      -0.711 -17.969  22.204  1.00 74.06           O  
-ANISOU  910  OE1 GLN A 130     9655   8568   9918    342   -639      2       O  
-ATOM    911  NE2 GLN A 130       0.388 -18.708  20.393  1.00 70.64           N  
-ANISOU  911  NE2 GLN A 130     9105   8208   9527    176   -687    -64       N  
-ATOM    912  N   PHE A 131      -3.992 -15.178  18.238  1.00 54.03           N  
-ANISOU  912  N   PHE A 131     6328   6890   7312    213   -412    487       N  
-ATOM    913  CA  PHE A 131      -5.144 -14.326  17.953  1.00 56.35           C  
-ANISOU  913  CA  PHE A 131     6476   7367   7569    238   -328    638       C  
-ATOM    914  C   PHE A 131      -6.026 -14.918  16.864  1.00 61.39           C  
-ANISOU  914  C   PHE A 131     6961   8220   8146     63   -288    712       C  
-ATOM    915  O   PHE A 131      -6.007 -14.468  15.721  1.00 62.51           O  
-ANISOU  915  O   PHE A 131     6956   8479   8315     17   -285    741       O  
-ATOM    916  CB  PHE A 131      -4.698 -12.914  17.576  1.00 49.07           C  
-ANISOU  916  CB  PHE A 131     5474   6440   6732    352   -348    668       C  
-ATOM    917  CG  PHE A 131      -4.042 -12.172  18.702  1.00 42.92           C  
-ANISOU  917  CG  PHE A 131     4855   5448   6006    533   -409    629       C  
-ATOM    918  CD1 PHE A 131      -4.787 -11.366  19.549  1.00 41.12           C  
-ANISOU  918  CD1 PHE A 131     4684   5217   5723    683   -361    717       C  
-ATOM    919  CD2 PHE A 131      -2.680 -12.285  18.921  1.00 38.93           C  
-ANISOU  919  CD2 PHE A 131     4456   4736   5599    562   -521    517       C  
-ATOM    920  CE1 PHE A 131      -4.181 -10.687  20.591  1.00 39.39           C  
-ANISOU  920  CE1 PHE A 131     4649   4778   5539    861   -441    677       C  
-ATOM    921  CE2 PHE A 131      -2.073 -11.608  19.960  1.00 36.49           C  
-ANISOU  921  CE2 PHE A 131     4311   4210   5345    720   -605    488       C  
-ATOM    922  CZ  PHE A 131      -2.824 -10.809  20.797  1.00 36.84           C  
-ANISOU  922  CZ  PHE A 131     4434   4238   5325    871   -573    560       C  
-ATOM    923  N   GLU A 132      -6.806 -15.924  17.240  1.00 62.61           N  
-ANISOU  923  N   GLU A 132     7150   8416   8222    -32   -267    751       N  
-ATOM    924  CA  GLU A 132      -7.645 -16.661  16.307  1.00 67.88           C  
-ANISOU  924  CA  GLU A 132     7706   9253   8833   -217   -266    826       C  
-ATOM    925  C   GLU A 132      -8.511 -15.753  15.439  1.00 69.65           C  
-ANISOU  925  C   GLU A 132     7726   9681   9055   -236   -203    973       C  
-ATOM    926  O   GLU A 132      -8.808 -16.079  14.293  1.00 70.58           O  
-ANISOU  926  O   GLU A 132     7744   9919   9155   -376   -229    999       O  
-ATOM    927  CB  GLU A 132      -8.514 -17.658  17.072  1.00 72.21           C  
-ANISOU  927  CB  GLU A 132     8307   9816   9314   -292   -254    899       C  
-ATOM    928  CG  GLU A 132      -9.586 -18.328  16.240  1.00 78.76           C  
-ANISOU  928  CG  GLU A 132     9013  10818  10093   -487   -271   1027       C  
-ATOM    929  CD  GLU A 132     -10.361 -19.364  17.029  1.00 82.85           C  
-ANISOU  929  CD  GLU A 132     9577  11337  10565   -566   -282   1116       C  
-ATOM    930  OE1 GLU A 132     -11.553 -19.585  16.720  1.00 85.25           O  
-ANISOU  930  OE1 GLU A 132     9750  11799  10842   -681   -270   1307       O  
-ATOM    931  OE2 GLU A 132      -9.775 -19.956  17.962  1.00 84.54           O  
-ANISOU  931  OE2 GLU A 132     9950  11393  10777   -516   -306   1008       O  
-ATOM    932  N   ASP A 133      -8.910 -14.610  15.983  1.00 77.45           N  
-ANISOU  932  N   ASP A 133     8669  10703  10054    -88   -123   1069       N  
-ATOM    933  CA  ASP A 133      -9.769 -13.681  15.253  1.00 79.15           C  
-ANISOU  933  CA  ASP A 133     8693  11116  10265    -92    -50   1218       C  
-ATOM    934  C   ASP A 133      -9.001 -13.018  14.115  1.00 75.73           C  
-ANISOU  934  C   ASP A 133     8168  10706   9901    -95    -86   1144       C  
-ATOM    935  O   ASP A 133      -9.514 -12.867  13.006  1.00 75.41           O  
-ANISOU  935  O   ASP A 133     7969  10830   9853   -195    -68   1214       O  
-ATOM    936  CB  ASP A 133     -10.334 -12.628  16.207  1.00 84.05           C  
-ANISOU  936  CB  ASP A 133     9321  11752  10863     96     44   1335       C  
-ATOM    937  CG  ASP A 133     -10.797 -13.229  17.526  1.00 89.88           C  
-ANISOU  937  CG  ASP A 133    10191  12422  11539    162     80   1388       C  
-ATOM    938  OD1 ASP A 133     -11.904 -13.815  17.558  1.00 93.42           O  
-ANISOU  938  OD1 ASP A 133    10557  13008  11932     69    132   1546       O  
-ATOM    939  OD2 ASP A 133     -10.050 -13.124  18.527  1.00 91.94           O  
-ANISOU  939  OD2 ASP A 133    10634  12488  11810    308     49   1282       O  
-ATOM    940  N   ILE A 134      -7.764 -12.627  14.404  1.00 77.77           N  
-ANISOU  940  N   ILE A 134     8523  10794  10232     19   -143   1015       N  
-ATOM    941  CA  ILE A 134      -6.884 -12.031  13.409  1.00 73.31           C  
-ANISOU  941  CA  ILE A 134     7870  10233   9750     35   -185    959       C  
-ATOM    942  C   ILE A 134      -6.374 -13.088  12.442  1.00 70.86           C  
-ANISOU  942  C   ILE A 134     7565   9930   9427    -98   -242    872       C  
-ATOM    943  O   ILE A 134      -6.439 -12.911  11.230  1.00 69.35           O  
-ANISOU  943  O   ILE A 134     7242   9867   9242   -155   -236    898       O  
-ATOM    944  CB  ILE A 134      -5.674 -11.344  14.071  1.00 73.22           C  
-ANISOU  944  CB  ILE A 134     7963  10021   9837    193   -250    876       C  
-ATOM    945  CG1 ILE A 134      -6.140 -10.225  15.007  1.00 72.75           C  
-ANISOU  945  CG1 ILE A 134     7935   9932   9774    350   -214    955       C  
-ATOM    946  CG2 ILE A 134      -4.724 -10.802  13.015  1.00 71.55           C  
-ANISOU  946  CG2 ILE A 134     7639   9819   9726    207   -297    847       C  
-ATOM    947  CD1 ILE A 134      -5.014  -9.494  15.695  1.00 74.16           C  
-ANISOU  947  CD1 ILE A 134     8236   9892  10051    502   -311    887       C  
-ATOM    948  N   LEU A 135      -5.861 -14.187  12.988  1.00 60.60           N  
-ANISOU  948  N   LEU A 135     6433   8490   8101   -133   -298    769       N  
-ATOM    949  CA  LEU A 135      -5.342 -15.277  12.174  1.00 60.00           C  
-ANISOU  949  CA  LEU A 135     6407   8400   7990   -238   -359    680       C  
-ATOM    950  C   LEU A 135      -6.353 -15.724  11.131  1.00 64.37           C  
-ANISOU  950  C   LEU A 135     6861   9135   8463   -388   -352    756       C  
-ATOM    951  O   LEU A 135      -6.047 -15.767   9.938  1.00 65.08           O  
-ANISOU  951  O   LEU A 135     6891   9291   8545   -418   -374    737       O  
-ATOM    952  CB  LEU A 135      -4.951 -16.469  13.046  1.00 55.50           C  
-ANISOU  952  CB  LEU A 135     6037   7671   7381   -271   -410    577       C  
-ATOM    953  CG  LEU A 135      -4.691 -17.767  12.276  1.00 53.52           C  
-ANISOU  953  CG  LEU A 135     5868   7415   7054   -394   -478    499       C  
-ATOM    954  CD1 LEU A 135      -3.582 -17.581  11.251  1.00 50.62           C  
-ANISOU  954  CD1 LEU A 135     5477   7034   6723   -333   -502    439       C  
-ATOM    955  CD2 LEU A 135      -4.362 -18.915  13.221  1.00 51.88           C  
-ANISOU  955  CD2 LEU A 135     5855   7051   6807   -427   -526    401       C  
-ATOM    956  N   PHE A 136      -7.559 -16.054  11.585  1.00 59.25           N  
-ANISOU  956  N   PHE A 136     6195   8561   7755   -476   -326    858       N  
-ATOM    957  CA  PHE A 136      -8.591 -16.564  10.689  1.00 65.20           C  
-ANISOU  957  CA  PHE A 136     6865   9469   8440   -640   -346    953       C  
-ATOM    958  C   PHE A 136      -9.414 -15.457  10.040  1.00 72.51           C  
-ANISOU  958  C   PHE A 136     7581  10582   9387   -636   -268   1096       C  
-ATOM    959  O   PHE A 136     -10.543 -15.683   9.619  1.00 73.87           O  
-ANISOU  959  O   PHE A 136     7662  10891   9514   -764   -266   1228       O  
-ATOM    960  CB  PHE A 136      -9.514 -17.541  11.419  1.00 59.64           C  
-ANISOU  960  CB  PHE A 136     6223   8761   7675   -757   -372   1028       C  
-ATOM    961  CG  PHE A 136      -8.902 -18.887  11.663  1.00 53.39           C  
-ANISOU  961  CG  PHE A 136     5626   7820   6838   -824   -475    894       C  
-ATOM    962  CD1 PHE A 136      -8.899 -19.847  10.667  1.00 50.80           C  
-ANISOU  962  CD1 PHE A 136     5357   7501   6442   -961   -583    851       C  
-ATOM    963  CD2 PHE A 136      -8.335 -19.195  12.887  1.00 50.33           C  
-ANISOU  963  CD2 PHE A 136     5377   7277   6469   -743   -469    811       C  
-ATOM    964  CE1 PHE A 136      -8.338 -21.090  10.886  1.00 49.74           C  
-ANISOU  964  CE1 PHE A 136     5417   7227   6255  -1015   -682    728       C  
-ATOM    965  CE2 PHE A 136      -7.775 -20.435  13.113  1.00 49.05           C  
-ANISOU  965  CE2 PHE A 136     5390   6981   6264   -806   -559    688       C  
-ATOM    966  CZ  PHE A 136      -7.777 -21.384  12.111  1.00 49.68           C  
-ANISOU  966  CZ  PHE A 136     5528   7076   6272   -942   -664    647       C  
-ATOM    967  N   GLY A 137      -8.846 -14.263   9.957  1.00113.70           N  
-ANISOU  967  N   GLY A 137    12720  15802  14678   -493   -214   1080       N  
-ATOM    968  CA  GLY A 137      -9.504 -13.172   9.266  1.00126.22           C  
-ANISOU  968  CA  GLY A 137    14108  17562  16287   -480   -142   1200       C  
-ATOM    969  C   GLY A 137      -9.209 -13.217   7.780  1.00132.71           C  
-ANISOU  969  C   GLY A 137    14849  18468  17108   -538   -177   1167       C  
-ATOM    970  O   GLY A 137      -9.048 -14.292   7.196  1.00130.54           O  
-ANISOU  970  O   GLY A 137    14664  18163  16772   -639   -258   1103       O  
-ATOM    971  N   ASN A 138      -9.142 -12.039   7.170  1.00138.43           N  
-ANISOU  971  N   ASN A 138    15412  19292  17892   -463   -119   1212       N  
-ATOM    972  CA  ASN A 138      -8.779 -11.904   5.764  1.00146.36           C  
-ANISOU  972  CA  ASN A 138    16325  20380  18905   -478   -137   1187       C  
-ATOM    973  C   ASN A 138      -8.052 -10.585   5.537  1.00148.68           C  
-ANISOU  973  C   ASN A 138    16493  20690  19309   -325    -91   1188       C  
-ATOM    974  O   ASN A 138      -8.663  -9.516   5.568  1.00148.59           O  
-ANISOU  974  O   ASN A 138    16336  20788  19332   -292    -20   1288       O  
-ATOM    975  CB  ASN A 138     -10.016 -12.007   4.869  1.00154.18           C  
-ANISOU  975  CB  ASN A 138    17197  21553  19833   -623   -122   1302       C  
-ATOM    976  CG  ASN A 138      -9.896 -11.171   3.609  1.00160.13           C  
-ANISOU  976  CG  ASN A 138    17781  22439  20622   -587    -86   1327       C  
-ATOM    977  OD1 ASN A 138      -9.032 -11.416   2.765  1.00165.15           O  
-ANISOU  977  OD1 ASN A 138    18447  23044  21258   -541   -127   1241       O  
-ATOM    978  ND2 ASN A 138     -10.772 -10.183   3.471  1.00164.94           N  
-ANISOU  978  ND2 ASN A 138    18210  23202  21258   -595     -1   1455       N  
-ATOM    979  N   ASN A 139      -6.743 -10.668   5.320  1.00153.12           N  
-ANISOU  979  N   ASN A 139    17110  21140  19927   -231   -138   1092       N  
-ATOM    980  CA  ASN A 139      -5.901  -9.480   5.239  1.00155.52           C  
-ANISOU  980  CA  ASN A 139    17305  21426  20359    -85   -124   1106       C  
-ATOM    981  C   ASN A 139      -4.815  -9.591   4.173  1.00157.25           C  
-ANISOU  981  C   ASN A 139    17484  21644  20621    -19   -152   1068       C  
-ATOM    982  O   ASN A 139      -4.031 -10.541   4.171  1.00159.74           O  
-ANISOU  982  O   ASN A 139    17942  21847  20905     -7   -204    986       O  
-ATOM    983  CB  ASN A 139      -5.260  -9.204   6.601  1.00153.86           C  
-ANISOU  983  CB  ASN A 139    17213  21028  20219     15   -161   1068       C  
-ATOM    984  CG  ASN A 139      -4.401 -10.358   7.087  1.00153.93           C  
-ANISOU  984  CG  ASN A 139    17420  20861  20206     10   -230    956       C  
-ATOM    985  OD1 ASN A 139      -4.904 -11.323   7.665  1.00152.63           O  
-ANISOU  985  OD1 ASN A 139    17391  20652  19948    -76   -241    917       O  
-ATOM    986  ND2 ASN A 139      -3.096 -10.264   6.853  1.00152.05           N  
-ANISOU  986  ND2 ASN A 139    17189  20525  20058    106   -278    918       N  
-ATOM    987  N   ASP A 140      -4.772  -8.613   3.272  1.00148.81           N  
-ANISOU  987  N   ASP A 140    16218  20704  19619     36   -111   1139       N  
-ATOM    988  CA  ASP A 140      -3.773  -8.581   2.207  1.00148.01           C  
-ANISOU  988  CA  ASP A 140    16047  20626  19565    127   -121   1137       C  
-ATOM    989  C   ASP A 140      -3.729  -9.896   1.431  1.00146.21           C  
-ANISOU  989  C   ASP A 140    15949  20406  19200     74   -144   1072       C  
-ATOM    990  O   ASP A 140      -2.723 -10.223   0.798  1.00145.96           O  
-ANISOU  990  O   ASP A 140    15942  20341  19175    174   -159   1053       O  
-ATOM    991  CB  ASP A 140      -2.400  -8.248   2.774  1.00148.83           C  
-ANISOU  991  CB  ASP A 140    16175  20569  19804    262   -173   1130       C  
-ATOM    992  N   MET A 141      -4.830 -10.640   1.486  1.00151.68           N  
-ANISOU  992  N   MET A 141    16728  21139  19766    -77   -153   1053       N  
-ATOM    993  CA  MET A 141      -4.936 -11.933   0.818  1.00147.48           C  
-ANISOU  993  CA  MET A 141    16353  20594  19087   -146   -208    991       C  
-ATOM    994  C   MET A 141      -3.789 -12.877   1.194  1.00142.48           C  
-ANISOU  994  C   MET A 141    15920  19788  18429    -74   -264    892       C  
-ATOM    995  O   MET A 141      -2.893 -13.135   0.389  1.00141.60           O  
-ANISOU  995  O   MET A 141    15837  19666  18297     40   -269    874       O  
-ATOM    996  CB  MET A 141      -5.030 -11.751  -0.703  1.00151.22           C  
-ANISOU  996  CB  MET A 141    16727  21213  19518   -114   -186   1028       C  
-ATOM    997  CG  MET A 141      -6.419 -11.359  -1.217  1.00156.04           C  
-ANISOU  997  CG  MET A 141    17210  21988  20090   -246   -159   1108       C  
-ATOM    998  SD  MET A 141      -7.065  -9.795  -0.580  1.00159.28           S  
-ANISOU  998  SD  MET A 141    17378  22505  20637   -247    -63   1218       S  
-ATOM    999  CE  MET A 141      -5.824  -8.641  -1.158  1.00159.77           C  
-ANISOU  999  CE  MET A 141    17264  22596  20846    -42    -14   1243       C  
-ATOM   1000  N   SER A 142      -3.830 -13.386   2.425  1.00 99.97           N  
-ANISOU 1000  N   SER A 142    10672  14271  13041   -130   -299    840       N  
-ATOM   1001  CA  SER A 142      -2.820 -14.318   2.925  1.00 95.95           C  
-ANISOU 1001  CA  SER A 142    10359  13590  12506    -80   -352    744       C  
-ATOM   1002  C   SER A 142      -3.190 -14.875   4.301  1.00 93.75           C  
-ANISOU 1002  C   SER A 142    10219  13190  12212   -171   -386    694       C  
-ATOM   1003  O   SER A 142      -4.327 -14.742   4.759  1.00 94.20           O  
-ANISOU 1003  O   SER A 142    10238  13305  12249   -281   -373    741       O  
-ATOM   1004  CB  SER A 142      -1.443 -13.648   2.985  1.00 93.24           C  
-ANISOU 1004  CB  SER A 142     9947  13179  12300     96   -331    764       C  
-ATOM   1005  OG  SER A 142      -0.464 -14.528   3.514  1.00 89.78           O  
-ANISOU 1005  OG  SER A 142     9692  12576  11844    144   -376    685       O  
-ATOM   1006  N   SER A 144      -2.339 -18.296   6.616  1.00114.48           N  
-ANISOU 1006  N   SER A 144    13478  15370  14649   -306   -562    408       N  
-ATOM   1007  CA  SER A 144      -2.085 -19.670   7.039  1.00119.29           C  
-ANISOU 1007  CA  SER A 144    14316  15850  15159   -365   -634    305       C  
-ATOM   1008  C   SER A 144      -0.598 -19.909   7.276  1.00116.40           C  
-ANISOU 1008  C   SER A 144    14051  15344  14832   -229   -634    231       C  
-ATOM   1009  O   SER A 144      -0.196 -20.413   8.327  1.00112.43           O  
-ANISOU 1009  O   SER A 144    13674  14699  14346   -236   -655    161       O  
-ATOM   1010  CB  SER A 144      -2.626 -20.665   6.006  1.00114.26           C  
-ANISOU 1010  CB  SER A 144    13785  15268  14360   -464   -712    286       C  
-ATOM   1011  OG  SER A 144      -1.961 -20.530   4.761  1.00115.46           O  
-ANISOU 1011  OG  SER A 144    13925  15472  14473   -348   -700    287       O  
-ATOM   1012  N   ILE A 145       0.212 -19.541   6.288  1.00 83.87           N  
-ANISOU 1012  N   ILE A 145     9869  11269  10730   -101   -605    261       N  
-ATOM   1013  CA  ILE A 145       1.662 -19.666   6.382  1.00 79.25           C  
-ANISOU 1013  CA  ILE A 145     9343  10572  10196     45   -595    237       C  
-ATOM   1014  C   ILE A 145       2.293 -18.281   6.306  1.00 65.58           C  
-ANISOU 1014  C   ILE A 145     7399   8873   8645    173   -542    343       C  
-ATOM   1015  O   ILE A 145       2.488 -17.732   5.228  1.00 59.09           O  
-ANISOU 1015  O   ILE A 145     6444   8167   7839    260   -505    423       O  
-ATOM   1016  CB  ILE A 145       2.215 -20.587   5.280  1.00 78.87           C  
-ANISOU 1016  CB  ILE A 145     9432  10536   9999    117   -613    204       C  
-ATOM   1017  CG1 ILE A 145       3.697 -20.314   5.048  1.00 82.25           C  
-ANISOU 1017  CG1 ILE A 145     9828  10914  10508    311   -569    254       C  
-ATOM   1018  CG2 ILE A 145       1.429 -20.409   3.998  1.00 85.09           C  
-ANISOU 1018  CG2 ILE A 145    10149  11487  10696     97   -611    253       C  
-ATOM   1019  CD1 ILE A 145       4.546 -20.589   6.240  1.00 82.68           C  
-ANISOU 1019  CD1 ILE A 145     9972  10795  10646    329   -584    209       C  
-ATOM   1020  N   GLY A 146       2.592 -17.712   7.467  1.00 53.16           N  
-ANISOU 1020  N   GLY A 146     5800   7190   7209    186   -551    348       N  
-ATOM   1021  CA  GLY A 146       3.035 -16.337   7.542  1.00 36.60           C  
-ANISOU 1021  CA  GLY A 146     3511   5103   5292    284   -534    454       C  
-ATOM   1022  C   GLY A 146       4.506 -16.169   7.852  1.00 31.20           C  
-ANISOU 1022  C   GLY A 146     2833   4282   4739    410   -561    492       C  
-ATOM   1023  O   GLY A 146       5.010 -15.049   7.861  1.00 23.05           O  
-ANISOU 1023  O   GLY A 146     1642   3243   3872    494   -572    599       O  
-ATOM   1024  N   VAL A 147       5.208 -17.265   8.115  1.00 43.78           N  
-ANISOU 1024  N   VAL A 147     4606   5762   6267    422   -580    419       N  
-ATOM   1025  CA  VAL A 147       6.647 -17.180   8.351  1.00 40.02           C  
-ANISOU 1025  CA  VAL A 147     4131   5161   5915    542   -602    479       C  
-ATOM   1026  C   VAL A 147       7.414 -18.168   7.485  1.00 51.98           C  
-ANISOU 1026  C   VAL A 147     5737   6697   7315    628   -568    480       C  
-ATOM   1027  O   VAL A 147       6.842 -19.108   6.943  1.00 61.93           O  
-ANISOU 1027  O   VAL A 147     7125   8022   8382    578   -551    394       O  
-ATOM   1028  CB  VAL A 147       7.002 -17.387   9.834  1.00 41.93           C  
-ANISOU 1028  CB  VAL A 147     4508   5194   6228    503   -665    408       C  
-ATOM   1029  CG1 VAL A 147       8.505 -17.439  10.027  1.00 37.09           C  
-ANISOU 1029  CG1 VAL A 147     3906   4448   5737    613   -696    481       C  
-ATOM   1030  CG2 VAL A 147       6.433 -16.266  10.654  1.00 38.05           C  
-ANISOU 1030  CG2 VAL A 147     3935   4667   5855    473   -703    434       C  
-ATOM   1031  N   VAL A 148       8.711 -17.933   7.335  1.00 33.16           N  
-ANISOU 1031  N   VAL A 148     3291   4259   5051    767   -565    597       N  
-ATOM   1032  CA  VAL A 148       9.569 -18.834   6.589  1.00 45.13           C  
-ANISOU 1032  CA  VAL A 148     4900   5787   6460    887   -520    624       C  
-ATOM   1033  C   VAL A 148      10.986 -18.772   7.160  1.00 45.93           C  
-ANISOU 1033  C   VAL A 148     4990   5743   6717    986   -544    725       C  
-ATOM   1034  O   VAL A 148      11.332 -17.839   7.879  1.00 31.57           O  
-ANISOU 1034  O   VAL A 148     3051   3835   5109    977   -604    805       O  
-ATOM   1035  CB  VAL A 148       9.568 -18.483   5.085  1.00 46.37           C  
-ANISOU 1035  CB  VAL A 148     4917   6134   6566   1014   -451    740       C  
-ATOM   1036  CG1 VAL A 148      10.703 -17.533   4.756  1.00 36.01           C  
-ANISOU 1036  CG1 VAL A 148     3384   4838   5462   1177   -434    961       C  
-ATOM   1037  CG2 VAL A 148       9.669 -19.740   4.254  1.00 65.47           C  
-ANISOU 1037  CG2 VAL A 148     7537   8595   8743   1084   -410    678       C  
-ATOM   1038  N   GLY A 149      11.800 -19.773   6.860  1.00 31.78           N  
-ANISOU 1038  N   GLY A 149     3336   3919   4819   1082   -506    730       N  
-ATOM   1039  CA  GLY A 149      13.167 -19.792   7.343  1.00 32.94           C  
-ANISOU 1039  CA  GLY A 149     3469   3936   5109   1179   -520    849       C  
-ATOM   1040  C   GLY A 149      14.133 -20.095   6.221  1.00 45.63           C  
-ANISOU 1040  C   GLY A 149     5037   5637   6665   1392   -434   1014       C  
-ATOM   1041  O   GLY A 149      13.930 -21.039   5.458  1.00 61.81           O  
-ANISOU 1041  O   GLY A 149     7245   7763   8478   1452   -372    941       O  
-ATOM   1042  N   VAL A 150      15.188 -19.298   6.111  1.00 34.53           N  
-ANISOU 1042  N   VAL A 150     3426   4219   5475   1517   -437   1251       N  
-ATOM   1043  CA  VAL A 150      16.103 -19.444   4.989  1.00 40.60           C  
-ANISOU 1043  CA  VAL A 150     4115   5100   6211   1749   -340   1457       C  
-ATOM   1044  C   VAL A 150      17.565 -19.558   5.391  1.00 47.36           C  
-ANISOU 1044  C   VAL A 150     4931   5844   7218   1865   -344   1653       C  
-ATOM   1045  O   VAL A 150      18.177 -18.587   5.836  1.00 47.47           O  
-ANISOU 1045  O   VAL A 150     4740   5789   7507   1862   -419   1834       O  
-ATOM   1046  CB  VAL A 150      15.974 -18.278   3.996  1.00 37.79           C  
-ANISOU 1046  CB  VAL A 150     3476   4914   5967   1847   -310   1640       C  
-ATOM   1047  CG1 VAL A 150      16.917 -18.499   2.834  1.00 36.05           C  
-ANISOU 1047  CG1 VAL A 150     3185   4818   5696   2115   -195   1865       C  
-ATOM   1048  CG2 VAL A 150      14.537 -18.138   3.514  1.00 34.28           C  
-ANISOU 1048  CG2 VAL A 150     3056   4592   5375   1739   -300   1468       C  
-ATOM   1049  N   LYS A 151      18.116 -20.753   5.222  1.00 58.73           N  
-ANISOU 1049  N   LYS A 151     6575   7263   8475   1966   -271   1625       N  
-ATOM   1050  CA  LYS A 151      19.544 -20.973   5.390  1.00 70.53           C  
-ANISOU 1050  CA  LYS A 151     8032   8685  10080   2113   -244   1845       C  
-ATOM   1051  C   LYS A 151      20.130 -21.340   4.031  1.00 77.16           C  
-ANISOU 1051  C   LYS A 151     8850   9695  10773   2394    -99   2032       C  
-ATOM   1052  O   LYS A 151      19.387 -21.565   3.074  1.00 75.27           O  
-ANISOU 1052  O   LYS A 151     8679   9598  10321   2454    -36   1942       O  
-ATOM   1053  CB  LYS A 151      19.805 -22.094   6.401  1.00 72.38           C  
-ANISOU 1053  CB  LYS A 151     8534   8745  10221   2020   -269   1674       C  
-ATOM   1054  CG  LYS A 151      20.987 -21.828   7.319  1.00 77.47           C  
-ANISOU 1054  CG  LYS A 151     9091   9225  11120   2019   -333   1851       C  
-ATOM   1055  CD  LYS A 151      21.270 -22.997   8.246  1.00 80.56           C  
-ANISOU 1055  CD  LYS A 151     9751   9455  11402   1942   -342   1682       C  
-ATOM   1056  CE  LYS A 151      21.878 -24.164   7.491  1.00 84.14           C  
-ANISOU 1056  CE  LYS A 151    10372   9983  11613   2142   -203   1727       C  
-ATOM   1057  NZ  LYS A 151      22.407 -25.200   8.418  1.00 85.10           N  
-ANISOU 1057  NZ  LYS A 151    10718   9942  11676   2086   -212   1620       N  
-ATOM   1058  N   MET A 152      21.456 -21.400   3.944  1.00 88.80           N  
-ANISOU 1058  N   MET A 152    10234  11151  12355   2575    -48   2305       N  
-ATOM   1059  CA  MET A 152      22.109 -21.827   2.708  1.00 98.90           C  
-ANISOU 1059  CA  MET A 152    11512  12587  13477   2882    107   2507       C  
-ATOM   1060  C   MET A 152      23.516 -22.380   2.926  1.00104.69           C  
-ANISOU 1060  C   MET A 152    12265  13256  14255   3052    169   2737       C  
-ATOM   1061  O   MET A 152      24.229 -21.963   3.838  1.00104.89           O  
-ANISOU 1061  O   MET A 152    12162  13147  14544   2956     88   2867       O  
-ATOM   1062  CB  MET A 152      22.135 -20.694   1.678  1.00103.32           C  
-ANISOU 1062  CB  MET A 152    11760  13326  14169   3027    148   2754       C  
-ATOM   1063  CG  MET A 152      22.898 -19.463   2.121  1.00107.15           C  
-ANISOU 1063  CG  MET A 152    11928  13782  15004   2915    105   3007       C  
-ATOM   1064  SD  MET A 152      22.953 -18.206   0.830  1.00113.27           S  
-ANISOU 1064  SD  MET A 152    12377  14793  15868   3002    212   3268       S  
-ATOM   1065  CE  MET A 152      23.812 -19.091  -0.472  1.00115.00           C  
-ANISOU 1065  CE  MET A 152    12667  15190  15837   3396    437   3491       C  
-ATOM   1066  N   SER A 153      23.900 -23.327   2.076  1.00 96.50           N  
-ANISOU 1066  N   SER A 153    11405  12313  12946   3303    314   2786       N  
-ATOM   1067  CA  SER A 153      25.215 -23.948   2.138  1.00107.44           C  
-ANISOU 1067  CA  SER A 153    12829  13666  14326   3506    405   3020       C  
-ATOM   1068  C   SER A 153      25.526 -24.633   0.814  1.00114.70           C  
-ANISOU 1068  C   SER A 153    13880  14755  14945   3860    584   3141       C  
-ATOM   1069  O   SER A 153      24.742 -25.449   0.335  1.00117.27           O  
-ANISOU 1069  O   SER A 153    14503  15114  14941   3881    611   2879       O  
-ATOM   1070  CB  SER A 153      25.272 -24.964   3.280  1.00106.77           C  
-ANISOU 1070  CB  SER A 153    13024  13388  14157   3334    349   2782       C  
-ATOM   1071  OG  SER A 153      26.524 -25.628   3.310  1.00107.08           O  
-ANISOU 1071  OG  SER A 153    13116  13401  14168   3536    449   3004       O  
-ATOM   1072  N   ALA A 154      26.672 -24.300   0.227  1.00142.05           N  
-ANISOU 1072  N   ALA A 154    17136  18341  18497   4091    725   3520       N  
-ATOM   1073  CA  ALA A 154      27.064 -24.868  -1.059  1.00149.19           C  
-ANISOU 1073  CA  ALA A 154    18151  19416  19119   4477    912   3682       C  
-ATOM   1074  C   ALA A 154      27.572 -26.298  -0.915  1.00153.78           C  
-ANISOU 1074  C   ALA A 154    19089  19911  19429   4663    973   3631       C  
-ATOM   1075  O   ALA A 154      28.549 -26.554  -0.209  1.00154.73           O  
-ANISOU 1075  O   ALA A 154    19174  19959  19657   4623   1014   3763       O  
-ATOM   1076  CB  ALA A 154      28.116 -23.994  -1.729  1.00153.52           C  
-ANISOU 1076  CB  ALA A 154    18342  20153  19835   4620   1082   4106       C  
-ATOM   1077  N   VAL A 155      26.899 -27.227  -1.586  1.00147.61           N  
-ANISOU 1077  N   VAL A 155    18665  19165  18256   4776   1012   3389       N  
-ATOM   1078  CA  VAL A 155      27.294 -28.628  -1.552  1.00155.90           C  
-ANISOU 1078  CA  VAL A 155    20101  20151  18983   4925   1085   3293       C  
-ATOM   1079  C   VAL A 155      28.667 -28.798  -2.186  1.00161.74           C  
-ANISOU 1079  C   VAL A 155    20765  21000  19688   5346   1279   3722       C  
-ATOM   1080  O   VAL A 155      29.675 -28.922  -1.490  1.00163.76           O  
-ANISOU 1080  O   VAL A 155    20926  21194  20100   5335   1322   3908       O  
-ATOM   1081  CB  VAL A 155      26.285 -29.516  -2.303  1.00156.00           C  
-ANISOU 1081  CB  VAL A 155    20517  20186  18571   4982   1071   2972       C  
-ATOM   1082  CG1 VAL A 155      26.709 -30.976  -2.235  1.00157.80           C  
-ANISOU 1082  CG1 VAL A 155    21166  20332  18460   5136   1127   2870       C  
-ATOM   1083  CG2 VAL A 155      24.889 -29.333  -1.731  1.00159.24           C  
-ANISOU 1083  CG2 VAL A 155    20979  20505  19021   4575    885   2586       C  
-ATOM   1084  N   ASP A 156      28.696 -28.794  -3.515  1.00161.30           N  
-ANISOU 1084  N   ASP A 156    20749  21120  19416   5701   1410   3876       N  
-ATOM   1085  CA  ASP A 156      29.937 -28.942  -4.262  1.00171.01           C  
-ANISOU 1085  CA  ASP A 156    21909  22511  20557   6096   1651   4268       C  
-ATOM   1086  C   ASP A 156      30.166 -27.726  -5.150  1.00172.30           C  
-ANISOU 1086  C   ASP A 156    21673  22903  20889   6202   1777   4568       C  
-ATOM   1087  O   ASP A 156      30.135 -27.824  -6.375  1.00175.79           O  
-ANISOU 1087  O   ASP A 156    22201  23506  21087   6550   1910   4679       O  
-ATOM   1088  CB  ASP A 156      29.901 -30.210  -5.112  1.00179.79           C  
-ANISOU 1088  CB  ASP A 156    23499  23631  21183   6490   1731   4201       C  
-ATOM   1089  CG  ASP A 156      31.209 -30.467  -5.824  1.00194.61           C  
-ANISOU 1089  CG  ASP A 156    25335  25683  22925   6904   2013   4589       C  
-ATOM   1090  OD1 ASP A 156      32.264 -30.108  -5.262  1.00197.96           O  
-ANISOU 1090  OD1 ASP A 156    25460  26145  23609   6834   2120   4860       O  
-ATOM   1091  OD2 ASP A 156      31.186 -31.022  -6.942  1.00199.37           O  
-ANISOU 1091  OD2 ASP A 156    26209  26382  23159   7306   2126   4634       O  
-ATOM   1092  N   GLY A 157      30.396 -26.578  -4.522  1.00142.48           N  
-ANISOU 1092  N   GLY A 157    17477  19133  17526   5900   1727   4701       N  
-ATOM   1093  CA  GLY A 157      30.551 -25.334  -5.250  1.00141.06           C  
-ANISOU 1093  CA  GLY A 157    16904  19149  17544   5933   1815   4977       C  
-ATOM   1094  C   GLY A 157      29.204 -24.679  -5.473  1.00135.33           C  
-ANISOU 1094  C   GLY A 157    16147  18417  16855   5744   1657   4711       C  
-ATOM   1095  O   GLY A 157      28.988 -23.534  -5.079  1.00133.40           O  
-ANISOU 1095  O   GLY A 157    15579  18172  16936   5455   1565   4748       O  
-ATOM   1096  N   GLN A 158      28.295 -25.413  -6.106  1.00141.79           N  
-ANISOU 1096  N   GLN A 158    17317  19223  17335   5910   1615   4448       N  
-ATOM   1097  CA  GLN A 158      26.935 -24.938  -6.314  1.00133.76           C  
-ANISOU 1097  CA  GLN A 158    16307  18190  16326   5737   1456   4175       C  
-ATOM   1098  C   GLN A 158      26.279 -24.648  -4.968  1.00125.11           C  
-ANISOU 1098  C   GLN A 158    15157  16898  15482   5288   1230   3912       C  
-ATOM   1099  O   GLN A 158      26.224 -25.517  -4.097  1.00121.68           O  
-ANISOU 1099  O   GLN A 158    14976  16285  14971   5163   1142   3707       O  
-ATOM   1100  CB  GLN A 158      26.116 -25.977  -7.083  1.00132.43           C  
-ANISOU 1100  CB  GLN A 158    16589  18002  15728   5949   1428   3918       C  
-ATOM   1101  CG  GLN A 158      24.733 -25.501  -7.505  1.00127.69           C  
-ANISOU 1101  CG  GLN A 158    15998  17438  15081   5751   1321   3643       C  
-ATOM   1102  CD  GLN A 158      24.779 -24.511  -8.654  1.00128.96           C  
-ANISOU 1102  CD  GLN A 158    15867  17808  15323   5995   1420   3910       C  
-ATOM   1103  OE1 GLN A 158      25.724 -24.502  -9.444  1.00129.26           O  
-ANISOU 1103  OE1 GLN A 158    15837  17998  15277   6342   1624   4228       O  
-ATOM   1104  NE2 GLN A 158      23.755 -23.668  -8.751  1.00128.68           N  
-ANISOU 1104  NE2 GLN A 158    15665  17809  15417   5754   1319   3756       N  
-ATOM   1105  N   ARG A 159      25.787 -23.423  -4.803  1.00129.36           N  
-ANISOU 1105  N   ARG A 159    15377  17476  16297   5034   1154   3911       N  
-ATOM   1106  CA  ARG A 159      25.148 -23.015  -3.557  1.00116.94           C  
-ANISOU 1106  CA  ARG A 159    13738  15730  14964   4629    949   3681       C  
-ATOM   1107  C   ARG A 159      23.784 -23.675  -3.386  1.00108.78           C  
-ANISOU 1107  C   ARG A 159    13027  14608  13697   4449    827   3243       C  
-ATOM   1108  O   ARG A 159      23.000 -23.769  -4.332  1.00106.96           O  
-ANISOU 1108  O   ARG A 159    12912  14484  13245   4533    855   3123       O  
-ATOM   1109  CB  ARG A 159      24.997 -21.493  -3.491  1.00119.14           C  
-ANISOU 1109  CB  ARG A 159    13617  16084  15567   4404    915   3803       C  
-ATOM   1110  CG  ARG A 159      23.979 -20.934  -4.470  1.00120.44           C  
-ANISOU 1110  CG  ARG A 159    13721  16392  15649   4447    915   3718       C  
-ATOM   1111  CD  ARG A 159      23.506 -19.545  -4.066  1.00121.05           C  
-ANISOU 1111  CD  ARG A 159    13486  16472  16034   4135    816   3719       C  
-ATOM   1112  NE  ARG A 159      24.574 -18.551  -4.110  1.00120.57           N  
-ANISOU 1112  NE  ARG A 159    13091  16482  16239   4107    900   4087       N  
-ATOM   1113  CZ  ARG A 159      24.924 -17.880  -5.203  1.00120.40           C  
-ANISOU 1113  CZ  ARG A 159    12859  16658  16229   4276   1047   4360       C  
-ATOM   1114  NH1 ARG A 159      25.905 -16.989  -5.152  1.00120.07           N  
-ANISOU 1114  NH1 ARG A 159    12511  16657  16455   4227   1102   4713       N  
-ATOM   1115  NH2 ARG A 159      24.297 -18.104  -6.351  1.00116.67           N  
-ANISOU 1115  NH2 ARG A 159    12486  16337  15506   4497   1130   4292       N  
-ATOM   1116  N   GLN A 160      23.512 -24.126  -2.166  1.00112.81           N  
-ANISOU 1116  N   GLN A 160    13687  14932  14244   4155    709   2996       N  
-ATOM   1117  CA  GLN A 160      22.248 -24.771  -1.840  1.00102.79           C  
-ANISOU 1117  CA  GLN A 160    12713  13578  12764   3904    604   2578       C  
-ATOM   1118  C   GLN A 160      21.460 -23.895  -0.873  1.00 93.55           C  
-ANISOU 1118  C   GLN A 160    11360  12324  11860   3538    453   2426       C  
-ATOM   1119  O   GLN A 160      21.994 -23.437   0.136  1.00 92.82           O  
-ANISOU 1119  O   GLN A 160    11104  12120  12043   3403    390   2513       O  
-ATOM   1120  CB  GLN A 160      22.507 -26.139  -1.210  1.00103.36           C  
-ANISOU 1120  CB  GLN A 160    13145  13504  12623   3877    596   2401       C  
-ATOM   1121  CG  GLN A 160      21.327 -27.082  -1.244  1.00101.73           C  
-ANISOU 1121  CG  GLN A 160    13303  13239  12109   3725    512   2021       C  
-ATOM   1122  CD  GLN A 160      21.162 -27.748  -2.591  1.00103.13           C  
-ANISOU 1122  CD  GLN A 160    13731  13527  11927   4013    591   2016       C  
-ATOM   1123  OE1 GLN A 160      21.603 -27.222  -3.613  1.00101.81           O  
-ANISOU 1123  OE1 GLN A 160    13409  13514  11761   4297    706   2270       O  
-ATOM   1124  NE2 GLN A 160      20.531 -28.917  -2.600  1.00104.70           N  
-ANISOU 1124  NE2 GLN A 160    14328  13639  11814   3951    520   1736       N  
-ATOM   1125  N   VAL A 161      20.191 -23.666  -1.190  1.00 77.78           N  
-ANISOU 1125  N   VAL A 161     9402  10378   9774   3388    392   2209       N  
-ATOM   1126  CA  VAL A 161      19.328 -22.825  -0.372  1.00 64.52           C  
-ANISOU 1126  CA  VAL A 161     7564   8640   8310   3068    264   2067       C  
-ATOM   1127  C   VAL A 161      18.223 -23.650   0.274  1.00 57.79           C  
-ANISOU 1127  C   VAL A 161     7003   7677   7276   2809    165   1703       C  
-ATOM   1128  O   VAL A 161      17.316 -24.130  -0.409  1.00 55.36           O  
-ANISOU 1128  O   VAL A 161     6878   7432   6725   2801    156   1537       O  
-ATOM   1129  CB  VAL A 161      18.686 -21.700  -1.213  1.00 63.69           C  
-ANISOU 1129  CB  VAL A 161     7208   8698   8295   3085    273   2146       C  
-ATOM   1130  CG1 VAL A 161      17.464 -21.125  -0.503  1.00 59.41           C  
-ANISOU 1130  CG1 VAL A 161     6612   8105   7855   2759    147   1924       C  
-ATOM   1131  CG2 VAL A 161      19.711 -20.612  -1.525  1.00 59.38           C  
-ANISOU 1131  CG2 VAL A 161     6295   8234   8031   3261    327   2517       C  
-ATOM   1132  N   GLY A 162      18.309 -23.819   1.589  1.00 61.96           N  
-ANISOU 1132  N   GLY A 162     7575   8038   7930   2601     81   1594       N  
-ATOM   1133  CA  GLY A 162      17.296 -24.542   2.335  1.00 53.87           C  
-ANISOU 1133  CA  GLY A 162     6792   6906   6772   2349    -15   1277       C  
-ATOM   1134  C   GLY A 162      16.218 -23.608   2.844  1.00 46.92           C  
-ANISOU 1134  C   GLY A 162     5748   6027   6053   2102   -107   1172       C  
-ATOM   1135  O   GLY A 162      16.513 -22.521   3.337  1.00 42.72           O  
-ANISOU 1135  O   GLY A 162     4958   5473   5799   2055   -138   1304       O  
-ATOM   1136  N   VAL A 163      14.964 -24.028   2.723  1.00 47.01           N  
-ANISOU 1136  N   VAL A 163     5915   6060   5888   1949   -160    949       N  
-ATOM   1137  CA  VAL A 163      13.843 -23.218   3.179  1.00 43.87           C  
-ANISOU 1137  CA  VAL A 163     5381   5677   5612   1725   -235    854       C  
-ATOM   1138  C   VAL A 163      12.881 -24.020   4.050  1.00 41.76           C  
-ANISOU 1138  C   VAL A 163     5333   5303   5230   1487   -324    598       C  
-ATOM   1139  O   VAL A 163      12.491 -25.130   3.697  1.00 42.35           O  
-ANISOU 1139  O   VAL A 163     5665   5370   5056   1477   -342    462       O  
-ATOM   1140  CB  VAL A 163      13.062 -22.635   1.988  1.00 45.26           C  
-ANISOU 1140  CB  VAL A 163     5440   6032   5723   1772   -207    893       C  
-ATOM   1141  CG1 VAL A 163      11.702 -22.129   2.438  1.00 43.61           C  
-ANISOU 1141  CG1 VAL A 163     5168   5838   5562   1525   -282    755       C  
-ATOM   1142  CG2 VAL A 163      13.863 -21.524   1.328  1.00 42.68           C  
-ANISOU 1142  CG2 VAL A 163     4818   5815   5584   1965   -132   1160       C  
-ATOM   1143  N   GLY A 164      12.503 -23.465   5.196  1.00 37.19           N  
-ANISOU 1143  N   GLY A 164     4662   4637   4830   1304   -387    541       N  
-ATOM   1144  CA  GLY A 164      11.519 -24.111   6.044  1.00 36.55           C  
-ANISOU 1144  CA  GLY A 164     4752   4473   4662   1085   -463    327       C  
-ATOM   1145  C   GLY A 164      10.352 -23.191   6.326  1.00 33.94           C  
-ANISOU 1145  C   GLY A 164     4263   4200   4431    927   -502    297       C  
-ATOM   1146  O   GLY A 164      10.534 -21.981   6.432  1.00 30.91           O  
-ANISOU 1146  O   GLY A 164     3646   3846   4251    955   -493    421       O  
-ATOM   1147  N   TYR A 165       9.154 -23.755   6.445  1.00 43.42           N  
-ANISOU 1147  N   TYR A 165     5590   5417   5491    763   -553    149       N  
-ATOM   1148  CA  TYR A 165       7.978 -22.949   6.746  1.00 43.44           C  
-ANISOU 1148  CA  TYR A 165     5451   5482   5573    617   -580    133       C  
-ATOM   1149  C   TYR A 165       6.913 -23.729   7.511  1.00 43.50           C  
-ANISOU 1149  C   TYR A 165     5616   5433   5479    418   -647    -21       C  
-ATOM   1150  O   TYR A 165       6.917 -24.961   7.503  1.00 44.03           O  
-ANISOU 1150  O   TYR A 165     5910   5440   5379    383   -685   -125       O  
-ATOM   1151  CB  TYR A 165       7.393 -22.354   5.464  1.00 46.34           C  
-ANISOU 1151  CB  TYR A 165     5681   6031   5895    663   -548    213       C  
-ATOM   1152  CG  TYR A 165       6.692 -23.335   4.548  1.00 48.55           C  
-ANISOU 1152  CG  TYR A 165     6142   6375   5928    630   -581    132       C  
-ATOM   1153  CD1 TYR A 165       5.333 -23.584   4.679  1.00 49.57           C  
-ANISOU 1153  CD1 TYR A 165     6315   6539   5980    438   -646     50       C  
-ATOM   1154  CD2 TYR A 165       7.381 -23.986   3.530  1.00 51.10           C  
-ANISOU 1154  CD2 TYR A 165     6598   6723   6096    801   -555    156       C  
-ATOM   1155  CE1 TYR A 165       4.683 -24.468   3.837  1.00 53.59           C  
-ANISOU 1155  CE1 TYR A 165     6999   7089   6275    395   -709    -10       C  
-ATOM   1156  CE2 TYR A 165       6.737 -24.868   2.678  1.00 54.24           C  
-ANISOU 1156  CE2 TYR A 165     7193   7158   6257    780   -611     81       C  
-ATOM   1157  CZ  TYR A 165       5.388 -25.105   2.838  1.00 55.21           C  
-ANISOU 1157  CZ  TYR A 165     7359   7299   6319    566   -700     -5       C  
-ATOM   1158  OH  TYR A 165       4.733 -25.983   2.005  1.00 57.94           O  
-ANISOU 1158  OH  TYR A 165     7912   7663   6441    530   -789    -69       O  
-ATOM   1159  N   VAL A 166       6.010 -23.009   8.175  1.00 32.27           N  
-ANISOU 1159  N   VAL A 166     4075   4031   4157    298   -662    -21       N  
-ATOM   1160  CA  VAL A 166       4.946 -23.640   8.940  1.00 32.93           C  
-ANISOU 1160  CA  VAL A 166     4269   4077   4165    119   -716   -126       C  
-ATOM   1161  C   VAL A 166       3.595 -23.097   8.505  1.00 35.39           C  
-ANISOU 1161  C   VAL A 166     4453   4536   4457     17   -720    -82       C  
-ATOM   1162  O   VAL A 166       3.350 -21.897   8.592  1.00 34.94           O  
-ANISOU 1162  O   VAL A 166     4199   4544   4534     40   -681      4       O  
-ATOM   1163  CB  VAL A 166       5.118 -23.384  10.461  1.00 32.32           C  
-ANISOU 1163  CB  VAL A 166     4198   3859   4223     79   -725   -162       C  
-ATOM   1164  CG1 VAL A 166       3.846 -23.766  11.230  1.00 28.83           C  
-ANISOU 1164  CG1 VAL A 166     3810   3417   3728    -87   -761   -224       C  
-ATOM   1165  CG2 VAL A 166       6.336 -24.128  11.008  1.00 30.58           C  
-ANISOU 1165  CG2 VAL A 166     4133   3478   4007    144   -734   -221       C  
-ATOM   1166  N   ASP A 167       2.721 -23.980   8.034  1.00 50.44           N  
-ANISOU 1166  N   ASP A 167     6476   6489   6199    -96   -778   -132       N  
-ATOM   1167  CA  ASP A 167       1.358 -23.597   7.691  1.00 53.74           C  
-ANISOU 1167  CA  ASP A 167     6783   7039   6597   -218   -795    -77       C  
-ATOM   1168  C   ASP A 167       0.437 -23.902   8.870  1.00 54.55           C  
-ANISOU 1168  C   ASP A 167     6916   7096   6716   -373   -829   -103       C  
-ATOM   1169  O   ASP A 167      -0.095 -25.005   8.993  1.00 53.72           O  
-ANISOU 1169  O   ASP A 167     6966   6953   6494   -496   -912   -159       O  
-ATOM   1170  CB  ASP A 167       0.889 -24.336   6.436  1.00 56.26           C  
-ANISOU 1170  CB  ASP A 167     7207   7432   6737   -256   -861    -88       C  
-ATOM   1171  CG  ASP A 167      -0.454 -23.830   5.926  1.00 59.76           C  
-ANISOU 1171  CG  ASP A 167     7510   8022   7174   -375   -878     -5       C  
-ATOM   1172  OD1 ASP A 167      -1.190 -23.185   6.708  1.00 59.30           O  
-ANISOU 1172  OD1 ASP A 167     7310   8000   7222   -457   -846     50       O  
-ATOM   1173  OD2 ASP A 167      -0.773 -24.079   4.740  1.00 62.36           O  
-ANISOU 1173  OD2 ASP A 167     7880   8427   7387   -376   -924     12       O  
-ATOM   1174  N   SER A 168       0.256 -22.914   9.738  1.00 60.84           N  
-ANISOU 1174  N   SER A 168     7569   7891   7655   -356   -771    -51       N  
-ATOM   1175  CA  SER A 168      -0.486 -23.104  10.982  1.00 62.70           C  
-ANISOU 1175  CA  SER A 168     7833   8077   7915   -454   -782    -61       C  
-ATOM   1176  C   SER A 168      -1.936 -23.532  10.777  1.00 64.60           C  
-ANISOU 1176  C   SER A 168     8052   8423   8069   -619   -826     -2       C  
-ATOM   1177  O   SER A 168      -2.447 -24.375  11.510  1.00 66.02           O  
-ANISOU 1177  O   SER A 168     8333   8547   8203   -724   -875    -28       O  
-ATOM   1178  CB  SER A 168      -0.417 -21.842  11.845  1.00 63.15           C  
-ANISOU 1178  CB  SER A 168     7755   8115   8124   -369   -714     -3       C  
-ATOM   1179  OG  SER A 168      -0.498 -20.675  11.049  1.00 64.94           O  
-ANISOU 1179  OG  SER A 168     7793   8465   8415   -302   -666     92       O  
-ATOM   1180  N   ILE A 169      -2.600 -22.956   9.783  1.00 53.78           N  
-ANISOU 1180  N   ILE A 169     6543   7205   6685   -644   -814     90       N  
-ATOM   1181  CA  ILE A 169      -3.997 -23.286   9.528  1.00 56.22           C  
-ANISOU 1181  CA  ILE A 169     6811   7621   6930   -808   -866    176       C  
-ATOM   1182  C   ILE A 169      -4.170 -24.697   8.962  1.00 59.95           C  
-ANISOU 1182  C   ILE A 169     7476   8048   7256   -926  -1002    118       C  
-ATOM   1183  O   ILE A 169      -5.032 -25.455   9.406  1.00 61.92           O  
-ANISOU 1183  O   ILE A 169     7779   8285   7463  -1075  -1080    152       O  
-ATOM   1184  CB  ILE A 169      -4.657 -22.272   8.574  1.00 53.48           C  
-ANISOU 1184  CB  ILE A 169     6263   7448   6610   -807   -820    294       C  
-ATOM   1185  CG1 ILE A 169      -4.650 -20.872   9.193  1.00 50.84           C  
-ANISOU 1185  CG1 ILE A 169     5747   7157   6411   -702   -702    364       C  
-ATOM   1186  CG2 ILE A 169      -6.076 -22.703   8.247  1.00 54.32           C  
-ANISOU 1186  CG2 ILE A 169     6332   7656   6651   -990   -891    401       C  
-ATOM   1187  CD1 ILE A 169      -5.374 -19.830   8.359  1.00 44.21           C  
-ANISOU 1187  CD1 ILE A 169     4699   6496   5603   -706   -648    486       C  
-ATOM   1188  N   GLN A 170      -3.345 -25.045   7.982  1.00 64.57           N  
-ANISOU 1188  N   GLN A 170     8170   8605   7758   -847  -1035     42       N  
-ATOM   1189  CA  GLN A 170      -3.477 -26.325   7.300  1.00 67.93           C  
-ANISOU 1189  CA  GLN A 170     8809   8981   8021   -932  -1180    -16       C  
-ATOM   1190  C   GLN A 170      -2.696 -27.424   8.009  1.00 69.22           C  
-ANISOU 1190  C   GLN A 170     9197   8976   8127   -921  -1229   -146       C  
-ATOM   1191  O   GLN A 170      -2.666 -28.569   7.552  1.00 70.57           O  
-ANISOU 1191  O   GLN A 170     9584   9077   8151   -976  -1358   -213       O  
-ATOM   1192  CB  GLN A 170      -3.029 -26.192   5.846  1.00 68.81           C  
-ANISOU 1192  CB  GLN A 170     8955   9146   8043   -828  -1191    -26       C  
-ATOM   1193  CG  GLN A 170      -3.767 -25.105   5.083  1.00 69.40           C  
-ANISOU 1193  CG  GLN A 170     8806   9390   8174   -837  -1140     96       C  
-ATOM   1194  CD  GLN A 170      -5.228 -25.437   4.863  1.00 70.88           C  
-ANISOU 1194  CD  GLN A 170     8967   9645   8318  -1045  -1251    191       C  
-ATOM   1195  OE1 GLN A 170      -6.102 -24.579   4.992  1.00 69.40           O  
-ANISOU 1195  OE1 GLN A 170     8564   9581   8224  -1108  -1192    314       O  
-ATOM   1196  NE2 GLN A 170      -5.501 -26.688   4.522  1.00 73.54           N  
-ANISOU 1196  NE2 GLN A 170     9528   9900   8514  -1152  -1422    146       N  
-ATOM   1197  N   ARG A 171      -2.071 -27.073   9.129  1.00 73.48           N  
-ANISOU 1197  N   ARG A 171     9699   9443   8778   -848  -1136   -183       N  
-ATOM   1198  CA  ARG A 171      -1.308 -28.038   9.909  1.00 73.32           C  
-ANISOU 1198  CA  ARG A 171     9874   9264   8722   -835  -1168   -304       C  
-ATOM   1199  C   ARG A 171      -0.271 -28.770   9.051  1.00 71.11           C  
-ANISOU 1199  C   ARG A 171     9793   8916   8309   -732  -1209   -398       C  
-ATOM   1200  O   ARG A 171      -0.238 -29.999   9.029  1.00 71.27           O  
-ANISOU 1200  O   ARG A 171    10035   8847   8198   -797  -1319   -480       O  
-ATOM   1201  CB  ARG A 171      -2.253 -29.052  10.565  1.00 79.21           C  
-ANISOU 1201  CB  ARG A 171    10714   9968   9416  -1023  -1279   -304       C  
-ATOM   1202  CG  ARG A 171      -3.315 -28.440  11.478  1.00 86.80           C  
-ANISOU 1202  CG  ARG A 171    11489  10999  10491  -1107  -1230   -186       C  
-ATOM   1203  CD  ARG A 171      -2.706 -27.859  12.755  1.00 92.15           C  
-ANISOU 1203  CD  ARG A 171    12120  11601  11292   -997  -1113   -220       C  
-ATOM   1204  NE  ARG A 171      -3.715 -27.523  13.761  1.00 97.35           N  
-ANISOU 1204  NE  ARG A 171    12661  12304  12025  -1058  -1074   -114       N  
-ATOM   1205  CZ  ARG A 171      -3.440 -26.988  14.949  1.00 98.43           C  
-ANISOU 1205  CZ  ARG A 171    12766  12377  12257   -965   -984   -124       C  
-ATOM   1206  NH1 ARG A 171      -2.185 -26.721  15.289  1.00 98.88           N  
-ANISOU 1206  NH1 ARG A 171    12891  12315  12364   -829   -939   -232       N  
-ATOM   1207  NH2 ARG A 171      -4.421 -26.720  15.802  1.00 99.51           N  
-ANISOU 1207  NH2 ARG A 171    12808  12564  12437   -997   -944    -10       N  
-ATOM   1208  N   LYS A 172       0.565 -28.017   8.342  1.00 57.22           N  
-ANISOU 1208  N   LYS A 172     7957   7202   6581   -560  -1122   -374       N  
-ATOM   1209  CA  LYS A 172       1.632 -28.613   7.546  1.00 55.82           C  
-ANISOU 1209  CA  LYS A 172     7955   6972   6281   -416  -1131   -435       C  
-ATOM   1210  C   LYS A 172       2.963 -27.981   7.918  1.00 52.82           C  
-ANISOU 1210  C   LYS A 172     7501   6545   6024   -237  -1010   -427       C  
-ATOM   1211  O   LYS A 172       3.050 -26.771   8.098  1.00 51.91           O  
-ANISOU 1211  O   LYS A 172     7163   6489   6070   -184   -924   -343       O  
-ATOM   1212  CB  LYS A 172       1.382 -28.412   6.048  1.00 57.56           C  
-ANISOU 1212  CB  LYS A 172     8168   7306   6396   -356  -1155   -379       C  
-ATOM   1213  CG  LYS A 172       0.042 -28.931   5.544  1.00 59.94           C  
-ANISOU 1213  CG  LYS A 172     8532   7655   6589   -537  -1296   -362       C  
-ATOM   1214  CD  LYS A 172       0.038 -30.443   5.371  1.00 61.43           C  
-ANISOU 1214  CD  LYS A 172     9038   7722   6579   -598  -1455   -463       C  
-ATOM   1215  CE  LYS A 172      -1.378 -31.004   5.476  1.00 63.08           C  
-ANISOU 1215  CE  LYS A 172     9280   7937   6749   -843  -1619   -429       C  
-ATOM   1216  NZ  LYS A 172      -1.439 -32.466   5.201  1.00 64.62           N  
-ANISOU 1216  NZ  LYS A 172     9798   8006   6748   -912  -1811   -517       N  
-ATOM   1217  N   LEU A 173       3.998 -28.803   8.045  1.00 50.99           N  
-ANISOU 1217  N   LEU A 173     7457   6199   5716   -147  -1013   -502       N  
-ATOM   1218  CA  LEU A 173       5.358 -28.297   8.184  1.00 47.91           C  
-ANISOU 1218  CA  LEU A 173     7006   5766   5430     37   -911   -463       C  
-ATOM   1219  C   LEU A 173       6.051 -28.425   6.832  1.00 48.27           C  
-ANISOU 1219  C   LEU A 173     7114   5872   5353    223   -881   -414       C  
-ATOM   1220  O   LEU A 173       6.303 -29.530   6.354  1.00 49.14           O  
-ANISOU 1220  O   LEU A 173     7470   5934   5267    266   -934   -483       O  
-ATOM   1221  CB  LEU A 173       6.134 -29.068   9.250  1.00 45.49           C  
-ANISOU 1221  CB  LEU A 173     6853   5297   5133     33   -915   -555       C  
-ATOM   1222  CG  LEU A 173       5.580 -29.064  10.674  1.00 42.04           C  
-ANISOU 1222  CG  LEU A 173     6390   4781   4804   -120   -939   -611       C  
-ATOM   1223  CD1 LEU A 173       6.629 -29.590  11.640  1.00 41.36           C  
-ANISOU 1223  CD1 LEU A 173     6422   4535   4757    -76   -920   -682       C  
-ATOM   1224  CD2 LEU A 173       5.137 -27.674  11.081  1.00 40.47           C  
-ANISOU 1224  CD2 LEU A 173     5937   4645   4793   -131   -887   -518       C  
-ATOM   1225  N   GLY A 174       6.342 -27.290   6.210  1.00 57.58           N  
-ANISOU 1225  N   GLY A 174     8078   7159   6642    345   -798   -288       N  
-ATOM   1226  CA  GLY A 174       6.873 -27.281   4.861  1.00 57.17           C  
-ANISOU 1226  CA  GLY A 174     8053   7191   6479    538   -758   -215       C  
-ATOM   1227  C   GLY A 174       8.384 -27.301   4.788  1.00 57.25           C  
-ANISOU 1227  C   GLY A 174     8076   7154   6523    758   -670   -141       C  
-ATOM   1228  O   GLY A 174       9.070 -26.609   5.537  1.00 54.78           O  
-ANISOU 1228  O   GLY A 174     7604   6795   6414    788   -616    -73       O  
-ATOM   1229  N   LEU A 175       8.901 -28.114   3.876  1.00 55.34           N  
-ANISOU 1229  N   LEU A 175     8036   6916   6074    919   -664   -143       N  
-ATOM   1230  CA  LEU A 175      10.331 -28.184   3.625  1.00 60.02           C  
-ANISOU 1230  CA  LEU A 175     8645   7488   6672   1162   -566    -37       C  
-ATOM   1231  C   LEU A 175      10.606 -27.941   2.150  1.00 63.55           C  
-ANISOU 1231  C   LEU A 175     9075   8068   7005   1394   -503     85       C  
-ATOM   1232  O   LEU A 175       9.778 -28.255   1.291  1.00 64.04           O  
-ANISOU 1232  O   LEU A 175     9254   8189   6888   1376   -565     29       O  
-ATOM   1233  CB  LEU A 175      10.880 -29.550   4.023  1.00 60.25           C  
-ANISOU 1233  CB  LEU A 175     8980   7381   6531   1185   -599   -147       C  
-ATOM   1234  CG  LEU A 175      11.182 -29.780   5.500  1.00 58.96           C  
-ANISOU 1234  CG  LEU A 175     8824   7075   6505   1047   -616   -223       C  
-ATOM   1235  CD1 LEU A 175      11.511 -31.242   5.725  1.00 60.99           C  
-ANISOU 1235  CD1 LEU A 175     9410   7213   6550   1054   -662   -353       C  
-ATOM   1236  CD2 LEU A 175      12.329 -28.885   5.956  1.00 57.01           C  
-ANISOU 1236  CD2 LEU A 175     8352   6810   6499   1163   -518    -65       C  
-ATOM   1237  N   CYS A 176      11.778 -27.393   1.856  1.00 60.37           N  
-ANISOU 1237  N   CYS A 176     7222   7736   7981    383    339    793       N  
-ATOM   1238  CA  CYS A 176      12.136 -27.090   0.482  1.00 65.16           C  
-ANISOU 1238  CA  CYS A 176     7983   8307   8469    360    401    791       C  
-ATOM   1239  C   CYS A 176      13.614 -26.730   0.373  1.00 68.92           C  
-ANISOU 1239  C   CYS A 176     8349   8911   8926    334    523    961       C  
-ATOM   1240  O   CYS A 176      14.072 -25.755   0.970  1.00 68.77           O  
-ANISOU 1240  O   CYS A 176     8230   8980   8921    237    432   1044       O  
-ATOM   1241  CB  CYS A 176      11.268 -25.951  -0.047  1.00 65.89           C  
-ANISOU 1241  CB  CYS A 176     8235   8329   8472    269    215    701       C  
-ATOM   1242  SG  CYS A 176      11.037 -25.987  -1.828  1.00 67.96           S  
-ANISOU 1242  SG  CYS A 176     8745   8493   8584    281    265    624       S  
-ATOM   1243  N   GLU A 177      14.360 -27.531  -0.382  1.00 74.50           N  
-ANISOU 1243  N   GLU A 177     9077   9628   9601    421    729   1020       N  
-ATOM   1244  CA  GLU A 177      15.780 -27.277  -0.592  1.00 80.28           C  
-ANISOU 1244  CA  GLU A 177     9698  10490  10316    412    868   1205       C  
-ATOM   1245  C   GLU A 177      16.091 -27.298  -2.079  1.00 80.57           C  
-ANISOU 1245  C   GLU A 177     9909  10479  10226    451    990   1209       C  
-ATOM   1246  O   GLU A 177      15.495 -28.070  -2.830  1.00 82.57           O  
-ANISOU 1246  O   GLU A 177    10336  10613  10424    537   1049   1089       O  
-ATOM   1247  CB  GLU A 177      16.625 -28.317   0.139  1.00 85.12           C  
-ANISOU 1247  CB  GLU A 177    10114  11203  11025    514   1045   1328       C  
-ATOM   1248  CG  GLU A 177      18.110 -28.002   0.148  1.00 94.26           C  
-ANISOU 1248  CG  GLU A 177    11102  12528  12185    495   1170   1552       C  
-ATOM   1249  CD  GLU A 177      18.863 -28.845   1.152  1.00 98.48           C  
-ANISOU 1249  CD  GLU A 177    11401  13189  12827    576   1298   1686       C  
-ATOM   1250  OE1 GLU A 177      20.046 -28.550   1.417  1.00102.01           O  
-ANISOU 1250  OE1 GLU A 177    11662  13800  13297    544   1369   1886       O  
-ATOM   1251  OE2 GLU A 177      18.266 -29.806   1.680  1.00 99.79           O  
-ANISOU 1251  OE2 GLU A 177    11562  13294  13060    671   1327   1602       O  
-ATOM   1252  N   PHE A 178      17.025 -26.453  -2.502  1.00 73.66           N  
-ANISOU 1252  N   PHE A 178     8991   9696   9302    387   1024   1351       N  
-ATOM   1253  CA  PHE A 178      17.308 -26.294  -3.923  1.00 72.79           C  
-ANISOU 1253  CA  PHE A 178     9049   9549   9059    421   1128   1367       C  
-ATOM   1254  C   PHE A 178      18.555 -25.452  -4.164  1.00 74.81           C  
-ANISOU 1254  C   PHE A 178     9188   9940   9297    355   1193   1579       C  
-ATOM   1255  O   PHE A 178      18.962 -24.676  -3.302  1.00 74.50           O  
-ANISOU 1255  O   PHE A 178     8978   9994   9333    232   1086   1675       O  
-ATOM   1256  CB  PHE A 178      16.118 -25.633  -4.620  1.00 68.85           C  
-ANISOU 1256  CB  PHE A 178     8776   8919   8466    361    954   1194       C  
-ATOM   1257  CG  PHE A 178      15.736 -24.308  -4.029  1.00 62.92           C  
-ANISOU 1257  CG  PHE A 178     7984   8181   7741    205    731   1186       C  
-ATOM   1258  CD1 PHE A 178      16.507 -23.184  -4.262  1.00 61.30           C  
-ANISOU 1258  CD1 PHE A 178     7733   8051   7508    102    711   1322       C  
-ATOM   1259  CD2 PHE A 178      14.607 -24.186  -3.239  1.00 60.14           C  
-ANISOU 1259  CD2 PHE A 178     7645   7763   7443    167    546   1051       C  
-ATOM   1260  CE1 PHE A 178      16.164 -21.964  -3.720  1.00 57.99           C  
-ANISOU 1260  CE1 PHE A 178     7300   7624   7109    -40    509   1310       C  
-ATOM   1261  CE2 PHE A 178      14.256 -22.965  -2.691  1.00 58.98           C  
-ANISOU 1261  CE2 PHE A 178     7482   7617   7309     41    353   1044       C  
-ATOM   1262  CZ  PHE A 178      15.038 -21.852  -2.932  1.00 57.13           C  
-ANISOU 1262  CZ  PHE A 178     7220   7443   7042    -64    333   1168       C  
-ATOM   1263  N   PRO A 179      19.169 -25.612  -5.344  1.00 54.45           N  
-ANISOU 1263  N   PRO A 179     6703   7369   6616    435   1369   1657       N  
-ATOM   1264  CA  PRO A 179      20.232 -24.715  -5.800  1.00 56.80           C  
-ANISOU 1264  CA  PRO A 179     6920   7780   6883    368   1425   1858       C  
-ATOM   1265  C   PRO A 179      19.623 -23.464  -6.424  1.00 57.31           C  
-ANISOU 1265  C   PRO A 179     7141   7770   6865    246   1252   1784       C  
-ATOM   1266  O   PRO A 179      18.493 -23.511  -6.911  1.00 56.15           O  
-ANISOU 1266  O   PRO A 179     7203   7488   6642    267   1157   1590       O  
-ATOM   1267  CB  PRO A 179      20.948 -25.536  -6.881  1.00 58.21           C  
-ANISOU 1267  CB  PRO A 179     7174   7976   6968    543   1698   1949       C  
-ATOM   1268  CG  PRO A 179      20.362 -26.927  -6.802  1.00 55.89           C  
-ANISOU 1268  CG  PRO A 179     6978   7581   6676    694   1786   1801       C  
-ATOM   1269  CD  PRO A 179      18.996 -26.754  -6.253  1.00 51.56           C  
-ANISOU 1269  CD  PRO A 179     6513   6914   6163    607   1546   1579       C  
-ATOM   1270  N   ASP A 180      20.369 -22.365  -6.416  1.00 74.80           N  
-ANISOU 1270  N   ASP A 180     9252  10074   9096    119   1211   1947       N  
-ATOM   1271  CA  ASP A 180      19.882 -21.110  -6.975  1.00 73.62           C  
-ANISOU 1271  CA  ASP A 180     9241   9855   8876      1   1058   1901       C  
-ATOM   1272  C   ASP A 180      21.015 -20.320  -7.628  1.00 75.05           C  
-ANISOU 1272  C   ASP A 180     9353  10133   9031    -56   1151   2127       C  
-ATOM   1273  O   ASP A 180      22.189 -20.529  -7.315  1.00 73.75           O  
-ANISOU 1273  O   ASP A 180     8978  10109   8935    -55   1279   2335       O  
-ATOM   1274  CB  ASP A 180      19.210 -20.274  -5.883  1.00 75.29           C  
-ANISOU 1274  CB  ASP A 180     9410  10028   9167   -155    804   1813       C  
-ATOM   1275  CG  ASP A 180      18.085 -19.409  -6.417  1.00 76.27           C  
-ANISOU 1275  CG  ASP A 180     9754  10019   9206   -210    635   1660       C  
-ATOM   1276  OD1 ASP A 180      18.041 -19.163  -7.641  1.00 78.87           O  
-ANISOU 1276  OD1 ASP A 180    10237  10311   9419   -170    700   1665       O  
-ATOM   1277  OD2 ASP A 180      17.238 -18.978  -5.608  1.00 78.31           O  
-ANISOU 1277  OD2 ASP A 180    10030  10215   9508   -284    443   1542       O  
-ATOM   1278  N   ASN A 181      20.664 -19.419  -8.541  1.00 67.41           N  
-ANISOU 1278  N   ASN A 181     8552   9097   7965   -103   1090   2101       N  
-ATOM   1279  CA  ASN A 181      21.666 -18.565  -9.172  1.00 70.38           C  
-ANISOU 1279  CA  ASN A 181     8866   9554   8322   -170   1166   2321       C  
-ATOM   1280  C   ASN A 181      21.981 -17.337  -8.323  1.00 71.62           C  
-ANISOU 1280  C   ASN A 181     8884   9743   8585   -394    984   2413       C  
-ATOM   1281  O   ASN A 181      21.373 -17.129  -7.277  1.00 71.75           O  
-ANISOU 1281  O   ASN A 181     8875   9714   8673   -484    800   2293       O  
-ATOM   1282  CB  ASN A 181      21.251 -18.160 -10.593  1.00 69.91           C  
-ANISOU 1282  CB  ASN A 181     9044   9415   8104   -109   1204   2277       C  
-ATOM   1283  CG  ASN A 181      19.944 -17.393 -10.627  1.00 67.48           C  
-ANISOU 1283  CG  ASN A 181     8923   8967   7750   -189    978   2076       C  
-ATOM   1284  OD1 ASN A 181      19.891 -16.223 -10.254  1.00 65.20           O  
-ANISOU 1284  OD1 ASN A 181     8606   8658   7510   -352    823   2112       O  
-ATOM   1285  ND2 ASN A 181      18.884 -18.047 -11.088  1.00 66.79           N  
-ANISOU 1285  ND2 ASN A 181     9032   8779   7567    -75    959   1869       N  
-ATOM   1286  N   ASP A 182      22.940 -16.535  -8.771  1.00 77.63           N  
-ANISOU 1286  N   ASP A 182     9561  10581   9355   -482   1038   2631       N  
-ATOM   1287  CA  ASP A 182      23.362 -15.354  -8.028  1.00 79.52           C  
-ANISOU 1287  CA  ASP A 182     9673  10846   9695   -711    870   2737       C  
-ATOM   1288  C   ASP A 182      22.212 -14.374  -7.829  1.00 77.76           C  
-ANISOU 1288  C   ASP A 182     9636  10464   9446   -820    634   2547       C  
-ATOM   1289  O   ASP A 182      22.192 -13.618  -6.859  1.00 76.06           O  
-ANISOU 1289  O   ASP A 182     9355  10230   9315   -991    452   2542       O  
-ATOM   1290  CB  ASP A 182      24.523 -14.657  -8.739  1.00 84.98           C  
-ANISOU 1290  CB  ASP A 182    10265  11631  10392   -783    978   3008       C  
-ATOM   1291  CG  ASP A 182      25.717 -15.571  -8.947  1.00 88.92           C  
-ANISOU 1291  CG  ASP A 182    10567  12302  10916   -664   1226   3230       C  
-ATOM   1292  OD1 ASP A 182      25.857 -16.126 -10.060  1.00 89.86           O  
-ANISOU 1292  OD1 ASP A 182    10783  12432  10927   -481   1433   3270       O  
-ATOM   1293  OD2 ASP A 182      26.514 -15.734  -7.997  1.00 92.79           O  
-ANISOU 1293  OD2 ASP A 182    10809  12919  11527   -747   1217   3370       O  
-ATOM   1294  N   GLN A 183      21.253 -14.393  -8.751  1.00 74.15           N  
-ANISOU 1294  N   GLN A 183     9415   9893   8864   -716    637   2395       N  
-ATOM   1295  CA  GLN A 183      20.119 -13.475  -8.698  1.00 70.90           C  
-ANISOU 1295  CA  GLN A 183     9189   9335   8413   -793    433   2231       C  
-ATOM   1296  C   GLN A 183      19.053 -13.963  -7.719  1.00 65.39           C  
-ANISOU 1296  C   GLN A 183     8528   8570   7747   -764    294   2014       C  
-ATOM   1297  O   GLN A 183      18.067 -13.269  -7.468  1.00 62.50           O  
-ANISOU 1297  O   GLN A 183     8296   8090   7361   -818    119   1878       O  
-ATOM   1298  CB  GLN A 183      19.502 -13.294 -10.089  1.00 73.73           C  
-ANISOU 1298  CB  GLN A 183     9777   9617   8620   -691    488   2168       C  
-ATOM   1299  CG  GLN A 183      20.489 -13.435 -11.231  1.00 79.63           C  
-ANISOU 1299  CG  GLN A 183    10500  10452   9303   -615    706   2360       C  
-ATOM   1300  CD  GLN A 183      21.741 -12.615 -11.019  1.00 84.61           C  
-ANISOU 1300  CD  GLN A 183    10943  11173  10032   -771    730   2617       C  
-ATOM   1301  OE1 GLN A 183      22.853 -13.109 -11.196  1.00 85.50           O  
-ANISOU 1301  OE1 GLN A 183    10892  11418  10177   -727    908   2811       O  
-ATOM   1302  NE2 GLN A 183      21.568 -11.356 -10.636  1.00 86.84           N  
-ANISOU 1302  NE2 GLN A 183    11250  11383  10364   -954    552   2628       N  
-ATOM   1303  N   PHE A 184      19.259 -15.160  -7.175  1.00 74.79           N  
-ANISOU 1303  N   PHE A 184     9597   9832   8989   -669    382   1995       N  
-ATOM   1304  CA  PHE A 184      18.314 -15.763  -6.241  1.00 67.74           C  
-ANISOU 1304  CA  PHE A 184     8715   8887   8135   -626    275   1810       C  
-ATOM   1305  C   PHE A 184      16.919 -15.842  -6.840  1.00 62.11           C  
-ANISOU 1305  C   PHE A 184     8234   8043   7321   -540    202   1606       C  
-ATOM   1306  O   PHE A 184      15.920 -15.638  -6.154  1.00 58.61           O  
-ANISOU 1306  O   PHE A 184     7848   7523   6899   -563     40   1463       O  
-ATOM   1307  CB  PHE A 184      18.300 -15.000  -4.917  1.00 71.21           C  
-ANISOU 1307  CB  PHE A 184     9059   9323   8674   -782     86   1809       C  
-ATOM   1308  CG  PHE A 184      19.550 -15.186  -4.103  1.00 77.08           C  
-ANISOU 1308  CG  PHE A 184     9551  10211   9526   -857    137   1984       C  
-ATOM   1309  CD1 PHE A 184      20.134 -16.437  -3.979  1.00 80.00           C  
-ANISOU 1309  CD1 PHE A 184     9773  10691   9932   -737    309   2048       C  
-ATOM   1310  CD2 PHE A 184      20.148 -14.109  -3.470  1.00 80.93           C  
-ANISOU 1310  CD2 PHE A 184     9951  10722  10075  -1050     11   2091       C  
-ATOM   1311  CE1 PHE A 184      21.284 -16.611  -3.237  1.00 84.45           C  
-ANISOU 1311  CE1 PHE A 184    10091  11403  10592   -801    356   2226       C  
-ATOM   1312  CE2 PHE A 184      21.301 -14.278  -2.725  1.00 84.28           C  
-ANISOU 1312  CE2 PHE A 184    10133  11293  10596  -1132     42   2262       C  
-ATOM   1313  CZ  PHE A 184      21.869 -15.529  -2.610  1.00 85.80           C  
-ANISOU 1313  CZ  PHE A 184    10164  11612  10824  -1003    217   2335       C  
-ATOM   1314  N   SER A 185      16.869 -16.147  -8.131  1.00 49.72           N  
-ANISOU 1314  N   SER A 185     6798   6458   5637   -437    326   1602       N  
-ATOM   1315  CA  SER A 185      15.612 -16.284  -8.850  1.00 44.84           C  
-ANISOU 1315  CA  SER A 185     6399   5732   4908   -356    265   1423       C  
-ATOM   1316  C   SER A 185      14.675 -17.254  -8.150  1.00 43.02           C  
-ANISOU 1316  C   SER A 185     6171   5457   4718   -284    203   1251       C  
-ATOM   1317  O   SER A 185      13.526 -16.925  -7.873  1.00 41.14           O  
-ANISOU 1317  O   SER A 185     6027   5136   4470   -303     40   1116       O  
-ATOM   1318  CB  SER A 185      15.866 -16.762 -10.281  1.00 42.72           C  
-ANISOU 1318  CB  SER A 185     6253   5473   4504   -234    437   1450       C  
-ATOM   1319  OG  SER A 185      16.915 -16.027 -10.878  1.00 40.73           O  
-ANISOU 1319  OG  SER A 185     5960   5286   4231   -283    534   1646       O  
-ATOM   1320  N   ASN A 186      15.170 -18.455  -7.875  1.00 52.80           N  
-ANISOU 1320  N   ASN A 186     7304   6753   6006   -196    341   1269       N  
-ATOM   1321  CA  ASN A 186      14.349 -19.493  -7.256  1.00 50.38           C  
-ANISOU 1321  CA  ASN A 186     6993   6402   5747   -121    305   1120       C  
-ATOM   1322  C   ASN A 186      13.749 -19.083  -5.913  1.00 47.66           C  
-ANISOU 1322  C   ASN A 186     6560   6039   5508   -201    123   1063       C  
-ATOM   1323  O   ASN A 186      12.551 -19.243  -5.689  1.00 42.58           O  
-ANISOU 1323  O   ASN A 186     6001   5316   4860   -176      2    915       O  
-ATOM   1324  CB  ASN A 186      15.144 -20.789  -7.117  1.00 52.25           C  
-ANISOU 1324  CB  ASN A 186     7116   6706   6030    -14    502   1180       C  
-ATOM   1325  CG  ASN A 186      15.458 -21.417  -8.457  1.00 52.39           C  
-ANISOU 1325  CG  ASN A 186     7272   6712   5923    106    683   1190       C  
-ATOM   1326  OD1 ASN A 186      14.563 -21.637  -9.271  1.00 53.50           O  
-ANISOU 1326  OD1 ASN A 186     7613   6758   5956    159    645   1048       O  
-ATOM   1327  ND2 ASN A 186      16.735 -21.697  -8.698  1.00 54.76           N  
-ANISOU 1327  ND2 ASN A 186     7466   7111   6228    154    880   1365       N  
-ATOM   1328  N   LEU A 187      14.583 -18.545  -5.029  1.00 58.93           N  
-ANISOU 1328  N   LEU A 187     7820   7545   7025   -297    101   1187       N  
-ATOM   1329  CA  LEU A 187      14.099 -18.049  -3.752  1.00 57.80           C  
-ANISOU 1329  CA  LEU A 187     7610   7385   6965   -373    -72   1140       C  
-ATOM   1330  C   LEU A 187      12.997 -17.029  -3.968  1.00 56.70           C  
-ANISOU 1330  C   LEU A 187     7646   7137   6761   -420   -245   1038       C  
-ATOM   1331  O   LEU A 187      11.975 -17.052  -3.285  1.00 54.54           O  
-ANISOU 1331  O   LEU A 187     7401   6807   6513   -399   -371    924       O  
-ATOM   1332  CB  LEU A 187      15.230 -17.422  -2.939  1.00 60.44           C  
-ANISOU 1332  CB  LEU A 187     7770   7815   7378   -495    -86   1295       C  
-ATOM   1333  CG  LEU A 187      14.807 -17.080  -1.508  1.00 59.39           C  
-ANISOU 1333  CG  LEU A 187     7567   7675   7325   -554   -252   1243       C  
-ATOM   1334  CD1 LEU A 187      14.218 -18.303  -0.817  1.00 59.39           C  
-ANISOU 1334  CD1 LEU A 187     7501   7681   7382   -432   -226   1147       C  
-ATOM   1335  CD2 LEU A 187      15.966 -16.521  -0.704  1.00 61.39           C  
-ANISOU 1335  CD2 LEU A 187     7649   8028   7647   -685   -277   1393       C  
-ATOM   1336  N   GLU A 188      13.210 -16.127  -4.919  1.00 53.51           N  
-ANISOU 1336  N   GLU A 188     7352   6707   6272   -473   -243   1093       N  
-ATOM   1337  CA  GLU A 188      12.223 -15.099  -5.207  1.00 51.18           C  
-ANISOU 1337  CA  GLU A 188     7226   6311   5909   -510   -393   1016       C  
-ATOM   1338  C   GLU A 188      10.923 -15.780  -5.602  1.00 46.68           C  
-ANISOU 1338  C   GLU A 188     6777   5677   5283   -398   -431    859       C  
-ATOM   1339  O   GLU A 188       9.857 -15.490  -5.060  1.00 43.01           O  
-ANISOU 1339  O   GLU A 188     6362   5151   4828   -392   -573    765       O  
-ATOM   1340  CB  GLU A 188      12.718 -14.176  -6.319  1.00 56.82           C  
-ANISOU 1340  CB  GLU A 188     8039   7015   6536   -566   -351   1113       C  
-ATOM   1341  CG  GLU A 188      11.897 -12.909  -6.489  1.00 63.26           C  
-ANISOU 1341  CG  GLU A 188     9012   7731   7294   -622   -502   1071       C  
-ATOM   1342  CD  GLU A 188      12.382 -12.027  -7.636  1.00 69.67           C  
-ANISOU 1342  CD  GLU A 188     9920   8530   8021   -668   -449   1176       C  
-ATOM   1343  OE1 GLU A 188      12.926 -12.556  -8.636  1.00 71.85           O  
-ANISOU 1343  OE1 GLU A 188    10204   8859   8236   -606   -298   1233       O  
-ATOM   1344  OE2 GLU A 188      12.219 -10.793  -7.525  1.00 73.44           O  
-ANISOU 1344  OE2 GLU A 188    10473   8940   8489   -759   -554   1206       O  
-ATOM   1345  N   ALA A 189      11.032 -16.720  -6.528  1.00 44.59           N  
-ANISOU 1345  N   ALA A 189     6556   5428   4960   -308   -301    837       N  
-ATOM   1346  CA  ALA A 189       9.879 -17.459  -7.003  1.00 42.75           C  
-ANISOU 1346  CA  ALA A 189     6439   5134   4669   -217   -335    692       C  
-ATOM   1347  C   ALA A 189       9.172 -18.142  -5.847  1.00 41.45           C  
-ANISOU 1347  C   ALA A 189     6182   4956   4612   -185   -412    605       C  
-ATOM   1348  O   ALA A 189       7.959 -18.012  -5.687  1.00 39.72           O  
-ANISOU 1348  O   ALA A 189     6033   4677   4382   -169   -545    507       O  
-ATOM   1349  CB  ALA A 189      10.312 -18.482  -8.029  1.00 41.75           C  
-ANISOU 1349  CB  ALA A 189     6366   5026   4472   -127   -168    686       C  
-ATOM   1350  N   LEU A 190       9.942 -18.876  -5.049  1.00 51.02           N  
-ANISOU 1350  N   LEU A 190     7228   6230   5927   -170   -319    657       N  
-ATOM   1351  CA  LEU A 190       9.398 -19.640  -3.930  1.00 48.24           C  
-ANISOU 1351  CA  LEU A 190     6770   5876   5683   -128   -364    593       C  
-ATOM   1352  C   LEU A 190       8.605 -18.747  -2.987  1.00 46.27           C  
-ANISOU 1352  C   LEU A 190     6514   5595   5470   -175   -545    562       C  
-ATOM   1353  O   LEU A 190       7.417 -18.968  -2.765  1.00 44.09           O  
-ANISOU 1353  O   LEU A 190     6284   5266   5203   -129   -644    465       O  
-ATOM   1354  CB  LEU A 190      10.517 -20.338  -3.162  1.00 51.54           C  
-ANISOU 1354  CB  LEU A 190     6997   6384   6203   -114   -236    687       C  
-ATOM   1355  CG  LEU A 190      10.075 -21.252  -2.022  1.00 51.30           C  
-ANISOU 1355  CG  LEU A 190     6844   6362   6287    -54   -253    637       C  
-ATOM   1356  CD1 LEU A 190       9.108 -22.316  -2.518  1.00 53.29           C  
-ANISOU 1356  CD1 LEU A 190     7187   6536   6526     35   -238    513       C  
-ATOM   1357  CD2 LEU A 190      11.286 -21.890  -1.363  1.00 51.70           C  
-ANISOU 1357  CD2 LEU A 190     6703   6515   6424    -36   -113    751       C  
-ATOM   1358  N   LEU A 191       9.263 -17.733  -2.437  1.00 43.17           N  
-ANISOU 1358  N   LEU A 191     6071   5234   5098   -265   -588    649       N  
-ATOM   1359  CA  LEU A 191       8.592 -16.798  -1.545  1.00 42.04           C  
-ANISOU 1359  CA  LEU A 191     5951   5050   4974   -304   -752    622       C  
-ATOM   1360  C   LEU A 191       7.255 -16.328  -2.101  1.00 42.02           C  
-ANISOU 1360  C   LEU A 191     6115   4959   4893   -270   -864    533       C  
-ATOM   1361  O   LEU A 191       6.262 -16.305  -1.381  1.00 41.33           O  
-ANISOU 1361  O   LEU A 191     6028   4839   4836   -225   -968    472       O  
-ATOM   1362  CB  LEU A 191       9.476 -15.592  -1.245  1.00 42.10           C  
-ANISOU 1362  CB  LEU A 191     5945   5073   4978   -427   -790    722       C  
-ATOM   1363  CG  LEU A 191      10.797 -15.905  -0.554  1.00 44.31           C  
-ANISOU 1363  CG  LEU A 191     6039   5456   5340   -480   -709    830       C  
-ATOM   1364  CD1 LEU A 191      11.517 -14.607  -0.185  1.00 45.51           C  
-ANISOU 1364  CD1 LEU A 191     6193   5609   5491   -625   -789    919       C  
-ATOM   1365  CD2 LEU A 191      10.569 -16.780   0.671  1.00 42.92           C  
-ANISOU 1365  CD2 LEU A 191     5723   5325   5258   -413   -719    793       C  
-ATOM   1366  N   ILE A 192       7.227 -15.954  -3.376  1.00 36.86           N  
-ANISOU 1366  N   ILE A 192     5595   4277   4134   -282   -839    536       N  
-ATOM   1367  CA  ILE A 192       5.998 -15.450  -3.975  1.00 34.97           C  
-ANISOU 1367  CA  ILE A 192     5510   3968   3809   -252   -945    468       C  
-ATOM   1368  C   ILE A 192       4.855 -16.471  -3.907  1.00 33.43           C  
-ANISOU 1368  C   ILE A 192     5309   3757   3636   -162   -984    367       C  
-ATOM   1369  O   ILE A 192       3.702 -16.106  -3.662  1.00 31.15           O  
-ANISOU 1369  O   ILE A 192     5071   3429   3336   -130  -1107    323       O  
-ATOM   1370  CB  ILE A 192       6.216 -14.988  -5.429  1.00 37.82           C  
-ANISOU 1370  CB  ILE A 192     6011   4315   4045   -271   -898    495       C  
-ATOM   1371  CG1 ILE A 192       7.023 -13.687  -5.455  1.00 38.17           C  
-ANISOU 1371  CG1 ILE A 192     6084   4351   4069   -368   -903    600       C  
-ATOM   1372  CG2 ILE A 192       4.883 -14.789  -6.131  1.00 38.42           C  
-ANISOU 1372  CG2 ILE A 192     6230   4340   4029   -220   -997    418       C  
-ATOM   1373  CD1 ILE A 192       7.364 -13.197  -6.851  1.00 36.14           C  
-ANISOU 1373  CD1 ILE A 192     5949   4088   3695   -384   -839    651       C  
-ATOM   1374  N   GLN A 193       5.163 -17.747  -4.109  1.00 41.43           N  
-ANISOU 1374  N   GLN A 193     6259   4798   4684   -120   -879    338       N  
-ATOM   1375  CA  GLN A 193       4.109 -18.760  -4.073  1.00 42.93           C  
-ANISOU 1375  CA  GLN A 193     6445   4962   4904    -51   -918    244       C  
-ATOM   1376  C   GLN A 193       3.799 -19.308  -2.665  1.00 43.11           C  
-ANISOU 1376  C   GLN A 193     6315   5001   5065    -14   -949    236       C  
-ATOM   1377  O   GLN A 193       2.750 -19.920  -2.448  1.00 42.28           O  
-ANISOU 1377  O   GLN A 193     6195   4869   5000     36  -1013    175       O  
-ATOM   1378  CB  GLN A 193       4.353 -19.876  -5.100  1.00 43.77           C  
-ANISOU 1378  CB  GLN A 193     6605   5061   4963    -18   -806    196       C  
-ATOM   1379  CG  GLN A 193       5.786 -20.349  -5.222  1.00 47.49           C  
-ANISOU 1379  CG  GLN A 193     7011   5580   5452    -19   -628    264       C  
-ATOM   1380  CD  GLN A 193       5.992 -21.231  -6.444  1.00 50.64           C  
-ANISOU 1380  CD  GLN A 193     7521   5956   5762     26   -516    217       C  
-ATOM   1381  OE1 GLN A 193       7.022 -21.886  -6.585  1.00 53.76           O  
-ANISOU 1381  OE1 GLN A 193     7871   6384   6171     57   -353    264       O  
-ATOM   1382  NE2 GLN A 193       5.012 -21.241  -7.339  1.00 52.53           N  
-ANISOU 1382  NE2 GLN A 193     7914   6144   5902     35   -602    129       N  
-ATOM   1383  N   ILE A 194       4.699 -19.089  -1.712  1.00 48.64           N  
-ANISOU 1383  N   ILE A 194     6895   5749   5837    -39   -906    306       N  
-ATOM   1384  CA  ILE A 194       4.366 -19.371  -0.322  1.00 47.35           C  
-ANISOU 1384  CA  ILE A 194     6600   5605   5784      1   -952    307       C  
-ATOM   1385  C   ILE A 194       3.673 -18.158   0.274  1.00 45.98           C  
-ANISOU 1385  C   ILE A 194     6480   5403   5586     -8  -1096    314       C  
-ATOM   1386  O   ILE A 194       2.627 -18.280   0.902  1.00 45.65           O  
-ANISOU 1386  O   ILE A 194     6417   5343   5584     56  -1180    283       O  
-ATOM   1387  CB  ILE A 194       5.597 -19.709   0.530  1.00 48.33           C  
-ANISOU 1387  CB  ILE A 194     6567   5805   5991    -15   -854    380       C  
-ATOM   1388  CG1 ILE A 194       5.974 -21.181   0.371  1.00 49.85           C  
-ANISOU 1388  CG1 ILE A 194     6673   6021   6245     43   -712    369       C  
-ATOM   1389  CG2 ILE A 194       5.310 -19.415   1.982  1.00 46.00           C  
-ANISOU 1389  CG2 ILE A 194     6176   5533   5770      7   -938    395       C  
-ATOM   1390  CD1 ILE A 194       7.308 -21.534   1.001  1.00 49.84           C  
-ANISOU 1390  CD1 ILE A 194     6516   6110   6311     32   -591    463       C  
-ATOM   1391  N   GLY A 195       4.264 -16.988   0.072  1.00 46.29           N  
-ANISOU 1391  N   GLY A 195     6594   5433   5561    -84  -1118    363       N  
-ATOM   1392  CA  GLY A 195       3.669 -15.737   0.501  1.00 44.91           C  
-ANISOU 1392  CA  GLY A 195     6511   5210   5344    -94  -1244    369       C  
-ATOM   1393  C   GLY A 195       3.692 -15.494   1.997  1.00 44.58           C  
-ANISOU 1393  C   GLY A 195     6384   5183   5370    -74  -1299    387       C  
-ATOM   1394  O   GLY A 195       2.662 -15.170   2.582  1.00 43.63           O  
-ANISOU 1394  O   GLY A 195     6299   5029   5249     -3  -1392    363       O  
-ATOM   1395  N   PRO A 196       4.868 -15.625   2.626  1.00 34.71           N  
-ANISOU 1395  N   PRO A 196     5023   3992   4172   -132  -1243    437       N  
-ATOM   1396  CA  PRO A 196       4.946 -15.397   4.069  1.00 34.30           C  
-ANISOU 1396  CA  PRO A 196     4898   3964   4172   -115  -1301    451       C  
-ATOM   1397  C   PRO A 196       4.870 -13.912   4.368  1.00 35.99           C  
-ANISOU 1397  C   PRO A 196     5253   4108   4314   -172  -1412    461       C  
-ATOM   1398  O   PRO A 196       5.025 -13.103   3.460  1.00 37.47           O  
-ANISOU 1398  O   PRO A 196     5566   4241   4428   -243  -1424    476       O  
-ATOM   1399  CB  PRO A 196       6.338 -15.913   4.418  1.00 32.47           C  
-ANISOU 1399  CB  PRO A 196     4513   3824   4000   -180  -1207    514       C  
-ATOM   1400  CG  PRO A 196       7.139 -15.630   3.203  1.00 32.70           C  
-ANISOU 1400  CG  PRO A 196     4596   3851   3978   -273  -1138    557       C  
-ATOM   1401  CD  PRO A 196       6.196 -15.879   2.040  1.00 33.60           C  
-ANISOU 1401  CD  PRO A 196     4826   3905   4035   -214  -1128    496       C  
-ATOM   1402  N   LYS A 197       4.631 -13.559   5.623  1.00 47.82           N  
-ANISOU 1402  N   LYS A 197     6741   5601   5827   -135  -1489    454       N  
-ATOM   1403  CA  LYS A 197       4.580 -12.163   6.023  1.00 50.73           C  
-ANISOU 1403  CA  LYS A 197     7264   5887   6124   -183  -1595    457       C  
-ATOM   1404  C   LYS A 197       5.911 -11.777   6.638  1.00 51.22           C  
-ANISOU 1404  C   LYS A 197     7271   5987   6202   -317  -1606    504       C  
-ATOM   1405  O   LYS A 197       6.322 -10.619   6.584  1.00 51.97           O  
-ANISOU 1405  O   LYS A 197     7493   6012   6242   -425  -1672    522       O  
-ATOM   1406  CB  LYS A 197       3.461 -11.945   7.040  1.00 54.49           C  
-ANISOU 1406  CB  LYS A 197     7789   6326   6588    -49  -1677    420       C  
-ATOM   1407  CG  LYS A 197       2.765 -10.603   6.926  1.00 62.08           C  
-ANISOU 1407  CG  LYS A 197     8971   7167   7451    -34  -1768    407       C  
-ATOM   1408  CD  LYS A 197       1.820 -10.589   5.737  1.00 68.21           C  
-ANISOU 1408  CD  LYS A 197     9826   7905   8187     22  -1755    399       C  
-ATOM   1409  CE  LYS A 197       1.011  -9.301   5.683  1.00 72.64           C  
-ANISOU 1409  CE  LYS A 197    10597   8350   8651     69  -1835    400       C  
-ATOM   1410  NZ  LYS A 197      -0.081  -9.364   4.666  1.00 74.26           N  
-ANISOU 1410  NZ  LYS A 197    10857   8541   8817    149  -1832    403       N  
-ATOM   1411  N   GLU A 198       6.578 -12.763   7.222  1.00 54.92           N  
-ANISOU 1411  N   GLU A 198     7547   6568   6751   -312  -1543    531       N  
-ATOM   1412  CA  GLU A 198       7.833 -12.542   7.920  1.00 55.73           C  
-ANISOU 1412  CA  GLU A 198     7561   6737   6878   -433  -1558    589       C  
-ATOM   1413  C   GLU A 198       8.854 -13.569   7.447  1.00 54.88           C  
-ANISOU 1413  C   GLU A 198     7263   6747   6840   -473  -1423    658       C  
-ATOM   1414  O   GLU A 198       8.516 -14.511   6.736  1.00 55.09           O  
-ANISOU 1414  O   GLU A 198     7241   6793   6896   -391  -1321    644       O  
-ATOM   1415  CB  GLU A 198       7.603 -12.672   9.426  1.00 57.15           C  
-ANISOU 1415  CB  GLU A 198     7688   6953   7075   -360  -1625    566       C  
-ATOM   1416  CG  GLU A 198       8.607 -11.955  10.310  1.00 61.19           C  
-ANISOU 1416  CG  GLU A 198     8192   7490   7568   -493  -1712    602       C  
-ATOM   1417  CD  GLU A 198       8.131 -11.883  11.754  1.00 62.56           C  
-ANISOU 1417  CD  GLU A 198     8378   7670   7721   -398  -1798    559       C  
-ATOM   1418  OE1 GLU A 198       6.946 -12.204  11.995  1.00 62.58           O  
-ANISOU 1418  OE1 GLU A 198     8418   7640   7720   -228  -1793    509       O  
-ATOM   1419  OE2 GLU A 198       8.932 -11.510  12.641  1.00 62.33           O  
-ANISOU 1419  OE2 GLU A 198     8320   7685   7678   -491  -1873    583       O  
-ATOM   1420  N   CYS A 199      10.109 -13.384   7.828  1.00 51.49           N  
-ANISOU 1420  N   CYS A 199     6733   6394   6435   -599  -1422    739       N  
-ATOM   1421  CA  CYS A 199      11.146 -14.341   7.474  1.00 51.42           C  
-ANISOU 1421  CA  CYS A 199     6532   6512   6493   -623  -1283    828       C  
-ATOM   1422  C   CYS A 199      12.291 -14.296   8.481  1.00 52.06           C  
-ANISOU 1422  C   CYS A 199     6458   6709   6614   -721  -1312    915       C  
-ATOM   1423  O   CYS A 199      12.767 -13.217   8.844  1.00 52.65           O  
-ANISOU 1423  O   CYS A 199     6598   6754   6651   -862  -1429    939       O  
-ATOM   1424  CB  CYS A 199      11.669 -14.054   6.072  1.00 52.16           C  
-ANISOU 1424  CB  CYS A 199     6679   6582   6557   -706  -1207    883       C  
-ATOM   1425  SG  CYS A 199      13.244 -14.856   5.706  1.00 54.75           S  
-ANISOU 1425  SG  CYS A 199     6783   7068   6950   -767  -1044   1034       S  
-ATOM   1426  N   VAL A 200      12.732 -15.462   8.943  1.00 37.48           N  
-ANISOU 1426  N   VAL A 200     4408   4992   4841   -649  -1211    964       N  
-ATOM   1427  CA  VAL A 200      13.855 -15.511   9.869  1.00 38.15           C  
-ANISOU 1427  CA  VAL A 200     4320   5212   4964   -736  -1232   1063       C  
-ATOM   1428  C   VAL A 200      15.129 -15.883   9.131  1.00 40.01           C  
-ANISOU 1428  C   VAL A 200     4405   5556   5240   -818  -1101   1206       C  
-ATOM   1429  O   VAL A 200      15.125 -16.731   8.230  1.00 37.33           O  
-ANISOU 1429  O   VAL A 200     4027   5230   4926   -731   -943   1224       O  
-ATOM   1430  CB  VAL A 200      13.621 -16.507  11.034  1.00 36.30           C  
-ANISOU 1430  CB  VAL A 200     3936   5072   4783   -599  -1206   1051       C  
-ATOM   1431  CG1 VAL A 200      12.343 -16.164  11.771  1.00 33.78           C  
-ANISOU 1431  CG1 VAL A 200     3758   4654   4422   -499  -1322    927       C  
-ATOM   1432  CG2 VAL A 200      13.583 -17.937  10.528  1.00 33.84           C  
-ANISOU 1432  CG2 VAL A 200     3495   4819   4545   -463  -1016   1077       C  
-ATOM   1433  N   LEU A 201      16.218 -15.226   9.504  1.00 39.12           N  
-ANISOU 1433  N   LEU A 201     4214   5519   5130   -986  -1170   1311       N  
-ATOM   1434  CA  LEU A 201      17.517 -15.541   8.942  1.00 47.35           C  
-ANISOU 1434  CA  LEU A 201     5083   6691   6218  -1066  -1049   1480       C  
-ATOM   1435  C   LEU A 201      18.510 -15.640  10.075  1.00 53.17           C  
-ANISOU 1435  C   LEU A 201     5614   7591   6996  -1150  -1101   1592       C  
-ATOM   1436  O   LEU A 201      18.334 -15.001  11.110  1.00 52.77           O  
-ANISOU 1436  O   LEU A 201     5612   7522   6915  -1216  -1273   1537       O  
-ATOM   1437  CB  LEU A 201      17.970 -14.453   7.970  1.00 46.85           C  
-ANISOU 1437  CB  LEU A 201     5129   6557   6116  -1229  -1083   1536       C  
-ATOM   1438  CG  LEU A 201      17.003 -14.064   6.857  1.00 46.25           C  
-ANISOU 1438  CG  LEU A 201     5281   6312   5978  -1175  -1068   1430       C  
-ATOM   1439  CD1 LEU A 201      17.577 -12.911   6.068  1.00 44.30           C  
-ANISOU 1439  CD1 LEU A 201     5123   6009   5699  -1349  -1111   1509       C  
-ATOM   1440  CD2 LEU A 201      16.726 -15.249   5.957  1.00 46.30           C  
-ANISOU 1440  CD2 LEU A 201     5254   6338   5998  -1008   -874   1420       C  
-ATOM   1441  N   PRO A 202      19.563 -16.443   9.888  1.00 54.35           N  
-ANISOU 1441  N   PRO A 202     5536   7907   7208  -1141   -951   1753       N  
-ATOM   1442  CA  PRO A 202      20.583 -16.457  10.934  1.00 62.31           C  
-ANISOU 1442  CA  PRO A 202     6334   9090   8252  -1239  -1012   1881       C  
-ATOM   1443  C   PRO A 202      21.196 -15.074  11.090  1.00 71.63           C  
-ANISOU 1443  C   PRO A 202     7569  10248   9399  -1490  -1198   1932       C  
-ATOM   1444  O   PRO A 202      21.504 -14.420  10.090  1.00 74.81           O  
-ANISOU 1444  O   PRO A 202     8046  10586   9791  -1598  -1182   1984       O  
-ATOM   1445  CB  PRO A 202      21.622 -17.451  10.402  1.00 60.58           C  
-ANISOU 1445  CB  PRO A 202     5879   9038   8100  -1185   -794   2069       C  
-ATOM   1446  CG  PRO A 202      21.361 -17.559   8.937  1.00 57.10           C  
-ANISOU 1446  CG  PRO A 202     5561   8493   7642  -1126   -652   2052       C  
-ATOM   1447  CD  PRO A 202      19.898 -17.325   8.756  1.00 55.02           C  
-ANISOU 1447  CD  PRO A 202     5551   8031   7324  -1041   -725   1833       C  
-ATOM   1448  N   GLY A 203      21.347 -14.627  12.332  1.00 67.16           N  
-ANISOU 1448  N   GLY A 203     6978   9727   8814  -1581  -1376   1913       N  
-ATOM   1449  CA  GLY A 203      22.177 -13.473  12.608  1.00 84.10           C  
-ANISOU 1449  CA  GLY A 203     9126  11886  10941  -1840  -1552   1993       C  
-ATOM   1450  C   GLY A 203      23.520 -13.797  11.998  1.00 98.57           C  
-ANISOU 1450  C   GLY A 203    10713  13893  12847  -1932  -1426   2231       C  
-ATOM   1451  O   GLY A 203      24.402 -12.937  11.886  1.00101.03           O  
-ANISOU 1451  O   GLY A 203    10982  14235  13168  -2161  -1526   2352       O  
-ATOM   1452  N   GLY A 204      23.666 -15.067  11.619  1.00179.37           N  
-ANISOU 1452  N   GLY A 204    20783  24238  23132  -1745  -1200   2304       N  
-ATOM   1453  CA  GLY A 204      24.722 -15.486  10.718  1.00196.72           C  
-ANISOU 1453  CA  GLY A 204    22793  26565  25387  -1764  -1018   2518       C  
-ATOM   1454  C   GLY A 204      25.034 -14.331   9.789  1.00206.93           C  
-ANISOU 1454  C   GLY A 204    24205  27757  26662  -1952  -1078   2567       C  
-ATOM   1455  O   GLY A 204      24.150 -13.761   9.165  1.00204.16           O  
-ANISOU 1455  O   GLY A 204    24105  27207  26259  -1935  -1113   2419       O  
-ATOM   1456  N   GLU A 205      26.313 -14.000   9.714  1.00188.04           N  
-ANISOU 1456  N   GLU A 205    21616  25512  24317  -2130  -1088   2793       N  
-ATOM   1457  CA  GLU A 205      26.800 -12.730   9.187  1.00199.61           C  
-ANISOU 1457  CA  GLU A 205    23157  26905  25781  -2372  -1204   2870       C  
-ATOM   1458  C   GLU A 205      26.165 -12.182   7.899  1.00202.18           C  
-ANISOU 1458  C   GLU A 205    23723  27030  26065  -2344  -1144   2788       C  
-ATOM   1459  O   GLU A 205      25.252 -12.770   7.320  1.00201.54           O  
-ANISOU 1459  O   GLU A 205    23775  26854  25948  -2134  -1016   2653       O  
-ATOM   1460  CB  GLU A 205      28.302 -12.842   8.974  1.00 20.00           C  
-ATOM   1461  N   THR A 206      26.693 -11.040   7.467  1.00201.25           N  
-ANISOU 1461  N   THR A 206    23652  26857  25956  -2570  -1243   2882       N  
-ATOM   1462  CA  THR A 206      26.190 -10.297   6.327  1.00204.27           C  
-ANISOU 1462  CA  THR A 206    24264  27052  26298  -2584  -1219   2825       C  
-ATOM   1463  C   THR A 206      27.002 -10.614   5.079  1.00202.72           C  
-ANISOU 1463  C   THR A 206    23931  26954  26138  -2551   -999   3040       C  
-ATOM   1464  O   THR A 206      27.153  -9.770   4.191  1.00206.22           O  
-ANISOU 1464  O   THR A 206    24474  27305  26575  -2656  -1000   3102       O  
-ATOM   1465  CB  THR A 206      26.275  -8.783   6.597  1.00209.74           C  
-ANISOU 1465  CB  THR A 206    25109  27605  26979  -2853  -1459   2804       C  
-ATOM   1466  OG1 THR A 206      25.948  -8.055   5.405  1.00213.58           O  
-ANISOU 1466  OG1 THR A 206    25785  27930  27436  -2873  -1413   2794       O  
-ATOM   1467  CG2 THR A 206      27.683  -8.411   7.044  1.00215.64           C  
-ANISOU 1467  CG2 THR A 206    25610  28519  27805  -3105  -1546   3043       C  
-ATOM   1468  N   ALA A 207      27.535 -11.831   5.026  1.00166.48           N  
-ANISOU 1468  N   ALA A 207    19117  22552  21587  -2397   -803   3162       N  
-ATOM   1469  CA  ALA A 207      28.343 -12.271   3.896  1.00162.21           C  
-ANISOU 1469  CA  ALA A 207    18438  22122  21073  -2328   -568   3379       C  
-ATOM   1470  C   ALA A 207      27.733 -11.805   2.581  1.00156.65           C  
-ANISOU 1470  C   ALA A 207    17973  21242  20303  -2271   -493   3306       C  
-ATOM   1471  O   ALA A 207      26.514 -11.706   2.458  1.00155.57           O  
-ANISOU 1471  O   ALA A 207    18087  20926  20096  -2175   -544   3066       O  
-ATOM   1472  CB  ALA A 207      28.485 -13.785   3.906  1.00166.78           C  
-ANISOU 1472  CB  ALA A 207    18858  22847  21664  -2079   -341   3422       C  
-ATOM   1473  N   GLY A 208      28.588 -11.513   1.605  1.00172.75           N  
-ANISOU 1473  N   GLY A 208    19928  23345  22365  -2327   -371   3526       N  
-ATOM   1474  CA  GLY A 208      28.144 -11.034   0.307  1.00162.18           C  
-ANISOU 1474  CA  GLY A 208    18798  21862  20961  -2277   -291   3490       C  
-ATOM   1475  C   GLY A 208      26.857 -11.693  -0.149  1.00152.81           C  
-ANISOU 1475  C   GLY A 208    17839  20541  19680  -2033   -211   3241       C  
-ATOM   1476  O   GLY A 208      25.975 -11.036  -0.704  1.00152.17           O  
-ANISOU 1476  O   GLY A 208    18010  20278  19530  -2030   -275   3092       O  
-ATOM   1477  N   ASP A 209      26.751 -12.997   0.089  1.00127.40           N  
-ANISOU 1477  N   ASP A 209    14530  17414  16462  -1832    -71   3204       N  
-ATOM   1478  CA  ASP A 209      25.548 -13.746  -0.255  1.00117.95           C  
-ANISOU 1478  CA  ASP A 209    13529  16099  15187  -1609     -2   2973       C  
-ATOM   1479  C   ASP A 209      24.344 -13.293   0.561  1.00109.24           C  
-ANISOU 1479  C   ASP A 209    12609  14839  14059  -1646   -223   2719       C  
-ATOM   1480  O   ASP A 209      23.317 -12.907   0.005  1.00107.75           O  
-ANISOU 1480  O   ASP A 209    12662  14483  13795  -1598   -268   2553       O  
-ATOM   1481  CB  ASP A 209      25.774 -15.244  -0.054  1.00116.70           C  
-ANISOU 1481  CB  ASP A 209    13222  16069  15050  -1404    188   3002       C  
-ATOM   1482  CG  ASP A 209      26.155 -15.949  -1.336  1.00117.84           C  
-ANISOU 1482  CG  ASP A 209    13372  16256  15146  -1230    455   3108       C  
-ATOM   1483  OD1 ASP A 209      25.812 -15.432  -2.421  1.00116.48           O  
-ANISOU 1483  OD1 ASP A 209    13384  15975  14898  -1218    483   3074       O  
-ATOM   1484  OD2 ASP A 209      26.786 -17.024  -1.258  1.00119.01           O  
-ANISOU 1484  OD2 ASP A 209    13350  16545  15325  -1095    640   3227       O  
-ATOM   1485  N   MET A 210      24.475 -13.349   1.882  1.00106.68           N  
-ANISOU 1485  N   MET A 210    12166  14578  13791  -1721   -355   2701       N  
-ATOM   1486  CA  MET A 210      23.383 -12.983   2.777  1.00 96.59           C  
-ANISOU 1486  CA  MET A 210    11046  13168  12487  -1736   -553   2476       C  
-ATOM   1487  C   MET A 210      22.912 -11.551   2.551  1.00 93.56           C  
-ANISOU 1487  C   MET A 210    10882  12608  12057  -1891   -728   2401       C  
-ATOM   1488  O   MET A 210      21.713 -11.276   2.564  1.00 91.17           O  
-ANISOU 1488  O   MET A 210    10801  12146  11695  -1825   -812   2201       O  
-ATOM   1489  CB  MET A 210      23.787 -13.193   4.240  1.00 92.70           C  
-ANISOU 1489  CB  MET A 210    10376  12792  12054  -1806   -666   2501       C  
-ATOM   1490  CG  MET A 210      24.199 -14.619   4.550  1.00 85.45           C  
-ANISOU 1490  CG  MET A 210     9241  12043  11182  -1640   -492   2575       C  
-ATOM   1491  SD  MET A 210      23.025 -15.799   3.863  1.00 78.76           S  
-ANISOU 1491  SD  MET A 210     8543  11097  10286  -1351   -320   2394       S  
-ATOM   1492  CE  MET A 210      21.584 -15.443   4.871  1.00 75.56           C  
-ANISOU 1492  CE  MET A 210     8326  10536   9847  -1334   -538   2130       C  
-ATOM   1493  N   GLY A 211      23.860 -10.642   2.345  1.00 79.91           N  
-ANISOU 1493  N   GLY A 211     9089  10910  10363  -2097   -779   2573       N  
-ATOM   1494  CA  GLY A 211      23.536  -9.253   2.084  1.00 76.56           C  
-ANISOU 1494  CA  GLY A 211     8871  10314   9906  -2256   -931   2527       C  
-ATOM   1495  C   GLY A 211      22.612  -9.089   0.891  1.00 75.93           C  
-ANISOU 1495  C   GLY A 211     9022  10087   9742  -2126   -851   2421       C  
-ATOM   1496  O   GLY A 211      21.772  -8.190   0.866  1.00 77.04           O  
-ANISOU 1496  O   GLY A 211     9391  10051   9830  -2166   -982   2288       O  
-ATOM   1497  N   LYS A 212      22.764  -9.963  -0.100  1.00 83.02           N  
-ANISOU 1497  N   LYS A 212     9866  11060  10619  -1963   -635   2482       N  
-ATOM   1498  CA  LYS A 212      21.945  -9.904  -1.307  1.00 82.92           C  
-ANISOU 1498  CA  LYS A 212    10062  10929  10515  -1833   -551   2391       C  
-ATOM   1499  C   LYS A 212      20.677 -10.734  -1.150  1.00 77.46           C  
-ANISOU 1499  C   LYS A 212     9491  10172   9769  -1631   -543   2167       C  
-ATOM   1500  O   LYS A 212      19.689 -10.519  -1.853  1.00 74.63           O  
-ANISOU 1500  O   LYS A 212     9341   9687   9328  -1545   -549   2040       O  
-ATOM   1501  CB  LYS A 212      22.745 -10.373  -2.523  1.00 87.81           C  
-ANISOU 1501  CB  LYS A 212    10591  11652  11122  -1758   -324   2570       C  
-ATOM   1502  CG  LYS A 212      24.016  -9.569  -2.770  1.00 97.07           C  
-ANISOU 1502  CG  LYS A 212    11626  12900  12357  -1952   -316   2823       C  
-ATOM   1503  CD  LYS A 212      23.707  -8.091  -2.974  1.00103.46           C  
-ANISOU 1503  CD  LYS A 212    12618  13545  13148  -2124   -475   2799       C  
-ATOM   1504  CE  LYS A 212      24.978  -7.270  -3.133  1.00108.48           C  
-ANISOU 1504  CE  LYS A 212    13107  14249  13863  -2343   -486   3058       C  
-ATOM   1505  NZ  LYS A 212      25.833  -7.332  -1.918  1.00113.43           N  
-ANISOU 1505  NZ  LYS A 212    13507  14999  14593  -2505   -590   3157       N  
-ATOM   1506  N   LEU A 213      20.720 -11.685  -0.221  1.00 89.36           N  
-ANISOU 1506  N   LEU A 213    10855  11772  11325  -1560   -530   2132       N  
-ATOM   1507  CA  LEU A 213      19.555 -12.488   0.125  1.00 83.68           C  
-ANISOU 1507  CA  LEU A 213    10221  10997  10576  -1388   -538   1933       C  
-ATOM   1508  C   LEU A 213      18.531 -11.614   0.830  1.00 82.73           C  
-ANISOU 1508  C   LEU A 213    10275  10731  10428  -1442   -749   1772       C  
-ATOM   1509  O   LEU A 213      17.330 -11.743   0.608  1.00 79.71           O  
-ANISOU 1509  O   LEU A 213    10056  10241   9988  -1323   -776   1611       O  
-ATOM   1510  CB  LEU A 213      19.956 -13.637   1.048  1.00 82.52           C  
-ANISOU 1510  CB  LEU A 213     9862  10990  10501  -1313   -476   1961       C  
-ATOM   1511  CG  LEU A 213      19.026 -14.848   1.043  1.00 78.01           C  
-ANISOU 1511  CG  LEU A 213     9332  10394   9913  -1101   -393   1813       C  
-ATOM   1512  CD1 LEU A 213      19.125 -15.567  -0.295  1.00 77.50           C  
-ANISOU 1512  CD1 LEU A 213     9310  10337   9798   -970   -189   1844       C  
-ATOM   1513  CD2 LEU A 213      19.368 -15.789   2.179  1.00 79.44           C  
-ANISOU 1513  CD2 LEU A 213     9311  10698  10173  -1048   -365   1838       C  
-ATOM   1514  N   ARG A 214      19.019 -10.721   1.682  1.00 76.76           N  
-ANISOU 1514  N   ARG A 214     9484   9971   9709  -1621   -900   1822       N  
-ATOM   1515  CA  ARG A 214      18.153  -9.807   2.413  1.00 78.88           C  
-ANISOU 1515  CA  ARG A 214     9932  10096   9944  -1675  -1098   1681       C  
-ATOM   1516  C   ARG A 214      17.532  -8.772   1.484  1.00 81.24           C  
-ANISOU 1516  C   ARG A 214    10468  10231  10168  -1702  -1138   1636       C  
-ATOM   1517  O   ARG A 214      16.507  -8.177   1.807  1.00 81.04           O  
-ANISOU 1517  O   ARG A 214    10631  10067  10092  -1675  -1259   1499       O  
-ATOM   1518  CB  ARG A 214      18.930  -9.118   3.537  1.00 79.70           C  
-ANISOU 1518  CB  ARG A 214     9952  10234  10096  -1872  -1250   1749       C  
-ATOM   1519  CG  ARG A 214      19.652 -10.088   4.456  1.00 79.61           C  
-ANISOU 1519  CG  ARG A 214     9686  10406  10155  -1855  -1212   1820       C  
-ATOM   1520  CD  ARG A 214      20.488  -9.384   5.512  1.00 80.52           C  
-ANISOU 1520  CD  ARG A 214     9715  10570  10310  -2067  -1376   1897       C  
-ATOM   1521  NE  ARG A 214      21.359 -10.325   6.214  1.00 81.92           N  
-ANISOU 1521  NE  ARG A 214     9615  10954  10555  -2057  -1316   2010       N  
-ATOM   1522  CZ  ARG A 214      21.001 -11.028   7.284  1.00 81.28           C  
-ANISOU 1522  CZ  ARG A 214     9466  10934  10482  -1954  -1349   1927       C  
-ATOM   1523  NH1 ARG A 214      19.782 -10.895   7.789  1.00 80.00           N  
-ANISOU 1523  NH1 ARG A 214     9490  10642  10265  -1852  -1441   1732       N  
-ATOM   1524  NH2 ARG A 214      21.864 -11.862   7.853  1.00 83.56           N  
-ANISOU 1524  NH2 ARG A 214     9494  11421  10833  -1945  -1283   2052       N  
-ATOM   1525  N   GLN A 215      18.158  -8.562   0.329  1.00 80.88           N  
-ANISOU 1525  N   GLN A 215    10410  10208  10114  -1744  -1027   1765       N  
-ATOM   1526  CA  GLN A 215      17.620  -7.652  -0.676  1.00 82.59           C  
-ANISOU 1526  CA  GLN A 215    10839  10284  10257  -1754  -1040   1742       C  
-ATOM   1527  C   GLN A 215      16.393  -8.258  -1.341  1.00 76.52           C  
-ANISOU 1527  C   GLN A 215    10204   9462   9409  -1546   -977   1597       C  
-ATOM   1528  O   GLN A 215      15.332  -7.638  -1.386  1.00 74.24           O  
-ANISOU 1528  O   GLN A 215    10112   9038   9059  -1509  -1073   1478       O  
-ATOM   1529  CB  GLN A 215      18.677  -7.314  -1.732  1.00 92.82           C  
-ANISOU 1529  CB  GLN A 215    12069  11633  11564  -1845   -925   1937       C  
-ATOM   1530  CG  GLN A 215      19.904  -6.595  -1.191  1.00108.20           C  
-ANISOU 1530  CG  GLN A 215    13885  13630  13597  -2078   -999   2104       C  
-ATOM   1531  CD  GLN A 215      19.574  -5.234  -0.615  1.00117.38           C  
-ANISOU 1531  CD  GLN A 215    15222  14626  14752  -2240  -1203   2045       C  
-ATOM   1532  OE1 GLN A 215      18.454  -4.744  -0.754  1.00124.59           O  
-ANISOU 1532  OE1 GLN A 215    16361  15386  15592  -2167  -1268   1899       O  
-ATOM   1533  NE2 GLN A 215      20.552  -4.614   0.036  1.00124.05           N  
-ANISOU 1533  NE2 GLN A 215    15965  15498  15669  -2461  -1304   2164       N  
-ATOM   1534  N   ILE A 216      16.544  -9.476  -1.850  1.00 73.98           N  
-ANISOU 1534  N   ILE A 216     9777   9246   9087  -1412   -818   1612       N  
-ATOM   1535  CA  ILE A 216      15.442 -10.176  -2.497  1.00 66.17           C  
-ANISOU 1535  CA  ILE A 216     8902   8215   8026  -1228   -761   1477       C  
-ATOM   1536  C   ILE A 216      14.255 -10.335  -1.556  1.00 60.57           C  
-ANISOU 1536  C   ILE A 216     8261   7438   7316  -1153   -888   1307       C  
-ATOM   1537  O   ILE A 216      13.105 -10.211  -1.975  1.00 58.65           O  
-ANISOU 1537  O   ILE A 216     8179   7103   7004  -1061   -929   1194       O  
-ATOM   1538  CB  ILE A 216      15.865 -11.573  -2.993  1.00 66.83           C  
-ANISOU 1538  CB  ILE A 216     8857   8418   8118  -1100   -574   1513       C  
-ATOM   1539  CG1 ILE A 216      17.154 -11.482  -3.803  1.00 67.51           C  
-ANISOU 1539  CG1 ILE A 216     8846   8594   8210  -1159   -431   1708       C  
-ATOM   1540  CG2 ILE A 216      14.755 -12.203  -3.825  1.00 65.75           C  
-ANISOU 1540  CG2 ILE A 216     8865   8222   7894   -936   -528   1376       C  
-ATOM   1541  CD1 ILE A 216      17.023 -10.622  -5.034  1.00 69.18           C  
-ANISOU 1541  CD1 ILE A 216     9221   8730   8334  -1180   -411   1747       C  
-ATOM   1542  N   ILE A 217      14.542 -10.615  -0.287  1.00 51.76           N  
-ANISOU 1542  N   ILE A 217     7014   6377   6276  -1187   -947   1303       N  
-ATOM   1543  CA  ILE A 217      13.501 -10.807   0.713  1.00 46.21           C  
-ANISOU 1543  CA  ILE A 217     6355   5625   5579  -1106  -1056   1162       C  
-ATOM   1544  C   ILE A 217      12.806  -9.494   1.042  1.00 48.65           C  
-ANISOU 1544  C   ILE A 217     6856   5790   5839  -1167  -1219   1099       C  
-ATOM   1545  O   ILE A 217      11.577  -9.422   1.084  1.00 45.08           O  
-ANISOU 1545  O   ILE A 217     6535   5254   5339  -1060  -1277    983       O  
-ATOM   1546  CB  ILE A 217      14.066 -11.400   2.019  1.00 40.17           C  
-ANISOU 1546  CB  ILE A 217     5399   4965   4899  -1125  -1075   1186       C  
-ATOM   1547  CG1 ILE A 217      14.776 -12.726   1.747  1.00 34.13           C  
-ANISOU 1547  CG1 ILE A 217     4442   4341   4186  -1051   -900   1260       C  
-ATOM   1548  CG2 ILE A 217      12.945 -11.598   3.052  1.00 34.74           C  
-ANISOU 1548  CG2 ILE A 217     4760   4227   4211  -1024  -1179   1048       C  
-ATOM   1549  CD1 ILE A 217      15.232 -13.430   3.003  1.00 32.40           C  
-ANISOU 1549  CD1 ILE A 217     4029   4235   4048  -1040   -905   1285       C  
-ATOM   1550  N   GLN A 218      13.599  -8.457   1.292  1.00 70.20           N  
-ANISOU 1550  N   GLN A 218     9601   8490   8581  -1341  -1292   1184       N  
-ATOM   1551  CA  GLN A 218      13.056  -7.128   1.548  1.00 74.37           C  
-ANISOU 1551  CA  GLN A 218    10335   8863   9059  -1409  -1436   1136       C  
-ATOM   1552  C   GLN A 218      12.295  -6.626   0.329  1.00 73.14           C  
-ANISOU 1552  C   GLN A 218    10362   8607   8821  -1347  -1406   1111       C  
-ATOM   1553  O   GLN A 218      11.258  -5.975   0.459  1.00 70.93           O  
-ANISOU 1553  O   GLN A 218    10263   8205   8482  -1290  -1494   1023       O  
-ATOM   1554  CB  GLN A 218      14.167  -6.144   1.907  1.00 85.22           C  
-ANISOU 1554  CB  GLN A 218    11691  10219  10469  -1630  -1513   1244       C  
-ATOM   1555  CG  GLN A 218      13.690  -4.708   2.049  1.00 98.49           C  
-ANISOU 1555  CG  GLN A 218    13611  11715  12094  -1711  -1650   1202       C  
-ATOM   1556  CD  GLN A 218      14.836  -3.716   2.104  1.00110.46           C  
-ANISOU 1556  CD  GLN A 218    15123  13199  13649  -1950  -1713   1326       C  
-ATOM   1557  OE1 GLN A 218      15.923  -4.032   2.592  1.00115.75           O  
-ANISOU 1557  OE1 GLN A 218    15601  13987  14390  -2070  -1715   1420       O  
-ATOM   1558  NE2 GLN A 218      14.603  -2.510   1.590  1.00118.55           N  
-ANISOU 1558  NE2 GLN A 218    16353  14063  14628  -2024  -1765   1336       N  
-ATOM   1559  N   ARG A 219      12.822  -6.930  -0.855  1.00 65.73           N  
-ANISOU 1559  N   ARG A 219     9375   7727   7871  -1348  -1274   1198       N  
-ATOM   1560  CA  ARG A 219      12.138  -6.609  -2.101  1.00 64.88           C  
-ANISOU 1560  CA  ARG A 219     9425   7551   7676  -1273  -1230   1180       C  
-ATOM   1561  C   ARG A 219      10.784  -7.302  -2.156  1.00 61.04           C  
-ANISOU 1561  C   ARG A 219     9002   7048   7141  -1090  -1239   1041       C  
-ATOM   1562  O   ARG A 219       9.839  -6.801  -2.767  1.00 61.78           O  
-ANISOU 1562  O   ARG A 219     9262   7057   7156  -1023  -1272    992       O  
-ATOM   1563  CB  ARG A 219      12.972  -7.031  -3.311  1.00 68.23           C  
-ANISOU 1563  CB  ARG A 219     9771   8063   8089  -1279  -1071   1295       C  
-ATOM   1564  CG  ARG A 219      14.147  -6.117  -3.618  1.00 75.03           C  
-ANISOU 1564  CG  ARG A 219    10606   8921   8981  -1455  -1057   1458       C  
-ATOM   1565  CD  ARG A 219      14.555  -6.217  -5.081  1.00 80.26           C  
-ANISOU 1565  CD  ARG A 219    11280   9626   9590  -1420   -907   1560       C  
-ATOM   1566  NE  ARG A 219      13.500  -5.741  -5.976  1.00 85.15           N  
-ANISOU 1566  NE  ARG A 219    12106  10146  10100  -1328   -921   1489       N  
-ATOM   1567  CZ  ARG A 219      12.881  -6.498  -6.878  1.00 87.76           C  
-ANISOU 1567  CZ  ARG A 219    12485  10512  10349  -1172   -836   1427       C  
-ATOM   1568  NH1 ARG A 219      13.215  -7.775  -7.015  1.00 89.62           N  
-ANISOU 1568  NH1 ARG A 219    12591  10862  10598  -1087   -721   1421       N  
-ATOM   1569  NH2 ARG A 219      11.934  -5.973  -7.648  1.00 89.37           N  
-ANISOU 1569  NH2 ARG A 219    12872  10634  10451  -1101   -866   1375       N  
-ATOM   1570  N   GLY A 220      10.700  -8.463  -1.518  1.00 63.86           N  
-ANISOU 1570  N   GLY A 220     9218   7493   7551  -1010  -1209    988       N  
-ATOM   1571  CA  GLY A 220       9.476  -9.239  -1.510  1.00 59.60           C  
-ANISOU 1571  CA  GLY A 220     8710   6949   6987   -849  -1217    869       C  
-ATOM   1572  C   GLY A 220       8.376  -8.553  -0.730  1.00 56.02           C  
-ANISOU 1572  C   GLY A 220     8381   6395   6510   -805  -1357    786       C  
-ATOM   1573  O   GLY A 220       7.197  -8.837  -0.920  1.00 52.64           O  
-ANISOU 1573  O   GLY A 220     8020   5939   6042   -681  -1383    707       O  
-ATOM   1574  N   GLY A 221       8.763  -7.632   0.142  1.00 71.85           N  
-ANISOU 1574  N   GLY A 221    10421   8344   8535   -907  -1449    811       N  
-ATOM   1575  CA  GLY A 221       7.824  -7.022   1.062  1.00 69.52           C  
-ANISOU 1575  CA  GLY A 221    10243   7955   8215   -853  -1573    736       C  
-ATOM   1576  C   GLY A 221       7.677  -7.917   2.278  1.00 66.11           C  
-ANISOU 1576  C   GLY A 221     9673   7597   7849   -784  -1592    684       C  
-ATOM   1577  O   GLY A 221       6.600  -8.029   2.862  1.00 64.30           O  
-ANISOU 1577  O   GLY A 221     9490   7335   7605   -659  -1648    612       O  
-ATOM   1578  N   ILE A 222       8.779  -8.560   2.650  1.00 51.28           N  
-ANISOU 1578  N   ILE A 222     7613   5826   6044   -857  -1538    738       N  
-ATOM   1579  CA  ILE A 222       8.800  -9.512   3.751  1.00 49.82           C  
-ANISOU 1579  CA  ILE A 222     7271   5731   5927   -793  -1536    708       C  
-ATOM   1580  C   ILE A 222       9.826  -9.080   4.793  1.00 51.82           C  
-ANISOU 1580  C   ILE A 222     7455   6017   6219   -927  -1601    758       C  
-ATOM   1581  O   ILE A 222      11.025  -9.038   4.504  1.00 53.05           O  
-ANISOU 1581  O   ILE A 222     7512   6235   6408  -1060  -1555    855       O  
-ATOM   1582  CB  ILE A 222       9.187 -10.907   3.238  1.00 45.94           C  
-ANISOU 1582  CB  ILE A 222     6603   5362   5492   -737  -1393    733       C  
-ATOM   1583  CG1 ILE A 222       8.257 -11.329   2.099  1.00 42.96           C  
-ANISOU 1583  CG1 ILE A 222     6306   4950   5066   -629  -1338    681       C  
-ATOM   1584  CG2 ILE A 222       9.160 -11.915   4.370  1.00 45.33           C  
-ANISOU 1584  CG2 ILE A 222     6361   5372   5489   -659  -1381    708       C  
-ATOM   1585  CD1 ILE A 222       8.545 -12.699   1.559  1.00 37.34           C  
-ANISOU 1585  CD1 ILE A 222     5462   4331   4396   -567  -1201    688       C  
-ATOM   1586  N   LEU A 223       9.371  -8.761   6.002  1.00 54.30           N  
-ANISOU 1586  N   LEU A 223     7817   6292   6521   -891  -1709    699       N  
-ATOM   1587  CA  LEU A 223      10.285  -8.204   6.999  1.00 57.90           C  
-ANISOU 1587  CA  LEU A 223     8244   6763   6992  -1032  -1800    735       C  
-ATOM   1588  C   LEU A 223      11.156  -9.261   7.662  1.00 59.27           C  
-ANISOU 1588  C   LEU A 223     8167   7105   7247  -1045  -1745    789       C  
-ATOM   1589  O   LEU A 223      10.663 -10.276   8.147  1.00 57.85           O  
-ANISOU 1589  O   LEU A 223     7882   6997   7102   -899  -1698    750       O  
-ATOM   1590  CB  LEU A 223       9.556  -7.348   8.049  1.00 56.91           C  
-ANISOU 1590  CB  LEU A 223     8297   6523   6802   -994  -1942    653       C  
-ATOM   1591  CG  LEU A 223       8.734  -8.009   9.154  1.00 54.03           C  
-ANISOU 1591  CG  LEU A 223     7889   6198   6443   -819  -1963    582       C  
-ATOM   1592  CD1 LEU A 223       9.104  -7.431  10.516  1.00 50.16           C  
-ANISOU 1592  CD1 LEU A 223     7446   5690   5921   -881  -2091    560       C  
-ATOM   1593  CD2 LEU A 223       7.250  -7.839   8.879  1.00 53.04           C  
-ANISOU 1593  CD2 LEU A 223     7916   5973   6262   -645  -1967    512       C  
-ATOM   1594  N   ILE A 224      12.459  -9.003   7.669  1.00 62.21           N  
-ANISOU 1594  N   ILE A 224     8440   7543   7653  -1221  -1750    892       N  
-ATOM   1595  CA  ILE A 224      13.432  -9.920   8.238  1.00 66.04           C  
-ANISOU 1595  CA  ILE A 224     8675   8203   8214  -1249  -1693    972       C  
-ATOM   1596  C   ILE A 224      13.266 -10.039   9.748  1.00 67.35           C  
-ANISOU 1596  C   ILE A 224     8805   8406   8378  -1209  -1795    920       C  
-ATOM   1597  O   ILE A 224      12.571  -9.241  10.378  1.00 67.57           O  
-ANISOU 1597  O   ILE A 224     9017   8318   8340  -1192  -1922    832       O  
-ATOM   1598  CB  ILE A 224      14.864  -9.450   7.955  1.00 68.79           C  
-ANISOU 1598  CB  ILE A 224     8927   8615   8596  -1463  -1696   1114       C  
-ATOM   1599  CG1 ILE A 224      14.955  -8.823   6.563  1.00 71.94           C  
-ANISOU 1599  CG1 ILE A 224     9437   8928   8969  -1530  -1643   1160       C  
-ATOM   1600  CG2 ILE A 224      15.839 -10.603   8.094  1.00 67.61           C  
-ANISOU 1600  CG2 ILE A 224     8496   8664   8528  -1454  -1575   1228       C  
-ATOM   1601  CD1 ILE A 224      14.652  -9.784   5.440  1.00 75.40           C  
-ANISOU 1601  CD1 ILE A 224     9823   9408   9416  -1388  -1467   1167       C  
-ATOM   1602  N   THR A 225      13.914 -11.045  10.321  1.00 56.36           N  
-ANISOU 1602  N   THR A 225     7181   7181   7053  -1183  -1731    983       N  
-ATOM   1603  CA  THR A 225      13.922 -11.232  11.759  1.00 57.76           C  
-ANISOU 1603  CA  THR A 225     7295   7424   7229  -1149  -1819    955       C  
-ATOM   1604  C   THR A 225      15.184 -11.979  12.132  1.00 61.30           C  
-ANISOU 1604  C   THR A 225     7472   8069   7750  -1219  -1758   1085       C  
-ATOM   1605  O   THR A 225      15.355 -13.143  11.778  1.00 59.85           O  
-ANISOU 1605  O   THR A 225     7115   7993   7634  -1116  -1599   1138       O  
-ATOM   1606  CB  THR A 225      12.707 -12.028  12.219  1.00 55.12           C  
-ANISOU 1606  CB  THR A 225     6969   7079   6896   -917  -1777    859       C  
-ATOM   1607  OG1 THR A 225      11.517 -11.357  11.792  1.00 52.92           O  
-ANISOU 1607  OG1 THR A 225     6926   6631   6551   -844  -1823    758       O  
-ATOM   1608  CG2 THR A 225      12.701 -12.169  13.737  1.00 53.53           C  
-ANISOU 1608  CG2 THR A 225     6712   6947   6681   -869  -1866    835       C  
-ATOM   1609  N   GLU A 226      16.076 -11.293  12.833  1.00 72.91           N  
-ANISOU 1609  N   GLU A 226     8914   9585   9205  -1397  -1887   1142       N  
-ATOM   1610  CA  GLU A 226      17.361 -11.863  13.198  1.00 79.41           C  
-ANISOU 1610  CA  GLU A 226     9470  10608  10093  -1488  -1849   1290       C  
-ATOM   1611  C   GLU A 226      17.207 -12.884  14.312  1.00 79.53           C  
-ANISOU 1611  C   GLU A 226     9328  10756  10132  -1336  -1820   1278       C  
-ATOM   1612  O   GLU A 226      16.418 -12.692  15.241  1.00 78.95           O  
-ANISOU 1612  O   GLU A 226     9369  10626  10003  -1248  -1920   1166       O  
-ATOM   1613  CB  GLU A 226      18.331 -10.757  13.610  1.00 85.13           C  
-ANISOU 1613  CB  GLU A 226    10216  11337  10792  -1746  -2019   1357       C  
-ATOM   1614  CG  GLU A 226      18.553  -9.725  12.523  1.00 93.43           C  
-ANISOU 1614  CG  GLU A 226    11412  12256  11830  -1906  -2044   1387       C  
-ATOM   1615  CD  GLU A 226      18.965 -10.355  11.208  1.00 97.98           C  
-ANISOU 1615  CD  GLU A 226    11860  12896  12472  -1873  -1843   1500       C  
-ATOM   1616  OE1 GLU A 226      19.581 -11.443  11.237  1.00101.60           O  
-ANISOU 1616  OE1 GLU A 226    12072  13535  12997  -1807  -1709   1607       O  
-ATOM   1617  OE2 GLU A 226      18.667  -9.768  10.147  1.00101.46           O  
-ANISOU 1617  OE2 GLU A 226    12454  13207  12891  -1901  -1814   1485       O  
-ATOM   1618  N   ARG A 227      17.965 -13.970  14.208  1.00 87.00           N  
-ANISOU 1618  N   ARG A 227    10015  11880  11160  -1293  -1672   1404       N  
-ATOM   1619  CA  ARG A 227      17.869 -15.068  15.159  1.00 86.95           C  
-ANISOU 1619  CA  ARG A 227     9837  12010  11190  -1135  -1611   1415       C  
-ATOM   1620  C   ARG A 227      19.220 -15.731  15.389  1.00 90.75           C  
-ANISOU 1620  C   ARG A 227    10026  12716  11739  -1198  -1532   1601       C  
-ATOM   1621  O   ARG A 227      20.025 -15.860  14.471  1.00 89.64           O  
-ANISOU 1621  O   ARG A 227     9783  12631  11644  -1274  -1425   1726       O  
-ATOM   1622  CB  ARG A 227      16.846 -16.096  14.676  1.00 82.14           C  
-ANISOU 1622  CB  ARG A 227     9243  11348  10620   -904  -1450   1342       C  
-ATOM   1623  CG  ARG A 227      15.410 -15.673  14.890  1.00 78.13           C  
-ANISOU 1623  CG  ARG A 227     8967  10668  10051   -794  -1535   1173       C  
-ATOM   1624  CD  ARG A 227      14.857 -16.256  16.180  1.00 75.86           C  
-ANISOU 1624  CD  ARG A 227     8619  10441   9764   -636  -1560   1128       C  
-ATOM   1625  NE  ARG A 227      13.980 -15.319  16.877  1.00 74.45           N  
-ANISOU 1625  NE  ARG A 227     8660  10138   9490   -616  -1725   1006       N  
-ATOM   1626  CZ  ARG A 227      13.207 -15.645  17.908  1.00 72.29           C  
-ANISOU 1626  CZ  ARG A 227     8396   9874   9197   -453  -1754    947       C  
-ATOM   1627  NH1 ARG A 227      13.191 -16.893  18.356  1.00 70.69           N  
-ANISOU 1627  NH1 ARG A 227     7991   9798   9071   -305  -1633    997       N  
-ATOM   1628  NH2 ARG A 227      12.444 -14.725  18.484  1.00 70.62           N  
-ANISOU 1628  NH2 ARG A 227     8403   9544   8887   -427  -1895    845       N  
-ATOM   1629  N   LYS A 228      19.453 -16.151  16.627  1.00 90.56           N  
-ANISOU 1629  N   LYS A 228     9865  12829  11716  -1154  -1581   1628       N  
-ATOM   1630  CA  LYS A 228      20.709 -16.777  17.015  1.00 95.39           C  
-ANISOU 1630  CA  LYS A 228    10184  13674  12384  -1204  -1519   1815       C  
-ATOM   1631  C   LYS A 228      21.141 -17.820  15.993  1.00 95.31           C  
-ANISOU 1631  C   LYS A 228    10011  13738  12463  -1109  -1269   1934       C  
-ATOM   1632  O   LYS A 228      20.323 -18.600  15.511  1.00 93.90           O  
-ANISOU 1632  O   LYS A 228     9885  13480  12313   -922  -1125   1858       O  
-ATOM   1633  CB  LYS A 228      20.568 -17.432  18.392  1.00100.45           C  
-ANISOU 1633  CB  LYS A 228    10705  14444  13019  -1077  -1548   1807       C  
-ATOM   1634  CG  LYS A 228      19.655 -16.684  19.359  1.00108.59           C  
-ANISOU 1634  CG  LYS A 228    11951  15358  13951  -1058  -1743   1639       C  
-ATOM   1635  CD  LYS A 228      20.203 -15.308  19.714  1.00116.60           C  
-ANISOU 1635  CD  LYS A 228    13086  16336  14882  -1311  -1980   1629       C  
-ATOM   1636  CE  LYS A 228      19.241 -14.551  20.619  1.00119.75           C  
-ANISOU 1636  CE  LYS A 228    13737  16596  15166  -1269  -2158   1453       C  
-ATOM   1637  NZ  LYS A 228      19.748 -13.198  20.980  1.00122.84           N  
-ANISOU 1637  NZ  LYS A 228    14279  16926  15469  -1519  -2394   1429       N  
-ATOM   1638  N   LYS A 229      22.430 -17.829  15.670  1.00 82.62           N  
-ANISOU 1638  N   LYS A 229     8211  12282  10898  -1239  -1219   2128       N  
-ATOM   1639  CA  LYS A 229      22.990 -18.831  14.769  1.00 83.99           C  
-ANISOU 1639  CA  LYS A 229     8220  12546  11147  -1140   -969   2267       C  
-ATOM   1640  C   LYS A 229      22.653 -20.233  15.268  1.00 80.27           C  
-ANISOU 1640  C   LYS A 229     7618  12154  10726   -898   -808   2266       C  
-ATOM   1641  O   LYS A 229      22.586 -21.186  14.494  1.00 78.20           O  
-ANISOU 1641  O   LYS A 229     7315  11884  10514   -749   -590   2298       O  
-ATOM   1642  CB  LYS A 229      24.510 -18.674  14.671  1.00 90.30           C  
-ANISOU 1642  CB  LYS A 229     8782  13543  11983  -1304   -951   2510       C  
-ATOM   1643  CG  LYS A 229      24.983 -17.273  14.310  1.00 98.81           C  
-ANISOU 1643  CG  LYS A 229     9958  14560  13027  -1572  -1126   2540       C  
-ATOM   1644  CD  LYS A 229      26.497 -17.241  14.136  1.00106.84           C  
-ANISOU 1644  CD  LYS A 229    10708  15788  14097  -1723  -1084   2810       C  
-ATOM   1645  CE  LYS A 229      27.010 -15.835  13.860  1.00112.75           C  
-ANISOU 1645  CE  LYS A 229    11538  16478  14823  -2011  -1273   2855       C  
-ATOM   1646  NZ  LYS A 229      26.866 -14.944  15.045  1.00116.45           N  
-ANISOU 1646  NZ  LYS A 229    12098  16917  15232  -2175  -1557   2756       N  
-ATOM   1647  N   ALA A 230      22.440 -20.345  16.573  1.00108.14           N  
-ANISOU 1647  N   ALA A 230    11093  15757  14239   -859   -916   2229       N  
-ATOM   1648  CA  ALA A 230      22.143 -21.625  17.197  1.00104.16           C  
-ANISOU 1648  CA  ALA A 230    10454  15337  13786   -636   -776   2241       C  
-ATOM   1649  C   ALA A 230      20.774 -22.153  16.784  1.00101.43           C  
-ANISOU 1649  C   ALA A 230    10286  14800  13451   -449   -691   2066       C  
-ATOM   1650  O   ALA A 230      20.616 -23.346  16.530  1.00 99.81           O  
-ANISOU 1650  O   ALA A 230     9996  14614  13315   -272   -490   2095       O  
-ATOM   1651  CB  ALA A 230      22.224 -21.499  18.705  1.00101.46           C  
-ANISOU 1651  CB  ALA A 230    10025  15118  13409   -645   -929   2243       C  
-ATOM   1652  N   ASP A 231      19.790 -21.261  16.723  1.00 94.58           N  
-ANISOU 1652  N   ASP A 231     9667  13750  12518   -492   -846   1892       N  
-ATOM   1653  CA  ASP A 231      18.412 -21.642  16.421  1.00 92.25           C  
-ANISOU 1653  CA  ASP A 231     9540  13281  12228   -331   -800   1730       C  
-ATOM   1654  C   ASP A 231      18.288 -22.533  15.188  1.00 91.09           C  
-ANISOU 1654  C   ASP A 231     9395  13073  12141   -230   -584   1743       C  
-ATOM   1655  O   ASP A 231      17.325 -23.285  15.058  1.00 92.32           O  
-ANISOU 1655  O   ASP A 231     9610  13136  12332    -71   -501   1651       O  
-ATOM   1656  CB  ASP A 231      17.535 -20.399  16.252  1.00 91.93           C  
-ANISOU 1656  CB  ASP A 231     9772  13055  12102   -417   -984   1573       C  
-ATOM   1657  CG  ASP A 231      17.317 -19.654  17.558  1.00 92.06           C  
-ANISOU 1657  CG  ASP A 231     9842  13090  12048   -458  -1188   1517       C  
-ATOM   1658  OD1 ASP A 231      16.337 -18.880  17.645  1.00 90.89           O  
-ANISOU 1658  OD1 ASP A 231     9919  12783  11832   -452  -1312   1376       O  
-ATOM   1659  OD2 ASP A 231      18.124 -19.843  18.494  1.00 92.00           O  
-ANISOU 1659  OD2 ASP A 231     9656  13255  12043   -489  -1221   1618       O  
-ATOM   1660  N   PHE A 232      19.262 -22.450  14.289  1.00 77.78           N  
-ANISOU 1660  N   PHE A 232     7586  10811  11156   1678    310   2121       N  
-ATOM   1661  CA  PHE A 232      19.229 -23.236  13.058  1.00 78.93           C  
-ANISOU 1661  CA  PHE A 232     8365  10557  11067   1812    489   2198       C  
-ATOM   1662  C   PHE A 232      19.846 -24.627  13.210  1.00 82.47           C  
-ANISOU 1662  C   PHE A 232     9120  10952  11261   2168    821   2407       C  
-ATOM   1663  O   PHE A 232      20.050 -25.328  12.220  1.00 82.87           O  
-ANISOU 1663  O   PHE A 232     9670  10713  11104   2338   1021   2511       O  
-ATOM   1664  CB  PHE A 232      19.910 -22.481  11.909  1.00 75.91           C  
-ANISOU 1664  CB  PHE A 232     8008  10135  10701   1867    560   2281       C  
-ATOM   1665  CG  PHE A 232      19.075 -21.366  11.332  1.00 70.62           C  
-ANISOU 1665  CG  PHE A 232     7282   9341  10211   1515    250   2065       C  
-ATOM   1666  CD1 PHE A 232      19.082 -20.106  11.909  1.00 68.08           C  
-ANISOU 1666  CD1 PHE A 232     6385   9323  10159   1311     24   1962       C  
-ATOM   1667  CD2 PHE A 232      18.290 -21.577  10.208  1.00 67.77           C  
-ANISOU 1667  CD2 PHE A 232     7443   8559   9749   1389    184   1966       C  
-ATOM   1668  CE1 PHE A 232      18.319 -19.085  11.384  1.00 66.17           C  
-ANISOU 1668  CE1 PHE A 232     6092   8966  10084    991   -260   1766       C  
-ATOM   1669  CE2 PHE A 232      17.527 -20.555   9.677  1.00 62.99           C  
-ANISOU 1669  CE2 PHE A 232     6787   7840   9307   1070   -102   1771       C  
-ATOM   1670  CZ  PHE A 232      17.541 -19.308  10.267  1.00 63.69           C  
-ANISOU 1670  CZ  PHE A 232     6301   8233   9666    872   -324   1671       C  
-ATOM   1671  N   SER A 233      20.135 -25.024  14.448  1.00 90.00           N  
-ANISOU 1671  N   SER A 233     9777  12186  12231   2278    878   2467       N  
-ATOM   1672  CA  SER A 233      20.742 -26.328  14.717  1.00 94.80           C  
-ANISOU 1672  CA  SER A 233    10632  12776  12610   2618   1188   2669       C  
-ATOM   1673  C   SER A 233      19.694 -27.431  14.740  1.00 96.83           C  
-ANISOU 1673  C   SER A 233    11378  12695  12719   2549   1162   2572       C  
-ATOM   1674  O   SER A 233      18.529 -27.182  15.038  1.00 95.62           O  
-ANISOU 1674  O   SER A 233    11213  12443  12675   2236    885   2345       O  
-ATOM   1675  CB  SER A 233      21.511 -26.312  16.039  1.00 96.50           C  
-ANISOU 1675  CB  SER A 233    10329  13437  12900   2775   1267   2781       C  
-ATOM   1676  OG  SER A 233      20.638 -26.147  17.140  1.00 97.52           O  
-ANISOU 1676  OG  SER A 233    10188  13692  13173   2532   1018   2601       O  
-ATOM   1677  N   THR A 234      20.117 -28.652  14.437  1.00 89.92           N  
-ANISOU 1677  N   THR A 234    10925  11646  11594   2842   1454   2744       N  
-ATOM   1678  CA  THR A 234      19.189 -29.768  14.302  1.00 93.67           C  
-ANISOU 1678  CA  THR A 234    11924  11763  11905   2802   1463   2669       C  
-ATOM   1679  C   THR A 234      19.181 -30.694  15.517  1.00 96.63           C  
-ANISOU 1679  C   THR A 234    12225  12277  12214   2928   1551   2726       C  
-ATOM   1680  O   THR A 234      18.677 -31.814  15.447  1.00 98.99           O  
-ANISOU 1680  O   THR A 234    12972  12303  12337   2985   1641   2726       O  
-ATOM   1681  CB  THR A 234      19.500 -30.592  13.042  1.00 94.73           C  
-ANISOU 1681  CB  THR A 234    12661  11541  11790   3020   1718   2799       C  
-ATOM   1682  OG1 THR A 234      20.856 -31.051  13.095  1.00 95.26           O  
-ANISOU 1682  OG1 THR A 234    12671  11789  11733   3408   2048   3070       O  
-ATOM   1683  CG2 THR A 234      19.309 -29.742  11.798  1.00 95.20           C  
-ANISOU 1683  CG2 THR A 234    12856  11411  11904   2861   1606   2715       C  
-ATOM   1684  N   LYS A 235      19.739 -30.228  16.629  1.00100.92           N  
-ANISOU 1684  N   LYS A 235    12204  13245  12897   2972   1527   2776       N  
-ATOM   1685  CA  LYS A 235      19.759 -31.025  17.849  1.00101.67           C  
-ANISOU 1685  CA  LYS A 235    12180  13507  12943   3086   1599   2831       C  
-ATOM   1686  C   LYS A 235      18.378 -31.590  18.151  1.00 99.86           C  
-ANISOU 1686  C   LYS A 235    12229  13019  12693   2844   1416   2632       C  
-ATOM   1687  O   LYS A 235      18.091 -32.750  17.857  1.00 99.85           O  
-ANISOU 1687  O   LYS A 235    12730  12722  12487   2960   1566   2676       O  
-ATOM   1688  CB  LYS A 235      20.241 -30.188  19.033  1.00100.58           C  
-ANISOU 1688  CB  LYS A 235    11346  13857  13014   3052   1495   2835       C  
-ATOM   1689  CG  LYS A 235      21.726 -29.859  19.005  1.00103.68           C  
-ANISOU 1689  CG  LYS A 235    11434  14556  13404   3351   1723   3066       C  
-ATOM   1690  CD  LYS A 235      22.085 -28.859  20.097  1.00101.01           C  
-ANISOU 1690  CD  LYS A 235    10390  14690  13301   3263   1575   3032       C  
-ATOM   1691  CE  LYS A 235      23.589 -28.608  20.166  1.00101.48           C  
-ANISOU 1691  CE  LYS A 235    10135  15071  13350   3576   1814   3267       C  
-ATOM   1692  NZ  LYS A 235      24.333 -29.753  20.767  1.00 98.98           N  
-ANISOU 1692  NZ  LYS A 235     9897  14861  12848   3930   2104   3483       N  
-ATOM   1693  N   ASP A 236      17.525 -30.752  18.727  1.00102.34           N  
-ANISOU 1693  N   ASP A 236    12216  13445  13225   2503   1092   2408       N  
-ATOM   1694  CA  ASP A 236      16.211 -31.181  19.194  1.00 99.75           C  
-ANISOU 1694  CA  ASP A 236    12062  12931  12908   2252    893   2205       C  
-ATOM   1695  C   ASP A 236      15.246 -31.563  18.076  1.00 97.15           C  
-ANISOU 1695  C   ASP A 236    12324  12117  12473   2099    828   2073       C  
-ATOM   1696  O   ASP A 236      14.202 -32.156  18.338  1.00 95.31           O  
-ANISOU 1696  O   ASP A 236    12342  11673  12199   1939    718   1930       O  
-ATOM   1697  CB  ASP A 236      15.570 -30.090  20.059  1.00102.29           C  
-ANISOU 1697  CB  ASP A 236    11855  13507  13502   1919    553   1993       C  
-ATOM   1698  CG  ASP A 236      16.139 -30.046  21.464  1.00105.83           C  
-ANISOU 1698  CG  ASP A 236    11785  14392  14033   2026    586   2076       C  
-ATOM   1699  OD1 ASP A 236      16.812 -31.020  21.865  1.00109.16           O  
-ANISOU 1699  OD1 ASP A 236    12308  14879  14288   2332    851   2274       O  
-ATOM   1700  OD2 ASP A 236      15.899 -29.043  22.170  1.00110.33           O  
-ANISOU 1700  OD2 ASP A 236    11847  15238  14834   1804    343   1941       O  
-ATOM   1701  N   ILE A 237      15.593 -31.231  16.837  1.00 81.50           N  
-ANISOU 1701  N   ILE A 237    10565   9959  10443   2149    897   2120       N  
-ATOM   1702  CA  ILE A 237      14.628 -31.305  15.738  1.00 78.49           C  
-ANISOU 1702  CA  ILE A 237    10670   9148  10006   1950    779   1962       C  
-ATOM   1703  C   ILE A 237      13.776 -32.580  15.721  1.00 79.76           C  
-ANISOU 1703  C   ILE A 237    11356   8964   9984   1943    830   1906       C  
-ATOM   1704  O   ILE A 237      12.548 -32.512  15.661  1.00 78.00           O  
-ANISOU 1704  O   ILE A 237    11291   8528   9816   1644    590   1678       O  
-ATOM   1705  CB  ILE A 237      15.289 -31.081  14.356  1.00 76.00           C  
-ANISOU 1705  CB  ILE A 237    10614   8665   9599   2092    933   2077       C  
-ATOM   1706  CG1 ILE A 237      14.214 -30.888  13.288  1.00 73.31           C  
-ANISOU 1706  CG1 ILE A 237    10679   7926   9249   1829    747   1878       C  
-ATOM   1707  CG2 ILE A 237      16.201 -32.233  13.996  1.00 74.86           C  
-ANISOU 1707  CG2 ILE A 237    10824   8422   9198   2488   1312   2330       C  
-ATOM   1708  CD1 ILE A 237      13.233 -29.789  13.610  1.00 69.31           C  
-ANISOU 1708  CD1 ILE A 237     9854   7488   8991   1428    364   1616       C  
-ATOM   1709  N   TYR A 238      14.423 -33.736  15.782  1.00 80.66           N  
-ANISOU 1709  N   TYR A 238    11736   9027   9884   2272   1140   2112       N  
-ATOM   1710  CA  TYR A 238      13.704 -35.000  15.735  1.00 80.66           C  
-ANISOU 1710  CA  TYR A 238    12251   8697   9699   2293   1218   2079       C  
-ATOM   1711  C   TYR A 238      12.777 -35.143  16.936  1.00 76.47           C  
-ANISOU 1711  C   TYR A 238    11528   8258   9269   2076   1014   1915       C  
-ATOM   1712  O   TYR A 238      11.627 -35.565  16.798  1.00 74.12           O  
-ANISOU 1712  O   TYR A 238    11558   7667   8938   1867    877   1737       O  
-ATOM   1713  CB  TYR A 238      14.687 -36.162  15.649  1.00 88.51           C  
-ANISOU 1713  CB  TYR A 238    13514   9659  10457   2706   1600   2347       C  
-ATOM   1714  CG  TYR A 238      15.567 -36.085  14.426  1.00 95.26           C  
-ANISOU 1714  CG  TYR A 238    14594  10401  11200   2922   1808   2505       C  
-ATOM   1715  CD1 TYR A 238      15.158 -36.638  13.221  1.00100.01           C  
-ANISOU 1715  CD1 TYR A 238    15789  10575  11637   2926   1880   2477       C  
-ATOM   1716  CD2 TYR A 238      16.797 -35.444  14.468  1.00 98.19           C  
-ANISOU 1716  CD2 TYR A 238    14582  11094  11631   3116   1930   2677       C  
-ATOM   1717  CE1 TYR A 238      15.955 -36.567  12.092  1.00105.37           C  
-ANISOU 1717  CE1 TYR A 238    16677  11149  12211   3121   2072   2620       C  
-ATOM   1718  CE2 TYR A 238      17.601 -35.365  13.342  1.00103.40           C  
-ANISOU 1718  CE2 TYR A 238    15447  11652  12189   3310   2122   2820       C  
-ATOM   1719  CZ  TYR A 238      17.174 -35.930  12.159  1.00106.19           C  
-ANISOU 1719  CZ  TYR A 238    16393  11577  12376   3311   2192   2791       C  
-ATOM   1720  OH  TYR A 238      17.968 -35.859  11.041  1.00109.04           O  
-ANISOU 1720  OH  TYR A 238    16962  11837  12633   3504   2384   2933       O  
-ATOM   1721  N   GLN A 239      13.283 -34.780  18.111  1.00 69.18           N  
-ANISOU 1721  N   GLN A 239    10067   7747   8470   2123    993   1973       N  
-ATOM   1722  CA  GLN A 239      12.477 -34.742  19.325  1.00 65.32           C  
-ANISOU 1722  CA  GLN A 239     9308   7406   8106   1906    781   1816       C  
-ATOM   1723  C   GLN A 239      11.237 -33.891  19.089  1.00 58.76           C  
-ANISOU 1723  C   GLN A 239     8436   6441   7451   1484    420   1522       C  
-ATOM   1724  O   GLN A 239      10.104 -34.353  19.235  1.00 55.78           O  
-ANISOU 1724  O   GLN A 239     8310   5832   7052   1280    280   1348       O  
-ATOM   1725  CB  GLN A 239      13.288 -34.131  20.467  1.00 68.95           C  
-ANISOU 1725  CB  GLN A 239     9119   8365   8714   1990    777   1909       C  
-ATOM   1726  CG  GLN A 239      13.254 -34.923  21.754  1.00 76.70           C  
-ANISOU 1726  CG  GLN A 239     9975   9517   9652   2083    844   1961       C  
-ATOM   1727  CD  GLN A 239      14.013 -36.235  21.656  1.00 85.11           C  
-ANISOU 1727  CD  GLN A 239    11395  10483  10461   2469   1208   2209       C  
-ATOM   1728  OE1 GLN A 239      13.760 -37.168  22.420  1.00 90.66           O  
-ANISOU 1728  OE1 GLN A 239    12207  11171  11070   2540   1283   2238       O  
-ATOM   1729  NE2 GLN A 239      14.955 -36.309  20.721  1.00 88.77           N  
-ANISOU 1729  NE2 GLN A 239    12038  10881  10811   2721   1436   2389       N  
-ATOM   1730  N   ASP A 240      11.476 -32.640  18.711  1.00 84.59           N  
-ANISOU 1730  N   ASP A 240    11386   9859  10895   1359    272   1469       N  
-ATOM   1731  CA  ASP A 240      10.416 -31.674  18.467  1.00 77.52           C  
-ANISOU 1731  CA  ASP A 240    10392   8875  10188    966    -77   1199       C  
-ATOM   1732  C   ASP A 240       9.406 -32.193  17.459  1.00 74.32           C  
-ANISOU 1732  C   ASP A 240    10588   7987   9662    822   -135   1061       C  
-ATOM   1733  O   ASP A 240       8.199 -32.027  17.634  1.00 71.28           O  
-ANISOU 1733  O   ASP A 240    10252   7465   9368    509   -396    822       O  
-ATOM   1734  CB  ASP A 240      11.012 -30.357  17.969  1.00 79.55           C  
-ANISOU 1734  CB  ASP A 240    10299   9317  10608    918   -162   1210       C  
-ATOM   1735  CG  ASP A 240      12.036 -29.776  18.932  1.00 81.14           C  
-ANISOU 1735  CG  ASP A 240     9888  10003  10938   1055   -109   1341       C  
-ATOM   1736  OD1 ASP A 240      12.632 -30.550  19.713  1.00 84.52           O  
-ANISOU 1736  OD1 ASP A 240    10249  10598  11265   1300     95   1504       O  
-ATOM   1737  OD2 ASP A 240      12.244 -28.542  18.907  1.00 81.95           O  
-ANISOU 1737  OD2 ASP A 240     9574  10320  11242    918   -272   1281       O  
-ATOM   1738  N   LEU A 241       9.905 -32.823  16.402  1.00 61.10           N  
-ANISOU 1738  N   LEU A 241     9370   6060   7784   1053    112   1210       N  
-ATOM   1739  CA  LEU A 241       9.043 -33.310  15.331  1.00 59.33           C  
-ANISOU 1739  CA  LEU A 241     9736   5374   7434    940     79   1094       C  
-ATOM   1740  C   LEU A 241       8.139 -34.448  15.782  1.00 59.52           C  
-ANISOU 1740  C   LEU A 241    10104   5173   7339    886     82   1008       C  
-ATOM   1741  O   LEU A 241       6.975 -34.520  15.386  1.00 57.40           O  
-ANISOU 1741  O   LEU A 241    10124   4610   7076    627   -107    796       O  
-ATOM   1742  CB  LEU A 241       9.870 -33.738  14.118  1.00 58.16           C  
-ANISOU 1742  CB  LEU A 241     9984   5026   7090   1221    360   1287       C  
-ATOM   1743  CG  LEU A 241      10.341 -32.593  13.218  1.00 55.28           C  
-ANISOU 1743  CG  LEU A 241     9464   4713   6827   1178    297   1297       C  
-ATOM   1744  CD1 LEU A 241      11.164 -33.121  12.055  1.00 54.74           C  
-ANISOU 1744  CD1 LEU A 241     9808   4443   6548   1471    594   1495       C  
-ATOM   1745  CD2 LEU A 241       9.151 -31.795  12.717  1.00 51.67           C  
-ANISOU 1745  CD2 LEU A 241     9057   4065   6511    790    -40   1021       C  
-ATOM   1746  N   ASN A 242       8.680 -35.338  16.605  1.00 74.47           N  
-ANISOU 1746  N   ASN A 242    11967   7204   9124   1131    298   1173       N  
-ATOM   1747  CA  ASN A 242       7.904 -36.466  17.101  1.00 74.34           C  
-ANISOU 1747  CA  ASN A 242    12264   6992   8989   1103    324   1112       C  
-ATOM   1748  C   ASN A 242       6.716 -36.008  17.933  1.00 70.05           C  
-ANISOU 1748  C   ASN A 242    11475   6511   8631    736    -10    849       C  
-ATOM   1749  O   ASN A 242       5.693 -36.692  18.004  1.00 68.80           O  
-ANISOU 1749  O   ASN A 242    11645   6090   8407    588    -86    708       O  
-ATOM   1750  CB  ASN A 242       8.782 -37.416  17.913  1.00 79.87           C  
-ANISOU 1750  CB  ASN A 242    12917   7874   9557   1441    613   1349       C  
-ATOM   1751  CG  ASN A 242       9.937 -37.966  17.109  1.00 83.60           C  
-ANISOU 1751  CG  ASN A 242    13657   8271   9835   1815    956   1609       C  
-ATOM   1752  OD1 ASN A 242      11.046 -38.123  17.617  1.00 87.87           O  
-ANISOU 1752  OD1 ASN A 242    13955   9091  10342   2098   1164   1826       O  
-ATOM   1753  ND2 ASN A 242       9.686 -38.257  15.843  1.00 86.05           N  
-ANISOU 1753  ND2 ASN A 242    14471   8207  10017   1818   1014   1586       N  
-ATOM   1754  N   ARG A 243       6.852 -34.847  18.563  1.00 64.87           N  
-ANISOU 1754  N   ARG A 243    10239   6203   8206    586   -210    782       N  
-ATOM   1755  CA  ARG A 243       5.766 -34.302  19.364  1.00 61.54           C  
-ANISOU 1755  CA  ARG A 243     9538   5868   7976    231   -539    529       C  
-ATOM   1756  C   ARG A 243       4.795 -33.508  18.500  1.00 57.49           C  
-ANISOU 1756  C   ARG A 243     9149   5119   7574   -100   -819    287       C  
-ATOM   1757  O   ARG A 243       3.588 -33.552  18.711  1.00 54.04           O  
-ANISOU 1757  O   ARG A 243     8814   4524   7196   -385  -1045     58       O  
-ATOM   1758  CB  ARG A 243       6.310 -33.426  20.489  1.00 62.71           C  
-ANISOU 1758  CB  ARG A 243     8997   6502   8329    212   -635    556       C  
-ATOM   1759  CG  ARG A 243       7.366 -34.106  21.345  1.00 69.83           C  
-ANISOU 1759  CG  ARG A 243     9727   7673   9132    549   -360    805       C  
-ATOM   1760  CD  ARG A 243       7.645 -33.302  22.601  1.00 74.54           C  
-ANISOU 1760  CD  ARG A 243     9650   8734   9938    474   -499    784       C  
-ATOM   1761  NE  ARG A 243       8.819 -33.784  23.322  1.00 81.32           N  
-ANISOU 1761  NE  ARG A 243    10297   9885  10714    816   -233   1039       N  
-ATOM   1762  CZ  ARG A 243      10.042 -33.283  23.178  1.00 85.32           C  
-ANISOU 1762  CZ  ARG A 243    10527  10646  11246   1038    -86   1226       C  
-ATOM   1763  NH1 ARG A 243      11.050 -33.785  23.879  1.00 87.52           N  
-ANISOU 1763  NH1 ARG A 243    10626  11184  11445   1345    152   1450       N  
-ATOM   1764  NH2 ARG A 243      10.256 -32.279  22.337  1.00 85.91           N  
-ANISOU 1764  NH2 ARG A 243    10500  10715  11426    952   -178   1187       N  
-ATOM   1765  N   LEU A 244       5.329 -32.794  17.514  1.00 67.03           N  
-ANISOU 1765  N   LEU A 244    10358   6302   8808    -57   -799    341       N  
-ATOM   1766  CA  LEU A 244       4.517 -31.940  16.652  1.00 63.71           C  
-ANISOU 1766  CA  LEU A 244    10024   5682   8499   -355  -1061    127       C  
-ATOM   1767  C   LEU A 244       3.783 -32.707  15.561  1.00 66.56           C  
-ANISOU 1767  C   LEU A 244    11050   5560   8680   -395  -1023     52       C  
-ATOM   1768  O   LEU A 244       2.689 -32.319  15.157  1.00 65.38           O  
-ANISOU 1768  O   LEU A 244    11032   5200   8609   -701  -1279   -184       O  
-ATOM   1769  CB  LEU A 244       5.378 -30.847  16.025  1.00 61.00           C  
-ANISOU 1769  CB  LEU A 244     9414   5506   8259   -298  -1058    214       C  
-ATOM   1770  CG  LEU A 244       5.871 -29.785  17.004  1.00 57.04           C  
-ANISOU 1770  CG  LEU A 244     8215   5467   7991   -357  -1185    217       C  
-ATOM   1771  CD1 LEU A 244       6.828 -28.837  16.307  1.00 56.71           C  
-ANISOU 1771  CD1 LEU A 244     7962   5568   8019   -257  -1133    333       C  
-ATOM   1772  CD2 LEU A 244       4.696 -29.022  17.606  1.00 54.61           C  
-ANISOU 1772  CD2 LEU A 244     7627   5216   7905   -756  -1561    -70       C  
-ATOM   1773  N   LEU A 245       4.385 -33.792  15.085  1.00 51.00           N  
-ANISOU 1773  N   LEU A 245     9495   3415   6469    -87   -705    251       N  
-ATOM   1774  CA  LEU A 245       3.787 -34.584  14.012  1.00 57.34           C  
-ANISOU 1774  CA  LEU A 245    10945   3758   7082    -93   -637    200       C  
-ATOM   1775  C   LEU A 245       2.638 -35.463  14.491  1.00 62.82           C  
-ANISOU 1775  C   LEU A 245    11918   4235   7717   -250   -721     40       C  
-ATOM   1776  O   LEU A 245       2.616 -35.907  15.637  1.00 63.26           O  
-ANISOU 1776  O   LEU A 245    11777   4473   7787   -216   -695     64       O  
-ATOM   1777  CB  LEU A 245       4.841 -35.447  13.321  1.00 53.16           C  
-ANISOU 1777  CB  LEU A 245    10768   3115   6316    295   -262    468       C  
-ATOM   1778  CG  LEU A 245       5.868 -34.706  12.465  1.00 51.34           C  
-ANISOU 1778  CG  LEU A 245    10430   2978   6098    448   -160    614       C  
-ATOM   1779  CD1 LEU A 245       6.840 -35.701  11.855  1.00 51.04           C  
-ANISOU 1779  CD1 LEU A 245    10769   2812   5811    834    219    873       C  
-ATOM   1780  CD2 LEU A 245       5.190 -33.881  11.377  1.00 46.57           C  
-ANISOU 1780  CD2 LEU A 245     9974   2150   5571    191   -383    433       C  
-ATOM   1781  N   LYS A 246       1.684 -35.706  13.600  1.00 89.04           N  
-ANISOU 1781  N   LYS A 246    15699   7165  10969   -423   -822   -124       N  
-ATOM   1782  CA  LYS A 246       0.567 -36.594  13.895  1.00 96.40           C  
-ANISOU 1782  CA  LYS A 246    16961   7842  11824   -570   -889   -280       C  
-ATOM   1783  C   LYS A 246       0.896 -38.028  13.483  1.00101.65           C  
-ANISOU 1783  C   LYS A 246    18167   8243  12212   -281   -561   -112       C  
-ATOM   1784  O   LYS A 246       1.460 -38.264  12.414  1.00103.11           O  
-ANISOU 1784  O   LYS A 246    18676   8247  12253    -90   -372     16       O  
-ATOM   1785  CB  LYS A 246      -0.712 -36.107  13.203  1.00100.94           C  
-ANISOU 1785  CB  LYS A 246    17739   8136  12478   -928  -1187   -564       C  
-ATOM   1786  CG  LYS A 246      -1.868 -37.099  13.247  1.00107.83           C  
-ANISOU 1786  CG  LYS A 246    19051   8677  13241  -1066  -1232   -724       C  
-ATOM   1787  CD  LYS A 246      -3.210 -36.419  13.002  1.00114.23           C  
-ANISOU 1787  CD  LYS A 246    19726   9615  14063  -1398  -1575   -929       C  
-ATOM   1788  CE  LYS A 246      -3.261 -35.734  11.646  1.00119.78           C  
-ANISOU 1788  CE  LYS A 246    20547  10256  14707  -1434  -1645   -929       C  
-ATOM   1789  NZ  LYS A 246      -4.581 -35.083  11.410  1.00123.02           N  
-ANISOU 1789  NZ  LYS A 246    20783  10861  15099  -1678  -1950  -1033       N  
-ATOM   1790  N   GLY A 247       0.543 -38.977  14.345  1.00 89.60           N  
-ANISOU 1790  N   GLY A 247    16732   6698  10614   -250   -495   -114       N  
-ATOM   1791  CA  GLY A 247       0.820 -40.381  14.106  1.00 95.55           C  
-ANISOU 1791  CA  GLY A 247    17974   7218  11114     19   -187     41       C  
-ATOM   1792  C   GLY A 247       0.177 -40.903  12.838  1.00101.43           C  
-ANISOU 1792  C   GLY A 247    19337   7497  11706    -36   -165    -50       C  
-ATOM   1793  O   GLY A 247      -1.016 -40.707  12.604  1.00102.34           O  
-ANISOU 1793  O   GLY A 247    19600   7402  11884   -346   -412   -301       O  
-ATOM   1794  N   LYS A 248       0.975 -41.574  12.015  1.00103.95           N  
-ANISOU 1794  N   LYS A 248    20018   7657  11823    268    134    152       N  
-ATOM   1795  CA  LYS A 248       0.490 -42.116  10.754  1.00108.09           C  
-ANISOU 1795  CA  LYS A 248    21143   7742  12184    253    189     90       C  
-ATOM   1796  C   LYS A 248       0.386 -43.636  10.817  1.00112.84           C  
-ANISOU 1796  C   LYS A 248    22225   8091  12558    439    437    173       C  
-ATOM   1797  O   LYS A 248       1.132 -44.289  11.547  1.00114.17           O  
-ANISOU 1797  O   LYS A 248    22300   8428  12650    698    662    370       O  
-ATOM   1798  CB  LYS A 248       1.417 -41.704   9.610  1.00108.52           C  
-ANISOU 1798  CB  LYS A 248    21291   7767  12174    443    334    241       C  
-ATOM   1799  CG  LYS A 248       2.844 -42.206   9.762  1.00109.08           C  
-ANISOU 1799  CG  LYS A 248    21305   8019  12120    854    682    555       C  
-ATOM   1800  CD  LYS A 248       3.716 -41.760   8.601  1.00109.52           C  
-ANISOU 1800  CD  LYS A 248    21455   8041  12118   1023    814    692       C  
-ATOM   1801  CE  LYS A 248       3.764 -40.245   8.496  1.00107.46           C  
-ANISOU 1801  CE  LYS A 248    20738   8009  12084    821    563    600       C  
-ATOM   1802  NZ  LYS A 248       4.774 -39.788   7.500  1.00108.18           N  
-ANISOU 1802  NZ  LYS A 248    20855   8124  12126   1016    715    764       N  
-ATOM   1803  N   LYS A 249      -0.552 -44.189  10.053  1.00108.63           N  
-ANISOU 1803  N   LYS A 249    22203   7153  11918    305    391     20       N  
-ATOM   1804  CA  LYS A 249      -0.712 -45.636   9.948  1.00114.11           C  
-ANISOU 1804  CA  LYS A 249    23410   7559  12389    469    624     85       C  
-ATOM   1805  C   LYS A 249      -0.979 -46.302  11.295  1.00114.82           C  
-ANISOU 1805  C   LYS A 249    23354   7781  12493    468    643     87       C  
-ATOM   1806  O   LYS A 249      -0.726 -47.494  11.465  1.00116.29           O  
-ANISOU 1806  O   LYS A 249    23844   7842  12500    693    897    221       O  
-ATOM   1807  CB  LYS A 249       0.520 -46.259   9.291  1.00118.16           C  
-ANISOU 1807  CB  LYS A 249    24167   8024  12703    870    988    367       C  
-ATOM   1808  CG  LYS A 249       0.273 -46.802   7.893  1.00122.62           C  
-ANISOU 1808  CG  LYS A 249    25341   8164  13086    913   1094    342       C  
-ATOM   1809  CD  LYS A 249      -0.297 -45.738   6.972  1.00122.24           C  
-ANISOU 1809  CD  LYS A 249    25283   8021  13143    645    833    152       C  
-ATOM   1810  CE  LYS A 249      -0.568 -46.302   5.588  1.00124.67           C  
-ANISOU 1810  CE  LYS A 249    26120   8069  13179    677    937    119       C  
-ATOM   1811  NZ  LYS A 249      -1.185 -45.295   4.684  1.00124.25           N  
-ANISOU 1811  NZ  LYS A 249    25995   8075  13140    407    676    -61       N  
-ATOM   1812  N   GLY A 250      -1.496 -45.533  12.248  1.00135.13           N  
-ANISOU 1812  N   GLY A 250    25462  10604  15276    215    374    -62       N  
-ATOM   1813  CA  GLY A 250      -1.785 -46.056  13.571  1.00135.98           C  
-ANISOU 1813  CA  GLY A 250    25388  10862  15416    189    365    -74       C  
-ATOM   1814  C   GLY A 250      -0.540 -46.547  14.285  1.00137.53           C  
-ANISOU 1814  C   GLY A 250    25389  11330  15537    550    653    216       C  
-ATOM   1815  O   GLY A 250      -0.601 -47.478  15.088  1.00136.45           O  
-ANISOU 1815  O   GLY A 250    25328  11199  15318    649    779    278       O  
-ATOM   1816  N   GLU A 251       0.593 -45.918  13.986  1.00124.36           N  
-ANISOU 1816  N   GLU A 251    23469   9886  13895    747    758    394       N  
-ATOM   1817  CA  GLU A 251       1.862 -46.271  14.612  1.00127.44           C  
-ANISOU 1817  CA  GLU A 251    23639  10559  14224   1097   1028    675       C  
-ATOM   1818  C   GLU A 251       2.373 -45.085  15.430  1.00125.97           C  
-ANISOU 1818  C   GLU A 251    22768  10836  14259   1039    877    695       C  
-ATOM   1819  O   GLU A 251       1.758 -44.018  15.434  1.00125.00           O  
-ANISOU 1819  O   GLU A 251    22374  10793  14329    736    575    495       O  
-ATOM   1820  CB  GLU A 251       2.889 -46.662  13.542  1.00131.51           C  
-ANISOU 1820  CB  GLU A 251    24467  10942  14558   1426   1327    897       C  
-ATOM   1821  CG  GLU A 251       4.011 -47.574  14.032  1.00135.34           C  
-ANISOU 1821  CG  GLU A 251    24968  11563  14893   1825   1673   1187       C  
-ATOM   1822  CD  GLU A 251       3.637 -49.047  13.992  1.00137.83           C  
-ANISOU 1822  CD  GLU A 251    25818  11555  14997   1944   1869   1220       C  
-ATOM   1823  OE1 GLU A 251       2.840 -49.436  13.113  1.00138.13           O  
-ANISOU 1823  OE1 GLU A 251    26333  11205  14946   1817   1830   1082       O  
-ATOM   1824  OE2 GLU A 251       4.139 -49.815  14.841  1.00139.09           O  
-ANISOU 1824  OE2 GLU A 251    25920  11849  15080   2165   2063   1384       O  
-ATOM   1825  N   GLN A 252       3.490 -45.272  16.128  1.00117.15           N  
-ANISOU 1825  N   GLN A 252    21372  10024  13116   1328   1085    932       N  
-ATOM   1826  CA  GLN A 252       4.100 -44.179  16.877  1.00114.90           C  
-ANISOU 1826  CA  GLN A 252    20438  10190  13030   1308    972    973       C  
-ATOM   1827  C   GLN A 252       5.062 -43.413  15.972  1.00111.21           C  
-ANISOU 1827  C   GLN A 252    19869   9808  12578   1449   1050   1097       C  
-ATOM   1828  O   GLN A 252       5.866 -44.011  15.256  1.00113.01           O  
-ANISOU 1828  O   GLN A 252    20400   9912  12628   1746   1331   1293       O  
-ATOM   1829  CB  GLN A 252       4.812 -44.689  18.138  1.00120.13           C  
-ANISOU 1829  CB  GLN A 252    20809  11165  13670   1535   1140   1157       C  
-ATOM   1830  CG  GLN A 252       6.306 -44.956  17.977  1.00128.74           C  
-ANISOU 1830  CG  GLN A 252    21847  12423  14645   1946   1463   1465       C  
-ATOM   1831  CD  GLN A 252       6.606 -46.168  17.110  1.00135.20           C  
-ANISOU 1831  CD  GLN A 252    23275  12893  15202   2212   1767   1610       C  
-ATOM   1832  OE1 GLN A 252       5.816 -47.109  17.039  1.00138.07           O  
-ANISOU 1832  OE1 GLN A 252    24065  12948  15447   2154   1793   1529       O  
-ATOM   1833  NE2 GLN A 252       7.756 -46.147  16.445  1.00139.04           N  
-ANISOU 1833  NE2 GLN A 252    23803  13427  15597   2504   1999   1823       N  
-ATOM   1834  N   MET A 253       4.963 -42.089  15.996  1.00111.63           N  
-ANISOU 1834  N   MET A 253    19498  10069  12846   1233    799    978       N  
-ATOM   1835  CA  MET A 253       5.735 -41.247  15.090  1.00105.83           C  
-ANISOU 1835  CA  MET A 253    18663   9400  12148   1315    832   1062       C  
-ATOM   1836  C   MET A 253       7.242 -41.355  15.308  1.00104.58           C  
-ANISOU 1836  C   MET A 253    18286   9523  11926   1693   1119   1358       C  
-ATOM   1837  O   MET A 253       7.711 -41.522  16.433  1.00103.94           O  
-ANISOU 1837  O   MET A 253    17868   9745  11881   1813   1186   1463       O  
-ATOM   1838  CB  MET A 253       5.284 -39.787  15.211  1.00102.17           C  
-ANISOU 1838  CB  MET A 253    17749   9126  11944    992    490    867       C  
-ATOM   1839  CG  MET A 253       6.139 -38.788  14.434  1.00 99.23           C  
-ANISOU 1839  CG  MET A 253    17179   8883  11639   1068    508    957       C  
-ATOM   1840  SD  MET A 253       6.239 -39.137  12.664  1.00 99.57           S  
-ANISOU 1840  SD  MET A 253    17847   8496  11489   1175    662   1002       S  
-ATOM   1841  CE  MET A 253       4.509 -39.089  12.206  1.00 96.51           C  
-ANISOU 1841  CE  MET A 253    17794   7730  11144    762    350    666       C  
-ATOM   1842  N   ASN A 254       7.990 -41.281  14.212  1.00 91.68           N  
-ANISOU 1842  N   ASN A 254    16857   7783  10193   1882   1290   1492       N  
-ATOM   1843  CA  ASN A 254       9.438 -41.135  14.268  1.00 91.38           C  
-ANISOU 1843  CA  ASN A 254    16572   8025  10125   2211   1530   1755       C  
-ATOM   1844  C   ASN A 254       9.918 -40.364  13.045  1.00 89.77           C  
-ANISOU 1844  C   ASN A 254    16421   7755   9933   2233   1541   1787       C  
-ATOM   1845  O   ASN A 254      10.112 -40.935  11.975  1.00 91.76           O  
-ANISOU 1845  O   ASN A 254    17148   7712  10006   2381   1722   1863       O  
-ATOM   1846  CB  ASN A 254      10.133 -42.493  14.361  1.00 93.07           C  
-ANISOU 1846  CB  ASN A 254    17107   8154  10101   2580   1888   1987       C  
-ATOM   1847  CG  ASN A 254      11.597 -42.372  14.752  1.00 95.74           C  
-ANISOU 1847  CG  ASN A 254    17102   8847  10428   2913   2119   2253       C  
-ATOM   1848  OD1 ASN A 254      12.011 -41.383  15.361  1.00 93.42           O  
-ANISOU 1848  OD1 ASN A 254    16255   8921  10319   2856   1998   2256       O  
-ATOM   1849  ND2 ASN A 254      12.389 -43.381  14.402  1.00 97.09           N  
-ANISOU 1849  ND2 ASN A 254    17598   8908  10383   3262   2453   2474       N  
-ATOM   1850  N   SER A 255      10.090 -39.058  13.212  1.00 99.36           N  
-ANISOU 1850  N   SER A 255    17145   9246  11362   2078   1342   1723       N  
-ATOM   1851  CA  SER A 255      10.449 -38.177  12.108  1.00 96.85           C  
-ANISOU 1851  CA  SER A 255    16828   8884  11088   2051   1308   1727       C  
-ATOM   1852  C   SER A 255      11.822 -38.513  11.538  1.00 98.88           C  
-ANISOU 1852  C   SER A 255    17184   9193  11192   2439   1648   2007       C  
-ATOM   1853  O   SER A 255      12.101 -38.250  10.366  1.00 99.96           O  
-ANISOU 1853  O   SER A 255    17550   9160  11269   2484   1709   2041       O  
-ATOM   1854  CB  SER A 255      10.397 -36.712  12.554  1.00 94.06           C  
-ANISOU 1854  CB  SER A 255    15880   8851  11007   1814   1030   1611       C  
-ATOM   1855  OG  SER A 255      11.169 -36.501  13.724  1.00 91.86           O  
-ANISOU 1855  OG  SER A 255    15085   8996  10822   1947   1087   1735       O  
-ATOM   1856  N   ALA A 256      12.673 -39.099  12.372  1.00 78.10           N  
-ANISOU 1856  N   ALA A 256    14381   6796   8496   2717   1868   2206       N  
-ATOM   1857  CA  ALA A 256      14.015 -39.481  11.956  1.00 81.57           C  
-ANISOU 1857  CA  ALA A 256    14890   7311   8790   3103   2202   2481       C  
-ATOM   1858  C   ALA A 256      13.996 -40.329  10.685  1.00 83.60           C  
-ANISOU 1858  C   ALA A 256    15798   7149   8816   3244   2401   2538       C  
-ATOM   1859  O   ALA A 256      14.810 -40.127   9.784  1.00 85.24           O  
-ANISOU 1859  O   ALA A 256    16103   7331   8955   3421   2561   2672       O  
-ATOM   1860  CB  ALA A 256      14.721 -40.223  13.083  1.00 83.04           C  
-ANISOU 1860  CB  ALA A 256    14887   7750   8916   3369   2407   2664       C  
-ATOM   1861  N   VAL A 257      13.062 -41.275  10.619  1.00109.06           N  
-ANISOU 1861  N   VAL A 257    19467  10048  11922   3163   2390   2433       N  
-ATOM   1862  CA  VAL A 257      12.977 -42.195   9.487  1.00111.62           C  
-ANISOU 1862  CA  VAL A 257    20431   9961  12017   3297   2582   2480       C  
-ATOM   1863  C   VAL A 257      12.414 -41.535   8.233  1.00109.93           C  
-ANISOU 1863  C   VAL A 257    20451   9488  11831   3082   2421   2327       C  
-ATOM   1864  O   VAL A 257      12.789 -41.895   7.117  1.00111.77           O  
-ANISOU 1864  O   VAL A 257    21079   9485  11904   3242   2603   2418       O  
-ATOM   1865  CB  VAL A 257      12.147 -43.458   9.836  1.00114.80           C  
-ANISOU 1865  CB  VAL A 257    21242  10094  12283   3280   2627   2416       C  
-ATOM   1866  CG1 VAL A 257      11.474 -43.302  11.187  1.00115.33           C  
-ANISOU 1866  CG1 VAL A 257    20948  10367  12504   3074   2415   2285       C  
-ATOM   1867  CG2 VAL A 257      11.124 -43.756   8.744  1.00114.74           C  
-ANISOU 1867  CG2 VAL A 257    21782   9629  12184   3094   2537   2241       C  
-ATOM   1868  N   LEU A 258      11.522 -40.566   8.424  1.00105.43           N  
-ANISOU 1868  N   LEU A 258    19631   8964  11462   2722   2080   2095       N  
-ATOM   1869  CA  LEU A 258      10.883 -39.882   7.303  1.00102.91           C  
-ANISOU 1869  CA  LEU A 258    19509   8405  11186   2486   1893   1929       C  
-ATOM   1870  C   LEU A 258      11.904 -39.486   6.235  1.00105.01           C  
-ANISOU 1870  C   LEU A 258    19835   8675  11388   2687   2067   2092       C  
-ATOM   1871  O   LEU A 258      12.925 -38.866   6.539  1.00105.63           O  
-ANISOU 1871  O   LEU A 258    19497   9088  11550   2832   2142   2240       O  
-ATOM   1872  CB  LEU A 258      10.085 -38.664   7.787  1.00 95.65           C  
-ANISOU 1872  CB  LEU A 258    18162   7650  10531   2109   1514   1698       C  
-ATOM   1873  CG  LEU A 258       8.956 -38.927   8.794  1.00 90.11           C  
-ANISOU 1873  CG  LEU A 258    17388   6936   9912   1862   1301   1503       C  
-ATOM   1874  CD1 LEU A 258       8.174 -37.656   9.078  1.00 85.27           C  
-ANISOU 1874  CD1 LEU A 258    16387   6456   9557   1486    924   1269       C  
-ATOM   1875  CD2 LEU A 258       8.020 -40.017   8.302  1.00 87.51           C  
-ANISOU 1875  CD2 LEU A 258    17669   6173   9408   1807   1333   1400       C  
-ATOM   1876  N   PRO A 259      11.626 -39.853   4.975  1.00105.99           N  
-ANISOU 1876  N   PRO A 259    20486   8426  11361   2696   2133   2065       N  
-ATOM   1877  CA  PRO A 259      12.575 -39.672   3.871  1.00107.70           C  
-ANISOU 1877  CA  PRO A 259    20851   8595  11476   2911   2333   2229       C  
-ATOM   1878  C   PRO A 259      12.783 -38.197   3.578  1.00106.80           C  
-ANISOU 1878  C   PRO A 259    20334   8684  11562   2746   2138   2174       C  
-ATOM   1879  O   PRO A 259      13.755 -37.819   2.924  1.00107.00           O  
-ANISOU 1879  O   PRO A 259    20310   8792  11555   2928   2291   2329       O  
-ATOM   1880  CB  PRO A 259      11.871 -40.350   2.694  1.00109.57           C  
-ANISOU 1880  CB  PRO A 259    21740   8359  11534   2864   2367   2140       C  
-ATOM   1881  CG  PRO A 259      10.422 -40.241   3.016  1.00107.50           C  
-ANISOU 1881  CG  PRO A 259    21533   7941  11371   2501   2057   1863       C  
-ATOM   1882  CD  PRO A 259      10.326 -40.369   4.509  1.00105.11           C  
-ANISOU 1882  CD  PRO A 259    20840   7918  11179   2472   1995   1855       C  
-ATOM   1883  N   GLU A 260      11.872 -37.374   4.081  1.00109.53           N  
-ANISOU 1883  N   GLU A 260    20389   9113  12116   2403   1802   1952       N  
-ATOM   1884  CA  GLU A 260      11.902 -35.941   3.837  1.00108.37           C  
-ANISOU 1884  CA  GLU A 260    19862   9139  12176   2203   1578   1867       C  
-ATOM   1885  C   GLU A 260      12.921 -35.240   4.722  1.00109.21           C  
-ANISOU 1885  C   GLU A 260    19352   9710  12432   2321   1616   2006       C  
-ATOM   1886  O   GLU A 260      12.949 -34.013   4.793  1.00108.72           O  
-ANISOU 1886  O   GLU A 260    18880   9854  12573   2144   1414   1931       O  
-ATOM   1887  CB  GLU A 260      10.515 -35.352   4.068  1.00105.84           C  
-ANISOU 1887  CB  GLU A 260    19465   8726  12022   1789   1201   1571       C  
-ATOM   1888  CG  GLU A 260       9.457 -35.934   3.147  1.00107.02           C  
-ANISOU 1888  CG  GLU A 260    20206   8417  12039   1645   1135   1414       C  
-ATOM   1889  CD  GLU A 260       8.143 -36.191   3.857  1.00105.52           C  
-ANISOU 1889  CD  GLU A 260    20049   8122  11920   1363    895   1181       C  
-ATOM   1890  OE1 GLU A 260       8.083 -37.136   4.674  1.00106.18           O  
-ANISOU 1890  OE1 GLU A 260    20194   8224  11926   1470   1008   1227       O  
-ATOM   1891  OE2 GLU A 260       7.171 -35.450   3.594  1.00104.07           O  
-ANISOU 1891  OE2 GLU A 260    19834   7837  11870   1036    593    952       O  
-ATOM   1892  N   MET A 261      13.762 -36.021   5.388  1.00100.21           N  
-ANISOU 1892  N   MET A 261    17032   8472  12572   1511   -207   1046       N  
-ATOM   1893  CA  MET A 261      14.751 -35.459   6.298  1.00101.08           C  
-ANISOU 1893  CA  MET A 261    17044   8656  12705   1605   -258   1259       C  
-ATOM   1894  C   MET A 261      16.134 -35.399   5.665  1.00103.15           C  
-ANISOU 1894  C   MET A 261    17276   8873  13045   2031   -312   1456       C  
-ATOM   1895  O   MET A 261      17.078 -34.881   6.261  1.00103.25           O  
-ANISOU 1895  O   MET A 261    17182   8952  13096   2155   -369   1654       O  
-ATOM   1896  CB  MET A 261      14.787 -36.253   7.603  1.00 99.80           C  
-ANISOU 1896  CB  MET A 261    17139   8349  12432   1375   -271   1381       C  
-ATOM   1897  CG  MET A 261      13.421 -36.380   8.270  1.00 96.79           C  
-ANISOU 1897  CG  MET A 261    16790   8024  11961    952   -214   1215       C  
-ATOM   1898  SD  MET A 261      12.587 -34.794   8.523  1.00 90.97           S  
-ANISOU 1898  SD  MET A 261    15648   7653  11264    790   -177   1039       S  
-ATOM   1899  CE  MET A 261      13.638 -34.046   9.765  1.00 87.31           C  
-ANISOU 1899  CE  MET A 261    15075   7295  10803    862   -249   1253       C  
-ATOM   1900  N   GLU A 262      16.244 -35.928   4.451  1.00120.62           N  
-ANISOU 1900  N   GLU A 262    19577  10979  15275   2259   -299   1404       N  
-ATOM   1901  CA  GLU A 262      17.488 -35.866   3.698  1.00123.60           C  
-ANISOU 1901  CA  GLU A 262    19905  11340  15717   2692   -338   1582       C  
-ATOM   1902  C   GLU A 262      17.824 -34.413   3.396  1.00118.81           C  
-ANISOU 1902  C   GLU A 262    18884  11019  15238   2841   -360   1615       C  
-ATOM   1903  O   GLU A 262      18.981 -34.065   3.159  1.00118.16           O  
-ANISOU 1903  O   GLU A 262    18625  11105  15164   3086   -388   1763       O  
-ATOM   1904  CB  GLU A 262      17.350 -36.652   2.396  1.00131.92           C  
-ANISOU 1904  CB  GLU A 262    21120  12253  16749   2892   -312   1473       C  
-ATOM   1905  CG  GLU A 262      16.260 -36.121   1.480  1.00141.65           C  
-ANISOU 1905  CG  GLU A 262    22165  13640  18017   2800   -262   1204       C  
-ATOM   1906  CD  GLU A 262      15.562 -37.218   0.702  1.00150.35           C  
-ANISOU 1906  CD  GLU A 262    23547  14536  19042   2759   -239   1023       C  
-ATOM   1907  OE1 GLU A 262      16.042 -38.370   0.739  1.00156.21           O  
-ANISOU 1907  OE1 GLU A 262    24626  15011  19715   2861   -266   1112       O  
-ATOM   1908  OE2 GLU A 262      14.529 -36.929   0.060  1.00154.24           O  
-ANISOU 1908  OE2 GLU A 262    23928  15131  19547   2621   -200    792       O  
-ATOM   1909  N   ASN A 263      16.794 -33.571   3.411  1.00106.77           N  
-ANISOU 1909  N   ASN A 263    17137   9685  13747   2609   -326   1410       N  
-ATOM   1910  CA  ASN A 263      16.941 -32.146   3.140  1.00101.53           C  
-ANISOU 1910  CA  ASN A 263    16074   9289  13213   2708   -352   1411       C  
-ATOM   1911  C   ASN A 263      17.638 -31.417   4.287  1.00 97.79           C  
-ANISOU 1911  C   ASN A 263    15475   8902  12778   2672   -429   1596       C  
-ATOM   1912  O   ASN A 263      17.002 -30.700   5.056  1.00 97.91           O  
-ANISOU 1912  O   ASN A 263    15358   9050  12795   2414   -430   1494       O  
-ATOM   1913  CB  ASN A 263      15.571 -31.518   2.867  1.00101.98           C  
-ANISOU 1913  CB  ASN A 263    15951   9511  13287   2457   -289   1130       C  
-ATOM   1914  CG  ASN A 263      14.915 -32.067   1.612  1.00102.90           C  
-ANISOU 1914  CG  ASN A 263    16139   9576  13382   2514   -228    948       C  
-ATOM   1915  OD1 ASN A 263      15.579 -32.303   0.605  1.00103.09           O  
-ANISOU 1915  OD1 ASN A 263    16168   9562  13441   2842   -239   1020       O  
-ATOM   1916  ND2 ASN A 263      13.604 -32.271   1.669  1.00103.52           N  
-ANISOU 1916  ND2 ASN A 263    16271   9662  13399   2198   -166    716       N  
-ATOM   1917  N   GLN A 264      18.951 -31.597   4.383  1.00 96.22           N  
-ANISOU 1917  N   GLN A 264    15255   8760  12544   2860   -467   1790       N  
-ATOM   1918  CA  GLN A 264      19.723 -31.112   5.524  1.00 91.08           C  
-ANISOU 1918  CA  GLN A 264    14517   8198  11893   2798   -539   1953       C  
-ATOM   1919  C   GLN A 264      19.544 -29.625   5.832  1.00 85.22           C  
-ANISOU 1919  C   GLN A 264    13421   7698  11260   2710   -592   1903       C  
-ATOM   1920  O   GLN A 264      19.389 -29.244   6.992  1.00 84.87           O  
-ANISOU 1920  O   GLN A 264    13399   7633  11215   2535   -650   1945       O  
-ATOM   1921  CB  GLN A 264      21.199 -31.442   5.337  1.00 92.98           C  
-ANISOU 1921  CB  GLN A 264    14724   8512  12093   3026   -552   2139       C  
-ATOM   1922  N   VAL A 265      19.572 -28.788   4.799  1.00 79.56           N  
-ANISOU 1922  N   VAL A 265    12387   7209  10632   2828   -576   1817       N  
-ATOM   1923  CA  VAL A 265      19.543 -27.341   4.995  1.00 71.96           C  
-ANISOU 1923  CA  VAL A 265    11071   6485   9785   2762   -636   1780       C  
-ATOM   1924  C   VAL A 265      18.134 -26.792   5.219  1.00 65.94           C  
-ANISOU 1924  C   VAL A 265    10278   5696   9079   2579   -626   1588       C  
-ATOM   1925  O   VAL A 265      17.951 -25.823   5.955  1.00 64.18           O  
-ANISOU 1925  O   VAL A 265     9898   5567   8919   2465   -694   1569       O  
-ATOM   1926  CB  VAL A 265      20.219 -26.594   3.829  1.00 71.05           C  
-ANISOU 1926  CB  VAL A 265    10615   6635   9744   2934   -618   1792       C  
-ATOM   1927  CG1 VAL A 265      20.236 -25.097   4.094  1.00 69.14           C  
-ANISOU 1927  CG1 VAL A 265    10027   6611   9631   2837   -690   1764       C  
-ATOM   1928  CG2 VAL A 265      21.631 -27.112   3.631  1.00 70.12           C  
-ANISOU 1928  CG2 VAL A 265    10525   6542   9574   3118   -610   1993       C  
-ATOM   1929  N   ALA A 266      17.138 -27.406   4.589  1.00 61.51           N  
-ANISOU 1929  N   ALA A 266     9871   4999   8501   2553   -541   1440       N  
-ATOM   1930  CA  ALA A 266      15.756 -27.011   4.832  1.00 56.30           C  
-ANISOU 1930  CA  ALA A 266     9151   4429   7813   2261   -475   1176       C  
-ATOM   1931  C   ALA A 266      15.379 -27.310   6.279  1.00 55.86           C  
-ANISOU 1931  C   ALA A 266     9281   4322   7623   1959   -472   1152       C  
-ATOM   1932  O   ALA A 266      14.834 -26.458   6.976  1.00 54.81           O  
-ANISOU 1932  O   ALA A 266     8998   4336   7492   1775   -486   1045       O  
-ATOM   1933  CB  ALA A 266      14.822 -27.724   3.884  1.00 54.45           C  
-ANISOU 1933  CB  ALA A 266     9022   4146   7522   2205   -364    979       C  
-ATOM   1934  N   VAL A 267      15.679 -28.526   6.721  1.00 53.72           N  
-ANISOU 1934  N   VAL A 267     9335   3844   7231   1921   -456   1257       N  
-ATOM   1935  CA  VAL A 267      15.476 -28.916   8.108  1.00 52.45           C  
-ANISOU 1935  CA  VAL A 267     9365   3628   6937   1662   -459   1281       C  
-ATOM   1936  C   VAL A 267      16.003 -27.854   9.075  1.00 51.70           C  
-ANISOU 1936  C   VAL A 267     9092   3666   6887   1652   -562   1375       C  
-ATOM   1937  O   VAL A 267      15.293 -27.437   9.989  1.00 52.21           O  
-ANISOU 1937  O   VAL A 267     9125   3836   6878   1403   -549   1254       O  
-ATOM   1938  CB  VAL A 267      16.145 -30.276   8.414  1.00 53.27           C  
-ANISOU 1938  CB  VAL A 267     9816   3481   6944   1710   -462   1464       C  
-ATOM   1939  CG1 VAL A 267      16.216 -30.507   9.915  1.00 52.89           C  
-ANISOU 1939  CG1 VAL A 267     9917   3401   6778   1492   -490   1550       C  
-ATOM   1940  CG2 VAL A 267      15.394 -31.409   7.718  1.00 51.30           C  
-ANISOU 1940  CG2 VAL A 267     9794   3077   6620   1632   -369   1333       C  
-ATOM   1941  N   SER A 268      17.242 -27.413   8.868  1.00 62.03           N  
-ANISOU 1941  N   SER A 268    10283   4974   8313   1927   -669   1593       N  
-ATOM   1942  CA  SER A 268      17.828 -26.381   9.720  1.00 62.60           C  
-ANISOU 1942  CA  SER A 268    10183   5157   8444   1934   -794   1696       C  
-ATOM   1943  C   SER A 268      16.955 -25.139   9.775  1.00 60.60           C  
-ANISOU 1943  C   SER A 268     9660   5114   8251   1801   -798   1475       C  
-ATOM   1944  O   SER A 268      16.833 -24.506  10.824  1.00 60.78           O  
-ANISOU 1944  O   SER A 268     9635   5222   8238   1654   -859   1441       O  
-ATOM   1945  CB  SER A 268      19.223 -25.996   9.234  1.00 63.77           C  
-ANISOU 1945  CB  SER A 268    10168   5340   8720   2233   -898   1927       C  
-ATOM   1946  OG  SER A 268      20.159 -27.019   9.518  1.00 68.99           O  
-ANISOU 1946  OG  SER A 268    11038   5890   9285   2298   -895   2105       O  
-ATOM   1947  N   SER A 269      16.359 -24.789   8.640  1.00 63.74           N  
-ANISOU 1947  N   SER A 269     9882   5597   8738   1864   -735   1323       N  
-ATOM   1948  CA  SER A 269      15.482 -23.626   8.570  1.00 60.48           C  
-ANISOU 1948  CA  SER A 269     9204   5383   8391   1753   -728   1107       C  
-ATOM   1949  C   SER A 269      14.172 -23.908   9.291  1.00 60.00           C  
-ANISOU 1949  C   SER A 269     9265   5367   8164   1422   -619    879       C  
-ATOM   1950  O   SER A 269      13.751 -23.140  10.154  1.00 60.31           O  
-ANISOU 1950  O   SER A 269     9212   5531   8173   1271   -650    780       O  
-ATOM   1951  CB  SER A 269      15.207 -23.245   7.116  1.00 58.73           C  
-ANISOU 1951  CB  SER A 269     8765   5244   8307   1915   -684   1022       C  
-ATOM   1952  OG  SER A 269      16.370 -22.728   6.498  1.00 58.27           O  
-ANISOU 1952  OG  SER A 269     8525   5199   8417   2219   -795   1236       O  
-ATOM   1953  N   LEU A 270      13.534 -25.015   8.925  1.00 51.17           N  
-ANISOU 1953  N   LEU A 270     8354   4148   6939   1316   -498    802       N  
-ATOM   1954  CA  LEU A 270      12.314 -25.462   9.579  1.00 50.93           C  
-ANISOU 1954  CA  LEU A 270     8460   4148   6744    996   -392    624       C  
-ATOM   1955  C   LEU A 270      12.464 -25.445  11.101  1.00 53.27           C  
-ANISOU 1955  C   LEU A 270     8872   4455   6914    834   -438    689       C  
-ATOM   1956  O   LEU A 270      11.565 -25.002  11.823  1.00 54.15           O  
-ANISOU 1956  O   LEU A 270     8928   4711   6936    617   -397    533       O  
-ATOM   1957  CB  LEU A 270      11.963 -26.868   9.106  1.00 48.46           C  
-ANISOU 1957  CB  LEU A 270     8416   3658   6337    929   -298    617       C  
-ATOM   1958  CG  LEU A 270      10.740 -27.508   9.751  1.00 48.70           C  
-ANISOU 1958  CG  LEU A 270     8609   3698   6198    589   -195    475       C  
-ATOM   1959  CD1 LEU A 270       9.569 -26.544   9.697  1.00 45.39           C  
-ANISOU 1959  CD1 LEU A 270     7942   3516   5787    433   -133    242       C  
-ATOM   1960  CD2 LEU A 270      10.399 -28.830   9.067  1.00 46.04           C  
-ANISOU 1960  CD2 LEU A 270     8516   3172   5805    543   -125    461       C  
-ATOM   1961  N   SER A 271      13.606 -25.921  11.584  1.00 54.69           N  
-ANISOU 1961  N   SER A 271     9208   4491   7080    950   -522    924       N  
-ATOM   1962  CA  SER A 271      13.861 -25.977  13.015  1.00 55.76           C  
-ANISOU 1962  CA  SER A 271     9467   4628   7091    814   -575   1009       C  
-ATOM   1963  C   SER A 271      13.898 -24.575  13.608  1.00 54.39           C  
-ANISOU 1963  C   SER A 271     9053   4640   6971    815   -670    944       C  
-ATOM   1964  O   SER A 271      13.461 -24.351  14.737  1.00 56.15           O  
-ANISOU 1964  O   SER A 271     9316   4955   7062    627   -671    875       O  
-ATOM   1965  CB  SER A 271      15.178 -26.696  13.288  1.00 56.67           C  
-ANISOU 1965  CB  SER A 271     9770   4556   7205    972   -656   1293       C  
-ATOM   1966  OG  SER A 271      15.482 -26.687  14.666  1.00 58.28           O  
-ANISOU 1966  OG  SER A 271    10077   4773   7293    851   -717   1385       O  
-ATOM   1967  N   ALA A 272      14.421 -23.632  12.835  1.00 51.22           N  
-ANISOU 1967  N   ALA A 272     8404   4296   6763   1033   -756    967       N  
-ATOM   1968  CA  ALA A 272      14.560 -22.255  13.289  1.00 47.28           C  
-ANISOU 1968  CA  ALA A 272     7670   3946   6347   1062   -875    917       C  
-ATOM   1969  C   ALA A 272      13.199 -21.591  13.417  1.00 44.56           C  
-ANISOU 1969  C   ALA A 272     7192   3787   5953    873   -789    629       C  
-ATOM   1970  O   ALA A 272      12.989 -20.742  14.282  1.00 43.49           O  
-ANISOU 1970  O   ALA A 272     6972   3772   5780    794   -854    541       O  
-ATOM   1971  CB  ALA A 272      15.435 -21.478  12.325  1.00 44.95           C  
-ANISOU 1971  CB  ALA A 272     7135   3657   6286   1340   -988   1033       C  
-ATOM   1972  N   VAL A 273      12.278 -21.986  12.545  1.00 48.70           N  
-ANISOU 1972  N   VAL A 273     7700   4334   6471    809   -647    483       N  
-ATOM   1973  CA  VAL A 273      10.940 -21.418  12.521  1.00 47.28           C  
-ANISOU 1973  CA  VAL A 273     7380   4335   6248    638   -550    220       C  
-ATOM   1974  C   VAL A 273      10.151 -21.930  13.710  1.00 49.11           C  
-ANISOU 1974  C   VAL A 273     7796   4616   6246    367   -468    141       C  
-ATOM   1975  O   VAL A 273       9.445 -21.171  14.381  1.00 49.02           O  
-ANISOU 1975  O   VAL A 273     7681   4778   6166    248   -457    -17       O  
-ATOM   1976  CB  VAL A 273      10.191 -21.812  11.244  1.00 44.53           C  
-ANISOU 1976  CB  VAL A 273     6979   3991   5948    635   -422    106       C  
-ATOM   1977  CG1 VAL A 273       8.901 -21.026  11.134  1.00 43.53           C  
-ANISOU 1977  CG1 VAL A 273     6654   4074   5812    493   -337   -149       C  
-ATOM   1978  CG2 VAL A 273      11.056 -21.573  10.039  1.00 41.30           C  
-ANISOU 1978  CG2 VAL A 273     6430   3518   5743    917   -489    223       C  
-ATOM   1979  N   ILE A 274      10.276 -23.227  13.967  1.00 45.37           N  
-ANISOU 1979  N   ILE A 274     7598   3992   5650    278   -413    258       N  
-ATOM   1980  CA  ILE A 274       9.584 -23.846  15.089  1.00 47.44           C  
-ANISOU 1980  CA  ILE A 274     8045   4292   5688     19   -336    223       C  
-ATOM   1981  C   ILE A 274       9.987 -23.181  16.404  1.00 48.06           C  
-ANISOU 1981  C   ILE A 274     8115   4460   5684     -1   -438    258       C  
-ATOM   1982  O   ILE A 274       9.149 -22.981  17.281  1.00 49.94           O  
-ANISOU 1982  O   ILE A 274     8357   4854   5763   -187   -381    134       O  
-ATOM   1983  CB  ILE A 274       9.839 -25.361  15.142  1.00 48.05           C  
-ANISOU 1983  CB  ILE A 274     8424   4161   5673    -50   -288    382       C  
-ATOM   1984  CG1 ILE A 274       9.423 -26.003  13.819  1.00 47.73           C  
-ANISOU 1984  CG1 ILE A 274     8404   4024   5709    -24   -202    328       C  
-ATOM   1985  CG2 ILE A 274       9.066 -25.984  16.280  1.00 51.14           C  
-ANISOU 1985  CG2 ILE A 274     8984   4607   5838   -330   -208    358       C  
-ATOM   1986  CD1 ILE A 274       9.975 -27.386  13.603  1.00 49.45           C  
-ANISOU 1986  CD1 ILE A 274     8905   3990   5893      3   -195    500       C  
-ATOM   1987  N   LYS A 275      11.262 -22.824  16.531  1.00 39.84           N  
-ANISOU 1987  N   LYS A 275     7058   3330   4749    197   -592    428       N  
-ATOM   1988  CA  LYS A 275      11.718 -22.082  17.698  1.00 43.22           C  
-ANISOU 1988  CA  LYS A 275     7463   3838   5122    200   -718    455       C  
-ATOM   1989  C   LYS A 275      10.989 -20.755  17.738  1.00 41.92           C  
-ANISOU 1989  C   LYS A 275     7051   3880   4996    186   -733    223       C  
-ATOM   1990  O   LYS A 275      10.374 -20.397  18.743  1.00 42.40           O  
-ANISOU 1990  O   LYS A 275     7123   4088   4898     47   -716    100       O  
-ATOM   1991  CB  LYS A 275      13.218 -21.813  17.628  1.00 46.97           C  
-ANISOU 1991  CB  LYS A 275     7920   4185   5743    430   -896    682       C  
-ATOM   1992  CG  LYS A 275      14.061 -23.016  17.266  1.00 54.51           C  
-ANISOU 1992  CG  LYS A 275     9075   4925   6711    516   -887    922       C  
-ATOM   1993  CD  LYS A 275      13.910 -24.137  18.268  1.00 61.06           C  
-ANISOU 1993  CD  LYS A 275    10189   5690   7322    328   -820   1002       C  
-ATOM   1994  CE  LYS A 275      14.937 -25.231  18.005  1.00 64.77           C  
-ANISOU 1994  CE  LYS A 275    10858   5933   7818    447   -842   1264       C  
-ATOM   1995  NZ  LYS A 275      16.331 -24.720  18.162  1.00 66.40           N  
-ANISOU 1995  NZ  LYS A 275    11003   6084   8143    663  -1020   1477       N  
-ATOM   1996  N   PHE A 276      11.062 -20.036  16.623  1.00 52.28           N  
-ANISOU 1996  N   PHE A 276     8138   5207   6519    343   -765    167       N  
-ATOM   1997  CA  PHE A 276      10.461 -18.713  16.502  1.00 50.04           C  
-ANISOU 1997  CA  PHE A 276     7599   5100   6315    364   -794    -41       C  
-ATOM   1998  C   PHE A 276       8.970 -18.694  16.853  1.00 51.40           C  
-ANISOU 1998  C   PHE A 276     7757   5456   6317    146   -632   -279       C  
-ATOM   1999  O   PHE A 276       8.529 -17.877  17.662  1.00 51.64           O  
-ANISOU 1999  O   PHE A 276     7716   5640   6265     93   -663   -420       O  
-ATOM   2000  CB  PHE A 276      10.694 -18.152  15.094  1.00 45.58           C  
-ANISOU 2000  CB  PHE A 276     6800   4515   6003    553   -824    -43       C  
-ATOM   2001  CG  PHE A 276      10.125 -16.778  14.889  1.00 41.85           C  
-ANISOU 2001  CG  PHE A 276     6054   4209   5639    588   -863   -243       C  
-ATOM   2002  CD1 PHE A 276      10.715 -15.676  15.485  1.00 41.12           C  
-ANISOU 2002  CD1 PHE A 276     5851   4146   5627    682  -1049   -235       C  
-ATOM   2003  CD2 PHE A 276       8.997 -16.588  14.107  1.00 38.37           C  
-ANISOU 2003  CD2 PHE A 276     5468   3889   5222    524   -721   -436       C  
-ATOM   2004  CE1 PHE A 276      10.187 -14.407  15.307  1.00 37.29           C  
-ANISOU 2004  CE1 PHE A 276     5123   3798   5248    718  -1094   -423       C  
-ATOM   2005  CE2 PHE A 276       8.467 -15.325  13.923  1.00 37.19           C  
-ANISOU 2005  CE2 PHE A 276     5066   3890   5175    561   -755   -616       C  
-ATOM   2006  CZ  PHE A 276       9.063 -14.231  14.523  1.00 36.42           C  
-ANISOU 2006  CZ  PHE A 276     4866   3810   5161    662   -942   -611       C  
-ATOM   2007  N   LEU A 277       8.197 -19.589  16.242  1.00 47.60           N  
-ANISOU 2007  N   LEU A 277     7344   4960   5780     27   -466   -318       N  
-ATOM   2008  CA  LEU A 277       6.759 -19.660  16.500  1.00 50.69           C  
-ANISOU 2008  CA  LEU A 277     7715   5531   6012   -189   -305   -515       C  
-ATOM   2009  C   LEU A 277       6.444 -20.247  17.879  1.00 55.76           C  
-ANISOU 2009  C   LEU A 277     8563   6230   6395   -381   -260   -488       C  
-ATOM   2010  O   LEU A 277       5.319 -20.134  18.367  1.00 57.54           O  
-ANISOU 2010  O   LEU A 277     8756   6644   6464   -550   -148   -639       O  
-ATOM   2011  CB  LEU A 277       6.062 -20.490  15.416  1.00 49.21           C  
-ANISOU 2011  CB  LEU A 277     7547   5299   5851   -269   -159   -547       C  
-ATOM   2012  CG  LEU A 277       6.216 -20.039  13.962  1.00 44.50           C  
-ANISOU 2012  CG  LEU A 277     6750   4670   5487    -94   -174   -582       C  
-ATOM   2013  CD1 LEU A 277       5.620 -21.077  13.038  1.00 42.69           C  
-ANISOU 2013  CD1 LEU A 277     6607   4368   5244   -186    -42   -593       C  
-ATOM   2014  CD2 LEU A 277       5.564 -18.683  13.752  1.00 43.59           C  
-ANISOU 2014  CD2 LEU A 277     6345   4760   5456    -57   -176   -784       C  
-ATOM   2015  N   GLU A 278       7.440 -20.880  18.492  1.00 55.14           N  
-ANISOU 2015  N   GLU A 278     8685   5998   6268   -351   -346   -284       N  
-ATOM   2016  CA  GLU A 278       7.284 -21.462  19.819  1.00 60.19           C  
-ANISOU 2016  CA  GLU A 278     9521   6683   6666   -518   -317   -226       C  
-ATOM   2017  C   GLU A 278       6.205 -22.531  19.811  1.00 61.71           C  
-ANISOU 2017  C   GLU A 278     9833   6910   6703   -756   -136   -250       C  
-ATOM   2018  O   GLU A 278       5.442 -22.674  20.766  1.00 64.35           O  
-ANISOU 2018  O   GLU A 278    10219   7405   6827   -934    -58   -304       O  
-ATOM   2019  CB  GLU A 278       6.961 -20.374  20.837  1.00 63.92           C  
-ANISOU 2019  CB  GLU A 278     9889   7367   7029   -529   -369   -373       C  
-ATOM   2020  CG  GLU A 278       8.022 -19.299  20.894  1.00 69.71           C  
-ANISOU 2020  CG  GLU A 278    10512   8054   7921   -310   -573   -346       C  
-ATOM   2021  CD  GLU A 278       7.645 -18.144  21.795  1.00 74.48           C  
-ANISOU 2021  CD  GLU A 278    11010   8856   8432   -305   -637   -525       C  
-ATOM   2022  OE1 GLU A 278       8.550 -17.366  22.163  1.00 75.62           O  
-ANISOU 2022  OE1 GLU A 278    11117   8956   8660   -160   -827   -486       O  
-ATOM   2023  OE2 GLU A 278       6.448 -18.008  22.131  1.00 78.76           O  
-ANISOU 2023  OE2 GLU A 278    11508   9601   8818   -441   -503   -702       O  
-ATOM   2024  N   LEU A 279       6.160 -23.287  18.722  1.00 52.03           N  
-ANISOU 2024  N   LEU A 279     8651   5534   5584   -752    -77   -203       N  
-ATOM   2025  CA  LEU A 279       5.124 -24.289  18.525  1.00 54.03           C  
-ANISOU 2025  CA  LEU A 279     9005   5795   5728   -978     77   -228       C  
-ATOM   2026  C   LEU A 279       5.009 -25.232  19.706  1.00 58.24           C  
-ANISOU 2026  C   LEU A 279     9768   6321   6041  -1172    113    -99       C  
-ATOM   2027  O   LEU A 279       3.913 -25.656  20.061  1.00 59.89           O  
-ANISOU 2027  O   LEU A 279    10002   6659   6096  -1398    236   -154       O  
-ATOM   2028  CB  LEU A 279       5.408 -25.117  17.272  1.00 50.94           C  
-ANISOU 2028  CB  LEU A 279     8693   5180   5480   -915     92   -153       C  
-ATOM   2029  CG  LEU A 279       5.277 -24.490  15.890  1.00 44.93           C  
-ANISOU 2029  CG  LEU A 279     7722   4429   4922   -766     96   -276       C  
-ATOM   2030  CD1 LEU A 279       5.640 -25.529  14.850  1.00 43.21           C  
-ANISOU 2030  CD1 LEU A 279     7648   3974   4795   -709    107   -176       C  
-ATOM   2031  CD2 LEU A 279       3.873 -23.994  15.676  1.00 42.25           C  
-ANISOU 2031  CD2 LEU A 279     7201   4316   4535   -919    217   -491       C  
-ATOM   2032  N   LEU A 280       6.148 -25.567  20.304  1.00 68.69           N  
-ANISOU 2032  N   LEU A 280    11250   7499   7351  -1083      6     88       N  
-ATOM   2033  CA  LEU A 280       6.197 -26.606  21.331  1.00 72.90           C  
-ANISOU 2033  CA  LEU A 280    12019   7983   7695  -1251     32    250       C  
-ATOM   2034  C   LEU A 280       5.683 -26.154  22.700  1.00 75.48           C  
-ANISOU 2034  C   LEU A 280    12319   8559   7800  -1377     55    196       C  
-ATOM   2035  O   LEU A 280       5.551 -26.966  23.615  1.00 77.65           O  
-ANISOU 2035  O   LEU A 280    12764   8844   7896  -1539     93    321       O  
-ATOM   2036  CB  LEU A 280       7.614 -27.171  21.455  1.00 74.44           C  
-ANISOU 2036  CB  LEU A 280    12396   7933   7956  -1106    -87    483       C  
-ATOM   2037  CG  LEU A 280       8.049 -28.104  20.325  1.00 74.52           C  
-ANISOU 2037  CG  LEU A 280    12529   7675   8112  -1029    -82    589       C  
-ATOM   2038  CD1 LEU A 280       9.507 -28.478  20.479  1.00 76.84           C  
-ANISOU 2038  CD1 LEU A 280    12967   7758   8471   -848   -204    818       C  
-ATOM   2039  CD2 LEU A 280       7.176 -29.342  20.310  1.00 76.15           C  
-ANISOU 2039  CD2 LEU A 280    12907   7817   8209  -1275     37    618       C  
-ATOM   2040  N   SER A 281       5.389 -24.866  22.832  1.00 50.91           N  
-ANISOU 2040  N   SER A 281     8995   5651   4699  -1294     29     11       N  
-ATOM   2041  CA  SER A 281       4.846 -24.333  24.072  1.00 54.88           C  
-ANISOU 2041  CA  SER A 281     9458   6410   4983  -1383     52    -73       C  
-ATOM   2042  C   SER A 281       3.324 -24.330  24.037  1.00 59.72           C  
-ANISOU 2042  C   SER A 281     9965   7254   5473  -1575    222   -226       C  
-ATOM   2043  O   SER A 281       2.678 -23.682  24.858  1.00 61.48           O  
-ANISOU 2043  O   SER A 281    10096   7735   5527  -1620    260   -346       O  
-ATOM   2044  CB  SER A 281       5.356 -22.916  24.295  1.00 50.94           C  
-ANISOU 2044  CB  SER A 281     8799   6002   4555  -1180    -82   -196       C  
-ATOM   2045  OG  SER A 281       6.721 -22.822  23.942  1.00 48.13           O  
-ANISOU 2045  OG  SER A 281     8485   5422   4380   -985   -241    -60       O  
-ATOM   2046  N   ASP A 282       2.758 -25.047  23.073  1.00 79.25           N  
-ANISOU 2046  N   ASP A 282    12448   9636   8026  -1679    318   -220       N  
-ATOM   2047  CA  ASP A 282       1.312 -25.133  22.926  1.00 84.31           C  
-ANISOU 2047  CA  ASP A 282    12985  10482   8568  -1875    476   -339       C  
-ATOM   2048  C   ASP A 282       0.880 -26.575  22.762  1.00 89.44           C  
-ANISOU 2048  C   ASP A 282    13813  11008   9164  -2100    561   -190       C  
-ATOM   2049  O   ASP A 282       1.198 -27.220  21.770  1.00 88.48           O  
-ANISOU 2049  O   ASP A 282    13772  10645   9200  -2076    542   -131       O  
-ATOM   2050  CB  ASP A 282       0.835 -24.298  21.738  1.00 83.20           C  
-ANISOU 2050  CB  ASP A 282    12613  10393   8605  -1779    504   -536       C  
-ATOM   2051  CG  ASP A 282       0.820 -22.806  22.042  1.00 82.80           C  
-ANISOU 2051  CG  ASP A 282    12354  10540   8566  -1617    452   -718       C  
-ATOM   2052  OD1 ASP A 282       0.378 -22.433  23.154  1.00 84.39           O  
-ANISOU 2052  OD1 ASP A 282    12538  10966   8561  -1676    482   -770       O  
-ATOM   2053  OD2 ASP A 282       1.254 -22.010  21.174  1.00 81.68           O  
-ANISOU 2053  OD2 ASP A 282    12068  10330   8636  -1427    376   -807       O  
-ATOM   2054  N   ASP A 283       0.157 -27.074  23.755  1.00109.89           N  
-ANISOU 2054  N   ASP A 283    16465  13765  11525  -2314    647   -124       N  
-ATOM   2055  CA  ASP A 283      -0.332 -28.446  23.753  1.00116.16           C  
-ANISOU 2055  CA  ASP A 283    17425  14459  12253  -2558    719     34       C  
-ATOM   2056  C   ASP A 283      -1.133 -28.779  22.497  1.00115.06           C  
-ANISOU 2056  C   ASP A 283    17220  14257  12242  -2656    792    -45       C  
-ATOM   2057  O   ASP A 283      -1.052 -29.891  21.978  1.00115.86           O  
-ANISOU 2057  O   ASP A 283    17492  14122  12409  -2758    785     76       O  
-ATOM   2058  CB  ASP A 283      -1.178 -28.690  25.005  1.00124.83           C  
-ANISOU 2058  CB  ASP A 283    18527  15826  13077  -2772    814     95       C  
-ATOM   2059  CG  ASP A 283      -2.028 -27.486  25.376  1.00130.39           C  
-ANISOU 2059  CG  ASP A 283    18986  16889  13666  -2741    888   -108       C  
-ATOM   2060  OD1 ASP A 283      -1.478 -26.529  25.963  1.00133.93           O  
-ANISOU 2060  OD1 ASP A 283    19376  17436  14076  -2556    816   -191       O  
-ATOM   2061  OD2 ASP A 283      -3.243 -27.494  25.079  1.00134.43           O  
-ANISOU 2061  OD2 ASP A 283    19367  17582  14127  -2897   1011   -184       O  
-ATOM   2062  N   SER A 284      -1.901 -27.810  22.011  1.00104.85           N  
-ANISOU 2062  N   SER A 284    15684  13172  10983  -2620    854   -251       N  
-ATOM   2063  CA  SER A 284      -2.770 -28.019  20.855  1.00103.35           C  
-ANISOU 2063  CA  SER A 284    15402  12968  10899  -2721    928   -341       C  
-ATOM   2064  C   SER A 284      -1.994 -28.346  19.580  1.00 98.72           C  
-ANISOU 2064  C   SER A 284    14893  12065  10550  -2573    846   -333       C  
-ATOM   2065  O   SER A 284      -2.569 -28.831  18.607  1.00 98.88           O  
-ANISOU 2065  O   SER A 284    14909  12004  10655  -2670    888   -368       O  
-ATOM   2066  CB  SER A 284      -3.660 -26.795  20.629  1.00105.08           C  
-ANISOU 2066  CB  SER A 284    15330  13486  11110  -2680   1007   -562       C  
-ATOM   2067  OG  SER A 284      -2.879 -25.627  20.442  1.00106.96           O  
-ANISOU 2067  OG  SER A 284    15447  13724  11469  -2401    918   -684       O  
-ATOM   2068  N   ASN A 285      -0.693 -28.073  19.590  1.00 84.15           N  
-ANISOU 2068  N   ASN A 285    13115  10052   8805  -2335    726   -283       N  
-ATOM   2069  CA  ASN A 285       0.164 -28.351  18.442  1.00 78.38           C  
-ANISOU 2069  CA  ASN A 285    12456   9038   8288  -2157    645   -256       C  
-ATOM   2070  C   ASN A 285       0.667 -29.792  18.431  1.00 79.10           C  
-ANISOU 2070  C   ASN A 285    12844   8836   8374  -2238    608    -55       C  
-ATOM   2071  O   ASN A 285       0.864 -30.387  17.370  1.00 79.52           O  
-ANISOU 2071  O   ASN A 285    12985   8669   8561  -2191    585    -43       O  
-ATOM   2072  CB  ASN A 285       1.348 -27.378  18.399  1.00 71.72           C  
-ANISOU 2072  CB  ASN A 285    11529   8154   7566  -1856    527   -274       C  
-ATOM   2073  CG  ASN A 285       0.916 -25.941  18.150  1.00 65.18           C  
-ANISOU 2073  CG  ASN A 285    10407   7564   6796  -1747    543   -484       C  
-ATOM   2074  OD1 ASN A 285       1.523 -24.996  18.660  1.00 60.53           O  
-ANISOU 2074  OD1 ASN A 285     9728   7049   6220  -1585    462   -514       O  
-ATOM   2075  ND2 ASN A 285      -0.142 -25.771  17.364  1.00 60.71           N  
-ANISOU 2075  ND2 ASN A 285     9690   7112   6265  -1839    641   -626       N  
-ATOM   2076  N   PHE A 286       0.876 -30.347  19.620  1.00 77.90           N  
-ANISOU 2076  N   PHE A 286    12850   8684   8063  -2351    599    103       N  
-ATOM   2077  CA  PHE A 286       1.367 -31.713  19.747  1.00 78.76           C  
-ANISOU 2077  CA  PHE A 286    13248   8518   8160  -2433    559    309       C  
-ATOM   2078  C   PHE A 286       0.470 -32.682  18.976  1.00 79.86           C  
-ANISOU 2078  C   PHE A 286    13471   8546   8326  -2641    617    302       C  
-ATOM   2079  O   PHE A 286      -0.746 -32.691  19.161  1.00 81.30           O  
-ANISOU 2079  O   PHE A 286    13554   8928   8408  -2872    712    242       O  
-ATOM   2080  CB  PHE A 286       1.446 -32.120  21.223  1.00 79.42           C  
-ANISOU 2080  CB  PHE A 286    13451   8683   8043  -2574    564    471       C  
-ATOM   2081  CG  PHE A 286       2.585 -31.478  21.982  1.00 76.66           C  
-ANISOU 2081  CG  PHE A 286    13103   8351   7675  -2365    472    529       C  
-ATOM   2082  CD1 PHE A 286       3.603 -32.257  22.512  1.00 75.16           C  
-ANISOU 2082  CD1 PHE A 286    13141   7950   7466  -2323    394    745       C  
-ATOM   2083  CD2 PHE A 286       2.630 -30.106  22.180  1.00 75.13           C  
-ANISOU 2083  CD2 PHE A 286    12685   8378   7482  -2217    456    373       C  
-ATOM   2084  CE1 PHE A 286       4.647 -31.682  23.217  1.00 72.67           C  
-ANISOU 2084  CE1 PHE A 286    12826   7654   7132  -2144    301    809       C  
-ATOM   2085  CE2 PHE A 286       3.674 -29.525  22.883  1.00 73.36           C  
-ANISOU 2085  CE2 PHE A 286    12470   8160   7245  -2038    352    429       C  
-ATOM   2086  CZ  PHE A 286       4.682 -30.315  23.401  1.00 72.33           C  
-ANISOU 2086  CZ  PHE A 286    12562   7827   7093  -2005    275    651       C  
-ATOM   2087  N   GLY A 287       1.075 -33.484  18.103  1.00 77.60           N  
-ANISOU 2087  N   GLY A 287    13365   7945   8173  -2552    553    366       N  
-ATOM   2088  CA  GLY A 287       0.346 -34.469  17.322  1.00 79.84           C  
-ANISOU 2088  CA  GLY A 287    13766   8075   8495  -2733    578    361       C  
-ATOM   2089  C   GLY A 287      -0.695 -33.863  16.399  1.00 80.02           C  
-ANISOU 2089  C   GLY A 287    13564   8265   8576  -2786    649    152       C  
-ATOM   2090  O   GLY A 287      -1.873 -34.219  16.460  1.00 81.74           O  
-ANISOU 2090  O   GLY A 287    13749   8593   8715  -3058    720    129       O  
-ATOM   2091  N   GLN A 288      -0.264 -32.952  15.533  1.00 91.66           N  
-ANISOU 2091  N   GLN A 288    14875   9763  10190  -2528    626     12       N  
-ATOM   2092  CA  GLN A 288      -1.198 -32.237  14.674  1.00 89.55           C  
-ANISOU 2092  CA  GLN A 288    14365   9678   9982  -2553    694   -189       C  
-ATOM   2093  C   GLN A 288      -0.693 -32.064  13.251  1.00 86.14           C  
-ANISOU 2093  C   GLN A 288    13900   9089   9740  -2315    645   -282       C  
-ATOM   2094  O   GLN A 288      -1.484 -31.944  12.317  1.00 85.08           O  
-ANISOU 2094  O   GLN A 288    13650   9011   9664  -2373    690   -418       O  
-ATOM   2095  CB  GLN A 288      -1.498 -30.860  15.260  1.00 89.49           C  
-ANISOU 2095  CB  GLN A 288    14077  10005   9922  -2500    747   -304       C  
-ATOM   2096  CG  GLN A 288      -2.246 -30.905  16.562  1.00 92.89           C  
-ANISOU 2096  CG  GLN A 288    14490  10659  10144  -2737    819   -250       C  
-ATOM   2097  CD  GLN A 288      -3.559 -31.633  16.433  1.00 95.58           C  
-ANISOU 2097  CD  GLN A 288    14845  11066  10406  -3054    904   -246       C  
-ATOM   2098  OE1 GLN A 288      -4.243 -31.519  15.417  1.00 93.76           O  
-ANISOU 2098  OE1 GLN A 288    14502  10861  10260  -3094    940   -371       O  
-ATOM   2099  NE2 GLN A 288      -3.912 -32.404  17.454  1.00 96.65           N  
-ANISOU 2099  NE2 GLN A 288    15113  11230  10378  -3286    929    -90       N  
-ATOM   2100  N   PHE A 289       0.624 -32.048  13.089  1.00 78.44           N  
-ANISOU 2100  N   PHE A 289    13018   7931   8856  -2044    555   -199       N  
-ATOM   2101  CA  PHE A 289       1.221 -31.608  11.833  1.00 74.65           C  
-ANISOU 2101  CA  PHE A 289    12447   7367   8551  -1763    510   -280       C  
-ATOM   2102  C   PHE A 289       1.626 -32.733  10.886  1.00 78.42           C  
-ANISOU 2102  C   PHE A 289    13165   7530   9100  -1692    458   -225       C  
-ATOM   2103  O   PHE A 289       2.150 -33.760  11.304  1.00 79.64           O  
-ANISOU 2103  O   PHE A 289    13594   7456   9208  -1724    409    -68       O  
-ATOM   2104  CB  PHE A 289       2.409 -30.675  12.107  1.00 67.10           C  
-ANISOU 2104  CB  PHE A 289    11381   6447   7667  -1473    440   -231       C  
-ATOM   2105  CG  PHE A 289       2.005 -29.319  12.623  1.00 59.68           C  
-ANISOU 2105  CG  PHE A 289    10155   5814   6707  -1472    475   -349       C  
-ATOM   2106  CD1 PHE A 289       1.774 -29.115  13.974  1.00 56.58           C  
-ANISOU 2106  CD1 PHE A 289     9765   5572   6161  -1617    497   -307       C  
-ATOM   2107  CD2 PHE A 289       1.844 -28.250  11.752  1.00 54.52           C  
-ANISOU 2107  CD2 PHE A 289     9230   5301   6185  -1319    484   -502       C  
-ATOM   2108  CE1 PHE A 289       1.397 -27.871  14.449  1.00 52.17           C  
-ANISOU 2108  CE1 PHE A 289     8959   5289   5576  -1599    523   -429       C  
-ATOM   2109  CE2 PHE A 289       1.467 -27.002  12.222  1.00 50.73           C  
-ANISOU 2109  CE2 PHE A 289     8496   5087   5692  -1311    509   -615       C  
-ATOM   2110  CZ  PHE A 289       1.245 -26.815  13.572  1.00 50.67           C  
-ANISOU 2110  CZ  PHE A 289     8509   5218   5526  -1447    526   -585       C  
-ATOM   2111  N   GLU A 290       1.362 -32.522   9.602  1.00 71.15           N  
-ANISOU 2111  N   GLU A 290    12139   6605   8290  -1591    467   -361       N  
-ATOM   2112  CA  GLU A 290       1.869 -33.400   8.563  1.00 75.77           C  
-ANISOU 2112  CA  GLU A 290    12926   6909   8953  -1447    408   -336       C  
-ATOM   2113  C   GLU A 290       3.052 -32.716   7.892  1.00 72.34           C  
-ANISOU 2113  C   GLU A 290    12382   6450   8653  -1060    352   -318       C  
-ATOM   2114  O   GLU A 290       2.967 -31.551   7.508  1.00 70.57           O  
-ANISOU 2114  O   GLU A 290    11866   6438   8509   -939    375   -424       O  
-ATOM   2115  CB  GLU A 290       0.781 -33.710   7.531  1.00 81.77           C  
-ANISOU 2115  CB  GLU A 290    13658   7675   9735  -1591    447   -493       C  
-ATOM   2116  CG  GLU A 290       1.182 -34.767   6.508  1.00 90.50           C  
-ANISOU 2116  CG  GLU A 290    15017   8474  10895  -1473    380   -480       C  
-ATOM   2117  CD  GLU A 290       0.149 -34.953   5.410  1.00 95.99           C  
-ANISOU 2117  CD  GLU A 290    15663   9189  11618  -1591    405   -651       C  
-ATOM   2118  OE1 GLU A 290       0.359 -34.412   4.303  1.00 98.70           O  
-ANISOU 2118  OE1 GLU A 290    15859   9581  12063  -1360    402   -758       O  
-ATOM   2119  OE2 GLU A 290      -0.872 -35.634   5.652  1.00 99.37           O  
-ANISOU 2119  OE2 GLU A 290    16194   9593  11970  -1916    424   -668       O  
-ATOM   2120  N   LEU A 291       4.162 -33.438   7.775  1.00 78.52           N  
-ANISOU 2120  N   LEU A 291    13393   6979   9463   -863    277   -171       N  
-ATOM   2121  CA  LEU A 291       5.346 -32.924   7.097  1.00 74.49           C  
-ANISOU 2121  CA  LEU A 291    12795   6432   9076   -485    218   -119       C  
-ATOM   2122  C   LEU A 291       5.167 -33.056   5.594  1.00 74.40           C  
-ANISOU 2122  C   LEU A 291    12751   6367   9152   -336    222   -241       C  
-ATOM   2123  O   LEU A 291       4.709 -34.089   5.109  1.00 74.52           O  
-ANISOU 2123  O   LEU A 291    12985   6203   9128   -443    221   -283       O  
-ATOM   2124  CB  LEU A 291       6.592 -33.687   7.541  1.00 74.61           C  
-ANISOU 2124  CB  LEU A 291    13067   6205   9075   -323    142     98       C  
-ATOM   2125  CG  LEU A 291       7.900 -33.342   6.831  1.00 70.67           C  
-ANISOU 2125  CG  LEU A 291    12511   5646   8695     80     77    195       C  
-ATOM   2126  CD1 LEU A 291       8.162 -31.852   6.908  1.00 69.85           C  
-ANISOU 2126  CD1 LEU A 291    12056   5802   8680    211     70    168       C  
-ATOM   2127  CD2 LEU A 291       9.059 -34.123   7.433  1.00 72.40           C  
-ANISOU 2127  CD2 LEU A 291    12988   5642   8880    206     10    425       C  
-ATOM   2128  N   THR A 292       5.519 -32.004   4.859  1.00 79.23           N  
-ANISOU 2128  N   THR A 292    13087   7134   9881    -93    218   -296       N  
-ATOM   2129  CA  THR A 292       5.350 -31.997   3.411  1.00 79.21           C  
-ANISOU 2129  CA  THR A 292    13013   7124   9960     67    226   -413       C  
-ATOM   2130  C   THR A 292       6.506 -31.291   2.716  1.00 77.30           C  
-ANISOU 2130  C   THR A 292    12602   6923   9846    463    176   -334       C  
-ATOM   2131  O   THR A 292       6.748 -30.105   2.947  1.00 76.86           O  
-ANISOU 2131  O   THR A 292    12265   7071   9869    548    171   -323       O  
-ATOM   2132  CB  THR A 292       4.033 -31.304   2.993  1.00 79.13           C  
-ANISOU 2132  CB  THR A 292    12752   7352   9963   -127    304   -622       C  
-ATOM   2133  OG1 THR A 292       4.012 -29.966   3.506  1.00 79.64           O  
-ANISOU 2133  OG1 THR A 292    12505   7675  10078   -111    325   -642       O  
-ATOM   2134  CG2 THR A 292       2.821 -32.067   3.520  1.00 79.40           C  
-ANISOU 2134  CG2 THR A 292    12943   7354   9873   -519    353   -692       C  
-ATOM   2135  N   THR A 293       7.217 -32.024   1.863  1.00 86.42           N  
-ANISOU 2135  N   THR A 293    13930   7884  11023    709    135   -273       N  
-ATOM   2136  CA  THR A 293       8.265 -31.432   1.041  1.00 83.98           C  
-ANISOU 2136  CA  THR A 293    13453   7626  10831   1101     94   -189       C  
-ATOM   2137  C   THR A 293       7.631 -30.625  -0.086  1.00 82.88           C  
-ANISOU 2137  C   THR A 293    13021   7693  10776   1163    136   -359       C  
-ATOM   2138  O   THR A 293       6.705 -31.089  -0.752  1.00 83.10           O  
-ANISOU 2138  O   THR A 293    13114   7698  10764   1029    178   -524       O  
-ATOM   2139  CB  THR A 293       9.198 -32.501   0.439  1.00 84.74           C  
-ANISOU 2139  CB  THR A 293    13827   7464  10905   1368     44    -72       C  
-ATOM   2140  OG1 THR A 293       9.743 -33.310   1.488  1.00 84.22           O  
-ANISOU 2140  OG1 THR A 293    14043   7197  10759   1297      7     90       O  
-ATOM   2141  CG2 THR A 293      10.340 -31.842  -0.327  1.00 81.65           C  
-ANISOU 2141  CG2 THR A 293    13238   7157  10628   1784      4     51       C  
-ATOM   2142  N   PHE A 294       8.129 -29.412  -0.289  1.00 77.18           N  
-ANISOU 2142  N   PHE A 294    11976   7171  10177   1358    118   -313       N  
-ATOM   2143  CA  PHE A 294       7.562 -28.510  -1.281  1.00 76.58           C  
-ANISOU 2143  CA  PHE A 294    11585   7315  10197   1419    157   -456       C  
-ATOM   2144  C   PHE A 294       8.381 -28.570  -2.566  1.00 79.36           C  
-ANISOU 2144  C   PHE A 294    11885   7646  10624   1800    126   -390       C  
-ATOM   2145  O   PHE A 294       9.606 -28.665  -2.524  1.00 80.21           O  
-ANISOU 2145  O   PHE A 294    12039   7672  10765   2070     64   -191       O  
-ATOM   2146  CB  PHE A 294       7.526 -27.083  -0.726  1.00 69.17           C  
-ANISOU 2146  CB  PHE A 294    10306   6617   9358   1388    149   -451       C  
-ATOM   2147  CG  PHE A 294       6.716 -26.125  -1.551  1.00 61.23           C  
-ANISOU 2147  CG  PHE A 294     8972   5849   8443   1375    200   -617       C  
-ATOM   2148  CD1 PHE A 294       5.344 -26.027  -1.379  1.00 58.65           C  
-ANISOU 2148  CD1 PHE A 294     8598   5629   8056   1060    281   -812       C  
-ATOM   2149  CD2 PHE A 294       7.328 -25.306  -2.486  1.00 56.74           C  
-ANISOU 2149  CD2 PHE A 294     8130   5408   8021   1677    167   -561       C  
-ATOM   2150  CE1 PHE A 294       4.595 -25.136  -2.134  1.00 56.06           C  
-ANISOU 2150  CE1 PHE A 294     7962   5525   7814   1051    330   -958       C  
-ATOM   2151  CE2 PHE A 294       6.587 -24.417  -3.248  1.00 53.50           C  
-ANISOU 2151  CE2 PHE A 294     7409   5218   7700   1666    212   -704       C  
-ATOM   2152  CZ  PHE A 294       5.219 -24.332  -3.072  1.00 53.64           C  
-ANISOU 2152  CZ  PHE A 294     7390   5335   7657   1353    295   -907       C  
-ATOM   2153  N   ASP A 295       7.699 -28.531  -3.707  1.00 98.27           N  
-ANISOU 2153  N   ASP A 295    14181  10124  13035   1826    170   -551       N  
-ATOM   2154  CA  ASP A 295       8.371 -28.542  -5.005  1.00102.14           C  
-ANISOU 2154  CA  ASP A 295    14596  10630  13582   2193    150   -505       C  
-ATOM   2155  C   ASP A 295       7.879 -27.400  -5.883  1.00 98.97           C  
-ANISOU 2155  C   ASP A 295    13802  10506  13297   2256    185   -611       C  
-ATOM   2156  O   ASP A 295       6.817 -27.491  -6.496  1.00 98.37           O  
-ANISOU 2156  O   ASP A 295    13692  10494  13190   2104    241   -807       O  
-ATOM   2157  CB  ASP A 295       8.157 -29.878  -5.723  1.00111.19           C  
-ANISOU 2157  CB  ASP A 295    16075  11559  14612   2223    155   -591       C  
-ATOM   2158  CG  ASP A 295       8.934 -29.971  -7.027  1.00116.62           C  
-ANISOU 2158  CG  ASP A 295    16716  12261  15333   2637    134   -535       C  
-ATOM   2159  OD1 ASP A 295      10.078 -29.470  -7.076  1.00120.88           O  
-ANISOU 2159  OD1 ASP A 295    17112  12863  15952   2939     94   -333       O  
-ATOM   2160  OD2 ASP A 295       8.402 -30.543  -8.002  1.00120.82           O  
-ANISOU 2160  OD2 ASP A 295    17351  12748  15806   2663    152   -688       O  
-ATOM   2161  N   PHE A 296       8.656 -26.326  -5.949  1.00 93.18           N  
-ANISOU 2161  N   PHE A 296    12475  11686  11243  -1897    345    218       N  
-ATOM   2162  CA  PHE A 296       8.233 -25.151  -6.696  1.00 91.77           C  
-ANISOU 2162  CA  PHE A 296    12300  11548  11019  -1871    232    171       C  
-ATOM   2163  C   PHE A 296       8.229 -25.399  -8.202  1.00 90.66           C  
-ANISOU 2163  C   PHE A 296    12310  11322  10815  -1968    364    181       C  
-ATOM   2164  O   PHE A 296       7.740 -24.574  -8.972  1.00 92.67           O  
-ANISOU 2164  O   PHE A 296    12565  11637  11008  -1978    288    157       O  
-ATOM   2165  CB  PHE A 296       9.112 -23.951  -6.351  1.00 92.19           C  
-ANISOU 2165  CB  PHE A 296    12256  11528  11245  -1743    120    212       C  
-ATOM   2166  CG  PHE A 296      10.572 -24.184  -6.579  1.00 92.72           C  
-ANISOU 2166  CG  PHE A 296    12348  11387  11495  -1712    239    341       C  
-ATOM   2167  CD1 PHE A 296      11.128 -23.983  -7.828  1.00 92.45           C  
-ANISOU 2167  CD1 PHE A 296    12401  11211  11513  -1717    334    397       C  
-ATOM   2168  CD2 PHE A 296      11.392 -24.593  -5.543  1.00 93.05           C  
-ANISOU 2168  CD2 PHE A 296    12312  11386  11658  -1679    259    429       C  
-ATOM   2169  CE1 PHE A 296      12.474 -24.190  -8.044  1.00 92.98           C  
-ANISOU 2169  CE1 PHE A 296    12489  11085  11756  -1674    453    542       C  
-ATOM   2170  CE2 PHE A 296      12.740 -24.801  -5.750  1.00 93.61           C  
-ANISOU 2170  CE2 PHE A 296    12390  11271  11906  -1649    375    590       C  
-ATOM   2171  CZ  PHE A 296      13.283 -24.600  -7.004  1.00 93.01           C  
-ANISOU 2171  CZ  PHE A 296    12411  11041  11887  -1639    476    648       C  
-ATOM   2172  N   SER A 297       8.772 -26.541  -8.614  1.00 70.48           N  
-ANISOU 2172  N   SER A 297     9876   8626   8276  -2044    574    223       N  
-ATOM   2173  CA  SER A 297       8.786 -26.922 -10.020  1.00 67.85           C  
-ANISOU 2173  CA  SER A 297     9714   8204   7861  -2159    729    218       C  
-ATOM   2174  C   SER A 297       7.406 -27.374 -10.474  1.00 66.51           C  
-ANISOU 2174  C   SER A 297     9627   8203   7441  -2322    712    128       C  
-ATOM   2175  O   SER A 297       7.200 -27.685 -11.645  1.00 66.13           O  
-ANISOU 2175  O   SER A 297     9728   8126   7271  -2459    820    108       O  
-ATOM   2176  CB  SER A 297       9.798 -28.041 -10.255  1.00 67.94           C  
-ANISOU 2176  CB  SER A 297     9846   7994   7975  -2186    989    290       C  
-ATOM   2177  OG  SER A 297      11.097 -27.630  -9.883  1.00 66.80           O  
-ANISOU 2177  OG  SER A 297     9617   7702   8063  -2045   1006    416       O  
-ATOM   2178  N   GLN A 298       6.465 -27.419  -9.539  1.00 79.77           N  
-ANISOU 2178  N   GLN A 298    11209  10066   9035  -2317    575     85       N  
-ATOM   2179  CA  GLN A 298       5.100 -27.800  -9.862  1.00 79.65           C  
-ANISOU 2179  CA  GLN A 298    11246  10234   8782  -2467    532     32       C  
-ATOM   2180  C   GLN A 298       4.273 -26.571 -10.180  1.00 74.92           C  
-ANISOU 2180  C   GLN A 298    10551   9809   8105  -2445    348     35       C  
-ATOM   2181  O   GLN A 298       3.171 -26.680 -10.705  1.00 75.55           O  
-ANISOU 2181  O   GLN A 298    10666  10052   7987  -2582    307     31       O  
-ATOM   2182  CB  GLN A 298       4.456 -28.540  -8.693  1.00 85.51           C  
-ANISOU 2182  CB  GLN A 298    11922  11094   9474  -2468    485     11       C  
-ATOM   2183  CG  GLN A 298       5.124 -29.844  -8.324  1.00 95.31           C  
-ANISOU 2183  CG  GLN A 298    13233  12185  10795  -2501    674     26       C  
-ATOM   2184  CD  GLN A 298       4.601 -30.411  -7.013  1.00100.33           C  
-ANISOU 2184  CD  GLN A 298    13747  12952  11420  -2465    600     24       C  
-ATOM   2185  OE1 GLN A 298       4.048 -29.684  -6.181  1.00103.62           O  
-ANISOU 2185  OE1 GLN A 298    14012  13540  11818  -2367    407     14       O  
-ATOM   2186  NE2 GLN A 298       4.773 -31.717  -6.824  1.00102.86           N  
-ANISOU 2186  NE2 GLN A 298    14134  13190  11758  -2542    766     37       N  
-ATOM   2187  N   TYR A 299       4.804 -25.400  -9.853  1.00 67.84           N  
-ANISOU 2187  N   TYR A 299     9528   8880   7370  -2278    244     58       N  
-ATOM   2188  CA  TYR A 299       4.050 -24.165 -10.015  1.00 63.40           C  
-ANISOU 2188  CA  TYR A 299     8848   8466   6774  -2229     84     71       C  
-ATOM   2189  C   TYR A 299       4.797 -23.121 -10.842  1.00 60.18           C  
-ANISOU 2189  C   TYR A 299     8414   7954   6499  -2162     76    115       C  
-ATOM   2190  O   TYR A 299       6.024 -23.068 -10.836  1.00 60.09           O  
-ANISOU 2190  O   TYR A 299     8422   7754   6656  -2083    140    136       O  
-ATOM   2191  CB  TYR A 299       3.665 -23.589  -8.647  1.00 62.70           C  
-ANISOU 2191  CB  TYR A 299     8607   8477   6738  -2082    -64     44       C  
-ATOM   2192  CG  TYR A 299       2.938 -24.567  -7.752  1.00 62.30           C  
-ANISOU 2192  CG  TYR A 299     8555   8546   6569  -2127    -72     14       C  
-ATOM   2193  CD1 TYR A 299       1.609 -24.900  -7.986  1.00 63.15           C  
-ANISOU 2193  CD1 TYR A 299     8675   8848   6473  -2241   -112     31       C  
-ATOM   2194  CD2 TYR A 299       3.580 -25.153  -6.673  1.00 61.96           C  
-ANISOU 2194  CD2 TYR A 299     8485   8436   6622  -2062    -45     -7       C  
-ATOM   2195  CE1 TYR A 299       0.945 -25.796  -7.175  1.00 63.88           C  
-ANISOU 2195  CE1 TYR A 299     8756   9052   6462  -2276   -128     17       C  
-ATOM   2196  CE2 TYR A 299       2.924 -26.048  -5.853  1.00 62.39           C  
-ANISOU 2196  CE2 TYR A 299     8517   8609   6578  -2097    -55    -23       C  
-ATOM   2197  CZ  TYR A 299       1.607 -26.369  -6.107  1.00 63.67           C  
-ANISOU 2197  CZ  TYR A 299     8697   8952   6541  -2199    -99    -16       C  
-ATOM   2198  OH  TYR A 299       0.952 -27.265  -5.288  1.00 64.13           O  
-ANISOU 2198  OH  TYR A 299     8725   9133   6509  -2229   -118    -19       O  
-ATOM   2199  N   MET A 300       4.043 -22.292 -11.553  1.00 56.71           N  
-ANISOU 2199  N   MET A 300     7912   7645   5990  -2195     -2    152       N  
-ATOM   2200  CA  MET A 300       4.629 -21.229 -12.355  1.00 51.35           C  
-ANISOU 2200  CA  MET A 300     7176   6894   5439  -2130    -23    207       C  
-ATOM   2201  C   MET A 300       5.404 -20.266 -11.478  1.00 48.37           C  
-ANISOU 2201  C   MET A 300     6680   6407   5290  -1923   -114    199       C  
-ATOM   2202  O   MET A 300       4.961 -19.921 -10.388  1.00 47.31           O  
-ANISOU 2202  O   MET A 300     6458   6342   5174  -1833   -212    157       O  
-ATOM   2203  CB  MET A 300       3.541 -20.457 -13.091  1.00 50.36           C  
-ANISOU 2203  CB  MET A 300     6958   6964   5211  -2194   -103    273       C  
-ATOM   2204  CG  MET A 300       4.064 -19.240 -13.834  1.00 47.24           C  
-ANISOU 2204  CG  MET A 300     6461   6515   4973  -2109   -141    343       C  
-ATOM   2205  SD  MET A 300       2.717 -18.164 -14.345  1.00 42.56           S  
-ANISOU 2205  SD  MET A 300     5689   6167   4315  -2139   -246    453       S  
-ATOM   2206  CE  MET A 300       1.762 -19.295 -15.346  1.00 43.42           C  
-ANISOU 2206  CE  MET A 300     5925   6465   4108  -2438   -173    497       C  
-ATOM   2207  N   LYS A 301       6.557 -19.821 -11.958  1.00 49.03           N  
-ANISOU 2207  N   LYS A 301     6767   6323   5541  -1854    -83    243       N  
-ATOM   2208  CA  LYS A 301       7.353 -18.854 -11.218  1.00 47.92           C  
-ANISOU 2208  CA  LYS A 301     6522   6072   5615  -1681   -178    248       C  
-ATOM   2209  C   LYS A 301       7.025 -17.425 -11.642  1.00 46.32           C  
-ANISOU 2209  C   LYS A 301     6183   5918   5498  -1602   -286    284       C  
-ATOM   2210  O   LYS A 301       6.549 -17.191 -12.750  1.00 46.61           O  
-ANISOU 2210  O   LYS A 301     6202   6038   5469  -1677   -266    342       O  
-ATOM   2211  CB  LYS A 301       8.838 -19.143 -11.406  1.00 48.96           C  
-ANISOU 2211  CB  LYS A 301     6715   5988   5899  -1639    -93    307       C  
-ATOM   2212  CG  LYS A 301       9.219 -20.537 -10.981  1.00 52.56           C  
-ANISOU 2212  CG  LYS A 301     7288   6379   6305  -1705     41    298       C  
-ATOM   2213  CD  LYS A 301      10.658 -20.847 -11.318  1.00 56.93           C  
-ANISOU 2213  CD  LYS A 301     7899   6718   7014  -1665    159    398       C  
-ATOM   2214  CE  LYS A 301      10.960 -22.316 -11.051  1.00 61.57           C  
-ANISOU 2214  CE  LYS A 301     8605   7232   7556  -1742    337    408       C  
-ATOM   2215  NZ  LYS A 301      10.036 -23.215 -11.810  1.00 64.03           N  
-ANISOU 2215  NZ  LYS A 301     9050   7627   7652  -1905    452    342       N  
-ATOM   2216  N   LEU A 302       7.262 -16.476 -10.742  1.00 40.05           N  
-ANISOU 2216  N   LEU A 302     5290   5077   4850  -1463   -395    253       N  
-ATOM   2217  CA  LEU A 302       7.094 -15.063 -11.040  1.00 38.72           C  
-ANISOU 2217  CA  LEU A 302     4988   4913   4810  -1368   -484    287       C  
-ATOM   2218  C   LEU A 302       8.236 -14.286 -10.419  1.00 39.68           C  
-ANISOU 2218  C   LEU A 302     5071   4857   5150  -1239   -556    280       C  
-ATOM   2219  O   LEU A 302       9.007 -14.830  -9.629  1.00 40.21           O  
-ANISOU 2219  O   LEU A 302     5200   4833   5246  -1230   -550    254       O  
-ATOM   2220  CB  LEU A 302       5.784 -14.542 -10.467  1.00 34.44           C  
-ANISOU 2220  CB  LEU A 302     4360   4531   4195  -1339   -544    246       C  
-ATOM   2221  CG  LEU A 302       4.513 -15.262 -10.897  1.00 31.57           C  
-ANISOU 2221  CG  LEU A 302     4018   4373   3605  -1472   -499    274       C  
-ATOM   2222  CD1 LEU A 302       3.303 -14.653 -10.199  1.00 31.24           C  
-ANISOU 2222  CD1 LEU A 302     3875   4473   3523  -1410   -557    261       C  
-ATOM   2223  CD2 LEU A 302       4.351 -15.192 -12.389  1.00 33.44           C  
-ANISOU 2223  CD2 LEU A 302     4237   4671   3798  -1577   -453    385       C  
-ATOM   2224  N   ASP A 303       8.359 -13.021 -10.796  1.00 51.50           N  
-ANISOU 2224  N   ASP A 303     6457   6308   6803  -1150   -623    321       N  
-ATOM   2225  CA  ASP A 303       9.220 -12.106 -10.068  1.00 51.70           C  
-ANISOU 2225  CA  ASP A 303     6438   6182   7023  -1036   -716    299       C  
-ATOM   2226  C   ASP A 303       8.315 -11.120  -9.348  1.00 51.50           C  
-ANISOU 2226  C   ASP A 303     6329   6217   7022   -961   -781    216       C  
-ATOM   2227  O   ASP A 303       7.110 -11.089  -9.609  1.00 51.07           O  
-ANISOU 2227  O   ASP A 303     6229   6316   6860   -985   -750    218       O  
-ATOM   2228  CB  ASP A 303      10.213 -11.391 -10.999  1.00 55.64           C  
-ANISOU 2228  CB  ASP A 303     6880   6546   7714   -981   -738    415       C  
-ATOM   2229  CG  ASP A 303       9.541 -10.700 -12.188  1.00 58.14           C  
-ANISOU 2229  CG  ASP A 303     7083   6951   8055   -978   -727    494       C  
-ATOM   2230  OD1 ASP A 303      10.214 -10.534 -13.227  1.00 58.01           O  
-ANISOU 2230  OD1 ASP A 303     7036   6875   8129   -974   -711    607       O  
-ATOM   2231  OD2 ASP A 303       8.360 -10.311 -12.092  1.00 62.30           O  
-ANISOU 2231  OD2 ASP A 303     7540   7614   8519   -979   -732    464       O  
-ATOM   2232  N   ILE A 304       8.878 -10.329  -8.440  1.00 44.43           N  
-ANISOU 2232  N   ILE A 304     5420   5202   6261   -880   -863    151       N  
-ATOM   2233  CA  ILE A 304       8.085  -9.342  -7.723  1.00 46.38           C  
-ANISOU 2233  CA  ILE A 304     5608   5473   6542   -802   -900     59       C  
-ATOM   2234  C   ILE A 304       7.312  -8.494  -8.721  1.00 47.72           C  
-ANISOU 2234  C   ILE A 304     5650   5697   6785   -757   -871    144       C  
-ATOM   2235  O   ILE A 304       6.089  -8.381  -8.638  1.00 48.14           O  
-ANISOU 2235  O   ILE A 304     5654   5887   6750   -749   -828    137       O  
-ATOM   2236  CB  ILE A 304       8.959  -8.408  -6.871  1.00 46.58           C  
-ANISOU 2236  CB  ILE A 304     5640   5327   6731   -736   -990    -11       C  
-ATOM   2237  CG1 ILE A 304      10.000  -9.202  -6.085  1.00 47.52           C  
-ANISOU 2237  CG1 ILE A 304     5856   5387   6811   -799  -1028    -31       C  
-ATOM   2238  CG2 ILE A 304       8.094  -7.617  -5.909  1.00 49.33           C  
-ANISOU 2238  CG2 ILE A 304     5976   5697   7072   -672   -996   -144       C  
-ATOM   2239  CD1 ILE A 304       9.408 -10.007  -4.949  1.00 49.69           C  
-ANISOU 2239  CD1 ILE A 304     6196   5786   6899   -848  -1011   -142       C  
-ATOM   2240  N   ALA A 305       8.038  -7.919  -9.677  1.00 40.76           N  
-ANISOU 2240  N   ALA A 305     4699   4720   6069   -729   -892    251       N  
-ATOM   2241  CA  ALA A 305       7.456  -7.012 -10.660  1.00 40.81           C  
-ANISOU 2241  CA  ALA A 305     4550   4773   6183   -684   -870    360       C  
-ATOM   2242  C   ALA A 305       6.262  -7.624 -11.391  1.00 40.52           C  
-ANISOU 2242  C   ALA A 305     4473   4960   5962   -775   -793    440       C  
-ATOM   2243  O   ALA A 305       5.291  -6.932 -11.691  1.00 40.67           O  
-ANISOU 2243  O   ALA A 305     4360   5077   6016   -742   -763    510       O  
-ATOM   2244  CB  ALA A 305       8.515  -6.559 -11.647  1.00 41.75           C  
-ANISOU 2244  CB  ALA A 305     4605   4778   6481   -658   -906    480       C  
-ATOM   2245  N   ALA A 306       6.335  -8.919 -11.677  1.00 39.96           N  
-ANISOU 2245  N   ALA A 306     4514   4968   5700   -897   -754    445       N  
-ATOM   2246  CA  ALA A 306       5.235  -9.608 -12.348  1.00 41.81           C  
-ANISOU 2246  CA  ALA A 306     4737   5418   5730  -1019   -690    517       C  
-ATOM   2247  C   ALA A 306       3.984  -9.579 -11.480  1.00 43.52           C  
-ANISOU 2247  C   ALA A 306     4934   5763   5840  -1001   -679    468       C  
-ATOM   2248  O   ALA A 306       2.934  -9.098 -11.906  1.00 44.98           O  
-ANISOU 2248  O   ALA A 306     4992   6090   6009  -1005   -652    575       O  
-ATOM   2249  CB  ALA A 306       5.618 -11.040 -12.683  1.00 39.79           C  
-ANISOU 2249  CB  ALA A 306     4638   5187   5294  -1158   -638    503       C  
-ATOM   2250  N   VAL A 307       4.111 -10.099 -10.260  1.00 45.84           N  
-ANISOU 2250  N   VAL A 307     5340   6013   6064   -979   -697    327       N  
-ATOM   2251  CA  VAL A 307       3.040 -10.076  -9.266  1.00 46.29           C  
-ANISOU 2251  CA  VAL A 307     5389   6173   6025   -939   -690    265       C  
-ATOM   2252  C   VAL A 307       2.370  -8.713  -9.202  1.00 48.31           C  
-ANISOU 2252  C   VAL A 307     5500   6424   6430   -817   -677    312       C  
-ATOM   2253  O   VAL A 307       1.167  -8.603  -8.953  1.00 47.27           O  
-ANISOU 2253  O   VAL A 307     5308   6433   6218   -799   -636    359       O  
-ATOM   2254  CB  VAL A 307       3.595 -10.375  -7.859  1.00 44.96           C  
-ANISOU 2254  CB  VAL A 307     5331   5905   5845   -893   -729     97       C  
-ATOM   2255  CG1 VAL A 307       2.510 -10.203  -6.811  1.00 43.11           C  
-ANISOU 2255  CG1 VAL A 307     5083   5771   5527   -831   -718     30       C  
-ATOM   2256  CG2 VAL A 307       4.190 -11.772  -7.805  1.00 45.30           C  
-ANISOU 2256  CG2 VAL A 307     5500   5956   5755  -1005   -720     70       C  
-ATOM   2257  N   ARG A 308       3.171  -7.678  -9.426  1.00 50.15           N  
-ANISOU 2257  N   ARG A 308     5674   6487   6894   -729   -704    313       N  
-ATOM   2258  CA  ARG A 308       2.728  -6.298  -9.299  1.00 55.23           C  
-ANISOU 2258  CA  ARG A 308     6187   7071   7726   -598   -678    343       C  
-ATOM   2259  C   ARG A 308       2.135  -5.790 -10.606  1.00 56.94           C  
-ANISOU 2259  C   ARG A 308     6219   7402   8014   -617   -632    558       C  
-ATOM   2260  O   ARG A 308       1.171  -5.024 -10.605  1.00 58.34           O  
-ANISOU 2260  O   ARG A 308     6262   7643   8263   -546   -568    650       O  
-ATOM   2261  CB  ARG A 308       3.909  -5.425  -8.887  1.00 57.18           C  
-ANISOU 2261  CB  ARG A 308     6460   7073   8194   -506   -736    243       C  
-ATOM   2262  CG  ARG A 308       3.555  -4.015  -8.483  1.00 63.68           C  
-ANISOU 2262  CG  ARG A 308     7192   7784   9220   -367   -697    220       C  
-ATOM   2263  CD  ARG A 308       4.772  -3.342  -7.870  1.00 69.45           C  
-ANISOU 2263  CD  ARG A 308     7997   8271  10118   -314   -771     87       C  
-ATOM   2264  NE  ARG A 308       5.278  -4.088  -6.720  1.00 72.93           N  
-ANISOU 2264  NE  ARG A 308     8616   8681  10412   -366   -827    -82       N  
-ATOM   2265  CZ  ARG A 308       6.514  -3.985  -6.242  1.00 74.09           C  
-ANISOU 2265  CZ  ARG A 308     8853   8668  10629   -385   -919   -166       C  
-ATOM   2266  NH1 ARG A 308       7.386  -3.168  -6.818  1.00 75.41           N  
-ANISOU 2266  NH1 ARG A 308     8959   8680  11013   -349   -971   -104       N  
-ATOM   2267  NH2 ARG A 308       6.881  -4.705  -5.191  1.00 75.52           N  
-ANISOU 2267  NH2 ARG A 308     9171   8857  10666   -448   -963   -291       N  
-ATOM   2268  N   ALA A 309       2.715  -6.223 -11.720  1.00 55.65           N  
-ANISOU 2268  N   ALA A 309     6042   7270   7831   -716   -656    651       N  
-ATOM   2269  CA  ALA A 309       2.290  -5.760 -13.035  1.00 57.01           C  
-ANISOU 2269  CA  ALA A 309     6030   7566   8065   -758   -625    864       C  
-ATOM   2270  C   ALA A 309       0.982  -6.421 -13.455  1.00 58.20           C  
-ANISOU 2270  C   ALA A 309     6136   7986   7990   -888   -574    997       C  
-ATOM   2271  O   ALA A 309       0.107  -5.778 -14.033  1.00 59.86           O  
-ANISOU 2271  O   ALA A 309     6156   8333   8256   -887   -528   1186       O  
-ATOM   2272  CB  ALA A 309       3.375  -6.029 -14.064  1.00 56.27           C  
-ANISOU 2272  CB  ALA A 309     5952   7420   8008   -826   -663    913       C  
-ATOM   2273  N   LEU A 310       0.858  -7.710 -13.160  1.00 47.94           N  
-ANISOU 2273  N   LEU A 310     5005   6767   6442  -1007   -581    915       N  
-ATOM   2274  CA  LEU A 310      -0.352  -8.453 -13.473  1.00 49.04           C  
-ANISOU 2274  CA  LEU A 310     5130   7160   6343  -1152   -549   1031       C  
-ATOM   2275  C   LEU A 310      -1.450  -8.177 -12.441  1.00 52.56           C  
-ANISOU 2275  C   LEU A 310     5535   7673   6762  -1057   -518   1031       C  
-ATOM   2276  O   LEU A 310      -2.522  -8.779 -12.487  1.00 52.48           O  
-ANISOU 2276  O   LEU A 310     5512   7872   6555  -1158   -499   1134       O  
-ATOM   2277  CB  LEU A 310      -0.044  -9.947 -13.537  1.00 43.86           C  
-ANISOU 2277  CB  LEU A 310     4676   6544   5445  -1314   -559    938       C  
-ATOM   2278  CG  LEU A 310       1.012 -10.356 -14.558  1.00 41.00           C  
-ANISOU 2278  CG  LEU A 310     4383   6112   5085  -1412   -559    940       C  
-ATOM   2279  CD1 LEU A 310       1.212 -11.856 -14.539  1.00 40.56           C  
-ANISOU 2279  CD1 LEU A 310     4535   6079   4796  -1566   -535    848       C  
-ATOM   2280  CD2 LEU A 310       0.578  -9.907 -15.931  1.00 41.76           C  
-ANISOU 2280  CD2 LEU A 310     4316   6370   5182  -1515   -541   1152       C  
-ATOM   2281  N   ASN A 311      -1.178  -7.259 -11.516  1.00 69.85           N  
-ANISOU 2281  N   ASN A 311     7710   9684   9146   -869   -510    921       N  
-ATOM   2282  CA  ASN A 311      -2.121  -6.926 -10.453  1.00 74.56           C  
-ANISOU 2282  CA  ASN A 311     8287  10310   9733   -756   -461    898       C  
-ATOM   2283  C   ASN A 311      -2.820  -8.145  -9.884  1.00 74.55           C  
-ANISOU 2283  C   ASN A 311     8399  10469   9457   -847   -474    865       C  
-ATOM   2284  O   ASN A 311      -4.000  -8.356 -10.136  1.00 75.85           O  
-ANISOU 2284  O   ASN A 311     8477  10845   9498   -906   -439   1042       O  
-ATOM   2285  CB  ASN A 311      -3.171  -5.931 -10.945  1.00 82.54           C  
-ANISOU 2285  CB  ASN A 311     9071  11428  10864   -696   -376   1136       C  
-ATOM   2286  CG  ASN A 311      -2.717  -4.499 -10.810  1.00 89.92           C  
-ANISOU 2286  CG  ASN A 311     9903  12150  12111   -519   -331   1113       C  
-ATOM   2287  OD1 ASN A 311      -3.315  -3.588 -11.384  1.00 94.27           O  
-ANISOU 2287  OD1 ASN A 311    10246  12752  12821   -466   -253   1321       O  
-ATOM   2288  ND2 ASN A 311      -1.642  -4.290 -10.055  1.00 94.63           N  
-ANISOU 2288  ND2 ASN A 311    10640  12510  12804   -438   -378    874       N  
-ATOM   2289  N   LEU A 312      -2.100  -8.949  -9.114  1.00 55.35           N  
-ANISOU 2289  N   LEU A 312     6147   7947   6937   -864   -525    660       N  
-ATOM   2290  CA  LEU A 312      -2.692 -10.162  -8.575  1.00 54.38           C  
-ANISOU 2290  CA  LEU A 312     6125   7971   6567   -952   -541    628       C  
-ATOM   2291  C   LEU A 312      -3.416  -9.905  -7.260  1.00 56.89           C  
-ANISOU 2291  C   LEU A 312     6446   8305   6865   -815   -516    560       C  
-ATOM   2292  O   LEU A 312      -4.462 -10.497  -6.998  1.00 58.32           O  
-ANISOU 2292  O   LEU A 312     6615   8672   6873   -854   -505    644       O  
-ATOM   2293  CB  LEU A 312      -1.633 -11.249  -8.409  1.00 48.74           C  
-ANISOU 2293  CB  LEU A 312     5581   7172   5767  -1043   -590    474       C  
-ATOM   2294  CG  LEU A 312      -0.915 -11.620  -9.706  1.00 44.48           C  
-ANISOU 2294  CG  LEU A 312     5064   6611   5227  -1178   -592    537       C  
-ATOM   2295  CD1 LEU A 312       0.058 -12.771  -9.480  1.00 41.68           C  
-ANISOU 2295  CD1 LEU A 312     4881   6166   4791  -1258   -607    406       C  
-ATOM   2296  CD2 LEU A 312      -1.924 -11.974 -10.785  1.00 40.33           C  
-ANISOU 2296  CD2 LEU A 312     4466   6312   4544  -1336   -567    736       C  
-ATOM   2297  N   PHE A 313      -2.865  -9.011  -6.444  1.00 67.90           N  
-ANISOU 2297  N   PHE A 313     7860   9507   8432   -662   -505    412       N  
-ATOM   2298  CA  PHE A 313      -3.423  -8.742  -5.123  1.00 70.56           C  
-ANISOU 2298  CA  PHE A 313     8228   9836   8746   -533   -471    312       C  
-ATOM   2299  C   PHE A 313      -3.530  -7.249  -4.841  1.00 75.77           C  
-ANISOU 2299  C   PHE A 313     8812  10344   9632   -364   -389    299       C  
-ATOM   2300  O   PHE A 313      -4.138  -6.830  -3.856  1.00 75.40           O  
-ANISOU 2300  O   PHE A 313     8779  10285   9584   -242   -324    240       O  
-ATOM   2301  CB  PHE A 313      -2.586  -9.430  -4.045  1.00 64.17           C  
-ANISOU 2301  CB  PHE A 313     7577   8946   7859   -547   -539     84       C  
-ATOM   2302  CG  PHE A 313      -2.311 -10.872  -4.332  1.00 57.61           C  
-ANISOU 2302  CG  PHE A 313     6822   8220   6849   -707   -599     90       C  
-ATOM   2303  CD1 PHE A 313      -3.331 -11.805  -4.282  1.00 56.31           C  
-ANISOU 2303  CD1 PHE A 313     6649   8268   6479   -777   -596    183       C  
-ATOM   2304  CD2 PHE A 313      -1.036 -11.298  -4.656  1.00 55.44           C  
-ANISOU 2304  CD2 PHE A 313     6626   7821   6618   -786   -647     16       C  
-ATOM   2305  CE1 PHE A 313      -3.087 -13.137  -4.552  1.00 54.89           C  
-ANISOU 2305  CE1 PHE A 313     6548   8164   6143   -929   -635    182       C  
-ATOM   2306  CE2 PHE A 313      -0.782 -12.629  -4.927  1.00 53.92           C  
-ANISOU 2306  CE2 PHE A 313     6510   7702   6276   -926   -670     24       C  
-ATOM   2307  CZ  PHE A 313      -1.811 -13.551  -4.874  1.00 53.75           C  
-ANISOU 2307  CZ  PHE A 313     6488   7881   6053  -1001   -661     97       C  
-ATOM   2308  N   GLN A 314      -2.934  -6.447  -5.714  1.00 77.67           N  
-ANISOU 2308  N   GLN A 314     8975  10465  10071   -354   -384    356       N  
-ATOM   2309  CA  GLN A 314      -3.049  -5.000  -5.610  1.00 84.52           C  
-ANISOU 2309  CA  GLN A 314     9752  11180  11182   -200   -292    370       C  
-ATOM   2310  C   GLN A 314      -3.437  -4.422  -6.965  1.00 88.11           C  
-ANISOU 2310  C   GLN A 314    10004  11706  11769   -218   -243    630       C  
-ATOM   2311  O   GLN A 314      -3.498  -5.147  -7.956  1.00 88.43           O  
-ANISOU 2311  O   GLN A 314     9997  11905  11696   -364   -294    771       O  
-ATOM   2312  CB  GLN A 314      -1.740  -4.381  -5.123  1.00 85.44           C  
-ANISOU 2312  CB  GLN A 314     9971  11034  11459   -152   -342    153       C  
-ATOM   2313  CG  GLN A 314      -1.939  -3.113  -4.309  1.00 88.82           C  
-ANISOU 2313  CG  GLN A 314    10402  11282  12062     10   -239     53       C  
-ATOM   2314  CD  GLN A 314      -0.787  -2.140  -4.451  1.00 89.07           C  
-ANISOU 2314  CD  GLN A 314    10449  11061  12333     46   -273    -45       C  
-ATOM   2315  OE1 GLN A 314      -0.870  -0.996  -4.004  1.00 88.76           O  
-ANISOU 2315  OE1 GLN A 314    10404  10847  12473    166   -180   -113       O  
-ATOM   2316  NE2 GLN A 314       0.293  -2.586  -5.085  1.00 86.29           N  
-ANISOU 2316  NE2 GLN A 314    10118  10679  11989    -57   -397    -45       N  
-ATOM   2317  N   GLY A 315      -3.701  -3.119  -7.006  1.00114.23           N  
-ANISOU 2317  N   GLY A 315    13190  14897  15317    -78   -136    697       N  
-ATOM   2318  CA  GLY A 315      -4.100  -2.470  -8.243  1.00118.95           C  
-ANISOU 2318  CA  GLY A 315    13559  15570  16068    -85    -78    970       C  
-ATOM   2319  C   GLY A 315      -3.832  -0.976  -8.303  1.00122.94           C  
-ANISOU 2319  C   GLY A 315    13953  15857  16903     69     16    982       C  
-ATOM   2320  O   GLY A 315      -2.949  -0.461  -7.615  1.00125.15           O  
-ANISOU 2320  O   GLY A 315    14357  15891  17303    144     -6    750       O  
-ATOM   2321  N   SER A 316      -4.603  -0.288  -9.142  1.00104.60           N  
-ANISOU 2321  N   SER A 316    11386  13629  14727    103    122   1270       N  
-ATOM   2322  CA  SER A 316      -4.479   1.155  -9.336  1.00106.53           C  
-ANISOU 2322  CA  SER A 316    11480  13682  15314    250    236   1335       C  
-ATOM   2323  C   SER A 316      -3.185   1.520 -10.052  1.00106.34           C  
-ANISOU 2323  C   SER A 316    11432  13515  15457    215    126   1276       C  
-ATOM   2324  O   SER A 316      -3.129   2.512 -10.779  1.00107.08           O  
-ANISOU 2324  O   SER A 316    11319  13550  15818    278    188   1441       O  
-ATOM   2325  CB  SER A 316      -4.582   1.892  -8.006  1.00107.62           C  
-ANISOU 2325  CB  SER A 316    11748  13584  15559    425    356   1125       C  
-ATOM   2326  N   SER A 323      -7.964   0.696 -10.073  1.00105.46           N  
-ANISOU 2326  N   SER A 323    10927  14184  14960    203    492   2104       N  
-ATOM   2327  CA  SER A 323      -8.725  -0.343 -10.758  1.00104.65           C  
-ANISOU 2327  CA  SER A 323    10752  14422  14590      9    420   2342       C  
-ATOM   2328  C   SER A 323      -9.205  -1.438  -9.802  1.00101.44           C  
-ANISOU 2328  C   SER A 323    10549  14113  13881    -25    372   2212       C  
-ATOM   2329  O   SER A 323     -10.257  -1.311  -9.175  1.00102.86           O  
-ANISOU 2329  O   SER A 323    10688  14361  14035     76    492   2337       O  
-ATOM   2330  CB  SER A 323      -7.903  -0.947 -11.890  1.00104.65           C  
-ANISOU 2330  CB  SER A 323    10749  14518  14497   -198    256   2344       C  
-ATOM   2331  N   GLN A 324      -8.424  -2.510  -9.699  1.00 95.36           N  
-ANISOU 2331  N   GLN A 324     9987  13349  12897   -160    206   1977       N  
-ATOM   2332  CA  GLN A 324      -8.793  -3.675  -8.903  1.00 88.08           C  
-ANISOU 2332  CA  GLN A 324     9244  12539  11684   -218    140   1862       C  
-ATOM   2333  C   GLN A 324      -7.637  -4.666  -8.942  1.00 81.16           C  
-ANISOU 2333  C   GLN A 324     8574  11608  10656   -356    -23   1601       C  
-ATOM   2334  O   GLN A 324      -6.675  -4.460  -9.675  1.00 81.80           O  
-ANISOU 2334  O   GLN A 324     8646  11593  10842   -411    -80   1551       O  
-ATOM   2335  CB  GLN A 324     -10.053  -4.327  -9.479  1.00 90.77           C  
-ANISOU 2335  CB  GLN A 324     9453  13211  11825   -357    143   2195       C  
-ATOM   2336  CG  GLN A 324     -10.732  -5.329  -8.550  1.00 91.82           C  
-ANISOU 2336  CG  GLN A 324     9721  13469  11697   -372    109   2141       C  
-ATOM   2337  CD  GLN A 324     -11.876  -6.075  -9.219  1.00 92.66           C  
-ANISOU 2337  CD  GLN A 324     9711  13911  11583   -552     78   2476       C  
-ATOM   2338  OE1 GLN A 324     -11.925  -6.192 -10.443  1.00 91.84           O  
-ANISOU 2338  OE1 GLN A 324     9487  13962  11445   -737     35   2680       O  
-ATOM   2339  NE2 GLN A 324     -12.801  -6.585  -8.415  1.00 93.16           N  
-ANISOU 2339  NE2 GLN A 324     9810  14099  11489   -509     94   2540       N  
-ATOM   2340  N   SER A 325      -7.720  -5.735  -8.156  1.00 62.09           N  
-ANISOU 2340  N   SER A 325     6333   9252   8006   -404    -91   1450       N  
-ATOM   2341  CA  SER A 325      -6.726  -6.798  -8.230  1.00 54.32           C  
-ANISOU 2341  CA  SER A 325     5529   8238   6873   -546   -224   1248       C  
-ATOM   2342  C   SER A 325      -7.347  -8.020  -8.881  1.00 49.26           C  
-ANISOU 2342  C   SER A 325     4892   7861   5962   -759   -286   1403       C  
-ATOM   2343  O   SER A 325      -8.564  -8.154  -8.916  1.00 49.58           O  
-ANISOU 2343  O   SER A 325     4832   8107   5898   -783   -246   1624       O  
-ATOM   2344  CB  SER A 325      -6.201  -7.155  -6.842  1.00 52.61           C  
-ANISOU 2344  CB  SER A 325     5507   7879   6602   -459   -258    951       C  
-ATOM   2345  OG  SER A 325      -7.166  -7.880  -6.102  1.00 52.15           O  
-ANISOU 2345  OG  SER A 325     5485   7987   6343   -459   -252    984       O  
-ATOM   2346  N   LEU A 326      -6.513  -8.908  -9.406  1.00 55.39           N  
-ANISOU 2346  N   LEU A 326     5789   8628   6628   -920   -374   1299       N  
-ATOM   2347  CA  LEU A 326      -7.014 -10.110 -10.063  1.00 51.03           C  
-ANISOU 2347  CA  LEU A 326     5275   8302   5813  -1148   -425   1416       C  
-ATOM   2348  C   LEU A 326      -7.684 -11.009  -9.033  1.00 51.09           C  
-ANISOU 2348  C   LEU A 326     5380   8409   5624  -1145   -448   1360       C  
-ATOM   2349  O   LEU A 326      -8.636 -11.735  -9.340  1.00 50.13           O  
-ANISOU 2349  O   LEU A 326     5233   8518   5298  -1287   -469   1534       O  
-ATOM   2350  CB  LEU A 326      -5.882 -10.862 -10.761  1.00 46.29           C  
-ANISOU 2350  CB  LEU A 326     4810   7625   5154  -1301   -484   1287       C  
-ATOM   2351  CG  LEU A 326      -6.337 -12.054 -11.594  1.00 42.54           C  
-ANISOU 2351  CG  LEU A 326     4391   7361   4411  -1563   -517   1398       C  
-ATOM   2352  CD1 LEU A 326      -7.204 -11.563 -12.740  1.00 43.23           C  
-ANISOU 2352  CD1 LEU A 326     4286   7663   4478  -1682   -494   1705       C  
-ATOM   2353  CD2 LEU A 326      -5.150 -12.846 -12.114  1.00 39.76           C  
-ANISOU 2353  CD2 LEU A 326     4209   6889   4010  -1687   -542   1236       C  
-ATOM   2354  N   ALA A 327      -7.171 -10.955  -7.807  1.00 37.48           N  
-ANISOU 2354  N   ALA A 327     3763   6520   3959   -991   -452   1123       N  
-ATOM   2355  CA  ALA A 327      -7.743 -11.715  -6.705  1.00 38.24           C  
-ANISOU 2355  CA  ALA A 327     3935   6701   3892   -959   -474   1058       C  
-ATOM   2356  C   ALA A 327      -9.076 -11.105  -6.293  1.00 40.39           C  
-ANISOU 2356  C   ALA A 327     4070   7104   4171   -838   -401   1255       C  
-ATOM   2357  O   ALA A 327     -10.041 -11.818  -6.030  1.00 39.58           O  
-ANISOU 2357  O   ALA A 327     3956   7200   3884   -889   -421   1379       O  
-ATOM   2358  CB  ALA A 327      -6.786 -11.754  -5.532  1.00 37.79           C  
-ANISOU 2358  CB  ALA A 327     4013   6447   3899   -843   -496    766       C  
-ATOM   2359  N   ALA A 328      -9.136  -9.779  -6.254  1.00 70.07           N  
-ANISOU 2359  N   ALA A 328     7721  10749   8155   -674   -307   1300       N  
-ATOM   2360  CA  ALA A 328     -10.385  -9.104  -5.925  1.00 74.27           C  
-ANISOU 2360  CA  ALA A 328     8110  11382   8727   -541   -201   1517       C  
-ATOM   2361  C   ALA A 328     -11.421  -9.346  -7.018  1.00 78.08           C  
-ANISOU 2361  C   ALA A 328     8431  12131   9104   -697   -201   1881       C  
-ATOM   2362  O   ALA A 328     -12.593  -9.004  -6.859  1.00 80.49           O  
-ANISOU 2362  O   ALA A 328     8601  12578   9405   -624   -121   2135       O  
-ATOM   2363  CB  ALA A 328     -10.154  -7.613  -5.727  1.00 74.02           C  
-ANISOU 2363  CB  ALA A 328     8000  11140   8983   -339    -77   1486       C  
-ATOM   2364  N   LEU A 329     -10.982  -9.936  -8.125  1.00 66.32           N  
-ANISOU 2364  N   LEU A 329     6959  10715   7525   -920   -283   1919       N  
-ATOM   2365  CA  LEU A 329     -11.859 -10.161  -9.265  1.00 70.27           C  
-ANISOU 2365  CA  LEU A 329     7314  11478   7908  -1115   -295   2259       C  
-ATOM   2366  C   LEU A 329     -12.411 -11.577  -9.274  1.00 70.71           C  
-ANISOU 2366  C   LEU A 329     7467  11746   7653  -1318   -393   2308       C  
-ATOM   2367  O   LEU A 329     -13.575 -11.792  -9.611  1.00 72.84           O  
-ANISOU 2367  O   LEU A 329     7619  12267   7789  -1421   -396   2615       O  
-ATOM   2368  CB  LEU A 329     -11.113  -9.901 -10.575  1.00 71.73           C  
-ANISOU 2368  CB  LEU A 329     7452  11635   8169  -1259   -316   2291       C  
-ATOM   2369  CG  LEU A 329     -11.957  -9.953 -11.850  1.00 75.41           C  
-ANISOU 2369  CG  LEU A 329     7742  12382   8530  -1480   -322   2659       C  
-ATOM   2370  CD1 LEU A 329     -12.567  -8.592 -12.136  1.00 78.10           C  
-ANISOU 2370  CD1 LEU A 329     7813  12753   9108  -1344   -203   2942       C  
-ATOM   2371  CD2 LEU A 329     -11.119 -10.409 -13.025  1.00 73.57           C  
-ANISOU 2371  CD2 LEU A 329     7574  12156   8223  -1706   -389   2598       C  
-ATOM   2372  N   LEU A 330     -11.567 -12.539  -8.912  1.00 78.54           N  
-ANISOU 2372  N   LEU A 330     8667  12636   8540  -1381   -470   2023       N  
-ATOM   2373  CA  LEU A 330     -11.942 -13.950  -8.968  1.00 79.23           C  
-ANISOU 2373  CA  LEU A 330     8866  12890   8347  -1587   -558   2037       C  
-ATOM   2374  C   LEU A 330     -12.294 -14.550  -7.609  1.00 79.36           C  
-ANISOU 2374  C   LEU A 330     8962  12916   8276  -1467   -584   1924       C  
-ATOM   2375  O   LEU A 330     -12.888 -15.625  -7.539  1.00 79.34           O  
-ANISOU 2375  O   LEU A 330     9010  13083   8052  -1609   -651   1995       O  
-ATOM   2376  CB  LEU A 330     -10.833 -14.776  -9.621  1.00 78.09           C  
-ANISOU 2376  CB  LEU A 330     8893  12647   8131  -1772   -608   1838       C  
-ATOM   2377  CG  LEU A 330     -10.909 -14.934 -11.138  1.00 78.30           C  
-ANISOU 2377  CG  LEU A 330     8883  12807   8061  -2034   -621   2014       C  
-ATOM   2378  CD1 LEU A 330     -10.978 -13.577 -11.809  1.00 79.21           C  
-ANISOU 2378  CD1 LEU A 330     8794  12920   8381  -1956   -560   2192       C  
-ATOM   2379  CD2 LEU A 330      -9.725 -15.741 -11.661  1.00 77.60           C  
-ANISOU 2379  CD2 LEU A 330     8990  12578   7917  -2181   -640   1785       C  
-ATOM   2380  N   ASN A 331     -11.925 -13.866  -6.533  1.00 71.43           N  
-ANISOU 2380  N   ASN A 331     7969  11735   7438  -1216   -533   1747       N  
-ATOM   2381  CA  ASN A 331     -12.184 -14.379  -5.196  1.00 70.28           C  
-ANISOU 2381  CA  ASN A 331     7892  11599   7213  -1095   -554   1624       C  
-ATOM   2382  C   ASN A 331     -13.582 -14.006  -4.715  1.00 72.91           C  
-ANISOU 2382  C   ASN A 331     8086  12106   7510   -975   -504   1882       C  
-ATOM   2383  O   ASN A 331     -13.759 -13.074  -3.932  1.00 74.14           O  
-ANISOU 2383  O   ASN A 331     8192  12166   7811   -743   -411   1852       O  
-ATOM   2384  CB  ASN A 331     -11.125 -13.876  -4.218  1.00 69.51           C  
-ANISOU 2384  CB  ASN A 331     7886  11246   7279   -908   -527   1310       C  
-ATOM   2385  CG  ASN A 331     -10.948 -14.795  -3.030  1.00 68.01           C  
-ANISOU 2385  CG  ASN A 331     7806  11062   6972   -873   -585   1122       C  
-ATOM   2386  OD1 ASN A 331     -11.504 -15.891  -2.991  1.00 66.98           O  
-ANISOU 2386  OD1 ASN A 331     7696  11106   6649   -991   -650   1204       O  
-ATOM   2387  ND2 ASN A 331     -10.158 -14.358  -2.056  1.00 68.06           N  
-ANISOU 2387  ND2 ASN A 331     7880  10885   7094   -723   -566    875       N  
-ATOM   2388  N   LYS A 332     -14.574 -14.742  -5.201  1.00 66.77           N  
-ANISOU 2388  N   LYS A 332     7252  11582   6535  -1142   -560   2144       N  
-ATOM   2389  CA  LYS A 332     -15.966 -14.506  -4.844  1.00 71.38           C  
-ANISOU 2389  CA  LYS A 332     7691  12364   7066  -1053   -521   2450       C  
-ATOM   2390  C   LYS A 332     -16.493 -15.658  -3.998  1.00 71.31           C  
-ANISOU 2390  C   LYS A 332     7748  12496   6850  -1072   -611   2436       C  
-ATOM   2391  O   LYS A 332     -17.657 -16.054  -4.118  1.00 73.39           O  
-ANISOU 2391  O   LYS A 332     7918  13001   6965  -1143   -645   2740       O  
-ATOM   2392  CB  LYS A 332     -16.821 -14.339  -6.104  1.00 72.97           C  
-ANISOU 2392  CB  LYS A 332     7735  12784   7207  -1238   -519   2841       C  
-ATOM   2393  CG  LYS A 332     -16.885 -12.912  -6.621  1.00 74.17           C  
-ANISOU 2393  CG  LYS A 332     7720  12863   7599  -1121   -387   2999       C  
-ATOM   2394  CD  LYS A 332     -15.521 -12.413  -7.044  1.00 73.74           C  
-ANISOU 2394  CD  LYS A 332     7743  12558   7718  -1115   -370   2720       C  
-ATOM   2395  CE  LYS A 332     -15.436 -10.898  -6.948  1.00 75.11           C  
-ANISOU 2395  CE  LYS A 332     7786  12569   8185   -885   -218   2761       C  
-ATOM   2396  NZ  LYS A 332     -15.508 -10.434  -5.532  1.00 76.16           N  
-ANISOU 2396  NZ  LYS A 332     7971  12550   8417   -602   -131   2593       N  
-ATOM   2397  N   CYS A 333     -15.628 -16.188  -3.138  1.00 76.44           N  
-ANISOU 2397  N   CYS A 333     8545  13002   7496  -1013   -651   2102       N  
-ATOM   2398  CA  CYS A 333     -15.968 -17.357  -2.339  1.00 73.26           C  
-ANISOU 2398  CA  CYS A 333     8202  12721   6913  -1040   -742   2062       C  
-ATOM   2399  C   CYS A 333     -16.876 -17.029  -1.158  1.00 73.38           C  
-ANISOU 2399  C   CYS A 333     8133  12822   6926   -803   -698   2159       C  
-ATOM   2400  O   CYS A 333     -16.871 -15.911  -0.640  1.00 72.18           O  
-ANISOU 2400  O   CYS A 333     7937  12550   6937   -579   -581   2119       O  
-ATOM   2401  CB  CYS A 333     -14.702 -18.074  -1.873  1.00 73.37           C  
-ANISOU 2401  CB  CYS A 333     8377  12567   6934  -1074   -793   1704       C  
-ATOM   2402  SG  CYS A 333     -13.923 -19.058  -3.170  1.00 73.88           S  
-ANISOU 2402  SG  CYS A 333     8563  12601   6907  -1394   -856   1642       S  
-ATOM   2403  N   LYS A 334     -17.654 -18.023  -0.743  1.00 66.54           N  
-ANISOU 2403  N   LYS A 334     7250  12159   5872   -854   -787   2288       N  
-ATOM   2404  CA  LYS A 334     -18.648 -17.845   0.306  1.00 68.63           C  
-ANISOU 2404  CA  LYS A 334     7425  12547   6105   -643   -754   2432       C  
-ATOM   2405  C   LYS A 334     -18.160 -18.342   1.665  1.00 65.87           C  
-ANISOU 2405  C   LYS A 334     7158  12137   5733   -510   -789   2146       C  
-ATOM   2406  O   LYS A 334     -18.685 -17.943   2.704  1.00 67.53           O  
-ANISOU 2406  O   LYS A 334     7319  12380   5959   -286   -729   2168       O  
-ATOM   2407  CB  LYS A 334     -19.954 -18.539  -0.088  1.00 71.95           C  
-ANISOU 2407  CB  LYS A 334     7742  13261   6335   -774   -835   2818       C  
-ATOM   2408  CG  LYS A 334     -20.686 -17.851  -1.231  1.00 78.56           C  
-ANISOU 2408  CG  LYS A 334     8447  14206   7198   -866   -780   3179       C  
-ATOM   2409  CD  LYS A 334     -21.044 -16.424  -0.851  1.00 83.68           C  
-ANISOU 2409  CD  LYS A 334     8982  14765   8047   -589   -601   3283       C  
-ATOM   2410  CE  LYS A 334     -21.597 -15.657  -2.030  1.00 87.12           C  
-ANISOU 2410  CE  LYS A 334     9265  15283   8552   -680   -529   3633       C  
-ATOM   2411  NZ  LYS A 334     -20.587 -15.532  -3.123  1.00 91.43           N  
-ANISOU 2411  NZ  LYS A 334     9876  15702   9160   -875   -551   3473       N  
-ATOM   2412  N   THR A 335     -17.153 -19.209   1.652  1.00 67.49           N  
-ANISOU 2412  N   THR A 335     7481  12259   5903   -650   -874   1893       N  
-ATOM   2413  CA  THR A 335     -16.572 -19.725   2.883  1.00 62.44           C  
-ANISOU 2413  CA  THR A 335     6902  11572   5251   -554   -911   1632       C  
-ATOM   2414  C   THR A 335     -15.098 -19.379   2.958  1.00 62.28           C  
-ANISOU 2414  C   THR A 335     6993  11297   5374   -555   -879   1300       C  
-ATOM   2415  O   THR A 335     -14.384 -19.501   1.966  1.00 61.26           O  
-ANISOU 2415  O   THR A 335     6927  11062   5287   -721   -888   1247       O  
-ATOM   2416  CB  THR A 335     -16.673 -21.250   2.960  1.00 60.85           C  
-ANISOU 2416  CB  THR A 335     6722  11516   4884   -722  -1042   1652       C  
-ATOM   2417  OG1 THR A 335     -15.791 -21.835   1.992  1.00 57.08           O  
-ANISOU 2417  OG1 THR A 335     6347  10930   4409   -954  -1073   1542       O  
-ATOM   2418  CG2 THR A 335     -18.098 -21.713   2.707  1.00 59.63           C  
-ANISOU 2418  CG2 THR A 335     6463  11623   4569   -775  -1101   2008       C  
-ATOM   2419  N   PRO A 336     -14.634 -18.966   4.144  1.00 68.14           N  
-ANISOU 2419  N   PRO A 336     7761  11947   6182   -380   -843   1085       N  
-ATOM   2420  CA  PRO A 336     -13.223 -18.648   4.375  1.00 67.18           C  
-ANISOU 2420  CA  PRO A 336     7739  11599   6188   -384   -825    782       C  
-ATOM   2421  C   PRO A 336     -12.269 -19.651   3.720  1.00 64.92           C  
-ANISOU 2421  C   PRO A 336     7527  11254   5887   -600   -899    690       C  
-ATOM   2422  O   PRO A 336     -11.308 -19.222   3.089  1.00 64.47           O  
-ANISOU 2422  O   PRO A 336     7535  11010   5949   -660   -868    575       O  
-ATOM   2423  CB  PRO A 336     -13.106 -18.718   5.894  1.00 65.95           C  
-ANISOU 2423  CB  PRO A 336     7585  11473   6000   -239   -833    617       C  
-ATOM   2424  CG  PRO A 336     -14.448 -18.286   6.373  1.00 66.07           C  
-ANISOU 2424  CG  PRO A 336     7512  11638   5953    -68   -778    812       C  
-ATOM   2425  CD  PRO A 336     -15.436 -18.823   5.373  1.00 68.20           C  
-ANISOU 2425  CD  PRO A 336     7705  12078   6130   -181   -820   1127       C  
-ATOM   2426  N   GLN A 337     -12.522 -20.951   3.863  1.00 67.51           N  
-ANISOU 2426  N   GLN A 337     7843  11727   6079   -710   -982    745       N  
-ATOM   2427  CA  GLN A 337     -11.645 -21.960   3.267  1.00 67.22           C  
-ANISOU 2427  CA  GLN A 337     7885  11619   6036   -911  -1020    663       C  
-ATOM   2428  C   GLN A 337     -11.519 -21.738   1.767  1.00 67.43           C  
-ANISOU 2428  C   GLN A 337     7963  11570   6088  -1064   -990    750       C  
-ATOM   2429  O   GLN A 337     -10.433 -21.849   1.205  1.00 66.00           O  
-ANISOU 2429  O   GLN A 337     7868  11219   5990  -1163   -966    621       O  
-ATOM   2430  CB  GLN A 337     -12.153 -23.381   3.530  1.00 67.23           C  
-ANISOU 2430  CB  GLN A 337     7859  11798   5888  -1013  -1100    752       C  
-ATOM   2431  CG  GLN A 337     -12.970 -23.538   4.785  1.00 68.01           C  
-ANISOU 2431  CG  GLN A 337     7855  12079   5906   -856  -1143    806       C  
-ATOM   2432  CD  GLN A 337     -14.389 -23.067   4.607  1.00 69.38           C  
-ANISOU 2432  CD  GLN A 337     7945  12422   5993   -779  -1143   1063       C  
-ATOM   2433  OE1 GLN A 337     -14.772 -22.016   5.115  1.00 68.78           O  
-ANISOU 2433  OE1 GLN A 337     7825  12340   5967   -589  -1082   1078       O  
-ATOM   2434  NE2 GLN A 337     -15.183 -23.846   3.887  1.00 71.06           N  
-ANISOU 2434  NE2 GLN A 337     8138  12784   6076   -935  -1203   1280       N  
-ATOM   2435  N   GLY A 338     -12.644 -21.436   1.127  1.00 65.84           N  
-ANISOU 2435  N   GLY A 338     7697  11507   5811  -1089   -988    991       N  
-ATOM   2436  CA  GLY A 338     -12.664 -21.134  -0.293  1.00 64.25           C  
-ANISOU 2436  CA  GLY A 338     7518  11276   5619  -1241   -962   1108       C  
-ATOM   2437  C   GLY A 338     -11.864 -19.881  -0.588  1.00 63.50           C  
-ANISOU 2437  C   GLY A 338     7434  10975   5717  -1145   -884    994       C  
-ATOM   2438  O   GLY A 338     -10.948 -19.906  -1.407  1.00 62.60           O  
-ANISOU 2438  O   GLY A 338     7397  10719   5669  -1261   -867    903       O  
-ATOM   2439  N   GLN A 339     -12.201 -18.787   0.090  1.00 57.56           N  
-ANISOU 2439  N   GLN A 339     6611  10199   5061   -930   -829    998       N  
-ATOM   2440  CA  GLN A 339     -11.467 -17.536  -0.058  1.00 59.36           C  
-ANISOU 2440  CA  GLN A 339     6848  10219   5487   -824   -753    881       C  
-ATOM   2441  C   GLN A 339      -9.975 -17.757   0.143  1.00 55.99           C  
-ANISOU 2441  C   GLN A 339     6533   9590   5151   -859   -771    610       C  
-ATOM   2442  O   GLN A 339      -9.147 -17.195  -0.571  1.00 56.09           O  
-ANISOU 2442  O   GLN A 339     6580   9437   5293   -893   -741    547       O  
-ATOM   2443  CB  GLN A 339     -11.978 -16.504   0.940  1.00 64.75           C  
-ANISOU 2443  CB  GLN A 339     7471  10885   6247   -581   -679    872       C  
-ATOM   2444  CG  GLN A 339     -13.408 -16.071   0.688  1.00 76.27           C  
-ANISOU 2444  CG  GLN A 339     8801  12516   7662   -517   -627   1177       C  
-ATOM   2445  CD  GLN A 339     -13.960 -15.209   1.804  1.00 83.72           C  
-ANISOU 2445  CD  GLN A 339     9703  13441   8666   -265   -532   1164       C  
-ATOM   2446  OE1 GLN A 339     -13.309 -15.009   2.834  1.00 87.41           O  
-ANISOU 2446  OE1 GLN A 339    10248  13787   9178   -157   -519    908       O  
-ATOM   2447  NE2 GLN A 339     -15.172 -14.694   1.610  1.00 87.87           N  
-ANISOU 2447  NE2 GLN A 339    10106  14091   9188   -179   -455   1452       N  
-ATOM   2448  N   ARG A 340      -9.643 -18.594   1.115  1.00 63.87           N  
-ANISOU 2448  N   ARG A 340     7571  10612   6083   -853   -820    478       N  
-ATOM   2449  CA  ARG A 340      -8.260 -18.884   1.451  1.00 59.92           C  
-ANISOU 2449  CA  ARG A 340     7156   9946   5665   -887   -836    258       C  
-ATOM   2450  C   ARG A 340      -7.589 -19.666   0.324  1.00 57.84           C  
-ANISOU 2450  C   ARG A 340     6965   9618   5394  -1086   -842    272       C  
-ATOM   2451  O   ARG A 340      -6.388 -19.534   0.090  1.00 56.17           O  
-ANISOU 2451  O   ARG A 340     6818   9224   5301  -1116   -824    146       O  
-ATOM   2452  CB  ARG A 340      -8.213 -19.689   2.756  1.00 60.44           C  
-ANISOU 2452  CB  ARG A 340     7215  10101   5650   -847   -885    163       C  
-ATOM   2453  CG  ARG A 340      -6.893 -19.610   3.503  1.00 60.92           C  
-ANISOU 2453  CG  ARG A 340     7324  10009   5812   -825   -892    -51       C  
-ATOM   2454  CD  ARG A 340      -6.953 -20.370   4.820  1.00 61.06           C  
-ANISOU 2454  CD  ARG A 340     7303  10155   5743   -790   -941   -114       C  
-ATOM   2455  NE  ARG A 340      -8.080 -19.953   5.654  1.00 60.99           N  
-ANISOU 2455  NE  ARG A 340     7227  10297   5649   -641   -940    -67       N  
-ATOM   2456  CZ  ARG A 340      -9.000 -20.782   6.144  1.00 60.17           C  
-ANISOU 2456  CZ  ARG A 340     7053  10404   5405   -628   -984     40       C  
-ATOM   2457  NH1 ARG A 340      -8.932 -22.084   5.893  1.00 59.62           N  
-ANISOU 2457  NH1 ARG A 340     6972  10414   5267   -766  -1033    101       N  
-ATOM   2458  NH2 ARG A 340      -9.991 -20.310   6.888  1.00 59.29           N  
-ANISOU 2458  NH2 ARG A 340     6884  10418   5227   -474   -969     93       N  
-ATOM   2459  N   LEU A 341      -8.377 -20.478  -0.374  1.00 49.96           N  
-ANISOU 2459  N   LEU A 341     5962   8769   4251  -1226   -862    432       N  
-ATOM   2460  CA  LEU A 341      -7.847 -21.391  -1.381  1.00 47.56           C  
-ANISOU 2460  CA  LEU A 341     5749   8416   3904  -1434   -853    437       C  
-ATOM   2461  C   LEU A 341      -7.618 -20.693  -2.719  1.00 50.26           C  
-ANISOU 2461  C   LEU A 341     6111   8675   4310  -1511   -811    501       C  
-ATOM   2462  O   LEU A 341      -6.615 -20.935  -3.392  1.00 50.44           O  
-ANISOU 2462  O   LEU A 341     6222   8548   4394  -1607   -776    422       O  
-ATOM   2463  CB  LEU A 341      -8.779 -22.591  -1.558  1.00 40.54           C  
-ANISOU 2463  CB  LEU A 341     4866   7720   2818  -1580   -894    570       C  
-ATOM   2464  CG  LEU A 341      -8.275 -23.678  -2.505  1.00 37.19           C  
-ANISOU 2464  CG  LEU A 341     4564   7236   2329  -1810   -865    555       C  
-ATOM   2465  CD1 LEU A 341      -6.908 -24.183  -2.076  1.00 32.50           C  
-ANISOU 2465  CD1 LEU A 341     4043   6450   1854  -1796   -820    367       C  
-ATOM   2466  CD2 LEU A 341      -9.269 -24.824  -2.609  1.00 33.61           C  
-ANISOU 2466  CD2 LEU A 341     4122   6974   1676  -1961   -910    684       C  
-ATOM   2467  N   VAL A 342      -8.553 -19.834  -3.107  1.00 56.58           N  
-ANISOU 2467  N   VAL A 342     6817   9580   5102  -1467   -806    665       N  
-ATOM   2468  CA  VAL A 342      -8.380 -19.025  -4.302  1.00 58.29           C  
-ANISOU 2468  CA  VAL A 342     7012   9737   5399  -1521   -767    746       C  
-ATOM   2469  C   VAL A 342      -7.046 -18.288  -4.236  1.00 59.83           C  
-ANISOU 2469  C   VAL A 342     7245   9685   5801  -1423   -733    565       C  
-ATOM   2470  O   VAL A 342      -6.227 -18.404  -5.142  1.00 60.00           O  
-ANISOU 2470  O   VAL A 342     7332   9595   5870  -1530   -710    532       O  
-ATOM   2471  CB  VAL A 342      -9.531 -18.015  -4.474  1.00 59.33           C  
-ANISOU 2471  CB  VAL A 342     6997  10002   5544  -1434   -749    960       C  
-ATOM   2472  CG1 VAL A 342      -9.189 -16.992  -5.549  1.00 57.73           C  
-ANISOU 2472  CG1 VAL A 342     6741   9714   5480  -1449   -701   1027       C  
-ATOM   2473  CG2 VAL A 342     -10.833 -18.744  -4.799  1.00 57.44           C  
-ANISOU 2473  CG2 VAL A 342     6712  10023   5090  -1575   -791   1196       C  
-ATOM   2474  N   ASN A 343      -6.823 -17.545  -3.155  1.00 55.59           N  
-ANISOU 2474  N   ASN A 343     6676   9065   5382  -1227   -729    452       N  
-ATOM   2475  CA  ASN A 343      -5.564 -16.835  -2.975  1.00 57.52           C  
-ANISOU 2475  CA  ASN A 343     6959   9081   5816  -1142   -712    285       C  
-ATOM   2476  C   ASN A 343      -4.374 -17.772  -3.075  1.00 56.51           C  
-ANISOU 2476  C   ASN A 343     6942   8838   5693  -1250   -723    166       C  
-ATOM   2477  O   ASN A 343      -3.286 -17.365  -3.477  1.00 56.76           O  
-ANISOU 2477  O   ASN A 343     7011   8691   5865  -1249   -707     97       O  
-ATOM   2478  CB  ASN A 343      -5.528 -16.114  -1.628  1.00 59.76           C  
-ANISOU 2478  CB  ASN A 343     7220   9309   6176   -952   -712    160       C  
-ATOM   2479  CG  ASN A 343      -6.535 -14.988  -1.539  1.00 64.02           C  
-ANISOU 2479  CG  ASN A 343     7659   9902   6765   -814   -662    268       C  
-ATOM   2480  OD1 ASN A 343      -6.973 -14.448  -2.552  1.00 65.13           O  
-ANISOU 2480  OD1 ASN A 343     7727  10071   6949   -842   -625    429       O  
-ATOM   2481  ND2 ASN A 343      -6.903 -14.624  -0.319  1.00 66.81           N  
-ANISOU 2481  ND2 ASN A 343     8001  10270   7113   -666   -647    189       N  
-ATOM   2482  N   GLN A 344      -4.581 -19.025  -2.692  1.00 66.52           N  
-ANISOU 2482  N   GLN A 344     8253  10204   6819  -1337   -742    159       N  
-ATOM   2483  CA  GLN A 344      -3.519 -20.014  -2.753  1.00 64.37           C  
-ANISOU 2483  CA  GLN A 344     8076   9822   6558  -1437   -724     72       C  
-ATOM   2484  C   GLN A 344      -3.291 -20.453  -4.199  1.00 62.51           C  
-ANISOU 2484  C   GLN A 344     7915   9548   6288  -1609   -674    145       C  
-ATOM   2485  O   GLN A 344      -2.177 -20.788  -4.593  1.00 60.98           O  
-ANISOU 2485  O   GLN A 344     7802   9194   6173  -1663   -627     85       O  
-ATOM   2486  CB  GLN A 344      -3.869 -21.216  -1.882  1.00 66.48           C  
-ANISOU 2486  CB  GLN A 344     8350  10208   6700  -1473   -747     55       C  
-ATOM   2487  CG  GLN A 344      -2.735 -22.202  -1.718  1.00 69.43           C  
-ANISOU 2487  CG  GLN A 344     8799  10462   7121  -1547   -708    -25       C  
-ATOM   2488  CD  GLN A 344      -3.173 -23.483  -1.027  1.00 73.21           C  
-ANISOU 2488  CD  GLN A 344     9269  11069   7480  -1603   -720    -12       C  
-ATOM   2489  OE1 GLN A 344      -3.279 -23.543   0.204  1.00 75.73           O  
-ANISOU 2489  OE1 GLN A 344     9515  11462   7797  -1505   -767    -58       O  
-ATOM   2490  NE2 GLN A 344      -3.441 -24.518  -1.822  1.00 74.62           N  
-ANISOU 2490  NE2 GLN A 344     9522  11276   7554  -1769   -674     51       N  
-ATOM   2491  N   TRP A 345      -4.356 -20.439  -4.990  1.00 55.58           N  
-ANISOU 2491  N   TRP A 345     7009   8825   5285  -1702   -679    288       N  
-ATOM   2492  CA  TRP A 345      -4.280 -20.858  -6.383  1.00 54.54           C  
-ANISOU 2492  CA  TRP A 345     6952   8692   5080  -1895   -635    362       C  
-ATOM   2493  C   TRP A 345      -3.650 -19.792  -7.264  1.00 51.65           C  
-ANISOU 2493  C   TRP A 345     6559   8205   4862  -1863   -609    379       C  
-ATOM   2494  O   TRP A 345      -2.937 -20.108  -8.219  1.00 52.33           O  
-ANISOU 2494  O   TRP A 345     6733   8194   4957  -1980   -555    368       O  
-ATOM   2495  CB  TRP A 345      -5.670 -21.204  -6.914  1.00 57.82           C  
-ANISOU 2495  CB  TRP A 345     7335   9342   5291  -2035   -664    535       C  
-ATOM   2496  CG  TRP A 345      -6.109 -22.579  -6.554  1.00 61.58           C  
-ANISOU 2496  CG  TRP A 345     7886   9916   5597  -2157   -674    532       C  
-ATOM   2497  CD1 TRP A 345      -5.404 -23.505  -5.839  1.00 61.38           C  
-ANISOU 2497  CD1 TRP A 345     7936   9788   5597  -2145   -648    398       C  
-ATOM   2498  CD2 TRP A 345      -7.352 -23.197  -6.896  1.00 64.17           C  
-ANISOU 2498  CD2 TRP A 345     8208  10465   5710  -2316   -715    687       C  
-ATOM   2499  NE1 TRP A 345      -6.138 -24.659  -5.708  1.00 62.59           N  
-ANISOU 2499  NE1 TRP A 345     8130  10075   5575  -2278   -664    448       N  
-ATOM   2500  CE2 TRP A 345      -7.339 -24.496  -6.351  1.00 64.24           C  
-ANISOU 2500  CE2 TRP A 345     8298  10483   5626  -2389   -713    622       C  
-ATOM   2501  CE3 TRP A 345      -8.480 -22.775  -7.606  1.00 66.60           C  
-ANISOU 2501  CE3 TRP A 345     8435  10972   5898  -2411   -754    899       C  
-ATOM   2502  CZ2 TRP A 345      -8.409 -25.378  -6.497  1.00 65.15           C  
-ANISOU 2502  CZ2 TRP A 345     8433  10791   5531  -2555   -757    745       C  
-ATOM   2503  CZ3 TRP A 345      -9.538 -23.649  -7.750  1.00 68.05           C  
-ANISOU 2503  CZ3 TRP A 345     8636  11358   5862  -2585   -802   1036       C  
-ATOM   2504  CH2 TRP A 345      -9.496 -24.936  -7.201  1.00 66.71           C  
-ANISOU 2504  CH2 TRP A 345     8564  11183   5599  -2656   -807    951       C  
-ATOM   2505  N   ILE A 346      -3.923 -18.530  -6.952  1.00 42.00           N  
-ANISOU 2505  N   ILE A 346     5214   6985   3759  -1703   -637    410       N  
-ATOM   2506  CA  ILE A 346      -3.379 -17.429  -7.735  1.00 39.78           C  
-ANISOU 2506  CA  ILE A 346     4880   6594   3641  -1656   -617    439       C  
-ATOM   2507  C   ILE A 346      -1.860 -17.349  -7.589  1.00 39.42           C  
-ANISOU 2507  C   ILE A 346     4909   6309   3760  -1597   -600    294       C  
-ATOM   2508  O   ILE A 346      -1.143 -17.152  -8.569  1.00 39.12           O  
-ANISOU 2508  O   ILE A 346     4896   6172   3795  -1651   -569    316       O  
-ATOM   2509  CB  ILE A 346      -4.021 -16.087  -7.353  1.00 38.02           C  
-ANISOU 2509  CB  ILE A 346     4509   6406   3532  -1486   -631    504       C  
-ATOM   2510  CG1 ILE A 346      -5.484 -16.061  -7.787  1.00 37.28           C  
-ANISOU 2510  CG1 ILE A 346     4315   6553   3297  -1558   -633    717       C  
-ATOM   2511  CG2 ILE A 346      -3.274 -14.949  -7.995  1.00 37.06           C  
-ANISOU 2511  CG2 ILE A 346     4330   6134   3619  -1416   -613    509       C  
-ATOM   2512  CD1 ILE A 346      -6.151 -14.725  -7.602  1.00 36.60           C  
-ANISOU 2512  CD1 ILE A 346     4070   6496   3342  -1397   -610    828       C  
-ATOM   2513  N   LYS A 347      -1.373 -17.519  -6.366  1.00 50.01           N  
-ANISOU 2513  N   LYS A 347     6278   7570   5152  -1494   -623    164       N  
-ATOM   2514  CA  LYS A 347       0.058 -17.522  -6.122  1.00 48.91           C  
-ANISOU 2514  CA  LYS A 347     6200   7225   5160  -1453   -613     59       C  
-ATOM   2515  C   LYS A 347       0.685 -18.778  -6.701  1.00 48.50           C  
-ANISOU 2515  C   LYS A 347     6267   7121   5040  -1601   -548     60       C  
-ATOM   2516  O   LYS A 347       1.891 -18.819  -6.950  1.00 47.53           O  
-ANISOU 2516  O   LYS A 347     6196   6824   5038  -1596   -512     32       O  
-ATOM   2517  CB  LYS A 347       0.348 -17.441  -4.626  1.00 50.59           C  
-ANISOU 2517  CB  LYS A 347     6401   7401   5418  -1337   -657    -58       C  
-ATOM   2518  CG  LYS A 347      -0.250 -16.226  -3.952  1.00 53.94           C  
-ANISOU 2518  CG  LYS A 347     6737   7854   5904  -1188   -697    -85       C  
-ATOM   2519  CD  LYS A 347       0.434 -15.935  -2.632  1.00 54.80           C  
-ANISOU 2519  CD  LYS A 347     6858   7873   6091  -1092   -737   -223       C  
-ATOM   2520  CE  LYS A 347       0.256 -17.083  -1.665  1.00 54.81           C  
-ANISOU 2520  CE  LYS A 347     6884   7984   5956  -1132   -751   -267       C  
-ATOM   2521  NZ  LYS A 347      -1.167 -17.216  -1.252  1.00 55.78           N  
-ANISOU 2521  NZ  LYS A 347     6956   8304   5932  -1098   -758   -227       N  
-ATOM   2522  N   GLN A 348      -0.134 -19.803  -6.923  1.00 44.97           N  
-ANISOU 2522  N   GLN A 348     5867   6816   4402  -1735   -522    103       N  
-ATOM   2523  CA  GLN A 348       0.383 -21.094  -7.388  1.00 46.66           C  
-ANISOU 2523  CA  GLN A 348     6214   6969   4545  -1882   -435     90       C  
-ATOM   2524  C   GLN A 348      -0.301 -21.662  -8.649  1.00 47.61           C  
-ANISOU 2524  C   GLN A 348     6408   7193   4489  -2083   -385    173       C  
-ATOM   2525  O   GLN A 348      -1.077 -22.615  -8.572  1.00 47.32           O  
-ANISOU 2525  O   GLN A 348     6420   7281   4277  -2205   -376    192       O  
-ATOM   2526  CB  GLN A 348       0.370 -22.109  -6.236  1.00 45.71           C  
-ANISOU 2526  CB  GLN A 348     6115   6878   4376  -1875   -433     29       C  
-ATOM   2527  CG  GLN A 348       1.103 -21.614  -4.991  1.00 46.97           C  
-ANISOU 2527  CG  GLN A 348     6206   6954   4687  -1713   -483    -47       C  
-ATOM   2528  CD  GLN A 348       0.910 -22.514  -3.778  1.00 48.23           C  
-ANISOU 2528  CD  GLN A 348     6344   7194   4786  -1703   -498    -87       C  
-ATOM   2529  OE1 GLN A 348      -0.038 -23.300  -3.716  1.00 49.21           O  
-ANISOU 2529  OE1 GLN A 348     6476   7467   4754  -1780   -499    -56       O  
-ATOM   2530  NE2 GLN A 348       1.815 -22.404  -2.807  1.00 46.45           N  
-ANISOU 2530  NE2 GLN A 348     6082   6884   4683  -1618   -516   -140       N  
-ATOM   2531  N   PRO A 349      -0.005 -21.069  -9.817  1.00 52.63           N  
-ANISOU 2531  N   PRO A 349     7049   7784   5165  -2130   -357    228       N  
-ATOM   2532  CA  PRO A 349      -0.493 -21.549 -11.116  1.00 55.25           C  
-ANISOU 2532  CA  PRO A 349     7460   8209   5325  -2347   -304    304       C  
-ATOM   2533  C   PRO A 349       0.102 -22.907 -11.490  1.00 57.13           C  
-ANISOU 2533  C   PRO A 349     7890   8334   5481  -2498   -176    240       C  
-ATOM   2534  O   PRO A 349       1.310 -23.114 -11.363  1.00 56.55           O  
-ANISOU 2534  O   PRO A 349     7880   8054   5552  -2428    -98    176       O  
-ATOM   2535  CB  PRO A 349       0.009 -20.483 -12.092  1.00 54.97           C  
-ANISOU 2535  CB  PRO A 349     7364   8112   5410  -2315   -301    362       C  
-ATOM   2536  CG  PRO A 349       0.244 -19.279 -11.262  1.00 55.35           C  
-ANISOU 2536  CG  PRO A 349     7265   8102   5662  -2083   -382    346       C  
-ATOM   2537  CD  PRO A 349       0.711 -19.791  -9.939  1.00 53.64           C  
-ANISOU 2537  CD  PRO A 349     7086   7793   5500  -1980   -389    230       C  
-ATOM   2538  N   LEU A 350      -0.748 -23.810 -11.968  1.00 49.30           N  
-ANISOU 2538  N   LEU A 350     6991   7476   4263  -2710   -148    271       N  
-ATOM   2539  CA  LEU A 350      -0.350 -25.183 -12.263  1.00 52.63           C  
-ANISOU 2539  CA  LEU A 350     7611   7794   4593  -2868     -9    203       C  
-ATOM   2540  C   LEU A 350       0.614 -25.312 -13.439  1.00 55.68           C  
-ANISOU 2540  C   LEU A 350     8136   8012   5009  -2957    131    181       C  
-ATOM   2541  O   LEU A 350       0.737 -24.409 -14.261  1.00 57.25           O  
-ANISOU 2541  O   LEU A 350     8278   8233   5240  -2954    104    240       O  
-ATOM   2542  CB  LEU A 350      -1.592 -26.037 -12.517  1.00 53.44           C  
-ANISOU 2542  CB  LEU A 350     7782   8092   4431  -3094    -27    246       C  
-ATOM   2543  CG  LEU A 350      -2.370 -26.412 -11.255  1.00 52.09           C  
-ANISOU 2543  CG  LEU A 350     7525   8043   4223  -3019   -120    251       C  
-ATOM   2544  CD1 LEU A 350      -3.709 -27.032 -11.611  1.00 52.99           C  
-ANISOU 2544  CD1 LEU A 350     7677   8383   4073  -3243   -171    340       C  
-ATOM   2545  CD2 LEU A 350      -1.538 -27.355 -10.397  1.00 50.57           C  
-ANISOU 2545  CD2 LEU A 350     7401   7674   4139  -2947    -27    145       C  
-ATOM   2546  N   MET A 351       1.292 -26.453 -13.509  1.00 58.41           N  
-ANISOU 2546  N   MET A 351     8656   8187   5350  -3032    293    107       N  
-ATOM   2547  CA  MET A 351       2.208 -26.741 -14.607  1.00 64.52           C  
-ANISOU 2547  CA  MET A 351     9592   8784   6139  -3121    462     84       C  
-ATOM   2548  C   MET A 351       1.830 -28.039 -15.327  1.00 70.54           C  
-ANISOU 2548  C   MET A 351    10586   9542   6675  -3395    611     35       C  
-ATOM   2549  O   MET A 351       2.031 -28.173 -16.531  1.00 71.51           O  
-ANISOU 2549  O   MET A 351    10851   9627   6694  -3558    719     29       O  
-ATOM   2550  CB  MET A 351       3.653 -26.811 -14.103  1.00 60.99           C  
-ANISOU 2550  CB  MET A 351     9153   8075   5946  -2931    567     57       C  
-ATOM   2551  CG  MET A 351       4.191 -25.504 -13.548  1.00 56.33           C  
-ANISOU 2551  CG  MET A 351     8366   7460   5575  -2691    432    100       C  
-ATOM   2552  SD  MET A 351       4.359 -24.217 -14.797  1.00 52.75           S  
-ANISOU 2552  SD  MET A 351     7848   7040   5155  -2684    379    173       S  
-ATOM   2553  CE  MET A 351       5.537 -24.982 -15.912  1.00 54.01           C  
-ANISOU 2553  CE  MET A 351     8225   6965   5332  -2774    622    163       C  
-ATOM   2554  N   ASP A 352       1.283 -28.993 -14.583  1.00 77.14           N  
-ANISOU 2554  N   ASP A 352    11462  10417   7431  -3453    618     -1       N  
-ATOM   2555  CA  ASP A 352       0.837 -30.252 -15.165  1.00 84.94           C  
-ANISOU 2555  CA  ASP A 352    12673  11399   8201  -3724    751    -54       C  
-ATOM   2556  C   ASP A 352      -0.373 -30.020 -16.066  1.00 88.27           C  
-ANISOU 2556  C   ASP A 352    13116  12077   8345  -3971    645      7       C  
-ATOM   2557  O   ASP A 352      -1.346 -29.384 -15.662  1.00 87.87           O  
-ANISOU 2557  O   ASP A 352    12887  12262   8238  -3938    448     99       O  
-ATOM   2558  CB  ASP A 352       0.502 -31.259 -14.059  1.00 90.61           C  
-ANISOU 2558  CB  ASP A 352    13391  12112   8923  -3708    761    -88       C  
-ATOM   2559  CG  ASP A 352      -0.165 -32.515 -14.591  1.00 96.72           C  
-ANISOU 2559  CG  ASP A 352    14383  12910   9458  -4004    867   -136       C  
-ATOM   2560  OD1 ASP A 352       0.554 -33.465 -14.969  1.00 99.26           O  
-ANISOU 2560  OD1 ASP A 352    14910  12999   9804  -4089   1104   -216       O  
-ATOM   2561  OD2 ASP A 352      -1.412 -32.548 -14.632  1.00101.69           O  
-ANISOU 2561  OD2 ASP A 352    14979  13783   9877  -4155    719    -83       O  
-ATOM   2562  N   LYS A 353      -0.308 -30.538 -17.287  1.00 77.72           N  
-ANISOU 2562  N   LYS A 353    11997  10700   6832  -4226    785    -32       N  
-ATOM   2563  CA  LYS A 353      -1.390 -30.348 -18.246  1.00 81.59           C  
-ANISOU 2563  CA  LYS A 353    12513  11447   7040  -4503    692     44       C  
-ATOM   2564  C   LYS A 353      -2.713 -30.900 -17.730  1.00 85.09           C  
-ANISOU 2564  C   LYS A 353    12931  12110   7290  -4649    564     97       C  
-ATOM   2565  O   LYS A 353      -3.757 -30.259 -17.855  1.00 85.50           O  
-ANISOU 2565  O   LYS A 353    12833  12439   7215  -4719    381    240       O  
-ATOM   2566  CB  LYS A 353      -1.036 -30.994 -19.587  1.00 81.42           C  
-ANISOU 2566  CB  LYS A 353    12770  11327   6840  -4782    890    -33       C  
-ATOM   2567  CG  LYS A 353      -2.176 -31.002 -20.588  1.00 79.60           C  
-ANISOU 2567  CG  LYS A 353    12596  11375   6273  -5135    805     46       C  
-ATOM   2568  CD  LYS A 353      -1.739 -31.602 -21.911  1.00 79.40           C  
-ANISOU 2568  CD  LYS A 353    12861  11244   6065  -5415   1013    -50       C  
-ATOM   2569  CE  LYS A 353      -2.937 -32.050 -22.734  1.00 80.60           C  
-ANISOU 2569  CE  LYS A 353    13135  11657   5833  -5838    951      1       C  
-ATOM   2570  NZ  LYS A 353      -3.893 -30.939 -23.000  1.00 82.65           N  
-ANISOU 2570  NZ  LYS A 353    13130  12271   6002  -5886    705    216       N  
-ATOM   2571  N   ASN A 354      -2.657 -32.090 -17.145  1.00 90.11           N  
-ANISOU 2571  N   ASN A 354    13701  12621   7917  -4688    665      4       N  
-ATOM   2572  CA  ASN A 354      -3.853 -32.756 -16.641  1.00 93.51           C  
-ANISOU 2572  CA  ASN A 354    14122  13239   8168  -4830    554     54       C  
-ATOM   2573  C   ASN A 354      -4.604 -31.958 -15.581  1.00 90.78           C  
-ANISOU 2573  C   ASN A 354    13485  13106   7902  -4615    320    184       C  
-ATOM   2574  O   ASN A 354      -5.783 -31.652 -15.747  1.00 90.47           O  
-ANISOU 2574  O   ASN A 354    13353  13342   7679  -4744    158    328       O  
-ATOM   2575  CB  ASN A 354      -3.505 -34.142 -16.096  1.00 97.83           C  
-ANISOU 2575  CB  ASN A 354    14837  13582   8752  -4863    719    -69       C  
-ATOM   2576  CG  ASN A 354      -3.290 -35.159 -17.192  1.00103.03           C  
-ANISOU 2576  CG  ASN A 354    15824  14096   9226  -5179    939   -180       C  
-ATOM   2577  OD1 ASN A 354      -3.382 -34.840 -18.377  1.00108.32           O  
-ANISOU 2577  OD1 ASN A 354    16604  14831   9723  -5386    963   -172       O  
-ATOM   2578  ND2 ASN A 354      -2.996 -36.392 -16.804  1.00105.53           N  
-ANISOU 2578  ND2 ASN A 354    16298  14215   9582  -5222   1113   -283       N  
-ATOM   2579  N   ARG A 355      -3.920 -31.633 -14.488  1.00107.83           N  
-ANISOU 2579  N   ARG A 355    15502  15138  10329  -4296    312    144       N  
-ATOM   2580  CA  ARG A 355      -4.556 -30.939 -13.374  1.00102.83           C  
-ANISOU 2580  CA  ARG A 355    14616  14677   9779  -4078    119    239       C  
-ATOM   2581  C   ARG A 355      -5.278 -29.682 -13.839  1.00 98.57           C  
-ANISOU 2581  C   ARG A 355    13913  14362   9178  -4073    -35    390       C  
-ATOM   2582  O   ARG A 355      -6.353 -29.359 -13.338  1.00 97.76           O  
-ANISOU 2582  O   ARG A 355    13657  14487   9002  -4046   -190    522       O  
-ATOM   2583  CB  ARG A 355      -3.537 -30.590 -12.289  1.00105.66           C  
-ANISOU 2583  CB  ARG A 355    14857  14856  10432  -3755    143    167       C  
-ATOM   2584  CG  ARG A 355      -2.919 -31.792 -11.596  1.00111.76           C  
-ANISOU 2584  CG  ARG A 355    15723  15444  11296  -3727    279     66       C  
-ATOM   2585  CD  ARG A 355      -2.029 -31.344 -10.449  1.00117.39           C  
-ANISOU 2585  CD  ARG A 355    16280  16039  12282  -3425    268     36       C  
-ATOM   2586  NE  ARG A 355      -2.791 -30.631  -9.426  1.00122.95           N  
-ANISOU 2586  NE  ARG A 355    16765  16946  13003  -3259     68    103       N  
-ATOM   2587  CZ  ARG A 355      -2.248 -29.900  -8.458  1.00125.25           C  
-ANISOU 2587  CZ  ARG A 355    16899  17200  13492  -3008      8     88       C  
-ATOM   2588  NH1 ARG A 355      -0.929 -29.771  -8.381  1.00125.65           N  
-ANISOU 2588  NH1 ARG A 355    16970  17028  13743  -2897    114     30       N  
-ATOM   2589  NH2 ARG A 355      -3.025 -29.291  -7.571  1.00127.44           N  
-ANISOU 2589  NH2 ARG A 355    17002  17662  13758  -2875   -155    140       N  
-ATOM   2590  N   ILE A 356      -4.679 -28.976 -14.795  1.00 70.19           N  
-ANISOU 2590  N   ILE A 356    10339  10702   5627  -4093     19    389       N  
-ATOM   2591  CA  ILE A 356      -5.308 -27.797 -15.378  1.00 65.76           C  
-ANISOU 2591  CA  ILE A 356     9615  10349   5022  -4108   -102    550       C  
-ATOM   2592  C   ILE A 356      -6.593 -28.203 -16.079  1.00 67.41           C  
-ANISOU 2592  C   ILE A 356     9864  10826   4922  -4429   -173    694       C  
-ATOM   2593  O   ILE A 356      -7.641 -27.592 -15.878  1.00 67.21           O  
-ANISOU 2593  O   ILE A 356     9654  11046   4837  -4417   -320    881       O  
-ATOM   2594  CB  ILE A 356      -4.392 -27.110 -16.397  1.00 60.25           C  
-ANISOU 2594  CB  ILE A 356     8946   9534   4414  -4105    -19    525       C  
-ATOM   2595  CG1 ILE A 356      -3.026 -26.828 -15.777  1.00 55.88           C  
-ANISOU 2595  CG1 ILE A 356     8377   8699   4155  -3818     60    395       C  
-ATOM   2596  CG2 ILE A 356      -5.023 -25.820 -16.889  1.00 58.03           C  
-ANISOU 2596  CG2 ILE A 356     8450   9467   4132  -4088   -143    710       C  
-ATOM   2597  CD1 ILE A 356      -1.976 -26.395 -16.787  1.00 51.74           C  
-ANISOU 2597  CD1 ILE A 356     7918   8021   3719  -3821    168    360       C  
-ATOM   2598  N   GLU A 357      -6.498 -29.235 -16.912  1.00 83.85           N  
-ANISOU 2598  N   GLU A 357    12195  12859   6807  -4726    -60    617       N  
-ATOM   2599  CA  GLU A 357      -7.669 -29.797 -17.558  1.00 85.76           C  
-ANISOU 2599  CA  GLU A 357    12514  13345   6727  -5079   -124    741       C  
-ATOM   2600  C   GLU A 357      -8.692 -30.133 -16.488  1.00 84.28           C  
-ANISOU 2600  C   GLU A 357    12213  13316   6493  -5022   -262    841       C  
-ATOM   2601  O   GLU A 357      -9.818 -29.643 -16.520  1.00 84.44           O  
-ANISOU 2601  O   GLU A 357    12071  13617   6395  -5087   -414   1065       O  
-ATOM   2602  CB  GLU A 357      -7.299 -31.048 -18.352  1.00 91.36           C  
-ANISOU 2602  CB  GLU A 357    13549  13912   7250  -5384     47    586       C  
-ATOM   2603  CG  GLU A 357      -6.351 -30.792 -19.509  1.00 98.88           C  
-ANISOU 2603  CG  GLU A 357    14635  14722   8211  -5470    197    497       C  
-ATOM   2604  CD  GLU A 357      -6.977 -29.957 -20.614  1.00104.95           C  
-ANISOU 2604  CD  GLU A 357    15307  15763   8808  -5676    100    682       C  
-ATOM   2605  OE1 GLU A 357      -6.246 -29.569 -21.551  1.00109.79           O  
-ANISOU 2605  OE1 GLU A 357    15980  16296   9440  -5721    198    637       O  
-ATOM   2606  OE2 GLU A 357      -8.195 -29.687 -20.552  1.00109.14           O  
-ANISOU 2606  OE2 GLU A 357    15687  16593   9188  -5792    -72    891       O  
-ATOM   2607  N   GLU A 358      -8.285 -30.961 -15.532  1.00 83.12           N  
-ANISOU 2607  N   GLU A 358    12137  12994   6452  -4892   -201    696       N  
-ATOM   2608  CA  GLU A 358      -9.149 -31.331 -14.420  1.00 81.72           C  
-ANISOU 2608  CA  GLU A 358    11845  12950   6254  -4808   -325    777       C  
-ATOM   2609  C   GLU A 358      -9.806 -30.098 -13.806  1.00 79.57           C  
-ANISOU 2609  C   GLU A 358    11282  12873   6077  -4574   -489    960       C  
-ATOM   2610  O   GLU A 358     -11.031 -30.013 -13.717  1.00 79.37           O  
-ANISOU 2610  O   GLU A 358    11147  13113   5896  -4665   -626   1168       O  
-ATOM   2611  CB  GLU A 358      -8.357 -32.094 -13.356  1.00 80.28           C  
-ANISOU 2611  CB  GLU A 358    11711  12532   6260  -4612   -231    598       C  
-ATOM   2612  CG  GLU A 358      -9.163 -32.435 -12.114  1.00 79.84           C  
-ANISOU 2612  CG  GLU A 358    11513  12614   6207  -4489   -360    677       C  
-ATOM   2613  CD  GLU A 358      -8.398 -33.301 -11.128  1.00 79.13           C  
-ANISOU 2613  CD  GLU A 358    11463  12313   6289  -4337   -260    518       C  
-ATOM   2614  OE1 GLU A 358      -7.602 -32.752 -10.334  1.00 78.60           O  
-ANISOU 2614  OE1 GLU A 358    11275  12123   6466  -4045   -241    448       O  
-ATOM   2615  OE2 GLU A 358      -8.601 -34.534 -11.141  1.00 78.94           O  
-ANISOU 2615  OE2 GLU A 358    11585  12251   6156  -4520   -199    475       O  
-ATOM   2616  N   ARG A 359      -8.982 -29.141 -13.395  1.00 85.20           N  
-ANISOU 2616  N   ARG A 359    11875  13448   7050  -4276   -464    891       N  
-ATOM   2617  CA  ARG A 359      -9.475 -27.914 -12.785  1.00 83.23           C  
-ANISOU 2617  CA  ARG A 359    11368  13333   6922  -4032   -583   1032       C  
-ATOM   2618  C   ARG A 359     -10.438 -27.194 -13.727  1.00 85.66           C  
-ANISOU 2618  C   ARG A 359    11569  13898   7078  -4203   -664   1279       C  
-ATOM   2619  O   ARG A 359     -11.444 -26.635 -13.291  1.00 85.20           O  
-ANISOU 2619  O   ARG A 359    11322  14051   7001  -4122   -776   1484       O  
-ATOM   2620  CB  ARG A 359      -8.306 -27.001 -12.398  1.00 79.93           C  
-ANISOU 2620  CB  ARG A 359    10878  12697   6796  -3736   -526    900       C  
-ATOM   2621  CG  ARG A 359      -8.593 -26.076 -11.223  1.00 75.17           C  
-ANISOU 2621  CG  ARG A 359    10058  12144   6361  -3424   -617    951       C  
-ATOM   2622  CD  ARG A 359      -7.575 -26.272 -10.104  1.00 70.83           C  
-ANISOU 2622  CD  ARG A 359     9524  11374   6016  -3188   -569    752       C  
-ATOM   2623  NE  ARG A 359      -6.622 -25.168 -10.017  1.00 67.16           N  
-ANISOU 2623  NE  ARG A 359     8987  10746   5785  -2977   -540    677       N  
-ATOM   2624  CZ  ARG A 359      -5.606 -25.118  -9.160  1.00 64.69           C  
-ANISOU 2624  CZ  ARG A 359     8674  10240   5664  -2782   -503    524       C  
-ATOM   2625  NH1 ARG A 359      -5.400 -26.116  -8.313  1.00 63.17           N  
-ANISOU 2625  NH1 ARG A 359     8535   9998   5468  -2764   -482    437       N  
-ATOM   2626  NH2 ARG A 359      -4.790 -24.071  -9.155  1.00 64.85           N  
-ANISOU 2626  NH2 ARG A 359     8632  10124   5883  -2615   -491    475       N  
-ATOM   2627  N   LEU A 360     -10.128 -27.219 -15.021  1.00 76.70           N  
-ANISOU 2627  N   LEU A 360    10551  12755   5837  -4443   -598   1276       N  
-ATOM   2628  CA  LEU A 360     -10.962 -26.561 -16.024  1.00 79.31           C  
-ANISOU 2628  CA  LEU A 360    10772  13345   6018  -4642   -668   1526       C  
-ATOM   2629  C   LEU A 360     -12.271 -27.309 -16.245  1.00 81.81           C  
-ANISOU 2629  C   LEU A 360    11116  13934   6033  -4942   -765   1723       C  
-ATOM   2630  O   LEU A 360     -13.346 -26.707 -16.290  1.00 82.93           O  
-ANISOU 2630  O   LEU A 360    11060  14343   6105  -4971   -876   2009       O  
-ATOM   2631  CB  LEU A 360     -10.204 -26.414 -17.346  1.00 79.13           C  
-ANISOU 2631  CB  LEU A 360    10868  13244   5955  -4825   -568   1459       C  
-ATOM   2632  CG  LEU A 360      -9.299 -25.184 -17.463  1.00 77.66           C  
-ANISOU 2632  CG  LEU A 360    10546  12917   6044  -4565   -527   1419       C  
-ATOM   2633  CD1 LEU A 360      -8.332 -25.324 -18.630  1.00 77.16           C  
-ANISOU 2633  CD1 LEU A 360    10648  12717   5951  -4723   -405   1296       C  
-ATOM   2634  CD2 LEU A 360     -10.129 -23.910 -17.597  1.00 77.03           C  
-ANISOU 2634  CD2 LEU A 360    10176  13072   6021  -4489   -628   1698       C  
-ATOM   2635  N   ASN A 361     -12.165 -28.626 -16.382  1.00 89.49           N  
-ANISOU 2635  N   ASN A 361    12336  14832   6836  -5167   -713   1583       N  
-ATOM   2636  CA  ASN A 361     -13.327 -29.490 -16.525  1.00 92.48           C  
-ANISOU 2636  CA  ASN A 361    12775  15440   6923  -5469   -807   1742       C  
-ATOM   2637  C   ASN A 361     -14.394 -29.216 -15.475  1.00 91.12           C  
-ANISOU 2637  C   ASN A 361    12376  15466   6778  -5290   -955   1961       C  
-ATOM   2638  O   ASN A 361     -15.581 -29.132 -15.791  1.00 92.53           O  
-ANISOU 2638  O   ASN A 361    12454  15942   6762  -5483  -1075   2255       O  
-ATOM   2639  CB  ASN A 361     -12.906 -30.959 -16.467  1.00 96.49           C  
-ANISOU 2639  CB  ASN A 361    13572  15762   7326  -5639   -709   1510       C  
-ATOM   2640  CG  ASN A 361     -12.347 -31.454 -17.782  1.00101.33           C  
-ANISOU 2640  CG  ASN A 361    14448  16280   7772  -5969   -576   1380       C  
-ATOM   2641  OD1 ASN A 361     -12.877 -31.143 -18.847  1.00105.21           O  
-ANISOU 2641  OD1 ASN A 361    14937  16984   8055  -6254   -622   1545       O  
-ATOM   2642  ND2 ASN A 361     -11.272 -32.229 -17.716  1.00103.06           N  
-ANISOU 2642  ND2 ASN A 361    14891  16186   8082  -5936   -400   1097       N  
-ATOM   2643  N   LEU A 362     -13.975 -29.082 -14.222  1.00 78.03           N  
-ANISOU 2643  N   LEU A 362    10637  13652   5357  -4929   -944   1833       N  
-ATOM   2644  CA  LEU A 362     -14.921 -28.791 -13.153  1.00 75.99           C  
-ANISOU 2644  CA  LEU A 362    10169  13564   5138  -4727  -1066   2021       C  
-ATOM   2645  C   LEU A 362     -15.656 -27.483 -13.431  1.00 76.56           C  
-ANISOU 2645  C   LEU A 362     9993  13853   5245  -4652  -1133   2315       C  
-ATOM   2646  O   LEU A 362     -16.884 -27.448 -13.463  1.00 78.74           O  
-ANISOU 2646  O   LEU A 362    10146  14407   5365  -4765  -1243   2621       O  
-ATOM   2647  CB  LEU A 362     -14.219 -28.749 -11.795  1.00 72.60           C  
-ANISOU 2647  CB  LEU A 362     9695  12927   4964  -4351  -1030   1814       C  
-ATOM   2648  CG  LEU A 362     -13.639 -30.087 -11.324  1.00 70.46           C  
-ANISOU 2648  CG  LEU A 362     9615  12474   4682  -4398   -967   1580       C  
-ATOM   2649  CD1 LEU A 362     -12.882 -29.933 -10.015  1.00 68.26           C  
-ANISOU 2649  CD1 LEU A 362     9260  12012   4662  -4036   -932   1402       C  
-ATOM   2650  CD2 LEU A 362     -14.733 -31.128 -11.201  1.00 68.07           C  
-ANISOU 2650  CD2 LEU A 362     9355  12367   4143  -4619  -1066   1727       C  
-ATOM   2651  N   VAL A 363     -14.902 -26.411 -13.646  1.00 70.99           N  
-ANISOU 2651  N   VAL A 363     9206  13017   4750  -4466  -1061   2244       N  
-ATOM   2652  CA  VAL A 363     -15.502 -25.125 -13.967  1.00 73.87           C  
-ANISOU 2652  CA  VAL A 363     9327  13556   5183  -4388  -1095   2519       C  
-ATOM   2653  C   VAL A 363     -16.453 -25.287 -15.143  1.00 79.49           C  
-ANISOU 2653  C   VAL A 363    10018  14565   5620  -4777  -1161   2818       C  
-ATOM   2654  O   VAL A 363     -17.495 -24.634 -15.213  1.00 80.57           O  
-ANISOU 2654  O   VAL A 363     9935  14955   5723  -4781  -1229   3164       O  
-ATOM   2655  CB  VAL A 363     -14.436 -24.084 -14.330  1.00 69.42           C  
-ANISOU 2655  CB  VAL A 363     8718  12799   4859  -4214  -1000   2383       C  
-ATOM   2656  CG1 VAL A 363     -15.013 -22.682 -14.207  1.00 67.19           C  
-ANISOU 2656  CG1 VAL A 363     8153  12641   4736  -4013  -1017   2637       C  
-ATOM   2657  CG2 VAL A 363     -13.220 -24.243 -13.440  1.00 67.45           C  
-ANISOU 2657  CG2 VAL A 363     8575  12229   4825  -3946   -927   2037       C  
-ATOM   2658  N   GLU A 364     -16.082 -26.175 -16.061  1.00100.40           N  
-ANISOU 2658  N   GLU A 364    12900  17181   8068  -5112  -1129   2692       N  
-ATOM   2659  CA  GLU A 364     -16.866 -26.443 -17.262  1.00107.30           C  
-ANISOU 2659  CA  GLU A 364    13799  18329   8642  -5544  -1188   2938       C  
-ATOM   2660  C   GLU A 364     -18.279 -26.910 -16.937  1.00108.63           C  
-ANISOU 2660  C   GLU A 364    13871  18783   8622  -5694  -1331   3238       C  
-ATOM   2661  O   GLU A 364     -19.184 -26.799 -17.761  1.00111.85           O  
-ANISOU 2661  O   GLU A 364    14147  19458   8893  -5993  -1425   3515       O  
-ATOM   2662  CB  GLU A 364     -16.168 -27.504 -18.113  1.00114.57           C  
-ANISOU 2662  CB  GLU A 364    15041  19117   9374  -5868  -1109   2686       C  
-ATOM   2663  CG  GLU A 364     -16.865 -27.817 -19.418  1.00127.17           C  
-ANISOU 2663  CG  GLU A 364    16701  20985  10632  -6356  -1160   2899       C  
-ATOM   2664  CD  GLU A 364     -16.195 -27.157 -20.603  1.00133.56           C  
-ANISOU 2664  CD  GLU A 364    17513  21779  11456  -6473  -1078   2870       C  
-ATOM   2665  OE1 GLU A 364     -15.530 -26.117 -20.410  1.00136.91           O  
-ANISOU 2665  OE1 GLU A 364    17779  22070  12170  -6150  -1023   2820       O  
-ATOM   2666  OE2 GLU A 364     -16.324 -27.686 -21.726  1.00138.69           O  
-ANISOU 2666  OE2 GLU A 364    18327  22549  11821  -6897  -1069   2895       O  
-ATOM   2667  N   ALA A 365     -18.466 -27.437 -15.733  1.00 89.17           N  
-ANISOU 2667  N   ALA A 365    11411  16240   6229  -5488  -1367   3154       N  
-ATOM   2668  CA  ALA A 365     -19.767 -27.957 -15.330  1.00 91.39           C  
-ANISOU 2668  CA  ALA A 365    11552  16736   6436  -5603  -1512   3385       C  
-ATOM   2669  C   ALA A 365     -20.616 -26.909 -14.613  1.00 91.02           C  
-ANISOU 2669  C   ALA A 365    11170  16849   6565  -5308  -1567   3685       C  
-ATOM   2670  O   ALA A 365     -21.817 -26.811 -14.847  1.00 93.66           O  
-ANISOU 2670  O   ALA A 365    11295  17456   6835  -5466  -1680   4023       O  
-ATOM   2671  CB  ALA A 365     -19.597 -29.193 -14.456  1.00 92.64           C  
-ANISOU 2671  CB  ALA A 365    11883  16744   6572  -5568  -1519   3158       C  
-ATOM   2672  N   PHE A 366     -19.989 -26.129 -13.741  1.00 91.24           N  
-ANISOU 2672  N   PHE A 366    11154  16708   6806  -4887  -1481   3569       N  
-ATOM   2673  CA  PHE A 366     -20.712 -25.133 -12.959  1.00 91.27           C  
-ANISOU 2673  CA  PHE A 366    10880  16821   6977  -4574  -1496   3821       C  
-ATOM   2674  C   PHE A 366     -21.111 -23.919 -13.787  1.00 94.53           C  
-ANISOU 2674  C   PHE A 366    11076  17401   7441  -4606  -1471   4133       C  
-ATOM   2675  O   PHE A 366     -21.753 -22.997 -13.283  1.00 94.46           O  
-ANISOU 2675  O   PHE A 366    10828  17487   7574  -4362  -1455   4387       O  
-ATOM   2676  CB  PHE A 366     -19.899 -24.713 -11.731  1.00 86.35           C  
-ANISOU 2676  CB  PHE A 366    10296  15954   6558  -4134  -1414   3570       C  
-ATOM   2677  CG  PHE A 366     -19.752 -25.803 -10.704  1.00 81.34           C  
-ANISOU 2677  CG  PHE A 366     9790  15219   5897  -4055  -1453   3353       C  
-ATOM   2678  CD1 PHE A 366     -20.605 -25.868  -9.615  1.00 79.06           C  
-ANISOU 2678  CD1 PHE A 366     9337  15027   5676  -3860  -1512   3486       C  
-ATOM   2679  CD2 PHE A 366     -18.766 -26.768 -10.835  1.00 79.41           C  
-ANISOU 2679  CD2 PHE A 366     9794  14767   5610  -4175  -1414   3014       C  
-ATOM   2680  CE1 PHE A 366     -20.475 -26.870  -8.676  1.00 76.38           C  
-ANISOU 2680  CE1 PHE A 366     9078  14600   5343  -3792  -1544   3294       C  
-ATOM   2681  CE2 PHE A 366     -18.634 -27.772  -9.901  1.00 77.07           C  
-ANISOU 2681  CE2 PHE A 366     9592  14388   5304  -4105  -1441   2842       C  
-ATOM   2682  CZ  PHE A 366     -19.489 -27.823  -8.821  1.00 76.14           C  
-ANISOU 2682  CZ  PHE A 366     9294  14379   5258  -3917  -1511   2977       C  
-ATOM   2683  N   VAL A 367     -20.730 -23.932 -15.061  1.00 81.94           N  
-ANISOU 2683  N   VAL A 367     9561  15840   5732  -4909  -1456   4122       N  
-ATOM   2684  CA  VAL A 367     -21.143 -22.896 -15.999  1.00 88.04           C  
-ANISOU 2684  CA  VAL A 367    10105  16806   6539  -5005  -1446   4439       C  
-ATOM   2685  C   VAL A 367     -22.321 -23.369 -16.851  1.00 94.09           C  
-ANISOU 2685  C   VAL A 367    10737  17907   7107  -5425  -1595   4754       C  
-ATOM   2686  O   VAL A 367     -23.266 -22.617 -17.096  1.00 95.88           O  
-ANISOU 2686  O   VAL A 367    10658  18382   7391  -5433  -1639   5149       O  
-ATOM   2687  CB  VAL A 367     -19.985 -22.476 -16.920  1.00 86.38           C  
-ANISOU 2687  CB  VAL A 367    10025  16453   6344  -5073  -1336   4261       C  
-ATOM   2688  CG1 VAL A 367     -18.995 -21.598 -16.170  1.00 85.17           C  
-ANISOU 2688  CG1 VAL A 367     9830  15988   6542  -4632  -1225   3996       C  
-ATOM   2689  CG2 VAL A 367     -19.295 -23.700 -17.496  1.00 87.03           C  
-ANISOU 2689  CG2 VAL A 367    10431  16422   6213  -5379  -1340   3951       C  
-ATOM   2690  N   GLU A 368     -22.264 -24.622 -17.292  1.00111.75           N  
-ANISOU 2690  N   GLU A 368    13203  20148   9108  -5779  -1666   4590       N  
-ATOM   2691  CA  GLU A 368     -23.326 -25.195 -18.113  1.00120.51           C  
-ANISOU 2691  CA  GLU A 368    14232  21569   9986  -6230  -1821   4861       C  
-ATOM   2692  C   GLU A 368     -24.419 -25.815 -17.249  1.00124.25           C  
-ANISOU 2692  C   GLU A 368    14596  22172  10442  -6212  -1941   5031       C  
-ATOM   2693  O   GLU A 368     -25.299 -26.514 -17.751  1.00126.77           O  
-ANISOU 2693  O   GLU A 368    14885  22726  10555  -6593  -2084   5225       O  
-ATOM   2694  CB  GLU A 368     -22.756 -26.238 -19.078  1.00123.80           C  
-ANISOU 2694  CB  GLU A 368    14978  21927  10135  -6656  -1824   4609       C  
-ATOM   2695  CG  GLU A 368     -21.669 -25.692 -19.998  1.00127.45           C  
-ANISOU 2695  CG  GLU A 368    15552  22270  10604  -6695  -1699   4443       C  
-ATOM   2696  CD  GLU A 368     -21.158 -26.720 -20.989  1.00130.59           C  
-ANISOU 2696  CD  GLU A 368    16283  22616  10719  -7128  -1680   4208       C  
-ATOM   2697  OE1 GLU A 368     -21.987 -27.429 -21.598  1.00133.39           O  
-ANISOU 2697  OE1 GLU A 368    16666  23201  10816  -7558  -1807   4361       O  
-ATOM   2698  OE2 GLU A 368     -19.925 -26.819 -21.159  1.00131.09           O  
-ANISOU 2698  OE2 GLU A 368    16588  22407  10813  -7042  -1528   3877       O  
-ATOM   2699  N   ASP A 369     -24.351 -25.552 -15.947  1.00107.72           N  
-ANISOU 2699  N   ASP A 369    12443  19928   8557  -5775  -1884   4961       N  
-ATOM   2700  CA  ASP A 369     -25.324 -26.072 -14.992  1.00111.67           C  
-ANISOU 2700  CA  ASP A 369    12822  20531   9077  -5692  -1978   5111       C  
-ATOM   2701  C   ASP A 369     -25.694 -24.962 -14.013  1.00112.48           C  
-ANISOU 2701  C   ASP A 369    12663  20640   9436  -5226  -1909   5301       C  
-ATOM   2702  O   ASP A 369     -25.545 -25.112 -12.801  1.00113.17           O  
-ANISOU 2702  O   ASP A 369    12784  20573   9641  -4903  -1867   5148       O  
-ATOM   2703  CB  ASP A 369     -24.745 -27.277 -14.242  1.00110.42           C  
-ANISOU 2703  CB  ASP A 369    12944  20136   8876  -5656  -1968   4737       C  
-ATOM   2704  CG  ASP A 369     -25.801 -28.071 -13.491  1.00112.43           C  
-ANISOU 2704  CG  ASP A 369    13093  20527   9100  -5690  -2088   4900       C  
-ATOM   2705  OD1 ASP A 369     -26.893 -27.524 -13.228  1.00111.46           O  
-ANISOU 2705  OD1 ASP A 369    12665  20636   9048  -5604  -2151   5276       O  
-ATOM   2706  OD2 ASP A 369     -25.534 -29.245 -13.154  1.00111.32           O  
-ANISOU 2706  OD2 ASP A 369    13165  20258   8873  -5793  -2111   4662       O  
-ATOM   2707  N   ALA A 370     -26.171 -23.844 -14.554  1.00128.07           N  
-ANISOU 2707  N   ALA A 370    14376  22793  11490  -5199  -1887   5639       N  
-ATOM   2708  CA  ALA A 370     -26.475 -22.660 -13.758  1.00126.83           C  
-ANISOU 2708  CA  ALA A 370    13986  22624  11578  -4764  -1782   5836       C  
-ATOM   2709  C   ALA A 370     -27.131 -22.998 -12.423  1.00126.38           C  
-ANISOU 2709  C   ALA A 370    13856  22565  11596  -4502  -1801   5882       C  
-ATOM   2710  O   ALA A 370     -26.796 -22.411 -11.397  1.00125.69           O  
-ANISOU 2710  O   ALA A 370    13775  22301  11681  -4085  -1683   5770       O  
-ATOM   2711  CB  ALA A 370     -27.346 -21.699 -14.552  1.00128.13           C  
-ANISOU 2711  CB  ALA A 370    13816  23075  11792  -4858  -1795   6318       C  
-ATOM   2712  N   GLU A 371     -28.065 -23.942 -12.442  1.00133.63           N  
-ANISOU 2712  N   GLU A 371    14710  23686  12378  -4758  -1951   6048       N  
-ATOM   2713  CA  GLU A 371     -28.755 -24.360 -11.226  1.00132.77           C  
-ANISOU 2713  CA  GLU A 371    14512  23601  12334  -4541  -1979   6113       C  
-ATOM   2714  C   GLU A 371     -27.780 -24.810 -10.143  1.00124.92           C  
-ANISOU 2714  C   GLU A 371    13766  22295  11402  -4263  -1906   5659       C  
-ATOM   2715  O   GLU A 371     -27.629 -24.153  -9.114  1.00123.06           O  
-ANISOU 2715  O   GLU A 371    13484  21941  11333  -3847  -1799   5609       O  
-ATOM   2716  CB  GLU A 371     -29.722 -25.499 -11.533  1.00139.45           C  
-ANISOU 2716  CB  GLU A 371    15305  24683  12998  -4926  -2163   6302       C  
-ATOM   2717  CG  GLU A 371     -30.234 -26.206 -10.296  1.00145.25           C  
-ANISOU 2717  CG  GLU A 371    16006  25401  13780  -4744  -2197   6281       C  
-ATOM   2718  CD  GLU A 371     -30.854 -27.547 -10.614  1.00150.78           C  
-ANISOU 2718  CD  GLU A 371    16755  26251  14285  -5157  -2372   6345       C  
-ATOM   2719  OE1 GLU A 371     -31.141 -27.807 -11.801  1.00154.05           O  
-ANISOU 2719  OE1 GLU A 371    17176  26841  14515  -5594  -2481   6497       O  
-ATOM   2720  OE2 GLU A 371     -31.048 -28.343  -9.674  1.00153.03           O  
-ANISOU 2720  OE2 GLU A 371    17073  26478  14592  -5052  -2401   6245       O  
-ATOM   2721  N   LEU A 372     -27.136 -25.946 -10.385  1.00108.19           N  
-ANISOU 2721  N   LEU A 372    11912  20053   9143  -4506  -1962   5342       N  
-ATOM   2722  CA  LEU A 372     -26.134 -26.494  -9.481  1.00100.39           C  
-ANISOU 2722  CA  LEU A 372    11157  18781   8206  -4294  -1902   4914       C  
-ATOM   2723  C   LEU A 372     -25.235 -25.404  -8.902  1.00 97.73           C  
-ANISOU 2723  C   LEU A 372    10855  18233   8044  -3886  -1755   4732       C  
-ATOM   2724  O   LEU A 372     -25.019 -25.340  -7.694  1.00 93.13           O  
-ANISOU 2724  O   LEU A 372    10281  17531   7575  -3552  -1708   4586       O  
-ATOM   2725  CB  LEU A 372     -25.295 -27.534 -10.224  1.00 96.91           C  
-ANISOU 2725  CB  LEU A 372    11015  18206   7601  -4629  -1928   4608       C  
-ATOM   2726  CG  LEU A 372     -24.075 -28.143  -9.532  1.00 90.69           C  
-ANISOU 2726  CG  LEU A 372    10483  17115   6860  -4465  -1855   4160       C  
-ATOM   2727  CD1 LEU A 372     -24.430 -28.681  -8.151  1.00 89.94           C  
-ANISOU 2727  CD1 LEU A 372    10315  16999   6858  -4222  -1881   4121       C  
-ATOM   2728  CD2 LEU A 372     -23.482 -29.237 -10.411  1.00 90.96           C  
-ANISOU 2728  CD2 LEU A 372    10795  17055   6709  -4847  -1871   3941       C  
-ATOM   2729  N   ARG A 373     -24.717 -24.547  -9.776  1.00 95.72           N  
-ANISOU 2729  N   ARG A 373    10620  17944   7805  -3928  -1685   4748       N  
-ATOM   2730  CA  ARG A 373     -23.839 -23.456  -9.369  1.00 96.49           C  
-ANISOU 2730  CA  ARG A 373    10761  17841   8059  -3579  -1547   4595       C  
-ATOM   2731  C   ARG A 373     -24.558 -22.504  -8.423  1.00101.93           C  
-ANISOU 2731  C   ARG A 373    11234  18592   8901  -3211  -1483   4835       C  
-ATOM   2732  O   ARG A 373     -24.060 -22.191  -7.345  1.00102.37           O  
-ANISOU 2732  O   ARG A 373    11361  18478   9058  -2870  -1414   4635       O  
-ATOM   2733  CB  ARG A 373     -23.346 -22.690 -10.599  1.00 95.37           C  
-ANISOU 2733  CB  ARG A 373    10629  17694   7912  -3727  -1486   4651       C  
-ATOM   2734  CG  ARG A 373     -22.313 -21.612 -10.305  1.00 91.13           C  
-ANISOU 2734  CG  ARG A 373    10151  16921   7554  -3410  -1342   4461       C  
-ATOM   2735  CD  ARG A 373     -22.595 -20.371 -11.123  1.00 89.78           C  
-ANISOU 2735  CD  ARG A 373     9767  16842   7502  -3412  -1262   4752       C  
-ATOM   2736  NE  ARG A 373     -22.905 -20.706 -12.508  1.00 89.77           N  
-ANISOU 2736  NE  ARG A 373     9746  17049   7314  -3836  -1334   4950       N  
-ATOM   2737  CZ  ARG A 373     -23.506 -19.880 -13.358  1.00 92.25           C  
-ANISOU 2737  CZ  ARG A 373     9816  17557   7676  -3942  -1314   5312       C  
-ATOM   2738  NH1 ARG A 373     -23.869 -18.670 -12.957  1.00 91.14           N  
-ANISOU 2738  NH1 ARG A 373     9467  17422   7739  -3643  -1195   5558       N  
-ATOM   2739  NH2 ARG A 373     -23.750 -20.264 -14.606  1.00 94.97           N  
-ANISOU 2739  NH2 ARG A 373    10126  18093   7865  -4352  -1407   5436       N  
-ATOM   2740  N   GLN A 374     -25.732 -22.043  -8.836  1.00 97.81           N  
-ANISOU 2740  N   GLN A 374    10450  18322   8393  -3286  -1502   5272       N  
-ATOM   2741  CA  GLN A 374     -26.509 -21.107  -8.036  1.00106.11           C  
-ANISOU 2741  CA  GLN A 374    11285  19440   9593  -2945  -1413   5553       C  
-ATOM   2742  C   GLN A 374     -26.921 -21.734  -6.712  1.00107.67           C  
-ANISOU 2742  C   GLN A 374    11480  19630   9800  -2739  -1448   5476       C  
-ATOM   2743  O   GLN A 374     -26.831 -21.102  -5.659  1.00106.04           O  
-ANISOU 2743  O   GLN A 374    11271  19314   9706  -2361  -1344   5427       O  
-ATOM   2744  CB  GLN A 374     -27.751 -20.654  -8.801  1.00111.89           C  
-ANISOU 2744  CB  GLN A 374    11707  20471  10334  -3107  -1438   6071       C  
-ATOM   2745  CG  GLN A 374     -27.452 -19.906 -10.084  1.00116.70           C  
-ANISOU 2745  CG  GLN A 374    12258  21122  10959  -3291  -1395   6203       C  
-ATOM   2746  CD  GLN A 374     -28.615 -19.940 -11.047  1.00122.83           C  
-ANISOU 2746  CD  GLN A 374    12753  22245  11670  -3606  -1501   6666       C  
-ATOM   2747  OE1 GLN A 374     -29.668 -20.501 -10.743  1.00125.57           O  
-ANISOU 2747  OE1 GLN A 374    12949  22798  11964  -3683  -1604   6904       O  
-ATOM   2748  NE2 GLN A 374     -28.433 -19.345 -12.218  1.00125.37           N  
-ANISOU 2748  NE2 GLN A 374    12991  22648  11996  -3800  -1484   6809       N  
-ATOM   2749  N   THR A 375     -27.374 -22.982  -6.771  1.00159.05           N  
-ANISOU 2749  N   THR A 375    17992  26254  16184  -2999  -1590   5470       N  
-ATOM   2750  CA  THR A 375     -27.838 -23.688  -5.582  1.00159.12           C  
-ANISOU 2750  CA  THR A 375    17969  26283  16207  -2842  -1630   5425       C  
-ATOM   2751  C   THR A 375     -26.742 -23.800  -4.525  1.00152.92           C  
-ANISOU 2751  C   THR A 375    17394  25231  15479  -2561  -1571   4989       C  
-ATOM   2752  O   THR A 375     -26.989 -24.247  -3.406  1.00151.78           O  
-ANISOU 2752  O   THR A 375    17221  25082  15365  -2374  -1583   4920       O  
-ATOM   2753  CB  THR A 375     -28.356 -25.096  -5.933  1.00167.39           C  
-ANISOU 2753  CB  THR A 375    19022  27470  17110  -3214  -1791   5460       C  
-ATOM   2754  OG1 THR A 375     -27.313 -25.847  -6.566  1.00171.92           O  
-ANISOU 2754  OG1 THR A 375    19864  27882  17577  -3469  -1829   5114       O  
-ATOM   2755  CG2 THR A 375     -29.551 -25.006  -6.873  1.00171.59           C  
-ANISOU 2755  CG2 THR A 375    19319  28306  17573  -3502  -1878   5924       C  
-ATOM   2756  N   LEU A 376     -25.531 -23.392  -4.889  1.00107.38           N  
-ANISOU 2756  N   LEU A 376    11819  19256   9725  -2539  -1511   4708       N  
-ATOM   2757  CA  LEU A 376     -24.397 -23.443  -3.978  1.00101.63           C  
-ANISOU 2757  CA  LEU A 376    11281  18285   9048  -2300  -1469   4301       C  
-ATOM   2758  C   LEU A 376     -23.902 -22.041  -3.652  1.00103.46           C  
-ANISOU 2758  C   LEU A 376    11531  18386   9394  -1980  -1340   4269       C  
-ATOM   2759  O   LEU A 376     -23.692 -21.697  -2.491  1.00104.73           O  
-ANISOU 2759  O   LEU A 376    11680  18430   9684  -1671  -1276   4097       O  
-ATOM   2760  CB  LEU A 376     -23.260 -24.250  -4.603  1.00 87.57           C  
-ANISOU 2760  CB  LEU A 376     9734  16346   7194  -2544  -1507   3962       C  
-ATOM   2761  CG  LEU A 376     -23.584 -25.691  -4.999  1.00 79.98           C  
-ANISOU 2761  CG  LEU A 376     8814  15463   6111  -2887  -1615   3950       C  
-ATOM   2762  CD1 LEU A 376     -22.574 -26.214  -6.007  1.00 72.07           C  
-ANISOU 2762  CD1 LEU A 376     8042  14323   5020  -3167  -1614   3708       C  
-ATOM   2763  CD2 LEU A 376     -23.647 -26.590  -3.767  1.00 71.93           C  
-ANISOU 2763  CD2 LEU A 376     7795  14412   5125  -2751  -1651   3800       C  
-ATOM   2764  N   GLN A 377     -23.727 -21.232  -4.691  1.00140.13           N  
-ANISOU 2764  N   GLN A 377    16127  23002  14113  -2081  -1267   4366       N  
-ATOM   2765  CA  GLN A 377     -23.108 -19.920  -4.554  1.00142.04           C  
-ANISOU 2765  CA  GLN A 377    16321  23029  14617  -1832  -1107   4224       C  
-ATOM   2766  C   GLN A 377     -23.951 -18.961  -3.720  1.00145.03           C  
-ANISOU 2766  C   GLN A 377    16524  23452  15128  -1507   -992   4459       C  
-ATOM   2767  O   GLN A 377     -23.532 -17.836  -3.452  1.00143.49           O  
-ANISOU 2767  O   GLN A 377    16292  23068  15161  -1273   -841   4345       O  
-ATOM   2768  CB  GLN A 377     -22.828 -19.321  -5.938  1.00144.10           C  
-ANISOU 2768  CB  GLN A 377    16543  23286  14923  -2034  -1064   4327       C  
-ATOM   2769  CG  GLN A 377     -21.757 -18.236  -5.952  1.00144.07           C  
-ANISOU 2769  CG  GLN A 377    16558  22998  15184  -1846   -928   4051       C  
-ATOM   2770  CD  GLN A 377     -22.334 -16.835  -6.012  1.00147.51           C  
-ANISOU 2770  CD  GLN A 377    16781  23448  15819  -1644   -779   4332       C  
-ATOM   2771  OE1 GLN A 377     -21.623 -15.849  -5.816  1.00148.61           O  
-ANISOU 2771  OE1 GLN A 377    16916  23355  16194  -1441   -655   4135       O  
-ATOM   2772  NE2 GLN A 377     -23.628 -16.739  -6.292  1.00148.61           N  
-ANISOU 2772  NE2 GLN A 377    16736  23859  15870  -1705   -784   4810       N  
-ATOM   2773  N   GLU A 378     -25.130 -19.406  -3.297  1.00135.33           N  
-ANISOU 2773  N   GLU A 378    15195  22464  13762  -1490  -1054   4788       N  
-ATOM   2774  CA  GLU A 378     -26.040 -18.521  -2.581  1.00139.76           C  
-ANISOU 2774  CA  GLU A 378    15582  23083  14438  -1188   -926   5070       C  
-ATOM   2775  C   GLU A 378     -26.985 -19.261  -1.643  1.00139.00           C  
-ANISOU 2775  C   GLU A 378    15441  23179  14195  -1094  -1011   5257       C  
-ATOM   2776  O   GLU A 378     -27.791 -18.634  -0.958  1.00142.00           O  
-ANISOU 2776  O   GLU A 378    15685  23616  14653   -830   -901   5500       O  
-ATOM   2777  CB  GLU A 378     -26.859 -17.698  -3.579  1.00147.00           C  
-ANISOU 2777  CB  GLU A 378    16293  24160  15402  -1275   -847   5550       C  
-ATOM   2778  CG  GLU A 378     -27.929 -18.499  -4.310  1.00157.20           C  
-ANISOU 2778  CG  GLU A 378    17456  25782  16492  -1589   -996   5965       C  
-ATOM   2779  CD  GLU A 378     -28.001 -18.171  -5.790  1.00161.83           C  
-ANISOU 2779  CD  GLU A 378    17931  26476  17080  -1893  -1005   6188       C  
-ATOM   2780  OE1 GLU A 378     -29.021 -18.511  -6.427  1.00165.05           O  
-ANISOU 2780  OE1 GLU A 378    18113  27152  17446  -2132  -1095   6537       O  
-ATOM   2781  OE2 GLU A 378     -27.034 -17.582  -6.319  1.00163.05           O  
-ANISOU 2781  OE2 GLU A 378    18196  26453  17301  -1903   -929   5996       O  
-ATOM   2782  N   ASP A 379     -26.896 -20.585  -1.607  1.00131.73           N  
-ANISOU 2782  N   ASP A 379    14590  22328  13134  -1309  -1177   5108       N  
-ATOM   2783  CA  ASP A 379     -27.848 -21.365  -0.823  1.00130.54           C  
-ANISOU 2783  CA  ASP A 379    14299  22340  12962  -1269  -1239   5236       C  
-ATOM   2784  C   ASP A 379     -27.205 -22.224   0.259  1.00122.83           C  
-ANISOU 2784  C   ASP A 379    13460  21252  11958  -1171  -1300   4846       C  
-ATOM   2785  O   ASP A 379     -27.593 -22.156   1.422  1.00122.30           O  
-ANISOU 2785  O   ASP A 379    13335  21212  11920   -899  -1263   4857       O  
-ATOM   2786  CB  ASP A 379     -28.709 -22.238  -1.739  1.00138.10           C  
-ANISOU 2786  CB  ASP A 379    15102  23525  13846  -1648  -1364   5499       C  
-ATOM   2787  CG  ASP A 379     -29.430 -21.432  -2.804  1.00146.82           C  
-ANISOU 2787  CG  ASP A 379    16019  24786  14981  -1771  -1321   5923       C  
-ATOM   2788  OD1 ASP A 379     -30.535 -20.921  -2.522  1.00151.12           O  
-ANISOU 2788  OD1 ASP A 379    16331  25496  15593  -1620  -1256   6315       O  
-ATOM   2789  OD2 ASP A 379     -28.889 -21.312  -3.923  1.00149.84           O  
-ANISOU 2789  OD2 ASP A 379    16474  25134  15324  -2017  -1345   5875       O  
-ATOM   2790  N   LEU A 380     -26.226 -23.034  -0.124  1.00111.25           N  
-ANISOU 2790  N   LEU A 380    12165  19665  10441  -1390  -1383   4517       N  
-ATOM   2791  CA  LEU A 380     -25.663 -24.007   0.804  1.00101.55           C  
-ANISOU 2791  CA  LEU A 380    11029  18352   9203  -1348  -1441   4189       C  
-ATOM   2792  C   LEU A 380     -24.260 -23.657   1.291  1.00 96.17           C  
-ANISOU 2792  C   LEU A 380    10550  17434   8556  -1186  -1407   3781       C  
-ATOM   2793  O   LEU A 380     -23.957 -23.803   2.474  1.00 94.93           O  
-ANISOU 2793  O   LEU A 380    10414  17226   8428   -972  -1404   3583       O  
-ATOM   2794  CB  LEU A 380     -25.677 -25.405   0.183  1.00 98.92           C  
-ANISOU 2794  CB  LEU A 380    10725  18063   8797  -1714  -1554   4139       C  
-ATOM   2795  CG  LEU A 380     -27.053 -25.899  -0.265  1.00 97.35           C  
-ANISOU 2795  CG  LEU A 380    10327  18114   8546  -1919  -1623   4529       C  
-ATOM   2796  CD1 LEU A 380     -26.953 -27.281  -0.887  1.00 96.67           C  
-ANISOU 2796  CD1 LEU A 380    10322  18042   8367  -2297  -1736   4445       C  
-ATOM   2797  CD2 LEU A 380     -28.017 -25.909   0.900  1.00 96.31           C  
-ANISOU 2797  CD2 LEU A 380    10008  18120   8464  -1667  -1602   4713       C  
-ATOM   2798  N   LEU A 381     -23.404 -23.196   0.386  1.00 94.49           N  
-ANISOU 2798  N   LEU A 381     8347  15836  11718  -5474  -1161   2984       N  
-ATOM   2799  CA  LEU A 381     -22.029 -22.891   0.761  1.00 90.98           C  
-ANISOU 2799  CA  LEU A 381     7922  15407  11241  -5405  -1202   2779       C  
-ATOM   2800  C   LEU A 381     -21.950 -21.890   1.911  1.00 89.43           C  
-ANISOU 2800  C   LEU A 381     7812  14916  11252  -5270  -1167   2806       C  
-ATOM   2801  O   LEU A 381     -21.225 -22.108   2.880  1.00 88.12           O  
-ANISOU 2801  O   LEU A 381     7804  14604  11072  -5096  -1167   2572       O  
-ATOM   2802  CB  LEU A 381     -21.222 -22.393  -0.440  1.00 86.19           C  
-ANISOU 2802  CB  LEU A 381     7090  15102  10555  -5605  -1268   2830       C  
-ATOM   2803  CG  LEU A 381     -20.744 -23.472  -1.411  1.00 83.35           C  
-ANISOU 2803  CG  LEU A 381     6670  15047   9951  -5700  -1317   2684       C  
-ATOM   2804  CD1 LEU A 381     -19.846 -22.860  -2.470  1.00 82.23           C  
-ANISOU 2804  CD1 LEU A 381     6317  15180   9747  -5893  -1374   2718       C  
-ATOM   2805  CD2 LEU A 381     -20.012 -24.571  -0.671  1.00 79.04           C  
-ANISOU 2805  CD2 LEU A 381     6312  14459   9261  -5513  -1333   2337       C  
-ATOM   2806  N   ARG A 382     -22.704 -20.800   1.812  1.00114.66           N  
-ANISOU 2806  N   ARG A 382    10910  18019  14638  -5346  -1141   3090       N  
-ATOM   2807  CA  ARG A 382     -22.649 -19.759   2.834  1.00112.77           C  
-ANISOU 2807  CA  ARG A 382    10738  17509  14602  -5231  -1111   3141       C  
-ATOM   2808  C   ARG A 382     -23.249 -20.235   4.159  1.00109.60           C  
-ANISOU 2808  C   ARG A 382    10575  16793  14276  -5017  -1040   3043       C  
-ATOM   2809  O   ARG A 382     -23.473 -19.440   5.070  1.00106.60           O  
-ANISOU 2809  O   ARG A 382    10267  16155  14080  -4914  -1000   3111       O  
-ATOM   2810  CB  ARG A 382     -23.337 -18.475   2.348  1.00119.03           C  
-ANISOU 2810  CB  ARG A 382    11367  18287  15573  -5368  -1110   3473       C  
-ATOM   2811  CG  ARG A 382     -24.815 -18.376   2.696  1.00126.04           C  
-ANISOU 2811  CG  ARG A 382    12297  18980  16612  -5334  -1047   3671       C  
-ATOM   2812  CD  ARG A 382     -25.688 -18.284   1.456  1.00136.05           C  
-ANISOU 2812  CD  ARG A 382    13384  20438  17869  -5534  -1070   3917       C  
-ATOM   2813  NE  ARG A 382     -26.882 -19.115   1.589  1.00143.40           N  
-ANISOU 2813  NE  ARG A 382    14388  21297  18801  -5496  -1014   3953       N  
-ATOM   2814  CZ  ARG A 382     -28.063 -18.677   2.015  1.00147.07           C  
-ANISOU 2814  CZ  ARG A 382    14869  21564  19448  -5459   -962   4132       C  
-ATOM   2815  NH1 ARG A 382     -28.225 -17.404   2.348  1.00148.10           N  
-ANISOU 2815  NH1 ARG A 382    14950  21544  19777  -5449   -963   4300       N  
-ATOM   2816  NH2 ARG A 382     -29.087 -19.516   2.104  1.00148.95           N  
-ANISOU 2816  NH2 ARG A 382    15171  21757  19668  -5433   -909   4139       N  
-ATOM   2817  N   ARG A 383     -23.498 -21.539   4.262  1.00 93.91           N  
-ANISOU 2817  N   ARG A 383     8717  14826  12140  -4955  -1023   2882       N  
-ATOM   2818  CA  ARG A 383     -24.069 -22.124   5.472  1.00 93.01           C  
-ANISOU 2818  CA  ARG A 383     8849  14424  12068  -4767   -954   2771       C  
-ATOM   2819  C   ARG A 383     -23.093 -23.055   6.181  1.00 92.42           C  
-ANISOU 2819  C   ARG A 383     8979  14299  11839  -4601   -979   2424       C  
-ATOM   2820  O   ARG A 383     -23.431 -23.668   7.194  1.00 92.16           O  
-ANISOU 2820  O   ARG A 383     9179  14031  11805  -4440   -930   2291       O  
-ATOM   2821  CB  ARG A 383     -25.354 -22.883   5.150  1.00 93.51           C  
-ANISOU 2821  CB  ARG A 383     8931  14501  12098  -4820   -904   2877       C  
-ATOM   2822  CG  ARG A 383     -26.525 -21.994   4.794  1.00 96.71           C  
-ANISOU 2822  CG  ARG A 383     9189  14863  12692  -4929   -865   3202       C  
-ATOM   2823  CD  ARG A 383     -27.770 -22.824   4.576  1.00 98.53           C  
-ANISOU 2823  CD  ARG A 383     9455  15096  12887  -4965   -812   3273       C  
-ATOM   2824  NE  ARG A 383     -28.860 -22.035   4.014  1.00101.30           N  
-ANISOU 2824  NE  ARG A 383     9631  15459  13399  -5091   -794   3580       N  
-ATOM   2825  CZ  ARG A 383     -29.862 -22.548   3.308  1.00103.12           C  
-ANISOU 2825  CZ  ARG A 383     9787  15801  13592  -5197   -777   3703       C  
-ATOM   2826  NH1 ARG A 383     -29.912 -23.853   3.076  1.00102.79           N  
-ANISOU 2826  NH1 ARG A 383     9833  15869  13353  -5198   -771   3551       N  
-ATOM   2827  NH2 ARG A 383     -30.813 -21.758   2.829  1.00105.66           N  
-ANISOU 2827  NH2 ARG A 383     9950  16124  14071  -5301   -771   3975       N  
-ATOM   2828  N   PHE A 384     -21.886 -23.162   5.639  1.00 91.19           N  
-ANISOU 2828  N   PHE A 384     8736  14362  11549  -4643  -1058   2271       N  
-ATOM   2829  CA  PHE A 384     -20.840 -23.979   6.242  1.00 90.09           C  
-ANISOU 2829  CA  PHE A 384     8771  14196  11262  -4487  -1101   1929       C  
-ATOM   2830  C   PHE A 384     -19.790 -23.120   6.935  1.00 88.61           C  
-ANISOU 2830  C   PHE A 384     8603  13893  11172  -4387  -1129   1824       C  
-ATOM   2831  O   PHE A 384     -19.183 -22.245   6.314  1.00 89.95           O  
-ANISOU 2831  O   PHE A 384     8574  14221  11382  -4507  -1167   1911       O  
-ATOM   2832  CB  PHE A 384     -20.163 -24.846   5.184  1.00 92.49           C  
-ANISOU 2832  CB  PHE A 384     8976  14836  11330  -4588  -1176   1785       C  
-ATOM   2833  CG  PHE A 384     -21.034 -25.938   4.646  1.00 91.85           C  
-ANISOU 2833  CG  PHE A 384     8928  14856  11114  -4647  -1158   1816       C  
-ATOM   2834  CD1 PHE A 384     -20.968 -27.217   5.173  1.00 89.96           C  
-ANISOU 2834  CD1 PHE A 384     8918  14549  10714  -4509  -1165   1567       C  
-ATOM   2835  CD2 PHE A 384     -21.916 -25.689   3.610  1.00 92.56           C  
-ANISOU 2835  CD2 PHE A 384     8828  15107  11235  -4842  -1138   2092       C  
-ATOM   2836  CE1 PHE A 384     -21.765 -28.223   4.678  1.00 88.97           C  
-ANISOU 2836  CE1 PHE A 384     8828  14518  10459  -4568  -1148   1595       C  
-ATOM   2837  CE2 PHE A 384     -22.718 -26.692   3.111  1.00 92.00           C  
-ANISOU 2837  CE2 PHE A 384     8785  15131  11041  -4898  -1122   2120       C  
-ATOM   2838  CZ  PHE A 384     -22.641 -27.962   3.645  1.00 90.15           C  
-ANISOU 2838  CZ  PHE A 384     8776  14831  10644  -4763  -1124   1873       C  
-ATOM   2839  N   PRO A 385     -19.563 -23.380   8.228  1.00 95.48           N  
-ANISOU 2839  N   PRO A 385     9721  14482  12074  -4171  -1111   1630       N  
-ATOM   2840  CA  PRO A 385     -18.570 -22.646   9.019  1.00 93.78           C  
-ANISOU 2840  CA  PRO A 385     9555  14126  11951  -4051  -1137   1507       C  
-ATOM   2841  C   PRO A 385     -17.143 -23.033   8.633  1.00 91.30           C  
-ANISOU 2841  C   PRO A 385     9188  14034  11468  -4044  -1232   1238       C  
-ATOM   2842  O   PRO A 385     -16.943 -24.044   7.955  1.00 91.89           O  
-ANISOU 2842  O   PRO A 385     9244  14327  11344  -4092  -1275   1107       O  
-ATOM   2843  CB  PRO A 385     -18.873 -23.096  10.450  1.00 91.57           C  
-ANISOU 2843  CB  PRO A 385     9585  13489  11717  -3823  -1091   1360       C  
-ATOM   2844  CG  PRO A 385     -19.457 -24.463  10.294  1.00 90.56           C  
-ANISOU 2844  CG  PRO A 385     9590  13404  11416  -3809  -1080   1260       C  
-ATOM   2845  CD  PRO A 385     -20.241 -24.428   9.013  1.00 94.24           C  
-ANISOU 2845  CD  PRO A 385     9826  14124  11858  -4031  -1065   1511       C  
-ATOM   2846  N   ASP A 386     -16.165 -22.233   9.047  1.00 87.99           N  
-ANISOU 2846  N   ASP A 386     8740  13564  11128  -3987  -1264   1154       N  
-ATOM   2847  CA  ASP A 386     -14.771 -22.558   8.780  1.00 85.19           C  
-ANISOU 2847  CA  ASP A 386     8337  13403  10627  -3967  -1352    876       C  
-ATOM   2848  C   ASP A 386     -14.394 -23.797   9.572  1.00 82.24           C  
-ANISOU 2848  C   ASP A 386     8227  12908  10112  -3757  -1390    542       C  
-ATOM   2849  O   ASP A 386     -13.981 -23.702  10.726  1.00 81.94           O  
-ANISOU 2849  O   ASP A 386     8383  12611  10140  -3562  -1397    380       O  
-ATOM   2850  CB  ASP A 386     -13.854 -21.396   9.166  1.00 85.77           C  
-ANISOU 2850  CB  ASP A 386     8338  13418  10832  -3941  -1372    857       C  
-ATOM   2851  CG  ASP A 386     -12.425 -21.585   8.670  1.00 86.15           C  
-ANISOU 2851  CG  ASP A 386     8272  13722  10738  -3968  -1460    600       C  
-ATOM   2852  OD1 ASP A 386     -12.070 -22.711   8.258  1.00 83.99           O  
-ANISOU 2852  OD1 ASP A 386     8024  13623  10265  -3956  -1512    388       O  
-ATOM   2853  OD2 ASP A 386     -11.656 -20.601   8.699  1.00 86.19           O  
-ANISOU 2853  OD2 ASP A 386     8164  13754  10832  -4003  -1476    606       O  
-ATOM   2854  N   LEU A 387     -14.546 -24.962   8.952  1.00 75.27           N  
-ANISOU 2854  N   LEU A 387     7362  12207   9032  -3797  -1420    442       N  
-ATOM   2855  CA  LEU A 387     -14.247 -26.216   9.627  1.00 73.27           C  
-ANISOU 2855  CA  LEU A 387     7370  11849   8622  -3607  -1464    128       C  
-ATOM   2856  C   LEU A 387     -12.840 -26.213  10.211  1.00 72.64           C  
-ANISOU 2856  C   LEU A 387     7359  11739   8503  -3452  -1549   -191       C  
-ATOM   2857  O   LEU A 387     -12.660 -26.443  11.403  1.00 74.03           O  
-ANISOU 2857  O   LEU A 387     7791  11628   8710  -3240  -1557   -369       O  
-ATOM   2858  CB  LEU A 387     -14.436 -27.402   8.684  1.00 71.40           C  
-ANISOU 2858  CB  LEU A 387     7097  11871   8159  -3697  -1500     61       C  
-ATOM   2859  CG  LEU A 387     -15.854 -27.569   8.137  1.00 70.34           C  
-ANISOU 2859  CG  LEU A 387     6918  11762   8046  -3836  -1421    349       C  
-ATOM   2860  CD1 LEU A 387     -15.990 -28.903   7.427  1.00 69.06           C  
-ANISOU 2860  CD1 LEU A 387     6786  11809   7646  -3880  -1461    232       C  
-ATOM   2861  CD2 LEU A 387     -16.877 -27.454   9.252  1.00 68.77           C  
-ANISOU 2861  CD2 LEU A 387     6942  11197   7989  -3715  -1332    450       C  
-ATOM   2862  N   ASN A 388     -11.846 -25.943   9.373  1.00 72.13           N  
-ANISOU 2862  N   ASN A 388     7067  11967   8373  -3562  -1612   -268       N  
-ATOM   2863  CA  ASN A 388     -10.467 -25.868   9.837  1.00 71.49           C  
-ANISOU 2863  CA  ASN A 388     7014  11887   8261  -3432  -1695   -572       C  
-ATOM   2864  C   ASN A 388     -10.331 -25.059  11.126  1.00 71.07           C  
-ANISOU 2864  C   ASN A 388     7113  11488   8401  -3264  -1668   -580       C  
-ATOM   2865  O   ASN A 388      -9.551 -25.415  12.010  1.00 71.36           O  
-ANISOU 2865  O   ASN A 388     7335  11372   8405  -3060  -1729   -873       O  
-ATOM   2866  CB  ASN A 388      -9.561 -25.301   8.741  1.00 69.99           C  
-ANISOU 2866  CB  ASN A 388     6513  12046   8035  -3616  -1736   -571       C  
-ATOM   2867  CG  ASN A 388      -8.639 -26.354   8.145  1.00 69.97           C  
-ANISOU 2867  CG  ASN A 388     6472  12315   7797  -3607  -1834   -882       C  
-ATOM   2868  OD1 ASN A 388      -9.082 -27.249   7.419  1.00 67.47           O  
-ANISOU 2868  OD1 ASN A 388     6139  12170   7326  -3686  -1843   -870       O  
-ATOM   2869  ND2 ASN A 388      -7.346 -26.248   8.445  1.00 69.34           N  
-ANISOU 2869  ND2 ASN A 388     6375  12279   7691  -3511  -1910  -1167       N  
-ATOM   2870  N   ARG A 389     -11.098 -23.977  11.230  1.00 73.23           N  
-ANISOU 2870  N   ARG A 389     7314  11635   8876  -3348  -1580   -260       N  
-ATOM   2871  CA  ARG A 389     -11.085 -23.153  12.433  1.00 73.34           C  
-ANISOU 2871  CA  ARG A 389     7467  11313   9084  -3200  -1545   -232       C  
-ATOM   2872  C   ARG A 389     -11.824 -23.835  13.577  1.00 74.39           C  
-ANISOU 2872  C   ARG A 389     7930  11102   9232  -3005  -1508   -297       C  
-ATOM   2873  O   ARG A 389     -11.331 -23.888  14.707  1.00 73.74           O  
-ANISOU 2873  O   ARG A 389     8066  10764   9189  -2798  -1535   -499       O  
-ATOM   2874  CB  ARG A 389     -11.708 -21.784  12.165  1.00 71.83           C  
-ANISOU 2874  CB  ARG A 389     7097  11096   9099  -3352  -1468    135       C  
-ATOM   2875  CG  ARG A 389     -11.737 -20.898  13.396  1.00 69.79           C  
-ANISOU 2875  CG  ARG A 389     6980  10490   9048  -3204  -1429    181       C  
-ATOM   2876  CD  ARG A 389     -12.181 -19.491  13.056  1.00 69.01           C  
-ANISOU 2876  CD  ARG A 389     6685  10396   9139  -3358  -1371    523       C  
-ATOM   2877  NE  ARG A 389     -12.000 -18.579  14.183  1.00 66.67           N  
-ANISOU 2877  NE  ARG A 389     6503   9797   9033  -3219  -1347    545       N  
-ATOM   2878  CZ  ARG A 389     -12.239 -17.273  14.133  1.00 66.18           C  
-ANISOU 2878  CZ  ARG A 389     6311   9685   9151  -3309  -1306    808       C  
-ATOM   2879  NH1 ARG A 389     -12.673 -16.721  13.006  1.00 67.71           N  
-ANISOU 2879  NH1 ARG A 389     6262  10108   9358  -3540  -1289   1069       N  
-ATOM   2880  NH2 ARG A 389     -12.047 -16.518  15.209  1.00 64.31           N  
-ANISOU 2880  NH2 ARG A 389     6195   9162   9076  -3168  -1288    809       N  
-ATOM   2881  N   LEU A 390     -13.012 -24.351  13.274  1.00 78.66           N  
-ANISOU 2881  N   LEU A 390     8509  11638   9740  -3079  -1446   -128       N  
-ATOM   2882  CA  LEU A 390     -13.830 -25.039  14.264  1.00 79.26           C  
-ANISOU 2882  CA  LEU A 390     8892  11407   9817  -2925  -1398   -173       C  
-ATOM   2883  C   LEU A 390     -13.105 -26.271  14.784  1.00 80.31           C  
-ANISOU 2883  C   LEU A 390     9270  11489   9756  -2741  -1486   -556       C  
-ATOM   2884  O   LEU A 390     -13.122 -26.556  15.980  1.00 80.54           O  
-ANISOU 2884  O   LEU A 390     9591  11200   9811  -2542  -1482   -706       O  
-ATOM   2885  CB  LEU A 390     -15.176 -25.441  13.662  1.00 79.12           C  
-ANISOU 2885  CB  LEU A 390     8835  11452   9774  -3064  -1322     62       C  
-ATOM   2886  CG  LEU A 390     -16.250 -25.900  14.651  1.00 80.34           C  
-ANISOU 2886  CG  LEU A 390     9275  11278   9974  -2947  -1240     92       C  
-ATOM   2887  CD1 LEU A 390     -16.517 -24.827  15.695  1.00 79.83           C  
-ANISOU 2887  CD1 LEU A 390     9291  10890  10149  -2855  -1172    217       C  
-ATOM   2888  CD2 LEU A 390     -17.529 -26.258  13.919  1.00 80.88           C  
-ANISOU 2888  CD2 LEU A 390     9262  11453  10015  -3105  -1168    324       C  
-ATOM   2889  N   ALA A 391     -12.460 -26.994  13.877  1.00 67.86           N  
-ANISOU 2889  N   ALA A 391     7577  10223   7982  -2807  -1569   -717       N  
-ATOM   2890  CA  ALA A 391     -11.720 -28.197  14.233  1.00 69.89           C  
-ANISOU 2890  CA  ALA A 391     8046  10473   8037  -2642  -1670  -1090       C  
-ATOM   2891  C   ALA A 391     -10.522 -27.879  15.114  1.00 70.17           C  
-ANISOU 2891  C   ALA A 391     8185  10360   8117  -2453  -1746  -1354       C  
-ATOM   2892  O   ALA A 391      -9.798 -28.778  15.533  1.00 70.80           O  
-ANISOU 2892  O   ALA A 391     8452  10402   8046  -2289  -1844  -1688       O  
-ATOM   2893  CB  ALA A 391     -11.268 -28.926  12.979  1.00 71.69           C  
-ANISOU 2893  CB  ALA A 391     8089  11093   8056  -2770  -1742  -1186       C  
-ATOM   2894  N   LYS A 392     -10.309 -26.597  15.386  1.00 86.48           N  
-ANISOU 2894  N   LYS A 392    10129  12342  10388  -2475  -1708  -1208       N  
-ATOM   2895  CA  LYS A 392      -9.191 -26.185  16.223  1.00 86.42           C  
-ANISOU 2895  CA  LYS A 392    10203  12190  10442  -2304  -1775  -1438       C  
-ATOM   2896  C   LYS A 392      -9.658 -25.918  17.648  1.00 85.74           C  
-ANISOU 2896  C   LYS A 392    10411  11664  10502  -2119  -1722  -1422       C  
-ATOM   2897  O   LYS A 392      -8.883 -26.046  18.593  1.00 84.64           O  
-ANISOU 2897  O   LYS A 392    10469  11325  10364  -1915  -1789  -1682       O  
-ATOM   2898  CB  LYS A 392      -8.500 -24.954  15.637  1.00 86.95           C  
-ANISOU 2898  CB  LYS A 392     9957  12451  10628  -2440  -1777  -1323       C  
-ATOM   2899  CG  LYS A 392      -7.026 -24.831  16.001  1.00 86.37           C  
-ANISOU 2899  CG  LYS A 392     9881  12406  10531  -2310  -1882  -1641       C  
-ATOM   2900  CD  LYS A 392      -6.351 -23.768  15.144  1.00 88.29           C  
-ANISOU 2900  CD  LYS A 392     9780  12922  10844  -2494  -1883  -1532       C  
-ATOM   2901  CE  LYS A 392      -4.865 -23.658  15.437  1.00 89.62           C  
-ANISOU 2901  CE  LYS A 392     9921  13145  10984  -2380  -1985  -1860       C  
-ATOM   2902  NZ  LYS A 392      -4.209 -22.654  14.558  1.00 90.08           N  
-ANISOU 2902  NZ  LYS A 392     9645  13485  11095  -2577  -1980  -1761       N  
-ATOM   2903  N   LYS A 393     -10.927 -25.548  17.796  1.00 78.00           N  
-ANISOU 2903  N   LYS A 393     9459  10533   9646  -2191  -1604  -1121       N  
-ATOM   2904  CA  LYS A 393     -11.526 -25.423  19.119  1.00 77.94           C  
-ANISOU 2904  CA  LYS A 393     9745  10107   9761  -2028  -1541  -1099       C  
-ATOM   2905  C   LYS A 393     -11.608 -26.784  19.800  1.00 79.29           C  
-ANISOU 2905  C   LYS A 393    10266  10103   9757  -1856  -1583  -1372       C  
-ATOM   2906  O   LYS A 393     -11.249 -26.922  20.970  1.00 79.06           O  
-ANISOU 2906  O   LYS A 393    10517   9770   9753  -1648  -1613  -1568       O  
-ATOM   2907  CB  LYS A 393     -12.920 -24.797  19.038  1.00 76.49           C  
-ANISOU 2907  CB  LYS A 393     9498   9828   9736  -2156  -1404   -722       C  
-ATOM   2908  CG  LYS A 393     -12.928 -23.280  18.985  1.00 76.19           C  
-ANISOU 2908  CG  LYS A 393     9247   9774   9929  -2242  -1353   -463       C  
-ATOM   2909  CD  LYS A 393     -14.331 -22.732  19.209  1.00 77.02           C  
-ANISOU 2909  CD  LYS A 393     9361   9701  10201  -2311  -1224   -136       C  
-ATOM   2910  CE  LYS A 393     -14.328 -21.212  19.269  1.00 77.69           C  
-ANISOU 2910  CE  LYS A 393     9266   9736  10517  -2374  -1182    110       C  
-ATOM   2911  NZ  LYS A 393     -13.448 -20.695  20.359  1.00 77.79           N  
-ANISOU 2911  NZ  LYS A 393     9426   9504  10625  -2188  -1219    -54       N  
-ATOM   2912  N   PHE A 394     -12.085 -27.785  19.065  1.00 83.36           N  
-ANISOU 2912  N   PHE A 394    10775  10806  10093  -1945  -1589  -1383       N  
-ATOM   2913  CA  PHE A 394     -12.192 -29.141  19.594  1.00 85.67           C  
-ANISOU 2913  CA  PHE A 394    11397  10961  10193  -1802  -1634  -1638       C  
-ATOM   2914  C   PHE A 394     -10.814 -29.700  19.890  1.00 88.53           C  
-ANISOU 2914  C   PHE A 394    11871  11348  10417  -1630  -1786  -2029       C  
-ATOM   2915  O   PHE A 394     -10.652 -30.589  20.727  1.00 88.02           O  
-ANISOU 2915  O   PHE A 394    12143  11064  10237  -1444  -1842  -2288       O  
-ATOM   2916  CB  PHE A 394     -12.900 -30.049  18.594  1.00 83.00           C  
-ANISOU 2916  CB  PHE A 394    10987  10867   9683  -1953  -1617  -1562       C  
-ATOM   2917  CG  PHE A 394     -14.338 -29.707  18.390  1.00 79.88           C  
-ANISOU 2917  CG  PHE A 394    10530  10420   9401  -2100  -1474  -1215       C  
-ATOM   2918  CD1 PHE A 394     -15.170 -29.503  19.473  1.00 78.64           C  
-ANISOU 2918  CD1 PHE A 394    10611   9897   9372  -2012  -1377  -1129       C  
-ATOM   2919  CD2 PHE A 394     -14.857 -29.578  17.116  1.00 78.93           C  
-ANISOU 2919  CD2 PHE A 394    10112  10614   9263  -2326  -1438   -980       C  
-ATOM   2920  CE1 PHE A 394     -16.499 -29.185  19.291  1.00 77.17           C  
-ANISOU 2920  CE1 PHE A 394    10359   9666   9295  -2145  -1246   -822       C  
-ATOM   2921  CE2 PHE A 394     -16.184 -29.258  16.926  1.00 77.40           C  
-ANISOU 2921  CE2 PHE A 394     9857  10372   9179  -2456  -1314   -670       C  
-ATOM   2922  CZ  PHE A 394     -17.007 -29.061  18.015  1.00 76.47           C  
-ANISOU 2922  CZ  PHE A 394     9969   9895   9190  -2364  -1217   -594       C  
-ATOM   2923  N   GLN A 395      -9.822 -29.167  19.189  1.00108.36           N  
-ANISOU 2923  N   GLN A 395    14100  14132  12941  -1697  -1853  -2075       N  
-ATOM   2924  CA  GLN A 395      -8.454 -29.639  19.323  1.00110.33           C  
-ANISOU 2924  CA  GLN A 395    14399  14458  13065  -1552  -2002  -2448       C  
-ATOM   2925  C   GLN A 395      -7.902 -29.372  20.716  1.00112.58           C  
-ANISOU 2925  C   GLN A 395    14952  14379  13446  -1312  -2041  -2641       C  
-ATOM   2926  O   GLN A 395      -7.466 -30.292  21.406  1.00112.38           O  
-ANISOU 2926  O   GLN A 395    15222  14193  13285  -1116  -2136  -2954       O  
-ATOM   2927  CB  GLN A 395      -7.555 -28.994  18.268  1.00111.25           C  
-ANISOU 2927  CB  GLN A 395    14132  14944  13194  -1697  -2047  -2434       C  
-ATOM   2928  CG  GLN A 395      -6.195 -29.639  18.203  1.00111.30           C  
-ANISOU 2928  CG  GLN A 395    14155  15094  13040  -1573  -2203  -2831       C  
-ATOM   2929  CD  GLN A 395      -6.285 -31.137  18.419  1.00111.76           C  
-ANISOU 2929  CD  GLN A 395    14498  15100  12867  -1443  -2283  -3089       C  
-ATOM   2930  OE1 GLN A 395      -5.639 -31.686  19.310  1.00113.63           O  
-ANISOU 2930  OE1 GLN A 395    15004  15135  13035  -1216  -2384  -3406       O  
-ATOM   2931  NE2 GLN A 395      -7.100 -31.805  17.607  1.00113.16           N  
-ANISOU 2931  NE2 GLN A 395    14626  15451  12919  -1587  -2241  -2953       N  
-ATOM   2932  N   ARG A 396      -7.924 -28.107  21.122  1.00 99.59           N  
-ANISOU 2932  N   ARG A 396    13210  12599  12031  -1328  -1973  -2453       N  
-ATOM   2933  CA  ARG A 396      -7.440 -27.715  22.441  1.00102.79           C  
-ANISOU 2933  CA  ARG A 396    13852  12650  12552  -1111  -2000  -2601       C  
-ATOM   2934  C   ARG A 396      -8.477 -27.990  23.532  1.00102.74           C  
-ANISOU 2934  C   ARG A 396    14198  12242  12597  -1003  -1917  -2530       C  
-ATOM   2935  O   ARG A 396      -8.474 -27.346  24.583  1.00102.39           O  
-ANISOU 2935  O   ARG A 396    14311  11879  12714   -879  -1884  -2510       O  
-ATOM   2936  CB  ARG A 396      -7.017 -26.240  22.445  1.00103.76           C  
-ANISOU 2936  CB  ARG A 396    13735  12791  12898  -1171  -1963  -2432       C  
-ATOM   2937  CG  ARG A 396      -7.904 -25.326  21.609  1.00106.88           C  
-ANISOU 2937  CG  ARG A 396    13836  13347  13425  -1419  -1837  -2018       C  
-ATOM   2938  CD  ARG A 396      -7.364 -23.899  21.568  1.00110.16           C  
-ANISOU 2938  CD  ARG A 396    14019  13799  14038  -1478  -1818  -1878       C  
-ATOM   2939  NE  ARG A 396      -7.508 -23.208  22.848  1.00112.83           N  
-ANISOU 2939  NE  ARG A 396    14564  13745  14563  -1324  -1774  -1834       N  
-ATOM   2940  CZ  ARG A 396      -8.488 -22.354  23.135  1.00114.10           C  
-ANISOU 2940  CZ  ARG A 396    14711  13732  14911  -1390  -1653  -1511       C  
-ATOM   2941  NH1 ARG A 396      -9.418 -22.078  22.230  1.00114.82           N  
-ANISOU 2941  NH1 ARG A 396    14591  14005  15030  -1604  -1567  -1204       N  
-ATOM   2942  NH2 ARG A 396      -8.536 -21.774  24.326  1.00115.45           N  
-ANISOU 2942  NH2 ARG A 396    15079  13544  15242  -1238  -1621  -1499       N  
-ATOM   2943  N   GLN A 397      -9.355 -28.958  23.274  1.00116.14           N  
-ANISOU 2943  N   GLN A 397    16019  13957  14151  -1054  -1881  -2497       N  
-ATOM   2944  CA  GLN A 397     -10.406 -29.330  24.215  1.00114.30           C  
-ANISOU 2944  CA  GLN A 397    16118  13370  13941   -976  -1792  -2436       C  
-ATOM   2945  C   GLN A 397     -11.101 -28.093  24.767  1.00113.54           C  
-ANISOU 2945  C   GLN A 397    15978  13050  14111  -1014  -1659  -2135       C  
-ATOM   2946  O   GLN A 397     -11.620 -28.105  25.881  1.00112.96           O  
-ANISOU 2946  O   GLN A 397    16201  12608  14110   -893  -1600  -2137       O  
-ATOM   2947  CB  GLN A 397      -9.838 -30.178  25.343  1.00113.30           C  
-ANISOU 2947  CB  GLN A 397    16403  12949  13698   -721  -1893  -2798       C  
-ATOM   2948  N   ALA A 398     -11.110 -27.028  23.974  1.00 97.94           N  
-ANISOU 2948  N   ALA A 398    13636  11299  12276  -1184  -1613  -1878       N  
-ATOM   2949  CA  ALA A 398     -11.712 -25.767  24.387  1.00 96.26           C  
-ANISOU 2949  CA  ALA A 398    13344  10910  12319  -1230  -1497  -1583       C  
-ATOM   2950  C   ALA A 398     -12.901 -25.403  23.504  1.00 95.57           C  
-ANISOU 2950  C   ALA A 398    13021  10992  12298  -1460  -1380  -1220       C  
-ATOM   2951  O   ALA A 398     -12.839 -24.456  22.721  1.00 96.23           O  
-ANISOU 2951  O   ALA A 398    12781  11292  12491  -1616  -1358  -1002       O  
-ATOM   2952  CB  ALA A 398     -10.672 -24.659  24.364  1.00 97.56           C  
-ANISOU 2952  CB  ALA A 398    13306  11143  12619  -1216  -1549  -1587       C  
-ATOM   2953  N   ALA A 399     -13.983 -26.163  23.634  1.00 91.71           N  
-ANISOU 2953  N   ALA A 399    12704  10401  11740  -1483  -1306  -1163       N  
-ATOM   2954  CA  ALA A 399     -15.196 -25.911  22.867  1.00 90.88           C  
-ANISOU 2954  CA  ALA A 399    12403  10433  11696  -1688  -1195   -836       C  
-ATOM   2955  C   ALA A 399     -16.435 -26.165  23.719  1.00 89.97           C  
-ANISOU 2955  C   ALA A 399    12547   9997  11640  -1645  -1074   -740       C  
-ATOM   2956  O   ALA A 399     -16.412 -26.980  24.641  1.00 90.38           O  
-ANISOU 2956  O   ALA A 399    12949   9796  11597  -1486  -1088   -965       O  
-ATOM   2957  CB  ALA A 399     -15.222 -26.774  21.614  1.00 90.26           C  
-ANISOU 2957  CB  ALA A 399    12163  10721  11412  -1831  -1241   -863       C  
-ATOM   2958  N   ASN A 400     -17.516 -25.461  23.409  1.00105.55           N  
-ANISOU 2958  N   ASN A 400    14352  11983  13770  -1789   -957   -412       N  
-ATOM   2959  CA  ASN A 400     -18.752 -25.597  24.167  1.00105.14           C  
-ANISOU 2959  CA  ASN A 400    14510  11644  13796  -1769   -829   -301       C  
-ATOM   2960  C   ASN A 400     -19.847 -26.271  23.356  1.00105.71           C  
-ANISOU 2960  C   ASN A 400    14501  11891  13772  -1932   -764   -163       C  
-ATOM   2961  O   ASN A 400     -19.647 -26.617  22.193  1.00105.43           O  
-ANISOU 2961  O   ASN A 400    14247  12198  13612  -2061   -820   -144       O  
-ATOM   2962  CB  ASN A 400     -19.230 -24.233  24.674  1.00104.61           C  
-ANISOU 2962  CB  ASN A 400    14354  11385  14007  -1777   -737    -45       C  
-ATOM   2963  CG  ASN A 400     -19.370 -23.209  23.559  1.00104.68           C  
-ANISOU 2963  CG  ASN A 400    13955  11683  14136  -1968   -729    246       C  
-ATOM   2964  OD1 ASN A 400     -20.348 -23.221  22.812  1.00104.32           O  
-ANISOU 2964  OD1 ASN A 400    13745  11787  14105  -2130   -664    463       O  
-ATOM   2965  ND2 ASN A 400     -18.394 -22.311  23.449  1.00103.90           N  
-ANISOU 2965  ND2 ASN A 400    13698  11657  14123  -1951   -797    250       N  
-ATOM   2966  N   LEU A 401     -21.004 -26.453  23.980  1.00105.66           N  
-ANISOU 2966  N   LEU A 401    14673  11648  13826  -1929   -643    -72       N  
-ATOM   2967  CA  LEU A 401     -22.125 -27.113  23.330  1.00107.22           C  
-ANISOU 2967  CA  LEU A 401    14821  11977  13941  -2076   -570     52       C  
-ATOM   2968  C   LEU A 401     -22.532 -26.379  22.058  1.00109.21           C  
-ANISOU 2968  C   LEU A 401    14661  12548  14285  -2284   -554    350       C  
-ATOM   2969  O   LEU A 401     -22.877 -27.004  21.057  1.00110.57           O  
-ANISOU 2969  O   LEU A 401    14700  12987  14323  -2420   -566    396       O  
-ATOM   2970  CB  LEU A 401     -23.312 -27.205  24.287  1.00106.72           C  
-ANISOU 2970  CB  LEU A 401    14992  11586  13969  -2042   -428    120       C  
-ATOM   2971  CG  LEU A 401     -24.196 -28.438  24.103  1.00107.93           C  
-ANISOU 2971  CG  LEU A 401    15300  11765  13944  -2106   -374     66       C  
-ATOM   2972  CD1 LEU A 401     -23.358 -29.700  24.239  1.00107.67           C  
-ANISOU 2972  CD1 LEU A 401    15520  11749  13640  -1998   -484   -272       C  
-ATOM   2973  CD2 LEU A 401     -25.346 -28.440  25.100  1.00107.32           C  
-ANISOU 2973  CD2 LEU A 401    15450  11355  13971  -2079   -224    129       C  
-ATOM   2974  N   GLN A 402     -22.488 -25.052  22.101  1.00 98.95           N  
-ANISOU 2974  N   GLN A 402    13171  11216  13211  -2309   -531    553       N  
-ATOM   2975  CA  GLN A 402     -22.859 -24.241  20.945  1.00101.81           C  
-ANISOU 2975  CA  GLN A 402    13156  11855  13672  -2503   -522    844       C  
-ATOM   2976  C   GLN A 402     -21.965 -24.540  19.749  1.00102.29           C  
-ANISOU 2976  C   GLN A 402    13002  12294  13571  -2599   -639    776       C  
-ATOM   2977  O   GLN A 402     -22.422 -24.535  18.608  1.00103.24           O  
-ANISOU 2977  O   GLN A 402    12875  12690  13660  -2777   -637    950       O  
-ATOM   2978  CB  GLN A 402     -22.802 -22.751  21.285  1.00102.54           C  
-ANISOU 2978  CB  GLN A 402    13112  11827  14020  -2493   -495   1043       C  
-ATOM   2979  CG  GLN A 402     -22.985 -21.833  20.087  1.00104.45           C  
-ANISOU 2979  CG  GLN A 402    12975  12356  14357  -2685   -510   1324       C  
-ATOM   2980  CD  GLN A 402     -22.860 -20.370  20.457  1.00104.08           C  
-ANISOU 2980  CD  GLN A 402    12815  12181  14549  -2667   -494   1505       C  
-ATOM   2981  OE1 GLN A 402     -23.150 -19.978  21.588  1.00103.00           O  
-ANISOU 2981  OE1 GLN A 402    12862  11720  14554  -2540   -430   1507       O  
-ATOM   2982  NE2 GLN A 402     -22.417 -19.553  19.505  1.00104.77           N  
-ANISOU 2982  NE2 GLN A 402    12609  12521  14678  -2796   -554   1656       N  
-ATOM   2983  N   ASP A 403     -20.691 -24.802  20.017  1.00103.67           N  
-ANISOU 2983  N   ASP A 403    13270  12477  13642  -2478   -742    515       N  
-ATOM   2984  CA  ASP A 403     -19.747 -25.123  18.956  1.00103.41           C  
-ANISOU 2984  CA  ASP A 403    13047  12796  13449  -2556   -855    413       C  
-ATOM   2985  C   ASP A 403     -20.161 -26.402  18.236  1.00102.49           C  
-ANISOU 2985  C   ASP A 403    12958  12873  13109  -2636   -867    340       C  
-ATOM   2986  O   ASP A 403     -20.061 -26.500  17.013  1.00101.82           O  
-ANISOU 2986  O   ASP A 403    12623  13124  12940  -2794   -909    422       O  
-ATOM   2987  CB  ASP A 403     -18.331 -25.256  19.517  1.00107.12           C  
-ANISOU 2987  CB  ASP A 403    13647  13207  13848  -2389   -962    110       C  
-ATOM   2988  CG  ASP A 403     -17.850 -23.984  20.187  1.00109.27           C  
-ANISOU 2988  CG  ASP A 403    13883  13302  14334  -2314   -956    177       C  
-ATOM   2989  OD1 ASP A 403     -18.533 -22.946  20.053  1.00111.86           O  
-ANISOU 2989  OD1 ASP A 403    14046  13599  14855  -2411   -880    470       O  
-ATOM   2990  OD2 ASP A 403     -16.787 -24.019  20.842  1.00111.89           O  
-ANISOU 2990  OD2 ASP A 403    14351  13525  14638  -2156  -1032    -65       O  
-ATOM   2991  N   CYS A 404     -20.633 -27.379  19.003  1.00 75.54           N  
-ANISOU 2991  N   CYS A 404     9859   9245   9599  -2529   -831    187       N  
-ATOM   2992  CA  CYS A 404     -21.101 -28.633  18.431  1.00 75.78           C  
-ANISOU 2992  CA  CYS A 404     9952   9426   9415  -2595   -835    116       C  
-ATOM   2993  C   CYS A 404     -22.335 -28.406  17.564  1.00 76.14           C  
-ANISOU 2993  C   CYS A 404     9774   9627   9528  -2797   -746    426       C  
-ATOM   2994  O   CYS A 404     -22.517 -29.074  16.550  1.00 76.24           O  
-ANISOU 2994  O   CYS A 404     9665   9912   9389  -2922   -775    447       O  
-ATOM   2995  CB  CYS A 404     -21.396 -29.655  19.532  1.00 75.07           C  
-ANISOU 2995  CB  CYS A 404    10271   9037   9214  -2440   -807   -106       C  
-ATOM   2996  SG  CYS A 404     -19.941 -30.191  20.473  1.00 73.05           S  
-ANISOU 2996  SG  CYS A 404    10313   8614   8828  -2194   -936   -515       S  
-ATOM   2997  N   TYR A 405     -23.176 -27.456  17.961  1.00109.63           N  
-ANISOU 2997  N   TYR A 405    13961  13694  14000  -2826   -644    664       N  
-ATOM   2998  CA  TYR A 405     -24.381 -27.138  17.203  1.00111.20           C  
-ANISOU 2998  CA  TYR A 405    13945  14016  14289  -3007   -562    962       C  
-ATOM   2999  C   TYR A 405     -24.035 -26.497  15.864  1.00108.70           C  
-ANISOU 2999  C   TYR A 405    13258  14052  13991  -3178   -626   1139       C  
-ATOM   3000  O   TYR A 405     -24.609 -26.841  14.832  1.00108.39           O  
-ANISOU 3000  O   TYR A 405    13051  14253  13880  -3336   -621   1268       O  
-ATOM   3001  CB  TYR A 405     -25.296 -26.214  18.007  1.00116.36           C  
-ANISOU 3001  CB  TYR A 405    14630  14388  15193  -2981   -446   1158       C  
-ATOM   3002  CG  TYR A 405     -26.578 -25.850  17.290  1.00123.19           C  
-ANISOU 3002  CG  TYR A 405    15278  15362  16168  -3154   -365   1457       C  
-ATOM   3003  CD1 TYR A 405     -27.613 -26.768  17.173  1.00125.53           C  
-ANISOU 3003  CD1 TYR A 405    15666  15658  16372  -3212   -294   1465       C  
-ATOM   3004  CD2 TYR A 405     -26.756 -24.586  16.736  1.00127.82           C  
-ANISOU 3004  CD2 TYR A 405    15573  16046  16946  -3259   -365   1727       C  
-ATOM   3005  CE1 TYR A 405     -28.786 -26.443  16.521  1.00129.85           C  
-ANISOU 3005  CE1 TYR A 405    16010  16305  17022  -3366   -224   1729       C  
-ATOM   3006  CE2 TYR A 405     -27.928 -24.252  16.083  1.00132.07           C  
-ANISOU 3006  CE2 TYR A 405    15917  16678  17584  -3409   -302   1992       C  
-ATOM   3007  CZ  TYR A 405     -28.940 -25.185  15.979  1.00132.24           C  
-ANISOU 3007  CZ  TYR A 405    16025  16701  17519  -3460   -232   1990       C  
-ATOM   3008  OH  TYR A 405     -30.112 -24.863  15.330  1.00134.69           O  
-ANISOU 3008  OH  TYR A 405    16138  17105  17933  -3605   -174   2244       O  
-ATOM   3009  N   ARG A 406     -23.099 -25.555  15.892  1.00100.86           N  
-ANISOU 3009  N   ARG A 406    12145  13083  13095  -3149   -684   1145       N  
-ATOM   3010  CA  ARG A 406     -22.611 -24.920  14.676  1.00 96.39           C  
-ANISOU 3010  CA  ARG A 406    11248  12840  12534  -3308   -750   1284       C  
-ATOM   3011  C   ARG A 406     -22.038 -25.967  13.724  1.00 93.12           C  
-ANISOU 3011  C   ARG A 406    10779  12736  11867  -3376   -836   1124       C  
-ATOM   3012  O   ARG A 406     -22.262 -25.905  12.514  1.00 92.71           O  
-ANISOU 3012  O   ARG A 406    10480  12972  11772  -3557   -855   1281       O  
-ATOM   3013  CB  ARG A 406     -21.562 -23.861  15.018  1.00 98.05           C  
-ANISOU 3013  CB  ARG A 406    11391  13000  12863  -3243   -801   1257       C  
-ATOM   3014  CG  ARG A 406     -22.139 -22.638  15.712  1.00100.63           C  
-ANISOU 3014  CG  ARG A 406    11704  13078  13453  -3215   -725   1472       C  
-ATOM   3015  CD  ARG A 406     -21.249 -22.137  16.846  1.00103.36           C  
-ANISOU 3015  CD  ARG A 406    12213  13175  13884  -3030   -747   1313       C  
-ATOM   3016  NE  ARG A 406     -19.955 -21.642  16.381  1.00105.02           N  
-ANISOU 3016  NE  ARG A 406    12265  13576  14062  -3053   -846   1233       N  
-ATOM   3017  CZ  ARG A 406     -19.050 -21.066  17.167  1.00105.12           C  
-ANISOU 3017  CZ  ARG A 406    12359  13430  14152  -2920   -880   1112       C  
-ATOM   3018  NH1 ARG A 406     -19.299 -20.906  18.461  1.00103.84           N  
-ANISOU 3018  NH1 ARG A 406    12440  12908  14105  -2751   -826   1063       N  
-ATOM   3019  NH2 ARG A 406     -17.899 -20.645  16.660  1.00105.93           N  
-ANISOU 3019  NH2 ARG A 406    12299  13731  14217  -2959   -966   1037       N  
-ATOM   3020  N   LEU A 407     -21.305 -26.930  14.279  1.00 71.37           N  
-ANISOU 3020  N   LEU A 407     8262   9913   8944  -3227   -892    808       N  
-ATOM   3021  CA  LEU A 407     -20.797 -28.056  13.501  1.00 68.48           C  
-ANISOU 3021  CA  LEU A 407     7886   9811   8324  -3267   -974    626       C  
-ATOM   3022  C   LEU A 407     -21.953 -28.914  13.002  1.00 70.58           C  
-ANISOU 3022  C   LEU A 407     8174  10151   8491  -3369   -917    725       C  
-ATOM   3023  O   LEU A 407     -21.973 -29.340  11.847  1.00 71.59           O  
-ANISOU 3023  O   LEU A 407     8126  10585   8491  -3514   -956    774       O  
-ATOM   3024  CB  LEU A 407     -19.834 -28.899  14.341  1.00 61.12           C  
-ANISOU 3024  CB  LEU A 407     7237   8746   7241  -3063  -1049    258       C  
-ATOM   3025  CG  LEU A 407     -19.388 -30.247  13.765  1.00 56.48           C  
-ANISOU 3025  CG  LEU A 407     6715   8371   6374  -3063  -1135     27       C  
-ATOM   3026  CD1 LEU A 407     -18.958 -30.124  12.314  1.00 57.13           C  
-ANISOU 3026  CD1 LEU A 407     6469   8860   6379  -3247  -1196    111       C  
-ATOM   3027  CD2 LEU A 407     -18.263 -30.842  14.608  1.00 56.17           C  
-ANISOU 3027  CD2 LEU A 407     6930   8198   6215  -2850  -1229   -340       C  
-ATOM   3028  N   TYR A 408     -22.917 -29.155  13.885  1.00 83.76           N  
-ANISOU 3028  N   TYR A 408    10063  11539  10223  -3297   -821    753       N  
-ATOM   3029  CA  TYR A 408     -24.124 -29.892  13.534  1.00 86.38           C  
-ANISOU 3029  CA  TYR A 408    10428  11906  10487  -3393   -750    857       C  
-ATOM   3030  C   TYR A 408     -24.847 -29.198  12.387  1.00 87.41           C  
-ANISOU 3030  C   TYR A 408    10222  12266  10724  -3605   -719   1181       C  
-ATOM   3031  O   TYR A 408     -25.058 -29.785  11.326  1.00 87.08           O  
-ANISOU 3031  O   TYR A 408    10048  12494  10545  -3739   -748   1228       O  
-ATOM   3032  CB  TYR A 408     -25.044 -30.004  14.751  1.00 86.96           C  
-ANISOU 3032  CB  TYR A 408    10770  11615  10655  -3289   -637    856       C  
-ATOM   3033  CG  TYR A 408     -26.312 -30.786  14.502  1.00 88.57           C  
-ANISOU 3033  CG  TYR A 408    11030  11832  10791  -3381   -553    944       C  
-ATOM   3034  CD1 TYR A 408     -27.527 -30.137  14.320  1.00 89.66           C  
-ANISOU 3034  CD1 TYR A 408    11020  11935  11112  -3494   -449   1227       C  
-ATOM   3035  CD2 TYR A 408     -26.295 -32.175  14.451  1.00 88.78           C  
-ANISOU 3035  CD2 TYR A 408    11260  11905  10567  -3354   -581    736       C  
-ATOM   3036  CE1 TYR A 408     -28.688 -30.848  14.092  1.00 90.39           C  
-ANISOU 3036  CE1 TYR A 408    11155  12044  11146  -3581   -371   1300       C  
-ATOM   3037  CE2 TYR A 408     -27.450 -32.896  14.223  1.00 89.78           C  
-ANISOU 3037  CE2 TYR A 408    11441  12046  10627  -3444   -501    813       C  
-ATOM   3038  CZ  TYR A 408     -28.644 -32.227  14.044  1.00 90.86           C  
-ANISOU 3038  CZ  TYR A 408    11417  12151  10953  -3559   -394   1094       C  
-ATOM   3039  OH  TYR A 408     -29.799 -32.942  13.816  1.00 91.41           O  
-ANISOU 3039  OH  TYR A 408    11533  12240  10960  -3652   -313   1163       O  
-ATOM   3040  N   GLN A 409     -25.220 -27.942  12.609  1.00 91.12           N  
-ANISOU 3040  N   GLN A 409    10562  12622  11438  -3631   -666   1403       N  
-ATOM   3041  CA  GLN A 409     -25.879 -27.145  11.584  1.00 92.93           C  
-ANISOU 3041  CA  GLN A 409    10480  13042  11788  -3822   -646   1716       C  
-ATOM   3042  C   GLN A 409     -25.205 -27.330  10.240  1.00 91.99           C  
-ANISOU 3042  C   GLN A 409    10130  13299  11523  -3963   -744   1722       C  
-ATOM   3043  O   GLN A 409     -25.869 -27.529   9.224  1.00 91.74           O  
-ANISOU 3043  O   GLN A 409     9929  13478  11450  -4125   -737   1886       O  
-ATOM   3044  CB  GLN A 409     -25.877 -25.668  11.971  1.00 97.49           C  
-ANISOU 3044  CB  GLN A 409    10943  13477  12623  -3809   -621   1899       C  
-ATOM   3045  CG  GLN A 409     -26.887 -25.340  13.039  1.00104.87           C  
-ANISOU 3045  CG  GLN A 409    12030  14079  13735  -3725   -507   1984       C  
-ATOM   3046  CD  GLN A 409     -28.274 -25.814  12.662  1.00110.17           C  
-ANISOU 3046  CD  GLN A 409    12672  14780  14407  -3830   -427   2133       C  
-ATOM   3047  OE1 GLN A 409     -28.892 -25.285  11.737  1.00114.89           O  
-ANISOU 3047  OE1 GLN A 409    13018  15550  15086  -3987   -424   2380       O  
-ATOM   3048  NE2 GLN A 409     -28.766 -26.829  13.365  1.00111.25           N  
-ANISOU 3048  NE2 GLN A 409    13072  14750  14449  -3746   -365   1978       N  
-ATOM   3049  N   GLY A 410     -23.878 -27.271  10.244  1.00103.32           N  
-ANISOU 3049  N   GLY A 410    11561  14816  12879  -3902   -833   1535       N  
-ATOM   3050  CA  GLY A 410     -23.108 -27.473   9.034  1.00101.30           C  
-ANISOU 3050  CA  GLY A 410    11100  14914  12475  -4028   -926   1503       C  
-ATOM   3051  C   GLY A 410     -23.401 -28.806   8.372  1.00100.57           C  
-ANISOU 3051  C   GLY A 410    11051  15007  12153  -4086   -946   1413       C  
-ATOM   3052  O   GLY A 410     -23.881 -28.855   7.240  1.00102.03           O  
-ANISOU 3052  O   GLY A 410    11033  15434  12300  -4264   -950   1589       O  
-ATOM   3053  N   ILE A 411     -23.124 -29.893   9.084  1.00 69.18           N  
-ANISOU 3053  N   ILE A 411     7352  10911   8022  -3936   -962   1139       N  
-ATOM   3054  CA  ILE A 411     -23.234 -31.230   8.511  1.00 68.98           C  
-ANISOU 3054  CA  ILE A 411     7395  11060   7753  -3972   -996   1013       C  
-ATOM   3055  C   ILE A 411     -24.666 -31.599   8.140  1.00 72.29           C  
-ANISOU 3055  C   ILE A 411     7797  11488   8183  -4086   -911   1216       C  
-ATOM   3056  O   ILE A 411     -24.906 -32.611   7.482  1.00 73.47           O  
-ANISOU 3056  O   ILE A 411     7958  11814   8144  -4154   -933   1170       O  
-ATOM   3057  CB  ILE A 411     -22.628 -32.287   9.453  1.00 63.44           C  
-ANISOU 3057  CB  ILE A 411     7025  10195   6883  -3772  -1038    665       C  
-ATOM   3058  CG1 ILE A 411     -21.127 -32.048   9.584  1.00 61.47           C  
-ANISOU 3058  CG1 ILE A 411     6755  10008   6591  -3677  -1143    444       C  
-ATOM   3059  CG2 ILE A 411     -22.886 -33.692   8.936  1.00 61.42           C  
-ANISOU 3059  CG2 ILE A 411     6869  10091   6376  -3806  -1066    547       C  
-ATOM   3060  CD1 ILE A 411     -20.482 -32.850  10.669  1.00 57.62           C  
-ANISOU 3060  CD1 ILE A 411     6600   9309   5984  -3456  -1190    108       C  
-ATOM   3061  N   ASN A 412     -25.620 -30.773   8.550  1.00 91.60           N  
-ANISOU 3061  N   ASN A 412    10208  13747  10850  -4107   -815   1439       N  
-ATOM   3062  CA  ASN A 412     -27.005 -31.012   8.175  1.00 94.85           C  
-ANISOU 3062  CA  ASN A 412    10574  14171  11295  -4221   -733   1642       C  
-ATOM   3063  C   ASN A 412     -27.311 -30.471   6.787  1.00 95.15           C  
-ANISOU 3063  C   ASN A 412    10275  14503  11374  -4433   -759   1903       C  
-ATOM   3064  O   ASN A 412     -28.432 -30.587   6.296  1.00 95.09           O  
-ANISOU 3064  O   ASN A 412    10182  14545  11401  -4547   -704   2092       O  
-ATOM   3065  CB  ASN A 412     -27.968 -30.429   9.207  1.00 97.57           C  
-ANISOU 3065  CB  ASN A 412    11028  14189  11854  -4153   -618   1757       C  
-ATOM   3066  CG  ASN A 412     -29.032 -31.422   9.626  1.00 99.88           C  
-ANISOU 3066  CG  ASN A 412    11528  14351  12069  -4136   -533   1715       C  
-ATOM   3067  OD1 ASN A 412     -28.845 -32.177  10.580  1.00100.15           O  
-ANISOU 3067  OD1 ASN A 412    11865  14186  12003  -3992   -516   1483       O  
-ATOM   3068  ND2 ASN A 412     -30.150 -31.438   8.906  1.00102.44           N  
-ANISOU 3068  ND2 ASN A 412    11698  14789  12437  -4286   -480   1933       N  
-ATOM   3069  N   GLN A 413     -26.302 -29.879   6.157  1.00 97.62           N  
-ANISOU 3069  N   GLN A 413    10402  15008  11682  -4487   -843   1907       N  
-ATOM   3070  CA  GLN A 413     -26.437 -29.398   4.792  1.00 96.05           C  
-ANISOU 3070  CA  GLN A 413     9898  15101  11496  -4694   -880   2131       C  
-ATOM   3071  C   GLN A 413     -25.781 -30.372   3.828  1.00 94.91           C  
-ANISOU 3071  C   GLN A 413     9703  15261  11098  -4767   -963   1991       C  
-ATOM   3072  O   GLN A 413     -26.042 -30.346   2.625  1.00 95.67           O  
-ANISOU 3072  O   GLN A 413     9586  15614  11149  -4945   -990   2153       O  
-ATOM   3073  CB  GLN A 413     -25.821 -28.010   4.648  1.00 97.36           C  
-ANISOU 3073  CB  GLN A 413     9877  15287  11829  -4734   -911   2254       C  
-ATOM   3074  CG  GLN A 413     -26.489 -26.958   5.507  1.00 99.11           C  
-ANISOU 3074  CG  GLN A 413    10125  15224  12310  -4673   -835   2418       C  
-ATOM   3075  CD  GLN A 413     -27.974 -26.830   5.229  1.00100.79           C  
-ANISOU 3075  CD  GLN A 413    10264  15397  12633  -4769   -761   2670       C  
-ATOM   3076  OE1 GLN A 413     -28.537 -27.580   4.432  1.00 99.47           O  
-ANISOU 3076  OE1 GLN A 413    10041  15406  12347  -4876   -763   2718       O  
-ATOM   3077  NE2 GLN A 413     -28.617 -25.873   5.886  1.00102.98           N  
-ANISOU 3077  NE2 GLN A 413    10539  15445  13143  -4728   -698   2828       N  
-ATOM   3078  N   LEU A 414     -24.935 -31.240   4.370  1.00 80.44           N  
-ANISOU 3078  N   LEU A 414     8073  13393   9096  -4625  -1009   1685       N  
-ATOM   3079  CA  LEU A 414     -24.271 -32.267   3.576  1.00 80.93           C  
-ANISOU 3079  CA  LEU A 414     8119  13725   8904  -4668  -1092   1513       C  
-ATOM   3080  C   LEU A 414     -25.247 -33.008   2.658  1.00 82.00           C  
-ANISOU 3080  C   LEU A 414     8189  14034   8935  -4812  -1071   1651       C  
-ATOM   3081  O   LEU A 414     -24.923 -33.277   1.503  1.00 84.44           O  
-ANISOU 3081  O   LEU A 414     8324  14642   9116  -4948  -1132   1679       O  
-ATOM   3082  CB  LEU A 414     -23.518 -33.244   4.482  1.00 77.43           C  
-ANISOU 3082  CB  LEU A 414     7967  13155   8299  -4468  -1133   1162       C  
-ATOM   3083  CG  LEU A 414     -22.072 -33.538   4.078  1.00 75.72           C  
-ANISOU 3083  CG  LEU A 414     7701  13150   7921  -4442  -1249    923       C  
-ATOM   3084  CD1 LEU A 414     -21.363 -32.260   3.654  1.00 73.36           C  
-ANISOU 3084  CD1 LEU A 414     7148  12962   7764  -4525  -1276   1034       C  
-ATOM   3085  CD2 LEU A 414     -21.321 -34.224   5.212  1.00 72.91           C  
-ANISOU 3085  CD2 LEU A 414     7644  12596   7463  -4212  -1291    583       C  
-ATOM   3086  N   PRO A 415     -26.445 -33.343   3.167  1.00 92.88           N  
-ANISOU 3086  N   PRO A 415     9702  15223  10364  -4787   -982   1733       N  
-ATOM   3087  CA  PRO A 415     -27.457 -33.921   2.277  1.00 92.18           C  
-ANISOU 3087  CA  PRO A 415     9527  15295  10203  -4935   -956   1892       C  
-ATOM   3088  C   PRO A 415     -27.873 -32.933   1.191  1.00 91.52           C  
-ANISOU 3088  C   PRO A 415     9123  15392  10257  -5130   -959   2202       C  
-ATOM   3089  O   PRO A 415     -27.761 -33.252   0.010  1.00 91.31           O  
-ANISOU 3089  O   PRO A 415     8935  15651  10109  -5275  -1013   2263       O  
-ATOM   3090  CB  PRO A 415     -28.637 -34.191   3.216  1.00 92.97           C  
-ANISOU 3090  CB  PRO A 415     9826  15111  10386  -4861   -846   1927       C  
-ATOM   3091  CG  PRO A 415     -28.034 -34.302   4.567  1.00 92.79           C  
-ANISOU 3091  CG  PRO A 415    10073  14816  10367  -4652   -837   1686       C  
-ATOM   3092  CD  PRO A 415     -26.888 -33.338   4.572  1.00 92.04           C  
-ANISOU 3092  CD  PRO A 415     9852  14759  10359  -4621   -903   1656       C  
-ATOM   3093  N   ASN A 416     -28.347 -31.754   1.590  1.00 88.29           N  
-ANISOU 3093  N   ASN A 416     8635  14814  10097  -5132   -906   2393       N  
-ATOM   3094  CA  ASN A 416     -28.757 -30.726   0.636  1.00 87.62           C  
-ANISOU 3094  CA  ASN A 416     8266  14870  10156  -5307   -915   2689       C  
-ATOM   3095  C   ASN A 416     -27.731 -30.530  -0.471  1.00 87.93           C  
-ANISOU 3095  C   ASN A 416     8108  15213  10087  -5430  -1014   2683       C  
-ATOM   3096  O   ASN A 416     -28.085 -30.294  -1.624  1.00 88.16           O  
-ANISOU 3096  O   ASN A 416     7927  15456  10113  -5610  -1040   2882       O  
-ATOM   3097  CB  ASN A 416     -28.995 -29.392   1.345  1.00 88.82           C  
-ANISOU 3097  CB  ASN A 416     8380  14792  10575  -5259   -870   2834       C  
-ATOM   3098  CG  ASN A 416     -30.461 -29.125   1.607  1.00 90.44           C  
-ANISOU 3098  CG  ASN A 416     8581  14832  10949  -5281   -780   3040       C  
-ATOM   3099  OD1 ASN A 416     -31.333 -29.656   0.921  1.00 91.94           O  
-ANISOU 3099  OD1 ASN A 416     8707  15141  11086  -5388   -764   3150       O  
-ATOM   3100  ND2 ASN A 416     -30.741 -28.287   2.598  1.00 92.17           N  
-ANISOU 3100  ND2 ASN A 416     8863  14780  11377  -5180   -722   3091       N  
-ATOM   3101  N   VAL A 417     -26.456 -30.632  -0.107  1.00 77.33           N  
-ANISOU 3101  N   VAL A 417     6839  13887   8657  -5332  -1067   2446       N  
-ATOM   3102  CA  VAL A 417     -25.360 -30.439  -1.050  1.00 78.42           C  
-ANISOU 3102  CA  VAL A 417     6801  14305   8691  -5438  -1156   2402       C  
-ATOM   3103  C   VAL A 417     -25.156 -31.660  -1.940  1.00 80.00           C  
-ANISOU 3103  C   VAL A 417     6992  14770   8636  -5511  -1208   2289       C  
-ATOM   3104  O   VAL A 417     -25.276 -31.566  -3.161  1.00 81.42           O  
-ANISOU 3104  O   VAL A 417     6968  15202   8766  -5696  -1241   2443       O  
-ATOM   3105  CB  VAL A 417     -24.040 -30.102  -0.322  1.00 76.00           C  
-ANISOU 3105  CB  VAL A 417     6568  13922   8385  -5303  -1196   2172       C  
-ATOM   3106  CG1 VAL A 417     -22.876 -30.141  -1.295  1.00 76.52           C  
-ANISOU 3106  CG1 VAL A 417     6471  14297   8306  -5409  -1284   2075       C  
-ATOM   3107  CG2 VAL A 417     -24.136 -28.741   0.350  1.00 75.36           C  
-ANISOU 3107  CG2 VAL A 417     6451  13625   8558  -5264  -1156   2314       C  
-ATOM   3108  N   ILE A 418     -24.848 -32.804  -1.334  1.00 89.84           N  
-ANISOU 3108  N   ILE A 418     8465  15955   9715  -5366  -1219   2020       N  
-ATOM   3109  CA  ILE A 418     -24.664 -34.033  -2.100  1.00 94.19           C  
-ANISOU 3109  CA  ILE A 418     9032  16743  10013  -5418  -1272   1897       C  
-ATOM   3110  C   ILE A 418     -25.869 -34.250  -3.007  1.00 99.95           C  
-ANISOU 3110  C   ILE A 418     9644  17590  10741  -5584  -1238   2150       C  
-ATOM   3111  O   ILE A 418     -25.790 -34.938  -4.021  1.00100.49           O  
-ANISOU 3111  O   ILE A 418     9629  17917  10637  -5698  -1285   2148       O  
-ATOM   3112  CB  ILE A 418     -24.467 -35.260  -1.191  1.00 90.66           C  
-ANISOU 3112  CB  ILE A 418     8887  16156   9402  -5229  -1278   1602       C  
-ATOM   3113  CG1 ILE A 418     -23.210 -35.094  -0.333  1.00 89.19           C  
-ANISOU 3113  CG1 ILE A 418     8818  15863   9207  -5058  -1326   1332       C  
-ATOM   3114  CG2 ILE A 418     -24.362 -36.527  -2.023  1.00 88.11           C  
-ANISOU 3114  CG2 ILE A 418     8580  16079   8817  -5289  -1334   1493       C  
-ATOM   3115  CD1 ILE A 418     -22.885 -36.307   0.519  1.00 87.28           C  
-ANISOU 3115  CD1 ILE A 418     8884  15494   8786  -4868  -1353   1018       C  
-ATOM   3116  N   GLN A 419     -26.987 -33.643  -2.627  1.00105.34           N  
-ANISOU 3116  N   GLN A 419    10321  18080  11622  -5595  -1157   2366       N  
-ATOM   3117  CA  GLN A 419     -28.185 -33.643  -3.448  1.00111.36           C  
-ANISOU 3117  CA  GLN A 419    10951  18933  12428  -5752  -1124   2628       C  
-ATOM   3118  C   GLN A 419     -27.956 -32.795  -4.696  1.00112.99           C  
-ANISOU 3118  C   GLN A 419    10868  19382  12681  -5950  -1177   2837       C  
-ATOM   3119  O   GLN A 419     -28.073 -33.283  -5.815  1.00114.19           O  
-ANISOU 3119  O   GLN A 419    10903  19783  12701  -6093  -1217   2904       O  
-ATOM   3120  CB  GLN A 419     -29.360 -33.092  -2.641  1.00118.42           C  
-ANISOU 3120  CB  GLN A 419    11904  19547  13543  -5701  -1027   2787       C  
-ATOM   3121  CG  GLN A 419     -30.714 -33.231  -3.305  1.00129.48           C  
-ANISOU 3121  CG  GLN A 419    13206  21003  14989  -5833   -986   3025       C  
-ATOM   3122  CD  GLN A 419     -31.828 -32.684  -2.434  1.00136.21           C  
-ANISOU 3122  CD  GLN A 419    14118  21572  16063  -5771   -889   3155       C  
-ATOM   3123  OE1 GLN A 419     -32.990 -32.643  -2.840  1.00139.31           O  
-ANISOU 3123  OE1 GLN A 419    14424  21974  16533  -5864   -848   3351       O  
-ATOM   3124  NE2 GLN A 419     -31.477 -32.258  -1.226  1.00141.31           N  
-ANISOU 3124  NE2 GLN A 419    14913  21964  16816  -5611   -852   3039       N  
-ATOM   3125  N   ALA A 420     -27.613 -31.527  -4.491  1.00 98.94           N  
-ANISOU 3125  N   ALA A 420     8984  17523  11084  -5957  -1179   2936       N  
-ATOM   3126  CA  ALA A 420     -27.414 -30.583  -5.589  1.00102.49           C  
-ANISOU 3126  CA  ALA A 420     9178  18169  11596  -6146  -1226   3144       C  
-ATOM   3127  C   ALA A 420     -26.516 -31.118  -6.706  1.00103.59           C  
-ANISOU 3127  C   ALA A 420     9206  18636  11517  -6268  -1306   3049       C  
-ATOM   3128  O   ALA A 420     -26.846 -31.001  -7.887  1.00102.66           O  
-ANISOU 3128  O   ALA A 420     8914  18726  11368  -6455  -1336   3234       O  
-ATOM   3129  CB  ALA A 420     -26.865 -29.262  -5.056  1.00102.14           C  
-ANISOU 3129  CB  ALA A 420     9083  17989  11737  -6108  -1226   3187       C  
-ATOM   3130  N   LEU A 421     -25.382 -31.702  -6.331  1.00117.62           N  
-ANISOU 3130  N   LEU A 421    11089  20457  13146  -6161  -1343   2758       N  
-ATOM   3131  CA  LEU A 421     -24.408 -32.173  -7.313  1.00121.18           C  
-ANISOU 3131  CA  LEU A 421    11435  21216  13393  -6264  -1419   2637       C  
-ATOM   3132  C   LEU A 421     -24.979 -33.230  -8.258  1.00127.09           C  
-ANISOU 3132  C   LEU A 421    12158  22166  13966  -6370  -1437   2682       C  
-ATOM   3133  O   LEU A 421     -24.736 -33.190  -9.464  1.00128.07           O  
-ANISOU 3133  O   LEU A 421    12103  22555  14002  -6550  -1484   2770       O  
-ATOM   3134  CB  LEU A 421     -23.138 -32.684  -6.624  1.00117.56           C  
-ANISOU 3134  CB  LEU A 421    11111  20746  12809  -6102  -1459   2289       C  
-ATOM   3135  CG  LEU A 421     -22.135 -31.603  -6.203  1.00114.37           C  
-ANISOU 3135  CG  LEU A 421    10647  20286  12523  -6067  -1474   2227       C  
-ATOM   3136  CD1 LEU A 421     -22.769 -30.602  -5.247  1.00110.64           C  
-ANISOU 3136  CD1 LEU A 421    10228  19506  12303  -5985  -1408   2378       C  
-ATOM   3137  CD2 LEU A 421     -20.885 -32.217  -5.588  1.00114.59           C  
-ANISOU 3137  CD2 LEU A 421    10805  20321  12413  -5906  -1523   1865       C  
-ATOM   3138  N   GLU A 422     -25.736 -34.172  -7.709  1.00129.59           N  
-ANISOU 3138  N   GLU A 422    12657  22354  14227  -6265  -1397   2621       N  
-ATOM   3139  CA  GLU A 422     -26.387 -35.186  -8.529  1.00138.22           C  
-ANISOU 3139  CA  GLU A 422    13742  23615  15162  -6359  -1407   2674       C  
-ATOM   3140  C   GLU A 422     -27.742 -34.685  -9.020  1.00148.82           C  
-ANISOU 3140  C   GLU A 422    14966  24923  16654  -6489  -1361   3001       C  
-ATOM   3141  O   GLU A 422     -28.321 -35.246  -9.951  1.00149.65           O  
-ANISOU 3141  O   GLU A 422    14999  25200  16662  -6615  -1376   3112       O  
-ATOM   3142  CB  GLU A 422     -26.551 -36.489  -7.746  1.00129.55           C  
-ANISOU 3142  CB  GLU A 422    12906  22404  13912  -6194  -1390   2445       C  
-ATOM   3143  CG  GLU A 422     -27.332 -36.340  -6.454  1.00120.54           C  
-ANISOU 3143  CG  GLU A 422    11951  20923  12924  -6042  -1305   2451       C  
-ATOM   3144  CD  GLU A 422     -27.370 -37.623  -5.650  1.00112.28           C  
-ANISOU 3144  CD  GLU A 422    11189  19762  11712  -5881  -1293   2201       C  
-ATOM   3145  OE1 GLU A 422     -26.807 -38.635  -6.118  1.00107.03           O  
-ANISOU 3145  OE1 GLU A 422    10571  19284  10811  -5883  -1357   2028       O  
-ATOM   3146  OE2 GLU A 422     -27.959 -37.617  -4.547  1.00106.21           O  
-ANISOU 3146  OE2 GLU A 422    10601  18710  11043  -5753  -1222   2175       O  
-ATOM   3147  N   LYS A 423     -28.235 -33.624  -8.388  1.00179.19           N  
-ANISOU 3147  N   LYS A 423    18795  28548  20741  -6452  -1311   3148       N  
-ATOM   3148  CA  LYS A 423     -29.517 -33.029  -8.748  1.00191.17           C  
-ANISOU 3148  CA  LYS A 423    20200  30007  22429  -6557  -1271   3450       C  
-ATOM   3149  C   LYS A 423     -29.636 -32.930 -10.255  1.00197.82           C  
-ANISOU 3149  C   LYS A 423    20827  31131  23204  -6779  -1329   3636       C  
-ATOM   3150  O   LYS A 423     -30.465 -33.598 -10.871  1.00197.55           O  
-ANISOU 3150  O   LYS A 423    20772  31190  23099  -6859  -1325   3733       O  
-ATOM   3151  CB  LYS A 423     -29.647 -31.633  -8.146  1.00196.85           C  
-ANISOU 3151  CB  LYS A 423    20865  30521  23407  -6524  -1241   3587       C  
-ATOM   3152  CG  LYS A 423     -31.004 -30.991  -8.361  1.00204.09           C  
-ANISOU 3152  CG  LYS A 423    21684  31344  24518  -6603  -1203   3880       C  
-ATOM   3153  CD  LYS A 423     -31.975 -31.431  -7.289  1.00210.40           C  
-ANISOU 3153  CD  LYS A 423    22660  31886  25395  -6460  -1114   3842       C  
-ATOM   3154  CE  LYS A 423     -31.383 -31.188  -5.912  1.00214.45           C  
-ANISOU 3154  CE  LYS A 423    23350  32154  25979  -6265  -1075   3653       C  
-ATOM   3155  NZ  LYS A 423     -30.974 -29.768  -5.726  1.00216.87           N  
-ANISOU 3155  NZ  LYS A 423    23547  32376  26477  -6273  -1090   3765       N  
-ATOM   3156  N   HIS A 424     -28.802 -32.084 -10.846  1.00184.68           N  
-ANISOU 3156  N   HIS A 424    19008  29600  21562  -6883  -1383   3684       N  
-ATOM   3157  CA  HIS A 424     -28.735 -31.992 -12.292  1.00191.61           C  
-ANISOU 3157  CA  HIS A 424    19693  30754  22355  -7100  -1443   3834       C  
-ATOM   3158  C   HIS A 424     -28.002 -33.213 -12.830  1.00194.04           C  
-ANISOU 3158  C   HIS A 424    20038  31297  22390  -7118  -1487   3624       C  
-ATOM   3159  O   HIS A 424     -28.590 -34.039 -13.529  1.00195.87           O  
-ANISOU 3159  O   HIS A 424    20257  31661  22503  -7195  -1497   3680       O  
-ATOM   3160  CB  HIS A 424     -28.023 -30.712 -12.724  1.00194.77           C  
-ANISOU 3160  CB  HIS A 424    19934  31219  22852  -7212  -1483   3935       C  
-ATOM   3161  CG  HIS A 424     -28.128 -30.433 -14.191  1.00198.86           C  
-ANISOU 3161  CG  HIS A 424    20258  31982  23316  -7449  -1540   4134       C  
-ATOM   3162  ND1 HIS A 424     -27.658 -31.305 -15.149  1.00200.01           N  
-ANISOU 3162  ND1 HIS A 424    20357  32400  23237  -7554  -1585   4050       N  
-ATOM   3163  CD2 HIS A 424     -28.654 -29.383 -14.865  1.00200.88           C  
-ANISOU 3163  CD2 HIS A 424    20365  32248  23713  -7601  -1562   4412       C  
-ATOM   3164  CE1 HIS A 424     -27.890 -30.805 -16.349  1.00201.15           C  
-ANISOU 3164  CE1 HIS A 424    20352  32703  23372  -7749  -1631   4268       C  
-ATOM   3165  NE2 HIS A 424     -28.491 -29.639 -16.205  1.00201.88           N  
-ANISOU 3165  NE2 HIS A 424    20408  32632  23664  -7759  -1626   4487       N  
-ATOM   3166  N   GLU A 425     -26.722 -33.327 -12.489  1.00189.87           N  
-ANISOU 3166  N   GLU A 425    19556  30819  21766  -7041  -1515   3377       N  
-ATOM   3167  CA  GLU A 425     -25.903 -34.447 -12.939  1.00191.06           C  
-ANISOU 3167  CA  GLU A 425    19743  31192  21659  -7042  -1565   3148       C  
-ATOM   3168  C   GLU A 425     -26.202 -34.769 -14.398  1.00192.19           C  
-ANISOU 3168  C   GLU A 425    19731  31608  21684  -7255  -1606   3305       C  
-ATOM   3169  O   GLU A 425     -26.364 -35.930 -14.772  1.00191.94           O  
-ANISOU 3169  O   GLU A 425    19760  31702  21468  -7258  -1623   3222       O  
-ATOM   3170  CB  GLU A 425     -26.141 -35.678 -12.060  1.00190.89           C  
-ANISOU 3170  CB  GLU A 425    19959  31045  21525  -6854  -1540   2936       C  
-ATOM   3171  CG  GLU A 425     -25.206 -36.846 -12.340  1.00190.83           C  
-ANISOU 3171  CG  GLU A 425    20020  31237  21251  -6818  -1599   2660       C  
-ATOM   3172  CD  GLU A 425     -25.567 -38.086 -11.544  1.00189.79           C  
-ANISOU 3172  CD  GLU A 425    20137  30977  20996  -6646  -1579   2475       C  
-ATOM   3173  OE1 GLU A 425     -25.235 -39.203 -11.997  1.00189.56           O  
-ANISOU 3173  OE1 GLU A 425    20161  31125  20738  -6649  -1627   2321       O  
-ATOM   3174  OE2 GLU A 425     -26.182 -37.943 -10.466  1.00189.16           O  
-ANISOU 3174  OE2 GLU A 425    20207  30619  21047  -6513  -1516   2480       O  
-ATOM   3175  N   GLY A 426     -26.280 -33.728 -15.220  1.00179.02           N  
-ANISOU 3175  N   GLY A 426    17872  30027  20120  -7436  -1625   3534       N  
-ATOM   3176  CA  GLY A 426     -26.622 -33.885 -16.620  1.00179.29           C  
-ANISOU 3176  CA  GLY A 426    17756  30300  20065  -7650  -1665   3713       C  
-ATOM   3177  C   GLY A 426     -25.549 -34.618 -17.396  1.00178.68           C  
-ANISOU 3177  C   GLY A 426    17634  30510  19745  -7724  -1721   3526       C  
-ATOM   3178  O   GLY A 426     -25.545 -34.609 -18.627  1.00180.35           O  
-ANISOU 3178  O   GLY A 426    17720  30941  19862  -7907  -1761   3652       O  
-ATOM   3179  N   LYS A 427     -24.635 -35.252 -16.669  1.00184.88           N  
-ANISOU 3179  N   LYS A 427    18544  31284  20417  -7564  -1728   3217       N  
-ATOM   3180  CA  LYS A 427     -23.544 -36.000 -17.280  1.00183.06           C  
-ANISOU 3180  CA  LYS A 427    18282  31318  19955  -7605  -1784   2997       C  
-ATOM   3181  C   LYS A 427     -22.608 -35.088 -18.068  1.00180.19           C  
-ANISOU 3181  C   LYS A 427    17728  31138  19598  -7778  -1816   3029       C  
-ATOM   3182  O   LYS A 427     -21.677 -35.558 -18.722  1.00181.09           O  
-ANISOU 3182  O   LYS A 427    17779  31497  19530  -7849  -1861   2867       O  
-ATOM   3183  CB  LYS A 427     -24.090 -37.119 -18.170  1.00184.66           C  
-ANISOU 3183  CB  LYS A 427    18484  31702  19975  -7690  -1808   3041       C  
-ATOM   3184  CG  LYS A 427     -24.228 -38.463 -17.472  1.00185.32           C  
-ANISOU 3184  CG  LYS A 427    18780  31721  19914  -7504  -1806   2822       C  
-ATOM   3185  CD  LYS A 427     -25.126 -38.388 -16.254  1.00185.36           C  
-ANISOU 3185  CD  LYS A 427    18951  31403  20073  -7335  -1741   2858       C  
-ATOM   3186  CE  LYS A 427     -25.191 -39.731 -15.548  1.00184.63           C  
-ANISOU 3186  CE  LYS A 427    19090  31243  19818  -7156  -1740   2623       C  
-ATOM   3187  NZ  LYS A 427     -25.687 -40.806 -16.452  1.00184.58           N  
-ANISOU 3187  NZ  LYS A 427    19082  31427  19623  -7250  -1767   2667       N  
-ATOM   3188  N   HIS A 428     -22.858 -33.783 -17.994  1.00195.33           N  
-ANISOU 3188  N   HIS A 428    19559  32936  21721  -7848  -1793   3233       N  
-ATOM   3189  CA  HIS A 428     -22.014 -32.795 -18.657  1.00189.85           C  
-ANISOU 3189  CA  HIS A 428    18729  32376  21030  -7994  -1815   3277       C  
-ATOM   3190  C   HIS A 428     -20.550 -33.136 -18.426  1.00181.69           C  
-ANISOU 3190  C   HIS A 428    17677  31482  19876  -7950  -1843   2943       C  
-ATOM   3191  O   HIS A 428     -19.791 -33.374 -19.365  1.00180.88           O  
-ANISOU 3191  O   HIS A 428    17508  31633  19587  -8060  -1872   2867       O  
-ATOM   3192  CB  HIS A 428     -22.300 -31.394 -18.107  1.00197.19           C  
-ANISOU 3192  CB  HIS A 428    19633  33084  22205  -7987  -1784   3453       C  
-ATOM   3193  CG  HIS A 428     -23.747 -31.009 -18.144  1.00204.06           C  
-ANISOU 3193  CG  HIS A 428    20529  33785  23221  -7998  -1762   3755       C  
-ATOM   3194  ND1 HIS A 428     -24.725 -31.826 -18.674  1.00207.35           N  
-ANISOU 3194  ND1 HIS A 428    20981  34249  23555  -8021  -1767   3869       N  
-ATOM   3195  CD2 HIS A 428     -24.382 -29.894 -17.716  1.00207.60           C  
-ANISOU 3195  CD2 HIS A 428    20970  34018  23892  -7983  -1739   3960       C  
-ATOM   3196  CE1 HIS A 428     -25.894 -31.231 -18.572  1.00209.79           C  
-ANISOU 3196  CE1 HIS A 428    21297  34381  24031  -8019  -1749   4123       C  
-ATOM   3197  NE2 HIS A 428     -25.721 -30.055 -17.994  1.00209.97           N  
-ANISOU 3197  NE2 HIS A 428    21295  34242  24242  -7994  -1734   4184       N  
-ATOM   3198  N   GLN A 429     -20.168 -33.158 -17.157  1.00137.29           N  
-ANISOU 3198  N   GLN A 429    12187  25662  14315  -7730  -1823   2744       N  
-ATOM   3199  CA  GLN A 429     -18.817 -33.499 -16.749  1.00128.33           C  
-ANISOU 3199  CA  GLN A 429    11083  24610  13067  -7628  -1852   2405       C  
-ATOM   3200  C   GLN A 429     -18.925 -34.394 -15.526  1.00123.27           C  
-ANISOU 3200  C   GLN A 429    10667  23772  12397  -7358  -1844   2186       C  
-ATOM   3201  O   GLN A 429     -17.958 -34.595 -14.793  1.00123.33           O  
-ANISOU 3201  O   GLN A 429    10751  23745  12362  -7206  -1864   1901       O  
-ATOM   3202  CB  GLN A 429     -18.052 -32.230 -16.385  1.00125.79           C  
-ANISOU 3202  CB  GLN A 429    10685  24223  12888  -7649  -1839   2392       C  
-ATOM   3203  CG  GLN A 429     -17.686 -31.362 -17.569  1.00121.68           C  
-ANISOU 3203  CG  GLN A 429     9955  23914  12365  -7918  -1852   2551       C  
-ATOM   3204  CD  GLN A 429     -16.453 -31.868 -18.281  1.00118.85           C  
-ANISOU 3204  CD  GLN A 429     9514  23854  11791  -7998  -1891   2309       C  
-ATOM   3205  OE1 GLN A 429     -15.969 -32.965 -18.000  1.00118.70           O  
-ANISOU 3205  OE1 GLN A 429     9568  23907  11626  -7870  -1922   2037       O  
-ATOM   3206  NE2 GLN A 429     -15.928 -31.068 -19.202  1.00118.77           N  
-ANISOU 3206  NE2 GLN A 429     9394  24002  11733  -8183  -1882   2404       N  
-ATOM   3207  N   LYS A 430     -20.120 -34.936 -15.322  1.00117.87           N  
-ANISOU 3207  N   LYS A 430    10091  22958  11735  -7303  -1817   2319       N  
-ATOM   3208  CA  LYS A 430     -20.470 -35.598 -14.070  1.00111.45           C  
-ANISOU 3208  CA  LYS A 430     9511  21900  10936  -7060  -1794   2171       C  
-ATOM   3209  C   LYS A 430     -19.678 -36.866 -13.786  1.00109.06           C  
-ANISOU 3209  C   LYS A 430     9343  21685  10410  -6916  -1844   1824       C  
-ATOM   3210  O   LYS A 430     -19.584 -37.300 -12.639  1.00108.01           O  
-ANISOU 3210  O   LYS A 430     9411  21349  10280  -6698  -1838   1632       O  
-ATOM   3211  CB  LYS A 430     -21.972 -35.879 -14.022  1.00107.46           C  
-ANISOU 3211  CB  LYS A 430     9077  21255  10498  -7063  -1747   2402       C  
-ATOM   3212  CG  LYS A 430     -22.796 -34.682 -13.584  1.00102.10           C  
-ANISOU 3212  CG  LYS A 430     8365  20346  10084  -7077  -1689   2661       C  
-ATOM   3213  CD  LYS A 430     -22.563 -33.473 -14.473  1.00 99.23           C  
-ANISOU 3213  CD  LYS A 430     7778  20108   9817  -7286  -1703   2868       C  
-ATOM   3214  CE  LYS A 430     -23.335 -32.266 -13.979  1.00 97.71           C  
-ANISOU 3214  CE  LYS A 430     7563  19676   9886  -7284  -1656   3110       C  
-ATOM   3215  NZ  LYS A 430     -23.064 -31.073 -14.818  1.00 97.94           N  
-ANISOU 3215  NZ  LYS A 430     7394  19819   9999  -7486  -1677   3303       N  
-ATOM   3216  N   LEU A 431     -19.105 -37.455 -14.826  1.00118.94           N  
-ANISOU 3216  N   LEU A 431    10489  23236  11467  -7037  -1898   1741       N  
-ATOM   3217  CA  LEU A 431     -18.275 -38.637 -14.650  1.00119.09           C  
-ANISOU 3217  CA  LEU A 431    10620  23365  11265  -6908  -1960   1403       C  
-ATOM   3218  C   LEU A 431     -17.181 -38.377 -13.615  1.00118.13           C  
-ANISOU 3218  C   LEU A 431    10578  23127  11180  -6726  -1980   1116       C  
-ATOM   3219  O   LEU A 431     -16.964 -39.187 -12.714  1.00114.85           O  
-ANISOU 3219  O   LEU A 431    10370  22583  10683  -6513  -2006    871       O  
-ATOM   3220  CB  LEU A 431     -17.669 -39.058 -15.974  1.00116.71           C  
-ANISOU 3220  CB  LEU A 431    10152  23418  10774  -7087  -2013   1361       C  
-ATOM   3221  N   LEU A 432     -16.501 -37.242 -13.744  1.00131.86           N  
-ANISOU 3221  N   LEU A 432    12159  24905  13037  -6812  -1972   1148       N  
-ATOM   3222  CA  LEU A 432     -15.432 -36.880 -12.816  1.00130.79           C  
-ANISOU 3222  CA  LEU A 432    12076  24668  12949  -6655  -1991    888       C  
-ATOM   3223  C   LEU A 432     -15.979 -36.274 -11.527  1.00126.78           C  
-ANISOU 3223  C   LEU A 432    11718  23801  12651  -6493  -1936    957       C  
-ATOM   3224  O   LEU A 432     -15.332 -36.325 -10.481  1.00125.39           O  
-ANISOU 3224  O   LEU A 432    11676  23470  12497  -6295  -1954    715       O  
-ATOM   3225  CB  LEU A 432     -14.444 -35.916 -13.475  1.00144.84           C  
-ANISOU 3225  CB  LEU A 432    13626  26642  14763  -6821  -2000    882       C  
-ATOM   3226  CG  LEU A 432     -13.593 -36.531 -14.586  1.00154.41           C  
-ANISOU 3226  CG  LEU A 432    14699  28211  15757  -6952  -2059    725       C  
-ATOM   3227  CD1 LEU A 432     -12.668 -35.492 -15.203  1.00164.01           C  
-ANISOU 3227  CD1 LEU A 432    15693  29604  17019  -7130  -2055    731       C  
-ATOM   3228  CD2 LEU A 432     -12.800 -37.711 -14.046  1.00163.24           C  
-ANISOU 3228  CD2 LEU A 432    15964  29363  16695  -6743  -2129    337       C  
-ATOM   3229  N   LEU A 433     -17.171 -35.695 -11.610  1.00101.08           N  
-ANISOU 3229  N   LEU A 433     8440  20413   9551  -6576  -1872   1283       N  
-ATOM   3230  CA  LEU A 433     -17.833 -35.140 -10.438  1.00 98.62           C  
-ANISOU 3230  CA  LEU A 433     8268  19761   9441  -6434  -1814   1373       C  
-ATOM   3231  C   LEU A 433     -18.092 -36.242  -9.416  1.00 97.48           C  
-ANISOU 3231  C   LEU A 433     8397  19427   9214  -6201  -1818   1169       C  
-ATOM   3232  O   LEU A 433     -18.122 -35.994  -8.213  1.00 99.61           O  
-ANISOU 3232  O   LEU A 433     8827  19422   9600  -6022  -1791   1089       O  
-ATOM   3233  CB  LEU A 433     -19.149 -34.477 -10.841  1.00 89.55           C  
-ANISOU 3233  CB  LEU A 433     7039  18536   8451  -6574  -1752   1755       C  
-ATOM   3234  CG  LEU A 433     -19.301 -33.002 -10.480  1.00 86.80           C  
-ANISOU 3234  CG  LEU A 433     6608  18021   8350  -6610  -1708   1950       C  
-ATOM   3235  CD1 LEU A 433     -18.076 -32.229 -10.916  1.00 81.67           C  
-ANISOU 3235  CD1 LEU A 433     5793  17541   7697  -6710  -1742   1869       C  
-ATOM   3236  CD2 LEU A 433     -20.562 -32.430 -11.109  1.00 79.72           C  
-ANISOU 3236  CD2 LEU A 433     5608  17102   7580  -6771  -1667   2320       C  
-ATOM   3237  N   ALA A 434     -18.280 -37.462  -9.910  1.00137.23           N  
-ANISOU 3237  N   ALA A 434    13492  24607  14042  -6208  -1854   1085       N  
-ATOM   3238  CA  ALA A 434     -18.485 -38.620  -9.051  1.00131.55           C  
-ANISOU 3238  CA  ALA A 434    13044  23734  13206  -6003  -1868    876       C  
-ATOM   3239  C   ALA A 434     -17.286 -38.830  -8.134  1.00129.91           C  
-ANISOU 3239  C   ALA A 434    12968  23446  12946  -5798  -1924    520       C  
-ATOM   3240  O   ALA A 434     -17.442 -39.047  -6.934  1.00127.39           O  
-ANISOU 3240  O   ALA A 434    12880  22852  12672  -5599  -1909    399       O  
-ATOM   3241  CB  ALA A 434     -18.730 -39.861  -9.893  1.00126.21           C  
-ANISOU 3241  CB  ALA A 434    12385  23273  12296  -6067  -1910    838       C  
-ATOM   3242  N   VAL A 435     -16.089 -38.765  -8.707  1.00111.52           N  
-ANISOU 3242  N   VAL A 435    10493  21357  10522  -5851  -1990    348       N  
-ATOM   3243  CA  VAL A 435     -14.859 -38.908  -7.936  1.00110.46           C  
-ANISOU 3243  CA  VAL A 435    10452  21178  10341  -5668  -2053     -1       C  
-ATOM   3244  C   VAL A 435     -14.627 -37.646  -7.109  1.00108.98           C  
-ANISOU 3244  C   VAL A 435    10245  20773  10390  -5612  -2008     50       C  
-ATOM   3245  O   VAL A 435     -13.543 -37.422  -6.571  1.00109.91           O  
-ANISOU 3245  O   VAL A 435    10379  20868  10515  -5498  -2052   -196       O  
-ATOM   3246  CB  VAL A 435     -13.649 -39.178  -8.854  1.00110.45           C  
-ANISOU 3246  CB  VAL A 435    10276  21517  10173  -5756  -2133   -202       C  
-ATOM   3247  CG1 VAL A 435     -12.449 -39.634  -8.039  1.00112.71           C  
-ANISOU 3247  CG1 VAL A 435    10694  21759  10372  -5537  -2215   -607       C  
-ATOM   3248  CG2 VAL A 435     -14.009 -40.226  -9.898  1.00112.43           C  
-ANISOU 3248  CG2 VAL A 435    10495  22009  10214  -5867  -2165   -171       C  
-ATOM   3249  N   PHE A 436     -15.668 -36.825  -7.011  1.00130.14           N  
-ANISOU 3249  N   PHE A 436    12889  23295  13263  -5690  -1922    371       N  
-ATOM   3250  CA  PHE A 436     -15.631 -35.610  -6.206  1.00127.07           C  
-ANISOU 3250  CA  PHE A 436    12495  22677  13110  -5638  -1872    459       C  
-ATOM   3251  C   PHE A 436     -16.822 -35.549  -5.247  1.00122.73           C  
-ANISOU 3251  C   PHE A 436    12137  21794  12699  -5527  -1798    608       C  
-ATOM   3252  O   PHE A 436     -16.777 -34.859  -4.230  1.00122.22           O  
-ANISOU 3252  O   PHE A 436    12162  21474  12802  -5405  -1765    599       O  
-ATOM   3253  CB  PHE A 436     -15.607 -34.380  -7.112  1.00132.50           C  
-ANISOU 3253  CB  PHE A 436    12905  23515  13924  -5871  -1842    719       C  
-ATOM   3254  CG  PHE A 436     -15.899 -33.097  -6.399  1.00134.50           C  
-ANISOU 3254  CG  PHE A 436    13149  23523  14430  -5848  -1781    892       C  
-ATOM   3255  CD1 PHE A 436     -14.876 -32.351  -5.844  1.00137.00           C  
-ANISOU 3255  CD1 PHE A 436    13440  23784  14831  -5777  -1797    745       C  
-ATOM   3256  CD2 PHE A 436     -17.198 -32.632  -6.291  1.00135.41           C  
-ANISOU 3256  CD2 PHE A 436    13279  23468  14701  -5895  -1709   1200       C  
-ATOM   3257  CE1 PHE A 436     -15.142 -31.168  -5.193  1.00139.72           C  
-ANISOU 3257  CE1 PHE A 436    13779  23903  15405  -5755  -1744    908       C  
-ATOM   3258  CE2 PHE A 436     -17.471 -31.453  -5.641  1.00138.29           C  
-ANISOU 3258  CE2 PHE A 436    13636  23610  15299  -5870  -1657   1358       C  
-ATOM   3259  CZ  PHE A 436     -16.442 -30.717  -5.091  1.00140.01           C  
-ANISOU 3259  CZ  PHE A 436    13834  23771  15593  -5800  -1674   1216       C  
-ATOM   3260  N   VAL A 437     -17.883 -36.281  -5.576  1.00102.21           N  
-ANISOU 3260  N   VAL A 437     9603  19202  10032  -5573  -1771    741       N  
-ATOM   3261  CA  VAL A 437     -19.071 -36.358  -4.731  1.00 96.01           C  
-ANISOU 3261  CA  VAL A 437     9002  18122   9357  -5480  -1696    869       C  
-ATOM   3262  C   VAL A 437     -18.958 -37.543  -3.781  1.00 91.07           C  
-ANISOU 3262  C   VAL A 437     8679  17336   8586  -5260  -1724    583       C  
-ATOM   3263  O   VAL A 437     -19.568 -37.559  -2.711  1.00 90.62           O  
-ANISOU 3263  O   VAL A 437     8828  16981   8622  -5123  -1670    586       O  
-ATOM   3264  CB  VAL A 437     -20.349 -36.519  -5.573  1.00 94.83           C  
-ANISOU 3264  CB  VAL A 437     8764  18056   9212  -5650  -1648   1166       C  
-ATOM   3265  CG1 VAL A 437     -20.889 -37.937  -5.456  1.00 95.06           C  
-ANISOU 3265  CG1 VAL A 437     8996  18071   9053  -5576  -1656   1053       C  
-ATOM   3266  CG2 VAL A 437     -21.399 -35.512  -5.143  1.00 93.15           C  
-ANISOU 3266  CG2 VAL A 437     8526  17613   9252  -5677  -1558   1451       C  
-ATOM   3267  N   THR A 438     -18.180 -38.540  -4.187  1.00 98.51           N  
-ANISOU 3267  N   THR A 438     9654  18479   9295  -5230  -1811    335       N  
-ATOM   3268  CA  THR A 438     -17.892 -39.681  -3.332  1.00 93.26           C  
-ANISOU 3268  CA  THR A 438     9283  17682   8470  -5017  -1861     28       C  
-ATOM   3269  C   THR A 438     -17.305 -39.233  -1.997  1.00 89.77           C  
-ANISOU 3269  C   THR A 438     9008  16960   8142  -4809  -1864   -157       C  
-ATOM   3270  O   THR A 438     -17.758 -39.678  -0.944  1.00 88.31           O  
-ANISOU 3270  O   THR A 438     9096  16498   7961  -4647  -1839   -242       O  
-ATOM   3271  CB  THR A 438     -16.928 -40.676  -4.007  1.00 93.29           C  
-ANISOU 3271  CB  THR A 438     9266  17965   8214  -5013  -1971   -235       C  
-ATOM   3272  OG1 THR A 438     -17.589 -41.311  -5.108  1.00 91.72           O  
-ANISOU 3272  OG1 THR A 438     8976  17987   7885  -5177  -1968    -82       O  
-ATOM   3273  CG2 THR A 438     -16.477 -41.738  -3.014  1.00 93.15           C  
-ANISOU 3273  CG2 THR A 438     9566  17787   8041  -4769  -2039   -581       C  
-ATOM   3274  N   PRO A 439     -16.294 -38.346  -2.033  1.00 75.32           N  
-ANISOU 3274  N   PRO A 439     7018  15197   6402  -4818  -1894   -221       N  
-ATOM   3275  CA  PRO A 439     -15.709 -37.869  -0.777  1.00 73.96           C  
-ANISOU 3275  CA  PRO A 439     6995  14760   6347  -4622  -1900   -392       C  
-ATOM   3276  C   PRO A 439     -16.747 -37.271   0.169  1.00 73.61           C  
-ANISOU 3276  C   PRO A 439     7082  14375   6510  -4564  -1797   -194       C  
-ATOM   3277  O   PRO A 439     -16.597 -37.415   1.377  1.00 73.01           O  
-ANISOU 3277  O   PRO A 439     7251  14023   6467  -4363  -1799   -365       O  
-ATOM   3278  CB  PRO A 439     -14.729 -36.788  -1.237  1.00 73.79           C  
-ANISOU 3278  CB  PRO A 439     6711  14901   6423  -4717  -1922   -382       C  
-ATOM   3279  CG  PRO A 439     -14.342 -37.202  -2.608  1.00 74.49           C  
-ANISOU 3279  CG  PRO A 439     6588  15368   6345  -4892  -1974   -387       C  
-ATOM   3280  CD  PRO A 439     -15.584 -37.807  -3.206  1.00 74.29           C  
-ANISOU 3280  CD  PRO A 439     6580  15391   6255  -5005  -1928   -166       C  
-ATOM   3281  N   LEU A 440     -17.770 -36.608  -0.363  1.00 78.13           N  
-ANISOU 3281  N   LEU A 440     7498  14965   7221  -4735  -1712    152       N  
-ATOM   3282  CA  LEU A 440     -18.818 -36.042   0.482  1.00 77.81           C  
-ANISOU 3282  CA  LEU A 440     7567  14615   7381  -4688  -1612    346       C  
-ATOM   3283  C   LEU A 440     -19.710 -37.142   1.041  1.00 78.84           C  
-ANISOU 3283  C   LEU A 440     7970  14576   7409  -4592  -1579    291       C  
-ATOM   3284  O   LEU A 440     -20.200 -37.049   2.164  1.00 77.88           O  
-ANISOU 3284  O   LEU A 440     8059  14141   7389  -4459  -1521    279       O  
-ATOM   3285  CB  LEU A 440     -19.660 -35.020  -0.284  1.00 76.53           C  
-ANISOU 3285  CB  LEU A 440     7155  14529   7395  -4897  -1541    724       C  
-ATOM   3286  CG  LEU A 440     -18.980 -33.708  -0.681  1.00 74.16           C  
-ANISOU 3286  CG  LEU A 440     6608  14328   7240  -4999  -1552    832       C  
-ATOM   3287  CD1 LEU A 440     -20.025 -32.692  -1.113  1.00 72.33           C  
-ANISOU 3287  CD1 LEU A 440     6207  14068   7207  -5160  -1475   1208       C  
-ATOM   3288  CD2 LEU A 440     -18.165 -33.160   0.467  1.00 73.77           C  
-ANISOU 3288  CD2 LEU A 440     6674  14059   7295  -4818  -1563    651       C  
-ATOM   3289  N   THR A 441     -19.915 -38.184   0.246  1.00 97.50           N  
-ANISOU 3289  N   THR A 441    10332  17148   9565  -4667  -1615    257       N  
-ATOM   3290  CA  THR A 441     -20.692 -39.337   0.678  1.00 99.65           C  
-ANISOU 3290  CA  THR A 441    10866  17292   9704  -4589  -1593    186       C  
-ATOM   3291  C   THR A 441     -19.962 -40.122   1.765  1.00100.50           C  
-ANISOU 3291  C   THR A 441    11287  17215   9683  -4351  -1656   -173       C  
-ATOM   3292  O   THR A 441     -20.590 -40.683   2.663  1.00 99.99           O  
-ANISOU 3292  O   THR A 441    11501  16896   9593  -4236  -1614   -236       O  
-ATOM   3293  CB  THR A 441     -21.019 -40.261  -0.506  1.00100.31           C  
-ANISOU 3293  CB  THR A 441    10863  17663   9586  -4732  -1625    234       C  
-ATOM   3294  OG1 THR A 441     -21.996 -39.628  -1.341  1.00100.23           O  
-ANISOU 3294  OG1 THR A 441    10624  17754   9705  -4936  -1552    585       O  
-ATOM   3295  CG2 THR A 441     -21.569 -41.589  -0.013  1.00101.07           C  
-ANISOU 3295  CG2 THR A 441    11263  17640   9500  -4629  -1624     90       C  
-ATOM   3296  N   ASP A 442     -18.636 -40.160   1.681  1.00106.35           N  
-ANISOU 3296  N   ASP A 442    16063  12569  11776  -5749    804   2069       N  
-ATOM   3297  CA  ASP A 442     -17.834 -40.790   2.721  1.00106.64           C  
-ANISOU 3297  CA  ASP A 442    16452  12254  11811  -5563    674   1844       C  
-ATOM   3298  C   ASP A 442     -17.882 -39.917   3.961  1.00104.44           C  
-ANISOU 3298  C   ASP A 442    15927  12009  11746  -5278    623   1766       C  
-ATOM   3299  O   ASP A 442     -18.296 -40.359   5.029  1.00105.50           O  
-ANISOU 3299  O   ASP A 442    16261  12165  11660  -5339    542   1729       O  
-ATOM   3300  CB  ASP A 442     -16.381 -40.957   2.275  1.00111.06           C  
-ANISOU 3300  CB  ASP A 442    17151  12399  12648  -5304    648   1653       C  
-ATOM   3301  CG  ASP A 442     -16.260 -41.583   0.903  1.00115.35           C  
-ANISOU 3301  CG  ASP A 442    17844  12923  13060  -5541    716   1732       C  
-ATOM   3302  OD1 ASP A 442     -17.279 -42.090   0.387  1.00120.12           O  
-ANISOU 3302  OD1 ASP A 442    18529  13802  13310  -5926    766   1921       O  
-ATOM   3303  OD2 ASP A 442     -15.141 -41.570   0.342  1.00117.25           O  
-ANISOU 3303  OD2 ASP A 442    18123  12875  13551  -5342    720   1603       O  
-ATOM   3304  N   LEU A 443     -17.462 -38.667   3.806  1.00 88.43           N  
-ANISOU 3304  N   LEU A 443    13462   9989  10147  -4969    672   1743       N  
-ATOM   3305  CA  LEU A 443     -17.452 -37.723   4.913  1.00 85.92           C  
-ANISOU 3305  CA  LEU A 443    12867   9703  10077  -4670    630   1667       C  
-ATOM   3306  C   LEU A 443     -18.784 -37.696   5.652  1.00 87.13           C  
-ANISOU 3306  C   LEU A 443    12955  10212   9939  -4893    625   1804       C  
-ATOM   3307  O   LEU A 443     -18.818 -37.526   6.869  1.00 87.48           O  
-ANISOU 3307  O   LEU A 443    13008  10222  10008  -4735    546   1706       O  
-ATOM   3308  CB  LEU A 443     -17.076 -36.320   4.431  1.00 81.60           C  
-ANISOU 3308  CB  LEU A 443    11803   9206   9997  -4380    706   1683       C  
-ATOM   3309  CG  LEU A 443     -15.587 -35.959   4.454  1.00 77.66           C  
-ANISOU 3309  CG  LEU A 443    11282   8304   9922  -3966    667   1463       C  
-ATOM   3310  CD1 LEU A 443     -15.061 -36.020   5.872  1.00 76.83           C  
-ANISOU 3310  CD1 LEU A 443    11324   7963   9905  -3694    542   1257       C  
-ATOM   3311  CD2 LEU A 443     -14.762 -36.862   3.545  1.00 75.16           C  
-ANISOU 3311  CD2 LEU A 443    11300   7710   9547  -4044    672   1395       C  
-ATOM   3312  N   ARG A 444     -19.883 -37.873   4.926  1.00 84.06           N  
-ANISOU 3312  N   ARG A 444    12504  10165   9271  -5261    708   2027       N  
-ATOM   3313  CA  ARG A 444     -21.188 -37.879   5.573  1.00 85.59           C  
-ANISOU 3313  CA  ARG A 444    12638  10711   9172  -5495    709   2163       C  
-ATOM   3314  C   ARG A 444     -21.325 -39.078   6.503  1.00 87.12           C  
-ANISOU 3314  C   ARG A 444    13319  10783   8998  -5650    603   2082       C  
-ATOM   3315  O   ARG A 444     -21.669 -38.926   7.675  1.00 87.50           O  
-ANISOU 3315  O   ARG A 444    13355  10894   8997  -5577    541   2034       O  
-ATOM   3316  CB  ARG A 444     -22.324 -37.863   4.551  1.00 87.47           C  
-ANISOU 3316  CB  ARG A 444    12720  11333   9180  -5868    820   2419       C  
-ATOM   3317  CG  ARG A 444     -23.690 -37.634   5.179  1.00 89.50           C  
-ANISOU 3317  CG  ARG A 444    12822  11986   9199  -6074    834   2565       C  
-ATOM   3318  CD  ARG A 444     -23.623 -36.539   6.245  1.00 90.29           C  
-ANISOU 3318  CD  ARG A 444    12585  12124   9598  -5738    798   2478       C  
-ATOM   3319  NE  ARG A 444     -24.922 -36.275   6.862  1.00 93.32           N  
-ANISOU 3319  NE  ARG A 444    12801  12891   9767  -5924    812   2611       N  
-ATOM   3320  CZ  ARG A 444     -25.336 -36.810   8.008  1.00 95.46           C  
-ANISOU 3320  CZ  ARG A 444    13301  13186   9784  -5999    733   2560       C  
-ATOM   3321  NH1 ARG A 444     -24.550 -37.642   8.679  1.00 96.65           N  
-ANISOU 3321  NH1 ARG A 444    13865  12994   9865  -5903    630   2379       N  
-ATOM   3322  NH2 ARG A 444     -26.537 -36.508   8.487  1.00 96.67           N  
-ANISOU 3322  NH2 ARG A 444    13269  13707   9754  -6171    756   2688       N  
-ATOM   3323  N   SER A 445     -21.043 -40.268   5.980  1.00 83.81           N  
-ANISOU 3323  N   SER A 445    13329  10188   8326  -5863    580   2064       N  
-ATOM   3324  CA  SER A 445     -21.113 -41.489   6.776  1.00 85.89           C  
-ANISOU 3324  CA  SER A 445    14090  10312   8234  -6023    475   1986       C  
-ATOM   3325  C   SER A 445     -20.047 -41.490   7.870  1.00 86.13           C  
-ANISOU 3325  C   SER A 445    14272   9972   8481  -5656    356   1734       C  
-ATOM   3326  O   SER A 445     -20.037 -42.359   8.742  1.00 87.13           O  
-ANISOU 3326  O   SER A 445    14779   9965   8363  -5725    254   1646       O  
-ATOM   3327  CB  SER A 445     -20.961 -42.727   5.889  1.00 85.21           C  
-ANISOU 3327  CB  SER A 445    14416  10099   7862  -6312    476   2016       C  
-ATOM   3328  OG  SER A 445     -19.629 -42.867   5.427  1.00 82.39           O  
-ANISOU 3328  OG  SER A 445    14183   9357   7764  -6073    451   1849       O  
-ATOM   3329  N   ASP A 446     -19.146 -40.515   7.813  1.00101.84           N  
-ANISOU 3329  N   ASP A 446    15966  11795  10933  -5267    368   1620       N  
-ATOM   3330  CA  ASP A 446     -18.120 -40.356   8.836  1.00101.26           C  
-ANISOU 3330  CA  ASP A 446    15978  11382  11114  -4885    260   1381       C  
-ATOM   3331  C   ASP A 446     -18.592 -39.412   9.936  1.00100.26           C  
-ANISOU 3331  C   ASP A 446    15535  11437  11121  -4700    241   1374       C  
-ATOM   3332  O   ASP A 446     -17.997 -39.356  11.009  1.00100.25           O  
-ANISOU 3332  O   ASP A 446    15628  11211  11250  -4433    142   1194       O  
-ATOM   3333  CB  ASP A 446     -16.814 -39.835   8.229  1.00103.43           C  
-ANISOU 3333  CB  ASP A 446    16120  11352  11828  -4545    276   1242       C  
-ATOM   3334  CG  ASP A 446     -16.047 -40.906   7.473  1.00105.41           C  
-ANISOU 3334  CG  ASP A 446    16775  11306  11969  -4646    254   1167       C  
-ATOM   3335  OD1 ASP A 446     -14.801 -40.824   7.427  1.00107.50           O  
-ANISOU 3335  OD1 ASP A 446    17099  11213  12534  -4342    212    978       O  
-ATOM   3336  OD2 ASP A 446     -16.687 -41.828   6.923  1.00108.26           O  
-ANISOU 3336  OD2 ASP A 446    17394  11792  11948  -5027    276   1293       O  
-ATOM   3337  N   PHE A 447     -19.654 -38.661   9.660  1.00 87.60           N  
-ANISOU 3337  N   PHE A 447    13551  10240   9492  -4839    334   1569       N  
-ATOM   3338  CA  PHE A 447     -20.261 -37.793  10.667  1.00 87.47           C  
-ANISOU 3338  CA  PHE A 447    13226  10445   9562  -4709    322   1584       C  
-ATOM   3339  C   PHE A 447     -21.633 -38.321  11.068  1.00 90.50           C  
-ANISOU 3339  C   PHE A 447    13722  11171   9493  -5091    328   1742       C  
-ATOM   3340  O   PHE A 447     -22.331 -37.710  11.877  1.00 92.46           O  
-ANISOU 3340  O   PHE A 447    13735  11656   9740  -5053    324   1780       O  
-ATOM   3341  CB  PHE A 447     -20.391 -36.355  10.153  1.00 81.28           C  
-ANISOU 3341  CB  PHE A 447    11865   9864   9152  -4523    417   1669       C  
-ATOM   3342  CG  PHE A 447     -19.099 -35.583  10.152  1.00 76.11           C  
-ANISOU 3342  CG  PHE A 447    11026   8899   8994  -4074    396   1491       C  
-ATOM   3343  CD1 PHE A 447     -18.489 -35.224  11.343  1.00 73.81           C  
-ANISOU 3343  CD1 PHE A 447    10722   8405   8918  -3731    302   1301       C  
-ATOM   3344  CD2 PHE A 447     -18.510 -35.196   8.962  1.00 72.79           C  
-ANISOU 3344  CD2 PHE A 447    10436   8395   8826  -3995    473   1517       C  
-ATOM   3345  CE1 PHE A 447     -17.308 -34.505  11.345  1.00 70.83           C  
-ANISOU 3345  CE1 PHE A 447    10169   7742   9000  -3317    282   1138       C  
-ATOM   3346  CE2 PHE A 447     -17.328 -34.476   8.955  1.00 70.11           C  
-ANISOU 3346  CE2 PHE A 447     9921   7774   8945  -3585    455   1356       C  
-ATOM   3347  CZ  PHE A 447     -16.726 -34.131  10.149  1.00 69.70           C  
-ANISOU 3347  CZ  PHE A 447     9859   7517   9105  -3245    360   1166       C  
-ATOM   3348  N   SER A 448     -22.007 -39.461  10.494  1.00106.00           N  
-ANISOU 3348  N   SER A 448    16045  13158  11073  -5458    337   1832       N  
-ATOM   3349  CA  SER A 448     -23.317 -40.064  10.724  1.00107.26           C  
-ANISOU 3349  CA  SER A 448    16337  13641  10777  -5860    350   1996       C  
-ATOM   3350  C   SER A 448     -23.577 -40.318  12.203  1.00107.14           C  
-ANISOU 3350  C   SER A 448    16488  13616  10606  -5817    250   1904       C  
-ATOM   3351  O   SER A 448     -24.699 -40.156  12.682  1.00107.64           O  
-ANISOU 3351  O   SER A 448    16427  14016  10456  -6004    272   2025       O  
-ATOM   3352  CB  SER A 448     -23.440 -41.373   9.941  1.00109.10           C  
-ANISOU 3352  CB  SER A 448    16999  13812  10642  -6221    354   2065       C  
-ATOM   3353  OG  SER A 448     -22.422 -42.285  10.315  1.00110.35           O  
-ANISOU 3353  OG  SER A 448    17604  13554  10769  -6114    246   1872       O  
-ATOM   3354  N   LYS A 449     -22.530 -40.716  12.920  1.00 90.34           N  
-ANISOU 3354  N   LYS A 449    14642  11100   8583  -5571    139   1686       N  
-ATOM   3355  CA  LYS A 449     -22.631 -41.006  14.347  1.00 89.00           C  
-ANISOU 3355  CA  LYS A 449    14665  10871   8279  -5504     33   1577       C  
-ATOM   3356  C   LYS A 449     -22.623 -39.736  15.198  1.00 86.90           C  
-ANISOU 3356  C   LYS A 449    13976  10699   8343  -5168     28   1514       C  
-ATOM   3357  O   LYS A 449     -23.211 -39.703  16.276  1.00 88.57           O  
-ANISOU 3357  O   LYS A 449    14195  11051   8406  -5192    -18   1506       O  
-ATOM   3358  CB  LYS A 449     -21.499 -41.938  14.781  1.00 90.14           C  
-ANISOU 3358  CB  LYS A 449    15284  10555   8411  -5369    -90   1365       C  
-ATOM   3359  CG  LYS A 449     -21.506 -43.280  14.070  1.00 92.98           C  
-ANISOU 3359  CG  LYS A 449    16101  10807   8422  -5703   -103   1413       C  
-ATOM   3360  CD  LYS A 449     -22.727 -44.100  14.457  1.00 95.50           C  
-ANISOU 3360  CD  LYS A 449    16654  11395   8238  -6118   -113   1554       C  
-ATOM   3361  CE  LYS A 449     -23.041 -45.161  13.413  1.00 96.83           C  
-ANISOU 3361  CE  LYS A 449    17125  11591   8076  -6503    -79   1677       C  
-ATOM   3362  NZ  LYS A 449     -23.633 -44.570  12.181  1.00 96.79           N  
-ANISOU 3362  NZ  LYS A 449    16765  11881   8128  -6654     62   1871       N  
-ATOM   3363  N   PHE A 450     -21.952 -38.696  14.717  1.00 86.63           N  
-ANISOU 3363  N   PHE A 450    13576  10585   8754  -4855     74   1468       N  
-ATOM   3364  CA  PHE A 450     -21.935 -37.412  15.410  1.00 84.98           C  
-ANISOU 3364  CA  PHE A 450    12929  10472   8887  -4528     76   1416       C  
-ATOM   3365  C   PHE A 450     -23.276 -36.718  15.236  1.00 87.09           C  
-ANISOU 3365  C   PHE A 450    12811  11226   9055  -4731    171   1628       C  
-ATOM   3366  O   PHE A 450     -23.795 -36.114  16.171  1.00 87.69           O  
-ANISOU 3366  O   PHE A 450    12671  11485   9161  -4638    152   1622       O  
-ATOM   3367  CB  PHE A 450     -20.804 -36.528  14.870  1.00 77.22           C  
-ANISOU 3367  CB  PHE A 450    11674   9255   8412  -4144     99   1309       C  
-ATOM   3368  CG  PHE A 450     -20.832 -35.104  15.379  1.00 69.34           C  
-ANISOU 3368  CG  PHE A 450    10169   8386   7791  -3820    117   1281       C  
-ATOM   3369  CD1 PHE A 450     -20.091 -34.733  16.489  1.00 67.36           C  
-ANISOU 3369  CD1 PHE A 450     9909   7901   7785  -3452     22   1079       C  
-ATOM   3370  CD2 PHE A 450     -21.583 -34.135  14.730  1.00 67.58           C  
-ANISOU 3370  CD2 PHE A 450     9480   8513   7686  -3880    225   1456       C  
-ATOM   3371  CE1 PHE A 450     -20.108 -33.427  16.951  1.00 66.44           C  
-ANISOU 3371  CE1 PHE A 450     9328   7899   8019  -3152     35   1051       C  
-ATOM   3372  CE2 PHE A 450     -21.606 -32.828  15.187  1.00 66.68           C  
-ANISOU 3372  CE2 PHE A 450     8899   8514   7922  -3582    237   1429       C  
-ATOM   3373  CZ  PHE A 450     -20.868 -32.474  16.300  1.00 66.11           C  
-ANISOU 3373  CZ  PHE A 450     8822   8207   8088  -3217    142   1227       C  
-ATOM   3374  N   GLN A 451     -23.830 -36.802  14.031  1.00 97.33           N  
-ANISOU 3374  N   GLN A 451    14017  12730  10233  -5006    273   1813       N  
-ATOM   3375  CA  GLN A 451     -25.134 -36.216  13.756  1.00 99.95           C  
-ANISOU 3375  CA  GLN A 451    14001  13527  10449  -5230    366   2024       C  
-ATOM   3376  C   GLN A 451     -26.184 -36.924  14.593  1.00102.05           C  
-ANISOU 3376  C   GLN A 451    14493  14013  10270  -5531    330   2090       C  
-ATOM   3377  O   GLN A 451     -27.171 -36.322  15.014  1.00101.05           O  
-ANISOU 3377  O   GLN A 451    14078  14233  10085  -5604    364   2191       O  
-ATOM   3378  CB  GLN A 451     -25.478 -36.327  12.272  1.00102.78           C  
-ANISOU 3378  CB  GLN A 451    14283  14034  10733  -5488    474   2204       C  
-ATOM   3379  CG  GLN A 451     -24.597 -35.484  11.371  1.00104.45           C  
-ANISOU 3379  CG  GLN A 451    14203  14097  11388  -5213    527   2170       C  
-ATOM   3380  CD  GLN A 451     -24.703 -34.002  11.676  1.00106.60           C  
-ANISOU 3380  CD  GLN A 451    13929  14531  12042  -4919    557   2172       C  
-ATOM   3381  OE1 GLN A 451     -25.657 -33.337  11.269  1.00108.57           O  
-ANISOU 3381  OE1 GLN A 451    13826  15147  12279  -5058    640   2346       O  
-ATOM   3382  NE2 GLN A 451     -23.719 -33.477  12.397  1.00107.30           N  
-ANISOU 3382  NE2 GLN A 451    13947  14346  12478  -4509    488   1974       N  
-ATOM   3383  N   GLU A 452     -25.961 -38.213  14.824  1.00 89.74           N  
-ANISOU 3383  N   GLU A 452    13453  12248   8397  -5707    259   2031       N  
-ATOM   3384  CA  GLU A 452     -26.782 -38.985  15.742  1.00 93.71           C  
-ANISOU 3384  CA  GLU A 452    14232  12892   8483  -5962    205   2061       C  
-ATOM   3385  C   GLU A 452     -26.697 -38.335  17.115  1.00 92.32           C  
-ANISOU 3385  C   GLU A 452    13903  12708   8468  -5674    136   1931       C  
-ATOM   3386  O   GLU A 452     -27.667 -37.765  17.607  1.00 92.89           O  
-ANISOU 3386  O   GLU A 452    13701  13121   8471  -5744    169   2023       O  
-ATOM   3387  CB  GLU A 452     -26.268 -40.425  15.821  1.00 98.65           C  
-ANISOU 3387  CB  GLU A 452    15451  13209   8821  -6115    120   1976       C  
-ATOM   3388  CG  GLU A 452     -27.349 -41.492  15.936  1.00108.35           C  
-ANISOU 3388  CG  GLU A 452    16996  14656   9517  -6575    118   2114       C  
-ATOM   3389  CD  GLU A 452     -27.494 -42.317  14.665  1.00112.72           C  
-ANISOU 3389  CD  GLU A 452    17768  15214   9848  -6898    173   2239       C  
-ATOM   3390  OE1 GLU A 452     -27.045 -41.849  13.596  1.00114.42           O  
-ANISOU 3390  OE1 GLU A 452    17777  15380  10316  -6804    243   2268       O  
-ATOM   3391  OE2 GLU A 452     -28.054 -43.434  14.734  1.00114.96           O  
-ANISOU 3391  OE2 GLU A 452    18428  15550   9702  -7247    145   2307       O  
-ATOM   3392  N   MET A 453     -25.510 -38.407  17.710  1.00 94.80           N  
-ANISOU 3392  N   MET A 453    14385  12627   9006  -5343     41   1714       N  
-ATOM   3393  CA  MET A 453     -25.272 -37.931  19.070  1.00 93.79           C  
-ANISOU 3393  CA  MET A 453    14184  12428   9025  -5053    -42   1563       C  
-ATOM   3394  C   MET A 453     -25.966 -36.619  19.425  1.00 94.68           C  
-ANISOU 3394  C   MET A 453    13758  12877   9340  -4922     14   1630       C  
-ATOM   3395  O   MET A 453     -26.897 -36.599  20.230  1.00 96.58           O  
-ANISOU 3395  O   MET A 453    13957  13383   9356  -5061      5   1685       O  
-ATOM   3396  CB  MET A 453     -23.772 -37.806  19.332  1.00 90.42           C  
-ANISOU 3396  CB  MET A 453    13858  11538   8958  -4640   -124   1330       C  
-ATOM   3397  CG  MET A 453     -23.442 -37.049  20.600  1.00 85.78           C  
-ANISOU 3397  CG  MET A 453    13093  10880   8618  -4279   -196   1174       C  
-ATOM   3398  SD  MET A 453     -21.717 -37.222  21.079  1.00 82.11           S  
-ANISOU 3398  SD  MET A 453    12877   9844   8478  -3847   -317    887       S  
-ATOM   3399  CE  MET A 453     -20.885 -36.586  19.627  1.00 78.81           C  
-ANISOU 3399  CE  MET A 453    12193   9286   8464  -3671   -230    899       C  
-ATOM   3400  N   ILE A 454     -25.500 -35.523  18.843  1.00 91.70           N  
-ANISOU 3400  N   ILE A 454    12969  12484   9388  -4651     70   1621       N  
-ATOM   3401  CA  ILE A 454     -26.024 -34.209  19.190  1.00 93.66           C  
-ANISOU 3401  CA  ILE A 454    12692  13013   9880  -4478    113   1664       C  
-ATOM   3402  C   ILE A 454     -27.547 -34.167  19.135  1.00 98.39           C  
-ANISOU 3402  C   ILE A 454    13134  14090  10158  -4840    185   1873       C  
-ATOM   3403  O   ILE A 454     -28.190 -33.524  19.961  1.00 99.74           O  
-ANISOU 3403  O   ILE A 454    13050  14501  10346  -4779    180   1883       O  
-ATOM   3404  CB  ILE A 454     -25.450 -33.106  18.283  1.00 88.22           C  
-ANISOU 3404  CB  ILE A 454    11583  12284   9654  -4216    181   1672       C  
-ATOM   3405  CG1 ILE A 454     -24.031 -32.742  18.720  1.00 85.59           C  
-ANISOU 3405  CG1 ILE A 454    11264  11533   9724  -3759    102   1440       C  
-ATOM   3406  CG2 ILE A 454     -26.326 -31.870  18.338  1.00 86.56           C  
-ANISOU 3406  CG2 ILE A 454    10828  12461   9598  -4172    249   1788       C  
-ATOM   3407  CD1 ILE A 454     -23.030 -33.855  18.541  1.00 84.04           C  
-ANISOU 3407  CD1 ILE A 454    11566  10925   9441  -3760     36   1314       C  
-ATOM   3408  N   GLU A 455     -28.121 -34.866  18.164  1.00103.08           N  
-ANISOU 3408  N   GLU A 455    13884  14823  10458  -5217    250   2038       N  
-ATOM   3409  CA  GLU A 455     -29.566 -34.861  17.985  1.00106.93           C  
-ANISOU 3409  CA  GLU A 455    14227  15764  10638  -5579    324   2246       C  
-ATOM   3410  C   GLU A 455     -30.262 -35.567  19.144  1.00106.85           C  
-ANISOU 3410  C   GLU A 455    14488  15867  10242  -5771    261   2232       C  
-ATOM   3411  O   GLU A 455     -31.405 -35.254  19.478  1.00108.02           O  
-ANISOU 3411  O   GLU A 455    14428  16393  10220  -5949    302   2350       O  
-ATOM   3412  CB  GLU A 455     -29.939 -35.513  16.652  1.00114.28           C  
-ANISOU 3412  CB  GLU A 455    15294  16786  11342  -5934    404   2417       C  
-ATOM   3413  CG  GLU A 455     -31.312 -35.123  16.133  1.00126.11           C  
-ANISOU 3413  CG  GLU A 455    16487  18760  12668  -6236    506   2644       C  
-ATOM   3414  CD  GLU A 455     -31.450 -35.330  14.633  1.00132.72           C  
-ANISOU 3414  CD  GLU A 455    17306  19663  13459  -6462    597   2799       C  
-ATOM   3415  OE1 GLU A 455     -30.597 -36.026  14.042  1.00136.93           O  
-ANISOU 3415  OE1 GLU A 455    18147  19885  13996  -6458    578   2740       O  
-ATOM   3416  OE2 GLU A 455     -32.409 -34.787  14.044  1.00137.33           O  
-ANISOU 3416  OE2 GLU A 455    17564  20609  14005  -6640    687   2979       O  
-ATOM   3417  N   THR A 456     -29.560 -36.510  19.766  1.00 96.33           N  
-ANISOU 3417  N   THR A 456    13617  14205   8779  -5731    161   2085       N  
-ATOM   3418  CA  THR A 456     -30.136 -37.303  20.846  1.00 96.77           C  
-ANISOU 3418  CA  THR A 456    13988  14330   8452  -5924     93   2066       C  
-ATOM   3419  C   THR A 456     -29.925 -36.665  22.214  1.00 94.57           C  
-ANISOU 3419  C   THR A 456    13568  14013   8352  -5609     19   1913       C  
-ATOM   3420  O   THR A 456     -30.505 -37.109  23.206  1.00 96.04           O  
-ANISOU 3420  O   THR A 456    13930  14311   8250  -5743    -29   1902       O  
-ATOM   3421  CB  THR A 456     -29.561 -38.737  20.877  1.00 96.61           C  
-ANISOU 3421  CB  THR A 456    14571  13982   8154  -6074     13   1990       C  
-ATOM   3422  OG1 THR A 456     -28.169 -38.698  21.216  1.00 98.41           O  
-ANISOU 3422  OG1 THR A 456    14935  13768   8689  -5695    -74   1772       O  
-ATOM   3423  CG2 THR A 456     -29.741 -39.417  19.529  1.00 98.13           C  
-ANISOU 3423  CG2 THR A 456    14922  14200   8162  -6386     81   2134       C  
-ATOM   3424  N   THR A 457     -29.102 -35.624  22.273  1.00105.83           N  
-ANISOU 3424  N   THR A 457    14676  15284  10250  -5191     11   1795       N  
-ATOM   3425  CA  THR A 457     -28.770 -35.024  23.561  1.00104.32           C  
-ANISOU 3425  CA  THR A 457    14365  15015  10258  -4859    -67   1632       C  
-ATOM   3426  C   THR A 457     -29.081 -33.528  23.648  1.00105.73           C  
-ANISOU 3426  C   THR A 457    13944  15438  10789  -4619    -12   1658       C  
-ATOM   3427  O   THR A 457     -29.381 -33.018  24.726  1.00106.39           O  
-ANISOU 3427  O   THR A 457    13868  15641  10915  -4478    -50   1594       O  
-ATOM   3428  CB  THR A 457     -27.294 -35.267  23.929  1.00100.99           C  
-ANISOU 3428  CB  THR A 457    14198  14092  10081  -4514   -169   1403       C  
-ATOM   3429  OG1 THR A 457     -26.450 -34.484  23.078  1.00 97.29           O  
-ANISOU 3429  OG1 THR A 457    13455  13461  10051  -4236   -129   1366       O  
-ATOM   3430  CG2 THR A 457     -26.942 -36.737  23.771  1.00 99.15           C  
-ANISOU 3430  CG2 THR A 457    14552  13603   9517  -4745   -227   1375       C  
-ATOM   3431  N   LEU A 458     -29.018 -32.830  22.519  1.00 83.82           N  
-ANISOU 3431  N   LEU A 458    10841  12741   8265  -4575     76   1752       N  
-ATOM   3432  CA  LEU A 458     -29.218 -31.384  22.513  1.00 88.58           C  
-ANISOU 3432  CA  LEU A 458    10871  13548   9238  -4328    124   1773       C  
-ATOM   3433  C   LEU A 458     -30.694 -31.004  22.549  1.00 98.47           C  
-ANISOU 3433  C   LEU A 458    11838  15300  10275  -4600    197   1956       C  
-ATOM   3434  O   LEU A 458     -31.537 -31.696  21.984  1.00101.10           O  
-ANISOU 3434  O   LEU A 458    12324  15844  10245  -5002    252   2119       O  
-ATOM   3435  CB  LEU A 458     -28.546 -30.754  21.294  1.00 75.88           C  
-ANISOU 3435  CB  LEU A 458     9016  11821   7994  -4165    186   1800       C  
-ATOM   3436  CG  LEU A 458     -27.661 -29.544  21.586  1.00 69.72           C  
-ANISOU 3436  CG  LEU A 458     7873  10872   7745  -3677    158   1656       C  
-ATOM   3437  CD1 LEU A 458     -26.192 -29.930  21.511  1.00 68.92           C  
-ANISOU 3437  CD1 LEU A 458     8051  10277   7858  -3414     90   1473       C  
-ATOM   3438  CD2 LEU A 458     -27.969 -28.413  20.617  1.00 68.88           C  
-ANISOU 3438  CD2 LEU A 458     7254  10994   7925  -3625    257   1788       C  
-ATOM   3439  N   ASP A 459     -30.996 -29.892  23.212  1.00140.52           N  
-ANISOU 3439  N   ASP A 459    16747  20813  15833  -4376    196   1924       N  
-ATOM   3440  CA  ASP A 459     -32.372 -29.430  23.353  1.00151.69           C  
-ANISOU 3440  CA  ASP A 459    17857  22702  17076  -4595    258   2078       C  
-ATOM   3441  C   ASP A 459     -32.738 -28.454  22.240  1.00156.11           C  
-ANISOU 3441  C   ASP A 459    17948  23491  17876  -4595    359   2225       C  
-ATOM   3442  O   ASP A 459     -32.389 -27.275  22.297  1.00154.31           O  
-ANISOU 3442  O   ASP A 459    17305  23262  18063  -4263    361   2170       O  
-ATOM   3443  CB  ASP A 459     -32.580 -28.774  24.720  1.00157.67           C  
-ANISOU 3443  CB  ASP A 459    18417  23561  17931  -4369    200   1966       C  
-ATOM   3444  CG  ASP A 459     -33.725 -29.393  25.494  1.00163.72           C  
-ANISOU 3444  CG  ASP A 459    19348  24617  18240  -4695    194   2035       C  
-ATOM   3445  OD1 ASP A 459     -34.098 -30.544  25.185  1.00170.39           O  
-ANISOU 3445  OD1 ASP A 459    20583  25476  18683  -5056    205   2121       O  
-ATOM   3446  OD2 ASP A 459     -34.249 -28.732  26.414  1.00167.27           O  
-ANISOU 3446  OD2 ASP A 459    19540  25282  18734  -4589    178   2001       O  
-ATOM   3447  N   MET A 460     -33.446 -28.956  21.233  1.00140.49           N  
-ANISOU 3447  N   MET A 460    16038  21708  15633  -4971    438   2413       N  
-ATOM   3448  CA  MET A 460     -33.826 -28.152  20.078  1.00146.87           C  
-ANISOU 3448  CA  MET A 460    16442  22733  16628  -5015    536   2567       C  
-ATOM   3449  C   MET A 460     -34.899 -27.130  20.439  1.00152.98           C  
-ANISOU 3449  C   MET A 460    16739  23929  17458  -5021    575   2654       C  
-ATOM   3450  O   MET A 460     -35.336 -26.350  19.593  1.00154.16           O  
-ANISOU 3450  O   MET A 460    16507  24301  17767  -5052    651   2785       O  
-ATOM   3451  CB  MET A 460     -34.328 -29.051  18.947  1.00146.15           C  
-ANISOU 3451  CB  MET A 460    16587  22738  16205  -5435    606   2743       C  
-ATOM   3452  CG  MET A 460     -33.477 -30.288  18.709  1.00144.50           C  
-ANISOU 3452  CG  MET A 460    16918  22155  15829  -5510    561   2667       C  
-ATOM   3453  SD  MET A 460     -31.749 -29.908  18.369  1.00140.48           S  
-ANISOU 3453  SD  MET A 460    16412  21153  15810  -5059    518   2485       S  
-ATOM   3454  CE  MET A 460     -31.082 -31.554  18.144  1.00138.45           C  
-ANISOU 3454  CE  MET A 460    16832  20541  15233  -5258    468   2425       C  
-ATOM   3455  N   ASP A 461     -35.321 -27.141  21.698  1.00176.44           N  
-ANISOU 3455  N   ASP A 461    19736  27009  20295  -4993    520   2578       N  
-ATOM   3456  CA  ASP A 461     -36.335 -26.210  22.173  1.00182.75           C  
-ANISOU 3456  CA  ASP A 461    20099  28203  21133  -4991    548   2641       C  
-ATOM   3457  C   ASP A 461     -35.688 -24.936  22.702  1.00181.51           C  
-ANISOU 3457  C   ASP A 461    19546  27949  21469  -4518    507   2501       C  
-ATOM   3458  O   ASP A 461     -36.045 -23.830  22.295  1.00181.73           O  
-ANISOU 3458  O   ASP A 461    19095  28194  21759  -4415    555   2574       O  
-ATOM   3459  CB  ASP A 461     -37.176 -26.859  23.272  1.00190.92           C  
-ANISOU 3459  CB  ASP A 461    21352  29428  21762  -5214    515   2634       C  
-ATOM   3460  CG  ASP A 461     -37.712 -28.218  22.869  1.00198.61           C  
-ANISOU 3460  CG  ASP A 461    22771  30451  22239  -5667    541   2751       C  
-ATOM   3461  OD1 ASP A 461     -36.973 -29.215  23.012  1.00201.54           O  
-ANISOU 3461  OD1 ASP A 461    23608  30494  22474  -5685    484   2661       O  
-ATOM   3462  OD2 ASP A 461     -38.872 -28.291  22.410  1.00202.54           O  
-ANISOU 3462  OD2 ASP A 461    23155  31315  22487  -6004    614   2930       O  
-ATOM   3463  N   GLN A 462     -34.733 -25.101  23.612  1.00184.64           N  
-ANISOU 3463  N   GLN A 462    20147  28016  21990  -4232    415   2300       N  
-ATOM   3464  CA  GLN A 462     -34.034 -23.970  24.209  1.00180.20           C  
-ANISOU 3464  CA  GLN A 462    19251  27326  21890  -3768    365   2148       C  
-ATOM   3465  C   GLN A 462     -33.058 -23.322  23.234  1.00174.56           C  
-ANISOU 3465  C   GLN A 462    18338  26378  21607  -3506    387   2128       C  
-ATOM   3466  O   GLN A 462     -32.649 -22.176  23.426  1.00173.10           O  
-ANISOU 3466  O   GLN A 462    17766  26163  21842  -3152    370   2052       O  
-ATOM   3467  CB  GLN A 462     -33.300 -24.398  25.482  1.00185.42           C  
-ANISOU 3467  CB  GLN A 462    20216  27697  22540  -3549    256   1937       C  
-ATOM   3468  CG  GLN A 462     -34.212 -24.610  26.677  1.00193.31           C  
-ANISOU 3468  CG  GLN A 462    21264  28948  23237  -3686    224   1924       C  
-ATOM   3469  CD  GLN A 462     -34.969 -23.352  27.055  1.00197.89           C  
-ANISOU 3469  CD  GLN A 462    21299  29880  24011  -3562    250   1957       C  
-ATOM   3470  OE1 GLN A 462     -34.383 -22.381  27.534  1.00200.46           O  
-ANISOU 3470  OE1 GLN A 462    21334  30100  24733  -3167    206   1829       O  
-ATOM   3471  NE2 GLN A 462     -36.279 -23.361  26.835  1.00203.29           N  
-ANISOU 3471  NE2 GLN A 462    21839  30983  24418  -3899    319   2128       N  
-ATOM   3472  N   VAL A 463     -32.685 -24.056  22.190  1.00144.13           N  
-ANISOU 3472  N   VAL A 463    14751  22360  17652  -3682    424   2196       N  
-ATOM   3473  CA  VAL A 463     -31.742 -23.544  21.202  1.00138.16           C  
-ANISOU 3473  CA  VAL A 463    13843  21373  17277  -3461    450   2182       C  
-ATOM   3474  C   VAL A 463     -32.267 -22.257  20.570  1.00137.87           C  
-ANISOU 3474  C   VAL A 463    13235  21626  17523  -3389    520   2303       C  
-ATOM   3475  O   VAL A 463     -31.492 -21.380  20.187  1.00134.89           O  
-ANISOU 3475  O   VAL A 463    12582  21091  17580  -3071    520   2248       O  
-ATOM   3476  CB  VAL A 463     -31.447 -24.580  20.100  1.00133.27           C  
-ANISOU 3476  CB  VAL A 463    13593  20593  16450  -3722    492   2263       C  
-ATOM   3477  CG1 VAL A 463     -32.672 -24.795  19.224  1.00130.44           C  
-ANISOU 3477  CG1 VAL A 463    13155  20615  15792  -4148    588   2499       C  
-ATOM   3478  CG2 VAL A 463     -30.260 -24.134  19.260  1.00127.48           C  
-ANISOU 3478  CG2 VAL A 463    12762  19549  16124  -3445    502   2203       C  
-ATOM   3479  N   GLU A 464     -33.589 -22.151  20.469  1.00175.32           N  
-ANISOU 3479  N   GLU A 464    17804  26792  22019  -3687    576   2468       N  
-ATOM   3480  CA  GLU A 464     -34.230 -20.950  19.947  1.00173.45           C  
-ANISOU 3480  CA  GLU A 464    17023  26867  22014  -3647    637   2589       C  
-ATOM   3481  C   GLU A 464     -34.046 -19.796  20.922  1.00172.13           C  
-ANISOU 3481  C   GLU A 464    16478  26724  22199  -3260    580   2459       C  
-ATOM   3482  O   GLU A 464     -33.879 -18.645  20.519  1.00169.23           O  
-ANISOU 3482  O   GLU A 464    15672  26407  22220  -3030    599   2476       O  
-ATOM   3483  CB  GLU A 464     -35.723 -21.193  19.721  1.00178.10           C  
-ANISOU 3483  CB  GLU A 464    17544  27902  22222  -4069    702   2784       C  
-ATOM   3484  CG  GLU A 464     -36.188 -20.951  18.296  1.00181.73           C  
-ANISOU 3484  CG  GLU A 464    17804  28550  22696  -4282    798   2984       C  
-ATOM   3485  CD  GLU A 464     -36.143 -22.205  17.448  1.00187.73           C  
-ANISOU 3485  CD  GLU A 464    19006  29203  23119  -4620    838   3074       C  
-ATOM   3486  OE1 GLU A 464     -35.096 -22.466  16.820  1.00191.77           O  
-ANISOU 3486  OE1 GLU A 464    19692  29381  23790  -4499    834   3021       O  
-ATOM   3487  OE2 GLU A 464     -37.159 -22.931  17.411  1.00192.99           O  
-ANISOU 3487  OE2 GLU A 464    19844  30122  23361  -5008    872   3197       O  
-ATOM   3488  N   ASN A 465     -34.082 -20.117  22.211  1.00152.78           N  
-ANISOU 3488  N   ASN A 465    14204  24237  19608  -3194    508   2329       N  
-ATOM   3489  CA  ASN A 465     -33.913 -19.122  23.262  1.00153.67           C  
-ANISOU 3489  CA  ASN A 465    14001  24365  20020  -2833    445   2191       C  
-ATOM   3490  C   ASN A 465     -32.446 -18.757  23.456  1.00152.42           C  
-ANISOU 3490  C   ASN A 465    13859  23774  20278  -2393    380   2001       C  
-ATOM   3491  O   ASN A 465     -32.023 -18.409  24.559  1.00152.57           O  
-ANISOU 3491  O   ASN A 465    13838  23673  20458  -2100    302   1833       O  
-ATOM   3492  CB  ASN A 465     -34.499 -19.639  24.577  1.00152.78           C  
-ANISOU 3492  CB  ASN A 465    14087  24376  19587  -2934    393   2122       C  
-ATOM   3493  CG  ASN A 465     -35.909 -20.179  24.416  1.00155.05           C  
-ANISOU 3493  CG  ASN A 465    14430  25064  19419  -3396    455   2301       C  
-ATOM   3494  OD1 ASN A 465     -36.889 -19.477  24.663  1.00155.55           O  
-ANISOU 3494  OD1 ASN A 465    14133  25495  19475  -3452    482   2374       O  
-ATOM   3495  ND2 ASN A 465     -36.016 -21.435  23.997  1.00154.20           N  
-ANISOU 3495  ND2 ASN A 465    14773  24886  18929  -3729    477   2371       N  
-ATOM   3496  N   HIS A 466     -31.677 -18.839  22.374  1.00169.62           N  
-ANISOU 3496  N   HIS A 466    16097  25723  22629  -2351    413   2029       N  
-ATOM   3497  CA  HIS A 466     -30.243 -18.575  22.415  1.00166.76           C  
-ANISOU 3497  CA  HIS A 466    15776  24934  22651  -1958    359   1857       C  
-ATOM   3498  C   HIS A 466     -29.601 -19.252  23.620  1.00166.60           C  
-ANISOU 3498  C   HIS A 466    16134  24633  22535  -1812    260   1657       C  
-ATOM   3499  O   HIS A 466     -28.829 -18.637  24.354  1.00165.83           O  
-ANISOU 3499  O   HIS A 466    15910  24331  22765  -1422    190   1486       O  
-ATOM   3500  CB  HIS A 466     -29.969 -17.071  22.441  1.00167.01           C  
-ANISOU 3500  CB  HIS A 466    15262  25005  23188  -1583    351   1816       C  
-ATOM   3501  CG  HIS A 466     -28.562 -16.709  22.076  1.00164.94           C  
-ANISOU 3501  CG  HIS A 466    14982  24341  23346  -1225    323   1690       C  
-ATOM   3502  ND1 HIS A 466     -27.930 -17.217  20.961  1.00164.70           N  
-ANISOU 3502  ND1 HIS A 466    15153  24096  23328  -1311    367   1736       N  
-ATOM   3503  CD2 HIS A 466     -27.665 -15.891  22.676  1.00163.98           C  
-ANISOU 3503  CD2 HIS A 466    14662  23996  23646   -781    257   1518       C  
-ATOM   3504  CE1 HIS A 466     -26.705 -16.728  20.890  1.00163.81           C  
-ANISOU 3504  CE1 HIS A 466    14968  23646  23627   -937    330   1597       C  
-ATOM   3505  NE2 HIS A 466     -26.519 -15.920  21.919  1.00163.64           N  
-ANISOU 3505  NE2 HIS A 466    14704  23610  23862   -610    262   1464       N  
-ATOM   3506  N   GLU A 467     -29.932 -20.522  23.820  1.00160.03           N  
-ANISOU 3506  N   GLU A 467    15764  23791  21249  -2128    253   1682       N  
-ATOM   3507  CA  GLU A 467     -29.402 -21.278  24.945  1.00159.86           C  
-ANISOU 3507  CA  GLU A 467    16140  23515  21086  -2035    158   1506       C  
-ATOM   3508  C   GLU A 467     -29.316 -22.759  24.597  1.00157.22           C  
-ANISOU 3508  C   GLU A 467    16364  23029  20344  -2359    160   1540       C  
-ATOM   3509  O   GLU A 467     -30.314 -23.382  24.239  1.00160.20           O  
-ANISOU 3509  O   GLU A 467    16864  23671  20332  -2762    215   1701       O  
-ATOM   3510  CB  GLU A 467     -30.272 -21.074  26.186  1.00163.59           C  
-ANISOU 3510  CB  GLU A 467    16510  24258  21389  -2062    122   1479       C  
-ATOM   3511  CG  GLU A 467     -29.665 -21.628  27.465  1.00170.11           C  
-ANISOU 3511  CG  GLU A 467    17674  24820  22141  -1894     15   1280       C  
-ATOM   3512  CD  GLU A 467     -29.494 -20.565  28.535  1.00171.08           C  
-ANISOU 3512  CD  GLU A 467    17458  24965  22579  -1515    -46   1139       C  
-ATOM   3513  OE1 GLU A 467     -30.518 -20.062  29.044  1.00172.24           O  
-ANISOU 3513  OE1 GLU A 467    17333  25476  22634  -1597    -29   1201       O  
-ATOM   3514  OE2 GLU A 467     -28.336 -20.231  28.865  1.00171.60           O  
-ANISOU 3514  OE2 GLU A 467    17528  24686  22988  -1133   -113    964       O  
-ATOM   3515  N   PHE A 468     -28.117 -23.318  24.706  1.00141.36           N  
-ANISOU 3515  N   PHE A 468    14691  20590  18430  -2178     97   1386       N  
-ATOM   3516  CA  PHE A 468     -27.882 -24.696  24.300  1.00136.41           C  
-ANISOU 3516  CA  PHE A 468    14594  19773  17464  -2450     92   1404       C  
-ATOM   3517  C   PHE A 468     -27.673 -25.598  25.509  1.00134.12           C  
-ANISOU 3517  C   PHE A 468    14735  19307  16919  -2455     -7   1261       C  
-ATOM   3518  O   PHE A 468     -26.577 -25.660  26.065  1.00132.26           O  
-ANISOU 3518  O   PHE A 468    14659  18706  16889  -2146    -90   1069       O  
-ATOM   3519  CB  PHE A 468     -26.669 -24.764  23.377  1.00133.39           C  
-ANISOU 3519  CB  PHE A 468    14302  19024  17355  -2277     98   1345       C  
-ATOM   3520  CG  PHE A 468     -26.572 -23.606  22.426  1.00129.52           C  
-ANISOU 3520  CG  PHE A 468    13329  18632  17251  -2123    171   1426       C  
-ATOM   3521  CD1 PHE A 468     -27.092 -23.695  21.147  1.00128.68           C  
-ANISOU 3521  CD1 PHE A 468    13141  18711  17039  -2406    270   1620       C  
-ATOM   3522  CD2 PHE A 468     -25.967 -22.423  22.818  1.00127.67           C  
-ANISOU 3522  CD2 PHE A 468    12720  18304  17483  -1697    139   1309       C  
-ATOM   3523  CE1 PHE A 468     -27.005 -22.628  20.273  1.00128.20           C  
-ANISOU 3523  CE1 PHE A 468    12638  18740  17331  -2268    335   1698       C  
-ATOM   3524  CE2 PHE A 468     -25.877 -21.353  21.950  1.00127.59           C  
-ANISOU 3524  CE2 PHE A 468    12266  18382  17829  -1557    202   1386       C  
-ATOM   3525  CZ  PHE A 468     -26.396 -21.455  20.676  1.00127.71           C  
-ANISOU 3525  CZ  PHE A 468    12208  18582  17734  -1844    301   1581       C  
-ATOM   3526  N   LEU A 469     -28.729 -26.296  25.912  1.00134.33           N  
-ANISOU 3526  N   LEU A 469    14950  19593  16496  -2808      3   1357       N  
-ATOM   3527  CA  LEU A 469     -28.657 -27.174  27.072  1.00130.96           C  
-ANISOU 3527  CA  LEU A 469    14934  19037  15789  -2851    -89   1240       C  
-ATOM   3528  C   LEU A 469     -29.012 -28.611  26.709  1.00128.80           C  
-ANISOU 3528  C   LEU A 469    15158  18747  15032  -3273    -80   1330       C  
-ATOM   3529  O   LEU A 469     -29.530 -28.880  25.624  1.00130.04           O  
-ANISOU 3529  O   LEU A 469    15308  19067  15036  -3566      5   1502       O  
-ATOM   3530  CB  LEU A 469     -29.568 -26.664  28.189  1.00132.99           C  
-ANISOU 3530  CB  LEU A 469    14966  19610  15953  -2846   -105   1238       C  
-ATOM   3531  CG  LEU A 469     -29.259 -25.256  28.703  1.00133.33           C  
-ANISOU 3531  CG  LEU A 469    14523  19678  16458  -2423   -126   1137       C  
-ATOM   3532  CD1 LEU A 469     -30.187 -24.888  29.853  1.00134.36           C  
-ANISOU 3532  CD1 LEU A 469    14481  20120  16449  -2448   -147   1130       C  
-ATOM   3533  CD2 LEU A 469     -27.804 -25.147  29.129  1.00133.62           C  
-ANISOU 3533  CD2 LEU A 469    14685  19251  16833  -2006   -217    914       C  
-ATOM   3534  N   VAL A 470     -28.732 -29.528  27.628  1.00 99.24           N  
-ANISOU 3534  N   VAL A 470    11849  14806  11051  -3301   -171   1213       N  
-ATOM   3535  CA  VAL A 470     -28.944 -30.950  27.390  1.00 96.97           C  
-ANISOU 3535  CA  VAL A 470    12077  14452  10315  -3673   -181   1273       C  
-ATOM   3536  C   VAL A 470     -30.392 -31.365  27.636  1.00100.57           C  
-ANISOU 3536  C   VAL A 470    12566  15325  10321  -4086   -136   1437       C  
-ATOM   3537  O   VAL A 470     -31.033 -30.893  28.574  1.00101.39           O  
-ANISOU 3537  O   VAL A 470    12479  15662  10384  -4049   -150   1423       O  
-ATOM   3538  CB  VAL A 470     -28.029 -31.796  28.294  1.00 90.82           C  
-ANISOU 3538  CB  VAL A 470    11769  13277   9462  -3536   -305   1077       C  
-ATOM   3539  CG1 VAL A 470     -28.091 -33.262  27.892  1.00 87.73           C  
-ANISOU 3539  CG1 VAL A 470    11915  12767   8651  -3896   -319   1134       C  
-ATOM   3540  CG2 VAL A 470     -26.602 -31.280  28.226  1.00 84.69           C  
-ANISOU 3540  CG2 VAL A 470    10926  12096   9155  -3088   -357    895       C  
-ATOM   3541  N   LYS A 471     -30.904 -32.248  26.783  1.00129.18           N  
-ANISOU 3541  N   LYS A 471    14884  16543  17656  -1693   4496  -3788       N  
-ATOM   3542  CA  LYS A 471     -32.221 -32.833  26.986  1.00133.90           C  
-ANISOU 3542  CA  LYS A 471    15538  17217  18119  -1920   4823  -3864       C  
-ATOM   3543  C   LYS A 471     -32.272 -33.478  28.362  1.00138.37           C  
-ANISOU 3543  C   LYS A 471    16599  17425  18552  -1841   4927  -3848       C  
-ATOM   3544  O   LYS A 471     -31.558 -34.449  28.613  1.00138.59           O  
-ANISOU 3544  O   LYS A 471    16905  17176  18577  -1817   4941  -3875       O  
-ATOM   3545  CB  LYS A 471     -32.503 -33.913  25.937  1.00134.27           C  
-ANISOU 3545  CB  LYS A 471    15438  17390  18189  -2196   5035  -3990       C  
-ATOM   3546  CG  LYS A 471     -32.670 -33.425  24.509  1.00132.48           C  
-ANISOU 3546  CG  LYS A 471    14712  17545  18079  -2329   4995  -4027       C  
-ATOM   3547  CD  LYS A 471     -33.036 -34.591  23.598  1.00136.29           C  
-ANISOU 3547  CD  LYS A 471    15095  18125  18563  -2610   5235  -4155       C  
-ATOM   3548  CE  LYS A 471     -33.137 -34.168  22.142  1.00137.82           C  
-ANISOU 3548  CE  LYS A 471    14798  18689  18880  -2744   5192  -4195       C  
-ATOM   3549  NZ  LYS A 471     -34.223 -33.176  21.917  1.00140.12           N  
-ANISOU 3549  NZ  LYS A 471    14787  19308  19145  -2817   5243  -4178       N  
-ATOM   3550  N   PRO A 472     -33.113 -32.946  29.263  1.00138.24           N  
-ANISOU 3550  N   PRO A 472    16694  17408  18421  -1800   5001  -3803       N  
-ATOM   3551  CA  PRO A 472     -33.295 -33.628  30.547  1.00142.18           C  
-ANISOU 3551  CA  PRO A 472    17656  17583  18782  -1754   5134  -3797       C  
-ATOM   3552  C   PRO A 472     -33.716 -35.072  30.305  1.00145.18           C  
-ANISOU 3552  C   PRO A 472    18166  17897  19098  -1999   5424  -3916       C  
-ATOM   3553  O   PRO A 472     -33.535 -35.931  31.165  1.00146.93           O  
-ANISOU 3553  O   PRO A 472    18784  17808  19236  -1970   5517  -3928       O  
-ATOM   3554  CB  PRO A 472     -34.442 -32.851  31.195  1.00144.71           C  
-ANISOU 3554  CB  PRO A 472    17955  18033  18995  -1757   5227  -3758       C  
-ATOM   3555  CG  PRO A 472     -34.378 -31.500  30.580  1.00143.14           C  
-ANISOU 3555  CG  PRO A 472    17370  18119  18897  -1670   5015  -3695       C  
-ATOM   3556  CD  PRO A 472     -33.911 -31.711  29.170  1.00139.07           C  
-ANISOU 3556  CD  PRO A 472    16519  17803  18520  -1788   4963  -3755       C  
-ATOM   3557  N   SER A 473     -34.268 -35.328  29.124  1.00121.65           N  
-ANISOU 3557  N   SER A 473    14850  15211  16160  -2240   5563  -4003       N  
-ATOM   3558  CA  SER A 473     -34.742 -36.657  28.762  1.00123.25           C  
-ANISOU 3558  CA  SER A 473    15128  15394  16308  -2494   5845  -4121       C  
-ATOM   3559  C   SER A 473     -33.640 -37.525  28.154  1.00122.60           C  
-ANISOU 3559  C   SER A 473    15091  15168  16322  -2500   5772  -4167       C  
-ATOM   3560  O   SER A 473     -33.915 -38.431  27.367  1.00124.73           O  
-ANISOU 3560  O   SER A 473    15263  15528  16599  -2727   5956  -4269       O  
-ATOM   3561  CB  SER A 473     -35.925 -36.549  27.799  1.00123.97           C  
-ANISOU 3561  CB  SER A 473    14841  15871  16390  -2760   6045  -4195       C  
-ATOM   3562  OG  SER A 473     -35.626 -35.677  26.721  1.00121.40           O  
-ANISOU 3562  OG  SER A 473    14090  15833  16203  -2744   5863  -4176       O  
-ATOM   3563  N   PHE A 474     -32.394 -37.241  28.518  1.00135.19           N  
-ANISOU 3563  N   PHE A 474    16834  16541  17991  -2251   5505  -4090       N  
-ATOM   3564  CA  PHE A 474     -31.263 -38.049  28.071  1.00134.16           C  
-ANISOU 3564  CA  PHE A 474    16787  16238  17948  -2228   5418  -4123       C  
-ATOM   3565  C   PHE A 474     -30.746 -38.922  29.209  1.00133.27           C  
-ANISOU 3565  C   PHE A 474    17178  15706  17754  -2121   5452  -4113       C  
-ATOM   3566  O   PHE A 474     -30.871 -40.146  29.172  1.00134.01           O  
-ANISOU 3566  O   PHE A 474    17450  15673  17796  -2276   5654  -4199       O  
-ATOM   3567  CB  PHE A 474     -30.140 -37.160  27.535  1.00130.94           C  
-ANISOU 3567  CB  PHE A 474    16164  15890  17697  -2031   5084  -4050       C  
-ATOM   3568  CG  PHE A 474     -28.826 -37.869  27.392  1.00130.07           C  
-ANISOU 3568  CG  PHE A 474    16221  15531  17667  -1936   4950  -4056       C  
-ATOM   3569  CD1 PHE A 474     -28.605 -38.742  26.341  1.00129.58           C  
-ANISOU 3569  CD1 PHE A 474    16016  15548  17670  -2116   5039  -4152       C  
-ATOM   3570  CD2 PHE A 474     -27.811 -37.661  28.310  1.00130.00           C  
-ANISOU 3570  CD2 PHE A 474    16514  15210  17669  -1666   4735  -3967       C  
-ATOM   3571  CE1 PHE A 474     -27.397 -39.396  26.209  1.00128.14           C  
-ANISOU 3571  CE1 PHE A 474    15989  15138  17561  -2028   4916  -4158       C  
-ATOM   3572  CE2 PHE A 474     -26.599 -38.311  28.183  1.00128.89           C  
-ANISOU 3572  CE2 PHE A 474    16529  14842  17603  -1577   4611  -3972       C  
-ATOM   3573  CZ  PHE A 474     -26.391 -39.180  27.130  1.00127.92           C  
-ANISOU 3573  CZ  PHE A 474    16261  14801  17543  -1758   4702  -4068       C  
-ATOM   3574  N   ASP A 475     -30.161 -38.282  30.215  1.00160.91           N  
-ANISOU 3574  N   ASP A 475    20904  18991  21243  -1855   5251  -4007       N  
-ATOM   3575  CA  ASP A 475     -29.756 -38.971  31.433  1.00160.34           C  
-ANISOU 3575  CA  ASP A 475    21319  18520  21081  -1735   5278  -3985       C  
-ATOM   3576  C   ASP A 475     -30.874 -38.829  32.459  1.00159.34           C  
-ANISOU 3576  C   ASP A 475    21381  18362  20798  -1764   5459  -3969       C  
-ATOM   3577  O   ASP A 475     -31.169 -37.720  32.906  1.00157.08           O  
-ANISOU 3577  O   ASP A 475    21024  18162  20496  -1634   5350  -3887       O  
-ATOM   3578  CB  ASP A 475     -28.451 -38.381  31.976  1.00163.96           C  
-ANISOU 3578  CB  ASP A 475    21933  18750  21616  -1425   4955  -3877       C  
-ATOM   3579  CG  ASP A 475     -27.980 -39.070  33.245  1.00169.43           C  
-ANISOU 3579  CG  ASP A 475    23131  19024  22220  -1291   4970  -3850       C  
-ATOM   3580  OD1 ASP A 475     -28.233 -40.283  33.397  1.00174.45           O  
-ANISOU 3580  OD1 ASP A 475    23988  19515  22781  -1441   5194  -3932       O  
-ATOM   3581  OD2 ASP A 475     -27.352 -38.398  34.089  1.00174.23           O  
-ANISOU 3581  OD2 ASP A 475    23918  19448  22833  -1034   4757  -3746       O  
-ATOM   3582  N   PRO A 476     -31.506 -39.953  32.830  1.00102.82           N  
-ANISOU 3582  N   PRO A 476    14463  11079  13524  -1935   5738  -4048       N  
-ATOM   3583  CA  PRO A 476     -32.665 -39.951  33.730  1.00104.03           C  
-ANISOU 3583  CA  PRO A 476    14789  11216  13522  -1999   5947  -4047       C  
-ATOM   3584  C   PRO A 476     -32.337 -39.318  35.080  1.00104.05           C  
-ANISOU 3584  C   PRO A 476    15097  10969  13467  -1730   5794  -3936       C  
-ATOM   3585  O   PRO A 476     -33.242 -38.934  35.823  1.00104.65           O  
-ANISOU 3585  O   PRO A 476    15257  11072  13432  -1732   5901  -3908       O  
-ATOM   3586  CB  PRO A 476     -32.994 -41.441  33.887  1.00105.78           C  
-ANISOU 3586  CB  PRO A 476    15270  11268  13652  -2191   6223  -4148       C  
-ATOM   3587  CG  PRO A 476     -31.738 -42.154  33.530  1.00105.54           C  
-ANISOU 3587  CG  PRO A 476    15344  11039  13716  -2131   6101  -4168       C  
-ATOM   3588  CD  PRO A 476     -31.081 -41.318  32.480  1.00103.70           C  
-ANISOU 3588  CD  PRO A 476    14726  11032  13644  -2063   5861  -4138       C  
-ATOM   3589  N   ASN A 477     -31.048 -39.210  35.383  1.00142.94           N  
-ANISOU 3589  N   ASN A 477    20186  15655  18469  -1501   5545  -3872       N  
-ATOM   3590  CA  ASN A 477     -30.602 -38.536  36.595  1.00141.24           C  
-ANISOU 3590  CA  ASN A 477    20241  15206  18218  -1228   5365  -3759       C  
-ATOM   3591  C   ASN A 477     -30.999 -37.062  36.591  1.00137.48           C  
-ANISOU 3591  C   ASN A 477    19500  14971  17765  -1122   5219  -3677       C  
-ATOM   3592  O   ASN A 477     -31.581 -36.564  37.555  1.00135.26           O  
-ANISOU 3592  O   ASN A 477    19372  14637  17384  -1040   5251  -3622       O  
-ATOM   3593  CB  ASN A 477     -29.087 -38.674  36.755  1.00146.52           C  
-ANISOU 3593  CB  ASN A 477    21088  15602  18981  -1011   5111  -3709       C  
-ATOM   3594  CG  ASN A 477     -28.585 -38.113  38.072  1.00149.82           C  
-ANISOU 3594  CG  ASN A 477    21828  15741  19355   -730   4936  -3597       C  
-ATOM   3595  OD1 ASN A 477     -29.314 -38.080  39.062  1.00154.96           O  
-ANISOU 3595  OD1 ASN A 477    22703  16297  19876   -718   5063  -3577       O  
-ATOM   3596  ND2 ASN A 477     -27.336 -37.663  38.086  1.00153.66           N  
-ANISOU 3596  ND2 ASN A 477    22338  16097  19949   -503   4643  -3523       N  
-ATOM   3597  N   LEU A 478     -30.685 -36.370  35.499  1.00128.42           N  
-ANISOU 3597  N   LEU A 478    17954  14090  16750  -1125   5061  -3669       N  
-ATOM   3598  CA  LEU A 478     -31.001 -34.952  35.372  1.00125.78           C  
-ANISOU 3598  CA  LEU A 478    17336  14003  16453  -1028   4909  -3593       C  
-ATOM   3599  C   LEU A 478     -32.505 -34.701  35.341  1.00127.75           C  
-ANISOU 3599  C   LEU A 478    17426  14511  16601  -1216   5145  -3630       C  
-ATOM   3600  O   LEU A 478     -33.006 -33.815  36.032  1.00129.88           O  
-ANISOU 3600  O   LEU A 478    17717  14820  16812  -1110   5104  -3559       O  
-ATOM   3601  CB  LEU A 478     -30.353 -34.367  34.117  1.00122.96           C  
-ANISOU 3601  CB  LEU A 478    16574  13885  16262  -1015   4705  -3587       C  
-ATOM   3602  CG  LEU A 478     -28.825 -34.418  34.056  1.00121.65           C  
-ANISOU 3602  CG  LEU A 478    16508  13501  16211   -812   4435  -3539       C  
-ATOM   3603  CD1 LEU A 478     -28.327 -33.954  32.696  1.00118.94           C  
-ANISOU 3603  CD1 LEU A 478    15738  13426  16027   -845   4276  -3550       C  
-ATOM   3604  CD2 LEU A 478     -28.210 -33.587  35.170  1.00120.61           C  
-ANISOU 3604  CD2 LEU A 478    16609  13149  16068   -509   4199  -3413       C  
-ATOM   3605  N   SER A 479     -33.220 -35.483  34.538  1.00106.00           N  
-ANISOU 3605  N   SER A 479    14515  11933  13829  -1494   5391  -3740       N  
-ATOM   3606  CA  SER A 479     -34.660 -35.304  34.383  1.00110.08           C  
-ANISOU 3606  CA  SER A 479    14853  12716  14256  -1695   5626  -3784       C  
-ATOM   3607  C   SER A 479     -35.353 -35.265  35.740  1.00115.03           C  
-ANISOU 3607  C   SER A 479    15810  13169  14726  -1633   5745  -3745       C  
-ATOM   3608  O   SER A 479     -36.338 -34.551  35.924  1.00115.64           O  
-ANISOU 3608  O   SER A 479    15754  13443  14740  -1672   5819  -3724       O  
-ATOM   3609  CB  SER A 479     -35.252 -36.418  33.517  1.00108.42           C  
-ANISOU 3609  CB  SER A 479    14530  12635  14030  -2000   5899  -3914       C  
-ATOM   3610  OG  SER A 479     -36.557 -36.081  33.077  1.00105.44           O  
-ANISOU 3610  OG  SER A 479    13878  12583  13601  -2197   6086  -3954       O  
-ATOM   3611  N   GLU A 480     -34.832 -36.039  36.687  1.00133.29           N  
-ANISOU 3611  N   GLU A 480    18554  15113  16977  -1538   5764  -3736       N  
-ATOM   3612  CA  GLU A 480     -35.337 -36.025  38.054  1.00138.62           C  
-ANISOU 3612  CA  GLU A 480    19579  15583  17508  -1452   5853  -3692       C  
-ATOM   3613  C   GLU A 480     -35.085 -34.668  38.694  1.00138.34           C  
-ANISOU 3613  C   GLU A 480    19530  15543  17489  -1192   5606  -3568       C  
-ATOM   3614  O   GLU A 480     -35.996 -34.044  39.236  1.00137.47           O  
-ANISOU 3614  O   GLU A 480    19409  15533  17289  -1188   5679  -3535       O  
-ATOM   3615  CB  GLU A 480     -34.661 -37.114  38.888  1.00145.08           C  
-ANISOU 3615  CB  GLU A 480    20857  15993  18274  -1383   5889  -3703       C  
-ATOM   3616  CG  GLU A 480     -35.102 -38.528  38.556  1.00156.40           C  
-ANISOU 3616  CG  GLU A 480    22388  17387  19650  -1640   6177  -3824       C  
-ATOM   3617  CD  GLU A 480     -34.385 -39.567  39.396  1.00163.52           C  
-ANISOU 3617  CD  GLU A 480    23747  17881  20504  -1560   6198  -3830       C  
-ATOM   3618  OE1 GLU A 480     -33.153 -39.445  39.568  1.00168.48           O  
-ANISOU 3618  OE1 GLU A 480    24494  18304  21215  -1353   5957  -3774       O  
-ATOM   3619  OE2 GLU A 480     -35.053 -40.499  39.891  1.00168.36           O  
-ANISOU 3619  OE2 GLU A 480    24600  18376  20995  -1702   6454  -3891       O  
-ATOM   3620  N   LEU A 481     -33.836 -34.219  38.622  1.00125.52           N  
-ANISOU 3620  N   LEU A 481    17907  13803  15980   -976   5313  -3500       N  
-ATOM   3621  CA  LEU A 481     -33.425 -32.961  39.234  1.00127.18           C  
-ANISOU 3621  CA  LEU A 481    18125  13979  16218   -708   5051  -3378       C  
-ATOM   3622  C   LEU A 481     -34.252 -31.782  38.734  1.00131.83           C  
-ANISOU 3622  C   LEU A 481    18325  14939  16825   -750   5027  -3352       C  
-ATOM   3623  O   LEU A 481     -34.562 -30.867  39.496  1.00132.55           O  
-ANISOU 3623  O   LEU A 481    18468  15030  16864   -604   4946  -3270       O  
-ATOM   3624  CB  LEU A 481     -31.939 -32.706  38.984  1.00119.40           C  
-ANISOU 3624  CB  LEU A 481    17138  12857  15373   -501   4743  -3321       C  
-ATOM   3625  CG  LEU A 481     -30.933 -33.472  39.846  1.00115.43           C  
-ANISOU 3625  CG  LEU A 481    17075  11932  14852   -347   4673  -3298       C  
-ATOM   3626  CD1 LEU A 481     -31.416 -34.879  40.165  1.00112.84           C  
-ANISOU 3626  CD1 LEU A 481    17023  11437  14413   -534   4970  -3393       C  
-ATOM   3627  CD2 LEU A 481     -29.577 -33.506  39.160  1.00112.14           C  
-ANISOU 3627  CD2 LEU A 481    16566  11454  14588   -240   4432  -3282       C  
-ATOM   3628  N   ARG A 482     -34.604 -31.805  37.453  1.00166.15           N  
-ANISOU 3628  N   ARG A 482    22283  19601  21244   -948   5095  -3422       N  
-ATOM   3629  CA  ARG A 482     -35.436 -30.753  36.881  1.00171.55           C  
-ANISOU 3629  CA  ARG A 482    22577  20657  21947  -1013   5091  -3407       C  
-ATOM   3630  C   ARG A 482     -36.858 -30.853  37.423  1.00177.88           C  
-ANISOU 3630  C   ARG A 482    23445  21546  22595  -1161   5365  -3438       C  
-ATOM   3631  O   ARG A 482     -37.530 -29.842  37.625  1.00177.76           O  
-ANISOU 3631  O   ARG A 482    23280  21713  22548  -1118   5337  -3387       O  
-ATOM   3632  CB  ARG A 482     -35.434 -30.826  35.353  1.00169.53           C  
-ANISOU 3632  CB  ARG A 482    21896  20709  21809  -1197   5103  -3479       C  
-ATOM   3633  CG  ARG A 482     -36.306 -29.774  34.685  1.00166.35           C  
-ANISOU 3633  CG  ARG A 482    21073  20703  21430  -1279   5106  -3470       C  
-ATOM   3634  CD  ARG A 482     -35.893 -28.368  35.093  1.00162.86           C  
-ANISOU 3634  CD  ARG A 482    20557  20287  21035  -1018   4820  -3347       C  
-ATOM   3635  NE  ARG A 482     -34.553 -28.029  34.623  1.00160.01           N  
-ANISOU 3635  NE  ARG A 482    20106  19866  20823   -848   4525  -3300       N  
-ATOM   3636  CZ  ARG A 482     -33.948 -26.869  34.860  1.00157.40           C  
-ANISOU 3636  CZ  ARG A 482    19707  19538  20560   -608   4239  -3193       C  
-ATOM   3637  NH1 ARG A 482     -34.562 -25.930  35.569  1.00156.58           N  
-ANISOU 3637  NH1 ARG A 482    19616  19492  20386   -508   4210  -3123       N  
-ATOM   3638  NH2 ARG A 482     -32.726 -26.649  34.391  1.00155.46           N  
-ANISOU 3638  NH2 ARG A 482    19381  19237  20450   -468   3983  -3156       N  
-ATOM   3639  N   GLU A 483     -37.310 -32.080  37.661  1.00182.15           N  
-ANISOU 3639  N   GLU A 483    30738  18585  19886  -1279   5090  -2679       N  
-ATOM   3640  CA  GLU A 483     -38.617 -32.309  38.262  1.00184.97           C  
-ANISOU 3640  CA  GLU A 483    31245  18551  20485  -1515   5151  -2535       C  
-ATOM   3641  C   GLU A 483     -38.647 -31.839  39.714  1.00182.81           C  
-ANISOU 3641  C   GLU A 483    31014  18247  20197  -1628   5287  -2321       C  
-ATOM   3642  O   GLU A 483     -39.615 -31.221  40.157  1.00181.38           O  
-ANISOU 3642  O   GLU A 483    30800  17990  20128  -1876   5405  -2188       O  
-ATOM   3643  CB  GLU A 483     -38.998 -33.789  38.178  1.00193.66           C  
-ANISOU 3643  CB  GLU A 483    32592  19255  21735  -1405   4986  -2594       C  
-ATOM   3644  CG  GLU A 483     -40.155 -34.182  39.083  1.00203.07           C  
-ANISOU 3644  CG  GLU A 483    33951  20065  23140  -1641   5034  -2383       C  
-ATOM   3645  CD  GLU A 483     -41.403 -33.359  38.831  1.00206.88           C  
-ANISOU 3645  CD  GLU A 483    34309  20537  23758  -1954   5169  -2301       C  
-ATOM   3646  OE1 GLU A 483     -41.563 -32.846  37.704  1.00209.21           O  
-ANISOU 3646  OE1 GLU A 483    34452  20985  24052  -1982   5163  -2440       O  
-ATOM   3647  OE2 GLU A 483     -42.222 -33.222  39.765  1.00209.88           O  
-ANISOU 3647  OE2 GLU A 483    34733  20779  24233  -2166   5277  -2100       O  
-ATOM   3648  N   ILE A 484     -37.581 -32.136  40.450  1.00173.79           N  
-ANISOU 3648  N   ILE A 484    29940  17186  18908  -1427   5263  -2303       N  
-ATOM   3649  CA  ILE A 484     -37.485 -31.747  41.852  1.00171.60           C  
-ANISOU 3649  CA  ILE A 484    29706  16902  18593  -1492   5380  -2115       C  
-ATOM   3650  C   ILE A 484     -37.456 -30.231  42.002  1.00165.85           C  
-ANISOU 3650  C   ILE A 484    28762  16463  17789  -1640   5500  -2053       C  
-ATOM   3651  O   ILE A 484     -38.219 -29.663  42.779  1.00164.34           O  
-ANISOU 3651  O   ILE A 484    28562  16208  17671  -1822   5606  -1917       O  
-ATOM   3652  CB  ILE A 484     -36.236 -32.346  42.525  1.00173.90           C  
-ANISOU 3652  CB  ILE A 484    30105  17243  18727  -1223   5317  -2129       C  
-ATOM   3653  CG1 ILE A 484     -36.263 -33.873  42.434  1.00177.91           C  
-ANISOU 3653  CG1 ILE A 484    30853  17420  19324  -1064   5144  -2195       C  
-ATOM   3654  CG2 ILE A 484     -36.151 -31.897  43.973  1.00176.67           C  
-ANISOU 3654  CG2 ILE A 484    30489  17603  19033  -1288   5441  -1936       C  
-ATOM   3655  CD1 ILE A 484     -35.086 -34.549  43.099  1.00179.13           C  
-ANISOU 3655  CD1 ILE A 484    31139  17586  19336   -787   5053  -2224       C  
-ATOM   3656  N   MET A 485     -36.571 -29.581  41.255  1.00166.43           N  
-ANISOU 3656  N   MET A 485    28657  16870  17710  -1558   5458  -2151       N  
-ATOM   3657  CA  MET A 485     -36.495 -28.126  41.270  1.00159.85           C  
-ANISOU 3657  CA  MET A 485    27622  16296  16819  -1712   5509  -2088       C  
-ATOM   3658  C   MET A 485     -37.851 -27.503  40.956  1.00157.11           C  
-ANISOU 3658  C   MET A 485    27218  15826  16650  -1978   5558  -2058       C  
-ATOM   3659  O   MET A 485     -38.286 -26.580  41.640  1.00156.65           O  
-ANISOU 3659  O   MET A 485    27110  15787  16623  -2119   5617  -1961       O  
-ATOM   3660  CB  MET A 485     -35.441 -27.625  40.281  1.00159.95           C  
-ANISOU 3660  CB  MET A 485    27430  16693  16649  -1626   5424  -2177       C  
-ATOM   3661  CG  MET A 485     -34.008 -27.816  40.749  1.00157.37           C  
-ANISOU 3661  CG  MET A 485    27095  16593  16106  -1392   5387  -2180       C  
-ATOM   3662  SD  MET A 485     -32.811 -27.105  39.604  1.00155.63           S  
-ANISOU 3662  SD  MET A 485    26576  16914  15641  -1336   5290  -2239       S  
-ATOM   3663  CE  MET A 485     -33.179 -28.030  38.116  1.00153.94           C  
-ANISOU 3663  CE  MET A 485    26343  16697  15452  -1235   5215  -2447       C  
-ATOM   3664  N   ASN A 486     -38.516 -28.014  39.924  1.00147.22           N  
-ANISOU 3664  N   ASN A 486    25975  14452  15510  -2025   5519  -2157       N  
-ATOM   3665  CA  ASN A 486     -39.842 -27.528  39.549  1.00144.67           C  
-ANISOU 3665  CA  ASN A 486    25605  14001  15362  -2269   5562  -2143       C  
-ATOM   3666  C   ASN A 486     -40.865 -27.724  40.664  1.00143.44           C  
-ANISOU 3666  C   ASN A 486    25572  13594  15335  -2389   5661  -2014       C  
-ATOM   3667  O   ASN A 486     -41.840 -26.978  40.762  1.00142.85           O  
-ANISOU 3667  O   ASN A 486    25424  13497  15354  -2582   5715  -1976       O  
-ATOM   3668  CB  ASN A 486     -40.324 -28.198  38.258  1.00143.43           C  
-ANISOU 3668  CB  ASN A 486    25454  13741  15302  -2271   5493  -2279       C  
-ATOM   3669  CG  ASN A 486     -40.193 -27.292  37.040  1.00141.99           C  
-ANISOU 3669  CG  ASN A 486    25054  13828  15067  -2352   5442  -2363       C  
-ATOM   3670  OD1 ASN A 486     -39.335 -27.504  36.182  1.00140.60           O  
-ANISOU 3670  OD1 ASN A 486    24790  13880  14753  -2200   5359  -2469       O  
-ATOM   3671  ND2 ASN A 486     -41.057 -26.283  36.957  1.00138.32           N  
-ANISOU 3671  ND2 ASN A 486    24495  13359  14703  -2587   5479  -2315       N  
-ATOM   3672  N   ASP A 487     -40.635 -28.733  41.498  1.00145.08           N  
-ANISOU 3672  N   ASP A 487    25956  13634  15533  -2272   5671  -1944       N  
-ATOM   3673  CA  ASP A 487     -41.475 -28.980  42.665  1.00143.35           C  
-ANISOU 3673  CA  ASP A 487    25836  13239  15393  -2380   5763  -1784       C  
-ATOM   3674  C   ASP A 487     -41.154 -27.980  43.774  1.00140.05           C  
-ANISOU 3674  C   ASP A 487    25339  13017  14855  -2376   5842  -1695       C  
-ATOM   3675  O   ASP A 487     -42.051 -27.348  44.331  1.00137.61           O  
-ANISOU 3675  O   ASP A 487    24968  12726  14591  -2519   5919  -1626       O  
-ATOM   3676  CB  ASP A 487     -41.293 -30.418  43.162  1.00148.42           C  
-ANISOU 3676  CB  ASP A 487    26695  13633  16064  -2271   5711  -1716       C  
-ATOM   3677  CG  ASP A 487     -41.957 -30.664  44.505  1.00149.43           C  
-ANISOU 3677  CG  ASP A 487    26904  13651  16222  -2379   5804  -1506       C  
-ATOM   3678  OD1 ASP A 487     -43.194 -30.837  44.540  1.00150.60           O  
-ANISOU 3678  OD1 ASP A 487    27052  13662  16506  -2581   5846  -1418       O  
-ATOM   3679  OD2 ASP A 487     -41.238 -30.694  45.526  1.00154.05           O  
-ANISOU 3679  OD2 ASP A 487    27540  14311  16682  -2261   5835  -1422       O  
-ATOM   3680  N   LEU A 488     -39.869 -27.837  44.087  1.00123.57           N  
-ANISOU 3680  N   LEU A 488    23250  11092  12608  -2194   5807  -1710       N  
-ATOM   3681  CA  LEU A 488     -39.428 -26.866  45.085  1.00121.96           C  
-ANISOU 3681  CA  LEU A 488    22975  11075  12289  -2164   5848  -1642       C  
-ATOM   3682  C   LEU A 488     -39.715 -25.445  44.618  1.00121.29           C  
-ANISOU 3682  C   LEU A 488    22704  11164  12217  -2295   5813  -1694       C  
-ATOM   3683  O   LEU A 488     -39.784 -24.518  45.421  1.00121.46           O  
-ANISOU 3683  O   LEU A 488    22664  11290  12196  -2314   5822  -1651       O  
-ATOM   3684  CB  LEU A 488     -37.931 -27.019  45.373  1.00117.36           C  
-ANISOU 3684  CB  LEU A 488    22420  10636  11535  -1945   5799  -1654       C  
-ATOM   3685  CG  LEU A 488     -37.489 -28.122  46.335  1.00116.28           C  
-ANISOU 3685  CG  LEU A 488    22471  10362  11349  -1791   5823  -1574       C  
-ATOM   3686  CD1 LEU A 488     -37.960 -29.490  45.865  1.00113.51           C  
-ANISOU 3686  CD1 LEU A 488    22279   9734  11117  -1786   5779  -1591       C  
-ATOM   3687  CD2 LEU A 488     -35.978 -28.098  46.510  1.00114.24           C  
-ANISOU 3687  CD2 LEU A 488    22207  10289  10910  -1571   5767  -1612       C  
-ATOM   3688  N   GLU A 489     -39.878 -25.283  43.311  1.00144.90           N  
-ANISOU 3688  N   GLU A 489    25609  14181  15267  -2377   5749  -1793       N  
-ATOM   3689  CA  GLU A 489     -40.124 -23.973  42.726  1.00143.74           C  
-ANISOU 3689  CA  GLU A 489    25291  14181  15143  -2519   5678  -1836       C  
-ATOM   3690  C   GLU A 489     -41.553 -23.529  43.013  1.00144.69           C  
-ANISOU 3690  C   GLU A 489    25393  14182  15400  -2686   5729  -1827       C  
-ATOM   3691  O   GLU A 489     -41.872 -22.344  42.939  1.00141.90           O  
-ANISOU 3691  O   GLU A 489    24925  13922  15069  -2785   5657  -1855       O  
-ATOM   3692  CB  GLU A 489     -39.862 -24.012  41.220  1.00145.19           C  
-ANISOU 3692  CB  GLU A 489    25380  14452  15332  -2555   5594  -1933       C  
-ATOM   3693  CG  GLU A 489     -39.573 -22.662  40.592  1.00144.05           C  
-ANISOU 3693  CG  GLU A 489    25048  14532  15151  -2675   5471  -1940       C  
-ATOM   3694  CD  GLU A 489     -39.005 -22.788  39.192  1.00146.40           C  
-ANISOU 3694  CD  GLU A 489    25230  15010  15386  -2675   5391  -2007       C  
-ATOM   3695  OE1 GLU A 489     -39.049 -23.900  38.626  1.00148.08           O  
-ANISOU 3695  OE1 GLU A 489    25512  15140  15611  -2577   5429  -2087       O  
-ATOM   3696  OE2 GLU A 489     -38.507 -21.776  38.660  1.00148.54           O  
-ANISOU 3696  OE2 GLU A 489    25334  15516  15588  -2769   5269  -1975       O  
-ATOM   3697  N   LYS A 490     -42.410 -24.488  43.348  1.00129.02           N  
-ANISOU 3697  N   LYS A 490    23520  11999  13504  -2716   5832  -1785       N  
-ATOM   3698  CA  LYS A 490     -43.797 -24.185  43.680  1.00131.84           C  
-ANISOU 3698  CA  LYS A 490    23844  12285  13966  -2867   5896  -1765       C  
-ATOM   3699  C   LYS A 490     -44.009 -24.127  45.191  1.00132.31           C  
-ANISOU 3699  C   LYS A 490    23933  12390  13947  -2810   5981  -1658       C  
-ATOM   3700  O   LYS A 490     -44.673 -23.222  45.694  1.00133.81           O  
-ANISOU 3700  O   LYS A 490    24028  12683  14132  -2857   5984  -1677       O  
-ATOM   3701  CB  LYS A 490     -44.742 -25.203  43.040  1.00136.30           C  
-ANISOU 3701  CB  LYS A 490    24478  12632  14678  -2978   5942  -1764       C  
-ATOM   3702  CG  LYS A 490     -44.719 -25.193  41.522  1.00141.15           C  
-ANISOU 3702  CG  LYS A 490    25043  13216  15370  -3033   5858  -1890       C  
-ATOM   3703  CD  LYS A 490     -45.687 -26.212  40.956  1.00146.47           C  
-ANISOU 3703  CD  LYS A 490    25798  13651  16202  -3133   5883  -1892       C  
-ATOM   3704  CE  LYS A 490     -45.579 -26.290  39.445  1.00149.06           C  
-ANISOU 3704  CE  LYS A 490    26082  13962  16591  -3149   5794  -2033       C  
-ATOM   3705  NZ  LYS A 490     -46.485 -27.332  38.887  1.00152.83           N  
-ANISOU 3705  NZ  LYS A 490    26654  14180  17234  -3229   5790  -2044       N  
-ATOM   3706  N   LYS A 491     -43.439 -25.088  45.913  1.00126.53           N  
-ANISOU 3706  N   LYS A 491    23330  11600  13147  -2695   6035  -1554       N  
-ATOM   3707  CA  LYS A 491     -43.538 -25.101  47.369  1.00126.51           C  
-ANISOU 3707  CA  LYS A 491    23351  11671  13045  -2630   6117  -1436       C  
-ATOM   3708  C   LYS A 491     -42.971 -23.813  47.951  1.00125.40           C  
-ANISOU 3708  C   LYS A 491    23111  11744  12790  -2528   6058  -1490       C  
-ATOM   3709  O   LYS A 491     -43.313 -23.417  49.064  1.00124.44           O  
-ANISOU 3709  O   LYS A 491    22953  11740  12590  -2481   6104  -1445       O  
-ATOM   3710  CB  LYS A 491     -42.803 -26.306  47.957  1.00123.74           C  
-ANISOU 3710  CB  LYS A 491    23166  11216  12635  -2513   6148  -1319       C  
-ATOM   3711  CG  LYS A 491     -43.418 -27.647  47.601  1.00120.96           C  
-ANISOU 3711  CG  LYS A 491    22939  10615  12406  -2612   6162  -1237       C  
-ATOM   3712  CD  LYS A 491     -42.846 -28.752  48.473  1.00119.97           C  
-ANISOU 3712  CD  LYS A 491    22981  10382  12219  -2509   6168  -1091       C  
-ATOM   3713  CE  LYS A 491     -41.330 -28.790  48.386  1.00118.04           C  
-ANISOU 3713  CE  LYS A 491    22798  10188  11865  -2285   6094  -1175       C  
-ATOM   3714  NZ  LYS A 491     -40.743 -29.763  49.345  1.00118.81           N  
-ANISOU 3714  NZ  LYS A 491    23061  10191  11892  -2169   6091  -1041       N  
-ATOM   3715  N   MET A 492     -42.097 -23.166  47.189  1.00155.18           N  
-ANISOU 3715  N   MET A 492    26833  15583  16546  -2494   5936  -1583       N  
-ATOM   3716  CA  MET A 492     -41.519 -21.897  47.604  1.00153.79           C  
-ANISOU 3716  CA  MET A 492    26568  15580  16287  -2424   5822  -1626       C  
-ATOM   3717  C   MET A 492     -42.494 -20.751  47.386  1.00153.84           C  
-ANISOU 3717  C   MET A 492    26450  15632  16370  -2537   5738  -1719       C  
-ATOM   3718  O   MET A 492     -42.574 -19.838  48.205  1.00153.29           O  
-ANISOU 3718  O   MET A 492    26327  15673  16244  -2465   5665  -1750       O  
-ATOM   3719  CB  MET A 492     -40.210 -21.634  46.863  1.00154.30           C  
-ANISOU 3719  CB  MET A 492    26606  15726  16296  -2375   5700  -1653       C  
-ATOM   3720  CG  MET A 492     -39.044 -22.444  47.391  1.00155.92           C  
-ANISOU 3720  CG  MET A 492    26913  15952  16377  -2199   5745  -1585       C  
-ATOM   3721  SD  MET A 492     -37.563 -22.258  46.388  1.00157.77           S  
-ANISOU 3721  SD  MET A 492    27078  16348  16518  -2145   5614  -1618       S  
-ATOM   3722  CE  MET A 492     -36.407 -23.234  47.340  1.00160.56           C  
-ANISOU 3722  CE  MET A 492    27569  16713  16723  -1907   5682  -1551       C  
-ATOM   3723  N   GLN A 493     -43.237 -20.794  46.285  1.00149.19           N  
-ANISOU 3723  N   GLN A 493    25821  14956  15910  -2696   5728  -1779       N  
-ATOM   3724  CA  GLN A 493     -44.266 -19.789  46.058  1.00150.20           C  
-ANISOU 3724  CA  GLN A 493    25842  15109  16120  -2802   5644  -1879       C  
-ATOM   3725  C   GLN A 493     -45.489 -20.103  46.914  1.00151.34           C  
-ANISOU 3725  C   GLN A 493    25978  15261  16265  -2809   5782  -1858       C  
-ATOM   3726  O   GLN A 493     -46.393 -19.280  47.042  1.00153.15           O  
-ANISOU 3726  O   GLN A 493    26112  15556  16523  -2843   5722  -1952       O  
-ATOM   3727  CB  GLN A 493     -44.655 -19.695  44.581  1.00151.17           C  
-ANISOU 3727  CB  GLN A 493    25915  15147  16374  -2973   5584  -1950       C  
-ATOM   3728  CG  GLN A 493     -45.345 -18.379  44.227  1.00150.40           C  
-ANISOU 3728  CG  GLN A 493    25706  15088  16352  -3069   5417  -2065       C  
-ATOM   3729  CD  GLN A 493     -46.358 -18.520  43.106  1.00149.60           C  
-ANISOU 3729  CD  GLN A 493    25566  14879  16396  -3245   5435  -2133       C  
-ATOM   3730  OE1 GLN A 493     -46.390 -19.530  42.403  1.00147.34           O  
-ANISOU 3730  OE1 GLN A 493    25331  14494  16159  -3300   5543  -2100       O  
-ATOM   3731  NE2 GLN A 493     -47.198 -17.504  42.939  1.00148.17           N  
-ANISOU 3731  NE2 GLN A 493    25300  14712  16286  -3320   5310  -2242       N  
-ATOM   3732  N   SER A 494     -45.508 -21.298  47.499  1.00146.79           N  
-ANISOU 3732  N   SER A 494    25494  14633  15646  -2777   5947  -1728       N  
-ATOM   3733  CA  SER A 494     -46.573 -21.682  48.421  1.00146.26           C  
-ANISOU 3733  CA  SER A 494    25401  14629  15544  -2796   6082  -1653       C  
-ATOM   3734  C   SER A 494     -46.427 -20.933  49.739  1.00144.33           C  
-ANISOU 3734  C   SER A 494    25095  14602  15142  -2626   6060  -1666       C  
-ATOM   3735  O   SER A 494     -47.389 -20.790  50.495  1.00145.98           O  
-ANISOU 3735  O   SER A 494    25214  14964  15288  -2616   6127  -1659       O  
-ATOM   3736  CB  SER A 494     -46.559 -23.192  48.675  1.00148.72           C  
-ANISOU 3736  CB  SER A 494    25837  14812  15859  -2832   6223  -1475       C  
-ATOM   3737  OG  SER A 494     -46.896 -23.916  47.505  1.00147.85           O  
-ANISOU 3737  OG  SER A 494    25781  14494  15902  -2978   6224  -1480       O  
-ATOM   3738  N   THR A 495     -45.214 -20.460  50.011  1.00138.96           N  
-ANISOU 3738  N   THR A 495    24452  13959  14387  -2482   5956  -1688       N  
-ATOM   3739  CA  THR A 495     -44.944 -19.691  51.219  1.00135.35           C  
-ANISOU 3739  CA  THR A 495    23948  13691  13787  -2295   5897  -1721       C  
-ATOM   3740  C   THR A 495     -45.032 -18.198  50.922  1.00131.47           C  
-ANISOU 3740  C   THR A 495    23361  13259  13334  -2265   5661  -1904       C  
-ATOM   3741  O   THR A 495     -44.973 -17.371  51.829  1.00130.13           O  
-ANISOU 3741  O   THR A 495    23140  13237  13067  -2099   5553  -1981       O  
-ATOM   3742  CB  THR A 495     -43.554 -20.011  51.799  1.00134.27           C  
-ANISOU 3742  CB  THR A 495    23913  13556  13546  -2145   5897  -1634       C  
-ATOM   3743  OG1 THR A 495     -42.542 -19.378  51.006  1.00133.33           O  
-ANISOU 3743  OG1 THR A 495    23803  13385  13472  -2147   5721  -1699       O  
-ATOM   3744  CG2 THR A 495     -43.317 -21.514  51.820  1.00134.10           C  
-ANISOU 3744  CG2 THR A 495    24017  13411  13522  -2186   6069  -1468       C  
-ATOM   3745  N   LEU A 496     -45.166 -17.861  49.643  1.00145.90           N  
-ANISOU 3745  N   LEU A 496    25168  14964  15305  -2422   5557  -1975       N  
-ATOM   3746  CA  LEU A 496     -45.367 -16.477  49.235  1.00142.01           C  
-ANISOU 3746  CA  LEU A 496    24592  14490  14876  -2436   5300  -2134       C  
-ATOM   3747  C   LEU A 496     -46.831 -16.099  49.416  1.00142.57           C  
-ANISOU 3747  C   LEU A 496    24564  14636  14971  -2453   5308  -2255       C  
-ATOM   3748  O   LEU A 496     -47.149 -14.986  49.837  1.00141.72           O  
-ANISOU 3748  O   LEU A 496    24385  14622  14839  -2342   5108  -2407       O  
-ATOM   3749  CB  LEU A 496     -44.948 -16.268  47.778  1.00141.45           C  
-ANISOU 3749  CB  LEU A 496    24523  14288  14935  -2613   5180  -2141       C  
-ATOM   3750  CG  LEU A 496     -45.385 -14.939  47.154  1.00139.74           C  
-ANISOU 3750  CG  LEU A 496    24223  14051  14820  -2693   4904  -2285       C  
-ATOM   3751  CD1 LEU A 496     -44.839 -13.763  47.945  1.00142.10           C  
-ANISOU 3751  CD1 LEU A 496    24506  14425  15059  -2540   4636  -2352       C  
-ATOM   3752  CD2 LEU A 496     -44.957 -14.855  45.701  1.00139.29           C  
-ANISOU 3752  CD2 LEU A 496    24154  13901  14869  -2889   4810  -2253       C  
-ATOM   3753  N   ILE A 497     -47.717 -17.034  49.087  1.00118.45           N  
-ANISOU 3753  N   ILE A 497    21502  11542  11962  -2584   5518  -2193       N  
-ATOM   3754  CA  ILE A 497     -49.147 -16.830  49.280  1.00120.21           C  
-ANISOU 3754  CA  ILE A 497    21612  11875  12187  -2610   5561  -2285       C  
-ATOM   3755  C   ILE A 497     -49.496 -16.865  50.769  1.00125.90           C  
-ANISOU 3755  C   ILE A 497    22265  12857  12716  -2420   5650  -2268       C  
-ATOM   3756  O   ILE A 497     -50.413 -16.177  51.215  1.00128.64           O  
-ANISOU 3756  O   ILE A 497    22484  13393  13001  -2330   5585  -2412       O  
-ATOM   3757  CB  ILE A 497     -49.987 -17.878  48.508  1.00115.63           C  
-ANISOU 3757  CB  ILE A 497    21040  11181  11714  -2824   5753  -2195       C  
-ATOM   3758  CG1 ILE A 497     -50.088 -17.507  47.025  1.00112.31           C  
-ANISOU 3758  CG1 ILE A 497    20625  10573  11474  -2992   5629  -2289       C  
-ATOM   3759  CG2 ILE A 497     -51.382 -17.993  49.097  1.00115.49           C  
-ANISOU 3759  CG2 ILE A 497    20895  11353  11633  -2834   5869  -2213       C  
-ATOM   3760  CD1 ILE A 497     -48.824 -17.756  46.227  1.00107.47           C  
-ANISOU 3760  CD1 ILE A 497    20113   9808  10914  -3035   5573  -2224       C  
-ATOM   3761  N   SER A 498     -48.744 -17.655  51.533  1.00125.12           N  
-ANISOU 3761  N   SER A 498    22243  12787  12509  -2345   5788  -2099       N  
-ATOM   3762  CA  SER A 498     -48.967 -17.782  52.972  1.00130.52           C  
-ANISOU 3762  CA  SER A 498    22861  13742  12989  -2168   5886  -2050       C  
-ATOM   3763  C   SER A 498     -48.360 -16.606  53.731  1.00132.74           C  
-ANISOU 3763  C   SER A 498    23115  14154  13168  -1911   5668  -2208       C  
-ATOM   3764  O   SER A 498     -48.871 -16.198  54.774  1.00133.84           O  
-ANISOU 3764  O   SER A 498    23139  14571  13142  -1722   5658  -2288       O  
-ATOM   3765  CB  SER A 498     -48.383 -19.095  53.498  1.00129.69           C  
-ANISOU 3765  CB  SER A 498    22862  13599  12816  -2194   6093  -1799       C  
-ATOM   3766  OG  SER A 498     -46.973 -19.020  53.614  1.00126.57           O  
-ANISOU 3766  OG  SER A 498    22589  13096  12405  -2085   6013  -1775       O  
-ATOM   3767  N   ALA A 499     -47.261 -16.073  53.205  1.00197.57           N  
-ANISOU 3767  N   ALA A 499    31420  22181  21465  -1900   5480  -2249       N  
-ATOM   3768  CA  ALA A 499     -46.644 -14.879  53.771  1.00198.82           C  
-ANISOU 3768  CA  ALA A 499    31568  22407  21568  -1686   5209  -2396       C  
-ATOM   3769  C   ALA A 499     -47.481 -13.652  53.432  1.00200.70           C  
-ANISOU 3769  C   ALA A 499    31707  22675  21874  -1653   4949  -2639       C  
-ATOM   3770  O   ALA A 499     -47.235 -12.557  53.936  1.00199.69           O  
-ANISOU 3770  O   ALA A 499    31558  22607  21708  -1457   4670  -2802       O  
-ATOM   3771  CB  ALA A 499     -45.224 -14.717  53.256  1.00196.27           C  
-ANISOU 3771  CB  ALA A 499    31360  21894  21318  -1725   5075  -2329       C  
-ATOM   3772  N   ALA A 500     -48.471 -13.844  52.566  1.00136.66           N  
-ANISOU 3772  N   ALA A 500    23545  14508  13871  -1839   5018  -2670       N  
-ATOM   3773  CA  ALA A 500     -49.427 -12.793  52.246  1.00137.73           C  
-ANISOU 3773  CA  ALA A 500    23583  14684  14066  -1808   4793  -2907       C  
-ATOM   3774  C   ALA A 500     -50.596 -12.846  53.225  1.00142.57           C  
-ANISOU 3774  C   ALA A 500    24042  15625  14503  -1642   4908  -3002       C  
-ATOM   3775  O   ALA A 500     -51.282 -11.849  53.445  1.00145.69           O  
-ANISOU 3775  O   ALA A 500    24339  16150  14867  -1483   4684  -3248       O  
-ATOM   3776  CB  ALA A 500     -49.920 -12.942  50.820  1.00138.10           C  
-ANISOU 3776  CB  ALA A 500    23640  14525  14308  -2084   4805  -2901       C  
-ATOM   3777  N   ARG A 501     -50.813 -14.020  53.811  1.00151.45           N  
-ANISOU 3777  N   ARG A 501    25140  16899  15504  -1679   5238  -2803       N  
-ATOM   3778  CA  ARG A 501     -51.855 -14.203  54.815  1.00157.18           C  
-ANISOU 3778  CA  ARG A 501    25691  18008  16021  -1542   5380  -2832       C  
-ATOM   3779  C   ARG A 501     -51.464 -13.557  56.138  1.00159.73           C  
-ANISOU 3779  C   ARG A 501    25961  18597  16134  -1197   5252  -2949       C  
-ATOM   3780  O   ARG A 501     -52.228 -12.781  56.711  1.00162.49           O  
-ANISOU 3780  O   ARG A 501    26156  19232  16350   -972   5116  -3177       O  
-ATOM   3781  CB  ARG A 501     -52.134 -15.692  55.035  1.00154.21           C  
-ANISOU 3781  CB  ARG A 501    25310  17700  15584  -1724   5742  -2532       C  
-ATOM   3782  CG  ARG A 501     -52.839 -16.374  53.879  1.00150.06           C  
-ANISOU 3782  CG  ARG A 501    24798  16981  15236  -2035   5871  -2438       C  
-ATOM   3783  CD  ARG A 501     -54.071 -15.593  53.459  1.00146.27           C  
-ANISOU 3783  CD  ARG A 501    24165  16626  14785  -2033   5758  -2666       C  
-ATOM   3784  NE  ARG A 501     -55.004 -16.406  52.684  1.00146.36           N  
-ANISOU 3784  NE  ARG A 501    24139  16568  14902  -2310   5938  -2546       N  
-ATOM   3785  CZ  ARG A 501     -56.090 -15.927  52.083  1.00147.10           C  
-ANISOU 3785  CZ  ARG A 501    24119  16712  15060  -2372   5873  -2712       C  
-ATOM   3786  NH1 ARG A 501     -56.886 -16.740  51.401  1.00146.39           N  
-ANISOU 3786  NH1 ARG A 501    24004  16546  15072  -2633   6041  -2581       N  
-ATOM   3787  NH2 ARG A 501     -56.378 -14.634  52.160  1.00150.10           N  
-ANISOU 3787  NH2 ARG A 501    24418  17203  15411  -2167   5615  -3015       N  
-ATOM   3788  N   ASP A 502     -50.269 -13.887  56.615  1.00194.81           N  
-ANISOU 3788  N   ASP A 502    30527  22953  20539  -1139   5286  -2806       N  
-ATOM   3789  CA  ASP A 502     -49.776 -13.378  57.890  1.00194.18           C  
-ANISOU 3789  CA  ASP A 502    30414  23104  20262   -813   5177  -2893       C  
-ATOM   3790  C   ASP A 502     -49.716 -11.854  57.905  1.00190.53           C  
-ANISOU 3790  C   ASP A 502    29934  22621  19837   -581   4756  -3218       C  
-ATOM   3791  O   ASP A 502     -50.358 -11.208  58.733  1.00188.27           O  
-ANISOU 3791  O   ASP A 502    29503  22653  19378   -298   4634  -3434       O  
-ATOM   3792  CB  ASP A 502     -48.394 -13.958  58.200  1.00203.76           C  
-ANISOU 3792  CB  ASP A 502    31791  24157  21472   -820   5257  -2688       C  
-ATOM   3793  CG  ASP A 502     -48.410 -15.470  58.338  1.00209.84           C  
-ANISOU 3793  CG  ASP A 502    32595  24942  22194  -1010   5623  -2376       C  
-ATOM   3794  OD1 ASP A 502     -49.254 -16.122  57.686  1.00217.68           O  
-ANISOU 3794  OD1 ASP A 502    33548  25899  23262  -1243   5786  -2282       O  
-ATOM   3795  OD2 ASP A 502     -47.574 -16.006  59.096  1.00218.71           O  
-ANISOU 3795  OD2 ASP A 502    33793  26097  23211   -926   5724  -2223       O  
-ATOM   3796  N   LEU A 503     -48.945 -11.284  56.985  1.00138.10           N  
-ANISOU 3796  N   LEU A 503    23435  15620  13415   -698   4513  -3250       N  
-ATOM   3797  CA  LEU A 503     -48.761  -9.838  56.936  1.00138.00           C  
-ANISOU 3797  CA  LEU A 503    23438  15519  13475   -517   4053  -3521       C  
-ATOM   3798  C   LEU A 503     -49.936  -9.139  56.263  1.00140.74           C  
-ANISOU 3798  C   LEU A 503    23693  15868  13912   -548   3871  -3751       C  
-ATOM   3799  O   LEU A 503     -49.907  -7.928  56.051  1.00142.57           O  
-ANISOU 3799  O   LEU A 503    23950  15980  14241   -433   3447  -3982       O  
-ATOM   3800  CB  LEU A 503     -47.454  -9.481  56.227  1.00130.61           C  
-ANISOU 3800  CB  LEU A 503    22672  14227  12728   -660   3837  -3425       C  
-ATOM   3801  CG  LEU A 503     -46.169 -10.001  56.875  1.00129.35           C  
-ANISOU 3801  CG  LEU A 503    22610  14052  12485   -601   3950  -3232       C  
-ATOM   3802  CD1 LEU A 503     -46.236  -9.843  58.389  1.00128.39           C  
-ANISOU 3802  CD1 LEU A 503    22418  14241  12125   -242   3949  -3336       C  
-ATOM   3803  CD2 LEU A 503     -45.915 -11.452  56.494  1.00124.68           C  
-ANISOU 3803  CD2 LEU A 503    22069  13407  11897   -842   4369  -2943       C  
-ATOM   3804  N   GLY A 504     -50.969  -9.908  55.933  1.00139.69           N  
-ANISOU 3804  N   GLY A 504    23459  15861  13754   -707   4172  -3682       N  
-ATOM   3805  CA  GLY A 504     -52.164  -9.361  55.316  1.00143.17           C  
-ANISOU 3805  CA  GLY A 504    23798  16335  14264   -739   4045  -3893       C  
-ATOM   3806  C   GLY A 504     -51.850  -8.574  54.060  1.00142.11           C  
-ANISOU 3806  C   GLY A 504    23783  15811  14401   -920   3724  -3968       C  
-ATOM   3807  O   GLY A 504     -52.650  -7.754  53.608  1.00140.76           O  
-ANISOU 3807  O   GLY A 504    23559  15617  14308   -886   3473  -4204       O  
-ATOM   3808  N   LEU A 505     -50.675  -8.829  53.498  1.00174.66           N  
-ANISOU 3808  N   LEU A 505    28057  19648  18657  -1113   3725  -3761       N  
-ATOM   3809  CA  LEU A 505     -50.228  -8.144  52.295  1.00176.58           C  
-ANISOU 3809  CA  LEU A 505    28399  19555  19138  -1320   3429  -3772       C  
-ATOM   3810  C   LEU A 505     -50.444  -9.028  51.071  1.00177.36           C  
-ANISOU 3810  C   LEU A 505    28521  19497  19372  -1670   3701  -3587       C  
-ATOM   3811  O   LEU A 505     -49.675  -9.957  50.828  1.00175.33           O  
-ANISOU 3811  O   LEU A 505    28335  19159  19123  -1821   3946  -3344       O  
-ATOM   3812  CB  LEU A 505     -48.750  -7.769  52.424  1.00174.53           C  
-ANISOU 3812  CB  LEU A 505    28264  19130  18918  -1305   3219  -3661       C  
-ATOM   3813  CG  LEU A 505     -48.114  -7.026  51.250  1.00172.86           C  
-ANISOU 3813  CG  LEU A 505    28138  18614  18926  -1536   2884  -3618       C  
-ATOM   3814  CD1 LEU A 505     -48.888  -5.755  50.942  1.00174.66           C  
-ANISOU 3814  CD1 LEU A 505    28338  18760  19263  -1472   2444  -3890       C  
-ATOM   3815  CD2 LEU A 505     -46.657  -6.718  51.550  1.00172.30           C  
-ANISOU 3815  CD2 LEU A 505    28161  18451  18855  -1508   2695  -3486       C  
-ATOM   3816  N   ASP A 506     -51.497  -8.731  50.312  1.00207.25           N  
-ANISOU 3816  N   ASP A 506    32244  23242  23258  -1776   3638  -3721       N  
-ATOM   3817  CA  ASP A 506     -51.859  -9.503  49.124  1.00208.68           C  
-ANISOU 3817  CA  ASP A 506    32436  23280  23573  -2089   3868  -3585       C  
-ATOM   3818  C   ASP A 506     -50.633 -10.017  48.370  1.00208.96           C  
-ANISOU 3818  C   ASP A 506    32589  23104  23704  -2302   3936  -3343       C  
-ATOM   3819  O   ASP A 506     -49.687  -9.266  48.130  1.00207.33           O  
-ANISOU 3819  O   ASP A 506    32447  22767  23562  -2316   3644  -3330       O  
-ATOM   3820  CB  ASP A 506     -52.732  -8.662  48.186  1.00214.45           C  
-ANISOU 3820  CB  ASP A 506    33129  23895  24458  -2186   3615  -3779       C  
-ATOM   3821  CG  ASP A 506     -54.052  -8.257  48.819  1.00220.19           C  
-ANISOU 3821  CG  ASP A 506    33719  24865  25079  -1975   3573  -4035       C  
-ATOM   3822  OD1 ASP A 506     -54.118  -8.154  50.062  1.00225.75           O  
-ANISOU 3822  OD1 ASP A 506    34357  25828  25589  -1691   3582  -4120       O  
-ATOM   3823  OD2 ASP A 506     -55.027  -8.036  48.070  1.00224.00           O  
-ANISOU 3823  OD2 ASP A 506    34146  25303  25659  -2081   3527  -4157       O  
-ATOM   3824  N   PRO A 507     -50.654 -11.303  47.984  1.00174.45           N  
-ANISOU 3824  N   PRO A 507    28237  18711  19336  -2467   4300  -3152       N  
-ATOM   3825  CA  PRO A 507     -49.514 -11.943  47.316  1.00175.08           C  
-ANISOU 3825  CA  PRO A 507    28412  18640  19469  -2627   4393  -2942       C  
-ATOM   3826  C   PRO A 507     -49.290 -11.378  45.917  1.00174.49           C  
-ANISOU 3826  C   PRO A 507    28352  18378  19567  -2845   4178  -2951       C  
-ATOM   3827  O   PRO A 507     -50.245 -10.955  45.266  1.00175.02           O  
-ANISOU 3827  O   PRO A 507    28369  18393  19738  -2939   4086  -3078       O  
-ATOM   3828  CB  PRO A 507     -49.940 -13.410  47.233  1.00174.21           C  
-ANISOU 3828  CB  PRO A 507    28311  18547  19334  -2726   4787  -2795       C  
-ATOM   3829  CG  PRO A 507     -51.425 -13.367  47.217  1.00174.48           C  
-ANISOU 3829  CG  PRO A 507    28243  18667  19385  -2748   4852  -2920       C  
-ATOM   3830  CD  PRO A 507     -51.815 -12.204  48.087  1.00174.26           C  
-ANISOU 3830  CD  PRO A 507    28137  18804  19270  -2517   4611  -3132       C  
-ATOM   3831  N   GLY A 508     -48.039 -11.361  45.468  1.00187.47           N  
-ANISOU 3831  N   GLY A 508    30051  19952  21228  -2925   4094  -2811       N  
-ATOM   3832  CA  GLY A 508     -47.707 -10.829  44.159  1.00185.11           C  
-ANISOU 3832  CA  GLY A 508    29742  19532  21060  -3144   3884  -2779       C  
-ATOM   3833  C   GLY A 508     -47.679  -9.312  44.129  1.00183.02           C  
-ANISOU 3833  C   GLY A 508    29460  19210  20869  -3135   3430  -2895       C  
-ATOM   3834  O   GLY A 508     -46.706  -8.713  43.672  1.00178.16           O  
-ANISOU 3834  O   GLY A 508    28854  18552  20288  -3240   3177  -2791       O  
-ATOM   3835  N   LYS A 509     -48.752  -8.693  44.614  1.00183.65           N  
-ANISOU 3835  N   LYS A 509    29510  19302  20968  -3009   3303  -3109       N  
-ATOM   3836  CA  LYS A 509     -48.856  -7.237  44.652  1.00185.30           C  
-ANISOU 3836  CA  LYS A 509    29719  19429  21258  -2964   2821  -3262       C  
-ATOM   3837  C   LYS A 509     -47.573  -6.604  45.181  1.00184.00           C  
-ANISOU 3837  C   LYS A 509    29605  19251  21055  -2890   2542  -3171       C  
-ATOM   3838  O   LYS A 509     -46.771  -6.076  44.413  1.00177.27           O  
-ANISOU 3838  O   LYS A 509    28765  18302  20287  -3086   2287  -3036       O  
-ATOM   3839  CB  LYS A 509     -50.050  -6.811  45.495  1.00191.81           C  
-ANISOU 3839  CB  LYS A 509    30500  20342  22038  -2724   2756  -3531       C  
-ATOM   3840  N   GLN A 510     -47.382  -6.661  46.495  1.00218.72           N  
-ANISOU 3840  N   GLN A 510    34021  23765  25316  -2615   2586  -3232       N  
-ATOM   3841  CA  GLN A 510     -46.170  -6.129  47.107  1.00217.33           C  
-ANISOU 3841  CA  GLN A 510    33898  23581  25098  -2522   2340  -3149       C  
-ATOM   3842  C   GLN A 510     -45.167  -7.240  47.404  1.00215.05           C  
-ANISOU 3842  C   GLN A 510    33633  23394  24684  -2522   2697  -2928       C  
-ATOM   3843  O   GLN A 510     -44.094  -7.296  46.804  1.00212.87           O  
-ANISOU 3843  O   GLN A 510    33369  23086  24427  -2692   2644  -2730       O  
-ATOM   3844  CB  GLN A 510     -46.506  -5.356  48.372  1.00224.88           C  
-ANISOU 3844  CB  GLN A 510    34863  24597  25984  -2191   2093  -3379       C  
-ATOM   3845  N   ILE A 511     -45.523  -8.126  48.329  1.00176.39           N  
-ANISOU 3845  N   ILE A 511    28733  18640  19647  -2333   3049  -2956       N  
-ATOM   3846  CA  ILE A 511     -44.643  -9.226  48.712  1.00176.94           C  
-ANISOU 3846  CA  ILE A 511    28842  18792  19596  -2306   3376  -2764       C  
-ATOM   3847  C   ILE A 511     -44.478 -10.238  47.581  1.00173.71           C  
-ANISOU 3847  C   ILE A 511    28433  18337  19233  -2547   3651  -2601       C  
-ATOM   3848  O   ILE A 511     -45.458 -10.715  47.009  1.00172.02           O  
-ANISOU 3848  O   ILE A 511    28188  18096  19077  -2650   3826  -2647       O  
-ATOM   3849  CB  ILE A 511     -45.148  -9.940  49.986  1.00175.91           C  
-ANISOU 3849  CB  ILE A 511    28705  18829  19305  -2064   3666  -2816       C  
-ATOM   3850  CG1 ILE A 511     -44.162 -11.028  50.415  1.00181.14           C  
-ANISOU 3850  CG1 ILE A 511    29427  19546  19852  -2032   3954  -2615       C  
-ATOM   3851  CG2 ILE A 511     -46.538 -10.522  49.765  1.00180.66           C  
-ANISOU 3851  CG2 ILE A 511    29243  19481  19917  -2114   3913  -2893       C  
-ATOM   3852  CD1 ILE A 511     -44.534 -11.702  51.714  1.00182.93           C  
-ANISOU 3852  CD1 ILE A 511    29648  19946  19912  -1813   4209  -2625       C  
-ATOM   3853  N   LYS A 512     -43.229 -10.557  47.259  1.00207.12           N  
-ANISOU 3853  N   LYS A 512    32692  22576  23430  -2623   3671  -2422       N  
-ATOM   3854  CA  LYS A 512     -42.931 -11.502  46.188  1.00198.97           C  
-ANISOU 3854  CA  LYS A 512    31652  21532  22417  -2808   3894  -2288       C  
-ATOM   3855  C   LYS A 512     -41.535 -12.093  46.353  1.00196.28           C  
-ANISOU 3855  C   LYS A 512    31343  21274  21960  -2766   3989  -2119       C  
-ATOM   3856  O   LYS A 512     -40.676 -11.502  47.007  1.00193.41           O  
-ANISOU 3856  O   LYS A 512    30992  20957  21537  -2668   3802  -2079       O  
-ATOM   3857  CB  LYS A 512     -43.066 -10.826  44.834  1.00202.20           C  
-ANISOU 3857  CB  LYS A 512    31997  21871  22958  -3054   3669  -2282       C  
-ATOM   3858  N   LEU A 513     -41.315 -13.262  45.760  1.00137.49           N  
-ANISOU 3858  N   LEU A 513    23912  13845  14484  -2826   4261  -2033       N  
-ATOM   3859  CA  LEU A 513     -40.021 -13.929  45.840  1.00138.01           C  
-ANISOU 3859  CA  LEU A 513    24004  14006  14429  -2766   4359  -1897       C  
-ATOM   3860  C   LEU A 513     -39.081 -13.436  44.745  1.00139.92           C  
-ANISOU 3860  C   LEU A 513    24153  14341  14670  -2936   4159  -1793       C  
-ATOM   3861  O   LEU A 513     -39.468 -12.618  43.910  1.00141.92           O  
-ANISOU 3861  O   LEU A 513    24332  14566  15026  -3118   3948  -1811       O  
-ATOM   3862  CB  LEU A 513     -40.186 -15.448  45.757  1.00127.04           C  
-ANISOU 3862  CB  LEU A 513    22681  12590  12999  -2719   4702  -1869       C  
-ATOM   3863  CG  LEU A 513     -40.665 -16.045  44.433  1.00122.18           C  
-ANISOU 3863  CG  LEU A 513    22034  11923  12465  -2881   4798  -1883       C  
-ATOM   3864  CD1 LEU A 513     -40.654 -17.564  44.509  1.00116.58           C  
-ANISOU 3864  CD1 LEU A 513    21418  11163  11713  -2797   5076  -1851       C  
-ATOM   3865  CD2 LEU A 513     -42.050 -15.539  44.059  1.00115.89           C  
-ANISOU 3865  CD2 LEU A 513    21201  11022  11811  -3003   4750  -1994       C  
-ATOM   3866  N   ASP A 514     -37.849 -13.935  44.752  1.00195.47           N  
-ANISOU 3866  N   ASP A 514    31182  21512  21575  -2879   4218  -1677       N  
-ATOM   3867  CA  ASP A 514     -36.838 -13.501  43.792  1.00194.55           C  
-ANISOU 3867  CA  ASP A 514    30944  21568  21410  -3031   4035  -1550       C  
-ATOM   3868  C   ASP A 514     -35.591 -14.377  43.882  1.00195.17           C  
-ANISOU 3868  C   ASP A 514    31018  21824  21314  -2910   4182  -1456       C  
-ATOM   3869  O   ASP A 514     -35.381 -15.066  44.878  1.00192.64           O  
-ANISOU 3869  O   ASP A 514    30807  21463  20924  -2706   4355  -1478       O  
-ATOM   3870  CB  ASP A 514     -36.465 -12.038  44.044  1.00199.83           C  
-ANISOU 3870  CB  ASP A 514    31560  22248  22120  -3119   3651  -1490       C  
-ATOM   3871  CG  ASP A 514     -35.865 -11.370  42.824  1.00198.29           C  
-ANISOU 3871  CG  ASP A 514    31209  22209  21924  -3376   3406  -1345       C  
-ATOM   3872  OD1 ASP A 514     -34.663 -11.577  42.556  1.00201.40           O  
-ANISOU 3872  OD1 ASP A 514    31515  22833  22173  -3394   3398  -1197       O  
-ATOM   3873  OD2 ASP A 514     -36.597 -10.630  42.134  1.00201.61           O  
-ANISOU 3873  OD2 ASP A 514    31583  22542  22476  -3562   3215  -1372       O  
-ATOM   3874  N   SER A 515     -34.762 -14.342  42.842  1.00175.29           N  
-ANISOU 3874  N   SER A 515    28363  19527  18712  -3032   4102  -1351       N  
-ATOM   3875  CA  SER A 515     -33.536 -15.137  42.815  1.00177.72           C  
-ANISOU 3875  CA  SER A 515    28638  20057  18832  -2904   4217  -1280       C  
-ATOM   3876  C   SER A 515     -32.289 -14.280  42.597  1.00176.55           C  
-ANISOU 3876  C   SER A 515    28333  20180  18569  -3009   3963  -1104       C  
-ATOM   3877  O   SER A 515     -32.367 -13.181  42.047  1.00175.60           O  
-ANISOU 3877  O   SER A 515    28100  20103  18516  -3239   3691  -1013       O  
-ATOM   3878  CB  SER A 515     -33.628 -16.233  41.751  1.00178.18           C  
-ANISOU 3878  CB  SER A 515    28659  20202  18839  -2889   4409  -1338       C  
-ATOM   3879  OG  SER A 515     -34.021 -15.699  40.500  1.00184.30           O  
-ANISOU 3879  OG  SER A 515    29293  21060  19672  -3119   4283  -1316       O  
-ATOM   3880  N   SER A 516     -31.142 -14.792  43.033  1.00162.65           N  
-ANISOU 3880  N   SER A 516    26564  18602  16634  -2849   4035  -1046       N  
-ATOM   3881  CA  SER A 516     -29.884 -14.060  42.931  1.00160.25           C  
-ANISOU 3881  CA  SER A 516    26103  18586  16200  -2939   3806   -859       C  
-ATOM   3882  C   SER A 516     -28.688 -14.986  43.129  1.00157.90           C  
-ANISOU 3882  C   SER A 516    25777  18539  15678  -2733   3962   -836       C  
-ATOM   3883  O   SER A 516     -28.847 -16.195  43.288  1.00152.78           O  
-ANISOU 3883  O   SER A 516    25243  17819  14989  -2521   4225   -971       O  
-ATOM   3884  CB  SER A 516     -29.842 -12.925  43.958  1.00160.50           C  
-ANISOU 3884  CB  SER A 516    26198  18459  16327  -2969   3553   -801       C  
-ATOM   3885  OG  SER A 516     -28.783 -13.106  44.883  1.00170.02           O  
-ANISOU 3885  OG  SER A 516    27436  19764  17400  -2793   3569   -744       O  
-ATOM   3886  N   ALA A 517     -27.490 -14.410  43.113  1.00169.58           N  
-ANISOU 3886  N   ALA A 517    27104  20312  17015  -2799   3776   -660       N  
-ATOM   3887  CA  ALA A 517     -26.269 -15.174  43.334  1.00170.41           C  
-ANISOU 3887  CA  ALA A 517    27162  20695  16891  -2597   3893   -637       C  
-ATOM   3888  C   ALA A 517     -25.960 -15.297  44.823  1.00171.22           C  
-ANISOU 3888  C   ALA A 517    27450  20605  17002  -2381   3943   -671       C  
-ATOM   3889  O   ALA A 517     -26.066 -14.325  45.569  1.00172.45           O  
-ANISOU 3889  O   ALA A 517    27655  20601  17266  -2452   3748   -606       O  
-ATOM   3890  CB  ALA A 517     -25.102 -14.528  42.606  1.00171.15           C  
-ANISOU 3890  CB  ALA A 517    26977  21252  16802  -2777   3676   -414       C  
-ATOM   3891  N   GLN A 518     -25.585 -16.501  45.246  1.00137.20           N  
-ANISOU 3891  N   GLN A 518    23245  16306  12578  -2106   4184   -780       N  
-ATOM   3892  CA  GLN A 518     -25.203 -16.757  46.633  1.00141.62           C  
-ANISOU 3892  CA  GLN A 518    23974  16719  13116  -1883   4254   -808       C  
-ATOM   3893  C   GLN A 518     -26.346 -16.513  47.614  1.00140.72           C  
-ANISOU 3893  C   GLN A 518    24063  16200  13204  -1852   4290   -892       C  
-ATOM   3894  O   GLN A 518     -26.155 -16.569  48.829  1.00138.95           O  
-ANISOU 3894  O   GLN A 518    23972  15851  12973  -1684   4326   -908       O  
-ATOM   3895  CB  GLN A 518     -23.987 -15.921  47.014  1.00143.51           C  
-ANISOU 3895  CB  GLN A 518    24090  17196  13241  -1927   4035   -635       C  
-ATOM   3896  N   PHE A 519     -27.535 -16.241  47.086  1.00207.47           N  
-ANISOU 3896  N   PHE A 519    32527  24481  21822  -2006   4280   -950       N  
-ATOM   3897  CA  PHE A 519     -28.706 -16.006  47.925  1.00206.69           C  
-ANISOU 3897  CA  PHE A 519    32585  24056  21892  -1975   4315  -1043       C  
-ATOM   3898  C   PHE A 519     -29.839 -16.970  47.593  1.00204.03           C  
-ANISOU 3898  C   PHE A 519    32347  23535  21641  -1950   4552  -1170       C  
-ATOM   3899  O   PHE A 519     -30.630 -17.334  48.462  1.00202.65           O  
-ANISOU 3899  O   PHE A 519    32320  23142  21536  -1843   4687  -1245       O  
-ATOM   3900  CB  PHE A 519     -29.195 -14.561  47.789  1.00215.89           C  
-ANISOU 3900  CB  PHE A 519    33680  25152  23198  -2184   4018   -999       C  
-ATOM   3901  CG  PHE A 519     -28.352 -13.558  48.528  1.00224.25           C  
-ANISOU 3901  CG  PHE A 519    34710  26269  24227  -2177   3750   -894       C  
-ATOM   3902  CD1 PHE A 519     -28.592 -13.283  49.865  1.00229.70           C  
-ANISOU 3902  CD1 PHE A 519    35537  26781  24959  -2001   3726   -964       C  
-ATOM   3903  CD2 PHE A 519     -27.330 -12.881  47.885  1.00230.55           C  
-ANISOU 3903  CD2 PHE A 519    35332  27316  24949  -2350   3507   -718       C  
-ATOM   3904  CE1 PHE A 519     -27.823 -12.358  50.547  1.00237.46           C  
-ANISOU 3904  CE1 PHE A 519    36503  27797  25924  -1979   3452   -881       C  
-ATOM   3905  CE2 PHE A 519     -26.557 -11.954  48.562  1.00238.32           C  
-ANISOU 3905  CE2 PHE A 519    36295  28335  25922  -2360   3229   -605       C  
-ATOM   3906  CZ  PHE A 519     -26.805 -11.693  49.895  1.00240.17           C  
-ANISOU 3906  CZ  PHE A 519    36688  28351  26215  -2166   3196   -698       C  
-ATOM   3907  N   GLY A 520     -29.914 -17.379  46.332  1.00123.83           N  
-ANISOU 3907  N   GLY A 520    22094  13487  11470  -2053   4592  -1185       N  
-ATOM   3908  CA  GLY A 520     -30.988 -18.243  45.881  1.00125.09           C  
-ANISOU 3908  CA  GLY A 520    22337  13466  11727  -2054   4777  -1299       C  
-ATOM   3909  C   GLY A 520     -32.307 -17.499  45.850  1.00129.09           C  
-ANISOU 3909  C   GLY A 520    22856  13770  12422  -2215   4714  -1343       C  
-ATOM   3910  O   GLY A 520     -32.377 -16.360  45.389  1.00135.05           O  
-ANISOU 3910  O   GLY A 520    23494  14584  13234  -2399   4491  -1294       O  
-ATOM   3911  N   TYR A 521     -33.355 -18.142  46.350  1.00191.48           N  
-ANISOU 3911  N   TYR A 521    30896  21440  20416  -2151   4891  -1428       N  
-ATOM   3912  CA  TYR A 521     -34.683 -17.543  46.370  1.00191.19           C  
-ANISOU 3912  CA  TYR A 521    30867  21234  20541  -2275   4855  -1491       C  
-ATOM   3913  C   TYR A 521     -34.940 -16.830  47.697  1.00189.58           C  
-ANISOU 3913  C   TYR A 521    30720  20958  20353  -2183   4784  -1502       C  
-ATOM   3914  O   TYR A 521     -34.595 -17.340  48.761  1.00187.66           O  
-ANISOU 3914  O   TYR A 521    30574  20703  20026  -2000   4898  -1485       O  
-ATOM   3915  CB  TYR A 521     -35.752 -18.610  46.104  1.00192.57           C  
-ANISOU 3915  CB  TYR A 521    31130  21237  20801  -2279   5072  -1566       C  
-ATOM   3916  CG  TYR A 521     -35.749 -19.144  44.684  1.00193.03           C  
-ANISOU 3916  CG  TYR A 521    31123  21342  20876  -2376   5097  -1594       C  
-ATOM   3917  CD1 TYR A 521     -36.932 -19.279  43.968  1.00192.66           C  
-ANISOU 3917  CD1 TYR A 521    31072  21159  20970  -2511   5144  -1665       C  
-ATOM   3918  CD2 TYR A 521     -34.563 -19.503  44.057  1.00195.21           C  
-ANISOU 3918  CD2 TYR A 521    31331  21828  21013  -2318   5068  -1560       C  
-ATOM   3919  CE1 TYR A 521     -36.934 -19.763  42.671  1.00195.10           C  
-ANISOU 3919  CE1 TYR A 521    31321  21518  21290  -2582   5156  -1704       C  
-ATOM   3920  CE2 TYR A 521     -34.555 -19.986  42.761  1.00197.58           C  
-ANISOU 3920  CE2 TYR A 521    31554  22215  21304  -2374   5080  -1606       C  
-ATOM   3921  CZ  TYR A 521     -35.742 -20.114  42.073  1.00197.09           C  
-ANISOU 3921  CZ  TYR A 521    31500  21993  21392  -2504   5122  -1680       C  
-ATOM   3922  OH  TYR A 521     -35.735 -20.595  40.783  1.00198.22           O  
-ANISOU 3922  OH  TYR A 521    31566  22227  21521  -2542   5126  -1738       O  
-ATOM   3923  N   TYR A 522     -35.536 -15.643  47.627  1.00188.60           N  
-ANISOU 3923  N   TYR A 522    30534  20794  20331  -2296   4574  -1542       N  
-ATOM   3924  CA  TYR A 522     -35.866 -14.880  48.828  1.00187.70           C  
-ANISOU 3924  CA  TYR A 522    30461  20626  20230  -2182   4463  -1593       C  
-ATOM   3925  C   TYR A 522     -37.047 -13.943  48.585  1.00185.47           C  
-ANISOU 3925  C   TYR A 522    30135  20247  20090  -2291   4298  -1702       C  
-ATOM   3926  O   TYR A 522     -37.484 -13.769  47.449  1.00184.59           O  
-ANISOU 3926  O   TYR A 522    29957  20106  20071  -2482   4243  -1714       O  
-ATOM   3927  CB  TYR A 522     -34.651 -14.085  49.317  1.00192.35           C  
-ANISOU 3927  CB  TYR A 522    31022  21319  20743  -2122   4230  -1514       C  
-ATOM   3928  CG  TYR A 522     -34.072 -13.146  48.282  1.00198.12           C  
-ANISOU 3928  CG  TYR A 522    31626  22135  21514  -2337   3937  -1428       C  
-ATOM   3929  CD1 TYR A 522     -34.825 -12.100  47.769  1.00200.68           C  
-ANISOU 3929  CD1 TYR A 522    31895  22372  21981  -2502   3685  -1478       C  
-ATOM   3930  CD2 TYR A 522     -32.769 -13.300  47.827  1.00201.08           C  
-ANISOU 3930  CD2 TYR A 522    31927  22701  21775  -2379   3896  -1286       C  
-ATOM   3931  CE1 TYR A 522     -34.305 -11.240  46.825  1.00202.62           C  
-ANISOU 3931  CE1 TYR A 522    32023  22698  22266  -2729   3392  -1365       C  
-ATOM   3932  CE2 TYR A 522     -32.237 -12.441  46.882  1.00203.36           C  
-ANISOU 3932  CE2 TYR A 522    32072  23116  22081  -2605   3620  -1168       C  
-ATOM   3933  CZ  TYR A 522     -33.011 -11.412  46.385  1.00203.73           C  
-ANISOU 3933  CZ  TYR A 522    32074  23052  22281  -2791   3363  -1195       C  
-ATOM   3934  OH  TYR A 522     -32.492 -10.551  45.446  1.00205.26           O  
-ANISOU 3934  OH  TYR A 522    32124  23371  22495  -3045   3064  -1045       O  
-ATOM   3935  N   PHE A 523     -37.562 -13.343  49.654  1.00159.87           N  
-ANISOU 3935  N   PHE A 523    26923  16969  16851  -2151   4209  -1795       N  
-ATOM   3936  CA  PHE A 523     -38.659 -12.386  49.536  1.00159.02           C  
-ANISOU 3936  CA  PHE A 523    26773  16785  16861  -2205   4014  -1933       C  
-ATOM   3937  C   PHE A 523     -38.143 -10.998  49.196  1.00156.86           C  
-ANISOU 3937  C   PHE A 523    26448  16491  16660  -2301   3585  -1923       C  
-ATOM   3938  O   PHE A 523     -36.950 -10.721  49.315  1.00157.63           O  
-ANISOU 3938  O   PHE A 523    26539  16653  16701  -2297   3442  -1804       O  
-ATOM   3939  CB  PHE A 523     -39.484 -12.324  50.821  1.00160.52           C  
-ANISOU 3939  CB  PHE A 523    26997  16992  17001  -1985   4079  -2062       C  
-ATOM   3940  CG  PHE A 523     -40.398 -13.496  51.010  1.00162.02           C  
-ANISOU 3940  CG  PHE A 523    27210  17193  17158  -1963   4441  -2068       C  
-ATOM   3941  CD1 PHE A 523     -41.638 -13.529  50.396  1.00160.90           C  
-ANISOU 3941  CD1 PHE A 523    27021  17000  17114  -2085   4496  -2154       C  
-ATOM   3942  CD2 PHE A 523     -40.020 -14.562  51.807  1.00163.28           C  
-ANISOU 3942  CD2 PHE A 523    27438  17409  17193  -1834   4706  -1974       C  
-ATOM   3943  CE1 PHE A 523     -42.482 -14.607  50.569  1.00160.27           C  
-ANISOU 3943  CE1 PHE A 523    26955  16931  17009  -2091   4805  -2132       C  
-ATOM   3944  CE2 PHE A 523     -40.859 -15.641  51.984  1.00163.47           C  
-ANISOU 3944  CE2 PHE A 523    27484  17431  17196  -1846   4999  -1945       C  
-ATOM   3945  CZ  PHE A 523     -42.093 -15.664  51.365  1.00161.95           C  
-ANISOU 3945  CZ  PHE A 523    27238  17194  17103  -1982   5047  -2016       C  
-ATOM   3946  N   ARG A 524     -39.054 -10.121  48.788  1.00135.44           N  
-ANISOU 3946  N   ARG A 524    23698  13686  14077  -2391   3359  -2041       N  
-ATOM   3947  CA  ARG A 524     -38.671  -8.786  48.351  1.00133.05           C  
-ANISOU 3947  CA  ARG A 524    23356  13325  13873  -2522   2900  -2019       C  
-ATOM   3948  C   ARG A 524     -39.744  -7.752  48.681  1.00132.04           C  
-ANISOU 3948  C   ARG A 524    23236  13080  13852  -2448   2613  -2230       C  
-ATOM   3949  O   ARG A 524     -40.937  -7.995  48.483  1.00130.69           O  
-ANISOU 3949  O   ARG A 524    23053  12878  13726  -2446   2758  -2366       O  
-ATOM   3950  CB  ARG A 524     -38.378  -8.788  46.857  1.00130.56           C  
-ANISOU 3950  CB  ARG A 524    22957  13027  13621  -2826   2850  -1879       C  
-ATOM   3951  N   VAL A 525     -39.307  -6.608  49.204  1.00144.78           N  
-ANISOU 3951  N   VAL A 525    24872  14634  15502  -2373   2186  -2264       N  
-ATOM   3952  CA  VAL A 525     -40.192  -5.480  49.487  1.00144.65           C  
-ANISOU 3952  CA  VAL A 525    24871  14495  15593  -2279   1811  -2485       C  
-ATOM   3953  C   VAL A 525     -39.393  -4.178  49.594  1.00145.27           C  
-ANISOU 3953  C   VAL A 525    24977  14461  15758  -2316   1241  -2437       C  
-ATOM   3954  O   VAL A 525     -38.231  -4.115  49.198  1.00145.70           O  
-ANISOU 3954  O   VAL A 525    25011  14544  15805  -2492   1142  -2200       O  
-ATOM   3955  CB  VAL A 525     -41.003  -5.682  50.787  1.00144.66           C  
-ANISOU 3955  CB  VAL A 525    24899  14576  15490  -1928   1961  -2716       C  
-ATOM   3956  CG1 VAL A 525     -42.486  -5.439  50.536  1.00144.25           C  
-ANISOU 3956  CG1 VAL A 525    24810  14494  15506  -1902   1946  -2940       C  
-ATOM   3957  CG2 VAL A 525     -40.777  -7.068  51.356  1.00143.72           C  
-ANISOU 3957  CG2 VAL A 525    24788  14617  15203  -1823   2485  -2622       C  
-ATOM   3958  N   THR A 526     -40.023  -3.138  50.131  1.00165.10           N  
-ANISOU 3958  N   THR A 526    27528  16853  18348  -2145    844  -2665       N  
-ATOM   3959  CA  THR A 526     -39.386  -1.824  50.241  1.00166.53           C  
-ANISOU 3959  CA  THR A 526    27754  16874  18644  -2176    221  -2641       C  
-ATOM   3960  C   THR A 526     -39.670  -1.165  51.587  1.00168.18           C  
-ANISOU 3960  C   THR A 526    28033  17048  18820  -1782    -53  -2911       C  
-ATOM   3961  O   THR A 526     -40.105  -1.833  52.524  1.00168.15           O  
-ANISOU 3961  O   THR A 526    28024  17205  18660  -1489    297  -3061       O  
-ATOM   3962  CB  THR A 526     -39.837  -0.924  49.099  1.00166.89           C  
-ANISOU 3962  CB  THR A 526    27785  16737  18887  -2456   -186  -2631       C  
-ATOM   3963  N   CYS A 527     -39.419   0.139  51.677  1.00176.34           N  
-ANISOU 3963  N   CYS A 527    29126  17881  19994  -1774   -699  -2966       N  
-ATOM   3964  CA  CYS A 527     -39.639   0.885  52.914  1.00178.26           C  
-ANISOU 3964  CA  CYS A 527    29439  18076  20215  -1374  -1051  -3249       C  
-ATOM   3965  C   CYS A 527     -40.781   0.328  53.777  1.00178.42           C  
-ANISOU 3965  C   CYS A 527    29423  18295  20074  -1003   -690  -3558       C  
-ATOM   3966  O   CYS A 527     -40.542  -0.096  54.909  1.00178.81           O  
-ANISOU 3966  O   CYS A 527    29474  18513  19951   -704   -481  -3624       O  
-ATOM   3967  CB  CYS A 527     -39.841   2.374  52.615  1.00180.20           C  
-ANISOU 3967  CB  CYS A 527    29755  18034  20678  -1417  -1822  -3369       C  
-ATOM   3968  N   LYS A 528     -42.005   0.329  53.248  1.00222.63           N  
-ANISOU 3968  N   LYS A 528    34975  23896  25717  -1030   -620  -3730       N  
-ATOM   3969  CA  LYS A 528     -43.182  -0.163  53.979  1.00223.85           C  
-ANISOU 3969  CA  LYS A 528    35061  24281  25710   -712   -295  -4006       C  
-ATOM   3970  C   LYS A 528     -42.952  -1.433  54.802  1.00222.93           C  
-ANISOU 3970  C   LYS A 528    34897  24445  25361   -569    315  -3907       C  
-ATOM   3971  O   LYS A 528     -43.514  -1.587  55.890  1.00223.51           O  
-ANISOU 3971  O   LYS A 528    34924  24740  25260   -211    438  -4121       O  
-ATOM   3972  CB  LYS A 528     -44.350  -0.401  53.016  1.00222.36           C  
-ANISOU 3972  CB  LYS A 528    34807  24090  25590   -891   -119  -4075       C  
-ATOM   3973  CG  LYS A 528     -45.138   0.843  52.643  1.00223.38           C  
-ANISOU 3973  CG  LYS A 528    34963  24029  25883   -843   -694  -4340       C  
-ATOM   3974  CD  LYS A 528     -46.372   1.023  53.518  1.00224.55           C  
-ANISOU 3974  CD  LYS A 528    35042  24382  25894   -422   -699  -4738       C  
-ATOM   3975  CE  LYS A 528     -47.212   2.195  53.032  1.00225.46           C  
-ANISOU 3975  CE  LYS A 528    35187  24303  26176   -377  -1264  -5019       C  
-ATOM   3976  NZ  LYS A 528     -48.542   2.262  53.697  1.00226.70           N  
-ANISOU 3976  NZ  LYS A 528    35240  24718  26179      7  -1209  -5410       N  
-ATOM   3977  N   GLU A 529     -42.144  -2.346  54.272  1.00342.14           N  
-ANISOU 3977  N   GLU A 529    50000  39551  40448   -844    680  -3587       N  
-ATOM   3978  CA  GLU A 529     -41.887  -3.617  54.936  1.00342.30           C  
-ANISOU 3978  CA  GLU A 529    49993  39795  40270   -750   1240  -3467       C  
-ATOM   3979  C   GLU A 529     -40.695  -3.514  55.877  1.00342.78           C  
-ANISOU 3979  C   GLU A 529    50115  39882  40243   -577   1138  -3385       C  
-ATOM   3980  O   GLU A 529     -40.671  -4.145  56.932  1.00343.35           O  
-ANISOU 3980  O   GLU A 529    50173  40157  40128   -328   1428  -3417       O  
-ATOM   3981  CB  GLU A 529     -41.624  -4.711  53.904  1.00341.49           C  
-ANISOU 3981  CB  GLU A 529    49872  39686  40191  -1094   1668  -3194       C  
-ATOM   3982  CG  GLU A 529     -41.686  -6.125  54.458  1.00342.73           C  
-ANISOU 3982  CG  GLU A 529    50006  40047  40167  -1016   2249  -3096       C  
-ATOM   3983  CD  GLU A 529     -43.096  -6.545  54.815  1.00344.67           C  
-ANISOU 3983  CD  GLU A 529    50173  40461  40326   -882   2502  -3270       C  
-ATOM   3984  OE1 GLU A 529     -43.635  -6.034  55.820  1.00347.08           O  
-ANISOU 3984  OE1 GLU A 529    50439  40908  40528   -569   2360  -3495       O  
-ATOM   3985  OE2 GLU A 529     -43.669  -7.382  54.086  1.00344.55           O  
-ANISOU 3985  OE2 GLU A 529    50123  40455  40337  -1085   2830  -3182       O  
-ATOM   3986  N   GLU A 530     -39.699  -2.725  55.486  1.00275.03           N  
-ANISOU 3986  N   GLU A 530    41596  31107  31797   -726    720  -3262       N  
-ATOM   3987  CA  GLU A 530     -38.509  -2.571  56.310  1.00275.52           C  
-ANISOU 3987  CA  GLU A 530    41716  31176  31794   -587    588  -3170       C  
-ATOM   3988  C   GLU A 530     -38.920  -2.075  57.690  1.00276.08           C  
-ANISOU 3988  C   GLU A 530    41801  31343  31752   -133    403  -3465       C  
-ATOM   3989  O   GLU A 530     -38.297  -2.417  58.692  1.00276.69           O  
-ANISOU 3989  O   GLU A 530    41901  31545  31685     85    536  -3440       O  
-ATOM   3990  CB  GLU A 530     -37.504  -1.614  55.665  1.00277.36           C  
-ANISOU 3990  CB  GLU A 530    41997  31186  32203   -830     73  -3000       C  
-ATOM   3991  CG  GLU A 530     -36.092  -1.720  56.236  1.00279.72           C  
-ANISOU 3991  CG  GLU A 530    42337  31513  32432   -796     42  -2806       C  
-ATOM   3992  CD  GLU A 530     -35.978  -1.167  57.646  1.00282.73           C  
-ANISOU 3992  CD  GLU A 530    42778  31908  32738   -381   -216  -3022       C  
-ATOM   3993  OE1 GLU A 530     -35.150  -1.682  58.427  1.00283.12           O  
-ANISOU 3993  OE1 GLU A 530    42848  32073  32651   -242    -13  -2929       O  
-ATOM   3994  OE2 GLU A 530     -36.714  -0.212  57.971  1.00284.90           O  
-ANISOU 3994  OE2 GLU A 530    43079  32085  33086   -178   -637  -3299       O  
-ATOM   3995  N   LYS A 531     -39.980  -1.275  57.734  1.00203.47           N  
-ANISOU 3995  N   LYS A 531    32586  22110  22614     24     92  -3758       N  
-ATOM   3996  CA  LYS A 531     -40.524  -0.796  59.000  1.00202.72           C  
-ANISOU 3996  CA  LYS A 531    32476  22164  22386    496    -91  -4088       C  
-ATOM   3997  C   LYS A 531     -41.024  -1.948  59.867  1.00200.54           C  
-ANISOU 3997  C   LYS A 531    32106  22246  21843    709    508  -4115       C  
-ATOM   3998  O   LYS A 531     -41.020  -1.859  61.091  1.00202.31           O  
-ANISOU 3998  O   LYS A 531    32310  22665  21893   1088    482  -4278       O  
-ATOM   3999  CB  LYS A 531     -41.659   0.200  58.756  1.00206.97           C  
-ANISOU 3999  CB  LYS A 531    32993  22623  23023    622   -517  -4414       C  
-ATOM   4000  CG  LYS A 531     -41.203   1.636  58.564  1.00211.02           C  
-ANISOU 4000  CG  LYS A 531    33618  22808  23753    629  -1296  -4508       C  
-ATOM   4001  CD  LYS A 531     -42.363   2.521  58.139  1.00215.37           C  
-ANISOU 4001  CD  LYS A 531    34158  23252  24419    708  -1702  -4816       C  
-ATOM   4002  CE  LYS A 531     -43.550   2.370  59.076  1.00219.17           C  
-ANISOU 4002  CE  LYS A 531    34528  24070  24676   1161  -1534  -5188       C  
-ATOM   4003  NZ  LYS A 531     -44.722   3.170  58.623  1.00221.81           N  
-ANISOU 4003  NZ  LYS A 531    34839  24331  25108   1249  -1902  -5504       N  
-ATOM   4004  N   VAL A 532     -41.456  -3.029  59.227  1.00165.20           N  
-ANISOU 4004  N   VAL A 532    27572  17861  17337    459   1025  -3945       N  
-ATOM   4005  CA  VAL A 532     -41.959  -4.196  59.943  1.00163.66           C  
-ANISOU 4005  CA  VAL A 532    27288  17986  16908    591   1584  -3915       C  
-ATOM   4006  C   VAL A 532     -40.805  -5.061  60.459  1.00165.65           C  
-ANISOU 4006  C   VAL A 532    27598  18287  17056    572   1887  -3658       C  
-ATOM   4007  O   VAL A 532     -41.021  -6.133  61.023  1.00165.91           O  
-ANISOU 4007  O   VAL A 532    27581  18550  16907    632   2349  -3566       O  
-ATOM   4008  CB  VAL A 532     -42.893  -5.039  59.044  1.00157.06           C  
-ANISOU 4008  CB  VAL A 532    26380  17197  16099    320   1982  -3827       C  
-ATOM   4009  CG1 VAL A 532     -43.614  -6.101  59.856  1.00154.89           C  
-ANISOU 4009  CG1 VAL A 532    25997  17271  15584    466   2475  -3815       C  
-ATOM   4010  CG2 VAL A 532     -43.901  -4.139  58.347  1.00153.81           C  
-ANISOU 4010  CG2 VAL A 532    25928  16686  15826    288   1652  -4058       C  
-ATOM   4011  N   LEU A 533     -39.578  -4.578  60.278  1.00293.12           N  
-ANISOU 4011  N   LEU A 533    43842  34218  33311    484   1602  -3535       N  
-ATOM   4012  CA  LEU A 533     -38.386  -5.342  60.646  1.00294.13           C  
-ANISOU 4012  CA  LEU A 533    44029  34372  33355    448   1853  -3291       C  
-ATOM   4013  C   LEU A 533     -38.254  -5.556  62.152  1.00296.84           C  
-ANISOU 4013  C   LEU A 533    44362  34950  33475    834   1960  -3387       C  
-ATOM   4014  O   LEU A 533     -37.809  -6.614  62.596  1.00294.61           O  
-ANISOU 4014  O   LEU A 533    44090  34794  33054    836   2366  -3210       O  
-ATOM   4015  CB  LEU A 533     -37.121  -4.680  60.092  1.00296.28           C  
-ANISOU 4015  CB  LEU A 533    44385  34399  33788    260   1486  -3136       C  
-ATOM   4016  CG  LEU A 533     -36.190  -5.608  59.307  1.00295.12           C  
-ANISOU 4016  CG  LEU A 533    44260  34213  33659    -58   1800  -2813       C  
-ATOM   4017  CD1 LEU A 533     -36.966  -6.325  58.214  1.00296.28           C  
-ANISOU 4017  CD1 LEU A 533    44355  34358  33860   -330   2116  -2743       C  
-ATOM   4018  CD2 LEU A 533     -35.013  -4.841  58.721  1.00297.41           C  
-ANISOU 4018  CD2 LEU A 533    44592  34322  34090   -259   1400  -2654       C  
-ATOM   4019  N   ARG A 534     -38.636  -4.551  62.935  1.00268.16           N  
-ANISOU 4019  N   ARG A 534    40709  31378  29803   1171   1574  -3674       N  
-ATOM   4020  CA  ARG A 534     -38.600  -4.665  64.390  1.00271.85           C  
-ANISOU 4020  CA  ARG A 534    41143  32112  30037   1576   1645  -3800       C  
-ATOM   4021  C   ARG A 534     -39.414  -5.865  64.858  1.00272.24           C  
-ANISOU 4021  C   ARG A 534    41079  32496  29862   1622   2213  -3743       C  
-ATOM   4022  O   ARG A 534     -39.136  -6.446  65.908  1.00274.59           O  
-ANISOU 4022  O   ARG A 534    41357  33021  29952   1827   2452  -3693       O  
-ATOM   4023  CB  ARG A 534     -39.115  -3.385  65.053  1.00275.78           C  
-ANISOU 4023  CB  ARG A 534    41611  32654  30517   1960   1123  -4174       C  
-ATOM   4024  CG  ARG A 534     -38.057  -2.302  65.223  1.00278.81           C  
-ANISOU 4024  CG  ARG A 534    42121  32769  31046   2049    550  -4221       C  
-ATOM   4025  CD  ARG A 534     -37.347  -2.013  63.910  1.00278.08           C  
-ANISOU 4025  CD  ARG A 534    42120  32310  31226   1604    348  -3987       C  
-ATOM   4026  NE  ARG A 534     -37.733  -0.734  63.318  1.00279.45           N  
-ANISOU 4026  NE  ARG A 534    42329  32238  31612   1576   -259  -4175       N  
-ATOM   4027  CZ  ARG A 534     -38.978  -0.390  63.003  1.00280.22           C  
-ANISOU 4027  CZ  ARG A 534    42359  32381  31732   1638   -351  -4411       C  
-ATOM   4028  NH1 ARG A 534     -39.221   0.796  62.462  1.00281.29           N  
-ANISOU 4028  NH1 ARG A 534    42548  32254  32077   1606   -951  -4571       N  
-ATOM   4029  NH2 ARG A 534     -39.980  -1.223  63.236  1.00280.10           N  
-ANISOU 4029  NH2 ARG A 534    42220  32674  31531   1725    134  -4479       N  
-ATOM   4030  N   ASN A 535     -40.418  -6.233  64.069  1.00272.88           N  
-ANISOU 4030  N   ASN A 535    41087  32605  29990   1414   2413  -3734       N  
-ATOM   4031  CA  ASN A 535     -41.233  -7.405  64.360  1.00272.38           C  
-ANISOU 4031  CA  ASN A 535    40915  32833  29743   1383   2932  -3632       C  
-ATOM   4032  C   ASN A 535     -40.480  -8.706  64.077  1.00267.81           C  
-ANISOU 4032  C   ASN A 535    40417  32172  29167   1112   3358  -3282       C  
-ATOM   4033  O   ASN A 535     -40.086  -9.408  65.009  1.00267.62           O  
-ANISOU 4033  O   ASN A 535    40396  32325  28962   1246   3603  -3168       O  
-ATOM   4034  CB  ASN A 535     -42.565  -7.340  63.597  1.00274.49           C  
-ANISOU 4034  CB  ASN A 535    41076  33148  30070   1249   2976  -3742       C  
-ATOM   4035  CG  ASN A 535     -42.856  -8.601  62.803  1.00275.14           C  
-ANISOU 4035  CG  ASN A 535    41155  33192  30193    884   3440  -3470       C  
-ATOM   4036  OD1 ASN A 535     -43.288  -9.612  63.356  1.00277.05           O  
-ANISOU 4036  OD1 ASN A 535    41320  33689  30256    894   3834  -3342       O  
-ATOM   4037  ND2 ASN A 535     -42.626  -8.542  61.496  1.00274.42           N  
-ANISOU 4037  ND2 ASN A 535    41143  32787  30338    557   3370  -3375       N  
-ATOM   4038  N   ASN A 536     -40.261  -9.000  62.797  1.00206.92           N  
-ANISOU 4038  N   ASN A 536    32770  24196  21654    750   3416  -3124       N  
-ATOM   4039  CA  ASN A 536     -39.612 -10.240  62.362  1.00200.64           C  
-ANISOU 4039  CA  ASN A 536    32051  23309  20873    497   3785  -2826       C  
-ATOM   4040  C   ASN A 536     -39.534 -11.328  63.433  1.00199.38           C  
-ANISOU 4040  C   ASN A 536    31881  23381  20492    628   4158  -2689       C  
-ATOM   4041  O   ASN A 536     -38.445 -11.734  63.839  1.00199.07           O  
-ANISOU 4041  O   ASN A 536    31937  23295  20406    667   4226  -2549       O  
-ATOM   4042  CB  ASN A 536     -38.221  -9.949  61.791  1.00200.80           C  
-ANISOU 4042  CB  ASN A 536    32191  23072  21033    362   3588  -2705       C  
-ATOM   4043  CG  ASN A 536     -38.275  -9.385  60.382  1.00199.13           C  
-ANISOU 4043  CG  ASN A 536    31986  22628  21046     77   3366  -2704       C  
-ATOM   4044  OD1 ASN A 536     -38.810  -8.300  60.154  1.00199.52           O  
-ANISOU 4044  OD1 ASN A 536    31998  22618  21191    119   3014  -2896       O  
-ATOM   4045  ND2 ASN A 536     -37.710 -10.118  59.429  1.00199.14           N  
-ANISOU 4045  ND2 ASN A 536    32033  22506  21127   -202   3553  -2494       N  
-ATOM   4046  N   LYS A 537     -40.698 -11.790  63.882  1.00152.18           N  
-ANISOU 4046  N   LYS A 537    25782  17668  14373    686   4385  -2718       N  
-ATOM   4047  CA  LYS A 537     -40.779 -12.838  64.895  1.00153.41           C  
-ANISOU 4047  CA  LYS A 537    25904  18076  14307    776   4730  -2558       C  
-ATOM   4048  C   LYS A 537     -39.902 -14.029  64.533  1.00150.81           C  
-ANISOU 4048  C   LYS A 537    25717  17552  14032    551   4991  -2268       C  
-ATOM   4049  O   LYS A 537     -38.933 -14.336  65.226  1.00151.58           O  
-ANISOU 4049  O   LYS A 537    25898  17655  14042    671   5034  -2172       O  
-ATOM   4050  CB  LYS A 537     -42.229 -13.298  65.079  1.00153.23           C  
-ANISOU 4050  CB  LYS A 537    25715  18344  14160    745   4956  -2561       C  
-ATOM   4051  CG  LYS A 537     -43.044 -12.443  66.044  1.00155.07           C  
-ANISOU 4051  CG  LYS A 537    25770  18956  14195   1092   4795  -2823       C  
-ATOM   4052  CD  LYS A 537     -44.522 -12.804  65.993  1.00153.96           C  
-ANISOU 4052  CD  LYS A 537    25438  19112  13948   1019   4992  -2832       C  
-ATOM   4053  CE  LYS A 537     -45.301 -12.157  67.125  1.00154.85           C  
-ANISOU 4053  CE  LYS A 537    25338  19712  13786   1401   4891  -3069       C  
-ATOM   4054  NZ  LYS A 537     -46.763 -12.362  66.949  1.00156.00           N  
-ANISOU 4054  NZ  LYS A 537    25274  20164  13836   1325   5040  -3103       N  
-ATOM   4055  N   ASN A 538     -40.249 -14.694  63.438  1.00192.32           N  
-ANISOU 4055  N   ASN A 538    31004  22638  19432    244   5147  -2147       N  
-ATOM   4056  CA  ASN A 538     -39.520 -15.873  62.996  1.00189.21           C  
-ANISOU 4056  CA  ASN A 538    30743  22057  19093     45   5370  -1904       C  
-ATOM   4057  C   ASN A 538     -38.768 -15.605  61.695  1.00185.62           C  
-ANISOU 4057  C   ASN A 538    30377  21302  18849   -148   5217  -1903       C  
-ATOM   4058  O   ASN A 538     -37.973 -16.430  61.241  1.00182.44           O  
-ANISOU 4058  O   ASN A 538    30083  20746  18491   -272   5339  -1744       O  
-ATOM   4059  CB  ASN A 538     -40.482 -17.051  62.829  1.00194.94           C  
-ANISOU 4059  CB  ASN A 538    31434  22841  19794   -148   5678  -1738       C  
-ATOM   4060  CG  ASN A 538     -41.797 -16.838  63.562  1.00198.68           C  
-ANISOU 4060  CG  ASN A 538    31724  23652  20112    -43   5740  -1814       C  
-ATOM   4061  OD1 ASN A 538     -41.943 -17.213  64.726  1.00204.27           O  
-ANISOU 4061  OD1 ASN A 538    32373  24634  20608    110   5873  -1734       O  
-ATOM   4062  ND2 ASN A 538     -42.760 -16.230  62.880  1.00201.94           N  
-ANISOU 4062  ND2 ASN A 538    32035  24077  20616   -120   5640  -1969       N  
-ATOM   4063  N   PHE A 539     -39.026 -14.440  61.107  1.00148.46           N  
-ANISOU 4063  N   PHE A 539    25615  16533  14260   -163   4931  -2082       N  
-ATOM   4064  CA  PHE A 539     -38.394 -14.041  59.853  1.00147.19           C  
-ANISOU 4064  CA  PHE A 539    25504  16136  14286   -363   4751  -2072       C  
-ATOM   4065  C   PHE A 539     -36.897 -13.776  59.999  1.00146.54           C  
-ANISOU 4065  C   PHE A 539    25505  15976  14197   -297   4598  -2008       C  
-ATOM   4066  O   PHE A 539     -36.446 -13.220  61.000  1.00149.07           O  
-ANISOU 4066  O   PHE A 539    25833  16385  14423    -62   4452  -2074       O  
-ATOM   4067  CB  PHE A 539     -39.086 -12.805  59.277  1.00144.84           C  
-ANISOU 4067  CB  PHE A 539    25126  15794  14111   -397   4443  -2269       C  
-ATOM   4068  CG  PHE A 539     -40.363 -13.108  58.553  1.00143.59           C  
-ANISOU 4068  CG  PHE A 539    24897  15634  14025   -570   4580  -2303       C  
-ATOM   4069  CD1 PHE A 539     -40.509 -14.293  57.855  1.00142.02           C  
-ANISOU 4069  CD1 PHE A 539    24735  15355  13870   -790   4873  -2136       C  
-ATOM   4070  CD2 PHE A 539     -41.417 -12.211  58.571  1.00142.35           C  
-ANISOU 4070  CD2 PHE A 539    24641  15553  13894   -500   4392  -2513       C  
-ATOM   4071  CE1 PHE A 539     -41.680 -14.580  57.185  1.00139.46           C  
-ANISOU 4071  CE1 PHE A 539    24349  15020  13621   -955   4987  -2162       C  
-ATOM   4072  CE2 PHE A 539     -42.593 -12.491  57.903  1.00139.11           C  
-ANISOU 4072  CE2 PHE A 539    24159  15151  13547   -660   4519  -2544       C  
-ATOM   4073  CZ  PHE A 539     -42.725 -13.678  57.209  1.00138.31           C  
-ANISOU 4073  CZ  PHE A 539    24094  14963  13496   -898   4823  -2359       C  
-ATOM   4074  N   SER A 540     -36.136 -14.173  58.984  1.00206.77           N  
-ANISOU 4074  N   SER A 540    33185  23463  21917   -498   4625  -1885       N  
-ATOM   4075  CA  SER A 540     -34.692 -13.984  58.985  1.00205.06           C  
-ANISOU 4075  CA  SER A 540    33023  23207  21685   -469   4492  -1803       C  
-ATOM   4076  C   SER A 540     -34.267 -13.008  57.895  1.00204.70           C  
-ANISOU 4076  C   SER A 540    32931  23061  21783   -650   4176  -1816       C  
-ATOM   4077  O   SER A 540     -34.518 -13.235  56.711  1.00200.96           O  
-ANISOU 4077  O   SER A 540    32426  22520  21409   -879   4220  -1775       O  
-ATOM   4078  CB  SER A 540     -33.980 -15.324  58.796  1.00204.16           C  
-ANISOU 4078  CB  SER A 540    32990  23072  21510   -521   4776  -1635       C  
-ATOM   4079  OG  SER A 540     -32.574 -15.151  58.760  1.00205.13           O  
-ANISOU 4079  OG  SER A 540    33145  23195  21599   -489   4653  -1561       O  
-ATOM   4080  N   THR A 541     -33.624 -11.919  58.300  1.00194.84           N  
-ANISOU 4080  N   THR A 541    31677  21808  20546   -554   3840  -1861       N  
-ATOM   4081  CA  THR A 541     -33.158 -10.918  57.349  1.00197.20           C  
-ANISOU 4081  CA  THR A 541    31928  22019  20980   -746   3486  -1834       C  
-ATOM   4082  C   THR A 541     -31.762 -11.247  56.837  1.00197.41           C  
-ANISOU 4082  C   THR A 541    31956  22079  20971   -862   3493  -1644       C  
-ATOM   4083  O   THR A 541     -30.802 -11.295  57.607  1.00199.94           O  
-ANISOU 4083  O   THR A 541    32319  22455  21195   -712   3469  -1589       O  
-ATOM   4084  CB  THR A 541     -33.164  -9.507  57.963  1.00199.53           C  
-ANISOU 4084  CB  THR A 541    32217  22267  21329   -609   3042  -1967       C  
-ATOM   4085  OG1 THR A 541     -32.728  -9.577  59.326  1.00202.41           O  
-ANISOU 4085  OG1 THR A 541    32636  22713  21557   -313   3068  -2009       O  
-ATOM   4086  CG2 THR A 541     -34.563  -8.918  57.916  1.00201.92           C  
-ANISOU 4086  CG2 THR A 541    32481  22531  21710   -575   2924  -2170       C  
-ATOM   4087  N   VAL A 542     -31.655 -11.475  55.534  1.00179.91           N  
-ANISOU 4087  N   VAL A 542    29680  19857  18819  -1119   3526  -1550       N  
-ATOM   4088  CA  VAL A 542     -30.374 -11.807  54.929  1.00178.86           C  
-ANISOU 4088  CA  VAL A 542    29511  19824  18625  -1229   3537  -1378       C  
-ATOM   4089  C   VAL A 542     -29.846 -10.653  54.085  1.00180.85           C  
-ANISOU 4089  C   VAL A 542    29659  20086  18969  -1457   3139  -1284       C  
-ATOM   4090  O   VAL A 542     -28.970  -9.908  54.522  1.00181.38           O  
-ANISOU 4090  O   VAL A 542    29717  20178  19022  -1426   2860  -1215       O  
-ATOM   4091  CB  VAL A 542     -30.470 -13.073  54.064  1.00175.86           C  
-ANISOU 4091  CB  VAL A 542    29124  19490  18205  -1327   3877  -1326       C  
-ATOM   4092  CG1 VAL A 542     -29.118 -13.396  53.450  1.00171.49           C  
-ANISOU 4092  CG1 VAL A 542    28508  19097  17554  -1400   3872  -1175       C  
-ATOM   4093  CG2 VAL A 542     -30.975 -14.242  54.898  1.00172.17           C  
-ANISOU 4093  CG2 VAL A 542    28768  18990  17660  -1135   4229  -1381       C  
-ATOM   4094  N   ASP A 543     -30.380 -10.508  52.877  1.00269.03           N  
-ANISOU 4094  N   ASP A 543    40749  31237  30233  -1698   3098  -1266       N  
-ATOM   4095  CA  ASP A 543     -29.954  -9.438  51.984  1.00269.25           C  
-ANISOU 4095  CA  ASP A 543    40666  31287  30349  -1958   2712  -1145       C  
-ATOM   4096  C   ASP A 543     -30.592  -8.110  52.388  1.00268.56           C  
-ANISOU 4096  C   ASP A 543    40610  31016  30413  -1950   2301  -1253       C  
-ATOM   4097  O   ASP A 543     -31.685  -8.087  52.949  1.00268.40           O  
-ANISOU 4097  O   ASP A 543    40661  30878  30440  -1792   2365  -1451       O  
-ATOM   4098  CB  ASP A 543     -30.296  -9.783  50.543  1.00267.94           C  
-ANISOU 4098  CB  ASP A 543    40400  31185  30219  -2210   2816  -1087       C  
-ATOM   4099  N   ILE A 544     -29.901  -7.008  52.109  1.00155.83           N  
-ANISOU 4099  N   ILE A 544    26275  16730  16205  -2115   1856  -1122       N  
-ATOM   4100  CA  ILE A 544     -30.409  -5.682  52.456  1.00152.45           C  
-ANISOU 4100  CA  ILE A 544    25890  16099  15936  -2104   1378  -1226       C  
-ATOM   4101  C   ILE A 544     -29.635  -4.563  51.762  1.00151.15           C  
-ANISOU 4101  C   ILE A 544    25639  15923  15867  -2401    868  -1009       C  
-ATOM   4102  O   ILE A 544     -28.531  -4.201  52.177  1.00152.43           O  
-ANISOU 4102  O   ILE A 544    25788  16144  15984  -2400    656   -861       O  
-ATOM   4103  CB  ILE A 544     -30.394  -5.487  53.966  1.00155.85           C  
-ANISOU 4103  CB  ILE A 544    26436  16457  16324  -1752   1319  -1388       C  
-ATOM   4104  N   GLN A 545     -30.230  -4.020  50.703  1.00187.97           N  
-ANISOU 4104  N   GLN A 545    30241  20517  20663  -2667    663   -976       N  
-ATOM   4105  CA  GLN A 545     -29.605  -2.963  49.911  1.00185.08           C  
-ANISOU 4105  CA  GLN A 545    29779  20147  20395  -3007    161   -734       C  
-ATOM   4106  C   GLN A 545     -30.315  -1.626  50.094  1.00185.94           C  
-ANISOU 4106  C   GLN A 545    29973  19955  20722  -3024   -404   -860       C  
-ATOM   4107  O   GLN A 545     -31.361  -1.561  50.734  1.00187.99           O  
-ANISOU 4107  O   GLN A 545    30343  20046  21039  -2765   -369  -1157       O  
-ATOM   4108  CB  GLN A 545     -29.561  -3.350  48.432  1.00179.24           C  
-ANISOU 4108  CB  GLN A 545    28881  19600  19623  -3339    315   -548       C  
-ATOM   4109  CG  GLN A 545     -28.252  -3.994  48.023  1.00169.38           C  
-ANISOU 4109  CG  GLN A 545    27486  18693  18177  -3454    513   -287       C  
-ATOM   4110  CD  GLN A 545     -27.554  -4.657  49.197  1.00162.51           C  
-ANISOU 4110  CD  GLN A 545    26694  17890  17163  -3139    762   -344       C  
-ATOM   4111  OE1 GLN A 545     -27.813  -5.819  49.513  1.00156.92           O  
-ANISOU 4111  OE1 GLN A 545    26041  17238  16344  -2914   1247   -487       O  
-ATOM   4112  NE2 GLN A 545     -26.664  -3.919  49.852  1.00159.49           N  
-ANISOU 4112  NE2 GLN A 545    26322  17488  16788  -3131    407   -222       N  
-ATOM   4113  N   LYS A 546     -29.747  -0.559  49.539  1.00140.87           N  
-ANISOU 4113  N   LYS A 546    24205  14192  15128  -3328   -948   -630       N  
-ATOM   4114  CA  LYS A 546     -30.274   0.786  49.784  1.00142.50           C  
-ANISOU 4114  CA  LYS A 546    24514  14076  15555  -3333  -1585   -742       C  
-ATOM   4115  C   LYS A 546     -31.709   0.952  49.268  1.00142.00           C  
-ANISOU 4115  C   LYS A 546    24489  13847  15618  -3338  -1586   -973       C  
-ATOM   4116  O   LYS A 546     -32.555   1.550  49.951  1.00142.71           O  
-ANISOU 4116  O   LYS A 546    24707  13699  15819  -3088  -1842  -1268       O  
-ATOM   4117  CB  LYS A 546     -29.356   1.853  49.188  1.00144.48           C  
-ANISOU 4117  CB  LYS A 546    24687  14298  15911  -3716  -2193   -397       C  
-ATOM   4118  N   ASN A 547     -31.986   0.425  48.075  1.00174.68           N  
-ANISOU 4118  N   ASN A 547    28511  18129  19729  -3599  -1308   -856       N  
-ATOM   4119  CA  ASN A 547     -33.314   0.555  47.475  1.00174.15           C  
-ANISOU 4119  CA  ASN A 547    28469  17919  19782  -3637  -1298  -1052       C  
-ATOM   4120  C   ASN A 547     -34.390  -0.215  48.236  1.00172.89           C  
-ANISOU 4120  C   ASN A 547    28398  17733  19561  -3254   -852  -1409       C  
-ATOM   4121  O   ASN A 547     -35.323   0.382  48.786  1.00173.59           O  
-ANISOU 4121  O   ASN A 547    28586  17618  19752  -3043  -1088  -1692       O  
-ATOM   4122  CB  ASN A 547     -33.271   0.107  46.020  1.00163.32           C  
-ANISOU 4122  CB  ASN A 547    26942  16737  18377  -3999  -1087   -830       C  
-ATOM   4123  CG  ASN A 547     -32.126   0.756  45.254  1.00164.77           C  
-ANISOU 4123  CG  ASN A 547    26991  17047  18568  -4398  -1477   -429       C  
-ATOM   4124  OD1 ASN A 547     -31.673   1.848  45.601  1.00166.65           O  
-ANISOU 4124  OD1 ASN A 547    27276  17118  18925  -4480  -2059   -326       O  
-ATOM   4125  ND2 ASN A 547     -31.654   0.088  44.214  1.00164.15           N  
-ANISOU 4125  ND2 ASN A 547    26735  17279  18355  -4644  -1178   -197       N  
-ATOM   4126  N   GLY A 548     -34.263  -1.539  48.257  1.00153.73           N  
-ANISOU 4126  N   GLY A 548    25926  15527  16959  -3167   -230  -1392       N  
-ATOM   4127  CA  GLY A 548     -35.225  -2.379  48.944  1.00153.57           C  
-ANISOU 4127  CA  GLY A 548    25969  15515  16864  -2852    216  -1668       C  
-ATOM   4128  C   GLY A 548     -34.562  -3.330  49.920  1.00153.28           C  
-ANISOU 4128  C   GLY A 548    25961  15637  16640  -2602    608  -1655       C  
-ATOM   4129  O   GLY A 548     -33.336  -3.354  50.041  1.00152.79           O  
-ANISOU 4129  O   GLY A 548    25870  15681  16504  -2661    550  -1448       O  
-ATOM   4130  N   VAL A 549     -35.377  -4.116  50.615  1.00148.30           N  
-ANISOU 4130  N   VAL A 549    25381  15038  15929  -2333   1000  -1866       N  
-ATOM   4131  CA  VAL A 549     -34.871  -5.086  51.576  1.00149.17           C  
-ANISOU 4131  CA  VAL A 549    25528  15287  15861  -2092   1385  -1859       C  
-ATOM   4132  C   VAL A 549     -35.288  -6.504  51.184  1.00148.54           C  
-ANISOU 4132  C   VAL A 549    25425  15327  15687  -2112   1959  -1844       C  
-ATOM   4133  O   VAL A 549     -36.331  -6.706  50.560  1.00144.95           O  
-ANISOU 4133  O   VAL A 549    24946  14827  15300  -2199   2083  -1936       O  
-ATOM   4134  CB  VAL A 549     -35.335  -4.751  53.009  1.00150.97           C  
-ANISOU 4134  CB  VAL A 549    25840  15473  16050  -1720   1297  -2099       C  
-ATOM   4135  CG1 VAL A 549     -36.231  -5.850  53.565  1.00153.32           C  
-ANISOU 4135  CG1 VAL A 549    26149  15878  16226  -1516   1802  -2239       C  
-ATOM   4136  CG2 VAL A 549     -34.134  -4.513  53.915  1.00153.36           C  
-ANISOU 4136  CG2 VAL A 549    26186  15809  16276  -1573   1139  -2012       C  
-ATOM   4137  N   LYS A 550     -34.459  -7.480  51.540  1.00146.93           N  
-ANISOU 4137  N   LYS A 550    25233  15260  15335  -2030   2280  -1728       N  
-ATOM   4138  CA  LYS A 550     -34.671  -8.859  51.114  1.00147.74           C  
-ANISOU 4138  CA  LYS A 550    25327  15453  15355  -2058   2766  -1690       C  
-ATOM   4139  C   LYS A 550     -34.471  -9.826  52.278  1.00154.11           C  
-ANISOU 4139  C   LYS A 550    26213  16331  16011  -1787   3099  -1719       C  
-ATOM   4140  O   LYS A 550     -33.436  -9.813  52.941  1.00153.98           O  
-ANISOU 4140  O   LYS A 550    26224  16378  15903  -1672   3051  -1639       O  
-ATOM   4141  CB  LYS A 550     -33.724  -9.191  49.959  1.00138.10           C  
-ANISOU 4141  CB  LYS A 550    24017  14352  14102  -2300   2800  -1478       C  
-ATOM   4142  CG  LYS A 550     -33.413  -7.977  49.090  1.00129.81           C  
-ANISOU 4142  CG  LYS A 550    22877  13280  13165  -2566   2353  -1369       C  
-ATOM   4143  CD  LYS A 550     -32.999  -8.354  47.681  1.00114.43           C  
-ANISOU 4143  CD  LYS A 550    20803  11485  11191  -2836   2434  -1200       C  
-ATOM   4144  CE  LYS A 550     -33.293  -7.212  46.721  1.00102.75           C  
-ANISOU 4144  CE  LYS A 550    19240   9941   9858  -3125   2031  -1135       C  
-ATOM   4145  NZ  LYS A 550     -34.721  -6.793  46.807  1.00102.53           N  
-ANISOU 4145  NZ  LYS A 550    19283   9690   9984  -3086   1957  -1354       N  
-ATOM   4146  N   PHE A 551     -35.472 -10.664  52.525  1.00174.89           N  
-ANISOU 4146  N   PHE A 551    28878  18956  18618  -1700   3424  -1818       N  
-ATOM   4147  CA  PHE A 551     -35.451 -11.566  53.670  1.00183.53           C  
-ANISOU 4147  CA  PHE A 551    30044  20116  19574  -1462   3722  -1833       C  
-ATOM   4148  C   PHE A 551     -35.871 -12.974  53.276  1.00186.25           C  
-ANISOU 4148  C   PHE A 551    30413  20470  19882  -1519   4129  -1782       C  
-ATOM   4149  O   PHE A 551     -36.654 -13.161  52.345  1.00186.73           O  
-ANISOU 4149  O   PHE A 551    30437  20475  20037  -1688   4194  -1809       O  
-ATOM   4150  CB  PHE A 551     -36.386 -11.046  54.758  1.00188.75           C  
-ANISOU 4150  CB  PHE A 551    30716  20785  20216  -1244   3649  -2014       C  
-ATOM   4151  CG  PHE A 551     -37.733 -10.644  54.242  1.00195.79           C  
-ANISOU 4151  CG  PHE A 551    31553  21621  21216  -1331   3589  -2157       C  
-ATOM   4152  CD1 PHE A 551     -38.784 -11.545  54.225  1.00198.50           C  
-ANISOU 4152  CD1 PHE A 551    31885  22003  21534  -1341   3919  -2189       C  
-ATOM   4153  CD2 PHE A 551     -37.944  -9.367  53.755  1.00198.74           C  
-ANISOU 4153  CD2 PHE A 551    31890  21899  21723  -1414   3180  -2250       C  
-ATOM   4154  CE1 PHE A 551     -40.025 -11.173  53.743  1.00201.05           C  
-ANISOU 4154  CE1 PHE A 551    32148  22291  21950  -1420   3866  -2323       C  
-ATOM   4155  CE2 PHE A 551     -39.176  -8.991  53.272  1.00201.30           C  
-ANISOU 4155  CE2 PHE A 551    32168  22171  22146  -1482   3114  -2395       C  
-ATOM   4156  CZ  PHE A 551     -40.220  -9.894  53.263  1.00201.94           C  
-ANISOU 4156  CZ  PHE A 551    32226  22313  22189  -1480   3469  -2438       C  
-ATOM   4157  N   THR A 552     -35.354 -13.962  53.996  1.00210.29           N  
-ANISOU 4157  N   THR A 552    33530  23570  22800  -1375   4377  -1709       N  
-ATOM   4158  CA  THR A 552     -35.700 -15.352  53.733  1.00212.92           C  
-ANISOU 4158  CA  THR A 552    33912  23882  23107  -1413   4718  -1653       C  
-ATOM   4159  C   THR A 552     -36.435 -15.967  54.920  1.00211.74           C  
-ANISOU 4159  C   THR A 552    33815  23765  22873  -1248   4933  -1675       C  
-ATOM   4160  O   THR A 552     -35.825 -16.303  55.936  1.00211.94           O  
-ANISOU 4160  O   THR A 552    33900  23852  22776  -1070   5005  -1625       O  
-ATOM   4161  CB  THR A 552     -34.453 -16.199  53.405  1.00216.00           C  
-ANISOU 4161  CB  THR A 552    34347  24306  23417  -1408   4824  -1528       C  
-ATOM   4162  OG1 THR A 552     -33.716 -16.466  54.605  1.00220.09           O  
-ANISOU 4162  OG1 THR A 552    34939  24882  23805  -1195   4879  -1486       O  
-ATOM   4163  CG2 THR A 552     -33.557 -15.470  52.412  1.00218.87           C  
-ANISOU 4163  CG2 THR A 552    34621  24728  23811  -1551   4587  -1479       C  
-ATOM   4164  N   ASN A 553     -37.750 -16.102  54.787  1.00215.90           N  
-ANISOU 4164  N   ASN A 553    34305  24272  23456  -1316   5029  -1739       N  
-ATOM   4165  CA  ASN A 553     -38.562 -16.750  55.811  1.00212.96           C  
-ANISOU 4165  CA  ASN A 553    33946  23978  22990  -1205   5245  -1725       C  
-ATOM   4166  C   ASN A 553     -37.948 -18.070  56.269  1.00209.07           C  
-ANISOU 4166  C   ASN A 553    33562  23471  22403  -1152   5480  -1568       C  
-ATOM   4167  O   ASN A 553     -37.247 -18.734  55.509  1.00208.15           O  
-ANISOU 4167  O   ASN A 553    33509  23254  22323  -1237   5528  -1495       O  
-ATOM   4168  CB  ASN A 553     -39.989 -16.970  55.301  1.00219.61           C  
-ANISOU 4168  CB  ASN A 553    34726  24800  23915  -1350   5348  -1771       C  
-ATOM   4169  CG  ASN A 553     -40.764 -17.964  56.142  1.00225.17           C  
-ANISOU 4169  CG  ASN A 553    35438  25594  24521  -1311   5611  -1681       C  
-ATOM   4170  OD1 ASN A 553     -41.025 -19.086  55.710  1.00229.54           O  
-ANISOU 4170  OD1 ASN A 553    36048  26050  25117  -1448   5797  -1562       O  
-ATOM   4171  ND2 ASN A 553     -41.131 -17.560  57.352  1.00230.35           N  
-ANISOU 4171  ND2 ASN A 553    36033  26450  25040  -1122   5604  -1729       N  
-ATOM   4172  N   SER A 554     -38.210 -18.440  57.518  1.00141.41           N  
-ANISOU 4172  N   SER A 554    25009  15019  13703  -1001   5608  -1523       N  
-ATOM   4173  CA  SER A 554     -37.653 -19.657  58.097  1.00138.21           C  
-ANISOU 4173  CA  SER A 554    24717  14593  13203   -943   5801  -1365       C  
-ATOM   4174  C   SER A 554     -37.929 -20.902  57.253  1.00137.40           C  
-ANISOU 4174  C   SER A 554    24690  14326  13189  -1125   5958  -1260       C  
-ATOM   4175  O   SER A 554     -37.086 -21.793  57.159  1.00138.89           O  
-ANISOU 4175  O   SER A 554    24996  14418  13358  -1102   6018  -1169       O  
-ATOM   4176  CB  SER A 554     -38.184 -19.850  59.517  1.00137.31           C  
-ANISOU 4176  CB  SER A 554    24576  14663  12932   -794   5918  -1315       C  
-ATOM   4177  OG  SER A 554     -39.581 -19.618  59.568  1.00131.56           O  
-ANISOU 4177  OG  SER A 554    23727  14048  12211   -861   5963  -1366       O  
-ATOM   4178  N   LYS A 555     -39.110 -20.962  56.644  1.00162.89           N  
-ANISOU 4178  N   LYS A 555    26395  21676  13819  -1750    238  -3548       N  
-ATOM   4179  CA  LYS A 555     -39.482 -22.098  55.803  1.00160.15           C  
-ANISOU 4179  CA  LYS A 555    25912  21219  13718  -1470    205  -3396       C  
-ATOM   4180  C   LYS A 555     -38.805 -22.029  54.441  1.00159.13           C  
-ANISOU 4180  C   LYS A 555    25812  20837  13815  -1342    298  -3404       C  
-ATOM   4181  O   LYS A 555     -38.436 -23.054  53.867  1.00156.41           O  
-ANISOU 4181  O   LYS A 555    25258  20466  13706  -1215    224  -3219       O  
-ATOM   4182  CB  LYS A 555     -41.000 -22.162  55.622  1.00154.82           C  
-ANISOU 4182  CB  LYS A 555    25399  20437  12988  -1227    273  -3484       C  
-ATOM   4183  CG  LYS A 555     -41.461 -23.160  54.568  1.00147.54           C  
-ANISOU 4183  CG  LYS A 555    24395  19345  12320   -911    274  -3367       C  
-ATOM   4184  CD  LYS A 555     -41.019 -24.575  54.911  1.00144.30           C  
-ANISOU 4184  CD  LYS A 555    23631  19129  12069   -918     78  -3080       C  
-ATOM   4185  CE  LYS A 555     -41.541 -25.582  53.898  1.00140.17           C  
-ANISOU 4185  CE  LYS A 555    23028  18439  11790   -599     75  -2964       C  
-ATOM   4186  NZ  LYS A 555     -43.028 -25.649  53.891  1.00136.65           N  
-ANISOU 4186  NZ  LYS A 555    22730  17926  11266   -392    126  -3041       N  
-ATOM   4187  N   LEU A 556     -38.649 -20.815  53.925  1.00178.86           N  
-ANISOU 4187  N   LEU A 556    28572  23149  16239  -1374    460  -3622       N  
-ATOM   4188  CA  LEU A 556     -38.020 -20.614  52.626  1.00177.01           C  
-ANISOU 4188  CA  LEU A 556    28392  22664  16199  -1263    563  -3654       C  
-ATOM   4189  C   LEU A 556     -36.555 -21.041  52.647  1.00173.75           C  
-ANISOU 4189  C   LEU A 556    27731  22366  15921  -1433    460  -3487       C  
-ATOM   4190  O   LEU A 556     -36.105 -21.778  51.771  1.00171.50           O  
-ANISOU 4190  O   LEU A 556    27302  21981  15880  -1289    438  -3356       O  
-ATOM   4191  CB  LEU A 556     -38.139 -19.152  52.190  1.00188.20           C  
-ANISOU 4191  CB  LEU A 556    30147  23879  17482  -1293    752  -3928       C  
-ATOM   4192  CG  LEU A 556     -37.570 -18.812  50.811  1.00195.54           C  
-ANISOU 4192  CG  LEU A 556    31170  24532  18596  -1173    877  -3989       C  
-ATOM   4193  CD1 LEU A 556     -38.221 -19.672  49.737  1.00200.94           C  
-ANISOU 4193  CD1 LEU A 556    31816  25023  19508   -836    906  -3912       C  
-ATOM   4194  CD2 LEU A 556     -37.756 -17.336  50.507  1.00203.40           C  
-ANISOU 4194  CD2 LEU A 556    32506  25344  19431  -1220   1056  -4265       C  
-ATOM   4195  N   THR A 557     -35.814 -20.574  53.648  1.00129.83           N  
-ANISOU 4195  N   THR A 557    22119  17014  10196  -1739    395  -3492       N  
-ATOM   4196  CA  THR A 557     -34.408 -20.936  53.783  1.00127.27           C  
-ANISOU 4196  CA  THR A 557    21559  16821   9977  -1926    291  -3336       C  
-ATOM   4197  C   THR A 557     -34.264 -22.454  53.790  1.00124.52           C  
-ANISOU 4197  C   THR A 557    20887  16592   9832  -1821    128  -3066       C  
-ATOM   4198  O   THR A 557     -33.280 -22.997  53.290  1.00126.76           O  
-ANISOU 4198  O   THR A 557    20983  16869  10311  -1826     74  -2925       O  
-ATOM   4199  CB  THR A 557     -33.780 -20.347  55.068  1.00127.72           C  
-ANISOU 4199  CB  THR A 557    21586  17130   9810  -2274    221  -3361       C  
-ATOM   4200  OG1 THR A 557     -32.357 -20.498  55.022  1.00128.01           O  
-ANISOU 4200  OG1 THR A 557    21438  17249   9950  -2450    153  -3245       O  
-ATOM   4201  CG2 THR A 557     -34.319 -21.046  56.304  1.00128.57           C  
-ANISOU 4201  CG2 THR A 557    21534  17511   9804  -2347     69  -3239       C  
-ATOM   4202  N   SER A 558     -35.265 -23.127  54.351  1.00129.93           N  
-ANISOU 4202  N   SER A 558    21511  17384  10471  -1722     51  -2996       N  
-ATOM   4203  CA  SER A 558     -35.287 -24.582  54.419  1.00125.23           C  
-ANISOU 4203  CA  SER A 558    20622  16905  10054  -1611   -108  -2744       C  
-ATOM   4204  C   SER A 558     -35.398 -25.184  53.022  1.00121.36           C  
-ANISOU 4204  C   SER A 558    20111  16166   9833  -1312    -52  -2688       C  
-ATOM   4205  O   SER A 558     -34.570 -26.002  52.620  1.00119.42           O  
-ANISOU 4205  O   SER A 558    19636  15943   9795  -1288   -140  -2509       O  
-ATOM   4206  CB  SER A 558     -36.452 -25.055  55.293  1.00122.47           C  
-ANISOU 4206  CB  SER A 558    20250  16706   9576  -1562   -185  -2707       C  
-ATOM   4207  OG  SER A 558     -36.439 -24.411  56.558  1.00118.77           O  
-ANISOU 4207  OG  SER A 558    19830  16453   8846  -1828   -221  -2781       O  
-ATOM   4208  N   LEU A 559     -36.426 -24.772  52.286  1.00154.77           N  
-ANISOU 4208  N   LEU A 559    24585  20163  14059  -1083     94  -2843       N  
-ATOM   4209  CA  LEU A 559     -36.620 -25.233  50.914  1.00150.90           C  
-ANISOU 4209  CA  LEU A 559    24110  19415  13812   -789    166  -2816       C  
-ATOM   4210  C   LEU A 559     -35.444 -24.842  50.024  1.00150.68           C  
-ANISOU 4210  C   LEU A 559    24084  19245  13923   -831    234  -2838       C  
-ATOM   4211  O   LEU A 559     -35.160 -25.507  49.027  1.00147.58           O  
-ANISOU 4211  O   LEU A 559    23588  18714  13773   -645    234  -2736       O  
-ATOM   4212  CB  LEU A 559     -37.921 -24.670  50.329  1.00150.41           C  
-ANISOU 4212  CB  LEU A 559    24339  19121  13688   -562    326  -3010       C  
-ATOM   4213  CG  LEU A 559     -39.246 -25.280  50.794  1.00149.43           C  
-ANISOU 4213  CG  LEU A 559    24211  19064  13502   -411    275  -2970       C  
-ATOM   4214  CD1 LEU A 559     -40.418 -24.599  50.104  1.00149.21           C  
-ANISOU 4214  CD1 LEU A 559    24491  18784  13419   -192    452  -3180       C  
-ATOM   4215  CD2 LEU A 559     -39.268 -26.777  50.534  1.00150.60           C  
-ANISOU 4215  CD2 LEU A 559    24081  19262  13879   -242    135  -2718       C  
-ATOM   4216  N   ASN A 560     -34.763 -23.761  50.391  1.00141.42           N  
-ANISOU 4216  N   ASN A 560    23029  18109  12595  -1076    292  -2971       N  
-ATOM   4217  CA  ASN A 560     -33.676 -23.225  49.578  1.00142.63           C  
-ANISOU 4217  CA  ASN A 560    23217  18124  12851  -1133    371  -3019       C  
-ATOM   4218  C   ASN A 560     -32.359 -23.967  49.781  1.00144.54           C  
-ANISOU 4218  C   ASN A 560    23151  18539  13230  -1282    224  -2806       C  
-ATOM   4219  O   ASN A 560     -31.492 -23.958  48.909  1.00145.89           O  
-ANISOU 4219  O   ASN A 560    23277  18588  13566  -1254    262  -2779       O  
-ATOM   4220  CB  ASN A 560     -33.495 -21.732  49.848  1.00144.04           C  
-ANISOU 4220  CB  ASN A 560    23660  18261  12807  -1331    497  -3255       C  
-ATOM   4221  CG  ASN A 560     -33.224 -20.943  48.584  1.00143.98           C  
-ANISOU 4221  CG  ASN A 560    23857  17959  12889  -1227    671  -3409       C  
-ATOM   4222  OD1 ASN A 560     -32.551 -19.913  48.611  1.00145.42           O  
-ANISOU 4222  OD1 ASN A 560    24171  18113  12968  -1414    746  -3540       O  
-ATOM   4223  ND2 ASN A 560     -33.745 -21.427  47.465  1.00141.64           N  
-ANISOU 4223  ND2 ASN A 560    23588  17442  12785   -928    734  -3392       N  
-ATOM   4224  N   GLU A 561     -32.217 -24.611  50.934  1.00136.83           N  
-ANISOU 4224  N   GLU A 561    21959  17847  12182  -1439     55  -2653       N  
-ATOM   4225  CA  GLU A 561     -31.043 -25.430  51.212  1.00138.48           C  
-ANISOU 4225  CA  GLU A 561    21857  18240  12520  -1573   -102  -2434       C  
-ATOM   4226  C   GLU A 561     -31.089 -26.727  50.409  1.00135.04           C  
-ANISOU 4226  C   GLU A 561    21216  17731  12361  -1319   -174  -2241       C  
-ATOM   4227  O   GLU A 561     -30.163 -27.536  50.464  1.00135.10           O  
-ANISOU 4227  O   GLU A 561    20955  17862  12513  -1381   -304  -2047       O  
-ATOM   4228  CB  GLU A 561     -30.950 -25.737  52.705  1.00141.01           C  
-ANISOU 4228  CB  GLU A 561    22016  18886  12677  -1811   -261  -2331       C  
-ATOM   4229  CG  GLU A 561     -30.796 -24.504  53.573  1.00144.77           C  
-ANISOU 4229  CG  GLU A 561    22668  19458  12879  -2083   -206  -2506       C  
-ATOM   4230  CD  GLU A 561     -31.374 -24.697  54.960  1.00146.34           C  
-ANISOU 4230  CD  GLU A 561    22808  19916  12879  -2222   -318  -2467       C  
-ATOM   4231  OE1 GLU A 561     -31.691 -25.852  55.318  1.00146.77           O  
-ANISOU 4231  OE1 GLU A 561    22645  20105  13017  -2143   -459  -2279       O  
-ATOM   4232  OE2 GLU A 561     -31.521 -23.694  55.691  1.00147.09           O  
-ANISOU 4232  OE2 GLU A 561    23076  20078  12734  -2409   -266  -2626       O  
-ATOM   4233  N   GLU A 562     -32.177 -26.921  49.669  1.00145.35           N  
-ANISOU 4233  N   GLU A 562    22650  18836  13739  -1031    -91  -2296       N  
-ATOM   4234  CA  GLU A 562     -32.309 -28.084  48.799  1.00139.82           C  
-ANISOU 4234  CA  GLU A 562    21787  18034  13304   -765   -142  -2133       C  
-ATOM   4235  C   GLU A 562     -32.429 -27.677  47.333  1.00134.58           C  
-ANISOU 4235  C   GLU A 562    21306  17043  12787   -537     29  -2253       C  
-ATOM   4236  O   GLU A 562     -32.067 -28.444  46.443  1.00132.31           O  
-ANISOU 4236  O   GLU A 562    20878  16653  12741   -366      3  -2129       O  
-ATOM   4237  CB  GLU A 562     -33.499 -28.956  49.210  1.00141.94           C  
-ANISOU 4237  CB  GLU A 562    21994  18372  13566   -602   -225  -2042       C  
-ATOM   4238  CG  GLU A 562     -33.695 -30.180  48.322  1.00144.71           C  
-ANISOU 4238  CG  GLU A 562    22180  18614  14188   -319   -281  -1872       C  
-ATOM   4239  CD  GLU A 562     -34.771 -31.118  48.832  1.00147.47           C  
-ANISOU 4239  CD  GLU A 562    22437  19066  14530   -184   -387  -1758       C  
-ATOM   4240  OE1 GLU A 562     -35.233 -30.929  49.977  1.00151.27           O  
-ANISOU 4240  OE1 GLU A 562    22937  19739  14801   -336   -442  -1782       O  
-ATOM   4241  OE2 GLU A 562     -35.154 -32.046  48.087  1.00148.61           O  
-ANISOU 4241  OE2 GLU A 562    22489  19098  14878     73   -416  -1644       O  
-ATOM   4242  N   TYR A 563     -32.934 -26.473  47.079  1.00138.19           N  
-ANISOU 4242  N   TYR A 563    22073  17335  13098   -532    201  -2495       N  
-ATOM   4243  CA  TYR A 563     -33.009 -25.978  45.709  1.00133.14           C  
-ANISOU 4243  CA  TYR A 563    21622  16384  12583   -335    371  -2625       C  
-ATOM   4244  C   TYR A 563     -31.628 -25.550  45.229  1.00132.74           C  
-ANISOU 4244  C   TYR A 563    21527  16297  12613   -478    400  -2628       C  
-ATOM   4245  O   TYR A 563     -31.438 -25.236  44.055  1.00133.52           O  
-ANISOU 4245  O   TYR A 563    21733  16154  12844   -335    523  -2704       O  
-ATOM   4246  CB  TYR A 563     -34.006 -24.826  45.574  1.00130.27           C  
-ANISOU 4246  CB  TYR A 563    21609  15850  12038   -280    546  -2885       C  
-ATOM   4247  CG  TYR A 563     -34.376 -24.518  44.136  1.00125.97           C  
-ANISOU 4247  CG  TYR A 563    21253  14974  11637    -17    712  -3002       C  
-ATOM   4248  CD1 TYR A 563     -35.445 -25.159  43.521  1.00122.56           C  
-ANISOU 4248  CD1 TYR A 563    20851  14396  11319    286    738  -2976       C  
-ATOM   4249  CD2 TYR A 563     -33.654 -23.594  43.390  1.00124.10           C  
-ANISOU 4249  CD2 TYR A 563    21161  14569  11421    -73    841  -3137       C  
-ATOM   4250  CE1 TYR A 563     -35.786 -24.885  42.210  1.00118.66           C  
-ANISOU 4250  CE1 TYR A 563    20529  13601  10957    526    890  -3082       C  
-ATOM   4251  CE2 TYR A 563     -33.988 -23.315  42.077  1.00120.38           C  
-ANISOU 4251  CE2 TYR A 563    20861  13797  11082    165    992  -3243       C  
-ATOM   4252  CZ  TYR A 563     -35.054 -23.963  41.494  1.00117.96           C  
-ANISOU 4252  CZ  TYR A 563    20581  13351  10887    465   1016  -3215       C  
-ATOM   4253  OH  TYR A 563     -35.391 -23.689  40.190  1.00115.40           O  
-ANISOU 4253  OH  TYR A 563    20426  12727  10694    702   1167  -3321       O  
-ATOM   4254  N   THR A 564     -30.670 -25.532  46.150  1.00119.17           N  
-ANISOU 4254  N   THR A 564    19647  14820  10811   -763    288  -2545       N  
-ATOM   4255  CA  THR A 564     -29.272 -25.340  45.791  1.00117.44           C  
-ANISOU 4255  CA  THR A 564    19327  14610  10686   -908    281  -2503       C  
-ATOM   4256  C   THR A 564     -28.536 -26.662  45.970  1.00116.96           C  
-ANISOU 4256  C   THR A 564    18908  14725  10807   -916     95  -2232       C  
-ATOM   4257  O   THR A 564     -27.350 -26.778  45.667  1.00117.06           O  
-ANISOU 4257  O   THR A 564    18778  14767  10933  -1012     59  -2150       O  
-ATOM   4258  CB  THR A 564     -28.604 -24.252  46.641  1.00118.09           C  
-ANISOU 4258  CB  THR A 564    19501  14827  10542  -1239    300  -2618       C  
-ATOM   4259  OG1 THR A 564     -28.468 -24.713  47.989  1.00117.86           O  
-ANISOU 4259  OG1 THR A 564    19285  15103  10392  -1442    136  -2493       O  
-ATOM   4260  CG2 THR A 564     -29.434 -22.978  46.622  1.00115.34           C  
-ANISOU 4260  CG2 THR A 564    19504  14330   9990  -1239    469  -2884       C  
-ATOM   4261  N   LYS A 565     -29.257 -27.657  46.476  1.00116.71           N  
-ANISOU 4261  N   LYS A 565    18734  14812  10799   -815    -26  -2094       N  
-ATOM   4262  CA  LYS A 565     -28.756 -29.023  46.541  1.00115.27           C  
-ANISOU 4262  CA  LYS A 565    18221  14769  10809   -768   -202  -1834       C  
-ATOM   4263  C   LYS A 565     -29.131 -29.741  45.249  1.00112.85           C  
-ANISOU 4263  C   LYS A 565    17891  14233  10755   -433   -161  -1776       C  
-ATOM   4264  O   LYS A 565     -28.570 -30.785  44.918  1.00111.17           O  
-ANISOU 4264  O   LYS A 565    17428  14062  10749   -354   -274  -1579       O  
-ATOM   4265  CB  LYS A 565     -29.359 -29.751  47.743  1.00115.43           C  
-ANISOU 4265  CB  LYS A 565    18098  15035  10727   -828   -358  -1710       C  
-ATOM   4266  CG  LYS A 565     -28.898 -31.191  47.911  1.00114.72           C  
-ANISOU 4266  CG  LYS A 565    17663  15103  10822   -787   -553  -1437       C  
-ATOM   4267  CD  LYS A 565     -29.605 -31.848  49.089  1.00115.92           C  
-ANISOU 4267  CD  LYS A 565    17699  15486  10861   -839   -697  -1330       C  
-ATOM   4268  CE  LYS A 565     -29.492 -30.993  50.344  1.00118.14           C  
-ANISOU 4268  CE  LYS A 565    18058  15965  10863  -1145   -707  -1428       C  
-ATOM   4269  NZ  LYS A 565     -30.247 -31.574  51.479  1.00117.76           N  
-ANISOU 4269  NZ  LYS A 565    17915  16135  10694  -1191   -837  -1338       N  
-ATOM   4270  N   ASN A 566     -30.088 -29.165  44.525  1.00121.14           N  
-ANISOU 4270  N   ASN A 566    19206  15037  11784   -237      1  -1951       N  
-ATOM   4271  CA  ASN A 566     -30.573 -29.732  43.270  1.00120.62           C  
-ANISOU 4271  CA  ASN A 566    19158  14731  11942     92     61  -1923       C  
-ATOM   4272  C   ASN A 566     -30.451 -28.771  42.088  1.00122.83           C  
-ANISOU 4272  C   ASN A 566    19680  14723  12267    189    260  -2113       C  
-ATOM   4273  O   ASN A 566     -31.078 -28.967  41.047  1.00120.10           O  
-ANISOU 4273  O   ASN A 566    19428  14144  12061    466    349  -2149       O  
-ATOM   4274  CB  ASN A 566     -32.021 -30.209  43.417  1.00115.65           C  
-ANISOU 4274  CB  ASN A 566    18594  14065  11282    301     54  -1922       C  
-ATOM   4275  CG  ASN A 566     -32.130 -31.503  44.198  1.00113.73           C  
-ANISOU 4275  CG  ASN A 566    18066  14055  11091    299   -153  -1686       C  
-ATOM   4276  OD1 ASN A 566     -31.295 -31.800  45.052  1.00113.65           O  
-ANISOU 4276  OD1 ASN A 566    17852  14288  11042     70   -291  -1562       O  
-ATOM   4277  ND2 ASN A 566     -33.156 -32.289  43.898  1.00110.45           N  
-ANISOU 4277  ND2 ASN A 566    17633  13566  10767    554   -177  -1621       N  
-ATOM   4278  N   LYS A 567     -29.644 -27.731  42.255  1.00131.92           N  
-ANISOU 4278  N   LYS A 567    20932  15892  13300    -43    328  -2233       N  
-ATOM   4279  CA  LYS A 567     -29.385 -26.790  41.175  1.00134.94           C  
-ANISOU 4279  CA  LYS A 567    21531  16018  13722     17    508  -2407       C  
-ATOM   4280  C   LYS A 567     -27.898 -26.806  40.859  1.00140.52           C  
-ANISOU 4280  C   LYS A 567    22077  16770  14543   -126    471  -2325       C  
-ATOM   4281  O   LYS A 567     -27.493 -26.615  39.713  1.00140.88           O  
-ANISOU 4281  O   LYS A 567    22176  16612  14741     -5    569  -2367       O  
-ATOM   4282  CB  LYS A 567     -29.842 -25.383  41.564  1.00137.07           C  
-ANISOU 4282  CB  LYS A 567    22111  16234  13735   -118    646  -2657       C  
-ATOM   4283  CG  LYS A 567     -29.977 -24.405  40.402  1.00136.19           C  
-ANISOU 4283  CG  LYS A 567    22276  15819  13652      2    851  -2863       C  
-ATOM   4284  CD  LYS A 567     -28.663 -23.717  40.074  1.00139.14           C  
-ANISOU 4284  CD  LYS A 567    22651  16175  14042   -185    896  -2906       C  
-ATOM   4285  CE  LYS A 567     -28.903 -22.493  39.207  1.00140.92           C  
-ANISOU 4285  CE  LYS A 567    23197  16129  14217   -125   1103  -3149       C  
-ATOM   4286  NZ  LYS A 567     -29.846 -21.543  39.863  1.00142.09           N  
-ANISOU 4286  NZ  LYS A 567    23610  16268  14108   -195   1186  -3346       N  
-ATOM   4287  N   THR A 568     -27.087 -27.039  41.886  1.00126.19           N  
-ANISOU 4287  N   THR A 568    20064  15227  12655   -385    329  -2206       N  
-ATOM   4288  CA  THR A 568     -25.654 -27.196  41.694  1.00133.14           C  
-ANISOU 4288  CA  THR A 568    20755  16186  13647   -528    269  -2100       C  
-ATOM   4289  C   THR A 568     -25.345 -28.640  41.333  1.00137.01           C  
-ANISOU 4289  C   THR A 568    20943  16728  14386   -369    128  -1856       C  
-ATOM   4290  O   THR A 568     -24.443 -28.912  40.543  1.00137.87           O  
-ANISOU 4290  O   THR A 568    20935  16772  14678   -328    125  -1782       O  
-ATOM   4291  CB  THR A 568     -24.851 -26.806  42.948  1.00132.09           C  
-ANISOU 4291  CB  THR A 568    20536  16326  13328   -884    176  -2077       C  
-ATOM   4292  OG1 THR A 568     -23.453 -26.795  42.634  1.00131.84           O  
-ANISOU 4292  OG1 THR A 568    20358  16337  13400  -1018    146  -2004       O  
-ATOM   4293  CG2 THR A 568     -25.100 -27.795  44.076  1.00132.02           C  
-ANISOU 4293  CG2 THR A 568    20297  16582  13281   -947    -13  -1895       C  
-ATOM   4294  N   GLU A 569     -26.101 -29.565  41.914  1.00235.77           N  
-ANISOU 4294  N   GLU A 569    33327  29353  26900   -280      9  -1731       N  
-ATOM   4295  CA  GLU A 569     -25.929 -30.975  41.606  1.00235.95           C  
-ANISOU 4295  CA  GLU A 569    33071  29423  27155   -115   -131  -1499       C  
-ATOM   4296  C   GLU A 569     -26.418 -31.248  40.189  1.00230.17           C  
-ANISOU 4296  C   GLU A 569    32422  28401  26630    217    -26  -1527       C  
-ATOM   4297  O   GLU A 569     -25.979 -32.197  39.541  1.00227.36           O  
-ANISOU 4297  O   GLU A 569    31865  28016  26504    363    -99  -1366       O  
-ATOM   4298  CB  GLU A 569     -26.683 -31.850  42.610  1.00247.30           C  
-ANISOU 4298  CB  GLU A 569    34372  31057  28534   -105   -282  -1367       C  
-ATOM   4299  CG  GLU A 569     -27.880 -32.576  42.021  1.00260.64           C  
-ANISOU 4299  CG  GLU A 569    36095  32595  30342    219   -268  -1334       C  
-ATOM   4300  CD  GLU A 569     -27.903 -34.047  42.388  1.00271.97           C  
-ANISOU 4300  CD  GLU A 569    37227  34194  31914    298   -468  -1080       C  
-ATOM   4301  OE1 GLU A 569     -28.619 -34.819  41.716  1.00278.31           O  
-ANISOU 4301  OE1 GLU A 569    38004  34866  32875    578   -475  -1013       O  
-ATOM   4302  OE2 GLU A 569     -27.203 -34.432  43.348  1.00281.83           O  
-ANISOU 4302  OE2 GLU A 569    38266  35703  33114     78   -620   -946       O  
-ATOM   4303  N   TYR A 570     -27.326 -30.401  39.714  1.00143.72           N  
-ANISOU 4303  N   TYR A 570    21773  17239  15596    335    145  -1733       N  
-ATOM   4304  CA  TYR A 570     -27.852 -30.519  38.361  1.00138.56           C  
-ANISOU 4304  CA  TYR A 570    21232  16294  15119    646    264  -1787       C  
-ATOM   4305  C   TYR A 570     -26.885 -29.903  37.364  1.00139.16           C  
-ANISOU 4305  C   TYR A 570    21368  16211  15296    629    375  -1863       C  
-ATOM   4306  O   TYR A 570     -26.653 -30.453  36.289  1.00140.94           O  
-ANISOU 4306  O   TYR A 570    21516  16286  15749    836    392  -1793       O  
-ATOM   4307  CB  TYR A 570     -29.211 -29.829  38.257  1.00130.53           C  
-ANISOU 4307  CB  TYR A 570    20517  15112  13966    775    406  -1983       C  
-ATOM   4308  CG  TYR A 570     -29.811 -29.842  36.868  1.00121.83           C  
-ANISOU 4308  CG  TYR A 570    19561  13699  13030   1090    544  -2058       C  
-ATOM   4309  CD1 TYR A 570     -30.695 -30.840  36.482  1.00115.77           C  
-ANISOU 4309  CD1 TYR A 570    18725  12859  12403   1367    500  -1956       C  
-ATOM   4310  CD2 TYR A 570     -29.499 -28.853  35.946  1.00117.41           C  
-ANISOU 4310  CD2 TYR A 570    19208  12919  12484   1110    716  -2232       C  
-ATOM   4311  CE1 TYR A 570     -31.250 -30.854  35.217  1.00108.30           C  
-ANISOU 4311  CE1 TYR A 570    17912  11628  11608   1656    626  -2025       C  
-ATOM   4312  CE2 TYR A 570     -30.048 -28.860  34.677  1.00109.96           C  
-ANISOU 4312  CE2 TYR A 570    18397  11691  11692   1397    843  -2302       C  
-ATOM   4313  CZ  TYR A 570     -30.922 -29.863  34.319  1.00106.64           C  
-ANISOU 4313  CZ  TYR A 570    17905  11203  11410   1670    797  -2198       C  
-ATOM   4314  OH  TYR A 570     -31.470 -29.873  33.058  1.00102.73           O  
-ANISOU 4314  OH  TYR A 570    17542  10425  11065   1955    923  -2267       O  
-ATOM   4315  N   GLU A 571     -26.320 -28.757  37.730  1.00134.65           N  
-ANISOU 4315  N   GLU A 571    20933  15675  14551    381    449  -2006       N  
-ATOM   4316  CA  GLU A 571     -25.396 -28.047  36.854  1.00133.36           C  
-ANISOU 4316  CA  GLU A 571    20846  15370  14456    337    560  -2094       C  
-ATOM   4317  C   GLU A 571     -24.069 -28.786  36.691  1.00131.96           C  
-ANISOU 4317  C   GLU A 571    20372  15314  14452    263    437  -1900       C  
-ATOM   4318  O   GLU A 571     -23.629 -29.045  35.572  1.00130.69           O  
-ANISOU 4318  O   GLU A 571    20166  14996  14495    421    482  -1867       O  
-ATOM   4319  CB  GLU A 571     -25.151 -26.626  37.367  1.00136.20           C  
-ANISOU 4319  CB  GLU A 571    21429  15748  14572     78    662  -2295       C  
-ATOM   4320  CG  GLU A 571     -24.162 -25.831  36.529  1.00136.17           C  
-ANISOU 4320  CG  GLU A 571    21507  15609  14622      8    775  -2390       C  
-ATOM   4321  CD  GLU A 571     -24.030 -24.391  36.985  1.00137.56           C  
-ANISOU 4321  CD  GLU A 571    21930  15782  14555   -230    884  -2601       C  
-ATOM   4322  OE1 GLU A 571     -23.011 -23.750  36.649  1.00139.03           O  
-ANISOU 4322  OE1 GLU A 571    22138  15941  14745   -375    936  -2652       O  
-ATOM   4323  OE2 GLU A 571     -24.947 -23.898  37.677  1.00137.36           O  
-ANISOU 4323  OE2 GLU A 571    22077  15782  14333   -270    918  -2717       O  
-ATOM   4324  N   GLU A 572     -23.436 -29.126  37.809  1.00130.75           N  
-ANISOU 4324  N   GLU A 572    20016  15444  14218     25    283  -1773       N  
-ATOM   4325  CA  GLU A 572     -22.129 -29.777  37.775  1.00129.25           C  
-ANISOU 4325  CA  GLU A 572    19543  15395  14171    -76    160  -1592       C  
-ATOM   4326  C   GLU A 572     -22.217 -31.183  37.194  1.00124.94           C  
-ANISOU 4326  C   GLU A 572    18764  14826  13882    176     53  -1389       C  
-ATOM   4327  O   GLU A 572     -21.200 -31.836  36.960  1.00123.48           O  
-ANISOU 4327  O   GLU A 572    18341  14723  13854    150    -44  -1233       O  
-ATOM   4328  CB  GLU A 572     -21.506 -29.815  39.171  1.00133.06           C  
-ANISOU 4328  CB  GLU A 572    19869  16191  14496   -391     16  -1505       C  
-ATOM   4329  CG  GLU A 572     -21.535 -28.479  39.903  1.00138.53           C  
-ANISOU 4329  CG  GLU A 572    20789  16929  14916   -645    106  -1699       C  
-ATOM   4330  CD  GLU A 572     -20.932 -27.345  39.093  1.00141.78           C  
-ANISOU 4330  CD  GLU A 572    21394  17162  15315   -701    270  -1871       C  
-ATOM   4331  OE1 GLU A 572     -20.209 -27.621  38.113  1.00144.02           O  
-ANISOU 4331  OE1 GLU A 572    21586  17339  15795   -604    290  -1813       O  
-ATOM   4332  OE2 GLU A 572     -21.186 -26.172  39.440  1.00143.78           O  
-ANISOU 4332  OE2 GLU A 572    21892  17379  15359   -844    379  -2064       O  
-ATOM   4333  N   ALA A 573     -23.441 -31.643  36.963  1.00133.16           N  
-ANISOU 4333  N   ALA A 573    19876  15757  14962    421     70  -1393       N  
-ATOM   4334  CA  ALA A 573     -23.661 -32.941  36.346  1.00129.41           C  
-ANISOU 4334  CA  ALA A 573    19209  15232  14728    685    -19  -1215       C  
-ATOM   4335  C   ALA A 573     -24.032 -32.772  34.880  1.00127.23           C  
-ANISOU 4335  C   ALA A 573    19088  14640  14614    968    136  -1311       C  
-ATOM   4336  O   ALA A 573     -23.898 -33.702  34.087  1.00126.34           O  
-ANISOU 4336  O   ALA A 573    18821  14449  14733   1181     88  -1178       O  
-ATOM   4337  CB  ALA A 573     -24.749 -33.702  37.082  1.00128.67           C  
-ANISOU 4337  CB  ALA A 573    19061  15241  14587    774   -122  -1130       C  
-ATOM   4338  N   GLN A 574     -24.498 -31.579  34.525  1.00122.84           N  
-ANISOU 4338  N   GLN A 574    18838  13902  13933    968    320  -1541       N  
-ATOM   4339  CA  GLN A 574     -24.896 -31.296  33.151  1.00120.95           C  
-ANISOU 4339  CA  GLN A 574    18774  13355  13827   1225    481  -1653       C  
-ATOM   4340  C   GLN A 574     -23.701 -30.863  32.313  1.00122.20           C  
-ANISOU 4340  C   GLN A 574    18913  13425  14091   1169    548  -1681       C  
-ATOM   4341  O   GLN A 574     -23.695 -31.033  31.096  1.00121.06           O  
-ANISOU 4341  O   GLN A 574    18797  13066  14133   1392    627  -1692       O  
-ATOM   4342  CB  GLN A 574     -25.978 -30.218  33.106  1.00117.42           C  
-ANISOU 4342  CB  GLN A 574    18671  12742  13203   1265    650  -1892       C  
-ATOM   4343  CG  GLN A 574     -26.569 -30.006  31.722  1.00110.39           C  
-ANISOU 4343  CG  GLN A 574    17965  11529  12448   1555    812  -2004       C  
-ATOM   4344  CD  GLN A 574     -27.256 -28.664  31.582  1.00107.18           C  
-ANISOU 4344  CD  GLN A 574    17912  10952  11860   1533   1001  -2266       C  
-ATOM   4345  OE1 GLN A 574     -28.365 -28.572  31.056  1.00103.41           O  
-ANISOU 4345  OE1 GLN A 574    17615  10280  11396   1758   1101  -2362       O  
-ATOM   4346  NE2 GLN A 574     -26.594 -27.611  32.046  1.00106.56           N  
-ANISOU 4346  NE2 GLN A 574    17935  10942  11610   1262   1050  -2384       N  
-ATOM   4347  N   ASP A 575     -22.692 -30.297  32.968  1.00142.95           N  
-ANISOU 4347  N   ASP A 575    21494  16222  16599    868    515  -1692       N  
-ATOM   4348  CA  ASP A 575     -21.463 -29.908  32.285  1.00142.70           C  
-ANISOU 4348  CA  ASP A 575    21421  16141  16656    783    563  -1704       C  
-ATOM   4349  C   ASP A 575     -20.407 -31.006  32.384  1.00139.10           C  
-ANISOU 4349  C   ASP A 575    20616  15866  16370    743    388  -1465       C  
-ATOM   4350  O   ASP A 575     -19.310 -30.880  31.839  1.00138.08           O  
-ANISOU 4350  O   ASP A 575    20403  15724  16339    681    400  -1438       O  
-ATOM   4351  CB  ASP A 575     -20.926 -28.586  32.839  1.00152.17           C  
-ANISOU 4351  CB  ASP A 575    22785  17400  17632    481    641  -1866       C  
-ATOM   4352  CG  ASP A 575     -20.934 -28.543  34.352  1.00158.92           C  
-ANISOU 4352  CG  ASP A 575    23573  18531  18278    222    523  -1826       C  
-ATOM   4353  OD1 ASP A 575     -20.786 -29.613  34.979  1.00165.47           O  
-ANISOU 4353  OD1 ASP A 575    24143  19561  19168    207    349  -1627       O  
-ATOM   4354  OD2 ASP A 575     -21.091 -27.440  34.917  1.00164.25           O  
-ANISOU 4354  OD2 ASP A 575    24456  19223  18728     34    604  -1994       O  
-ATOM   4355  N   ALA A 576     -20.745 -32.083  33.086  1.00125.82           N  
-ANISOU 4355  N   ALA A 576    18731  14354  14719    780    223  -1291       N  
-ATOM   4356  CA  ALA A 576     -19.871 -33.246  33.165  1.00121.34           C  
-ANISOU 4356  CA  ALA A 576    17827  13951  14325    775     48  -1053       C  
-ATOM   4357  C   ALA A 576     -19.960 -34.026  31.864  1.00115.18           C  
-ANISOU 4357  C   ALA A 576    16974  12975  13816   1093     67   -977       C  
-ATOM   4358  O   ALA A 576     -18.943 -34.392  31.275  1.00115.65           O  
-ANISOU 4358  O   ALA A 576    16865  13037  14038   1103     30   -881       O  
-ATOM   4359  CB  ALA A 576     -20.258 -34.128  34.341  1.00123.09           C  
-ANISOU 4359  CB  ALA A 576    17867  14412  14488    715   -133   -897       C  
-ATOM   4360  N   ILE A 577     -21.187 -34.273  31.417  1.00104.07           N  
-ANISOU 4360  N   ILE A 577    15694  11395  12453   1352    126  -1021       N  
-ATOM   4361  CA  ILE A 577     -21.410 -34.943  30.144  1.00 97.00           C  
-ANISOU 4361  CA  ILE A 577    14762  10289  11806   1670    161   -969       C  
-ATOM   4362  C   ILE A 577     -21.000 -34.042  28.986  1.00 94.54           C  
-ANISOU 4362  C   ILE A 577    14629   9743  11549   1722    342  -1126       C  
-ATOM   4363  O   ILE A 577     -20.571 -34.524  27.939  1.00 93.93           O  
-ANISOU 4363  O   ILE A 577    14457   9543  11689   1899    354  -1060       O  
-ATOM   4364  CB  ILE A 577     -22.878 -35.367  29.967  1.00 93.01           C  
-ANISOU 4364  CB  ILE A 577    14367   9651  11322   1932    187   -988       C  
-ATOM   4365  CG1 ILE A 577     -23.809 -34.193  30.267  1.00 91.17           C  
-ANISOU 4365  CG1 ILE A 577    14458   9320  10861   1876    339  -1218       C  
-ATOM   4366  CG2 ILE A 577     -23.202 -36.554  30.865  1.00 92.20           C  
-ANISOU 4366  CG2 ILE A 577    14033   9762  11238   1941    -13   -787       C  
-ATOM   4367  CD1 ILE A 577     -25.273 -34.515  30.076  1.00 87.84           C  
-ANISOU 4367  CD1 ILE A 577    14166   8762  10448   2129    378  -1254       C  
-ATOM   4368  N   VAL A 578     -21.127 -32.732  29.178  1.00 77.57           N  
-ANISOU 4368  N   VAL A 578    12738   7535   9201   1566    483  -1335       N  
-ATOM   4369  CA  VAL A 578     -20.685 -31.780  28.165  1.00 77.43           C  
-ANISOU 4369  CA  VAL A 578    12898   7308   9212   1580    654  -1493       C  
-ATOM   4370  C   VAL A 578     -19.200 -31.977  27.883  1.00 78.50           C  
-ANISOU 4370  C   VAL A 578    12823   7539   9465   1458    592  -1386       C  
-ATOM   4371  O   VAL A 578     -18.765 -31.943  26.732  1.00 77.75           O  
-ANISOU 4371  O   VAL A 578    12734   7273   9533   1594    670  -1403       O  
-ATOM   4372  CB  VAL A 578     -20.940 -30.321  28.588  1.00 78.37           C  
-ANISOU 4372  CB  VAL A 578    13312   7388   9078   1385    794  -1725       C  
-ATOM   4373  CG1 VAL A 578     -20.255 -29.366  27.627  1.00 78.53           C  
-ANISOU 4373  CG1 VAL A 578    13479   7231   9129   1356    949  -1866       C  
-ATOM   4374  CG2 VAL A 578     -22.431 -30.041  28.642  1.00 77.10           C  
-ANISOU 4374  CG2 VAL A 578    13389   7088   8818   1540    884  -1854       C  
-ATOM   4375  N   LYS A 579     -18.428 -32.199  28.941  1.00 95.25           N  
-ANISOU 4375  N   LYS A 579    14753   9937  11502   1202    449  -1272       N  
-ATOM   4376  CA  LYS A 579     -17.001 -32.457  28.800  1.00 97.77           C  
-ANISOU 4376  CA  LYS A 579    14849  10377  11923   1070    370  -1155       C  
-ATOM   4377  C   LYS A 579     -16.768 -33.724  27.979  1.00 96.24           C  
-ANISOU 4377  C   LYS A 579    14420  10138  12009   1320    282   -971       C  
-ATOM   4378  O   LYS A 579     -15.725 -33.879  27.346  1.00 95.43           O  
-ANISOU 4378  O   LYS A 579    14185  10030  12045   1312    271   -908       O  
-ATOM   4379  CB  LYS A 579     -16.339 -32.568  30.178  1.00101.30           C  
-ANISOU 4379  CB  LYS A 579    15125  11139  12226    761    219  -1055       C  
-ATOM   4380  CG  LYS A 579     -14.823 -32.421  30.163  1.00105.00           C  
-ANISOU 4380  CG  LYS A 579    15431  11736  12730    553    173   -991       C  
-ATOM   4381  CD  LYS A 579     -14.120 -33.765  30.029  1.00108.20           C  
-ANISOU 4381  CD  LYS A 579    15494  12269  13349    634      0   -746       C  
-ATOM   4382  CE  LYS A 579     -13.729 -34.333  31.390  1.00112.79           C  
-ANISOU 4382  CE  LYS A 579    15852  13164  13838    412   -191   -592       C  
-ATOM   4383  NZ  LYS A 579     -14.906 -34.605  32.262  1.00113.43           N  
-ANISOU 4383  NZ  LYS A 579    15989  13310  13800    441   -243   -588       N  
-ATOM   4384  N   GLU A 580     -17.749 -34.623  27.994  1.00104.76           N  
-ANISOU 4384  N   GLU A 580    15451  11186  13167   1541    218   -885       N  
-ATOM   4385  CA  GLU A 580     -17.687 -35.850  27.205  1.00103.07           C  
-ANISOU 4385  CA  GLU A 580    15032  10913  13218   1803    136   -716       C  
-ATOM   4386  C   GLU A 580     -18.023 -35.598  25.741  1.00 98.10           C  
-ANISOU 4386  C   GLU A 580    14563   9973  12737   2071    298   -822       C  
-ATOM   4387  O   GLU A 580     -17.216 -35.878  24.856  1.00 98.54           O  
-ANISOU 4387  O   GLU A 580    14503   9963  12973   2153    303   -764       O  
-ATOM   4388  CB  GLU A 580     -18.635 -36.913  27.764  1.00107.23           C  
-ANISOU 4388  CB  GLU A 580    15450  11518  13773   1942      5   -584       C  
-ATOM   4389  CG  GLU A 580     -18.179 -37.557  29.059  1.00116.70           C  
-ANISOU 4389  CG  GLU A 580    16408  13034  14900   1730   -196   -415       C  
-ATOM   4390  CD  GLU A 580     -18.944 -38.834  29.372  1.00120.24           C  
-ANISOU 4390  CD  GLU A 580    16695  13547  15442   1909   -343   -245       C  
-ATOM   4391  OE1 GLU A 580     -19.797 -39.240  28.551  1.00120.90           O  
-ANISOU 4391  OE1 GLU A 580    16851  13431  15656   2202   -290   -254       O  
-ATOM   4392  OE2 GLU A 580     -18.688 -39.434  30.437  1.00124.04           O  
-ANISOU 4392  OE2 GLU A 580    16980  14281  15869   1755   -513   -101       O  
-ATOM   4393  N   ILE A 581     -19.221 -35.078  25.493  1.00 88.80           N  
-ANISOU 4393  N   ILE A 581    16622   6975  10142  -4701    895    547       N  
-ATOM   4394  CA  ILE A 581     -19.677 -34.813  24.134  1.00 83.06           C  
-ANISOU 4394  CA  ILE A 581    15384   6578   9596  -4770    877    537       C  
-ATOM   4395  C   ILE A 581     -18.596 -34.102  23.319  1.00 78.98           C  
-ANISOU 4395  C   ILE A 581    14440   6553   9014  -4674    573    683       C  
-ATOM   4396  O   ILE A 581     -18.423 -34.370  22.130  1.00 79.21           O  
-ANISOU 4396  O   ILE A 581    14130   6907   9059  -4606    475    657       O  
-ATOM   4397  CB  ILE A 581     -20.964 -33.958  24.123  1.00 83.13           C  
-ANISOU 4397  CB  ILE A 581    15183   6623   9778  -4888   1065    495       C  
-ATOM   4398  CG1 ILE A 581     -21.977 -34.484  25.144  1.00 84.97           C  
-ANISOU 4398  CG1 ILE A 581    15816   6489   9980  -4878   1364    320       C  
-ATOM   4399  CG2 ILE A 581     -21.571 -33.925  22.727  1.00 81.67           C  
-ANISOU 4399  CG2 ILE A 581    14533   6713   9783  -4963   1064    467       C  
-ATOM   4400  CD1 ILE A 581     -22.548 -35.846  24.811  1.00 86.05           C  
-ANISOU 4400  CD1 ILE A 581    16110   6450  10134  -4864   1539    128       C  
-ATOM   4401  N   VAL A 582     -17.870 -33.199  23.970  1.00 72.74           N  
-ANISOU 4401  N   VAL A 582    13685   5807   8147  -4680    437    829       N  
-ATOM   4402  CA  VAL A 582     -16.779 -32.478  23.328  1.00 67.77           C  
-ANISOU 4402  CA  VAL A 582    12684   5616   7448  -4593    162    958       C  
-ATOM   4403  C   VAL A 582     -15.548 -33.365  23.167  1.00 66.86           C  
-ANISOU 4403  C   VAL A 582    12625   5677   7102  -4325    -54    943       C  
-ATOM   4404  O   VAL A 582     -14.932 -33.395  22.103  1.00 66.62           O  
-ANISOU 4404  O   VAL A 582    12243   6012   7059  -4216   -217    962       O  
-ATOM   4405  CB  VAL A 582     -16.406 -31.209  24.118  1.00 65.63           C  
-ANISOU 4405  CB  VAL A 582    12444   5330   7164  -4709    109   1108       C  
-ATOM   4406  CG1 VAL A 582     -15.077 -30.646  23.633  1.00 64.75           C  
-ANISOU 4406  CG1 VAL A 582    12028   5643   6930  -4585   -183   1215       C  
-ATOM   4407  CG2 VAL A 582     -17.511 -30.175  24.003  1.00 62.85           C  
-ANISOU 4407  CG2 VAL A 582    11913   4921   7047  -4935    309   1146       C  
-ATOM   4408  N   ASN A 583     -15.191 -34.079  24.229  1.00 72.37           N  
-ANISOU 4408  N   ASN A 583    13773   6103   7621  -4215    -47    914       N  
-ATOM   4409  CA  ASN A 583     -14.095 -35.037  24.173  1.00 71.12           C  
-ANISOU 4409  CA  ASN A 583    13710   6064   7249  -3942   -220    906       C  
-ATOM   4410  C   ASN A 583     -14.262 -35.993  22.994  1.00 69.03           C  
-ANISOU 4410  C   ASN A 583    13260   5950   7019  -3841   -168    798       C  
-ATOM   4411  O   ASN A 583     -13.304 -36.297  22.277  1.00 69.37           O  
-ANISOU 4411  O   ASN A 583    13087   6292   6977  -3661   -348    834       O  
-ATOM   4412  CB  ASN A 583     -14.030 -35.835  25.477  1.00 74.83           C  
-ANISOU 4412  CB  ASN A 583    14749   6141   7542  -3851   -143    864       C  
-ATOM   4413  CG  ASN A 583     -12.837 -36.770  25.532  1.00 77.53           C  
-ANISOU 4413  CG  ASN A 583    15201   6600   7656  -3549   -327    887       C  
-ATOM   4414  OD1 ASN A 583     -11.746 -36.432  25.071  1.00 78.73           O  
-ANISOU 4414  OD1 ASN A 583    15053   7110   7749  -3426   -586    992       O  
-ATOM   4415  ND2 ASN A 583     -13.040 -37.954  26.097  1.00 78.67           N  
-ANISOU 4415  ND2 ASN A 583    15777   6434   7679  -3422   -178    790       N  
-ATOM   4416  N   ILE A 584     -15.493 -36.459  22.805  1.00 57.52           N  
-ANISOU 4416  N   ILE A 584    11894   4272   5690  -3971     93    663       N  
-ATOM   4417  CA  ILE A 584     -15.815 -37.408  21.751  1.00 56.20           C  
-ANISOU 4417  CA  ILE A 584    11599   4206   5549  -3922    185    539       C  
-ATOM   4418  C   ILE A 584     -15.724 -36.763  20.378  1.00 55.80           C  
-ANISOU 4418  C   ILE A 584    11010   4571   5621  -3982     57    589       C  
-ATOM   4419  O   ILE A 584     -15.358 -37.421  19.400  1.00 57.09           O  
-ANISOU 4419  O   ILE A 584    11008   4945   5738  -3877     12    545       O  
-ATOM   4420  CB  ILE A 584     -17.233 -37.992  21.939  1.00 53.75           C  
-ANISOU 4420  CB  ILE A 584    11514   3551   5356  -4081    507    368       C  
-ATOM   4421  CG1 ILE A 584     -17.273 -38.922  23.151  1.00 54.23           C  
-ANISOU 4421  CG1 ILE A 584    12152   3188   5265  -3981    666    283       C  
-ATOM   4422  CG2 ILE A 584     -17.685 -38.736  20.692  1.00 52.27           C  
-ANISOU 4422  CG2 ILE A 584    11109   3528   5224  -4101    597    244       C  
-ATOM   4423  CD1 ILE A 584     -18.636 -39.513  23.409  1.00 53.02           C  
-ANISOU 4423  CD1 ILE A 584    12251   2664   5229  -4137   1005     96       C  
-ATOM   4424  N   SER A 585     -16.048 -35.476  20.308  1.00 70.90           N  
-ANISOU 4424  N   SER A 585    12667   6586   7684  -4151     14    684       N  
-ATOM   4425  CA  SER A 585     -16.040 -34.756  19.038  1.00 69.62           C  
-ANISOU 4425  CA  SER A 585    12009   6801   7644  -4215    -94    737       C  
-ATOM   4426  C   SER A 585     -14.628 -34.511  18.508  1.00 69.85           C  
-ANISOU 4426  C   SER A 585    11805   7179   7554  -4036   -360    836       C  
-ATOM   4427  O   SER A 585     -14.424 -34.420  17.295  1.00 68.42           O  
-ANISOU 4427  O   SER A 585    11281   7298   7416  -4019   -443    838       O  
-ATOM   4428  CB  SER A 585     -16.785 -33.425  19.166  1.00 67.12           C  
-ANISOU 4428  CB  SER A 585    11505   6478   7521  -4433    -36    824       C  
-ATOM   4429  OG  SER A 585     -18.135 -33.632  19.547  1.00 67.45           O  
-ANISOU 4429  OG  SER A 585    11713   6204   7710  -4605    221    734       O  
-ATOM   4430  N   SER A 586     -13.658 -34.408  19.411  1.00 70.48           N  
-ANISOU 4430  N   SER A 586    12076   7216   7488  -3908   -492    913       N  
-ATOM   4431  CA  SER A 586     -12.284 -34.151  19.003  1.00 71.43           C  
-ANISOU 4431  CA  SER A 586    11975   7655   7510  -3739   -744   1005       C  
-ATOM   4432  C   SER A 586     -11.797 -35.231  18.040  1.00 72.05           C  
-ANISOU 4432  C   SER A 586    11970   7881   7524  -3566   -776    940       C  
-ATOM   4433  O   SER A 586     -10.850 -35.022  17.279  1.00 71.97           O  
-ANISOU 4433  O   SER A 586    11681   8170   7494  -3455   -947    995       O  
-ATOM   4434  CB  SER A 586     -11.364 -34.080  20.222  1.00 73.79           C  
-ANISOU 4434  CB  SER A 586    12538   7855   7644  -3622   -878   1085       C  
-ATOM   4435  OG  SER A 586     -10.761 -35.340  20.473  1.00 77.61           O  
-ANISOU 4435  OG  SER A 586    13273   8248   7966  -3395   -906   1046       O  
-ATOM   4436  N   GLY A 587     -12.457 -36.383  18.078  1.00 58.16           N  
-ANISOU 4436  N   GLY A 587    10467   5895   5737  -3552   -585    817       N  
-ATOM   4437  CA  GLY A 587     -12.093 -37.513  17.245  1.00 59.49           C  
-ANISOU 4437  CA  GLY A 587    10621   6150   5832  -3408   -556    747       C  
-ATOM   4438  C   GLY A 587     -12.770 -37.475  15.891  1.00 59.47           C  
-ANISOU 4438  C   GLY A 587    10312   6329   5955  -3550   -485    678       C  
-ATOM   4439  O   GLY A 587     -12.665 -38.415  15.101  1.00 61.39           O  
-ANISOU 4439  O   GLY A 587    10550   6628   6149  -3486   -417    603       O  
-ATOM   4440  N   TYR A 588     -13.483 -36.387  15.629  1.00 57.95           N  
-ANISOU 4440  N   TYR A 588     9874   6223   5920  -3750   -491    710       N  
-ATOM   4441  CA  TYR A 588     -14.030 -36.141  14.304  1.00 57.75           C  
-ANISOU 4441  CA  TYR A 588     9508   6423   6012  -3881   -477    676       C  
-ATOM   4442  C   TYR A 588     -13.243 -35.025  13.619  1.00 54.56           C  
-ANISOU 4442  C   TYR A 588     8726   6355   5650  -3856   -687    797       C  
-ATOM   4443  O   TYR A 588     -13.603 -34.582  12.530  1.00 53.16           O  
-ANISOU 4443  O   TYR A 588     8241   6389   5567  -3960   -707    796       O  
-ATOM   4444  CB  TYR A 588     -15.506 -35.750  14.386  1.00 61.42           C  
-ANISOU 4444  CB  TYR A 588     9945   6752   6641  -4122   -312    624       C  
-ATOM   4445  CG  TYR A 588     -16.436 -36.859  14.821  1.00 67.63           C  
-ANISOU 4445  CG  TYR A 588    11057   7225   7416  -4182    -73    469       C  
-ATOM   4446  CD1 TYR A 588     -16.904 -37.797  13.912  1.00 69.98           C  
-ANISOU 4446  CD1 TYR A 588    11324   7567   7698  -4231     38    339       C  
-ATOM   4447  CD2 TYR A 588     -16.863 -36.955  16.140  1.00 71.26           C  
-ANISOU 4447  CD2 TYR A 588    11869   7333   7874  -4207     59    445       C  
-ATOM   4448  CE1 TYR A 588     -17.764 -38.809  14.306  1.00 74.19           C  
-ANISOU 4448  CE1 TYR A 588    12159   7812   8217  -4297    282    179       C  
-ATOM   4449  CE2 TYR A 588     -17.723 -37.963  16.546  1.00 74.57           C  
-ANISOU 4449  CE2 TYR A 588    12602   7445   8287  -4262    303    287       C  
-ATOM   4450  CZ  TYR A 588     -18.170 -38.888  15.625  1.00 75.70           C  
-ANISOU 4450  CZ  TYR A 588    12696   7648   8417  -4306    417    150       C  
-ATOM   4451  OH  TYR A 588     -19.027 -39.891  16.022  1.00 78.13           O  
-ANISOU 4451  OH  TYR A 588    13318   7651   8715  -4372    682    -25       O  
-ATOM   4452  N   VAL A 589     -12.170 -34.569  14.259  1.00 56.19           N  
-ANISOU 4452  N   VAL A 589     8959   6609   5781  -3722   -841    896       N  
-ATOM   4453  CA  VAL A 589     -11.405 -33.440  13.739  1.00 53.44           C  
-ANISOU 4453  CA  VAL A 589     8274   6557   5473  -3706  -1019    999       C  
-ATOM   4454  C   VAL A 589     -10.822 -33.735  12.353  1.00 54.26           C  
-ANISOU 4454  C   VAL A 589     8122   6923   5571  -3626  -1096    977       C  
-ATOM   4455  O   VAL A 589     -10.901 -32.905  11.449  1.00 52.50           O  
-ANISOU 4455  O   VAL A 589     7586   6925   5438  -3707  -1147   1008       O  
-ATOM   4456  CB  VAL A 589     -10.291 -32.987  14.713  1.00 52.01           C  
-ANISOU 4456  CB  VAL A 589     8180   6386   5197  -3580  -1174   1094       C  
-ATOM   4457  CG1 VAL A 589      -9.256 -32.153  13.981  1.00 50.22           C  
-ANISOU 4457  CG1 VAL A 589     7608   6486   4987  -3514  -1352   1165       C  
-ATOM   4458  CG2 VAL A 589     -10.883 -32.197  15.858  1.00 48.80           C  
-ANISOU 4458  CG2 VAL A 589     7928   5789   4826  -3725  -1110   1143       C  
-ATOM   4459  N   GLU A 590     -10.253 -34.926  12.188  1.00 61.63           N  
-ANISOU 4459  N   GLU A 590     9208   7810   6398  -3468  -1083    927       N  
-ATOM   4460  CA  GLU A 590      -9.705 -35.345  10.904  1.00 64.02           C  
-ANISOU 4460  CA  GLU A 590     9322   8311   6690  -3399  -1118    901       C  
-ATOM   4461  C   GLU A 590     -10.778 -35.288   9.819  1.00 64.56           C  
-ANISOU 4461  C   GLU A 590     9224   8458   6846  -3596  -1019    831       C  
-ATOM   4462  O   GLU A 590     -10.575 -34.667   8.779  1.00 63.75           O  
-ANISOU 4462  O   GLU A 590     8830   8592   6801  -3637  -1100    856       O  
-ATOM   4463  CB  GLU A 590      -9.100 -36.748  11.016  1.00 66.91           C  
-ANISOU 4463  CB  GLU A 590     9937   8554   6930  -3214  -1057    859       C  
-ATOM   4464  CG  GLU A 590      -8.218 -37.168   9.855  1.00 70.18           C  
-ANISOU 4464  CG  GLU A 590    10186   9151   7327  -3104  -1099    861       C  
-ATOM   4465  CD  GLU A 590      -9.004 -37.672   8.655  1.00 71.98           C  
-ANISOU 4465  CD  GLU A 590    10351   9418   7579  -3256   -959    762       C  
-ATOM   4466  OE1 GLU A 590     -10.245 -37.791   8.755  1.00 72.97           O  
-ANISOU 4466  OE1 GLU A 590    10559   9432   7734  -3436   -831    685       O  
-ATOM   4467  OE2 GLU A 590      -8.376 -37.952   7.608  1.00 72.57           O  
-ANISOU 4467  OE2 GLU A 590    10295   9631   7646  -3205   -974    759       O  
-ATOM   4468  N   PRO A 591     -11.929 -35.935  10.056  1.00 71.92           N  
-ANISOU 4468  N   PRO A 591    10346   9193   7789  -3722   -844    737       N  
-ATOM   4469  CA  PRO A 591     -13.023 -35.850   9.085  1.00 72.31           C  
-ANISOU 4469  CA  PRO A 591    10223   9327   7925  -3926   -764    672       C  
-ATOM   4470  C   PRO A 591     -13.392 -34.414   8.735  1.00 72.69           C  
-ANISOU 4470  C   PRO A 591     9952   9560   8108  -4048   -859    759       C  
-ATOM   4471  O   PRO A 591     -13.650 -34.124   7.568  1.00 73.45           O  
-ANISOU 4471  O   PRO A 591     9799   9859   8250  -4137   -894    754       O  
-ATOM   4472  CB  PRO A 591     -14.184 -36.522   9.818  1.00 72.23           C  
-ANISOU 4472  CB  PRO A 591    10482   9035   7929  -4040   -567    571       C  
-ATOM   4473  CG  PRO A 591     -13.522 -37.538  10.673  1.00 72.82           C  
-ANISOU 4473  CG  PRO A 591    10908   8898   7863  -3857   -506    540       C  
-ATOM   4474  CD  PRO A 591     -12.226 -36.904  11.126  1.00 72.80           C  
-ANISOU 4474  CD  PRO A 591    10846   8997   7819  -3672   -701    672       C  
-ATOM   4475  N   MET A 592     -13.422 -33.526   9.722  1.00 74.69           N  
-ANISOU 4475  N   MET A 592    10226   9737   8414  -4057   -887    842       N  
-ATOM   4476  CA  MET A 592     -13.841 -32.152   9.462  1.00 75.49           C  
-ANISOU 4476  CA  MET A 592    10048   9988   8645  -4176   -931    933       C  
-ATOM   4477  C   MET A 592     -12.745 -31.326   8.788  1.00 75.26           C  
-ANISOU 4477  C   MET A 592     9761  10235   8600  -4078  -1094   1013       C  
-ATOM   4478  O   MET A 592     -13.033 -30.377   8.063  1.00 74.11           O  
-ANISOU 4478  O   MET A 592     9342  10275   8540  -4161  -1125   1066       O  
-ATOM   4479  CB  MET A 592     -14.342 -31.474  10.741  1.00 74.79           C  
-ANISOU 4479  CB  MET A 592    10091   9699   8625  -4250   -858    993       C  
-ATOM   4480  CG  MET A 592     -13.312 -31.371  11.839  1.00 75.87           C  
-ANISOU 4480  CG  MET A 592    10424   9744   8660  -4112   -933   1046       C  
-ATOM   4481  SD  MET A 592     -14.072 -31.278  13.467  1.00 76.70           S  
-ANISOU 4481  SD  MET A 592    10870   9478   8796  -4209   -784   1057       S  
-ATOM   4482  CE  MET A 592     -15.028 -29.769  13.317  1.00 76.13           C  
-ANISOU 4482  CE  MET A 592    10533   9472   8921  -4418   -705   1157       C  
-ATOM   4483  N   GLN A 593     -11.490 -31.693   9.026  1.00 72.13           N  
-ANISOU 4483  N   GLN A 593     9451   9859   8097  -3895  -1190   1021       N  
-ATOM   4484  CA  GLN A 593     -10.371 -31.042   8.358  1.00 70.61           C  
-ANISOU 4484  CA  GLN A 593     9024   9912   7893  -3792  -1331   1073       C  
-ATOM   4485  C   GLN A 593     -10.277 -31.504   6.909  1.00 71.07           C  
-ANISOU 4485  C   GLN A 593     8932  10126   7945  -3791  -1342   1016       C  
-ATOM   4486  O   GLN A 593      -9.800 -30.771   6.043  1.00 69.91           O  
-ANISOU 4486  O   GLN A 593     8541  10192   7831  -3779  -1419   1047       O  
-ATOM   4487  CB  GLN A 593      -9.062 -31.312   9.103  1.00 72.22           C  
-ANISOU 4487  CB  GLN A 593     9353  10085   8001  -3598  -1434   1101       C  
-ATOM   4488  CG  GLN A 593      -8.845 -30.396  10.299  1.00 73.51           C  
-ANISOU 4488  CG  GLN A 593     9568  10198   8165  -3611  -1478   1182       C  
-ATOM   4489  CD  GLN A 593      -7.743 -30.885  11.227  1.00 77.20           C  
-ANISOU 4489  CD  GLN A 593    10221  10592   8518  -3432  -1580   1205       C  
-ATOM   4490  OE1 GLN A 593      -7.408 -32.072  11.244  1.00 78.45           O  
-ANISOU 4490  OE1 GLN A 593    10550  10658   8601  -3300  -1574   1162       O  
-ATOM   4491  NE2 GLN A 593      -7.175 -29.969  12.007  1.00 78.87           N  
-ANISOU 4491  NE2 GLN A 593    10404  10850   8712  -3429  -1669   1277       N  
-ATOM   4492  N   THR A 594     -10.742 -32.723   6.650  1.00 64.59           N  
-ANISOU 4492  N   THR A 594     8278   9188   7074  -3815  -1245    926       N  
-ATOM   4493  CA  THR A 594     -10.812 -33.234   5.285  1.00 65.08           C  
-ANISOU 4493  CA  THR A 594     8237   9374   7118  -3859  -1228    865       C  
-ATOM   4494  C   THR A 594     -11.995 -32.608   4.557  1.00 66.47           C  
-ANISOU 4494  C   THR A 594     8215   9659   7383  -4063  -1204    863       C  
-ATOM   4495  O   THR A 594     -11.914 -32.304   3.370  1.00 67.51           O  
-ANISOU 4495  O   THR A 594     8148   9979   7522  -4105  -1256    863       O  
-ATOM   4496  CB  THR A 594     -10.918 -34.776   5.241  1.00 63.98           C  
-ANISOU 4496  CB  THR A 594     8358   9070   6880  -3835  -1103    764       C  
-ATOM   4497  OG1 THR A 594      -9.622 -35.354   5.445  1.00 62.57           O  
-ANISOU 4497  OG1 THR A 594     8290   8861   6623  -3621  -1140    783       O  
-ATOM   4498  CG2 THR A 594     -11.458 -35.240   3.900  1.00 63.33           C  
-ANISOU 4498  CG2 THR A 594     8190   9089   6783  -3974  -1046    688       C  
-ATOM   4499  N   LEU A 595     -13.092 -32.401   5.277  1.00 74.27           N  
-ANISOU 4499  N   LEU A 595     9259  10520   8440  -4186  -1124    866       N  
-ATOM   4500  CA  LEU A 595     -14.266 -31.769   4.690  1.00 75.26           C  
-ANISOU 4500  CA  LEU A 595     9179  10744   8671  -4370  -1102    883       C  
-ATOM   4501  C   LEU A 595     -13.954 -30.324   4.318  1.00 72.77           C  
-ANISOU 4501  C   LEU A 595     8588  10635   8427  -4355  -1200    999       C  
-ATOM   4502  O   LEU A 595     -14.535 -29.769   3.388  1.00 73.27           O  
-ANISOU 4502  O   LEU A 595     8427  10866   8547  -4455  -1225   1027       O  
-ATOM   4503  CB  LEU A 595     -15.454 -31.816   5.655  1.00 79.78           C  
-ANISOU 4503  CB  LEU A 595     9874  11106   9331  -4493   -976    870       C  
-ATOM   4504  CG  LEU A 595     -16.812 -31.459   5.040  1.00 82.97           C  
-ANISOU 4504  CG  LEU A 595    10082  11588   9855  -4691   -933    872       C  
-ATOM   4505  CD1 LEU A 595     -17.220 -32.519   4.030  1.00 85.78           C  
-ANISOU 4505  CD1 LEU A 595    10449  12004  10140  -4783   -909    751       C  
-ATOM   4506  CD2 LEU A 595     -17.875 -31.313   6.109  1.00 84.66           C  
-ANISOU 4506  CD2 LEU A 595    10401  11575  10192  -4798   -798    878       C  
-ATOM   4507  N   ASN A 596     -13.031 -29.720   5.053  1.00 70.61           N  
-ANISOU 4507  N   ASN A 596     8337  10349   8141  -4231  -1250   1065       N  
-ATOM   4508  CA  ASN A 596     -12.660 -28.337   4.809  1.00 67.31           C  
-ANISOU 4508  CA  ASN A 596     7686  10110   7779  -4215  -1311   1163       C  
-ATOM   4509  C   ASN A 596     -12.145 -28.141   3.387  1.00 66.45           C  
-ANISOU 4509  C   ASN A 596     7374  10233   7642  -4180  -1393   1150       C  
-ATOM   4510  O   ASN A 596     -12.668 -27.331   2.626  1.00 64.13           O  
-ANISOU 4510  O   ASN A 596     6866  10091   7408  -4259  -1398   1198       O  
-ATOM   4511  CB  ASN A 596     -11.600 -27.899   5.814  1.00 63.45           C  
-ANISOU 4511  CB  ASN A 596     7281   9576   7253  -4090  -1354   1210       C  
-ATOM   4512  CG  ASN A 596     -11.405 -26.405   5.832  1.00 59.59           C  
-ANISOU 4512  CG  ASN A 596     6590   9226   6825  -4109  -1363   1307       C  
-ATOM   4513  OD1 ASN A 596     -12.189 -25.675   6.439  1.00 56.13           O  
-ANISOU 4513  OD1 ASN A 596     6141   8718   6469  -4217  -1272   1379       O  
-ATOM   4514  ND2 ASN A 596     -10.353 -25.937   5.169  1.00 59.55           N  
-ANISOU 4514  ND2 ASN A 596     6434   9406   6786  -4008  -1447   1309       N  
-ATOM   4515  N   ASP A 597     -11.114 -28.901   3.041  1.00 73.38           N  
-ANISOU 4515  N   ASP A 597     8332  11120   8429  -4057  -1445   1088       N  
-ATOM   4516  CA  ASP A 597     -10.531 -28.856   1.709  1.00 73.93           C  
-ANISOU 4516  CA  ASP A 597     8259  11364   8468  -4022  -1504   1061       C  
-ATOM   4517  C   ASP A 597     -11.592 -29.072   0.639  1.00 74.69           C  
-ANISOU 4517  C   ASP A 597     8269  11538   8571  -4181  -1481   1031       C  
-ATOM   4518  O   ASP A 597     -11.777 -28.232  -0.247  1.00 75.34           O  
-ANISOU 4518  O   ASP A 597     8147  11794   8685  -4227  -1520   1072       O  
-ATOM   4519  CB  ASP A 597      -9.441 -29.918   1.573  1.00 77.18           C  
-ANISOU 4519  CB  ASP A 597     8817  11712   8794  -3885  -1522    996       C  
-ATOM   4520  CG  ASP A 597      -8.374 -29.793   2.637  1.00 77.78           C  
-ANISOU 4520  CG  ASP A 597     8971  11725   8858  -3721  -1568   1029       C  
-ATOM   4521  OD1 ASP A 597      -8.237 -28.697   3.218  1.00 79.30           O  
-ANISOU 4521  OD1 ASP A 597     9063  11971   9098  -3715  -1601   1096       O  
-ATOM   4522  OD2 ASP A 597      -7.671 -30.792   2.894  1.00 79.66           O  
-ANISOU 4522  OD2 ASP A 597     9372  11860   9034  -3601  -1566    993       O  
-ATOM   4523  N   VAL A 598     -12.284 -30.202   0.730  1.00 59.81           N  
-ANISOU 4523  N   VAL A 598     6548   9527   6649  -4266  -1415    957       N  
-ATOM   4524  CA  VAL A 598     -13.320 -30.548  -0.235  1.00 59.61           C  
-ANISOU 4524  CA  VAL A 598     6456   9576   6616  -4439  -1397    914       C  
-ATOM   4525  C   VAL A 598     -14.302 -29.400  -0.458  1.00 59.27           C  
-ANISOU 4525  C   VAL A 598     6178   9663   6679  -4550  -1423   1003       C  
-ATOM   4526  O   VAL A 598     -14.679 -29.103  -1.592  1.00 59.25           O  
-ANISOU 4526  O   VAL A 598     6012   9831   6668  -4633  -1477   1014       O  
-ATOM   4527  CB  VAL A 598     -14.091 -31.799   0.194  1.00 58.75           C  
-ANISOU 4527  CB  VAL A 598     6562   9290   6472  -4537  -1290    817       C  
-ATOM   4528  CG1 VAL A 598     -15.207 -32.092  -0.788  1.00 59.42           C  
-ANISOU 4528  CG1 VAL A 598     6554   9473   6550  -4741  -1281    768       C  
-ATOM   4529  CG2 VAL A 598     -13.147 -32.983   0.292  1.00 60.91           C  
-ANISOU 4529  CG2 VAL A 598     7072   9439   6631  -4421  -1239    739       C  
-ATOM   4530  N   LEU A 599     -14.711 -28.746   0.619  1.00 68.24           N  
-ANISOU 4530  N   LEU A 599     7305  10711   7913  -4550  -1378   1075       N  
-ATOM   4531  CA  LEU A 599     -15.627 -27.624   0.488  1.00 68.04           C  
-ANISOU 4531  CA  LEU A 599     7058  10790   8005  -4641  -1372   1180       C  
-ATOM   4532  C   LEU A 599     -14.948 -26.417  -0.141  1.00 66.99           C  
-ANISOU 4532  C   LEU A 599     6726  10852   7876  -4555  -1436   1266       C  
-ATOM   4533  O   LEU A 599     -15.553 -25.712  -0.942  1.00 66.50           O  
-ANISOU 4533  O   LEU A 599     6459  10951   7858  -4619  -1462   1332       O  
-ATOM   4534  CB  LEU A 599     -16.241 -27.265   1.838  1.00 69.37           C  
-ANISOU 4534  CB  LEU A 599     7297  10777   8283  -4675  -1269   1237       C  
-ATOM   4535  CG  LEU A 599     -17.166 -28.371   2.341  1.00 70.41           C  
-ANISOU 4535  CG  LEU A 599     7605  10715   8433  -4788  -1182   1145       C  
-ATOM   4536  CD1 LEU A 599     -17.686 -28.050   3.724  1.00 71.86           C  
-ANISOU 4536  CD1 LEU A 599     7902  10676   8725  -4817  -1064   1193       C  
-ATOM   4537  CD2 LEU A 599     -18.306 -28.578   1.359  1.00 71.74           C  
-ANISOU 4537  CD2 LEU A 599     7611  11005   8642  -4950  -1197   1122       C  
-ATOM   4538  N   ALA A 600     -13.692 -26.179   0.215  1.00 65.53           N  
-ANISOU 4538  N   ALA A 600     6600  10654   7645  -4408  -1457   1263       N  
-ATOM   4539  CA  ALA A 600     -12.958 -25.063  -0.367  1.00 65.57           C  
-ANISOU 4539  CA  ALA A 600     6435  10831   7649  -4324  -1494   1319       C  
-ATOM   4540  C   ALA A 600     -12.826 -25.278  -1.864  1.00 66.35           C  
-ANISOU 4540  C   ALA A 600     6445  11083   7682  -4338  -1565   1273       C  
-ATOM   4541  O   ALA A 600     -13.269 -24.455  -2.662  1.00 65.89           O  
-ANISOU 4541  O   ALA A 600     6205  11181   7649  -4378  -1580   1337       O  
-ATOM   4542  CB  ALA A 600     -11.592 -24.927   0.269  1.00 65.67           C  
-ANISOU 4542  CB  ALA A 600     6530  10799   7621  -4173  -1510   1299       C  
-ATOM   4543  N   GLN A 601     -12.226 -26.403  -2.237  1.00 77.92           N  
-ANISOU 4543  N   GLN A 601     8055  12494   9058  -4308  -1595   1169       N  
-ATOM   4544  CA  GLN A 601     -12.034 -26.735  -3.642  1.00 79.31           C  
-ANISOU 4544  CA  GLN A 601     8197  12780   9158  -4339  -1645   1115       C  
-ATOM   4545  C   GLN A 601     -13.326 -26.649  -4.441  1.00 80.52           C  
-ANISOU 4545  C   GLN A 601     8233  13044   9317  -4507  -1672   1142       C  
-ATOM   4546  O   GLN A 601     -13.300 -26.381  -5.634  1.00 81.45           O  
-ANISOU 4546  O   GLN A 601     8261  13303   9385  -4538  -1726   1142       O  
-ATOM   4547  CB  GLN A 601     -11.439 -28.129  -3.798  1.00 83.52           C  
-ANISOU 4547  CB  GLN A 601     8938  13194   9602  -4317  -1631   1005       C  
-ATOM   4548  CG  GLN A 601     -11.169 -28.502  -5.237  1.00 88.84           C  
-ANISOU 4548  CG  GLN A 601     9612  13952  10191  -4364  -1659    948       C  
-ATOM   4549  CD  GLN A 601     -10.553 -29.869  -5.363  1.00 94.03           C  
-ANISOU 4549  CD  GLN A 601    10488  14472  10768  -4344  -1605    851       C  
-ATOM   4550  OE1 GLN A 601     -10.681 -30.699  -4.463  1.00 97.54           O  
-ANISOU 4550  OE1 GLN A 601    11087  14768  11204  -4332  -1546    821       O  
-ATOM   4551  NE2 GLN A 601      -9.871 -30.116  -6.477  1.00 96.49           N  
-ANISOU 4551  NE2 GLN A 601    10830  14815  11018  -4337  -1604    805       N  
-ATOM   4552  N   LEU A 602     -14.457 -26.893  -3.793  1.00 66.21           N  
-ANISOU 4552  N   LEU A 602     6426  11166   7566  -4618  -1635   1163       N  
-ATOM   4553  CA  LEU A 602     -15.739 -26.751  -4.468  1.00 67.24           C  
-ANISOU 4553  CA  LEU A 602     6410  11414   7723  -4778  -1670   1200       C  
-ATOM   4554  C   LEU A 602     -16.144 -25.287  -4.471  1.00 65.17           C  
-ANISOU 4554  C   LEU A 602     5919  11279   7563  -4749  -1672   1346       C  
-ATOM   4555  O   LEU A 602     -16.551 -24.743  -5.496  1.00 66.88           O  
-ANISOU 4555  O   LEU A 602     5972  11674   7765  -4792  -1737   1401       O  
-ATOM   4556  CB  LEU A 602     -16.817 -27.580  -3.779  1.00 68.06           C  
-ANISOU 4556  CB  LEU A 602     6598  11388   7874  -4913  -1612   1157       C  
-ATOM   4557  CG  LEU A 602     -18.173 -27.479  -4.476  1.00 70.68           C  
-ANISOU 4557  CG  LEU A 602     6752  11856   8246  -5089  -1658   1190       C  
-ATOM   4558  CD1 LEU A 602     -18.037 -27.913  -5.923  1.00 69.87           C  
-ANISOU 4558  CD1 LEU A 602     6634  11909   8004  -5166  -1756   1131       C  
-ATOM   4559  CD2 LEU A 602     -19.214 -28.313  -3.761  1.00 71.29           C  
-ANISOU 4559  CD2 LEU A 602     6913  11788   8386  -5227  -1580   1127       C  
-ATOM   4560  N   ASP A 603     -16.026 -24.657  -3.307  1.00 73.14           N  
-ANISOU 4560  N   ASP A 603     6935  12188   8667  -4679  -1590   1414       N  
-ATOM   4561  CA  ASP A 603     -16.334 -23.244  -3.154  1.00 71.32           C  
-ANISOU 4561  CA  ASP A 603     6556  12036   8508  -4609  -1531   1564       C  
-ATOM   4562  C   ASP A 603     -15.536 -22.407  -4.148  1.00 70.88           C  
-ANISOU 4562  C   ASP A 603     6409  12147   8375  -4494  -1567   1593       C  
-ATOM   4563  O   ASP A 603     -15.918 -21.284  -4.482  1.00 69.00           O  
-ANISOU 4563  O   ASP A 603     6043  12018   8155  -4437  -1526   1716       O  
-ATOM   4564  CB  ASP A 603     -16.010 -22.792  -1.733  1.00 69.28           C  
-ANISOU 4564  CB  ASP A 603     6391  11617   8315  -4538  -1421   1608       C  
-ATOM   4565  CG  ASP A 603     -16.397 -21.354  -1.479  1.00 68.23           C  
-ANISOU 4565  CG  ASP A 603     6158  11530   8235  -4457  -1319   1767       C  
-ATOM   4566  OD1 ASP A 603     -17.380 -20.890  -2.091  1.00 69.83           O  
-ANISOU 4566  OD1 ASP A 603     6219  11839   8475  -4489  -1318   1861       O  
-ATOM   4567  OD2 ASP A 603     -15.723 -20.690  -0.666  1.00 69.24           O  
-ANISOU 4567  OD2 ASP A 603     6349  11593   8365  -4370  -1239   1799       O  
-ATOM   4568  N   ALA A 604     -14.422 -22.964  -4.612  1.00 65.76           N  
-ANISOU 4568  N   ALA A 604     5833  11504   7650  -4460  -1630   1476       N  
-ATOM   4569  CA  ALA A 604     -13.531 -22.270  -5.534  1.00 64.90           C  
-ANISOU 4569  CA  ALA A 604     5667  11517   7474  -4353  -1649   1472       C  
-ATOM   4570  C   ALA A 604     -14.015 -22.382  -6.980  1.00 66.91           C  
-ANISOU 4570  C   ALA A 604     5845  11921   7658  -4432  -1737   1468       C  
-ATOM   4571  O   ALA A 604     -14.253 -21.370  -7.639  1.00 68.06           O  
-ANISOU 4571  O   ALA A 604     5873  12198   7789  -4382  -1725   1559       O  
-ATOM   4572  CB  ALA A 604     -12.112 -22.804  -5.400  1.00 65.56           C  
-ANISOU 4572  CB  ALA A 604     5881  11519   7509  -4258  -1661   1356       C  
-ATOM   4573  N   VAL A 605     -14.165 -23.611  -7.470  1.00 61.71           N  
-ANISOU 4573  N   VAL A 605     5287  11230   6931  -4545  -1809   1366       N  
-ATOM   4574  CA  VAL A 605     -14.630 -23.828  -8.835  1.00 64.07           C  
-ANISOU 4574  CA  VAL A 605     5544  11662   7136  -4649  -1901   1352       C  
-ATOM   4575  C   VAL A 605     -15.928 -23.071  -9.081  1.00 66.37           C  
-ANISOU 4575  C   VAL A 605     5633  12101   7483  -4720  -1936   1487       C  
-ATOM   4576  O   VAL A 605     -16.215 -22.667 -10.204  1.00 68.40           O  
-ANISOU 4576  O   VAL A 605     5799  12513   7675  -4751  -2012   1528       O  
-ATOM   4577  CB  VAL A 605     -14.865 -25.323  -9.149  1.00 64.32           C  
-ANISOU 4577  CB  VAL A 605     5740  11621   7078  -4791  -1937   1233       C  
-ATOM   4578  CG1 VAL A 605     -13.707 -26.174  -8.648  1.00 61.54           C  
-ANISOU 4578  CG1 VAL A 605     5600  11090   6693  -4703  -1871   1124       C  
-ATOM   4579  CG2 VAL A 605     -16.174 -25.797  -8.552  1.00 64.74           C  
-ANISOU 4579  CG2 VAL A 605     5751  11652   7194  -4937  -1938   1253       C  
-ATOM   4580  N   VAL A 606     -16.713 -22.884  -8.027  1.00 71.83           N  
-ANISOU 4580  N   VAL A 606     6284  12725   8285  -4725  -1866   1566       N  
-ATOM   4581  CA  VAL A 606     -17.961 -22.139  -8.135  1.00 73.96           C  
-ANISOU 4581  CA  VAL A 606     6374  13104   8622  -4755  -1867   1717       C  
-ATOM   4582  C   VAL A 606     -17.675 -20.646  -8.252  1.00 72.67           C  
-ANISOU 4582  C   VAL A 606     6105  13026   8482  -4591  -1793   1854       C  
-ATOM   4583  O   VAL A 606     -18.327 -19.938  -9.015  1.00 73.94           O  
-ANISOU 4583  O   VAL A 606     6104  13347   8641  -4594  -1834   1967       O  
-ATOM   4584  CB  VAL A 606     -18.890 -22.407  -6.937  1.00 75.50           C  
-ANISOU 4584  CB  VAL A 606     6572  13167   8948  -4816  -1790   1754       C  
-ATOM   4585  CG1 VAL A 606     -20.089 -21.473  -6.973  1.00 76.24           C  
-ANISOU 4585  CG1 VAL A 606     6463  13360   9146  -4818  -1767   1933       C  
-ATOM   4586  CG2 VAL A 606     -19.339 -23.855  -6.949  1.00 77.24           C  
-ANISOU 4586  CG2 VAL A 606     6882  13322   9143  -5000  -1849   1614       C  
-ATOM   4587  N   SER A 607     -16.690 -20.172  -7.501  1.00 73.60           N  
-ANISOU 4587  N   SER A 607     6310  13040   8616  -4455  -1683   1839       N  
-ATOM   4588  CA  SER A 607     -16.299 -18.775  -7.583  1.00 72.31           C  
-ANISOU 4588  CA  SER A 607     6072  12944   8458  -4307  -1582   1941       C  
-ATOM   4589  C   SER A 607     -15.856 -18.464  -9.006  1.00 72.20           C  
-ANISOU 4589  C   SER A 607     6004  13086   8341  -4281  -1657   1916       C  
-ATOM   4590  O   SER A 607     -16.213 -17.430  -9.568  1.00 72.38           O  
-ANISOU 4590  O   SER A 607     5895  13239   8366  -4226  -1627   2034       O  
-ATOM   4591  CB  SER A 607     -15.171 -18.479  -6.598  1.00 70.98           C  
-ANISOU 4591  CB  SER A 607     6024  12645   8299  -4191  -1469   1891       C  
-ATOM   4592  OG  SER A 607     -14.979 -17.085  -6.460  1.00 71.98           O  
-ANISOU 4592  OG  SER A 607     6088  12820   8441  -4069  -1335   1995       O  
-ATOM   4593  N   PHE A 608     -15.084 -19.376  -9.586  1.00 70.60           N  
-ANISOU 4593  N   PHE A 608     5913  12858   8053  -4324  -1747   1762       N  
-ATOM   4594  CA  PHE A 608     -14.610 -19.235 -10.960  1.00 70.79           C  
-ANISOU 4594  CA  PHE A 608     5928  12995   7975  -4323  -1823   1711       C  
-ATOM   4595  C   PHE A 608     -15.749 -19.267 -11.970  1.00 76.85           C  
-ANISOU 4595  C   PHE A 608     6573  13928   8697  -4445  -1953   1787       C  
-ATOM   4596  O   PHE A 608     -15.933 -18.328 -12.748  1.00 79.62           O  
-ANISOU 4596  O   PHE A 608     6812  14420   9021  -4394  -1963   1875       O  
-ATOM   4597  CB  PHE A 608     -13.601 -20.333 -11.284  1.00 62.14           C  
-ANISOU 4597  CB  PHE A 608     4996  11803   6812  -4365  -1880   1530       C  
-ATOM   4598  CG  PHE A 608     -12.245 -20.075 -10.724  1.00 52.49           C  
-ANISOU 4598  CG  PHE A 608     3853  10471   5618  -4221  -1778   1454       C  
-ATOM   4599  CD1 PHE A 608     -11.182 -20.904 -11.026  1.00 49.44           C  
-ANISOU 4599  CD1 PHE A 608     3634   9978   5174  -4196  -1787   1314       C  
-ATOM   4600  CD2 PHE A 608     -12.032 -18.989  -9.897  1.00 47.67           C  
-ANISOU 4600  CD2 PHE A 608     3189   9851   5072  -4088  -1644   1535       C  
-ATOM   4601  CE1 PHE A 608      -9.926 -20.650 -10.512  1.00 43.72           C  
-ANISOU 4601  CE1 PHE A 608     2958   9167   4488  -4058  -1703   1248       C  
-ATOM   4602  CE2 PHE A 608     -10.781 -18.730  -9.376  1.00 43.01           C  
-ANISOU 4602  CE2 PHE A 608     2660   9181   4502  -3969  -1560   1459       C  
-ATOM   4603  CZ  PHE A 608      -9.726 -19.560  -9.683  1.00 42.06           C  
-ANISOU 4603  CZ  PHE A 608     2642   8982   4357  -3963  -1608   1313       C  
-ATOM   4604  N   ALA A 609     -16.505 -20.359 -11.955  1.00 82.37           N  
-ANISOU 4604  N   ALA A 609     7294  14616   9387  -4612  -2055   1747       N  
-ATOM   4605  CA  ALA A 609     -17.632 -20.529 -12.858  1.00 87.32           C  
-ANISOU 4605  CA  ALA A 609     7801  15410   9967  -4759  -2201   1806       C  
-ATOM   4606  C   ALA A 609     -18.575 -19.333 -12.788  1.00 89.02           C  
-ANISOU 4606  C   ALA A 609     7794  15758  10272  -4691  -2173   2011       C  
-ATOM   4607  O   ALA A 609     -19.198 -18.966 -13.783  1.00 91.90           O  
-ANISOU 4607  O   ALA A 609     8023  16309  10586  -4739  -2292   2093       O  
-ATOM   4608  CB  ALA A 609     -18.376 -21.816 -12.534  1.00 90.20           C  
-ANISOU 4608  CB  ALA A 609     8211  15722  10337  -4948  -2267   1732       C  
-ATOM   4609  N   HIS A 610     -18.673 -18.727 -11.610  1.00 85.57           N  
-ANISOU 4609  N   HIS A 610     7325  15222   9966  -4584  -2015   2098       N  
-ATOM   4610  CA  HIS A 610     -19.522 -17.558 -11.421  1.00 87.71           C  
-ANISOU 4610  CA  HIS A 610     7397  15586  10341  -4511  -1944   2303       C  
-ATOM   4611  C   HIS A 610     -18.938 -16.340 -12.116  1.00 87.38           C  
-ANISOU 4611  C   HIS A 610     7297  15653  10250  -4365  -1884   2372       C  
-ATOM   4612  O   HIS A 610     -19.580 -15.739 -12.976  1.00 88.44           O  
-ANISOU 4612  O   HIS A 610     7260  15972  10371  -4366  -1958   2495       O  
-ATOM   4613  CB  HIS A 610     -19.697 -17.259  -9.933  1.00 86.67           C  
-ANISOU 4613  CB  HIS A 610     7296  15283  10351  -4448  -1767   2364       C  
-ATOM   4614  CG  HIS A 610     -20.288 -15.912  -9.650  1.00 87.09           C  
-ANISOU 4614  CG  HIS A 610     7190  15390  10512  -4341  -1632   2573       C  
-ATOM   4615  ND1 HIS A 610     -21.423 -15.448 -10.281  1.00 89.96           N  
-ANISOU 4615  ND1 HIS A 610     7322  15926  10933  -4377  -1699   2739       N  
-ATOM   4616  CD2 HIS A 610     -19.903 -14.932  -8.800  1.00 86.57           C  
-ANISOU 4616  CD2 HIS A 610     7166  15225  10503  -4203  -1428   2647       C  
-ATOM   4617  CE1 HIS A 610     -21.710 -14.239  -9.832  1.00 90.63           C  
-ANISOU 4617  CE1 HIS A 610     7311  16008  11117  -4254  -1525   2915       C  
-ATOM   4618  NE2 HIS A 610     -20.803 -13.902  -8.932  1.00 88.53           N  
-ANISOU 4618  NE2 HIS A 610     7222  15571  10843  -4152  -1352   2857       N  
-ATOM   4619  N   VAL A 611     -17.720 -15.977 -11.732  1.00 92.81           N  
-ANISOU 4619  N   VAL A 611     8122  16230  10913  -4240  -1750   2290       N  
-ATOM   4620  CA  VAL A 611     -17.068 -14.801 -12.291  1.00 93.26           C  
-ANISOU 4620  CA  VAL A 611     8143  16365  10928  -4098  -1650   2328       C  
-ATOM   4621  C   VAL A 611     -17.083 -14.845 -13.814  1.00 93.67           C  
-ANISOU 4621  C   VAL A 611     8147  16582  10861  -4143  -1812   2303       C  
-ATOM   4622  O   VAL A 611     -17.357 -13.836 -14.466  1.00 94.32           O  
-ANISOU 4622  O   VAL A 611     8133  16793  10913  -4049  -1773   2426       O  
-ATOM   4623  CB  VAL A 611     -15.627 -14.652 -11.784  1.00 92.70           C  
-ANISOU 4623  CB  VAL A 611     8241  16152  10830  -3989  -1513   2191       C  
-ATOM   4624  CG1 VAL A 611     -15.009 -13.389 -12.340  1.00 93.83           C  
-ANISOU 4624  CG1 VAL A 611     8343  16372  10938  -3851  -1379   2219       C  
-ATOM   4625  CG2 VAL A 611     -15.610 -14.611 -10.274  1.00 94.37           C  
-ANISOU 4625  CG2 VAL A 611     8518  16206  11133  -3953  -1379   2216       C  
-ATOM   4626  N   SER A 612     -16.797 -16.016 -14.376  1.00 73.14           N  
-ANISOU 4626  N   SER A 612     5691  13945   8153  -4255  -1964   2152       N  
-ATOM   4627  CA  SER A 612     -16.896 -16.210 -15.816  1.00 76.77           C  
-ANISOU 4627  CA  SER A 612     6202  14519   8449  -4303  -2113   2129       C  
-ATOM   4628  C   SER A 612     -18.284 -15.812 -16.298  1.00 82.09           C  
-ANISOU 4628  C   SER A 612     6664  15394   9133  -4355  -2231   2316       C  
-ATOM   4629  O   SER A 612     -18.468 -14.752 -16.888  1.00 84.73           O  
-ANISOU 4629  O   SER A 612     6909  15848   9436  -4238  -2197   2443       O  
-ATOM   4630  CB  SER A 612     -16.616 -17.665 -16.188  1.00 75.82           C  
-ANISOU 4630  CB  SER A 612     6263  14317   8229  -4464  -2243   1957       C  
-ATOM   4631  OG  SER A 612     -15.274 -18.016 -15.916  1.00 70.58           O  
-ANISOU 4631  OG  SER A 612     5792  13476   7551  -4397  -2141   1796       O  
-ATOM   4632  N   ASN A 613     -19.257 -16.672 -16.031  1.00 96.03           N  
-ANISOU 4632  N   ASN A 613     8346  17193  10947  -4527  -2361   2331       N  
-ATOM   4633  CA  ASN A 613     -20.637 -16.442 -16.432  1.00102.51           C  
-ANISOU 4633  CA  ASN A 613     8939  18212  11799  -4600  -2495   2501       C  
-ATOM   4634  C   ASN A 613     -21.058 -14.975 -16.379  1.00103.27           C  
-ANISOU 4634  C   ASN A 613     8837  18416  11985  -4425  -2382   2723       C  
-ATOM   4635  O   ASN A 613     -21.752 -14.492 -17.271  1.00105.48           O  
-ANISOU 4635  O   ASN A 613     8984  18887  12205  -4410  -2497   2861       O  
-ATOM   4636  CB  ASN A 613     -21.575 -17.288 -15.565  1.00106.89           C  
-ANISOU 4636  CB  ASN A 613     9393  18731  12491  -4764  -2541   2500       C  
-ATOM   4637  CG  ASN A 613     -22.974 -17.396 -16.144  1.00114.52           C  
-ANISOU 4637  CG  ASN A 613    10137  19907  13469  -4894  -2729   2627       C  
-ATOM   4638  OD1 ASN A 613     -23.237 -18.237 -17.004  1.00118.23           O  
-ANISOU 4638  OD1 ASN A 613    10662  20468  13792  -5062  -2920   2542       O  
-ATOM   4639  ND2 ASN A 613     -23.884 -16.552 -15.666  1.00116.72           N  
-ANISOU 4639  ND2 ASN A 613    10160  20262  13926  -4827  -2669   2833       N  
-ATOM   4640  N   GLY A 614     -20.625 -14.268 -15.341  1.00 88.62           N  
-ANISOU 4640  N   GLY A 614     6971  16437  10263  -4296  -2150   2760       N  
-ATOM   4641  CA  GLY A 614     -21.098 -12.918 -15.093  1.00 90.01           C  
-ANISOU 4641  CA  GLY A 614     6963  16687  10549  -4147  -1990   2979       C  
-ATOM   4642  C   GLY A 614     -20.098 -11.825 -15.409  1.00 87.94           C  
-ANISOU 4642  C   GLY A 614     6800  16407  10208  -3950  -1804   2978       C  
-ATOM   4643  O   GLY A 614     -19.880 -10.915 -14.606  1.00 87.34           O  
-ANISOU 4643  O   GLY A 614     6686  16261  10239  -3836  -1560   3057       O  
-ATOM   4644  N   ALA A 615     -19.494 -11.911 -16.588  1.00109.58           N  
-ANISOU 4644  N   ALA A 615     9680  19199  12756  -3920  -1902   2881       N  
-ATOM   4645  CA  ALA A 615     -18.532 -10.914 -17.041  1.00107.81           C  
-ANISOU 4645  CA  ALA A 615     9570  18952  12441  -3737  -1725   2854       C  
-ATOM   4646  C   ALA A 615     -19.096 -10.174 -18.246  1.00108.65           C  
-ANISOU 4646  C   ALA A 615     9602  19245  12434  -3649  -1795   3004       C  
-ATOM   4647  O   ALA A 615     -20.036 -10.659 -18.877  1.00111.34           O  
-ANISOU 4647  O   ALA A 615     9843  19732  12731  -3757  -2033   3083       O  
-ATOM   4648  CB  ALA A 615     -17.222 -11.585 -17.406  1.00104.49           C  
-ANISOU 4648  CB  ALA A 615     9409  18394  11897  -3759  -1745   2600       C  
-ATOM   4649  N   PRO A 616     -18.531  -8.996 -18.567  1.00 87.18           N  
-ANISOU 4649  N   PRO A 616     6938  16526   9662  -3455  -1584   3043       N  
-ATOM   4650  CA  PRO A 616     -18.936  -8.262 -19.770  1.00 87.47           C  
-ANISOU 4650  CA  PRO A 616     6949  16723   9564  -3345  -1633   3175       C  
-ATOM   4651  C   PRO A 616     -19.274  -9.229 -20.892  1.00 89.29           C  
-ANISOU 4651  C   PRO A 616     7246  17047   9633  -3494  -1962   3115       C  
-ATOM   4652  O   PRO A 616     -20.355  -9.152 -21.474  1.00 89.99           O  
-ANISOU 4652  O   PRO A 616     7175  17327   9690  -3521  -2144   3291       O  
-ATOM   4653  CB  PRO A 616     -17.685  -7.463 -20.110  1.00 89.34           C  
-ANISOU 4653  CB  PRO A 616     7394  16851   9702  -3177  -1392   3051       C  
-ATOM   4654  CG  PRO A 616     -17.088  -7.156 -18.768  1.00 89.34           C  
-ANISOU 4654  CG  PRO A 616     7383  16705   9857  -3145  -1132   2997       C  
-ATOM   4655  CD  PRO A 616     -17.451  -8.301 -17.843  1.00 84.87           C  
-ANISOU 4655  CD  PRO A 616     6747  16083   9418  -3333  -1282   2953       C  
-ATOM   4656  N   VAL A 617     -18.348 -10.136 -21.185  1.00 89.04           N  
-ANISOU 4656  N   VAL A 617     7450  16881   9502  -3595  -2032   2874       N  
-ATOM   4657  CA  VAL A 617     -18.641 -11.279 -22.040  1.00 92.50           C  
-ANISOU 4657  CA  VAL A 617     7974  17370   9800  -3794  -2323   2790       C  
-ATOM   4658  C   VAL A 617     -18.124 -12.543 -21.358  1.00 93.50           C  
-ANISOU 4658  C   VAL A 617     8210  17333   9984  -3960  -2357   2590       C  
-ATOM   4659  O   VAL A 617     -17.017 -12.557 -20.816  1.00 93.75           O  
-ANISOU 4659  O   VAL A 617     8379  17181  10060  -3895  -2179   2442       O  
-ATOM   4660  CB  VAL A 617     -18.038 -11.134 -23.458  1.00 93.82           C  
-ANISOU 4660  CB  VAL A 617     8381  17530   9735  -3757  -2376   2704       C  
-ATOM   4661  CG1 VAL A 617     -17.681  -9.683 -23.742  1.00 90.79           C  
-ANISOU 4661  CG1 VAL A 617     8016  17158   9323  -3501  -2148   2793       C  
-ATOM   4662  CG2 VAL A 617     -16.824 -12.035 -23.632  1.00 93.33           C  
-ANISOU 4662  CG2 VAL A 617     8605  17252   9603  -3849  -2352   2434       C  
-ATOM   4663  N   PRO A 618     -18.943 -13.603 -21.354  1.00103.35           N  
-ANISOU 4663  N   PRO A 618     9388  18650  11230  -4171  -2577   2590       N  
-ATOM   4664  CA  PRO A 618     -18.590 -14.863 -20.692  1.00101.53           C  
-ANISOU 4664  CA  PRO A 618     9259  18270  11048  -4332  -2601   2415       C  
-ATOM   4665  C   PRO A 618     -17.206 -15.357 -21.089  1.00 97.37           C  
-ANISOU 4665  C   PRO A 618     9032  17551  10414  -4329  -2529   2192       C  
-ATOM   4666  O   PRO A 618     -16.898 -15.433 -22.275  1.00 99.24           O  
-ANISOU 4666  O   PRO A 618     9436  17798  10473  -4359  -2605   2134       O  
-ATOM   4667  CB  PRO A 618     -19.660 -15.829 -21.202  1.00102.24           C  
-ANISOU 4667  CB  PRO A 618     9282  18499  11064  -4567  -2864   2437       C  
-ATOM   4668  CG  PRO A 618     -20.838 -14.961 -21.461  1.00104.20           C  
-ANISOU 4668  CG  PRO A 618     9263  18977  11350  -4509  -2951   2679       C  
-ATOM   4669  CD  PRO A 618     -20.285 -13.651 -21.958  1.00106.64           C  
-ANISOU 4669  CD  PRO A 618     9615  19301  11604  -4270  -2807   2759       C  
-ATOM   4670  N   TYR A 619     -16.385 -15.690 -20.100  1.00101.42           N  
-ANISOU 4670  N   TYR A 619     9615  17882  11037  -4296  -2383   2072       N  
-ATOM   4671  CA  TYR A 619     -15.052 -16.211 -20.368  1.00 94.50           C  
-ANISOU 4671  CA  TYR A 619     8997  16812  10095  -4287  -2304   1866       C  
-ATOM   4672  C   TYR A 619     -15.107 -17.498 -21.190  1.00 93.92           C  
-ANISOU 4672  C   TYR A 619     9101  16706   9877  -4502  -2467   1751       C  
-ATOM   4673  O   TYR A 619     -16.158 -18.123 -21.321  1.00 94.31           O  
-ANISOU 4673  O   TYR A 619     9066  16875   9892  -4676  -2638   1808       O  
-ATOM   4674  CB  TYR A 619     -14.289 -16.448 -19.063  1.00 90.66           C  
-ANISOU 4674  CB  TYR A 619     8523  16162   9763  -4226  -2152   1779       C  
-ATOM   4675  CG  TYR A 619     -14.007 -15.193 -18.269  1.00 85.05           C  
-ANISOU 4675  CG  TYR A 619     7689  15453   9174  -4033  -1956   1859       C  
-ATOM   4676  CD1 TYR A 619     -13.158 -15.220 -17.169  1.00 82.27           C  
-ANISOU 4676  CD1 TYR A 619     7365  14959   8936  -3963  -1809   1776       C  
-ATOM   4677  CD2 TYR A 619     -14.591 -13.982 -18.612  1.00 83.92           C  
-ANISOU 4677  CD2 TYR A 619     7409  15455   9022  -3925  -1908   2023       C  
-ATOM   4678  CE1 TYR A 619     -12.897 -14.074 -16.437  1.00 79.20           C  
-ANISOU 4678  CE1 TYR A 619     6878  14573   8643  -3814  -1618   1842       C  
-ATOM   4679  CE2 TYR A 619     -14.333 -12.833 -17.888  1.00 80.73           C  
-ANISOU 4679  CE2 TYR A 619     6911  15044   8720  -3763  -1692   2095       C  
-ATOM   4680  CZ  TYR A 619     -13.490 -12.885 -16.802  1.00 78.14           C  
-ANISOU 4680  CZ  TYR A 619     6620  14574   8497  -3720  -1546   1999       C  
-ATOM   4681  OH  TYR A 619     -13.240 -11.741 -16.082  1.00 75.04           O  
-ANISOU 4681  OH  TYR A 619     6147  14177   8189  -3586  -1321   2065       O  
-ATOM   4682  N   VAL A 620     -13.963 -17.889 -21.736  1.00 74.92           N  
-ANISOU 4682  N   VAL A 620     6944  14129   7392  -4497  -2396   1586       N  
-ATOM   4683  CA  VAL A 620     -13.882 -19.046 -22.614  1.00 74.27           C  
-ANISOU 4683  CA  VAL A 620     7076  13984   7159  -4702  -2503   1473       C  
-ATOM   4684  C   VAL A 620     -12.853 -20.044 -22.102  1.00 71.57           C  
-ANISOU 4684  C   VAL A 620     6909  13411   6874  -4731  -2390   1303       C  
-ATOM   4685  O   VAL A 620     -11.810 -19.657 -21.586  1.00 71.00           O  
-ANISOU 4685  O   VAL A 620     6868  13203   6905  -4562  -2225   1238       O  
-ATOM   4686  CB  VAL A 620     -13.510 -18.614 -24.049  1.00 75.24           C  
-ANISOU 4686  CB  VAL A 620     7385  14098   7104  -4691  -2519   1443       C  
-ATOM   4687  CG1 VAL A 620     -12.864 -19.757 -24.819  1.00 77.66           C  
-ANISOU 4687  CG1 VAL A 620     7992  14228   7286  -4864  -2522   1277       C  
-ATOM   4688  CG2 VAL A 620     -14.740 -18.087 -24.772  1.00 77.10           C  
-ANISOU 4688  CG2 VAL A 620     7485  14582   7226  -4744  -2707   1610       C  
-ATOM   4689  N   ARG A 621     -13.149 -21.331 -22.243  1.00 75.50           N  
-ANISOU 4689  N   ARG A 621     7517  13868   7302  -4945  -2470   1234       N  
-ATOM   4690  CA  ARG A 621     -12.216 -22.371 -21.820  1.00 72.29           C  
-ANISOU 4690  CA  ARG A 621     7290  13238   6938  -4974  -2354   1086       C  
-ATOM   4691  C   ARG A 621     -10.938 -22.383 -22.649  1.00 70.44           C  
-ANISOU 4691  C   ARG A 621     7303  12811   6649  -4919  -2230    962       C  
-ATOM   4692  O   ARG A 621     -10.941 -22.814 -23.799  1.00 70.38           O  
-ANISOU 4692  O   ARG A 621     7494  12766   6481  -5070  -2272    912       O  
-ATOM   4693  CB  ARG A 621     -12.863 -23.751 -21.893  1.00 73.32           C  
-ANISOU 4693  CB  ARG A 621     7510  13364   6986  -5229  -2438   1039       C  
-ATOM   4694  CG  ARG A 621     -11.882 -24.871 -21.633  1.00 71.38           C  
-ANISOU 4694  CG  ARG A 621     7485  12876   6759  -5260  -2297    895       C  
-ATOM   4695  CD  ARG A 621     -12.576 -26.211 -21.579  1.00 74.70           C  
-ANISOU 4695  CD  ARG A 621     7991  13292   7099  -5507  -2342    849       C  
-ATOM   4696  NE  ARG A 621     -11.695 -27.241 -21.042  1.00 75.98           N  
-ANISOU 4696  NE  ARG A 621     8331  13225   7313  -5494  -2182    738       N  
-ATOM   4697  CZ  ARG A 621     -12.094 -28.462 -20.701  1.00 78.01           C  
-ANISOU 4697  CZ  ARG A 621     8680  13428   7531  -5661  -2153    682       C  
-ATOM   4698  NH1 ARG A 621     -13.367 -28.811 -20.839  1.00 79.62           N  
-ANISOU 4698  NH1 ARG A 621     8808  13796   7649  -5870  -2280    712       N  
-ATOM   4699  NH2 ARG A 621     -11.219 -29.333 -20.218  1.00 79.74           N  
-ANISOU 4699  NH2 ARG A 621     9065  13432   7801  -5615  -1990    597       N  
-ATOM   4700  N   PRO A 622      -9.829 -21.931 -22.057  1.00 74.20           N  
-ANISOU 4700  N   PRO A 622     7777  13154   7263  -4715  -2070    907       N  
-ATOM   4701  CA  PRO A 622      -8.558 -21.951 -22.781  1.00 72.25           C  
-ANISOU 4701  CA  PRO A 622     7752  12701   6998  -4655  -1930    778       C  
-ATOM   4702  C   PRO A 622      -8.124 -23.374 -23.102  1.00 71.57           C  
-ANISOU 4702  C   PRO A 622     7905  12427   6862  -4819  -1888    668       C  
-ATOM   4703  O   PRO A 622      -8.013 -24.193 -22.189  1.00 71.59           O  
-ANISOU 4703  O   PRO A 622     7886  12366   6950  -4832  -1857    646       O  
-ATOM   4704  CB  PRO A 622      -7.578 -21.339 -21.776  1.00 70.93           C  
-ANISOU 4704  CB  PRO A 622     7478  12456   7017  -4423  -1784    745       C  
-ATOM   4705  CG  PRO A 622      -8.186 -21.603 -20.444  1.00 70.35           C  
-ANISOU 4705  CG  PRO A 622     7214  12471   7043  -4420  -1839    821       C  
-ATOM   4706  CD  PRO A 622      -9.667 -21.470 -20.668  1.00 72.99           C  
-ANISOU 4706  CD  PRO A 622     7426  13018   7287  -4551  -2005    950       C  
-ATOM   4707  N   ALA A 623      -7.885 -23.669 -24.375  1.00 55.80           N  
-ANISOU 4707  N   ALA A 623     6150  10329   4722  -4943  -1869    602       N  
-ATOM   4708  CA  ALA A 623      -7.282 -24.946 -24.730  1.00 57.30           C  
-ANISOU 4708  CA  ALA A 623     6600  10296   4877  -5085  -1768    493       C  
-ATOM   4709  C   ALA A 623      -5.849 -24.917 -24.234  1.00 55.51           C  
-ANISOU 4709  C   ALA A 623     6412   9849   4831  -4886  -1571    403       C  
-ATOM   4710  O   ALA A 623      -5.194 -23.888 -24.304  1.00 55.10           O  
-ANISOU 4710  O   ALA A 623     6304   9773   4857  -4702  -1500    382       O  
-ATOM   4711  CB  ALA A 623      -7.331 -25.170 -26.221  1.00 58.04           C  
-ANISOU 4711  CB  ALA A 623     6962  10316   4776  -5271  -1776    447       C  
-ATOM   4712  N   ILE A 624      -5.363 -26.037 -23.714  1.00 77.40           N  
-ANISOU 4712  N   ILE A 624     9272  12466   7671  -4920  -1478    350       N  
-ATOM   4713  CA  ILE A 624      -4.047 -26.053 -23.085  1.00 76.43           C  
-ANISOU 4713  CA  ILE A 624     9139  12161   7740  -4718  -1316    284       C  
-ATOM   4714  C   ILE A 624      -3.057 -26.968 -23.800  1.00 77.19           C  
-ANISOU 4714  C   ILE A 624     9520  11966   7844  -4784  -1133    181       C  
-ATOM   4715  O   ILE A 624      -3.337 -28.145 -24.035  1.00 77.62           O  
-ANISOU 4715  O   ILE A 624     9748  11936   7808  -4973  -1102    169       O  
-ATOM   4716  CB  ILE A 624      -4.130 -26.464 -21.597  1.00 76.47           C  
-ANISOU 4716  CB  ILE A 624     8968  12219   7869  -4626  -1341    328       C  
-ATOM   4717  CG1 ILE A 624      -5.234 -25.679 -20.885  1.00 75.37           C  
-ANISOU 4717  CG1 ILE A 624     8573  12343   7722  -4599  -1504    439       C  
-ATOM   4718  CG2 ILE A 624      -2.789 -26.256 -20.915  1.00 74.54           C  
-ANISOU 4718  CG2 ILE A 624     8666  11835   7820  -4396  -1211    275       C  
-ATOM   4719  CD1 ILE A 624      -5.065 -24.176 -20.950  1.00 75.47           C  
-ANISOU 4719  CD1 ILE A 624     8430  12463   7784  -4434  -1510    467       C  
-ATOM   4720  N   LEU A 625      -1.899 -26.414 -24.142  1.00 63.59           N  
-ANISOU 4720  N   LEU A 625     7847  10080   6235  -4634   -991    103       N  
-ATOM   4721  CA  LEU A 625      -0.835 -27.174 -24.784  1.00 65.98           C  
-ANISOU 4721  CA  LEU A 625     8404  10074   6590  -4668   -785      7       C  
-ATOM   4722  C   LEU A 625       0.283 -27.441 -23.790  1.00 67.03           C  
-ANISOU 4722  C   LEU A 625     8430  10085   6955  -4460   -668    -21       C  
-ATOM   4723  O   LEU A 625       0.551 -26.619 -22.918  1.00 66.16           O  
-ANISOU 4723  O   LEU A 625     8074  10094   6968  -4262   -716     -5       O  
-ATOM   4724  CB  LEU A 625      -0.277 -26.408 -25.983  1.00 65.34           C  
-ANISOU 4724  CB  LEU A 625     8483   9859   6483  -4656   -687    -74       C  
-ATOM   4725  CG  LEU A 625      -1.132 -26.288 -27.247  1.00 66.82           C  
-ANISOU 4725  CG  LEU A 625     8870  10092   6427  -4877   -767    -63       C  
-ATOM   4726  CD1 LEU A 625      -2.462 -25.594 -26.977  1.00 66.79           C  
-ANISOU 4726  CD1 LEU A 625     8651  10429   6296  -4902  -1011     49       C  
-ATOM   4727  CD2 LEU A 625      -0.351 -25.541 -28.313  1.00 66.34           C  
-ANISOU 4727  CD2 LEU A 625     8991   9841   6374  -4824   -627   -160       C  
-ATOM   4728  N   GLU A 626       0.939 -28.587 -23.927  1.00 73.83           N  
-ANISOU 4728  N   GLU A 626     9477  10706   7869  -4510   -506    -57       N  
-ATOM   4729  CA  GLU A 626       2.049 -28.924 -23.046  1.00 77.24           C  
-ANISOU 4729  CA  GLU A 626     9812  11011   8523  -4308   -395    -72       C  
-ATOM   4730  C   GLU A 626       3.100 -27.819 -23.031  1.00 76.59           C  
-ANISOU 4730  C   GLU A 626     9599  10884   8618  -4092   -329   -144       C  
-ATOM   4731  O   GLU A 626       3.119 -26.945 -23.898  1.00 77.31           O  
-ANISOU 4731  O   GLU A 626     9748  10965   8661  -4111   -307   -201       O  
-ATOM   4732  CB  GLU A 626       2.681 -30.260 -23.445  1.00 81.87           C  
-ANISOU 4732  CB  GLU A 626    10655  11308   9145  -4393   -185    -97       C  
-ATOM   4733  CG  GLU A 626       1.919 -31.483 -22.954  1.00 88.36           C  
-ANISOU 4733  CG  GLU A 626    11551  12166   9856  -4530   -209    -29       C  
-ATOM   4734  CD  GLU A 626       2.021 -31.682 -21.446  1.00 90.90           C  
-ANISOU 4734  CD  GLU A 626    11645  12598  10296  -4340   -285     35       C  
-ATOM   4735  OE1 GLU A 626       2.765 -30.920 -20.785  1.00 92.07           O  
-ANISOU 4735  OE1 GLU A 626    11577  12788  10617  -4109   -318     29       O  
-ATOM   4736  OE2 GLU A 626       1.356 -32.603 -20.921  1.00 93.38           O  
-ANISOU 4736  OE2 GLU A 626    12007  12951  10522  -4431   -305     85       O  
-ATOM   4737  N   LYS A 627       3.969 -27.865 -22.030  1.00 77.51           N  
-ANISOU 4737  N   LYS A 627     9542  10976   8934  -3889   -294   -144       N  
-ATOM   4738  CA  LYS A 627       5.027 -26.877 -21.885  1.00 76.67           C  
-ANISOU 4738  CA  LYS A 627     9285  10836   9011  -3687   -225   -224       C  
-ATOM   4739  C   LYS A 627       6.135 -27.115 -22.901  1.00 78.54           C  
-ANISOU 4739  C   LYS A 627     9723  10753   9365  -3685     11   -331       C  
-ATOM   4740  O   LYS A 627       6.843 -28.115 -22.830  1.00 78.91           O  
-ANISOU 4740  O   LYS A 627     9859  10593   9530  -3663    145   -328       O  
-ATOM   4741  CB  LYS A 627       5.606 -26.938 -20.473  1.00 74.95           C  
-ANISOU 4741  CB  LYS A 627     8818  10700   8961  -3490   -278   -186       C  
-ATOM   4742  CG  LYS A 627       6.703 -25.933 -20.209  1.00 71.36           C  
-ANISOU 4742  CG  LYS A 627     8179  10239   8696  -3293   -215   -274       C  
-ATOM   4743  CD  LYS A 627       7.710 -26.480 -19.223  1.00 70.53           C  
-ANISOU 4743  CD  LYS A 627     7932  10074   8792  -3122   -190   -258       C  
-ATOM   4744  CE  LYS A 627       8.747 -25.428 -18.882  1.00 69.54           C  
-ANISOU 4744  CE  LYS A 627     7593   9982   8848  -2943   -149   -352       C  
-ATOM   4745  NZ  LYS A 627      10.015 -26.016 -18.363  1.00 70.22           N  
-ANISOU 4745  NZ  LYS A 627     7585   9931   9166  -2785    -71   -367       N  
-ATOM   4746  N   GLY A 628       6.285 -26.193 -23.845  1.00 86.46           N  
-ANISOU 4746  N   GLY A 628    10807  11702  10340  -3701     80   -423       N  
-ATOM   4747  CA  GLY A 628       7.347 -26.291 -24.830  1.00 89.41           C  
-ANISOU 4747  CA  GLY A 628    11383  11750  10838  -3697    322   -540       C  
-ATOM   4748  C   GLY A 628       6.852 -26.265 -26.262  1.00 92.56           C  
-ANISOU 4748  C   GLY A 628    12102  12017  11049  -3904    388   -582       C  
-ATOM   4749  O   GLY A 628       7.619 -25.987 -27.180  1.00 94.08           O  
-ANISOU 4749  O   GLY A 628    12473  11955  11320  -3902    584   -697       O  
-ATOM   4750  N   GLN A 629       5.570 -26.561 -26.452  1.00 80.91           N  
-ANISOU 4750  N   GLN A 629    10705  10709   9327  -4090    226   -492       N  
-ATOM   4751  CA  GLN A 629       4.964 -26.522 -27.776  1.00 83.98           C  
-ANISOU 4751  CA  GLN A 629    11389  11020   9500  -4306    242   -516       C  
-ATOM   4752  C   GLN A 629       5.198 -25.165 -28.417  1.00 81.33           C  
-ANISOU 4752  C   GLN A 629    11061  10683   9157  -4217    279   -607       C  
-ATOM   4753  O   GLN A 629       5.366 -25.059 -29.631  1.00 81.47           O  
-ANISOU 4753  O   GLN A 629    11370  10489   9096  -4327    404   -683       O  
-ATOM   4754  CB  GLN A 629       3.466 -26.813 -27.694  1.00 88.86           C  
-ANISOU 4754  CB  GLN A 629    11996  11905   9863  -4490     10   -399       C  
-ATOM   4755  CG  GLN A 629       3.147 -28.227 -27.260  1.00 96.82           C  
-ANISOU 4755  CG  GLN A 629    13069  12882  10837  -4622     10   -329       C  
-ATOM   4756  CD  GLN A 629       3.792 -29.261 -28.159  1.00101.41           C  
-ANISOU 4756  CD  GLN A 629    13998  13105  11430  -4774    257   -385       C  
-ATOM   4757  OE1 GLN A 629       4.753 -29.925 -27.771  1.00100.77           O  
-ANISOU 4757  OE1 GLN A 629    13926  12817  11545  -4674    435   -400       O  
-ATOM   4758  NE2 GLN A 629       3.265 -29.402 -29.368  1.00104.52           N  
-ANISOU 4758  NE2 GLN A 629    14684  13418  11609  -5019    275   -407       N  
-ATOM   4759  N   GLY A 630       5.212 -24.128 -27.590  1.00 82.38           N  
-ANISOU 4759  N   GLY A 630    10893  11042   9367  -4021    187   -601       N  
-ATOM   4760  CA  GLY A 630       5.491 -22.786 -28.062  1.00 78.05           C  
-ANISOU 4760  CA  GLY A 630    10330  10500   8824  -3908    254   -693       C  
-ATOM   4761  C   GLY A 630       4.354 -22.180 -28.857  1.00 75.28           C  
-ANISOU 4761  C   GLY A 630    10093  10303   8206  -4026    125   -641       C  
-ATOM   4762  O   GLY A 630       4.566 -21.602 -29.918  1.00 74.74           O  
-ANISOU 4762  O   GLY A 630    10241  10085   8070  -4045    239   -729       O  
-ATOM   4763  N   ARG A 631       3.137 -22.310 -28.345  1.00 72.29           N  
-ANISOU 4763  N   ARG A 631     9569  10219   7678  -4103   -112   -496       N  
-ATOM   4764  CA  ARG A 631       1.979 -21.720 -29.005  1.00 71.75           C  
-ANISOU 4764  CA  ARG A 631     9557  10339   7365  -4203   -264   -422       C  
-ATOM   4765  C   ARG A 631       1.065 -20.996 -28.020  1.00 67.69           C  
-ANISOU 4765  C   ARG A 631     8713  10187   6821  -4107   -457   -294       C  
-ATOM   4766  O   ARG A 631       0.586 -21.582 -27.055  1.00 67.68           O  
-ANISOU 4766  O   ARG A 631     8532  10333   6850  -4133   -585   -202       O  
-ATOM   4767  CB  ARG A 631       1.195 -22.784 -29.772  1.00 77.30           C  
-ANISOU 4767  CB  ARG A 631    10504  11004   7863  -4482   -358   -366       C  
-ATOM   4768  CG  ARG A 631       1.995 -23.471 -30.866  1.00 85.41           C  
-ANISOU 4768  CG  ARG A 631    11906  11656   8890  -4612   -148   -480       C  
-ATOM   4769  CD  ARG A 631       1.137 -24.469 -31.628  1.00 93.75           C  
-ANISOU 4769  CD  ARG A 631    13213  12699   9710  -4918   -241   -423       C  
-ATOM   4770  NE  ARG A 631      -0.016 -23.823 -32.247  1.00101.05           N  
-ANISOU 4770  NE  ARG A 631    14156  13856  10382  -5014   -446   -346       N  
-ATOM   4771  CZ  ARG A 631      -0.989 -24.475 -32.873  1.00106.73           C  
-ANISOU 4771  CZ  ARG A 631    15035  14657  10861  -5284   -591   -281       C  
-ATOM   4772  NH1 ARG A 631      -0.950 -25.799 -32.960  1.00109.55           N  
-ANISOU 4772  NH1 ARG A 631    15565  14870  11189  -5495   -526   -292       N  
-ATOM   4773  NH2 ARG A 631      -2.001 -23.804 -33.408  1.00110.33           N  
-ANISOU 4773  NH2 ARG A 631    15474  15344  11103  -5344   -792   -202       N  
-ATOM   4774  N   ILE A 632       0.839 -19.712 -28.270  1.00 64.87           N  
-ANISOU 4774  N   ILE A 632     8292   9950   6407  -3995   -454   -290       N  
-ATOM   4775  CA  ILE A 632      -0.069 -18.907 -27.464  1.00 60.75           C  
-ANISOU 4775  CA  ILE A 632     7481   9752   5850  -3909   -602   -159       C  
-ATOM   4776  C   ILE A 632      -0.875 -18.006 -28.383  1.00 62.97           C  
-ANISOU 4776  C   ILE A 632     7842  10153   5930  -3926   -663   -100       C  
-ATOM   4777  O   ILE A 632      -0.328 -17.098 -29.006  1.00 62.32           O  
-ANISOU 4777  O   ILE A 632     7869   9967   5842  -3813   -505   -190       O  
-ATOM   4778  CB  ILE A 632       0.691 -18.015 -26.467  1.00 55.49           C  
-ANISOU 4778  CB  ILE A 632     6578   9128   5376  -3680   -479   -209       C  
-ATOM   4779  CG1 ILE A 632       1.614 -18.860 -25.586  1.00 50.62           C  
-ANISOU 4779  CG1 ILE A 632     5884   8385   4963  -3642   -421   -270       C  
-ATOM   4780  CG2 ILE A 632      -0.288 -17.211 -25.623  1.00 51.41           C  
-ANISOU 4780  CG2 ILE A 632     5788   8926   4821  -3613   -607    -61       C  
-ATOM   4781  CD1 ILE A 632       2.247 -18.096 -24.438  1.00 45.03           C  
-ANISOU 4781  CD1 ILE A 632     4915   7765   4430  -3448   -348   -301       C  
-ATOM   4782  N   ILE A 633      -2.175 -18.250 -28.475  1.00 68.68           N  
-ANISOU 4782  N   ILE A 633     8510  11095   6489  -4062   -887     51       N  
-ATOM   4783  CA  ILE A 633      -2.993 -17.530 -29.438  1.00 72.09           C  
-ANISOU 4783  CA  ILE A 633     9031  11647   6714  -4094   -975    126       C  
-ATOM   4784  C   ILE A 633      -4.312 -17.095 -28.818  1.00 72.59           C  
-ANISOU 4784  C   ILE A 633     8810  12052   6718  -4083  -1179    321       C  
-ATOM   4785  O   ILE A 633      -5.140 -17.927 -28.451  1.00 73.58           O  
-ANISOU 4785  O   ILE A 633     8844  12308   6806  -4238  -1362    414       O  
-ATOM   4786  CB  ILE A 633      -3.270 -18.405 -30.669  1.00 75.97           C  
-ANISOU 4786  CB  ILE A 633     9840  12012   7013  -4336  -1050    103       C  
-ATOM   4787  CG1 ILE A 633      -2.035 -19.250 -30.999  1.00 77.64           C  
-ANISOU 4787  CG1 ILE A 633    10306  11867   7328  -4393   -850    -68       C  
-ATOM   4788  CG2 ILE A 633      -3.687 -17.540 -31.851  1.00 77.73           C  
-ANISOU 4788  CG2 ILE A 633    10233  12268   7031  -4329  -1077    131       C  
-ATOM   4789  CD1 ILE A 633      -2.338 -20.509 -31.779  1.00 82.98           C  
-ANISOU 4789  CD1 ILE A 633    11250  12423   7855  -4679   -918    -74       C  
-ATOM   4790  N   LEU A 634      -4.509 -15.786 -28.709  1.00 70.57           N  
-ANISOU 4790  N   LEU A 634     8422  11932   6461  -3902  -1124    381       N  
-ATOM   4791  CA  LEU A 634      -5.659 -15.260 -27.981  1.00 73.03           C  
-ANISOU 4791  CA  LEU A 634     8437  12546   6764  -3860  -1268    573       C  
-ATOM   4792  C   LEU A 634      -6.526 -14.337 -28.830  1.00 76.73           C  
-ANISOU 4792  C   LEU A 634     8922  13179   7053  -3821  -1344    698       C  
-ATOM   4793  O   LEU A 634      -6.225 -13.157 -28.991  1.00 76.21           O  
-ANISOU 4793  O   LEU A 634     8854  13114   6988  -3632  -1181    691       O  
-ATOM   4794  CB  LEU A 634      -5.190 -14.534 -26.718  1.00 68.59           C  
-ANISOU 4794  CB  LEU A 634     7634  12029   6398  -3667  -1120    569       C  
-ATOM   4795  CG  LEU A 634      -4.118 -15.269 -25.906  1.00 65.22           C  
-ANISOU 4795  CG  LEU A 634     7200  11427   6155  -3659  -1020    433       C  
-ATOM   4796  CD1 LEU A 634      -3.622 -14.402 -24.766  1.00 61.16           C  
-ANISOU 4796  CD1 LEU A 634     6469  10964   5804  -3474   -871    422       C  
-ATOM   4797  CD2 LEU A 634      -4.638 -16.602 -25.389  1.00 64.16           C  
-ANISOU 4797  CD2 LEU A 634     7018  11325   6034  -3835  -1200    485       C  
-ATOM   4798  N   LYS A 635      -7.614 -14.882 -29.361  1.00 90.66           N  
-ANISOU 4798  N   LYS A 635    10699  15090   8659  -4001  -1587    816       N  
-ATOM   4799  CA  LYS A 635      -8.501 -14.118 -30.226  1.00 93.95           C  
-ANISOU 4799  CA  LYS A 635    11129  15678   8890  -3978  -1700    953       C  
-ATOM   4800  C   LYS A 635      -9.429 -13.206 -29.434  1.00 92.99           C  
-ANISOU 4800  C   LYS A 635    10668  15833   8832  -3838  -1746   1155       C  
-ATOM   4801  O   LYS A 635     -10.087 -13.642 -28.492  1.00 93.04           O  
-ANISOU 4801  O   LYS A 635    10431  15981   8940  -3904  -1862   1251       O  
-ATOM   4802  CB  LYS A 635      -9.308 -15.057 -31.126  1.00102.41           C  
-ANISOU 4802  CB  LYS A 635    12338  16814   9759  -4243  -1956   1001       C  
-ATOM   4803  CG  LYS A 635      -8.452 -15.810 -32.134  1.00110.52           C  
-ANISOU 4803  CG  LYS A 635    13756  17552  10685  -4389  -1883    819       C  
-ATOM   4804  CD  LYS A 635      -7.508 -14.856 -32.851  1.00117.80           C  
-ANISOU 4804  CD  LYS A 635    14907  18272  11581  -4207  -1650    707       C  
-ATOM   4805  CE  LYS A 635      -6.669 -15.565 -33.902  1.00123.72           C  
-ANISOU 4805  CE  LYS A 635    16068  18701  12239  -4358  -1555    529       C  
-ATOM   4806  NZ  LYS A 635      -7.483 -16.014 -35.068  1.00129.51           N  
-ANISOU 4806  NZ  LYS A 635    17012  19497  12697  -4588  -1775    596       N  
-ATOM   4807  N   ALA A 636      -9.468 -11.937 -29.825  1.00 65.68           N  
-ANISOU 4807  N   ALA A 636     7211  12429   5317  -3643  -1629   1218       N  
-ATOM   4808  CA  ALA A 636     -10.335 -10.956 -29.188  1.00 68.54           C  
-ANISOU 4808  CA  ALA A 636     7276  13034   5732  -3496  -1629   1425       C  
-ATOM   4809  C   ALA A 636     -10.227 -11.051 -27.677  1.00 67.24           C  
-ANISOU 4809  C   ALA A 636     6856  12897   5797  -3460  -1549   1437       C  
-ATOM   4810  O   ALA A 636     -11.095 -11.629 -27.022  1.00 68.22           O  
-ANISOU 4810  O   ALA A 636     6774  13166   5981  -3576  -1726   1553       O  
-ATOM   4811  CB  ALA A 636     -11.772 -11.157 -29.629  1.00 71.77           C  
-ANISOU 4811  CB  ALA A 636     7559  13700   6011  -3613  -1926   1636       C  
-ATOM   4812  N   SER A 637      -9.159 -10.486 -27.126  1.00102.53           N  
-ANISOU 4812  N   SER A 637    11347  17220  10390  -3308  -1278   1310       N  
-ATOM   4813  CA  SER A 637      -8.916 -10.569 -25.692  1.00 95.26           C  
-ANISOU 4813  CA  SER A 637    10219  16302   9672  -3280  -1193   1302       C  
-ATOM   4814  C   SER A 637      -9.046  -9.213 -25.005  1.00 98.56           C  
-ANISOU 4814  C   SER A 637    10457  16823  10168  -3084   -982   1408       C  
-ATOM   4815  O   SER A 637      -8.576  -8.197 -25.515  1.00 94.63           O  
-ANISOU 4815  O   SER A 637    10064  16278   9613  -2926   -772   1366       O  
-ATOM   4816  CB  SER A 637      -7.532 -11.161 -25.418  1.00 78.56           C  
-ANISOU 4816  CB  SER A 637     8248  13942   7658  -3293  -1063   1066       C  
-ATOM   4817  OG  SER A 637      -6.512 -10.232 -25.739  1.00 75.61           O  
-ANISOU 4817  OG  SER A 637     8000  13435   7293  -3126   -794    932       O  
-ATOM   4818  N   ARG A 638      -9.692  -9.211 -23.844  1.00 86.29           N  
-ANISOU 4818  N   ARG A 638     8651  15395   8742  -3102  -1017   1542       N  
-ATOM   4819  CA  ARG A 638      -9.793  -8.016 -23.021  1.00 86.10           C  
-ANISOU 4819  CA  ARG A 638     8459  15446   8810  -2946   -790   1643       C  
-ATOM   4820  C   ARG A 638      -8.930  -8.216 -21.780  1.00 68.54           C  
-ANISOU 4820  C   ARG A 638     6180  13112   6750  -2950   -658   1519       C  
-ATOM   4821  O   ARG A 638      -8.493  -9.332 -21.502  1.00 65.73           O  
-ANISOU 4821  O   ARG A 638     5875  12655   6444  -3068   -781   1402       O  
-ATOM   4822  CB  ARG A 638     -11.246  -7.758 -22.617  1.00110.02           C  
-ANISOU 4822  CB  ARG A 638    11243  18691  11867  -2966   -906   1912       C  
-ATOM   4823  CG  ARG A 638     -12.254  -7.850 -23.755  1.00134.12           C  
-ANISOU 4823  CG  ARG A 638    14306  21887  14765  -3006  -1127   2054       C  
-ATOM   4824  CD  ARG A 638     -12.625  -9.294 -24.066  1.00143.92           C  
-ANISOU 4824  CD  ARG A 638    15590  23132  15962  -3233  -1437   2009       C  
-ATOM   4825  NE  ARG A 638     -13.238  -9.961 -22.922  1.00151.53           N  
-ANISOU 4825  NE  ARG A 638    16349  24150  17077  -3351  -1540   2079       N  
-ATOM   4826  CZ  ARG A 638     -13.681 -11.214 -22.935  1.00158.97           C  
-ANISOU 4826  CZ  ARG A 638    17290  25105  18007  -3554  -1778   2051       C  
-ATOM   4827  NH1 ARG A 638     -13.579 -11.943 -24.037  1.00162.35           N  
-ANISOU 4827  NH1 ARG A 638    17910  25502  18275  -3676  -1940   1962       N  
-ATOM   4828  NH2 ARG A 638     -14.226 -11.739 -21.848  1.00163.34           N  
-ANISOU 4828  NH2 ARG A 638    17670  25689  18703  -3644  -1836   2107       N  
-ATOM   4829  N   HIS A 639      -8.671  -7.145 -21.038  1.00122.24           N  
-ANISOU 4829  N   HIS A 639    12887  19931  13626  -2824   -401   1548       N  
-ATOM   4830  CA  HIS A 639      -7.912  -7.268 -19.799  1.00104.25           C  
-ANISOU 4830  CA  HIS A 639    10546  17572  11492  -2837   -288   1447       C  
-ATOM   4831  C   HIS A 639      -8.859  -7.539 -18.639  1.00109.50           C  
-ANISOU 4831  C   HIS A 639    11004  18338  12263  -2922   -385   1621       C  
-ATOM   4832  O   HIS A 639      -9.677  -6.690 -18.290  1.00114.74           O  
-ANISOU 4832  O   HIS A 639    11529  19118  12950  -2870   -284   1809       O  
-ATOM   4833  CB  HIS A 639      -7.085  -6.010 -19.531  1.00 89.15           C  
-ANISOU 4833  CB  HIS A 639     8654  15619   9600  -2688     55   1366       C  
-ATOM   4834  CG  HIS A 639      -6.183  -6.129 -18.338  1.00 73.57           C  
-ANISOU 4834  CG  HIS A 639     6630  13567   7755  -2712    161   1241       C  
-ATOM   4835  ND1 HIS A 639      -4.856  -5.761 -18.374  1.00 60.88           N  
-ANISOU 4835  ND1 HIS A 639     5123  11840   6170  -2642    363   1022       N  
-ATOM   4836  CD2 HIS A 639      -6.419  -6.570 -17.083  1.00 68.37           C  
-ANISOU 4836  CD2 HIS A 639     5838  12931   7207  -2799     88   1302       C  
-ATOM   4837  CE1 HIS A 639      -4.310  -5.974 -17.187  1.00 51.37           C  
-ANISOU 4837  CE1 HIS A 639     3832  10608   5079  -2687    392    962       C  
-ATOM   4838  NE2 HIS A 639      -5.242  -6.466 -16.386  1.00 52.53           N  
-ANISOU 4838  NE2 HIS A 639     3850  10835   5275  -2781    227   1132       N  
-ATOM   4839  N   ALA A 640      -8.737  -8.723 -18.046  1.00 79.60           N  
-ANISOU 4839  N   ALA A 640     7210  14489   8547  -3050   -561   1558       N  
-ATOM   4840  CA  ALA A 640      -9.635  -9.166 -16.980  1.00 82.43           C  
-ANISOU 4840  CA  ALA A 640     7407  14909   9005  -3150   -670   1699       C  
-ATOM   4841  C   ALA A 640     -10.128  -8.044 -16.065  1.00 70.12           C  
-ANISOU 4841  C   ALA A 640     5693  13424   7526  -3085   -464   1858       C  
-ATOM   4842  O   ALA A 640     -11.325  -7.925 -15.815  1.00 69.00           O  
-ANISOU 4842  O   ALA A 640     5409  13385   7424  -3124   -522   2057       O  
-ATOM   4843  CB  ALA A 640      -8.977 -10.263 -16.158  1.00 73.30           C  
-ANISOU 4843  CB  ALA A 640     6291  13630   7928  -3239   -759   1565       C  
-ATOM   4844  N   CYS A 641      -9.205  -7.229 -15.568  1.00126.85           N  
-ANISOU 4844  N   CYS A 641    12906  20551  14740  -2996   -211   1769       N  
-ATOM   4845  CA  CYS A 641      -9.556  -6.169 -14.627  1.00110.31           C  
-ANISOU 4845  CA  CYS A 641    10694  18502  12715  -2956     26   1905       C  
-ATOM   4846  C   CYS A 641      -9.913  -4.849 -15.304  1.00119.52           C  
-ANISOU 4846  C   CYS A 641    11844  19757  13811  -2820    249   2021       C  
-ATOM   4847  O   CYS A 641     -10.832  -4.158 -14.873  1.00116.64           O  
-ANISOU 4847  O   CYS A 641    11396  19450  13472  -2772    338   2221       O  
-ATOM   4848  CB  CYS A 641      -8.421  -5.942 -13.629  1.00 92.69           C  
-ANISOU 4848  CB  CYS A 641     8576  16143  10500  -2905    165   1742       C  
-ATOM   4849  SG  CYS A 641      -8.075  -7.352 -12.561  1.00 85.55           S  
-ANISOU 4849  SG  CYS A 641     7702  15133   9671  -3028    -57   1651       S  
-ATOM   4850  N   VAL A 642      -9.181  -4.497 -16.356  1.00 89.28           N  
-ANISOU 4850  N   VAL A 642     8152  15898   9872  -2719    327   1886       N  
-ATOM   4851  CA  VAL A 642      -9.389  -3.225 -17.041  1.00 99.98           C  
-ANISOU 4851  CA  VAL A 642     9529  17318  11141  -2569    568   1974       C  
-ATOM   4852  C   VAL A 642     -10.578  -3.295 -18.001  1.00123.68           C  
-ANISOU 4852  C   VAL A 642    12482  20443  14067  -2546    385   2168       C  
-ATOM   4853  O   VAL A 642     -10.834  -2.362 -18.760  1.00130.04           O  
-ANISOU 4853  O   VAL A 642    13320  21310  14779  -2409    535   2256       O  
-ATOM   4854  CB  VAL A 642      -8.125  -2.790 -17.807  1.00 99.42           C  
-ANISOU 4854  CB  VAL A 642     9648  17146  10980  -2466    745   1738       C  
-ATOM   4855  CG1 VAL A 642      -8.223  -1.328 -18.214  1.00106.82           C  
-ANISOU 4855  CG1 VAL A 642    10617  18131  11840  -2303   1083   1813       C  
-ATOM   4856  CG2 VAL A 642      -6.893  -3.012 -16.953  1.00 91.88           C  
-ANISOU 4856  CG2 VAL A 642     8727  16077  10107  -2514    840   1521       C  
-ATOM   4857  N   GLU A 643     -11.308  -4.404 -17.955  1.00 54.12           N  
-ANISOU 4857  N   GLU A 643     3596  11674   5292  -2681     64   2234       N  
-ATOM   4858  CA  GLU A 643     -12.466  -4.598 -18.817  1.00 80.88           C  
-ANISOU 4858  CA  GLU A 643     6917  15200   8615  -2692   -153   2413       C  
-ATOM   4859  C   GLU A 643     -13.754  -4.225 -18.091  1.00 77.43           C  
-ANISOU 4859  C   GLU A 643     6245  14882   8293  -2706   -135   2686       C  
-ATOM   4860  O   GLU A 643     -14.788  -4.005 -18.718  1.00 95.19           O  
-ANISOU 4860  O   GLU A 643     8391  17272  10505  -2672   -241   2882       O  
-ATOM   4861  CB  GLU A 643     -12.538  -6.051 -19.292  1.00 93.48           C  
-ANISOU 4861  CB  GLU A 643     8575  16773  10170  -2851   -503   2314       C  
-ATOM   4862  CG  GLU A 643     -13.677  -6.343 -20.258  1.00119.87           C  
-ANISOU 4862  CG  GLU A 643    11858  20266  13420  -2894   -757   2471       C  
-ATOM   4863  CD  GLU A 643     -13.842  -7.826 -20.525  1.00128.53           C  
-ANISOU 4863  CD  GLU A 643    13003  21344  14487  -3090  -1077   2379       C  
-ATOM   4864  OE1 GLU A 643     -13.230  -8.633 -19.795  1.00115.91           O  
-ANISOU 4864  OE1 GLU A 643    11452  19621  12969  -3183  -1096   2231       O  
-ATOM   4865  OE2 GLU A 643     -14.582  -8.186 -21.463  1.00147.59           O  
-ANISOU 4865  OE2 GLU A 643    15415  23870  16792  -3154  -1302   2457       O  
-ATOM   4866  N   VAL A 644     -13.687  -4.156 -16.766  1.00122.75           N  
-ANISOU 4866  N   VAL A 644    11903  20559  14177  -2759     -1   2702       N  
-ATOM   4867  CA  VAL A 644     -14.869  -3.869 -15.961  1.00113.47           C  
-ANISOU 4867  CA  VAL A 644    10520  19453  13141  -2793     40   2949       C  
-ATOM   4868  C   VAL A 644     -14.630  -2.726 -14.984  1.00102.95           C  
-ANISOU 4868  C   VAL A 644     9222  18035  11860  -2681    382   3000       C  
-ATOM   4869  O   VAL A 644     -15.337  -2.605 -13.983  1.00103.84           O  
-ANISOU 4869  O   VAL A 644     9296  18088  12072  -2680    393   3128       O  
-ATOM   4870  CB  VAL A 644     -15.316  -5.107 -15.158  1.00 98.50           C  
-ANISOU 4870  CB  VAL A 644     8551  17514  11362  -2981   -199   2933       C  
-ATOM   4871  CG1 VAL A 644     -16.748  -5.477 -15.508  1.00 92.86           C  
-ANISOU 4871  CG1 VAL A 644     7657  16934  10690  -3041   -422   3138       C  
-ATOM   4872  CG2 VAL A 644     -14.375  -6.279 -15.408  1.00 93.55           C  
-ANISOU 4872  CG2 VAL A 644     8088  16791  10664  -3070   -402   2673       C  
-ATOM   4873  N   GLN A 645     -13.637  -1.891 -15.276  1.00141.33           N  
-ANISOU 4873  N   GLN A 645    14254  22830  16616  -2535    600   2860       N  
-ATOM   4874  CA  GLN A 645     -13.248  -0.822 -14.361  1.00135.65           C  
-ANISOU 4874  CA  GLN A 645    13679  21960  15903  -2380    831   2818       C  
-ATOM   4875  C   GLN A 645     -14.410   0.118 -14.063  1.00140.08           C  
-ANISOU 4875  C   GLN A 645    14138  22552  16533  -2268    959   3090       C  
-ATOM   4876  O   GLN A 645     -15.203  -0.133 -13.157  1.00144.35           O  
-ANISOU 4876  O   GLN A 645    14598  23054  17193  -2332    892   3222       O  
-ATOM   4877  CB  GLN A 645     -12.049  -0.044 -14.910  1.00147.96           C  
-ANISOU 4877  CB  GLN A 645    15419  23449  17349  -2242   1033   2607       C  
-ATOM   4878  CG  GLN A 645     -11.500   1.001 -13.948  1.00138.59           C  
-ANISOU 4878  CG  GLN A 645    14381  22089  16187  -2117   1245   2505       C  
-ATOM   4879  CD  GLN A 645     -10.067   1.387 -14.256  1.00134.68           C  
-ANISOU 4879  CD  GLN A 645    14069  21490  15615  -2051   1379   2212       C  
-ATOM   4880  OE1 GLN A 645      -9.545   2.363 -13.717  1.00137.09           O  
-ANISOU 4880  OE1 GLN A 645    14496  21661  15930  -1951   1571   2106       O  
-ATOM   4881  NE2 GLN A 645      -9.420   0.615 -15.122  1.00128.69           N  
-ANISOU 4881  NE2 GLN A 645    13328  20776  14791  -2118   1284   2074       N  
-ATOM   4882  N   ASP A 646     -14.506   1.201 -14.823  1.00184.71           N  
-ANISOU 4882  N   ASP A 646    24680  22783  22720  -2807  -6408   4528       N  
-ATOM   4883  CA  ASP A 646     -15.594   2.152 -14.648  1.00165.03           C  
-ANISOU 4883  CA  ASP A 646    22328  20460  19917  -2748  -6746   4180       C  
-ATOM   4884  C   ASP A 646     -16.652   1.921 -15.715  1.00148.69           C  
-ANISOU 4884  C   ASP A 646    20293  18519  17682  -2691  -6581   3703       C  
-ATOM   4885  O   ASP A 646     -17.343   2.850 -16.130  1.00137.74           O  
-ANISOU 4885  O   ASP A 646    19034  17262  16038  -2623  -6844   3439       O  
-ATOM   4886  CB  ASP A 646     -15.068   3.575 -14.715  1.00177.37           C  
-ANISOU 4886  CB  ASP A 646    24010  22024  21357  -2707  -7180   4385       C  
-ATOM   4887  N   GLU A 647     -16.774   0.670 -16.149  1.00320.85           N  
-ANISOU 4887  N   GLU A 647    41984  40288  39637  -2719  -6142   3595       N  
-ATOM   4888  CA  GLU A 647     -17.649   0.321 -17.261  1.00301.51           C  
-ANISOU 4888  CA  GLU A 647    39549  37943  37067  -2671  -5931   3175       C  
-ATOM   4889  C   GLU A 647     -17.288   1.151 -18.484  1.00310.96           C  
-ANISOU 4889  C   GLU A 647    40825  39153  38173  -2608  -6061   3202       C  
-ATOM   4890  O   GLU A 647     -18.145   1.486 -19.302  1.00295.73           O  
-ANISOU 4890  O   GLU A 647    38975  37354  36035  -2544  -6097   2831       O  
-ATOM   4891  CB  GLU A 647     -19.120   0.514 -16.886  1.00165.31           C  
-ANISOU 4891  CB  GLU A 647    22380  20874  19558  -2637  -6057   2699       C  
-ATOM   4892  CG  GLU A 647     -19.616  -0.438 -15.808  1.00162.80           C  
-ANISOU 4892  CG  GLU A 647    21979  20556  19323  -2697  -5875   2608       C  
-ATOM   4893  CD  GLU A 647     -19.423  -1.899 -16.181  1.00158.85           C  
-ANISOU 4893  CD  GLU A 647    21329  19971  19057  -2745  -5369   2612       C  
-ATOM   4894  OE1 GLU A 647     -20.434  -2.590 -16.430  1.00156.47           O  
-ANISOU 4894  OE1 GLU A 647    21006  19763  18683  -2736  -5142   2219       O  
-ATOM   4895  OE2 GLU A 647     -18.261  -2.360 -16.217  1.00158.36           O  
-ANISOU 4895  OE2 GLU A 647    21170  19749  19251  -2792  -5199   3007       O  
-ATOM   4896  N   ILE A 648     -16.006   1.480 -18.593  1.00134.30           N  
-ANISOU 4896  N   ILE A 648    18429  16641  15959  -2626  -6132   3648       N  
-ATOM   4897  CA  ILE A 648     -15.498   2.248 -19.718  1.00148.87           C  
-ANISOU 4897  CA  ILE A 648    20339  18477  17749  -2572  -6250   3735       C  
-ATOM   4898  C   ILE A 648     -15.638   1.444 -21.002  1.00140.44           C  
-ANISOU 4898  C   ILE A 648    19211  17409  16742  -2556  -5864   3548       C  
-ATOM   4899  O   ILE A 648     -16.184   0.342 -20.999  1.00126.53           O  
-ANISOU 4899  O   ILE A 648    17364  15663  15050  -2584  -5524   3335       O  
-ATOM   4900  CB  ILE A 648     -14.019   2.610 -19.513  1.00173.67           C  
-ANISOU 4900  CB  ILE A 648    23449  21455  21084  -2605  -6360   4281       C  
-ATOM   4901  CG1 ILE A 648     -13.160   1.344 -19.520  1.00179.06           C  
-ANISOU 4901  CG1 ILE A 648    23968  21977  22089  -2676  -5943   4557       C  
-ATOM   4902  CG2 ILE A 648     -13.835   3.371 -18.210  1.00182.92           C  
-ANISOU 4902  CG2 ILE A 648    24674  22619  22207  -2627  -6733   4483       C  
-ATOM   4903  CD1 ILE A 648     -11.698   1.595 -19.237  1.00196.50           C  
-ANISOU 4903  CD1 ILE A 648    26135  24019  24508  -2715  -6027   5103       C  
-ATOM   4904  N   ALA A 649     -15.142   1.997 -22.102  1.00152.22           N  
-ANISOU 4904  N   ALA A 649    20746  18883  18208  -2511  -5917   3629       N  
-ATOM   4905  CA  ALA A 649     -15.190   1.305 -23.381  1.00134.68           C  
-ANISOU 4905  CA  ALA A 649    18470  16656  16046  -2493  -5566   3477       C  
-ATOM   4906  C   ALA A 649     -13.886   0.565 -23.630  1.00133.80           C  
-ANISOU 4906  C   ALA A 649    18232  16357  16249  -2548  -5282   3895       C  
-ATOM   4907  O   ALA A 649     -12.864   1.176 -23.939  1.00145.03           O  
-ANISOU 4907  O   ALA A 649    19674  17689  17743  -2541  -5426   4237       O  
-ATOM   4908  CB  ALA A 649     -15.467   2.287 -24.504  1.00135.40           C  
-ANISOU 4908  CB  ALA A 649    18681  16843  15921  -2411  -5765   3293       C  
-ATOM   4909  N   PHE A 650     -13.921  -0.754 -23.488  1.00122.33           N  
-ANISOU 4909  N   PHE A 650    16650  14846  14985  -2603  -4877   3870       N  
-ATOM   4910  CA  PHE A 650     -12.731  -1.562 -23.712  1.00113.17           C  
-ANISOU 4910  CA  PHE A 650    15361  13508  14132  -2658  -4576   4250       C  
-ATOM   4911  C   PHE A 650     -12.830  -2.315 -25.034  1.00 97.76           C  
-ANISOU 4911  C   PHE A 650    13353  11553  12240  -2641  -4200   4073       C  
-ATOM   4912  O   PHE A 650     -13.868  -2.898 -25.347  1.00 88.74           O  
-ANISOU 4912  O   PHE A 650    12201  10514  11003  -2627  -3999   3666       O  
-ATOM   4913  CB  PHE A 650     -12.505  -2.530 -22.548  1.00110.78           C  
-ANISOU 4913  CB  PHE A 650    14941  13115  14036  -2739  -4384   4422       C  
-ATOM   4914  CG  PHE A 650     -11.115  -3.089 -22.494  1.00103.72           C  
-ANISOU 4914  CG  PHE A 650    13930  12027  13453  -2797  -4186   4906       C  
-ATOM   4915  CD1 PHE A 650     -10.133  -2.464 -21.744  1.00121.95           C  
-ANISOU 4915  CD1 PHE A 650    16248  14237  15849  -2824  -4447   5337       C  
-ATOM   4916  CD2 PHE A 650     -10.783  -4.227 -23.208  1.00 89.19           C  
-ANISOU 4916  CD2 PHE A 650    11971  10104  11815  -2826  -3742   4932       C  
-ATOM   4917  CE1 PHE A 650      -8.850  -2.971 -21.697  1.00123.70           C  
-ANISOU 4917  CE1 PHE A 650    16363  14282  16357  -2878  -4267   5784       C  
-ATOM   4918  CE2 PHE A 650      -9.502  -4.737 -23.167  1.00 91.75           C  
-ANISOU 4918  CE2 PHE A 650    12188  10249  12425  -2879  -3560   5378       C  
-ATOM   4919  CZ  PHE A 650      -8.534  -4.110 -22.410  1.00107.87           C  
-ANISOU 4919  CZ  PHE A 650    14239  12194  14552  -2905  -3823   5805       C  
-ATOM   4920  N   ILE A 651     -11.748  -2.294 -25.808  1.00104.38           N  
-ANISOU 4920  N   ILE A 651    11342  17470  10848   -753  -1666   1810       N  
-ATOM   4921  CA  ILE A 651     -11.736  -2.938 -27.116  1.00 96.07           C  
-ANISOU 4921  CA  ILE A 651    10401  16557   9545  -1004  -1732   1876       C  
-ATOM   4922  C   ILE A 651     -10.694  -4.058 -27.179  1.00 67.04           C  
-ANISOU 4922  C   ILE A 651     7022  12643   5806  -1256  -1644   1687       C  
-ATOM   4923  O   ILE A 651      -9.511  -3.836 -26.919  1.00 54.89           O  
-ANISOU 4923  O   ILE A 651     5663  10746   4445  -1160  -1531   1603       O  
-ATOM   4924  CB  ILE A 651     -11.517  -1.904 -28.250  1.00109.06           C  
-ANISOU 4924  CB  ILE A 651    12056  18173  11210   -836  -1766   2087       C  
-ATOM   4925  CG1 ILE A 651     -10.033  -1.594 -28.447  1.00 91.56           C  
-ANISOU 4925  CG1 ILE A 651    10104  15532   9151   -772  -1642   2028       C  
-ATOM   4926  CG2 ILE A 651     -12.300  -0.630 -27.968  1.00140.69           C  
-ANISOU 4926  CG2 ILE A 651    15802  22288  15364   -501  -1815   2260       C  
-ATOM   4927  CD1 ILE A 651      -9.427  -2.280 -29.650  1.00 79.30           C  
-ANISOU 4927  CD1 ILE A 651     8769  13968   7393  -1016  -1637   2026       C  
-ATOM   4928  N   PRO A 652     -11.137  -5.280 -27.515  1.00 76.36           N  
-ANISOU 4928  N   PRO A 652     8255  14025   6733  -1583  -1695   1619       N  
-ATOM   4929  CA  PRO A 652     -10.226  -6.432 -27.527  1.00 73.95           C  
-ANISOU 4929  CA  PRO A 652     8241  13491   6365  -1816  -1605   1433       C  
-ATOM   4930  C   PRO A 652      -9.086  -6.267 -28.529  1.00 72.57           C  
-ANISOU 4930  C   PRO A 652     8300  13081   6194  -1805  -1535   1448       C  
-ATOM   4931  O   PRO A 652      -9.179  -5.450 -29.442  1.00 73.67           O  
-ANISOU 4931  O   PRO A 652     8384  13306   6303  -1701  -1584   1618       O  
-ATOM   4932  CB  PRO A 652     -11.128  -7.597 -27.964  1.00 69.41           C  
-ANISOU 4932  CB  PRO A 652     7661  13226   5485  -2170  -1697   1403       C  
-ATOM   4933  CG  PRO A 652     -12.517  -7.144 -27.702  1.00 71.02           C  
-ANISOU 4933  CG  PRO A 652     7530  13817   5636  -2114  -1821   1535       C  
-ATOM   4934  CD  PRO A 652     -12.511  -5.656 -27.885  1.00 77.23           C  
-ANISOU 4934  CD  PRO A 652     8157  14584   6601  -1755  -1836   1712       C  
-ATOM   4935  N   ASN A 653      -8.020  -7.039 -28.343  1.00 82.22           N  
-ANISOU 4935  N   ASN A 653     9773  14015   7450  -1904  -1418   1279       N  
-ATOM   4936  CA  ASN A 653      -6.945  -7.139 -29.323  1.00 81.50           C  
-ANISOU 4936  CA  ASN A 653     9917  13731   7319  -1944  -1337   1266       C  
-ATOM   4937  C   ASN A 653      -6.571  -8.602 -29.536  1.00 81.04           C  
-ANISOU 4937  C   ASN A 653    10107  13597   7089  -2230  -1278   1089       C  
-ATOM   4938  O   ASN A 653      -6.919  -9.460 -28.727  1.00 80.14           O  
-ANISOU 4938  O   ASN A 653    10006  13494   6951  -2361  -1279    970       O  
-ATOM   4939  CB  ASN A 653      -5.717  -6.345 -28.876  1.00 79.63           C  
-ANISOU 4939  CB  ASN A 653     9744  13147   7366  -1692  -1219   1249       C  
-ATOM   4940  CG  ASN A 653      -6.006  -4.868 -28.708  1.00 80.68           C  
-ANISOU 4940  CG  ASN A 653     9675  13302   7678  -1409  -1263   1416       C  
-ATOM   4941  OD1 ASN A 653      -6.153  -4.137 -29.688  1.00 81.14           O  
-ANISOU 4941  OD1 ASN A 653     9695  13454   7680  -1346  -1310   1586       O  
-ATOM   4942  ND2 ASN A 653      -6.076  -4.416 -27.459  1.00 81.27           N  
-ANISOU 4942  ND2 ASN A 653     9631  13279   7967  -1236  -1242   1368       N  
-ATOM   4943  N   ASP A 654      -5.872  -8.894 -30.627  1.00 84.93           N  
-ANISOU 4943  N   ASP A 654    10804  14008   7456  -2327  -1220   1073       N  
-ATOM   4944  CA  ASP A 654      -5.397 -10.255 -30.867  1.00 83.02           C  
-ANISOU 4944  CA  ASP A 654    10832  13645   7067  -2569  -1138    893       C  
-ATOM   4945  C   ASP A 654      -3.989 -10.437 -30.314  1.00 76.54           C  
-ANISOU 4945  C   ASP A 654    10183  12441   6459  -2436   -974    769       C  
-ATOM   4946  O   ASP A 654      -3.257  -9.468 -30.130  1.00 73.69           O  
-ANISOU 4946  O   ASP A 654     9763  11926   6310  -2195   -921    835       O  
-ATOM   4947  CB  ASP A 654      -5.441 -10.602 -32.357  1.00 90.74           C  
-ANISOU 4947  CB  ASP A 654    11953  14761   7762  -2769  -1155    917       C  
-ATOM   4948  CG  ASP A 654      -6.840 -10.952 -32.834  1.00 98.06           C  
-ANISOU 4948  CG  ASP A 654    12766  16077   8415  -3011  -1316    977       C  
-ATOM   4949  OD1 ASP A 654      -7.823 -10.527 -32.185  1.00100.91           O  
-ANISOU 4949  OD1 ASP A 654    12870  16646   8827  -2952  -1428   1069       O  
-ATOM   4950  OD2 ASP A 654      -6.956 -11.653 -33.862  1.00104.30           O  
-ANISOU 4950  OD2 ASP A 654    13720  16977   8931  -3264  -1327    930       O  
-ATOM   4951  N   VAL A 655      -3.624 -11.683 -30.033  1.00 71.31           N  
-ANISOU 4951  N   VAL A 655     9729  11628   5738  -2595   -895    596       N  
-ATOM   4952  CA  VAL A 655      -2.297 -12.006 -29.524  1.00 64.85           C  
-ANISOU 4952  CA  VAL A 655     9073  10466   5100  -2477   -740    480       C  
-ATOM   4953  C   VAL A 655      -1.794 -13.283 -30.167  1.00 64.61           C  
-ANISOU 4953  C   VAL A 655     9343  10310   4895  -2675   -640    331       C  
-ATOM   4954  O   VAL A 655      -2.381 -14.350 -29.992  1.00 63.95           O  
-ANISOU 4954  O   VAL A 655     9366  10268   4665  -2898   -666    233       O  
-ATOM   4955  CB  VAL A 655      -2.289 -12.202 -27.997  1.00 62.37           C  
-ANISOU 4955  CB  VAL A 655     8684  10033   4980  -2391   -733    415       C  
-ATOM   4956  CG1 VAL A 655      -1.045 -12.964 -27.575  1.00 60.99           C  
-ANISOU 4956  CG1 VAL A 655     8721   9539   4915  -2348   -584    278       C  
-ATOM   4957  CG2 VAL A 655      -2.350 -10.864 -27.295  1.00 59.08           C  
-ANISOU 4957  CG2 VAL A 655     8020   9637   4791  -2136   -777    527       C  
-ATOM   4958  N   TYR A 656      -0.706 -13.176 -30.914  1.00 61.83           N  
-ANISOU 4958  N   TYR A 656     9133   9801   4558  -2598   -518    312       N  
-ATOM   4959  CA  TYR A 656      -0.173 -14.337 -31.597  1.00 62.69           C  
-ANISOU 4959  CA  TYR A 656     9536   9781   4501  -2758   -402    163       C  
-ATOM   4960  C   TYR A 656       1.248 -14.637 -31.140  1.00 59.93           C  
-ANISOU 4960  C   TYR A 656     9318   9104   4348  -2583   -228     68       C  
-ATOM   4961  O   TYR A 656       2.057 -13.732 -30.940  1.00 57.77           O  
-ANISOU 4961  O   TYR A 656     8933   8740   4277  -2356   -179    142       O  
-ATOM   4962  CB  TYR A 656      -0.239 -14.147 -33.116  1.00 67.93           C  
-ANISOU 4962  CB  TYR A 656    10279  10604   4929  -2870   -402    209       C  
-ATOM   4963  CG  TYR A 656       0.140 -15.378 -33.906  1.00 72.90           C  
-ANISOU 4963  CG  TYR A 656    11225  11132   5342  -3067   -287     37       C  
-ATOM   4964  CD1 TYR A 656      -0.757 -16.426 -34.070  1.00 75.98           C  
-ANISOU 4964  CD1 TYR A 656    11749  11622   5498  -3361   -348    -65       C  
-ATOM   4965  CD2 TYR A 656       1.392 -15.490 -34.491  1.00 74.91           C  
-ANISOU 4965  CD2 TYR A 656    11648  11192   5622  -2964   -110    -27       C  
-ATOM   4966  CE1 TYR A 656      -0.416 -17.554 -34.791  1.00 79.00           C  
-ANISOU 4966  CE1 TYR A 656    12449  11887   5682  -3546   -234   -238       C  
-ATOM   4967  CE2 TYR A 656       1.743 -16.613 -35.215  1.00 78.95           C  
-ANISOU 4967  CE2 TYR A 656    12460  11600   5936  -3126     11   -197       C  
-ATOM   4968  CZ  TYR A 656       0.835 -17.644 -35.361  1.00 80.41           C  
-ANISOU 4968  CZ  TYR A 656    12799  11861   5894  -3416    -50   -308       C  
-ATOM   4969  OH  TYR A 656       1.176 -18.767 -36.082  1.00 83.23           O  
-ANISOU 4969  OH  TYR A 656    13481  12090   6051  -3582     79   -493       O  
-ATOM   4970  N   PHE A 657       1.527 -15.922 -30.961  1.00 68.91           N  
-ANISOU 4970  N   PHE A 657    10690  10068   5423  -2694   -139    -91       N  
-ATOM   4971  CA  PHE A 657       2.843 -16.399 -30.573  1.00 68.46           C  
-ANISOU 4971  CA  PHE A 657    10774   9709   5527  -2536     29   -185       C  
-ATOM   4972  C   PHE A 657       3.049 -17.789 -31.165  1.00 74.63           C  
-ANISOU 4972  C   PHE A 657    11883  10353   6120  -2709    142   -354       C  
-ATOM   4973  O   PHE A 657       2.316 -18.720 -30.834  1.00 74.63           O  
-ANISOU 4973  O   PHE A 657    12000  10346   6011  -2905     95   -433       O  
-ATOM   4974  CB  PHE A 657       2.950 -16.479 -29.049  1.00 60.47           C  
-ANISOU 4974  CB  PHE A 657     9660   8572   4744  -2413      7   -189       C  
-ATOM   4975  CG  PHE A 657       3.547 -15.253 -28.400  1.00 49.42           C  
-ANISOU 4975  CG  PHE A 657     8024   7150   3604  -2155     -2    -81       C  
-ATOM   4976  CD1 PHE A 657       4.828 -14.836 -28.723  1.00 46.15           C  
-ANISOU 4976  CD1 PHE A 657     7624   6598   3314  -1974    126    -70       C  
-ATOM   4977  CD2 PHE A 657       2.842 -14.550 -27.428  1.00 43.88           C  
-ANISOU 4977  CD2 PHE A 657     7090   6562   3020  -2100   -130      1       C  
-ATOM   4978  CE1 PHE A 657       5.386 -13.719 -28.113  1.00 41.04           C  
-ANISOU 4978  CE1 PHE A 657     6770   5923   2899  -1767    116     21       C  
-ATOM   4979  CE2 PHE A 657       3.393 -13.439 -26.816  1.00 39.79           C  
-ANISOU 4979  CE2 PHE A 657     6381   6004   2735  -1878   -133     81       C  
-ATOM   4980  CZ  PHE A 657       4.666 -13.022 -27.157  1.00 38.25           C  
-ANISOU 4980  CZ  PHE A 657     6210   5665   2659  -1722    -14     91       C  
-ATOM   4981  N   GLU A 658       4.036 -17.932 -32.046  1.00 74.44           N  
-ANISOU 4981  N   GLU A 658    12014  10217   6054  -2643    297   -410       N  
-ATOM   4982  CA  GLU A 658       4.382 -19.247 -32.588  1.00 83.85           C  
-ANISOU 4982  CA  GLU A 658    13538  11233   7087  -2766    437   -589       C  
-ATOM   4983  C   GLU A 658       5.875 -19.543 -32.452  1.00 84.45           C  
-ANISOU 4983  C   GLU A 658    13720  11036   7332  -2526    641   -655       C  
-ATOM   4984  O   GLU A 658       6.693 -18.628 -32.378  1.00 82.40           O  
-ANISOU 4984  O   GLU A 658    13286  10777   7246  -2306    684   -561       O  
-ATOM   4985  CB  GLU A 658       3.945 -19.385 -34.046  1.00 92.66           C  
-ANISOU 4985  CB  GLU A 658    14795  12520   7892  -2985    438   -631       C  
-ATOM   4986  CG  GLU A 658       3.983 -20.819 -34.566  1.00106.10           C  
-ANISOU 4986  CG  GLU A 658    16864  14061   9390  -3178    554   -837       C  
-ATOM   4987  CD  GLU A 658       2.688 -21.568 -34.327  1.00113.21           C  
-ANISOU 4987  CD  GLU A 658    17847  15050  10116  -3486    418   -892       C  
-ATOM   4988  OE1 GLU A 658       1.611 -20.977 -34.549  1.00118.02           O  
-ANISOU 4988  OE1 GLU A 658    18273  15966  10603  -3641    238   -785       O  
-ATOM   4989  OE2 GLU A 658       2.744 -22.747 -33.916  1.00116.67           O  
-ANISOU 4989  OE2 GLU A 658    18531  15255  10542  -3574    491  -1034       O  
-ATOM   4990  N   LYS A 659       6.217 -20.830 -32.435  1.00 92.99           N  
-ANISOU 4990  N   LYS A 659    15088  11886   8359  -2573    767   -815       N  
-ATOM   4991  CA  LYS A 659       7.559 -21.288 -32.075  1.00 94.62           C  
-ANISOU 4991  CA  LYS A 659    15389  11818   8745  -2328    955   -876       C  
-ATOM   4992  C   LYS A 659       8.676 -20.795 -32.999  1.00 93.99           C  
-ANISOU 4992  C   LYS A 659    15298  11741   8673  -2163   1114   -871       C  
-ATOM   4993  O   LYS A 659       9.682 -20.266 -32.526  1.00 93.91           O  
-ANISOU 4993  O   LYS A 659    15129  11663   8888  -1911   1182   -802       O  
-ATOM   4994  CB  LYS A 659       7.586 -22.817 -31.960  1.00103.58           C  
-ANISOU 4994  CB  LYS A 659    16864  12695   9797  -2421   1059  -1047       C  
-ATOM   4995  CG  LYS A 659       8.925 -23.400 -31.527  1.00111.67           C  
-ANISOU 4995  CG  LYS A 659    17991  13427  11010  -2148   1252  -1102       C  
-ATOM   4996  CD  LYS A 659       8.794 -24.877 -31.189  1.00122.77           C  
-ANISOU 4996  CD  LYS A 659    19724  14558  12365  -2234   1325  -1243       C  
-ATOM   4997  CE  LYS A 659      10.153 -25.539 -31.030  1.00130.83           C  
-ANISOU 4997  CE  LYS A 659    20886  15290  13535  -1952   1544  -1308       C  
-ATOM   4998  NZ  LYS A 659      10.937 -25.505 -32.299  1.00137.90           N  
-ANISOU 4998  NZ  LYS A 659    21891  16184  14319  -1877   1731  -1397       N  
-ATOM   4999  N   ASP A 660       8.515 -20.969 -34.306  1.00 84.34           N  
-ANISOU 4999  N   ASP A 660    14240  10611   7196  -2316   1174   -944       N  
-ATOM   5000  CA  ASP A 660       9.550 -20.523 -35.233  1.00 83.46           C  
-ANISOU 5000  CA  ASP A 660    14123  10523   7066  -2177   1335   -939       C  
-ATOM   5001  C   ASP A 660       9.071 -19.413 -36.158  1.00 82.13           C  
-ANISOU 5001  C   ASP A 660    13801  10650   6753  -2282   1236   -815       C  
-ATOM   5002  O   ASP A 660       9.762 -19.039 -37.099  1.00 83.74           O  
-ANISOU 5002  O   ASP A 660    14018  10915   6883  -2225   1358   -805       O  
-ATOM   5003  CB  ASP A 660      10.106 -21.698 -36.038  1.00 85.17           C  
-ANISOU 5003  CB  ASP A 660    14682  10561   7116  -2206   1550  -1141       C  
-ATOM   5004  CG  ASP A 660      10.855 -22.693 -35.171  1.00 87.09           C  
-ANISOU 5004  CG  ASP A 660    15064  10487   7541  -2024   1683  -1237       C  
-ATOM   5005  OD1 ASP A 660      10.720 -23.912 -35.416  1.00 87.98           O  
-ANISOU 5005  OD1 ASP A 660    15498  10413   7517  -2129   1779  -1411       O  
-ATOM   5006  OD2 ASP A 660      11.573 -22.254 -34.245  1.00 84.47           O  
-ANISOU 5006  OD2 ASP A 660    14523  10089   7483  -1781   1688  -1136       O  
-ATOM   5007  N   LYS A 661       7.887 -18.884 -35.878  1.00 79.39           N  
-ANISOU 5007  N   LYS A 661    13303  10495   6368  -2427   1018   -710       N  
-ATOM   5008  CA  LYS A 661       7.343 -17.778 -36.652  1.00 77.41           C  
-ANISOU 5008  CA  LYS A 661    12886  10528   5999  -2507    901   -560       C  
-ATOM   5009  C   LYS A 661       7.475 -16.462 -35.882  1.00 71.79           C  
-ANISOU 5009  C   LYS A 661    11848   9876   5553  -2316    799   -365       C  
-ATOM   5010  O   LYS A 661       8.155 -15.536 -36.328  1.00 70.58           O  
-ANISOU 5010  O   LYS A 661    11575   9776   5466  -2190    852   -257       O  
-ATOM   5011  CB  LYS A 661       5.876 -18.035 -36.998  1.00 83.46           C  
-ANISOU 5011  CB  LYS A 661    13695  11503   6514  -2802    725   -564       C  
-ATOM   5012  CG  LYS A 661       5.487 -19.500 -37.035  1.00 91.64           C  
-ANISOU 5012  CG  LYS A 661    15032  12409   7377  -3008    770   -770       C  
-ATOM   5013  CD  LYS A 661       5.840 -20.182 -38.341  1.00102.87           C  
-ANISOU 5013  CD  LYS A 661    16745  13817   8525  -3139    925   -923       C  
-ATOM   5014  CE  LYS A 661       4.618 -20.894 -38.919  1.00110.73           C  
-ANISOU 5014  CE  LYS A 661    17913  14963   9196  -3502    815  -1017       C  
-ATOM   5015  NZ  LYS A 661       3.925 -21.736 -37.901  1.00114.38           N  
-ANISOU 5015  NZ  LYS A 661    18444  15301   9715  -3622    733  -1090       N  
-ATOM   5016  N   GLN A 662       6.830 -16.379 -34.722  1.00 77.38           N  
-ANISOU 5016  N   GLN A 662    12421  10571   6407  -2303    660   -324       N  
-ATOM   5017  CA  GLN A 662       6.827 -15.144 -33.937  1.00 71.97           C  
-ANISOU 5017  CA  GLN A 662    11443   9941   5962  -2138    555   -158       C  
-ATOM   5018  C   GLN A 662       6.906 -15.398 -32.430  1.00 67.39           C  
-ANISOU 5018  C   GLN A 662    10783   9206   5618  -2026    522   -184       C  
-ATOM   5019  O   GLN A 662       6.002 -15.988 -31.839  1.00 66.38           O  
-ANISOU 5019  O   GLN A 662    10684   9097   5441  -2152    422   -229       O  
-ATOM   5020  CB  GLN A 662       5.581 -14.321 -34.251  1.00 71.15           C  
-ANISOU 5020  CB  GLN A 662    11180  10106   5747  -2258    361    -17       C  
-ATOM   5021  CG  GLN A 662       5.313 -14.117 -35.726  1.00 72.36           C  
-ANISOU 5021  CG  GLN A 662    11410  10453   5629  -2401    361     25       C  
-ATOM   5022  CD  GLN A 662       4.172 -13.153 -35.960  1.00 73.39           C  
-ANISOU 5022  CD  GLN A 662    11341  10855   5688  -2465    164    203       C  
-ATOM   5023  OE1 GLN A 662       4.108 -12.094 -35.338  1.00 72.49           O  
-ANISOU 5023  OE1 GLN A 662    11002  10757   5783  -2305     86    345       O  
-ATOM   5024  NE2 GLN A 662       3.252 -13.520 -36.845  1.00 74.29           N  
-ANISOU 5024  NE2 GLN A 662    11537  11186   5505  -2699     81    196       N  
-ATOM   5025  N   MET A 663       7.989 -14.935 -31.816  1.00 74.65           N  
-ANISOU 5025  N   MET A 663    11593   9989   6782  -1803    602   -150       N  
-ATOM   5026  CA  MET A 663       8.239 -15.179 -30.403  1.00 70.66           C  
-ANISOU 5026  CA  MET A 663    11015   9338   6495  -1684    584   -175       C  
-ATOM   5027  C   MET A 663       8.575 -13.893 -29.662  1.00 65.98           C  
-ANISOU 5027  C   MET A 663    10156   8771   6144  -1514    523    -47       C  
-ATOM   5028  O   MET A 663       8.696 -13.890 -28.435  1.00 65.24           O  
-ANISOU 5028  O   MET A 663     9965   8596   6229  -1420    483    -50       O  
-ATOM   5029  CB  MET A 663       9.382 -16.179 -30.225  1.00 74.50           C  
-ANISOU 5029  CB  MET A 663    11667   9594   7045  -1575    763   -292       C  
-ATOM   5030  CG  MET A 663       9.000 -17.619 -30.513  1.00 80.26           C  
-ANISOU 5030  CG  MET A 663    12684  10225   7587  -1729    818   -442       C  
-ATOM   5031  SD  MET A 663       7.828 -18.292 -29.308  1.00 84.22           S  
-ANISOU 5031  SD  MET A 663    13198  10709   8091  -1865    664   -468       S  
-ATOM   5032  CE  MET A 663       8.890 -19.343 -28.330  1.00 87.19           C  
-ANISOU 5032  CE  MET A 663    13703  10784   8643  -1690    799   -550       C  
-ATOM   5033  N   PHE A 664       8.725 -12.805 -30.409  1.00 58.17           N  
-ANISOU 5033  N   PHE A 664     9061   7890   5152  -1483    516     65       N  
-ATOM   5034  CA  PHE A 664       9.035 -11.506 -29.827  1.00 53.74           C  
-ANISOU 5034  CA  PHE A 664     8271   7339   4810  -1340    462    186       C  
-ATOM   5035  C   PHE A 664       8.121 -10.447 -30.439  1.00 52.95           C  
-ANISOU 5035  C   PHE A 664     8061   7424   4632  -1400    339    323       C  
-ATOM   5036  O   PHE A 664       7.703 -10.576 -31.582  1.00 55.51           O  
-ANISOU 5036  O   PHE A 664     8480   7870   4740  -1522    338    345       O  
-ATOM   5037  CB  PHE A 664      10.495 -11.170 -30.105  1.00 49.75           C  
-ANISOU 5037  CB  PHE A 664     7746   6732   4425  -1204    616    201       C  
-ATOM   5038  CG  PHE A 664      11.092 -10.172 -29.159  1.00 46.41           C  
-ANISOU 5038  CG  PHE A 664     7119   6250   4263  -1056    588    274       C  
-ATOM   5039  CD1 PHE A 664      11.969 -10.585 -28.172  1.00 45.63           C  
-ANISOU 5039  CD1 PHE A 664     6987   6017   4332   -941    649    210       C  
-ATOM   5040  CD2 PHE A 664      10.805  -8.822 -29.273  1.00 44.88           C  
-ANISOU 5040  CD2 PHE A 664     6776   6132   4144  -1035    504    408       C  
-ATOM   5041  CE1 PHE A 664      12.541  -9.677 -27.306  1.00 43.31           C  
-ANISOU 5041  CE1 PHE A 664     6510   5683   4263   -829    621    266       C  
-ATOM   5042  CE2 PHE A 664      11.374  -7.905 -28.407  1.00 43.18           C  
-ANISOU 5042  CE2 PHE A 664     6396   5845   4164   -919    485    458       C  
-ATOM   5043  CZ  PHE A 664      12.244  -8.334 -27.420  1.00 42.37           C  
-ANISOU 5043  CZ  PHE A 664     6258   5627   4215   -826    541    381       C  
-ATOM   5044  N   HIS A 665       7.802  -9.405 -29.685  1.00 42.96           N  
-ANISOU 5044  N   HIS A 665     6603   6182   3538  -1309    234    417       N  
-ATOM   5045  CA  HIS A 665       6.928  -8.359 -30.194  1.00 42.16           C  
-ANISOU 5045  CA  HIS A 665     6392   6241   3387  -1331    117    563       C  
-ATOM   5046  C   HIS A 665       7.363  -6.992 -29.699  1.00 42.54           C  
-ANISOU 5046  C   HIS A 665     6270   6222   3671  -1174     98    671       C  
-ATOM   5047  O   HIS A 665       7.266  -6.696 -28.504  1.00 41.42           O  
-ANISOU 5047  O   HIS A 665     6016   6015   3706  -1088     46    647       O  
-ATOM   5048  CB  HIS A 665       5.480  -8.592 -29.764  1.00 41.75           C  
-ANISOU 5048  CB  HIS A 665     6283   6336   3244  -1420    -36    562       C  
-ATOM   5049  CG  HIS A 665       4.859  -9.822 -30.345  1.00 43.75           C  
-ANISOU 5049  CG  HIS A 665     6701   6682   3240  -1617    -42    471       C  
-ATOM   5050  ND1 HIS A 665       4.332  -9.857 -31.618  1.00 46.27           N  
-ANISOU 5050  ND1 HIS A 665     7089   7173   3319  -1754    -70    525       N  
-ATOM   5051  CD2 HIS A 665       4.656 -11.055 -29.820  1.00 43.26           C  
-ANISOU 5051  CD2 HIS A 665     6756   6565   3116  -1714    -27    331       C  
-ATOM   5052  CE1 HIS A 665       3.845 -11.062 -31.858  1.00 47.94           C  
-ANISOU 5052  CE1 HIS A 665     7457   7429   3328  -1938    -71    408       C  
-ATOM   5053  NE2 HIS A 665       4.023 -11.806 -30.782  1.00 45.94           N  
-ANISOU 5053  NE2 HIS A 665     7241   7029   3184  -1917    -43    291       N  
-ATOM   5054  N   ILE A 666       7.833  -6.152 -30.616  1.00 48.00           N  
-ANISOU 5054  N   ILE A 666     6952   6927   4357  -1150    142    790       N  
-ATOM   5055  CA  ILE A 666       8.121  -4.763 -30.281  1.00 48.93           C  
-ANISOU 5055  CA  ILE A 666     6931   6979   4682  -1027    115    910       C  
-ATOM   5056  C   ILE A 666       6.858  -3.935 -30.466  1.00 50.36           C  
-ANISOU 5056  C   ILE A 666     7018   7293   4822  -1019    -33   1045       C  
-ATOM   5057  O   ILE A 666       6.293  -3.888 -31.557  1.00 51.72           O  
-ANISOU 5057  O   ILE A 666     7232   7617   4801  -1099    -70   1140       O  
-ATOM   5058  CB  ILE A 666       9.249  -4.186 -31.134  1.00 48.96           C  
-ANISOU 5058  CB  ILE A 666     6966   6925   4713  -1008    235    992       C  
-ATOM   5059  CG1 ILE A 666      10.553  -4.932 -30.851  1.00 48.37           C  
-ANISOU 5059  CG1 ILE A 666     6946   6728   4705   -984    386    866       C  
-ATOM   5060  CG2 ILE A 666       9.411  -2.700 -30.855  1.00 47.89           C  
-ANISOU 5060  CG2 ILE A 666     6706   6713   4778   -909    194   1129       C  
-ATOM   5061  CD1 ILE A 666      11.536  -4.890 -32.010  1.00 50.90           C  
-ANISOU 5061  CD1 ILE A 666     7341   7059   4940  -1014    531    911       C  
-ATOM   5062  N   ILE A 667       6.415  -3.294 -29.389  1.00 51.62           N  
-ANISOU 5062  N   ILE A 667     7047   7408   5160   -916   -115   1053       N  
-ATOM   5063  CA  ILE A 667       5.185  -2.514 -29.408  1.00 55.13           C  
-ANISOU 5063  CA  ILE A 667     7382   7975   5591   -871   -251   1174       C  
-ATOM   5064  C   ILE A 667       5.471  -1.026 -29.296  1.00 57.88           C  
-ANISOU 5064  C   ILE A 667     7647   8204   6139   -731   -257   1306       C  
-ATOM   5065  O   ILE A 667       5.873  -0.537 -28.242  1.00 56.57           O  
-ANISOU 5065  O   ILE A 667     7419   7886   6188   -635   -243   1248       O  
-ATOM   5066  CB  ILE A 667       4.254  -2.915 -28.260  1.00 53.51           C  
-ANISOU 5066  CB  ILE A 667     7087   7830   5415   -855   -341   1081       C  
-ATOM   5067  CG1 ILE A 667       4.013  -4.424 -28.275  1.00 53.67           C  
-ANISOU 5067  CG1 ILE A 667     7209   7934   5251  -1009   -330    946       C  
-ATOM   5068  CG2 ILE A 667       2.942  -2.145 -28.347  1.00 53.22           C  
-ANISOU 5068  CG2 ILE A 667     6920   7951   5351   -795   -473   1212       C  
-ATOM   5069  CD1 ILE A 667       2.981  -4.870 -27.289  1.00 54.26           C  
-ANISOU 5069  CD1 ILE A 667     7197   8105   5313  -1029   -423    876       C  
-ATOM   5070  N   THR A 668       5.254  -0.305 -30.389  1.00 63.33           N  
-ANISOU 5070  N   THR A 668     8349   8961   6751   -729   -280   1484       N  
-ATOM   5071  CA  THR A 668       5.520   1.124 -30.417  1.00 67.70           C  
-ANISOU 5071  CA  THR A 668     8855   9382   7485   -607   -281   1630       C  
-ATOM   5072  C   THR A 668       4.218   1.898 -30.553  1.00 70.00           C  
-ANISOU 5072  C   THR A 668     9049   9789   7760   -512   -413   1782       C  
-ATOM   5073  O   THR A 668       3.249   1.406 -31.124  1.00 71.41           O  
-ANISOU 5073  O   THR A 668     9207  10194   7731   -575   -497   1831       O  
-ATOM   5074  CB  THR A 668       6.471   1.488 -31.567  1.00 69.85           C  
-ANISOU 5074  CB  THR A 668     9221   9609   7709   -663   -186   1745       C  
-ATOM   5075  OG1 THR A 668       5.958   0.962 -32.797  1.00 72.21           O  
-ANISOU 5075  OG1 THR A 668     9583  10120   7732   -773   -212   1824       O  
-ATOM   5076  CG2 THR A 668       7.849   0.900 -31.314  1.00 68.92           C  
-ANISOU 5076  CG2 THR A 668     9166   9366   7653   -719    -44   1604       C  
-ATOM   5077  N   GLY A 669       4.201   3.111 -30.017  1.00 51.23           N  
-ANISOU 5077  N   GLY A 669     6610   7255   5601   -360   -431   1856       N  
-ATOM   5078  CA  GLY A 669       2.997   3.916 -30.017  1.00 54.13           C  
-ANISOU 5078  CA  GLY A 669     6874   7704   5988   -224   -545   1998       C  
-ATOM   5079  C   GLY A 669       3.087   5.036 -29.004  1.00 57.35           C  
-ANISOU 5079  C   GLY A 669     7231   7886   6673    -51   -538   1987       C  
-ATOM   5080  O   GLY A 669       4.057   5.119 -28.249  1.00 57.40           O  
-ANISOU 5080  O   GLY A 669     7275   7692   6842    -62   -456   1856       O  
-ATOM   5081  N   PRO A 670       2.067   5.905 -28.979  1.00 67.79           N  
-ANISOU 5081  N   PRO A 670     8467   9244   8046    111   -624   2123       N  
-ATOM   5082  CA  PRO A 670       2.035   7.076 -28.099  1.00 69.77           C  
-ANISOU 5082  CA  PRO A 670     8687   9268   8556    296   -614   2122       C  
-ATOM   5083  C   PRO A 670       1.797   6.705 -26.640  1.00 70.50           C  
-ANISOU 5083  C   PRO A 670     8699   9340   8746    339   -614   1898       C  
-ATOM   5084  O   PRO A 670       1.250   5.640 -26.341  1.00 69.22           O  
-ANISOU 5084  O   PRO A 670     8471   9387   8442    264   -654   1792       O  
-ATOM   5085  CB  PRO A 670       0.843   7.871 -28.631  1.00 71.90           C  
-ANISOU 5085  CB  PRO A 670     8875   9644   8798    464   -711   2341       C  
-ATOM   5086  CG  PRO A 670      -0.056   6.844 -29.208  1.00 69.84           C  
-ANISOU 5086  CG  PRO A 670     8534   9734   8269    368   -799   2369       C  
-ATOM   5087  CD  PRO A 670       0.847   5.795 -29.797  1.00 68.14           C  
-ANISOU 5087  CD  PRO A 670     8432   9564   7894    132   -736   2286       C  
-ATOM   5088  N   ASN A 671       2.222   7.580 -25.739  1.00 86.63           N  
-ANISOU 5088  N   ASN A 671    10760  11133  11024    445   -567   1826       N  
-ATOM   5089  CA  ASN A 671       1.945   7.391 -24.327  1.00 86.56           C  
-ANISOU 5089  CA  ASN A 671    10675  11106  11108    502   -567   1624       C  
-ATOM   5090  C   ASN A 671       0.436   7.349 -24.113  1.00 87.20           C  
-ANISOU 5090  C   ASN A 671    10609  11408  11115    634   -658   1664       C  
-ATOM   5091  O   ASN A 671      -0.299   8.140 -24.705  1.00 91.05           O  
-ANISOU 5091  O   ASN A 671    11057  11925  11611    780   -706   1849       O  
-ATOM   5092  CB  ASN A 671       2.582   8.512 -23.507  1.00 91.20           C  
-ANISOU 5092  CB  ASN A 671    11317  11383  11950    597   -506   1557       C  
-ATOM   5093  CG  ASN A 671       2.554   8.236 -22.020  1.00 91.24           C  
-ANISOU 5093  CG  ASN A 671    11265  11365  12036    615   -491   1323       C  
-ATOM   5094  OD1 ASN A 671       2.010   9.018 -21.242  1.00 91.87           O  
-ANISOU 5094  OD1 ASN A 671    11305  11357  12246    776   -495   1275       O  
-ATOM   5095  ND2 ASN A 671       3.138   7.114 -21.617  1.00 92.70           N  
-ANISOU 5095  ND2 ASN A 671    11451  11632  12139    457   -470   1177       N  
-ATOM   5096  N   MET A 672      -0.016   6.415 -23.280  1.00 69.74           N  
-ANISOU 5096  N   MET A 672     8311   9361   8825    581   -680   1502       N  
-ATOM   5097  CA  MET A 672      -1.443   6.205 -23.036  1.00 68.72           C  
-ANISOU 5097  CA  MET A 672     8019   9490   8600    672   -762   1526       C  
-ATOM   5098  C   MET A 672      -2.129   5.543 -24.227  1.00 67.81           C  
-ANISOU 5098  C   MET A 672     7861   9659   8243    574   -843   1678       C  
-ATOM   5099  O   MET A 672      -3.353   5.546 -24.334  1.00 69.28           O  
-ANISOU 5099  O   MET A 672     7899  10086   8338    654   -925   1762       O  
-ATOM   5100  CB  MET A 672      -2.140   7.524 -22.695  1.00 70.04           C  
-ANISOU 5100  CB  MET A 672     8114   9565   8933    937   -772   1605       C  
-ATOM   5101  CG  MET A 672      -1.615   8.212 -21.434  1.00 70.26           C  
-ANISOU 5101  CG  MET A 672     8184   9325   9185   1033   -695   1432       C  
-ATOM   5102  SD  MET A 672      -2.216   7.495 -19.881  1.00 68.60           S  
-ANISOU 5102  SD  MET A 672     7842   9272   8949   1033   -694   1190       S  
-ATOM   5103  CE  MET A 672      -1.269   5.972 -19.776  1.00 66.31           C  
-ANISOU 5103  CE  MET A 672     7629   9046   8520    736   -677   1052       C  
-ATOM   5104  N   GLY A 673      -1.328   4.976 -25.120  1.00 91.97           N  
-ANISOU 5104  N   GLY A 673    11047  12705  11194    397   -817   1708       N  
-ATOM   5105  CA  GLY A 673      -1.850   4.328 -26.308  1.00 90.03           C  
-ANISOU 5105  CA  GLY A 673    10791  12716  10701    274   -885   1836       C  
-ATOM   5106  C   GLY A 673      -2.497   2.993 -25.995  1.00 85.85           C  
-ANISOU 5106  C   GLY A 673    10197  12442   9980    116   -932   1714       C  
-ATOM   5107  O   GLY A 673      -3.378   2.536 -26.727  1.00 86.12           O  
-ANISOU 5107  O   GLY A 673    10163  12752   9806     38  -1018   1811       O  
-ATOM   5108  N   GLY A 674      -2.053   2.367 -24.908  1.00 59.89           N  
-ANISOU 5108  N   GLY A 674     6933   9065   6757     56   -877   1507       N  
-ATOM   5109  CA  GLY A 674      -2.580   1.080 -24.495  1.00 54.70           C  
-ANISOU 5109  CA  GLY A 674     6238   8610   5936   -104   -910   1384       C  
-ATOM   5110  C   GLY A 674      -1.566  -0.046 -24.587  1.00 50.68           C  
-ANISOU 5110  C   GLY A 674     5894   8009   5354   -302   -839   1254       C  
-ATOM   5111  O   GLY A 674      -1.918  -1.220 -24.446  1.00 50.18           O  
-ANISOU 5111  O   GLY A 674     5845   8090   5133   -465   -860   1164       O  
-ATOM   5112  N   LYS A 675      -0.305   0.308 -24.826  1.00 55.50           N  
-ANISOU 5112  N   LYS A 675     6630   8379   6079   -287   -750   1246       N  
-ATOM   5113  CA  LYS A 675       0.743  -0.694 -24.983  1.00 50.83           C  
-ANISOU 5113  CA  LYS A 675     6188   7695   5430   -441   -669   1136       C  
-ATOM   5114  C   LYS A 675       0.883  -1.533 -23.714  1.00 48.22           C  
-ANISOU 5114  C   LYS A 675     5852   7332   5139   -487   -646    951       C  
-ATOM   5115  O   LYS A 675       0.727  -2.755 -23.739  1.00 45.49           O  
-ANISOU 5115  O   LYS A 675     5565   7081   4639   -640   -648    872       O  
-ATOM   5116  CB  LYS A 675       2.081  -0.031 -25.312  1.00 48.18           C  
-ANISOU 5116  CB  LYS A 675     5949   7119   5238   -395   -574   1165       C  
-ATOM   5117  CG  LYS A 675       2.021   0.990 -26.430  1.00 46.63           C  
-ANISOU 5117  CG  LYS A 675     5761   6918   5039   -331   -589   1363       C  
-ATOM   5118  CD  LYS A 675       3.417   1.419 -26.851  1.00 44.38           C  
-ANISOU 5118  CD  LYS A 675     5585   6420   4858   -340   -483   1385       C  
-ATOM   5119  CE  LYS A 675       4.208   2.004 -25.686  1.00 42.81           C  
-ANISOU 5119  CE  LYS A 675     5367   5993   4907   -253   -428   1283       C  
-ATOM   5120  NZ  LYS A 675       3.637   3.290 -25.184  1.00 43.75           N  
-ANISOU 5120  NZ  LYS A 675     5402   6029   5192    -83   -476   1351       N  
-ATOM   5121  N   SER A 676       1.183  -0.862 -22.606  1.00 55.55           N  
-ANISOU 5121  N   SER A 676     6719   8119   6267   -360   -624    885       N  
-ATOM   5122  CA  SER A 676       1.365  -1.517 -21.317  1.00 53.15           C  
-ANISOU 5122  CA  SER A 676     6401   7782   6010   -388   -605    723       C  
-ATOM   5123  C   SER A 676       0.193  -2.450 -21.016  1.00 53.74           C  
-ANISOU 5123  C   SER A 676     6412   8090   5915   -486   -675    686       C  
-ATOM   5124  O   SER A 676       0.380  -3.640 -20.768  1.00 51.06           O  
-ANISOU 5124  O   SER A 676     6150   7771   5478   -625   -657    595       O  
-ATOM   5125  CB  SER A 676       1.511  -0.467 -20.217  1.00 52.91           C  
-ANISOU 5125  CB  SER A 676     6287   7624   6191   -229   -595    673       C  
-ATOM   5126  OG  SER A 676       2.217  -0.991 -19.108  1.00 51.41           O  
-ANISOU 5126  OG  SER A 676     6122   7344   6069   -264   -553    525       O  
-ATOM   5127  N   THR A 677      -1.018  -1.906 -21.053  1.00 51.54           N  
-ANISOU 5127  N   THR A 677     5992   7989   5602   -412   -752    766       N  
-ATOM   5128  CA  THR A 677      -2.216  -2.713 -20.876  1.00 51.26           C  
-ANISOU 5128  CA  THR A 677     5870   8215   5392   -520   -825    754       C  
-ATOM   5129  C   THR A 677      -2.195  -3.946 -21.766  1.00 52.56           C  
-ANISOU 5129  C   THR A 677     6162   8468   5342   -744   -832    752       C  
-ATOM   5130  O   THR A 677      -2.492  -5.044 -21.310  1.00 52.16           O  
-ANISOU 5130  O   THR A 677     6140   8498   5180   -894   -841    663       O  
-ATOM   5131  CB  THR A 677      -3.484  -1.918 -21.192  1.00 51.89           C  
-ANISOU 5131  CB  THR A 677     5771   8506   5438   -410   -910    885       C  
-ATOM   5132  OG1 THR A 677      -3.588  -0.810 -20.291  1.00 51.42           O  
-ANISOU 5132  OG1 THR A 677     5604   8356   5576   -192   -892    867       O  
-ATOM   5133  CG2 THR A 677      -4.713  -2.806 -21.058  1.00 49.09           C  
-ANISOU 5133  CG2 THR A 677     5311   8456   4886   -552   -987    877       C  
-ATOM   5134  N   TYR A 678      -1.850  -3.768 -23.037  1.00 58.00           N  
-ANISOU 5134  N   TYR A 678     6937   9136   5965   -773   -824    849       N  
-ATOM   5135  CA  TYR A 678      -1.851  -4.884 -23.976  1.00 57.42           C  
-ANISOU 5135  CA  TYR A 678     6999   9148   5670   -987   -824    839       C  
-ATOM   5136  C   TYR A 678      -0.954  -6.021 -23.495  1.00 55.48           C  
-ANISOU 5136  C   TYR A 678     6917   8738   5423  -1098   -739    685       C  
-ATOM   5137  O   TYR A 678      -1.387  -7.167 -23.437  1.00 53.98           O  
-ANISOU 5137  O   TYR A 678     6793   8641   5076  -1276   -756    616       O  
-ATOM   5138  CB  TYR A 678      -1.457  -4.426 -25.385  1.00 58.61           C  
-ANISOU 5138  CB  TYR A 678     7228   9284   5758   -987   -811    962       C  
-ATOM   5139  CG  TYR A 678      -1.348  -5.551 -26.399  1.00 57.38           C  
-ANISOU 5139  CG  TYR A 678     7237   9198   5366  -1209   -794    931       C  
-ATOM   5140  CD1 TYR A 678      -2.480  -6.204 -26.871  1.00 59.01           C  
-ANISOU 5140  CD1 TYR A 678     7412   9670   5339  -1383   -887    955       C  
-ATOM   5141  CD2 TYR A 678      -0.110  -5.952 -26.891  1.00 56.58           C  
-ANISOU 5141  CD2 TYR A 678     7321   8905   5271  -1248   -679    873       C  
-ATOM   5142  CE1 TYR A 678      -2.375  -7.232 -27.801  1.00 61.08           C  
-ANISOU 5142  CE1 TYR A 678     7848   9983   5376  -1602   -867    908       C  
-ATOM   5143  CE2 TYR A 678       0.001  -6.977 -27.813  1.00 57.71           C  
-ANISOU 5143  CE2 TYR A 678     7633   9097   5197  -1441   -648    826       C  
-ATOM   5144  CZ  TYR A 678      -1.133  -7.612 -28.265  1.00 60.14           C  
-ANISOU 5144  CZ  TYR A 678     7931   9650   5271  -1622   -742    838       C  
-ATOM   5145  OH  TYR A 678      -1.028  -8.629 -29.185  1.00 60.60           O  
-ANISOU 5145  OH  TYR A 678     8177   9745   5102  -1829   -708    775       O  
-ATOM   5146  N   ILE A 679       0.286  -5.709 -23.138  1.00 51.57           N  
-ANISOU 5146  N   ILE A 679     6488   8001   5104   -994   -647    638       N  
-ATOM   5147  CA  ILE A 679       1.207  -6.751 -22.704  1.00 49.86           C  
-ANISOU 5147  CA  ILE A 679     6416   7630   4898  -1068   -564    512       C  
-ATOM   5148  C   ILE A 679       0.796  -7.358 -21.358  1.00 49.44           C  
-ANISOU 5148  C   ILE A 679     6313   7605   4867  -1097   -590    414       C  
-ATOM   5149  O   ILE A 679       0.670  -8.571 -21.238  1.00 48.30           O  
-ANISOU 5149  O   ILE A 679     6275   7476   4600  -1247   -581    342       O  
-ATOM   5150  CB  ILE A 679       2.670  -6.255 -22.667  1.00 48.56           C  
-ANISOU 5150  CB  ILE A 679     6308   7232   4911   -952   -463    497       C  
-ATOM   5151  CG1 ILE A 679       2.842  -5.104 -21.677  1.00 46.23           C  
-ANISOU 5151  CG1 ILE A 679     5874   6858   4834   -783   -477    502       C  
-ATOM   5152  CG2 ILE A 679       3.105  -5.813 -24.043  1.00 49.32           C  
-ANISOU 5152  CG2 ILE A 679     6472   7311   4957   -954   -424    595       C  
-ATOM   5153  CD1 ILE A 679       4.260  -4.620 -21.566  1.00 43.53           C  
-ANISOU 5153  CD1 ILE A 679     5571   6306   4661   -699   -387    485       C  
-ATOM   5154  N   ARG A 680       0.577  -6.521 -20.351  1.00 50.51           N  
-ANISOU 5154  N   ARG A 680     6298   7741   5151   -961   -619    409       N  
-ATOM   5155  CA  ARG A 680       0.176  -7.019 -19.041  1.00 50.69           C  
-ANISOU 5155  CA  ARG A 680     6262   7811   5186   -986   -642    322       C  
-ATOM   5156  C   ARG A 680      -1.060  -7.885 -19.182  1.00 52.13           C  
-ANISOU 5156  C   ARG A 680     6426   8217   5163  -1159   -711    328       C  
-ATOM   5157  O   ARG A 680      -1.074  -9.028 -18.738  1.00 51.94           O  
-ANISOU 5157  O   ARG A 680     6494   8185   5054  -1298   -698    256       O  
-ATOM   5158  CB  ARG A 680      -0.093  -5.868 -18.076  1.00 51.89           C  
-ANISOU 5158  CB  ARG A 680     6244   7974   5499   -815   -666    319       C  
-ATOM   5159  CG  ARG A 680       1.121  -4.995 -17.806  1.00 54.61           C  
-ANISOU 5159  CG  ARG A 680     6606   8095   6048   -671   -603    300       C  
-ATOM   5160  CD  ARG A 680       0.908  -4.171 -16.559  1.00 58.51           C  
-ANISOU 5160  CD  ARG A 680     6969   8583   6679   -543   -618    244       C  
-ATOM   5161  NE  ARG A 680      -0.404  -3.536 -16.565  1.00 64.09           N  
-ANISOU 5161  NE  ARG A 680     7528   9471   7351   -476   -681    299       N  
-ATOM   5162  CZ  ARG A 680      -0.605  -2.245 -16.798  1.00 67.78           C  
-ANISOU 5162  CZ  ARG A 680     7919   9903   7933   -315   -689    363       C  
-ATOM   5163  NH1 ARG A 680      -1.838  -1.750 -16.789  1.00 69.78           N  
-ANISOU 5163  NH1 ARG A 680     8027  10338   8149   -236   -743    419       N  
-ATOM   5164  NH2 ARG A 680       0.429  -1.450 -17.034  1.00 69.85           N  
-ANISOU 5164  NH2 ARG A 680     8246   9947   8346   -233   -638    376       N  
-ATOM   5165  N   GLN A 681      -2.092  -7.338 -19.814  1.00 55.14           N  
-ANISOU 5165  N   GLN A 681     6687   8801   5463  -1156   -785    423       N  
-ATOM   5166  CA  GLN A 681      -3.311  -8.086 -20.087  1.00 57.43           C  
-ANISOU 5166  CA  GLN A 681     6936   9344   5540  -1341   -861    444       C  
-ATOM   5167  C   GLN A 681      -2.993  -9.479 -20.615  1.00 55.70           C  
-ANISOU 5167  C   GLN A 681     6936   9067   5160  -1567   -828    383       C  
-ATOM   5168  O   GLN A 681      -3.633 -10.454 -20.231  1.00 55.05           O  
-ANISOU 5168  O   GLN A 681     6879   9091   4948  -1747   -858    335       O  
-ATOM   5169  CB  GLN A 681      -4.185  -7.323 -21.082  1.00 63.93           C  
-ANISOU 5169  CB  GLN A 681     7632  10375   6283  -1307   -940    581       C  
-ATOM   5170  CG  GLN A 681      -4.850  -8.178 -22.150  1.00 71.81           C  
-ANISOU 5170  CG  GLN A 681     8696  11563   7026  -1543   -996    618       C  
-ATOM   5171  CD  GLN A 681      -5.472  -7.335 -23.252  1.00 77.56           C  
-ANISOU 5171  CD  GLN A 681     9311  12476   7683  -1488  -1071    774       C  
-ATOM   5172  OE1 GLN A 681      -5.291  -6.116 -23.292  1.00 79.84           O  
-ANISOU 5172  OE1 GLN A 681     9503  12707   8127  -1262  -1068    859       O  
-ATOM   5173  NE2 GLN A 681      -6.209  -7.981 -24.152  1.00 81.68           N  
-ANISOU 5173  NE2 GLN A 681     9852  13219   7962  -1701  -1141    816       N  
-ATOM   5174  N   THR A 682      -1.994  -9.571 -21.486  1.00 54.99           N  
-ANISOU 5174  N   THR A 682     7011   8802   5079  -1559   -759    381       N  
-ATOM   5175  CA  THR A 682      -1.596 -10.854 -22.051  1.00 54.62           C  
-ANISOU 5175  CA  THR A 682     7197   8668   4889  -1747   -706    309       C  
-ATOM   5176  C   THR A 682      -1.127 -11.792 -20.955  1.00 53.53           C  
-ANISOU 5176  C   THR A 682     7158   8377   4803  -1784   -654    203       C  
-ATOM   5177  O   THR A 682      -1.534 -12.951 -20.902  1.00 54.01           O  
-ANISOU 5177  O   THR A 682     7339   8463   4718  -1983   -660    148       O  
-ATOM   5178  CB  THR A 682      -0.460 -10.699 -23.076  1.00 55.44           C  
-ANISOU 5178  CB  THR A 682     7449   8599   5018  -1691   -616    318       C  
-ATOM   5179  OG1 THR A 682      -0.769  -9.638 -23.987  1.00 55.44           O  
-ANISOU 5179  OG1 THR A 682     7344   8718   5001  -1620   -662    439       O  
-ATOM   5180  CG2 THR A 682      -0.261 -11.997 -23.850  1.00 55.13           C  
-ANISOU 5180  CG2 THR A 682     7650   8505   4790  -1893   -563    243       C  
-ATOM   5181  N   GLY A 683      -0.264 -11.286 -20.083  1.00 55.80           N  
-ANISOU 5181  N   GLY A 683     7399   8505   5296  -1602   -605    179       N  
-ATOM   5182  CA  GLY A 683       0.223 -12.073 -18.966  1.00 53.35           C  
-ANISOU 5182  CA  GLY A 683     7161   8063   5045  -1612   -564     99       C  
-ATOM   5183  C   GLY A 683      -0.912 -12.561 -18.087  1.00 52.16           C  
-ANISOU 5183  C   GLY A 683     6929   8085   4805  -1737   -637     84       C  
-ATOM   5184  O   GLY A 683      -0.952 -13.723 -17.691  1.00 53.20           O  
-ANISOU 5184  O   GLY A 683     7195   8163   4854  -1880   -620     33       O  
-ATOM   5185  N   VAL A 684      -1.842 -11.664 -17.786  1.00 46.67           N  
-ANISOU 5185  N   VAL A 684     6013   7595   4124  -1680   -713    134       N  
-ATOM   5186  CA  VAL A 684      -2.976 -11.997 -16.939  1.00 46.86           C  
-ANISOU 5186  CA  VAL A 684     5919   7824   4062  -1787   -777    128       C  
-ATOM   5187  C   VAL A 684      -3.752 -13.191 -17.488  1.00 50.34           C  
-ANISOU 5187  C   VAL A 684     6473   8380   4275  -2065   -811    123       C  
-ATOM   5188  O   VAL A 684      -4.121 -14.098 -16.747  1.00 52.41           O  
-ANISOU 5188  O   VAL A 684     6781   8669   4462  -2215   -818     84       O  
-ATOM   5189  CB  VAL A 684      -3.930 -10.804 -16.787  1.00 45.58           C  
-ANISOU 5189  CB  VAL A 684     5494   7891   3934  -1668   -846    192       C  
-ATOM   5190  CG1 VAL A 684      -5.199 -11.232 -16.066  1.00 45.23           C  
-ANISOU 5190  CG1 VAL A 684     5313   8105   3766  -1802   -909    192       C  
-ATOM   5191  CG2 VAL A 684      -3.244  -9.667 -16.051  1.00 42.01           C  
-ANISOU 5191  CG2 VAL A 684     4945   7313   3704  -1415   -810    175       C  
-ATOM   5192  N   ILE A 685      -3.997 -13.191 -18.791  1.00 47.21           N  
-ANISOU 5192  N   ILE A 685     6128   8050   3758  -2150   -833    162       N  
-ATOM   5193  CA  ILE A 685      -4.752 -14.269 -19.412  1.00 49.35           C  
-ANISOU 5193  CA  ILE A 685     6513   8440   3796  -2439   -871    149       C  
-ATOM   5194  C   ILE A 685      -4.013 -15.595 -19.266  1.00 49.48           C  
-ANISOU 5194  C   ILE A 685     6818   8205   3778  -2570   -789     56       C  
-ATOM   5195  O   ILE A 685      -4.629 -16.633 -19.040  1.00 50.56           O  
-ANISOU 5195  O   ILE A 685     7047   8393   3769  -2807   -811     23       O  
-ATOM   5196  CB  ILE A 685      -5.028 -13.986 -20.912  1.00 50.30           C  
-ANISOU 5196  CB  ILE A 685     6652   8676   3785  -2503   -908    206       C  
-ATOM   5197  CG1 ILE A 685      -5.553 -12.557 -21.103  1.00 51.42           C  
-ANISOU 5197  CG1 ILE A 685     6525   9015   3999  -2313   -976    319       C  
-ATOM   5198  CG2 ILE A 685      -5.986 -15.019 -21.489  1.00 51.14           C  
-ANISOU 5198  CG2 ILE A 685     6842   8959   3628  -2830   -967    190       C  
-ATOM   5199  CD1 ILE A 685      -6.609 -12.143 -20.087  1.00 51.63           C  
-ANISOU 5199  CD1 ILE A 685     6291   9277   4049  -2275  -1047    354       C  
-ATOM   5200  N   VAL A 686      -2.690 -15.556 -19.382  1.00 55.67           N  
-ANISOU 5200  N   VAL A 686     7741   8713   4697  -2412   -692     20       N  
-ATOM   5201  CA  VAL A 686      -1.885 -16.774 -19.357  1.00 56.73           C  
-ANISOU 5201  CA  VAL A 686     8156   8587   4812  -2491   -600    -59       C  
-ATOM   5202  C   VAL A 686      -1.888 -17.440 -17.985  1.00 56.66           C  
-ANISOU 5202  C   VAL A 686     8168   8507   4853  -2519   -595    -85       C  
-ATOM   5203  O   VAL A 686      -2.033 -18.659 -17.874  1.00 56.94           O  
-ANISOU 5203  O   VAL A 686     8404   8451   4780  -2709   -572   -129       O  
-ATOM   5204  CB  VAL A 686      -0.434 -16.496 -19.779  1.00 55.83           C  
-ANISOU 5204  CB  VAL A 686     8146   8224   4841  -2287   -493    -79       C  
-ATOM   5205  CG1 VAL A 686       0.384 -17.783 -19.737  1.00 55.05           C  
-ANISOU 5205  CG1 VAL A 686     8332   7858   4727  -2340   -389   -157       C  
-ATOM   5206  CG2 VAL A 686      -0.404 -15.873 -21.161  1.00 56.75           C  
-ANISOU 5206  CG2 VAL A 686     8258   8412   4892  -2274   -491    -45       C  
-ATOM   5207  N   LEU A 687      -1.713 -16.636 -16.944  1.00 62.23           N  
-ANISOU 5207  N   LEU A 687     8680   9248   5718  -2334   -612    -58       N  
-ATOM   5208  CA  LEU A 687      -1.768 -17.144 -15.581  1.00 61.52           C  
-ANISOU 5208  CA  LEU A 687     8579   9132   5665  -2354   -616    -70       C  
-ATOM   5209  C   LEU A 687      -3.150 -17.716 -15.272  1.00 64.21           C  
-ANISOU 5209  C   LEU A 687     8869   9699   5827  -2606   -692    -56       C  
-ATOM   5210  O   LEU A 687      -3.264 -18.792 -14.694  1.00 65.74           O  
-ANISOU 5210  O   LEU A 687     9206   9819   5953  -2761   -679    -73       O  
-ATOM   5211  CB  LEU A 687      -1.381 -16.051 -14.584  1.00 58.53           C  
-ANISOU 5211  CB  LEU A 687     7989   8781   5470  -2118   -626    -54       C  
-ATOM   5212  CG  LEU A 687      -1.760 -16.267 -13.122  1.00 56.76           C  
-ANISOU 5212  CG  LEU A 687     7672   8637   5256  -2142   -655    -55       C  
-ATOM   5213  CD1 LEU A 687      -0.785 -15.547 -12.202  1.00 56.12           C  
-ANISOU 5213  CD1 LEU A 687     7503   8455   5366  -1909   -627    -68       C  
-ATOM   5214  CD2 LEU A 687      -3.171 -15.783 -12.886  1.00 54.82           C  
-ANISOU 5214  CD2 LEU A 687     7207   8707   4916  -2227   -736    -28       C  
-ATOM   5215  N   MET A 688      -4.198 -17.002 -15.670  1.00 55.87           N  
-ANISOU 5215  N   MET A 688     7609   8924   4696  -2647   -771    -14       N  
-ATOM   5216  CA  MET A 688      -5.556 -17.491 -15.472  1.00 59.87           C  
-ANISOU 5216  CA  MET A 688     8033   9693   5023  -2896   -846      7       C  
-ATOM   5217  C   MET A 688      -5.746 -18.888 -16.057  1.00 62.37           C  
-ANISOU 5217  C   MET A 688     8621   9920   5158  -3196   -833    -30       C  
-ATOM   5218  O   MET A 688      -6.244 -19.788 -15.388  1.00 64.45           O  
-ANISOU 5218  O   MET A 688     8952  10208   5329  -3398   -844    -37       O  
-ATOM   5219  CB  MET A 688      -6.575 -16.530 -16.079  1.00 61.33           C  
-ANISOU 5219  CB  MET A 688     7963  10194   5144  -2883   -931     69       C  
-ATOM   5220  CG  MET A 688      -6.618 -15.173 -15.411  1.00 62.22           C  
-ANISOU 5220  CG  MET A 688     7807  10412   5422  -2607   -946    104       C  
-ATOM   5221  SD  MET A 688      -7.978 -14.163 -16.031  1.00 63.43           S  
-ANISOU 5221  SD  MET A 688     7654  10955   5491  -2587  -1047    196       S  
-ATOM   5222  CE  MET A 688      -9.391 -15.139 -15.523  1.00 64.16           C  
-ANISOU 5222  CE  MET A 688     7659  11356   5361  -2910  -1113    208       C  
-ATOM   5223  N   ALA A 689      -5.352 -19.064 -17.310  1.00 65.38           N  
-ANISOU 5223  N   ALA A 689     9168  10192   5482  -3233   -804    -58       N  
-ATOM   5224  CA  ALA A 689      -5.441 -20.368 -17.948  1.00 68.15           C  
-ANISOU 5224  CA  ALA A 689     9811  10420   5661  -3509   -776   -116       C  
-ATOM   5225  C   ALA A 689      -4.856 -21.463 -17.059  1.00 67.79           C  
-ANISOU 5225  C   ALA A 689     9995  10101   5662  -3553   -703   -157       C  
-ATOM   5226  O   ALA A 689      -5.419 -22.547 -16.955  1.00 70.47           O  
-ANISOU 5226  O   ALA A 689    10497  10425   5854  -3832   -712   -180       O  
-ATOM   5227  CB  ALA A 689      -4.749 -20.345 -19.305  1.00 68.58           C  
-ANISOU 5227  CB  ALA A 689    10040  10331   5687  -3471   -720   -158       C  
-ATOM   5228  N   GLN A 690      -3.736 -21.171 -16.405  1.00 64.75           N  
-ANISOU 5228  N   GLN A 690     9619   9505   5479  -3282   -635   -156       N  
-ATOM   5229  CA  GLN A 690      -3.066 -22.165 -15.565  1.00 64.61           C  
-ANISOU 5229  CA  GLN A 690     9811   9220   5518  -3281   -566   -173       C  
-ATOM   5230  C   GLN A 690      -3.598 -22.203 -14.120  1.00 63.60           C  
-ANISOU 5230  C   GLN A 690     9534   9222   5410  -3313   -617   -121       C  
-ATOM   5231  O   GLN A 690      -3.224 -23.074 -13.327  1.00 63.19           O  
-ANISOU 5231  O   GLN A 690     9644   8987   5380  -3346   -577   -112       O  
-ATOM   5232  CB  GLN A 690      -1.545 -21.963 -15.605  1.00 61.74           C  
-ANISOU 5232  CB  GLN A 690     9540   8576   5344  -2989   -467   -191       C  
-ATOM   5233  CG  GLN A 690      -0.914 -22.415 -16.910  1.00 64.19           C  
-ANISOU 5233  CG  GLN A 690    10095   8687   5608  -3001   -381   -256       C  
-ATOM   5234  CD  GLN A 690       0.524 -21.954 -17.067  1.00 64.03           C  
-ANISOU 5234  CD  GLN A 690    10088   8466   5774  -2696   -288   -263       C  
-ATOM   5235  OE1 GLN A 690       0.802 -20.979 -17.767  1.00 64.42           O  
-ANISOU 5235  OE1 GLN A 690    10008   8595   5872  -2566   -287   -256       O  
-ATOM   5236  NE2 GLN A 690       1.447 -22.658 -16.422  1.00 64.60           N  
-ANISOU 5236  NE2 GLN A 690    10313   8286   5947  -2584   -211   -265       N  
-ATOM   5237  N   ILE A 691      -4.475 -21.259 -13.796  1.00 59.74           N  
-ANISOU 5237  N   ILE A 691     8738   9053   4908  -3297   -699    -81       N  
-ATOM   5238  CA  ILE A 691      -5.138 -21.232 -12.503  1.00 60.00           C  
-ANISOU 5238  CA  ILE A 691     8604   9267   4928  -3347   -745    -39       C  
-ATOM   5239  C   ILE A 691      -6.356 -22.141 -12.569  1.00 62.60           C  
-ANISOU 5239  C   ILE A 691     8985   9761   5040  -3710   -794    -26       C  
-ATOM   5240  O   ILE A 691      -6.934 -22.518 -11.547  1.00 65.39           O  
-ANISOU 5240  O   ILE A 691     9277  10231   5338  -3834   -818     10       O  
-ATOM   5241  CB  ILE A 691      -5.558 -19.800 -12.140  1.00 58.26           C  
-ANISOU 5241  CB  ILE A 691     8032   9316   4789  -3156   -797    -13       C  
-ATOM   5242  CG1 ILE A 691      -4.402 -19.073 -11.473  1.00 56.65           C  
-ANISOU 5242  CG1 ILE A 691     7777   8951   4798  -2844   -751    -23       C  
-ATOM   5243  CG2 ILE A 691      -6.753 -19.784 -11.208  1.00 59.60           C  
-ANISOU 5243  CG2 ILE A 691     7996   9791   4860  -3295   -856     24       C  
-ATOM   5244  CD1 ILE A 691      -4.846 -17.831 -10.753  1.00 55.42           C  
-ANISOU 5244  CD1 ILE A 691     7309   9029   4718  -2681   -791    -10       C  
-ATOM   5245  N   GLY A 692      -6.728 -22.508 -13.789  1.00 54.31           N  
-ANISOU 5245  N   GLY A 692     8055   8727   3855  -3896   -809    -57       N  
-ATOM   5246  CA  GLY A 692      -7.844 -23.403 -13.999  1.00 56.95           C  
-ANISOU 5246  CA  GLY A 692     8459   9212   3969  -4275   -858    -54       C  
-ATOM   5247  C   GLY A 692      -9.133 -22.636 -14.184  1.00 59.10           C  
-ANISOU 5247  C   GLY A 692     8397   9926   4134  -4364   -961     -7       C  
-ATOM   5248  O   GLY A 692     -10.213 -23.219 -14.212  1.00 63.03           O  
-ANISOU 5248  O   GLY A 692     8867  10639   4444  -4683  -1019     12       O  
-ATOM   5249  N   CYS A 693      -9.022 -21.320 -14.301  1.00 70.82           N  
-ANISOU 5249  N   CYS A 693     9624  11548   5738  -4081   -983     19       N  
-ATOM   5250  CA  CYS A 693     -10.183 -20.483 -14.559  1.00 71.95           C  
-ANISOU 5250  CA  CYS A 693     9438  12102   5799  -4105  -1075     75       C  
-ATOM   5251  C   CYS A 693     -10.324 -20.159 -16.052  1.00 74.75           C  
-ANISOU 5251  C   CYS A 693     9803  12529   6069  -4138  -1116     77       C  
-ATOM   5252  O   CYS A 693      -9.338 -20.121 -16.788  1.00 74.14           O  
-ANISOU 5252  O   CYS A 693     9919  12186   6063  -4017  -1059     35       O  
-ATOM   5253  CB  CYS A 693     -10.089 -19.194 -13.745  1.00 67.68           C  
-ANISOU 5253  CB  CYS A 693     8604  11678   5435  -3773  -1075    108       C  
-ATOM   5254  SG  CYS A 693     -11.338 -17.970 -14.176  1.00 65.02           S  
-ANISOU 5254  SG  CYS A 693     7863  11799   5044  -3699  -1171    185       S  
-ATOM   5255  N   PHE A 694     -11.556 -19.930 -16.493  1.00 63.88           N  
-ANISOU 5255  N   PHE A 694     8208  11532   4532  -4305  -1213    132       N  
-ATOM   5256  CA  PHE A 694     -11.804 -19.507 -17.863  1.00 66.75           C  
-ANISOU 5256  CA  PHE A 694     8534  12029   4800  -4329  -1270    157       C  
-ATOM   5257  C   PHE A 694     -11.167 -18.149 -18.103  1.00 64.29           C  
-ANISOU 5257  C   PHE A 694     8079  11666   4684  -3936  -1252    195       C  
-ATOM   5258  O   PHE A 694     -10.863 -17.425 -17.157  1.00 62.41           O  
-ANISOU 5258  O   PHE A 694     7695  11390   4629  -3673  -1219    208       O  
-ATOM   5259  CB  PHE A 694     -13.302 -19.445 -18.150  1.00 72.97           C  
-ANISOU 5259  CB  PHE A 694     9060  13282   5382  -4562  -1391    232       C  
-ATOM   5260  CG  PHE A 694     -13.921 -20.783 -18.435  1.00 80.13           C  
-ANISOU 5260  CG  PHE A 694    10152  14245   6049  -5016  -1423    191       C  
-ATOM   5261  CD1 PHE A 694     -13.155 -21.938 -18.416  1.00 82.96           C  
-ANISOU 5261  CD1 PHE A 694    10906  14221   6393  -5173  -1339     92       C  
-ATOM   5262  CD2 PHE A 694     -15.268 -20.884 -18.736  1.00 84.02           C  
-ANISOU 5262  CD2 PHE A 694    10424  15173   6328  -5288  -1537    255       C  
-ATOM   5263  CE1 PHE A 694     -13.725 -23.167 -18.682  1.00 87.15           C  
-ANISOU 5263  CE1 PHE A 694    11635  14773   6704  -5603  -1364     47       C  
-ATOM   5264  CE2 PHE A 694     -15.843 -22.107 -19.005  1.00 87.13           C  
-ANISOU 5264  CE2 PHE A 694    10994  15618   6493  -5737  -1570    212       C  
-ATOM   5265  CZ  PHE A 694     -15.071 -23.251 -18.978  1.00 88.54           C  
-ANISOU 5265  CZ  PHE A 694    11594  15384   6662  -5901  -1481    103       C  
-ATOM   5266  N   VAL A 695     -10.981 -17.805 -19.373  1.00 57.92           N  
-ANISOU 5266  N   VAL A 695     7319  10862   3825  -3911  -1274    213       N  
-ATOM   5267  CA  VAL A 695     -10.224 -16.612 -19.752  1.00 55.00           C  
-ANISOU 5267  CA  VAL A 695     6877  10385   3635  -3566  -1245    250       C  
-ATOM   5268  C   VAL A 695     -11.014 -15.651 -20.649  1.00 58.76           C  
-ANISOU 5268  C   VAL A 695     7107  11183   4037  -3506  -1344    364       C  
-ATOM   5269  O   VAL A 695     -11.818 -16.082 -21.470  1.00 59.00           O  
-ANISOU 5269  O   VAL A 695     7125  11449   3844  -3763  -1426    393       O  
-ATOM   5270  CB  VAL A 695      -8.912 -17.011 -20.453  1.00 51.89           C  
-ANISOU 5270  CB  VAL A 695     6807   9618   3289  -3525  -1148    174       C  
-ATOM   5271  CG1 VAL A 695      -7.915 -17.561 -19.435  1.00 48.71           C  
-ANISOU 5271  CG1 VAL A 695     6586   8881   3041  -3438  -1043     94       C  
-ATOM   5272  CG2 VAL A 695      -9.188 -18.044 -21.529  1.00 50.13           C  
-ANISOU 5272  CG2 VAL A 695     6812   9413   2824  -3854  -1166    126       C  
-ATOM   5273  N   PRO A 696     -10.779 -14.340 -20.485  1.00 68.72           N  
-ANISOU 5273  N   PRO A 696     8175  12451   5484  -3169  -1340    432       N  
-ATOM   5274  CA  PRO A 696     -11.451 -13.274 -21.237  1.00 75.40           C  
-ANISOU 5274  CA  PRO A 696     8777  13570   6301  -3042  -1427    563       C  
-ATOM   5275  C   PRO A 696     -11.075 -13.286 -22.723  1.00 80.37           C  
-ANISOU 5275  C   PRO A 696     9563  14155   6820  -3109  -1443    593       C  
-ATOM   5276  O   PRO A 696     -10.241 -12.486 -23.156  1.00 77.96           O  
-ANISOU 5276  O   PRO A 696     9303  13666   6654  -2873  -1396    624       O  
-ATOM   5277  CB  PRO A 696     -10.916 -11.990 -20.583  1.00 70.71           C  
-ANISOU 5277  CB  PRO A 696     8045  12844   5976  -2652  -1377    593       C  
-ATOM   5278  CG  PRO A 696     -10.335 -12.409 -19.278  1.00 67.53           C  
-ANISOU 5278  CG  PRO A 696     7730  12224   5705  -2616  -1292    484       C  
-ATOM   5279  CD  PRO A 696      -9.844 -13.805 -19.482  1.00 65.69           C  
-ANISOU 5279  CD  PRO A 696     7801  11804   5354  -2888  -1249    388       C  
-ATOM   5280  N   CYS A 697     -11.684 -14.181 -23.493  1.00111.19           N  
-ANISOU 5280  N   CYS A 697    13552  18231  10464  -3441  -1506    582       N  
-ATOM   5281  CA  CYS A 697     -11.361 -14.305 -24.909  1.00115.55           C  
-ANISOU 5281  CA  CYS A 697    14272  18759  10873  -3543  -1519    594       C  
-ATOM   5282  C   CYS A 697     -12.527 -14.839 -25.721  1.00120.77           C  
-ANISOU 5282  C   CYS A 697    14865  19792  11230  -3875  -1645    639       C  
-ATOM   5283  O   CYS A 697     -13.480 -15.397 -25.175  1.00122.58           O  
-ANISOU 5283  O   CYS A 697    14977  20249  11347  -4088  -1708    632       O  
-ATOM   5284  CB  CYS A 697     -10.170 -15.242 -25.105  1.00118.16           C  
-ANISOU 5284  CB  CYS A 697    14987  18696  11214  -3633  -1393    444       C  
-ATOM   5285  SG  CYS A 697      -8.591 -14.572 -24.583  1.00122.09           S  
-ANISOU 5285  SG  CYS A 697    15586  18769  12032  -3257  -1248    406       S  
-ATOM   5286  N   GLU A 698     -12.433 -14.662 -27.033  1.00 81.40           N  
-ANISOU 5286  N   GLU A 698     9950  14878   6101  -3931  -1684    688       N  
-ATOM   5287  CA  GLU A 698     -13.326 -15.323 -27.965  1.00 87.29           C  
-ANISOU 5287  CA  GLU A 698    10707  15933   6526  -4294  -1795    702       C  
-ATOM   5288  C   GLU A 698     -12.784 -16.722 -28.185  1.00 86.20           C  
-ANISOU 5288  C   GLU A 698    10960  15534   6259  -4600  -1710    513       C  
-ATOM   5289  O   GLU A 698     -13.529 -17.698 -28.228  1.00 90.18           O  
-ANISOU 5289  O   GLU A 698    11522  16195   6548  -4963  -1766    453       O  
-ATOM   5290  CB  GLU A 698     -13.349 -14.561 -29.284  1.00 91.03           C  
-ANISOU 5290  CB  GLU A 698    11121  16573   6893  -4222  -1863    829       C  
-ATOM   5291  CG  GLU A 698     -14.156 -15.210 -30.386  1.00 98.59           C  
-ANISOU 5291  CG  GLU A 698    12112  17852   7496  -4603  -1980    840       C  
-ATOM   5292  CD  GLU A 698     -14.086 -14.419 -31.675  1.00 99.63           C  
-ANISOU 5292  CD  GLU A 698    12196  18137   7523  -4512  -2043    978       C  
-ATOM   5293  OE1 GLU A 698     -13.088 -13.691 -31.865  1.00 97.02           O  
-ANISOU 5293  OE1 GLU A 698    11945  17541   7376  -4217  -1951   1006       O  
-ATOM   5294  OE2 GLU A 698     -15.029 -14.514 -32.490  1.00 99.81           O  
-ANISOU 5294  OE2 GLU A 698    12093  18558   7274  -4741  -2187   1067       O  
-ATOM   5295  N   SER A 699     -11.467 -16.800 -28.318  1.00100.85           N  
-ANISOU 5295  N   SER A 699    13083  16983   8251  -4444  -1569    421       N  
-ATOM   5296  CA  SER A 699     -10.759 -18.065 -28.434  1.00 97.18           C  
-ANISOU 5296  CA  SER A 699    13009  16197   7718  -4652  -1455    237       C  
-ATOM   5297  C   SER A 699      -9.453 -17.942 -27.668  1.00 92.25           C  
-ANISOU 5297  C   SER A 699    12520  15148   7383  -4355  -1301    171       C  
-ATOM   5298  O   SER A 699      -8.949 -16.836 -27.478  1.00 89.60           O  
-ANISOU 5298  O   SER A 699    12029  14760   7254  -4021  -1278    258       O  
-ATOM   5299  CB  SER A 699     -10.477 -18.390 -29.899  1.00 99.53           C  
-ANISOU 5299  CB  SER A 699    13533  16493   7791  -4823  -1444    188       C  
-ATOM   5300  OG  SER A 699      -9.292 -19.153 -30.032  1.00 96.93           O  
-ANISOU 5300  OG  SER A 699    13574  15744   7510  -4818  -1278     25       O  
-ATOM   5301  N   ALA A 700      -8.905 -19.067 -27.224  1.00 75.94           N  
-ANISOU 5301  N   ALA A 700    10743  12780   5331  -4478  -1197     23       N  
-ATOM   5302  CA  ALA A 700      -7.661 -19.038 -26.467  1.00 71.76           C  
-ANISOU 5302  CA  ALA A 700    10335  11867   5064  -4207  -1056    -33       C  
-ATOM   5303  C   ALA A 700      -6.961 -20.389 -26.436  1.00 70.61           C  
-ANISOU 5303  C   ALA A 700    10576  11376   4878  -4360   -931   -195       C  
-ATOM   5304  O   ALA A 700      -7.558 -21.408 -26.093  1.00 71.31           O  
-ANISOU 5304  O   ALA A 700    10784  11471   4840  -4642   -953   -260       O  
-ATOM   5305  CB  ALA A 700      -7.913 -18.533 -25.052  1.00 70.24           C  
-ANISOU 5305  CB  ALA A 700     9896  11717   5075  -4028  -1084     31       C  
-ATOM   5306  N   GLU A 701      -5.688 -20.385 -26.810  1.00 88.13           N  
-ANISOU 5306  N   GLU A 701    12989  13291   7206  -4170   -796   -256       N  
-ATOM   5307  CA  GLU A 701      -4.846 -21.563 -26.693  1.00 87.99           C  
-ANISOU 5307  CA  GLU A 701    13327  12903   7201  -4226   -654   -401       C  
-ATOM   5308  C   GLU A 701      -3.569 -21.146 -25.989  1.00 81.70           C  
-ANISOU 5308  C   GLU A 701    12520  11827   6694  -3865   -540   -391       C  
-ATOM   5309  O   GLU A 701      -2.807 -20.337 -26.515  1.00 81.18           O  
-ANISOU 5309  O   GLU A 701    12398  11724   6723  -3640   -489   -355       O  
-ATOM   5310  CB  GLU A 701      -4.501 -22.124 -28.070  1.00 97.01           C  
-ANISOU 5310  CB  GLU A 701    14754  13962   8144  -4379   -581   -507       C  
-ATOM   5311  CG  GLU A 701      -5.690 -22.346 -28.978  1.00110.38           C  
-ANISOU 5311  CG  GLU A 701    16435  15975   9528  -4729   -705   -507       C  
-ATOM   5312  CD  GLU A 701      -5.270 -22.834 -30.348  1.00118.99           C  
-ANISOU 5312  CD  GLU A 701    17814  16982  10413  -4867   -624   -623       C  
-ATOM   5313  OE1 GLU A 701      -4.305 -23.625 -30.427  1.00123.57           O  
-ANISOU 5313  OE1 GLU A 701    18711  17203  11038  -4822   -461   -759       O  
-ATOM   5314  OE2 GLU A 701      -5.894 -22.418 -31.347  1.00124.99           O  
-ANISOU 5314  OE2 GLU A 701    18481  18043  10965  -5010   -721   -574       O  
-ATOM   5315  N   VAL A 702      -3.337 -21.686 -24.800  1.00 71.15           N  
-ANISOU 5315  N   VAL A 702    11232  10311   5492  -3821   -503   -414       N  
-ATOM   5316  CA  VAL A 702      -2.163 -21.314 -24.029  1.00 64.36           C  
-ANISOU 5316  CA  VAL A 702    10340   9215   4898  -3494   -410   -398       C  
-ATOM   5317  C   VAL A 702      -1.228 -22.496 -23.825  1.00 63.26           C  
-ANISOU 5317  C   VAL A 702    10530   8706   4801  -3483   -267   -504       C  
-ATOM   5318  O   VAL A 702      -1.668 -23.594 -23.502  1.00 63.47           O  
-ANISOU 5318  O   VAL A 702    10746   8642   4726  -3705   -266   -562       O  
-ATOM   5319  CB  VAL A 702      -2.556 -20.757 -22.661  1.00 60.68           C  
-ANISOU 5319  CB  VAL A 702     9607   8863   4584  -3384   -489   -312       C  
-ATOM   5320  CG1 VAL A 702      -1.320 -20.314 -21.901  1.00 60.01           C  
-ANISOU 5320  CG1 VAL A 702     9481   8559   4760  -3060   -404   -296       C  
-ATOM   5321  CG2 VAL A 702      -3.522 -19.601 -22.827  1.00 58.30           C  
-ANISOU 5321  CG2 VAL A 702     8982   8920   4250  -3372   -622   -207       C  
-ATOM   5322  N   SER A 703       0.065 -22.266 -24.020  1.00 65.00           N  
-ANISOU 5322  N   SER A 703    10814   8711   5172  -3222   -145   -523       N  
-ATOM   5323  CA  SER A 703       1.064 -23.287 -23.737  1.00 65.67           C  
-ANISOU 5323  CA  SER A 703    11175   8444   5334  -3141     -1   -604       C  
-ATOM   5324  C   SER A 703       1.583 -23.096 -22.324  1.00 64.23           C  
-ANISOU 5324  C   SER A 703    10858   8166   5382  -2925     -2   -537       C  
-ATOM   5325  O   SER A 703       1.939 -21.983 -21.936  1.00 63.09           O  
-ANISOU 5325  O   SER A 703    10453   8121   5397  -2708    -34   -458       O  
-ATOM   5326  CB  SER A 703       2.217 -23.223 -24.743  1.00 66.28           C  
-ANISOU 5326  CB  SER A 703    11391   8357   5435  -2976    145   -663       C  
-ATOM   5327  OG  SER A 703       1.803 -23.666 -26.027  1.00 68.30           O  
-ANISOU 5327  OG  SER A 703    11842   8659   5450  -3202    168   -751       O  
-ATOM   5328  N   ILE A 704       1.614 -24.181 -21.554  1.00 68.51           N  
-ANISOU 5328  N   ILE A 704    11585   8513   5933  -2996     31   -565       N  
-ATOM   5329  CA  ILE A 704       2.063 -24.128 -20.165  1.00 65.87           C  
-ANISOU 5329  CA  ILE A 704    11142   8097   5789  -2819     23   -496       C  
-ATOM   5330  C   ILE A 704       3.363 -23.348 -20.044  1.00 61.55           C  
-ANISOU 5330  C   ILE A 704    10465   7466   5454  -2478     95   -461       C  
-ATOM   5331  O   ILE A 704       4.403 -23.764 -20.556  1.00 61.03           O  
-ANISOU 5331  O   ILE A 704    10574   7180   5435  -2343    228   -510       O  
-ATOM   5332  CB  ILE A 704       2.234 -25.537 -19.565  1.00 69.35           C  
-ANISOU 5332  CB  ILE A 704    11872   8263   6216  -2902     88   -529       C  
-ATOM   5333  CG1 ILE A 704       0.863 -26.173 -19.313  1.00 71.71           C  
-ANISOU 5333  CG1 ILE A 704    12232   8683   6330  -3253    -10   -534       C  
-ATOM   5334  CG2 ILE A 704       3.037 -25.473 -18.275  1.00 69.38           C  
-ANISOU 5334  CG2 ILE A 704    11781   8152   6427  -2658    104   -452       C  
-ATOM   5335  CD1 ILE A 704       0.905 -27.671 -19.143  1.00 73.32           C  
-ANISOU 5335  CD1 ILE A 704    12804   8591   6464  -3411     66   -589       C  
-ATOM   5336  N   VAL A 705       3.286 -22.209 -19.366  1.00 59.69           N  
-ANISOU 5336  N   VAL A 705     9921   7416   5341  -2346     10   -380       N  
-ATOM   5337  CA  VAL A 705       4.417 -21.300 -19.222  1.00 55.33           C  
-ANISOU 5337  CA  VAL A 705     9209   6828   4985  -2057     56   -341       C  
-ATOM   5338  C   VAL A 705       5.335 -21.643 -18.047  1.00 53.67           C  
-ANISOU 5338  C   VAL A 705     8999   6451   4944  -1873     97   -309       C  
-ATOM   5339  O   VAL A 705       4.888 -21.857 -16.924  1.00 53.02           O  
-ANISOU 5339  O   VAL A 705     8857   6410   4879  -1920     26   -269       O  
-ATOM   5340  CB  VAL A 705       3.933 -19.843 -19.065  1.00 53.07           C  
-ANISOU 5340  CB  VAL A 705     8605   6802   4756  -2000    -51   -276       C  
-ATOM   5341  CG1 VAL A 705       4.879 -19.050 -18.180  1.00 50.75           C  
-ANISOU 5341  CG1 VAL A 705     8125   6475   4682  -1748    -42   -228       C  
-ATOM   5342  CG2 VAL A 705       3.777 -19.186 -20.423  1.00 53.09           C  
-ANISOU 5342  CG2 VAL A 705     8583   6914   4675  -2030    -45   -281       C  
-ATOM   5343  N   ASP A 706       6.628 -21.697 -18.334  1.00 55.03           N  
-ANISOU 5343  N   ASP A 706     9227   6451   5229  -1665    214   -318       N  
-ATOM   5344  CA  ASP A 706       7.659 -21.860 -17.325  1.00 54.43           C  
-ANISOU 5344  CA  ASP A 706     9108   6248   5325  -1454    251   -271       C  
-ATOM   5345  C   ASP A 706       7.439 -20.860 -16.203  1.00 51.09           C  
-ANISOU 5345  C   ASP A 706     8395   6010   5005  -1395    133   -203       C  
-ATOM   5346  O   ASP A 706       7.151 -21.231 -15.070  1.00 52.03           O  
-ANISOU 5346  O   ASP A 706     8494   6138   5137  -1426     74   -167       O  
-ATOM   5347  CB  ASP A 706       9.020 -21.608 -17.974  1.00 57.25           C  
-ANISOU 5347  CB  ASP A 706     9464   6495   5792  -1231    377   -280       C  
-ATOM   5348  CG  ASP A 706      10.171 -22.066 -17.116  1.00 60.85           C  
-ANISOU 5348  CG  ASP A 706     9924   6797   6401  -1016    437   -234       C  
-ATOM   5349  OD1 ASP A 706      10.098 -23.191 -16.577  1.00 64.79           O  
-ANISOU 5349  OD1 ASP A 706    10607   7138   6871  -1046    457   -228       O  
-ATOM   5350  OD2 ASP A 706      11.144 -21.295 -16.979  1.00 61.77           O  
-ANISOU 5350  OD2 ASP A 706     9853   6955   6662   -823    462   -194       O  
-ATOM   5351  N   CYS A 707       7.584 -19.584 -16.538  1.00 58.91           N  
-ANISOU 5351  N   CYS A 707     9175   7144   6066  -1314    105   -189       N  
-ATOM   5352  CA  CYS A 707       7.353 -18.501 -15.596  1.00 54.84           C  
-ANISOU 5352  CA  CYS A 707     8394   6798   5645  -1258      3   -145       C  
-ATOM   5353  C   CYS A 707       7.027 -17.208 -16.339  1.00 52.21           C  
-ANISOU 5353  C   CYS A 707     7897   6619   5322  -1250    -33   -139       C  
-ATOM   5354  O   CYS A 707       7.179 -17.127 -17.553  1.00 51.96           O  
-ANISOU 5354  O   CYS A 707     7944   6562   5236  -1266     26   -156       O  
-ATOM   5355  CB  CYS A 707       8.573 -18.309 -14.696  1.00 54.27           C  
-ANISOU 5355  CB  CYS A 707     8224   6651   5747  -1053     30   -108       C  
-ATOM   5356  SG  CYS A 707      10.149 -18.535 -15.518  1.00 52.66           S  
-ANISOU 5356  SG  CYS A 707     8104   6267   5639   -862    180   -112       S  
-ATOM   5357  N   ILE A 708       6.567 -16.203 -15.602  1.00 40.48           N  
-ANISOU 5357  N   ILE A 708     6192   5289   3898  -1224   -126   -113       N  
-ATOM   5358  CA  ILE A 708       6.205 -14.924 -16.187  1.00 36.13           C  
-ANISOU 5358  CA  ILE A 708     5485   4870   3372  -1200   -166    -94       C  
-ATOM   5359  C   ILE A 708       7.019 -13.843 -15.509  1.00 36.14           C  
-ANISOU 5359  C   ILE A 708     5304   4868   3558  -1029   -172    -75       C  
-ATOM   5360  O   ILE A 708       6.834 -13.585 -14.322  1.00 36.14           O  
-ANISOU 5360  O   ILE A 708     5189   4929   3613  -1003   -232    -79       O  
-ATOM   5361  CB  ILE A 708       4.711 -14.627 -15.990  1.00 32.25           C  
-ANISOU 5361  CB  ILE A 708     4897   4582   2775  -1332   -272    -85       C  
-ATOM   5362  CG1 ILE A 708       3.860 -15.681 -16.701  1.00 29.80           C  
-ANISOU 5362  CG1 ILE A 708     4760   4298   2264  -1540   -275   -104       C  
-ATOM   5363  CG2 ILE A 708       4.375 -13.237 -16.490  1.00 32.24           C  
-ANISOU 5363  CG2 ILE A 708     4724   4704   2821  -1267   -314    -49       C  
-ATOM   5364  CD1 ILE A 708       2.376 -15.386 -16.657  1.00 26.53           C  
-ANISOU 5364  CD1 ILE A 708     4227   4121   1732  -1681   -380    -84       C  
-ATOM   5365  N   LEU A 709       7.926 -13.217 -16.252  1.00 41.64           N  
-ANISOU 5365  N   LEU A 709     5979   5501   4341   -927   -108    -59       N  
-ATOM   5366  CA  LEU A 709       8.805 -12.206 -15.674  1.00 41.98           C  
-ANISOU 5366  CA  LEU A 709     5862   5529   4559   -788   -108    -44       C  
-ATOM   5367  C   LEU A 709       8.480 -10.822 -16.238  1.00 43.59           C  
-ANISOU 5367  C   LEU A 709     5945   5808   4810   -764   -140    -14       C  
-ATOM   5368  O   LEU A 709       8.168 -10.691 -17.424  1.00 43.93           O  
-ANISOU 5368  O   LEU A 709     6047   5871   4774   -810   -117     14       O  
-ATOM   5369  CB  LEU A 709      10.260 -12.572 -15.950  1.00 40.88           C  
-ANISOU 5369  CB  LEU A 709     5778   5253   4501   -683     -3    -37       C  
-ATOM   5370  CG  LEU A 709      10.553 -14.067 -15.803  1.00 42.01           C  
-ANISOU 5370  CG  LEU A 709     6095   5288   4577   -694     54    -55       C  
-ATOM   5371  CD1 LEU A 709      12.034 -14.357 -15.967  1.00 41.68           C  
-ANISOU 5371  CD1 LEU A 709     6071   5131   4634   -552    162    -40       C  
-ATOM   5372  CD2 LEU A 709      10.068 -14.563 -14.459  1.00 41.55           C  
-ANISOU 5372  CD2 LEU A 709     6018   5264   4507   -730    -24    -60       C  
-ATOM   5373  N   ALA A 710       8.538  -9.788 -15.398  1.00 37.55           N  
-ANISOU 5373  N   ALA A 710     5020   5080   4166   -696   -191    -18       N  
-ATOM   5374  CA  ALA A 710       8.181  -8.447 -15.861  1.00 38.71           C  
-ANISOU 5374  CA  ALA A 710     5067   5272   4370   -662   -220     16       C  
-ATOM   5375  C   ALA A 710       9.227  -7.388 -15.550  1.00 41.83           C  
-ANISOU 5375  C   ALA A 710     5362   5592   4941   -565   -196     19       C  
-ATOM   5376  O   ALA A 710       9.939  -7.484 -14.551  1.00 41.06           O  
-ANISOU 5376  O   ALA A 710     5213   5462   4925   -527   -197    -19       O  
-ATOM   5377  CB  ALA A 710       6.829  -8.029 -15.311  1.00 35.70           C  
-ANISOU 5377  CB  ALA A 710     4596   5026   3944   -692   -312      5       C  
-ATOM   5378  N   ARG A 711       9.315  -6.390 -16.428  1.00 49.63           N  
-ANISOU 5378  N   ARG A 711     6325   6556   5977   -538   -178     73       N  
-ATOM   5379  CA  ARG A 711      10.131  -5.204 -16.202  1.00 55.35           C  
-ANISOU 5379  CA  ARG A 711     6958   7207   6865   -473   -164     82       C  
-ATOM   5380  C   ARG A 711       9.296  -3.967 -16.517  1.00 60.29           C  
-ANISOU 5380  C   ARG A 711     7529   7851   7526   -447   -211    123       C  
-ATOM   5381  O   ARG A 711       9.794  -2.965 -17.023  1.00 61.17           O  
-ANISOU 5381  O   ARG A 711     7621   7885   7734   -415   -182    173       O  
-ATOM   5382  CB  ARG A 711      11.392  -5.232 -17.059  1.00 56.39           C  
-ANISOU 5382  CB  ARG A 711     7128   7256   7040   -461    -67    127       C  
-ATOM   5383  CG  ARG A 711      12.330  -4.060 -16.800  1.00 59.31           C  
-ANISOU 5383  CG  ARG A 711     7403   7554   7577   -425    -50    138       C  
-ATOM   5384  CD  ARG A 711      12.559  -3.890 -15.305  1.00 61.18           C  
-ANISOU 5384  CD  ARG A 711     7546   7798   7902   -407   -105     57       C  
-ATOM   5385  NE  ARG A 711      12.745  -2.507 -14.849  1.00 64.32           N  
-ANISOU 5385  NE  ARG A 711     7861   8142   8437   -395   -133     40       N  
-ATOM   5386  CZ  ARG A 711      12.501  -1.404 -15.558  1.00 67.14           C  
-ANISOU 5386  CZ  ARG A 711     8226   8437   8849   -389   -126     95       C  
-ATOM   5387  NH1 ARG A 711      12.718  -0.216 -15.007  1.00 67.64           N  
-ANISOU 5387  NH1 ARG A 711     8234   8424   9043   -383   -147     64       N  
-ATOM   5388  NH2 ARG A 711      12.044  -1.470 -16.804  1.00 68.57           N  
-ANISOU 5388  NH2 ARG A 711     8478   8625   8950   -392    -99    183       N  
-ATOM   5389  N   VAL A 712       8.007  -4.062 -16.222  1.00 66.86           N  
-ANISOU 5389  N   VAL A 712     8337   8789   8276   -457   -280    109       N  
-ATOM   5390  CA  VAL A 712       7.104  -2.926 -16.308  1.00 73.92           C  
-ANISOU 5390  CA  VAL A 712     9161   9716   9210   -400   -330    144       C  
-ATOM   5391  C   VAL A 712       7.433  -1.904 -15.220  1.00 78.41           C  
-ANISOU 5391  C   VAL A 712     9645  10209   9940   -329   -342     78       C  
-ATOM   5392  O   VAL A 712       7.244  -0.702 -15.405  1.00 81.14           O  
-ANISOU 5392  O   VAL A 712     9958  10491  10381   -261   -349    111       O  
-ATOM   5393  CB  VAL A 712       5.644  -3.385 -16.150  1.00 74.23           C  
-ANISOU 5393  CB  VAL A 712     9168   9922   9114   -429   -398    141       C  
-ATOM   5394  CG1 VAL A 712       4.701  -2.188 -16.087  1.00 75.67           C  
-ANISOU 5394  CG1 VAL A 712     9254  10148   9351   -334   -445    175       C  
-ATOM   5395  CG2 VAL A 712       5.268  -4.324 -17.279  1.00 75.59           C  
-ANISOU 5395  CG2 VAL A 712     9434  10172   9115   -525   -392    200       C  
-ATOM   5396  N   GLY A 713       7.931  -2.392 -14.087  1.00 91.33           N  
-ANISOU 5396  N   GLY A 713    11256  11846  11598   -348   -346    -15       N  
-ATOM   5397  CA  GLY A 713       8.282  -1.537 -12.966  1.00 95.99           C  
-ANISOU 5397  CA  GLY A 713    11774  12382  12315   -307   -360    -99       C  
-ATOM   5398  C   GLY A 713       9.133  -0.345 -13.358  1.00 99.27           C  
-ANISOU 5398  C   GLY A 713    12190  12646  12881   -279   -323    -71       C  
-ATOM   5399  O   GLY A 713       8.866   0.786 -12.948  1.00102.45           O  
-ANISOU 5399  O   GLY A 713    12559  12984  13382   -227   -338   -108       O  
-ATOM   5400  N   SER A 723      19.977   3.733  -6.443  1.00104.08           N  
-ANISOU 5400  N   SER A 723    12152  13141  14254  -1033   -415   -631       N  
-ATOM   5401  CA  SER A 723      19.917   4.285  -7.794  1.00102.06           C  
-ANISOU 5401  CA  SER A 723    11974  12727  14078  -1019   -335   -534       C  
-ATOM   5402  C   SER A 723      18.760   3.681  -8.582  1.00 98.19           C  
-ANISOU 5402  C   SER A 723    11581  12203  13523   -869   -302   -465       C  
-ATOM   5403  O   SER A 723      18.611   2.461  -8.653  1.00 98.20           O  
-ANISOU 5403  O   SER A 723    11561  12322  13429   -789   -303   -415       O  
-ATOM   5404  CB  SER A 723      21.235   4.048  -8.539  1.00106.57           C  
-ANISOU 5404  CB  SER A 723    12447  13355  14690  -1079   -282   -413       C  
-ATOM   5405  OG  SER A 723      22.339   4.572  -7.821  1.00112.04           O  
-ANISOU 5405  OG  SER A 723    13025  14111  15433  -1235   -320   -467       O  
-ATOM   5406  N   THR A 724      17.940   4.541  -9.173  1.00 68.09           N  
-ANISOU 5406  N   THR A 724     7880   8230   9761   -835   -276   -459       N  
-ATOM   5407  CA  THR A 724      16.807   4.086  -9.964  1.00 62.12           C  
-ANISOU 5407  CA  THR A 724     7204   7459   8939   -709   -254   -389       C  
-ATOM   5408  C   THR A 724      17.267   3.348 -11.216  1.00 59.03           C  
-ANISOU 5408  C   THR A 724     6815   7103   8512   -687   -190   -241       C  
-ATOM   5409  O   THR A 724      16.652   2.361 -11.618  1.00 58.17           O  
-ANISOU 5409  O   THR A 724     6736   7066   8299   -607   -183   -195       O  
-ATOM   5410  CB  THR A 724      15.886   5.254 -10.359  1.00 61.19           C  
-ANISOU 5410  CB  THR A 724     7192   7168   8891   -666   -242   -394       C  
-ATOM   5411  OG1 THR A 724      15.074   4.862 -11.473  1.00 59.85           O  
-ANISOU 5411  OG1 THR A 724     7081   6999   8661   -569   -214   -276       O  
-ATOM   5412  CG2 THR A 724      16.709   6.477 -10.748  1.00 61.26           C  
-ANISOU 5412  CG2 THR A 724     7230   7010   9037   -770   -205   -370       C  
-ATOM   5413  N   PHE A 725      18.346   3.829 -11.829  1.00 70.69           N  
-ANISOU 5413  N   PHE A 725     8261   8531  10068   -770   -137   -173       N  
-ATOM   5414  CA  PHE A 725      18.925   3.172 -13.000  1.00 67.20           C  
-ANISOU 5414  CA  PHE A 725     7811   8134   9589   -755    -59    -43       C  
-ATOM   5415  C   PHE A 725      19.528   1.830 -12.613  1.00 64.71           C  
-ANISOU 5415  C   PHE A 725     7409   7981   9197   -719    -57    -45       C  
-ATOM   5416  O   PHE A 725      19.240   0.804 -13.229  1.00 62.43           O  
-ANISOU 5416  O   PHE A 725     7163   7743   8814   -638    -20     11       O  
-ATOM   5417  CB  PHE A 725      19.990   4.058 -13.644  1.00 68.98           C  
-ANISOU 5417  CB  PHE A 725     8006   8288   9917   -866      1     27       C  
-ATOM   5418  CG  PHE A 725      20.780   3.375 -14.725  1.00 69.82           C  
-ANISOU 5418  CG  PHE A 725     8076   8472   9981   -857     94    147       C  
-ATOM   5419  CD1 PHE A 725      20.222   3.143 -15.972  1.00 69.40           C  
-ANISOU 5419  CD1 PHE A 725     8122   8386   9860   -796    153    246       C  
-ATOM   5420  CD2 PHE A 725      22.090   2.984 -14.503  1.00 71.61           C  
-ANISOU 5420  CD2 PHE A 725     8162   8817  10229   -909    126    162       C  
-ATOM   5421  CE1 PHE A 725      20.952   2.521 -16.972  1.00 69.54           C  
-ANISOU 5421  CE1 PHE A 725     8117   8479   9827   -788    251    341       C  
-ATOM   5422  CE2 PHE A 725      22.824   2.363 -15.499  1.00 73.45           C  
-ANISOU 5422  CE2 PHE A 725     8357   9127  10424   -884    228    265       C  
-ATOM   5423  CZ  PHE A 725      22.254   2.131 -16.734  1.00 71.20           C  
-ANISOU 5423  CZ  PHE A 725     8188   8797  10066   -825    295    347       C  
-ATOM   5424  N   MET A 726      20.362   1.849 -11.579  1.00 63.74           N  
-ANISOU 5424  N   MET A 726     7170   7937   9112   -781   -100   -107       N  
-ATOM   5425  CA  MET A 726      20.969   0.637 -11.050  1.00 62.91           C  
-ANISOU 5425  CA  MET A 726     6972   7987   8945   -734   -110   -100       C  
-ATOM   5426  C   MET A 726      19.937  -0.449 -10.767  1.00 59.16           C  
-ANISOU 5426  C   MET A 726     6574   7552   8353   -626   -141   -121       C  
-ATOM   5427  O   MET A 726      20.208  -1.637 -10.936  1.00 57.22           O  
-ANISOU 5427  O   MET A 726     6321   7379   8040   -552   -110    -71       O  
-ATOM   5428  CB  MET A 726      21.741   0.958  -9.771  1.00 66.70           C  
-ANISOU 5428  CB  MET A 726     7320   8558   9466   -823   -184   -176       C  
-ATOM   5429  CG  MET A 726      22.466  -0.223  -9.176  1.00 70.86           C  
-ANISOU 5429  CG  MET A 726     7733   9256   9936   -766   -203   -147       C  
-ATOM   5430  SD  MET A 726      23.473  -1.050 -10.414  1.00 75.33           S  
-ANISOU 5430  SD  MET A 726     8246   9872  10505   -687    -80     -2       S  
-ATOM   5431  CE  MET A 726      24.123   0.356 -11.308  1.00 77.83           C  
-ANISOU 5431  CE  MET A 726     8533  10104  10935   -828    -16     35       C  
-ATOM   5432  N   ALA A 727      18.754  -0.036 -10.329  1.00 62.49           N  
-ANISOU 5432  N   ALA A 727     7070   7922   8751   -620   -197   -196       N  
-ATOM   5433  CA  ALA A 727      17.696  -0.981 -10.003  1.00 59.46           C  
-ANISOU 5433  CA  ALA A 727     6750   7589   8252   -546   -232   -218       C  
-ATOM   5434  C   ALA A 727      17.221  -1.709 -11.249  1.00 58.41           C  
-ANISOU 5434  C   ALA A 727     6717   7428   8047   -484   -166   -130       C  
-ATOM   5435  O   ALA A 727      17.060  -2.929 -11.248  1.00 56.83           O  
-ANISOU 5435  O   ALA A 727     6553   7285   7754   -434   -158   -108       O  
-ATOM   5436  CB  ALA A 727      16.540  -0.264  -9.341  1.00 57.18           C  
-ANISOU 5436  CB  ALA A 727     6500   7267   7957   -551   -293   -314       C  
-ATOM   5437  N   GLU A 728      16.999  -0.947 -12.314  1.00 62.01           N  
-ANISOU 5437  N   GLU A 728     7228   7791   8541   -495   -121    -79       N  
-ATOM   5438  CA  GLU A 728      16.537  -1.508 -13.576  1.00 60.43           C  
-ANISOU 5438  CA  GLU A 728     7127   7576   8259   -456    -62      2       C  
-ATOM   5439  C   GLU A 728      17.514  -2.551 -14.116  1.00 57.71           C  
-ANISOU 5439  C   GLU A 728     6776   7275   7878   -430     18     59       C  
-ATOM   5440  O   GLU A 728      17.105  -3.567 -14.675  1.00 56.50           O  
-ANISOU 5440  O   GLU A 728     6712   7140   7616   -390     52     83       O  
-ATOM   5441  CB  GLU A 728      16.323  -0.397 -14.602  1.00 65.45           C  
-ANISOU 5441  CB  GLU A 728     7807   8114   8947   -480    -29     65       C  
-ATOM   5442  CG  GLU A 728      15.971  -0.895 -15.987  1.00 71.29           C  
-ANISOU 5442  CG  GLU A 728     8642   8857   9589   -458     33    157       C  
-ATOM   5443  CD  GLU A 728      15.767   0.238 -16.972  1.00 77.08           C  
-ANISOU 5443  CD  GLU A 728     9416   9503  10367   -480     58    240       C  
-ATOM   5444  OE1 GLU A 728      15.055   1.208 -16.628  1.00 79.95           O  
-ANISOU 5444  OE1 GLU A 728     9786   9802  10791   -471      1    221       O  
-ATOM   5445  OE2 GLU A 728      16.329   0.164 -18.086  1.00 80.08           O  
-ANISOU 5445  OE2 GLU A 728     9827   9879  10721   -500    140    328       O  
-ATOM   5446  N   MET A 729      18.806  -2.297 -13.940  1.00 45.31           N  
-ANISOU 5446  N   MET A 729     5097   5724   6393   -454     51     76       N  
-ATOM   5447  CA  MET A 729      19.828  -3.234 -14.385  1.00 43.91           C  
-ANISOU 5447  CA  MET A 729     4888   5601   6195   -404    137    130       C  
-ATOM   5448  C   MET A 729      19.743  -4.553 -13.638  1.00 42.92           C  
-ANISOU 5448  C   MET A 729     4776   5536   5997   -330    111    103       C  
-ATOM   5449  O   MET A 729      19.821  -5.625 -14.244  1.00 42.47           O  
-ANISOU 5449  O   MET A 729     4797   5475   5865   -261    183    137       O  
-ATOM   5450  CB  MET A 729      21.218  -2.626 -14.227  1.00 43.54           C  
-ANISOU 5450  CB  MET A 729     4688   5596   6259   -452    168    158       C  
-ATOM   5451  CG  MET A 729      21.467  -1.436 -15.146  1.00 44.94           C  
-ANISOU 5451  CG  MET A 729     4868   5704   6504   -535    219    210       C  
-ATOM   5452  SD  MET A 729      21.330  -1.837 -16.912  1.00 46.88           S  
-ANISOU 5452  SD  MET A 729     5233   5918   6661   -496    348    305       S  
-ATOM   5453  CE  MET A 729      19.572  -1.650 -17.223  1.00 43.13           C  
-ANISOU 5453  CE  MET A 729     4926   5361   6102   -488    281    285       C  
-ATOM   5454  N   LEU A 730      19.592  -4.467 -12.319  1.00 47.94           N  
-ANISOU 5454  N   LEU A 730     5345   6219   6650   -347     12     42       N  
-ATOM   5455  CA  LEU A 730      19.488  -5.649 -11.477  1.00 46.48           C  
-ANISOU 5455  CA  LEU A 730     5172   6093   6396   -287    -26     30       C  
-ATOM   5456  C   LEU A 730      18.224  -6.409 -11.821  1.00 46.33           C  
-ANISOU 5456  C   LEU A 730     5315   6029   6258   -269    -28     18       C  
-ATOM   5457  O   LEU A 730      18.213  -7.639 -11.866  1.00 45.56           O  
-ANISOU 5457  O   LEU A 730     5294   5928   6087   -210      3     42       O  
-ATOM   5458  CB  LEU A 730      19.457  -5.253 -10.009  1.00 43.86           C  
-ANISOU 5458  CB  LEU A 730     4742   5835   6088   -332   -137    -36       C  
-ATOM   5459  CG  LEU A 730      20.755  -4.714  -9.420  1.00 44.40           C  
-ANISOU 5459  CG  LEU A 730     4637   5985   6249   -367   -157    -29       C  
-ATOM   5460  CD1 LEU A 730      20.500  -4.134  -8.034  1.00 40.76           C  
-ANISOU 5460  CD1 LEU A 730     4108   5589   5790   -442   -272   -120       C  
-ATOM   5461  CD2 LEU A 730      21.824  -5.797  -9.377  1.00 44.80           C  
-ANISOU 5461  CD2 LEU A 730     4616   6113   6294   -271   -113     52       C  
-ATOM   5462  N   GLU A 731      17.158  -5.665 -12.074  1.00 55.43           N  
-ANISOU 5462  N   GLU A 731     6519   7148   7394   -322    -63    -15       N  
-ATOM   5463  CA  GLU A 731      15.889  -6.276 -12.420  1.00 55.44           C  
-ANISOU 5463  CA  GLU A 731     6651   7137   7276   -328    -76    -24       C  
-ATOM   5464  C   GLU A 731      16.009  -7.064 -13.723  1.00 54.30           C  
-ANISOU 5464  C   GLU A 731     6624   6945   7061   -303     22     31       C  
-ATOM   5465  O   GLU A 731      15.443  -8.149 -13.851  1.00 53.38           O  
-ANISOU 5465  O   GLU A 731     6624   6823   6836   -300     31     28       O  
-ATOM   5466  CB  GLU A 731      14.798  -5.214 -12.524  1.00 60.09           C  
-ANISOU 5466  CB  GLU A 731     7245   7717   7871   -371   -128    -54       C  
-ATOM   5467  CG  GLU A 731      13.388  -5.761 -12.398  1.00 65.91           C  
-ANISOU 5467  CG  GLU A 731     8059   8497   8485   -390   -176    -77       C  
-ATOM   5468  CD  GLU A 731      12.538  -4.920 -11.468  1.00 71.16           C  
-ANISOU 5468  CD  GLU A 731     8658   9208   9173   -405   -258   -144       C  
-ATOM   5469  OE1 GLU A 731      11.301  -4.880 -11.654  1.00 74.88           O  
-ANISOU 5469  OE1 GLU A 731     9163   9721   9568   -417   -289   -150       O  
-ATOM   5470  OE2 GLU A 731      13.116  -4.291 -10.554  1.00 74.62           O  
-ANISOU 5470  OE2 GLU A 731     9005   9650   9698   -405   -287   -195       O  
-ATOM   5471  N   THR A 732      16.754  -6.518 -14.682  1.00 43.83           N  
-ANISOU 5471  N   THR A 732     5277   5587   5791   -297    100     77       N  
-ATOM   5472  CA  THR A 732      16.969  -7.187 -15.965  1.00 44.92           C  
-ANISOU 5472  CA  THR A 732     5524   5689   5854   -274    208    120       C  
-ATOM   5473  C   THR A 732      17.970  -8.333 -15.839  1.00 44.22           C  
-ANISOU 5473  C   THR A 732     5443   5595   5762   -188    284    132       C  
-ATOM   5474  O   THR A 732      17.802  -9.392 -16.443  1.00 43.56           O  
-ANISOU 5474  O   THR A 732     5500   5471   5580   -159    352    131       O  
-ATOM   5475  CB  THR A 732      17.451  -6.202 -17.045  1.00 45.62           C  
-ANISOU 5475  CB  THR A 732     5584   5758   5993   -300    274    176       C  
-ATOM   5476  OG1 THR A 732      18.354  -5.263 -16.456  1.00 48.36           O  
-ANISOU 5476  OG1 THR A 732     5776   6118   6480   -311    257    183       O  
-ATOM   5477  CG2 THR A 732      16.275  -5.443 -17.639  1.00 45.88           C  
-ANISOU 5477  CG2 THR A 732     5678   5777   5977   -360    227    191       C  
-ATOM   5478  N   ALA A 733      19.009  -8.119 -15.042  1.00 40.01           N  
-ANISOU 5478  N   ALA A 733     4760   5106   5335   -147    274    144       N  
-ATOM   5479  CA  ALA A 733      19.942  -9.190 -14.728  1.00 41.01           C  
-ANISOU 5479  CA  ALA A 733     4867   5244   5470    -39    330    168       C  
-ATOM   5480  C   ALA A 733      19.202 -10.383 -14.123  1.00 40.38           C  
-ANISOU 5480  C   ALA A 733     4916   5129   5298    -13    288    144       C  
-ATOM   5481  O   ALA A 733      19.585 -11.530 -14.339  1.00 41.42           O  
-ANISOU 5481  O   ALA A 733     5137   5210   5390     78    365    163       O  
-ATOM   5482  CB  ALA A 733      21.020  -8.697 -13.782  1.00 40.63           C  
-ANISOU 5482  CB  ALA A 733     4613   5284   5539    -18    289    189       C  
-ATOM   5483  N   SER A 734      18.146 -10.107 -13.359  1.00 52.75           N  
-ANISOU 5483  N   SER A 734     6495   6719   6830    -92    173    101       N  
-ATOM   5484  CA  SER A 734      17.310 -11.169 -12.800  1.00 52.54           C  
-ANISOU 5484  CA  SER A 734     6591   6668   6702   -102    129     83       C  
-ATOM   5485  C   SER A 734      16.585 -11.924 -13.904  1.00 51.39           C  
-ANISOU 5485  C   SER A 734     6648   6441   6437   -133    197     72       C  
-ATOM   5486  O   SER A 734      16.770 -13.129 -14.071  1.00 51.40           O  
-ANISOU 5486  O   SER A 734     6781   6365   6383    -81    261     82       O  
-ATOM   5487  CB  SER A 734      16.291 -10.609 -11.803  1.00 53.39           C  
-ANISOU 5487  CB  SER A 734     6650   6845   6789   -189      2     37       C  
-ATOM   5488  OG  SER A 734      16.884 -10.376 -10.533  1.00 58.18           O  
-ANISOU 5488  OG  SER A 734     7115   7528   7462   -165    -67     37       O  
-ATOM   5489  N   ILE A 735      15.763 -11.203 -14.659  1.00 47.15           N  
-ANISOU 5489  N   ILE A 735     6140   5918   5857   -220    183     53       N  
-ATOM   5490  CA  ILE A 735      14.997 -11.781 -15.758  1.00 46.94           C  
-ANISOU 5490  CA  ILE A 735     6291   5845   5698   -280    231     40       C  
-ATOM   5491  C   ILE A 735      15.853 -12.596 -16.721  1.00 48.00           C  
-ANISOU 5491  C   ILE A 735     6537   5894   5805   -208    374     51       C  
-ATOM   5492  O   ILE A 735      15.470 -13.689 -17.132  1.00 47.97           O  
-ANISOU 5492  O   ILE A 735     6720   5818   5689   -230    421     24       O  
-ATOM   5493  CB  ILE A 735      14.295 -10.690 -16.571  1.00 46.95           C  
-ANISOU 5493  CB  ILE A 735     6267   5895   5678   -356    205     46       C  
-ATOM   5494  CG1 ILE A 735      13.389  -9.863 -15.665  1.00 46.98           C  
-ANISOU 5494  CG1 ILE A 735     6165   5976   5709   -406     78     27       C  
-ATOM   5495  CG2 ILE A 735      13.502 -11.305 -17.713  1.00 46.28           C  
-ANISOU 5495  CG2 ILE A 735     6357   5794   5434   -434    244     36       C  
-ATOM   5496  CD1 ILE A 735      12.771  -8.676 -16.362  1.00 49.38           C  
-ANISOU 5496  CD1 ILE A 735     6426   6317   6019   -447     50     50       C  
-ATOM   5497  N   LEU A 736      17.009 -12.056 -17.089  1.00 40.58           N  
-ANISOU 5497  N   LEU A 736     5490   4966   4964   -129    449     85       N  
-ATOM   5498  CA  LEU A 736      17.851 -12.701 -18.092  1.00 44.35           C  
-ANISOU 5498  CA  LEU A 736     6054   5383   5414    -49    602     92       C  
-ATOM   5499  C   LEU A 736      18.479 -13.991 -17.588  1.00 48.34           C  
-ANISOU 5499  C   LEU A 736     6630   5810   5928     74    662     91       C  
-ATOM   5500  O   LEU A 736      18.919 -14.828 -18.376  1.00 51.61           O  
-ANISOU 5500  O   LEU A 736     7177   6141   6290    145    796     76       O  
-ATOM   5501  CB  LEU A 736      18.935 -11.745 -18.596  1.00 40.07           C  
-ANISOU 5501  CB  LEU A 736     5354   4897   4974     -5    671    138       C  
-ATOM   5502  CG  LEU A 736      18.401 -10.548 -19.378  1.00 35.80           C  
-ANISOU 5502  CG  LEU A 736     4787   4400   4414   -114    643    157       C  
-ATOM   5503  CD1 LEU A 736      19.544  -9.669 -19.814  1.00 33.40           C  
-ANISOU 5503  CD1 LEU A 736     4336   4143   4213    -84    717    212       C  
-ATOM   5504  CD2 LEU A 736      17.570 -11.007 -20.564  1.00 32.65           C  
-ANISOU 5504  CD2 LEU A 736     4585   3973   3849   -185    690    133       C  
-ATOM   5505  N   ARG A 737      18.523 -14.154 -16.275  1.00 56.52           N  
-ANISOU 5505  N   ARG A 737     7582   6868   7026    105    568    110       N  
-ATOM   5506  CA  ARG A 737      19.138 -15.340 -15.701  1.00 61.49           C  
-ANISOU 5506  CA  ARG A 737     8267   7424   7673    237    613    134       C  
-ATOM   5507  C   ARG A 737      18.103 -16.184 -14.971  1.00 61.31           C  
-ANISOU 5507  C   ARG A 737     8393   7339   7562    166    530    115       C  
-ATOM   5508  O   ARG A 737      18.436 -17.183 -14.343  1.00 63.29           O  
-ANISOU 5508  O   ARG A 737     8710   7516   7822    260    544    147       O  
-ATOM   5509  CB  ARG A 737      20.294 -14.939 -14.788  1.00 64.57           C  
-ANISOU 5509  CB  ARG A 737     8423   7909   8203    349    584    198       C  
-ATOM   5510  CG  ARG A 737      21.319 -14.083 -15.511  1.00 70.36           C  
-ANISOU 5510  CG  ARG A 737     8997   8716   9019    391    667    223       C  
-ATOM   5511  CD  ARG A 737      22.325 -13.483 -14.556  1.00 76.82           C  
-ANISOU 5511  CD  ARG A 737     9559   9664   9966    446    608    280       C  
-ATOM   5512  NE  ARG A 737      23.369 -12.749 -15.260  1.00 81.99           N  
-ANISOU 5512  NE  ARG A 737    10059  10396  10696    475    698    311       N  
-ATOM   5513  CZ  ARG A 737      24.472 -13.309 -15.745  1.00 86.44           C  
-ANISOU 5513  CZ  ARG A 737    10579  10971  11294    628    835    355       C  
-ATOM   5514  NH1 ARG A 737      24.672 -14.611 -15.607  1.00 89.54           N  
-ANISOU 5514  NH1 ARG A 737    11087  11277  11659    782    899    370       N  
-ATOM   5515  NH2 ARG A 737      25.373 -12.569 -16.372  1.00 89.54           N  
-ANISOU 5515  NH2 ARG A 737    10816  11457  11748    630    914    387       N  
-ATOM   5516  N   SER A 738      16.843 -15.769 -15.072  1.00 61.46           N  
-ANISOU 5516  N   SER A 738     8460   7395   7496      2    445     72       N  
-ATOM   5517  CA  SER A 738      15.726 -16.538 -14.542  1.00 61.98           C  
-ANISOU 5517  CA  SER A 738     8670   7423   7456   -102    374     50       C  
-ATOM   5518  C   SER A 738      14.998 -17.256 -15.668  1.00 62.75           C  
-ANISOU 5518  C   SER A 738     9006   7425   7410   -199    443     -3       C  
-ATOM   5519  O   SER A 738      14.747 -18.458 -15.594  1.00 64.04           O  
-ANISOU 5519  O   SER A 738     9369   7464   7498   -215    477    -17       O  
-ATOM   5520  CB  SER A 738      14.730 -15.624 -13.827  1.00 61.02           C  
-ANISOU 5520  CB  SER A 738     8424   7437   7324   -226    230     36       C  
-ATOM   5521  OG  SER A 738      15.313 -14.979 -12.711  1.00 65.32           O  
-ANISOU 5521  OG  SER A 738     8767   8070   7980   -163    159     67       O  
-ATOM   5522  N   ALA A 739      14.660 -16.508 -16.713  1.00 68.70           N  
-ANISOU 5522  N   ALA A 739     9747   8236   8119   -272    461    -31       N  
-ATOM   5523  CA  ALA A 739      13.797 -17.016 -17.770  1.00 69.30           C  
-ANISOU 5523  CA  ALA A 739    10027   8271   8034   -405    497    -84       C  
-ATOM   5524  C   ALA A 739      14.396 -18.189 -18.541  1.00 71.70           C  
-ANISOU 5524  C   ALA A 739    10554   8408   8280   -341    650   -122       C  
-ATOM   5525  O   ALA A 739      15.617 -18.346 -18.623  1.00 71.95           O  
-ANISOU 5525  O   ALA A 739    10550   8379   8409   -167    756   -101       O  
-ATOM   5526  CB  ALA A 739      13.417 -15.892 -18.724  1.00 70.18           C  
-ANISOU 5526  CB  ALA A 739    10057   8496   8112   -478    480    -83       C  
-ATOM   5527  N   THR A 740      13.513 -19.011 -19.096  1.00 45.42           N  
-ANISOU 5527  N   THR A 740     7455   5012   4791   -486    663   -183       N  
-ATOM   5528  CA  THR A 740      13.904 -20.080 -20.003  1.00 48.78           C  
-ANISOU 5528  CA  THR A 740     8133   5269   5132   -458    816   -247       C  
-ATOM   5529  C   THR A 740      13.061 -20.004 -21.274  1.00 51.67           C  
-ANISOU 5529  C   THR A 740     8632   5685   5315   -643    829   -314       C  
-ATOM   5530  O   THR A 740      12.221 -19.114 -21.420  1.00 50.30           O  
-ANISOU 5530  O   THR A 740     8336   5681   5095   -771    716   -291       O  
-ATOM   5531  CB  THR A 740      13.740 -21.477 -19.358  1.00 48.01           C  
-ANISOU 5531  CB  THR A 740     8254   4986   5002   -462    835   -266       C  
-ATOM   5532  OG1 THR A 740      12.348 -21.794 -19.222  1.00 46.76           O  
-ANISOU 5532  OG1 THR A 740     8205   4860   4702   -703    730   -297       O  
-ATOM   5533  CG2 THR A 740      14.414 -21.530 -17.997  1.00 44.77           C  
-ANISOU 5533  CG2 THR A 740     7699   4560   4753   -300    791   -179       C  
-ATOM   5534  N   LYS A 741      13.281 -20.946 -22.185  1.00 63.41           N  
-ANISOU 5534  N   LYS A 741    10372   7028   6693   -653    967   -396       N  
-ATOM   5535  CA  LYS A 741      12.604 -20.940 -23.473  1.00 67.60           C  
-ANISOU 5535  CA  LYS A 741    11043   7612   7029   -831    993   -467       C  
-ATOM   5536  C   LYS A 741      11.087 -21.043 -23.341  1.00 66.69           C  
-ANISOU 5536  C   LYS A 741    10981   7592   6768  -1091    844   -482       C  
-ATOM   5537  O   LYS A 741      10.354 -20.715 -24.273  1.00 66.44           O  
-ANISOU 5537  O   LYS A 741    10980   7687   6579  -1257    810   -507       O  
-ATOM   5538  CB  LYS A 741      13.135 -22.073 -24.353  1.00 76.15           C  
-ANISOU 5538  CB  LYS A 741    12420   8499   8015   -796   1179   -573       C  
-ATOM   5539  CG  LYS A 741      12.683 -23.466 -23.936  1.00 84.91           C  
-ANISOU 5539  CG  LYS A 741    13809   9400   9054   -879   1196   -641       C  
-ATOM   5540  CD  LYS A 741      13.409 -24.537 -24.742  1.00 95.80           C  
-ANISOU 5540  CD  LYS A 741    15478  10549  10371   -789   1405   -751       C  
-ATOM   5541  CE  LYS A 741      12.709 -25.886 -24.657  1.00103.48           C  
-ANISOU 5541  CE  LYS A 741    16791  11308  11217   -951   1422   -843       C  
-ATOM   5542  NZ  LYS A 741      11.409 -25.893 -25.390  1.00108.59           N  
-ANISOU 5542  NZ  LYS A 741    17558  12069  11631  -1283   1335   -917       N  
-ATOM   5543  N   ASP A 742      10.617 -21.496 -22.182  1.00 76.21           N  
-ANISOU 5543  N   ASP A 742    12185   8757   8015  -1130    754   -457       N  
-ATOM   5544  CA  ASP A 742       9.185 -21.685 -21.962  1.00 74.28           C  
-ANISOU 5544  CA  ASP A 742    11979   8612   7631  -1381    620   -467       C  
-ATOM   5545  C   ASP A 742       8.596 -20.537 -21.155  1.00 68.05           C  
-ANISOU 5545  C   ASP A 742    10891   8042   6922  -1389    461   -378       C  
-ATOM   5546  O   ASP A 742       7.435 -20.583 -20.751  1.00 67.22           O  
-ANISOU 5546  O   ASP A 742    10758   8054   6729  -1566    342   -369       O  
-ATOM   5547  CB  ASP A 742       8.915 -23.005 -21.239  1.00 80.29           C  
-ANISOU 5547  CB  ASP A 742    12958   9190   8358  -1456    628   -498       C  
-ATOM   5548  CG  ASP A 742       9.835 -24.121 -21.695  1.00 86.55           C  
-ANISOU 5548  CG  ASP A 742    14029   9706   9150  -1347    808   -571       C  
-ATOM   5549  OD1 ASP A 742       9.678 -24.595 -22.840  1.00 90.95           O  
-ANISOU 5549  OD1 ASP A 742    14804  10200   9551  -1459    894   -671       O  
-ATOM   5550  OD2 ASP A 742      10.709 -24.532 -20.901  1.00 89.36           O  
-ANISOU 5550  OD2 ASP A 742    14387   9910   9656  -1146    863   -528       O  
-ATOM   5551  N   SER A 743       9.401 -19.508 -20.928  1.00 59.03           N  
-ANISOU 5551  N   SER A 743     9528   6957   5943  -1200    465   -318       N  
-ATOM   5552  CA  SER A 743       8.974 -18.370 -20.127  1.00 51.89           C  
-ANISOU 5552  CA  SER A 743     8353   6228   5133  -1181    333   -246       C  
-ATOM   5553  C   SER A 743       8.234 -17.334 -20.957  1.00 47.29           C  
-ANISOU 5553  C   SER A 743     7657   5836   4476  -1270    266   -222       C  
-ATOM   5554  O   SER A 743       8.374 -17.289 -22.175  1.00 47.71           O  
-ANISOU 5554  O   SER A 743     7800   5892   4436  -1304    333   -242       O  
-ATOM   5555  CB  SER A 743      10.183 -17.709 -19.474  1.00 50.87           C  
-ANISOU 5555  CB  SER A 743     8048   6068   5213   -957    364   -197       C  
-ATOM   5556  OG  SER A 743      10.879 -18.627 -18.658  1.00 51.56           O  
-ANISOU 5556  OG  SER A 743     8215   6003   5372   -856    414   -198       O  
-ATOM   5557  N   LEU A 744       7.439 -16.507 -20.290  1.00 46.85           N  
-ANISOU 5557  N   LEU A 744     7405   5941   4455  -1301    137   -173       N  
-ATOM   5558  CA  LEU A 744       6.875 -15.322 -20.915  1.00 42.22           C  
-ANISOU 5558  CA  LEU A 744     6668   5526   3846  -1323     70   -122       C  
-ATOM   5559  C   LEU A 744       7.448 -14.089 -20.244  1.00 39.86           C  
-ANISOU 5559  C   LEU A 744     6145   5252   3747  -1153     43    -68       C  
-ATOM   5560  O   LEU A 744       7.163 -13.821 -19.083  1.00 38.77           O  
-ANISOU 5560  O   LEU A 744     5883   5158   3691  -1123    -31    -60       O  
-ATOM   5561  CB  LEU A 744       5.358 -15.299 -20.783  1.00 40.19           C  
-ANISOU 5561  CB  LEU A 744     6361   5453   3458  -1495    -56   -110       C  
-ATOM   5562  CG  LEU A 744       4.753 -13.909 -21.010  1.00 38.72           C  
-ANISOU 5562  CG  LEU A 744     5960   5450   3302  -1459   -145    -34       C  
-ATOM   5563  CD1 LEU A 744       4.893 -13.501 -22.454  1.00 37.89           C  
-ANISOU 5563  CD1 LEU A 744     5903   5381   3113  -1478   -106     -1       C  
-ATOM   5564  CD2 LEU A 744       3.293 -13.877 -20.594  1.00 38.70           C  
-ANISOU 5564  CD2 LEU A 744     5859   5647   3198  -1591   -269    -16       C  
-ATOM   5565  N   ILE A 745       8.263 -13.340 -20.973  1.00 40.74           N  
-ANISOU 5565  N   ILE A 745     6212   5338   3928  -1056    107    -34       N  
-ATOM   5566  CA  ILE A 745       8.864 -12.132 -20.433  1.00 38.81           C  
-ANISOU 5566  CA  ILE A 745     5774   5101   3870   -918     88     14       C  
-ATOM   5567  C   ILE A 745       8.052 -10.928 -20.878  1.00 39.21           C  
-ANISOU 5567  C   ILE A 745     5702   5287   3910   -941      7     79       C  
-ATOM   5568  O   ILE A 745       7.498 -10.917 -21.970  1.00 39.17           O  
-ANISOU 5568  O   ILE A 745     5760   5356   3766  -1027      3    107       O  
-ATOM   5569  CB  ILE A 745      10.314 -11.988 -20.899  1.00 37.04           C  
-ANISOU 5569  CB  ILE A 745     5562   4769   3744   -801    212     24       C  
-ATOM   5570  CG1 ILE A 745      11.115 -13.216 -20.467  1.00 37.22           C  
-ANISOU 5570  CG1 ILE A 745     5701   4659   3781   -747    297    -29       C  
-ATOM   5571  CG2 ILE A 745      10.939 -10.702 -20.362  1.00 34.40           C  
-ANISOU 5571  CG2 ILE A 745     5031   4443   3596   -692    188     72       C  
-ATOM   5572  CD1 ILE A 745      12.477 -13.308 -21.095  1.00 38.86           C  
-ANISOU 5572  CD1 ILE A 745     5937   4778   4049   -635    439    -24       C  
-ATOM   5573  N   ILE A 746       7.976  -9.918 -20.023  1.00 42.74           N  
-ANISOU 5573  N   ILE A 746     5976   5765   4497   -861    -58    104       N  
-ATOM   5574  CA  ILE A 746       7.193  -8.730 -20.320  1.00 44.00           C  
-ANISOU 5574  CA  ILE A 746     6018   6031   4670   -851   -134    170       C  
-ATOM   5575  C   ILE A 746       7.966  -7.474 -19.951  1.00 46.07           C  
-ANISOU 5575  C   ILE A 746     6153   6223   5127   -726   -122    202       C  
-ATOM   5576  O   ILE A 746       8.349  -7.292 -18.802  1.00 44.91           O  
-ANISOU 5576  O   ILE A 746     5928   6034   5103   -666   -138    158       O  
-ATOM   5577  CB  ILE A 746       5.865  -8.747 -19.571  1.00 42.36           C  
-ANISOU 5577  CB  ILE A 746     5730   5958   4407   -902   -244    157       C  
-ATOM   5578  CG1 ILE A 746       4.902  -9.730 -20.236  1.00 42.72           C  
-ANISOU 5578  CG1 ILE A 746     5885   6110   4236  -1062   -271    151       C  
-ATOM   5579  CG2 ILE A 746       5.258  -7.360 -19.546  1.00 43.79           C  
-ANISOU 5579  CG2 ILE A 746     5756   6217   4664   -826   -311    222       C  
-ATOM   5580  CD1 ILE A 746       3.552  -9.806 -19.557  1.00 44.00           C  
-ANISOU 5580  CD1 ILE A 746     5952   6440   4327  -1133   -376    147       C  
-ATOM   5581  N   ILE A 747       8.193  -6.607 -20.932  1.00 36.57           N  
-ANISOU 5581  N   ILE A 747     4939   5011   3944   -701    -97    281       N  
-ATOM   5582  CA  ILE A 747       9.001  -5.418 -20.720  1.00 38.17           C  
-ANISOU 5582  CA  ILE A 747     5047   5127   4327   -609    -74    317       C  
-ATOM   5583  C   ILE A 747       8.272  -4.157 -21.148  1.00 44.11           C  
-ANISOU 5583  C   ILE A 747     5729   5920   5110   -575   -134    408       C  
-ATOM   5584  O   ILE A 747       7.413  -4.186 -22.024  1.00 46.17           O  
-ANISOU 5584  O   ILE A 747     6023   6283   5237   -621   -170    474       O  
-ATOM   5585  CB  ILE A 747      10.339  -5.522 -21.454  1.00 35.55           C  
-ANISOU 5585  CB  ILE A 747     4772   4708   4027   -597     43    339       C  
-ATOM   5586  CG1 ILE A 747      11.094  -6.761 -20.977  1.00 32.76           C  
-ANISOU 5586  CG1 ILE A 747     4481   4306   3661   -594    107    257       C  
-ATOM   5587  CG2 ILE A 747      11.177  -4.281 -21.217  1.00 34.46           C  
-ANISOU 5587  CG2 ILE A 747     4533   4487   4073   -533     62    379       C  
-ATOM   5588  CD1 ILE A 747      12.429  -6.947 -21.633  1.00 30.73           C  
-ANISOU 5588  CD1 ILE A 747     4260   3982   3435   -562    235    273       C  
-ATOM   5589  N   ASP A 748       8.623  -3.050 -20.506  1.00 56.16           N  
-ANISOU 5589  N   ASP A 748     7163   7365   6810   -496   -147    413       N  
-ATOM   5590  CA  ASP A 748       7.963  -1.777 -20.731  1.00 65.92           C  
-ANISOU 5590  CA  ASP A 748     8337   8600   8108   -436   -199    496       C  
-ATOM   5591  C   ASP A 748       8.907  -0.649 -20.330  1.00 70.10           C  
-ANISOU 5591  C   ASP A 748     8822   8976   8836   -379   -165    500       C  
-ATOM   5592  O   ASP A 748       9.398  -0.610 -19.207  1.00 67.96           O  
-ANISOU 5592  O   ASP A 748     8501   8649   8671   -361   -165    404       O  
-ATOM   5593  CB  ASP A 748       6.666  -1.712 -19.921  1.00 64.57           C  
-ANISOU 5593  CB  ASP A 748     8087   8532   7913   -401   -293    458       C  
-ATOM   5594  CG  ASP A 748       6.053  -0.329 -19.909  1.00 70.40           C  
-ANISOU 5594  CG  ASP A 748     8753   9244   8753   -296   -338    528       C  
-ATOM   5595  OD1 ASP A 748       5.382   0.022 -18.911  1.00 69.29           O  
-ANISOU 5595  OD1 ASP A 748     8528   9132   8668   -230   -387    467       O  
-ATOM   5596  OD2 ASP A 748       6.244   0.409 -20.898  1.00 73.66           O  
-ANISOU 5596  OD2 ASP A 748     9197   9604   9188   -275   -319    646       O  
-ATOM   5597  N   GLU A 749       9.167   0.260 -21.261  1.00103.64           N  
-ANISOU 5597  N   GLU A 749    13093  13159  13126   -366   -136    616       N  
-ATOM   5598  CA  GLU A 749      10.096   1.356 -21.021  1.00102.60           C  
-ANISOU 5598  CA  GLU A 749    12938  12871  13176   -343    -97    632       C  
-ATOM   5599  C   GLU A 749      11.388   0.833 -20.405  1.00100.14           C  
-ANISOU 5599  C   GLU A 749    12606  12514  12928   -388    -36    539       C  
-ATOM   5600  O   GLU A 749      11.570   0.882 -19.189  1.00 97.21           O  
-ANISOU 5600  O   GLU A 749    12175  12114  12645   -371    -64    434       O  
-ATOM   5601  CB  GLU A 749       9.463   2.400 -20.117  1.00108.31           C  
-ANISOU 5601  CB  GLU A 749    13602  13523  14028   -259   -160    599       C  
-ATOM   5602  N   LEU A 750      12.280   0.324 -21.247  1.00 65.53           N  
-ANISOU 5602  N   LEU A 750     8902   6634   9361   1967   -311   1930       N  
-ATOM   5603  CA  LEU A 750      13.553  -0.209 -20.777  1.00 62.65           C  
-ANISOU 5603  CA  LEU A 750     8634   6445   8725   1968   -317   1349       C  
-ATOM   5604  C   LEU A 750      14.743   0.535 -21.388  1.00 63.92           C  
-ANISOU 5604  C   LEU A 750     8782   6816   8688   1829   -130   1201       C  
-ATOM   5605  O   LEU A 750      14.914   0.559 -22.606  1.00 67.19           O  
-ANISOU 5605  O   LEU A 750     9148   7506   8876   1739   -256   1345       O  
-ATOM   5606  CB  LEU A 750      13.649  -1.700 -21.092  1.00 56.74           C  
-ANISOU 5606  CB  LEU A 750     7940   5980   7639   2029   -730   1094       C  
-ATOM   5607  CG  LEU A 750      15.063  -2.279 -21.133  1.00 55.99           C  
-ANISOU 5607  CG  LEU A 750     7925   6194   7155   1996   -801    539       C  
-ATOM   5608  CD1 LEU A 750      15.696  -2.283 -19.753  1.00 52.14           C  
-ANISOU 5608  CD1 LEU A 750     7526   5519   6764   2057   -604    116       C  
-ATOM   5609  CD2 LEU A 750      15.037  -3.679 -21.713  1.00 54.30           C  
-ANISOU 5609  CD2 LEU A 750     7747   6286   6600   2042  -1233    380       C  
-ATOM   5610  N   GLY A 751      15.562   1.137 -20.530  1.00 69.68           N  
-ANISOU 5610  N   GLY A 751     9557   7412   9505   1811    170    913       N  
-ATOM   5611  CA  GLY A 751      16.729   1.882 -20.968  1.00 69.71           C  
-ANISOU 5611  CA  GLY A 751     9552   7585   9348   1682    376    747       C  
-ATOM   5612  C   GLY A 751      16.508   3.384 -20.986  1.00 70.50           C  
-ANISOU 5612  C   GLY A 751     9579   7445   9762   1603    740   1099       C  
-ATOM   5613  O   GLY A 751      17.118   4.100 -21.783  1.00 71.59           O  
-ANISOU 5613  O   GLY A 751     9672   7744   9784   1476    865   1166       O  
-ATOM   5614  N   ARG A 752      15.639   3.863 -20.100  1.00 59.81           N  
-ANISOU 5614  N   ARG A 752     8215   5705   8805   1677    912   1322       N  
-ATOM   5615  CA  ARG A 752      15.281   5.277 -20.053  1.00 60.68           C  
-ANISOU 5615  CA  ARG A 752     8255   5551   9248   1616   1251   1689       C  
-ATOM   5616  C   ARG A 752      16.070   6.012 -18.980  1.00 55.41           C  
-ANISOU 5616  C   ARG A 752     7639   4678   8736   1608   1601   1399       C  
-ATOM   5617  O   ARG A 752      15.932   7.221 -18.816  1.00 56.44           O  
-ANISOU 5617  O   ARG A 752     7724   4582   9139   1556   1911   1639       O  
-ATOM   5618  CB  ARG A 752      13.785   5.436 -19.764  1.00 67.10           C  
-ANISOU 5618  CB  ARG A 752     9019   6052  10425   1701   1240   2149       C  
-ATOM   5619  CG  ARG A 752      12.874   4.599 -20.653  1.00 78.40           C  
-ANISOU 5619  CG  ARG A 752    10406   7644  11740   1733    875   2429       C  
-ATOM   5620  CD  ARG A 752      12.164   5.462 -21.689  1.00 89.70           C  
-ANISOU 5620  CD  ARG A 752    11726   9057  13298   1648    928   2979       C  
-ATOM   5621  NE  ARG A 752      10.923   6.036 -21.180  1.00 97.58           N  
-ANISOU 5621  NE  ARG A 752    12674   9678  14725   1713   1060   3398       N  
-ATOM   5622  CZ  ARG A 752       9.709   5.639 -21.549  1.00104.10           C  
-ANISOU 5622  CZ  ARG A 752    13372  10565  15617   1717    872   3674       C  
-ATOM   5623  NH1 ARG A 752       8.636   6.219 -21.029  1.00108.94           N  
-ANISOU 5623  NH1 ARG A 752    13813  11019  16559   1698   1053   3882       N  
-ATOM   5624  NH2 ARG A 752       9.567   4.669 -22.444  1.00105.79           N  
-ANISOU 5624  NH2 ARG A 752    13610  11024  15561   1735    505   3720       N  
-ATOM   5625  N   GLY A 753      16.893   5.278 -18.243  1.00 60.70           N  
-ANISOU 5625  N   GLY A 753     8405   5424   9233   1661   1547    882       N  
-ATOM   5626  CA  GLY A 753      17.583   5.855 -17.107  1.00 55.59           C  
-ANISOU 5626  CA  GLY A 753     7818   4563   8741   1673   1856    584       C  
-ATOM   5627  C   GLY A 753      18.944   6.406 -17.451  1.00 52.55           C  
-ANISOU 5627  C   GLY A 753     7440   4380   8148   1547   2026    307       C  
-ATOM   5628  O   GLY A 753      19.673   6.870 -16.580  1.00 49.64           O  
-ANISOU 5628  O   GLY A 753     7123   3871   7867   1546   2276     18       O  
-ATOM   5629  N   THR A 754      19.288   6.354 -18.731  1.00 47.21           N  
-ANISOU 5629  N   THR A 754     6712   4032   7193   1442   1891    397       N  
-ATOM   5630  CA  THR A 754      20.614   6.751 -19.181  1.00 47.38           C  
-ANISOU 5630  CA  THR A 754     6739   4296   6969   1320   2014    123       C  
-ATOM   5631  C   THR A 754      20.548   7.488 -20.514  1.00 50.98           C  
-ANISOU 5631  C   THR A 754     7095   4917   7357   1185   2047    501       C  
-ATOM   5632  O   THR A 754      19.477   7.627 -21.102  1.00 51.88           O  
-ANISOU 5632  O   THR A 754     7141   4970   7601   1191   1957    963       O  
-ATOM   5633  CB  THR A 754      21.528   5.515 -19.325  1.00 43.46           C  
-ANISOU 5633  CB  THR A 754     6316   4147   6051   1339   1742   -374       C  
-ATOM   5634  OG1 THR A 754      22.851   5.924 -19.692  1.00 45.23           O  
-ANISOU 5634  OG1 THR A 754     6544   4593   6047   1222   1878   -657       O  
-ATOM   5635  CG2 THR A 754      20.981   4.567 -20.376  1.00 41.40           C  
-ANISOU 5635  CG2 THR A 754     6026   4158   5546   1352   1361   -205       C  
-ATOM   5636  N   SER A 755      21.698   7.968 -20.974  1.00 52.79           N  
-ANISOU 5636  N   SER A 755     7318   5352   7389   1065   2182    303       N  
-ATOM   5637  CA  SER A 755      21.821   8.571 -22.296  1.00 56.38           C  
-ANISOU 5637  CA  SER A 755     7688   6019   7716    930   2197    596       C  
-ATOM   5638  C   SER A 755      21.145   7.693 -23.343  1.00 57.31           C  
-ANISOU 5638  C   SER A 755     7773   6379   7622    949   1827    816       C  
-ATOM   5639  O   SER A 755      21.363   6.486 -23.373  1.00 56.11           O  
-ANISOU 5639  O   SER A 755     7678   6441   7202   1012   1537    525       O  
-ATOM   5640  CB  SER A 755      23.296   8.763 -22.643  1.00 58.20           C  
-ANISOU 5640  CB  SER A 755     7936   6524   7655    818   2294    225       C  
-ATOM   5641  OG  SER A 755      23.460   9.044 -24.022  1.00 64.45           O  
-ANISOU 5641  OG  SER A 755     8655   7593   8240    698   2229    455       O  
-ATOM   5642  N   THR A 756      20.332   8.299 -24.202  1.00 49.77           N  
-ANISOU 5642  N   THR A 756     6730   5391   6790    894   1836   1328       N  
-ATOM   5643  CA  THR A 756      19.494   7.539 -25.126  1.00 50.02           C  
-ANISOU 5643  CA  THR A 756     6726   5595   6683    924   1495   1601       C  
-ATOM   5644  C   THR A 756      20.268   6.654 -26.094  1.00 49.23           C  
-ANISOU 5644  C   THR A 756     6646   5947   6112    877   1217   1349       C  
-ATOM   5645  O   THR A 756      19.771   5.613 -26.518  1.00 48.22           O  
-ANISOU 5645  O   THR A 756     6529   5978   5814    941    878   1378       O  
-ATOM   5646  CB  THR A 756      18.540   8.447 -25.925  1.00 54.00           C  
-ANISOU 5646  CB  THR A 756     7129   5987   7402    863   1574   2203       C  
-ATOM   5647  OG1 THR A 756      19.211   9.664 -26.271  1.00 54.74           O  
-ANISOU 5647  OG1 THR A 756     7179   6083   7536    729   1880   2279       O  
-ATOM   5648  CG2 THR A 756      17.305   8.777 -25.099  1.00 53.00           C  
-ANISOU 5648  CG2 THR A 756     6984   5446   7706    960   1671   2518       C  
-ATOM   5649  N   TYR A 757      21.473   7.065 -26.464  1.00 44.64           N  
-ANISOU 5649  N   TYR A 757     6067   5575   5320    766   1355   1108       N  
-ATOM   5650  CA  TYR A 757      22.297   6.202 -27.295  1.00 44.27           C  
-ANISOU 5650  CA  TYR A 757     6046   5958   4818    728   1102    822       C  
-ATOM   5651  C   TYR A 757      22.576   4.909 -26.544  1.00 39.38           C  
-ANISOU 5651  C   TYR A 757     5521   5408   4033    846    875    365       C  
-ATOM   5652  O   TYR A 757      22.321   3.822 -27.060  1.00 38.90           O  
-ANISOU 5652  O   TYR A 757     5480   5571   3731    897    529    322       O  
-ATOM   5653  CB  TYR A 757      23.597   6.898 -27.708  1.00 49.95           C  
-ANISOU 5653  CB  TYR A 757     6752   6871   5355    591   1316    615       C  
-ATOM   5654  CG  TYR A 757      23.384   8.059 -28.653  1.00 56.55           C  
-ANISOU 5654  CG  TYR A 757     7494   7705   6286    465   1493   1060       C  
-ATOM   5655  CD1 TYR A 757      22.318   8.066 -29.540  1.00 60.20           C  
-ANISOU 5655  CD1 TYR A 757     7893   8186   6796    463   1331   1542       C  
-ATOM   5656  CD2 TYR A 757      24.241   9.153 -28.649  1.00 59.06           C  
-ANISOU 5656  CD2 TYR A 757     7787   8001   6653    348   1822   1002       C  
-ATOM   5657  CE1 TYR A 757      22.117   9.128 -30.403  1.00 64.89           C  
-ANISOU 5657  CE1 TYR A 757     8403   8776   7477    348   1491   1951       C  
-ATOM   5658  CE2 TYR A 757      24.045  10.217 -29.503  1.00 63.58           C  
-ANISOU 5658  CE2 TYR A 757     8275   8569   7314    233   1984   1410       C  
-ATOM   5659  CZ  TYR A 757      22.983  10.198 -30.379  1.00 66.19           C  
-ANISOU 5659  CZ  TYR A 757     8545   8918   7685    234   1818   1883       C  
-ATOM   5660  OH  TYR A 757      22.779  11.253 -31.237  1.00 69.37           O  
-ANISOU 5660  OH  TYR A 757     8866   9316   8175    119   1976   2292       O  
-ATOM   5661  N   ASP A 758      23.084   5.036 -25.319  1.00 56.54           N  
-ANISOU 5661  N   ASP A 758     7756   7384   6342    891   1070     27       N  
-ATOM   5662  CA  ASP A 758      23.337   3.873 -24.473  1.00 51.38           C  
-ANISOU 5662  CA  ASP A 758     7198   6756   5567   1009    883   -412       C  
-ATOM   5663  C   ASP A 758      22.036   3.145 -24.151  1.00 48.22           C  
-ANISOU 5663  C   ASP A 758     6807   6186   5327   1139    655   -191       C  
-ATOM   5664  O   ASP A 758      21.985   1.913 -24.160  1.00 45.59           O  
-ANISOU 5664  O   ASP A 758     6527   6020   4775   1220    339   -406       O  
-ATOM   5665  CB  ASP A 758      24.044   4.273 -23.178  1.00 52.71           C  
-ANISOU 5665  CB  ASP A 758     7429   6704   5896   1032   1165   -773       C  
-ATOM   5666  CG  ASP A 758      25.383   4.948 -23.424  1.00 56.32           C  
-ANISOU 5666  CG  ASP A 758     7881   7327   6192    906   1388  -1027       C  
-ATOM   5667  OD1 ASP A 758      25.725   5.881 -22.661  1.00 59.23           O  
-ANISOU 5667  OD1 ASP A 758     8253   7452   6800    879   1721  -1084       O  
-ATOM   5668  OD2 ASP A 758      26.096   4.541 -24.371  1.00 58.87           O  
-ANISOU 5668  OD2 ASP A 758     8196   8023   6150    836   1231  -1174       O  
-ATOM   5669  N   GLY A 759      20.988   3.909 -23.866  1.00 36.96           N  
-ANISOU 5669  N   GLY A 759     5329   4427   4287   1160    815    239       N  
-ATOM   5670  CA  GLY A 759      19.693   3.331 -23.566  1.00 34.50           C  
-ANISOU 5670  CA  GLY A 759     5015   3931   4164   1279    624    492       C  
-ATOM   5671  C   GLY A 759      19.186   2.467 -24.699  1.00 35.49           C  
-ANISOU 5671  C   GLY A 759     5112   4335   4039   1285    248    674       C  
-ATOM   5672  O   GLY A 759      18.648   1.379 -24.473  1.00 34.17           O  
-ANISOU 5672  O   GLY A 759     4984   4187   3812   1393    -36    605       O  
-ATOM   5673  N   PHE A 760      19.348   2.964 -25.922  1.00 40.16           N  
-ANISOU 5673  N   PHE A 760     5635   5139   4486   1168    248    915       N  
-ATOM   5674  CA  PHE A 760      18.974   2.209 -27.109  1.00 41.38           C  
-ANISOU 5674  CA  PHE A 760     5761   5588   4374   1160   -100   1083       C  
-ATOM   5675  C   PHE A 760      19.905   1.013 -27.279  1.00 40.76           C  
-ANISOU 5675  C   PHE A 760     5759   5860   3868   1181   -365    589       C  
-ATOM   5676  O   PHE A 760      19.471  -0.079 -27.658  1.00 38.38           O  
-ANISOU 5676  O   PHE A 760     5477   5720   3386   1249   -716    581       O  
-ATOM   5677  CB  PHE A 760      19.019   3.088 -28.357  1.00 43.49           C  
-ANISOU 5677  CB  PHE A 760     5941   6000   4582   1024    -13   1437       C  
-ATOM   5678  CG  PHE A 760      19.018   2.305 -29.628  1.00 43.33           C  
-ANISOU 5678  CG  PHE A 760     5908   6355   4202    998   -356   1494       C  
-ATOM   5679  CD1 PHE A 760      17.835   1.798 -30.136  1.00 45.11           C  
-ANISOU 5679  CD1 PHE A 760     6098   6565   4476   1056   -622   1854       C  
-ATOM   5680  CD2 PHE A 760      20.201   2.044 -30.299  1.00 41.99           C  
-ANISOU 5680  CD2 PHE A 760     5760   6553   3642    919   -418   1180       C  
-ATOM   5681  CE1 PHE A 760      17.829   1.057 -31.293  1.00 46.15           C  
-ANISOU 5681  CE1 PHE A 760     6221   7039   4274   1036   -944   1901       C  
-ATOM   5682  CE2 PHE A 760      20.198   1.300 -31.453  1.00 44.86           C  
-ANISOU 5682  CE2 PHE A 760     6115   7260   3669    900   -737   1225       C  
-ATOM   5683  CZ  PHE A 760      19.014   0.804 -31.947  1.00 47.11           C  
-ANISOU 5683  CZ  PHE A 760     6368   7524   4006    960  -1002   1584       C  
-ATOM   5684  N   GLY A 761      21.189   1.224 -27.002  1.00 52.22           N  
-ANISOU 5684  N   GLY A 761     7251   7429   5160   1124   -198    177       N  
-ATOM   5685  CA  GLY A 761      22.153   0.141 -27.037  1.00 52.14           C  
-ANISOU 5685  CA  GLY A 761     7317   7731   4761   1147   -417   -329       C  
-ATOM   5686  C   GLY A 761      21.687  -1.015 -26.175  1.00 49.83           C  
-ANISOU 5686  C   GLY A 761     7100   7343   4490   1296   -649   -540       C  
-ATOM   5687  O   GLY A 761      21.609  -2.156 -26.639  1.00 47.82           O  
-ANISOU 5687  O   GLY A 761     6877   7331   3962   1346  -1000   -657       O  
-ATOM   5688  N   LEU A 762      21.370  -0.708 -24.917  1.00 45.96           N  
-ANISOU 5688  N   LEU A 762     6640   6494   4328   1369   -451   -583       N  
-ATOM   5689  CA  LEU A 762      20.864  -1.700 -23.977  1.00 43.36           C  
-ANISOU 5689  CA  LEU A 762     6381   6024   4070   1513   -632   -760       C  
-ATOM   5690  C   LEU A 762      19.576  -2.328 -24.487  1.00 42.89           C  
-ANISOU 5690  C   LEU A 762     6285   5953   4057   1580   -931   -385       C  
-ATOM   5691  O   LEU A 762      19.461  -3.552 -24.564  1.00 41.18           O  
-ANISOU 5691  O   LEU A 762     6118   5902   3627   1657  -1263   -566       O  
-ATOM   5692  CB  LEU A 762      20.610  -1.060 -22.615  1.00 44.49           C  
-ANISOU 5692  CB  LEU A 762     6548   5753   4605   1571   -332   -778       C  
-ATOM   5693  CG  LEU A 762      21.826  -0.570 -21.828  1.00 46.01           C  
-ANISOU 5693  CG  LEU A 762     6793   5902   4786   1534    -47  -1202       C  
-ATOM   5694  CD1 LEU A 762      21.379   0.193 -20.589  1.00 45.42           C  
-ANISOU 5694  CD1 LEU A 762     6729   5390   5140   1588    258  -1116       C  
-ATOM   5695  CD2 LEU A 762      22.738  -1.733 -21.459  1.00 45.46           C  
-ANISOU 5695  CD2 LEU A 762     6823   6058   4391   1588   -250  -1772       C  
-ATOM   5696  N   ALA A 763      18.606  -1.491 -24.831  1.00 35.99           N  
-ANISOU 5696  N   ALA A 763     5326   4883   3467   1551   -814    137       N  
-ATOM   5697  CA  ALA A 763      17.355  -1.983 -25.389  1.00 37.26           C  
-ANISOU 5697  CA  ALA A 763     5442   5028   3688   1604  -1083    534       C  
-ATOM   5698  C   ALA A 763      17.604  -3.023 -26.484  1.00 38.89           C  
-ANISOU 5698  C   ALA A 763     5660   5643   3473   1591  -1463    433       C  
-ATOM   5699  O   ALA A 763      17.103  -4.146 -26.413  1.00 37.85           O  
-ANISOU 5699  O   ALA A 763     5564   5568   3248   1688  -1779    371       O  
-ATOM   5700  CB  ALA A 763      16.538  -0.829 -25.931  1.00 37.50           C  
-ANISOU 5700  CB  ALA A 763     5369   4883   3998   1537   -900   1097       C  
-ATOM   5701  N   TRP A 764      18.394  -2.640 -27.485  1.00 40.18           N  
-ANISOU 5701  N   TRP A 764     5041   6116   4109   -144    265   -249       N  
-ATOM   5702  CA  TRP A 764      18.667  -3.488 -28.641  1.00 41.51           C  
-ANISOU 5702  CA  TRP A 764     5321   6214   4237   -211    305   -348       C  
-ATOM   5703  C   TRP A 764      19.376  -4.772 -28.245  1.00 40.44           C  
-ANISOU 5703  C   TRP A 764     5173   5975   4219   -164    284   -445       C  
-ATOM   5704  O   TRP A 764      18.917  -5.869 -28.561  1.00 39.93           O  
-ANISOU 5704  O   TRP A 764     5189   5856   4126   -215    220   -446       O  
-ATOM   5705  CB  TRP A 764      19.524  -2.725 -29.660  1.00 45.14           C  
-ANISOU 5705  CB  TRP A 764     5817   6666   4667   -232    462   -456       C  
-ATOM   5706  CG  TRP A 764      19.920  -3.525 -30.869  1.00 47.63           C  
-ANISOU 5706  CG  TRP A 764     6251   6909   4938   -296    526   -574       C  
-ATOM   5707  CD1 TRP A 764      20.923  -4.446 -30.952  1.00 48.62           C  
-ANISOU 5707  CD1 TRP A 764     6380   6932   5160   -258    580   -716       C  
-ATOM   5708  CD2 TRP A 764      19.331  -3.454 -32.173  1.00 49.33           C  
-ANISOU 5708  CD2 TRP A 764     6600   7149   4995   -407    549   -562       C  
-ATOM   5709  NE1 TRP A 764      20.982  -4.966 -32.221  1.00 50.76           N  
-ANISOU 5709  NE1 TRP A 764     6787   7157   5343   -339    641   -800       N  
-ATOM   5710  CE2 TRP A 764      20.018  -4.370 -32.991  1.00 50.66           C  
-ANISOU 5710  CE2 TRP A 764     6857   7223   5167   -437    620   -709       C  
-ATOM   5711  CE3 TRP A 764      18.286  -2.708 -32.726  1.00 49.71           C  
-ANISOU 5711  CE3 TRP A 764     6700   7291   4896   -482    516   -437       C  
-ATOM   5712  CZ2 TRP A 764      19.694  -4.560 -34.331  1.00 52.12           C  
-ANISOU 5712  CZ2 TRP A 764     7190   7409   5205   -547    658   -743       C  
-ATOM   5713  CZ3 TRP A 764      17.966  -2.898 -34.057  1.00 51.12           C  
-ANISOU 5713  CZ3 TRP A 764     7016   7477   4930   -591    544   -461       C  
-ATOM   5714  CH2 TRP A 764      18.668  -3.816 -34.844  1.00 52.24           C  
-ANISOU 5714  CH2 TRP A 764     7252   7527   5070   -627    614   -616       C  
-ATOM   5715  N   ALA A 765      20.504  -4.630 -27.562  1.00 47.17           N  
-ANISOU 5715  N   ALA A 765     5923   6798   5203    -68    338   -527       N  
-ATOM   5716  CA  ALA A 765      21.326  -5.779 -27.217  1.00 46.80           C  
-ANISOU 5716  CA  ALA A 765     5852   6650   5278     -6    334   -621       C  
-ATOM   5717  C   ALA A 765      20.596  -6.772 -26.311  1.00 45.77           C  
-ANISOU 5717  C   ALA A 765     5712   6498   5182     12    186   -527       C  
-ATOM   5718  O   ALA A 765      20.822  -7.980 -26.409  1.00 46.56           O  
-ANISOU 5718  O   ALA A 765     5858   6497   5334     20    166   -581       O  
-ATOM   5719  CB  ALA A 765      22.630  -5.326 -26.583  1.00 44.99           C  
-ANISOU 5719  CB  ALA A 765     5494   6417   5183     94    408   -706       C  
-ATOM   5720  N   ILE A 766      19.722  -6.274 -25.435  1.00 35.01           N  
-ANISOU 5720  N   ILE A 766     4294   5221   3789     19     91   -386       N  
-ATOM   5721  CA  ILE A 766      18.959  -7.166 -24.567  1.00 34.54           C  
-ANISOU 5721  CA  ILE A 766     4223   5148   3751     28    -46   -283       C  
-ATOM   5722  C   ILE A 766      17.871  -7.870 -25.362  1.00 35.78           C  
-ANISOU 5722  C   ILE A 766     4506   5287   3800    -85   -108   -230       C  
-ATOM   5723  O   ILE A 766      17.638  -9.068 -25.195  1.00 37.76           O  
-ANISOU 5723  O   ILE A 766     4801   5461   4085   -100   -178   -224       O  
-ATOM   5724  CB  ILE A 766      18.306  -6.427 -23.389  1.00 33.17           C  
-ANISOU 5724  CB  ILE A 766     3955   5077   3570     68   -123   -145       C  
-ATOM   5725  CG1 ILE A 766      19.365  -5.931 -22.406  1.00 30.98           C  
-ANISOU 5725  CG1 ILE A 766     3552   4813   3405    177    -89   -196       C  
-ATOM   5726  CG2 ILE A 766      17.320  -7.337 -22.680  1.00 32.97           C  
-ANISOU 5726  CG2 ILE A 766     3938   5049   3541     54   -260    -24       C  
-ATOM   5727  CD1 ILE A 766      18.838  -4.897 -21.429  1.00 26.66           C  
-ANISOU 5727  CD1 ILE A 766     2927   4373   2831    207   -127    -87       C  
-ATOM   5728  N   SER A 767      17.201  -7.123 -26.230  1.00 37.95           N  
-ANISOU 5728  N   SER A 767     4839   5634   3946   -171    -83   -188       N  
-ATOM   5729  CA  SER A 767      16.174  -7.713 -27.076  1.00 39.14           C  
-ANISOU 5729  CA  SER A 767     5108   5784   3981   -293   -143   -139       C  
-ATOM   5730  C   SER A 767      16.781  -8.836 -27.906  1.00 42.30           C  
-ANISOU 5730  C   SER A 767     5617   6055   4400   -331    -98   -282       C  
-ATOM   5731  O   SER A 767      16.129  -9.837 -28.198  1.00 41.87           O  
-ANISOU 5731  O   SER A 767     5652   5952   4306   -411   -172   -262       O  
-ATOM   5732  CB  SER A 767      15.555  -6.658 -27.988  1.00 38.11           C  
-ANISOU 5732  CB  SER A 767     5020   5753   3708   -370   -108    -85       C  
-ATOM   5733  OG  SER A 767      14.943  -5.634 -27.230  1.00 32.80           O  
-ANISOU 5733  OG  SER A 767     4253   5190   3020   -330   -143     50       O  
-ATOM   5734  N   GLU A 768      18.043  -8.662 -28.274  1.00 48.73           N  
-ANISOU 5734  N   GLU A 768     6424   6814   5279   -274     30   -427       N  
-ATOM   5735  CA  GLU A 768      18.752  -9.645 -29.075  1.00 53.66           C  
-ANISOU 5735  CA  GLU A 768     7148   7311   5931   -292    101   -576       C  
-ATOM   5736  C   GLU A 768      19.115 -10.861 -28.234  1.00 53.83           C  
-ANISOU 5736  C   GLU A 768     7143   7221   6089   -219     47   -599       C  
-ATOM   5737  O   GLU A 768      19.010 -11.999 -28.690  1.00 53.94           O  
-ANISOU 5737  O   GLU A 768     7266   7126   6101   -267     33   -653       O  
-ATOM   5738  CB  GLU A 768      20.013  -9.016 -29.661  1.00 58.74           C  
-ANISOU 5738  CB  GLU A 768     7772   7938   6610   -244    264   -716       C  
-ATOM   5739  CG  GLU A 768      20.781  -9.914 -30.594  1.00 66.77           C  
-ANISOU 5739  CG  GLU A 768     8895   8830   7646   -259    363   -878       C  
-ATOM   5740  CD  GLU A 768      21.986  -9.218 -31.173  1.00 72.60           C  
-ANISOU 5740  CD  GLU A 768     9602   9566   8415   -215    529  -1005       C  
-ATOM   5741  OE1 GLU A 768      21.798  -8.297 -31.995  1.00 75.02           O  
-ANISOU 5741  OE1 GLU A 768     9953   9949   8604   -283    592  -1000       O  
-ATOM   5742  OE2 GLU A 768      23.121  -9.575 -30.793  1.00 76.37           O  
-ANISOU 5742  OE2 GLU A 768    10006   9972   9038   -110    598  -1101       O  
-ATOM   5743  N   TYR A 769      19.541 -10.615 -27.000  1.00 50.41           N  
-ANISOU 5743  N   TYR A 769     6570   6811   5772   -104     17   -556       N  
-ATOM   5744  CA  TYR A 769      19.917 -11.704 -26.110  1.00 51.65           C  
-ANISOU 5744  CA  TYR A 769     6689   6872   6063    -21    -39   -561       C  
-ATOM   5745  C   TYR A 769      18.717 -12.595 -25.822  1.00 50.77           C  
-ANISOU 5745  C   TYR A 769     6646   6737   5909    -94   -174   -448       C  
-ATOM   5746  O   TYR A 769      18.847 -13.816 -25.747  1.00 51.80           O  
-ANISOU 5746  O   TYR A 769     6835   6743   6105    -86   -200   -483       O  
-ATOM   5747  CB  TYR A 769      20.488 -11.156 -24.808  1.00 53.38           C  
-ANISOU 5747  CB  TYR A 769     6743   7148   6391    104    -60   -518       C  
-ATOM   5748  CG  TYR A 769      21.170 -12.190 -23.941  1.00 58.20           C  
-ANISOU 5748  CG  TYR A 769     7299   7661   7153    211    -96   -539       C  
-ATOM   5749  CD1 TYR A 769      22.538 -12.403 -24.030  1.00 61.23           C  
-ANISOU 5749  CD1 TYR A 769     7632   7974   7657    306      3   -669       C  
-ATOM   5750  CD2 TYR A 769      20.452 -12.942 -23.019  1.00 59.49           C  
-ANISOU 5750  CD2 TYR A 769     7457   7807   7341    219   -226   -421       C  
-ATOM   5751  CE1 TYR A 769      23.173 -13.340 -23.232  1.00 63.38           C  
-ANISOU 5751  CE1 TYR A 769     7848   8160   8072    414    -31   -677       C  
-ATOM   5752  CE2 TYR A 769      21.079 -13.881 -22.216  1.00 62.70           C  
-ANISOU 5752  CE2 TYR A 769     7816   8122   7885    322   -259   -429       C  
-ATOM   5753  CZ  TYR A 769      22.439 -14.074 -22.328  1.00 63.98           C  
-ANISOU 5753  CZ  TYR A 769     7927   8216   8166    422   -164   -555       C  
-ATOM   5754  OH  TYR A 769      23.066 -15.005 -21.536  1.00 67.27           O  
-ANISOU 5754  OH  TYR A 769     8291   8545   8722    533   -199   -552       O  
-ATOM   5755  N   ILE A 770      17.549 -11.977 -25.669  1.00 39.85           N  
-ANISOU 5755  N   ILE A 770     5252   5471   4418   -166   -256   -310       N  
-ATOM   5756  CA  ILE A 770      16.316 -12.713 -25.419  1.00 38.72           C  
-ANISOU 5756  CA  ILE A 770     5160   5327   4223   -250   -386   -189       C  
-ATOM   5757  C   ILE A 770      15.863 -13.539 -26.624  1.00 42.29           C  
-ANISOU 5757  C   ILE A 770     5778   5703   4588   -385   -385   -248       C  
-ATOM   5758  O   ILE A 770      15.814 -14.764 -26.560  1.00 43.52           O  
-ANISOU 5758  O   ILE A 770     6006   5738   4793   -406   -425   -273       O  
-ATOM   5759  CB  ILE A 770      15.174 -11.768 -25.014  1.00 33.81           C  
-ANISOU 5759  CB  ILE A 770     4476   4863   3507   -290   -462    -25       C  
-ATOM   5760  CG1 ILE A 770      15.508 -11.069 -23.698  1.00 30.37           C  
-ANISOU 5760  CG1 ILE A 770     3891   4496   3154   -165   -475     39       C  
-ATOM   5761  CG2 ILE A 770      13.858 -12.529 -24.906  1.00 33.95           C  
-ANISOU 5761  CG2 ILE A 770     4547   4890   3464   -395   -591    100       C  
-ATOM   5762  CD1 ILE A 770      14.334 -10.365 -23.074  1.00 29.46           C  
-ANISOU 5762  CD1 ILE A 770     3712   4515   2965   -189   -558    211       C  
-ATOM   5763  N   ALA A 771      15.533 -12.866 -27.722  1.00 51.84           N  
-ANISOU 5763  N   ALA A 771     7052   6981   5663   -479   -340   -268       N  
-ATOM   5764  CA  ALA A 771      14.988 -13.535 -28.905  1.00 55.21           C  
-ANISOU 5764  CA  ALA A 771     7640   7360   5977   -627   -350   -315       C  
-ATOM   5765  C   ALA A 771      15.876 -14.654 -29.451  1.00 57.54           C  
-ANISOU 5765  C   ALA A 771     8047   7478   6339   -619   -272   -485       C  
-ATOM   5766  O   ALA A 771      15.381 -15.622 -30.027  1.00 57.71           O  
-ANISOU 5766  O   ALA A 771     8203   7419   6307   -730   -311   -514       O  
-ATOM   5767  CB  ALA A 771      14.692 -12.514 -29.999  1.00 55.78           C  
-ANISOU 5767  CB  ALA A 771     7756   7542   5897   -710   -298   -318       C  
-ATOM   5768  N   THR A 772      17.185 -14.518 -29.268  1.00 54.65           N  
-ANISOU 5768  N   THR A 772     7624   7051   6089   -488   -158   -598       N  
-ATOM   5769  CA  THR A 772      18.130 -15.494 -29.800  1.00 58.54           C  
-ANISOU 5769  CA  THR A 772     8210   7376   6656   -458    -61   -764       C  
-ATOM   5770  C   THR A 772      18.636 -16.488 -28.758  1.00 57.93           C  
-ANISOU 5770  C   THR A 772     8082   7177   6753   -343    -94   -764       C  
-ATOM   5771  O   THR A 772      18.346 -17.679 -28.834  1.00 60.58           O  
-ANISOU 5771  O   THR A 772     8523   7385   7110   -389   -135   -782       O  
-ATOM   5772  CB  THR A 772      19.348 -14.814 -30.450  1.00 60.95           C  
-ANISOU 5772  CB  THR A 772     8494   7681   6982   -391    106   -905       C  
-ATOM   5773  OG1 THR A 772      18.937 -14.123 -31.636  1.00 64.06           O  
-ANISOU 5773  OG1 THR A 772     8977   8156   7206   -511    151   -927       O  
-ATOM   5774  CG2 THR A 772      20.387 -15.856 -30.818  1.00 64.88           C  
-ANISOU 5774  CG2 THR A 772     9064   8003   7584   -331    211  -1068       C  
-ATOM   5775  N   LYS A 773      19.412 -15.999 -27.798  1.00 56.49           N  
-ANISOU 5775  N   LYS A 773     7741   7029   6692   -196    -75   -745       N  
-ATOM   5776  CA  LYS A 773      19.994 -16.863 -26.781  1.00 55.23           C  
-ANISOU 5776  CA  LYS A 773     7519   6766   6700    -71   -104   -739       C  
-ATOM   5777  C   LYS A 773      18.902 -17.618 -26.024  1.00 53.74           C  
-ANISOU 5777  C   LYS A 773     7353   6558   6506   -122   -257   -596       C  
-ATOM   5778  O   LYS A 773      18.933 -18.849 -25.924  1.00 55.09           O  
-ANISOU 5778  O   LYS A 773     7604   6581   6748   -118   -279   -619       O  
-ATOM   5779  CB  LYS A 773      20.854 -16.041 -25.818  1.00 55.14           C  
-ANISOU 5779  CB  LYS A 773     7321   6836   6794     76    -82   -718       C  
-ATOM   5780  CG  LYS A 773      20.796 -16.489 -24.367  1.00 56.06           C  
-ANISOU 5780  CG  LYS A 773     7333   6945   7021    172   -192   -604       C  
-ATOM   5781  CD  LYS A 773      21.568 -17.771 -24.129  1.00 58.20           C  
-ANISOU 5781  CD  LYS A 773     7630   7044   7440    265   -169   -669       C  
-ATOM   5782  CE  LYS A 773      21.336 -18.292 -22.715  1.00 58.22           C  
-ANISOU 5782  CE  LYS A 773     7549   7040   7533    343   -294   -535       C  
-ATOM   5783  NZ  LYS A 773      21.710 -17.296 -21.669  1.00 56.38           N  
-ANISOU 5783  NZ  LYS A 773     7137   6949   7336    438   -325   -467       N  
-ATOM   5784  N   ILE A 774      17.928 -16.877 -25.504  1.00 55.07           N  
-ANISOU 5784  N   ILE A 774     7455   6875   6594   -170   -355   -448       N  
-ATOM   5785  CA  ILE A 774      16.863 -17.462 -24.695  1.00 51.86           C  
-ANISOU 5785  CA  ILE A 774     7047   6475   6182   -216   -498   -297       C  
-ATOM   5786  C   ILE A 774      15.760 -18.053 -25.563  1.00 51.39           C  
-ANISOU 5786  C   ILE A 774     7140   6387   6000   -394   -553   -278       C  
-ATOM   5787  O   ILE A 774      15.545 -19.258 -25.564  1.00 52.87           O  
-ANISOU 5787  O   ILE A 774     7424   6440   6226   -437   -592   -288       O  
-ATOM   5788  CB  ILE A 774      16.240 -16.420 -23.746  1.00 48.79           C  
-ANISOU 5788  CB  ILE A 774     6519   6261   5757   -190   -576   -141       C  
-ATOM   5789  CG1 ILE A 774      17.291 -15.895 -22.765  1.00 46.67           C  
-ANISOU 5789  CG1 ILE A 774     6103   6023   5608    -24   -539   -155       C  
-ATOM   5790  CG2 ILE A 774      15.067 -17.022 -23.009  1.00 46.52           C  
-ANISOU 5790  CG2 ILE A 774     6236   5988   5451   -251   -715     17       C  
-ATOM   5791  CD1 ILE A 774      16.771 -14.847 -21.811  1.00 46.68           C  
-ANISOU 5791  CD1 ILE A 774     5975   6186   5574      7   -601    -19       C  
-ATOM   5792  N   GLY A 775      15.056 -17.192 -26.287  1.00 42.40           N  
-ANISOU 5792  N   GLY A 775     6021   5377   4713   -501   -558   -246       N  
-ATOM   5793  CA  GLY A 775      13.987 -17.618 -27.169  1.00 43.47           C  
-ANISOU 5793  CA  GLY A 775     6288   5514   4713   -682   -616   -223       C  
-ATOM   5794  C   GLY A 775      12.651 -17.837 -26.486  1.00 44.04           C  
-ANISOU 5794  C   GLY A 775     6327   5660   4746   -762   -767    -40       C  
-ATOM   5795  O   GLY A 775      11.929 -18.769 -26.825  1.00 45.64           O  
-ANISOU 5795  O   GLY A 775     6638   5796   4906   -891   -835    -23       O  
-ATOM   5796  N   ALA A 776      12.308 -16.974 -25.535  1.00 50.14           N  
-ANISOU 5796  N   ALA A 776     6952   6571   5529   -693   -814     96       N  
-ATOM   5797  CA  ALA A 776      11.027 -17.081 -24.838  1.00 51.23           C  
-ANISOU 5797  CA  ALA A 776     7040   6796   5628   -760   -947    280       C  
-ATOM   5798  C   ALA A 776       9.977 -16.138 -25.412  1.00 51.96           C  
-ANISOU 5798  C   ALA A 776     7115   7060   5568   -866   -985    378       C  
-ATOM   5799  O   ALA A 776      10.309 -15.153 -26.062  1.00 51.86           O  
-ANISOU 5799  O   ALA A 776     7091   7120   5493   -850   -908    326       O  
-ATOM   5800  CB  ALA A 776      11.211 -16.803 -23.360  1.00 49.66           C  
-ANISOU 5800  CB  ALA A 776     6695   6640   5532   -618   -979    381       C  
-ATOM   5801  N   PHE A 777       8.706 -16.444 -25.169  1.00 54.30           N  
-ANISOU 5801  N   PHE A 777     7402   7423   5808   -973  -1104    525       N  
-ATOM   5802  CA  PHE A 777       7.629 -15.523 -25.510  1.00 55.11           C  
-ANISOU 5802  CA  PHE A 777     7454   7705   5780  -1053  -1152    652       C  
-ATOM   5803  C   PHE A 777       7.958 -14.203 -24.840  1.00 52.24           C  
-ANISOU 5803  C   PHE A 777     6952   7455   5441   -909  -1098    703       C  
-ATOM   5804  O   PHE A 777       8.153 -14.160 -23.628  1.00 51.90           O  
-ANISOU 5804  O   PHE A 777     6812   7414   5493   -797  -1112    762       O  
-ATOM   5805  CB  PHE A 777       6.280 -16.017 -24.973  1.00 59.55           C  
-ANISOU 5805  CB  PHE A 777     7981   8332   6314  -1152  -1288    828       C  
-ATOM   5806  CG  PHE A 777       5.963 -17.449 -25.312  1.00 66.71           C  
-ANISOU 5806  CG  PHE A 777     9014   9106   7225  -1287  -1351    791       C  
-ATOM   5807  CD1 PHE A 777       5.343 -17.772 -26.507  1.00 70.55           C  
-ANISOU 5807  CD1 PHE A 777     9613   9603   7588  -1467  -1389    762       C  
-ATOM   5808  CD2 PHE A 777       6.263 -18.468 -24.421  1.00 70.07           C  
-ANISOU 5808  CD2 PHE A 777     9449   9398   7777  -1237  -1376    791       C  
-ATOM   5809  CE1 PHE A 777       5.043 -19.085 -26.814  1.00 73.31           C  
-ANISOU 5809  CE1 PHE A 777    10089   9825   7940  -1602  -1446    721       C  
-ATOM   5810  CE2 PHE A 777       5.969 -19.780 -24.723  1.00 73.51           C  
-ANISOU 5810  CE2 PHE A 777    10009   9699   8222  -1362  -1428    758       C  
-ATOM   5811  CZ  PHE A 777       5.357 -20.090 -25.921  1.00 74.78           C  
-ANISOU 5811  CZ  PHE A 777    10288   9865   8261  -1548  -1462    718       C  
-ATOM   5812  N   CYS A 778       8.028 -13.128 -25.614  1.00 61.48           N  
-ANISOU 5812  N   CYS A 778     8119   8717   6525   -914  -1035    680       N  
-ATOM   5813  CA  CYS A 778       8.405 -11.840 -25.049  1.00 57.26           C  
-ANISOU 5813  CA  CYS A 778     7468   8273   6014   -783   -970    712       C  
-ATOM   5814  C   CYS A 778       7.586 -10.703 -25.624  1.00 57.59           C  
-ANISOU 5814  C   CYS A 778     7479   8472   5932   -831   -972    813       C  
-ATOM   5815  O   CYS A 778       7.205 -10.731 -26.786  1.00 58.09           O  
-ANISOU 5815  O   CYS A 778     7628   8559   5884   -949   -979    794       O  
-ATOM   5816  CB  CYS A 778       9.886 -11.562 -25.292  1.00 54.69           C  
-ANISOU 5816  CB  CYS A 778     7162   7860   5758   -683   -842    536       C  
-ATOM   5817  SG  CYS A 778      10.445  -9.998 -24.593  1.00 47.09           S  
-ANISOU 5817  SG  CYS A 778     6064   6996   4831   -534   -758    558       S  
-ATOM   5818  N   MET A 779       7.312  -9.697 -24.806  1.00 52.55           N  
-ANISOU 5818  N   MET A 779     6719   7939   5307   -738   -965    923       N  
-ATOM   5819  CA  MET A 779       6.682  -8.490 -25.312  1.00 53.14           C  
-ANISOU 5819  CA  MET A 779     6759   8151   5280   -754   -944   1014       C  
-ATOM   5820  C   MET A 779       7.406  -7.259 -24.805  1.00 51.35           C  
-ANISOU 5820  C   MET A 779     6456   7954   5100   -614   -841    989       C  
-ATOM   5821  O   MET A 779       7.598  -7.085 -23.604  1.00 51.10           O  
-ANISOU 5821  O   MET A 779     6337   7926   5154   -510   -841   1024       O  
-ATOM   5822  CB  MET A 779       5.196  -8.439 -24.966  1.00 56.59           C  
-ANISOU 5822  CB  MET A 779     7129   8715   5658   -813  -1054   1218       C  
-ATOM   5823  CG  MET A 779       4.347  -9.364 -25.812  1.00 62.75           C  
-ANISOU 5823  CG  MET A 779     7990   9502   6352   -986  -1152   1252       C  
-ATOM   5824  SD  MET A 779       2.582  -9.111 -25.519  1.00 68.07           S  
-ANISOU 5824  SD  MET A 779     8561  10353   6949  -1057  -1273   1503       S  
-ATOM   5825  CE  MET A 779       1.861 -10.087 -26.835  1.00 67.45           C  
-ANISOU 5825  CE  MET A 779     8600  10276   6751  -1280  -1372   1494       C  
-ATOM   5826  N   PHE A 780       7.809  -6.413 -25.747  1.00 49.80           N  
-ANISOU 5826  N   PHE A 780     6300   7778   4843   -620   -752    927       N  
-ATOM   5827  CA  PHE A 780       8.607  -5.243 -25.453  1.00 47.51           C  
-ANISOU 5827  CA  PHE A 780     5957   7500   4595   -505   -640    879       C  
-ATOM   5828  C   PHE A 780       7.884  -3.994 -25.925  1.00 47.01           C  
-ANISOU 5828  C   PHE A 780     5870   7558   4434   -513   -613    994       C  
-ATOM   5829  O   PHE A 780       7.791  -3.739 -27.120  1.00 46.99           O  
-ANISOU 5829  O   PHE A 780     5942   7577   4336   -589   -584    974       O  
-ATOM   5830  CB  PHE A 780       9.960  -5.364 -26.148  1.00 47.46           C  
-ANISOU 5830  CB  PHE A 780     6023   7387   4622   -494   -534    683       C  
-ATOM   5831  CG  PHE A 780      10.982  -4.385 -25.663  1.00 46.04           C  
-ANISOU 5831  CG  PHE A 780     5781   7196   4517   -376   -424    610       C  
-ATOM   5832  CD1 PHE A 780      10.596  -3.198 -25.069  1.00 44.95           C  
-ANISOU 5832  CD1 PHE A 780     5562   7148   4370   -310   -402    714       C  
-ATOM   5833  CD2 PHE A 780      12.333  -4.652 -25.799  1.00 44.84           C  
-ANISOU 5833  CD2 PHE A 780     5651   6941   4445   -334   -340    438       C  
-ATOM   5834  CE1 PHE A 780      11.538  -2.293 -24.617  1.00 44.91           C  
-ANISOU 5834  CE1 PHE A 780     5505   7127   4430   -216   -302    641       C  
-ATOM   5835  CE2 PHE A 780      13.278  -3.754 -25.350  1.00 44.19           C  
-ANISOU 5835  CE2 PHE A 780     5503   6854   4432   -238   -243    371       C  
-ATOM   5836  CZ  PHE A 780      12.881  -2.570 -24.761  1.00 44.29           C  
-ANISOU 5836  CZ  PHE A 780     5444   6954   4430   -185   -226    470       C  
-ATOM   5837  N   ALA A 781       7.361  -3.223 -24.978  1.00 47.05           N  
-ANISOU 5837  N   ALA A 781     5775   7642   4461   -431   -620   1118       N  
-ATOM   5838  CA  ALA A 781       6.755  -1.937 -25.293  1.00 46.95           C  
-ANISOU 5838  CA  ALA A 781     5731   7732   4376   -410   -577   1229       C  
-ATOM   5839  C   ALA A 781       7.792  -0.835 -25.104  1.00 47.28           C  
-ANISOU 5839  C   ALA A 781     5757   7739   4467   -310   -443   1136       C  
-ATOM   5840  O   ALA A 781       8.338  -0.664 -24.013  1.00 46.47           O  
-ANISOU 5840  O   ALA A 781     5594   7605   4459   -216   -416   1099       O  
-ATOM   5841  CB  ALA A 781       5.539  -1.692 -24.422  1.00 46.68           C  
-ANISOU 5841  CB  ALA A 781     5600   7802   4334   -379   -649   1420       C  
-ATOM   5842  N   THR A 782       8.057  -0.086 -26.170  1.00 51.17           N  
-ANISOU 5842  N   THR A 782     6308   8240   4894   -337   -362   1101       N  
-ATOM   5843  CA  THR A 782       9.171   0.853 -26.176  1.00 51.97           C  
-ANISOU 5843  CA  THR A 782     6412   8291   5042   -265   -227    989       C  
-ATOM   5844  C   THR A 782       8.888   2.105 -26.995  1.00 53.95           C  
-ANISOU 5844  C   THR A 782     6690   8600   5210   -269   -148   1055       C  
-ATOM   5845  O   THR A 782       8.039   2.097 -27.887  1.00 56.59           O  
-ANISOU 5845  O   THR A 782     7065   9001   5436   -344   -193   1152       O  
-ATOM   5846  CB  THR A 782      10.430   0.176 -26.740  1.00 50.06           C  
-ANISOU 5846  CB  THR A 782     6238   7942   4840   -296   -174    793       C  
-ATOM   5847  OG1 THR A 782      11.504   1.118 -26.804  1.00 47.80           O  
-ANISOU 5847  OG1 THR A 782     5947   7616   4599   -238    -40    689       O  
-ATOM   5848  CG2 THR A 782      10.158  -0.364 -28.121  1.00 49.23           C  
-ANISOU 5848  CG2 THR A 782     6238   7838   4628   -416   -194    773       C  
-ATOM   5849  N   HIS A 783       9.604   3.180 -26.677  1.00 55.85           N  
-ANISOU 5849  N   HIS A 783     6908   8814   5500   -189    -33   1005       N  
-ATOM   5850  CA AHIS A 783       9.476   4.427 -27.420  0.50 54.72           C  
-ANISOU 5850  CA AHIS A 783     6797   8705   5291   -183     60   1058       C  
-ATOM   5851  CA BHIS A 783       9.490   4.441 -27.399  0.50 54.72           C  
-ANISOU 5851  CA BHIS A 783     6795   8703   5293   -181     61   1057       C  
-ATOM   5852  C   HIS A 783      10.596   4.550 -28.443  1.00 56.29           C  
-ANISOU 5852  C   HIS A 783     7078   8835   5475   -227    164    903       C  
-ATOM   5853  O   HIS A 783      10.647   5.511 -29.213  1.00 56.23           O  
-ANISOU 5853  O   HIS A 783     7114   8842   5409   -235    251    928       O  
-ATOM   5854  CB AHIS A 783       9.472   5.634 -26.481  0.50 53.64           C  
-ANISOU 5854  CB AHIS A 783     6594   8577   5209    -75    132   1110       C  
-ATOM   5855  CB BHIS A 783       9.579   5.623 -26.432  0.50 53.60           C  
-ANISOU 5855  CB BHIS A 783     6588   8564   5213    -72    137   1095       C  
-ATOM   5856  CG AHIS A 783       8.164   5.853 -25.789  0.50 60.17           C  
-ANISOU 5856  CG AHIS A 783     7353   9492   6016    -32     59   1298       C  
-ATOM   5857  CG BHIS A 783      10.901   5.734 -25.738  0.50 50.71           C  
-ANISOU 5857  CG BHIS A 783     6198   8112   4957    -20    213    930       C  
-ATOM   5858  ND1AHIS A 783       7.017   6.205 -26.465  0.50 56.05           N  
-ANISOU 5858  ND1AHIS A 783     6839   9060   5397    -60     24   1465       N  
-ATOM   5859  ND1BHIS A 783      11.599   6.920 -25.650  0.50 57.59           N  
-ANISOU 5859  ND1BHIS A 783     7070   8947   5863     28    341    876       N  
-ATOM   5860  CD2AHIS A 783       7.822   5.775 -24.481  0.50 59.70           C  
-ANISOU 5860  CD2AHIS A 783     7213   9450   6019     39     18   1348       C  
-ATOM   5861  CD2BHIS A 783      11.656   4.808 -25.098  0.50 50.25           C  
-ANISOU 5861  CD2BHIS A 783     6111   7998   4984    -11    175    811       C  
-ATOM   5862  CE1AHIS A 783       6.024   6.333 -25.605  0.50 58.82           C  
-ANISOU 5862  CE1AHIS A 783     7111   9479   5759     -4    -31   1611       C  
-ATOM   5863  CE1BHIS A 783      12.725   6.720 -24.988  0.50 50.81           C  
-ANISOU 5863  CE1BHIS A 783     6179   8025   5103     58    374    728       C  
-ATOM   5864  NE2AHIS A 783       6.485   6.077 -24.395  0.50 54.71           N  
-ANISOU 5864  NE2AHIS A 783     6541   8915   5332     55    -32   1541       N  
-ATOM   5865  NE2BHIS A 783      12.785   5.446 -24.646  0.50 56.09           N  
-ANISOU 5865  NE2BHIS A 783     6826   8681   5804     40    275    690       N  
-ATOM   5866  N   PHE A 784      11.490   3.567 -28.451  1.00 48.43           N  
-ANISOU 5866  N   PHE A 784     6103   7763   4536   -252    159    749       N  
-ATOM   5867  CA  PHE A 784      12.567   3.524 -29.431  1.00 47.22           C  
-ANISOU 5867  CA  PHE A 784     6025   7544   4373   -296    260    595       C  
-ATOM   5868  C   PHE A 784      12.055   2.995 -30.756  1.00 49.45           C  
-ANISOU 5868  C   PHE A 784     6409   7855   4524   -408    222    617       C  
-ATOM   5869  O   PHE A 784      12.124   1.798 -31.020  1.00 49.56           O  
-ANISOU 5869  O   PHE A 784     6466   7833   4532   -468    160    549       O  
-ATOM   5870  CB  PHE A 784      13.711   2.625 -28.964  1.00 42.71           C  
-ANISOU 5870  CB  PHE A 784     5434   6879   3915   -274    272    424       C  
-ATOM   5871  CG  PHE A 784      14.430   3.130 -27.758  1.00 38.14           C  
-ANISOU 5871  CG  PHE A 784     4760   6271   3460   -175    315    376       C  
-ATOM   5872  CD1 PHE A 784      15.252   4.240 -27.842  1.00 35.01           C  
-ANISOU 5872  CD1 PHE A 784     4353   5854   3096   -142    446    311       C  
-ATOM   5873  CD2 PHE A 784      14.306   2.483 -26.540  1.00 35.76           C  
-ANISOU 5873  CD2 PHE A 784     4383   5964   3239   -123    225    393       C  
-ATOM   5874  CE1 PHE A 784      15.929   4.707 -26.728  1.00 32.46           C  
-ANISOU 5874  CE1 PHE A 784     3944   5508   2882    -64    480    260       C  
-ATOM   5875  CE2 PHE A 784      14.978   2.942 -25.426  1.00 32.82           C  
-ANISOU 5875  CE2 PHE A 784     3927   5574   2969    -39    258    347       C  
-ATOM   5876  CZ  PHE A 784      15.789   4.056 -25.519  1.00 30.82           C  
-ANISOU 5876  CZ  PHE A 784     3662   5303   2745    -12    383    277       C  
-ATOM   5877  N   HIS A 785      11.529   3.876 -31.591  1.00 54.19           N  
-ANISOU 5877  N   HIS A 785     7054   8519   5018   -439    259    713       N  
-ATOM   5878  CA AHIS A 785      11.137   3.490 -32.940  0.50 54.91           C  
-ANISOU 5878  CA AHIS A 785     7250   8645   4968   -553    233    727       C  
-ATOM   5879  CA BHIS A 785      11.132   3.469 -32.925  0.50 54.89           C  
-ANISOU 5879  CA BHIS A 785     7246   8642   4966   -553    231    726       C  
-ATOM   5880  C   HIS A 785      12.312   2.802 -33.628  1.00 53.60           C  
-ANISOU 5880  C   HIS A 785     7165   8387   4814   -601    309    526       C  
-ATOM   5881  O   HIS A 785      12.138   1.818 -34.348  1.00 49.24           O  
-ANISOU 5881  O   HIS A 785     6694   7827   4189   -695    254    481       O  
-ATOM   5882  CB AHIS A 785      10.695   4.717 -33.743  0.50 66.97           C  
-ANISOU 5882  CB AHIS A 785     8813  10243   6390   -562    293    842       C  
-ATOM   5883  CB BHIS A 785      10.610   4.663 -33.724  0.50 66.88           C  
-ANISOU 5883  CB BHIS A 785     8800  10237   6376   -564    282    851       C  
-ATOM   5884  CG AHIS A 785      10.612   4.477 -35.220  0.50 74.47           C  
-ANISOU 5884  CG AHIS A 785     9884  11221   7192   -676    301    823       C  
-ATOM   5885  CG BHIS A 785       9.239   5.105 -33.315  0.50 71.48           C  
-ANISOU 5885  CG BHIS A 785     9316  10924   6918   -537    187   1066       C  
-ATOM   5886  ND1AHIS A 785       9.648   3.676 -35.793  0.50 74.60           N  
-ANISOU 5886  ND1AHIS A 785     9945  11307   7094   -778    171    899       N  
-ATOM   5887  ND1BHIS A 785       8.108   4.372 -33.602  0.50 71.91           N  
-ANISOU 5887  ND1BHIS A 785     9376  11062   6885   -615     44   1179       N  
-ATOM   5888  CD2AHIS A 785      11.378   4.933 -36.240  0.50 82.10           C  
-ANISOU 5888  CD2AHIS A 785    10939  12158   8099   -713    424    737       C  
-ATOM   5889  CD2BHIS A 785       8.818   6.199 -32.640  0.50 76.14           C  
-ANISOU 5889  CD2BHIS A 785     9832  11549   7548   -441    220   1189       C  
-ATOM   5890  CE1AHIS A 785       9.822   3.650 -37.102  0.50 78.31           C  
-ANISOU 5890  CE1AHIS A 785    10531  11791   7434   -871    210    856       C  
-ATOM   5891  CE1BHIS A 785       7.048   4.997 -33.123  0.50 73.66           C  
-ANISOU 5891  CE1BHIS A 785     9519  11373   7097   -563     -7   1368       C  
-ATOM   5892  NE2AHIS A 785      10.866   4.403 -37.399  0.50 82.84           N  
-ANISOU 5892  NE2AHIS A 785    11133  12304   8037   -831    366    760       N  
-ATOM   5893  NE2BHIS A 785       7.451   6.109 -32.535  0.50 76.15           N  
-ANISOU 5893  NE2BHIS A 785     9789  11657   7488   -453    101   1377       N  
-ATOM   5894  N   GLU A 786      13.510   3.332 -33.390  1.00 54.32           N  
-ANISOU 5894  N   GLU A 786     7232   8408   4999   -538    439    403       N  
-ATOM   5895  CA  GLU A 786      14.739   2.797 -33.964  1.00 54.36           C  
-ANISOU 5895  CA  GLU A 786     7295   8325   5036   -564    534    210       C  
-ATOM   5896  C   GLU A 786      14.855   1.301 -33.712  1.00 53.26           C  
-ANISOU 5896  C   GLU A 786     7167   8127   4943   -588    450    125       C  
-ATOM   5897  O   GLU A 786      15.377   0.550 -34.534  1.00 54.28           O  
-ANISOU 5897  O   GLU A 786     7384   8202   5038   -649    488      2       O  
-ATOM   5898  CB  GLU A 786      15.954   3.501 -33.357  1.00 54.68           C  
-ANISOU 5898  CB  GLU A 786     7264   8305   5207   -478    659    106       C  
-ATOM   5899  CG  GLU A 786      15.840   5.018 -33.297  1.00 58.81           C  
-ANISOU 5899  CG  GLU A 786     7761   8868   5716   -438    740    195       C  
-ATOM   5900  CD  GLU A 786      15.164   5.517 -32.026  1.00 59.48           C  
-ANISOU 5900  CD  GLU A 786     7745   8991   5863   -357    670    318       C  
-ATOM   5901  OE1 GLU A 786      15.885   5.991 -31.117  1.00 58.98           O  
-ANISOU 5901  OE1 GLU A 786     7604   8888   5916   -283    725    258       O  
-ATOM   5902  OE2 GLU A 786      13.918   5.438 -31.933  1.00 60.50           O  
-ANISOU 5902  OE2 GLU A 786     7872   9194   5923   -369    562    474       O  
-ATOM   5903  N   LEU A 787      14.360   0.874 -32.560  1.00 58.07           N  
-ANISOU 5903  N   LEU A 787     7692   8744   5629   -539    341    192       N  
-ATOM   5904  CA  LEU A 787      14.471  -0.515 -32.143  1.00 55.92           C  
-ANISOU 5904  CA  LEU A 787     7421   8407   5420   -548    260    124       C  
-ATOM   5905  C   LEU A 787      13.840  -1.481 -33.148  1.00 56.31           C  
-ANISOU 5905  C   LEU A 787     7588   8460   5349   -671    190    124       C  
-ATOM   5906  O   LEU A 787      14.303  -2.612 -33.305  1.00 54.82           O  
-ANISOU 5906  O   LEU A 787     7451   8184   5195   -699    182      6       O  
-ATOM   5907  CB  LEU A 787      13.849  -0.690 -30.757  1.00 54.27           C  
-ANISOU 5907  CB  LEU A 787     7105   8225   5291   -482    149    231       C  
-ATOM   5908  CG  LEU A 787      13.920  -2.079 -30.135  1.00 52.95           C  
-ANISOU 5908  CG  LEU A 787     6926   7989   5202   -479     60    184       C  
-ATOM   5909  CD1 LEU A 787      15.298  -2.680 -30.310  1.00 53.53           C  
-ANISOU 5909  CD1 LEU A 787     7023   7949   5367   -450    149     -8       C  
-ATOM   5910  CD2 LEU A 787      13.559  -1.992 -28.669  1.00 51.57           C  
-ANISOU 5910  CD2 LEU A 787     6634   7842   5118   -393    -16    278       C  
-ATOM   5911  N   THR A 788      12.794  -1.024 -33.831  1.00 49.77           N  
-ANISOU 5911  N   THR A 788     6803   7729   4378   -746    141    255       N  
-ATOM   5912  CA  THR A 788      12.026  -1.885 -34.728  1.00 50.81           C  
-ANISOU 5912  CA  THR A 788     7040   7886   4380   -878     51    277       C  
-ATOM   5913  C   THR A 788      12.903  -2.542 -35.789  1.00 52.86           C  
-ANISOU 5913  C   THR A 788     7428   8059   4598   -944    138     95       C  
-ATOM   5914  O   THR A 788      12.599  -3.639 -36.266  1.00 54.36           O  
-ANISOU 5914  O   THR A 788     7708   8216   4731  -1040     71     50       O  
-ATOM   5915  CB  THR A 788      10.884  -1.117 -35.411  1.00 50.81           C  
-ANISOU 5915  CB  THR A 788     7060   8019   4225   -944     -1    448       C  
-ATOM   5916  OG1 THR A 788      11.400   0.089 -35.980  1.00 53.81           O  
-ANISOU 5916  OG1 THR A 788     7457   8421   4568   -912    130    439       O  
-ATOM   5917  CG2 THR A 788       9.807  -0.759 -34.410  1.00 49.01           C  
-ANISOU 5917  CG2 THR A 788     6715   7878   4030   -894   -108    636       C  
-ATOM   5918  N   ALA A 789      13.996  -1.869 -36.145  1.00 48.01           N  
-ANISOU 5918  N   ALA A 789     6822   7405   4013   -896    292    -12       N  
-ATOM   5919  CA  ALA A 789      14.957  -2.396 -37.114  1.00 50.97           C  
-ANISOU 5919  CA  ALA A 789     7310   7697   4361   -943    402   -194       C  
-ATOM   5920  C   ALA A 789      15.312  -3.853 -36.834  1.00 52.93           C  
-ANISOU 5920  C   ALA A 789     7590   7832   4689   -949    365   -314       C  
-ATOM   5921  O   ALA A 789      15.559  -4.632 -37.754  1.00 52.69           O  
-ANISOU 5921  O   ALA A 789     7688   7744   4588  -1031    398   -428       O  
-ATOM   5922  CB  ALA A 789      16.220  -1.555 -37.110  1.00 48.79           C  
-ANISOU 5922  CB  ALA A 789     6991   7380   4167   -859    571   -295       C  
-ATOM   5923  N   LEU A 790      15.338  -4.208 -35.553  1.00 65.74           N  
-ANISOU 5923  N   LEU A 790     9102   9420   6457   -861    299   -286       N  
-ATOM   5924  CA  LEU A 790      15.737  -5.539 -35.125  1.00 68.53           C  
-ANISOU 5924  CA  LEU A 790     9470   9656   6911   -845    267   -388       C  
-ATOM   5925  C   LEU A 790      14.956  -6.603 -35.885  1.00 70.74           C  
-ANISOU 5925  C   LEU A 790     9886   9918   7074   -982    179   -392       C  
-ATOM   5926  O   LEU A 790      15.476  -7.677 -36.177  1.00 71.38           O  
-ANISOU 5926  O   LEU A 790    10051   9884   7188  -1003    208   -528       O  
-ATOM   5927  CB  LEU A 790      15.532  -5.690 -33.615  1.00 70.49           C  
-ANISOU 5927  CB  LEU A 790     9582   9903   7299   -747    175   -304       C  
-ATOM   5928  CG  LEU A 790      16.174  -6.899 -32.934  1.00 72.83           C  
-ANISOU 5928  CG  LEU A 790     9862  10072   7738   -689    160   -403       C  
-ATOM   5929  CD1 LEU A 790      17.671  -6.922 -33.193  1.00 75.64           C  
-ANISOU 5929  CD1 LEU A 790    10215  10336   8187   -617    314   -581       C  
-ATOM   5930  CD2 LEU A 790      15.890  -6.886 -31.445  1.00 72.53           C  
-ANISOU 5930  CD2 LEU A 790     9687  10055   7815   -597     66   -298       C  
-ATOM   5931  N   ALA A 791      13.705  -6.292 -36.210  1.00 52.06           N  
-ANISOU 5931  N   ALA A 791     7542   7668   4572  -1075     73   -242       N  
-ATOM   5932  CA  ALA A 791      12.838  -7.232 -36.914  1.00 53.83           C  
-ANISOU 5932  CA  ALA A 791     7888   7895   4671  -1224    -30   -229       C  
-ATOM   5933  C   ALA A 791      13.466  -7.697 -38.222  1.00 55.54           C  
-ANISOU 5933  C   ALA A 791     8270   8042   4792  -1309     71   -398       C  
-ATOM   5934  O   ALA A 791      13.196  -8.802 -38.688  1.00 56.36           O  
-ANISOU 5934  O   ALA A 791     8491   8082   4841  -1413     21   -464       O  
-ATOM   5935  CB  ALA A 791      11.472  -6.613 -37.165  1.00 54.18           C  
-ANISOU 5935  CB  ALA A 791     7914   8097   4574  -1307   -146    -35       C  
-ATOM   5936  N   ASN A 792      14.300  -6.848 -38.814  1.00 70.36           N  
-ANISOU 5936  N   ASN A 792    10160   9929   6645  -1270    219   -470       N  
-ATOM   5937  CA  ASN A 792      15.057  -7.230 -39.998  1.00 72.02           C  
-ANISOU 5937  CA  ASN A 792    10519  10068   6777  -1332    342   -643       C  
-ATOM   5938  C   ASN A 792      16.022  -8.372 -39.686  1.00 72.07           C  
-ANISOU 5938  C   ASN A 792    10552   9905   6925  -1274    407   -817       C  
-ATOM   5939  O   ASN A 792      16.022  -9.391 -40.375  1.00 73.35           O  
-ANISOU 5939  O   ASN A 792    10859   9987   7024  -1365    410   -925       O  
-ATOM   5940  CB  ASN A 792      15.814  -6.031 -40.581  1.00 74.36           C  
-ANISOU 5940  CB  ASN A 792    10806  10408   7038  -1289    498   -676       C  
-ATOM   5941  CG  ASN A 792      14.883  -4.934 -41.085  1.00 74.47           C  
-ANISOU 5941  CG  ASN A 792    10821  10580   6896  -1352    448   -508       C  
-ATOM   5942  OD1 ASN A 792      13.728  -5.190 -41.432  1.00 75.21           O  
-ANISOU 5942  OD1 ASN A 792    10967  10753   6858  -1463    313   -401       O  
-ATOM   5943  ND2 ASN A 792      15.388  -3.704 -41.128  1.00 73.96           N  
-ANISOU 5943  ND2 ASN A 792    10695  10559   6846  -1281    557   -482       N  
-ATOM   5944  N   GLN A 793      16.830  -8.208 -38.641  1.00 64.19           N  
-ANISOU 5944  N   GLN A 793     9418   8854   6118  -1124    456   -842       N  
-ATOM   5945  CA  GLN A 793      17.808  -9.232 -38.273  1.00 65.15           C  
-ANISOU 5945  CA  GLN A 793     9544   8819   6391  -1047    520   -994       C  
-ATOM   5946  C   GLN A 793      17.146 -10.556 -37.949  1.00 64.84           C  
-ANISOU 5946  C   GLN A 793     9566   8702   6369  -1103    393   -984       C  
-ATOM   5947  O   GLN A 793      17.424 -11.578 -38.573  1.00 66.98           O  
-ANISOU 5947  O   GLN A 793     9973   8858   6619  -1158    433  -1117       O  
-ATOM   5948  CB  GLN A 793      18.637  -8.798 -37.067  1.00 65.27           C  
-ANISOU 5948  CB  GLN A 793     9380   8815   6603   -880    560   -989       C  
-ATOM   5949  CG  GLN A 793      19.655  -7.718 -37.356  1.00 69.63           C  
-ANISOU 5949  CG  GLN A 793     9876   9398   7183   -813    720  -1052       C  
-ATOM   5950  CD  GLN A 793      20.605  -7.497 -36.194  1.00 71.27           C  
-ANISOU 5950  CD  GLN A 793     9916   9570   7593   -658    761  -1077       C  
-ATOM   5951  OE1 GLN A 793      20.652  -8.291 -35.250  1.00 72.28           O  
-ANISOU 5951  OE1 GLN A 793     9984   9632   7846   -592    685  -1070       O  
-ATOM   5952  NE2 GLN A 793      21.372  -6.414 -36.259  1.00 71.95           N  
-ANISOU 5952  NE2 GLN A 793     9927   9700   7711   -604    878  -1104       N  
-ATOM   5953  N   ILE A 794      16.266 -10.526 -36.960  1.00 62.48           N  
-ANISOU 5953  N   ILE A 794     9170   8461   6109  -1090    244   -826       N  
-ATOM   5954  CA  ILE A 794      15.686 -11.740 -36.414  1.00 61.39           C  
-ANISOU 5954  CA  ILE A 794     9060   8245   6019  -1126    121   -800       C  
-ATOM   5955  C   ILE A 794      14.270 -11.963 -36.923  1.00 63.08           C  
-ANISOU 5955  C   ILE A 794     9358   8543   6065  -1295    -20   -689       C  
-ATOM   5956  O   ILE A 794      13.384 -11.138 -36.701  1.00 62.83           O  
-ANISOU 5956  O   ILE A 794     9249   8658   5967  -1319   -107   -524       O  
-ATOM   5957  CB  ILE A 794      15.674 -11.675 -34.888  1.00 58.28           C  
-ANISOU 5957  CB  ILE A 794     8498   7856   5790   -998     49   -699       C  
-ATOM   5958  CG1 ILE A 794      17.096 -11.459 -34.374  1.00 54.80           C  
-ANISOU 5958  CG1 ILE A 794     7965   7343   5515   -837    179   -807       C  
-ATOM   5959  CG2 ILE A 794      15.071 -12.938 -34.307  1.00 59.05           C  
-ANISOU 5959  CG2 ILE A 794     8628   7870   5940  -1036    -75   -663       C  
-ATOM   5960  CD1 ILE A 794      17.164 -10.747 -33.046  1.00 51.14           C  
-ANISOU 5960  CD1 ILE A 794     7317   6946   5167   -713    136   -696       C  
-ATOM   5961  N   PRO A 795      14.057 -13.090 -37.609  1.00 62.09           N  
-ANISOU 5961  N   PRO A 795     9393   8325   5874  -1414    -42   -780       N  
-ATOM   5962  CA  PRO A 795      12.768 -13.460 -38.200  1.00 63.60           C  
-ANISOU 5962  CA  PRO A 795     9682   8586   5899  -1598   -178   -698       C  
-ATOM   5963  C   PRO A 795      11.662 -13.544 -37.158  1.00 62.93           C  
-ANISOU 5963  C   PRO A 795     9482   8574   5856  -1608   -349   -507       C  
-ATOM   5964  O   PRO A 795      10.548 -13.081 -37.408  1.00 63.15           O  
-ANISOU 5964  O   PRO A 795     9492   8749   5755  -1709   -457   -362       O  
-ATOM   5965  CB  PRO A 795      13.039 -14.850 -38.777  1.00 65.00           C  
-ANISOU 5965  CB  PRO A 795    10037   8594   6066  -1684   -152   -862       C  
-ATOM   5966  CG  PRO A 795      14.508 -14.882 -39.010  1.00 64.59           C  
-ANISOU 5966  CG  PRO A 795    10011   8422   6110  -1563     37  -1045       C  
-ATOM   5967  CD  PRO A 795      15.104 -14.084 -37.895  1.00 62.84           C  
-ANISOU 5967  CD  PRO A 795     9589   8236   6052  -1378     72   -978       C  
-ATOM   5968  N   THR A 796      11.963 -14.129 -36.003  1.00 72.95           N  
-ANISOU 5968  N   THR A 796    10670   9747   7300  -1502   -372   -500       N  
-ATOM   5969  CA  THR A 796      10.945 -14.312 -34.974  1.00 70.95           C  
-ANISOU 5969  CA  THR A 796    10314   9553   7091  -1511   -526   -324       C  
-ATOM   5970  C   THR A 796      10.550 -12.988 -34.320  1.00 66.05           C  
-ANISOU 5970  C   THR A 796     9523   9098   6475  -1427   -554   -158       C  
-ATOM   5971  O   THR A 796       9.439 -12.846 -33.820  1.00 64.91           O  
-ANISOU 5971  O   THR A 796     9304   9058   6300  -1471   -681     12       O  
-ATOM   5972  CB  THR A 796      11.385 -15.316 -33.896  1.00 73.79           C  
-ANISOU 5972  CB  THR A 796    10639   9762   7634  -1418   -541   -356       C  
-ATOM   5973  OG1 THR A 796      12.155 -14.643 -32.893  1.00 75.78           O  
-ANISOU 5973  OG1 THR A 796    10738  10026   8029  -1232   -481   -336       O  
-ATOM   5974  CG2 THR A 796      12.208 -16.442 -34.512  1.00 75.86           C  
-ANISOU 5974  CG2 THR A 796    11061   9832   7932  -1441   -453   -556       C  
-ATOM   5975  N   VAL A 797      11.458 -12.020 -34.322  1.00 56.04           N  
-ANISOU 5975  N   VAL A 797     8194   7850   5247  -1308   -429   -209       N  
-ATOM   5976  CA  VAL A 797      11.113 -10.677 -33.872  1.00 52.30           C  
-ANISOU 5976  CA  VAL A 797     7584   7526   4761  -1238   -437    -67       C  
-ATOM   5977  C   VAL A 797      10.060 -10.082 -34.799  1.00 52.96           C  
-ANISOU 5977  C   VAL A 797     7712   7756   4656  -1369   -497     41       C  
-ATOM   5978  O   VAL A 797      10.075 -10.321 -36.008  1.00 55.68           O  
-ANISOU 5978  O   VAL A 797     8193   8090   4871  -1485   -469    -42       O  
-ATOM   5979  CB  VAL A 797      12.339  -9.750 -33.824  1.00 49.56           C  
-ANISOU 5979  CB  VAL A 797     7181   7164   4485  -1104   -283   -158       C  
-ATOM   5980  CG1 VAL A 797      11.914  -8.311 -33.537  1.00 47.48           C  
-ANISOU 5980  CG1 VAL A 797     6805   7050   4186  -1054   -283    -15       C  
-ATOM   5981  CG2 VAL A 797      13.318 -10.241 -32.778  1.00 49.30           C  
-ANISOU 5981  CG2 VAL A 797     7074   7013   4643   -966   -241   -236       C  
-ATOM   5982  N   ASN A 798       9.140  -9.315 -34.230  1.00 62.26           N  
-ANISOU 5982  N   ASN A 798     8771   9071   5814  -1350   -579    229       N  
-ATOM   5983  CA  ASN A 798       8.036  -8.771 -35.001  1.00 62.99           C  
-ANISOU 5983  CA  ASN A 798     8882   9313   5737  -1465   -653    361       C  
-ATOM   5984  C   ASN A 798       7.527  -7.458 -34.438  1.00 61.97           C  
-ANISOU 5984  C   ASN A 798     8610   9323   5612  -1375   -662    533       C  
-ATOM   5985  O   ASN A 798       7.650  -7.193 -33.242  1.00 61.26           O  
-ANISOU 5985  O   ASN A 798     8398   9226   5652  -1252   -660    586       O  
-ATOM   5986  CB  ASN A 798       6.884  -9.768 -35.062  1.00 64.04           C  
-ANISOU 5986  CB  ASN A 798     9054   9472   5808  -1612   -812    442       C  
-ATOM   5987  CG  ASN A 798       5.598  -9.130 -35.537  1.00 64.96           C  
-ANISOU 5987  CG  ASN A 798     9134   9772   5776  -1708   -914    626       C  
-ATOM   5988  OD1 ASN A 798       4.848  -8.559 -34.745  1.00 63.79           O  
-ANISOU 5988  OD1 ASN A 798     8846   9729   5661  -1651   -978    801       O  
-ATOM   5989  ND2 ASN A 798       5.341  -9.211 -36.837  1.00 65.82           N  
-ANISOU 5989  ND2 ASN A 798     9367   9925   5717  -1851   -928    591       N  
-ATOM   5990  N   ASN A 799       6.939  -6.645 -35.308  1.00 55.03           N  
-ANISOU 5990  N   ASN A 799     7751   8570   4588  -1438   -670    622       N  
-ATOM   5991  CA  ASN A 799       6.448  -5.339 -34.911  1.00 54.17           C  
-ANISOU 5991  CA  ASN A 799     7520   8586   4475  -1352   -664    786       C  
-ATOM   5992  C   ASN A 799       4.930  -5.215 -34.873  1.00 54.37           C  
-ANISOU 5992  C   ASN A 799     7481   8764   4413  -1427   -810   1001       C  
-ATOM   5993  O   ASN A 799       4.239  -5.555 -35.835  1.00 55.24           O  
-ANISOU 5993  O   ASN A 799     7667   8941   4379  -1575   -890   1037       O  
-ATOM   5994  CB  ASN A 799       7.055  -4.257 -35.795  1.00 54.95           C  
-ANISOU 5994  CB  ASN A 799     7666   8712   4500  -1326   -536    742       C  
-ATOM   5995  CG  ASN A 799       8.461  -3.899 -35.375  1.00 56.26           C  
-ANISOU 5995  CG  ASN A 799     7815   8765   4795  -1196   -384    594       C  
-ATOM   5996  OD1 ASN A 799       9.386  -3.874 -36.186  1.00 58.45           O  
-ANISOU 5996  OD1 ASN A 799     8188   8978   5043  -1212   -272    446       O  
-ATOM   5997  ND2 ASN A 799       8.631  -3.629 -34.089  1.00 57.02           N  
-ANISOU 5997  ND2 ASN A 799     7788   8842   5035  -1069   -379    632       N  
-ATOM   5998  N   LEU A 800       4.429  -4.740 -33.736  1.00 51.26           N  
-ANISOU 5998  N   LEU A 800     6943   8425   4108  -1325   -844   1140       N  
-ATOM   5999  CA  LEU A 800       3.030  -4.377 -33.573  1.00 52.40           C  
-ANISOU 5999  CA  LEU A 800     6994   8727   4190  -1359   -958   1363       C  
-ATOM   6000  C   LEU A 800       2.998  -2.948 -33.073  1.00 54.27           C  
-ANISOU 6000  C   LEU A 800     7123   9032   4465  -1212   -880   1471       C  
-ATOM   6001  O   LEU A 800       4.026  -2.407 -32.678  1.00 52.64           O  
-ANISOU 6001  O   LEU A 800     6910   8743   4347  -1095   -756   1370       O  
-ATOM   6002  CB  LEU A 800       2.359  -5.285 -32.549  1.00 50.87           C  
-ANISOU 6002  CB  LEU A 800     6725   8528   4076  -1376  -1072   1436       C  
-ATOM   6003  CG  LEU A 800       2.449  -6.784 -32.833  1.00 51.99           C  
-ANISOU 6003  CG  LEU A 800     6972   8571   4211  -1509  -1143   1321       C  
-ATOM   6004  CD1 LEU A 800       2.089  -7.576 -31.588  1.00 51.44           C  
-ANISOU 6004  CD1 LEU A 800     6822   8462   4259  -1483  -1219   1374       C  
-ATOM   6005  CD2 LEU A 800       1.575  -7.191 -34.025  1.00 51.77           C  
-ANISOU 6005  CD2 LEU A 800     7026   8632   4014  -1701  -1248   1369       C  
-ATOM   6006  N   HIS A 801       1.826  -2.328 -33.087  1.00 57.01           N  
-ANISOU 6006  N   HIS A 801     7385   9528   4747  -1218   -951   1677       N  
-ATOM   6007  CA  HIS A 801       1.721  -0.974 -32.572  1.00 62.39           C  
-ANISOU 6007  CA  HIS A 801     7969  10267   5470  -1073   -873   1789       C  
-ATOM   6008  C   HIS A 801       0.280  -0.555 -32.335  1.00 67.54           C  
-ANISOU 6008  C   HIS A 801     8504  11080   6080  -1073   -970   2032       C  
-ATOM   6009  O   HIS A 801      -0.651  -1.175 -32.844  1.00 67.81           O  
-ANISOU 6009  O   HIS A 801     8539  11203   6023  -1204  -1099   2122       O  
-ATOM   6010  CB  HIS A 801       2.390   0.011 -33.524  1.00 62.24           C  
-ANISOU 6010  CB  HIS A 801     8025  10240   5384  -1050   -753   1733       C  
-ATOM   6011  CG  HIS A 801       1.535   0.387 -34.689  1.00 63.44           C  
-ANISOU 6011  CG  HIS A 801     8208  10523   5372  -1145   -812   1863       C  
-ATOM   6012  ND1 HIS A 801       1.403  -0.411 -35.805  1.00 63.98           N  
-ANISOU 6012  ND1 HIS A 801     8390  10609   5312  -1310   -882   1806       N  
-ATOM   6013  CD2 HIS A 801       0.764   1.476 -34.910  1.00 62.54           C  
-ANISOU 6013  CD2 HIS A 801     8029  10533   5200  -1098   -812   2050       C  
-ATOM   6014  CE1 HIS A 801       0.585   0.170 -36.663  1.00 65.11           C  
-ANISOU 6014  CE1 HIS A 801     8531  10890   5317  -1366   -932   1956       C  
-ATOM   6015  NE2 HIS A 801       0.183   1.316 -36.144  1.00 64.35           N  
-ANISOU 6015  NE2 HIS A 801     8324  10860   5265  -1234   -890   2111       N  
-ATOM   6016  N   VAL A 802       0.116   0.503 -31.546  1.00 73.54           N  
-ANISOU 6016  N   VAL A 802     9161  11874   6908   -926   -904   2136       N  
-ATOM   6017  CA  VAL A 802      -1.188   1.093 -31.284  1.00 82.17           C  
-ANISOU 6017  CA  VAL A 802    10131  13116   7972   -893   -967   2373       C  
-ATOM   6018  C   VAL A 802      -1.140   2.577 -31.625  1.00 88.34           C  
-ANISOU 6018  C   VAL A 802    10900  13939   8727   -787   -858   2452       C  
-ATOM   6019  O   VAL A 802      -0.182   3.269 -31.281  1.00 88.36           O  
-ANISOU 6019  O   VAL A 802    10928  13844   8801   -679   -724   2349       O  
-ATOM   6020  CB  VAL A 802      -1.611   0.912 -29.811  1.00 80.30           C  
-ANISOU 6020  CB  VAL A 802     9772  12884   7855   -803   -991   2447       C  
-ATOM   6021  CG1 VAL A 802      -0.562   1.493 -28.871  1.00 78.03           C  
-ANISOU 6021  CG1 VAL A 802     9479  12481   7689   -652   -855   2332       C  
-ATOM   6022  CG2 VAL A 802      -2.970   1.553 -29.566  1.00 80.77           C  
-ANISOU 6022  CG2 VAL A 802     9699  13103   7888   -761  -1043   2696       C  
-ATOM   6023  N   THR A 803      -2.176   3.063 -32.303  1.00111.01           N  
-ANISOU 6023  N   THR A 803    13730  16953  11495   -821   -919   2639       N  
-ATOM   6024  CA  THR A 803      -2.192   4.443 -32.784  1.00117.42           C  
-ANISOU 6024  CA  THR A 803    14542  17804  12268   -730   -821   2729       C  
-ATOM   6025  C   THR A 803      -3.301   5.299 -32.185  1.00118.10           C  
-ANISOU 6025  C   THR A 803    14484  18005  12383   -618   -829   2965       C  
-ATOM   6026  O   THR A 803      -4.245   4.793 -31.577  1.00118.00           O  
-ANISOU 6026  O   THR A 803    14364  18076  12394   -632   -931   3086       O  
-ATOM   6027  CB  THR A 803      -2.317   4.512 -34.321  1.00122.24           C  
-ANISOU 6027  CB  THR A 803    15247  18482  12716   -851   -858   2750       C  
-ATOM   6028  OG1 THR A 803      -3.370   3.642 -34.757  1.00126.42           O  
-ANISOU 6028  OG1 THR A 803    15745  19137  13153   -994  -1030   2856       O  
-ATOM   6029  CG2 THR A 803      -1.015   4.099 -34.982  1.00126.03           C  
-ANISOU 6029  CG2 THR A 803    15882  18832  13171   -918   -786   2511       C  
-ATOM   6030  N   ALA A 804      -3.167   6.606 -32.379  1.00115.65           N  
-ANISOU 6030  N   ALA A 804    14176  17693  12071   -504   -713   3030       N  
-ATOM   6031  CA  ALA A 804      -4.182   7.565 -31.973  1.00116.84           C  
-ANISOU 6031  CA  ALA A 804    14205  17946  12243   -384   -699   3258       C  
-ATOM   6032  C   ALA A 804      -4.544   8.456 -33.156  1.00118.67           C  
-ANISOU 6032  C   ALA A 804    14468  18261  12362   -386   -683   3390       C  
-ATOM   6033  O   ALA A 804      -3.789   8.555 -34.122  1.00120.35           O  
-ANISOU 6033  O   ALA A 804    14806  18423  12500   -450   -640   3280       O  
-ATOM   6034  CB  ALA A 804      -3.678   8.402 -30.816  1.00117.77           C  
-ANISOU 6034  CB  ALA A 804    14291  17963  12494   -212   -553   3217       C  
-ATOM   6035  N   LEU A 805      -5.703   9.099 -33.077  1.00 98.00           N  
-ANISOU 6035  N   LEU A 805    11732  15773   9731   -313   -715   3632       N  
-ATOM   6036  CA  LEU A 805      -6.152   9.998 -34.131  1.00 98.98           C  
-ANISOU 6036  CA  LEU A 805    11868  15986   9752   -298   -704   3790       C  
-ATOM   6037  C   LEU A 805      -5.976  11.443 -33.696  1.00 98.94           C  
-ANISOU 6037  C   LEU A 805    11849  15917   9828   -105   -535   3858       C  
-ATOM   6038  O   LEU A 805      -6.208  11.785 -32.537  1.00 98.39           O  
-ANISOU 6038  O   LEU A 805    11691  15818   9875     23   -476   3898       O  
-ATOM   6039  CB  LEU A 805      -7.612   9.721 -34.482  1.00 98.39           C  
-ANISOU 6039  CB  LEU A 805    11669  16115   9601   -355   -865   4032       C  
-ATOM   6040  CG  LEU A 805      -7.885   8.297 -34.967  1.00 97.31           C  
-ANISOU 6040  CG  LEU A 805    11549  16048   9375   -563  -1042   3976       C  
-ATOM   6041  CD1 LEU A 805      -9.363   8.095 -35.259  1.00 95.78           C  
-ANISOU 6041  CD1 LEU A 805    11215  16066   9110   -619  -1202   4227       C  
-ATOM   6042  CD2 LEU A 805      -7.032   7.978 -36.195  1.00 97.41           C  
-ANISOU 6042  CD2 LEU A 805    11737  16011   9265   -700  -1044   3816       C  
-ATOM   6043  N   THR A 806      -5.569  12.293 -34.631  1.00 88.04           N  
-ANISOU 6043  N   THR A 806    10561  14511   8380    -89   -453   3870       N  
-ATOM   6044  CA  THR A 806      -5.218  13.666 -34.299  1.00 90.00           C  
-ANISOU 6044  CA  THR A 806    10826  14666   8704     80   -276   3902       C  
-ATOM   6045  C   THR A 806      -6.193  14.714 -34.833  1.00 95.40           C  
-ANISOU 6045  C   THR A 806    11449  15459   9338    172   -266   4170       C  
-ATOM   6046  O   THR A 806      -6.548  14.718 -36.010  1.00 96.16           O  
-ANISOU 6046  O   THR A 806    11577  15659   9302     89   -342   4271       O  
-ATOM   6047  CB  THR A 806      -3.795  14.001 -34.774  1.00 86.98           C  
-ANISOU 6047  CB  THR A 806    10604  14129   8317     55   -145   3690       C  
-ATOM   6048  OG1 THR A 806      -3.573  13.407 -36.059  1.00 85.08           O  
-ANISOU 6048  OG1 THR A 806    10458  13938   7932   -106   -225   3640       O  
-ATOM   6049  CG2 THR A 806      -2.773  13.454 -33.797  1.00 83.32           C  
-ANISOU 6049  CG2 THR A 806    10169  13522   7965     54    -89   3449       C  
-ATOM   6050  N   THR A 807      -6.626  15.595 -33.939  1.00101.85           N  
-ANISOU 6050  N   THR A 807    12181  16253  10263    348   -170   4286       N  
-ATOM   6051  CA  THR A 807      -7.424  16.755 -34.299  1.00111.07           C  
-ANISOU 6051  CA  THR A 807    13297  17488  11415    474   -121   4532       C  
-ATOM   6052  C   THR A 807      -6.568  17.972 -33.996  1.00115.07           C  
-ANISOU 6052  C   THR A 807    13898  17818  12006    608     92   4454       C  
-ATOM   6053  O   THR A 807      -5.539  17.855 -33.338  1.00115.57           O  
-ANISOU 6053  O   THR A 807    14031  17732  12147    607    181   4231       O  
-ATOM   6054  CB  THR A 807      -8.717  16.828 -33.469  1.00111.17           C  
-ANISOU 6054  CB  THR A 807    13117  17614  11507    581   -167   4731       C  
-ATOM   6055  OG1 THR A 807      -9.396  15.567 -33.520  1.00113.17           O  
-ANISOU 6055  OG1 THR A 807    13271  18009  11721    441   -356   4751       O  
-ATOM   6056  CG2 THR A 807      -9.638  17.919 -33.992  1.00113.00           C  
-ANISOU 6056  CG2 THR A 807    13275  17937  11724    703   -135   4996       C  
-ATOM   6057  N   GLU A 808      -6.981  19.139 -34.473  1.00138.79           N  
-ANISOU 6057  N   GLU A 808    16904  20835  14994    721    172   4639       N  
-ATOM   6058  CA  GLU A 808      -6.214  20.349 -34.214  1.00142.60           C  
-ANISOU 6058  CA  GLU A 808    17483  21142  15558    845    380   4576       C  
-ATOM   6059  C   GLU A 808      -6.258  20.711 -32.735  1.00143.27           C  
-ANISOU 6059  C   GLU A 808    17506  21135  15795    987    484   4538       C  
-ATOM   6060  O   GLU A 808      -5.475  21.536 -32.262  1.00142.51           O  
-ANISOU 6060  O   GLU A 808    17494  20873  15782   1070    654   4427       O  
-ATOM   6061  CB  GLU A 808      -6.722  21.513 -35.064  1.00148.39           C  
-ANISOU 6061  CB  GLU A 808    18232  21908  16242    939    441   4802       C  
-ATOM   6062  CG  GLU A 808      -5.770  22.692 -35.085  1.00154.96           C  
-ANISOU 6062  CG  GLU A 808    19199  22548  17132   1024    651   4715       C  
-ATOM   6063  CD  GLU A 808      -4.362  22.282 -35.474  1.00158.47           C  
-ANISOU 6063  CD  GLU A 808    19790  22878  17545    883    690   4443       C  
-ATOM   6064  OE1 GLU A 808      -4.216  21.318 -36.256  1.00163.67           O  
-ANISOU 6064  OE1 GLU A 808    20473  23623  18090    722    558   4381       O  
-ATOM   6065  OE2 GLU A 808      -3.400  22.918 -34.993  1.00161.54           O  
-ANISOU 6065  OE2 GLU A 808    20266  23090  18023    932    853   4288       O  
-ATOM   6066  N   GLU A 809      -7.176  20.081 -32.009  1.00128.65           N  
-ANISOU 6066  N   GLU A 809    15511  19396  13974   1007    381   4629       N  
-ATOM   6067  CA  GLU A 809      -7.315  20.315 -30.579  1.00129.53           C  
-ANISOU 6067  CA  GLU A 809    15558  19442  14216   1134    467   4601       C  
-ATOM   6068  C   GLU A 809      -7.827  19.073 -29.858  1.00126.57           C  
-ANISOU 6068  C   GLU A 809    15067  19169  13853   1065    323   4583       C  
-ATOM   6069  O   GLU A 809      -8.502  19.176 -28.836  1.00128.00           O  
-ANISOU 6069  O   GLU A 809    15141  19379  14113   1173    346   4667       O  
-ATOM   6070  CB  GLU A 809      -8.246  21.500 -30.323  1.00137.21           C  
-ANISOU 6070  CB  GLU A 809    16457  20433  15242   1330    569   4839       C  
-ATOM   6071  CG  GLU A 809      -9.596  21.381 -31.008  1.00146.35           C  
-ANISOU 6071  CG  GLU A 809    17482  21798  16328   1339    437   5124       C  
-ATOM   6072  CD  GLU A 809     -10.324  22.708 -31.087  1.00152.28           C  
-ANISOU 6072  CD  GLU A 809    18192  22547  17120   1534    555   5360       C  
-ATOM   6073  OE1 GLU A 809      -9.802  23.707 -30.547  1.00154.39           O  
-ANISOU 6073  OE1 GLU A 809    18542  22645  17476   1661    745   5295       O  
-ATOM   6074  OE2 GLU A 809     -11.414  22.754 -31.696  1.00155.48           O  
-ANISOU 6074  OE2 GLU A 809    18476  23121  17479   1557    460   5601       O  
-ATOM   6075  N   THR A 810      -7.497  17.901 -30.393  1.00136.49           N  
-ANISOU 6075  N   THR A 810    16352  20476  15033    885    181   4471       N  
-ATOM   6076  CA  THR A 810      -7.904  16.636 -29.790  1.00131.16           C  
-ANISOU 6076  CA  THR A 810    15584  19886  14366    798     40   4440       C  
-ATOM   6077  C   THR A 810      -6.959  15.503 -30.173  1.00127.88           C  
-ANISOU 6077  C   THR A 810    15263  19424  13900    617    -44   4212       C  
-ATOM   6078  O   THR A 810      -6.463  15.451 -31.296  1.00126.93           O  
-ANISOU 6078  O   THR A 810    15243  19295  13689    519    -64   4157       O  
-ATOM   6079  CB  THR A 810      -9.330  16.238 -30.217  1.00131.60           C  
-ANISOU 6079  CB  THR A 810    15473  20146  14383    763   -109   4664       C  
-ATOM   6080  OG1 THR A 810     -10.238  17.306 -29.923  1.00129.54           O  
-ANISOU 6080  OG1 THR A 810    15108  19933  14179    941    -24   4883       O  
-ATOM   6081  CG2 THR A 810      -9.775  14.976 -29.492  1.00130.64           C  
-ANISOU 6081  CG2 THR A 810    15243  20098  14295    675   -236   4625       C  
-ATOM   6082  N   LEU A 811      -6.713  14.596 -29.233  1.00137.55           N  
-ANISOU 6082  N   LEU A 811    16460  20618  15184    577    -88   4081       N  
-ATOM   6083  CA  LEU A 811      -5.912  13.407 -29.504  1.00131.63           C  
-ANISOU 6083  CA  LEU A 811    15787  19828  14399    413   -175   3877       C  
-ATOM   6084  C   LEU A 811      -6.508  12.207 -28.777  1.00128.35           C  
-ANISOU 6084  C   LEU A 811    15272  19490  14007    349   -309   3891       C  
-ATOM   6085  O   LEU A 811      -6.441  12.115 -27.550  1.00125.76           O  
-ANISOU 6085  O   LEU A 811    14895  19113  13774    424   -266   3846       O  
-ATOM   6086  CB  LEU A 811      -4.455  13.624 -29.088  1.00132.89           C  
-ANISOU 6086  CB  LEU A 811    16064  19803  14627    433    -45   3627       C  
-ATOM   6087  CG  LEU A 811      -3.411  12.651 -29.646  1.00132.31           C  
-ANISOU 6087  CG  LEU A 811    16096  19663  14512    280    -95   3407       C  
-ATOM   6088  CD1 LEU A 811      -2.010  13.226 -29.504  1.00133.68           C  
-ANISOU 6088  CD1 LEU A 811    16380  19669  14743    316     57   3201       C  
-ATOM   6089  CD2 LEU A 811      -3.502  11.291 -28.978  1.00135.00           C  
-ANISOU 6089  CD2 LEU A 811    16388  20025  14881    198   -216   3331       C  
-ATOM   6090  N   THR A 812      -7.089  11.290 -29.542  1.00110.17           N  
-ANISOU 6090  N   THR A 812    12943  17307  11611    203   -470   3955       N  
-ATOM   6091  CA  THR A 812      -7.802  10.155 -28.968  1.00107.56           C  
-ANISOU 6091  CA  THR A 812    12505  17060  11304    126   -604   3989       C  
-ATOM   6092  C   THR A 812      -7.192   8.823 -29.399  1.00104.86           C  
-ANISOU 6092  C   THR A 812    12256  16682  10904    -56   -715   3819       C  
-ATOM   6093  O   THR A 812      -6.697   8.692 -30.516  1.00106.90           O  
-ANISOU 6093  O   THR A 812    12623  16924  11072   -157   -736   3740       O  
-ATOM   6094  CB  THR A 812      -9.287  10.196 -29.353  1.00108.82           C  
-ANISOU 6094  CB  THR A 812    12506  17407  11434    108   -704   4235       C  
-ATOM   6095  OG1 THR A 812      -9.405  10.236 -30.779  1.00109.93           O  
-ANISOU 6095  OG1 THR A 812    12706  17622  11439      5   -778   4292       O  
-ATOM   6096  CG2 THR A 812      -9.946  11.436 -28.771  1.00109.43           C  
-ANISOU 6096  CG2 THR A 812    12473  17514  11592    303   -585   4402       C  
-ATOM   6097  N   MET A 813      -7.236   7.837 -28.508  1.00100.94           N  
-ANISOU 6097  N   MET A 813    11717  16170  10467    -96   -778   3756       N  
-ATOM   6098  CA  MET A 813      -6.596   6.549 -28.756  1.00 95.77           C  
-ANISOU 6098  CA  MET A 813    11148  15451   9788   -252   -863   3575       C  
-ATOM   6099  C   MET A 813      -7.578   5.504 -29.268  1.00 96.06           C  
-ANISOU 6099  C   MET A 813    11131  15623   9746   -413  -1045   3680       C  
-ATOM   6100  O   MET A 813      -8.752   5.501 -28.903  1.00 95.46           O  
-ANISOU 6100  O   MET A 813    10913  15678   9680   -396  -1112   3875       O  
-ATOM   6101  CB  MET A 813      -5.918   6.037 -27.487  1.00 89.88           C  
-ANISOU 6101  CB  MET A 813    10405  14588   9157   -206   -821   3426       C  
-ATOM   6102  CG  MET A 813      -5.163   7.106 -26.714  1.00 81.25           C  
-ANISOU 6102  CG  MET A 813     9333  13387   8153    -38   -651   3353       C  
-ATOM   6103  SD  MET A 813      -3.697   7.715 -27.561  1.00 73.38           S  
-ANISOU 6103  SD  MET A 813     8498  12249   7135    -40   -528   3151       S  
-ATOM   6104  CE  MET A 813      -3.095   8.904 -26.369  1.00 66.66           C  
-ANISOU 6104  CE  MET A 813     7635  11294   6400    150   -349   3101       C  
-ATOM   6105  N   LEU A 814      -7.078   4.607 -30.109  1.00113.29           N  
-ANISOU 6105  N   LEU A 814    13425  17767  11854   -574  -1119   3542       N  
-ATOM   6106  CA  LEU A 814      -7.906   3.574 -30.711  1.00113.74           C  
-ANISOU 6106  CA  LEU A 814    13457  17936  11823   -753  -1293   3615       C  
-ATOM   6107  C   LEU A 814      -7.795   2.275 -29.927  1.00108.48           C  
-ANISOU 6107  C   LEU A 814    12788  17208  11222   -832  -1364   3515       C  
-ATOM   6108  O   LEU A 814      -8.726   1.473 -29.911  1.00109.55           O  
-ANISOU 6108  O   LEU A 814    12849  17445  11329   -944  -1501   3620       O  
-ATOM   6109  CB  LEU A 814      -7.493   3.335 -32.164  1.00122.50           C  
-ANISOU 6109  CB  LEU A 814    14704  19044  12797   -895  -1334   3526       C  
-ATOM   6110  CG  LEU A 814      -7.491   4.538 -33.108  1.00130.88           C  
-ANISOU 6110  CG  LEU A 814    15796  20158  13775   -838  -1268   3611       C  
-ATOM   6111  CD1 LEU A 814      -6.978   4.125 -34.477  1.00137.45           C  
-ANISOU 6111  CD1 LEU A 814    16780  20976  14469   -994  -1308   3493       C  
-ATOM   6112  CD2 LEU A 814      -8.880   5.147 -33.214  1.00135.36           C  
-ANISOU 6112  CD2 LEU A 814    16210  20916  14304   -798  -1337   3895       C  
-ATOM   6113  N   TYR A 815      -6.647   2.072 -29.289  1.00 94.90           N  
-ANISOU 6113  N   TYR A 815    11146  15322   9590   -775  -1272   3317       N  
-ATOM   6114  CA  TYR A 815      -6.414   0.873 -28.493  1.00 88.03           C  
-ANISOU 6114  CA  TYR A 815    10282  14373   8791   -831  -1325   3216       C  
-ATOM   6115  C   TYR A 815      -6.394  -0.383 -29.356  1.00 87.28           C  
-ANISOU 6115  C   TYR A 815    10281  14265   8616  -1036  -1448   3128       C  
-ATOM   6116  O   TYR A 815      -6.549  -1.494 -28.848  1.00 87.37           O  
-ANISOU 6116  O   TYR A 815    10285  14244   8668  -1117  -1528   3095       O  
-ATOM   6117  CB  TYR A 815      -7.470   0.754 -27.394  1.00 84.00           C  
-ANISOU 6117  CB  TYR A 815     9613  13957   8345   -781  -1374   3392       C  
-ATOM   6118  CG  TYR A 815      -7.484   1.942 -26.465  1.00 78.84           C  
-ANISOU 6118  CG  TYR A 815     8878  13307   7772   -578  -1244   3466       C  
-ATOM   6119  CD1 TYR A 815      -6.299   2.480 -25.990  1.00 76.47           C  
-ANISOU 6119  CD1 TYR A 815     8651  12864   7540   -461  -1107   3304       C  
-ATOM   6120  CD2 TYR A 815      -8.676   2.539 -26.078  1.00 77.40           C  
-ANISOU 6120  CD2 TYR A 815     8543  13267   7598   -505  -1255   3694       C  
-ATOM   6121  CE1 TYR A 815      -6.294   3.570 -25.145  1.00 74.59           C  
-ANISOU 6121  CE1 TYR A 815     8352  12620   7370   -286   -986   3360       C  
-ATOM   6122  CE2 TYR A 815      -8.682   3.633 -25.233  1.00 75.51           C  
-ANISOU 6122  CE2 TYR A 815     8229  13010   7450   -323  -1113   3736       C  
-ATOM   6123  CZ  TYR A 815      -7.485   4.144 -24.772  1.00 74.43           C  
-ANISOU 6123  CZ  TYR A 815     8191  12730   7360   -214   -988   3576       C  
-ATOM   6124  OH  TYR A 815      -7.474   5.231 -23.931  1.00 75.34           O  
-ANISOU 6124  OH  TYR A 815     8248  12823   7554    -41   -849   3610       O  
-ATOM   6125  N   GLN A 816      -6.202  -0.199 -30.659  1.00 74.45           N  
-ANISOU 6125  N   GLN A 816     8751  12661   6874  -1121  -1458   3089       N  
-ATOM   6126  CA  GLN A 816      -6.083  -1.321 -31.582  1.00 74.06           C  
-ANISOU 6126  CA  GLN A 816     8816  12588   6734  -1318  -1558   2982       C  
-ATOM   6127  C   GLN A 816      -4.625  -1.703 -31.773  1.00 70.88           C  
-ANISOU 6127  C   GLN A 816     8569  11998   6363  -1318  -1465   2722       C  
-ATOM   6128  O   GLN A 816      -3.788  -0.851 -32.067  1.00 68.67           O  
-ANISOU 6128  O   GLN A 816     8347  11660   6085  -1226  -1340   2641       O  
-ATOM   6129  CB  GLN A 816      -6.684  -0.971 -32.942  1.00 76.84           C  
-ANISOU 6129  CB  GLN A 816     9195  13075   6927  -1424  -1626   3081       C  
-ATOM   6130  CG  GLN A 816      -8.179  -0.755 -32.941  1.00 79.59           C  
-ANISOU 6130  CG  GLN A 816     9386  13625   7228  -1456  -1744   3342       C  
-ATOM   6131  CD  GLN A 816      -8.709  -0.434 -34.326  1.00 82.32           C  
-ANISOU 6131  CD  GLN A 816     9763  14108   7407  -1566  -1819   3436       C  
-ATOM   6132  OE1 GLN A 816      -8.855   0.732 -34.693  1.00 82.61           O  
-ANISOU 6132  OE1 GLN A 816     9764  14216   7407  -1464  -1758   3548       O  
-ATOM   6133  NE2 GLN A 816      -8.997  -1.472 -35.104  1.00 84.14           N  
-ANISOU 6133  NE2 GLN A 816    10066  14373   7532  -1778  -1953   3391       N  
-ATOM   6134  N   VAL A 817      -4.321  -2.985 -31.606  1.00 76.34           N  
-ANISOU 6134  N   VAL A 817     9328  12593   7083  -1421  -1522   2594       N  
-ATOM   6135  CA  VAL A 817      -2.974  -3.473 -31.866  1.00 73.88           C  
-ANISOU 6135  CA  VAL A 817     9163  12107   6800  -1430  -1441   2349       C  
-ATOM   6136  C   VAL A 817      -2.877  -3.963 -33.302  1.00 76.45           C  
-ANISOU 6136  C   VAL A 817     9631  12437   6981  -1601  -1488   2263       C  
-ATOM   6137  O   VAL A 817      -3.226  -5.109 -33.612  1.00 75.96           O  
-ANISOU 6137  O   VAL A 817     9625  12363   6875  -1760  -1596   2228       O  
-ATOM   6138  CB  VAL A 817      -2.565  -4.603 -30.908  1.00 72.54           C  
-ANISOU 6138  CB  VAL A 817     9005  11809   6749  -1434  -1461   2244       C  
-ATOM   6139  CG1 VAL A 817      -1.159  -5.086 -31.235  1.00 68.93           C  
-ANISOU 6139  CG1 VAL A 817     8693  11174   6324  -1434  -1372   1996       C  
-ATOM   6140  CG2 VAL A 817      -2.642  -4.120 -29.471  1.00 68.62           C  
-ANISOU 6140  CG2 VAL A 817     8376  11314   6383  -1269  -1414   2325       C  
-ATOM   6141  N   LYS A 818      -2.410  -3.071 -34.171  1.00 80.74           N  
-ANISOU 6141  N   LYS A 818    10236  12996   7447  -1570  -1402   2231       N  
-ATOM   6142  CA  LYS A 818      -2.260  -3.352 -35.591  1.00 84.38           C  
-ANISOU 6142  CA  LYS A 818    10838  13469   7753  -1719  -1427   2151       C  
-ATOM   6143  C   LYS A 818      -0.823  -3.758 -35.874  1.00 83.08           C  
-ANISOU 6143  C   LYS A 818    10820  13123   7622  -1710  -1310   1895       C  
-ATOM   6144  O   LYS A 818       0.102  -3.266 -35.229  1.00 80.96           O  
-ANISOU 6144  O   LYS A 818    10534  12757   7471  -1561  -1183   1810       O  
-ATOM   6145  CB  LYS A 818      -2.633  -2.113 -36.402  1.00 87.99           C  
-ANISOU 6145  CB  LYS A 818    11275  14059   8098  -1690  -1401   2283       C  
-ATOM   6146  CG  LYS A 818      -3.975  -1.510 -35.999  1.00 95.25           C  
-ANISOU 6146  CG  LYS A 818    12026  15155   9011  -1651  -1489   2550       C  
-ATOM   6147  CD  LYS A 818      -4.272  -0.214 -36.745  1.00101.01           C  
-ANISOU 6147  CD  LYS A 818    12734  16000   9644  -1596  -1447   2687       C  
-ATOM   6148  CE  LYS A 818      -5.638   0.344 -36.368  1.00104.57           C  
-ANISOU 6148  CE  LYS A 818    13010  16630  10093  -1552  -1535   2960       C  
-ATOM   6149  NZ  LYS A 818      -5.969   1.583 -37.123  1.00106.68           N  
-ANISOU 6149  NZ  LYS A 818    13256  17009  10267  -1495  -1499   3108       N  
-ATOM   6150  N   LYS A 819      -0.637  -4.662 -36.831  1.00 91.67           N  
-ANISOU 6150  N   LYS A 819    12052  14169   8608  -1872  -1353   1770       N  
-ATOM   6151  CA  LYS A 819       0.698  -5.144 -37.161  1.00 91.37           C  
-ANISOU 6151  CA  LYS A 819    12157  13959   8601  -1869  -1239   1524       C  
-ATOM   6152  C   LYS A 819       1.544  -4.004 -37.718  1.00 90.95           C  
-ANISOU 6152  C   LYS A 819    12144  13895   8517  -1775  -1089   1470       C  
-ATOM   6153  O   LYS A 819       1.048  -2.896 -37.925  1.00 89.88           O  
-ANISOU 6153  O   LYS A 819    11942  13882   8326  -1725  -1081   1623       O  
-ATOM   6154  CB  LYS A 819       0.630  -6.296 -38.166  1.00 95.87           C  
-ANISOU 6154  CB  LYS A 819    12884  14493   9049  -2070  -1311   1409       C  
-ATOM   6155  CG  LYS A 819       1.869  -7.185 -38.171  1.00 99.61           C  
-ANISOU 6155  CG  LYS A 819    13486  14764   9597  -2066  -1216   1160       C  
-ATOM   6156  CD  LYS A 819       2.156  -7.748 -39.555  1.00106.54           C  
-ANISOU 6156  CD  LYS A 819    14554  15610  10317  -2227  -1208   1016       C  
-ATOM   6157  CE  LYS A 819       0.970  -8.525 -40.101  1.00112.40           C  
-ANISOU 6157  CE  LYS A 819    15336  16447  10924  -2435  -1383   1098       C  
-ATOM   6158  NZ  LYS A 819       1.166  -8.890 -41.534  1.00116.14           N  
-ANISOU 6158  NZ  LYS A 819    15998  16917  11212  -2598  -1377    974       N  
-ATOM   6159  N   GLY A 820       2.822  -4.277 -37.951  1.00 51.61           N  
-ANISOU 6159  N   GLY A 820     7268   8763   3577  -1748   -965   1256       N  
-ATOM   6160  CA  GLY A 820       3.725  -3.266 -38.464  1.00 54.41           C  
-ANISOU 6160  CA  GLY A 820     7666   9095   3914  -1666   -811   1188       C  
-ATOM   6161  C   GLY A 820       4.125  -2.254 -37.411  1.00 57.36           C  
-ANISOU 6161  C   GLY A 820     7913   9450   4433  -1476   -717   1237       C  
-ATOM   6162  O   GLY A 820       3.911  -2.470 -36.223  1.00 58.58           O  
-ANISOU 6162  O   GLY A 820     7960   9583   4715  -1400   -757   1285       O  
-ATOM   6163  N   VAL A 821       4.701  -1.142 -37.854  1.00 85.12           N  
-ANISOU 6163  N   VAL A 821    11446  12972   7923  -1406   -591   1225       N  
-ATOM   6164  CA  VAL A 821       5.248  -0.143 -36.944  1.00 87.40           C  
-ANISOU 6164  CA  VAL A 821    11637  13225   8346  -1236   -482   1240       C  
-ATOM   6165  C   VAL A 821       4.387   1.118 -36.890  1.00 93.70           C  
-ANISOU 6165  C   VAL A 821    12347  14153   9102  -1173   -491   1455       C  
-ATOM   6166  O   VAL A 821       3.632   1.407 -37.816  1.00 92.10           O  
-ANISOU 6166  O   VAL A 821    12177  14064   8752  -1254   -547   1572       O  
-ATOM   6167  CB  VAL A 821       6.696   0.226 -37.334  1.00 84.01           C  
-ANISOU 6167  CB  VAL A 821    11286  12682   7953  -1187   -309   1053       C  
-ATOM   6168  CG1 VAL A 821       7.255   1.298 -36.406  1.00 80.13           C  
-ANISOU 6168  CG1 VAL A 821    10695  12156   7596  -1025   -199   1067       C  
-ATOM   6169  CG2 VAL A 821       7.573  -1.014 -37.307  1.00 79.89           C  
-ANISOU 6169  CG2 VAL A 821    10837  12025   7491  -1227   -290    845       C  
-ATOM   6170  N   CYS A 822       4.510   1.857 -35.790  1.00133.04           N  
-ANISOU 6170  N   CYS A 822    17219  19116  14214  -1026   -434   1506       N  
-ATOM   6171  CA  CYS A 822       3.754   3.088 -35.573  1.00142.05           C  
-ANISOU 6171  CA  CYS A 822    18272  20359  15343   -940   -424   1704       C  
-ATOM   6172  C   CYS A 822       3.916   4.081 -36.723  1.00148.27           C  
-ANISOU 6172  C   CYS A 822    19134  21186  16014   -954   -339   1739       C  
-ATOM   6173  O   CYS A 822       5.029   4.494 -37.051  1.00148.29           O  
-ANISOU 6173  O   CYS A 822    19207  21099  16039   -925   -202   1600       O  
-ATOM   6174  CB  CYS A 822       4.173   3.738 -34.251  1.00141.45           C  
-ANISOU 6174  CB  CYS A 822    18098  20221  15427   -780   -340   1698       C  
-ATOM   6175  SG  CYS A 822       3.239   5.219 -33.810  1.00146.03           S  
-ANISOU 6175  SG  CYS A 822    18569  20903  16014   -657   -313   1934       S  
-ATOM   6176  N   ASP A 823       2.790   4.460 -37.321  1.00153.12           N  
-ANISOU 6176  N   ASP A 823    19728  21941  16509   -997   -423   1933       N  
-ATOM   6177  CA  ASP A 823       2.764   5.369 -38.466  1.00159.66           C  
-ANISOU 6177  CA  ASP A 823    20627  22828  17209  -1018   -366   2001       C  
-ATOM   6178  C   ASP A 823       3.728   6.544 -38.333  1.00160.03           C  
-ANISOU 6178  C   ASP A 823    20691  22786  17328   -898   -182   1943       C  
-ATOM   6179  O   ASP A 823       4.636   6.711 -39.147  1.00160.95           O  
-ANISOU 6179  O   ASP A 823    20918  22843  17394   -937    -79   1817       O  
-ATOM   6180  CB  ASP A 823       1.343   5.899 -38.690  1.00165.22           C  
-ANISOU 6180  CB  ASP A 823    21250  23699  17826  -1018   -471   2264       C  
-ATOM   6181  CG  ASP A 823       0.789   6.623 -37.472  1.00169.12           C  
-ANISOU 6181  CG  ASP A 823    21597  24213  18448   -864   -457   2408       C  
-ATOM   6182  OD1 ASP A 823       0.980   6.124 -36.342  1.00171.56           O  
-ANISOU 6182  OD1 ASP A 823    21842  24456  18888   -814   -465   2340       O  
-ATOM   6183  OD2 ASP A 823       0.169   7.695 -37.646  1.00171.81           O  
-ANISOU 6183  OD2 ASP A 823    21889  24634  18756   -790   -434   2592       O  
-ATOM   6184  N   GLN A 824       3.518   7.355 -37.302  1.00143.34           N  
-ANISOU 6184  N   GLN A 824    18469  20662  15330   -758   -137   2036       N  
-ATOM   6185  CA  GLN A 824       4.273   8.586 -37.128  1.00142.23           C  
-ANISOU 6185  CA  GLN A 824    18338  20445  15257   -646     30   2008       C  
-ATOM   6186  C   GLN A 824       4.513   8.874 -35.654  1.00137.28           C  
-ANISOU 6186  C   GLN A 824    17612  19747  14803   -515     78   1983       C  
-ATOM   6187  O   GLN A 824       4.635   7.960 -34.839  1.00137.67           O  
-ANISOU 6187  O   GLN A 824    17616  19760  14932   -521     17   1900       O  
-ATOM   6188  CB  GLN A 824       3.517   9.757 -37.756  1.00146.19           C  
-ANISOU 6188  CB  GLN A 824    18836  21040  15669   -607     51   2217       C  
-ATOM   6189  CG  GLN A 824       2.150  10.010 -37.131  1.00149.16           C  
-ANISOU 6189  CG  GLN A 824    19084  21529  16060   -541    -50   2446       C  
-ATOM   6190  CD  GLN A 824       1.499  11.281 -37.639  1.00151.23           C  
-ANISOU 6190  CD  GLN A 824    19334  21865  16260   -472     -7   2654       C  
-ATOM   6191  OE1 GLN A 824       2.029  11.953 -38.524  1.00152.13           O  
-ANISOU 6191  OE1 GLN A 824    19544  21952  16307   -485     91   2635       O  
-ATOM   6192  NE2 GLN A 824       0.342  11.618 -37.079  1.00150.83           N  
-ANISOU 6192  NE2 GLN A 824    19165  21909  16234   -395    -74   2861       N  
-ATOM   6193  N   SER A 825       4.572  10.159 -35.321  1.00125.31           N  
-ANISOU 6193  N   SER A 825    16067  18208  13338   -401    189   2058       N  
-ATOM   6194  CA  SER A 825       4.796  10.593 -33.952  1.00117.84           C  
-ANISOU 6194  CA  SER A 825    15037  17196  12542   -276    247   2037       C  
-ATOM   6195  C   SER A 825       3.717  11.582 -33.530  1.00112.48           C  
-ANISOU 6195  C   SER A 825    14278  16589  11870   -170    248   2259       C  
-ATOM   6196  O   SER A 825       3.135  12.273 -34.367  1.00112.92           O  
-ANISOU 6196  O   SER A 825    14359  16714  11833   -170    258   2408       O  
-ATOM   6197  CB  SER A 825       6.179  11.230 -33.820  1.00119.44           C  
-ANISOU 6197  CB  SER A 825    15292  17266  12824   -235    413   1864       C  
-ATOM   6198  OG  SER A 825       7.201  10.296 -34.120  1.00122.28           O  
-ANISOU 6198  OG  SER A 825    15709  17557  13193   -318    419   1658       O  
-ATOM   6199  N   PHE A 826       3.449  11.644 -32.230  1.00 99.94           N  
-ANISOU 6199  N   PHE A 826    12858  14475  10639    475  -1679   2304       N  
-ATOM   6200  CA  PHE A 826       2.411  12.524 -31.708  1.00 95.30           C  
-ANISOU 6200  CA  PHE A 826    12109  13996  10104    760  -1754   2530       C  
-ATOM   6201  C   PHE A 826       2.982  13.543 -30.728  1.00 89.44           C  
-ANISOU 6201  C   PHE A 826    11406  13025   9553   1020  -1595   2483       C  
-ATOM   6202  O   PHE A 826       2.266  14.409 -30.231  1.00 92.15           O  
-ANISOU 6202  O   PHE A 826    11641  13413   9958   1280  -1628   2654       O  
-ATOM   6203  CB  PHE A 826       1.309  11.706 -31.026  1.00 95.05           C  
-ANISOU 6203  CB  PHE A 826    11796  14213  10104    781  -1885   2598       C  
-ATOM   6204  CG  PHE A 826       0.583  10.773 -31.954  1.00 96.69           C  
-ANISOU 6204  CG  PHE A 826    11945  14674  10119    545  -2057   2676       C  
-ATOM   6205  CD1 PHE A 826      -0.435  11.239 -32.768  1.00 98.52           C  
-ANISOU 6205  CD1 PHE A 826    12133  15106  10195    584  -2214   2930       C  
-ATOM   6206  CD2 PHE A 826       0.914   9.429 -32.006  1.00 95.68           C  
-ANISOU 6206  CD2 PHE A 826    11808  14583   9962    284  -2061   2498       C  
-ATOM   6207  CE1 PHE A 826      -1.106  10.384 -33.620  1.00 99.05           C  
-ANISOU 6207  CE1 PHE A 826    12146  15410  10079    362  -2371   3004       C  
-ATOM   6208  CE2 PHE A 826       0.245   8.569 -32.857  1.00 96.71           C  
-ANISOU 6208  CE2 PHE A 826    11890  14945   9910     62  -2217   2569       C  
-ATOM   6209  CZ  PHE A 826      -0.766   9.048 -33.664  1.00 98.60           C  
-ANISOU 6209  CZ  PHE A 826    12084  15386   9993     98  -2372   2823       C  
-ATOM   6210  N   GLY A 827       4.276  13.433 -30.459  1.00 78.06           N  
-ANISOU 6210  N   GLY A 827    10120  11338   8200    946  -1421   2249       N  
-ATOM   6211  CA  GLY A 827       4.934  14.276 -29.479  1.00 72.13           C  
-ANISOU 6211  CA  GLY A 827     9413  10360   7635   1163  -1256   2173       C  
-ATOM   6212  C   GLY A 827       4.581  15.748 -29.568  1.00 70.11           C  
-ANISOU 6212  C   GLY A 827     9207  10051   7379   1420  -1253   2370       C  
-ATOM   6213  O   GLY A 827       3.940  16.295 -28.674  1.00 70.51           O  
-ANISOU 6213  O   GLY A 827     9106  10139   7546   1670  -1263   2478       O  
-ATOM   6214  N   ILE A 828       5.000  16.395 -30.648  1.00 84.33           N  
-ANISOU 6214  N   ILE A 828    11226  11764   9050   1360  -1237   2417       N  
-ATOM   6215  CA  ILE A 828       4.836  17.837 -30.777  1.00 82.52           C  
-ANISOU 6215  CA  ILE A 828    11085  11447   8820   1594  -1213   2584       C  
-ATOM   6216  C   ILE A 828       3.369  18.251 -30.734  1.00 82.91           C  
-ANISOU 6216  C   ILE A 828    10940  11729   8832   1784  -1379   2859       C  
-ATOM   6217  O   ILE A 828       3.034  19.335 -30.262  1.00 81.94           O  
-ANISOU 6217  O   ILE A 828    10795  11553   8784   2053  -1353   2990       O  
-ATOM   6218  CB  ILE A 828       5.499  18.367 -32.063  1.00 83.27           C  
-ANISOU 6218  CB  ILE A 828    11451  11429   8760   1465  -1184   2592       C  
-ATOM   6219  CG1 ILE A 828       6.954  17.902 -32.136  1.00 81.17           C  
-ANISOU 6219  CG1 ILE A 828    11372  10946   8524   1266  -1022   2315       C  
-ATOM   6220  CG2 ILE A 828       5.424  19.882 -32.118  1.00 81.64           C  
-ANISOU 6220  CG2 ILE A 828    11349  11105   8564   1713  -1143   2748       C  
-ATOM   6221  CD1 ILE A 828       7.719  18.500 -33.297  1.00 85.15           C  
-ANISOU 6221  CD1 ILE A 828    12151  11312   8891   1153   -971   2304       C  
-ATOM   6222  N   HIS A 829       2.494  17.378 -31.216  1.00 75.14           N  
-ANISOU 6222  N   HIS A 829     9815  11005   7729   1643  -1548   2946       N  
-ATOM   6223  CA  HIS A 829       1.068  17.666 -31.192  1.00 79.08           C  
-ANISOU 6223  CA  HIS A 829    10113  11750   8183   1806  -1715   3206       C  
-ATOM   6224  C   HIS A 829       0.551  17.774 -29.755  1.00 77.76           C  
-ANISOU 6224  C   HIS A 829     9723  11613   8208   2047  -1693   3222       C  
-ATOM   6225  O   HIS A 829      -0.336  18.578 -29.461  1.00 80.55           O  
-ANISOU 6225  O   HIS A 829     9965  12055   8587   2295  -1755   3426       O  
-ATOM   6226  CB  HIS A 829       0.289  16.600 -31.964  1.00 83.61           C  
-ANISOU 6226  CB  HIS A 829    10578  12600   8591   1581  -1895   3275       C  
-ATOM   6227  CG  HIS A 829      -1.188  16.834 -31.981  1.00 90.58           C  
-ANISOU 6227  CG  HIS A 829    11247  13754   9415   1732  -2073   3543       C  
-ATOM   6228  ND1 HIS A 829      -1.744  18.043 -32.340  1.00 94.10           N  
-ANISOU 6228  ND1 HIS A 829    11721  14218   9813   1944  -2120   3770       N  
-ATOM   6229  CD2 HIS A 829      -2.225  16.021 -31.669  1.00 92.35           C  
-ANISOU 6229  CD2 HIS A 829    11224  14243   9620   1705  -2215   3620       C  
-ATOM   6230  CE1 HIS A 829      -3.059  17.963 -32.254  1.00 95.65           C  
-ANISOU 6230  CE1 HIS A 829    11693  14683   9965   2043  -2283   3977       C  
-ATOM   6231  NE2 HIS A 829      -3.378  16.747 -31.849  1.00 94.82           N  
-ANISOU 6231  NE2 HIS A 829    11417  14735   9874   1899  -2344   3891       N  
-ATOM   6232  N   VAL A 830       1.117  16.964 -28.866  1.00 73.16           N  
-ANISOU 6232  N   VAL A 830     9081  10956   7760   1974  -1601   3006       N  
-ATOM   6233  CA  VAL A 830       0.765  16.996 -27.450  1.00 71.93           C  
-ANISOU 6233  CA  VAL A 830     8726  10809   7797   2182  -1563   2989       C  
-ATOM   6234  C   VAL A 830       1.216  18.303 -26.804  1.00 73.55           C  
-ANISOU 6234  C   VAL A 830     9022  10786   8138   2450  -1418   3002       C  
-ATOM   6235  O   VAL A 830       0.581  18.798 -25.874  1.00 73.37           O  
-ANISOU 6235  O   VAL A 830     8840  10802   8235   2698  -1423   3098       O  
-ATOM   6236  CB  VAL A 830       1.402  15.820 -26.682  1.00 65.71           C  
-ANISOU 6236  CB  VAL A 830     7877   9970   7120   2024  -1487   2737       C  
-ATOM   6237  CG1 VAL A 830       0.936  15.813 -25.238  1.00 64.43           C  
-ANISOU 6237  CG1 VAL A 830     7493   9841   7147   2231  -1464   2734       C  
-ATOM   6238  CG2 VAL A 830       1.062  14.503 -27.355  1.00 65.82           C  
-ANISOU 6238  CG2 VAL A 830     7827  10186   6994   1741  -1618   2706       C  
-ATOM   6239  N   ALA A 831       2.317  18.857 -27.300  1.00 87.67           N  
-ANISOU 6239  N   ALA A 831    11069  12336   9905   2395  -1288   2903       N  
-ATOM   6240  CA  ALA A 831       2.833  20.119 -26.787  1.00 88.50           C  
-ANISOU 6240  CA  ALA A 831    11294  12210  10123   2628  -1144   2908       C  
-ATOM   6241  C   ALA A 831       1.860  21.257 -27.064  1.00 93.37           C  
-ANISOU 6241  C   ALA A 831    11877  12912  10686   2870  -1234   3184       C  
-ATOM   6242  O   ALA A 831       1.627  22.106 -26.207  1.00 93.52           O  
-ANISOU 6242  O   ALA A 831    11840  12860  10834   3138  -1175   3252       O  
-ATOM   6243  CB  ALA A 831       4.189  20.425 -27.396  1.00 88.13           C  
-ANISOU 6243  CB  ALA A 831    11537  11910  10038   2492  -1000   2751       C  
-ATOM   6244  N   GLU A 832       1.294  21.271 -28.266  1.00 85.08           N  
-ANISOU 6244  N   GLU A 832    10866  12017   9444   2776  -1376   3344       N  
-ATOM   6245  CA  GLU A 832       0.326  22.294 -28.642  1.00 91.28           C  
-ANISOU 6245  CA  GLU A 832    11619  12904  10160   2991  -1477   3618       C  
-ATOM   6246  C   GLU A 832      -0.920  22.187 -27.777  1.00 92.55           C  
-ANISOU 6246  C   GLU A 832    11486  13279  10400   3187  -1582   3762       C  
-ATOM   6247  O   GLU A 832      -1.450  23.193 -27.311  1.00 94.93           O  
-ANISOU 6247  O   GLU A 832    11735  13565  10769   3469  -1576   3915       O  
-ATOM   6248  CB  GLU A 832      -0.051  22.162 -30.116  1.00 95.00           C  
-ANISOU 6248  CB  GLU A 832    12172  13522  10403   2818  -1620   3752       C  
-ATOM   6249  CG  GLU A 832       1.079  22.463 -31.082  1.00 96.61           C  
-ANISOU 6249  CG  GLU A 832    12676  13522  10510   2649  -1527   3648       C  
-ATOM   6250  CD  GLU A 832       0.744  22.049 -32.501  1.00 98.61           C  
-ANISOU 6250  CD  GLU A 832    12991  13940  10538   2425  -1671   3745       C  
-ATOM   6251  OE1 GLU A 832      -0.098  21.139 -32.667  1.00 97.60           O  
-ANISOU 6251  OE1 GLU A 832    12678  14067  10339   2316  -1820   3809       O  
-ATOM   6252  OE2 GLU A 832       1.318  22.632 -33.448  1.00 98.68           O  
-ANISOU 6252  OE2 GLU A 832    13232  13824  10438   2353  -1636   3758       O  
-ATOM   6253  N   LEU A 833      -1.382  20.958 -27.569  1.00 99.83           N  
-ANISOU 6253  N   LEU A 833    12218  14400  11311   3035  -1677   3711       N  
-ATOM   6254  CA  LEU A 833      -2.544  20.704 -26.724  1.00101.40           C  
-ANISOU 6254  CA  LEU A 833    12125  14818  11583   3192  -1780   3828       C  
-ATOM   6255  C   LEU A 833      -2.320  21.212 -25.306  1.00100.56           C  
-ANISOU 6255  C   LEU A 833    11948  14560  11700   3433  -1643   3755       C  
-ATOM   6256  O   LEU A 833      -3.223  21.779 -24.692  1.00101.23           O  
-ANISOU 6256  O   LEU A 833    11868  14744  11851   3686  -1691   3917       O  
-ATOM   6257  CB  LEU A 833      -2.873  19.210 -26.696  1.00102.71           C  
-ANISOU 6257  CB  LEU A 833    12128  15191  11708   2954  -1881   3741       C  
-ATOM   6258  CG  LEU A 833      -3.314  18.607 -28.029  1.00106.37           C  
-ANISOU 6258  CG  LEU A 833    12616  15854  11946   2717  -2040   3835       C  
-ATOM   6259  CD1 LEU A 833      -3.687  17.144 -27.864  1.00108.19           C  
-ANISOU 6259  CD1 LEU A 833    12672  16287  12148   2501  -2136   3750       C  
-ATOM   6260  CD2 LEU A 833      -4.479  19.397 -28.589  1.00109.91           C  
-ANISOU 6260  CD2 LEU A 833    12988  16489  12283   2887  -2186   4134       C  
-ATOM   6261  N   ALA A 834      -1.112  21.007 -24.790  1.00 78.54           N  
-ANISOU 6261  N   ALA A 834     9282  11533   9025   3353  -1472   3511       N  
-ATOM   6262  CA  ALA A 834      -0.764  21.462 -23.448  1.00 78.01           C  
-ANISOU 6262  CA  ALA A 834     9168  11302   9171   3559  -1328   3420       C  
-ATOM   6263  C   ALA A 834      -0.480  22.960 -23.432  1.00 78.45           C  
-ANISOU 6263  C   ALA A 834     9387  11156   9265   3798  -1225   3510       C  
-ATOM   6264  O   ALA A 834       0.242  23.453 -22.568  1.00 78.46           O  
-ANISOU 6264  O   ALA A 834     9455  10937   9420   3916  -1060   3389       O  
-ATOM   6265  CB  ALA A 834       0.430  20.687 -22.917  1.00 77.88           C  
-ANISOU 6265  CB  ALA A 834     9223  11110   9257   3381  -1184   3129       C  
-ATOM   6266  N   ASN A 835      -1.055  23.675 -24.396  1.00102.41           N  
-ANISOU 6266  N   ASN A 835    12488  14268  12156   3864  -1323   3723       N  
-ATOM   6267  CA  ASN A 835      -0.903  25.124 -24.503  1.00102.70           C  
-ANISOU 6267  CA  ASN A 835    12683  14132  12205   4092  -1246   3837       C  
-ATOM   6268  C   ASN A 835       0.556  25.580 -24.468  1.00 98.38           C  
-ANISOU 6268  C   ASN A 835    12404  13260  11715   4037  -1045   3642       C  
-ATOM   6269  O   ASN A 835       0.923  26.453 -23.683  1.00 97.60           O  
-ANISOU 6269  O   ASN A 835    12363  12972  11750   4241   -910   3616       O  
-ATOM   6270  CB  ASN A 835      -1.712  25.830 -23.420  1.00101.63           C  
-ANISOU 6270  CB  ASN A 835    12370  14035  12209   4419  -1241   3967       C  
-ATOM   6271  N   PHE A 836       1.384  24.985 -25.320  1.00 94.96           N  
-ANISOU 6271  N   PHE A 836    12135  12767  11177   3757  -1025   3504       N  
-ATOM   6272  CA  PHE A 836       2.769  25.419 -25.454  1.00 90.87           C  
-ANISOU 6272  CA  PHE A 836    11885  11957  10686   3683   -846   3328       C  
-ATOM   6273  C   PHE A 836       2.824  26.689 -26.291  1.00 93.49           C  
-ANISOU 6273  C   PHE A 836    12426  12182  10914   3794   -837   3483       C  
-ATOM   6274  O   PHE A 836       2.113  26.806 -27.290  1.00 93.50           O  
-ANISOU 6274  O   PHE A 836    12428  12341  10755   3765   -983   3666       O  
-ATOM   6275  CB  PHE A 836       3.618  24.324 -26.104  1.00 86.51           C  
-ANISOU 6275  CB  PHE A 836    11433  11386  10052   3344   -830   3129       C  
-ATOM   6276  CG  PHE A 836       4.572  23.655 -25.161  1.00 80.83           C  
-ANISOU 6276  CG  PHE A 836    10703  10523   9484   3255   -684   2864       C  
-ATOM   6277  CD1 PHE A 836       5.870  24.115 -25.026  1.00 79.29           C  
-ANISOU 6277  CD1 PHE A 836    10729  10050   9349   3226   -497   2692       C  
-ATOM   6278  CD2 PHE A 836       4.171  22.567 -24.409  1.00 79.10           C  
-ANISOU 6278  CD2 PHE A 836    10254  10452   9348   3199   -734   2789       C  
-ATOM   6279  CE1 PHE A 836       6.751  23.503 -24.155  1.00 76.75           C  
-ANISOU 6279  CE1 PHE A 836    10394   9600   9166   3147   -363   2452       C  
-ATOM   6280  CE2 PHE A 836       5.048  21.948 -23.533  1.00 76.54           C  
-ANISOU 6280  CE2 PHE A 836     9919   9997   9166   3120   -601   2548       C  
-ATOM   6281  CZ  PHE A 836       6.341  22.417 -23.408  1.00 74.84           C  
-ANISOU 6281  CZ  PHE A 836     9922   9505   9009   3095   -415   2380       C  
-ATOM   6282  N   PRO A 837       3.668  27.650 -25.886  1.00 70.76           N  
-ANISOU 6282  N   PRO A 837     9726   9035   8123   3919   -666   3411       N  
-ATOM   6283  CA  PRO A 837       3.758  28.906 -26.631  1.00 72.53           C  
-ANISOU 6283  CA  PRO A 837    10161   9141   8255   4031   -648   3554       C  
-ATOM   6284  C   PRO A 837       3.919  28.615 -28.111  1.00 73.75           C  
-ANISOU 6284  C   PRO A 837    10462   9358   8201   3791   -738   3586       C  
-ATOM   6285  O   PRO A 837       4.743  27.774 -28.471  1.00 72.46           O  
-ANISOU 6285  O   PRO A 837    10381   9151   7998   3526   -697   3394       O  
-ATOM   6286  CB  PRO A 837       5.040  29.541 -26.091  1.00 70.90           C  
-ANISOU 6286  CB  PRO A 837    10161   8619   8158   4067   -428   3374       C  
-ATOM   6287  CG  PRO A 837       5.199  28.979 -24.735  1.00 68.72           C  
-ANISOU 6287  CG  PRO A 837     9716   8322   8073   4115   -345   3221       C  
-ATOM   6288  CD  PRO A 837       4.637  27.587 -24.780  1.00 68.30           C  
-ANISOU 6288  CD  PRO A 837     9445   8514   7991   3939   -479   3188       C  
-ATOM   6289  N   LYS A 838       3.139  29.290 -28.951  1.00102.87           N  
-ANISOU 6289  N   LYS A 838    14180  13150  11757   3882   -860   3824       N  
-ATOM   6290  CA  LYS A 838       3.241  29.116 -30.397  1.00103.41           C  
-ANISOU 6290  CA  LYS A 838    14393  13279  11619   3665   -951   3874       C  
-ATOM   6291  C   LYS A 838       4.695  29.206 -30.848  1.00102.08           C  
-ANISOU 6291  C   LYS A 838    14505  12862  11420   3476   -799   3669       C  
-ATOM   6292  O   LYS A 838       5.157  28.404 -31.657  1.00101.44           O  
-ANISOU 6292  O   LYS A 838    14498  12817  11226   3196   -827   3563       O  
-ATOM   6293  CB  LYS A 838       2.392  30.155 -31.119  1.00104.02           C  
-ANISOU 6293  CB  LYS A 838    14511  13429  11581   3839  -1060   4154       C  
-ATOM   6294  N   HIS A 839       5.411  30.186 -30.308  1.00108.00           N  
-ANISOU 6294  N   HIS A 839    15407  13358  12269   3630   -635   3611       N  
-ATOM   6295  CA  HIS A 839       6.815  30.405 -30.635  1.00106.40           C  
-ANISOU 6295  CA  HIS A 839    15475  12905  12048   3479   -477   3420       C  
-ATOM   6296  C   HIS A 839       7.661  29.142 -30.492  1.00101.73           C  
-ANISOU 6296  C   HIS A 839    14868  12296  11487   3208   -415   3157       C  
-ATOM   6297  O   HIS A 839       8.505  28.853 -31.340  1.00100.31           O  
-ANISOU 6297  O   HIS A 839    14872  12041  11202   2971   -378   3038       O  
-ATOM   6298  CB  HIS A 839       7.384  31.505 -29.739  1.00108.62           C  
-ANISOU 6298  CB  HIS A 839    15865  12933  12471   3705   -302   3378       C  
-ATOM   6299  CG  HIS A 839       8.837  31.784 -29.965  1.00111.23           C  
-ANISOU 6299  CG  HIS A 839    16466  13002  12793   3566   -129   3180       C  
-ATOM   6300  ND1 HIS A 839       9.496  31.408 -31.116  1.00113.41           N  
-ANISOU 6300  ND1 HIS A 839    16917  13259  12915   3296   -140   3100       N  
-ATOM   6301  CD2 HIS A 839       9.758  32.402 -29.189  1.00111.55           C  
-ANISOU 6301  CD2 HIS A 839    16632  12794  12957   3655     61   3045       C  
-ATOM   6302  CE1 HIS A 839      10.763  31.785 -31.038  1.00114.74           C  
-ANISOU 6302  CE1 HIS A 839    17304  13179  13113   3228     34   2924       C  
-ATOM   6303  NE2 HIS A 839      10.945  32.389 -29.878  1.00113.09           N  
-ANISOU 6303  NE2 HIS A 839    17070  12829  13070   3442    159   2888       N  
-ATOM   6304  N   VAL A 840       7.431  28.394 -29.417  1.00 94.05           N  
-ANISOU 6304  N   VAL A 840    13677  11396  10660   3243   -404   3067       N  
-ATOM   6305  CA  VAL A 840       8.279  27.251 -29.085  1.00 88.22           C  
-ANISOU 6305  CA  VAL A 840    12920  10617   9981   3018   -325   2807       C  
-ATOM   6306  C   VAL A 840       7.911  25.970 -29.831  1.00 87.36           C  
-ANISOU 6306  C   VAL A 840    12713  10729   9750   2760   -469   2789       C  
-ATOM   6307  O   VAL A 840       8.791  25.218 -30.248  1.00 84.93           O  
-ANISOU 6307  O   VAL A 840    12509  10363   9398   2507   -416   2599       O  
-ATOM   6308  CB  VAL A 840       8.287  26.970 -27.573  1.00 86.08           C  
-ANISOU 6308  CB  VAL A 840    12469  10313   9923   3153   -240   2701       C  
-ATOM   6309  CG1 VAL A 840       9.259  25.842 -27.254  1.00 81.93           C  
-ANISOU 6309  CG1 VAL A 840    11946   9725   9458   2921   -148   2427       C  
-ATOM   6310  CG2 VAL A 840       8.657  28.232 -26.809  1.00 82.67           C  
-ANISOU 6310  CG2 VAL A 840    12136   9661   9612   3404    -93   2716       C  
-ATOM   6311  N   ILE A 841       6.615  25.719 -29.994  1.00 85.52           N  
-ANISOU 6311  N   ILE A 841    12283  10750   9462   2823   -648   2984       N  
-ATOM   6312  CA  ILE A 841       6.172  24.549 -30.743  1.00 85.57           C  
-ANISOU 6312  CA  ILE A 841    12195  10979   9339   2583   -795   2988       C  
-ATOM   6313  C   ILE A 841       6.637  24.625 -32.194  1.00 87.09           C  
-ANISOU 6313  C   ILE A 841    12613  11142   9334   2370   -824   2997       C  
-ATOM   6314  O   ILE A 841       6.537  23.650 -32.941  1.00 86.87           O  
-ANISOU 6314  O   ILE A 841    12564  11257   9187   2126   -918   2961       O  
-ATOM   6315  CB  ILE A 841       4.640  24.375 -30.707  1.00 87.33           C  
-ANISOU 6315  CB  ILE A 841    12168  11488   9524   2700   -989   3220       C  
-ATOM   6316  CG1 ILE A 841       3.942  25.708 -30.980  1.00 90.89           C  
-ANISOU 6316  CG1 ILE A 841    12658  11944   9932   2953  -1040   3474       C  
-ATOM   6317  CG2 ILE A 841       4.194  23.804 -29.371  1.00 85.82           C  
-ANISOU 6317  CG2 ILE A 841    11723  11377   9506   2812   -984   3167       C  
-ATOM   6318  CD1 ILE A 841       2.433  25.649 -30.841  1.00 93.28           C  
-ANISOU 6318  CD1 ILE A 841    12707  12522  10212   3103  -1220   3710       C  
-ATOM   6319  N   GLU A 842       7.152  25.787 -32.586  1.00 92.46           N  
-ANISOU 6319  N   GLU A 842    13514  11637   9981   2460   -742   3041       N  
-ATOM   6320  CA  GLU A 842       7.670  25.973 -33.937  1.00 93.27           C  
-ANISOU 6320  CA  GLU A 842    13848  11688   9901   2268   -755   3045       C  
-ATOM   6321  C   GLU A 842       9.167  25.712 -33.981  1.00 87.41           C  
-ANISOU 6321  C   GLU A 842    13307  10720   9184   2080   -581   2776       C  
-ATOM   6322  O   GLU A 842       9.643  24.930 -34.801  1.00 87.19           O  
-ANISOU 6322  O   GLU A 842    13363  10722   9043   1807   -600   2666       O  
-ATOM   6323  CB  GLU A 842       7.347  27.375 -34.453  1.00102.05           C  
-ANISOU 6323  CB  GLU A 842    15095  12739  10940   2456   -777   3258       C  
-ATOM   6324  CG  GLU A 842       5.854  27.675 -34.487  1.00114.86           C  
-ANISOU 6324  CG  GLU A 842    16524  14592  12527   2646   -953   3536       C  
-ATOM   6325  CD  GLU A 842       5.048  26.566 -35.141  1.00121.50           C  
-ANISOU 6325  CD  GLU A 842    17207  15716  13243   2456  -1135   3602       C  
-ATOM   6326  OE1 GLU A 842       5.544  25.958 -36.112  1.00126.36           O  
-ANISOU 6326  OE1 GLU A 842    17942  16346  13722   2180  -1156   3514       O  
-ATOM   6327  OE2 GLU A 842       3.921  26.296 -34.676  1.00125.76           O  
-ANISOU 6327  OE2 GLU A 842    17501  16464  13818   2579  -1255   3739       O  
-ATOM   6328  N   CYS A 843       9.905  26.371 -33.095  1.00100.58           N  
-ANISOU 6328  N   CYS A 843    15052  12164  11000   2226   -411   2671       N  
-ATOM   6329  CA ACYS A 843      11.336  26.132 -32.980  0.50 81.53           C  
-ANISOU 6329  CA ACYS A 843    12810   9536   8630   2067   -236   2409       C  
-ATOM   6330  CA BCYS A 843      11.337  26.132 -32.956  0.50 81.46           C  
-ANISOU 6330  CA BCYS A 843    12799   9526   8625   2070   -234   2408       C  
-ATOM   6331  C   CYS A 843      11.599  24.642 -32.782  1.00 68.43           C  
-ANISOU 6331  C   CYS A 843    11032   7969   7001   1842   -244   2219       C  
-ATOM   6332  O   CYS A 843      12.693  24.149 -33.070  1.00 66.54           O  
-ANISOU 6332  O   CYS A 843    10932   7611   6739   1631   -143   2010       O  
-ATOM   6333  CB ACYS A 843      11.928  26.940 -31.824  0.50 82.86           C  
-ANISOU 6333  CB ACYS A 843    13021   9484   8978   2278    -61   2330       C  
-ATOM   6334  CB BCYS A 843      11.894  26.901 -31.756  0.50 82.79           C  
-ANISOU 6334  CB BCYS A 843    12996   9482   8979   2284    -63   2329       C  
-ATOM   6335  SG ACYS A 843      11.831  28.733 -32.036  0.50 99.95           S  
-ANISOU 6335  SG ACYS A 843    15370  11495  11113   2531    -19   2522       S  
-ATOM   6336  SG BCYS A 843      13.535  26.354 -31.198  0.50 64.28           S  
-ANISOU 6336  SG BCYS A 843    10772   6910   6741   2113    154   1987       S  
-ATOM   6337  N   ALA A 844      10.583  23.933 -32.300  1.00 74.96           N  
-ANISOU 6337  N   ALA A 844    11602   9008   7872   1887   -367   2295       N  
-ATOM   6338  CA  ALA A 844      10.676  22.497 -32.074  1.00 71.45           C  
-ANISOU 6338  CA  ALA A 844    11023   8671   7453   1688   -393   2136       C  
-ATOM   6339  C   ALA A 844      10.348  21.718 -33.345  1.00 74.20           C  
-ANISOU 6339  C   ALA A 844    11393   9196   7604   1434   -536   2178       C  
-ATOM   6340  O   ALA A 844      11.041  20.758 -33.688  1.00 72.37           O  
-ANISOU 6340  O   ALA A 844    11218   8948   7333   1184   -501   1993       O  
-ATOM   6341  CB  ALA A 844       9.764  22.080 -30.940  1.00 68.26           C  
-ANISOU 6341  CB  ALA A 844    10336   8411   7187   1845   -455   2189       C  
-ATOM   6342  N   LYS A 845       9.288  22.129 -34.037  1.00 69.14           N  
-ANISOU 6342  N   LYS A 845    10706   8724   6839   1500   -695   2424       N  
-ATOM   6343  CA  LYS A 845       8.961  21.557 -35.343  1.00 70.61           C  
-ANISOU 6343  CA  LYS A 845    10936   9071   6820   1268   -831   2489       C  
-ATOM   6344  C   LYS A 845      10.149  21.698 -36.287  1.00 72.28           C  
-ANISOU 6344  C   LYS A 845    11428   9109   6926   1064   -733   2353       C  
-ATOM   6345  O   LYS A 845      10.386  20.847 -37.144  1.00 72.14           O  
-ANISOU 6345  O   LYS A 845    11465   9163   6781    797   -780   2275       O  
-ATOM   6346  CB  LYS A 845       7.724  22.228 -35.946  1.00 73.20           C  
-ANISOU 6346  CB  LYS A 845    11202   9578   7034   1400  -1000   2787       C  
-ATOM   6347  CG  LYS A 845       6.407  21.677 -35.422  1.00 73.99           C  
-ANISOU 6347  CG  LYS A 845    11008   9937   7166   1494  -1153   2927       C  
-ATOM   6348  CD  LYS A 845       5.211  22.415 -36.008  1.00 76.36           C  
-ANISOU 6348  CD  LYS A 845    11250  10408   7355   1639  -1313   3227       C  
-ATOM   6349  CE  LYS A 845       3.897  21.851 -35.477  1.00 76.89           C  
-ANISOU 6349  CE  LYS A 845    11019  10745   7452   1729  -1465   3364       C  
-ATOM   6350  NZ  LYS A 845       2.719  22.643 -35.927  1.00 79.43           N  
-ANISOU 6350  NZ  LYS A 845    11269  11230   7682   1905  -1613   3663       N  
-ATOM   6351  N   GLN A 846      10.895  22.781 -36.107  1.00 87.43           N  
-ANISOU 6351  N   GLN A 846    13523  10799   8898   1191   -594   2323       N  
-ATOM   6352  CA  GLN A 846      12.105  23.027 -36.872  1.00 89.69           C  
-ANISOU 6352  CA  GLN A 846    14081  10897   9101   1021   -480   2184       C  
-ATOM   6353  C   GLN A 846      13.140  21.953 -36.568  1.00 86.38           C  
-ANISOU 6353  C   GLN A 846    13683  10393   8744    810   -365   1898       C  
-ATOM   6354  O   GLN A 846      13.586  21.234 -37.462  1.00 84.94           O  
-ANISOU 6354  O   GLN A 846    13598  10240   8437    546   -382   1799       O  
-ATOM   6355  CB  GLN A 846      12.658  24.405 -36.518  1.00 95.27           C  
-ANISOU 6355  CB  GLN A 846    14948  11374   9878   1226   -345   2205       C  
-ATOM   6356  CG  GLN A 846      13.808  24.878 -37.382  1.00103.87           C  
-ANISOU 6356  CG  GLN A 846    16329  12273  10865   1077   -238   2101       C  
-ATOM   6357  CD  GLN A 846      14.247  26.282 -37.013  1.00110.55           C  
-ANISOU 6357  CD  GLN A 846    17327  12904  11774   1292   -116   2144       C  
-ATOM   6358  OE1 GLN A 846      15.217  26.469 -36.277  1.00114.12           O  
-ANISOU 6358  OE1 GLN A 846    17854  13159  12349   1324     56   1967       O  
-ATOM   6359  NE2 GLN A 846      13.522  27.280 -37.511  1.00116.29           N  
-ANISOU 6359  NE2 GLN A 846    18099  13669  12417   1442   -205   2381       N  
-ATOM   6360  N   LYS A 847      13.509  21.846 -35.294  1.00 86.84           N  
-ANISOU 6360  N   LYS A 847    13650  10351   8996    931   -249   1769       N  
-ATOM   6361  CA  LYS A 847      14.478  20.850 -34.849  1.00 83.23           C  
-ANISOU 6361  CA  LYS A 847    13195   9808   8620    761   -134   1499       C  
-ATOM   6362  C   LYS A 847      14.031  19.440 -35.196  1.00 84.29           C  
-ANISOU 6362  C   LYS A 847    13194  10147   8687    546   -253   1456       C  
-ATOM   6363  O   LYS A 847      14.856  18.547 -35.391  1.00 83.67           O  
-ANISOU 6363  O   LYS A 847    13177  10018   8594    324   -187   1248       O  
-ATOM   6364  CB  LYS A 847      14.698  20.956 -33.343  1.00 79.60           C  
-ANISOU 6364  CB  LYS A 847    12615   9246   8384    951    -17   1406       C  
-ATOM   6365  CG  LYS A 847      16.073  21.459 -32.948  1.00 76.67           C  
-ANISOU 6365  CG  LYS A 847    12427   8604   8099    957    193   1215       C  
-ATOM   6366  CD  LYS A 847      17.161  20.455 -33.281  1.00 73.98           C  
-ANISOU 6366  CD  LYS A 847    12181   8198   7730    682    278    964       C  
-ATOM   6367  CE  LYS A 847      18.521  20.949 -32.797  1.00 72.93           C  
-ANISOU 6367  CE  LYS A 847    12214   7804   7692    698    491    773       C  
-ATOM   6368  NZ  LYS A 847      19.618  19.957 -33.011  1.00 71.44           N  
-ANISOU 6368  NZ  LYS A 847    12105   7548   7492    445    585    519       N  
-ATOM   6369  N   ALA A 848      12.721  19.241 -35.260  1.00 82.28           N  
-ANISOU 6369  N   ALA A 848    12752  10121   8389    613   -428   1652       N  
-ATOM   6370  CA  ALA A 848      12.178  17.938 -35.603  1.00 83.86           C  
-ANISOU 6370  CA  ALA A 848    12818  10532   8514    415   -555   1634       C  
-ATOM   6371  C   ALA A 848      12.696  17.497 -36.968  1.00 85.27           C  
-ANISOU 6371  C   ALA A 848    13179  10716   8502    127   -577   1570       C  
-ATOM   6372  O   ALA A 848      13.154  16.366 -37.136  1.00 84.54           O  
-ANISOU 6372  O   ALA A 848    13088  10646   8387    -99   -560   1396       O  
-ATOM   6373  CB  ALA A 848      10.660  17.979 -35.595  1.00 85.50           C  
-ANISOU 6373  CB  ALA A 848    12817  10988   8680    540   -746   1885       C  
-ATOM   6374  N   LEU A 849      12.628  18.407 -37.935  1.00 92.31           N  
-ANISOU 6374  N   LEU A 849    14230  11585   9257    138   -613   1711       N  
-ATOM   6375  CA  LEU A 849      13.046  18.113 -39.299  1.00 92.89           C  
-ANISOU 6375  CA  LEU A 849    14485  11672   9138   -126   -643   1675       C  
-ATOM   6376  C   LEU A 849      14.538  17.812 -39.395  1.00 90.12           C  
-ANISOU 6376  C   LEU A 849    14324  11109   8810   -298   -466   1405       C  
-ATOM   6377  O   LEU A 849      14.948  16.884 -40.088  1.00 89.14           O  
-ANISOU 6377  O   LEU A 849    14262  11020   8586   -560   -475   1279       O  
-ATOM   6378  CB  LEU A 849      12.670  19.265 -40.233  1.00 98.30           C  
-ANISOU 6378  CB  LEU A 849    15302  12363   9684    -53   -711   1890       C  
-ATOM   6379  CG  LEU A 849      11.168  19.486 -40.424  1.00102.25           C  
-ANISOU 6379  CG  LEU A 849    15631  13102  10117     73   -907   2171       C  
-ATOM   6380  CD1 LEU A 849      10.912  20.672 -41.341  1.00106.71           C  
-ANISOU 6380  CD1 LEU A 849    16346  13649  10550    147   -959   2371       C  
-ATOM   6381  CD2 LEU A 849      10.490  18.227 -40.958  1.00104.95           C  
-ANISOU 6381  CD2 LEU A 849    15843  13687  10347   -144  -1057   2188       C  
-ATOM   6382  N   GLU A 850      15.349  18.600 -38.701  1.00 89.84           N  
-ANISOU 6382  N   GLU A 850    14381  10853   8902   -150   -304   1316       N  
-ATOM   6383  CA AGLU A 850      16.796  18.405 -38.702  0.50 78.49           C  
-ANISOU 6383  CA AGLU A 850    13120   9207   7497   -290   -125   1061       C  
-ATOM   6384  CA BGLU A 850      16.790  18.398 -38.730  0.50 78.57           C  
-ANISOU 6384  CA BGLU A 850    13131   9219   7502   -295   -128   1063       C  
-ATOM   6385  C   GLU A 850      17.165  17.019 -38.185  1.00 76.02           C  
-ANISOU 6385  C   GLU A 850    12696   8925   7262   -444    -88    850       C  
-ATOM   6386  O   GLU A 850      18.250  16.505 -38.463  1.00 71.49           O  
-ANISOU 6386  O   GLU A 850    12255   8238   6671   -634     22    637       O  
-ATOM   6387  CB AGLU A 850      17.489  19.466 -37.843  0.50 71.52           C  
-ANISOU 6387  CB AGLU A 850    12317   8098   6758    -79     38   1012       C  
-ATOM   6388  CB BGLU A 850      17.494  19.506 -37.948  0.50 71.73           C  
-ANISOU 6388  CB BGLU A 850    12358   8125   6770    -88     34   1019       C  
-ATOM   6389  CG AGLU A 850      18.991  19.261 -37.723  0.50 63.38           C  
-ANISOU 6389  CG AGLU A 850    11451   6857   5775   -211    229    745       C  
-ATOM   6390  CG BGLU A 850      17.100  20.903 -38.405  0.50 75.69           C  
-ANISOU 6390  CG BGLU A 850    12970   8590   7200     79     -2   1234       C  
-ATOM   6391  CD AGLU A 850      19.569  19.814 -36.435  0.50 59.62           C  
-ANISOU 6391  CD AGLU A 850    10954   6200   5497    -11    388    651       C  
-ATOM   6392  CD BGLU A 850      17.688  21.996 -37.538  0.50 72.36           C  
-ANISOU 6392  CD BGLU A 850    12624   7952   6916    299    153   1203       C  
-ATOM   6393  OE1AGLU A 850      19.063  20.843 -35.940  0.50 61.32           O  
-ANISOU 6393  OE1AGLU A 850    11138   6386   5776    235    381    807       O  
-ATOM   6394  OE1BGLU A 850      18.750  21.764 -36.927  0.50 66.26           O  
-ANISOU 6394  OE1BGLU A 850    11905   7018   6251    258    314    984       O  
-ATOM   6395  OE2AGLU A 850      20.533  19.211 -35.915  0.50 57.68           O  
-ANISOU 6395  OE2AGLU A 850    10726   5845   5345   -102    520    421       O  
-ATOM   6396  OE2BGLU A 850      17.083  23.087 -37.466  0.50 76.64           O  
-ANISOU 6396  OE2BGLU A 850    13173   8486   7459    514    113   1401       O  
-ATOM   6397  N   LEU A 851      16.253  16.418 -37.427  1.00102.17           N  
-ANISOU 6397  N   LEU A 851    15766  12393  10661   -359   -180    910       N  
-ATOM   6398  CA  LEU A 851      16.493  15.121 -36.800  1.00103.68           C  
-ANISOU 6398  CA  LEU A 851    15832  12621  10942   -477   -152    724       C  
-ATOM   6399  C   LEU A 851      15.569  14.032 -37.326  1.00109.60           C  
-ANISOU 6399  C   LEU A 851    16446  13616  11580   -639   -326    793       C  
-ATOM   6400  O   LEU A 851      15.323  13.043 -36.644  1.00108.42           O  
-ANISOU 6400  O   LEU A 851    16128  13550  11515   -673   -350    712       O  
-ATOM   6401  CB  LEU A 851      16.316  15.234 -35.284  1.00 98.96           C  
-ANISOU 6401  CB  LEU A 851    15056  11983  10563   -247    -94    701       C  
-ATOM   6402  CG  LEU A 851      16.998  16.422 -34.601  1.00 94.82           C  
-ANISOU 6402  CG  LEU A 851    14630  11237  10162    -40     62    675       C  
-ATOM   6403  CD1 LEU A 851      16.536  16.545 -33.160  1.00 92.46           C  
-ANISOU 6403  CD1 LEU A 851    14125  10944  10063    197     83    700       C  
-ATOM   6404  CD2 LEU A 851      18.512  16.303 -34.682  1.00 91.70           C  
-ANISOU 6404  CD2 LEU A 851    14427  10626   9790   -179    246    426       C  
-ATOM   6405  N   GLU A 852      15.050  14.215 -38.534  1.00118.65           N  
-ANISOU 6405  N   GLU A 852    17667  14880  12534   -742   -449    944       N  
-ATOM   6406  CA  GLU A 852      14.126  13.243 -39.110  1.00127.07           C  
-ANISOU 6406  CA  GLU A 852    18614  16190  13478   -901   -622   1027       C  
-ATOM   6407  C   GLU A 852      14.859  12.024 -39.664  1.00129.02           C  
-ANISOU 6407  C   GLU A 852    18943  16426  13651  -1204   -585    814       C  
-ATOM   6408  O   GLU A 852      14.285  11.231 -40.411  1.00130.08           O  
-ANISOU 6408  O   GLU A 852    19039  16740  13646  -1389   -714    863       O  
-ATOM   6409  CB  GLU A 852      13.284  13.879 -40.219  1.00133.07           C  
-ANISOU 6409  CB  GLU A 852    19420  17087  14053   -904   -770   1273       C  
-ATOM   6410  CG  GLU A 852      14.100  14.386 -41.400  1.00140.00           C  
-ANISOU 6410  CG  GLU A 852    20565  17843  14785  -1051   -714   1236       C  
-ATOM   6411  CD  GLU A 852      13.462  14.060 -42.739  1.00145.41           C  
-ANISOU 6411  CD  GLU A 852    21289  18714  15246  -1249   -872   1368       C  
-ATOM   6412  OE1 GLU A 852      13.568  14.886 -43.671  1.00148.30           O  
-ANISOU 6412  OE1 GLU A 852    21822  19041  15484  -1267   -889   1470       O  
-ATOM   6413  OE2 GLU A 852      12.863  12.970 -42.862  1.00147.01           O  
-ANISOU 6413  OE2 GLU A 852    21360  19101  15398  -1390   -981   1368       O  
-ATOM   6414  N   GLU A 853      16.123  11.875 -39.286  1.00163.08           N  
-ANISOU 6414  N   GLU A 853    23371  20533  18060  -1254   -407    579       N  
-ATOM   6415  CA  GLU A 853      16.973  10.824 -39.839  1.00164.38           C  
-ANISOU 6415  CA  GLU A 853    23643  20657  18157  -1534   -348    363       C  
-ATOM   6416  C   GLU A 853      16.782   9.479 -39.137  1.00162.31           C  
-ANISOU 6416  C   GLU A 853    23206  20484  17979  -1616   -370    240       C  
-ATOM   6417  O   GLU A 853      16.999   8.426 -39.733  1.00163.20           O  
-ANISOU 6417  O   GLU A 853    23357  20653  17998  -1861   -393    128       O  
-ATOM   6418  CB  GLU A 853      18.445  11.259 -39.800  1.00168.48           C  
-ANISOU 6418  CB  GLU A 853    24367  20917  18729  -1559   -147    164       C  
-ATOM   6419  CG  GLU A 853      19.404  10.230 -39.223  1.00173.15           C  
-ANISOU 6419  CG  GLU A 853    24955  21408  19427  -1679    -19   -108       C  
-ATOM   6420  CD  GLU A 853      19.571   9.014 -40.115  1.00177.64           C  
-ANISOU 6420  CD  GLU A 853    25576  22063  19858  -1979    -64   -218       C  
-ATOM   6421  OE1 GLU A 853      19.389   9.140 -41.345  1.00181.50           O  
-ANISOU 6421  OE1 GLU A 853    26185  22620  20158  -2124   -142   -133       O  
-ATOM   6422  OE2 GLU A 853      19.869   7.925 -39.580  1.00178.08           O  
-ANISOU 6422  OE2 GLU A 853    25551  22119  19992  -2069    -25   -386       O  
-ATOM   6423  N   PHE A 854      16.356   9.526 -37.879  1.00117.71           N  
-ANISOU 6423  N   PHE A 854    17369  14851  12504  -1410   -365    266       N  
-ATOM   6424  CA  PHE A 854      16.248   8.329 -37.042  1.00115.31           C  
-ANISOU 6424  CA  PHE A 854    16897  14608  12307  -1461   -369    139       C  
-ATOM   6425  C   PHE A 854      15.677   7.092 -37.743  1.00119.49           C  
-ANISOU 6425  C   PHE A 854    17372  15334  12696  -1702   -504    141       C  
-ATOM   6426  O   PHE A 854      14.460   6.932 -37.877  1.00121.91           O  
-ANISOU 6426  O   PHE A 854    17531  15855  12936  -1678   -672    327       O  
-ATOM   6427  CB  PHE A 854      15.489   8.643 -35.747  1.00104.13           C  
-ANISOU 6427  CB  PHE A 854    15260  13245  11061  -1198   -399    240       C  
-ATOM   6428  CG  PHE A 854      16.339   9.320 -34.709  1.00 91.22           C  
-ANISOU 6428  CG  PHE A 854    13654  11391   9615  -1013   -224    128       C  
-ATOM   6429  CD1 PHE A 854      16.603  10.679 -34.788  1.00 85.96           C  
-ANISOU 6429  CD1 PHE A 854    13105  10596   8960   -847   -158    215       C  
-ATOM   6430  CD2 PHE A 854      16.897   8.593 -33.669  1.00 83.24           C  
-ANISOU 6430  CD2 PHE A 854    12560  10300   8766  -1012   -124    -66       C  
-ATOM   6431  CE1 PHE A 854      17.396  11.302 -33.844  1.00 79.44           C  
-ANISOU 6431  CE1 PHE A 854    12313   9570   8302   -686      5    111       C  
-ATOM   6432  CE2 PHE A 854      17.693   9.210 -32.722  1.00 76.18           C  
-ANISOU 6432  CE2 PHE A 854    11694   9208   8042   -851     38   -169       C  
-ATOM   6433  CZ  PHE A 854      17.942  10.567 -32.809  1.00 75.57           C  
-ANISOU 6433  CZ  PHE A 854    11734   9007   7972   -689    104    -81       C  
-ATOM   6434  N   GLN A 855      16.587   6.218 -38.172  1.00140.21           N  
-ANISOU 6434  N   GLN A 855    20116  17880  15276  -1934   -425    -71       N  
-ATOM   6435  CA  GLN A 855      16.248   5.006 -38.913  0.50143.89           C  
-ANISOU 6435  CA  GLN A 855    20569  18500  15602  -2193   -528   -104       C  
-ATOM   6436  C   GLN A 855      15.328   5.315 -40.088  1.00145.73           C  
-ANISOU 6436  C   GLN A 855    20831  18912  15628  -2268   -692    117       C  
-ATOM   6437  O   GLN A 855      14.387   4.572 -40.369  1.00145.80           O  
-ANISOU 6437  O   GLN A 855    20722  19131  15546  -2370   -843    210       O  
-ATOM   6438  CB  GLN A 855      15.604   3.967 -37.996  0.50149.06           C  
-ANISOU 6438  CB  GLN A 855    21001  19283  16353  -2183   -595   -132       C  
-ATOM   6439  CG  GLN A 855      15.527   2.577 -38.602  0.50158.42           C  
-ANISOU 6439  CG  GLN A 855    22191  20580  17420  -2465   -659   -228       C  
-ATOM   6440  CD  GLN A 855      14.477   1.719 -37.937  0.50164.58           C  
-ANISOU 6440  CD  GLN A 855    22737  21555  18240  -2451   -787   -165       C  
-ATOM   6441  OE1 GLN A 855      14.764   0.995 -36.987  0.50166.67           O  
-ANISOU 6441  OE1 GLN A 855    22908  21773  18645  -2437   -726   -313       O  
-ATOM   6442  NE2 GLN A 855      13.248   1.802 -38.428  0.50170.91           N  
-ANISOU 6442  NE2 GLN A 855    23442  22580  18917  -2454   -967     58       N  
-ATOM   6443  N   TYR A 856      15.613   6.419 -40.769  1.00133.46           N  
-ANISOU 6443  N   TYR A 856    19435  17273  14000  -2219   -663    201       N  
-ATOM   6444  CA  TYR A 856      14.813   6.868 -41.901  1.00135.39           C  
-ANISOU 6444  CA  TYR A 856    19723  17668  14051  -2274   -809    418       C  
-ATOM   6445  C   TYR A 856      14.531   5.735 -42.884  1.00135.35           C  
-ANISOU 6445  C   TYR A 856    19741  17817  13867  -2569   -912    392       C  
-ATOM   6446  O   TYR A 856      15.447   5.178 -43.486  1.00135.62           O  
-ANISOU 6446  O   TYR A 856    19937  17757  13837  -2784   -828    210       O  
-ATOM   6447  CB  TYR A 856      15.504   8.018 -42.605  1.00137.00           C  
-ANISOU 6447  CB  TYR A 856    20146  17717  14191  -2245   -728    441       C  
-ATOM   6448  N   LYS A 872       9.270   8.692 -48.300  1.00164.37           N  
-ANISOU 6448  N   LYS A 872    23439  22458  16555  -2656  -1802   1791       N  
-ATOM   6449  CA  LYS A 872       8.862   7.726 -49.313  1.00167.99           C  
-ANISOU 6449  CA  LYS A 872    23910  23100  16818  -2948  -1920   1808       C  
-ATOM   6450  C   LYS A 872      10.037   6.863 -49.764  1.00165.60           C  
-ANISOU 6450  C   LYS A 872    23784  22659  16477  -3217  -1798   1537       C  
-ATOM   6451  O   LYS A 872      10.217   5.746 -49.280  1.00163.77           O  
-ANISOU 6451  O   LYS A 872    23481  22442  16304  -3326  -1768   1374       O  
-ATOM   6452  CB  LYS A 872       8.230   8.435 -50.504  1.00168.28           C  
-ANISOU 6452  CB  LYS A 872    24019  23262  16658  -2988  -2049   2042       C  
-ATOM   6453  N   CYS A 873      10.835   7.388 -50.690  1.00215.59           N  
-ANISOU 6453  N   CYS A 873    30347  28858  22710  -3323  -1728   1491       N  
-ATOM   6454  CA  CYS A 873      11.971   6.647 -51.232  1.00214.22           C  
-ANISOU 6454  CA  CYS A 873    30355  28553  22484  -3582  -1611   1242       C  
-ATOM   6455  C   CYS A 873      13.201   6.732 -50.332  1.00210.96           C  
-ANISOU 6455  C   CYS A 873    30010  27881  22265  -3488  -1406   1002       C  
-ATOM   6456  O   CYS A 873      13.646   7.823 -49.972  1.00210.40           O  
-ANISOU 6456  O   CYS A 873    30005  27652  22287  -3289  -1315   1021       O  
-ATOM   6457  CB  CYS A 873      12.303   7.134 -52.633  1.00213.81           C  
-ANISOU 6457  CB  CYS A 873    30522  28478  22237  -3750  -1625   1290       C  
-ATOM   6458  N   TYR A 874      13.744   5.572 -49.978  1.00186.70           N  
-ANISOU 6458  N   TYR A 874    26924  24768  19247  -3634  -1333    779       N  
-ATOM   6459  CA  TYR A 874      14.924   5.500 -49.125  1.00180.90           C  
-ANISOU 6459  CA  TYR A 874    26243  23799  18691  -3567  -1139    539       C  
-ATOM   6460  C   TYR A 874      16.157   5.052 -49.908  1.00177.18           C  
-ANISOU 6460  C   TYR A 874    25999  23183  18140  -3814  -1015    314       C  
-ATOM   6461  O   TYR A 874      17.267   5.510 -49.644  1.00177.32           O  
-ANISOU 6461  O   TYR A 874    26144  22982  18249  -3759   -850    162       O  
-ATOM   6462  CB  TYR A 874      14.672   4.573 -47.944  1.00183.02           C  
-ANISOU 6462  CB  TYR A 874    26313  24111  19115  -3509  -1134    445       C  
-ATOM   6463  N   LEU A 875      15.959   4.155 -50.870  1.00163.57           N  
-ANISOU 6463  N   LEU A 875    24324  21583  16243  -4088  -1093    293       N  
-ATOM   6464  CA  LEU A 875      17.053   3.714 -51.729  1.00155.86           C  
-ANISOU 6464  CA  LEU A 875    23564  20486  15168  -4338   -988     93       C  
-ATOM   6465  C   LEU A 875      17.676   4.918 -52.429  1.00151.33           C  
-ANISOU 6465  C   LEU A 875    23190  19778  14529  -4306   -922    131       C  
-ATOM   6466  O   LEU A 875      18.865   4.919 -52.749  1.00151.85           O  
-ANISOU 6466  O   LEU A 875    23438  19667  14590  -4412   -776    -60       O  
-ATOM   6467  CB  LEU A 875      16.557   2.697 -52.748  1.00159.36           C  
-ANISOU 6467  CB  LEU A 875    24026  21109  15413  -4629  -1106    111       C  
-ATOM   6468  N   GLU A 876      16.860   5.942 -52.660  1.00132.25           N  
-ANISOU 6468  N   GLU A 876    20738  17449  12063  -4158  -1031    382       N  
-ATOM   6469  CA  GLU A 876      17.334   7.185 -53.254  1.00126.32           C  
-ANISOU 6469  CA  GLU A 876    20164  16576  11255  -4098   -981    447       C  
-ATOM   6470  C   GLU A 876      17.731   8.183 -52.174  1.00118.81           C  
-ANISOU 6470  C   GLU A 876    19188  15453  10500  -3801   -869    440       C  
-ATOM   6471  O   GLU A 876      18.493   9.114 -52.428  1.00117.84           O  
-ANISOU 6471  O   GLU A 876    19233  15165  10375  -3751   -768    412       O  
-ATOM   6472  CB  GLU A 876      16.271   7.789 -54.174  1.00127.03           C  
-ANISOU 6472  CB  GLU A 876    20249  16846  11172  -4106  -1159    726       C  
-ATOM   6473  CG  GLU A 876      16.088   7.035 -55.481  1.00126.72           C  
-ANISOU 6473  CG  GLU A 876    20298  16942  10909  -4422  -1249    730       C  
-ATOM   6474  CD  GLU A 876      17.330   7.066 -56.357  1.00124.91           C  
-ANISOU 6474  CD  GLU A 876    20325  16547  10588  -4626  -1121    548       C  
-ATOM   6475  OE1 GLU A 876      17.483   8.029 -57.139  1.00125.32           O  
-ANISOU 6475  OE1 GLU A 876    20525  16555  10537  -4625  -1129    649       O  
-ATOM   6476  OE2 GLU A 876      18.151   6.127 -56.265  1.00121.68           O  
-ANISOU 6476  OE2 GLU A 876    19970  16053  10209  -4785  -1014    306       O  
-ATOM   6477  N   ARG A 877      17.206   7.990 -50.970  1.00119.12           N  
-ANISOU 6477  N   ARG A 877    19019  15535  10706  -3610   -886    466       N  
-ATOM   6478  CA  ARG A 877      17.635   8.794 -49.836  1.00110.18           C  
-ANISOU 6478  CA  ARG A 877    17853  14235   9774  -3339   -767    432       C  
-ATOM   6479  C   ARG A 877      19.120   8.552 -49.593  1.00104.60           C  
-ANISOU 6479  C   ARG A 877    17292  13299   9151  -3417   -563    148       C  
-ATOM   6480  O   ARG A 877      19.900   9.493 -49.470  1.00102.53           O  
-ANISOU 6480  O   ARG A 877    17160  12855   8942  -3311   -441    105       O  
-ATOM   6481  CB  ARG A 877      16.830   8.454 -48.578  1.00109.79           C  
-ANISOU 6481  CB  ARG A 877    17548  14281   9887  -3149   -820    488       C  
-ATOM   6482  CG  ARG A 877      17.145   9.355 -47.386  1.00108.37           C  
-ANISOU 6482  CG  ARG A 877    17320  13943   9911  -2855   -710    479       C  
-ATOM   6483  CD  ARG A 877      16.464   8.881 -46.110  1.00109.92           C  
-ANISOU 6483  CD  ARG A 877    17267  14224  10274  -2691   -748    499       C  
-ATOM   6484  NE  ARG A 877      16.349   9.953 -45.121  1.00111.69           N  
-ANISOU 6484  NE  ARG A 877    17422  14357  10659  -2382   -698    584       N  
-ATOM   6485  CZ  ARG A 877      17.215  10.171 -44.134  1.00110.66           C  
-ANISOU 6485  CZ  ARG A 877    17304  14033  10708  -2256   -534    424       C  
-ATOM   6486  NH1 ARG A 877      17.016  11.174 -43.287  1.00110.58           N  
-ANISOU 6486  NH1 ARG A 877    17232  13954  10831  -1978   -501    521       N  
-ATOM   6487  NH2 ARG A 877      18.273   9.385 -43.985  1.00108.65           N  
-ANISOU 6487  NH2 ARG A 877    17124  13656  10501  -2407   -404    168       N  
-ATOM   6488  N   GLU A 878      19.508   7.283 -49.528  1.00 92.24           N  
-ANISOU 6488  N   GLU A 878    15707  11745   7594  -3603   -525    -45       N  
-ATOM   6489  CA  GLU A 878      20.906   6.925 -49.329  1.00 89.23           C  
-ANISOU 6489  CA  GLU A 878    15456  11161   7285  -3694   -335   -322       C  
-ATOM   6490  C   GLU A 878      21.716   7.328 -50.551  1.00 90.11           C  
-ANISOU 6490  C   GLU A 878    15819  11180   7238  -3871   -276   -377       C  
-ATOM   6491  O   GLU A 878      22.895   7.670 -50.447  1.00 88.73           O  
-ANISOU 6491  O   GLU A 878    15788  10807   7118  -3871   -111   -545       O  
-ATOM   6492  CB  GLU A 878      21.042   5.432 -49.068  1.00 88.18           C  
-ANISOU 6492  CB  GLU A 878    15245  11079   7181  -3862   -324   -499       C  
-ATOM   6493  N   GLN A 879      21.066   7.285 -51.711  1.00104.78           N  
-ANISOU 6493  N   GLN A 879    17727  13189   8896  -4026   -414   -234       N  
-ATOM   6494  CA  GLN A 879      21.686   7.673 -52.971  1.00107.27           C  
-ANISOU 6494  CA  GLN A 879    18274  13443   9039  -4207   -383   -259       C  
-ATOM   6495  C   GLN A 879      22.024   9.164 -52.963  1.00106.54           C  
-ANISOU 6495  C   GLN A 879    18295  13215   8972  -4023   -323   -168       C  
-ATOM   6496  O   GLN A 879      23.184   9.547 -53.097  1.00104.29           O  
-ANISOU 6496  O   GLN A 879    18182  12742   8701  -4058   -170   -323       O  
-ATOM   6497  CB  GLN A 879      20.745   7.345 -54.134  1.00113.32           C  
-ANISOU 6497  CB  GLN A 879    19043  14422   9591  -4391   -562    -92       C  
-ATOM   6498  CG  GLN A 879      21.415   7.238 -55.497  1.00120.61           C  
-ANISOU 6498  CG  GLN A 879    20194  15310  10322  -4663   -533   -173       C  
-ATOM   6499  CD  GLN A 879      22.225   5.963 -55.659  1.00124.10           C  
-ANISOU 6499  CD  GLN A 879    20694  15706  10751  -4901   -440   -435       C  
-ATOM   6500  OE1 GLN A 879      22.461   5.235 -54.693  1.00126.30           O  
-ANISOU 6500  OE1 GLN A 879    20863  15945  11181  -4851   -373   -579       O  
-ATOM   6501  NE2 GLN A 879      22.652   5.687 -56.886  1.00127.29           N  
-ANISOU 6501  NE2 GLN A 879    21275  16115  10973  -5162   -436   -498       N  
-ATOM   6502  N   GLY A 880      21.003   9.997 -52.789  1.00 98.80           N  
-ANISOU 6502  N   GLY A 880    17216  12330   7995  -3826   -442     83       N  
-ATOM   6503  CA  GLY A 880      21.179  11.438 -52.745  1.00101.10           C  
-ANISOU 6503  CA  GLY A 880    17601  12502   8309  -3634   -400    195       C  
-ATOM   6504  C   GLY A 880      22.158  11.910 -51.685  1.00 98.98           C  
-ANISOU 6504  C   GLY A 880    17362  12013   8234  -3461   -215     38       C  
-ATOM   6505  O   GLY A 880      22.678  13.021 -51.758  1.00 97.98           O  
-ANISOU 6505  O   GLY A 880    17372  11742   8114  -3357   -136     62       O  
-ATOM   6506  N   GLU A 881      22.406  11.068 -50.688  1.00121.02           N  
-ANISOU 6506  N   GLU A 881    20025  14778  11180  -3432   -146   -121       N  
-ATOM   6507  CA  GLU A 881      23.380  11.390 -49.653  1.00119.52           C  
-ANISOU 6507  CA  GLU A 881    19854  14382  11175  -3288     35   -288       C  
-ATOM   6508  C   GLU A 881      24.796  11.243 -50.199  1.00117.39           C  
-ANISOU 6508  C   GLU A 881    19802  13945  10855  -3476    194   -521       C  
-ATOM   6509  O   GLU A 881      25.680  12.036 -49.877  1.00115.81           O  
-ANISOU 6509  O   GLU A 881    19715  13561  10727  -3379    336   -601       O  
-ATOM   6510  CB  GLU A 881      23.175  10.508 -48.419  1.00121.81           C  
-ANISOU 6510  CB  GLU A 881    19933  14704  11644  -3202     53   -380       C  
-ATOM   6511  CG  GLU A 881      21.913  10.840 -47.638  1.00127.38           C  
-ANISOU 6511  CG  GLU A 881    20422  15540  12438  -2965    -72   -165       C  
-ATOM   6512  CD  GLU A 881      21.588   9.806 -46.578  1.00130.19           C  
-ANISOU 6512  CD  GLU A 881    20565  15963  12939  -2924    -82   -247       C  
-ATOM   6513  OE1 GLU A 881      22.322   8.801 -46.485  1.00131.03           O  
-ANISOU 6513  OE1 GLU A 881    20693  16018  13073  -3085      3   -468       O  
-ATOM   6514  OE2 GLU A 881      20.597   9.995 -45.841  1.00133.99           O  
-ANISOU 6514  OE2 GLU A 881    20856  16549  13506  -2731   -175    -90       O  
-ATOM   6515  N   LYS A 882      25.003  10.226 -51.031  1.00113.87           N  
-ANISOU 6515  N   LYS A 882    19414  13567  10284  -3747    171   -629       N  
-ATOM   6516  CA  LYS A 882      26.276  10.057 -51.720  1.00110.51           C  
-ANISOU 6516  CA  LYS A 882    19201  13005   9783  -3949    307   -837       C  
-ATOM   6517  C   LYS A 882      26.507  11.244 -52.649  1.00109.84           C  
-ANISOU 6517  C   LYS A 882    19314  12859   9563  -3960    308   -731       C  
-ATOM   6518  O   LYS A 882      27.618  11.764 -52.747  1.00110.21           O  
-ANISOU 6518  O   LYS A 882    19527  12729   9619  -3978    456   -864       O  
-ATOM   6519  CB  LYS A 882      26.291   8.751 -52.499  1.00111.22           C  
-ANISOU 6519  CB  LYS A 882    19309  13201   9750  -4235    262   -944       C  
-ATOM   6520  N   ILE A 883      25.445  11.668 -53.326  1.00100.36           N  
-ANISOU 6520  N   ILE A 883    22034   8407   7693   -827   1703   1691       N  
-ATOM   6521  CA  ILE A 883      25.481  12.862 -54.162  1.00 94.65           C  
-ANISOU 6521  CA  ILE A 883    20354   8087   7523   -974   1814   1849       C  
-ATOM   6522  C   ILE A 883      25.999  14.057 -53.370  1.00 89.32           C  
-ANISOU 6522  C   ILE A 883    18604   7764   7571   -712   1792   1783       C  
-ATOM   6523  O   ILE A 883      26.875  14.789 -53.828  1.00 88.14           O  
-ANISOU 6523  O   ILE A 883    17774   7891   7824   -330   1910   1782       O  
-ATOM   6524  CB  ILE A 883      24.076  13.216 -54.684  1.00 91.21           C  
-ANISOU 6524  CB  ILE A 883    19813   7740   7102  -1840   1783   2083       C  
-ATOM   6525  CG1 ILE A 883      23.547  12.115 -55.604  1.00 93.58           C  
-ANISOU 6525  CG1 ILE A 883    21128   7730   6700  -2156   1815   2171       C  
-ATOM   6526  CG2 ILE A 883      24.095  14.551 -55.400  1.00 90.37           C  
-ANISOU 6526  CG2 ILE A 883    18645   8068   7624  -1981   1890   2242       C  
-ATOM   6527  CD1 ILE A 883      22.116  12.332 -56.049  1.00 89.41           C  
-ANISOU 6527  CD1 ILE A 883    20586   7280   6105  -3031   1769   2401       C  
-ATOM   6528  N   ILE A 884      25.447  14.249 -52.175  1.00 91.96           N  
-ANISOU 6528  N   ILE A 884    18800   8085   8057   -931   1641   1729       N  
-ATOM   6529  CA  ILE A 884      25.810  15.383 -51.335  1.00 85.88           C  
-ANISOU 6529  CA  ILE A 884    17045   7627   7957   -755   1607   1669       C  
-ATOM   6530  C   ILE A 884      27.209  15.217 -50.764  1.00 88.61           C  
-ANISOU 6530  C   ILE A 884    17321   7975   8370     62   1629   1450       C  
-ATOM   6531  O   ILE A 884      27.939  16.190 -50.595  1.00 86.39           O  
-ANISOU 6531  O   ILE A 884    16173   8015   8638    370   1679   1414       O  
-ATOM   6532  CB  ILE A 884      24.808  15.585 -50.188  1.00 80.55           C  
-ANISOU 6532  CB  ILE A 884    16289   6923   7395  -1216   1438   1671       C  
-ATOM   6533  CG1 ILE A 884      23.427  15.917 -50.750  1.00 75.60           C  
-ANISOU 6533  CG1 ILE A 884    15579   6377   6768  -2027   1423   1911       C  
-ATOM   6534  CG2 ILE A 884      25.275  16.695 -49.261  1.00 76.10           C  
-ANISOU 6534  CG2 ILE A 884    14771   6651   7492   -981   1405   1589       C  
-ATOM   6535  CD1 ILE A 884      22.410  16.279 -49.692  1.00 70.36           C  
-ANISOU 6535  CD1 ILE A 884    14704   5751   6277  -2499   1271   1943       C  
-ATOM   6536  N   GLN A 885      27.579  13.979 -50.466  1.00 84.57           N  
-ANISOU 6536  N   GLN A 885    17734   7112   7285    408   1593   1308       N  
-ATOM   6537  CA  GLN A 885      28.925  13.691 -49.997  1.00 90.71           C  
-ANISOU 6537  CA  GLN A 885    18537   7884   8044   1217   1623   1110       C  
-ATOM   6538  C   GLN A 885      29.927  14.074 -51.077  1.00 94.06           C  
-ANISOU 6538  C   GLN A 885    18556   8544   8638   1642   1803   1150       C  
-ATOM   6539  O   GLN A 885      30.872  14.823 -50.823  1.00 94.37           O  
-ANISOU 6539  O   GLN A 885    17844   8885   9128   2087   1848   1078       O  
-ATOM   6540  CB  GLN A 885      29.065  12.210 -49.636  1.00 94.81           C  
-ANISOU 6540  CB  GLN A 885    20223   7955   7845   1489   1571    974       C  
-ATOM   6541  CG  GLN A 885      30.469  11.802 -49.216  1.00 99.72           C  
-ANISOU 6541  CG  GLN A 885    20951   8563   8374   2363   1613    781       C  
-ATOM   6542  CD  GLN A 885      30.981  12.587 -48.020  1.00 97.79           C  
-ANISOU 6542  CD  GLN A 885    19927   8573   8655   2640   1530    655       C  
-ATOM   6543  OE1 GLN A 885      30.212  13.232 -47.301  1.00 95.54           O  
-ANISOU 6543  OE1 GLN A 885    19206   8382   8712   2185   1417    684       O  
-ATOM   6544  NE2 GLN A 885      32.290  12.534 -47.800  1.00 98.30           N  
-ANISOU 6544  NE2 GLN A 885    19814   8761   8774   3393   1590    520       N  
-ATOM   6545  N   GLU A 886      29.702  13.563 -52.284  1.00101.51           N  
-ANISOU 6545  N   GLU A 886    20001   9355   9212   1484   1906   1267       N  
-ATOM   6546  CA  GLU A 886      30.545  13.883 -53.429  1.00104.83           C  
-ANISOU 6546  CA  GLU A 886    20092   9984   9755   1827   2083   1327       C  
-ATOM   6547  C   GLU A 886      30.679  15.392 -53.598  1.00 97.08           C  
-ANISOU 6547  C   GLU A 886    17886   9469   9530   1705   2132   1416       C  
-ATOM   6548  O   GLU A 886      31.787  15.921 -53.665  1.00 96.83           O  
-ANISOU 6548  O   GLU A 886    17269   9704   9817   2233   2215   1352       O  
-ATOM   6549  CB  GLU A 886      29.966  13.272 -54.706  1.00116.15           C  
-ANISOU 6549  CB  GLU A 886    22171  11223  10739   1474   2169   1478       C  
-ATOM   6550  CG  GLU A 886      30.823  13.500 -55.942  1.00131.91           C  
-ANISOU 6550  CG  GLU A 886    23913  13402  12803   1832   2356   1541       C  
-ATOM   6551  CD  GLU A 886      32.149  12.768 -55.871  1.00143.70           C  
-ANISOU 6551  CD  GLU A 886    25804  14798  13998   2681   2429   1376       C  
-ATOM   6552  OE1 GLU A 886      32.222  11.740 -55.166  1.00151.21           O  
-ANISOU 6552  OE1 GLU A 886    27562  15414  14476   2914   2353   1241       O  
-ATOM   6553  OE2 GLU A 886      33.117  13.220 -56.518  1.00149.18           O  
-ANISOU 6553  OE2 GLU A 886    26003  15756  14922   3122   2564   1385       O  
-ATOM   6554  N   PHE A 887      29.543  16.078 -53.667  1.00 92.62           N  
-ANISOU 6554  N   PHE A 887    16948   9008   9236   1005   2084   1570       N  
-ATOM   6555  CA  PHE A 887      29.524  17.532 -53.796  1.00 83.72           C  
-ANISOU 6555  CA  PHE A 887    14695   8299   8817    822   2129   1669       C  
-ATOM   6556  C   PHE A 887      30.424  18.201 -52.763  1.00 82.68           C  
-ANISOU 6556  C   PHE A 887    13879   8392   9142   1291   2090   1510       C  
-ATOM   6557  O   PHE A 887      31.194  19.102 -53.092  1.00 82.20           O  
-ANISOU 6557  O   PHE A 887    13033   8666   9535   1554   2188   1521       O  
-ATOM   6558  CB  PHE A 887      28.090  18.053 -53.668  1.00 73.41           C  
-ANISOU 6558  CB  PHE A 887    13181   7028   7684     24   2048   1832       C  
-ATOM   6559  CG  PHE A 887      27.996  19.524 -53.364  1.00 62.61           C  
-ANISOU 6559  CG  PHE A 887    10700   6044   7046   -148   2056   1896       C  
-ATOM   6560  CD1 PHE A 887      27.932  20.453 -54.388  1.00 60.09           C  
-ANISOU 6560  CD1 PHE A 887     9729   6013   7091   -349   2185   2066       C  
-ATOM   6561  CD2 PHE A 887      27.949  19.976 -52.053  1.00 59.75           C  
-ANISOU 6561  CD2 PHE A 887     9965   5742   6994   -120   1936   1789       C  
-ATOM   6562  CE1 PHE A 887      27.835  21.807 -54.113  1.00 57.04           C  
-ANISOU 6562  CE1 PHE A 887     8353   5962   7359   -510   2200   2128       C  
-ATOM   6563  CE2 PHE A 887      27.854  21.329 -51.775  1.00 56.70           C  
-ANISOU 6563  CE2 PHE A 887     8591   5690   7261   -282   1951   1849       C  
-ATOM   6564  CZ  PHE A 887      27.798  22.243 -52.808  1.00 55.38           C  
-ANISOU 6564  CZ  PHE A 887     7798   5801   7444   -475   2085   2019       C  
-ATOM   6565  N   LEU A 888      30.328  17.746 -51.517  1.00 79.66           N  
-ANISOU 6565  N   LEU A 888    13813   7828   8626   1385   1947   1364       N  
-ATOM   6566  CA  LEU A 888      31.055  18.357 -50.404  1.00 80.33           C  
-ANISOU 6566  CA  LEU A 888    13283   8111   9127   1764   1888   1212       C  
-ATOM   6567  C   LEU A 888      32.550  18.035 -50.410  1.00 86.25           C  
-ANISOU 6567  C   LEU A 888    14041   8938   9792   2577   1963   1060       C  
-ATOM   6568  O   LEU A 888      33.361  18.829 -49.937  1.00 85.89           O  
-ANISOU 6568  O   LEU A 888    13246   9193  10195   2910   1975    983       O  
-ATOM   6569  CB  LEU A 888      30.424  17.958 -49.066  1.00 74.12           C  
-ANISOU 6569  CB  LEU A 888    12847   7103   8214   1582   1707   1110       C  
-ATOM   6570  CG  LEU A 888      29.161  18.726 -48.670  1.00 66.70           C  
-ANISOU 6570  CG  LEU A 888    11502   6240   7602    873   1620   1235       C  
-ATOM   6571  CD1 LEU A 888      28.379  17.995 -47.588  1.00 63.55           C  
-ANISOU 6571  CD1 LEU A 888    11728   5536   6884    633   1447   1158       C  
-ATOM   6572  CD2 LEU A 888      29.523  20.123 -48.212  1.00 60.90           C  
-ANISOU 6572  CD2 LEU A 888     9669   5887   7584    924   1635   1229       C  
-ATOM   6573  N   SER A 889      32.910  16.871 -50.939  1.00112.40           N  
-ANISOU 6573  N   SER A 889    18205  11987  12515   2894   2015   1022       N  
-ATOM   6574  CA  SER A 889      34.315  16.520 -51.104  1.00119.29           C  
-ANISOU 6574  CA  SER A 889    19119  12946  13259   3679   2107    905       C  
-ATOM   6575  C   SER A 889      34.915  17.311 -52.265  1.00119.73           C  
-ANISOU 6575  C   SER A 889    18509  13345  13639   3796   2274   1017       C  
-ATOM   6576  O   SER A 889      36.073  17.725 -52.215  1.00121.01           O  
-ANISOU 6576  O   SER A 889    18145  13793  14042   4339   2340    943       O  
-ATOM   6577  CB  SER A 889      34.475  15.019 -51.343  1.00127.55           C  
-ANISOU 6577  CB  SER A 889    21326  13588  13551   3981   2123    839       C  
-ATOM   6578  OG  SER A 889      33.804  14.620 -52.524  1.00135.46           O  
-ANISOU 6578  OG  SER A 889    22816  14415  14238   3594   2201    993       O  
-ATOM   6579  N   LYS A 890      34.119  17.509 -53.313  1.00 98.26           N  
-ANISOU 6579  N   LYS A 890    15818  10605  10912   3278   2341   1199       N  
-ATOM   6580  CA  LYS A 890      34.527  18.341 -54.436  1.00 99.59           C  
-ANISOU 6580  CA  LYS A 890    15324  11096  11419   3291   2494   1324       C  
-ATOM   6581  C   LYS A 890      34.939  19.706 -53.912  1.00 97.16           C  
-ANISOU 6581  C   LYS A 890    13894  11202  11819   3327   2487   1306       C  
-ATOM   6582  O   LYS A 890      36.040  20.185 -54.184  1.00 99.58           O  
-ANISOU 6582  O   LYS A 890    13659  11806  12369   3791   2582   1270       O  
-ATOM   6583  CB  LYS A 890      33.374  18.518 -55.429  1.00 99.80           C  
-ANISOU 6583  CB  LYS A 890    15447  11057  11414   2597   2535   1534       C  
-ATOM   6584  CG  LYS A 890      32.982  17.271 -56.204  1.00105.78           C  
-ANISOU 6584  CG  LYS A 890    17263  11442  11486   2511   2571   1582       C  
-ATOM   6585  CD  LYS A 890      33.966  16.969 -57.319  1.00108.03           C  
-ANISOU 6585  CD  LYS A 890    17672  11792  11581   3002   2740   1597       C  
-ATOM   6586  CE  LYS A 890      33.436  15.877 -58.235  1.00108.37           C  
-ANISOU 6586  CE  LYS A 890    18710  11480  10987   2803   2789   1678       C  
-ATOM   6587  NZ  LYS A 890      32.144  16.261 -58.867  1.00107.15           N  
-ANISOU 6587  NZ  LYS A 890    18482  11318  10912   1997   2780   1878       N  
-ATOM   6588  N   VAL A 891      34.040  20.318 -53.147  1.00 83.19           N  
-ANISOU 6588  N   VAL A 891    11796   9449  10362   2827   2374   1335       N  
-ATOM   6589  CA  VAL A 891      34.224  21.681 -52.662  1.00 81.24           C  
-ANISOU 6589  CA  VAL A 891    10505   9567  10795   2743   2366   1339       C  
-ATOM   6590  C   VAL A 891      35.428  21.821 -51.731  1.00 86.85           C  
-ANISOU 6590  C   VAL A 891    10878  10451  11671   3365   2333   1148       C  
-ATOM   6591  O   VAL A 891      36.116  22.841 -51.747  1.00 85.10           O  
-ANISOU 6591  O   VAL A 891     9805  10594  11936   3528   2392   1145       O  
-ATOM   6592  CB  VAL A 891      32.957  22.195 -51.949  1.00 72.78           C  
-ANISOU 6592  CB  VAL A 891     9254   8438   9962   2093   2245   1405       C  
-ATOM   6593  CG1 VAL A 891      33.151  23.629 -51.493  1.00 66.35           C  
-ANISOU 6593  CG1 VAL A 891     7379   7987   9843   2009   2252   1415       C  
-ATOM   6594  CG2 VAL A 891      31.757  22.089 -52.870  1.00 68.05           C  
-ANISOU 6594  CG2 VAL A 891     8946   7711   9198   1466   2278   1608       C  
-ATOM   6595  N   LYS A 892      35.682  20.796 -50.924  1.00111.10           N  
-ANISOU 6595  N   LYS A 892    14619  13268  14325   3706   2239    993       N  
-ATOM   6596  CA  LYS A 892      36.824  20.808 -50.013  1.00118.63           C  
-ANISOU 6596  CA  LYS A 892    15324  14377  15372   4320   2202    811       C  
-ATOM   6597  C   LYS A 892      38.127  20.542 -50.762  1.00128.27           C  
-ANISOU 6597  C   LYS A 892    16518  15776  16444   4971   2340    779       C  
-ATOM   6598  O   LYS A 892      39.215  20.759 -50.230  1.00129.61           O  
-ANISOU 6598  O   LYS A 892    16295  16189  16762   5497   2343    660       O  
-ATOM   6599  CB  LYS A 892      36.629  19.794 -48.881  1.00118.22           C  
-ANISOU 6599  CB  LYS A 892    16010  13992  14917   4465   2055    660       C  
-ATOM   6600  CG  LYS A 892      35.473  20.133 -47.948  1.00112.83           C  
-ANISOU 6600  CG  LYS A 892    15259  13184  14428   3885   1907    670       C  
-ATOM   6601  CD  LYS A 892      35.381  19.169 -46.769  1.00112.20           C  
-ANISOU 6601  CD  LYS A 892    15860  12798  13971   4069   1760    508       C  
-ATOM   6602  CE  LYS A 892      35.160  17.732 -47.226  1.00113.99           C  
-ANISOU 6602  CE  LYS A 892    17216  12618  13478   4169   1769    501       C  
-ATOM   6603  NZ  LYS A 892      34.988  16.786 -46.083  1.00112.95           N  
-ANISOU 6603  NZ  LYS A 892    17785  12165  12966   4306   1625    349       N  
-ATOM   6604  N   GLN A 893      38.002  20.073 -52.001  1.00127.72           N  
-ANISOU 6604  N   GLN A 893    16861  15595  16070   4928   2456    893       N  
-ATOM   6605  CA  GLN A 893      39.155  19.828 -52.864  1.00139.10           C  
-ANISOU 6605  CA  GLN A 893    18292  17203  17356   5507   2603    889       C  
-ATOM   6606  C   GLN A 893      39.259  20.907 -53.938  1.00142.98           C  
-ANISOU 6606  C   GLN A 893    18008  18032  18286   5294   2735   1041       C  
-ATOM   6607  O   GLN A 893      39.561  20.624 -55.097  1.00144.63           O  
-ANISOU 6607  O   GLN A 893    18409  18253  18290   5437   2869   1126       O  
-ATOM   6608  CB  GLN A 893      39.059  18.448 -53.500  1.00144.29           C  
-ANISOU 6608  CB  GLN A 893    20031  17482  17311   5687   2650    896       C  
-ATOM   6609  N   MET A 894      39.001  22.147 -53.539  1.00125.37           N  
-ANISOU 6609  N   MET A 894    14913  16066  16655   4951   2701   1076       N  
-ATOM   6610  CA  MET A 894      39.034  23.274 -54.457  1.00127.63           C  
-ANISOU 6610  CA  MET A 894    14419  16674  17402   4704   2819   1220       C  
-ATOM   6611  C   MET A 894      40.181  24.202 -54.086  1.00136.74           C  
-ANISOU 6611  C   MET A 894    14680  18265  19009   5089   2852   1144       C  
-ATOM   6612  O   MET A 894      40.373  24.519 -52.914  1.00134.52           O  
-ANISOU 6612  O   MET A 894    14105  18064  18941   5172   2745   1026       O  
-ATOM   6613  CB  MET A 894      37.706  24.031 -54.408  1.00119.42           C  
-ANISOU 6613  CB  MET A 894    13098  15586  16689   3933   2769   1351       C  
-ATOM   6614  CG  MET A 894      37.587  25.160 -55.414  1.00107.93           C  
-ANISOU 6614  CG  MET A 894    10907  14422  15678   3623   2895   1518       C  
-ATOM   6615  SD  MET A 894      36.068  26.113 -55.214  1.00 96.20           S  
-ANISOU 6615  SD  MET A 894     9039  12915  14596   2769   2836   1670       S  
-ATOM   6616  CE  MET A 894      34.830  24.835 -55.421  1.00 89.33           C  
-ANISOU 6616  CE  MET A 894     9268  11568  13104   2386   2763   1736       C  
-ATOM   6617  N   PRO A 895      40.955  24.637 -55.088  1.00143.78           N  
-ANISOU 6617  N   PRO A 895    15142  19449  20040   5317   3000   1213       N  
-ATOM   6618  CA  PRO A 895      42.106  25.510 -54.853  1.00149.64           C  
-ANISOU 6618  CA  PRO A 895    15033  20638  21184   5682   3043   1152       C  
-ATOM   6619  C   PRO A 895      41.693  26.973 -54.711  1.00150.19           C  
-ANISOU 6619  C   PRO A 895    14197  20962  21907   5188   3042   1228       C  
-ATOM   6620  O   PRO A 895      42.298  27.836 -55.347  1.00150.98           O  
-ANISOU 6620  O   PRO A 895    13733  21366  22265   5152   3107   1311       O  
-ATOM   6621  CB  PRO A 895      42.934  25.324 -56.123  1.00149.32           C  
-ANISOU 6621  CB  PRO A 895    14981  20770  20982   6051   3208   1221       C  
-ATOM   6622  CG  PRO A 895      41.917  25.060 -57.178  1.00145.46           C  
-ANISOU 6622  CG  PRO A 895    14925  20026  20318   5582   3269   1381       C  
-ATOM   6623  CD  PRO A 895      40.811  24.282 -56.510  1.00145.61           C  
-ANISOU 6623  CD  PRO A 895    15696  19606  20025   5252   3134   1352       C  
-ATOM   6624  N   PHE A 896      40.686  27.251 -53.886  1.00174.57           N  
-ANISOU 6624  N   PHE A 896    17288  23877  25162   4715   2923   1226       N  
-ATOM   6625  CA  PHE A 896      40.220  28.624 -53.704  1.00172.41           C  
-ANISOU 6625  CA  PHE A 896    16357  23752  25398   4138   2872   1324       C  
-ATOM   6626  C   PHE A 896      41.288  29.477 -53.030  1.00173.21           C  
-ANISOU 6626  C   PHE A 896    16095  24066  25650   4187   2739   1265       C  
-ATOM   6627  O   PHE A 896      41.096  30.671 -52.802  1.00170.84           O  
-ANISOU 6627  O   PHE A 896    15471  23787  25654   3697   2642   1335       O  
-ATOM   6628  CB  PHE A 896      38.901  28.674 -52.920  1.00172.21           C  
-ANISOU 6628  CB  PHE A 896    16430  23502  25500   3670   2784   1329       C  
-ATOM   6629  CG  PHE A 896      39.052  28.423 -51.444  1.00172.73           C  
-ANISOU 6629  CG  PHE A 896    16606  23486  25539   3845   2631   1154       C  
-ATOM   6630  CD1 PHE A 896      39.165  29.481 -50.556  1.00175.75           C  
-ANISOU 6630  CD1 PHE A 896    16658  23924  26195   3500   2468   1143       C  
-ATOM   6631  CD2 PHE A 896      39.066  27.133 -50.943  1.00173.66           C  
-ANISOU 6631  CD2 PHE A 896    17512  23316  25156   4151   2554   1036       C  
-ATOM   6632  CE1 PHE A 896      39.297  29.255 -49.198  1.00179.68           C  
-ANISOU 6632  CE1 PHE A 896    17244  24358  26668   3644   2333    983       C  
-ATOM   6633  CE2 PHE A 896      39.198  26.901 -49.587  1.00174.96           C  
-ANISOU 6633  CE2 PHE A 896    17773  23405  25297   4315   2413    876       C  
-ATOM   6634  CZ  PHE A 896      39.314  27.963 -48.714  1.00177.38           C  
-ANISOU 6634  CZ  PHE A 896    17407  23919  26070   4149   2343    835       C  
-ATOM   6635  N   THR A 897      42.418  28.851 -52.719  1.00168.08           N  
-ANISOU 6635  N   THR A 897    15551  23553  24759   4807   2744   1131       N  
-ATOM   6636  CA  THR A 897      43.556  29.557 -52.152  1.00167.79           C  
-ANISOU 6636  CA  THR A 897    15162  23777  24815   4914   2648   1069       C  
-ATOM   6637  C   THR A 897      44.292  30.330 -53.241  1.00167.28           C  
-ANISOU 6637  C   THR A 897    14748  23961  24848   4861   2726   1192       C  
-ATOM   6638  O   THR A 897      45.148  31.164 -52.951  1.00170.98           O  
-ANISOU 6638  O   THR A 897    14867  24649  25447   4832   2660   1172       O  
-ATOM   6639  CB  THR A 897      44.536  28.586 -51.467  1.00171.06           C  
-ANISOU 6639  CB  THR A 897    15813  24282  24901   5616   2626    896       C  
-ATOM   6640  OG1 THR A 897      44.945  27.578 -52.400  1.00170.07           O  
-ANISOU 6640  OG1 THR A 897    16023  24158  24439   6163   2780    904       O  
-ATOM   6641  CG2 THR A 897      43.878  27.920 -50.267  1.00170.25           C  
-ANISOU 6641  CG2 THR A 897    16058  23917  24713   5666   2523    762       C  
-ATOM   6642  N   GLU A 898      43.949  30.053 -54.496  1.00182.79           N  
-ANISOU 6642  N   GLU A 898    20949  25598  22904  -1188    278   1113       N  
-ATOM   6643  CA  GLU A 898      44.620  30.690 -55.625  1.00180.65           C  
-ANISOU 6643  CA  GLU A 898    20523  25290  22824  -1475    292   1437       C  
-ATOM   6644  C   GLU A 898      43.736  30.833 -56.865  1.00174.15           C  
-ANISOU 6644  C   GLU A 898    19943  24444  21781  -1798    406   1487       C  
-ATOM   6645  O   GLU A 898      44.200  30.653 -57.991  1.00173.56           O  
-ANISOU 6645  O   GLU A 898    19888  24395  21663  -2006    725   1743       O  
-ATOM   6646  CB  GLU A 898      45.916  29.945 -55.966  1.00188.30           C  
-ANISOU 6646  CB  GLU A 898    21380  26342  23824  -1417    746   1690       C  
-ATOM   6647  CG  GLU A 898      45.845  28.431 -55.797  1.00193.96           C  
-ANISOU 6647  CG  GLU A 898    22343  27179  24175  -1220   1304   1591       C  
-ATOM   6648  CD  GLU A 898      45.502  27.703 -57.085  1.00198.02           C  
-ANISOU 6648  CD  GLU A 898    23135  27749  24354  -1437   1811   1710       C  
-ATOM   6649  OE1 GLU A 898      46.238  26.760 -57.446  1.00198.57           O  
-ANISOU 6649  OE1 GLU A 898    23237  27908  24304  -1385   2306   1859       O  
-ATOM   6650  OE2 GLU A 898      44.497  28.065 -57.731  1.00199.00           O  
-ANISOU 6650  OE2 GLU A 898    23448  27829  24334  -1658   1718   1652       O  
-ATOM   6651  N   MET A 899      42.466  31.165 -56.652  1.00155.39           N  
-ANISOU 6651  N   MET A 899    17750  22020  19273  -1838    140   1243       N  
-ATOM   6652  CA  MET A 899      41.546  31.426 -57.757  1.00147.88           C  
-ANISOU 6652  CA  MET A 899    17020  21034  18134  -2145    178   1269       C  
-ATOM   6653  C   MET A 899      41.081  32.880 -57.734  1.00145.04           C  
-ANISOU 6653  C   MET A 899    16516  20548  18044  -2315   -435   1240       C  
-ATOM   6654  O   MET A 899      41.289  33.589 -56.750  1.00147.97           O  
-ANISOU 6654  O   MET A 899    16659  20863  18699  -2168   -886   1146       O  
-ATOM   6655  CB  MET A 899      40.335  30.492 -57.689  1.00143.61           C  
-ANISOU 6655  CB  MET A 899    16864  20548  17153  -2078    444   1008       C  
-ATOM   6656  CG  MET A 899      40.668  29.015 -57.819  1.00140.91           C  
-ANISOU 6656  CG  MET A 899    16704  20330  16504  -1934   1076   1030       C  
-ATOM   6657  SD  MET A 899      39.227  27.947 -57.614  1.00136.56           S  
-ANISOU 6657  SD  MET A 899    16596  19841  15450  -1833   1353    700       S  
-ATOM   6658  CE  MET A 899      38.229  28.430 -59.020  1.00139.38           C  
-ANISOU 6658  CE  MET A 899    17175  20146  15638  -2231   1354    769       C  
-ATOM   6659  N   SER A 900      40.455  33.321 -58.820  1.00120.47           N  
-ANISOU 6659  N   SER A 900    13537  17392  14843  -2625   -451   1322       N  
-ATOM   6660  CA  SER A 900      39.892  34.664 -58.875  1.00117.41           C  
-ANISOU 6660  CA  SER A 900    13050  16886  14676  -2804  -1014   1285       C  
-ATOM   6661  C   SER A 900      38.462  34.641 -58.356  1.00111.01           C  
-ANISOU 6661  C   SER A 900    12486  16050  13643  -2745  -1212    946       C  
-ATOM   6662  O   SER A 900      37.761  33.641 -58.496  1.00107.43           O  
-ANISOU 6662  O   SER A 900    12342  15666  12810  -2696   -842    805       O  
-ATOM   6663  CB  SER A 900      39.924  35.209 -60.304  1.00115.74           C  
-ANISOU 6663  CB  SER A 900    12851  16633  14492  -3174   -958   1543       C  
-ATOM   6664  OG  SER A 900      39.030  34.497 -61.142  1.00110.75           O  
-ANISOU 6664  OG  SER A 900    12572  16044  13463  -3315   -587   1492       O  
-ATOM   6665  N   GLU A 901      38.032  35.746 -57.754  1.00139.37           N  
-ANISOU 6665  N   GLU A 901    15939  19543  17471  -2750  -1794    815       N  
-ATOM   6666  CA  GLU A 901      36.680  35.842 -57.219  1.00131.13           C  
-ANISOU 6666  CA  GLU A 901    15107  18467  16251  -2698  -2035    491       C  
-ATOM   6667  C   GLU A 901      35.635  35.431 -58.251  1.00127.29           C  
-ANISOU 6667  C   GLU A 901    14969  17997  15399  -2919  -1757    456       C  
-ATOM   6668  O   GLU A 901      34.596  34.872 -57.906  1.00123.53           O  
-ANISOU 6668  O   GLU A 901    14761  17547  14627  -2826  -1679    192       O  
-ATOM   6669  CB  GLU A 901      36.396  37.256 -56.712  1.00134.99           C  
-ANISOU 6669  CB  GLU A 901    15385  18834  17072  -2751  -2711    413       C  
-ATOM   6670  CG  GLU A 901      34.972  37.469 -56.214  1.00136.54           C  
-ANISOU 6670  CG  GLU A 901    15789  18986  17104  -2722  -2996     86       C  
-ATOM   6671  CD  GLU A 901      34.642  36.652 -54.974  1.00139.12           C  
-ANISOU 6671  CD  GLU A 901    16221  19372  17268  -2380  -2929   -207       C  
-ATOM   6672  OE1 GLU A 901      33.794  37.108 -54.180  1.00142.89           O  
-ANISOU 6672  OE1 GLU A 901    16731  19795  17766  -2291  -3322   -472       O  
-ATOM   6673  OE2 GLU A 901      35.218  35.557 -54.793  1.00142.07           O  
-ANISOU 6673  OE2 GLU A 901    16646  19845  17491  -2200  -2487   -176       O  
-ATOM   6674  N   GLU A 902      35.912  35.711 -59.518  1.00 92.90           N  
-ANISOU 6674  N   GLU A 902    10609  13625  11063  -3214  -1610    722       N  
-ATOM   6675  CA  GLU A 902      35.026  35.282 -60.589  1.00 91.90           C  
-ANISOU 6675  CA  GLU A 902    10805  13519  10592  -3436  -1306    721       C  
-ATOM   6676  C   GLU A 902      35.049  33.763 -60.706  1.00 91.02           C  
-ANISOU 6676  C   GLU A 902    10943  13533  10107  -3298   -680    685       C  
-ATOM   6677  O   GLU A 902      34.007  33.133 -60.862  1.00 89.09           O  
-ANISOU 6677  O   GLU A 902    11016  13322   9512  -3305   -480    499       O  
-ATOM   6678  CB  GLU A 902      35.429  35.924 -61.905  1.00 93.74           C  
-ANISOU 6678  CB  GLU A 902    10956  13709  10952  -3776  -1284   1032       C  
-ATOM   6679  N   ASN A 903      36.241  33.180 -60.627  1.00102.47           N  
-ANISOU 6679  N   ASN A 903    12246  15053  11635  -3171   -374    862       N  
-ATOM   6680  CA  ASN A 903      36.394  31.731 -60.717  1.00 99.24           C  
-ANISOU 6680  CA  ASN A 903    12046  14765  10894  -3029    229    846       C  
-ATOM   6681  C   ASN A 903      35.622  30.987 -59.631  1.00 92.69           C  
-ANISOU 6681  C   ASN A 903    11408  13980   9829  -2743    262    503       C  
-ATOM   6682  O   ASN A 903      34.871  30.054 -59.919  1.00 88.55           O  
-ANISOU 6682  O   ASN A 903    11203  13519   8922  -2736    630    379       O  
-ATOM   6683  CB  ASN A 903      37.873  31.334 -60.682  1.00106.89           C  
-ANISOU 6683  CB  ASN A 903    12786  15793  12036  -2920    492   1088       C  
-ATOM   6684  CG  ASN A 903      38.546  31.463 -62.037  1.00110.88           C  
-ANISOU 6684  CG  ASN A 903    13238  16303  12590  -3204    747   1432       C  
-ATOM   6685  OD1 ASN A 903      38.063  32.175 -62.919  1.00115.63           O  
-ANISOU 6685  OD1 ASN A 903    13886  16839  13208  -3493    595   1517       O  
-ATOM   6686  ND2 ASN A 903      39.668  30.768 -62.209  1.00113.70           N  
-ANISOU 6686  ND2 ASN A 903    13497  16736  12968  -3123   1139   1631       N  
-ATOM   6687  N   ILE A 904      35.812  31.402 -58.382  1.00 98.30           N  
-ANISOU 6687  N   ILE A 904    11922  14657  10769  -2508   -123    351       N  
-ATOM   6688  CA  ILE A 904      35.127  30.770 -57.263  1.00 89.74           C  
-ANISOU 6688  CA  ILE A 904    10994  13610   9494  -2225   -134     22       C  
-ATOM   6689  C   ILE A 904      33.620  30.793 -57.465  1.00 84.95           C  
-ANISOU 6689  C   ILE A 904    10694  12975   8608  -2332   -217   -214       C  
-ATOM   6690  O   ILE A 904      32.981  29.746 -57.527  1.00 83.31           O  
-ANISOU 6690  O   ILE A 904    10786  12841   8026  -2259    162   -360       O  
-ATOM   6691  CB  ILE A 904      35.460  31.452 -55.920  1.00 88.54           C  
-ANISOU 6691  CB  ILE A 904    10567  13405   9669  -1993   -632   -109       C  
-ATOM   6692  CG1 ILE A 904      36.895  31.139 -55.497  1.00 89.07           C  
-ANISOU 6692  CG1 ILE A 904    10372  13522   9949  -1810   -481     67       C  
-ATOM   6693  CG2 ILE A 904      34.498  31.002 -54.838  1.00 84.87           C  
-ANISOU 6693  CG2 ILE A 904    10286  12956   9003  -1750   -728   -475       C  
-ATOM   6694  CD1 ILE A 904      37.906  32.143 -55.978  1.00 91.58           C  
-ANISOU 6694  CD1 ILE A 904    10362  13777  10656  -1981   -713    364       C  
-ATOM   6695  N   THR A 905      33.062  31.994 -57.571  1.00 98.59           N  
-ANISOU 6695  N   THR A 905    12345  14595  10521  -2506   -716   -251       N  
-ATOM   6696  CA  THR A 905      31.620  32.163 -57.712  1.00 92.87           C  
-ANISOU 6696  CA  THR A 905    11886  13831   9570  -2612   -864   -481       C  
-ATOM   6697  C   THR A 905      31.051  31.233 -58.776  1.00 91.21           C  
-ANISOU 6697  C   THR A 905    12016  13689   8951  -2766   -338   -447       C  
-ATOM   6698  O   THR A 905      29.932  30.735 -58.644  1.00 86.81           O  
-ANISOU 6698  O   THR A 905    11749  13152   8083  -2729   -248   -691       O  
-ATOM   6699  CB  THR A 905      31.248  33.620 -58.064  1.00 94.21           C  
-ANISOU 6699  CB  THR A 905    11919  13875  10002  -2860  -1405   -434       C  
-ATOM   6700  OG1 THR A 905      31.772  34.506 -57.068  1.00 92.37           O  
-ANISOU 6700  OG1 THR A 905    11365  13577  10153  -2718  -1903   -467       O  
-ATOM   6701  CG2 THR A 905      29.737  33.786 -58.136  1.00 88.94           C  
-ANISOU 6701  CG2 THR A 905    11525  13166   9101  -2953  -1571   -690       C  
-ATOM   6702  N   ILE A 906      31.829  30.997 -59.826  1.00 83.70           N  
-ANISOU 6702  N   ILE A 906    11029  12774   8001  -2937     10   -145       N  
-ATOM   6703  CA  ILE A 906      31.373  30.188 -60.950  1.00 83.15           C  
-ANISOU 6703  CA  ILE A 906    11261  12765   7567  -3113    508    -76       C  
-ATOM   6704  C   ILE A 906      31.604  28.699 -60.711  1.00 82.40           C  
-ANISOU 6704  C   ILE A 906    11344  12795   7170  -2892   1072   -132       C  
-ATOM   6705  O   ILE A 906      30.712  27.881 -60.936  1.00 80.63           O  
-ANISOU 6705  O   ILE A 906    11442  12622   6570  -2889   1373   -289       O  
-ATOM   6706  CB  ILE A 906      32.057  30.616 -62.266  1.00 85.28           C  
-ANISOU 6706  CB  ILE A 906    11426  13015   7963  -3418    635    278       C  
-ATOM   6707  CG1 ILE A 906      31.778  32.095 -62.547  1.00 85.98           C  
-ANISOU 6707  CG1 ILE A 906    11353  12977   8339  -3648     79    332       C  
-ATOM   6708  CG2 ILE A 906      31.576  29.751 -63.418  1.00 84.67           C  
-ANISOU 6708  CG2 ILE A 906    11668  13003   7501  -3595   1159    344       C  
-ATOM   6709  CD1 ILE A 906      32.544  32.651 -63.724  1.00 88.25           C  
-ANISOU 6709  CD1 ILE A 906    11489  13234   8807  -3935    137    683       C  
-ATOM   6710  N   LYS A 907      32.804  28.355 -60.255  1.00 88.87           N  
-ANISOU 6710  N   LYS A 907    11949  13663   8154  -2709   1213     -4       N  
-ATOM   6711  CA  LYS A 907      33.136  26.968 -59.961  1.00 86.01           C  
-ANISOU 6711  CA  LYS A 907    11723  13418   7537  -2483   1733    -46       C  
-ATOM   6712  C   LYS A 907      32.118  26.395 -58.984  1.00 81.96           C  
-ANISOU 6712  C   LYS A 907    11433  12932   6776  -2250   1702   -410       C  
-ATOM   6713  O   LYS A 907      31.724  25.233 -59.089  1.00 80.66           O  
-ANISOU 6713  O   LYS A 907    11542  12855   6251  -2164   2154   -510       O  
-ATOM   6714  CB  LYS A 907      34.538  26.870 -59.365  1.00 90.19           C  
-ANISOU 6714  CB  LYS A 907    11949  13979   8339  -2287   1763    105       C  
-ATOM   6715  CG  LYS A 907      35.175  25.501 -59.515  1.00 91.88           C  
-ANISOU 6715  CG  LYS A 907    12270  14316   8325  -2147   2381    189       C  
-ATOM   6716  CD  LYS A 907      35.489  25.188 -60.976  1.00 98.18           C  
-ANISOU 6716  CD  LYS A 907    13162  15149   8993  -2419   2805    470       C  
-ATOM   6717  CE  LYS A 907      36.659  26.021 -61.508  1.00105.27           C  
-ANISOU 6717  CE  LYS A 907    13733  16001  10263  -2578   2662    797       C  
-ATOM   6718  NZ  LYS A 907      36.325  27.459 -61.728  1.00108.57           N  
-ANISOU 6718  NZ  LYS A 907    14003  16297  10953  -2794   2108    830       N  
-ATOM   6719  N   LEU A 908      31.699  27.223 -58.032  1.00 82.38           N  
-ANISOU 6719  N   LEU A 908    14248   7965   9088  -2851    236   -437       N  
-ATOM   6720  CA  LEU A 908      30.679  26.844 -57.062  1.00 79.55           C  
-ANISOU 6720  CA  LEU A 908    13724   7846   8656  -2730    128   -377       C  
-ATOM   6721  C   LEU A 908      29.334  26.609 -57.736  1.00 81.81           C  
-ANISOU 6721  C   LEU A 908    13838   8621   8625  -2780     27    -88       C  
-ATOM   6722  O   LEU A 908      28.707  25.571 -57.542  1.00 80.69           O  
-ANISOU 6722  O   LEU A 908    13578   8752   8327  -2934    -75   -106       O  
-ATOM   6723  CB  LEU A 908      30.524  27.926 -55.990  1.00 77.60           C  
-ANISOU 6723  CB  LEU A 908    13468   7416   8599  -2342    157   -323       C  
-ATOM   6724  CG  LEU A 908      31.628  28.076 -54.943  1.00 73.13           C  
-ANISOU 6724  CG  LEU A 908    13034   6401   8352  -2243    226   -611       C  
-ATOM   6725  CD1 LEU A 908      31.247  29.137 -53.916  1.00 70.60           C  
-ANISOU 6725  CD1 LEU A 908    12681   5969   8176  -1850    238   -512       C  
-ATOM   6726  CD2 LEU A 908      31.890  26.746 -54.261  1.00 70.38           C  
-ANISOU 6726  CD2 LEU A 908    12669   6045   8026  -2449    165   -874       C  
-ATOM   6727  N   LYS A 909      28.895  27.586 -58.524  1.00 70.48           N  
-ANISOU 6727  N   LYS A 909    12392   7292   7097  -2649     56    177       N  
-ATOM   6728  CA  LYS A 909      27.603  27.513 -59.201  1.00 73.94           C  
-ANISOU 6728  CA  LYS A 909    12668   8184   7240  -2668    -37    474       C  
-ATOM   6729  C   LYS A 909      27.511  26.286 -60.109  1.00 73.27           C  
-ANISOU 6729  C   LYS A 909    12557   8349   6933  -3048    -99    435       C  
-ATOM   6730  O   LYS A 909      26.440  25.696 -60.261  1.00 73.58           O  
-ANISOU 6730  O   LYS A 909    12436   8779   6742  -3123   -211    583       O  
-ATOM   6731  CB  LYS A 909      27.353  28.790 -60.009  1.00 78.66           C  
-ANISOU 6731  CB  LYS A 909    13292   8802   7795  -2486     20    740       C  
-ATOM   6732  CG  LYS A 909      25.917  28.986 -60.470  1.00 84.71           C  
-ANISOU 6732  CG  LYS A 909    13879  10014   8293  -2406    -76   1073       C  
-ATOM   6733  CD  LYS A 909      25.775  30.290 -61.242  1.00 91.75           C  
-ANISOU 6733  CD  LYS A 909    14815  10884   9162  -2220    -12   1318       C  
-ATOM   6734  CE  LYS A 909      24.376  30.461 -61.820  1.00 97.58           C  
-ANISOU 6734  CE  LYS A 909    15381  12071   9623  -2162   -108   1651       C  
-ATOM   6735  NZ  LYS A 909      24.305  31.628 -62.754  1.00102.04           N  
-ANISOU 6735  NZ  LYS A 909    16004  12622  10143  -2030    -47   1882       N  
-ATOM   6736  N   GLN A 910      28.636  25.905 -60.708  1.00 75.12           N  
-ANISOU 6736  N   GLN A 910    12949   8355   7239  -3286    -27    235       N  
-ATOM   6737  CA  GLN A 910      28.665  24.768 -61.616  1.00 75.07           C  
-ANISOU 6737  CA  GLN A 910    12940   8550   7033  -3653    -75    183       C  
-ATOM   6738  C   GLN A 910      28.644  23.445 -60.863  1.00 69.71           C  
-ANISOU 6738  C   GLN A 910    12201   7941   6344  -3833   -156    -32       C  
-ATOM   6739  O   GLN A 910      28.193  22.432 -61.394  1.00 68.86           O  
-ANISOU 6739  O   GLN A 910    12022   8124   6019  -4091   -240    -14       O  
-ATOM   6740  CB  GLN A 910      29.876  24.839 -62.549  1.00 80.70           C  
-ANISOU 6740  CB  GLN A 910    13845   8995   7824  -3843     36     49       C  
-ATOM   6741  CG  GLN A 910      29.759  25.904 -63.629  1.00 91.31           C  
-ANISOU 6741  CG  GLN A 910    15236  10366   9091  -3753     98    291       C  
-ATOM   6742  CD  GLN A 910      30.977  25.964 -64.531  1.00 96.21           C  
-ANISOU 6742  CD  GLN A 910    16049  10714   9793  -3943    213    153       C  
-ATOM   6743  OE1 GLN A 910      31.952  25.236 -64.332  1.00 97.51           O  
-ANISOU 6743  OE1 GLN A 910    16314  10652  10085  -4135    251   -131       O  
-ATOM   6744  NE2 GLN A 910      30.925  26.835 -65.534  1.00100.59           N  
-ANISOU 6744  NE2 GLN A 910    16656  11288  10275  -3888    271    354       N  
-ATOM   6745  N   LEU A 911      29.131  23.455 -59.626  1.00 75.67           N  
-ANISOU 6745  N   LEU A 911    12990   8427   7333  -3696   -132   -236       N  
-ATOM   6746  CA  LEU A 911      29.062  22.270 -58.771  1.00 69.83           C  
-ANISOU 6746  CA  LEU A 911    12191   7745   6598  -3829   -211   -436       C  
-ATOM   6747  C   LEU A 911      27.652  22.064 -58.218  1.00 67.92           C  
-ANISOU 6747  C   LEU A 911    11739   7881   6188  -3708   -332   -243       C  
-ATOM   6748  O   LEU A 911      27.152  20.942 -58.172  1.00 66.36           O  
-ANISOU 6748  O   LEU A 911    11444   7939   5830  -3911   -429   -281       O  
-ATOM   6749  CB  LEU A 911      30.072  22.365 -57.624  1.00 68.85           C  
-ANISOU 6749  CB  LEU A 911    12178   7197   6783  -3719   -145   -721       C  
-ATOM   6750  CG  LEU A 911      31.543  22.177 -58.001  1.00 68.46           C  
-ANISOU 6750  CG  LEU A 911    12328   6777   6908  -3904    -42   -986       C  
-ATOM   6751  CD1 LEU A 911      32.444  22.364 -56.786  1.00 67.85           C  
-ANISOU 6751  CD1 LEU A 911    12267   6466   7048  -3612     73  -1116       C  
-ATOM   6752  CD2 LEU A 911      31.746  20.806 -58.621  1.00 69.77           C  
-ANISOU 6752  CD2 LEU A 911    12459   7190   6861  -4186    -45  -1034       C  
-ATOM   6753  N   LYS A 912      27.019  23.154 -57.797  1.00 58.23           N  
-ANISOU 6753  N   LYS A 912    10444   6682   5000  -3375   -324    -39       N  
-ATOM   6754  CA  LYS A 912      25.624  23.122 -57.379  1.00 58.35           C  
-ANISOU 6754  CA  LYS A 912    10255   7065   4849  -3235   -430    183       C  
-ATOM   6755  C   LYS A 912      24.741  22.700 -58.545  1.00 62.39           C  
-ANISOU 6755  C   LYS A 912    10658   7999   5049  -3427   -510    408       C  
-ATOM   6756  O   LYS A 912      23.756  21.981 -58.372  1.00 63.82           O  
-ANISOU 6756  O   LYS A 912    10677   8525   5047  -3496   -622    497       O  
-ATOM   6757  CB  LYS A 912      25.193  24.498 -56.884  1.00 55.35           C  
-ANISOU 6757  CB  LYS A 912     9842   6618   4571  -2842   -391    376       C  
-ATOM   6758  CG  LYS A 912      25.954  24.972 -55.676  1.00 48.61           C  
-ANISOU 6758  CG  LYS A 912     9085   5367   4019  -2624   -321    176       C  
-ATOM   6759  CD  LYS A 912      25.542  26.377 -55.291  1.00 45.53           C  
-ANISOU 6759  CD  LYS A 912     8671   4910   3720  -2240   -279    378       C  
-ATOM   6760  CE  LYS A 912      26.347  26.876 -54.106  1.00 41.44           C  
-ANISOU 6760  CE  LYS A 912     8260   3978   3508  -2024   -207    174       C  
-ATOM   6761  NZ  LYS A 912      26.250  28.353 -53.959  1.00 40.98           N  
-ANISOU 6761  NZ  LYS A 912     8231   3775   3563  -1677   -139    346       N  
-ATOM   6762  N   ALA A 913      25.102  23.161 -59.738  1.00 60.42           N  
-ANISOU 6762  N   ALA A 913    10499   7716   4740  -3512   -452    500       N  
-ATOM   6763  CA  ALA A 913      24.396  22.774 -60.949  1.00 64.32           C  
-ANISOU 6763  CA  ALA A 913    10917   8578   4944  -3712   -520    699       C  
-ATOM   6764  C   ALA A 913      24.419  21.259 -61.118  1.00 64.86           C  
-ANISOU 6764  C   ALA A 913    10954   8812   4876  -4065   -600    538       C  
-ATOM   6765  O   ALA A 913      23.387  20.642 -61.378  1.00 65.17           O  
-ANISOU 6765  O   ALA A 913    10839   9241   4680  -4169   -713    686       O  
-ATOM   6766  CB  ALA A 913      25.010  23.452 -62.150  1.00 64.47           C  
-ANISOU 6766  CB  ALA A 913    11074   8465   4955  -3767   -429    768       C  
-ATOM   6767  N   GLU A 914      25.599  20.665 -60.968  1.00 82.81           N  
-ANISOU 6767  N   GLU A 914    13375  10787   7301  -4248   -541    235       N  
-ATOM   6768  CA  GLU A 914      25.737  19.214 -61.039  1.00 84.24           C  
-ANISOU 6768  CA  GLU A 914    13545  11084   7380  -4580   -610     51       C  
-ATOM   6769  C   GLU A 914      24.718  18.529 -60.144  1.00 83.17           C  
-ANISOU 6769  C   GLU A 914    13226  11226   7150  -4545   -730     85       C  
-ATOM   6770  O   GLU A 914      24.053  17.578 -60.559  1.00 83.80           O  
-ANISOU 6770  O   GLU A 914    13203  11637   7002  -4766   -832    140       O  
-ATOM   6771  CB  GLU A 914      27.139  18.775 -60.623  1.00 87.32           C  
-ANISOU 6771  CB  GLU A 914    14108  11067   8002  -4705   -528   -302       C  
-ATOM   6772  CG  GLU A 914      28.213  19.013 -61.663  1.00 97.58           C  
-ANISOU 6772  CG  GLU A 914    15589  12134   9354  -4860   -423   -382       C  
-ATOM   6773  CD  GLU A 914      29.513  18.317 -61.312  1.00101.48           C  
-ANISOU 6773  CD  GLU A 914    16234  12285  10039  -5041   -363   -739       C  
-ATOM   6774  OE1 GLU A 914      29.485  17.401 -60.462  1.00104.54           O  
-ANISOU 6774  OE1 GLU A 914    16557  12730  10434  -5046   -376   -843       O  
-ATOM   6775  OE2 GLU A 914      30.560  18.688 -61.883  1.00105.39           O  
-ANISOU 6775  OE2 GLU A 914    16893  12495  10656  -5101   -253   -841       O  
-ATOM   6776  N   VAL A 915      24.609  19.016 -58.912  1.00 66.13           N  
-ANISOU 6776  N   VAL A 915    11032   8925   5168  -4267   -717     49       N  
-ATOM   6777  CA  VAL A 915      23.674  18.456 -57.946  1.00 65.52           C  
-ANISOU 6777  CA  VAL A 915    10787   9080   5027  -4201   -820     76       C  
-ATOM   6778  C   VAL A 915      22.233  18.595 -58.427  1.00 68.94           C  
-ANISOU 6778  C   VAL A 915    11027   9970   5198  -4147   -918    407       C  
-ATOM   6779  O   VAL A 915      21.537  17.597 -58.614  1.00 70.95           O  
-ANISOU 6779  O   VAL A 915    11162  10546   5248  -4348  -1024    443       O  
-ATOM   6780  CB  VAL A 915      23.822  19.122 -56.556  1.00 62.65           C  
-ANISOU 6780  CB  VAL A 915    10430   8464   4910  -3877   -778     -2       C  
-ATOM   6781  CG1 VAL A 915      22.639  18.770 -55.669  1.00 61.65           C  
-ANISOU 6781  CG1 VAL A 915    10108   8627   4688  -3761   -883    103       C  
-ATOM   6782  CG2 VAL A 915      25.133  18.707 -55.898  1.00 59.10           C  
-ANISOU 6782  CG2 VAL A 915    10145   7604   4705  -3959   -710   -358       C  
-ATOM   6783  N   ILE A 916      21.792  19.833 -58.630  1.00 69.00           N  
-ANISOU 6783  N   ILE A 916    11002  10001   5212  -3876   -883    649       N  
-ATOM   6784  CA  ILE A 916      20.421  20.101 -59.052  1.00 72.97           C  
-ANISOU 6784  CA  ILE A 916    11322  10921   5483  -3788   -971    976       C  
-ATOM   6785  C   ILE A 916      20.038  19.251 -60.257  1.00 77.03           C  
-ANISOU 6785  C   ILE A 916    11790  11754   5725  -4113  -1048   1060       C  
-ATOM   6786  O   ILE A 916      18.902  18.793 -60.368  1.00 78.60           O  
-ANISOU 6786  O   ILE A 916    11811  12341   5711  -4159  -1160   1233       O  
-ATOM   6787  CB  ILE A 916      20.219  21.581 -59.434  1.00 72.37           C  
-ANISOU 6787  CB  ILE A 916    11262  10792   5445  -3501   -906   1215       C  
-ATOM   6788  CG1 ILE A 916      20.558  22.505 -58.260  1.00 69.82           C  
-ANISOU 6788  CG1 ILE A 916    10984  10157   5388  -3161   -830   1150       C  
-ATOM   6789  CG2 ILE A 916      18.787  21.820 -59.885  1.00 73.02           C  
-ANISOU 6789  CG2 ILE A 916    11149  11314   5282  -3417  -1002   1552       C  
-ATOM   6790  CD1 ILE A 916      19.384  22.781 -57.342  1.00 68.16           C  
-ANISOU 6790  CD1 ILE A 916    10587  10169   5141  -2900   -900   1320       C  
-ATOM   6791  N   ALA A 917      20.996  19.044 -61.156  1.00 89.60           N  
-ANISOU 6791  N   ALA A 917    13544  13175   7326  -4339   -987    936       N  
-ATOM   6792  CA  ALA A 917      20.734  18.372 -62.426  1.00 94.96           C  
-ANISOU 6792  CA  ALA A 917    14206  14123   7752  -4639  -1045   1024       C  
-ATOM   6793  C   ALA A 917      20.562  16.861 -62.279  1.00 97.12           C  
-ANISOU 6793  C   ALA A 917    14417  14583   7900  -4941  -1143    873       C  
-ATOM   6794  O   ALA A 917      20.262  16.168 -63.253  1.00 97.76           O  
-ANISOU 6794  O   ALA A 917    14471  14916   7759  -5204  -1208    938       O  
-ATOM   6795  CB  ALA A 917      21.835  18.690 -63.429  1.00 94.22           C  
-ANISOU 6795  CB  ALA A 917    14312  13773   7715  -4770   -940    942       C  
-ATOM   6796  N   LYS A 918      20.749  16.355 -61.064  1.00 94.14           N  
-ANISOU 6796  N   LYS A 918    14022  14083   7665  -4901  -1155    672       N  
-ATOM   6797  CA  LYS A 918      20.582  14.928 -60.802  1.00 96.92           C  
-ANISOU 6797  CA  LYS A 918    14313  14599   7912  -5170  -1247    519       C  
-ATOM   6798  C   LYS A 918      19.158  14.572 -60.394  1.00102.30           C  
-ANISOU 6798  C   LYS A 918    14765  15690   8414  -5111  -1375    712       C  
-ATOM   6799  O   LYS A 918      18.807  13.397 -60.309  1.00104.20           O  
-ANISOU 6799  O   LYS A 918    14930  16140   8522  -5339  -1467    639       O  
-ATOM   6800  CB  LYS A 918      21.578  14.447 -59.747  1.00 93.12           C  
-ANISOU 6800  CB  LYS A 918    13943  13770   7670  -5193  -1196    182       C  
-ATOM   6801  CG  LYS A 918      22.867  13.934 -60.352  1.00 90.10           C  
-ANISOU 6801  CG  LYS A 918    13754  13123   7358  -5461  -1127    -66       C  
-ATOM   6802  CD  LYS A 918      24.001  13.877 -59.351  1.00 84.99           C  
-ANISOU 6802  CD  LYS A 918    13243  12050   6998  -5406  -1045   -377       C  
-ATOM   6803  CE  LYS A 918      25.291  13.471 -60.046  1.00 82.94           C  
-ANISOU 6803  CE  LYS A 918    13148  11512   6854  -5571   -856   -482       C  
-ATOM   6804  NZ  LYS A 918      26.464  13.473 -59.132  1.00 80.18           N  
-ANISOU 6804  NZ  LYS A 918    12911  10765   6790  -5381   -654   -633       N  
-ATOM   6805  N   ASN A 919      18.343  15.594 -60.153  1.00 94.06           N  
-ANISOU 6805  N   ASN A 919    13612  14760   7367  -4805  -1379    960       N  
-ATOM   6806  CA  ASN A 919      16.944  15.403 -59.788  1.00100.11           C  
-ANISOU 6806  CA  ASN A 919    14152  15918   7968  -4716  -1494   1171       C  
-ATOM   6807  C   ASN A 919      16.741  14.282 -58.764  1.00 97.86           C  
-ANISOU 6807  C   ASN A 919    13788  15701   7694  -4816  -1564    993       C  
-ATOM   6808  O   ASN A 919      15.939  13.372 -58.974  1.00 98.34           O  
-ANISOU 6808  O   ASN A 919    13714  16106   7546  -5001  -1676   1062       O  
-ATOM   6809  CB  ASN A 919      16.102  15.147 -61.042  1.00105.65           C  
-ANISOU 6809  CB  ASN A 919    14754  17014   8375  -4890  -1582   1413       C  
-ATOM   6810  CG  ASN A 919      14.615  15.340 -60.799  1.00113.20           C  
-ANISOU 6810  CG  ASN A 919    15475  18361   9173  -4727  -1684   1694       C  
-ATOM   6811  OD1 ASN A 919      14.209  16.013 -59.850  1.00115.66           O  
-ANISOU 6811  OD1 ASN A 919    15711  18633   9601  -4425  -1668   1763       O  
-ATOM   6812  ND2 ASN A 919      13.794  14.751 -61.661  1.00115.58           N  
-ANISOU 6812  ND2 ASN A 919    15661  19045   9209  -4926  -1791   1859       N  
-ATOM   6813  N   ASN A 920      17.477  14.349 -57.658  1.00122.19           N  
-ANISOU 6813  N   ASN A 920    16958  18449  11020  -4696  -1498    763       N  
-ATOM   6814  CA  ASN A 920      17.320  13.379 -56.577  1.00117.22           C  
-ANISOU 6814  CA  ASN A 920    16263  17850  10424  -4757  -1556    588       C  
-ATOM   6815  C   ASN A 920      16.244  13.837 -55.596  1.00115.18           C  
-ANISOU 6815  C   ASN A 920    15829  17762  10173  -4460  -1599    758       C  
-ATOM   6816  O   ASN A 920      16.398  14.869 -54.939  1.00114.40           O  
-ANISOU 6816  O   ASN A 920    15761  17449  10255  -4149  -1527    786       O  
-ATOM   6817  CB  ASN A 920      18.649  13.163 -55.844  1.00119.26           C  
-ANISOU 6817  CB  ASN A 920    16706  17666  10940  -4783  -1470    246       C  
-ATOM   6818  CG  ASN A 920      18.607  11.981 -54.892  1.00119.44           C  
-ANISOU 6818  CG  ASN A 920    16666  17687  11029  -4901  -1491     65       C  
-ATOM   6819  OD1 ASN A 920      18.225  12.116 -53.730  1.00121.98           O  
-ANISOU 6819  OD1 ASN A 920    16916  17991  11438  -4694  -1510     44       O  
-ATOM   6820  ND2 ASN A 920      19.006  10.814 -55.383  1.00122.20           N  
-ANISOU 6820  ND2 ASN A 920    17019  18000  11413  -5194  -1392      2       N  
-ATOM   6821  N   SER A 921      15.157  13.073 -55.506  1.00 80.44           N  
-ANISOU 6821  N   SER A 921    11245  13746   5574  -4557  -1717    871       N  
-ATOM   6822  CA  SER A 921      14.023  13.454 -54.669  1.00 79.38           C  
-ANISOU 6822  CA  SER A 921    10924  13821   5417  -4293  -1765   1057       C  
-ATOM   6823  C   SER A 921      14.467  13.868 -53.271  1.00 75.02           C  
-ANISOU 6823  C   SER A 921    10427  12953   5124  -4035  -1697    895       C  
-ATOM   6824  O   SER A 921      14.041  14.903 -52.755  1.00 76.42           O  
-ANISOU 6824  O   SER A 921    10550  13101   5387  -3706  -1663   1047       O  
-ATOM   6825  CB  SER A 921      13.011  12.327 -54.597  1.00 80.48           C  
-ANISOU 6825  CB  SER A 921    10881  14358   5340  -4480  -1896   1118       C  
-ATOM   6826  N   PHE A 922      15.333  13.060 -52.670  1.00 99.33           N  
-ANISOU 6826  N   PHE A 922    13619  15794   8329  -4185  -1677    587       N  
-ATOM   6827  CA  PHE A 922      15.840  13.344 -51.334  1.00 95.41           C  
-ANISOU 6827  CA  PHE A 922    13191  14980   8082  -3967  -1617    404       C  
-ATOM   6828  C   PHE A 922      16.516  14.711 -51.244  1.00 95.54           C  
-ANISOU 6828  C   PHE A 922    13336  14654   8310  -3688  -1498    419       C  
-ATOM   6829  O   PHE A 922      16.162  15.531 -50.394  1.00 93.35           O  
-ANISOU 6829  O   PHE A 922    13011  14309   8147  -3366  -1470    503       O  
-ATOM   6830  CB  PHE A 922      16.805  12.247 -50.882  1.00 90.50           C  
-ANISOU 6830  CB  PHE A 922    12685  14116   7585  -4201  -1590     68       C  
-ATOM   6831  CG  PHE A 922      17.574  12.595 -49.643  1.00 85.43           C  
-ANISOU 6831  CG  PHE A 922    12154  13078   7227  -3994  -1507   -144       C  
-ATOM   6832  CD1 PHE A 922      16.937  12.665 -48.415  1.00 84.36           C  
-ANISOU 6832  CD1 PHE A 922    11918  12997   7137  -3776  -1545   -131       C  
-ATOM   6833  CD2 PHE A 922      18.933  12.852 -49.705  1.00 83.03           C  
-ANISOU 6833  CD2 PHE A 922    12052  12343   7154  -4008  -1381   -345       C  
-ATOM   6834  CE1 PHE A 922      17.643  12.989 -47.267  1.00 82.51           C  
-ANISOU 6834  CE1 PHE A 922    11789  12393   7168  -3581  -1468   -323       C  
-ATOM   6835  CE2 PHE A 922      19.643  13.172 -48.564  1.00 82.63           C  
-ANISOU 6835  CE2 PHE A 922    12097  11920   7378  -3805  -1291   -520       C  
-ATOM   6836  CZ  PHE A 922      18.997  13.241 -47.342  1.00 81.38           C  
-ANISOU 6836  CZ  PHE A 922    11844  11818   7260  -3594  -1339   -515       C  
-ATOM   6837  N   VAL A 923      17.482  14.953 -52.128  1.00 97.86           N  
-ANISOU 6837  N   VAL A 923    13793  14735   8654  -3811  -1429    340       N  
-ATOM   6838  CA  VAL A 923      18.263  16.189 -52.100  1.00 99.13           C  
-ANISOU 6838  CA  VAL A 923    14097  14541   9026  -3578  -1311    327       C  
-ATOM   6839  C   VAL A 923      17.440  17.437 -52.424  1.00103.58           C  
-ANISOU 6839  C   VAL A 923    14566  15257   9533  -3295  -1300    652       C  
-ATOM   6840  O   VAL A 923      17.597  18.472 -51.778  1.00104.98           O  
-ANISOU 6840  O   VAL A 923    14783  15217   9889  -2984  -1231    681       O  
-ATOM   6841  CB  VAL A 923      19.468  16.123 -53.053  1.00 97.77           C  
-ANISOU 6841  CB  VAL A 923    14118  14123   8908  -3795  -1240    174       C  
-ATOM   6842  CG1 VAL A 923      20.199  17.453 -53.067  1.00 98.07           C  
-ANISOU 6842  CG1 VAL A 923    14293  13815   9154  -3547  -1120    185       C  
-ATOM   6843  CG2 VAL A 923      20.406  15.002 -52.641  1.00 94.60           C  
-ANISOU 6843  CG2 VAL A 923    13829  13513   8600  -4042  -1237   -168       C  
-ATOM   6844  N   ASN A 924      16.566  17.338 -53.422  1.00 89.31           N  
-ANISOU 6844  N   ASN A 924    12636  13821   7477  -3400  -1370    896       N  
-ATOM   6845  CA  ASN A 924      15.704  18.457 -53.790  1.00 95.23           C  
-ANISOU 6845  CA  ASN A 924    13283  14751   8149  -3147  -1370   1218       C  
-ATOM   6846  C   ASN A 924      14.840  18.923 -52.622  1.00 96.62           C  
-ANISOU 6846  C   ASN A 924    13319  15013   8381  -2829  -1393   1331       C  
-ATOM   6847  O   ASN A 924      14.295  20.029 -52.646  1.00 98.51           O  
-ANISOU 6847  O   ASN A 924    13501  15304   8626  -2549  -1370   1560       O  
-ATOM   6848  CB  ASN A 924      14.823  18.101 -54.993  1.00 97.65           C  
-ANISOU 6848  CB  ASN A 924    13465  15476   8162  -3337  -1460   1452       C  
-ATOM   6849  CG  ASN A 924      15.600  18.063 -56.299  1.00 98.61           C  
-ANISOU 6849  CG  ASN A 924    13730  15507   8229  -3571  -1419   1415       C  
-ATOM   6850  OD1 ASN A 924      16.678  18.645 -56.412  1.00 98.92           O  
-ANISOU 6850  OD1 ASN A 924    13952  15184   8450  -3522  -1312   1286       O  
-ATOM   6851  ND2 ASN A 924      15.045  17.387 -57.298  1.00 97.79           N  
-ANISOU 6851  ND2 ASN A 924    13546  15735   7875  -3824  -1505   1533       N  
-ATOM   6852  N   GLU A 925      14.721  18.077 -51.602  1.00113.22           N  
-ANISOU 6852  N   GLU A 925    15370  17126  10521  -2873  -1436   1169       N  
-ATOM   6853  CA  GLU A 925      13.936  18.413 -50.419  1.00113.65           C  
-ANISOU 6853  CA  GLU A 925    15297  17253  10632  -2586  -1456   1253       C  
-ATOM   6854  C   GLU A 925      14.753  19.238 -49.428  1.00108.41           C  
-ANISOU 6854  C   GLU A 925    14773  16160  10259  -2313  -1352   1101       C  
-ATOM   6855  O   GLU A 925      14.247  20.201 -48.851  1.00108.86           O  
-ANISOU 6855  O   GLU A 925    14770  16208  10385  -1983  -1327   1254       O  
-ATOM   6856  CB  GLU A 925      13.388  17.153 -49.742  1.00120.19           C  
-ANISOU 6856  CB  GLU A 925    16004  18296  11368  -2744  -1549   1157       C  
-ATOM   6857  CG  GLU A 925      12.283  17.432 -48.730  1.00133.27           C  
-ANISOU 6857  CG  GLU A 925    17482  20141  13012  -2474  -1589   1311       C  
-ATOM   6858  CD  GLU A 925      12.563  16.821 -47.369  1.00138.46           C  
-ANISOU 6858  CD  GLU A 925    18165  20629  13816  -2441  -1587   1070       C  
-ATOM   6859  OE1 GLU A 925      12.063  17.361 -46.357  1.00143.11           O  
-ANISOU 6859  OE1 GLU A 925    18682  21201  14492  -2147  -1575   1137       O  
-ATOM   6860  OE2 GLU A 925      13.285  15.803 -47.310  1.00142.97           O  
-ANISOU 6860  OE2 GLU A 925    18829  21080  14412  -2707  -1598    813       O  
-ATOM   6861  N   ILE A 926      16.013  18.859 -49.226  1.00 87.53           N  
-ANISOU 6861  N   ILE A 926    12314  13160   7783  -2448  -1293    800       N  
-ATOM   6862  CA  ILE A 926      16.903  19.644 -48.376  1.00 83.10           C  
-ANISOU 6862  CA  ILE A 926    11905  12166   7505  -2209  -1192    642       C  
-ATOM   6863  C   ILE A 926      16.998  21.058 -48.929  1.00 85.67           C  
-ANISOU 6863  C   ILE A 926    12282  12381   7888  -1975  -1116    831       C  
-ATOM   6864  O   ILE A 926      16.861  22.037 -48.195  1.00 86.31           O  
-ANISOU 6864  O   ILE A 926    12363  12322   8108  -1645  -1069    902       O  
-ATOM   6865  CB  ILE A 926      18.331  19.055 -48.296  1.00 74.40           C  
-ANISOU 6865  CB  ILE A 926    11006  10694   6570  -2418  -1137    296       C  
-ATOM   6866  CG1 ILE A 926      18.350  17.760 -47.482  1.00 67.87           C  
-ANISOU 6866  CG1 ILE A 926    10148   9901   5737  -2595  -1200     75       C  
-ATOM   6867  CG2 ILE A 926      19.281  20.058 -47.664  1.00 73.25           C  
-ANISOU 6867  CG2 ILE A 926    11024  10097   6710  -2166  -1026    170       C  
-ATOM   6868  CD1 ILE A 926      17.823  16.561 -48.228  1.00 61.06           C  
-ANISOU 6868  CD1 ILE A 926     9183   9395   4621  -2935  -1298    108       C  
-ATOM   6869  N   ILE A 927      17.230  21.149 -50.235  1.00 82.38           N  
-ANISOU 6869  N   ILE A 927    11913  12027   7360  -2150  -1104    913       N  
-ATOM   6870  CA  ILE A 927      17.303  22.431 -50.924  1.00 85.28           C  
-ANISOU 6870  CA  ILE A 927    12332  12317   7755  -1964  -1037   1104       C  
-ATOM   6871  C   ILE A 927      15.990  23.192 -50.792  1.00 90.56           C  
-ANISOU 6871  C   ILE A 927    12818  13280   8310  -1690  -1079   1427       C  
-ATOM   6872  O   ILE A 927      15.984  24.415 -50.656  1.00 91.86           O  
-ANISOU 6872  O   ILE A 927    13015  13306   8581  -1396  -1016   1553       O  
-ATOM   6873  CB  ILE A 927      17.640  22.250 -52.419  1.00 85.11           C  
-ANISOU 6873  CB  ILE A 927    12373  12373   7592  -2232  -1032   1152       C  
-ATOM   6874  CG1 ILE A 927      18.978  21.528 -52.579  1.00 81.18           C  
-ANISOU 6874  CG1 ILE A 927    12061  11572   7212  -2501   -982    831       C  
-ATOM   6875  CG2 ILE A 927      17.676  23.592 -53.129  1.00 84.62           C  
-ANISOU 6875  CG2 ILE A 927    12362  12237   7552  -2033   -962   1359       C  
-ATOM   6876  CD1 ILE A 927      19.362  21.268 -54.017  1.00 81.47           C  
-ANISOU 6876  CD1 ILE A 927    12169  11674   7113  -2780   -974    858       C  
-ATOM   6877  N   SER A 928      14.878  22.465 -50.833  1.00 98.92           N  
-ANISOU 6877  N   SER A 928    13685  14745   9154  -1787  -1188   1561       N  
-ATOM   6878  CA  SER A 928      13.566  23.077 -50.663  1.00105.80           C  
-ANISOU 6878  CA  SER A 928    14366  15924   9910  -1540  -1237   1864       C  
-ATOM   6879  C   SER A 928      13.404  23.575 -49.232  1.00107.28           C  
-ANISOU 6879  C   SER A 928    14529  15954  10277  -1218  -1207   1824       C  
-ATOM   6880  O   SER A 928      12.647  24.508 -48.969  1.00109.50           O  
-ANISOU 6880  O   SER A 928    14716  16336  10554   -920  -1203   2049       O  
-ATOM   6881  CB  SER A 928      12.458  22.076 -50.990  1.00107.05           C  
-ANISOU 6881  CB  SER A 928    14325  16546   9805  -1741  -1363   1992       C  
-ATOM   6882  OG  SER A 928      12.115  21.310 -49.847  1.00107.37           O  
-ANISOU 6882  OG  SER A 928    14278  16643   9874  -1735  -1411   1872       O  
-ATOM   6883  N   ARG A 929      14.127  22.945 -48.312  1.00124.10           N  
-ANISOU 6883  N   ARG A 929    16750  17836  12566  -1280  -1187   1535       N  
-ATOM   6884  CA  ARG A 929      14.067  23.305 -46.900  1.00125.35           C  
-ANISOU 6884  CA  ARG A 929    16903  17821  12903   -997  -1159   1462       C  
-ATOM   6885  C   ARG A 929      14.996  24.473 -46.571  1.00125.89           C  
-ANISOU 6885  C   ARG A 929    17150  17459  13225   -748  -1043   1386       C  
-ATOM   6886  O   ARG A 929      15.291  24.730 -45.403  1.00125.33           O  
-ANISOU 6886  O   ARG A 929    17131  17145  13345   -545  -1004   1255       O  
-ATOM   6887  CB  ARG A 929      14.417  22.096 -46.029  1.00124.43           C  
-ANISOU 6887  CB  ARG A 929    16806  17628  12842  -1171  -1192   1184       C  
-ATOM   6888  CG  ARG A 929      13.323  21.041 -45.943  1.00126.09           C  
-ANISOU 6888  CG  ARG A 929    16816  18260  12833  -1329  -1307   1268       C  
-ATOM   6889  CD  ARG A 929      13.803  19.826 -45.164  1.00125.68           C  
-ANISOU 6889  CD  ARG A 929    16809  18102  12842  -1526  -1334    973       C  
-ATOM   6890  NE  ARG A 929      14.742  20.199 -44.109  1.00125.72           N  
-ANISOU 6890  NE  ARG A 929    16972  17673  13121  -1352  -1254    741       N  
-ATOM   6891  CZ  ARG A 929      15.125  19.396 -43.120  1.00124.70           C  
-ANISOU 6891  CZ  ARG A 929    16887  17400  13092  -1418  -1265    491       C  
-ATOM   6892  NH1 ARG A 929      14.642  18.163 -43.034  1.00124.04           N  
-ANISOU 6892  NH1 ARG A 929    16699  17572  12857  -1655  -1353    439       N  
-ATOM   6893  NH2 ARG A 929      15.987  19.831 -42.211  1.00123.84           N  
-ANISOU 6893  NH2 ARG A 929    16928  16889  13236  -1245  -1191    293       N  
-ATOM   6894  N   ILE A 930      15.447  25.179 -47.603  1.00124.14           N  
-ANISOU 6894  N   ILE A 930    17022  17145  13002   -763   -989   1470       N  
-ATOM   6895  CA  ILE A 930      16.370  26.299 -47.431  1.00123.15           C  
-ANISOU 6895  CA  ILE A 930    17072  16611  13109   -548   -877   1403       C  
-ATOM   6896  C   ILE A 930      15.752  27.606 -47.930  1.00125.35           C  
-ANISOU 6896  C   ILE A 930    17299  16990  13339   -282   -851   1711       C  
-ATOM   6897  O   ILE A 930      14.791  27.601 -48.698  1.00127.86           O  
-ANISOU 6897  O   ILE A 930    17472  17677  13433   -325   -914   1962       O  
-ATOM   6898  CB  ILE A 930      17.709  26.039 -48.162  1.00120.83           C  
-ANISOU 6898  CB  ILE A 930    16977  16027  12904   -799   -815   1184       C  
-ATOM   6899  CG1 ILE A 930      18.320  24.717 -47.693  1.00118.47           C  
-ANISOU 6899  CG1 ILE A 930    16730  15634  12649  -1070   -844    878       C  
-ATOM   6900  CG2 ILE A 930      18.683  27.182 -47.933  1.00121.53           C  
-ANISOU 6900  CG2 ILE A 930    17248  15684  13245   -578   -698   1106       C  
-ATOM   6901  CD1 ILE A 930      19.647  24.393 -48.338  1.00115.72           C  
-ANISOU 6901  CD1 ILE A 930    16575  14998  12396  -1320   -783    646       C  
-TER    6902      ILE A 930                                                      
-ATOM   6903  N   LYS B 217     -47.341   7.621  17.803  1.00126.99           N  
-ANISOU 6903  N   LYS B 217    11401  22556  14295  -1073    -49  -2133       N  
-ATOM   6904  CA  LYS B 217     -45.966   7.395  18.231  1.00125.94           C  
-ANISOU 6904  CA  LYS B 217    11544  22030  14279  -1067    -66  -2030       C  
-ATOM   6905  C   LYS B 217     -45.902   7.033  19.712  1.00124.62           C  
-ANISOU 6905  C   LYS B 217    11556  21680  14113  -1160      7  -2107       C  
-ATOM   6906  O   LYS B 217     -44.876   7.227  20.364  1.00123.47           O  
-ANISOU 6906  O   LYS B 217    11611  21214  14089  -1087    -31  -2019       O  
-ATOM   6907  CB  LYS B 217     -45.111   8.620  17.940  1.00123.94           C  
-ANISOU 6907  CB  LYS B 217    11295  21596  14201   -782   -206  -1856       C  
-ATOM   6908  N   SER B 218     -47.006   6.511  20.239  1.00145.45           N  
-ANISOU 6908  N   SER B 218    14122  24530  16612  -1326    112  -2275       N  
-ATOM   6909  CA  SER B 218     -47.065   6.110  21.639  1.00143.35           C  
-ANISOU 6909  CA  SER B 218    14023  24121  16324  -1441    192  -2363       C  
-ATOM   6910  C   SER B 218     -46.226   4.856  21.871  1.00139.43           C  
-ANISOU 6910  C   SER B 218    13796  23381  15800  -1651    266  -2355       C  
-ATOM   6911  O   SER B 218     -45.839   4.554  22.999  1.00138.51           O  
-ANISOU 6911  O   SER B 218    13881  23044  15702  -1716    303  -2370       O  
-ATOM   6912  CB  SER B 218     -48.514   5.876  22.078  1.00147.81           C  
-ANISOU 6912  CB  SER B 218    14429  24992  16739  -1574    292  -2557       C  
-ATOM   6913  OG  SER B 218     -48.599   5.660  23.477  1.00151.31           O  
-ANISOU 6913  OG  SER B 218    15025  25299  17166  -1665    360  -2639       O  
-ATOM   6914  N   ILE B 219     -45.942   4.131  20.794  1.00130.43           N  
-ANISOU 6914  N   ILE B 219    12658  22281  14620  -1757    289  -2330       N  
-ATOM   6915  CA  ILE B 219     -45.087   2.955  20.872  1.00124.57           C  
-ANISOU 6915  CA  ILE B 219    12161  21299  13870  -1942    357  -2312       C  
-ATOM   6916  C   ILE B 219     -43.638   3.374  21.094  1.00117.84           C  
-ANISOU 6916  C   ILE B 219    11498  20076  13199  -1781    255  -2143       C  
-ATOM   6917  O   ILE B 219     -42.721   2.564  20.970  1.00117.52           O  
-ANISOU 6917  O   ILE B 219    11649  19810  13194  -1881    280  -2091       O  
-ATOM   6918  CB  ILE B 219     -45.182   2.085  19.598  1.00126.29           C  
-ANISOU 6918  CB  ILE B 219    12318  21667  14000  -2104    418  -2338       C  
-ATOM   6919  CG1 ILE B 219     -44.475   2.760  18.417  1.00126.92           C  
-ANISOU 6919  CG1 ILE B 219    12316  21717  14191  -1922    298  -2190       C  
-ATOM   6920  CG2 ILE B 219     -46.637   1.789  19.260  1.00128.19           C  
-ANISOU 6920  CG2 ILE B 219    12337  22308  14061  -2245    507  -2504       C  
-ATOM   6921  CD1 ILE B 219     -45.248   3.909  17.804  1.00129.03           C  
-ANISOU 6921  CD1 ILE B 219    12305  22265  14454  -1731    207  -2174       C  
-ATOM   6922  N   TYR B 220     -43.446   4.649  21.418  1.00112.45           N  
-ANISOU 6922  N   TYR B 220    10756  19335  12634  -1532    143  -2062       N  
-ATOM   6923  CA  TYR B 220     -42.119   5.202  21.668  1.00103.47           C  
-ANISOU 6923  CA  TYR B 220     9778  17865  11671  -1361     41  -1909       C  
-ATOM   6924  C   TYR B 220     -42.021   5.761  23.082  1.00 99.56           C  
-ANISOU 6924  C   TYR B 220     9382  17215  11231  -1280     21  -1913       C  
-ATOM   6925  O   TYR B 220     -42.944   6.418  23.563  1.00 99.99           O  
-ANISOU 6925  O   TYR B 220     9296  17445  11249  -1219     27  -1987       O  
-ATOM   6926  CB  TYR B 220     -41.794   6.311  20.660  1.00100.43           C  
-ANISOU 6926  CB  TYR B 220     9244  17521  11395  -1121    -81  -1788       C  
-ATOM   6927  CG  TYR B 220     -41.377   5.821  19.288  1.00 96.00           C  
-ANISOU 6927  CG  TYR B 220     8654  16994  10826  -1178    -87  -1736       C  
-ATOM   6928  CD1 TYR B 220     -40.608   4.674  19.142  1.00 93.51           C  
-ANISOU 6928  CD1 TYR B 220     8527  16494  10508  -1354    -27  -1729       C  
-ATOM   6929  CD2 TYR B 220     -41.752   6.509  18.140  1.00 94.36           C  
-ANISOU 6929  CD2 TYR B 220     8233  17003  10615  -1057   -151  -1694       C  
-ATOM   6930  CE1 TYR B 220     -40.227   4.225  17.893  1.00 91.31           C  
-ANISOU 6930  CE1 TYR B 220     8221  16246  10227  -1416    -23  -1691       C  
-ATOM   6931  CE2 TYR B 220     -41.375   6.067  16.887  1.00 92.29           C  
-ANISOU 6931  CE2 TYR B 220     7947  16779  10340  -1121   -153  -1650       C  
-ATOM   6932  CZ  TYR B 220     -40.612   4.924  16.768  1.00 91.09           C  
-ANISOU 6932  CZ  TYR B 220     7981  16441  10188  -1305    -85  -1654       C  
-ATOM   6933  OH  TYR B 220     -40.233   4.478  15.520  1.00 90.22           O  
-ANISOU 6933  OH  TYR B 220     7845  16366  10067  -1380    -78  -1619       O  
-ATOM   6934  N   THR B 221     -40.899   5.500  23.742  1.00 93.27           N  
-ANISOU 6934  N   THR B 221     8825  16092  10523  -1282     -3  -1835       N  
-ATOM   6935  CA  THR B 221     -40.635   6.083  25.048  1.00 86.78           C  
-ANISOU 6935  CA  THR B 221     8111  15098   9764  -1197    -34  -1821       C  
-ATOM   6936  C   THR B 221     -40.427   7.582  24.881  1.00 83.31           C  
-ANISOU 6936  C   THR B 221     7546  14650   9458   -914   -148  -1732       C  
-ATOM   6937  O   THR B 221     -40.037   8.040  23.806  1.00 82.57           O  
-ANISOU 6937  O   THR B 221     7364  14572   9438   -783   -218  -1642       O  
-ATOM   6938  CB  THR B 221     -39.375   5.481  25.685  1.00 85.33           C  
-ANISOU 6938  CB  THR B 221     8206  14563   9651  -1249    -49  -1741       C  
-ATOM   6939  OG1 THR B 221     -38.214   5.987  25.017  1.00 83.52           O  
-ANISOU 6939  OG1 THR B 221     8011  14146   9576  -1078   -154  -1597       O  
-ATOM   6940  CG2 THR B 221     -39.397   3.965  25.583  1.00 82.42           C  
-ANISOU 6940  CG2 THR B 221     7969  14171   9174  -1511     57  -1801       C  
-ATOM   6941  N   PRO B 222     -40.684   8.358  25.944  1.00 97.32           N  
-ANISOU 6941  N   PRO B 222     9317  16397  11264   -824   -161  -1758       N  
-ATOM   6942  CA  PRO B 222     -40.501   9.811  25.874  1.00 94.22           C  
-ANISOU 6942  CA  PRO B 222     8814  15983  11004   -556   -256  -1680       C  
-ATOM   6943  C   PRO B 222     -39.120  10.195  25.355  1.00 90.32           C  
-ANISOU 6943  C   PRO B 222     8423  15235  10660   -407   -355  -1521       C  
-ATOM   6944  O   PRO B 222     -39.018  10.991  24.419  1.00 89.74           O  
-ANISOU 6944  O   PRO B 222     8216  15223  10660   -234   -423  -1446       O  
-ATOM   6945  CB  PRO B 222     -40.647  10.251  27.332  1.00 94.05           C  
-ANISOU 6945  CB  PRO B 222     8868  15872  10996   -544   -236  -1731       C  
-ATOM   6946  CG  PRO B 222     -41.531   9.224  27.942  1.00 95.25           C  
-ANISOU 6946  CG  PRO B 222     9052  16156  10982   -794   -119  -1878       C  
-ATOM   6947  CD  PRO B 222     -41.193   7.925  27.257  1.00 97.16           C  
-ANISOU 6947  CD  PRO B 222     9395  16368  11154   -976    -79  -1870       C  
-ATOM   6948  N   LEU B 223     -38.075   9.632  25.956  1.00 72.08           N  
-ANISOU 6948  N   LEU B 223     6347  12645   8394   -475   -362  -1472       N  
-ATOM   6949  CA  LEU B 223     -36.710   9.984  25.585  1.00 67.95           C  
-ANISOU 6949  CA  LEU B 223     5933  11866   8020   -340   -452  -1334       C  
-ATOM   6950  C   LEU B 223     -36.480   9.798  24.090  1.00 68.40           C  
-ANISOU 6950  C   LEU B 223     5904  11992   8093   -320   -479  -1277       C  
-ATOM   6951  O   LEU B 223     -35.963  10.689  23.414  1.00 66.87           O  
-ANISOU 6951  O   LEU B 223     5649  11751   8009   -131   -559  -1183       O  
-ATOM   6952  CB  LEU B 223     -35.699   9.160  26.385  1.00 63.13           C  
-ANISOU 6952  CB  LEU B 223     5583  10971   7434   -453   -448  -1302       C  
-ATOM   6953  CG  LEU B 223     -34.237   9.578  26.221  1.00 56.62           C  
-ANISOU 6953  CG  LEU B 223     4879   9862   6771   -309   -543  -1170       C  
-ATOM   6954  CD1 LEU B 223     -34.057  11.026  26.632  1.00 54.00           C  
-ANISOU 6954  CD1 LEU B 223     4488   9484   6547    -83   -611  -1124       C  
-ATOM   6955  CD2 LEU B 223     -33.307   8.671  27.022  1.00 53.82           C  
-ANISOU 6955  CD2 LEU B 223     4773   9244   6433   -430   -539  -1143       C  
-ATOM   6956  N   GLU B 224     -36.869   8.634  23.581  1.00 72.54           N  
-ANISOU 6956  N   GLU B 224     6429  12628   8503   -523   -404  -1340       N  
-ATOM   6957  CA  GLU B 224     -36.717   8.326  22.165  1.00 74.50           C  
-ANISOU 6957  CA  GLU B 224     6598  12961   8748   -543   -413  -1302       C  
-ATOM   6958  C   GLU B 224     -37.322   9.430  21.300  1.00 75.79           C  
-ANISOU 6958  C   GLU B 224     6526  13345   8926   -364   -470  -1275       C  
-ATOM   6959  O   GLU B 224     -36.739   9.834  20.293  1.00 74.78           O  
-ANISOU 6959  O   GLU B 224     6360  13180   8874   -256   -534  -1182       O  
-ATOM   6960  CB  GLU B 224     -37.357   6.972  21.845  1.00 75.80           C  
-ANISOU 6960  CB  GLU B 224     6763  13277   8761   -803   -302  -1405       C  
-ATOM   6961  CG  GLU B 224     -36.640   5.776  22.470  1.00 76.44           C  
-ANISOU 6961  CG  GLU B 224     7087  13120   8836   -982   -246  -1413       C  
-ATOM   6962  CD  GLU B 224     -37.398   4.472  22.279  1.00 78.12           C  
-ANISOU 6962  CD  GLU B 224     7301  13490   8890  -1245   -119  -1529       C  
-ATOM   6963  OE1 GLU B 224     -38.635   4.525  22.111  1.00 79.84           O  
-ANISOU 6963  OE1 GLU B 224     7346  14006   8984  -1303    -64  -1631       O  
-ATOM   6964  OE2 GLU B 224     -36.759   3.398  22.292  1.00 76.89           O  
-ANISOU 6964  OE2 GLU B 224     7317  13160   8736  -1395    -69  -1522       O  
-ATOM   6965  N   LEU B 225     -38.488   9.920  21.711  1.00 90.92           N  
-ANISOU 6965  N   LEU B 225     8288  15487  10771   -332   -445  -1355       N  
-ATOM   6966  CA  LEU B 225     -39.166  11.002  21.003  1.00 92.81           C  
-ANISOU 6966  CA  LEU B 225     8295  15944  11024   -152   -499  -1332       C  
-ATOM   6967  C   LEU B 225     -38.382  12.306  21.112  1.00 91.58           C  
-ANISOU 6967  C   LEU B 225     8160  15602  11034    107   -599  -1212       C  
-ATOM   6968  O   LEU B 225     -38.297  13.076  20.155  1.00 90.68           O  
-ANISOU 6968  O   LEU B 225     7930  15551  10975    266   -668  -1130       O  
-ATOM   6969  CB  LEU B 225     -40.590  11.180  21.537  1.00 97.67           C  
-ANISOU 6969  CB  LEU B 225     8746  16832  11534   -184   -443  -1458       C  
-ATOM   6970  CG  LEU B 225     -41.585  10.078  21.159  1.00100.50           C  
-ANISOU 6970  CG  LEU B 225     9016  17453  11715   -417   -346  -1585       C  
-ATOM   6971  CD1 LEU B 225     -42.769  10.061  22.109  1.00104.22           C  
-ANISOU 6971  CD1 LEU B 225     9403  18106  12090   -491   -272  -1730       C  
-ATOM   6972  CD2 LEU B 225     -42.047  10.234  19.719  1.00102.45           C  
-ANISOU 6972  CD2 LEU B 225     9061  17948  11916   -378   -379  -1558       C  
-ATOM   6973  N   GLN B 226     -37.806  12.547  22.283  1.00 89.68           N  
-ANISOU 6973  N   GLN B 226     8073  15134  10869    144   -604  -1203       N  
-ATOM   6974  CA  GLN B 226     -36.944  13.700  22.472  1.00 89.18           C  
-ANISOU 6974  CA  GLN B 226     8057  14865  10963    368   -686  -1097       C  
-ATOM   6975  C   GLN B 226     -35.760  13.594  21.516  1.00 87.76           C  
-ANISOU 6975  C   GLN B 226     7965  14511  10870    409   -746   -984       C  
-ATOM   6976  O   GLN B 226     -35.288  14.596  20.980  1.00 88.11           O  
-ANISOU 6976  O   GLN B 226     7965  14492  11019    605   -818   -890       O  
-ATOM   6977  CB  GLN B 226     -36.449  13.760  23.914  1.00 89.73           C  
-ANISOU 6977  CB  GLN B 226     8298  14715  11081    355   -673  -1115       C  
-ATOM   6978  CG  GLN B 226     -36.424  15.154  24.510  1.00 92.06           C  
-ANISOU 6978  CG  GLN B 226     8544  14952  11483    571   -714  -1084       C  
-ATOM   6979  CD  GLN B 226     -35.938  15.150  25.943  1.00 92.12           C  
-ANISOU 6979  CD  GLN B 226     8723  14754  11524    534   -696  -1108       C  
-ATOM   6980  OE1 GLN B 226     -35.214  14.246  26.360  1.00 91.39           O  
-ANISOU 6980  OE1 GLN B 226     8819  14488  11416    396   -686  -1102       O  
-ATOM   6981  NE2 GLN B 226     -36.337  16.159  26.709  1.00 92.95           N  
-ANISOU 6981  NE2 GLN B 226     8764  14878  11673    656   -692  -1136       N  
-ATOM   6982  N   TYR B 227     -35.289  12.368  21.306  1.00 84.34           N  
-ANISOU 6982  N   TYR B 227     7658  13997  10392    220   -708   -999       N  
-ATOM   6983  CA  TYR B 227     -34.159  12.115  20.418  1.00 83.61           C  
-ANISOU 6983  CA  TYR B 227     7655  13734  10379    228   -751   -909       C  
-ATOM   6984  C   TYR B 227     -34.546  12.386  18.976  1.00 85.52           C  
-ANISOU 6984  C   TYR B 227     7724  14178  10590    275   -776   -875       C  
-ATOM   6985  O   TYR B 227     -33.926  13.205  18.298  1.00 85.51           O  
-ANISOU 6985  O   TYR B 227     7704  14098  10689    438   -849   -778       O  
-ATOM   6986  CB  TYR B 227     -33.669  10.672  20.570  1.00 80.14           C  
-ANISOU 6986  CB  TYR B 227     7382  13170   9896      2   -691   -945       C  
-ATOM   6987  CG  TYR B 227     -32.767  10.195  19.450  1.00 75.76           C  
-ANISOU 6987  CG  TYR B 227     6881  12510   9395    -37   -710   -882       C  
-ATOM   6988  CD1 TYR B 227     -31.439  10.595  19.378  1.00 73.45           C  
-ANISOU 6988  CD1 TYR B 227     6711  11944   9254     78   -779   -788       C  
-ATOM   6989  CD2 TYR B 227     -33.242   9.330  18.473  1.00 74.37           C  
-ANISOU 6989  CD2 TYR B 227     6631  12511   9117   -198   -653   -927       C  
-ATOM   6990  CE1 TYR B 227     -30.610  10.155  18.354  1.00 71.21           C  
-ANISOU 6990  CE1 TYR B 227     6473  11561   9024     35   -790   -741       C  
-ATOM   6991  CE2 TYR B 227     -32.423   8.884  17.447  1.00 72.15           C  
-ANISOU 6991  CE2 TYR B 227     6397  12132   8886   -246   -661   -878       C  
-ATOM   6992  CZ  TYR B 227     -31.109   9.300  17.391  1.00 70.55           C  
-ANISOU 6992  CZ  TYR B 227     6315  11653   8839   -128   -730   -786       C  
-ATOM   6993  OH  TYR B 227     -30.297   8.856  16.371  1.00 68.17           O  
-ANISOU 6993  OH  TYR B 227     6056  11253   8591   -182   -733   -748       O  
-ATOM   6994  N   ILE B 228     -35.576  11.688  18.513  1.00 94.33           N  
-ANISOU 6994  N   ILE B 228     8720  15560  11563    125   -714   -957       N  
-ATOM   6995  CA  ILE B 228     -36.063  11.850  17.152  1.00 96.32           C  
-ANISOU 6995  CA  ILE B 228     8796  16041  11759    145   -735   -934       C  
-ATOM   6996  C   ILE B 228     -36.148  13.320  16.769  1.00 96.78           C  
-ANISOU 6996  C   ILE B 228     8728  16146  11899    406   -825   -846       C  
-ATOM   6997  O   ILE B 228     -35.613  13.736  15.744  1.00 97.01           O  
-ANISOU 6997  O   ILE B 228     8734  16144  11982    495   -884   -755       O  
-ATOM   6998  CB  ILE B 228     -37.453  11.220  16.985  1.00 98.96           C  
-ANISOU 6998  CB  ILE B 228     8973  16708  11920    -10   -660  -1052       C  
-ATOM   6999  CG1 ILE B 228     -37.385   9.709  17.222  1.00 99.81           C  
-ANISOU 6999  CG1 ILE B 228     9208  16777  11939   -283   -558  -1140       C  
-ATOM   7000  CG2 ILE B 228     -38.004  11.521  15.608  1.00 99.39           C  
-ANISOU 7000  CG2 ILE B 228     8829  17020  11915     29   -694  -1022       C  
-ATOM   7001  CD1 ILE B 228     -38.728   9.017  17.165  1.00103.45           C  
-ANISOU 7001  CD1 ILE B 228     9532  17553  12223   -458   -468  -1273       C  
-ATOM   7002  N   GLU B 229     -36.817  14.100  17.608  1.00 90.74           N  
-ANISOU 7002  N   GLU B 229     7886  15448  11144    524   -830   -876       N  
-ATOM   7003  CA  GLU B 229     -37.036  15.514  17.341  1.00 92.27           C  
-ANISOU 7003  CA  GLU B 229     7950  15696  11414    776   -904   -801       C  
-ATOM   7004  C   GLU B 229     -35.731  16.269  17.089  1.00 89.49           C  
-ANISOU 7004  C   GLU B 229     7719  15067  11218    938   -977   -676       C  
-ATOM   7005  O   GLU B 229     -35.699  17.224  16.314  1.00 90.27           O  
-ANISOU 7005  O   GLU B 229     7722  15207  11368   1114  -1042   -588       O  
-ATOM   7006  CB  GLU B 229     -37.803  16.154  18.501  1.00 96.66           C  
-ANISOU 7006  CB  GLU B 229     8441  16308  11978    861   -882   -865       C  
-ATOM   7007  CG  GLU B 229     -38.077  17.636  18.326  1.00104.33           C  
-ANISOU 7007  CG  GLU B 229     9277  17326  13038   1127   -947   -794       C  
-ATOM   7008  CD  GLU B 229     -37.471  18.479  19.433  1.00106.70           C  
-ANISOU 7008  CD  GLU B 229     9690  17380  13471   1266   -957   -770       C  
-ATOM   7009  OE1 GLU B 229     -36.563  17.985  20.136  1.00108.43           O  
-ANISOU 7009  OE1 GLU B 229    10110  17359  13731   1178   -939   -775       O  
-ATOM   7010  OE2 GLU B 229     -37.908  19.636  19.602  1.00107.94           O  
-ANISOU 7010  OE2 GLU B 229     9733  17588  13693   1462   -983   -746       O  
-ATOM   7011  N   MET B 230     -34.655  15.840  17.739  1.00 88.18           N  
-ANISOU 7011  N   MET B 230     7762  14618  11125    878   -966   -667       N  
-ATOM   7012  CA  MET B 230     -33.368  16.513  17.589  1.00 86.66           C  
-ANISOU 7012  CA  MET B 230     7692  14154  11082   1020  -1028   -563       C  
-ATOM   7013  C   MET B 230     -32.494  15.890  16.509  1.00 88.01           C  
-ANISOU 7013  C   MET B 230     7937  14233  11268    935  -1044   -513       C  
-ATOM   7014  O   MET B 230     -31.705  16.583  15.876  1.00 87.55           O  
-ANISOU 7014  O   MET B 230     7908  14049  11308   1065  -1102   -422       O  
-ATOM   7015  CB  MET B 230     -32.608  16.547  18.914  1.00 82.24           C  
-ANISOU 7015  CB  MET B 230     7311  13330  10608   1028  -1019   -576       C  
-ATOM   7016  CG  MET B 230     -32.899  17.765  19.766  1.00 80.03           C  
-ANISOU 7016  CG  MET B 230     6985  13029  10395   1214  -1035   -571       C  
-ATOM   7017  SD  MET B 230     -31.989  17.732  21.322  1.00 75.90           S  
-ANISOU 7017  SD  MET B 230     6675  12210   9955   1198  -1022   -591       S  
-ATOM   7018  CE  MET B 230     -32.552  16.173  22.009  1.00 74.78           C  
-ANISOU 7018  CE  MET B 230     6596  12148   9669    918   -943   -705       C  
-ATOM   7019  N   LYS B 231     -32.626  14.585  16.304  1.00 86.99           N  
-ANISOU 7019  N   LYS B 231     7844  14162  11045    710   -985   -577       N  
-ATOM   7020  CA  LYS B 231     -31.834  13.906  15.286  1.00 91.05           C  
-ANISOU 7020  CA  LYS B 231     8425  14594  11574    607   -986   -544       C  
-ATOM   7021  C   LYS B 231     -32.263  14.358  13.895  1.00 97.83           C  
-ANISOU 7021  C   LYS B 231     9122  15662  12387    663  -1022   -494       C  
-ATOM   7022  O   LYS B 231     -31.572  14.108  12.908  1.00 98.90           O  
-ANISOU 7022  O   LYS B 231     9295  15732  12549    619  -1037   -449       O  
-ATOM   7023  CB  LYS B 231     -31.953  12.384  15.421  1.00 85.49           C  
-ANISOU 7023  CB  LYS B 231     7794  13910  10778    346   -901   -632       C  
-ATOM   7024  CG  LYS B 231     -31.099  11.602  14.428  1.00 77.71           C  
-ANISOU 7024  CG  LYS B 231     6886  12821   9818    224   -887   -609       C  
-ATOM   7025  CD  LYS B 231     -29.644  12.057  14.470  1.00 70.21           C  
-ANISOU 7025  CD  LYS B 231     6086  11552   9038    339   -946   -527       C  
-ATOM   7026  CE  LYS B 231     -28.810  11.395  13.381  1.00 65.39           C  
-ANISOU 7026  CE  LYS B 231     5533  10849   8462    230   -934   -507       C  
-ATOM   7027  NZ  LYS B 231     -28.786   9.911  13.513  1.00 63.83           N  
-ANISOU 7027  NZ  LYS B 231     5420  10626   8208    -11   -846   -584       N  
-ATOM   7028  N   GLN B 232     -33.405  15.032  13.825  1.00125.40           N  
-ANISOU 7028  N   GLN B 232    12431  19404  15810    760  -1038   -502       N  
-ATOM   7029  CA  GLN B 232     -33.926  15.518  12.553  1.00131.82           C  
-ANISOU 7029  CA  GLN B 232    13076  20441  16568    825  -1082   -448       C  
-ATOM   7030  C   GLN B 232     -33.312  16.855  12.151  1.00131.19           C  
-ANISOU 7030  C   GLN B 232    13000  20236  16611   1067  -1168   -327       C  
-ATOM   7031  O   GLN B 232     -33.003  17.080  10.982  1.00131.34           O  
-ANISOU 7031  O   GLN B 232    12987  20286  16630   1094  -1210   -255       O  
-ATOM   7032  CB  GLN B 232     -35.451  15.611  12.588  1.00142.20           C  
-ANISOU 7032  CB  GLN B 232    14180  22096  17753    822  -1065   -511       C  
-ATOM   7033  CG  GLN B 232     -36.143  14.259  12.579  1.00153.37           C  
-ANISOU 7033  CG  GLN B 232    15562  23692  19018    561   -976   -630       C  
-ATOM   7034  CD  GLN B 232     -37.627  14.365  12.292  1.00162.35           C  
-ANISOU 7034  CD  GLN B 232    16465  25201  20018    554   -967   -688       C  
-ATOM   7035  OE1 GLN B 232     -38.350  15.110  12.956  1.00166.39           O  
-ANISOU 7035  OE1 GLN B 232    16878  25803  20541    688   -983   -707       O  
-ATOM   7036  NE2 GLN B 232     -38.088  13.626  11.288  1.00167.14           N  
-ANISOU 7036  NE2 GLN B 232    16976  26032  20498    393   -939   -722       N  
-ATOM   7037  N   GLN B 233     -33.131  17.744  13.120  1.00114.78           N  
-ANISOU 7037  N   GLN B 233    10964  18014  14633   1236  -1190   -306       N  
-ATOM   7038  CA  GLN B 233     -32.429  18.989  12.854  1.00114.27           C  
-ANISOU 7038  CA  GLN B 233    10933  17790  14696   1458  -1257   -197       C  
-ATOM   7039  C   GLN B 233     -30.953  18.701  12.588  1.00108.63           C  
-ANISOU 7039  C   GLN B 233    10408  16785  14080   1414  -1267   -157       C  
-ATOM   7040  O   GLN B 233     -30.184  19.602  12.259  1.00108.46           O  
-ANISOU 7040  O   GLN B 233    10474  16586  14148   1555  -1299    -76       O  
-ATOM   7041  CB  GLN B 233     -32.595  19.961  14.022  1.00120.54           C  
-ANISOU 7041  CB  GLN B 233    11729  18496  15573   1633  -1262   -200       C  
-ATOM   7042  CG  GLN B 233     -32.236  19.366  15.370  1.00128.00           C  
-ANISOU 7042  CG  GLN B 233    12816  19272  16546   1532  -1210   -279       C  
-ATOM   7043  CD  GLN B 233     -32.527  20.303  16.526  1.00132.84           C  
-ANISOU 7043  CD  GLN B 233    13416  19833  17226   1684  -1205   -294       C  
-ATOM   7044  OE1 GLN B 233     -33.673  20.437  16.958  1.00135.92           O  
-ANISOU 7044  OE1 GLN B 233    13671  20425  17548   1695  -1179   -354       O  
-ATOM   7045  NE2 GLN B 233     -31.488  20.958  17.034  1.00132.96           N  
-ANISOU 7045  NE2 GLN B 233    13567  19577  17373   1797  -1226   -248       N  
-ATOM   7046  N   HIS B 234     -30.567  17.433  12.720  1.00103.47           N  
-ANISOU 7046  N   HIS B 234     9856  16065  13394   1201  -1216   -222       N  
-ATOM   7047  CA  HIS B 234     -29.177  17.023  12.529  1.00 96.95           C  
-ANISOU 7047  CA  HIS B 234     9207  14963  12666   1143  -1218   -198       C  
-ATOM   7048  C   HIS B 234     -29.023  15.562  12.118  1.00 92.92           C  
-ANISOU 7048  C   HIS B 234     8747  14473  12087    892  -1160   -261       C  
-ATOM   7049  O   HIS B 234     -28.410  14.772  12.839  1.00 92.37           O  
-ANISOU 7049  O   HIS B 234     8819  14220  12058    784  -1123   -306       O  
-ATOM   7050  CB  HIS B 234     -28.371  17.254  13.807  1.00 95.91           C  
-ANISOU 7050  CB  HIS B 234     9231  14559  12653   1208  -1219   -207       C  
-ATOM   7051  CG  HIS B 234     -28.375  18.673  14.276  1.00 94.31           C  
-ANISOU 7051  CG  HIS B 234     9001  14299  12533   1444  -1263   -152       C  
-ATOM   7052  ND1 HIS B 234     -27.648  19.664  13.653  1.00 93.36           N  
-ANISOU 7052  ND1 HIS B 234     8967  14024  12481   1577  -1285    -73       N  
-ATOM   7053  CD2 HIS B 234     -29.018  19.269  15.308  1.00 93.95           C  
-ANISOU 7053  CD2 HIS B 234     8910  14298  12489   1542  -1255   -178       C  
-ATOM   7054  CE1 HIS B 234     -27.842  20.810  14.281  1.00 92.57           C  
-ANISOU 7054  CE1 HIS B 234     8886  13870  12416   1740  -1282    -52       C  
-ATOM   7055  NE2 HIS B 234     -28.671  20.598  15.288  1.00 93.72           N  
-ANISOU 7055  NE2 HIS B 234     8945  14136  12527   1727  -1266   -115       N  
-ATOM   7056  N   LYS B 235     -29.568  15.199  10.964  1.00 74.60           N  
-ANISOU 7056  N   LYS B 235     6310  12371   9663    799  -1149   -263       N  
-ATOM   7057  CA  LYS B 235     -29.393  13.844  10.462  1.00 69.27           C  
-ANISOU 7057  CA  LYS B 235     5679  11712   8927    557  -1084   -323       C  
-ATOM   7058  C   LYS B 235     -27.949  13.634  10.039  1.00 64.87           C  
-ANISOU 7058  C   LYS B 235     5277  10875   8494    530  -1094   -288       C  
-ATOM   7059  O   LYS B 235     -27.503  12.503   9.858  1.00 62.65           O  
-ANISOU 7059  O   LYS B 235     5079  10516   8211    342  -1036   -339       O  
-ATOM   7060  CB  LYS B 235     -30.312  13.573   9.274  1.00 70.17           C  
-ANISOU 7060  CB  LYS B 235     5624  12140   8896    461  -1070   -335       C  
-ATOM   7061  CG  LYS B 235     -31.787  13.496   9.619  1.00 71.25           C  
-ANISOU 7061  CG  LYS B 235     5597  12581   8892    436  -1045   -395       C  
-ATOM   7062  CD  LYS B 235     -32.510  14.778   9.233  1.00 73.72           C  
-ANISOU 7062  CD  LYS B 235     5744  13081   9185    646  -1122   -323       C  
-ATOM   7063  CE  LYS B 235     -34.025  14.610   9.340  1.00 77.51           C  
-ANISOU 7063  CE  LYS B 235     6034  13903   9515    600  -1096   -392       C  
-ATOM   7064  NZ  LYS B 235     -34.780  15.850   8.984  1.00 79.07           N  
-ANISOU 7064  NZ  LYS B 235     6058  14288   9698    815  -1174   -321       N  
-ATOM   7065  N   ASP B 236     -27.220  14.736   9.889  1.00 84.42           N  
-ANISOU 7065  N   ASP B 236     7792  13197  11085    720  -1162   -205       N  
-ATOM   7066  CA  ASP B 236     -25.858  14.698   9.367  1.00 80.57           C  
-ANISOU 7066  CA  ASP B 236     7435  12459  10719    712  -1176   -171       C  
-ATOM   7067  C   ASP B 236     -24.807  14.638  10.467  1.00 76.16           C  
-ANISOU 7067  C   ASP B 236     7049  11590  10299    753  -1180   -182       C  
-ATOM   7068  O   ASP B 236     -23.630  14.898  10.223  1.00 74.26           O  
-ANISOU 7068  O   ASP B 236     6914  11120  10182    801  -1205   -149       O  
-ATOM   7069  CB  ASP B 236     -25.603  15.912   8.470  1.00 84.49           C  
-ANISOU 7069  CB  ASP B 236     7884  12963  11257    881  -1243    -78       C  
-ATOM   7070  CG  ASP B 236     -25.706  17.229   9.221  1.00 86.37           C  
-ANISOU 7070  CG  ASP B 236     8110  13145  11560   1122  -1297    -23       C  
-ATOM   7071  OD1 ASP B 236     -26.377  17.265  10.276  1.00 90.17           O  
-ANISOU 7071  OD1 ASP B 236     8562  13685  12013   1156  -1284    -59       O  
-ATOM   7072  OD2 ASP B 236     -25.119  18.231   8.751  1.00 88.34           O  
-ANISOU 7072  OD2 ASP B 236     8430  13266  11868   1255  -1322     46       O  
-ATOM   7073  N   ALA B 237     -25.233  14.292  11.677  1.00 67.79           N  
-ANISOU 7073  N   ALA B 237     6016  10528   9214    730  -1155   -230       N  
-ATOM   7074  CA  ALA B 237     -24.319  14.235  12.809  1.00 62.92           C  
-ANISOU 7074  CA  ALA B 237     5557   9637   8713    767  -1165   -237       C  
-ATOM   7075  C   ALA B 237     -24.667  13.090  13.746  1.00 61.05           C  
-ANISOU 7075  C   ALA B 237     5379   9402   8417    607  -1107   -312       C  
-ATOM   7076  O   ALA B 237     -25.843  12.806  13.983  1.00 62.33           O  
-ANISOU 7076  O   ALA B 237     5444   9789   8451    542  -1070   -357       O  
-ATOM   7077  CB  ALA B 237     -24.330  15.552  13.564  1.00 60.68           C  
-ANISOU 7077  CB  ALA B 237     5266   9299   8491    987  -1218   -193       C  
-ATOM   7078  N   VAL B 238     -23.634  12.435  14.269  1.00 60.52           N  
-ANISOU 7078  N   VAL B 238     5471   9082   8443    543  -1100   -325       N  
-ATOM   7079  CA  VAL B 238     -23.800  11.404  15.285  1.00 57.48           C  
-ANISOU 7079  CA  VAL B 238     5173   8649   8018    408  -1053   -383       C  
-ATOM   7080  C   VAL B 238     -24.017  12.079  16.631  1.00 57.16           C  
-ANISOU 7080  C   VAL B 238     5162   8567   7988    528  -1084   -378       C  
-ATOM   7081  O   VAL B 238     -23.272  12.991  16.990  1.00 56.34           O  
-ANISOU 7081  O   VAL B 238     5109   8301   7995    688  -1142   -330       O  
-ATOM   7082  CB  VAL B 238     -22.559  10.502  15.372  1.00 55.31           C  
-ANISOU 7082  CB  VAL B 238     5060   8106   7851    313  -1043   -388       C  
-ATOM   7083  CG1 VAL B 238     -22.770   9.406  16.402  1.00 53.25           C  
-ANISOU 7083  CG1 VAL B 238     4896   7796   7541    171   -994   -439       C  
-ATOM   7084  CG2 VAL B 238     -22.253   9.901  14.016  1.00 53.36           C  
-ANISOU 7084  CG2 VAL B 238     4785   7880   7610    196  -1007   -398       C  
-ATOM   7085  N   LEU B 239     -25.028  11.635  17.375  1.00 51.69           N  
-ANISOU 7085  N   LEU B 239     4439   8022   7179    443  -1038   -434       N  
-ATOM   7086  CA  LEU B 239     -25.424  12.324  18.604  1.00 50.92           C  
-ANISOU 7086  CA  LEU B 239     4346   7929   7074    545  -1058   -440       C  
-ATOM   7087  C   LEU B 239     -25.140  11.551  19.897  1.00 49.97           C  
-ANISOU 7087  C   LEU B 239     4378   7659   6951    447  -1038   -473       C  
-ATOM   7088  O   LEU B 239     -25.407  10.352  19.985  1.00 50.77           O  
-ANISOU 7088  O   LEU B 239     4526   7787   6976    262   -978   -522       O  
-ATOM   7089  CB  LEU B 239     -26.907  12.691  18.534  1.00 50.33           C  
-ANISOU 7089  CB  LEU B 239     4098   8159   6868    555  -1028   -478       C  
-ATOM   7090  CG  LEU B 239     -27.289  13.684  17.438  1.00 48.96           C  
-ANISOU 7090  CG  LEU B 239     3764   8143   6694    692  -1063   -432       C  
-ATOM   7091  CD1 LEU B 239     -28.779  13.951  17.470  1.00 48.89           C  
-ANISOU 7091  CD1 LEU B 239     3581   8437   6557    697  -1035   -477       C  
-ATOM   7092  CD2 LEU B 239     -26.512  14.976  17.612  1.00 46.88           C  
-ANISOU 7092  CD2 LEU B 239     3534   7712   6566    911  -1132   -359       C  
-ATOM   7093  N   CYS B 240     -24.589  12.246  20.889  1.00 68.32           N  
-ANISOU 7093  N   CYS B 240     6782   9823   9355    567  -1086   -446       N  
-ATOM   7094  CA  CYS B 240     -24.458  11.707  22.240  1.00 66.99           C  
-ANISOU 7094  CA  CYS B 240     6745   9540   9167    492  -1075   -473       C  
-ATOM   7095  C   CYS B 240     -25.444  12.428  23.137  1.00 66.62           C  
-ANISOU 7095  C   CYS B 240     6626   9639   9048    551  -1063   -508       C  
-ATOM   7096  O   CYS B 240     -25.344  13.642  23.321  1.00 65.53           O  
-ANISOU 7096  O   CYS B 240     6439   9485   8973    725  -1103   -478       O  
-ATOM   7097  CB  CYS B 240     -23.056  11.942  22.789  1.00 66.99           C  
-ANISOU 7097  CB  CYS B 240     6895   9250   9310    574  -1140   -422       C  
-ATOM   7098  SG  CYS B 240     -21.741  11.580  21.636  1.00 69.27           S  
-ANISOU 7098  SG  CYS B 240     7239   9351   9730    575  -1171   -376       S  
-ATOM   7099  N   VAL B 241     -26.392  11.692  23.701  1.00 51.72           N  
-ANISOU 7099  N   VAL B 241     4734   7888   7031    404  -1000   -577       N  
-ATOM   7100  CA  VAL B 241     -27.386  12.307  24.569  1.00 52.00           C  
-ANISOU 7100  CA  VAL B 241     4695   8069   6992    441   -978   -626       C  
-ATOM   7101  C   VAL B 241     -26.999  12.154  26.044  1.00 50.93           C  
-ANISOU 7101  C   VAL B 241     4715   7772   6863    406   -986   -636       C  
-ATOM   7102  O   VAL B 241     -26.776  11.040  26.522  1.00 50.47           O  
-ANISOU 7102  O   VAL B 241     4790   7626   6761    248   -961   -654       O  
-ATOM   7103  CB  VAL B 241     -28.776  11.694  24.322  1.00 52.42           C  
-ANISOU 7103  CB  VAL B 241     4631   8398   6889    301   -899   -709       C  
-ATOM   7104  CG1 VAL B 241     -29.854  12.541  24.983  1.00 53.72           C  
-ANISOU 7104  CG1 VAL B 241     4675   8740   6995    372   -878   -762       C  
-ATOM   7105  CG2 VAL B 241     -29.033  11.563  22.825  1.00 53.57           C  
-ANISOU 7105  CG2 VAL B 241     4648   8691   7016    294   -890   -697       C  
-ATOM   7106  N   GLU B 242     -26.888  13.273  26.757  1.00 53.57           N  
-ANISOU 7106  N   GLU B 242     5039   8063   7254    550  -1020   -623       N  
-ATOM   7107  CA  GLU B 242     -26.665  13.212  28.195  1.00 55.80           C  
-ANISOU 7107  CA  GLU B 242     5451   8227   7524    510  -1023   -641       C  
-ATOM   7108  C   GLU B 242     -27.926  12.689  28.861  1.00 58.53           C  
-ANISOU 7108  C   GLU B 242     5764   8760   7716    362   -946   -733       C  
-ATOM   7109  O   GLU B 242     -29.004  13.269  28.725  1.00 60.82           O  
-ANISOU 7109  O   GLU B 242     5895   9263   7951    402   -908   -785       O  
-ATOM   7110  CB  GLU B 242     -26.291  14.571  28.787  1.00 54.59           C  
-ANISOU 7110  CB  GLU B 242     5285   7995   7463    691  -1065   -615       C  
-ATOM   7111  CG  GLU B 242     -26.184  14.537  30.310  1.00 54.56           C  
-ANISOU 7111  CG  GLU B 242     5404   7900   7428    633  -1062   -643       C  
-ATOM   7112  CD  GLU B 242     -25.575  15.794  30.905  1.00 53.87           C  
-ANISOU 7112  CD  GLU B 242     5329   7696   7444    799  -1103   -615       C  
-ATOM   7113  OE1 GLU B 242     -26.081  16.906  30.632  1.00 53.13           O  
-ANISOU 7113  OE1 GLU B 242     5095   7708   7383    938  -1089   -625       O  
-ATOM   7114  OE2 GLU B 242     -24.584  15.664  31.656  1.00 53.87           O  
-ANISOU 7114  OE2 GLU B 242     5479   7497   7492    788  -1149   -582       O  
-ATOM   7115  N   CYS B 243     -27.782  11.581  29.576  1.00 65.88           N  
-ANISOU 7115  N   CYS B 243     6846   9607   8579    190   -923   -754       N  
-ATOM   7116  CA  CYS B 243     -28.923  10.868  30.127  1.00 67.12           C  
-ANISOU 7116  CA  CYS B 243     6994   9929   8580     15   -839   -846       C  
-ATOM   7117  C   CYS B 243     -28.555  10.315  31.494  1.00 68.01           C  
-ANISOU 7117  C   CYS B 243     7300   9889   8652    -97   -841   -852       C  
-ATOM   7118  O   CYS B 243     -28.360   9.117  31.661  1.00 68.43           O  
-ANISOU 7118  O   CYS B 243     7486   9866   8650   -257   -817   -852       O  
-ATOM   7119  CB  CYS B 243     -29.337   9.743  29.172  1.00 66.76           C  
-ANISOU 7119  CB  CYS B 243     6919   9990   8458   -132   -783   -874       C  
-ATOM   7120  SG  CYS B 243     -30.614   8.633  29.793  1.00 68.95           S  
-ANISOU 7120  SG  CYS B 243     7215  10445   8536   -381   -669   -994       S  
-ATOM   7121  N   GLY B 244     -28.447  11.204  32.472  1.00 53.92           N  
-ANISOU 7121  N   GLY B 244     5535   8056   6896    -13   -867   -853       N  
-ATOM   7122  CA  GLY B 244     -28.034  10.812  33.804  1.00 55.56           C  
-ANISOU 7122  CA  GLY B 244     5927   8117   7068   -106   -880   -850       C  
-ATOM   7123  C   GLY B 244     -26.531  10.926  33.949  1.00 57.47           C  
-ANISOU 7123  C   GLY B 244     6302   8094   7439    -16   -976   -748       C  
-ATOM   7124  O   GLY B 244     -25.958  11.988  33.705  1.00 57.03           O  
-ANISOU 7124  O   GLY B 244     6189   7979   7502    163  -1029   -706       O  
-ATOM   7125  N   TYR B 245     -25.886   9.830  34.337  1.00 58.26           N  
-ANISOU 7125  N   TYR B 245     6582   8035   7521   -137   -997   -710       N  
-ATOM   7126  CA  TYR B 245     -24.444   9.845  34.555  1.00 58.85           C  
-ANISOU 7126  CA  TYR B 245     6787   7857   7716    -60  -1092   -618       C  
-ATOM   7127  C   TYR B 245     -23.676   9.530  33.266  1.00 54.57           C  
-ANISOU 7127  C   TYR B 245     6222   7226   7287      1  -1125   -560       C  
-ATOM   7128  O   TYR B 245     -22.459   9.696  33.207  1.00 52.30           O  
-ANISOU 7128  O   TYR B 245     6005   6742   7123     93  -1204   -490       O  
-ATOM   7129  CB  TYR B 245     -24.040   8.886  35.694  1.00 67.02           C  
-ANISOU 7129  CB  TYR B 245     8033   8746   8687   -205  -1111   -594       C  
-ATOM   7130  CG  TYR B 245     -23.910   7.433  35.282  1.00 76.86           C  
-ANISOU 7130  CG  TYR B 245     9380   9928   9897   -352  -1085   -575       C  
-ATOM   7131  CD1 TYR B 245     -22.708   6.939  34.794  1.00 81.25           C  
-ANISOU 7131  CD1 TYR B 245    10019  10279  10573   -310  -1151   -494       C  
-ATOM   7132  CD2 TYR B 245     -24.984   6.556  35.382  1.00 81.16           C  
-ANISOU 7132  CD2 TYR B 245     9935  10611  10291   -534   -988   -646       C  
-ATOM   7133  CE1 TYR B 245     -22.578   5.619  34.404  1.00 85.78           C  
-ANISOU 7133  CE1 TYR B 245    10684  10783  11125   -442  -1118   -479       C  
-ATOM   7134  CE2 TYR B 245     -24.860   5.229  34.995  1.00 86.04           C  
-ANISOU 7134  CE2 TYR B 245    10649  11163  10880   -672   -953   -632       C  
-ATOM   7135  CZ  TYR B 245     -23.654   4.766  34.505  1.00 87.30           C  
-ANISOU 7135  CZ  TYR B 245    10890  11112  11167   -623  -1018   -546       C  
-ATOM   7136  OH  TYR B 245     -23.513   3.450  34.114  1.00 88.85           O  
-ANISOU 7136  OH  TYR B 245    11182  11231  11346   -757   -975   -533       O  
-ATOM   7137  N   LYS B 246     -24.384   9.092  32.230  1.00 60.16           N  
-ANISOU 7137  N   LYS B 246     6824   8083   7950    -55  -1062   -597       N  
-ATOM   7138  CA  LYS B 246     -23.716   8.633  31.018  1.00 58.23           C  
-ANISOU 7138  CA  LYS B 246     6568   7761   7797    -34  -1079   -553       C  
-ATOM   7139  C   LYS B 246     -24.324   9.230  29.742  1.00 54.31           C  
-ANISOU 7139  C   LYS B 246     5873   7450   7312     45  -1048   -577       C  
-ATOM   7140  O   LYS B 246     -25.435   9.757  29.763  1.00 54.65           O  
-ANISOU 7140  O   LYS B 246     5786   7707   7273     54  -1001   -636       O  
-ATOM   7141  CB  LYS B 246     -23.754   7.105  30.959  1.00 63.17           C  
-ANISOU 7141  CB  LYS B 246     7308   8338   8357   -227  -1031   -561       C  
-ATOM   7142  CG  LYS B 246     -25.101   6.558  30.539  1.00 70.18           C  
-ANISOU 7142  CG  LYS B 246     8101   9465   9100   -368   -924   -646       C  
-ATOM   7143  CD  LYS B 246     -25.323   5.142  31.033  1.00 78.23           C  
-ANISOU 7143  CD  LYS B 246     9267  10439  10017   -579   -863   -670       C  
-ATOM   7144  CE  LYS B 246     -26.708   4.666  30.636  1.00 84.07           C  
-ANISOU 7144  CE  LYS B 246     9903  11435  10606   -723   -748   -769       C  
-ATOM   7145  NZ  LYS B 246     -27.070   3.388  31.283  1.00 88.38           N  
-ANISOU 7145  NZ  LYS B 246    10597  11953  11031   -937   -674   -806       N  
-ATOM   7146  N   TYR B 247     -23.588   9.150  28.635  1.00 49.31           N  
-ANISOU 7146  N   TYR B 247     5216   6736   6782    101  -1077   -532       N  
-ATOM   7147  CA  TYR B 247     -24.106   9.579  27.338  1.00 44.79           C  
-ANISOU 7147  CA  TYR B 247     4470   6335   6213    158  -1051   -546       C  
-ATOM   7148  C   TYR B 247     -24.615   8.390  26.538  1.00 46.11           C  
-ANISOU 7148  C   TYR B 247     4617   6602   6299    -13   -977   -584       C  
-ATOM   7149  O   TYR B 247     -24.041   7.305  26.584  1.00 45.37           O  
-ANISOU 7149  O   TYR B 247     4654   6364   6222   -129   -966   -570       O  
-ATOM   7150  CB  TYR B 247     -23.046  10.340  26.542  1.00 37.35           C  
-ANISOU 7150  CB  TYR B 247     3503   5262   5427    322  -1120   -480       C  
-ATOM   7151  CG  TYR B 247     -22.867  11.769  26.986  1.00 32.86           C  
-ANISOU 7151  CG  TYR B 247     2888   4675   4923    509  -1170   -459       C  
-ATOM   7152  CD1 TYR B 247     -23.672  12.779  26.486  1.00 30.52           C  
-ANISOU 7152  CD1 TYR B 247     2424   4566   4606    617  -1153   -475       C  
-ATOM   7153  CD2 TYR B 247     -21.897  12.109  27.910  1.00 31.56           C  
-ANISOU 7153  CD2 TYR B 247     2845   4307   4841    575  -1231   -423       C  
-ATOM   7154  CE1 TYR B 247     -23.513  14.089  26.894  1.00 27.20           C  
-ANISOU 7154  CE1 TYR B 247     1965   4119   4251    787  -1188   -456       C  
-ATOM   7155  CE2 TYR B 247     -21.733  13.415  28.323  1.00 27.95           C  
-ANISOU 7155  CE2 TYR B 247     2346   3832   4441    736  -1264   -410       C  
-ATOM   7156  CZ  TYR B 247     -22.543  14.400  27.812  1.00 26.26           C  
-ANISOU 7156  CZ  TYR B 247     1971   3795   4211    841  -1238   -428       C  
-ATOM   7157  OH  TYR B 247     -22.380  15.703  28.223  1.00 24.74           O  
-ANISOU 7157  OH  TYR B 247     1743   3575   4083   1001  -1261   -417       O  
-ATOM   7158  N   ARG B 248     -25.692   8.598  25.794  1.00 42.39           N  
-ANISOU 7158  N   ARG B 248     3981   6382   5745    -28   -924   -633       N  
-ATOM   7159  CA  ARG B 248     -26.331   7.499  25.086  1.00 45.70           C  
-ANISOU 7159  CA  ARG B 248     4366   6933   6066   -206   -841   -685       C  
-ATOM   7160  C   ARG B 248     -26.380   7.720  23.581  1.00 45.13           C  
-ANISOU 7160  C   ARG B 248     4154   6972   6023   -164   -838   -673       C  
-ATOM   7161  O   ARG B 248     -26.676   8.820  23.109  1.00 45.11           O  
-ANISOU 7161  O   ARG B 248     4011   7085   6042    -17   -873   -656       O  
-ATOM   7162  CB  ARG B 248     -27.742   7.272  25.632  1.00 50.67           C  
-ANISOU 7162  CB  ARG B 248     4929   7796   6528   -319   -763   -775       C  
-ATOM   7163  CG  ARG B 248     -27.778   7.117  27.135  1.00 56.74           C  
-ANISOU 7163  CG  ARG B 248     5833   8473   7254   -369   -762   -793       C  
-ATOM   7164  CD  ARG B 248     -28.285   5.747  27.550  1.00 63.71           C  
-ANISOU 7164  CD  ARG B 248     6816   9381   8008   -601   -673   -854       C  
-ATOM   7165  NE  ARG B 248     -29.743   5.679  27.569  1.00 71.01           N  
-ANISOU 7165  NE  ARG B 248     7613  10588   8778   -698   -586   -958       N  
-ATOM   7166  CZ  ARG B 248     -30.480   5.155  26.597  1.00 75.17           C  
-ANISOU 7166  CZ  ARG B 248     8026  11310   9225   -800   -513  -1015       C  
-ATOM   7167  NH1 ARG B 248     -29.893   4.646  25.523  1.00 78.59           N  
-ANISOU 7167  NH1 ARG B 248     8462  11682   9717   -824   -512   -978       N  
-ATOM   7168  NH2 ARG B 248     -31.803   5.137  26.702  1.00 78.68           N  
-ANISOU 7168  NH2 ARG B 248     8351  12015   9529   -884   -438  -1116       N  
-ATOM   7169  N   PHE B 249     -26.073   6.664  22.835  1.00 52.08           N  
-ANISOU 7169  N   PHE B 249     5077   7808   6904   -298   -795   -679       N  
-ATOM   7170  CA  PHE B 249     -26.210   6.672  21.386  1.00 52.70           C  
-ANISOU 7170  CA  PHE B 249     5028   8010   6984   -306   -775   -680       C  
-ATOM   7171  C   PHE B 249     -27.505   5.967  21.010  1.00 56.71           C  
-ANISOU 7171  C   PHE B 249     5434   8788   7325   -476   -676   -768       C  
-ATOM   7172  O   PHE B 249     -27.980   5.098  21.747  1.00 55.96           O  
-ANISOU 7172  O   PHE B 249     5417   8710   7137   -629   -609   -825       O  
-ATOM   7173  CB  PHE B 249     -25.025   5.964  20.724  1.00 47.96           C  
-ANISOU 7173  CB  PHE B 249     4530   7195   6498   -355   -781   -643       C  
-ATOM   7174  CG  PHE B 249     -23.699   6.618  20.990  1.00 43.67           C  
-ANISOU 7174  CG  PHE B 249     4078   6391   6122   -194   -877   -566       C  
-ATOM   7175  CD1 PHE B 249     -23.303   7.734  20.270  1.00 41.01           C  
-ANISOU 7175  CD1 PHE B 249     3653   6057   5872    -26   -939   -519       C  
-ATOM   7176  CD2 PHE B 249     -22.844   6.113  21.952  1.00 42.32           C  
-ANISOU 7176  CD2 PHE B 249     4084   5976   6021   -214   -904   -540       C  
-ATOM   7177  CE1 PHE B 249     -22.084   8.334  20.512  1.00 37.08           C  
-ANISOU 7177  CE1 PHE B 249     3239   5324   5525    114  -1019   -460       C  
-ATOM   7178  CE2 PHE B 249     -21.622   6.709  22.194  1.00 39.47           C  
-ANISOU 7178  CE2 PHE B 249     3798   5387   5811    -70   -993   -477       C  
-ATOM   7179  CZ  PHE B 249     -21.245   7.823  21.475  1.00 37.46           C  
-ANISOU 7179  CZ  PHE B 249     3452   5141   5641     91  -1046   -442       C  
-ATOM   7180  N   PHE B 250     -28.077   6.338  19.867  1.00 62.03           N  
-ANISOU 7180  N   PHE B 250     5936   9675   7958   -454   -665   -779       N  
-ATOM   7181  CA  PHE B 250     -29.329   5.736  19.421  1.00 66.58           C  
-ANISOU 7181  CA  PHE B 250     6393  10533   8371   -611   -574   -867       C  
-ATOM   7182  C   PHE B 250     -29.317   5.355  17.943  1.00 67.46           C  
-ANISOU 7182  C   PHE B 250     6414  10751   8468   -688   -542   -871       C  
-ATOM   7183  O   PHE B 250     -28.605   5.961  17.136  1.00 67.24           O  
-ANISOU 7183  O   PHE B 250     6356  10651   8543   -571   -605   -803       O  
-ATOM   7184  CB  PHE B 250     -30.503   6.668  19.719  1.00 71.13           C  
-ANISOU 7184  CB  PHE B 250     6806  11360   8860   -517   -586   -900       C  
-ATOM   7185  CG  PHE B 250     -30.778   6.842  21.186  1.00 76.14           C  
-ANISOU 7185  CG  PHE B 250     7518  11941   9469   -501   -586   -928       C  
-ATOM   7186  CD1 PHE B 250     -31.288   5.793  21.936  1.00 78.35           C  
-ANISOU 7186  CD1 PHE B 250     7886  12245   9640   -695   -499  -1008       C  
-ATOM   7187  CD2 PHE B 250     -30.527   8.051  21.816  1.00 77.99           C  
-ANISOU 7187  CD2 PHE B 250     7744  12102   9787   -301   -665   -878       C  
-ATOM   7188  CE1 PHE B 250     -31.537   5.945  23.278  1.00 80.04           C  
-ANISOU 7188  CE1 PHE B 250     8177  12411   9824   -693   -497  -1035       C  
-ATOM   7189  CE2 PHE B 250     -30.778   8.207  23.165  1.00 79.87           C  
-ANISOU 7189  CE2 PHE B 250     8053  12295   9998   -300   -660   -909       C  
-ATOM   7190  CZ  PHE B 250     -31.284   7.152  23.894  1.00 80.65           C  
-ANISOU 7190  CZ  PHE B 250     8240  12421   9984   -498   -578   -987       C  
-ATOM   7191  N   GLY B 251     -30.116   4.348  17.600  1.00 64.22           N  
-ANISOU 7191  N   GLY B 251     5961  10514   7924   -893   -437   -956       N  
-ATOM   7192  CA  GLY B 251     -30.246   3.901  16.224  1.00 65.63           C  
-ANISOU 7192  CA  GLY B 251     6045  10828   8063   -998   -391   -977       C  
-ATOM   7193  C   GLY B 251     -28.918   3.695  15.525  1.00 64.84           C  
-ANISOU 7193  C   GLY B 251     6040  10486   8109   -984   -418   -913       C  
-ATOM   7194  O   GLY B 251     -28.001   3.098  16.086  1.00 64.41           O  
-ANISOU 7194  O   GLY B 251     6162  10162   8149  -1020   -413   -894       O  
-ATOM   7195  N   GLU B 252     -28.813   4.190  14.297  1.00 65.35           N  
-ANISOU 7195  N   GLU B 252     5987  10649   8193   -932   -449   -881       N  
-ATOM   7196  CA  GLU B 252     -27.578   4.064  13.537  1.00 65.01           C  
-ANISOU 7196  CA  GLU B 252     6020  10393   8287   -921   -472   -829       C  
-ATOM   7197  C   GLU B 252     -26.386   4.561  14.350  1.00 63.53           C  
-ANISOU 7197  C   GLU B 252     5981   9889   8269   -762   -558   -756       C  
-ATOM   7198  O   GLU B 252     -25.331   3.929  14.362  1.00 62.87           O  
-ANISOU 7198  O   GLU B 252     6035   9554   8298   -812   -547   -742       O  
-ATOM   7199  CB  GLU B 252     -27.681   4.812  12.211  1.00 63.96           C  
-ANISOU 7199  CB  GLU B 252     5734  10420   8146   -851   -514   -794       C  
-ATOM   7200  N   ASP B 253     -26.565   5.686  15.037  1.00 72.58           N  
-ANISOU 7200  N   ASP B 253     7094  11049   9433   -572   -640   -713       N  
-ATOM   7201  CA  ASP B 253     -25.511   6.248  15.877  1.00 71.33           C  
-ANISOU 7201  CA  ASP B 253     7067  10615   9422   -418   -721   -649       C  
-ATOM   7202  C   ASP B 253     -24.963   5.219  16.862  1.00 70.71           C  
-ANISOU 7202  C   ASP B 253     7172  10315   9380   -525   -687   -668       C  
-ATOM   7203  O   ASP B 253     -23.771   5.213  17.166  1.00 69.72           O  
-ANISOU 7203  O   ASP B 253     7174   9920   9397   -463   -736   -620       O  
-ATOM   7204  CB  ASP B 253     -26.022   7.476  16.631  1.00 73.21           C  
-ANISOU 7204  CB  ASP B 253     7239  10933   9644   -234   -787   -622       C  
-ATOM   7205  CG  ASP B 253     -26.471   8.581  15.702  1.00 74.22           C  
-ANISOU 7205  CG  ASP B 253     7197  11250   9755   -100   -832   -587       C  
-ATOM   7206  OD1 ASP B 253     -27.488   9.236  16.003  1.00 76.26           O  
-ANISOU 7206  OD1 ASP B 253     7336  11710   9929    -27   -841   -601       O  
-ATOM   7207  OD2 ASP B 253     -25.806   8.795  14.668  1.00 74.84           O  
-ANISOU 7207  OD2 ASP B 253     7261  11271   9905    -67   -858   -545       O  
-ATOM   7208  N   ALA B 254     -25.835   4.348  17.359  1.00 56.14           N  
-ANISOU 7208  N   ALA B 254     5338   8587   7405   -687   -603   -737       N  
-ATOM   7209  CA  ALA B 254     -25.416   3.290  18.275  1.00 56.74           C  
-ANISOU 7209  CA  ALA B 254     5594   8467   7499   -804   -563   -753       C  
-ATOM   7210  C   ALA B 254     -24.567   2.247  17.559  1.00 57.27           C  
-ANISOU 7210  C   ALA B 254     5748   8367   7646   -931   -512   -756       C  
-ATOM   7211  O   ALA B 254     -23.518   1.841  18.053  1.00 57.50           O  
-ANISOU 7211  O   ALA B 254     5930   8121   7796   -919   -540   -718       O  
-ATOM   7212  CB  ALA B 254     -26.622   2.632  18.915  1.00 58.33           C  
-ANISOU 7212  CB  ALA B 254     5786   8848   7530   -956   -475   -834       C  
-ATOM   7213  N   GLU B 255     -25.028   1.814  16.392  1.00 70.01           N  
-ANISOU 7213  N   GLU B 255     7256  10150   9194  -1054   -438   -804       N  
-ATOM   7214  CA  GLU B 255     -24.311   0.811  15.612  1.00 70.97           C  
-ANISOU 7214  CA  GLU B 255     7443  10135   9387  -1192   -372   -820       C  
-ATOM   7215  C   GLU B 255     -22.934   1.318  15.200  1.00 66.19           C  
-ANISOU 7215  C   GLU B 255     6887   9290   8973  -1056   -456   -750       C  
-ATOM   7216  O   GLU B 255     -21.953   0.574  15.236  1.00 65.69           O  
-ANISOU 7216  O   GLU B 255     6951   8980   9029  -1110   -439   -742       O  
-ATOM   7217  CB  GLU B 255     -25.132   0.380  14.394  1.00 79.24           C  
-ANISOU 7217  CB  GLU B 255     8349  11442  10315  -1349   -276   -889       C  
-ATOM   7218  CG  GLU B 255     -26.125  -0.733  14.700  1.00 92.20           C  
-ANISOU 7218  CG  GLU B 255    10003  13226  11801  -1567   -148   -980       C  
-ATOM   7219  CD  GLU B 255     -27.157  -0.927  13.606  1.00100.13           C  
-ANISOU 7219  CD  GLU B 255    10835  14552  12657  -1701    -66  -1054       C  
-ATOM   7220  OE1 GLU B 255     -26.932  -1.771  12.713  1.00104.13           O  
-ANISOU 7220  OE1 GLU B 255    11345  15049  13170  -1864     24  -1096       O  
-ATOM   7221  OE2 GLU B 255     -28.197  -0.235  13.642  1.00106.43           O  
-ANISOU 7221  OE2 GLU B 255    11489  15615  13333  -1647    -90  -1072       O  
-ATOM   7222  N   ILE B 256     -22.869   2.588  14.816  1.00 56.14           N  
-ANISOU 7222  N   ILE B 256     5513   8088   7731   -880   -545   -703       N  
-ATOM   7223  CA  ILE B 256     -21.599   3.249  14.542  1.00 51.74           C  
-ANISOU 7223  CA  ILE B 256     5001   7310   7349   -732   -631   -640       C  
-ATOM   7224  C   ILE B 256     -20.703   3.234  15.775  1.00 51.94           C  
-ANISOU 7224  C   ILE B 256     5186   7059   7488   -643   -693   -598       C  
-ATOM   7225  O   ILE B 256     -19.536   2.845  15.706  1.00 50.91           O  
-ANISOU 7225  O   ILE B 256     5161   6679   7505   -641   -710   -579       O  
-ATOM   7226  CB  ILE B 256     -21.814   4.714  14.143  1.00 47.05           C  
-ANISOU 7226  CB  ILE B 256     4281   6845   6750   -544   -714   -594       C  
-ATOM   7227  CG1 ILE B 256     -22.716   4.804  12.915  1.00 44.98           C  
-ANISOU 7227  CG1 ILE B 256     3853   6870   6368   -619   -668   -624       C  
-ATOM   7228  CG2 ILE B 256     -20.482   5.405  13.888  1.00 44.02           C  
-ANISOU 7228  CG2 ILE B 256     3954   6228   6545   -398   -796   -536       C  
-ATOM   7229  CD1 ILE B 256     -23.054   6.221  12.533  1.00 42.52           C  
-ANISOU 7229  CD1 ILE B 256     3415   6702   6038   -434   -748   -572       C  
-ATOM   7230  N   ALA B 257     -21.255   3.668  16.905  1.00 56.75           N  
-ANISOU 7230  N   ALA B 257     5811   7721   8031   -571   -729   -586       N  
-ATOM   7231  CA  ALA B 257     -20.495   3.733  18.146  1.00 57.88           C  
-ANISOU 7231  CA  ALA B 257     6099   7631   8262   -486   -795   -544       C  
-ATOM   7232  C   ALA B 257     -19.925   2.369  18.516  1.00 60.29           C  
-ANISOU 7232  C   ALA B 257     6558   7736   8614   -630   -745   -557       C  
-ATOM   7233  O   ALA B 257     -18.802   2.266  19.008  1.00 60.29           O  
-ANISOU 7233  O   ALA B 257     6679   7478   8752   -566   -804   -514       O  
-ATOM   7234  CB  ALA B 257     -21.361   4.269  19.268  1.00 57.77           C  
-ANISOU 7234  CB  ALA B 257     6071   7739   8140   -430   -817   -546       C  
-ATOM   7235  N   ALA B 258     -20.701   1.322  18.270  1.00 58.70           N  
-ANISOU 7235  N   ALA B 258     6349   7654   8299   -824   -635   -617       N  
-ATOM   7236  CA  ALA B 258     -20.269  -0.031  18.589  1.00 61.28           C  
-ANISOU 7236  CA  ALA B 258     6822   7800   8662   -972   -571   -632       C  
-ATOM   7237  C   ALA B 258     -19.138  -0.491  17.674  1.00 62.92           C  
-ANISOU 7237  C   ALA B 258     7063   7814   9031   -996   -560   -625       C  
-ATOM   7238  O   ALA B 258     -18.233  -1.211  18.099  1.00 64.53           O  
-ANISOU 7238  O   ALA B 258     7406   7764   9349  -1018   -566   -601       O  
-ATOM   7239  CB  ALA B 258     -21.441  -0.987  18.498  1.00 62.24           C  
-ANISOU 7239  CB  ALA B 258     6922   8113   8615  -1180   -442   -708       C  
-ATOM   7240  N   ARG B 259     -19.199  -0.068  16.416  1.00 75.92           N  
-ANISOU 7240  N   ARG B 259     8579   9583  10685   -993   -543   -645       N  
-ATOM   7241  CA  ARG B 259     -18.229  -0.482  15.408  1.00 77.40           C  
-ANISOU 7241  CA  ARG B 259     8777   9617  11013  -1036   -517   -655       C  
-ATOM   7242  C   ARG B 259     -16.922   0.309  15.476  1.00 75.25           C  
-ANISOU 7242  C   ARG B 259     8547   9120  10926   -852   -631   -596       C  
-ATOM   7243  O   ARG B 259     -15.846  -0.228  15.212  1.00 74.86           O  
-ANISOU 7243  O   ARG B 259     8573   8841  11029   -873   -627   -595       O  
-ATOM   7244  CB  ARG B 259     -18.845  -0.358  14.011  1.00 80.17           C  
-ANISOU 7244  CB  ARG B 259     8974  10202  11285  -1123   -450   -704       C  
-ATOM   7245  CG  ARG B 259     -17.840  -0.414  12.876  1.00 85.12           C  
-ANISOU 7245  CG  ARG B 259     9587  10698  12055  -1136   -441   -711       C  
-ATOM   7246  CD  ARG B 259     -18.532  -0.463  11.519  1.00 89.65           C  
-ANISOU 7246  CD  ARG B 259    10017  11517  12528  -1260   -362   -764       C  
-ATOM   7247  NE  ARG B 259     -19.376   0.703  11.265  1.00 91.45           N  
-ANISOU 7247  NE  ARG B 259    10105  12005  12638  -1152   -420   -740       N  
-ATOM   7248  CZ  ARG B 259     -20.700   0.713  11.390  1.00 94.32           C  
-ANISOU 7248  CZ  ARG B 259    10376  12644  12816  -1210   -382   -769       C  
-ATOM   7249  NH1 ARG B 259     -21.343  -0.382  11.770  1.00 94.37           N  
-ANISOU 7249  NH1 ARG B 259    10421  12707  12727  -1384   -280   -827       N  
-ATOM   7250  NH2 ARG B 259     -21.382   1.821  11.133  1.00 96.43           N  
-ANISOU 7250  NH2 ARG B 259    10512  13129  12997  -1093   -442   -741       N  
-ATOM   7251  N   GLU B 260     -17.024   1.585  15.836  1.00 74.82           N  
-ANISOU 7251  N   GLU B 260     8440   9132  10858   -673   -728   -553       N  
-ATOM   7252  CA  GLU B 260     -15.876   2.481  15.803  1.00 71.73           C  
-ANISOU 7252  CA  GLU B 260     8068   8561  10624   -498   -830   -506       C  
-ATOM   7253  C   GLU B 260     -15.176   2.605  17.153  1.00 68.74           C  
-ANISOU 7253  C   GLU B 260     7818   7973  10326   -388   -916   -457       C  
-ATOM   7254  O   GLU B 260     -13.956   2.772  17.213  1.00 68.22           O  
-ANISOU 7254  O   GLU B 260     7815   7681  10423   -300   -978   -432       O  
-ATOM   7255  CB  GLU B 260     -16.299   3.866  15.305  1.00 73.48           C  
-ANISOU 7255  CB  GLU B 260     8158   8962  10798   -362   -880   -486       C  
-ATOM   7256  CG  GLU B 260     -16.914   3.872  13.913  1.00 76.69           C  
-ANISOU 7256  CG  GLU B 260     8432   9580  11127   -453   -814   -523       C  
-ATOM   7257  CD  GLU B 260     -15.897   3.606  12.819  1.00 78.36           C  
-ANISOU 7257  CD  GLU B 260     8653   9647  11473   -498   -793   -541       C  
-ATOM   7258  OE1 GLU B 260     -16.312   3.443  11.652  1.00 80.03           O  
-ANISOU 7258  OE1 GLU B 260     8770  10014  11625   -603   -729   -576       O  
-ATOM   7259  OE2 GLU B 260     -14.684   3.567  13.123  1.00 78.91           O  
-ANISOU 7259  OE2 GLU B 260     8820   9454  11707   -432   -839   -524       O  
-ATOM   7260  N   LEU B 261     -15.949   2.523  18.231  1.00 60.20           N  
-ANISOU 7260  N   LEU B 261     6773   6974   9128   -399   -919   -448       N  
-ATOM   7261  CA  LEU B 261     -15.410   2.718  19.573  1.00 55.87           C  
-ANISOU 7261  CA  LEU B 261     6340   6259   8628   -300  -1003   -400       C  
-ATOM   7262  C   LEU B 261     -15.208   1.395  20.300  1.00 55.90           C  
-ANISOU 7262  C   LEU B 261     6489   6112   8638   -425   -968   -398       C  
-ATOM   7263  O   LEU B 261     -14.730   1.366  21.437  1.00 55.60           O  
-ANISOU 7263  O   LEU B 261     6565   5925   8637   -366  -1037   -353       O  
-ATOM   7264  CB  LEU B 261     -16.341   3.609  20.389  1.00 52.20           C  
-ANISOU 7264  CB  LEU B 261     5828   5971   8033   -220  -1037   -389       C  
-ATOM   7265  CG  LEU B 261     -16.791   4.909  19.729  1.00 48.61           C  
-ANISOU 7265  CG  LEU B 261     5224   5699   7548   -100  -1060   -389       C  
-ATOM   7266  CD1 LEU B 261     -17.716   5.653  20.664  1.00 47.13           C  
-ANISOU 7266  CD1 LEU B 261     5000   5666   7241    -32  -1083   -384       C  
-ATOM   7267  CD2 LEU B 261     -15.603   5.768  19.375  1.00 45.58           C  
-ANISOU 7267  CD2 LEU B 261     4842   5152   7326     56  -1140   -354       C  
-ATOM   7268  N   ASN B 262     -15.573   0.302  19.639  1.00 54.31           N  
-ANISOU 7268  N   ASN B 262     6288   5950   8399   -602   -859   -444       N  
-ATOM   7269  CA  ASN B 262     -15.444  -1.025  20.228  1.00 56.06           C  
-ANISOU 7269  CA  ASN B 262     6648   6028   8623   -734   -808   -444       C  
-ATOM   7270  C   ASN B 262     -16.189  -1.133  21.553  1.00 57.44           C  
-ANISOU 7270  C   ASN B 262     6900   6263   8660   -756   -818   -427       C  
-ATOM   7271  O   ASN B 262     -15.609  -1.450  22.590  1.00 56.87           O  
-ANISOU 7271  O   ASN B 262     6966   6005   8636   -724   -877   -377       O  
-ATOM   7272  CB  ASN B 262     -13.970  -1.394  20.400  1.00 56.18           C  
-ANISOU 7272  CB  ASN B 262     6773   5731   8840   -672   -869   -402       C  
-ATOM   7273  CG  ASN B 262     -13.174  -1.197  19.125  1.00 56.28           C  
-ANISOU 7273  CG  ASN B 262     6710   5676   8998   -646   -861   -427       C  
-ATOM   7274  OD1 ASN B 262     -12.070  -0.656  19.145  1.00 57.04           O  
-ANISOU 7274  OD1 ASN B 262     6823   5602   9247   -511   -951   -397       O  
-ATOM   7275  ND2 ASN B 262     -13.743  -1.622  18.003  1.00 56.42           N  
-ANISOU 7275  ND2 ASN B 262     6642   5835   8961   -782   -751   -489       N  
-ATOM   7276  N   ILE B 263     -17.481  -0.846  21.509  1.00 44.35           N  
-ANISOU 7276  N   ILE B 263     5148   4874   6828   -810   -764   -470       N  
-ATOM   7277  CA  ILE B 263     -18.335  -1.020  22.667  1.00 48.70           C  
-ANISOU 7277  CA  ILE B 263     5762   5511   7232   -863   -751   -473       C  
-ATOM   7278  C   ILE B 263     -19.552  -1.820  22.241  1.00 53.97           C  
-ANISOU 7278  C   ILE B 263     6382   6387   7739  -1060   -613   -551       C  
-ATOM   7279  O   ILE B 263     -19.737  -2.096  21.059  1.00 52.68           O  
-ANISOU 7279  O   ILE B 263     6125   6316   7576  -1138   -538   -597       O  
-ATOM   7280  CB  ILE B 263     -18.769   0.328  23.266  1.00 45.08           C  
-ANISOU 7280  CB  ILE B 263     5228   5185   6714   -713   -831   -457       C  
-ATOM   7281  CG1 ILE B 263     -19.551   1.147  22.240  1.00 43.50           C  
-ANISOU 7281  CG1 ILE B 263     4834   5242   6451   -679   -803   -500       C  
-ATOM   7282  CG2 ILE B 263     -17.564   1.108  23.752  1.00 44.40           C  
-ANISOU 7282  CG2 ILE B 263     5195   4895   6780   -529   -960   -387       C  
-ATOM   7283  CD1 ILE B 263     -19.971   2.510  22.753  1.00 39.25           C  
-ANISOU 7283  CD1 ILE B 263     4214   4829   5872   -523   -874   -484       C  
-ATOM   7284  N   TYR B 264     -20.376  -2.201  23.207  1.00 67.14           N  
-ANISOU 7284  N   TYR B 264     8116   8132   9264  -1149   -574   -571       N  
-ATOM   7285  CA  TYR B 264     -21.551  -3.009  22.920  1.00 75.19           C  
-ANISOU 7285  CA  TYR B 264     9101   9347  10120  -1348   -436   -655       C  
-ATOM   7286  C   TYR B 264     -22.774  -2.149  22.651  1.00 74.38           C  
-ANISOU 7286  C   TYR B 264     8821   9565   9875  -1328   -417   -711       C  
-ATOM   7287  O   TYR B 264     -23.000  -1.137  23.314  1.00 75.49           O  
-ANISOU 7287  O   TYR B 264     8923   9770   9990  -1197   -496   -689       O  
-ATOM   7288  CB  TYR B 264     -21.846  -3.967  24.076  1.00 85.98           C  
-ANISOU 7288  CB  TYR B 264    10640  10631  11398  -1476   -388   -657       C  
-ATOM   7289  CG  TYR B 264     -20.725  -4.934  24.375  1.00 97.45           C  
-ANISOU 7289  CG  TYR B 264    12275  11770  12983  -1505   -400   -598       C  
-ATOM   7290  CD1 TYR B 264     -20.460  -6.002  23.528  1.00102.30           C  
-ANISOU 7290  CD1 TYR B 264    12917  12302  13652  -1638   -298   -628       C  
-ATOM   7291  CD2 TYR B 264     -19.936  -4.785  25.507  1.00103.78           C  
-ANISOU 7291  CD2 TYR B 264    13218  12359  13855  -1402   -510   -514       C  
-ATOM   7292  CE1 TYR B 264     -19.439  -6.890  23.795  1.00109.83           C  
-ANISOU 7292  CE1 TYR B 264    14031  12962  14737  -1657   -307   -573       C  
-ATOM   7293  CE2 TYR B 264     -18.911  -5.670  25.784  1.00111.34           C  
-ANISOU 7293  CE2 TYR B 264    14336  13032  14937  -1419   -528   -454       C  
-ATOM   7294  CZ  TYR B 264     -18.667  -6.721  24.923  1.00112.92           C  
-ANISOU 7294  CZ  TYR B 264    14558  13147  15200  -1542   -426   -484       C  
-ATOM   7295  OH  TYR B 264     -17.649  -7.606  25.191  1.00118.49           O  
-ANISOU 7295  OH  TYR B 264    15419  13562  16041  -1552   -442   -424       O  
-ATOM   7296  N   CYS B 265     -23.557  -2.562  21.666  1.00 68.94           N  
-ANISOU 7296  N   CYS B 265     8019   9078   9096  -1461   -310   -787       N  
-ATOM   7297  CA  CYS B 265     -24.870  -1.983  21.446  1.00 68.06           C  
-ANISOU 7297  CA  CYS B 265     7742   9291   8828  -1478   -274   -852       C  
-ATOM   7298  C   CYS B 265     -25.889  -3.119  21.364  1.00 69.07           C  
-ANISOU 7298  C   CYS B 265     7879   9571   8795  -1717   -123   -948       C  
-ATOM   7299  O   CYS B 265     -25.566  -4.226  20.928  1.00 67.36           O  
-ANISOU 7299  O   CYS B 265     7740   9248   8604  -1863    -36   -969       O  
-ATOM   7300  CB  CYS B 265     -24.887  -1.142  20.171  1.00 66.84           C  
-ANISOU 7300  CB  CYS B 265     7402   9283   8712  -1384   -305   -851       C  
-ATOM   7301  SG  CYS B 265     -24.757  -2.121  18.676  1.00 67.49           S  
-ANISOU 7301  SG  CYS B 265     7438   9397   8810  -1555   -193   -901       S  
-ATOM   7302  N   HIS B 266     -27.118  -2.846  21.789  1.00 65.43           N  
-ANISOU 7302  N   HIS B 266     7335   9355   8169  -1760    -86  -1013       N  
-ATOM   7303  CA  HIS B 266     -28.151  -3.871  21.829  1.00 68.06           C  
-ANISOU 7303  CA  HIS B 266     7677   9845   8336  -1990     60  -1116       C  
-ATOM   7304  C   HIS B 266     -29.524  -3.241  21.680  1.00 69.46           C  
-ANISOU 7304  C   HIS B 266     7663  10373   8355  -2000     89  -1198       C  
-ATOM   7305  O   HIS B 266     -29.737  -2.094  22.071  1.00 70.61           O  
-ANISOU 7305  O   HIS B 266     7725  10597   8506  -1834     -5  -1171       O  
-ATOM   7306  CB  HIS B 266     -28.086  -4.631  23.149  1.00 68.38           C  
-ANISOU 7306  CB  HIS B 266     7928   9718   8336  -2081     89  -1111       C  
-ATOM   7307  CG  HIS B 266     -28.413  -3.785  24.337  1.00 67.43           C  
-ANISOU 7307  CG  HIS B 266     7822   9629   8170  -1971      9  -1092       C  
-ATOM   7308  ND1 HIS B 266     -29.697  -3.644  24.818  1.00 67.55           N  
-ANISOU 7308  ND1 HIS B 266     7765   9890   8012  -2050     69  -1183       N  
-ATOM   7309  CD2 HIS B 266     -27.628  -3.013  25.125  1.00 65.97           C  
-ANISOU 7309  CD2 HIS B 266     7708   9268   8090  -1792   -123  -1001       C  
-ATOM   7310  CE1 HIS B 266     -29.686  -2.833  25.861  1.00 68.57           C  
-ANISOU 7310  CE1 HIS B 266     7924   9985   8144  -1929    -19  -1148       C  
-ATOM   7311  NE2 HIS B 266     -28.443  -2.435  26.067  1.00 67.49           N  
-ANISOU 7311  NE2 HIS B 266     7875   9597   8173  -1773   -135  -1037       N  
-ATOM   7312  N   LEU B 267     -30.456  -4.000  21.116  1.00 80.06           N  
-ANISOU 7312  N   LEU B 267     8935  11926   9559  -2196    222  -1302       N  
-ATOM   7313  CA  LEU B 267     -31.806  -3.507  20.912  1.00 82.73           C  
-ANISOU 7313  CA  LEU B 267     9079  12615   9741  -2222    258  -1392       C  
-ATOM   7314  C   LEU B 267     -32.423  -3.149  22.248  1.00 84.23           C  
-ANISOU 7314  C   LEU B 267     9312  12844   9847  -2196    240  -1417       C  
-ATOM   7315  O   LEU B 267     -32.436  -3.958  23.174  1.00 83.12           O  
-ANISOU 7315  O   LEU B 267     9345  12579   9656  -2322    300  -1440       O  
-ATOM   7316  CB  LEU B 267     -32.666  -4.546  20.188  1.00 84.06           C  
-ANISOU 7316  CB  LEU B 267     9186  12987   9765  -2466    419  -1510       C  
-ATOM   7317  CG  LEU B 267     -34.079  -4.091  19.817  1.00 84.79           C  
-ANISOU 7317  CG  LEU B 267     9054  13469   9694  -2502    458  -1612       C  
-ATOM   7318  CD1 LEU B 267     -34.050  -2.721  19.153  1.00 87.32           C  
-ANISOU 7318  CD1 LEU B 267     9183  13917  10079  -2278    330  -1550       C  
-ATOM   7319  CD2 LEU B 267     -34.754  -5.115  18.917  1.00 83.84           C  
-ANISOU 7319  CD2 LEU B 267     8866  13541   9448  -2742    613  -1723       C  
-ATOM   7320  N   ASP B 268     -32.919  -1.922  22.342  1.00 85.11           N  
-ANISOU 7320  N   ASP B 268     9268  13123   9946  -2034    159  -1413       N  
-ATOM   7321  CA  ASP B 268     -33.595  -1.459  23.541  1.00 86.32           C  
-ANISOU 7321  CA  ASP B 268     9431  13345  10020  -2006    146  -1450       C  
-ATOM   7322  C   ASP B 268     -34.849  -0.686  23.159  1.00 87.31           C  
-ANISOU 7322  C   ASP B 268     9313  13821  10039  -1968    157  -1531       C  
-ATOM   7323  O   ASP B 268     -34.771   0.406  22.591  1.00 87.14           O  
-ANISOU 7323  O   ASP B 268     9141  13880  10089  -1779     64  -1479       O  
-ATOM   7324  CB  ASP B 268     -32.670  -0.580  24.374  1.00 88.32           C  
-ANISOU 7324  CB  ASP B 268     9779  13368  10412  -1802     12  -1341       C  
-ATOM   7325  CG  ASP B 268     -33.345  -0.052  25.615  1.00 91.83           C  
-ANISOU 7325  CG  ASP B 268    10232  13882  10779  -1776      1  -1382       C  
-ATOM   7326  OD1 ASP B 268     -33.989   1.015  25.531  1.00 95.87           O  
-ANISOU 7326  OD1 ASP B 268    10566  14586  11273  -1650    -40  -1405       O  
-ATOM   7327  OD2 ASP B 268     -33.241  -0.709  26.672  1.00 93.77           O  
-ANISOU 7327  OD2 ASP B 268    10662  13988  10980  -1885     36  -1393       O  
-ATOM   7328  N   HIS B 269     -36.003  -1.262  23.476  1.00 81.98           N  
-ANISOU 7328  N   HIS B 269     8602  13353   9195  -2148    272  -1658       N  
-ATOM   7329  CA  HIS B 269     -37.279  -0.698  23.065  1.00 82.15           C  
-ANISOU 7329  CA  HIS B 269     8382  13729   9102  -2140    298  -1752       C  
-ATOM   7330  C   HIS B 269     -37.385  -0.635  21.546  1.00 81.65           C  
-ANISOU 7330  C   HIS B 269     8143  13839   9042  -2130    299  -1748       C  
-ATOM   7331  O   HIS B 269     -37.706  -1.632  20.900  1.00 82.22           O  
-ANISOU 7331  O   HIS B 269     8206  14008   9024  -2328    410  -1820       O  
-ATOM   7332  CB  HIS B 269     -37.495   0.683  23.687  1.00 81.35           C  
-ANISOU 7332  CB  HIS B 269     8186  13674   9049  -1922    192  -1720       C  
-ATOM   7333  CG  HIS B 269     -37.805   0.641  25.151  1.00 81.95           C  
-ANISOU 7333  CG  HIS B 269     8382  13684   9070  -1971    217  -1768       C  
-ATOM   7334  ND1 HIS B 269     -36.838   0.442  26.113  1.00 81.55           N  
-ANISOU 7334  ND1 HIS B 269     8562  13324   9099  -1953    176  -1690       N  
-ATOM   7335  CD2 HIS B 269     -38.978   0.766  25.818  1.00 83.14           C  
-ANISOU 7335  CD2 HIS B 269     8453  14044   9091  -2043    280  -1888       C  
-ATOM   7336  CE1 HIS B 269     -37.400   0.452  27.309  1.00 81.19           C  
-ANISOU 7336  CE1 HIS B 269     8580  13300   8969  -2017    212  -1757       C  
-ATOM   7337  NE2 HIS B 269     -38.698   0.647  27.157  1.00 81.97           N  
-ANISOU 7337  NE2 HIS B 269     8494  13708   8944  -2075    279  -1881       N  
-ATOM   7338  N   ASN B 270     -37.106   0.530  20.975  1.00 81.03           N  
-ANISOU 7338  N   ASN B 270     7931  13795   9063  -1908    180  -1664       N  
-ATOM   7339  CA  ASN B 270     -37.248   0.710  19.534  1.00 80.03           C  
-ANISOU 7339  CA  ASN B 270     7629  13849   8931  -1888    169  -1654       C  
-ATOM   7340  C   ASN B 270     -35.928   0.940  18.796  1.00 77.16           C  
-ANISOU 7340  C   ASN B 270     7330  13256   8732  -1772     85  -1525       C  
-ATOM   7341  O   ASN B 270     -35.843   0.736  17.583  1.00 77.35           O  
-ANISOU 7341  O   ASN B 270     7266  13373   8752  -1816    101  -1519       O  
-ATOM   7342  CB  ASN B 270     -38.226   1.846  19.236  1.00 81.01           C  
-ANISOU 7342  CB  ASN B 270     7505  14270   9007  -1744    112  -1676       C  
-ATOM   7343  CG  ASN B 270     -39.616   1.567  19.761  1.00 84.00           C  
-ANISOU 7343  CG  ASN B 270     7784  14917   9214  -1876    206  -1822       C  
-ATOM   7344  OD1 ASN B 270     -40.491   1.112  19.026  1.00 85.52           O  
-ANISOU 7344  OD1 ASN B 270     7832  15385   9276  -2012    284  -1916       O  
-ATOM   7345  ND2 ASN B 270     -39.825   1.831  21.041  1.00 85.45           N  
-ANISOU 7345  ND2 ASN B 270     8045  15029   9395  -1845    204  -1850       N  
-ATOM   7346  N   PHE B 271     -34.902   1.361  19.529  1.00 91.64           N  
-ANISOU 7346  N   PHE B 271     9315  14797  10708  -1632     -1  -1429       N  
-ATOM   7347  CA  PHE B 271     -33.600   1.626  18.929  1.00 87.14           C  
-ANISOU 7347  CA  PHE B 271     8812  13993  10304  -1515    -82  -1314       C  
-ATOM   7348  C   PHE B 271     -32.507   0.738  19.515  1.00 85.53           C  
-ANISOU 7348  C   PHE B 271     8854  13455  10189  -1592    -63  -1276       C  
-ATOM   7349  O   PHE B 271     -32.679   0.146  20.582  1.00 84.05           O  
-ANISOU 7349  O   PHE B 271     8799  13186   9949  -1690    -13  -1315       O  
-ATOM   7350  CB  PHE B 271     -33.207   3.093  19.127  1.00 85.98           C  
-ANISOU 7350  CB  PHE B 271     8610  13788  10272  -1244   -219  -1220       C  
-ATOM   7351  CG  PHE B 271     -34.070   4.067  18.373  1.00 86.43           C  
-ANISOU 7351  CG  PHE B 271     8427  14136  10277  -1130   -258  -1228       C  
-ATOM   7352  CD1 PHE B 271     -35.054   4.793  19.027  1.00 88.03           C  
-ANISOU 7352  CD1 PHE B 271     8516  14520  10412  -1052   -270  -1272       C  
-ATOM   7353  CD2 PHE B 271     -33.890   4.266  17.013  1.00 86.14           C  
-ANISOU 7353  CD2 PHE B 271     8279  14190  10262  -1101   -283  -1189       C  
-ATOM   7354  CE1 PHE B 271     -35.841   5.694  18.337  1.00 88.19           C  
-ANISOU 7354  CE1 PHE B 271     8313  14803  10394   -935   -311  -1273       C  
-ATOM   7355  CE2 PHE B 271     -34.676   5.162  16.321  1.00 86.44           C  
-ANISOU 7355  CE2 PHE B 271     8100  14493  10249   -991   -326  -1185       C  
-ATOM   7356  CZ  PHE B 271     -35.652   5.876  16.983  1.00 87.42           C  
-ANISOU 7356  CZ  PHE B 271     8110  14793  10313   -902   -343  -1224       C  
-ATOM   7357  N   MET B 272     -31.387   0.646  18.804  1.00 73.95           N  
-ANISOU 7357  N   MET B 272     7446  11796   8857  -1548   -102  -1201       N  
-ATOM   7358  CA  MET B 272     -30.174   0.084  19.375  1.00 72.51           C  
-ANISOU 7358  CA  MET B 272     7482  11269   8800  -1555   -120  -1140       C  
-ATOM   7359  C   MET B 272     -29.647   1.123  20.354  1.00 69.30           C  
-ANISOU 7359  C   MET B 272     7131  10709   8489  -1345   -242  -1062       C  
-ATOM   7360  O   MET B 272     -30.029   2.292  20.281  1.00 70.60           O  
-ANISOU 7360  O   MET B 272     7159  11010   8654  -1184   -311  -1044       O  
-ATOM   7361  CB  MET B 272     -29.134  -0.181  18.286  1.00 75.05           C  
-ANISOU 7361  CB  MET B 272     7826  11442   9248  -1553   -132  -1089       C  
-ATOM   7362  CG  MET B 272     -29.545  -1.222  17.257  1.00 78.98           C  
-ANISOU 7362  CG  MET B 272     8273  12073   9663  -1769     -6  -1167       C  
-ATOM   7363  SD  MET B 272     -29.614  -2.892  17.936  1.00 80.75           S  
-ANISOU 7363  SD  MET B 272     8689  12167   9824  -2024    138  -1237       S  
-ATOM   7364  CE  MET B 272     -27.915  -3.134  18.431  1.00 80.66           C  
-ANISOU 7364  CE  MET B 272     8900  11717  10030  -1932     63  -1128       C  
-ATOM   7365  N   THR B 273     -28.771   0.711  21.263  1.00 62.01           N  
-ANISOU 7365  N   THR B 273     6407   9505   7648  -1344   -267  -1016       N  
-ATOM   7366  CA  THR B 273     -28.320   1.604  22.320  1.00 56.66           C  
-ANISOU 7366  CA  THR B 273     5795   8691   7044  -1172   -371   -953       C  
-ATOM   7367  C   THR B 273     -26.852   1.380  22.675  1.00 53.67           C  
-ANISOU 7367  C   THR B 273     5595   7969   6827  -1110   -439   -865       C  
-ATOM   7368  O   THR B 273     -26.326   0.288  22.493  1.00 52.21           O  
-ANISOU 7368  O   THR B 273     5527   7635   6674  -1236   -388   -864       O  
-ATOM   7369  CB  THR B 273     -29.221   1.454  23.569  1.00 56.72           C  
-ANISOU 7369  CB  THR B 273     5846   8786   6918  -1249   -329  -1015       C  
-ATOM   7370  OG1 THR B 273     -30.446   2.163  23.349  1.00 57.85           O  
-ANISOU 7370  OG1 THR B 273     5793   9236   6953  -1219   -309  -1080       O  
-ATOM   7371  CG2 THR B 273     -28.543   2.000  24.821  1.00 53.75           C  
-ANISOU 7371  CG2 THR B 273     5601   8202   6619  -1127   -419   -950       C  
-ATOM   7372  N   ALA B 274     -26.192   2.432  23.155  1.00 59.75           N  
-ANISOU 7372  N   ALA B 274     6380   8620   7703   -913   -551   -794       N  
-ATOM   7373  CA  ALA B 274     -24.826   2.342  23.667  1.00 56.01           C  
-ANISOU 7373  CA  ALA B 274     6071   7833   7379   -839   -629   -713       C  
-ATOM   7374  C   ALA B 274     -24.596   3.469  24.673  1.00 54.52           C  
-ANISOU 7374  C   ALA B 274     5899   7586   7230   -667   -725   -670       C  
-ATOM   7375  O   ALA B 274     -25.243   4.518  24.592  1.00 55.41           O  
-ANISOU 7375  O   ALA B 274     5872   7876   7307   -560   -746   -685       O  
-ATOM   7376  CB  ALA B 274     -23.823   2.426  22.533  1.00 55.78           C  
-ANISOU 7376  CB  ALA B 274     6017   7682   7495   -772   -663   -668       C  
-ATOM   7377  N   SER B 275     -23.680   3.262  25.616  1.00 57.56           N  
-ANISOU 7377  N   SER B 275     6453   7727   7691   -639   -783   -615       N  
-ATOM   7378  CA  SER B 275     -23.467   4.235  26.684  1.00 55.27           C  
-ANISOU 7378  CA  SER B 275     6194   7381   7426   -502   -865   -581       C  
-ATOM   7379  C   SER B 275     -21.997   4.479  26.980  1.00 52.77           C  
-ANISOU 7379  C   SER B 275     5990   6786   7274   -382   -967   -498       C  
-ATOM   7380  O   SER B 275     -21.158   3.593  26.806  1.00 50.99           O  
-ANISOU 7380  O   SER B 275     5876   6372   7126   -440   -972   -466       O  
-ATOM   7381  CB  SER B 275     -24.164   3.786  27.971  1.00 57.00           C  
-ANISOU 7381  CB  SER B 275     6508   7638   7511   -619   -827   -619       C  
-ATOM   7382  OG  SER B 275     -25.560   3.644  27.777  1.00 59.70           O  
-ANISOU 7382  OG  SER B 275     6737   8248   7698   -726   -732   -709       O  
-ATOM   7383  N   ILE B 276     -21.696   5.691  27.435  1.00 47.83           N  
-ANISOU 7383  N   ILE B 276     5331   6137   6705   -214  -1045   -467       N  
-ATOM   7384  CA  ILE B 276     -20.377   6.023  27.965  1.00 45.05           C  
-ANISOU 7384  CA  ILE B 276     5088   5539   6491   -100  -1144   -398       C  
-ATOM   7385  C   ILE B 276     -20.529   6.963  29.162  1.00 46.94           C  
-ANISOU 7385  C   ILE B 276     5343   5792   6699    -11  -1191   -393       C  
-ATOM   7386  O   ILE B 276     -21.268   7.944  29.096  1.00 47.05           O  
-ANISOU 7386  O   ILE B 276     5229   5978   6671     66  -1177   -425       O  
-ATOM   7387  CB  ILE B 276     -19.488   6.698  26.909  1.00 42.43           C  
-ANISOU 7387  CB  ILE B 276     4683   5127   6311     43  -1194   -363       C  
-ATOM   7388  CG1 ILE B 276     -20.130   7.992  26.418  1.00 39.79           C  
-ANISOU 7388  CG1 ILE B 276     4180   4982   5958    170  -1193   -382       C  
-ATOM   7389  CG2 ILE B 276     -19.250   5.767  25.745  1.00 41.34           C  
-ANISOU 7389  CG2 ILE B 276     4535   4960   6211    -53  -1146   -372       C  
-ATOM   7390  CD1 ILE B 276     -19.210   8.848  25.592  1.00 39.99           C  
-ANISOU 7390  CD1 ILE B 276     4152   4913   6129    327  -1251   -343       C  
-ATOM   7391  N   PRO B 277     -19.851   6.655  30.274  1.00 40.45           N  
-ANISOU 7391  N   PRO B 277     4679   4793   5896    -27  -1246   -353       N  
-ATOM   7392  CA  PRO B 277     -19.869   7.591  31.399  1.00 41.17           C  
-ANISOU 7392  CA  PRO B 277     4789   4886   5969     55  -1293   -348       C  
-ATOM   7393  C   PRO B 277     -19.416   8.951  30.892  1.00 41.65           C  
-ANISOU 7393  C   PRO B 277     4736   4947   6142    251  -1341   -333       C  
-ATOM   7394  O   PRO B 277     -18.539   8.987  30.035  1.00 40.39           O  
-ANISOU 7394  O   PRO B 277     4564   4674   6107    322  -1377   -299       O  
-ATOM   7395  CB  PRO B 277     -18.842   6.992  32.369  1.00 41.29           C  
-ANISOU 7395  CB  PRO B 277     4992   4669   6027     26  -1365   -289       C  
-ATOM   7396  CG  PRO B 277     -18.073   5.969  31.575  1.00 39.27           C  
-ANISOU 7396  CG  PRO B 277     4794   4264   5861    -20  -1370   -254       C  
-ATOM   7397  CD  PRO B 277     -19.025   5.470  30.546  1.00 41.16           C  
-ANISOU 7397  CD  PRO B 277     4933   4675   6030   -117  -1268   -309       C  
-ATOM   7398  N   THR B 278     -19.995  10.042  31.387  1.00 46.92           N  
-ANISOU 7398  N   THR B 278     5326   5733   6770    331  -1336   -361       N  
-ATOM   7399  CA  THR B 278     -19.666  11.356  30.835  1.00 47.21           C  
-ANISOU 7399  CA  THR B 278     5250   5779   6908    516  -1367   -349       C  
-ATOM   7400  C   THR B 278     -18.195  11.720  31.030  1.00 48.13           C  
-ANISOU 7400  C   THR B 278     5454   5664   7171    625  -1456   -292       C  
-ATOM   7401  O   THR B 278     -17.643  12.529  30.278  1.00 47.90           O  
-ANISOU 7401  O   THR B 278     5355   5595   7250    760  -1482   -275       O  
-ATOM   7402  CB  THR B 278     -20.552  12.488  31.396  1.00 46.99           C  
-ANISOU 7402  CB  THR B 278     5124   5909   6820    587  -1338   -392       C  
-ATOM   7403  OG1 THR B 278     -20.155  12.786  32.735  1.00 49.09           O  
-ANISOU 7403  OG1 THR B 278     5495   6075   7081    593  -1376   -385       O  
-ATOM   7404  CG2 THR B 278     -22.015  12.090  31.372  1.00 48.48           C  
-ANISOU 7404  CG2 THR B 278     5232   6329   6861    470  -1251   -458       C  
-ATOM   7405  N   HIS B 279     -17.552  11.114  32.021  1.00 57.50           N  
-ANISOU 7405  N   HIS B 279     6792   6699   8357    562  -1504   -264       N  
-ATOM   7406  CA  HIS B 279     -16.138  11.377  32.248  1.00 57.08           C  
-ANISOU 7406  CA  HIS B 279     6820   6430   8438    657  -1593   -214       C  
-ATOM   7407  C   HIS B 279     -15.289  10.760  31.130  1.00 55.26           C  
-ANISOU 7407  C   HIS B 279     6597   6074   8324    665  -1613   -186       C  
-ATOM   7408  O   HIS B 279     -14.057  10.843  31.143  1.00 54.49           O  
-ANISOU 7408  O   HIS B 279     6559   5792   8353    737  -1684   -150       O  
-ATOM   7409  CB  HIS B 279     -15.703  10.875  33.631  1.00 60.75           C  
-ANISOU 7409  CB  HIS B 279     7442   6778   8864    587  -1646   -187       C  
-ATOM   7410  CG  HIS B 279     -15.424   9.406  33.688  1.00 64.61           C  
-ANISOU 7410  CG  HIS B 279     8053   7160   9335    453  -1655   -154       C  
-ATOM   7411  ND1 HIS B 279     -16.377   8.479  34.051  1.00 67.55           N  
-ANISOU 7411  ND1 HIS B 279     8474   7626   9567    291  -1593   -176       N  
-ATOM   7412  CD2 HIS B 279     -14.293   8.704  33.437  1.00 66.39           C  
-ANISOU 7412  CD2 HIS B 279     8364   7188   9672    458  -1715   -105       C  
-ATOM   7413  CE1 HIS B 279     -15.846   7.269  34.017  1.00 69.54           C  
-ANISOU 7413  CE1 HIS B 279     8843   7737   9843    202  -1611   -136       C  
-ATOM   7414  NE2 HIS B 279     -14.584   7.378  33.648  1.00 69.01           N  
-ANISOU 7414  NE2 HIS B 279     8797   7492   9932    304  -1687    -91       N  
-ATOM   7415  N   ARG B 280     -15.959  10.148  30.158  1.00 53.18           N  
-ANISOU 7415  N   ARG B 280     6268   5919   8019    586  -1546   -209       N  
-ATOM   7416  CA  ARG B 280     -15.278   9.543  29.027  1.00 50.81           C  
-ANISOU 7416  CA  ARG B 280     5964   5520   7820    574  -1547   -194       C  
-ATOM   7417  C   ARG B 280     -15.773  10.154  27.734  1.00 50.09           C  
-ANISOU 7417  C   ARG B 280     5718   5574   7739    630  -1499   -219       C  
-ATOM   7418  O   ARG B 280     -15.527   9.627  26.652  1.00 49.91           O  
-ANISOU 7418  O   ARG B 280     5667   5528   7767    592  -1476   -221       O  
-ATOM   7419  CB  ARG B 280     -15.527   8.043  29.006  1.00 50.85           C  
-ANISOU 7419  CB  ARG B 280     6052   5502   7768    400  -1504   -195       C  
-ATOM   7420  CG  ARG B 280     -14.934   7.326  30.178  1.00 49.65           C  
-ANISOU 7420  CG  ARG B 280     6065   5184   7615    344  -1558   -156       C  
-ATOM   7421  CD  ARG B 280     -13.440   7.257  30.045  1.00 47.57           C  
-ANISOU 7421  CD  ARG B 280     5867   4685   7522    427  -1642   -110       C  
-ATOM   7422  NE  ARG B 280     -13.059   6.277  29.037  1.00 46.93           N  
-ANISOU 7422  NE  ARG B 280     5795   4521   7516    358  -1610   -110       N  
-ATOM   7423  CZ  ARG B 280     -11.813   5.867  28.829  1.00 48.10           C  
-ANISOU 7423  CZ  ARG B 280     6007   4456   7814    394  -1667    -79       C  
-ATOM   7424  NH1 ARG B 280     -10.826   6.358  29.567  1.00 49.16           N  
-ANISOU 7424  NH1 ARG B 280     6200   4445   8033    499  -1765    -43       N  
-ATOM   7425  NH2 ARG B 280     -11.558   4.965  27.889  1.00 48.45           N  
-ANISOU 7425  NH2 ARG B 280     6051   4434   7924    320  -1622    -89       N  
-ATOM   7426  N   LEU B 281     -16.483  11.267  27.846  1.00 49.13           N  
-ANISOU 7426  N   LEU B 281     5496   5603   7569    719  -1484   -239       N  
-ATOM   7427  CA  LEU B 281     -16.987  11.949  26.666  1.00 47.08           C  
-ANISOU 7427  CA  LEU B 281     5087   5488   7313    788  -1448   -253       C  
-ATOM   7428  C   LEU B 281     -15.853  12.300  25.704  1.00 44.95           C  
-ANISOU 7428  C   LEU B 281     4809   5075   7194    883  -1487   -227       C  
-ATOM   7429  O   LEU B 281     -15.818  11.805  24.581  1.00 43.64           O  
-ANISOU 7429  O   LEU B 281     4602   4930   7048    831  -1458   -231       O  
-ATOM   7430  CB  LEU B 281     -17.751  13.213  27.062  1.00 47.24           C  
-ANISOU 7430  CB  LEU B 281     5011   5653   7284    898  -1436   -269       C  
-ATOM   7431  CG  LEU B 281     -18.398  13.965  25.898  1.00 42.06           C  
-ANISOU 7431  CG  LEU B 281     4196   5164   6621    978  -1402   -276       C  
-ATOM   7432  CD1 LEU B 281     -19.375  13.059  25.162  1.00 40.95           C  
-ANISOU 7432  CD1 LEU B 281     3986   5200   6373    840  -1338   -306       C  
-ATOM   7433  CD2 LEU B 281     -19.090  15.219  26.401  1.00 40.96           C  
-ANISOU 7433  CD2 LEU B 281     3971   5143   6449   1097  -1392   -289       C  
-ATOM   7434  N   PHE B 282     -14.921  13.139  26.157  1.00 48.35           N  
-ANISOU 7434  N   PHE B 282     5282   5363   7726   1010  -1547   -206       N  
-ATOM   7435  CA  PHE B 282     -13.846  13.646  25.302  1.00 47.01           C  
-ANISOU 7435  CA  PHE B 282     5102   5062   7699   1111  -1581   -190       C  
-ATOM   7436  C   PHE B 282     -13.151  12.543  24.507  1.00 46.90           C  
-ANISOU 7436  C   PHE B 282     5133   4930   7755   1018  -1581   -188       C  
-ATOM   7437  O   PHE B 282     -12.805  12.731  23.340  1.00 45.63           O  
-ANISOU 7437  O   PHE B 282     4918   4757   7664   1046  -1569   -192       O  
-ATOM   7438  CB  PHE B 282     -12.819  14.435  26.119  1.00 44.39           C  
-ANISOU 7438  CB  PHE B 282     4852   4569   7446   1198  -1634   -187       C  
-ATOM   7439  CG  PHE B 282     -11.878  13.572  26.910  1.00 43.52           C  
-ANISOU 7439  CG  PHE B 282     4870   4273   7394   1148  -1695   -169       C  
-ATOM   7440  CD1 PHE B 282     -10.608  13.297  26.440  1.00 42.76           C  
-ANISOU 7440  CD1 PHE B 282     4838   4019   7390   1092  -1714   -189       C  
-ATOM   7441  CD2 PHE B 282     -12.261  13.039  28.129  1.00 44.70           C  
-ANISOU 7441  CD2 PHE B 282     5090   4429   7464   1089  -1714   -155       C  
-ATOM   7442  CE1 PHE B 282      -9.737  12.499  27.169  1.00 42.75           C  
-ANISOU 7442  CE1 PHE B 282     4943   3859   7440   1044  -1775   -172       C  
-ATOM   7443  CE2 PHE B 282     -11.395  12.244  28.861  1.00 42.73           C  
-ANISOU 7443  CE2 PHE B 282     4968   4007   7259   1040  -1774   -131       C  
-ATOM   7444  CZ  PHE B 282     -10.131  11.974  28.380  1.00 41.68           C  
-ANISOU 7444  CZ  PHE B 282     4878   3698   7260   1053  -1815   -127       C  
-ATOM   7445  N   VAL B 283     -12.949  11.391  25.134  1.00 47.10           N  
-ANISOU 7445  N   VAL B 283     5263   4867   7767    903  -1590   -183       N  
-ATOM   7446  CA  VAL B 283     -12.282  10.289  24.457  1.00 47.47           C  
-ANISOU 7446  CA  VAL B 283     5358   4789   7891    811  -1582   -184       C  
-ATOM   7447  C   VAL B 283     -13.076   9.838  23.247  1.00 49.02           C  
-ANISOU 7447  C   VAL B 283     5461   5139   8025    718  -1502   -210       C  
-ATOM   7448  O   VAL B 283     -12.587   9.881  22.121  1.00 50.09           O  
-ANISOU 7448  O   VAL B 283     5553   5235   8243    729  -1491   -219       O  
-ATOM   7449  CB  VAL B 283     -12.086   9.078  25.375  1.00 47.60           C  
-ANISOU 7449  CB  VAL B 283     5503   4695   7886    698  -1597   -169       C  
-ATOM   7450  CG1 VAL B 283     -11.474   7.927  24.595  1.00 44.47           C  
-ANISOU 7450  CG1 VAL B 283     5148   4174   7576    602  -1575   -174       C  
-ATOM   7451  CG2 VAL B 283     -11.207   9.450  26.549  1.00 46.40           C  
-ANISOU 7451  CG2 VAL B 283     5447   4386   7796    783  -1686   -138       C  
-ATOM   7452  N   HIS B 284     -14.307   9.409  23.482  1.00 43.24           N  
-ANISOU 7452  N   HIS B 284     4697   4588   7143    618  -1445   -228       N  
-ATOM   7453  CA  HIS B 284     -15.111   8.831  22.419  1.00 44.49           C  
-ANISOU 7453  CA  HIS B 284     4772   4906   7227    505  -1365   -259       C  
-ATOM   7454  C   HIS B 284     -15.553   9.849  21.379  1.00 44.25           C  
-ANISOU 7454  C   HIS B 284     4597   5033   7183    592  -1351   -264       C  
-ATOM   7455  O   HIS B 284     -15.906   9.483  20.260  1.00 45.64           O  
-ANISOU 7455  O   HIS B 284     4700   5311   7331    516  -1298   -284       O  
-ATOM   7456  CB  HIS B 284     -16.314   8.096  23.002  1.00 46.83           C  
-ANISOU 7456  CB  HIS B 284     5073   5359   7362    369  -1305   -285       C  
-ATOM   7457  CG  HIS B 284     -15.938   6.939  23.871  1.00 48.08           C  
-ANISOU 7457  CG  HIS B 284     5380   5365   7522    260  -1307   -276       C  
-ATOM   7458  ND1 HIS B 284     -15.489   5.740  23.360  1.00 48.23           N  
-ANISOU 7458  ND1 HIS B 284     5460   5274   7591    138  -1270   -283       N  
-ATOM   7459  CD2 HIS B 284     -15.931   6.801  25.218  1.00 48.41           C  
-ANISOU 7459  CD2 HIS B 284     5525   5343   7524    253  -1342   -258       C  
-ATOM   7460  CE1 HIS B 284     -15.225   4.913  24.355  1.00 49.36           C  
-ANISOU 7460  CE1 HIS B 284     5741   5287   7727     70  -1284   -264       C  
-ATOM   7461  NE2 HIS B 284     -15.485   5.531  25.492  1.00 49.01           N  
-ANISOU 7461  NE2 HIS B 284     5727   5271   7624    135  -1331   -246       N  
-ATOM   7462  N   VAL B 285     -15.541  11.124  21.744  1.00 53.03           N  
-ANISOU 7462  N   VAL B 285     5670   6166   8312    749  -1394   -245       N  
-ATOM   7463  CA  VAL B 285     -15.857  12.164  20.779  1.00 50.98           C  
-ANISOU 7463  CA  VAL B 285     5287   6030   8053    851  -1388   -238       C  
-ATOM   7464  C   VAL B 285     -14.683  12.355  19.829  1.00 50.14           C  
-ANISOU 7464  C   VAL B 285     5197   5765   8088    899  -1413   -227       C  
-ATOM   7465  O   VAL B 285     -14.863  12.438  18.616  1.00 49.72           O  
-ANISOU 7465  O   VAL B 285     5065   5799   8029    880  -1383   -231       O  
-ATOM   7466  CB  VAL B 285     -16.200  13.496  21.452  1.00 50.43           C  
-ANISOU 7466  CB  VAL B 285     5174   6020   7966   1007  -1417   -222       C  
-ATOM   7467  CG1 VAL B 285     -16.274  14.602  20.416  1.00 48.65           C  
-ANISOU 7467  CG1 VAL B 285     4842   5871   7772   1131  -1419   -203       C  
-ATOM   7468  CG2 VAL B 285     -17.513  13.376  22.182  1.00 50.20           C  
-ANISOU 7468  CG2 VAL B 285     5098   6184   7791    954  -1380   -245       C  
-ATOM   7469  N   ARG B 286     -13.477  12.406  20.380  1.00 54.20           N  
-ANISOU 7469  N   ARG B 286     5816   6051   8727    953  -1467   -217       N  
-ATOM   7470  CA  ARG B 286     -12.292  12.605  19.562  1.00 52.89           C  
-ANISOU 7470  CA  ARG B 286     5671   5721   8702    996  -1489   -218       C  
-ATOM   7471  C   ARG B 286     -12.010  11.380  18.697  1.00 54.00           C  
-ANISOU 7471  C   ARG B 286     5827   5814   8875    848  -1448   -242       C  
-ATOM   7472  O   ARG B 286     -11.502  11.508  17.587  1.00 54.54           O  
-ANISOU 7472  O   ARG B 286     5863   5844   9014    847  -1434   -254       O  
-ATOM   7473  CB  ARG B 286     -11.088  12.949  20.433  1.00 54.50           C  
-ANISOU 7473  CB  ARG B 286     6015   5720   8974    997  -1525   -238       C  
-ATOM   7474  CG  ARG B 286     -11.268  14.226  21.229  1.00 56.98           C  
-ANISOU 7474  CG  ARG B 286     6345   6079   9224   1070  -1531   -244       C  
-ATOM   7475  CD  ARG B 286     -10.224  14.358  22.326  1.00 59.87           C  
-ANISOU 7475  CD  ARG B 286     6820   6291   9638   1057  -1581   -261       C  
-ATOM   7476  NE  ARG B 286      -8.917  14.767  21.822  1.00 62.08           N  
-ANISOU 7476  NE  ARG B 286     7136   6456   9997   1018  -1593   -301       N  
-ATOM   7477  CZ  ARG B 286      -8.536  16.032  21.676  1.00 64.06           C  
-ANISOU 7477  CZ  ARG B 286     7385   6718  10236   1054  -1582   -328       C  
-ATOM   7478  NH1 ARG B 286      -9.363  17.019  21.987  1.00 61.50           N  
-ANISOU 7478  NH1 ARG B 286     7033   6502   9832   1132  -1552   -318       N  
-ATOM   7479  NH2 ARG B 286      -7.325  16.312  21.215  1.00 66.06           N  
-ANISOU 7479  NH2 ARG B 286     7657   6880  10561   1012  -1599   -366       N  
-ATOM   7480  N   ARG B 287     -12.345  10.195  19.196  1.00 44.08           N  
-ANISOU 7480  N   ARG B 287     4624   4558   7565    714  -1420   -253       N  
-ATOM   7481  CA  ARG B 287     -12.204   8.978  18.401  1.00 45.84           C  
-ANISOU 7481  CA  ARG B 287     4861   4749   7809    557  -1363   -282       C  
-ATOM   7482  C   ARG B 287     -13.134   9.017  17.195  1.00 46.99           C  
-ANISOU 7482  C   ARG B 287     4883   5114   7856    488  -1295   -301       C  
-ATOM   7483  O   ARG B 287     -12.740   8.654  16.090  1.00 47.64           O  
-ANISOU 7483  O   ARG B 287     4942   5166   7993    419  -1259   -325       O  
-ATOM   7484  CB  ARG B 287     -12.504   7.736  19.240  1.00 47.70           C  
-ANISOU 7484  CB  ARG B 287     5182   4951   7990    427  -1337   -286       C  
-ATOM   7485  CG  ARG B 287     -11.529   7.505  20.379  1.00 48.82           C  
-ANISOU 7485  CG  ARG B 287     5453   4866   8229    476  -1408   -261       C  
-ATOM   7486  CD  ARG B 287     -11.937   6.300  21.203  1.00 51.57           C  
-ANISOU 7486  CD  ARG B 287     5892   5197   8506    345  -1380   -257       C  
-ATOM   7487  NE  ARG B 287     -11.554   5.041  20.573  1.00 53.01           N  
-ANISOU 7487  NE  ARG B 287     6116   5276   8749    208  -1325   -280       N  
-ATOM   7488  CZ  ARG B 287     -11.953   3.846  20.994  1.00 53.87           C  
-ANISOU 7488  CZ  ARG B 287     6299   5373   8798     67  -1275   -284       C  
-ATOM   7489  NH1 ARG B 287     -12.760   3.746  22.040  1.00 54.64           N  
-ANISOU 7489  NH1 ARG B 287     6437   5561   8763     39  -1275   -269       N  
-ATOM   7490  NH2 ARG B 287     -11.551   2.750  20.366  1.00 54.49           N  
-ANISOU 7490  NH2 ARG B 287     6412   5344   8946    -51  -1217   -308       N  
-ATOM   7491  N   LEU B 288     -14.370   9.454  17.414  1.00 50.85           N  
-ANISOU 7491  N   LEU B 288     5291   5830   8199    502  -1277   -295       N  
-ATOM   7492  CA  LEU B 288     -15.344   9.552  16.333  1.00 52.16           C  
-ANISOU 7492  CA  LEU B 288     5329   6232   8257    446  -1222   -310       C  
-ATOM   7493  C   LEU B 288     -14.980  10.662  15.347  1.00 52.41           C  
-ANISOU 7493  C   LEU B 288     5290   6279   8346    565  -1251   -288       C  
-ATOM   7494  O   LEU B 288     -15.136  10.503  14.136  1.00 51.56           O  
-ANISOU 7494  O   LEU B 288     5113   6261   8215    495  -1211   -301       O  
-ATOM   7495  CB  LEU B 288     -16.754   9.783  16.888  1.00 53.20           C  
-ANISOU 7495  CB  LEU B 288     5384   6603   8225    444  -1202   -312       C  
-ATOM   7496  CG  LEU B 288     -17.556   8.539  17.260  1.00 52.94           C  
-ANISOU 7496  CG  LEU B 288     5372   6665   8079    264  -1133   -352       C  
-ATOM   7497  CD1 LEU B 288     -19.015   8.886  17.481  1.00 52.84           C  
-ANISOU 7497  CD1 LEU B 288     5249   6927   7902    260  -1105   -368       C  
-ATOM   7498  CD2 LEU B 288     -17.428   7.530  16.150  1.00 54.64           C  
-ANISOU 7498  CD2 LEU B 288     5574   6887   8298    102  -1064   -387       C  
-ATOM   7499  N   VAL B 289     -14.505  11.787  15.874  1.00 55.09           N  
-ANISOU 7499  N   VAL B 289     5650   6530   8752    738  -1314   -256       N  
-ATOM   7500  CA  VAL B 289     -14.151  12.934  15.048  1.00 55.73           C  
-ANISOU 7500  CA  VAL B 289     5678   6611   8885    863  -1340   -231       C  
-ATOM   7501  C   VAL B 289     -13.021  12.584  14.090  1.00 56.41           C  
-ANISOU 7501  C   VAL B 289     5806   6533   9094    811  -1332   -252       C  
-ATOM   7502  O   VAL B 289     -12.959  13.102  12.974  1.00 56.68           O  
-ANISOU 7502  O   VAL B 289     5780   6621   9133    831  -1323   -245       O  
-ATOM   7503  CB  VAL B 289     -13.749  14.149  15.913  1.00 54.93           C  
-ANISOU 7503  CB  VAL B 289     5640   6407   8822   1019  -1382   -211       C  
-ATOM   7504  CG1 VAL B 289     -12.983  15.165  15.088  1.00 55.33           C  
-ANISOU 7504  CG1 VAL B 289     5747   6361   8913   1051  -1367   -218       C  
-ATOM   7505  CG2 VAL B 289     -14.981  14.784  16.538  1.00 55.55           C  
-ANISOU 7505  CG2 VAL B 289     5646   6683   8779   1088  -1378   -192       C  
-ATOM   7506  N   ALA B 290     -12.141  11.689  14.532  1.00 47.19           N  
-ANISOU 7506  N   ALA B 290     4740   5166   8024    742  -1336   -279       N  
-ATOM   7507  CA  ALA B 290     -11.001  11.255  13.732  1.00 49.44           C  
-ANISOU 7507  CA  ALA B 290     5068   5273   8443    685  -1324   -311       C  
-ATOM   7508  C   ALA B 290     -11.432  10.344  12.585  1.00 50.95           C  
-ANISOU 7508  C   ALA B 290     5205   5574   8579    509  -1247   -344       C  
-ATOM   7509  O   ALA B 290     -10.846  10.378  11.501  1.00 50.23           O  
-ANISOU 7509  O   ALA B 290     5099   5432   8556    471  -1225   -367       O  
-ATOM   7510  CB  ALA B 290      -9.972  10.558  14.608  1.00 49.54           C  
-ANISOU 7510  CB  ALA B 290     5200   5044   8580    672  -1355   -327       C  
-ATOM   7511  N   LYS B 291     -12.454   9.528  12.823  1.00 69.24           N  
-ANISOU 7511  N   LYS B 291     7494   8044  10770    391  -1199   -353       N  
-ATOM   7512  CA  LYS B 291     -12.998   8.675  11.771  1.00 71.26           C  
-ANISOU 7512  CA  LYS B 291     7689   8435  10953    214  -1116   -390       C  
-ATOM   7513  C   LYS B 291     -13.666   9.512  10.687  1.00 69.83           C  
-ANISOU 7513  C   LYS B 291     7386   8468  10678    243  -1109   -372       C  
-ATOM   7514  O   LYS B 291     -14.003   9.003   9.619  1.00 71.69           O  
-ANISOU 7514  O   LYS B 291     7560   8820  10858    106  -1047   -401       O  
-ATOM   7515  CB  LYS B 291     -14.001   7.675  12.342  1.00 77.73           C  
-ANISOU 7515  CB  LYS B 291     8506   9381  11647     84  -1062   -409       C  
-ATOM   7516  CG  LYS B 291     -13.398   6.676  13.311  1.00 84.32           C  
-ANISOU 7516  CG  LYS B 291     9468  10009  12560     28  -1060   -422       C  
-ATOM   7517  CD  LYS B 291     -12.260   5.910  12.665  1.00 91.34           C  
-ANISOU 7517  CD  LYS B 291    10416  10688  13601    -59  -1028   -460       C  
-ATOM   7518  CE  LYS B 291     -11.647   4.920  13.644  1.00 96.70           C  
-ANISOU 7518  CE  LYS B 291    11223  11154  14366   -101  -1033   -464       C  
-ATOM   7519  NZ  LYS B 291     -10.439   4.250  13.077  1.00 99.99           N  
-ANISOU 7519  NZ  LYS B 291    11694  11342  14955   -162  -1010   -500       N  
-ATOM   7520  N   GLY B 292     -13.863  10.795  10.972  1.00 47.53           N  
-ANISOU 7520  N   GLY B 292     4527   5695   7836    421  -1171   -323       N  
-ATOM   7521  CA  GLY B 292     -14.444  11.709  10.007  1.00 45.67           C  
-ANISOU 7521  CA  GLY B 292     4183   5646   7522    478  -1177   -291       C  
-ATOM   7522  C   GLY B 292     -15.894  12.047  10.287  1.00 46.98           C  
-ANISOU 7522  C   GLY B 292     4245   6083   7524    509  -1177   -264       C  
-ATOM   7523  O   GLY B 292     -16.499  12.858   9.587  1.00 49.70           O  
-ANISOU 7523  O   GLY B 292     4491   6600   7794    575  -1191   -228       O  
-ATOM   7524  N   TYR B 293     -16.454  11.429  11.321  1.00 60.59           N  
-ANISOU 7524  N   TYR B 293     6354   8627   8041   2349   -867   -421       N  
-ATOM   7525  CA  TYR B 293     -17.847  11.659  11.680  1.00 58.22           C  
-ANISOU 7525  CA  TYR B 293     6077   8386   7659   2434   -896   -357       C  
-ATOM   7526  C   TYR B 293     -18.037  13.046  12.272  1.00 57.16           C  
-ANISOU 7526  C   TYR B 293     6095   8137   7488   2429   -706   -257       C  
-ATOM   7527  O   TYR B 293     -17.142  13.582  12.919  1.00 55.11           O  
-ANISOU 7527  O   TYR B 293     5895   7732   7313   2294   -614   -256       O  
-ATOM   7528  CB  TYR B 293     -18.329  10.605  12.680  1.00 57.27           C  
-ANISOU 7528  CB  TYR B 293     5836   8293   7630   2311  -1111   -418       C  
-ATOM   7529  CG  TYR B 293     -18.362   9.193  12.136  1.00 57.19           C  
-ANISOU 7529  CG  TYR B 293     5668   8403   7657   2327  -1326   -513       C  
-ATOM   7530  CD1 TYR B 293     -19.345   8.794  11.235  1.00 56.61           C  
-ANISOU 7530  CD1 TYR B 293     5543   8482   7486   2511  -1404   -506       C  
-ATOM   7531  CD2 TYR B 293     -17.416   8.257  12.531  1.00 58.48           C  
-ANISOU 7531  CD2 TYR B 293     5735   8525   7961   2163  -1463   -616       C  
-ATOM   7532  CE1 TYR B 293     -19.378   7.506  10.737  1.00 56.64           C  
-ANISOU 7532  CE1 TYR B 293     5401   8591   7529   2531  -1610   -598       C  
-ATOM   7533  CE2 TYR B 293     -17.442   6.965  12.042  1.00 58.27           C  
-ANISOU 7533  CE2 TYR B 293     5563   8603   7974   2180  -1669   -707       C  
-ATOM   7534  CZ  TYR B 293     -18.423   6.593  11.146  1.00 57.65           C  
-ANISOU 7534  CZ  TYR B 293     5434   8675   7797   2364  -1742   -697       C  
-ATOM   7535  OH  TYR B 293     -18.436   5.302  10.663  1.00 55.72           O  
-ANISOU 7535  OH  TYR B 293     5043   8529   7598   2383  -1958   -793       O  
-ATOM   7536  N   LYS B 294     -19.206  13.627  12.036  1.00 45.72           N  
-ANISOU 7536  N   LYS B 294     4705   6749   5917   2583   -654   -179       N  
-ATOM   7537  CA  LYS B 294     -19.585  14.866  12.697  1.00 46.03           C  
-ANISOU 7537  CA  LYS B 294     4877   6692   5922   2587   -503    -92       C  
-ATOM   7538  C   LYS B 294     -20.347  14.502  13.968  1.00 41.71           C  
-ANISOU 7538  C   LYS B 294     4277   6144   5426   2488   -617   -108       C  
-ATOM   7539  O   LYS B 294     -21.311  13.736  13.920  1.00 40.95           O  
-ANISOU 7539  O   LYS B 294     4084   6171   5306   2545   -758   -129       O  
-ATOM   7540  CB  LYS B 294     -20.452  15.732  11.778  1.00 53.06           C  
-ANISOU 7540  CB  LYS B 294     5864   7643   6654   2810   -387     -1       C  
-ATOM   7541  CG  LYS B 294     -20.865  17.052  12.398  1.00 61.23           C  
-ANISOU 7541  CG  LYS B 294     7037   8576   7651   2828   -233     87       C  
-ATOM   7542  CD  LYS B 294     -21.980  17.722  11.626  1.00 70.48           C  
-ANISOU 7542  CD  LYS B 294     8282   9824   8673   3050   -170    164       C  
-ATOM   7543  CE  LYS B 294     -21.445  18.559  10.484  1.00 78.05           C  
-ANISOU 7543  CE  LYS B 294     9363  10749   9542   3170     -4    230       C  
-ATOM   7544  NZ  LYS B 294     -22.537  19.342   9.830  1.00 82.19           N  
-ANISOU 7544  NZ  LYS B 294     9982  11326   9921   3385     60    311       N  
-ATOM   7545  N   VAL B 295     -19.924  15.043  15.104  1.00 40.85           N  
-ANISOU 7545  N   VAL B 295     4234   5898   5391   2343   -556    -99       N  
-ATOM   7546  CA  VAL B 295     -20.514  14.635  16.369  1.00 39.79           C  
-ANISOU 7546  CA  VAL B 295     4053   5758   5306   2231   -662   -119       C  
-ATOM   7547  C   VAL B 295     -21.289  15.745  17.084  1.00 41.14           C  
-ANISOU 7547  C   VAL B 295     4336   5877   5417   2271   -541    -44       C  
-ATOM   7548  O   VAL B 295     -20.764  16.826  17.336  1.00 39.92           O  
-ANISOU 7548  O   VAL B 295     4308   5594   5267   2250   -388     -2       O  
-ATOM   7549  CB  VAL B 295     -19.447  14.071  17.309  1.00 37.14           C  
-ANISOU 7549  CB  VAL B 295     3682   5314   5114   2009   -745   -194       C  
-ATOM   7550  CG1 VAL B 295     -20.072  13.684  18.633  1.00 35.90           C  
-ANISOU 7550  CG1 VAL B 295     3495   5151   4994   1896   -847   -206       C  
-ATOM   7551  CG2 VAL B 295     -18.774  12.880  16.665  1.00 36.52           C  
-ANISOU 7551  CG2 VAL B 295     3478   5296   5101   1970   -888   -280       C  
-ATOM   7552  N   GLY B 296     -22.545  15.470  17.410  1.00 63.07           N  
-ANISOU 7552  N   GLY B 296     7062   8753   8147   2328   -611    -29       N  
-ATOM   7553  CA  GLY B 296     -23.350  16.409  18.167  1.00 62.92           C  
-ANISOU 7553  CA  GLY B 296     7131   8698   8077   2361   -512     29       C  
-ATOM   7554  C   GLY B 296     -23.476  15.990  19.618  1.00 62.06           C  
-ANISOU 7554  C   GLY B 296     6992   8549   8039   2192   -591     -3       C  
-ATOM   7555  O   GLY B 296     -23.872  14.863  19.916  1.00 60.78           O  
-ANISOU 7555  O   GLY B 296     6705   8473   7915   2130   -750    -46       O  
-ATOM   7556  N   VAL B 297     -23.124  16.892  20.525  1.00 41.55           N  
-ANISOU 7556  N   VAL B 297     4512   5818   5458   2116   -484     18       N  
-ATOM   7557  CA  VAL B 297     -23.272  16.625  21.950  1.00 42.47           C  
-ANISOU 7557  CA  VAL B 297     4624   5889   5622   1966   -542     -7       C  
-ATOM   7558  C   VAL B 297     -24.569  17.219  22.491  1.00 43.28           C  
-ANISOU 7558  C   VAL B 297     4761   6043   5642   2052   -478     42       C  
-ATOM   7559  O   VAL B 297     -24.736  18.438  22.513  1.00 44.84           O  
-ANISOU 7559  O   VAL B 297     5077   6175   5784   2138   -329     91       O  
-ATOM   7560  CB  VAL B 297     -22.097  17.198  22.750  1.00 41.23           C  
-ANISOU 7560  CB  VAL B 297     4575   5549   5541   1822   -481    -26       C  
-ATOM   7561  CG1 VAL B 297     -22.360  17.048  24.233  1.00 41.10           C  
-ANISOU 7561  CG1 VAL B 297     4579   5489   5549   1690   -530    -45       C  
-ATOM   7562  CG2 VAL B 297     -20.818  16.499  22.365  1.00 43.17           C  
-ANISOU 7562  CG2 VAL B 297     4771   5744   5889   1716   -561    -89       C  
-ATOM   7563  N   VAL B 298     -25.485  16.354  22.917  1.00 52.95           N  
-ANISOU 7563  N   VAL B 298     5876   7381   6863   2030   -591     28       N  
-ATOM   7564  CA  VAL B 298     -26.750  16.789  23.504  1.00 53.30           C  
-ANISOU 7564  CA  VAL B 298     5929   7483   6839   2100   -538     65       C  
-ATOM   7565  C   VAL B 298     -26.712  16.732  25.023  1.00 52.46           C  
-ANISOU 7565  C   VAL B 298     5860   7311   6763   1940   -550     49       C  
-ATOM   7566  O   VAL B 298     -26.469  15.677  25.597  1.00 52.09           O  
-ANISOU 7566  O   VAL B 298     5736   7276   6778   1793   -684      9       O  
-ATOM   7567  CB  VAL B 298     -27.908  15.898  23.036  1.00 54.39           C  
-ANISOU 7567  CB  VAL B 298     5915   7794   6958   2184   -647     63       C  
-ATOM   7568  CG1 VAL B 298     -29.170  16.187  23.846  1.00 54.37           C  
-ANISOU 7568  CG1 VAL B 298     5902   7849   6909   2219   -603     90       C  
-ATOM   7569  CG2 VAL B 298     -28.147  16.090  21.545  1.00 54.81           C  
-ANISOU 7569  CG2 VAL B 298     5949   7919   6959   2376   -627     82       C  
-ATOM   7570  N   LYS B 299     -26.966  17.862  25.673  1.00 46.94           N  
-ANISOU 7570  N   LYS B 299     5282   6540   6014   1972   -414     79       N  
-ATOM   7571  CA  LYS B 299     -26.944  17.913  27.131  1.00 47.54           C  
-ANISOU 7571  CA  LYS B 299     5412   6550   6102   1835   -413     64       C  
-ATOM   7572  C   LYS B 299     -28.306  18.257  27.730  1.00 48.71           C  
-ANISOU 7572  C   LYS B 299     5551   6784   6173   1910   -352     93       C  
-ATOM   7573  O   LYS B 299     -29.178  18.801  27.051  1.00 51.57           O  
-ANISOU 7573  O   LYS B 299     5900   7221   6474   2082   -280    127       O  
-ATOM   7574  CB  LYS B 299     -25.909  18.929  27.620  1.00 45.71           C  
-ANISOU 7574  CB  LYS B 299     5340   6136   5892   1779   -315     58       C  
-ATOM   7575  CG  LYS B 299     -24.469  18.611  27.253  1.00 44.03           C  
-ANISOU 7575  CG  LYS B 299     5138   5817   5773   1677   -370     20       C  
-ATOM   7576  CD  LYS B 299     -23.515  19.542  27.989  1.00 44.77           C  
-ANISOU 7576  CD  LYS B 299     5382   5722   5907   1599   -290      7       C  
-ATOM   7577  CE  LYS B 299     -22.060  19.171  27.750  1.00 43.67           C  
-ANISOU 7577  CE  LYS B 299     5242   5469   5880   1479   -352    -41       C  
-ATOM   7578  NZ  LYS B 299     -21.149  19.992  28.605  1.00 46.16           N  
-ANISOU 7578  NZ  LYS B 299     5695   5593   6251   1389   -294    -62       N  
-ATOM   7579  N   GLN B 300     -28.477  17.940  29.010  1.00 44.05           N  
-ANISOU 7579  N   GLN B 300     4971   6180   5586   1781   -382     78       N  
-ATOM   7580  CA  GLN B 300     -29.682  18.320  29.736  1.00 45.79           C  
-ANISOU 7580  CA  GLN B 300     5194   6471   5735   1836   -308    100       C  
-ATOM   7581  C   GLN B 300     -29.611  19.793  30.116  1.00 47.84           C  
-ANISOU 7581  C   GLN B 300     5613   6623   5941   1910   -149    114       C  
-ATOM   7582  O   GLN B 300     -28.551  20.292  30.490  1.00 47.59           O  
-ANISOU 7582  O   GLN B 300     5701   6442   5940   1833   -123     97       O  
-ATOM   7583  CB  GLN B 300     -29.843  17.465  30.990  1.00 45.16           C  
-ANISOU 7583  CB  GLN B 300     5080   6411   5669   1668   -388     83       C  
-ATOM   7584  CG  GLN B 300     -29.911  15.978  30.717  1.00 42.61           C  
-ANISOU 7584  CG  GLN B 300     4599   6182   5408   1581   -556     70       C  
-ATOM   7585  CD  GLN B 300     -29.704  15.156  31.970  1.00 41.24           C  
-ANISOU 7585  CD  GLN B 300     4426   5985   5260   1385   -646     53       C  
-ATOM   7586  OE1 GLN B 300     -29.869  13.934  31.962  1.00 38.30           O  
-ANISOU 7586  OE1 GLN B 300     3929   5686   4936   1299   -785     47       O  
-ATOM   7587  NE2 GLN B 300     -29.336  15.825  33.059  1.00 37.51           N  
-ANISOU 7587  NE2 GLN B 300     4098   5403   4752   1316   -573     45       N  
-ATOM   7588  N   THR B 301     -30.742  20.484  30.023  1.00 55.42           N  
-ANISOU 7588  N   THR B 301     6571   7657   6829   2060    -51    141       N  
-ATOM   7589  CA  THR B 301     -30.778  21.923  30.259  1.00 58.96           C  
-ANISOU 7589  CA  THR B 301     7164   8011   7227   2156     95    154       C  
-ATOM   7590  C   THR B 301     -31.361  22.316  31.619  1.00 59.29           C  
-ANISOU 7590  C   THR B 301     7263   8048   7217   2119    159    142       C  
-ATOM   7591  O   THR B 301     -31.245  23.468  32.031  1.00 60.09           O  
-ANISOU 7591  O   THR B 301     7497   8051   7284   2170    266    141       O  
-ATOM   7592  CB  THR B 301     -31.544  22.653  29.141  1.00 61.24           C  
-ANISOU 7592  CB  THR B 301     7440   8361   7469   2372    171    189       C  
-ATOM   7593  OG1 THR B 301     -32.901  22.193  29.107  1.00 63.72           O  
-ANISOU 7593  OG1 THR B 301     7625   8837   7749   2449    152    193       O  
-ATOM   7594  CG2 THR B 301     -30.892  22.383  27.794  1.00 63.08           C  
-ANISOU 7594  CG2 THR B 301     7642   8588   7737   2417    123    203       C  
-ATOM   7595  N   GLU B 302     -31.991  21.369  32.310  1.00 58.56           N  
-ANISOU 7595  N   GLU B 302     7073   8060   7118   2032     96    133       N  
-ATOM   7596  CA  GLU B 302     -32.471  21.628  33.669  1.00 60.87           C  
-ANISOU 7596  CA  GLU B 302     7421   8350   7355   1979    155    121       C  
-ATOM   7597  C   GLU B 302     -31.820  20.715  34.714  1.00 58.18           C  
-ANISOU 7597  C   GLU B 302     7096   7968   7043   1767     58     98       C  
-ATOM   7598  O   GLU B 302     -31.154  19.741  34.367  1.00 57.49           O  
-ANISOU 7598  O   GLU B 302     6944   7874   7024   1662    -69     90       O  
-ATOM   7599  CB  GLU B 302     -34.006  21.588  33.749  1.00 65.74           C  
-ANISOU 7599  CB  GLU B 302     7933   9128   7919   2085    209    136       C  
-ATOM   7600  CG  GLU B 302     -34.672  20.357  33.157  1.00 69.23           C  
-ANISOU 7600  CG  GLU B 302     8182   9722   8401   2078    105    150       C  
-ATOM   7601  CD  GLU B 302     -36.184  20.514  33.048  1.00 73.92           C  
-ANISOU 7601  CD  GLU B 302     8669  10460   8956   2215    170    162       C  
-ATOM   7602  OE1 GLU B 302     -36.681  21.648  33.222  1.00 76.34           O  
-ANISOU 7602  OE1 GLU B 302     9053  10749   9205   2339    297    158       O  
-ATOM   7603  OE2 GLU B 302     -36.875  19.507  32.783  1.00 77.26           O  
-ANISOU 7603  OE2 GLU B 302     8929  11010   9416   2201     91    171       O  
-ATOM   7604  N   THR B 303     -31.996  21.049  35.988  1.00 52.65           N  
-ANISOU 7604  N   THR B 303     6485   7233   6285   1709    113     83       N  
-ATOM   7605  CA  THR B 303     -31.366  20.288  37.061  1.00 51.28           C  
-ANISOU 7605  CA  THR B 303     6354   7005   6125   1514     25     62       C  
-ATOM   7606  C   THR B 303     -32.389  19.790  38.083  1.00 51.11           C  
-ANISOU 7606  C   THR B 303     6285   7099   6035   1463     46     74       C  
-ATOM   7607  O   THR B 303     -33.409  20.437  38.326  1.00 53.18           O  
-ANISOU 7607  O   THR B 303     6545   7435   6226   1577    167     83       O  
-ATOM   7608  CB  THR B 303     -30.258  21.099  37.754  1.00 49.90           C  
-ANISOU 7608  CB  THR B 303     6367   6640   5953   1456     50     26       C  
-ATOM   7609  OG1 THR B 303     -30.772  22.374  38.153  1.00 50.73           O  
-ANISOU 7609  OG1 THR B 303     6574   6718   5982   1580    195     22       O  
-ATOM   7610  CG2 THR B 303     -29.103  21.317  36.808  1.00 50.26           C  
-ANISOU 7610  CG2 THR B 303     6441   6569   6088   1460      8     15       C  
-ATOM   7611  N   ALA B 304     -32.102  18.634  38.674  1.00 46.18           N  
-ANISOU 7611  N   ALA B 304     5624   6487   5435   1292    -72     74       N  
-ATOM   7612  CA  ALA B 304     -33.074  17.906  39.488  1.00 45.43           C  
-ANISOU 7612  CA  ALA B 304     5454   6517   5290   1227    -70     98       C  
-ATOM   7613  C   ALA B 304     -33.833  18.757  40.510  1.00 47.23           C  
-ANISOU 7613  C   ALA B 304     5771   6767   5406   1283     82     96       C  
-ATOM   7614  O   ALA B 304     -35.050  18.911  40.416  1.00 47.56           O  
-ANISOU 7614  O   ALA B 304     5719   6943   5409   1386    174    116       O  
-ATOM   7615  CB  ALA B 304     -32.404  16.732  40.170  1.00 44.74           C  
-ANISOU 7615  CB  ALA B 304     5371   6390   5237   1020   -216     95       C  
-ATOM   7616  N   ALA B 305     -33.113  19.300  41.486  1.00 46.23           N  
-ANISOU 7616  N   ALA B 305     5823   6509   5234   1218    105     64       N  
-ATOM   7617  CA  ALA B 305     -33.735  20.042  42.581  1.00 49.78           C  
-ANISOU 7617  CA  ALA B 305     6373   6972   5569   1257    237     54       C  
-ATOM   7618  C   ALA B 305     -34.595  21.234  42.141  1.00 53.67           C  
-ANISOU 7618  C   ALA B 305     6857   7516   6020   1464    391     49       C  
-ATOM   7619  O   ALA B 305     -35.480  21.669  42.884  1.00 56.60           O  
-ANISOU 7619  O   ALA B 305     7249   7957   6301   1518    508     45       O  
-ATOM   7620  CB  ALA B 305     -32.680  20.487  43.582  1.00 48.66           C  
-ANISOU 7620  CB  ALA B 305     6434   6658   5395   1167    217     11       C  
-ATOM   7621  N   LEU B 306     -34.335  21.763  40.947  1.00 46.73           N  
-ANISOU 7621  N   LEU B 306     5952   6599   5203   1580    392     48       N  
-ATOM   7622  CA  LEU B 306     -35.095  22.907  40.441  1.00 50.99           C  
-ANISOU 7622  CA  LEU B 306     6491   7173   5710   1781    522     44       C  
-ATOM   7623  C   LEU B 306     -36.278  22.487  39.577  1.00 51.73           C  
-ANISOU 7623  C   LEU B 306     6392   7439   5824   1885    536     75       C  
-ATOM   7624  O   LEU B 306     -37.312  23.156  39.558  1.00 53.62           O  
-ANISOU 7624  O   LEU B 306     6600   7758   6017   2027    649     71       O  
-ATOM   7625  CB  LEU B 306     -34.196  23.873  39.667  1.00 50.46           C  
-ANISOU 7625  CB  LEU B 306     6525   6958   5690   1864    529     30       C  
-ATOM   7626  CG  LEU B 306     -33.199  24.626  40.543  1.00 52.84           C  
-ANISOU 7626  CG  LEU B 306     7025   7080   5972   1807    544     -9       C  
-ATOM   7627  CD1 LEU B 306     -32.700  25.878  39.852  1.00 52.38           C  
-ANISOU 7627  CD1 LEU B 306     7061   6896   5945   1934    601    -19       C  
-ATOM   7628  CD2 LEU B 306     -33.853  24.979  41.874  1.00 53.10           C  
-ANISOU 7628  CD2 LEU B 306     7132   7146   5898   1805    632    -34       C  
-ATOM   7629  N   LYS B 307     -36.119  21.382  38.857  1.00 62.29           N  
-ANISOU 7629  N   LYS B 307     7600   8831   7238   1818    415    101       N  
-ATOM   7630  CA  LYS B 307     -37.186  20.876  38.006  1.00 64.37           C  
-ANISOU 7630  CA  LYS B 307     7674   9251   7534   1910    404    126       C  
-ATOM   7631  C   LYS B 307     -38.377  20.488  38.877  1.00 68.43           C  
-ANISOU 7631  C   LYS B 307     8100   9901   7998   1887    468    136       C  
-ATOM   7632  O   LYS B 307     -39.526  20.743  38.522  1.00 69.44           O  
-ANISOU 7632  O   LYS B 307     8121  10143   8119   2021    541    139       O  
-ATOM   7633  CB  LYS B 307     -36.698  19.672  37.195  1.00 60.99           C  
-ANISOU 7633  CB  LYS B 307     7130   8846   7199   1824    244    145       C  
-ATOM   7634  CG  LYS B 307     -37.626  19.248  36.063  1.00 60.14           C  
-ANISOU 7634  CG  LYS B 307     6837   8874   7139   1943    213    163       C  
-ATOM   7635  CD  LYS B 307     -37.513  17.752  35.808  1.00 57.94           C  
-ANISOU 7635  CD  LYS B 307     6415   8660   6938   1815     55    181       C  
-ATOM   7636  CE  LYS B 307     -37.924  17.365  34.394  1.00 57.19           C  
-ANISOU 7636  CE  LYS B 307     6171   8649   6910   1935    -18    188       C  
-ATOM   7637  NZ  LYS B 307     -39.319  17.747  34.053  1.00 58.44           N  
-ANISOU 7637  NZ  LYS B 307     6223   8930   7053   2101     64    193       N  
-ATOM   7638  N   ALA B 308     -38.085  19.886  40.027  1.00 80.72           N  
-ANISOU 7638  N   ALA B 308     9707  11442   9522   1716    442    140       N  
-ATOM   7639  CA  ALA B 308     -39.115  19.424  40.954  1.00 87.41           C  
-ANISOU 7639  CA  ALA B 308    10482  12414  10317   1667    506    157       C  
-ATOM   7640  C   ALA B 308     -39.880  20.573  41.600  1.00 93.17           C  
-ANISOU 7640  C   ALA B 308    11282  13168  10951   1789    681    130       C  
-ATOM   7641  O   ALA B 308     -40.716  20.355  42.473  1.00 96.55           O  
-ANISOU 7641  O   ALA B 308    11670  13694  11321   1756    762    138       O  
-ATOM   7642  CB  ALA B 308     -38.496  18.544  42.029  1.00 91.31           C  
-ANISOU 7642  CB  ALA B 308    11041  12866  10788   1452    431    171       C  
-ATOM   7643  N   ILE B 309     -39.594  21.796  41.172  1.00 59.83           N  
-ANISOU 7643  N   ILE B 309     7163   8857   6713   1930    742     98       N  
-ATOM   7644  CA  ILE B 309     -40.215  22.967  41.772  1.00 66.41           C  
-ANISOU 7644  CA  ILE B 309     8078   9695   7459   2054    897     63       C  
-ATOM   7645  C   ILE B 309     -40.962  23.792  40.736  1.00 73.06           C  
-ANISOU 7645  C   ILE B 309     8848  10582   8328   2269    959     50       C  
-ATOM   7646  O   ILE B 309     -42.049  24.302  40.997  1.00 79.05           O  
-ANISOU 7646  O   ILE B 309     9558  11432   9044   2382   1074     30       O  
-ATOM   7647  CB  ILE B 309     -39.166  23.856  42.467  1.00 62.62           C  
-ANISOU 7647  CB  ILE B 309     7825   9042   6924   2027    919     26       C  
-ATOM   7648  CG1 ILE B 309     -39.257  23.689  43.986  1.00 62.35           C  
-ANISOU 7648  CG1 ILE B 309     7882   9018   6791   1915    972     13       C  
-ATOM   7649  CG2 ILE B 309     -39.339  25.324  42.055  1.00 62.80           C  
-ANISOU 7649  CG2 ILE B 309     7929   9006   6928   2223   1017     -9       C  
-ATOM   7650  CD1 ILE B 309     -38.294  24.563  44.749  1.00 58.55           C  
-ANISOU 7650  CD1 ILE B 309     7625   8367   6253   1896    988    -31       C  
-ATOM   7651  N   GLY B 310     -40.375  23.920  39.554  1.00 67.03           N  
-ANISOU 7651  N   GLY B 310     8082   9753   7634   2327    882     61       N  
-ATOM   7652  CA  GLY B 310     -40.989  24.700  38.500  1.00 76.57           C  
-ANISOU 7652  CA  GLY B 310     9241  10989   8864   2531    926     53       C  
-ATOM   7653  C   GLY B 310     -42.276  24.080  37.997  1.00 83.31           C  
-ANISOU 7653  C   GLY B 310     9882  12016   9756   2602    924     66       C  
-ATOM   7654  O   GLY B 310     -42.827  23.158  38.603  1.00 85.99           O  
-ANISOU 7654  O   GLY B 310    10112  12462  10100   2499    916     79       O  
-ATOM   7655  N   ASP B 311     -42.752  24.597  36.872  1.00144.49           N  
-ANISOU 7655  N   ASP B 311    17575  19786  17539   2781    927     62       N  
-ATOM   7656  CA  ASP B 311     -43.972  24.106  36.250  1.00149.12           C  
-ANISOU 7656  CA  ASP B 311    17960  20524  18175   2875    913     65       C  
-ATOM   7657  C   ASP B 311     -43.894  22.618  35.916  1.00145.47           C  
-ANISOU 7657  C   ASP B 311    17347  20136  17788   2746    780    100       C  
-ATOM   7658  O   ASP B 311     -44.429  21.787  36.650  1.00141.01           O  
-ANISOU 7658  O   ASP B 311    16679  19667  17233   2636    784    111       O  
-ATOM   7659  CB  ASP B 311     -44.284  24.926  34.997  1.00159.65           C  
-ANISOU 7659  CB  ASP B 311    19289  21841  19531   3089    914     55       C  
-ATOM   7660  CG  ASP B 311     -43.037  25.497  34.353  1.00166.58           C  
-ANISOU 7660  CG  ASP B 311    20326  22563  20404   3102    874     70       C  
-ATOM   7661  OD1 ASP B 311     -42.018  24.779  34.282  1.00176.52           O  
-ANISOU 7661  OD1 ASP B 311    21613  23767  21691   2957    782     95       O  
-ATOM   7662  OD2 ASP B 311     -43.073  26.671  33.930  1.00174.15           O  
-ANISOU 7662  OD2 ASP B 311    21383  23452  21335   3256    935     57       O  
-ATOM   7663  N   ASN B 312     -43.227  22.285  34.813  1.00123.81           N  
-ANISOU 7663  N   ASN B 312    14594  17349  15100   2759    664    119       N  
-ATOM   7664  CA  ASN B 312     -43.156  20.902  34.343  1.00120.67           C  
-ANISOU 7664  CA  ASN B 312    14048  17018  14782   2659    522    145       C  
-ATOM   7665  C   ASN B 312     -42.292  20.004  35.222  1.00122.23           C  
-ANISOU 7665  C   ASN B 312    14287  17174  14982   2426    458    163       C  
-ATOM   7666  O   ASN B 312     -41.372  19.349  34.741  1.00123.36           O  
-ANISOU 7666  O   ASN B 312    14436  17265  15172   2339    334    176       O  
-ATOM   7667  CB  ASN B 312     -42.658  20.843  32.896  1.00117.88           C  
-ANISOU 7667  CB  ASN B 312    13682  16629  14477   2750    419    153       C  
-ATOM   7668  CG  ASN B 312     -41.184  21.185  32.772  1.00113.72           C  
-ANISOU 7668  CG  ASN B 312    13328  15948  13931   2681    392    159       C  
-ATOM   7669  OD1 ASN B 312     -40.388  20.382  32.283  1.00112.79           O  
-ANISOU 7669  OD1 ASN B 312    13187  15805  13863   2591    272    172       O  
-ATOM   7670  ND2 ASN B 312     -40.813  22.378  33.220  1.00110.12           N  
-ANISOU 7670  ND2 ASN B 312    13042  15387  13410   2725    502    146       N  
-ATOM   7671  N   ARG B 313     -42.596  19.970  36.513  1.00 85.27           N  
-ANISOU 7671  N   ARG B 313     9634  12516  10247   2329    539    162       N  
-ATOM   7672  CA  ARG B 313     -41.846  19.145  37.447  1.00 87.77           C  
-ANISOU 7672  CA  ARG B 313    10003  12792  10555   2111    479    180       C  
-ATOM   7673  C   ARG B 313     -42.088  17.667  37.164  1.00 83.83           C  
-ANISOU 7673  C   ARG B 313     9324  12385  10144   2002    344    212       C  
-ATOM   7674  O   ARG B 313     -41.325  16.808  37.599  1.00 81.51           O  
-ANISOU 7674  O   ARG B 313     9055  12046   9868   1824    246    229       O  
-ATOM   7675  CB  ARG B 313     -42.232  19.485  38.890  1.00 91.76           C  
-ANISOU 7675  CB  ARG B 313    10584  13312  10969   2049    607    173       C  
-ATOM   7676  CG  ARG B 313     -43.670  19.149  39.254  1.00102.36           C  
-ANISOU 7676  CG  ARG B 313    11763  14816  12315   2081    685    183       C  
-ATOM   7677  CD  ARG B 313     -44.006  19.592  40.671  1.00109.94           C  
-ANISOU 7677  CD  ARG B 313    12815  15788  13168   2033    828    172       C  
-ATOM   7678  NE  ARG B 313     -44.249  21.029  40.756  1.00119.00           N  
-ANISOU 7678  NE  ARG B 313    14070  16897  14247   2200    962    125       N  
-ATOM   7679  CZ  ARG B 313     -44.491  21.678  41.891  1.00125.75           C  
-ANISOU 7679  CZ  ARG B 313    15031  17749  15000   2199   1095    100       C  
-ATOM   7680  NH1 ARG B 313     -44.516  21.018  43.040  1.00131.21           N  
-ANISOU 7680  NH1 ARG B 313    15740  18475  15637   2038   1119    122       N  
-ATOM   7681  NH2 ARG B 313     -44.705  22.987  41.879  1.00129.65           N  
-ANISOU 7681  NH2 ARG B 313    15616  18202  15443   2360   1202     52       N  
-ATOM   7682  N   SER B 314     -43.147  17.382  36.414  1.00139.15           N  
-ANISOU 7682  N   SER B 314    16149  19512  17211   2114    331    215       N  
-ATOM   7683  CA  SER B 314     -43.564  16.008  36.161  1.00130.58           C  
-ANISOU 7683  CA  SER B 314    14873  18522  16219   2026    207    242       C  
-ATOM   7684  C   SER B 314     -43.377  15.599  34.705  1.00124.07           C  
-ANISOU 7684  C   SER B 314    13952  17706  15482   2114     67    236       C  
-ATOM   7685  O   SER B 314     -44.348  15.294  34.011  1.00122.59           O  
-ANISOU 7685  O   SER B 314    13595  17622  15360   2220     36    233       O  
-ATOM   7686  CB  SER B 314     -45.031  15.833  36.550  1.00134.97           C  
-ANISOU 7686  CB  SER B 314    15269  19221  16793   2069    293    249       C  
-ATOM   7687  OG  SER B 314     -45.844  16.791  35.893  1.00140.65           O  
-ANISOU 7687  OG  SER B 314    15952  19980  17508   2287    379    217       O  
-ATOM   7688  N   SER B 315     -42.131  15.579  34.247  1.00 79.77           N  
-ANISOU 7688  N   SER B 315     8448  11986   9874   2072    -19    231       N  
-ATOM   7689  CA  SER B 315     -41.850  15.186  32.873  1.00 73.10           C  
-ANISOU 7689  CA  SER B 315     7529  11147   9100   2152   -150    223       C  
-ATOM   7690  C   SER B 315     -40.381  14.859  32.654  1.00 67.29           C  
-ANISOU 7690  C   SER B 315     6895  10295   8376   2041   -254    218       C  
-ATOM   7691  O   SER B 315     -39.628  14.645  33.601  1.00 68.33           O  
-ANISOU 7691  O   SER B 315     7124  10352   8485   1875   -260    224       O  
-ATOM   7692  CB  SER B 315     -42.308  16.272  31.892  1.00 71.24           C  
-ANISOU 7692  CB  SER B 315     7313  10917   8838   2387    -77    203       C  
-ATOM   7693  OG  SER B 315     -41.835  17.551  32.281  1.00 67.91           O  
-ANISOU 7693  OG  SER B 315     7083  10392   8327   2434     55    193       O  
-ATOM   7694  N   LEU B 316     -39.988  14.825  31.387  1.00 85.49           N  
-ANISOU 7694  N   LEU B 316     9178  12586  10718   2140   -336    206       N  
-ATOM   7695  CA  LEU B 316     -38.638  14.452  30.995  1.00 77.39           C  
-ANISOU 7695  CA  LEU B 316     8222  11464   9720   2051   -441    196       C  
-ATOM   7696  C   LEU B 316     -37.710  15.648  31.103  1.00 75.87           C  
-ANISOU 7696  C   LEU B 316     8234  11135   9460   2080   -336    187       C  
-ATOM   7697  O   LEU B 316     -38.096  16.772  30.779  1.00 74.64           O  
-ANISOU 7697  O   LEU B 316     8143  10967   9250   2239   -218    187       O  
-ATOM   7698  CB  LEU B 316     -38.648  13.948  29.552  1.00 75.40           C  
-ANISOU 7698  CB  LEU B 316     7860  11262   9528   2159   -563    184       C  
-ATOM   7699  CG  LEU B 316     -37.496  13.069  29.069  1.00 70.08           C  
-ANISOU 7699  CG  LEU B 316     7177  10536   8913   2054   -718    167       C  
-ATOM   7700  CD1 LEU B 316     -37.400  11.799  29.901  1.00 68.17           C  
-ANISOU 7700  CD1 LEU B 316     6850  10316   8735   1849   -837    172       C  
-ATOM   7701  CD2 LEU B 316     -37.691  12.733  27.600  1.00 68.96           C  
-ANISOU 7701  CD2 LEU B 316     6931  10458   8811   2200   -816    152       C  
-ATOM   7702  N   PHE B 317     -36.487  15.403  31.561  1.00 66.30           N  
-ANISOU 7702  N   PHE B 317     7120   9812   8259   1925   -387    177       N  
-ATOM   7703  CA  PHE B 317     -35.464  16.443  31.590  1.00 66.36           C  
-ANISOU 7703  CA  PHE B 317     7312   9675   8227   1939   -308    166       C  
-ATOM   7704  C   PHE B 317     -35.247  17.043  30.205  1.00 64.91           C  
-ANISOU 7704  C   PHE B 317     7144   9474   8043   2108   -292    165       C  
-ATOM   7705  O   PHE B 317     -34.833  16.352  29.273  1.00 65.00           O  
-ANISOU 7705  O   PHE B 317     7082   9506   8108   2112   -405    158       O  
-ATOM   7706  CB  PHE B 317     -34.145  15.886  32.121  1.00 67.13           C  
-ANISOU 7706  CB  PHE B 317     7482   9660   8364   1746   -399    147       C  
-ATOM   7707  CG  PHE B 317     -33.977  16.044  33.599  1.00 69.79           C  
-ANISOU 7707  CG  PHE B 317     7924   9934   8660   1611   -350    145       C  
-ATOM   7708  CD1 PHE B 317     -34.628  15.198  34.479  1.00 70.73           C  
-ANISOU 7708  CD1 PHE B 317     7964  10134   8777   1501   -389    160       C  
-ATOM   7709  CD2 PHE B 317     -33.164  17.039  34.110  1.00 70.01           C  
-ANISOU 7709  CD2 PHE B 317     8132   9819   8650   1595   -266    128       C  
-ATOM   7710  CE1 PHE B 317     -34.472  15.342  35.841  1.00 70.57           C  
-ANISOU 7710  CE1 PHE B 317     8052  10058   8704   1381   -342    159       C  
-ATOM   7711  CE2 PHE B 317     -33.003  17.189  35.473  1.00 69.45           C  
-ANISOU 7711  CE2 PHE B 317     8166   9688   8534   1479   -229    120       C  
-ATOM   7712  CZ  PHE B 317     -33.657  16.338  36.339  1.00 69.80           C  
-ANISOU 7712  CZ  PHE B 317     8139   9818   8562   1374   -265    136       C  
-ATOM   7713  N   SER B 318     -35.526  18.333  30.075  1.00 70.39           N  
-ANISOU 7713  N   SER B 318     7939  10131   8674   2250   -152    174       N  
-ATOM   7714  CA  SER B 318     -35.375  19.004  28.795  1.00 68.73           C  
-ANISOU 7714  CA  SER B 318     7763   9900   8451   2418   -123    182       C  
-ATOM   7715  C   SER B 318     -33.915  19.017  28.346  1.00 67.20           C  
-ANISOU 7715  C   SER B 318     7659   9584   8289   2348   -162    176       C  
-ATOM   7716  O   SER B 318     -33.005  19.228  29.150  1.00 66.26           O  
-ANISOU 7716  O   SER B 318     7649   9347   8180   2217   -141    164       O  
-ATOM   7717  CB  SER B 318     -35.940  20.423  28.865  1.00 68.51           C  
-ANISOU 7717  CB  SER B 318     7838   9841   8352   2572     32    194       C  
-ATOM   7718  OG  SER B 318     -35.354  21.153  29.926  1.00 65.82           O  
-ANISOU 7718  OG  SER B 318     7647   9380   7981   2487    120    187       O  
-ATOM   7719  N   ARG B 319     -33.702  18.786  27.054  1.00 67.41           N  
-ANISOU 7719  N   ARG B 319     7638   9639   8334   2440   -218    180       N  
-ATOM   7720  CA  ARG B 319     -32.357  18.714  26.500  1.00 64.17           C  
-ANISOU 7720  CA  ARG B 319     7291   9130   7960   2382   -254    171       C  
-ATOM   7721  C   ARG B 319     -32.222  19.537  25.225  1.00 65.48           C  
-ANISOU 7721  C   ARG B 319     7519   9274   8088   2560   -187    196       C  
-ATOM   7722  O   ARG B 319     -33.209  19.816  24.543  1.00 65.77           O  
-ANISOU 7722  O   ARG B 319     7511   9398   8079   2731   -164    214       O  
-ATOM   7723  CB  ARG B 319     -31.984  17.259  26.221  1.00 59.95           C  
-ANISOU 7723  CB  ARG B 319     6625   8655   7500   2272   -425    144       C  
-ATOM   7724  CG  ARG B 319     -32.095  16.371  27.435  1.00 56.24           C  
-ANISOU 7724  CG  ARG B 319     6095   8203   7069   2091   -504    126       C  
-ATOM   7725  CD  ARG B 319     -31.857  14.912  27.098  1.00 51.60           C  
-ANISOU 7725  CD  ARG B 319     5365   7680   6560   1997   -686    100       C  
-ATOM   7726  NE  ARG B 319     -31.591  14.146  28.310  1.00 47.04           N  
-ANISOU 7726  NE  ARG B 319     4774   7076   6024   1795   -762     85       N  
-ATOM   7727  CZ  ARG B 319     -32.530  13.572  29.054  1.00 45.75           C  
-ANISOU 7727  CZ  ARG B 319     4523   6998   5861   1742   -793     98       C  
-ATOM   7728  NH1 ARG B 319     -33.805  13.666  28.698  1.00 45.51           N  
-ANISOU 7728  NH1 ARG B 319     4399   7090   5804   1878   -757    120       N  
-ATOM   7729  NH2 ARG B 319     -32.191  12.904  30.150  1.00 44.28           N  
-ANISOU 7729  NH2 ARG B 319     4345   6775   5704   1554   -860     89       N  
-ATOM   7730  N   LYS B 320     -30.989  19.923  24.912  1.00 63.63           N  
-ANISOU 7730  N   LYS B 320     7387   8917   7871   2517   -156    198       N  
-ATOM   7731  CA  LYS B 320     -30.699  20.655  23.686  1.00 66.15           C  
-ANISOU 7731  CA  LYS B 320     7775   9205   8154   2666    -89    228       C  
-ATOM   7732  C   LYS B 320     -29.286  20.340  23.208  1.00 63.79           C  
-ANISOU 7732  C   LYS B 320     7505   8821   7910   2573   -124    214       C  
-ATOM   7733  O   LYS B 320     -28.380  20.129  24.018  1.00 64.08           O  
-ANISOU 7733  O   LYS B 320     7576   8761   8009   2402   -145    186       O  
-ATOM   7734  CB  LYS B 320     -30.842  22.166  23.904  1.00 71.04           C  
-ANISOU 7734  CB  LYS B 320     8547   9728   8716   2762     71    264       C  
-ATOM   7735  CG  LYS B 320     -29.632  22.810  24.573  1.00 78.24           C  
-ANISOU 7735  CG  LYS B 320     9597  10465   9666   2638    141    261       C  
-ATOM   7736  CD  LYS B 320     -29.839  24.297  24.837  1.00 86.16           C  
-ANISOU 7736  CD  LYS B 320    10746  11371  10619   2735    288    293       C  
-ATOM   7737  CE  LYS B 320     -29.818  25.110  23.550  1.00 93.04           C  
-ANISOU 7737  CE  LYS B 320    11685  12221  11444   2908    365    344       C  
-ATOM   7738  NZ  LYS B 320     -29.921  26.578  23.816  1.00 96.82           N  
-ANISOU 7738  NZ  LYS B 320    12314  12587  11886   2993    501    377       N  
-ATOM   7739  N   LEU B 321     -29.102  20.297  21.892  1.00 69.69           N  
-ANISOU 7739  N   LEU B 321     8238   9604   8636   2688   -132    230       N  
-ATOM   7740  CA  LEU B 321     -27.766  20.191  21.327  1.00 65.95           C  
-ANISOU 7740  CA  LEU B 321     7804   9047   8206   2624   -133    221       C  
-ATOM   7741  C   LEU B 321     -26.988  21.412  21.782  1.00 64.83           C  
-ANISOU 7741  C   LEU B 321     7825   8735   8071   2586      9    247       C  
-ATOM   7742  O   LEU B 321     -27.423  22.540  21.572  1.00 66.34           O  
-ANISOU 7742  O   LEU B 321     8117   8892   8199   2715    129    296       O  
-ATOM   7743  CB  LEU B 321     -27.828  20.157  19.805  1.00 66.65           C  
-ANISOU 7743  CB  LEU B 321     7875   9206   8244   2785   -135    244       C  
-ATOM   7744  CG  LEU B 321     -26.483  20.014  19.097  1.00 66.17           C  
-ANISOU 7744  CG  LEU B 321     7843   9075   8222   2733   -126    234       C  
-ATOM   7745  CD1 LEU B 321     -25.931  18.608  19.274  1.00 66.91           C  
-ANISOU 7745  CD1 LEU B 321     7806   9212   8404   2585   -287    165       C  
-ATOM   7746  CD2 LEU B 321     -26.628  20.335  17.634  1.00 66.62           C  
-ANISOU 7746  CD2 LEU B 321     7929   9186   8198   2921    -81    274       C  
-ATOM   7747  N   THR B 322     -25.845  21.192  22.416  1.00 62.96           N  
-ANISOU 7747  N   THR B 322     7615   8387   7920   2410    -12    212       N  
-ATOM   7748  CA  THR B 322     -25.074  22.299  22.966  1.00 62.14           C  
-ANISOU 7748  CA  THR B 322     7659   8109   7843   2359    108    228       C  
-ATOM   7749  C   THR B 322     -23.857  22.608  22.109  1.00 60.52           C  
-ANISOU 7749  C   THR B 322     7507   7808   7681   2351    165    241       C  
-ATOM   7750  O   THR B 322     -23.373  23.741  22.093  1.00 60.02           O  
-ANISOU 7750  O   THR B 322     7571   7614   7621   2375    293    278       O  
-ATOM   7751  CB  THR B 322     -24.619  22.022  24.416  1.00 61.99           C  
-ANISOU 7751  CB  THR B 322     7655   8004   7895   2168     56    178       C  
-ATOM   7752  OG1 THR B 322     -23.586  21.027  24.420  1.00 63.32           O  
-ANISOU 7752  OG1 THR B 322     7755   8144   8158   2018    -55    124       O  
-ATOM   7753  CG2 THR B 322     -25.789  21.550  25.262  1.00 62.54           C  
-ANISOU 7753  CG2 THR B 322     7658   8182   7923   2161     -3    166       C  
-ATOM   7754  N   ALA B 323     -23.362  21.602  21.396  1.00 49.23           N  
-ANISOU 7754  N   ALA B 323     5977   6442   6287   2316     71    208       N  
-ATOM   7755  CA  ALA B 323     -22.180  21.796  20.564  1.00 49.45           C  
-ANISOU 7755  CA  ALA B 323     6041   6390   6359   2302    127    214       C  
-ATOM   7756  C   ALA B 323     -22.012  20.734  19.479  1.00 48.66           C  
-ANISOU 7756  C   ALA B 323     5823   6411   6256   2336     31    187       C  
-ATOM   7757  O   ALA B 323     -22.588  19.644  19.554  1.00 48.02           O  
-ANISOU 7757  O   ALA B 323     5617   6455   6174   2321   -112    146       O  
-ATOM   7758  CB  ALA B 323     -20.929  21.873  21.435  1.00 49.05           C  
-ANISOU 7758  CB  ALA B 323     6032   6173   6431   2112    127    170       C  
-ATOM   7759  N   LEU B 324     -21.221  21.075  18.468  1.00 60.28           N  
-ANISOU 7759  N   LEU B 324     7336   7842   7727   2383    114    211       N  
-ATOM   7760  CA  LEU B 324     -20.842  20.131  17.426  1.00 58.94           C  
-ANISOU 7760  CA  LEU B 324     7067   7768   7560   2408     37    177       C  
-ATOM   7761  C   LEU B 324     -19.326  20.074  17.310  1.00 58.01           C  
-ANISOU 7761  C   LEU B 324     6958   7532   7550   2280     70    142       C  
-ATOM   7762  O   LEU B 324     -18.619  20.990  17.753  1.00 57.07           O  
-ANISOU 7762  O   LEU B 324     6943   7255   7485   2214    186    165       O  
-ATOM   7763  CB  LEU B 324     -21.431  20.542  16.082  1.00 60.80           C  
-ANISOU 7763  CB  LEU B 324     7338   8096   7669   2623    109    241       C  
-ATOM   7764  CG  LEU B 324     -22.862  20.108  15.791  1.00 61.02           C  
-ANISOU 7764  CG  LEU B 324     7296   8286   7602   2765     19    248       C  
-ATOM   7765  CD1 LEU B 324     -23.382  20.861  14.586  1.00 63.93           C  
-ANISOU 7765  CD1 LEU B 324     7747   8700   7842   2981    119    322       C  
-ATOM   7766  CD2 LEU B 324     -22.923  18.609  15.557  1.00 62.97           C  
-ANISOU 7766  CD2 LEU B 324     7378   8659   7887   2724   -168    171       C  
-ATOM   7767  N   TYR B 325     -18.829  18.999  16.705  1.00 50.47           N  
-ANISOU 7767  N   TYR B 325     5892   6653   6633   2248    -34     80       N  
-ATOM   7768  CA  TYR B 325     -17.395  18.807  16.546  1.00 49.07           C  
-ANISOU 7768  CA  TYR B 325     5699   6378   6567   2127    -16     32       C  
-ATOM   7769  C   TYR B 325     -17.079  18.024  15.287  1.00 49.09           C  
-ANISOU 7769  C   TYR B 325     5614   6493   6544   2198    -61      1       C  
-ATOM   7770  O   TYR B 325     -17.763  17.049  14.966  1.00 48.23           O  
-ANISOU 7770  O   TYR B 325     5400   6533   6394   2254   -204    -35       O  
-ATOM   7771  CB  TYR B 325     -16.810  18.088  17.763  1.00 46.38           C  
-ANISOU 7771  CB  TYR B 325     5295   5962   6366   1919   -149    -56       C  
-ATOM   7772  CG  TYR B 325     -17.065  18.801  19.064  1.00 45.09           C  
-ANISOU 7772  CG  TYR B 325     5221   5685   6225   1843   -114    -35       C  
-ATOM   7773  CD1 TYR B 325     -16.247  19.843  19.479  1.00 43.55           C  
-ANISOU 7773  CD1 TYR B 325     5139   5311   6097   1780     16    -13       C  
-ATOM   7774  CD2 TYR B 325     -18.126  18.434  19.880  1.00 43.92           C  
-ANISOU 7774  CD2 TYR B 325     5044   5609   6036   1837   -210    -38       C  
-ATOM   7775  CE1 TYR B 325     -16.479  20.498  20.670  1.00 42.22           C  
-ANISOU 7775  CE1 TYR B 325     5057   5039   5947   1720     41     -1       C  
-ATOM   7776  CE2 TYR B 325     -18.363  19.083  21.076  1.00 41.84           C  
-ANISOU 7776  CE2 TYR B 325     4866   5249   5784   1775   -174    -23       C  
-ATOM   7777  CZ  TYR B 325     -17.538  20.114  21.464  1.00 42.25           C  
-ANISOU 7777  CZ  TYR B 325     5035   5123   5895   1720    -52     -7       C  
-ATOM   7778  OH  TYR B 325     -17.773  20.763  22.652  1.00 43.15           O  
-ANISOU 7778  OH  TYR B 325     5238   5140   6017   1666    -23      1       O  
-ATOM   7779  N   THR B 326     -16.046  18.476  14.576  1.00 48.95           N  
-ANISOU 7779  N   THR B 326     5642   6404   6553   2198     64     15       N  
-ATOM   7780  CA  THR B 326     -15.489  17.761  13.434  1.00 50.01           C  
-ANISOU 7780  CA  THR B 326     5698   6626   6679   2243     38    -26       C  
-ATOM   7781  C   THR B 326     -13.967  17.851  13.499  1.00 50.59           C  
-ANISOU 7781  C   THR B 326     5767   6564   6892   2100    104    -72       C  
-ATOM   7782  O   THR B 326     -13.413  18.332  14.484  1.00 48.73           O  
-ANISOU 7782  O   THR B 326     5576   6173   6767   1962    138    -81       O  
-ATOM   7783  CB  THR B 326     -15.967  18.348  12.086  1.00 51.16           C  
-ANISOU 7783  CB  THR B 326     5918   6857   6663   2458    163     61       C  
-ATOM   7784  OG1 THR B 326     -15.128  19.448  11.714  1.00 49.70           O  
-ANISOU 7784  OG1 THR B 326     5850   6545   6488   2458    371    127       O  
-ATOM   7785  CG2 THR B 326     -17.424  18.808  12.168  1.00 49.53           C  
-ANISOU 7785  CG2 THR B 326     5768   6722   6329   2602    161    131       C  
-ATOM   7786  N   LYS B 327     -13.298  17.406  12.441  1.00 47.54           N  
-ANISOU 7786  N   LYS B 327     5326   6235   6502   2138    123   -104       N  
-ATOM   7787  CA  LYS B 327     -11.837  17.354  12.414  1.00 48.48           C  
-ANISOU 7787  CA  LYS B 327     5415   6242   6765   2004    176   -161       C  
-ATOM   7788  C   LYS B 327     -11.145  18.699  12.649  1.00 52.00           C  
-ANISOU 7788  C   LYS B 327     5988   6504   7264   1956    385    -88       C  
-ATOM   7789  O   LYS B 327     -10.011  18.736  13.118  1.00 53.27           O  
-ANISOU 7789  O   LYS B 327     6125   6529   7586   1803    405   -144       O  
-ATOM   7790  CB  LYS B 327     -11.345  16.738  11.094  1.00 47.90           C  
-ANISOU 7790  CB  LYS B 327     5269   6279   6650   2085    187   -198       C  
-ATOM   7791  CG  LYS B 327     -10.770  15.334  11.232  1.00 43.08           C  
-ANISOU 7791  CG  LYS B 327     4493   5719   6155   1976    -11   -341       C  
-ATOM   7792  CD  LYS B 327     -10.815  14.570   9.928  1.00 40.06           C  
-ANISOU 7792  CD  LYS B 327     4035   5504   5681   2109    -52   -377       C  
-ATOM   7793  CE  LYS B 327     -10.280  13.151  10.109  1.00 39.26           C  
-ANISOU 7793  CE  LYS B 327     3766   5450   5702   2002   -266   -525       C  
-ATOM   7794  NZ  LYS B 327     -10.598  12.252   8.947  1.00 39.28           N  
-ANISOU 7794  NZ  LYS B 327     3683   5638   5604   2146   -358   -571       N  
-ATOM   7795  N   SER B 328     -11.815  19.799  12.321  1.00 51.59           N  
-ANISOU 7795  N   SER B 328     6070   6443   7089   2088    533     32       N  
-ATOM   7796  CA  SER B 328     -11.178  21.111  12.403  1.00 56.77           C  
-ANISOU 7796  CA  SER B 328     6851   6928   7792   2059    737    112       C  
-ATOM   7797  C   SER B 328     -11.762  21.991  13.500  1.00 58.93           C  
-ANISOU 7797  C   SER B 328     7226   7093   8073   2033    758    162       C  
-ATOM   7798  O   SER B 328     -11.194  23.034  13.833  1.00 60.27           O  
-ANISOU 7798  O   SER B 328     7491   7095   8315   1979    895    211       O  
-ATOM   7799  CB  SER B 328     -11.284  21.839  11.066  1.00 57.79           C  
-ANISOU 7799  CB  SER B 328     7073   7104   7780   2228    921    220       C  
-ATOM   7800  OG  SER B 328     -12.561  22.428  10.921  1.00 55.79           O  
-ANISOU 7800  OG  SER B 328     6916   6913   7367   2387    944    311       O  
-ATOM   7801  N   THR B 329     -12.897  21.565  14.050  1.00 71.84           N  
-ANISOU 7801  N   THR B 329     8835   8823   9637   2072    622    149       N  
-ATOM   7802  CA  THR B 329     -13.614  22.332  15.064  1.00 72.59           C  
-ANISOU 7802  CA  THR B 329     9020   8843   9717   2068    634    192       C  
-ATOM   7803  C   THR B 329     -13.537  21.676  16.443  1.00 70.88           C  
-ANISOU 7803  C   THR B 329     8738   8580   9614   1903    472     99       C  
-ATOM   7804  O   THR B 329     -14.493  21.720  17.218  1.00 71.43           O  
-ANISOU 7804  O   THR B 329     8827   8680   9633   1919    407    108       O  
-ATOM   7805  CB  THR B 329     -15.088  22.495  14.676  1.00 75.22           C  
-ANISOU 7805  CB  THR B 329     9390   9318   9873   2254    623    258       C  
-ATOM   7806  OG1 THR B 329     -15.626  21.217  14.318  1.00 75.94           O  
-ANISOU 7806  OG1 THR B 329     9350   9586   9916   2292    458    196       O  
-ATOM   7807  CG2 THR B 329     -15.221  23.434  13.495  1.00 75.18           C  
-ANISOU 7807  CG2 THR B 329     9495   9321   9750   2420    798    367       C  
-ATOM   7808  N   LEU B 330     -12.389  21.078  16.741  1.00 52.46           N  
-ANISOU 7808  N   LEU B 330     6330   6171   7433   1745    410      9       N  
-ATOM   7809  CA  LEU B 330     -12.173  20.384  18.003  1.00 49.50           C  
-ANISOU 7809  CA  LEU B 330     5896   5741   7172   1579    245    -85       C  
-ATOM   7810  C   LEU B 330     -11.754  21.353  19.110  1.00 52.41           C  
-ANISOU 7810  C   LEU B 330     6371   5910   7633   1479    310    -74       C  
-ATOM   7811  O   LEU B 330     -10.588  21.398  19.501  1.00 51.60           O  
-ANISOU 7811  O   LEU B 330     6259   5660   7688   1342    311   -132       O  
-ATOM   7812  CB  LEU B 330     -11.104  19.313  17.813  1.00 42.56           C  
-ANISOU 7812  CB  LEU B 330     4889   4860   6420   1459    137   -194       C  
-ATOM   7813  CG  LEU B 330     -11.297  17.992  18.552  1.00 35.03           C  
-ANISOU 7813  CG  LEU B 330     3821   3971   5516   1355    -96   -294       C  
-ATOM   7814  CD1 LEU B 330     -12.747  17.543  18.466  1.00 31.91           C  
-ANISOU 7814  CD1 LEU B 330     3400   3753   4973   1471   -180   -258       C  
-ATOM   7815  CD2 LEU B 330     -10.374  16.935  17.981  1.00 32.05           C  
-ANISOU 7815  CD2 LEU B 330     3313   3630   5235   1288   -193   -393       C  
-ATOM   7816  N   ILE B 331     -12.715  22.122  19.614  1.00 70.97           N  
-ANISOU 7816  N   ILE B 331     8818   8255   9891   1554    358     -7       N  
-ATOM   7817  CA  ILE B 331     -12.452  23.122  20.647  1.00 74.06           C  
-ANISOU 7817  CA  ILE B 331     9323   8465  10352   1484    421      7       C  
-ATOM   7818  C   ILE B 331     -13.495  23.053  21.760  1.00 73.34           C  
-ANISOU 7818  C   ILE B 331     9260   8410  10196   1482    330      1       C  
-ATOM   7819  O   ILE B 331     -14.686  22.874  21.496  1.00 73.70           O  
-ANISOU 7819  O   ILE B 331     9290   8608  10103   1602    311     42       O  
-ATOM   7820  CB  ILE B 331     -12.452  24.552  20.055  1.00 79.42           C  
-ANISOU 7820  CB  ILE B 331    10129   9060  10986   1596    629    115       C  
-ATOM   7821  CG1 ILE B 331     -11.354  24.692  19.006  1.00 83.21           C  
-ANISOU 7821  CG1 ILE B 331    10590   9491  11536   1588    739    129       C  
-ATOM   7822  CG2 ILE B 331     -12.236  25.585  21.142  1.00 79.57           C  
-ANISOU 7822  CG2 ILE B 331    10264   8891  11079   1533    681    125       C  
-ATOM   7823  CD1 ILE B 331      -9.972  24.448  19.562  1.00 90.49           C  
-ANISOU 7823  CD1 ILE B 331    11467  10254  12661   1402    700     39       C  
-ATOM   7824  N   GLY B 332     -13.048  23.193  23.005  1.00 60.50           N  
-ANISOU 7824  N   GLY B 332     7674   6642   8670   1347    275    -53       N  
-ATOM   7825  CA  GLY B 332     -13.967  23.222  24.129  1.00 59.35           C  
-ANISOU 7825  CA  GLY B 332     7570   6518   8462   1339    208    -57       C  
-ATOM   7826  C   GLY B 332     -13.688  22.211  25.223  1.00 57.18           C  
-ANISOU 7826  C   GLY B 332     7238   6224   8265   1177     25   -154       C  
-ATOM   7827  O   GLY B 332     -13.090  21.164  24.983  1.00 55.65           O  
-ANISOU 7827  O   GLY B 332     6937   6063   8144   1091    -89   -222       O  
-ATOM   7828  N   GLU B 333     -14.141  22.530  26.432  1.00 69.84           N  
-ANISOU 7828  N   GLU B 333     8917   7773   9846   1140     -4   -162       N  
-ATOM   7829  CA  GLU B 333     -13.881  21.705  27.606  1.00 67.74           C  
-ANISOU 7829  CA  GLU B 333     8627   7467   9643    984   -170   -247       C  
-ATOM   7830  C   GLU B 333     -14.453  20.304  27.441  1.00 64.39           C  
-ANISOU 7830  C   GLU B 333     8071   7222   9172    965   -320   -275       C  
-ATOM   7831  O   GLU B 333     -13.932  19.343  28.003  1.00 62.07           O  
-ANISOU 7831  O   GLU B 333     7721   6903   8961    825   -476   -354       O  
-ATOM   7832  CB  GLU B 333     -14.457  22.362  28.860  1.00 70.42           C  
-ANISOU 7832  CB  GLU B 333     9082   7742   9931    978   -156   -237       C  
-ATOM   7833  CG  GLU B 333     -15.954  22.634  28.791  1.00 76.03           C  
-ANISOU 7833  CG  GLU B 333     9807   8607  10473   1121    -96   -165       C  
-ATOM   7834  CD  GLU B 333     -16.555  22.969  30.149  1.00 80.41           C  
-ANISOU 7834  CD  GLU B 333    10452   9127  10975   1094   -114   -174       C  
-ATOM   7835  OE1 GLU B 333     -16.151  22.338  31.154  1.00 84.17           O  
-ANISOU 7835  OE1 GLU B 333    10931   9545  11505    951   -241   -242       O  
-ATOM   7836  OE2 GLU B 333     -17.426  23.867  30.211  1.00 83.61           O  
-ANISOU 7836  OE2 GLU B 333    10928   9560  11279   1217     -2   -116       O  
-ATOM   7837  N   ASP B 334     -15.522  20.195  26.660  1.00 64.37           N  
-ANISOU 7837  N   ASP B 334     8020   7393   9043   1107   -280   -213       N  
-ATOM   7838  CA  ASP B 334     -16.137  18.905  26.375  1.00 62.11           C  
-ANISOU 7838  CA  ASP B 334     7602   7282   8715   1107   -418   -234       C  
-ATOM   7839  C   ASP B 334     -15.133  17.951  25.749  1.00 60.22           C  
-ANISOU 7839  C   ASP B 334     7255   7043   8584   1026   -520   -303       C  
-ATOM   7840  O   ASP B 334     -15.314  16.732  25.772  1.00 58.64           O  
-ANISOU 7840  O   ASP B 334     6943   6941   8396    972   -678   -348       O  
-ATOM   7841  CB  ASP B 334     -17.327  19.081  25.428  1.00 64.32           C  
-ANISOU 7841  CB  ASP B 334     7849   7732   8857   1293   -344   -157       C  
-ATOM   7842  CG  ASP B 334     -18.595  19.491  26.153  1.00 66.23           C  
-ANISOU 7842  CG  ASP B 334     8141   8034   8989   1358   -311   -111       C  
-ATOM   7843  OD1 ASP B 334     -18.654  19.330  27.394  1.00 67.99           O  
-ANISOU 7843  OD1 ASP B 334     8399   8204   9231   1249   -375   -143       O  
-ATOM   7844  OD2 ASP B 334     -19.537  19.964  25.483  1.00 67.02           O  
-ANISOU 7844  OD2 ASP B 334     8245   8235   8983   1521   -223    -46       O  
-ATOM   7845  N   VAL B 335     -14.061  18.515  25.207  1.00 42.50           N  
-ANISOU 7845  N   VAL B 335     5042   4682   6425   1016   -429   -312       N  
-ATOM   7846  CA  VAL B 335     -13.167  17.764  24.350  1.00 40.26           C  
-ANISOU 7846  CA  VAL B 335     4653   4416   6229    977   -485   -368       C  
-ATOM   7847  C   VAL B 335     -11.703  17.867  24.761  1.00 44.60           C  
-ANISOU 7847  C   VAL B 335     5220   4774   6952    829   -504   -444       C  
-ATOM   7848  O   VAL B 335     -10.911  16.978  24.464  1.00 43.91           O  
-ANISOU 7848  O   VAL B 335     5032   4687   6964    747   -610   -524       O  
-ATOM   7849  CB  VAL B 335     -13.352  18.215  22.895  1.00 35.21           C  
-ANISOU 7849  CB  VAL B 335     4003   3865   5511   1142   -344   -301       C  
-ATOM   7850  CG1 VAL B 335     -12.029  18.583  22.262  1.00 31.16           C  
-ANISOU 7850  CG1 VAL B 335     3494   3235   5111   1104   -254   -324       C  
-ATOM   7851  CG2 VAL B 335     -14.067  17.135  22.104  1.00 30.50           C  
-ANISOU 7851  CG2 VAL B 335     3281   3471   4837   1220   -448   -308       C  
-ATOM   7852  N   ASN B 336     -11.355  18.939  25.465  1.00 62.84           N  
-ANISOU 7852  N   ASN B 336     7653   6919   9304    797   -409   -426       N  
-ATOM   7853  CA  ASN B 336      -9.962  19.206  25.826  1.00 69.06           C  
-ANISOU 7853  CA  ASN B 336     8465   7507  10268    668   -410   -495       C  
-ATOM   7854  C   ASN B 336      -9.639  19.120  27.319  1.00 74.96           C  
-ANISOU 7854  C   ASN B 336     9274   8113  11096    525   -529   -562       C  
-ATOM   7855  O   ASN B 336      -9.577  20.145  28.005  1.00 74.11           O  
-ANISOU 7855  O   ASN B 336     9289   7871  11000    522   -449   -538       O  
-ATOM   7856  CB  ASN B 336      -9.533  20.580  25.305  1.00 70.98           C  
-ANISOU 7856  CB  ASN B 336     8800   7636  10534    740   -199   -428       C  
-ATOM   7857  CG  ASN B 336      -9.591  20.675  23.800  1.00 71.79           C  
-ANISOU 7857  CG  ASN B 336     8852   7850  10575    866    -78   -369       C  
-ATOM   7858  OD1 ASN B 336      -9.283  19.716  23.093  1.00 72.79           O  
-ANISOU 7858  OD1 ASN B 336     8859   8072  10725    854   -151   -416       O  
-ATOM   7859  ND2 ASN B 336      -9.986  21.840  23.297  1.00 73.72           N  
-ANISOU 7859  ND2 ASN B 336     9191   8081  10738    992    105   -266       N  
-ATOM   7860  N   PRO B 337      -9.413  17.897  27.823  1.00 70.81           N  
-ANISOU 7860  N   PRO B 337     8667   7611  10626    407   -729   -648       N  
-ATOM   7861  CA  PRO B 337      -8.932  17.705  29.193  1.00 76.16           C  
-ANISOU 7861  CA  PRO B 337     9403   8142  11393    259   -862   -724       C  
-ATOM   7862  C   PRO B 337      -7.448  18.047  29.298  1.00 80.93           C  
-ANISOU 7862  C   PRO B 337    10019   8537  12194    156   -859   -802       C  
-ATOM   7863  O   PRO B 337      -6.719  17.937  28.309  1.00 79.94           O  
-ANISOU 7863  O   PRO B 337     9810   8411  12154    164   -811   -823       O  
-ATOM   7864  CB  PRO B 337      -9.139  16.209  29.420  1.00 73.49           C  
-ANISOU 7864  CB  PRO B 337     8958   7912  11053    178  -1074   -785       C  
-ATOM   7865  CG  PRO B 337      -8.997  15.622  28.071  1.00 73.05           C  
-ANISOU 7865  CG  PRO B 337     8768   7983  11005    239  -1064   -788       C  
-ATOM   7866  CD  PRO B 337      -9.620  16.613  27.132  1.00 71.36           C  
-ANISOU 7866  CD  PRO B 337     8592   7846  10676    410   -851   -680       C  
-ATOM   7867  N   LEU B 338      -7.015  18.463  30.484  1.00122.63           N  
-ANISOU 7867  N   LEU B 338    21335  12258  12999  -1100   2471  -4410       N  
-ATOM   7868  CA  LEU B 338      -5.621  18.820  30.721  1.00126.84           C  
-ANISOU 7868  CA  LEU B 338    21861  12666  13666   -752   2291  -4268       C  
-ATOM   7869  C   LEU B 338      -4.736  17.576  30.738  1.00127.42           C  
-ANISOU 7869  C   LEU B 338    22464  12635  13313   -631   2435  -4039       C  
-ATOM   7870  O   LEU B 338      -5.102  16.554  31.318  1.00129.41           O  
-ANISOU 7870  O   LEU B 338    23096  12869  13205   -799   2638  -4050       O  
-ATOM   7871  CB  LEU B 338      -5.491  19.578  32.044  1.00138.20           C  
-ANISOU 7871  CB  LEU B 338    23103  14071  15334   -692   2144  -4437       C  
-ATOM   7872  CG  LEU B 338      -5.944  21.042  32.080  1.00145.63           C  
-ANISOU 7872  CG  LEU B 338    23457  15060  16815   -699   1924  -4631       C  
-ATOM   7873  CD1 LEU B 338      -4.940  21.921  31.363  1.00150.25           C  
-ANISOU 7873  CD1 LEU B 338    23743  15551  17793   -394   1677  -4484       C  
-ATOM   7874  CD2 LEU B 338      -7.339  21.225  31.495  1.00152.71           C  
-ANISOU 7874  CD2 LEU B 338    24139  16094  17788  -1000   2012  -4787       C  
-ATOM   7875  N   ILE B 339      -3.573  17.665  30.098  1.00 99.05           N  
-ANISOU 7875  N   ILE B 339    18890   8961   9784   -337   2330  -3828       N  
-ATOM   7876  CA  ILE B 339      -2.650  16.536  30.033  1.00 98.73           C  
-ANISOU 7876  CA  ILE B 339    19329   8813   9372   -195   2456  -3598       C  
-ATOM   7877  C   ILE B 339      -1.226  16.944  30.403  1.00101.15           C  
-ANISOU 7877  C   ILE B 339    19616   8989   9827    168   2270  -3458       C  
-ATOM   7878  O   ILE B 339      -0.941  18.117  30.642  1.00100.71           O  
-ANISOU 7878  O   ILE B 339    19163   8919  10182    313   2037  -3528       O  
-ATOM   7879  CB  ILE B 339      -2.598  15.935  28.621  1.00 92.25           C  
-ANISOU 7879  CB  ILE B 339    18638   8028   8383   -200   2573  -3429       C  
-ATOM   7880  CG1 ILE B 339      -1.790  16.850  27.699  1.00 88.19           C  
-ANISOU 7880  CG1 ILE B 339    17794   7506   8210     80   2365  -3313       C  
-ATOM   7881  CG2 ILE B 339      -3.997  15.720  28.081  1.00 92.29           C  
-ANISOU 7881  CG2 ILE B 339    18580   8175   8310   -545   2722  -3565       C  
-ATOM   7882  CD1 ILE B 339      -0.995  16.116  26.645  1.00 82.61           C  
-ANISOU 7882  CD1 ILE B 339    17310   6785   7293    233   2447  -3021       C  
-ATOM   7883  N   LYS B 340      -0.335  15.960  30.443  1.00110.40           N  
-ANISOU 7883  N   LYS B 340    21216  10052  10679    311   2374  -3253       N  
-ATOM   7884  CA  LYS B 340       1.087  16.213  30.629  1.00112.56           C  
-ANISOU 7884  CA  LYS B 340    21512  10196  11058    669   2219  -3079       C  
-ATOM   7885  C   LYS B 340       1.843  15.823  29.358  1.00113.52           C  
-ANISOU 7885  C   LYS B 340    21743  10283  11106    858   2254  -2833       C  
-ATOM   7886  O   LYS B 340       1.582  14.774  28.765  1.00112.97           O  
-ANISOU 7886  O   LYS B 340    21995  10235  10694    732   2470  -2750       O  
-ATOM   7887  CB  LYS B 340       1.629  15.423  31.823  1.00114.08           C  
-ANISOU 7887  CB  LYS B 340    22113  10279  10955    712   2299  -3038       C  
-ATOM   7888  CG  LYS B 340       0.783  15.510  33.080  1.00116.70           C  
-ANISOU 7888  CG  LYS B 340    22433  10656  11253    481   2330  -3277       C  
-ATOM   7889  CD  LYS B 340       0.844  16.891  33.713  1.00116.24           C  
-ANISOU 7889  CD  LYS B 340    21912  10630  11625    573   2077  -3442       C  
-ATOM   7890  CE  LYS B 340      -0.013  16.962  34.972  1.00117.62           C  
-ANISOU 7890  CE  LYS B 340    22074  10864  11751    339   2121  -3693       C  
-ATOM   7891  NZ  LYS B 340       0.040  18.309  35.606  1.00116.59           N  
-ANISOU 7891  NZ  LYS B 340    21485  10764  12048    423   1877  -3868       N  
-ATOM   7892  N   LEU B 341       2.776  16.673  28.939  1.00130.01           N  
-ANISOU 7892  N   LEU B 341    23493  12353  13552   1139   2022  -2620       N  
-ATOM   7893  CA  LEU B 341       3.557  16.413  27.735  1.00131.29           C  
-ANISOU 7893  CA  LEU B 341    23644  12536  13703   1318   2013  -2272       C  
-ATOM   7894  C   LEU B 341       5.011  16.086  28.066  1.00131.68           C  
-ANISOU 7894  C   LEU B 341    23919  12434  13679   1640   1956  -2030       C  
-ATOM   7895  O   LEU B 341       5.837  16.980  28.245  1.00131.65           O  
-ANISOU 7895  O   LEU B 341    23590  12402  14030   1880   1709  -1871       O  
-ATOM   7896  CB  LEU B 341       3.476  17.599  26.783  1.00130.71           C  
-ANISOU 7896  CB  LEU B 341    22951  12607  14106   1368   1786  -2110       C  
-ATOM   7897  N   ALA B 344       5.413  20.769  31.266  1.00109.33           N  
-ANISOU 7897  N   ALA B 344    19511   9562  12469   1946    989  -2432       N  
-ATOM   7898  CA  ALA B 344       4.894  19.574  30.616  1.00110.28           C  
-ANISOU 7898  CA  ALA B 344    20044   9714  12144   1771   1269  -2432       C  
-ATOM   7899  C   ALA B 344       3.455  19.295  31.041  1.00111.32           C  
-ANISOU 7899  C   ALA B 344    20294   9912  12092   1416   1448  -2807       C  
-ATOM   7900  O   ALA B 344       3.080  18.147  31.259  1.00112.38           O  
-ANISOU 7900  O   ALA B 344    20925  10011  11762   1264   1704  -2926       O  
-ATOM   7901  CB  ALA B 344       5.784  18.378  30.917  1.00109.12           C  
-ANISOU 7901  CB  ALA B 344    20468   9433  11561   1910   1426  -2300       C  
-ATOM   7902  N   VAL B 345       2.660  20.353  31.166  1.00121.54           N  
-ANISOU 7902  N   VAL B 345    21123  11295  13760   1287   1312  -2992       N  
-ATOM   7903  CA  VAL B 345       1.246  20.221  31.505  1.00122.34           C  
-ANISOU 7903  CA  VAL B 345    21268  11473  13743    948   1462  -3345       C  
-ATOM   7904  C   VAL B 345       0.396  20.909  30.441  1.00122.46           C  
-ANISOU 7904  C   VAL B 345    20828  11638  14062    801   1401  -3324       C  
-ATOM   7905  O   VAL B 345      -0.408  21.790  30.737  1.00119.91           O  
-ANISOU 7905  O   VAL B 345    20128  11381  14052    660   1303  -3538       O  
-ATOM   7906  CB  VAL B 345       0.927  20.822  32.893  1.00123.14           C  
-ANISOU 7906  CB  VAL B 345    21252  11549  13987    884   1376  -3649       C  
-ATOM   7907  CG1 VAL B 345      -0.502  20.491  33.304  1.00127.93           C  
-ANISOU 7907  CG1 VAL B 345    21912  12293  14401    510   1552  -3898       C  
-ATOM   7908  CG2 VAL B 345       1.910  20.308  33.934  1.00126.96           C  
-ANISOU 7908  CG2 VAL B 345    22069  11935  14235   1050   1379  -3565       C  
-ATOM   7909  N   ASN B 346       0.586  20.499  29.195  1.00121.96           N  
-ANISOU 7909  N   ASN B 346    20797  11635  13907    834   1460  -3063       N  
-ATOM   7910  CA  ASN B 346      -0.114  21.107  28.074  1.00120.87           C  
-ANISOU 7910  CA  ASN B 346    20229  11653  14042    712   1397  -2990       C  
-ATOM   7911  C   ASN B 346      -1.489  20.477  27.866  1.00124.02           C  
-ANISOU 7911  C   ASN B 346    20821  12146  14156    356   1637  -3237       C  
-ATOM   7912  O   ASN B 346      -1.952  19.691  28.686  1.00119.82           O  
-ANISOU 7912  O   ASN B 346    20713  11556  13259    201   1833  -3491       O  
-ATOM   7913  CB  ASN B 346       0.737  20.976  26.803  1.00119.02           C  
-ANISOU 7913  CB  ASN B 346    19924  11461  13839    908   1346  -2589       C  
-ATOM   7914  CG  ASN B 346       0.176  21.762  25.634  1.00121.90           C  
-ANISOU 7914  CG  ASN B 346    19771  11998  14548    822   1233  -2464       C  
-ATOM   7915  OD1 ASN B 346      -0.624  22.680  25.813  1.00122.21           O  
-ANISOU 7915  OD1 ASN B 346    19399  12104  14933    685   1120  -2630       O  
-ATOM   7916  ND2 ASN B 346       0.592  21.401  24.425  1.00124.96           N  
-ANISOU 7916  ND2 ASN B 346    20173  12463  14844    898   1265  -2168       N  
-ATOM   7917  N   VAL B 347      -2.144  20.850  26.774  1.00131.92           N  
-ANISOU 7917  N   VAL B 347    21493  13297  15332    226   1615  -3158       N  
-ATOM   7918  CA  VAL B 347      -3.370  20.194  26.340  1.00138.14           C  
-ANISOU 7918  CA  VAL B 347    22461  14189  15837    -99   1844  -3333       C  
-ATOM   7919  C   VAL B 347      -3.051  19.399  25.075  1.00141.98           C  
-ANISOU 7919  C   VAL B 347    23142  14741  16062    -71   1967  -3064       C  
-ATOM   7920  O   VAL B 347      -2.297  19.865  24.216  1.00140.59           O  
-ANISOU 7920  O   VAL B 347    22681  14614  16123    130   1809  -2748       O  
-ATOM   7921  CB  VAL B 347      -4.502  21.210  26.075  1.00136.32           C  
-ANISOU 7921  CB  VAL B 347    21705  14096  15996   -308   1739  -3476       C  
-ATOM   7922  CG1 VAL B 347      -4.779  21.334  24.587  1.00143.61           C  
-ANISOU 7922  CG1 VAL B 347    22364  15185  17016   -372   1727  -3242       C  
-ATOM   7923  CG2 VAL B 347      -5.760  20.799  26.820  1.00143.65           C  
-ANISOU 7923  CG2 VAL B 347    22856  15034  16692   -625   1931  -3869       C  
-ATOM   7924  N   ASP B 348      -3.613  18.199  24.972  1.00154.62           N  
-ANISOU 7924  N   ASP B 348    25227  16346  17176   -272   2248  -3192       N  
-ATOM   7925  CA  ASP B 348      -3.264  17.268  23.901  1.00158.81           C  
-ANISOU 7925  CA  ASP B 348    26033  16917  17391   -247   2400  -2973       C  
-ATOM   7926  C   ASP B 348      -2.987  17.961  22.566  1.00159.56           C  
-ANISOU 7926  C   ASP B 348    25662  17165  17799   -152   2237  -2664       C  
-ATOM   7927  O   ASP B 348      -3.777  18.778  22.104  1.00157.13           O  
-ANISOU 7927  O   ASP B 348    24905  17001  17796   -299   2135  -2697       O  
-ATOM   7928  CB  ASP B 348      -4.355  16.209  23.736  1.00163.81           C  
-ANISOU 7928  CB  ASP B 348    27056  17598  17586   -567   2696  -3193       C  
-ATOM   7929  CG  ASP B 348      -3.951  15.103  22.783  1.00169.07           C  
-ANISOU 7929  CG  ASP B 348    28084  18278  17875   -541   2882  -3005       C  
-ATOM   7930  OD1 ASP B 348      -3.197  14.201  23.205  1.00173.62           O  
-ANISOU 7930  OD1 ASP B 348    29127  18704  18137   -408   3002  -2966       O  
-ATOM   7931  OD2 ASP B 348      -4.385  15.135  21.612  1.00172.47           O  
-ANISOU 7931  OD2 ASP B 348    28329  18875  18328   -655   2908  -2898       O  
-ATOM   7932  N   GLU B 349      -1.853  17.629  21.956  1.00144.64           N  
-ANISOU 7932  N   GLU B 349    23876  15246  15833     95   2212  -2358       N  
-ATOM   7933  CA  GLU B 349      -1.456  18.224  20.683  1.00142.83           C  
-ANISOU 7933  CA  GLU B 349    23229  15165  15873    210   2059  -2035       C  
-ATOM   7934  C   GLU B 349      -2.374  17.775  19.551  1.00143.68           C  
-ANISOU 7934  C   GLU B 349    23338  15461  15792    -51   2219  -2039       C  
-ATOM   7935  O   GLU B 349      -3.160  16.842  19.713  1.00146.66           O  
-ANISOU 7935  O   GLU B 349    24112  15831  15780   -290   2468  -2267       O  
-ATOM   7936  CB  GLU B 349      -0.007  17.855  20.353  1.00143.76           C  
-ANISOU 7936  CB  GLU B 349    23517  15201  15905    533   2020  -1720       C  
-ATOM   7937  CG  GLU B 349       0.227  16.360  20.182  1.00143.85           C  
-ANISOU 7937  CG  GLU B 349    24156  15141  15358    505   2307  -1728       C  
-ATOM   7938  CD  GLU B 349       1.683  16.014  19.932  1.00141.73           C  
-ANISOU 7938  CD  GLU B 349    24052  14777  15021    834   2267  -1425       C  
-ATOM   7939  OE1 GLU B 349       2.062  15.850  18.753  1.00140.09           O  
-ANISOU 7939  OE1 GLU B 349    23762  14684  14782    902   2275  -1175       O  
-ATOM   7940  OE2 GLU B 349       2.447  15.902  20.915  1.00139.45           O  
-ANISOU 7940  OE2 GLU B 349    23973  14305  14707   1021   2228  -1437       O  
-ATOM   7941  N   ILE B 350      -2.272  18.444  18.407  1.00124.42           N  
-ANISOU 7941  N   ILE B 350    20448  13195  13631     -7   2071  -1782       N  
-ATOM   7942  CA  ILE B 350      -3.044  18.060  17.232  1.00123.57           C  
-ANISOU 7942  CA  ILE B 350    20307  13289  13355   -237   2206  -1747       C  
-ATOM   7943  C   ILE B 350      -2.618  16.668  16.773  1.00122.29           C  
-ANISOU 7943  C   ILE B 350    20702  13094  12669   -221   2459  -1687       C  
-ATOM   7944  O   ILE B 350      -1.453  16.443  16.445  1.00122.65           O  
-ANISOU 7944  O   ILE B 350    20841  13090  12672     43   2418  -1433       O  
-ATOM   7945  CB  ILE B 350      -2.851  19.058  16.073  1.00119.19           C  
-ANISOU 7945  CB  ILE B 350    19149  12934  13205   -159   1981  -1437       C  
-ATOM   7946  CG1 ILE B 350      -3.054  20.499  16.554  1.00118.35           C  
-ANISOU 7946  CG1 ILE B 350    18467  12829  13670   -117   1702  -1456       C  
-ATOM   7947  CG2 ILE B 350      -3.799  18.737  14.927  1.00121.14           C  
-ANISOU 7947  CG2 ILE B 350    19326  13409  13291   -435   2114  -1431       C  
-ATOM   7948  CD1 ILE B 350      -4.480  20.822  16.946  1.00113.32           C  
-ANISOU 7948  CD1 ILE B 350    17685  12247  13123   -434   1748  -1768       C  
-ATOM   7949  N   MET B 351      -3.568  15.737  16.752  1.00159.25           N  
-ANISOU 7949  N   MET B 351    25747  17800  16961   -504   2720  -1925       N  
-ATOM   7950  CA  MET B 351      -3.283  14.341  16.422  1.00153.15           C  
-ANISOU 7950  CA  MET B 351    25539  16975  15677   -521   2986  -1920       C  
-ATOM   7951  C   MET B 351      -2.763  14.154  14.997  1.00145.52           C  
-ANISOU 7951  C   MET B 351    24462  16170  14658   -437   2989  -1618       C  
-ATOM   7952  O   MET B 351      -2.247  13.092  14.649  1.00143.24           O  
-ANISOU 7952  O   MET B 351    24596  15830  14000   -379   3174  -1556       O  
-ATOM   7953  CB  MET B 351      -4.529  13.479  16.648  1.00163.04           C  
-ANISOU 7953  CB  MET B 351    27146  18237  16563   -868   3253  -2245       C  
-ATOM   7954  CG  MET B 351      -5.784  14.021  15.981  1.00173.08           C  
-ANISOU 7954  CG  MET B 351    28041  19733  17987  -1160   3232  -2329       C  
-ATOM   7955  SD  MET B 351      -7.274  13.101  16.421  1.00183.96           S  
-ANISOU 7955  SD  MET B 351    29820  21106  18970  -1565   3527  -2732       S  
-ATOM   7956  CE  MET B 351      -8.525  14.057  15.567  1.00190.10           C  
-ANISOU 7956  CE  MET B 351    30013  22160  20058  -1838   3421  -2748       C  
-ATOM   7957  N   THR B 352      -2.903  15.189  14.177  1.00108.54           N  
-ANISOU 7957  N   THR B 352    19205  11686  10349   -435   2784  -1431       N  
-ATOM   7958  CA  THR B 352      -2.463  15.126  12.790  1.00102.04           C  
-ANISOU 7958  CA  THR B 352    18215  11052   9505   -369   2766  -1136       C  
-ATOM   7959  C   THR B 352      -0.955  15.337  12.682  1.00 98.45           C  
-ANISOU 7959  C   THR B 352    17707  10515   9185     11   2616   -826       C  
-ATOM   7960  O   THR B 352      -0.371  16.106  13.445  1.00101.22           O  
-ANISOU 7960  O   THR B 352    17862  10740   9856    218   2411   -772       O  
-ATOM   7961  CB  THR B 352      -3.189  16.179  11.928  1.00 97.51           C  
-ANISOU 7961  CB  THR B 352    17022  10738   9291   -515   2596  -1031       C  
-ATOM   7962  OG1 THR B 352      -2.734  17.489  12.284  1.00 96.61           O  
-ANISOU 7962  OG1 THR B 352    16405  10598   9705   -318   2288   -887       O  
-ATOM   7963  CG2 THR B 352      -4.691  16.097  12.146  1.00 98.28           C  
-ANISOU 7963  CG2 THR B 352    17131  10904   9307   -882   2719  -1342       C  
-ATOM   7964  N   ASP B 353      -0.330  14.638  11.738  1.00 96.22           N  
-ANISOU 7964  N   ASP B 353    17603  10304   8654     99   2722   -629       N  
-ATOM   7965  CA  ASP B 353       1.092  14.813  11.452  1.00 91.20           C  
-ANISOU 7965  CA  ASP B 353    16896   9621   8135    451   2588   -307       C  
-ATOM   7966  C   ASP B 353       1.335  16.247  10.993  1.00 88.05           C  
-ANISOU 7966  C   ASP B 353    15811   9371   8272    576   2265    -51       C  
-ATOM   7967  O   ASP B 353       2.372  16.841  11.289  1.00 86.05           O  
-ANISOU 7967  O   ASP B 353    15382   9023   8291    873   2064    151       O  
-ATOM   7968  CB  ASP B 353       1.538  13.827  10.365  1.00 88.36           C  
-ANISOU 7968  CB  ASP B 353    16805   9356   7410    475   2773   -158       C  
-ATOM   7969  CG  ASP B 353       3.035  13.875  10.098  1.00 83.70           C  
-ANISOU 7969  CG  ASP B 353    16201   8704   6896    841   2663    163       C  
-ATOM   7970  OD1 ASP B 353       3.478  14.739   9.315  1.00 80.59           O  
-ANISOU 7970  OD1 ASP B 353    15325   8479   6817    972   2450    451       O  
-ATOM   7971  OD2 ASP B 353       3.767  13.032  10.657  1.00 80.51           O  
-ANISOU 7971  OD2 ASP B 353    16269   8086   6237    994   2793    133       O  
-ATOM   7972  N   THR B 354       0.358  16.795  10.277  1.00115.28           N  
-ANISOU 7972  N   THR B 354    18872  13053  11878    342   2216    -59       N  
-ATOM   7973  CA  THR B 354       0.428  18.159   9.765  1.00111.40           C  
-ANISOU 7973  CA  THR B 354    17699  12722  11905    417   1918    179       C  
-ATOM   7974  C   THR B 354       0.713  19.175  10.871  1.00105.85           C  
-ANISOU 7974  C   THR B 354    16736  11848  11636    579   1681    144       C  
-ATOM   7975  O   THR B 354       1.382  20.183  10.635  1.00104.19           O  
-ANISOU 7975  O   THR B 354    16063  11679  11847    791   1415    408       O  
-ATOM   7976  CB  THR B 354      -0.884  18.548   9.053  1.00115.13           C  
-ANISOU 7976  CB  THR B 354    17833  13444  12468     89   1925    105       C  
-ATOM   7977  OG1 THR B 354      -1.156  17.615   8.000  1.00117.97           O  
-ANISOU 7977  OG1 THR B 354    18422  13978  12422    -69   2144    134       O  
-ATOM   7978  CG2 THR B 354      -0.782  19.945   8.473  1.00116.57           C  
-ANISOU 7978  CG2 THR B 354    17297  13796  13198    171   1615    378       C  
-ATOM   7979  N   SER B 355       0.200  18.900  12.070  1.00 83.31           N  
-ANISOU 7979  N   SER B 355    14175   8806   8673    474   1778   -186       N  
-ATOM   7980  CA  SER B 355       0.360  19.783  13.227  1.00 77.86           C  
-ANISOU 7980  CA  SER B 355    13283   7949   8353    593   1581   -280       C  
-ATOM   7981  C   SER B 355      -0.613  20.967  13.227  1.00 73.89           C  
-ANISOU 7981  C   SER B 355    12214   7565   8297    421   1403   -356       C  
-ATOM   7982  O   SER B 355      -0.688  21.713  14.205  1.00 74.42           O  
-ANISOU 7982  O   SER B 355    12097   7505   8674    470   1256   -488       O  
-ATOM   7983  CB  SER B 355       1.805  20.267  13.356  1.00 78.83           C  
-ANISOU 7983  CB  SER B 355    13264   7968   8718    976   1372      9       C  
-ATOM   7984  N   THR B 356      -1.356  21.135  12.136  1.00 73.20           N  
-ANISOU 7984  N   THR B 356    11847   7721   8243    218   1418   -274       N  
-ATOM   7985  CA  THR B 356      -2.398  22.156  12.069  1.00 67.78           C  
-ANISOU 7985  CA  THR B 356    10646   7158   7950     18   1279   -356       C  
-ATOM   7986  C   THR B 356      -3.760  21.495  11.914  1.00 66.16           C  
-ANISOU 7986  C   THR B 356    10657   7051   7428   -356   1519   -632       C  
-ATOM   7987  O   THR B 356      -3.857  20.270  11.879  1.00 66.30           O  
-ANISOU 7987  O   THR B 356    11219   7036   6937   -450   1783   -758       O  
-ATOM   7988  CB  THR B 356      -2.184  23.137  10.898  1.00 65.97           C  
-ANISOU 7988  CB  THR B 356     9788   7155   8123     88   1047      4       C  
-ATOM   7989  OG1 THR B 356      -2.505  22.494   9.656  1.00 64.63           O  
-ANISOU 7989  OG1 THR B 356     9692   7215   7650    -69   1198    124       O  
-ATOM   7990  CG2 THR B 356      -0.745  23.629  10.862  1.00 63.38           C  
-ANISOU 7990  CG2 THR B 356     9289   6749   8042    466    834    320       C  
-ATOM   7991  N   SER B 357      -4.811  22.302  11.815  1.00 79.38           N  
-ANISOU 7991  N   SER B 357    11904   8844   9412   -571   1426   -723       N  
-ATOM   7992  CA  SER B 357      -6.163  21.770  11.674  1.00 78.53           C  
-ANISOU 7992  CA  SER B 357    11956   8838   9042   -936   1637   -984       C  
-ATOM   7993  C   SER B 357      -7.065  22.724  10.892  1.00 76.23           C  
-ANISOU 7993  C   SER B 357    11060   8780   9123  -1130   1496   -894       C  
-ATOM   7994  O   SER B 357      -8.038  23.253  11.432  1.00 77.01           O  
-ANISOU 7994  O   SER B 357    10959   8864   9436  -1318   1465  -1119       O  
-ATOM   7995  CB  SER B 357      -6.768  21.485  13.050  1.00 79.37           C  
-ANISOU 7995  CB  SER B 357    12386   8741   9029  -1055   1754  -1383       C  
-ATOM   7996  OG  SER B 357      -6.869  22.672  13.817  1.00 80.20           O  
-ANISOU 7996  OG  SER B 357    12068   8763   9640   -988   1524  -1448       O  
-ATOM   7997  N   TYR B 358      -6.747  22.924   9.615  1.00 55.00           N  
-ANISOU 7997  N   TYR B 358     8082   6311   6504  -1088   1417   -564       N  
-ATOM   7998  CA  TYR B 358      -7.419  23.928   8.794  1.00 52.39           C  
-ANISOU 7998  CA  TYR B 358     7117   6212   6577  -1229   1245   -405       C  
-ATOM   7999  C   TYR B 358      -8.744  23.488   8.185  1.00 53.10           C  
-ANISOU 7999  C   TYR B 358     7245   6500   6430  -1606   1427   -552       C  
-ATOM   8000  O   TYR B 358      -8.891  22.358   7.716  1.00 53.51           O  
-ANISOU 8000  O   TYR B 358     7735   6622   5976  -1728   1670   -609       O  
-ATOM   8001  CB  TYR B 358      -6.489  24.413   7.679  1.00 52.17           C  
-ANISOU 8001  CB  TYR B 358     6716   6354   6753  -1019   1060     37       C  
-ATOM   8002  CG  TYR B 358      -5.664  25.620   8.055  1.00 51.56           C  
-ANISOU 8002  CG  TYR B 358     6177   6175   7238   -731    747    236       C  
-ATOM   8003  CD1 TYR B 358      -6.220  26.891   8.044  1.00 51.56           C  
-ANISOU 8003  CD1 TYR B 358     5551   6241   7800   -796    518    285       C  
-ATOM   8004  CD2 TYR B 358      -4.329  25.491   8.416  1.00 51.02           C  
-ANISOU 8004  CD2 TYR B 358     6294   5943   7150   -396    680    376       C  
-ATOM   8005  CE1 TYR B 358      -5.473  27.996   8.388  1.00 51.07           C  
-ANISOU 8005  CE1 TYR B 358     5062   6079   8265   -535    231    460       C  
-ATOM   8006  CE2 TYR B 358      -3.571  26.591   8.759  1.00 50.50           C  
-ANISOU 8006  CE2 TYR B 358     5805   5783   7598   -135    393    556       C  
-ATOM   8007  CZ  TYR B 358      -4.150  27.840   8.746  1.00 50.53           C  
-ANISOU 8007  CZ  TYR B 358     5192   5850   8157   -206    169    593       C  
-ATOM   8008  OH  TYR B 358      -3.407  28.945   9.088  1.00 50.57           O  
-ANISOU 8008  OH  TYR B 358     4769   5756   8691     50   -118    767       O  
-ATOM   8009  N   LEU B 359      -9.705  24.404   8.201  1.00 49.21           N  
-ANISOU 8009  N   LEU B 359     5082   7651   5966   2350    228    896       N  
-ATOM   8010  CA  LEU B 359     -10.940  24.252   7.447  1.00 49.30           C  
-ANISOU 8010  CA  LEU B 359     4871   7951   5908   2540    251    944       C  
-ATOM   8011  C   LEU B 359     -10.824  25.113   6.194  1.00 49.82           C  
-ANISOU 8011  C   LEU B 359     4988   8028   5912   2690    279   1022       C  
-ATOM   8012  O   LEU B 359     -10.680  26.337   6.284  1.00 51.31           O  
-ANISOU 8012  O   LEU B 359     5416   8041   6039   2828    367   1087       O  
-ATOM   8013  CB  LEU B 359     -12.140  24.703   8.281  1.00 47.14           C  
-ANISOU 8013  CB  LEU B 359     4629   7735   5547   2742    352    985       C  
-ATOM   8014  CG  LEU B 359     -13.496  24.789   7.569  1.00 46.27           C  
-ANISOU 8014  CG  LEU B 359     4324   7903   5352   2979    395   1051       C  
-ATOM   8015  CD1 LEU B 359     -13.877  23.451   6.942  1.00 43.35           C  
-ANISOU 8015  CD1 LEU B 359     3615   7809   5046   2881    297    999       C  
-ATOM   8016  CD2 LEU B 359     -14.590  25.264   8.520  1.00 44.80           C  
-ANISOU 8016  CD2 LEU B 359     4193   7740   5090   3165    502   1091       C  
-ATOM   8017  N   LEU B 360     -10.872  24.474   5.028  1.00 50.09           N  
-ANISOU 8017  N   LEU B 360     4801   8266   5965   2663    208   1016       N  
-ATOM   8018  CA  LEU B 360     -10.705  25.184   3.767  1.00 51.53           C  
-ANISOU 8018  CA  LEU B 360     5014   8477   6089   2792    226   1090       C  
-ATOM   8019  C   LEU B 360     -11.984  25.156   2.935  1.00 53.41           C  
-ANISOU 8019  C   LEU B 360     5037   9022   6234   3013    246   1146       C  
-ATOM   8020  O   LEU B 360     -12.428  24.087   2.514  1.00 51.98           O  
-ANISOU 8020  O   LEU B 360     4583   9084   6084   2951    169   1094       O  
-ATOM   8021  CB  LEU B 360      -9.550  24.568   2.974  1.00 50.52           C  
-ANISOU 8021  CB  LEU B 360     4829   8315   6051   2579    125   1039       C  
-ATOM   8022  CG  LEU B 360      -9.185  25.265   1.663  1.00 49.80           C  
-ANISOU 8022  CG  LEU B 360     4783   8230   5908   2686    140   1114       C  
-ATOM   8023  CD1 LEU B 360      -9.022  26.755   1.904  1.00 49.45           C  
-ANISOU 8023  CD1 LEU B 360     5034   7955   5799   2852    256   1207       C  
-ATOM   8024  CD2 LEU B 360      -7.926  24.666   1.061  1.00 50.24           C  
-ANISOU 8024  CD2 LEU B 360     4812   8212   6065   2454     47   1057       C  
-ATOM   8025  N   CYS B 361     -12.576  26.325   2.700  1.00 48.30           N  
-ANISOU 8025  N   CYS B 361     4510   8365   5476   3271    350   1251       N  
-ATOM   8026  CA  CYS B 361     -13.799  26.406   1.903  1.00 52.41           C  
-ANISOU 8026  CA  CYS B 361     4839   9173   5900   3500    374   1316       C  
-ATOM   8027  C   CYS B 361     -13.509  26.951   0.514  1.00 54.26           C  
-ANISOU 8027  C   CYS B 361     5076   9463   6076   3606    372   1390       C  
-ATOM   8028  O   CYS B 361     -12.871  27.996   0.369  1.00 53.79           O  
-ANISOU 8028  O   CYS B 361     5255   9189   5994   3666    437   1458       O  
-ATOM   8029  CB  CYS B 361     -14.845  27.281   2.586  1.00 53.50           C  
-ANISOU 8029  CB  CYS B 361     5076   9302   5948   3740    496   1392       C  
-ATOM   8030  SG  CYS B 361     -16.365  27.475   1.619  1.00 51.52           S  
-ANISOU 8030  SG  CYS B 361     4600   9399   5577   4038    530   1483       S  
-ATOM   8031  N   ILE B 362     -14.003  26.252  -0.503  1.00 53.45           N  
-ANISOU 8031  N   ILE B 362     4707   9652   5951   3634    302   1378       N  
-ATOM   8032  CA  ILE B 362     -13.616  26.532  -1.880  1.00 57.97           C  
-ANISOU 8032  CA  ILE B 362     5249  10301   6475   3694    278   1431       C  
-ATOM   8033  C   ILE B 362     -14.788  26.943  -2.771  1.00 64.27           C  
-ANISOU 8033  C   ILE B 362     5908  11369   7144   3973    314   1523       C  
-ATOM   8034  O   ILE B 362     -15.793  26.237  -2.861  1.00 63.55           O  
-ANISOU 8034  O   ILE B 362     5570  11544   7033   4022    274   1490       O  
-ATOM   8035  CB  ILE B 362     -12.884  25.320  -2.491  1.00 54.42           C  
-ANISOU 8035  CB  ILE B 362     4619   9944   6116   3451    145   1325       C  
-ATOM   8036  CG1 ILE B 362     -11.722  24.916  -1.581  1.00 50.02           C  
-ANISOU 8036  CG1 ILE B 362     4199   9117   5690   3176    109   1239       C  
-ATOM   8037  CG2 ILE B 362     -12.396  25.637  -3.897  1.00 53.86           C  
-ANISOU 8037  CG2 ILE B 362     4536   9937   5993   3508    125   1379       C  
-ATOM   8038  CD1 ILE B 362     -10.984  23.686  -2.026  1.00 45.18           C  
-ANISOU 8038  CD1 ILE B 362     3413   8571   5182   2923    -15   1132       C  
-ATOM   8039  N   SER B 363     -14.640  28.094  -3.422  1.00 60.29           N  
-ANISOU 8039  N   SER B 363     5560  10791   6555   4155    392   1643       N  
-ATOM   8040  CA  SER B 363     -15.661  28.639  -4.315  1.00 69.33           C  
-ANISOU 8040  CA  SER B 363     6603  12170   7569   4437    436   1750       C  
-ATOM   8041  C   SER B 363     -15.046  29.127  -5.621  1.00 73.03           C  
-ANISOU 8041  C   SER B 363     7110  12655   7983   4501    432   1826       C  
-ATOM   8042  O   SER B 363     -13.888  29.540  -5.655  1.00 73.72           O  
-ANISOU 8042  O   SER B 363     7397  12493   8121   4395    449   1836       O  
-ATOM   8043  CB  SER B 363     -16.402  29.792  -3.641  1.00 72.02           C  
-ANISOU 8043  CB  SER B 363     7115  12408   7841   4670    574   1855       C  
-ATOM   8044  OG  SER B 363     -16.901  30.700  -4.609  1.00 75.14           O  
-ANISOU 8044  OG  SER B 363     7519  12914   8117   4936    640   1991       O  
-ATOM   8045  N   GLU B 364     -15.833  29.096  -6.691  1.00 81.79           N  
-ANISOU 8045  N   GLU B 364     8029  14060   8987   4680    412   1881       N  
-ATOM   8046  CA  GLU B 364     -15.334  29.471  -8.010  1.00 85.80           C  
-ANISOU 8046  CA  GLU B 364     8543  14627   9429   4752    403   1954       C  
-ATOM   8047  C   GLU B 364     -16.370  30.226  -8.845  1.00 91.06           C  
-ANISOU 8047  C   GLU B 364     9141  15513   9943   5073    464   2091       C  
-ATOM   8048  O   GLU B 364     -17.496  30.445  -8.402  1.00 91.75           O  
-ANISOU 8048  O   GLU B 364     9170  15709   9981   5238    512   2127       O  
-ATOM   8049  CB  GLU B 364     -14.844  28.227  -8.756  1.00 82.93           C  
-ANISOU 8049  CB  GLU B 364     7962  14435   9111   4549    261   1837       C  
-ATOM   8050  CG  GLU B 364     -15.865  27.105  -8.845  1.00 81.27           C  
-ANISOU 8050  CG  GLU B 364     7433  14552   8895   4534    168   1743       C  
-ATOM   8051  CD  GLU B 364     -15.247  25.799  -9.303  1.00 78.24           C  
-ANISOU 8051  CD  GLU B 364     6859  14274   8594   4282     32   1602       C  
-ATOM   8052  OE1 GLU B 364     -14.000  25.711  -9.324  1.00 77.10           O  
-ANISOU 8052  OE1 GLU B 364     6846  13920   8530   4093     11   1568       O  
-ATOM   8053  OE2 GLU B 364     -16.004  24.863  -9.641  1.00 74.76           O  
-ANISOU 8053  OE2 GLU B 364     6137  14123   8145   4272    -54   1523       O  
-ATOM   8054  N   ASN B 365     -15.973  30.630 -10.049  1.00 83.32           N  
-ANISOU 8054  N   ASN B 365     8171  14595   8891   5162    465   2171       N  
-ATOM   8055  CA  ASN B 365     -16.877  31.287 -10.990  1.00 88.75           C  
-ANISOU 8055  CA  ASN B 365     8779  15515   9428   5462    511   2305       C  
-ATOM   8056  C   ASN B 365     -16.232  31.442 -12.363  1.00 89.50           C  
-ANISOU 8056  C   ASN B 365     8858  15691   9458   5496    484   2364       C  
-ATOM   8057  O   ASN B 365     -15.091  31.026 -12.568  1.00 89.48           O  
-ANISOU 8057  O   ASN B 365     8905  15561   9533   5283    430   2297       O  
-ATOM   8058  CB  ASN B 365     -17.318  32.656 -10.465  1.00 94.87           C  
-ANISOU 8058  CB  ASN B 365     9774  16116  10157   5694    668   2450       C  
-ATOM   8059  CG  ASN B 365     -16.329  33.758 -10.799  1.00 98.71           C  
-ANISOU 8059  CG  ASN B 365    10530  16332  10645   5741    762   2564       C  
-ATOM   8060  OD1 ASN B 365     -15.129  33.515 -10.935  1.00101.28           O  
-ANISOU 8060  OD1 ASN B 365    10944  16489  11050   5539    723   2512       O  
-ATOM   8061  ND2 ASN B 365     -16.832  34.980 -10.937  1.00101.73           N  
-ANISOU 8061  ND2 ASN B 365    11039  16668  10944   6011    891   2724       N  
-ATOM   8062  N   LYS B 366     -16.964  32.049 -13.295  1.00 86.71           N  
-ANISOU 8062  N   LYS B 366     8436  15549   8961   5767    523   2493       N  
-ATOM   8063  CA  LYS B 366     -16.458  32.285 -14.648  1.00 86.98           C  
-ANISOU 8063  CA  LYS B 366     8454  15684   8912   5839    508   2569       C  
-ATOM   8064  C   LYS B 366     -17.172  33.452 -15.335  1.00 87.02           C  
-ANISOU 8064  C   LYS B 366     8503  15791   8769   6180    613   2764       C  
-ATOM   8065  O   LYS B 366     -16.722  34.597 -15.273  1.00 86.56           O  
-ANISOU 8065  O   LYS B 366     8690  15488   8709   6287    738   2895       O  
-ATOM   8066  CB  LYS B 366     -16.582  31.020 -15.486  1.00 87.91           C  
-ANISOU 8066  CB  LYS B 366     8278  16123   9002   5729    355   2447       C  
-ATOM   8067  N   ASN B 376      -8.452  28.630 -16.849  1.00 90.82           N  
-ANISOU 8067  N   ASN B 376     9094  15465   9949   4315    100   2062       N  
-ATOM   8068  CA  ASN B 376      -9.820  28.752 -17.336  1.00 91.18           C  
-ANISOU 8068  CA  ASN B 376     8967  15839   9839   4569     99   2115       C  
-ATOM   8069  C   ASN B 376     -10.880  28.749 -16.227  1.00 89.42           C  
-ANISOU 8069  C   ASN B 376     8711  15635   9631   4626    116   2087       C  
-ATOM   8070  O   ASN B 376     -11.978  28.221 -16.416  1.00 90.12           O  
-ANISOU 8070  O   ASN B 376     8570  16025   9646   4717     58   2045       O  
-ATOM   8071  CB  ASN B 376     -10.122  27.661 -18.369  1.00 96.96           C  
-ANISOU 8071  CB  ASN B 376     9405  16931  10504   4532    -28   2017       C  
-ATOM   8072  CG  ASN B 376     -10.055  26.264 -17.783  1.00 98.95           C  
-ANISOU 8072  CG  ASN B 376     9480  17234  10884   4259   -150   1816       C  
-ATOM   8073  OD1 ASN B 376     -10.320  26.058 -16.600  1.00100.59           O  
-ANISOU 8073  OD1 ASN B 376     9716  17319  11186   4167   -146   1756       O  
-ATOM   8074  ND2 ASN B 376      -9.693  25.294 -18.612  1.00101.29           N  
-ANISOU 8074  ND2 ASN B 376     9593  17710  11183   4128   -256   1711       N  
-ATOM   8075  N   ILE B 377     -10.546  29.338 -15.077  1.00 68.28           N  
-ANISOU 8075  N   ILE B 377     6261  12636   7048   4574    196   2110       N  
-ATOM   8076  CA  ILE B 377     -11.505  29.511 -13.980  1.00 64.24           C  
-ANISOU 8076  CA  ILE B 377     5757  12107   6544   4649    235   2103       C  
-ATOM   8077  C   ILE B 377     -10.938  30.312 -12.808  1.00 62.61           C  
-ANISOU 8077  C   ILE B 377     5843  11511   6435   4596    334   2138       C  
-ATOM   8078  O   ILE B 377      -9.776  30.159 -12.450  1.00 61.92           O  
-ANISOU 8078  O   ILE B 377     5889  11170   6467   4378    320   2083       O  
-ATOM   8079  CB  ILE B 377     -12.037  28.158 -13.461  1.00 60.02           C  
-ANISOU 8079  CB  ILE B 377     4981  11752   6072   4480    118   1933       C  
-ATOM   8080  CG1 ILE B 377     -13.230  28.378 -12.524  1.00 58.53           C  
-ANISOU 8080  CG1 ILE B 377     4768  11611   5861   4612    165   1948       C  
-ATOM   8081  CG2 ILE B 377     -10.923  27.356 -12.796  1.00 58.54           C  
-ANISOU 8081  CG2 ILE B 377     4842  11348   6054   4151     54   1798       C  
-ATOM   8082  CD1 ILE B 377     -14.059  27.140 -12.286  1.00 52.82           C  
-ANISOU 8082  CD1 ILE B 377     3759  11147   5163   4526     59   1813       C  
-ATOM   8083  N   PHE B 378     -11.770  31.162 -12.213  1.00 70.98           N  
-ANISOU 8083  N   PHE B 378     6998  12527   7444   4796    434   2226       N  
-ATOM   8084  CA  PHE B 378     -11.358  31.981 -11.075  1.00 69.71           C  
-ANISOU 8084  CA  PHE B 378     7112  12011   7363   4771    533   2257       C  
-ATOM   8085  C   PHE B 378     -11.848  31.353  -9.777  1.00 65.43           C  
-ANISOU 8085  C   PHE B 378     6523  11444   6894   4651    500   2140       C  
-ATOM   8086  O   PHE B 378     -13.033  31.066  -9.632  1.00 65.46           O  
-ANISOU 8086  O   PHE B 378     6359  11680   6834   4770    488   2131       O  
-ATOM   8087  CB  PHE B 378     -11.913  33.397 -11.213  1.00 76.82           C  
-ANISOU 8087  CB  PHE B 378     8168  12852   8168   5073    677   2432       C  
-ATOM   8088  CG  PHE B 378     -11.216  34.413 -10.353  1.00 81.71           C  
-ANISOU 8088  CG  PHE B 378     9101  13076   8869   5054    789   2481       C  
-ATOM   8089  CD1 PHE B 378      -9.834  34.486 -10.326  1.00 83.64           C  
-ANISOU 8089  CD1 PHE B 378     9509  13049   9223   4859    783   2453       C  
-ATOM   8090  CD2 PHE B 378     -11.944  35.316  -9.598  1.00 86.06           C  
-ANISOU 8090  CD2 PHE B 378     9781  13527   9390   5236    903   2555       C  
-ATOM   8091  CE1 PHE B 378      -9.189  35.427  -9.547  1.00 86.84           C  
-ANISOU 8091  CE1 PHE B 378    10197  13090   9707   4840    883   2492       C  
-ATOM   8092  CE2 PHE B 378     -11.307  36.263  -8.817  1.00 88.78           C  
-ANISOU 8092  CE2 PHE B 378    10414  13508   9812   5220   1006   2591       C  
-ATOM   8093  CZ  PHE B 378      -9.927  36.319  -8.790  1.00 88.77           C  
-ANISOU 8093  CZ  PHE B 378    10569  13238   9920   5021    993   2557       C  
-ATOM   8094  N   ILE B 379     -10.930  31.140  -8.840  1.00 67.45           N  
-ANISOU 8094  N   ILE B 379     6925  11421   7283   4417    487   2055       N  
-ATOM   8095  CA  ILE B 379     -11.239  30.411  -7.613  1.00 61.89           C  
-ANISOU 8095  CA  ILE B 379     6171  10689   6657   4269    445   1934       C  
-ATOM   8096  C   ILE B 379     -10.922  31.201  -6.340  1.00 60.66           C  
-ANISOU 8096  C   ILE B 379     6289  10197   6563   4249    537   1948       C  
-ATOM   8097  O   ILE B 379      -9.817  31.718  -6.168  1.00 58.30           O  
-ANISOU 8097  O   ILE B 379     6208   9609   6336   4149    570   1961       O  
-ATOM   8098  CB  ILE B 379     -10.513  29.042  -7.581  1.00 57.98           C  
-ANISOU 8098  CB  ILE B 379     5529  10227   6273   3963    309   1781       C  
-ATOM   8099  CG1 ILE B 379     -11.332  27.990  -8.334  1.00 56.77           C  
-ANISOU 8099  CG1 ILE B 379     5047  10456   6068   3980    209   1721       C  
-ATOM   8100  CG2 ILE B 379     -10.259  28.599  -6.156  1.00 56.29           C  
-ANISOU 8100  CG2 ILE B 379     5390   9823   6174   3766    292   1677       C  
-ATOM   8101  CD1 ILE B 379     -10.671  26.628  -8.397  1.00 52.18           C  
-ANISOU 8101  CD1 ILE B 379     4305   9925   5597   3691     79   1571       C  
-ATOM   8102  N   GLY B 380     -11.911  31.300  -5.458  1.00 73.09           N  
-ANISOU 8102  N   GLY B 380     7849  11814   8109   4348    581   1944       N  
-ATOM   8103  CA  GLY B 380     -11.729  31.943  -4.171  1.00 71.84           C  
-ANISOU 8103  CA  GLY B 380     7928  11366   8001   4328    662   1939       C  
-ATOM   8104  C   GLY B 380     -11.746  30.914  -3.056  1.00 69.07           C  
-ANISOU 8104  C   GLY B 380     7503  11003   7738   4113    589   1798       C  
-ATOM   8105  O   GLY B 380     -12.562  29.991  -3.068  1.00 67.33           O  
-ANISOU 8105  O   GLY B 380     7038  11043   7501   4102    523   1741       O  
-ATOM   8106  N   ILE B 381     -10.836  31.057  -2.100  1.00 66.21           N  
-ANISOU 8106  N   ILE B 381     7346  10340   7472   3939    598   1743       N  
-ATOM   8107  CA  ILE B 381     -10.776  30.131  -0.975  1.00 63.96           C  
-ANISOU 8107  CA  ILE B 381     7011  10021   7271   3733    535   1617       C  
-ATOM   8108  C   ILE B 381     -10.643  30.856   0.359  1.00 63.08           C  
-ANISOU 8108  C   ILE B 381     7153   9631   7183   3736    619   1612       C  
-ATOM   8109  O   ILE B 381      -9.893  31.831   0.483  1.00 63.42           O  
-ANISOU 8109  O   ILE B 381     7448   9404   7246   3752    685   1656       O  
-ATOM   8110  CB  ILE B 381      -9.609  29.118  -1.108  1.00 62.46           C  
-ANISOU 8110  CB  ILE B 381     6761   9772   7200   3429    414   1509       C  
-ATOM   8111  CG1 ILE B 381      -8.258  29.833  -1.046  1.00 62.40           C  
-ANISOU 8111  CG1 ILE B 381     7017   9432   7261   3326    442   1526       C  
-ATOM   8112  CG2 ILE B 381      -9.736  28.300  -2.387  1.00 62.72           C  
-ANISOU 8112  CG2 ILE B 381     6531  10086   7212   3410    325   1496       C  
-ATOM   8113  CD1 ILE B 381      -7.086  28.887  -1.023  1.00 60.07           C  
-ANISOU 8113  CD1 ILE B 381     6683   9049   7091   3023    331   1422       C  
-ATOM   8114  N   VAL B 382     -11.381  30.378   1.354  1.00 56.74           N  
-ANISOU 8114  N   VAL B 382     6282   8897   6380   3723    617   1555       N  
-ATOM   8115  CA  VAL B 382     -11.238  30.885   2.711  1.00 56.31           C  
-ANISOU 8115  CA  VAL B 382     6450   8596   6350   3697    682   1529       C  
-ATOM   8116  C   VAL B 382     -10.782  29.754   3.625  1.00 53.63           C  
-ANISOU 8116  C   VAL B 382     6048   8220   6109   3428    588   1399       C  
-ATOM   8117  O   VAL B 382     -11.377  28.675   3.641  1.00 53.53           O  
-ANISOU 8117  O   VAL B 382     5792   8439   6109   3369    520   1345       O  
-ATOM   8118  CB  VAL B 382     -12.550  31.502   3.241  1.00 57.61           C  
-ANISOU 8118  CB  VAL B 382     6630   8841   6417   3948    791   1592       C  
-ATOM   8119  CG1 VAL B 382     -12.354  32.027   4.647  1.00 56.04           C  
-ANISOU 8119  CG1 VAL B 382     6670   8382   6239   3917    858   1556       C  
-ATOM   8120  CG2 VAL B 382     -13.012  32.624   2.329  1.00 57.40           C  
-ANISOU 8120  CG2 VAL B 382     6661   8853   6296   4221    887   1729       C  
-ATOM   8121  N   GLY B 383      -9.713  30.000   4.371  1.00 55.64           N  
-ANISOU 8121  N   GLY B 383     6521   8182   6438   3264    584   1349       N  
-ATOM   8122  CA  GLY B 383      -9.155  28.991   5.247  1.00 53.67           C  
-ANISOU 8122  CA  GLY B 383     6234   7873   6284   3003    496   1233       C  
-ATOM   8123  C   GLY B 383      -9.099  29.462   6.684  1.00 52.79           C  
-ANISOU 8123  C   GLY B 383     6338   7545   6174   2989    555   1200       C  
-ATOM   8124  O   GLY B 383      -8.398  30.414   7.014  1.00 50.94           O  
-ANISOU 8124  O   GLY B 383     6364   7040   5950   2994    608   1215       O  
-ATOM   8125  N   VAL B 384      -9.850  28.797   7.547  1.00 55.81           N  
-ANISOU 8125  N   VAL B 384     6611   8048   6547   2974    547   1154       N  
-ATOM   8126  CA  VAL B 384      -9.851  29.151   8.957  1.00 57.23           C  
-ANISOU 8126  CA  VAL B 384     6980   8045   6718   2959    600   1117       C  
-ATOM   8127  C   VAL B 384      -9.215  28.051   9.790  1.00 56.73           C  
-ANISOU 8127  C   VAL B 384     6866   7939   6750   2687    502   1009       C  
-ATOM   8128  O   VAL B 384      -9.184  26.888   9.387  1.00 54.37           O  
-ANISOU 8128  O   VAL B 384     6331   7815   6512   2549    407    968       O  
-ATOM   8129  CB  VAL B 384     -11.276  29.419   9.469  1.00 59.00           C  
-ANISOU 8129  CB  VAL B 384     7157   8416   6843   3185    694   1161       C  
-ATOM   8130  CG1 VAL B 384     -11.803  30.720   8.901  1.00 59.54           C  
-ANISOU 8130  CG1 VAL B 384     7344   8460   6819   3458    810   1270       C  
-ATOM   8131  CG2 VAL B 384     -12.189  28.263   9.102  1.00 58.56           C  
-ANISOU 8131  CG2 VAL B 384     6774   8687   6790   3185    638   1150       C  
-ATOM   8132  N   GLN B 385      -8.689  28.427  10.946  1.00 59.50           N  
-ANISOU 8132  N   GLN B 385     7439   8053   7114   2611    525    964       N  
-ATOM   8133  CA  GLN B 385      -8.169  27.446  11.882  1.00 58.69           C  
-ANISOU 8133  CA  GLN B 385     7303   7909   7089   2373    443    870       C  
-ATOM   8134  C   GLN B 385      -8.763  27.674  13.262  1.00 61.12           C  
-ANISOU 8134  C   GLN B 385     7721   8165   7337   2441    512    850       C  
-ATOM   8135  O   GLN B 385      -8.143  28.314  14.110  1.00 59.98           O  
-ANISOU 8135  O   GLN B 385     7826   7776   7189   2399    538    817       O  
-ATOM   8136  CB  GLN B 385      -6.647  27.488  11.935  1.00 55.86           C  
-ANISOU 8136  CB  GLN B 385     7099   7300   6827   2150    372    817       C  
-ATOM   8137  CG  GLN B 385      -6.074  26.379  12.783  1.00 50.28           C  
-ANISOU 8137  CG  GLN B 385     6329   6570   6207   1895    276    726       C  
-ATOM   8138  CD  GLN B 385      -4.640  26.062  12.438  1.00 46.36           C  
-ANISOU 8138  CD  GLN B 385     5875   5913   5826   1656    179    679       C  
-ATOM   8139  OE1 GLN B 385      -4.146  24.980  12.752  1.00 42.65           O  
-ANISOU 8139  OE1 GLN B 385     5288   5472   5446   1438     85    615       O  
-ATOM   8140  NE2 GLN B 385      -3.958  27.005  11.786  1.00 45.94           N  
-ANISOU 8140  NE2 GLN B 385     5988   5688   5780   1695    204    715       N  
-ATOM   8141  N   PRO B 386      -9.970  27.133  13.490  1.00 75.01           N  
-ANISOU 8141  N   PRO B 386     9290  10160   9049   2546    540    867       N  
-ATOM   8142  CA  PRO B 386     -10.762  27.373  14.700  1.00 76.52           C  
-ANISOU 8142  CA  PRO B 386     9561  10345   9168   2655    623    864       C  
-ATOM   8143  C   PRO B 386      -9.945  27.205  15.975  1.00 75.94           C  
-ANISOU 8143  C   PRO B 386     9658  10067   9130   2472    591    784       C  
-ATOM   8144  O   PRO B 386     -10.197  27.893  16.960  1.00 78.97           O  
-ANISOU 8144  O   PRO B 386    10233  10329   9443   2567    672    779       O  
-ATOM   8145  CB  PRO B 386     -11.838  26.289  14.630  1.00 77.35           C  
-ANISOU 8145  CB  PRO B 386     9360  10751   9277   2681    604    871       C  
-ATOM   8146  CG  PRO B 386     -11.966  25.981  13.180  1.00 77.43           C  
-ANISOU 8146  CG  PRO B 386     9166  10941   9314   2706    555    907       C  
-ATOM   8147  CD  PRO B 386     -10.592  26.127  12.611  1.00 76.00           C  
-ANISOU 8147  CD  PRO B 386     9095  10578   9204   2540    483    879       C  
-ATOM   8148  N   ALA B 387      -8.976  26.300  15.954  1.00 57.79           N  
-ANISOU 8148  N   ALA B 387     7288   7731   6937   2216    475    721       N  
-ATOM   8149  CA  ALA B 387      -8.174  26.028  17.137  1.00 54.88           C  
-ANISOU 8149  CA  ALA B 387     7057   7187   6606   2029    432    645       C  
-ATOM   8150  C   ALA B 387      -7.259  27.189  17.502  1.00 53.70           C  
-ANISOU 8150  C   ALA B 387     7232   6731   6440   2023    461    625       C  
-ATOM   8151  O   ALA B 387      -6.914  27.361  18.669  1.00 53.44           O  
-ANISOU 8151  O   ALA B 387     7370   6545   6389   1961    468    572       O  
-ATOM   8152  CB  ALA B 387      -7.363  24.762  16.947  1.00 54.95           C  
-ANISOU 8152  CB  ALA B 387     6899   7239   6742   1760    300    590       C  
-ATOM   8153  N   THR B 388      -6.867  27.984  16.509  1.00 53.67           N  
-ANISOU 8153  N   THR B 388     7310   6639   6445   2090    478    666       N  
-ATOM   8154  CA  THR B 388      -5.927  29.077  16.746  1.00 54.34           C  
-ANISOU 8154  CA  THR B 388     7691   6422   6535   2073    502    646       C  
-ATOM   8155  C   THR B 388      -6.421  30.436  16.243  1.00 57.10           C  
-ANISOU 8155  C   THR B 388     8184   6706   6806   2329    623    721       C  
-ATOM   8156  O   THR B 388      -5.747  31.453  16.428  1.00 57.83           O  
-ANISOU 8156  O   THR B 388     8526   6544   6903   2343    661    711       O  
-ATOM   8157  CB  THR B 388      -4.560  28.785  16.119  1.00 51.90           C  
-ANISOU 8157  CB  THR B 388     7390   5983   6345   1851    397    613       C  
-ATOM   8158  OG1 THR B 388      -4.654  28.888  14.693  1.00 50.31           O  
-ANISOU 8158  OG1 THR B 388     7067   5886   6161   1925    398    681       O  
-ATOM   8159  CG2 THR B 388      -4.093  27.392  16.499  1.00 50.21           C  
-ANISOU 8159  CG2 THR B 388     7011   5849   6219   1601    278    548       C  
-ATOM   8160  N   GLY B 389      -7.586  30.454  15.603  1.00 69.09           N  
-ANISOU 8160  N   GLY B 389     9541   8451   8259   2529    684    798       N  
-ATOM   8161  CA  GLY B 389      -8.204  31.703  15.191  1.00 72.94           C  
-ANISOU 8161  CA  GLY B 389    10148   8901   8666   2792    808    880       C  
-ATOM   8162  C   GLY B 389      -7.683  32.299  13.894  1.00 74.71           C  
-ANISOU 8162  C   GLY B 389    10398   9065   8924   2833    810    942       C  
-ATOM   8163  O   GLY B 389      -8.277  33.238  13.363  1.00 78.11           O  
-ANISOU 8163  O   GLY B 389    10883   9505   9290   3062    911   1026       O  
-ATOM   8164  N   GLU B 390      -6.578  31.760  13.383  1.00 62.73           N  
-ANISOU 8164  N   GLU B 390     8841   7486   7508   2618    704    905       N  
-ATOM   8165  CA  GLU B 390      -5.982  32.250  12.143  1.00 62.93           C  
-ANISOU 8165  CA  GLU B 390     8886   7451   7573   2638    701    963       C  
-ATOM   8166  C   GLU B 390      -6.940  32.156  10.971  1.00 62.44           C  
-ANISOU 8166  C   GLU B 390     8614   7657   7454   2820    730   1056       C  
-ATOM   8167  O   GLU B 390      -7.478  31.092  10.686  1.00 62.79           O  
-ANISOU 8167  O   GLU B 390     8403   7956   7499   2779    668   1046       O  
-ATOM   8168  CB  GLU B 390      -4.706  31.476  11.821  1.00 63.72           C  
-ANISOU 8168  CB  GLU B 390     8938   7476   7795   2361    573    903       C  
-ATOM   8169  CG  GLU B 390      -3.477  31.994  12.545  1.00 67.05           C  
-ANISOU 8169  CG  GLU B 390     9618   7571   8286   2209    554    838       C  
-ATOM   8170  CD  GLU B 390      -2.509  30.885  12.916  1.00 66.15           C  
-ANISOU 8170  CD  GLU B 390     9434   7423   8278   1911    420    747       C  
-ATOM   8171  OE1 GLU B 390      -2.176  30.054  12.037  1.00 66.56           O  
-ANISOU 8171  OE1 GLU B 390     9295   7601   8395   1794    339    752       O  
-ATOM   8172  OE2 GLU B 390      -2.093  30.840  14.096  1.00 67.06           O  
-ANISOU 8172  OE2 GLU B 390     9682   7388   8409   1797    398    671       O  
-ATOM   8173  N   VAL B 391      -7.154  33.280  10.299  1.00 62.54           N  
-ANISOU 8173  N   VAL B 391     8733   7611   7418   3025    826   1147       N  
-ATOM   8174  CA  VAL B 391      -7.971  33.306   9.093  1.00 62.42           C  
-ANISOU 8174  CA  VAL B 391     8535   7836   7344   3207    854   1245       C  
-ATOM   8175  C   VAL B 391      -7.102  33.617   7.876  1.00 59.75           C  
-ANISOU 8175  C   VAL B 391     8217   7428   7057   3174    830   1294       C  
-ATOM   8176  O   VAL B 391      -6.202  34.462   7.932  1.00 58.31           O  
-ANISOU 8176  O   VAL B 391     8261   6972   6921   3143    864   1300       O  
-ATOM   8177  CB  VAL B 391      -9.118  34.332   9.196  1.00 64.97           C  
-ANISOU 8177  CB  VAL B 391     8931   8197   7557   3510    996   1333       C  
-ATOM   8178  CG1 VAL B 391      -9.929  34.357   7.909  1.00 65.86           C  
-ANISOU 8178  CG1 VAL B 391     8850   8566   7607   3698   1018   1437       C  
-ATOM   8179  CG2 VAL B 391     -10.011  34.004  10.374  1.00 68.12           C  
-ANISOU 8179  CG2 VAL B 391     9301   8677   7904   3550   1025   1289       C  
-ATOM   8180  N   VAL B 392      -7.376  32.921   6.781  1.00 52.73           N  
-ANISOU 8180  N   VAL B 392     7087   6788   6161   3179    772   1326       N  
-ATOM   8181  CA  VAL B 392      -6.563  33.020   5.584  1.00 52.11           C  
-ANISOU 8181  CA  VAL B 392     6992   6679   6127   3131    737   1368       C  
-ATOM   8182  C   VAL B 392      -7.451  32.949   4.350  1.00 54.49           C  
-ANISOU 8182  C   VAL B 392     7087   7269   6346   3320    753   1459       C  
-ATOM   8183  O   VAL B 392      -8.399  32.167   4.309  1.00 54.39           O  
-ANISOU 8183  O   VAL B 392     6851   7527   6288   3361    719   1445       O  
-ATOM   8184  CB  VAL B 392      -5.520  31.890   5.548  1.00 47.28           C  
-ANISOU 8184  CB  VAL B 392     6287   6049   5629   2828    600   1271       C  
-ATOM   8185  CG1 VAL B 392      -5.256  31.452   4.128  1.00 45.23           C  
-ANISOU 8185  CG1 VAL B 392     5854   5948   5385   2806    542   1310       C  
-ATOM   8186  CG2 VAL B 392      -4.239  32.335   6.233  1.00 43.87           C  
-ANISOU 8186  CG2 VAL B 392     6105   5273   5291   2658    591   1218       C  
-ATOM   8187  N   PHE B 393      -7.155  33.776   3.352  1.00 55.53           N  
-ANISOU 8187  N   PHE B 393     7294   7344   6460   3441    806   1556       N  
-ATOM   8188  CA  PHE B 393      -7.942  33.783   2.125  1.00 59.30           C  
-ANISOU 8188  CA  PHE B 393     7587   8093   6850   3630    821   1650       C  
-ATOM   8189  C   PHE B 393      -7.054  33.978   0.906  1.00 59.87           C  
-ANISOU 8189  C   PHE B 393     7668   8123   6955   3595    799   1703       C  
-ATOM   8190  O   PHE B 393      -5.903  34.399   1.023  1.00 58.32           O  
-ANISOU 8190  O   PHE B 393     7660   7654   6845   3472    803   1690       O  
-ATOM   8191  CB  PHE B 393      -9.001  34.882   2.175  1.00 63.53           C  
-ANISOU 8191  CB  PHE B 393     8204   8654   7279   3935    958   1758       C  
-ATOM   8192  CG  PHE B 393      -8.437  36.270   2.080  1.00 67.52           C  
-ANISOU 8192  CG  PHE B 393     8980   8877   7796   4043   1069   1840       C  
-ATOM   8193  CD1 PHE B 393      -8.608  37.024   0.932  1.00 69.69           C  
-ANISOU 8193  CD1 PHE B 393     9256   9207   8015   4242   1136   1971       C  
-ATOM   8194  CD2 PHE B 393      -7.731  36.818   3.136  1.00 68.42           C  
-ANISOU 8194  CD2 PHE B 393     9346   8673   7979   3947   1105   1785       C  
-ATOM   8195  CE1 PHE B 393      -8.089  38.298   0.842  1.00 70.38           C  
-ANISOU 8195  CE1 PHE B 393     9587   9028   8125   4342   1245   2051       C  
-ATOM   8196  CE2 PHE B 393      -7.211  38.091   3.052  1.00 68.74           C  
-ANISOU 8196  CE2 PHE B 393     9631   8445   8042   4042   1208   1854       C  
-ATOM   8197  CZ  PHE B 393      -7.388  38.832   1.903  1.00 69.87           C  
-ANISOU 8197  CZ  PHE B 393     9770   8639   8139   4240   1281   1990       C  
-ATOM   8198  N   ASP B 394      -7.588  33.671  -0.269  1.00 62.56           N  
-ANISOU 8198  N   ASP B 394     7805   8737   7229   3706    776   1762       N  
-ATOM   8199  CA  ASP B 394      -6.812  33.821  -1.486  1.00 63.88           C  
-ANISOU 8199  CA  ASP B 394     7965   8893   7414   3687    758   1818       C  
-ATOM   8200  C   ASP B 394      -7.694  33.753  -2.723  1.00 67.15           C  
-ANISOU 8200  C   ASP B 394     8174   9626   7714   3890    762   1907       C  
-ATOM   8201  O   ASP B 394      -8.651  32.979  -2.776  1.00 67.63           O  
-ANISOU 8201  O   ASP B 394     8008   9968   7719   3928    712   1873       O  
-ATOM   8202  CB  ASP B 394      -5.733  32.744  -1.549  1.00 61.18           C  
-ANISOU 8202  CB  ASP B 394     7547   8514   7185   3383    630   1708       C  
-ATOM   8203  CG  ASP B 394      -4.471  33.228  -2.224  1.00 58.84           C  
-ANISOU 8203  CG  ASP B 394     7391   8008   6958   3305    638   1748       C  
-ATOM   8204  OD1 ASP B 394      -4.266  34.460  -2.276  1.00 58.64           O  
-ANISOU 8204  OD1 ASP B 394     7577   7782   6921   3446    748   1841       O  
-ATOM   8205  OD2 ASP B 394      -3.683  32.377  -2.689  1.00 56.96           O  
-ANISOU 8205  OD2 ASP B 394     7050   7801   6792   3103    539   1687       O  
-ATOM   8206  N   SER B 395      -7.365  34.575  -3.715  1.00 80.33           N  
-ANISOU 8206  N   SER B 395     9922  11250   9350   4022    824   2022       N  
-ATOM   8207  CA  SER B 395      -8.070  34.570  -4.992  1.00 83.80           C  
-ANISOU 8207  CA  SER B 395    10181  11984   9677   4214    827   2115       C  
-ATOM   8208  C   SER B 395      -7.075  34.391  -6.137  1.00 84.47           C  
-ANISOU 8208  C   SER B 395    10238  12065   9792   4123    780   2138       C  
-ATOM   8209  O   SER B 395      -5.990  34.976  -6.128  1.00 83.99           O  
-ANISOU 8209  O   SER B 395    10378  11723   9812   4043    818   2162       O  
-ATOM   8210  CB  SER B 395      -8.855  35.866  -5.171  1.00 85.69           C  
-ANISOU 8210  CB  SER B 395    10532  12210   9817   4527    969   2264       C  
-ATOM   8211  OG  SER B 395      -8.046  36.991  -4.880  1.00 86.67           O  
-ANISOU 8211  OG  SER B 395    10941  11989  10002   4544   1069   2323       O  
-ATOM   8212  N   PHE B 396      -7.448  33.578  -7.120  1.00 68.83           N  
-ANISOU 8212  N   PHE B 396     8007  10396   7750   4134    698   2127       N  
-ATOM   8213  CA  PHE B 396      -6.544  33.235  -8.208  1.00 68.91           C  
-ANISOU 8213  CA  PHE B 396     7963  10436   7785   4032    641   2132       C  
-ATOM   8214  C   PHE B 396      -7.278  32.414  -9.260  1.00 72.96           C  
-ANISOU 8214  C   PHE B 396     8181  11342   8198   4101    561   2122       C  
-ATOM   8215  O   PHE B 396      -8.189  31.651  -8.930  1.00 73.76           O  
-ANISOU 8215  O   PHE B 396     8092  11664   8268   4099    502   2049       O  
-ATOM   8216  CB  PHE B 396      -5.375  32.420  -7.667  1.00 64.20           C  
-ANISOU 8216  CB  PHE B 396     7397   9658   7338   3704    550   1998       C  
-ATOM   8217  CG  PHE B 396      -5.797  31.165  -6.971  1.00 57.51           C  
-ANISOU 8217  CG  PHE B 396     6362   8959   6529   3539    443   1854       C  
-ATOM   8218  CD1 PHE B 396      -6.015  30.000  -7.686  1.00 54.68           C  
-ANISOU 8218  CD1 PHE B 396     5734   8887   6154   3456    332   1782       C  
-ATOM   8219  CD2 PHE B 396      -5.995  31.154  -5.603  1.00 55.11           C  
-ANISOU 8219  CD2 PHE B 396     6151   8511   6277   3470    458   1790       C  
-ATOM   8220  CE1 PHE B 396      -6.415  28.842  -7.048  1.00 55.20           C  
-ANISOU 8220  CE1 PHE B 396     5622   9085   6267   3305    240   1653       C  
-ATOM   8221  CE2 PHE B 396      -6.392  29.997  -4.952  1.00 54.80           C  
-ANISOU 8221  CE2 PHE B 396     5938   8608   6277   3322    366   1666       C  
-ATOM   8222  CZ  PHE B 396      -6.606  28.838  -5.677  1.00 54.78           C  
-ANISOU 8222  CZ  PHE B 396     5662   8884   6268   3239    259   1599       C  
-ATOM   8223  N   GLN B 397      -6.881  32.562 -10.522  1.00 75.14           N  
-ANISOU 8223  N   GLN B 397     9156  11110   8283   3828   1422   1852       N  
-ATOM   8224  CA  GLN B 397      -7.457  31.748 -11.588  1.00 81.16           C  
-ANISOU 8224  CA  GLN B 397     9926  12077   8834   3862   1318   1812       C  
-ATOM   8225  C   GLN B 397      -6.577  30.548 -11.903  1.00 79.43           C  
-ANISOU 8225  C   GLN B 397     9742  11788   8649   3753   1269   1678       C  
-ATOM   8226  O   GLN B 397      -5.361  30.603 -11.748  1.00 77.61           O  
-ANISOU 8226  O   GLN B 397     9552  11356   8580   3720   1366   1653       O  
-ATOM   8227  CB  GLN B 397      -7.739  32.577 -12.840  1.00 87.24           C  
-ANISOU 8227  CB  GLN B 397    10747  12969   9433   4068   1425   1945       C  
-ATOM   8228  CG  GLN B 397      -6.634  33.522 -13.241  1.00 96.00           C  
-ANISOU 8228  CG  GLN B 397    11942  13899  10633   4169   1649   2034       C  
-ATOM   8229  CD  GLN B 397      -7.095  34.505 -14.300  1.00101.91           C  
-ANISOU 8229  CD  GLN B 397    12745  14766  11210   4383   1759   2194       C  
-ATOM   8230  OE1 GLN B 397      -8.297  34.656 -14.537  1.00104.40           O  
-ANISOU 8230  OE1 GLN B 397    13014  15288  11365   4464   1664   2254       O  
-ATOM   8231  NE2 GLN B 397      -6.142  35.180 -14.946  1.00102.60           N  
-ANISOU 8231  NE2 GLN B 397    12931  14720  11331   4480   1962   2264       N  
-ATOM   8232  N   ASP B 398      -7.208  29.463 -12.335  1.00 93.99           N  
-ANISOU 8232  N   ASP B 398    11562  13799  10352   3696   1122   1584       N  
-ATOM   8233  CA  ASP B 398      -6.530  28.183 -12.451  1.00 91.75           C  
-ANISOU 8233  CA  ASP B 398    11294  13450  10116   3566   1057   1441       C  
-ATOM   8234  C   ASP B 398      -6.872  27.469 -13.756  1.00 91.66           C  
-ANISOU 8234  C   ASP B 398    11304  13628   9895   3601   1014   1387       C  
-ATOM   8235  O   ASP B 398      -8.010  27.516 -14.224  1.00 91.30           O  
-ANISOU 8235  O   ASP B 398    11223  13811   9655   3664    940   1411       O  
-ATOM   8236  CB  ASP B 398      -6.900  27.295 -11.260  1.00 95.61           C  
-ANISOU 8236  CB  ASP B 398    11723  13908  10695   3390    902   1336       C  
-ATOM   8237  CG  ASP B 398      -5.788  26.340 -10.873  1.00 96.42           C  
-ANISOU 8237  CG  ASP B 398    11849  13821  10966   3256    879   1224       C  
-ATOM   8238  OD1 ASP B 398      -4.883  26.104 -11.703  1.00 99.80           O  
-ANISOU 8238  OD1 ASP B 398    12325  14183  11413   3286    959   1195       O  
-ATOM   8239  OD2 ASP B 398      -5.822  25.822  -9.737  1.00 99.05           O  
-ANISOU 8239  OD2 ASP B 398    12154  14067  11415   3123    782   1165       O  
-ATOM   8240  N   SER B 399      -5.872  26.809 -14.335  1.00 73.70           N  
-ANISOU 8240  N   SER B 399     9082  11256   7665   3558   1063   1307       N  
-ATOM   8241  CA  SER B 399      -6.055  26.024 -15.548  1.00 74.59           C  
-ANISOU 8241  CA  SER B 399     9220  11527   7595   3564   1034   1233       C  
-ATOM   8242  C   SER B 399      -6.788  24.724 -15.247  1.00 73.30           C  
-ANISOU 8242  C   SER B 399     8989  11478   7383   3419    858   1089       C  
-ATOM   8243  O   SER B 399      -7.111  24.440 -14.097  1.00 72.94           O  
-ANISOU 8243  O   SER B 399     8889  11377   7449   3316    766   1053       O  
-ATOM   8244  CB  SER B 399      -4.700  25.724 -16.187  1.00 75.30           C  
-ANISOU 8244  CB  SER B 399     9383  11450   7777   3548   1159   1181       C  
-ATOM   8245  OG  SER B 399      -3.821  25.119 -15.255  1.00 74.57           O  
-ANISOU 8245  OG  SER B 399     9269  11133   7932   3413   1138   1093       O  
-ATOM   8246  N   ALA B 400      -7.046  23.933 -16.282  1.00 85.53           N  
-ANISOU 8246  N   ALA B 400    10547  13186   8766   3405    822   1000       N  
-ATOM   8247  CA  ALA B 400      -7.771  22.679 -16.108  1.00 84.16           C  
-ANISOU 8247  CA  ALA B 400    10309  13131   8537   3266    674    850       C  
-ATOM   8248  C   ALA B 400      -7.050  21.702 -15.179  1.00 82.84           C  
-ANISOU 8248  C   ALA B 400    10132  12748   8596   3096    638    739       C  
-ATOM   8249  O   ALA B 400      -7.659  20.761 -14.665  1.00 82.30           O  
-ANISOU 8249  O   ALA B 400    10011  12729   8531   2970    520    631       O  
-ATOM   8250  CB  ALA B 400      -8.043  22.032 -17.454  1.00 84.73           C  
-ANISOU 8250  CB  ALA B 400    10396  13401   8395   3278    664    765       C  
-ATOM   8251  N   SER B 401      -5.757  21.926 -14.969  1.00 68.91           N  
-ANISOU 8251  N   SER B 401     8418  10742   7024   3095    741    765       N  
-ATOM   8252  CA  SER B 401      -4.961  21.049 -14.115  1.00 67.21           C  
-ANISOU 8252  CA  SER B 401     8195  10309   7033   2952    705    673       C  
-ATOM   8253  C   SER B 401      -5.172  21.364 -12.635  1.00 64.92           C  
-ANISOU 8253  C   SER B 401     7872   9915   6880   2900    633    720       C  
-ATOM   8254  O   SER B 401      -4.729  20.621 -11.762  1.00 64.25           O  
-ANISOU 8254  O   SER B 401     7779   9674   6960   2778    571    653       O  
-ATOM   8255  CB  SER B 401      -3.476  21.162 -14.465  1.00 66.14           C  
-ANISOU 8255  CB  SER B 401     8113   9957   7060   2973    837    670       C  
-ATOM   8256  OG  SER B 401      -2.990  22.466 -14.200  1.00 63.67           O  
-ANISOU 8256  OG  SER B 401     7825   9539   6826   3081    944    801       O  
-ATOM   8257  N   ARG B 402      -5.847  22.475 -12.363  1.00 76.16           N  
-ANISOU 8257  N   ARG B 402     9279  11423   8234   2993    646    838       N  
-ATOM   8258  CA  ARG B 402      -6.091  22.915 -10.993  1.00 73.33           C  
-ANISOU 8258  CA  ARG B 402     8893  10976   7993   2947    598    888       C  
-ATOM   8259  C   ARG B 402      -4.803  22.927 -10.169  1.00 71.10           C  
-ANISOU 8259  C   ARG B 402     8636  10421   7957   2890    635    887       C  
-ATOM   8260  O   ARG B 402      -4.839  22.834  -8.945  1.00 69.45           O  
-ANISOU 8260  O   ARG B 402     8412  10113   7863   2799    564    883       O  
-ATOM   8261  CB  ARG B 402      -7.149  22.032 -10.323  1.00 74.42           C  
-ANISOU 8261  CB  ARG B 402     8984  11214   8080   2820    449    800       C  
-ATOM   8262  CG  ARG B 402      -8.524  22.069 -10.989  1.00 77.84           C  
-ANISOU 8262  CG  ARG B 402     9369  11925   8283   2870    397    790       C  
-ATOM   8263  CD  ARG B 402      -9.146  23.466 -10.952  1.00 79.86           C  
-ANISOU 8263  CD  ARG B 402     9603  12272   8470   3009    446    932       C  
-ATOM   8264  NE  ARG B 402     -10.501  23.492 -11.505  1.00 81.48           N  
-ANISOU 8264  NE  ARG B 402     9746  12745   8467   3060    378    920       N  
-ATOM   8265  CZ  ARG B 402     -10.801  23.821 -12.760  1.00 82.17           C  
-ANISOU 8265  CZ  ARG B 402     9836  13014   8372   3194    408    958       C  
-ATOM   8266  NH1 ARG B 402      -9.842  24.157 -13.611  1.00 82.47           N  
-ANISOU 8266  NH1 ARG B 402     9947  12986   8403   3284    521   1012       N  
-ATOM   8267  NH2 ARG B 402     -12.063  23.813 -13.166  1.00 81.78           N  
-ANISOU 8267  NH2 ARG B 402     9718  13213   8143   3236    326    939       N  
-ATOM   8268  N   SER B 403      -3.665  23.055 -10.845  1.00 68.61           N  
-ANISOU 8268  N   SER B 403     8360   9988   7721   2942    747    886       N  
-ATOM   8269  CA  SER B 403      -2.372  23.015 -10.172  1.00 67.67           C  
-ANISOU 8269  CA  SER B 403     8251   9615   7845   2893    781    868       C  
-ATOM   8270  C   SER B 403      -2.144  24.228  -9.266  1.00 67.32           C  
-ANISOU 8270  C   SER B 403     8199   9468   7910   2936    836    970       C  
-ATOM   8271  O   SER B 403      -1.252  24.215  -8.420  1.00 69.19           O  
-ANISOU 8271  O   SER B 403     8430   9512   8346   2878    829    952       O  
-ATOM   8272  CB  SER B 403      -1.232  22.899 -11.187  1.00 68.30           C  
-ANISOU 8272  CB  SER B 403     8366   9595   7988   2941    905    830       C  
-ATOM   8273  OG  SER B 403      -0.880  24.171 -11.699  1.00 68.23           O  
-ANISOU 8273  OG  SER B 403     8389   9569   7967   3076   1066    931       O  
-ATOM   8274  N   GLU B 404      -2.937  25.280  -9.444  1.00 68.62           N  
-ANISOU 8274  N   GLU B 404     8360   9762   7950   3037    893   1075       N  
-ATOM   8275  CA  GLU B 404      -2.817  26.452  -8.580  1.00 67.91           C  
-ANISOU 8275  CA  GLU B 404     8259   9582   7961   3071    958   1167       C  
-ATOM   8276  C   GLU B 404      -3.599  26.260  -7.283  1.00 63.85           C  
-ANISOU 8276  C   GLU B 404     7709   9088   7464   2961    826   1158       C  
-ATOM   8277  O   GLU B 404      -3.272  26.852  -6.259  1.00 61.27           O  
-ANISOU 8277  O   GLU B 404     7372   8637   7269   2926    844   1190       O  
-ATOM   8278  CB  GLU B 404      -3.265  27.731  -9.296  1.00 72.01           C  
-ANISOU 8278  CB  GLU B 404     8793  10205   8363   3234   1097   1292       C  
-ATOM   8279  CG  GLU B 404      -2.135  28.509  -9.966  1.00 78.69           C  
-ANISOU 8279  CG  GLU B 404     9685  10919   9295   3337   1289   1336       C  
-ATOM   8280  CD  GLU B 404      -1.116  29.065  -8.975  1.00 81.34           C  
-ANISOU 8280  CD  GLU B 404    10006  11028   9871   3293   1357   1335       C  
-ATOM   8281  OE1 GLU B 404      -0.596  28.287  -8.144  1.00 83.96           O  
-ANISOU 8281  OE1 GLU B 404    10313  11245  10344   3165   1249   1245       O  
-ATOM   8282  OE2 GLU B 404      -0.837  30.284  -9.026  1.00 80.12           O  
-ANISOU 8282  OE2 GLU B 404     9865  10812   9764   3389   1519   1422       O  
-ATOM   8283  N   LEU B 405      -4.636  25.434  -7.339  1.00 69.25           N  
-ANISOU 8283  N   LEU B 405     8375   9927   8011   2901    702   1105       N  
-ATOM   8284  CA  LEU B 405      -5.396  25.077  -6.151  1.00 66.71           C  
-ANISOU 8284  CA  LEU B 405     8029   9618   7699   2779    578   1076       C  
-ATOM   8285  C   LEU B 405      -4.648  24.001  -5.381  1.00 67.21           C  
-ANISOU 8285  C   LEU B 405     8113   9518   7905   2637    481    986       C  
-ATOM   8286  O   LEU B 405      -4.540  24.053  -4.155  1.00 64.26           O  
-ANISOU 8286  O   LEU B 405     7743   9037   7634   2547    427    989       O  
-ATOM   8287  CB  LEU B 405      -6.780  24.569  -6.546  1.00 64.94           C  
-ANISOU 8287  CB  LEU B 405     7773   9619   7281   2765    493   1039       C  
-ATOM   8288  CG  LEU B 405      -7.576  23.823  -5.476  1.00 61.89           C  
-ANISOU 8288  CG  LEU B 405     7372   9250   6895   2613    360    969       C  
-ATOM   8289  CD1 LEU B 405      -7.705  24.654  -4.205  1.00 61.13           C  
-ANISOU 8289  CD1 LEU B 405     7271   9063   6893   2573    373   1033       C  
-ATOM   8290  CD2 LEU B 405      -8.949  23.439  -6.015  1.00 61.54           C  
-ANISOU 8290  CD2 LEU B 405     7281   9440   6660   2617    298    923       C  
-ATOM   8291  N   GLU B 406      -4.125  23.029  -6.118  1.00 69.44           N  
-ANISOU 8291  N   GLU B 406     8411   9781   8193   2620    462    906       N  
-ATOM   8292  CA  GLU B 406      -3.374  21.936  -5.524  1.00 70.96           C  
-ANISOU 8292  CA  GLU B 406     8622   9814   8527   2502    374    823       C  
-ATOM   8293  C   GLU B 406      -2.155  22.464  -4.780  1.00 68.53           C  
-ANISOU 8293  C   GLU B 406     8321   9292   8427   2501    410    856       C  
-ATOM   8294  O   GLU B 406      -1.558  21.761  -3.970  1.00 69.66           O  
-ANISOU 8294  O   GLU B 406     8476   9290   8703   2406    320    810       O  
-ATOM   8295  CB  GLU B 406      -2.953  20.936  -6.598  1.00 77.89           C  
-ANISOU 8295  CB  GLU B 406     9508  10701   9387   2502    382    735       C  
-ATOM   8296  CG  GLU B 406      -2.510  19.598  -6.049  1.00 87.25           C  
-ANISOU 8296  CG  GLU B 406    10707  11758  10686   2373    275    641       C  
-ATOM   8297  CD  GLU B 406      -1.027  19.355  -6.228  1.00 92.08           C  
-ANISOU 8297  CD  GLU B 406    11324  12168  11494   2386    319    611       C  
-ATOM   8298  OE1 GLU B 406      -0.468  19.801  -7.255  1.00 95.42           O  
-ANISOU 8298  OE1 GLU B 406    11744  12593  11917   2482    442    618       O  
-ATOM   8299  OE2 GLU B 406      -0.419  18.718  -5.339  1.00 92.80           O  
-ANISOU 8299  OE2 GLU B 406    11423  12095  11740   2303    232    580       O  
-ATOM   8300  N   THR B 407      -1.790  23.710  -5.053  1.00 59.75           N  
-ANISOU 8300  N   THR B 407     7200   8161   7342   2610    543    935       N  
-ATOM   8301  CA  THR B 407      -0.689  24.340  -4.344  1.00 57.01           C  
-ANISOU 8301  CA  THR B 407     6848   7625   7190   2610    591    958       C  
-ATOM   8302  C   THR B 407      -1.155  24.826  -2.983  1.00 56.61           C  
-ANISOU 8302  C   THR B 407     6791   7555   7163   2538    531    999       C  
-ATOM   8303  O   THR B 407      -0.525  24.543  -1.964  1.00 56.31           O  
-ANISOU 8303  O   THR B 407     6757   7376   7262   2450    452    971       O  
-ATOM   8304  CB  THR B 407      -0.113  25.528  -5.127  1.00 54.81           C  
-ANISOU 8304  CB  THR B 407     6565   7321   6940   2748    780   1019       C  
-ATOM   8305  OG1 THR B 407       0.509  25.053  -6.326  1.00 54.06           O  
-ANISOU 8305  OG1 THR B 407     6485   7210   6845   2801    846    970       O  
-ATOM   8306  CG2 THR B 407       0.923  26.259  -4.286  1.00 52.36           C  
-ANISOU 8306  CG2 THR B 407     6236   6825   6832   2737    835   1030       C  
-ATOM   8307  N   ARG B 408      -2.264  25.558  -2.974  1.00 61.50           N  
-ANISOU 8307  N   ARG B 408     7401   8319   7648   2575    568   1063       N  
-ATOM   8308  CA  ARG B 408      -2.815  26.095  -1.739  1.00 59.73           C  
-ANISOU 8308  CA  ARG B 408     7171   8087   7436   2504    533   1100       C  
-ATOM   8309  C   ARG B 408      -3.120  24.957  -0.771  1.00 56.69           C  
-ANISOU 8309  C   ARG B 408     6813   7673   7053   2348    361   1034       C  
-ATOM   8310  O   ARG B 408      -2.875  25.063   0.427  1.00 54.47           O  
-ANISOU 8310  O   ARG B 408     6548   7289   6859   2256    306   1035       O  
-ATOM   8311  CB  ARG B 408      -4.090  26.885  -2.026  1.00 61.37           C  
-ANISOU 8311  CB  ARG B 408     7357   8470   7492   2570    593   1168       C  
-ATOM   8312  CG  ARG B 408      -4.003  27.812  -3.233  1.00 64.55           C  
-ANISOU 8312  CG  ARG B 408     7747   8938   7841   2740    752   1241       C  
-ATOM   8313  CD  ARG B 408      -2.895  28.846  -3.081  1.00 68.17           C  
-ANISOU 8313  CD  ARG B 408     8206   9239   8458   2799    897   1285       C  
-ATOM   8314  NE  ARG B 408      -3.110  30.022  -3.925  1.00 70.98           N  
-ANISOU 8314  NE  ARG B 408     8557   9658   8754   2956   1069   1383       N  
-ATOM   8315  CZ  ARG B 408      -2.684  30.140  -5.179  1.00 72.62           C  
-ANISOU 8315  CZ  ARG B 408     8789   9886   8918   3075   1170   1403       C  
-ATOM   8316  NH1 ARG B 408      -2.018  29.154  -5.758  1.00 74.14           N  
-ANISOU 8316  NH1 ARG B 408     9002  10040   9126   3050   1121   1323       N  
-ATOM   8317  NH2 ARG B 408      -2.928  31.248  -5.860  1.00 75.51           N  
-ANISOU 8317  NH2 ARG B 408     9163  10304   9222   3219   1326   1505       N  
-ATOM   8318  N   MET B 409      -3.647  23.862  -1.304  1.00 59.59           N  
-ANISOU 8318  N   MET B 409     7192   8129   7321   2316    282    974       N  
-ATOM   8319  CA  MET B 409      -3.987  22.705  -0.492  1.00 56.98           C  
-ANISOU 8319  CA  MET B 409     6896   7768   6984   2172    134    909       C  
-ATOM   8320  C   MET B 409      -2.758  21.964   0.016  1.00 56.48           C  
-ANISOU 8320  C   MET B 409     6863   7512   7085   2111     59    868       C  
-ATOM   8321  O   MET B 409      -2.769  21.426   1.120  1.00 56.53           O  
-ANISOU 8321  O   MET B 409     6910   7436   7131   1996    -51    851       O  
-ATOM   8322  CB  MET B 409      -4.868  21.743  -1.278  1.00 57.97           C  
-ANISOU 8322  CB  MET B 409     7019   8042   6966   2155     90    843       C  
-ATOM   8323  CG  MET B 409      -6.200  22.316  -1.676  1.00 58.78           C  
-ANISOU 8323  CG  MET B 409     7083   8348   6902   2202    129    870       C  
-ATOM   8324  SD  MET B 409      -7.288  21.028  -2.317  1.00 62.00           S  
-ANISOU 8324  SD  MET B 409     7481   8925   7153   2142     49    762       S  
-ATOM   8325  CE  MET B 409      -7.449  19.982  -0.868  1.00 62.31           C  
-ANISOU 8325  CE  MET B 409     7581   8839   7256   1948    -78    699       C  
-ATOM   8326  N   SER B 410      -1.707  21.914  -0.792  1.00 50.50           N  
-ANISOU 8326  N   SER B 410     6087   6679   6423   2190    119    852       N  
-ATOM   8327  CA  SER B 410      -0.493  21.220  -0.381  1.00 48.89           C  
-ANISOU 8327  CA  SER B 410     5895   6288   6394   2147     48    810       C  
-ATOM   8328  C   SER B 410       0.249  21.966   0.719  1.00 48.50           C  
-ANISOU 8328  C   SER B 410     5841   6105   6482   2125     36    848       C  
-ATOM   8329  O   SER B 410       0.929  21.351   1.540  1.00 49.61           O  
-ANISOU 8329  O   SER B 410     6002   6110   6739   2053    -77    823       O  
-ATOM   8330  CB  SER B 410       0.432  20.978  -1.573  1.00 48.18           C  
-ANISOU 8330  CB  SER B 410     5777   6147   6381   2233    128    770       C  
-ATOM   8331  OG  SER B 410       0.047  19.805  -2.274  1.00 46.63           O  
-ANISOU 8331  OG  SER B 410     5596   6013   6110   2202     86    702       O  
-ATOM   8332  N   SER B 411       0.111  23.288   0.740  1.00 47.42           N  
-ANISOU 8332  N   SER B 411     5677   6010   6331   2187    152    908       N  
-ATOM   8333  CA  SER B 411       0.810  24.109   1.722  1.00 47.71           C  
-ANISOU 8333  CA  SER B 411     5700   5932   6496   2166    164    933       C  
-ATOM   8334  C   SER B 411      -0.051  24.354   2.961  1.00 47.87           C  
-ANISOU 8334  C   SER B 411     5754   5992   6442   2060     95    964       C  
-ATOM   8335  O   SER B 411       0.465  24.625   4.046  1.00 46.40           O  
-ANISOU 8335  O   SER B 411     5576   5706   6348   1994     44    966       O  
-ATOM   8336  CB  SER B 411       1.235  25.443   1.103  1.00 47.61           C  
-ANISOU 8336  CB  SER B 411     5640   5917   6532   2285    353    973       C  
-ATOM   8337  OG  SER B 411       0.113  26.276   0.868  1.00 49.37           O  
-ANISOU 8337  OG  SER B 411     5861   6286   6610   2328    445   1038       O  
-ATOM   8338  N   LEU B 412      -1.364  24.257   2.792  1.00 54.57           N  
-ANISOU 8338  N   LEU B 412     6620   6989   7125   2041     95    980       N  
-ATOM   8339  CA  LEU B 412      -2.292  24.414   3.900  1.00 55.25           C  
-ANISOU 8339  CA  LEU B 412     6740   7117   7134   1931     40    997       C  
-ATOM   8340  C   LEU B 412      -2.469  23.088   4.627  1.00 55.87           C  
-ANISOU 8340  C   LEU B 412     6889   7149   7190   1801   -127    950       C  
-ATOM   8341  O   LEU B 412      -2.363  23.012   5.849  1.00 53.68           O  
-ANISOU 8341  O   LEU B 412     6660   6793   6943   1694   -210    953       O  
-ATOM   8342  CB  LEU B 412      -3.638  24.896   3.376  1.00 56.94           C  
-ANISOU 8342  CB  LEU B 412     6932   7510   7194   1972    119   1026       C  
-ATOM   8343  CG  LEU B 412      -4.235  26.073   4.140  1.00 56.74           C  
-ANISOU 8343  CG  LEU B 412     6892   7514   7151   1948    195   1077       C  
-ATOM   8344  CD1 LEU B 412      -3.133  27.024   4.580  1.00 56.62           C  
-ANISOU 8344  CD1 LEU B 412     6857   7372   7285   1974    271   1104       C  
-ATOM   8345  CD2 LEU B 412      -5.285  26.789   3.293  1.00 59.00           C  
-ANISOU 8345  CD2 LEU B 412     7129   7965   7323   2049    306   1121       C  
-ATOM   8346  N   GLN B 413      -2.723  22.040   3.855  1.00 49.69           N  
-ANISOU 8346  N   GLN B 413     6115   6412   6352   1810   -169    904       N  
-ATOM   8347  CA  GLN B 413      -2.961  20.713   4.402  1.00 50.65           C  
-ANISOU 8347  CA  GLN B 413     6306   6490   6450   1694   -306    857       C  
-ATOM   8348  C   GLN B 413      -4.225  20.719   5.244  1.00 50.55           C  
-ANISOU 8348  C   GLN B 413     6340   6555   6312   1581   -336    858       C  
-ATOM   8349  O   GLN B 413      -4.180  20.443   6.442  1.00 50.72           O  
-ANISOU 8349  O   GLN B 413     6433   6488   6351   1468   -424    863       O  
-ATOM   8350  CB  GLN B 413      -1.763  20.238   5.226  1.00 52.29           C  
-ANISOU 8350  CB  GLN B 413     6551   6510   6805   1647   -413    855       C  
-ATOM   8351  CG  GLN B 413      -0.422  20.489   4.554  1.00 54.83           C  
-ANISOU 8351  CG  GLN B 413     6812   6739   7283   1756   -367    850       C  
-ATOM   8352  CD  GLN B 413       0.690  19.601   5.082  1.00 54.88           C  
-ANISOU 8352  CD  GLN B 413     6844   6572   7436   1720   -495    826       C  
-ATOM   8353  OE1 GLN B 413       1.503  20.025   5.902  1.00 54.98           O  
-ANISOU 8353  OE1 GLN B 413     6852   6479   7557   1706   -542    846       O  
-ATOM   8354  NE2 GLN B 413       0.736  18.363   4.601  1.00 56.17           N  
-ANISOU 8354  NE2 GLN B 413     7029   6705   7607   1707   -552    781       N  
-ATOM   8355  N   PRO B 414      -5.364  21.044   4.613  1.00 59.12           N  
-ANISOU 8355  N   PRO B 414     7385   7807   7270   1614   -262    852       N  
-ATOM   8356  CA  PRO B 414      -6.662  21.095   5.292  1.00 57.60           C  
-ANISOU 8356  CA  PRO B 414     7219   7702   6966   1513   -272    839       C  
-ATOM   8357  C   PRO B 414      -7.091  19.722   5.795  1.00 55.91           C  
-ANISOU 8357  C   PRO B 414     7086   7452   6707   1380   -380    772       C  
-ATOM   8358  O   PRO B 414      -6.897  18.721   5.098  1.00 56.91           O  
-ANISOU 8358  O   PRO B 414     7214   7575   6833   1395   -414    721       O  
-ATOM   8359  CB  PRO B 414      -7.624  21.545   4.183  1.00 58.58           C  
-ANISOU 8359  CB  PRO B 414     7262   8017   6979   1609   -181    833       C  
-ATOM   8360  CG  PRO B 414      -6.765  22.150   3.126  1.00 58.33           C  
-ANISOU 8360  CG  PRO B 414     7172   7987   7003   1766    -99    875       C  
-ATOM   8361  CD  PRO B 414      -5.475  21.398   3.187  1.00 61.22           C  
-ANISOU 8361  CD  PRO B 414     7576   8193   7492   1753   -164    854       C  
-ATOM   8362  N   VAL B 415      -7.673  19.684   6.989  1.00 41.47           N  
-ANISOU 8362  N   VAL B 415     5326   5589   4840   1247   -419    770       N  
-ATOM   8363  CA  VAL B 415      -8.231  18.457   7.537  1.00 39.23           C  
-ANISOU 8363  CA  VAL B 415     5132   5271   4501   1111   -499    708       C  
-ATOM   8364  C   VAL B 415      -9.700  18.353   7.127  1.00 38.87           C  
-ANISOU 8364  C   VAL B 415     5047   5393   4328   1079   -445    642       C  
-ATOM   8365  O   VAL B 415     -10.286  17.270   7.113  1.00 38.14           O  
-ANISOU 8365  O   VAL B 415     4996   5314   4181    994   -481    565       O  
-ATOM   8366  CB  VAL B 415      -8.096  18.419   9.077  1.00 37.30           C  
-ANISOU 8366  CB  VAL B 415     5002   4897   4272    973   -567    736       C  
-ATOM   8367  CG1 VAL B 415      -6.696  18.005   9.480  1.00 35.27           C  
-ANISOU 8367  CG1 VAL B 415     4799   4470   4133    984   -664    775       C  
-ATOM   8368  CG2 VAL B 415      -8.430  19.774   9.675  1.00 38.05           C  
-ANISOU 8368  CG2 VAL B 415     5069   5032   4356    962   -494    781       C  
-ATOM   8369  N   GLU B 416     -10.290  19.488   6.771  1.00 44.79           N  
-ANISOU 8369  N   GLU B 416     5709   6271   5039   1152   -355    670       N  
-ATOM   8370  CA  GLU B 416     -11.686  19.514   6.366  1.00 45.30           C  
-ANISOU 8370  CA  GLU B 416     5714   6505   4992   1138   -308    608       C  
-ATOM   8371  C   GLU B 416     -11.879  20.457   5.185  1.00 44.93           C  
-ANISOU 8371  C   GLU B 416     5543   6611   4916   1308   -225    645       C  
-ATOM   8372  O   GLU B 416     -11.150  21.440   5.034  1.00 43.56           O  
-ANISOU 8372  O   GLU B 416     5340   6402   4807   1410   -173    730       O  
-ATOM   8373  CB  GLU B 416     -12.564  19.938   7.544  1.00 46.43           C  
-ANISOU 8373  CB  GLU B 416     5897   6639   5104   1009   -287    600       C  
-ATOM   8374  CG  GLU B 416     -14.055  19.721   7.335  1.00 48.35           C  
-ANISOU 8374  CG  GLU B 416     6089   7033   5247    957   -254    510       C  
-ATOM   8375  CD  GLU B 416     -14.860  19.954   8.606  1.00 47.73           C  
-ANISOU 8375  CD  GLU B 416     6071   6914   5152    800   -230    486       C  
-ATOM   8376  OE1 GLU B 416     -16.064  19.615   8.628  1.00 46.18           O  
-ANISOU 8376  OE1 GLU B 416     5848   6810   4888    724   -207    393       O  
-ATOM   8377  OE2 GLU B 416     -14.285  20.472   9.587  1.00 47.63           O  
-ANISOU 8377  OE2 GLU B 416     6129   6776   5193    747   -231    550       O  
-ATOM   8378  N   LEU B 417     -12.855  20.144   4.339  1.00 41.36           N  
-ANISOU 8378  N   LEU B 417     5022   6329   4365   1338   -212    577       N  
-ATOM   8379  CA  LEU B 417     -13.196  21.008   3.217  1.00 42.35           C  
-ANISOU 8379  CA  LEU B 417     5036   6619   4437   1500   -143    614       C  
-ATOM   8380  C   LEU B 417     -14.683  21.356   3.219  1.00 44.69           C  
-ANISOU 8380  C   LEU B 417     5257   7080   4643   1482   -114    570       C  
-ATOM   8381  O   LEU B 417     -15.535  20.476   3.356  1.00 45.85           O  
-ANISOU 8381  O   LEU B 417     5407   7285   4730   1375   -154    460       O  
-ATOM   8382  CB  LEU B 417     -12.820  20.350   1.885  1.00 38.09           C  
-ANISOU 8382  CB  LEU B 417     4463   6154   3856   1594   -159    578       C  
-ATOM   8383  CG  LEU B 417     -11.342  20.172   1.541  1.00 35.74           C  
-ANISOU 8383  CG  LEU B 417     4206   5719   3653   1654   -163    623       C  
-ATOM   8384  CD1 LEU B 417     -11.198  19.388   0.248  1.00 31.78           C  
-ANISOU 8384  CD1 LEU B 417     3674   5306   3095   1716   -172    560       C  
-ATOM   8385  CD2 LEU B 417     -10.654  21.520   1.436  1.00 34.21           C  
-ANISOU 8385  CD2 LEU B 417     3987   5486   3525   1780    -81    740       C  
-ATOM   8386  N   LEU B 418     -14.986  22.642   3.066  1.00 46.24           N  
-ANISOU 8386  N   LEU B 418     5382   7346   4840   1588    -37    650       N  
-ATOM   8387  CA  LEU B 418     -16.360  23.088   2.892  1.00 47.71           C  
-ANISOU 8387  CA  LEU B 418     5473   7701   4952   1607     -7    618       C  
-ATOM   8388  C   LEU B 418     -16.612  23.302   1.407  1.00 50.64           C  
-ANISOU 8388  C   LEU B 418     5747   8261   5232   1784      3    633       C  
-ATOM   8389  O   LEU B 418     -16.051  24.223   0.808  1.00 51.54           O  
-ANISOU 8389  O   LEU B 418     5836   8383   5362   1939     65    743       O  
-ATOM   8390  CB  LEU B 418     -16.592  24.394   3.645  1.00 45.74           C  
-ANISOU 8390  CB  LEU B 418     5202   7410   4766   1619     79    701       C  
-ATOM   8391  CG  LEU B 418     -18.020  24.937   3.586  1.00 45.24           C  
-ANISOU 8391  CG  LEU B 418     5032   7503   4653   1637    116    670       C  
-ATOM   8392  CD1 LEU B 418     -19.016  23.856   3.978  1.00 43.38           C  
-ANISOU 8392  CD1 LEU B 418     4801   7319   4364   1477     54    520       C  
-ATOM   8393  CD2 LEU B 418     -18.176  26.166   4.468  1.00 42.21           C  
-ANISOU 8393  CD2 LEU B 418     4639   7046   4354   1623    213    745       C  
-ATOM   8394  N   LEU B 419     -17.444  22.454   0.809  1.00 51.12           N  
-ANISOU 8394  N   LEU B 419     5758   8474   5193   1759    -52    519       N  
-ATOM   8395  CA  LEU B 419     -17.666  22.514  -0.635  1.00 55.03           C  
-ANISOU 8395  CA  LEU B 419     6168   9160   5579   1916    -60    520       C  
-ATOM   8396  C   LEU B 419     -19.131  22.671  -1.024  1.00 58.58           C  
-ANISOU 8396  C   LEU B 419     6495   9832   5931   1947    -77    453       C  
-ATOM   8397  O   LEU B 419     -20.018  22.134  -0.359  1.00 59.27           O  
-ANISOU 8397  O   LEU B 419     6564   9937   6017   1805   -105    339       O  
-ATOM   8398  CB  LEU B 419     -17.099  21.269  -1.321  1.00 50.96           C  
-ANISOU 8398  CB  LEU B 419     5694   8645   5025   1884   -116    436       C  
-ATOM   8399  CG  LEU B 419     -15.627  20.961  -1.078  1.00 47.10           C  
-ANISOU 8399  CG  LEU B 419     5311   7945   4638   1862   -111    486       C  
-ATOM   8400  CD1 LEU B 419     -15.201  19.768  -1.915  1.00 45.48           C  
-ANISOU 8400  CD1 LEU B 419     5125   7762   4392   1845   -154    396       C  
-ATOM   8401  CD2 LEU B 419     -14.775  22.177  -1.382  1.00 45.84           C  
-ANISOU 8401  CD2 LEU B 419     5155   7731   4531   2016    -34    636       C  
-ATOM   8402  N   PRO B 420     -19.383  23.401  -2.120  1.00 57.98           N  
-ANISOU 8402  N   PRO B 420     6334   9923   5771   2135    -60    522       N  
-ATOM   8403  CA  PRO B 420     -20.728  23.514  -2.683  1.00 60.71           C  
-ANISOU 8403  CA  PRO B 420     6548  10507   6012   2191    -96    458       C  
-ATOM   8404  C   PRO B 420     -21.156  22.164  -3.224  1.00 64.92           C  
-ANISOU 8404  C   PRO B 420     7057  11161   6450   2104   -178    286       C  
-ATOM   8405  O   PRO B 420     -20.302  21.394  -3.660  1.00 64.74           O  
-ANISOU 8405  O   PRO B 420     7104  11082   6412   2082   -196    260       O  
-ATOM   8406  CB  PRO B 420     -20.541  24.498  -3.838  1.00 63.70           C  
-ANISOU 8406  CB  PRO B 420     6879  11008   6316   2426    -64    594       C  
-ATOM   8407  CG  PRO B 420     -19.262  25.206  -3.546  1.00 61.95           C  
-ANISOU 8407  CG  PRO B 420     6756  10583   6198   2477     23    739       C  
-ATOM   8408  CD  PRO B 420     -18.405  24.203  -2.872  1.00 57.18           C  
-ANISOU 8408  CD  PRO B 420     6260   9794   5673   2309     -2    668       C  
-ATOM   8409  N   SER B 421     -22.454  21.880  -3.188  1.00 76.65           N  
-ANISOU 8409  N   SER B 421     8436  12804   7882   2051   -220    161       N  
-ATOM   8410  CA  SER B 421     -22.975  20.616  -3.695  1.00 81.86           C  
-ANISOU 8410  CA  SER B 421     9056  13593   8453   1960   -288    -24       C  
-ATOM   8411  C   SER B 421     -22.403  20.303  -5.078  1.00 84.65           C  
-ANISOU 8411  C   SER B 421     9408  14067   8690   2080   -319    -12       C  
-ATOM   8412  O   SER B 421     -22.028  19.165  -5.365  1.00 86.23           O  
-ANISOU 8412  O   SER B 421     9653  14245   8866   1986   -343   -122       O  
-ATOM   8413  CB  SER B 421     -24.506  20.644  -3.749  1.00 84.82           C  
-ANISOU 8413  CB  SER B 421     9281  14174   8774   1944   -325   -146       C  
-ATOM   8414  OG  SER B 421     -25.061  21.019  -2.500  1.00 85.57           O  
-ANISOU 8414  OG  SER B 421     9376  14158   8980   1836   -281   -156       O  
-ATOM   8415  N   ALA B 422     -22.324  21.323  -5.927  1.00 68.62           N  
-ANISOU 8415  N   ALA B 422     7332  12152   6589   2286   -308    122       N  
-ATOM   8416  CA  ALA B 422     -21.890  21.132  -7.307  1.00 69.78           C  
-ANISOU 8416  CA  ALA B 422     7477  12435   6602   2410   -332    136       C  
-ATOM   8417  C   ALA B 422     -20.619  21.908  -7.639  1.00 68.07           C  
-ANISOU 8417  C   ALA B 422     7358  12086   6420   2542   -259    321       C  
-ATOM   8418  O   ALA B 422     -20.631  23.136  -7.704  1.00 69.02           O  
-ANISOU 8418  O   ALA B 422     7461  12213   6549   2692   -212    475       O  
-ATOM   8419  CB  ALA B 422     -23.003  21.518  -8.267  1.00 72.74           C  
-ANISOU 8419  CB  ALA B 422     7709  13108   6820   2546   -394    112       C  
-ATOM   8420  N   LEU B 423     -19.524  21.185  -7.852  1.00 76.44           N  
-ANISOU 8420  N   LEU B 423     8517  13018   7510   2487   -241    299       N  
-ATOM   8421  CA  LEU B 423     -18.282  21.800  -8.310  1.00 74.48           C  
-ANISOU 8421  CA  LEU B 423     8355  12652   7291   2607   -167    447       C  
-ATOM   8422  C   LEU B 423     -17.924  21.344  -9.720  1.00 76.41           C  
-ANISOU 8422  C   LEU B 423     8609  13031   7394   2686   -178    413       C  
-ATOM   8423  O   LEU B 423     -18.352  20.278 -10.169  1.00 75.76           O  
-ANISOU 8423  O   LEU B 423     8489  13071   7226   2599   -240    255       O  
-ATOM   8424  CB  LEU B 423     -17.124  21.494  -7.357  1.00 69.99           C  
-ANISOU 8424  CB  LEU B 423     7899  11794   6899   2492   -123    468       C  
-ATOM   8425  CG  LEU B 423     -16.950  22.384  -6.123  1.00 66.39           C  
-ANISOU 8425  CG  LEU B 423     7473  11164   6590   2471    -73    573       C  
-ATOM   8426  CD1 LEU B 423     -15.619  22.087  -5.453  1.00 65.10           C  
-ANISOU 8426  CD1 LEU B 423     7420  10737   6578   2389    -39    600       C  
-ATOM   8427  CD2 LEU B 423     -17.041  23.855  -6.485  1.00 65.03           C  
-ANISOU 8427  CD2 LEU B 423     7267  11046   6394   2660     -2    735       C  
-ATOM   8428  N   SER B 424     -17.139  22.161 -10.416  1.00 70.71           N  
-ANISOU 8428  N   SER B 424     7939  12281   6648   2843   -106    556       N  
-ATOM   8429  CA  SER B 424     -16.672  21.809 -11.746  1.00 74.36           C  
-ANISOU 8429  CA  SER B 424     8430  12845   6977   2916    -96    537       C  
-ATOM   8430  C   SER B 424     -16.062  20.413 -11.734  1.00 76.80           C  
-ANISOU 8430  C   SER B 424     8786  13058   7338   2751   -112    385       C  
-ATOM   8431  O   SER B 424     -15.483  19.988 -10.734  1.00 76.48           O  
-ANISOU 8431  O   SER B 424     8796  12796   7468   2623    -98    361       O  
-ATOM   8432  CB  SER B 424     -15.655  22.833 -12.248  1.00 74.47           C  
-ANISOU 8432  CB  SER B 424     8527  12759   7011   3076     15    712       C  
-ATOM   8433  OG  SER B 424     -14.593  22.997 -11.328  1.00 74.65           O  
-ANISOU 8433  OG  SER B 424     8626  12500   7239   3012     87    764       O  
-ATOM   8434  N   GLU B 425     -16.215  19.701 -12.845  1.00 87.38           N  
-ANISOU 8434  N   GLU B 425    10106  14568   8528   2753   -142    281       N  
-ATOM   8435  CA  GLU B 425     -15.688  18.349 -12.980  1.00 91.08           C  
-ANISOU 8435  CA  GLU B 425    10609  14961   9036   2602   -145    127       C  
-ATOM   8436  C   GLU B 425     -14.185  18.334 -12.746  1.00 87.21           C  
-ANISOU 8436  C   GLU B 425    10229  14195   8713   2588    -58    195       C  
-ATOM   8437  O   GLU B 425     -13.646  17.404 -12.148  1.00 86.48           O  
-ANISOU 8437  O   GLU B 425    10173  13927   8757   2443    -60    110       O  
-ATOM   8438  CB  GLU B 425     -15.997  17.801 -14.375  1.00101.23           C  
-ANISOU 8438  CB  GLU B 425    11861  16483  10119   2633   -169     24       C  
-ATOM   8439  CG  GLU B 425     -17.467  17.871 -14.760  1.00115.18           C  
-ANISOU 8439  CG  GLU B 425    13505  18553  11705   2668   -264    -47       C  
-ATOM   8440  CD  GLU B 425     -17.714  17.483 -16.210  1.00124.15           C  
-ANISOU 8440  CD  GLU B 425    14612  19940  12618   2719   -290   -132       C  
-ATOM   8441  OE1 GLU B 425     -16.728  17.326 -16.966  1.00129.05           O  
-ANISOU 8441  OE1 GLU B 425    15319  20497  13218   2746   -219   -112       O  
-ATOM   8442  OE2 GLU B 425     -18.896  17.335 -16.591  1.00128.02           O  
-ANISOU 8442  OE2 GLU B 425    14991  20693  12956   2729   -381   -227       O  
-ATOM   8443  N   GLN B 426     -13.516  19.377 -13.222  1.00 86.93           N  
-ANISOU 8443  N   GLN B 426    10243  14119   8669   2742     22    348       N  
-ATOM   8444  CA  GLN B 426     -12.070  19.481 -13.099  1.00 83.83           C  
-ANISOU 8444  CA  GLN B 426     9943  13475   8435   2745    115    410       C  
-ATOM   8445  C   GLN B 426     -11.638  19.441 -11.642  1.00 79.25           C  
-ANISOU 8445  C   GLN B 426     9387  12652   8074   2642    107    431       C  
-ATOM   8446  O   GLN B 426     -10.724  18.702 -11.272  1.00 77.98           O  
-ANISOU 8446  O   GLN B 426     9273  12295   8059   2543    119    378       O  
-ATOM   8447  CB  GLN B 426     -11.566  20.764 -13.762  1.00 84.89           C  
-ANISOU 8447  CB  GLN B 426    10121  13609   8523   2933    215    576       C  
-ATOM   8448  CG  GLN B 426     -11.515  20.704 -15.283  1.00 89.33           C  
-ANISOU 8448  CG  GLN B 426    10706  14345   8892   3028    251    561       C  
-ATOM   8449  CD  GLN B 426     -12.888  20.571 -15.917  1.00 92.30           C  
-ANISOU 8449  CD  GLN B 426    10999  15034   9037   3064    152    505       C  
-ATOM   8450  OE1 GLN B 426     -13.877  21.096 -15.402  1.00 94.32           O  
-ANISOU 8450  OE1 GLN B 426    11183  15392   9261   3101     89    548       O  
-ATOM   8451  NE2 GLN B 426     -12.954  19.863 -17.042  1.00 91.35           N  
-ANISOU 8451  NE2 GLN B 426    10880  15070   8757   3051    140    401       N  
-ATOM   8452  N   THR B 427     -12.310  20.236 -10.817  1.00 78.51           N  
-ANISOU 8452  N   THR B 427     9258  12573   7999   2667     84    510       N  
-ATOM   8453  CA  THR B 427     -11.981  20.331  -9.401  1.00 73.66           C  
-ANISOU 8453  CA  THR B 427     8670  11746   7571   2573     76    539       C  
-ATOM   8454  C   THR B 427     -12.370  19.071  -8.637  1.00 72.90           C  
-ANISOU 8454  C   THR B 427     8568  11607   7524   2385     -9    396       C  
-ATOM   8455  O   THR B 427     -11.579  18.545  -7.861  1.00 71.95           O  
-ANISOU 8455  O   THR B 427     8505  11274   7559   2284    -15    378       O  
-ATOM   8456  CB  THR B 427     -12.659  21.545  -8.745  1.00 72.26           C  
-ANISOU 8456  CB  THR B 427     8456  11602   7396   2642     89    654       C  
-ATOM   8457  OG1 THR B 427     -12.382  22.722  -9.514  1.00 71.11           O  
-ANISOU 8457  OG1 THR B 427     8319  11503   7196   2827    179    791       O  
-ATOM   8458  CG2 THR B 427     -12.149  21.732  -7.328  1.00 68.55           C  
-ANISOU 8458  CG2 THR B 427     8028  10902   7115   2548     96    691       C  
-ATOM   8459  N   GLU B 428     -13.587  18.590  -8.856  1.00 71.61           N  
-ANISOU 8459  N   GLU B 428     8335  11644   7229   2339    -74    294       N  
-ATOM   8460  CA  GLU B 428     -14.066  17.408  -8.150  1.00 74.15           C  
-ANISOU 8460  CA  GLU B 428     8652  11931   7590   2158   -139    150       C  
-ATOM   8461  C   GLU B 428     -13.045  16.270  -8.228  1.00 75.33           C  
-ANISOU 8461  C   GLU B 428     8869  11915   7839   2063   -129     73       C  
-ATOM   8462  O   GLU B 428     -12.841  15.537  -7.260  1.00 76.26           O  
-ANISOU 8462  O   GLU B 428     9032  11867   8077   1926   -158     24       O  
-ATOM   8463  CB  GLU B 428     -15.417  16.960  -8.712  1.00 75.61           C  
-ANISOU 8463  CB  GLU B 428     8743  12379   7608   2134   -194     23       C  
-ATOM   8464  CG  GLU B 428     -16.399  16.455  -7.660  1.00 75.87           C  
-ANISOU 8464  CG  GLU B 428     8745  12410   7673   1984   -246    -75       C  
-ATOM   8465  CD  GLU B 428     -17.001  17.574  -6.823  1.00 74.27           C  
-ANISOU 8465  CD  GLU B 428     8514  12207   7498   2026   -245     28       C  
-ATOM   8466  OE1 GLU B 428     -17.982  18.203  -7.279  1.00 74.43           O  
-ANISOU 8466  OE1 GLU B 428     8438  12438   7403   2118   -264     36       O  
-ATOM   8467  OE2 GLU B 428     -16.500  17.819  -5.706  1.00 72.92           O  
-ANISOU 8467  OE2 GLU B 428     8412  11827   7467   1968   -227     98       O  
-ATOM   8468  N   ALA B 429     -12.396  16.140  -9.381  1.00 87.71           N  
-ANISOU 8468  N   ALA B 429    10446  13521   9359   2137    -83     65       N  
-ATOM   8469  CA  ALA B 429     -11.410  15.085  -9.601  1.00 88.29           C  
-ANISOU 8469  CA  ALA B 429    10571  13443   9532   2058    -61    -14       C  
-ATOM   8470  C   ALA B 429     -10.155  15.312  -8.766  1.00 86.06           C  
-ANISOU 8470  C   ALA B 429    10362  12878   9459   2051    -35     80       C  
-ATOM   8471  O   ALA B 429      -9.521  14.361  -8.305  1.00 85.69           O  
-ANISOU 8471  O   ALA B 429    10358  12655   9546   1945    -51     19       O  
-ATOM   8472  CB  ALA B 429     -11.060  14.990 -11.076  1.00 89.57           C  
-ANISOU 8472  CB  ALA B 429    10724  13723   9584   2139     -5    -47       C  
-ATOM   8473  N   LEU B 430      -9.800  16.579  -8.582  1.00 79.61           N  
-ANISOU 8473  N   LEU B 430     9556  12020   8672   2167      6    225       N  
-ATOM   8474  CA  LEU B 430      -8.665  16.947  -7.745  1.00 77.80           C  
-ANISOU 8474  CA  LEU B 430     9382  11542   8637   2167     28    312       C  
-ATOM   8475  C   LEU B 430      -8.941  16.649  -6.279  1.00 76.28           C  
-ANISOU 8475  C   LEU B 430     9214  11230   8539   2042    -47    307       C  
-ATOM   8476  O   LEU B 430      -8.196  15.911  -5.633  1.00 76.94           O  
-ANISOU 8476  O   LEU B 430     9347  11121   8767   1953    -79    279       O  
-ATOM   8477  CB  LEU B 430      -8.334  18.429  -7.901  1.00 77.72           C  
-ANISOU 8477  CB  LEU B 430     9371  11532   8628   2316    104    458       C  
-ATOM   8478  CG  LEU B 430      -7.290  18.933  -6.906  1.00 78.40           C  
-ANISOU 8478  CG  LEU B 430     9499  11377   8911   2309    125    540       C  
-ATOM   8479  CD1 LEU B 430      -5.958  18.249  -7.146  1.00 78.27           C  
-ANISOU 8479  CD1 LEU B 430     9519  11178   9043   2285    148    496       C  
-ATOM   8480  CD2 LEU B 430      -7.140  20.440  -7.000  1.00 82.10           C  
-ANISOU 8480  CD2 LEU B 430     9960  11858   9376   2447    214    674       C  
-ATOM   8481  N   ILE B 431     -10.009  17.238  -5.753  1.00 67.89           N  
-ANISOU 8481  N   ILE B 431     8120  10279   7397   2038    -73    337       N  
-ATOM   8482  CA  ILE B 431     -10.374  17.011  -4.364  1.00 67.80           C  
-ANISOU 8482  CA  ILE B 431     8140  10166   7456   1912   -133    330       C  
-ATOM   8483  C   ILE B 431     -10.539  15.518  -4.137  1.00 71.10           C  
-ANISOU 8483  C   ILE B 431     8587  10536   7891   1764   -190    198       C  
-ATOM   8484  O   ILE B 431     -10.249  15.008  -3.057  1.00 71.84           O  
-ANISOU 8484  O   ILE B 431     8745  10459   8091   1655   -235    193       O  
-ATOM   8485  CB  ILE B 431     -11.655  17.776  -3.960  1.00 62.84           C  
-ANISOU 8485  CB  ILE B 431     7461   9687   6729   1920   -141    356       C  
-ATOM   8486  CG1 ILE B 431     -12.854  17.316  -4.791  1.00 62.77           C  
-ANISOU 8486  CG1 ILE B 431     7377   9920   6552   1917   -163    248       C  
-ATOM   8487  CG2 ILE B 431     -11.444  19.279  -4.100  1.00 63.42           C  
-ANISOU 8487  CG2 ILE B 431     7512   9781   6805   2067    -72    497       C  
-ATOM   8488  CD1 ILE B 431     -13.580  16.101  -4.230  1.00 56.38           C  
-ANISOU 8488  CD1 ILE B 431     6577   9111   5733   1745   -221    106       C  
-ATOM   8489  N   HIS B 432     -10.988  14.818  -5.171  1.00 66.15           N  
-ANISOU 8489  N   HIS B 432     7917  10060   7157   1761   -183     89       N  
-ATOM   8490  CA  HIS B 432     -11.102  13.369  -5.108  1.00 71.91           C  
-ANISOU 8490  CA  HIS B 432     8669  10744   7908   1624   -213    -48       C  
-ATOM   8491  C   HIS B 432      -9.729  12.748  -4.891  1.00 72.06           C  
-ANISOU 8491  C   HIS B 432     8758  10522   8100   1597   -210    -33       C  
-ATOM   8492  O   HIS B 432      -9.540  11.929  -3.993  1.00 72.28           O  
-ANISOU 8492  O   HIS B 432     8847  10389   8227   1482   -253    -63       O  
-ATOM   8493  CB  HIS B 432     -11.722  12.831  -6.396  1.00 78.55           C  
-ANISOU 8493  CB  HIS B 432     9442  11801   8603   1637   -192   -171       C  
-ATOM   8494  CG  HIS B 432     -11.835  11.339  -6.433  1.00 85.27           C  
-ANISOU 8494  CG  HIS B 432    10310  12610   9479   1495   -201   -325       C  
-ATOM   8495  ND1 HIS B 432     -12.851  10.654  -5.803  1.00 88.11           N  
-ANISOU 8495  ND1 HIS B 432    10665  13008   9806   1362   -232   -429       N  
-ATOM   8496  CD2 HIS B 432     -11.057  10.403  -7.024  1.00 87.71           C  
-ANISOU 8496  CD2 HIS B 432    10640  12832   9853   1463   -168   -398       C  
-ATOM   8497  CE1 HIS B 432     -12.695   9.357  -6.006  1.00 90.10           C  
-ANISOU 8497  CE1 HIS B 432    10937  13197  10099   1255   -216   -556       C  
-ATOM   8498  NE2 HIS B 432     -11.613   9.178  -6.743  1.00 89.69           N  
-ANISOU 8498  NE2 HIS B 432    10900  13070  10110   1315   -179   -539       N  
-ATOM   8499  N   ARG B 433      -8.772  13.150  -5.720  1.00 88.56           N  
-ANISOU 8499  N   ARG B 433    10839  12583  10228   1708   -157     15       N  
-ATOM   8500  CA  ARG B 433      -7.407  12.654  -5.622  1.00 89.07           C  
-ANISOU 8500  CA  ARG B 433    10950  12422  10471   1700   -147     26       C  
-ATOM   8501  C   ARG B 433      -6.818  12.924  -4.237  1.00 87.32           C  
-ANISOU 8501  C   ARG B 433    10787  11991  10399   1665   -202    118       C  
-ATOM   8502  O   ARG B 433      -6.094  12.093  -3.684  1.00 85.73           O  
-ANISOU 8502  O   ARG B 433    10635  11598  10339   1596   -242     99       O  
-ATOM   8503  CB  ARG B 433      -6.537  13.298  -6.703  1.00 90.00           C  
-ANISOU 8503  CB  ARG B 433    11045  12550  10600   1833    -64     70       C  
-ATOM   8504  CG  ARG B 433      -5.150  12.694  -6.841  1.00 93.79           C  
-ANISOU 8504  CG  ARG B 433    11553  12815  11267   1826    -39     51       C  
-ATOM   8505  CD  ARG B 433      -4.353  13.388  -7.937  1.00 97.68           C  
-ANISOU 8505  CD  ARG B 433    12027  13323  11765   1953     62     85       C  
-ATOM   8506  NE  ARG B 433      -5.073  13.418  -9.209  1.00103.41           N  
-ANISOU 8506  NE  ARG B 433    12718  14282  12291   1995    116     28       N  
-ATOM   8507  CZ  ARG B 433      -5.574  14.518  -9.762  1.00105.60           C  
-ANISOU 8507  CZ  ARG B 433    12974  14730  12418   2109    157    101       C  
-ATOM   8508  NH1 ARG B 433      -5.429  15.690  -9.161  1.00108.07           N  
-ANISOU 8508  NH1 ARG B 433    13295  14998  12770   2186    166    230       N  
-ATOM   8509  NH2 ARG B 433      -6.215  14.449 -10.922  1.00106.48           N  
-ANISOU 8509  NH2 ARG B 433    13057  15059  12340   2146    191     45       N  
-ATOM   8510  N   ALA B 434      -7.131  14.091  -3.681  1.00 94.08           N  
-ANISOU 8510  N   ALA B 434    11637  12886  11222   1715   -204    217       N  
-ATOM   8511  CA  ALA B 434      -6.631  14.465  -2.362  1.00 92.97           C  
-ANISOU 8511  CA  ALA B 434    11550  12571  11204   1679   -254    302       C  
-ATOM   8512  C   ALA B 434      -7.314  13.662  -1.256  1.00 93.29           C  
-ANISOU 8512  C   ALA B 434    11648  12561  11236   1530   -332    258       C  
-ATOM   8513  O   ALA B 434      -6.772  13.503  -0.163  1.00 92.41           O  
-ANISOU 8513  O   ALA B 434    11603  12273  11234   1470   -392    303       O  
-ATOM   8514  CB  ALA B 434      -6.808  15.960  -2.131  1.00 90.45           C  
-ANISOU 8514  CB  ALA B 434    11203  12312  10851   1768   -214    410       C  
-ATOM   8515  N   THR B 435      -8.505  13.156  -1.556  1.00 85.50           N  
-ANISOU 8515  N   THR B 435    10638  11732  10116   1468   -329    166       N  
-ATOM   8516  CA  THR B 435      -9.272  12.357  -0.607  1.00 86.86           C  
-ANISOU 8516  CA  THR B 435    10867  11867  10268   1319   -380    106       C  
-ATOM   8517  C   THR B 435      -8.805  10.904  -0.611  1.00 90.39           C  
-ANISOU 8517  C   THR B 435    11367  12179  10798   1232   -404     24       C  
-ATOM   8518  O   THR B 435      -9.058  10.156   0.333  1.00 91.56           O  
-ANISOU 8518  O   THR B 435    11595  12219  10975   1111   -447     -1       O  
-ATOM   8519  CB  THR B 435     -10.779  12.408  -0.935  1.00 86.19           C  
-ANISOU 8519  CB  THR B 435    10722  12008  10018   1285   -358     23       C  
-ATOM   8520  OG1 THR B 435     -11.268  13.739  -0.731  1.00 85.09           O  
-ANISOU 8520  OG1 THR B 435    10540  11971   9820   1356   -340    107       O  
-ATOM   8521  CG2 THR B 435     -11.563  11.445  -0.055  1.00 85.95           C  
-ANISOU 8521  CG2 THR B 435    10753  11931   9973   1119   -390    -64       C  
-ATOM   8522  N   SER B 436      -8.114  10.513  -1.677  1.00 93.33           N  
-ANISOU 8522  N   SER B 436    11701  12548  11211   1294   -365    -15       N  
-ATOM   8523  CA  SER B 436      -7.657   9.135  -1.828  1.00 98.93           C  
-ANISOU 8523  CA  SER B 436    12447  13132  12010   1219   -368   -101       C  
-ATOM   8524  C   SER B 436      -6.410   8.831  -0.995  1.00101.00           C  
-ANISOU 8524  C   SER B 436    12784  13130  12463   1213   -426    -23       C  
-ATOM   8525  O   SER B 436      -6.411   7.893  -0.195  1.00101.16           O  
-ANISOU 8525  O   SER B 436    12883  13010  12543   1111   -473    -43       O  
-ATOM   8526  CB  SER B 436      -7.405   8.814  -3.303  1.00 99.80           C  
-ANISOU 8526  CB  SER B 436    12486  13341  12093   1278   -296   -185       C  
-ATOM   8527  OG  SER B 436      -8.587   8.980  -4.065  1.00 99.81           O  
-ANISOU 8527  OG  SER B 436    12419  13596  11909   1278   -258   -266       O  
-ATOM   8528  N   VAL B 437      -5.353   9.617  -1.183  1.00204.74           N  
-ANISOU 8528  N   VAL B 437    25896  26199  25695   1324   -422     63       N  
-ATOM   8529  CA  VAL B 437      -4.104   9.400  -0.456  1.00205.64           C  
-ANISOU 8529  CA  VAL B 437    26060  26075  26000   1333   -485    130       C  
-ATOM   8530  C   VAL B 437      -4.353   9.235   1.037  1.00208.65           C  
-ANISOU 8530  C   VAL B 437    26538  26347  26394   1240   -579    187       C  
-ATOM   8531  O   VAL B 437      -4.241   8.135   1.581  1.00209.83           O  
-ANISOU 8531  O   VAL B 437    26759  26359  26607   1156   -628    162       O  
-ATOM   8532  CB  VAL B 437      -3.119  10.568  -0.658  1.00126.19           C  
-ANISOU 8532  CB  VAL B 437    15950  15977  16020   1459   -464    218       C  
-ATOM   8533  CG1 VAL B 437      -1.883  10.381   0.214  1.00126.18           C  
-ANISOU 8533  CG1 VAL B 437    15989  15738  16215   1464   -547    281       C  
-ATOM   8534  CG2 VAL B 437      -2.737  10.700  -2.129  1.00126.54           C  
-ANISOU 8534  CG2 VAL B 437    15918  16102  16060   1550   -362    166       C  
-ATOM   8535  N   SER B 438      -4.684  10.345   1.689  1.00170.39           N  
-ANISOU 8535  N   SER B 438    21697  21558  21486   1256   -597    266       N  
-ATOM   8536  CA  SER B 438      -5.007  10.352   3.110  1.00176.93           C  
-ANISOU 8536  CA  SER B 438    22620  22304  22300   1162   -676    320       C  
-ATOM   8537  C   SER B 438      -5.768   9.097   3.537  1.00179.16           C  
-ANISOU 8537  C   SER B 438    22985  22552  22535   1027   -697    247       C  
-ATOM   8538  O   SER B 438      -6.923   8.896   3.161  1.00180.15           O  
-ANISOU 8538  O   SER B 438    23089  22829  22531    973   -641    163       O  
-ATOM   8539  CB  SER B 438      -5.813  11.604   3.454  1.00 81.73           C  
-ANISOU 8539  CB  SER B 438    10540  10389  10125   1170   -649    366       C  
-ATOM   8540  OG  SER B 438      -6.838  11.823   2.497  1.00 81.80           O  
-ANISOU 8540  OG  SER B 438    10472  10610   9998   1193   -567    297       O  
-ATOM   8541  N   VAL B 439      -5.103   8.259   4.325  1.00199.21           N  
-ANISOU 8541  N   VAL B 439    25618  24888  25183    977   -775    278       N  
-ATOM   8542  CA  VAL B 439      -5.679   7.010   4.814  1.00198.44           C  
-ANISOU 8542  CA  VAL B 439    25620  24716  25062    851   -787    222       C  
-ATOM   8543  C   VAL B 439      -6.844   7.291   5.764  1.00200.24           C  
-ANISOU 8543  C   VAL B 439    25923  25008  25150    741   -791    225       C  
-ATOM   8544  O   VAL B 439      -7.188   8.447   6.005  1.00199.04           O  
-ANISOU 8544  O   VAL B 439    25737  24961  24929    766   -784    270       O  
-ATOM   8545  CB  VAL B 439      -4.603   6.170   5.536  1.00104.35           C  
-ANISOU 8545  CB  VAL B 439    13797  12552  13301    841   -881    283       C  
-ATOM   8546  CG1 VAL B 439      -5.140   4.790   5.920  1.00105.27           C  
-ANISOU 8546  CG1 VAL B 439    14021  12573  13404    720   -873    224       C  
-ATOM   8547  CG2 VAL B 439      -3.359   6.045   4.657  1.00104.54           C  
-ANISOU 8547  CG2 VAL B 439    13733  12501  13488    957   -877    282       C  
-ATOM   8548  N   GLN B 440      -7.453   6.234   6.296  1.00114.79           N  
-ANISOU 8548  N   GLN B 440    15203  14116  14295    616   -788    172       N  
-ATOM   8549  CA  GLN B 440      -8.563   6.372   7.236  1.00118.22           C  
-ANISOU 8549  CA  GLN B 440    15723  14588  14606    493   -778    161       C  
-ATOM   8550  C   GLN B 440      -8.152   7.147   8.486  1.00117.80           C  
-ANISOU 8550  C   GLN B 440    15755  14443  14559    483   -864    290       C  
-ATOM   8551  O   GLN B 440      -8.996   7.522   9.301  1.00119.35           O  
-ANISOU 8551  O   GLN B 440    16015  14676  14655    388   -852    292       O  
-ATOM   8552  CB  GLN B 440      -9.111   5.002   7.616  1.00124.18           C  
-ANISOU 8552  CB  GLN B 440    16591  15244  15347    360   -751     85       C  
-ATOM   8553  N   ASP B 441      -6.851   7.381   8.632  1.00127.34           N  
-ANISOU 8553  N   ASP B 441    16961  15531  15890    575   -948    385       N  
-ATOM   8554  CA  ASP B 441      -6.330   8.140   9.764  1.00124.26           C  
-ANISOU 8554  CA  ASP B 441    16639  15062  15514    572  -1037    500       C  
-ATOM   8555  C   ASP B 441      -6.620   9.632   9.629  1.00119.17           C  
-ANISOU 8555  C   ASP B 441    15897  14572  14811    623   -993    523       C  
-ATOM   8556  O   ASP B 441      -7.403  10.195  10.396  1.00117.77           O  
-ANISOU 8556  O   ASP B 441    15768  14445  14533    540   -976    533       O  
-ATOM   8557  CB  ASP B 441      -4.826   7.894   9.941  1.00130.54           C  
-ANISOU 8557  CB  ASP B 441    17445  15683  16470    658  -1145    582       C  
-ATOM   8558  CG  ASP B 441      -4.063   7.907   8.623  1.00131.97           C  
-ANISOU 8558  CG  ASP B 441    17482  15893  16767    789  -1105    546       C  
-ATOM   8559  OD1 ASP B 441      -3.081   7.144   8.503  1.00135.90           O  
-ANISOU 8559  OD1 ASP B 441    17990  16241  17406    834  -1162    562       O  
-ATOM   8560  OD2 ASP B 441      -4.432   8.675   7.710  1.00134.49           O  
-ANISOU 8560  OD2 ASP B 441    17683  16380  17038    849  -1015    503       O  
-ATOM   8561  N   ASP B 442      -5.983  10.265   8.651  1.00 96.92           N  
-ANISOU 8561  N   ASP B 442    12945  11819  12062    758   -963    529       N  
-ATOM   8562  CA  ASP B 442      -6.182  11.683   8.394  1.00 91.40           C  
-ANISOU 8562  CA  ASP B 442    12148  11257  11322    826   -905    556       C  
-ATOM   8563  C   ASP B 442      -6.875  11.913   7.058  1.00 86.18           C  
-ANISOU 8563  C   ASP B 442    11364  10785  10594    891   -797    480       C  
-ATOM   8564  O   ASP B 442      -6.413  12.702   6.237  1.00 85.86           O  
-ANISOU 8564  O   ASP B 442    11220  10814  10590   1014   -751    501       O  
-ATOM   8565  CB  ASP B 442      -4.849  12.427   8.432  1.00 90.32           C  
-ANISOU 8565  CB  ASP B 442    11964  11041  11314    934   -949    635       C  
-ATOM   8566  CG  ASP B 442      -4.660  13.212   9.712  1.00 92.24           C  
-ANISOU 8566  CG  ASP B 442    12271  11227  11549    883  -1006    713       C  
-ATOM   8567  OD1 ASP B 442      -4.893  14.439   9.693  1.00 90.53           O  
-ANISOU 8567  OD1 ASP B 442    11990  11109  11300    918   -942    736       O  
-ATOM   8568  OD2 ASP B 442      -4.283  12.601  10.735  1.00 92.20           O  
-ANISOU 8568  OD2 ASP B 442    12384  11080  11569    809  -1112    751       O  
-ATOM   8569  N   ARG B 443      -7.988  11.221   6.850  1.00113.82           N  
-ANISOU 8569  N   ARG B 443    14881  14370  13997    807   -755    389       N  
-ATOM   8570  CA  ARG B 443      -8.783  11.392   5.642  1.00106.06           C  
-ANISOU 8570  CA  ARG B 443    13782  13587  12929    857   -666    307       C  
-ATOM   8571  C   ARG B 443      -9.463  12.754   5.658  1.00 96.43           C  
-ANISOU 8571  C   ARG B 443    12493  12519  11628    898   -615    341       C  
-ATOM   8572  O   ARG B 443     -10.330  13.012   6.491  1.00 95.76           O  
-ANISOU 8572  O   ARG B 443    12451  12459  11473    803   -608    335       O  
-ATOM   8573  CB  ARG B 443      -9.833  10.285   5.541  1.00114.75           C  
-ANISOU 8573  CB  ARG B 443    14914  14735  13949    742   -638    186       C  
-ATOM   8574  CG  ARG B 443      -9.940   9.652   4.170  1.00125.28           C  
-ANISOU 8574  CG  ARG B 443    16158  16173  15269    790   -585     85       C  
-ATOM   8575  CD  ARG B 443     -10.728   8.359   4.233  1.00138.81           C  
-ANISOU 8575  CD  ARG B 443    17922  17878  16941    659   -561    -38       C  
-ATOM   8576  NE  ARG B 443     -10.409   7.475   3.117  1.00150.25           N  
-ANISOU 8576  NE  ARG B 443    19318  19345  18425    689   -525   -127       N  
-ATOM   8577  CZ  ARG B 443     -10.430   6.147   3.188  1.00156.63           C  
-ANISOU 8577  CZ  ARG B 443    20190  20048  19274    595   -512   -207       C  
-ATOM   8578  NH1 ARG B 443     -10.753   5.548   4.327  1.00158.65           N  
-ANISOU 8578  NH1 ARG B 443    20574  20169  19535    471   -535   -203       N  
-ATOM   8579  NH2 ARG B 443     -10.125   5.418   2.123  1.00160.42           N  
-ANISOU 8579  NH2 ARG B 443    20611  20550  19791    623   -467   -293       N  
-ATOM   8580  N   ILE B 444      -9.064  13.628   4.741  1.00 62.99           N  
-ANISOU 8580  N   ILE B 444     8153   8373   7407   1039   -569    376       N  
-ATOM   8581  CA  ILE B 444      -9.659  14.952   4.656  1.00 52.70           C  
-ANISOU 8581  CA  ILE B 444     6777   7207   6038   1098   -509    418       C  
-ATOM   8582  C   ILE B 444     -11.177  14.841   4.608  1.00 49.17           C  
-ANISOU 8582  C   ILE B 444     6301   6920   5461   1026   -472    335       C  
-ATOM   8583  O   ILE B 444     -11.736  14.268   3.673  1.00 49.19           O  
-ANISOU 8583  O   ILE B 444     6246   7047   5397   1040   -448    244       O  
-ATOM   8584  CB  ILE B 444      -9.139  15.729   3.430  1.00 46.85           C  
-ANISOU 8584  CB  ILE B 444     5931   6558   5312   1267   -447    454       C  
-ATOM   8585  CG1 ILE B 444      -7.645  16.004   3.584  1.00 45.09           C  
-ANISOU 8585  CG1 ILE B 444     5728   6170   5234   1333   -470    530       C  
-ATOM   8586  CG2 ILE B 444      -9.895  17.036   3.259  1.00 45.49           C  
-ANISOU 8586  CG2 ILE B 444     5684   6537   5063   1335   -376    497       C  
-ATOM   8587  CD1 ILE B 444      -7.016  16.615   2.362  1.00 41.17           C  
-ANISOU 8587  CD1 ILE B 444     5146   5731   4764   1488   -397    555       C  
-ATOM   8588  N   ARG B 445     -11.837  15.375   5.634  1.00 56.40           N  
-ANISOU 8588  N   ARG B 445     7254   7830   6344    943   -466    355       N  
-ATOM   8589  CA  ARG B 445     -13.293  15.323   5.730  1.00 52.50           C  
-ANISOU 8589  CA  ARG B 445     6730   7472   5746    863   -427    270       C  
-ATOM   8590  C   ARG B 445     -13.927  16.354   4.811  1.00 51.64           C  
-ANISOU 8590  C   ARG B 445     6480   7566   5573    989   -363    278       C  
-ATOM   8591  O   ARG B 445     -13.490  17.504   4.767  1.00 50.55           O  
-ANISOU 8591  O   ARG B 445     6304   7433   5471   1091   -330    378       O  
-ATOM   8592  CB  ARG B 445     -13.751  15.575   7.168  1.00 50.71           C  
-ANISOU 8592  CB  ARG B 445     6595   7157   5515    724   -431    287       C  
-ATOM   8593  CG  ARG B 445     -15.222  15.259   7.409  1.00 47.91           C  
-ANISOU 8593  CG  ARG B 445     6228   6903   5072    608   -390    174       C  
-ATOM   8594  CD  ARG B 445     -15.730  15.825   8.734  1.00 48.24           C  
-ANISOU 8594  CD  ARG B 445     6342   6880   5107    487   -367    197       C  
-ATOM   8595  NE  ARG B 445     -16.597  16.984   8.526  1.00 48.57           N  
-ANISOU 8595  NE  ARG B 445     6266   7073   5116    540   -294    199       N  
-ATOM   8596  CZ  ARG B 445     -17.925  16.931   8.467  1.00 48.71           C  
-ANISOU 8596  CZ  ARG B 445     6221   7214   5072    477   -245     95       C  
-ATOM   8597  NH1 ARG B 445     -18.626  18.043   8.264  1.00 46.47           N  
-ANISOU 8597  NH1 ARG B 445     5822   7059   4776    544   -184    110       N  
-ATOM   8598  NH2 ARG B 445     -18.549  15.770   8.617  1.00 47.40           N  
-ANISOU 8598  NH2 ARG B 445     6106   7038   4867    349   -250    -29       N  
-ATOM   8599  N   VAL B 446     -14.958  15.945   4.079  1.00 44.53           N  
-ANISOU 8599  N   VAL B 446     5503   6835   4581    984   -342    171       N  
-ATOM   8600  CA  VAL B 446     -15.656  16.864   3.191  1.00 44.78           C  
-ANISOU 8600  CA  VAL B 446     5400   7074   4539   1108   -295    178       C  
-ATOM   8601  C   VAL B 446     -17.059  17.197   3.679  1.00 45.31           C  
-ANISOU 8601  C   VAL B 446     5420   7249   4548   1033   -265    116       C  
-ATOM   8602  O   VAL B 446     -17.909  16.323   3.815  1.00 45.00           O  
-ANISOU 8602  O   VAL B 446     5382   7253   4462    916   -273    -13       O  
-ATOM   8603  CB  VAL B 446     -15.765  16.302   1.774  1.00 43.71           C  
-ANISOU 8603  CB  VAL B 446     5184   7091   4333   1191   -299    104       C  
-ATOM   8604  CG1 VAL B 446     -16.726  17.142   0.958  1.00 43.60           C  
-ANISOU 8604  CG1 VAL B 446     5036   7311   4220   1304   -265     99       C  
-ATOM   8605  CG2 VAL B 446     -14.394  16.258   1.119  1.00 43.59           C  
-ANISOU 8605  CG2 VAL B 446     5192   6991   4380   1296   -304    175       C  
-ATOM   8606  N   GLU B 447     -17.296  18.474   3.944  1.00 57.93           N  
-ANISOU 8606  N   GLU B 447     5146   7729   9136   1984  -2266    126       N  
-ATOM   8607  CA  GLU B 447     -18.636  18.946   4.258  1.00 61.68           C  
-ANISOU 8607  CA  GLU B 447     5521   8425   9490   1982  -2098    251       C  
-ATOM   8608  C   GLU B 447     -19.250  19.597   3.029  1.00 65.16           C  
-ANISOU 8608  C   GLU B 447     5776   9169   9811   2265  -1972    245       C  
-ATOM   8609  O   GLU B 447     -18.670  20.520   2.453  1.00 65.10           O  
-ANISOU 8609  O   GLU B 447     5823   9173   9738   2485  -1815    248       O  
-ATOM   8610  CB  GLU B 447     -18.603  19.961   5.398  1.00 62.11           C  
-ANISOU 8610  CB  GLU B 447     5740   8383   9476   1950  -1858    399       C  
-ATOM   8611  CG  GLU B 447     -19.899  20.741   5.547  1.00 64.47           C  
-ANISOU 8611  CG  GLU B 447     5925   8933   9639   2033  -1624    520       C  
-ATOM   8612  CD  GLU B 447     -21.020  19.925   6.180  1.00 67.50           C  
-ANISOU 8612  CD  GLU B 447     6211   9405  10032   1794  -1706    555       C  
-ATOM   8613  OE1 GLU B 447     -20.726  18.893   6.827  1.00 68.87           O  
-ANISOU 8613  OE1 GLU B 447     6474   9388  10305   1528  -1910    522       O  
-ATOM   8614  OE2 GLU B 447     -22.197  20.323   6.026  1.00 68.39           O  
-ANISOU 8614  OE2 GLU B 447     6155   9776  10055   1873  -1565    618       O  
-ATOM   8615  N   ARG B 448     -20.423  19.118   2.630  1.00 51.46           N  
-ANISOU 8615  N   ARG B 448     3838   7675   8041   2244  -2038    234       N  
-ATOM   8616  CA  ARG B 448     -21.133  19.700   1.499  1.00 57.94           C  
-ANISOU 8616  CA  ARG B 448     4469   8807   8738   2509  -1940    237       C  
-ATOM   8617  C   ARG B 448     -22.189  20.690   1.977  1.00 60.14           C  
-ANISOU 8617  C   ARG B 448     4686   9265   8901   2591  -1686    396       C  
-ATOM   8618  O   ARG B 448     -22.709  20.562   3.086  1.00 61.92           O  
-ANISOU 8618  O   ARG B 448     4944   9438   9146   2390  -1638    474       O  
-ATOM   8619  CB  ARG B 448     -21.787  18.598   0.664  1.00 59.76           C  
-ANISOU 8619  CB  ARG B 448     4491   9218   8998   2456  -2178    113       C  
-ATOM   8620  CG  ARG B 448     -20.803  17.621   0.047  1.00 64.11           C  
-ANISOU 8620  CG  ARG B 448     5126   9594   9640   2381  -2399    -75       C  
-ATOM   8621  CD  ARG B 448     -20.084  18.223  -1.154  1.00 67.36           C  
-ANISOU 8621  CD  ARG B 448     5622  10039   9932   2607  -2285   -163       C  
-ATOM   8622  NE  ARG B 448     -19.050  17.332  -1.679  1.00 70.77           N  
-ANISOU 8622  NE  ARG B 448     6134  10290  10466   2545  -2477   -351       N  
-ATOM   8623  CZ  ARG B 448     -18.364  17.548  -2.799  1.00 73.34           C  
-ANISOU 8623  CZ  ARG B 448     6507  10646  10714   2706  -2438   -468       C  
-ATOM   8624  NH1 ARG B 448     -18.601  18.625  -3.537  1.00 75.56           N  
-ANISOU 8624  NH1 ARG B 448     6778  11129  10801   2932  -2225   -405       N  
-ATOM   8625  NH2 ARG B 448     -17.439  16.680  -3.187  1.00 74.19           N  
-ANISOU 8625  NH2 ARG B 448     6669  10584  10937   2646  -2617   -647       N  
-ATOM   8626  N   MET B 449     -22.491  21.684   1.146  1.00 76.76           N  
-ANISOU 8626  N   MET B 449     6716  11572  10879   2884  -1515    443       N  
-ATOM   8627  CA  MET B 449     -23.633  22.556   1.389  1.00 79.53           C  
-ANISOU 8627  CA  MET B 449     6950  12139  11128   3009  -1301    578       C  
-ATOM   8628  C   MET B 449     -24.093  23.215   0.099  1.00 84.66           C  
-ANISOU 8628  C   MET B 449     7507  13045  11616   3287  -1210    578       C  
-ATOM   8629  O   MET B 449     -23.280  23.586  -0.740  1.00 84.98           O  
-ANISOU 8629  O   MET B 449     7692  13026  11569   3407  -1169    527       O  
-ATOM   8630  CB  MET B 449     -23.328  23.605   2.461  1.00 75.76           C  
-ANISOU 8630  CB  MET B 449     6673  11488  10625   3014  -1041    706       C  
-ATOM   8631  CG  MET B 449     -22.403  24.724   2.025  1.00 69.97           C  
-ANISOU 8631  CG  MET B 449     6115  10648   9821   3240   -860    739       C  
-ATOM   8632  SD  MET B 449     -22.521  26.172   3.100  1.00 67.14           S  
-ANISOU 8632  SD  MET B 449     5905  10194   9410   3331   -517    905       S  
-ATOM   8633  CE  MET B 449     -22.081  25.472   4.690  1.00 66.58           C  
-ANISOU 8633  CE  MET B 449     6015   9839   9444   2945   -591    894       C  
-ATOM   8634  N   ASP B 450     -25.406  23.349  -0.049  1.00 73.34           N  
-ANISOU 8634  N   ASP B 450     5833  11900  10132   3373  -1178    636       N  
-ATOM   8635  CA  ASP B 450     -26.014  23.845  -1.280  1.00 79.41           C  
-ANISOU 8635  CA  ASP B 450     6492  12944  10737   3621  -1132    637       C  
-ATOM   8636  C   ASP B 450     -25.380  25.117  -1.824  1.00 80.13           C  
-ANISOU 8636  C   ASP B 450     6791  12978  10675   3863   -908    707       C  
-ATOM   8637  O   ASP B 450     -24.893  25.958  -1.070  1.00 80.21           O  
-ANISOU 8637  O   ASP B 450     6983  12800  10692   3884   -706    803       O  
-ATOM   8638  CB  ASP B 450     -27.518  24.039  -1.090  1.00 82.93           C  
-ANISOU 8638  CB  ASP B 450     6656  13688  11164   3692  -1081    720       C  
-ATOM   8639  CG  ASP B 450     -28.320  22.870  -1.623  1.00 88.44           C  
-ANISOU 8639  CG  ASP B 450     7084  14613  11908   3577  -1343    607       C  
-ATOM   8640  OD1 ASP B 450     -27.890  22.284  -2.640  1.00 88.91           O  
-ANISOU 8640  OD1 ASP B 450     7167  14689  11925   3582  -1516    476       O  
-ATOM   8641  OD2 ASP B 450     -29.370  22.536  -1.030  1.00 91.05           O  
-ANISOU 8641  OD2 ASP B 450     7188  15101  12307   3464  -1365    638       O  
-ATOM   8642  N   ASN B 451     -25.398  25.244  -3.146  1.00 89.02           N  
-ANISOU 8642  N   ASN B 451     7889  14274  11662   4042   -950    660       N  
-ATOM   8643  CA  ASN B 451     -24.759  26.366  -3.820  1.00 89.35           C  
-ANISOU 8643  CA  ASN B 451     8122  14278  11550   4266   -764    724       C  
-ATOM   8644  C   ASN B 451     -25.491  27.669  -3.555  1.00 90.85           C  
-ANISOU 8644  C   ASN B 451     8305  14570  11643   4483   -511    908       C  
-ATOM   8645  O   ASN B 451     -24.949  28.751  -3.785  1.00 90.21           O  
-ANISOU 8645  O   ASN B 451     8417  14400  11459   4645   -314    998       O  
-ATOM   8646  CB  ASN B 451     -24.677  26.109  -5.326  1.00 92.28           C  
-ANISOU 8646  CB  ASN B 451     8439  14835  11788   4410   -889    631       C  
-ATOM   8647  CG  ASN B 451     -24.264  24.689  -5.652  1.00 90.67           C  
-ANISOU 8647  CG  ASN B 451     8176  14588  11687   4210  -1165    431       C  
-ATOM   8648  OD1 ASN B 451     -25.084  23.772  -5.626  1.00 92.06           O  
-ANISOU 8648  OD1 ASN B 451     8136  14911  11932   4102  -1353    362       O  
-ATOM   8649  ND2 ASN B 451     -22.988  24.498  -5.963  1.00 89.80           N  
-ANISOU 8649  ND2 ASN B 451     8251  14274  11596   4160  -1191    334       N  
-ATOM   8650  N   ILE B 452     -26.727  27.560  -3.081  1.00 87.13           N  
-ANISOU 8650  N   ILE B 452     7606  14287  11213   4486   -516    960       N  
-ATOM   8651  CA  ILE B 452     -27.515  28.735  -2.736  1.00 89.28           C  
-ANISOU 8651  CA  ILE B 452     7845  14659  11419   4694   -279   1123       C  
-ATOM   8652  C   ILE B 452     -26.686  29.717  -1.916  1.00 87.70           C  
-ANISOU 8652  C   ILE B 452     7925  14166  11232   4700    -33   1217       C  
-ATOM   8653  O   ILE B 452     -26.686  30.918  -2.182  1.00 90.76           O  
-ANISOU 8653  O   ILE B 452     8428  14554  11503   4928    174   1336       O  
-ATOM   8654  CB  ILE B 452     -28.786  28.366  -1.936  1.00 89.98           C  
-ANISOU 8654  CB  ILE B 452     7655  14921  11611   4619   -299   1148       C  
-ATOM   8655  CG1 ILE B 452     -29.779  27.591  -2.809  1.00 94.52           C  
-ANISOU 8655  CG1 ILE B 452     7924  15833  12158   4650   -518   1072       C  
-ATOM   8656  CG2 ILE B 452     -29.451  29.617  -1.391  1.00 91.63           C  
-ANISOU 8656  CG2 ILE B 452     7860  15177  11779   4822    -22   1306       C  
-ATOM   8657  CD1 ILE B 452     -29.350  26.178  -3.148  1.00 94.74           C  
-ANISOU 8657  CD1 ILE B 452     7905  15825  12265   4409   -807    900       C  
-ATOM   8658  N   TYR B 453     -25.973  29.197  -0.924  1.00 83.92           N  
-ANISOU 8658  N   TYR B 453     7555  13434  10896   4448    -68   1163       N  
-ATOM   8659  CA  TYR B 453     -25.202  30.036  -0.016  1.00 80.87           C  
-ANISOU 8659  CA  TYR B 453     7420  12767  10540   4421    146   1236       C  
-ATOM   8660  C   TYR B 453     -23.886  30.466  -0.647  1.00 78.80           C  
-ANISOU 8660  C   TYR B 453     7415  12319  10207   4456    187   1212       C  
-ATOM   8661  O   TYR B 453     -23.150  31.281  -0.091  1.00 76.99           O  
-ANISOU 8661  O   TYR B 453     7409  11863   9982   4454    369   1271       O  
-ATOM   8662  CB  TYR B 453     -24.953  29.292   1.295  1.00 77.73           C  
-ANISOU 8662  CB  TYR B 453     7028  12184  10320   4146     75   1191       C  
-ATOM   8663  CG  TYR B 453     -26.216  28.710   1.888  1.00 76.50           C  
-ANISOU 8663  CG  TYR B 453     6590  12228  10249   4077     15   1204       C  
-ATOM   8664  CD1 TYR B 453     -26.639  27.433   1.547  1.00 76.47           C  
-ANISOU 8664  CD1 TYR B 453     6371  12373  10313   3930   -255   1103       C  
-ATOM   8665  CD2 TYR B 453     -26.995  29.443   2.774  1.00 75.94           C  
-ANISOU 8665  CD2 TYR B 453     6470  12200  10182   4141    239   1307       C  
-ATOM   8666  CE1 TYR B 453     -27.794  26.897   2.078  1.00 76.71           C  
-ANISOU 8666  CE1 TYR B 453     6186  12580  10382   3793   -292   1107       C  
-ATOM   8667  CE2 TYR B 453     -28.152  28.914   3.309  1.00 76.32           C  
-ANISOU 8667  CE2 TYR B 453     6313  12431  10255   3999    213   1306       C  
-ATOM   8668  CZ  TYR B 453     -28.546  27.642   2.956  1.00 76.55           C  
-ANISOU 8668  CZ  TYR B 453     6149  12600  10335   3819    -53   1209       C  
-ATOM   8669  OH  TYR B 453     -29.696  27.109   3.483  1.00 77.60           O  
-ANISOU 8669  OH  TYR B 453     6071  12916  10498   3660    -72   1207       O  
-ATOM   8670  N   PHE B 454     -23.604  29.910  -1.819  1.00 77.45           N  
-ANISOU 8670  N   PHE B 454     7202  12254   9973   4486     20   1118       N  
-ATOM   8671  CA  PHE B 454     -22.400  30.243  -2.561  1.00 75.86           C  
-ANISOU 8671  CA  PHE B 454     7202  11920   9700   4529     53   1082       C  
-ATOM   8672  C   PHE B 454     -22.688  31.256  -3.670  1.00 81.00           C  
-ANISOU 8672  C   PHE B 454     7875  12744  10157   4833    188   1186       C  
-ATOM   8673  O   PHE B 454     -21.774  31.908  -4.171  1.00 81.06           O  
-ANISOU 8673  O   PHE B 454     8071  12637  10090   4912    298   1212       O  
-ATOM   8674  CB  PHE B 454     -21.773  28.980  -3.154  1.00 68.93           C  
-ANISOU 8674  CB  PHE B 454     6281  11028   8882   4375   -208    900       C  
-ATOM   8675  CG  PHE B 454     -21.058  28.120  -2.149  1.00 60.05           C  
-ANISOU 8675  CG  PHE B 454     5217   9653   7947   4089   -330    803       C  
-ATOM   8676  CD1 PHE B 454     -19.751  28.403  -1.783  1.00 55.97           C  
-ANISOU 8676  CD1 PHE B 454     4923   8860   7484   3996   -261    778       C  
-ATOM   8677  CD2 PHE B 454     -21.679  27.017  -1.588  1.00 56.17           C  
-ANISOU 8677  CD2 PHE B 454     4554   9205   7583   3914   -523    741       C  
-ATOM   8678  CE1 PHE B 454     -19.082  27.615  -0.863  1.00 52.29           C  
-ANISOU 8678  CE1 PHE B 454     4510   8164   7192   3749   -391    694       C  
-ATOM   8679  CE2 PHE B 454     -21.015  26.223  -0.669  1.00 52.29           C  
-ANISOU 8679  CE2 PHE B 454     4128   8476   7264   3665   -651    668       C  
-ATOM   8680  CZ  PHE B 454     -19.714  26.522  -0.307  1.00 50.77           C  
-ANISOU 8680  CZ  PHE B 454     4161   8008   7120   3590   -590    645       C  
-ATOM   8681  N   GLU B 455     -23.954  31.382  -4.059  1.00 83.35           N  
-ANISOU 8681  N   GLU B 455     7970  13320  10378   5007    174   1249       N  
-ATOM   8682  CA  GLU B 455     -24.340  32.350  -5.082  1.00 90.27           C  
-ANISOU 8682  CA  GLU B 455     8853  14374  11070   5321    288   1366       C  
-ATOM   8683  C   GLU B 455     -23.962  33.747  -4.605  1.00 89.23           C  
-ANISOU 8683  C   GLU B 455     8949  14052  10902   5440    580   1522       C  
-ATOM   8684  O   GLU B 455     -24.165  34.078  -3.440  1.00 90.32           O  
-ANISOU 8684  O   GLU B 455     9126  14057  11135   5361    705   1574       O  
-ATOM   8685  CB  GLU B 455     -25.840  32.263  -5.367  1.00 99.31           C  
-ANISOU 8685  CB  GLU B 455     9722  15844  12167   5478    223   1411       C  
-ATOM   8686  CG  GLU B 455     -26.260  32.883  -6.690  1.00112.98           C  
-ANISOU 8686  CG  GLU B 455    11407  17815  13705   5798    236   1491       C  
-ATOM   8687  CD  GLU B 455     -26.228  34.398  -6.663  1.00119.71           C  
-ANISOU 8687  CD  GLU B 455    12435  18587  14462   6046    513   1684       C  
-ATOM   8688  OE1 GLU B 455     -26.371  34.968  -5.562  1.00122.29           O  
-ANISOU 8688  OE1 GLU B 455    12832  18759  14875   6005    688   1761       O  
-ATOM   8689  OE2 GLU B 455     -26.059  35.017  -7.737  1.00122.99           O  
-ANISOU 8689  OE2 GLU B 455    12922  19090  14719   6285    557   1758       O  
-ATOM   8690  N   TYR B 456     -23.411  34.564  -5.498  1.00 84.02           N  
-ANISOU 8690  N   TYR B 456     8442  13376  10105   5631    692   1595       N  
-ATOM   8691  CA  TYR B 456     -22.836  35.847  -5.093  1.00 82.44           C  
-ANISOU 8691  CA  TYR B 456     8489  12950   9884   5714    963   1729       C  
-ATOM   8692  C   TYR B 456     -23.801  36.766  -4.348  1.00 83.84           C  
-ANISOU 8692  C   TYR B 456     8646  13143  10066   5860   1153   1876       C  
-ATOM   8693  O   TYR B 456     -23.510  37.204  -3.236  1.00 83.80           O  
-ANISOU 8693  O   TYR B 456     8773  12911  10157   5749   1304   1905       O  
-ATOM   8694  CB  TYR B 456     -22.228  36.595  -6.282  1.00 82.47           C  
-ANISOU 8694  CB  TYR B 456     8636  12966   9733   5926   1054   1803       C  
-ATOM   8695  CG  TYR B 456     -21.586  37.903  -5.872  1.00 80.26           C  
-ANISOU 8695  CG  TYR B 456     8618  12434   9445   5996   1335   1937       C  
-ATOM   8696  CD1 TYR B 456     -20.378  37.916  -5.192  1.00 78.90           C  
-ANISOU 8696  CD1 TYR B 456     8632  11967   9380   5766   1399   1876       C  
-ATOM   8697  CD2 TYR B 456     -22.194  39.122  -6.149  1.00 79.75           C  
-ANISOU 8697  CD2 TYR B 456     8609  12420   9274   6293   1530   2123       C  
-ATOM   8698  CE1 TYR B 456     -19.786  39.103  -4.804  1.00 77.05           C  
-ANISOU 8698  CE1 TYR B 456     8631  11498   9148   5815   1652   1989       C  
-ATOM   8699  CE2 TYR B 456     -21.606  40.318  -5.765  1.00 77.68           C  
-ANISOU 8699  CE2 TYR B 456     8593  11906   9014   6352   1791   2242       C  
-ATOM   8700  CZ  TYR B 456     -20.402  40.299  -5.089  1.00 76.57           C  
-ANISOU 8700  CZ  TYR B 456     8633  11477   8982   6104   1852   2170       C  
-ATOM   8701  OH  TYR B 456     -19.799  41.472  -4.695  1.00 75.91           O  
-ANISOU 8701  OH  TYR B 456     8792  11140   8911   6146   2107   2276       O  
-ATOM   8702  N   SER B 457     -24.934  37.070  -4.974  1.00 95.54           N  
-ANISOU 8702  N   SER B 457     9959  14894  11447   6119   1146   1962       N  
-ATOM   8703  CA  SER B 457     -25.921  37.972  -4.388  1.00 95.86           C  
-ANISOU 8703  CA  SER B 457     9956  14975  11491   6302   1327   2100       C  
-ATOM   8704  C   SER B 457     -26.298  37.535  -2.978  1.00 92.57           C  
-ANISOU 8704  C   SER B 457     9458  14475  11238   6084   1340   2043       C  
-ATOM   8705  O   SER B 457     -26.300  38.340  -2.045  1.00 92.90           O  
-ANISOU 8705  O   SER B 457     9626  14338  11332   6098   1555   2118       O  
-ATOM   8706  CB  SER B 457     -27.168  38.044  -5.270  1.00 99.13           C  
-ANISOU 8706  CB  SER B 457    10128  15738  11798   6582   1245   2164       C  
-ATOM   8707  OG  SER B 457     -28.147  38.892  -4.697  1.00101.11           O  
-ANISOU 8707  OG  SER B 457    10316  16035  12068   6771   1417   2287       O  
-ATOM   8708  N   HIS B 458     -26.615  36.254  -2.833  1.00 89.47           N  
-ANISOU 8708  N   HIS B 458     8857  14209  10928   5886   1112   1909       N  
-ATOM   8709  CA  HIS B 458     -26.930  35.692  -1.530  1.00 85.96           C  
-ANISOU 8709  CA  HIS B 458     8324  13694  10643   5661   1102   1850       C  
-ATOM   8710  C   HIS B 458     -25.732  35.822  -0.593  1.00 81.73           C  
-ANISOU 8710  C   HIS B 458     8052  12805  10198   5443   1199   1817       C  
-ATOM   8711  O   HIS B 458     -25.867  36.287   0.537  1.00 79.85           O  
-ANISOU 8711  O   HIS B 458     7878  12425  10035   5397   1367   1858       O  
-ATOM   8712  CB  HIS B 458     -27.344  34.226  -1.665  1.00 86.26           C  
-ANISOU 8712  CB  HIS B 458     8108  13912  10755   5474    820   1709       C  
-ATOM   8713  CG  HIS B 458     -27.854  33.623  -0.392  1.00 87.36           C  
-ANISOU 8713  CG  HIS B 458     8111  14026  11054   5268    807   1665       C  
-ATOM   8714  ND1 HIS B 458     -29.184  33.326  -0.189  1.00 90.05           N  
-ANISOU 8714  ND1 HIS B 458     8150  14631  11435   5315    772   1674       N  
-ATOM   8715  CD2 HIS B 458     -27.211  33.263   0.744  1.00 86.81           C  
-ANISOU 8715  CD2 HIS B 458     8158  13711  11116   5017    827   1615       C  
-ATOM   8716  CE1 HIS B 458     -29.339  32.808   1.017  1.00 89.57           C  
-ANISOU 8716  CE1 HIS B 458     8025  14488  11521   5096    784   1633       C  
-ATOM   8717  NE2 HIS B 458     -28.157  32.758   1.603  1.00 88.40           N  
-ANISOU 8717  NE2 HIS B 458     8133  14029  11426   4920    811   1600       N  
-ATOM   8718  N   ALA B 459     -24.560  35.416  -1.069  1.00 70.03           N  
-ANISOU 8718  N   ALA B 459     6713  11187   8708   5315   1094   1736       N  
-ATOM   8719  CA  ALA B 459     -23.344  35.464  -0.260  1.00 67.98           C  
-ANISOU 8719  CA  ALA B 459     6686  10604   8540   5101   1154   1690       C  
-ATOM   8720  C   ALA B 459     -22.994  36.883   0.188  1.00 69.14           C  
-ANISOU 8720  C   ALA B 459     7069  10550   8651   5221   1446   1815       C  
-ATOM   8721  O   ALA B 459     -22.604  37.105   1.335  1.00 67.72           O  
-ANISOU 8721  O   ALA B 459     7016  10148   8567   5079   1553   1807       O  
-ATOM   8722  CB  ALA B 459     -22.184  34.848  -1.014  1.00 67.44           C  
-ANISOU 8722  CB  ALA B 459     6703  10457   8464   4983    997   1580       C  
-ATOM   8723  N   PHE B 460     -23.123  37.840  -0.725  1.00 69.71           N  
-ANISOU 8723  N   PHE B 460     7205  10695   8587   5486   1572   1929       N  
-ATOM   8724  CA  PHE B 460     -22.849  39.236  -0.411  1.00 71.80           C  
-ANISOU 8724  CA  PHE B 460     7695  10769   8815   5625   1853   2057       C  
-ATOM   8725  C   PHE B 460     -23.795  39.705   0.676  1.00 73.23           C  
-ANISOU 8725  C   PHE B 460     7824  10945   9055   5678   2008   2115       C  
-ATOM   8726  O   PHE B 460     -23.420  40.493   1.542  1.00 72.47           O  
-ANISOU 8726  O   PHE B 460     7920  10612   9003   5648   2212   2154       O  
-ATOM   8727  CB  PHE B 460     -23.011  40.116  -1.653  1.00 76.82           C  
-ANISOU 8727  CB  PHE B 460     8376  11518   9293   5935   1944   2184       C  
-ATOM   8728  CG  PHE B 460     -22.655  41.553  -1.422  1.00 80.81           C  
-ANISOU 8728  CG  PHE B 460     9131  11806   9768   6081   2232   2318       C  
-ATOM   8729  CD1 PHE B 460     -21.335  41.966  -1.467  1.00 82.37           C  
-ANISOU 8729  CD1 PHE B 460     9572  11749   9976   5978   2322   2309       C  
-ATOM   8730  CD2 PHE B 460     -23.637  42.489  -1.152  1.00 82.76           C  
-ANISOU 8730  CD2 PHE B 460     9360  12098   9987   6322   2414   2447       C  
-ATOM   8731  CE1 PHE B 460     -21.002  43.284  -1.247  1.00 84.33           C  
-ANISOU 8731  CE1 PHE B 460    10051  11785  10207   6101   2589   2427       C  
-ATOM   8732  CE2 PHE B 460     -23.312  43.809  -0.933  1.00 83.25           C  
-ANISOU 8732  CE2 PHE B 460     9661  11939  10030   6459   2681   2565       C  
-ATOM   8733  CZ  PHE B 460     -21.992  44.208  -0.979  1.00 84.15           C  
-ANISOU 8733  CZ  PHE B 460    10026  11793  10155   6343   2770   2556       C  
-ATOM   8734  N   GLN B 461     -25.026  39.208   0.623  1.00 71.88           N  
-ANISOU 8734  N   GLN B 461     7383  11042   8888   5755   1914   2112       N  
-ATOM   8735  CA  GLN B 461     -26.045  39.571   1.598  1.00 75.79           C  
-ANISOU 8735  CA  GLN B 461     7777  11578   9442   5818   2060   2155       C  
-ATOM   8736  C   GLN B 461     -25.658  39.115   3.000  1.00 69.98           C  
-ANISOU 8736  C   GLN B 461     7100  10643   8845   5536   2083   2064       C  
-ATOM   8737  O   GLN B 461     -25.691  39.895   3.947  1.00 69.04           O  
-ANISOU 8737  O   GLN B 461     7112  10358   8761   5554   2307   2103       O  
-ATOM   8738  CB  GLN B 461     -27.395  38.970   1.210  1.00 84.85           C  
-ANISOU 8738  CB  GLN B 461     8582  13078  10580   5927   1925   2148       C  
-ATOM   8739  CG  GLN B 461     -28.491  39.275   2.208  1.00 98.32           C  
-ANISOU 8739  CG  GLN B 461    10143  14856  12357   5987   2080   2178       C  
-ATOM   8740  CD  GLN B 461     -28.699  40.764   2.379  1.00107.16           C  
-ANISOU 8740  CD  GLN B 461    11425  15865  13426   6249   2371   2311       C  
-ATOM   8741  OE1 GLN B 461     -29.003  41.241   3.474  1.00111.21           O  
-ANISOU 8741  OE1 GLN B 461    11978  16269  14007   6236   2571   2317       O  
-ATOM   8742  NE2 GLN B 461     -28.531  41.512   1.291  1.00110.60           N  
-ANISOU 8742  NE2 GLN B 461    11960  16323  13739   6494   2404   2415       N  
-ATOM   8743  N   ALA B 462     -25.290  37.844   3.116  1.00 85.25           N  
-ANISOU 8743  N   ALA B 462     8943  12593  10857   5285   1847   1941       N  
-ATOM   8744  CA  ALA B 462     -24.877  37.264   4.388  1.00 79.93           C  
-ANISOU 8744  CA  ALA B 462     8315  11739  10317   5015   1829   1853       C  
-ATOM   8745  C   ALA B 462     -23.679  37.996   4.983  1.00 77.21           C  
-ANISOU 8745  C   ALA B 462     8292  11056   9990   4931   1982   1857       C  
-ATOM   8746  O   ALA B 462     -23.605  38.199   6.193  1.00 74.44           O  
-ANISOU 8746  O   ALA B 462     8028  10543   9712   4828   2111   1837       O  
-ATOM   8747  CB  ALA B 462     -24.558  35.788   4.214  1.00 75.47           C  
-ANISOU 8747  CB  ALA B 462     7618  11228   9829   4783   1525   1730       C  
-ATOM   8748  N   VAL B 463     -22.739  38.389   4.131  1.00 62.27           N  
-ANISOU 8748  N   VAL B 463     6567   9064   8028   4971   1974   1875       N  
-ATOM   8749  CA  VAL B 463     -21.533  39.064   4.595  1.00 62.65           C  
-ANISOU 8749  CA  VAL B 463     6903   8802   8099   4879   2105   1871       C  
-ATOM   8750  C   VAL B 463     -21.833  40.445   5.171  1.00 69.61           C  
-ANISOU 8750  C   VAL B 463     7942   9558   8948   5040   2416   1974       C  
-ATOM   8751  O   VAL B 463     -21.521  40.721   6.325  1.00 69.61           O  
-ANISOU 8751  O   VAL B 463     8079   9352   9019   4920   2537   1940       O  
-ATOM   8752  CB  VAL B 463     -20.490  39.185   3.476  1.00 57.41           C  
-ANISOU 8752  CB  VAL B 463     6355   8086   7372   4893   2043   1865       C  
-ATOM   8753  CG1 VAL B 463     -19.394  40.161   3.876  1.00 53.37           C  
-ANISOU 8753  CG1 VAL B 463     6128   7276   6875   4849   2234   1888       C  
-ATOM   8754  CG2 VAL B 463     -19.916  37.816   3.156  1.00 53.34           C  
-ANISOU 8754  CG2 VAL B 463     5737   7612   6919   4684   1752   1728       C  
-ATOM   8755  N   THR B 464     -22.436  41.307   4.361  1.00 89.09           N  
-ANISOU 8755  N   THR B 464    10395  12145  11309   5321   2541   2095       N  
-ATOM   8756  CA  THR B 464     -22.799  42.647   4.803  1.00 98.14           C  
-ANISOU 8756  CA  THR B 464    11685  13176  12426   5510   2835   2199       C  
-ATOM   8757  C   THR B 464     -23.781  42.566   5.969  1.00103.57           C  
-ANISOU 8757  C   THR B 464    12258  13913  13180   5494   2931   2173       C  
-ATOM   8758  O   THR B 464     -23.825  43.452   6.825  1.00104.43           O  
-ANISOU 8758  O   THR B 464    12524  13847  13308   5533   3171   2196       O  
-ATOM   8759  CB  THR B 464     -23.408  43.474   3.650  1.00101.08           C  
-ANISOU 8759  CB  THR B 464    12027  13701  12677   5846   2921   2342       C  
-ATOM   8760  OG1 THR B 464     -24.517  42.765   3.080  1.00101.99           O  
-ANISOU 8760  OG1 THR B 464    11841  14149  12761   5954   2758   2343       O  
-ATOM   8761  CG2 THR B 464     -22.367  43.726   2.564  1.00100.20           C  
-ANISOU 8761  CG2 THR B 464    12066  13513  12493   5872   2886   2374       C  
-ATOM   8762  N   GLU B 465     -24.561  41.490   5.997  1.00106.42           N  
-ANISOU 8762  N   GLU B 465    12342  14515  13577   5431   2752   2116       N  
-ATOM   8763  CA  GLU B 465     -25.509  41.247   7.078  1.00111.34           C  
-ANISOU 8763  CA  GLU B 465    12814  15221  14268   5390   2835   2076       C  
-ATOM   8764  C   GLU B 465     -24.774  40.811   8.338  1.00108.22           C  
-ANISOU 8764  C   GLU B 465    12549  14600  13968   5105   2844   1966       C  
-ATOM   8765  O   GLU B 465     -25.230  41.058   9.453  1.00108.80           O  
-ANISOU 8765  O   GLU B 465    12645  14629  14066   5053   3019   1942       O  
-ATOM   8766  CB  GLU B 465     -26.516  40.175   6.660  1.00116.39           C  
-ANISOU 8766  CB  GLU B 465    13102  16195  14926   5391   2631   2046       C  
-ATOM   8767  CG  GLU B 465     -27.599  39.883   7.678  1.00123.53           C  
-ANISOU 8767  CG  GLU B 465    13798  17238  15900   5353   2727   2006       C  
-ATOM   8768  CD  GLU B 465     -28.686  38.985   7.117  1.00129.60           C  
-ANISOU 8768  CD  GLU B 465    14197  18361  16683   5390   2544   1992       C  
-ATOM   8769  OE1 GLU B 465     -29.523  38.491   7.904  1.00137.07           O  
-ANISOU 8769  OE1 GLU B 465    14985  19440  17655   5239   2563   1956       O  
-ATOM   8770  OE2 GLU B 465     -28.704  38.776   5.884  1.00130.28           O  
-ANISOU 8770  OE2 GLU B 465    14205  18591  16704   5498   2367   2025       O  
-ATOM   8771  N   PHE B 466     -23.632  40.160   8.151  1.00103.15           N  
-ANISOU 8771  N   PHE B 466    12008  13823  13363   4904   2651   1900       N  
-ATOM   8772  CA  PHE B 466     -22.816  39.703   9.267  1.00 96.95           C  
-ANISOU 8772  CA  PHE B 466    11375  12812  12649   4608   2611   1804       C  
-ATOM   8773  C   PHE B 466     -22.063  40.875   9.876  1.00 96.78           C  
-ANISOU 8773  C   PHE B 466    11659  12495  12618   4627   2854   1816       C  
-ATOM   8774  O   PHE B 466     -22.390  41.334  10.967  1.00 98.77           O  
-ANISOU 8774  O   PHE B 466    12023  12661  12844   4549   3035   1811       O  
-ATOM   8775  CB  PHE B 466     -21.832  38.629   8.800  1.00 88.48           C  
-ANISOU 8775  CB  PHE B 466    10291  11691  11635   4417   2314   1726       C  
-ATOM   8776  CG  PHE B 466     -20.949  38.089   9.892  1.00 77.91           C  
-ANISOU 8776  CG  PHE B 466     9135  10125  10342   4068   2218   1643       C  
-ATOM   8777  CD1 PHE B 466     -21.383  37.056  10.703  1.00 74.70           C  
-ANISOU 8777  CD1 PHE B 466     8651   9784   9946   3800   2072   1600       C  
-ATOM   8778  CD2 PHE B 466     -19.681  38.606  10.096  1.00 73.29           C  
-ANISOU 8778  CD2 PHE B 466     8798   9262   9785   4004   2267   1611       C  
-ATOM   8779  CE1 PHE B 466     -20.574  36.554  11.704  1.00 71.57           C  
-ANISOU 8779  CE1 PHE B 466     8434   9177   9581   3487   1968   1536       C  
-ATOM   8780  CE2 PHE B 466     -18.864  38.108  11.094  1.00 69.47           C  
-ANISOU 8780  CE2 PHE B 466     8476   8578   9342   3692   2159   1536       C  
-ATOM   8781  CZ  PHE B 466     -19.311  37.080  11.900  1.00 69.23           C  
-ANISOU 8781  CZ  PHE B 466     8377   8613   9314   3439   2004   1502       C  
-ATOM   8782  N   TYR B 467     -21.056  41.359   9.161  1.00 87.66           N  
-ANISOU 8782  N   TYR B 467    10669  11193  11443   4663   2846   1840       N  
-ATOM   8783  CA  TYR B 467     -20.275  42.491   9.630  1.00 85.69           C  
-ANISOU 8783  CA  TYR B 467    10714  10660  11184   4662   3064   1853       C  
-ATOM   8784  C   TYR B 467     -21.157  43.722   9.756  1.00 90.93           C  
-ANISOU 8784  C   TYR B 467    11429  11339  11783   4911   3357   1952       C  
-ATOM   8785  O   TYR B 467     -22.046  43.948   8.936  1.00 93.56           O  
-ANISOU 8785  O   TYR B 467    11611  11885  12053   5140   3375   2048       O  
-ATOM   8786  CB  TYR B 467     -19.089  42.752   8.700  1.00 78.66           C  
-ANISOU 8786  CB  TYR B 467     9961   9653  10272   4638   2999   1871       C  
-ATOM   8787  CG  TYR B 467     -18.176  41.555   8.573  1.00 68.58           C  
-ANISOU 8787  CG  TYR B 467     8633   8354   9069   4399   2714   1762       C  
-ATOM   8788  CD1 TYR B 467     -17.291  41.226   9.593  1.00 64.16           C  
-ANISOU 8788  CD1 TYR B 467     8205   7567   8604   4162   2659   1656       C  
-ATOM   8789  CD2 TYR B 467     -18.205  40.744   7.443  1.00 63.59           C  
-ANISOU 8789  CD2 TYR B 467     7826   7924   8413   4417   2493   1758       C  
-ATOM   8790  CE1 TYR B 467     -16.459  40.128   9.492  1.00 59.32           C  
-ANISOU 8790  CE1 TYR B 467     7544   6923   8071   3958   2387   1559       C  
-ATOM   8791  CE2 TYR B 467     -17.376  39.644   7.335  1.00 59.03           C  
-ANISOU 8791  CE2 TYR B 467     7203   7316   7910   4206   2236   1648       C  
-ATOM   8792  CZ  TYR B 467     -16.507  39.342   8.365  1.00 57.63           C  
-ANISOU 8792  CZ  TYR B 467     7151   6906   7838   3981   2181   1553       C  
-ATOM   8793  OH  TYR B 467     -15.676  38.253   8.272  1.00 55.86           O  
-ANISOU 8793  OH  TYR B 467     6882   6641   7701   3784   1915   1447       O  
-ATOM   8794  N   ALA B 468     -20.916  44.500  10.805  1.00 92.11           N  
-ANISOU 8794  N   ALA B 468    11791  11258  11949   4869   3581   1918       N  
-ATOM   8795  CA  ALA B 468     -21.701  45.692  11.078  1.00 97.30           C  
-ANISOU 8795  CA  ALA B 468    12522  11890  12558   5093   3876   1993       C  
-ATOM   8796  C   ALA B 468     -21.096  46.450  12.250  1.00 98.59           C  
-ANISOU 8796  C   ALA B 468    12969  11749  12743   4981   4092   1919       C  
-ATOM   8797  O   ALA B 468     -20.834  45.869  13.305  1.00100.46           O  
-ANISOU 8797  O   ALA B 468    13262  11917  12993   4706   4033   1816       O  
-ATOM   8798  CB  ALA B 468     -23.138  45.317  11.375  1.00102.71           C  
-ANISOU 8798  CB  ALA B 468    12947  12844  13236   5199   3909   1996       C  
-ATOM   8799  N   LYS B 469     -20.877  47.747  12.061  1.00107.90           N  
-ANISOU 8799  N   LYS B 469    14358  12748  13890   5136   4315   1993       N  
-ATOM   8800  CA  LYS B 469     -20.268  48.574  13.094  1.00107.62           C  
-ANISOU 8800  CA  LYS B 469    14613  12407  13871   5037   4530   1919       C  
-ATOM   8801  C   LYS B 469     -21.242  48.857  14.237  1.00107.59           C  
-ANISOU 8801  C   LYS B 469    14605  12429  13845   5074   4746   1860       C  
-ATOM   8802  O   LYS B 469     -21.297  48.116  15.221  1.00104.69           O  
-ANISOU 8802  O   LYS B 469    14232  12095  13449   4788   4654   1778       O  
-ATOM   8803  CB  LYS B 469     -19.754  49.874  12.494  1.00107.32           C  
-ANISOU 8803  CB  LYS B 469    14797  12166  13813   5192   4709   2017       C  
-ATOM   8804  N   GLY B 482     -13.258  46.904   7.903  1.00131.89           N  
-ANISOU 8804  N   GLY B 482    17830  15208  17073   4410   3606   1881       N  
-ATOM   8805  CA  GLY B 482     -14.541  47.600   7.895  1.00132.46           C  
-ANISOU 8805  CA  GLY B 482    17897  15367  17065   4666   3787   2003       C  
-ATOM   8806  C   GLY B 482     -15.297  47.306   6.603  1.00133.86           C  
-ANISOU 8806  C   GLY B 482    17884  15826  17149   4885   3699   2111       C  
-ATOM   8807  O   GLY B 482     -16.053  46.338   6.523  1.00133.50           O  
-ANISOU 8807  O   GLY B 482    17621  16013  17091   4887   3514   2088       O  
-ATOM   8808  N   ILE B 483     -15.096  48.149   5.595  1.00131.93           N  
-ANISOU 8808  N   ILE B 483    17729  15560  16840   5071   3836   2225       N  
-ATOM   8809  CA  ILE B 483     -15.595  47.861   4.256  1.00132.91           C  
-ANISOU 8809  CA  ILE B 483    17697  15939  16864   5269   3738   2316       C  
-ATOM   8810  C   ILE B 483     -14.681  46.823   3.621  1.00133.18           C  
-ANISOU 8810  C   ILE B 483    17630  16049  16923   5088   3498   2217       C  
-ATOM   8811  O   ILE B 483     -13.765  47.155   2.866  1.00134.16           O  
-ANISOU 8811  O   ILE B 483    17845  16092  17036   5089   3544   2232       O  
-ATOM   8812  CB  ILE B 483     -15.650  49.124   3.375  1.00131.70           C  
-ANISOU 8812  CB  ILE B 483    17690  15722  16627   5544   3970   2478       C  
-ATOM   8813  CG1 ILE B 483     -16.708  50.098   3.901  1.00132.72           C  
-ANISOU 8813  CG1 ILE B 483    17891  15805  16732   5767   4193   2579       C  
-ATOM   8814  CG2 ILE B 483     -15.958  48.756   1.930  1.00132.11           C  
-ANISOU 8814  CG2 ILE B 483    17595  16031  16569   5728   3848   2555       C  
-ATOM   8815  CD1 ILE B 483     -18.133  49.601   3.748  1.00130.32           C  
-ANISOU 8815  CD1 ILE B 483    17347  15798  16371   5944   4089   2624       C  
-ATOM   8816  N   VAL B 484     -14.924  45.561   3.955  1.00130.08           N  
-ANISOU 8816  N   VAL B 484    17049  15802  16573   4932   3250   2108       N  
-ATOM   8817  CA  VAL B 484     -14.081  44.472   3.484  1.00129.18           C  
-ANISOU 8817  CA  VAL B 484    16833  15747  16503   4748   3006   1990       C  
-ATOM   8818  C   VAL B 484     -14.501  44.018   2.087  1.00128.78           C  
-ANISOU 8818  C   VAL B 484    16623  15963  16346   4915   2883   2037       C  
-ATOM   8819  O   VAL B 484     -14.907  42.876   1.879  1.00126.73           O  
-ANISOU 8819  O   VAL B 484    16165  15899  16089   4857   2648   1963       O  
-ATOM   8820  CB  VAL B 484     -14.080  43.283   4.483  1.00128.77           C  
-ANISOU 8820  CB  VAL B 484    16668  15702  16555   4502   2787   1846       C  
-ATOM   8821  CG1 VAL B 484     -15.491  42.738   4.687  1.00129.98           C  
-ANISOU 8821  CG1 VAL B 484    16635  16079  16674   4597   2706   1875       C  
-ATOM   8822  CG2 VAL B 484     -13.120  42.192   4.028  1.00129.47           C  
-ANISOU 8822  CG2 VAL B 484    16666  15818  16707   4316   2538   1716       C  
-ATOM   8823  N   ASN B 485     -14.408  44.931   1.127  1.00159.49           N  
-ANISOU 8823  N   ASN B 485    20608  19851  20140   5129   3046   2158       N  
-ATOM   8824  CA  ASN B 485     -14.708  44.597  -0.258  1.00158.49           C  
-ANISOU 8824  CA  ASN B 485    20357  19964  19897   5304   2946   2204       C  
-ATOM   8825  C   ASN B 485     -13.612  43.716  -0.847  1.00152.53           C  
-ANISOU 8825  C   ASN B 485    19549  19222  19183   5130   2765   2072       C  
-ATOM   8826  O   ASN B 485     -12.466  44.147  -0.995  1.00151.38           O  
-ANISOU 8826  O   ASN B 485    19543  18893  19083   5053   2862   2051       O  
-ATOM   8827  CB  ASN B 485     -14.878  45.863  -1.097  1.00168.39           C  
-ANISOU 8827  CB  ASN B 485    21749  21195  21038   5597   3183   2380       C  
-ATOM   8828  CG  ASN B 485     -15.395  45.571  -2.491  1.00177.26           C  
-ANISOU 8828  CG  ASN B 485    22738  22592  22019   5822   3083   2443       C  
-ATOM   8829  OD1 ASN B 485     -14.622  45.433  -3.439  1.00182.76           O  
-ANISOU 8829  OD1 ASN B 485    23457  23308  22676   5831   3052   2424       O  
-ATOM   8830  ND2 ASN B 485     -16.712  45.463  -2.619  1.00183.88           N  
-ANISOU 8830  ND2 ASN B 485    23430  23653  22784   6009   3031   2509       N  
-ATOM   8831  N   LEU B 486     -13.969  42.478  -1.177  1.00108.05           N  
-ANISOU 8831  N   LEU B 486    13709  13802  13543   5071   2505   1975       N  
-ATOM   8832  CA  LEU B 486     -12.996  41.505  -1.657  1.00100.78           C  
-ANISOU 8832  CA  LEU B 486    12718  12896  12677   4901   2311   1826       C  
-ATOM   8833  C   LEU B 486     -13.331  40.991  -3.048  1.00100.23           C  
-ANISOU 8833  C   LEU B 486    12512  13087  12483   5063   2186   1827       C  
-ATOM   8834  O   LEU B 486     -14.215  41.516  -3.726  1.00104.73           O  
-ANISOU 8834  O   LEU B 486    13058  13817  12916   5323   2266   1959       O  
-ATOM   8835  CB  LEU B 486     -12.906  40.323  -0.690  1.00 93.34           C  
-ANISOU 8835  CB  LEU B 486    11666  11928  11871   4636   2085   1668       C  
-ATOM   8836  CG  LEU B 486     -12.551  40.623   0.766  1.00 87.68           C  
-ANISOU 8836  CG  LEU B 486    11068  10966  11280   4453   2163   1640       C  
-ATOM   8837  CD1 LEU B 486     -12.414  39.328   1.539  1.00 80.82           C  
-ANISOU 8837  CD1 LEU B 486    10082  10089  10538   4212   1909   1486       C  
-ATOM   8838  CD2 LEU B 486     -11.273  41.442   0.860  1.00 81.82           C  
-ANISOU 8838  CD2 LEU B 486    10516   9976  10594   4381   2328   1635       C  
-ATOM   8839  N   GLU B 487     -12.616  39.951  -3.462  1.00106.37           N  
-ANISOU 8839  N   GLU B 487    13197  13906  13314   4916   1984   1671       N  
-ATOM   8840  CA  GLU B 487     -12.841  39.329  -4.756  1.00104.03           C  
-ANISOU 8840  CA  GLU B 487    12767  13852  12909   5046   1844   1635       C  
-ATOM   8841  C   GLU B 487     -14.219  38.699  -4.849  1.00100.33           C  
-ANISOU 8841  C   GLU B 487    12111  13636  12374   5136   1691   1642       C  
-ATOM   8842  O   GLU B 487     -14.839  38.384  -3.838  1.00 97.13           O  
-ANISOU 8842  O   GLU B 487    11646  13213  12046   5029   1635   1625       O  
-ATOM   8843  CB  GLU B 487     -11.764  38.286  -5.042  1.00103.31           C  
-ANISOU 8843  CB  GLU B 487    12612  13727  12914   4852   1657   1442       C  
-ATOM   8844  CG  GLU B 487     -10.457  38.893  -5.505  1.00105.78           C  
-ANISOU 8844  CG  GLU B 487    13062  13879  13249   4843   1806   1439       C  
-ATOM   8845  CD  GLU B 487     -10.637  39.765  -6.732  1.00108.40           C  
-ANISOU 8845  CD  GLU B 487    13460  14322  13406   5131   1981   1584       C  
-ATOM   8846  OE1 GLU B 487      -9.910  40.772  -6.856  1.00108.50           O  
-ANISOU 8846  OE1 GLU B 487    13639  14166  13421   5178   2210   1667       O  
-ATOM   8847  OE2 GLU B 487     -11.509  39.447  -7.571  1.00110.13           O  
-ANISOU 8847  OE2 GLU B 487    13564  14794  13487   5314   1890   1614       O  
-ATOM   8848  N   LYS B 488     -14.692  38.517  -6.076  1.00104.71           N  
-ANISOU 8848  N   LYS B 488    12567  14432  12787   5337   1626   1665       N  
-ATOM   8849  CA  LYS B 488     -16.021  37.968  -6.316  1.00100.54           C  
-ANISOU 8849  CA  LYS B 488    11842  14170  12188   5448   1480   1672       C  
-ATOM   8850  C   LYS B 488     -16.236  36.615  -5.630  1.00 96.55           C  
-ANISOU 8850  C   LYS B 488    11177  13693  11816   5203   1231   1504       C  
-ATOM   8851  O   LYS B 488     -17.215  36.436  -4.905  1.00 94.07           O  
-ANISOU 8851  O   LYS B 488    10765  13442  11537   5183   1195   1530       O  
-ATOM   8852  CB  LYS B 488     -16.282  37.840  -7.821  1.00100.37           C  
-ANISOU 8852  CB  LYS B 488    11736  14401  12000   5678   1413   1687       C  
-ATOM   8853  CG  LYS B 488     -17.682  38.245  -8.254  1.00103.13           C  
-ANISOU 8853  CG  LYS B 488    11977  14998  12211   5951   1430   1823       C  
-ATOM   8854  CD  LYS B 488     -17.846  39.754  -8.221  1.00101.40           C  
-ANISOU 8854  CD  LYS B 488    11930  14681  11916   6176   1713   2038       C  
-ATOM   8855  CE  LYS B 488     -19.115  40.188  -8.934  1.00 99.07           C  
-ANISOU 8855  CE  LYS B 488    11526  14650  11467   6501   1720   2177       C  
-ATOM   8856  NZ  LYS B 488     -19.246  41.671  -8.973  1.00 95.13           N  
-ANISOU 8856  NZ  LYS B 488    11208  14039  10898   6746   1996   2390       N  
-ATOM   8857  N   PRO B 489     -15.321  35.657  -5.855  1.00 90.84           N  
-ANISOU 8857  N   PRO B 489    10425  12917  11174   5024   1062   1330       N  
-ATOM   8858  CA  PRO B 489     -15.538  34.293  -5.359  1.00 88.60           C  
-ANISOU 8858  CA  PRO B 489     9987  12663  11013   4815    806   1168       C  
-ATOM   8859  C   PRO B 489     -15.125  34.063  -3.901  1.00 84.43           C  
-ANISOU 8859  C   PRO B 489     9522  11891  10667   4560    794   1122       C  
-ATOM   8860  O   PRO B 489     -15.647  33.136  -3.283  1.00 82.83           O  
-ANISOU 8860  O   PRO B 489     9196  11718  10558   4423    622   1046       O  
-ATOM   8861  CB  PRO B 489     -14.675  33.451  -6.297  1.00 89.13           C  
-ANISOU 8861  CB  PRO B 489    10012  12765  11090   4765    645   1004       C  
-ATOM   8862  CG  PRO B 489     -13.540  34.351  -6.637  1.00 91.46           C  
-ANISOU 8862  CG  PRO B 489    10485  12907  11360   4811    838   1052       C  
-ATOM   8863  CD  PRO B 489     -14.095  35.754  -6.668  1.00 90.62           C  
-ANISOU 8863  CD  PRO B 489    10489  12815  11128   5028   1095   1272       C  
-ATOM   8864  N   VAL B 490     -14.215  34.868  -3.359  1.00 75.86           N  
-ANISOU 8864  N   VAL B 490     8621  10570   9632   4498    966   1166       N  
-ATOM   8865  CA  VAL B 490     -13.809  34.685  -1.968  1.00 70.01           C  
-ANISOU 8865  CA  VAL B 490     7945   9602   9054   4269    951   1122       C  
-ATOM   8866  C   VAL B 490     -14.960  35.068  -1.046  1.00 69.29           C  
-ANISOU 8866  C   VAL B 490     7831   9542   8955   4309   1039   1233       C  
-ATOM   8867  O   VAL B 490     -15.176  34.447  -0.005  1.00 68.57           O  
-ANISOU 8867  O   VAL B 490     7695   9378   8982   4141    937   1182       O  
-ATOM   8868  CB  VAL B 490     -12.553  35.501  -1.603  1.00 68.42           C  
-ANISOU 8868  CB  VAL B 490     7940   9146   8911   4194   1116   1135       C  
-ATOM   8869  CG1 VAL B 490     -11.408  35.156  -2.536  1.00 66.18           C  
-ANISOU 8869  CG1 VAL B 490     7660   8843   8644   4166   1046   1023       C  
-ATOM   8870  CG2 VAL B 490     -12.848  36.985  -1.643  1.00 67.12           C  
-ANISOU 8870  CG2 VAL B 490     7917   8948   8639   4383   1408   1318       C  
-ATOM   8871  N   ILE B 491     -15.705  36.093  -1.444  1.00 69.50           N  
-ANISOU 8871  N   ILE B 491     7885   9676   8846   4546   1230   1389       N  
-ATOM   8872  CA  ILE B 491     -16.900  36.485  -0.718  1.00 67.83           C  
-ANISOU 8872  CA  ILE B 491     7623   9529   8619   4628   1323   1493       C  
-ATOM   8873  C   ILE B 491     -17.903  35.345  -0.729  1.00 67.92           C  
-ANISOU 8873  C   ILE B 491     7397   9754   8655   4590   1104   1426       C  
-ATOM   8874  O   ILE B 491     -18.545  35.068   0.278  1.00 68.25           O  
-ANISOU 8874  O   ILE B 491     7371   9784   8778   4504   1086   1430       O  
-ATOM   8875  CB  ILE B 491     -17.548  37.741  -1.319  1.00 66.43           C  
-ANISOU 8875  CB  ILE B 491     7500   9450   8291   4924   1547   1668       C  
-ATOM   8876  CG1 ILE B 491     -16.826  38.990  -0.818  1.00 65.05           C  
-ANISOU 8876  CG1 ILE B 491     7570   9018   8129   4940   1807   1756       C  
-ATOM   8877  CG2 ILE B 491     -19.013  37.806  -0.951  1.00 66.25           C  
-ANISOU 8877  CG2 ILE B 491     7328   9604   8241   5048   1567   1745       C  
-ATOM   8878  CD1 ILE B 491     -17.547  40.278  -1.134  1.00 65.27           C  
-ANISOU 8878  CD1 ILE B 491     7668   9093   8037   5227   2044   1938       C  
-ATOM   8879  N   CYS B 492     -18.029  34.671  -1.865  1.00 82.88           N  
-ANISOU 8879  N   CYS B 492     9162  11843  10484   4653    939   1360       N  
-ATOM   8880  CA  CYS B 492     -18.972  33.564  -1.973  1.00 83.48           C  
-ANISOU 8880  CA  CYS B 492     9004  12129  10586   4615    721   1287       C  
-ATOM   8881  C   CYS B 492     -18.618  32.373  -1.088  1.00 80.70           C  
-ANISOU 8881  C   CYS B 492     8605  11647  10412   4329    523   1149       C  
-ATOM   8882  O   CYS B 492     -19.475  31.542  -0.801  1.00 80.20           O  
-ANISOU 8882  O   CYS B 492     8359  11709  10404   4264    375   1112       O  
-ATOM   8883  CB  CYS B 492     -19.104  33.106  -3.420  1.00 85.46           C  
-ANISOU 8883  CB  CYS B 492     9140  12606  10725   4744    584   1230       C  
-ATOM   8884  SG  CYS B 492     -19.873  34.314  -4.489  1.00 91.93           S  
-ANISOU 8884  SG  CYS B 492     9955  13645  11329   5113    762   1405       S  
-ATOM   8885  N   SER B 493     -17.362  32.285  -0.664  1.00 70.44           N  
-ANISOU 8885  N   SER B 493     7459  10097   9207   4162    514   1078       N  
-ATOM   8886  CA  SER B 493     -16.928  31.176   0.177  1.00 66.39           C  
-ANISOU 8886  CA  SER B 493     6920   9437   8868   3905    315    955       C  
-ATOM   8887  C   SER B 493     -16.849  31.609   1.631  1.00 64.32           C  
-ANISOU 8887  C   SER B 493     6768   8974   8698   3795    430   1019       C  
-ATOM   8888  O   SER B 493     -17.044  30.803   2.537  1.00 63.65           O  
-ANISOU 8888  O   SER B 493     6624   8823   8737   3629    291    977       O  
-ATOM   8889  CB  SER B 493     -15.572  30.649  -0.279  1.00 64.81           C  
-ANISOU 8889  CB  SER B 493     6794   9097   8733   3789    191    815       C  
-ATOM   8890  OG  SER B 493     -14.563  31.616  -0.062  1.00 63.86           O  
-ANISOU 8890  OG  SER B 493     6869   8784   8610   3790    375    856       O  
-ATOM   8891  N   LEU B 494     -16.552  32.885   1.852  1.00 65.09           N  
-ANISOU 8891  N   LEU B 494     7033   8966   8734   3891    683   1121       N  
-ATOM   8892  CA  LEU B 494     -16.565  33.447   3.198  1.00 62.77           C  
-ANISOU 8892  CA  LEU B 494     6854   8492   8504   3821    826   1183       C  
-ATOM   8893  C   LEU B 494     -17.986  33.457   3.747  1.00 63.99           C  
-ANISOU 8893  C   LEU B 494     6871   8800   8644   3897    876   1265       C  
-ATOM   8894  O   LEU B 494     -18.207  33.212   4.929  1.00 64.23           O  
-ANISOU 8894  O   LEU B 494     6902   8731   8770   3779    870   1266       O  
-ATOM   8895  CB  LEU B 494     -15.982  34.858   3.199  1.00 59.80           C  
-ANISOU 8895  CB  LEU B 494     6687   7975   8060   3923   1096   1271       C  
-ATOM   8896  CG  LEU B 494     -16.108  35.644   4.501  1.00 57.04           C  
-ANISOU 8896  CG  LEU B 494     6472   7452   7749   3895   1288   1340       C  
-ATOM   8897  CD1 LEU B 494     -15.612  34.819   5.669  1.00 56.05           C  
-ANISOU 8897  CD1 LEU B 494     6373   7148   7777   3650   1133   1246       C  
-ATOM   8898  CD2 LEU B 494     -15.340  36.945   4.407  1.00 53.46           C  
-ANISOU 8898  CD2 LEU B 494     6235   6833   7246   3967   1528   1402       C  
-ATOM   8899  N   ALA B 495     -18.949  33.730   2.878  1.00 65.94           N  
-ANISOU 8899  N   ALA B 495     6986   9295   8772   4102    923   1332       N  
-ATOM   8900  CA  ALA B 495     -20.348  33.675   3.268  1.00 65.74           C  
-ANISOU 8900  CA  ALA B 495     6781   9457   8739   4185    957   1396       C  
-ATOM   8901  C   ALA B 495     -20.749  32.257   3.660  1.00 63.49           C  
-ANISOU 8901  C   ALA B 495     6303   9246   8573   4001    701   1304       C  
-ATOM   8902  O   ALA B 495     -21.671  32.066   4.453  1.00 64.02           O  
-ANISOU 8902  O   ALA B 495     6239   9390   8694   3979    724   1340       O  
-ATOM   8903  CB  ALA B 495     -21.235  34.194   2.151  1.00 67.08           C  
-ANISOU 8903  CB  ALA B 495     6836   9890   8761   4449   1023   1478       C  
-ATOM   8904  N   ALA B 496     -20.063  31.264   3.103  1.00 58.26           N  
-ANISOU 8904  N   ALA B 496     5619   8559   7959   3870    464   1185       N  
-ATOM   8905  CA  ALA B 496     -20.333  29.874   3.457  1.00 55.87           C  
-ANISOU 8905  CA  ALA B 496     5156   8290   7782   3680    202   1097       C  
-ATOM   8906  C   ALA B 496     -19.597  29.499   4.737  1.00 52.65           C  
-ANISOU 8906  C   ALA B 496     4874   7609   7520   3463    142   1070       C  
-ATOM   8907  O   ALA B 496     -20.143  28.810   5.602  1.00 52.71           O  
-ANISOU 8907  O   ALA B 496     4825   7621   7581   3272     52   1071       O  
-ATOM   8908  CB  ALA B 496     -19.945  28.941   2.321  1.00 54.83           C  
-ANISOU 8908  CB  ALA B 496     4951   8238   7645   3642    -32    970       C  
-ATOM   8909  N   ILE B 497     -18.355  29.960   4.855  1.00 53.48           N  
-ANISOU 8909  N   ILE B 497     5201   7481   7637   3417    202   1042       N  
-ATOM   8910  CA  ILE B 497     -17.567  29.742   6.063  1.00 49.70           C  
-ANISOU 8910  CA  ILE B 497     4871   6729   7283   3228    151   1022       C  
-ATOM   8911  C   ILE B 497     -18.274  30.324   7.287  1.00 50.91           C  
-ANISOU 8911  C   ILE B 497     5113   6854   7377   3146    344   1117       C  
-ATOM   8912  O   ILE B 497     -18.250  29.740   8.369  1.00 50.14           O  
-ANISOU 8912  O   ILE B 497     5094   6642   7316   2884    255   1105       O  
-ATOM   8913  CB  ILE B 497     -16.159  30.345   5.926  1.00 46.70           C  
-ANISOU 8913  CB  ILE B 497     4709   6131   6903   3202    224    977       C  
-ATOM   8914  CG1 ILE B 497     -15.201  29.301   5.364  1.00 44.11           C  
-ANISOU 8914  CG1 ILE B 497     4365   5734   6660   3068    -37    834       C  
-ATOM   8915  CG2 ILE B 497     -15.646  30.827   7.268  1.00 43.66           C  
-ANISOU 8915  CG2 ILE B 497     4516   5494   6580   3094    320   1013       C  
-ATOM   8916  CD1 ILE B 497     -14.948  28.148   6.304  1.00 39.62           C  
-ANISOU 8916  CD1 ILE B 497     3789   5013   6252   2851   -294    782       C  
-ATOM   8917  N   ILE B 498     -18.917  31.471   7.103  1.00 50.15           N  
-ANISOU 8917  N   ILE B 498     5006   6863   7185   3375    609   1212       N  
-ATOM   8918  CA  ILE B 498     -19.733  32.066   8.153  1.00 51.35           C  
-ANISOU 8918  CA  ILE B 498     5212   7026   7274   3336    815   1295       C  
-ATOM   8919  C   ILE B 498     -20.851  31.117   8.573  1.00 52.19           C  
-ANISOU 8919  C   ILE B 498     5141   7309   7378   3175    697   1295       C  
-ATOM   8920  O   ILE B 498     -20.911  30.689   9.720  1.00 52.15           O  
-ANISOU 8920  O   ILE B 498     5226   7202   7385   2918    667   1293       O  
-ATOM   8921  CB  ILE B 498     -20.369  33.391   7.693  1.00 52.45           C  
-ANISOU 8921  CB  ILE B 498     5327   7281   7321   3653   1102   1393       C  
-ATOM   8922  CG1 ILE B 498     -19.305  34.477   7.534  1.00 52.69           C  
-ANISOU 8922  CG1 ILE B 498     5577   7096   7347   3776   1271   1409       C  
-ATOM   8923  CG2 ILE B 498     -21.424  33.834   8.686  1.00 53.20           C  
-ANISOU 8923  CG2 ILE B 498     5416   7441   7358   3624   1297   1462       C  
-ATOM   8924  CD1 ILE B 498     -19.864  35.821   7.131  1.00 54.88           C  
-ANISOU 8924  CD1 ILE B 498     5888   7449   7514   4049   1554   1516       C  
-ATOM   8925  N   LYS B 499     -21.737  30.797   7.636  1.00 54.13           N  
-ANISOU 8925  N   LYS B 499     5138   7826   7604   3323    632   1300       N  
-ATOM   8926  CA  LYS B 499     -22.869  29.924   7.912  1.00 55.69           C  
-ANISOU 8926  CA  LYS B 499     5136   8220   7805   3183    528   1296       C  
-ATOM   8927  C   LYS B 499     -22.424  28.686   8.677  1.00 54.98           C  
-ANISOU 8927  C   LYS B 499     5117   7977   7796   2827    292   1229       C  
-ATOM   8928  O   LYS B 499     -23.005  28.329   9.703  1.00 55.42           O  
-ANISOU 8928  O   LYS B 499     5184   8033   7840   2611    313   1256       O  
-ATOM   8929  CB  LYS B 499     -23.559  29.522   6.608  1.00 56.59           C  
-ANISOU 8929  CB  LYS B 499     4976   8617   7909   3362    403   1273       C  
-ATOM   8930  CG  LYS B 499     -24.708  28.550   6.789  1.00 59.46           C  
-ANISOU 8930  CG  LYS B 499     5109   9193   8289   3205    274   1255       C  
-ATOM   8931  CD  LYS B 499     -25.371  28.244   5.454  1.00 63.30           C  
-ANISOU 8931  CD  LYS B 499     5327   9968   8757   3399    151   1225       C  
-ATOM   8932  CE  LYS B 499     -26.390  27.110   5.564  1.00 67.19           C  
-ANISOU 8932  CE  LYS B 499     5584  10656   9288   3202    -22   1182       C  
-ATOM   8933  NZ  LYS B 499     -27.640  27.506   6.264  1.00 69.70           N  
-ANISOU 8933  NZ  LYS B 499     5771  11146   9564   3197    169   1259       N  
-ATOM   8934  N   TYR B 500     -21.379  28.040   8.178  1.00 59.71           N  
-ANISOU 8934  N   TYR B 500     5770   8442   8476   2770     72   1143       N  
-ATOM   8935  CA  TYR B 500     -20.877  26.814   8.786  1.00 57.75           C  
-ANISOU 8935  CA  TYR B 500     5591   8033   8319   2458   -183   1076       C  
-ATOM   8936  C   TYR B 500     -20.397  27.064  10.210  1.00 56.90           C  
-ANISOU 8936  C   TYR B 500     5734   7685   8202   2246   -100   1116       C  
-ATOM   8937  O   TYR B 500     -20.897  26.458  11.149  1.00 57.39           O  
-ANISOU 8937  O   TYR B 500     5816   7732   8258   2002   -149   1141       O  
-ATOM   8938  CB  TYR B 500     -19.747  26.228   7.936  1.00 56.65           C  
-ANISOU 8938  CB  TYR B 500     5470   7781   8275   2482   -408    968       C  
-ATOM   8939  CG  TYR B 500     -19.413  24.787   8.247  1.00 55.40           C  
-ANISOU 8939  CG  TYR B 500     5317   7506   8226   2206   -717    887       C  
-ATOM   8940  CD1 TYR B 500     -20.280  23.762   7.897  1.00 55.64           C  
-ANISOU 8940  CD1 TYR B 500     5149   7709   8284   2116   -890    851       C  
-ATOM   8941  CD2 TYR B 500     -18.222  24.453   8.875  1.00 55.62           C  
-ANISOU 8941  CD2 TYR B 500     5547   7247   8338   2039   -843    843       C  
-ATOM   8942  CE1 TYR B 500     -19.975  22.445   8.177  1.00 56.70           C  
-ANISOU 8942  CE1 TYR B 500     5303   7715   8525   1865  -1171    780       C  
-ATOM   8943  CE2 TYR B 500     -17.908  23.139   9.158  1.00 55.64           C  
-ANISOU 8943  CE2 TYR B 500     5565   7127   8449   1802  -1134    776       C  
-ATOM   8944  CZ  TYR B 500     -18.787  22.137   8.807  1.00 56.32           C  
-ANISOU 8944  CZ  TYR B 500     5468   7371   8560   1715  -1294    746       C  
-ATOM   8945  OH  TYR B 500     -18.478  20.823   9.088  1.00 53.74           O  
-ANISOU 8945  OH  TYR B 500     5171   6901   8347   1478  -1583    682       O  
-ATOM   8946  N   LEU B 501     -19.425  27.958  10.362  1.00 60.55           N  
-ANISOU 8946  N   LEU B 501     6390   7961   8657   2332     25   1121       N  
-ATOM   8947  CA  LEU B 501     -18.905  28.319  11.678  1.00 60.88           C  
-ANISOU 8947  CA  LEU B 501     6681   7773   8676   2150    111   1151       C  
-ATOM   8948  C   LEU B 501     -20.010  28.676  12.663  1.00 64.43           C  
-ANISOU 8948  C   LEU B 501     7139   8317   9023   2068    312   1235       C  
-ATOM   8949  O   LEU B 501     -19.903  28.392  13.854  1.00 66.06           O  
-ANISOU 8949  O   LEU B 501     7504   8388   9207   1816    292   1253       O  
-ATOM   8950  CB  LEU B 501     -17.940  29.495  11.565  1.00 58.74           C  
-ANISOU 8950  CB  LEU B 501     6581   7344   8394   2308    284   1151       C  
-ATOM   8951  CG  LEU B 501     -16.468  29.201  11.822  1.00 57.04           C  
-ANISOU 8951  CG  LEU B 501     6541   6859   8272   2174    117   1076       C  
-ATOM   8952  CD1 LEU B 501     -15.970  28.112  10.891  1.00 57.16           C  
-ANISOU 8952  CD1 LEU B 501     6425   6890   8403   2167   -173    982       C  
-ATOM   8953  CD2 LEU B 501     -15.660  30.476  11.654  1.00 55.13           C  
-ANISOU 8953  CD2 LEU B 501     6443   6490   8013   2340    328   1081       C  
-ATOM   8954  N   LYS B 502     -21.062  29.316  12.166  1.00 52.68           N  
-ANISOU 8954  N   LYS B 502     5483   7064   7470   2287    508   1286       N  
-ATOM   8955  CA  LYS B 502     -22.202  29.657  13.004  1.00 55.90           C  
-ANISOU 8955  CA  LYS B 502     5856   7594   7788   2237    714   1355       C  
-ATOM   8956  C   LYS B 502     -22.787  28.403  13.650  1.00 55.75           C  
-ANISOU 8956  C   LYS B 502     5767   7628   7786   1931    538   1350       C  
-ATOM   8957  O   LYS B 502     -23.211  28.428  14.804  1.00 56.86           O  
-ANISOU 8957  O   LYS B 502     6005   7738   7862   1741    649   1391       O  
-ATOM   8958  CB  LYS B 502     -23.274  30.376  12.187  1.00 59.45           C  
-ANISOU 8958  CB  LYS B 502     6083   8316   8190   2541    902   1401       C  
-ATOM   8959  CG  LYS B 502     -23.106  31.879  12.113  1.00 62.87           C  
-ANISOU 8959  CG  LYS B 502     6632   8692   8563   2804   1195   1449       C  
-ATOM   8960  CD  LYS B 502     -24.179  32.496  11.227  1.00 68.37           C  
-ANISOU 8960  CD  LYS B 502     7095   9662   9220   3121   1342   1500       C  
-ATOM   8961  CE  LYS B 502     -24.259  34.006  11.392  1.00 71.32           C  
-ANISOU 8961  CE  LYS B 502     7591   9979   9529   3364   1668   1564       C  
-ATOM   8962  NZ  LYS B 502     -24.654  34.380  12.781  1.00 75.97           N  
-ANISOU 8962  NZ  LYS B 502     8311  10494  10062   3210   1870   1584       N  
-ATOM   8963  N   GLU B 503     -22.804  27.307  12.899  1.00 57.46           N  
-ANISOU 8963  N   GLU B 503     5824   7921   8087   1878    269   1296       N  
-ATOM   8964  CA  GLU B 503     -23.353  26.051  13.396  1.00 57.46           C  
-ANISOU 8964  CA  GLU B 503     5751   7963   8117   1585     85   1289       C  
-ATOM   8965  C   GLU B 503     -22.581  25.534  14.607  1.00 55.65           C  
-ANISOU 8965  C   GLU B 503     5790   7459   7895   1273    -26   1295       C  
-ATOM   8966  O   GLU B 503     -23.096  24.736  15.387  1.00 57.19           O  
-ANISOU 8966  O   GLU B 503     5994   7658   8076   1003    -99   1323       O  
-ATOM   8967  CB  GLU B 503     -23.377  24.997  12.289  1.00 58.16           C  
-ANISOU 8967  CB  GLU B 503     5641   8151   8305   1599   -195   1213       C  
-ATOM   8968  CG  GLU B 503     -24.285  25.354  11.122  1.00 62.81           C  
-ANISOU 8968  CG  GLU B 503     5947   9045   8873   1876   -119   1209       C  
-ATOM   8969  CD  GLU B 503     -24.239  24.322  10.005  1.00 65.72           C  
-ANISOU 8969  CD  GLU B 503     6135   9505   9329   1887   -402   1118       C  
-ATOM   8970  OE1 GLU B 503     -23.518  23.309  10.160  1.00 67.56           O  
-ANISOU 8970  OE1 GLU B 503     6462   9555   9651   1678   -653   1056       O  
-ATOM   8971  OE2 GLU B 503     -24.919  24.528   8.973  1.00 68.02           O  
-ANISOU 8971  OE2 GLU B 503     6196  10050   9599   2109   -379   1105       O  
-ATOM   8972  N   PHE B 504     -21.350  26.004  14.765  1.00 52.28           N  
-ANISOU 8972  N   PHE B 504     5581   6796   7487   1310    -39   1272       N  
-ATOM   8973  CA  PHE B 504     -20.502  25.587  15.874  1.00 50.59           C  
-ANISOU 8973  CA  PHE B 504     5630   6314   7278   1039   -162   1275       C  
-ATOM   8974  C   PHE B 504     -20.393  26.690  16.925  1.00 52.56           C  
-ANISOU 8974  C   PHE B 504     6096   6465   7408   1023    106   1328       C  
-ATOM   8975  O   PHE B 504     -19.728  26.525  17.948  1.00 52.55           O  
-ANISOU 8975  O   PHE B 504     6334   6250   7381    807     38   1338       O  
-ATOM   8976  CB  PHE B 504     -19.100  25.245  15.365  1.00 44.76           C  
-ANISOU 8976  CB  PHE B 504     4981   5367   6659   1065   -398   1194       C  
-ATOM   8977  CG  PHE B 504     -19.061  24.106  14.380  1.00 40.06           C  
-ANISOU 8977  CG  PHE B 504     4204   4831   6186   1066   -678   1122       C  
-ATOM   8978  CD1 PHE B 504     -18.693  22.832  14.782  1.00 37.36           C  
-ANISOU 8978  CD1 PHE B 504     3926   4340   5928    809   -974   1095       C  
-ATOM   8979  CD2 PHE B 504     -19.368  24.317  13.045  1.00 37.80           C  
-ANISOU 8979  CD2 PHE B 504     3696   4740   5927   1329   -650   1079       C  
-ATOM   8980  CE1 PHE B 504     -18.640  21.791  13.874  1.00 34.45           C  
-ANISOU 8980  CE1 PHE B 504     3400   4010   5679    814  -1229   1015       C  
-ATOM   8981  CE2 PHE B 504     -19.325  23.279  12.133  1.00 34.45           C  
-ANISOU 8981  CE2 PHE B 504     3113   4371   5606   1328   -905    997       C  
-ATOM   8982  CZ  PHE B 504     -18.961  22.013  12.547  1.00 33.59           C  
-ANISOU 8982  CZ  PHE B 504     3067   4106   5591   1070  -1192    959       C  
-ATOM   8983  N   ASN B 505     -21.043  27.817  16.659  1.00 50.92           N  
-ANISOU 8983  N   ASN B 505     5809   6410   7128   1259    403   1359       N  
-ATOM   8984  CA  ASN B 505     -20.866  29.012  17.477  1.00 53.27           C  
-ANISOU 8984  CA  ASN B 505     6311   6605   7324   1299    677   1391       C  
-ATOM   8985  C   ASN B 505     -19.398  29.415  17.521  1.00 51.01           C  
-ANISOU 8985  C   ASN B 505     6245   6054   7084   1315    607   1344       C  
-ATOM   8986  O   ASN B 505     -18.883  29.849  18.546  1.00 50.91           O  
-ANISOU 8986  O   ASN B 505     6475   5862   7007   1182    682   1351       O  
-ATOM   8987  CB  ASN B 505     -21.422  28.801  18.883  1.00 57.28           C  
-ANISOU 8987  CB  ASN B 505     6950   7093   7721   1024    761   1440       C  
-ATOM   8988  CG  ASN B 505     -22.923  28.628  18.888  1.00 62.31           C  
-ANISOU 8988  CG  ASN B 505     7360   8008   8307   1028    899   1483       C  
-ATOM   8989  OD1 ASN B 505     -23.657  29.463  18.359  1.00 66.21           O  
-ANISOU 8989  OD1 ASN B 505     7696   8684   8776   1286   1127   1497       O  
-ATOM   8990  ND2 ASN B 505     -23.390  27.527  19.463  1.00 65.69           N  
-ANISOU 8990  ND2 ASN B 505     7763   8470   8725    741    755   1506       N  
-ATOM   8991  N   LEU B 506     -18.733  29.270  16.382  1.00 52.37           N  
-ANISOU 8991  N   LEU B 506     6322   6212   7365   1476    464   1290       N  
-ATOM   8992  CA  LEU B 506     -17.317  29.589  16.262  1.00 51.31           C  
-ANISOU 8992  CA  LEU B 506     6352   5847   7297   1501    386   1234       C  
-ATOM   8993  C   LEU B 506     -17.088  30.802  15.368  1.00 53.24           C  
-ANISOU 8993  C   LEU B 506     6565   6123   7540   1815    603   1229       C  
-ATOM   8994  O   LEU B 506     -15.962  31.269  15.216  1.00 52.32           O  
-ANISOU 8994  O   LEU B 506     6576   5829   7473   1859    596   1184       O  
-ATOM   8995  CB  LEU B 506     -16.553  28.376  15.729  1.00 45.70           C  
-ANISOU 8995  CB  LEU B 506     5581   5059   6723   1406     34   1163       C  
-ATOM   8996  CG  LEU B 506     -16.385  27.271  16.774  1.00 41.39           C  
-ANISOU 8996  CG  LEU B 506     5154   4381   6190   1074   -202   1169       C  
-ATOM   8997  CD1 LEU B 506     -15.821  25.989  16.173  1.00 37.68           C  
-ANISOU 8997  CD1 LEU B 506     4595   3854   5867   1001   -553   1099       C  
-ATOM   8998  CD2 LEU B 506     -15.502  27.784  17.902  1.00 38.49           C  
-ANISOU 8998  CD2 LEU B 506     5072   3775   5777    931   -165   1172       C  
-ATOM   8999  N   GLU B 507     -18.168  31.315  14.791  1.00 64.52           N  
-ANISOU 8999  N   GLU B 507     7825   7777   8913   2029    796   1279       N  
-ATOM   9000  CA  GLU B 507     -18.098  32.456  13.886  1.00 66.98           C  
-ANISOU 9000  CA  GLU B 507     8101   8135   9212   2345   1004   1295       C  
-ATOM   9001  C   GLU B 507     -17.372  33.663  14.484  1.00 67.19           C  
-ANISOU 9001  C   GLU B 507     8380   7950   9201   2376   1222   1299       C  
-ATOM   9002  O   GLU B 507     -16.907  34.531  13.750  1.00 67.03           O  
-ANISOU 9002  O   GLU B 507     8385   7888   9197   2593   1349   1300       O  
-ATOM   9003  CB  GLU B 507     -19.507  32.867  13.447  1.00 71.91           C  
-ANISOU 9003  CB  GLU B 507     8525   9031   9766   2552   1191   1362       C  
-ATOM   9004  CG  GLU B 507     -20.372  33.454  14.564  1.00 79.80           C  
-ANISOU 9004  CG  GLU B 507     9599  10060  10663   2494   1437   1417       C  
-ATOM   9005  CD  GLU B 507     -20.696  32.449  15.659  1.00 83.06           C  
-ANISOU 9005  CD  GLU B 507    10044  10461  11054   2160   1305   1412       C  
-ATOM   9006  OE1 GLU B 507     -21.744  31.776  15.565  1.00 86.00           O  
-ANISOU 9006  OE1 GLU B 507    10212  11047  11418   2116   1256   1433       O  
-ATOM   9007  OE2 GLU B 507     -19.904  32.336  16.618  1.00 85.67           O  
-ANISOU 9007  OE2 GLU B 507    10609  10570  11373   1937   1249   1389       O  
-ATOM   9008  N   LYS B 508     -17.274  33.713  15.810  1.00 62.27           N  
-ANISOU 9008  N   LYS B 508     7948   7189   8521   2149   1264   1301       N  
-ATOM   9009  CA  LYS B 508     -16.745  34.893  16.494  1.00 64.73           C  
-ANISOU 9009  CA  LYS B 508     8502   7312   8780   2163   1491   1300       C  
-ATOM   9010  C   LYS B 508     -15.331  35.283  16.062  1.00 62.79           C  
-ANISOU 9010  C   LYS B 508     8375   6861   8620   2203   1433   1241       C  
-ATOM   9011  O   LYS B 508     -14.866  36.387  16.357  1.00 62.70           O  
-ANISOU 9011  O   LYS B 508     8542   6702   8581   2263   1639   1236       O  
-ATOM   9012  CB  LYS B 508     -16.793  34.712  18.015  1.00 68.03           C  
-ANISOU 9012  CB  LYS B 508     9115   7618   9114   1877   1498   1299       C  
-ATOM   9013  CG  LYS B 508     -16.256  35.915  18.781  1.00 72.81           C  
-ANISOU 9013  CG  LYS B 508     9982   8026   9656   1872   1727   1282       C  
-ATOM   9014  CD  LYS B 508     -16.464  35.795  20.283  1.00 76.98           C  
-ANISOU 9014  CD  LYS B 508    10702   8477  10068   1604   1763   1283       C  
-ATOM   9015  CE  LYS B 508     -16.034  37.082  20.981  1.00 80.13           C  
-ANISOU 9015  CE  LYS B 508    11354   8696  10396   1623   2017   1255       C  
-ATOM   9016  NZ  LYS B 508     -16.409  37.125  22.422  1.00 84.70           N  
-ANISOU 9016  NZ  LYS B 508    12122   9232  10830   1394   2110   1255       N  
-ATOM   9017  N   MET B 509     -14.652  34.376  15.365  1.00 69.57           N  
-ANISOU 9017  N   MET B 509     9134   7711   9590   2166   1160   1188       N  
-ATOM   9018  CA  MET B 509     -13.284  34.626  14.931  1.00 66.69           C  
-ANISOU 9018  CA  MET B 509     8852   7167   9321   2189   1089   1120       C  
-ATOM   9019  C   MET B 509     -13.232  35.279  13.551  1.00 67.85           C  
-ANISOU 9019  C   MET B 509     8882   7404   9494   2490   1217   1133       C  
-ATOM   9020  O   MET B 509     -12.213  35.857  13.166  1.00 66.67           O  
-ANISOU 9020  O   MET B 509     8818   7114   9401   2550   1265   1093       O  
-ATOM   9021  CB  MET B 509     -12.468  33.335  14.947  1.00 63.71           C  
-ANISOU 9021  CB  MET B 509     8440   6710   9056   1993    732   1044       C  
-ATOM   9022  CG  MET B 509     -13.030  32.224  14.081  1.00 61.60           C  
-ANISOU 9022  CG  MET B 509     7932   6635   8839   2038    530   1038       C  
-ATOM   9023  SD  MET B 509     -11.747  31.029  13.652  1.00 57.98           S  
-ANISOU 9023  SD  MET B 509     7429   6048   8552   1918    156    923       S  
-ATOM   9024  CE  MET B 509     -12.695  29.797  12.772  1.00 58.16           C  
-ANISOU 9024  CE  MET B 509     7185   6309   8604   1961    -38    920       C  
-ATOM   9025  N   LEU B 510     -14.331  35.188  12.809  1.00 67.80           N  
-ANISOU 9025  N   LEU B 510     8680   7637   9443   2673   1273   1191       N  
-ATOM   9026  CA  LEU B 510     -14.411  35.828  11.499  1.00 68.63           C  
-ANISOU 9026  CA  LEU B 510     8681   7849   9546   2972   1398   1222       C  
-ATOM   9027  C   LEU B 510     -14.543  37.337  11.644  1.00 71.73           C  
-ANISOU 9027  C   LEU B 510     9222   8165   9867   3144   1738   1287       C  
-ATOM   9028  O   LEU B 510     -14.198  38.086  10.731  1.00 73.22           O  
-ANISOU 9028  O   LEU B 510     9417   8341  10061   3356   1864   1310       O  
-ATOM   9029  CB  LEU B 510     -15.574  35.273  10.675  1.00 66.91           C  
-ANISOU 9029  CB  LEU B 510     8208   7920   9296   3117   1337   1263       C  
-ATOM   9030  CG  LEU B 510     -15.500  33.790  10.309  1.00 65.42           C  
-ANISOU 9030  CG  LEU B 510     7856   7819   9183   2981   1005   1194       C  
-ATOM   9031  CD1 LEU B 510     -16.614  33.423   9.344  1.00 63.48           C  
-ANISOU 9031  CD1 LEU B 510     7357   7864   8899   3157    971   1229       C  
-ATOM   9032  CD2 LEU B 510     -14.142  33.449   9.720  1.00 63.80           C  
-ANISOU 9032  CD2 LEU B 510     7684   7474   9083   2951    840   1101       C  
-ATOM   9033  N   SER B 511     -15.055  37.780  12.789  1.00 65.90           N  
-ANISOU 9033  N   SER B 511     8145   7337   9557   1289   1607   3294       N  
-ATOM   9034  CA  SER B 511     -15.072  39.202  13.109  1.00 70.55           C  
-ANISOU 9034  CA  SER B 511     8806   7868  10131   1317   1821   3400       C  
-ATOM   9035  C   SER B 511     -13.634  39.652  13.322  1.00 71.38           C  
-ANISOU 9035  C   SER B 511     9026   7944  10151   1262   1941   3328       C  
-ATOM   9036  O   SER B 511     -12.790  38.860  13.746  1.00 70.36           O  
-ANISOU 9036  O   SER B 511     8911   7807  10017   1180   1875   3208       O  
-ATOM   9037  CB  SER B 511     -15.921  39.485  14.353  1.00 69.64           C  
-ANISOU 9037  CB  SER B 511     8662   7649  10150   1268   1921   3477       C  
-ATOM   9038  OG  SER B 511     -15.358  38.899  15.513  1.00 68.37           O  
-ANISOU 9038  OG  SER B 511     8534   7411  10033   1152   1934   3399       O  
-ATOM   9039  N   LYS B 512     -13.362  40.917  13.020  1.00 85.71           N  
-ANISOU 9039  N   LYS B 512    10920   9742  11904   1311   2122   3393       N  
-ATOM   9040  CA  LYS B 512     -11.993  41.428  12.987  1.00 87.24           C  
-ANISOU 9040  CA  LYS B 512    11214   9916  12016   1269   2249   3311       C  
-ATOM   9041  C   LYS B 512     -11.240  40.918  11.758  1.00 90.53           C  
-ANISOU 9041  C   LYS B 512    11652  10421  12324   1309   2137   3222       C  
-ATOM   9042  O   LYS B 512     -10.258  40.185  11.888  1.00 87.11           O  
-ANISOU 9042  O   LYS B 512    11225  10000  11873   1237   2064   3085       O  
-ATOM   9043  CB  LYS B 512     -11.236  41.059  14.266  1.00 86.20           C  
-ANISOU 9043  CB  LYS B 512    11098   9720  11935   1142   2275   3208       C  
-ATOM   9044  CG  LYS B 512     -11.555  41.947  15.459  1.00 86.97           C  
-ANISOU 9044  CG  LYS B 512    11224   9715  12104   1095   2463   3278       C  
-ATOM   9045  CD  LYS B 512     -10.743  43.228  15.409  1.00 89.04           C  
-ANISOU 9045  CD  LYS B 512    11578   9940  12314   1088   2695   3269       C  
-ATOM   9046  CE  LYS B 512      -9.253  42.921  15.320  1.00 90.16           C  
-ANISOU 9046  CE  LYS B 512    11758  10106  12394   1026   2682   3095       C  
-ATOM   9047  NZ  LYS B 512      -8.425  44.147  15.120  1.00 91.70           N  
-ANISOU 9047  NZ  LYS B 512    12034  10263  12543   1018   2919   3065       N  
-ATOM   9048  N   PRO B 513     -11.705  41.304  10.557  1.00 78.35           N  
-ANISOU 9048  N   PRO B 513    10124   8940  10705   1432   2124   3299       N  
-ATOM   9049  CA  PRO B 513     -11.057  40.907   9.304  1.00 81.59           C  
-ANISOU 9049  CA  PRO B 513    10570   9431  11000   1482   2032   3227       C  
-ATOM   9050  C   PRO B 513      -9.671  41.520   9.150  1.00 84.49           C  
-ANISOU 9050  C   PRO B 513    11049   9757  11296   1442   2203   3143       C  
-ATOM   9051  O   PRO B 513      -8.932  41.121   8.254  1.00 84.53           O  
-ANISOU 9051  O   PRO B 513    11090   9812  11217   1457   2143   3057       O  
-ATOM   9052  CB  PRO B 513     -11.993  41.470   8.230  1.00 80.21           C  
-ANISOU 9052  CB  PRO B 513    10407   9313  10756   1640   2024   3356       C  
-ATOM   9053  CG  PRO B 513     -13.296  41.674   8.917  1.00 79.71           C  
-ANISOU 9053  CG  PRO B 513    10259   9224  10802   1662   2019   3470       C  
-ATOM   9054  CD  PRO B 513     -12.939  42.069  10.310  1.00 76.65           C  
-ANISOU 9054  CD  PRO B 513     9890   8725  10507   1541   2177   3460       C  
-ATOM   9055  N   GLU B 514      -9.323  42.476  10.007  1.00106.77           N  
-ANISOU 9055  N   GLU B 514    13922  12488  14159   1387   2419   3158       N  
-ATOM   9056  CA  GLU B 514      -7.997  43.083   9.968  1.00109.91           C  
-ANISOU 9056  CA  GLU B 514    14410  12839  14513   1333   2598   3056       C  
-ATOM   9057  C   GLU B 514      -6.928  42.014  10.115  1.00107.61           C  
-ANISOU 9057  C   GLU B 514    14084  12577  14224   1240   2464   2874       C  
-ATOM   9058  O   GLU B 514      -5.796  42.185   9.667  1.00106.02           O  
-ANISOU 9058  O   GLU B 514    13940  12370  13973   1214   2544   2761       O  
-ATOM   9059  CB  GLU B 514      -7.829  44.112  11.088  1.00115.35           C  
-ANISOU 9059  CB  GLU B 514    15131  13428  15269   1265   2829   3075       C  
-ATOM   9060  CG  GLU B 514      -8.888  45.192  11.124  1.00125.29           C  
-ANISOU 9060  CG  GLU B 514    16420  14642  16542   1347   2980   3257       C  
-ATOM   9061  CD  GLU B 514     -10.202  44.697  11.691  1.00131.18           C  
-ANISOU 9061  CD  GLU B 514    17068  15403  17372   1364   2836   3359       C  
-ATOM   9062  OE1 GLU B 514     -10.358  44.715  12.929  1.00135.30           O  
-ANISOU 9062  OE1 GLU B 514    17556  15864  17986   1276   2877   3354       O  
-ATOM   9063  OE2 GLU B 514     -11.078  44.291  10.900  1.00133.56           O  
-ANISOU 9063  OE2 GLU B 514    17326  15775  17646   1466   2686   3437       O  
-ATOM   9064  N   ASN B 515      -7.299  40.909  10.751  1.00108.91           N  
-ANISOU 9064  N   ASN B 515    14158  12769  14455   1193   2268   2843       N  
-ATOM   9065  CA  ASN B 515      -6.353  39.847  11.050  1.00104.23           C  
-ANISOU 9065  CA  ASN B 515    13532  12198  13874   1111   2136   2679       C  
-ATOM   9066  C   ASN B 515      -6.423  38.686  10.066  1.00101.62           C  
-ANISOU 9066  C   ASN B 515    13160  11953  13498   1149   1916   2636       C  
-ATOM   9067  O   ASN B 515      -5.856  37.619  10.307  1.00101.80           O  
-ANISOU 9067  O   ASN B 515    13143  11998  13539   1091   1774   2518       O  
-ATOM   9068  CB  ASN B 515      -6.561  39.360  12.481  1.00108.45           C  
-ANISOU 9068  CB  ASN B 515    14014  12689  14502   1033   2084   2659       C  
-ATOM   9069  CG  ASN B 515      -6.685  40.504  13.460  1.00112.06           C  
-ANISOU 9069  CG  ASN B 515    14509  13064  15005   1000   2294   2715       C  
-ATOM   9070  OD1 ASN B 515      -6.149  41.589  13.231  1.00115.73           O  
-ANISOU 9070  OD1 ASN B 515    15038  13497  15438   1002   2493   2708       O  
-ATOM   9071  ND2 ASN B 515      -7.404  40.276  14.550  1.00115.48           N  
-ANISOU 9071  ND2 ASN B 515    14907  13453  15516    967   2265   2771       N  
-ATOM   9072  N   PHE B 516      -7.129  38.895   8.959  1.00 74.65           N  
-ANISOU 9072  N   PHE B 516     9758   8588  10019   1252   1886   2732       N  
-ATOM   9073  CA  PHE B 516      -7.081  37.951   7.856  1.00 73.02           C  
-ANISOU 9073  CA  PHE B 516     9528   8467   9748   1294   1703   2681       C  
-ATOM   9074  C   PHE B 516      -5.704  38.072   7.238  1.00 71.56           C  
-ANISOU 9074  C   PHE B 516     9420   8279   9490   1269   1779   2557       C  
-ATOM   9075  O   PHE B 516      -5.019  39.073   7.433  1.00 72.91           O  
-ANISOU 9075  O   PHE B 516     9665   8388   9650   1248   1989   2539       O  
-ATOM   9076  CB  PHE B 516      -8.138  38.271   6.802  1.00 68.58           C  
-ANISOU 9076  CB  PHE B 516     8971   7965   9120   1426   1662   2809       C  
-ATOM   9077  CG  PHE B 516      -9.543  38.027   7.255  1.00 64.14           C  
-ANISOU 9077  CG  PHE B 516     8311   7418   8640   1455   1563   2912       C  
-ATOM   9078  CD1 PHE B 516      -9.822  37.767   8.585  1.00 61.56           C  
-ANISOU 9078  CD1 PHE B 516     7924   7030   8435   1367   1566   2912       C  
-ATOM   9079  CD2 PHE B 516     -10.585  38.046   6.347  1.00 61.35           C  
-ANISOU 9079  CD2 PHE B 516     7926   7142   8244   1575   1467   3001       C  
-ATOM   9080  CE1 PHE B 516     -11.120  37.537   9.005  1.00 58.52           C  
-ANISOU 9080  CE1 PHE B 516     7449   6646   8139   1388   1492   2999       C  
-ATOM   9081  CE2 PHE B 516     -11.883  37.819   6.757  1.00 58.25           C  
-ANISOU 9081  CE2 PHE B 516     7426   6762   7943   1599   1379   3079       C  
-ATOM   9082  CZ  PHE B 516     -12.152  37.563   8.088  1.00 57.63           C  
-ANISOU 9082  CZ  PHE B 516     7289   6610   7999   1500   1399   3078       C  
-ATOM   9083  N   LYS B 517      -5.294  37.054   6.495  1.00 84.73           N  
-ANISOU 9083  N   LYS B 517    11068  10010  11117   1266   1618   2463       N  
-ATOM   9084  CA  LYS B 517      -3.991  37.081   5.852  1.00 81.46           C  
-ANISOU 9084  CA  LYS B 517    10721   9590  10641   1241   1683   2335       C  
-ATOM   9085  C   LYS B 517      -4.105  36.693   4.386  1.00 82.93           C  
-ANISOU 9085  C   LYS B 517    10943   9848  10718   1324   1586   2339       C  
-ATOM   9086  O   LYS B 517      -4.790  35.726   4.041  1.00 79.58           O  
-ANISOU 9086  O   LYS B 517    10448   9496  10293   1350   1379   2351       O  
-ATOM   9087  CB  LYS B 517      -3.010  36.150   6.570  1.00 79.47           C  
-ANISOU 9087  CB  LYS B 517    10414   9327  10453   1132   1597   2171       C  
-ATOM   9088  CG  LYS B 517      -2.678  36.563   7.994  1.00 76.29           C  
-ANISOU 9088  CG  LYS B 517     9993   8857  10138   1055   1699   2139       C  
-ATOM   9089  CD  LYS B 517      -1.956  37.899   8.040  1.00 76.75           C  
-ANISOU 9089  CD  LYS B 517    10130   8852  10181   1041   1958   2115       C  
-ATOM   9090  CE  LYS B 517      -1.588  38.289   9.466  1.00 75.86           C  
-ANISOU 9090  CE  LYS B 517     9993   8680  10152    961   2051   2064       C  
-ATOM   9091  NZ  LYS B 517      -2.790  38.533  10.313  1.00 73.49           N  
-ANISOU 9091  NZ  LYS B 517     9665   8356   9900    976   2047   2211       N  
-ATOM   9092  N   GLN B 518      -3.445  37.461   3.525  1.00 72.12           N  
-ANISOU 9092  N   GLN B 518     9689   8456   9259   1366   1746   2325       N  
-ATOM   9093  CA  GLN B 518      -3.369  37.117   2.117  1.00 77.15           C  
-ANISOU 9093  CA  GLN B 518    10384   9152   9778   1443   1672   2313       C  
-ATOM   9094  C   GLN B 518      -2.500  35.873   2.005  1.00 76.36           C  
-ANISOU 9094  C   GLN B 518    10230   9080   9702   1357   1524   2146       C  
-ATOM   9095  O   GLN B 518      -1.326  35.891   2.371  1.00 77.48           O  
-ANISOU 9095  O   GLN B 518    10384   9169   9885   1270   1616   2016       O  
-ATOM   9096  CB  GLN B 518      -2.770  38.272   1.308  1.00 81.80           C  
-ANISOU 9096  CB  GLN B 518    11130   9684  10268   1503   1914   2332       C  
-ATOM   9097  CG  GLN B 518      -3.006  38.178  -0.196  1.00 90.31           C  
-ANISOU 9097  CG  GLN B 518    12300  10820  11194   1626   1860   2373       C  
-ATOM   9098  CD  GLN B 518      -4.440  38.488  -0.588  1.00 93.73           C  
-ANISOU 9098  CD  GLN B 518    12733  11318  11563   1769   1781   2548       C  
-ATOM   9099  OE1 GLN B 518      -5.085  39.350   0.009  1.00 94.06           O  
-ANISOU 9099  OE1 GLN B 518    12775  11322  11640   1805   1890   2666       O  
-ATOM   9100  NE2 GLN B 518      -4.945  37.781  -1.595  1.00 95.08           N  
-ANISOU 9100  NE2 GLN B 518    12897  11588  11640   1854   1587   2557       N  
-ATOM   9101  N   LEU B 519      -3.085  34.786   1.518  1.00 76.81           N  
-ANISOU 9101  N   LEU B 519    10221   9221   9741   1382   1296   2143       N  
-ATOM   9102  CA  LEU B 519      -2.368  33.524   1.444  1.00 76.17           C  
-ANISOU 9102  CA  LEU B 519    10084   9167   9690   1303   1147   1995       C  
-ATOM   9103  C   LEU B 519      -1.191  33.627   0.483  1.00 79.65           C  
-ANISOU 9103  C   LEU B 519    10622   9590  10051   1298   1237   1888       C  
-ATOM   9104  O   LEU B 519      -0.112  33.105   0.755  1.00 79.27           O  
-ANISOU 9104  O   LEU B 519    10552   9513  10054   1209   1235   1742       O  
-ATOM   9105  CB  LEU B 519      -3.306  32.390   1.031  1.00 70.75           C  
-ANISOU 9105  CB  LEU B 519     9311   8572   9000   1333    903   2013       C  
-ATOM   9106  CG  LEU B 519      -2.763  30.981   1.267  1.00 63.02           C  
-ANISOU 9106  CG  LEU B 519     8252   7608   8084   1242    742   1875       C  
-ATOM   9107  CD1 LEU B 519      -2.138  30.883   2.647  1.00 59.14           C  
-ANISOU 9107  CD1 LEU B 519     7719   7046   7706   1145    793   1812       C  
-ATOM   9108  CD2 LEU B 519      -3.858  29.934   1.096  1.00 59.67           C  
-ANISOU 9108  CD2 LEU B 519     7726   7259   7686   1259    527   1900       C  
-ATOM   9109  N   SER B 520      -1.396  34.312  -0.638  1.00102.55           N  
-ANISOU 9109  N   SER B 520    13637  12503  12826   1401   1322   1960       N  
-ATOM   9110  CA  SER B 520      -0.333  34.489  -1.621  1.00106.21           C  
-ANISOU 9110  CA  SER B 520    14215  12934  13206   1405   1435   1868       C  
-ATOM   9111  C   SER B 520      -0.025  35.966  -1.859  1.00107.84           C  
-ANISOU 9111  C   SER B 520    14562  13056  13355   1457   1721   1928       C  
-ATOM   9112  O   SER B 520      -0.926  36.768  -2.103  1.00106.82           O  
-ANISOU 9112  O   SER B 520    14494  12935  13158   1566   1781   2082       O  
-ATOM   9113  CB  SER B 520      -0.690  33.797  -2.941  1.00107.23           C  
-ANISOU 9113  CB  SER B 520    14381  13149  13214   1484   1280   1873       C  
-ATOM   9114  OG  SER B 520      -1.784  34.430  -3.581  1.00111.58           O  
-ANISOU 9114  OG  SER B 520    14995  13747  13655   1627   1278   2031       O  
-ATOM   9115  N   SER B 521       1.255  36.318  -1.781  1.00102.25           N  
-ANISOU 9115  N   SER B 521    13905  12264  12683   1379   1902   1799       N  
-ATOM   9116  CA  SER B 521       1.693  37.690  -2.009  1.00103.97           C  
-ANISOU 9116  CA  SER B 521    14260  12382  12861   1410   2205   1827       C  
-ATOM   9117  C   SER B 521       2.888  37.699  -2.954  1.00104.27           C  
-ANISOU 9117  C   SER B 521    14405  12364  12849   1388   2337   1694       C  
-ATOM   9118  O   SER B 521       4.036  37.638  -2.514  1.00104.23           O  
-ANISOU 9118  O   SER B 521    14361  12298  12942   1273   2432   1527       O  
-ATOM   9119  CB  SER B 521       2.061  38.361  -0.686  1.00106.14           C  
-ANISOU 9119  CB  SER B 521    14475  12584  13269   1317   2356   1789       C  
-ATOM   9120  OG  SER B 521       2.279  39.748  -0.861  1.00111.96           O  
-ANISOU 9120  OG  SER B 521    15342  13224  13975   1354   2658   1837       O  
-ATOM   9121  N   LYS B 522       2.608  37.780  -4.252  1.00 80.41           N  
-ANISOU 9121  N   LYS B 522    11518   9362   9673   1502   2344   1763       N  
-ATOM   9122  CA  LYS B 522       3.628  37.593  -5.284  1.00 80.05           C  
-ANISOU 9122  CA  LYS B 522    11580   9271   9565   1489   2435   1642       C  
-ATOM   9123  C   LYS B 522       4.858  38.476  -5.098  1.00 77.99           C  
-ANISOU 9123  C   LYS B 522    11390   8870   9373   1410   2752   1521       C  
-ATOM   9124  O   LYS B 522       5.956  38.117  -5.516  1.00 79.09           O  
-ANISOU 9124  O   LYS B 522    11548   8963   9538   1337   2813   1357       O  
-ATOM   9125  CB  LYS B 522       3.027  37.804  -6.671  1.00 81.85           C  
-ANISOU 9125  CB  LYS B 522    11975   9529   9594   1651   2434   1763       C  
-ATOM   9126  N   MET B 523       4.672  39.629  -4.467  1.00 88.09           N  
-ANISOU 9126  N   MET B 523    12700  10079  10690   1418   2961   1592       N  
-ATOM   9127  CA  MET B 523       5.763  40.578  -4.284  1.00 85.05           C  
-ANISOU 9127  CA  MET B 523    12383   9557  10377   1344   3288   1475       C  
-ATOM   9128  C   MET B 523       6.559  40.304  -3.014  1.00 81.05           C  
-ANISOU 9128  C   MET B 523    11699   9037  10059   1183   3271   1299       C  
-ATOM   9129  O   MET B 523       7.667  40.813  -2.846  1.00 79.09           O  
-ANISOU 9129  O   MET B 523    11462   8691   9898   1093   3499   1138       O  
-ATOM   9130  CB  MET B 523       5.221  42.003  -4.268  1.00 83.07           C  
-ANISOU 9130  CB  MET B 523    12263   9226  10073   1433   3548   1630       C  
-ATOM   9131  N   GLU B 524       5.995  39.497  -2.122  1.00 88.81           N  
-ANISOU 9131  N   GLU B 524    12520  10119  11105   1151   3005   1322       N  
-ATOM   9132  CA  GLU B 524       6.581  39.313  -0.800  1.00 84.38           C  
-ANISOU 9132  CA  GLU B 524    11802   9554  10705   1025   2978   1184       C  
-ATOM   9133  C   GLU B 524       7.208  37.938  -0.592  1.00 81.40           C  
-ANISOU 9133  C   GLU B 524    11294   9240  10394    947   2740   1026       C  
-ATOM   9134  O   GLU B 524       8.186  37.810   0.146  1.00 81.14           O  
-ANISOU 9134  O   GLU B 524    11166   9182  10482    844   2772    844       O  
-ATOM   9135  CB  GLU B 524       5.537  39.593   0.286  1.00 82.99           C  
-ANISOU 9135  CB  GLU B 524    11553   9414  10565   1042   2905   1325       C  
-ATOM   9136  CG  GLU B 524       4.848  40.942   0.128  1.00 84.17           C  
-ANISOU 9136  CG  GLU B 524    11826   9501  10654   1127   3135   1493       C  
-ATOM   9137  CD  GLU B 524       4.705  41.699   1.437  1.00 84.04           C  
-ANISOU 9137  CD  GLU B 524    11745   9445  10743   1069   3248   1506       C  
-ATOM   9138  OE1 GLU B 524       4.083  41.159   2.378  1.00 84.82           O  
-ANISOU 9138  OE1 GLU B 524    11722   9609  10895   1047   3050   1551       O  
-ATOM   9139  OE2 GLU B 524       5.220  42.837   1.523  1.00 86.10           O  
-ANISOU 9139  OE2 GLU B 524    12078   9603  11033   1042   3547   1465       O  
-ATOM   9140  N   PHE B 525       6.664  36.922  -1.256  1.00 86.58           N  
-ANISOU 9140  N   PHE B 525    11945   9980  10971   1000   2505   1087       N  
-ATOM   9141  CA  PHE B 525       7.080  35.547  -0.995  1.00 83.22           C  
-ANISOU 9141  CA  PHE B 525    11394   9619  10607    936   2263    963       C  
-ATOM   9142  C   PHE B 525       7.446  34.737  -2.231  1.00 83.15           C  
-ANISOU 9142  C   PHE B 525    11438   9633  10523    954   2179    904       C  
-ATOM   9143  O   PHE B 525       6.727  34.741  -3.231  1.00 82.60           O  
-ANISOU 9143  O   PHE B 525    11468   9594  10322   1049   2144   1029       O  
-ATOM   9144  CB  PHE B 525       5.991  34.815  -0.215  1.00 79.63           C  
-ANISOU 9144  CB  PHE B 525    10832   9254  10171    955   2009   1075       C  
-ATOM   9145  CG  PHE B 525       5.539  35.550   1.005  1.00 77.38           C  
-ANISOU 9145  CG  PHE B 525    10501   8946   9954    941   2079   1145       C  
-ATOM   9146  CD1 PHE B 525       6.384  35.685   2.092  1.00 77.11           C  
-ANISOU 9146  CD1 PHE B 525    10385   8876  10037    849   2139   1003       C  
-ATOM   9147  CD2 PHE B 525       4.278  36.115   1.064  1.00 75.46           C  
-ANISOU 9147  CD2 PHE B 525    10295   8720   9656   1022   2086   1345       C  
-ATOM   9148  CE1 PHE B 525       5.979  36.366   3.213  1.00 76.77           C  
-ANISOU 9148  CE1 PHE B 525    10307   8812  10049    834   2207   1061       C  
-ATOM   9149  CE2 PHE B 525       3.868  36.795   2.183  1.00 74.65           C  
-ANISOU 9149  CE2 PHE B 525    10154   8591   9619   1004   2160   1408       C  
-ATOM   9150  CZ  PHE B 525       4.719  36.921   3.261  1.00 75.69           C  
-ANISOU 9150  CZ  PHE B 525    10214   8684   9862    907   2223   1267       C  
-ATOM   9151  N   MET B 526       8.563  34.026  -2.139  1.00 74.91           N  
-ANISOU 9151  N   MET B 526    10323   8577   9562    867   2140    709       N  
-ATOM   9152  CA  MET B 526       8.980  33.126  -3.199  1.00 73.97           C  
-ANISOU 9152  CA  MET B 526    10236   8479   9391    868   2047    635       C  
-ATOM   9153  C   MET B 526       7.860  32.151  -3.528  1.00 74.51           C  
-ANISOU 9153  C   MET B 526    10278   8653   9380    930   1778    762       C  
-ATOM   9154  O   MET B 526       7.317  31.498  -2.640  1.00 75.84           O  
-ANISOU 9154  O   MET B 526    10327   8881   9608    913   1589    795       O  
-ATOM   9155  CB  MET B 526      10.221  32.346  -2.777  1.00 73.02           C  
-ANISOU 9155  CB  MET B 526    10003   8345   9396    764   1995    412       C  
-ATOM   9156  CG  MET B 526      10.804  31.483  -3.878  1.00 72.04           C  
-ANISOU 9156  CG  MET B 526     9915   8224   9232    753   1935    315       C  
-ATOM   9157  SD  MET B 526      11.961  30.244  -3.257  1.00 67.94           S  
-ANISOU 9157  SD  MET B 526     9233   7722   8860    653   1782     86       S  
-ATOM   9158  CE  MET B 526      13.054  31.260  -2.271  1.00 66.99           C  
-ANISOU 9158  CE  MET B 526     9051   7520   8882    578   2008    -80       C  
-ATOM   9159  N   THR B 527       7.514  32.059  -4.805  1.00 69.95           N  
-ANISOU 9159  N   THR B 527     9815   8094   8667   1004   1768    826       N  
-ATOM   9160  CA  THR B 527       6.503  31.116  -5.249  1.00 70.84           C  
-ANISOU 9160  CA  THR B 527     9899   8312   8704   1061   1517    920       C  
-ATOM   9161  C   THR B 527       7.060  29.710  -5.202  1.00 68.81           C  
-ANISOU 9161  C   THR B 527     9538   8092   8516    983   1330    780       C  
-ATOM   9162  O   THR B 527       8.231  29.488  -5.499  1.00 70.18           O  
-ANISOU 9162  O   THR B 527     9724   8212   8731    920   1408    623       O  
-ATOM   9163  CB  THR B 527       6.068  31.394  -6.690  1.00 72.32           C  
-ANISOU 9163  CB  THR B 527    10246   8517   8717   1169   1555   1007       C  
-ATOM   9164  OG1 THR B 527       5.553  32.726  -6.787  1.00 73.93           O  
-ANISOU 9164  OG1 THR B 527    10564   8680   8846   1258   1740   1145       O  
-ATOM   9165  CG2 THR B 527       4.998  30.401  -7.126  1.00 73.48           C  
-ANISOU 9165  CG2 THR B 527    10342   8784   8793   1224   1282   1083       C  
-ATOM   9166  N   ILE B 528       6.213  28.763  -4.824  1.00 73.82           N  
-ANISOU 9166  N   ILE B 528    10069   8811   9170    989   1092    834       N  
-ATOM   9167  CA  ILE B 528       6.578  27.357  -4.845  1.00 68.30           C  
-ANISOU 9167  CA  ILE B 528     9279   8148   8524    928    907    721       C  
-ATOM   9168  C   ILE B 528       5.368  26.515  -5.186  1.00 65.77           C  
-ANISOU 9168  C   ILE B 528     8917   7924   8148    975    686    815       C  
-ATOM   9169  O   ILE B 528       4.443  26.382  -4.383  1.00 63.76           O  
-ANISOU 9169  O   ILE B 528     8580   7707   7938    987    584    906       O  
-ATOM   9170  CB  ILE B 528       7.117  26.880  -3.498  1.00 67.92           C  
-ANISOU 9170  CB  ILE B 528     9102   8079   8627    848    853    629       C  
-ATOM   9171  CG1 ILE B 528       8.420  27.603  -3.158  1.00 66.32           C  
-ANISOU 9171  CG1 ILE B 528     8914   7790   8494    793   1054    495       C  
-ATOM   9172  CG2 ILE B 528       7.342  25.381  -3.535  1.00 66.93           C  
-ANISOU 9172  CG2 ILE B 528     8892   7991   8546    803    655    536       C  
-ATOM   9173  CD1 ILE B 528       9.058  27.130  -1.876  1.00 66.43           C  
-ANISOU 9173  CD1 ILE B 528     8803   7792   8644    728    991    384       C  
-ATOM   9174  N   ASN B 529       5.380  25.946  -6.382  1.00 73.66           N  
-ANISOU 9174  N   ASN B 529     9972   8961   9055    998    620    784       N  
-ATOM   9175  CA  ASN B 529       4.285  25.112  -6.826  1.00 73.96           C  
-ANISOU 9175  CA  ASN B 529     9965   9097   9041   1038    412    845       C  
-ATOM   9176  C   ASN B 529       3.991  23.957  -5.869  1.00 73.04           C  
-ANISOU 9176  C   ASN B 529     9693   9007   9051    971    233    809       C  
-ATOM   9177  O   ASN B 529       4.867  23.487  -5.137  1.00 72.27           O  
-ANISOU 9177  O   ASN B 529     9538   8860   9063    894    240    704       O  
-ATOM   9178  CB  ASN B 529       4.573  24.576  -8.223  1.00 74.89           C  
-ANISOU 9178  CB  ASN B 529    10162   9243   9048   1055    372    779       C  
-ATOM   9179  CG  ASN B 529       3.395  23.836  -8.807  1.00 75.46           C  
-ANISOU 9179  CG  ASN B 529    10194   9427   9052   1107    166    835       C  
-ATOM   9180  OD1 ASN B 529       3.483  22.649  -9.113  1.00 75.44           O  
-ANISOU 9180  OD1 ASN B 529    10130   9460   9072   1056     25    745       O  
-ATOM   9181  ND2 ASN B 529       2.267  24.531  -8.942  1.00 76.07           N  
-ANISOU 9181  ND2 ASN B 529    10294   9560   9049   1208    148    975       N  
-ATOM   9182  N   GLY B 530       2.744  23.505  -5.879  1.00 50.85           N  
-ANISOU 9182  N   GLY B 530     6820   6275   6227   1009     77    893       N  
-ATOM   9183  CA  GLY B 530       2.363  22.332  -5.122  1.00 49.26           C  
-ANISOU 9183  CA  GLY B 530     6487   6093   6136    951    -83    860       C  
-ATOM   9184  C   GLY B 530       3.144  21.119  -5.582  1.00 46.65           C  
-ANISOU 9184  C   GLY B 530     6135   5759   5829    885   -163    717       C  
-ATOM   9185  O   GLY B 530       3.203  20.114  -4.883  1.00 43.29           O  
-ANISOU 9185  O   GLY B 530     5619   5321   5509    827   -259    663       O  
-ATOM   9186  N   THR B 531       3.744  21.210  -6.765  1.00 56.88           N  
-ANISOU 9186  N   THR B 531     7526   7059   7028    898   -113    658       N  
-ATOM   9187  CA  THR B 531       4.540  20.115  -7.312  1.00 55.23           C  
-ANISOU 9187  CA  THR B 531     7307   6841   6835    836   -173    519       C  
-ATOM   9188  C   THR B 531       5.988  20.236  -6.869  1.00 53.38           C  
-ANISOU 9188  C   THR B 531     7087   6516   6678    775    -49    405       C  
-ATOM   9189  O   THR B 531       6.659  19.234  -6.621  1.00 51.07           O  
-ANISOU 9189  O   THR B 531     6735   6199   6469    711   -111    293       O  
-ATOM   9190  CB  THR B 531       4.455  20.056  -8.855  1.00 57.91           C  
-ANISOU 9190  CB  THR B 531     7744   7231   7028    878   -188    500       C  
-ATOM   9191  OG1 THR B 531       3.351  19.227  -9.244  1.00 57.63           O  
-ANISOU 9191  OG1 THR B 531     7641   7289   6966    896   -371    523       O  
-ATOM   9192  CG2 THR B 531       5.738  19.492  -9.453  1.00 56.83           C  
-ANISOU 9192  CG2 THR B 531     7651   7042   6900    815   -139    352       C  
-ATOM   9193  N   THR B 532       6.460  21.474  -6.763  1.00 47.67           N  
-ANISOU 9193  N   THR B 532     6439   5742   5933    799    129    429       N  
-ATOM   9194  CA  THR B 532       7.809  21.738  -6.287  1.00 46.05           C  
-ANISOU 9194  CA  THR B 532     6234   5452   5811    743    260    310       C  
-ATOM   9195  C   THR B 532       7.884  21.418  -4.801  1.00 46.17           C  
-ANISOU 9195  C   THR B 532     6133   5450   5958    707    202    296       C  
-ATOM   9196  O   THR B 532       8.885  20.894  -4.314  1.00 46.53           O  
-ANISOU 9196  O   THR B 532     6126   5455   6097    655    198    168       O  
-ATOM   9197  CB  THR B 532       8.199  23.205  -6.502  1.00 44.92           C  
-ANISOU 9197  CB  THR B 532     6196   5254   5618    774    483    337       C  
-ATOM   9198  OG1 THR B 532       7.661  23.666  -7.747  1.00 45.45           O  
-ANISOU 9198  OG1 THR B 532     6388   5349   5532    846    524    417       O  
-ATOM   9199  CG2 THR B 532       9.709  23.359  -6.505  1.00 41.43           C  
-ANISOU 9199  CG2 THR B 532     5767   4727   5247    711    628    171       C  
-ATOM   9200  N   LEU B 533       6.810  21.741  -4.086  1.00 47.62           N  
-ANISOU 9200  N   LEU B 533     6283   5664   6148    743    157    428       N  
-ATOM   9201  CA  LEU B 533       6.683  21.408  -2.674  1.00 44.81           C  
-ANISOU 9201  CA  LEU B 533     5833   5292   5899    721     95    437       C  
-ATOM   9202  C   LEU B 533       6.965  19.928  -2.481  1.00 44.17           C  
-ANISOU 9202  C   LEU B 533     5681   5216   5886    679    -54    346       C  
-ATOM   9203  O   LEU B 533       7.849  19.549  -1.717  1.00 42.63           O  
-ANISOU 9203  O   LEU B 533     5443   4980   5776    649    -57    247       O  
-ATOM   9204  CB  LEU B 533       5.268  21.722  -2.198  1.00 43.31           C  
-ANISOU 9204  CB  LEU B 533     5620   5140   5696    766     44    598       C  
-ATOM   9205  CG  LEU B 533       5.071  22.642  -0.996  1.00 39.43           C  
-ANISOU 9205  CG  LEU B 533     5114   4613   5253    777    131    670       C  
-ATOM   9206  CD1 LEU B 533       6.185  23.659  -0.902  1.00 38.90           C  
-ANISOU 9206  CD1 LEU B 533     5098   4491   5191    763    313    597       C  
-ATOM   9207  CD2 LEU B 533       3.710  23.324  -1.082  1.00 36.45           C  
-ANISOU 9207  CD2 LEU B 533     4753   4274   4823    836    134    836       C  
-ATOM   9208  N   ARG B 534       6.206  19.095  -3.187  1.00 53.38           N  
-ANISOU 9208  N   ARG B 534     6835   6434   7014    683   -176    374       N  
-ATOM   9209  CA  ARG B 534       6.379  17.647  -3.128  1.00 53.93           C  
-ANISOU 9209  CA  ARG B 534     6844   6503   7143    643   -307    292       C  
-ATOM   9210  C   ARG B 534       7.784  17.182  -3.532  1.00 53.81           C  
-ANISOU 9210  C   ARG B 534     6842   6449   7154    601   -274    134       C  
-ATOM   9211  O   ARG B 534       8.487  16.568  -2.731  1.00 52.37           O  
-ANISOU 9211  O   ARG B 534     6610   6227   7062    579   -304     53       O  
-ATOM   9212  CB  ARG B 534       5.320  16.938  -3.981  1.00 58.11           C  
-ANISOU 9212  CB  ARG B 534     7359   7099   7622    649   -425    334       C  
-ATOM   9213  CG  ARG B 534       4.026  16.627  -3.245  1.00 63.25           C  
-ANISOU 9213  CG  ARG B 534     7940   7773   8318    662   -515    435       C  
-ATOM   9214  CD  ARG B 534       2.852  17.455  -3.750  1.00 70.42           C  
-ANISOU 9214  CD  ARG B 534     8866   8746   9145    719   -513    556       C  
-ATOM   9215  NE  ARG B 534       2.051  16.751  -4.750  1.00 76.52           N  
-ANISOU 9215  NE  ARG B 534     9612   9593   9869    724   -630    545       N  
-ATOM   9216  CZ  ARG B 534       2.232  16.850  -6.064  1.00 79.47           C  
-ANISOU 9216  CZ  ARG B 534    10048  10016  10130    744   -633    508       C  
-ATOM   9217  NH1 ARG B 534       3.195  17.620  -6.546  1.00 81.47           N  
-ANISOU 9217  NH1 ARG B 534    10401  10238  10315    759   -511    482       N  
-ATOM   9218  NH2 ARG B 534       1.452  16.174  -6.898  1.00 81.96           N  
-ANISOU 9218  NH2 ARG B 534    10330  10408  10404    750   -753    489       N  
-ATOM   9219  N   ASN B 535       8.191  17.467  -4.768  1.00 46.16           N  
-ANISOU 9219  N   ASN B 535     5945   5488   6106    598   -210     89       N  
-ATOM   9220  CA  ASN B 535       9.486  17.006  -5.265  1.00 46.30           C  
-ANISOU 9220  CA  ASN B 535     5976   5464   6153    554   -170    -66       C  
-ATOM   9221  C   ASN B 535      10.632  17.266  -4.295  1.00 47.21           C  
-ANISOU 9221  C   ASN B 535     6050   5518   6369    535    -97   -165       C  
-ATOM   9222  O   ASN B 535      11.384  16.356  -3.955  1.00 47.78           O  
-ANISOU 9222  O   ASN B 535     6067   5565   6521    508   -156   -275       O  
-ATOM   9223  CB  ASN B 535       9.818  17.644  -6.616  1.00 46.77           C  
-ANISOU 9223  CB  ASN B 535     6143   5521   6108    561    -58    -90       C  
-ATOM   9224  CG  ASN B 535       8.793  17.323  -7.690  1.00 48.22           C  
-ANISOU 9224  CG  ASN B 535     6370   5775   6176    589   -145    -17       C  
-ATOM   9225  OD1 ASN B 535       8.473  18.172  -8.527  1.00 48.93           O  
-ANISOU 9225  OD1 ASN B 535     6558   5884   6148    637    -67     45       O  
-ATOM   9226  ND2 ASN B 535       8.278  16.097  -7.677  1.00 48.85           N  
-ANISOU 9226  ND2 ASN B 535     6379   5893   6287    565   -302    -30       N  
-ATOM   9227  N   LEU B 536      10.760  18.512  -3.854  1.00 42.73           N  
-ANISOU 9227  N   LEU B 536     5508   4929   5797    555     31   -130       N  
-ATOM   9228  CA  LEU B 536      11.850  18.904  -2.969  1.00 42.16           C  
-ANISOU 9228  CA  LEU B 536     5392   4808   5817    539    110   -240       C  
-ATOM   9229  C   LEU B 536      11.590  18.476  -1.527  1.00 41.44           C  
-ANISOU 9229  C   LEU B 536     5222   4723   5801    557      5   -210       C  
-ATOM   9230  O   LEU B 536      12.394  18.748  -0.631  1.00 41.09           O  
-ANISOU 9230  O   LEU B 536     5133   4652   5829    557     42   -297       O  
-ATOM   9231  CB  LEU B 536      12.057  20.413  -3.029  1.00 42.24           C  
-ANISOU 9231  CB  LEU B 536     5461   4789   5799    548    301   -221       C  
-ATOM   9232  CG  LEU B 536      12.340  20.980  -4.416  1.00 42.53           C  
-ANISOU 9232  CG  LEU B 536     5604   4802   5752    542    439   -243       C  
-ATOM   9233  CD1 LEU B 536      12.432  22.495  -4.363  1.00 41.86           C  
-ANISOU 9233  CD1 LEU B 536     5585   4677   5641    558    644   -207       C  
-ATOM   9234  CD2 LEU B 536      13.616  20.377  -4.965  1.00 43.98           C  
-ANISOU 9234  CD2 LEU B 536     5776   4943   5992    491    468   -428       C  
-ATOM   9235  N   GLU B 537      10.459  17.808  -1.315  1.00 56.64           N  
-ANISOU 9235  N   GLU B 537     7132   6683   7707    576   -121    -95       N  
-ATOM   9236  CA  GLU B 537      10.080  17.313   0.003  1.00 54.28           C  
-ANISOU 9236  CA  GLU B 537     6778   6378   7469    598   -214    -51       C  
-ATOM   9237  C   GLU B 537      10.226  18.395   1.062  1.00 53.83           C  
-ANISOU 9237  C   GLU B 537     6716   6303   7435    619   -126    -27       C  
-ATOM   9238  O   GLU B 537      10.885  18.197   2.085  1.00 53.31           O  
-ANISOU 9238  O   GLU B 537     6608   6216   7433    632   -151   -101       O  
-ATOM   9239  CB  GLU B 537      10.904  16.080   0.368  1.00 54.34           C  
-ANISOU 9239  CB  GLU B 537     6737   6361   7547    591   -308   -173       C  
-ATOM   9240  CG  GLU B 537      10.582  14.871  -0.494  1.00 56.49           C  
-ANISOU 9240  CG  GLU B 537     7009   6647   7806    567   -404   -183       C  
-ATOM   9241  CD  GLU B 537      11.542  13.716  -0.281  1.00 59.09           C  
-ANISOU 9241  CD  GLU B 537     7300   6945   8205    562   -473   -314       C  
-ATOM   9242  OE1 GLU B 537      12.702  13.819  -0.733  1.00 62.94           O  
-ANISOU 9242  OE1 GLU B 537     7783   7416   8716    542   -419   -449       O  
-ATOM   9243  OE2 GLU B 537      11.138  12.704   0.331  1.00 61.42           O  
-ANISOU 9243  OE2 GLU B 537     7573   7226   8536    580   -572   -284       O  
-ATOM   9244  N   ILE B 538       9.596  19.537   0.803  1.00 42.01           N  
-ANISOU 9244  N   ILE B 538     5264   4817   5882    629    -26     76       N  
-ATOM   9245  CA  ILE B 538       9.661  20.684   1.698  1.00 41.93           C  
-ANISOU 9245  CA  ILE B 538     5255   4787   5888    643     81    105       C  
-ATOM   9246  C   ILE B 538       8.931  20.449   3.020  1.00 42.12           C  
-ANISOU 9246  C   ILE B 538     5246   4809   5947    670      2    196       C  
-ATOM   9247  O   ILE B 538       9.471  20.724   4.093  1.00 41.27           O  
-ANISOU 9247  O   ILE B 538     5114   4681   5887    680     23    143       O  
-ATOM   9248  CB  ILE B 538       9.055  21.922   1.037  1.00 41.28           C  
-ANISOU 9248  CB  ILE B 538     5241   4712   5732    655    213    210       C  
-ATOM   9249  CG1 ILE B 538       9.836  22.272  -0.227  1.00 42.36           C  
-ANISOU 9249  CG1 ILE B 538     5433   4835   5827    634    323    120       C  
-ATOM   9250  CG2 ILE B 538       9.043  23.081   2.008  1.00 40.92           C  
-ANISOU 9250  CG2 ILE B 538     5195   4641   5710    664    330    247       C  
-ATOM   9251  CD1 ILE B 538      11.328  22.347  -0.008  1.00 43.17           C  
-ANISOU 9251  CD1 ILE B 538     5503   4895   6005    596    400    -70       C  
-ATOM   9252  N   LEU B 539       7.701  19.951   2.940  1.00 49.62           N  
-ANISOU 9252  N   LEU B 539     6199   5780   6875    684    -85    324       N  
-ATOM   9253  CA  LEU B 539       6.884  19.754   4.130  1.00 48.85           C  
-ANISOU 9253  CA  LEU B 539     6083   5667   6811    708   -139    422       C  
-ATOM   9254  C   LEU B 539       6.794  18.288   4.533  1.00 49.15           C  
-ANISOU 9254  C   LEU B 539     6092   5689   6892    711   -278    395       C  
-ATOM   9255  O   LEU B 539       6.697  17.972   5.716  1.00 46.37           O  
-ANISOU 9255  O   LEU B 539     5735   5303   6579    736   -313    414       O  
-ATOM   9256  CB  LEU B 539       5.489  20.342   3.917  1.00 48.55           C  
-ANISOU 9256  CB  LEU B 539     6061   5649   6735    722   -116    586       C  
-ATOM   9257  CG  LEU B 539       5.472  21.866   3.767  1.00 47.20           C  
-ANISOU 9257  CG  LEU B 539     5930   5480   6523    732     37    637       C  
-ATOM   9258  CD1 LEU B 539       4.128  22.358   3.241  1.00 43.95           C  
-ANISOU 9258  CD1 LEU B 539     5536   5100   6062    760     47    791       C  
-ATOM   9259  CD2 LEU B 539       5.834  22.550   5.086  1.00 45.68           C  
-ANISOU 9259  CD2 LEU B 539     5733   5249   6374    736    111    629       C  
-ATOM   9260  N   GLN B 540       6.841  17.391   3.555  1.00 55.15           N  
-ANISOU 9260  N   GLN B 540     6843   6468   7643    690   -346    348       N  
-ATOM   9261  CA  GLN B 540       6.753  15.969   3.857  1.00 59.11           C  
-ANISOU 9261  CA  GLN B 540     7324   6947   8190    691   -461    320       C  
-ATOM   9262  C   GLN B 540       7.529  15.108   2.873  1.00 62.15           C  
-ANISOU 9262  C   GLN B 540     7699   7342   8575    663   -506    199       C  
-ATOM   9263  O   GLN B 540       7.582  15.409   1.689  1.00 63.03           O  
-ANISOU 9263  O   GLN B 540     7822   7488   8637    638   -475    179       O  
-ATOM   9264  CB  GLN B 540       5.293  15.529   3.922  1.00 61.04           C  
-ANISOU 9264  CB  GLN B 540     7557   7193   8443    688   -512    443       C  
-ATOM   9265  CG  GLN B 540       4.445  16.014   2.768  1.00 64.64           C  
-ANISOU 9265  CG  GLN B 540     8009   7707   8843    673   -500    508       C  
-ATOM   9266  CD  GLN B 540       2.968  15.737   2.985  1.00 66.44           C  
-ANISOU 9266  CD  GLN B 540     8207   7941   9096    675   -545    621       C  
-ATOM   9267  OE1 GLN B 540       2.461  15.864   4.101  1.00 66.60           O  
-ANISOU 9267  OE1 GLN B 540     8227   7918   9161    691   -527    694       O  
-ATOM   9268  NE2 GLN B 540       2.271  15.350   1.917  1.00 68.97           N  
-ANISOU 9268  NE2 GLN B 540     8502   8314   9391    658   -601    627       N  
-ATOM   9269  N   ASN B 541       8.144  14.043   3.377  1.00 50.12           N  
-ANISOU 9269  N   ASN B 541     6161   5782   7101    675   -575    119       N  
-ATOM   9270  CA  ASN B 541       8.906  13.133   2.532  1.00 54.29           C  
-ANISOU 9270  CA  ASN B 541     6677   6311   7640    650   -617      2       C  
-ATOM   9271  C   ASN B 541       7.974  12.384   1.594  1.00 59.24           C  
-ANISOU 9271  C   ASN B 541     7299   6960   8250    613   -671     45       C  
-ATOM   9272  O   ASN B 541       6.876  11.999   1.979  1.00 59.41           O  
-ANISOU 9272  O   ASN B 541     7311   6973   8288    616   -711    138       O  
-ATOM   9273  CB  ASN B 541       9.713  12.145   3.376  1.00 49.66           C  
-ANISOU 9273  CB  ASN B 541     6080   5678   7111    687   -679    -83       C  
-ATOM   9274  CG  ASN B 541       8.871  10.994   3.892  1.00 46.44           C  
-ANISOU 9274  CG  ASN B 541     5680   5230   6734    701   -752    -15       C  
-ATOM   9275  OD1 ASN B 541       8.665  10.001   3.191  1.00 44.83           O  
-ANISOU 9275  OD1 ASN B 541     5468   5021   6545    669   -796    -40       O  
-ATOM   9276  ND2 ASN B 541       8.381  11.119   5.123  1.00 43.84           N  
-ANISOU 9276  ND2 ASN B 541     5373   4866   6417    748   -752     68       N  
-ATOM   9277  N   GLN B 542       8.417  12.176   0.360  1.00 84.65           N  
-ANISOU 9277  N   GLN B 542    10521  10205  11439    575   -669    -33       N  
-ATOM   9278  CA  GLN B 542       7.553  11.613  -0.671  1.00 90.81           C  
-ANISOU 9278  CA  GLN B 542    11295  11022  12187    540   -719     -5       C  
-ATOM   9279  C   GLN B 542       7.678  10.101  -0.798  1.00 90.71           C  
-ANISOU 9279  C   GLN B 542    11258  10979  12227    514   -796    -75       C  
-ATOM   9280  O   GLN B 542       7.811   9.569  -1.897  1.00 91.86           O  
-ANISOU 9280  O   GLN B 542    11405  11148  12350    474   -819   -141       O  
-ATOM   9281  CB  GLN B 542       7.820  12.289  -2.017  1.00100.44           C  
-ANISOU 9281  CB  GLN B 542    12549  12288  13324    520   -667    -38       C  
-ATOM   9282  CG  GLN B 542       7.645  13.798  -1.985  1.00114.65           C  
-ANISOU 9282  CG  GLN B 542    14385  14111  15067    549   -571     37       C  
-ATOM   9283  CD  GLN B 542       6.306  14.221  -1.412  1.00123.45           C  
-ANISOU 9283  CD  GLN B 542    15483  15247  16174    576   -591    182       C  
-ATOM   9284  OE1 GLN B 542       5.345  13.453  -1.411  1.00130.60           O  
-ANISOU 9284  OE1 GLN B 542    16352  16168  17101    567   -675    225       O  
-ATOM   9285  NE2 GLN B 542       6.240  15.449  -0.912  1.00128.21           N  
-ANISOU 9285  NE2 GLN B 542    16110  15847  16758    606   -503    251       N  
-ATOM   9286  N   THR B 543       7.638   9.418   0.339  1.00 71.56           N  
-ANISOU 9286  N   THR B 543     8824   8497   9869    542   -828    -61       N  
-ATOM   9287  CA  THR B 543       7.626   7.963   0.368  1.00 71.04           C  
-ANISOU 9287  CA  THR B 543     8746   8387   9860    526   -885   -110       C  
-ATOM   9288  C   THR B 543       6.783   7.537   1.553  1.00 71.26           C  
-ANISOU 9288  C   THR B 543     8776   8360   9938    557   -898    -20       C  
-ATOM   9289  O   THR B 543       6.597   6.345   1.805  1.00 72.10           O  
-ANISOU 9289  O   THR B 543     8884   8411  10099    552   -926    -39       O  
-ATOM   9290  CB  THR B 543       9.032   7.376   0.587  1.00 68.69           C  
-ANISOU 9290  CB  THR B 543     8456   8045   9599    549   -891   -229       C  
-ATOM   9291  OG1 THR B 543       9.269   7.211   1.992  1.00 66.29           O  
-ANISOU 9291  OG1 THR B 543     8168   7685   9333    618   -899   -204       O  
-ATOM   9292  CG2 THR B 543      10.112   8.273  -0.014  1.00 68.29           C  
-ANISOU 9292  CG2 THR B 543     8408   8027   9512    542   -840   -312       C  
-ATOM   9293  N   ASP B 544       6.268   8.529   2.272  1.00 86.12           N  
-ANISOU 9293  N   ASP B 544    10668  10250  11803    587   -864     77       N  
-ATOM   9294  CA  ASP B 544       5.668   8.305   3.574  1.00 84.87           C  
-ANISOU 9294  CA  ASP B 544    10530  10028  11688    627   -857    160       C  
-ATOM   9295  C   ASP B 544       4.599   9.351   3.865  1.00 82.44           C  
-ANISOU 9295  C   ASP B 544    10215   9748  11362    628   -820    280       C  
-ATOM   9296  O   ASP B 544       3.645   9.086   4.596  1.00 82.88           O  
-ANISOU 9296  O   ASP B 544    10274   9756  11460    635   -811    361       O  
-ATOM   9297  CB  ASP B 544       6.766   8.365   4.635  1.00 88.76           C  
-ANISOU 9297  CB  ASP B 544    11062  10475  12186    698   -851    120       C  
-ATOM   9298  CG  ASP B 544       6.288   7.935   5.997  1.00 91.52           C  
-ANISOU 9298  CG  ASP B 544    11459  10746  12570    754   -846    195       C  
-ATOM   9299  OD1 ASP B 544       5.294   7.186   6.071  1.00 94.80           O  
-ANISOU 9299  OD1 ASP B 544    11876  11115  13027    730   -844    248       O  
-ATOM   9300  OD2 ASP B 544       6.919   8.339   6.996  1.00 93.71           O  
-ANISOU 9300  OD2 ASP B 544    11772  11002  12831    822   -838    192       O  
-ATOM   9301  N   MET B 545       4.771  10.537   3.288  1.00 72.07           N  
-ANISOU 9301  N   MET B 545     8895   8501   9988    622   -787    291       N  
-ATOM   9302  CA  MET B 545       3.842  11.650   3.476  1.00 68.93           C  
-ANISOU 9302  CA  MET B 545     8491   8133   9565    630   -744    405       C  
-ATOM   9303  C   MET B 545       4.013  12.330   4.832  1.00 65.41           C  
-ANISOU 9303  C   MET B 545     8080   7643   9131    678   -693    461       C  
-ATOM   9304  O   MET B 545       3.283  13.266   5.161  1.00 65.91           O  
-ANISOU 9304  O   MET B 545     8144   7718   9182    687   -646    560       O  
-ATOM   9305  CB  MET B 545       2.393  11.190   3.316  1.00 70.47           C  
-ANISOU 9305  CB  MET B 545     8646   8331   9797    603   -774    475       C  
-ATOM   9306  CG  MET B 545       2.120  10.337   2.084  1.00 74.17           C  
-ANISOU 9306  CG  MET B 545     9073   8843  10264    554   -836    407       C  
-ATOM   9307  SD  MET B 545       2.467  11.154   0.509  1.00 75.34           S  
-ANISOU 9307  SD  MET B 545     9223   9098  10305    544   -840    368       S  
-ATOM   9308  CE  MET B 545       4.155  10.634   0.206  1.00 75.10           C  
-ANISOU 9308  CE  MET B 545     9229   9039  10266    534   -836    231       C  
-ATOM   9309  N   LYS B 546       4.979  11.861   5.614  1.00 67.74           N  
-ANISOU 9309  N   LYS B 546     8404   7888   9445    714   -706    396       N  
-ATOM   9310  CA  LYS B 546       5.193  12.398   6.952  1.00 63.80           C  
-ANISOU 9310  CA  LYS B 546     7943   7350   8949    768   -670    435       C  
-ATOM   9311  C   LYS B 546       6.304  13.434   6.965  1.00 60.00           C  
-ANISOU 9311  C   LYS B 546     7461   6906   8432    783   -627    364       C  
-ATOM   9312  O   LYS B 546       7.165  13.444   6.089  1.00 59.83           O  
-ANISOU 9312  O   LYS B 546     7419   6919   8396    762   -630    262       O  
-ATOM   9313  CB  LYS B 546       5.527  11.275   7.932  1.00 66.09           C  
-ANISOU 9313  CB  LYS B 546     8274   7563   9274    818   -713    407       C  
-ATOM   9314  CG  LYS B 546       4.585  10.088   7.845  1.00 67.23           C  
-ANISOU 9314  CG  LYS B 546     8422   7655   9469    796   -737    448       C  
-ATOM   9315  CD  LYS B 546       3.152  10.484   8.145  1.00 68.55           C  
-ANISOU 9315  CD  LYS B 546     8581   7804   9660    772   -694    574       C  
-ATOM   9316  CE  LYS B 546       2.201   9.374   7.733  1.00 70.52           C  
-ANISOU 9316  CE  LYS B 546     8805   8017   9971    727   -712    584       C  
-ATOM   9317  NZ  LYS B 546       2.663   8.041   8.227  1.00 73.31           N  
-ANISOU 9317  NZ  LYS B 546     9210   8285  10360    758   -730    532       N  
-ATOM   9318  N   THR B 547       6.282  14.300   7.971  1.00 53.25           N  
-ANISOU 9318  N   THR B 547     6628   6037   7567    817   -577    411       N  
-ATOM   9319  CA  THR B 547       7.301  15.334   8.119  1.00 51.02           C  
-ANISOU 9319  CA  THR B 547     6338   5784   7262    828   -521    334       C  
-ATOM   9320  C   THR B 547       8.721  14.762   8.165  1.00 51.82           C  
-ANISOU 9320  C   THR B 547     6424   5886   7378    856   -570    173       C  
-ATOM   9321  O   THR B 547       9.649  15.348   7.612  1.00 51.90           O  
-ANISOU 9321  O   THR B 547     6405   5930   7384    835   -528     67       O  
-ATOM   9322  CB  THR B 547       7.052  16.197   9.373  1.00 47.90           C  
-ANISOU 9322  CB  THR B 547     5971   5367   6860    864   -468    400       C  
-ATOM   9323  OG1 THR B 547       5.879  16.997   9.178  1.00 45.51           O  
-ANISOU 9323  OG1 THR B 547     5672   5073   6547    834   -402    535       O  
-ATOM   9324  CG2 THR B 547       8.236  17.112   9.631  1.00 47.20           C  
-ANISOU 9324  CG2 THR B 547     5866   5307   6762    875   -416    287       C  
-ATOM   9325  N   LYS B 548       8.889  13.618   8.821  1.00 60.24           N  
-ANISOU 9325  N   LYS B 548     7514   6910   8466    906   -650    153       N  
-ATOM   9326  CA  LYS B 548      10.206  12.994   8.933  1.00 60.62           C  
-ANISOU 9326  CA  LYS B 548     7545   6957   8529    949   -708      2       C  
-ATOM   9327  C   LYS B 548      10.865  12.901   7.560  1.00 58.07           C  
-ANISOU 9327  C   LYS B 548     7175   6671   8219    890   -699   -102       C  
-ATOM   9328  O   LYS B 548      10.317  12.297   6.641  1.00 57.47           O  
-ANISOU 9328  O   LYS B 548     7098   6593   8144    842   -715    -68       O  
-ATOM   9329  CB  LYS B 548      10.103  11.603   9.577  1.00 65.70           C  
-ANISOU 9329  CB  LYS B 548     8234   7541   9189   1013   -790     17       C  
-ATOM   9330  CG  LYS B 548      11.449  10.955   9.927  1.00 71.88           C  
-ANISOU 9330  CG  LYS B 548     9007   8321   9984   1087   -860   -130       C  
-ATOM   9331  CD  LYS B 548      11.249   9.550  10.507  1.00 77.15           C  
-ANISOU 9331  CD  LYS B 548     9738   8916  10658   1158   -926    -96       C  
-ATOM   9332  CE  LYS B 548      12.532   8.994  11.138  1.00 80.68           C  
-ANISOU 9332  CE  LYS B 548    10189   9361  11103   1267  -1003   -225       C  
-ATOM   9333  NZ  LYS B 548      13.661   8.850  10.171  1.00 81.39           N  
-ANISOU 9333  NZ  LYS B 548    10200   9495  11231   1236  -1025   -384       N  
-ATOM   9334  N   GLY B 549      12.035  13.516   7.422  1.00 53.82           N  
-ANISOU 9334  N   GLY B 549     6596   6162   7690    890   -667   -238       N  
-ATOM   9335  CA  GLY B 549      12.774  13.468   6.174  1.00 50.34           C  
-ANISOU 9335  CA  GLY B 549     6119   5742   7265    836   -640   -350       C  
-ATOM   9336  C   GLY B 549      12.566  14.670   5.273  1.00 48.42           C  
-ANISOU 9336  C   GLY B 549     5876   5529   6994    769   -525   -327       C  
-ATOM   9337  O   GLY B 549      13.173  14.754   4.206  1.00 49.93           O  
-ANISOU 9337  O   GLY B 549     6053   5730   7190    723   -481   -418       O  
-ATOM   9338  N   SER B 550      11.706  15.592   5.698  1.00 34.13           N  
-ANISOU 9338  N   SER B 550     4091   3726   5152    768   -467   -205       N  
-ATOM   9339  CA  SER B 550      11.445  16.813   4.943  1.00 31.87           C  
-ANISOU 9339  CA  SER B 550     3819   3461   4831    722   -345   -166       C  
-ATOM   9340  C   SER B 550      12.420  17.894   5.363  1.00 30.71           C  
-ANISOU 9340  C   SER B 550     3647   3315   4706    722   -245   -275       C  
-ATOM   9341  O   SER B 550      13.194  17.702   6.294  1.00 29.35           O  
-ANISOU 9341  O   SER B 550     3439   3139   4574    762   -288   -374       O  
-ATOM   9342  CB  SER B 550      10.020  17.301   5.188  1.00 32.69           C  
-ANISOU 9342  CB  SER B 550     3956   3568   4895    725   -325     19       C  
-ATOM   9343  OG  SER B 550       9.866  17.779   6.514  1.00 30.94           O  
-ANISOU 9343  OG  SER B 550     3738   3330   4686    763   -312     61       O  
-ATOM   9344  N   LEU B 551      12.389  19.031   4.676  1.00 38.11           N  
-ANISOU 9344  N   LEU B 551     4605   4258   5618    683   -108   -262       N  
-ATOM   9345  CA  LEU B 551      13.265  20.139   5.041  1.00 38.38           C  
-ANISOU 9345  CA  LEU B 551     4614   4286   5684    672     16   -372       C  
-ATOM   9346  C   LEU B 551      12.808  20.738   6.362  1.00 38.57           C  
-ANISOU 9346  C   LEU B 551     4637   4309   5708    706     23   -300       C  
-ATOM   9347  O   LEU B 551      13.617  20.971   7.260  1.00 38.19           O  
-ANISOU 9347  O   LEU B 551     4544   4265   5702    727     24   -418       O  
-ATOM   9348  CB  LEU B 551      13.283  21.220   3.957  1.00 38.03           C  
-ANISOU 9348  CB  LEU B 551     4611   4230   5607    625    186   -365       C  
-ATOM   9349  CG  LEU B 551      14.044  22.490   4.348  1.00 36.94           C  
-ANISOU 9349  CG  LEU B 551     4453   4074   5509    604    348   -467       C  
-ATOM   9350  CD1 LEU B 551      15.538  22.273   4.222  1.00 36.06           C  
-ANISOU 9350  CD1 LEU B 551     4274   3950   5476    582    370   -702       C  
-ATOM   9351  CD2 LEU B 551      13.606  23.675   3.508  1.00 38.28           C  
-ANISOU 9351  CD2 LEU B 551     4697   4222   5627    577    530   -385       C  
-ATOM   9352  N   LEU B 552      11.505  20.990   6.461  1.00 44.15           N  
-ANISOU 9352  N   LEU B 552     5392   5016   6368    713     28   -112       N  
-ATOM   9353  CA  LEU B 552      10.897  21.521   7.677  1.00 44.74           C  
-ANISOU 9353  CA  LEU B 552     5478   5083   6440    741     41    -20       C  
-ATOM   9354  C   LEU B 552      11.327  20.705   8.889  1.00 46.25           C  
-ANISOU 9354  C   LEU B 552     5645   5269   6659    796    -82    -83       C  
-ATOM   9355  O   LEU B 552      11.569  21.245   9.967  1.00 44.45           O  
-ANISOU 9355  O   LEU B 552     5409   5040   6440    822    -60   -113       O  
-ATOM   9356  CB  LEU B 552       9.377  21.494   7.562  1.00 43.50           C  
-ANISOU 9356  CB  LEU B 552     5364   4921   6242    746     24    186       C  
-ATOM   9357  CG  LEU B 552       8.638  21.976   8.805  1.00 41.51           C  
-ANISOU 9357  CG  LEU B 552     5131   4651   5991    773     41    294       C  
-ATOM   9358  CD1 LEU B 552       9.059  23.393   9.128  1.00 41.84           C  
-ANISOU 9358  CD1 LEU B 552     5172   4689   6036    755    193    257       C  
-ATOM   9359  CD2 LEU B 552       7.135  21.892   8.607  1.00 41.31           C  
-ANISOU 9359  CD2 LEU B 552     5135   4619   5941    774     25    483       C  
-ATOM   9360  N   TRP B 553      11.405  19.394   8.702  1.00 45.67           N  
-ANISOU 9360  N   TRP B 553     5568   5192   6593    818   -210   -103       N  
-ATOM   9361  CA  TRP B 553      11.943  18.505   9.715  1.00 47.59           C  
-ANISOU 9361  CA  TRP B 553     5800   5427   6854    886   -328   -174       C  
-ATOM   9362  C   TRP B 553      13.364  18.938  10.061  1.00 46.98           C  
-ANISOU 9362  C   TRP B 553     5662   5374   6813    901   -307   -376       C  
-ATOM   9363  O   TRP B 553      13.660  19.264  11.207  1.00 47.31           O  
-ANISOU 9363  O   TRP B 553     5697   5423   6854    951   -323   -417       O  
-ATOM   9364  CB  TRP B 553      11.933  17.071   9.193  1.00 52.24           C  
-ANISOU 9364  CB  TRP B 553     6394   6003   7451    898   -440   -181       C  
-ATOM   9365  CG  TRP B 553      12.539  16.067  10.115  1.00 57.34           C  
-ANISOU 9365  CG  TRP B 553     7042   6635   8111    981   -558   -255       C  
-ATOM   9366  CD1 TRP B 553      12.039  15.652  11.310  1.00 58.40           C  
-ANISOU 9366  CD1 TRP B 553     7230   6738   8223   1053   -617   -173       C  
-ATOM   9367  CD2 TRP B 553      13.750  15.328   9.905  1.00 60.52           C  
-ANISOU 9367  CD2 TRP B 553     7400   7047   8547   1012   -627   -422       C  
-ATOM   9368  NE1 TRP B 553      12.866  14.704  11.864  1.00 61.17           N  
-ANISOU 9368  NE1 TRP B 553     7581   7080   8581   1136   -721   -273       N  
-ATOM   9369  CE2 TRP B 553      13.925  14.489  11.021  1.00 61.49           C  
-ANISOU 9369  CE2 TRP B 553     7554   7149   8660   1113   -734   -429       C  
-ATOM   9370  CE3 TRP B 553      14.704  15.297   8.883  1.00 61.50           C  
-ANISOU 9370  CE3 TRP B 553     7466   7192   8711    967   -604   -567       C  
-ATOM   9371  CZ2 TRP B 553      15.016  13.631  11.146  1.00 62.47           C  
-ANISOU 9371  CZ2 TRP B 553     7647   7279   8810   1179   -827   -574       C  
-ATOM   9372  CZ3 TRP B 553      15.786  14.446   9.008  1.00 62.23           C  
-ANISOU 9372  CZ3 TRP B 553     7518   7286   8840   1020   -691   -716       C  
-ATOM   9373  CH2 TRP B 553      15.933  13.625  10.130  1.00 62.97           C  
-ANISOU 9373  CH2 TRP B 553     7638   7367   8922   1129   -806   -718       C  
-ATOM   9374  N   VAL B 554      14.239  18.959   9.062  1.00 43.66           N  
-ANISOU 9374  N   VAL B 554     5197   4966   6427    858   -269   -510       N  
-ATOM   9375  CA  VAL B 554      15.630  19.344   9.274  1.00 43.48           C  
-ANISOU 9375  CA  VAL B 554     5098   4964   6460    863   -240   -727       C  
-ATOM   9376  C   VAL B 554      15.733  20.621  10.094  1.00 42.71           C  
-ANISOU 9376  C   VAL B 554     4983   4878   6366    859   -140   -755       C  
-ATOM   9377  O   VAL B 554      16.705  20.823  10.822  1.00 42.88           O  
-ANISOU 9377  O   VAL B 554     4941   4925   6427    893   -161   -923       O  
-ATOM   9378  CB  VAL B 554      16.367  19.568   7.941  1.00 44.77           C  
-ANISOU 9378  CB  VAL B 554     5226   5122   6662    791   -146   -845       C  
-ATOM   9379  CG1 VAL B 554      17.819  19.919   8.197  1.00 45.27           C  
-ANISOU 9379  CG1 VAL B 554     5197   5202   6803    793   -113  -1090       C  
-ATOM   9380  CG2 VAL B 554      16.267  18.333   7.064  1.00 46.01           C  
-ANISOU 9380  CG2 VAL B 554     5402   5268   6813    788   -236   -823       C  
-ATOM   9381  N   LEU B 555      14.720  21.473   9.978  1.00 44.02           N  
-ANISOU 9381  N   LEU B 555     5203   5027   6494    820    -35   -596       N  
-ATOM   9382  CA  LEU B 555      14.759  22.794  10.592  1.00 44.14           C  
-ANISOU 9382  CA  LEU B 555     5209   5045   6516    800     94   -614       C  
-ATOM   9383  C   LEU B 555      13.999  22.894  11.911  1.00 45.41           C  
-ANISOU 9383  C   LEU B 555     5410   5204   6638    853     43   -497       C  
-ATOM   9384  O   LEU B 555      14.278  23.782  12.715  1.00 46.11           O  
-ANISOU 9384  O   LEU B 555     5478   5304   6739    854    112   -557       O  
-ATOM   9385  CB  LEU B 555      14.204  23.845   9.628  1.00 42.21           C  
-ANISOU 9385  CB  LEU B 555     5005   4776   6256    728    273   -522       C  
-ATOM   9386  CG  LEU B 555      14.970  24.150   8.339  1.00 43.57           C  
-ANISOU 9386  CG  LEU B 555     5158   4936   6460    668    388   -640       C  
-ATOM   9387  CD1 LEU B 555      14.175  25.123   7.479  1.00 42.96           C  
-ANISOU 9387  CD1 LEU B 555     5154   4830   6338    625    552   -500       C  
-ATOM   9388  CD2 LEU B 555      16.351  24.710   8.641  1.00 43.23           C  
-ANISOU 9388  CD2 LEU B 555     5029   4898   6498    646    468   -885       C  
-ATOM   9389  N   ASP B 556      13.041  22.000  12.142  1.00 43.60           N  
-ANISOU 9389  N   ASP B 556     5241   4957   6368    893    -64   -337       N  
-ATOM   9390  CA AASP B 556      12.201  22.118  13.329  0.50 41.86           C  
-ANISOU 9390  CA AASP B 556     5075   4718   6111    937    -89   -208       C  
-ATOM   9391  CA BASP B 556      12.195  22.081  13.331  0.50 41.86           C  
-ANISOU 9391  CA BASP B 556     5076   4717   6111    938    -93   -207       C  
-ATOM   9392  C   ASP B 556      12.956  21.827  14.633  1.00 50.86           C  
-ANISOU 9392  C   ASP B 556     6202   5877   7245   1020   -185   -327       C  
-ATOM   9393  O   ASP B 556      13.147  20.679  15.033  1.00 54.49           O  
-ANISOU 9393  O   ASP B 556     6682   6332   7689   1095   -325   -344       O  
-ATOM   9394  CB AASP B 556      10.950  21.248  13.214  0.50 35.31           C  
-ANISOU 9394  CB AASP B 556     4312   3852   5252    952   -158    -16       C  
-ATOM   9395  CB BASP B 556      10.963  21.157  13.217  0.50 35.26           C  
-ANISOU 9395  CB BASP B 556     4307   3845   5246    955   -168    -17       C  
-ATOM   9396  CG AASP B 556       9.827  21.733  14.109  0.50 30.84           C  
-ANISOU 9396  CG AASP B 556     3806   3252   4659    963   -115    149       C  
-ATOM   9397  CG BASP B 556      11.323  19.666  13.116  0.50 33.68           C  
-ANISOU 9397  CG BASP B 556     4108   3639   5049   1006   -316    -66       C  
-ATOM   9398  OD1AASP B 556      10.118  22.395  15.126  0.50 30.97           O  
-ANISOU 9398  OD1AASP B 556     3827   3273   4667    988    -81    107       O  
-ATOM   9399  OD1BASP B 556      12.480  19.287  13.395  0.50 35.81           O  
-ANISOU 9399  OD1BASP B 556     4338   3934   5336   1051   -384   -232       O  
-ATOM   9400  OD2AASP B 556       8.653  21.456  13.795  0.50 28.06           O  
-ANISOU 9400  OD2AASP B 556     3492   2871   4299    946   -114    312       O  
-ATOM   9401  OD2BASP B 556      10.427  18.862  12.765  0.50 30.34           O  
-ANISOU 9401  OD2BASP B 556     3724   3185   4617   1002   -362     58       O  
-ATOM   9402  N   HIS B 557      13.393  22.894  15.292  1.00 47.52           N  
-ANISOU 9402  N   HIS B 557     5748   5475   6831   1011   -103   -413       N  
-ATOM   9403  CA  HIS B 557      14.003  22.770  16.610  1.00 51.09           C  
-ANISOU 9403  CA  HIS B 557     6193   5955   7263   1097   -192   -520       C  
-ATOM   9404  C   HIS B 557      13.300  23.722  17.568  1.00 51.14           C  
-ANISOU 9404  C   HIS B 557     6249   5945   7237   1092   -107   -423       C  
-ATOM   9405  O   HIS B 557      13.890  24.234  18.520  1.00 51.25           O  
-ANISOU 9405  O   HIS B 557     6238   5992   7244   1127   -110   -542       O  
-ATOM   9406  CB  HIS B 557      15.511  23.024  16.564  1.00 54.97           C  
-ANISOU 9406  CB  HIS B 557     6573   6504   7808   1102   -202   -789       C  
-ATOM   9407  CG  HIS B 557      16.295  21.888  15.984  1.00 60.95           C  
-ANISOU 9407  CG  HIS B 557     7288   7279   8593   1141   -323   -899       C  
-ATOM   9408  ND1 HIS B 557      16.611  20.754  16.703  1.00 63.22           N  
-ANISOU 9408  ND1 HIS B 557     7598   7577   8844   1260   -500   -931       N  
-ATOM   9409  CD2 HIS B 557      16.825  21.708  14.751  1.00 61.95           C  
-ANISOU 9409  CD2 HIS B 557     7357   7404   8776   1080   -286   -982       C  
-ATOM   9410  CE1 HIS B 557      17.298  19.925  15.938  1.00 64.16           C  
-ANISOU 9410  CE1 HIS B 557     7669   7705   9004   1268   -567  -1029       C  
-ATOM   9411  NE2 HIS B 557      17.445  20.482  14.750  1.00 63.09           N  
-ANISOU 9411  NE2 HIS B 557     7482   7562   8926   1155   -440  -1064       N  
-ATOM   9412  N   THR B 558      12.024  23.957  17.292  1.00 49.73           N  
-ANISOU 9412  N   THR B 558     6137   5717   7043   1048    -31   -210       N  
-ATOM   9413  CA  THR B 558      11.211  24.818  18.127  1.00 50.68           C  
-ANISOU 9413  CA  THR B 558     6310   5808   7137   1037     59    -92       C  
-ATOM   9414  C   THR B 558      10.859  24.088  19.414  1.00 52.28           C  
-ANISOU 9414  C   THR B 558     6596   5987   7282   1135    -57    -30       C  
-ATOM   9415  O   THR B 558      10.863  22.861  19.455  1.00 51.69           O  
-ANISOU 9415  O   THR B 558     6556   5898   7186   1200   -188    -12       O  
-ATOM   9416  CB  THR B 558       9.920  25.220  17.405  1.00 49.75           C  
-ANISOU 9416  CB  THR B 558     6234   5645   7025    971    166    116       C  
-ATOM   9417  OG1 THR B 558       9.312  24.054  16.839  1.00 50.70           O  
-ANISOU 9417  OG1 THR B 558     6384   5741   7138    989     67    220       O  
-ATOM   9418  CG2 THR B 558      10.218  26.208  16.293  1.00 47.45           C  
-ANISOU 9418  CG2 THR B 558     5887   5369   6771    887    314     67       C  
-ATOM   9419  N   LYS B 559      10.561  24.851  20.463  1.00 54.67           N  
-ANISOU 9419  N   LYS B 559     6939   6278   7557   1145      3      3       N  
-ATOM   9420  CA  LYS B 559      10.205  24.297  21.767  1.00 57.25           C  
-ANISOU 9420  CA  LYS B 559     7365   6572   7817   1241    -83     66       C  
-ATOM   9421  C   LYS B 559       8.713  24.422  22.036  1.00 53.28           C  
-ANISOU 9421  C   LYS B 559     6954   5986   7303   1214     -5    302       C  
-ATOM   9422  O   LYS B 559       8.172  23.737  22.903  1.00 53.37           O  
-ANISOU 9422  O   LYS B 559     7068   5942   7267   1286    -65    396       O  
-ATOM   9423  CB  LYS B 559      10.985  25.002  22.880  1.00 66.29           C  
-ANISOU 9423  CB  LYS B 559     8496   7764   8929   1284    -84    -84       C  
-ATOM   9424  CG  LYS B 559      12.424  24.548  23.012  1.00 80.82           C  
-ANISOU 9424  CG  LYS B 559    10261   9683  10764   1358   -214   -323       C  
-ATOM   9425  CD  LYS B 559      13.144  25.316  24.105  1.00 91.86           C  
-ANISOU 9425  CD  LYS B 559    11633  11139  12132   1398   -215   -485       C  
-ATOM   9426  CE  LYS B 559      14.480  24.677  24.429  1.00 99.13           C  
-ANISOU 9426  CE  LYS B 559    12489  12141  13035   1505   -382   -716       C  
-ATOM   9427  NZ  LYS B 559      14.307  23.306  24.990  1.00105.28           N  
-ANISOU 9427  NZ  LYS B 559    13380  12890  13730   1647   -550   -638       N  
-ATOM   9428  N   THR B 560       8.050  25.301  21.294  1.00 49.05           N  
-ANISOU 9428  N   THR B 560     6387   5437   6814   1117    134    395       N  
-ATOM   9429  CA  THR B 560       6.625  25.517  21.476  1.00 44.91           C  
-ANISOU 9429  CA  THR B 560     5930   4839   6295   1087    215    609       C  
-ATOM   9430  C   THR B 560       5.828  25.128  20.236  1.00 42.27           C  
-ANISOU 9430  C   THR B 560     5572   4487   6003   1037    226    726       C  
-ATOM   9431  O   THR B 560       6.294  25.276  19.110  1.00 40.39           O  
-ANISOU 9431  O   THR B 560     5262   4295   5791    994    239    659       O  
-ATOM   9432  CB  THR B 560       6.326  26.983  21.800  1.00 44.67           C  
-ANISOU 9432  CB  THR B 560     5892   4804   6278   1027    380    642       C  
-ATOM   9433  OG1 THR B 560       6.483  27.777  20.617  1.00 45.70           O  
-ANISOU 9433  OG1 THR B 560     5945   4966   6454    949    486    618       O  
-ATOM   9434  CG2 THR B 560       7.259  27.491  22.887  1.00 41.98           C  
-ANISOU 9434  CG2 THR B 560     5551   4499   5901   1065    376    487       C  
-ATOM   9435  N   SER B 561       4.614  24.638  20.451  1.00 47.85           N  
-ANISOU 9435  N   SER B 561     6339   5124   6716   1042    224    895       N  
-ATOM   9436  CA  SER B 561       3.756  24.234  19.347  1.00 46.70           C  
-ANISOU 9436  CA  SER B 561     6165   4967   6612   1000    223   1001       C  
-ATOM   9437  C   SER B 561       3.325  25.425  18.485  1.00 47.10           C  
-ANISOU 9437  C   SER B 561     6164   5043   6690    929    352   1059       C  
-ATOM   9438  O   SER B 561       3.150  25.283  17.275  1.00 44.42           O  
-ANISOU 9438  O   SER B 561     5777   4733   6367    899    343   1075       O  
-ATOM   9439  CB  SER B 561       2.535  23.486  19.868  1.00 44.97           C  
-ANISOU 9439  CB  SER B 561     6015   4663   6410   1019    206   1151       C  
-ATOM   9440  OG  SER B 561       1.763  24.324  20.700  1.00 44.49           O  
-ANISOU 9440  OG  SER B 561     5999   4550   6354   1006    316   1258       O  
-ATOM   9441  N   PHE B 562       3.143  26.591  19.099  1.00 48.46           N  
-ANISOU 9441  N   PHE B 562     6351   5200   6860    909    476   1094       N  
-ATOM   9442  CA  PHE B 562       2.845  27.795  18.330  1.00 49.60           C  
-ANISOU 9442  CA  PHE B 562     6458   5363   7024    854    615   1143       C  
-ATOM   9443  C   PHE B 562       4.117  28.281  17.634  1.00 50.90           C  
-ANISOU 9443  C   PHE B 562     6569   5590   7182    832    648    977       C  
-ATOM   9444  O   PHE B 562       4.066  29.049  16.671  1.00 52.71           O  
-ANISOU 9444  O   PHE B 562     6771   5837   7420    794    751    994       O  
-ATOM   9445  CB  PHE B 562       2.224  28.892  19.209  1.00 49.85           C  
-ANISOU 9445  CB  PHE B 562     6527   5349   7063    837    754   1235       C  
-ATOM   9446  CG  PHE B 562       2.928  29.093  20.519  1.00 50.76           C  
-ANISOU 9446  CG  PHE B 562     6680   5457   7151    861    755   1138       C  
-ATOM   9447  CD1 PHE B 562       4.024  29.932  20.610  1.00 51.94           C  
-ANISOU 9447  CD1 PHE B 562     6792   5652   7292    841    823    984       C  
-ATOM   9448  CD2 PHE B 562       2.491  28.443  21.662  1.00 51.13           C  
-ANISOU 9448  CD2 PHE B 562     6801   5447   7178    908    693   1193       C  
-ATOM   9449  CE1 PHE B 562       4.679  30.114  21.813  1.00 50.90           C  
-ANISOU 9449  CE1 PHE B 562     6684   5525   7131    869    811    877       C  
-ATOM   9450  CE2 PHE B 562       3.140  28.624  22.870  1.00 51.08           C  
-ANISOU 9450  CE2 PHE B 562     6839   5440   7128    944    685   1100       C  
-ATOM   9451  CZ  PHE B 562       4.236  29.460  22.944  1.00 51.02           C  
-ANISOU 9451  CZ  PHE B 562     6782   5494   7111    926    735    938       C  
-ATOM   9452  N   GLY B 563       5.261  27.813  18.122  1.00 45.68           N  
-ANISOU 9452  N   GLY B 563     5893   4957   6505    862    564    811       N  
-ATOM   9453  CA  GLY B 563       6.528  28.073  17.466  1.00 45.69           C  
-ANISOU 9453  CA  GLY B 563     5832   5013   6515    841    581    629       C  
-ATOM   9454  C   GLY B 563       6.640  27.249  16.198  1.00 45.60           C  
-ANISOU 9454  C   GLY B 563     5792   5025   6510    836    502    617       C  
-ATOM   9455  O   GLY B 563       7.029  27.752  15.149  1.00 44.93           O  
-ANISOU 9455  O   GLY B 563     5673   4963   6435    796    581    567       O  
-ATOM   9456  N   ARG B 564       6.283  25.974  16.296  1.00 62.13           N  
-ANISOU 9456  N   ARG B 564     7908   7106   8594    877    357    662       N  
-ATOM   9457  CA  ARG B 564       6.325  25.071  15.155  1.00 64.55           C  
-ANISOU 9457  CA  ARG B 564     8189   7432   8905    871    273    652       C  
-ATOM   9458  C   ARG B 564       5.361  25.498  14.049  1.00 64.24           C  
-ANISOU 9458  C   ARG B 564     8147   7392   8868    831    345    784       C  
-ATOM   9459  O   ARG B 564       5.728  25.522  12.876  1.00 65.23           O  
-ANISOU 9459  O   ARG B 564     8246   7550   8989    807    358    735       O  
-ATOM   9460  CB  ARG B 564       6.020  23.638  15.599  1.00 68.42           C  
-ANISOU 9460  CB  ARG B 564     8712   7895   9391    922    123    684       C  
-ATOM   9461  CG  ARG B 564       5.929  22.640  14.456  1.00 74.57           C  
-ANISOU 9461  CG  ARG B 564     9465   8688  10179    911     39    682       C  
-ATOM   9462  CD  ARG B 564       5.879  21.212  14.983  1.00 81.81           C  
-ANISOU 9462  CD  ARG B 564    10416   9571  11097    964    -94    679       C  
-ATOM   9463  NE  ARG B 564       7.058  20.885  15.782  1.00 88.94           N  
-ANISOU 9463  NE  ARG B 564    11326  10486  11982   1024   -161    536       N  
-ATOM   9464  CZ  ARG B 564       7.039  20.644  17.090  1.00 92.14           C  
-ANISOU 9464  CZ  ARG B 564    11794  10855  12361   1091   -196    549       C  
-ATOM   9465  NH1 ARG B 564       5.893  20.679  17.757  1.00 93.96           N  
-ANISOU 9465  NH1 ARG B 564    12090  11022  12588   1096   -157    703       N  
-ATOM   9466  NH2 ARG B 564       8.167  20.357  17.728  1.00 93.15           N  
-ANISOU 9466  NH2 ARG B 564    11921  11008  12464   1159   -270    405       N  
-ATOM   9467  N   ARG B 565       4.129  25.829  14.423  1.00 54.31           N  
-ANISOU 9467  N   ARG B 565     6921   6099   7616    830    390    949       N  
-ATOM   9468  CA  ARG B 565       3.114  26.220  13.451  1.00 52.24           C  
-ANISOU 9468  CA  ARG B 565     6653   5843   7353    810    443   1080       C  
-ATOM   9469  C   ARG B 565       3.563  27.427  12.627  1.00 52.14           C  
-ANISOU 9469  C   ARG B 565     6633   5856   7321    784    583   1047       C  
-ATOM   9470  O   ARG B 565       3.125  27.624  11.491  1.00 51.64           O  
-ANISOU 9470  O   ARG B 565     6568   5816   7237    781    609   1106       O  
-ATOM   9471  CB  ARG B 565       1.785  26.521  14.149  1.00 51.07           C  
-ANISOU 9471  CB  ARG B 565     6531   5647   7225    816    484   1247       C  
-ATOM   9472  CG  ARG B 565       1.090  25.302  14.730  1.00 50.44           C  
-ANISOU 9472  CG  ARG B 565     6466   5526   7172    838    370   1302       C  
-ATOM   9473  CD  ARG B 565      -0.355  25.602  15.136  1.00 48.13           C  
-ANISOU 9473  CD  ARG B 565     6186   5185   6917    834    424   1469       C  
-ATOM   9474  NE  ARG B 565      -0.450  26.603  16.197  1.00 46.59           N  
-ANISOU 9474  NE  ARG B 565     6030   4949   6723    832    539   1512       N  
-ATOM   9475  CZ  ARG B 565      -0.540  26.316  17.492  1.00 44.87           C  
-ANISOU 9475  CZ  ARG B 565     5866   4669   6512    851    534   1525       C  
-ATOM   9476  NH1 ARG B 565      -0.548  25.056  17.899  1.00 46.39           N  
-ANISOU 9476  NH1 ARG B 565     6087   4828   6711    878    425   1503       N  
-ATOM   9477  NH2 ARG B 565      -0.621  27.292  18.381  1.00 44.77           N  
-ANISOU 9477  NH2 ARG B 565     5890   4625   6496    845    645   1560       N  
-ATOM   9478  N   LYS B 566       4.446  28.229  13.213  1.00 50.04           N  
-ANISOU 9478  N   LYS B 566     6367   5585   7061    769    679    946       N  
-ATOM   9479  CA  LYS B 566       4.918  29.450  12.581  1.00 49.93           C  
-ANISOU 9479  CA  LYS B 566     6356   5577   7040    740    848    904       C  
-ATOM   9480  C   LYS B 566       6.119  29.158  11.703  1.00 49.47           C  
-ANISOU 9480  C   LYS B 566     6268   5549   6979    723    834    737       C  
-ATOM   9481  O   LYS B 566       6.204  29.641  10.573  1.00 49.32           O  
-ANISOU 9481  O   LYS B 566     6265   5535   6938    710    924    742       O  
-ATOM   9482  CB  LYS B 566       5.290  30.492  13.636  1.00 51.18           C  
-ANISOU 9482  CB  LYS B 566     6518   5710   7218    721    977    858       C  
-ATOM   9483  CG  LYS B 566       5.662  31.838  13.047  1.00 51.70           C  
-ANISOU 9483  CG  LYS B 566     6595   5764   7286    686   1186    828       C  
-ATOM   9484  CD  LYS B 566       6.046  32.827  14.125  1.00 53.31           C  
-ANISOU 9484  CD  LYS B 566     6796   5943   7518    659   1316    765       C  
-ATOM   9485  CE  LYS B 566       5.955  34.238  13.597  1.00 58.14           C  
-ANISOU 9485  CE  LYS B 566     7438   6520   8131    629   1552    803       C  
-ATOM   9486  NZ  LYS B 566       4.583  34.504  13.081  1.00 61.85           N  
-ANISOU 9486  NZ  LYS B 566     7959   6972   8571    661   1584   1030       N  
-ATOM   9487  N   LEU B 567       7.054  28.374  12.233  1.00 47.03           N  
-ANISOU 9487  N   LEU B 567     5923   5255   6690    731    725    588       N  
-ATOM   9488  CA  LEU B 567       8.211  27.946  11.459  1.00 45.68           C  
-ANISOU 9488  CA  LEU B 567     5715   5110   6530    716    696    418       C  
-ATOM   9489  C   LEU B 567       7.733  27.332  10.157  1.00 44.89           C  
-ANISOU 9489  C   LEU B 567     5632   5024   6400    718    641    490       C  
-ATOM   9490  O   LEU B 567       8.354  27.510   9.110  1.00 45.51           O  
-ANISOU 9490  O   LEU B 567     5710   5111   6472    696    702    410       O  
-ATOM   9491  CB  LEU B 567       9.035  26.921  12.238  1.00 45.17           C  
-ANISOU 9491  CB  LEU B 567     5610   5064   6487    747    542    281       C  
-ATOM   9492  CG  LEU B 567      10.330  26.467  11.568  1.00 43.97           C  
-ANISOU 9492  CG  LEU B 567     5408   4938   6362    734    510     84       C  
-ATOM   9493  CD1 LEU B 567      11.255  27.657  11.441  1.00 45.11           C  
-ANISOU 9493  CD1 LEU B 567     5520   5079   6542    688    684    -60       C  
-ATOM   9494  CD2 LEU B 567      11.004  25.350  12.340  1.00 42.26           C  
-ANISOU 9494  CD2 LEU B 567     5157   4740   6158    784    339    -28       C  
-ATOM   9495  N   LYS B 568       6.616  26.616  10.222  1.00 43.54           N  
-ANISOU 9495  N   LYS B 568     5478   4853   6212    744    533    636       N  
-ATOM   9496  CA  LYS B 568       6.069  25.983   9.034  1.00 46.30           C  
-ANISOU 9496  CA  LYS B 568     5835   5225   6533    748    466    699       C  
-ATOM   9497  C   LYS B 568       5.688  27.017   7.972  1.00 48.22           C  
-ANISOU 9497  C   LYS B 568     6116   5474   6732    742    603    773       C  
-ATOM   9498  O   LYS B 568       5.932  26.816   6.787  1.00 49.12           O  
-ANISOU 9498  O   LYS B 568     6243   5608   6811    739    600    740       O  
-ATOM   9499  CB  LYS B 568       4.861  25.114   9.378  1.00 46.57           C  
-ANISOU 9499  CB  LYS B 568     5869   5254   6571    771    342    832       C  
-ATOM   9500  CG  LYS B 568       4.340  24.344   8.183  1.00 47.88           C  
-ANISOU 9500  CG  LYS B 568     6028   5451   6713    773    256    869       C  
-ATOM   9501  CD  LYS B 568       3.075  23.581   8.501  1.00 48.40           C  
-ANISOU 9501  CD  LYS B 568     6082   5508   6800    787    157    990       C  
-ATOM   9502  CE  LYS B 568       2.576  22.842   7.266  1.00 50.41           C  
-ANISOU 9502  CE  LYS B 568     6317   5803   7032    784     70   1006       C  
-ATOM   9503  NZ  LYS B 568       1.273  22.164   7.511  1.00 55.25           N  
-ANISOU 9503  NZ  LYS B 568     6905   6407   7680    791    -11   1111       N  
-ATOM   9504  N   LYS B 569       5.082  28.121   8.398  1.00 41.51           N  
-ANISOU 9504  N   LYS B 569     3735   5962   6075   -553   -792   1688       N  
-ATOM   9505  CA  LYS B 569       4.676  29.164   7.463  1.00 43.35           C  
-ANISOU 9505  CA  LYS B 569     4101   6161   6210   -159   -242   1809       C  
-ATOM   9506  C   LYS B 569       5.900  29.869   6.896  1.00 41.00           C  
-ANISOU 9506  C   LYS B 569     4164   5372   6041   -114    100   1210       C  
-ATOM   9507  O   LYS B 569       5.882  30.351   5.771  1.00 40.99           O  
-ANISOU 9507  O   LYS B 569     4264   5262   6050     95    334   1202       O  
-ATOM   9508  CB  LYS B 569       3.740  30.173   8.132  1.00 49.46           C  
-ANISOU 9508  CB  LYS B 569     4876   7197   6719    193    335   2175       C  
-ATOM   9509  CG  LYS B 569       2.390  29.598   8.483  1.00 57.58           C  
-ANISOU 9509  CG  LYS B 569     5510   8780   7589    214     68   2859       C  
-ATOM   9510  CD  LYS B 569       1.376  30.691   8.757  1.00 66.41           C  
-ANISOU 9510  CD  LYS B 569     6630  10182   8421    666    686   3254       C  
-ATOM   9511  CE  LYS B 569       0.091  30.116   9.351  1.00 72.18           C  
-ANISOU 9511  CE  LYS B 569     6937  11516   8972    665    433   3937       C  
-ATOM   9512  NZ  LYS B 569       0.327  29.480  10.688  1.00 74.34           N  
-ANISOU 9512  NZ  LYS B 569     7089  11914   9241    375    135   3898       N  
-ATOM   9513  N   TRP B 570       6.964  29.931   7.683  1.00 48.24           N  
-ANISOU 9513  N   TRP B 570     5268   6005   7057   -316    128    721       N  
-ATOM   9514  CA  TRP B 570       8.197  30.515   7.195  1.00 45.13           C  
-ANISOU 9514  CA  TRP B 570     5186   5160   6801   -327    398    157       C  
-ATOM   9515  C   TRP B 570       8.740  29.680   6.048  1.00 43.67           C  
-ANISOU 9515  C   TRP B 570     4933   4867   6791   -485    -61    -27       C  
-ATOM   9516  O   TRP B 570       9.193  30.225   5.042  1.00 45.63           O  
-ANISOU 9516  O   TRP B 570     5345   4905   7086   -339    207   -220       O  
-ATOM   9517  CB  TRP B 570       9.235  30.624   8.305  1.00 41.43           C  
-ANISOU 9517  CB  TRP B 570     4900   4426   6414   -549    442   -317       C  
-ATOM   9518  CG  TRP B 570       9.007  31.790   9.208  1.00 42.52           C  
-ANISOU 9518  CG  TRP B 570     5244   4523   6387   -316   1038   -292       C  
-ATOM   9519  CD1 TRP B 570       7.856  32.513   9.345  1.00 44.03           C  
-ANISOU 9519  CD1 TRP B 570     5407   4977   6344     41   1429    163       C  
-ATOM   9520  CD2 TRP B 570       9.961  32.381  10.095  1.00 41.19           C  
-ANISOU 9520  CD2 TRP B 570     5358   4028   6265   -402   1296   -749       C  
-ATOM   9521  NE1 TRP B 570       8.033  33.514  10.271  1.00 43.81           N  
-ANISOU 9521  NE1 TRP B 570     5642   4800   6202    202   1907      6       N  
-ATOM   9522  CE2 TRP B 570       9.317  33.456  10.745  1.00 43.55           C  
-ANISOU 9522  CE2 TRP B 570     5809   4394   6345    -74   1829   -550       C  
-ATOM   9523  CE3 TRP B 570      11.296  32.105  10.406  1.00 41.48           C  
-ANISOU 9523  CE3 TRP B 570     5535   3725   6501   -715   1117  -1306       C  
-ATOM   9524  CZ2 TRP B 570       9.965  34.256  11.683  1.00 44.97           C  
-ANISOU 9524  CZ2 TRP B 570     6297   4287   6503    -52   2167   -896       C  
-ATOM   9525  CZ3 TRP B 570      11.937  32.896  11.342  1.00 43.99           C  
-ANISOU 9525  CZ3 TRP B 570     6136   3769   6808   -716   1460  -1635       C  
-ATOM   9526  CH2 TRP B 570      11.271  33.961  11.969  1.00 45.26           C  
-ANISOU 9526  CH2 TRP B 570     6464   3979   6752   -388   1972  -1432       C  
-ATOM   9527  N   VAL B 571       8.687  28.359   6.189  1.00 47.17           N  
-ANISOU 9527  N   VAL B 571     5144   5460   7320   -770   -764     41       N  
-ATOM   9528  CA  VAL B 571       9.210  27.476   5.151  1.00 44.73           C  
-ANISOU 9528  CA  VAL B 571     4784   5052   7161   -904  -1270   -152       C  
-ATOM   9529  C   VAL B 571       8.322  27.466   3.917  1.00 46.42           C  
-ANISOU 9529  C   VAL B 571     4883   5450   7306   -660  -1297    247       C  
-ATOM   9530  O   VAL B 571       8.811  27.521   2.796  1.00 46.93           O  
-ANISOU 9530  O   VAL B 571     5044   5352   7435   -566  -1289     37       O  
-ATOM   9531  CB  VAL B 571       9.377  26.034   5.650  1.00 41.41           C  
-ANISOU 9531  CB  VAL B 571     4171   4719   6845  -1273  -2070   -187       C  
-ATOM   9532  CG1 VAL B 571       9.709  25.118   4.499  1.00 38.53           C  
-ANISOU 9532  CG1 VAL B 571     3754   4292   6594  -1341  -2623   -312       C  
-ATOM   9533  CG2 VAL B 571      10.462  25.964   6.704  1.00 39.10           C  
-ANISOU 9533  CG2 VAL B 571     4014   4193   6649  -1528  -2092   -673       C  
-ATOM   9534  N   THR B 572       7.014  27.399   4.123  1.00 48.12           N  
-ANISOU 9534  N   THR B 572     4883   6022   7380   -550  -1328    831       N  
-ATOM   9535  CA  THR B 572       6.082  27.349   3.006  1.00 51.36           C  
-ANISOU 9535  CA  THR B 572     5162   6632   7722   -327  -1385   1252       C  
-ATOM   9536  C   THR B 572       6.130  28.638   2.179  1.00 52.66           C  
-ANISOU 9536  C   THR B 572     5549   6646   7812     40   -678   1185       C  
-ATOM   9537  O   THR B 572       5.678  28.666   1.034  1.00 52.74           O  
-ANISOU 9537  O   THR B 572     5521   6723   7796    235   -692   1387       O  
-ATOM   9538  CB  THR B 572       4.636  27.073   3.479  1.00 52.70           C  
-ANISOU 9538  CB  THR B 572     5030   7250   7743   -286  -1531   1930       C  
-ATOM   9539  OG1 THR B 572       4.183  28.154   4.302  1.00 55.99           O  
-ANISOU 9539  OG1 THR B 572     5510   7777   7987    -66   -886   2091       O  
-ATOM   9540  CG2 THR B 572       4.569  25.767   4.266  1.00 53.22           C  
-ANISOU 9540  CG2 THR B 572     4867   7469   7887   -675  -2266   2035       C  
-ATOM   9541  N   GLN B 573       6.676  29.702   2.762  1.00 45.86           N  
-ANISOU 9541  N   GLN B 573     4934   5572   6919    131    -81    907       N  
-ATOM   9542  CA  GLN B 573       6.836  30.966   2.046  1.00 49.70           C  
-ANISOU 9542  CA  GLN B 573     5669   5867   7349    447    584    808       C  
-ATOM   9543  C   GLN B 573       8.145  31.672   2.409  1.00 48.08           C  
-ANISOU 9543  C   GLN B 573     5771   5259   7239    364    946    235       C  
-ATOM   9544  O   GLN B 573       8.192  32.458   3.354  1.00 49.02           O  
-ANISOU 9544  O   GLN B 573     6043   5297   7286    418   1354    174       O  
-ATOM   9545  CB  GLN B 573       5.624  31.889   2.265  1.00 56.44           C  
-ANISOU 9545  CB  GLN B 573     6504   6958   7981    793   1083   1291       C  
-ATOM   9546  CG  GLN B 573       5.357  32.297   3.710  1.00 64.93           C  
-ANISOU 9546  CG  GLN B 573     7602   8129   8938    794   1321   1366       C  
-ATOM   9547  CD  GLN B 573       3.911  32.725   3.958  1.00 70.73           C  
-ANISOU 9547  CD  GLN B 573     8179   9264   9432   1103   1570   1970       C  
-ATOM   9548  OE1 GLN B 573       3.332  33.494   3.186  1.00 73.67           O  
-ANISOU 9548  OE1 GLN B 573     8619   9678   9693   1440   1959   2192       O  
-ATOM   9549  NE2 GLN B 573       3.320  32.219   5.040  1.00 75.60           N  
-ANISOU 9549  NE2 GLN B 573     8572  10194   9957    994   1342   2248       N  
-ATOM   9550  N   PRO B 574       9.221  31.377   1.661  1.00 49.95           N  
-ANISOU 9550  N   PRO B 574     6096   5251   7631    235    778   -183       N  
-ATOM   9551  CA  PRO B 574      10.506  32.051   1.863  1.00 50.64           C  
-ANISOU 9551  CA  PRO B 574     6455   4965   7820    145   1114   -710       C  
-ATOM   9552  C   PRO B 574      10.389  33.517   1.467  1.00 53.19           C  
-ANISOU 9552  C   PRO B 574     7028   5132   8051    455   1848   -660       C  
-ATOM   9553  O   PRO B 574       9.505  33.863   0.687  1.00 53.74           O  
-ANISOU 9553  O   PRO B 574     7054   5358   8006    738   2031   -293       O  
-ATOM   9554  CB  PRO B 574      11.445  31.316   0.902  1.00 46.32           C  
-ANISOU 9554  CB  PRO B 574     5877   4301   7421      5    731  -1047       C  
-ATOM   9555  CG  PRO B 574      10.744  30.041   0.551  1.00 46.54           C  
-ANISOU 9555  CG  PRO B 574     5627   4612   7444    -60     63   -762       C  
-ATOM   9556  CD  PRO B 574       9.294  30.362   0.598  1.00 51.06           C  
-ANISOU 9556  CD  PRO B 574     6079   5468   7852    173    235   -178       C  
-ATOM   9557  N   LEU B 575      11.267  34.365   1.991  1.00 51.28           N  
-ANISOU 9557  N   LEU B 575     7052   4574   7859    398   2241  -1019       N  
-ATOM   9558  CA  LEU B 575      11.150  35.806   1.784  1.00 57.23           C  
-ANISOU 9558  CA  LEU B 575     8080   5143   8521    675   2922   -970       C  
-ATOM   9559  C   LEU B 575      11.826  36.291   0.501  1.00 62.10           C  
-ANISOU 9559  C   LEU B 575     8825   5557   9212    753   3150  -1149       C  
-ATOM   9560  O   LEU B 575      12.803  35.703   0.041  1.00 62.42           O  
-ANISOU 9560  O   LEU B 575     8817   5500   9399    542   2870  -1479       O  
-ATOM   9561  CB  LEU B 575      11.709  36.559   2.994  1.00 54.45           C  
-ANISOU 9561  CB  LEU B 575     7981   4529   8177    589   3233  -1240       C  
-ATOM   9562  CG  LEU B 575      11.091  36.181   4.345  1.00 51.09           C  
-ANISOU 9562  CG  LEU B 575     7451   4305   7656    536   3060  -1078       C  
-ATOM   9563  CD1 LEU B 575      11.776  36.938   5.474  1.00 50.88           C  
-ANISOU 9563  CD1 LEU B 575     7710   3978   7644    458   3355  -1403       C  
-ATOM   9564  CD2 LEU B 575       9.585  36.426   4.353  1.00 46.31           C  
-ANISOU 9564  CD2 LEU B 575     6725   4046   6823    872   3217   -512       C  
-ATOM   9565  N   LEU B 576      11.291  37.361  -0.078  1.00 66.65           N  
-ANISOU 9565  N   LEU B 576     9561   6089   9673   1071   3656   -921       N  
-ATOM   9566  CA  LEU B 576      11.905  37.986  -1.244  1.00 73.01           C  
-ANISOU 9566  CA  LEU B 576    10514   6695  10531   1160   3946  -1060       C  
-ATOM   9567  C   LEU B 576      12.580  39.297  -0.849  1.00 78.55           C  
-ANISOU 9567  C   LEU B 576    11571   7019  11255   1169   4490  -1292       C  
-ATOM   9568  O   LEU B 576      13.526  39.739  -1.498  1.00 79.51           O  
-ANISOU 9568  O   LEU B 576    11826   6905  11480   1095   4673  -1546       O  
-ATOM   9569  CB  LEU B 576      10.866  38.239  -2.340  1.00 74.13           C  
-ANISOU 9569  CB  LEU B 576    10590   7038  10537   1506   4099   -636       C  
-ATOM   9570  CG  LEU B 576      10.195  37.019  -2.972  1.00 75.41           C  
-ANISOU 9570  CG  LEU B 576    10425   7547  10681   1521   3563   -383       C  
-ATOM   9571  CD1 LEU B 576       9.085  37.442  -3.916  1.00 74.97           C  
-ANISOU 9571  CD1 LEU B 576    10336   7674  10475   1886   3783     62       C  
-ATOM   9572  CD2 LEU B 576      11.215  36.164  -3.696  1.00 78.33           C  
-ANISOU 9572  CD2 LEU B 576    10696   7865  11199   1313   3163   -718       C  
-ATOM   9573  N   LYS B 577      12.089  39.910   0.223  1.00 84.62           N  
-ANISOU 9573  N   LYS B 577    12492   7738  11920   1265   4731  -1194       N  
-ATOM   9574  CA  LYS B 577      12.606  41.192   0.686  1.00 90.28           C  
-ANISOU 9574  CA  LYS B 577    13584   8079  12638   1303   5222  -1386       C  
-ATOM   9575  C   LYS B 577      13.963  41.041   1.362  1.00 89.32           C  
-ANISOU 9575  C   LYS B 577    13558   7674  12706    925   5090  -1878       C  
-ATOM   9576  O   LYS B 577      14.062  40.474   2.449  1.00 88.29           O  
-ANISOU 9576  O   LYS B 577    13357   7591  12598    745   4822  -2003       O  
-ATOM   9577  CB  LYS B 577      11.620  41.828   1.665  1.00 98.01           C  
-ANISOU 9577  CB  LYS B 577    14700   9119  13421   1560   5477  -1134       C  
-ATOM   9578  CG  LYS B 577      10.171  41.399   1.459  1.00106.28           C  
-ANISOU 9578  CG  LYS B 577    15494  10605  14281   1838   5369   -631       C  
-ATOM   9579  CD  LYS B 577       9.395  42.347   0.544  1.00116.10           C  
-ANISOU 9579  CD  LYS B 577    16871  11864  15377   2235   5801   -309       C  
-ATOM   9580  CE  LYS B 577       9.762  42.192  -0.931  1.00120.94           C  
-ANISOU 9580  CE  LYS B 577    17411  12448  16093   2216   5767   -327       C  
-ATOM   9581  NZ  LYS B 577      11.037  42.870  -1.293  1.00127.70           N  
-ANISOU 9581  NZ  LYS B 577    18530  12888  17102   2050   6004   -711       N  
-ATOM   9582  N   LEU B 578      15.005  41.558   0.719  1.00 75.15           N  
-ANISOU 9582  N   LEU B 578    11912   5599  11041    800   5277  -2137       N  
-ATOM   9583  CA  LEU B 578      16.350  41.490   1.276  1.00 76.18           C  
-ANISOU 9583  CA  LEU B 578    12067   5547  11331    359   5126  -2480       C  
-ATOM   9584  C   LEU B 578      16.384  42.116   2.666  1.00 78.83           C  
-ANISOU 9584  C   LEU B 578    12635   5691  11626    297   5279  -2554       C  
-ATOM   9585  O   LEU B 578      17.073  41.631   3.564  1.00 78.09           O  
-ANISOU 9585  O   LEU B 578    12460   5595  11617    -18   5011  -2782       O  
-ATOM   9586  CB  LEU B 578      17.352  42.200   0.364  1.00 76.91           C  
-ANISOU 9586  CB  LEU B 578    12260   5441  11520    224   5368  -2584       C  
-ATOM   9587  CG  LEU B 578      18.810  42.147   0.828  1.00 77.00           C  
-ANISOU 9587  CG  LEU B 578    12234   5330  11692   -216   5242  -2914       C  
-ATOM   9588  CD1 LEU B 578      19.384  40.756   0.647  1.00 75.10           C  
-ANISOU 9588  CD1 LEU B 578    11619   5372  11542   -446   4716  -3088       C  
-ATOM   9589  CD2 LEU B 578      19.644  43.164   0.080  1.00 78.07           C  
-ANISOU 9589  CD2 LEU B 578    12547   5216  11900   -287   5607  -2975       C  
-ATOM   9590  N   ARG B 579      15.636  43.201   2.829  1.00 83.69           N  
-ANISOU 9590  N   ARG B 579    13537   6166  12095    621   5706  -2353       N  
-ATOM   9591  CA  ARG B 579      15.545  43.887   4.110  1.00 86.90           C  
-ANISOU 9591  CA  ARG B 579    14211   6385  12422    650   5876  -2406       C  
-ATOM   9592  C   ARG B 579      15.342  42.902   5.259  1.00 83.29           C  
-ANISOU 9592  C   ARG B 579    13570   6125  11951    540   5504  -2498       C  
-ATOM   9593  O   ARG B 579      16.098  42.902   6.231  1.00 82.78           O  
-ANISOU 9593  O   ARG B 579    13567   5930  11954    256   5387  -2730       O  
-ATOM   9594  CB  ARG B 579      14.400  44.901   4.086  1.00 93.36           C  
-ANISOU 9594  CB  ARG B 579    15288   7163  13022   1136   6307  -2108       C  
-ATOM   9595  CG  ARG B 579      14.543  45.973   3.024  1.00102.78           C  
-ANISOU 9595  CG  ARG B 579    16709   8127  14215   1264   6694  -2003       C  
-ATOM   9596  CD  ARG B 579      14.920  47.315   3.633  1.00113.14           C  
-ANISOU 9596  CD  ARG B 579    18472   9021  15494   1280   7038  -2097       C  
-ATOM   9597  NE  ARG B 579      13.891  47.809   4.543  1.00120.95           N  
-ANISOU 9597  NE  ARG B 579    19664  10038  16252   1662   7217  -1936       N  
-ATOM   9598  CZ  ARG B 579      14.106  48.117   5.817  1.00125.79           C  
-ANISOU 9598  CZ  ARG B 579    20487  10486  16820   1608   7205  -2100       C  
-ATOM   9599  NH1 ARG B 579      15.318  47.989   6.337  1.00128.24           N  
-ANISOU 9599  NH1 ARG B 579    20822  10592  17312   1163   7021  -2418       N  
-ATOM   9600  NH2 ARG B 579      13.110  48.561   6.571  1.00129.37           N  
-ANISOU 9600  NH2 ARG B 579    21114  11010  17030   2016   7381  -1937       N  
-ATOM   9601  N   GLU B 580      14.327  42.053   5.136  1.00104.44           N  
-ANISOU 9601  N   GLU B 580    17948   8912  12822  -1745   4005   -587       N  
-ATOM   9602  CA  GLU B 580      13.932  41.179   6.238  1.00100.63           C  
-ANISOU 9602  CA  GLU B 580    17113   8717  12405  -1640   3703   -450       C  
-ATOM   9603  C   GLU B 580      14.749  39.887   6.321  1.00 96.40           C  
-ANISOU 9603  C   GLU B 580    16300   8453  11873  -1712   3358   -612       C  
-ATOM   9604  O   GLU B 580      14.956  39.352   7.407  1.00 95.26           O  
-ANISOU 9604  O   GLU B 580    15864   8590  11742  -1721   3223   -692       O  
-ATOM   9605  CB  GLU B 580      12.431  40.869   6.169  1.00102.98           C  
-ANISOU 9605  CB  GLU B 580    17392   8932  12802  -1369   3465     59       C  
-ATOM   9606  CG  GLU B 580      11.866  40.167   7.402  1.00106.18           C  
-ANISOU 9606  CG  GLU B 580    17466   9601  13278  -1247   3214    224       C  
-ATOM   9607  CD  GLU B 580      11.833  41.050   8.647  1.00110.68           C  
-ANISOU 9607  CD  GLU B 580    17992  10236  13824  -1293   3524     97       C  
-ATOM   9608  OE1 GLU B 580      12.257  42.225   8.580  1.00114.31           O  
-ANISOU 9608  OE1 GLU B 580    18678  10542  14212  -1425   3945   -127       O  
-ATOM   9609  OE2 GLU B 580      11.373  40.560   9.701  1.00112.55           O  
-ANISOU 9609  OE2 GLU B 580    17971  10679  14115  -1200   3348    221       O  
-ATOM   9610  N   ILE B 581      15.212  39.387   5.179  1.00 71.13           N  
-ANISOU 9610  N   ILE B 581    13196   5171   8661  -1762   3220   -656       N  
-ATOM   9611  CA  ILE B 581      16.032  38.178   5.165  1.00 66.95           C  
-ANISOU 9611  CA  ILE B 581    12424   4881   8132  -1834   2909   -816       C  
-ATOM   9612  C   ILE B 581      17.321  38.383   5.953  1.00 68.41           C  
-ANISOU 9612  C   ILE B 581    12472   5282   8239  -2055   3100  -1287       C  
-ATOM   9613  O   ILE B 581      17.699  37.546   6.771  1.00 67.75           O  
-ANISOU 9613  O   ILE B 581    12081   5495   8167  -2065   2879  -1377       O  
-ATOM   9614  CB  ILE B 581      16.359  37.723   3.739  1.00 61.99           C  
-ANISOU 9614  CB  ILE B 581    11958   4099   7498  -1869   2775   -806       C  
-ATOM   9615  CG1 ILE B 581      15.070  37.343   3.012  1.00 59.50           C  
-ANISOU 9615  CG1 ILE B 581    11731   3616   7260  -1643   2526   -327       C  
-ATOM   9616  CG2 ILE B 581      17.319  36.549   3.765  1.00 57.48           C  
-ANISOU 9616  CG2 ILE B 581    11144   3776   6921  -1963   2497  -1013       C  
-ATOM   9617  CD1 ILE B 581      15.291  36.736   1.646  1.00 55.71           C  
-ANISOU 9617  CD1 ILE B 581    11380   3006   6781  -1660   2338   -275       C  
-ATOM   9618  N   ASN B 582      17.990  39.503   5.708  1.00 86.50           N  
-ANISOU 9618  N   ASN B 582    14994   7425  10448  -2232   3515  -1587       N  
-ATOM   9619  CA  ASN B 582      19.140  39.878   6.514  1.00 88.76           C  
-ANISOU 9619  CA  ASN B 582    15168   7903  10653  -2448   3749  -2035       C  
-ATOM   9620  C   ASN B 582      18.750  39.941   7.985  1.00 87.26           C  
-ANISOU 9620  C   ASN B 582    14742   7932  10480  -2388   3752  -1993       C  
-ATOM   9621  O   ASN B 582      19.498  39.491   8.851  1.00 87.24           O  
-ANISOU 9621  O   ASN B 582    14476   8225  10448  -2483   3680  -2239       O  
-ATOM   9622  CB  ASN B 582      19.707  41.223   6.060  1.00 94.48           C  
-ANISOU 9622  CB  ASN B 582    16211   8399  11289  -2629   4235  -2319       C  
-ATOM   9623  CG  ASN B 582      20.323  41.160   4.675  1.00 97.07           C  
-ANISOU 9623  CG  ASN B 582    16759   8539  11586  -2728   4256  -2442       C  
-ATOM   9624  OD1 ASN B 582      21.082  40.243   4.361  1.00 97.78           O  
-ANISOU 9624  OD1 ASN B 582    16703   8776  11674  -2799   4022  -2590       O  
-ATOM   9625  ND2 ASN B 582      19.996  42.137   3.838  1.00100.04           N  
-ANISOU 9625  ND2 ASN B 582    17491   8583  11935  -2731   4540  -2380       N  
-ATOM   9626  N   ALA B 583      17.569  40.484   8.262  1.00 90.85           N  
-ANISOU 9626  N   ALA B 583    15291   8245  10983  -2226   3830  -1674       N  
-ATOM   9627  CA  ALA B 583      17.074  40.578   9.632  1.00 89.05           C  
-ANISOU 9627  CA  ALA B 583    14859   8197  10779  -2155   3837  -1596       C  
-ATOM   9628  C   ALA B 583      17.112  39.225  10.336  1.00 85.70           C  
-ANISOU 9628  C   ALA B 583    14062   8096  10403  -2076   3410  -1526       C  
-ATOM   9629  O   ALA B 583      17.876  39.032  11.284  1.00 85.59           O  
-ANISOU 9629  O   ALA B 583    13824   8353  10344  -2191   3424  -1803       O  
-ATOM   9630  CB  ALA B 583      15.663  41.150   9.651  1.00 90.30           C  
-ANISOU 9630  CB  ALA B 583    15166   8140  11003  -1954   3905  -1193       C  
-ATOM   9631  N   ARG B 584      16.284  38.295   9.866  1.00 77.33           N  
-ANISOU 9631  N   ARG B 584    12942   7010   9431  -1880   3037  -1156       N  
-ATOM   9632  CA  ARG B 584      16.250  36.943  10.413  1.00 73.50           C  
-ANISOU 9632  CA  ARG B 584    12125   6807   8996  -1789   2615  -1057       C  
-ATOM   9633  C   ARG B 584      17.658  36.380  10.567  1.00 75.36           C  
-ANISOU 9633  C   ARG B 584    12186   7285   9164  -1973   2556  -1457       C  
-ATOM   9634  O   ARG B 584      17.997  35.802  11.598  1.00 75.73           O  
-ANISOU 9634  O   ARG B 584    11946   7625   9203  -1983   2416  -1564       O  
-ATOM   9635  CB  ARG B 584      15.423  36.017   9.520  1.00 66.84           C  
-ANISOU 9635  CB  ARG B 584    11295   5865   8237  -1602   2245   -671       C  
-ATOM   9636  CG  ARG B 584      13.929  36.296   9.524  1.00 59.50           C  
-ANISOU 9636  CG  ARG B 584    10456   4765   7388  -1385   2208   -230       C  
-ATOM   9637  CD  ARG B 584      13.173  35.250   8.721  1.00 51.33           C  
-ANISOU 9637  CD  ARG B 584     9392   3680   6432  -1211   1811    131       C  
-ATOM   9638  NE  ARG B 584      11.744  35.544   8.639  1.00 45.58           N  
-ANISOU 9638  NE  ARG B 584     8759   2781   5777  -1004   1779    552       N  
-ATOM   9639  CZ  ARG B 584      10.891  34.916   7.832  1.00 43.79           C  
-ANISOU 9639  CZ  ARG B 584     8573   2449   5618   -845   1501    905       C  
-ATOM   9640  NH1 ARG B 584      11.318  33.954   7.021  1.00 42.79           N  
-ANISOU 9640  NH1 ARG B 584     8409   2359   5491   -870   1233    891       N  
-ATOM   9641  NH2 ARG B 584       9.608  35.260   7.825  1.00 40.29           N  
-ANISOU 9641  NH2 ARG B 584     8209   1862   5238   -661   1496   1271       N  
-ATOM   9642  N   LEU B 585      18.474  36.548   9.533  1.00 69.10           N  
-ANISOU 9642  N   LEU B 585    11567   6367   8321  -2115   2664  -1676       N  
-ATOM   9643  CA  LEU B 585      19.849  36.065   9.563  1.00 71.85           C  
-ANISOU 9643  CA  LEU B 585    11771   6924   8605  -2298   2627  -2068       C  
-ATOM   9644  C   LEU B 585      20.666  36.726  10.674  1.00 75.32           C  
-ANISOU 9644  C   LEU B 585    12099   7559   8962  -2470   2911  -2446       C  
-ATOM   9645  O   LEU B 585      21.361  36.051  11.427  1.00 76.43           O  
-ANISOU 9645  O   LEU B 585    11959   8005   9076  -2524   2761  -2640       O  
-ATOM   9646  CB  LEU B 585      20.518  36.274   8.202  1.00 70.66           C  
-ANISOU 9646  CB  LEU B 585    11866   6565   8417  -2425   2737  -2231       C  
-ATOM   9647  CG  LEU B 585      20.221  35.207   7.149  1.00 67.99           C  
-ANISOU 9647  CG  LEU B 585    11539   6154   8142  -2313   2373  -1984       C  
-ATOM   9648  CD1 LEU B 585      20.503  35.722   5.750  1.00 67.73           C  
-ANISOU 9648  CD1 LEU B 585    11834   5821   8080  -2404   2545  -2051       C  
-ATOM   9649  CD2 LEU B 585      21.025  33.953   7.440  1.00 65.12           C  
-ANISOU 9649  CD2 LEU B 585    10875   6091   7778  -2348   2061  -2133       C  
-ATOM   9650  N   ASP B 586      20.573  38.047  10.777  1.00 91.56           N  
-ANISOU 9650  N   ASP B 586    14377   9439  10973  -2555   3323  -2549       N  
-ATOM   9651  CA  ASP B 586      21.339  38.788  11.775  1.00 95.48           C  
-ANISOU 9651  CA  ASP B 586    14799  10097  11382  -2736   3633  -2918       C  
-ATOM   9652  C   ASP B 586      20.985  38.341  13.189  1.00 92.65           C  
-ANISOU 9652  C   ASP B 586    14133  10021  11047  -2645   3472  -2833       C  
-ATOM   9653  O   ASP B 586      21.832  38.336  14.082  1.00 92.58           O  
-ANISOU 9653  O   ASP B 586    13929  10277  10971  -2781   3543  -3150       O  
-ATOM   9654  CB  ASP B 586      21.108  40.291  11.620  1.00103.14           C  
-ANISOU 9654  CB  ASP B 586    16083  10796  12308  -2816   4104  -2982       C  
-ATOM   9655  CG  ASP B 586      21.380  40.778  10.209  1.00109.51           C  
-ANISOU 9655  CG  ASP B 586    17218  11301  13091  -2894   4275  -3044       C  
-ATOM   9656  OD1 ASP B 586      22.138  40.102   9.479  1.00111.57           O  
-ANISOU 9656  OD1 ASP B 586    17446  11605  13339  -2967   4110  -3188       O  
-ATOM   9657  OD2 ASP B 586      20.826  41.832   9.828  1.00114.61           O  
-ANISOU 9657  OD2 ASP B 586    18155  11661  13729  -2878   4575  -2944       O  
-ATOM   9658  N   ALA B 587      19.728  37.961  13.379  1.00 78.28           N  
-ANISOU 9658  N   ALA B 587    12273   8148   9321  -2414   3252  -2404       N  
-ATOM   9659  CA  ALA B 587      19.263  37.446  14.659  1.00 76.71           C  
-ANISOU 9659  CA  ALA B 587    11791   8198   9157  -2302   3064  -2274       C  
-ATOM   9660  C   ALA B 587      19.886  36.086  14.974  1.00 74.51           C  
-ANISOU 9660  C   ALA B 587    11195   8234   8880  -2289   2684  -2356       C  
-ATOM   9661  O   ALA B 587      20.381  35.865  16.075  1.00 75.81           O  
-ANISOU 9661  O   ALA B 587    11116   8684   9003  -2345   2661  -2546       O  
-ATOM   9662  CB  ALA B 587      17.749  37.355  14.670  1.00 79.25           C  
-ANISOU 9662  CB  ALA B 587    12163   8366   9584  -2057   2919  -1788       C  
-ATOM   9663  N   VAL B 588      19.857  35.172  14.009  1.00 67.08           N  
-ANISOU 9663  N   VAL B 588    10259   7241   7986  -2212   2389  -2210       N  
-ATOM   9664  CA  VAL B 588      20.500  33.875  14.188  1.00 65.69           C  
-ANISOU 9664  CA  VAL B 588     9806   7343   7810  -2203   2041  -2294       C  
-ATOM   9665  C   VAL B 588      21.980  34.061  14.496  1.00 68.43           C  
-ANISOU 9665  C   VAL B 588    10056   7894   8051  -2437   2211  -2790       C  
-ATOM   9666  O   VAL B 588      22.535  33.382  15.357  1.00 70.12           O  
-ANISOU 9666  O   VAL B 588     9984   8422   8236  -2454   2049  -2937       O  
-ATOM   9667  CB  VAL B 588      20.370  32.982  12.942  1.00 61.02           C  
-ANISOU 9667  CB  VAL B 588     9280   6630   7273  -2121   1752  -2106       C  
-ATOM   9668  CG1 VAL B 588      21.098  31.666  13.165  1.00 58.18           C  
-ANISOU 9668  CG1 VAL B 588     8635   6562   6908  -2119   1416  -2214       C  
-ATOM   9669  CG2 VAL B 588      18.913  32.735  12.611  1.00 60.35           C  
-ANISOU 9669  CG2 VAL B 588     9279   6362   7291  -1891   1563  -1617       C  
-ATOM   9670  N   SER B 589      22.615  34.987  13.786  1.00 78.29           N  
-ANISOU 9670  N   SER B 589    11545   8964   9239  -2617   2541  -3048       N  
-ATOM   9671  CA  SER B 589      24.018  35.294  14.021  1.00 83.50           C  
-ANISOU 9671  CA  SER B 589    12138   9796   9794  -2856   2745  -3536       C  
-ATOM   9672  C   SER B 589      24.220  35.695  15.474  1.00 84.80           C  
-ANISOU 9672  C   SER B 589    12111  10207   9902  -2917   2890  -3712       C  
-ATOM   9673  O   SER B 589      25.168  35.263  16.124  1.00 86.79           O  
-ANISOU 9673  O   SER B 589    12120  10763  10093  -3017   2826  -4000       O  
-ATOM   9674  CB  SER B 589      24.483  36.430  13.106  1.00 88.43           C  
-ANISOU 9674  CB  SER B 589    13089  10149  10362  -3034   3135  -3758       C  
-ATOM   9675  OG  SER B 589      24.357  36.078  11.738  1.00 92.45           O  
-ANISOU 9675  OG  SER B 589    13782  10428  10915  -2990   3011  -3614       O  
-ATOM   9676  N   GLU B 590      23.310  36.518  15.983  1.00 81.44           N  
-ANISOU 9676  N   GLU B 590    11795   9652   9497  -2853   3084  -3534       N  
-ATOM   9677  CA  GLU B 590      23.439  37.056  17.331  1.00 83.97           C  
-ANISOU 9677  CA  GLU B 590    11975  10169   9762  -2923   3271  -3698       C  
-ATOM   9678  C   GLU B 590      23.153  36.001  18.398  1.00 82.69           C  
-ANISOU 9678  C   GLU B 590    11474  10312   9634  -2778   2919  -3550       C  
-ATOM   9679  O   GLU B 590      23.758  36.016  19.470  1.00 84.11           O  
-ANISOU 9679  O   GLU B 590    11442  10771   9745  -2872   2970  -3796       O  
-ATOM   9680  CB  GLU B 590      22.526  38.269  17.513  1.00 85.96           C  
-ANISOU 9680  CB  GLU B 590    12462  10169  10028  -2896   3596  -3541       C  
-ATOM   9681  CG  GLU B 590      22.818  39.076  18.760  1.00 92.08           C  
-ANISOU 9681  CG  GLU B 590    13157  11103  10727  -3025   3888  -3781       C  
-ATOM   9682  CD  GLU B 590      22.114  40.415  18.752  1.00 93.65           C  
-ANISOU 9682  CD  GLU B 590    13640  11018  10926  -3040   4281  -3692       C  
-ATOM   9683  OE1 GLU B 590      21.252  40.631  17.872  1.00 96.11           O  
-ANISOU 9683  OE1 GLU B 590    14185  11025  11308  -2912   4282  -3389       O  
-ATOM   9684  OE2 GLU B 590      22.426  41.253  19.624  1.00 91.91           O  
-ANISOU 9684  OE2 GLU B 590    13409  10880  10631  -3181   4590  -3925       O  
-ATOM   9685  N   VAL B 591      22.232  35.089  18.102  1.00 75.26           N  
-ANISOU 9685  N   VAL B 591    10483   9317   8796  -2553   2566  -3150       N  
-ATOM   9686  CA  VAL B 591      21.917  34.001  19.020  1.00 74.66           C  
-ANISOU 9686  CA  VAL B 591    10098   9511   8757  -2401   2211  -2986       C  
-ATOM   9687  C   VAL B 591      23.055  32.986  19.057  1.00 76.02           C  
-ANISOU 9687  C   VAL B 591    10031   9971   8882  -2469   1978  -3236       C  
-ATOM   9688  O   VAL B 591      23.361  32.421  20.106  1.00 75.05           O  
-ANISOU 9688  O   VAL B 591     9632  10156   8729  -2450   1831  -3322       O  
-ATOM   9689  CB  VAL B 591      20.613  33.281  18.626  1.00 71.02           C  
-ANISOU 9689  CB  VAL B 591     9660   8906   8419  -2146   1899  -2490       C  
-ATOM   9690  CG1 VAL B 591      20.400  32.056  19.499  1.00 69.20           C  
-ANISOU 9690  CG1 VAL B 591     9110   8960   8221  -1999   1519  -2345       C  
-ATOM   9691  CG2 VAL B 591      19.430  34.232  18.729  1.00 71.23           C  
-ANISOU 9691  CG2 VAL B 591     9889   8680   8497  -2058   2108  -2224       C  
-ATOM   9692  N   LEU B 592      23.687  32.767  17.908  1.00 76.37           N  
-ANISOU 9692  N   LEU B 592    10187   9913   8917  -2545   1952  -3354       N  
-ATOM   9693  CA  LEU B 592      24.767  31.792  17.801  1.00 81.31           C  
-ANISOU 9693  CA  LEU B 592    10606  10785   9504  -2604   1732  -3581       C  
-ATOM   9694  C   LEU B 592      26.021  32.223  18.545  1.00 89.53           C  
-ANISOU 9694  C   LEU B 592    11507  12084  10426  -2819   1949  -4053       C  
-ATOM   9695  O   LEU B 592      26.613  31.437  19.283  1.00 89.57           O  
-ANISOU 9695  O   LEU B 592    11224  12412  10395  -2813   1750  -4184       O  
-ATOM   9696  CB  LEU B 592      25.118  31.535  16.337  1.00 76.64           C  
-ANISOU 9696  CB  LEU B 592    10193   9994   8934  -2644   1680  -3594       C  
-ATOM   9697  CG  LEU B 592      24.187  30.607  15.565  1.00 70.84           C  
-ANISOU 9697  CG  LEU B 592     9500   9110   8306  -2434   1337  -3171       C  
-ATOM   9698  CD1 LEU B 592      24.552  30.599  14.090  1.00 68.35           C  
-ANISOU 9698  CD1 LEU B 592     9407   8562   8000  -2505   1361  -3215       C  
-ATOM   9699  CD2 LEU B 592      24.237  29.201  16.148  1.00 67.66           C  
-ANISOU 9699  CD2 LEU B 592     8782   8995   7930  -2300    931  -3065       C  
-ATOM   9700  N   HIS B 593      26.425  33.472  18.339  1.00 97.71           N  
-ANISOU 9700  N   HIS B 593    12749  12977  11398  -3009   2359  -4308       N  
-ATOM   9701  CA  HIS B 593      27.696  33.959  18.858  1.00107.83           C  
-ANISOU 9701  CA  HIS B 593    13932  14478  12562  -3244   2597  -4789       C  
-ATOM   9702  C   HIS B 593      27.553  34.619  20.227  1.00112.05           C  
-ANISOU 9702  C   HIS B 593    14356  15176  13041  -3288   2790  -4882       C  
-ATOM   9703  O   HIS B 593      28.158  34.170  21.202  1.00111.69           O  
-ANISOU 9703  O   HIS B 593    14029  15471  12936  -3322   2687  -5068       O  
-ATOM   9704  CB  HIS B 593      28.333  34.939  17.869  1.00116.78           C  
-ANISOU 9704  CB  HIS B 593    15348  15379  13645  -3450   2951  -5057       C  
-ATOM   9705  CG  HIS B 593      28.358  34.440  16.457  1.00125.04           C  
-ANISOU 9705  CG  HIS B 593    16551  16211  14747  -3409   2801  -4942       C  
-ATOM   9706  ND1 HIS B 593      28.119  35.259  15.376  1.00129.63           N  
-ANISOU 9706  ND1 HIS B 593    17476  16436  15343  -3467   3043  -4907       N  
-ATOM   9707  CD2 HIS B 593      28.593  33.207  15.952  1.00127.38           C  
-ANISOU 9707  CD2 HIS B 593    16713  16597  15087  -3318   2438  -4853       C  
-ATOM   9708  CE1 HIS B 593      28.202  34.551  14.263  1.00131.83           C  
-ANISOU 9708  CE1 HIS B 593    17824  16596  15671  -3415   2831  -4802       C  
-ATOM   9709  NE2 HIS B 593      28.490  33.301  14.587  1.00131.34           N  
-ANISOU 9709  NE2 HIS B 593    17475  16800  15629  -3328   2464  -4768       N  
-ATOM   9710  N   SER B 594      26.755  35.682  20.287  1.00113.38           N  
-ANISOU 9710  N   SER B 594    14752  15101  13227  -3287   3072  -4751       N  
-ATOM   9711  CA  SER B 594      26.641  36.513  21.485  1.00119.31           C  
-ANISOU 9711  CA  SER B 594    15453  15959  13919  -3362   3329  -4866       C  
-ATOM   9712  C   SER B 594      26.846  35.720  22.774  1.00123.19           C  
-ANISOU 9712  C   SER B 594    15585  16837  14383  -3304   3088  -4904       C  
-ATOM   9713  O   SER B 594      26.239  34.667  22.973  1.00123.43           O  
-ANISOU 9713  O   SER B 594    15457  16951  14489  -3095   2715  -4602       O  
-ATOM   9714  CB  SER B 594      25.295  37.242  21.510  1.00118.32           C  
-ANISOU 9714  CB  SER B 594    15546  15543  13868  -3237   3474  -4518       C  
-ATOM   9715  OG  SER B 594      25.219  38.146  22.599  1.00116.52           O  
-ANISOU 9715  OG  SER B 594    15302  15391  13581  -3330   3765  -4647       O  
-ATOM   9716  N   GLU B 595      27.710  36.235  23.644  1.00130.78           N  
-ANISOU 9716  N   GLU B 595    16424  18035  15232  -3494   3307  -5280       N  
-ATOM   9717  CA  GLU B 595      28.065  35.544  24.879  1.00133.56           C  
-ANISOU 9717  CA  GLU B 595    16433  18777  15537  -3466   3105  -5372       C  
-ATOM   9718  C   GLU B 595      27.092  35.868  26.005  1.00130.99           C  
-ANISOU 9718  C   GLU B 595    16061  18473  15235  -3365   3148  -5153       C  
-ATOM   9719  O   GLU B 595      26.931  35.085  26.943  1.00128.55           O  
-ANISOU 9719  O   GLU B 595    15492  18422  14931  -3249   2887  -5056       O  
-ATOM   9720  CB  GLU B 595      29.485  35.916  25.310  1.00141.53           C  
-ANISOU 9720  CB  GLU B 595    17314  20055  16406  -3722   3311  -5889       C  
-ATOM   9721  CG  GLU B 595      30.521  35.818  24.206  1.00149.28           C  
-ANISOU 9721  CG  GLU B 595    18370  20997  17354  -3862   3349  -6159       C  
-ATOM   9722  CD  GLU B 595      31.143  37.161  23.887  1.00156.93           C  
-ANISOU 9722  CD  GLU B 595    19562  21826  18237  -4124   3827  -6509       C  
-ATOM   9723  OE1 GLU B 595      30.542  38.192  24.259  1.00160.62           O  
-ANISOU 9723  OE1 GLU B 595    20199  22134  18697  -4165   4125  -6457       O  
-ATOM   9724  OE2 GLU B 595      32.231  37.188  23.272  1.00161.10           O  
-ANISOU 9724  OE2 GLU B 595    20038  22401  18770  -4304   3891  -6748       O  
-ATOM   9725  N   SER B 596      26.452  37.029  25.907  1.00140.42           N  
-ANISOU 9725  N   SER B 596    17515  19394  16443  -3409   3484  -5079       N  
-ATOM   9726  CA  SER B 596      25.518  37.485  26.930  1.00135.65           C  
-ANISOU 9726  CA  SER B 596    16901  18776  15863  -3331   3577  -4883       C  
-ATOM   9727  C   SER B 596      24.588  36.365  27.384  1.00129.34           C  
-ANISOU 9727  C   SER B 596    15919  18063  15163  -3062   3159  -4485       C  
-ATOM   9728  O   SER B 596      24.091  35.586  26.571  1.00127.02           O  
-ANISOU 9728  O   SER B 596    15660  17641  14962  -2894   2878  -4202       O  
-ATOM   9729  CB  SER B 596      24.708  38.682  26.426  1.00136.94           C  
-ANISOU 9729  CB  SER B 596    17409  18554  16068  -3344   3920  -4733       C  
-ATOM   9730  OG  SER B 596      24.083  38.386  25.191  1.00138.55           O  
-ANISOU 9730  OG  SER B 596    17801  18468  16372  -3201   3779  -4439       O  
-ATOM   9731  N   SER B 597      24.363  36.293  28.691  1.00116.26           N  
-ANISOU 9731  N   SER B 597    14069  16624  13479  -3030   3126  -4470       N  
-ATOM   9732  CA  SER B 597      23.552  35.238  29.281  1.00108.36           C  
-ANISOU 9732  CA  SER B 597    12874  15739  12559  -2791   2745  -4128       C  
-ATOM   9733  C   SER B 597      22.084  35.348  28.881  1.00103.94           C  
-ANISOU 9733  C   SER B 597    12501  14858  12133  -2589   2696  -3664       C  
-ATOM   9734  O   SER B 597      21.314  34.402  29.045  1.00102.44           O  
-ANISOU 9734  O   SER B 597    12193  14700  12031  -2372   2355  -3334       O  
-ATOM   9735  CB  SER B 597      23.684  35.272  30.804  1.00108.84           C  
-ANISOU 9735  CB  SER B 597    12707  16098  12551  -2825   2768  -4247       C  
-ATOM   9736  OG  SER B 597      23.484  36.585  31.302  1.00108.28           O  
-ANISOU 9736  OG  SER B 597    12789  15915  12437  -2962   3181  -4356       O  
-ATOM   9737  N   VAL B 598      21.708  36.507  28.350  1.00100.81           N  
-ANISOU 9737  N   VAL B 598    12396  14157  11750  -2662   3041  -3645       N  
-ATOM   9738  CA  VAL B 598      20.319  36.802  28.008  1.00 93.68           C  
-ANISOU 9738  CA  VAL B 598    11687  12941  10965  -2486   3053  -3225       C  
-ATOM   9739  C   VAL B 598      19.626  35.675  27.243  1.00 90.10           C  
-ANISOU 9739  C   VAL B 598    11208  12399  10626  -2256   2646  -2856       C  
-ATOM   9740  O   VAL B 598      18.522  35.258  27.599  1.00 88.57           O  
-ANISOU 9740  O   VAL B 598    10967  12161  10526  -2054   2454  -2493       O  
-ATOM   9741  CB  VAL B 598      20.217  38.098  27.179  1.00 92.86           C  
-ANISOU 9741  CB  VAL B 598    11928  12501  10853  -2601   3460  -3285       C  
-ATOM   9742  CG1 VAL B 598      18.774  38.375  26.798  1.00 89.33           C  
-ANISOU 9742  CG1 VAL B 598    11676  11739  10528  -2405   3459  -2841       C  
-ATOM   9743  CG2 VAL B 598      20.800  39.266  27.954  1.00 89.72           C  
-ANISOU 9743  CG2 VAL B 598    11575  12170  10345  -2827   3886  -3629       C  
-ATOM   9744  N   PHE B 599      20.282  35.190  26.193  1.00 86.31           N  
-ANISOU 9744  N   PHE B 599    10762  11894  10137  -2293   2523  -2956       N  
-ATOM   9745  CA  PHE B 599      19.689  34.198  25.302  1.00 81.75           C  
-ANISOU 9745  CA  PHE B 599    10197  11203   9661  -2100   2170  -2629       C  
-ATOM   9746  C   PHE B 599      19.405  32.878  26.003  1.00 77.34           C  
-ANISOU 9746  C   PHE B 599     9348  10895   9143  -1927   1753  -2444       C  
-ATOM   9747  O   PHE B 599      18.339  32.291  25.827  1.00 73.16           O  
-ANISOU 9747  O   PHE B 599     8820  10259   8719  -1719   1511  -2054       O  
-ATOM   9748  CB  PHE B 599      20.581  33.984  24.078  1.00 81.94           C  
-ANISOU 9748  CB  PHE B 599    10314  11165   9655  -2203   2149  -2820       C  
-ATOM   9749  CG  PHE B 599      20.752  35.216  23.241  1.00 83.50           C  
-ANISOU 9749  CG  PHE B 599    10826  11078   9823  -2350   2538  -2957       C  
-ATOM   9750  CD1 PHE B 599      21.840  36.051  23.430  1.00 83.62           C  
-ANISOU 9750  CD1 PHE B 599    10879  11169   9723  -2597   2873  -3392       C  
-ATOM   9751  CD2 PHE B 599      19.815  35.550  22.277  1.00 84.26           C  
-ANISOU 9751  CD2 PHE B 599    11181  10830  10003  -2241   2575  -2651       C  
-ATOM   9752  CE1 PHE B 599      21.995  37.191  22.668  1.00 83.82           C  
-ANISOU 9752  CE1 PHE B 599    11205  10925   9719  -2734   3243  -3521       C  
-ATOM   9753  CE2 PHE B 599      19.964  36.688  21.511  1.00 84.89           C  
-ANISOU 9753  CE2 PHE B 599    11560  10643  10053  -2369   2938  -2772       C  
-ATOM   9754  CZ  PHE B 599      21.055  37.510  21.708  1.00 84.93           C  
-ANISOU 9754  CZ  PHE B 599    11609  10717   9943  -2616   3276  -3208       C  
-ATOM   9755  N   GLY B 600      20.361  32.413  26.798  1.00 97.57           N  
-ANISOU 9755  N   GLY B 600    11661  13792  11618  -2012   1673  -2725       N  
-ATOM   9756  CA  GLY B 600      20.155  31.218  27.591  1.00 94.75           C  
-ANISOU 9756  CA  GLY B 600    11024  13691  11285  -1856   1306  -2579       C  
-ATOM   9757  C   GLY B 600      18.901  31.342  28.436  1.00 91.77           C  
-ANISOU 9757  C   GLY B 600    10629  13259  10980  -1700   1280  -2257       C  
-ATOM   9758  O   GLY B 600      18.082  30.423  28.494  1.00 86.75           O  
-ANISOU 9758  O   GLY B 600     9904  12626  10431  -1494    962  -1924       O  
-ATOM   9759  N   GLN B 601      18.748  32.492  29.085  1.00 85.24           N  
-ANISOU 9759  N   GLN B 601     9892  12379  10116  -1804   1625  -2359       N  
-ATOM   9760  CA  GLN B 601      17.603  32.738  29.954  1.00 85.51           C  
-ANISOU 9760  CA  GLN B 601     9916  12359  10214  -1677   1646  -2083       C  
-ATOM   9761  C   GLN B 601      16.291  32.653  29.178  1.00 83.27           C  
-ANISOU 9761  C   GLN B 601     9807  11766  10066  -1483   1541  -1643       C  
-ATOM   9762  O   GLN B 601      15.368  31.948  29.584  1.00 83.25           O  
-ANISOU 9762  O   GLN B 601     9698  11786  10146  -1288   1283  -1323       O  
-ATOM   9763  CB  GLN B 601      17.728  34.104  30.639  1.00 94.24           C  
-ANISOU 9763  CB  GLN B 601    11127  13426  11253  -1845   2081  -2290       C  
-ATOM   9764  CG  GLN B 601      19.021  34.303  31.428  1.00104.62           C  
-ANISOU 9764  CG  GLN B 601    12277  15048  12425  -2055   2219  -2742       C  
-ATOM   9765  CD  GLN B 601      19.132  35.695  32.029  1.00112.31           C  
-ANISOU 9765  CD  GLN B 601    13377  15964  13331  -2235   2670  -2949       C  
-ATOM   9766  OE1 GLN B 601      18.153  36.441  32.084  1.00114.81           O  
-ANISOU 9766  OE1 GLN B 601    13872  16039  13713  -2178   2857  -2728       O  
-ATOM   9767  NE2 GLN B 601      20.330  36.052  32.482  1.00117.60           N  
-ANISOU 9767  NE2 GLN B 601    13956  16858  13869  -2454   2850  -3377       N  
-ATOM   9768  N   ILE B 602      16.213  33.364  28.058  1.00 64.89           N  
-ANISOU 9768  N   ILE B 602     7745   9153   7756  -1537   1739  -1631       N  
-ATOM   9769  CA  ILE B 602      14.981  33.399  27.276  1.00 61.53           C  
-ANISOU 9769  CA  ILE B 602     7502   8426   7451  -1363   1669  -1225       C  
-ATOM   9770  C   ILE B 602      14.608  32.021  26.733  1.00 61.10           C  
-ANISOU 9770  C   ILE B 602     7333   8408   7473  -1180   1223   -960       C  
-ATOM   9771  O   ILE B 602      13.434  31.659  26.704  1.00 59.95           O  
-ANISOU 9771  O   ILE B 602     7197   8149   7431   -987   1048   -579       O  
-ATOM   9772  CB  ILE B 602      15.063  34.402  26.109  1.00 58.49           C  
-ANISOU 9772  CB  ILE B 602     7430   7733   7060  -1461   1965  -1283       C  
-ATOM   9773  CG1 ILE B 602      15.634  35.738  26.587  1.00 56.89           C  
-ANISOU 9773  CG1 ILE B 602     7343   7510   6764  -1672   2422  -1605       C  
-ATOM   9774  CG2 ILE B 602      13.693  34.597  25.487  1.00 55.65           C  
-ANISOU 9774  CG2 ILE B 602     7257   7070   6819  -1276   1933   -855       C  
-ATOM   9775  CD1 ILE B 602      15.628  36.808  25.526  1.00 52.08           C  
-ANISOU 9775  CD1 ILE B 602     7059   6582   6147  -1760   2745  -1647       C  
-ATOM   9776  N   GLU B 603      15.603  31.251  26.304  1.00 86.63           N  
-ANISOU 9776  N   GLU B 603    10459  11801  10655  -1243   1045  -1161       N  
-ATOM   9777  CA  GLU B 603      15.337  29.900  25.832  1.00 85.36           C  
-ANISOU 9777  CA  GLU B 603    10181  11694  10557  -1082    627   -934       C  
-ATOM   9778  C   GLU B 603      14.635  29.105  26.923  1.00 84.19           C  
-ANISOU 9778  C   GLU B 603     9808  11725  10456   -914    371   -710       C  
-ATOM   9779  O   GLU B 603      13.650  28.420  26.663  1.00 80.75           O  
-ANISOU 9779  O   GLU B 603     9363  11201  10118   -725    117   -350       O  
-ATOM   9780  CB  GLU B 603      16.624  29.196  25.409  1.00 86.10           C  
-ANISOU 9780  CB  GLU B 603    10163  11974  10577  -1188    492  -1224       C  
-ATOM   9781  CG  GLU B 603      16.395  27.775  24.922  1.00 86.48           C  
-ANISOU 9781  CG  GLU B 603    10092  12080  10685  -1028     68  -1000       C  
-ATOM   9782  CD  GLU B 603      17.686  27.016  24.688  1.00 89.72           C  
-ANISOU 9782  CD  GLU B 603    10358  12711  11020  -1122    -74  -1291       C  
-ATOM   9783  OE1 GLU B 603      18.702  27.655  24.338  1.00 92.70           O  
-ANISOU 9783  OE1 GLU B 603    10813  13091  11317  -1316    162  -1633       O  
-ATOM   9784  OE2 GLU B 603      17.686  25.778  24.863  1.00 91.90           O  
-ANISOU 9784  OE2 GLU B 603    10442  13158  11317  -1001   -417  -1180       O  
-ATOM   9785  N   ASN B 604      15.141  29.207  28.146  1.00 84.91           N  
-ANISOU 9785  N   ASN B 604     9721  12067  10474   -987    444   -927       N  
-ATOM   9786  CA  ASN B 604      14.520  28.533  29.277  1.00 84.27           C  
-ANISOU 9786  CA  ASN B 604     9431  12160  10426   -840    231   -740       C  
-ATOM   9787  C   ASN B 604      13.050  28.894  29.409  1.00 82.17           C  
-ANISOU 9787  C   ASN B 604     9277  11672  10271   -687    260   -357       C  
-ATOM   9788  O   ASN B 604      12.221  28.051  29.745  1.00 80.15           O  
-ANISOU 9788  O   ASN B 604     8907  11456  10091   -502    -18    -61       O  
-ATOM   9789  CB  ASN B 604      15.241  28.883  30.577  1.00 91.16           C  
-ANISOU 9789  CB  ASN B 604    10140  13300  11195   -966    386  -1045       C  
-ATOM   9790  CG  ASN B 604      15.948  27.692  31.190  1.00 94.85           C  
-ANISOU 9790  CG  ASN B 604    10324  14107  11608   -931     86  -1165       C  
-ATOM   9791  OD1 ASN B 604      16.731  27.013  30.525  1.00 99.59           O  
-ANISOU 9791  OD1 ASN B 604    10871  14792  12176   -960    -74  -1292       O  
-ATOM   9792  ND2 ASN B 604      15.667  27.424  32.462  1.00 98.33           N  
-ANISOU 9792  ND2 ASN B 604    10583  14742  12036   -865     10  -1120       N  
-ATOM   9793  N   HIS B 605      12.736  30.154  29.139  1.00 72.21           N  
-ANISOU 9793  N   HIS B 605     8243  10175   9018   -763    605   -365       N  
-ATOM   9794  CA  HIS B 605      11.385  30.661  29.333  1.00 70.96           C  
-ANISOU 9794  CA  HIS B 605     8198   9805   8958   -631    685    -29       C  
-ATOM   9795  C   HIS B 605      10.380  30.085  28.335  1.00 66.93           C  
-ANISOU 9795  C   HIS B 605     7780   9086   8563   -444    444    362       C  
-ATOM   9796  O   HIS B 605       9.173  30.194  28.541  1.00 66.54           O  
-ANISOU 9796  O   HIS B 605     7772   8903   8608   -295    414    688       O  
-ATOM   9797  CB  HIS B 605      11.376  32.192  29.275  1.00 75.88           C  
-ANISOU 9797  CB  HIS B 605     9051  10228   9552   -767   1137   -155       C  
-ATOM   9798  CG  HIS B 605      12.127  32.843  30.398  1.00 80.76           C  
-ANISOU 9798  CG  HIS B 605     9583  11035  10066   -938   1393   -491       C  
-ATOM   9799  ND1 HIS B 605      12.536  32.158  31.519  1.00 81.72           N  
-ANISOU 9799  ND1 HIS B 605     9439  11472  10140   -938   1227   -608       N  
-ATOM   9800  CD2 HIS B 605      12.542  34.122  30.566  1.00 83.03           C  
-ANISOU 9800  CD2 HIS B 605    10020  11243  10285  -1118   1809   -736       C  
-ATOM   9801  CE1 HIS B 605      13.172  32.980  32.330  1.00 84.25           C  
-ANISOU 9801  CE1 HIS B 605     9741  11905  10364  -1113   1522   -911       C  
-ATOM   9802  NE2 HIS B 605      13.189  34.181  31.778  1.00 84.19           N  
-ANISOU 9802  NE2 HIS B 605     9984  11662  10343  -1229   1882   -997       N  
-ATOM   9803  N   LEU B 606      10.877  29.474  27.263  1.00 64.42           N  
-ANISOU 9803  N   LEU B 606     7493   8746   8238   -456    274    326       N  
-ATOM   9804  CA  LEU B 606      10.016  28.884  26.238  1.00 59.30           C  
-ANISOU 9804  CA  LEU B 606     6932   7912   7688   -295     38    674       C  
-ATOM   9805  C   LEU B 606       9.883  27.376  26.413  1.00 57.67           C  
-ANISOU 9805  C   LEU B 606     6502   7895   7516   -157   -390    826       C  
-ATOM   9806  O   LEU B 606       9.034  26.745  25.781  1.00 55.56           O  
-ANISOU 9806  O   LEU B 606     6265   7510   7335     -4   -624   1148       O  
-ATOM   9807  CB  LEU B 606      10.575  29.164  24.839  1.00 55.58           C  
-ANISOU 9807  CB  LEU B 606     6662   7265   7192   -393    124    562       C  
-ATOM   9808  CG  LEU B 606      10.601  30.592  24.282  1.00 52.11           C  
-ANISOU 9808  CG  LEU B 606     6501   6569   6730   -508    526    465       C  
-ATOM   9809  CD1 LEU B 606      11.567  30.677  23.107  1.00 48.75           C  
-ANISOU 9809  CD1 LEU B 606     6209   6067   6245   -646    587    238       C  
-ATOM   9810  CD2 LEU B 606       9.209  31.058  23.873  1.00 49.57           C  
-ANISOU 9810  CD2 LEU B 606     6354   5970   6511   -354    569    852       C  
-ATOM   9811  N   ARG B 607      10.712  26.815  27.291  1.00 92.27           N  
-ANISOU 9811  N   ARG B 607    10661  12572  11824   -211   -485    595       N  
-ATOM   9812  CA  ARG B 607      10.918  25.366  27.369  1.00 91.04           C  
-ANISOU 9812  CA  ARG B 607    10298  12620  11674   -114   -870    656       C  
-ATOM   9813  C   ARG B 607       9.660  24.489  27.428  1.00 89.84           C  
-ANISOU 9813  C   ARG B 607    10082  12421  11631    110  -1172   1075       C  
-ATOM   9814  O   ARG B 607       9.426  23.677  26.530  1.00 88.91           O  
-ANISOU 9814  O   ARG B 607     9986  12237  11560    194  -1416   1250       O  
-ATOM   9815  CB  ARG B 607      11.892  25.009  28.504  1.00 91.29           C  
-ANISOU 9815  CB  ARG B 607    10094  12984  11608   -191   -898    360       C  
-ATOM   9816  CG  ARG B 607      13.338  25.393  28.199  1.00 92.15           C  
-ANISOU 9816  CG  ARG B 607    10218  13193  11603   -402   -723    -65       C  
-ATOM   9817  CD  ARG B 607      14.345  24.806  29.185  1.00 92.28           C  
-ANISOU 9817  CD  ARG B 607     9977  13562  11522   -458   -819   -342       C  
-ATOM   9818  NE  ARG B 607      15.707  25.246  28.878  1.00 93.21           N  
-ANISOU 9818  NE  ARG B 607    10113  13771  11533   -666   -634   -752       N  
-ATOM   9819  CZ  ARG B 607      16.528  24.629  28.032  1.00 92.87           C  
-ANISOU 9819  CZ  ARG B 607    10052  13773  11460   -711   -768   -886       C  
-ATOM   9820  NH1 ARG B 607      16.130  23.533  27.400  1.00 91.59           N  
-ANISOU 9820  NH1 ARG B 607     9860  13574  11365   -565  -1090   -640       N  
-ATOM   9821  NH2 ARG B 607      17.748  25.110  27.817  1.00 93.83           N  
-ANISOU 9821  NH2 ARG B 607    10189  13977  11485   -908   -575  -1270       N  
-ATOM   9822  N   LYS B 608       8.856  24.640  28.476  1.00 66.90           N  
-ANISOU 9822  N   LYS B 608     9749   8093   7577   2415    -96  -1446       N  
-ATOM   9823  CA  LYS B 608       7.740  23.719  28.693  1.00 66.56           C  
-ANISOU 9823  CA  LYS B 608     9793   7848   7650   2324   -265  -1394       C  
-ATOM   9824  C   LYS B 608       6.375  24.403  28.740  1.00 63.58           C  
-ANISOU 9824  C   LYS B 608     9353   7438   7366   2146   -253  -1281       C  
-ATOM   9825  O   LYS B 608       5.533  24.072  29.569  1.00 63.05           O  
-ANISOU 9825  O   LYS B 608     9276   7262   7420   2022   -311  -1175       O  
-ATOM   9826  CB  LYS B 608       7.970  22.896  29.957  1.00 69.30           C  
-ANISOU 9826  CB  LYS B 608    10148   8114   8070   2306   -310  -1346       C  
-ATOM   9827  N   LEU B 609       6.157  25.355  27.843  1.00 65.39           N  
-ANISOU 9827  N   LEU B 609     9538   7766   7542   2138   -176  -1297       N  
-ATOM   9828  CA  LEU B 609       4.880  26.048  27.785  1.00 60.25           C  
-ANISOU 9828  CA  LEU B 609     8825   7096   6972   1980   -155  -1185       C  
-ATOM   9829  C   LEU B 609       3.809  25.124  27.240  1.00 59.74           C  
-ANISOU 9829  C   LEU B 609     8874   6848   6977   1930   -359  -1168       C  
-ATOM   9830  O   LEU B 609       4.118  24.140  26.574  1.00 58.46           O  
-ANISOU 9830  O   LEU B 609     8849   6596   6769   2035   -501  -1271       O  
-ATOM   9831  CB  LEU B 609       4.983  27.280  26.893  1.00 59.71           C  
-ANISOU 9831  CB  LEU B 609     8682   7184   6821   1996    -19  -1212       C  
-ATOM   9832  CG  LEU B 609       6.097  28.262  27.243  1.00 60.38           C  
-ANISOU 9832  CG  LEU B 609     8660   7461   6819   2050    180  -1239       C  
-ATOM   9833  CD1 LEU B 609       6.060  29.443  26.284  1.00 62.13           C  
-ANISOU 9833  CD1 LEU B 609     8815   7822   6969   2058    300  -1260       C  
-ATOM   9834  CD2 LEU B 609       5.970  28.728  28.686  1.00 59.43           C  
-ANISOU 9834  CD2 LEU B 609     8442   7364   6774   1931    289  -1120       C  
-ATOM   9835  N   PRO B 610       2.542  25.429  27.544  1.00 51.10           N  
-ANISOU 9835  N   PRO B 610     7728   5696   5993   1768   -374  -1030       N  
-ATOM   9836  CA  PRO B 610       1.398  24.787  26.897  1.00 51.13           C  
-ANISOU 9836  CA  PRO B 610     7818   5549   6060   1696   -556   -993       C  
-ATOM   9837  C   PRO B 610       1.063  25.505  25.596  1.00 50.63           C  
-ANISOU 9837  C   PRO B 610     7747   5560   5930   1702   -530  -1026       C  
-ATOM   9838  O   PRO B 610       1.646  26.552  25.312  1.00 49.41           O  
-ANISOU 9838  O   PRO B 610     7506   5572   5694   1750   -361  -1063       O  
-ATOM   9839  CB  PRO B 610       0.275  25.008  27.903  1.00 49.89           C  
-ANISOU 9839  CB  PRO B 610     7574   5335   6047   1521   -541   -809       C  
-ATOM   9840  CG  PRO B 610       0.623  26.282  28.552  1.00 49.16           C  
-ANISOU 9840  CG  PRO B 610     7336   5406   5937   1493   -310   -755       C  
-ATOM   9841  CD  PRO B 610       2.121  26.317  28.640  1.00 49.59           C  
-ANISOU 9841  CD  PRO B 610     7398   5566   5878   1640   -225   -889       C  
-ATOM   9842  N   ASP B 611       0.137  24.954  24.819  1.00 51.26           N  
-ANISOU 9842  N   ASP B 611     7915   5520   6043   1649   -699  -1010       N  
-ATOM   9843  CA  ASP B 611      -0.299  25.593  23.588  1.00 49.81           C  
-ANISOU 9843  CA  ASP B 611     7723   5397   5804   1640   -689  -1027       C  
-ATOM   9844  C   ASP B 611      -1.169  26.802  23.916  1.00 47.77           C  
-ANISOU 9844  C   ASP B 611     7305   5228   5616   1498   -544   -870       C  
-ATOM   9845  O   ASP B 611      -2.401  26.743  23.861  1.00 46.48           O  
-ANISOU 9845  O   ASP B 611     7128   4986   5547   1363   -625   -742       O  
-ATOM   9846  CB  ASP B 611      -1.062  24.600  22.714  1.00 52.23           C  
-ANISOU 9846  CB  ASP B 611     8179   5541   6126   1611   -923  -1047       C  
-ATOM   9847  CG  ASP B 611      -1.237  25.087  21.287  1.00 52.51           C  
-ANISOU 9847  CG  ASP B 611     8239   5639   6072   1642   -931  -1109       C  
-ATOM   9848  OD1 ASP B 611      -1.130  26.311  21.050  1.00 51.27           O  
-ANISOU 9848  OD1 ASP B 611     7956   5647   5878   1641   -752  -1089       O  
-ATOM   9849  OD2 ASP B 611      -1.479  24.237  20.401  1.00 54.55           O  
-ANISOU 9849  OD2 ASP B 611     8650   5780   6295   1668  -1116  -1178       O  
-ATOM   9850  N   ILE B 612      -0.510  27.899  24.266  1.00 50.21           N  
-ANISOU 9850  N   ILE B 612     7496   5704   5877   1530   -328   -875       N  
-ATOM   9851  CA  ILE B 612      -1.192  29.134  24.608  1.00 47.61           C  
-ANISOU 9851  CA  ILE B 612     7020   5471   5598   1414   -161   -735       C  
-ATOM   9852  C   ILE B 612      -2.102  29.621  23.475  1.00 48.53           C  
-ANISOU 9852  C   ILE B 612     7120   5609   5712   1357   -186   -693       C  
-ATOM   9853  O   ILE B 612      -3.137  30.242  23.721  1.00 47.03           O  
-ANISOU 9853  O   ILE B 612     6839   5426   5604   1227   -128   -535       O  
-ATOM   9854  CB  ILE B 612      -0.172  30.225  24.970  1.00 44.62           C  
-ANISOU 9854  CB  ILE B 612     6541   5273   5140   1477     69   -778       C  
-ATOM   9855  CG1 ILE B 612       0.688  29.764  26.148  1.00 43.90           C  
-ANISOU 9855  CG1 ILE B 612     6458   5166   5056   1519     93   -803       C  
-ATOM   9856  CG2 ILE B 612      -0.876  31.522  25.292  1.00 42.96           C  
-ANISOU 9856  CG2 ILE B 612     6194   5155   4974   1361    248   -636       C  
-ATOM   9857  CD1 ILE B 612       1.747  30.765  26.558  1.00 42.29           C  
-ANISOU 9857  CD1 ILE B 612     6163   5134   4770   1574    303   -843       C  
-ATOM   9858  N   GLU B 613      -1.717  29.331  22.236  1.00 43.72           N  
-ANISOU 9858  N   GLU B 613     6600   5008   5003   1458   -271   -829       N  
-ATOM   9859  CA  GLU B 613      -2.512  29.721  21.087  1.00 44.00           C  
-ANISOU 9859  CA  GLU B 613     6630   5063   5024   1413   -308   -802       C  
-ATOM   9860  C   GLU B 613      -3.895  29.110  21.156  1.00 45.99           C  
-ANISOU 9860  C   GLU B 613     6912   5166   5396   1263   -475   -660       C  
-ATOM   9861  O   GLU B 613      -4.900  29.806  21.007  1.00 45.95           O  
-ANISOU 9861  O   GLU B 613     6814   5195   5450   1147   -426   -519       O  
-ATOM   9862  N   ARG B 614      -3.946  27.803  21.391  1.00 44.03           N  
-ANISOU 9862  N   ARG B 614     6793   4753   5185   1267   -673   -690       N  
-ATOM   9863  CA  ARG B 614      -5.213  27.087  21.471  1.00 47.62           C  
-ANISOU 9863  CA  ARG B 614     7288   5051   5753   1125   -857   -558       C  
-ATOM   9864  C   ARG B 614      -5.977  27.478  22.729  1.00 45.29           C  
-ANISOU 9864  C   ARG B 614     6866   4748   5595    990   -770   -358       C  
-ATOM   9865  O   ARG B 614      -7.204  27.563  22.721  1.00 44.12           O  
-ANISOU 9865  O   ARG B 614     6671   4551   5542    851   -825   -192       O  
-ATOM   9866  CB  ARG B 614      -4.976  25.576  21.446  1.00 54.38           C  
-ANISOU 9866  CB  ARG B 614     8323   5730   6608   1172  -1085   -650       C  
-ATOM   9867  CG  ARG B 614      -6.203  24.769  21.071  1.00 65.58           C  
-ANISOU 9867  CG  ARG B 614     9822   6987   8107   1042  -1314   -553       C  
-ATOM   9868  CD  ARG B 614      -5.886  23.773  19.964  1.00 75.91           C  
-ANISOU 9868  CD  ARG B 614    11331   8191   9319   1126  -1514   -713       C  
-ATOM   9869  NE  ARG B 614      -6.121  22.400  20.389  1.00 84.48           N  
-ANISOU 9869  NE  ARG B 614    12555   9077  10467   1094  -1727   -709       N  
-ATOM   9870  CZ  ARG B 614      -5.220  21.653  21.014  1.00 89.09           C  
-ANISOU 9870  CZ  ARG B 614    13218   9601  11033   1200  -1745   -808       C  
-ATOM   9871  NH1 ARG B 614      -4.018  22.146  21.284  1.00 90.61           N  
-ANISOU 9871  NH1 ARG B 614    13361   9921  11145   1342  -1566   -914       N  
-ATOM   9872  NH2 ARG B 614      -5.523  20.412  21.367  1.00 91.81           N  
-ANISOU 9872  NH2 ARG B 614    13687   9759  11439   1162  -1942   -795       N  
-ATOM   9873  N   GLY B 615      -5.239  27.724  23.807  1.00 50.62           N  
-ANISOU 9873  N   GLY B 615     7485   5472   6275   1034   -631   -369       N  
-ATOM   9874  CA  GLY B 615      -5.839  28.097  25.075  1.00 47.87           C  
-ANISOU 9874  CA  GLY B 615     7026   5117   6044    923   -534   -192       C  
-ATOM   9875  C   GLY B 615      -6.658  29.373  24.999  1.00 45.47           C  
-ANISOU 9875  C   GLY B 615     6581   4921   5775    827   -370    -40       C  
-ATOM   9876  O   GLY B 615      -7.810  29.407  25.430  1.00 45.58           O  
-ANISOU 9876  O   GLY B 615     6538   4876   5905    695   -396    149       O  
-ATOM   9877  N   LEU B 616      -6.064  30.425  24.448  1.00 47.88           N  
-ANISOU 9877  N   LEU B 616     6828   5386   5980    895   -199   -115       N  
-ATOM   9878  CA  LEU B 616      -6.738  31.712  24.328  1.00 45.66           C  
-ANISOU 9878  CA  LEU B 616     6414   5218   5718    819    -22     17       C  
-ATOM   9879  C   LEU B 616      -7.978  31.631  23.436  1.00 47.12           C  
-ANISOU 9879  C   LEU B 616     6595   5356   5952    722   -140    126       C  
-ATOM   9880  O   LEU B 616      -8.967  32.322  23.682  1.00 47.04           O  
-ANISOU 9880  O   LEU B 616     6479   5374   6020    613    -51    313       O  
-ATOM   9881  CB  LEU B 616      -5.765  32.782  23.816  1.00 41.14           C  
-ANISOU 9881  CB  LEU B 616     5792   4822   5018    922    169   -105       C  
-ATOM   9882  CG  LEU B 616      -4.572  33.109  24.725  1.00 36.20           C  
-ANISOU 9882  CG  LEU B 616     5144   4270   4339   1000    319   -186       C  
-ATOM   9883  CD1 LEU B 616      -3.504  33.901  23.981  1.00 33.65           C  
-ANISOU 9883  CD1 LEU B 616     4800   4108   3878   1119    451   -335       C  
-ATOM   9884  CD2 LEU B 616      -5.038  33.862  25.966  1.00 34.30           C  
-ANISOU 9884  CD2 LEU B 616     4800   4053   4178    901    489    -19       C  
-ATOM   9885  N   CYS B 617      -7.931  30.779  22.415  1.00 51.54           N  
-ANISOU 9885  N   CYS B 617     7273   5844   6465    761   -341     17       N  
-ATOM   9886  CA  CYS B 617      -9.063  30.630  21.503  1.00 54.55           C  
-ANISOU 9886  CA  CYS B 617     7663   6179   6884    665   -475    112       C  
-ATOM   9887  C   CYS B 617     -10.251  29.958  22.170  1.00 55.00           C  
-ANISOU 9887  C   CYS B 617     7714   6095   7088    519   -612    307       C  
-ATOM   9888  O   CYS B 617     -11.396  30.376  21.988  1.00 56.17           O  
-ANISOU 9888  O   CYS B 617     7780   6252   7310    399   -608    489       O  
-ATOM   9889  CB  CYS B 617      -8.661  29.844  20.259  1.00 57.00           C  
-ANISOU 9889  CB  CYS B 617     8122   6438   7097    745   -662    -62       C  
-ATOM   9890  SG  CYS B 617      -7.751  30.832  19.067  1.00 60.85           S  
-ANISOU 9890  SG  CYS B 617     8587   7109   7423    880   -513   -229       S  
-ATOM   9891  N   SER B 618      -9.974  28.905  22.929  1.00 54.57           N  
-ANISOU 9891  N   SER B 618     7746   5911   7078    531   -736    273       N  
-ATOM   9892  CA  SER B 618     -11.007  28.226  23.689  1.00 53.26           C  
-ANISOU 9892  CA  SER B 618     7572   5609   7055    401   -863    456       C  
-ATOM   9893  C   SER B 618     -11.699  29.257  24.576  1.00 49.48           C  
-ANISOU 9893  C   SER B 618     6928   5208   6666    313   -661    667       C  
-ATOM   9894  O   SER B 618     -12.928  29.319  24.633  1.00 49.67           O  
-ANISOU 9894  O   SER B 618     6888   5193   6793    184   -706    874       O  
-ATOM   9895  CB  SER B 618     -10.392  27.109  24.536  1.00 55.21           C  
-ANISOU 9895  CB  SER B 618     7919   5732   7327    450   -972    375       C  
-ATOM   9896  OG  SER B 618     -11.360  26.134  24.893  1.00 57.48           O  
-ANISOU 9896  OG  SER B 618     8247   5858   7736    335  -1173    510       O  
-ATOM   9897  N   ILE B 619     -10.903  30.079  25.254  1.00 34.59           N  
-ANISOU 9897  N   ILE B 619     4975   3431   4737    384   -435    621       N  
-ATOM   9898  CA  ILE B 619     -11.444  31.119  26.120  1.00 33.10           C  
-ANISOU 9898  CA  ILE B 619     4645   3316   4615    315   -222    806       C  
-ATOM   9899  C   ILE B 619     -12.245  32.159  25.341  1.00 35.84           C  
-ANISOU 9899  C   ILE B 619     4893   3765   4958    256   -117    924       C  
-ATOM   9900  O   ILE B 619     -13.398  32.435  25.662  1.00 36.91           O  
-ANISOU 9900  O   ILE B 619     4945   3883   5198    142    -92   1149       O  
-ATOM   9901  CB  ILE B 619     -10.330  31.857  26.864  1.00 26.82           C  
-ANISOU 9901  CB  ILE B 619     3814   2626   3749    405      0    710       C  
-ATOM   9902  CG1 ILE B 619      -9.540  30.887  27.738  1.00 25.13           C  
-ANISOU 9902  CG1 ILE B 619     3684   2321   3544    461    -86    612       C  
-ATOM   9903  CG2 ILE B 619     -10.914  33.001  27.687  1.00 24.43           C  
-ANISOU 9903  CG2 ILE B 619     3381   2397   3504    335    230    900       C  
-ATOM   9904  CD1 ILE B 619      -8.345  31.518  28.406  1.00 21.27           C  
-ANISOU 9904  CD1 ILE B 619     3170   1936   2974    551    108    504       C  
-ATOM   9905  N   TYR B 620     -11.618  32.742  24.324  1.00 43.88           N  
-ANISOU 9905  N   TYR B 620     5918   4898   5857    337    -49    779       N  
-ATOM   9906  CA  TYR B 620     -12.255  33.765  23.501  1.00 45.83           C  
-ANISOU 9906  CA  TYR B 620     6071   5255   6086    296     59    870       C  
-ATOM   9907  C   TYR B 620     -13.654  33.332  23.072  1.00 47.53           C  
-ANISOU 9907  C   TYR B 620     6270   5390   6401    164   -104   1057       C  
-ATOM   9908  O   TYR B 620     -14.589  34.132  23.073  1.00 46.82           O  
-ANISOU 9908  O   TYR B 620     6065   5358   6368     80      8   1252       O  
-ATOM   9909  CB  TYR B 620     -11.382  34.064  22.277  1.00 48.47           C  
-ANISOU 9909  CB  TYR B 620     6450   5689   6278    407     73    661       C  
-ATOM   9910  CG  TYR B 620     -11.893  35.146  21.350  1.00 50.47           C  
-ANISOU 9910  CG  TYR B 620     6608   6069   6498    381    192    728       C  
-ATOM   9911  CD1 TYR B 620     -11.947  36.473  21.756  1.00 51.09           C  
-ANISOU 9911  CD1 TYR B 620     6562   6275   6573    374    459    819       C  
-ATOM   9912  CD2 TYR B 620     -12.287  34.842  20.053  1.00 53.06           C  
-ANISOU 9912  CD2 TYR B 620     6980   6391   6791    367     40    695       C  
-ATOM   9913  CE1 TYR B 620     -12.400  37.466  20.904  1.00 53.04           C  
-ANISOU 9913  CE1 TYR B 620     6721   6640   6790    355    574    882       C  
-ATOM   9914  CE2 TYR B 620     -12.743  35.824  19.194  1.00 54.21           C  
-ANISOU 9914  CE2 TYR B 620     7035   6657   6906    344    149    758       C  
-ATOM   9915  CZ  TYR B 620     -12.796  37.134  19.622  1.00 54.02           C  
-ANISOU 9915  CZ  TYR B 620     6880   6761   6886    340    418    852       C  
-ATOM   9916  OH  TYR B 620     -13.248  38.113  18.765  1.00 55.25           O  
-ANISOU 9916  OH  TYR B 620     6944   7038   7012    322    532    917       O  
-ATOM   9917  N   HIS B 621     -13.794  32.059  22.718  1.00 45.66           N  
-ANISOU 9917  N   HIS B 621     6151   5016   6183    144   -369   1003       N  
-ATOM   9918  CA  HIS B 621     -15.076  31.526  22.275  1.00 50.99           C  
-ANISOU 9918  CA  HIS B 621     6824   5603   6946     11   -557   1173       C  
-ATOM   9919  C   HIS B 621     -15.982  31.185  23.447  1.00 52.16           C  
-ANISOU 9919  C   HIS B 621     6916   5656   7246    -99   -584   1400       C  
-ATOM   9920  O   HIS B 621     -17.141  30.801  23.259  1.00 52.96           O  
-ANISOU 9920  O   HIS B 621     6994   5689   7440   -224   -725   1584       O  
-ATOM   9921  CB  HIS B 621     -14.862  30.285  21.417  1.00 56.36           C  
-ANISOU 9921  CB  HIS B 621     7669   6166   7580     29   -837   1023       C  
-ATOM   9922  CG  HIS B 621     -14.405  30.590  20.032  1.00 61.73           C  
-ANISOU 9922  CG  HIS B 621     8396   6928   8129    102   -849    863       C  
-ATOM   9923  ND1 HIS B 621     -15.251  31.089  19.065  1.00 64.32           N  
-ANISOU 9923  ND1 HIS B 621     8665   7317   8455     24   -864    967       N  
-ATOM   9924  CD2 HIS B 621     -13.190  30.474  19.446  1.00 63.99           C  
-ANISOU 9924  CD2 HIS B 621     8781   7252   8282    248   -844    612       C  
-ATOM   9925  CE1 HIS B 621     -14.576  31.269  17.945  1.00 65.89           C  
-ANISOU 9925  CE1 HIS B 621     8927   7585   8524    119   -869    781       C  
-ATOM   9926  NE2 HIS B 621     -13.325  30.903  18.149  1.00 66.82           N  
-ANISOU 9926  NE2 HIS B 621     9140   7688   8559    258   -856    565       N  
-ATOM   9927  N   LYS B 622     -15.439  31.328  24.654  1.00 52.54           N  
-ANISOU 9927  N   LYS B 622     6943   5704   7316    -54   -451   1390       N  
-ATOM   9928  CA  LYS B 622     -16.156  31.016  25.886  1.00 54.19           C  
-ANISOU 9928  CA  LYS B 622     7103   5826   7662   -139   -457   1591       C  
-ATOM   9929  C   LYS B 622     -16.580  29.553  25.923  1.00 56.61           C  
-ANISOU 9929  C   LYS B 622     7510   5956   8043   -202   -751   1611       C  
-ATOM   9930  O   LYS B 622     -17.686  29.218  26.353  1.00 56.30           O  
-ANISOU 9930  O   LYS B 622     7422   5840   8131   -320   -836   1833       O  
-ATOM   9931  CB  LYS B 622     -17.346  31.958  26.083  1.00 56.16           C  
-ANISOU 9931  CB  LYS B 622     7202   6141   7996   -240   -312   1864       C  
-ATOM   9932  CG  LYS B 622     -16.923  33.418  26.142  1.00 58.42           C  
-ANISOU 9932  CG  LYS B 622     7396   6591   8209   -178     -9   1849       C  
-ATOM   9933  CD  LYS B 622     -17.882  34.254  26.964  1.00 60.81           C  
-ANISOU 9933  CD  LYS B 622     7566   6931   8608   -254    178   2120       C  
-ATOM   9934  CE  LYS B 622     -18.657  35.229  26.094  1.00 63.74           C  
-ANISOU 9934  CE  LYS B 622     7835   7413   8970   -300    283   2254       C  
-ATOM   9935  NZ  LYS B 622     -19.599  36.046  26.912  1.00 65.12           N  
-ANISOU 9935  NZ  LYS B 622     7885   7621   9237   -364    478   2529       N  
-ATOM   9936  N   LYS B 623     -15.677  28.689  25.470  1.00 48.14           N  
-ANISOU 9936  N   LYS B 623     6581   4820   6890   -118   -902   1379       N  
-ATOM   9937  CA  LYS B 623     -15.910  27.255  25.463  1.00 51.87           C  
-ANISOU 9937  CA  LYS B 623     7176   5118   7414   -161  -1182   1361       C  
-ATOM   9938  C   LYS B 623     -14.949  26.525  26.394  1.00 49.65           C  
-ANISOU 9938  C   LYS B 623     6976   4762   7128    -74  -1202   1227       C  
-ATOM   9939  O   LYS B 623     -14.879  25.300  26.376  1.00 51.74           O  
-ANISOU 9939  O   LYS B 623     7363   4882   7414    -79  -1424   1164       O  
-ATOM   9940  CB  LYS B 623     -15.764  26.707  24.045  1.00 57.05           C  
-ANISOU 9940  CB  LYS B 623     7958   5739   7978   -142  -1374   1212       C  
-ATOM   9941  CG  LYS B 623     -16.984  26.901  23.169  1.00 65.41           C  
-ANISOU 9941  CG  LYS B 623     8969   6807   9077   -271  -1468   1380       C  
-ATOM   9942  CD  LYS B 623     -16.874  26.060  21.908  1.00 72.18           C  
-ANISOU 9942  CD  LYS B 623     9987   7586   9854   -266  -1710   1233       C  
-ATOM   9943  CE  LYS B 623     -18.187  26.012  21.152  1.00 76.65           C  
-ANISOU 9943  CE  LYS B 623    10518   8128  10476   -421  -1854   1422       C  
-ATOM   9944  NZ  LYS B 623     -18.137  25.005  20.059  1.00 83.57           N  
-ANISOU 9944  NZ  LYS B 623    11577   8894  11283   -433  -2124   1288       N  
-ATOM   9945  N   CYS B 624     -14.224  27.273  27.219  1.00 58.74           N  
-ANISOU 9945  N   CYS B 624     8060   6008   8251      2   -973   1189       N  
-ATOM   9946  CA  CYS B 624     -13.157  26.690  28.025  1.00 56.23           C  
-ANISOU 9946  CA  CYS B 624     7813   5645   7908     98   -971   1043       C  
-ATOM   9947  C   CYS B 624     -13.587  26.326  29.442  1.00 54.90           C  
-ANISOU 9947  C   CYS B 624     7598   5394   7869     36   -965   1201       C  
-ATOM   9948  O   CYS B 624     -14.528  26.901  29.986  1.00 54.15           O  
-ANISOU 9948  O   CYS B 624     7387   5321   7867    -58   -870   1422       O  
-ATOM   9949  CB  CYS B 624     -11.979  27.652  28.099  1.00 55.08           C  
-ANISOU 9949  CB  CYS B 624     7633   5651   7643    220   -737    892       C  
-ATOM   9950  SG  CYS B 624     -12.370  29.177  28.978  1.00 56.81           S  
-ANISOU 9950  SG  CYS B 624     7678   6007   7902    173   -428   1075       S  
-ATOM   9951  N   SER B 625     -12.884  25.362  30.031  1.00 51.28           N  
-ANISOU 9951  N   SER B 625     7231   4841   7412     94  -1063   1089       N  
-ATOM   9952  CA  SER B 625     -13.064  25.023  31.437  1.00 50.81           C  
-ANISOU 9952  CA  SER B 625     7132   4715   7460     59  -1040   1207       C  
-ATOM   9953  C   SER B 625     -12.400  26.082  32.298  1.00 49.23           C  
-ANISOU 9953  C   SER B 625     6843   4643   7218    116   -766   1197       C  
-ATOM   9954  O   SER B 625     -11.932  27.098  31.785  1.00 47.88           O  
-ANISOU 9954  O   SER B 625     6634   4611   6949    167   -599   1121       O  
-ATOM   9955  CB  SER B 625     -12.463  23.652  31.739  1.00 51.17           C  
-ANISOU 9955  CB  SER B 625     7307   4623   7513    111  -1230   1080       C  
-ATOM   9956  OG  SER B 625     -11.081  23.620  31.432  1.00 50.15           O  
-ANISOU 9956  OG  SER B 625     7254   4550   7249    254  -1182    837       O  
-ATOM   9957  N   THR B 626     -12.362  25.846  33.605  1.00 44.39           N  
-ANISOU 9957  N   THR B 626     6202   3984   6680    102   -722   1275       N  
-ATOM   9958  CA  THR B 626     -11.733  26.790  34.518  1.00 43.92           C  
-ANISOU 9958  CA  THR B 626     6072   4034   6581    147   -472   1270       C  
-ATOM   9959  C   THR B 626     -10.284  26.399  34.793  1.00 46.56           C  
-ANISOU 9959  C   THR B 626     6483   4387   6822    268   -462   1049       C  
-ATOM   9960  O   THR B 626      -9.441  27.256  35.066  1.00 44.45           O  
-ANISOU 9960  O   THR B 626     6180   4242   6466    330   -267    968       O  
-ATOM   9961  CB  THR B 626     -12.505  26.904  35.841  1.00 41.41           C  
-ANISOU 9961  CB  THR B 626     5673   3671   6389     65   -398   1492       C  
-ATOM   9962  OG1 THR B 626     -12.549  25.626  36.487  1.00 43.53           O  
-ANISOU 9962  OG1 THR B 626     6002   3796   6743     53   -583   1502       O  
-ATOM   9963  CG2 THR B 626     -13.917  27.367  35.582  1.00 39.52           C  
-ANISOU 9963  CG2 THR B 626     5348   3428   6239    -46   -386   1727       C  
-ATOM   9964  N   GLN B 627      -9.994  25.103  34.720  1.00 56.62           N  
-ANISOU 9964  N   GLN B 627     7861   5539   8114    300   -674    956       N  
-ATOM   9965  CA  GLN B 627      -8.618  24.647  34.869  1.00 59.24           C  
-ANISOU 9965  CA  GLN B 627     8269   5886   8354    423   -679    748       C  
-ATOM   9966  C   GLN B 627      -7.834  25.125  33.663  1.00 57.99           C  
-ANISOU 9966  C   GLN B 627     8148   5835   8050    517   -635    567       C  
-ATOM   9967  O   GLN B 627      -6.672  25.520  33.767  1.00 56.74           O  
-ANISOU 9967  O   GLN B 627     7992   5778   7788    616   -512    427       O  
-ATOM   9968  CB  GLN B 627      -8.535  23.121  34.987  1.00 64.35           C  
-ANISOU 9968  CB  GLN B 627     9028   6370   9052    441   -919    694       C  
-ATOM   9969  CG  GLN B 627      -9.706  22.363  34.388  1.00 70.36           C  
-ANISOU 9969  CG  GLN B 627     9834   6996   9903    345  -1139    797       C  
-ATOM   9970  CD  GLN B 627     -10.824  22.154  35.392  1.00 73.52           C  
-ANISOU 9970  CD  GLN B 627    10161   7310  10462    223  -1169   1033       C  
-ATOM   9971  OE1 GLN B 627     -11.757  21.388  35.153  1.00 76.62           O  
-ANISOU 9971  OE1 GLN B 627    10588   7578  10947    138  -1363   1136       O  
-ATOM   9972  NE2 GLN B 627     -10.732  22.836  36.529  1.00 74.22           N  
-ANISOU 9972  NE2 GLN B 627    10153   7466  10582    214   -979   1124       N  
-ATOM   9973  N   GLU B 628      -8.500  25.086  32.515  1.00 64.21           N  
-ANISOU 9973  N   GLU B 628     8963   6601   8833    481   -739    579       N  
-ATOM   9974  CA  GLU B 628      -7.940  25.560  31.260  1.00 62.50           C  
-ANISOU 9974  CA  GLU B 628     8779   6482   8487    560   -707    428       C  
-ATOM   9975  C   GLU B 628      -7.605  27.030  31.389  1.00 57.73           C  
-ANISOU 9975  C   GLU B 628     8063   6053   7818    576   -442    441       C  
-ATOM   9976  O   GLU B 628      -6.461  27.434  31.195  1.00 56.33           O  
-ANISOU 9976  O   GLU B 628     7896   5981   7525    683   -336    285       O  
-ATOM   9977  CB  GLU B 628      -8.958  25.356  30.142  1.00 66.98           C  
-ANISOU 9977  CB  GLU B 628     9376   6993   9081    486   -857    488       C  
-ATOM   9978  CG  GLU B 628      -8.403  25.407  28.740  1.00 74.94           C  
-ANISOU 9978  CG  GLU B 628    10462   8053   9959    574   -903    311       C  
-ATOM   9979  CD  GLU B 628      -9.367  24.797  27.735  1.00 82.11           C  
-ANISOU 9979  CD  GLU B 628    11440   8858  10899    498  -1116    356       C  
-ATOM   9980  OE1 GLU B 628     -10.268  24.041  28.167  1.00 84.88           O  
-ANISOU 9980  OE1 GLU B 628    11807   9074  11370    394  -1269    493       O  
-ATOM   9981  OE2 GLU B 628      -9.228  25.070  26.520  1.00 86.57           O  
-ANISOU 9981  OE2 GLU B 628    12044   9478  11371    539  -1135    260       O  
-ATOM   9982  N   PHE B 629      -8.608  27.824  31.741  1.00 52.96           N  
-ANISOU 9982  N   PHE B 629     7353   5479   7290    469   -334    635       N  
-ATOM   9983  CA  PHE B 629      -8.426  29.261  31.876  1.00 49.88           C  
-ANISOU 9983  CA  PHE B 629     6861   5246   6846    472    -77    668       C  
-ATOM   9984  C   PHE B 629      -7.299  29.605  32.835  1.00 50.62           C  
-ANISOU 9984  C   PHE B 629     6942   5411   6882    541     77    585       C  
-ATOM   9985  O   PHE B 629      -6.488  30.491  32.563  1.00 49.05           O  
-ANISOU 9985  O   PHE B 629     6715   5348   6574    605    237    485       O  
-ATOM   9986  CB  PHE B 629      -9.714  29.931  32.353  1.00 45.87           C  
-ANISOU 9986  CB  PHE B 629     6249   4736   6444    348     17    914       C  
-ATOM   9987  CG  PHE B 629      -9.603  31.423  32.470  1.00 40.83           C  
-ANISOU 9987  CG  PHE B 629     5517   4248   5750    348    284    957       C  
-ATOM   9988  CD1 PHE B 629     -10.063  32.246  31.459  1.00 38.61           C  
-ANISOU 9988  CD1 PHE B 629     5187   4052   5432    330    352    989       C  
-ATOM   9989  CD2 PHE B 629      -9.021  32.000  33.585  1.00 38.57           C  
-ANISOU 9989  CD2 PHE B 629     5197   4016   5443    366    467    964       C  
-ATOM   9990  CE1 PHE B 629      -9.953  33.612  31.559  1.00 36.22           C  
-ANISOU 9990  CE1 PHE B 629     4803   3883   5075    332    601   1027       C  
-ATOM   9991  CE2 PHE B 629      -8.908  33.370  33.693  1.00 35.85           C  
-ANISOU 9991  CE2 PHE B 629     4780   3801   5041    363    711   1000       C  
-ATOM   9992  CZ  PHE B 629      -9.374  34.176  32.676  1.00 35.59           C  
-ANISOU 9992  CZ  PHE B 629     4699   3850   4974    347    780   1031       C  
-ATOM   9993  N   PHE B 630      -7.257  28.914  33.967  1.00 46.32           N  
-ANISOU 9993  N   PHE B 630     6538   5265   5795     57     91   -220       N  
-ATOM   9994  CA  PHE B 630      -6.281  29.242  34.990  1.00 47.73           C  
-ANISOU 9994  CA  PHE B 630     6511   5825   5798     83    115   -273       C  
-ATOM   9995  C   PHE B 630      -4.870  28.927  34.512  1.00 43.98           C  
-ANISOU 9995  C   PHE B 630     6092   5226   5391     19    183   -241       C  
-ATOM   9996  O   PHE B 630      -3.959  29.732  34.685  1.00 43.43           O  
-ANISOU 9996  O   PHE B 630     6025   5248   5227    -16    181   -439       O  
-ATOM   9997  CB  PHE B 630      -6.591  28.530  36.307  1.00 55.02           C  
-ANISOU 9997  CB  PHE B 630     7109   7200   6595    184    135    -36       C  
-ATOM   9998  CG  PHE B 630      -5.765  29.023  37.456  1.00 62.52           C  
-ANISOU 9998  CG  PHE B 630     7833   8599   7324    213    143   -124       C  
-ATOM   9999  CD1 PHE B 630      -6.172  30.119  38.199  1.00 65.63           C  
-ANISOU 9999  CD1 PHE B 630     8137   9268   7531    244     85   -385       C  
-ATOM  10000  CD2 PHE B 630      -4.568  28.408  37.777  1.00 64.70           C  
-ANISOU10000  CD2 PHE B 630     7979   9017   7588    207    205     36       C  
-ATOM  10001  CE1 PHE B 630      -5.407  30.583  39.248  1.00 67.63           C  
-ANISOU10001  CE1 PHE B 630     8174   9947   7576    267     90   -489       C  
-ATOM  10002  CE2 PHE B 630      -3.796  28.867  38.822  1.00 67.33           C  
-ANISOU10002  CE2 PHE B 630     8102   9770   7712    229    208    -47       C  
-ATOM  10003  CZ  PHE B 630      -4.215  29.958  39.560  1.00 68.68           C  
-ANISOU10003  CZ  PHE B 630     8185  10228   7683    258    151   -315       C  
-ATOM  10004  N   LEU B 631      -4.691  27.762  33.900  1.00 51.27           N  
-ANISOU10004  N   LEU B 631     7055   5935   6492      4    241     -5       N  
-ATOM  10005  CA  LEU B 631      -3.396  27.402  33.330  1.00 48.60           C  
-ANISOU10005  CA  LEU B 631     6777   5442   6247    -61    310     16       C  
-ATOM  10006  C   LEU B 631      -2.891  28.480  32.381  1.00 46.36           C  
-ANISOU10006  C   LEU B 631     6754   4891   5969   -166    291   -282       C  
-ATOM  10007  O   LEU B 631      -1.756  28.945  32.507  1.00 45.12           O  
-ANISOU10007  O   LEU B 631     6581   4815   5747   -204    316   -399       O  
-ATOM  10008  CB  LEU B 631      -3.479  26.074  32.577  1.00 46.86           C  
-ANISOU10008  CB  LEU B 631     6598   4946   6260    -71    366    258       C  
-ATOM  10009  CG  LEU B 631      -2.235  25.698  31.764  1.00 44.32           C  
-ANISOU10009  CG  LEU B 631     6372   4399   6068   -149    440    244       C  
-ATOM  10010  CD1 LEU B 631      -1.047  25.454  32.672  1.00 43.06           C  
-ANISOU10010  CD1 LEU B 631     5981   4545   5836   -118    487    336       C  
-ATOM  10011  CD2 LEU B 631      -2.504  24.478  30.904  1.00 43.73           C  
-ANISOU10011  CD2 LEU B 631     6355   4016   6245   -162    484    427       C  
-ATOM  10012  N   ILE B 632      -3.736  28.872  31.432  1.00 45.38           N  
-ANISOU10012  N   ILE B 632     6863   4452   5926   -216    242   -391       N  
-ATOM  10013  CA  ILE B 632      -3.354  29.866  30.437  1.00 45.12           C  
-ANISOU10013  CA  ILE B 632     7083   4146   5915   -328    214   -640       C  
-ATOM  10014  C   ILE B 632      -3.022  31.221  31.060  1.00 45.75           C  
-ANISOU10014  C   ILE B 632     7122   4421   5840   -331    156   -896       C  
-ATOM  10015  O   ILE B 632      -2.039  31.856  30.687  1.00 45.59           O  
-ANISOU10015  O   ILE B 632     7189   4323   5809   -410    166  -1050       O  
-ATOM  10016  CB  ILE B 632      -4.438  30.030  29.354  1.00 44.32           C  
-ANISOU10016  CB  ILE B 632     7221   3694   5924   -380    157   -686       C  
-ATOM  10017  CG1 ILE B 632      -4.036  29.268  28.096  1.00 42.74           C  
-ANISOU10017  CG1 ILE B 632     7193   3164   5883   -467    220   -607       C  
-ATOM  10018  CG2 ILE B 632      -4.624  31.486  29.000  1.00 44.46           C  
-ANISOU10018  CG2 ILE B 632     7398   3602   5892   -446     68   -961       C  
-ATOM  10019  CD1 ILE B 632      -3.593  27.850  28.356  1.00 43.06           C  
-ANISOU10019  CD1 ILE B 632     7070   3275   6017   -415    313   -357       C  
-ATOM  10020  N   VAL B 633      -3.834  31.662  32.014  1.00 46.04           N  
-ANISOU10020  N   VAL B 633     7013   4714   5765   -248     95   -949       N  
-ATOM  10021  CA  VAL B 633      -3.599  32.952  32.649  1.00 48.94           C  
-ANISOU10021  CA  VAL B 633     7318   5274   6003   -245     34  -1219       C  
-ATOM  10022  C   VAL B 633      -2.425  32.895  33.620  1.00 52.17           C  
-ANISOU10022  C   VAL B 633     7507   6035   6279   -213     86  -1215       C  
-ATOM  10023  O   VAL B 633      -1.686  33.864  33.768  1.00 54.34           O  
-ANISOU10023  O   VAL B 633     7786   6367   6495   -252     62  -1441       O  
-ATOM  10024  CB  VAL B 633      -4.847  33.468  33.374  1.00 49.08           C  
-ANISOU10024  CB  VAL B 633     7233   5470   5945   -166    -46  -1311       C  
-ATOM  10025  CG1 VAL B 633      -4.535  34.767  34.073  1.00 51.28           C  
-ANISOU10025  CG1 VAL B 633     7417   5959   6108   -159   -106  -1612       C  
-ATOM  10026  CG2 VAL B 633      -5.970  33.670  32.383  1.00 50.50           C  
-ANISOU10026  CG2 VAL B 633     7637   5285   6264   -205   -110  -1340       C  
-ATOM  10027  N   LYS B 634      -2.252  31.757  34.281  1.00 45.64           N  
-ANISOU10027  N   LYS B 634     6482   5444   5417   -144    151   -949       N  
-ATOM  10028  CA  LYS B 634      -1.102  31.566  35.151  1.00 48.06           C  
-ANISOU10028  CA  LYS B 634     6576   6078   5608   -119    201   -902       C  
-ATOM  10029  C   LYS B 634       0.175  31.624  34.322  1.00 46.49           C  
-ANISOU10029  C   LYS B 634     6523   5639   5501   -215    252   -957       C  
-ATOM  10030  O   LYS B 634       1.102  32.374  34.632  1.00 47.00           O  
-ANISOU10030  O   LYS B 634     6546   5829   5481   -243    248  -1136       O  
-ATOM  10031  CB  LYS B 634      -1.192  30.219  35.862  1.00 52.85           C  
-ANISOU10031  CB  LYS B 634     6952   6926   6202    -40    256   -557       C  
-ATOM  10032  CG  LYS B 634      -0.082  29.975  36.866  1.00 59.65           C  
-ANISOU10032  CG  LYS B 634     7562   8168   6934     -8    297   -475       C  
-ATOM  10033  CD  LYS B 634       0.040  28.497  37.179  1.00 64.73           C  
-ANISOU10033  CD  LYS B 634     8032   8908   7656     39    357    -89       C  
-ATOM  10034  CE  LYS B 634       0.960  28.252  38.363  1.00 71.10           C  
-ANISOU10034  CE  LYS B 634     8543  10162   8308     81    381     26       C  
-ATOM  10035  NZ  LYS B 634       0.383  28.764  39.645  1.00 73.99           N  
-ANISOU10035  NZ  LYS B 634     8679  11012   8420    151    329    -33       N  
-ATOM  10036  N   THR B 635       0.210  30.826  33.259  1.00 53.23           N  
-ANISOU10036  N   THR B 635     7541   6153   6532   -266    302   -813       N  
-ATOM  10037  CA  THR B 635       1.373  30.749  32.387  1.00 52.82           C  
-ANISOU10037  CA  THR B 635     7626   5867   6578   -361    363   -850       C  
-ATOM  10038  C   THR B 635       1.725  32.109  31.803  1.00 52.78           C  
-ANISOU10038  C   THR B 635     7809   5696   6550   -455    313  -1153       C  
-ATOM  10039  O   THR B 635       2.887  32.513  31.819  1.00 53.15           O  
-ANISOU10039  O   THR B 635     7844   5783   6566   -504    342  -1257       O  
-ATOM  10040  CB  THR B 635       1.144  29.762  31.237  1.00 51.92           C  
-ANISOU10040  CB  THR B 635     7671   5397   6660   -407    414   -692       C  
-ATOM  10041  OG1 THR B 635       0.939  28.449  31.770  1.00 54.61           O  
-ANISOU10041  OG1 THR B 635     7818   5870   7061   -323    460   -398       O  
-ATOM  10042  CG2 THR B 635       2.344  29.737  30.316  1.00 53.87           C  
-ANISOU10042  CG2 THR B 635     8054   5421   6994   -512    481   -758       C  
-ATOM  10043  N   LEU B 636       0.722  32.817  31.289  1.00 47.91           N  
-ANISOU10043  N   LEU B 636     7356   4886   5962   -483    234  -1284       N  
-ATOM  10044  CA  LEU B 636       0.949  34.144  30.723  1.00 48.35           C  
-ANISOU10044  CA  LEU B 636     7582   4765   6025   -575    170  -1552       C  
-ATOM  10045  C   LEU B 636       1.591  35.070  31.741  1.00 54.48           C  
-ANISOU10045  C   LEU B 636     8189   5842   6670   -545    137  -1746       C  
-ATOM  10046  O   LEU B 636       2.638  35.653  31.477  1.00 55.68           O  
-ANISOU10046  O   LEU B 636     8390   5938   6826   -620    149  -1878       O  
-ATOM  10047  CB  LEU B 636      -0.352  34.762  30.206  1.00 45.47           C  
-ANISOU10047  CB  LEU B 636     7373   4187   5716   -592     73  -1646       C  
-ATOM  10048  CG  LEU B 636      -0.981  34.099  28.974  1.00 41.98           C  
-ANISOU10048  CG  LEU B 636     7146   3393   5410   -652     88  -1511       C  
-ATOM  10049  CD1 LEU B 636      -2.013  35.019  28.335  1.00 37.52           C  
-ANISOU10049  CD1 LEU B 636     6762   2590   4904   -701    -23  -1651       C  
-ATOM  10050  CD2 LEU B 636       0.089  33.697  27.962  1.00 41.19           C  
-ANISOU10050  CD2 LEU B 636     7185   3079   5386   -761    170  -1469       C  
-ATOM  10051  N   TYR B 637       0.959  35.197  32.905  1.00 38.64           N  
-ANISOU10051  N   TYR B 637     5974   4164   4542   -438     96  -1768       N  
-ATOM  10052  CA  TYR B 637       1.472  36.051  33.971  1.00 43.69           C  
-ANISOU10052  CA  TYR B 637     6423   5135   5043   -400     61  -1971       C  
-ATOM  10053  C   TYR B 637       2.926  35.726  34.259  1.00 44.15           C  
-ANISOU10053  C   TYR B 637     6379   5344   5053   -419    138  -1920       C  
-ATOM  10054  O   TYR B 637       3.746  36.620  34.457  1.00 46.38           O  
-ANISOU10054  O   TYR B 637     6635   5690   5297   -458    115  -2132       O  
-ATOM  10055  CB  TYR B 637       0.642  35.889  35.249  1.00 51.40           C  
-ANISOU10055  CB  TYR B 637     7148   6511   5870   -277     33  -1941       C  
-ATOM  10056  CG  TYR B 637       1.138  36.729  36.409  1.00 62.19           C  
-ANISOU10056  CG  TYR B 637     8291   8266   7074   -234     -1  -2166       C  
-ATOM  10057  CD1 TYR B 637       0.700  38.037  36.580  1.00 66.35           C  
-ANISOU10057  CD1 TYR B 637     8824   8786   7599   -239    -98  -2489       C  
-ATOM  10058  CD2 TYR B 637       2.047  36.217  37.328  1.00 65.72           C  
-ANISOU10058  CD2 TYR B 637     8508   9082   7380   -192     58  -2062       C  
-ATOM  10059  CE1 TYR B 637       1.151  38.813  37.634  1.00 68.72           C  
-ANISOU10059  CE1 TYR B 637     8907   9442   7760   -201   -130  -2724       C  
-ATOM  10060  CE2 TYR B 637       2.508  36.986  38.386  1.00 68.21           C  
-ANISOU10060  CE2 TYR B 637     8611   9771   7535   -157     25  -2281       C  
-ATOM  10061  CZ  TYR B 637       2.055  38.284  38.535  1.00 69.77           C  
-ANISOU10061  CZ  TYR B 637     8818   9959   7732   -161    -67  -2623       C  
-ATOM  10062  OH  TYR B 637       2.502  39.057  39.583  1.00 71.77           O  
-ANISOU10062  OH  TYR B 637     8848  10585   7836   -126   -102  -2869       O  
-ATOM  10063  N   HIS B 638       3.242  34.438  34.280  1.00 66.89           N  
-ANISOU10063  N   HIS B 638     9192   8272   7953   -393    225  -1638       N  
-ATOM  10064  CA  HIS B 638       4.602  34.002  34.554  1.00 67.94           C  
-ANISOU10064  CA  HIS B 638     9213   8541   8060   -405    300  -1560       C  
-ATOM  10065  C   HIS B 638       5.573  34.476  33.477  1.00 64.63           C  
-ANISOU10065  C   HIS B 638     9004   7803   7750   -529    326  -1688       C  
-ATOM  10066  O   HIS B 638       6.703  34.863  33.774  1.00 64.62           O  
-ANISOU10066  O   HIS B 638     8930   7922   7701   -556    347  -1787       O  
-ATOM  10067  CB  HIS B 638       4.661  32.484  34.663  1.00 71.27           C  
-ANISOU10067  CB  HIS B 638     9529   9015   8534   -357    380  -1220       C  
-ATOM  10068  CG  HIS B 638       6.052  31.948  34.767  1.00 76.60           C  
-ANISOU10068  CG  HIS B 638    10110   9764   9231   -379    459  -1122       C  
-ATOM  10069  ND1 HIS B 638       6.466  30.815  34.102  1.00 78.64           N  
-ANISOU10069  ND1 HIS B 638    10411   9817   9650   -403    541   -905       N  
-ATOM  10070  CD2 HIS B 638       7.130  32.398  35.453  1.00 80.33           C  
-ANISOU10070  CD2 HIS B 638    10438  10488   9596   -380    465  -1223       C  
-ATOM  10071  CE1 HIS B 638       7.738  30.587  34.376  1.00 81.83           C  
-ANISOU10071  CE1 HIS B 638    10702  10338  10050   -417    595   -871       C  
-ATOM  10072  NE2 HIS B 638       8.164  31.532  35.195  1.00 82.15           N  
-ANISOU10072  NE2 HIS B 638    10631  10659   9923   -404    550  -1055       N  
-ATOM  10073  N   LEU B 639       5.132  34.433  32.223  1.00 58.38           N  
-ANISOU10073  N   LEU B 639     8467   6618   7098   -607    327  -1680       N  
-ATOM  10074  CA  LEU B 639       5.933  34.940  31.115  1.00 57.34           C  
-ANISOU10074  CA  LEU B 639     8546   6182   7060   -738    346  -1799       C  
-ATOM  10075  C   LEU B 639       6.054  36.454  31.217  1.00 58.56           C  
-ANISOU10075  C   LEU B 639     8743   6332   7177   -785    255  -2089       C  
-ATOM  10076  O   LEU B 639       7.148  37.008  31.113  1.00 58.66           O  
-ANISOU10076  O   LEU B 639     8762   6337   7189   -850    271  -2212       O  
-ATOM  10077  CB  LEU B 639       5.303  34.552  29.777  1.00 54.87           C  
-ANISOU10077  CB  LEU B 639     8481   5485   6883   -814    358  -1721       C  
-ATOM  10078  CG  LEU B 639       5.343  33.061  29.442  1.00 54.28           C  
-ANISOU10078  CG  LEU B 639     8386   5342   6896   -791    455  -1463       C  
-ATOM  10079  CD1 LEU B 639       4.372  32.720  28.317  1.00 53.71           C  
-ANISOU10079  CD1 LEU B 639     8528   4945   6936   -840    443  -1404       C  
-ATOM  10080  CD2 LEU B 639       6.762  32.649  29.096  1.00 52.60           C  
-ANISOU10080  CD2 LEU B 639     8161   5094   6730   -852    553  -1435       C  
-ATOM  10081  N   LYS B 640       4.920  37.115  31.428  1.00 54.95           N  
-ANISOU10081  N   LYS B 640     8302   5871   6706   -749    158  -2200       N  
-ATOM  10082  CA  LYS B 640       4.889  38.558  31.619  1.00 59.23           C  
-ANISOU10082  CA  LYS B 640     8852   6409   7244   -779     57  -2486       C  
-ATOM  10083  C   LYS B 640       5.876  38.979  32.702  1.00 63.89           C  
-ANISOU10083  C   LYS B 640     9219   7338   7719   -738     63  -2619       C  
-ATOM  10084  O   LYS B 640       6.506  40.028  32.605  1.00 66.25           O  
-ANISOU10084  O   LYS B 640     9543   7579   8051   -802     18  -2836       O  
-ATOM  10085  CB  LYS B 640       3.471  39.011  31.980  1.00 59.38           C  
-ANISOU10085  CB  LYS B 640     8847   6457   7256   -712    -41  -2570       C  
-ATOM  10086  CG  LYS B 640       3.294  40.520  32.110  1.00 61.03           C  
-ANISOU10086  CG  LYS B 640     9062   6617   7509   -742   -160  -2877       C  
-ATOM  10087  CD  LYS B 640       3.684  41.018  33.493  1.00 62.49           C  
-ANISOU10087  CD  LYS B 640     8972   7211   7559   -656   -181  -3059       C  
-ATOM  10088  CE  LYS B 640       3.418  42.509  33.644  1.00 62.64           C  
-ANISOU10088  CE  LYS B 640     8977   7168   7655   -677   -306  -3388       C  
-ATOM  10089  NZ  LYS B 640       4.159  43.315  32.634  1.00 62.62           N  
-ANISOU10089  NZ  LYS B 640     9162   6821   7808   -815   -338  -3488       N  
-ATOM  10090  N   SER B 641       6.015  38.147  33.727  1.00 64.87           N  
-ANISOU10090  N   SER B 641     9115   7818   7714   -636    117  -2478       N  
-ATOM  10091  CA  SER B 641       6.877  38.465  34.858  1.00 70.79           C  
-ANISOU10091  CA  SER B 641     9625   8943   8328   -588    120  -2588       C  
-ATOM  10092  C   SER B 641       8.361  38.300  34.539  1.00 73.96           C  
-ANISOU10092  C   SER B 641    10045   9295   8760   -659    194  -2560       C  
-ATOM  10093  O   SER B 641       9.183  39.123  34.937  1.00 75.48           O  
-ANISOU10093  O   SER B 641    10158   9607   8915   -683    168  -2761       O  
-ATOM  10094  CB  SER B 641       6.499  37.607  36.064  1.00 71.52           C  
-ANISOU10094  CB  SER B 641     9456   9457   8262   -463    147  -2418       C  
-ATOM  10095  OG  SER B 641       5.169  37.880  36.468  1.00 69.47           O  
-ANISOU10095  OG  SER B 641     9152   9285   7957   -396     77  -2480       O  
-ATOM  10096  N   GLU B 642       8.697  37.232  33.823  1.00 90.86           N  
-ANISOU10096  N   GLU B 642    12281  11261  10979   -693    286  -2321       N  
-ATOM  10097  CA  GLU B 642      10.084  36.956  33.468  1.00 94.71           C  
-ANISOU10097  CA  GLU B 642    12783  11693  11510   -760    367  -2280       C  
-ATOM  10098  C   GLU B 642      10.599  37.914  32.398  1.00 93.68           C  
-ANISOU10098  C   GLU B 642    12875  11231  11488   -895    347  -2466       C  
-ATOM  10099  O   GLU B 642      11.709  38.431  32.501  1.00 94.17           O  
-ANISOU10099  O   GLU B 642    12896  11341  11543   -944    360  -2587       O  
-ATOM  10100  CB  GLU B 642      10.238  35.508  33.001  1.00 97.05           C  
-ANISOU10100  CB  GLU B 642    13101  11890  11883   -754    470  -1987       C  
-ATOM  10101  CG  GLU B 642      10.092  34.478  34.107  1.00105.34           C  
-ANISOU10101  CG  GLU B 642    13892  13289  12845   -632    500  -1762       C  
-ATOM  10102  CD  GLU B 642      10.085  33.053  33.581  1.00109.03           C  
-ANISOU10102  CD  GLU B 642    14380  13607  13439   -624    587  -1473       C  
-ATOM  10103  OE1 GLU B 642       9.271  32.756  32.680  1.00110.89           O  
-ANISOU10103  OE1 GLU B 642    14800  13551  13782   -655    589  -1420       O  
-ATOM  10104  OE2 GLU B 642      10.891  32.229  34.069  1.00111.46           O  
-ANISOU10104  OE2 GLU B 642    14512  14087  13752   -588    649  -1304       O  
-ATOM  10105  N   PHE B 643       9.784  38.151  31.375  1.00 80.65           N  
-ANISOU10105  N   PHE B 643    11452   9252   9939   -961    311  -2477       N  
-ATOM  10106  CA  PHE B 643      10.176  39.028  30.275  1.00 79.70           C  
-ANISOU10106  CA  PHE B 643    11548   8810   9925  -1102    286  -2615       C  
-ATOM  10107  C   PHE B 643      10.236  40.498  30.683  1.00 82.02           C  
-ANISOU10107  C   PHE B 643    11801   9144  10217  -1121    175  -2893       C  
-ATOM  10108  O   PHE B 643      11.110  41.237  30.230  1.00 84.42           O  
-ANISOU10108  O   PHE B 643    12174   9321  10582  -1222    167  -3017       O  
-ATOM  10109  CB  PHE B 643       9.254  38.834  29.069  1.00 74.32           C  
-ANISOU10109  CB  PHE B 643    11110   7786   9344  -1171    272  -2530       C  
-ATOM  10110  CG  PHE B 643       9.633  37.665  28.210  1.00 68.74           C  
-ANISOU10110  CG  PHE B 643    10502   6925   8692  -1219    389  -2329       C  
-ATOM  10111  CD1 PHE B 643       9.471  36.371  28.669  1.00 66.29           C  
-ANISOU10111  CD1 PHE B 643    10065   6763   8359  -1121    462  -2123       C  
-ATOM  10112  CD2 PHE B 643      10.162  37.859  26.947  1.00 66.81           C  
-ANISOU10112  CD2 PHE B 643    10460   6396   8528  -1366    423  -2348       C  
-ATOM  10113  CE1 PHE B 643       9.826  35.292  27.887  1.00 62.27           C  
-ANISOU10113  CE1 PHE B 643     9629   6101   7931  -1162    566  -1961       C  
-ATOM  10114  CE2 PHE B 643      10.518  36.782  26.156  1.00 63.73           C  
-ANISOU10114  CE2 PHE B 643    10146   5880   8190  -1411    535  -2194       C  
-ATOM  10115  CZ  PHE B 643      10.349  35.497  26.627  1.00 61.48           C  
-ANISOU10115  CZ  PHE B 643     9730   5724   7905  -1306    606  -2010       C  
-ATOM  10116  N   GLN B 644       9.308  40.920  31.534  1.00 88.84           N  
-ANISOU10116  N   GLN B 644    12545  10185  11025  -1026     89  -2996       N  
-ATOM  10117  CA  GLN B 644       9.342  42.273  32.074  1.00 89.37           C  
-ANISOU10117  CA  GLN B 644    12528  10326  11104  -1026    -18  -3285       C  
-ATOM  10118  C   GLN B 644      10.603  42.435  32.915  1.00 88.78           C  
-ANISOU10118  C   GLN B 644    12256  10534  10941  -1005     17  -3381       C  
-ATOM  10119  O   GLN B 644      11.143  43.531  33.042  1.00 91.54           O  
-ANISOU10119  O   GLN B 644    12573  10867  11341  -1051    -46  -3614       O  
-ATOM  10120  CB  GLN B 644       8.104  42.538  32.931  1.00 93.47           C  
-ANISOU10120  CB  GLN B 644    12918  11032  11563   -914   -102  -3379       C  
-ATOM  10121  CG  GLN B 644       8.040  43.933  33.531  1.00101.26           C  
-ANISOU10121  CG  GLN B 644    13793  12097  12583   -904   -218  -3709       C  
-ATOM  10122  CD  GLN B 644       7.653  44.993  32.516  1.00102.36           C  
-ANISOU10122  CD  GLN B 644    14137  11829  12927  -1013   -319  -3840       C  
-ATOM  10123  OE1 GLN B 644       6.675  44.842  31.781  1.00104.61           O  
-ANISOU10123  OE1 GLN B 644    14587  11869  13290  -1036   -350  -3740       O  
-ATOM  10124  NE2 GLN B 644       8.425  46.073  32.467  1.00103.09           N  
-ANISOU10124  NE2 GLN B 644    14211  11845  13115  -1083   -376  -4055       N  
-ATOM  10125  N   ALA B 645      11.070  41.325  33.478  1.00 62.84           N  
-ANISOU10125  N   ALA B 645     8833   7502   7541   -937    113  -3191       N  
-ATOM  10126  CA  ALA B 645      12.248  41.322  34.340  1.00 62.09           C  
-ANISOU10126  CA  ALA B 645     8532   7710   7348   -909    150  -3245       C  
-ATOM  10127  C   ALA B 645      13.520  41.216  33.519  1.00 58.99           C  
-ANISOU10127  C   ALA B 645     8254   7117   7042  -1020    226  -3199       C  
-ATOM  10128  O   ALA B 645      14.620  41.449  34.020  1.00 60.32           O  
-ANISOU10128  O   ALA B 645     8292   7459   7169  -1027    246  -3283       O  
-ATOM  10129  CB  ALA B 645      12.171  40.173  35.327  1.00 65.42           C  
-ANISOU10129  CB  ALA B 645     8739   8501   7617   -791    211  -3038       C  
-ATOM  10130  N   ILE B 646      13.362  40.854  32.253  1.00 73.12           N  
-ANISOU10130  N   ILE B 646    10282   8552   8948  -1110    269  -3071       N  
-ATOM  10131  CA  ILE B 646      14.498  40.621  31.376  1.00 70.23           C  
-ANISOU10131  CA  ILE B 646    10030   7994   8659  -1221    355  -3010       C  
-ATOM  10132  C   ILE B 646      14.766  41.847  30.505  1.00 70.34           C  
-ANISOU10132  C   ILE B 646    10217   7719   8790  -1358    293  -3193       C  
-ATOM  10133  O   ILE B 646      15.807  41.944  29.856  1.00 68.78           O  
-ANISOU10133  O   ILE B 646    10095   7390   8649  -1462    350  -3195       O  
-ATOM  10134  CB  ILE B 646      14.263  39.364  30.507  1.00 66.28           C  
-ANISOU10134  CB  ILE B 646     9663   7311   8210  -1243    453  -2755       C  
-ATOM  10135  CG1 ILE B 646      15.451  38.409  30.604  1.00 63.14           C  
-ANISOU10135  CG1 ILE B 646     9165   7018   7806  -1240    574  -2616       C  
-ATOM  10136  CG2 ILE B 646      13.950  39.740  29.068  1.00 64.20           C  
-ANISOU10136  CG2 ILE B 646     9677   6652   8064  -1379    442  -2771       C  
-ATOM  10137  CD1 ILE B 646      15.184  37.060  29.978  1.00 59.37           C  
-ANISOU10137  CD1 ILE B 646     8755   6411   7391  -1233    668  -2374       C  
-ATOM  10138  N   ILE B 647      13.827  42.788  30.517  1.00 68.42           N  
-ANISOU10138  N   ILE B 647    10021   7384   8591  -1357    173  -3343       N  
-ATOM  10139  CA  ILE B 647      13.934  44.006  29.718  1.00 71.24           C  
-ANISOU10139  CA  ILE B 647    10528   7455   9086  -1486     91  -3500       C  
-ATOM  10140  C   ILE B 647      15.318  44.670  29.773  1.00 76.44           C  
-ANISOU10140  C   ILE B 647    11127   8136   9779  -1561    104  -3633       C  
-ATOM  10141  O   ILE B 647      15.904  44.965  28.731  1.00 76.08           O  
-ANISOU10141  O   ILE B 647    11242   7835   9829  -1701    126  -3610       O  
-ATOM  10142  CB  ILE B 647      12.841  45.030  30.099  1.00 69.30           C  
-ANISOU10142  CB  ILE B 647    10254   7182   8894  -1445    -56  -3688       C  
-ATOM  10143  CG1 ILE B 647      11.477  44.568  29.586  1.00 64.93           C  
-ANISOU10143  CG1 ILE B 647     9838   6473   8359  -1424    -79  -3552       C  
-ATOM  10144  CG2 ILE B 647      13.175  46.403  29.543  1.00 67.83           C  
-ANISOU10144  CG2 ILE B 647    10150   6751   8872  -1567   -155  -3874       C  
-ATOM  10145  CD1 ILE B 647      10.354  45.529  29.910  1.00 63.29           C  
-ANISOU10145  CD1 ILE B 647     9604   6221   8224  -1384   -223  -3731       C  
-ATOM  10146  N   PRO B 648      15.847  44.906  30.986  1.00 87.13           N  
-ANISOU10146  N   PRO B 648    12244   9809  11051  -1472     89  -3771       N  
-ATOM  10147  CA  PRO B 648      17.167  45.537  31.102  1.00 90.77           C  
-ANISOU10147  CA  PRO B 648    12635  10305  11550  -1538     97  -3906       C  
-ATOM  10148  C   PRO B 648      18.215  44.896  30.198  1.00 93.23           C  
-ANISOU10148  C   PRO B 648    13064  10473  11886  -1642    221  -3742       C  
-ATOM  10149  O   PRO B 648      18.758  45.560  29.316  1.00 94.35           O  
-ANISOU10149  O   PRO B 648    13339  10367  12143  -1780    210  -3790       O  
-ATOM  10150  CB  PRO B 648      17.532  45.294  32.565  1.00 91.98           C  
-ANISOU10150  CB  PRO B 648    12505  10891  11553  -1404    106  -3981       C  
-ATOM  10151  CG  PRO B 648      16.224  45.286  33.262  1.00 90.24           C  
-ANISOU10151  CG  PRO B 648    12202  10823  11263  -1288     34  -4022       C  
-ATOM  10152  CD  PRO B 648      15.254  44.637  32.309  1.00 87.17           C  
-ANISOU10152  CD  PRO B 648    12027  10174  10918  -1314     60  -3815       C  
-ATOM  10153  N   ALA B 649      18.494  43.618  30.426  1.00 83.12           N  
-ANISOU10153  N   ALA B 649    11722   9352  10509  -1578    336  -3549       N  
-ATOM  10154  CA  ALA B 649      19.523  42.910  29.677  1.00 83.36           C  
-ANISOU10154  CA  ALA B 649    11828   9279  10567  -1661    463  -3408       C  
-ATOM  10155  C   ALA B 649      19.274  43.005  28.175  1.00 81.21           C  
-ANISOU10155  C   ALA B 649    11823   8635  10398  -1807    482  -3338       C  
-ATOM  10156  O   ALA B 649      20.212  43.093  27.385  1.00 80.61           O  
-ANISOU10156  O   ALA B 649    11834   8416  10377  -1929    546  -3327       O  
-ATOM  10157  CB  ALA B 649      19.593  41.458  30.120  1.00 82.39           C  
-ANISOU10157  CB  ALA B 649    11595   9349  10359  -1560    567  -3196       C  
-ATOM  10158  N   VAL B 650      18.004  42.996  27.787  1.00 87.92           N  
-ANISOU10158  N   VAL B 650    12797   9344  11266  -1796    425  -3290       N  
-ATOM  10159  CA  VAL B 650      17.637  43.125  26.384  1.00 86.26           C  
-ANISOU10159  CA  VAL B 650    12835   8801  11138  -1935    427  -3222       C  
-ATOM  10160  C   VAL B 650      18.151  44.432  25.794  1.00 85.63           C  
-ANISOU10160  C   VAL B 650    12841   8534  11161  -2080    355  -3362       C  
-ATOM  10161  O   VAL B 650      18.881  44.431  24.806  1.00 82.96           O  
-ANISOU10161  O   VAL B 650    12624   8035  10862  -2220    420  -3310       O  
-ATOM  10162  CB  VAL B 650      16.111  43.062  26.189  1.00 86.19           C  
-ANISOU10162  CB  VAL B 650    12925   8685  11137  -1893    351  -3170       C  
-ATOM  10163  CG1 VAL B 650      15.761  43.253  24.722  1.00 87.85           C  
-ANISOU10163  CG1 VAL B 650    13388   8567  11425  -2048    344  -3098       C  
-ATOM  10164  CG2 VAL B 650      15.568  41.742  26.703  1.00 84.95           C  
-ANISOU10164  CG2 VAL B 650    12686   8695  10896  -1759    421  -3009       C  
-ATOM  10165  N   ASN B 651      17.766  45.546  26.406  1.00 84.36           N  
-ANISOU10165  N   ASN B 651    12604   8397  11052  -2048    219  -3542       N  
-ATOM  10166  CA  ASN B 651      18.155  46.863  25.915  1.00 85.15           C  
-ANISOU10166  CA  ASN B 651    12764   8302  11286  -2180    128  -3676       C  
-ATOM  10167  C   ASN B 651      19.667  47.056  25.830  1.00 87.19           C  
-ANISOU10167  C   ASN B 651    12968   8601  11561  -2261    198  -3719       C  
-ATOM  10168  O   ASN B 651      20.153  47.845  25.021  1.00 88.22           O  
-ANISOU10168  O   ASN B 651    13198   8524  11799  -2413    167  -3746       O  
-ATOM  10169  CB  ASN B 651      17.544  47.968  26.786  1.00 88.48           C  
-ANISOU10169  CB  ASN B 651    13060   8776  11782  -2107    -29  -3894       C  
-ATOM  10170  CG  ASN B 651      16.046  48.105  26.596  1.00 87.62           C  
-ANISOU10170  CG  ASN B 651    13041   8539  11713  -2072   -125  -3872       C  
-ATOM  10171  OD1 ASN B 651      15.526  47.892  25.503  1.00 91.25           O  
-ANISOU10171  OD1 ASN B 651    13675   8797  12199  -2144   -107  -3681       O  
-ATOM  10172  ND2 ASN B 651      15.346  48.470  27.661  1.00 88.01           N  
-ANISOU10172  ND2 ASN B 651    12931   8755  11752  -1940   -213  -4029       N  
-ATOM  10173  N   SER B 652      20.409  46.333  26.661  1.00 80.49           N  
-ANISOU10173  N   SER B 652    11954   8021  10609  -2165    290  -3713       N  
-ATOM  10174  CA  SER B 652      21.842  46.578  26.793  1.00 84.38           C  
-ANISOU10174  CA  SER B 652    12356   8587  11118  -2220    345  -3782       C  
-ATOM  10175  C   SER B 652      22.718  45.522  26.128  1.00 85.66           C  
-ANISOU10175  C   SER B 652    12576   8736  11233  -2280    509  -3615       C  
-ATOM  10176  O   SER B 652      23.940  45.651  26.110  1.00 88.38           O  
-ANISOU10176  O   SER B 652    12861   9124  11597  -2338    568  -3655       O  
-ATOM  10177  CB  SER B 652      22.223  46.723  28.269  1.00 86.44           C  
-ANISOU10177  CB  SER B 652    12356   9174  11313  -2081    313  -3932       C  
-ATOM  10178  OG  SER B 652      21.762  45.618  29.028  1.00 83.99           O  
-ANISOU10178  OG  SER B 652    11940   9107  10865  -1933    368  -3824       O  
-ATOM  10179  N   HIS B 653      22.096  44.486  25.576  1.00 96.94           N  
-ANISOU10179  N   HIS B 653    14115  10103  12615  -2266    583  -3440       N  
-ATOM  10180  CA  HIS B 653      22.845  43.419  24.917  1.00 96.80           C  
-ANISOU10180  CA  HIS B 653    14143  10064  12574  -2316    741  -3298       C  
-ATOM  10181  C   HIS B 653      22.307  43.115  23.526  1.00 93.90           C  
-ANISOU10181  C   HIS B 653    14007   9440  12229  -2438    779  -3180       C  
-ATOM  10182  O   HIS B 653      23.032  43.219  22.539  1.00 92.18           O  
-ANISOU10182  O   HIS B 653    13894   9089  12043  -2588    846  -3160       O  
-ATOM  10183  CB  HIS B 653      22.843  42.153  25.773  1.00100.01           C  
-ANISOU10183  CB  HIS B 653    14391  10707  12901  -2159    820  -3193       C  
-ATOM  10184  CG  HIS B 653      23.591  42.301  27.061  1.00104.30           C  
-ANISOU10184  CG  HIS B 653    14695  11534  13400  -2058    805  -3284       C  
-ATOM  10185  ND1 HIS B 653      23.360  41.490  28.151  1.00106.13           N  
-ANISOU10185  ND1 HIS B 653    14743  12032  13549  -1898    819  -3210       N  
-ATOM  10186  CD2 HIS B 653      24.566  43.161  27.431  1.00106.94           C  
-ANISOU10186  CD2 HIS B 653    14936  11938  13760  -2098    775  -3436       C  
-ATOM  10187  CE1 HIS B 653      24.160  41.848  29.140  1.00108.96           C  
-ANISOU10187  CE1 HIS B 653    14905  12627  13869  -1845    797  -3315       C  
-ATOM  10188  NE2 HIS B 653      24.903  42.861  28.727  1.00109.43           N  
-ANISOU10188  NE2 HIS B 653    15016  12567  13997  -1962    771  -3462       N  
-ATOM  10189  N   ILE B 654      21.036  42.739  23.451  1.00 90.71           N  
-ANISOU10189  N   ILE B 654    13676   8985  11804  -2376    737  -3104       N  
-ATOM  10190  CA  ILE B 654      20.415  42.440  22.170  1.00 87.36           C  
-ANISOU10190  CA  ILE B 654    13466   8335  11393  -2485    762  -2997       C  
-ATOM  10191  C   ILE B 654      20.446  43.651  21.242  1.00 89.54           C  
-ANISOU10191  C   ILE B 654    13895   8394  11734  -2662    680  -3051       C  
-ATOM  10192  O   ILE B 654      20.014  44.743  21.613  1.00 87.77           O  
-ANISOU10192  O   ILE B 654    13645   8139  11563  -2650    543  -3139       O  
-ATOM  10193  CB  ILE B 654      18.966  41.970  22.340  1.00 85.13           C  
-ANISOU10193  CB  ILE B 654    13226   8033  11088  -2383    707  -2921       C  
-ATOM  10194  CG1 ILE B 654      18.894  40.847  23.374  1.00 82.27           C  
-ANISOU10194  CG1 ILE B 654    12686   7902  10672  -2205    770  -2851       C  
-ATOM  10195  CG2 ILE B 654      18.398  41.508  21.004  1.00 84.64           C  
-ANISOU10195  CG2 ILE B 654    13372   7757  11031  -2494    748  -2807       C  
-ATOM  10196  CD1 ILE B 654      17.517  40.237  23.516  1.00 80.03           C  
-ANISOU10196  CD1 ILE B 654    12433   7606  10368  -2105    734  -2753       C  
-ATOM  10197  N   GLN B 655      20.954  43.440  20.030  1.00 88.22           N  
-ANISOU10197  N   GLN B 655    13850   8114  11555  -2811    773  -2965       N  
-ATOM  10198  CA  GLN B 655      21.116  44.513  19.054  1.00 91.81           C  
-ANISOU10198  CA  GLN B 655    14402   8446  12036  -2963    725  -2925       C  
-ATOM  10199  C   GLN B 655      20.155  44.366  17.881  1.00 90.19           C  
-ANISOU10199  C   GLN B 655    14362   8127  11779  -3027    720  -2760       C  
-ATOM  10200  O   GLN B 655      19.752  45.353  17.273  1.00 91.21           O  
-ANISOU10200  O   GLN B 655    14570   8149  11936  -3112    620  -2711       O  
-ATOM  10201  CB  GLN B 655      22.557  44.549  18.541  1.00 98.98           C  
-ANISOU10201  CB  GLN B 655    15309   9350  12950  -3105    831  -2959       C  
-ATOM  10202  CG  GLN B 655      23.565  45.064  19.556  1.00111.81           C  
-ANISOU10202  CG  GLN B 655    16781  11063  14639  -3077    805  -3129       C  
-ATOM  10203  CD  GLN B 655      23.500  46.570  19.730  1.00119.38           C  
-ANISOU10203  CD  GLN B 655    17710  11959  15691  -3116    655  -3201       C  
-ATOM  10204  OE1 GLN B 655      23.818  47.099  20.795  1.00123.48           O  
-ANISOU10204  OE1 GLN B 655    18089  12561  16268  -3042    583  -3361       O  
-ATOM  10205  NE2 GLN B 655      23.090  47.269  18.678  1.00125.35           N  
-ANISOU10205  NE2 GLN B 655    18593  12567  16469  -3238    601  -3090       N  
-ATOM  10206  N   SER B 656      19.788  43.132  17.565  1.00 80.67           N  
-ANISOU10206  N   SER B 656    13201   6942  10509  -2988    820  -2677       N  
-ATOM  10207  CA  SER B 656      18.909  42.881  16.433  1.00 78.82           C  
-ANISOU10207  CA  SER B 656    13119   6619  10211  -3049    823  -2536       C  
-ATOM  10208  C   SER B 656      17.609  43.658  16.554  1.00 78.30           C  
-ANISOU10208  C   SER B 656    13092   6490  10170  -2993    660  -2488       C  
-ATOM  10209  O   SER B 656      16.771  43.332  17.385  1.00 76.89           O  
-ANISOU10209  O   SER B 656    12850   6357  10006  -2841    610  -2501       O  
-ATOM  10210  CB  SER B 656      18.601  41.392  16.317  1.00 76.34           C  
-ANISOU10210  CB  SER B 656    12811   6341   9853  -2979    941  -2480       C  
-ATOM  10211  OG  SER B 656      17.643  41.163  15.298  1.00 74.56           O  
-ANISOU10211  OG  SER B 656    12723   6041   9564  -3026    930  -2360       O  
-ATOM  10212  N   ASP B 657      17.438  44.680  15.723  1.00109.63           N  
-ANISOU10212  N   ASP B 657    17158  10348  14149  -3121    573  -2434       N  
-ATOM  10213  CA  ASP B 657      16.202  45.455  15.724  1.00109.19           C  
-ANISOU10213  CA  ASP B 657    17140  10208  14138  -3080    411  -2383       C  
-ATOM  10214  C   ASP B 657      14.980  44.545  15.741  1.00104.30           C  
-ANISOU10214  C   ASP B 657    16561   9607  13462  -2967    416  -2301       C  
-ATOM  10215  O   ASP B 657      13.957  44.882  16.330  1.00102.94           O  
-ANISOU10215  O   ASP B 657    16352   9421  13340  -2855    299  -2308       O  
-ATOM  10216  CB  ASP B 657      16.137  46.392  14.513  1.00116.54           C  
-ANISOU10216  CB  ASP B 657    18203  11002  15074  -3262    334  -2287       C  
-ATOM  10217  CG  ASP B 657      17.034  47.604  14.664  1.00123.15           C  
-ANISOU10217  CG  ASP B 657    18982  11788  16022  -3354    267  -2364       C  
-ATOM  10218  OD1 ASP B 657      18.145  47.456  15.215  1.00126.73           O  
-ANISOU10218  OD1 ASP B 657    19338  12323  16492  -3349    351  -2474       O  
-ATOM  10219  OD2 ASP B 657      16.624  48.706  14.236  1.00128.53           O  
-ANISOU10219  OD2 ASP B 657    19708  12340  16789  -3432    122  -2314       O  
-ATOM  10220  N   LEU B 658      15.089  43.389  15.098  1.00 87.57           N  
-ANISOU10220  N   LEU B 658    14508   7515  11251  -2997    550  -2233       N  
-ATOM  10221  CA  LEU B 658      13.968  42.464  15.032  1.00 82.20           C  
-ANISOU10221  CA  LEU B 658    13863   6842  10528  -2899    561  -2152       C  
-ATOM  10222  C   LEU B 658      13.734  41.809  16.383  1.00 78.30           C  
-ANISOU10222  C   LEU B 658    13226   6446  10079  -2712    572  -2217       C  
-ATOM  10223  O   LEU B 658      12.611  41.774  16.880  1.00 76.88           O  
-ANISOU10223  O   LEU B 658    13026   6266   9918  -2598    487  -2191       O  
-ATOM  10224  CB  LEU B 658      14.210  41.386  13.975  1.00 82.63           C  
-ANISOU10224  CB  LEU B 658    14008   6895  10492  -2986    704  -2087       C  
-ATOM  10225  CG  LEU B 658      13.049  40.404  13.801  1.00 80.94           C  
-ANISOU10225  CG  LEU B 658    13833   6676  10246  -2895    714  -2004       C  
-ATOM  10226  CD1 LEU B 658      11.789  41.134  13.344  1.00 81.65           C  
-ANISOU10226  CD1 LEU B 658    14023   6682  10318  -2907    564  -1914       C  
-ATOM  10227  CD2 LEU B 658      13.416  39.303  12.825  1.00 81.18           C  
-ANISOU10227  CD2 LEU B 658    13925   6710  10211  -2978    865  -1981       C  
-ATOM  10228  N   LEU B 659      14.801  41.284  16.972  1.00 73.13           N  
-ANISOU10228  N   LEU B 659    12470   5875   9441  -2690    675  -2301       N  
-ATOM  10229  CA  LEU B 659      14.702  40.596  18.251  1.00 69.48           C  
-ANISOU10229  CA  LEU B 659    11870   5515   9016  -2530    689  -2361       C  
-ATOM  10230  C   LEU B 659      14.269  41.553  19.346  1.00 70.77           C  
-ANISOU10230  C   LEU B 659    11938   5724   9226  -2439    547  -2461       C  
-ATOM  10231  O   LEU B 659      13.228  41.365  19.972  1.00 70.43           O  
-ANISOU10231  O   LEU B 659    11860   5710   9192  -2319    480  -2452       O  
-ATOM  10232  CB  LEU B 659      16.040  39.966  18.623  1.00 66.08           C  
-ANISOU10232  CB  LEU B 659    11348   5158   8603  -2542    814  -2438       C  
-ATOM  10233  CG  LEU B 659      16.007  38.459  18.851  1.00 61.78           C  
-ANISOU10233  CG  LEU B 659    10754   4643   8077  -2461    922  -2394       C  
-ATOM  10234  CD1 LEU B 659      15.560  37.752  17.586  1.00 61.13           C  
-ANISOU10234  CD1 LEU B 659    10793   4473   7960  -2527    996  -2278       C  
-ATOM  10235  CD2 LEU B 659      17.375  37.964  19.295  1.00 59.28           C  
-ANISOU10235  CD2 LEU B 659    10324   4402   7796  -2467   1030  -2471       C  
-ATOM  10236  N   ARG B 660      15.078  42.581  19.571  1.00 70.50           N  
-ANISOU10236  N   ARG B 660    11857   5698   9230  -2498    504  -2570       N  
-ATOM  10237  CA  ARG B 660      14.790  43.571  20.595  1.00 72.57           C  
-ANISOU10237  CA  ARG B 660    12012   6009   9553  -2421    370  -2705       C  
-ATOM  10238  C   ARG B 660      13.310  43.935  20.611  1.00 71.48           C  
-ANISOU10238  C   ARG B 660    11910   5813   9437  -2352    248  -2656       C  
-ATOM  10239  O   ARG B 660      12.629  43.736  21.614  1.00 71.54           O  
-ANISOU10239  O   ARG B 660    11824   5911   9448  -2218    198  -2723       O  
-ATOM  10240  CB  ARG B 660      15.646  44.825  20.397  1.00 76.78           C  
-ANISOU10240  CB  ARG B 660    12531   6492  10151  -2529    317  -2793       C  
-ATOM  10241  CG  ARG B 660      15.366  45.926  21.405  1.00 82.68           C  
-ANISOU10241  CG  ARG B 660    13152   7277  10986  -2454    172  -2959       C  
-ATOM  10242  CD  ARG B 660      16.449  46.993  21.413  1.00 89.07           C  
-ANISOU10242  CD  ARG B 660    13908   8058  11878  -2549    138  -3074       C  
-ATOM  10243  NE  ARG B 660      16.602  47.642  20.114  1.00 96.57           N  
-ANISOU10243  NE  ARG B 660    14993   8832  12868  -2711    118  -2955       N  
-ATOM  10244  CZ  ARG B 660      17.614  47.418  19.281  1.00100.30           C  
-ANISOU10244  CZ  ARG B 660    15539   9272  13299  -2849    224  -2890       C  
-ATOM  10245  NH1 ARG B 660      18.569  46.560  19.612  1.00102.86           N  
-ANISOU10245  NH1 ARG B 660    15810   9713  13561  -2837    358  -2934       N  
-ATOM  10246  NH2 ARG B 660      17.674  48.056  18.119  1.00103.62           N  
-ANISOU10246  NH2 ARG B 660    16081   9545  13744  -3004    192  -2783       N  
-ATOM  10247  N   THR B 661      12.804  44.436  19.489  1.00 81.97           N  
-ANISOU10247  N   THR B 661    13374   6998  10774  -2448    198  -2541       N  
-ATOM  10248  CA  THR B 661      11.435  44.949  19.446  1.00 80.52           C  
-ANISOU10248  CA  THR B 661    13222   6739  10632  -2395     64  -2500       C  
-ATOM  10249  C   THR B 661      10.347  43.873  19.401  1.00 77.83           C  
-ANISOU10249  C   THR B 661    12925   6417  10230  -2305     94  -2389       C  
-ATOM  10250  O   THR B 661       9.165  44.188  19.239  1.00 76.67           O  
-ANISOU10250  O   THR B 661    12819   6203  10111  -2267     -8  -2337       O  
-ATOM  10251  CB  THR B 661      11.235  45.926  18.278  1.00 82.45           C  
-ANISOU10251  CB  THR B 661    13593   6818  10918  -2534    -22  -2412       C  
-ATOM  10252  OG1 THR B 661      11.458  45.242  17.040  1.00 83.02           O  
-ANISOU10252  OG1 THR B 661    13812   6846  10887  -2650     79  -2265       O  
-ATOM  10253  CG2 THR B 661      12.203  47.094  18.399  1.00 82.16           C  
-ANISOU10253  CG2 THR B 661    13497   6743  10977  -2617    -76  -2523       C  
-ATOM  10254  N   VAL B 662      10.745  42.612  19.542  1.00 73.00           N  
-ANISOU10254  N   VAL B 662    12297   5886   9555  -2271    229  -2355       N  
-ATOM  10255  CA  VAL B 662       9.786  41.517  19.655  1.00 70.91           C  
-ANISOU10255  CA  VAL B 662    12045   5641   9257  -2174    260  -2263       C  
-ATOM  10256  C   VAL B 662       9.693  41.083  21.117  1.00 70.70           C  
-ANISOU10256  C   VAL B 662    11863   5752   9246  -2029    256  -2369       C  
-ATOM  10257  O   VAL B 662       8.604  40.829  21.637  1.00 69.85           O  
-ANISOU10257  O   VAL B 662    11726   5669   9145  -1924    198  -2354       O  
-ATOM  10258  CB  VAL B 662      10.170  40.319  18.759  1.00 68.79           C  
-ANISOU10258  CB  VAL B 662    11857   5347   8933  -2233    405  -2149       C  
-ATOM  10259  CG1 VAL B 662       9.406  39.076  19.172  1.00 66.21           C  
-ANISOU10259  CG1 VAL B 662    11495   5055   8608  -2115    447  -2082       C  
-ATOM  10260  CG2 VAL B 662       9.902  40.644  17.302  1.00 69.09           C  
-ANISOU10260  CG2 VAL B 662    12058   5268   8924  -2366    393  -2043       C  
-ATOM  10261  N   ILE B 663      10.844  41.018  21.777  1.00 71.83           N  
-ANISOU10261  N   ILE B 663    11909   5996   9389  -2029    313  -2484       N  
-ATOM  10262  CA  ILE B 663      10.900  40.719  23.201  1.00 71.50           C  
-ANISOU10262  CA  ILE B 663    11715   6115   9338  -1906    298  -2613       C  
-ATOM  10263  C   ILE B 663      10.247  41.829  24.015  1.00 74.99           C  
-ANISOU10263  C   ILE B 663    12073   6618   9803  -1840    153  -2761       C  
-ATOM  10264  O   ILE B 663       9.458  41.561  24.915  1.00 77.40           O  
-ANISOU10264  O   ILE B 663    12262   7077  10070  -1702    119  -2764       O  
-ATOM  10265  CB  ILE B 663      12.352  40.546  23.684  1.00 70.70           C  
-ANISOU10265  CB  ILE B 663    11475   6187   9202  -1902    393  -2653       C  
-ATOM  10266  CG1 ILE B 663      12.880  39.160  23.318  1.00 69.22           C  
-ANISOU10266  CG1 ILE B 663    11281   6024   8996  -1897    546  -2501       C  
-ATOM  10267  CG2 ILE B 663      12.441  40.755  25.183  1.00 68.20           C  
-ANISOU10267  CG2 ILE B 663    10923   6160   8829  -1754    355  -2742       C  
-ATOM  10268  CD1 ILE B 663      13.011  38.928  21.837  1.00 70.29           C  
-ANISOU10268  CD1 ILE B 663    11625   5914   9168  -2055    603  -2444       C  
-ATOM  10269  N   LEU B 664      10.575  43.077  23.695  1.00 66.65           N  
-ANISOU10269  N   LEU B 664    11026   5496   8802  -1916     81  -2833       N  
-ATOM  10270  CA  LEU B 664      10.059  44.220  24.444  1.00 69.40           C  
-ANISOU10270  CA  LEU B 664    11274   5886   9208  -1859    -59  -3001       C  
-ATOM  10271  C   LEU B 664       8.539  44.319  24.380  1.00 69.18           C  
-ANISOU10271  C   LEU B 664    11281   5795   9210  -1791   -150  -2943       C  
-ATOM  10272  O   LEU B 664       7.893  44.675  25.362  1.00 70.03           O  
-ANISOU10272  O   LEU B 664    11272   6009   9329  -1689   -234  -3091       O  
-ATOM  10273  CB  LEU B 664      10.677  45.527  23.941  1.00 68.32           C  
-ANISOU10273  CB  LEU B 664    11151   5640   9169  -1966   -124  -3065       C  
-ATOM  10274  CG  LEU B 664      12.200  45.654  23.948  1.00 68.49           C  
-ANISOU10274  CG  LEU B 664    11136   5706   9182  -2047    -51  -3135       C  
-ATOM  10275  CD1 LEU B 664      12.604  47.105  23.759  1.00 68.72           C  
-ANISOU10275  CD1 LEU B 664    11136   5639   9336  -2124   -152  -3242       C  
-ATOM  10276  CD2 LEU B 664      12.775  45.109  25.235  1.00 66.18           C  
-ANISOU10276  CD2 LEU B 664    10690   5645   8812  -1951     -7  -3293       C  
-ATOM  10277  N   GLU B 665       7.972  44.003  23.221  1.00 93.24           N  
-ANISOU10277  N   GLU B 665    14483   8684  12260  -1850   -133  -2741       N  
-ATOM  10278  CA  GLU B 665       6.540  44.171  22.995  1.00 91.54           C  
-ANISOU10278  CA  GLU B 665    14315   8386  12081  -1802   -226  -2671       C  
-ATOM  10279  C   GLU B 665       5.719  43.166  23.806  1.00 87.61           C  
-ANISOU10279  C   GLU B 665    13758   8003  11526  -1672   -202  -2664       C  
-ATOM  10280  O   GLU B 665       4.554  43.412  24.124  1.00 86.14           O  
-ANISOU10280  O   GLU B 665    13546   7809  11374  -1597   -293  -2686       O  
-ATOM  10281  CB  GLU B 665       6.229  44.053  21.498  1.00 96.19           C  
-ANISOU10281  CB  GLU B 665    15086   8801  12661  -1909   -214  -2462       C  
-ATOM  10282  CG  GLU B 665       4.932  44.720  21.048  1.00103.48           C  
-ANISOU10282  CG  GLU B 665    16068   9599  13652  -1900   -349  -2406       C  
-ATOM  10283  CD  GLU B 665       4.868  44.915  19.536  1.00110.12           C  
-ANISOU10283  CD  GLU B 665    17083  10281  14476  -2036   -359  -2236       C  
-ATOM  10284  OE1 GLU B 665       3.840  44.542  18.925  1.00114.41           O  
-ANISOU10284  OE1 GLU B 665    17718  10760  14992  -2028   -389  -2106       O  
-ATOM  10285  OE2 GLU B 665       5.844  45.446  18.961  1.00114.71           O  
-ANISOU10285  OE2 GLU B 665    17707  10812  15065  -2157   -342  -2239       O  
-ATOM  10286  N   ILE B 666       6.347  42.047  24.158  1.00 65.65           N  
-ANISOU10286  N   ILE B 666    10949   5324   8672  -1647    -83  -2637       N  
-ATOM  10287  CA  ILE B 666       5.673  40.949  24.857  1.00 63.60           C  
-ANISOU10287  CA  ILE B 666    10640   5160   8364  -1535    -49  -2603       C  
-ATOM  10288  C   ILE B 666       5.123  41.298  26.250  1.00 63.80           C  
-ANISOU10288  C   ILE B 666    10452   5447   8342  -1384   -116  -2718       C  
-ATOM  10289  O   ILE B 666       3.921  41.166  26.490  1.00 65.88           O  
-ANISOU10289  O   ILE B 666    10706   5714   8611  -1308   -172  -2691       O  
-ATOM  10290  CB  ILE B 666       6.576  39.693  24.937  1.00 59.60           C  
-ANISOU10290  CB  ILE B 666    10066   4788   7790  -1509    107  -2461       C  
-ATOM  10291  CG1 ILE B 666       6.630  39.002  23.574  1.00 57.89           C  
-ANISOU10291  CG1 ILE B 666    10051   4328   7617  -1625    178  -2325       C  
-ATOM  10292  CG2 ILE B 666       6.068  38.733  25.999  1.00 59.96           C  
-ANISOU10292  CG2 ILE B 666     9927   5090   7766  -1343    146  -2357       C  
-ATOM  10293  CD1 ILE B 666       7.684  37.916  23.465  1.00 54.45           C  
-ANISOU10293  CD1 ILE B 666     9560   3973   7157  -1629    330  -2222       C  
-ATOM  10294  N   PRO B 667       5.994  41.741  27.173  1.00 59.23           N  
-ANISOU10294  N   PRO B 667     9695   5100   7710  -1342   -108  -2853       N  
-ATOM  10295  CA  PRO B 667       5.498  42.031  28.523  1.00 58.37           C  
-ANISOU10295  CA  PRO B 667     9363   5283   7532  -1201   -164  -2975       C  
-ATOM  10296  C   PRO B 667       4.487  43.171  28.518  1.00 59.08           C  
-ANISOU10296  C   PRO B 667     9485   5241   7720  -1203   -313  -3151       C  
-ATOM  10297  O   PRO B 667       3.526  43.134  29.283  1.00 59.10           O  
-ANISOU10297  O   PRO B 667     9370   5403   7683  -1091   -358  -3192       O  
-ATOM  10298  CB  PRO B 667       6.763  42.422  29.294  1.00 59.70           C  
-ANISOU10298  CB  PRO B 667     9362   5683   7640  -1189   -134  -3107       C  
-ATOM  10299  CG  PRO B 667       7.745  42.815  28.256  1.00 59.49           C  
-ANISOU10299  CG  PRO B 667     9496   5408   7699  -1342   -111  -3117       C  
-ATOM  10300  CD  PRO B 667       7.437  42.002  27.042  1.00 56.66           C  
-ANISOU10300  CD  PRO B 667     9353   4796   7381  -1421    -51  -2908       C  
-ATOM  10301  N   GLU B 668       4.694  44.162  27.660  1.00 96.13           N  
-ANISOU10301  N   GLU B 668    14326   9648  12550  -1333   -390  -3247       N  
-ATOM  10302  CA  GLU B 668       3.731  45.244  27.511  1.00 96.02           C  
-ANISOU10302  CA  GLU B 668    14328   9486  12669  -1336   -532  -3358       C  
-ATOM  10303  C   GLU B 668       2.364  44.684  27.134  1.00 94.57           C  
-ANISOU10303  C   GLU B 668    14230   9208  12494  -1292   -553  -3198       C  
-ATOM  10304  O   GLU B 668       1.345  45.066  27.708  1.00 94.39           O  
-ANISOU10304  O   GLU B 668    14126   9233  12506  -1209   -641  -3311       O  
-ATOM  10305  CB  GLU B 668       4.209  46.242  26.458  1.00 96.09           C  
-ANISOU10305  CB  GLU B 668    14425   9272  12813  -1458   -579  -3304       C  
-ATOM  10306  N   LEU B 669       2.355  43.777  26.163  1.00 65.35           N  
-ANISOU10306  N   LEU B 669    10685   5381   8765  -1347   -469  -2947       N  
-ATOM  10307  CA  LEU B 669       1.121  43.179  25.663  1.00 62.38           C  
-ANISOU10307  CA  LEU B 669    10401   4903   8398  -1315   -482  -2773       C  
-ATOM  10308  C   LEU B 669       0.434  42.300  26.700  1.00 61.30           C  
-ANISOU10308  C   LEU B 669    10176   4933   8184  -1193   -460  -2819       C  
-ATOM  10309  O   LEU B 669      -0.785  42.140  26.673  1.00 62.81           O  
-ANISOU10309  O   LEU B 669    10385   5078   8403  -1138   -511  -2764       O  
-ATOM  10310  CB  LEU B 669       1.402  42.362  24.399  1.00 59.36           C  
-ANISOU10310  CB  LEU B 669    10187   4380   7988  -1405   -389  -2522       C  
-ATOM  10311  CG  LEU B 669       1.571  43.152  23.102  1.00 58.00           C  
-ANISOU10311  CG  LEU B 669    10143   4024   7871  -1528   -433  -2425       C  
-ATOM  10312  CD1 LEU B 669       2.172  42.286  22.003  1.00 55.25           C  
-ANISOU10312  CD1 LEU B 669     9931   3610   7452  -1622   -315  -2238       C  
-ATOM  10313  CD2 LEU B 669       0.235  43.736  22.665  1.00 57.59           C  
-ANISOU10313  CD2 LEU B 669    10139   3847   7895  -1512   -560  -2375       C  
-ATOM  10314  N   LEU B 670       1.220  41.737  27.611  1.00 58.22           N  
-ANISOU10314  N   LEU B 670     9607   4846   7669  -1115   -365  -2809       N  
-ATOM  10315  CA  LEU B 670       0.707  40.787  28.596  1.00 58.38           C  
-ANISOU10315  CA  LEU B 670     9450   5159   7573   -968   -310  -2704       C  
-ATOM  10316  C   LEU B 670       0.238  41.427  29.902  1.00 60.82           C  
-ANISOU10316  C   LEU B 670     9530   5759   7819   -851   -379  -2893       C  
-ATOM  10317  O   LEU B 670      -0.166  40.721  30.825  1.00 62.11           O  
-ANISOU10317  O   LEU B 670     9518   6216   7866   -731   -338  -2812       O  
-ATOM  10318  CB  LEU B 670       1.762  39.724  28.910  1.00 55.88           C  
-ANISOU10318  CB  LEU B 670     9037   5038   7155   -942   -171  -2550       C  
-ATOM  10319  CG  LEU B 670       2.066  38.708  27.808  1.00 51.51           C  
-ANISOU10319  CG  LEU B 670     8655   4266   6650  -1020    -77  -2337       C  
-ATOM  10320  CD1 LEU B 670       3.147  37.736  28.258  1.00 46.29           C  
-ANISOU10320  CD1 LEU B 670     7859   3813   5915   -983     50  -2210       C  
-ATOM  10321  CD2 LEU B 670       0.804  37.961  27.405  1.00 48.83           C  
-ANISOU10321  CD2 LEU B 670     8399   3802   6353   -985    -87  -2179       C  
-ATOM  10322  N   SER B 671       0.283  42.753  29.979  1.00 77.49           N  
-ANISOU10322  N   SER B 671    11631   7799  10014   -888   -486  -3146       N  
-ATOM  10323  CA  SER B 671      -0.061  43.456  31.215  1.00 80.97           C  
-ANISOU10323  CA  SER B 671    11836   8524  10404   -783   -552  -3378       C  
-ATOM  10324  C   SER B 671      -1.477  43.167  31.734  1.00 79.58           C  
-ANISOU10324  C   SER B 671    11578   8462  10196   -675   -589  -3356       C  
-ATOM  10325  O   SER B 671      -1.665  42.981  32.936  1.00 80.98           O  
-ANISOU10325  O   SER B 671    11516   9020  10231   -559   -570  -3414       O  
-ATOM  10326  CB  SER B 671       0.159  44.966  31.070  1.00 84.95           C  
-ANISOU10326  CB  SER B 671    12353   8866  11060   -851   -673  -3664       C  
-ATOM  10327  OG  SER B 671      -0.812  45.556  30.224  1.00 91.68           O  
-ANISOU10327  OG  SER B 671    13373   9370  12092   -910   -783  -3688       O  
-ATOM  10328  N   PRO B 672      -2.477  43.126  30.836  1.00 67.00           N  
-ANISOU10328  N   PRO B 672    10174   6557   8726   -715   -644  -3267       N  
-ATOM  10329  CA  PRO B 672      -3.861  42.898  31.276  1.00 66.41           C  
-ANISOU10329  CA  PRO B 672    10027   6567   8638   -616   -685  -3251       C  
-ATOM  10330  C   PRO B 672      -4.025  41.625  32.100  1.00 65.67           C  
-ANISOU10330  C   PRO B 672     9772   6818   8362   -504   -577  -3051       C  
-ATOM  10331  O   PRO B 672      -4.899  41.567  32.967  1.00 64.94           O  
-ANISOU10331  O   PRO B 672     9511   6966   8198   -398   -599  -3097       O  
-ATOM  10332  CB  PRO B 672      -4.627  42.755  29.959  1.00 67.34           C  
-ANISOU10332  CB  PRO B 672    10412   6270   8906   -701   -730  -3109       C  
-ATOM  10333  CG  PRO B 672      -3.817  43.507  28.975  1.00 70.59           C  
-ANISOU10333  CG  PRO B 672    11000   6381   9441   -847   -769  -3170       C  
-ATOM  10334  CD  PRO B 672      -2.391  43.290  29.376  1.00 66.90           C  
-ANISOU10334  CD  PRO B 672    10441   6115   8862   -858   -672  -3175       C  
-ATOM  10335  N   VAL B 673      -3.195  40.624  31.828  1.00 63.12           N  
-ANISOU10335  N   VAL B 673     9490   6516   7975   -530   -464  -2828       N  
-ATOM  10336  CA  VAL B 673      -3.304  39.326  32.489  1.00 65.44           C  
-ANISOU10336  CA  VAL B 673     9639   7092   8135   -437   -365  -2590       C  
-ATOM  10337  C   VAL B 673      -3.315  39.407  34.015  1.00 70.46           C  
-ANISOU10337  C   VAL B 673     9964   8216   8593   -319   -358  -2685       C  
-ATOM  10338  O   VAL B 673      -4.162  38.800  34.669  1.00 70.52           O  
-ANISOU10338  O   VAL B 673     9834   8445   8517   -225   -344  -2571       O  
-ATOM  10339  CB  VAL B 673      -2.179  38.371  32.035  1.00 63.18           C  
-ANISOU10339  CB  VAL B 673     9411   6761   7833   -487   -250  -2378       C  
-ATOM  10340  CG1 VAL B 673      -1.758  37.452  33.172  1.00 62.80           C  
-ANISOU10340  CG1 VAL B 673     9108   7130   7625   -388   -163  -2226       C  
-ATOM  10341  CG2 VAL B 673      -2.630  37.572  30.824  1.00 62.96           C  
-ANISOU10341  CG2 VAL B 673     9610   6388   7925   -548   -221  -2166       C  
-ATOM  10342  N   GLU B 674      -2.375  40.160  34.575  1.00 76.31           N  
-ANISOU10342  N   GLU B 674    10586   9135   9272   -328   -368  -2893       N  
-ATOM  10343  CA  GLU B 674      -2.209  40.228  36.023  1.00 84.82           C  
-ANISOU10343  CA  GLU B 674    11357  10715  10157   -228   -355  -2991       C  
-ATOM  10344  C   GLU B 674      -3.519  40.470  36.772  1.00 86.64           C  
-ANISOU10344  C   GLU B 674    11438  11151  10331   -133   -414  -3094       C  
-ATOM  10345  O   GLU B 674      -3.727  39.941  37.863  1.00 88.76           O  
-ANISOU10345  O   GLU B 674    11462  11848  10413    -40   -373  -3021       O  
-ATOM  10346  CB  GLU B 674      -1.186  41.303  36.388  1.00 91.60           C  
-ANISOU10346  CB  GLU B 674    12134  11669  11001   -263   -389  -3280       C  
-ATOM  10347  CG  GLU B 674      -0.982  41.481  37.879  1.00102.51           C  
-ANISOU10347  CG  GLU B 674    13189  13588  12172   -168   -383  -3424       C  
-ATOM  10348  CD  GLU B 674       0.112  42.478  38.191  1.00108.01           C  
-ANISOU10348  CD  GLU B 674    13807  14365  12865   -206   -413  -3706       C  
-ATOM  10349  OE1 GLU B 674       0.801  42.916  37.244  1.00109.44           O  
-ANISOU10349  OE1 GLU B 674    14189  14190  13204   -309   -427  -3745       O  
-ATOM  10350  OE2 GLU B 674       0.286  42.824  39.378  1.00110.66           O  
-ANISOU10350  OE2 GLU B 674    13875  15133  13039   -138   -424  -3888       O  
-ATOM  10351  N   HIS B 675      -4.399  41.268  36.180  1.00 99.37           N  
-ANISOU10351  N   HIS B 675    13188  12464  12105   -161   -511  -3257       N  
-ATOM  10352  CA  HIS B 675      -5.659  41.627  36.820  1.00101.09           C  
-ANISOU10352  CA  HIS B 675    13271  12841  12299    -77   -575  -3395       C  
-ATOM  10353  C   HIS B 675      -6.587  40.434  37.011  1.00 97.39           C  
-ANISOU10353  C   HIS B 675    12760  12492  11751     -7   -521  -3101       C  
-ATOM  10354  O   HIS B 675      -7.374  40.400  37.956  1.00 97.61           O  
-ANISOU10354  O   HIS B 675    12577  12851  11661     85   -530  -3155       O  
-ATOM  10355  CB  HIS B 675      -6.378  42.706  36.009  1.00107.07           C  
-ANISOU10355  CB  HIS B 675    14203  13192  13288   -132   -698  -3606       C  
-ATOM  10356  CG  HIS B 675      -7.733  43.061  36.542  1.00115.05           C  
-ANISOU10356  CG  HIS B 675    15092  14313  14309    -50   -767  -3748       C  
-ATOM  10357  ND1 HIS B 675      -8.840  42.262  36.352  1.00117.70           N  
-ANISOU10357  ND1 HIS B 675    15475  14600  14646     -8   -752  -3531       N  
-ATOM  10358  CD2 HIS B 675      -8.159  44.131  37.252  1.00119.88           C  
-ANISOU10358  CD2 HIS B 675    15528  15077  14943     -2   -851  -4098       C  
-ATOM  10359  CE1 HIS B 675      -9.889  42.822  36.927  1.00121.46           C  
-ANISOU10359  CE1 HIS B 675    15813  15201  15135     62   -821  -3732       C  
-ATOM  10360  NE2 HIS B 675      -9.504  43.959  37.479  1.00122.04           N  
-ANISOU10360  NE2 HIS B 675    15746  15398  15224     67   -881  -4085       N  
-ATOM  10361  N   TYR B 676      -6.499  39.459  36.113  1.00 86.89           N  
-ANISOU10361  N   TYR B 676    11621  10900  10495    -53   -463  -2798       N  
-ATOM  10362  CA  TYR B 676      -7.437  38.339  36.120  1.00 83.73           C  
-ANISOU10362  CA  TYR B 676    11209  10531  10074      2   -423  -2514       C  
-ATOM  10363  C   TYR B 676      -6.993  37.166  36.987  1.00 83.22           C  
-ANISOU10363  C   TYR B 676    10930  10858   9831     68   -319  -2249       C  
-ATOM  10364  O   TYR B 676      -7.799  36.586  37.710  1.00 84.23           O  
-ANISOU10364  O   TYR B 676    10887  11257   9861    151   -303  -2117       O  
-ATOM  10365  CB  TYR B 676      -7.732  37.881  34.693  1.00 80.47           C  
-ANISOU10365  CB  TYR B 676    11098   9625   9852    -78   -425  -2337       C  
-ATOM  10366  CG  TYR B 676      -8.501  38.913  33.911  1.00 78.68           C  
-ANISOU10366  CG  TYR B 676    11055   9041   9797   -131   -540  -2541       C  
-ATOM  10367  CD1 TYR B 676      -7.860  40.013  33.358  1.00 78.36           C  
-ANISOU10367  CD1 TYR B 676    11139   8774   9860   -221   -603  -2765       C  
-ATOM  10368  CD2 TYR B 676      -9.873  38.799  33.741  1.00 77.99           C  
-ANISOU10368  CD2 TYR B 676    11006   8846   9781    -93   -592  -2500       C  
-ATOM  10369  CE1 TYR B 676      -8.563  40.969  32.650  1.00 78.13           C  
-ANISOU10369  CE1 TYR B 676    11262   8414  10008   -274   -720  -2930       C  
-ATOM  10370  CE2 TYR B 676     -10.586  39.749  33.034  1.00 78.15           C  
-ANISOU10370  CE2 TYR B 676    11184   8538   9973   -142   -707  -2676       C  
-ATOM  10371  CZ  TYR B 676      -9.927  40.831  32.490  1.00 78.17           C  
-ANISOU10371  CZ  TYR B 676    11303   8315  10083   -234   -773  -2885       C  
-ATOM  10372  OH  TYR B 676     -10.640  41.776  31.787  1.00 79.14           O  
-ANISOU10372  OH  TYR B 676    11569   8104  10396   -288   -898  -3036       O  
-ATOM  10373  N   LEU B 677      -5.716  36.813  36.910  1.00 63.22           N  
-ANISOU10373  N   LEU B 677     8399   8355   7267     27   -253  -2159       N  
-ATOM  10374  CA  LEU B 677      -5.192  35.749  37.747  1.00 64.42           C  
-ANISOU10374  CA  LEU B 677     8332   8876   7268     83   -164  -1903       C  
-ATOM  10375  C   LEU B 677      -5.393  36.098  39.215  1.00 71.32           C  
-ANISOU10375  C   LEU B 677     8887  10296   7914    171   -179  -2029       C  
-ATOM  10376  O   LEU B 677      -5.749  35.247  40.031  1.00 73.08           O  
-ANISOU10376  O   LEU B 677     8899  10863   8005    242   -137  -1803       O  
-ATOM  10377  CB  LEU B 677      -3.707  35.533  37.481  1.00 55.68           C  
-ANISOU10377  CB  LEU B 677     7263   7721   6170     22   -103  -1849       C  
-ATOM  10378  CG  LEU B 677      -3.144  34.404  38.336  1.00 51.19           C  
-ANISOU10378  CG  LEU B 677     6459   7522   5470     78    -20  -1563       C  
-ATOM  10379  CD1 LEU B 677      -3.820  33.111  37.938  1.00 47.82           C  
-ANISOU10379  CD1 LEU B 677     6072   6951   5145    101     23  -1213       C  
-ATOM  10380  CD2 LEU B 677      -1.640  34.284  38.202  1.00 46.49           C  
-ANISOU10380  CD2 LEU B 677     5869   6919   4877     25     36  -1541       C  
-ATOM  10381  N   LYS B 678      -5.158  37.361  39.548  1.00101.92           N  
-ANISOU10381  N   LYS B 678    14286  14039  10400  -2808   1641  -1905       N  
-ATOM  10382  CA  LYS B 678      -5.218  37.794  40.934  1.00108.19           C  
-ANISOU10382  CA  LYS B 678    15076  15030  11002  -2801   1653  -1913       C  
-ATOM  10383  C   LYS B 678      -6.600  37.554  41.534  1.00105.42           C  
-ANISOU10383  C   LYS B 678    14747  14548  10758  -2581   1693  -1822       C  
-ATOM  10384  O   LYS B 678      -6.719  37.189  42.702  1.00106.32           O  
-ANISOU10384  O   LYS B 678    14734  14854  10809  -2478   1716  -1729       O  
-ATOM  10385  CB  LYS B 678      -4.842  39.272  41.050  1.00119.21           C  
-ANISOU10385  CB  LYS B 678    16711  16427  12158  -3030   1632  -2119       C  
-ATOM  10386  CG  LYS B 678      -4.425  39.690  42.445  1.00135.30           C  
-ANISOU10386  CG  LYS B 678    18709  18747  13951  -3085   1636  -2138       C  
-ATOM  10387  CD  LYS B 678      -3.188  38.928  42.896  1.00148.35           C  
-ANISOU10387  CD  LYS B 678    20094  20742  15530  -3123   1617  -2049       C  
-ATOM  10388  CE  LYS B 678      -2.861  39.221  44.352  1.00157.59           C  
-ANISOU10388  CE  LYS B 678    21208  22199  16470  -3155   1620  -2045       C  
-ATOM  10389  NZ  LYS B 678      -3.966  38.806  45.264  1.00163.64           N  
-ANISOU10389  NZ  LYS B 678    21935  22940  17301  -2936   1662  -1927       N  
-ATOM  10390  N   ILE B 679      -7.640  37.742  40.727  1.00 91.17           N  
-ANISOU10390  N   ILE B 679    13103  12418   9121  -2510   1701  -1847       N  
-ATOM  10391  CA  ILE B 679      -9.010  37.691  41.231  1.00 88.49           C  
-ANISOU10391  CA  ILE B 679    12820  11923   8880  -2319   1739  -1786       C  
-ATOM  10392  C   ILE B 679      -9.625  36.298  41.188  1.00 84.69           C  
-ANISOU10392  C   ILE B 679    12131  11408   8641  -2077   1768  -1587       C  
-ATOM  10393  O   ILE B 679     -10.821  36.143  41.422  1.00 84.38           O  
-ANISOU10393  O   ILE B 679    12130  11206   8724  -1906   1800  -1527       O  
-ATOM  10394  CB  ILE B 679      -9.934  38.672  40.479  1.00 88.92           C  
-ANISOU10394  CB  ILE B 679    13163  11637   8986  -2355   1734  -1913       C  
-ATOM  10395  CG1 ILE B 679     -10.348  38.103  39.121  1.00 88.54           C  
-ANISOU10395  CG1 ILE B 679    13121  11332   9188  -2291   1720  -1870       C  
-ATOM  10396  CG2 ILE B 679      -9.250  40.017  40.308  1.00 90.05           C  
-ANISOU10396  CG2 ILE B 679    13518  11790   8905  -2608   1706  -2115       C  
-ATOM  10397  CD1 ILE B 679     -11.182  39.066  38.292  1.00 90.06           C  
-ANISOU10397  CD1 ILE B 679    13596  11191   9433  -2337   1706  -1995       C  
-ATOM  10398  N   LEU B 680      -8.813  35.289  40.894  1.00 77.06           N  
-ANISOU10398  N   LEU B 680    10942  10592   7745  -2062   1760  -1485       N  
-ATOM  10399  CA  LEU B 680      -9.294  33.911  40.902  1.00 73.96           C  
-ANISOU10399  CA  LEU B 680    10336  10193   7572  -1837   1793  -1292       C  
-ATOM  10400  C   LEU B 680      -8.729  33.112  42.062  1.00 77.22           C  
-ANISOU10400  C   LEU B 680    10496  10936   7908  -1756   1814  -1159       C  
-ATOM  10401  O   LEU B 680      -7.566  33.267  42.429  1.00 77.79           O  
-ANISOU10401  O   LEU B 680    10488  11262   7805  -1895   1791  -1192       O  
-ATOM  10402  CB  LEU B 680      -8.953  33.193  39.598  1.00 68.55           C  
-ANISOU10402  CB  LEU B 680     9581   9394   7072  -1846   1781  -1251       C  
-ATOM  10403  CG  LEU B 680      -9.763  33.576  38.365  1.00 63.93           C  
-ANISOU10403  CG  LEU B 680     9200   8449   6643  -1855   1767  -1324       C  
-ATOM  10404  CD1 LEU B 680      -9.776  32.417  37.380  1.00 60.70           C  
-ANISOU10404  CD1 LEU B 680     8653   7939   6472  -1763   1776  -1207       C  
-ATOM  10405  CD2 LEU B 680     -11.175  33.960  38.763  1.00 62.65           C  
-ANISOU10405  CD2 LEU B 680     9174   8091   6539  -1718   1789  -1323       C  
-ATOM  10406  N   ASN B 681      -9.563  32.248  42.629  1.00 78.59           N  
-ANISOU10406  N   ASN B 681    10543  11101   8216  -1529   1858  -1006       N  
-ATOM  10407  CA  ASN B 681      -9.111  31.317  43.649  1.00 83.65           C  
-ANISOU10407  CA  ASN B 681    10929  12035   8819  -1424   1882   -856       C  
-ATOM  10408  C   ASN B 681      -8.480  30.099  42.991  1.00 85.30           C  
-ANISOU10408  C   ASN B 681    10915  12311   9186  -1371   1886   -730       C  
-ATOM  10409  O   ASN B 681      -9.180  29.245  42.449  1.00 85.65           O  
-ANISOU10409  O   ASN B 681    10895  12188   9461  -1210   1916   -623       O  
-ATOM  10410  CB  ASN B 681     -10.273  30.895  44.547  1.00 83.40           C  
-ANISOU10410  CB  ASN B 681    10858  11964   8865  -1202   1933   -745       C  
-ATOM  10411  CG  ASN B 681      -9.844  29.934  45.639  1.00 85.84           C  
-ANISOU10411  CG  ASN B 681    10909  12573   9132  -1087   1959   -587       C  
-ATOM  10412  OD1 ASN B 681      -8.681  29.914  46.044  1.00 85.57           O  
-ANISOU10412  OD1 ASN B 681    10762  12811   8938  -1200   1933   -589       O  
-ATOM  10413  ND2 ASN B 681     -10.782  29.124  46.116  1.00 84.13           N  
-ANISOU10413  ND2 ASN B 681    10596  12307   9061   -860   2010   -446       N  
-ATOM  10414  N   GLU B 682      -7.154  30.029  43.033  1.00 95.32           N  
-ANISOU10414  N   GLU B 682    12068  13821  10329  -1510   1858   -744       N  
-ATOM  10415  CA  GLU B 682      -6.414  28.960  42.371  1.00 95.89           C  
-ANISOU10415  CA  GLU B 682    11935  13965  10533  -1487   1864   -638       C  
-ATOM  10416  C   GLU B 682      -6.965  27.575  42.694  1.00 93.82           C  
-ANISOU10416  C   GLU B 682    11457  13727  10463  -1236   1917   -430       C  
-ATOM  10417  O   GLU B 682      -6.973  26.687  41.840  1.00 91.45           O  
-ANISOU10417  O   GLU B 682    11057  13326  10363  -1164   1938   -344       O  
-ATOM  10418  CB  GLU B 682      -4.934  29.032  42.744  1.00101.46           C  
-ANISOU10418  CB  GLU B 682    12512  14988  11052  -1644   1832   -659       C  
-ATOM  10419  CG  GLU B 682      -4.081  27.934  42.136  1.00105.80           C  
-ANISOU10419  CG  GLU B 682    12837  15635  11728  -1625   1842   -547       C  
-ATOM  10420  CD  GLU B 682      -2.595  28.202  42.295  1.00111.87           C  
-ANISOU10420  CD  GLU B 682    13515  16677  12312  -1816   1803   -600       C  
-ATOM  10421  OE1 GLU B 682      -2.239  29.154  43.023  1.00115.88           O  
-ANISOU10421  OE1 GLU B 682    14114  17328  12587  -1949   1769   -708       O  
-ATOM  10422  OE2 GLU B 682      -1.784  27.468  41.689  1.00114.96           O  
-ANISOU10422  OE2 GLU B 682    13747  17139  12792  -1837   1809   -536       O  
-ATOM  10423  N   GLN B 683      -7.430  27.402  43.928  1.00107.80           N  
-ANISOU10423  N   GLN B 683    13161  15628  12170  -1108   1943   -351       N  
-ATOM  10424  CA  GLN B 683      -7.921  26.109  44.393  1.00104.64           C  
-ANISOU10424  CA  GLN B 683    12551  15278  11928   -870   1998   -152       C  
-ATOM  10425  C   GLN B 683      -9.181  25.667  43.653  1.00100.99           C  
-ANISOU10425  C   GLN B 683    12154  14498  11720   -712   2035   -104       C  
-ATOM  10426  O   GLN B 683      -9.277  24.525  43.207  1.00 99.53           O  
-ANISOU10426  O   GLN B 683    11809  14276  11730   -581   2071     32       O  
-ATOM  10427  CB  GLN B 683      -8.166  26.141  45.898  1.00103.59           C  
-ANISOU10427  CB  GLN B 683    12360  15346  11655   -781   2016    -95       C  
-ATOM  10428  N   ALA B 684     -10.143  26.574  43.520  1.00 77.04           N  
-ANISOU10428  N   ALA B 684     9354  11234   8683   -726   2027   -215       N  
-ATOM  10429  CA  ALA B 684     -11.413  26.240  42.884  1.00 73.15           C  
-ANISOU10429  CA  ALA B 684     8934  10438   8422   -577   2057   -174       C  
-ATOM  10430  C   ALA B 684     -11.280  26.102  41.374  1.00 70.50           C  
-ANISOU10430  C   ALA B 684     8655   9890   8241   -648   2037   -213       C  
-ATOM  10431  O   ALA B 684     -11.878  25.207  40.776  1.00 68.45           O  
-ANISOU10431  O   ALA B 684     8324   9476   8207   -508   2070   -109       O  
-ATOM  10432  CB  ALA B 684     -12.473  27.274  43.228  1.00 72.56           C  
-ANISOU10432  CB  ALA B 684     9089  10185   8295   -571   2055   -278       C  
-ATOM  10433  N   ALA B 685     -10.504  26.991  40.761  1.00 60.58           N  
-ANISOU10433  N   ALA B 685     7531   8623   6862   -870   1986   -365       N  
-ATOM  10434  CA  ALA B 685     -10.316  26.969  39.312  1.00 58.75           C  
-ANISOU10434  CA  ALA B 685     7375   8190   6757   -961   1964   -419       C  
-ATOM  10435  C   ALA B 685      -9.788  25.614  38.856  1.00 58.16           C  
-ANISOU10435  C   ALA B 685     7065   8192   6841   -880   1997   -270       C  
-ATOM  10436  O   ALA B 685     -10.290  25.029  37.898  1.00 55.88           O  
-ANISOU10436  O   ALA B 685     6779   7690   6762   -810   2014   -221       O  
-ATOM  10437  CB  ALA B 685      -9.373  28.080  38.882  1.00 58.71           C  
-ANISOU10437  CB  ALA B 685     7521   8220   6568  -1218   1909   -598       C  
-ATOM  10438  N   LYS B 686      -8.779  25.120  39.564  1.00 86.74           N  
-ANISOU10438  N   LYS B 686    10480  12119  10357   -891   2006   -195       N  
-ATOM  10439  CA  LYS B 686      -8.177  23.829  39.261  1.00 88.26           C  
-ANISOU10439  CA  LYS B 686    10432  12419  10683   -814   2043    -47       C  
-ATOM  10440  C   LYS B 686      -9.146  22.679  39.505  1.00 86.03           C  
-ANISOU10440  C   LYS B 686    10017  12066  10606   -561   2105    128       C  
-ATOM  10441  O   LYS B 686      -8.894  21.548  39.089  1.00 83.73           O  
-ANISOU10441  O   LYS B 686     9548  11795  10470   -474   2146    257       O  
-ATOM  10442  CB  LYS B 686      -6.917  23.625  40.102  1.00 94.57           C  
-ANISOU10442  CB  LYS B 686    11043  13578  11310   -876   2036     -5       C  
-ATOM  10443  CG  LYS B 686      -5.811  24.631  39.812  1.00103.03           C  
-ANISOU10443  CG  LYS B 686    12214  14744  12187  -1133   1977   -167       C  
-ATOM  10444  CD  LYS B 686      -4.543  24.306  40.590  1.00112.38           C  
-ANISOU10444  CD  LYS B 686    13187  16288  13223  -1186   1970   -109       C  
-ATOM  10445  CE  LYS B 686      -3.383  25.191  40.156  1.00118.09           C  
-ANISOU10445  CE  LYS B 686    13992  17097  13779  -1444   1917   -264       C  
-ATOM  10446  NZ  LYS B 686      -2.110  24.820  40.836  1.00123.29           N  
-ANISOU10446  NZ  LYS B 686    14431  18106  14307  -1498   1907   -200       N  
-ATOM  10447  N   VAL B 687     -10.253  22.981  40.177  1.00 85.36           N  
-ANISOU10447  N   VAL B 687    10019  11894  10521   -445   2117    131       N  
-ATOM  10448  CA  VAL B 687     -11.225  21.968  40.578  1.00 83.98           C  
-ANISOU10448  CA  VAL B 687     9723  11665  10520   -201   2179    292       C  
-ATOM  10449  C   VAL B 687     -12.469  21.966  39.696  1.00 81.74           C  
-ANISOU10449  C   VAL B 687     9583  11034  10440   -122   2188    277       C  
-ATOM  10450  O   VAL B 687     -13.048  20.915  39.430  1.00 80.50           O  
-ANISOU10450  O   VAL B 687     9313  10785  10487     45   2238    409       O  
-ATOM  10451  CB  VAL B 687     -11.659  22.157  42.047  1.00 85.86           C  
-ANISOU10451  CB  VAL B 687     9932  12059  10632   -100   2196    329       C  
-ATOM  10452  CG1 VAL B 687     -12.946  21.398  42.325  1.00 85.90           C  
-ANISOU10452  CG1 VAL B 687     9889  11925  10824    138   2255    455       C  
-ATOM  10453  CG2 VAL B 687     -10.548  21.716  42.992  1.00 85.69           C  
-ANISOU10453  CG2 VAL B 687     9701  12396  10463   -112   2201    410       C  
-ATOM  10454  N   GLY B 688     -12.883  23.146  39.252  1.00 54.80           N  
-ANISOU10454  N   GLY B 688     6421   7431   6971   -242   2141    116       N  
-ATOM  10455  CA  GLY B 688     -14.049  23.257  38.399  1.00 53.60           C  
-ANISOU10455  CA  GLY B 688     6420   6947   6999   -181   2140     91       C  
-ATOM  10456  C   GLY B 688     -15.232  23.894  39.096  1.00 53.75           C  
-ANISOU10456  C   GLY B 688     6573   6853   6996    -90   2145     57       C  
-ATOM  10457  O   GLY B 688     -16.300  24.045  38.505  1.00 52.85           O  
-ANISOU10457  O   GLY B 688     6587   6466   7029    -29   2143     38       O  
-ATOM  10458  N   ASP B 689     -15.044  24.269  40.357  1.00 76.40           N  
-ANISOU10458  N   ASP B 689     9412   9932   9683    -84   2152     50       N  
-ATOM  10459  CA  ASP B 689     -16.107  24.894  41.135  1.00 76.93           C  
-ANISOU10459  CA  ASP B 689     9603   9914   9713     -2   2165     18       C  
-ATOM  10460  C   ASP B 689     -16.224  26.373  40.787  1.00 75.58           C  
-ANISOU10460  C   ASP B 689     9704   9596   9416   -176   2111   -177       C  
-ATOM  10461  O   ASP B 689     -15.312  27.157  41.051  1.00 75.23           O  
-ANISOU10461  O   ASP B 689     9719   9707   9159   -351   2076   -284       O  
-ATOM  10462  CB  ASP B 689     -15.845  24.725  42.633  1.00 79.51           C  
-ANISOU10462  CB  ASP B 689     9800  10524   9887     67   2197     85       C  
-ATOM  10463  CG  ASP B 689     -16.998  25.219  43.491  1.00 80.64           C  
-ANISOU10463  CG  ASP B 689    10050  10578  10011    175   2225     72       C  
-ATOM  10464  OD1 ASP B 689     -17.944  25.822  42.941  1.00 82.53           O  
-ANISOU10464  OD1 ASP B 689    10476  10544  10338    181   2214     -5       O  
-ATOM  10465  OD2 ASP B 689     -16.952  25.009  44.722  1.00 82.64           O  
-ANISOU10465  OD2 ASP B 689    10201  11036  10161    254   2258    138       O  
-ATOM  10466  N   LYS B 690     -17.354  26.752  40.202  1.00 74.26           N  
-ANISOU10466  N   LYS B 690     9702   9133   9381   -127   2105   -220       N  
-ATOM  10467  CA  LYS B 690     -17.571  28.136  39.808  1.00 72.52           C  
-ANISOU10467  CA  LYS B 690     9748   8744   9061   -278   2058   -398       C  
-ATOM  10468  C   LYS B 690     -18.065  28.992  40.974  1.00 75.63           C  
-ANISOU10468  C   LYS B 690    10246   9188   9302   -261   2075   -456       C  
-ATOM  10469  O   LYS B 690     -18.002  30.223  40.916  1.00 76.11           O  
-ANISOU10469  O   LYS B 690    10515   9184   9219   -408   2042   -610       O  
-ATOM  10470  CB  LYS B 690     -18.540  28.208  38.626  1.00 68.06           C  
-ANISOU10470  CB  LYS B 690     9320   7836   8703   -241   2040   -421       C  
-ATOM  10471  CG  LYS B 690     -18.157  27.281  37.480  1.00 63.33           C  
-ANISOU10471  CG  LYS B 690     8617   7172   8272   -244   2032   -353       C  
-ATOM  10472  CD  LYS B 690     -18.531  27.852  36.118  1.00 58.44           C  
-ANISOU10472  CD  LYS B 690     8201   6254   7748   -341   1981   -455       C  
-ATOM  10473  CE  LYS B 690     -18.031  26.960  34.983  1.00 55.59           C  
-ANISOU10473  CE  LYS B 690     7743   5844   7534   -366   1975   -396       C  
-ATOM  10474  NZ  LYS B 690     -18.448  27.462  33.643  1.00 51.34           N  
-ANISOU10474  NZ  LYS B 690     7403   5007   7097   -454   1926   -487       N  
-ATOM  10475  N   THR B 691     -18.540  28.339  42.035  1.00 66.36           N  
-ANISOU10475  N   THR B 691     8931   8129   8155    -83   2131   -332       N  
-ATOM  10476  CA  THR B 691     -19.032  29.048  43.215  1.00 71.18           C  
-ANISOU10476  CA  THR B 691     9626   8795   8626    -53   2157   -373       C  
-ATOM  10477  C   THR B 691     -17.886  29.607  44.049  1.00 74.25           C  
-ANISOU10477  C   THR B 691    10001   9474   8738   -208   2141   -441       C  
-ATOM  10478  O   THR B 691     -17.909  30.769  44.454  1.00 76.52           O  
-ANISOU10478  O   THR B 691    10469   9754   8853   -322   2128   -573       O  
-ATOM  10479  CB  THR B 691     -19.911  28.150  44.117  1.00 70.44           C  
-ANISOU10479  CB  THR B 691     9384   8733   8647    187   2227   -217       C  
-ATOM  10480  OG1 THR B 691     -19.084  27.249  44.865  1.00 71.72           O  
-ANISOU10480  OG1 THR B 691     9313   9195   8744    233   2251    -99       O  
-ATOM  10481  CG2 THR B 691     -20.913  27.360  43.286  1.00 71.26           C  
-ANISOU10481  CG2 THR B 691     9453   8587   9036    347   2245   -124       C  
-ATOM  10482  N   GLU B 692     -16.882  28.774  44.300  1.00 79.03           N  
-ANISOU10482  N   GLU B 692    10392  10334   9301   -213   2142   -350       N  
-ATOM  10483  CA  GLU B 692     -15.731  29.186  45.095  1.00 81.88           C  
-ANISOU10483  CA  GLU B 692    10712  10993   9406   -355   2122   -400       C  
-ATOM  10484  C   GLU B 692     -14.636  29.747  44.204  1.00 80.31           C  
-ANISOU10484  C   GLU B 692    10585  10818   9112   -583   2061   -522       C  
-ATOM  10485  O   GLU B 692     -13.454  29.698  44.539  1.00 80.95           O  
-ANISOU10485  O   GLU B 692    10562  11159   9037   -696   2040   -528       O  
-ATOM  10486  CB  GLU B 692     -15.198  28.008  45.913  1.00 87.48           C  
-ANISOU10486  CB  GLU B 692    11146  11982  10112   -239   2155   -232       C  
-ATOM  10487  CG  GLU B 692     -16.242  27.396  46.826  1.00 93.35           C  
-ANISOU10487  CG  GLU B 692    11809  12712  10947    -12   2220   -106       C  
-ATOM  10488  CD  GLU B 692     -16.929  28.440  47.680  1.00 98.36           C  
-ANISOU10488  CD  GLU B 692    12626  13299  11447    -25   2236   -200       C  
-ATOM  10489  OE1 GLU B 692     -16.219  29.282  48.270  1.00102.06           O  
-ANISOU10489  OE1 GLU B 692    13168  13937  11675   -183   2211   -301       O  
-ATOM  10490  OE2 GLU B 692     -18.177  28.428  47.745  1.00100.90           O  
-ANISOU10490  OE2 GLU B 692    13020  13411  11906    118   2276   -174       O  
-ATOM  10491  N   LEU B 693     -15.043  30.295  43.068  1.00 79.68           N  
-ANISOU10491  N   LEU B 693    10685  10464   9125   -651   2033   -620       N  
-ATOM  10492  CA  LEU B 693     -14.095  30.731  42.060  1.00 79.23           C  
-ANISOU10492  CA  LEU B 693    10699  10390   9014   -855   1979   -729       C  
-ATOM  10493  C   LEU B 693     -13.598  32.155  42.305  1.00 82.31           C  
-ANISOU10493  C   LEU B 693    11291  10827   9156  -1068   1944   -914       C  
-ATOM  10494  O   LEU B 693     -12.396  32.416  42.254  1.00 83.03           O  
-ANISOU10494  O   LEU B 693    11353  11103   9092  -1240   1911   -977       O  
-ATOM  10495  CB  LEU B 693     -14.719  30.601  40.671  1.00 69.49           C  
-ANISOU10495  CB  LEU B 693     9562   8841   7999   -833   1964   -743       C  
-ATOM  10496  CG  LEU B 693     -13.770  30.739  39.486  1.00 63.29           C  
-ANISOU10496  CG  LEU B 693     8814   8024   7211  -1012   1917   -822       C  
-ATOM  10497  CD1 LEU B 693     -12.449  30.059  39.791  1.00 59.43           C  
-ANISOU10497  CD1 LEU B 693     8104   7841   6636  -1067   1918   -756       C  
-ATOM  10498  CD2 LEU B 693     -14.407  30.153  38.239  1.00 57.93           C  
-ANISOU10498  CD2 LEU B 693     8152   7073   6787   -936   1915   -774       C  
-ATOM  10499  N   PHE B 694     -14.521  33.069  42.579  1.00 96.14           N  
-ANISOU10499  N   PHE B 694    13245  12410  10872  -1058   1954  -1000       N  
-ATOM  10500  CA  PHE B 694     -14.159  34.467  42.776  1.00100.33           C  
-ANISOU10500  CA  PHE B 694    13990  12955  11176  -1257   1928  -1181       C  
-ATOM  10501  C   PHE B 694     -14.005  34.793  44.252  1.00106.41           C  
-ANISOU10501  C   PHE B 694    14731  13960  11739  -1256   1956  -1180       C  
-ATOM  10502  O   PHE B 694     -14.992  34.930  44.973  1.00106.56           O  
-ANISOU10502  O   PHE B 694    14800  13908  11780  -1129   1998  -1151       O  
-ATOM  10503  CB  PHE B 694     -15.196  35.380  42.129  1.00 99.99           C  
-ANISOU10503  CB  PHE B 694    14207  12579  11205  -1268   1922  -1289       C  
-ATOM  10504  CG  PHE B 694     -15.451  35.062  40.688  1.00 97.58           C  
-ANISOU10504  CG  PHE B 694    13941  12027  11108  -1261   1893  -1285       C  
-ATOM  10505  CD1 PHE B 694     -14.488  35.327  39.730  1.00 98.03           C  
-ANISOU10505  CD1 PHE B 694    14044  12084  11118  -1446   1845  -1375       C  
-ATOM  10506  CD2 PHE B 694     -16.647  34.488  40.290  1.00 97.06           C  
-ANISOU10506  CD2 PHE B 694    13865  11730  11283  -1073   1914  -1192       C  
-ATOM  10507  CE1 PHE B 694     -14.712  35.031  38.403  1.00 98.23           C  
-ANISOU10507  CE1 PHE B 694    14111  11882  11330  -1446   1819  -1371       C  
-ATOM  10508  CE2 PHE B 694     -16.878  34.191  38.962  1.00 97.43           C  
-ANISOU10508  CE2 PHE B 694    13951  11552  11517  -1072   1884  -1187       C  
-ATOM  10509  CZ  PHE B 694     -15.908  34.463  38.017  1.00 98.05           C  
-ANISOU10509  CZ  PHE B 694    14080  11631  11542  -1260   1837  -1277       C  
-ATOM  10510  N   LYS B 695     -12.760  34.926  44.693  1.00 91.22           N  
-ANISOU10510  N   LYS B 695    12728  12317   9615  -1403   1932  -1214       N  
-ATOM  10511  CA  LYS B 695     -12.468  35.067  46.114  1.00100.65           C  
-ANISOU10511  CA  LYS B 695    13857  13776  10610  -1404   1954  -1194       C  
-ATOM  10512  C   LYS B 695     -12.754  36.462  46.673  1.00105.43           C  
-ANISOU10512  C   LYS B 695    14707  14334  11017  -1523   1961  -1352       C  
-ATOM  10513  O   LYS B 695     -12.519  36.722  47.853  1.00108.76           O  
-ANISOU10513  O   LYS B 695    15106  14964  11253  -1546   1979  -1355       O  
-ATOM  10514  CB  LYS B 695     -11.025  34.644  46.410  1.00103.74           C  
-ANISOU10514  CB  LYS B 695    14058  14496  10861  -1512   1923  -1161       C  
-ATOM  10515  CG  LYS B 695      -9.996  35.177  45.431  1.00107.82           C  
-ANISOU10515  CG  LYS B 695    14647  15013  11306  -1735   1868  -1288       C  
-ATOM  10516  CD  LYS B 695      -8.623  34.604  45.744  1.00110.10           C  
-ANISOU10516  CD  LYS B 695    14716  15631  11487  -1814   1842  -1231       C  
-ATOM  10517  CE  LYS B 695      -7.558  35.164  44.817  1.00110.33           C  
-ANISOU10517  CE  LYS B 695    14816  15670  11434  -2045   1792  -1362       C  
-ATOM  10518  NZ  LYS B 695      -6.205  34.621  45.123  1.00110.10           N  
-ANISOU10518  NZ  LYS B 695    14567  15964  11302  -2124   1767  -1307       N  
-ATOM  10519  N   ASP B 696     -13.265  37.354  45.831  1.00108.75           N  
-ANISOU10519  N   ASP B 696    15363  14480  11478  -1598   1948  -1481       N  
-ATOM  10520  CA  ASP B 696     -13.657  38.684  46.288  1.00113.86           C  
-ANISOU10520  CA  ASP B 696    16257  15045  11961  -1698   1964  -1629       C  
-ATOM  10521  C   ASP B 696     -15.033  39.054  45.751  1.00115.12           C  
-ANISOU10521  C   ASP B 696    16595  14852  12294  -1590   1988  -1655       C  
-ATOM  10522  O   ASP B 696     -15.154  39.734  44.734  1.00114.87           O  
-ANISOU10522  O   ASP B 696    16743  14601  12301  -1690   1959  -1767       O  
-ATOM  10523  CB  ASP B 696     -12.622  39.729  45.874  1.00115.56           C  
-ANISOU10523  CB  ASP B 696    16617  15318  11971  -1966   1919  -1806       C  
-ATOM  10524  CG  ASP B 696     -12.880  41.082  46.505  1.00116.74           C  
-ANISOU10524  CG  ASP B 696    17006  15431  11917  -2082   1941  -1957       C  
-ATOM  10525  OD1 ASP B 696     -12.551  41.250  47.699  1.00116.59           O  
-ANISOU10525  OD1 ASP B 696    16944  15645  11710  -2111   1963  -1953       O  
-ATOM  10526  OD2 ASP B 696     -13.413  41.974  45.810  1.00117.44           O  
-ANISOU10526  OD2 ASP B 696    17328  15259  12035  -2144   1939  -2077       O  
-ATOM  10527  N   LEU B 697     -16.068  38.604  46.451  1.00127.48           N  
-ANISOU10527  N   LEU B 697    18108  16365  13964  -1387   2042  -1548       N  
-ATOM  10528  CA  LEU B 697     -17.442  38.754  45.987  1.00127.75           C  
-ANISOU10528  CA  LEU B 697    18270  16075  14196  -1251   2067  -1541       C  
-ATOM  10529  C   LEU B 697     -17.995  40.155  46.236  1.00130.79           C  
-ANISOU10529  C   LEU B 697    18931  16306  14458  -1339   2089  -1694       C  
-ATOM  10530  O   LEU B 697     -19.207  40.339  46.352  1.00129.86           O  
-ANISOU10530  O   LEU B 697    18906  15975  14459  -1206   2130  -1677       O  
-ATOM  10531  CB  LEU B 697     -18.336  37.707  46.657  1.00125.74           C  
-ANISOU10531  CB  LEU B 697    17846  15825  14105   -996   2121  -1367       C  
-ATOM  10532  CG  LEU B 697     -17.955  36.240  46.436  1.00122.18           C  
-ANISOU10532  CG  LEU B 697    17120  15501  13801   -878   2112  -1199       C  
-ATOM  10533  CD1 LEU B 697     -18.669  35.347  47.434  1.00120.20           C  
-ANISOU10533  CD1 LEU B 697    16708  15325  13639   -653   2174  -1041       C  
-ATOM  10534  CD2 LEU B 697     -18.255  35.807  45.009  1.00121.69           C  
-ANISOU10534  CD2 LEU B 697    17062  15202  13973   -842   2078  -1177       C  
-ATOM  10535  N   SER B 698     -17.105  41.140  46.310  1.00143.00           N  
-ANISOU10535  N   SER B 698    20606  17959  15770  -1564   2065  -1843       N  
-ATOM  10536  CA  SER B 698     -17.509  42.521  46.554  1.00146.73           C  
-ANISOU10536  CA  SER B 698    21347  18302  16103  -1669   2090  -1999       C  
-ATOM  10537  C   SER B 698     -18.584  42.966  45.570  1.00147.00           C  
-ANISOU10537  C   SER B 698    21564  17967  16324  -1612   2088  -2044       C  
-ATOM  10538  O   SER B 698     -19.668  43.392  45.971  1.00146.91           O  
-ANISOU10538  O   SER B 698    21670  17789  16361  -1511   2138  -2050       O  
-ATOM  10539  CB  SER B 698     -16.303  43.460  46.481  1.00148.23           C  
-ANISOU10539  CB  SER B 698    21648  18635  16037  -1936   2054  -2158       C  
-ATOM  10540  OG  SER B 698     -15.388  43.195  47.530  1.00151.36           O  
-ANISOU10540  OG  SER B 698    21897  19373  16239  -1994   2058  -2126       O  
-ATOM  10541  N   ASP B 699     -18.281  42.863  44.281  1.00146.66           N  
-ANISOU10541  N   ASP B 699    21543  17795  16385  -1678   2031  -2073       N  
-ATOM  10542  CA  ASP B 699     -19.249  43.207  43.246  1.00146.30           C  
-ANISOU10542  CA  ASP B 699    21659  17402  16526  -1626   2018  -2106       C  
-ATOM  10543  C   ASP B 699     -20.079  41.999  42.841  1.00146.25           C  
-ANISOU10543  C   ASP B 699    21489  17274  16806  -1399   2020  -1939       C  
-ATOM  10544  O   ASP B 699     -20.370  41.791  41.663  1.00144.96           O  
-ANISOU10544  O   ASP B 699    21359  16902  16817  -1381   1980  -1931       O  
-ATOM  10545  CB  ASP B 699     -18.560  43.826  42.030  1.00147.00           C  
-ANISOU10545  CB  ASP B 699    21888  17390  16574  -1824   1956  -2237       C  
-ATOM  10546  CG  ASP B 699     -18.319  45.314  42.197  1.00148.16           C  
-ANISOU10546  CG  ASP B 699    22294  17501  16500  -2017   1964  -2425       C  
-ATOM  10547  OD1 ASP B 699     -19.091  45.957  42.940  1.00148.89           O  
-ANISOU10547  OD1 ASP B 699    22509  17520  16542  -1966   2018  -2457       O  
-ATOM  10548  OD2 ASP B 699     -17.363  45.840  41.586  1.00149.42           O  
-ANISOU10548  OD2 ASP B 699    22536  17701  16536  -2220   1922  -2541       O  
-ATOM  10549  N   PHE B 700     -20.456  41.205  43.835  1.00128.88           N  
-ANISOU10549  N   PHE B 700    19116  15206  14648  -1229   2069  -1805       N  
-ATOM  10550  CA  PHE B 700     -21.331  40.068  43.614  1.00128.43           C  
-ANISOU10550  CA  PHE B 700    18903  15040  14855  -1001   2084  -1643       C  
-ATOM  10551  C   PHE B 700     -22.301  39.930  44.781  1.00128.16           C  
-ANISOU10551  C   PHE B 700    18836  15011  14847   -825   2158  -1567       C  
-ATOM  10552  O   PHE B 700     -22.304  38.917  45.474  1.00129.06           O  
-ANISOU10552  O   PHE B 700    18738  15291  15007   -689   2189  -1429       O  
-ATOM  10553  CB  PHE B 700     -20.515  38.801  43.441  1.00129.71           C  
-ANISOU10553  CB  PHE B 700    18805  15402  15075   -967   2060  -1520       C  
-ATOM  10554  N   PRO B 701     -23.130  40.961  45.005  1.00156.20           N  
-ANISOU10554  N   PRO B 701    22602  18378  18368   -829   2191  -1659       N  
-ATOM  10555  CA  PRO B 701     -24.106  40.925  46.098  1.00153.97           C  
-ANISOU10555  CA  PRO B 701    22311  18079  18111   -667   2269  -1598       C  
-ATOM  10556  C   PRO B 701     -25.138  39.834  45.847  1.00148.22           C  
-ANISOU10556  C   PRO B 701    21439  17208  17668   -427   2287  -1439       C  
-ATOM  10557  O   PRO B 701     -25.465  39.061  46.745  1.00148.10           O  
-ANISOU10557  O   PRO B 701    21265  17312  17695   -273   2339  -1318       O  
-ATOM  10558  CB  PRO B 701     -24.760  42.307  46.028  1.00156.31           C  
-ANISOU10558  CB  PRO B 701    22890  18153  18349   -739   2290  -1741       C  
-ATOM  10559  CG  PRO B 701     -24.583  42.741  44.614  1.00156.08           C  
-ANISOU10559  CG  PRO B 701    22990  17929  18386   -852   2219  -1828       C  
-ATOM  10560  CD  PRO B 701     -23.265  42.171  44.177  1.00157.30           C  
-ANISOU10560  CD  PRO B 701    23004  18294  18470   -972   2160  -1817       C  
-ATOM  10561  N   LEU B 702     -25.635  39.780  44.617  1.00130.19           N  
-ANISOU10561  N   LEU B 702    19216  14671  15578   -401   2243  -1442       N  
-ATOM  10562  CA  LEU B 702     -26.549  38.732  44.187  1.00123.23           C  
-ANISOU10562  CA  LEU B 702    18201  13643  14976   -193   2249  -1298       C  
-ATOM  10563  C   LEU B 702     -25.862  37.368  44.203  1.00116.91           C  
-ANISOU10563  C   LEU B 702    17133  13055  14232   -131   2238  -1161       C  
-ATOM  10564  O   LEU B 702     -26.448  36.358  43.805  1.00115.37           O  
-ANISOU10564  O   LEU B 702    16802  12771  14263     31   2242  -1034       O  
-ATOM  10565  CB  LEU B 702     -27.104  39.054  42.792  1.00125.51           C  
-ANISOU10565  CB  LEU B 702    18629  13623  15436   -211   2194  -1345       C  
-ATOM  10566  CG  LEU B 702     -26.164  39.260  41.590  1.00128.58           C  
-ANISOU10566  CG  LEU B 702    19074  13992  15787   -394   2113  -1426       C  
-ATOM  10567  CD1 LEU B 702     -26.640  40.435  40.738  1.00130.59           C  
-ANISOU10567  CD1 LEU B 702    19597  13968  16055   -490   2078  -1562       C  
-ATOM  10568  CD2 LEU B 702     -24.695  39.457  41.976  1.00131.74           C  
-ANISOU10568  CD2 LEU B 702    19435  14684  15936   -580   2097  -1493       C  
-ATOM  10569  N   ILE B 703     -24.615  37.351  44.665  1.00 88.82           N  
-ANISOU10569  N   ILE B 703    13501   9779  10467   -263   2226  -1188       N  
-ATOM  10570  CA  ILE B 703     -23.838  36.122  44.775  1.00 82.27           C  
-ANISOU10570  CA  ILE B 703    12416   9180   9663   -219   2218  -1063       C  
-ATOM  10571  C   ILE B 703     -23.447  35.859  46.225  1.00 82.68           C  
-ANISOU10571  C   ILE B 703    12342   9520   9551   -183   2270  -1008       C  
-ATOM  10572  O   ILE B 703     -23.686  34.776  46.755  1.00 83.01           O  
-ANISOU10572  O   ILE B 703    12185   9664   9692    -15   2308   -859       O  
-ATOM  10573  CB  ILE B 703     -22.555  36.185  43.922  1.00 76.60           C  
-ANISOU10573  CB  ILE B 703    11689   8559   8857   -412   2149  -1129       C  
-ATOM  10574  CG1 ILE B 703     -22.907  36.363  42.445  1.00 71.71           C  
-ANISOU10574  CG1 ILE B 703    11187   7657   8404   -448   2096  -1176       C  
-ATOM  10575  CG2 ILE B 703     -21.704  34.943  44.134  1.00 73.44           C  
-ANISOU10575  CG2 ILE B 703    11020   8415   8470   -367   2148   -999       C  
-ATOM  10576  CD1 ILE B 703     -23.874  35.327  41.923  1.00 66.24           C  
-ANISOU10576  CD1 ILE B 703    10381   6791   7998   -243   2108  -1036       C  
-ATOM  10577  N   LYS B 704     -22.844  36.858  46.862  1.00 77.07           N  
-ANISOU10577  N   LYS B 704    11754   8942   8586   -345   2271  -1131       N  
-ATOM  10578  CA  LYS B 704     -22.431  36.741  48.254  1.00 78.69           C  
-ANISOU10578  CA  LYS B 704    11865   9424   8609   -335   2315  -1094       C  
-ATOM  10579  C   LYS B 704     -23.654  36.551  49.144  1.00 77.34           C  
-ANISOU10579  C   LYS B 704    11688   9170   8527   -137   2393  -1016       C  
-ATOM  10580  O   LYS B 704     -23.562  36.008  50.242  1.00 79.37           O  
-ANISOU10580  O   LYS B 704    11807   9631   8719    -52   2438   -927       O  
-ATOM  10581  CB  LYS B 704     -21.644  37.976  48.688  1.00 82.15           C  
-ANISOU10581  CB  LYS B 704    12469   9985   8759   -560   2301  -1256       C  
-ATOM  10582  CG  LYS B 704     -21.085  37.875  50.090  1.00 87.29           C  
-ANISOU10582  CG  LYS B 704    13023  10942   9202   -575   2336  -1224       C  
-ATOM  10583  CD  LYS B 704     -20.380  39.152  50.505  1.00 91.15           C  
-ANISOU10583  CD  LYS B 704    13692  11535   9407   -802   2326  -1392       C  
-ATOM  10584  CE  LYS B 704     -20.099  39.156  52.001  1.00 93.96           C  
-ANISOU10584  CE  LYS B 704    13985  12154   9563   -799   2372  -1363       C  
-ATOM  10585  NZ  LYS B 704     -21.353  39.053  52.809  1.00 96.53           N  
-ANISOU10585  NZ  LYS B 704    14335  12366   9976   -611   2454  -1297       N  
-ATOM  10586  N   LYS B 705     -24.802  37.004  48.655  1.00102.55           N  
-ANISOU10586  N   LYS B 705    15032  12061  11873    -65   2409  -1051       N  
-ATOM  10587  CA  LYS B 705     -26.057  36.820  49.363  1.00101.29           C  
-ANISOU10587  CA  LYS B 705    14871  11786  11830    131   2485   -978       C  
-ATOM  10588  C   LYS B 705     -26.504  35.372  49.227  1.00 98.44           C  
-ANISOU10588  C   LYS B 705    14280  11421  11702    341   2501   -797       C  
-ATOM  10589  O   LYS B 705     -26.850  34.727  50.215  1.00 98.60           O  
-ANISOU10589  O   LYS B 705    14171  11554  11739    486   2563   -689       O  
-ATOM  10590  CB  LYS B 705     -27.125  37.757  48.805  1.00100.75           C  
-ANISOU10590  CB  LYS B 705    15031  11387  11861    140   2493  -1070       C  
-ATOM  10591  CG  LYS B 705     -28.306  37.971  49.728  1.00103.39           C  
-ANISOU10591  CG  LYS B 705    15421  11619  12243    290   2580  -1041       C  
-ATOM  10592  CD  LYS B 705     -29.455  38.632  48.990  1.00105.59           C  
-ANISOU10592  CD  LYS B 705    15882  11549  12687    337   2582  -1097       C  
-ATOM  10593  CE  LYS B 705     -29.961  37.745  47.857  1.00106.41           C  
-ANISOU10593  CE  LYS B 705    15884  11477  13070    457   2539  -1000       C  
-ATOM  10594  NZ  LYS B 705     -31.138  38.342  47.161  1.00108.96           N  
-ANISOU10594  NZ  LYS B 705    16374  11461  13565    516   2538  -1043       N  
-ATOM  10595  N   ARG B 706     -26.495  34.863  47.999  1.00 96.92           N  
-ANISOU10595  N   ARG B 706    14041  11097  11689    354   2448   -764       N  
-ATOM  10596  CA  ARG B 706     -26.809  33.461  47.751  1.00 94.44           C  
-ANISOU10596  CA  ARG B 706    13506  10783  11593    535   2460   -597       C  
-ATOM  10597  C   ARG B 706     -25.976  32.549  48.637  1.00 94.38           C  
-ANISOU10597  C   ARG B 706    13274  11099  11486    570   2483   -489       C  
-ATOM  10598  O   ARG B 706     -26.496  31.611  49.231  1.00 95.07           O  
-ANISOU10598  O   ARG B 706    13205  11234  11685    756   2538   -352       O  
-ATOM  10599  CB  ARG B 706     -26.546  33.091  46.293  1.00 95.32           C  
-ANISOU10599  CB  ARG B 706    13599  10765  11854    489   2391   -594       C  
-ATOM  10600  CG  ARG B 706     -27.620  33.518  45.314  1.00 97.69           C  
-ANISOU10600  CG  ARG B 706    14055  10720  12344    530   2371   -636       C  
-ATOM  10601  CD  ARG B 706     -28.850  32.630  45.394  1.00 99.20           C  
-ANISOU10601  CD  ARG B 706    14139  10766  12786    769   2420   -498       C  
-ATOM  10602  NE  ARG B 706     -29.751  32.894  44.276  1.00 99.49           N  
-ANISOU10602  NE  ARG B 706    14298  10483  13019    800   2386   -526       N  
-ATOM  10603  CZ  ARG B 706     -30.649  33.876  44.249  1.00100.30           C  
-ANISOU10603  CZ  ARG B 706    14599  10368  13144    803   2395   -611       C  
-ATOM  10604  NH1 ARG B 706     -30.780  34.694  45.289  1.00100.71           N  
-ANISOU10604  NH1 ARG B 706    14753  10481  13031    778   2444   -678       N  
-ATOM  10605  NH2 ARG B 706     -31.420  34.038  43.180  1.00100.58           N  
-ANISOU10605  NH2 ARG B 706    14730  10120  13364    831   2356   -626       N  
-ATOM  10606  N   LYS B 707     -24.679  32.820  48.718  1.00 70.04           N  
-ANISOU10606  N   LYS B 707     8960   6874  10779    632   1991   -666       N  
-ATOM  10607  CA  LYS B 707     -23.771  31.937  49.444  1.00 70.17           C  
-ANISOU10607  CA  LYS B 707     8703   7098  10860    557   1914   -613       C  
-ATOM  10608  C   LYS B 707     -24.021  31.980  50.946  1.00 69.47           C  
-ANISOU10608  C   LYS B 707     8486   7225  10686    508   1741   -704       C  
-ATOM  10609  O   LYS B 707     -23.854  30.977  51.639  1.00 70.23           O  
-ANISOU10609  O   LYS B 707     8395   7528  10760    526   1639   -637       O  
-ATOM  10610  CB  LYS B 707     -22.315  32.276  49.121  1.00 73.88           C  
-ANISOU10610  CB  LYS B 707     9064   7513  11494    400   2015   -607       C  
-ATOM  10611  CG  LYS B 707     -22.005  32.231  47.635  1.00 74.16           C  
-ANISOU10611  CG  LYS B 707     9213   7362  11604    445   2194   -511       C  
-ATOM  10612  CD  LYS B 707     -20.523  32.391  47.367  1.00 75.41           C  
-ANISOU10612  CD  LYS B 707     9220   7513  11918    287   2290   -495       C  
-ATOM  10613  CE  LYS B 707     -19.733  31.255  47.988  1.00 73.68           C  
-ANISOU10613  CE  LYS B 707     8721   7528  11746    274   2195   -446       C  
-ATOM  10614  NZ  LYS B 707     -18.282  31.369  47.692  1.00 73.46           N  
-ANISOU10614  NZ  LYS B 707     8532   7516  11864    130   2289   -442       N  
-ATOM  10615  N   ASP B 708     -24.422  33.148  51.439  1.00 89.53           N  
-ANISOU10615  N   ASP B 708    11127   9715  13174    454   1707   -855       N  
-ATOM  10616  CA  ASP B 708     -24.793  33.303  52.839  1.00 88.99           C  
-ANISOU10616  CA  ASP B 708    10953   9859  13001    426   1542   -963       C  
-ATOM  10617  C   ASP B 708     -26.079  32.549  53.135  1.00 82.47           C  
-ANISOU10617  C   ASP B 708    10164   9162  12008    582   1451   -916       C  
-ATOM  10618  O   ASP B 708     -26.147  31.769  54.082  1.00 82.59           O  
-ANISOU10618  O   ASP B 708    10006   9419  11955    590   1330   -877       O  
-ATOM  10619  CB  ASP B 708     -24.961  34.779  53.194  1.00 94.45           C  
-ANISOU10619  CB  ASP B 708    11760  10445  13683    346   1528  -1153       C  
-ATOM  10620  CG  ASP B 708     -23.635  35.493  53.354  1.00101.64           C  
-ANISOU10620  CG  ASP B 708    12563  11300  14755    154   1573  -1229       C  
-ATOM  10621  OD1 ASP B 708     -22.606  34.800  53.518  1.00103.10           O  
-ANISOU10621  OD1 ASP B 708    12537  11608  15028     83   1575  -1156       O  
-ATOM  10622  OD2 ASP B 708     -23.621  36.743  53.327  1.00106.11           O  
-ANISOU10622  OD2 ASP B 708    13254  11700  15362     74   1603  -1367       O  
-ATOM  10623  N   GLU B 709     -27.097  32.784  52.317  1.00 72.25           N  
-ANISOU10623  N   GLU B 709     9093   7713  10645    704   1511   -920       N  
-ATOM  10624  CA  GLU B 709     -28.365  32.089  52.468  1.00 64.56           C  
-ANISOU10624  CA  GLU B 709     8161   6849   9519    849   1441   -886       C  
-ATOM  10625  C   GLU B 709     -28.158  30.579  52.515  1.00 59.99           C  
-ANISOU10625  C   GLU B 709     7419   6410   8965    889   1412   -714       C  
-ATOM  10626  O   GLU B 709     -28.967  29.850  53.082  1.00 57.76           O  
-ANISOU10626  O   GLU B 709     7084   6294   8568    957   1319   -674       O  
-ATOM  10627  CB  GLU B 709     -29.320  32.459  51.334  1.00 63.15           C  
-ANISOU10627  CB  GLU B 709     8240   6464   9289    986   1534   -903       C  
-ATOM  10628  CG  GLU B 709     -30.722  31.904  51.509  1.00 62.83           C  
-ANISOU10628  CG  GLU B 709     8249   6541   9084   1130   1461   -906       C  
-ATOM  10629  CD  GLU B 709     -31.653  32.290  50.371  1.00 63.16           C  
-ANISOU10629  CD  GLU B 709     8538   6391   9068   1280   1549   -941       C  
-ATOM  10630  OE1 GLU B 709     -32.879  32.358  50.614  1.00 62.81           O  
-ANISOU10630  OE1 GLU B 709     8571   6425   8869   1386   1483  -1020       O  
-ATOM  10631  OE2 GLU B 709     -31.163  32.525  49.240  1.00 64.00           O  
-ANISOU10631  OE2 GLU B 709     8757   6284   9276   1297   1683   -891       O  
-ATOM  10632  N   ILE B 710     -27.066  30.108  51.929  1.00 49.63           N  
-ANISOU10632  N   ILE B 710     6024   5031   7804    844   1491   -612       N  
-ATOM  10633  CA  ILE B 710     -26.770  28.684  51.952  1.00 46.39           C  
-ANISOU10633  CA  ILE B 710     5457   4733   7435    886   1457   -454       C  
-ATOM  10634  C   ILE B 710     -26.065  28.300  53.248  1.00 48.67           C  
-ANISOU10634  C   ILE B 710     5510   5259   7722    792   1332   -438       C  
-ATOM  10635  O   ILE B 710     -26.315  27.234  53.805  1.00 49.63           O  
-ANISOU10635  O   ILE B 710     5518   5542   7797    839   1241   -333       O  
-ATOM  10636  CB  ILE B 710     -25.935  28.253  50.732  1.00 41.16           C  
-ANISOU10636  CB  ILE B 710     4799   3916   6925    905   1586   -357       C  
-ATOM  10637  CG1 ILE B 710     -26.734  28.478  49.446  1.00 37.74           C  
-ANISOU10637  CG1 ILE B 710     4594   3276   6468   1030   1701   -358       C  
-ATOM  10638  CG2 ILE B 710     -25.539  26.796  50.851  1.00 40.68           C  
-ANISOU10638  CG2 ILE B 710     4566   3973   6919    949   1532   -209       C  
-ATOM  10639  CD1 ILE B 710     -25.999  28.089  48.180  1.00 32.87           C  
-ANISOU10639  CD1 ILE B 710     3988   2520   5980   1066   1834   -269       C  
-ATOM  10640  N   GLN B 711     -25.192  29.174  53.734  1.00 60.57           N  
-ANISOU10640  N   GLN B 711     6944   6787   9282    660   1327   -544       N  
-ATOM  10641  CA  GLN B 711     -24.542  28.940  55.016  1.00 63.90           C  
-ANISOU10641  CA  GLN B 711     7140   7453   9686    579   1202   -557       C  
-ATOM  10642  C   GLN B 711     -25.583  28.928  56.131  1.00 62.29           C  
-ANISOU10642  C   GLN B 711     6921   7450   9297    619   1066   -602       C  
-ATOM  10643  O   GLN B 711     -25.598  28.033  56.972  1.00 61.51           O  
-ANISOU10643  O   GLN B 711     6669   7568   9134    640    960   -509       O  
-ATOM  10644  CB  GLN B 711     -23.477  30.003  55.291  1.00 69.04           C  
-ANISOU10644  CB  GLN B 711     7721   8082  10430    427   1225   -697       C  
-ATOM  10645  CG  GLN B 711     -22.601  29.685  56.491  1.00 76.99           C  
-ANISOU10645  CG  GLN B 711     8469   9346  11437    351   1105   -712       C  
-ATOM  10646  CD  GLN B 711     -21.879  28.363  56.335  1.00 80.96           C  
-ANISOU10646  CD  GLN B 711     8818   9931  12011    394   1095   -540       C  
-ATOM  10647  OE1 GLN B 711     -21.698  27.872  55.221  1.00 84.16           O  
-ANISOU10647  OE1 GLN B 711     9288  10176  12512    444   1200   -440       O  
-ATOM  10648  NE2 GLN B 711     -21.467  27.776  57.450  1.00 84.85           N  
-ANISOU10648  NE2 GLN B 711     9105  10680  12453    387    964   -508       N  
-ATOM  10649  N   GLY B 712     -26.454  29.930  56.123  1.00 67.53           N  
-ANISOU10649  N   GLY B 712     7747   8042   9871    634   1072   -741       N  
-ATOM  10650  CA  GLY B 712     -27.540  30.004  57.076  1.00 64.48           C  
-ANISOU10650  CA  GLY B 712     7360   7845   9295    682    954   -802       C  
-ATOM  10651  C   GLY B 712     -28.334  28.715  57.124  1.00 60.95           C  
-ANISOU10651  C   GLY B 712     6887   7508   8764    785    915   -638       C  
-ATOM  10652  O   GLY B 712     -28.400  28.050  58.162  1.00 61.40           O  
-ANISOU10652  O   GLY B 712     6786   7813   8732    780    803   -572       O  
-ATOM  10653  N   VAL B 713     -28.936  28.354  55.997  1.00 46.81           N  
-ANISOU10653  N   VAL B 713     5250   5534   7002    878   1008   -572       N  
-ATOM  10654  CA  VAL B 713     -29.734  27.138  55.931  1.00 45.67           C  
-ANISOU10654  CA  VAL B 713     5092   5462   6799    971    980   -428       C  
-ATOM  10655  C   VAL B 713     -28.966  25.930  56.468  1.00 48.42           C  
-ANISOU10655  C   VAL B 713     5237   5952   7207    943    918   -256       C  
-ATOM  10656  O   VAL B 713     -29.557  25.001  57.011  1.00 48.89           O  
-ANISOU10656  O   VAL B 713     5229   6161   7186    981    845   -144       O  
-ATOM  10657  CB  VAL B 713     -30.222  26.863  54.500  1.00 40.55           C  
-ANISOU10657  CB  VAL B 713     4616   4578   6215   1075   1099   -385       C  
-ATOM  10658  CG1 VAL B 713     -30.777  25.452  54.384  1.00 37.88           C  
-ANISOU10658  CG1 VAL B 713     4228   4295   5868   1151   1072   -225       C  
-ATOM  10659  CG2 VAL B 713     -31.273  27.891  54.100  1.00 39.26           C  
-ANISOU10659  CG2 VAL B 713     4657   4315   5944   1138   1135   -541       C  
-ATOM  10660  N   ILE B 714     -27.646  25.953  56.326  1.00 54.79           N  
-ANISOU10660  N   ILE B 714     5948   6715   8156    876    947   -235       N  
-ATOM  10661  CA  ILE B 714     -26.818  24.865  56.829  1.00 58.42           C  
-ANISOU10661  CA  ILE B 714     6214   7308   8676    862    882    -85       C  
-ATOM  10662  C   ILE B 714     -26.717  24.929  58.342  1.00 62.45           C  
-ANISOU10662  C   ILE B 714     6563   8105   9060    807    744   -106       C  
-ATOM  10663  O   ILE B 714     -26.682  23.900  59.009  1.00 63.32           O  
-ANISOU10663  O   ILE B 714     6548   8380   9132    832    658     42       O  
-ATOM  10664  CB  ILE B 714     -25.407  24.878  56.207  1.00 59.35           C  
-ANISOU10664  CB  ILE B 714     6262   7313   8976    814    953    -73       C  
-ATOM  10665  CG1 ILE B 714     -25.466  24.371  54.765  1.00 57.34           C  
-ANISOU10665  CG1 ILE B 714     6123   6824   8838    896   1072      4       C  
-ATOM  10666  CG2 ILE B 714     -24.454  24.019  57.027  1.00 58.17           C  
-ANISOU10666  CG2 ILE B 714     5890   7352   8860    791    856     34       C  
-ATOM  10667  CD1 ILE B 714     -24.129  24.355  54.071  1.00 58.20           C  
-ANISOU10667  CD1 ILE B 714     6162   6834   9116    857   1152     16       C  
-ATOM  10668  N   ASP B 715     -26.674  26.143  58.876  1.00 64.67           N  
-ANISOU10668  N   ASP B 715     6849   8445   9277    738    720   -289       N  
-ATOM  10669  CA  ASP B 715     -26.666  26.337  60.319  1.00 69.54           C  
-ANISOU10669  CA  ASP B 715     7316   9353   9754    698    586   -342       C  
-ATOM  10670  C   ASP B 715     -27.941  25.773  60.920  1.00 67.81           C  
-ANISOU10670  C   ASP B 715     7113   9300   9353    765    514   -266       C  
-ATOM  10671  O   ASP B 715     -27.902  24.960  61.840  1.00 69.42           O  
-ANISOU10671  O   ASP B 715     7171   9732   9473    774    418   -141       O  
-ATOM  10672  CB  ASP B 715     -26.553  27.821  60.662  1.00 73.83           C  
-ANISOU10672  CB  ASP B 715     7888   9897  10266    624    577   -582       C  
-ATOM  10673  CG  ASP B 715     -25.248  28.429  60.189  1.00 80.03           C  
-ANISOU10673  CG  ASP B 715     8636  10538  11232    530    647   -664       C  
-ATOM  10674  OD1 ASP B 715     -24.270  27.670  60.003  1.00 82.93           O  
-ANISOU10674  OD1 ASP B 715     8883  10912  11714    516    662   -546       O  
-ATOM  10675  OD2 ASP B 715     -25.198  29.666  60.006  1.00 81.79           O  
-ANISOU10675  OD2 ASP B 715     8949  10642  11485    468    687   -847       O  
-ATOM  10676  N   GLU B 716     -29.071  26.218  60.388  1.00 73.71           N  
-ANISOU10676  N   GLU B 716     8036   9936  10033    813    563   -342       N  
-ATOM  10677  CA  GLU B 716     -30.369  25.745  60.837  1.00 69.71           C  
-ANISOU10677  CA  GLU B 716     7554   9578   9354    872    511   -289       C  
-ATOM  10678  C   GLU B 716     -30.382  24.226  60.975  1.00 67.42           C  
-ANISOU10678  C   GLU B 716     7172   9360   9084    903    483    -43       C  
-ATOM  10679  O   GLU B 716     -30.815  23.692  61.999  1.00 67.78           O  
-ANISOU10679  O   GLU B 716     7111   9655   8988    901    391     44       O  
-ATOM  10680  CB  GLU B 716     -31.459  26.201  59.867  1.00 68.66           C  
-ANISOU10680  CB  GLU B 716     7636   9255   9198    941    595   -379       C  
-ATOM  10681  CG  GLU B 716     -31.545  27.711  59.697  1.00 69.93           C  
-ANISOU10681  CG  GLU B 716     7916   9319   9337    925    619   -616       C  
-ATOM  10682  CD  GLU B 716     -32.336  28.115  58.466  1.00 68.85           C  
-ANISOU10682  CD  GLU B 716     8007   8932   9222   1007    723   -681       C  
-ATOM  10683  OE1 GLU B 716     -32.927  27.226  57.818  1.00 69.83           O  
-ANISOU10683  OE1 GLU B 716     8184   8991   9359   1079    768   -561       O  
-ATOM  10684  OE2 GLU B 716     -32.363  29.320  58.141  1.00 67.81           O  
-ANISOU10684  OE2 GLU B 716     8003   8666   9097   1004    758   -855       O  
-ATOM  10685  N   ILE B 717     -29.899  23.536  59.948  1.00 51.57           N  
-ANISOU10685  N   ILE B 717     5206   7134   7253    932    562     71       N  
-ATOM  10686  CA  ILE B 717     -29.894  22.078  59.942  1.00 50.21           C  
-ANISOU10686  CA  ILE B 717     4967   6981   7131    969    539    299       C  
-ATOM  10687  C   ILE B 717     -28.900  21.507  60.953  1.00 52.24           C  
-ANISOU10687  C   ILE B 717     5025   7434   7391    932    440    416       C  
-ATOM  10688  O   ILE B 717     -29.130  20.445  61.529  1.00 52.33           O  
-ANISOU10688  O   ILE B 717     4957   7570   7355    952    374    599       O  
-ATOM  10689  CB  ILE B 717     -29.585  21.522  58.541  1.00 46.07           C  
-ANISOU10689  CB  ILE B 717     4533   6171   6801   1024    642    366       C  
-ATOM  10690  CG1 ILE B 717     -30.682  21.927  57.558  1.00 45.13           C  
-ANISOU10690  CG1 ILE B 717     4607   5880   6660   1084    731    271       C  
-ATOM  10691  CG2 ILE B 717     -29.459  20.009  58.576  1.00 44.48           C  
-ANISOU10691  CG2 ILE B 717     4252   5976   6674   1063    603    593       C  
-ATOM  10692  CD1 ILE B 717     -30.483  21.375  56.164  1.00 43.78           C  
-ANISOU10692  CD1 ILE B 717     4524   5450   6660   1154    831    326       C  
-ATOM  10693  N   ARG B 718     -27.796  22.214  61.165  1.00 63.63           N  
-ANISOU10693  N   ARG B 718     6387   8903   8887    879    431    309       N  
-ATOM  10694  CA  ARG B 718     -26.811  21.804  62.159  1.00 65.94           C  
-ANISOU10694  CA  ARG B 718     6481   9405   9167    854    331    385       C  
-ATOM  10695  C   ARG B 718     -27.390  21.948  63.565  1.00 65.60           C  
-ANISOU10695  C   ARG B 718     6344   9681   8900    839    217    377       C  
-ATOM  10696  O   ARG B 718     -27.201  21.078  64.417  1.00 66.38           O  
-ANISOU10696  O   ARG B 718     6313   9975   8932    858    127    542       O  
-ATOM  10697  CB  ARG B 718     -25.529  22.632  62.031  1.00 70.83           C  
-ANISOU10697  CB  ARG B 718     7030   9986   9897    792    354    238       C  
-ATOM  10698  CG  ARG B 718     -24.787  22.455  60.719  1.00 75.22           C  
-ANISOU10698  CG  ARG B 718     7645  10269  10666    802    466    255       C  
-ATOM  10699  CD  ARG B 718     -23.389  21.903  60.946  1.00 81.25           C  
-ANISOU10699  CD  ARG B 718     8231  11105  11537    794    424    323       C  
-ATOM  10700  NE  ARG B 718     -23.221  20.587  60.337  1.00 85.38           N  
-ANISOU10700  NE  ARG B 718     8753  11519  12168    877    435    520       N  
-ATOM  10701  CZ  ARG B 718     -22.742  20.389  59.114  1.00 87.61           C  
-ANISOU10701  CZ  ARG B 718     9093  11573  12620    903    535    528       C  
-ATOM  10702  NH1 ARG B 718     -22.376  21.426  58.372  1.00 89.73           N  
-ANISOU10702  NH1 ARG B 718     9429  11701  12965    844    642    367       N  
-ATOM  10703  NH2 ARG B 718     -22.625  19.157  58.636  1.00 88.88           N  
-ANISOU10703  NH2 ARG B 718     9246  11650  12876    990    528    697       N  
-ATOM  10704  N   MET B 719     -28.090  23.054  63.800  1.00 59.69           N  
-ANISOU10704  N   MET B 719     5661   8986   8031    813    218    185       N  
-ATOM  10705  CA  MET B 719     -28.742  23.293  65.079  1.00 60.29           C  
-ANISOU10705  CA  MET B 719     5652   9377   7878    807    114    149       C  
-ATOM  10706  C   MET B 719     -29.708  22.160  65.378  1.00 58.74           C  
-ANISOU10706  C   MET B 719     5459   9284   7577    849     88    363       C  
-ATOM  10707  O   MET B 719     -29.706  21.590  66.467  1.00 59.73           O  
-ANISOU10707  O   MET B 719     5447   9676   7570    852     -6    489       O  
-ATOM  10708  CB  MET B 719     -29.508  24.617  65.046  1.00 61.75           C  
-ANISOU10708  CB  MET B 719     5943   9553   7966    793    131    -99       C  
-ATOM  10709  CG  MET B 719     -28.639  25.853  64.946  1.00 67.18           C  
-ANISOU10709  CG  MET B 719     6623  10163   8739    735    143   -326       C  
-ATOM  10710  SD  MET B 719     -28.317  26.623  66.544  1.00 72.52           S  
-ANISOU10710  SD  MET B 719     7105  11209   9240    698     -3   -492       S  
-ATOM  10711  CE  MET B 719     -27.434  25.321  67.403  1.00 77.13           C  
-ANISOU10711  CE  MET B 719     7466  12032   9806    712    -91   -252       C  
-ATOM  10712  N   HIS B 720     -30.531  21.837  64.390  1.00 55.01           N  
-ANISOU10712  N   HIS B 720     5142   8596   7165    881    175    403       N  
-ATOM  10713  CA  HIS B 720     -31.573  20.832  64.540  1.00 54.25           C  
-ANISOU10713  CA  HIS B 720     5065   8563   6986    906    167    582       C  
-ATOM  10714  C   HIS B 720     -31.047  19.510  65.079  1.00 57.20           C  
-ANISOU10714  C   HIS B 720     5315   9027   7390    912    106    849       C  
-ATOM  10715  O   HIS B 720     -31.822  18.643  65.467  1.00 58.05           O  
-ANISOU10715  O   HIS B 720     5409   9232   7414    916     82   1021       O  
-ATOM  10716  CB  HIS B 720     -32.263  20.604  63.202  1.00 48.34           C  
-ANISOU10716  CB  HIS B 720     4491   7523   6354    946    276    578       C  
-ATOM  10717  CG  HIS B 720     -33.373  19.611  63.259  1.00 43.22           C  
-ANISOU10717  CG  HIS B 720     3865   6916   5641    962    276    737       C  
-ATOM  10718  ND1 HIS B 720     -34.638  19.935  63.699  1.00 42.14           N  
-ANISOU10718  ND1 HIS B 720     3755   6948   5310    956    263    665       N  
-ATOM  10719  CD2 HIS B 720     -33.415  18.300  62.923  1.00 41.77           C  
-ANISOU10719  CD2 HIS B 720     3677   6625   5568    978    288    956       C  
-ATOM  10720  CE1 HIS B 720     -35.410  18.866  63.632  1.00 42.50           C  
-ANISOU10720  CE1 HIS B 720     3807   6992   5350    957    274    837       C  
-ATOM  10721  NE2 HIS B 720     -34.695  17.862  63.164  1.00 41.38           N  
-ANISOU10721  NE2 HIS B 720     3652   6674   5398    969    288   1016       N  
-ATOM  10722  N   LEU B 721     -29.731  19.348  65.089  1.00 53.25           N  
-ANISOU10722  N   LEU B 721     4727   8492   7014    914     82    884       N  
-ATOM  10723  CA  LEU B 721     -29.143  18.132  65.622  1.00 58.92           C  
-ANISOU10723  CA  LEU B 721     5330   9296   7762    937     13   1130       C  
-ATOM  10724  C   LEU B 721     -29.480  18.029  67.105  1.00 64.77           C  
-ANISOU10724  C   LEU B 721     5942  10403   8266    923    -94   1207       C  
-ATOM  10725  O   LEU B 721     -29.761  16.946  67.620  1.00 66.28           O  
-ANISOU10725  O   LEU B 721     6090  10690   8405    937   -139   1446       O  
-ATOM  10726  CB  LEU B 721     -27.632  18.125  65.411  1.00 56.66           C  
-ANISOU10726  CB  LEU B 721     4957   8938   7632    950     -1   1114       C  
-ATOM  10727  CG  LEU B 721     -26.943  16.843  65.872  1.00 55.91           C  
-ANISOU10727  CG  LEU B 721     4754   8908   7583    997    -78   1363       C  
-ATOM  10728  CD1 LEU B 721     -27.429  15.665  65.046  1.00 51.55           C  
-ANISOU10728  CD1 LEU B 721     4305   8117   7164   1038    -32   1554       C  
-ATOM  10729  CD2 LEU B 721     -25.437  16.979  65.788  1.00 56.18           C  
-ANISOU10729  CD2 LEU B 721     4678   8928   7741   1013   -103   1306       C  
-ATOM  10730  N   GLN B 722     -29.451  19.172  67.782  1.00 82.09           N  
-ANISOU10730  N   GLN B 722     8075  12799  10315    895   -135   1000       N  
-ATOM  10731  CA  GLN B 722     -29.861  19.258  69.177  1.00 88.34           C  
-ANISOU10731  CA  GLN B 722     8743  13968  10854    889   -233   1028       C  
-ATOM  10732  C   GLN B 722     -31.180  18.528  69.407  1.00 87.30           C  
-ANISOU10732  C   GLN B 722     8659  13917  10594    884   -222   1196       C  
-ATOM  10733  O   GLN B 722     -31.214  17.463  70.024  1.00 88.39           O  
-ANISOU10733  O   GLN B 722     8727  14182  10676    894   -270   1451       O  
-ATOM  10734  CB  GLN B 722     -30.003  20.722  69.597  1.00 95.79           C  
-ANISOU10734  CB  GLN B 722     9663  15060  11671    864   -258    729       C  
-ATOM  10735  CG  GLN B 722     -28.692  21.393  69.966  1.00107.57           C  
-ANISOU10735  CG  GLN B 722    11031  16625  13214    854   -312    582       C  
-ATOM  10736  CD  GLN B 722     -28.118  20.858  71.262  1.00115.72           C  
-ANISOU10736  CD  GLN B 722    11866  17997  14106    883   -433    713       C  
-ATOM  10737  OE1 GLN B 722     -27.548  19.767  71.300  1.00118.85           O  
-ANISOU10737  OE1 GLN B 722    12214  18372  14573    917   -455    945       O  
-ATOM  10738  NE2 GLN B 722     -28.273  21.623  72.337  1.00119.28           N  
-ANISOU10738  NE2 GLN B 722    12202  18769  14350    882   -519    561       N  
-ATOM  10739  N   GLU B 723     -32.265  19.106  68.902  1.00 79.20           N  
-ANISOU10739  N   GLU B 723     7753  12816   9522    869   -158   1053       N  
-ATOM  10740  CA AGLU B 723     -33.589  18.527  69.080  0.50 77.99           C  
-ANISOU10740  CA AGLU B 723     7638  12751   9242    855   -139   1174       C  
-ATOM  10741  CA BGLU B 723     -33.594  18.526  69.067  0.50 77.93           C  
-ANISOU10741  CA BGLU B 723     7633  12740   9237    855   -138   1173       C  
-ATOM  10742  C   GLU B 723     -33.615  17.061  68.651  1.00 90.65           C  
-ANISOU10742  C   GLU B 723     9275  14181  10988    856   -109   1465       C  
-ATOM  10743  O   GLU B 723     -34.311  16.243  69.251  1.00100.63           O  
-ANISOU10743  O   GLU B 723    10499  15595  12139    832   -130   1665       O  
-ATOM  10744  CB AGLU B 723     -34.629  19.338  68.304  0.50 61.88           C  
-ANISOU10744  CB AGLU B 723     5742  10585   7185    856    -63    957       C  
-ATOM  10745  CB BGLU B 723     -34.634  19.317  68.267  0.50 61.79           C  
-ANISOU10745  CB BGLU B 723     5734  10563   7179    856    -60    959       C  
-ATOM  10746  CG AGLU B 723     -34.439  20.844  68.425  0.50 49.95           C  
-ANISOU10746  CG AGLU B 723     4239   9134   5607    864    -83    647       C  
-ATOM  10747  CG BGLU B 723     -35.988  18.631  68.149  0.50 59.12           C  
-ANISOU10747  CG BGLU B 723     5451  10250   6763    840    -19   1072       C  
-ATOM  10748  CD AGLU B 723     -34.268  21.307  69.864  0.50 52.96           C  
-ANISOU10748  CD AGLU B 723     4452   9908   5764    856   -196    592       C  
-ATOM  10749  CD BGLU B 723     -36.635  18.353  69.495  0.50 63.48           C  
-ANISOU10749  CD BGLU B 723     5871  11195   7053    807    -90   1182       C  
-ATOM  10750  OE1AGLU B 723     -34.850  20.676  70.774  0.50 56.64           O  
-ANISOU10750  OE1AGLU B 723     4823  10652   6046    846   -244    751       O  
-ATOM  10751  OE1BGLU B 723     -36.327  19.069  70.471  0.50 62.37           O  
-ANISOU10751  OE1BGLU B 723     5618  11334   6744    813   -170   1075       O  
-ATOM  10752  OE2AGLU B 723     -33.540  22.299  70.085  0.50 52.38           O  
-ANISOU10752  OE2AGLU B 723     4335   9870   5698    857   -235    388       O  
-ATOM  10753  OE2BGLU B 723     -37.454  17.414  69.577  0.50 67.76           O  
-ANISOU10753  OE2BGLU B 723     6416  11773   7557    774    -65   1373       O  
-ATOM  10754  N   ILE B 724     -32.849  16.736  67.615  1.00 71.31           N  
-ANISOU10754  N   ILE B 724     6894  11413   8787    884    -61   1486       N  
-ATOM  10755  CA  ILE B 724     -32.754  15.362  67.139  1.00 71.68           C  
-ANISOU10755  CA  ILE B 724     6973  11266   8998    899    -42   1739       C  
-ATOM  10756  C   ILE B 724     -32.219  14.450  68.237  1.00 74.89           C  
-ANISOU10756  C   ILE B 724     7246  11876   9334    903   -138   1996       C  
-ATOM  10757  O   ILE B 724     -32.635  13.298  68.360  1.00 76.68           O  
-ANISOU10757  O   ILE B 724     7481  12070   9585    893   -144   2243       O  
-ATOM  10758  CB  ILE B 724     -31.860  15.252  65.888  1.00 68.11           C  
-ANISOU10758  CB  ILE B 724     6594  10470   8813    943     15   1692       C  
-ATOM  10759  CG1 ILE B 724     -32.660  15.609  64.635  1.00 65.63           C  
-ANISOU10759  CG1 ILE B 724     6441   9905   8591    952    123   1545       C  
-ATOM  10760  CG2 ILE B 724     -31.310  13.849  65.748  1.00 68.55           C  
-ANISOU10760  CG2 ILE B 724     6624  10394   9026    976    -14   1956       C  
-ATOM  10761  CD1 ILE B 724     -31.898  15.399  63.349  1.00 62.93           C  
-ANISOU10761  CD1 ILE B 724     6173   9235   8501   1001    187   1517       C  
-ATOM  10762  N   ARG B 725     -31.298  14.978  69.037  1.00 69.80           N  
-ANISOU10762  N   ARG B 725     6477  11439   8603    921   -215   1933       N  
-ATOM  10763  CA  ARG B 725     -30.692  14.217  70.122  1.00 73.80           C  
-ANISOU10763  CA  ARG B 725     6850  12167   9025    946   -316   2159       C  
-ATOM  10764  C   ARG B 725     -31.702  13.914  71.223  1.00 76.45           C  
-ANISOU10764  C   ARG B 725     7131  12811   9107    908   -353   2304       C  
-ATOM  10765  O   ARG B 725     -31.678  12.839  71.821  1.00 78.89           O  
-ANISOU10765  O   ARG B 725     7394  13201   9378    917   -399   2589       O  
-ATOM  10766  CB  ARG B 725     -29.488  14.968  70.696  1.00 73.42           C  
-ANISOU10766  CB  ARG B 725     6672  12290   8935    978   -390   2014       C  
-ATOM  10767  CG  ARG B 725     -28.322  15.121  69.730  1.00 71.29           C  
-ANISOU10767  CG  ARG B 725     6424  11751   8911   1010   -359   1910       C  
-ATOM  10768  CD  ARG B 725     -27.121  15.736  70.439  1.00 70.71           C  
-ANISOU10768  CD  ARG B 725     6195  11885   8788   1034   -441   1788       C  
-ATOM  10769  NE  ARG B 725     -25.848  15.381  69.817  1.00 69.47           N  
-ANISOU10769  NE  ARG B 725     6010  11540   8847   1079   -442   1801       N  
-ATOM  10770  CZ  ARG B 725     -25.056  16.240  69.185  1.00 67.70           C  
-ANISOU10770  CZ  ARG B 725     5777  11194   8751   1061   -400   1571       C  
-ATOM  10771  NH1 ARG B 725     -25.404  17.514  69.079  1.00 67.08           N  
-ANISOU10771  NH1 ARG B 725     5733  11136   8618    999   -357   1313       N  
-ATOM  10772  NH2 ARG B 725     -23.915  15.823  68.654  1.00 68.49           N  
-ANISOU10772  NH2 ARG B 725     5837  11150   9035   1104   -401   1598       N  
-ATOM  10773  N   LYS B 726     -32.586  14.870  71.489  1.00 82.63           N  
-ANISOU10773  N   LYS B 726     7918  13765   9713    870   -333   2110       N  
-ATOM  10774  CA  LYS B 726     -33.658  14.671  72.454  1.00 86.24           C  
-ANISOU10774  CA  LYS B 726     8321  14529   9917    829   -355   2218       C  
-ATOM  10775  C   LYS B 726     -34.582  13.552  71.986  1.00 88.61           C  
-ANISOU10775  C   LYS B 726     8714  14658  10294    783   -289   2444       C  
-ATOM  10776  O   LYS B 726     -34.708  12.523  72.647  1.00 91.49           O  
-ANISOU10776  O   LYS B 726     9030  15132  10599    765   -322   2735       O  
-ATOM  10777  CB  LYS B 726     -34.454  15.962  72.641  1.00 82.45           C  
-ANISOU10777  CB  LYS B 726     7841  14230   9257    809   -343   1925       C  
-ATOM  10778  CG  LYS B 726     -33.602  17.184  72.933  1.00 80.84           C  
-ANISOU10778  CG  LYS B 726     7565  14136   9015    845   -399   1655       C  
-ATOM  10779  CD  LYS B 726     -34.459  18.345  73.422  1.00 78.09           C  
-ANISOU10779  CD  LYS B 726     7193  14036   8443    834   -415   1399       C  
-ATOM  10780  CE  LYS B 726     -33.603  19.535  73.855  1.00 76.04           C  
-ANISOU10780  CE  LYS B 726     6845  13907   8141    864   -485   1133       C  
-ATOM  10781  NZ  LYS B 726     -34.392  20.538  74.638  1.00 74.77           N  
-ANISOU10781  NZ  LYS B 726     6622  14067   7722    869   -534    912       N  
-ATOM  10782  N   ILE B 727     -35.222  13.762  70.840  1.00 89.68           N  
-ANISOU10782  N   ILE B 727     8984  14525  10566    765   -197   2307       N  
-ATOM  10783  CA  ILE B 727     -36.095  12.761  70.234  1.00 93.10           C  
-ANISOU10783  CA  ILE B 727     9508  14761  11105    721   -129   2474       C  
-ATOM  10784  C   ILE B 727     -35.526  11.348  70.344  1.00 95.62           C  
-ANISOU10784  C   ILE B 727     9813  14952  11565    727   -161   2805       C  
-ATOM  10785  O   ILE B 727     -36.256  10.396  70.619  1.00 97.47           O  
-ANISOU10785  O   ILE B 727    10053  15207  11774    669   -147   3035       O  
-ATOM  10786  CB  ILE B 727     -36.349  13.077  68.742  1.00 91.98           C  
-ANISOU10786  CB  ILE B 727     9515  14263  11171    740    -36   2281       C  
-ATOM  10787  CG1 ILE B 727     -37.076  14.416  68.590  1.00 92.40           C  
-ANISOU10787  CG1 ILE B 727     9605  14421  11082    740     -2   1968       C  
-ATOM  10788  CG2 ILE B 727     -37.144  11.961  68.084  1.00 92.49           C  
-ANISOU10788  CG2 ILE B 727     9660  14110  11372    702     25   2447       C  
-ATOM  10789  CD1 ILE B 727     -37.253  14.846  67.149  1.00 91.56           C  
-ANISOU10789  CD1 ILE B 727     9648  13983  11159    778     86   1770       C  
-ATOM  10790  N   LEU B 728     -34.220  11.217  70.131  1.00 90.37           N  
-ANISOU10790  N   LEU B 728     9130  14155  11051    797   -206   2824       N  
-ATOM  10791  CA  LEU B 728     -33.566   9.913  70.172  1.00 94.32           C  
-ANISOU10791  CA  LEU B 728     9624  14511  11701    828   -249   3117       C  
-ATOM  10792  C   LEU B 728     -33.055   9.590  71.569  1.00 97.44           C  
-ANISOU10792  C   LEU B 728     9887  15228  11909    848   -351   3319       C  
-ATOM  10793  O   LEU B 728     -32.722   8.442  71.870  1.00100.29           O  
-ANISOU10793  O   LEU B 728    10239  15533  12335    869   -397   3609       O  
-ATOM  10794  CB  LEU B 728     -32.402   9.865  69.182  1.00 95.64           C  
-ANISOU10794  CB  LEU B 728     9834  14377  12129    909   -247   3034       C  
-ATOM  10795  CG  LEU B 728     -32.734  10.167  67.721  1.00 95.40           C  
-ANISOU10795  CG  LEU B 728     9934  14020  12295    911   -147   2839       C  
-ATOM  10796  CD1 LEU B 728     -31.478  10.109  66.864  1.00 95.97           C  
-ANISOU10796  CD1 LEU B 728    10022  13845  12599    993   -150   2773       C  
-ATOM  10797  CD2 LEU B 728     -33.793   9.206  67.201  1.00 95.49           C  
-ANISOU10797  CD2 LEU B 728    10035  13844  12401    866    -91   2982       C  
-ATOM  10798  N   LYS B 729     -33.000  10.610  72.420  1.00 90.45           N  
-ANISOU10798  N   LYS B 729     8899  14679  10788    850   -392   3161       N  
-ATOM  10799  CA  LYS B 729     -32.430  10.465  73.752  1.00 94.67           C  
-ANISOU10799  CA  LYS B 729     9292  15556  11124    889   -496   3308       C  
-ATOM  10800  C   LYS B 729     -31.021   9.888  73.653  1.00 96.36           C  
-ANISOU10800  C   LYS B 729     9474  15636  11503    984   -565   3417       C  
-ATOM  10801  O   LYS B 729     -30.640   9.005  74.425  1.00 99.99           O  
-ANISOU10801  O   LYS B 729     9877  16211  11904   1026   -639   3692       O  
-ATOM  10802  CB  LYS B 729     -33.324   9.593  74.638  1.00 97.85           C  
-ANISOU10802  CB  LYS B 729     9669  16158  11352    831   -503   3610       C  
-ATOM  10803  CG  LYS B 729     -34.638  10.261  75.033  1.00 97.66           C  
-ANISOU10803  CG  LYS B 729     9626  16385  11096    747   -454   3490       C  
-ATOM  10804  CD  LYS B 729     -35.521   9.336  75.864  1.00 97.98           C  
-ANISOU10804  CD  LYS B 729     9636  16619  10972    674   -448   3807       C  
-ATOM  10805  CE  LYS B 729     -36.381   8.441  74.986  1.00 94.29           C  
-ANISOU10805  CE  LYS B 729     9299  15830  10698    589   -355   3943       C  
-ATOM  10806  NZ  LYS B 729     -37.439   9.215  74.279  1.00 92.64           N  
-ANISOU10806  NZ  LYS B 729     9149  15571  10479    530   -267   3669       N  
-ATOM  10807  N   ASN B 730     -30.258  10.399  72.691  1.00 80.79           N  
-ANISOU10807  N   ASN B 730     7539  13425   9731   1022   -540   3199       N  
-ATOM  10808  CA  ASN B 730     -28.893   9.946  72.461  1.00 81.17           C  
-ANISOU10808  CA  ASN B 730     7552  13340   9949   1115   -599   3255       C  
-ATOM  10809  C   ASN B 730     -27.970  11.104  72.102  1.00 80.09           C  
-ANISOU10809  C   ASN B 730     7361  13203   9865   1142   -600   2937       C  
-ATOM  10810  O   ASN B 730     -27.748  11.382  70.925  1.00 79.61           O  
-ANISOU10810  O   ASN B 730     7387  12850  10013   1138   -528   2782       O  
-ATOM  10811  CB  ASN B 730     -28.856   8.878  71.363  1.00 79.50           C  
-ANISOU10811  CB  ASN B 730     7464  12723  10018   1133   -555   3400       C  
-ATOM  10812  CG  ASN B 730     -27.450   8.389  71.069  1.00 78.40           C  
-ANISOU10812  CG  ASN B 730     7285  12446  10058   1241   -619   3444       C  
-ATOM  10813  OD1 ASN B 730     -26.494   8.769  71.744  1.00 78.62           O  
-ANISOU10813  OD1 ASN B 730     7186  12691   9994   1300   -699   3388       O  
-ATOM  10814  ND2 ASN B 730     -27.318   7.538  70.062  1.00 76.01           N  
-ANISOU10814  ND2 ASN B 730     7080  11792  10008   1273   -589   3531       N  
-ATOM  10815  N   PRO B 731     -27.436  11.789  73.124  1.00 93.13           N  
-ANISOU10815  N   PRO B 731     8867  15191  11326   1167   -680   2839       N  
-ATOM  10816  CA  PRO B 731     -26.504  12.910  72.957  1.00 92.80           C  
-ANISOU10816  CA  PRO B 731     8750  15186  11323   1181   -691   2538       C  
-ATOM  10817  C   PRO B 731     -25.309  12.576  72.067  1.00 92.95           C  
-ANISOU10817  C   PRO B 731     8778  14936  11604   1238   -686   2516       C  
-ATOM  10818  O   PRO B 731     -24.505  13.463  71.782  1.00 93.36           O  
-ANISOU10818  O   PRO B 731     8774  14979  11721   1235   -678   2270       O  
-ATOM  10819  CB  PRO B 731     -26.023  13.173  74.384  1.00 93.88           C  
-ANISOU10819  CB  PRO B 731     8706  15746  11218   1227   -810   2546       C  
-ATOM  10820  CG  PRO B 731     -27.148  12.739  75.239  1.00 92.43           C  
-ANISOU10820  CG  PRO B 731     8526  15786  10808   1200   -824   2746       C  
-ATOM  10821  CD  PRO B 731     -27.786  11.570  74.538  1.00 95.39           C  
-ANISOU10821  CD  PRO B 731     9047  15864  11333   1177   -760   3003       C  
-ATOM  10822  N   SER B 732     -25.187  11.323  71.642  1.00 87.34           N  
-ANISOU10822  N   SER B 732     8131  14013  11042   1287   -690   2763       N  
-ATOM  10823  CA  SER B 732     -24.081  10.923  70.778  1.00 87.68           C  
-ANISOU10823  CA  SER B 732     8177  13808  11329   1354   -689   2746       C  
-ATOM  10824  C   SER B 732     -24.488  10.942  69.308  1.00 84.92           C  
-ANISOU10824  C   SER B 732     7982  13082  11203   1317   -568   2656       C  
-ATOM  10825  O   SER B 732     -23.656  10.741  68.420  1.00 84.46           O  
-ANISOU10825  O   SER B 732     7935  12804  11353   1365   -547   2603       O  
-ATOM  10826  CB  SER B 732     -23.574   9.533  71.162  1.00 89.35           C  
-ANISOU10826  CB  SER B 732     8360  14005  11585   1456   -781   3053       C  
-ATOM  10827  OG  SER B 732     -23.226   9.486  72.534  1.00 90.93           O  
-ANISOU10827  OG  SER B 732     8422  14568  11561   1505   -894   3151       O  
-ATOM  10828  N   ALA B 733     -25.773  11.177  69.061  1.00 89.51           N  
-ANISOU10828  N   ALA B 733     8673  13607  11728   1240   -491   2634       N  
-ATOM  10829  CA  ALA B 733     -26.300  11.228  67.702  1.00 84.23           C  
-ANISOU10829  CA  ALA B 733     8154  12608  11243   1212   -376   2542       C  
-ATOM  10830  C   ALA B 733     -25.564  12.278  66.881  1.00 80.29           C  
-ANISOU10830  C   ALA B 733     7655  11996  10855   1206   -315   2260       C  
-ATOM  10831  O   ALA B 733     -25.374  13.407  67.335  1.00 80.14           O  
-ANISOU10831  O   ALA B 733     7571  12160  10717   1164   -320   2062       O  
-ATOM  10832  CB  ALA B 733     -27.788  11.521  67.727  1.00 82.19           C  
-ANISOU10832  CB  ALA B 733     7988  12377  10862   1133   -313   2520       C  
-ATOM  10833  N   GLN B 734     -25.153  11.904  65.673  1.00 92.81           N  
-ANISOU10833  N   GLN B 734     9311  13282  12671   1246   -256   2242       N  
-ATOM  10834  CA  GLN B 734     -24.378  12.800  64.825  1.00 88.40           C  
-ANISOU10834  CA  GLN B 734     8752  12604  12232   1238   -188   2004       C  
-ATOM  10835  C   GLN B 734     -24.712  12.629  63.345  1.00 83.45           C  
-ANISOU10835  C   GLN B 734     8268  11642  11797   1254    -77   1954       C  
-ATOM  10836  O   GLN B 734     -24.894  11.510  62.868  1.00 82.03           O  
-ANISOU10836  O   GLN B 734     8140  11288  11740   1311    -82   2120       O  
-ATOM  10837  CB  GLN B 734     -22.883  12.577  65.056  1.00 91.34           C  
-ANISOU10837  CB  GLN B 734     8980  13047  12679   1299   -260   2010       C  
-ATOM  10838  CG  GLN B 734     -21.985  13.448  64.193  1.00 94.45           C  
-ANISOU10838  CG  GLN B 734     9355  13329  13204   1279   -185   1776       C  
-ATOM  10839  CD  GLN B 734     -22.189  14.930  64.443  1.00 96.09           C  
-ANISOU10839  CD  GLN B 734     9558  13654  13297   1181   -139   1534       C  
-ATOM  10840  OE1 GLN B 734     -21.861  15.442  65.515  1.00 98.84           O  
-ANISOU10840  OE1 GLN B 734     9783  14271  13501   1155   -216   1473       O  
-ATOM  10841  NE2 GLN B 734     -22.737  15.628  63.453  1.00 96.24           N  
-ANISOU10841  NE2 GLN B 734     9715  13472  13381   1134    -19   1391       N  
-ATOM  10842  N   TYR B 735     -24.797  13.748  62.629  1.00 76.43           N  
-ANISOU10842  N   TYR B 735     7445  10665  10931   1208     22   1725       N  
-ATOM  10843  CA  TYR B 735     -25.012  13.730  61.183  1.00 72.55           C  
-ANISOU10843  CA  TYR B 735     7082   9875  10607   1233    134   1653       C  
-ATOM  10844  C   TYR B 735     -23.879  13.004  60.472  1.00 75.09           C  
-ANISOU10844  C   TYR B 735     7354  10046  11132   1312    129   1706       C  
-ATOM  10845  O   TYR B 735     -22.725  13.067  60.901  1.00 77.36           O  
-ANISOU10845  O   TYR B 735     7507  10451  11434   1325     72   1691       O  
-ATOM  10846  CB  TYR B 735     -25.094  15.157  60.631  1.00 65.21           C  
-ANISOU10846  CB  TYR B 735     6220   8898   9657   1174    234   1401       C  
-ATOM  10847  CG  TYR B 735     -26.368  15.892  60.959  1.00 55.70           C  
-ANISOU10847  CG  TYR B 735     5107   7773   8285   1120    260   1315       C  
-ATOM  10848  CD1 TYR B 735     -27.576  15.220  61.059  1.00 51.11           C  
-ANISOU10848  CD1 TYR B 735     4596   7182   7640   1131    252   1436       C  
-ATOM  10849  CD2 TYR B 735     -26.361  17.261  61.169  1.00 52.18           C  
-ANISOU10849  CD2 TYR B 735     4670   7411   7746   1056    288   1104       C  
-ATOM  10850  CE1 TYR B 735     -28.745  15.897  61.362  1.00 45.73           C  
-ANISOU10850  CE1 TYR B 735     3986   6594   6795   1088    273   1344       C  
-ATOM  10851  CE2 TYR B 735     -27.523  17.944  61.472  1.00 46.87           C  
-ANISOU10851  CE2 TYR B 735     4078   6817   6914   1022    302   1011       C  
-ATOM  10852  CZ  TYR B 735     -28.709  17.259  61.568  1.00 44.58           C  
-ANISOU10852  CZ  TYR B 735     3850   6538   6552   1041    294   1128       C  
-ATOM  10853  OH  TYR B 735     -29.861  17.943  61.868  1.00 42.64           O  
-ANISOU10853  OH  TYR B 735     3673   6390   6140   1013    305   1022       O  
-ATOM  10854  N   VAL B 736     -24.205  12.326  59.377  1.00 75.19           N  
-ANISOU10854  N   VAL B 736     7465   9809  11295   1372    185   1751       N  
-ATOM  10855  CA  VAL B 736     -23.182  11.711  58.542  1.00 77.21           C  
-ANISOU10855  CA  VAL B 736     7680   9911  11746   1457    191   1767       C  
-ATOM  10856  C   VAL B 736     -23.539  11.804  57.065  1.00 76.24           C  
-ANISOU10856  C   VAL B 736     7683   9530  11754   1494    312   1669       C  
-ATOM  10857  O   VAL B 736     -24.702  11.671  56.684  1.00 76.11           O  
-ANISOU10857  O   VAL B 736     7789   9410  11721   1492    356   1679       O  
-ATOM  10858  CB  VAL B 736     -22.962  10.231  58.899  1.00 78.84           C  
-ANISOU10858  CB  VAL B 736     7835  10093  12028   1544     79   1999       C  
-ATOM  10859  CG1 VAL B 736     -22.402  10.097  60.305  1.00 80.29           C  
-ANISOU10859  CG1 VAL B 736     7883  10539  12085   1534    -44   2103       C  
-ATOM  10860  CG2 VAL B 736     -24.260   9.452  58.746  1.00 78.13           C  
-ANISOU10860  CG2 VAL B 736     7862   9876  11946   1550     83   2129       C  
-ATOM  10861  N   THR B 737     -22.530  12.038  56.235  1.00 78.64           N  
-ANISOU10861  N   THR B 737     7948   9748  12182   1529    366   1568       N  
-ATOM  10862  CA  THR B 737     -22.726  12.029  54.794  1.00 76.80           C  
-ANISOU10862  CA  THR B 737     7819   9286  12076   1585    477   1486       C  
-ATOM  10863  C   THR B 737     -22.255  10.699  54.221  1.00 78.76           C  
-ANISOU10863  C   THR B 737     8028   9399  12499   1710    426   1599       C  
-ATOM  10864  O   THR B 737     -21.189  10.201  54.579  1.00 78.21           O  
-ANISOU10864  O   THR B 737     7828   9401  12486   1754    346   1657       O  
-ATOM  10865  CB  THR B 737     -21.985  13.187  54.102  1.00 76.16           C  
-ANISOU10865  CB  THR B 737     7733   9186  12020   1544    589   1298       C  
-ATOM  10866  OG1 THR B 737     -22.480  14.438  54.594  1.00 77.41           O  
-ANISOU10866  OG1 THR B 737     7944   9441  12029   1433    631   1184       O  
-ATOM  10867  CG2 THR B 737     -22.199  13.127  52.600  1.00 75.00           C  
-ANISOU10867  CG2 THR B 737     7692   8817  11988   1617    704   1229       C  
-ATOM  10868  N   VAL B 738     -23.066  10.120  53.342  1.00 82.68           N  
-ANISOU10868  N   VAL B 738     8633   9703  13079   1776    467   1617       N  
-ATOM  10869  CA  VAL B 738     -22.744   8.842  52.721  1.00 85.18           C  
-ANISOU10869  CA  VAL B 738     8926   9867  13573   1903    416   1706       C  
-ATOM  10870  C   VAL B 738     -23.252   8.795  51.286  1.00 85.35           C  
-ANISOU10870  C   VAL B 738     9054   9682  13694   1976    521   1603       C  
-ATOM  10871  O   VAL B 738     -24.459   8.720  51.047  1.00 84.93           O  
-ANISOU10871  O   VAL B 738     9114   9545  13612   1968    554   1601       O  
-ATOM  10872  CB  VAL B 738     -23.351   7.664  53.503  1.00 87.10           C  
-ANISOU10872  CB  VAL B 738     9172  10097  13826   1921    296   1910       C  
-ATOM  10873  CG1 VAL B 738     -23.182   6.365  52.726  1.00 90.24           C  
-ANISOU10873  CG1 VAL B 738     9571  10290  14427   2055    249   1981       C  
-ATOM  10874  CG2 VAL B 738     -22.717   7.559  54.877  1.00 88.02           C  
-ANISOU10874  CG2 VAL B 738     9172  10423  13849   1881    182   2030       C  
-ATOM  10875  N   SER B 739     -22.320   8.838  50.338  1.00 80.44           N  
-ANISOU10875  N   SER B 739     8385   8996  13182   2052    572   1513       N  
-ATOM  10876  CA  SER B 739     -22.652   8.814  48.918  1.00 78.62           C  
-ANISOU10876  CA  SER B 739     8239   8593  13040   2141    673   1407       C  
-ATOM  10877  C   SER B 739     -23.368  10.096  48.508  1.00 77.01           C  
-ANISOU10877  C   SER B 739     8159   8390  12713   2069    808   1272       C  
-ATOM  10878  O   SER B 739     -24.422  10.056  47.876  1.00 73.51           O  
-ANISOU10878  O   SER B 739     7834   7834  12262   2107    861   1230       O  
-ATOM  10879  CB  SER B 739     -23.511   7.591  48.575  1.00 76.42           C  
-ANISOU10879  CB  SER B 739     8017   8152  12867   2233    614   1488       C  
-ATOM  10880  OG  SER B 739     -22.871   6.384  48.957  1.00 74.37           O  
-ANISOU10880  OG  SER B 739     7659   7868  12730   2307    481   1621       O  
-ATOM  10881  N   GLY B 740     -22.793  11.233  48.882  1.00 91.75           N  
-ANISOU10881  N   GLY B 740     9995  10380  14485   1968    860   1199       N  
-ATOM  10882  CA  GLY B 740     -23.348  12.521  48.509  1.00 89.28           C  
-ANISOU10882  CA  GLY B 740     9802  10057  14062   1901    984   1069       C  
-ATOM  10883  C   GLY B 740     -24.450  13.008  49.432  1.00 84.81           C  
-ANISOU10883  C   GLY B 740     9315   9570  13340   1809    956   1081       C  
-ATOM  10884  O   GLY B 740     -24.585  14.211  49.660  1.00 82.59           O  
-ANISOU10884  O   GLY B 740     9086   9351  12945   1720   1017    983       O  
-ATOM  10885  N   GLN B 741     -25.246  12.080  49.958  1.00 76.03           N  
-ANISOU10885  N   GLN B 741     8209   8456  12224   1829    864   1196       N  
-ATOM  10886  CA  GLN B 741     -26.328  12.441  50.867  1.00 72.46           C  
-ANISOU10886  CA  GLN B 741     7813   8103  11614   1745    833   1214       C  
-ATOM  10887  C   GLN B 741     -25.794  12.873  52.224  1.00 72.90           C  
-ANISOU10887  C   GLN B 741     7767   8369  11564   1639    757   1257       C  
-ATOM  10888  O   GLN B 741     -25.085  12.121  52.888  1.00 75.21           O  
-ANISOU10888  O   GLN B 741     7938   8735  11902   1646    657   1380       O  
-ATOM  10889  CB  GLN B 741     -27.308  11.282  51.039  1.00 73.49           C  
-ANISOU10889  CB  GLN B 741     7969   8178  11777   1783    764   1335       C  
-ATOM  10890  CG  GLN B 741     -28.334  11.178  49.933  1.00 71.34           C  
-ANISOU10890  CG  GLN B 741     7823   7746  11537   1858    843   1249       C  
-ATOM  10891  CD  GLN B 741     -29.716  10.853  50.462  1.00 70.30           C  
-ANISOU10891  CD  GLN B 741     7745   7649  11318   1817    808   1297       C  
-ATOM  10892  OE1 GLN B 741     -30.609  11.702  50.460  1.00 68.89           O  
-ANISOU10892  OE1 GLN B 741     7657   7518  11001   1782    864   1190       O  
-ATOM  10893  NE2 GLN B 741     -29.901   9.618  50.914  1.00 69.26           N  
-ANISOU10893  NE2 GLN B 741     7558   7492  11267   1821    714   1457       N  
-ATOM  10894  N   GLU B 742     -26.148  14.085  52.636  1.00 69.76           N  
-ANISOU10894  N   GLU B 742     7418   8069  11019   1551    798   1147       N  
-ATOM  10895  CA  GLU B 742     -25.659  14.630  53.893  1.00 70.12           C  
-ANISOU10895  CA  GLU B 742     7363   8326  10955   1453    729   1152       C  
-ATOM  10896  C   GLU B 742     -26.751  14.635  54.955  1.00 70.14           C  
-ANISOU10896  C   GLU B 742     7384   8474  10791   1399    663   1205       C  
-ATOM  10897  O   GLU B 742     -27.916  14.350  54.671  1.00 70.92           O  
-ANISOU10897  O   GLU B 742     7583   8507  10858   1424    683   1218       O  
-ATOM  10898  CB  GLU B 742     -25.153  16.053  53.678  1.00 67.28           C  
-ANISOU10898  CB  GLU B 742     7026   7983  10555   1385    815    977       C  
-ATOM  10899  CG  GLU B 742     -24.392  16.236  52.389  1.00 63.61           C  
-ANISOU10899  CG  GLU B 742     6586   7353  10230   1433    922    904       C  
-ATOM  10900  CD  GLU B 742     -24.475  17.656  51.869  1.00 59.49           C  
-ANISOU10900  CD  GLU B 742     6173   6773   9659   1376   1041    736       C  
-ATOM  10901  OE1 GLU B 742     -25.198  17.875  50.872  1.00 55.84           O  
-ANISOU10901  OE1 GLU B 742     5858   6158   9201   1436   1134    681       O  
-ATOM  10902  OE2 GLU B 742     -23.818  18.548  52.452  1.00 58.00           O  
-ANISOU10902  OE2 GLU B 742     5921   6686   9430   1276   1039    657       O  
-ATOM  10903  N   PHE B 743     -26.360  14.955  56.183  1.00 66.85           N  
-ANISOU10903  N   PHE B 743     6861   8273  10265   1327    582   1227       N  
-ATOM  10904  CA  PHE B 743     -27.318  15.192  57.251  1.00 65.67           C  
-ANISOU10904  CA  PHE B 743     6717   8306   9928   1268    526   1248       C  
-ATOM  10905  C   PHE B 743     -28.142  13.955  57.559  1.00 67.22           C  
-ANISOU10905  C   PHE B 743     6918   8502  10119   1297    466   1436       C  
-ATOM  10906  O   PHE B 743     -29.339  14.044  57.822  1.00 64.86           O  
-ANISOU10906  O   PHE B 743     6684   8257   9702   1269    472   1432       O  
-ATOM  10907  CB  PHE B 743     -28.243  16.346  56.867  1.00 59.03           C  
-ANISOU10907  CB  PHE B 743     6011   7432   8985   1240    610   1067       C  
-ATOM  10908  CG  PHE B 743     -27.515  17.607  56.500  1.00 51.27           C  
-ANISOU10908  CG  PHE B 743     5048   6415   8019   1202    679    885       C  
-ATOM  10909  CD1 PHE B 743     -26.446  18.052  57.262  1.00 48.52           C  
-ANISOU10909  CD1 PHE B 743     4567   6213   7656   1140    628    854       C  
-ATOM  10910  CD2 PHE B 743     -27.887  18.338  55.383  1.00 47.12           C  
-ANISOU10910  CD2 PHE B 743     4670   5707   7525   1228    796    748       C  
-ATOM  10911  CE1 PHE B 743     -25.773  19.207  56.924  1.00 46.18           C  
-ANISOU10911  CE1 PHE B 743     4284   5872   7389   1088    695    686       C  
-ATOM  10912  CE2 PHE B 743     -27.214  19.491  55.039  1.00 44.88           C  
-ANISOU10912  CE2 PHE B 743     4414   5374   7265   1183    865    598       C  
-ATOM  10913  CZ  PHE B 743     -26.155  19.925  55.809  1.00 45.47           C  
-ANISOU10913  CZ  PHE B 743     4354   5585   7339   1104    816    567       C  
-ATOM  10914  N   MET B 744     -27.498  12.798  57.519  1.00 71.03           N  
-ANISOU10914  N   MET B 744     7331   8924  10735   1351    409   1597       N  
-ATOM  10915  CA  MET B 744     -28.183  11.552  57.814  1.00 74.31           C  
-ANISOU10915  CA  MET B 744     7751   9312  11172   1372    349   1794       C  
-ATOM  10916  C   MET B 744     -27.925  11.109  59.244  1.00 78.27           C  
-ANISOU10916  C   MET B 744     8135  10042  11563   1335    231   1965       C  
-ATOM  10917  O   MET B 744     -26.796  11.176  59.735  1.00 78.99           O  
-ANISOU10917  O   MET B 744     8115  10237  11659   1347    172   1984       O  
-ATOM  10918  CB  MET B 744     -27.752  10.452  56.846  1.00 74.64           C  
-ANISOU10918  CB  MET B 744     7805   9118  11438   1469    351   1874       C  
-ATOM  10919  CG  MET B 744     -28.434  10.504  55.501  1.00 72.89           C  
-ANISOU10919  CG  MET B 744     7709   8675  11311   1520    454   1758       C  
-ATOM  10920  SD  MET B 744     -27.988   9.065  54.514  1.00 72.58           S  
-ANISOU10920  SD  MET B 744     7664   8383  11530   1643    430   1859       S  
-ATOM  10921  CE  MET B 744     -26.204   9.189  54.570  1.00 72.63           C  
-ANISOU10921  CE  MET B 744     7543   8439  11614   1686    392   1849       C  
-ATOM  10922  N   ILE B 745     -28.985  10.654  59.903  1.00 71.26           N  
-ANISOU10922  N   ILE B 745     7267   9242  10567   1291    199   2088       N  
-ATOM  10923  CA  ILE B 745     -28.887  10.109  61.247  1.00 77.79           C  
-ANISOU10923  CA  ILE B 745     7994  10286  11277   1261     92   2284       C  
-ATOM  10924  C   ILE B 745     -28.725   8.599  61.150  1.00 84.30           C  
-ANISOU10924  C   ILE B 745     8813  10960  12257   1316     32   2521       C  
-ATOM  10925  O   ILE B 745     -29.581   7.913  60.595  1.00 86.41           O  
-ANISOU10925  O   ILE B 745     9163  11055  12612   1316     66   2582       O  
-ATOM  10926  CB  ILE B 745     -30.141  10.436  62.068  1.00 73.99           C  
-ANISOU10926  CB  ILE B 745     7530  10004  10580   1175     93   2300       C  
-ATOM  10927  CG1 ILE B 745     -30.405  11.943  62.067  1.00 70.91           C  
-ANISOU10927  CG1 ILE B 745     7164   9731  10047   1134    149   2044       C  
-ATOM  10928  CG2 ILE B 745     -29.989   9.932  63.490  1.00 74.66           C  
-ANISOU10928  CG2 ILE B 745     7504  10341  10521   1148    -13   2508       C  
-ATOM  10929  CD1 ILE B 745     -29.349  12.741  62.795  1.00 68.35           C  
-ANISOU10929  CD1 ILE B 745     6729   9602   9640   1124     96   1960       C  
-ATOM  10930  N   GLU B 746     -27.622   8.086  61.686  1.00 97.55           N  
-ANISOU10930  N   GLU B 746    10392  12700  13974   1369    -60   2646       N  
-ATOM  10931  CA  GLU B 746     -27.283   6.673  61.539  1.00106.86           C  
-ANISOU10931  CA  GLU B 746    11568  13712  15321   1443   -128   2859       C  
-ATOM  10932  C   GLU B 746     -27.554   5.873  62.817  1.00114.43           C  
-ANISOU10932  C   GLU B 746    12480  14831  16166   1416   -226   3129       C  
-ATOM  10933  O   GLU B 746     -27.209   6.307  63.918  1.00113.67           O  
-ANISOU10933  O   GLU B 746    12292  15012  15886   1394   -283   3162       O  
-ATOM  10934  CB  GLU B 746     -25.816   6.532  61.126  1.00106.92           C  
-ANISOU10934  CB  GLU B 746    11503  13651  15472   1546   -168   2816       C  
-ATOM  10935  CG  GLU B 746     -25.473   5.206  60.466  1.00109.32           C  
-ANISOU10935  CG  GLU B 746    11832  13698  16005   1650   -214   2951       C  
-ATOM  10936  CD  GLU B 746     -24.048   5.169  59.938  1.00109.86           C  
-ANISOU10936  CD  GLU B 746    11822  13711  16207   1758   -243   2868       C  
-ATOM  10937  OE1 GLU B 746     -23.126   5.583  60.674  1.00109.58           O  
-ANISOU10937  OE1 GLU B 746    11673  13886  16078   1768   -300   2851       O  
-ATOM  10938  OE2 GLU B 746     -23.851   4.732  58.784  1.00109.08           O  
-ANISOU10938  OE2 GLU B 746    11767  13374  16305   1836   -210   2807       O  
-ATOM  10939  N   ILE B 747     -28.177   4.706  62.662  1.00127.16           N  
-ANISOU10939  N   ILE B 747    14157  16270  17888   1418   -244   3322       N  
-ATOM  10940  CA  ILE B 747     -28.488   3.839  63.798  1.00136.78           C  
-ANISOU10940  CA  ILE B 747    15349  17605  19016   1387   -326   3610       C  
-ATOM  10941  C   ILE B 747     -28.520   2.364  63.401  1.00146.22           C  
-ANISOU10941  C   ILE B 747    16602  18519  20435   1440   -374   3823       C  
-ATOM  10942  O   ILE B 747     -28.866   2.025  62.270  1.00145.43           O  
-ANISOU10942  O   ILE B 747    16582  18147  20529   1461   -320   3740       O  
-ATOM  10943  CB  ILE B 747     -29.836   4.219  64.458  1.00137.34           C  
-ANISOU10943  CB  ILE B 747    15443  17862  18879   1254   -277   3638       C  
-ATOM  10944  CG1 ILE B 747     -30.945   4.332  63.408  1.00132.59           C  
-ANISOU10944  CG1 ILE B 747    14947  17062  18368   1203   -168   3499       C  
-ATOM  10945  CG2 ILE B 747     -29.709   5.519  65.234  1.00133.43           C  
-ANISOU10945  CG2 ILE B 747    14867  17697  18132   1214   -272   3485       C  
-ATOM  10946  CD1 ILE B 747     -31.568   3.008  63.021  1.00134.51           C  
-ANISOU10946  CD1 ILE B 747    15261  17054  18793   1191   -174   3686       C  
-ATOM  10947  N   LYS B 748     -28.165   1.494  64.343  1.00111.50           N  
-ANISOU10947  N   LYS B 748    12168  14190  16008   1469   -479   4095       N  
-ATOM  10948  CA  LYS B 748     -28.139   0.053  64.101  1.00126.16           C  
-ANISOU10948  CA  LYS B 748    14082  15776  18076   1523   -541   4321       C  
-ATOM  10949  C   LYS B 748     -29.523  -0.489  63.760  1.00131.89           C  
-ANISOU10949  C   LYS B 748    14905  16334  18873   1413   -474   4394       C  
-ATOM  10950  O   LYS B 748     -30.532   0.003  64.264  1.00132.84           O  
-ANISOU10950  O   LYS B 748    15029  16635  18810   1285   -412   4391       O  
-ATOM  10951  CB  LYS B 748     -27.585  -0.678  65.324  1.00128.09           C  
-ANISOU10951  CB  LYS B 748    14275  16159  18233   1567   -665   4617       C  
-ATOM  10952  CG  LYS B 748     -26.219  -0.191  65.775  1.00131.11           C  
-ANISOU10952  CG  LYS B 748    14544  16741  18530   1680   -743   4549       C  
-ATOM  10953  CD  LYS B 748     -25.167  -0.417  64.701  1.00132.72           C  
-ANISOU10953  CD  LYS B 748    14741  16716  18972   1820   -769   4406       C  
-ATOM  10954  CE  LYS B 748     -23.791   0.017  65.181  1.00135.96           C  
-ANISOU10954  CE  LYS B 748    15023  17337  19299   1927   -849   4339       C  
-ATOM  10955  NZ  LYS B 748     -22.738  -0.247  64.166  1.00139.19           N  
-ANISOU10955  NZ  LYS B 748    15410  17546  19931   2065   -876   4205       N  
-ATOM  10956  N   ASN B 749     -29.563  -1.510  62.908  1.00179.08           N  
-ANISOU10956  N   ASN B 749    20953  21973  25118   1466   -491   4447       N  
-ATOM  10957  CA  ASN B 749     -30.827  -2.101  62.473  1.00183.53           C  
-ANISOU10957  CA  ASN B 749    21601  22345  25787   1366   -430   4494       C  
-ATOM  10958  C   ASN B 749     -31.628  -2.717  63.612  1.00185.74           C  
-ANISOU10958  C   ASN B 749    21889  22736  25946   1239   -451   4792       C  
-ATOM  10959  O   ASN B 749     -32.791  -3.078  63.438  1.00183.91           O  
-ANISOU10959  O   ASN B 749    21710  22413  25756   1121   -389   4833       O  
-ATOM  10960  CB  ASN B 749     -30.585  -3.158  61.396  1.00193.52           C  
-ANISOU10960  CB  ASN B 749    22928  23223  27378   1462   -465   4497       C  
-ATOM  10961  CG  ASN B 749     -30.032  -2.571  60.119  1.00195.17           C  
-ANISOU10961  CG  ASN B 749    23134  23316  27706   1572   -420   4190       C  
-ATOM  10962  OD1 ASN B 749     -30.253  -1.399  59.814  1.00199.93           O  
-ANISOU10962  OD1 ASN B 749    23724  24064  28177   1538   -328   3960       O  
-ATOM  10963  ND2 ASN B 749     -29.312  -3.385  59.360  1.00201.78           N  
-ANISOU10963  ND2 ASN B 749    23986  23890  28792   1708   -485   4188       N  
-ATOM  10964  N   SER B 750     -30.998  -2.838  64.775  1.00194.75           N  
-ANISOU10964  N   SER B 750    22973  24087  26935   1266   -536   4999       N  
-ATOM  10965  CA  SER B 750     -31.635  -3.464  65.927  1.00196.00           C  
-ANISOU10965  CA  SER B 750    23136  24370  26964   1159   -560   5317       C  
-ATOM  10966  C   SER B 750     -32.218  -2.430  66.887  1.00193.69           C  
-ANISOU10966  C   SER B 750    22774  24487  26334   1049   -506   5279       C  
-ATOM  10967  O   SER B 750     -32.896  -2.783  67.852  1.00199.15           O  
-ANISOU10967  O   SER B 750    23456  25337  26874    941   -504   5517       O  
-ATOM  10968  CB  SER B 750     -30.635  -4.360  66.657  1.00204.16           C  
-ANISOU10968  CB  SER B 750    24158  25382  28031   1270   -696   5601       C  
-ATOM  10969  OG  SER B 750     -29.458  -3.643  66.983  1.00209.22           O  
-ANISOU10969  OG  SER B 750    24709  26237  28549   1394   -755   5490       O  
-ATOM  10970  N   ALA B 751     -31.951  -1.156  66.618  1.00139.02           N  
-ANISOU10970  N   ALA B 751    15798  17732  19293   1076   -463   4981       N  
-ATOM  10971  CA  ALA B 751     -32.466  -0.074  67.451  1.00138.46           C  
-ANISOU10971  CA  ALA B 751    15656  18042  18909    989   -419   4895       C  
-ATOM  10972  C   ALA B 751     -33.432   0.820  66.673  1.00131.08           C  
-ANISOU10972  C   ALA B 751    14754  17099  17950    910   -300   4605       C  
-ATOM  10973  O   ALA B 751     -33.829   1.882  67.152  1.00129.37           O  
-ANISOU10973  O   ALA B 751    14486  17172  17495    857   -261   4460       O  
-ATOM  10974  CB  ALA B 751     -31.319   0.749  68.023  1.00139.08           C  
-ANISOU10974  CB  ALA B 751    15635  18374  18834   1087   -483   4799       C  
-ATOM  10975  N   VAL B 752     -33.812   0.375  65.479  1.00169.48           N  
-ANISOU10975  N   VAL B 752    19703  21634  23058    915   -249   4515       N  
-ATOM  10976  CA  VAL B 752     -34.675   1.156  64.595  1.00160.35           C  
-ANISOU10976  CA  VAL B 752    18588  20436  21901    869   -141   4230       C  
-ATOM  10977  C   VAL B 752     -36.023   1.495  65.234  1.00157.38           C  
-ANISOU10977  C   VAL B 752    18196  20297  21306    719    -77   4245       C  
-ATOM  10978  O   VAL B 752     -36.712   2.416  64.797  1.00153.18           O  
-ANISOU10978  O   VAL B 752    17677  19840  20684    688      2   3994       O  
-ATOM  10979  CB  VAL B 752     -34.910   0.429  63.251  1.00161.81           C  
-ANISOU10979  CB  VAL B 752    18860  20230  22390    906   -107   4161       C  
-ATOM  10980  CG1 VAL B 752     -35.672   1.324  62.283  1.00155.85           C  
-ANISOU10980  CG1 VAL B 752    18148  19446  21623    891      0   3846       C  
-ATOM  10981  CG2 VAL B 752     -33.588  -0.003  62.643  1.00158.06           C  
-ANISOU10981  CG2 VAL B 752    18392  19532  22131   1059   -177   4157       C  
-ATOM  10982  N   SER B 753     -36.395   0.752  66.271  1.00134.11           N  
-ANISOU10982  N   SER B 753    15218  17474  18265    632   -110   4542       N  
-ATOM  10983  CA  SER B 753     -37.646   1.007  66.978  1.00133.44           C  
-ANISOU10983  CA  SER B 753    15099  17649  17955    484    -51   4580       C  
-ATOM  10984  C   SER B 753     -37.596   2.343  67.714  1.00130.08           C  
-ANISOU10984  C   SER B 753    14592  17614  17220    489    -49   4415       C  
-ATOM  10985  O   SER B 753     -38.626   2.884  68.116  1.00131.62           O  
-ANISOU10985  O   SER B 753    14752  18047  17209    392      7   4340       O  
-ATOM  10986  CB  SER B 753     -37.944  -0.126  67.963  1.00137.01           C  
-ANISOU10986  CB  SER B 753    15534  18152  18373    391    -88   4966       C  
-ATOM  10987  OG  SER B 753     -36.870  -0.309  68.869  1.00139.61           O  
-ANISOU10987  OG  SER B 753    15815  18616  18616    471   -188   5163       O  
-ATOM  10988  N   CYS B 754     -36.389   2.870  67.877  1.00146.06           N  
-ANISOU10988  N   CYS B 754    16577  19702  19217    605   -114   4344       N  
-ATOM  10989  CA  CYS B 754     -36.179   4.104  68.621  1.00139.14           C  
-ANISOU10989  CA  CYS B 754    15615  19183  18070    619   -130   4188       C  
-ATOM  10990  C   CYS B 754     -36.527   5.342  67.789  1.00129.74           C  
-ANISOU10990  C   CYS B 754    14458  17979  16858    634    -56   3815       C  
-ATOM  10991  O   CYS B 754     -36.887   6.385  68.336  1.00127.18           O  
-ANISOU10991  O   CYS B 754    14080  17945  16296    607    -45   3657       O  
-ATOM  10992  CB  CYS B 754     -34.729   4.173  69.113  1.00142.62           C  
-ANISOU10992  CB  CYS B 754    15993  19696  18502    733   -229   4246       C  
-ATOM  10993  SG  CYS B 754     -34.424   5.364  70.438  1.00145.69           S  
-ANISOU10993  SG  CYS B 754    16244  20578  18535    742   -281   4152       S  
-ATOM  10994  N   ILE B 755     -36.429   5.220  66.467  1.00109.49           N  
-ANISOU10994  N   ILE B 755    11985  15077  14539    683    -10   3675       N  
-ATOM  10995  CA  ILE B 755     -36.692   6.347  65.571  1.00 96.53           C  
-ANISOU10995  CA  ILE B 755    10394  13386  12897    714     62   3336       C  
-ATOM  10996  C   ILE B 755     -38.181   6.514  65.262  1.00 91.42           C  
-ANISOU10996  C   ILE B 755     9790  12767  12180    630    146   3231       C  
-ATOM  10997  O   ILE B 755     -38.874   5.538  64.964  1.00 88.47           O  
-ANISOU10997  O   ILE B 755     9450  12238  11925    572    173   3364       O  
-ATOM  10998  CB  ILE B 755     -35.872   6.252  64.253  1.00 94.08           C  
-ANISOU10998  CB  ILE B 755    10156  12731  12858    821     79   3212       C  
-ATOM  10999  CG1 ILE B 755     -36.330   5.068  63.397  1.00 93.65           C  
-ANISOU10999  CG1 ILE B 755    10175  12360  13048    816    106   3316       C  
-ATOM  11000  CG2 ILE B 755     -34.381   6.159  64.552  1.00 92.93           C  
-ANISOU11000  CG2 ILE B 755     9954  12585  12772    907     -3   3287       C  
-ATOM  11001  CD1 ILE B 755     -37.321   5.436  62.305  1.00 93.50           C  
-ANISOU11001  CD1 ILE B 755    10238  12202  13084    809    204   3087       C  
-ATOM  11002  N   PRO B 756     -38.672   7.761  65.337  1.00 80.31           N  
-ANISOU11002  N   PRO B 756     8376  11557  10581    624    182   2982       N  
-ATOM  11003  CA  PRO B 756     -40.076   8.124  65.112  1.00 76.90           C  
-ANISOU11003  CA  PRO B 756     7973  11206  10039    562    254   2837       C  
-ATOM  11004  C   PRO B 756     -40.649   7.532  63.827  1.00 73.83           C  
-ANISOU11004  C   PRO B 756     7680  10494   9878    574    322   2776       C  
-ATOM  11005  O   PRO B 756     -39.908   6.995  63.005  1.00 72.11           O  
-ANISOU11005  O   PRO B 756     7514   9980   9905    644    317   2806       O  
-ATOM  11006  CB  PRO B 756     -40.023   9.647  65.015  1.00 75.65           C  
-ANISOU11006  CB  PRO B 756     7826  11189   9727    617    268   2531       C  
-ATOM  11007  CG  PRO B 756     -38.871  10.021  65.870  1.00 77.46           C  
-ANISOU11007  CG  PRO B 756     7976  11581   9874    649    189   2587       C  
-ATOM  11008  CD  PRO B 756     -37.851   8.938  65.674  1.00 79.03           C  
-ANISOU11008  CD  PRO B 756     8174  11557  10295    685    147   2812       C  
-ATOM  11009  N   THR B 757     -41.962   7.636  63.661  1.00 82.27           N  
-ANISOU11009  N   THR B 757     8761  11635  10861    511    383   2678       N  
-ATOM  11010  CA  THR B 757     -42.633   7.038  62.516  1.00 79.79           C  
-ANISOU11010  CA  THR B 757     8521  11049  10746    516    445   2612       C  
-ATOM  11011  C   THR B 757     -42.441   7.873  61.259  1.00 76.84           C  
-ANISOU11011  C   THR B 757     8244  10492  10460    643    491   2316       C  
-ATOM  11012  O   THR B 757     -42.162   7.337  60.188  1.00 74.17           O  
-ANISOU11012  O   THR B 757     7970   9850  10361    709    513   2291       O  
-ATOM  11013  CB  THR B 757     -44.141   6.873  62.771  1.00 79.92           C  
-ANISOU11013  CB  THR B 757     8505  11228  10633    404    496   2591       C  
-ATOM  11014  OG1 THR B 757     -44.781   8.156  62.752  1.00 80.70           O  
-ANISOU11014  OG1 THR B 757     8612  11539  10513    437    528   2312       O  
-ATOM  11015  CG2 THR B 757     -44.380   6.207  64.116  1.00 79.34           C  
-ANISOU11015  CG2 THR B 757     8330  11391  10423    269    460   2883       C  
-ATOM  11016  N   ASP B 758     -42.589   9.188  61.395  1.00 88.16           N  
-ANISOU11016  N   ASP B 758     9689  12111  11697    681    505   2093       N  
-ATOM  11017  CA  ASP B 758     -42.526  10.085  60.243  1.00 82.70           C  
-ANISOU11017  CA  ASP B 758     9101  11265  11058    798    557   1813       C  
-ATOM  11018  C   ASP B 758     -41.135  10.173  59.610  1.00 80.27           C  
-ANISOU11018  C   ASP B 758     8836  10731  10933    894    544   1809       C  
-ATOM  11019  O   ASP B 758     -41.009  10.531  58.440  1.00 78.04           O  
-ANISOU11019  O   ASP B 758     8645  10243  10765    991    596   1635       O  
-ATOM  11020  CB  ASP B 758     -43.071  11.482  60.587  1.00 85.60           C  
-ANISOU11020  CB  ASP B 758     9477  11879  11168    815    569   1578       C  
-ATOM  11021  CG  ASP B 758     -42.445  12.072  61.839  1.00 87.29           C  
-ANISOU11021  CG  ASP B 758     9607  12360  11201    778    500   1637       C  
-ATOM  11022  OD1 ASP B 758     -41.396  11.561  62.284  1.00 90.07           O  
-ANISOU11022  OD1 ASP B 758     9907  12680  11637    765    448   1829       O  
-ATOM  11023  OD2 ASP B 758     -42.999  13.057  62.373  1.00 90.95           O  
-ANISOU11023  OD2 ASP B 758    10052  13071  11435    773    493   1478       O  
-ATOM  11024  N   TRP B 759     -40.096   9.841  60.372  1.00 69.07           N  
-ANISOU11024  N   TRP B 759     7346   9362   9535    872    476   1998       N  
-ATOM  11025  CA  TRP B 759     -38.744   9.869  59.825  1.00 66.68           C  
-ANISOU11025  CA  TRP B 759     7065   8869   9403    958    460   1997       C  
-ATOM  11026  C   TRP B 759     -38.654   8.984  58.599  1.00 66.40           C  
-ANISOU11026  C   TRP B 759     7092   8506   9631   1023    494   2013       C  
-ATOM  11027  O   TRP B 759     -39.094   7.839  58.618  1.00 66.74           O  
-ANISOU11027  O   TRP B 759     7119   8460   9781    980    479   2174       O  
-ATOM  11028  CB  TRP B 759     -37.711   9.408  60.848  1.00 64.39           C  
-ANISOU11028  CB  TRP B 759     6676   8684   9106    929    372   2220       C  
-ATOM  11029  CG  TRP B 759     -37.388  10.419  61.885  1.00 62.01           C  
-ANISOU11029  CG  TRP B 759     6306   8675   8579    902    331   2163       C  
-ATOM  11030  CD1 TRP B 759     -38.191  11.428  62.329  1.00 60.97           C  
-ANISOU11030  CD1 TRP B 759     6173   8772   8220    868    349   1999       C  
-ATOM  11031  CD2 TRP B 759     -36.162  10.529  62.612  1.00 61.61           C  
-ANISOU11031  CD2 TRP B 759     6172   8729   8508    917    258   2250       C  
-ATOM  11032  NE1 TRP B 759     -37.543  12.154  63.300  1.00 60.22           N  
-ANISOU11032  NE1 TRP B 759     5997   8913   7970    857    290   1978       N  
-ATOM  11033  CE2 TRP B 759     -36.296  11.623  63.490  1.00 61.28           C  
-ANISOU11033  CE2 TRP B 759     6077   8980   8226    885    235   2129       C  
-ATOM  11034  CE3 TRP B 759     -34.965   9.807  62.608  1.00 59.42           C  
-ANISOU11034  CE3 TRP B 759     5853   8334   8390    962    203   2406       C  
-ATOM  11035  CZ2 TRP B 759     -35.278  12.014  64.355  1.00 62.02           C  
-ANISOU11035  CZ2 TRP B 759     6073   9253   8238    891    162   2155       C  
-ATOM  11036  CZ3 TRP B 759     -33.956  10.194  63.471  1.00 60.96           C  
-ANISOU11036  CZ3 TRP B 759     5952   8714   8497    971    132   2436       C  
-ATOM  11037  CH2 TRP B 759     -34.119  11.289  64.332  1.00 61.94           C  
-ANISOU11037  CH2 TRP B 759     6019   9130   8384    934    113   2309       C  
-ATOM  11038  N   VAL B 760     -38.077   9.528  57.536  1.00 76.69           N  
-ANISOU11038  N   VAL B 760     8465   9634  11040   1126    539   1842       N  
-ATOM  11039  CA  VAL B 760     -37.899   8.799  56.288  1.00 77.09           C  
-ANISOU11039  CA  VAL B 760     8570   9388  11333   1212    571   1824       C  
-ATOM  11040  C   VAL B 760     -36.580   8.039  56.271  1.00 82.50           C  
-ANISOU11040  C   VAL B 760     9206   9939  12200   1254    512   1984       C  
-ATOM  11041  O   VAL B 760     -35.524   8.607  56.551  1.00 79.19           O  
-ANISOU11041  O   VAL B 760     8753   9585  11752   1276    489   1972       O  
-ATOM  11042  CB  VAL B 760     -37.930   9.758  55.081  1.00 74.26           C  
-ANISOU11042  CB  VAL B 760     8312   8915  10989   1315    656   1563       C  
-ATOM  11043  CG1 VAL B 760     -37.210   9.145  53.898  1.00 72.17           C  
-ANISOU11043  CG1 VAL B 760     8078   8376  10968   1424    676   1554       C  
-ATOM  11044  CG2 VAL B 760     -39.361  10.120  54.726  1.00 69.88           C  
-ANISOU11044  CG2 VAL B 760     7821   8407  10325   1313    714   1403       C  
-ATOM  11045  N   LYS B 761     -36.641   6.753  55.942  1.00 95.16           N  
-ANISOU11045  N   LYS B 761    10802  11357  13997   1268    483   2124       N  
-ATOM  11046  CA  LYS B 761     -35.427   5.963  55.791  1.00104.64           C  
-ANISOU11046  CA  LYS B 761    11964  12406  15388   1333    421   2258       C  
-ATOM  11047  C   LYS B 761     -34.767   6.241  54.441  1.00108.60           C  
-ANISOU11047  C   LYS B 761    12514  12710  16039   1464    472   2082       C  
-ATOM  11048  O   LYS B 761     -35.257   5.809  53.396  1.00107.82           O  
-ANISOU11048  O   LYS B 761    12469  12421  16076   1527    513   1995       O  
-ATOM  11049  CB  LYS B 761     -35.726   4.471  55.938  1.00107.34           C  
-ANISOU11049  CB  LYS B 761    12287  12604  15892   1305    362   2472       C  
-ATOM  11050  CG  LYS B 761     -34.484   3.592  55.919  1.00113.25           C  
-ANISOU11050  CG  LYS B 761    12994  13209  16828   1381    278   2626       C  
-ATOM  11051  CD  LYS B 761     -34.567   2.537  54.826  1.00117.96           C  
-ANISOU11051  CD  LYS B 761    13627  13501  17692   1464    273   2617       C  
-ATOM  11052  CE  LYS B 761     -35.760   1.618  55.034  1.00122.30           C  
-ANISOU11052  CE  LYS B 761    14195  13979  18296   1370    267   2732       C  
-ATOM  11053  NZ  LYS B 761     -35.870   0.607  53.947  1.00125.37           N  
-ANISOU11053  NZ  LYS B 761    14615  14064  18957   1452    257   2697       N  
-ATOM  11054  N   VAL B 762     -33.656   6.969  54.471  1.00 96.55           N  
-ANISOU11054  N   VAL B 762    12409  10791  13483    155   2804    438       N  
-ATOM  11055  CA  VAL B 762     -32.935   7.313  53.252  1.00100.60           C  
-ANISOU11055  CA  VAL B 762    12804  11366  14053    162   2704    402       C  
-ATOM  11056  C   VAL B 762     -31.758   6.369  53.021  1.00106.41           C  
-ANISOU11056  C   VAL B 762    13593  11903  14936    149   2744    455       C  
-ATOM  11057  O   VAL B 762     -31.219   6.294  51.917  1.00106.73           O  
-ANISOU11057  O   VAL B 762    13529  11971  15051    113   2717    398       O  
-ATOM  11058  CB  VAL B 762     -32.425   8.765  53.287  1.00 99.03           C  
-ANISOU11058  CB  VAL B 762    12608  11248  13772    307   2476    482       C  
-ATOM  11059  CG1 VAL B 762     -33.592   9.733  53.371  1.00 96.77           C  
-ANISOU11059  CG1 VAL B 762    12257  11165  13345    328   2444    425       C  
-ATOM  11060  CG2 VAL B 762     -31.475   8.967  54.454  1.00 97.08           C  
-ANISOU11060  CG2 VAL B 762    12536  10831  13518    430   2376    654       C  
-ATOM  11061  N   GLY B 763     -31.365   5.649  54.066  1.00125.71           N  
-ANISOU11061  N   GLY B 763    16199  14148  17416    184   2811    567       N  
-ATOM  11062  CA  GLY B 763     -30.257   4.717  53.975  1.00133.73           C  
-ANISOU11062  CA  GLY B 763    17280  14966  18566    193   2859    636       C  
-ATOM  11063  C   GLY B 763     -30.576   3.385  54.619  1.00139.79           C  
-ANISOU11063  C   GLY B 763    18160  15560  19392    125   3085    650       C  
-ATOM  11064  O   GLY B 763     -31.206   3.331  55.675  1.00140.14           O  
-ANISOU11064  O   GLY B 763    18310  15575  19360    142   3140    696       O  
-ATOM  11065  N   SER B 764     -30.143   2.305  53.979  1.00149.04           N  
-ANISOU11065  N   SER B 764    19317  16612  20701     45   3227    609       N  
-ATOM  11066  CA  SER B 764     -30.372   0.965  54.503  1.00154.05           C  
-ANISOU11066  CA  SER B 764    20070  17057  21405    -22   3468    621       C  
-ATOM  11067  C   SER B 764     -29.213   0.027  54.187  1.00157.09           C  
-ANISOU11067  C   SER B 764    20506  17241  21941      1   3535    688       C  
-ATOM  11068  O   SER B 764     -28.855  -0.178  53.027  1.00158.01           O  
-ANISOU11068  O   SER B 764    20503  17385  22149    -73   3551    595       O  
-ATOM  11069  CB  SER B 764     -31.683   0.389  53.964  1.00157.29           C  
-ANISOU11069  CB  SER B 764    20387  17560  21815   -222   3686    424       C  
-ATOM  11070  OG  SER B 764     -31.677   0.351  52.549  1.00159.35           O  
-ANISOU11070  OG  SER B 764    20468  17938  22140   -333   3701    274       O  
-ATOM  11071  N   THR B 765     -28.628  -0.530  55.240  1.00129.72           N  
-ANISOU11071  N   THR B 765    17219  13576  18493    111   3575    854       N  
-ATOM  11072  CA  THR B 765     -27.556  -1.506  55.122  1.00134.27           C  
-ANISOU11072  CA  THR B 765    17868  13942  19205    157   3659    941       C  
-ATOM  11073  C   THR B 765     -27.919  -2.700  55.989  1.00140.10           C  
-ANISOU11073  C   THR B 765    18780  14476  19974    138   3909    999       C  
-ATOM  11074  O   THR B 765     -28.604  -2.546  56.998  1.00143.13           O  
-ANISOU11074  O   THR B 765    19261  14867  20254    161   3933   1044       O  
-ATOM  11075  CB  THR B 765     -26.216  -0.916  55.599  1.00128.80           C  
-ANISOU11075  CB  THR B 765    17229  13213  18497    361   3427   1123       C  
-ATOM  11076  OG1 THR B 765     -25.790   0.103  54.686  1.00126.46           O  
-ANISOU11076  OG1 THR B 765    16778  13082  18190    367   3220   1060       O  
-ATOM  11077  CG2 THR B 765     -25.147  -1.995  55.683  1.00126.28           C  
-ANISOU11077  CG2 THR B 765    17005  12670  18305    435   3527   1236       C  
-ATOM  11078  N   LYS B 766     -27.470  -3.889  55.600  1.00206.25           N  
-ANISOU11078  N   LYS B 766    27204  22667  28494     94   4106    998       N  
-ATOM  11079  CA  LYS B 766     -27.771  -5.095  56.364  1.00210.52           C  
-ANISOU11079  CA  LYS B 766    27924  22990  29074     76   4373   1055       C  
-ATOM  11080  C   LYS B 766     -27.114  -5.064  57.744  1.00209.61           C  
-ANISOU11080  C   LYS B 766    27994  22752  28895    291   4288   1295       C  
-ATOM  11081  O   LYS B 766     -27.118  -6.061  58.468  1.00211.76           O  
-ANISOU11081  O   LYS B 766    28440  22820  29200    325   4490   1390       O  
-ATOM  11082  CB  LYS B 766     -27.348  -6.349  55.593  1.00218.99           C  
-ANISOU11082  CB  LYS B 766    29009  23879  30320     -8   4608   1005       C  
-ATOM  11083  CG  LYS B 766     -25.845  -6.555  55.509  1.00225.65           C  
-ANISOU11083  CG  LYS B 766    29889  24592  31254    161   4509   1163       C  
-ATOM  11084  CD  LYS B 766     -25.495  -7.714  54.585  1.00232.74           C  
-ANISOU11084  CD  LYS B 766    30774  25328  32329     58   4743   1087       C  
-ATOM  11085  CE  LYS B 766     -26.088  -9.022  55.081  1.00238.95           C  
-ANISOU11085  CE  LYS B 766    31729  25893  33169    -21   5092   1084       C  
-ATOM  11086  NZ  LYS B 766     -25.833 -10.142  54.133  1.00242.93           N  
-ANISOU11086  NZ  LYS B 766    32218  26239  33845   -145   5345    988       N  
-ATOM  11087  N   ALA B 767     -26.552  -3.912  58.101  1.00152.84           N  
-ANISOU11087  N   ALA B 767    20769  15695  21610    435   3997   1391       N  
-ATOM  11088  CA  ALA B 767     -25.925  -3.730  59.404  1.00150.64           C  
-ANISOU11088  CA  ALA B 767    20640  15347  21248    637   3885   1609       C  
-ATOM  11089  C   ALA B 767     -26.479  -2.502  60.129  1.00147.09           C  
-ANISOU11089  C   ALA B 767    20178  15080  20629    674   3693   1622       C  
-ATOM  11090  O   ALA B 767     -26.745  -2.548  61.331  1.00149.81           O  
-ANISOU11090  O   ALA B 767    20665  15376  20881    748   3714   1734       O  
-ATOM  11091  CB  ALA B 767     -24.412  -3.623  59.254  1.00153.25           C  
-ANISOU11091  CB  ALA B 767    20958  15638  21632    802   3722   1742       C  
-ATOM  11092  N   VAL B 768     -26.662  -1.411  59.387  1.00152.08           N  
-ANISOU11092  N   VAL B 768    20645  15918  21222    622   3516   1506       N  
-ATOM  11093  CA  VAL B 768     -27.074  -0.135  59.969  1.00145.10           C  
-ANISOU11093  CA  VAL B 768    19739  15209  20184    668   3320   1518       C  
-ATOM  11094  C   VAL B 768     -27.990   0.653  59.023  1.00137.56           C  
-ANISOU11094  C   VAL B 768    18611  14458  19197    530   3277   1324       C  
-ATOM  11095  O   VAL B 768     -27.866   0.550  57.802  1.00137.95           O  
-ANISOU11095  O   VAL B 768    18526  14552  19335    443   3294   1206       O  
-ATOM  11096  CB  VAL B 768     -25.838   0.721  60.326  1.00146.53           C  
-ANISOU11096  CB  VAL B 768    19922  15437  20314    844   3058   1658       C  
-ATOM  11097  CG1 VAL B 768     -25.044   1.063  59.072  1.00144.68           C  
-ANISOU11097  CG1 VAL B 768    19538  15267  20167    830   2943   1587       C  
-ATOM  11098  CG2 VAL B 768     -26.243   1.979  61.068  1.00142.81           C  
-ANISOU11098  CG2 VAL B 768    19457  15123  19683    892   2882   1680       C  
-ATOM  11099  N   SER B 769     -28.911   1.431  59.592  1.00143.64           N  
-ANISOU11099  N   SER B 769    19383  15356  19837    516   3223   1294       N  
-ATOM  11100  CA  SER B 769     -29.831   2.255  58.802  1.00131.43           C  
-ANISOU11100  CA  SER B 769    17677  14021  18239    412   3175   1126       C  
-ATOM  11101  C   SER B 769     -29.555   3.752  58.953  1.00122.42           C  
-ANISOU11101  C   SER B 769    16488  13037  16988    516   2914   1167       C  
-ATOM  11102  O   SER B 769     -28.837   4.176  59.863  1.00120.06           O  
-ANISOU11102  O   SER B 769    16291  12696  16632    652   2783   1316       O  
-ATOM  11103  CB  SER B 769     -31.288   1.965  59.176  1.00131.97           C  
-ANISOU11103  CB  SER B 769    17762  14133  18247    291   3349   1024       C  
-ATOM  11104  OG  SER B 769     -31.672   0.659  58.790  1.00133.28           O  
-ANISOU11104  OG  SER B 769    17943  14183  18516    157   3608    938       O  
-ATOM  11105  N   ARG B 770     -30.136   4.549  58.060  1.00 98.98           N  
-ANISOU11105  N   ARG B 770    13365  10256  13985    451   2850   1032       N  
-ATOM  11106  CA  ARG B 770     -29.928   5.992  58.072  1.00 89.13           C  
-ANISOU11106  CA  ARG B 770    12072   9155  12639    541   2625   1056       C  
-ATOM  11107  C   ARG B 770     -31.232   6.726  57.795  1.00 84.06           C  
-ANISOU11107  C   ARG B 770    11331   8707  11901    474   2633    930       C  
-ATOM  11108  O   ARG B 770     -31.967   6.377  56.872  1.00 84.77           O  
-ANISOU11108  O   ARG B 770    11297   8885  12026    352   2744    783       O  
-ATOM  11109  CB  ARG B 770     -28.871   6.377  57.040  1.00 87.34           C  
-ANISOU11109  CB  ARG B 770    11749   8957  12481    575   2492   1047       C  
-ATOM  11110  CG  ARG B 770     -27.621   5.524  57.122  1.00 86.34           C  
-ANISOU11110  CG  ARG B 770    11691   8649  12465    629   2507   1149       C  
-ATOM  11111  CD  ARG B 770     -26.514   6.067  56.240  1.00 83.74           C  
-ANISOU11111  CD  ARG B 770    11274   8356  12186    674   2349   1148       C  
-ATOM  11112  NE  ARG B 770     -25.294   5.270  56.343  1.00 83.61           N  
-ANISOU11112  NE  ARG B 770    11319   8178  12272    737   2357   1248       N  
-ATOM  11113  CZ  ARG B 770     -24.993   4.259  55.536  1.00 83.28           C  
-ANISOU11113  CZ  ARG B 770    11232   8041  12368    667   2484   1198       C  
-ATOM  11114  NH1 ARG B 770     -25.824   3.915  54.561  1.00 85.19           N  
-ANISOU11114  NH1 ARG B 770    11365   8343  12659    520   2612   1042       N  
-ATOM  11115  NH2 ARG B 770     -23.861   3.592  55.701  1.00 82.23           N  
-ANISOU11115  NH2 ARG B 770    11160   7763  12320    745   2485   1302       N  
-ATOM  11116  N   PHE B 771     -31.514   7.748  58.595  1.00 79.41           N  
-ANISOU11116  N   PHE B 771    10792   8193  11187    555   2518    986       N  
-ATOM  11117  CA  PHE B 771     -32.798   8.431  58.522  1.00 75.42           C  
-ANISOU11117  CA  PHE B 771    10212   7864  10580    511   2534    884       C  
-ATOM  11118  C   PHE B 771     -32.696   9.940  58.301  1.00 70.75           C  
-ANISOU11118  C   PHE B 771     9565   7419   9896    601   2343    892       C  
-ATOM  11119  O   PHE B 771     -31.800  10.608  58.822  1.00 69.20           O  
-ANISOU11119  O   PHE B 771     9448   7176   9668    710   2197   1004       O  
-ATOM  11120  CB  PHE B 771     -33.615   8.164  59.793  1.00 75.53           C  
-ANISOU11120  CB  PHE B 771    10347   7833  10519    501   2631    921       C  
-ATOM  11121  CG  PHE B 771     -34.010   6.731  59.974  1.00 76.31           C  
-ANISOU11121  CG  PHE B 771    10497   7805  10691    394   2854    886       C  
-ATOM  11122  CD1 PHE B 771     -34.946   6.148  59.139  1.00 77.62           C  
-ANISOU11122  CD1 PHE B 771    10544   8055  10894    247   3016    719       C  
-ATOM  11123  CD2 PHE B 771     -33.459   5.970  60.990  1.00 75.42           C  
-ANISOU11123  CD2 PHE B 771    10556   7496  10606    440   2912   1019       C  
-ATOM  11124  CE1 PHE B 771     -35.313   4.825  59.305  1.00 79.03           C  
-ANISOU11124  CE1 PHE B 771    10779   8109  11141    135   3242    675       C  
-ATOM  11125  CE2 PHE B 771     -33.824   4.651  61.159  1.00 75.93           C  
-ANISOU11125  CE2 PHE B 771    10684   7427  10738    344   3136    991       C  
-ATOM  11126  CZ  PHE B 771     -34.750   4.079  60.316  1.00 77.90           C  
-ANISOU11126  CZ  PHE B 771    10821   7747  11030    186   3307    814       C  
-ATOM  11127  N   HIS B 772     -33.633  10.461  57.518  1.00 80.32           N  
-ANISOU11127  N   HIS B 772    10641   8816  11062    554   2357    767       N  
-ATOM  11128  CA  HIS B 772     -33.860  11.891  57.421  1.00 74.71           C  
-ANISOU11128  CA  HIS B 772     9890   8252  10244    640   2217    768       C  
-ATOM  11129  C   HIS B 772     -35.119  12.216  58.212  1.00 74.40           C  
-ANISOU11129  C   HIS B 772     9876   8299  10093    633   2277    742       C  
-ATOM  11130  O   HIS B 772     -36.153  11.574  58.031  1.00 73.12           O  
-ANISOU11130  O   HIS B 772     9647   8205   9930    532   2423    636       O  
-ATOM  11131  CB  HIS B 772     -34.063  12.306  55.964  1.00 74.71           C  
-ANISOU11131  CB  HIS B 772     9714   8415  10257    612   2189    655       C  
-ATOM  11132  CG  HIS B 772     -32.806  12.693  55.250  1.00 73.06           C  
-ANISOU11132  CG  HIS B 772     9486   8165  10108    666   2059    696       C  
-ATOM  11133  ND1 HIS B 772     -31.586  12.794  55.890  1.00 73.45           N  
-ANISOU11133  ND1 HIS B 772     9659   8063  10186    742   1961    822       N  
-ATOM  11134  CD2 HIS B 772     -32.576  13.014  53.956  1.00 72.83           C  
-ANISOU11134  CD2 HIS B 772     9327   8235  10110    654   2013    624       C  
-ATOM  11135  CE1 HIS B 772     -30.660  13.157  55.011  1.00 73.42           C  
-ANISOU11135  CE1 HIS B 772     9601   8064  10233    769   1862    819       C  
-ATOM  11136  NE2 HIS B 772     -31.241  13.296  53.835  1.00 73.51           N  
-ANISOU11136  NE2 HIS B 772     9464   8219  10248    716   1892    703       N  
-ATOM  11137  N   SER B 773     -35.038  13.202  59.097  1.00 60.99           N  
-ANISOU11137  N   SER B 773     8272   6602   8299    733   2172    829       N  
-ATOM  11138  CA  SER B 773     -36.235  13.684  59.769  1.00 62.28           C  
-ANISOU11138  CA  SER B 773     8449   6864   8351    737   2216    800       C  
-ATOM  11139  C   SER B 773     -37.088  14.447  58.763  1.00 62.49           C  
-ANISOU11139  C   SER B 773     8313   7109   8321    742   2204    688       C  
-ATOM  11140  O   SER B 773     -36.572  14.963  57.775  1.00 62.04           O  
-ANISOU11140  O   SER B 773     8174   7113   8287    780   2117    672       O  
-ATOM  11141  CB  SER B 773     -35.872  14.582  60.949  1.00 61.89           C  
-ANISOU11141  CB  SER B 773     8542   6758   8214    841   2108    921       C  
-ATOM  11142  OG  SER B 773     -35.347  15.816  60.500  1.00 60.03           O  
-ANISOU11142  OG  SER B 773     8280   6588   7939    933   1964    945       O  
-ATOM  11143  N   PRO B 774     -38.402  14.523  59.010  1.00 78.20           N  
-ANISOU11143  N   PRO B 774    10255   9225  10232    707   2293    611       N  
-ATOM  11144  CA  PRO B 774     -39.282  15.228  58.073  1.00 77.44           C  
-ANISOU11144  CA  PRO B 774     9995   9361  10069    725   2287    507       C  
-ATOM  11145  C   PRO B 774     -38.818  16.670  57.879  1.00 75.05           C  
-ANISOU11145  C   PRO B 774     9706   9105   9703    867   2131    576       C  
-ATOM  11146  O   PRO B 774     -38.850  17.197  56.768  1.00 75.49           O  
-ANISOU11146  O   PRO B 774     9640   9296   9748    903   2086    527       O  
-ATOM  11147  CB  PRO B 774     -40.646  15.184  58.773  1.00 78.58           C  
-ANISOU11147  CB  PRO B 774    10130   9603  10123    689   2392    446       C  
-ATOM  11148  CG  PRO B 774     -40.336  14.926  60.228  1.00 78.01           C  
-ANISOU11148  CG  PRO B 774    10253   9340  10047    696   2403    554       C  
-ATOM  11149  CD  PRO B 774     -39.115  14.064  60.214  1.00 81.97           C  
-ANISOU11149  CD  PRO B 774    10833   9646  10666    665   2394    623       C  
-ATOM  11150  N   PHE B 775     -38.377  17.292  58.966  1.00 59.55           N  
-ANISOU11150  N   PHE B 775     7899   7031   7695    944   2058    689       N  
-ATOM  11151  CA  PHE B 775     -37.867  18.654  58.926  1.00 56.16           C  
-ANISOU11151  CA  PHE B 775     7513   6619   7208   1069   1926    757       C  
-ATOM  11152  C   PHE B 775     -36.585  18.743  58.106  1.00 54.91           C  
-ANISOU11152  C   PHE B 775     7343   6394   7128   1090   1831    788       C  
-ATOM  11153  O   PHE B 775     -36.402  19.682  57.332  1.00 53.72           O  
-ANISOU11153  O   PHE B 775     7140   6326   6947   1163   1759    780       O  
-ATOM  11154  CB  PHE B 775     -37.618  19.148  60.350  1.00 52.75           C  
-ANISOU11154  CB  PHE B 775     7255   6073   6716   1120   1885    861       C  
-ATOM  11155  CG  PHE B 775     -36.919  20.477  60.428  1.00 47.71           C  
-ANISOU11155  CG  PHE B 775     6686   5417   6025   1230   1763    931       C  
-ATOM  11156  CD1 PHE B 775     -37.642  21.660  60.422  1.00 46.80           C  
-ANISOU11156  CD1 PHE B 775     6558   5417   5807   1315   1753    920       C  
-ATOM  11157  CD2 PHE B 775     -35.538  20.541  60.527  1.00 45.97           C  
-ANISOU11157  CD2 PHE B 775     6547   5066   5855   1248   1669   1007       C  
-ATOM  11158  CE1 PHE B 775     -37.000  22.880  60.509  1.00 45.92           C  
-ANISOU11158  CE1 PHE B 775     6524   5275   5648   1408   1662    980       C  
-ATOM  11159  CE2 PHE B 775     -34.889  21.761  60.609  1.00 45.40           C  
-ANISOU11159  CE2 PHE B 775     6541   4978   5731   1333   1571   1057       C  
-ATOM  11160  CZ  PHE B 775     -35.622  22.929  60.604  1.00 45.38           C  
-ANISOU11160  CZ  PHE B 775     6536   5075   5630   1410   1573   1043       C  
-ATOM  11161  N   ILE B 776     -35.698  17.768  58.285  1.00 59.55           N  
-ANISOU11161  N   ILE B 776     7982   6829   7814   1031   1837    825       N  
-ATOM  11162  CA  ILE B 776     -34.429  17.739  57.556  1.00 57.48           C  
-ANISOU11162  CA  ILE B 776     7709   6496   7636   1043   1751    852       C  
-ATOM  11163  C   ILE B 776     -34.626  17.517  56.059  1.00 56.81           C  
-ANISOU11163  C   ILE B 776     7455   6529   7601   1000   1777    749       C  
-ATOM  11164  O   ILE B 776     -33.898  18.078  55.244  1.00 55.64           O  
-ANISOU11164  O   ILE B 776     7270   6396   7473   1042   1689    753       O  
-ATOM  11165  CB  ILE B 776     -33.471  16.666  58.116  1.00 58.66           C  
-ANISOU11165  CB  ILE B 776     7949   6461   7880    998   1762    919       C  
-ATOM  11166  CG1 ILE B 776     -32.608  17.255  59.232  1.00 56.49           C  
-ANISOU11166  CG1 ILE B 776     7828   6078   7559   1075   1661   1040       C  
-ATOM  11167  CG2 ILE B 776     -32.588  16.104  57.018  1.00 55.70           C  
-ANISOU11167  CG2 ILE B 776     7496   6048   7621    960   1743    890       C  
-ATOM  11168  CD1 ILE B 776     -31.822  16.223  59.997  1.00 60.55           C  
-ANISOU11168  CD1 ILE B 776     8439   6431   8138   1052   1679   1121       C  
-ATOM  11169  N   VAL B 777     -35.615  16.704  55.701  1.00 50.21           N  
-ANISOU11169  N   VAL B 777     6514   5785   6779    909   1902    650       N  
-ATOM  11170  CA  VAL B 777     -35.921  16.458  54.297  1.00 48.80           C  
-ANISOU11170  CA  VAL B 777     6159   5747   6634    856   1937    538       C  
-ATOM  11171  C   VAL B 777     -36.304  17.749  53.588  1.00 49.66           C  
-ANISOU11171  C   VAL B 777     6190   6032   6648    956   1863    518       C  
-ATOM  11172  O   VAL B 777     -35.679  18.131  52.608  1.00 48.94           O  
-ANISOU11172  O   VAL B 777     6040   5970   6584    985   1793    510       O  
-ATOM  11173  CB  VAL B 777     -37.070  15.458  54.134  1.00 47.28           C  
-ANISOU11173  CB  VAL B 777     5864   5653   6448    734   2097    420       C  
-ATOM  11174  CG1 VAL B 777     -37.612  15.498  52.717  1.00 47.36           C  
-ANISOU11174  CG1 VAL B 777     5673   5874   6446    696   2124    295       C  
-ATOM  11175  CG2 VAL B 777     -36.604  14.066  54.497  1.00 47.79           C  
-ANISOU11175  CG2 VAL B 777     5991   5539   6628    625   2193    425       C  
-ATOM  11176  N   GLU B 778     -37.331  18.422  54.094  1.00 64.41           N  
-ANISOU11176  N   GLU B 778     8060   8012   8402   1014   1884    513       N  
-ATOM  11177  CA  GLU B 778     -37.838  19.631  53.456  1.00 64.78           C  
-ANISOU11177  CA  GLU B 778     8031   8235   8347   1124   1834    499       C  
-ATOM  11178  C   GLU B 778     -36.773  20.722  53.372  1.00 62.59           C  
-ANISOU11178  C   GLU B 778     7853   7867   8061   1234   1706    593       C  
-ATOM  11179  O   GLU B 778     -36.741  21.490  52.413  1.00 61.70           O  
-ANISOU11179  O   GLU B 778     7668   7862   7912   1306   1661    578       O  
-ATOM  11180  CB  GLU B 778     -39.075  20.159  54.190  1.00 69.90           C  
-ANISOU11180  CB  GLU B 778     8686   8995   8876   1177   1883    491       C  
-ATOM  11181  CG  GLU B 778     -38.818  21.397  55.041  1.00 76.39           C  
-ANISOU11181  CG  GLU B 778     9659   9742   9623   1305   1805    598       C  
-ATOM  11182  CD  GLU B 778     -39.676  22.586  54.631  1.00 81.43           C  
-ANISOU11182  CD  GLU B 778    10233  10566  10140   1432   1797    587       C  
-ATOM  11183  OE1 GLU B 778     -39.708  23.589  55.380  1.00 84.31           O  
-ANISOU11183  OE1 GLU B 778    10715  10885  10433   1531   1765    661       O  
-ATOM  11184  OE2 GLU B 778     -40.318  22.520  53.560  1.00 85.02           O  
-ANISOU11184  OE2 GLU B 778    10518  11218  10568   1436   1829    504       O  
-ATOM  11185  N   ASN B 779     -35.904  20.789  54.376  1.00 57.51           N  
-ANISOU11185  N   ASN B 779     7373   7032   7445   1245   1655    686       N  
-ATOM  11186  CA  ASN B 779     -34.866  21.817  54.416  1.00 55.45           C  
-ANISOU11186  CA  ASN B 779     7215   6683   7171   1333   1544    765       C  
-ATOM  11187  C   ASN B 779     -33.615  21.445  53.621  1.00 53.21           C  
-ANISOU11187  C   ASN B 779     6911   6314   6993   1295   1483    765       C  
-ATOM  11188  O   ASN B 779     -32.877  22.318  53.173  1.00 51.20           O  
-ANISOU11188  O   ASN B 779     6688   6039   6726   1359   1403    794       O  
-ATOM  11189  CB  ASN B 779     -34.508  22.179  55.860  1.00 56.32           C  
-ANISOU11189  CB  ASN B 779     7500   6656   7243   1364   1513    857       C  
-ATOM  11190  CG  ASN B 779     -35.295  23.363  56.367  1.00 59.14           C  
-ANISOU11190  CG  ASN B 779     7907   7087   7475   1462   1519    880       C  
-ATOM  11191  OD1 ASN B 779     -36.023  23.262  57.350  1.00 59.39           O  
-ANISOU11191  OD1 ASN B 779     7989   7120   7457   1454   1571    892       O  
-ATOM  11192  ND2 ASN B 779     -35.162  24.498  55.687  1.00 61.56           N  
-ANISOU11192  ND2 ASN B 779     8205   7453   7732   1556   1475    886       N  
-ATOM  11193  N   TYR B 780     -33.377  20.148  53.458  1.00 55.72           N  
-ANISOU11193  N   TYR B 780     7181   6575   7414   1188   1531    731       N  
-ATOM  11194  CA  TYR B 780     -32.297  19.676  52.605  1.00 53.25           C  
-ANISOU11194  CA  TYR B 780     6828   6195   7209   1143   1489    718       C  
-ATOM  11195  C   TYR B 780     -32.734  19.896  51.168  1.00 53.12           C  
-ANISOU11195  C   TYR B 780     6652   6347   7184   1140   1502    629       C  
-ATOM  11196  O   TYR B 780     -31.944  20.293  50.317  1.00 53.15           O  
-ANISOU11196  O   TYR B 780     6631   6343   7219   1161   1434    627       O  
-ATOM  11197  CB  TYR B 780     -32.019  18.197  52.860  1.00 52.30           C  
-ANISOU11197  CB  TYR B 780     6706   5964   7200   1033   1559    706       C  
-ATOM  11198  CG  TYR B 780     -30.783  17.669  52.172  1.00 48.85           C  
-ANISOU11198  CG  TYR B 780     6250   5429   6882    993   1516    708       C  
-ATOM  11199  CD1 TYR B 780     -29.607  18.404  52.150  1.00 46.60           C  
-ANISOU11199  CD1 TYR B 780     6036   5066   6602   1057   1396    768       C  
-ATOM  11200  CD2 TYR B 780     -30.785  16.420  51.564  1.00 49.21           C  
-ANISOU11200  CD2 TYR B 780     6207   5456   7035    885   1604    641       C  
-ATOM  11201  CE1 TYR B 780     -28.468  17.918  51.525  1.00 47.11           C  
-ANISOU11201  CE1 TYR B 780     6077   5046   6776   1021   1356    765       C  
-ATOM  11202  CE2 TYR B 780     -29.656  15.924  50.944  1.00 49.09           C  
-ANISOU11202  CE2 TYR B 780     6174   5346   7132    850   1570    642       C  
-ATOM  11203  CZ  TYR B 780     -28.497  16.677  50.924  1.00 48.27           C  
-ANISOU11203  CZ  TYR B 780     6135   5173   7031    921   1441    705       C  
-ATOM  11204  OH  TYR B 780     -27.367  16.184  50.301  1.00 47.30           O  
-ANISOU11204  OH  TYR B 780     5989   4963   7020    887   1407    701       O  
-ATOM  11205  N   ARG B 781     -34.011  19.639  50.914  1.00 43.69           N  
-ANISOU11205  N   ARG B 781     5346   5315   5940   1112   1592    553       N  
-ATOM  11206  CA  ARG B 781     -34.632  19.955  49.642  1.00 43.79           C  
-ANISOU11206  CA  ARG B 781     5197   5532   5910   1126   1607    471       C  
-ATOM  11207  C   ARG B 781     -34.377  21.426  49.312  1.00 43.27           C  
-ANISOU11207  C   ARG B 781     5174   5509   5759   1268   1516    525       C  
-ATOM  11208  O   ARG B 781     -33.830  21.756  48.263  1.00 42.84           O  
-ANISOU11208  O   ARG B 781     5064   5488   5724   1287   1468    509       O  
-ATOM  11209  CB  ARG B 781     -36.128  19.676  49.738  1.00 44.71           C  
-ANISOU11209  CB  ARG B 781     5207   5830   5949   1100   1711    394       C  
-ATOM  11210  CG  ARG B 781     -36.753  19.144  48.478  1.00 50.84           C  
-ANISOU11210  CG  ARG B 781     5779   6807   6729   1027   1775    269       C  
-ATOM  11211  CD  ARG B 781     -38.043  18.393  48.783  1.00 58.14           C  
-ANISOU11211  CD  ARG B 781     6611   7864   7616    941   1903    176       C  
-ATOM  11212  NE  ARG B 781     -39.165  18.904  48.003  1.00 66.04           N  
-ANISOU11212  NE  ARG B 781     7443   9152   8499    990   1929     97       N  
-ATOM  11213  CZ  ARG B 781     -39.289  18.758  46.686  1.00 70.52           C  
-ANISOU11213  CZ  ARG B 781     7837   9894   9062    956   1938     10       C  
-ATOM  11214  NH1 ARG B 781     -38.348  18.125  45.991  1.00 73.47           N  
-ANISOU11214  NH1 ARG B 781     8191  10172   9553    866   1926    -14       N  
-ATOM  11215  NH2 ARG B 781     -40.353  19.254  46.064  1.00 72.45           N  
-ANISOU11215  NH2 ARG B 781     7926  10419   9182   1017   1959    -53       N  
-ATOM  11216  N   HIS B 782     -34.760  22.307  50.225  1.00 53.49           N  
-ANISOU11216  N   HIS B 782     6573   6790   6959   1363   1502    590       N  
-ATOM  11217  CA  HIS B 782     -34.545  23.737  50.054  1.00 52.20           C  
-ANISOU11217  CA  HIS B 782     6477   6643   6712   1500   1438    648       C  
-ATOM  11218  C   HIS B 782     -33.075  24.027  49.776  1.00 50.79           C  
-ANISOU11218  C   HIS B 782     6384   6312   6602   1499   1350    690       C  
-ATOM  11219  O   HIS B 782     -32.735  24.737  48.833  1.00 49.29           O  
-ANISOU11219  O   HIS B 782     6166   6169   6392   1558   1311    686       O  
-ATOM  11220  CB  HIS B 782     -34.981  24.472  51.317  1.00 54.67           C  
-ANISOU11220  CB  HIS B 782     6924   6912   6938   1576   1445    715       C  
-ATOM  11221  CG  HIS B 782     -34.993  25.962  51.185  1.00 57.28           C  
-ANISOU11221  CG  HIS B 782     7325   7270   7170   1719   1413    766       C  
-ATOM  11222  ND1 HIS B 782     -34.569  26.802  52.192  1.00 59.06           N  
-ANISOU11222  ND1 HIS B 782     7722   7365   7354   1775   1384    843       N  
-ATOM  11223  CD2 HIS B 782     -35.398  26.766  50.172  1.00 59.57           C  
-ANISOU11223  CD2 HIS B 782     7540   7704   7390   1820   1416    753       C  
-ATOM  11224  CE1 HIS B 782     -34.699  28.057  51.802  1.00 60.45           C  
-ANISOU11224  CE1 HIS B 782     7935   7588   7446   1900   1380    872       C  
-ATOM  11225  NE2 HIS B 782     -35.200  28.063  50.582  1.00 61.30           N  
-ANISOU11225  NE2 HIS B 782     7898   7860   7533   1937   1398    825       N  
-ATOM  11226  N   LEU B 783     -32.205  23.458  50.601  1.00 46.54           N  
-ANISOU11226  N   LEU B 783     5946   5596   6141   1435   1321    730       N  
-ATOM  11227  CA  LEU B 783     -30.770  23.701  50.500  1.00 46.13           C  
-ANISOU11227  CA  LEU B 783     5977   5400   6149   1431   1236    768       C  
-ATOM  11228  C   LEU B 783     -30.237  23.408  49.114  1.00 46.70           C  
-ANISOU11228  C   LEU B 783     5938   5512   6295   1391   1215    711       C  
-ATOM  11229  O   LEU B 783     -29.514  24.217  48.541  1.00 45.48           O  
-ANISOU11229  O   LEU B 783     5816   5334   6130   1438   1156    723       O  
-ATOM  11230  CB  LEU B 783     -30.000  22.857  51.512  1.00 45.63           C  
-ANISOU11230  CB  LEU B 783     6002   5173   6163   1362   1219    812       C  
-ATOM  11231  CG  LEU B 783     -28.487  22.937  51.334  1.00 43.44           C  
-ANISOU11231  CG  LEU B 783     5781   4768   5955   1347   1132    838       C  
-ATOM  11232  CD1 LEU B 783     -28.000  24.335  51.652  1.00 43.71           C  
-ANISOU11232  CD1 LEU B 783     5934   4770   5905   1432   1072    882       C  
-ATOM  11233  CD2 LEU B 783     -27.785  21.921  52.201  1.00 42.99           C  
-ANISOU11233  CD2 LEU B 783     5782   4577   5977   1285   1123    879       C  
-ATOM  11234  N   ASN B 784     -30.582  22.239  48.586  1.00 51.22           N  
-ANISOU11234  N   ASN B 784     6384   6138   6941   1295   1272    643       N  
-ATOM  11235  CA  ASN B 784     -30.104  21.840  47.269  1.00 53.46           C  
-ANISOU11235  CA  ASN B 784     6551   6462   7300   1239   1261    579       C  
-ATOM  11236  C   ASN B 784     -30.662  22.720  46.152  1.00 56.18           C  
-ANISOU11236  C   ASN B 784     6803   6983   7558   1313   1258    543       C  
-ATOM  11237  O   ASN B 784     -30.045  22.865  45.096  1.00 56.66           O  
-ANISOU11237  O   ASN B 784     6812   7060   7656   1304   1221    514       O  
-ATOM  11238  CB  ASN B 784     -30.407  20.366  47.001  1.00 51.34           C  
-ANISOU11238  CB  ASN B 784     6171   6210   7127   1109   1343    507       C  
-ATOM  11239  CG  ASN B 784     -29.511  19.439  47.795  1.00 48.74           C  
-ANISOU11239  CG  ASN B 784     5930   5682   6906   1041   1339    549       C  
-ATOM  11240  OD1 ASN B 784     -29.914  18.342  48.173  1.00 48.14           O  
-ANISOU11240  OD1 ASN B 784     5830   5579   6883    959   1425    524       O  
-ATOM  11241  ND2 ASN B 784     -28.288  19.885  48.066  1.00 44.25           N  
-ANISOU11241  ND2 ASN B 784     5467   4979   6367   1080   1246    613       N  
-ATOM  11242  N   GLN B 785     -31.829  23.310  46.384  1.00 65.84           N  
-ANISOU11242  N   GLN B 785     8007   8344   8665   1394   1299    548       N  
-ATOM  11243  CA  GLN B 785     -32.392  24.242  45.419  1.00 66.90           C  
-ANISOU11243  CA  GLN B 785     8066   8653   8700   1495   1297    533       C  
-ATOM  11244  C   GLN B 785     -31.555  25.519  45.362  1.00 65.59           C  
-ANISOU11244  C   GLN B 785     8036   8390   8494   1600   1228    604       C  
-ATOM  11245  O   GLN B 785     -31.495  26.182  44.331  1.00 64.29           O  
-ANISOU11245  O   GLN B 785     7828   8313   8288   1665   1213    596       O  
-ATOM  11246  CB  GLN B 785     -33.844  24.561  45.763  1.00 69.89           C  
-ANISOU11246  CB  GLN B 785     8393   9203   8958   1568   1361    527       C  
-ATOM  11247  CG  GLN B 785     -34.753  23.350  45.738  1.00 75.21           C  
-ANISOU11247  CG  GLN B 785     8923   9997   9658   1456   1444    438       C  
-ATOM  11248  CD  GLN B 785     -35.949  23.535  46.635  1.00 79.77           C  
-ANISOU11248  CD  GLN B 785     9509  10660  10140   1505   1503    446       C  
-ATOM  11249  OE1 GLN B 785     -36.662  22.582  46.947  1.00 82.16           O  
-ANISOU11249  OE1 GLN B 785     9735  11021  10460   1408   1578    381       O  
-ATOM  11250  NE2 GLN B 785     -36.174  24.770  47.065  1.00 82.08           N  
-ANISOU11250  NE2 GLN B 785     9901  10956  10331   1651   1477    522       N  
-ATOM  11251  N   LEU B 786     -30.906  25.859  46.471  1.00 62.79           N  
-ANISOU11251  N   LEU B 786     7847   7860   8150   1612   1194    671       N  
-ATOM  11252  CA  LEU B 786     -30.029  27.022  46.494  1.00 62.59           C  
-ANISOU11252  CA  LEU B 786     7960   7729   8093   1688   1141    724       C  
-ATOM  11253  C   LEU B 786     -28.662  26.683  45.913  1.00 62.71           C  
-ANISOU11253  C   LEU B 786     7981   7631   8215   1609   1079    702       C  
-ATOM  11254  O   LEU B 786     -28.109  27.454  45.131  1.00 63.27           O  
-ANISOU11254  O   LEU B 786     8077   7696   8268   1653   1051    701       O  
-ATOM  11255  CB  LEU B 786     -29.875  27.571  47.912  1.00 62.80           C  
-ANISOU11255  CB  LEU B 786     8156   7631   8076   1723   1134    792       C  
-ATOM  11256  CG  LEU B 786     -31.154  28.013  48.622  1.00 64.57           C  
-ANISOU11256  CG  LEU B 786     8397   7945   8193   1804   1195    819       C  
-ATOM  11257  CD1 LEU B 786     -30.820  28.614  49.978  1.00 64.33           C  
-ANISOU11257  CD1 LEU B 786     8543   7776   8123   1828   1184    883       C  
-ATOM  11258  CD2 LEU B 786     -31.937  28.997  47.770  1.00 63.66           C  
-ANISOU11258  CD2 LEU B 786     8235   7980   7972   1935   1231    821       C  
-ATOM  11259  N   ARG B 787     -28.113  25.537  46.303  1.00 55.68           N  
-ANISOU11259  N   ARG B 787     7073   6648   7434   1497   1063    686       N  
-ATOM  11260  CA  ARG B 787     -26.858  25.078  45.729  1.00 54.93           C  
-ANISOU11260  CA  ARG B 787     6965   6457   7450   1419   1010    660       C  
-ATOM  11261  C   ARG B 787     -26.953  25.198  44.219  1.00 54.78           C  
-ANISOU11261  C   ARG B 787     6824   6555   7436   1420   1015    600       C  
-ATOM  11262  O   ARG B 787     -26.135  25.860  43.582  1.00 53.59           O  
-ANISOU11262  O   ARG B 787     6712   6363   7288   1441    971    598       O  
-ATOM  11263  CB  ARG B 787     -26.581  23.622  46.101  1.00 54.38           C  
-ANISOU11263  CB  ARG B 787     6848   6317   7498   1306   1023    641       C  
-ATOM  11264  CG  ARG B 787     -25.647  23.428  47.283  1.00 54.64           C  
-ANISOU11264  CG  ARG B 787     7009   6183   7570   1288    976    700       C  
-ATOM  11265  CD  ARG B 787     -26.420  23.087  48.541  1.00 55.49           C  
-ANISOU11265  CD  ARG B 787     7168   6279   7636   1296   1021    744       C  
-ATOM  11266  NE  ARG B 787     -26.067  21.781  49.097  1.00 53.47           N  
-ANISOU11266  NE  ARG B 787     6908   5930   7480   1216   1039    755       N  
-ATOM  11267  CZ  ARG B 787     -25.043  21.567  49.919  1.00 52.60           C  
-ANISOU11267  CZ  ARG B 787     6892   5686   7407   1208    986    810       C  
-ATOM  11268  NH1 ARG B 787     -24.249  22.569  50.270  1.00 52.97           N  
-ANISOU11268  NH1 ARG B 787     7040   5685   7402   1259    910    846       N  
-ATOM  11269  NH2 ARG B 787     -24.806  20.349  50.386  1.00 51.06           N  
-ANISOU11269  NH2 ARG B 787     6692   5411   7297   1151   1016    829       N  
-ATOM  11270  N   GLU B 788     -27.970  24.558  43.655  1.00 62.16           N  
-ANISOU11270  N   GLU B 788     7610   7645   8364   1391   1075    547       N  
-ATOM  11271  CA  GLU B 788     -28.154  24.543  42.214  1.00 62.07           C  
-ANISOU11271  CA  GLU B 788     7460   7774   8351   1381   1086    483       C  
-ATOM  11272  C   GLU B 788     -28.261  25.949  41.636  1.00 61.38           C  
-ANISOU11272  C   GLU B 788     7418   7755   8150   1515   1068    517       C  
-ATOM  11273  O   GLU B 788     -27.654  26.253  40.608  1.00 60.24           O  
-ANISOU11273  O   GLU B 788     7248   7619   8022   1514   1039    493       O  
-ATOM  11274  CB  GLU B 788     -29.380  23.712  41.840  1.00 66.12           C  
-ANISOU11274  CB  GLU B 788     7803   8472   8848   1333   1163    415       C  
-ATOM  11275  CG  GLU B 788     -29.227  22.232  42.148  1.00 71.85           C  
-ANISOU11275  CG  GLU B 788     8473   9127   9698   1185   1204    366       C  
-ATOM  11276  CD  GLU B 788     -30.226  21.374  41.394  1.00 77.56           C  
-ANISOU11276  CD  GLU B 788     9005  10042  10421   1103   1289    266       C  
-ATOM  11277  OE1 GLU B 788     -31.151  21.947  40.775  1.00 82.62           O  
-ANISOU11277  OE1 GLU B 788     9551  10892  10948   1174   1309    241       O  
-ATOM  11278  OE2 GLU B 788     -30.084  20.130  41.415  1.00 78.92           O  
-ANISOU11278  OE2 GLU B 788     9121  10162  10702    970   1341    210       O  
-ATOM  11279  N   GLN B 789     -29.023  26.808  42.302  1.00 56.54           N  
-ANISOU11279  N   GLN B 789     6880   7181   7420   1631   1093    574       N  
-ATOM  11280  CA  GLN B 789     -29.224  28.169  41.827  1.00 55.26           C  
-ANISOU11280  CA  GLN B 789     6776   7078   7143   1775   1097    617       C  
-ATOM  11281  C   GLN B 789     -27.947  28.992  41.917  1.00 53.50           C  
-ANISOU11281  C   GLN B 789     6716   6672   6940   1792   1049    652       C  
-ATOM  11282  O   GLN B 789     -27.727  29.894  41.109  1.00 54.31           O  
-ANISOU11282  O   GLN B 789     6851   6798   6988   1869   1050    664       O  
-ATOM  11283  CB  GLN B 789     -30.333  28.861  42.612  1.00 55.92           C  
-ANISOU11283  CB  GLN B 789     6910   7233   7105   1896   1147    671       C  
-ATOM  11284  CG  GLN B 789     -30.654  30.249  42.100  1.00 55.33           C  
-ANISOU11284  CG  GLN B 789     6894   7224   6904   2063   1170    722       C  
-ATOM  11285  CD  GLN B 789     -31.227  30.223  40.696  1.00 54.94           C  
-ANISOU11285  CD  GLN B 789     6679   7390   6805   2109   1188    685       C  
-ATOM  11286  OE1 GLN B 789     -32.117  29.429  40.392  1.00 53.87           O  
-ANISOU11286  OE1 GLN B 789     6372   7436   6661   2071   1214    630       O  
-ATOM  11287  NE2 GLN B 789     -30.705  31.083  39.828  1.00 54.62           N  
-ANISOU11287  NE2 GLN B 789     6690   7337   6728   2185   1178    708       N  
-ATOM  11288  N   LEU B 790     -27.110  28.695  42.904  1.00 52.86           N  
-ANISOU11288  N   LEU B 790     6738   6417   6930   1719   1012    668       N  
-ATOM  11289  CA  LEU B 790     -25.828  29.377  43.004  1.00 51.17           C  
-ANISOU11289  CA  LEU B 790     6663   6042   6738   1712    967    683       C  
-ATOM  11290  C   LEU B 790     -24.987  29.044  41.774  1.00 50.47           C  
-ANISOU11290  C   LEU B 790     6497   5949   6730   1643    931    625       C  
-ATOM  11291  O   LEU B 790     -24.235  29.877  41.274  1.00 49.11           O  
-ANISOU11291  O   LEU B 790     6405   5715   6540   1670    915    625       O  
-ATOM  11292  CB  LEU B 790     -25.085  28.977  44.278  1.00 49.23           C  
-ANISOU11292  CB  LEU B 790     6514   5641   6550   1640    928    703       C  
-ATOM  11293  CG  LEU B 790     -23.719  29.647  44.443  1.00 47.52           C  
-ANISOU11293  CG  LEU B 790     6429   5275   6350   1619    881    705       C  
-ATOM  11294  CD1 LEU B 790     -23.881  31.156  44.468  1.00 47.93           C  
-ANISOU11294  CD1 LEU B 790     6615   5315   6283   1729    923    739       C  
-ATOM  11295  CD2 LEU B 790     -23.015  29.169  45.696  1.00 49.21           C  
-ANISOU11295  CD2 LEU B 790     6715   5370   6611   1551    838    724       C  
-ATOM  11296  N   VAL B 791     -25.124  27.816  41.289  1.00 60.62           N  
-ANISOU11296  N   VAL B 791     7630   7297   8104   1547    927    572       N  
-ATOM  11297  CA  VAL B 791     -24.413  27.393  40.097  1.00 60.59           C  
-ANISOU11297  CA  VAL B 791     7538   7302   8183   1472    900    510       C  
-ATOM  11298  C   VAL B 791     -24.848  28.234  38.907  1.00 61.05           C  
-ANISOU11298  C   VAL B 791     7554   7492   8150   1560    924    503       C  
-ATOM  11299  O   VAL B 791     -24.018  28.806  38.204  1.00 60.70           O  
-ANISOU11299  O   VAL B 791     7558   7393   8114   1564    899    491       O  
-ATOM  11300  CB  VAL B 791     -24.664  25.912  39.788  1.00 61.44           C  
-ANISOU11300  CB  VAL B 791     7483   7467   8394   1354    916    448       C  
-ATOM  11301  CG1 VAL B 791     -24.125  25.566  38.412  1.00 62.12           C  
-ANISOU11301  CG1 VAL B 791     7461   7594   8548   1284    902    378       C  
-ATOM  11302  CG2 VAL B 791     -24.030  25.038  40.857  1.00 61.26           C  
-ANISOU11302  CG2 VAL B 791     7511   7292   8472   1271    894    462       C  
-ATOM  11303  N   LEU B 792     -26.155  28.316  38.689  1.00 46.28           N  
-ANISOU11303  N   LEU B 792     5593   5802   6188   1635    976    511       N  
-ATOM  11304  CA  LEU B 792     -26.687  29.118  37.594  1.00 47.69           C  
-ANISOU11304  CA  LEU B 792     5725   6133   6261   1743   1003    517       C  
-ATOM  11305  C   LEU B 792     -26.165  30.548  37.638  1.00 51.03           C  
-ANISOU11305  C   LEU B 792     6330   6451   6607   1857   1004    579       C  
-ATOM  11306  O   LEU B 792     -25.898  31.147  36.599  1.00 52.44           O  
-ANISOU11306  O   LEU B 792     6510   6666   6749   1904   1009    575       O  
-ATOM  11307  CB  LEU B 792     -28.215  29.122  37.621  1.00 43.98           C  
-ANISOU11307  CB  LEU B 792     5150   5877   5683   1832   1059    530       C  
-ATOM  11308  CG  LEU B 792     -28.882  27.809  37.224  1.00 42.04           C  
-ANISOU11308  CG  LEU B 792     4697   5790   5488   1722   1080    448       C  
-ATOM  11309  CD1 LEU B 792     -30.386  27.980  37.167  1.00 41.27           C  
-ANISOU11309  CD1 LEU B 792     4491   5929   5261   1821   1136    453       C  
-ATOM  11310  CD2 LEU B 792     -28.352  27.349  35.884  1.00 41.09           C  
-ANISOU11310  CD2 LEU B 792     4456   5729   5427   1637   1061    376       C  
-ATOM  11311  N   ASP B 793     -26.016  31.087  38.843  1.00 67.29           N  
-ANISOU11311  N   ASP B 793     8547   8378   8642   1894   1010    632       N  
-ATOM  11312  CA  ASP B 793     -25.574  32.466  39.014  1.00 71.86           C  
-ANISOU11312  CA  ASP B 793     9313   8848   9144   1992   1033    684       C  
-ATOM  11313  C   ASP B 793     -24.065  32.594  38.851  1.00 72.86           C  
-ANISOU11313  C   ASP B 793     9530   8799   9353   1898    988    648       C  
-ATOM  11314  O   ASP B 793     -23.567  33.627  38.402  1.00 73.98           O  
-ANISOU11314  O   ASP B 793     9787   8878   9444   1955   1013    661       O  
-ATOM  11315  CB  ASP B 793     -26.005  33.001  40.383  1.00 73.82           C  
-ANISOU11315  CB  ASP B 793     9691   9028   9330   2056   1066    744       C  
-ATOM  11316  CG  ASP B 793     -27.483  33.344  40.438  1.00 76.34           C  
-ANISOU11316  CG  ASP B 793     9958   9515   9533   2194   1129    791       C  
-ATOM  11317  OD1 ASP B 793     -28.241  32.855  39.574  1.00 76.72           O  
-ANISOU11317  OD1 ASP B 793     9837   9753   9562   2214   1136    766       O  
-ATOM  11318  OD2 ASP B 793     -27.889  34.100  41.348  1.00 77.99           O  
-ANISOU11318  OD2 ASP B 793    10291   9676   9667   2280   1174    848       O  
-ATOM  11319  N   CYS B 794     -23.342  31.545  39.224  1.00 74.20           N  
-ANISOU11319  N   CYS B 794     9653   8893   9647   1757    928    602       N  
-ATOM  11320  CA  CYS B 794     -21.889  31.547  39.113  1.00 75.34           C  
-ANISOU11320  CA  CYS B 794     9863   8887   9875   1661    877    560       C  
-ATOM  11321  C   CYS B 794     -21.425  31.343  37.675  1.00 75.41           C  
-ANISOU11321  C   CYS B 794     9779   8941   9931   1616    861    503       C  
-ATOM  11322  O   CYS B 794     -20.463  31.970  37.231  1.00 75.25           O  
-ANISOU11322  O   CYS B 794     9846   8828   9918   1599    852    480       O  
-ATOM  11323  CB  CYS B 794     -21.269  30.491  40.032  1.00 75.66           C  
-ANISOU11323  CB  CYS B 794     9884   8837  10026   1543    821    541       C  
-ATOM  11324  SG  CYS B 794     -21.086  31.017  41.754  1.00 77.16           S  
-ANISOU11324  SG  CYS B 794    10244   8907  10166   1566    820    595       S  
-ATOM  11325  N   SER B 795     -22.114  30.468  36.951  1.00 74.11           N  
-ANISOU11325  N   SER B 795     9438   8924   9797   1590    864    474       N  
-ATOM  11326  CA  SER B 795     -21.782  30.217  35.557  1.00 73.64           C  
-ANISOU11326  CA  SER B 795     9272   8930   9776   1543    853    416       C  
-ATOM  11327  C   SER B 795     -22.039  31.464  34.715  1.00 74.40           C  
-ANISOU11327  C   SER B 795     9432   9085   9750   1670    897    449       C  
-ATOM  11328  O   SER B 795     -21.288  31.762  33.786  1.00 75.01           O  
-ANISOU11328  O   SER B 795     9525   9130   9847   1642    887    414       O  
-ATOM  11329  CB  SER B 795     -22.580  29.032  35.013  1.00 73.99           C  
-ANISOU11329  CB  SER B 795     9109   9139   9865   1483    862    371       C  
-ATOM  11330  OG  SER B 795     -23.959  29.338  34.955  1.00 75.81           O  
-ANISOU11330  OG  SER B 795     9282   9548   9975   1596    913    409       O  
-ATOM  11331  N   ALA B 796     -23.101  32.194  35.048  1.00 63.61           N  
-ANISOU11331  N   ALA B 796     8109   7804   8256   1815    951    519       N  
-ATOM  11332  CA  ALA B 796     -23.418  33.439  34.356  1.00 63.30           C  
-ANISOU11332  CA  ALA B 796     8150   7815   8088   1964   1008    569       C  
-ATOM  11333  C   ALA B 796     -22.316  34.472  34.567  1.00 62.96           C  
-ANISOU11333  C   ALA B 796     8316   7568   8037   1969   1023    578       C  
-ATOM  11334  O   ALA B 796     -21.800  35.050  33.610  1.00 63.42           O  
-ANISOU11334  O   ALA B 796     8419   7606   8073   1988   1041    565       O  
-ATOM  11335  CB  ALA B 796     -24.748  33.982  34.830  1.00 64.14           C  
-ANISOU11335  CB  ALA B 796     8267   8040   8065   2123   1068    646       C  
-ATOM  11336  N   GLU B 797     -21.962  34.705  35.827  1.00 71.81           N  
-ANISOU11336  N   GLU B 797     9567   8546   9172   1947   1021    596       N  
-ATOM  11337  CA  GLU B 797     -20.875  35.619  36.154  1.00 72.32           C  
-ANISOU11337  CA  GLU B 797     9826   8422   9231   1926   1040    586       C  
-ATOM  11338  C   GLU B 797     -19.566  35.125  35.554  1.00 68.31           C  
-ANISOU11338  C   GLU B 797     9286   7832   8837   1779    978    500       C  
-ATOM  11339  O   GLU B 797     -18.629  35.896  35.366  1.00 67.75           O  
-ANISOU11339  O   GLU B 797     9348   7636   8757   1755   1000    473       O  
-ATOM  11340  CB  GLU B 797     -20.738  35.776  37.668  1.00 76.01           C  
-ANISOU11340  CB  GLU B 797    10407   8777   9696   1906   1040    607       C  
-ATOM  11341  CG  GLU B 797     -21.825  36.629  38.302  1.00 84.45           C  
-ANISOU11341  CG  GLU B 797    11567   9880  10640   2058   1122    691       C  
-ATOM  11342  CD  GLU B 797     -21.681  38.101  37.965  1.00 89.06           C  
-ANISOU11342  CD  GLU B 797    12333  10386  11118   2168   1221    725       C  
-ATOM  11343  OE1 GLU B 797     -20.839  38.776  38.595  1.00 90.69           O  
-ANISOU11343  OE1 GLU B 797    12707  10431  11321   2121   1250    704       O  
-ATOM  11344  OE2 GLU B 797     -22.407  38.585  37.069  1.00 91.21           O  
-ANISOU11344  OE2 GLU B 797    12584  10764  11309   2301   1277    771       O  
-ATOM  11345  N   TRP B 798     -19.510  33.830  35.261  1.00 66.22           N  
-ANISOU11345  N   TRP B 798     8845   7635   8680   1675    910    453       N  
-ATOM  11346  CA  TRP B 798     -18.354  33.246  34.600  1.00 60.95           C  
-ANISOU11346  CA  TRP B 798     8123   6908   8129   1539    853    371       C  
-ATOM  11347  C   TRP B 798     -18.316  33.688  33.136  1.00 62.28           C  
-ANISOU11347  C   TRP B 798     8262   7141   8259   1572    882    351       C  
-ATOM  11348  O   TRP B 798     -17.295  34.175  32.655  1.00 61.33           O  
-ANISOU11348  O   TRP B 798     8226   6918   8159   1524    882    306       O  
-ATOM  11349  CB  TRP B 798     -18.381  31.717  34.720  1.00 54.43           C  
-ANISOU11349  CB  TRP B 798     7122   6130   7428   1427    791    331       C  
-ATOM  11350  CG  TRP B 798     -17.327  31.023  33.920  1.00 44.49           C  
-ANISOU11350  CG  TRP B 798     5783   4830   6292   1295    740    248       C  
-ATOM  11351  CD1 TRP B 798     -17.515  30.224  32.828  1.00 42.18           C  
-ANISOU11351  CD1 TRP B 798     5325   4642   6058   1238    731    199       C  
-ATOM  11352  CD2 TRP B 798     -15.914  31.070  34.144  1.00 39.07           C  
-ANISOU11352  CD2 TRP B 798     5172   3991   5681   1200    696    196       C  
-ATOM  11353  NE1 TRP B 798     -16.305  29.770  32.359  1.00 39.08           N  
-ANISOU11353  NE1 TRP B 798     4907   4161   5780   1116    686    125       N  
-ATOM  11354  CE2 TRP B 798     -15.306  30.275  33.150  1.00 37.23           C  
-ANISOU11354  CE2 TRP B 798     4815   3772   5557   1094    660    122       C  
-ATOM  11355  CE3 TRP B 798     -15.103  31.706  35.089  1.00 37.08           C  
-ANISOU11355  CE3 TRP B 798     5072   3604   5411   1190    685    198       C  
-ATOM  11356  CZ2 TRP B 798     -13.929  30.099  33.073  1.00 35.23           C  
-ANISOU11356  CZ2 TRP B 798     4587   3402   5397    988    612     54       C  
-ATOM  11357  CZ3 TRP B 798     -13.733  31.529  35.013  1.00 36.48           C  
-ANISOU11357  CZ3 TRP B 798     5014   3425   5420   1081    636    126       C  
-ATOM  11358  CH2 TRP B 798     -13.160  30.732  34.010  1.00 35.20           C  
-ANISOU11358  CH2 TRP B 798     4727   3279   5369    986    598     57       C  
-ATOM  11359  N   LEU B 799     -19.435  33.538  32.436  1.00 53.35           N  
-ANISOU11359  N   LEU B 799     7014   6191   7067   1654    909    381       N  
-ATOM  11360  CA  LEU B 799     -19.487  33.904  31.027  1.00 55.96           C  
-ANISOU11360  CA  LEU B 799     7301   6611   7349   1694    935    369       C  
-ATOM  11361  C   LEU B 799     -19.366  35.406  30.823  1.00 61.23           C  
-ANISOU11361  C   LEU B 799     8164   7206   7896   1822   1011    423       C  
-ATOM  11362  O   LEU B 799     -18.975  35.856  29.754  1.00 62.97           O  
-ANISOU11362  O   LEU B 799     8406   7429   8090   1834   1034    405       O  
-ATOM  11363  CB  LEU B 799     -20.765  33.383  30.370  1.00 51.19           C  
-ANISOU11363  CB  LEU B 799     6510   6247   6692   1756    947    387       C  
-ATOM  11364  CG  LEU B 799     -20.948  31.863  30.358  1.00 46.95           C  
-ANISOU11364  CG  LEU B 799     5770   5796   6271   1619    895    320       C  
-ATOM  11365  CD1 LEU B 799     -21.983  31.474  29.312  1.00 44.08           C  
-ANISOU11365  CD1 LEU B 799     5216   5685   5847   1656    916    308       C  
-ATOM  11366  CD2 LEU B 799     -19.632  31.144  30.102  1.00 40.35           C  
-ANISOU11366  CD2 LEU B 799     4912   4830   5591   1445    838    233       C  
-ATOM  11367  N   ASP B 800     -19.700  36.188  31.839  1.00 94.04           N  
-ANISOU11367  N   ASP B 800    12466  11289  11976   1916   1061    487       N  
-ATOM  11368  CA  ASP B 800     -19.504  37.627  31.738  1.00 99.09           C  
-ANISOU11368  CA  ASP B 800    13314  11827  12508   2027   1153    533       C  
-ATOM  11369  C   ASP B 800     -18.178  38.036  32.356  1.00 95.32           C  
-ANISOU11369  C   ASP B 800    13001  11130  12087   1916   1153    476       C  
-ATOM  11370  O   ASP B 800     -17.908  39.220  32.548  1.00 95.95           O  
-ANISOU11370  O   ASP B 800    13278  11090  12087   1979   1242    500       O  
-ATOM  11371  CB  ASP B 800     -20.666  38.398  32.360  1.00111.72           C  
-ANISOU11371  CB  ASP B 800    14992  13478  13977   2208   1233    636       C  
-ATOM  11372  CG  ASP B 800     -21.825  38.571  31.397  1.00122.43           C  
-ANISOU11372  CG  ASP B 800    16246  15047  15226   2368   1271    701       C  
-ATOM  11373  OD1 ASP B 800     -21.749  39.466  30.525  1.00127.83           O  
-ANISOU11373  OD1 ASP B 800    17019  15726  15824   2470   1341    737       O  
-ATOM  11374  OD2 ASP B 800     -22.809  37.809  31.508  1.00131.10           O  
-ANISOU11374  OD2 ASP B 800    17172  16322  16318   2391   1236    715       O  
-ATOM  11375  N   PHE B 801     -17.355  37.042  32.663  1.00 70.33           N  
-ANISOU11375  N   PHE B 801     9749   7917   9055   1749   1060    397       N  
-ATOM  11376  CA  PHE B 801     -16.002  37.288  33.128  1.00 64.95           C  
-ANISOU11376  CA  PHE B 801     9186   7060   8433   1628   1044    326       C  
-ATOM  11377  C   PHE B 801     -15.037  36.975  31.998  1.00 63.50           C  
-ANISOU11377  C   PHE B 801     8944   6855   8327   1520   1008    241       C  
-ATOM  11378  O   PHE B 801     -13.984  37.593  31.881  1.00 62.97           O  
-ANISOU11378  O   PHE B 801     9002   6658   8266   1455   1033    182       O  
-ATOM  11379  CB  PHE B 801     -15.692  36.435  34.353  1.00 59.04           C  
-ANISOU11379  CB  PHE B 801     8389   6273   7771   1530    967    303       C  
-ATOM  11380  CG  PHE B 801     -14.229  36.304  34.643  1.00 51.83           C  
-ANISOU11380  CG  PHE B 801     7522   5229   6941   1382    919    212       C  
-ATOM  11381  CD1 PHE B 801     -13.562  37.279  35.361  1.00 48.22           C  
-ANISOU11381  CD1 PHE B 801     7248   4644   6430   1366    968    190       C  
-ATOM  11382  CD2 PHE B 801     -13.521  35.200  34.203  1.00 49.57           C  
-ANISOU11382  CD2 PHE B 801     7091   4957   6785   1258    830    143       C  
-ATOM  11383  CE1 PHE B 801     -12.215  37.158  35.632  1.00 46.46           C  
-ANISOU11383  CE1 PHE B 801     7053   4326   6274   1228    923     98       C  
-ATOM  11384  CE2 PHE B 801     -12.175  35.073  34.468  1.00 46.13           C  
-ANISOU11384  CE2 PHE B 801     6687   4418   6423   1132    783     60       C  
-ATOM  11385  CZ  PHE B 801     -11.519  36.056  35.181  1.00 46.06           C  
-ANISOU11385  CZ  PHE B 801     6851   4298   6350   1117    826     35       C  
-ATOM  11386  N   LEU B 802     -15.407  36.005  31.170  1.00 56.73           N  
-ANISOU11386  N   LEU B 802     7896   6131   7529   1492    955    226       N  
-ATOM  11387  CA  LEU B 802     -14.685  35.727  29.939  1.00 54.77           C  
-ANISOU11387  CA  LEU B 802     7580   5888   7342   1405    931    153       C  
-ATOM  11388  C   LEU B 802     -14.959  36.853  28.956  1.00 58.00           C  
-ANISOU11388  C   LEU B 802     8090   6317   7630   1521   1021    191       C  
-ATOM  11389  O   LEU B 802     -14.082  37.259  28.189  1.00 58.34           O  
-ANISOU11389  O   LEU B 802     8198   6283   7686   1464   1040    133       O  
-ATOM  11390  CB  LEU B 802     -15.140  34.396  29.341  1.00 51.17           C  
-ANISOU11390  CB  LEU B 802     6889   5581   6971   1347    866    129       C  
-ATOM  11391  CG  LEU B 802     -14.965  33.169  30.237  1.00 45.48           C  
-ANISOU11391  CG  LEU B 802     6063   4845   6374   1242    790    101       C  
-ATOM  11392  CD1 LEU B 802     -15.409  31.904  29.525  1.00 41.55           C  
-ANISOU11392  CD1 LEU B 802     5344   4485   5958   1176    754     66       C  
-ATOM  11393  CD2 LEU B 802     -13.524  33.058  30.687  1.00 43.30           C  
-ANISOU11393  CD2 LEU B 802     5853   4406   6194   1116    744     28       C  
-ATOM  11394  N   GLU B 803     -16.190  37.354  28.981  1.00 57.98           N  
-ANISOU11394  N   GLU B 803     8102   6421   7506   1690   1081    290       N  
-ATOM  11395  CA  GLU B 803     -16.582  38.457  28.115  1.00 61.03           C  
-ANISOU11395  CA  GLU B 803     8592   6838   7760   1835   1178    349       C  
-ATOM  11396  C   GLU B 803     -15.658  39.649  28.339  1.00 60.40           C  
-ANISOU11396  C   GLU B 803     8758   6549   7641   1830   1262    331       C  
-ATOM  11397  O   GLU B 803     -15.053  40.158  27.404  1.00 60.93           O  
-ANISOU11397  O   GLU B 803     8897   6564   7690   1814   1305    298       O  
-ATOM  11398  CB  GLU B 803     -18.035  38.850  28.374  1.00 64.00           C  
-ANISOU11398  CB  GLU B 803     8959   7350   8008   2031   1233    465       C  
-ATOM  11399  CG  GLU B 803     -18.599  39.838  27.376  1.00 71.42           C  
-ANISOU11399  CG  GLU B 803     9969   8365   8804   2208   1329    543       C  
-ATOM  11400  CD  GLU B 803     -18.533  39.337  25.940  1.00 74.32           C  
-ANISOU11400  CD  GLU B 803    10182   8871   9184   2173   1291    506       C  
-ATOM  11401  OE1 GLU B 803     -17.856  39.986  25.113  1.00 75.97           O  
-ANISOU11401  OE1 GLU B 803    10499   9001   9366   2172   1341    489       O  
-ATOM  11402  OE2 GLU B 803     -19.161  38.301  25.632  1.00 76.43           O  
-ANISOU11402  OE2 GLU B 803    10225   9330   9486   2140   1220    488       O  
-ATOM  11403  N   LYS B 804     -15.540  40.080  29.590  1.00 72.29           N  
-ANISOU11403  N   LYS B 804    10395   7939   9134   1831   1291    344       N  
-ATOM  11404  CA  LYS B 804     -14.634  41.165  29.945  1.00 72.52           C  
-ANISOU11404  CA  LYS B 804    10655   7770   9129   1800   1379    308       C  
-ATOM  11405  C   LYS B 804     -13.200  40.837  29.540  1.00 69.11           C  
-ANISOU11405  C   LYS B 804    10215   7240   8804   1611   1327    179       C  
-ATOM  11406  O   LYS B 804     -12.394  41.733  29.314  1.00 68.00           O  
-ANISOU11406  O   LYS B 804    10246   6961   8630   1576   1409    131       O  
-ATOM  11407  CB  LYS B 804     -14.696  41.454  31.451  1.00 76.36           C  
-ANISOU11407  CB  LYS B 804    11245   8170   9600   1798   1399    323       C  
-ATOM  11408  CG  LYS B 804     -16.080  41.780  31.972  1.00 83.70           C  
-ANISOU11408  CG  LYS B 804    12188   9186  10430   1977   1452    444       C  
-ATOM  11409  CD  LYS B 804     -16.026  42.240  33.420  1.00 89.31           C  
-ANISOU11409  CD  LYS B 804    13032   9786  11115   1966   1491    451       C  
-ATOM  11410  CE  LYS B 804     -17.404  42.201  34.076  1.00 93.80           C  
-ANISOU11410  CE  LYS B 804    13560  10462  11617   2112   1508    557       C  
-ATOM  11411  NZ  LYS B 804     -18.379  43.132  33.443  1.00 95.47           N  
-ANISOU11411  NZ  LYS B 804    13850  10728  11696   2322   1626    661       N  
-ATOM  11412  N   PHE B 805     -12.880  39.552  29.454  1.00 65.99           N  
-ANISOU11412  N   PHE B 805     9624   6914   8536   1487   1199    120       N  
-ATOM  11413  CA  PHE B 805     -11.517  39.143  29.152  1.00 63.60           C  
-ANISOU11413  CA  PHE B 805     9296   6527   8344   1308   1142     -3       C  
-ATOM  11414  C   PHE B 805     -11.212  39.196  27.648  1.00 66.15           C  
-ANISOU11414  C   PHE B 805     9582   6879   8672   1288   1157    -40       C  
-ATOM  11415  O   PHE B 805     -10.086  39.494  27.243  1.00 66.02           O  
-ANISOU11415  O   PHE B 805     9638   6754   8691   1179   1171   -134       O  
-ATOM  11416  CB  PHE B 805     -11.254  37.749  29.712  1.00 56.94           C  
-ANISOU11416  CB  PHE B 805     8268   5730   7636   1192   1010    -46       C  
-ATOM  11417  CG  PHE B 805      -9.829  37.297  29.578  1.00 51.21           C  
-ANISOU11417  CG  PHE B 805     7512   4919   7025   1017    947   -169       C  
-ATOM  11418  CD1 PHE B 805      -8.900  37.601  30.557  1.00 49.20           C  
-ANISOU11418  CD1 PHE B 805     7360   4550   6785    934    942   -228       C  
-ATOM  11419  CD2 PHE B 805      -9.420  36.556  28.480  1.00 48.37           C  
-ANISOU11419  CD2 PHE B 805     7014   4607   6757    933    894   -230       C  
-ATOM  11420  CE1 PHE B 805      -7.586  37.174  30.445  1.00 46.96           C  
-ANISOU11420  CE1 PHE B 805     7036   4207   6601    780    880   -344       C  
-ATOM  11421  CE2 PHE B 805      -8.109  36.135  28.356  1.00 45.53           C  
-ANISOU11421  CE2 PHE B 805     6623   4172   6504    777    838   -344       C  
-ATOM  11422  CZ  PHE B 805      -7.190  36.442  29.340  1.00 45.56           C  
-ANISOU11422  CZ  PHE B 805     6723   4069   6518    705    829   -400       C  
-ATOM  11423  N   SER B 806     -12.218  38.914  26.826  1.00 64.79           N  
-ANISOU11423  N   SER B 806     8753   8017   7849   1129    768   -340       N  
-ATOM  11424  CA  SER B 806     -12.052  38.935  25.376  1.00 66.83           C  
-ANISOU11424  CA  SER B 806     9228   7892   8271   1147    806   -188       C  
-ATOM  11425  C   SER B 806     -11.586  40.304  24.890  1.00 71.73           C  
-ANISOU11425  C   SER B 806    10053   8137   9066   1160    949   -405       C  
-ATOM  11426  O   SER B 806     -11.074  40.438  23.783  1.00 71.02           O  
-ANISOU11426  O   SER B 806    10143   7719   9122   1116    995   -333       O  
-ATOM  11427  CB  SER B 806     -13.362  38.562  24.677  1.00 66.73           C  
-ANISOU11427  CB  SER B 806     9263   7868   8225   1307    759     49       C  
-ATOM  11428  OG  SER B 806     -14.138  39.718  24.398  1.00 68.39           O  
-ANISOU11428  OG  SER B 806     9601   7885   8499   1471    852    -76       O  
-ATOM  11429  N   GLU B 807     -11.779  41.322  25.720  1.00 75.70           N  
-ANISOU11429  N   GLU B 807    10529   8691   9544   1216   1011   -669       N  
-ATOM  11430  CA  GLU B 807     -11.334  42.668  25.392  1.00 80.94           C  
-ANISOU11430  CA  GLU B 807    11388   9008  10358   1220   1129   -893       C  
-ATOM  11431  C   GLU B 807      -9.833  42.691  25.127  1.00 78.31           C  
-ANISOU11431  C   GLU B 807    11117   8509  10127   1011   1174   -957       C  
-ATOM  11432  O   GLU B 807      -9.341  43.529  24.376  1.00 78.90           O  
-ANISOU11432  O   GLU B 807    11401   8228  10349    972   1258  -1038       O  
-ATOM  11433  CB  GLU B 807     -11.672  43.638  26.526  1.00 91.66           C  
-ANISOU11433  CB  GLU B 807    12671  10505  11650   1300   1166  -1185       C  
-ATOM  11434  CG  GLU B 807     -13.120  43.595  26.981  1.00105.82           C  
-ANISOU11434  CG  GLU B 807    14354  12542  13310   1501   1117  -1158       C  
-ATOM  11435  CD  GLU B 807     -14.089  44.067  25.914  1.00114.61           C  
-ANISOU11435  CD  GLU B 807    15662  13374  14511   1683   1137  -1063       C  
-ATOM  11436  OE1 GLU B 807     -13.626  44.519  24.846  1.00119.92           O  
-ANISOU11436  OE1 GLU B 807    16569  13644  15353   1649   1192  -1031       O  
-ATOM  11437  OE2 GLU B 807     -15.315  43.986  26.145  1.00119.90           O  
-ANISOU11437  OE2 GLU B 807    16248  14234  15073   1856   1095  -1022       O  
-ATOM  11438  N   HIS B 808      -9.107  41.768  25.749  1.00 65.05           N  
-ANISOU11438  N   HIS B 808     9256   7096   8363    872   1111   -923       N  
-ATOM  11439  CA  HIS B 808      -7.656  41.736  25.621  1.00 61.87           C  
-ANISOU11439  CA  HIS B 808     8878   6592   8037    675   1146  -1004       C  
-ATOM  11440  C   HIS B 808      -7.186  40.587  24.738  1.00 57.94           C  
-ANISOU11440  C   HIS B 808     8386   6060   7568    594   1078   -753       C  
-ATOM  11441  O   HIS B 808      -5.987  40.337  24.619  1.00 55.97           O  
-ANISOU11441  O   HIS B 808     8125   5779   7363    434   1086   -796       O  
-ATOM  11442  CB  HIS B 808      -7.007  41.636  26.998  1.00 62.32           C  
-ANISOU11442  CB  HIS B 808     8733   6957   7989    569   1126  -1193       C  
-ATOM  11443  CG  HIS B 808      -7.398  42.741  27.925  1.00 63.59           C  
-ANISOU11443  CG  HIS B 808     8874   7171   8115    644   1188  -1456       C  
-ATOM  11444  ND1 HIS B 808      -7.073  44.060  27.688  1.00 64.77           N  
-ANISOU11444  ND1 HIS B 808     9206   7019   8386    641   1297  -1668       N  
-ATOM  11445  CD2 HIS B 808      -8.095  42.727  29.085  1.00 64.88           C  
-ANISOU11445  CD2 HIS B 808     8858   7661   8132    724   1147  -1545       C  
-ATOM  11446  CE1 HIS B 808      -7.549  44.810  28.665  1.00 66.51           C  
-ANISOU11446  CE1 HIS B 808     9363   7367   8541    729   1318  -1882       C  
-ATOM  11447  NE2 HIS B 808      -8.174  44.027  29.526  1.00 66.69           N  
-ANISOU11447  NE2 HIS B 808     9159   7779   8401    782   1234  -1816       N  
-ATOM  11448  N   TYR B 809      -8.131  39.897  24.111  1.00 72.07           N  
-ANISOU11448  N   TYR B 809    10193   7859   9331    710   1008   -498       N  
-ATOM  11449  CA  TYR B 809      -7.809  38.717  23.316  1.00 68.31           C  
-ANISOU11449  CA  TYR B 809     9712   7374   8867    656    921   -246       C  
-ATOM  11450  C   TYR B 809      -6.714  38.972  22.286  1.00 69.79           C  
-ANISOU11450  C   TYR B 809    10054   7255   9208    535    993   -267       C  
-ATOM  11451  O   TYR B 809      -5.670  38.321  22.304  1.00 67.03           O  
-ANISOU11451  O   TYR B 809     9628   6983   8856    399    950   -264       O  
-ATOM  11452  CB  TYR B 809      -9.062  38.193  22.624  1.00 63.72           C  
-ANISOU11452  CB  TYR B 809     9178   6772   8260    811    859     18       C  
-ATOM  11453  CG  TYR B 809      -8.821  37.043  21.677  1.00 57.21           C  
-ANISOU11453  CG  TYR B 809     8378   5897   7461    774    769    284       C  
-ATOM  11454  CD1 TYR B 809      -8.395  35.808  22.143  1.00 55.92           C  
-ANISOU11454  CD1 TYR B 809     8050   6003   7195    693    627    392       C  
-ATOM  11455  CD2 TYR B 809      -9.044  37.187  20.321  1.00 55.82           C  
-ANISOU11455  CD2 TYR B 809     8394   5406   7410    825    813    427       C  
-ATOM  11456  CE1 TYR B 809      -8.187  34.754  21.283  1.00 56.42           C  
-ANISOU11456  CE1 TYR B 809     8139   6017   7280    673    529    626       C  
-ATOM  11457  CE2 TYR B 809      -8.840  36.137  19.448  1.00 56.36           C  
-ANISOU11457  CE2 TYR B 809     8482   5433   7500    800    727    665       C  
-ATOM  11458  CZ  TYR B 809      -8.412  34.923  19.934  1.00 56.42           C  
-ANISOU11458  CZ  TYR B 809     8324   5708   7405    730    583    760       C  
-ATOM  11459  OH  TYR B 809      -8.209  33.879  19.058  1.00 57.13           O  
-ANISOU11459  OH  TYR B 809     8440   5750   7518    717    484    988       O  
-ATOM  11460  N   HIS B 810      -6.948  39.925  21.393  1.00 75.08           N  
-ANISOU11460  N   HIS B 810    10939   7584  10005    581   1097   -294       N  
-ATOM  11461  CA  HIS B 810      -5.985  40.204  20.334  1.00 77.83           C  
-ANISOU11461  CA  HIS B 810    11443   7640  10489    456   1168   -301       C  
-ATOM  11462  C   HIS B 810      -4.674  40.732  20.881  1.00 76.00           C  
-ANISOU11462  C   HIS B 810    11178   7421  10279    276   1233   -553       C  
-ATOM  11463  O   HIS B 810      -3.600  40.400  20.384  1.00 74.47           O  
-ANISOU11463  O   HIS B 810    10988   7175  10132    130   1241   -548       O  
-ATOM  11464  CB  HIS B 810      -6.574  41.155  19.295  1.00 86.73           C  
-ANISOU11464  CB  HIS B 810    12819   8397  11738    536   1255   -274       C  
-ATOM  11465  CG  HIS B 810      -7.600  40.509  18.421  1.00 93.71           C  
-ANISOU11465  CG  HIS B 810    13759   9219  12626    677   1197      6       C  
-ATOM  11466  ND1 HIS B 810      -8.953  40.723  18.576  1.00 98.20           N  
-ANISOU11466  ND1 HIS B 810    14345   9814  13152    868   1177     67       N  
-ATOM  11467  CD2 HIS B 810      -7.473  39.627  17.403  1.00 96.03           C  
-ANISOU11467  CD2 HIS B 810    14087   9443  12957    657   1148    239       C  
-ATOM  11468  CE1 HIS B 810      -9.614  40.013  17.679  1.00 98.39           C  
-ANISOU11468  CE1 HIS B 810    14418   9778  13188    953   1123    331       C  
-ATOM  11469  NE2 HIS B 810      -8.739  39.338  16.955  1.00 98.23           N  
-ANISOU11469  NE2 HIS B 810    14412   9694  13218    829   1104    442       N  
-ATOM  11470  N   SER B 811      -4.763  41.555  21.912  1.00 78.66           N  
-ANISOU11470  N   SER B 811    11474   7838  10577    288   1279   -779       N  
-ATOM  11471  CA  SER B 811      -3.569  42.049  22.565  1.00 75.53           C  
-ANISOU11471  CA  SER B 811    11030   7482  10186    119   1336  -1024       C  
-ATOM  11472  C   SER B 811      -2.703  40.869  23.014  1.00 72.38           C  
-ANISOU11472  C   SER B 811    10426   7365   9709      7   1246   -981       C  
-ATOM  11473  O   SER B 811      -1.478  40.919  22.927  1.00 70.88           O  
-ANISOU11473  O   SER B 811    10226   7149   9556   -160   1282  -1091       O  
-ATOM  11474  CB  SER B 811      -3.950  42.937  23.752  1.00 77.35           C  
-ANISOU11474  CB  SER B 811    11212   7815  10361    177   1372  -1255       C  
-ATOM  11475  OG  SER B 811      -2.809  43.537  24.335  1.00 77.75           O  
-ANISOU11475  OG  SER B 811    11242   7872  10428     12   1436  -1500       O  
-ATOM  11476  N   LEU B 812      -3.349  39.803  23.476  1.00 47.77           N  
-ANISOU11476  N   LEU B 812     7151   4520   6480     96   1120   -819       N  
-ATOM  11477  CA  LEU B 812      -2.635  38.648  24.015  1.00 44.99           C  
-ANISOU11477  CA  LEU B 812     6606   4449   6040      6   1005   -777       C  
-ATOM  11478  C   LEU B 812      -2.168  37.689  22.921  1.00 42.73           C  
-ANISOU11478  C   LEU B 812     6351   4081   5802    -33    938   -576       C  
-ATOM  11479  O   LEU B 812      -1.117  37.054  23.047  1.00 42.49           O  
-ANISOU11479  O   LEU B 812     6221   4168   5756   -150    882   -611       O  
-ATOM  11480  CB  LEU B 812      -3.498  37.910  25.040  1.00 42.14           C  
-ANISOU11480  CB  LEU B 812     6064   4425   5523     97    882   -693       C  
-ATOM  11481  CG  LEU B 812      -3.829  38.688  26.317  1.00 43.13           C  
-ANISOU11481  CG  LEU B 812     6101   4715   5571    121    929   -911       C  
-ATOM  11482  CD1 LEU B 812      -4.897  37.979  27.146  1.00 39.52           C  
-ANISOU11482  CD1 LEU B 812     5483   4581   4952    222    810   -793       C  
-ATOM  11483  CD2 LEU B 812      -2.570  38.926  27.135  1.00 42.62           C  
-ANISOU11483  CD2 LEU B 812     5940   4758   5497    -42    960  -1148       C  
-ATOM  11484  N   CYS B 813      -2.948  37.576  21.850  1.00 77.78           N  
-ANISOU11484  N   CYS B 813    10927   8327  10299     72    937   -372       N  
-ATOM  11485  CA  CYS B 813      -2.519  36.794  20.696  1.00 73.31           C  
-ANISOU11485  CA  CYS B 813    10414   7649   9793     41    887   -193       C  
-ATOM  11486  C   CYS B 813      -1.221  37.359  20.130  1.00 74.22           C  
-ANISOU11486  C   CYS B 813    10606   7584  10009   -123    992   -352       C  
-ATOM  11487  O   CYS B 813      -0.280  36.614  19.868  1.00 73.03           O  
-ANISOU11487  O   CYS B 813    10380   7511   9856   -215    932   -335       O  
-ATOM  11488  CB  CYS B 813      -3.600  36.763  19.617  1.00 70.83           C  
-ANISOU11488  CB  CYS B 813    10253   7127   9534    179    892     34       C  
-ATOM  11489  SG  CYS B 813      -5.063  35.816  20.072  1.00 65.86           S  
-ANISOU11489  SG  CYS B 813     9521   6732   8771    354    743    274       S  
-ATOM  11490  N   LYS B 814      -1.174  38.676  19.948  1.00 60.42           N  
-ANISOU11490  N   LYS B 814     9009   5605   8342   -161   1140   -510       N  
-ATOM  11491  CA  LYS B 814       0.043  39.331  19.483  1.00 59.90           C  
-ANISOU11491  CA  LYS B 814     9022   5378   8358   -340   1245   -675       C  
-ATOM  11492  C   LYS B 814       1.234  38.886  20.320  1.00 57.50           C  
-ANISOU11492  C   LYS B 814     8531   5328   7989   -476   1205   -833       C  
-ATOM  11493  O   LYS B 814       2.277  38.517  19.785  1.00 56.81           O  
-ANISOU11493  O   LYS B 814     8418   5241   7928   -599   1202   -852       O  
-ATOM  11494  CB  LYS B 814      -0.081  40.856  19.553  1.00 65.93           C  
-ANISOU11494  CB  LYS B 814     9955   5908   9188   -372   1386   -860       C  
-ATOM  11495  CG  LYS B 814      -0.989  41.472  18.503  1.00 71.33           C  
-ANISOU11495  CG  LYS B 814    10868   6272   9964   -275   1440   -736       C  
-ATOM  11496  CD  LYS B 814      -0.485  42.851  18.089  1.00 77.37           C  
-ANISOU11496  CD  LYS B 814    11835   6739  10822   -401   1571   -912       C  
-ATOM  11497  CE  LYS B 814       0.879  42.756  17.397  1.00 81.09           C  
-ANISOU11497  CE  LYS B 814    12322   7155  11335   -620   1616   -958       C  
-ATOM  11498  NZ  LYS B 814       1.415  44.087  16.974  1.00 84.73           N  
-ANISOU11498  NZ  LYS B 814    12987   7333  11875   -775   1736  -1119       N  
-ATOM  11499  N   ALA B 815       1.073  38.932  21.636  1.00 54.25           N  
-ANISOU11499  N   ALA B 815     7983   5143   7488   -454   1174   -952       N  
-ATOM  11500  CA  ALA B 815       2.135  38.537  22.547  1.00 51.66           C  
-ANISOU11500  CA  ALA B 815     7472   5066   7091   -575   1130  -1109       C  
-ATOM  11501  C   ALA B 815       2.621  37.120  22.249  1.00 49.46           C  
-ANISOU11501  C   ALA B 815     7068   4954   6772   -584    983   -961       C  
-ATOM  11502  O   ALA B 815       3.819  36.846  22.302  1.00 49.32           O  
-ANISOU11502  O   ALA B 815     6965   5023   6750   -714    970  -1076       O  
-ATOM  11503  CB  ALA B 815       1.661  38.648  23.983  1.00 49.51           C  
-ANISOU11503  CB  ALA B 815     7067   5030   6716   -523   1096  -1213       C  
-ATOM  11504  N   VAL B 816       1.693  36.225  21.932  1.00 41.25           N  
-ANISOU11504  N   VAL B 816     6019   3958   5698   -444    863   -712       N  
-ATOM  11505  CA  VAL B 816       2.045  34.838  21.654  1.00 39.77           C  
-ANISOU11505  CA  VAL B 816     5725   3917   5467   -433    697   -557       C  
-ATOM  11506  C   VAL B 816       2.768  34.711  20.317  1.00 41.50           C  
-ANISOU11506  C   VAL B 816     6037   3947   5783   -494    732   -513       C  
-ATOM  11507  O   VAL B 816       3.757  33.987  20.201  1.00 40.00           O  
-ANISOU11507  O   VAL B 816     5748   3873   5578   -566    651   -547       O  
-ATOM  11508  CB  VAL B 816       0.797  33.918  21.668  1.00 35.56           C  
-ANISOU11508  CB  VAL B 816     5169   3478   4863   -273    551   -289       C  
-ATOM  11509  CG1 VAL B 816       1.170  32.496  21.280  1.00 32.23           C  
-ANISOU11509  CG1 VAL B 816     4667   3173   4405   -260    363   -123       C  
-ATOM  11510  CG2 VAL B 816       0.139  33.941  23.038  1.00 32.87           C  
-ANISOU11510  CG2 VAL B 816     4709   3376   4403   -231    502   -336       C  
-ATOM  11511  N   HIS B 817       2.277  35.423  19.308  1.00 62.14           N  
-ANISOU11511  N   HIS B 817     8840   6278   8493   -465    848   -443       N  
-ATOM  11512  CA  HIS B 817       2.907  35.407  17.994  1.00 63.53           C  
-ANISOU11512  CA  HIS B 817     9114   6267   8757   -534    895   -401       C  
-ATOM  11513  C   HIS B 817       4.338  35.926  18.073  1.00 64.57           C  
-ANISOU11513  C   HIS B 817     9206   6416   8910   -729    985   -651       C  
-ATOM  11514  O   HIS B 817       5.204  35.506  17.305  1.00 63.24           O  
-ANISOU11514  O   HIS B 817     9019   6243   8768   -807    970   -652       O  
-ATOM  11515  CB  HIS B 817       2.081  36.208  16.991  1.00 69.64           C  
-ANISOU11515  CB  HIS B 817    10108   6725   9626   -480   1009   -295       C  
-ATOM  11516  CG  HIS B 817       0.783  35.556  16.630  1.00 72.81           C  
-ANISOU11516  CG  HIS B 817    10551   7101  10014   -295    915    -25       C  
-ATOM  11517  ND1 HIS B 817      -0.395  36.259  16.497  1.00 76.50           N  
-ANISOU11517  ND1 HIS B 817    11156   7400  10512   -185    981     47       N  
-ATOM  11518  CD2 HIS B 817       0.478  34.261  16.376  1.00 74.19           C  
-ANISOU11518  CD2 HIS B 817    10649   7399  10142   -201    753    188       C  
-ATOM  11519  CE1 HIS B 817      -1.370  35.426  16.177  1.00 77.39           C  
-ANISOU11519  CE1 HIS B 817    11265   7544  10594    -37    873    295       C  
-ATOM  11520  NE2 HIS B 817      -0.866  34.207  16.097  1.00 76.47           N  
-ANISOU11520  NE2 HIS B 817    11026   7599  10431    -48    732    390       N  
-ATOM  11521  N   HIS B 818       4.585  36.832  19.014  1.00 47.69           N  
-ANISOU11521  N   HIS B 818     7051   4314   6754   -806   1076   -866       N  
-ATOM  11522  CA  HIS B 818       5.937  37.320  19.259  1.00 49.44           C  
-ANISOU11522  CA  HIS B 818     7220   4586   6979   -998   1155  -1113       C  
-ATOM  11523  C   HIS B 818       6.787  36.224  19.884  1.00 48.44           C  
-ANISOU11523  C   HIS B 818     6872   4764   6770  -1027   1016  -1166       C  
-ATOM  11524  O   HIS B 818       7.965  36.080  19.563  1.00 50.24           O  
-ANISOU11524  O   HIS B 818     7039   5047   7004  -1156   1028  -1283       O  
-ATOM  11525  CB  HIS B 818       5.923  38.563  20.147  1.00 52.65           C  
-ANISOU11525  CB  HIS B 818     7670   4949   7384  -1064   1276  -1326       C  
-ATOM  11526  CG  HIS B 818       5.422  39.789  19.459  1.00 56.68           C  
-ANISOU11526  CG  HIS B 818     8415   5135   7984  -1080   1416  -1331       C  
-ATOM  11527  ND1 HIS B 818       4.806  39.745  18.223  1.00 57.75           N  
-ANISOU11527  ND1 HIS B 818     8708   5044   8192  -1013   1428  -1133       N  
-ATOM  11528  CD2 HIS B 818       5.447  41.094  19.815  1.00 59.24           C  
-ANISOU11528  CD2 HIS B 818     8856   5313   8340  -1154   1539  -1509       C  
-ATOM  11529  CE1 HIS B 818       4.471  40.969  17.857  1.00 58.74           C  
-ANISOU11529  CE1 HIS B 818     9037   4895   8387  -1046   1549  -1188       C  
-ATOM  11530  NE2 HIS B 818       4.853  41.806  18.805  1.00 60.66           N  
-ANISOU11530  NE2 HIS B 818     9263   5178   8608  -1130   1613  -1417       N  
-ATOM  11531  N   LEU B 819       6.184  35.448  20.777  1.00 56.11           N  
-ANISOU11531  N   LEU B 819     7723   5938   7658   -910    876  -1082       N  
-ATOM  11532  CA  LEU B 819       6.864  34.299  21.357  1.00 54.52           C  
-ANISOU11532  CA  LEU B 819     7327   6014   7376   -917    708  -1101       C  
-ATOM  11533  C   LEU B 819       7.180  33.291  20.266  1.00 51.36           C  
-ANISOU11533  C   LEU B 819     6921   5595   6999   -880    600   -950       C  
-ATOM  11534  O   LEU B 819       8.279  32.738  20.218  1.00 50.98           O  
-ANISOU11534  O   LEU B 819     6759   5682   6930   -952    533  -1051       O  
-ATOM  11535  CB  LEU B 819       6.007  33.652  22.443  1.00 55.41           C  
-ANISOU11535  CB  LEU B 819     7335   6330   7388   -803    566  -1004       C  
-ATOM  11536  CG  LEU B 819       6.150  34.249  23.842  1.00 57.72           C  
-ANISOU11536  CG  LEU B 819     7535   6779   7617   -864    612  -1208       C  
-ATOM  11537  CD1 LEU B 819       5.097  33.692  24.780  1.00 59.30           C  
-ANISOU11537  CD1 LEU B 819     7654   7163   7715   -749    484  -1083       C  
-ATOM  11538  CD2 LEU B 819       7.543  33.986  24.379  1.00 57.88           C  
-ANISOU11538  CD2 LEU B 819     7406   6982   7603   -998    576  -1413       C  
-ATOM  11539  N   ALA B 820       6.211  33.060  19.385  1.00 41.73           N  
-ANISOU11539  N   ALA B 820     5824   4211   5821   -761    580   -715       N  
-ATOM  11540  CA  ALA B 820       6.409  32.150  18.263  1.00 40.13           C  
-ANISOU11540  CA  ALA B 820     5634   3967   5647   -714    482   -559       C  
-ATOM  11541  C   ALA B 820       7.615  32.575  17.433  1.00 40.57           C  
-ANISOU11541  C   ALA B 820     5708   3944   5763   -862    592   -715       C  
-ATOM  11542  O   ALA B 820       8.414  31.739  17.012  1.00 39.54           O  
-ANISOU11542  O   ALA B 820     5484   3921   5617   -874    488   -726       O  
-ATOM  11543  CB  ALA B 820       5.163  32.087  17.397  1.00 38.22           C  
-ANISOU11543  CB  ALA B 820     5545   3524   5453   -581    484   -300       C  
-ATOM  11544  N   THR B 821       7.750  33.879  17.218  1.00 48.74           N  
-ANISOU11544  N   THR B 821     6864   4798   6857   -977    794   -842       N  
-ATOM  11545  CA  THR B 821       8.857  34.400  16.428  1.00 50.44           C  
-ANISOU11545  CA  THR B 821     7109   4938   7118  -1146    912   -989       C  
-ATOM  11546  C   THR B 821      10.188  34.091  17.093  1.00 51.99           C  
-ANISOU11546  C   THR B 821     7115   5388   7251  -1261    869  -1216       C  
-ATOM  11547  O   THR B 821      11.111  33.589  16.452  1.00 53.50           O  
-ANISOU11547  O   THR B 821     7232   5658   7438  -1320    831  -1266       O  
-ATOM  11548  CB  THR B 821       8.748  35.919  16.209  1.00 51.86           C  
-ANISOU11548  CB  THR B 821     7466   4877   7362  -1267   1123  -1091       C  
-ATOM  11549  OG1 THR B 821       7.493  36.227  15.591  1.00 51.30           O  
-ANISOU11549  OG1 THR B 821     7576   4565   7352  -1150   1157   -887       O  
-ATOM  11550  CG2 THR B 821       9.883  36.403  15.315  1.00 51.28           C  
-ANISOU11550  CG2 THR B 821     7427   4737   7321  -1463   1234  -1221       C  
-ATOM  11551  N   VAL B 822      10.285  34.400  18.379  1.00 45.34           N  
-ANISOU11551  N   VAL B 822     6191   4681   6357  -1291    873  -1361       N  
-ATOM  11552  CA  VAL B 822      11.504  34.136  19.134  1.00 48.13           C  
-ANISOU11552  CA  VAL B 822     6360   5280   6646  -1396    830  -1582       C  
-ATOM  11553  C   VAL B 822      11.869  32.659  19.045  1.00 46.54           C  
-ANISOU11553  C   VAL B 822     6007   5282   6394  -1299    611  -1506       C  
-ATOM  11554  O   VAL B 822      13.041  32.306  18.917  1.00 48.27           O  
-ANISOU11554  O   VAL B 822     6104   5648   6587  -1382    575  -1656       O  
-ATOM  11555  CB  VAL B 822      11.349  34.549  20.617  1.00 49.30           C  
-ANISOU11555  CB  VAL B 822     6439   5553   6739  -1411    840  -1712       C  
-ATOM  11556  CG1 VAL B 822      12.527  34.061  21.441  1.00 49.70           C  
-ANISOU11556  CG1 VAL B 822     6287   5879   6717  -1492    759  -1912       C  
-ATOM  11557  CG2 VAL B 822      11.201  36.060  20.733  1.00 55.91           C  
-ANISOU11557  CG2 VAL B 822     7420   6199   7624  -1521   1050  -1836       C  
-ATOM  11558  N   ASP B 823      10.854  31.804  19.098  1.00 45.66           N  
-ANISOU11558  N   ASP B 823     5907   5178   6264  -1123    457  -1274       N  
-ATOM  11559  CA  ASP B 823      11.061  30.365  19.066  1.00 45.74           C  
-ANISOU11559  CA  ASP B 823     5796   5361   6223  -1016    219  -1178       C  
-ATOM  11560  C   ASP B 823      11.678  29.928  17.738  1.00 45.53           C  
-ANISOU11560  C   ASP B 823     5779   5280   6240  -1021    199  -1151       C  
-ATOM  11561  O   ASP B 823      12.576  29.082  17.702  1.00 44.90           O  
-ANISOU11561  O   ASP B 823     5562   5378   6121  -1015     59  -1234       O  
-ATOM  11562  CB  ASP B 823       9.735  29.642  19.302  1.00 42.20           C  
-ANISOU11562  CB  ASP B 823     5388   4902   5744   -842     70   -912       C  
-ATOM  11563  CG  ASP B 823       9.923  28.200  19.732  1.00 41.00           C  
-ANISOU11563  CG  ASP B 823     5100   4966   5511   -748   -207   -840       C  
-ATOM  11564  OD1 ASP B 823      11.060  27.814  20.089  1.00 40.17           O  
-ANISOU11564  OD1 ASP B 823     4854   5038   5369   -809   -285  -1022       O  
-ATOM  11565  OD2 ASP B 823       8.925  27.454  19.720  1.00 41.09           O  
-ANISOU11565  OD2 ASP B 823     5150   4970   5494   -614   -355   -600       O  
-ATOM  11566  N   CYS B 824      11.186  30.509  16.649  1.00 52.85           N  
-ANISOU11566  N   CYS B 824     6869   5965   7245  -1028    334  -1039       N  
-ATOM  11567  CA  CYS B 824      11.719  30.230  15.322  1.00 52.52           C  
-ANISOU11567  CA  CYS B 824     6850   5860   7246  -1048    342  -1013       C  
-ATOM  11568  C   CYS B 824      13.187  30.633  15.217  1.00 54.73           C  
-ANISOU11568  C   CYS B 824     7027   6259   7510  -1229    433  -1290       C  
-ATOM  11569  O   CYS B 824      14.035  29.819  14.851  1.00 55.91           O  
-ANISOU11569  O   CYS B 824     7049   6566   7628  -1217    316  -1356       O  
-ATOM  11570  CB  CYS B 824      10.891  30.943  14.254  1.00 52.69           C  
-ANISOU11570  CB  CYS B 824     7079   5588   7352  -1045    491   -852       C  
-ATOM  11571  SG  CYS B 824       9.206  30.313  14.116  1.00 50.92           S  
-ANISOU11571  SG  CYS B 824     6967   5237   7144   -821    371   -510       S  
-ATOM  11572  N   ILE B 825      13.485  31.887  15.546  1.00 45.70           N  
-ANISOU11572  N   ILE B 825     5937   5047   6381  -1397    633  -1455       N  
-ATOM  11573  CA  ILE B 825      14.864  32.361  15.516  1.00 49.41           C  
-ANISOU11573  CA  ILE B 825     6312   5638   6825  -1592    730  -1722       C  
-ATOM  11574  C   ILE B 825      15.777  31.416  16.289  1.00 51.57           C  
-ANISOU11574  C   ILE B 825     6358   6218   7017  -1563    559  -1871       C  
-ATOM  11575  O   ILE B 825      16.825  31.018  15.791  1.00 55.45           O  
-ANISOU11575  O   ILE B 825     6734   6854   7481  -1619    523  -2000       O  
-ATOM  11576  CB  ILE B 825      15.009  33.782  16.091  1.00 49.41           C  
-ANISOU11576  CB  ILE B 825     6392   5547   6836  -1768    935  -1885       C  
-ATOM  11577  CG1 ILE B 825      14.273  34.787  15.206  1.00 52.55           C  
-ANISOU11577  CG1 ILE B 825     7024   5628   7314  -1818   1101  -1767       C  
-ATOM  11578  CG2 ILE B 825      16.478  34.158  16.212  1.00 49.90           C  
-ANISOU11578  CG2 ILE B 825     6331   5778   6851  -1974   1012  -2166       C  
-ATOM  11579  CD1 ILE B 825      14.589  34.637  13.729  1.00 53.42           C  
-ANISOU11579  CD1 ILE B 825     7188   5652   7458  -1867   1133  -1696       C  
-ATOM  11580  N   PHE B 826      15.376  31.059  17.504  1.00 52.06           N  
-ANISOU11580  N   PHE B 826     6357   6388   7037  -1476    448  -1859       N  
-ATOM  11581  CA  PHE B 826      16.134  30.104  18.302  1.00 52.74           C  
-ANISOU11581  CA  PHE B 826     6241   6752   7045  -1435    258  -1979       C  
-ATOM  11582  C   PHE B 826      16.241  28.762  17.591  1.00 48.40           C  
-ANISOU11582  C   PHE B 826     5626   6279   6483  -1285     39  -1862       C  
-ATOM  11583  O   PHE B 826      17.272  28.097  17.659  1.00 46.98           O  
-ANISOU11583  O   PHE B 826     5287   6307   6255  -1288    -82  -2015       O  
-ATOM  11584  CB  PHE B 826      15.491  29.924  19.679  1.00 58.02           C  
-ANISOU11584  CB  PHE B 826     6876   7501   7668  -1363    166  -1941       C  
-ATOM  11585  CG  PHE B 826      15.907  30.964  20.679  1.00 64.58           C  
-ANISOU11585  CG  PHE B 826     7678   8382   8478  -1516    319  -2158       C  
-ATOM  11586  CD1 PHE B 826      15.287  32.200  20.714  1.00 66.27           C  
-ANISOU11586  CD1 PHE B 826     8044   8395   8740  -1589    524  -2149       C  
-ATOM  11587  CD2 PHE B 826      16.924  30.704  21.582  1.00 68.01           C  
-ANISOU11587  CD2 PHE B 826     7936   9060   8845  -1582    250  -2376       C  
-ATOM  11588  CE1 PHE B 826      15.672  33.157  21.630  1.00 67.61           C  
-ANISOU11588  CE1 PHE B 826     8192   8604   8891  -1725    656  -2352       C  
-ATOM  11589  CE2 PHE B 826      17.315  31.658  22.498  1.00 70.43           C  
-ANISOU11589  CE2 PHE B 826     8215   9412   9132  -1724    391  -2575       C  
-ATOM  11590  CZ  PHE B 826      16.688  32.887  22.523  1.00 70.22           C  
-ANISOU11590  CZ  PHE B 826     8345   9183   9154  -1796    594  -2563       C  
-ATOM  11591  N   SER B 827      15.174  28.366  16.909  1.00 46.81           N  
-ANISOU11591  N   SER B 827     5549   5911   6324  -1148    -18  -1595       N  
-ATOM  11592  CA  SER B 827      15.180  27.105  16.191  1.00 44.24           C  
-ANISOU11592  CA  SER B 827     5184   5635   5992   -997   -232  -1465       C  
-ATOM  11593  C   SER B 827      16.229  27.118  15.091  1.00 45.13           C  
-ANISOU11593  C   SER B 827     5242   5787   6120  -1073   -176  -1602       C  
-ATOM  11594  O   SER B 827      17.018  26.180  14.964  1.00 44.19           O  
-ANISOU11594  O   SER B 827     4980   5852   5957  -1011   -352  -1692       O  
-ATOM  11595  CB  SER B 827      13.810  26.812  15.593  1.00 41.04           C  
-ANISOU11595  CB  SER B 827     4938   5024   5633   -854   -275  -1151       C  
-ATOM  11596  OG  SER B 827      13.861  25.632  14.808  1.00 38.41           O  
-ANISOU11596  OG  SER B 827     4575   4723   5295   -715   -477  -1030       O  
-ATOM  11597  N   LEU B 828      16.232  28.181  14.292  1.00 46.44           N  
-ANISOU11597  N   LEU B 828     5522   5783   6341  -1209     62  -1620       N  
-ATOM  11598  CA  LEU B 828      17.217  28.331  13.228  1.00 47.20           C  
-ANISOU11598  CA  LEU B 828     5569   5924   6441  -1317    143  -1754       C  
-ATOM  11599  C   LEU B 828      18.626  28.414  13.806  1.00 51.21           C  
-ANISOU11599  C   LEU B 828     5885   6695   6878  -1446    149  -2068       C  
-ATOM  11600  O   LEU B 828      19.573  27.875  13.237  1.00 52.38           O  
-ANISOU11600  O   LEU B 828     5901   7011   6991  -1452     78  -2197       O  
-ATOM  11601  CB  LEU B 828      16.918  29.567  12.381  1.00 44.43           C  
-ANISOU11601  CB  LEU B 828     5395   5333   6154  -1469    400  -1713       C  
-ATOM  11602  CG  LEU B 828      15.566  29.571  11.663  1.00 39.96           C  
-ANISOU11602  CG  LEU B 828     5026   4494   5662  -1351    413  -1412       C  
-ATOM  11603  CD1 LEU B 828      15.441  30.802  10.780  1.00 40.47           C  
-ANISOU11603  CD1 LEU B 828     5260   4331   5785  -1519    656  -1401       C  
-ATOM  11604  CD2 LEU B 828      15.348  28.291  10.855  1.00 37.18           C  
-ANISOU11604  CD2 LEU B 828     4640   4174   5314  -1166    213  -1247       C  
-ATOM  11605  N   ALA B 829      18.760  29.092  14.939  1.00 53.02           N  
-ANISOU11605  N   ALA B 829     6094   6967   7084  -1546    232  -2197       N  
-ATOM  11606  CA  ALA B 829      20.039  29.155  15.634  1.00 58.25           C  
-ANISOU11606  CA  ALA B 829     6572   7884   7675  -1662    230  -2491       C  
-ATOM  11607  C   ALA B 829      20.513  27.744  15.957  1.00 59.23           C  
-ANISOU11607  C   ALA B 829     6519   8243   7743  -1496    -53  -2531       C  
-ATOM  11608  O   ALA B 829      21.699  27.442  15.865  1.00 61.77           O  
-ANISOU11608  O   ALA B 829     6673   8786   8011  -1545   -100  -2753       O  
-ATOM  11609  CB  ALA B 829      19.911  29.973  16.903  1.00 58.62           C  
-ANISOU11609  CB  ALA B 829     6636   7928   7709  -1758    331  -2584       C  
-ATOM  11610  N   LYS B 830      19.573  26.884  16.336  1.00 64.24           N  
-ANISOU11610  N   LYS B 830     7195   8830   8384  -1301   -250  -2318       N  
-ATOM  11611  CA  LYS B 830      19.880  25.491  16.620  1.00 64.18           C  
-ANISOU11611  CA  LYS B 830     7054   9007   8325  -1130   -551  -2321       C  
-ATOM  11612  C   LYS B 830      20.317  24.793  15.347  1.00 63.78           C  
-ANISOU11612  C   LYS B 830     6962   8990   8283  -1051   -643  -2312       C  
-ATOM  11613  O   LYS B 830      21.282  24.030  15.344  1.00 63.18           O  
-ANISOU11613  O   LYS B 830     6720   9132   8154   -999   -807  -2482       O  
-ATOM  11614  CB  LYS B 830      18.657  24.783  17.194  1.00 64.61           C  
-ANISOU11614  CB  LYS B 830     7192   8976   8380   -959   -736  -2059       C  
-ATOM  11615  CG  LYS B 830      18.211  25.295  18.545  1.00 67.09           C  
-ANISOU11615  CG  LYS B 830     7521   9302   8670  -1015   -687  -2070       C  
-ATOM  11616  CD  LYS B 830      19.163  24.868  19.637  1.00 69.34           C  
-ANISOU11616  CD  LYS B 830     7624   9845   8876  -1039   -825  -2291       C  
-ATOM  11617  CE  LYS B 830      18.502  25.014  20.997  1.00 71.08           C  
-ANISOU11617  CE  LYS B 830     7859  10087   9060  -1043   -856  -2237       C  
-ATOM  11618  NZ  LYS B 830      17.921  26.377  21.197  1.00 71.02           N  
-ANISOU11618  NZ  LYS B 830     7969   9919   9095  -1169   -574  -2227       N  
-ATOM  11619  N   VAL B 831      19.591  25.057  14.265  1.00 57.96           N  
-ANISOU11619  N   VAL B 831     6375   8036   7610  -1035   -541  -2118       N  
-ATOM  11620  CA  VAL B 831      19.908  24.495  12.958  1.00 57.68           C  
-ANISOU11620  CA  VAL B 831     6317   8010   7588   -968   -601  -2093       C  
-ATOM  11621  C   VAL B 831      21.356  24.761  12.560  1.00 61.00           C  
-ANISOU11621  C   VAL B 831     6573   8644   7961  -1108   -517  -2398       C  
-ATOM  11622  O   VAL B 831      22.062  23.861  12.109  1.00 61.38           O  
-ANISOU11622  O   VAL B 831     6484   8867   7970  -1010   -690  -2497       O  
-ATOM  11623  CB  VAL B 831      18.978  25.073  11.876  1.00 55.74           C  
-ANISOU11623  CB  VAL B 831     6269   7487   7421   -990   -434  -1869       C  
-ATOM  11624  CG1 VAL B 831      19.562  24.850  10.488  1.00 54.00           C  
-ANISOU11624  CG1 VAL B 831     6009   7300   7207  -1000   -415  -1913       C  
-ATOM  11625  CG2 VAL B 831      17.595  24.461  11.992  1.00 53.70           C  
-ANISOU11625  CG2 VAL B 831     6148   7057   7200   -803   -576  -1554       C  
-ATOM  11626  N   ALA B 832      21.792  26.000  12.743  1.00 50.92           N  
-ANISOU11626  N   ALA B 832     5308   7358   6680  -1339   -260  -2550       N  
-ATOM  11627  CA  ALA B 832      23.130  26.417  12.346  1.00 59.48           C  
-ANISOU11627  CA  ALA B 832     6248   8643   7710  -1514   -146  -2834       C  
-ATOM  11628  C   ALA B 832      24.182  26.123  13.410  1.00 64.82           C  
-ANISOU11628  C   ALA B 832     6718   9605   8305  -1535   -247  -3105       C  
-ATOM  11629  O   ALA B 832      25.369  26.367  13.199  1.00 66.01           O  
-ANISOU11629  O   ALA B 832     6719   9968   8395  -1670   -177  -3364       O  
-ATOM  11630  CB  ALA B 832      23.131  27.898  12.012  1.00 59.28           C  
-ANISOU11630  CB  ALA B 832     6344   8469   7709  -1771    168  -2867       C  
-ATOM  11631  N   LYS B 833      23.755  25.613  14.557  1.00 86.77           N  
-ANISOU11631  N   LYS B 833     9489  12401  11079  -1412   -410  -3048       N  
-ATOM  11632  CA  LYS B 833      24.697  25.332  15.631  1.00 94.45           C  
-ANISOU11632  CA  LYS B 833    10277  13631  11978  -1430   -515  -3294       C  
-ATOM  11633  C   LYS B 833      25.284  23.933  15.491  1.00 98.46           C  
-ANISOU11633  C   LYS B 833    10624  14347  12438  -1232   -820  -3371       C  
-ATOM  11634  O   LYS B 833      25.801  23.370  16.452  1.00 98.99           O  
-ANISOU11634  O   LYS B 833    10562  14598  12453  -1172   -995  -3509       O  
-ATOM  11635  CB  LYS B 833      24.035  25.505  17.002  1.00 97.82           C  
-ANISOU11635  CB  LYS B 833    10762  13997  12410  -1415   -543  -3219       C  
-ATOM  11636  CG  LYS B 833      25.001  25.377  18.173  1.00102.77           C  
-ANISOU11636  CG  LYS B 833    11209  14876  12963  -1463   -619  -3477       C  
-ATOM  11637  CD  LYS B 833      24.297  25.515  19.511  1.00108.46           C  
-ANISOU11637  CD  LYS B 833    11985  15541  13682  -1448   -653  -3392       C  
-ATOM  11638  CE  LYS B 833      23.893  26.955  19.786  1.00113.50           C  
-ANISOU11638  CE  LYS B 833    12749  16017  14357  -1639   -354  -3386       C  
-ATOM  11639  NZ  LYS B 833      23.411  27.129  21.185  1.00115.52           N  
-ANISOU11639  NZ  LYS B 833    13019  16278  14597  -1640   -381  -3365       N  
-ATOM  11640  N   GLN B 834      25.206  23.371  14.292  1.00101.20           N  
-ANISOU11640  N   GLN B 834    10985  14663  12805  -1127   -893  -3285       N  
-ATOM  11641  CA  GLN B 834      25.759  22.044  14.062  1.00106.67           C  
-ANISOU11641  CA  GLN B 834    11533  15543  13454   -924  -1195  -3365       C  
-ATOM  11642  C   GLN B 834      26.182  21.824  12.617  1.00108.50           C  
-ANISOU11642  C   GLN B 834    11718  15822  13684   -902  -1175  -3406       C  
-ATOM  11643  O   GLN B 834      25.528  22.289  11.684  1.00108.49           O  
-ANISOU11643  O   GLN B 834    11860  15621  13740   -949  -1019  -3227       O  
-ATOM  11644  CB  GLN B 834      24.773  20.962  14.501  1.00106.90           C  
-ANISOU11644  CB  GLN B 834    11654  15458  13507   -689  -1482  -3114       C  
-ATOM  11645  CG  GLN B 834      23.442  20.988  13.775  1.00109.18           C  
-ANISOU11645  CG  GLN B 834    12154  15456  13873   -621  -1440  -2776       C  
-ATOM  11646  CD  GLN B 834      22.438  20.022  14.384  1.00108.80           C  
-ANISOU11646  CD  GLN B 834    12199  15308  13833   -425  -1710  -2527       C  
-ATOM  11647  OE1 GLN B 834      22.345  19.894  15.607  1.00106.83           O  
-ANISOU11647  OE1 GLN B 834    11926  15116  13548   -424  -1804  -2545       O  
-ATOM  11648  NE2 GLN B 834      21.686  19.331  13.533  1.00108.06           N  
-ANISOU11648  NE2 GLN B 834    12210  15071  13777   -268  -1839  -2291       N  
-ATOM  11649  N   GLY B 835      27.288  21.108  12.446  1.00122.41           N  
-ANISOU11649  N   GLY B 835    13274  17860  15378   -826  -1341  -3651       N  
-ATOM  11650  CA  GLY B 835      27.831  20.833  11.131  1.00121.28           C  
-ANISOU11650  CA  GLY B 835    13047  17821  15214   -799  -1341  -3736       C  
-ATOM  11651  C   GLY B 835      28.447  22.070  10.516  1.00119.94           C  
-ANISOU11651  C   GLY B 835    12845  17709  15019  -1082  -1006  -3886       C  
-ATOM  11652  O   GLY B 835      28.807  23.017  11.217  1.00120.10           O  
-ANISOU11652  O   GLY B 835    12850  17767  15016  -1290   -814  -4011       O  
-ATOM  11653  N   ASP B 836      28.569  22.061   9.195  1.00110.83           N  
-ANISOU11653  N   ASP B 836    11683  16562  13864  -1097   -942  -3871       N  
-ATOM  11654  CA  ASP B 836      29.122  23.195   8.472  1.00109.54           C  
-ANISOU11654  CA  ASP B 836    11502  16452  13668  -1379   -637  -3992       C  
-ATOM  11655  C   ASP B 836      27.999  24.093   7.983  1.00103.77           C  
-ANISOU11655  C   ASP B 836    11032  15371  13026  -1498   -414  -3706       C  
-ATOM  11656  O   ASP B 836      27.570  23.994   6.833  1.00104.99           O  
-ANISOU11656  O   ASP B 836    11268  15410  13215  -1468   -384  -3556       O  
-ATOM  11657  CB  ASP B 836      29.959  22.717   7.282  1.00114.46           C  
-ANISOU11657  CB  ASP B 836    11955  17312  14223  -1351   -686  -4157       C  
-ATOM  11658  CG  ASP B 836      31.117  21.826   7.698  1.00118.98           C  
-ANISOU11658  CG  ASP B 836    12258  18246  14702  -1219   -916  -4466       C  
-ATOM  11659  OD1 ASP B 836      32.276  22.293   7.652  1.00121.29           O  
-ANISOU11659  OD1 ASP B 836    12365  18823  14897  -1399   -797  -4762       O  
-ATOM  11660  OD2 ASP B 836      30.865  20.659   8.073  1.00119.93           O  
-ANISOU11660  OD2 ASP B 836    12357  18369  14842   -939  -1223  -4413       O  
-ATOM  11661  N   TYR B 837      27.519  24.967   8.860  1.00 84.11           N  
-ANISOU11661  N   TYR B 837     8671  12714  10572  -1627   -265  -3636       N  
-ATOM  11662  CA  TYR B 837      26.451  25.884   8.490  1.00 77.29           C  
-ANISOU11662  CA  TYR B 837     8059  11514   9793  -1735    -59  -3383       C  
-ATOM  11663  C   TYR B 837      26.937  27.322   8.436  1.00 78.04           C  
-ANISOU11663  C   TYR B 837     8193  11600   9860  -2066    244  -3513       C  
-ATOM  11664  O   TYR B 837      27.369  27.877   9.443  1.00 80.98           O  
-ANISOU11664  O   TYR B 837     8519  12050  10199  -2189    316  -3666       O  
-ATOM  11665  CB  TYR B 837      25.258  25.738   9.432  1.00 67.87           C  
-ANISOU11665  CB  TYR B 837     7025  10087   8674  -1595   -141  -3149       C  
-ATOM  11666  CG  TYR B 837      24.181  24.843   8.870  1.00 56.99           C  
-ANISOU11666  CG  TYR B 837     5765   8525   7364  -1353   -314  -2858       C  
-ATOM  11667  CD1 TYR B 837      24.380  23.471   8.756  1.00 52.47           C  
-ANISOU11667  CD1 TYR B 837     5073   8097   6766  -1111   -609  -2868       C  
-ATOM  11668  CD2 TYR B 837      22.970  25.367   8.439  1.00 50.99           C  
-ANISOU11668  CD2 TYR B 837     5239   7445   6690  -1363   -191  -2578       C  
-ATOM  11669  CE1 TYR B 837      23.402  22.649   8.235  1.00 46.13           C  
-ANISOU11669  CE1 TYR B 837     4384   7123   6019   -897   -773  -2598       C  
-ATOM  11670  CE2 TYR B 837      21.983  24.552   7.924  1.00 44.44           C  
-ANISOU11670  CE2 TYR B 837     4515   6454   5916  -1148   -346  -2309       C  
-ATOM  11671  CZ  TYR B 837      22.205  23.195   7.822  1.00 42.94           C  
-ANISOU11671  CZ  TYR B 837     4207   6411   5698   -921   -636  -2317       C  
-ATOM  11672  OH  TYR B 837      21.224  22.384   7.301  1.00 41.43           O  
-ANISOU11672  OH  TYR B 837     4129   6055   5558   -714   -796  -2045       O  
-ATOM  11673  N   CYS B 838      26.865  27.915   7.251  1.00 71.80           N  
-ANISOU11673  N   CYS B 838     7492  10710   9079  -2214    413  -3447       N  
-ATOM  11674  CA  CYS B 838      27.405  29.247   7.034  1.00 72.65           C  
-ANISOU11674  CA  CYS B 838     7640  10818   9145  -2548    685  -3572       C  
-ATOM  11675  C   CYS B 838      26.295  30.246   6.780  1.00 71.18           C  
-ANISOU11675  C   CYS B 838     7744  10249   9052  -2651    864  -3324       C  
-ATOM  11676  O   CYS B 838      25.253  29.900   6.224  1.00 70.80           O  
-ANISOU11676  O   CYS B 838     7844   9969   9088  -2495    811  -3062       O  
-ATOM  11677  CB  CYS B 838      28.366  29.247   5.844  1.00 74.88           C  
-ANISOU11677  CB  CYS B 838     7784  11326   9340  -2689    747  -3730       C  
-ATOM  11678  SG  CYS B 838      27.553  29.099   4.224  1.00 70.71           S  
-ANISOU11678  SG  CYS B 838     7413  10578   8874  -2641    777  -3464       S  
-ATOM  11679  N   ARG B 839      26.525  31.489   7.191  1.00 72.36           N  
-ANISOU11679  N   ARG B 839     7976  10332   9186  -2913   1070  -3412       N  
-ATOM  11680  CA  ARG B 839      25.608  32.570   6.872  1.00 72.38           C  
-ANISOU11680  CA  ARG B 839     8255   9979   9266  -3042   1249  -3214       C  
-ATOM  11681  C   ARG B 839      25.726  32.884   5.393  1.00 71.39           C  
-ANISOU11681  C   ARG B 839     8194   9803   9127  -3190   1358  -3155       C  
-ATOM  11682  O   ARG B 839      26.757  33.371   4.932  1.00 72.74           O  
-ANISOU11682  O   ARG B 839     8268  10166   9202  -3439   1470  -3349       O  
-ATOM  11683  CB  ARG B 839      25.926  33.819   7.693  1.00 74.86           C  
-ANISOU11683  CB  ARG B 839     8638  10248   9558  -3291   1424  -3348       C  
-ATOM  11684  CG  ARG B 839      24.895  34.929   7.541  1.00 76.30           C  
-ANISOU11684  CG  ARG B 839     9122  10041   9828  -3390   1579  -3149       C  
-ATOM  11685  CD  ARG B 839      25.325  36.206   8.248  1.00 81.49           C  
-ANISOU11685  CD  ARG B 839     9848  10661  10453  -3657   1748  -3304       C  
-ATOM  11686  NE  ARG B 839      24.286  37.228   8.182  1.00 85.61           N  
-ANISOU11686  NE  ARG B 839    10665  10799  11065  -3717   1868  -3121       N  
-ATOM  11687  CZ  ARG B 839      23.888  37.811   7.055  1.00 87.91           C  
-ANISOU11687  CZ  ARG B 839    11145  10867  11389  -3838   1970  -2979       C  
-ATOM  11688  NH1 ARG B 839      24.441  37.468   5.901  1.00 89.38           N  
-ANISOU11688  NH1 ARG B 839    11250  11186  11523  -3920   1975  -2995       N  
-ATOM  11689  NH2 ARG B 839      22.935  38.732   7.080  1.00 91.76           N  
-ANISOU11689  NH2 ARG B 839    11902  11002  11960  -3874   2060  -2826       N  
-ATOM  11690  N   PRO B 840      24.669  32.595   4.633  1.00 60.16           N  
-ANISOU11690  N   PRO B 840     6932   8132   7793  -3043   1322  -2884       N  
-ATOM  11691  CA  PRO B 840      24.722  32.826   3.192  1.00 60.98           C  
-ANISOU11691  CA  PRO B 840     7100   8182   7887  -3170   1413  -2811       C  
-ATOM  11692  C   PRO B 840      24.532  34.300   2.856  1.00 63.16           C  
-ANISOU11692  C   PRO B 840     7602   8217   8178  -3472   1645  -2765       C  
-ATOM  11693  O   PRO B 840      23.469  34.860   3.119  1.00 62.55           O  
-ANISOU11693  O   PRO B 840     7759   7808   8198  -3433   1694  -2574       O  
-ATOM  11694  CB  PRO B 840      23.538  32.009   2.676  1.00 58.13           C  
-ANISOU11694  CB  PRO B 840     6851   7610   7627  -2887   1282  -2522       C  
-ATOM  11695  CG  PRO B 840      22.557  32.065   3.784  1.00 57.03           C  
-ANISOU11695  CG  PRO B 840     6836   7263   7570  -2730   1233  -2386       C  
-ATOM  11696  CD  PRO B 840      23.371  32.047   5.059  1.00 57.39           C  
-ANISOU11696  CD  PRO B 840     6709   7548   7548  -2762   1195  -2632       C  
-ATOM  11697  N   THR B 841      25.556  34.923   2.285  1.00 63.41           N  
-ANISOU11697  N   THR B 841     8129   6910   9053  -1744   3724  -1348       N  
-ATOM  11698  CA  THR B 841      25.438  36.299   1.829  1.00 67.59           C  
-ANISOU11698  CA  THR B 841     9029   7231   9423  -1858   4164  -1317       C  
-ATOM  11699  C   THR B 841      24.302  36.410   0.825  1.00 69.29           C  
-ANISOU11699  C   THR B 841     9531   7210   9587  -1559   4118  -1070       C  
-ATOM  11700  O   THR B 841      24.319  35.754  -0.211  1.00 69.91           O  
-ANISOU11700  O   THR B 841     9599   7307   9657  -1371   3952  -1067       O  
-ATOM  11701  CB  THR B 841      26.720  36.768   1.145  1.00 69.37           C  
-ANISOU11701  CB  THR B 841     9311   7547   9499  -2071   4481  -1588       C  
-ATOM  11702  OG1 THR B 841      27.825  36.619   2.043  1.00 67.75           O  
-ANISOU11702  OG1 THR B 841     8803   7624   9315  -2341   4517  -1843       O  
-ATOM  11703  CG2 THR B 841      26.595  38.224   0.732  1.00 72.94           C  
-ANISOU11703  CG2 THR B 841    10195   7757   9762  -2202   4975  -1565       C  
-ATOM  11704  N   VAL B 842      23.312  37.237   1.131  1.00 73.09           N  
-ANISOU11704  N   VAL B 842    10263   7484  10025  -1509   4266   -864       N  
-ATOM  11705  CA  VAL B 842      22.174  37.407   0.238  1.00 73.09           C  
-ANISOU11705  CA  VAL B 842    10530   7294   9947  -1203   4233   -627       C  
-ATOM  11706  C   VAL B 842      22.359  38.657  -0.601  1.00 79.09           C  
-ANISOU11706  C   VAL B 842    11708   7857  10487  -1243   4700   -638       C  
-ATOM  11707  O   VAL B 842      23.119  39.548  -0.232  1.00 79.28           O  
-ANISOU11707  O   VAL B 842    11853   7851  10420  -1533   5077   -787       O  
-ATOM  11708  CB  VAL B 842      20.856  37.512   1.018  1.00 69.50           C  
-ANISOU11708  CB  VAL B 842    10110   6743   9553  -1066   4091   -378       C  
-ATOM  11709  CG1 VAL B 842      19.669  37.387   0.075  1.00 67.72           C  
-ANISOU11709  CG1 VAL B 842    10067   6414   9249   -709   3961   -154       C  
-ATOM  11710  CG2 VAL B 842      20.800  36.438   2.076  1.00 64.73           C  
-ANISOU11710  CG2 VAL B 842     9125   6311   9158  -1102   3703   -405       C  
-ATOM  11711  N   GLN B 843      21.670  38.709  -1.735  1.00 75.85           N  
-ANISOU11711  N   GLN B 843    11525   7320   9974   -955   4686   -489       N  
-ATOM  11712  CA  GLN B 843      21.727  39.861  -2.626  1.00 84.28           C  
-ANISOU11712  CA  GLN B 843    13035   8175  10811   -931   5120   -476       C  
-ATOM  11713  C   GLN B 843      20.367  40.065  -3.270  1.00 87.63           C  
-ANISOU11713  C   GLN B 843    13706   8455  11135   -550   5061   -192       C  
-ATOM  11714  O   GLN B 843      19.481  39.222  -3.141  1.00 87.76           O  
-ANISOU11714  O   GLN B 843    13516   8567  11261   -329   4670    -41       O  
-ATOM  11715  CB  GLN B 843      22.776  39.646  -3.716  1.00 87.57           C  
-ANISOU11715  CB  GLN B 843    13467   8637  11170   -998   5208   -691       C  
-ATOM  11716  CG  GLN B 843      24.191  39.481  -3.205  1.00 91.82           C  
-ANISOU11716  CG  GLN B 843    13765   9359  11765  -1363   5290  -1002       C  
-ATOM  11717  CD  GLN B 843      25.177  39.222  -4.323  1.00 94.55           C  
-ANISOU11717  CD  GLN B 843    14116   9760  12050  -1412   5353  -1214       C  
-ATOM  11718  OE1 GLN B 843      26.379  39.102  -4.090  1.00 94.31           O  
-ANISOU11718  OE1 GLN B 843    13902   9902  12028  -1691   5435  -1490       O  
-ATOM  11719  NE2 GLN B 843      24.672  39.135  -5.549  1.00 98.35           N  
-ANISOU11719  NE2 GLN B 843    14798  10108  12461  -1139   5313  -1093       N  
-ATOM  11720  N   GLU B 844      20.203  41.180  -3.969  1.00112.08           N  
-ANISOU11720  N   GLU B 844    17251  11335  14001   -469   5460   -131       N  
-ATOM  11721  CA  GLU B 844      18.959  41.438  -4.678  1.00115.83           C  
-ANISOU11721  CA  GLU B 844    17977  11697  14336    -73   5434    129       C  
-ATOM  11722  C   GLU B 844      19.008  40.786  -6.048  1.00116.55           C  
-ANISOU11722  C   GLU B 844    18047  11838  14400    146   5269    109       C  
-ATOM  11723  O   GLU B 844      18.012  40.244  -6.525  1.00115.35           O  
-ANISOU11723  O   GLU B 844    17831  11752  14243    469   4991    287       O  
-ATOM  11724  CB  GLU B 844      18.707  42.940  -4.816  1.00119.43           C  
-ANISOU11724  CB  GLU B 844    18961  11889  14529    -40   5951    221       C  
-ATOM  11725  CG  GLU B 844      17.392  43.288  -5.506  1.00122.42           C  
-ANISOU11725  CG  GLU B 844    19617  12172  14725    409   5946    498       C  
-ATOM  11726  CD  GLU B 844      16.168  42.886  -4.693  1.00122.41           C  
-ANISOU11726  CD  GLU B 844    19410  12282  14818    592   5615    715       C  
-ATOM  11727  OE1 GLU B 844      16.325  42.525  -3.508  1.00122.84           O  
-ANISOU11727  OE1 GLU B 844    19178  12427  15068    355   5454    666       O  
-ATOM  11728  OE2 GLU B 844      15.046  42.931  -5.240  1.00124.00           O  
-ANISOU11728  OE2 GLU B 844    19734  12492  14887    976   5519    926       O  
-ATOM  11729  N   GLU B 845      20.180  40.833  -6.670  1.00119.07           N  
-ANISOU11729  N   GLU B 845    18409  12140  14694    -45   5446   -120       N  
-ATOM  11730  CA  GLU B 845      20.369  40.263  -7.995  1.00118.40           C  
-ANISOU11730  CA  GLU B 845    18316  12082  14587    122   5323   -160       C  
-ATOM  11731  C   GLU B 845      20.509  38.746  -7.928  1.00111.98           C  
-ANISOU11731  C   GLU B 845    17022  11519  14007    131   4824   -212       C  
-ATOM  11732  O   GLU B 845      21.489  38.233  -7.388  1.00111.04           O  
-ANISOU11732  O   GLU B 845    16627  11533  14029   -139   4737   -415       O  
-ATOM  11733  CB  GLU B 845      21.602  40.870  -8.660  1.00127.90           C  
-ANISOU11733  CB  GLU B 845    19747  13174  15677   -107   5702   -404       C  
-ATOM  11734  CG  GLU B 845      21.352  41.360 -10.072  1.00140.98           C  
-ANISOU11734  CG  GLU B 845    21785  14650  17131    142   5905   -339       C  
-ATOM  11735  CD  GLU B 845      20.574  40.360 -10.901  1.00147.32           C  
-ANISOU11735  CD  GLU B 845    22404  15570  18001    485   5499   -183       C  
-ATOM  11736  OE1 GLU B 845      21.211  39.540 -11.595  1.00152.68           O  
-ANISOU11736  OE1 GLU B 845    22884  16348  18780    441   5315   -316       O  
-ATOM  11737  OE2 GLU B 845      19.325  40.392 -10.857  1.00152.21           O  
-ANISOU11737  OE2 GLU B 845    23074  16198  18562    792   5371     67       O  
-ATOM  11738  N   ARG B 846      19.533  38.036  -8.486  1.00 93.45           N  
-ANISOU11738  N   ARG B 846    14583   9246  11676    445   4513    -35       N  
-ATOM  11739  CA  ARG B 846      19.505  36.576  -8.409  1.00 87.65           C  
-ANISOU11739  CA  ARG B 846    13433   8733  11137    473   4051    -60       C  
-ATOM  11740  C   ARG B 846      20.828  35.943  -8.829  1.00 84.26           C  
-ANISOU11740  C   ARG B 846    12825   8387  10802    271   4007   -303       C  
-ATOM  11741  O   ARG B 846      21.450  36.353  -9.811  1.00 86.94           O  
-ANISOU11741  O   ARG B 846    13364   8628  11041    247   4234   -404       O  
-ATOM  11742  CB  ARG B 846      18.342  35.999  -9.221  1.00 87.51           C  
-ANISOU11742  CB  ARG B 846    13400   8780  11068    824   3799    136       C  
-ATOM  11743  CG  ARG B 846      18.387  36.329 -10.698  1.00 90.87           C  
-ANISOU11743  CG  ARG B 846    14082   9108  11337   1003   3965    153       C  
-ATOM  11744  CD  ARG B 846      18.623  35.085 -11.531  1.00 89.61           C  
-ANISOU11744  CD  ARG B 846    13675   9095  11279   1057   3660     96       C  
-ATOM  11745  NE  ARG B 846      18.657  35.412 -12.950  1.00 92.15           N  
-ANISOU11745  NE  ARG B 846    14239   9317  11456   1225   3818    114       N  
-ATOM  11746  CZ  ARG B 846      19.727  35.892 -13.572  1.00 94.50           C  
-ANISOU11746  CZ  ARG B 846    14714   9478  11712   1076   4086    -54       C  
-ATOM  11747  NH1 ARG B 846      20.849  36.095 -12.898  1.00 96.54           N  
-ANISOU11747  NH1 ARG B 846    14915   9716  12051    750   4224   -262       N  
-ATOM  11748  NH2 ARG B 846      19.675  36.172 -14.866  1.00 95.97           N  
-ANISOU11748  NH2 ARG B 846    15132   9564  11767   1246   4220    -28       N  
-ATOM  11749  N   LYS B 847      21.237  34.932  -8.071  1.00 80.83           N  
-ANISOU11749  N   LYS B 847    12021   8138  10553    139   3713   -399       N  
-ATOM  11750  CA  LYS B 847      22.538  34.305  -8.231  1.00 76.12           C  
-ANISOU11750  CA  LYS B 847    11217   7662  10045    -58   3659   -639       C  
-ATOM  11751  C   LYS B 847      22.638  33.156  -7.242  1.00 69.05           C  
-ANISOU11751  C   LYS B 847     9936   6970   9330   -115   3299   -676       C  
-ATOM  11752  O   LYS B 847      22.085  33.233  -6.148  1.00 67.00           O  
-ANISOU11752  O   LYS B 847     9603   6728   9126   -138   3226   -592       O  
-ATOM  11753  CB  LYS B 847      23.644  35.320  -7.945  1.00 79.68           C  
-ANISOU11753  CB  LYS B 847    11807   8049  10417   -357   4054   -851       C  
-ATOM  11754  CG  LYS B 847      25.025  34.706  -7.822  1.00 83.83           C  
-ANISOU11754  CG  LYS B 847    12064   8761  11026   -589   3994  -1125       C  
-ATOM  11755  CD  LYS B 847      25.962  35.618  -7.055  1.00 89.67           C  
-ANISOU11755  CD  LYS B 847    12849   9519  11703   -923   4337  -1337       C  
-ATOM  11756  CE  LYS B 847      26.045  36.990  -7.694  1.00 95.76           C  
-ANISOU11756  CE  LYS B 847    14063  10053  12269   -995   4813  -1364       C  
-ATOM  11757  NZ  LYS B 847      26.925  37.908  -6.915  1.00100.79           N  
-ANISOU11757  NZ  LYS B 847    14763  10713  12820  -1355   5183  -1582       N  
-ATOM  11758  N   ILE B 848      23.328  32.086  -7.618  1.00 64.00           N  
-ANISOU11758  N   ILE B 848     9066   6476   8775   -129   3080   -798       N  
-ATOM  11759  CA  ILE B 848      23.520  30.972  -6.698  1.00 57.35           C  
-ANISOU11759  CA  ILE B 848     7889   5822   8080   -168   2762   -848       C  
-ATOM  11760  C   ILE B 848      24.940  30.442  -6.753  1.00 57.06           C  
-ANISOU11760  C   ILE B 848     7652   5945   8084   -329   2744  -1097       C  
-ATOM  11761  O   ILE B 848      25.253  29.567  -7.551  1.00 56.94           O  
-ANISOU11761  O   ILE B 848     7546   5997   8091   -239   2576  -1133       O  
-ATOM  11762  CB  ILE B 848      22.534  29.818  -6.970  1.00 53.92           C  
-ANISOU11762  CB  ILE B 848     7345   5439   7702     70   2400   -682       C  
-ATOM  11763  CG1 ILE B 848      21.101  30.346  -7.036  1.00 50.11           C  
-ANISOU11763  CG1 ILE B 848     7052   4841   7147    250   2418   -449       C  
-ATOM  11764  CG2 ILE B 848      22.649  28.744  -5.885  1.00 49.45           C  
-ANISOU11764  CG2 ILE B 848     6489   5034   7267     33   2105   -728       C  
-ATOM  11765  CD1 ILE B 848      20.076  29.285  -7.356  1.00 46.87           C  
-ANISOU11765  CD1 ILE B 848     6545   4507   6756    462   2095   -307       C  
-ATOM  11766  N   VAL B 849      25.794  30.983  -5.894  1.00 61.55           N  
-ANISOU11766  N   VAL B 849     8147   6591   8650   -570   2924  -1272       N  
-ATOM  11767  CA  VAL B 849      27.174  30.537  -5.799  1.00 64.17           C  
-ANISOU11767  CA  VAL B 849     8256   7129   8996   -729   2915  -1531       C  
-ATOM  11768  C   VAL B 849      27.397  29.774  -4.503  1.00 63.15           C  
-ANISOU11768  C   VAL B 849     7821   7203   8971   -766   2683  -1583       C  
-ATOM  11769  O   VAL B 849      27.637  30.377  -3.462  1.00 65.12           O  
-ANISOU11769  O   VAL B 849     8018   7505   9221   -945   2823  -1656       O  
-ATOM  11770  CB  VAL B 849      28.134  31.725  -5.818  1.00 65.57           C  
-ANISOU11770  CB  VAL B 849     8560   7298   9055  -1003   3325  -1745       C  
-ATOM  11771  CG1 VAL B 849      29.564  31.237  -5.949  1.00 66.98           C  
-ANISOU11771  CG1 VAL B 849     8509   7722   9219  -1148   3315  -2031       C  
-ATOM  11772  CG2 VAL B 849      27.776  32.667  -6.948  1.00 71.13           C  
-ANISOU11772  CG2 VAL B 849     9638   7752   9636   -963   3607  -1674       C  
-ATOM  11773  N   ILE B 850      27.312  28.452  -4.561  1.00 56.46           N  
-ANISOU11773  N   ILE B 850     6787   6465   8202   -597   2341  -1546       N  
-ATOM  11774  CA  ILE B 850      27.503  27.636  -3.370  1.00 54.55           C  
-ANISOU11774  CA  ILE B 850     6281   6403   8043   -593   2111  -1591       C  
-ATOM  11775  C   ILE B 850      28.828  26.901  -3.450  1.00 56.90           C  
-ANISOU11775  C   ILE B 850     6348   6952   8319   -628   2037  -1820       C  
-ATOM  11776  O   ILE B 850      29.200  26.390  -4.502  1.00 55.93           O  
-ANISOU11776  O   ILE B 850     6239   6844   8166   -542   1983  -1856       O  
-ATOM  11777  CB  ILE B 850      26.378  26.595  -3.208  1.00 52.62           C  
-ANISOU11777  CB  ILE B 850     6013   6103   7878   -365   1778  -1386       C  
-ATOM  11778  CG1 ILE B 850      25.041  27.168  -3.676  1.00 49.64           C  
-ANISOU11778  CG1 ILE B 850     5881   5499   7482   -267   1829  -1157       C  
-ATOM  11779  CG2 ILE B 850      26.284  26.133  -1.768  1.00 48.17           C  
-ANISOU11779  CG2 ILE B 850     5265   5645   7394   -385   1611  -1396       C  
-ATOM  11780  CD1 ILE B 850      23.953  26.132  -3.779  1.00 47.73           C  
-ANISOU11780  CD1 ILE B 850     5627   5226   7282    -57   1526   -984       C  
-ATOM  11781  N   LYS B 851      29.540  26.844  -2.334  1.00 59.13           N  
-ANISOU11781  N   LYS B 851     6412   7445   8609   -744   2034  -1974       N  
-ATOM  11782  CA  LYS B 851      30.806  26.126  -2.293  1.00 64.02           C  
-ANISOU11782  CA  LYS B 851     6787   8352   9184   -750   1954  -2198       C  
-ATOM  11783  C   LYS B 851      30.756  25.001  -1.265  1.00 60.73           C  
-ANISOU11783  C   LYS B 851     6156   8091   8828   -602   1655  -2177       C  
-ATOM  11784  O   LYS B 851      30.533  25.241  -0.077  1.00 60.92           O  
-ANISOU11784  O   LYS B 851     6098   8153   8895   -671   1650  -2167       O  
-ATOM  11785  CB  LYS B 851      31.949  27.088  -1.986  1.00 72.19           C  
-ANISOU11785  CB  LYS B 851     7735   9574  10120  -1029   2260  -2464       C  
-ATOM  11786  CG  LYS B 851      31.678  28.494  -2.471  1.00 82.58           C  
-ANISOU11786  CG  LYS B 851     9326  10672  11378  -1220   2616  -2448       C  
-ATOM  11787  CD  LYS B 851      32.860  29.053  -3.224  1.00 94.13           C  
-ANISOU11787  CD  LYS B 851    10804  12254  12708  -1414   2886  -2713       C  
-ATOM  11788  CE  LYS B 851      33.077  28.300  -4.516  1.00100.66           C  
-ANISOU11788  CE  LYS B 851    11664  13052  13531  -1247   2744  -2707       C  
-ATOM  11789  NZ  LYS B 851      34.266  28.810  -5.244  1.00109.99           N  
-ANISOU11789  NZ  LYS B 851    12853  14357  14583  -1446   2998  -2986       N  
-ATOM  11790  N   ASN B 852      30.954  23.772  -1.730  1.00 66.11           N  
-ANISOU11790  N   ASN B 852     6767   8846   9505   -395   1416  -2167       N  
-ATOM  11791  CA  ASN B 852      30.898  22.607  -0.856  1.00 60.74           C  
-ANISOU11791  CA  ASN B 852     5935   8288   8854   -220   1140  -2144       C  
-ATOM  11792  C   ASN B 852      29.550  22.451  -0.164  1.00 56.15           C  
-ANISOU11792  C   ASN B 852     5461   7503   8372   -149   1000  -1925       C  
-ATOM  11793  O   ASN B 852      29.475  21.918   0.937  1.00 53.83           O  
-ANISOU11793  O   ASN B 852     5052   7293   8109    -89    851  -1929       O  
-ATOM  11794  CB  ASN B 852      32.010  22.663   0.192  1.00 63.07           C  
-ANISOU11794  CB  ASN B 852     5966   8904   9093   -307   1182  -2371       C  
-ATOM  11795  CG  ASN B 852      33.372  22.340  -0.383  1.00 62.68           C  
-ANISOU11795  CG  ASN B 852     5758   9132   8925   -297   1221  -2599       C  
-ATOM  11796  OD1 ASN B 852      33.782  21.180  -0.409  1.00 64.70           O  
-ANISOU11796  OD1 ASN B 852     5911   9534   9138    -83   1013  -2628       O  
-ATOM  11797  ND2 ASN B 852      34.085  23.365  -0.840  1.00 63.28           N  
-ANISOU11797  ND2 ASN B 852     5828   9285   8931   -529   1499  -2772       N  
-ATOM  11798  N   GLY B 853      28.489  22.917  -0.812  1.00 44.33           N  
-ANISOU11798  N   GLY B 853     4184   5749   6911   -149   1050  -1743       N  
-ATOM  11799  CA  GLY B 853      27.141  22.752  -0.298  1.00 39.69           C  
-ANISOU11799  CA  GLY B 853     3703   4980   6397    -76    914  -1540       C  
-ATOM  11800  C   GLY B 853      26.749  21.290  -0.190  1.00 36.99           C  
-ANISOU11800  C   GLY B 853     3341   4649   6064    134    619  -1473       C  
-ATOM  11801  O   GLY B 853      27.393  20.432  -0.792  1.00 37.47           O  
-ANISOU11801  O   GLY B 853     3356   4812   6069    247    532  -1541       O  
-ATOM  11802  N   ARG B 854      25.700  21.006   0.582  1.00 52.62           N  
-ANISOU11802  N   ARG B 854     5372   6521   8102    180    478  -1346       N  
-ATOM  11803  CA  ARG B 854      25.234  19.634   0.798  1.00 50.84           C  
-ANISOU11803  CA  ARG B 854     5167   6283   7866    356    222  -1292       C  
-ATOM  11804  C   ARG B 854      23.718  19.596   0.900  1.00 48.67           C  
-ANISOU11804  C   ARG B 854     5046   5819   7627    380    131  -1112       C  
-ATOM  11805  O   ARG B 854      23.110  20.543   1.388  1.00 48.42           O  
-ANISOU11805  O   ARG B 854     5048   5698   7650    271    221  -1045       O  
-ATOM  11806  CB  ARG B 854      25.800  19.072   2.102  1.00 51.41           C  
-ANISOU11806  CB  ARG B 854     5086   6497   7949    389    113  -1402       C  
-ATOM  11807  CG  ARG B 854      27.167  19.602   2.489  1.00 53.75           C  
-ANISOU11807  CG  ARG B 854     5182   7020   8221    294    253  -1594       C  
-ATOM  11808  CD  ARG B 854      27.629  19.027   3.827  1.00 54.78           C  
-ANISOU11808  CD  ARG B 854     5156   7308   8350    354    134  -1693       C  
-ATOM  11809  NE  ARG B 854      26.934  19.622   4.967  1.00 53.48           N  
-ANISOU11809  NE  ARG B 854     4987   7049   8284    235    143  -1634       N  
-ATOM  11810  CZ  ARG B 854      27.254  20.796   5.503  1.00 54.95           C  
-ANISOU11810  CZ  ARG B 854     5075   7293   8511     25    335  -1696       C  
-ATOM  11811  NH1 ARG B 854      28.246  21.509   4.988  1.00 56.58           N  
-ANISOU11811  NH1 ARG B 854     5190   7653   8655    -97    543  -1834       N  
-ATOM  11812  NH2 ARG B 854      26.578  21.263   6.545  1.00 52.97           N  
-ANISOU11812  NH2 ARG B 854     4830   6941   8354    -77    333  -1629       N  
-ATOM  11813  N   HIS B 855      23.101  18.502   0.468  1.00 53.28           N  
-ANISOU11813  N   HIS B 855     5725   6355   8164    515    -37  -1043       N  
-ATOM  11814  CA  HIS B 855      21.666  18.343   0.679  1.00 51.27           C  
-ANISOU11814  CA  HIS B 855     5594   5966   7919    530   -139   -906       C  
-ATOM  11815  C   HIS B 855      21.389  18.383   2.177  1.00 51.41           C  
-ANISOU11815  C   HIS B 855     5558   5966   8011    477   -214   -925       C  
-ATOM  11816  O   HIS B 855      21.980  17.617   2.932  1.00 51.95           O  
-ANISOU11816  O   HIS B 855     5553   6110   8076    532   -315  -1022       O  
-ATOM  11817  CB  HIS B 855      21.166  17.029   0.090  1.00 50.31           C  
-ANISOU11817  CB  HIS B 855     5577   5826   7712    658   -295   -868       C  
-ATOM  11818  CG  HIS B 855      19.682  16.979  -0.098  1.00 49.15           C  
-ANISOU11818  CG  HIS B 855     5557   5581   7536    656   -359   -741       C  
-ATOM  11819  ND1 HIS B 855      18.819  16.550   0.887  1.00 47.44           N  
-ANISOU11819  ND1 HIS B 855     5383   5312   7330    642   -488   -724       N  
-ATOM  11820  CD2 HIS B 855      18.908  17.300  -1.161  1.00 49.46           C  
-ANISOU11820  CD2 HIS B 855     5685   5589   7520    669   -309   -638       C  
-ATOM  11821  CE1 HIS B 855      17.578  16.603   0.437  1.00 47.25           C  
-ANISOU11821  CE1 HIS B 855     5457   5243   7251    638   -516   -625       C  
-ATOM  11822  NE2 HIS B 855      17.604  17.057  -0.803  1.00 47.37           N  
-ANISOU11822  NE2 HIS B 855     5496   5281   7222    664   -410   -567       N  
-ATOM  11823  N   PRO B 856      20.494  19.282   2.613  1.00 47.07           N  
-ANISOU11823  N   PRO B 856     5051   5315   7519    381   -162   -832       N  
-ATOM  11824  CA  PRO B 856      20.198  19.481   4.036  1.00 46.28           C  
-ANISOU11824  CA  PRO B 856     4898   5180   7505    304   -216   -841       C  
-ATOM  11825  C   PRO B 856      19.755  18.201   4.730  1.00 45.23           C  
-ANISOU11825  C   PRO B 856     4803   5024   7357    390   -437   -866       C  
-ATOM  11826  O   PRO B 856      20.181  17.947   5.851  1.00 42.93           O  
-ANISOU11826  O   PRO B 856     4430   4767   7116    378   -497   -945       O  
-ATOM  11827  CB  PRO B 856      19.034  20.469   4.011  1.00 45.98           C  
-ANISOU11827  CB  PRO B 856     4956   5019   7496    230   -143   -701       C  
-ATOM  11828  CG  PRO B 856      19.159  21.170   2.722  1.00 48.18           C  
-ANISOU11828  CG  PRO B 856     5299   5295   7712    243     26   -650       C  
-ATOM  11829  CD  PRO B 856      19.684  20.160   1.756  1.00 48.38           C  
-ANISOU11829  CD  PRO B 856     5328   5396   7660    358    -46   -705       C  
-ATOM  11830  N   VAL B 857      18.906  17.419   4.070  1.00 46.96           N  
-ANISOU11830  N   VAL B 857     5157   5192   7493    471   -541   -806       N  
-ATOM  11831  CA  VAL B 857      18.358  16.195   4.648  1.00 47.90           C  
-ANISOU11831  CA  VAL B 857     5366   5269   7566    533   -722   -835       C  
-ATOM  11832  C   VAL B 857      19.367  15.047   4.656  1.00 51.29           C  
-ANISOU11832  C   VAL B 857     5788   5776   7923    663   -786   -945       C  
-ATOM  11833  O   VAL B 857      19.543  14.378   5.679  1.00 51.30           O  
-ANISOU11833  O   VAL B 857     5798   5767   7925    708   -884  -1016       O  
-ATOM  11834  CB  VAL B 857      17.092  15.740   3.901  1.00 47.17           C  
-ANISOU11834  CB  VAL B 857     5424   5122   7376    551   -785   -754       C  
-ATOM  11835  CG1 VAL B 857      16.506  14.508   4.561  1.00 44.92           C  
-ANISOU11835  CG1 VAL B 857     5259   4783   7025    581   -943   -809       C  
-ATOM  11836  CG2 VAL B 857      16.067  16.861   3.855  1.00 45.99           C  
-ANISOU11836  CG2 VAL B 857     5283   4926   7267    463   -726   -643       C  
-ATOM  11837  N   ILE B 858      20.013  14.811   3.515  1.00 62.34           N  
-ANISOU11837  N   ILE B 858     7186   7249   9251    735   -727   -955       N  
-ATOM  11838  CA  ILE B 858      21.051  13.788   3.412  1.00 66.04           C  
-ANISOU11838  CA  ILE B 858     7647   7808   9636    877   -768  -1051       C  
-ATOM  11839  C   ILE B 858      22.199  14.103   4.361  1.00 68.65           C  
-ANISOU11839  C   ILE B 858     7801   8261  10020    890   -741  -1163       C  
-ATOM  11840  O   ILE B 858      22.839  13.203   4.904  1.00 69.31           O  
-ANISOU11840  O   ILE B 858     7883   8415  10038   1026   -818  -1250       O  
-ATOM  11841  CB  ILE B 858      21.613  13.684   1.976  1.00 66.85           C  
-ANISOU11841  CB  ILE B 858     7753   7975   9671    930   -691  -1041       C  
-ATOM  11842  CG1 ILE B 858      20.696  12.841   1.089  1.00 67.21           C  
-ANISOU11842  CG1 ILE B 858     7982   7942   9611    967   -745   -966       C  
-ATOM  11843  CG2 ILE B 858      23.000  13.069   1.986  1.00 68.32           C  
-ANISOU11843  CG2 ILE B 858     7859   8303   9798   1059   -692  -1157       C  
-ATOM  11844  CD1 ILE B 858      19.421  13.531   0.679  1.00 67.60           C  
-ANISOU11844  CD1 ILE B 858     8086   7915   9684    861   -719   -854       C  
-ATOM  11845  N   ASP B 859      22.450  15.392   4.556  1.00 63.60           N  
-ANISOU11845  N   ASP B 859     7023   7659   9483    751   -617  -1163       N  
-ATOM  11846  CA  ASP B 859      23.506  15.851   5.447  1.00 68.37           C  
-ANISOU11846  CA  ASP B 859     7435   8412  10131    718   -560  -1281       C  
-ATOM  11847  C   ASP B 859      23.305  15.326   6.870  1.00 69.88           C  
-ANISOU11847  C   ASP B 859     7621   8582  10350    758   -688  -1320       C  
-ATOM  11848  O   ASP B 859      24.271  15.013   7.564  1.00 69.97           O  
-ANISOU11848  O   ASP B 859     7506   8751  10330    840   -709  -1438       O  
-ATOM  11849  CB  ASP B 859      23.552  17.381   5.450  1.00 70.69           C  
-ANISOU11849  CB  ASP B 859     7631   8708  10520    519   -377  -1261       C  
-ATOM  11850  CG  ASP B 859      24.789  17.930   6.130  1.00 73.85           C  
-ANISOU11850  CG  ASP B 859     7815   9309  10935    451   -271  -1409       C  
-ATOM  11851  OD1 ASP B 859      24.694  19.017   6.739  1.00 75.34           O  
-ANISOU11851  OD1 ASP B 859     7935   9483  11208    274   -149  -1405       O  
-ATOM  11852  OD2 ASP B 859      25.855  17.284   6.051  1.00 76.82           O  
-ANISOU11852  OD2 ASP B 859     8091   9873  11225    572   -300  -1534       O  
-ATOM  11853  N   VAL B 860      22.051  15.227   7.300  1.00 72.95           N  
-ANISOU11853  N   VAL B 860     8145   8787  10785    706   -774  -1229       N  
-ATOM  11854  CA  VAL B 860      21.746  14.791   8.661  1.00 75.89           C  
-ANISOU11854  CA  VAL B 860     8536   9103  11194    722   -891  -1264       C  
-ATOM  11855  C   VAL B 860      21.777  13.276   8.823  1.00 81.75           C  
-ANISOU11855  C   VAL B 860     9434   9822  11807    920  -1029  -1315       C  
-ATOM  11856  O   VAL B 860      22.294  12.763   9.816  1.00 83.34           O  
-ANISOU11856  O   VAL B 860     9603  10077  11985   1020  -1094  -1403       O  
-ATOM  11857  CB  VAL B 860      20.373  15.304   9.129  1.00 73.07           C  
-ANISOU11857  CB  VAL B 860     8269   8561  10935    574   -926  -1161       C  
-ATOM  11858  CG1 VAL B 860      19.808  14.393  10.208  1.00 70.47           C  
-ANISOU11858  CG1 VAL B 860     8056   8123  10596    624  -1084  -1196       C  
-ATOM  11859  CG2 VAL B 860      20.484  16.734   9.631  1.00 72.15           C  
-ANISOU11859  CG2 VAL B 860     7997   8462  10953    392   -796  -1135       C  
-ATOM  11860  N   LEU B 861      21.215  12.569   7.848  1.00 66.36           N  
-ANISOU11860  N   LEU B 861     7666   7792   9757    976  -1059  -1262       N  
-ATOM  11861  CA  LEU B 861      21.139  11.113   7.890  1.00 75.26           C  
-ANISOU11861  CA  LEU B 861     8997   8866  10732   1145  -1156  -1303       C  
-ATOM  11862  C   LEU B 861      22.501  10.478   7.653  1.00 87.75           C  
-ANISOU11862  C   LEU B 861    10523  10617  12201   1349  -1137  -1390       C  
-ATOM  11863  O   LEU B 861      22.648   9.258   7.736  1.00 89.80           O  
-ANISOU11863  O   LEU B 861    10959  10849  12311   1527  -1195  -1430       O  
-ATOM  11864  CB  LEU B 861      20.161  10.609   6.831  1.00 64.64           C  
-ANISOU11864  CB  LEU B 861     7851   7412   9298   1115  -1162  -1227       C  
-ATOM  11865  CG  LEU B 861      18.831  11.357   6.748  1.00 56.68           C  
-ANISOU11865  CG  LEU B 861     6868   6297   8372    926  -1163  -1137       C  
-ATOM  11866  CD1 LEU B 861      18.096  11.019   5.458  1.00 51.32           C  
-ANISOU11866  CD1 LEU B 861     6318   5593   7587    905  -1139  -1070       C  
-ATOM  11867  CD2 LEU B 861      17.966  11.070   7.974  1.00 49.65           C  
-ANISOU11867  CD2 LEU B 861     6082   5274   7508    866  -1264  -1165       C  
-ATOM  11868  N   LEU B 862      23.493  11.310   7.351  1.00111.90           N  
-ANISOU11868  N   LEU B 862    13349  13856  15313   1323  -1043  -1426       N  
-ATOM  11869  CA  LEU B 862      24.818  10.823   6.980  1.00126.51           C  
-ANISOU11869  CA  LEU B 862    15112  15909  17047   1506  -1016  -1517       C  
-ATOM  11870  C   LEU B 862      25.929  11.776   7.427  1.00133.10           C  
-ANISOU11870  C   LEU B 862    15649  16979  17945   1455   -933  -1618       C  
-ATOM  11871  O   LEU B 862      26.704  11.458   8.327  1.00133.90           O  
-ANISOU11871  O   LEU B 862    15646  17239  17991   1587   -969  -1724       O  
-ATOM  11872  CB  LEU B 862      24.893  10.597   5.465  1.00133.86           C  
-ANISOU11872  CB  LEU B 862    16116  16835  17910   1524   -962  -1465       C  
-ATOM  11873  CG  LEU B 862      23.909   9.584   4.863  1.00138.88           C  
-ANISOU11873  CG  LEU B 862    17037  17283  18448   1566  -1018  -1382       C  
-ATOM  11874  CD1 LEU B 862      23.748   9.791   3.363  1.00144.73           C  
-ANISOU11874  CD1 LEU B 862    17803  18009  19179   1499   -944  -1308       C  
-ATOM  11875  CD2 LEU B 862      24.326   8.151   5.177  1.00142.70           C  
-ANISOU11875  CD2 LEU B 862    17698  17771  18750   1807  -1082  -1439       C  
-ATOM  11876  N   GLY B 863      25.998  12.946   6.797  1.00146.28           N  
-ANISOU11876  N   GLY B 863    17191  18679  19708   1265   -806  -1595       N  
-ATOM  11877  CA  GLY B 863      27.045  13.912   7.083  1.00153.13           C  
-ANISOU11877  CA  GLY B 863    17794  19776  20614   1171   -685  -1708       C  
-ATOM  11878  C   GLY B 863      28.137  13.842   6.034  1.00158.37           C  
-ANISOU11878  C   GLY B 863    18364  20631  21178   1240   -605  -1791       C  
-ATOM  11879  O   GLY B 863      27.913  13.308   4.947  1.00160.67           O  
-ANISOU11879  O   GLY B 863    18802  20831  21414   1310   -624  -1724       O  
-ATOM  11880  N   GLU B 864      29.313  14.382   6.346  1.00140.95           N  
-ANISOU11880  N   GLU B 864    15911  18703  18941   1208   -511  -1946       N  
-ATOM  11881  CA  GLU B 864      30.458  14.248   5.450  1.00144.60           C  
-ANISOU11881  CA  GLU B 864    16266  19387  19289   1283   -445  -2059       C  
-ATOM  11882  C   GLU B 864      30.734  12.771   5.226  1.00143.95           C  
-ANISOU11882  C   GLU B 864    16303  19337  19056   1587   -587  -2056       C  
-ATOM  11883  O   GLU B 864      31.053  12.041   6.166  1.00145.12           O  
-ANISOU11883  O   GLU B 864    16428  19594  19117   1781   -684  -2114       O  
-ATOM  11884  CB  GLU B 864      31.706  14.929   6.020  1.00150.92           C  
-ANISOU11884  CB  GLU B 864    16764  20536  20042   1212   -332  -2262       C  
-ATOM  11885  CG  GLU B 864      32.984  14.629   5.231  1.00158.45           C  
-ANISOU11885  CG  GLU B 864    17586  21772  20846   1323   -287  -2412       C  
-ATOM  11886  CD  GLU B 864      34.237  15.210   5.868  1.00161.87           C  
-ANISOU11886  CD  GLU B 864    17700  22610  21195   1259   -180  -2646       C  
-ATOM  11887  OE1 GLU B 864      34.128  16.215   6.602  1.00162.54           O  
-ANISOU11887  OE1 GLU B 864    17667  22726  21363   1030    -68  -2689       O  
-ATOM  11888  OE2 GLU B 864      35.334  14.659   5.634  1.00163.33           O  
-ANISOU11888  OE2 GLU B 864    17748  23096  21214   1436   -200  -2792       O  
-ATOM  11889  N   GLN B 865      30.606  12.329   3.980  1.00157.01           N  
-ANISOU11889  N   GLN B 865    18100  20888  20669   1636   -587  -1986       N  
-ATOM  11890  CA  GLN B 865      30.766  10.917   3.673  1.00154.35           C  
-ANISOU11890  CA  GLN B 865    17925  20540  20181   1909   -697  -1962       C  
-ATOM  11891  C   GLN B 865      31.519  10.691   2.371  1.00153.11           C  
-ANISOU11891  C   GLN B 865    17750  20481  19942   1965   -644  -1995       C  
-ATOM  11892  O   GLN B 865      31.912  11.639   1.692  1.00154.61           O  
-ANISOU11892  O   GLN B 865    17806  20743  20194   1787   -523  -2046       O  
-ATOM  11893  CB  GLN B 865      29.404  10.230   3.620  1.00153.51           C  
-ANISOU11893  CB  GLN B 865    18117  20113  20098   1925   -785  -1797       C  
-ATOM  11894  CG  GLN B 865      28.463  10.801   2.580  1.00149.76           C  
-ANISOU11894  CG  GLN B 865    17746  19425  19731   1722   -726  -1669       C  
-ATOM  11895  CD  GLN B 865      27.144  10.064   2.542  1.00147.62           C  
-ANISOU11895  CD  GLN B 865    17748  18893  19447   1733   -809  -1536       C  
-ATOM  11896  OE1 GLN B 865      26.788   9.361   3.487  1.00145.96           O  
-ANISOU11896  OE1 GLN B 865    17651  18620  19187   1834   -899  -1540       O  
-ATOM  11897  NE2 GLN B 865      26.414  10.212   1.446  1.00146.86           N  
-ANISOU11897  NE2 GLN B 865    17763  18656  19381   1626   -772  -1430       N  
-ATOM  11898  N   ASP B 866      31.714   9.422   2.032  1.00152.62           N  
-ANISOU11898  N   ASP B 866    17847  20410  19733   2211   -723  -1968       N  
-ATOM  11899  CA  ASP B 866      32.455   9.043   0.838  1.00150.28           C  
-ANISOU11899  CA  ASP B 866    17550  20205  19346   2294   -687  -1994       C  
-ATOM  11900  C   ASP B 866      31.576   9.062  -0.410  1.00143.66           C  
-ANISOU11900  C   ASP B 866    16901  19100  18584   2157   -655  -1845       C  
-ATOM  11901  O   ASP B 866      32.063   9.282  -1.518  1.00143.21           O  
-ANISOU11901  O   ASP B 866    16798  19087  18528   2105   -588  -1864       O  
-ATOM  11902  CB  ASP B 866      33.088   7.664   1.031  1.00154.13           C  
-ANISOU11902  CB  ASP B 866    18138  20805  19619   2635   -770  -2025       C  
-ATOM  11903  CG  ASP B 866      32.242   6.754   1.905  1.00156.40           C  
-ANISOU11903  CG  ASP B 866    18675  20901  19848   2777   -862  -1938       C  
-ATOM  11904  OD1 ASP B 866      32.262   6.931   3.142  1.00158.21           O  
-ANISOU11904  OD1 ASP B 866    18819  21208  20085   2816   -902  -1998       O  
-ATOM  11905  OD2 ASP B 866      31.562   5.860   1.358  1.00157.12           O  
-ANISOU11905  OD2 ASP B 866    19056  20766  19878   2837   -885  -1818       O  
-ATOM  11906  N   GLN B 867      30.279   8.839  -0.223  1.00145.32           N  
-ANISOU11906  N   GLN B 867    17317  19048  18849   2095   -702  -1706       N  
-ATOM  11907  CA  GLN B 867      29.339   8.830  -1.340  1.00136.04           C  
-ANISOU11907  CA  GLN B 867    16314  17649  17726   1971   -674  -1567       C  
-ATOM  11908  C   GLN B 867      28.882  10.239  -1.715  1.00126.39           C  
-ANISOU11908  C   GLN B 867    14988  16366  16670   1713   -580  -1536       C  
-ATOM  11909  O   GLN B 867      29.428  10.848  -2.634  1.00125.90           O  
-ANISOU11909  O   GLN B 867    14832  16365  16640   1629   -486  -1571       O  
-ATOM  11910  CB  GLN B 867      28.137   7.933  -1.030  1.00141.36           C  
-ANISOU11910  CB  GLN B 867    17257  18104  18351   2011   -752  -1454       C  
-ATOM  11911  CG  GLN B 867      28.495   6.463  -0.863  1.00151.99           C  
-ANISOU11911  CG  GLN B 867    18790  19459  19501   2267   -808  -1467       C  
-ATOM  11912  CD  GLN B 867      27.288   5.589  -0.581  1.00158.01           C  
-ANISOU11912  CD  GLN B 867    19848  19995  20192   2271   -853  -1379       C  
-ATOM  11913  OE1 GLN B 867      27.425   4.418  -0.224  1.00162.33           O  
-ANISOU11913  OE1 GLN B 867    20599  20511  20568   2469   -881  -1392       O  
-ATOM  11914  NE2 GLN B 867      26.096   6.153  -0.743  1.00162.93           N  
-ANISOU11914  NE2 GLN B 867    20512  20469  20926   2056   -847  -1298       N  
-ATOM  11915  N   TYR B 868      27.885  10.755  -1.002  1.00 97.87           N  
-ANISOU11915  N   TYR B 868    11409  12627  13151   1594   -596  -1473       N  
-ATOM  11916  CA  TYR B 868      27.343  12.077  -1.304  1.00 87.43           C  
-ANISOU11916  CA  TYR B 868    10029  11227  11962   1375   -496  -1425       C  
-ATOM  11917  C   TYR B 868      28.248  13.202  -0.805  1.00 83.71           C  
-ANISOU11917  C   TYR B 868     9328  10925  11552   1269   -388  -1554       C  
-ATOM  11918  O   TYR B 868      27.929  13.895   0.165  1.00 84.15           O  
-ANISOU11918  O   TYR B 868     9319  10970  11686   1167   -369  -1562       O  
-ATOM  11919  CB  TYR B 868      25.931  12.224  -0.738  1.00 78.84           C  
-ANISOU11919  CB  TYR B 868     9063   9956  10936   1293   -549  -1310       C  
-ATOM  11920  CG  TYR B 868      24.910  11.337  -1.415  1.00 71.50           C  
-ANISOU11920  CG  TYR B 868     8355   8874   9938   1332   -613  -1194       C  
-ATOM  11921  CD1 TYR B 868      23.996  11.861  -2.315  1.00 67.91           C  
-ANISOU11921  CD1 TYR B 868     7969   8314   9521   1218   -562  -1084       C  
-ATOM  11922  CD2 TYR B 868      24.865   9.973  -1.158  1.00 68.68           C  
-ANISOU11922  CD2 TYR B 868     8147   8493   9456   1483   -709  -1202       C  
-ATOM  11923  CE1 TYR B 868      23.063  11.055  -2.937  1.00 63.87           C  
-ANISOU11923  CE1 TYR B 868     7637   7705   8927   1236   -610   -996       C  
-ATOM  11924  CE2 TYR B 868      23.934   9.159  -1.773  1.00 64.62           C  
-ANISOU11924  CE2 TYR B 868     7844   7853   8857   1485   -739  -1115       C  
-ATOM  11925  CZ  TYR B 868      23.036   9.706  -2.663  1.00 63.18           C  
-ANISOU11925  CZ  TYR B 868     7693   7596   8716   1352   -693  -1017       C  
-ATOM  11926  OH  TYR B 868      22.108   8.902  -3.282  1.00 61.92           O  
-ANISOU11926  OH  TYR B 868     7721   7351   8453   1338   -713   -947       O  
-ATOM  11927  N   VAL B 869      29.375  13.375  -1.488  1.00 87.93           N  
-ANISOU11927  N   VAL B 869     9746  11622  12043   1277   -307  -1664       N  
-ATOM  11928  CA  VAL B 869      30.357  14.402  -1.163  1.00 83.11           C  
-ANISOU11928  CA  VAL B 869     8917  11209  11453   1153   -174  -1824       C  
-ATOM  11929  C   VAL B 869      29.857  15.792  -1.554  1.00 78.35           C  
-ANISOU11929  C   VAL B 869     8336  10478  10955    916     -8  -1780       C  
-ATOM  11930  O   VAL B 869      29.167  15.940  -2.563  1.00 77.93           O  
-ANISOU11930  O   VAL B 869     8434  10245  10932    879     23  -1658       O  
-ATOM  11931  CB  VAL B 869      31.685  14.112  -1.891  1.00 84.13           C  
-ANISOU11931  CB  VAL B 869     8930  11555  11481   1227   -134  -1970       C  
-ATOM  11932  CG1 VAL B 869      31.412  13.503  -3.259  1.00 82.21           C  
-ANISOU11932  CG1 VAL B 869     8854  11168  11215   1289   -159  -1865       C  
-ATOM  11933  CG2 VAL B 869      32.527  15.373  -2.020  1.00 83.41           C  
-ANISOU11933  CG2 VAL B 869     8662  11623  11408   1022     59  -2133       C  
-ATOM  11934  N   PRO B 870      30.201  16.814  -0.748  1.00 66.62           N  
-ANISOU11934  N   PRO B 870     6710   9091   9510    760    112  -1878       N  
-ATOM  11935  CA  PRO B 870      29.868  18.223  -0.996  1.00 63.52           C  
-ANISOU11935  CA  PRO B 870     6353   8591   9190    533    313  -1857       C  
-ATOM  11936  C   PRO B 870      30.006  18.632  -2.463  1.00 61.88           C  
-ANISOU11936  C   PRO B 870     6245   8302   8966    476    439  -1845       C  
-ATOM  11937  O   PRO B 870      30.767  18.023  -3.214  1.00 61.97           O  
-ANISOU11937  O   PRO B 870     6219   8417   8910    562    409  -1921       O  
-ATOM  11938  CB  PRO B 870      30.901  18.966  -0.152  1.00 64.35           C  
-ANISOU11938  CB  PRO B 870     6242   8937   9270    394    450  -2059       C  
-ATOM  11939  CG  PRO B 870      31.145  18.065   0.995  1.00 64.52           C  
-ANISOU11939  CG  PRO B 870     6142   9112   9260    548    275  -2105       C  
-ATOM  11940  CD  PRO B 870      30.948  16.649   0.513  1.00 64.17           C  
-ANISOU11940  CD  PRO B 870     6206   9016   9160    800     74  -2021       C  
-ATOM  11941  N   ASN B 871      29.274  19.671  -2.854  1.00 66.45           N  
-ANISOU11941  N   ASN B 871     6956   8694   9598    341    586  -1749       N  
-ATOM  11942  CA  ASN B 871      29.222  20.090  -4.247  1.00 65.52           C  
-ANISOU11942  CA  ASN B 871     6972   8460   9464    304    707  -1712       C  
-ATOM  11943  C   ASN B 871      29.179  21.597  -4.433  1.00 66.47           C  
-ANISOU11943  C   ASN B 871     7173   8491   9593    105    979  -1737       C  
-ATOM  11944  O   ASN B 871      28.461  22.305  -3.728  1.00 66.28           O  
-ANISOU11944  O   ASN B 871     7204   8367   9611     30   1043  -1655       O  
-ATOM  11945  CB  ASN B 871      28.011  19.473  -4.938  1.00 64.75           C  
-ANISOU11945  CB  ASN B 871     7050   8168   9385    435    572  -1499       C  
-ATOM  11946  CG  ASN B 871      28.243  18.039  -5.340  1.00 64.61           C  
-ANISOU11946  CG  ASN B 871     7017   8211   9322    608    381  -1491       C  
-ATOM  11947  OD1 ASN B 871      29.302  17.693  -5.866  1.00 63.82           O  
-ANISOU11947  OD1 ASN B 871     6837   8239   9172    635    397  -1615       O  
-ATOM  11948  ND2 ASN B 871      27.252  17.189  -5.095  1.00 64.40           N  
-ANISOU11948  ND2 ASN B 871     7077   8094   9297    721    210  -1352       N  
-ATOM  11949  N   ASN B 872      29.939  22.072  -5.415  1.00 59.93           N  
-ANISOU11949  N   ASN B 872     6373   7684   8713     21   1148  -1850       N  
-ATOM  11950  CA  ASN B 872      29.973  23.485  -5.760  1.00 61.56           C  
-ANISOU11950  CA  ASN B 872     6711   7784   8896   -166   1443  -1889       C  
-ATOM  11951  C   ASN B 872      28.922  23.838  -6.809  1.00 59.41           C  
-ANISOU11951  C   ASN B 872     6690   7253   8631    -97   1491  -1692       C  
-ATOM  11952  O   ASN B 872      28.582  23.024  -7.664  1.00 57.88           O  
-ANISOU11952  O   ASN B 872     6542   7006   8442     52   1340  -1593       O  
-ATOM  11953  CB  ASN B 872      31.371  23.862  -6.251  1.00 65.33           C  
-ANISOU11953  CB  ASN B 872     7105   8425   9293   -310   1626  -2144       C  
-ATOM  11954  CG  ASN B 872      32.451  23.487  -5.257  1.00 68.49           C  
-ANISOU11954  CG  ASN B 872     7228   9139   9655   -358   1576  -2356       C  
-ATOM  11955  OD1 ASN B 872      32.380  23.853  -4.083  1.00 70.97           O  
-ANISOU11955  OD1 ASN B 872     7453   9530   9984   -440   1609  -2384       O  
-ATOM  11956  ND2 ASN B 872      33.446  22.736  -5.714  1.00 70.93           N  
-ANISOU11956  ND2 ASN B 872     7397   9646   9906   -292   1493  -2504       N  
-ATOM  11957  N   THR B 873      28.407  25.058  -6.739  1.00 56.41           N  
-ANISOU11957  N   THR B 873     6476   6722   8234   -200   1714  -1634       N  
-ATOM  11958  CA  THR B 873      27.378  25.494  -7.668  1.00 55.58           C  
-ANISOU11958  CA  THR B 873     6615   6393   8108   -109   1777  -1446       C  
-ATOM  11959  C   THR B 873      27.511  26.976  -7.966  1.00 59.00           C  
-ANISOU11959  C   THR B 873     7255   6695   8466   -258   2131  -1491       C  
-ATOM  11960  O   THR B 873      27.272  27.807  -7.094  1.00 57.91           O  
-ANISOU11960  O   THR B 873     7163   6519   8321   -365   2278  -1481       O  
-ATOM  11961  CB  THR B 873      25.981  25.237  -7.104  1.00 52.56           C  
-ANISOU11961  CB  THR B 873     6275   5925   7770     23   1608  -1223       C  
-ATOM  11962  OG1 THR B 873      25.823  23.835  -6.855  1.00 49.39           O  
-ANISOU11962  OG1 THR B 873     5724   5625   7417    152   1304  -1189       O  
-ATOM  11963  CG2 THR B 873      24.919  25.703  -8.084  1.00 50.15           C  
-ANISOU11963  CG2 THR B 873     6203   5438   7414    139   1677  -1038       C  
-ATOM  11964  N   ASP B 874      27.886  27.300  -9.200  1.00 68.71           N  
-ANISOU11964  N   ASP B 874     8629   7842   9634   -268   2281  -1542       N  
-ATOM  11965  CA  ASP B 874      28.045  28.688  -9.612  1.00 74.33           C  
-ANISOU11965  CA  ASP B 874     9593   8403  10247   -401   2647  -1597       C  
-ATOM  11966  C   ASP B 874      27.085  29.052 -10.740  1.00 73.72           C  
-ANISOU11966  C   ASP B 874     9789   8105  10115   -230   2710  -1404       C  
-ATOM  11967  O   ASP B 874      27.272  28.646 -11.884  1.00 73.02           O  
-ANISOU11967  O   ASP B 874     9743   7986  10016   -151   2666  -1410       O  
-ATOM  11968  CB  ASP B 874      29.490  28.953 -10.041  1.00 82.09           C  
-ANISOU11968  CB  ASP B 874    10535   9485  11169   -601   2838  -1881       C  
-ATOM  11969  CG  ASP B 874      29.716  30.387 -10.500  1.00 89.96           C  
-ANISOU11969  CG  ASP B 874    11832  10311  12039   -764   3254  -1968       C  
-ATOM  11970  OD1 ASP B 874      28.877  30.924 -11.256  1.00 97.61           O  
-ANISOU11970  OD1 ASP B 874    13083  11049  12956   -637   3363  -1798       O  
-ATOM  11971  OD2 ASP B 874      30.741  30.980 -10.103  1.00 93.69           O  
-ANISOU11971  OD2 ASP B 874    12267  10889  12443  -1018   3487  -2216       O  
-ATOM  11972  N   LEU B 875      26.058  29.826 -10.413  1.00 59.62           N  
-ANISOU11972  N   LEU B 875     8188   6179   8286   -165   2817  -1233       N  
-ATOM  11973  CA  LEU B 875      25.134  30.330 -11.420  1.00 60.04           C  
-ANISOU11973  CA  LEU B 875     8517   6045   8250     17   2915  -1054       C  
-ATOM  11974  C   LEU B 875      24.923  31.825 -11.240  1.00 67.63           C  
-ANISOU11974  C   LEU B 875     9782   6829   9086    -53   3288  -1035       C  
-ATOM  11975  O   LEU B 875      23.874  32.263 -10.773  1.00 68.31           O  
-ANISOU11975  O   LEU B 875     9977   6841   9138     61   3302   -850       O  
-ATOM  11976  CB  LEU B 875      23.797  29.601 -11.341  1.00 50.86           C  
-ANISOU11976  CB  LEU B 875     7290   4908   7126    255   2624   -814       C  
-ATOM  11977  CG  LEU B 875      23.833  28.089 -11.541  1.00 42.31           C  
-ANISOU11977  CG  LEU B 875     5958   3977   6141    338   2273   -809       C  
-ATOM  11978  CD1 LEU B 875      23.037  27.398 -10.451  1.00 41.01           C  
-ANISOU11978  CD1 LEU B 875     5625   3909   6048    398   2015   -703       C  
-ATOM  11979  CD2 LEU B 875      23.300  27.724 -12.911  1.00 42.24           C  
-ANISOU11979  CD2 LEU B 875     6049   3919   6083    521   2209   -695       C  
-ATOM  11980  N   SER B 876      25.930  32.604 -11.615  1.00 76.90           N  
-ANISOU11980  N   SER B 876    11107   7936  10176   -247   3604  -1234       N  
-ATOM  11981  CA  SER B 876      25.866  34.050 -11.472  1.00 85.96           C  
-ANISOU11981  CA  SER B 876    12586   8900  11176   -346   4015  -1246       C  
-ATOM  11982  C   SER B 876      25.554  34.694 -12.810  1.00 92.39           C  
-ANISOU11982  C   SER B 876    13761   9497  11846   -197   4232  -1176       C  
-ATOM  11983  O   SER B 876      25.332  34.005 -13.802  1.00 92.31           O  
-ANISOU11983  O   SER B 876    13714   9495  11865    -19   4043  -1109       O  
-ATOM  11984  CB  SER B 876      27.195  34.583 -10.939  1.00 84.70           C  
-ANISOU11984  CB  SER B 876    12389   8813  10980   -693   4277  -1542       C  
-ATOM  11985  OG  SER B 876      28.269  34.177 -11.770  1.00 81.94           O  
-ANISOU11985  OG  SER B 876    11963   8539  10632   -794   4280  -1757       O  
-ATOM  11986  N   GLU B 877      25.533  36.022 -12.829  1.00119.29           N  
-ANISOU11986  N   GLU B 877    17533  12707  15085   -267   4643  -1193       N  
-ATOM  11987  CA  GLU B 877      25.384  36.759 -14.072  1.00125.05           C  
-ANISOU11987  CA  GLU B 877    18656  13211  15648   -142   4912  -1161       C  
-ATOM  11988  C   GLU B 877      26.751  36.863 -14.731  1.00126.38           C  
-ANISOU11988  C   GLU B 877    18864  13369  15786   -390   5102  -1459       C  
-ATOM  11989  O   GLU B 877      26.870  36.811 -15.956  1.00126.56           O  
-ANISOU11989  O   GLU B 877    19040  13287  15760   -288   5142  -1474       O  
-ATOM  11990  CB  GLU B 877      24.817  38.153 -13.806  1.00133.72           C  
-ANISOU11990  CB  GLU B 877    20174  14086  16548   -107   5307  -1060       C  
-ATOM  11991  CG  GLU B 877      24.263  38.844 -15.042  1.00144.45           C  
-ANISOU11991  CG  GLU B 877    21960  15209  17714    148   5532   -938       C  
-ATOM  11992  CD  GLU B 877      22.922  38.280 -15.471  1.00149.15           C  
-ANISOU11992  CD  GLU B 877    22491  15854  18326    548   5224   -643       C  
-ATOM  11993  OE1 GLU B 877      22.417  37.363 -14.790  1.00152.47           O  
-ANISOU11993  OE1 GLU B 877    22551  16475  18904    604   4848   -541       O  
-ATOM  11994  OE2 GLU B 877      22.371  38.756 -16.485  1.00153.20           O  
-ANISOU11994  OE2 GLU B 877    23319  16215  18675    805   5368   -522       O  
-ATOM  11995  N   ASP B 878      27.782  37.000 -13.902  1.00101.15           N  
-ANISOU11995  N   ASP B 878    15518  10301  12615   -720   5217  -1706       N  
-ATOM  11996  CA  ASP B 878      29.159  37.038 -14.374  1.00101.73           C  
-ANISOU11996  CA  ASP B 878    15568  10430  12654   -992   5380  -2029       C  
-ATOM  11997  C   ASP B 878      29.650  35.636 -14.713  1.00 98.62           C  
-ANISOU11997  C   ASP B 878    14775  10261  12436   -950   4972  -2091       C  
-ATOM  11998  O   ASP B 878      30.849  35.377 -14.744  1.00101.49           O  
-ANISOU11998  O   ASP B 878    14968  10782  12813  -1183   4999  -2369       O  
-ATOM  11999  CB  ASP B 878      30.061  37.680 -13.331  1.00106.68           C  
-ANISOU11999  CB  ASP B 878    16152  11165  13218  -1362   5653  -2282       C  
-ATOM  12000  N   SER B 879      28.711  34.732 -14.961  1.00112.28           N  
-ANISOU12000  N   SER B 879    16363  12018  14281   -653   4607  -1838       N  
-ATOM  12001  CA  SER B 879      29.043  33.371 -15.355  1.00105.09           C  
-ANISOU12001  CA  SER B 879    15123  11288  13520   -582   4232  -1860       C  
-ATOM  12002  C   SER B 879      27.864  32.758 -16.095  1.00 99.31           C  
-ANISOU12002  C   SER B 879    14418  10483  12831   -248   3979  -1574       C  
-ATOM  12003  O   SER B 879      27.103  33.459 -16.762  1.00 98.31           O  
-ANISOU12003  O   SER B 879    14607  10155  12592    -83   4146  -1425       O  
-ATOM  12004  CB  SER B 879      29.409  32.522 -14.132  1.00104.89           C  
-ANISOU12004  CB  SER B 879    14691  11538  13624   -674   3966  -1925       C  
-ATOM  12005  OG  SER B 879      29.807  31.213 -14.507  1.00103.78           O  
-ANISOU12005  OG  SER B 879    14264  11565  13601   -603   3635  -1957       O  
-ATOM  12006  N   GLU B 880      27.708  31.449 -15.963  1.00 84.99           N  
-ANISOU12006  N   GLU B 880    12282   8850  11161   -146   3590  -1503       N  
-ATOM  12007  CA  GLU B 880      26.654  30.747 -16.671  1.00 80.34           C  
-ANISOU12007  CA  GLU B 880    11685   8237  10605    133   3345  -1263       C  
-ATOM  12008  C   GLU B 880      25.342  30.778 -15.909  1.00 76.89           C  
-ANISOU12008  C   GLU B 880    11239   7813  10164    306   3224  -1026       C  
-ATOM  12009  O   GLU B 880      25.319  30.726 -14.681  1.00 75.37           O  
-ANISOU12009  O   GLU B 880    10897   7717  10024    217   3161  -1040       O  
-ATOM  12010  CB  GLU B 880      27.083  29.314 -16.952  1.00 77.40           C  
-ANISOU12010  CB  GLU B 880    11009   8037  10363    152   3014  -1302       C  
-ATOM  12011  CG  GLU B 880      28.078  28.794 -15.948  1.00 76.55           C  
-ANISOU12011  CG  GLU B 880    10618   8132  10337    -38   2915  -1494       C  
-ATOM  12012  CD  GLU B 880      28.745  27.526 -16.413  1.00 74.70           C  
-ANISOU12012  CD  GLU B 880    10150   8042  10191    -27   2665  -1570       C  
-ATOM  12013  OE1 GLU B 880      28.375  27.021 -17.493  1.00 73.13           O  
-ANISOU12013  OE1 GLU B 880    10004   7778  10005    113   2562  -1461       O  
-ATOM  12014  OE2 GLU B 880      29.642  27.040 -15.698  1.00 74.22           O  
-ANISOU12014  OE2 GLU B 880     9856   8170  10175   -150   2581  -1738       O  
-ATOM  12015  N   ARG B 881      24.249  30.868 -16.655  1.00 89.32           N  
-ANISOU12015  N   ARG B 881    12969   9302  11665    554   3195   -815       N  
-ATOM  12016  CA AARG B 881      22.919  30.907 -16.067  0.50 77.89           C  
-ANISOU12016  CA AARG B 881    11523   7886  10187    741   3080   -592       C  
-ATOM  12017  CA BARG B 881      22.920  30.908 -16.066  0.50 77.82           C  
-ANISOU12017  CA BARG B 881    11514   7877  10178    741   3080   -592       C  
-ATOM  12018  C   ARG B 881      22.269  29.532 -16.118  1.00 69.02           C  
-ANISOU12018  C   ARG B 881    10131   6938   9155    873   2692   -477       C  
-ATOM  12019  O   ARG B 881      21.453  29.191 -15.268  1.00 61.77           O  
-ANISOU12019  O   ARG B 881     9090   6115   8263    938   2516   -364       O  
-ATOM  12020  CB AARG B 881      22.050  31.920 -16.812  0.50 86.18           C  
-ANISOU12020  CB AARG B 881    12918   8771  11057    956   3307   -435       C  
-ATOM  12021  CB BARG B 881      22.049  31.929 -16.800  0.50 85.73           C  
-ANISOU12021  CB BARG B 881    12861   8713  10999    955   3309   -435       C  
-ATOM  12022  CG AARG B 881      22.599  33.332 -16.787  0.50 99.38           C  
-ANISOU12022  CG AARG B 881    14923  10237  12601    836   3735   -538       C  
-ATOM  12023  CG BARG B 881      22.661  33.317 -16.890  0.50 99.13           C  
-ANISOU12023  CG BARG B 881    14897  10200  12568    834   3740   -548       C  
-ATOM  12024  CD AARG B 881      22.094  34.140 -17.967  0.50116.81           C  
-ANISOU12024  CD AARG B 881    17499  12263  14622   1057   3969   -435       C  
-ATOM  12025  CD BARG B 881      21.619  34.344 -17.300  0.50112.65           C  
-ANISOU12025  CD BARG B 881    16963  11759  14079   1089   3960   -357       C  
-ATOM  12026  NE AARG B 881      22.589  35.512 -17.931  0.50128.69           N  
-ANISOU12026  NE AARG B 881    19378  13545  15975    943   4414   -536       N  
-ATOM  12027  NE BARG B 881      21.034  34.044 -18.603  0.50127.39           N  
-ANISOU12027  NE BARG B 881    18908  13620  15874   1350   3879   -236       N  
-ATOM  12028  CZ AARG B 881      23.841  35.860 -18.208  0.50138.51           C  
-ANISOU12028  CZ AARG B 881    20719  14694  17215    683   4644   -784       C  
-ATOM  12029  CZ BARG B 881      21.397  34.636 -19.736  0.50140.62           C  
-ANISOU12029  CZ BARG B 881    20875  15121  17434   1400   4126   -287       C  
-ATOM  12030  NH1AARG B 881      24.732  34.935 -18.538  0.50143.30           N  
-ANISOU12030  NH1AARG B 881    21060  15418  17968    531   4453   -947       N  
-ATOM  12031  NH1BARG B 881      22.342  35.567 -19.725  0.50144.67           N  
-ANISOU12031  NH1BARG B 881    21645  15444  17880   1195   4481   -469       N  
-ATOM  12032  NH2AARG B 881      24.205  37.133 -18.149  0.50147.05           N  
-ANISOU12032  NH2AARG B 881    22173  15569  18129    570   5078   -878       N  
-ATOM  12033  NH2BARG B 881      20.815  34.302 -20.879  0.50153.48           N  
-ANISOU12033  NH2BARG B 881    22544  16769  19004   1646   4029   -168       N  
-ATOM  12034  N   VAL B 882      22.638  28.747 -17.124  1.00 71.28           N  
-ANISOU12034  N   VAL B 882    10343   7259   9480    899   2574   -513       N  
-ATOM  12035  CA  VAL B 882      22.061  27.422 -17.322  1.00 64.77           C  
-ANISOU12035  CA  VAL B 882     9302   6590   8718   1008   2244   -415       C  
-ATOM  12036  C   VAL B 882      23.095  26.326 -17.083  1.00 61.43           C  
-ANISOU12036  C   VAL B 882     8633   6278   8430    854   2064   -568       C  
-ATOM  12037  O   VAL B 882      24.291  26.529 -17.305  1.00 61.94           O  
-ANISOU12037  O   VAL B 882     8704   6305   8526    699   2190   -749       O  
-ATOM  12038  CB  VAL B 882      21.496  27.272 -18.735  1.00 63.36           C  
-ANISOU12038  CB  VAL B 882     9232   6383   8458   1190   2236   -302       C  
-ATOM  12039  CG1 VAL B 882      20.793  25.937 -18.891  1.00 61.86           C  
-ANISOU12039  CG1 VAL B 882     8832   6368   8304   1281   1924   -200       C  
-ATOM  12040  CG2 VAL B 882      20.550  28.417 -19.043  1.00 63.99           C  
-ANISOU12040  CG2 VAL B 882     9578   6363   8372   1379   2439   -159       C  
-ATOM  12041  N   MET B 883      22.624  25.166 -16.634  1.00 61.81           N  
-ANISOU12041  N   MET B 883     8477   6471   8536    902   1780   -501       N  
-ATOM  12042  CA  MET B 883      23.501  24.054 -16.299  1.00 56.62           C  
-ANISOU12042  CA  MET B 883     7603   5928   7982    798   1600   -624       C  
-ATOM  12043  C   MET B 883      22.903  22.747 -16.819  1.00 53.74           C  
-ANISOU12043  C   MET B 883     7138   5657   7623    907   1354   -520       C  
-ATOM  12044  O   MET B 883      22.007  22.171 -16.201  1.00 52.83           O  
-ANISOU12044  O   MET B 883     6947   5628   7498    972   1185   -421       O  
-ATOM  12045  CB  MET B 883      23.701  24.001 -14.784  1.00 55.60           C  
-ANISOU12045  CB  MET B 883     7337   5878   7909    705   1538   -689       C  
-ATOM  12046  CG  MET B 883      24.883  23.172 -14.309  1.00 55.81           C  
-ANISOU12046  CG  MET B 883     7166   6025   8015    594   1427   -860       C  
-ATOM  12047  SD  MET B 883      25.117  23.254 -12.516  1.00 55.02           S  
-ANISOU12047  SD  MET B 883     6915   6025   7966    495   1382   -939       S  
-ATOM  12048  CE  MET B 883      25.355  25.013 -12.269  1.00 56.58           C  
-ANISOU12048  CE  MET B 883     7282   6103   8113    360   1730  -1005       C  
-ATOM  12049  N   ILE B 884      23.390  22.290 -17.971  1.00 48.02           N  
-ANISOU12049  N   ILE B 884     6425   4914   6907    911   1348   -549       N  
-ATOM  12050  CA  ILE B 884      22.887  21.062 -18.575  1.00 45.79           C  
-ANISOU12050  CA  ILE B 884     6067   4714   6617    990   1150   -457       C  
-ATOM  12051  C   ILE B 884      23.598  19.853 -17.986  1.00 44.06           C  
-ANISOU12051  C   ILE B 884     5676   4597   6468    923    972   -548       C  
-ATOM  12052  O   ILE B 884      24.818  19.725 -18.101  1.00 44.22           O  
-ANISOU12052  O   ILE B 884     5643   4616   6542    835   1006   -693       O  
-ATOM  12053  CB  ILE B 884      23.081  21.050 -20.094  1.00 45.32           C  
-ANISOU12053  CB  ILE B 884     6098   4587   6536   1023   1222   -439       C  
-ATOM  12054  CG1 ILE B 884      22.612  22.366 -20.717  1.00 46.01           C  
-ANISOU12054  CG1 ILE B 884     6393   4551   6539   1103   1442   -378       C  
-ATOM  12055  CG2 ILE B 884      22.338  19.880 -20.708  1.00 45.43           C  
-ANISOU12055  CG2 ILE B 884     6049   4697   6517   1100   1044   -322       C  
-ATOM  12056  CD1 ILE B 884      22.873  22.452 -22.212  1.00 46.26           C  
-ANISOU12056  CD1 ILE B 884     6532   4494   6550   1135   1533   -373       C  
-ATOM  12057  N   ILE B 885      22.827  18.967 -17.360  1.00 50.95           N  
-ANISOU12057  N   ILE B 885     6473   5564   7321    971    790   -469       N  
-ATOM  12058  CA  ILE B 885      23.384  17.824 -16.646  1.00 49.17           C  
-ANISOU12058  CA  ILE B 885     6122   5427   7135    939    630   -542       C  
-ATOM  12059  C   ILE B 885      23.056  16.518 -17.361  1.00 49.67           C  
-ANISOU12059  C   ILE B 885     6178   5538   7155    983    496   -474       C  
-ATOM  12060  O   ILE B 885      21.891  16.234 -17.651  1.00 49.88           O  
-ANISOU12060  O   ILE B 885     6246   5599   7108   1036    444   -351       O  
-ATOM  12061  CB  ILE B 885      22.823  17.733 -15.213  1.00 47.42           C  
-ANISOU12061  CB  ILE B 885     5845   5259   6914    942    537   -527       C  
-ATOM  12062  CG1 ILE B 885      22.754  19.116 -14.562  1.00 45.74           C  
-ANISOU12062  CG1 ILE B 885     5669   4989   6720    902    685   -546       C  
-ATOM  12063  CG2 ILE B 885      23.664  16.791 -14.369  1.00 46.27           C  
-ANISOU12063  CG2 ILE B 885     5586   5190   6803    919    416   -636       C  
-ATOM  12064  CD1 ILE B 885      23.995  19.486 -13.792  1.00 43.97           C  
-ANISOU12064  CD1 ILE B 885     5361   4785   6561    798    755   -714       C  
-ATOM  12065  N   THR B 886      24.082  15.721 -17.641  1.00 49.81           N  
-ANISOU12065  N   THR B 886     6145   5576   7205    957    451   -559       N  
-ATOM  12066  CA  THR B 886      23.886  14.443 -18.310  1.00 49.58           C  
-ANISOU12066  CA  THR B 886     6130   5580   7129    985    348   -499       C  
-ATOM  12067  C   THR B 886      24.498  13.334 -17.479  1.00 48.92           C  
-ANISOU12067  C   THR B 886     5987   5562   7037   1000    228   -570       C  
-ATOM  12068  O   THR B 886      25.351  13.585 -16.627  1.00 48.56           O  
-ANISOU12068  O   THR B 886     5865   5551   7036    991    230   -687       O  
-ATOM  12069  CB  THR B 886      24.537  14.416 -19.704  1.00 50.03           C  
-ANISOU12069  CB  THR B 886     6219   5581   7211    963    421   -513       C  
-ATOM  12070  OG1 THR B 886      25.936  14.702 -19.584  1.00 52.74           O  
-ANISOU12070  OG1 THR B 886     6502   5914   7622    915    475   -669       O  
-ATOM  12071  CG2 THR B 886      23.890  15.437 -20.635  1.00 51.17           C  
-ANISOU12071  CG2 THR B 886     6449   5652   7340    977    547   -434       C  
-ATOM  12072  N   GLY B 887      24.068  12.106 -17.735  1.00 53.57           N  
-ANISOU12072  N   GLY B 887     6624   6180   7552   1026    137   -504       N  
-ATOM  12073  CA  GLY B 887      24.560  10.968 -16.988  1.00 53.72           C  
-ANISOU12073  CA  GLY B 887     6637   6246   7529   1068     38   -557       C  
-ATOM  12074  C   GLY B 887      23.425  10.052 -16.582  1.00 53.61           C  
-ANISOU12074  C   GLY B 887     6710   6255   7405   1078    -42   -476       C  
-ATOM  12075  O   GLY B 887      22.253  10.412 -16.719  1.00 51.72           O  
-ANISOU12075  O   GLY B 887     6499   6025   7129   1047    -32   -395       O  
-ATOM  12076  N   PRO B 888      23.764   8.860 -16.075  1.00 41.71           N  
-ANISOU12076  N   PRO B 888     5256   4766   5825   1127   -112   -508       N  
-ATOM  12077  CA  PRO B 888      22.754   7.873 -15.691  1.00 42.10           C  
-ANISOU12077  CA  PRO B 888     5427   4825   5744   1117   -164   -457       C  
-ATOM  12078  C   PRO B 888      21.949   8.343 -14.479  1.00 42.69           C  
-ANISOU12078  C   PRO B 888     5482   4917   5821   1107   -213   -468       C  
-ATOM  12079  O   PRO B 888      22.418   9.170 -13.688  1.00 39.69           O  
-ANISOU12079  O   PRO B 888     5003   4540   5539   1130   -221   -527       O  
-ATOM  12080  CB  PRO B 888      23.589   6.634 -15.336  1.00 40.45           C  
-ANISOU12080  CB  PRO B 888     5301   4611   5457   1200   -201   -508       C  
-ATOM  12081  CG  PRO B 888      24.955   6.895 -15.907  1.00 40.25           C  
-ANISOU12081  CG  PRO B 888     5184   4594   5515   1246   -169   -565       C  
-ATOM  12082  CD  PRO B 888      25.130   8.370 -15.837  1.00 39.72           C  
-ANISOU12082  CD  PRO B 888     4970   4538   5585   1202   -131   -605       C  
-ATOM  12083  N   ASN B 889      20.735   7.819 -14.348  1.00 50.31           N  
-ANISOU12083  N   ASN B 889     6540   5903   6671   1057   -237   -420       N  
-ATOM  12084  CA  ASN B 889      19.868   8.190 -13.244  1.00 52.53           C  
-ANISOU12084  CA  ASN B 889     6813   6201   6945   1036   -289   -430       C  
-ATOM  12085  C   ASN B 889      20.333   7.602 -11.918  1.00 54.97           C  
-ANISOU12085  C   ASN B 889     7165   6479   7242   1093   -359   -513       C  
-ATOM  12086  O   ASN B 889      19.873   6.536 -11.508  1.00 54.85           O  
-ANISOU12086  O   ASN B 889     7295   6450   7095   1085   -389   -530       O  
-ATOM  12087  CB  ASN B 889      18.419   7.785 -13.528  1.00 51.33           C  
-ANISOU12087  CB  ASN B 889     6742   6111   6651    952   -290   -379       C  
-ATOM  12088  CG  ASN B 889      17.700   8.782 -14.409  1.00 49.02           C  
-ANISOU12088  CG  ASN B 889     6366   5884   6374    926   -239   -301       C  
-ATOM  12089  OD1 ASN B 889      18.168   9.901 -14.599  1.00 47.67           O  
-ANISOU12089  OD1 ASN B 889     6103   5683   6328    968   -199   -284       O  
-ATOM  12090  ND2 ASN B 889      16.548   8.388 -14.937  1.00 48.25           N  
-ANISOU12090  ND2 ASN B 889     6313   5891   6130    860   -226   -263       N  
-ATOM  12091  N   MET B 890      21.255   8.294 -11.258  1.00 60.27           N  
-ANISOU12091  N   MET B 890     7720   7145   8035   1149   -370   -572       N  
-ATOM  12092  CA AMET B 890      21.698   7.879  -9.935  0.50 64.16           C  
-ANISOU12092  CA AMET B 890     8225   7631   8520   1220   -437   -653       C  
-ATOM  12093  CA BMET B 890      21.728   7.894  -9.939  0.50 64.32           C  
-ANISOU12093  CA BMET B 890     8243   7653   8544   1221   -437   -654       C  
-ATOM  12094  C   MET B 890      21.169   8.848  -8.880  1.00 64.22           C  
-ANISOU12094  C   MET B 890     8148   7637   8616   1176   -468   -664       C  
-ATOM  12095  O   MET B 890      20.775   9.981  -9.191  1.00 64.84           O  
-ANISOU12095  O   MET B 890     8141   7721   8776   1113   -420   -619       O  
-ATOM  12096  CB AMET B 890      23.224   7.790  -9.861  0.50 71.41           C  
-ANISOU12096  CB AMET B 890     9062   8589   9480   1324   -430   -733       C  
-ATOM  12097  CB BMET B 890      23.257   7.899  -9.895  0.50 71.86           C  
-ANISOU12097  CB BMET B 890     9106   8649   9549   1320   -425   -734       C  
-ATOM  12098  CG AMET B 890      23.924   9.128  -9.710  0.50 75.19           C  
-ANISOU12098  CG AMET B 890     9349   9114  10105   1297   -386   -785       C  
-ATOM  12099  CG BMET B 890      23.914   7.264 -11.108  0.50 74.80           C  
-ANISOU12099  CG BMET B 890     9524   9026   9872   1355   -381   -717       C  
-ATOM  12100  SD AMET B 890      25.326   9.026  -8.583  0.50 78.89           S  
-ANISOU12100  SD AMET B 890     9699   9686  10588   1413   -421   -930       S  
-ATOM  12101  SD BMET B 890      23.667   5.484 -11.216  0.50 67.00           S  
-ANISOU12101  SD BMET B 890     8783   7992   8682   1420   -398   -690       S  
-ATOM  12102  CE AMET B 890      25.925  10.704  -8.625  0.50 84.10           C  
-ANISOU12102  CE AMET B 890    10157  10402  11396   1307   -320   -995       C  
-ATOM  12103  CE BMET B 890      24.850   4.903 -10.007  0.50 76.94           C  
-ANISOU12103  CE BMET B 890    10042   9299   9892   1614   -454   -799       C  
-ATOM  12104  N   GLY B 891      21.148   8.395  -7.631  1.00 66.08           N  
-ANISOU12104  N   GLY B 891     8424   7857   8826   1215   -539   -722       N  
-ATOM  12105  CA  GLY B 891      20.645   9.201  -6.534  1.00 65.41           C  
-ANISOU12105  CA  GLY B 891     8268   7760   8825   1168   -575   -734       C  
-ATOM  12106  C   GLY B 891      21.459  10.454  -6.262  1.00 65.63           C  
-ANISOU12106  C   GLY B 891     8113   7825   9000   1158   -524   -769       C  
-ATOM  12107  O   GLY B 891      20.931  11.447  -5.759  1.00 66.29           O  
-ANISOU12107  O   GLY B 891     8133   7891   9165   1086   -508   -744       O  
-ATOM  12108  N   GLY B 892      22.747  10.409  -6.588  1.00 66.27           N  
-ANISOU12108  N   GLY B 892     8116   7964   9101   1221   -487   -834       N  
-ATOM  12109  CA  GLY B 892      23.634  11.537  -6.350  1.00 64.10           C  
-ANISOU12109  CA  GLY B 892     7671   7748   8936   1189   -414   -902       C  
-ATOM  12110  C   GLY B 892      23.374  12.707  -7.278  1.00 61.30           C  
-ANISOU12110  C   GLY B 892     7284   7361   8647   1092   -297   -845       C  
-ATOM  12111  O   GLY B 892      23.690  13.856  -6.961  1.00 60.08           O  
-ANISOU12111  O   GLY B 892     7033   7218   8575   1022   -208   -882       O  
-ATOM  12112  N   LYS B 893      22.801  12.411  -8.437  1.00 49.77           N  
-ANISOU12112  N   LYS B 893     5916   5859   7134   1090   -281   -757       N  
-ATOM  12113  CA  LYS B 893      22.441  13.450  -9.385  1.00 47.31           C  
-ANISOU12113  CA  LYS B 893     5606   5511   6860   1029   -169   -690       C  
-ATOM  12114  C   LYS B 893      21.210  14.177  -8.862  1.00 46.31           C  
-ANISOU12114  C   LYS B 893     5506   5346   6744    985   -168   -609       C  
-ATOM  12115  O   LYS B 893      21.208  15.398  -8.713  1.00 47.28           O  
-ANISOU12115  O   LYS B 893     5594   5442   6930    939    -65   -601       O  
-ATOM  12116  CB  LYS B 893      22.159  12.839 -10.755  1.00 44.78           C  
-ANISOU12116  CB  LYS B 893     5370   5178   6468   1050   -161   -620       C  
-ATOM  12117  CG  LYS B 893      22.066  13.850 -11.880  1.00 40.84           C  
-ANISOU12117  CG  LYS B 893     4875   4643   5998   1017    -34   -568       C  
-ATOM  12118  CD  LYS B 893      21.749  13.176 -13.203  1.00 38.25           C  
-ANISOU12118  CD  LYS B 893     4620   4314   5598   1035    -34   -497       C  
-ATOM  12119  CE  LYS B 893      20.412  12.458 -13.148  1.00 37.73           C  
-ANISOU12119  CE  LYS B 893     4630   4282   5424   1036   -115   -413       C  
-ATOM  12120  NZ  LYS B 893      20.063  11.842 -14.450  1.00 38.34           N  
-ANISOU12120  NZ  LYS B 893     4768   4382   5418   1033    -97   -348       N  
-ATOM  12121  N   SER B 894      20.164  13.412  -8.575  1.00 51.11           N  
-ANISOU12121  N   SER B 894     6190   5954   7274    996   -270   -558       N  
-ATOM  12122  CA  SER B 894      18.948  13.970  -8.006  1.00 48.86           C  
-ANISOU12122  CA  SER B 894     5925   5657   6983    960   -290   -493       C  
-ATOM  12123  C   SER B 894      19.268  14.801  -6.775  1.00 46.45           C  
-ANISOU12123  C   SER B 894     5541   5324   6782    923   -273   -538       C  
-ATOM  12124  O   SER B 894      18.780  15.919  -6.633  1.00 44.44           O  
-ANISOU12124  O   SER B 894     5278   5043   6566    889   -197   -483       O  
-ATOM  12125  CB  SER B 894      17.966  12.857  -7.645  1.00 49.28           C  
-ANISOU12125  CB  SER B 894     6067   5732   6927    954   -409   -483       C  
-ATOM  12126  OG  SER B 894      16.782  12.952  -8.424  1.00 50.97           O  
-ANISOU12126  OG  SER B 894     6327   5997   7043    940   -396   -398       O  
-ATOM  12127  N   SER B 895      20.096  14.259  -5.888  1.00 54.39           N  
-ANISOU12127  N   SER B 895     6499   6344   7822    936   -332   -637       N  
-ATOM  12128  CA  SER B 895      20.483  14.977  -4.679  1.00 54.43           C  
-ANISOU12128  CA  SER B 895     6412   6346   7924    890   -314   -693       C  
-ATOM  12129  C   SER B 895      21.023  16.365  -4.977  1.00 56.10           C  
-ANISOU12129  C   SER B 895     6558   6551   8207    826   -144   -700       C  
-ATOM  12130  O   SER B 895      20.622  17.339  -4.341  1.00 55.88           O  
-ANISOU12130  O   SER B 895     6515   6483   8232    760    -83   -670       O  
-ATOM  12131  CB  SER B 895      21.517  14.186  -3.880  1.00 54.03           C  
-ANISOU12131  CB  SER B 895     6301   6352   7877    943   -385   -812       C  
-ATOM  12132  OG  SER B 895      20.879  13.261  -3.014  1.00 54.57           O  
-ANISOU12132  OG  SER B 895     6446   6390   7899    976   -519   -814       O  
-ATOM  12133  N   TYR B 896      21.933  16.454  -5.943  1.00 38.22           N  
-ANISOU12133  N   TYR B 896     4271   4316   5933    838    -56   -746       N  
-ATOM  12134  CA  TYR B 896      22.552  17.728  -6.277  1.00 39.90           C  
-ANISOU12134  CA  TYR B 896     4452   4518   6192    761    133   -783       C  
-ATOM  12135  C   TYR B 896      21.525  18.707  -6.839  1.00 39.39           C  
-ANISOU12135  C   TYR B 896     4496   4361   6109    747    237   -654       C  
-ATOM  12136  O   TYR B 896      21.489  19.878  -6.457  1.00 39.52           O  
-ANISOU12136  O   TYR B 896     4525   4330   6159    676    379   -647       O  
-ATOM  12137  CB  TYR B 896      23.701  17.541  -7.264  1.00 41.77           C  
-ANISOU12137  CB  TYR B 896     4656   4804   6410    771    200   -871       C  
-ATOM  12138  CG  TYR B 896      24.258  18.856  -7.739  1.00 45.65           C  
-ANISOU12138  CG  TYR B 896     5154   5266   6924    674    419   -921       C  
-ATOM  12139  CD1 TYR B 896      25.209  19.538  -6.994  1.00 45.83           C  
-ANISOU12139  CD1 TYR B 896     5073   5359   6982    569    531  -1063       C  
-ATOM  12140  CD2 TYR B 896      23.811  19.435  -8.921  1.00 47.05           C  
-ANISOU12140  CD2 TYR B 896     5457   5350   7071    683    532   -835       C  
-ATOM  12141  CE1 TYR B 896      25.711  20.752  -7.421  1.00 47.95           C  
-ANISOU12141  CE1 TYR B 896     5379   5592   7247    453    765  -1127       C  
-ATOM  12142  CE2 TYR B 896      24.303  20.648  -9.354  1.00 47.57           C  
-ANISOU12142  CE2 TYR B 896     5574   5363   7137    596    758   -888       C  
-ATOM  12143  CZ  TYR B 896      25.251  21.300  -8.598  1.00 48.92           C  
-ANISOU12143  CZ  TYR B 896     5660   5591   7336    470    881  -1038       C  
-ATOM  12144  OH  TYR B 896      25.755  22.503  -9.019  1.00 51.38           O  
-ANISOU12144  OH  TYR B 896     6051   5845   7626    357   1135  -1111       O  
-ATOM  12145  N   ILE B 897      20.693  18.221  -7.748  1.00 46.27           N  
-ANISOU12145  N   ILE B 897     5453   5219   6910    821    180   -552       N  
-ATOM  12146  CA  ILE B 897      19.611  19.018  -8.298  1.00 45.62           C  
-ANISOU12146  CA  ILE B 897     5469   5087   6776    852    258   -424       C  
-ATOM  12147  C   ILE B 897      18.791  19.653  -7.179  1.00 45.62           C  
-ANISOU12147  C   ILE B 897     5475   5060   6798    823    250   -372       C  
-ATOM  12148  O   ILE B 897      18.578  20.868  -7.157  1.00 46.07           O  
-ANISOU12148  O   ILE B 897     5591   5057   6856    807    406   -322       O  
-ATOM  12149  CB  ILE B 897      18.695  18.142  -9.161  1.00 45.47           C  
-ANISOU12149  CB  ILE B 897     5504   5115   6657    932    152   -338       C  
-ATOM  12150  CG1 ILE B 897      19.503  17.497 -10.281  1.00 46.71           C  
-ANISOU12150  CG1 ILE B 897     5661   5287   6798    952    163   -380       C  
-ATOM  12151  CG2 ILE B 897      17.586  18.956  -9.751  1.00 44.50           C  
-ANISOU12151  CG2 ILE B 897     5465   4987   6455    993    229   -213       C  
-ATOM  12152  CD1 ILE B 897      20.295  18.501 -11.079  1.00 51.25           C  
-ANISOU12152  CD1 ILE B 897     6265   5803   7404    934    349   -407       C  
-ATOM  12153  N   LYS B 898      18.342  18.821  -6.244  1.00 43.74           N  
-ANISOU12153  N   LYS B 898     5195   4856   6570    816     80   -385       N  
-ATOM  12154  CA  LYS B 898      17.513  19.284  -5.142  1.00 41.04           C  
-ANISOU12154  CA  LYS B 898     4852   4486   6254    782     46   -340       C  
-ATOM  12155  C   LYS B 898      18.323  20.167  -4.196  1.00 41.85           C  
-ANISOU12155  C   LYS B 898     4895   4545   6462    686    157   -406       C  
-ATOM  12156  O   LYS B 898      17.874  21.245  -3.818  1.00 42.39           O  
-ANISOU12156  O   LYS B 898     5006   4556   6546    651    267   -343       O  
-ATOM  12157  CB  LYS B 898      16.915  18.098  -4.387  1.00 38.07           C  
-ANISOU12157  CB  LYS B 898     4462   4146   5858    784   -157   -364       C  
-ATOM  12158  CG  LYS B 898      16.003  17.210  -5.224  1.00 36.96           C  
-ANISOU12158  CG  LYS B 898     4387   4070   5588    842   -248   -315       C  
-ATOM  12159  CD  LYS B 898      15.798  15.874  -4.528  1.00 37.25           C  
-ANISOU12159  CD  LYS B 898     4438   4124   5590    822   -413   -385       C  
-ATOM  12160  CE  LYS B 898      15.065  14.863  -5.400  1.00 37.91           C  
-ANISOU12160  CE  LYS B 898     4597   4282   5526    847   -475   -367       C  
-ATOM  12161  NZ  LYS B 898      13.606  15.143  -5.491  1.00 41.70           N  
-ANISOU12161  NZ  LYS B 898     5105   4835   5905    840   -501   -299       N  
-ATOM  12162  N   GLN B 899      19.518  19.716  -3.825  1.00 39.27           N  
-ANISOU12162  N   GLN B 899     4470   4260   6189    646    139   -536       N  
-ATOM  12163  CA  GLN B 899      20.369  20.483  -2.919  1.00 41.29           C  
-ANISOU12163  CA  GLN B 899     4642   4520   6527    538    250   -626       C  
-ATOM  12164  C   GLN B 899      20.407  21.945  -3.322  1.00 41.60           C  
-ANISOU12164  C   GLN B 899     4759   4489   6559    472    494   -587       C  
-ATOM  12165  O   GLN B 899      20.370  22.827  -2.476  1.00 40.83           O  
-ANISOU12165  O   GLN B 899     4656   4351   6507    376    600   -586       O  
-ATOM  12166  CB  GLN B 899      21.804  19.953  -2.917  1.00 45.56           C  
-ANISOU12166  CB  GLN B 899     5064   5164   7081    525    249   -784       C  
-ATOM  12167  CG  GLN B 899      22.824  21.028  -3.298  1.00 51.90           C  
-ANISOU12167  CG  GLN B 899     5841   5987   7890    422    483   -874       C  
-ATOM  12168  CD  GLN B 899      24.245  20.677  -2.918  1.00 56.70           C  
-ANISOU12168  CD  GLN B 899     6287   6747   8508    383    488  -1060       C  
-ATOM  12169  OE1 GLN B 899      24.579  19.507  -2.714  1.00 60.86           O  
-ANISOU12169  OE1 GLN B 899     6743   7361   9019    481    316  -1109       O  
-ATOM  12170  NE2 GLN B 899      25.095  21.696  -2.817  1.00 57.54           N  
-ANISOU12170  NE2 GLN B 899     6344   6900   8618    242    701  -1174       N  
-ATOM  12171  N   VAL B 900      20.498  22.195  -4.623  1.00 47.62           N  
-ANISOU12171  N   VAL B 900     5611   5227   7256    523    598   -556       N  
-ATOM  12172  CA  VAL B 900      20.643  23.554  -5.122  1.00 47.25           C  
-ANISOU12172  CA  VAL B 900     5680   5096   7176    474    861   -534       C  
-ATOM  12173  C   VAL B 900      19.413  24.372  -4.765  1.00 46.72           C  
-ANISOU12173  C   VAL B 900     5730   4943   7079    507    914   -383       C  
-ATOM  12174  O   VAL B 900      19.527  25.464  -4.210  1.00 47.50           O  
-ANISOU12174  O   VAL B 900     5885   4973   7190    413   1102   -383       O  
-ATOM  12175  CB  VAL B 900      20.868  23.589  -6.641  1.00 48.46           C  
-ANISOU12175  CB  VAL B 900     5930   5227   7257    545    948   -522       C  
-ATOM  12176  CG1 VAL B 900      21.004  25.021  -7.113  1.00 49.60           C  
-ANISOU12176  CG1 VAL B 900     6238   5260   7346    500   1242   -506       C  
-ATOM  12177  CG2 VAL B 900      22.104  22.799  -7.007  1.00 48.20           C  
-ANISOU12177  CG2 VAL B 900     5782   5282   7250    513    897   -672       C  
-ATOM  12178  N   ALA B 901      18.236  23.839  -5.075  1.00 39.54           N  
-ANISOU12178  N   ALA B 901     4857   4051   6114    635    759   -261       N  
-ATOM  12179  CA  ALA B 901      16.999  24.531  -4.753  1.00 38.68           C  
-ANISOU12179  CA  ALA B 901     4844   3897   5955    692    786   -120       C  
-ATOM  12180  C   ALA B 901      16.825  24.684  -3.240  1.00 38.67           C  
-ANISOU12180  C   ALA B 901     4770   3874   6047    586    731   -135       C  
-ATOM  12181  O   ALA B 901      16.448  25.751  -2.759  1.00 38.64           O  
-ANISOU12181  O   ALA B 901     4851   3793   6038    554    877    -65       O  
-ATOM  12182  CB  ALA B 901      15.811  23.813  -5.370  1.00 35.91           C  
-ANISOU12182  CB  ALA B 901     4513   3625   5507    837    618    -21       C  
-ATOM  12183  N   LEU B 902      17.109  23.625  -2.488  1.00 41.14           N  
-ANISOU12183  N   LEU B 902     4942   4249   6439    537    532   -223       N  
-ATOM  12184  CA  LEU B 902      16.973  23.681  -1.036  1.00 41.56           C  
-ANISOU12184  CA  LEU B 902     4921   4282   6587    438    464   -245       C  
-ATOM  12185  C   LEU B 902      17.875  24.742  -0.419  1.00 45.24           C  
-ANISOU12185  C   LEU B 902     5369   4702   7120    291    681   -309       C  
-ATOM  12186  O   LEU B 902      17.418  25.566   0.372  1.00 45.63           O  
-ANISOU12186  O   LEU B 902     5457   4680   7199    222    765   -248       O  
-ATOM  12187  CB  LEU B 902      17.249  22.318  -0.408  1.00 40.44           C  
-ANISOU12187  CB  LEU B 902     4657   4209   6498    432    232   -344       C  
-ATOM  12188  CG  LEU B 902      16.119  21.309  -0.591  1.00 38.46           C  
-ANISOU12188  CG  LEU B 902     4443   3992   6179    524     24   -288       C  
-ATOM  12189  CD1 LEU B 902      16.537  19.945  -0.097  1.00 37.38           C  
-ANISOU12189  CD1 LEU B 902     4236   3900   6065    527   -161   -396       C  
-ATOM  12190  CD2 LEU B 902      14.877  21.785   0.133  1.00 38.52           C  
-ANISOU12190  CD2 LEU B 902     4493   3958   6186    509    -17   -193       C  
-ATOM  12191  N   ILE B 903      19.152  24.720  -0.782  1.00 43.61           N  
-ANISOU12191  N   ILE B 903     5102   4546   6922    231    781   -441       N  
-ATOM  12192  CA  ILE B 903      20.106  25.694  -0.265  1.00 47.98           C  
-ANISOU12192  CA  ILE B 903     5628   5093   7509     62   1012   -539       C  
-ATOM  12193  C   ILE B 903      19.696  27.116  -0.623  1.00 50.93           C  
-ANISOU12193  C   ILE B 903     6200   5337   7814     30   1289   -440       C  
-ATOM  12194  O   ILE B 903      20.096  28.070   0.043  1.00 52.39           O  
-ANISOU12194  O   ILE B 903     6406   5482   8017   -128   1497   -481       O  
-ATOM  12195  CB  ILE B 903      21.539  25.421  -0.768  1.00 49.72           C  
-ANISOU12195  CB  ILE B 903     5752   5424   7715      9   1081   -717       C  
-ATOM  12196  CG1 ILE B 903      22.135  24.224  -0.027  1.00 51.78           C  
-ANISOU12196  CG1 ILE B 903     5811   5826   8037     22    857   -833       C  
-ATOM  12197  CG2 ILE B 903      22.423  26.644  -0.573  1.00 49.43           C  
-ANISOU12197  CG2 ILE B 903     5738   5383   7660   -181   1391   -823       C  
-ATOM  12198  CD1 ILE B 903      23.573  23.938  -0.383  1.00 54.82           C  
-ANISOU12198  CD1 ILE B 903     6073   6360   8395    -19    914  -1020       C  
-ATOM  12199  N   THR B 904      18.888  27.257  -1.669  1.00 68.25           N  
-ANISOU12199  N   THR B 904     8548   7471   9912    186   1304   -311       N  
-ATOM  12200  CA  THR B 904      18.403  28.573  -2.065  1.00 69.02           C  
-ANISOU12200  CA  THR B 904     8872   7440   9913    210   1568   -200       C  
-ATOM  12201  C   THR B 904      17.183  28.978  -1.240  1.00 66.81           C  
-ANISOU12201  C   THR B 904     8647   7102   9637    249   1522    -48       C  
-ATOM  12202  O   THR B 904      16.983  30.155  -0.948  1.00 67.53           O  
-ANISOU12202  O   THR B 904     8893   7083   9682    201   1760     19       O  
-ATOM  12203  CB  THR B 904      18.075  28.640  -3.572  1.00 72.37           C  
-ANISOU12203  CB  THR B 904     9449   7839  10210    385   1625   -125       C  
-ATOM  12204  OG1 THR B 904      18.674  29.810  -4.137  1.00 74.77           O  
-ANISOU12204  OG1 THR B 904     9946   8035  10429    326   1965   -157       O  
-ATOM  12205  CG2 THR B 904      16.574  28.702  -3.797  1.00 72.65           C  
-ANISOU12205  CG2 THR B 904     9582   7864  10159    580   1531     65       C  
-ATOM  12206  N   ILE B 905      16.372  27.996  -0.861  1.00 51.05           N  
-ANISOU12206  N   ILE B 905     6538   5176   7681    331   1228     -2       N  
-ATOM  12207  CA  ILE B 905      15.198  28.257  -0.039  1.00 47.02           C  
-ANISOU12207  CA  ILE B 905     6056   4630   7178    360   1151    122       C  
-ATOM  12208  C   ILE B 905      15.607  28.561   1.393  1.00 46.78           C  
-ANISOU12208  C   ILE B 905     5937   4558   7281    163   1180     64       C  
-ATOM  12209  O   ILE B 905      15.130  29.523   1.992  1.00 46.30           O  
-ANISOU12209  O   ILE B 905     5974   4403   7214    116   1321    155       O  
-ATOM  12210  CB  ILE B 905      14.240  27.065  -0.028  1.00 43.71           C  
-ANISOU12210  CB  ILE B 905     5545   4311   6752    472    835    154       C  
-ATOM  12211  CG1 ILE B 905      13.682  26.819  -1.429  1.00 42.64           C  
-ANISOU12211  CG1 ILE B 905     5492   4242   6466    664    814    223       C  
-ATOM  12212  CG2 ILE B 905      13.114  27.301   0.968  1.00 42.10           C  
-ANISOU12212  CG2 ILE B 905     5348   4081   6566    468    746    248       C  
-ATOM  12213  CD1 ILE B 905      12.628  25.741  -1.477  1.00 38.75           C  
-ANISOU12213  CD1 ILE B 905     4927   3871   5926    756    543    248       C  
-ATOM  12214  N   MET B 906      16.496  27.741   1.941  1.00 51.95           N  
-ANISOU12214  N   MET B 906     6406   5288   8043     57   1054    -87       N  
-ATOM  12215  CA  MET B 906      16.974  27.957   3.298  1.00 52.97           C  
-ANISOU12215  CA  MET B 906     6424   5409   8295   -128   1075   -160       C  
-ATOM  12216  C   MET B 906      17.445  29.395   3.493  1.00 54.36           C  
-ANISOU12216  C   MET B 906     6711   5497   8445   -277   1422   -155       C  
-ATOM  12217  O   MET B 906      17.062  30.052   4.460  1.00 54.14           O  
-ANISOU12217  O   MET B 906     6709   5393   8468   -381   1496    -95       O  
-ATOM  12218  CB  MET B 906      18.088  26.970   3.649  1.00 55.09           C  
-ANISOU12218  CB  MET B 906     6489   5803   8639   -189    942   -340       C  
-ATOM  12219  CG  MET B 906      17.608  25.535   3.781  1.00 56.74           C  
-ANISOU12219  CG  MET B 906     6613   6071   8874    -70    615   -350       C  
-ATOM  12220  SD  MET B 906      18.829  24.411   4.491  1.00 56.62           S  
-ANISOU12220  SD  MET B 906     6385   6194   8934   -112    463   -545       S  
-ATOM  12221  CE  MET B 906      19.060  25.121   6.121  1.00 59.80           C  
-ANISOU12221  CE  MET B 906     6688   6576   9458   -308    538   -583       C  
-ATOM  12222  N   ALA B 907      18.260  29.885   2.566  1.00 51.90           N  
-ANISOU12222  N   ALA B 907     6484   5188   8047   -299   1648   -223       N  
-ATOM  12223  CA  ALA B 907      18.798  31.240   2.659  1.00 53.47           C  
-ANISOU12223  CA  ALA B 907     6825   5302   8190   -463   2021   -248       C  
-ATOM  12224  C   ALA B 907      17.707  32.306   2.626  1.00 54.22           C  
-ANISOU12224  C   ALA B 907     7172   5231   8199   -392   2193    -50       C  
-ATOM  12225  O   ALA B 907      17.790  33.316   3.325  1.00 54.17           O  
-ANISOU12225  O   ALA B 907     7261   5134   8187   -550   2436    -30       O  
-ATOM  12226  CB  ALA B 907      19.814  31.486   1.550  1.00 53.51           C  
-ANISOU12226  CB  ALA B 907     6899   5335   8097   -489   2225   -371       C  
-ATOM  12227  N   GLN B 908      16.688  32.083   1.805  1.00 53.28           N  
-ANISOU12227  N   GLN B 908     7162   5089   7994   -150   2077     95       N  
-ATOM  12228  CA  GLN B 908      15.602  33.047   1.684  1.00 54.12           C  
-ANISOU12228  CA  GLN B 908     7508   5071   7985    -26   2226    289       C  
-ATOM  12229  C   GLN B 908      14.586  32.900   2.813  1.00 52.15           C  
-ANISOU12229  C   GLN B 908     7183   4813   7820    -24   2038    395       C  
-ATOM  12230  O   GLN B 908      13.621  33.659   2.895  1.00 52.66           O  
-ANISOU12230  O   GLN B 908     7422   4793   7794     80   2135    559       O  
-ATOM  12231  CB  GLN B 908      14.927  32.937   0.316  1.00 56.86           C  
-ANISOU12231  CB  GLN B 908     7996   5433   8176    247   2197    393       C  
-ATOM  12232  CG  GLN B 908      15.866  33.223  -0.844  1.00 61.62           C  
-ANISOU12232  CG  GLN B 908     8716   6009   8687    248   2414    301       C  
-ATOM  12233  CD  GLN B 908      15.132  33.585  -2.118  1.00 65.08           C  
-ANISOU12233  CD  GLN B 908     9377   6412   8937    516   2497    436       C  
-ATOM  12234  OE1 GLN B 908      15.491  33.135  -3.206  1.00 66.81           O  
-ANISOU12234  OE1 GLN B 908     9595   6679   9112    603   2464    383       O  
-ATOM  12235  NE2 GLN B 908      14.096  34.403  -1.989  1.00 65.52           N  
-ANISOU12235  NE2 GLN B 908     9628   6393   8874    662   2608    614       N  
-ATOM  12236  N   ILE B 909      14.807  31.917   3.681  1.00 52.41           N  
-ANISOU12236  N   ILE B 909     6967   4934   8014   -129   1773    296       N  
-ATOM  12237  CA  ILE B 909      14.024  31.793   4.903  1.00 49.76           C  
-ANISOU12237  CA  ILE B 909     6551   4573   7781   -181   1610    361       C  
-ATOM  12238  C   ILE B 909      14.715  32.555   6.028  1.00 50.06           C  
-ANISOU12238  C   ILE B 909     6565   4538   7918   -441   1812    307       C  
-ATOM  12239  O   ILE B 909      14.093  32.920   7.023  1.00 50.04           O  
-ANISOU12239  O   ILE B 909     6569   4463   7982   -511   1796    390       O  
-ATOM  12240  CB  ILE B 909      13.839  30.324   5.323  1.00 47.43           C  
-ANISOU12240  CB  ILE B 909     6031   4392   7597   -158   1229    280       C  
-ATOM  12241  CG1 ILE B 909      12.816  29.634   4.426  1.00 46.29           C  
-ANISOU12241  CG1 ILE B 909     5922   4322   7343     74   1028    356       C  
-ATOM  12242  CG2 ILE B 909      13.367  30.231   6.760  1.00 45.56           C  
-ANISOU12242  CG2 ILE B 909     5701   4113   7497   -279   1096    297       C  
-ATOM  12243  CD1 ILE B 909      12.507  28.214   4.851  1.00 44.39           C  
-ANISOU12243  CD1 ILE B 909     5512   4175   7179     85    685    277       C  
-ATOM  12244  N   GLY B 910      16.008  32.802   5.858  1.00 66.74           N  
-ANISOU12244  N   GLY B 910     8645   6685  10030   -594   2010    158       N  
-ATOM  12245  CA  GLY B 910      16.775  33.534   6.846  1.00 65.84           C  
-ANISOU12245  CA  GLY B 910     8493   6542   9982   -866   2235     76       C  
-ATOM  12246  C   GLY B 910      17.701  32.633   7.637  1.00 65.74           C  
-ANISOU12246  C   GLY B 910     8183   6684  10111  -1007   2054   -112       C  
-ATOM  12247  O   GLY B 910      18.358  33.079   8.574  1.00 65.02           O  
-ANISOU12247  O   GLY B 910     8003   6618  10084  -1239   2197   -201       O  
-ATOM  12248  N   SER B 911      17.759  31.361   7.253  1.00 48.25           N  
-ANISOU12248  N   SER B 911     5822   4582   7927   -861   1751   -174       N  
-ATOM  12249  CA  SER B 911      18.579  30.381   7.960  1.00 49.10           C  
-ANISOU12249  CA  SER B 911     5667   4845   8145   -933   1555   -343       C  
-ATOM  12250  C   SER B 911      19.980  30.255   7.374  1.00 52.31           C  
-ANISOU12250  C   SER B 911     5980   5404   8493   -995   1679   -535       C  
-ATOM  12251  O   SER B 911      20.202  30.556   6.205  1.00 52.65           O  
-ANISOU12251  O   SER B 911     6154   5431   8421   -931   1825   -537       O  
-ATOM  12252  CB  SER B 911      17.901  29.009   7.937  1.00 48.00           C  
-ANISOU12252  CB  SER B 911     5444   4740   8052   -743   1172   -316       C  
-ATOM  12253  OG  SER B 911      18.738  28.023   8.520  1.00 49.24           O  
-ANISOU12253  OG  SER B 911     5385   5041   8283   -771    999   -478       O  
-ATOM  12254  N   TYR B 912      20.923  29.810   8.197  1.00 40.38           N  
-ANISOU12254  N   TYR B 912     4239   4054   7051  -1114   1621   -703       N  
-ATOM  12255  CA  TYR B 912      22.238  29.432   7.706  1.00 44.54           C  
-ANISOU12255  CA  TYR B 912     4628   4778   7516  -1138   1668   -905       C  
-ATOM  12256  C   TYR B 912      22.071  28.236   6.777  1.00 41.17           C  
-ANISOU12256  C   TYR B 912     4195   4386   7061   -892   1408   -891       C  
-ATOM  12257  O   TYR B 912      21.033  27.573   6.792  1.00 38.82           O  
-ANISOU12257  O   TYR B 912     3950   3997   6804   -735   1170   -761       O  
-ATOM  12258  CB  TYR B 912      23.180  29.081   8.860  1.00 51.87           C  
-ANISOU12258  CB  TYR B 912     5289   5910   8508  -1270   1618  -1082       C  
-ATOM  12259  CG  TYR B 912      23.788  30.278   9.565  1.00 61.83           C  
-ANISOU12259  CG  TYR B 912     6520   7219   9755  -1563   1946  -1169       C  
-ATOM  12260  CD1 TYR B 912      24.943  30.145  10.331  1.00 65.57           C  
-ANISOU12260  CD1 TYR B 912     6737   7950  10227  -1711   1989  -1383       C  
-ATOM  12261  CD2 TYR B 912      23.209  31.537   9.471  1.00 65.05           C  
-ANISOU12261  CD2 TYR B 912     7161   7427  10129  -1689   2227  -1043       C  
-ATOM  12262  CE1 TYR B 912      25.506  31.233  10.976  1.00 68.41           C  
-ANISOU12262  CE1 TYR B 912     7059   8377  10555  -2007   2308  -1480       C  
-ATOM  12263  CE2 TYR B 912      23.765  32.633  10.117  1.00 67.85           C  
-ANISOU12263  CE2 TYR B 912     7512   7816  10452  -1980   2558  -1128       C  
-ATOM  12264  CZ  TYR B 912      24.912  32.473  10.868  1.00 69.74           C  
-ANISOU12264  CZ  TYR B 912     7481   8322  10694  -2154   2599  -1351       C  
-ATOM  12265  OH  TYR B 912      25.469  33.552  11.512  1.00 69.35           O  
-ANISOU12265  OH  TYR B 912     7420   8331  10598  -2470   2945  -1451       O  
-ATOM  12266  N   VAL B 913      23.089  27.964   5.967  1.00 59.10           N  
-ANISOU12266  N   VAL B 913     6406   6796   9253   -872   1464  -1035       N  
-ATOM  12267  CA  VAL B 913      23.011  26.896   4.973  1.00 56.31           C  
-ANISOU12267  CA  VAL B 913     6064   6471   8861   -656   1258  -1022       C  
-ATOM  12268  C   VAL B 913      24.140  25.881   5.142  1.00 55.55           C  
-ANISOU12268  C   VAL B 913     5748   6603   8757   -612   1118  -1209       C  
-ATOM  12269  O   VAL B 913      25.244  26.239   5.557  1.00 53.63           O  
-ANISOU12269  O   VAL B 913     5355   6534   8489   -758   1264  -1384       O  
-ATOM  12270  CB  VAL B 913      23.045  27.470   3.545  1.00 56.80           C  
-ANISOU12270  CB  VAL B 913     6310   6456   8817   -621   1448   -988       C  
-ATOM  12271  CG1 VAL B 913      21.911  28.465   3.350  1.00 56.04           C  
-ANISOU12271  CG1 VAL B 913     6450   6147   8695   -617   1592   -796       C  
-ATOM  12272  CG2 VAL B 913      24.384  28.132   3.274  1.00 56.74           C  
-ANISOU12272  CG2 VAL B 913     6250   6573   8735   -797   1722  -1184       C  
-ATOM  12273  N   PRO B 914      23.862  24.606   4.819  1.00 42.40           N  
-ANISOU12273  N   PRO B 914     4067   4952   7090   -407    847  -1177       N  
-ATOM  12274  CA  PRO B 914      24.827  23.510   4.943  1.00 45.21           C  
-ANISOU12274  CA  PRO B 914     4249   5510   7417   -308    695  -1329       C  
-ATOM  12275  C   PRO B 914      25.878  23.584   3.843  1.00 48.80           C  
-ANISOU12275  C   PRO B 914     4675   6091   7774   -309    826  -1454       C  
-ATOM  12276  O   PRO B 914      25.930  22.719   2.964  1.00 49.44           O  
-ANISOU12276  O   PRO B 914     4794   6182   7809   -148    700  -1441       O  
-ATOM  12277  CB  PRO B 914      23.959  22.270   4.747  1.00 41.33           C  
-ANISOU12277  CB  PRO B 914     3842   4928   6932   -100    416  -1219       C  
-ATOM  12278  CG  PRO B 914      22.882  22.731   3.839  1.00 40.70           C  
-ANISOU12278  CG  PRO B 914     3964   4663   6839    -78    467  -1051       C  
-ATOM  12279  CD  PRO B 914      22.576  24.138   4.275  1.00 41.24           C  
-ANISOU12279  CD  PRO B 914     4084   4638   6946   -253    687   -997       C  
-ATOM  12280  N   ALA B 915      26.707  24.621   3.899  1.00 58.51           N  
-ANISOU12280  N   ALA B 915     5846   7418   8968   -507   1092  -1583       N  
-ATOM  12281  CA  ALA B 915      27.730  24.852   2.888  1.00 63.79           C  
-ANISOU12281  CA  ALA B 915     6496   8205   9537   -551   1254  -1729       C  
-ATOM  12282  C   ALA B 915      28.956  25.496   3.527  1.00 68.21           C  
-ANISOU12282  C   ALA B 915     6865   9010  10043   -763   1460  -1962       C  
-ATOM  12283  O   ALA B 915      28.874  26.051   4.623  1.00 69.06           O  
-ANISOU12283  O   ALA B 915     6904   9143  10193   -909   1539  -1977       O  
-ATOM  12284  CB  ALA B 915      27.179  25.734   1.785  1.00 62.58           C  
-ANISOU12284  CB  ALA B 915     6589   7838   9352   -595   1449  -1619       C  
-ATOM  12285  N   GLU B 916      30.096  25.418   2.849  1.00 64.12           N  
-ANISOU12285  N   GLU B 916     6253   8688   9422   -792   1551  -2152       N  
-ATOM  12286  CA  GLU B 916      31.315  26.034   3.363  1.00 69.94           C  
-ANISOU12286  CA  GLU B 916     6795   9707  10073  -1011   1767  -2409       C  
-ATOM  12287  C   GLU B 916      31.186  27.549   3.290  1.00 74.95           C  
-ANISOU12287  C   GLU B 916     7593  10208  10677  -1292   2131  -2421       C  
-ATOM  12288  O   GLU B 916      31.583  28.270   4.206  1.00 75.47           O  
-ANISOU12288  O   GLU B 916     7555  10402  10720  -1516   2316  -2538       O  
-ATOM  12289  CB  GLU B 916      32.534  25.557   2.578  1.00 71.80           C  
-ANISOU12289  CB  GLU B 916     6897  10196  10189   -968   1772  -2621       C  
-ATOM  12290  CG  GLU B 916      33.853  25.847   3.259  1.00 73.72           C  
-ANISOU12290  CG  GLU B 916     6863  10830  10319  -1141   1916  -2916       C  
-ATOM  12291  CD  GLU B 916      34.914  24.811   2.942  1.00 73.17           C  
-ANISOU12291  CD  GLU B 916     6578  11076  10147   -967   1756  -3091       C  
-ATOM  12292  OE1 GLU B 916      34.832  24.179   1.866  1.00 71.87           O  
-ANISOU12292  OE1 GLU B 916     6521  10806   9979   -796   1639  -3022       O  
-ATOM  12293  OE2 GLU B 916      35.826  24.621   3.775  1.00 73.37           O  
-ANISOU12293  OE2 GLU B 916     6325  11468  10086   -993   1749  -3295       O  
-ATOM  12294  N   GLU B 917      30.618  28.019   2.186  1.00 67.04           N  
-ANISOU12294  N   GLU B 917     6861   8948   9662  -1273   2244  -2298       N  
-ATOM  12295  CA  GLU B 917      30.240  29.417   2.034  1.00 73.79           C  
-ANISOU12295  CA  GLU B 917     7957   9600  10479  -1479   2584  -2251       C  
-ATOM  12296  C   GLU B 917      29.217  29.498   0.911  1.00 71.19           C  
-ANISOU12296  C   GLU B 917     7922   8962  10164  -1311   2559  -2026       C  
-ATOM  12297  O   GLU B 917      29.058  28.544   0.153  1.00 70.85           O  
-ANISOU12297  O   GLU B 917     7869   8908  10143  -1094   2325  -1964       O  
-ATOM  12298  CB  GLU B 917      31.460  30.291   1.738  1.00 86.40           C  
-ANISOU12298  CB  GLU B 917     9535  11366  11926  -1756   2939  -2527       C  
-ATOM  12299  CG  GLU B 917      31.744  30.520   0.269  1.00102.36           C  
-ANISOU12299  CG  GLU B 917    11749  13286  13856  -1740   3080  -2574       C  
-ATOM  12300  CD  GLU B 917      32.945  31.413   0.058  1.00114.20           C  
-ANISOU12300  CD  GLU B 917    13242  14955  15193  -2047   3452  -2876       C  
-ATOM  12301  OE1 GLU B 917      32.985  32.134  -0.960  1.00120.64           O  
-ANISOU12301  OE1 GLU B 917    14326  15594  15918  -2126   3707  -2900       O  
-ATOM  12302  OE2 GLU B 917      33.850  31.391   0.917  1.00120.38           O  
-ANISOU12302  OE2 GLU B 917    13754  16059  15925  -2213   3499  -3100       O  
-ATOM  12303  N   ALA B 918      28.509  30.617   0.806  1.00 73.10           N  
-ANISOU12303  N   ALA B 918     8430   8965  10379  -1400   2804  -1900       N  
-ATOM  12304  CA  ALA B 918      27.445  30.714  -0.186  1.00 71.44           C  
-ANISOU12304  CA  ALA B 918     8490   8488  10165  -1210   2774  -1675       C  
-ATOM  12305  C   ALA B 918      26.921  32.127  -0.404  1.00 70.11           C  
-ANISOU12305  C   ALA B 918     8645   8083   9910  -1316   3129  -1581       C  
-ATOM  12306  O   ALA B 918      26.788  32.907   0.535  1.00 68.67           O  
-ANISOU12306  O   ALA B 918     8497   7867   9728  -1486   3306  -1573       O  
-ATOM  12307  CB  ALA B 918      26.304  29.790   0.188  1.00 68.43           C  
-ANISOU12307  CB  ALA B 918     8059   8040   9903   -976   2416  -1457       C  
-ATOM  12308  N   THR B 919      26.613  32.438  -1.658  1.00 95.59           N  
-ANISOU12308  N   THR B 919    12123  11142  13054  -1205   3237  -1505       N  
-ATOM  12309  CA  THR B 919      25.993  33.705  -2.018  1.00 93.67           C  
-ANISOU12309  CA  THR B 919    12240  10649  12702  -1230   3563  -1384       C  
-ATOM  12310  C   THR B 919      24.685  33.443  -2.744  1.00 89.99           C  
-ANISOU12310  C   THR B 919    11942  10009  12242   -923   3390  -1116       C  
-ATOM  12311  O   THR B 919      24.660  32.776  -3.777  1.00 89.66           O  
-ANISOU12311  O   THR B 919    11896   9976  12195   -755   3236  -1098       O  
-ATOM  12312  CB  THR B 919      26.896  34.546  -2.936  1.00 98.59           C  
-ANISOU12312  CB  THR B 919    13070  11223  13165  -1391   3939  -1567       C  
-ATOM  12313  OG1 THR B 919      28.117  34.855  -2.255  1.00 97.46           O  
-ANISOU12313  OG1 THR B 919    12765  11280  12986  -1704   4131  -1844       O  
-ATOM  12314  CG2 THR B 919      26.195  35.839  -3.330  1.00101.55           C  
-ANISOU12314  CG2 THR B 919    13869  11315  13402  -1377   4290  -1426       C  
-ATOM  12315  N   ILE B 920      23.597  33.968  -2.195  1.00 68.79           N  
-ANISOU12315  N   ILE B 920     9395   7184   9559   -854   3417   -914       N  
-ATOM  12316  CA  ILE B 920      22.284  33.806  -2.797  1.00 63.38           C  
-ANISOU12316  CA  ILE B 920     8859   6372   8849   -563   3269   -666       C  
-ATOM  12317  C   ILE B 920      21.750  35.126  -3.328  1.00 63.38           C  
-ANISOU12317  C   ILE B 920     9253   6150   8680   -510   3625   -545       C  
-ATOM  12318  O   ILE B 920      21.842  36.159  -2.670  1.00 63.48           O  
-ANISOU12318  O   ILE B 920     9418   6068   8634   -678   3921   -554       O  
-ATOM  12319  CB  ILE B 920      21.272  33.220  -1.790  1.00 59.10           C  
-ANISOU12319  CB  ILE B 920     8161   5868   8428   -467   2966   -512       C  
-ATOM  12320  CG1 ILE B 920      21.721  31.829  -1.347  1.00 56.00           C  
-ANISOU12320  CG1 ILE B 920     7425   5674   8179   -473   2611   -619       C  
-ATOM  12321  CG2 ILE B 920      19.875  33.165  -2.398  1.00 58.02           C  
-ANISOU12321  CG2 ILE B 920     8179   5636   8229   -181   2845   -274       C  
-ATOM  12322  CD1 ILE B 920      21.905  30.861  -2.492  1.00 52.82           C  
-ANISOU12322  CD1 ILE B 920     6965   5341   7765   -313   2423   -646       C  
-ATOM  12323  N   GLY B 921      21.201  35.085  -4.534  1.00 68.61           N  
-ANISOU12323  N   GLY B 921    10090   6732   9248   -269   3608   -432       N  
-ATOM  12324  CA  GLY B 921      20.524  36.233  -5.096  1.00 67.83           C  
-ANISOU12324  CA  GLY B 921    10380   6427   8965   -136   3909   -284       C  
-ATOM  12325  C   GLY B 921      19.037  35.968  -5.075  1.00 65.29           C  
-ANISOU12325  C   GLY B 921    10074   6102   8633    158   3679    -29       C  
-ATOM  12326  O   GLY B 921      18.570  35.016  -5.698  1.00 64.81           O  
-ANISOU12326  O   GLY B 921     9876   6143   8606    353   3381     31       O  
-ATOM  12327  N   ILE B 922      18.294  36.803  -4.359  1.00 62.78           N  
-ANISOU12327  N   ILE B 922     9919   5680   8255    181   3824    114       N  
-ATOM  12328  CA  ILE B 922      16.862  36.590  -4.181  1.00 61.52           C  
-ANISOU12328  CA  ILE B 922     9749   5549   8075    442   3604    341       C  
-ATOM  12329  C   ILE B 922      16.149  36.156  -5.466  1.00 60.11           C  
-ANISOU12329  C   ILE B 922     9630   5421   7789    761   3461    450       C  
-ATOM  12330  O   ILE B 922      16.054  36.908  -6.438  1.00 61.64           O  
-ANISOU12330  O   ILE B 922    10127   5498   7797    914   3716    506       O  
-ATOM  12331  CB  ILE B 922      16.179  37.819  -3.548  1.00 62.90           C  
-ANISOU12331  CB  ILE B 922    10198   5568   8132    467   3876    494       C  
-ATOM  12332  CG1 ILE B 922      16.696  38.018  -2.119  1.00 62.95           C  
-ANISOU12332  CG1 ILE B 922    10068   5568   8281    149   3930    404       C  
-ATOM  12333  CG2 ILE B 922      14.666  37.650  -3.558  1.00 62.15           C  
-ANISOU12333  CG2 ILE B 922    10114   5528   7974    777   3663    723       C  
-ATOM  12334  CD1 ILE B 922      16.420  39.387  -1.538  1.00 65.25           C  
-ANISOU12334  CD1 ILE B 922    10673   5671   8447     82   4310    504       C  
-ATOM  12335  N   VAL B 923      15.667  34.917  -5.441  1.00 55.31           N  
-ANISOU12335  N   VAL B 923     8735   4992   7290    852   3061    470       N  
-ATOM  12336  CA  VAL B 923      14.978  34.288  -6.558  1.00 54.65           C  
-ANISOU12336  CA  VAL B 923     8632   5010   7121   1119   2875    554       C  
-ATOM  12337  C   VAL B 923      13.470  34.417  -6.366  1.00 55.04           C  
-ANISOU12337  C   VAL B 923     8723   5127   7063   1367   2758    758       C  
-ATOM  12338  O   VAL B 923      12.939  34.028  -5.328  1.00 55.86           O  
-ANISOU12338  O   VAL B 923     8654   5305   7266   1309   2557    788       O  
-ATOM  12339  CB  VAL B 923      15.343  32.790  -6.625  1.00 51.90           C  
-ANISOU12339  CB  VAL B 923     7953   4832   6934   1049   2521    440       C  
-ATOM  12340  CG1 VAL B 923      14.320  32.020  -7.432  1.00 49.89           C  
-ANISOU12340  CG1 VAL B 923     7631   4725   6600   1302   2278    548       C  
-ATOM  12341  CG2 VAL B 923      16.746  32.608  -7.183  1.00 49.21           C  
-ANISOU12341  CG2 VAL B 923     7586   4460   6652    884   2624    251       C  
-ATOM  12342  N   ASP B 924      12.781  34.956  -7.365  1.00 56.46           N  
-ANISOU12342  N   ASP B 924     9128   5296   7029   1650   2884    888       N  
-ATOM  12343  CA  ASP B 924      11.354  35.244  -7.240  1.00 57.42           C  
-ANISOU12343  CA  ASP B 924     9313   5506   6999   1915   2818   1079       C  
-ATOM  12344  C   ASP B 924      10.501  33.996  -7.031  1.00 54.30           C  
-ANISOU12344  C   ASP B 924     8603   5361   6668   1974   2404   1092       C  
-ATOM  12345  O   ASP B 924       9.429  34.067  -6.429  1.00 54.35           O  
-ANISOU12345  O   ASP B 924     8570   5462   6617   2081   2292   1199       O  
-ATOM  12346  CB  ASP B 924      10.847  36.002  -8.468  1.00 61.94           C  
-ANISOU12346  CB  ASP B 924    10182   6051   7302   2240   3032   1204       C  
-ATOM  12347  CG  ASP B 924      10.624  35.093  -9.656  1.00 65.36           C  
-ANISOU12347  CG  ASP B 924    10480   6664   7688   2403   2827   1188       C  
-ATOM  12348  OD1 ASP B 924      11.465  34.201  -9.880  1.00 68.14           O  
-ANISOU12348  OD1 ASP B 924    10640   7042   8207   2214   2685   1040       O  
-ATOM  12349  OD2 ASP B 924       9.606  35.263 -10.360  1.00 66.06           O  
-ANISOU12349  OD2 ASP B 924    10652   6884   7563   2723   2811   1323       O  
-ATOM  12350  N   GLY B 925      10.967  32.861  -7.540  1.00 44.04           N  
-ANISOU12350  N   GLY B 925     7095   4168   5471   1900   2193    976       N  
-ATOM  12351  CA  GLY B 925      10.208  31.628  -7.454  1.00 41.62           C  
-ANISOU12351  CA  GLY B 925     6524   4091   5198   1939   1835    968       C  
-ATOM  12352  C   GLY B 925      11.052  30.414  -7.789  1.00 39.58           C  
-ANISOU12352  C   GLY B 925     6063   3886   5088   1782   1653    815       C  
-ATOM  12353  O   GLY B 925      12.168  30.538  -8.290  1.00 39.88           O  
-ANISOU12353  O   GLY B 925     6160   3810   5183   1685   1796    725       O  
-ATOM  12354  N   ILE B 926      10.529  29.230  -7.493  1.00 50.98           N  
-ANISOU12354  N   ILE B 926     7282   5504   6584   1751   1349    779       N  
-ATOM  12355  CA  ILE B 926      11.202  27.996  -7.872  1.00 47.88           C  
-ANISOU12355  CA  ILE B 926     6721   5175   6298   1637   1175    652       C  
-ATOM  12356  C   ILE B 926      10.236  27.027  -8.532  1.00 49.35           C  
-ANISOU12356  C   ILE B 926     6795   5590   6367   1765    960    678       C  
-ATOM  12357  O   ILE B 926       9.153  26.750  -8.004  1.00 47.58           O  
-ANISOU12357  O   ILE B 926     6495   5507   6077   1811    809    718       O  
-ATOM  12358  CB  ILE B 926      11.846  27.305  -6.680  1.00 43.16           C  
-ANISOU12358  CB  ILE B 926     5957   4537   5904   1399   1031    530       C  
-ATOM  12359  CG1 ILE B 926      13.017  28.130  -6.163  1.00 41.44           C  
-ANISOU12359  CG1 ILE B 926     5813   4134   5798   1239   1251    463       C  
-ATOM  12360  CG2 ILE B 926      12.349  25.941  -7.084  1.00 42.62           C  
-ANISOU12360  CG2 ILE B 926     5735   4555   5902   1330    839    418       C  
-ATOM  12361  CD1 ILE B 926      13.863  27.386  -5.175  1.00 39.21           C  
-ANISOU12361  CD1 ILE B 926     5352   3844   5702   1024   1119    322       C  
-ATOM  12362  N   PHE B 927      10.648  26.509  -9.685  1.00 41.06           N  
-ANISOU12362  N   PHE B 927     5734   4584   5284   1805    956    642       N  
-ATOM  12363  CA  PHE B 927       9.806  25.636 -10.487  1.00 47.02           C  
-ANISOU12363  CA  PHE B 927     6395   5565   5904   1915    794    661       C  
-ATOM  12364  C   PHE B 927      10.562  24.364 -10.835  1.00 46.07           C  
-ANISOU12364  C   PHE B 927     6150   5464   5891   1771    658    542       C  
-ATOM  12365  O   PHE B 927      11.672  24.420 -11.359  1.00 47.03           O  
-ANISOU12365  O   PHE B 927     6314   5457   6099   1713    760    488       O  
-ATOM  12366  CB  PHE B 927       9.374  26.357 -11.768  1.00 55.11           C  
-ANISOU12366  CB  PHE B 927     7560   6648   6731   2160    953    768       C  
-ATOM  12367  CG  PHE B 927       8.801  27.727 -11.530  1.00 63.67           C  
-ANISOU12367  CG  PHE B 927     8826   7677   7690   2336   1142    893       C  
-ATOM  12368  CD1 PHE B 927       9.622  28.783 -11.171  1.00 67.52           C  
-ANISOU12368  CD1 PHE B 927     9493   7908   8252   2279   1380    899       C  
-ATOM  12369  CD2 PHE B 927       7.445  27.961 -11.675  1.00 65.17           C  
-ANISOU12369  CD2 PHE B 927     9014   8085   7662   2557   1097    998       C  
-ATOM  12370  CE1 PHE B 927       9.101  30.041 -10.951  1.00 69.62           C  
-ANISOU12370  CE1 PHE B 927     9963   8105   8385   2440   1581   1021       C  
-ATOM  12371  CE2 PHE B 927       6.917  29.223 -11.457  1.00 66.78           C  
-ANISOU12371  CE2 PHE B 927     9405   8238   7730   2746   1280   1125       C  
-ATOM  12372  CZ  PHE B 927       7.749  30.262 -11.096  1.00 68.79           C  
-ANISOU12372  CZ  PHE B 927     9867   8204   8067   2688   1529   1143       C  
-ATOM  12373  N   THR B 928       9.967  23.217 -10.532  1.00 53.90           N  
-ANISOU12373  N   THR B 928     7001   6615   6863   1708    440    493       N  
-ATOM  12374  CA  THR B 928      10.600  21.942 -10.833  1.00 51.59           C  
-ANISOU12374  CA  THR B 928     6617   6341   6642   1583    320    389       C  
-ATOM  12375  C   THR B 928       9.682  21.064 -11.660  1.00 53.94           C  
-ANISOU12375  C   THR B 928     6852   6874   6769   1642    210    396       C  
-ATOM  12376  O   THR B 928       8.461  21.212 -11.622  1.00 51.92           O  
-ANISOU12376  O   THR B 928     6572   6803   6351   1737    165    447       O  
-ATOM  12377  CB  THR B 928      10.961  21.166  -9.556  1.00 48.90           C  
-ANISOU12377  CB  THR B 928     6191   5942   6445   1404    175    286       C  
-ATOM  12378  OG1 THR B 928       9.765  20.873  -8.825  1.00 43.23           O  
-ANISOU12378  OG1 THR B 928     5425   5356   5644   1398     41    294       O  
-ATOM  12379  CG2 THR B 928      11.916  21.971  -8.687  1.00 46.53           C  
-ANISOU12379  CG2 THR B 928     5924   5444   6310   1323    282    260       C  
-ATOM  12380  N   ARG B 929      10.282  20.140 -12.398  1.00 54.98           N  
-ANISOU12380  N   ARG B 929     6951   7013   6925   1577    173    338       N  
-ATOM  12381  CA  ARG B 929       9.527  19.126 -13.112  1.00 59.79           C  
-ANISOU12381  CA  ARG B 929     7496   7843   7380   1578     74    320       C  
-ATOM  12382  C   ARG B 929      10.359  17.853 -13.183  1.00 64.07           C  
-ANISOU12382  C   ARG B 929     8008   8324   8012   1423     -5    220       C  
-ATOM  12383  O   ARG B 929      11.120  17.662 -14.124  1.00 65.11           O  
-ANISOU12383  O   ARG B 929     8161   8399   8179   1428     57    220       O  
-ATOM  12384  CB  ARG B 929       9.165  19.622 -14.511  1.00 59.79           C  
-ANISOU12384  CB  ARG B 929     7529   7958   7231   1748    183    408       C  
-ATOM  12385  CG  ARG B 929       8.031  18.863 -15.185  1.00 58.78           C  
-ANISOU12385  CG  ARG B 929     7316   8135   6882   1777    102    404       C  
-ATOM  12386  CD  ARG B 929       8.466  17.481 -15.644  1.00 60.29           C  
-ANISOU12386  CD  ARG B 929     7463   8350   7093   1617     30    318       C  
-ATOM  12387  NE  ARG B 929       8.074  16.438 -14.700  1.00 60.42           N  
-ANISOU12387  NE  ARG B 929     7434   8430   7092   1450   -108    216       N  
-ATOM  12388  CZ  ARG B 929       8.733  15.296 -14.530  1.00 59.97           C  
-ANISOU12388  CZ  ARG B 929     7392   8284   7111   1290   -165    129       C  
-ATOM  12389  NH1 ARG B 929       9.831  15.047 -15.231  1.00 60.71           N  
-ANISOU12389  NH1 ARG B 929     7520   8235   7312   1273   -110    132       N  
-ATOM  12390  NH2 ARG B 929       8.301  14.404 -13.650  1.00 59.33           N  
-ANISOU12390  NH2 ARG B 929     7306   8251   6987   1153   -269     33       N  
-ATOM  12391  N   MET B 930      10.224  16.991 -12.177  1.00 75.28           N  
-ANISOU12391  N   MET B 930     9395   9747   9461   1293   -133    136       N  
-ATOM  12392  CA  MET B 930      10.959  15.731 -12.154  1.00 80.36           C  
-ANISOU12392  CA  MET B 930    10041  10332  10159   1170   -200     44       C  
-ATOM  12393  C   MET B 930      10.339  14.712 -11.216  1.00 84.82           C  
-ANISOU12393  C   MET B 930    10604  10961  10661   1053   -331    -44       C  
-ATOM  12394  O   MET B 930       9.514  15.058 -10.372  1.00 84.48           O  
-ANISOU12394  O   MET B 930    10544  10972  10584   1047   -382    -47       O  
-ATOM  12395  CB  MET B 930      12.413  15.962 -11.747  1.00 76.57           C  
-ANISOU12395  CB  MET B 930     9578   9634   9883   1140   -159      7       C  
-ATOM  12396  CG  MET B 930      12.656  16.100 -10.255  1.00 72.55           C  
-ANISOU12396  CG  MET B 930     9055   9022   9490   1078   -218    -47       C  
-ATOM  12397  SD  MET B 930      12.402  17.773  -9.623  1.00 68.60           S  
-ANISOU12397  SD  MET B 930     8558   8454   9053   1141   -120     30       S  
-ATOM  12398  CE  MET B 930      13.686  17.883  -8.378  1.00 66.15           C  
-ANISOU12398  CE  MET B 930     8218   7969   8946   1043   -121    -60       C  
-ATOM  12399  N   GLY B 931      10.738  13.453 -11.379  1.00104.95           N  
-ANISOU12399  N   GLY B 931    13192  13497  13187    961   -372   -119       N  
-ATOM  12400  CA  GLY B 931      10.385  12.407 -10.436  1.00108.69           C  
-ANISOU12400  CA  GLY B 931    13716  13976  13607    843   -470   -221       C  
-ATOM  12401  C   GLY B 931       8.994  11.825 -10.598  1.00110.37           C  
-ANISOU12401  C   GLY B 931    13932  14412  13591    770   -506   -265       C  
-ATOM  12402  O   GLY B 931       8.119  12.033  -9.754  1.00107.78           O  
-ANISOU12402  O   GLY B 931    13588  14152  13212    737   -568   -298       O  
-ATOM  12403  N   ALA B 932       8.795  11.081 -11.681  1.00117.86           N  
-ANISOU12403  N   ALA B 932    14898  15489  14393    731   -462   -275       N  
-ATOM  12404  CA  ALA B 932       7.528  10.406 -11.922  1.00121.43           C  
-ANISOU12404  CA  ALA B 932    15350  16191  14595    629   -474   -345       C  
-ATOM  12405  C   ALA B 932       7.672   8.910 -11.670  1.00122.80           C  
-ANISOU12405  C   ALA B 932    15663  16318  14676    464   -478   -465       C  
-ATOM  12406  O   ALA B 932       6.996   8.100 -12.299  1.00126.90           O  
-ANISOU12406  O   ALA B 932    16213  17023  14979    352   -434   -527       O  
-ATOM  12407  CB  ALA B 932       7.050  10.668 -13.339  1.00125.94           C  
-ANISOU12407  CB  ALA B 932    15840  16985  15027    691   -400   -278       C  
-ATOM  12408  N   SER B 941       2.542  12.033 -14.137  1.00 60.45           N  
-ANISOU12408  N   SER B 941     7180   9810   5979    841   -425   -310       N  
-ATOM  12409  CA  SER B 941       2.647  10.637 -14.538  1.00 61.89           C  
-ANISOU12409  CA  SER B 941     7425  10037   6054    625   -392   -425       C  
-ATOM  12410  C   SER B 941       2.635  10.520 -16.055  1.00 62.64           C  
-ANISOU12410  C   SER B 941     7453  10320   6026    674   -299   -370       C  
-ATOM  12411  O   SER B 941       3.605  10.059 -16.660  1.00 62.20           O  
-ANISOU12411  O   SER B 941     7471  10077   6087    639   -245   -331       O  
-ATOM  12412  CB  SER B 941       1.512   9.823 -13.936  1.00 59.85           C  
-ANISOU12412  CB  SER B 941     7165  10022   5553    423   -429   -607       C  
-ATOM  12413  N   THR B 942       1.534  10.952 -16.663  1.00 82.64           N  
-ANISOU12413  N   THR B 942     9843  13238   8319    766   -282   -368       N  
-ATOM  12414  CA  THR B 942       1.359  10.849 -18.107  1.00 84.21           C  
-ANISOU12414  CA  THR B 942     9958  13675   8364    817   -194   -326       C  
-ATOM  12415  C   THR B 942       2.110  11.942 -18.870  1.00 82.49           C  
-ANISOU12415  C   THR B 942     9736  13290   8317   1077   -146   -141       C  
-ATOM  12416  O   THR B 942       2.288  13.053 -18.366  1.00 82.42           O  
-ANISOU12416  O   THR B 942     9744  13132   8439   1265   -168    -47       O  
-ATOM  12417  CB  THR B 942      -0.134  10.896 -18.497  1.00 87.61           C  
-ANISOU12417  CB  THR B 942    10218  14634   8435    833   -188   -408       C  
-ATOM  12418  OG1 THR B 942      -0.266  10.713 -19.911  1.00 92.54           O  
-ANISOU12418  OG1 THR B 942    10755  15500   8907    869    -97   -374       O  
-ATOM  12419  CG2 THR B 942      -0.749  12.228 -18.110  1.00 87.77           C  
-ANISOU12419  CG2 THR B 942    10151  14771   8425   1102   -238   -323       C  
-ATOM  12420  N   PHE B 943       2.546  11.612 -20.085  1.00 62.36           N  
-ANISOU12420  N   PHE B 943     7181  10759   5755   1072    -66    -97       N  
-ATOM  12421  CA  PHE B 943       3.242  12.554 -20.963  1.00 62.07           C  
-ANISOU12421  CA  PHE B 943     7157  10574   5852   1298     -1     59       C  
-ATOM  12422  C   PHE B 943       2.561  13.914 -20.982  1.00 63.80           C  
-ANISOU12422  C   PHE B 943     7314  10948   5978   1588      7    153       C  
-ATOM  12423  O   PHE B 943       3.203  14.953 -20.817  1.00 64.57           O  
-ANISOU12423  O   PHE B 943     7496  10780   6257   1765     38    263       O  
-ATOM  12424  CB  PHE B 943       3.280  12.008 -22.391  1.00 59.78           C  
-ANISOU12424  CB  PHE B 943     6818  10446   5450   1259     82     73       C  
-ATOM  12425  CG  PHE B 943       4.086  12.845 -23.341  1.00 56.79           C  
-ANISOU12425  CG  PHE B 943     6480   9878   5218   1460    155    216       C  
-ATOM  12426  CD1 PHE B 943       5.122  13.635 -22.876  1.00 54.69           C  
-ANISOU12426  CD1 PHE B 943     6332   9222   5225   1561    159    291       C  
-ATOM  12427  CD2 PHE B 943       3.810  12.841 -24.700  1.00 56.05           C  
-ANISOU12427  CD2 PHE B 943     6311  10007   4980   1534    232    261       C  
-ATOM  12428  CE1 PHE B 943       5.870  14.407 -23.749  1.00 52.04           C  
-ANISOU12428  CE1 PHE B 943     6058   8706   5010   1723    246    399       C  
-ATOM  12429  CE2 PHE B 943       4.553  13.613 -25.576  1.00 52.48           C  
-ANISOU12429  CE2 PHE B 943     5920   9361   4660   1715    307    382       C  
-ATOM  12430  CZ  PHE B 943       5.583  14.396 -25.099  1.00 51.61           C  
-ANISOU12430  CZ  PHE B 943     5946   8849   4816   1804    318    446       C  
-ATOM  12431  N   MET B 944       1.253  13.896 -21.204  1.00 66.28           N  
-ANISOU12431  N   MET B 944     7489  11710   5986   1636     -5    101       N  
-ATOM  12432  CA  MET B 944       0.478  15.121 -21.244  1.00 69.13           C  
-ANISOU12432  CA  MET B 944     7789  12275   6202   1937      7    186       C  
-ATOM  12433  C   MET B 944       0.732  15.951 -19.995  1.00 68.72           C  
-ANISOU12433  C   MET B 944     7834  11944   6333   2016    -38    234       C  
-ATOM  12434  O   MET B 944       1.246  17.065 -20.075  1.00 69.56           O  
-ANISOU12434  O   MET B 944     8037  11826   6565   2236     27    368       O  
-ATOM  12435  CB  MET B 944      -1.010  14.806 -21.367  1.00 70.86           C  
-ANISOU12435  CB  MET B 944     7825  13051   6049   1932    -26     78       C  
-ATOM  12436  CG  MET B 944      -1.882  16.044 -21.420  1.00 74.49           C  
-ANISOU12436  CG  MET B 944     8216  13769   6316   2279    -15    167       C  
-ATOM  12437  SD  MET B 944      -1.665  16.975 -22.947  1.00 75.37           S  
-ANISOU12437  SD  MET B 944     8343  13940   6353   2634    116    341       S  
-ATOM  12438  CE  MET B 944      -2.449  15.866 -24.114  1.00 76.74           C  
-ANISOU12438  CE  MET B 944     8304  14648   6206   2493    136    218       C  
-ATOM  12439  N   GLU B 945       0.383  15.397 -18.839  1.00 70.19           N  
-ANISOU12439  N   GLU B 945     7627   9900   9143   3262    607   1081       N  
-ATOM  12440  CA  GLU B 945       0.542  16.106 -17.574  1.00 70.40           C  
-ANISOU12440  CA  GLU B 945     7821   9793   9135   3303    658   1232       C  
-ATOM  12441  C   GLU B 945       1.926  16.716 -17.415  1.00 68.88           C  
-ANISOU12441  C   GLU B 945     7819   9387   8966   3309    685   1238       C  
-ATOM  12442  O   GLU B 945       2.063  17.827 -16.904  1.00 67.65           O  
-ANISOU12442  O   GLU B 945     7832   9185   8686   3415    760   1350       O  
-ATOM  12443  CB  GLU B 945       0.236  15.184 -16.393  1.00 73.36           C  
-ANISOU12443  CB  GLU B 945     8140  10070   9663   3172    608   1278       C  
-ATOM  12444  CG  GLU B 945      -1.242  14.928 -16.177  1.00 79.27           C  
-ANISOU12444  CG  GLU B 945     8747  11020  10351   3194    610   1332       C  
-ATOM  12445  CD  GLU B 945      -1.495  13.816 -15.176  1.00 82.98           C  
-ANISOU12445  CD  GLU B 945     9136  11392  10999   3043    554   1351       C  
-ATOM  12446  OE1 GLU B 945      -0.505  13.246 -14.659  1.00 84.65           O  
-ANISOU12446  OE1 GLU B 945     9404  11379  11379   2925    511   1322       O  
-ATOM  12447  OE2 GLU B 945      -2.681  13.510 -14.912  1.00 85.08           O  
-ANISOU12447  OE2 GLU B 945     9281  11808  11238   3043    554   1396       O  
-ATOM  12448  N   GLU B 946       2.950  15.994 -17.850  1.00 68.78           N  
-ANISOU12448  N   GLU B 946     7779   9242   9112   3195    626   1116       N  
-ATOM  12449  CA  GLU B 946       4.308  16.508 -17.755  1.00 68.20           C  
-ANISOU12449  CA  GLU B 946     7869   8969   9073   3191    647   1111       C  
-ATOM  12450  C   GLU B 946       4.472  17.757 -18.605  1.00 67.58           C  
-ANISOU12450  C   GLU B 946     7896   8977   8804   3349    732   1122       C  
-ATOM  12451  O   GLU B 946       5.125  18.714 -18.192  1.00 65.99           O  
-ANISOU12451  O   GLU B 946     7876   8659   8540   3409    792   1195       O  
-ATOM  12452  CB  GLU B 946       5.328  15.450 -18.165  1.00 70.24           C  
-ANISOU12452  CB  GLU B 946     8060   9090   9537   3045    569    972       C  
-ATOM  12453  CG  GLU B 946       5.602  14.407 -17.098  1.00 72.18           C  
-ANISOU12453  CG  GLU B 946     8274   9167   9986   2891    499    982       C  
-ATOM  12454  CD  GLU B 946       6.616  13.367 -17.552  1.00 73.49           C  
-ANISOU12454  CD  GLU B 946     8374   9198  10350   2756    427    844       C  
-ATOM  12455  OE1 GLU B 946       7.254  13.578 -18.611  1.00 74.01           O  
-ANISOU12455  OE1 GLU B 946     8446   9279  10395   2786    437    750       O  
-ATOM  12456  OE2 GLU B 946       6.767  12.338 -16.853  1.00 73.65           O  
-ANISOU12456  OE2 GLU B 946     8338   9099  10545   2625    363    833       O  
-ATOM  12457  N   LEU B 947       3.866  17.750 -19.787  1.00 69.43           N  
-ANISOU12457  N   LEU B 947     8018   9418   8944   3417    738   1050       N  
-ATOM  12458  CA  LEU B 947       3.954  18.898 -20.684  1.00 70.29           C  
-ANISOU12458  CA  LEU B 947     8216   9626   8864   3576    822   1058       C  
-ATOM  12459  C   LEU B 947       3.138  20.087 -20.184  1.00 70.93           C  
-ANISOU12459  C   LEU B 947     8406   9805   8741   3735    914   1212       C  
-ATOM  12460  O   LEU B 947       3.541  21.239 -20.355  1.00 71.41           O  
-ANISOU12460  O   LEU B 947     8627   9835   8669   3853   1000   1266       O  
-ATOM  12461  CB  LEU B 947       3.541  18.522 -22.110  1.00 70.15           C  
-ANISOU12461  CB  LEU B 947     8045   9807   8800   3607    799    934       C  
-ATOM  12462  CG  LEU B 947       4.496  17.593 -22.869  1.00 69.38           C  
-ANISOU12462  CG  LEU B 947     7874   9618   8870   3484    730    773       C  
-ATOM  12463  CD1 LEU B 947       4.014  17.379 -24.294  1.00 68.76           C  
-ANISOU12463  CD1 LEU B 947     7660   9754   8711   3538    718    660       C  
-ATOM  12464  CD2 LEU B 947       5.912  18.149 -22.855  1.00 67.03           C  
-ANISOU12464  CD2 LEU B 947     7743   9113   8611   3481    767    769       C  
-ATOM  12465  N   THR B 948       1.993  19.806 -19.571  1.00 76.22           N  
-ANISOU12465  N   THR B 948     8989  10587   9386   3739    900   1282       N  
-ATOM  12466  CA  THR B 948       1.174  20.858 -18.982  1.00 76.69           C  
-ANISOU12466  CA  THR B 948     9146  10732   9260   3886    987   1435       C  
-ATOM  12467  C   THR B 948       1.944  21.573 -17.874  1.00 74.38           C  
-ANISOU12467  C   THR B 948     9069  10216   8975   3887   1034   1538       C  
-ATOM  12468  O   THR B 948       1.916  22.799 -17.781  1.00 73.86           O  
-ANISOU12468  O   THR B 948     9162  10159   8742   4028   1130   1632       O  
-ATOM  12469  CB  THR B 948      -0.150  20.307 -18.421  1.00 77.99           C  
-ANISOU12469  CB  THR B 948     9169  11043   9422   3871    958   1491       C  
-ATOM  12470  OG1 THR B 948      -0.855  19.603 -19.451  1.00 79.53           O  
-ANISOU12470  OG1 THR B 948     9155  11446   9616   3857    907   1386       O  
-ATOM  12471  CG2 THR B 948      -1.017  21.440 -17.906  1.00 80.54           C  
-ANISOU12471  CG2 THR B 948     9592  11470   9541   4039   1054   1649       C  
-ATOM  12472  N   ASP B 949       2.633  20.801 -17.039  1.00 87.82           N  
-ANISOU12472  N   ASP B 949    10779  11720  10870   3731    967   1520       N  
-ATOM  12473  CA  ASP B 949       3.470  21.369 -15.989  1.00 85.75           C  
-ANISOU12473  CA  ASP B 949    10712  11237  10633   3713    996   1602       C  
-ATOM  12474  C   ASP B 949       4.541  22.265 -16.586  1.00 83.14           C  
-ANISOU12474  C   ASP B 949    10532  10813  10244   3770   1053   1573       C  
-ATOM  12475  O   ASP B 949       4.779  23.371 -16.105  1.00 82.49           O  
-ANISOU12475  O   ASP B 949    10636  10659  10048   3858   1134   1669       O  
-ATOM  12476  CB  ASP B 949       4.128  20.268 -15.158  1.00 89.93           C  
-ANISOU12476  CB  ASP B 949    11203  11575  11392   3529    903   1566       C  
-ATOM  12477  CG  ASP B 949       3.150  19.575 -14.232  1.00 93.62           C  
-ANISOU12477  CG  ASP B 949    11574  12087  11909   3477    866   1633       C  
-ATOM  12478  OD1 ASP B 949       1.950  19.510 -14.576  1.00 97.05           O  
-ANISOU12478  OD1 ASP B 949    11892  12732  12252   3542    880   1651       O  
-ATOM  12479  OD2 ASP B 949       3.581  19.095 -13.160  1.00 95.76           O  
-ANISOU12479  OD2 ASP B 949    11887  12186  12311   3372    824   1668       O  
-ATOM  12480  N   THR B 950       5.188  21.777 -17.638  1.00 56.75           N  
-ANISOU12480  N   THR B 950     7110   7470   6981   3718   1014   1438       N  
-ATOM  12481  CA  THR B 950       6.243  22.534 -18.290  1.00 54.87           C  
-ANISOU12481  CA  THR B 950     6999   7146   6702   3762   1067   1399       C  
-ATOM  12482  C   THR B 950       5.686  23.838 -18.852  1.00 56.12           C  
-ANISOU12482  C   THR B 950     7255   7449   6619   3958   1181   1469       C  
-ATOM  12483  O   THR B 950       6.254  24.911 -18.636  1.00 56.95           O  
-ANISOU12483  O   THR B 950     7549   7452   6637   4028   1262   1531       O  
-ATOM  12484  CB  THR B 950       6.903  21.727 -19.419  1.00 52.09           C  
-ANISOU12484  CB  THR B 950     6526   6796   6469   3683   1007   1239       C  
-ATOM  12485  OG1 THR B 950       7.145  20.385 -18.977  1.00 49.72           O  
-ANISOU12485  OG1 THR B 950     6103   6403   6384   3512    900   1172       O  
-ATOM  12486  CG2 THR B 950       8.220  22.368 -19.822  1.00 49.86           C  
-ANISOU12486  CG2 THR B 950     6384   6367   6195   3690   1051   1202       C  
-ATOM  12487  N   ALA B 951       4.569  23.743 -19.566  1.00 56.89           N  
-ANISOU12487  N   ALA B 951     7223   7783   6608   4045   1188   1459       N  
-ATOM  12488  CA  ALA B 951       3.925  24.923 -20.128  1.00 59.03           C  
-ANISOU12488  CA  ALA B 951     7570   8215   6644   4242   1295   1529       C  
-ATOM  12489  C   ALA B 951       3.641  25.961 -19.048  1.00 59.55           C  
-ANISOU12489  C   ALA B 951     7817   8220   6591   4332   1380   1688       C  
-ATOM  12490  O   ALA B 951       3.788  27.161 -19.276  1.00 59.35           O  
-ANISOU12490  O   ALA B 951     7951   8192   6406   4468   1485   1750       O  
-ATOM  12491  CB  ALA B 951       2.641  24.536 -20.842  1.00 58.94           C  
-ANISOU12491  CB  ALA B 951     7373   8476   6547   4309   1275   1505       C  
-ATOM  12492  N   GLU B 952       3.235  25.493 -17.872  1.00 75.85           N  
-ANISOU12492  N   GLU B 952     9859  10230   8730   4258   1337   1754       N  
-ATOM  12493  CA  GLU B 952       2.905  26.393 -16.775  1.00 77.04           C  
-ANISOU12493  CA  GLU B 952    10175  10324   8772   4338   1412   1905       C  
-ATOM  12494  C   GLU B 952       4.152  27.024 -16.166  1.00 74.51           C  
-ANISOU12494  C   GLU B 952    10065   9753   8491   4297   1445   1929       C  
-ATOM  12495  O   GLU B 952       4.095  28.122 -15.619  1.00 74.04           O  
-ANISOU12495  O   GLU B 952    10189   9646   8298   4399   1538   2038       O  
-ATOM  12496  CB  GLU B 952       2.081  25.669 -15.709  1.00 82.33           C  
-ANISOU12496  CB  GLU B 952    10754  11017   9512   4270   1356   1967       C  
-ATOM  12497  CG  GLU B 952       0.681  25.303 -16.179  1.00 93.16           C  
-ANISOU12497  CG  GLU B 952    11941  12653  10804   4339   1346   1974       C  
-ATOM  12498  CD  GLU B 952      -0.017  24.323 -15.255  1.00 98.62           C  
-ANISOU12498  CD  GLU B 952    12505  13357  11608   4234   1275   2006       C  
-ATOM  12499  OE1 GLU B 952      -1.213  24.037 -15.488  1.00102.53           O  
-ANISOU12499  OE1 GLU B 952    12850  14064  12041   4284   1269   2024       O  
-ATOM  12500  OE2 GLU B 952       0.629  23.835 -14.301  1.00101.99           O  
-ANISOU12500  OE2 GLU B 952    12981  13585  12187   4104   1226   2013       O  
-ATOM  12501  N   ILE B 953       5.278  26.333 -16.270  1.00 59.62           N  
-ANISOU12501  N   ILE B 953     8153   7711   6788   4149   1371   1825       N  
-ATOM  12502  CA  ILE B 953       6.539  26.892 -15.809  1.00 59.38           C  
-ANISOU12502  CA  ILE B 953     8306   7452   6804   4102   1397   1833       C  
-ATOM  12503  C   ILE B 953       6.979  28.004 -16.749  1.00 62.49           C  
-ANISOU12503  C   ILE B 953     8823   7863   7057   4223   1499   1822       C  
-ATOM  12504  O   ILE B 953       7.416  29.066 -16.304  1.00 63.12           O  
-ANISOU12504  O   ILE B 953     9103   7830   7049   4280   1582   1896       O  
-ATOM  12505  CB  ILE B 953       7.643  25.829 -15.745  1.00 54.59           C  
-ANISOU12505  CB  ILE B 953     7625   6684   6431   3916   1290   1722       C  
-ATOM  12506  CG1 ILE B 953       7.221  24.680 -14.831  1.00 52.99           C  
-ANISOU12506  CG1 ILE B 953     7301   6457   6374   3795   1192   1731       C  
-ATOM  12507  CG2 ILE B 953       8.943  26.446 -15.254  1.00 51.52           C  
-ANISOU12507  CG2 ILE B 953     7422   6068   6086   3869   1316   1732       C  
-ATOM  12508  CD1 ILE B 953       8.294  23.645 -14.636  1.00 49.32           C  
-ANISOU12508  CD1 ILE B 953     6777   5823   6139   3618   1091   1636       C  
-ATOM  12509  N   ILE B 954       6.852  27.768 -18.050  1.00 68.35           N  
-ANISOU12509  N   ILE B 954     9447   8747   7777   4261   1495   1730       N  
-ATOM  12510  CA  ILE B 954       7.232  28.765 -19.046  1.00 71.48           C  
-ANISOU12510  CA  ILE B 954     9946   9179   8035   4384   1594   1717       C  
-ATOM  12511  C   ILE B 954       6.426  30.053 -18.884  1.00 75.05           C  
-ANISOU12511  C   ILE B 954    10552   9702   8262   4564   1718   1855       C  
-ATOM  12512  O   ILE B 954       6.927  31.147 -19.143  1.00 76.06           O  
-ANISOU12512  O   ILE B 954    10870   9734   8297   4635   1816   1897       O  
-ATOM  12513  CB  ILE B 954       7.044  28.231 -20.479  1.00 20.00           C  
-ATOM  12514  CG1 ILE B 954       8.176  27.268 -20.842  1.00 20.00           C  
-ATOM  12515  CG2 ILE B 954       6.978  29.382 -21.471  1.00 20.00           C  
-ATOM  12516  CD1 ILE B 954       7.700  25.974 -21.465  1.00 20.00           C  
-ATOM  12517  N   ARG B 955       5.177  29.911 -18.453  1.00 83.21           N  
-ANISOU12517  N   ARG B 955    11502  10901   9212   4634   1715   1926       N  
-ATOM  12518  CA  ARG B 955       4.287  31.051 -18.254  1.00 87.42           C  
-ANISOU12518  CA  ARG B 955    12154  11538   9523   4820   1830   2059       C  
-ATOM  12519  C   ARG B 955       4.540  31.824 -16.963  1.00 86.83           C  
-ANISOU12519  C   ARG B 955    12289  11288   9415   4825   1888   2174       C  
-ATOM  12520  O   ARG B 955       4.300  33.028 -16.901  1.00 86.92           O  
-ANISOU12520  O   ARG B 955    12469  11310   9246   4973   2008   2270       O  
-ATOM  12521  CB  ARG B 955       2.826  30.593 -18.289  1.00 91.95           C  
-ANISOU12521  CB  ARG B 955    12558  12350  10029   4885   1803   2097       C  
-ATOM  12522  CG  ARG B 955       2.300  30.298 -19.684  1.00100.35           C  
-ANISOU12522  CG  ARG B 955    13456  13641  11030   4958   1791   2016       C  
-ATOM  12523  CD  ARG B 955       0.935  29.626 -19.640  1.00105.87           C  
-ANISOU12523  CD  ARG B 955    13958  14563  11703   4981   1739   2036       C  
-ATOM  12524  NE  ARG B 955       0.232  29.728 -20.917  1.00109.93           N  
-ANISOU12524  NE  ARG B 955    14354  15327  12086   5107   1760   1995       N  
-ATOM  12525  CZ  ARG B 955       0.595  29.094 -22.029  1.00111.27           C  
-ANISOU12525  CZ  ARG B 955    14397  15559  12323   5055   1701   1857       C  
-ATOM  12526  NH1 ARG B 955       1.669  28.313 -22.030  1.00111.61           N  
-ANISOU12526  NH1 ARG B 955    14414  15428  12566   4880   1622   1748       N  
-ATOM  12527  NH2 ARG B 955      -0.111  29.247 -23.142  1.00112.57           N  
-ANISOU12527  NH2 ARG B 955    14462  15961  12350   5182   1723   1829       N  
-ATOM  12528  N   LYS B 956       5.020  31.133 -15.935  1.00 86.17           N  
-ANISOU12528  N   LYS B 956    12198  11044   9500   4665   1803   2166       N  
-ATOM  12529  CA  LYS B 956       5.114  31.725 -14.605  1.00 84.22           C  
-ANISOU12529  CA  LYS B 956    12128  10648   9223   4663   1841   2277       C  
-ATOM  12530  C   LYS B 956       6.541  32.096 -14.214  1.00 81.69           C  
-ANISOU12530  C   LYS B 956    11973  10076   8990   4566   1847   2248       C  
-ATOM  12531  O   LYS B 956       6.756  32.866 -13.281  1.00 81.58           O  
-ANISOU12531  O   LYS B 956    12146   9932   8918   4586   1902   2335       O  
-ATOM  12532  CB  LYS B 956       4.509  30.778 -13.567  1.00 87.19           C  
-ANISOU12532  CB  LYS B 956    12393  11030   9704   4569   1751   2312       C  
-ATOM  12533  CG  LYS B 956       3.055  30.420 -13.835  1.00 92.90           C  
-ANISOU12533  CG  LYS B 956    12951  12000  10345   4657   1747   2350       C  
-ATOM  12534  CD  LYS B 956       2.587  29.290 -12.931  1.00 96.82           C  
-ANISOU12534  CD  LYS B 956    13312  12492  10982   4534   1646   2360       C  
-ATOM  12535  CE  LYS B 956       1.148  28.891 -13.228  1.00100.25           C  
-ANISOU12535  CE  LYS B 956    13567  13178  11344   4610   1640   2390       C  
-ATOM  12536  NZ  LYS B 956       0.182  29.986 -12.919  1.00100.98           N  
-ANISOU12536  NZ  LYS B 956    13769  13382  11217   4798   1755   2531       N  
-ATOM  12537  N   ALA B 957       7.514  31.549 -14.933  1.00 77.32           N  
-ANISOU12537  N   ALA B 957    11348   9457   8572   4462   1789   2123       N  
-ATOM  12538  CA  ALA B 957       8.916  31.793 -14.620  1.00 76.17           C  
-ANISOU12538  CA  ALA B 957    11333   9081   8526   4358   1784   2084       C  
-ATOM  12539  C   ALA B 957       9.412  33.089 -15.245  1.00 75.70           C  
-ANISOU12539  C   ALA B 957    11453   8983   8326   4467   1911   2099       C  
-ATOM  12540  O   ALA B 957       9.117  33.383 -16.403  1.00 76.51           O  
-ANISOU12540  O   ALA B 957    11516   9226   8330   4574   1967   2070       O  
-ATOM  12541  CB  ALA B 957       9.765  30.629 -15.083  1.00 76.81           C  
-ANISOU12541  CB  ALA B 957    11260   9104   8819   4199   1669   1947       C  
-ATOM  12542  N   THR B 958      10.169  33.860 -14.473  1.00 74.67           N  
-ANISOU12542  N   THR B 958    11523   8663   8185   4439   1958   2145       N  
-ATOM  12543  CA  THR B 958      10.772  35.090 -14.972  1.00 73.02           C  
-ANISOU12543  CA  THR B 958    11501   8384   7861   4521   2082   2157       C  
-ATOM  12544  C   THR B 958      12.280  34.918 -15.065  1.00 72.79           C  
-ANISOU12544  C   THR B 958    11504   8163   7989   4374   2041   2062       C  
-ATOM  12545  O   THR B 958      12.797  33.813 -14.919  1.00 70.91           O  
-ANISOU12545  O   THR B 958    11129   7872   7941   4226   1919   1982       O  
-ATOM  12546  CB  THR B 958      10.470  36.286 -14.049  1.00 73.34           C  
-ANISOU12546  CB  THR B 958    11770   8352   7745   4615   2188   2287       C  
-ATOM  12547  OG1 THR B 958      11.336  36.248 -12.905  1.00 70.60           O  
-ANISOU12547  OG1 THR B 958    11525   7790   7508   4477   2139   2292       O  
-ATOM  12548  CG2 THR B 958       9.015  36.257 -13.589  1.00 70.27           C  
-ANISOU12548  CG2 THR B 958    11337   8126   7238   4727   2202   2389       C  
-ATOM  12549  N   SER B 959      12.986  36.015 -15.308  1.00 79.09           N  
-ANISOU12549  N   SER B 959    12486   8856   8708   4417   2147   2074       N  
-ATOM  12550  CA  SER B 959      14.440  35.979 -15.369  1.00 79.36           C  
-ANISOU12550  CA  SER B 959    12566   8706   8882   4282   2121   1991       C  
-ATOM  12551  C   SER B 959      14.996  35.799 -13.972  1.00 77.96           C  
-ANISOU12551  C   SER B 959    12461   8349   8811   4148   2052   2017       C  
-ATOM  12552  O   SER B 959      16.174  35.506 -13.793  1.00 76.70           O  
-ANISOU12552  O   SER B 959    12304   8036   8801   4009   1995   1948       O  
-ATOM  12553  CB  SER B 959      14.986  37.263 -15.998  1.00 80.08           C  
-ANISOU12553  CB  SER B 959    12840   8736   8849   4368   2265   2002       C  
-ATOM  12554  OG  SER B 959      14.502  38.409 -15.320  1.00 82.39           O  
-ANISOU12554  OG  SER B 959    13338   8996   8972   4474   2374   2120       O  
-ATOM  12555  N   GLN B 960      14.129  35.975 -12.983  1.00 82.06           N  
-ANISOU12555  N   GLN B 960    13037   8893   9249   4197   2058   2119       N  
-ATOM  12556  CA  GLN B 960      14.505  35.814 -11.587  1.00 79.34           C  
-ANISOU12556  CA  GLN B 960    12766   8395   8986   4086   1993   2156       C  
-ATOM  12557  C   GLN B 960      14.289  34.383 -11.107  1.00 75.87           C  
-ANISOU12557  C   GLN B 960    12129   7985   8713   3972   1844   2123       C  
-ATOM  12558  O   GLN B 960      14.932  33.935 -10.161  1.00 74.54           O  
-ANISOU12558  O   GLN B 960    11973   7677   8673   3841   1759   2113       O  
-ATOM  12559  CB  GLN B 960      13.706  36.783 -10.716  1.00 82.64           C  
-ANISOU12559  CB  GLN B 960    13363   8813   9224   4199   2084   2288       C  
-ATOM  12560  CG  GLN B 960      14.095  38.230 -10.913  1.00 86.21           C  
-ANISOU12560  CG  GLN B 960    14046   9182   9529   4285   2229   2326       C  
-ATOM  12561  CD  GLN B 960      15.530  38.492 -10.501  1.00 88.42           C  
-ANISOU12561  CD  GLN B 960    14438   9242   9916   4144   2209   2272       C  
-ATOM  12562  OE1 GLN B 960      15.900  38.296  -9.344  1.00 91.18           O  
-ANISOU12562  OE1 GLN B 960    14839   9466  10338   4040   2142   2291       O  
-ATOM  12563  NE2 GLN B 960      16.349  38.926 -11.449  1.00 91.01           N  
-ANISOU12563  NE2 GLN B 960    14800   9527  10253   4138   2267   2205       N  
-ATOM  12564  N   SER B 961      13.381  33.672 -11.767  1.00 61.87           N  
-ANISOU12564  N   SER B 961    10175   6396   6936   4023   1813   2104       N  
-ATOM  12565  CA  SER B 961      13.024  32.324 -11.361  1.00 58.62           C  
-ANISOU12565  CA  SER B 961     9575   6028   6671   3926   1684   2077       C  
-ATOM  12566  C   SER B 961      14.208  31.380 -11.391  1.00 55.92           C  
-ANISOU12566  C   SER B 961     9137   5560   6551   3753   1572   1968       C  
-ATOM  12567  O   SER B 961      15.209  31.644 -12.054  1.00 56.90           O  
-ANISOU12567  O   SER B 961     9293   5608   6717   3719   1592   1895       O  
-ATOM  12568  CB  SER B 961      11.926  31.778 -12.265  1.00 58.70           C  
-ANISOU12568  CB  SER B 961     9405   6263   6637   4009   1678   2058       C  
-ATOM  12569  OG  SER B 961      10.795  32.623 -12.248  1.00 59.71           O  
-ANISOU12569  OG  SER B 961     9609   6520   6557   4177   1780   2163       O  
-ATOM  12570  N   LEU B 962      14.085  30.286 -10.651  1.00 52.75           N  
-ANISOU12570  N   LEU B 962     8620   5135   6289   3648   1458   1962       N  
-ATOM  12571  CA  LEU B 962      15.003  29.168 -10.770  1.00 48.10           C  
-ANISOU12571  CA  LEU B 962     7897   4460   5917   3495   1343   1858       C  
-ATOM  12572  C   LEU B 962      14.227  27.980 -11.311  1.00 47.90           C  
-ANISOU12572  C   LEU B 962     7649   4585   5967   3480   1273   1808       C  
-ATOM  12573  O   LEU B 962      13.343  27.453 -10.639  1.00 46.22           O  
-ANISOU12573  O   LEU B 962     7371   4431   5758   3478   1233   1865       O  
-ATOM  12574  CB  LEU B 962      15.611  28.807  -9.422  1.00 45.09           C  
-ANISOU12574  CB  LEU B 962     7570   3911   5653   3373   1263   1887       C  
-ATOM  12575  CG  LEU B 962      16.257  27.420  -9.453  1.00 41.29           C  
-ANISOU12575  CG  LEU B 962     6917   3374   5399   3225   1134   1793       C  
-ATOM  12576  CD1 LEU B 962      17.410  27.393 -10.452  1.00 38.32           C  
-ANISOU12576  CD1 LEU B 962     6511   2941   5109   3174   1132   1680       C  
-ATOM  12577  CD2 LEU B 962      16.718  26.975  -8.069  1.00 40.20           C  
-ANISOU12577  CD2 LEU B 962     6818   3086   5370   3116   1050   1832       C  
-ATOM  12578  N   VAL B 963      14.554  27.567 -12.529  1.00 54.96           N  
-ANISOU12578  N   VAL B 963     8427   5539   6918   3468   1261   1701       N  
-ATOM  12579  CA  VAL B 963      13.821  26.500 -13.188  1.00 56.58           C  
-ANISOU12579  CA  VAL B 963     8421   5894   7181   3458   1201   1642       C  
-ATOM  12580  C   VAL B 963      14.656  25.241 -13.266  1.00 54.97           C  
-ANISOU12580  C   VAL B 963     8081   5600   7206   3303   1086   1537       C  
-ATOM  12581  O   VAL B 963      15.755  25.248 -13.815  1.00 54.62           O  
-ANISOU12581  O   VAL B 963     8046   5466   7240   3250   1080   1456       O  
-ATOM  12582  CB  VAL B 963      13.419  26.890 -14.613  1.00 57.93           C  
-ANISOU12582  CB  VAL B 963     8546   6230   7236   3573   1272   1595       C  
-ATOM  12583  CG1 VAL B 963      12.857  25.684 -15.341  1.00 59.38           C  
-ANISOU12583  CG1 VAL B 963     8504   6551   7506   3537   1196   1509       C  
-ATOM  12584  CG2 VAL B 963      12.415  28.027 -14.600  1.00 61.89           C  
-ANISOU12584  CG2 VAL B 963     9159   6850   7507   3741   1385   1703       C  
-ATOM  12585  N   ILE B 964      14.125  24.156 -12.719  1.00 56.60           N  
-ANISOU12585  N   ILE B 964     8158   5829   7517   3231    999   1539       N  
-ATOM  12586  CA  ILE B 964      14.809  22.877 -12.769  1.00 53.88           C  
-ANISOU12586  CA  ILE B 964     7677   5404   7390   3088    891   1443       C  
-ATOM  12587  C   ILE B 964      13.984  21.865 -13.541  1.00 54.19           C  
-ANISOU12587  C   ILE B 964     7515   5600   7474   3080    847   1375       C  
-ATOM  12588  O   ILE B 964      13.015  21.320 -13.022  1.00 53.94           O  
-ANISOU12588  O   ILE B 964     7407   5642   7447   3074    814   1421       O  
-ATOM  12589  CB  ILE B 964      15.069  22.333 -11.369  1.00 53.38           C  
-ANISOU12589  CB  ILE B 964     7639   5200   7444   2985    816   1498       C  
-ATOM  12590  CG1 ILE B 964      15.996  23.280 -10.612  1.00 51.33           C  
-ANISOU12590  CG1 ILE B 964     7574   4778   7152   2978    849   1551       C  
-ATOM  12591  CG2 ILE B 964      15.663  20.944 -11.458  1.00 53.29           C  
-ANISOU12591  CG2 ILE B 964     7475   5118   7654   2848    707   1402       C  
-ATOM  12592  CD1 ILE B 964      16.094  22.997  -9.134  1.00 51.22           C  
-ANISOU12592  CD1 ILE B 964     7616   4643   7202   2907    791   1629       C  
-ATOM  12593  N   LEU B 965      14.370  21.621 -14.786  1.00 39.75           N  
-ANISOU12593  N   LEU B 965     5604   3822   5678   3080    847   1264       N  
-ATOM  12594  CA  LEU B 965      13.645  20.696 -15.636  1.00 41.92           C  
-ANISOU12594  CA  LEU B 965     5690   4249   5990   3072    806   1184       C  
-ATOM  12595  C   LEU B 965      14.433  19.412 -15.788  1.00 42.71           C  
-ANISOU12595  C   LEU B 965     5666   4249   6314   2928    708   1074       C  
-ATOM  12596  O   LEU B 965      15.625  19.438 -16.099  1.00 45.28           O  
-ANISOU12596  O   LEU B 965     6027   4454   6723   2879    700   1011       O  
-ATOM  12597  CB  LEU B 965      13.397  21.323 -17.003  1.00 43.27           C  
-ANISOU12597  CB  LEU B 965     5850   4569   6021   3188    880   1135       C  
-ATOM  12598  CG  LEU B 965      12.478  22.540 -16.996  1.00 44.81           C  
-ANISOU12598  CG  LEU B 965     6151   4891   5984   3347    983   1241       C  
-ATOM  12599  CD1 LEU B 965      12.378  23.146 -18.378  1.00 43.83           C  
-ANISOU12599  CD1 LEU B 965     6022   4901   5729   3461   1055   1188       C  
-ATOM  12600  CD2 LEU B 965      11.102  22.144 -16.489  1.00 46.53           C  
-ANISOU12600  CD2 LEU B 965     6279   5244   6155   3373    961   1306       C  
-ATOM  12601  N   ASP B 966      13.767  18.284 -15.582  1.00 50.32           N  
-ANISOU12601  N   ASP B 966     6483   5263   7375   2860    636   1052       N  
-ATOM  12602  CA  ASP B 966      14.453  17.000 -15.611  1.00 50.10           C  
-ANISOU12602  CA  ASP B 966     6342   5131   7564   2721    543    956       C  
-ATOM  12603  C   ASP B 966      13.769  15.991 -16.525  1.00 49.72           C  
-ANISOU12603  C   ASP B 966     6105   5221   7567   2694    502    856       C  
-ATOM  12604  O   ASP B 966      12.550  15.857 -16.518  1.00 48.35           O  
-ANISOU12604  O   ASP B 966     5858   5197   7317   2734    508    888       O  
-ATOM  12605  CB  ASP B 966      14.604  16.453 -14.193  1.00 50.72           C  
-ANISOU12605  CB  ASP B 966     6443   5067   7760   2628    482   1027       C  
-ATOM  12606  CG  ASP B 966      14.928  14.976 -14.167  1.00 51.30           C  
-ANISOU12606  CG  ASP B 966     6375   5067   8049   2494    387    942       C  
-ATOM  12607  OD1 ASP B 966      16.033  14.592 -14.609  1.00 53.00           O  
-ANISOU12607  OD1 ASP B 966     6572   5178   8386   2432    356    853       O  
-ATOM  12608  OD2 ASP B 966      14.081  14.193 -13.685  1.00 53.04           O  
-ANISOU12608  OD2 ASP B 966     6504   5331   8319   2452    347    966       O  
-ATOM  12609  N   GLU B 967      14.577  15.292 -17.314  1.00 56.82           N  
-ANISOU12609  N   GLU B 967     6926   6068   8594   2625    462    731       N  
-ATOM  12610  CA  GLU B 967      14.083  14.345 -18.302  1.00 57.85           C  
-ANISOU12610  CA  GLU B 967     6885   6319   8777   2595    424    616       C  
-ATOM  12611  C   GLU B 967      12.844  14.848 -19.028  1.00 58.40           C  
-ANISOU12611  C   GLU B 967     6909   6620   8661   2710    475    627       C  
-ATOM  12612  O   GLU B 967      11.824  14.168 -19.087  1.00 58.62           O  
-ANISOU12612  O   GLU B 967     6810   6768   8696   2689    442    611       O  
-ATOM  12613  CB  GLU B 967      13.848  12.976 -17.669  1.00 60.12           C  
-ANISOU12613  CB  GLU B 967     7055   6545   9243   2466    336    594       C  
-ATOM  12614  CG  GLU B 967      15.141  12.208 -17.464  1.00 63.73           C  
-ANISOU12614  CG  GLU B 967     7508   6804   9904   2351    277    530       C  
-ATOM  12615  CD  GLU B 967      14.983  11.011 -16.552  1.00 67.85           C  
-ANISOU12615  CD  GLU B 967     7954   7232  10595   2232    201    542       C  
-ATOM  12616  OE1 GLU B 967      13.988  10.267 -16.701  1.00 69.88           O  
-ANISOU12616  OE1 GLU B 967     8085   7594  10871   2203    175    515       O  
-ATOM  12617  OE2 GLU B 967      15.856  10.824 -15.676  1.00 70.07           O  
-ANISOU12617  OE2 GLU B 967     8300   7335  10990   2169    168    580       O  
-ATOM  12618  N   LEU B 968      12.953  16.051 -19.584  1.00 47.66           N  
-ANISOU12618  N   LEU B 968     5653   5321   7133   2833    559    654       N  
-ATOM  12619  CA  LEU B 968      11.897  16.625 -20.405  1.00 49.91           C  
-ANISOU12619  CA  LEU B 968     5903   5830   7229   2961    615    660       C  
-ATOM  12620  C   LEU B 968      11.946  16.033 -21.813  1.00 52.04           C  
-ANISOU12620  C   LEU B 968     6044   6205   7524   2954    593    514       C  
-ATOM  12621  O   LEU B 968      12.991  16.043 -22.460  1.00 53.18           O  
-ANISOU12621  O   LEU B 968     6215   6267   7725   2935    599    434       O  
-ATOM  12622  CB  LEU B 968      12.055  18.143 -20.465  1.00 49.55           C  
-ANISOU12622  CB  LEU B 968     6031   5797   6997   3098    719    746       C  
-ATOM  12623  CG  LEU B 968      11.191  18.904 -21.474  1.00 50.38           C  
-ANISOU12623  CG  LEU B 968     6125   6124   6894   3251    791    750       C  
-ATOM  12624  CD1 LEU B 968       9.713  18.536 -21.341  1.00 51.43           C  
-ANISOU12624  CD1 LEU B 968     6138   6444   6959   3282    770    784       C  
-ATOM  12625  CD2 LEU B 968      11.397  20.404 -21.309  1.00 47.06           C  
-ANISOU12625  CD2 LEU B 968     5898   5680   6302   3379    899    853       C  
-ATOM  12626  N   GLY B 969      10.818  15.514 -22.286  1.00 55.50           N  
-ANISOU12626  N   GLY B 969     6340   6828   7920   2968    567    476       N  
-ATOM  12627  CA  GLY B 969      10.777  14.873 -23.588  1.00 57.87           C  
-ANISOU12627  CA  GLY B 969     6508   7237   8244   2954    539    332       C  
-ATOM  12628  C   GLY B 969      10.635  13.370 -23.473  1.00 59.47           C  
-ANISOU12628  C   GLY B 969     6553   7406   8637   2805    441    241       C  
-ATOM  12629  O   GLY B 969      10.446  12.673 -24.470  1.00 58.78           O  
-ANISOU12629  O   GLY B 969     6339   7416   8580   2777    406    117       O  
-ATOM  12630  N   ARG B 970      10.739  12.873 -22.243  1.00 69.59           N  
-ANISOU12630  N   ARG B 970     7849   8545  10046   2708    399    305       N  
-ATOM  12631  CA  ARG B 970      10.491  11.471 -21.939  1.00 71.13           C  
-ANISOU12631  CA  ARG B 970     7907   8700  10421   2567    314    243       C  
-ATOM  12632  C   ARG B 970       9.001  11.187 -22.055  1.00 71.31           C  
-ANISOU12632  C   ARG B 970     7802   8929  10362   2588    303    252       C  
-ATOM  12633  O   ARG B 970       8.178  11.944 -21.550  1.00 72.03           O  
-ANISOU12633  O   ARG B 970     7938   9117  10312   2675    347    368       O  
-ATOM  12634  CB  ARG B 970      10.997  11.142 -20.530  1.00 74.03           C  
-ANISOU12634  CB  ARG B 970     8341   8860  10927   2476    283    326       C  
-ATOM  12635  CG  ARG B 970      10.329   9.942 -19.863  1.00 79.09           C  
-ANISOU12635  CG  ARG B 970     8862   9486  11704   2359    216    323       C  
-ATOM  12636  CD  ARG B 970       9.205  10.366 -18.921  1.00 84.30           C  
-ANISOU12636  CD  ARG B 970     9540  10229  12260   2406    240    460       C  
-ATOM  12637  NE  ARG B 970       9.686  11.197 -17.818  1.00 88.42           N  
-ANISOU12637  NE  ARG B 970    10229  10619  12747   2443    276    594       N  
-ATOM  12638  CZ  ARG B 970       9.976  10.740 -16.602  1.00 89.81           C  
-ANISOU12638  CZ  ARG B 970    10443  10633  13046   2359    241    661       C  
-ATOM  12639  NH1 ARG B 970       9.831   9.451 -16.326  1.00 90.88           N  
-ANISOU12639  NH1 ARG B 970    10464  10715  13353   2234    174    612       N  
-ATOM  12640  NH2 ARG B 970      10.408  11.572 -15.662  1.00 89.04           N  
-ANISOU12640  NH2 ARG B 970    10503  10429  12899   2401    274    777       N  
-ATOM  12641  N   GLY B 971       8.653  10.100 -22.729  1.00 64.33           N  
-ANISOU12641  N   GLY B 971     7579   8687   8175   2413   -231   1883       N  
-ATOM  12642  CA  GLY B 971       7.259   9.742 -22.906  1.00 64.24           C  
-ANISOU12642  CA  GLY B 971     7507   8861   8040   2569   -361   2048       C  
-ATOM  12643  C   GLY B 971       6.833   9.817 -24.358  1.00 65.26           C  
-ANISOU12643  C   GLY B 971     7707   9110   7978   2625   -299   2057       C  
-ATOM  12644  O   GLY B 971       5.663   9.614 -24.687  1.00 65.51           O  
-ANISOU12644  O   GLY B 971     7705   9311   7873   2760   -388   2190       O  
-ATOM  12645  N   THR B 972       7.790  10.111 -25.232  1.00 65.45           N  
-ANISOU12645  N   THR B 972     7826   9055   7988   2521   -145   1914       N  
-ATOM  12646  CA  THR B 972       7.524  10.183 -26.659  1.00 64.83           C  
-ANISOU12646  CA  THR B 972     7816   9092   7726   2562    -73   1904       C  
-ATOM  12647  C   THR B 972       8.695   9.575 -27.412  1.00 63.30           C  
-ANISOU12647  C   THR B 972     7535   8846   7672   2378    -34   1663       C  
-ATOM  12648  O   THR B 972       9.672   9.144 -26.802  1.00 62.46           O  
-ANISOU12648  O   THR B 972     7322   8611   7798   2229    -60   1515       O  
-ATOM  12649  CB  THR B 972       7.306  11.644 -27.116  1.00 67.36           C  
-ANISOU12649  CB  THR B 972     8438   9375   7782   2684    146   2044       C  
-ATOM  12650  OG1 THR B 972       6.944  11.672 -28.502  1.00 67.76           O  
-ANISOU12650  OG1 THR B 972     8542   9566   7636   2742    201   2055       O  
-ATOM  12651  CG2 THR B 972       8.567  12.470 -26.900  1.00 67.83           C  
-ANISOU12651  CG2 THR B 972     8655   9211   7908   2565    344   1943       C  
-ATOM  12652  N   SER B 973       8.590   9.531 -28.734  1.00 47.08           N  
-ANISOU12652  N   SER B 973     5520   6900   5468   2393     28   1622       N  
-ATOM  12653  CA ASER B 973       9.675   9.006 -29.549  0.50 50.50           C  
-ANISOU12653  CA ASER B 973     5882   7296   6010   2227     80   1393       C  
-ATOM  12654  CA BSER B 973       9.665   9.027 -29.579  0.50 50.59           C  
-ANISOU12654  CA BSER B 973     5899   7309   6014   2230     84   1395       C  
-ATOM  12655  C   SER B 973      10.931   9.852 -29.390  1.00 49.20           C  
-ANISOU12655  C   SER B 973     5875   6922   5895   2116    283   1305       C  
-ATOM  12656  O   SER B 973      10.880  10.975 -28.891  1.00 45.90           O  
-ANISOU12656  O   SER B 973     5658   6402   5380   2183    411   1431       O  
-ATOM  12657  CB ASER B 973       9.265   8.922 -31.018  0.50 52.26           C  
-ANISOU12657  CB ASER B 973     6138   7691   6027   2281    122   1381       C  
-ATOM  12658  CB BSER B 973       9.249   9.068 -31.048  0.50 52.03           C  
-ANISOU12658  CB BSER B 973     6139   7658   5973   2293    143   1396       C  
-ATOM  12659  OG ASER B 973       8.370   7.844 -31.228  0.50 54.07           O  
-ANISOU12659  OG ASER B 973     6159   8107   6278   2325    -85   1381       O  
-ATOM  12660  OG BSER B 973       9.085  10.404 -31.490  0.50 48.66           O  
-ANISOU12660  OG BSER B 973     5988   7208   5292   2402    348   1539       O  
-ATOM  12661  N   THR B 974      12.059   9.298 -29.813  1.00 50.89           N  
-ANISOU12661  N   THR B 974     5994   7072   6271   1944    313   1082       N  
-ATOM  12662  CA  THR B 974      13.340   9.972 -29.668  1.00 52.78           C  
-ANISOU12662  CA  THR B 974     6350   7117   6588   1815    496    971       C  
-ATOM  12663  C   THR B 974      13.380  11.337 -30.350  1.00 56.60           C  
-ANISOU12663  C   THR B 974     7125   7555   6825   1883    742   1070       C  
-ATOM  12664  O   THR B 974      13.646  12.353 -29.710  1.00 56.81           O  
-ANISOU12664  O   THR B 974     7323   7433   6831   1894    872   1141       O  
-ATOM  12665  CB  THR B 974      14.468   9.122 -30.242  1.00 53.37           C  
-ANISOU12665  CB  THR B 974     6272   7162   6845   1631    495    716       C  
-ATOM  12666  OG1 THR B 974      14.195   7.740 -29.986  1.00 52.06           O  
-ANISOU12666  OG1 THR B 974     5832   7085   6864   1597    263    638       O  
-ATOM  12667  CG2 THR B 974      15.799   9.513 -29.620  1.00 51.63           C  
-ANISOU12667  CG2 THR B 974     6085   6734   6798   1478    609    586       C  
-ATOM  12668  N   HIS B 975      13.122  11.357 -31.653  1.00 65.71           N  
-ANISOU12668  N   HIS B 975     8334   8837   7795   1928    809   1072       N  
-ATOM  12669  CA  HIS B 975      13.266  12.584 -32.424  1.00 69.71           C  
-ANISOU12669  CA  HIS B 975     9109   9301   8077   1983   1055   1156       C  
-ATOM  12670  C   HIS B 975      12.277  13.653 -31.968  1.00 69.65           C  
-ANISOU12670  C   HIS B 975     9301   9287   7875   2172   1112   1415       C  
-ATOM  12671  O   HIS B 975      12.576  14.845 -32.025  1.00 70.42           O  
-ANISOU12671  O   HIS B 975     9634   9255   7867   2198   1325   1492       O  
-ATOM  12672  CB  HIS B 975      13.118  12.308 -33.921  1.00 73.98           C  
-ANISOU12672  CB  HIS B 975     9650  10012   8448   2005   1098   1113       C  
-ATOM  12673  CG  HIS B 975      11.703  12.321 -34.401  1.00 78.14           C  
-ANISOU12673  CG  HIS B 975    10200  10753   8735   2205   1016   1300       C  
-ATOM  12674  ND1 HIS B 975      11.209  13.304 -35.233  1.00 81.07           N  
-ANISOU12674  ND1 HIS B 975    10794  11192   8816   2346   1179   1464       N  
-ATOM  12675  CD2 HIS B 975      10.672  11.475 -34.166  1.00 79.37           C  
-ANISOU12675  CD2 HIS B 975    10181  11075   8900   2288    790   1353       C  
-ATOM  12676  CE1 HIS B 975       9.937  13.061 -35.490  1.00 82.48           C  
-ANISOU12676  CE1 HIS B 975    10930  11579   8830   2511   1051   1606       C  
-ATOM  12677  NE2 HIS B 975       9.585  11.958 -34.854  1.00 81.05           N  
-ANISOU12677  NE2 HIS B 975    10508  11460   8827   2475    815   1539       N  
-ATOM  12678  N   ASP B 976      11.104  13.223 -31.513  1.00 72.57           N  
-ANISOU12678  N   ASP B 976     9574   9793   8206   2304    925   1546       N  
-ATOM  12679  CA  ASP B 976      10.125  14.148 -30.949  1.00 72.56           C  
-ANISOU12679  CA  ASP B 976     9736   9790   8043   2488    956   1789       C  
-ATOM  12680  C   ASP B 976      10.633  14.754 -29.647  1.00 70.88           C  
-ANISOU12680  C   ASP B 976     9594   9365   7974   2438   1008   1796       C  
-ATOM  12681  O   ASP B 976      10.612  15.969 -29.465  1.00 71.41           O  
-ANISOU12681  O   ASP B 976     9894   9314   7924   2508   1185   1914       O  
-ATOM  12682  CB  ASP B 976       8.795  13.443 -30.693  1.00 75.32           C  
-ANISOU12682  CB  ASP B 976     9936  10338   8344   2626    730   1912       C  
-ATOM  12683  CG  ASP B 976       7.789  13.685 -31.792  1.00 80.44           C  
-ANISOU12683  CG  ASP B 976    10666  11190   8708   2795    754   2054       C  
-ATOM  12684  OD1 ASP B 976       8.093  14.465 -32.716  1.00 85.07           O  
-ANISOU12684  OD1 ASP B 976    11440  11758   9123   2818    952   2079       O  
-ATOM  12685  OD2 ASP B 976       6.687  13.105 -31.723  1.00 83.39           O  
-ANISOU12685  OD2 ASP B 976    10913  11745   9026   2906    575   2147       O  
-ATOM  12686  N   GLY B 977      11.087  13.892 -28.743  1.00 54.65           N  
-ANISOU12686  N   GLY B 977     7331   7262   6173   2317    852   1666       N  
-ATOM  12687  CA  GLY B 977      11.564  14.321 -27.442  1.00 50.62           C  
-ANISOU12687  CA  GLY B 977     6849   6577   5808   2263    871   1656       C  
-ATOM  12688  C   GLY B 977      12.667  15.355 -27.530  1.00 51.02           C  
-ANISOU12688  C   GLY B 977     7095   6422   5867   2162   1117   1578       C  
-ATOM  12689  O   GLY B 977      12.555  16.442 -26.965  1.00 53.00           O  
-ANISOU12689  O   GLY B 977     7536   6555   6047   2227   1242   1687       O  
-ATOM  12690  N   ILE B 978      13.737  15.013 -28.238  1.00 48.78           N  
-ANISOU12690  N   ILE B 978     6763   6094   5677   2000   1189   1384       N  
-ATOM  12691  CA  ILE B 978      14.878  15.907 -28.383  1.00 49.22           C  
-ANISOU12691  CA  ILE B 978     6983   5957   5761   1881   1425   1288       C  
-ATOM  12692  C   ILE B 978      14.447  17.275 -28.885  1.00 51.22           C  
-ANISOU12692  C   ILE B 978     7534   6159   5769   2012   1647   1466       C  
-ATOM  12693  O   ILE B 978      14.959  18.301 -28.438  1.00 51.14           O  
-ANISOU12693  O   ILE B 978     7697   5964   5770   1977   1822   1474       O  
-ATOM  12694  CB  ILE B 978      15.919  15.333 -29.344  1.00 47.78           C  
-ANISOU12694  CB  ILE B 978     6713   5777   5665   1716   1479   1077       C  
-ATOM  12695  CG1 ILE B 978      16.415  13.983 -28.833  1.00 46.57           C  
-ANISOU12695  CG1 ILE B 978     6265   5656   5774   1584   1269    896       C  
-ATOM  12696  CG2 ILE B 978      17.081  16.292 -29.493  1.00 47.69           C  
-ANISOU12696  CG2 ILE B 978     6873   5566   5681   1591   1731    985       C  
-ATOM  12697  CD1 ILE B 978      17.441  13.332 -29.737  1.00 47.88           C  
-ANISOU12697  CD1 ILE B 978     6324   5826   6041   1423   1309    677       C  
-ATOM  12698  N   ALA B 979      13.502  17.281 -29.819  1.00 69.02           N  
-ANISOU12698  N   ALA B 979     9842   8580   7803   2163   1640   1607       N  
-ATOM  12699  CA  ALA B 979      12.964  18.525 -30.351  1.00 71.09           C  
-ANISOU12699  CA  ALA B 979    10379   8817   7815   2315   1839   1802       C  
-ATOM  12700  C   ALA B 979      12.423  19.375 -29.212  1.00 70.64           C  
-ANISOU12700  C   ALA B 979    10448   8653   7738   2424   1861   1956       C  
-ATOM  12701  O   ALA B 979      12.845  20.514 -29.021  1.00 72.61           O  
-ANISOU12701  O   ALA B 979    10911   8717   7959   2414   2072   1991       O  
-ATOM  12702  CB  ALA B 979      11.872  18.239 -31.371  1.00 72.23           C  
-ANISOU12702  CB  ALA B 979    10516   9197   7730   2481   1774   1940       C  
-ATOM  12703  N   ILE B 980      11.497  18.801 -28.453  1.00 63.57           N  
-ANISOU12703  N   ILE B 980     9415   7874   6864   2522   1644   2041       N  
-ATOM  12704  CA  ILE B 980      10.888  19.481 -27.321  1.00 62.95           C  
-ANISOU12704  CA  ILE B 980     9428   7723   6767   2635   1636   2185       C  
-ATOM  12705  C   ILE B 980      11.935  19.928 -26.313  1.00 61.90           C  
-ANISOU12705  C   ILE B 980     9329   7365   6826   2485   1720   2053       C  
-ATOM  12706  O   ILE B 980      11.886  21.051 -25.810  1.00 61.81           O  
-ANISOU12706  O   ILE B 980     9517   7208   6761   2541   1871   2140       O  
-ATOM  12707  CB  ILE B 980       9.877  18.574 -26.606  1.00 61.67           C  
-ANISOU12707  CB  ILE B 980     9062   7729   6640   2728   1366   2260       C  
-ATOM  12708  CG1 ILE B 980       8.675  18.317 -27.511  1.00 63.69           C  
-ANISOU12708  CG1 ILE B 980     9309   8211   6679   2905   1293   2419       C  
-ATOM  12709  CG2 ILE B 980       9.430  19.207 -25.299  1.00 62.59           C  
-ANISOU12709  CG2 ILE B 980     9250   7760   6773   2815   1354   2373       C  
-ATOM  12710  CD1 ILE B 980       7.755  17.227 -27.016  1.00 62.96           C  
-ANISOU12710  CD1 ILE B 980     8980   8304   6638   2968   1020   2462       C  
-ATOM  12711  N   ALA B 981      12.877  19.046 -26.010  1.00 56.51           N  
-ANISOU12711  N   ALA B 981     8446   6656   6370   2295   1622   1839       N  
-ATOM  12712  CA  ALA B 981      13.917  19.381 -25.052  1.00 57.87           C  
-ANISOU12712  CA  ALA B 981     8622   6636   6731   2143   1685   1697       C  
-ATOM  12713  C   ALA B 981      14.764  20.550 -25.552  1.00 61.10           C  
-ANISOU12713  C   ALA B 981     9269   6852   7095   2069   1976   1652       C  
-ATOM  12714  O   ALA B 981      14.912  21.557 -24.859  1.00 62.01           O  
-ANISOU12714  O   ALA B 981     9545   6806   7210   2079   2108   1687       O  
-ATOM  12715  CB  ALA B 981      14.783  18.168 -24.764  1.00 59.54           C  
-ANISOU12715  CB  ALA B 981     8566   6871   7187   1960   1528   1479       C  
-ATOM  12716  N   TYR B 982      15.305  20.414 -26.761  1.00 54.02           N  
-ANISOU12716  N   TYR B 982     8394   5973   6160   1995   2080   1573       N  
-ATOM  12717  CA  TYR B 982      16.169  21.440 -27.339  1.00 58.73           C  
-ANISOU12717  CA  TYR B 982     9202   6392   6722   1911   2362   1525       C  
-ATOM  12718  C   TYR B 982      15.427  22.760 -27.427  1.00 58.95           C  
-ANISOU12718  C   TYR B 982     9511   6343   6543   2085   2542   1746       C  
-ATOM  12719  O   TYR B 982      15.925  23.802 -26.998  1.00 59.22           O  
-ANISOU12719  O   TYR B 982     9720   6172   6609   2040   2732   1735       O  
-ATOM  12720  CB  TYR B 982      16.655  21.021 -28.729  1.00 64.04           C  
-ANISOU12720  CB  TYR B 982     9847   7139   7346   1839   2430   1440       C  
-ATOM  12721  CG  TYR B 982      17.787  21.873 -29.268  1.00 72.05           C  
-ANISOU12721  CG  TYR B 982    11029   7967   8380   1703   2706   1342       C  
-ATOM  12722  CD1 TYR B 982      19.111  21.487 -29.102  1.00 74.56           C  
-ANISOU12722  CD1 TYR B 982    11227   8188   8915   1476   2729   1098       C  
-ATOM  12723  CD2 TYR B 982      17.530  23.060 -29.946  1.00 74.89           C  
-ANISOU12723  CD2 TYR B 982    11663   8249   8544   1804   2949   1500       C  
-ATOM  12724  CE1 TYR B 982      20.146  22.259 -29.590  1.00 76.44           C  
-ANISOU12724  CE1 TYR B 982    11610   8259   9176   1346   2984   1007       C  
-ATOM  12725  CE2 TYR B 982      18.558  23.841 -30.435  1.00 77.03           C  
-ANISOU12725  CE2 TYR B 982    12086   8343   8839   1676   3209   1417       C  
-ATOM  12726  CZ  TYR B 982      19.865  23.435 -30.255  1.00 78.25           C  
-ANISOU12726  CZ  TYR B 982    12113   8406   9212   1444   3225   1167       C  
-ATOM  12727  OH  TYR B 982      20.900  24.201 -30.738  1.00 81.16           O  
-ANISOU12727  OH  TYR B 982    12624   8601   9611   1309   3486   1081       O  
-ATOM  12728  N   ALA B 983      14.225  22.702 -27.986  1.00 64.76           N  
-ANISOU12728  N   ALA B 983    10285   7247   7072   2285   2482   1944       N  
-ATOM  12729  CA  ALA B 983      13.408  23.890 -28.153  1.00 65.74           C  
-ANISOU12729  CA  ALA B 983    10669   7325   6986   2477   2642   2176       C  
-ATOM  12730  C   ALA B 983      13.151  24.553 -26.811  1.00 65.11           C  
-ANISOU12730  C   ALA B 983    10661   7112   6966   2525   2643   2232       C  
-ATOM  12731  O   ALA B 983      13.336  25.758 -26.663  1.00 66.71           O  
-ANISOU12731  O   ALA B 983    11095   7126   7126   2548   2864   2290       O  
-ATOM  12732  CB  ALA B 983      12.099  23.540 -28.835  1.00 65.93           C  
-ANISOU12732  CB  ALA B 983    10671   7586   6793   2687   2527   2370       C  
-ATOM  12733  N   THR B 984      12.735  23.763 -25.827  1.00 66.67           N  
-ANISOU12733  N   THR B 984    10661   7406   7266   2538   2402   2210       N  
-ATOM  12734  CA  THR B 984      12.433  24.317 -24.514  1.00 66.36           C  
-ANISOU12734  CA  THR B 984    10671   7267   7274   2592   2384   2262       C  
-ATOM  12735  C   THR B 984      13.661  24.952 -23.886  1.00 66.09           C  
-ANISOU12735  C   THR B 984    10709   6993   7409   2408   2539   2087       C  
-ATOM  12736  O   THR B 984      13.627  26.112 -23.487  1.00 67.23           O  
-ANISOU12736  O   THR B 984    11064   6970   7510   2457   2716   2152       O  
-ATOM  12737  CB  THR B 984      11.884  23.270 -23.548  1.00 64.04           C  
-ANISOU12737  CB  THR B 984    10130   7124   7077   2617   2094   2254       C  
-ATOM  12738  OG1 THR B 984      10.637  22.773 -24.041  1.00 67.02           O  
-ANISOU12738  OG1 THR B 984    10449   7721   7293   2800   1954   2429       O  
-ATOM  12739  CG2 THR B 984      11.662  23.899 -22.190  1.00 65.88           C  
-ANISOU12739  CG2 THR B 984    10423   7254   7356   2664   2093   2295       C  
-ATOM  12740  N   LEU B 985      14.744  24.192 -23.789  1.00 51.80           N  
-ANISOU12740  N   LEU B 985     8721   5166   5796   2198   2474   1860       N  
-ATOM  12741  CA  LEU B 985      15.960  24.722 -23.188  1.00 55.85           C  
-ANISOU12741  CA  LEU B 985     9276   5467   6478   2010   2609   1675       C  
-ATOM  12742  C   LEU B 985      16.348  26.032 -23.854  1.00 62.67           C  
-ANISOU12742  C   LEU B 985    10425   6138   7250   2003   2923   1713       C  
-ATOM  12743  O   LEU B 985      16.661  27.011 -23.181  1.00 63.89           O  
-ANISOU12743  O   LEU B 985    10727   6104   7446   1973   3072   1691       O  
-ATOM  12744  CB  LEU B 985      17.114  23.722 -23.273  1.00 49.76           C  
-ANISOU12744  CB  LEU B 985     8280   4716   5912   1789   2520   1430       C  
-ATOM  12745  CG  LEU B 985      18.416  24.221 -22.642  1.00 45.18           C  
-ANISOU12745  CG  LEU B 985     7721   3932   5513   1585   2649   1225       C  
-ATOM  12746  CD1 LEU B 985      18.184  24.637 -21.198  1.00 41.30           C  
-ANISOU12746  CD1 LEU B 985     7236   3378   5080   1619   2593   1237       C  
-ATOM  12747  CD2 LEU B 985      19.502  23.160 -22.730  1.00 41.83           C  
-ANISOU12747  CD2 LEU B 985     7056   3548   5288   1382   2544    992       C  
-ATOM  12748  N   GLU B 986      16.317  26.049 -25.181  1.00 77.00           N  
-ANISOU12748  N   GLU B 986    12315   8003   8939   2031   3027   1770       N  
-ATOM  12749  CA  GLU B 986      16.655  27.256 -25.920  1.00 84.09           C  
-ANISOU12749  CA  GLU B 986    13483   8727   9740   2033   3332   1827       C  
-ATOM  12750  C   GLU B 986      15.810  28.428 -25.437  1.00 84.57           C  
-ANISOU12750  C   GLU B 986    13775   8683   9675   2214   3451   2027       C  
-ATOM  12751  O   GLU B 986      16.324  29.513 -25.167  1.00 85.27           O  
-ANISOU12751  O   GLU B 986    14052   8543   9803   2159   3674   2000       O  
-ATOM  12752  CB  GLU B 986      16.453  27.044 -27.417  1.00 92.89           C  
-ANISOU12752  CB  GLU B 986    14639   9963  10692   2091   3395   1911       C  
-ATOM  12753  CG  GLU B 986      16.965  28.190 -28.262  1.00107.11           C  
-ANISOU12753  CG  GLU B 986    16700  11587  12410   2067   3717   1954       C  
-ATOM  12754  CD  GLU B 986      17.532  27.722 -29.587  1.00115.89           C  
-ANISOU12754  CD  GLU B 986    17769  12783  13480   1982   3779   1885       C  
-ATOM  12755  OE1 GLU B 986      16.872  26.905 -30.265  1.00120.88           O  
-ANISOU12755  OE1 GLU B 986    18287  13647  13993   2080   3625   1953       O  
-ATOM  12756  OE2 GLU B 986      18.647  28.160 -29.942  1.00121.05           O  
-ANISOU12756  OE2 GLU B 986    18497  13275  14221   1813   3981   1755       O  
-ATOM  12757  N   TYR B 987      14.504  28.203 -25.332  1.00 63.60           N  
-ANISOU12757  N   TYR B 987    11099   6194   6873   2429   3301   2222       N  
-ATOM  12758  CA  TYR B 987      13.582  29.240 -24.884  1.00 63.59           C  
-ANISOU12758  CA  TYR B 987    11302   6119   6740   2625   3394   2426       C  
-ATOM  12759  C   TYR B 987      14.051  29.869 -23.577  1.00 60.13           C  
-ANISOU12759  C   TYR B 987    10911   5480   6455   2537   3453   2317       C  
-ATOM  12760  O   TYR B 987      14.038  31.090 -23.423  1.00 61.14           O  
-ANISOU12760  O   TYR B 987    11278   5408   6546   2578   3681   2380       O  
-ATOM  12761  CB  TYR B 987      12.173  28.667 -24.717  1.00 66.34           C  
-ANISOU12761  CB  TYR B 987    11549   6699   6957   2839   3166   2607       C  
-ATOM  12762  CG  TYR B 987      11.180  29.644 -24.129  1.00 73.64           C  
-ANISOU12762  CG  TYR B 987    12661   7562   7756   3048   3240   2812       C  
-ATOM  12763  CD1 TYR B 987      10.124  30.131 -24.888  1.00 77.37           C  
-ANISOU12763  CD1 TYR B 987    13359   8023   8014   3237   3410   3034       C  
-ATOM  12764  CD2 TYR B 987      11.298  30.079 -22.816  1.00 75.93           C  
-ANISOU12764  CD2 TYR B 987    12902   7809   8138   3062   3142   2785       C  
-ATOM  12765  CE1 TYR B 987       9.214  31.024 -24.355  1.00 79.17           C  
-ANISOU12765  CE1 TYR B 987    13760   8190   8132   3436   3483   3223       C  
-ATOM  12766  CE2 TYR B 987      10.393  30.971 -22.274  1.00 77.81           C  
-ANISOU12766  CE2 TYR B 987    13310   7991   8262   3256   3213   2966       C  
-ATOM  12767  CZ  TYR B 987       9.353  31.441 -23.048  1.00 79.46           C  
-ANISOU12767  CZ  TYR B 987    13744   8181   8268   3443   3385   3184       C  
-ATOM  12768  OH  TYR B 987       8.449  32.330 -22.514  1.00 80.74           O  
-ANISOU12768  OH  TYR B 987    14076   8281   8319   3644   3461   3366       O  
-ATOM  12769  N   PHE B 988      14.465  29.025 -22.637  1.00 70.30           N  
-ANISOU12769  N   PHE B 988    11969   6825   7918   2416   3248   2151       N  
-ATOM  12770  CA  PHE B 988      14.940  29.491 -21.339  1.00 67.85           C  
-ANISOU12770  CA  PHE B 988    11665   6361   7753   2326   3269   2029       C  
-ATOM  12771  C   PHE B 988      16.294  30.184 -21.408  1.00 69.47           C  
-ANISOU12771  C   PHE B 988    11973   6328   8096   2112   3500   1837       C  
-ATOM  12772  O   PHE B 988      16.630  30.992 -20.542  1.00 67.59           O  
-ANISOU12772  O   PHE B 988    11832   5914   7936   2062   3607   1767       O  
-ATOM  12773  CB  PHE B 988      15.004  28.328 -20.342  1.00 61.45           C  
-ANISOU12773  CB  PHE B 988    10564   5699   7087   2257   2979   1911       C  
-ATOM  12774  CG  PHE B 988      13.672  27.960 -19.759  1.00 55.31           C  
-ANISOU12774  CG  PHE B 988     9715   5096   6206   2465   2778   2092       C  
-ATOM  12775  CD1 PHE B 988      13.130  28.698 -18.716  1.00 53.51           C  
-ANISOU12775  CD1 PHE B 988     9586   4798   5948   2571   2799   2167       C  
-ATOM  12776  CD2 PHE B 988      12.958  26.883 -20.256  1.00 51.84           C  
-ANISOU12776  CD2 PHE B 988     9107   4891   5700   2551   2571   2181       C  
-ATOM  12777  CE1 PHE B 988      11.906  28.375 -18.185  1.00 50.36           C  
-ANISOU12777  CE1 PHE B 988     9120   4564   5452   2762   2621   2336       C  
-ATOM  12778  CE2 PHE B 988      11.732  26.551 -19.724  1.00 47.05           C  
-ANISOU12778  CE2 PHE B 988     8429   4445   5001   2737   2391   2348       C  
-ATOM  12779  CZ  PHE B 988      11.203  27.301 -18.688  1.00 47.10           C  
-ANISOU12779  CZ  PHE B 988     8536   4383   4975   2844   2417   2430       C  
-ATOM  12780  N   ILE B 989      17.070  29.872 -22.438  1.00 76.30           N  
-ANISOU12780  N   ILE B 989    12811   7190   8990   1983   3577   1745       N  
-ATOM  12781  CA  ILE B 989      18.418  30.409 -22.541  1.00 80.32           C  
-ANISOU12781  CA  ILE B 989    13387   7488   9643   1762   3784   1547       C  
-ATOM  12782  C   ILE B 989      18.433  31.874 -22.956  1.00 87.12           C  
-ANISOU12782  C   ILE B 989    14564   8121  10417   1810   4105   1649       C  
-ATOM  12783  O   ILE B 989      19.162  32.677 -22.377  1.00 86.31           O  
-ANISOU12783  O   ILE B 989    14559   7803  10432   1686   4267   1524       O  
-ATOM  12784  CB  ILE B 989      19.279  29.588 -23.513  1.00 77.80           C  
-ANISOU12784  CB  ILE B 989    12930   7241   9388   1604   3770   1410       C  
-ATOM  12785  CG1 ILE B 989      19.454  28.163 -22.987  1.00 73.91           C  
-ANISOU12785  CG1 ILE B 989    12118   6936   9028   1525   3469   1274       C  
-ATOM  12786  CG2 ILE B 989      20.635  30.241 -23.703  1.00 76.02           C  
-ANISOU12786  CG2 ILE B 989    12794   6795   9297   1384   4010   1223       C  
-ATOM  12787  CD1 ILE B 989      20.275  27.281 -23.894  1.00 73.69           C  
-ANISOU12787  CD1 ILE B 989    11938   6986   9074   1376   3438   1130       C  
-ATOM  12788  N   ARG B 990      17.625  32.221 -23.951  1.00 80.20           N  
-ANISOU12788  N   ARG B 990    13845   7293   9336   1991   4197   1875       N  
-ATOM  12789  CA  ARG B 990      17.609  33.590 -24.456  1.00 90.95           C  
-ANISOU12789  CA  ARG B 990    15511   8439  10607   2052   4511   1997       C  
-ATOM  12790  C   ARG B 990      16.374  34.395 -24.048  1.00 91.57           C  
-ANISOU12790  C   ARG B 990    15769   8489  10535   2301   4548   2233       C  
-ATOM  12791  O   ARG B 990      16.482  35.577 -23.733  1.00 93.22           O  
-ANISOU12791  O   ARG B 990    16195   8464  10759   2314   4771   2262       O  
-ATOM  12792  CB  ARG B 990      17.796  33.618 -25.979  1.00103.27           C  
-ANISOU12792  CB  ARG B 990    17159  10031  12048   2058   4659   2077       C  
-ATOM  12793  CG  ARG B 990      16.785  32.803 -26.774  1.00118.76           C  
-ANISOU12793  CG  ARG B 990    19031  12272  13819   2240   4483   2250       C  
-ATOM  12794  CD  ARG B 990      17.082  32.885 -28.266  1.00136.11           C  
-ANISOU12794  CD  ARG B 990    21318  14498  15900   2231   4646   2308       C  
-ATOM  12795  NE  ARG B 990      16.227  32.008 -29.062  1.00149.35           N  
-ANISOU12795  NE  ARG B 990    22882  16460  17405   2378   4467   2436       N  
-ATOM  12796  CZ  ARG B 990      15.086  32.388 -29.630  1.00158.45           C  
-ANISOU12796  CZ  ARG B 990    24168  17712  18325   2624   4496   2699       C  
-ATOM  12797  NH1 ARG B 990      14.655  33.634 -29.491  1.00163.49           N  
-ANISOU12797  NH1 ARG B 990    25063  18178  18876   2758   4701   2872       N  
-ATOM  12798  NH2 ARG B 990      14.376  31.521 -30.340  1.00163.31           N  
-ANISOU12798  NH2 ARG B 990    24656  18600  18795   2737   4321   2785       N  
-ATOM  12799  N   ASP B 991      15.206  33.761 -24.046  1.00 99.42           N  
-ANISOU12799  N   ASP B 991    16669   9715  11390   2498   4333   2398       N  
-ATOM  12800  CA  ASP B 991      13.966  34.477 -23.758  1.00100.65           C  
-ANISOU12800  CA  ASP B 991    16987   9869  11387   2753   4362   2639       C  
-ATOM  12801  C   ASP B 991      13.781  34.802 -22.275  1.00 97.57           C  
-ANISOU12801  C   ASP B 991    16583   9395  11096   2762   4296   2580       C  
-ATOM  12802  O   ASP B 991      13.539  35.951 -21.910  1.00 99.72           O  
-ANISOU12802  O   ASP B 991    17073   9476  11339   2845   4483   2659       O  
-ATOM  12803  CB  ASP B 991      12.758  33.702 -24.284  1.00105.58           C  
-ANISOU12803  CB  ASP B 991    17510  10781  11823   2961   4157   2835       C  
-ATOM  12804  CG  ASP B 991      12.693  33.682 -25.799  1.00112.22           C  
-ANISOU12804  CG  ASP B 991    18430  11699  12508   3016   4266   2951       C  
-ATOM  12805  OD1 ASP B 991      13.759  33.588 -26.448  1.00118.32           O  
-ANISOU12805  OD1 ASP B 991    19196  12399  13363   2830   4380   2807       O  
-ATOM  12806  OD2 ASP B 991      11.572  33.763 -26.343  1.00113.80           O  
-ANISOU12806  OD2 ASP B 991    18696  12044  12500   3247   4237   3187       O  
-ATOM  12807  N   VAL B 992      13.892  33.787 -21.425  1.00 83.07           N  
-ANISOU12807  N   VAL B 992    14489   7701   9374   2679   4034   2442       N  
-ATOM  12808  CA  VAL B 992      13.655  33.955 -19.996  1.00 77.30           C  
-ANISOU12808  CA  VAL B 992    13712   6936   8721   2698   3938   2390       C  
-ATOM  12809  C   VAL B 992      14.899  34.421 -19.255  1.00 76.67           C  
-ANISOU12809  C   VAL B 992    13645   6639   8847   2465   4056   2137       C  
-ATOM  12810  O   VAL B 992      14.831  35.325 -18.432  1.00 76.79           O  
-ANISOU12810  O   VAL B 992    13792   6493   8891   2490   4166   2123       O  
-ATOM  12811  CB  VAL B 992      13.145  32.654 -19.364  1.00 72.71           C  
-ANISOU12811  CB  VAL B 992    12845   6617   8164   2729   3598   2376       C  
-ATOM  12812  CG1 VAL B 992      13.234  32.727 -17.853  1.00 71.11           C  
-ANISOU12812  CG1 VAL B 992    12563   6376   8080   2687   3501   2264       C  
-ATOM  12813  CG2 VAL B 992      11.719  32.384 -19.809  1.00 67.85           C  
-ANISOU12813  CG2 VAL B 992    12235   6203   7341   2988   3483   2639       C  
-ATOM  12814  N   LYS B 993      16.031  33.793 -19.546  1.00 92.89           N  
-ANISOU12814  N   LYS B 993    15554   8695  11044   2239   4032   1930       N  
-ATOM  12815  CA  LYS B 993      17.300  34.172 -18.935  1.00 90.87           C  
-ANISOU12815  CA  LYS B 993    15290   8249  10987   2000   4143   1674       C  
-ATOM  12816  C   LYS B 993      17.297  33.940 -17.427  1.00 85.29           C  
-ANISOU12816  C   LYS B 993    14439   7580  10388   1967   3970   1554       C  
-ATOM  12817  O   LYS B 993      17.885  34.715 -16.673  1.00 84.54           O  
-ANISOU12817  O   LYS B 993    14423   7300  10397   1862   4099   1414       O  
-ATOM  12818  CB  LYS B 993      17.628  35.639 -19.233  1.00 98.83           C  
-ANISOU12818  CB  LYS B 993    16598   8968  11985   1984   4486   1695       C  
-ATOM  12819  CG  LYS B 993      17.420  36.058 -20.683  1.00107.75           C  
-ANISOU12819  CG  LYS B 993    17913  10055  12971   2069   4680   1870       C  
-ATOM  12820  CD  LYS B 993      18.074  37.406 -20.970  1.00118.42           C  
-ANISOU12820  CD  LYS B 993    19530  11097  14369   1988   5030   1838       C  
-ATOM  12821  CE  LYS B 993      19.594  37.286 -20.977  1.00124.26           C  
-ANISOU12821  CE  LYS B 993    20183  11718  15313   1687   5114   1555       C  
-ATOM  12822  NZ  LYS B 993      20.271  38.578 -21.272  1.00130.22           N  
-ANISOU12822  NZ  LYS B 993    21187  12165  16127   1591   5461   1515       N  
-ATOM  12823  N   SER B 994      16.631  32.875 -16.993  1.00 74.05           N  
-ANISOU12823  N   SER B 994    12801   6399   8937   2055   3682   1609       N  
-ATOM  12824  CA  SER B 994      16.574  32.536 -15.576  1.00 66.63           C  
-ANISOU12824  CA  SER B 994    11702   5529   8086   2035   3497   1514       C  
-ATOM  12825  C   SER B 994      17.627  31.500 -15.237  1.00 61.59           C  
-ANISOU12825  C   SER B 994    10795   4973   7632   1816   3336   1280       C  
-ATOM  12826  O   SER B 994      18.100  30.792 -16.122  1.00 62.39           O  
-ANISOU12826  O   SER B 994    10798   5139   7769   1727   3304   1234       O  
-ATOM  12827  CB  SER B 994      15.200  31.976 -15.227  1.00 64.70           C  
-ANISOU12827  CB  SER B 994    11374   5502   7708   2264   3276   1722       C  
-ATOM  12828  OG  SER B 994      14.933  30.807 -15.981  1.00 61.05           O  
-ANISOU12828  OG  SER B 994    10739   5246   7213   2288   3098   1785       O  
-ATOM  12829  N   LEU B 995      17.995  31.409 -13.961  1.00 57.93           N  
-ANISOU12829  N   LEU B 995    10211   4514   7286   1735   3235   1131       N  
-ATOM  12830  CA  LEU B 995      18.862  30.329 -13.517  1.00 50.71           C  
-ANISOU12830  CA  LEU B 995     9017   3711   6539   1558   3046    934       C  
-ATOM  12831  C   LEU B 995      18.127  29.042 -13.812  1.00 45.69           C  
-ANISOU12831  C   LEU B 995     8183   3324   5853   1666   2789   1063       C  
-ATOM  12832  O   LEU B 995      16.919  28.962 -13.615  1.00 43.98           O  
-ANISOU12832  O   LEU B 995     7987   3221   5503   1871   2687   1265       O  
-ATOM  12833  CB  LEU B 995      19.150  30.432 -12.027  1.00 48.90           C  
-ANISOU12833  CB  LEU B 995     8688   3483   6407   1499   2957    795       C  
-ATOM  12834  CG  LEU B 995      19.726  31.758 -11.534  1.00 50.82           C  
-ANISOU12834  CG  LEU B 995     9126   3489   6696   1410   3197    665       C  
-ATOM  12835  CD1 LEU B 995      20.168  31.613 -10.091  1.00 50.26           C  
-ANISOU12835  CD1 LEU B 995     8896   3464   6735   1322   3070    490       C  
-ATOM  12836  CD2 LEU B 995      20.887  32.207 -12.406  1.00 51.46           C  
-ANISOU12836  CD2 LEU B 995     9300   3384   6870   1214   3425    513       C  
-ATOM  12837  N   THR B 996      18.846  28.041 -14.302  1.00 52.27           N  
-ANISOU12837  N   THR B 996     8825   4240   6796   1528   2689    946       N  
-ATOM  12838  CA  THR B 996      18.202  26.823 -14.763  1.00 48.34           C  
-ANISOU12838  CA  THR B 996     8149   3960   6258   1616   2469   1059       C  
-ATOM  12839  C   THR B 996      19.104  25.607 -14.666  1.00 46.77           C  
-ANISOU12839  C   THR B 996     7671   3858   6240   1444   2299    877       C  
-ATOM  12840  O   THR B 996      20.260  25.649 -15.075  1.00 47.99           O  
-ANISOU12840  O   THR B 996     7810   3913   6510   1257   2408    694       O  
-ATOM  12841  CB  THR B 996      17.764  26.954 -16.229  1.00 48.23           C  
-ANISOU12841  CB  THR B 996     8274   3947   6103   1702   2584   1201       C  
-ATOM  12842  OG1 THR B 996      16.689  27.895 -16.333  1.00 48.85           O  
-ANISOU12842  OG1 THR B 996     8583   3983   5995   1907   2696   1416       O  
-ATOM  12843  CG2 THR B 996      17.310  25.612 -16.766  1.00 44.97           C  
-ANISOU12843  CG2 THR B 996     7652   3756   5680   1749   2359   1264       C  
-ATOM  12844  N   LEU B 997      18.565  24.521 -14.126  1.00 48.01           N  
-ANISOU12844  N   LEU B 997     7606   4210   6426   1511   2035    932       N  
-ATOM  12845  CA  LEU B 997      19.235  23.236 -14.194  1.00 45.24           C  
-ANISOU12845  CA  LEU B 997     6985   3970   6235   1383   1859    800       C  
-ATOM  12846  C   LEU B 997      18.430  22.358 -15.132  1.00 44.49           C  
-ANISOU12846  C   LEU B 997     6816   4029   6060   1493   1738    945       C  
-ATOM  12847  O   LEU B 997      17.279  22.029 -14.844  1.00 42.64           O  
-ANISOU12847  O   LEU B 997     6543   3928   5729   1665   1594   1124       O  
-ATOM  12848  CB  LEU B 997      19.313  22.587 -12.817  1.00 43.49           C  
-ANISOU12848  CB  LEU B 997     6543   3851   6129   1363   1644    742       C  
-ATOM  12849  CG  LEU B 997      19.904  23.448 -11.704  1.00 44.84           C  
-ANISOU12849  CG  LEU B 997     6775   3907   6355   1285   1732    616       C  
-ATOM  12850  CD1 LEU B 997      19.861  22.692 -10.386  1.00 43.89           C  
-ANISOU12850  CD1 LEU B 997     6421   3928   6328   1289   1497    587       C  
-ATOM  12851  CD2 LEU B 997      21.320  23.857 -12.046  1.00 44.21           C  
-ANISOU12851  CD2 LEU B 997     6729   3669   6400   1064   1907    384       C  
-ATOM  12852  N   PHE B 998      19.032  21.994 -16.261  1.00 44.14           N  
-ANISOU12852  N   PHE B 998     6751   3970   6051   1393   1801    862       N  
-ATOM  12853  CA  PHE B 998      18.369  21.152 -17.246  1.00 44.43           C  
-ANISOU12853  CA  PHE B 998     6713   4154   6016   1479   1697    970       C  
-ATOM  12854  C   PHE B 998      18.989  19.762 -17.215  1.00 43.29           C  
-ANISOU12854  C   PHE B 998     6277   4114   6057   1355   1504    827       C  
-ATOM  12855  O   PHE B 998      20.134  19.581 -17.622  1.00 45.04           O  
-ANISOU12855  O   PHE B 998     6444   4265   6403   1180   1576    640       O  
-ATOM  12856  CB  PHE B 998      18.494  21.768 -18.648  1.00 45.45           C  
-ANISOU12856  CB  PHE B 998     7041   4204   6024   1477   1917    997       C  
-ATOM  12857  CG  PHE B 998      17.447  21.290 -19.618  1.00 45.98           C  
-ANISOU12857  CG  PHE B 998     7109   4424   5936   1631   1844   1170       C  
-ATOM  12858  CD1 PHE B 998      17.688  20.204 -20.445  1.00 46.09           C  
-ANISOU12858  CD1 PHE B 998     6954   4551   6008   1568   1742   1097       C  
-ATOM  12859  CD2 PHE B 998      16.216  21.923 -19.694  1.00 47.33           C  
-ANISOU12859  CD2 PHE B 998     7445   4632   5905   1841   1877   1398       C  
-ATOM  12860  CE1 PHE B 998      16.719  19.756 -21.327  1.00 47.40           C  
-ANISOU12860  CE1 PHE B 998     7111   4869   6029   1705   1671   1243       C  
-ATOM  12861  CE2 PHE B 998      15.246  21.481 -20.573  1.00 47.15           C  
-ANISOU12861  CE2 PHE B 998     7413   4766   5735   1983   1805   1552       C  
-ATOM  12862  CZ  PHE B 998      15.498  20.396 -21.390  1.00 48.07           C  
-ANISOU12862  CZ  PHE B 998     7357   4999   5908   1912   1700   1470       C  
-ATOM  12863  N   VAL B 999      18.248  18.777 -16.721  1.00 42.48           N  
-ANISOU12863  N   VAL B 999     5984   4176   5982   1445   1263    915       N  
-ATOM  12864  CA  VAL B 999      18.758  17.411 -16.736  1.00 41.96           C  
-ANISOU12864  CA  VAL B 999     5640   4206   6096   1342   1078    796       C  
-ATOM  12865  C   VAL B 999      18.216  16.702 -17.964  1.00 42.78           C  
-ANISOU12865  C   VAL B 999     5702   4421   6132   1399   1027    862       C  
-ATOM  12866  O   VAL B 999      17.034  16.820 -18.279  1.00 42.49           O  
-ANISOU12866  O   VAL B 999     5744   4472   5927   1569    997   1053       O  
-ATOM  12867  CB  VAL B 999      18.372  16.625 -15.475  1.00 40.95           C  
-ANISOU12867  CB  VAL B 999     5300   4191   6068   1387    839    838       C  
-ATOM  12868  CG1 VAL B 999      19.149  15.311 -15.418  1.00 39.09           C  
-ANISOU12868  CG1 VAL B 999     4785   4016   6052   1254    679    687       C  
-ATOM  12869  CG2 VAL B 999      18.646  17.452 -14.235  1.00 40.43           C  
-ANISOU12869  CG2 VAL B 999     5303   4042   6017   1372    889    809       C  
-ATOM  12870  N   THR B1000      19.079  15.965 -18.654  1.00 41.52           N  
-ANISOU12870  N   THR B1000     5413   4263   6099   1258   1017    699       N  
-ATOM  12871  CA  THR B1000      18.728  15.425 -19.962  1.00 43.69           C  
-ANISOU12871  CA  THR B1000     5672   4627   6301   1290   1009    726       C  
-ATOM  12872  C   THR B1000      19.525  14.179 -20.333  1.00 44.64           C  
-ANISOU12872  C   THR B1000     5550   4794   6616   1149    897    548       C  
-ATOM  12873  O   THR B1000      20.667  14.009 -19.909  1.00 46.30           O  
-ANISOU12873  O   THR B1000     5663   4924   7005    992    911    368       O  
-ATOM  12874  CB  THR B1000      18.941  16.489 -21.068  1.00 43.78           C  
-ANISOU12874  CB  THR B1000     5941   4540   6152   1285   1271    734       C  
-ATOM  12875  OG1 THR B1000      18.429  16.006 -22.315  1.00 44.09           O  
-ANISOU12875  OG1 THR B1000     5973   4695   6084   1346   1255    787       O  
-ATOM  12876  CG2 THR B1000      20.417  16.819 -21.229  1.00 43.14           C  
-ANISOU12876  CG2 THR B1000     5881   4309   6202   1082   1431    517       C  
-ATOM  12877  N   HIS B1001      18.909  13.310 -21.129  1.00 55.40           N  
-ANISOU12877  N   HIS B1001     6813   6291   7946   1208    787    594       N  
-ATOM  12878  CA  HIS B1001      19.597  12.151 -21.683  1.00 55.25           C  
-ANISOU12878  CA  HIS B1001     6581   6315   8095   1085    700    425       C  
-ATOM  12879  C   HIS B1001      19.767  12.278 -23.198  1.00 55.73           C  
-ANISOU12879  C   HIS B1001     6742   6389   8044   1060    841    375       C  
-ATOM  12880  O   HIS B1001      20.046  11.297 -23.889  1.00 54.99           O  
-ANISOU12880  O   HIS B1001     6488   6363   8041    995    766    264       O  
-ATOM  12881  CB  HIS B1001      18.831  10.871 -21.355  1.00 56.93           C  
-ANISOU12881  CB  HIS B1001     6559   6675   8396   1154    442    487       C  
-ATOM  12882  CG  HIS B1001      18.754  10.574 -19.892  1.00 57.40           C  
-ANISOU12882  CG  HIS B1001     6487   6735   8586   1167    290    525       C  
-ATOM  12883  ND1 HIS B1001      19.871  10.310 -19.131  1.00 59.57           N  
-ANISOU12883  ND1 HIS B1001     6634   6933   9068   1027    266    368       N  
-ATOM  12884  CD2 HIS B1001      17.698  10.501 -19.051  1.00 57.80           C  
-ANISOU12884  CD2 HIS B1001     6509   6866   8585   1307    156    705       C  
-ATOM  12885  CE1 HIS B1001      19.505  10.086 -17.881  1.00 60.52           C  
-ANISOU12885  CE1 HIS B1001     6654   7089   9252   1082    122    452       C  
-ATOM  12886  NE2 HIS B1001      18.190  10.195 -17.806  1.00 58.13           N  
-ANISOU12886  NE2 HIS B1001     6411   6879   8797   1250     56    657       N  
-ATOM  12887  N   TYR B1002      19.592  13.493 -23.708  1.00 53.58           N  
-ANISOU12887  N   TYR B1002     6732   6051   7574   1115   1049    460       N  
-ATOM  12888  CA  TYR B1002      19.690  13.754 -25.141  1.00 53.88           C  
-ANISOU12888  CA  TYR B1002     6891   6108   7473   1109   1202    441       C  
-ATOM  12889  C   TYR B1002      20.970  14.514 -25.479  1.00 52.46           C  
-ANISOU12889  C   TYR B1002     6832   5765   7334    954   1434    289       C  
-ATOM  12890  O   TYR B1002      21.032  15.736 -25.310  1.00 54.09           O  
-ANISOU12890  O   TYR B1002     7262   5851   7438    976   1617    357       O  
-ATOM  12891  CB  TYR B1002      18.494  14.581 -25.617  1.00 55.26           C  
-ANISOU12891  CB  TYR B1002     7283   6340   7374   1301   1281    670       C  
-ATOM  12892  CG  TYR B1002      17.137  13.954 -25.389  1.00 55.10           C  
-ANISOU12892  CG  TYR B1002     7165   6489   7281   1466   1073    835       C  
-ATOM  12893  CD1 TYR B1002      16.935  12.592 -25.562  1.00 55.61           C  
-ANISOU12893  CD1 TYR B1002     6981   6688   7459   1445    865    771       C  
-ATOM  12894  CD2 TYR B1002      16.054  14.734 -25.015  1.00 54.54           C  
-ANISOU12894  CD2 TYR B1002     7250   6441   7030   1643   1091   1055       C  
-ATOM  12895  CE1 TYR B1002      15.689  12.028 -25.364  1.00 55.50           C  
-ANISOU12895  CE1 TYR B1002     6875   6827   7384   1589    681    920       C  
-ATOM  12896  CE2 TYR B1002      14.810  14.179 -24.813  1.00 54.20           C  
-ANISOU12896  CE2 TYR B1002     7116   6558   6919   1793    906   1207       C  
-ATOM  12897  CZ  TYR B1002      14.630  12.827 -24.987  1.00 54.32           C  
-ANISOU12897  CZ  TYR B1002     6882   6707   7052   1762    701   1139       C  
-ATOM  12898  OH  TYR B1002      13.383  12.277 -24.784  1.00 54.15           O  
-ANISOU12898  OH  TYR B1002     6764   6843   6969   1905    521   1288       O  
-ATOM  12899  N   PRO B1003      21.991  13.797 -25.971  1.00 40.08           N  
-ANISOU12899  N   PRO B1003     5117   4190   5920    796   1432     83       N  
-ATOM  12900  CA  PRO B1003      23.268  14.419 -26.348  1.00 39.30           C  
-ANISOU12900  CA  PRO B1003     5109   3947   5876    635   1649    -77       C  
-ATOM  12901  C   PRO B1003      23.130  15.638 -27.286  1.00 39.68           C  
-ANISOU12901  C   PRO B1003     5445   3934   5699    685   1907     19       C  
-ATOM  12902  O   PRO B1003      23.906  16.585 -27.161  1.00 40.53           O  
-ANISOU12902  O   PRO B1003     5696   3881   5821    593   2107    -38       O  
-ATOM  12903  CB  PRO B1003      24.014  13.278 -27.036  1.00 40.01           C  
-ANISOU12903  CB  PRO B1003     4989   4100   6114    510   1580   -272       C  
-ATOM  12904  CG  PRO B1003      23.460  12.046 -26.395  1.00 37.77           C  
-ANISOU12904  CG  PRO B1003     4460   3934   5958    559   1302   -257       C  
-ATOM  12905  CD  PRO B1003      22.018  12.332 -26.131  1.00 37.80           C  
-ANISOU12905  CD  PRO B1003     4557   4023   5782    758   1223    -17       C  
-ATOM  12906  N   PRO B1004      22.162  15.615 -28.215  1.00 39.14           N  
-ANISOU12906  N   PRO B1004     5455   3992   5425    827   1907    164       N  
-ATOM  12907  CA  PRO B1004      21.898  16.785 -29.055  1.00 40.62           C  
-ANISOU12907  CA  PRO B1004     5919   4132   5381    904   2143    291       C  
-ATOM  12908  C   PRO B1004      21.596  18.056 -28.279  1.00 42.87           C  
-ANISOU12908  C   PRO B1004     6422   4278   5589    976   2268    431       C  
-ATOM  12909  O   PRO B1004      21.815  19.144 -28.801  1.00 44.55           O  
-ANISOU12909  O   PRO B1004     6865   4381   5681    979   2509    483       O  
-ATOM  12910  CB  PRO B1004      20.654  16.365 -29.833  1.00 40.61           C  
-ANISOU12910  CB  PRO B1004     5915   4331   5185   1080   2041    449       C  
-ATOM  12911  CG  PRO B1004      20.819  14.918 -30.002  1.00 39.73           C  
-ANISOU12911  CG  PRO B1004     5526   4348   5223   1011   1833    304       C  
-ATOM  12912  CD  PRO B1004      21.449  14.428 -28.714  1.00 38.50           C  
-ANISOU12912  CD  PRO B1004     5194   4106   5329    899   1704    181       C  
-ATOM  12913  N   VAL B1005      21.078  17.931 -27.063  1.00 45.55           N  
-ANISOU12913  N   VAL B1005     6693   4621   5993   1038   2113    495       N  
-ATOM  12914  CA  VAL B1005      20.730  19.110 -26.284  1.00 49.30           C  
-ANISOU12914  CA  VAL B1005     7367   4970   6393   1116   2221    623       C  
-ATOM  12915  C   VAL B1005      21.993  19.818 -25.809  1.00 52.64           C  
-ANISOU12915  C   VAL B1005     7857   5187   6958    938   2394    462       C  
-ATOM  12916  O   VAL B1005      22.033  21.041 -25.715  1.00 54.93           O  
-ANISOU12916  O   VAL B1005     8377   5331   7164    960   2598    530       O  
-ATOM  12917  CB  VAL B1005      19.828  18.758 -25.092  1.00 48.64           C  
-ANISOU12917  CB  VAL B1005     7183   4960   6337   1232   2004    731       C  
-ATOM  12918  CG1 VAL B1005      19.705  19.942 -24.141  1.00 49.90           C  
-ANISOU12918  CG1 VAL B1005     7525   4971   6464   1276   2119    811       C  
-ATOM  12919  CG2 VAL B1005      18.456  18.321 -25.583  1.00 46.27           C  
-ANISOU12919  CG2 VAL B1005     6867   4850   5865   1427   1873    923       C  
-ATOM  12920  N   CYS B1006      23.034  19.044 -25.535  1.00 57.80           N  
-ANISOU12920  N   CYS B1006     8304   5829   7829    761   2316    244       N  
-ATOM  12921  CA  CYS B1006      24.295  19.612 -25.083  1.00 61.69           C  
-ANISOU12921  CA  CYS B1006     8826   6144   8469    578   2464     67       C  
-ATOM  12922  C   CYS B1006      24.853  20.615 -26.083  1.00 66.06           C  
-ANISOU12922  C   CYS B1006     9604   6568   8926    517   2760     53       C  
-ATOM  12923  O   CYS B1006      25.595  21.518 -25.698  1.00 67.32           O  
-ANISOU12923  O   CYS B1006     9881   6552   9147    412   2938    -24       O  
-ATOM  12924  CB  CYS B1006      25.324  18.512 -24.834  1.00 61.26           C  
-ANISOU12924  CB  CYS B1006     8499   6123   8654    405   2331   -163       C  
-ATOM  12925  SG  CYS B1006      24.788  17.228 -23.696  1.00 57.62           S  
-ANISOU12925  SG  CYS B1006     7752   5809   8331    462   1987   -153       S  
-ATOM  12926  N   GLU B1007      24.504  20.455 -27.359  1.00 71.02           N  
-ANISOU12926  N   GLU B1007    10289   7289   9407    582   2816    125       N  
-ATOM  12927  CA  GLU B1007      25.014  21.339 -28.407  1.00 76.27           C  
-ANISOU12927  CA  GLU B1007    11160   7849   9969    531   3098    124       C  
-ATOM  12928  C   GLU B1007      24.882  22.801 -27.999  1.00 76.88           C  
-ANISOU12928  C   GLU B1007    11505   7740   9965    575   3312    237       C  
-ATOM  12929  O   GLU B1007      25.742  23.623 -28.307  1.00 78.75           O  
-ANISOU12929  O   GLU B1007    11879   7812  10230    455   3553    161       O  
-ATOM  12930  CB  GLU B1007      24.275  21.123 -29.733  1.00 81.08           C  
-ANISOU12930  CB  GLU B1007    11830   8609  10366    662   3117    258       C  
-ATOM  12931  CG  GLU B1007      24.056  19.675 -30.141  1.00 87.31           C  
-ANISOU12931  CG  GLU B1007    12368   9607  11199    668   2883    188       C  
-ATOM  12932  CD  GLU B1007      25.343  18.913 -30.381  1.00 92.00           C  
-ANISOU12932  CD  GLU B1007    12773  10188  11996    458   2873    -73       C  
-ATOM  12933  OE1 GLU B1007      25.270  17.787 -30.920  1.00 93.54           O  
-ANISOU12933  OE1 GLU B1007    12781  10539  12222    451   2722   -146       O  
-ATOM  12934  OE2 GLU B1007      26.424  19.431 -30.030  1.00 95.82           O  
-ANISOU12934  OE2 GLU B1007    13290  10507  12611    298   3016   -210       O  
-ATOM  12935  N   LEU B1008      23.797  23.114 -27.299  1.00 69.78           N  
-ANISOU12935  N   LEU B1008    10676   6864   8973    746   3225    416       N  
-ATOM  12936  CA  LEU B1008      23.488  24.485 -26.907  1.00 70.65           C  
-ANISOU12936  CA  LEU B1008    11046   6806   8992    819   3416    544       C  
-ATOM  12937  C   LEU B1008      24.626  25.213 -26.194  1.00 71.43           C  
-ANISOU12937  C   LEU B1008    11194   6686   9260    634   3572    373       C  
-ATOM  12938  O   LEU B1008      24.624  26.438 -26.123  1.00 72.78           O  
-ANISOU12938  O   LEU B1008    11600   6683   9369    654   3792    445       O  
-ATOM  12939  CB  LEU B1008      22.218  24.526 -26.051  1.00 68.28           C  
-ANISOU12939  CB  LEU B1008    10759   6580   8605   1016   3255    727       C  
-ATOM  12940  CG  LEU B1008      20.928  24.263 -26.834  1.00 68.52           C  
-ANISOU12940  CG  LEU B1008    10831   6791   8413   1234   3177    950       C  
-ATOM  12941  CD1 LEU B1008      19.730  24.116 -25.909  1.00 67.29           C  
-ANISOU12941  CD1 LEU B1008    10638   6728   8200   1412   2986   1107       C  
-ATOM  12942  CD2 LEU B1008      20.690  25.362 -27.864  1.00 67.67           C  
-ANISOU12942  CD2 LEU B1008    11004   6602   8105   1323   3445   1104       C  
-ATOM  12943  N   GLU B1009      25.598  24.474 -25.671  1.00 69.98           N  
-ANISOU12943  N   GLU B1009    10788   6510   9291    453   3462    145       N  
-ATOM  12944  CA  GLU B1009      26.725  25.109 -24.995  1.00 72.60           C  
-ANISOU12944  CA  GLU B1009    11143   6651   9789    266   3600    -37       C  
-ATOM  12945  C   GLU B1009      27.585  25.926 -25.959  1.00 76.86           C  
-ANISOU12945  C   GLU B1009    11855   7036  10313    144   3903    -98       C  
-ATOM  12946  O   GLU B1009      28.030  27.027 -25.634  1.00 78.72           O  
-ANISOU12946  O   GLU B1009    12259   7071  10580     73   4112   -129       O  
-ATOM  12947  CB  GLU B1009      27.589  24.076 -24.279  1.00 71.05           C  
-ANISOU12947  CB  GLU B1009    10656   6518   9822    106   3409   -265       C  
-ATOM  12948  CG  GLU B1009      28.747  24.698 -23.526  1.00 73.16           C  
-ANISOU12948  CG  GLU B1009    10927   6610  10259    -87   3534   -463       C  
-ATOM  12949  CD  GLU B1009      29.516  23.686 -22.698  1.00 73.52           C  
-ANISOU12949  CD  GLU B1009    10678   6734  10522   -222   3327   -670       C  
-ATOM  12950  OE1 GLU B1009      29.667  22.530 -23.159  1.00 73.71           O  
-ANISOU12950  OE1 GLU B1009    10503   6902  10602   -244   3175   -727       O  
-ATOM  12951  OE2 GLU B1009      29.958  24.048 -21.581  1.00 73.01           O  
-ANISOU12951  OE2 GLU B1009    10580   6591  10571   -302   3317   -774       O  
-ATOM  12952  N   LYS B1010      27.810  25.380 -27.148  1.00 70.94           N  
-ANISOU12952  N   LYS B1010    11059   6380   9516    119   3929   -116       N  
-ATOM  12953  CA  LYS B1010      28.630  26.041 -28.159  1.00 75.31           C  
-ANISOU12953  CA  LYS B1010    11756   6810  10047      5   4210   -170       C  
-ATOM  12954  C   LYS B1010      27.970  27.308 -28.702  1.00 79.01           C  
-ANISOU12954  C   LYS B1010    12542   7165  10315    141   4450     54       C  
-ATOM  12955  O   LYS B1010      28.651  28.274 -29.040  1.00 81.44           O  
-ANISOU12955  O   LYS B1010    13021   7284  10637     41   4722     21       O  
-ATOM  12956  CB  LYS B1010      28.961  25.067 -29.290  1.00 73.44           C  
-ANISOU12956  CB  LYS B1010    11378   6728   9797    -41   4159   -241       C  
-ATOM  12957  CG  LYS B1010      29.939  23.981 -28.874  1.00 71.51           C  
-ANISOU12957  CG  LYS B1010    10842   6544   9783   -219   3995   -496       C  
-ATOM  12958  CD  LYS B1010      29.946  22.813 -29.844  1.00 69.70           C  
-ANISOU12958  CD  LYS B1010    10443   6506   9532   -214   3874   -543       C  
-ATOM  12959  CE  LYS B1010      30.959  21.758 -29.412  1.00 67.63           C  
-ANISOU12959  CE  LYS B1010     9893   6289   9514   -390   3721   -798       C  
-ATOM  12960  NZ  LYS B1010      30.931  20.539 -30.274  1.00 66.00           N  
-ANISOU12960  NZ  LYS B1010     9504   6268   9304   -381   3584   -855       N  
-ATOM  12961  N   ASN B1011      26.643  27.303 -28.767  1.00 93.64           N  
-ANISOU12961  N   ASN B1011    14468   9127  11984    372   4351    284       N  
-ATOM  12962  CA  ASN B1011      25.889  28.468 -29.218  1.00 97.00           C  
-ANISOU12962  CA  ASN B1011    15187   9458  12210    533   4557    520       C  
-ATOM  12963  C   ASN B1011      25.858  29.579 -28.168  1.00 97.94           C  
-ANISOU12963  C   ASN B1011    15466   9363  12384    533   4675    543       C  
-ATOM  12964  O   ASN B1011      25.779  30.759 -28.504  1.00 99.62           O  
-ANISOU12964  O   ASN B1011    15937   9405  12510    575   4933    659       O  
-ATOM  12965  CB  ASN B1011      24.458  28.075 -29.597  1.00100.10           C  
-ANISOU12965  CB  ASN B1011    15591  10053  12389    784   4401    755       C  
-ATOM  12966  CG  ASN B1011      24.408  26.974 -30.638  1.00102.91           C  
-ANISOU12966  CG  ASN B1011    15788  10631  12681    792   4279    729       C  
-ATOM  12967  OD1 ASN B1011      25.413  26.321 -30.920  1.00105.77           O  
-ANISOU12967  OD1 ASN B1011    15992  11014  13183    611   4262    521       O  
-ATOM  12968  ND2 ASN B1011      23.230  26.757 -31.210  1.00104.61           N  
-ANISOU12968  ND2 ASN B1011    16041  11019  12687   1003   4192    935       N  
-ATOM  12969  N   TYR B1012      25.912  29.199 -26.894  1.00 82.77           N  
-ANISOU12969  N   TYR B1012    13391   7452  10607    490   4487    433       N  
-ATOM  12970  CA  TYR B1012      25.912  30.177 -25.812  1.00 84.12           C  
-ANISOU12970  CA  TYR B1012    13687   7435  10838    481   4577    427       C  
-ATOM  12971  C   TYR B1012      27.004  29.855 -24.799  1.00 86.40           C  
-ANISOU12971  C   TYR B1012    13789   7667  11371    263   4501    154       C  
-ATOM  12972  O   TYR B1012      26.725  29.664 -23.622  1.00 86.26           O  
-ANISOU12972  O   TYR B1012    13674   7681  11420    290   4332    121       O  
-ATOM  12973  CB  TYR B1012      24.557  30.198 -25.106  1.00 77.83           C  
-ANISOU12973  CB  TYR B1012    12921   6728   9923    710   4414    622       C  
-ATOM  12974  CG  TYR B1012      23.368  30.296 -26.034  1.00 72.92           C  
-ANISOU12974  CG  TYR B1012    12432   6217   9056    944   4428    892       C  
-ATOM  12975  CD1 TYR B1012      22.915  29.184 -26.727  1.00 69.16           C  
-ANISOU12975  CD1 TYR B1012    11797   5980   8500   1016   4239    941       C  
-ATOM  12976  CD2 TYR B1012      22.689  31.496 -26.208  1.00 71.63           C  
-ANISOU12976  CD2 TYR B1012    12549   5924   8744   1097   4629   1097       C  
-ATOM  12977  CE1 TYR B1012      21.827  29.260 -27.572  1.00 65.81           C  
-ANISOU12977  CE1 TYR B1012    11483   5677   7846   1230   4244   1180       C  
-ATOM  12978  CE2 TYR B1012      21.595  31.581 -27.054  1.00 67.76           C  
-ANISOU12978  CE2 TYR B1012    12172   5550   8022   1320   4637   1350       C  
-ATOM  12979  CZ  TYR B1012      21.170  30.456 -27.733  1.00 65.59           C  
-ANISOU12979  CZ  TYR B1012    11728   5528   7665   1384   4440   1387       C  
-ATOM  12980  OH  TYR B1012      20.085  30.517 -28.576  1.00 62.34           O  
-ANISOU12980  OH  TYR B1012    11416   5252   7018   1603   4439   1629       O  
-ATOM  12981  N   SER B1013      28.248  29.806 -25.257  1.00 91.76           N  
-ANISOU12981  N   SER B1013    14416   8271  12178     50   4628    -40       N  
-ATOM  12982  CA  SER B1013      29.368  29.402 -24.410  1.00 93.17           C  
-ANISOU12982  CA  SER B1013    14392   8420  12589   -166   4550   -312       C  
-ATOM  12983  C   SER B1013      29.363  30.056 -23.029  1.00 94.82           C  
-ANISOU12983  C   SER B1013    14635   8509  12882   -186   4542   -369       C  
-ATOM  12984  O   SER B1013      29.743  29.429 -22.041  1.00 93.58           O  
-ANISOU12984  O   SER B1013    14264   8423  12868   -269   4351   -524       O  
-ATOM  12985  CB  SER B1013      30.698  29.682 -25.117  1.00 95.80           C  
-ANISOU12985  CB  SER B1013    14741   8629  13031   -389   4772   -491       C  
-ATOM  12986  OG  SER B1013      31.793  29.314 -24.296  1.00 96.54           O  
-ANISOU12986  OG  SER B1013    14633   8699  13347   -596   4699   -756       O  
-ATOM  12987  N   HIS B1014      28.922  31.308 -22.965  1.00100.18           N  
-ANISOU12987  N   HIS B1014    14151  11066  12846  -1315   4614  -2253       N  
-ATOM  12988  CA  HIS B1014      29.023  32.095 -21.736  1.00102.28           C  
-ANISOU12988  CA  HIS B1014    14335  11357  13171  -1194   4448  -2276       C  
-ATOM  12989  C   HIS B1014      27.850  31.933 -20.769  1.00 98.13           C  
-ANISOU12989  C   HIS B1014    13812  11038  12435   -984   4151  -2078       C  
-ATOM  12990  O   HIS B1014      27.985  32.210 -19.578  1.00 98.16           O  
-ANISOU12990  O   HIS B1014    13673  11099  12523   -866   3966  -2108       O  
-ATOM  12991  CB  HIS B1014      29.220  33.577 -22.068  1.00107.12           C  
-ANISOU12991  CB  HIS B1014    15136  11830  13733  -1263   4620  -2313       C  
-ATOM  12992  CG  HIS B1014      30.596  33.910 -22.550  1.00114.23           C  
-ANISOU12992  CG  HIS B1014    15963  12526  14914  -1448   4870  -2554       C  
-ATOM  12993  ND1 HIS B1014      31.585  34.377 -21.711  1.00117.15           N  
-ANISOU12993  ND1 HIS B1014    16139  12819  15554  -1448   4846  -2746       N  
-ATOM  12994  CD2 HIS B1014      31.151  33.838 -23.783  1.00117.72           C  
-ANISOU12994  CD2 HIS B1014    16493  12828  15407  -1642   5153  -2643       C  
-ATOM  12995  CE1 HIS B1014      32.689  34.582 -22.408  1.00119.95           C  
-ANISOU12995  CE1 HIS B1014    16464  12992  16119  -1637   5105  -2946       C  
-ATOM  12996  NE2 HIS B1014      32.453  34.262 -23.667  1.00120.01           N  
-ANISOU12996  NE2 HIS B1014    16642  12959  15998  -1760   5297  -2886       N  
-ATOM  12997  N   GLN B1015      26.703  31.500 -21.278  1.00 99.63           N  
-ANISOU12997  N   GLN B1015    14161  11346  12349   -939   4109  -1884       N  
-ATOM  12998  CA  GLN B1015      25.523  31.315 -20.439  1.00 93.28           C  
-ANISOU12998  CA  GLN B1015    13370  10745  11329   -751   3841  -1695       C  
-ATOM  12999  C   GLN B1015      25.353  29.862 -20.010  1.00 86.93           C  
-ANISOU12999  C   GLN B1015    12374  10068  10589   -689   3674  -1656       C  
-ATOM  13000  O   GLN B1015      24.854  29.580 -18.922  1.00 84.83           O  
-ANISOU13000  O   GLN B1015    12003   9951  10279   -537   3427  -1571       O  
-ATOM  13001  CB  GLN B1015      24.260  31.788 -21.166  1.00 97.52           C  
-ANISOU13001  CB  GLN B1015    14200  11348  11506   -720   3873  -1501       C  
-ATOM  13002  CG  GLN B1015      24.179  33.287 -21.381  1.00103.53           C  
-ANISOU13002  CG  GLN B1015    15168  12011  12156   -734   3978  -1496       C  
-ATOM  13003  CD  GLN B1015      25.280  33.807 -22.279  1.00109.61           C  
-ANISOU13003  CD  GLN B1015    15993  12557  13098   -926   4272  -1660       C  
-ATOM  13004  OE1 GLN B1015      25.370  33.433 -23.448  1.00112.39           O  
-ANISOU13004  OE1 GLN B1015    16450  12842  13410  -1054   4466  -1665       O  
-ATOM  13005  NE2 GLN B1015      26.130  34.671 -21.735  1.00112.52           N  
-ANISOU13005  NE2 GLN B1015    16286  12809  13658   -950   4310  -1803       N  
-ATOM  13006  N   VAL B1016      25.772  28.944 -20.874  1.00 73.68           N  
-ANISOU13006  N   VAL B1016    10652   8328   9014   -811   3813  -1719       N  
-ATOM  13007  CA  VAL B1016      25.527  27.527 -20.658  1.00 66.50           C  
-ANISOU13007  CA  VAL B1016     9593   7526   8148   -766   3680  -1669       C  
-ATOM  13008  C   VAL B1016      26.807  26.734 -20.409  1.00 64.58           C  
-ANISOU13008  C   VAL B1016     9084   7189   8265   -832   3699  -1866       C  
-ATOM  13009  O   VAL B1016      27.856  27.025 -20.980  1.00 65.89           O  
-ANISOU13009  O   VAL B1016     9218   7190   8627   -974   3904  -2048       O  
-ATOM  13010  CB  VAL B1016      24.783  26.918 -21.859  1.00 62.81           C  
-ANISOU13010  CB  VAL B1016     9285   7094   7485   -833   3794  -1563       C  
-ATOM  13011  CG1 VAL B1016      24.444  25.462 -21.590  1.00 62.32           C  
-ANISOU13011  CG1 VAL B1016     9072   7147   7460   -780   3646  -1502       C  
-ATOM  13012  CG2 VAL B1016      23.525  27.714 -22.156  1.00 61.23           C  
-ANISOU13012  CG2 VAL B1016     9352   6985   6927   -764   3775  -1379       C  
-ATOM  13013  N   GLY B1017      26.712  25.731 -19.545  1.00 65.50           N  
-ANISOU13013  N   GLY B1017     9010   7411   8465   -727   3484  -1830       N  
-ATOM  13014  CA  GLY B1017      27.816  24.821 -19.307  1.00 64.39           C  
-ANISOU13014  CA  GLY B1017     8617   7196   8652   -770   3476  -1999       C  
-ATOM  13015  C   GLY B1017      27.315  23.397 -19.209  1.00 61.89           C  
-ANISOU13015  C   GLY B1017     8209   6984   8321   -717   3341  -1898       C  
-ATOM  13016  O   GLY B1017      26.172  23.163 -18.824  1.00 60.18           O  
-ANISOU13016  O   GLY B1017     8068   6925   7873   -602   3179  -1700       O  
-ATOM  13017  N   ASN B1018      28.163  22.442 -19.568  1.00 63.10           N  
-ANISOU13017  N   ASN B1018     8200   7049   8727   -804   3411  -2038       N  
-ATOM  13018  CA  ASN B1018      27.791  21.035 -19.482  1.00 61.24           C  
-ANISOU13018  CA  ASN B1018     7863   6890   8514   -762   3290  -1958       C  
-ATOM  13019  C   ASN B1018      28.392  20.361 -18.260  1.00 60.34           C  
-ANISOU13019  C   ASN B1018     7495   6798   8635   -654   3073  -2016       C  
-ATOM  13020  O   ASN B1018      29.533  20.630 -17.892  1.00 60.11           O  
-ANISOU13020  O   ASN B1018     7313   6664   8863   -677   3095  -2207       O  
-ATOM  13021  CB  ASN B1018      28.179  20.285 -20.756  1.00 61.48           C  
-ANISOU13021  CB  ASN B1018     7893   6823   8645   -921   3499  -2054       C  
-ATOM  13022  CG  ASN B1018      27.048  20.223 -21.760  1.00 61.11           C  
-ANISOU13022  CG  ASN B1018     8073   6847   8298   -961   3596  -1897       C  
-ATOM  13023  OD1 ASN B1018      25.880  20.124 -21.389  1.00 60.17           O  
-ANISOU13023  OD1 ASN B1018     8047   6879   7935   -848   3445  -1697       O  
-ATOM  13024  ND2 ASN B1018      27.390  20.274 -23.040  1.00 64.42           N  
-ANISOU13024  ND2 ASN B1018     8578   7164   8734  -1123   3848  -1992       N  
-ATOM  13025  N   TYR B1019      27.612  19.492 -17.626  1.00 62.03           N  
-ANISOU13025  N   TYR B1019     7667   7147   8755   -534   2864  -1852       N  
-ATOM  13026  CA  TYR B1019      28.061  18.818 -16.416  1.00 62.29           C  
-ANISOU13026  CA  TYR B1019     7478   7214   8977   -416   2638  -1875       C  
-ATOM  13027  C   TYR B1019      27.545  17.394 -16.315  1.00 63.60           C  
-ANISOU13027  C   TYR B1019     7576   7451   9140   -370   2514  -1756       C  
-ATOM  13028  O   TYR B1019      26.632  16.996 -17.036  1.00 62.81           O  
-ANISOU13028  O   TYR B1019     7610   7408   8846   -407   2571  -1627       O  
-ATOM  13029  CB  TYR B1019      27.628  19.601 -15.182  1.00 60.20           C  
-ANISOU13029  CB  TYR B1019     7224   7069   8580   -261   2439  -1777       C  
-ATOM  13030  CG  TYR B1019      28.220  20.983 -15.104  1.00 59.00           C  
-ANISOU13030  CG  TYR B1019     7108   6842   8467   -291   2536  -1907       C  
-ATOM  13031  CD1 TYR B1019      27.550  22.074 -15.633  1.00 58.25           C  
-ANISOU13031  CD1 TYR B1019     7240   6765   8128   -325   2651  -1832       C  
-ATOM  13032  CD2 TYR B1019      29.451  21.199 -14.504  1.00 59.48           C  
-ANISOU13032  CD2 TYR B1019     6976   6811   8813   -284   2512  -2109       C  
-ATOM  13033  CE1 TYR B1019      28.087  23.344 -15.566  1.00 57.75           C  
-ANISOU13033  CE1 TYR B1019     7215   6623   8106   -356   2744  -1949       C  
-ATOM  13034  CE2 TYR B1019      29.996  22.464 -14.432  1.00 59.64           C  
-ANISOU13034  CE2 TYR B1019     7025   6758   8878   -317   2607  -2236       C  
-ATOM  13035  CZ  TYR B1019      29.308  23.532 -14.965  1.00 58.72           C  
-ANISOU13035  CZ  TYR B1019     7139   6654   8518   -355   2725  -2151       C  
-ATOM  13036  OH  TYR B1019      29.844  24.793 -14.900  1.00 59.13           O  
-ANISOU13036  OH  TYR B1019     7225   6623   8620   -391   2823  -2275       O  
-ATOM  13037  N   HIS B1020      28.138  16.634 -15.402  1.00 53.41           N  
-ANISOU13037  N   HIS B1020     6075   6154   8066   -286   2340  -1804       N  
-ATOM  13038  CA  HIS B1020      27.739  15.257 -15.163  1.00 56.83           C  
-ANISOU13038  CA  HIS B1020     6426   6640   8525   -233   2204  -1695       C  
-ATOM  13039  C   HIS B1020      28.196  14.837 -13.769  1.00 59.61           C  
-ANISOU13039  C   HIS B1020     6587   7028   9034    -87   1955  -1698       C  
-ATOM  13040  O   HIS B1020      29.178  15.360 -13.249  1.00 60.63           O  
-ANISOU13040  O   HIS B1020     6594   7090   9351    -64   1932  -1859       O  
-ATOM  13041  CB  HIS B1020      28.371  14.340 -16.204  1.00 55.48           C  
-ANISOU13041  CB  HIS B1020     6181   6336   8563   -368   2365  -1830       C  
-ATOM  13042  CG  HIS B1020      29.838  14.140 -16.007  1.00 55.56           C  
-ANISOU13042  CG  HIS B1020     5976   6201   8933   -399   2384  -2072       C  
-ATOM  13043  ND1 HIS B1020      30.769  15.098 -16.343  1.00 54.81           N  
-ANISOU13043  ND1 HIS B1020     5865   5995   8965   -486   2545  -2274       N  
-ATOM  13044  CD2 HIS B1020      30.535  13.101 -15.490  1.00 55.53           C  
-ANISOU13044  CD2 HIS B1020     5764   6145   9191   -349   2258  -2149       C  
-ATOM  13045  CE1 HIS B1020      31.978  14.655 -16.050  1.00 55.83           C  
-ANISOU13045  CE1 HIS B1020     5777   6015   9421   -492   2519  -2475       C  
-ATOM  13046  NE2 HIS B1020      31.864  13.445 -15.531  1.00 56.53           N  
-ANISOU13046  NE2 HIS B1020     5746   6137   9597   -405   2341  -2403       N  
-ATOM  13047  N   MET B1021      27.479  13.898 -13.161  1.00 72.43           N  
-ANISOU13047  N   MET B1021     8185   8757  10578     13   1768  -1522       N  
-ATOM  13048  CA  MET B1021      27.888  13.360 -11.871  1.00 76.06           C  
-ANISOU13048  CA  MET B1021     8469   9249  11182    153   1528  -1510       C  
-ATOM  13049  C   MET B1021      29.056  12.404 -12.056  1.00 81.13           C  
-ANISOU13049  C   MET B1021     8914   9739  12174    111   1547  -1690       C  
-ATOM  13050  O   MET B1021      28.872  11.255 -12.459  1.00 80.22           O  
-ANISOU13050  O   MET B1021     8769   9594  12118     79   1548  -1643       O  
-ATOM  13051  CB  MET B1021      26.726  12.646 -11.181  1.00 74.11           C  
-ANISOU13051  CB  MET B1021     8269   9160  10729    265   1333  -1257       C  
-ATOM  13052  CG  MET B1021      25.634  13.575 -10.683  1.00 72.70           C  
-ANISOU13052  CG  MET B1021     8247   9153  10224    342   1258  -1088       C  
-ATOM  13053  SD  MET B1021      26.241  14.847  -9.553  1.00 74.92           S  
-ANISOU13053  SD  MET B1021     8461   9469  10537    449   1146  -1178       S  
-ATOM  13054  CE  MET B1021      26.907  13.847  -8.221  1.00 77.21           C  
-ANISOU13054  CE  MET B1021     8521   9769  11047    592    885  -1182       C  
-ATOM  13055  N   GLY B1022      30.258  12.884 -11.764  1.00 81.98           N  
-ANISOU13055  N   GLY B1022     8882   9749  12518    111   1562  -1903       N  
-ATOM  13056  CA  GLY B1022      31.451  12.075 -11.917  1.00 89.74           C  
-ANISOU13056  CA  GLY B1022     9666  10585  13848     74   1579  -2103       C  
-ATOM  13057  C   GLY B1022      31.711  11.168 -10.729  1.00 97.45           C  
-ANISOU13057  C   GLY B1022    10475  11592  14959    230   1313  -2055       C  
-ATOM  13058  O   GLY B1022      32.547  11.478  -9.881  1.00100.22           O  
-ANISOU13058  O   GLY B1022    10683  11924  15473    317   1199  -2178       O  
-ATOM  13059  N   PHE B1023      31.000  10.045 -10.666  1.00105.25           N  
-ANISOU13059  N   PHE B1023    11484  12626  15882    268   1215  -1879       N  
-ATOM  13060  CA  PHE B1023      31.183   9.092  -9.574  1.00110.23           C  
-ANISOU13060  CA  PHE B1023    11974  13279  16629    414    964  -1810       C  
-ATOM  13061  C   PHE B1023      32.154   7.973  -9.947  1.00116.34           C  
-ANISOU13061  C   PHE B1023    12575  13892  17736    374    981  -1972       C  
-ATOM  13062  O   PHE B1023      32.465   7.776 -11.121  1.00119.27           O  
-ANISOU13062  O   PHE B1023    12951  14153  18213    225   1190  -2100       O  
-ATOM  13063  CB  PHE B1023      29.842   8.499  -9.140  1.00111.05           C  
-ANISOU13063  CB  PHE B1023    12195  13528  16471    490    826  -1516       C  
-ATOM  13064  CG  PHE B1023      29.250   7.540 -10.132  1.00110.54           C  
-ANISOU13064  CG  PHE B1023    12200  13426  16376    387    938  -1438       C  
-ATOM  13065  CD1 PHE B1023      29.667   6.219 -10.174  1.00110.07           C  
-ANISOU13065  CD1 PHE B1023    12014  13268  16541    393    878  -1465       C  
-ATOM  13066  CD2 PHE B1023      28.265   7.954 -11.013  1.00110.01           C  
-ANISOU13066  CD2 PHE B1023    12322  13423  16053    290   1097  -1341       C  
-ATOM  13067  CE1 PHE B1023      29.123   5.332 -11.084  1.00108.49           C  
-ANISOU13067  CE1 PHE B1023    11870  13033  16319    297    982  -1403       C  
-ATOM  13068  CE2 PHE B1023      27.715   7.071 -11.923  1.00109.69           C  
-ANISOU13068  CE2 PHE B1023    12338  13355  15983    198   1198  -1280       C  
-ATOM  13069  CZ  PHE B1023      28.145   5.759 -11.960  1.00108.96           C  
-ANISOU13069  CZ  PHE B1023    12113  13165  16123    199   1143  -1313       C  
-ATOM  13070  N   LEU B1024      32.624   7.238  -8.942  1.00 94.69           N  
-ANISOU13070  N   LEU B1024     9682  11140  15157    511    758  -1965       N  
-ATOM  13071  CA  LEU B1024      33.567   6.145  -9.165  1.00101.60           C  
-ANISOU13071  CA  LEU B1024    10380  11863  16361    497    742  -2118       C  
-ATOM  13072  C   LEU B1024      33.048   4.833  -8.586  1.00105.22           C  
-ANISOU13072  C   LEU B1024    10817  12347  16814    599    545  -1921       C  
-ATOM  13073  O   LEU B1024      32.447   4.812  -7.510  1.00102.00           O  
-ANISOU13073  O   LEU B1024    10448  12066  16242    738    342  -1725       O  
-ATOM  13074  CB  LEU B1024      34.931   6.479  -8.555  1.00 96.64           C  
-ANISOU13074  CB  LEU B1024     9553  11156  16008    564    667  -2361       C  
-ATOM  13075  CG  LEU B1024      35.598   7.788  -8.987  1.00 96.80           C  
-ANISOU13075  CG  LEU B1024     9568  11138  16072    472    848  -2580       C  
-ATOM  13076  CD1 LEU B1024      36.923   7.979  -8.261  1.00 94.84           C  
-ANISOU13076  CD1 LEU B1024     9104  10822  16109    557    743  -2818       C  
-ATOM  13077  CD2 LEU B1024      35.793   7.830 -10.497  1.00 95.40           C  
-ANISOU13077  CD2 LEU B1024     9439  10847  15960    265   1141  -2720       C  
-ATOM  13078  N   VAL B1025      33.283   3.739  -9.306  1.00147.80           N  
-ANISOU13078  N   VAL B1025    16150  17620  22389    526    609  -1975       N  
-ATOM  13079  CA  VAL B1025      32.875   2.415  -8.850  1.00153.76           C  
-ANISOU13079  CA  VAL B1025    16877  18369  23176    609    439  -1806       C  
-ATOM  13080  C   VAL B1025      33.931   1.813  -7.928  1.00156.13           C  
-ANISOU13080  C   VAL B1025    16977  18586  23760    747    233  -1910       C  
-ATOM  13081  O   VAL B1025      35.121   2.097  -8.066  1.00154.47           O  
-ANISOU13081  O   VAL B1025    16619  18271  23801    730    278  -2172       O  
-ATOM  13082  CB  VAL B1025      32.626   1.455 -10.035  1.00159.58           C  
-ANISOU13082  CB  VAL B1025    17635  19010  23988    473    595  -1818       C  
-ATOM  13083  CG1 VAL B1025      31.411   1.900 -10.837  1.00164.78           C  
-ANISOU13083  CG1 VAL B1025    18502  19772  24335    363    762  -1673       C  
-ATOM  13084  CG2 VAL B1025      33.858   1.373 -10.924  1.00166.41           C  
-ANISOU13084  CG2 VAL B1025    18357  19705  25168    362    758  -2128       C  
-ATOM  13085  N   SER B1026      33.493   0.985  -6.985  1.00121.70           N  
-ANISOU13085  N   SER B1026    12613  14272  19354    884      6  -1707       N  
-ATOM  13086  CA  SER B1026      34.412   0.346  -6.050  1.00128.27           C  
-ANISOU13086  CA  SER B1026    13271  15031  20434   1033   -213  -1777       C  
-ATOM  13087  C   SER B1026      35.122  -0.838  -6.700  1.00129.83           C  
-ANISOU13087  C   SER B1026    13337  15041  20950    982   -176  -1920       C  
-ATOM  13088  O   SER B1026      35.385  -1.851  -6.053  1.00140.10           O  
-ANISOU13088  O   SER B1026    14550  16282  22398   1098   -368  -1864       O  
-ATOM  13089  CB  SER B1026      33.674  -0.097  -4.796  1.00136.44           C  
-ANISOU13089  CB  SER B1026    14363  16185  21294   1197   -467  -1499       C  
-ATOM  13090  N   PHE B1043      32.447  -2.525  -3.284  1.00167.02           N  
-ANISOU13090  N   PHE B1043    18298  20088  25073   1416   -874   -987       N  
-ATOM  13091  CA  PHE B1043      31.175  -2.944  -2.709  1.00171.09           C  
-ANISOU13091  CA  PHE B1043    18962  20730  25313   1462   -976   -667       C  
-ATOM  13092  C   PHE B1043      30.027  -2.048  -3.167  1.00164.37           C  
-ANISOU13092  C   PHE B1043    18288  20037  24127   1360   -822   -554       C  
-ATOM  13093  O   PHE B1043      28.943  -2.534  -3.492  1.00160.42           O  
-ANISOU13093  O   PHE B1043    17913  19587  23452   1297   -770   -365       O  
-ATOM  13094  CB  PHE B1043      31.260  -2.966  -1.187  1.00169.37           C  
-ANISOU13094  CB  PHE B1043    18716  20604  25031   1661  -1251   -534       C  
-ATOM  13095  N   VAL B1044      30.268  -0.740  -3.191  1.00148.46           N  
-ANISOU13095  N   VAL B1044    16281  18099  22028   1346   -750   -676       N  
-ATOM  13096  CA  VAL B1044      29.247   0.221  -3.601  1.00141.18           C  
-ANISOU13096  CA  VAL B1044    15525  17324  20793   1261   -611   -585       C  
-ATOM  13097  C   VAL B1044      29.789   1.249  -4.597  1.00138.82           C  
-ANISOU13097  C   VAL B1044    15216  16976  20554   1135   -386   -825       C  
-ATOM  13098  O   VAL B1044      30.640   0.933  -5.431  1.00133.98           O  
-ANISOU13098  O   VAL B1044    14504  16201  20201   1048   -262  -1033       O  
-ATOM  13099  CB  VAL B1044      28.637   0.953  -2.383  1.00142.86           C  
-ANISOU13099  CB  VAL B1044    15809  17737  20735   1390   -778   -415       C  
-ATOM  13100  CG1 VAL B1044      27.767   0.006  -1.573  1.00148.56           C  
-ANISOU13100  CG1 VAL B1044    16593  18536  21316   1477   -954   -136       C  
-ATOM  13101  CG2 VAL B1044      29.734   1.551  -1.515  1.00150.50           C  
-ANISOU13101  CG2 VAL B1044    16637  18699  21849   1515   -914   -571       C  
-ATOM  13102  N   THR B1045      29.281   2.475  -4.509  1.00129.38           N  
-ANISOU13102  N   THR B1045    14126  15918  19115   1124   -332   -793       N  
-ATOM  13103  CA  THR B1045      29.721   3.567  -5.373  1.00130.53           C  
-ANISOU13103  CA  THR B1045    14285  16027  19285   1010   -121   -998       C  
-ATOM  13104  C   THR B1045      29.924   4.847  -4.564  1.00132.19           C  
-ANISOU13104  C   THR B1045    14492  16345  19389   1097   -194  -1040       C  
-ATOM  13105  O   THR B1045      29.242   5.072  -3.565  1.00131.36           O  
-ANISOU13105  O   THR B1045    14444  16395  19070   1211   -358   -856       O  
-ATOM  13106  CB  THR B1045      28.714   3.828  -6.503  1.00128.92           C  
-ANISOU13106  CB  THR B1045    14255  15865  18863    862     92   -922       C  
-ATOM  13107  OG1 THR B1045      27.398   3.948  -5.951  1.00135.52           O  
-ANISOU13107  OG1 THR B1045    15238  16882  19372    918      0   -661       O  
-ATOM  13108  CG2 THR B1045      28.729   2.682  -7.501  1.00136.15           C  
-ANISOU13108  CG2 THR B1045    15151  16651  19930    753    206   -951       C  
-ATOM  13109  N   PHE B1046      30.857   5.687  -5.000  1.00134.45           N  
-ANISOU13109  N   PHE B1046    14708  16551  19827   1037    -67  -1286       N  
-ATOM  13110  CA  PHE B1046      31.243   6.854  -4.214  1.00129.68           C  
-ANISOU13110  CA  PHE B1046    14068  16025  19180   1122   -139  -1365       C  
-ATOM  13111  C   PHE B1046      31.568   8.088  -5.053  1.00125.88           C  
-ANISOU13111  C   PHE B1046    13631  15504  18692    997     88  -1548       C  
-ATOM  13112  O   PHE B1046      31.269   8.143  -6.247  1.00122.93           O  
-ANISOU13112  O   PHE B1046    13355  15074  18278    845    305  -1573       O  
-ATOM  13113  CB  PHE B1046      32.442   6.511  -3.327  1.00131.96           C  
-ANISOU13113  CB  PHE B1046    14149  16246  19745   1249   -318  -1511       C  
-ATOM  13114  CG  PHE B1046      33.654   6.057  -4.094  1.00130.65           C  
-ANISOU13114  CG  PHE B1046    13833  15879  19929   1166   -203  -1775       C  
-ATOM  13115  CD1 PHE B1046      34.688   6.937  -4.366  1.00131.29           C  
-ANISOU13115  CD1 PHE B1046    13815  15884  20185   1117    -91  -2048       C  
-ATOM  13116  CD2 PHE B1046      33.757   4.751  -4.547  1.00130.13           C  
-ANISOU13116  CD2 PHE B1046    13721  15701  20023   1133   -203  -1756       C  
-ATOM  13117  CE1 PHE B1046      35.802   6.524  -5.071  1.00130.23           C  
-ANISOU13117  CE1 PHE B1046    13537  15572  20373   1035     19  -2302       C  
-ATOM  13118  CE2 PHE B1046      34.869   4.333  -5.253  1.00128.20           C  
-ANISOU13118  CE2 PHE B1046    13332  15277  20103   1057    -99  -2009       C  
-ATOM  13119  CZ  PHE B1046      35.893   5.221  -5.514  1.00128.93           C  
-ANISOU13119  CZ  PHE B1046    13324  15302  20363   1007     13  -2283       C  
-ATOM  13120  N   LEU B1047      32.181   9.074  -4.403  1.00134.29           N  
-ANISOU13120  N   LEU B1047    14625  16601  19798   1064     35  -1676       N  
-ATOM  13121  CA  LEU B1047      32.592  10.321  -5.044  1.00126.85           C  
-ANISOU13121  CA  LEU B1047    13714  15616  18868    958    235  -1860       C  
-ATOM  13122  C   LEU B1047      31.512  10.898  -5.954  1.00119.70           C  
-ANISOU13122  C   LEU B1047    13029  14766  17687    838    421  -1737       C  
-ATOM  13123  O   LEU B1047      31.767  11.200  -7.117  1.00116.84           O  
-ANISOU13123  O   LEU B1047    12714  14299  17382    684    656  -1865       O  
-ATOM  13124  CB  LEU B1047      33.895  10.124  -5.828  1.00125.90           C  
-ANISOU13124  CB  LEU B1047    13449  15299  19089    853    386  -2150       C  
-ATOM  13125  CG  LEU B1047      34.594  11.396  -6.321  1.00128.36           C  
-ANISOU13125  CG  LEU B1047    13751  15546  19474    756    575  -2381       C  
-ATOM  13126  CD1 LEU B1047      35.006  12.262  -5.142  1.00129.77           C  
-ANISOU13126  CD1 LEU B1047    13842  15805  19658    891    419  -2445       C  
-ATOM  13127  CD2 LEU B1047      35.795  11.064  -7.193  1.00131.13           C  
-ANISOU13127  CD2 LEU B1047    13965  15706  20154    634    741  -2658       C  
-ATOM  13128  N   TYR B1048      30.304  11.049  -5.427  1.00114.24           N  
-ANISOU13128  N   TYR B1048    12472  14243  16690    910    314  -1492       N  
-ATOM  13129  CA  TYR B1048      29.230  11.654  -6.201  1.00106.35           C  
-ANISOU13129  CA  TYR B1048    11683  13314  15413    816    468  -1373       C  
-ATOM  13130  C   TYR B1048      29.450  13.150  -6.318  1.00102.95           C  
-ANISOU13130  C   TYR B1048    11306  12892  14918    783    577  -1492       C  
-ATOM  13131  O   TYR B1048      28.688  13.936  -5.759  1.00103.11           O  
-ANISOU13131  O   TYR B1048    11427  13058  14694    852    503  -1369       O  
-ATOM  13132  CB  TYR B1048      27.875  11.404  -5.545  1.00102.59           C  
-ANISOU13132  CB  TYR B1048    11325  13023  14631    909    314  -1089       C  
-ATOM  13133  CG  TYR B1048      27.396   9.981  -5.634  1.00100.49           C  
-ANISOU13133  CG  TYR B1048    11055  12751  14374    912    249   -941       C  
-ATOM  13134  CD1 TYR B1048      28.039   9.060  -6.445  1.00100.56           C  
-ANISOU13134  CD1 TYR B1048    10984  12596  14627    821    352  -1054       C  
-ATOM  13135  CD2 TYR B1048      26.290   9.561  -4.913  1.00 98.39           C  
-ANISOU13135  CD2 TYR B1048    10865  12643  13875   1002     89   -692       C  
-ATOM  13136  CE1 TYR B1048      27.599   7.757  -6.528  1.00 96.71           C  
-ANISOU13136  CE1 TYR B1048    10492  12096  14158    823    294   -922       C  
-ATOM  13137  CE2 TYR B1048      25.840   8.266  -4.991  1.00 94.25           C  
-ANISOU13137  CE2 TYR B1048    10340  12107  13362    999     37   -556       C  
-ATOM  13138  CZ  TYR B1048      26.498   7.365  -5.797  1.00 94.80           C  
-ANISOU13138  CZ  TYR B1048    10331  12006  13683    911    137   -671       C  
-ATOM  13139  OH  TYR B1048      26.048   6.066  -5.872  1.00 92.42           O  
-ANISOU13139  OH  TYR B1048    10027  11685  13402    908     85   -538       O  
-ATOM  13140  N   GLN B1049      30.489  13.548  -7.041  1.00 85.55           N  
-ANISOU13140  N   GLN B1049     9036  10533  12936    675    755  -1734       N  
-ATOM  13141  CA  GLN B1049      30.781  14.966  -7.189  1.00 81.05           C  
-ANISOU13141  CA  GLN B1049     8515   9950  12330    632    873  -1861       C  
-ATOM  13142  C   GLN B1049      30.434  15.482  -8.580  1.00 75.10           C  
-ANISOU13142  C   GLN B1049     7933   9130  11471    461   1146  -1882       C  
-ATOM  13143  O   GLN B1049      30.814  14.890  -9.591  1.00 75.27           O  
-ANISOU13143  O   GLN B1049     7942   9027  11631    335   1306  -1972       O  
-ATOM  13144  CB  GLN B1049      32.241  15.271  -6.839  1.00 83.98           C  
-ANISOU13144  CB  GLN B1049     8684  10207  13017    644    870  -2133       C  
-ATOM  13145  CG  GLN B1049      33.264  14.537  -7.685  1.00 88.22           C  
-ANISOU13145  CG  GLN B1049     9101  10561  13858    530   1009  -2334       C  
-ATOM  13146  CD  GLN B1049      34.690  14.826  -7.250  1.00 90.43           C  
-ANISOU13146  CD  GLN B1049     9169  10742  14450    555    987  -2610       C  
-ATOM  13147  OE1 GLN B1049      34.919  15.525  -6.259  1.00 89.24           O  
-ANISOU13147  OE1 GLN B1049     8953  10662  14292    667    854  -2647       O  
-ATOM  13148  NE2 GLN B1049      35.658  14.287  -7.989  1.00 91.59           N  
-ANISOU13148  NE2 GLN B1049     9199  10727  14875    450   1118  -2817       N  
-ATOM  13149  N   ILE B1050      29.691  16.584  -8.615  1.00 72.40           N  
-ANISOU13149  N   ILE B1050     7756   8876  10877    460   1191  -1796       N  
-ATOM  13150  CA  ILE B1050      29.329  17.234  -9.867  1.00 65.51           C  
-ANISOU13150  CA  ILE B1050     7066   7948   9877    313   1440  -1808       C  
-ATOM  13151  C   ILE B1050      30.598  17.608 -10.630  1.00 65.16           C  
-ANISOU13151  C   ILE B1050     6943   7714  10100    177   1651  -2079       C  
-ATOM  13152  O   ILE B1050      31.545  18.137 -10.049  1.00 65.73           O  
-ANISOU13152  O   ILE B1050     6880   7737  10359    211   1617  -2252       O  
-ATOM  13153  CB  ILE B1050      28.454  18.479  -9.610  1.00 59.26           C  
-ANISOU13153  CB  ILE B1050     6445   7275   8796    357   1429  -1694       C  
-ATOM  13154  CG1 ILE B1050      27.750  18.919 -10.889  1.00 54.68           C  
-ANISOU13154  CG1 ILE B1050     6087   6670   8018    228   1650  -1634       C  
-ATOM  13155  CG2 ILE B1050      29.274  19.607  -9.009  1.00 57.74           C  
-ANISOU13155  CG2 ILE B1050     6174   7046   8720    391   1420  -1862       C  
-ATOM  13156  CD1 ILE B1050      26.817  17.882 -11.442  1.00 49.72           C  
-ANISOU13156  CD1 ILE B1050     5545   6100   7245    204   1650  -1462       C  
-ATOM  13157  N   THR B1051      30.623  17.312 -11.926  1.00 75.30           N  
-ANISOU13157  N   THR B1051     8307   8899  11405     22   1870  -2122       N  
-ATOM  13158  CA  THR B1051      31.821  17.517 -12.733  1.00 77.45           C  
-ANISOU13158  CA  THR B1051     8501   8991  11936   -122   2084  -2381       C  
-ATOM  13159  C   THR B1051      31.486  18.200 -14.052  1.00 76.61           C  
-ANISOU13159  C   THR B1051     8600   8826  11683   -282   2355  -2386       C  
-ATOM  13160  O   THR B1051      30.470  17.892 -14.674  1.00 76.24           O  
-ANISOU13160  O   THR B1051     8713   8843  11411   -311   2398  -2214       O  
-ATOM  13161  CB  THR B1051      32.511  16.179 -13.048  1.00 78.13           C  
-ANISOU13161  CB  THR B1051     8420   8981  12283   -164   2087  -2483       C  
-ATOM  13162  OG1 THR B1051      32.501  15.346 -11.882  1.00 81.22           O  
-ANISOU13162  OG1 THR B1051     8666   9449  12745     -2   1816  -2406       O  
-ATOM  13163  CG2 THR B1051      33.948  16.405 -13.503  1.00 79.11           C  
-ANISOU13163  CG2 THR B1051     8400   8933  12726   -276   2250  -2787       C  
-ATOM  13164  N   ARG B1052      32.345  19.123 -14.477  1.00 67.39           N  
-ANISOU13164  N   ARG B1052     7426   7536  10642   -385   2537  -2585       N  
-ATOM  13165  CA  ARG B1052      32.149  19.823 -15.745  1.00 68.08           C  
-ANISOU13165  CA  ARG B1052     7710   7551  10606   -544   2807  -2605       C  
-ATOM  13166  C   ARG B1052      32.445  18.916 -16.936  1.00 67.25           C  
-ANISOU13166  C   ARG B1052     7593   7349  10610   -691   2985  -2681       C  
-ATOM  13167  O   ARG B1052      33.329  18.060 -16.876  1.00 68.38           O  
-ANISOU13167  O   ARG B1052     7536   7415  11032   -711   2966  -2833       O  
-ATOM  13168  CB  ARG B1052      33.010  21.088 -15.814  1.00 71.13           C  
-ANISOU13168  CB  ARG B1052     8094   7827  11104   -618   2954  -2798       C  
-ATOM  13169  CG  ARG B1052      32.938  21.803 -17.158  1.00 75.15           C  
-ANISOU13169  CG  ARG B1052     8805   8241  11509   -794   3250  -2833       C  
-ATOM  13170  CD  ARG B1052      33.861  23.010 -17.221  1.00 79.46           C  
-ANISOU13170  CD  ARG B1052     9339   8662  12190   -877   3406  -3035       C  
-ATOM  13171  NE  ARG B1052      33.261  24.202 -16.626  1.00 81.84           N  
-ANISOU13171  NE  ARG B1052     9771   9033  12290   -790   3336  -2928       N  
-ATOM  13172  CZ  ARG B1052      32.291  24.911 -17.196  1.00 83.52           C  
-ANISOU13172  CZ  ARG B1052    10242   9284  12206   -813   3423  -2765       C  
-ATOM  13173  NH1 ARG B1052      31.794  24.539 -18.369  1.00 84.87           N  
-ANISOU13173  NH1 ARG B1052    10570   9437  12240   -919   3582  -2685       N  
-ATOM  13174  NH2 ARG B1052      31.810  25.985 -16.589  1.00 85.30           N  
-ANISOU13174  NH2 ARG B1052    10568   9569  12274   -727   3347  -2685       N  
-ATOM  13175  N   GLY B1053      31.699  19.113 -18.019  1.00 57.56           N  
-ANISOU13175  N   GLY B1053     6579   6130   9161   -788   3155  -2580       N  
-ATOM  13176  CA  GLY B1053      31.835  18.284 -19.198  1.00 55.88           C  
-ANISOU13176  CA  GLY B1053     6376   5845   9011   -925   3327  -2634       C  
-ATOM  13177  C   GLY B1053      30.670  17.325 -19.332  1.00 53.92           C  
-ANISOU13177  C   GLY B1053     6203   5721   8565   -867   3222  -2415       C  
-ATOM  13178  O   GLY B1053      29.980  17.028 -18.361  1.00 52.68           O  
-ANISOU13178  O   GLY B1053     6025   5690   8300   -715   2988  -2250       O  
-ATOM  13179  N   ILE B1054      30.456  16.833 -20.546  1.00 57.58           N  
-ANISOU13179  N   ILE B1054     6748   6147   8981   -992   3399  -2419       N  
-ATOM  13180  CA  ILE B1054      29.369  15.905 -20.815  1.00 56.77           C  
-ANISOU13180  CA  ILE B1054     6717   6153   8699   -956   3328  -2231       C  
-ATOM  13181  C   ILE B1054      29.727  14.504 -20.340  1.00 60.98           C  
-ANISOU13181  C   ILE B1054     7032   6676   9461   -904   3179  -2262       C  
-ATOM  13182  O   ILE B1054      30.898  14.123 -20.326  1.00 60.52           O  
-ANISOU13182  O   ILE B1054     6787   6496   9712   -954   3215  -2468       O  
-ATOM  13183  CB  ILE B1054      29.043  15.869 -22.313  1.00 53.81           C  
-ANISOU13183  CB  ILE B1054     6502   5746   8198  -1109   3574  -2239       C  
-ATOM  13184  CG1 ILE B1054      28.592  17.252 -22.788  1.00 52.53           C  
-ANISOU13184  CG1 ILE B1054     6580   5596   7784  -1149   3712  -2183       C  
-ATOM  13185  CG2 ILE B1054      27.975  14.831 -22.603  1.00 51.70           C  
-ANISOU13185  CG2 ILE B1054     6284   5587   7772  -1075   3502  -2068       C  
-ATOM  13186  CD1 ILE B1054      28.423  17.350 -24.283  1.00 52.91           C  
-ANISOU13186  CD1 ILE B1054     6790   5597   7716  -1305   3973  -2213       C  
-ATOM  13187  N   ALA B1055      28.713  13.741 -19.950  1.00 52.90           N  
-ANISOU13187  N   ALA B1055     6036   5778   8287   -805   3011  -2061       N  
-ATOM  13188  CA  ALA B1055      28.916  12.395 -19.424  1.00 60.22           C  
-ANISOU13188  CA  ALA B1055     6776   6700   9405   -741   2850  -2056       C  
-ATOM  13189  C   ALA B1055      29.700  11.514 -20.383  1.00 67.32           C  
-ANISOU13189  C   ALA B1055     7561   7467  10549   -876   3006  -2236       C  
-ATOM  13190  O   ALA B1055      29.245  11.230 -21.491  1.00 68.59           O  
-ANISOU13190  O   ALA B1055     7828   7629  10604   -981   3165  -2216       O  
-ATOM  13191  CB  ALA B1055      27.582  11.748 -19.093  1.00 59.50           C  
-ANISOU13191  CB  ALA B1055     6768   6761   9080   -645   2694  -1805       C  
-ATOM  13192  N   ALA B1056      30.877  11.080 -19.946  1.00 83.32           N  
-ANISOU13192  N   ALA B1056     9368   9386  12904   -867   2954  -2417       N  
-ATOM  13193  CA  ALA B1056      31.699  10.176 -20.736  1.00 93.43           C  
-ANISOU13193  CA  ALA B1056    10510  10539  14450   -982   3078  -2606       C  
-ATOM  13194  C   ALA B1056      30.865   9.003 -21.239  1.00 95.62           C  
-ANISOU13194  C   ALA B1056    10819  10867  14647   -992   3059  -2476       C  
-ATOM  13195  O   ALA B1056      30.220   8.308 -20.452  1.00 94.25           O  
-ANISOU13195  O   ALA B1056    10618  10776  14418   -867   2848  -2306       O  
-ATOM  13196  CB  ALA B1056      32.876   9.680 -19.914  1.00 92.67           C  
-ANISOU13196  CB  ALA B1056    10160  10349  14700   -919   2945  -2773       C  
-ATOM  13197  N   ARG B1057      30.879   8.791 -22.551  1.00105.24           N  
-ANISOU13197  N   ARG B1057    12094  12035  15856  -1145   3283  -2561       N  
-ATOM  13198  CA  ARG B1057      30.087   7.733 -23.168  1.00105.34           C  
-ANISOU13198  CA  ARG B1057    12142  12094  15789  -1172   3294  -2458       C  
-ATOM  13199  C   ARG B1057      30.202   6.411 -22.414  1.00104.57           C  
-ANISOU13199  C   ARG B1057    11860  11979  15891  -1073   3084  -2426       C  
-ATOM  13200  O   ARG B1057      31.236   6.109 -21.820  1.00103.97           O  
-ANISOU13200  O   ARG B1057    11592  11808  16104  -1036   2998  -2569       O  
-ATOM  13201  CB  ARG B1057      30.492   7.536 -24.629  1.00112.17           C  
-ANISOU13201  CB  ARG B1057    13021  12875  16725  -1356   3562  -2627       C  
-ATOM  13202  CG  ARG B1057      30.003   6.225 -25.216  1.00119.75           C  
-ANISOU13202  CG  ARG B1057    13941  13849  17709  -1388   3564  -2588       C  
-ATOM  13203  CD  ARG B1057      30.570   5.972 -26.602  1.00124.79           C  
-ANISOU13203  CD  ARG B1057    14557  14397  18460  -1569   3822  -2789       C  
-ATOM  13204  NE  ARG B1057      29.629   6.348 -27.651  1.00123.40           N  
-ANISOU13204  NE  ARG B1057    14599  14308  17979  -1649   3988  -2694       N  
-ATOM  13205  CZ  ARG B1057      28.457   5.753 -27.846  1.00120.21           C  
-ANISOU13205  CZ  ARG B1057    14285  14016  17374  -1610   3930  -2516       C  
-ATOM  13206  NH1 ARG B1057      27.662   6.157 -28.825  1.00118.14           N  
-ANISOU13206  NH1 ARG B1057    14219  13832  16836  -1681   4084  -2448       N  
-ATOM  13207  NH2 ARG B1057      28.074   4.759 -27.057  1.00119.01           N  
-ANISOU13207  NH2 ARG B1057    14029  13897  17294  -1499   3718  -2406       N  
-ATOM  13208  N   SER B1058      29.125   5.631 -22.440  1.00 86.22           N  
-ANISOU13208  N   SER B1058     9599   9748  13411  -1030   3001  -2238       N  
-ATOM  13209  CA  SER B1058      29.089   4.335 -21.771  1.00 88.02           C  
-ANISOU13209  CA  SER B1058     9679   9962  13802   -941   2807  -2178       C  
-ATOM  13210  C   SER B1058      29.307   4.461 -20.264  1.00 86.52           C  
-ANISOU13210  C   SER B1058     9403   9797  13672   -775   2556  -2102       C  
-ATOM  13211  O   SER B1058      30.070   3.697 -19.675  1.00 90.64           O  
-ANISOU13211  O   SER B1058     9738  10232  14468   -717   2429  -2183       O  
-ATOM  13212  CB  SER B1058      30.127   3.388 -22.380  1.00 90.63           C  
-ANISOU13212  CB  SER B1058     9821  10139  14476  -1032   2893  -2403       C  
-ATOM  13213  OG  SER B1058      29.831   3.105 -23.737  1.00 92.27           O  
-ANISOU13213  OG  SER B1058    10099  10338  14622  -1177   3107  -2459       O  
-ATOM  13214  N   TYR B1059      28.629   5.422 -19.643  1.00 99.69           N  
-ANISOU13214  N   TYR B1059    11209  11587  15081   -694   2481  -1948       N  
-ATOM  13215  CA  TYR B1059      28.766   5.642 -18.208  1.00 95.10           C  
-ANISOU13215  CA  TYR B1059    10561  11051  14523   -535   2245  -1869       C  
-ATOM  13216  C   TYR B1059      28.019   4.575 -17.421  1.00 92.78           C  
-ANISOU13216  C   TYR B1059    10237  10829  14188   -419   2029  -1668       C  
-ATOM  13217  O   TYR B1059      28.578   3.940 -16.524  1.00 91.35           O  
-ANISOU13217  O   TYR B1059     9900  10599  14209   -321   1850  -1682       O  
-ATOM  13218  CB  TYR B1059      28.253   7.029 -17.817  1.00 92.69           C  
-ANISOU13218  CB  TYR B1059    10411  10856  13950   -489   2238  -1775       C  
-ATOM  13219  CG  TYR B1059      29.112   7.700 -16.773  1.00 90.13           C  
-ANISOU13219  CG  TYR B1059     9979  10505  13760   -397   2119  -1862       C  
-ATOM  13220  CD1 TYR B1059      30.065   8.638 -17.138  1.00 90.14           C  
-ANISOU13220  CD1 TYR B1059     9956  10415  13879   -476   2269  -2070       C  
-ATOM  13221  CD2 TYR B1059      28.987   7.380 -15.428  1.00 89.06           C  
-ANISOU13221  CD2 TYR B1059     9764  10436  13637   -234   1859  -1744       C  
-ATOM  13222  CE1 TYR B1059      30.864   9.249 -16.199  1.00 90.91           C  
-ANISOU13222  CE1 TYR B1059     9945  10488  14108   -394   2164  -2167       C  
-ATOM  13223  CE2 TYR B1059      29.782   7.990 -14.478  1.00 89.76           C  
-ANISOU13223  CE2 TYR B1059     9749  10508  13848   -145   1747  -1834       C  
-ATOM  13224  CZ  TYR B1059      30.721   8.923 -14.872  1.00 90.68           C  
-ANISOU13224  CZ  TYR B1059     9835  10533  14086   -225   1900  -2051       C  
-ATOM  13225  OH  TYR B1059      31.521   9.536 -13.938  1.00 93.16           O  
-ANISOU13225  OH  TYR B1059    10036  10832  14529   -139   1792  -2156       O  
-ATOM  13226  N   GLY B1060      26.750   4.385 -17.763  1.00109.67           N  
-ANISOU13226  N   GLY B1060    12526  13083  16059   -430   2046  -1481       N  
-ATOM  13227  CA  GLY B1060      25.919   3.415 -17.080  1.00108.22           C  
-ANISOU13227  CA  GLY B1060    12336  12977  15806   -335   1862  -1279       C  
-ATOM  13228  C   GLY B1060      26.448   2.009 -17.265  1.00109.69           C  
-ANISOU13228  C   GLY B1060    12361  13038  16279   -358   1834  -1354       C  
-ATOM  13229  O   GLY B1060      26.351   1.174 -16.367  1.00110.88           O  
-ANISOU13229  O   GLY B1060    12430  13191  16509   -254   1638  -1247       O  
-ATOM  13230  N   LEU B1061      27.017   1.748 -18.436  1.00 84.50           N  
-ANISOU13230  N   LEU B1061     9126   9736  13245   -496   2032  -1541       N  
-ATOM  13231  CA  LEU B1061      27.494   0.413 -18.767  1.00 86.08           C  
-ANISOU13231  CA  LEU B1061     9176   9813  13719   -533   2028  -1630       C  
-ATOM  13232  C   LEU B1061      28.540  -0.073 -17.767  1.00 89.28           C  
-ANISOU13232  C   LEU B1061     9386  10112  14423   -429   1847  -1710       C  
-ATOM  13233  O   LEU B1061      28.500  -1.223 -17.328  1.00 90.38           O  
-ANISOU13233  O   LEU B1061     9433  10208  14701   -368   1707  -1645       O  
-ATOM  13234  CB  LEU B1061      28.050   0.388 -20.190  1.00 84.45           C  
-ANISOU13234  CB  LEU B1061     8947   9508  13633   -702   2283  -1848       C  
-ATOM  13235  CG  LEU B1061      27.103   0.940 -21.259  1.00 80.89           C  
-ANISOU13235  CG  LEU B1061     8692   9156  12885   -806   2476  -1789       C  
-ATOM  13236  CD1 LEU B1061      27.630   0.637 -22.655  1.00 80.36           C  
-ANISOU13236  CD1 LEU B1061     8585   8991  12956   -971   2713  -1995       C  
-ATOM  13237  CD2 LEU B1061      25.701   0.377 -21.079  1.00 77.77           C  
-ANISOU13237  CD2 LEU B1061     8405   8892  12252   -754   2384  -1546       C  
-ATOM  13238  N   ASN B1062      29.464   0.812 -17.405  1.00103.95           N  
-ANISOU13238  N   ASN B1062    14848  12274  12373   -350  -1741      0       N  
-ATOM  13239  CA  ASN B1062      30.519   0.486 -16.449  0.50106.42           C  
-ANISOU13239  CA  ASN B1062    15037  12611  12788   -471  -1881    102       C  
-ATOM  13240  C   ASN B1062      29.974  -0.077 -15.146  1.00103.44           C  
-ANISOU13240  C   ASN B1062    14744  12182  12375   -341  -1943     36       C  
-ATOM  13241  O   ASN B1062      30.679  -0.771 -14.414  1.00103.47           O  
-ANISOU13241  O   ASN B1062    14571  12250  12492   -383  -2001    105       O  
-ATOM  13242  CB  ASN B1062      31.353   1.725 -16.138  0.50114.06           C  
-ANISOU13242  CB  ASN B1062    16160  13484  13695   -714  -2093    206       C  
-ATOM  13243  CG  ASN B1062      31.909   2.371 -17.381  0.50119.92           C  
-ANISOU13243  CG  ASN B1062    16838  14259  14468   -840  -2046    263       C  
-ATOM  13244  OD1 ASN B1062      32.244   1.691 -18.350  0.50122.85           O  
-ANISOU13244  OD1 ASN B1062    16948  14749  14980   -819  -1885    288       O  
-ATOM  13245  ND2 ASN B1062      32.006   3.693 -17.365  0.50125.01           N  
-ANISOU13245  ND2 ASN B1062    17730  14788  14980   -974  -2172    280       N  
-ATOM  13246  N   VAL B1063      28.717   0.232 -14.859  1.00 95.67           N  
-ANISOU13246  N   VAL B1063    14032  11075  11243   -184  -1928    -88       N  
-ATOM  13247  CA  VAL B1063      28.109  -0.172 -13.604  1.00 91.71           C  
-ANISOU13247  CA  VAL B1063    13664  10483  10697    -55  -1993   -163       C  
-ATOM  13248  C   VAL B1063      27.017  -1.217 -13.820  1.00 86.86           C  
-ANISOU13248  C   VAL B1063    12975   9929  10100    226  -1800   -298       C  
-ATOM  13249  O   VAL B1063      26.635  -1.930 -12.894  1.00 84.88           O  
-ANISOU13249  O   VAL B1063    12732   9654   9866    366  -1810   -367       O  
-ATOM  13250  CB  VAL B1063      27.547   1.042 -12.848  1.00 93.95           C  
-ANISOU13250  CB  VAL B1063    14364  10532  10799   -104  -2141   -187       C  
-ATOM  13251  CG1 VAL B1063      26.253   1.524 -13.493  1.00 93.72           C  
-ANISOU13251  CG1 VAL B1063    14544  10414  10653     55  -2015   -277       C  
-ATOM  13252  CG2 VAL B1063      27.341   0.698 -11.382  1.00 94.66           C  
-ANISOU13252  CG2 VAL B1063    14587  10513  10868    -56  -2258   -226       C  
-ATOM  13253  N   ALA B1064      26.517  -1.311 -15.046  1.00 66.21           N  
-ANISOU13253  N   ALA B1064    10290   7391   7475    304  -1623   -334       N  
-ATOM  13254  CA  ALA B1064      25.574  -2.368 -15.377  1.00 61.83           C  
-ANISOU13254  CA  ALA B1064     9633   6924   6935    544  -1425   -446       C  
-ATOM  13255  C   ALA B1064      26.290  -3.713 -15.313  1.00 61.76           C  
-ANISOU13255  C   ALA B1064     9274   7097   7096    571  -1315   -428       C  
-ATOM  13256  O   ALA B1064      25.654  -4.767 -15.260  1.00 59.10           O  
-ANISOU13256  O   ALA B1064     8834   6838   6783    772  -1162   -525       O  
-ATOM  13257  CB  ALA B1064      24.969  -2.143 -16.744  1.00 60.34           C  
-ANISOU13257  CB  ALA B1064     9444   6791   6693    576  -1267   -466       C  
-ATOM  13258  N   LYS B1065      27.621  -3.678 -15.316  1.00 67.99           N  
-ANISOU13258  N   LYS B1065     9876   7952   8005    369  -1383   -292       N  
-ATOM  13259  CA  LYS B1065      28.398  -4.898 -15.125  1.00 69.12           C  
-ANISOU13259  CA  LYS B1065     9684   8253   8327    378  -1282   -238       C  
-ATOM  13260  C   LYS B1065      28.438  -5.226 -13.640  1.00 66.12           C  
-ANISOU13260  C   LYS B1065     9347   7817   7958    431  -1427   -256       C  
-ATOM  13261  O   LYS B1065      28.540  -6.387 -13.254  1.00 63.88           O  
-ANISOU13261  O   LYS B1065     8844   7644   7783    546  -1317   -277       O  
-ATOM  13262  CB  LYS B1065      29.814  -4.763 -15.693  1.00 77.65           C  
-ANISOU13262  CB  LYS B1065    10536   9416   9552    142  -1290    -59       C  
-ATOM  13263  CG  LYS B1065      30.669  -3.720 -15.007  1.00 90.57           C  
-ANISOU13263  CG  LYS B1065    12295  10950  11168    -80  -1564     63       C  
-ATOM  13264  CD  LYS B1065      32.068  -3.673 -15.599  1.00102.82           C  
-ANISOU13264  CD  LYS B1065    13598  12587  12881   -297  -1561    251       C  
-ATOM  13265  CE  LYS B1065      32.924  -2.632 -14.899  1.00112.48           C  
-ANISOU13265  CE  LYS B1065    14949  13719  14071   -530  -1841    378       C  
-ATOM  13266  NZ  LYS B1065      34.307  -2.593 -15.432  1.00120.05           N  
-ANISOU13266  NZ  LYS B1065    15661  14755  15199   -738  -1847    577       N  
-ATOM  13267  N   LEU B1066      28.346  -4.192 -12.810  1.00 78.21           N  
-ANISOU13267  N   LEU B1066    11172   9171   9372    342  -1662   -249       N  
-ATOM  13268  CA  LEU B1066      28.226  -4.383 -11.368  1.00 75.23           C  
-ANISOU13268  CA  LEU B1066    10906   8702   8976    387  -1811   -283       C  
-ATOM  13269  C   LEU B1066      26.891  -5.030 -11.017  1.00 68.67           C  
-ANISOU13269  C   LEU B1066    10185   7822   8084    682  -1700   -469       C  
-ATOM  13270  O   LEU B1066      26.808  -5.826 -10.087  1.00 67.02           O  
-ANISOU13270  O   LEU B1066     9911   7625   7928    795  -1711   -521       O  
-ATOM  13271  CB  LEU B1066      28.378  -3.057 -10.615  1.00 80.85           C  
-ANISOU13271  CB  LEU B1066    11953   9213   9555    201  -2067   -233       C  
-ATOM  13272  CG  LEU B1066      29.796  -2.503 -10.471  1.00 86.72           C  
-ANISOU13272  CG  LEU B1066    12602   9991  10355   -104  -2238    -42       C  
-ATOM  13273  CD1 LEU B1066      29.807  -1.316  -9.522  1.00 90.99           C  
-ANISOU13273  CD1 LEU B1066    13510  10324  10739   -274  -2478    -16       C  
-ATOM  13274  CD2 LEU B1066      30.725  -3.596  -9.973  1.00 89.88           C  
-ANISOU13274  CD2 LEU B1066    12657  10553  10941   -138  -2234     60       C  
-ATOM  13275  N   ALA B1067      25.849  -4.681 -11.763  1.00 72.18           N  
-ANISOU13275  N   ALA B1067    10794   8212   8420    806  -1596   -562       N  
-ATOM  13276  CA  ALA B1067      24.536  -5.277 -11.558  1.00 65.90           C  
-ANISOU13276  CA  ALA B1067    10099   7372   7567   1091  -1479   -726       C  
-ATOM  13277  C   ALA B1067      24.472  -6.659 -12.199  1.00 61.47           C  
-ANISOU13277  C   ALA B1067     9209   7034   7111   1243  -1228   -779       C  
-ATOM  13278  O   ALA B1067      23.439  -7.330 -12.152  1.00 57.07           O  
-ANISOU13278  O   ALA B1067     8683   6483   6517   1485  -1099   -916       O  
-ATOM  13279  CB  ALA B1067      23.448  -4.380 -12.113  1.00 63.19           C  
-ANISOU13279  CB  ALA B1067    10045   6892   7073   1155  -1459   -774       C  
-ATOM  13280  N   ASP B1068      25.583  -7.064 -12.811  1.00 70.12           N  
-ANISOU13280  N   ASP B1068    10000   8303   8338   1094  -1148   -662       N  
-ATOM  13281  CA  ASP B1068      25.750  -8.411 -13.360  1.00 66.11           C  
-ANISOU13281  CA  ASP B1068     9160   8006   7951   1196   -887   -682       C  
-ATOM  13282  C   ASP B1068      24.893  -8.699 -14.594  1.00 61.51           C  
-ANISOU13282  C   ASP B1068     8569   7502   7301   1306   -657   -763       C  
-ATOM  13283  O   ASP B1068      24.513  -9.842 -14.845  1.00 59.53           O  
-ANISOU13283  O   ASP B1068     8149   7385   7086   1466   -429   -844       O  
-ATOM  13284  CB  ASP B1068      25.517  -9.480 -12.284  1.00 69.90           C  
-ANISOU13284  CB  ASP B1068     9547   8521   8491   1388   -851   -775       C  
-ATOM  13285  CG  ASP B1068      26.218 -10.793 -12.600  1.00 71.97           C  
-ANISOU13285  CG  ASP B1068     9416   9007   8923   1411   -612   -727       C  
-ATOM  13286  OD1 ASP B1068      25.612 -11.864 -12.377  1.00 74.95           O  
-ANISOU13286  OD1 ASP B1068     9698   9465   9315   1635   -436   -853       O  
-ATOM  13287  OD2 ASP B1068      27.376 -10.756 -13.070  1.00 74.37           O  
-ANISOU13287  OD2 ASP B1068     9508   9399   9350   1206   -588   -557       O  
-ATOM  13288  N   VAL B1069      24.591  -7.667 -15.370  1.00 51.09           N  
-ANISOU13288  N   VAL B1069     7430   6105   5877   1212   -707   -736       N  
-ATOM  13289  CA  VAL B1069      24.023  -7.894 -16.688  1.00 47.28           C  
-ANISOU13289  CA  VAL B1069     6900   5721   5345   1246   -494   -768       C  
-ATOM  13290  C   VAL B1069      25.116  -8.555 -17.537  1.00 46.21           C  
-ANISOU13290  C   VAL B1069     6442   5757   5360   1100   -313   -665       C  
-ATOM  13291  O   VAL B1069      26.242  -8.054 -17.601  1.00 48.03           O  
-ANISOU13291  O   VAL B1069     6593   5975   5682    894   -415   -528       O  
-ATOM  13292  CB  VAL B1069      23.560  -6.577 -17.334  1.00 46.04           C  
-ANISOU13292  CB  VAL B1069     6992   5445   5056   1155   -595   -739       C  
-ATOM  13293  CG1 VAL B1069      22.949  -6.839 -18.704  1.00 44.49           C  
-ANISOU13293  CG1 VAL B1069     6742   5358   4804   1177   -380   -763       C  
-ATOM  13294  CG2 VAL B1069      22.568  -5.878 -16.432  1.00 44.28           C  
-ANISOU13294  CG2 VAL B1069     7095   5024   4705   1283   -759   -810       C  
-ATOM  13295  N   PRO B1070      24.795  -9.691 -18.176  1.00 42.30           N  
-ANISOU13295  N   PRO B1070     5767   5414   4891   1202    -33   -722       N  
-ATOM  13296  CA  PRO B1070      25.773 -10.492 -18.926  1.00 43.38           C  
-ANISOU13296  CA  PRO B1070     5599   5702   5182   1082    194   -624       C  
-ATOM  13297  C   PRO B1070      26.754  -9.639 -19.729  1.00 46.89           C  
-ANISOU13297  C   PRO B1070     6012   6114   5690    823    130   -473       C  
-ATOM  13298  O   PRO B1070      26.358  -8.635 -20.317  1.00 49.94           O  
-ANISOU13298  O   PRO B1070     6595   6419   5962    754     33   -479       O  
-ATOM  13299  CB  PRO B1070      24.894 -11.307 -19.867  1.00 43.19           C  
-ANISOU13299  CB  PRO B1070     5536   5793   5080   1190    484   -722       C  
-ATOM  13300  CG  PRO B1070      23.617 -11.470 -19.120  1.00 40.97           C  
-ANISOU13300  CG  PRO B1070     5436   5465   4665   1437    427   -881       C  
-ATOM  13301  CD  PRO B1070      23.426 -10.219 -18.310  1.00 40.57           C  
-ANISOU13301  CD  PRO B1070     5649   5221   4545   1426     99   -874       C  
-ATOM  13302  N   GLY B1071      28.019 -10.040 -19.754  1.00 46.40           N  
-ANISOU13302  N   GLY B1071     5702   6113   5816    686    193   -331       N  
-ATOM  13303  CA  GLY B1071      29.040  -9.276 -20.446  1.00 50.03           C  
-ANISOU13303  CA  GLY B1071     6119   6533   6359    446    129   -179       C  
-ATOM  13304  C   GLY B1071      28.750  -9.050 -21.922  1.00 52.29           C  
-ANISOU13304  C   GLY B1071     6444   6835   6587    364    293   -191       C  
-ATOM  13305  O   GLY B1071      29.025  -7.978 -22.460  1.00 55.11           O  
-ANISOU13305  O   GLY B1071     6918   7108   6912    217    160   -138       O  
-ATOM  13306  N   GLU B1072      28.195 -10.061 -22.582  1.00 59.12           N  
-ANISOU13306  N   GLU B1072     7219   7810   7435    451    588   -262       N  
-ATOM  13307  CA  GLU B1072      27.915  -9.978 -24.012  1.00 59.40           C  
-ANISOU13307  CA  GLU B1072     7284   7871   7414    354    770   -269       C  
-ATOM  13308  C   GLU B1072      27.043  -8.777 -24.341  1.00 57.44           C  
-ANISOU13308  C   GLU B1072     7317   7531   6976    352    581   -335       C  
-ATOM  13309  O   GLU B1072      27.262  -8.095 -25.338  1.00 58.43           O  
-ANISOU13309  O   GLU B1072     7492   7621   7087    196    582   -284       O  
-ATOM  13310  CB  GLU B1072      27.208 -11.241 -24.503  1.00 58.95           C  
-ANISOU13310  CB  GLU B1072     7139   7946   7314    465   1100   -359       C  
-ATOM  13311  CG  GLU B1072      27.879 -12.537 -24.108  1.00 62.82           C  
-ANISOU13311  CG  GLU B1072     7359   8537   7974    506   1333   -310       C  
-ATOM  13312  CD  GLU B1072      27.360 -13.094 -22.789  1.00 62.01           C  
-ANISOU13312  CD  GLU B1072     7249   8469   7843    737   1263   -412       C  
-ATOM  13313  OE1 GLU B1072      26.515 -14.017 -22.825  1.00 61.42           O  
-ANISOU13313  OE1 GLU B1072     7161   8490   7687    897   1470   -534       O  
-ATOM  13314  OE2 GLU B1072      27.801 -12.614 -21.720  1.00 62.15           O  
-ANISOU13314  OE2 GLU B1072     7282   8415   7917    752   1003   -370       O  
-ATOM  13315  N   ILE B1073      26.045  -8.532 -23.501  1.00 51.27           N  
-ANISOU13315  N   ILE B1073     6717   6705   6057    529    431   -442       N  
-ATOM  13316  CA  ILE B1073      25.062  -7.491 -23.769  1.00 48.57           C  
-ANISOU13316  CA  ILE B1073     6640   6278   5535    556    290   -496       C  
-ATOM  13317  C   ILE B1073      25.642  -6.099 -23.580  1.00 48.81           C  
-ANISOU13317  C   ILE B1073     6806   6172   5566    416     28   -416       C  
-ATOM  13318  O   ILE B1073      25.401  -5.209 -24.388  1.00 49.15           O  
-ANISOU13318  O   ILE B1073     6975   6171   5528    324    -11   -397       O  
-ATOM  13319  CB  ILE B1073      23.828  -7.641 -22.875  1.00 46.05           C  
-ANISOU13319  CB  ILE B1073     6486   5925   5087    793    220   -618       C  
-ATOM  13320  CG1 ILE B1073      23.262  -9.056 -22.993  1.00 44.40           C  
-ANISOU13320  CG1 ILE B1073     6141   5858   4871    943    482   -707       C  
-ATOM  13321  CG2 ILE B1073      22.779  -6.606 -23.242  1.00 45.79           C  
-ANISOU13321  CG2 ILE B1073     6713   5804   4883    819    113   -643       C  
-ATOM  13322  CD1 ILE B1073      22.056  -9.299 -22.121  1.00 44.06           C  
-ANISOU13322  CD1 ILE B1073     6247   5780   4715   1193    427   -832       C  
-ATOM  13323  N   LEU B1074      26.407  -5.910 -22.514  1.00 40.56           N  
-ANISOU13323  N   LEU B1074     5738   5067   4607    393   -147   -366       N  
-ATOM  13324  CA  LEU B1074      27.045  -4.621 -22.282  1.00 43.21           C  
-ANISOU13324  CA  LEU B1074     6201   5280   4938    241   -389   -286       C  
-ATOM  13325  C   LEU B1074      27.947  -4.256 -23.458  1.00 45.59           C  
-ANISOU13325  C   LEU B1074     6392   5602   5327     33   -322   -185       C  
-ATOM  13326  O   LEU B1074      27.923  -3.123 -23.940  1.00 47.60           O  
-ANISOU13326  O   LEU B1074     6800   5778   5507    -66   -431   -165       O  
-ATOM  13327  CB  LEU B1074      27.838  -4.629 -20.972  1.00 44.83           C  
-ANISOU13327  CB  LEU B1074     6367   5438   5228    217   -570   -229       C  
-ATOM  13328  CG  LEU B1074      26.990  -4.854 -19.717  1.00 43.97           C  
-ANISOU13328  CG  LEU B1074     6403   5272   5033    410   -665   -331       C  
-ATOM  13329  CD1 LEU B1074      27.743  -4.407 -18.481  1.00 43.98           C  
-ANISOU13329  CD1 LEU B1074     6453   5183   5073    326   -906   -262       C  
-ATOM  13330  CD2 LEU B1074      25.674  -4.110 -19.838  1.00 42.06           C  
-ANISOU13330  CD2 LEU B1074     6452   4928   4601    520   -711   -425       C  
-ATOM  13331  N   LYS B1075      28.730  -5.226 -23.920  1.00 41.92           N  
-ANISOU13331  N   LYS B1075     5665   5236   5026    -29   -126   -121       N  
-ATOM  13332  CA  LYS B1075      29.598  -5.029 -25.075  1.00 44.55           C  
-ANISOU13332  CA  LYS B1075     5884   5576   5467   -220    -25    -23       C  
-ATOM  13333  C   LYS B1075      28.781  -4.660 -26.315  1.00 40.52           C  
-ANISOU13333  C   LYS B1075     5494   5071   4829   -240     83    -88       C  
-ATOM  13334  O   LYS B1075      29.017  -3.627 -26.946  1.00 40.36           O  
-ANISOU13334  O   LYS B1075     5574   4980   4780   -367    -10    -54       O  
-ATOM  13335  CB  LYS B1075      30.410  -6.294 -25.344  1.00 49.76           C  
-ANISOU13335  CB  LYS B1075     6252   6330   6325   -259    223     59       C  
-ATOM  13336  CG  LYS B1075      31.878  -6.041 -25.597  1.00 60.82           C  
-ANISOU13336  CG  LYS B1075     7497   7689   7924   -455    195    229       C  
-ATOM  13337  CD  LYS B1075      32.603  -5.634 -24.322  1.00 69.37           C  
-ANISOU13337  CD  LYS B1075     8565   8726   9067   -481    -68    315       C  
-ATOM  13338  CE  LYS B1075      33.809  -4.751 -24.632  1.00 76.67           C  
-ANISOU13338  CE  LYS B1075     9460   9569  10103   -690   -207    463       C  
-ATOM  13339  NZ  LYS B1075      34.671  -5.296 -25.727  1.00 82.24           N  
-ANISOU13339  NZ  LYS B1075     9953  10290  11006   -814     37    581       N  
-ATOM  13340  N   LYS B1076      27.818  -5.512 -26.651  1.00 47.98           N  
-ANISOU13340  N   LYS B1076     6430   6107   5695   -120    282   -177       N  
-ATOM  13341  CA  LYS B1076      26.924  -5.272 -27.777  1.00 44.45           C  
-ANISOU13341  CA  LYS B1076     6093   5685   5112   -140    389   -230       C  
-ATOM  13342  C   LYS B1076      26.240  -3.918 -27.660  1.00 44.02           C  
-ANISOU13342  C   LYS B1076     6291   5534   4902   -120    163   -257       C  
-ATOM  13343  O   LYS B1076      26.092  -3.204 -28.646  1.00 43.52           O  
-ANISOU13343  O   LYS B1076     6304   5449   4781   -227    170   -239       O  
-ATOM  13344  CB  LYS B1076      25.863  -6.361 -27.849  1.00 40.78           C  
-ANISOU13344  CB  LYS B1076     5608   5332   4555     12    592   -325       C  
-ATOM  13345  CG  LYS B1076      24.862  -6.172 -28.968  1.00 40.00           C  
-ANISOU13345  CG  LYS B1076     5621   5275   4301    -16    697   -365       C  
-ATOM  13346  CD  LYS B1076      25.493  -6.414 -30.322  1.00 42.49           C  
-ANISOU13346  CD  LYS B1076     5827   5626   4693   -224    904   -304       C  
-ATOM  13347  CE  LYS B1076      24.440  -6.419 -31.422  1.00 41.49           C  
-ANISOU13347  CE  LYS B1076     5799   5565   4401   -263   1033   -341       C  
-ATOM  13348  NZ  LYS B1076      24.988  -6.892 -32.739  1.00 43.11           N  
-ANISOU13348  NZ  LYS B1076     5902   5806   4673   -472   1284   -292       N  
-ATOM  13349  N   ALA B1077      25.818  -3.566 -26.451  1.00 45.06           N  
-ANISOU13349  N   ALA B1077     6556   5598   4967     14    -25   -295       N  
-ATOM  13350  CA  ALA B1077      25.157  -2.288 -26.229  1.00 45.56           C  
-ANISOU13350  CA  ALA B1077     6873   5550   4887     39   -215   -308       C  
-ATOM  13351  C   ALA B1077      26.110  -1.120 -26.480  1.00 48.10           C  
-ANISOU13351  C   ALA B1077     7240   5783   5253   -144   -364   -227       C  
-ATOM  13352  O   ALA B1077      25.746  -0.154 -27.145  1.00 49.50           O  
-ANISOU13352  O   ALA B1077     7553   5916   5339   -201   -401   -218       O  
-ATOM  13353  CB  ALA B1077      24.586  -2.220 -24.829  1.00 45.32           C  
-ANISOU13353  CB  ALA B1077     6987   5441   4792    208   -363   -359       C  
-ATOM  13354  N   ALA B1078      27.323  -1.203 -25.940  1.00 39.68           N  
-ANISOU13354  N   ALA B1078     6056   4694   4326   -235   -446   -162       N  
-ATOM  13355  CA  ALA B1078      28.330  -0.170 -26.169  1.00 41.18           C  
-ANISOU13355  CA  ALA B1078     6271   4807   4569   -416   -583    -80       C  
-ATOM  13356  C   ALA B1078      28.589  -0.025 -27.664  1.00 41.33           C  
-ANISOU13356  C   ALA B1078     6214   4861   4629   -544   -440    -55       C  
-ATOM  13357  O   ALA B1078      28.746   1.086 -28.179  1.00 42.03           O  
-ANISOU13357  O   ALA B1078     6416   4882   4671   -644   -527    -36       O  
-ATOM  13358  CB  ALA B1078      29.617  -0.508 -25.441  1.00 42.21           C  
-ANISOU13358  CB  ALA B1078     6241   4934   4864   -500   -664      9       C  
-ATOM  13359  N   HIS B1079      28.633  -1.162 -28.355  1.00 45.62           N  
-ANISOU13359  N   HIS B1079     6574   5503   5257   -546   -206    -58       N  
-ATOM  13360  CA  HIS B1079      28.817  -1.178 -29.798  1.00 47.67           C  
-ANISOU13360  CA  HIS B1079     6770   5789   5554   -675    -38    -38       C  
-ATOM  13361  C   HIS B1079      27.648  -0.481 -30.481  1.00 46.37           C  
-ANISOU13361  C   HIS B1079     6789   5625   5204   -646    -39    -99       C  
-ATOM  13362  O   HIS B1079      27.786   0.630 -30.978  1.00 48.04           O  
-ANISOU13362  O   HIS B1079     7106   5770   5377   -737   -135    -80       O  
-ATOM  13363  CB  HIS B1079      28.948  -2.614 -30.308  1.00 49.47           C  
-ANISOU13363  CB  HIS B1079     6795   6117   5884   -680    241    -32       C  
-ATOM  13364  CG  HIS B1079      30.203  -3.299 -29.858  1.00 54.95           C  
-ANISOU13364  CG  HIS B1079     7276   6809   6792   -735    286     63       C  
-ATOM  13365  ND1 HIS B1079      31.319  -2.615 -29.439  1.00 58.12           N  
-ANISOU13365  ND1 HIS B1079     7648   7126   7308   -836    105    158       N  
-ATOM  13366  CD2 HIS B1079      30.509  -4.618 -29.768  1.00 56.10           C  
-ANISOU13366  CD2 HIS B1079     7224   7032   7061   -708    505     92       C  
-ATOM  13367  CE1 HIS B1079      32.264  -3.475 -29.108  1.00 58.46           C  
-ANISOU13367  CE1 HIS B1079     7474   7194   7544   -870    199    256       C  
-ATOM  13368  NE2 HIS B1079      31.799  -4.697 -29.293  1.00 57.58           N  
-ANISOU13368  NE2 HIS B1079     7254   7178   7445   -789    449    219       N  
-ATOM  13369  N   LYS B1080      26.494  -1.138 -30.489  1.00 50.15           N  
-ANISOU13369  N   LYS B1080     7301   6184   5571   -515     73   -163       N  
-ATOM  13370  CA  LYS B1080      25.286  -0.596 -31.110  1.00 48.10           C  
-ANISOU13370  CA  LYS B1080     7198   5941   5138   -480     85   -195       C  
-ATOM  13371  C   LYS B1080      25.056   0.866 -30.761  1.00 49.63           C  
-ANISOU13371  C   LYS B1080     7594   6024   5239   -472   -129   -179       C  
-ATOM  13372  O   LYS B1080      24.507   1.625 -31.553  1.00 48.50           O  
-ANISOU13372  O   LYS B1080     7551   5876   5001   -518   -125   -166       O  
-ATOM  13373  CB  LYS B1080      24.064  -1.418 -30.701  1.00 45.90           C  
-ANISOU13373  CB  LYS B1080     6952   5740   4748   -299    169   -257       C  
-ATOM  13374  CG  LYS B1080      23.487  -2.272 -31.814  1.00 44.37           C  
-ANISOU13374  CG  LYS B1080     6683   5671   4506   -343    410   -273       C  
-ATOM  13375  CD  LYS B1080      22.910  -1.414 -32.922  1.00 46.88           C  
-ANISOU13375  CD  LYS B1080     7108   5991   4713   -446    411   -240       C  
-ATOM  13376  CE  LYS B1080      22.301  -2.277 -34.024  1.00 48.16           C  
-ANISOU13376  CE  LYS B1080     7210   6282   4807   -517    646   -247       C  
-ATOM  13377  NZ  LYS B1080      21.880  -1.502 -35.249  1.00 50.90           N  
-ANISOU13377  NZ  LYS B1080     7635   6642   5064   -660    661   -200       N  
-ATOM  13378  N   SER B1081      25.473   1.259 -29.566  1.00 41.47           N  
-ANISOU13378  N   SER B1081     6624   4904   4229   -422   -306   -173       N  
-ATOM  13379  CA  SER B1081      25.309   2.636 -29.139  1.00 44.79           C  
-ANISOU13379  CA  SER B1081     7255   5207   4557   -425   -490   -155       C  
-ATOM  13380  C   SER B1081      26.237   3.545 -29.934  1.00 49.40           C  
-ANISOU13380  C   SER B1081     7823   5749   5196   -609   -533   -109       C  
-ATOM  13381  O   SER B1081      25.798   4.541 -30.506  1.00 50.24           O  
-ANISOU13381  O   SER B1081     8059   5821   5209   -642   -555    -99       O  
-ATOM  13382  CB  SER B1081      25.573   2.774 -27.640  1.00 42.83           C  
-ANISOU13382  CB  SER B1081     7091   4870   4314   -354   -659   -159       C  
-ATOM  13383  OG  SER B1081      25.340   4.103 -27.210  1.00 43.14           O  
-ANISOU13383  OG  SER B1081     7363   4784   4245   -366   -809   -140       O  
-ATOM  13384  N   LYS B1082      27.519   3.197 -29.967  1.00 53.84           N  
-ANISOU13384  N   LYS B1082     8224   6312   5919   -723   -537    -73       N  
-ATOM  13385  CA  LYS B1082      28.486   3.960 -30.743  1.00 59.52           C  
-ANISOU13385  CA  LYS B1082     8914   6986   6715   -893   -569    -30       C  
-ATOM  13386  C   LYS B1082      28.067   4.025 -32.209  1.00 58.06           C  
-ANISOU13386  C   LYS B1082     8707   6850   6504   -959   -413    -44       C  
-ATOM  13387  O   LYS B1082      28.243   5.048 -32.870  1.00 58.54           O  
-ANISOU13387  O   LYS B1082     8844   6862   6536  -1049   -457    -34       O  
-ATOM  13388  CB  LYS B1082      29.886   3.358 -30.626  1.00 66.13           C  
-ANISOU13388  CB  LYS B1082     9550   7821   7755   -997   -562     33       C  
-ATOM  13389  CG  LYS B1082      30.861   3.902 -31.657  1.00 75.91           C  
-ANISOU13389  CG  LYS B1082    10726   9015   9102  -1169   -542     77       C  
-ATOM  13390  CD  LYS B1082      32.235   3.272 -31.525  1.00 84.75           C  
-ANISOU13390  CD  LYS B1082    11640  10120  10442  -1267   -522    167       C  
-ATOM  13391  CE  LYS B1082      32.930   3.717 -30.247  1.00 90.72           C  
-ANISOU13391  CE  LYS B1082    12428  10823  11217  -1279   -746    224       C  
-ATOM  13392  NZ  LYS B1082      34.293   3.123 -30.124  1.00 95.10           N  
-ANISOU13392  NZ  LYS B1082    12765  11370  11999  -1383   -731    345       N  
-ATOM  13393  N   GLU B1083      27.508   2.932 -32.714  1.00 64.75           N  
-ANISOU13393  N   GLU B1083     9456   7795   7352   -922   -226    -66       N  
-ATOM  13394  CA  GLU B1083      27.066   2.892 -34.101  1.00 63.37           C  
-ANISOU13394  CA  GLU B1083     9266   7673   7140  -1006    -70    -73       C  
-ATOM  13395  C   GLU B1083      25.984   3.925 -34.372  1.00 61.87           C  
-ANISOU13395  C   GLU B1083     9258   7476   6774   -962   -134    -81       C  
-ATOM  13396  O   GLU B1083      26.059   4.656 -35.350  1.00 62.10           O  
-ANISOU13396  O   GLU B1083     9318   7489   6787  -1071   -118    -67       O  
-ATOM  13397  CB  GLU B1083      26.557   1.504 -34.486  1.00 62.82           C  
-ANISOU13397  CB  GLU B1083     9081   7715   7072   -978    148    -94       C  
-ATOM  13398  CG  GLU B1083      25.826   1.486 -35.820  1.00 64.27           C  
-ANISOU13398  CG  GLU B1083     9290   7964   7165  -1065    297    -98       C  
-ATOM  13399  CD  GLU B1083      25.469   0.085 -36.279  1.00 65.52           C  
-ANISOU13399  CD  GLU B1083     9340   8231   7324  -1079    536   -114       C  
-ATOM  13400  OE1 GLU B1083      24.280  -0.289 -36.184  1.00 65.80           O  
-ANISOU13400  OE1 GLU B1083     9432   8354   7214   -976    582   -139       O  
-ATOM  13401  OE2 GLU B1083      26.379  -0.644 -36.732  1.00 67.90           O  
-ANISOU13401  OE2 GLU B1083     9503   8524   7773  -1195    689    -95       O  
-ATOM  13402  N   LEU B1084      24.978   3.985 -33.508  1.00 61.27           N  
-ANISOU13402  N   LEU B1084     9301   7405   6575   -799   -197    -95       N  
-ATOM  13403  CA  LEU B1084      23.860   4.899 -33.717  1.00 60.34           C  
-ANISOU13403  CA  LEU B1084     9351   7277   6300   -744   -232    -75       C  
-ATOM  13404  C   LEU B1084      24.275   6.361 -33.587  1.00 62.06           C  
-ANISOU13404  C   LEU B1084     9700   7384   6495   -796   -375    -50       C  
-ATOM  13405  O   LEU B1084      23.815   7.208 -34.351  1.00 63.22           O  
-ANISOU13405  O   LEU B1084     9921   7532   6566   -839   -356    -20       O  
-ATOM  13406  CB  LEU B1084      22.714   4.600 -32.752  1.00 58.83           C  
-ANISOU13406  CB  LEU B1084     9264   7088   6002   -549   -256    -83       C  
-ATOM  13407  CG  LEU B1084      21.481   5.463 -33.013  1.00 57.61           C  
-ANISOU13407  CG  LEU B1084     9271   6921   5698   -487   -262    -31       C  
-ATOM  13408  CD1 LEU B1084      20.979   5.190 -34.412  1.00 56.26           C  
-ANISOU13408  CD1 LEU B1084     9019   6871   5488   -582   -116     -1       C  
-ATOM  13409  CD2 LEU B1084      20.389   5.214 -31.987  1.00 55.65           C  
-ANISOU13409  CD2 LEU B1084     9140   6641   5363   -286   -289    -28       C  
-ATOM  13410  N   GLU B1085      25.129   6.664 -32.615  1.00 56.93           N  
-ANISOU13410  N   GLU B1085     9081   6645   5903   -797   -512    -56       N  
-ATOM  13411  CA  GLU B1085      25.633   8.027 -32.477  1.00 60.35           C  
-ANISOU13411  CA  GLU B1085     9644   6977   6311   -865   -637    -36       C  
-ATOM  13412  C   GLU B1085      26.402   8.410 -33.736  1.00 61.37           C  
-ANISOU13412  C   GLU B1085     9679   7119   6519  -1027   -588    -33       C  
-ATOM  13413  O   GLU B1085      25.958   9.264 -34.504  1.00 62.52           O  
-ANISOU13413  O   GLU B1085     9901   7265   6590  -1060   -558    -20       O  
-ATOM  13414  CB  GLU B1085      26.521   8.186 -31.240  1.00 62.83           C  
-ANISOU13414  CB  GLU B1085     9996   7202   6673   -874   -793    -35       C  
-ATOM  13415  CG  GLU B1085      27.065   9.597 -31.070  1.00 68.09           C  
-ANISOU13415  CG  GLU B1085    10810   7765   7295   -959   -914    -17       C  
-ATOM  13416  CD  GLU B1085      27.803   9.816 -29.754  1.00 71.66           C  
-ANISOU13416  CD  GLU B1085    11339   8130   7759   -981  -1078     -4       C  
-ATOM  13417  OE1 GLU B1085      28.216   8.822 -29.118  1.00 73.19           O  
-ANISOU13417  OE1 GLU B1085    11413   8352   8042   -961  -1104     -2       O  
-ATOM  13418  OE2 GLU B1085      27.969  10.993 -29.357  1.00 73.29           O  
-ANISOU13418  OE2 GLU B1085    11727   8241   7877  -1029  -1172     11       O  
-ATOM  13419  N   GLY B1086      27.547   7.767 -33.949  1.00 60.34           N  
-ANISOU13419  N   GLY B1086     9383   6995   6550  -1124   -569    -36       N  
-ATOM  13420  CA  GLY B1086      28.344   8.003 -35.138  1.00 60.06           C  
-ANISOU13420  CA  GLY B1086     9254   6950   6615  -1277   -509    -34       C  
-ATOM  13421  C   GLY B1086      27.457   8.177 -36.355  1.00 58.87           C  
-ANISOU13421  C   GLY B1086     9125   6862   6382  -1304   -382    -41       C  
-ATOM  13422  O   GLY B1086      27.609   9.129 -37.119  1.00 58.50           O  
-ANISOU13422  O   GLY B1086     9127   6783   6318  -1383   -393    -42       O  
-ATOM  13423  N   LEU B1087      26.514   7.258 -36.521  1.00 58.75           N  
-ANISOU13423  N   LEU B1087     9071   6941   6309  -1240   -263    -42       N  
-ATOM  13424  CA  LEU B1087      25.551   7.325 -37.610  1.00 58.83           C  
-ANISOU13424  CA  LEU B1087     9100   7029   6222  -1274   -147    -29       C  
-ATOM  13425  C   LEU B1087      24.842   8.679 -37.623  1.00 60.18           C  
-ANISOU13425  C   LEU B1087     9434   7170   6260  -1230   -227      1       C  
-ATOM  13426  O   LEU B1087      25.057   9.491 -38.524  1.00 61.21           O  
-ANISOU13426  O   LEU B1087     9580   7285   6393  -1331   -216      7       O  
-ATOM  13427  CB  LEU B1087      24.540   6.184 -37.484  1.00 55.54           C  
-ANISOU13427  CB  LEU B1087     8648   6719   5736  -1187    -35    -26       C  
-ATOM  13428  CG  LEU B1087      23.564   5.914 -38.628  1.00 55.18           C  
-ANISOU13428  CG  LEU B1087     8591   6780   5593  -1248    107      2       C  
-ATOM  13429  CD1 LEU B1087      23.369   4.416 -38.815  1.00 55.20           C  
-ANISOU13429  CD1 LEU B1087     8480   6877   5615  -1261    270    -17       C  
-ATOM  13430  CD2 LEU B1087      22.233   6.604 -38.379  1.00 53.88           C  
-ANISOU13430  CD2 LEU B1087     8563   6645   5263  -1130     56     56       C  
-ATOM  13431  N   ILE B1088      24.008   8.927 -36.617  1.00 65.59           N  
-ANISOU13431  N   ILE B1088    10243   7839   6838  -1077   -294     24       N  
-ATOM  13432  CA  ILE B1088      23.261  10.177 -36.543  1.00 66.54           C  
-ANISOU13432  CA  ILE B1088    10527   7919   6835  -1025   -338     74       C  
-ATOM  13433  C   ILE B1088      24.146  11.388 -36.791  1.00 68.43           C  
-ANISOU13433  C   ILE B1088    10819   8076   7107  -1119   -410     61       C  
-ATOM  13434  O   ILE B1088      23.803  12.256 -37.593  1.00 69.62           O  
-ANISOU13434  O   ILE B1088    11012   8239   7203  -1164   -372     93       O  
-ATOM  13435  CB  ILE B1088      22.547  10.347 -35.187  1.00 66.56           C  
-ANISOU13435  CB  ILE B1088    10682   7857   6750   -855   -411     99       C  
-ATOM  13436  CG1 ILE B1088      21.112   9.832 -35.280  1.00 65.52           C  
-ANISOU13436  CG1 ILE B1088    10570   7803   6521   -744   -322    155       C  
-ATOM  13437  CG2 ILE B1088      22.541  11.807 -34.765  1.00 66.08           C  
-ANISOU13437  CG2 ILE B1088    10804   7685   6619   -842   -486    133       C  
-ATOM  13438  CD1 ILE B1088      21.017   8.383 -35.672  1.00 64.91           C  
-ANISOU13438  CD1 ILE B1088    10332   7843   6487   -758   -226    120       C  
-ATOM  13439  N   ASN B1089      25.290  11.435 -36.115  1.00 67.45           N  
-ANISOU13439  N   ASN B1089    10685   7872   7071  -1152   -513     20       N  
-ATOM  13440  CA  ASN B1089      26.132  12.627 -36.139  1.00 69.42           C  
-ANISOU13440  CA  ASN B1089    11009   8034   7335  -1229   -598      6       C  
-ATOM  13441  C   ASN B1089      26.946  12.834 -37.420  1.00 69.73           C  
-ANISOU13441  C   ASN B1089    10936   8083   7477  -1376   -551    -23       C  
-ATOM  13442  O   ASN B1089      27.448  13.929 -37.671  1.00 70.71           O  
-ANISOU13442  O   ASN B1089    11126   8148   7594  -1432   -597    -37       O  
-ATOM  13443  CB  ASN B1089      27.009  12.684 -34.887  1.00 70.88           C  
-ANISOU13443  CB  ASN B1089    11242   8130   7559  -1223   -739     -9       C  
-ATOM  13444  CG  ASN B1089      26.213  13.052 -33.645  1.00 72.99           C  
-ANISOU13444  CG  ASN B1089    11700   8338   7694  -1098   -797     20       C  
-ATOM  13445  OD1 ASN B1089      25.241  13.805 -33.726  1.00 72.26           O  
-ANISOU13445  OD1 ASN B1089    11746   8229   7480  -1034   -749     58       O  
-ATOM  13446  ND2 ASN B1089      26.614  12.520 -32.493  1.00 74.29           N  
-ANISOU13446  ND2 ASN B1089    11875   8461   7889  -1066   -892     11       N  
-ATOM  13447  N   THR B1090      27.062  11.787 -38.231  1.00 66.33           N  
-ANISOU13447  N   THR B1090    10347   7718   7136  -1440   -446    -34       N  
-ATOM  13448  CA  THR B1090      27.716  11.894 -39.531  1.00 65.96           C  
-ANISOU13448  CA  THR B1090    10208   7666   7189  -1585   -375    -59       C  
-ATOM  13449  C   THR B1090      26.736  12.460 -40.548  1.00 65.31           C  
-ANISOU13449  C   THR B1090    10169   7647   6998  -1606   -289    -36       C  
-ATOM  13450  O   THR B1090      27.114  13.214 -41.445  1.00 66.54           O  
-ANISOU13450  O   THR B1090    10326   7774   7181  -1698   -273    -57       O  
-ATOM  13451  CB  THR B1090      28.230  10.527 -40.022  1.00 65.92           C  
-ANISOU13451  CB  THR B1090    10034   7687   7324  -1666   -266    -68       C  
-ATOM  13452  OG1 THR B1090      29.636  10.424 -39.767  1.00 67.21           O  
-ANISOU13452  OG1 THR B1090    10123   7758   7655  -1732   -325    -80       O  
-ATOM  13453  CG2 THR B1090      27.986  10.363 -41.508  1.00 65.64           C  
-ANISOU13453  CG2 THR B1090     9945   7694   7303  -1790   -121    -73       C  
-ATOM  13454  N   LYS B1091      25.469  12.093 -40.393  1.00 62.71           N  
-ANISOU13454  N   LYS B1091     9873   7405   6549  -1519   -235     14       N  
-ATOM  13455  CA  LYS B1091      24.421  12.578 -41.279  1.00 61.18           C  
-ANISOU13455  CA  LYS B1091     9711   7288   6245  -1538   -157     69       C  
-ATOM  13456  C   LYS B1091      23.970  13.987 -40.917  1.00 61.65           C  
-ANISOU13456  C   LYS B1091     9917   7306   6201  -1460   -214    112       C  
-ATOM  13457  O   LYS B1091      23.391  14.688 -41.742  1.00 61.72           O  
-ANISOU13457  O   LYS B1091     9944   7360   6146  -1496   -156    162       O  
-ATOM  13458  CB  LYS B1091      23.228  11.623 -41.283  1.00 58.51           C  
-ANISOU13458  CB  LYS B1091     9346   7063   5821  -1483    -73    127       C  
-ATOM  13459  CG  LYS B1091      23.556  10.259 -41.847  1.00 57.01           C  
-ANISOU13459  CG  LYS B1091     9021   6929   5713  -1583     31     92       C  
-ATOM  13460  CD  LYS B1091      22.299   9.443 -42.097  1.00 56.23           C  
-ANISOU13460  CD  LYS B1091     8904   6960   5502  -1559    130    153       C  
-ATOM  13461  CE  LYS B1091      22.641   8.060 -42.637  1.00 55.40           C  
-ANISOU13461  CE  LYS B1091     8679   6906   5466  -1670    262    115       C  
-ATOM  13462  NZ  LYS B1091      23.434   8.141 -43.905  1.00 54.39           N  
-ANISOU13462  NZ  LYS B1091     8491   6746   5428  -1877    342     87       N  
-ATOM  13463  N   ARG B1092      24.234  14.404 -39.684  1.00 56.53           N  
-ANISOU13463  N   ARG B1092     9376   6569   5532  -1364   -314    102       N  
-ATOM  13464  CA  ARG B1092      23.878  15.753 -39.265  1.00 57.73           C  
-ANISOU13464  CA  ARG B1092     9690   6661   5584  -1300   -343    144       C  
-ATOM  13465  C   ARG B1092      24.956  16.755 -39.662  1.00 57.38           C  
-ANISOU13465  C   ARG B1092     9663   6547   5591  -1394   -385     82       C  
-ATOM  13466  O   ARG B1092      24.650  17.879 -40.045  1.00 57.06           O  
-ANISOU13466  O   ARG B1092     9700   6498   5481  -1394   -345    112       O  
-ATOM  13467  CB  ARG B1092      23.611  15.814 -37.759  1.00 60.02           C  
-ANISOU13467  CB  ARG B1092    10124   6871   5811  -1172   -416    165       C  
-ATOM  13468  CG  ARG B1092      22.175  15.472 -37.382  1.00 62.90           C  
-ANISOU13468  CG  ARG B1092    10547   7276   6076  -1042   -355    259       C  
-ATOM  13469  CD  ARG B1092      21.939  15.538 -35.873  1.00 64.31           C  
-ANISOU13469  CD  ARG B1092    10887   7346   6202   -918   -423    273       C  
-ATOM  13470  NE  ARG B1092      22.143  16.877 -35.322  1.00 66.53           N  
-ANISOU13470  NE  ARG B1092    11355   7508   6416   -915   -449    293       N  
-ATOM  13471  CZ  ARG B1092      22.996  17.158 -34.343  1.00 67.49           C  
-ANISOU13471  CZ  ARG B1092    11577   7522   6544   -937   -554    239       C  
-ATOM  13472  NH1 ARG B1092      23.727  16.192 -33.804  1.00 68.55           N  
-ANISOU13472  NH1 ARG B1092    11625   7657   6762   -956   -651    172       N  
-ATOM  13473  NH2 ARG B1092      23.120  18.403 -33.901  1.00 68.20           N  
-ANISOU13473  NH2 ARG B1092    11854   7506   6553   -950   -555    261       N  
-ATOM  13474  N   LYS B1093      26.215  16.339 -39.570  1.00 61.58           N  
-ANISOU13474  N   LYS B1093    10118   7030   6250  -1470   -456      4       N  
-ATOM  13475  CA  LYS B1093      27.330  17.193 -39.957  1.00 63.48           C  
-ANISOU13475  CA  LYS B1093    10364   7199   6556  -1560   -503    -57       C  
-ATOM  13476  C   LYS B1093      27.361  17.376 -41.469  1.00 63.19           C  
-ANISOU13476  C   LYS B1093    10234   7206   6569  -1659   -410    -79       C  
-ATOM  13477  O   LYS B1093      27.589  18.482 -41.966  1.00 63.94           O  
-ANISOU13477  O   LYS B1093    10381   7272   6643  -1689   -402   -103       O  
-ATOM  13478  CB  LYS B1093      28.657  16.621 -39.449  1.00 66.21           C  
-ANISOU13478  CB  LYS B1093    10639   7478   7040  -1618   -604   -107       C  
-ATOM  13479  CG  LYS B1093      29.031  17.062 -38.047  1.00 71.12           C  
-ANISOU13479  CG  LYS B1093    11392   8023   7608  -1570   -731    -99       C  
-ATOM  13480  CD  LYS B1093      29.682  15.930 -37.244  1.00 74.87           C  
-ANISOU13480  CD  LYS B1093    11775   8486   8188  -1576   -807    -95       C  
-ATOM  13481  CE  LYS B1093      30.057  16.370 -35.819  1.00 77.43           C  
-ANISOU13481  CE  LYS B1093    12238   8734   8446  -1553   -946    -80       C  
-ATOM  13482  NZ  LYS B1093      28.914  16.969 -35.070  1.00 78.06           N  
-ANISOU13482  NZ  LYS B1093    12518   8796   8345  -1447   -929    -46       N  
-ATOM  13483  N   ARG B1094      27.126  16.293 -42.202  1.00 63.85           N  
-ANISOU13483  N   ARG B1094    10189   7358   6713  -1715   -330    -71       N  
-ATOM  13484  CA  ARG B1094      27.042  16.392 -43.646  1.00 62.03           C  
-ANISOU13484  CA  ARG B1094     9885   7168   6516  -1827   -234    -83       C  
-ATOM  13485  C   ARG B1094      25.969  17.411 -44.003  1.00 60.85           C  
-ANISOU13485  C   ARG B1094     9816   7081   6224  -1782   -184    -18       C  
-ATOM  13486  O   ARG B1094      26.271  18.472 -44.537  1.00 62.21           O  
-ANISOU13486  O   ARG B1094    10021   7221   6394  -1815   -178    -47       O  
-ATOM  13487  CB  ARG B1094      26.738  15.038 -44.285  1.00 62.88           C  
-ANISOU13487  CB  ARG B1094     9874   7346   6670  -1903   -135    -66       C  
-ATOM  13488  CG  ARG B1094      27.521  14.807 -45.575  1.00 63.92           C  
-ANISOU13488  CG  ARG B1094     9915   7438   6935  -2071    -61   -121       C  
-ATOM  13489  CD  ARG B1094      27.055  13.575 -46.328  1.00 65.52           C  
-ANISOU13489  CD  ARG B1094    10031   7715   7148  -2172     71    -93       C  
-ATOM  13490  NE  ARG B1094      27.168  12.362 -45.526  1.00 69.17           N  
-ANISOU13490  NE  ARG B1094    10442   8187   7652  -2126     83    -85       N  
-ATOM  13491  CZ  ARG B1094      26.148  11.783 -44.904  1.00 70.41           C  
-ANISOU13491  CZ  ARG B1094    10615   8445   7694  -2029     97    -30       C  
-ATOM  13492  NH1 ARG B1094      26.343  10.677 -44.196  1.00 71.31           N  
-ANISOU13492  NH1 ARG B1094    10673   8563   7857  -1986    116    -35       N  
-ATOM  13493  NH2 ARG B1094      24.933  12.309 -44.994  1.00 70.12           N  
-ANISOU13493  NH2 ARG B1094    10642   8500   7500  -1972    101     37       N  
-ATOM  13494  N   LEU B1095      24.720  17.102 -43.678  1.00 61.53           N  
-ANISOU13494  N   LEU B1095     9931   7253   6196  -1700   -141     79       N  
-ATOM  13495  CA  LEU B1095      23.616  18.011 -43.970  1.00 60.40           C  
-ANISOU13495  CA  LEU B1095     9852   7171   5927  -1652    -79    180       C  
-ATOM  13496  C   LEU B1095      23.888  19.445 -43.528  1.00 62.07           C  
-ANISOU13496  C   LEU B1095    10190   7301   6092  -1593   -107    171       C  
-ATOM  13497  O   LEU B1095      23.746  20.380 -44.318  1.00 63.37           O  
-ANISOU13497  O   LEU B1095    10358   7489   6232  -1629    -47    188       O  
-ATOM  13498  CB  LEU B1095      22.318  17.510 -43.340  1.00 56.83           C  
-ANISOU13498  CB  LEU B1095     9437   6788   5369  -1540    -48    298       C  
-ATOM  13499  CG  LEU B1095      21.478  16.638 -44.273  1.00 54.73           C  
-ANISOU13499  CG  LEU B1095     9062   6656   5077  -1616     38    368       C  
-ATOM  13500  CD1 LEU B1095      22.372  15.698 -45.080  1.00 54.90           C  
-ANISOU13500  CD1 LEU B1095     8963   6683   5215  -1772     56    266       C  
-ATOM  13501  CD2 LEU B1095      20.421  15.865 -43.499  1.00 52.84           C  
-ANISOU13501  CD2 LEU B1095     8848   6469   4759  -1500     49    457       C  
-ATOM  13502  N   LYS B1096      24.269  19.626 -42.270  1.00 52.81           N  
-ANISOU13502  N   LYS B1096     9127   6037   4903  -1509   -189    146       N  
-ATOM  13503  CA  LYS B1096      24.462  20.974 -41.754  1.00 54.90           C  
-ANISOU13503  CA  LYS B1096     9541   6221   5098  -1462   -196    145       C  
-ATOM  13504  C   LYS B1096      25.450  21.750 -42.612  1.00 57.09           C  
-ANISOU13504  C   LYS B1096     9782   6467   5441  -1559   -199     49       C  
-ATOM  13505  O   LYS B1096      25.267  22.940 -42.847  1.00 56.90           O  
-ANISOU13505  O   LYS B1096     9835   6434   5350  -1541   -137     69       O  
-ATOM  13506  CB  LYS B1096      24.919  20.966 -40.294  1.00 54.16           C  
-ANISOU13506  CB  LYS B1096     9576   6022   4980  -1401   -297    119       C  
-ATOM  13507  CG  LYS B1096      25.216  22.360 -39.763  1.00 54.60           C  
-ANISOU13507  CG  LYS B1096     9807   5987   4952  -1382   -293    111       C  
-ATOM  13508  CD  LYS B1096      25.464  22.390 -38.263  1.00 55.50           C  
-ANISOU13508  CD  LYS B1096    10081   5995   5010  -1336   -379    111       C  
-ATOM  13509  CE  LYS B1096      25.591  23.837 -37.773  1.00 55.94           C  
-ANISOU13509  CE  LYS B1096    10342   5961   4953  -1331   -336    120       C  
-ATOM  13510  NZ  LYS B1096      25.805  23.959 -36.303  1.00 55.29           N  
-ANISOU13510  NZ  LYS B1096    10451   5763   4794  -1313   -410    127       N  
-ATOM  13511  N   TYR B1097      26.489  21.071 -43.088  1.00 65.99           N  
-ANISOU13511  N   TYR B1097    10793   7572   6707  -1657   -258    -48       N  
-ATOM  13512  CA  TYR B1097      27.523  21.734 -43.881  1.00 69.37           C  
-ANISOU13512  CA  TYR B1097    11189   7949   7221  -1745   -269   -148       C  
-ATOM  13513  C   TYR B1097      27.282  21.657 -45.388  1.00 69.60           C  
-ANISOU13513  C   TYR B1097    11102   8043   7300  -1837   -176   -155       C  
-ATOM  13514  O   TYR B1097      28.130  22.059 -46.183  1.00 69.16           O  
-ANISOU13514  O   TYR B1097    11006   7936   7337  -1916   -177   -244       O  
-ATOM  13515  CB  TYR B1097      28.914  21.222 -43.501  1.00 72.88           C  
-ANISOU13515  CB  TYR B1097    11590   8298   7802  -1803   -383   -236       C  
-ATOM  13516  CG  TYR B1097      29.314  21.678 -42.123  1.00 78.83           C  
-ANISOU13516  CG  TYR B1097    12479   8980   8492  -1744   -484   -236       C  
-ATOM  13517  CD1 TYR B1097      29.920  22.912 -41.929  1.00 81.15           C  
-ANISOU13517  CD1 TYR B1097    12885   9207   8741  -1751   -513   -285       C  
-ATOM  13518  CD2 TYR B1097      29.052  20.893 -41.009  1.00 81.71           C  
-ANISOU13518  CD2 TYR B1097    12872   9344   8829  -1689   -542   -187       C  
-ATOM  13519  CE1 TYR B1097      30.274  23.343 -40.667  1.00 84.28           C  
-ANISOU13519  CE1 TYR B1097    13425   9537   9060  -1725   -600   -278       C  
-ATOM  13520  CE2 TYR B1097      29.401  21.316 -39.742  1.00 84.90           C  
-ANISOU13520  CE2 TYR B1097    13415   9677   9166  -1656   -636   -182       C  
-ATOM  13521  CZ  TYR B1097      30.012  22.542 -39.577  1.00 85.88           C  
-ANISOU13521  CZ  TYR B1097    13659   9735   9238  -1684   -664   -224       C  
-ATOM  13522  OH  TYR B1097      30.362  22.968 -38.316  1.00 89.33           O  
-ANISOU13522  OH  TYR B1097    14251  10098   9591  -1679   -752   -213       O  
-ATOM  13523  N   PHE B1098      26.117  21.140 -45.765  1.00 68.15           N  
-ANISOU13523  N   PHE B1098    10872   7968   7053  -1832    -97    -55       N  
-ATOM  13524  CA  PHE B1098      25.655  21.191 -47.144  1.00 68.45           C  
-ANISOU13524  CA  PHE B1098    10822   8086   7098  -1928     -3    -30       C  
-ATOM  13525  C   PHE B1098      24.654  22.328 -47.266  1.00 69.36           C  
-ANISOU13525  C   PHE B1098    11000   8270   7084  -1858     75     75       C  
-ATOM  13526  O   PHE B1098      24.522  22.946 -48.318  1.00 69.59           O  
-ANISOU13526  O   PHE B1098    10984   8342   7115  -1923    143     79       O  
-ATOM  13527  CB  PHE B1098      25.011  19.862 -47.549  1.00 68.66           C  
-ANISOU13527  CB  PHE B1098    10754   8203   7130  -1994     41     31       C  
-ATOM  13528  CG  PHE B1098      24.129  19.958 -48.763  1.00 67.88           C  
-ANISOU13528  CG  PHE B1098    10593   8220   6980  -2087    140    113       C  
-ATOM  13529  CD1 PHE B1098      24.679  20.046 -50.031  1.00 68.41           C  
-ANISOU13529  CD1 PHE B1098    10593   8268   7131  -2238    180     43       C  
-ATOM  13530  CD2 PHE B1098      22.751  19.952 -48.637  1.00 67.21           C  
-ANISOU13530  CD2 PHE B1098    10517   8256   6765  -2030    193    272       C  
-ATOM  13531  CE1 PHE B1098      23.869  20.134 -51.151  1.00 68.07           C  
-ANISOU13531  CE1 PHE B1098    10495   8335   7033  -2344    264    126       C  
-ATOM  13532  CE2 PHE B1098      21.937  20.036 -49.749  1.00 67.39           C  
-ANISOU13532  CE2 PHE B1098    10473   8397   6737  -2132    275    370       C  
-ATOM  13533  CZ  PHE B1098      22.496  20.128 -51.010  1.00 67.50           C  
-ANISOU13533  CZ  PHE B1098    10422   8401   6825  -2297    308    296       C  
-ATOM  13534  N   ALA B1099      23.957  22.602 -46.170  1.00 74.56           N  
-ANISOU13534  N   ALA B1099    11763   8929   7636  -1727     77    167       N  
-ATOM  13535  CA  ALA B1099      23.004  23.700 -46.125  1.00 75.81           C  
-ANISOU13535  CA  ALA B1099    11996   9129   7680  -1647    175    292       C  
-ATOM  13536  C   ALA B1099      23.732  25.035 -46.209  1.00 76.89           C  
-ANISOU13536  C   ALA B1099    12207   9194   7815  -1638    196    210       C  
-ATOM  13537  O   ALA B1099      23.361  25.906 -46.996  1.00 77.05           O  
-ANISOU13537  O   ALA B1099    12203   9268   7805  -1652    296    256       O  
-ATOM  13538  CB  ALA B1099      22.173  23.630 -44.857  1.00 75.30           C  
-ANISOU13538  CB  ALA B1099    12049   9044   7518  -1511    182    407       C  
-ATOM  13539  N   LYS B1100      24.768  25.194 -45.393  1.00 85.38           N  
-ANISOU13539  N   LYS B1100    13368  10153   8918  -1620    103     95       N  
-ATOM  13540  CA  LYS B1100      25.516  26.441 -45.364  1.00 87.00           C  
-ANISOU13540  CA  LYS B1100    13661  10286   9108  -1614    119     10       C  
-ATOM  13541  C   LYS B1100      26.172  26.666 -46.713  1.00 84.91           C  
-ANISOU13541  C   LYS B1100    13280  10038   8945  -1714    131    -95       C  
-ATOM  13542  O   LYS B1100      26.132  27.768 -47.258  1.00 84.07           O  
-ANISOU13542  O   LYS B1100    13193   9946   8805  -1704    221   -106       O  
-ATOM  13543  CB  LYS B1100      26.573  26.414 -44.260  1.00 91.13           C  
-ANISOU13543  CB  LYS B1100    14289  10690   9646  -1606     -5    -88       C  
-ATOM  13544  CG  LYS B1100      26.095  25.763 -42.972  1.00 97.26           C  
-ANISOU13544  CG  LYS B1100    15152  11440  10361  -1536    -55    -10       C  
-ATOM  13545  CD  LYS B1100      26.745  26.378 -41.746  1.00101.32           C  
-ANISOU13545  CD  LYS B1100    15847  11841  10810  -1513   -118    -51       C  
-ATOM  13546  CE  LYS B1100      26.228  27.788 -41.511  1.00104.39           C  
-ANISOU13546  CE  LYS B1100    16400  12204  11060  -1456     22      9       C  
-ATOM  13547  NZ  LYS B1100      26.590  28.299 -40.159  1.00106.82           N  
-ANISOU13547  NZ  LYS B1100    16923  12397  11267  -1441    -14      2       N  
-ATOM  13548  N   LEU B1101      26.754  25.600 -47.255  1.00 80.09           N  
-ANISOU13548  N   LEU B1101    12551   9418   8463  -1810     58   -167       N  
-ATOM  13549  CA  LEU B1101      27.515  25.675 -48.497  1.00 77.38           C  
-ANISOU13549  CA  LEU B1101    12111   9050   8241  -1918     63   -278       C  
-ATOM  13550  C   LEU B1101      26.647  25.993 -49.708  1.00 76.63           C  
-ANISOU13550  C   LEU B1101    11937   9064   8115  -1966    180   -209       C  
-ATOM  13551  O   LEU B1101      27.125  26.560 -50.687  1.00 76.50           O  
-ANISOU13551  O   LEU B1101    11880   9027   8161  -2027    213   -295       O  
-ATOM  13552  CB  LEU B1101      28.263  24.366 -48.737  1.00 76.14           C  
-ANISOU13552  CB  LEU B1101    11858   8839   8231  -2016    -13   -344       C  
-ATOM  13553  CG  LEU B1101      29.264  24.392 -49.887  1.00 74.08           C  
-ANISOU13553  CG  LEU B1101    11523   8500   8123  -2131    -13   -469       C  
-ATOM  13554  CD1 LEU B1101      30.151  25.614 -49.779  1.00 74.52           C  
-ANISOU13554  CD1 LEU B1101    11653   8468   8194  -2088    -44   -576       C  
-ATOM  13555  CD2 LEU B1101      30.094  23.130 -49.880  1.00 74.63           C  
-ANISOU13555  CD2 LEU B1101    11522   8486   8347  -2215    -71   -513       C  
-ATOM  13556  N   TRP B1102      25.372  25.627 -49.646  1.00 68.38           N  
-ANISOU13556  N   TRP B1102    10869   8134   6977  -1943    240    -49       N  
-ATOM  13557  CA  TRP B1102      24.484  25.846 -50.780  1.00 67.22           C  
-ANISOU13557  CA  TRP B1102    10635   8108   6796  -2008    343     50       C  
-ATOM  13558  C   TRP B1102      24.265  27.331 -51.050  1.00 67.46           C  
-ANISOU13558  C   TRP B1102    10704   8162   6766  -1947    441     75       C  
-ATOM  13559  O   TRP B1102      23.922  27.720 -52.163  1.00 68.18           O  
-ANISOU13559  O   TRP B1102    10712   8330   6865  -2018    517    108       O  
-ATOM  13560  CB  TRP B1102      23.145  25.138 -50.577  1.00 66.53           C  
-ANISOU13560  CB  TRP B1102    10516   8142   6619  -1993    381    240       C  
-ATOM  13561  CG  TRP B1102      22.393  24.926 -51.858  1.00 65.04           C  
-ANISOU13561  CG  TRP B1102    10210   8083   6419  -2122    453    337       C  
-ATOM  13562  CD1 TRP B1102      21.229  25.526 -52.235  1.00 63.90           C  
-ANISOU13562  CD1 TRP B1102    10031   8065   6182  -2105    552    523       C  
-ATOM  13563  CD2 TRP B1102      22.764  24.056 -52.937  1.00 64.16           C  
-ANISOU13563  CD2 TRP B1102    10006   7982   6391  -2304    437    268       C  
-ATOM  13564  NE1 TRP B1102      20.845  25.077 -53.477  1.00 62.77           N  
-ANISOU13564  NE1 TRP B1102     9774   8024   6050  -2274    582    575       N  
-ATOM  13565  CE2 TRP B1102      21.773  24.176 -53.929  1.00 63.08           C  
-ANISOU13565  CE2 TRP B1102     9788   7988   6192  -2403    518    413       C  
-ATOM  13566  CE3 TRP B1102      23.836  23.188 -53.158  1.00 65.49           C  
-ANISOU13566  CE3 TRP B1102    10157   8044   6683  -2402    377    112       C  
-ATOM  13567  CZ2 TRP B1102      21.823  23.461 -55.125  1.00 63.40           C  
-ANISOU13567  CZ2 TRP B1102     9748   8067   6276  -2610    534    394       C  
-ATOM  13568  CZ3 TRP B1102      23.883  22.478 -54.347  1.00 66.06           C  
-ANISOU13568  CZ3 TRP B1102    10152   8139   6808  -2596    413     95       C  
-ATOM  13569  CH2 TRP B1102      22.883  22.618 -55.313  1.00 64.57           C  
-ANISOU13569  CH2 TRP B1102     9901   8092   6540  -2705    488    229       C  
-ATOM  13570  N   THR B1103      24.468  28.157 -50.029  1.00 64.76           N  
-ANISOU13570  N   THR B1103    10492   7753   6360  -1824    451     63       N  
-ATOM  13571  CA  THR B1103      24.322  29.601 -50.181  1.00 64.26           C  
-ANISOU13571  CA  THR B1103    10482   7700   6232  -1758    571     81       C  
-ATOM  13572  C   THR B1103      25.657  30.331 -50.041  1.00 65.43           C  
-ANISOU13572  C   THR B1103    10705   7728   6428  -1748    526   -118       C  
-ATOM  13573  O   THR B1103      25.711  31.465 -49.567  1.00 64.95           O  
-ANISOU13573  O   THR B1103    10756   7638   6285  -1665    609   -120       O  
-ATOM  13574  CB  THR B1103      23.311  30.178 -49.176  1.00 63.83           C  
-ANISOU13574  CB  THR B1103    10542   7667   6042  -1628    676    260       C  
-ATOM  13575  OG1 THR B1103      23.801  30.003 -47.839  1.00 63.77           O  
-ANISOU13575  OG1 THR B1103    10681   7546   6004  -1565    594    206       O  
-ATOM  13576  CG2 THR B1103      21.973  29.477 -49.318  1.00 61.24           C  
-ANISOU13576  CG2 THR B1103    10138   7457   5674  -1631    719    471       C  
-ATOM  13577  N   MET B1104      26.732  29.669 -50.454  1.00 68.59           N  
-ANISOU13577  N   MET B1104    11048   8052   6960  -1838    406   -275       N  
-ATOM  13578  CA  MET B1104      28.043  30.301 -50.510  1.00 70.32           C  
-ANISOU13578  CA  MET B1104    11314   8156   7248  -1843    355   -459       C  
-ATOM  13579  C   MET B1104      28.425  30.538 -51.973  1.00 71.95           C  
-ANISOU13579  C   MET B1104    11412   8365   7561  -1928    390   -558       C  
-ATOM  13580  O   MET B1104      28.426  29.608 -52.786  1.00 69.80           O  
-ANISOU13580  O   MET B1104    11033   8101   7387  -2039    359   -564       O  
-ATOM  13581  CB  MET B1104      29.097  29.422 -49.840  1.00 70.95           C  
-ANISOU13581  CB  MET B1104    11414   8122   7421  -1877    195   -552       C  
-ATOM  13582  CG  MET B1104      28.719  28.894 -48.468  1.00 72.57           C  
-ANISOU13582  CG  MET B1104    11704   8325   7544  -1817    139   -457       C  
-ATOM  13583  SD  MET B1104      28.934  30.079 -47.121  1.00 75.02           S  
-ANISOU13583  SD  MET B1104    12225   8572   7706  -1717    155   -459       S  
-ATOM  13584  CE  MET B1104      27.234  30.467 -46.707  1.00 74.10           C  
-ANISOU13584  CE  MET B1104    12176   8555   7423  -1620    318   -248       C  
-ATOM  13585  N   HIS B1105      28.745  31.786 -52.303  1.00 70.23           N  
-ANISOU13585  N   HIS B1105    11233   8133   7319  -1882    467   -637       N  
-ATOM  13586  CA  HIS B1105      29.110  32.149 -53.666  1.00 72.23           C  
-ANISOU13586  CA  HIS B1105    11395   8378   7670  -1949    508   -742       C  
-ATOM  13587  C   HIS B1105      30.502  32.760 -53.687  1.00 74.43           C  
-ANISOU13587  C   HIS B1105    11731   8517   8031  -1932    450   -947       C  
-ATOM  13588  O   HIS B1105      31.384  32.311 -54.416  1.00 72.83           O  
-ANISOU13588  O   HIS B1105    11471   8212   7988  -2015    378  -1074       O  
-ATOM  13589  CB  HIS B1105      28.097  33.140 -54.230  1.00 71.65           C  
-ANISOU13589  CB  HIS B1105    11289   8438   7498  -1906    678   -637       C  
-ATOM  13590  CG  HIS B1105      26.688  32.850 -53.823  1.00 72.59           C  
-ANISOU13590  CG  HIS B1105    11391   8689   7499  -1878    750   -400       C  
-ATOM  13591  ND1 HIS B1105      26.172  33.234 -52.603  1.00 73.35           N  
-ANISOU13591  ND1 HIS B1105    11606   8797   7468  -1764    802   -287       N  
-ATOM  13592  CD2 HIS B1105      25.690  32.199 -54.465  1.00 73.96           C  
-ANISOU13592  CD2 HIS B1105    11453   8982   7667  -1958    780   -247       C  
-ATOM  13593  CE1 HIS B1105      24.914  32.841 -52.516  1.00 74.66           C  
-ANISOU13593  CE1 HIS B1105    11727   9075   7567  -1758    862    -74       C  
-ATOM  13594  NE2 HIS B1105      24.597  32.209 -53.633  1.00 74.76           N  
-ANISOU13594  NE2 HIS B1105    11596   9164   7647  -1876    845    -43       N  
-ATOM  13595  N   ASN B1106      30.692  33.788 -52.871  1.00 94.48           N  
-ANISOU13595  N   ASN B1106    14393  11043  10461  -1828    492   -970       N  
-ATOM  13596  CA  ASN B1106      31.973  34.466 -52.784  1.00 98.09           C  
-ANISOU13596  CA  ASN B1106    14920  11379  10970  -1806    441  -1153       C  
-ATOM  13597  C   ASN B1106      33.077  33.510 -52.355  1.00102.61           C  
-ANISOU13597  C   ASN B1106    15494  11819  11673  -1868    257  -1228       C  
-ATOM  13598  O   ASN B1106      32.807  32.380 -51.951  1.00102.81           O  
-ANISOU13598  O   ASN B1106    15484  11853  11727  -1913    183  -1135       O  
-ATOM  13599  CB  ASN B1106      31.881  35.634 -51.806  1.00 97.10           C  
-ANISOU13599  CB  ASN B1106    14952  11271  10670  -1703    528  -1138       C  
-ATOM  13600  CG  ASN B1106      30.636  36.474 -52.018  1.00 95.85           C  
-ANISOU13600  CG  ASN B1106    14795  11246  10376  -1634    737  -1007       C  
-ATOM  13601  OD1 ASN B1106      30.659  37.467 -52.744  1.00 96.42           O  
-ANISOU13601  OD1 ASN B1106    14848  11350  10438  -1597    864  -1071       O  
-ATOM  13602  ND2 ASN B1106      29.539  36.074 -51.385  1.00 94.45           N  
-ANISOU13602  ND2 ASN B1106    14638  11145  10104  -1611    782   -812       N  
-ATOM  13603  N   ALA B1107      34.320  33.964 -52.447  1.00100.90           N  
-ANISOU13603  N   ALA B1107    15315  11482  11542  -1869    192  -1386       N  
-ATOM  13604  CA  ALA B1107      35.452  33.139 -52.055  1.00107.39           C  
-ANISOU13604  CA  ALA B1107    16129  12171  12505  -1929     24  -1437       C  
-ATOM  13605  C   ALA B1107      35.673  33.171 -50.544  1.00111.78           C  
-ANISOU13605  C   ALA B1107    16807  12720  12946  -1897    -60  -1378       C  
-ATOM  13606  O   ALA B1107      36.238  32.237 -49.976  1.00113.17           O  
-ANISOU13606  O   ALA B1107    16962  12830  13209  -1949   -194  -1347       O  
-ATOM  13607  CB  ALA B1107      36.708  33.571 -52.793  1.00107.09           C  
-ANISOU13607  CB  ALA B1107    16073  11993  12622  -1947    -17  -1612       C  
-ATOM  13608  N   GLN B1108      35.229  34.243 -49.893  1.00124.55           N  
-ANISOU13608  N   GLN B1108    18557  14400  14367  -1822     30  -1355       N  
-ATOM  13609  CA  GLN B1108      35.360  34.338 -48.442  1.00128.65           C  
-ANISOU13609  CA  GLN B1108    19221  14908  14754  -1811    -34  -1293       C  
-ATOM  13610  C   GLN B1108      34.212  33.595 -47.773  1.00127.50           C  
-ANISOU13610  C   GLN B1108    19081  14842  14523  -1796    -14  -1124       C  
-ATOM  13611  O   GLN B1108      34.315  33.186 -46.617  1.00128.10           O  
-ANISOU13611  O   GLN B1108    19240  14893  14540  -1809   -106  -1060       O  
-ATOM  13612  CB  GLN B1108      35.400  35.793 -47.971  1.00136.27           C  
-ANISOU13612  CB  GLN B1108    20356  15886  15536  -1753     76  -1337       C  
-ATOM  13613  CG  GLN B1108      34.039  36.384 -47.662  1.00147.08           C  
-ANISOU13613  CG  GLN B1108    21806  17359  16718  -1681    268  -1211       C  
-ATOM  13614  CD  GLN B1108      33.174  36.503 -48.893  1.00152.38           C  
-ANISOU13614  CD  GLN B1108    22341  18122  17436  -1646    409  -1184       C  
-ATOM  13615  OE1 GLN B1108      33.674  36.737 -49.994  1.00155.75           O  
-ANISOU13615  OE1 GLN B1108    22669  18529  17979  -1658    417  -1307       O  
-ATOM  13616  NE2 GLN B1108      31.867  36.336 -48.718  1.00155.45           N  
-ANISOU13616  NE2 GLN B1108    22723  18605  17736  -1609    520  -1015       N  
-ATOM  13617  N   ASP B1109      33.114  33.430 -48.503  1.00111.22           N  
-ANISOU13617  N   ASP B1109    16931  12875  12451  -1773    103  -1048       N  
-ATOM  13618  CA  ASP B1109      32.032  32.576 -48.040  1.00109.45           C  
-ANISOU13618  CA  ASP B1109    16685  12724  12177  -1762    114   -888       C  
-ATOM  13619  C   ASP B1109      32.616  31.210 -47.700  1.00107.38           C  
-ANISOU13619  C   ASP B1109    16351  12403  12044  -1830    -55   -888       C  
-ATOM  13620  O   ASP B1109      32.296  30.623 -46.669  1.00109.91           O  
-ANISOU13620  O   ASP B1109    16724  12730  12306  -1816   -112   -797       O  
-ATOM  13621  CB  ASP B1109      30.946  32.436 -49.110  1.00110.32           C  
-ANISOU13621  CB  ASP B1109    16674  12944  12300  -1760    237   -810       C  
-ATOM  13622  CG  ASP B1109      29.950  33.579 -49.085  1.00111.98           C  
-ANISOU13622  CG  ASP B1109    16955  13240  12351  -1675    427   -718       C  
-ATOM  13623  OD1 ASP B1109      29.913  34.316 -48.077  1.00112.71           O  
-ANISOU13623  OD1 ASP B1109    17211  13304  12308  -1616    477   -691       O  
-ATOM  13624  OD2 ASP B1109      29.195  33.733 -50.067  1.00110.63           O  
-ANISOU13624  OD2 ASP B1109    16681  13163  12192  -1679    537   -660       O  
-ATOM  13625  N   LEU B1110      33.482  30.716 -48.578  1.00 92.47           N  
-ANISOU13625  N   LEU B1110    14345  10448  10341  -1902   -122   -987       N  
-ATOM  13626  CA  LEU B1110      34.178  29.458 -48.349  1.00 90.29           C  
-ANISOU13626  CA  LEU B1110    13991  10100  10215  -1972   -256   -984       C  
-ATOM  13627  C   LEU B1110      35.181  29.600 -47.214  1.00 91.71           C  
-ANISOU13627  C   LEU B1110    14263  10196  10386  -1976   -389  -1008       C  
-ATOM  13628  O   LEU B1110      35.426  28.654 -46.467  1.00 93.56           O  
-ANISOU13628  O   LEU B1110    14473  10407  10667  -2006   -492   -947       O  
-ATOM  13629  CB  LEU B1110      34.897  29.013 -49.622  1.00 82.32           C  
-ANISOU13629  CB  LEU B1110    12853   9012   9414  -2054   -262  -1076       C  
-ATOM  13630  CG  LEU B1110      34.222  27.920 -50.449  1.00 76.24           C  
-ANISOU13630  CG  LEU B1110    11959   8288   8720  -2122   -206  -1017       C  
-ATOM  13631  CD1 LEU B1110      32.711  28.093 -50.450  1.00 70.96           C  
-ANISOU13631  CD1 LEU B1110    11304   7777   7882  -2074    -99   -903       C  
-ATOM  13632  CD2 LEU B1110      34.778  27.914 -51.866  1.00 70.58           C  
-ANISOU13632  CD2 LEU B1110    11160   7487   8169  -2204   -163  -1120       C  
-ATOM  13633  N   GLN B1111      35.767  30.785 -47.095  1.00 96.55           N  
-ANISOU13633  N   GLN B1111    14979  10769  10936  -1954   -384  -1093       N  
-ATOM  13634  CA  GLN B1111      36.746  31.040 -46.049  1.00 97.28           C  
-ANISOU13634  CA  GLN B1111    15172  10789  11000  -1980   -511  -1111       C  
-ATOM  13635  C   GLN B1111      36.119  30.826 -44.675  1.00 98.32           C  
-ANISOU13635  C   GLN B1111    15420  10966  10970  -1961   -540   -992       C  
-ATOM  13636  O   GLN B1111      36.711  30.189 -43.807  1.00 97.95           O  
-ANISOU13636  O   GLN B1111    15380  10876  10961  -2010   -680   -950       O  
-ATOM  13637  CB  GLN B1111      37.310  32.450 -46.175  1.00 95.81           C  
-ANISOU13637  CB  GLN B1111    15099  10571  10734  -1959   -469  -1221       C  
-ATOM  13638  N   LYS B1112      34.912  31.350 -44.491  1.00110.01           N  
-ANISOU13638  N   LYS B1112    16990  12527  12280  -1890   -400   -929       N  
-ATOM  13639  CA  LYS B1112      34.193  31.215 -43.230  1.00111.48           C  
-ANISOU13639  CA  LYS B1112    17308  12737  12311  -1863   -399   -814       C  
-ATOM  13640  C   LYS B1112      33.601  29.817 -43.079  1.00110.74           C  
-ANISOU13640  C   LYS B1112    17100  12681  12294  -1859   -449   -721       C  
-ATOM  13641  O   LYS B1112      33.603  29.242 -41.990  1.00112.76           O  
-ANISOU13641  O   LYS B1112    17413  12917  12514  -1869   -540   -656       O  
-ATOM  13642  CB  LYS B1112      33.081  32.263 -43.137  1.00115.78           C  
-ANISOU13642  CB  LYS B1112    17988  13335  12667  -1784   -205   -759       C  
-ATOM  13643  CG  LYS B1112      33.561  33.700 -43.276  1.00121.59           C  
-ANISOU13643  CG  LYS B1112    18848  14044  13305  -1780   -115   -849       C  
-ATOM  13644  CD  LYS B1112      32.403  34.679 -43.168  1.00126.43           C  
-ANISOU13644  CD  LYS B1112    19588  14708  13742  -1700    112   -767       C  
-ATOM  13645  CE  LYS B1112      32.880  36.120 -43.235  1.00129.14           C  
-ANISOU13645  CE  LYS B1112    20068  15026  13974  -1696    229   -857       C  
-ATOM  13646  NZ  LYS B1112      33.501  36.438 -44.548  1.00130.35           N  
-ANISOU13646  NZ  LYS B1112    20075  15195  14257  -1693    235   -995       N  
-ATOM  13647  N   TRP B1113      33.090  29.276 -44.179  1.00 99.32           N  
-ANISOU13647  N   TRP B1113    15500  11291  10947  -1851   -383   -716       N  
-ATOM  13648  CA  TRP B1113      32.470  27.957 -44.164  1.00 99.08           C  
-ANISOU13648  CA  TRP B1113    15359  11308  10979  -1851   -404   -633       C  
-ATOM  13649  C   TRP B1113      33.437  26.886 -43.669  1.00101.40           C  
-ANISOU13649  C   TRP B1113    15579  11538  11410  -1915   -559   -643       C  
-ATOM  13650  O   TRP B1113      33.115  26.124 -42.760  1.00103.43           O  
-ANISOU13650  O   TRP B1113    15852  11809  11638  -1898   -614   -567       O  
-ATOM  13651  CB  TRP B1113      31.949  27.597 -45.554  1.00 91.32           C  
-ANISOU13651  CB  TRP B1113    14227  10388  10083  -1871   -309   -637       C  
-ATOM  13652  CG  TRP B1113      31.328  26.242 -45.629  1.00 83.43           C  
-ANISOU13652  CG  TRP B1113    13119   9443   9138  -1887   -314   -558       C  
-ATOM  13653  CD1 TRP B1113      30.090  25.881 -45.180  1.00 80.13           C  
-ANISOU13653  CD1 TRP B1113    12727   9109   8609  -1825   -259   -438       C  
-ATOM  13654  CD2 TRP B1113      31.908  25.062 -46.198  1.00 78.78           C  
-ANISOU13654  CD2 TRP B1113    12384   8822   8726  -1972   -361   -587       C  
-ATOM  13655  NE1 TRP B1113      29.865  24.549 -45.430  1.00 75.57           N  
-ANISOU13655  NE1 TRP B1113    12028   8567   8118  -1865   -276   -403       N  
-ATOM  13656  CE2 TRP B1113      30.966  24.023 -46.054  1.00 75.91           C  
-ANISOU13656  CE2 TRP B1113    11967   8540   8335  -1960   -328   -491       C  
-ATOM  13657  CE3 TRP B1113      33.132  24.784 -46.813  1.00 76.32           C  
-ANISOU13657  CE3 TRP B1113    11990   8411   8599  -2057   -412   -678       C  
-ATOM  13658  CZ2 TRP B1113      31.212  22.726 -46.501  1.00 73.36           C  
-ANISOU13658  CZ2 TRP B1113    11514   8209   8149  -2038   -332   -489       C  
-ATOM  13659  CZ3 TRP B1113      33.373  23.499 -47.258  1.00 74.88           C  
-ANISOU13659  CZ3 TRP B1113    11680   8206   8566  -2134   -410   -663       C  
-ATOM  13660  CH2 TRP B1113      32.418  22.485 -47.099  1.00 73.70           C  
-ANISOU13660  CH2 TRP B1113    11484   8148   8372  -2127   -364   -573       C  
-ATOM  13661  N   THR B1114      34.623  26.834 -44.266  1.00102.81           N  
-ANISOU13661  N   THR B1114    15675  11640  11748  -1985   -623   -730       N  
-ATOM  13662  CA  THR B1114      35.624  25.843 -43.883  1.00104.58           C  
-ANISOU13662  CA  THR B1114    15809  11795  12131  -2051   -753   -718       C  
-ATOM  13663  C   THR B1114      36.100  26.026 -42.442  1.00106.67           C  
-ANISOU13663  C   THR B1114    16191  12028  12309  -2058   -881   -677       C  
-ATOM  13664  O   THR B1114      36.813  25.179 -41.905  1.00106.03           O  
-ANISOU13664  O   THR B1114    16038  11908  12339  -2108   -994   -634       O  
-ATOM  13665  CB  THR B1114      36.837  25.859 -44.839  1.00104.70           C  
-ANISOU13665  CB  THR B1114    15723  11710  12348  -2123   -782   -805       C  
-ATOM  13666  OG1 THR B1114      37.280  27.208 -45.034  1.00104.86           O  
-ANISOU13666  OG1 THR B1114    15844  11696  12302  -2110   -776   -895       O  
-ATOM  13667  CG2 THR B1114      36.458  25.266 -46.185  1.00103.17           C  
-ANISOU13667  CG2 THR B1114    15399  11526  12274  -2152   -670   -828       C  
-ATOM  13668  N   GLU B1115      35.701  27.132 -41.820  1.00112.52           N  
-ANISOU13668  N   GLU B1115    17116  12786  12852  -2019   -850   -679       N  
-ATOM  13669  CA  GLU B1115      36.084  27.413 -40.440  1.00116.58           C  
-ANISOU13669  CA  GLU B1115    17779  13265  13252  -2048   -958   -638       C  
-ATOM  13670  C   GLU B1115      35.231  26.613 -39.463  1.00120.74           C  
-ANISOU13670  C   GLU B1115    18341  13830  13705  -2008   -974   -536       C  
-ATOM  13671  O   GLU B1115      35.754  25.921 -38.589  1.00122.18           O  
-ANISOU13671  O   GLU B1115    18507  13987  13930  -2055  -1105   -487       O  
-ATOM  13672  CB  GLU B1115      35.973  28.909 -40.140  1.00116.33           C  
-ANISOU13672  CB  GLU B1115    17956  13220  13024  -2036   -890   -677       C  
-ATOM  13673  CG  GLU B1115      36.485  29.309 -38.767  1.00118.83           C  
-ANISOU13673  CG  GLU B1115    18454  13488  13208  -2103   -997   -642       C  
-ATOM  13674  CD  GLU B1115      35.413  29.958 -37.911  1.00119.48           C  
-ANISOU13674  CD  GLU B1115    18761  13579  13057  -2056   -886   -583       C  
-ATOM  13675  OE1 GLU B1115      34.235  29.955 -38.329  1.00118.99           O  
-ANISOU13675  OE1 GLU B1115    18689  13566  12955  -1959   -737   -549       O  
-ATOM  13676  OE2 GLU B1115      35.748  30.474 -36.823  1.00119.77           O  
-ANISOU13676  OE2 GLU B1115    18990  13565  12951  -2125   -941   -559       O  
-ATOM  13677  N   GLU B1116      33.914  26.711 -39.611  1.00118.95           N  
-ANISOU13677  N   GLU B1116    18160  13663  13372  -1920   -839   -497       N  
-ATOM  13678  CA  GLU B1116      33.005  25.926 -38.789  1.00125.26           C  
-ANISOU13678  CA  GLU B1116    18988  14492  14112  -1865   -839   -404       C  
-ATOM  13679  C   GLU B1116      33.232  24.445 -39.045  1.00131.18           C  
-ANISOU13679  C   GLU B1116    19532  15269  15040  -1882   -902   -387       C  
-ATOM  13680  O   GLU B1116      33.060  23.618 -38.152  1.00132.82           O  
-ANISOU13680  O   GLU B1116    19739  15481  15246  -1867   -969   -328       O  
-ATOM  13681  CB  GLU B1116      31.554  26.278 -39.108  1.00120.78           C  
-ANISOU13681  CB  GLU B1116    18478  13984  13428  -1766   -671   -351       C  
-ATOM  13682  CG  GLU B1116      31.257  27.761 -39.103  1.00115.82           C  
-ANISOU13682  CG  GLU B1116    18028  13335  12644  -1742   -552   -358       C  
-ATOM  13683  CD  GLU B1116      29.792  28.051 -39.353  1.00111.33           C  
-ANISOU13683  CD  GLU B1116    17502  12821  11977  -1643   -377   -266       C  
-ATOM  13684  OE1 GLU B1116      29.449  29.227 -39.600  1.00108.77           O  
-ANISOU13684  OE1 GLU B1116    17284  12495  11549  -1616   -238   -258       O  
-ATOM  13685  OE2 GLU B1116      28.985  27.098 -39.298  1.00107.44           O  
-ANISOU13685  OE2 GLU B1116    16934  12376  11513  -1593   -370   -192       O  
-ATOM  13686  N   PHE B1117      33.622  24.117 -40.272  1.00135.36           N  
-ANISOU13686  N   PHE B1117    19896  15812  15724  -1918   -867   -437       N  
-ATOM  13687  CA  PHE B1117      33.815  22.728 -40.676  1.00140.90           C  
-ANISOU13687  CA  PHE B1117    20408  16531  16598  -1946   -881   -418       C  
-ATOM  13688  C   PHE B1117      34.935  22.030 -39.906  1.00145.90           C  
-ANISOU13688  C   PHE B1117    20978  17106  17350  -2009  -1024   -392       C  
-ATOM  13689  O   PHE B1117      34.676  21.136 -39.100  1.00147.52           O  
-ANISOU13689  O   PHE B1117    21158  17338  17556  -1985  -1064   -330       O  
-ATOM  13690  CB  PHE B1117      34.071  22.634 -42.181  1.00141.62           C  
-ANISOU13690  CB  PHE B1117    20365  16619  16827  -1995   -797   -478       C  
-ATOM  13691  CG  PHE B1117      34.435  21.255 -42.645  1.00141.20           C  
-ANISOU13691  CG  PHE B1117    20133  16556  16960  -2050   -786   -459       C  
-ATOM  13692  CD1 PHE B1117      33.475  20.260 -42.721  1.00140.47           C  
-ANISOU13692  CD1 PHE B1117    19978  16545  16848  -2019   -709   -405       C  
-ATOM  13693  CD2 PHE B1117      35.737  20.953 -43.003  1.00141.76           C  
-ANISOU13693  CD2 PHE B1117    20104  16532  17228  -2135   -837   -485       C  
-ATOM  13694  CE1 PHE B1117      33.807  18.989 -43.144  1.00140.63           C  
-ANISOU13694  CE1 PHE B1117    19847  16556  17029  -2078   -670   -386       C  
-ATOM  13695  CE2 PHE B1117      36.076  19.684 -43.428  1.00142.27           C  
-ANISOU13695  CE2 PHE B1117    20013  16572  17470  -2191   -793   -452       C  
-ATOM  13696  CZ  PHE B1117      35.110  18.701 -43.498  1.00141.59           C  
-ANISOU13696  CZ  PHE B1117    19874  16573  17351  -2166   -702   -407       C  
-ATOM  13697  N   ASN B1118      36.176  22.435 -40.159  1.00141.29           N  
-ANISOU13697  N   ASN B1118    20364  16447  16874  -2088  -1097   -433       N  
-ATOM  13698  CA  ASN B1118      37.327  21.820 -39.502  1.00145.59           C  
-ANISOU13698  CA  ASN B1118    20829  16936  17551  -2161  -1233   -382       C  
-ATOM  13699  C   ASN B1118      37.270  21.953 -37.980  1.00144.01           C  
-ANISOU13699  C   ASN B1118    20763  16745  17211  -2159  -1350   -320       C  
-ATOM  13700  O   ASN B1118      38.057  21.336 -37.261  1.00144.05           O  
-ANISOU13700  O   ASN B1118    20699  16726  17306  -2218  -1469   -252       O  
-ATOM  13701  CB  ASN B1118      38.638  22.398 -40.044  1.00151.12           C  
-ANISOU13701  CB  ASN B1118    21493  17546  18381  -2243  -1291   -425       C  
-ATOM  13702  CG  ASN B1118      38.843  23.849 -39.654  1.00159.37           C  
-ANISOU13702  CG  ASN B1118    22726  18570  19256  -2252  -1341   -476       C  
-ATOM  13703  OD1 ASN B1118      37.884  24.603 -39.499  1.00162.81           O  
-ANISOU13703  OD1 ASN B1118    23313  19053  19496  -2189  -1265   -505       O  
-ATOM  13704  ND2 ASN B1118      40.100  24.245 -39.492  1.00163.92           N  
-ANISOU13704  ND2 ASN B1118    23299  19073  19909  -2335  -1456   -476       N  
-ATOM  13705  N   MET B1119      36.331  22.765 -37.503  1.00143.21           N  
-ANISOU13705  N   MET B1119    20853  16670  16891  -2099  -1306   -333       N  
-ATOM  13706  CA  MET B1119      36.095  22.943 -36.075  1.00138.64           C  
-ANISOU13706  CA  MET B1119    20440  16082  16155  -2100  -1390   -278       C  
-ATOM  13707  C   MET B1119      35.242  21.799 -35.534  1.00135.30           C  
-ANISOU13707  C   MET B1119    19967  15707  15735  -2026  -1371   -218       C  
-ATOM  13708  O   MET B1119      35.709  20.987 -34.737  1.00132.94           O  
-ANISOU13708  O   MET B1119    19605  15404  15504  -2061  -1479   -161       O  
-ATOM  13709  CB  MET B1119      35.394  24.281 -35.824  1.00137.01           C  
-ANISOU13709  CB  MET B1119    20476  15861  15722  -2066  -1311   -306       C  
-ATOM  13710  CG  MET B1119      35.146  24.617 -34.358  1.00138.62           C  
-ANISOU13710  CG  MET B1119    20899  16024  15745  -2086  -1374   -251       C  
-ATOM  13711  SD  MET B1119      36.593  25.291 -33.520  1.00134.37           S  
-ANISOU13711  SD  MET B1119    20469  15419  15166  -2254  -1551   -243       S  
-ATOM  13712  CE  MET B1119      35.850  25.933 -32.021  1.00123.50           C  
-ANISOU13712  CE  MET B1119    19419  13985  13519  -2271  -1541   -191       C  
-ATOM  13713  N   GLU B1120      33.990  21.736 -35.977  1.00141.93           N  
-ANISOU13713  N   GLU B1120    20827  16597  16503  -1923  -1234   -226       N  
-ATOM  13714  CA  GLU B1120      33.069  20.701 -35.518  1.00140.07           C  
-ANISOU13714  CA  GLU B1120    20554  16409  16256  -1838  -1203   -176       C  
-ATOM  13715  C   GLU B1120      33.446  19.334 -36.078  1.00139.70           C  
-ANISOU13715  C   GLU B1120    20264  16405  16410  -1854  -1195   -168       C  
-ATOM  13716  O   GLU B1120      33.683  18.385 -35.331  1.00143.34           O  
-ANISOU13716  O   GLU B1120    20654  16873  16934  -1854  -1263   -123       O  
-ATOM  13717  CB  GLU B1120      31.632  21.050 -35.911  1.00131.93           C  
-ANISOU13717  CB  GLU B1120    19606  15421  15099  -1731  -1053   -167       C  
-ATOM  13718  CG  GLU B1120      30.594  20.034 -35.460  1.00125.25           C  
-ANISOU13718  CG  GLU B1120    18735  14623  14232  -1632  -1015   -116       C  
-ATOM  13719  CD  GLU B1120      29.179  20.449 -35.820  1.00119.04           C  
-ANISOU13719  CD  GLU B1120    18033  13873  13322  -1531   -872    -79       C  
-ATOM  13720  OE1 GLU B1120      28.998  21.589 -36.301  1.00114.07           O  
-ANISOU13720  OE1 GLU B1120    17495  13230  12615  -1538   -799    -86       O  
-ATOM  13721  OE2 GLU B1120      28.248  19.638 -35.625  1.00112.66           O  
-ANISOU13721  OE2 GLU B1120    17195  13111  12500  -1445   -827    -35       O  
-TER   13722      GLU B1120                                                      
-ATOM  13723  O5'  DT D   3     -19.583 -11.687  72.118  1.00239.19           O  
-ANISOU13723  O5'  DT D   3    32139  26595  32146   8508  -1510  10082       O  
-ATOM  13724  C5'  DT D   3     -18.299 -11.766  71.512  1.00239.91           C  
-ANISOU13724  C5'  DT D   3    32178  26684  32293   8510  -1457   9700       C  
-ATOM  13725  C4'  DT D   3     -17.762 -10.382  71.194  1.00240.12           C  
-ANISOU13725  C4'  DT D   3    32231  26714  32288   8428   -995   9465       C  
-ATOM  13726  O4'  DT D   3     -16.389 -10.501  70.738  1.00240.91           O  
-ANISOU13726  O4'  DT D   3    32259  26829  32448   8428   -959   9064       O  
-ATOM  13727  C3'  DT D   3     -18.502  -9.643  70.082  1.00239.51           C  
-ANISOU13727  C3'  DT D   3    32322  26511  32170   8413   -730   9615       C  
-ATOM  13728  O3'  DT D   3     -18.456  -8.231  70.294  1.00239.47           O  
-ANISOU13728  O3'  DT D   3    32339  26539  32109   8326   -305   9533       O  
-ATOM  13729  C2'  DT D   3     -17.697 -10.039  68.851  1.00239.91           C  
-ANISOU13729  C2'  DT D   3    32397  26478  32279   8451   -756   9373       C  
-ATOM  13730  C1'  DT D   3     -16.281 -10.006  69.417  1.00240.82           C  
-ANISOU13730  C1'  DT D   3    32359  26704  32436   8423   -729   8976       C  
-ATOM  13731  N1   DT D   3     -15.303 -10.844  68.654  1.00241.39           N  
-ANISOU13731  N1   DT D   3    32393  26740  32586   8476   -911   8719       N  
-ATOM  13732  C2   DT D   3     -13.952 -10.666  68.863  1.00242.22           C  
-ANISOU13732  C2   DT D   3    32383  26922  32729   8447   -822   8325       C  
-ATOM  13733  O2   DT D   3     -13.496  -9.855  69.648  1.00242.52           O  
-ANISOU13733  O2   DT D   3    32347  27057  32742   8379   -601   8170       O  
-ATOM  13734  N3   DT D   3     -13.146 -11.483  68.111  1.00242.69           N  
-ANISOU13734  N3   DT D   3    32416  26938  32858   8501  -1004   8118       N  
-ATOM  13735  C4   DT D   3     -13.546 -12.437  67.192  1.00242.43           C  
-ANISOU13735  C4   DT D   3    32459  26795  32858   8580  -1259   8261       C  
-ATOM  13736  O4   DT D   3     -12.745 -13.123  66.564  1.00242.90           O  
-ANISOU13736  O4   DT D   3    32487  26825  32980   8624  -1407   8051       O  
-ATOM  13737  C5   DT D   3     -14.971 -12.569  67.022  1.00241.56           C  
-ANISOU13737  C5   DT D   3    32467  26610  32704   8606  -1339   8675       C  
-ATOM  13738  C7   DT D   3     -15.526 -13.570  66.053  1.00241.20           C  
-ANISOU13738  C7   DT D   3    32513  26443  32689   8690  -1612   8864       C  
-ATOM  13739  C6   DT D   3     -15.769 -11.777  67.750  1.00241.09           C  
-ANISOU13739  C6   DT D   3    32434  26591  32577   8554  -1164   8881       C  
-ATOM  13740  P    DC D   4     -19.611  -7.286  69.698  1.00264.49           P  
-ANISOU13740  P    DC D   4    35674  29614  35208   8294    -19   9804       P  
-ATOM  13741  OP1  DC D   4     -20.709  -7.228  70.688  1.00263.92           O  
-ANISOU13741  OP1  DC D   4    35608  29587  35083   8284    -93  10143       O  
-ATOM  13742  OP2  DC D   4     -19.887  -7.721  68.311  1.00264.03           O  
-ANISOU13742  OP2  DC D   4    35734  29413  35174   8349    -85   9874       O  
-ATOM  13743  O5'  DC D   4     -18.924  -5.843  69.639  1.00264.81           O  
-ANISOU13743  O5'  DC D   4    35710  29688  35217   8202    452   9529       O  
-ATOM  13744  C5'  DC D   4     -17.809  -5.519  70.459  1.00265.54           C  
-ANISOU13744  C5'  DC D   4    35662  29905  35327   8155    543   9209       C  
-ATOM  13745  C4'  DC D   4     -16.877  -4.592  69.701  1.00265.97           C  
-ANISOU13745  C4'  DC D   4    35733  29937  35387   8105    903   8873       C  
-ATOM  13746  O4'  DC D   4     -15.771  -5.356  69.151  1.00266.64           O  
-ANISOU13746  O4'  DC D   4    35753  30010  35548   8148    735   8580       O  
-ATOM  13747  C3'  DC D   4     -17.522  -3.879  68.516  1.00265.42           C  
-ANISOU13747  C3'  DC D   4    35828  29737  35281   8093   1168   8995       C  
-ATOM  13748  O3'  DC D   4     -16.949  -2.584  68.360  1.00265.66           O  
-ANISOU13748  O3'  DC D   4    35867  29789  35284   8013   1595   8758       O  
-ATOM  13749  C2'  DC D   4     -17.176  -4.811  67.361  1.00265.58           C  
-ANISOU13749  C2'  DC D   4    35885  29658  35364   8166    957   8916       C  
-ATOM  13750  C1'  DC D   4     -15.764  -5.231  67.743  1.00266.50           C  
-ANISOU13750  C1'  DC D   4    35850  29864  35543   8168    853   8539       C  
-ATOM  13751  N1   DC D   4     -15.356  -6.527  67.124  1.00266.77           N  
-ANISOU13751  N1   DC D   4    35864  29848  35649   8252    503   8474       N  
-ATOM  13752  C2   DC D   4     -14.003  -6.875  67.076  1.00267.61           C  
-ANISOU13752  C2   DC D   4    35860  30003  35818   8259    444   8101       C  
-ATOM  13753  O2   DC D   4     -13.168  -6.102  67.558  1.00268.08           O  
-ANISOU13753  O2   DC D   4    35840  30148  35872   8195    683   7831       O  
-ATOM  13754  N3   DC D   4     -13.651  -8.053  66.505  1.00267.85           N  
-ANISOU13754  N3   DC D   4    35873  29985  35913   8336    125   8047       N  
-ATOM  13755  C4   DC D   4     -14.587  -8.858  65.997  1.00267.29           C  
-ANISOU13755  C4   DC D   4    35890  29822  35846   8403   -126   8347       C  
-ATOM  13756  N4   DC D   4     -14.192 -10.010  65.444  1.00267.56           N  
-ANISOU13756  N4   DC D   4    35904  29811  35944   8478   -436   8280       N  
-ATOM  13757  C5   DC D   4     -15.971  -8.517  66.035  1.00266.43           C  
-ANISOU13757  C5   DC D   4    35895  29662  35674   8397    -70   8729       C  
-ATOM  13758  C6   DC D   4     -16.307  -7.353  66.600  1.00266.12           C  
-ANISOU13758  C6   DC D   4    35871  29671  35571   8321    245   8779       C  
-ATOM  13759  P    DT D   5     -17.344  -1.663  67.101  1.00295.23           P  
-ANISOU13759  P    DT D   5    39769  33410  38995   7987   1936   8795       P  
-ATOM  13760  OP1  DT D   5     -17.935  -0.411  67.617  1.00294.84           O  
-ANISOU13760  OP1  DT D   5    39762  33394  38869   7910   2274   8913       O  
-ATOM  13761  OP2  DT D   5     -18.111  -2.492  66.145  1.00294.73           O  
-ANISOU13761  OP2  DT D   5    39815  33220  38948   8063   1709   9037       O  
-ATOM  13762  O5'  DT D   5     -15.930  -1.287  66.459  1.00296.00           O  
-ANISOU13762  O5'  DT D   5    39820  33510  39136   7962   2135   8351       O  
-ATOM  13763  C5'  DT D   5     -14.943  -0.677  67.280  1.00296.64           C  
-ANISOU13763  C5'  DT D   5    39779  33712  39219   7899   2310   8054       C  
-ATOM  13764  C4'  DT D   5     -13.551  -0.985  66.762  1.00297.41           C  
-ANISOU13764  C4'  DT D   5    39801  33817  39385   7913   2291   7656       C  
-ATOM  13765  O4'  DT D   5     -13.460  -2.398  66.437  1.00297.57           O  
-ANISOU13765  O4'  DT D   5    39798  33799  39467   8001   1877   7696       O  
-ATOM  13766  C3'  DT D   5     -13.151  -0.227  65.501  1.00297.52           C  
-ANISOU13766  C3'  DT D   5    39907  33738  39400   7889   2609   7472       C  
-ATOM  13767  O3'  DT D   5     -11.781   0.140  65.598  1.00298.33           O  
-ANISOU13767  O3'  DT D   5    39907  33908  39537   7850   2762   7060       O  
-ATOM  13768  C2'  DT D   5     -13.391  -1.250  64.395  1.00297.34           C  
-ANISOU13768  C2'  DT D   5    39959  33594  39421   7973   2348   7568       C  
-ATOM  13769  C1'  DT D   5     -13.048  -2.562  65.093  1.00297.70           C  
-ANISOU13769  C1'  DT D   5    39884  33707  39522   8033   1916   7554       C  
-ATOM  13770  N1   DT D   5     -13.739  -3.754  64.498  1.00297.31           N  
-ANISOU13770  N1   DT D   5    39899  33564  39500   8123   1559   7801       N  
-ATOM  13771  C2   DT D   5     -12.989  -4.803  64.006  1.00297.79           C  
-ANISOU13771  C2   DT D   5    39910  33601  39634   8186   1289   7628       C  
-ATOM  13772  O2   DT D   5     -11.772  -4.830  64.028  1.00298.53           O  
-ANISOU13772  O2   DT D   5    39908  33747  39773   8175   1321   7280       O  
-ATOM  13773  N3   DT D   5     -13.726  -5.836  63.482  1.00297.36           N  
-ANISOU13773  N3   DT D   5    39924  33460  39599   8265    976   7882       N  
-ATOM  13774  C4   DT D   5     -15.104  -5.926  63.399  1.00296.52           C  
-ANISOU13774  C4   DT D   5    39928  33289  39448   8287    906   8282       C  
-ATOM  13775  O4   DT D   5     -15.672  -6.898  62.909  1.00296.19           O  
-ANISOU13775  O4   DT D   5    39940  33170  39429   8360    614   8485       O  
-ATOM  13776  C5   DT D   5     -15.825  -4.796  63.928  1.00296.00           C  
-ANISOU13776  C5   DT D   5    39909  33252  39307   8217   1200   8444       C  
-ATOM  13777  C7   DT D   5     -17.324  -4.779  63.893  1.00294.87           C  
-ANISOU13777  C7   DT D   5    39884  33044  39110   8233   1156   8875       C  
-ATOM  13778  C6   DT D   5     -15.118  -3.781  64.443  1.00296.46           C  
-ANISOU13778  C6   DT D   5    39902  33396  39345   8140   1508   8199       C  
-ATOM  13779  P    DA D   6     -11.219   1.406  64.783  1.00273.85           P  
-ANISOU13779  P    DA D   6    36865  30767  36418   7786   3217   6813       P  
-ATOM  13780  OP1  DA D   6     -10.586   2.328  65.752  1.00274.26           O  
-ANISOU13780  OP1  DA D   6    36820  30941  36445   7705   3467   6606       O  
-ATOM  13781  OP2  DA D   6     -12.303   1.902  63.906  1.00273.07           O  
-ANISOU13781  OP2  DA D   6    36934  30548  36272   7786   3384   7079       O  
-ATOM  13782  O5'  DA D   6     -10.080   0.772  63.857  1.00274.05           O  
-ANISOU13782  O5'  DA D   6    36857  30748  36521   7830   3112   6497       O  
-ATOM  13783  C5'  DA D   6      -8.993   1.560  63.387  1.00273.62           C  
-ANISOU13783  C5'  DA D   6    36779  30702  36482   7782   3418   6132       C  
-ATOM  13784  C4'  DA D   6      -7.856   0.669  62.916  1.00273.67           C  
-ANISOU13784  C4'  DA D   6    36708  30703  36570   7832   3208   5841       C  
-ATOM  13785  O4'  DA D   6      -8.289  -0.717  62.911  1.00273.61           O  
-ANISOU13785  O4'  DA D   6    36694  30665  36599   7918   2768   6038       O  
-ATOM  13786  C3'  DA D   6      -7.378   0.945  61.498  1.00273.23           C  
-ANISOU13786  C3'  DA D   6    36737  30539  36540   7840   3391   5656       C  
-ATOM  13787  O3'  DA D   6      -6.011   0.580  61.353  1.00273.70           O  
-ANISOU13787  O3'  DA D   6    36691  30637  36665   7850   3332   5280       O  
-ATOM  13788  C2'  DA D   6      -8.284   0.038  60.677  1.00272.85           C  
-ANISOU13788  C2'  DA D   6    36798  30371  36503   7920   3128   5944       C  
-ATOM  13789  C1'  DA D   6      -8.386  -1.187  61.580  1.00273.75           C  
-ANISOU13789  C1'  DA D   6    36812  30553  36648   7974   2696   6059       C  
-ATOM  13790  N9   DA D   6      -9.646  -1.907  61.416  1.00274.00           N  
-ANISOU13790  N9   DA D   6    36932  30511  36663   8033   2441   6454       N  
-ATOM  13791  C8   DA D   6     -10.874  -1.551  61.902  1.00273.76           C  
-ANISOU13791  C8   DA D   6    36968  30479  36569   8015   2482   6800       C  
-ATOM  13792  N7   DA D   6     -11.831  -2.393  61.592  1.00273.41           N  
-ANISOU13792  N7   DA D   6    36997  30360  36525   8081   2207   7112       N  
-ATOM  13793  C5   DA D   6     -11.187  -3.370  60.850  1.00273.81           C  
-ANISOU13793  C5   DA D   6    37030  30361  36646   8147   1971   6961       C  
-ATOM  13794  C6   DA D   6     -11.646  -4.546  60.225  1.00273.56           C  
-ANISOU13794  C6   DA D   6    37049  30241  36650   8233   1628   7139       C  
-ATOM  13795  N6   DA D   6     -12.921  -4.950  60.255  1.00272.81           N  
-ANISOU13795  N6   DA D   6    37039  30094  36524   8269   1458   7528       N  
-ATOM  13796  N1   DA D   6     -10.738  -5.295  59.565  1.00274.10           N  
-ANISOU13796  N1   DA D   6    37079  30279  36788   8281   1466   6902       N  
-ATOM  13797  C2   DA D   6      -9.462  -4.891  59.536  1.00274.85           C  
-ANISOU13797  C2   DA D   6    37090  30427  36914   8245   1636   6513       C  
-ATOM  13798  N3   DA D   6      -8.915  -3.808  60.083  1.00275.12           N  
-ANISOU13798  N3   DA D   6    37069  30543  36920   8165   1957   6312       N  
-ATOM  13799  C4   DA D   6      -9.840  -3.084  60.731  1.00274.45           C  
-ANISOU13799  C4   DA D   6    37025  30488  36767   8118   2111   6556       C  
-ATOM  13800  P    DT D   7      -5.227   0.919  59.992  1.00216.25           P  
-ANISOU13800  P    DT D   7    29473  23270  29422   7851   3541   5005       P  
-ATOM  13801  OP1  DT D   7      -3.777   0.876  60.279  1.00217.17           O  
-ANISOU13801  OP1  DT D   7    29452  23471  29591   7833   3560   4599       O  
-ATOM  13802  OP2  DT D   7      -5.827   2.140  59.413  1.00215.74           O  
-ANISOU13802  OP2  DT D   7    29536  23139  29296   7797   3930   5100       O  
-ATOM  13803  O5'  DT D   7      -5.577  -0.316  59.040  1.00216.03           O  
-ANISOU13803  O5'  DT D   7    29512  23130  29440   7947   3204   5148       O  
-ATOM  13804  C5'  DT D   7      -5.413  -0.175  57.639  1.00215.98           C  
-ANISOU13804  C5'  DT D   7    29610  23002  29452   7967   3333   5061       C  
-ATOM  13805  C4'  DT D   7      -5.220  -1.523  56.975  1.00216.14           C  
-ANISOU13805  C4'  DT D   7    29629  22956  29537   8058   2964   5061       C  
-ATOM  13806  O4'  DT D   7      -6.294  -2.418  57.362  1.00215.58           O  
-ANISOU13806  O4'  DT D   7    29585  22870  29456   8113   2629   5424       O  
-ATOM  13807  C3'  DT D   7      -5.238  -1.473  55.454  1.00215.98           C  
-ANISOU13807  C3'  DT D   7    29734  22794  29533   8087   3066   5028       C  
-ATOM  13808  O3'  DT D   7      -4.332  -2.432  54.922  1.00216.55           O  
-ANISOU13808  O3'  DT D   7    29752  22845  29682   8146   2832   4806       O  
-ATOM  13809  C2'  DT D   7      -6.689  -1.812  55.136  1.00215.08           C  
-ANISOU13809  C2'  DT D   7    29750  22590  29382   8128   2930   5454       C  
-ATOM  13810  C1'  DT D   7      -7.001  -2.842  56.213  1.00215.07           C  
-ANISOU13810  C1'  DT D   7    29655  22666  29395   8169   2540   5622       C  
-ATOM  13811  N1   DT D   7      -8.449  -2.907  56.540  1.00214.22           N  
-ANISOU13811  N1   DT D   7    29632  22530  29233   8180   2452   6049       N  
-ATOM  13812  C2   DT D   7      -9.160  -4.062  56.295  1.00213.85           C  
-ANISOU13812  C2   DT D   7    29626  22421  29206   8260   2086   6307       C  
-ATOM  13813  O2   DT D   7      -8.666  -5.070  55.821  1.00214.18           O  
-ANISOU13813  O2   DT D   7    29639  22429  29309   8325   1820   6207       O  
-ATOM  13814  N3   DT D   7     -10.486  -3.995  56.635  1.00213.07           N  
-ANISOU13814  N3   DT D   7    29604  22300  29052   8262   2041   6693       N  
-ATOM  13815  C4   DT D   7     -11.158  -2.914  57.179  1.00212.63           C  
-ANISOU13815  C4   DT D   7    29588  22278  28925   8194   2320   6842       C  
-ATOM  13816  O4   DT D   7     -12.354  -2.947  57.451  1.00211.93           O  
-ANISOU13816  O4   DT D   7    29568  22166  28791   8202   2253   7195       O  
-ATOM  13817  C5   DT D   7     -10.354  -1.741  57.404  1.00213.06           C  
-ANISOU13817  C5   DT D   7    29595  22396  28961   8113   2696   6555       C  
-ATOM  13818  C7   DT D   7     -10.973  -0.508  57.990  1.00212.65           C  
-ANISOU13818  C7   DT D   7    29580  22384  28833   8034   3021   6682       C  
-ATOM  13819  C6   DT D   7      -9.058  -1.792  57.077  1.00213.82           C  
-ANISOU13819  C6   DT D   7    29617  22514  29111   8110   2743   6178       C  
-ATOM  13820  P    DC D   8      -3.911  -2.376  53.372  1.00184.39           P  
-ANISOU13820  P    DC D   8    24533  22199  23329   6407  -5459   4543       P  
-ATOM  13821  OP1  DC D   8      -2.434  -2.322  53.302  1.00187.35           O  
-ANISOU13821  OP1  DC D   8    24641  22301  24244   6434  -5445   4803       O  
-ATOM  13822  OP2  DC D   8      -4.721  -1.325  52.716  1.00184.56           O  
-ANISOU13822  OP2  DC D   8    24683  22411  23030   6338  -5558   4398       O  
-ATOM  13823  O5'  DC D   8      -4.399  -3.787  52.803  1.00183.52           O  
-ANISOU13823  O5'  DC D   8    24531  22144  23053   6343  -4938   4427       O  
-ATOM  13824  C5'  DC D   8      -5.705  -4.226  53.132  1.00177.49           C  
-ANISOU13824  C5'  DC D   8    24008  21607  21822   6339  -4920   4198       C  
-ATOM  13825  C4'  DC D   8      -6.131  -5.407  52.288  1.00173.95           C  
-ANISOU13825  C4'  DC D   8    23654  21212  21226   6252  -4385   4088       C  
-ATOM  13826  O4'  DC D   8      -7.536  -5.646  52.540  1.00170.39           O  
-ANISOU13826  O4'  DC D   8    23457  21014  20270   6240  -4399   3842       O  
-ATOM  13827  C3'  DC D   8      -6.070  -5.188  50.787  1.00171.01           C  
-ANISOU13827  C3'  DC D   8    23268  20855  20853   6129  -4034   4067       C  
-ATOM  13828  O3'  DC D   8      -6.184  -6.447  50.129  1.00168.10           O  
-ANISOU13828  O3'  DC D   8    22941  20477  20453   6065  -3527   4015       O  
-ATOM  13829  C2'  DC D   8      -7.312  -4.328  50.592  1.00168.17           C  
-ANISOU13829  C2'  DC D   8    23116  20757  20024   6088  -4214   3853       C  
-ATOM  13830  C1'  DC D   8      -8.301  -5.045  51.510  1.00168.29           C  
-ANISOU13830  C1'  DC D   8    23316  20923  19702   6138  -4283   3690       C  
-ATOM  13831  N1   DC D   8      -9.317  -4.145  52.129  1.00164.83           N  
-ANISOU13831  N1   DC D   8    23045  20696  18888   6171  -4692   3536       N  
-ATOM  13832  C2   DC D   8     -10.633  -4.596  52.283  1.00161.92           C  
-ANISOU13832  C2   DC D   8    22914  20558  18050   6151  -4624   3301       C  
-ATOM  13833  O2   DC D   8     -10.929  -5.736  51.905  1.00158.42           O  
-ANISOU13833  O2   DC D   8    22541  20140  17513   6105  -4226   3224       O  
-ATOM  13834  N3   DC D   8     -11.549  -3.769  52.847  1.00159.67           N  
-ANISOU13834  N3   DC D   8    22779  20463  17426   6183  -4997   3164       N  
-ATOM  13835  C4   DC D   8     -11.191  -2.547  53.244  1.00160.57           C  
-ANISOU13835  C4   DC D   8    22813  20542  17654   6232  -5421   3253       C  
-ATOM  13836  N4   DC D   8     -12.130  -1.770  53.794  1.00157.66           N  
-ANISOU13836  N4   DC D   8    22600  20366  16938   6262  -5777   3111       N  
-ATOM  13837  C5   DC D   8      -9.855  -2.071  53.094  1.00163.41           C  
-ANISOU13837  C5   DC D   8    22930  20668  18491   6252  -5497   3491       C  
-ATOM  13838  C6   DC D   8      -8.959  -2.893  52.537  1.00166.06           C  
-ANISOU13838  C6   DC D   8    23118  20817  19159   6220  -5126   3626       C  
-ATOM  13839  P    DT D   9      -6.318  -6.516  48.528  1.00166.16           P  
-ANISOU13839  P    DT D   9    22722  20275  20137   5929  -3077   3953       P  
-ATOM  13840  OP1  DT D   9      -5.905  -7.868  48.093  1.00168.08           O  
-ANISOU13840  OP1  DT D   9    22914  20402  20545   5896  -2602   3998       O  
-ATOM  13841  OP2  DT D   9      -5.650  -5.323  47.962  1.00167.39           O  
-ANISOU13841  OP2  DT D   9    22741  20350  20511   5904  -3229   4075       O  
-ATOM  13842  O5'  DT D   9      -7.889  -6.366  48.277  1.00160.41           O  
-ANISOU13842  O5'  DT D   9    22269  19849  18830   5871  -3060   3668       O  
-ATOM  13843  C5'  DT D   9      -8.791  -7.342  48.785  1.00154.39           C  
-ANISOU13843  C5'  DT D   9    21681  19219  17763   5886  -2950   3506       C  
-ATOM  13844  C4'  DT D   9     -10.173  -7.100  48.211  1.00147.12           C  
-ANISOU13844  C4'  DT D   9    20999  18573  16327   5806  -2869   3249       C  
-ATOM  13845  O4'  DT D   9     -10.815  -6.012  48.927  1.00138.51           O  
-ANISOU13845  O4'  DT D   9    20004  17629  14996   5857  -3351   3168       O  
-ATOM  13846  C3'  DT D   9     -10.150  -6.699  46.739  1.00149.09           C  
-ANISOU13846  C3'  DT D   9    21240  18851  16556   5688  -2577   3223       C  
-ATOM  13847  O3'  DT D   9     -11.169  -7.381  46.011  1.00154.02           O  
-ANISOU13847  O3'  DT D   9    22055  19655  16810   5599  -2212   3013       O  
-ATOM  13848  C2'  DT D   9     -10.389  -5.191  46.792  1.00141.66           C  
-ANISOU13848  C2'  DT D   9    20317  18003  15504   5697  -2986   3204       C  
-ATOM  13849  C1'  DT D   9     -11.319  -5.080  47.994  1.00130.87           C  
-ANISOU13849  C1'  DT D   9    19110  16799  13815   5775  -3347   3069       C  
-ATOM  13850  N1   DT D   9     -11.340  -3.721  48.614  1.00120.01           N  
-ANISOU13850  N1   DT D   9    17718  15461  12419   5834  -3867   3100       N  
-ATOM  13851  C2   DT D   9     -12.511  -3.243  49.160  1.00112.86           C  
-ANISOU13851  C2   DT D   9    17010  14784  11087   5856  -4147   2912       C  
-ATOM  13852  O2   DT D   9     -13.550  -3.879  49.173  1.00110.23           O  
-ANISOU13852  O2   DT D   9    16868  14628  10388   5828  -3993   2719       O  
-ATOM  13853  N3   DT D   9     -12.419  -1.984  49.697  1.00110.34           N  
-ANISOU13853  N3   DT D   9    16657  14480  10788   5911  -4618   2959       N  
-ATOM  13854  C4   DT D   9     -11.298  -1.172  49.739  1.00109.99           C  
-ANISOU13854  C4   DT D   9    16405  14248  11140   5945  -4832   3170       C  
-ATOM  13855  O4   DT D   9     -11.309  -0.052  50.244  1.00110.57           O  
-ANISOU13855  O4   DT D   9    16464  14349  11197   5994  -5259   3196       O  
-ATOM  13856  C5   DT D   9     -10.109  -1.734  49.149  1.00112.35           C  
-ANISOU13856  C5   DT D   9    16502  14313  11872   5920  -4518   3359       C  
-ATOM  13857  C7   DT D   9      -8.830  -0.949  49.135  1.00111.32           C  
-ANISOU13857  C7   DT D   9    16135  13966  12197   5952  -4709   3596       C  
-ATOM  13858  C6   DT D   9     -10.187  -2.962  48.622  1.00115.35           C  
-ANISOU13858  C6   DT D   9    16914  14677  12236   5867  -4057   3315       C  
-ATOM  13859  P    DG D  10     -10.844  -8.016  44.571  1.00157.56           P  
-ANISOU13859  P    DG D  10    22460  20041  17363   5486  -1657   3026       P  
-ATOM  13860  OP1  DG D  10      -9.859  -9.104  44.764  1.00159.59           O  
-ANISOU13860  OP1  DG D  10    22563  20074  18000   5518  -1416   3191       O  
-ATOM  13861  OP2  DG D  10     -10.541  -6.906  43.642  1.00158.20           O  
-ANISOU13861  OP2  DG D  10    22473  20114  17521   5426  -1693   3074       O  
-ATOM  13862  O5'  DG D  10     -12.239  -8.649  44.116  1.00157.79           O  
-ANISOU13862  O5'  DG D  10    22743  20320  16889   5409  -1383   2754       O  
-ATOM  13863  C5'  DG D  10     -13.105  -9.238  45.072  1.00157.26           C  
-ANISOU13863  C5'  DG D  10    22834  20384  16535   5461  -1494   2614       C  
-ATOM  13864  C4'  DG D  10     -14.415  -8.473  45.119  1.00154.34           C  
-ANISOU13864  C4'  DG D  10    22678  20287  15679   5438  -1719   2393       C  
-ATOM  13865  O4'  DG D  10     -14.203  -7.189  45.761  1.00151.66           O  
-ANISOU13865  O4'  DG D  10    22281  19941  15403   5507  -2223   2467       O  
-ATOM  13866  C3'  DG D  10     -15.012  -8.148  43.756  1.00154.05           C  
-ANISOU13866  C3'  DG D  10    22742  20394  15396   5316  -1445   2255       C  
-ATOM  13867  O3'  DG D  10     -16.431  -8.180  43.812  1.00155.16           O  
-ANISOU13867  O3'  DG D  10    23126  20802  15025   5285  -1466   2002       O  
-ATOM  13868  C2'  DG D  10     -14.524  -6.726  43.516  1.00151.38           C  
-ANISOU13868  C2'  DG D  10    22298  20014  15205   5321  -1746   2359       C  
-ATOM  13869  C1'  DG D  10     -14.712  -6.176  44.921  1.00146.78           C  
-ANISOU13869  C1'  DG D  10    21737  19465  14569   5434  -2266   2370       C  
-ATOM  13870  N9   DG D  10     -13.988  -4.940  45.182  1.00136.41           N  
-ANISOU13870  N9   DG D  10    20278  18050  13500   5483  -2650   2526       N  
-ATOM  13871  C8   DG D  10     -12.735  -4.597  44.737  1.00136.56           C  
-ANISOU13871  C8   DG D  10    20076  17849  13961   5480  -2608   2744       C  
-ATOM  13872  N7   DG D  10     -12.349  -3.417  45.136  1.00132.99           N  
-ANISOU13872  N7   DG D  10    19538  17355  13636   5530  -3018   2841       N  
-ATOM  13873  C5   DG D  10     -13.414  -2.949  45.897  1.00127.16           C  
-ANISOU13873  C5   DG D  10    18977  16823  12514   5571  -3353   2676       C  
-ATOM  13874  C6   DG D  10     -13.577  -1.724  46.589  1.00122.14           C  
-ANISOU13874  C6   DG D  10    18351  16246  11809   5633  -3858   2683       C  
-ATOM  13875  O6   DG D  10     -12.781  -0.776  46.673  1.00115.80           O  
-ANISOU13875  O6   DG D  10    17396  15321  11281   5665  -4118   2841       O  
-ATOM  13876  N1   DG D  10     -14.813  -1.657  47.233  1.00119.21           N  
-ANISOU13876  N1   DG D  10    18194  16103  10998   5658  -4058   2481       N  
-ATOM  13877  C2   DG D  10     -15.767  -2.650  47.208  1.00120.46           C  
-ANISOU13877  C2   DG D  10    18531  16411  10826   5626  -3803   2296       C  
-ATOM  13878  N2   DG D  10     -16.899  -2.411  47.884  1.00115.78           N  
-ANISOU13878  N2   DG D  10    18131  16032   9830   5657  -4055   2115       N  
-ATOM  13879  N3   DG D  10     -15.626  -3.800  46.563  1.00124.45           N  
-ANISOU13879  N3   DG D  10    19029  16863  11394   5567  -3330   2286       N  
-ATOM  13880  C4   DG D  10     -14.430  -3.878  45.933  1.00129.47           C  
-ANISOU13880  C4   DG D  10    19460  17279  12455   5543  -3131   2482       C  
-ATOM  13881  P    DA D  11     -17.284  -8.343  42.461  1.00146.24           P  
-ANISOU13881  P    DA D  11    22149  19850  13567   5153  -1073   1811       P  
-ATOM  13882  OP1  DA D  11     -17.200  -9.758  42.040  1.00148.49           O  
-ANISOU13882  OP1  DA D  11    22443  20076  13901   5107   -592   1791       O  
-ATOM  13883  OP2  DA D  11     -16.869  -7.269  41.529  1.00147.30           O  
-ANISOU13883  OP2  DA D  11    22198  19955  13814   5099  -1099   1879       O  
-ATOM  13884  O5'  DA D  11     -18.785  -8.022  42.915  1.00144.48           O  
-ANISOU13884  O5'  DA D  11    22176  19917  12804   5156  -1292   1559       O  
-ATOM  13885  C5'  DA D  11     -19.134  -7.790  44.272  1.00144.77           C  
-ANISOU13885  C5'  DA D  11    22265  20006  12734   5259  -1716   1537       C  
-ATOM  13886  C4'  DA D  11     -19.933  -6.503  44.402  1.00142.38           C  
-ANISOU13886  C4'  DA D  11    22079  19897  12121   5263  -2093   1419       C  
-ATOM  13887  O4'  DA D  11     -19.105  -5.492  45.023  1.00143.26           O  
-ANISOU13887  O4'  DA D  11    22035  19876  12523   5344  -2512   1600       O  
-ATOM  13888  C3'  DA D  11     -20.394  -5.879  43.089  1.00142.09           C  
-ANISOU13888  C3'  DA D  11    22114  19991  11882   5153  -1910   1313       C  
-ATOM  13889  O3'  DA D  11     -21.670  -6.388  42.670  1.00137.43           O  
-ANISOU13889  O3'  DA D  11    21749  19635  10834   5083  -1681   1064       O  
-ATOM  13890  C2'  DA D  11     -20.428  -4.385  43.384  1.00142.05           C  
-ANISOU13890  C2'  DA D  11    22094  20039  11841   5192  -2376   1340       C  
-ATOM  13891  C1'  DA D  11     -19.389  -4.217  44.485  1.00142.37           C  
-ANISOU13891  C1'  DA D  11    21954  19868  12273   5306  -2702   1557       C  
-ATOM  13892  N9   DA D  11     -18.133  -3.646  44.024  1.00144.79           N  
-ANISOU13892  N9   DA D  11    22037  19960  13015   5304  -2715   1778       N  
-ATOM  13893  C8   DA D  11     -17.218  -4.220  43.189  1.00145.14           C  
-ANISOU13893  C8   DA D  11    21935  19824  13387   5253  -2334   1910       C  
-ATOM  13894  N7   DA D  11     -16.171  -3.463  42.961  1.00147.66           N  
-ANISOU13894  N7   DA D  11    22064  19971  14068   5267  -2458   2104       N  
-ATOM  13895  C5   DA D  11     -16.418  -2.318  43.701  1.00149.57           C  
-ANISOU13895  C5   DA D  11    22330  20286  14212   5331  -2954   2097       C  
-ATOM  13896  C6   DA D  11     -15.692  -1.128  43.889  1.00151.72           C  
-ANISOU13896  C6   DA D  11    22462  20455  14731   5373  -3305   2251       C  
-ATOM  13897  N6   DA D  11     -14.511  -0.886  43.315  1.00154.66           N  
-ANISOU13897  N6   DA D  11    22626  20617  15519   5356  -3201   2451       N  
-ATOM  13898  N1   DA D  11     -16.232  -0.194  44.695  1.00152.68           N  
-ANISOU13898  N1   DA D  11    22662  20696  14652   5434  -3767   2189       N  
-ATOM  13899  C2   DA D  11     -17.415  -0.433  45.270  1.00151.69           C  
-ANISOU13899  C2   DA D  11    22743  20781  14111   5452  -3870   1990       C  
-ATOM  13900  N3   DA D  11     -18.190  -1.509  45.170  1.00148.72           N  
-ANISOU13900  N3   DA D  11    22514  20520  13471   5416  -3573   1833       N  
-ATOM  13901  C4   DA D  11     -17.625  -2.418  44.364  1.00146.98           C  
-ANISOU13901  C4   DA D  11    22211  20176  13460   5355  -3118   1897       C  
-ATOM  13902  P    DA D  12     -22.972  -6.222  43.604  1.00177.96           P  
-ANISOU13902  P    DA D  12    20798  22765  24054  -3774  -2711   3140       P  
-ATOM  13903  OP1  DA D  12     -22.776  -7.044  44.817  1.00181.21           O  
-ANISOU13903  OP1  DA D  12    21349  23122  24382  -4240  -2885   3321       O  
-ATOM  13904  OP2  DA D  12     -24.167  -6.423  42.757  1.00178.97           O  
-ANISOU13904  OP2  DA D  12    20741  23261  23999  -3629  -2481   2869       O  
-ATOM  13905  O5'  DA D  12     -22.937  -4.690  44.046  1.00170.82           O  
-ANISOU13905  O5'  DA D  12    19963  21935  23005  -3559  -2700   3023       O  
-ATOM  13906  C5'  DA D  12     -23.251  -4.367  45.393  1.00156.23           C  
-ANISOU13906  C5'  DA D  12    18243  20266  20850  -3823  -2778   2995       C  
-ATOM  13907  C4'  DA D  12     -23.510  -2.881  45.558  1.00142.50           C  
-ANISOU13907  C4'  DA D  12    16522  18690  18932  -3554  -2707   2806       C  
-ATOM  13908  O4'  DA D  12     -22.361  -2.129  45.089  1.00134.86           O  
-ANISOU13908  O4'  DA D  12    15599  17337  18304  -3264  -2784   2948       O  
-ATOM  13909  C3'  DA D  12     -24.701  -2.341  44.777  1.00134.86           C  
-ANISOU13909  C3'  DA D  12    15385  18125  17729  -3268  -2457   2468       C  
-ATOM  13910  O3'  DA D  12     -25.316  -1.314  45.541  1.00133.57           O  
-ANISOU13910  O3'  DA D  12    15273  18254  17225  -3245  -2415   2279       O  
-ATOM  13911  C2'  DA D  12     -24.048  -1.790  43.514  1.00127.76           C  
-ANISOU13911  C2'  DA D  12    14405  16971  17166  -2835  -2399   2486       C  
-ATOM  13912  C1'  DA D  12     -22.772  -1.204  44.104  1.00125.42           C  
-ANISOU13912  C1'  DA D  12    14278  16283  17093  -2837  -2602   2725       C  
-ATOM  13913  N9   DA D  12     -21.683  -1.059  43.146  1.00109.19           N  
-ANISOU13913  N9   DA D  12    12201  13819  15469  -2558  -2644   2889       N  
-ATOM  13914  C8   DA D  12     -21.423  -1.848  42.062  1.00107.19           C  
-ANISOU13914  C8   DA D  12    11838  13398  15493  -2455  -2599   2965       C  
-ATOM  13915  N7   DA D  12     -20.362  -1.483  41.381  1.00100.89           N  
-ANISOU13915  N7   DA D  12    11049  12222  15063  -2198  -2656   3117       N  
-ATOM  13916  C5   DA D  12     -19.896  -0.375  42.066  1.00 94.67           C  
-ANISOU13916  C5   DA D  12    10385  11349  14236  -2127  -2745   3142       C  
-ATOM  13917  C6   DA D  12     -18.800   0.480  41.850  1.00 86.86           C  
-ANISOU13917  C6   DA D  12     9464  10010  13529  -1881  -2835   3279       C  
-ATOM  13918  N6   DA D  12     -17.945   0.333  40.835  1.00 82.05           N  
-ANISOU13918  N6   DA D  12     8804   9061  13311  -1653  -2850   3421       N  
-ATOM  13919  N1   DA D  12     -18.616   1.494  42.720  1.00 83.09           N  
-ANISOU13919  N1   DA D  12     9110   9546  12915  -1878  -2911   3264       N  
-ATOM  13920  C2   DA D  12     -19.476   1.635  43.736  1.00 85.89           C  
-ANISOU13920  C2   DA D  12     9515  10243  12876  -2106  -2896   3121       C  
-ATOM  13921  N3   DA D  12     -20.543   0.896  44.042  1.00 93.77           N  
-ANISOU13921  N3   DA D  12    10458  11591  13579  -2349  -2813   2984       N  
-ATOM  13922  C4   DA D  12     -20.697  -0.101  43.158  1.00 99.89           C  
-ANISOU13922  C4   DA D  12    11111  12342  14502  -2346  -2739   3003       C  
-ATOM  13923  P    DG D  13     -26.526  -0.459  44.923  1.00126.22           P  
-ANISOU13923  P    DG D  13    14194  17754  16010  -2932  -2168   1913       P  
-ATOM  13924  OP1  DG D  13     -27.310   0.101  46.047  1.00130.42           O  
-ANISOU13924  OP1  DG D  13    14797  18632  16126  -3096  -2157   1752       O  
-ATOM  13925  OP2  DG D  13     -27.186  -1.284  43.886  1.00128.28           O  
-ANISOU13925  OP2  DG D  13    14279  18163  16297  -2865  -2010   1803       O  
-ATOM  13926  O5'  DG D  13     -25.788   0.744  44.178  1.00120.90           O  
-ANISOU13926  O5'  DG D  13    13514  16843  15579  -2486  -2151   1912       O  
-ATOM  13927  C5'  DG D  13     -26.550   1.778  43.576  1.00109.92           C  
-ANISOU13927  C5'  DG D  13    12016  15735  14012  -2131  -1959   1622       C  
-ATOM  13928  C4'  DG D  13     -25.819   3.095  43.743  1.00101.00           C  
-ANISOU13928  C4'  DG D  13    10982  14414  12980  -1884  -2027   1656       C  
-ATOM  13929  O4'  DG D  13     -24.398   2.822  43.858  1.00 95.30           O  
-ANISOU13929  O4'  DG D  13    10375  13192  12644  -1951  -2231   1986       O  
-ATOM  13930  C3'  DG D  13     -25.989   4.069  42.582  1.00 96.15           C  
-ANISOU13930  C3'  DG D  13    10246  13850  12438  -1399  -1860   1468       C  
-ATOM  13931  O3'  DG D  13     -27.075   4.993  42.815  1.00 92.90           O  
-ANISOU13931  O3'  DG D  13     9793  13864  11642  -1273  -1713   1162       O  
-ATOM  13932  C2'  DG D  13     -24.618   4.735  42.503  1.00 92.62           C  
-ANISOU13932  C2'  DG D  13     9904  12951  12337  -1223  -2008   1688       C  
-ATOM  13933  C1'  DG D  13     -23.671   3.628  42.950  1.00 88.77           C  
-ANISOU13933  C1'  DG D  13     9517  12108  12105  -1552  -2210   2015       C  
-ATOM  13934  N9   DG D  13     -23.137   2.790  41.874  1.00 81.87           N  
-ANISOU13934  N9   DG D  13     8552  10969  11585  -1461  -2199   2155       N  
-ATOM  13935  C8   DG D  13     -23.680   1.632  41.370  1.00 78.78           C  
-ANISOU13935  C8   DG D  13     8048  10697  11188  -1589  -2118   2127       C  
-ATOM  13936  N7   DG D  13     -22.972   1.091  40.417  1.00 76.95           N  
-ANISOU13936  N7   DG D  13     7757  10158  11322  -1461  -2134   2279       N  
-ATOM  13937  C5   DG D  13     -21.887   1.943  40.281  1.00 76.84           C  
-ANISOU13937  C5   DG D  13     7821   9800  11574  -1235  -2231   2419       C  
-ATOM  13938  C6   DG D  13     -20.783   1.873  39.403  1.00 75.52           C  
-ANISOU13938  C6   DG D  13     7639   9215  11841  -1022  -2288   2614       C  
-ATOM  13939  O6   DG D  13     -20.536   1.014  38.545  1.00 77.69           O  
-ANISOU13939  O6   DG D  13     7825   9334  12358   -988  -2265   2704       O  
-ATOM  13940  N1   DG D  13     -19.910   2.941  39.592  1.00 74.35           N  
-ANISOU13940  N1   DG D  13     7591   8818  11841   -835  -2383   2705       N  
-ATOM  13941  C2   DG D  13     -20.085   3.946  40.512  1.00 74.50           C  
-ANISOU13941  C2   DG D  13     7713   8974  11619   -851  -2419   2618       C  
-ATOM  13942  N2   DG D  13     -19.138   4.890  40.552  1.00 74.77           N  
-ANISOU13942  N2   DG D  13     7835   8723  11852   -653  -2514   2729       N  
-ATOM  13943  N3   DG D  13     -21.114   4.024  41.340  1.00 75.98           N  
-ANISOU13943  N3   DG D  13     7917   9553  11399  -1048  -2367   2435       N  
-ATOM  13944  C4   DG D  13     -21.972   2.993  41.168  1.00 77.92           C  
-ANISOU13944  C4   DG D  13     8065  10046  11496  -1233  -2273   2345       C  
-ATOM  13945  P    DC D  14     -26.939   6.154  43.922  1.00103.93           P  
-ANISOU13945  P    DC D  14    11340  15309  12840  -1292  -1805   1132       P  
-ATOM  13946  OP1  DC D  14     -26.580   5.522  45.206  1.00108.53           O  
-ANISOU13946  OP1  DC D  14    12077  15797  13364  -1731  -1997   1333       O  
-ATOM  13947  OP2  DC D  14     -28.137   7.014  43.831  1.00107.03           O  
-ANISOU13947  OP2  DC D  14    11648  16151  12868  -1101  -1615    791       O  
-ATOM  13948  O5'  DC D  14     -25.704   7.023  43.414  1.00 98.28           O  
-ANISOU13948  O5'  DC D  14    10678  14177  12488   -972  -1888   1283       O  
-ATOM  13949  C5'  DC D  14     -25.931   7.884  42.328  1.00 87.91           C  
-ANISOU13949  C5'  DC D  14     9247  12929  11225   -531  -1725   1099       C  
-ATOM  13950  C4'  DC D  14     -24.679   8.234  41.547  1.00 83.14           C  
-ANISOU13950  C4'  DC D  14     8658  11871  11060   -256  -1798   1291       C  
-ATOM  13951  O4'  DC D  14     -23.989   7.051  41.075  1.00 77.03           O  
-ANISOU13951  O4'  DC D  14     7863  10791  10614   -383  -1875   1528       O  
-ATOM  13952  C3'  DC D  14     -24.990   9.048  40.301  1.00 79.13           C  
-ANISOU13952  C3'  DC D  14     8009  11449  10606    213  -1610   1086       C  
-ATOM  13953  O3'  DC D  14     -24.058  10.094  40.213  1.00 80.80           O  
-ANISOU13953  O3'  DC D  14     8301  11375  11025    463  -1690   1180       O  
-ATOM  13954  C2'  DC D  14     -24.850   8.049  39.161  1.00 73.70           C  
-ANISOU13954  C2'  DC D  14     7192  10625  10185    280  -1544   1156       C  
-ATOM  13955  C1'  DC D  14     -23.717   7.193  39.698  1.00 69.50           C  
-ANISOU13955  C1'  DC D  14     6784   9691   9933    -17  -1768   1505       C  
-ATOM  13956  N1   DC D  14     -23.654   5.855  39.062  1.00 58.88           N  
-ANISOU13956  N1   DC D  14     5351   8244   8776   -142  -1755   1615       N  
-ATOM  13957  C2   DC D  14     -22.470   5.441  38.445  1.00 54.05           C  
-ANISOU13957  C2   DC D  14     4753   7182   8603    -66  -1858   1874       C  
-ATOM  13958  O2   DC D  14     -21.498   6.206  38.450  1.00 55.20           O  
-ANISOU13958  O2   DC D  14     4982   7023   8968    103  -1958   2007       O  
-ATOM  13959  N3   DC D  14     -22.417   4.216  37.860  1.00 49.50           N  
-ANISOU13959  N3   DC D  14     4096   6513   8198   -178  -1847   1973       N  
-ATOM  13960  C4   DC D  14     -23.490   3.425  37.876  1.00 48.64           C  
-ANISOU13960  C4   DC D  14     3897   6742   7841   -360  -1737   1823       C  
-ATOM  13961  N4   DC D  14     -23.396   2.226  37.290  1.00 43.61           N  
-ANISOU13961  N4   DC D  14     3185   6000   7386   -465  -1732   1927       N  
-ATOM  13962  C5   DC D  14     -24.709   3.831  38.499  1.00 51.68           C  
-ANISOU13962  C5   DC D  14     4266   7590   7779   -441  -1629   1558       C  
-ATOM  13963  C6   DC D  14     -24.746   5.042  39.070  1.00 55.91           C  
-ANISOU13963  C6   DC D  14     4882   8212   8149   -327  -1642   1462       C  
-ATOM  13964  P    DC D  15     -24.468  11.569  40.687  1.00 80.53           P  
-ANISOU13964  P    DC D  15     8317  11559  10722    654  -1643    974       P  
-ATOM  13965  OP1  DC D  15     -23.303  12.456  40.472  1.00 81.97           O  
-ANISOU13965  OP1  DC D  15     8578  11361  11204    902  -1746   1127       O  
-ATOM  13966  OP2  DC D  15     -25.075  11.463  42.033  1.00 81.88           O  
-ANISOU13966  OP2  DC D  15     8585  11995  10531    304  -1704    920       O  
-ATOM  13967  O5'  DC D  15     -25.645  11.964  39.681  1.00 79.96           O  
-ANISOU13967  O5'  DC D  15     8060  11868  10455    970  -1381    637       O  
-ATOM  13968  C5'  DC D  15     -25.355  12.195  38.313  1.00 73.39           C  
-ANISOU13968  C5'  DC D  15     7108  10885   9891   1351  -1274    610       C  
-ATOM  13969  C4'  DC D  15     -26.570  11.940  37.439  1.00 67.50           C  
-ANISOU13969  C4'  DC D  15     6176  10513   8958   1498  -1038    333       C  
-ATOM  13970  O4'  DC D  15     -26.848  10.520  37.405  1.00 69.10           O  
-ANISOU13970  O4'  DC D  15     6325  10756   9173   1206  -1040    408       O  
-ATOM  13971  C3'  DC D  15     -27.876  12.605  37.855  1.00 65.10           C  
-ANISOU13971  C3'  DC D  15     5835  10706   8195   1527   -895      9       C  
-ATOM  13972  O3'  DC D  15     -28.564  13.000  36.671  1.00 57.36           O  
-ANISOU13972  O3'  DC D  15     4688   9928   7179   1891   -678   -234       O  
-ATOM  13973  C2'  DC D  15     -28.606  11.476  38.580  1.00 68.58           C  
-ANISOU13973  C2'  DC D  15     6273  11389   8394   1107   -906     -2       C  
-ATOM  13974  C1'  DC D  15     -28.211  10.299  37.699  1.00 70.41           C  
-ANISOU13974  C1'  DC D  15     6417  11400   8937   1076   -902    153       C  
-ATOM  13975  N1   DC D  15     -28.274   8.965  38.344  1.00 75.54           N  
-ANISOU13975  N1   DC D  15     7102  12046   9552    637   -997    300       N  
-ATOM  13976  C2   DC D  15     -28.334   7.821  37.544  1.00 77.84           C  
-ANISOU13976  C2   DC D  15     7282  12278  10014    590   -945    358       C  
-ATOM  13977  O2   DC D  15     -28.348   7.947  36.316  1.00 81.80           O  
-ANISOU13977  O2   DC D  15     7655  12736  10688    916   -818    282       O  
-ATOM  13978  N3   DC D  15     -28.377   6.607  38.137  1.00 80.14           N  
-ANISOU13978  N3   DC D  15     7609  12561  10278    189  -1035    496       N  
-ATOM  13979  C4   DC D  15     -28.355   6.517  39.464  1.00 81.43           C  
-ANISOU13979  C4   DC D  15     7914  12773  10254   -153  -1172    576       C  
-ATOM  13980  N4   DC D  15     -28.401   5.298  40.013  1.00 84.65           N  
-ANISOU13980  N4   DC D  15     8354  13171  10640   -544  -1258    712       N  
-ATOM  13981  C5   DC D  15     -28.291   7.674  40.292  1.00 80.02           C  
-ANISOU13981  C5   DC D  15     7850  12654   9899   -108  -1226    518       C  
-ATOM  13982  C6   DC D  15     -28.248   8.869  39.699  1.00 77.39           C  
-ANISOU13982  C6   DC D  15     7480  12327   9596    288  -1138    382       C  
-ATOM  13983  P    DG D  16     -29.511  14.298  36.674  1.00 55.68           P  
-ANISOU13983  P    DG D  16     4030  10855   6272  -1426  -1085   1887       P  
-ATOM  13984  OP1  DG D  16     -29.122  15.151  35.538  1.00 55.87           O  
-ANISOU13984  OP1  DG D  16     4286  10779   6164  -1653  -1758   1896       O  
-ATOM  13985  OP2  DG D  16     -29.472  14.887  38.027  1.00 58.10           O  
-ANISOU13985  OP2  DG D  16     4343  11272   6459  -1108   -977   1873       O  
-ATOM  13986  O5'  DG D  16     -30.969  13.697  36.397  1.00 59.07           O  
-ANISOU13986  O5'  DG D  16     4095  11122   7228  -1409   -901   1607       O  
-ATOM  13987  C5'  DG D  16     -31.539  13.684  35.088  1.00 60.80           C  
-ANISOU13987  C5'  DG D  16     4256  11153   7693  -1647  -1250   1463       C  
-ATOM  13988  C4'  DG D  16     -31.565  12.306  34.440  1.00 61.61           C  
-ANISOU13988  C4'  DG D  16     4240  11241   7929  -1857   -832   1544       C  
-ATOM  13989  O4'  DG D  16     -30.908  11.327  35.267  1.00 61.73           O  
-ANISOU13989  O4'  DG D  16     4250  11443   7760  -1780   -184   1771       O  
-ATOM  13990  C3'  DG D  16     -32.943  11.724  34.156  1.00 63.72           C  
-ANISOU13990  C3'  DG D  16     4161  11352   8699  -1852   -664   1280       C  
-ATOM  13991  O3'  DG D  16     -33.297  12.127  32.858  1.00 63.52           O  
-ANISOU13991  O3'  DG D  16     4169  11148   8817  -2080  -1192   1152       O  
-ATOM  13992  C2'  DG D  16     -32.720  10.216  34.195  1.00 65.30           C  
-ANISOU13992  C2'  DG D  16     4250  11631   8930  -1943     -5   1436       C  
-ATOM  13993  C1'  DG D  16     -31.404  10.046  34.949  1.00 64.72           C  
-ANISOU13993  C1'  DG D  16     4406  11781   8405  -1882    280   1748       C  
-ATOM  13994  N9   DG D  16     -31.528   9.309  36.201  1.00 68.67           N  
-ANISOU13994  N9   DG D  16     4736  12415   8942  -1646    937   1797       N  
-ATOM  13995  C8   DG D  16     -31.661   9.844  37.458  1.00 71.33           C  
-ANISOU13995  C8   DG D  16     5033  12843   9227  -1339   1049   1753       C  
-ATOM  13996  N7   DG D  16     -31.746   8.946  38.396  1.00 72.51           N  
-ANISOU13996  N7   DG D  16     5020  13106   9423  -1180   1692   1817       N  
-ATOM  13997  C5   DG D  16     -31.660   7.736  37.719  1.00 72.37           C  
-ANISOU13997  C5   DG D  16     4932  13069   9495  -1398   2029   1911       C  
-ATOM  13998  C6   DG D  16     -31.692   6.409  38.208  1.00 74.00           C  
-ANISOU13998  C6   DG D  16     4970  13362   9784  -1363   2733   2011       C  
-ATOM  13999  O6   DG D  16     -31.808   6.021  39.379  1.00 75.40           O  
-ANISOU13999  O6   DG D  16     5020  13657   9973  -1124   3221   2039       O  
-ATOM  14000  N1   DG D  16     -31.575   5.481  37.178  1.00 73.71           N  
-ANISOU14000  N1   DG D  16     4923  13263   9821  -1642   2850   2082       N  
-ATOM  14001  C2   DG D  16     -31.440   5.792  35.846  1.00 72.47           C  
-ANISOU14001  C2   DG D  16     4900  12978   9656  -1917   2352   2061       C  
-ATOM  14002  N2   DG D  16     -31.337   4.756  35.002  1.00 72.58           N  
-ANISOU14002  N2   DG D  16     4884  12949   9745  -2158   2565   2140       N  
-ATOM  14003  N3   DG D  16     -31.410   7.030  35.376  1.00 71.15           N  
-ANISOU14003  N3   DG D  16     4889  12731   9413  -1952   1692   1970       N  
-ATOM  14004  C4   DG D  16     -31.524   7.944  36.367  1.00 70.40           C  
-ANISOU14004  C4   DG D  16     4807  12694   9248  -1685   1570   1899       C  
-ATOM  14005  P    DA D  17     -34.823  12.051  32.369  1.00 68.92           P  
-ANISOU14005  P    DA D  17     4536  11624  10026  -2082  -1301    817       P  
-ATOM  14006  OP1  DA D  17     -34.958  12.917  31.182  1.00 69.81           O  
-ANISOU14006  OP1  DA D  17     4774  11578  10172  -2273  -1997    706       O  
-ATOM  14007  OP2  DA D  17     -35.691  12.300  33.534  1.00 71.56           O  
-ANISOU14007  OP2  DA D  17     4643  11973  10575  -1759  -1093    635       O  
-ATOM  14008  O5'  DA D  17     -35.008  10.524  31.936  1.00 70.52           O  
-ANISOU14008  O5'  DA D  17     4563  11816  10416  -2248   -768    876       O  
-ATOM  14009  C5'  DA D  17     -34.146   9.950  30.970  1.00 73.31           C  
-ANISOU14009  C5'  DA D  17     5101  12185  10567  -2541   -783   1084       C  
-ATOM  14010  C4'  DA D  17     -34.477   8.493  30.696  1.00 77.68           C  
-ANISOU14010  C4'  DA D  17     5451  12721  11343  -2659   -239   1106       C  
-ATOM  14011  O4'  DA D  17     -34.153   7.676  31.847  1.00 79.46           O  
-ANISOU14011  O4'  DA D  17     5601  13117  11473  -2485    428   1257       O  
-ATOM  14012  C3'  DA D  17     -35.927   8.169  30.366  1.00 82.05           C  
-ANISOU14012  C3'  DA D  17     5670  13096  12411  -2654   -205    809       C  
-ATOM  14013  O3'  DA D  17     -35.937   7.046  29.500  1.00 83.70           O  
-ANISOU14013  O3'  DA D  17     5816  13249  12737  -2899     32    865       O  
-ATOM  14014  C2'  DA D  17     -36.499   7.830  31.735  1.00 84.49           C  
-ANISOU14014  C2'  DA D  17     5738  13488  12876  -2349    313    739       C  
-ATOM  14015  C1'  DA D  17     -35.327   7.086  32.367  1.00 83.45           C  
-ANISOU14015  C1'  DA D  17     5759  13564  12386  -2334    813   1056       C  
-ATOM  14016  N9   DA D  17     -35.257   7.198  33.822  1.00 85.96           N  
-ANISOU14016  N9   DA D  17     6020  14030  12611  -2024   1169   1096       N  
-ATOM  14017  C8   DA D  17     -35.410   8.330  34.573  1.00 87.41           C  
-ANISOU14017  C8   DA D  17     6242  14238  12730  -1789    891    998       C  
-ATOM  14018  N7   DA D  17     -35.286   8.135  35.864  1.00 88.54           N  
-ANISOU14018  N7   DA D  17     6322  14530  12790  -1532   1331   1066       N  
-ATOM  14019  C5   DA D  17     -35.028   6.780  35.969  1.00 88.56           C  
-ANISOU14019  C5   DA D  17     6237  14609  12801  -1605   1942   1222       C  
-ATOM  14020  C6   DA D  17     -34.798   5.939  37.075  1.00 88.99           C  
-ANISOU14020  C6   DA D  17     6197  14823  12792  -1431   2608   1356       C  
-ATOM  14021  N6   DA D  17     -34.792   6.372  38.339  1.00 90.91           N  
-ANISOU14021  N6   DA D  17     6416  15183  12944  -1133   2772   1354       N  
-ATOM  14022  N1   DA D  17     -34.572   4.631  36.830  1.00 88.01           N  
-ANISOU14022  N1   DA D  17     6006  14734  12699  -1574   3101   1494       N  
-ATOM  14023  C2   DA D  17     -34.577   4.200  35.564  1.00 86.71           C  
-ANISOU14023  C2   DA D  17     5870  14452  12623  -1869   2934   1495       C  
-ATOM  14024  N3   DA D  17     -34.781   4.894  34.446  1.00 86.52           N  
-ANISOU14024  N3   DA D  17     5933  14276  12664  -2055   2327   1375       N  
-ATOM  14025  C4   DA D  17     -35.003   6.188  34.721  1.00 87.26           C  
-ANISOU14025  C4   DA D  17     6089  14339  12726  -1908   1850   1242       C  
-ATOM  14026  P    DT D  18     -37.221   6.739  28.585  1.00 80.61           P  
-ANISOU14026  P    DT D  18     5162  12640  12828  -3028   -105    588       P  
-ATOM  14027  OP1  DT D  18     -36.739   6.257  27.275  1.00 79.73           O  
-ANISOU14027  OP1  DT D  18     5190  12463  12640  -3357   -260    694       O  
-ATOM  14028  OP2  DT D  18     -38.117   7.913  28.648  1.00 82.70           O  
-ANISOU14028  OP2  DT D  18     5335  12785  13301  -2890   -593    318       O  
-ATOM  14029  O5'  DT D  18     -37.935   5.528  29.344  1.00 86.83           O  
-ANISOU14029  O5'  DT D  18     5626  13457  13910  -2900    610    536       O  
-ATOM  14030  C5'  DT D  18     -37.146   4.397  29.685  1.00 92.91           C  
-ANISOU14030  C5'  DT D  18     6446  14370  14486  -2943   1191    791       C  
-ATOM  14031  C4'  DT D  18     -37.844   3.515  30.702  1.00 98.91           C  
-ANISOU14031  C4'  DT D  18     6903  15177  15503  -2743   1840    729       C  
-ATOM  14032  O4'  DT D  18     -37.566   3.963  32.051  1.00100.84           O  
-ANISOU14032  O4'  DT D  18     7171  15575  15569  -2448   2031    790       O  
-ATOM  14033  C3'  DT D  18     -39.360   3.472  30.560  1.00103.79           C  
-ANISOU14033  C3'  DT D  18     7179  15622  16635  -2687   1802    407       C  
-ATOM  14034  O3'  DT D  18     -39.713   2.154  30.189  1.00106.70           O  
-ANISOU14034  O3'  DT D  18     7365  15943  17233  -2827   2248    415       O  
-ATOM  14035  C2'  DT D  18     -39.903   3.863  31.938  1.00105.85           C  
-ANISOU14035  C2'  DT D  18     7269  15956  16992  -2340   2019    302       C  
-ATOM  14036  C1'  DT D  18     -38.696   3.701  32.858  1.00104.29           C  
-ANISOU14036  C1'  DT D  18     7277  15981  16368  -2226   2357    591       C  
-ATOM  14037  N1   DT D  18     -38.656   4.651  34.010  1.00105.32           N  
-ANISOU14037  N1   DT D  18     7441  16209  16365  -1924   2278    561       N  
-ATOM  14038  C2   DT D  18     -38.211   4.200  35.234  1.00104.80           C  
-ANISOU14038  C2   DT D  18     7361  16325  16134  -1717   2815    718       C  
-ATOM  14039  O2   DT D  18     -37.856   3.053  35.434  1.00102.58           O  
-ANISOU14039  O2   DT D  18     7036  16128  15811  -1766   3361    881       O  
-ATOM  14040  N3   DT D  18     -38.203   5.149  36.224  1.00105.62           N  
-ANISOU14040  N3   DT D  18     7504  16506  16120  -1445   2689    675       N  
-ATOM  14041  C4   DT D  18     -38.584   6.474  36.117  1.00107.37           C  
-ANISOU14041  C4   DT D  18     7779  16643  16373  -1361   2093    496       C  
-ATOM  14042  O4   DT D  18     -38.542   7.250  37.067  1.00107.36           O  
-ANISOU14042  O4   DT D  18     7815  16721  16257  -1109   2027    471       O  
-ATOM  14043  C5   DT D  18     -39.035   6.880  34.811  1.00108.00           C  
-ANISOU14043  C5   DT D  18     7871  16534  16629  -1589   1553    341       C  
-ATOM  14044  C7   DT D  18     -39.476   8.294  34.575  1.00110.83           C  
-ANISOU14044  C7   DT D  18     8288  16784  17037  -1522    884    141       C  
-ATOM  14045  C6   DT D  18     -39.047   5.964  33.834  1.00107.52           C  
-ANISOU14045  C6   DT D  18     7772  16398  16684  -1855   1669    380       C  
-ATOM  14046  P    DC D  19     -41.228   1.801  29.798  1.00 94.74           P  
-ANISOU14046  P    DC D  19     5492  14238  16265  -2847   2267    110       P  
-ATOM  14047  OP1  DC D  19     -41.207   1.077  28.506  1.00 94.76           O  
-ANISOU14047  OP1  DC D  19     5515  14125  16363  -3166   2205    128       O  
-ATOM  14048  OP2  DC D  19     -42.037   3.032  29.946  1.00 97.05           O  
-ANISOU14048  OP2  DC D  19     5704  14440  16730  -2690   1783   -140       O  
-ATOM  14049  O5'  DC D  19     -41.677   0.793  30.949  1.00 99.48           O  
-ANISOU14049  O5'  DC D  19     5822  14927  17048  -2645   3011    120       O  
-ATOM  14050  C5'  DC D  19     -40.721  -0.097  31.509  1.00101.73           C  
-ANISOU14050  C5'  DC D  19     6212  15383  17058  -2637   3555    398       C  
-ATOM  14051  C4'  DC D  19     -41.217  -0.517  32.873  1.00106.62           C  
-ANISOU14051  C4'  DC D  19     6598  16095  17819  -2345   4110    365       C  
-ATOM  14052  O4'  DC D  19     -40.909   0.523  33.836  1.00105.97           O  
-ANISOU14052  O4'  DC D  19     6618  16129  17518  -2091   3952    383       O  
-ATOM  14053  C3'  DC D  19     -42.728  -0.713  32.903  1.00112.18           C  
-ANISOU14053  C3'  DC D  19     6921  16654  19047  -2272   4186     69       C  
-ATOM  14054  O3'  DC D  19     -43.061  -1.937  33.534  1.00121.68           O  
-ANISOU14054  O3'  DC D  19     8106  17788  20340  -2137   4760     88       O  
-ATOM  14055  C2'  DC D  19     -43.249   0.484  33.691  1.00111.80           C  
-ANISOU14055  C2'  DC D  19     6814  16616  19049  -1993   3903   -100       C  
-ATOM  14056  C1'  DC D  19     -42.066   0.820  34.592  1.00109.15           C  
-ANISOU14056  C1'  DC D  19     6732  16487  18254  -1844   4031    146       C  
-ATOM  14057  N1   DC D  19     -42.055   2.260  35.002  1.00108.64           N  
-ANISOU14057  N1   DC D  19     6784  16437  18057  -1660   3540     55       N  
-ATOM  14058  C2   DC D  19     -41.536   2.636  36.247  1.00106.97           C  
-ANISOU14058  C2   DC D  19     6657  16399  17589  -1396   3738    169       C  
-ATOM  14059  O2   DC D  19     -41.076   1.772  37.002  1.00103.71           O  
-ANISOU14059  O2   DC D  19     6220  16128  17056  -1316   4321    349       O  
-ATOM  14060  N3   DC D  19     -41.547   3.948  36.588  1.00106.54           N  
-ANISOU14060  N3   DC D  19     6710  16349  17422  -1234   3279     79       N  
-ATOM  14061  C4   DC D  19     -42.054   4.857  35.754  1.00108.01           C  
-ANISOU14061  C4   DC D  19     6918  16378  17742  -1324   2656   -114       C  
-ATOM  14062  N4   DC D  19     -42.046   6.137  36.139  1.00107.80           N  
-ANISOU14062  N4   DC D  19     7002  16360  17596  -1155   2222   -197       N  
-ATOM  14063  C5   DC D  19     -42.592   4.492  34.486  1.00109.35           C  
-ANISOU14063  C5   DC D  19     7000  16373  18175  -1590   2448   -233       C  
-ATOM  14064  C6   DC D  19     -42.574   3.197  34.156  1.00110.21           C  
-ANISOU14064  C6   DC D  19     7005  16478  18392  -1750   2901   -144       C  
-ATOM  14065  P    DG D  20     -44.600  -2.375  33.678  1.00105.56           P  
-ANISOU14065  P    DG D  20     7943  17143  15021  -3212   3401    619       P  
-ATOM  14066  OP1  DG D  20     -44.695  -3.816  33.361  1.00106.82           O  
-ANISOU14066  OP1  DG D  20     7833  17257  15495  -3346   3722    624       O  
-ATOM  14067  OP2  DG D  20     -45.421  -1.404  32.919  1.00107.11           O  
-ANISOU14067  OP2  DG D  20     8056  17509  15132  -3159   3313    375       O  
-ATOM  14068  O5'  DG D  20     -44.910  -2.161  35.236  1.00112.66           O  
-ANISOU14068  O5'  DG D  20     9174  17980  15651  -3058   3452    752       O  
-ATOM  14069  C5'  DG D  20     -44.132  -2.811  36.238  1.00117.36           C  
-ANISOU14069  C5'  DG D  20     9945  18410  16238  -3064   3485   1006       C  
-ATOM  14070  C4'  DG D  20     -44.551  -2.364  37.630  1.00123.22           C  
-ANISOU14070  C4'  DG D  20    11011  19122  16686  -2896   3500   1095       C  
-ATOM  14071  O4'  DG D  20     -44.187  -0.973  37.838  1.00122.22           O  
-ANISOU14071  O4'  DG D  20    11150  19016  16272  -2783   3133   1114       O  
-ATOM  14072  C3'  DG D  20     -46.047  -2.461  37.918  1.00126.73           C  
-ANISOU14072  C3'  DG D  20    11392  19678  17081  -2811   3795    929       C  
-ATOM  14073  O3'  DG D  20     -46.246  -2.914  39.247  1.00137.76           O  
-ANISOU14073  O3'  DG D  20    12988  20988  18367  -2727   3968   1081       O  
-ATOM  14074  C2'  DG D  20     -46.522  -1.024  37.753  1.00123.62           C  
-ANISOU14074  C2'  DG D  20    11133  19408  16430  -2684   3559    785       C  
-ATOM  14075  C1'  DG D  20     -45.319  -0.255  38.278  1.00124.61           C  
-ANISOU14075  C1'  DG D  20    11566  19426  16353  -2634   3188    980       C  
-ATOM  14076  N9   DG D  20     -45.255   1.096  37.740  1.00124.11           N  
-ANISOU14076  N9   DG D  20    11588  19456  16114  -2572   2861    869       N  
-ATOM  14077  C8   DG D  20     -45.402   1.475  36.428  1.00124.28           C  
-ANISOU14077  C8   DG D  20    11373  19593  16253  -2645   2769    678       C  
-ATOM  14078  N7   DG D  20     -45.302   2.760  36.247  1.00123.59           N  
-ANISOU14078  N7   DG D  20    11439  19569  15952  -2561   2458    618       N  
-ATOM  14079  C5   DG D  20     -45.075   3.263  37.521  1.00123.48           C  
-ANISOU14079  C5   DG D  20    11786  19473  15659  -2423   2336    779       C  
-ATOM  14080  C6   DG D  20     -44.883   4.595  37.951  1.00123.02           C  
-ANISOU14080  C6   DG D  20    12026  19427  15288  -2287   2010    802       C  
-ATOM  14081  O6   DG D  20     -44.876   5.626  37.264  1.00124.34           O  
-ANISOU14081  O6   DG D  20    12195  19685  15363  -2263   1757    681       O  
-ATOM  14082  N1   DG D  20     -44.684   4.666  39.328  1.00121.62           N  
-ANISOU14082  N1   DG D  20    12171  19142  14896  -2171   1990    988       N  
-ATOM  14083  C2   DG D  20     -44.673   3.587  40.179  1.00121.07           C  
-ANISOU14083  C2   DG D  20    12128  18968  14904  -2186   2255   1133       C  
-ATOM  14084  N2   DG D  20     -44.468   3.856  41.477  1.00120.06           N  
-ANISOU14084  N2   DG D  20    12336  18747  14535  -2059   2188   1302       N  
-ATOM  14085  N3   DG D  20     -44.850   2.333  39.788  1.00122.66           N  
-ANISOU14085  N3   DG D  20    12049  19157  15399  -2314   2563   1115       N  
-ATOM  14086  C4   DG D  20     -45.044   2.251  38.451  1.00124.47           C  
-ANISOU14086  C4   DG D  20    11966  19488  15839  -2427   2582    935       C  
-ATOM  14087  P    DA D  21     -47.694  -3.421  39.723  1.00128.03           P  
-ANISOU14087  P    DA D  21    11674  19835  17138  -2661   4351    967       P  
-ATOM  14088  OP1  DA D  21     -47.620  -4.884  39.924  1.00130.57           O  
-ANISOU14088  OP1  DA D  21    11833  20065  17713  -2771   4661   1065       O  
-ATOM  14089  OP2  DA D  21     -48.704  -2.852  38.804  1.00132.78           O  
-ANISOU14089  OP2  DA D  21    12088  20614  17748  -2645   4379    698       O  
-ATOM  14090  O5'  DA D  21     -47.885  -2.715  41.141  1.00133.34           O  
-ANISOU14090  O5'  DA D  21    12730  20474  17461  -2469   4272   1083       O  
-ATOM  14091  C5'  DA D  21     -46.808  -2.714  42.065  1.00135.20           C  
-ANISOU14091  C5'  DA D  21    13241  20552  17578  -2440   4106   1336       C  
-ATOM  14092  C4'  DA D  21     -46.989  -1.586  43.060  1.00137.11           C  
-ANISOU14092  C4'  DA D  21    13844  20803  17450  -2246   3917   1382       C  
-ATOM  14093  O4'  DA D  21     -46.667  -0.326  42.417  1.00128.72           O  
-ANISOU14093  O4'  DA D  21    12855  19807  16246  -2212   3561   1293       O  
-ATOM  14094  C3'  DA D  21     -48.413  -1.450  43.585  1.00142.49           C  
-ANISOU14094  C3'  DA D  21    14547  21594  17998  -2114   4160   1253       C  
-ATOM  14095  O3'  DA D  21     -48.393  -1.170  44.978  1.00156.11           O  
-ANISOU14095  O3'  DA D  21    16610  23246  19458  -1962   4135   1411       O  
-ATOM  14096  C2'  DA D  21     -48.978  -0.284  42.780  1.00132.83           C  
-ANISOU14096  C2'  DA D  21    13282  20528  16658  -2058   3980   1029       C  
-ATOM  14097  C1'  DA D  21     -47.740   0.579  42.577  1.00123.16           C  
-ANISOU14097  C1'  DA D  21    12237  19236  15321  -2066   3557   1129       C  
-ATOM  14098  N9   DA D  21     -47.825   1.422  41.388  1.00108.76           N  
-ANISOU14098  N9   DA D  21    10279  17533  13512  -2097   3352    938       N  
-ATOM  14099  C8   DA D  21     -47.913   1.007  40.089  1.00104.27           C  
-ANISOU14099  C8   DA D  21     9366  17036  13217  -2244   3424    790       C  
-ATOM  14100  N7   DA D  21     -47.980   1.990  39.223  1.00 98.15           N  
-ANISOU14100  N7   DA D  21     8545  16366  12380  -2235   3194    635       N  
-ATOM  14101  C5   DA D  21     -47.933   3.127  40.007  1.00 94.51           C  
-ANISOU14101  C5   DA D  21     8423  15903  11584  -2071   2951    685       C  
-ATOM  14102  C6   DA D  21     -47.965   4.496  39.686  1.00 89.56           C  
-ANISOU14102  C6   DA D  21     7926  15360  10741  -1983   2640    583       C  
-ATOM  14103  N6   DA D  21     -48.055   4.955  38.435  1.00 88.47           N  
-ANISOU14103  N6   DA D  21     7580  15332  10702  -2052   2520    403       N  
-ATOM  14104  N1   DA D  21     -47.901   5.376  40.706  1.00 87.15           N  
-ANISOU14104  N1   DA D  21     7977  15022  10113  -1819   2454    674       N  
-ATOM  14105  C2   DA D  21     -47.812   4.910  41.959  1.00 86.84           C  
-ANISOU14105  C2   DA D  21     8147  14874   9975  -1747   2576    854       C  
-ATOM  14106  N3   DA D  21     -47.774   3.647  42.382  1.00 92.68           N  
-ANISOU14106  N3   DA D  21     8791  15528  10895  -1818   2867    965       N  
-ATOM  14107  C4   DA D  21     -47.838   2.797  41.345  1.00 99.08           C  
-ANISOU14107  C4   DA D  21     9246  16373  12026  -1983   3044    871       C  
-ATOM  14108  P    DT D  22     -49.696  -1.448  45.876  1.00159.52           P  
-ANISOU14108  P    DT D  22    17088  23739  19783  -1834   4460   1365       P  
-ATOM  14109  OP1  DT D  22     -49.302  -2.342  46.987  1.00164.56           O  
-ANISOU14109  OP1  DT D  22    17857  24232  20435  -1828   4620   1592       O  
-ATOM  14110  OP2  DT D  22     -50.794  -1.856  44.970  1.00164.21           O  
-ANISOU14110  OP2  DT D  22    17342  24476  20573  -1899   4722   1135       O  
-ATOM  14111  O5'  DT D  22     -50.056  -0.006  46.466  1.00160.35           O  
-ANISOU14111  O5'  DT D  22    17509  23911  19506  -1629   4222   1323       O  
-ATOM  14112  C5'  DT D  22     -50.374   1.044  45.568  1.00154.55           C  
-ANISOU14112  C5'  DT D  22    16718  23308  18695  -1605   4019   1125       C  
-ATOM  14113  C4'  DT D  22     -50.195   2.400  46.219  1.00148.78           C  
-ANISOU14113  C4'  DT D  22    16348  22580  17601  -1431   3699   1163       C  
-ATOM  14114  O4'  DT D  22     -49.723   3.325  45.207  1.00138.97           O  
-ANISOU14114  O4'  DT D  22    15067  21392  16344  -1473   3375   1059       O  
-ATOM  14115  C3'  DT D  22     -51.473   3.015  46.768  1.00149.84           C  
-ANISOU14115  C3'  DT D  22    16595  22837  17499  -1250   3813   1037       C  
-ATOM  14116  O3'  DT D  22     -51.191   3.961  47.792  1.00155.29           O  
-ANISOU14116  O3'  DT D  22    17677  23478  17850  -1077   3574   1150       O  
-ATOM  14117  C2'  DT D  22     -52.034   3.699  45.528  1.00140.85           C  
-ANISOU14117  C2'  DT D  22    15251  21860  16406  -1280   3728    783       C  
-ATOM  14118  C1'  DT D  22     -50.765   4.216  44.855  1.00129.60           C  
-ANISOU14118  C1'  DT D  22    13860  20370  15013  -1370   3357    840       C  
-ATOM  14119  N1   DT D  22     -50.886   4.289  43.366  1.00114.10           N  
-ANISOU14119  N1   DT D  22    11577  18513  13262  -1502   3322    643       N  
-ATOM  14120  C2   DT D  22     -50.949   5.526  42.762  1.00105.73           C  
-ANISOU14120  C2   DT D  22    10571  17551  12052  -1448   3037    505       C  
-ATOM  14121  O2   DT D  22     -50.901   6.574  43.378  1.00103.47           O  
-ANISOU14121  O2   DT D  22    10582  17265  11466  -1298   2806    536       O  
-ATOM  14122  N3   DT D  22     -51.066   5.496  41.396  1.00100.10           N  
-ANISOU14122  N3   DT D  22     9549  16933  11553  -1574   3029    328       N  
-ATOM  14123  C4   DT D  22     -51.132   4.376  40.589  1.00 97.11           C  
-ANISOU14123  C4   DT D  22     8822  16560  11514  -1745   3272    274       C  
-ATOM  14124  O4   DT D  22     -51.238   4.451  39.368  1.00 96.56           O  
-ANISOU14124  O4   DT D  22     8494  16580  11615  -1846   3241    110       O  
-ATOM  14125  C5   DT D  22     -51.067   3.116  41.285  1.00 99.39           C  
-ANISOU14125  C5   DT D  22     9076  16743  11944  -1793   3562    423       C  
-ATOM  14126  C7   DT D  22     -51.129   1.830  40.517  1.00 94.32           C  
-ANISOU14126  C7   DT D  22     8074  16095  11669  -1973   3837    381       C  
-ATOM  14127  C6   DT D  22     -50.949   3.131  42.620  1.00105.42           C  
-ANISOU14127  C6   DT D  22    10137  17415  12504  -1672   3574    599       C  
-ATOM  14128  P    DG D  23     -52.351   4.428  48.800  1.00163.51           P  
-ANISOU14128  P    DG D  23    18917  24598  18610   -865   3713   1103       P  
-ATOM  14129  OP1  DG D  23     -51.862   4.229  50.181  1.00166.88           O  
-ANISOU14129  OP1  DG D  23    19652  24883  18870   -769   3705   1340       O  
-ATOM  14130  OP2  DG D  23     -53.614   3.795  48.364  1.00165.72           O  
-ANISOU14130  OP2  DG D  23    18901  25009  19055   -895   4081    925       O  
-ATOM  14131  O5'  DG D  23     -52.479   5.999  48.528  1.00161.97           O  
-ANISOU14131  O5'  DG D  23    18902  24497  18142   -740   3370    977       O  
-ATOM  14132  C5'  DG D  23     -51.469   6.891  48.987  1.00159.01           C  
-ANISOU14132  C5'  DG D  23    18850  24024  17543   -671   2986   1116       C  
-ATOM  14133  C4'  DG D  23     -51.872   8.340  48.767  1.00153.68           C  
-ANISOU14133  C4'  DG D  23    18327  23462  16604   -536   2720    967       C  
-ATOM  14134  O4'  DG D  23     -52.060   8.587  47.351  1.00146.90           O  
-ANISOU14134  O4'  DG D  23    17180  22721  15916   -650   2663    763       O  
-ATOM  14135  C3'  DG D  23     -53.172   8.773  49.434  1.00154.13           C  
-ANISOU14135  C3'  DG D  23    18498  23632  16431   -346   2885    861       C  
-ATOM  14136  O3'  DG D  23     -53.100  10.150  49.789  1.00153.56           O  
-ANISOU14136  O3'  DG D  23    18734  23583  16028   -184   2559    843       O  
-ATOM  14137  C2'  DG D  23     -54.215   8.526  48.348  1.00149.56           C  
-ANISOU14137  C2'  DG D  23    17557  23221  16048   -421   3112    612       C  
-ATOM  14138  C1'  DG D  23     -53.433   8.778  47.061  1.00140.41           C  
-ANISOU14138  C1'  DG D  23    16217  22067  15065   -581   2871    544       C  
-ATOM  14139  N9   DG D  23     -53.785   7.862  45.980  1.00130.18           N  
-ANISOU14139  N9   DG D  23    14510  20837  14114   -756   3121    415       N  
-ATOM  14140  C8   DG D  23     -54.148   6.541  46.107  1.00126.74           C  
-ANISOU14140  C8   DG D  23    13866  20377  13914   -843   3494    450       C  
-ATOM  14141  N7   DG D  23     -54.403   5.963  44.966  1.00122.69           N  
-ANISOU14141  N7   DG D  23    12993  19933  13689   -998   3641    308       N  
-ATOM  14142  C5   DG D  23     -54.193   6.963  44.023  1.00120.69           C  
-ANISOU14142  C5   DG D  23    12708  19758  13390  -1014   3350    172       C  
-ATOM  14143  C6   DG D  23     -54.318   6.926  42.614  1.00116.71           C  
-ANISOU14143  C6   DG D  23    11883  19349  13111  -1151   3342    -12       C  
-ATOM  14144  O6   DG D  23     -54.647   5.971  41.899  1.00117.07           O  
-ANISOU14144  O6   DG D  23    11602  19430  13450  -1290   3599    -94       O  
-ATOM  14145  N1   DG D  23     -54.017   8.155  42.033  1.00114.01           N  
-ANISOU14145  N1   DG D  23    11629  19066  12625  -1115   2992   -103       N  
-ATOM  14146  C2   DG D  23     -53.642   9.279  42.727  1.00114.67           C  
-ANISOU14146  C2   DG D  23    12067  19116  12387   -967   2683    -25       C  
-ATOM  14147  N2   DG D  23     -53.394  10.370  41.988  1.00111.98           N  
-ANISOU14147  N2   DG D  23    11753  18840  11953   -957   2367   -133       N  
-ATOM  14148  N3   DG D  23     -53.520   9.330  44.048  1.00118.65           N  
-ANISOU14148  N3   DG D  23    12878  19527  12675   -836   2683    146       N  
-ATOM  14149  C4   DG D  23     -53.811   8.139  44.629  1.00122.50           C  
-ANISOU14149  C4   DG D  23    13284  19961  13301   -868   3026    236       C  
-TER   14150       DG D  23                                                      
-ATOM  14151  O5'  DT E  26     -54.251   5.797  31.553  1.00190.57           O  
-ANISOU14151  O5'  DT E  26    19866  28863  23680   -931    498  -4317       O  
-ATOM  14152  C5'  DT E  26     -54.843   6.356  30.384  1.00189.08           C  
-ANISOU14152  C5'  DT E  26    19368  28775  23698   -885    -66  -4376       C  
-ATOM  14153  C4'  DT E  26     -55.561   7.659  30.696  1.00189.56           C  
-ANISOU14153  C4'  DT E  26    19018  28696  24309   -742   -788  -4759       C  
-ATOM  14154  O4'  DT E  26     -56.511   7.436  31.774  1.00187.68           O  
-ANISOU14154  O4'  DT E  26    18673  28412  24226   -817   -447  -5575       O  
-ATOM  14155  C3'  DT E  26     -54.660   8.799  31.163  1.00187.01           C  
-ANISOU14155  C3'  DT E  26    18685  28149  24220   -542  -1377  -4221       C  
-ATOM  14156  O3'  DT E  26     -55.179  10.066  30.747  1.00189.09           O  
-ANISOU14156  O3'  DT E  26    18553  28347  24947   -394  -2219  -4334       O  
-ATOM  14157  C2'  DT E  26     -54.725   8.634  32.676  1.00183.16           C  
-ANISOU14157  C2'  DT E  26    18297  27514  23782   -567   -983  -4596       C  
-ATOM  14158  C1'  DT E  26     -56.204   8.305  32.849  1.00183.89           C  
-ANISOU14158  C1'  DT E  26    18139  27700  24032   -683   -756  -5545       C  
-ATOM  14159  N1   DT E  26     -56.524   7.647  34.157  1.00178.41           N  
-ANISOU14159  N1   DT E  26    17579  26947  23261   -789   -107  -6071       N  
-ATOM  14160  C2   DT E  26     -56.785   8.433  35.260  1.00176.95           C  
-ANISOU14160  C2   DT E  26    17233  26567  23433   -695   -362  -6395       C  
-ATOM  14161  O2   DT E  26     -56.774   9.649  35.234  1.00179.72           O  
-ANISOU14161  O2   DT E  26    17333  26787  24165   -528  -1095  -6280       O  
-ATOM  14162  N3   DT E  26     -57.063   7.738  36.409  1.00174.91           N  
-ANISOU14162  N3   DT E  26    17118  26270  23068   -805    277  -6865       N  
-ATOM  14163  C4   DT E  26     -57.104   6.365  36.565  1.00170.82           C  
-ANISOU14163  C4   DT E  26    16886  25886  22133   -996   1130  -7039       C  
-ATOM  14164  O4   DT E  26     -57.364   5.832  37.640  1.00172.36           O  
-ANISOU14164  O4   DT E  26    17192  26032  22264  -1084   1658  -7468       O  
-ATOM  14165  C5   DT E  26     -56.821   5.604  35.375  1.00170.17           C  
-ANISOU14165  C5   DT E  26    16961  26004  21693  -1085   1353  -6681       C  
-ATOM  14166  C7   DT E  26     -56.837   4.106  35.421  1.00163.47           C  
-ANISOU14166  C7   DT E  26    16424  25311  20375  -1291   2260  -6828       C  
-ATOM  14167  C6   DT E  26     -56.549   6.270  34.245  1.00172.50           C  
-ANISOU14167  C6   DT E  26    17116  26340  22087   -979    735  -6222       C  
-ATOM  14168  P    DC E  27     -54.219  11.356  30.687  1.00177.96           P  
-ANISOU14168  P    DC E  27    17090  26752  23776   -174  -2998  -3637       P  
-ATOM  14169  OP1  DC E  27     -54.409  12.005  29.371  1.00182.89           O  
-ANISOU14169  OP1  DC E  27    17473  27461  24557    -96  -3645  -3414       O  
-ATOM  14170  OP2  DC E  27     -52.865  10.937  31.109  1.00178.51           O  
-ANISOU14170  OP2  DC E  27    17565  26752  23507   -168  -2660  -2955       O  
-ATOM  14171  O5'  DC E  27     -54.832  12.335  31.796  1.00174.51           O  
-ANISOU14171  O5'  DC E  27    16376  26113  23818    -68  -3368  -4156       O  
-ATOM  14172  C5'  DC E  27     -55.405  11.802  32.987  1.00164.18           C  
-ANISOU14172  C5'  DC E  27    15110  24760  22510   -167  -2818  -4798       C  
-ATOM  14173  C4'  DC E  27     -54.797  12.431  34.227  1.00157.03           C  
-ANISOU14173  C4'  DC E  27    14276  23617  21773    -54  -2948  -4645       C  
-ATOM  14174  O4'  DC E  27     -54.953  11.531  35.355  1.00151.58           O  
-ANISOU14174  O4'  DC E  27    13794  22909  20892   -184  -2190  -5055       O  
-ATOM  14175  C3'  DC E  27     -53.307  12.734  34.120  1.00153.49           C  
-ANISOU14175  C3'  DC E  27    14090  23071  21158     56  -3144  -3707       C  
-ATOM  14176  O3'  DC E  27     -53.087  14.091  34.483  1.00149.95           O  
-ANISOU14176  O3'  DC E  27    13434  22421  21121    249  -3882  -3537       O  
-ATOM  14177  C2'  DC E  27     -52.647  11.758  35.094  1.00148.95           C  
-ANISOU14177  C2'  DC E  27    13910  22465  20220    -45  -2369  -3602       C  
-ATOM  14178  C1'  DC E  27     -53.756  11.486  36.103  1.00143.24           C  
-ANISOU14178  C1'  DC E  27    13049  21715  19660   -135  -2012  -4503       C  
-ATOM  14179  N1   DC E  27     -53.657  10.144  36.766  1.00132.76           N  
-ANISOU14179  N1   DC E  27    12054  20457  17931   -312  -1082  -4697       N  
-ATOM  14180  C2   DC E  27     -53.684  10.037  38.165  1.00128.08           C  
-ANISOU14180  C2   DC E  27    11550  19723  17390   -330   -744  -5020       C  
-ATOM  14181  O2   DC E  27     -53.793  11.060  38.854  1.00130.86           O  
-ANISOU14181  O2   DC E  27    11703  19893  18123   -199  -1220  -5146       O  
-ATOM  14182  N3   DC E  27     -53.593   8.805  38.729  1.00121.94           N  
-ANISOU14182  N3   DC E  27    11078  19013  16241   -492    101  -5188       N  
-ATOM  14183  C4   DC E  27     -53.477   7.719  37.961  1.00119.34           C  
-ANISOU14183  C4   DC E  27    10959  18881  15505   -631    600  -5047       C  
-ATOM  14184  N4   DC E  27     -53.390   6.528  38.563  1.00117.91           N  
-ANISOU14184  N4   DC E  27    11077  18757  14967   -788   1429  -5222       N  
-ATOM  14185  C5   DC E  27     -53.445   7.809  36.539  1.00120.01           C  
-ANISOU14185  C5   DC E  27    10956  19111  15531   -616    268  -4719       C  
-ATOM  14186  C6   DC E  27     -53.537   9.026  35.993  1.00125.38           C  
-ANISOU14186  C6   DC E  27    11335  19724  16579   -456   -565  -4556       C  
-ATOM  14187  P    DA E  28     -51.763  14.857  33.988  1.00164.31           P  
-ANISOU14187  P    DA E  28    15364  24143  22923    411  -4430  -2578       P  
-ATOM  14188  OP1  DA E  28     -51.864  16.267  34.423  1.00166.72           O  
-ANISOU14188  OP1  DA E  28    15385  24246  23714    596  -5184  -2611       O  
-ATOM  14189  OP2  DA E  28     -51.565  14.545  32.555  1.00165.50           O  
-ANISOU14189  OP2  DA E  28    15548  24478  22856    378  -4524  -2180       O  
-ATOM  14190  O5'  DA E  28     -50.594  14.165  34.832  1.00154.28           O  
-ANISOU14190  O5'  DA E  28    14533  22803  21283    371  -3847  -2120       O  
-ATOM  14191  C5'  DA E  28     -49.568  14.949  35.416  1.00143.18           C  
-ANISOU14191  C5'  DA E  28    13223  21197  19980    521  -4195  -1567       C  
-ATOM  14192  C4'  DA E  28     -49.769  15.076  36.915  1.00138.13           C  
-ANISOU14192  C4'  DA E  28    12590  20390  19504    528  -3977  -1996       C  
-ATOM  14193  O4'  DA E  28     -50.520  13.936  37.414  1.00140.25           O  
-ANISOU14193  O4'  DA E  28    12951  20766  19573    342  -3204  -2645       O  
-ATOM  14194  C3'  DA E  28     -48.470  15.104  37.708  1.00130.43           C  
-ANISOU14194  C3'  DA E  28    11933  19266  18358    590  -3833  -1389       C  
-ATOM  14195  O3'  DA E  28     -48.600  15.942  38.852  1.00117.64           O  
-ANISOU14195  O3'  DA E  28    10173  17435  17090    693  -4107  -1641       O  
-ATOM  14196  C2'  DA E  28     -48.299  13.639  38.089  1.00134.03           C  
-ANISOU14196  C2'  DA E  28    12743  19837  18347    405  -2887  -1490       C  
-ATOM  14197  C1'  DA E  28     -49.739  13.217  38.351  1.00137.73           C  
-ANISOU14197  C1'  DA E  28    12996  20388  18947    282  -2591  -2439       C  
-ATOM  14198  N9   DA E  28     -49.928  11.779  38.168  1.00139.45           N  
-ANISOU14198  N9   DA E  28    13457  20793  18734     83  -1771  -2632       N  
-ATOM  14199  C8   DA E  28     -49.903  11.095  36.986  1.00138.01           C  
-ANISOU14199  C8   DA E  28    13359  20814  18264     -5  -1595  -2423       C  
-ATOM  14200  N7   DA E  28     -50.093   9.803  37.115  1.00137.13           N  
-ANISOU14200  N7   DA E  28    13477  20838  17787   -186   -801  -2672       N  
-ATOM  14201  C5   DA E  28     -50.250   9.623  38.477  1.00139.17           C  
-ANISOU14201  C5   DA E  28    13810  20974  18093   -218   -428  -3069       C  
-ATOM  14202  C6   DA E  28     -50.484   8.474  39.257  1.00139.26           C  
-ANISOU14202  C6   DA E  28    14049  21035  17827   -383    408  -3469       C  
-ATOM  14203  N6   DA E  28     -50.603   7.245  38.744  1.00133.94           N  
-ANISOU14203  N6   DA E  28    13578  20555  16758   -551   1041  -3534       N  
-ATOM  14204  N1   DA E  28     -50.589   8.640  40.591  1.00143.15           N  
-ANISOU14204  N1   DA E  28    14554  21369  18466   -368    569  -3800       N  
-ATOM  14205  C2   DA E  28     -50.469   9.873  41.100  1.00148.51           C  
-ANISOU14205  C2   DA E  28    15031  21855  19542   -200    -66  -3734       C  
-ATOM  14206  N3   DA E  28     -50.250  11.026  40.468  1.00147.13           N  
-ANISOU14206  N3   DA E  28    14633  21613  19657    -35   -875  -3374       N  
-ATOM  14207  C4   DA E  28     -50.148  10.831  39.143  1.00141.04           C  
-ANISOU14207  C4   DA E  28    13855  21002  18731    -54  -1017  -3049       C  
-ATOM  14208  P    DT E  29     -47.310  16.301  39.742  1.00119.28           P  
-ANISOU14208  P    DT E  29    10634  17450  17238    797  -4141  -1033       P  
-ATOM  14209  OP1  DT E  29     -47.223  17.775  39.849  1.00116.44           O  
-ANISOU14209  OP1  DT E  29    10001  16909  17332    992  -4993   -883       O  
-ATOM  14210  OP2  DT E  29     -46.160  15.533  39.214  1.00112.92           O  
-ANISOU14210  OP2  DT E  29    10207  16737  15960    749  -3784   -301       O  
-ATOM  14211  O5'  DT E  29     -47.665  15.692  41.176  1.00114.75           O  
-ANISOU14211  O5'  DT E  29    10178  16806  16617    698  -3500  -1600       O  
-ATOM  14212  C5'  DT E  29     -48.105  14.345  41.246  1.00115.13           C  
-ANISOU14212  C5'  DT E  29    10407  17015  16322    502  -2689  -1987       C  
-ATOM  14213  C4'  DT E  29     -47.465  13.607  42.404  1.00112.04           C  
-ANISOU14213  C4'  DT E  29    10364  16553  15653    433  -2022  -1912       C  
-ATOM  14214  O4'  DT E  29     -47.726  12.189  42.245  1.00113.12           O  
-ANISOU14214  O4'  DT E  29    10727  16873  15379    236  -1212  -2150       O  
-ATOM  14215  C3'  DT E  29     -45.954  13.758  42.525  1.00109.53           C  
-ANISOU14215  C3'  DT E  29    10349  16141  15126    524  -2084  -1026       C  
-ATOM  14216  O3'  DT E  29     -45.615  13.858  43.914  1.00108.42           O  
-ANISOU14216  O3'  DT E  29    10332  15828  15036    549  -1871  -1111       O  
-ATOM  14217  C2'  DT E  29     -45.419  12.503  41.835  1.00108.77           C  
-ANISOU14217  C2'  DT E  29    10591  16234  14504    388  -1473   -664       C  
-ATOM  14218  C1'  DT E  29     -46.519  11.472  42.074  1.00112.43           C  
-ANISOU14218  C1'  DT E  29    11040  16830  14848    202   -817  -1454       C  
-ATOM  14219  N1   DT E  29     -46.709  10.500  40.949  1.00117.38           N  
-ANISOU14219  N1   DT E  29    11768  17692  15140     68   -459  -1409       N  
-ATOM  14220  C2   DT E  29     -47.020   9.188  41.237  1.00118.70           C  
-ANISOU14220  C2   DT E  29    12154  17982  14964   -118    375  -1762       C  
-ATOM  14221  O2   DT E  29     -47.152   8.762  42.369  1.00119.92           O  
-ANISOU14221  O2   DT E  29    12427  18066  15071   -182    848  -2114       O  
-ATOM  14222  N3   DT E  29     -47.175   8.378  40.143  1.00121.95           N  
-ANISOU14222  N3   DT E  29    12643  18607  15087   -231    644  -1690       N  
-ATOM  14223  C4   DT E  29     -47.051   8.740  38.816  1.00124.35           C  
-ANISOU14223  C4   DT E  29    12829  19010  15408   -177    171  -1308       C  
-ATOM  14224  O4   DT E  29     -47.209   7.940  37.899  1.00128.52           O  
-ANISOU14224  O4   DT E  29    13441  19731  15660   -289    469  -1275       O  
-ATOM  14225  C5   DT E  29     -46.726  10.123  38.584  1.00124.40           C  
-ANISOU14225  C5   DT E  29    12609  18879  15780     20   -696   -950       C  
-ATOM  14226  C7   DT E  29     -46.569  10.627  37.181  1.00126.72           C  
-ANISOU14226  C7   DT E  29    12761  19263  16124     93  -1268   -519       C  
-ATOM  14227  C6   DT E  29     -46.572  10.926  39.644  1.00120.59           C  
-ANISOU14227  C6   DT E  29    12049  18186  15582    131   -966  -1017       C  
-ATOM  14228  P    DC E  30     -44.167  13.394  44.437  1.00108.42           P  
-ANISOU14228  P    DC E  30    10765  15763  14666    558  -1490   -398       P  
-ATOM  14229  OP1  DC E  30     -43.918  14.053  45.737  1.00105.32           O  
-ANISOU14229  OP1  DC E  30    10356  15151  14509    651  -1627   -472       O  
-ATOM  14230  OP2  DC E  30     -43.203  13.565  43.329  1.00104.61           O  
-ANISOU14230  OP2  DC E  30    10399  15340  14007    628  -1805    423       O  
-ATOM  14231  O5'  DC E  30     -44.350  11.832  44.701  1.00107.74           O  
-ANISOU14231  O5'  DC E  30    10974  15825  14136    349   -515   -689       O  
-ATOM  14232  C5'  DC E  30     -45.094  11.394  45.822  1.00112.13           C  
-ANISOU14232  C5'  DC E  30    11518  16341  14746    253    -38  -1403       C  
-ATOM  14233  C4'  DC E  30     -44.647   9.997  46.192  1.00114.15           C  
-ANISOU14233  C4'  DC E  30    12179  16689  14505     95    862  -1327       C  
-ATOM  14234  O4'  DC E  30     -44.922   9.113  45.076  1.00113.51           O  
-ANISOU14234  O4'  DC E  30    12164  16831  14132    -29   1170  -1327       O  
-ATOM  14235  C3'  DC E  30     -43.154   9.869  46.467  1.00115.34           C  
-ANISOU14235  C3'  DC E  30    12690  16763  14370    154    994   -507       C  
-ATOM  14236  O3'  DC E  30     -42.942   8.869  47.453  1.00118.83           O  
-ANISOU14236  O3'  DC E  30    13437  17198  14514     35   1777   -668       O  
-ATOM  14237  C2'  DC E  30     -42.619   9.447  45.104  1.00113.13           C  
-ANISOU14237  C2'  DC E  30    12542  16651  13790    130    980     64       C  
-ATOM  14238  C1'  DC E  30     -43.721   8.499  44.656  1.00110.11           C  
-ANISOU14238  C1'  DC E  30    12097  16461  13277    -45   1454   -574       C  
-ATOM  14239  N1   DC E  30     -43.751   8.302  43.183  1.00107.24           N  
-ANISOU14239  N1   DC E  30    11692  16278  12777    -70   1285   -298       N  
-ATOM  14240  C2   DC E  30     -44.178   7.085  42.642  1.00105.36           C  
-ANISOU14240  C2   DC E  30    11588  16244  12201   -247   1902   -538       C  
-ATOM  14241  O2   DC E  30     -44.536   6.178  43.400  1.00105.39           O  
-ANISOU14241  O2   DC E  30    11744  16276  12023   -383   2587   -983       O  
-ATOM  14242  N3   DC E  30     -44.192   6.933  41.295  1.00105.50           N  
-ANISOU14242  N3   DC E  30    11562  16423  12099   -267   1732   -276       N  
-ATOM  14243  C4   DC E  30     -43.798   7.933  40.506  1.00106.10           C  
-ANISOU14243  C4   DC E  30    11474  16462  12377   -118    985    205       C  
-ATOM  14244  N4   DC E  30     -43.826   7.740  39.183  1.00107.24           N  
-ANISOU14244  N4   DC E  30    11583  16771  12392   -145    843    450       N  
-ATOM  14245  C5   DC E  30     -43.356   9.179  41.040  1.00106.03           C  
-ANISOU14245  C5   DC E  30    11331  16245  12712     63    349    458       C  
-ATOM  14246  C6   DC E  30     -43.347   9.317  42.369  1.00105.81           C  
-ANISOU14246  C6   DC E  30    11345  16059  12800     81    525    195       C  
-ATOM  14247  P    DG E  31     -41.450   8.444  47.874  1.00122.95           P  
-ANISOU14247  P    DG E  31    14388  17662  14665     58   2112     97       P  
-ATOM  14248  OP1  DG E  31     -41.278   8.746  49.311  1.00122.82           O  
-ANISOU14248  OP1  DG E  31    14419  17456  14790    101   2211    -78       O  
-ATOM  14249  OP2  DG E  31     -40.510   9.023  46.889  1.00122.35           O  
-ANISOU14249  OP2  DG E  31    14340  17593  14554    181   1579    908       O  
-ATOM  14250  O5'  DG E  31     -41.449   6.858  47.682  1.00121.06           O  
-ANISOU14250  O5'  DG E  31    14471  17609  13917   -141   3014     12       O  
-ATOM  14251  C5'  DG E  31     -41.961   6.311  46.480  1.00123.08           C  
-ANISOU14251  C5'  DG E  31    14669  18068  14026   -234   3105    -85       C  
-ATOM  14252  C4'  DG E  31     -41.585   4.853  46.334  1.00121.69           C  
-ANISOU14252  C4'  DG E  31    14872  18044  13319   -398   3942     53       C  
-ATOM  14253  O4'  DG E  31     -41.793   4.474  44.951  1.00123.11           O  
-ANISOU14253  O4'  DG E  31    15014  18419  13343   -455   3901    187       O  
-ATOM  14254  C3'  DG E  31     -40.125   4.532  46.615  1.00118.82           C  
-ANISOU14254  C3'  DG E  31    14901  17628  12618   -360   4186    837       C  
-ATOM  14255  O3'  DG E  31     -40.000   3.152  46.953  1.00115.44           O  
-ANISOU14255  O3'  DG E  31    14809  17299  11753   -525   5070    731       O  
-ATOM  14256  C2'  DG E  31     -39.482   4.859  45.271  1.00120.05           C  
-ANISOU14256  C2'  DG E  31    15053  17867  12692   -283   3734   1524       C  
-ATOM  14257  C1'  DG E  31     -40.545   4.369  44.291  1.00121.13           C  
-ANISOU14257  C1'  DG E  31    15016  18201  12808   -401   3836   1058       C  
-ATOM  14258  N9   DG E  31     -40.591   5.137  43.048  1.00122.04           N  
-ANISOU14258  N9   DG E  31    14894  18372  13105   -307   3140   1351       N  
-ATOM  14259  C8   DG E  31     -40.352   6.481  42.893  1.00121.96           C  
-ANISOU14259  C8   DG E  31    14646  18229  13466   -126   2313   1634       C  
-ATOM  14260  N7   DG E  31     -40.462   6.891  41.659  1.00122.55           N  
-ANISOU14260  N7   DG E  31    14547  18397  13620    -80   1832   1859       N  
-ATOM  14261  C5   DG E  31     -40.799   5.746  40.950  1.00122.99           C  
-ANISOU14261  C5   DG E  31    14731  18661  13337   -242   2374   1714       C  
-ATOM  14262  C6   DG E  31     -41.049   5.573  39.570  1.00123.85           C  
-ANISOU14262  C6   DG E  31    14751  18948  13360   -279   2210   1840       C  
-ATOM  14263  O6   DG E  31     -41.021   6.427  38.673  1.00123.72           O  
-ANISOU14263  O6   DG E  31    14515  18937  13555   -171   1530   2113       O  
-ATOM  14264  N1   DG E  31     -41.357   4.250  39.267  1.00124.91           N  
-ANISOU14264  N1   DG E  31    15080  19265  13117   -463   2939   1612       N  
-ATOM  14265  C2   DG E  31     -41.417   3.223  40.179  1.00125.09           C  
-ANISOU14265  C2   DG E  31    15353  19297  12878   -595   3725   1303       C  
-ATOM  14266  N2   DG E  31     -41.732   2.012  39.695  1.00126.35           N  
-ANISOU14266  N2   DG E  31    15674  19646  12686   -766   4352   1118       N  
-ATOM  14267  N3   DG E  31     -41.183   3.374  41.477  1.00123.81           N  
-ANISOU14267  N3   DG E  31    15279  18970  12794   -562   3885   1184       N  
-ATOM  14268  C4   DG E  31     -40.882   4.658  41.790  1.00122.56           C  
-ANISOU14268  C4   DG E  31    14932  18633  13002   -383   3182   1402       C  
-ATOM  14269  P    DA E  32     -38.564   2.535  47.336  1.00136.12           P  
-ANISOU14269  P    DA E  32    17466  17520  16733  -1737   3397   1598       P  
-ATOM  14270  OP1  DA E  32     -38.724   1.742  48.574  1.00137.33           O  
-ANISOU14270  OP1  DA E  32    17957  17503  16720  -1862   3360   1742       O  
-ATOM  14271  OP2  DA E  32     -37.572   3.633  47.302  1.00134.76           O  
-ANISOU14271  OP2  DA E  32    17146  17369  16688  -1435   3276   1543       O  
-ATOM  14272  O5'  DA E  32     -38.265   1.517  46.136  1.00135.26           O  
-ANISOU14272  O5'  DA E  32    17352  17232  16808  -1792   3379   1523       O  
-ATOM  14273  C5'  DA E  32     -39.267   0.588  45.727  1.00133.87           C  
-ANISOU14273  C5'  DA E  32    17219  17086  16560  -2072   3518   1531       C  
-ATOM  14274  C4'  DA E  32     -38.841  -0.214  44.504  1.00131.93           C  
-ANISOU14274  C4'  DA E  32    16935  16678  16515  -2077   3485   1443       C  
-ATOM  14275  O4'  DA E  32     -38.944   0.591  43.300  1.00125.69           O  
-ANISOU14275  O4'  DA E  32    15799  16106  15852  -1991   3558   1305       O  
-ATOM  14276  C3'  DA E  32     -37.413  -0.744  44.529  1.00132.11           C  
-ANISOU14276  C3'  DA E  32    17130  16354  16712  -1885   3271   1450       C  
-ATOM  14277  O3'  DA E  32     -37.368  -2.008  43.887  1.00136.82           O  
-ANISOU14277  O3'  DA E  32    17846  16746  17393  -2014   3261   1437       O  
-ATOM  14278  C2'  DA E  32     -36.646   0.309  43.736  1.00125.63           C  
-ANISOU14278  C2'  DA E  32    16033  15622  16077  -1620   3212   1333       C  
-ATOM  14279  C1'  DA E  32     -37.676   0.713  42.687  1.00120.50           C  
-ANISOU14279  C1'  DA E  32    15086  15276  15423  -1744   3404   1234       C  
-ATOM  14280  N9   DA E  32     -37.544   2.095  42.243  1.00111.02           N  
-ANISOU14280  N9   DA E  32    13575  14320  14289  -1557   3431   1143       N  
-ATOM  14281  C8   DA E  32     -37.245   3.185  43.014  1.00108.66           C  
-ANISOU14281  C8   DA E  32    13224  14126  13935  -1389   3383   1171       C  
-ATOM  14282  N7   DA E  32     -37.198   4.311  42.344  1.00102.74           N  
-ANISOU14282  N7   DA E  32    12167  13601  13270  -1244   3425   1071       N  
-ATOM  14283  C5   DA E  32     -37.488   3.932  41.044  1.00 99.78           C  
-ANISOU14283  C5   DA E  32    11630  13271  13011  -1321   3508    970       C  
-ATOM  14284  C6   DA E  32     -37.597   4.660  39.847  1.00 94.54           C  
-ANISOU14284  C6   DA E  32    10634  12813  12473  -1239   3586    838       C  
-ATOM  14285  N6   DA E  32     -37.414   5.982  39.772  1.00 92.02           N  
-ANISOU14285  N6   DA E  32    10076  12700  12186  -1054   3593    784       N  
-ATOM  14286  N1   DA E  32     -37.903   3.972  38.729  1.00 92.28           N  
-ANISOU14286  N1   DA E  32    10273  12511  12279  -1353   3655    764       N  
-ATOM  14287  C2   DA E  32     -38.086   2.651  38.809  1.00 93.86           C  
-ANISOU14287  C2   DA E  32    10711  12503  12448  -1538   3646    818       C  
-ATOM  14288  N3   DA E  32     -38.010   1.859  39.873  1.00 99.24           N  
-ANISOU14288  N3   DA E  32    11711  12978  13016  -1633   3578    941       N  
-ATOM  14289  C4   DA E  32     -37.706   2.570  40.966  1.00103.46           C  
-ANISOU14289  C4   DA E  32    12314  13535  13460  -1514   3511   1013       C  
-ATOM  14290  P    DT E  33     -36.001  -2.850  43.861  1.00137.58           P  
-ANISOU14290  P    DT E  33    18159  16453  17662  -1868   3052   1452       P  
-ATOM  14291  OP1  DT E  33     -36.325  -4.256  44.188  1.00142.73           O  
-ANISOU14291  OP1  DT E  33    19095  16895  18240  -2089   3058   1535       O  
-ATOM  14292  OP2  DT E  33     -35.000  -2.117  44.666  1.00139.73           O  
-ANISOU14292  OP2  DT E  33    18488  16643  17961  -1615   2897   1489       O  
-ATOM  14293  O5'  DT E  33     -35.551  -2.776  42.332  1.00133.43           O  
-ANISOU14293  O5'  DT E  33    17394  15932  17371  -1761   3043   1307       O  
-ATOM  14294  C5'  DT E  33     -36.410  -3.309  41.335  1.00126.90           C  
-ANISOU14294  C5'  DT E  33    16452  15207  16557  -1961   3186   1243       C  
-ATOM  14295  C4'  DT E  33     -35.829  -3.077  39.954  1.00116.45           C  
-ANISOU14295  C4'  DT E  33    14893  13887  15464  -1809   3157   1106       C  
-ATOM  14296  O4'  DT E  33     -35.908  -1.666  39.625  1.00109.28           O  
-ANISOU14296  O4'  DT E  33    13677  13261  14582  -1657   3212   1027       O  
-ATOM  14297  C3'  DT E  33     -34.359  -3.456  39.810  1.00113.52           C  
-ANISOU14297  C3'  DT E  33    14645  13198  15290  -1589   2948   1097       C  
-ATOM  14298  O3'  DT E  33     -34.130  -3.944  38.498  1.00110.38           O  
-ANISOU14298  O3'  DT E  33    14134  12734  15073  -1581   2951    995       O  
-ATOM  14299  C2'  DT E  33     -33.665  -2.119  40.033  1.00108.27           C  
-ANISOU14299  C2'  DT E  33    13815  12638  14685  -1316   2874   1066       C  
-ATOM  14300  C1'  DT E  33     -34.619  -1.220  39.261  1.00103.00           C  
-ANISOU14300  C1'  DT E  33    12812  12335  13989  -1370   3055    971       C  
-ATOM  14301  N1   DT E  33     -34.478   0.229  39.576  1.00 96.02           N  
-ANISOU14301  N1   DT E  33    11727  11669  13086  -1185   3057    948       N  
-ATOM  14302  C2   DT E  33     -34.694   1.148  38.575  1.00 91.08           C  
-ANISOU14302  C2   DT E  33    10764  11293  12551  -1100   3146    829       C  
-ATOM  14303  O2   DT E  33     -35.002   0.833  37.437  1.00 90.93           O  
-ANISOU14303  O2   DT E  33    10600  11326  12624  -1170   3224    741       O  
-ATOM  14304  N3   DT E  33     -34.536   2.458  38.954  1.00 87.37           N  
-ANISOU14304  N3   DT E  33    10129  11009  12058   -929   3140    817       N  
-ATOM  14305  C4   DT E  33     -34.187   2.926  40.207  1.00 85.62           C  
-ANISOU14305  C4   DT E  33    10045  10749  11736   -835   3054    908       C  
-ATOM  14306  O4   DT E  33     -34.068   4.123  40.451  1.00 83.95           O  
-ANISOU14306  O4   DT E  33     9666  10718  11514   -680   3054    887       O  
-ATOM  14307  C5   DT E  33     -33.974   1.910  41.205  1.00 88.73           C  
-ANISOU14307  C5   DT E  33    10797  10879  12039   -928   2963   1030       C  
-ATOM  14308  C7   DT E  33     -33.595   2.300  42.603  1.00 86.07           C  
-ANISOU14308  C7   DT E  33    10638  10477  11586   -836   2864   1136       C  
-ATOM  14309  C6   DT E  33     -34.125   0.629  40.847  1.00 92.42           C  
-ANISOU14309  C6   DT E  33    11426  11162  12527  -1096   2970   1045       C  
-ATOM  14310  P    DC E  34     -32.766  -4.717  38.148  1.00111.46           P  
-ANISOU14310  P    DC E  34    14424  12510  15417  -1420   2755    984       P  
-ATOM  14311  OP1  DC E  34     -33.121  -6.034  37.579  1.00113.53           O  
-ANISOU14311  OP1  DC E  34    14810  12626  15701  -1623   2792    980       O  
-ATOM  14312  OP2  DC E  34     -31.873  -4.628  39.324  1.00110.10           O  
-ANISOU14312  OP2  DC E  34    14473  12141  15218  -1272   2593   1080       O  
-ATOM  14313  O5'  DC E  34     -32.120  -3.827  36.995  1.00108.36           O  
-ANISOU14313  O5'  DC E  34    13720  12215  15236  -1180   2728    849       O  
-ATOM  14314  C5'  DC E  34     -32.933  -3.128  36.065  1.00104.69           C  
-ANISOU14314  C5'  DC E  34    12938  12062  14779  -1225   2890    746       C  
-ATOM  14315  C4'  DC E  34     -32.026  -2.205  35.283  1.00 97.14           C  
-ANISOU14315  C4'  DC E  34    11736  11146  14026   -940   2816    643       C  
-ATOM  14316  O4'  DC E  34     -32.006  -0.896  35.912  1.00 94.23           O  
-ANISOU14316  O4'  DC E  34    11236  10977  13592   -801   2823    654       O  
-ATOM  14317  C3'  DC E  34     -30.581  -2.688  35.275  1.00 95.91           C  
-ANISOU14317  C3'  DC E  34    11742  10650  14051   -737   2606    655       C  
-ATOM  14318  O3'  DC E  34     -29.982  -2.418  34.019  1.00 91.57           O  
-ANISOU14318  O3'  DC E  34    10972  10099  13720   -569   2577    537       O  
-ATOM  14319  C2'  DC E  34     -29.943  -1.859  36.386  1.00 94.52           C  
-ANISOU14319  C2'  DC E  34    11628  10454  13831   -553   2497    722       C  
-ATOM  14320  C1'  DC E  34     -30.661  -0.538  36.155  1.00 90.68           C  
-ANISOU14320  C1'  DC E  34    10829  10340  13286   -525   2637    659       C  
-ATOM  14321  N1   DC E  34     -30.599   0.410  37.304  1.00 87.64           N  
-ANISOU14321  N1   DC E  34    10462  10057  12780   -429   2607    726       N  
-ATOM  14322  C2   DC E  34     -31.171   1.678  37.172  1.00 85.03           C  
-ANISOU14322  C2   DC E  34     9852  10058  12397   -384   2722    673       C  
-ATOM  14323  O2   DC E  34     -31.720   1.977  36.104  1.00 85.16           O  
-ANISOU14323  O2   DC E  34     9613  10276  12467   -425   2848    573       O  
-ATOM  14324  N3   DC E  34     -31.108   2.539  38.220  1.00 84.36           N  
-ANISOU14324  N3   DC E  34     9785  10065  12203   -295   2692    734       N  
-ATOM  14325  C4   DC E  34     -30.504   2.171  39.351  1.00 84.60           C  
-ANISOU14325  C4   DC E  34    10097   9869  12179   -250   2554    841       C  
-ATOM  14326  N4   DC E  34     -30.462   3.050  40.358  1.00 85.38           N  
-ANISOU14326  N4   DC E  34    10204  10067  12171   -159   2527    896       N  
-ATOM  14327  C5   DC E  34     -29.911   0.882  39.499  1.00 85.43           C  
-ANISOU14327  C5   DC E  34    10489   9634  12337   -294   2437    895       C  
-ATOM  14328  C6   DC E  34     -29.979   0.042  38.461  1.00 85.73           C  
-ANISOU14328  C6   DC E  34    10506   9585  12482   -384   2468    836       C  
-ATOM  14329  P    DG E  35     -28.683  -3.240  33.551  1.00 98.46           P  
-ANISOU14329  P    DG E  35    11986  10619  14806   -419   2395    523       P  
-ATOM  14330  OP1  DG E  35     -29.141  -4.439  32.817  1.00100.30           O  
-ANISOU14330  OP1  DG E  35    12295  10756  15058   -619   2453    499       O  
-ATOM  14331  OP2  DG E  35     -27.779  -3.371  34.717  1.00 98.35           O  
-ANISOU14331  OP2  DG E  35    12230  10367  14773   -301   2224    626       O  
-ATOM  14332  O5'  DG E  35     -27.972  -2.256  32.523  1.00 93.55           O  
-ANISOU14332  O5'  DG E  35    11057  10092  14395   -151   2362    403       O  
-ATOM  14333  C5'  DG E  35     -28.740  -1.494  31.611  1.00 87.27           C  
-ANISOU14333  C5'  DG E  35     9937   9611  13609   -176   2522    300       C  
-ATOM  14334  C4'  DG E  35     -28.001  -0.201  31.343  1.00 80.24           C  
-ANISOU14334  C4'  DG E  35     8805   8829  12852    112   2467    236       C  
-ATOM  14335  O4'  DG E  35     -28.206   0.682  32.470  1.00 78.08           O  
-ANISOU14335  O4'  DG E  35     8541   8693  12431    145   2474    302       O  
-ATOM  14336  C3'  DG E  35     -26.491  -0.372  31.209  1.00 77.98           C  
-ANISOU14336  C3'  DG E  35     8605   8248  12775    367   2262    233       C  
-ATOM  14337  O3'  DG E  35     -25.986   0.466  30.179  1.00 72.10           O  
-ANISOU14337  O3'  DG E  35     7567   7608  12219    585   2258    121       O  
-ATOM  14338  C2'  DG E  35     -25.947   0.019  32.577  1.00 78.66           C  
-ANISOU14338  C2'  DG E  35     8866   8240  12781    471   2144    335       C  
-ATOM  14339  C1'  DG E  35     -26.952   1.087  32.979  1.00 76.09           C  
-ANISOU14339  C1'  DG E  35     8359   8263  12288    403   2293    332       C  
-ATOM  14340  N9   DG E  35     -27.065   1.272  34.417  1.00 76.07           N  
-ANISOU14340  N9   DG E  35     8549   8245  12108    366   2254    446       N  
-ATOM  14341  C8   DG E  35     -26.798   0.354  35.406  1.00 77.51           C  
-ANISOU14341  C8   DG E  35     9072   8172  12206    285   2155    559       C  
-ATOM  14342  N7   DG E  35     -26.998   0.823  36.609  1.00 77.43           N  
-ANISOU14342  N7   DG E  35     9161   8223  12035    276   2145    644       N  
-ATOM  14343  C5   DG E  35     -27.422   2.132  36.397  1.00 75.20           C  
-ANISOU14343  C5   DG E  35     8584   8256  11732    355   2244    583       C  
-ATOM  14344  C6   DG E  35     -27.786   3.137  37.322  1.00 74.20           C  
-ANISOU14344  C6   DG E  35     8407   8327  11459    385   2280    627       C  
-ATOM  14345  O6   DG E  35     -27.806   3.068  38.560  1.00 74.40           O  
-ANISOU14345  O6   DG E  35     8645   8285  11337    349   2229    732       O  
-ATOM  14346  N1   DG E  35     -28.153   4.318  36.675  1.00 72.13           N  
-ANISOU14346  N1   DG E  35     7806   8369  11233    469   2386    533       N  
-ATOM  14347  C2   DG E  35     -28.168   4.502  35.315  1.00 70.76           C  
-ANISOU14347  C2   DG E  35     7376   8294  11214    518   2450    414       C  
-ATOM  14348  N2   DG E  35     -28.549   5.705  34.874  1.00 68.10           N  
-ANISOU14348  N2   DG E  35     6729   8259  10888    598   2551    337       N  
-ATOM  14349  N3   DG E  35     -27.828   3.572  34.441  1.00 71.35           N  
-ANISOU14349  N3   DG E  35     7497   8187  11427    493   2417    372       N  
-ATOM  14350  C4   DG E  35     -27.468   2.420  35.053  1.00 73.77           C  
-ANISOU14350  C4   DG E  35     8130   8197  11701    411   2313    461       C  
-ATOM  14351  P    DC E  36     -25.628  -0.158  28.741  1.00 73.32           P  
-ANISOU14351  P    DC E  36     7624   7658  12575    622   2250     23       P  
-ATOM  14352  OP1  DC E  36     -25.313   0.958  27.821  1.00 71.00           O  
-ANISOU14352  OP1  DC E  36     6995   7547  12436    838   2278    -87       O  
-ATOM  14353  OP2  DC E  36     -26.693  -1.131  28.392  1.00 72.69           O  
-ANISOU14353  OP2  DC E  36     7616   7616  12388    331   2380     21       O  
-ATOM  14354  O5'  DC E  36     -24.272  -0.967  29.008  1.00 73.99           O  
-ANISOU14354  O5'  DC E  36     7968   7344  12799    765   2033     76       O  
-ATOM  14355  C5'  DC E  36     -23.055  -0.259  29.218  1.00 71.01           C  
-ANISOU14355  C5'  DC E  36     7554   6861  12566   1058   1880     75       C  
-ATOM  14356  C4'  DC E  36     -21.863  -1.201  29.256  1.00 71.26           C  
-ANISOU14356  C4'  DC E  36     7825   6512  12740   1163   1691    114       C  
-ATOM  14357  O4'  DC E  36     -21.962  -2.057  30.421  1.00 75.07           O  
-ANISOU14357  O4'  DC E  36     8647   6809  13069   1010   1633    235       O  
-ATOM  14358  C3'  DC E  36     -21.727  -2.152  28.073  1.00 70.15           C  
-ANISOU14358  C3'  DC E  36     7680   6238  12736   1117   1694     49       C  
-ATOM  14359  O3'  DC E  36     -20.370  -2.533  27.903  1.00 69.56           O  
-ANISOU14359  O3'  DC E  36     7716   5860  12854   1323   1508     55       O  
-ATOM  14360  C2'  DC E  36     -22.548  -3.347  28.542  1.00 75.20           C  
-ANISOU14360  C2'  DC E  36     8574   6794  13203    816   1752    121       C  
-ATOM  14361  C1'  DC E  36     -22.154  -3.399  30.016  1.00 79.06           C  
-ANISOU14361  C1'  DC E  36     9327   7135  13579    833   1639    244       C  
-ATOM  14362  N1   DC E  36     -23.189  -3.996  30.902  1.00 84.68           N  
-ANISOU14362  N1   DC E  36    10237   7886  14052    552   1728    333       N  
-ATOM  14363  C2   DC E  36     -22.974  -5.253  31.476  1.00 88.52           C  
-ANISOU14363  C2   DC E  36    11057   8087  14489    429   1643    421       C  
-ATOM  14364  O2   DC E  36     -21.919  -5.855  31.231  1.00 89.41           O  
-ANISOU14364  O2   DC E  36    11295   7918  14757    556   1493    423       O  
-ATOM  14365  N3   DC E  36     -23.935  -5.769  32.284  1.00 90.98           N  
-ANISOU14365  N3   DC E  36    11542   8442  14583    175   1729    503       N  
-ATOM  14366  C4   DC E  36     -25.055  -5.081  32.518  1.00 90.14           C  
-ANISOU14366  C4   DC E  36    11290   8645  14315     47   1890    498       C  
-ATOM  14367  N4   DC E  36     -25.977  -5.625  33.317  1.00 91.82           N  
-ANISOU14367  N4   DC E  36    11681   8889  14317   -202   1972    582       N  
-ATOM  14368  C5   DC E  36     -25.286  -3.801  31.941  1.00 87.87           C  
-ANISOU14368  C5   DC E  36    10664   8650  14073    168   1977    407       C  
-ATOM  14369  C6   DC E  36     -24.335  -3.303  31.149  1.00 85.41           C  
-ANISOU14369  C6   DC E  36    10183   8293  13976    419   1892    327       C  
-ATOM  14370  P    DA E  37     -19.376  -1.617  27.036  1.00 61.39           P  
-ANISOU14370  P    DA E  37     8062   8180   7085   -566  -2255    499       P  
-ATOM  14371  OP1  DA E  37     -20.128  -1.123  25.859  1.00 60.64           O  
-ANISOU14371  OP1  DA E  37     7864   7831   7344   -600  -2437    447       O  
-ATOM  14372  OP2  DA E  37     -18.105  -2.363  26.862  1.00 59.54           O  
-ANISOU14372  OP2  DA E  37     8022   8087   6515   -499  -2280    723       O  
-ATOM  14373  O5'  DA E  37     -19.100  -0.355  27.986  1.00 59.65           O  
-ANISOU14373  O5'  DA E  37     7724   8097   6842   -578  -2237    301       O  
-ATOM  14374  C5'  DA E  37     -19.612   0.919  27.618  1.00 58.28           C  
-ANISOU14374  C5'  DA E  37     7380   7791   6972   -617  -2375    119       C  
-ATOM  14375  C4'  DA E  37     -18.958   2.014  28.436  1.00 59.57           C  
-ANISOU14375  C4'  DA E  37     7482   8121   7029   -612  -2380    -15       C  
-ATOM  14376  O4'  DA E  37     -19.512   2.011  29.772  1.00 63.23           O  
-ANISOU14376  O4'  DA E  37     7880   8694   7449   -643  -2149   -157       O  
-ATOM  14377  C3'  DA E  37     -17.451   1.848  28.577  1.00 58.86           C  
-ANISOU14377  C3'  DA E  37     7542   8237   6586   -549  -2426    135       C  
-ATOM  14378  O3'  DA E  37     -16.762   3.057  28.284  1.00 57.21           O  
-ANISOU14378  O3'  DA E  37     7277   8050   6411   -539  -2610     65       O  
-ATOM  14379  C2'  DA E  37     -17.207   1.454  30.032  1.00 63.00           C  
-ANISOU14379  C2'  DA E  37     8108   8993   6835   -543  -2188    108       C  
-ATOM  14380  C1'  DA E  37     -18.558   1.577  30.718  1.00 66.48           C  
-ANISOU14380  C1'  DA E  37     8409   9357   7492   -604  -2022    -80       C  
-ATOM  14381  N9   DA E  37     -18.976   0.296  31.264  1.00 70.83           N  
-ANISOU14381  N9   DA E  37     9044   9954   7915   -602  -1807      8       N  
-ATOM  14382  C8   DA E  37     -18.395  -0.917  31.029  1.00 72.25           C  
-ANISOU14382  C8   DA E  37     9399  10195   7857   -556  -1768    232       C  
-ATOM  14383  N7   DA E  37     -18.975  -1.913  31.654  1.00 74.34           N  
-ANISOU14383  N7   DA E  37     9704  10489   8052   -566  -1555    263       N  
-ATOM  14384  C5   DA E  37     -20.007  -1.306  32.350  1.00 76.27           C  
-ANISOU14384  C5   DA E  37     9788  10689   8502   -622  -1448     43       C  
-ATOM  14385  C6   DA E  37     -20.997  -1.816  33.208  1.00 78.19           C  
-ANISOU14385  C6   DA E  37     9983  10932   8792   -658  -1220    -42       C  
-ATOM  14386  N6   DA E  37     -21.102  -3.110  33.513  1.00 79.63           N  
-ANISOU14386  N6   DA E  37    10282  11165   8810   -641  -1053     93       N  
-ATOM  14387  N1   DA E  37     -21.878  -0.942  33.736  1.00 79.93           N  
-ANISOU14387  N1   DA E  37    10032  11098   9239   -711  -1167   -269       N  
-ATOM  14388  C2   DA E  37     -21.769   0.358  33.418  1.00 79.57           C  
-ANISOU14388  C2   DA E  37     9871  11000   9361   -727  -1333   -402       C  
-ATOM  14389  N3   DA E  37     -20.880   0.958  32.623  1.00 77.48           N  
-ANISOU14389  N3   DA E  37     9635  10728   9074   -698  -1554   -343       N  
-ATOM  14390  C4   DA E  37     -20.022   0.057  32.119  1.00 75.18           C  
-ANISOU14390  C4   DA E  37     9516  10494   8556   -645  -1601   -116       C  
-ATOM  14391  P    DG E  38     -15.199   3.195  28.633  1.00 56.93           P  
-ANISOU14391  P    DG E  38     7360   8250   6021   -481  -2654    168       P  
-ATOM  14392  OP1  DG E  38     -14.669   4.372  27.909  1.00 55.48           O  
-ANISOU14392  OP1  DG E  38     7115   8011   5955   -474  -2890    117       O  
-ATOM  14393  OP2  DG E  38     -14.572   1.868  28.444  1.00 56.62           O  
-ANISOU14393  OP2  DG E  38     7510   8287   5715   -430  -2603    410       O  
-ATOM  14394  O5'  DG E  38     -15.192   3.545  30.193  1.00 58.69           O  
-ANISOU14394  O5'  DG E  38     7529   8677   6093   -501  -2452     15       O  
-ATOM  14395  C5'  DG E  38     -14.083   3.179  30.992  1.00 58.37           C  
-ANISOU14395  C5'  DG E  38     7611   8891   5677   -458  -2364    111       C  
-ATOM  14396  C4'  DG E  38     -13.980   4.112  32.181  1.00 58.87           C  
-ANISOU14396  C4'  DG E  38     7577   9109   5681   -484  -2273    -83       C  
-ATOM  14397  O4'  DG E  38     -15.291   4.216  32.787  1.00 59.98           O  
-ANISOU14397  O4'  DG E  38     7588   9165   6035   -542  -2117   -261       O  
-ATOM  14398  C3'  DG E  38     -13.080   3.629  33.303  1.00 60.23           C  
-ANISOU14398  C3'  DG E  38     7859   9559   5466   -451  -2117    -13       C  
-ATOM  14399  O3'  DG E  38     -12.794   4.711  34.153  1.00 64.81           O  
-ANISOU14399  O3'  DG E  38     8349  10270   6007   -472  -2099   -187       O  
-ATOM  14400  C2'  DG E  38     -14.027   2.659  33.986  1.00 58.63           C  
-ANISOU14400  C2'  DG E  38     7662   9349   5264   -473  -1880    -22       C  
-ATOM  14401  C1'  DG E  38     -15.249   3.565  34.042  1.00 59.30           C  
-ANISOU14401  C1'  DG E  38     7555   9268   5707   -539  -1879   -259       C  
-ATOM  14402  N9   DG E  38     -16.512   2.872  34.275  1.00 57.01           N  
-ANISOU14402  N9   DG E  38     7222   8865   5575   -575  -1714   -303       N  
-ATOM  14403  C8   DG E  38     -16.847   1.589  33.925  1.00 56.51           C  
-ANISOU14403  C8   DG E  38     7258   8737   5475   -559  -1638   -143       C  
-ATOM  14404  N7   DG E  38     -18.059   1.260  34.277  1.00 57.00           N  
-ANISOU14404  N7   DG E  38     7243   8701   5713   -603  -1489   -237       N  
-ATOM  14405  C5   DG E  38     -18.561   2.398  34.899  1.00 56.93           C  
-ANISOU14405  C5   DG E  38     7073   8689   5867   -648  -1463   -473       C  
-ATOM  14406  C6   DG E  38     -19.827   2.650  35.482  1.00 58.04           C  
-ANISOU14406  C6   DG E  38     7074   8744   6235   -705  -1324   -661       C  
-ATOM  14407  O6   DG E  38     -20.800   1.889  35.578  1.00 59.39           O  
-ANISOU14407  O6   DG E  38     7231   8820   6513   -729  -1190   -657       O  
-ATOM  14408  N1   DG E  38     -19.910   3.941  35.997  1.00 57.45           N  
-ANISOU14408  N1   DG E  38     6863   8699   6265   -737  -1349   -870       N  
-ATOM  14409  C2   DG E  38     -18.901   4.874  35.955  1.00 56.87           C  
-ANISOU14409  C2   DG E  38     6789   8728   6092   -718  -1490   -897       C  
-ATOM  14410  N2   DG E  38     -19.167   6.070  36.504  1.00 57.81           N  
-ANISOU14410  N2   DG E  38     6768   8859   6340   -756  -1488  -1114       N  
-ATOM  14411  N3   DG E  38     -17.715   4.651  35.409  1.00 55.85           N  
-ANISOU14411  N3   DG E  38     6789   8681   5752   -665  -1623   -723       N  
-ATOM  14412  C4   DG E  38     -17.618   3.398  34.902  1.00 56.86           C  
-ANISOU14412  C4   DG E  38     7051   8780   5775   -632  -1601   -516       C  
-ATOM  14413  P    DC E  39     -11.287   5.238  34.307  1.00 65.90           P  
-ANISOU14413  P    DC E  39     8560  10610   5869   -430  -2208   -125       P  
-ATOM  14414  OP1  DC E  39     -10.901   5.890  33.037  1.00 67.07           O  
-ANISOU14414  OP1  DC E  39     8692  10617   6174   -416  -2471    -85       O  
-ATOM  14415  OP2  DC E  39     -10.473   4.137  34.859  1.00 65.04           O  
-ANISOU14415  OP2  DC E  39     8617  10706   5388   -381  -2081     61       O  
-ATOM  14416  O5'  DC E  39     -11.395   6.352  35.435  1.00 69.03           O  
-ANISOU14416  O5'  DC E  39     8829  11124   6276   -473  -2128   -362       O  
-ATOM  14417  C5'  DC E  39     -11.550   5.910  36.767  1.00 73.34           C  
-ANISOU14417  C5'  DC E  39     9391  11844   6632   -484  -1887   -412       C  
-ATOM  14418  C4'  DC E  39     -12.487   6.810  37.542  1.00 76.24           C  
-ANISOU14418  C4'  DC E  39     9588  12175   7203   -548  -1791   -675       C  
-ATOM  14419  O4'  DC E  39     -13.807   6.731  36.949  1.00 76.03           O  
-ANISOU14419  O4'  DC E  39     9466  11898   7525   -585  -1793   -745       O  
-ATOM  14420  C3'  DC E  39     -12.682   6.398  38.992  1.00 79.56           C  
-ANISOU14420  C3'  DC E  39    10019  12781   7430   -562  -1532   -740       C  
-ATOM  14421  O3'  DC E  39     -11.615   6.888  39.822  1.00 83.28           O  
-ANISOU14421  O3'  DC E  39    10525  13496   7623   -548  -1515   -765       O  
-ATOM  14422  C2'  DC E  39     -14.053   7.003  39.267  1.00 79.73           C  
-ANISOU14422  C2'  DC E  39     9869  12646   7779   -627  -1458   -968       C  
-ATOM  14423  C1'  DC E  39     -14.770   6.619  37.978  1.00 78.01           C  
-ANISOU14423  C1'  DC E  39     9637  12167   7835   -628  -1574   -892       C  
-ATOM  14424  N1   DC E  39     -15.329   5.228  37.983  1.00 77.00           N  
-ANISOU14424  N1   DC E  39     9594  12001   7663   -616  -1426   -760       N  
-ATOM  14425  C2   DC E  39     -16.580   5.000  38.565  1.00 77.53           C  
-ANISOU14425  C2   DC E  39     9572  11990   7897   -661  -1246   -886       C  
-ATOM  14426  O2   DC E  39     -17.183   5.960  39.062  1.00 77.87           O  
-ANISOU14426  O2   DC E  39     9470  12000   8118   -708  -1214  -1102       O  
-ATOM  14427  N3   DC E  39     -17.092   3.741  38.568  1.00 76.67           N  
-ANISOU14427  N3   DC E  39     9538  11844   7750   -651  -1111   -767       N  
-ATOM  14428  C4   DC E  39     -16.404   2.737  38.025  1.00 75.56           C  
-ANISOU14428  C4   DC E  39     9556  11740   7414   -599  -1149   -534       C  
-ATOM  14429  N4   DC E  39     -16.951   1.518  38.053  1.00 74.89           N  
-ANISOU14429  N4   DC E  39     9540  11613   7300   -593  -1009   -427       N  
-ATOM  14430  C5   DC E  39     -15.125   2.948  37.429  1.00 75.06           C  
-ANISOU14430  C5   DC E  39     9586  11756   7178   -551  -1330   -401       C  
-ATOM  14431  C6   DC E  39     -14.633   4.193  37.428  1.00 76.40           C  
-ANISOU14431  C6   DC E  39     9678  11962   7388   -562  -1464   -520       C  
-ATOM  14432  P    DT E  40     -11.588   8.424  40.298  1.00 74.87           P  
-ANISOU14432  P    DT E  40     9316  12462   6670   -593  -1571  -1003       P  
-ATOM  14433  OP1  DT E  40     -11.941   9.272  39.131  1.00 74.49           O  
-ANISOU14433  OP1  DT E  40     9171  12184   6949   -610  -1788  -1067       O  
-ATOM  14434  OP2  DT E  40     -10.309   8.659  41.002  1.00 74.29           O  
-ANISOU14434  OP2  DT E  40     9318  12651   6258   -567  -1566   -965       O  
-ATOM  14435  O5'  DT E  40     -12.757   8.499  41.387  1.00 80.18           O  
-ANISOU14435  O5'  DT E  40     9880  13128   7458   -647  -1344  -1200       O  
-ATOM  14436  C5'  DT E  40     -13.760   9.513  41.295  1.00 82.96           C  
-ANISOU14436  C5'  DT E  40    10059  13308   8155   -704  -1375  -1422       C  
-ATOM  14437  C4'  DT E  40     -14.887   9.229  42.269  1.00 84.63           C  
-ANISOU14437  C4'  DT E  40    10198  13511   8447   -746  -1137  -1556       C  
-ATOM  14438  O4'  DT E  40     -15.560   7.998  41.896  1.00 81.61           O  
-ANISOU14438  O4'  DT E  40     9873  13020   8114   -732  -1054  -1425       O  
-ATOM  14439  C3'  DT E  40     -14.407   9.042  43.701  1.00 88.94           C  
-ANISOU14439  C3'  DT E  40    10793  14322   8680   -744   -940  -1590       C  
-ATOM  14440  O3'  DT E  40     -15.271   9.727  44.599  1.00 99.93           O  
-ANISOU14440  O3'  DT E  40    12048  15702  10217   -800   -805  -1825       O  
-ATOM  14441  C2'  DT E  40     -14.441   7.526  43.885  1.00 85.13           C  
-ANISOU14441  C2'  DT E  40    10442  13900   8004   -707   -791  -1401       C  
-ATOM  14442  C1'  DT E  40     -15.623   7.135  43.012  1.00 81.89           C  
-ANISOU14442  C1'  DT E  40     9975  13222   7917   -725   -815  -1395       C  
-ATOM  14443  N1   DT E  40     -15.561   5.720  42.545  1.00 74.93           N  
-ANISOU14443  N1   DT E  40     9231  12320   6919   -682   -774  -1167       N  
-ATOM  14444  C2   DT E  40     -16.674   4.911  42.656  1.00 74.53           C  
-ANISOU14444  C2   DT E  40     9162  12157   7000   -701   -623  -1169       C  
-ATOM  14445  O2   DT E  40     -17.737   5.280  43.119  1.00 77.32           O  
-ANISOU14445  O2   DT E  40     9390  12423   7565   -750   -518  -1347       O  
-ATOM  14446  N3   DT E  40     -16.501   3.632  42.197  1.00 72.76           N  
-ANISOU14446  N3   DT E  40     9073  11922   6649   -659   -596   -950       N  
-ATOM  14447  C4   DT E  40     -15.353   3.093  41.652  1.00 71.32           C  
-ANISOU14447  C4   DT E  40     9040  11829   6228   -601   -702   -734       C  
-ATOM  14448  O4   DT E  40     -15.299   1.929  41.271  1.00 67.29           O  
-ANISOU14448  O4   DT E  40     8647  11299   5621   -567   -662   -547       O  
-ATOM  14449  C5   DT E  40     -14.227   3.988  41.564  1.00 69.93           C  
-ANISOU14449  C5   DT E  40     8875  11770   5926   -583   -858   -742       C  
-ATOM  14450  C7   DT E  40     -12.930   3.506  40.990  1.00 69.23           C  
-ANISOU14450  C7   DT E  40     8941  11784   5578   -520   -981   -515       C  
-ATOM  14451  C6   DT E  40     -14.380   5.241  42.014  1.00 72.13           C  
-ANISOU14451  C6   DT E  40     9022  12061   6325   -625   -886   -956       C  
-ATOM  14452  P    DT E  41     -14.784  10.054  46.094  1.00 94.06           P  
-ANISOU14452  P    DT E  41    12156  14085   9498   4691    -31   3089       P  
-ATOM  14453  OP1  DT E  41     -15.029  11.493  46.349  1.00 92.93           O  
-ANISOU14453  OP1  DT E  41    12006  14042   9263   4290    233   2975       O  
-ATOM  14454  OP2  DT E  41     -13.427   9.488  46.265  1.00 94.15           O  
-ANISOU14454  OP2  DT E  41    12260  14704   8807   5036   -541   2955       O  
-ATOM  14455  O5'  DT E  41     -15.774   9.192  47.003  1.00107.32           O  
-ANISOU14455  O5'  DT E  41    14299  15021  11457   4886    502   3491       O  
-ATOM  14456  C5'  DT E  41     -16.114   7.891  46.572  1.00123.19           C  
-ANISOU14456  C5'  DT E  41    16242  16654  13909   5156    425   3662       C  
-ATOM  14457  C4'  DT E  41     -17.410   7.454  47.208  1.00135.59           C  
-ANISOU14457  C4'  DT E  41    18132  17415  15971   5167   1038   4025       C  
-ATOM  14458  O4'  DT E  41     -17.812   6.192  46.630  1.00142.99           O  
-ANISOU14458  O4'  DT E  41    18940  17958  17433   5404    951   4180       O  
-ATOM  14459  C3'  DT E  41     -17.296   7.188  48.694  1.00144.83           C  
-ANISOU14459  C3'  DT E  41    19938  18488  16604   5396   1346   4244       C  
-ATOM  14460  O3'  DT E  41     -18.576   7.266  49.276  1.00147.35           O  
-ANISOU14460  O3'  DT E  41    20510  18102  17374   5264   1980   4530       O  
-ATOM  14461  C2'  DT E  41     -16.755   5.765  48.711  1.00153.16           C  
-ANISOU14461  C2'  DT E  41    21110  19574  17511   5855   1040   4345       C  
-ATOM  14462  C1'  DT E  41     -17.419   5.138  47.487  1.00156.66           C  
-ANISOU14462  C1'  DT E  41    21107  19644  18774   5823    938   4372       C  
-ATOM  14463  N1   DT E  41     -16.502   4.238  46.740  1.00166.57           N  
-ANISOU14463  N1   DT E  41    22113  21279  19897   6118    337   4231       N  
-ATOM  14464  C2   DT E  41     -16.941   2.985  46.382  1.00172.81           C  
-ANISOU14464  C2   DT E  41    22864  21636  21160   6368    319   4420       C  
-ATOM  14465  O2   DT E  41     -18.057   2.568  46.638  1.00175.37           O  
-ANISOU14465  O2   DT E  41    23344  21273  22014   6357    773   4700       O  
-ATOM  14466  N3   DT E  41     -16.017   2.235  45.702  1.00175.32           N  
-ANISOU14466  N3   DT E  41    22948  22360  21305   6631   -258   4267       N  
-ATOM  14467  C4   DT E  41     -14.730   2.602  45.356  1.00177.59           C  
-ANISOU14467  C4   DT E  41    23042  23427  21009   6669   -803   3952       C  
-ATOM  14468  O4   DT E  41     -13.976   1.853  44.743  1.00175.54           O  
-ANISOU14468  O4   DT E  41    22578  23481  20640   6918  -1299   3835       O  
-ATOM  14469  C5   DT E  41     -14.337   3.925  45.765  1.00176.04           C  
-ANISOU14469  C5   DT E  41    22900  23646  20341   6397   -747   3770       C  
-ATOM  14470  C7   DT E  41     -12.964   4.435  45.447  1.00181.54           C  
-ANISOU14470  C7   DT E  41    23399  25191  20388   6407  -1305   3425       C  
-ATOM  14471  C6   DT E  41     -15.228   4.669  46.430  1.00172.50           C  
-ANISOU14471  C6   DT E  41    22680  22807  20055   6138   -188   3916       C  
-ATOM  14472  P    DC E  42     -18.776   6.917  50.828  1.00130.35           P  
-ANISOU14472  P    DC E  42    19030  15671  14827   5482   2417   4825       P  
-ATOM  14473  OP1  DC E  42     -19.925   7.704  51.327  1.00132.22           O  
-ANISOU14473  OP1  DC E  42    19424  15408  15407   5167   3032   4981       O  
-ATOM  14474  OP2  DC E  42     -17.456   7.020  51.490  1.00133.60           O  
-ANISOU14474  OP2  DC E  42    19687  16751  14324   5691   2091   4677       O  
-ATOM  14475  O5'  DC E  42     -19.195   5.378  50.810  1.00134.42           O  
-ANISOU14475  O5'  DC E  42    19671  15690  15713   5842   2458   5103       O  
-ATOM  14476  C5'  DC E  42     -20.235   4.962  49.940  1.00128.78           C  
-ANISOU14476  C5'  DC E  42    18645  14413  15872   5733   2603   5214       C  
-ATOM  14477  C4'  DC E  42     -20.554   3.492  50.147  1.00128.16           C  
-ANISOU14477  C4'  DC E  42    18777  13884  16034   6107   2668   5496       C  
-ATOM  14478  O4'  DC E  42     -19.565   2.655  49.490  1.00122.14           O  
-ANISOU14478  O4'  DC E  42    17799  13537  15070   6402   2067   5348       O  
-ATOM  14479  C3'  DC E  42     -20.577   3.039  51.599  1.00135.55           C  
-ANISOU14479  C3'  DC E  42    20352  14622  16529   6366   3009   5767       C  
-ATOM  14480  O3'  DC E  42     -21.504   1.980  51.712  1.00146.94           O  
-ANISOU14480  O3'  DC E  42    21940  15372  18518   6538   3312   6086       O  
-ATOM  14481  C2'  DC E  42     -19.145   2.551  51.797  1.00131.16           C  
-ANISOU14481  C2'  DC E  42    19902  14718  15216   6709   2481   5619       C  
-ATOM  14482  C1'  DC E  42     -18.879   1.877  50.454  1.00122.62           C  
-ANISOU14482  C1'  DC E  42    18316  13748  14526   6797   1993   5474       C  
-ATOM  14483  N1   DC E  42     -17.437   1.814  50.055  1.00107.50           N  
-ANISOU14483  N1   DC E  42    16223  12614  12008   6969   1341   5180       N  
-ATOM  14484  C2   DC E  42     -16.933   0.654  49.461  1.00102.13           C  
-ANISOU14484  C2   DC E  42    15387  12030  11388   7295    915   5166       C  
-ATOM  14485  O2   DC E  42     -17.692  -0.304  49.282  1.00100.95           O  
-ANISOU14485  O2   DC E  42    15254  11313  11790   7436   1085   5398       O  
-ATOM  14486  N3   DC E  42     -15.627   0.612  49.100  1.00 97.14           N  
-ANISOU14486  N3   DC E  42    14590  12111  10207   7447    326   4897       N  
-ATOM  14487  C4   DC E  42     -14.839   1.668  49.311  1.00 95.46           C  
-ANISOU14487  C4   DC E  42    14365  12496   9410   7285    160   4650       C  
-ATOM  14488  N4   DC E  42     -13.558   1.581  48.935  1.00 90.79           N  
-ANISOU14488  N4   DC E  42    13605  12599   8292   7444   -426   4388       N  
-ATOM  14489  C5   DC E  42     -15.333   2.861  49.916  1.00 97.94           C  
-ANISOU14489  C5   DC E  42    14836  12721   9654   6951    588   4659       C  
-ATOM  14490  C6   DC E  42     -16.623   2.888  50.266  1.00104.17           C  
-ANISOU14490  C6   DC E  42    15787  12805  10987   6806   1167   4926       C  
-ATOM  14491  P    DA E  43     -22.277   1.725  53.094  1.00151.66           P  
-ANISOU14491  P    DA E  43    23139  15420  19064   6637   3936   6451       P  
-ATOM  14492  OP1  DA E  43     -23.593   2.391  53.008  1.00154.26           O  
-ANISOU14492  OP1  DA E  43    23391  15188  20034   6274   4461   6569       O  
-ATOM  14493  OP2  DA E  43     -21.354   2.063  54.200  1.00154.48           O  
-ANISOU14493  OP2  DA E  43    23915  16251  18529   6780   3889   6406       O  
-ATOM  14494  O5'  DA E  43     -22.503   0.143  53.104  1.00157.72           O  
-ANISOU14494  O5'  DA E  43    24045  15772  20109   7032   3910   6710       O  
-ATOM  14495  C5'  DA E  43     -22.897  -0.528  51.910  1.00152.39           C  
-ANISOU14495  C5'  DA E  43    22936  14846  20120   7043   3709   6694       C  
-ATOM  14496  C4'  DA E  43     -22.270  -1.912  51.824  1.00148.10           C  
-ANISOU14496  C4'  DA E  43    22466  14377  19428   7491   3348   6765       C  
-ATOM  14497  O4'  DA E  43     -20.882  -1.813  51.405  1.00142.49           O  
-ANISOU14497  O4'  DA E  43    21561  14448  18132   7614   2722   6455       O  
-ATOM  14498  C3'  DA E  43     -22.255  -2.698  53.127  1.00152.90           C  
-ANISOU14498  C3'  DA E  43    23681  14752  19661   7831   3617   7065       C  
-ATOM  14499  O3'  DA E  43     -22.404  -4.080  52.851  1.00158.98           O  
-ANISOU14499  O3'  DA E  43    24455  15199  20753   8154   3503   7240       O  
-ATOM  14500  C2'  DA E  43     -20.861  -2.406  53.668  1.00149.52           C  
-ANISOU14500  C2'  DA E  43    23440  15080  18292   7997   3246   6867       C  
-ATOM  14501  C1'  DA E  43     -20.043  -2.398  52.383  1.00143.62           C  
-ANISOU14501  C1'  DA E  43    22150  14855  17564   7982   2609   6536       C  
-ATOM  14502  N9   DA E  43     -18.816  -1.610  52.479  1.00133.37           N  
-ANISOU14502  N9   DA E  43    20811  14349  15514   7946   2225   6232       N  
-ATOM  14503  C8   DA E  43     -18.635  -0.458  53.192  1.00133.84           C  
-ANISOU14503  C8   DA E  43    21066  14671  15115   7729   2421   6146       C  
-ATOM  14504  N7   DA E  43     -17.426   0.043  53.098  1.00131.38           N  
-ANISOU14504  N7   DA E  43    20658  15101  14159   7749   1974   5855       N  
-ATOM  14505  C5   DA E  43     -16.765  -0.842  52.264  1.00125.98           C  
-ANISOU14505  C5   DA E  43    19696  14660  13511   7997   1447   5743       C  
-ATOM  14506  C6   DA E  43     -15.446  -0.875  51.772  1.00121.65           C  
-ANISOU14506  C6   DA E  43    18928  14842  12451   8137    820   5449       C  
-ATOM  14507  N6   DA E  43     -14.528   0.051  52.068  1.00116.74           N  
-ANISOU14507  N6   DA E  43    18337  14861  11159   8038    615   5206       N  
-ATOM  14508  N1   DA E  43     -15.107  -1.898  50.960  1.00118.64           N  
-ANISOU14508  N1   DA E  43    18293  14508  12277   8383    410   5413       N  
-ATOM  14509  C2   DA E  43     -16.031  -2.822  50.668  1.00119.99           C  
-ANISOU14509  C2   DA E  43    18433  14034  13123   8480    618   5655       C  
-ATOM  14510  N3   DA E  43     -17.300  -2.898  51.069  1.00124.92           N  
-ANISOU14510  N3   DA E  43    19247  13940  14277   8366   1196   5942       N  
-ATOM  14511  C4   DA E  43     -17.607  -1.867  51.873  1.00128.32           C  
-ANISOU14511  C4   DA E  43    19928  14345  14484   8122   1592   5971       C  
-ATOM  14512  P    DG E  44     -23.325  -4.998  53.794  1.00166.05           P  
-ANISOU14512  P    DG E  44    25827  15365  21899   8364   4029   7666       P  
-ATOM  14513  OP1  DG E  44     -24.672  -5.066  53.184  1.00166.24           O  
-ANISOU14513  OP1  DG E  44    25613  14708  22842   8135   4381   7811       O  
-ATOM  14514  OP2  DG E  44     -23.163  -4.526  55.188  1.00171.27           O  
-ANISOU14514  OP2  DG E  44    27025  16108  21940   8398   4358   7783       O  
-ATOM  14515  O5'  DG E  44     -22.634  -6.437  53.707  1.00170.05           O  
-ANISOU14515  O5'  DG E  44    26415  15963  22235   8838   3639   7735       O  
-ATOM  14516  C5'  DG E  44     -22.215  -6.949  52.453  1.00167.95           C  
-ANISOU14516  C5'  DG E  44    25667  15905  22242   8912   3121   7543       C  
-ATOM  14517  C4'  DG E  44     -20.840  -7.567  52.595  1.00168.57           C  
-ANISOU14517  C4'  DG E  44    25847  16581  21622   9285   2587   7416       C  
-ATOM  14518  O4'  DG E  44     -19.838  -6.525  52.689  1.00165.43           O  
-ANISOU14518  O4'  DG E  44    25389  16911  20555   9154   2306   7115       O  
-ATOM  14519  C3'  DG E  44     -20.681  -8.428  53.843  1.00174.67           C  
-ANISOU14519  C3'  DG E  44    27211  17181  21973   9661   2784   7699       C  
-ATOM  14520  O3'  DG E  44     -20.317  -9.744  53.463  1.00180.24           O  
-ANISOU14520  O3'  DG E  44    27869  17847  22767  10030   2451   7761       O  
-ATOM  14521  C2'  DG E  44     -19.583  -7.737  54.651  1.00174.33           C  
-ANISOU14521  C2'  DG E  44    27436  17802  21001   9710   2623   7538       C  
-ATOM  14522  C1'  DG E  44     -18.837  -6.956  53.582  1.00167.19           C  
-ANISOU14522  C1'  DG E  44    26012  17520  19994   9499   2121   7138       C  
-ATOM  14523  N9   DG E  44     -18.143  -5.789  54.109  1.00164.75           N  
-ANISOU14523  N9   DG E  44    25813  17769  19014   9332   2077   6936       N  
-ATOM  14524  C8   DG E  44     -18.633  -4.860  54.993  1.00165.01           C  
-ANISOU14524  C8   DG E  44    26139  17662  18897   9100   2557   7023       C  
-ATOM  14525  N7   DG E  44     -17.776  -3.922  55.285  1.00163.74           N  
-ANISOU14525  N7   DG E  44    26008  18115  18089   8995   2373   6787       N  
-ATOM  14526  C5   DG E  44     -16.647  -4.252  54.547  1.00162.35           C  
-ANISOU14526  C5   DG E  44    25542  18527  17618   9167   1731   6528       C  
-ATOM  14527  C6   DG E  44     -15.394  -3.603  54.456  1.00160.39           C  
-ANISOU14527  C6   DG E  44    25184  19076  16681   9155   1278   6206       C  
-ATOM  14528  O6   DG E  44     -15.024  -2.571  55.033  1.00160.60           O  
-ANISOU14528  O6   DG E  44    25355  19456  16210   8983   1359   6082       O  
-ATOM  14529  N1   DG E  44     -14.526  -4.272  53.594  1.00158.07           N  
-ANISOU14529  N1   DG E  44    24580  19177  16304   9372    679   6022       N  
-ATOM  14530  C2   DG E  44     -14.833  -5.423  52.905  1.00158.55           C  
-ANISOU14530  C2   DG E  44    24458  18902  16882   9575    535   6132       C  
-ATOM  14531  N2   DG E  44     -13.869  -5.925  52.119  1.00157.93           N  
-ANISOU14531  N2   DG E  44    24083  19298  16625   9769    -69   5917       N  
-ATOM  14532  N3   DG E  44     -16.004  -6.040  52.982  1.00160.34           N  
-ANISOU14532  N3   DG E  44    24785  18380  17758   9588    955   6432       N  
-ATOM  14533  C4   DG E  44     -16.857  -5.400  53.818  1.00162.44           C  
-ANISOU14533  C4   DG E  44    25352  18256  18111   9377   1541   6616       C  
-ATOM  14534  P    DA E  45     -19.584 -10.714  54.511  1.00165.29           P  
-ANISOU14534  P    DA E  45    26492  16078  20234  10500   2369   7933       P  
-ATOM  14535  OP1  DA E  45     -19.920 -12.109  54.152  1.00165.45           O  
-ANISOU14535  OP1  DA E  45    26487  15665  20713  10793   2302   8129       O  
-ATOM  14536  OP2  DA E  45     -19.883 -10.225  55.876  1.00167.60           O  
-ANISOU14536  OP2  DA E  45    27312  16216  20152  10461   2871   8128       O  
-ATOM  14537  O5'  DA E  45     -18.030 -10.474  54.217  1.00168.27           O  
-ANISOU14537  O5'  DA E  45    26712  17351  19873  10629   1717   7585       O  
-ATOM  14538  C5'  DA E  45     -17.490 -10.834  52.949  1.00170.71           C  
-ANISOU14538  C5'  DA E  45    26518  17964  20379  10678   1157   7346       C  
-ATOM  14539  C4'  DA E  45     -15.988 -11.024  53.044  1.00171.00           C  
-ANISOU14539  C4'  DA E  45    26596  18760  19616  10954    593   7126       C  
-ATOM  14540  O4'  DA E  45     -15.363  -9.744  53.318  1.00165.32           O  
-ANISOU14540  O4'  DA E  45    25872  18607  18334  10722    520   6883       O  
-ATOM  14541  C3'  DA E  45     -15.530 -11.970  54.149  1.00178.45           C  
-ANISOU14541  C3'  DA E  45    28080  19681  20040  11388    631   7348       C  
-ATOM  14542  O3'  DA E  45     -14.397 -12.718  53.720  1.00184.15           O  
-ANISOU14542  O3'  DA E  45    28678  20892  20398  11712     31   7188       O  
-ATOM  14543  C2'  DA E  45     -15.189 -11.020  55.292  1.00174.76           C  
-ANISOU14543  C2'  DA E  45    28003  19507  18892  11292    866   7333       C  
-ATOM  14544  C1'  DA E  45     -14.665  -9.800  54.545  1.00165.06           C  
-ANISOU14544  C1'  DA E  45    26348  18852  17516  10959    564   6956       C  
-ATOM  14545  N9   DA E  45     -14.914  -8.554  55.258  1.00158.02           N  
-ANISOU14545  N9   DA E  45    25646  18022  16372  10655    934   6934       N  
-ATOM  14546  C8   DA E  45     -16.093  -8.161  55.827  1.00155.05           C  
-ANISOU14546  C8   DA E  45    25485  17055  16373  10438   1559   7171       C  
-ATOM  14547  N7   DA E  45     -16.034  -6.986  56.407  1.00153.36           N  
-ANISOU14547  N7   DA E  45    25408  17062  15799  10185   1771   7082       N  
-ATOM  14548  C5   DA E  45     -14.724  -6.585  56.201  1.00152.27           C  
-ANISOU14548  C5   DA E  45    25133  17715  15006  10240   1247   6765       C  
-ATOM  14549  C6   DA E  45     -14.020  -5.424  56.572  1.00150.39           C  
-ANISOU14549  C6   DA E  45    24937  18052  14151  10059   1158   6533       C  
-ATOM  14550  N6   DA E  45     -14.576  -4.420  57.257  1.00149.38           N  
-ANISOU14550  N6   DA E  45    25011  17775  13971   9778   1617   6589       N  
-ATOM  14551  N1   DA E  45     -12.724  -5.335  56.210  1.00149.32           N  
-ANISOU14551  N1   DA E  45    24626  18650  13457  10180    578   6239       N  
-ATOM  14552  C2   DA E  45     -12.172  -6.342  55.526  1.00150.34           C  
-ANISOU14552  C2   DA E  45    24554  18928  13640  10464    119   6182       C  
-ATOM  14553  N3   DA E  45     -12.731  -7.480  55.121  1.00151.27           N  
-ANISOU14553  N3   DA E  45    24613  18555  14309  10656    145   6380       N  
-ATOM  14554  C4   DA E  45     -14.018  -7.539  55.494  1.00153.53           C  
-ANISOU14554  C4   DA E  45    25075  18114  15145  10528    727   6670       C  
-ATOM  14555  P    DT E  46     -13.401 -13.369  54.800  1.00188.28           P  
-ANISOU14555  P    DT E  46    33110  22756  15672   8035  -6888   -228       P  
-ATOM  14556  OP1  DT E  46     -12.612 -14.418  54.119  1.00188.03           O  
-ANISOU14556  OP1  DT E  46    32953  22588  15900   7987  -6977   -227       O  
-ATOM  14557  OP2  DT E  46     -14.188 -13.706  56.007  1.00189.56           O  
-ANISOU14557  OP2  DT E  46    33062  23016  15948   8007  -6777    -11       O  
-ATOM  14558  O5'  DT E  46     -12.419 -12.168  55.174  1.00187.12           O  
-ANISOU14558  O5'  DT E  46    33291  22759  15046   7976  -6826   -224       O  
-ATOM  14559  C5'  DT E  46     -11.532 -11.668  54.187  1.00185.79           C  
-ANISOU14559  C5'  DT E  46    33365  22532  14693   7988  -6910   -410       C  
-ATOM  14560  C4'  DT E  46     -10.254 -11.208  54.854  1.00184.97           C  
-ANISOU14560  C4'  DT E  46    33434  22568  14280   7864  -6836   -277       C  
-ATOM  14561  O4'  DT E  46     -10.503  -9.961  55.551  1.00184.77           O  
-ANISOU14561  O4'  DT E  46    33621  22706  13878   7878  -6740   -271       O  
-ATOM  14562  C3'  DT E  46      -9.706 -12.188  55.884  1.00185.63           C  
-ANISOU14562  C3'  DT E  46    33288  22714  14529   7728  -6759     17       C  
-ATOM  14563  O3'  DT E  46      -8.288 -12.251  55.774  1.00184.66           O  
-ANISOU14563  O3'  DT E  46    33279  22606  14278   7627  -6771     60       O  
-ATOM  14564  C2'  DT E  46     -10.177 -11.607  57.215  1.00186.24           C  
-ANISOU14564  C2'  DT E  46    33376  22977  14410   7698  -6617    187       C  
-ATOM  14565  C1'  DT E  46     -10.268 -10.110  56.936  1.00185.34           C  
-ANISOU14565  C1'  DT E  46    33600  22934  13887   7768  -6611      1       C  
-ATOM  14566  N1   DT E  46     -11.378  -9.444  57.681  1.00186.06           N  
-ANISOU14566  N1   DT E  46    33700  23134  13860   7825  -6523     33       N  
-ATOM  14567  C2   DT E  46     -11.180  -8.185  58.203  1.00185.47           C  
-ANISOU14567  C2   DT E  46    33889  23213  13368   7817  -6445     24       C  
-ATOM  14568  O2   DT E  46     -10.136  -7.568  58.084  1.00184.37           O  
-ANISOU14568  O2   DT E  46    33981  23128  12945   7766  -6443    -10       O  
-ATOM  14569  N3   DT E  46     -12.263  -7.671  58.872  1.00186.22           N  
-ANISOU14569  N3   DT E  46    33966  23398  13390   7872  -6369     56       N  
-ATOM  14570  C4   DT E  46     -13.491  -8.276  59.068  1.00187.47           C  
-ANISOU14570  C4   DT E  46    33876  23509  13845   7933  -6363     96       C  
-ATOM  14571  O4   DT E  46     -14.403  -7.733  59.684  1.00188.06           O  
-ANISOU14571  O4   DT E  46    33957  23673  13823   7979  -6291    123       O  
-ATOM  14572  C5   DT E  46     -13.629  -9.592  58.499  1.00188.03           C  
-ANISOU14572  C5   DT E  46    33679  23417  14347   7938  -6447    103       C  
-ATOM  14573  C7   DT E  46     -14.917 -10.345  58.649  1.00189.38           C  
-ANISOU14573  C7   DT E  46    33566  23523  14868   8001  -6448    145       C  
-ATOM  14574  C6   DT E  46     -12.581 -10.105  57.843  1.00187.31           C  
-ANISOU14574  C6   DT E  46    33601  23237  14330   7885  -6522     72       C  
-ATOM  14575  P    DA E  47      -7.401 -12.801  56.995  1.00197.46           P  
-ANISOU14575  P    DA E  47    34783  24351  15890   7467  -6666    364       P  
-ATOM  14576  OP1  DA E  47      -6.132 -13.321  56.438  1.00197.16           O  
-ANISOU14576  OP1  DA E  47    34771  24241  15899   7391  -6732    360       O  
-ATOM  14577  OP2  DA E  47      -8.254 -13.687  57.818  1.00199.71           O  
-ANISOU14577  OP2  DA E  47    34753  24650  16476   7452  -6606    557       O  
-ATOM  14578  O5'  DA E  47      -7.054 -11.480  57.826  1.00197.81           O  
-ANISOU14578  O5'  DA E  47    35099  24594  15464   7431  -6557    411       O  
-ATOM  14579  C5'  DA E  47      -6.554 -10.342  57.131  1.00196.76           C  
-ANISOU14579  C5'  DA E  47    35298  24471  14989   7472  -6599    205       C  
-ATOM  14580  C4'  DA E  47      -6.206  -9.219  58.090  1.00195.72           C  
-ANISOU14580  C4'  DA E  47    35387  24539  14439   7421  -6481    292       C  
-ATOM  14581  O4'  DA E  47      -7.421  -8.663  58.654  1.00195.67           O  
-ANISOU14581  O4'  DA E  47    35367  24610  14368   7494  -6414    296       O  
-ATOM  14582  C3'  DA E  47      -5.322  -9.637  59.258  1.00195.87           C  
-ANISOU14582  C3'  DA E  47    35321  24687  14415   7270  -6379    573       C  
-ATOM  14583  O3'  DA E  47      -4.300  -8.668  59.466  1.00195.40           O  
-ANISOU14583  O3'  DA E  47    35547  24742  13953   7210  -6338    564       O  
-ATOM  14584  C2'  DA E  47      -6.283  -9.724  60.441  1.00196.31           C  
-ANISOU14584  C2'  DA E  47    35207  24853  14527   7266  -6267    756       C  
-ATOM  14585  C1'  DA E  47      -7.435  -8.797  60.061  1.00195.50           C  
-ANISOU14585  C1'  DA E  47    35233  24745  14304   7404  -6282    560       C  
-ATOM  14586  N9   DA E  47      -8.742  -9.317  60.461  1.00195.76           N  
-ANISOU14586  N9   DA E  47    35018  24758  14604   7461  -6255    627       N  
-ATOM  14587  C8   DA E  47      -9.213 -10.583  60.249  1.00194.58           C  
-ANISOU14587  C8   DA E  47    34563  24484  14884   7470  -6303    683       C  
-ATOM  14588  N7   DA E  47     -10.424 -10.786  60.711  1.00194.73           N  
-ANISOU14588  N7   DA E  47    34408  24514  15066   7526  -6262    736       N  
-ATOM  14589  C5   DA E  47     -10.777  -9.568  61.265  1.00195.96           C  
-ANISOU14589  C5   DA E  47    34769  24813  14872   7555  -6182    714       C  
-ATOM  14590  C6   DA E  47     -11.946  -9.129  61.919  1.00196.31           C  
-ANISOU14590  C6   DA E  47    34773  24938  14876   7616  -6109    748       C  
-ATOM  14591  N6   DA E  47     -13.011  -9.908  62.126  1.00194.12           N  
-ANISOU14591  N6   DA E  47    34223  24606  14929   7659  -6105    812       N  
-ATOM  14592  N1   DA E  47     -11.976  -7.852  62.352  1.00197.08           N  
-ANISOU14592  N1   DA E  47    35123  25176  14581   7631  -6039    711       N  
-ATOM  14593  C2   DA E  47     -10.905  -7.077  62.141  1.00197.86           C  
-ANISOU14593  C2   DA E  47    35494  25329  14353   7588  -6043    646       C  
-ATOM  14594  N3   DA E  47      -9.754  -7.375  61.540  1.00196.53           N  
-ANISOU14594  N3   DA E  47    35393  25097  14184   7529  -6108    609       N  
-ATOM  14595  C4   DA E  47      -9.753  -8.650  61.120  1.00196.26           C  
-ANISOU14595  C4   DA E  47    35104  24923  14543   7516  -6176    647       C  
-ATOM  14596  P    DG E  48      -3.082  -8.980  60.468  1.00213.60           P  
-ANISOU14596  P    DG E  48    37827  27172  16158   7049  -6250    818       P  
-ATOM  14597  OP1  DG E  48      -1.846  -8.430  59.869  1.00212.20           O  
-ANISOU14597  OP1  DG E  48    37910  26991  15726   7010  -6296    709       O  
-ATOM  14598  OP2  DG E  48      -3.143 -10.413  60.829  1.00214.85           O  
-ANISOU14598  OP2  DG E  48    37647  27273  16715   6988  -6248   1009       O  
-ATOM  14599  O5'  DG E  48      -3.433  -8.110  61.763  1.00214.25           O  
-ANISOU14599  O5'  DG E  48    37994  27461  15949   7023  -6107    959       O  
-ATOM  14600  C5'  DG E  48      -3.663  -6.709  61.633  1.00213.77           C  
-ANISOU14600  C5'  DG E  48    38228  27477  15518   7090  -6087    801       C  
-ATOM  14601  C4'  DG E  48      -4.431  -6.160  62.824  1.00214.71           C  
-ANISOU14601  C4'  DG E  48    38332  27758  15489   7092  -5961    935       C  
-ATOM  14602  O4'  DG E  48      -5.770  -6.719  62.842  1.00215.96           O  
-ANISOU14602  O4'  DG E  48    38255  27849  15950   7174  -5971    938       O  
-ATOM  14603  C3'  DG E  48      -3.821  -6.465  64.191  1.00215.25           C  
-ANISOU14603  C3'  DG E  48    38305  27983  15499   6955  -5838   1230       C  
-ATOM  14604  O3'  DG E  48      -3.780  -5.285  64.989  1.00214.98           O  
-ANISOU14604  O3'  DG E  48    38484  28127  15073   6940  -5736   1268       O  
-ATOM  14605  C2'  DG E  48      -4.764  -7.506  64.789  1.00216.75           C  
-ANISOU14605  C2'  DG E  48    38154  28150  16053   6958  -5804   1395       C  
-ATOM  14606  C1'  DG E  48      -6.090  -7.097  64.165  1.00217.01           C  
-ANISOU14606  C1'  DG E  48    38201  28105  16147   7107  -5853   1196       C  
-ATOM  14607  N9   DG E  48      -7.068  -8.180  64.120  1.00218.21           N  
-ANISOU14607  N9   DG E  48    38037  28154  16719   7149  -5881   1248       N  
-ATOM  14608  C8   DG E  48      -6.927  -9.399  63.503  1.00218.50           C  
-ANISOU14608  C8   DG E  48    37855  28035  17130   7139  -5966   1252       C  
-ATOM  14609  N7   DG E  48      -7.970 -10.170  63.629  1.00219.65           N  
-ANISOU14609  N7   DG E  48    37737  28117  17604   7185  -5970   1303       N  
-ATOM  14610  C5   DG E  48      -8.861  -9.415  64.379  1.00220.10           C  
-ANISOU14610  C5   DG E  48    37841  28295  17493   7229  -5881   1337       C  
-ATOM  14611  C6   DG E  48     -10.164  -9.728  64.831  1.00221.23           C  
-ANISOU14611  C6   DG E  48    37778  28438  17840   7290  -5843   1396       C  
-ATOM  14612  O6   DG E  48     -10.809 -10.771  64.651  1.00221.88           O  
-ANISOU14612  O6   DG E  48    37588  28410  18305   7317  -5881   1432       O  
-ATOM  14613  N1   DG E  48     -10.719  -8.678  65.562  1.00221.44           N  
-ANISOU14613  N1   DG E  48    37946  28613  17578   7319  -5750   1412       N  
-ATOM  14614  C2   DG E  48     -10.092  -7.481  65.819  1.00220.59           C  
-ANISOU14614  C2   DG E  48    38138  28635  17041   7293  -5700   1375       C  
-ATOM  14615  N2   DG E  48     -10.783  -6.588  66.542  1.00220.86           N  
-ANISOU14615  N2   DG E  48    38267  28802  16848   7328  -5612   1399       N  
-ATOM  14616  N3   DG E  48      -8.872  -7.175  65.401  1.00219.41           N  
-ANISOU14616  N3   DG E  48    38182  28486  16697   7237  -5735   1319       N  
-ATOM  14617  C4   DG E  48      -8.320  -8.187  64.689  1.00219.29           C  
-ANISOU14617  C4   DG E  48    38034  28328  16958   7208  -5825   1303       C  
-ATOM  14618  P    DG E  49      -3.050  -5.302  66.422  1.00239.42           P  
-ANISOU14618  P    DG E  49    41551  31410  18008   6801  -5601   1551       P  
-ATOM  14619  OP1  DG E  49      -2.231  -4.074  66.532  1.00238.27           O  
-ANISOU14619  OP1  DG E  49    41734  31381  17416   6770  -5564   1490       O  
-ATOM  14620  OP2  DG E  49      -2.416  -6.628  66.597  1.00239.82           O  
-ANISOU14620  OP2  DG E  49    41355  31404  18360   6704  -5614   1726       O  
-ATOM  14621  O5'  DG E  49      -4.258  -5.171  67.462  1.00240.65           O  
-ANISOU14621  O5'  DG E  49    41573  31671  18191   6833  -5499   1680       O  
-ATOM  14622  C5'  DG E  49      -4.929  -3.924  67.608  1.00240.47           C  
-ANISOU14622  C5'  DG E  49    41758  31737  17874   6911  -5457   1569       C  
-ATOM  14623  C4'  DG E  49      -5.790  -3.927  68.858  1.00241.64           C  
-ANISOU14623  C4'  DG E  49    41759  32015  18037   6902  -5338   1760       C  
-ATOM  14624  O4'  DG E  49      -6.905  -4.833  68.668  1.00242.78           O  
-ANISOU14624  O4'  DG E  49    41625  32047  18573   6968  -5375   1767       O  
-ATOM  14625  C3'  DG E  49      -5.076  -4.390  70.124  1.00242.01           C  
-ANISOU14625  C3'  DG E  49    41689  32199  18064   6761  -5229   2054       C  
-ATOM  14626  O3'  DG E  49      -5.518  -3.625  71.237  1.00242.31           O  
-ANISOU14626  O3'  DG E  49    41790  32414  17861   6752  -5106   2167       O  
-ATOM  14627  C2'  DG E  49      -5.505  -5.848  70.243  1.00243.17           C  
-ANISOU14627  C2'  DG E  49    41476  32248  18668   6743  -5248   2192       C  
-ATOM  14628  C1'  DG E  49      -6.936  -5.763  69.729  1.00243.79           C  
-ANISOU14628  C1'  DG E  49    41485  32237  18907   6881  -5294   2040       C  
-ATOM  14629  N9   DG E  49      -7.458  -7.025  69.220  1.00244.53           N  
-ANISOU14629  N9   DG E  49    41290  32168  19452   6912  -5368   2044       N  
-ATOM  14630  C8   DG E  49      -6.754  -8.049  68.631  1.00244.30           C  
-ANISOU14630  C8   DG E  49    41131  32013  19678   6864  -5447   2057       C  
-ATOM  14631  N7   DG E  49      -7.505  -9.055  68.277  1.00245.25           N  
-ANISOU14631  N7   DG E  49    40990  32003  20191   6910  -5501   2057       N  
-ATOM  14632  C5   DG E  49      -8.786  -8.672  68.653  1.00246.14           C  
-ANISOU14632  C5   DG E  49    41056  32156  20309   6994  -5455   2042       C  
-ATOM  14633  C6   DG E  49     -10.019  -9.354  68.525  1.00247.27           C  
-ANISOU14633  C6   DG E  49    40955  32207  20791   7072  -5480   2034       C  
-ATOM  14634  O6   DG E  49     -10.229 -10.472  68.034  1.00247.80           O  
-ANISOU14634  O6   DG E  49    40788  32131  21234   7083  -5550   2038       O  
-ATOM  14635  N1   DG E  49     -11.078  -8.605  69.037  1.00247.80           N  
-ANISOU14635  N1   DG E  49    41067  32362  20724   7143  -5414   2018       N  
-ATOM  14636  C2   DG E  49     -10.960  -7.356  69.603  1.00247.21           C  
-ANISOU14636  C2   DG E  49    41241  32446  20240   7139  -5335   2012       C  
-ATOM  14637  N2   DG E  49     -12.093  -6.788  70.043  1.00247.71           N  
-ANISOU14637  N2   DG E  49    41309  32575  20235   7214  -5280   1997       N  
-ATOM  14638  N3   DG E  49      -9.811  -6.708  69.729  1.00246.12           N  
-ANISOU14638  N3   DG E  49    41334  32397  19783   7066  -5311   2019       N  
-ATOM  14639  C4   DG E  49      -8.773  -7.425  69.234  1.00245.65           C  
-ANISOU14639  C4   DG E  49    41234  32253  19850   6996  -5374   2034       C  
-TER   14640       DG E  49                                                      
-HETATM14641  PB  ADP A 935       0.945   3.094 -22.714  1.00 75.98           P  
-ANISOU14641  PB  ADP A 935     9391  11078   8401   2846    793   2839       P  
-HETATM14642  O1B ADP A 935       1.502   1.740 -22.347  1.00 75.54           O  
-ANISOU14642  O1B ADP A 935     9684  11012   8005   2735    650   2864       O  
-HETATM14643  O2B ADP A 935       1.142   3.455 -24.167  1.00 74.62           O  
-ANISOU14643  O2B ADP A 935     9154  10733   8465   2876    728   2955       O  
-HETATM14644  O3B ADP A 935       1.300   4.204 -21.748  1.00 76.62           O  
-ANISOU14644  O3B ADP A 935     9301  11184   8627   3041    940   2566       O  
-HETATM14645  PA  ADP A 935      -1.303   2.236 -21.250  1.00 79.31           P  
-ANISOU14645  PA  ADP A 935     9722  11944   8468   2564    930   3022       P  
-HETATM14646  O1A ADP A 935      -1.460   0.752 -21.486  1.00 79.04           O  
-ANISOU14646  O1A ADP A 935     9968  11936   8127   2356    779   3220       O  
-HETATM14647  O2A ADP A 935      -0.565   2.725 -20.023  1.00 79.96           O  
-ANISOU14647  O2A ADP A 935     9811  12041   8531   2722   1010   2733       O  
-HETATM14648  O3A ADP A 935      -0.650   2.922 -22.554  1.00 77.67           O  
-ANISOU14648  O3A ADP A 935     9442  11514   8554   2681    880   3031       O  
-HETATM14649  O5' ADP A 935      -2.775   2.878 -21.235  1.00 83.29           O  
-ANISOU14649  O5' ADP A 935     9911  12626   9110   2510   1081   3135       O  
-HETATM14650  C5' ADP A 935      -3.669   2.491 -20.200  1.00 88.61           C  
-ANISOU14650  C5' ADP A 935    10563  13522   9584   2403   1159   3157       C  
-HETATM14651  C4' ADP A 935      -4.964   3.290 -20.257  1.00 92.24           C  
-ANISOU14651  C4' ADP A 935    10696  14126  10225   2384   1312   3242       C  
-HETATM14652  O4' ADP A 935      -5.540   3.216 -21.562  1.00 92.06           O  
-ANISOU14652  O4' ADP A 935    10601  14054  10324   2291   1258   3480       O  
-HETATM14653  C3' ADP A 935      -5.955   2.706 -19.265  1.00 94.88           C  
-ANISOU14653  C3' ADP A 935    11035  14694  10321   2242   1373   3302       C  
-HETATM14654  O3' ADP A 935      -6.288   3.678 -18.275  1.00 97.48           O  
-ANISOU14654  O3' ADP A 935    11136  15141  10761   2358   1551   3124       O  
-HETATM14655  C2' ADP A 935      -7.174   2.310 -20.071  1.00 96.15           C  
-ANISOU14655  C2' ADP A 935    11114  14943  10476   2060   1356   3590       C  
-HETATM14656  O2' ADP A 935      -8.325   3.029 -19.617  1.00 98.42           O  
-ANISOU14656  O2' ADP A 935    11115  15408  10874   2057   1524   3604       O  
-HETATM14657  C1' ADP A 935      -6.846   2.648 -21.519  1.00 95.09           C  
-ANISOU14657  C1' ADP A 935    10936  14621  10572   2099   1281   3693       C  
-HETATM14658  N9  ADP A 935      -6.780   1.399 -22.313  1.00 95.38           N  
-ANISOU14658  N9  ADP A 935    11228  14598  10414   1927   1104   3908       N  
-HETATM14659  C8  ADP A 935      -5.671   0.651 -22.470  1.00 95.65           C  
-ANISOU14659  C8  ADP A 935    11553  14489  10300   1930    955   3866       C  
-HETATM14660  N7  ADP A 935      -5.914  -0.432 -23.249  1.00 95.91           N  
-ANISOU14660  N7  ADP A 935    11769  14499  10172   1750    815   4100       N  
-HETATM14661  C5  ADP A 935      -7.212  -0.385 -23.605  1.00 96.06           C  
-ANISOU14661  C5  ADP A 935    11611  14651  10236   1627    873   4299       C  
-HETATM14662  C6  ADP A 935      -8.122  -1.220 -24.424  1.00 96.32           C  
-ANISOU14662  C6  ADP A 935    11693  14740  10166   1416    793   4595       C  
-HETATM14663  N6  ADP A 935      -7.684  -2.349 -25.028  1.00 95.67           N  
-ANISOU14663  N6  ADP A 935    11891  14564   9895   1297    619   4729       N  
-HETATM14664  N1  ADP A 935      -9.406  -0.815 -24.546  1.00 96.92           N  
-ANISOU14664  N1  ADP A 935    11521  14962  10341   1345    900   4728       N  
-HETATM14665  C2  ADP A 935      -9.853   0.306 -23.947  1.00 97.25           C  
-ANISOU14665  C2  ADP A 935    11282  15097  10571   1462   1074   4598       C  
-HETATM14666  N3  ADP A 935      -9.086   1.112 -23.190  1.00 96.95           N  
-ANISOU14666  N3  ADP A 935    11184  15016  10636   1655   1156   4329       N  
-HETATM14667  C4  ADP A 935      -7.778   0.825 -22.986  1.00 96.49           C  
-ANISOU14667  C4  ADP A 935    11352  14814  10495   1745   1064   4171       C  
-HETATM14668  O   HOH A 936       4.750   4.963 -22.363  1.00 60.12           O  
-HETATM14669  O   HOH A 937       4.411   1.912 -22.188  1.00 57.45           O  
-HETATM14670  O   HOH A 938      11.846   1.823 -24.150  1.00 60.94           O  
-HETATM14671  O   HOH A 939       6.484  -1.609 -33.199  1.00 39.84           O  
-HETATM14672  O   HOH A 940      -4.881   1.997 -33.009  1.00 84.94           O  
-HETATM14673  O   HOH A 941      10.443   8.047 -23.487  1.00 55.88           O  
-HETATM14674  O   HOH A 942       4.076  -1.219  27.979  1.00 42.72           O  
-HETATM14675  O   HOH B   1      32.911   5.621 -18.751  1.00 59.98           O  
-HETATM14676  O   HOH B   2      23.041  11.815 -20.420  1.00 51.22           O  
-HETATM14677  O   HOH B   3      26.302  17.368 -19.894  1.00 51.12           O  
-HETATM14678  O   HOH B   4      24.564  10.465 -13.214  1.00 42.41           O  
-HETATM14679  O   HOH B   5      32.906  18.733  -5.560  1.00 50.88           O  
-HETATM14680  O   HOH B   6      14.434  16.479  -1.281  1.00 41.18           O  
-HETATM14681  O   HOH B   7       0.646  22.386  -7.823  1.00 75.42           O  
-HETATM14682  O   HOH B  12      11.620  10.225 -25.463  1.00 54.17           O  
-CONECT1464114642146431464414648                                                 
-CONECT1464214641                                                                
-CONECT1464314641                                                                
-CONECT1464414641                                                                
-CONECT1464514646146471464814649                                                 
-CONECT1464614645                                                                
-CONECT1464714645                                                                
-CONECT146481464114645                                                           
-CONECT146491464514650                                                           
-CONECT146501464914651                                                           
-CONECT14651146501465214653                                                      
-CONECT146521465114657                                                           
-CONECT14653146511465414655                                                      
-CONECT1465414653                                                                
-CONECT14655146531465614657                                                      
-CONECT1465614655                                                                
-CONECT14657146521465514658                                                      
-CONECT14658146571465914667                                                      
-CONECT146591465814660                                                           
-CONECT146601465914661                                                           
-CONECT14661146601466214667                                                      
-CONECT14662146611466314664                                                      
-CONECT1466314662                                                                
-CONECT146641466214665                                                           
-CONECT146651466414666                                                           
-CONECT146661466514667                                                           
-CONECT14667146581466114666                                                      
-MASTER     1232    0    1   77   54    0    4    614628    4   27  147          
-END                                                                             
diff --git a/plip/test/pdb/4agl.pdb b/plip/test/pdb/4agl.pdb
deleted file mode 100644
index 3ea3130..0000000
--- a/plip/test/pdb/4agl.pdb
+++ /dev/null
@@ -1,4509 +0,0 @@
-HEADER    CELL CYCLE                              30-JAN-12   4AGL              
-TITLE     STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO THE            
-TITLE    2 STABILIZING SMALL MOLECULE PHIKAN784                                 
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 FRAGMENT: DNA-BINDING DOMAIN, RESIDUES 94-312;                       
-COMPND   5 SYNONYM: ANTIGEN NY-CO-13, PHOSPHOPROTEIN P53, TUMOR SUPPRESSOR P53; 
-COMPND   6 ENGINEERED: YES;                                                     
-COMPND   7 MUTATION: YES                                                        
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
-KEYWDS    TRANSCRIPTION, CELL CYCLE, APOPTOSIS, CANCER MUTATION, SURFACE        
-KEYWDS   2 CREVICE, PROTEIN FOLDING, AGGREGATION, MUTANT RESCUE,                
-KEYWDS   3 SMALL-MOLECULE DRUG, PROTEIN STABILIZATION, HALOGEN BONDING          
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    A.C.JOERGER,R.WILCKEN,F.M.BOECKLER,A.R.FERSHT                         
-REVDAT   2   02-MAY-12 4AGL    1       JRNL                                     
-REVDAT   1   21-MAR-12 4AGL    0                                                
-JRNL        AUTH   R.WILCKEN,X.LIU,M.O.ZIMMERMANN,T.J.RUTHERFORD,A.R.FERSHT,    
-JRNL        AUTH 2 A.C.JOERGER,F.M.BOECKLER                                     
-JRNL        TITL   HALOGEN-ENRICHED FRAGMENT LIBRARIES AS LEADS FOR DRUG        
-JRNL        TITL 2 RESCUE OF MUTANT P53.                                        
-JRNL        REF    J.AM.CHEM.SOC.                V. 134  6810 2012              
-JRNL        REFN                   ISSN 0002-7863                               
-JRNL        PMID   22439615                                                     
-JRNL        DOI    10.1021/JA301056A                                            
-REMARK   1                                                                      
-REMARK   1 REFERENCE 1                                                          
-REMARK   1  AUTH   A.C.JOERGER,H.C.ANG,A.R.FERSHT                               
-REMARK   1  TITL   STRUCTURAL BASIS FOR UNDERSTANDING ONCOGENIC P53 MUTATIONS   
-REMARK   1  TITL 2 AND DESIGNING RESCUE DRUGS.                                  
-REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V. 103 15056 2006              
-REMARK   1  REFN                   ISSN 0027-8424                               
-REMARK   1  PMID   17015838                                                     
-REMARK   1  DOI    10.1073/PNAS.0607286103                                      
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
-REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
-REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
-REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
-REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
-REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
-REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : ML                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.700                          
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.757                         
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.75                          
-REMARK   3   NUMBER OF REFLECTIONS             : 54631                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1647                          
-REMARK   3   R VALUE            (WORKING SET) : 0.1632                          
-REMARK   3   FREE R VALUE                     : 0.1925                          
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
-REMARK   3   FREE R VALUE TEST SET COUNT      : 2732                            
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 24.7594 -  4.6051    0.99     2793   123  0.1787 0.1761        
-REMARK   3     2  4.6051 -  3.6590    1.00     2684   126  0.1463 0.1647        
-REMARK   3     3  3.6590 -  3.1976    1.00     2653   139  0.1476 0.1652        
-REMARK   3     4  3.1976 -  2.9057    1.00     2632   129  0.1580 0.1702        
-REMARK   3     5  2.9057 -  2.6977    1.00     2600   143  0.1587 0.2209        
-REMARK   3     6  2.6977 -  2.5388    1.00     2605   134  0.1591 0.1899        
-REMARK   3     7  2.5388 -  2.4118    1.00     2612   137  0.1592 0.1673        
-REMARK   3     8  2.4118 -  2.3069    1.00     2581   135  0.1579 0.1837        
-REMARK   3     9  2.3069 -  2.2181    1.00     2606   122  0.1529 0.1807        
-REMARK   3    10  2.2181 -  2.1416    1.00     2581   139  0.1585 0.1952        
-REMARK   3    11  2.1416 -  2.0747    1.00     2547   158  0.1540 0.1989        
-REMARK   3    12  2.0747 -  2.0154    1.00     2596   125  0.1566 0.1983        
-REMARK   3    13  2.0154 -  1.9624    1.00     2572   122  0.1636 0.1859        
-REMARK   3    14  1.9624 -  1.9145    1.00     2567   141  0.1486 0.2117        
-REMARK   3    15  1.9145 -  1.8710    1.00     2548   138  0.1608 0.1749        
-REMARK   3    16  1.8710 -  1.8312    1.00     2579   151  0.1656 0.2153        
-REMARK   3    17  1.8312 -  1.7946    1.00     2526   158  0.1684 0.2473        
-REMARK   3    18  1.7946 -  1.7607    0.99     2533   142  0.1721 0.1909        
-REMARK   3    19  1.7607 -  1.7293    1.00     2584   124  0.1753 0.2071        
-REMARK   3    20  1.7293 -  1.7000    0.99     2500   146  0.1789 0.2251        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.11                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
-REMARK   3   K_SOL              : 0.364                                         
-REMARK   3   B_SOL              : 40.542                                        
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.17             
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.50            
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 12.27                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.9                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 7.0608                                               
-REMARK   3    B22 (A**2) : -1.8381                                              
-REMARK   3    B33 (A**2) : -5.2227                                              
-REMARK   3    B12 (A**2) : 0.0000                                               
-REMARK   3    B13 (A**2) : 0.0000                                               
-REMARK   3    B23 (A**2) : 0.0000                                               
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.007           3232                                  
-REMARK   3   ANGLE     :  1.032           4403                                  
-REMARK   3   CHIRALITY :  0.078            479                                  
-REMARK   3   PLANARITY :  0.005            582                                  
-REMARK   3   DIHEDRAL  : 14.260           1227                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 4AGL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-12.                  
-REMARK 100 THE PDBE ID CODE IS EBI-50576.                                       
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : NULL                               
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : NULL                               
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : DIAMOND                            
-REMARK 200  BEAMLINE                       : I04                                
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
-REMARK 200  DATA SCALING SOFTWARE          : NULL                               
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54754                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.70                               
-REMARK 200  RESOLUTION RANGE LOW       (A) : 42.40                              
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
-REMARK 200  DATA REDUNDANCY                : 5.4                                
-REMARK 200  R MERGE                    (I) : 0.01                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.90                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 5.4                                
-REMARK 200  R MERGE FOR SHELL          (I) : 0.31                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.30                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
-REMARK 200 SOFTWARE USED: PHENIX                                                
-REMARK 200 STARTING MODEL: PDB ENTRY 2J1X                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NONE                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 51                                        
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5                      
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING-DROP VAPOR DIFFUSION AT          
-REMARK 280  21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM             
-REMARK 280  SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR           
-REMARK 280  BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE                
-REMARK 280  GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN            
-REMARK 280  100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19%           
-REMARK 280  (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150            
-REMARK 280  MM KCL.                                                             
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.66500            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.82500            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.52000            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.82500            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.66500            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.52000            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2                                                    
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 400                                                                      
-REMARK 400 COMPOUND                                                             
-REMARK 400 ENGINEERED RESIDUE IN CHAIN A, MET 133 TO LEU                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 203 TO ALA                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TYR 220 TO CYS                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 239 TO TYR                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 268 TO ASP                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN B, MET 133 TO LEU                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 203 TO ALA                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN B, TYR 220 TO CYS                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 239 TO TYR                        
-REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 268 TO ASP                        
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     SER A    94                                                      
-REMARK 465     SER A    95                                                      
-REMARK 465     LYS A   291                                                      
-REMARK 465     LYS A   292                                                      
-REMARK 465     GLY A   293                                                      
-REMARK 465     GLU A   294                                                      
-REMARK 465     PRO A   295                                                      
-REMARK 465     HIS A   296                                                      
-REMARK 465     HIS A   297                                                      
-REMARK 465     GLU A   298                                                      
-REMARK 465     LEU A   299                                                      
-REMARK 465     PRO A   300                                                      
-REMARK 465     PRO A   301                                                      
-REMARK 465     GLY A   302                                                      
-REMARK 465     SER A   303                                                      
-REMARK 465     THR A   304                                                      
-REMARK 465     LYS A   305                                                      
-REMARK 465     ARG A   306                                                      
-REMARK 465     ALA A   307                                                      
-REMARK 465     LEU A   308                                                      
-REMARK 465     PRO A   309                                                      
-REMARK 465     ASN A   310                                                      
-REMARK 465     ASN A   311                                                      
-REMARK 465     THR A   312                                                      
-REMARK 465     LYS B   291                                                      
-REMARK 465     LYS B   292                                                      
-REMARK 465     GLY B   293                                                      
-REMARK 465     GLU B   294                                                      
-REMARK 465     PRO B   295                                                      
-REMARK 465     HIS B   296                                                      
-REMARK 465     HIS B   297                                                      
-REMARK 465     GLU B   298                                                      
-REMARK 465     LEU B   299                                                      
-REMARK 465     PRO B   300                                                      
-REMARK 465     PRO B   301                                                      
-REMARK 465     GLY B   302                                                      
-REMARK 465     SER B   303                                                      
-REMARK 465     THR B   304                                                      
-REMARK 465     LYS B   305                                                      
-REMARK 465     ARG B   306                                                      
-REMARK 465     ALA B   307                                                      
-REMARK 465     LEU B   308                                                      
-REMARK 465     PRO B   309                                                      
-REMARK 465     ASN B   310                                                      
-REMARK 465     ASN B   311                                                      
-REMARK 465     THR B   312                                                      
-REMARK 600                                                                      
-REMARK 600 HETEROGEN                                                            
-REMARK 600 2,4-DIIODO-6-{[METHYL(1-METHYLPIPERIDIN-4-YL)AMINO]METHYL}PHENOL     
-REMARK 610                                                                      
-REMARK 610 MISSING HETEROATOM                                                   
-REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 610 I=INSERTION CODE):                                                   
-REMARK 610   M RES C SSEQI                                                      
-REMARK 610     P84 A  400                                                       
-REMARK 610     P84 B  400                                                       
-REMARK 620                                                                      
-REMARK 620 METAL COORDINATION                                                   
-REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              ZN A1300  ZN                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 CYS A 176   SG                                                     
-REMARK 620 2 HIS A 179   ND1 104.5                                              
-REMARK 620 3 CYS A 238   SG  111.0 101.2                                        
-REMARK 620 4 CYS A 238   SG  111.9 120.7  22.4                                  
-REMARK 620 5 CYS A 242   SG  110.7 104.9 122.3 103.8                            
-REMARK 620 N                    1     2     3     4                             
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              ZN B1300  ZN                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 HIS B 179   ND1                                                    
-REMARK 620 2 CYS B 238   SG  108.7                                              
-REMARK 620 3 CYS B 176   SG  102.6 111.6                                        
-REMARK 620 4 CYS B 242   SG  106.8 115.3 110.9                                  
-REMARK 620 N                    1     2     3                                   
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P84 A 400                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1300                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P84 B 400                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1300                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 2BIQ   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT T123A-M133L-H168R-V203A-               
-REMARK 900  N239Y-R249S-N268D                                                   
-REMARK 900 RELATED ID: 1DT7   RELATED DB: PDB                                   
-REMARK 900  SOLUTION STRUCTURE OF THE C-TERMINAL NEGATIVE REGULATORY            
-REMARK 900   DOMAIN OF P53 IN A COMPLEX WITH CA2+-BOUND S100B(                  
-REMARK 900  BB)                                                                 
-REMARK 900 RELATED ID: 2YBG   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF LYS120-ACETYLATED P53 CORE DOMAIN                      
-REMARK 900 RELATED ID: 1UOL   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN P53 CORE DOMAIN MUTANT               
-REMARK 900   M133L/V203A/N239Y/N268D AT 1.9 A RESOLUTION.                       
-REMARK 900 RELATED ID: 2J1X   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-Y220C-N239Y-               
-REMARK 900  N268D                                                               
-REMARK 900 RELATED ID: 2FOJ   RELATED DB: PDB                                   
-REMARK 900  THE CRYSTAL STRUCURE OF THE N-TERMINAL DOMAIN OF                    
-REMARK 900  HAUSP/USP7COMPLEXED WITH P53 PEPTIDE 364-367                        
-REMARK 900 RELATED ID: 2B3G   RELATED DB: PDB                                   
-REMARK 900  P53N (FRAGMENT 33-60) BOUND TO RPA70N                               
-REMARK 900 RELATED ID: 2BIN   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-H168R-V203A-N239Y-               
-REMARK 900  N268D                                                               
-REMARK 900 RELATED ID: 1OLH   RELATED DB: PDB                                   
-REMARK 900  P53 (OLIGOMERIZATION DOMAIN) (NMR, 35 STRUCTURES)                   
-REMARK 900 RELATED ID: 1TSR   RELATED DB: PDB                                   
-REMARK 900  P53 CORE DOMAIN IN COMPLEX WITH DEOXYRIBONUCLEIC ACID               
-REMARK 900 RELATED ID: 1PES   RELATED DB: PDB                                   
-REMARK 900  TUMOR ANTIGEN P53 (TETRAMERIZATION DOMAIN) (P53TET) (NMR            
-REMARK 900  , MINIMIZED AVERAGE STRUCTURE)                                      
-REMARK 900 RELATED ID: 2J21   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-N268D-               
-REMARK 900  R282W                                                               
-REMARK 900 RELATED ID: 2GS0   RELATED DB: PDB                                   
-REMARK 900  NMR STRUCTURE OF THE COMPLEX BETWEEN THE PH DOMAIN                  
-REMARK 900  OF THETFB1 SUBUNIT FROM TFIIH AND THE ACTIVATION                    
-REMARK 900  DOMAIN OF P53                                                       
-REMARK 900 RELATED ID: 2J0Z   RELATED DB: PDB                                   
-REMARK 900  P53 TETRAMERIZATION DOMAIN WILD TYPE                                
-REMARK 900 RELATED ID: 2X0V   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO 4-(TRIFLUOROMETHYL)BENZENE-1,2-DIAMINE                           
-REMARK 900 RELATED ID: 1C26   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF P53 TETRAMERIZATION DOMAIN                     
-REMARK 900 RELATED ID: 1SAL   RELATED DB: PDB                                   
-REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE                       
-REMARK 900  OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR              
-REMARK 900   (SAD STRUCTURES)                                                   
-REMARK 900 RELATED ID: 1KZY   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE 53BP1 BRCT REGION COMPLEXED                
-REMARK 900  TOTUMOR SUPPRESSOR P53                                              
-REMARK 900 RELATED ID: 1XQH   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF                           
-REMARK 900  THEMETHYLTRANSFERASE SET9 (ALSO KNOWN AS SET7/9) WITH               
-REMARK 900  A P53PEPTIDE AND SAH                                                
-REMARK 900 RELATED ID: 2FEJ   RELATED DB: PDB                                   
-REMARK 900  SOLUTION STRUCTURE OF HUMAN P53 DNA BINDING DOMAIN.                 
-REMARK 900 RELATED ID: 1A1U   RELATED DB: PDB                                   
-REMARK 900  SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT                    
-REMARK 900  DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE               
-REMARK 900 RELATED ID: 2AHI   RELATED DB: PDB                                   
-REMARK 900  STRUCTURAL BASIS OF DNA RECOGNITION BY P53 TETRAMERS(               
-REMARK 900  COMPLEX III)                                                        
-REMARK 900 RELATED ID: 2WGX   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-Y236F-N239Y-               
-REMARK 900  T253I-N268D                                                         
-REMARK 900 RELATED ID: 3SAK   RELATED DB: PDB                                   
-REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE                       
-REMARK 900  OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR              
-REMARK 900   (SAC STRUCTURES)                                                   
-REMARK 900 RELATED ID: 1SAF   RELATED DB: PDB                                   
-REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE                       
-REMARK 900  OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR              
-REMARK 900   (SAD STRUCTURES)                                                   
-REMARK 900 RELATED ID: 2FOO   RELATED DB: PDB                                   
-REMARK 900  THE CRYSTAL STRUCURE OF THE N-TERMINAL DOMAIN OF                    
-REMARK 900  HAUSP/USP7COMPLEXED WITH P53 PEPTIDE 359-362                        
-REMARK 900 RELATED ID: 2BIO   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-R249S-               
-REMARK 900  N268D                                                               
-REMARK 900 RELATED ID: 2YDR   RELATED DB: PDB                                   
-REMARK 900  CPOGA D298N IN COMPLEX WITH P53-DERIVED O-GLCNAC                    
-REMARK 900  PEPTIDE                                                             
-REMARK 900 RELATED ID: 1OLG   RELATED DB: PDB                                   
-REMARK 900  P53 (OLIGOMERIZATION DOMAIN) (NMR, MINIMIZED AVERAGE                
-REMARK 900  STRUCTURE)                                                          
-REMARK 900 RELATED ID: 2BIP   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-H168R-V203A-N239Y-               
-REMARK 900  R249S-N268D                                                         
-REMARK 900 RELATED ID: 2J11   RELATED DB: PDB                                   
-REMARK 900  P53 TETRAMERIZATION DOMAIN MUTANT Y327S T329G Q331G                 
-REMARK 900 RELATED ID: 1PET   RELATED DB: PDB                                   
-REMARK 900  TUMOR ANTIGEN P53 (TETRAMERIZATION DOMAIN) (P53TET) (NMR            
-REMARK 900  , 19 STRUCTURES)                                                    
-REMARK 900 RELATED ID: 2J1Y   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-G245S-               
-REMARK 900  N268D                                                               
-REMARK 900 RELATED ID: 1JSP   RELATED DB: PDB                                   
-REMARK 900  NMR STRUCTURE OF CBP BROMODOMAIN IN COMPLEX WITH P53                
-REMARK 900  PEPTIDE                                                             
-REMARK 900 RELATED ID: 1MA3   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF A SIR2 ENZYME BOUND TO AN ACETYLATED                   
-REMARK 900  P53PEPTIDE                                                          
-REMARK 900 RELATED ID: 2X0W   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO 5,6-DIMETHOXY-2-METHYLBENZOTHIAZOLE                              
-REMARK 900 RELATED ID: 2XWR   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF HUMAN                
-REMARK 900  P53 WITH EXTENDED N TERMINUS                                        
-REMARK 900 RELATED ID: 2VUK   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO THE STABILIZING SMALL-MOLECULE DRUG PHIKAN083                    
-REMARK 900 RELATED ID: 1AIE   RELATED DB: PDB                                   
-REMARK 900  P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE                        
-REMARK 900 RELATED ID: 2H1L   RELATED DB: PDB                                   
-REMARK 900  THE STRUCTURE OF THE ONCOPROTEIN SV40 LARGE T ANTIGEN               
-REMARK 900   ANDP53 TUMOR SUPPRESSOR COMPLEX                                    
-REMARK 900 RELATED ID: 1SAJ   RELATED DB: PDB                                   
-REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE                       
-REMARK 900  OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR              
-REMARK 900   (SAD STRUCTURES)                                                   
-REMARK 900 RELATED ID: 1TUP   RELATED DB: PDB                                   
-REMARK 900  TUMOR SUPPRESSOR P53 COMPLEXED WITH DEOXYRIBONUCLEIC ACID           
-REMARK 900 RELATED ID: 1HS5   RELATED DB: PDB                                   
-REMARK 900  NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER                        
-REMARK 900 RELATED ID: 2ATA   RELATED DB: PDB                                   
-REMARK 900  STRUCTURAL BASIS OF DNA RECOGNITION BY P53 TETRAMERS(               
-REMARK 900  COMPLEX II)                                                         
-REMARK 900 RELATED ID: 2X0U   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO A 2-AMINO SUBSTITUTED BENZOTHIAZOLE SCAFFOLD                     
-REMARK 900 RELATED ID: 1YCQ   RELATED DB: PDB                                   
-REMARK 900  XENOPUS LAEVIS MDM2 BOUND TO THE TRANSACTIVATION DOMAIN             
-REMARK 900   OF HUMAN P53                                                       
-REMARK 900 RELATED ID: 1GZH   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE BRCT DOMAINS OF HUMAN 53BP1                
-REMARK 900  BOUND TO THE P53 TUMOR SUPRESSOR                                    
-REMARK 900 RELATED ID: 1SAH   RELATED DB: PDB                                   
-REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE                       
-REMARK 900  OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR              
-REMARK 900   (SAD STRUCTURES)                                                   
-REMARK 900 RELATED ID: 2BIM   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-N268D-               
-REMARK 900  R273H                                                               
-REMARK 900 RELATED ID: 1YCR   RELATED DB: PDB                                   
-REMARK 900  MDM2 BOUND TO THE TRANSACTIVATION DOMAIN OF P53                     
-REMARK 900 RELATED ID: 1SAK   RELATED DB: PDB                                   
-REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE                       
-REMARK 900  OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR              
-REMARK 900   (SAC STRUCTURES)                                                   
-REMARK 900 RELATED ID: 2J10   RELATED DB: PDB                                   
-REMARK 900  P53 TETRAMERIZATION DOMAIN MUTANT T329F Q331K                       
-REMARK 900 RELATED ID: 2ADY   RELATED DB: PDB                                   
-REMARK 900  STRUCTURAL BASIS OF DNA RECOGNITION BY P53 TETRAMERS(               
-REMARK 900  COMPLEX IV)                                                         
-REMARK 900 RELATED ID: 1SAE   RELATED DB: PDB                                   
-REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE                       
-REMARK 900  OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR              
-REMARK 900   (SAC STRUCTURES)                                                   
-REMARK 900 RELATED ID: 2J1Z   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-N268D-               
-REMARK 900  F270L                                                               
-REMARK 900 RELATED ID: 4AGO   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO THE STABILIZING SMALL MOLECULE PHIKAN5174                        
-REMARK 900 RELATED ID: 1YCS   RELATED DB: PDB                                   
-REMARK 900  P53-53BP2 COMPLEX                                                   
-REMARK 900 RELATED ID: 2AC0   RELATED DB: PDB                                   
-REMARK 900  STRUCTURAL BASIS OF DNA RECOGNITION BY P53 TETRAMERS(               
-REMARK 900  COMPLEX I)                                                          
-REMARK 900 RELATED ID: 2J20   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-N268D-               
-REMARK 900  R273C                                                               
-REMARK 900 RELATED ID: 1H26   RELATED DB: PDB                                   
-REMARK 900  CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT              
-REMARK 900   PEPTIDE FROM P53                                                   
-REMARK 900 RELATED ID: 2J1W   RELATED DB: PDB                                   
-REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V143A-V203A-N239Y-               
-REMARK 900  N268D                                                               
-REMARK 900 RELATED ID: 4AGM   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO THE STABILIZING SMALL MOLECULE PHIKAN5086                        
-REMARK 900 RELATED ID: 4AGN   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO THE STABILIZING SMALL MOLECULE PHIKAN5116                        
-REMARK 900 RELATED ID: 4AGP   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO THE STABILIZING SMALL MOLECULE PHIKAN5176                        
-REMARK 900 RELATED ID: 4AGQ   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND                 
-REMARK 900  TO THE STABILIZING SMALL MOLECULE PHIKAN5196                        
-DBREF  4AGL A   94   312  UNP    P04637   P53_HUMAN       94    312             
-DBREF  4AGL B   94   312  UNP    P04637   P53_HUMAN       94    312             
-SEQADV 4AGL LEU A  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
-SEQADV 4AGL ALA A  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
-SEQADV 4AGL CYS A  220  UNP  P04637    TYR   220 ENGINEERED MUTATION            
-SEQADV 4AGL TYR A  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
-SEQADV 4AGL ASP A  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
-SEQADV 4AGL LEU B  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
-SEQADV 4AGL ALA B  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
-SEQADV 4AGL CYS B  220  UNP  P04637    TYR   220 ENGINEERED MUTATION            
-SEQADV 4AGL TYR B  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
-SEQADV 4AGL ASP B  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
-SEQRES   1 A  219  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
-SEQRES   2 A  219  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
-SEQRES   3 A  219  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
-SEQRES   4 A  219  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
-SEQRES   5 A  219  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
-SEQRES   6 A  219  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
-SEQRES   7 A  219  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
-SEQRES   8 A  219  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
-SEQRES   9 A  219  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
-SEQRES  10 A  219  THR PHE ARG HIS SER VAL VAL VAL PRO CYS GLU PRO PRO          
-SEQRES  11 A  219  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
-SEQRES  12 A  219  MET CYS TYR SER SER CYS MET GLY GLY MET ASN ARG ARG          
-SEQRES  13 A  219  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
-SEQRES  14 A  219  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
-SEQRES  15 A  219  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
-SEQRES  16 A  219  LEU ARG LYS LYS GLY GLU PRO HIS HIS GLU LEU PRO PRO          
-SEQRES  17 A  219  GLY SER THR LYS ARG ALA LEU PRO ASN ASN THR                  
-SEQRES   1 B  219  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
-SEQRES   2 B  219  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
-SEQRES   3 B  219  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
-SEQRES   4 B  219  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
-SEQRES   5 B  219  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
-SEQRES   6 B  219  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
-SEQRES   7 B  219  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
-SEQRES   8 B  219  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
-SEQRES   9 B  219  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
-SEQRES  10 B  219  THR PHE ARG HIS SER VAL VAL VAL PRO CYS GLU PRO PRO          
-SEQRES  11 B  219  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
-SEQRES  12 B  219  MET CYS TYR SER SER CYS MET GLY GLY MET ASN ARG ARG          
-SEQRES  13 B  219  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
-SEQRES  14 B  219  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
-SEQRES  15 B  219  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
-SEQRES  16 B  219  LEU ARG LYS LYS GLY GLU PRO HIS HIS GLU LEU PRO PRO          
-SEQRES  17 B  219  GLY SER THR LYS ARG ALA LEU PRO ASN ASN THR                  
-HET    P84  A 400      13                                                       
-HET     ZN  A1300       1                                                       
-HET    P84  B 400      13                                                       
-HET     ZN  B1300       1                                                       
-HETNAM     P84 2,4-BIS(IODANYL)-6-[[METHYL-(1-METHYLPIPERIDIN-4-YL)             
-HETNAM   2 P84  AMINO]METHYL}PHENOL                                             
-HETNAM      ZN ZINC ION                                                         
-FORMUL   3  P84    2(C16 H22 I2 N2 O)                                           
-FORMUL   4   ZN    2(ZN 2+)                                                     
-FORMUL   5  HOH   *638(H2 O)                                                    
-HELIX    1   1 GLN A  165  MET A  169  5                                   5    
-HELIX    2   2 HIS A  178  CYS A  182  5                                   5    
-HELIX    3   3 CYS A  277  ARG A  290  1                                  14    
-HELIX    4   4 HIS B  178  CYS B  182  5                                   5    
-HELIX    5   5 CYS B  277  ARG B  290  1                                  14    
-SHEET    1  AA 4 ARG A 110  GLY A 112  0                                        
-SHEET    2  AA 4 CYS A 141  TRP A 146 -1  O  GLN A 144   N  GLY A 112           
-SHEET    3  AA 4 THR A 230  TYR A 236 -1  O  THR A 230   N  LEU A 145           
-SHEET    4  AA 4 ILE A 195  VAL A 197 -1  O  ARG A 196   N  ASN A 235           
-SHEET    1  AB 7 CYS A 124  SER A 127  0                                        
-SHEET    2  AB 7 LYS A 132  CYS A 135 -1  O  LYS A 132   N  SER A 127           
-SHEET    3  AB 7 LEU A 264  VAL A 274  1  O  GLU A 271   N  LEU A 133           
-SHEET    4  AB 7 ILE A 251  GLU A 258 -1  O  ILE A 251   N  VAL A 272           
-SHEET    5  AB 7 ARG A 156  TYR A 163 -1  O  ARG A 156   N  GLU A 258           
-SHEET    6  AB 7 HIS A 214  PRO A 219 -1  O  VAL A 216   N  ALA A 159           
-SHEET    7  AB 7 GLU A 204  ASP A 207 -1  O  GLU A 204   N  VAL A 217           
-SHEET    1  BA 4 ARG B 110  GLY B 112  0                                        
-SHEET    2  BA 4 CYS B 141  TRP B 146 -1  O  GLN B 144   N  GLY B 112           
-SHEET    3  BA 4 THR B 230  TYR B 236 -1  O  THR B 230   N  LEU B 145           
-SHEET    4  BA 4 ILE B 195  VAL B 197 -1  O  ARG B 196   N  ASN B 235           
-SHEET    1  BB 7 CYS B 124  SER B 127  0                                        
-SHEET    2  BB 7 LYS B 132  CYS B 135 -1  O  LYS B 132   N  SER B 127           
-SHEET    3  BB 7 LEU B 264  VAL B 274  1  O  GLU B 271   N  LEU B 133           
-SHEET    4  BB 7 ILE B 251  GLU B 258 -1  O  ILE B 251   N  VAL B 272           
-SHEET    5  BB 7 ARG B 156  TYR B 163 -1  O  ARG B 156   N  GLU B 258           
-SHEET    6  BB 7 HIS B 214  PRO B 219 -1  O  VAL B 216   N  ALA B 159           
-SHEET    7  BB 7 GLU B 204  ASP B 207 -1  O  GLU B 204   N  VAL B 217           
-LINK        ZN    ZN A1300                 SG  CYS A 176     1555   1555  2.36  
-LINK        ZN    ZN A1300                 ND1 HIS A 179     1555   1555  2.02  
-LINK        ZN    ZN A1300                 SG ACYS A 238     1555   1555  2.47  
-LINK        ZN    ZN A1300                 SG BCYS A 238     1555   1555  2.27  
-LINK        ZN    ZN A1300                 SG  CYS A 242     1555   1555  2.33  
-LINK        ZN    ZN B1300                 SG  CYS B 238     1555   1555  2.35  
-LINK        ZN    ZN B1300                 SG  CYS B 176     1555   1555  2.35  
-LINK        ZN    ZN B1300                 SG  CYS B 242     1555   1555  2.33  
-LINK        ZN    ZN B1300                 ND1 HIS B 179     1555   1555  2.04  
-SITE     1 AC1  8 LEU A 145  VAL A 147  THR A 150  GLU A 221                    
-SITE     2 AC1  8 PRO A 222  PRO A 223  THR A 230  HOH A2110                    
-SITE     1 AC2  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
-SITE     1 AC3  7 LEU B 145  VAL B 147  THR B 150  GLU B 221                    
-SITE     2 AC3  7 PRO B 222  PRO B 223  HOH B2093                               
-SITE     1 AC4  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
-CRYST1   65.330   71.040  105.650  90.00  90.00  90.00 P 21 21 21    8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.015307  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.014077  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.009465        0.00000                         
-ATOM      1  N   SER A  96     115.078  73.616 -36.053  1.00 40.08           N  
-ATOM      2  CA  SER A  96     115.079  75.050 -36.303  1.00 32.83           C  
-ATOM      3  C   SER A  96     114.097  75.789 -35.396  1.00 30.32           C  
-ATOM      4  O   SER A  96     113.393  75.179 -34.584  1.00 29.83           O  
-ATOM      5  CB  SER A  96     114.760  75.345 -37.770  1.00 38.74           C  
-ATOM      6  OG  SER A  96     113.478  74.854 -38.125  1.00 41.81           O  
-ATOM      7  N   VAL A  97     114.061  77.108 -35.553  1.00 29.30           N  
-ATOM      8  CA  VAL A  97     113.240  77.975 -34.726  1.00 22.29           C  
-ATOM      9  C   VAL A  97     112.646  79.085 -35.588  1.00 26.56           C  
-ATOM     10  O   VAL A  97     113.378  79.838 -36.232  1.00 23.09           O  
-ATOM     11  CB  VAL A  97     114.077  78.624 -33.608  1.00 22.96           C  
-ATOM     12  CG1 VAL A  97     113.227  79.577 -32.774  1.00 24.67           C  
-ATOM     13  CG2 VAL A  97     114.726  77.558 -32.731  1.00 20.45           C  
-ATOM     14  N   PRO A  98     111.314  79.198 -35.593  1.00 17.02           N  
-ATOM     15  CA  PRO A  98     110.641  80.241 -36.374  1.00 18.53           C  
-ATOM     16  C   PRO A  98     111.056  81.632 -35.909  1.00 19.72           C  
-ATOM     17  O   PRO A  98     111.250  81.850 -34.722  1.00 17.02           O  
-ATOM     18  CB  PRO A  98     109.152  80.004 -36.066  1.00 20.08           C  
-ATOM     19  CG  PRO A  98     109.075  78.596 -35.585  1.00 23.62           C  
-ATOM     20  CD  PRO A  98     110.359  78.355 -34.854  1.00 19.24           C  
-ATOM     21  N   SER A  99     111.181  82.569 -36.842  1.00 16.12           N  
-ATOM     22  CA  SER A  99     111.508  83.943 -36.490  1.00 17.46           C  
-ATOM     23  C   SER A  99     110.384  84.580 -35.676  1.00 15.55           C  
-ATOM     24  O   SER A  99     109.211  84.273 -35.882  1.00 17.06           O  
-ATOM     25  CB  SER A  99     111.756  84.763 -37.762  1.00 19.83           C  
-ATOM     26  OG  SER A  99     111.934  86.134 -37.448  1.00 22.54           O  
-ATOM     27  N   GLN A 100     110.745  85.472 -34.760  1.00 16.17           N  
-ATOM     28  CA  GLN A 100     109.751  86.229 -33.997  1.00 17.06           C  
-ATOM     29  C   GLN A 100     109.943  87.725 -34.191  1.00 20.02           C  
-ATOM     30  O   GLN A 100     109.435  88.532 -33.422  1.00 18.38           O  
-ATOM     31  CB  GLN A 100     109.831  85.886 -32.505  1.00 16.79           C  
-ATOM     32  CG  GLN A 100     111.177  86.192 -31.876  1.00 18.47           C  
-ATOM     33  CD  GLN A 100     111.208  85.850 -30.398  1.00 20.80           C  
-ATOM     34  OE1 GLN A 100     111.591  84.744 -30.011  1.00 26.02           O  
-ATOM     35  NE2 GLN A 100     110.800  86.798 -29.567  1.00 16.39           N  
-ATOM     36  N   LYS A 101     110.683  88.092 -35.229  1.00 16.41           N  
-ATOM     37  CA  LYS A 101     110.993  89.493 -35.486  1.00 16.24           C  
-ATOM     38  C   LYS A 101     109.755  90.256 -35.967  1.00 17.09           C  
-ATOM     39  O   LYS A 101     109.140  89.872 -36.960  1.00 15.26           O  
-ATOM     40  CB  LYS A 101     112.100  89.573 -36.540  1.00 17.99           C  
-ATOM     41  CG  LYS A 101     112.325  90.951 -37.135  1.00 23.71           C  
-ATOM     42  CD  LYS A 101     113.110  91.842 -36.201  1.00 31.95           C  
-ATOM     43  CE  LYS A 101     113.551  93.120 -36.911  1.00 34.74           C  
-ATOM     44  NZ  LYS A 101     114.457  92.840 -38.061  1.00 37.01           N  
-ATOM     45  N   THR A 102     109.398  91.331 -35.269  1.00 14.84           N  
-ATOM     46  CA  THR A 102     108.262  92.161 -35.681  1.00 12.85           C  
-ATOM     47  C   THR A 102     108.545  92.756 -37.059  1.00 14.04           C  
-ATOM     48  O   THR A 102     109.627  93.291 -37.299  1.00 15.62           O  
-ATOM     49  CB  THR A 102     107.969  93.288 -34.667  1.00 15.05           C  
-ATOM     50  OG1 THR A 102     107.621  92.715 -33.404  1.00 19.05           O  
-ATOM     51  CG2 THR A 102     106.815  94.163 -35.127  1.00 14.04           C  
-ATOM     52  N   TYR A 103     107.567  92.649 -37.956  1.00 10.29           N  
-ATOM     53  CA  TYR A 103     107.721  93.097 -39.338  1.00 11.24           C  
-ATOM     54  C   TYR A 103     106.372  93.554 -39.888  1.00 13.22           C  
-ATOM     55  O   TYR A 103     105.501  92.727 -40.158  1.00 10.70           O  
-ATOM     56  CB  TYR A 103     108.270  91.938 -40.178  1.00 11.44           C  
-ATOM     57  CG  TYR A 103     108.366  92.201 -41.663  1.00 16.37           C  
-ATOM     58  CD1 TYR A 103     109.124  93.249 -42.153  1.00 16.40           C  
-ATOM     59  CD2 TYR A 103     107.724  91.366 -42.572  1.00 17.44           C  
-ATOM     60  CE1 TYR A 103     109.217  93.483 -43.525  1.00 20.28           C  
-ATOM     61  CE2 TYR A 103     107.817  91.587 -43.937  1.00 16.54           C  
-ATOM     62  CZ  TYR A 103     108.559  92.645 -44.401  1.00 19.67           C  
-ATOM     63  OH  TYR A 103     108.647  92.859 -45.759  1.00 30.47           O  
-ATOM     64  N   GLN A 104     106.190  94.859 -40.065  1.00 10.58           N  
-ATOM     65  CA  GLN A 104     104.917  95.357 -40.590  1.00 10.47           C  
-ATOM     66  C   GLN A 104     104.704  95.057 -42.067  1.00 11.23           C  
-ATOM     67  O   GLN A 104     103.570  94.860 -42.501  1.00 10.63           O  
-ATOM     68  CB  GLN A 104     104.760  96.855 -40.337  1.00 11.26           C  
-ATOM     69  CG  GLN A 104     104.551  97.180 -38.862  1.00 12.38           C  
-ATOM     70  CD  GLN A 104     103.682  98.409 -38.652  1.00 17.16           C  
-ATOM     71  OE1 GLN A 104     103.370  99.142 -39.598  1.00 18.90           O  
-ATOM     72  NE2 GLN A 104     103.289  98.645 -37.413  1.00 17.46           N  
-ATOM     73  N   GLY A 105     105.786  95.049 -42.841  1.00 13.00           N  
-ATOM     74  CA  GLY A 105     105.687  94.738 -44.260  1.00 13.41           C  
-ATOM     75  C   GLY A 105     104.993  95.823 -45.075  1.00 12.80           C  
-ATOM     76  O   GLY A 105     104.723  96.920 -44.574  1.00 12.24           O  
-ATOM     77  N   SER A 106     104.688  95.513 -46.332  1.00 11.21           N  
-ATOM     78  CA  SER A 106     104.152  96.506 -47.265  1.00 11.90           C  
-ATOM     79  C   SER A 106     102.757  96.984 -46.896  1.00 13.04           C  
-ATOM     80  O   SER A 106     102.332  98.074 -47.305  1.00 13.87           O  
-ATOM     81  CB  SER A 106     104.121  95.935 -48.689  1.00 14.07           C  
-ATOM     82  OG  SER A 106     105.400  95.453 -49.052  1.00 25.56           O  
-ATOM     83  N   TYR A 107     102.040  96.164 -46.132  1.00 11.46           N  
-ATOM     84  CA  TYR A 107     100.649  96.461 -45.828  1.00 10.45           C  
-ATOM     85  C   TYR A 107     100.432  97.071 -44.449  1.00 10.50           C  
-ATOM     86  O   TYR A 107      99.303  97.372 -44.092  1.00 11.20           O  
-ATOM     87  CB  TYR A 107      99.775  95.221 -46.039  1.00 10.39           C  
-ATOM     88  CG  TYR A 107      99.939  94.698 -47.443  1.00  9.86           C  
-ATOM     89  CD1 TYR A 107      99.362  95.370 -48.515  1.00 15.96           C  
-ATOM     90  CD2 TYR A 107     100.707  93.569 -47.708  1.00 13.64           C  
-ATOM     91  CE1 TYR A 107      99.529  94.924 -49.810  1.00 14.69           C  
-ATOM     92  CE2 TYR A 107     100.871  93.111 -49.021  1.00 16.11           C  
-ATOM     93  CZ  TYR A 107     100.280  93.799 -50.058  1.00 19.94           C  
-ATOM     94  OH  TYR A 107     100.430  93.373 -51.366  1.00 18.22           O  
-ATOM     95  N   GLY A 108     101.512  97.277 -43.703  1.00  8.67           N  
-ATOM     96  CA  GLY A 108     101.423  97.894 -42.386  1.00 10.03           C  
-ATOM     97  C   GLY A 108     100.714  97.002 -41.377  1.00  9.26           C  
-ATOM     98  O   GLY A 108      99.861  97.458 -40.614  1.00 11.29           O  
-ATOM     99  N   PHE A 109     101.061  95.722 -41.391  1.00  9.01           N  
-ATOM    100  CA  PHE A 109     100.411  94.725 -40.532  1.00  7.14           C  
-ATOM    101  C   PHE A 109     100.824  94.820 -39.066  1.00  9.88           C  
-ATOM    102  O   PHE A 109     102.010  94.846 -38.750  1.00  9.08           O  
-ATOM    103  CB  PHE A 109     100.742  93.326 -41.060  1.00  5.69           C  
-ATOM    104  CG  PHE A 109     100.162  92.208 -40.231  1.00  5.60           C  
-ATOM    105  CD1 PHE A 109      98.799  91.950 -40.253  1.00  8.68           C  
-ATOM    106  CD2 PHE A 109     100.983  91.428 -39.420  1.00  8.18           C  
-ATOM    107  CE1 PHE A 109      98.256  90.911 -39.483  1.00  9.83           C  
-ATOM    108  CE2 PHE A 109     100.451  90.383 -38.648  1.00  7.64           C  
-ATOM    109  CZ  PHE A 109      99.089  90.131 -38.684  1.00 10.14           C  
-ATOM    110  N   ARG A 110      99.841  94.845 -38.169  1.00  7.09           N  
-ATOM    111  CA  ARG A 110     100.117  94.706 -36.735  1.00  7.43           C  
-ATOM    112  C   ARG A 110      98.875  94.234 -35.990  1.00  8.62           C  
-ATOM    113  O   ARG A 110      97.763  94.300 -36.523  1.00  8.25           O  
-ATOM    114  CB  ARG A 110     100.631  96.025 -36.127  1.00  9.71           C  
-ATOM    115  CG  ARG A 110      99.582  97.133 -35.981  1.00  8.53           C  
-ATOM    116  CD  ARG A 110      99.377  97.881 -37.322  1.00  7.77           C  
-ATOM    117  NE  ARG A 110      98.470  99.013 -37.149  1.00  9.79           N  
-ATOM    118  CZ  ARG A 110      98.074  99.814 -38.137  1.00 14.48           C  
-ATOM    119  NH1 ARG A 110      98.506  99.611 -39.376  1.00 13.19           N  
-ATOM    120  NH2 ARG A 110      97.241 100.821 -37.886  1.00 12.64           N  
-ATOM    121  N   LEU A 111      99.067  93.758 -34.756  1.00  7.13           N  
-ATOM    122  CA  LEU A 111      97.959  93.262 -33.936  1.00  6.06           C  
-ATOM    123  C   LEU A 111      97.369  94.347 -33.056  1.00  8.50           C  
-ATOM    124  O   LEU A 111      97.979  95.398 -32.878  1.00 10.53           O  
-ATOM    125  CB  LEU A 111      98.441  92.109 -33.045  1.00  7.16           C  
-ATOM    126  CG  LEU A 111      99.084  90.934 -33.768  1.00  7.17           C  
-ATOM    127  CD1 LEU A 111      99.629  89.898 -32.749  1.00  6.53           C  
-ATOM    128  CD2 LEU A 111      98.079  90.282 -34.710  1.00  6.67           C  
-ATOM    129  N   GLY A 112      96.179  94.077 -32.516  1.00  6.45           N  
-ATOM    130  CA  GLY A 112      95.527  94.949 -31.549  1.00  7.53           C  
-ATOM    131  C   GLY A 112      94.809  94.109 -30.507  1.00  8.21           C  
-ATOM    132  O   GLY A 112      94.352  93.004 -30.793  1.00  7.98           O  
-ATOM    133  N   PHE A 113      94.711  94.627 -29.288  1.00  6.46           N  
-ATOM    134  CA  PHE A 113      94.012  93.905 -28.233  1.00  8.03           C  
-ATOM    135  C   PHE A 113      92.986  94.799 -27.542  1.00 11.61           C  
-ATOM    136  O   PHE A 113      93.157  96.011 -27.488  1.00 11.53           O  
-ATOM    137  CB  PHE A 113      95.007  93.366 -27.204  1.00 11.84           C  
-ATOM    138  CG  PHE A 113      95.987  92.386 -27.778  1.00  9.00           C  
-ATOM    139  CD1 PHE A 113      97.146  92.834 -28.390  1.00  8.92           C  
-ATOM    140  CD2 PHE A 113      95.750  91.019 -27.700  1.00  8.77           C  
-ATOM    141  CE1 PHE A 113      98.054  91.936 -28.932  1.00 11.55           C  
-ATOM    142  CE2 PHE A 113      96.651  90.110 -28.232  1.00 10.01           C  
-ATOM    143  CZ  PHE A 113      97.809  90.566 -28.847  1.00  9.18           C  
-ATOM    144  N   LEU A 114      91.922  94.186 -27.029  1.00 11.01           N  
-ATOM    145  CA  LEU A 114      90.898  94.917 -26.292  1.00 12.54           C  
-ATOM    146  C   LEU A 114      91.455  95.349 -24.944  1.00 13.83           C  
-ATOM    147  O   LEU A 114      92.497  94.854 -24.512  1.00 13.23           O  
-ATOM    148  CB  LEU A 114      89.677  94.020 -26.071  1.00 15.18           C  
-ATOM    149  CG  LEU A 114      88.947  93.585 -27.341  1.00 17.50           C  
-ATOM    150  CD1 LEU A 114      87.762  92.694 -26.998  1.00 23.56           C  
-ATOM    151  CD2 LEU A 114      88.497  94.800 -28.119  1.00 21.40           C  
-ATOM    152  N   HIS A 115      90.750  96.257 -24.272  1.00 13.30           N  
-ATOM    153  CA  HIS A 115      91.119  96.670 -22.921  1.00 12.62           C  
-ATOM    154  C   HIS A 115      90.122  96.095 -21.922  1.00 15.83           C  
-ATOM    155  O   HIS A 115      89.090  96.694 -21.634  1.00 17.56           O  
-ATOM    156  CB  HIS A 115      91.220  98.197 -22.838  1.00 13.87           C  
-ATOM    157  CG  HIS A 115      92.144  98.771 -23.868  1.00 12.84           C  
-ATOM    158  ND1 HIS A 115      93.501  98.892 -23.667  1.00 18.37           N  
-ATOM    159  CD2 HIS A 115      91.914  99.184 -25.136  1.00 14.65           C  
-ATOM    160  CE1 HIS A 115      94.063  99.386 -24.758  1.00 11.16           C  
-ATOM    161  NE2 HIS A 115      93.120  99.577 -25.661  1.00 21.38           N  
-ATOM    162  N   SER A 116      90.439  94.914 -21.402  1.00 11.92           N  
-ATOM    163  CA  SER A 116      89.462  94.127 -20.653  1.00 12.31           C  
-ATOM    164  C   SER A 116      89.552  94.297 -19.148  1.00 16.51           C  
-ATOM    165  O   SER A 116      88.668  93.841 -18.426  1.00 15.82           O  
-ATOM    166  CB  SER A 116      89.601  92.640 -20.997  1.00 15.95           C  
-ATOM    167  OG  SER A 116      89.423  92.442 -22.393  1.00 20.97           O  
-ATOM    168  N   GLY A 117      90.625  94.921 -18.674  1.00 15.73           N  
-ATOM    169  CA  GLY A 117      90.791  95.159 -17.244  1.00 16.14           C  
-ATOM    170  C   GLY A 117      91.334  93.962 -16.488  1.00 16.92           C  
-ATOM    171  O   GLY A 117      91.658  92.935 -17.088  1.00 15.53           O  
-ATOM    172  N   THR A 118      91.429  94.078 -15.163  1.00 15.15           N  
-ATOM    173  CA  THR A 118      92.055  93.029 -14.364  1.00 14.95           C  
-ATOM    174  C   THR A 118      91.198  92.537 -13.194  1.00 18.89           C  
-ATOM    175  O   THR A 118      91.726  92.002 -12.221  1.00 17.97           O  
-ATOM    176  CB  THR A 118      93.426  93.478 -13.815  1.00 18.94           C  
-ATOM    177  OG1 THR A 118      93.251  94.635 -12.991  1.00 17.72           O  
-ATOM    178  CG2 THR A 118      94.376  93.832 -14.964  1.00 22.09           C  
-ATOM    179  N   ALA A 119      89.884  92.694 -13.300  1.00 15.56           N  
-ATOM    180  CA  ALA A 119      88.983  92.172 -12.274  1.00 17.88           C  
-ATOM    181  C   ALA A 119      89.180  90.670 -12.141  1.00 26.89           C  
-ATOM    182  O   ALA A 119      89.557  90.006 -13.106  1.00 21.80           O  
-ATOM    183  CB  ALA A 119      87.539  92.497 -12.620  1.00 22.47           C  
-ATOM    184  N   LYS A 120      88.933  90.122 -10.953  1.00 22.49           N  
-ATOM    185  CA  LYS A 120      89.165  88.696 -10.743  1.00 23.37           C  
-ATOM    186  C   LYS A 120      88.316  87.823 -11.673  1.00 25.12           C  
-ATOM    187  O   LYS A 120      88.677  86.681 -11.962  1.00 25.95           O  
-ATOM    188  CB  LYS A 120      88.954  88.301  -9.274  1.00 33.35           C  
-ATOM    189  CG  LYS A 120      87.503  88.166  -8.850  1.00 46.00           C  
-ATOM    190  CD  LYS A 120      87.404  87.609  -7.430  1.00 52.59           C  
-ATOM    191  CE  LYS A 120      85.953  87.404  -7.010  1.00 64.15           C  
-ATOM    192  NZ  LYS A 120      85.841  86.788  -5.656  1.00 64.50           N  
-ATOM    193  N   SER A 121      87.206  88.368 -12.162  1.00 20.96           N  
-ATOM    194  CA  SER A 121      86.314  87.614 -13.045  1.00 21.99           C  
-ATOM    195  C   SER A 121      86.682  87.661 -14.541  1.00 24.33           C  
-ATOM    196  O   SER A 121      86.015  87.035 -15.364  1.00 23.53           O  
-ATOM    197  CB  SER A 121      84.874  88.099 -12.876  1.00 31.21           C  
-ATOM    198  OG  SER A 121      84.729  89.424 -13.357  1.00 35.08           O  
-ATOM    199  N   VAL A 122      87.719  88.409 -14.904  1.00 20.54           N  
-ATOM    200  CA  VAL A 122      88.065  88.537 -16.322  1.00 15.23           C  
-ATOM    201  C   VAL A 122      88.622  87.214 -16.878  1.00 14.07           C  
-ATOM    202  O   VAL A 122      89.339  86.495 -16.183  1.00 15.28           O  
-ATOM    203  CB  VAL A 122      89.051  89.714 -16.553  1.00 13.98           C  
-ATOM    204  CG1 VAL A 122      90.463  89.322 -16.146  1.00 17.51           C  
-ATOM    205  CG2 VAL A 122      88.998  90.195 -17.999  1.00 17.73           C  
-ATOM    206  N   THR A 123      88.297  86.889 -18.132  1.00 11.40           N  
-ATOM    207  CA  THR A 123      88.685  85.589 -18.702  1.00 10.35           C  
-ATOM    208  C   THR A 123      89.845  85.695 -19.695  1.00 12.21           C  
-ATOM    209  O   THR A 123      90.465  84.682 -20.070  1.00 12.07           O  
-ATOM    210  CB  THR A 123      87.497  84.911 -19.436  1.00 13.64           C  
-ATOM    211  OG1 THR A 123      87.055  85.750 -20.511  1.00 14.86           O  
-ATOM    212  CG2 THR A 123      86.333  84.659 -18.480  1.00 17.60           C  
-ATOM    213  N   CYS A 124      90.109  86.919 -20.140  1.00 11.49           N  
-ATOM    214  CA  CYS A 124      91.169  87.190 -21.101  1.00  8.95           C  
-ATOM    215  C   CYS A 124      91.550  88.657 -20.955  1.00 10.93           C  
-ATOM    216  O   CYS A 124      90.686  89.526 -20.971  1.00 11.54           O  
-ATOM    217  CB  CYS A 124      90.691  86.901 -22.531  1.00 10.81           C  
-ATOM    218  SG  CYS A 124      91.924  87.249 -23.824  1.00 12.65           S  
-ATOM    219  N   THR A 125      92.836  88.939 -20.796  1.00  8.92           N  
-ATOM    220  CA  THR A 125      93.260  90.323 -20.633  1.00  7.92           C  
-ATOM    221  C   THR A 125      94.693  90.491 -21.135  1.00  7.43           C  
-ATOM    222  O   THR A 125      95.533  89.618 -20.938  1.00  9.11           O  
-ATOM    223  CB  THR A 125      93.099  90.796 -19.160  1.00  9.11           C  
-ATOM    224  OG1 THR A 125      93.360  92.206 -19.068  1.00 11.72           O  
-ATOM    225  CG2 THR A 125      94.030  90.023 -18.220  1.00  8.96           C  
-ATOM    226  N   TYR A 126      94.950  91.602 -21.816  1.00  8.35           N  
-ATOM    227  CA  TYR A 126      96.247  91.831 -22.431  1.00  7.63           C  
-ATOM    228  C   TYR A 126      97.018  92.932 -21.705  1.00  9.08           C  
-ATOM    229  O   TYR A 126      96.464  93.994 -21.414  1.00  9.77           O  
-ATOM    230  CB  TYR A 126      96.070  92.233 -23.905  1.00  8.07           C  
-ATOM    231  CG  TYR A 126      97.370  92.630 -24.554  1.00  8.67           C  
-ATOM    232  CD1 TYR A 126      98.324  91.671 -24.883  1.00  7.69           C  
-ATOM    233  CD2 TYR A 126      97.650  93.968 -24.835  1.00  7.36           C  
-ATOM    234  CE1 TYR A 126      99.534  92.032 -25.471  1.00  8.47           C  
-ATOM    235  CE2 TYR A 126      98.848  94.339 -25.422  1.00  7.26           C  
-ATOM    236  CZ  TYR A 126      99.786  93.365 -25.738  1.00  9.98           C  
-ATOM    237  OH  TYR A 126     100.990  93.738 -26.306  1.00  9.74           O  
-ATOM    238  N   SER A 127      98.303  92.681 -21.458  1.00  7.64           N  
-ATOM    239  CA  SER A 127      99.186  93.672 -20.844  1.00 10.21           C  
-ATOM    240  C   SER A 127     100.138  94.291 -21.863  1.00  7.94           C  
-ATOM    241  O   SER A 127     101.064  93.632 -22.336  1.00  8.74           O  
-ATOM    242  CB  SER A 127     100.018  93.013 -19.738  1.00 10.87           C  
-ATOM    243  OG  SER A 127     101.022  93.899 -19.267  1.00 10.61           O  
-ATOM    244  N   PRO A 128      99.915  95.563 -22.214  1.00  9.17           N  
-ATOM    245  CA  PRO A 128     100.853  96.209 -23.137  1.00  9.45           C  
-ATOM    246  C   PRO A 128     102.255  96.353 -22.543  1.00  9.89           C  
-ATOM    247  O   PRO A 128     103.233  96.242 -23.273  1.00 11.70           O  
-ATOM    248  CB  PRO A 128     100.228  97.594 -23.374  1.00 11.69           C  
-ATOM    249  CG  PRO A 128      98.759  97.412 -23.094  1.00 12.82           C  
-ATOM    250  CD  PRO A 128      98.682  96.342 -22.005  1.00  7.09           C  
-ATOM    251  N   ALA A 129     102.355  96.611 -21.239  1.00 11.44           N  
-ATOM    252  CA  ALA A 129     103.669  96.769 -20.621  1.00 13.27           C  
-ATOM    253  C   ALA A 129     104.509  95.502 -20.701  1.00 13.46           C  
-ATOM    254  O   ALA A 129     105.733  95.572 -20.801  1.00 15.27           O  
-ATOM    255  CB  ALA A 129     103.540  97.237 -19.172  1.00 14.14           C  
-ATOM    256  N   LEU A 130     103.849  94.345 -20.662  1.00  9.33           N  
-ATOM    257  CA  LEU A 130     104.542  93.057 -20.739  1.00  9.92           C  
-ATOM    258  C   LEU A 130     104.489  92.440 -22.139  1.00 10.88           C  
-ATOM    259  O   LEU A 130     105.136  91.421 -22.383  1.00 12.67           O  
-ATOM    260  CB  LEU A 130     103.924  92.068 -19.733  1.00  8.70           C  
-ATOM    261  CG  LEU A 130     104.030  92.479 -18.258  1.00 13.09           C  
-ATOM    262  CD1 LEU A 130     103.068  91.672 -17.367  1.00 12.12           C  
-ATOM    263  CD2 LEU A 130     105.481  92.338 -17.784  1.00 13.53           C  
-ATOM    264  N   ASN A 131     103.727  93.059 -23.046  1.00  9.37           N  
-ATOM    265  CA  ASN A 131     103.348  92.421 -24.325  1.00  9.44           C  
-ATOM    266  C   ASN A 131     102.939  90.971 -24.085  1.00  7.19           C  
-ATOM    267  O   ASN A 131     103.486  90.044 -24.695  1.00  8.62           O  
-ATOM    268  CB  ASN A 131     104.467  92.478 -25.370  1.00  9.42           C  
-ATOM    269  CG  ASN A 131     104.014  91.963 -26.736  1.00 12.14           C  
-ATOM    270  OD1 ASN A 131     102.842  92.082 -27.100  1.00 10.30           O  
-ATOM    271  ND2 ASN A 131     104.947  91.420 -27.504  1.00 11.40           N  
-ATOM    272  N   LYS A 132     101.953  90.786 -23.219  1.00  9.27           N  
-ATOM    273  CA  LYS A 132     101.594  89.457 -22.749  1.00  7.60           C  
-ATOM    274  C   LYS A 132     100.087  89.329 -22.545  1.00  7.05           C  
-ATOM    275  O   LYS A 132      99.467  90.162 -21.884  1.00  8.22           O  
-ATOM    276  CB  LYS A 132     102.339  89.154 -21.443  1.00  7.92           C  
-ATOM    277  CG  LYS A 132     102.095  87.762 -20.868  1.00  8.07           C  
-ATOM    278  CD  LYS A 132     103.085  87.467 -19.736  1.00 13.73           C  
-ATOM    279  CE  LYS A 132     102.906  86.053 -19.195  1.00 12.70           C  
-ATOM    280  NZ  LYS A 132     104.008  85.670 -18.255  1.00 15.30           N  
-ATOM    281  N   LEU A 133      99.516  88.287 -23.141  1.00  6.98           N  
-ATOM    282  CA  LEU A 133      98.099  87.960 -22.990  1.00  6.13           C  
-ATOM    283  C   LEU A 133      97.942  86.928 -21.867  1.00  8.44           C  
-ATOM    284  O   LEU A 133      98.667  85.943 -21.830  1.00 10.07           O  
-ATOM    285  CB  LEU A 133      97.580  87.358 -24.298  1.00  8.63           C  
-ATOM    286  CG  LEU A 133      96.081  87.086 -24.377  1.00 10.35           C  
-ATOM    287  CD1 LEU A 133      95.334  88.411 -24.411  1.00 12.07           C  
-ATOM    288  CD2 LEU A 133      95.768  86.275 -25.626  1.00 12.87           C  
-ATOM    289  N   PHE A 134      97.002  87.175 -20.958  1.00  8.31           N  
-ATOM    290  CA  PHE A 134      96.680  86.251 -19.872  1.00  7.89           C  
-ATOM    291  C   PHE A 134      95.255  85.759 -20.121  1.00  9.73           C  
-ATOM    292  O   PHE A 134      94.348  86.575 -20.302  1.00  9.72           O  
-ATOM    293  CB  PHE A 134      96.705  86.998 -18.536  1.00  9.78           C  
-ATOM    294  CG  PHE A 134      98.050  87.553 -18.163  1.00  9.99           C  
-ATOM    295  CD1 PHE A 134      98.509  88.742 -18.718  1.00  8.44           C  
-ATOM    296  CD2 PHE A 134      98.840  86.904 -17.228  1.00 12.63           C  
-ATOM    297  CE1 PHE A 134      99.743  89.258 -18.361  1.00 10.81           C  
-ATOM    298  CE2 PHE A 134     100.078  87.415 -16.861  1.00 10.89           C  
-ATOM    299  CZ  PHE A 134     100.532  88.594 -17.438  1.00 12.12           C  
-ATOM    300  N   CYS A 135      95.047  84.444 -20.152  1.00  9.76           N  
-ATOM    301  CA  CYS A 135      93.709  83.928 -20.455  1.00  9.60           C  
-ATOM    302  C   CYS A 135      93.412  82.626 -19.726  1.00 10.80           C  
-ATOM    303  O   CYS A 135      94.323  81.881 -19.369  1.00 10.74           O  
-ATOM    304  CB  CYS A 135      93.535  83.708 -21.960  1.00  8.76           C  
-ATOM    305  SG  CYS A 135      94.672  82.472 -22.661  1.00 12.46           S  
-ATOM    306  N   GLN A 136      92.127  82.367 -19.520  1.00 11.01           N  
-ATOM    307  CA  GLN A 136      91.672  81.092 -18.969  1.00 11.01           C  
-ATOM    308  C   GLN A 136      91.684  79.990 -20.025  1.00 10.72           C  
-ATOM    309  O   GLN A 136      91.686  80.250 -21.224  1.00  9.78           O  
-ATOM    310  CB  GLN A 136      90.275  81.251 -18.359  1.00 11.24           C  
-ATOM    311  CG  GLN A 136      90.286  82.069 -17.069  1.00 14.78           C  
-ATOM    312  CD  GLN A 136      88.901  82.314 -16.495  1.00 22.23           C  
-ATOM    313  OE1 GLN A 136      87.889  82.054 -17.145  1.00 22.76           O  
-ATOM    314  NE2 GLN A 136      88.854  82.834 -15.272  1.00 25.12           N  
-ATOM    315  N   LEU A 137      91.702  78.748 -19.561  1.00  9.61           N  
-ATOM    316  CA  LEU A 137      91.692  77.591 -20.435  1.00  8.81           C  
-ATOM    317  C   LEU A 137      90.484  77.568 -21.372  1.00 12.51           C  
-ATOM    318  O   LEU A 137      89.337  77.633 -20.916  1.00 10.75           O  
-ATOM    319  CB  LEU A 137      91.680  76.341 -19.548  1.00 10.25           C  
-ATOM    320  CG  LEU A 137      91.657  74.995 -20.254  1.00 14.51           C  
-ATOM    321  CD1 LEU A 137      92.940  74.781 -21.002  1.00 14.98           C  
-ATOM    322  CD2 LEU A 137      91.465  73.915 -19.193  1.00 17.57           C  
-ATOM    323  N   ALA A 138      90.752  77.490 -22.677  1.00  9.88           N  
-ATOM    324  CA  ALA A 138      89.717  77.320 -23.700  1.00 10.61           C  
-ATOM    325  C   ALA A 138      88.732  78.483 -23.850  1.00 18.42           C  
-ATOM    326  O   ALA A 138      87.705  78.334 -24.504  1.00 24.81           O  
-ATOM    327  CB  ALA A 138      88.953  75.998 -23.482  1.00 15.44           C  
-ATOM    328  N   LYS A 139      89.041  79.638 -23.270  1.00 11.35           N  
-ATOM    329  CA  LYS A 139      88.140  80.778 -23.385  1.00  9.86           C  
-ATOM    330  C   LYS A 139      88.500  81.634 -24.585  1.00 11.35           C  
-ATOM    331  O   LYS A 139      89.640  81.630 -25.043  1.00 10.79           O  
-ATOM    332  CB  LYS A 139      88.171  81.641 -22.118  1.00  9.30           C  
-ATOM    333  CG  LYS A 139      87.840  80.888 -20.826  1.00 16.83           C  
-ATOM    334  CD  LYS A 139      86.411  80.396 -20.794  1.00 24.61           C  
-ATOM    335  CE  LYS A 139      86.039  79.887 -19.394  1.00 27.77           C  
-ATOM    336  NZ  LYS A 139      84.608  79.500 -19.318  1.00 39.70           N  
-ATOM    337  N   THR A 140      87.511  82.363 -25.089  1.00  8.63           N  
-ATOM    338  CA  THR A 140      87.693  83.229 -26.259  1.00  7.84           C  
-ATOM    339  C   THR A 140      88.782  84.280 -26.044  1.00 11.18           C  
-ATOM    340  O   THR A 140      88.739  85.011 -25.063  1.00 10.21           O  
-ATOM    341  CB  THR A 140      86.366  83.928 -26.591  1.00  9.18           C  
-ATOM    342  OG1 THR A 140      85.362  82.931 -26.832  1.00 10.70           O  
-ATOM    343  CG2 THR A 140      86.508  84.823 -27.836  1.00  9.84           C  
-ATOM    344  N   CYS A 141      89.747  84.359 -26.968  1.00  8.43           N  
-ATOM    345  CA  CYS A 141      90.758  85.419 -26.939  1.00  8.23           C  
-ATOM    346  C   CYS A 141      90.670  86.238 -28.219  1.00  7.25           C  
-ATOM    347  O   CYS A 141      91.186  85.813 -29.264  1.00  7.86           O  
-ATOM    348  CB  CYS A 141      92.173  84.834 -26.835  1.00  6.88           C  
-ATOM    349  SG  CYS A 141      92.465  83.840 -25.355  1.00 10.30           S  
-ATOM    350  N   PRO A 142      90.009  87.402 -28.156  1.00  7.33           N  
-ATOM    351  CA  PRO A 142      89.882  88.271 -29.332  1.00  8.29           C  
-ATOM    352  C   PRO A 142      91.211  88.933 -29.660  1.00  9.92           C  
-ATOM    353  O   PRO A 142      91.813  89.605 -28.818  1.00 12.21           O  
-ATOM    354  CB  PRO A 142      88.862  89.330 -28.894  1.00 13.17           C  
-ATOM    355  CG  PRO A 142      88.268  88.811 -27.594  1.00 15.42           C  
-ATOM    356  CD  PRO A 142      89.332  87.962 -26.975  1.00 14.54           C  
-ATOM    357  N   VAL A 143      91.673  88.729 -30.887  1.00  7.88           N  
-ATOM    358  CA  VAL A 143      92.894  89.359 -31.345  1.00  7.23           C  
-ATOM    359  C   VAL A 143      92.572  90.135 -32.622  1.00  7.31           C  
-ATOM    360  O   VAL A 143      92.068  89.569 -33.591  1.00  8.76           O  
-ATOM    361  CB  VAL A 143      94.010  88.328 -31.593  1.00  8.09           C  
-ATOM    362  CG1 VAL A 143      95.255  89.010 -32.153  1.00  9.86           C  
-ATOM    363  CG2 VAL A 143      94.343  87.591 -30.286  1.00  8.19           C  
-ATOM    364  N   GLN A 144      92.870  91.430 -32.615  1.00  7.16           N  
-ATOM    365  CA  GLN A 144      92.589  92.272 -33.781  1.00  5.93           C  
-ATOM    366  C   GLN A 144      93.722  92.244 -34.795  1.00  9.26           C  
-ATOM    367  O   GLN A 144      94.901  92.182 -34.426  1.00  7.07           O  
-ATOM    368  CB  GLN A 144      92.373  93.732 -33.353  1.00  9.58           C  
-ATOM    369  CG  GLN A 144      91.242  93.909 -32.370  1.00  8.24           C  
-ATOM    370  CD  GLN A 144      91.143  95.323 -31.853  1.00 11.99           C  
-ATOM    371  OE1 GLN A 144      92.120  96.076 -31.858  1.00 12.64           O  
-ATOM    372  NE2 GLN A 144      89.963  95.683 -31.368  1.00 18.20           N  
-ATOM    373  N   LEU A 145      93.349  92.295 -36.072  1.00  7.37           N  
-ATOM    374  CA  LEU A 145      94.305  92.463 -37.173  1.00  8.57           C  
-ATOM    375  C   LEU A 145      94.114  93.845 -37.780  1.00  8.14           C  
-ATOM    376  O   LEU A 145      92.996  94.204 -38.172  1.00  9.08           O  
-ATOM    377  CB  LEU A 145      94.066  91.409 -38.257  1.00  7.67           C  
-ATOM    378  CG  LEU A 145      94.003  89.957 -37.775  1.00 10.26           C  
-ATOM    379  CD1 LEU A 145      93.688  89.013 -38.938  1.00 13.41           C  
-ATOM    380  CD2 LEU A 145      95.306  89.554 -37.100  1.00 12.43           C  
-ATOM    381  N   TRP A 146      95.206  94.602 -37.870  1.00  6.04           N  
-ATOM    382  CA  TRP A 146      95.185  95.951 -38.436  1.00  6.71           C  
-ATOM    383  C   TRP A 146      96.136  96.044 -39.603  1.00  9.33           C  
-ATOM    384  O   TRP A 146      97.245  95.518 -39.539  1.00  9.24           O  
-ATOM    385  CB  TRP A 146      95.630  96.968 -37.377  1.00  8.03           C  
-ATOM    386  CG  TRP A 146      94.655  97.165 -36.263  1.00  9.67           C  
-ATOM    387  CD1 TRP A 146      94.604  96.480 -35.082  1.00  8.37           C  
-ATOM    388  CD2 TRP A 146      93.585  98.114 -36.226  1.00 10.81           C  
-ATOM    389  NE1 TRP A 146      93.567  96.953 -34.304  1.00  9.93           N  
-ATOM    390  CE2 TRP A 146      92.927  97.955 -34.983  1.00 10.88           C  
-ATOM    391  CE3 TRP A 146      93.117  99.079 -37.121  1.00 11.29           C  
-ATOM    392  CZ2 TRP A 146      91.824  98.721 -34.618  1.00 10.32           C  
-ATOM    393  CZ3 TRP A 146      92.017  99.846 -36.755  1.00 11.93           C  
-ATOM    394  CH2 TRP A 146      91.393  99.670 -35.514  1.00 11.65           C  
-ATOM    395  N   VAL A 147      95.710  96.721 -40.671  1.00  9.32           N  
-ATOM    396  CA  VAL A 147      96.604  97.007 -41.791  1.00  7.71           C  
-ATOM    397  C   VAL A 147      96.356  98.411 -42.299  1.00 10.17           C  
-ATOM    398  O   VAL A 147      95.277  98.966 -42.079  1.00 12.93           O  
-ATOM    399  CB  VAL A 147      96.411  96.018 -42.983  1.00  8.26           C  
-ATOM    400  CG1 VAL A 147      96.874  94.621 -42.613  1.00 10.71           C  
-ATOM    401  CG2 VAL A 147      94.956  96.018 -43.473  1.00 10.02           C  
-ATOM    402  N   ASP A 148      97.347  98.983 -42.978  1.00 10.88           N  
-ATOM    403  CA  ASP A 148      97.189 100.311 -43.574  1.00 14.31           C  
-ATOM    404  C   ASP A 148      96.556 100.227 -44.947  1.00 14.69           C  
-ATOM    405  O   ASP A 148      95.862 101.153 -45.371  1.00 13.09           O  
-ATOM    406  CB  ASP A 148      98.533 101.026 -43.703  1.00 11.39           C  
-ATOM    407  CG  ASP A 148      99.148 101.368 -42.362  1.00 15.77           C  
-ATOM    408  OD1 ASP A 148      98.399 101.695 -41.412  1.00 14.84           O  
-ATOM    409  OD2 ASP A 148     100.389 101.314 -42.271  1.00 18.56           O  
-ATOM    410  N   SER A 149      96.815  99.125 -45.648  1.00 12.77           N  
-ATOM    411  CA  SER A 149      96.271  98.931 -46.988  1.00 16.32           C  
-ATOM    412  C   SER A 149      95.836  97.482 -47.194  1.00 13.50           C  
-ATOM    413  O   SER A 149      96.291  96.580 -46.480  1.00 11.97           O  
-ATOM    414  CB  SER A 149      97.284  99.353 -48.055  1.00 16.34           C  
-ATOM    415  OG  SER A 149      98.535  98.725 -47.853  1.00 22.69           O  
-ATOM    416  N   THR A 150      94.935  97.276 -48.150  1.00 12.44           N  
-ATOM    417  CA  THR A 150      94.321  95.968 -48.371  1.00 12.56           C  
-ATOM    418  C   THR A 150      95.289  94.992 -49.036  1.00 11.99           C  
-ATOM    419  O   THR A 150      95.830  95.273 -50.103  1.00 13.69           O  
-ATOM    420  CB  THR A 150      93.049  96.090 -49.240  1.00 18.17           C  
-ATOM    421  OG1 THR A 150      92.117  96.985 -48.612  1.00 17.35           O  
-ATOM    422  CG2 THR A 150      92.395  94.724 -49.433  1.00 18.17           C  
-ATOM    423  N   PRO A 151      95.511  93.834 -48.402  1.00 10.19           N  
-ATOM    424  CA  PRO A 151      96.398  92.820 -48.983  1.00 11.01           C  
-ATOM    425  C   PRO A 151      95.667  92.081 -50.096  1.00  9.72           C  
-ATOM    426  O   PRO A 151      94.439  92.147 -50.176  1.00 10.45           O  
-ATOM    427  CB  PRO A 151      96.669  91.852 -47.821  1.00 12.25           C  
-ATOM    428  CG  PRO A 151      96.009  92.426 -46.619  1.00 16.75           C  
-ATOM    429  CD  PRO A 151      95.010  93.458 -47.069  1.00 11.83           C  
-ATOM    430  N   PRO A 152      96.414  91.382 -50.960  1.00 10.15           N  
-ATOM    431  CA  PRO A 152      95.789  90.690 -52.094  1.00 11.27           C  
-ATOM    432  C   PRO A 152      94.827  89.561 -51.712  1.00 13.89           C  
-ATOM    433  O   PRO A 152      94.961  88.943 -50.649  1.00  9.39           O  
-ATOM    434  CB  PRO A 152      96.993  90.132 -52.866  1.00  9.76           C  
-ATOM    435  CG  PRO A 152      98.125  91.029 -52.497  1.00 11.22           C  
-ATOM    436  CD  PRO A 152      97.882  91.364 -51.039  1.00  9.26           C  
-ATOM    437  N   PRO A 153      93.854  89.271 -52.588  1.00 12.69           N  
-ATOM    438  CA  PRO A 153      93.017  88.092 -52.348  1.00 12.79           C  
-ATOM    439  C   PRO A 153      93.889  86.848 -52.192  1.00 11.81           C  
-ATOM    440  O   PRO A 153      94.846  86.672 -52.945  1.00 10.68           O  
-ATOM    441  CB  PRO A 153      92.179  87.982 -53.630  1.00 13.22           C  
-ATOM    442  CG  PRO A 153      92.153  89.391 -54.186  1.00 11.52           C  
-ATOM    443  CD  PRO A 153      93.505  89.970 -53.843  1.00 11.82           C  
-ATOM    444  N   GLY A 154      93.574  85.996 -51.225  1.00 10.66           N  
-ATOM    445  CA  GLY A 154      94.380  84.807 -51.007  1.00 12.33           C  
-ATOM    446  C   GLY A 154      95.378  84.971 -49.872  1.00 11.04           C  
-ATOM    447  O   GLY A 154      96.048  84.028 -49.483  1.00 11.39           O  
-ATOM    448  N   THR A 155      95.472  86.179 -49.325  1.00  7.57           N  
-ATOM    449  CA  THR A 155      96.329  86.400 -48.165  1.00  8.33           C  
-ATOM    450  C   THR A 155      95.758  85.633 -46.978  1.00 10.59           C  
-ATOM    451  O   THR A 155      94.535  85.512 -46.842  1.00 10.50           O  
-ATOM    452  CB  THR A 155      96.399  87.896 -47.843  1.00  9.77           C  
-ATOM    453  OG1 THR A 155      96.985  88.594 -48.955  1.00  9.58           O  
-ATOM    454  CG2 THR A 155      97.231  88.146 -46.589  1.00  8.76           C  
-ATOM    455  N   ARG A 156      96.638  85.101 -46.129  1.00  7.31           N  
-ATOM    456  CA  ARG A 156      96.205  84.318 -44.969  1.00  7.42           C  
-ATOM    457  C   ARG A 156      96.906  84.781 -43.694  1.00  7.59           C  
-ATOM    458  O   ARG A 156      97.903  85.512 -43.748  1.00  7.87           O  
-ATOM    459  CB  ARG A 156      96.448  82.823 -45.193  1.00  8.31           C  
-ATOM    460  CG  ARG A 156      95.738  82.279 -46.425  1.00 10.37           C  
-ATOM    461  CD  ARG A 156      95.402  80.784 -46.285  1.00 10.82           C  
-ATOM    462  NE  ARG A 156      96.588  79.934 -46.304  1.00 11.34           N  
-ATOM    463  CZ  ARG A 156      96.549  78.617 -46.106  1.00 10.90           C  
-ATOM    464  NH1 ARG A 156      95.389  78.026 -45.848  1.00 10.15           N  
-ATOM    465  NH2 ARG A 156      97.667  77.898 -46.146  1.00 12.96           N  
-ATOM    466  N   VAL A 157      96.372  84.345 -42.551  1.00  6.46           N  
-ATOM    467  CA  VAL A 157      96.879  84.734 -41.230  1.00  7.31           C  
-ATOM    468  C   VAL A 157      97.116  83.458 -40.421  1.00  7.13           C  
-ATOM    469  O   VAL A 157      96.178  82.701 -40.166  1.00  7.16           O  
-ATOM    470  CB  VAL A 157      95.854  85.617 -40.480  1.00  6.55           C  
-ATOM    471  CG1 VAL A 157      96.423  86.098 -39.143  1.00  6.96           C  
-ATOM    472  CG2 VAL A 157      95.452  86.826 -41.349  1.00  8.56           C  
-ATOM    473  N   ARG A 158      98.370  83.216 -40.056  1.00  6.96           N  
-ATOM    474  CA  ARG A 158      98.766  81.999 -39.336  1.00  7.11           C  
-ATOM    475  C   ARG A 158      99.155  82.294 -37.882  1.00  7.39           C  
-ATOM    476  O   ARG A 158      99.791  83.314 -37.583  1.00  8.14           O  
-ATOM    477  CB  ARG A 158      99.924  81.292 -40.066  1.00  7.78           C  
-ATOM    478  CG  ARG A 158     100.385  79.975 -39.423  1.00  8.91           C  
-ATOM    479  CD  ARG A 158     101.534  79.311 -40.204  1.00 11.06           C  
-ATOM    480  NE  ARG A 158     101.190  79.197 -41.624  1.00 10.46           N  
-ATOM    481  CZ  ARG A 158     100.480  78.209 -42.165  1.00 10.06           C  
-ATOM    482  NH1 ARG A 158     100.036  77.196 -41.425  1.00 10.73           N  
-ATOM    483  NH2 ARG A 158     100.209  78.237 -43.462  1.00 13.05           N  
-ATOM    484  N   ALA A 159      98.782  81.388 -36.975  1.00  6.83           N  
-ATOM    485  CA  ALA A 159      99.216  81.474 -35.573  1.00  5.78           C  
-ATOM    486  C   ALA A 159      99.998  80.219 -35.190  1.00  7.43           C  
-ATOM    487  O   ALA A 159      99.617  79.115 -35.567  1.00  7.56           O  
-ATOM    488  CB  ALA A 159      98.007  81.648 -34.640  1.00  8.13           C  
-ATOM    489  N   MET A 160     101.107  80.413 -34.479  1.00  7.43           N  
-ATOM    490  CA  MET A 160     101.982  79.324 -34.031  1.00  8.34           C  
-ATOM    491  C   MET A 160     102.538  79.688 -32.656  1.00  8.13           C  
-ATOM    492  O   MET A 160     102.847  80.847 -32.400  1.00  8.85           O  
-ATOM    493  CB  MET A 160     103.140  79.158 -35.033  1.00  9.31           C  
-ATOM    494  CG  MET A 160     104.116  78.027 -34.713  1.00 14.32           C  
-ATOM    495  SD  MET A 160     105.536  78.022 -35.851  1.00 14.71           S  
-ATOM    496  CE  MET A 160     104.838  77.312 -37.358  1.00 15.95           C  
-ATOM    497  N   ALA A 161     102.668  78.706 -31.763  1.00  7.94           N  
-ATOM    498  CA  ALA A 161     103.300  78.948 -30.470  1.00  9.23           C  
-ATOM    499  C   ALA A 161     104.736  78.418 -30.465  1.00 10.26           C  
-ATOM    500  O   ALA A 161     105.013  77.383 -31.057  1.00 10.42           O  
-ATOM    501  CB  ALA A 161     102.502  78.283 -29.348  1.00  9.29           C  
-ATOM    502  N   ILE A 162     105.641  79.140 -29.807  1.00  8.83           N  
-ATOM    503  CA  ILE A 162     106.981  78.614 -29.525  1.00 10.26           C  
-ATOM    504  C   ILE A 162     107.341  78.875 -28.067  1.00 11.65           C  
-ATOM    505  O   ILE A 162     106.777  79.763 -27.431  1.00 10.13           O  
-ATOM    506  CB  ILE A 162     108.064  79.252 -30.431  1.00 12.48           C  
-ATOM    507  CG1 ILE A 162     108.175  80.755 -30.171  1.00 12.07           C  
-ATOM    508  CG2 ILE A 162     107.777  78.960 -31.897  1.00 13.75           C  
-ATOM    509  CD1 ILE A 162     109.452  81.372 -30.757  1.00 14.50           C  
-ATOM    510  N   TYR A 163     108.277  78.103 -27.519  1.00 11.34           N  
-ATOM    511  CA  TYR A 163     108.766  78.425 -26.186  1.00 11.19           C  
-ATOM    512  C   TYR A 163     109.605  79.700 -26.235  1.00 10.33           C  
-ATOM    513  O   TYR A 163     110.357  79.919 -27.179  1.00 12.78           O  
-ATOM    514  CB  TYR A 163     109.527  77.244 -25.552  1.00 13.26           C  
-ATOM    515  CG  TYR A 163     108.571  76.143 -25.151  1.00 10.20           C  
-ATOM    516  CD1 TYR A 163     107.659  76.343 -24.123  1.00 14.79           C  
-ATOM    517  CD2 TYR A 163     108.538  74.936 -25.837  1.00 13.11           C  
-ATOM    518  CE1 TYR A 163     106.757  75.366 -23.768  1.00 12.39           C  
-ATOM    519  CE2 TYR A 163     107.638  73.953 -25.490  1.00 13.82           C  
-ATOM    520  CZ  TYR A 163     106.748  74.180 -24.454  1.00 12.32           C  
-ATOM    521  OH  TYR A 163     105.844  73.209 -24.109  1.00 15.84           O  
-ATOM    522  N   LYS A 164     109.456  80.534 -25.212  1.00 10.79           N  
-ATOM    523  CA  LYS A 164     110.115  81.837 -25.166  1.00 12.79           C  
-ATOM    524  C   LYS A 164     111.593  81.730 -24.785  1.00 16.03           C  
-ATOM    525  O   LYS A 164     112.427  82.511 -25.261  1.00 16.21           O  
-ATOM    526  CB  LYS A 164     109.395  82.746 -24.169  1.00 13.26           C  
-ATOM    527  CG  LYS A 164     109.995  84.133 -24.059  1.00 17.00           C  
-ATOM    528  CD  LYS A 164     109.364  84.914 -22.919  1.00 25.36           C  
-ATOM    529  CE  LYS A 164     110.089  86.232 -22.703  1.00 31.57           C  
-ATOM    530  NZ  LYS A 164     109.533  86.962 -21.531  1.00 32.96           N  
-ATOM    531  N   GLN A 165     111.913  80.762 -23.931  1.00 17.77           N  
-ATOM    532  CA  GLN A 165     113.286  80.576 -23.450  1.00 18.79           C  
-ATOM    533  C   GLN A 165     114.121  79.827 -24.482  1.00 15.24           C  
-ATOM    534  O   GLN A 165     113.706  78.786 -24.982  1.00 17.07           O  
-ATOM    535  CB  GLN A 165     113.280  79.809 -22.124  1.00 15.56           C  
-ATOM    536  CG  GLN A 165     112.625  80.554 -20.970  1.00 19.77           C  
-ATOM    537  CD  GLN A 165     112.199  79.627 -19.839  1.00 25.23           C  
-ATOM    538  OE1 GLN A 165     111.424  78.690 -20.042  1.00 20.03           O  
-ATOM    539  NE2 GLN A 165     112.704  79.891 -18.639  1.00 34.84           N  
-ATOM    540  N   SER A 166     115.313  80.343 -24.775  1.00 18.95           N  
-ATOM    541  C   SER A 166     116.444  78.304 -25.670  1.00 14.19           C  
-ATOM    542  O   SER A 166     116.519  77.569 -26.657  1.00 19.10           O  
-ATOM    543  CA ASER A 166     116.144  79.791 -25.841  0.41 20.53           C  
-ATOM    544  CB ASER A 166     117.447  80.584 -25.984  0.41 22.84           C  
-ATOM    545  OG ASER A 166     117.201  81.872 -26.526  0.41 22.38           O  
-ATOM    546  CA BSER A 166     116.159  79.794 -25.832  0.59 20.52           C  
-ATOM    547  CB BSER A 166     117.475  80.571 -25.915  0.59 22.86           C  
-ATOM    548  OG BSER A 166     118.013  80.791 -24.623  0.59 24.36           O  
-ATOM    549  N   GLN A 167     116.608  77.863 -24.429  1.00 18.35           N  
-ATOM    550  CA  GLN A 167     116.933  76.462 -24.181  1.00 22.21           C  
-ATOM    551  C   GLN A 167     115.769  75.509 -24.453  1.00 23.43           C  
-ATOM    552  O   GLN A 167     115.956  74.292 -24.459  1.00 20.67           O  
-ATOM    553  CB  GLN A 167     117.481  76.251 -22.763  1.00 25.82           C  
-ATOM    554  CG  GLN A 167     116.486  76.521 -21.648  1.00 22.58           C  
-ATOM    555  CD  GLN A 167     116.505  77.962 -21.179  1.00 27.15           C  
-ATOM    556  OE1 GLN A 167     116.612  78.893 -21.979  1.00 27.81           O  
-ATOM    557  NE2 GLN A 167     116.399  78.153 -19.869  1.00 31.50           N  
-ATOM    558  N   HIS A 168     114.580  76.061 -24.695  1.00 14.58           N  
-ATOM    559  CA  HIS A 168     113.409  75.246 -25.010  1.00 17.44           C  
-ATOM    560  C   HIS A 168     112.852  75.523 -26.412  1.00 15.78           C  
-ATOM    561  O   HIS A 168     111.894  74.884 -26.841  1.00 19.19           O  
-ATOM    562  CB  HIS A 168     112.308  75.458 -23.960  1.00 16.63           C  
-ATOM    563  CG  HIS A 168     112.723  75.105 -22.566  1.00 19.50           C  
-ATOM    564  ND1 HIS A 168     113.087  73.827 -22.197  1.00 20.73           N  
-ATOM    565  CD2 HIS A 168     112.830  75.863 -21.449  1.00 16.17           C  
-ATOM    566  CE1 HIS A 168     113.405  73.815 -20.915  1.00 17.50           C  
-ATOM    567  NE2 HIS A 168     113.255  75.036 -20.437  1.00 20.07           N  
-ATOM    568  N   MET A 169     113.473  76.447 -27.137  1.00 17.09           N  
-ATOM    569  CA  MET A 169     112.918  76.920 -28.403  1.00 16.34           C  
-ATOM    570  C   MET A 169     112.756  75.864 -29.475  1.00 19.75           C  
-ATOM    571  O   MET A 169     111.860  75.970 -30.319  1.00 19.30           O  
-ATOM    572  CB  MET A 169     113.765  78.046 -28.974  1.00 20.09           C  
-ATOM    573  CG  MET A 169     113.534  79.354 -28.309  1.00 24.45           C  
-ATOM    574  SD  MET A 169     113.828  80.693 -29.475  1.00 42.52           S  
-ATOM    575  CE  MET A 169     113.508  82.075 -28.384  1.00 25.38           C  
-ATOM    576  N   THR A 170     113.630  74.862 -29.477  1.00 15.75           N  
-ATOM    577  CA  THR A 170     113.546  73.832 -30.505  1.00 19.55           C  
-ATOM    578  C   THR A 170     112.482  72.795 -30.192  1.00 17.21           C  
-ATOM    579  O   THR A 170     112.197  71.933 -31.028  1.00 21.81           O  
-ATOM    580  CB  THR A 170     114.893  73.113 -30.742  1.00 22.97           C  
-ATOM    581  OG1 THR A 170     115.295  72.439 -29.545  1.00 24.09           O  
-ATOM    582  CG2 THR A 170     115.968  74.108 -31.158  1.00 26.49           C  
-ATOM    583  N   GLU A 171     111.892  72.870 -29.000  1.00 18.54           N  
-ATOM    584  CA  GLU A 171     110.854  71.914 -28.625  1.00 15.44           C  
-ATOM    585  C   GLU A 171     109.480  72.346 -29.150  1.00 14.77           C  
-ATOM    586  O   GLU A 171     109.066  73.486 -28.947  1.00 14.85           O  
-ATOM    587  CB  GLU A 171     110.809  71.706 -27.103  1.00 18.67           C  
-ATOM    588  CG  GLU A 171     109.788  70.652 -26.682  1.00 21.27           C  
-ATOM    589  CD  GLU A 171     109.778  70.369 -25.189  1.00 26.09           C  
-ATOM    590  OE1 GLU A 171     110.820  70.569 -24.522  1.00 25.80           O  
-ATOM    591  OE2 GLU A 171     108.723  69.929 -24.685  1.00 23.93           O  
-ATOM    592  N   VAL A 172     108.789  71.443 -29.842  1.00 13.96           N  
-ATOM    593  CA  VAL A 172     107.442  71.728 -30.326  1.00 11.30           C  
-ATOM    594  C   VAL A 172     106.506  71.989 -29.140  1.00 12.60           C  
-ATOM    595  O   VAL A 172     106.444  71.185 -28.195  1.00 12.96           O  
-ATOM    596  CB  VAL A 172     106.888  70.560 -31.175  1.00 14.95           C  
-ATOM    597  CG1 VAL A 172     105.410  70.776 -31.504  1.00 12.03           C  
-ATOM    598  CG2 VAL A 172     107.708  70.388 -32.452  1.00 13.88           C  
-ATOM    599  N   VAL A 173     105.808  73.124 -29.171  1.00  9.84           N  
-ATOM    600  CA  VAL A 173     104.758  73.408 -28.192  1.00  8.99           C  
-ATOM    601  C   VAL A 173     103.515  72.610 -28.562  1.00  9.45           C  
-ATOM    602  O   VAL A 173     102.977  72.757 -29.665  1.00 10.26           O  
-ATOM    603  CB  VAL A 173     104.373  74.908 -28.169  1.00 12.70           C  
-ATOM    604  CG1 VAL A 173     103.246  75.148 -27.147  1.00  9.98           C  
-ATOM    605  CG2 VAL A 173     105.579  75.764 -27.837  1.00 10.18           C  
-ATOM    606  N   ARG A 174     103.055  71.767 -27.639  1.00  9.27           N  
-ATOM    607  CA  ARG A 174     101.897  70.916 -27.883  1.00  9.62           C  
-ATOM    608  C   ARG A 174     101.085  70.754 -26.597  1.00  8.50           C  
-ATOM    609  O   ARG A 174     101.546  71.114 -25.507  1.00 11.91           O  
-ATOM    610  CB  ARG A 174     102.358  69.531 -28.363  1.00 11.39           C  
-ATOM    611  CG  ARG A 174     103.235  68.807 -27.323  1.00  9.49           C  
-ATOM    612  CD  ARG A 174     103.496  67.348 -27.713  1.00 15.01           C  
-ATOM    613  NE  ARG A 174     104.176  67.222 -29.007  1.00 14.15           N  
-ATOM    614  CZ  ARG A 174     103.571  66.911 -30.154  1.00 14.10           C  
-ATOM    615  NH1 ARG A 174     102.259  66.697 -30.189  1.00 11.50           N  
-ATOM    616  NH2 ARG A 174     104.281  66.814 -31.277  1.00 14.73           N  
-ATOM    617  N   ARG A 175      99.877  70.209 -26.722  1.00  9.59           N  
-ATOM    618  CA  ARG A 175      99.073  69.921 -25.543  1.00  9.33           C  
-ATOM    619  C   ARG A 175      99.679  68.781 -24.730  1.00  8.48           C  
-ATOM    620  O   ARG A 175     100.356  67.895 -25.278  1.00  9.91           O  
-ATOM    621  CB  ARG A 175      97.624  69.598 -25.929  1.00 10.53           C  
-ATOM    622  CG  ARG A 175      96.867  70.779 -26.557  1.00  9.51           C  
-ATOM    623  CD  ARG A 175      95.442  70.353 -26.870  1.00 11.26           C  
-ATOM    624  NE  ARG A 175      94.534  70.535 -25.746  1.00 11.82           N  
-ATOM    625  CZ  ARG A 175      93.296  70.050 -25.714  1.00  9.36           C  
-ATOM    626  NH1 ARG A 175      92.852  69.293 -26.713  1.00 12.60           N  
-ATOM    627  NH2 ARG A 175      92.515  70.304 -24.680  1.00 12.83           N  
-ATOM    628  N   CYS A 176      99.413  68.816 -23.428  1.00  9.02           N  
-ATOM    629  CA  CYS A 176      99.954  67.846 -22.477  1.00  9.09           C  
-ATOM    630  C   CYS A 176      99.328  66.465 -22.655  1.00 11.47           C  
-ATOM    631  O   CYS A 176      98.347  66.297 -23.379  1.00  9.30           O  
-ATOM    632  CB  CYS A 176      99.772  68.351 -21.031  1.00  9.39           C  
-ATOM    633  SG  CYS A 176      98.086  68.227 -20.395  1.00 10.24           S  
-ATOM    634  N   PRO A 177      99.903  65.450 -21.991  1.00 10.89           N  
-ATOM    635  CA  PRO A 177      99.418  64.082 -22.211  1.00 13.66           C  
-ATOM    636  C   PRO A 177      97.976  63.883 -21.746  1.00 10.10           C  
-ATOM    637  O   PRO A 177      97.304  62.962 -22.225  1.00 11.91           O  
-ATOM    638  CB  PRO A 177     100.368  63.232 -21.351  1.00 11.28           C  
-ATOM    639  CG  PRO A 177     101.588  64.073 -21.186  1.00 15.58           C  
-ATOM    640  CD  PRO A 177     101.117  65.490 -21.160  1.00 12.98           C  
-ATOM    641  N   HIS A 178      97.519  64.709 -20.804  1.00  9.34           N  
-ATOM    642  CA  HIS A 178      96.129  64.668 -20.380  1.00  9.98           C  
-ATOM    643  C   HIS A 178      95.213  65.339 -21.392  1.00 11.63           C  
-ATOM    644  O   HIS A 178      94.246  64.736 -21.866  1.00 11.92           O  
-ATOM    645  CB  HIS A 178      95.932  65.347 -19.021  1.00 12.95           C  
-ATOM    646  CG  HIS A 178      94.497  65.642 -18.717  1.00 13.02           C  
-ATOM    647  ND1 HIS A 178      93.557  64.650 -18.549  1.00 16.06           N  
-ATOM    648  CD2 HIS A 178      93.834  66.816 -18.586  1.00 14.52           C  
-ATOM    649  CE1 HIS A 178      92.377  65.199 -18.318  1.00 19.68           C  
-ATOM    650  NE2 HIS A 178      92.518  66.513 -18.339  1.00 17.55           N  
-ATOM    651  N   HIS A 179      95.503  66.595 -21.719  1.00 11.42           N  
-ATOM    652  CA  HIS A 179      94.579  67.346 -22.570  1.00  9.90           C  
-ATOM    653  C   HIS A 179      94.498  66.828 -24.016  1.00 10.28           C  
-ATOM    654  O   HIS A 179      93.449  66.941 -24.660  1.00 12.69           O  
-ATOM    655  CB  HIS A 179      94.858  68.847 -22.512  1.00 11.17           C  
-ATOM    656  CG  HIS A 179      94.326  69.499 -21.274  1.00  9.89           C  
-ATOM    657  ND1 HIS A 179      95.142  70.064 -20.319  1.00 11.23           N  
-ATOM    658  CD2 HIS A 179      93.057  69.650 -20.821  1.00 11.68           C  
-ATOM    659  CE1 HIS A 179      94.402  70.552 -19.337  1.00 11.11           C  
-ATOM    660  NE2 HIS A 179      93.133  70.312 -19.615  1.00 10.98           N  
-ATOM    661  N   GLU A 180      95.578  66.250 -24.534  1.00  8.03           N  
-ATOM    662  CA  GLU A 180      95.493  65.707 -25.888  1.00  8.54           C  
-ATOM    663  C   GLU A 180      94.541  64.510 -25.971  1.00 10.54           C  
-ATOM    664  O   GLU A 180      94.167  64.091 -27.062  1.00 12.72           O  
-ATOM    665  CB  GLU A 180      96.880  65.350 -26.457  1.00 11.44           C  
-ATOM    666  CG  GLU A 180      97.481  64.066 -25.896  1.00  9.45           C  
-ATOM    667  CD  GLU A 180      98.740  63.620 -26.643  1.00 13.53           C  
-ATOM    668  OE1 GLU A 180      99.177  64.326 -27.572  1.00 11.53           O  
-ATOM    669  OE2 GLU A 180      99.295  62.545 -26.314  1.00 16.08           O  
-ATOM    670  N   ARG A 181      94.150  63.963 -24.819  1.00 10.96           N  
-ATOM    671  CA  ARG A 181      93.284  62.784 -24.784  1.00 14.37           C  
-ATOM    672  C   ARG A 181      91.901  63.031 -24.160  1.00 19.27           C  
-ATOM    673  O   ARG A 181      91.203  62.076 -23.816  1.00 17.35           O  
-ATOM    674  CB  ARG A 181      93.959  61.651 -23.990  1.00 11.63           C  
-ATOM    675  CG  ARG A 181      95.274  61.155 -24.567  1.00 10.76           C  
-ATOM    676  CD  ARG A 181      95.848  59.987 -23.733  1.00  8.79           C  
-ATOM    677  NE  ARG A 181      95.003  58.791 -23.715  1.00  9.70           N  
-ATOM    678  CZ  ARG A 181      94.440  58.275 -22.621  1.00 10.49           C  
-ATOM    679  NH1 ARG A 181      94.590  58.863 -21.430  1.00  9.16           N  
-ATOM    680  NH2 ARG A 181      93.710  57.174 -22.719  1.00 12.53           N  
-ATOM    681  N  ACYS A 182      91.502  64.285 -23.985  0.57 16.66           N  
-ATOM    682  CA ACYS A 182      90.245  64.524 -23.278  0.57 21.47           C  
-ATOM    683  C  ACYS A 182      89.025  64.661 -24.203  0.57 25.06           C  
-ATOM    684  O  ACYS A 182      87.938  65.024 -23.753  0.57 26.18           O  
-ATOM    685  CB ACYS A 182      90.361  65.708 -22.310  0.57 20.90           C  
-ATOM    686  SG ACYS A 182      90.513  67.305 -23.102  0.57 18.60           S  
-ATOM    687  N  BCYS A 182      91.520  64.302 -24.031  0.43 16.69           N  
-ATOM    688  CA BCYS A 182      90.283  64.684 -23.344  0.43 21.57           C  
-ATOM    689  C  BCYS A 182      89.024  64.561 -24.190  0.43 25.07           C  
-ATOM    690  O  BCYS A 182      87.909  64.669 -23.680  0.43 26.27           O  
-ATOM    691  CB BCYS A 182      90.384  66.120 -22.835  0.43 20.33           C  
-ATOM    692  SG BCYS A 182      91.152  66.254 -21.237  0.43 19.89           S  
-ATOM    693  N   SER A 183      89.206  64.356 -25.484  1.00 26.28           N  
-ATOM    694  CA  SER A 183      88.076  64.272 -26.411  1.00 33.08           C  
-ATOM    695  C   SER A 183      87.236  65.555 -26.434  1.00 35.35           C  
-ATOM    696  O   SER A 183      86.005  65.504 -26.459  1.00 38.93           O  
-ATOM    697  CB  SER A 183      87.185  63.069 -26.065  1.00 36.47           C  
-ATOM    698  OG  SER A 183      87.931  61.863 -26.034  1.00 41.73           O  
-ATOM    699  N   ASP A 184      87.905  66.702 -26.432  1.00 25.49           N  
-ATOM    700  CA  ASP A 184      87.210  67.981 -26.473  1.00 24.63           C  
-ATOM    701  C   ASP A 184      87.300  68.589 -27.868  1.00 25.38           C  
-ATOM    702  O   ASP A 184      87.262  69.802 -28.031  1.00 23.65           O  
-ATOM    703  CB  ASP A 184      87.785  68.934 -25.422  1.00 21.12           C  
-ATOM    704  CG  ASP A 184      89.274  69.175 -25.601  1.00 18.67           C  
-ATOM    705  OD1 ASP A 184      89.844  68.740 -26.622  1.00 15.99           O  
-ATOM    706  OD2 ASP A 184      89.873  69.811 -24.716  1.00 17.68           O  
-ATOM    707  N   SER A 185      87.411  67.722 -28.868  1.00 25.26           N  
-ATOM    708  CA  SER A 185      87.512  68.134 -30.263  1.00 28.41           C  
-ATOM    709  C   SER A 185      86.357  69.025 -30.714  1.00 32.37           C  
-ATOM    710  O   SER A 185      85.224  68.877 -30.255  1.00 32.37           O  
-ATOM    711  CB  SER A 185      87.577  66.900 -31.162  1.00 38.21           C  
-ATOM    712  OG  SER A 185      87.053  67.180 -32.448  1.00 38.36           O  
-ATOM    713  N   ASP A 186      86.655  69.953 -31.618  1.00 29.58           N  
-ATOM    714  CA  ASP A 186      85.618  70.772 -32.227  1.00 30.35           C  
-ATOM    715  C   ASP A 186      85.321  70.248 -33.628  1.00 30.48           C  
-ATOM    716  O   ASP A 186      84.577  70.858 -34.394  1.00 34.57           O  
-ATOM    717  CB  ASP A 186      86.047  72.238 -32.278  1.00 28.11           C  
-ATOM    718  CG  ASP A 186      87.299  72.452 -33.107  1.00 26.40           C  
-ATOM    719  OD1 ASP A 186      87.829  71.472 -33.672  1.00 23.43           O  
-ATOM    720  OD2 ASP A 186      87.751  73.611 -33.193  1.00 30.43           O  
-ATOM    721  N   GLY A 187      85.921  69.112 -33.959  1.00 29.90           N  
-ATOM    722  CA  GLY A 187      85.693  68.477 -35.242  1.00 33.18           C  
-ATOM    723  C   GLY A 187      86.665  68.891 -36.330  1.00 32.80           C  
-ATOM    724  O   GLY A 187      86.645  68.329 -37.420  1.00 34.12           O  
-ATOM    725  N   LEU A 188      87.514  69.873 -36.041  1.00 26.30           N  
-ATOM    726  CA  LEU A 188      88.460  70.382 -37.034  1.00 19.92           C  
-ATOM    727  C   LEU A 188      89.897  70.420 -36.503  1.00 17.91           C  
-ATOM    728  O   LEU A 188      90.836  69.984 -37.171  1.00 17.48           O  
-ATOM    729  CB  LEU A 188      88.034  71.778 -37.505  1.00 26.97           C  
-ATOM    730  CG  LEU A 188      88.689  72.323 -38.774  1.00 33.03           C  
-ATOM    731  CD1 LEU A 188      88.663  71.291 -39.902  1.00 28.51           C  
-ATOM    732  CD2 LEU A 188      88.013  73.626 -39.213  1.00 28.74           C  
-ATOM    733  N   ALA A 189      90.066  70.940 -35.295  1.00 14.47           N  
-ATOM    734  CA  ALA A 189      91.393  71.008 -34.692  1.00  8.88           C  
-ATOM    735  C   ALA A 189      91.863  69.623 -34.240  1.00 10.86           C  
-ATOM    736  O   ALA A 189      91.137  68.919 -33.543  1.00 11.82           O  
-ATOM    737  CB  ALA A 189      91.372  71.960 -33.498  1.00 10.01           C  
-ATOM    738  N   PRO A 190      93.084  69.232 -34.632  1.00  9.27           N  
-ATOM    739  CA  PRO A 190      93.635  68.000 -34.052  1.00 10.21           C  
-ATOM    740  C   PRO A 190      93.732  68.151 -32.542  1.00 11.44           C  
-ATOM    741  O   PRO A 190      94.005  69.252 -32.042  1.00 10.24           O  
-ATOM    742  CB  PRO A 190      95.039  67.920 -34.659  1.00 11.74           C  
-ATOM    743  CG  PRO A 190      94.978  68.805 -35.904  1.00 13.61           C  
-ATOM    744  CD  PRO A 190      94.057  69.924 -35.494  1.00 11.02           C  
-ATOM    745  N   PRO A 191      93.513  67.057 -31.804  1.00 11.37           N  
-ATOM    746  CA  PRO A 191      93.528  67.105 -30.339  1.00 12.48           C  
-ATOM    747  C   PRO A 191      94.874  67.527 -29.738  1.00  8.77           C  
-ATOM    748  O   PRO A 191      94.884  67.968 -28.589  1.00  9.82           O  
-ATOM    749  CB  PRO A 191      93.205  65.664 -29.926  1.00 11.65           C  
-ATOM    750  CG  PRO A 191      93.356  64.841 -31.142  1.00 13.03           C  
-ATOM    751  CD  PRO A 191      93.114  65.736 -32.322  1.00 11.24           C  
-ATOM    752  N   GLN A 192      95.965  67.400 -30.490  1.00  9.62           N  
-ATOM    753  CA  GLN A 192      97.296  67.796 -30.005  1.00  7.92           C  
-ATOM    754  C   GLN A 192      97.569  69.310 -30.032  1.00  9.64           C  
-ATOM    755  O   GLN A 192      98.470  69.801 -29.344  1.00  9.96           O  
-ATOM    756  CB  GLN A 192      98.398  67.105 -30.817  1.00 12.11           C  
-ATOM    757  CG  GLN A 192      98.323  65.575 -30.853  1.00 11.93           C  
-ATOM    758  CD  GLN A 192      97.618  65.055 -32.106  1.00 12.80           C  
-ATOM    759  OE1 GLN A 192      96.610  65.611 -32.542  1.00 13.71           O  
-ATOM    760  NE2 GLN A 192      98.144  63.972 -32.682  1.00 10.82           N  
-ATOM    761  N   HIS A 193      96.814  70.046 -30.839  1.00  8.94           N  
-ATOM    762  CA  HIS A 193      97.127  71.463 -31.076  1.00  6.78           C  
-ATOM    763  C   HIS A 193      96.742  72.368 -29.914  1.00  6.41           C  
-ATOM    764  O   HIS A 193      95.596  72.348 -29.469  1.00  8.66           O  
-ATOM    765  CB  HIS A 193      96.396  71.948 -32.334  1.00  6.37           C  
-ATOM    766  CG  HIS A 193      97.066  71.560 -33.615  1.00  9.02           C  
-ATOM    767  ND1 HIS A 193      97.227  72.443 -34.660  1.00  7.72           N  
-ATOM    768  CD2 HIS A 193      97.639  70.398 -34.013  1.00 11.18           C  
-ATOM    769  CE1 HIS A 193      97.855  71.840 -35.655  1.00  8.80           C  
-ATOM    770  NE2 HIS A 193      98.116  70.595 -35.289  1.00 10.16           N  
-ATOM    771  N   LEU A 194      97.684  73.188 -29.449  1.00  5.63           N  
-ATOM    772  CA  LEU A 194      97.409  74.148 -28.367  1.00  6.26           C  
-ATOM    773  C   LEU A 194      96.459  75.263 -28.790  1.00  9.43           C  
-ATOM    774  O   LEU A 194      95.537  75.621 -28.049  1.00  8.35           O  
-ATOM    775  CB  LEU A 194      98.714  74.789 -27.891  1.00  6.76           C  
-ATOM    776  CG  LEU A 194      98.581  75.843 -26.782  1.00  6.17           C  
-ATOM    777  CD1 LEU A 194      98.121  75.194 -25.491  1.00  9.07           C  
-ATOM    778  CD2 LEU A 194      99.888  76.610 -26.552  1.00  9.25           C  
-ATOM    779  N   ILE A 195      96.710  75.833 -29.969  1.00  7.60           N  
-ATOM    780  CA  ILE A 195      95.947  76.985 -30.430  1.00  6.91           C  
-ATOM    781  C   ILE A 195      94.873  76.584 -31.426  1.00  6.96           C  
-ATOM    782  O   ILE A 195      95.162  75.935 -32.423  1.00  7.59           O  
-ATOM    783  CB  ILE A 195      96.854  78.026 -31.104  1.00  8.00           C  
-ATOM    784  CG1 ILE A 195      98.036  78.392 -30.200  1.00  8.02           C  
-ATOM    785  CG2 ILE A 195      96.043  79.282 -31.487  1.00  6.95           C  
-ATOM    786  CD1 ILE A 195      98.969  79.455 -30.837  1.00  8.66           C  
-ATOM    787  N   ARG A 196      93.635  76.964 -31.134  1.00  8.74           N  
-ATOM    788  CA  ARG A 196      92.526  76.800 -32.057  1.00  7.94           C  
-ATOM    789  C   ARG A 196      91.973  78.160 -32.472  1.00  8.87           C  
-ATOM    790  O   ARG A 196      92.094  79.159 -31.742  1.00  9.54           O  
-ATOM    791  CB  ARG A 196      91.386  76.026 -31.401  1.00  7.78           C  
-ATOM    792  CG  ARG A 196      91.732  74.601 -31.004  1.00  8.13           C  
-ATOM    793  CD  ARG A 196      90.507  73.902 -30.434  1.00 10.17           C  
-ATOM    794  NE  ARG A 196      90.857  72.575 -29.940  1.00  9.31           N  
-ATOM    795  CZ  ARG A 196      90.039  71.776 -29.269  1.00 15.80           C  
-ATOM    796  NH1 ARG A 196      88.804  72.167 -28.967  1.00 16.47           N  
-ATOM    797  NH2 ARG A 196      90.475  70.586 -28.887  1.00 15.40           N  
-ATOM    798  N   VAL A 197      91.354  78.190 -33.646  1.00 11.06           N  
-ATOM    799  CA  VAL A 197      90.528  79.324 -34.037  1.00  8.53           C  
-ATOM    800  C   VAL A 197      89.064  78.947 -33.861  1.00 12.18           C  
-ATOM    801  O   VAL A 197      88.619  77.898 -34.330  1.00 15.11           O  
-ATOM    802  CB  VAL A 197      90.789  79.755 -35.492  1.00  9.03           C  
-ATOM    803  CG1 VAL A 197      89.734  80.772 -35.950  1.00 12.05           C  
-ATOM    804  CG2 VAL A 197      92.173  80.358 -35.625  1.00  9.79           C  
-ATOM    805  N   GLU A 198      88.326  79.817 -33.179  1.00 11.27           N  
-ATOM    806  CA  GLU A 198      86.909  79.631 -32.890  1.00 11.45           C  
-ATOM    807  C   GLU A 198      86.017  80.166 -34.003  1.00 14.50           C  
-ATOM    808  O   GLU A 198      86.214  81.277 -34.469  1.00 14.27           O  
-ATOM    809  CB  GLU A 198      86.565  80.423 -31.625  1.00 17.08           C  
-ATOM    810  CG  GLU A 198      86.146  79.601 -30.477  1.00 22.68           C  
-ATOM    811  CD  GLU A 198      85.621  80.441 -29.341  1.00 14.57           C  
-ATOM    812  OE1 GLU A 198      86.325  81.371 -28.897  1.00 15.17           O  
-ATOM    813  OE2 GLU A 198      84.506  80.145 -28.879  1.00 19.25           O  
-ATOM    814  N   GLY A 199      85.025  79.379 -34.404  1.00 15.86           N  
-ATOM    815  CA  GLY A 199      83.957  79.860 -35.260  1.00 20.26           C  
-ATOM    816  C   GLY A 199      84.372  80.319 -36.645  1.00 22.19           C  
-ATOM    817  O   GLY A 199      83.848  81.309 -37.161  1.00 22.41           O  
-ATOM    818  N   ASN A 200      85.323  79.611 -37.242  1.00 19.38           N  
-ATOM    819  CA  ASN A 200      85.727  79.894 -38.614  1.00 18.45           C  
-ATOM    820  C   ASN A 200      85.890  78.585 -39.369  1.00 18.65           C  
-ATOM    821  O   ASN A 200      86.850  77.846 -39.157  1.00 16.37           O  
-ATOM    822  CB  ASN A 200      87.022  80.712 -38.655  1.00 17.15           C  
-ATOM    823  CG  ASN A 200      87.345  81.218 -40.056  1.00 18.97           C  
-ATOM    824  OD1 ASN A 200      86.966  80.601 -41.053  1.00 20.95           O  
-ATOM    825  ND2 ASN A 200      88.039  82.348 -40.135  1.00 15.34           N  
-ATOM    826  N   LEU A 201      84.929  78.291 -40.238  1.00 15.95           N  
-ATOM    827  CA  LEU A 201      84.900  77.012 -40.944  1.00 22.35           C  
-ATOM    828  C   LEU A 201      86.020  76.879 -41.977  1.00 23.32           C  
-ATOM    829  O   LEU A 201      86.290  75.785 -42.478  1.00 22.53           O  
-ATOM    830  CB  LEU A 201      83.529  76.805 -41.601  1.00 25.65           C  
-ATOM    831  CG  LEU A 201      82.399  76.580 -40.590  1.00 31.99           C  
-ATOM    832  CD1 LEU A 201      81.030  76.543 -41.264  1.00 34.78           C  
-ATOM    833  CD2 LEU A 201      82.649  75.308 -39.785  1.00 36.25           C  
-ATOM    834  N   ARG A 202      86.672  77.993 -42.288  1.00 17.02           N  
-ATOM    835  CA  ARG A 202      87.778  77.988 -43.233  1.00 16.47           C  
-ATOM    836  C   ARG A 202      89.148  77.862 -42.566  1.00 13.76           C  
-ATOM    837  O   ARG A 202      90.180  77.914 -43.239  1.00 14.04           O  
-ATOM    838  CB  ARG A 202      87.714  79.224 -44.133  1.00 20.00           C  
-ATOM    839  CG  ARG A 202      86.519  79.187 -45.088  1.00 27.34           C  
-ATOM    840  CD  ARG A 202      86.717  80.104 -46.283  1.00 33.10           C  
-ATOM    841  NE  ARG A 202      86.671  81.514 -45.914  1.00 38.75           N  
-ATOM    842  CZ  ARG A 202      87.046  82.507 -46.718  1.00 43.80           C  
-ATOM    843  NH1 ARG A 202      87.505  82.240 -47.936  1.00 42.05           N  
-ATOM    844  NH2 ARG A 202      86.970  83.765 -46.301  1.00 41.51           N  
-ATOM    845  N   ALA A 203      89.156  77.675 -41.247  1.00 14.47           N  
-ATOM    846  CA  ALA A 203      90.401  77.434 -40.537  1.00 11.06           C  
-ATOM    847  C   ALA A 203      91.042  76.119 -40.987  1.00 15.91           C  
-ATOM    848  O   ALA A 203      90.359  75.112 -41.199  1.00 16.71           O  
-ATOM    849  CB  ALA A 203      90.169  77.430 -39.021  1.00 12.84           C  
-ATOM    850  N   GLU A 204      92.358  76.146 -41.153  1.00 10.03           N  
-ATOM    851  C   GLU A 204      94.196  74.717 -40.471  1.00 10.77           C  
-ATOM    852  O   GLU A 204      94.832  75.657 -40.007  1.00 10.32           O  
-ATOM    853  CA AGLU A 204      93.109  74.952 -41.508  0.61 10.93           C  
-ATOM    854  CB AGLU A 204      93.712  75.093 -42.905  0.61 13.54           C  
-ATOM    855  CG AGLU A 204      92.665  75.229 -44.002  0.61 11.27           C  
-ATOM    856  CD AGLU A 204      93.273  75.329 -45.392  0.61 13.92           C  
-ATOM    857  OE1AGLU A 204      94.504  75.177 -45.525  0.61 13.70           O  
-ATOM    858  OE2AGLU A 204      92.513  75.554 -46.352  0.61 13.16           O  
-ATOM    859  CA BGLU A 204      93.129  74.964 -41.526  0.39 10.96           C  
-ATOM    860  CB BGLU A 204      93.800  75.163 -42.886  0.39 13.49           C  
-ATOM    861  CG BGLU A 204      94.746  74.033 -43.281  0.39 14.96           C  
-ATOM    862  CD BGLU A 204      95.711  74.430 -44.391  0.39 12.79           C  
-ATOM    863  OE1BGLU A 204      95.303  75.175 -45.302  0.39 12.41           O  
-ATOM    864  OE2BGLU A 204      96.881  73.995 -44.348  0.39 12.96           O  
-ATOM    865  N   TYR A 205      94.383  73.457 -40.087  1.00  8.55           N  
-ATOM    866  CA  TYR A 205      95.379  73.106 -39.085  1.00  9.27           C  
-ATOM    867  C   TYR A 205      96.543  72.364 -39.726  1.00 14.97           C  
-ATOM    868  O   TYR A 205      96.339  71.387 -40.447  1.00 16.17           O  
-ATOM    869  CB  TYR A 205      94.725  72.274 -37.975  1.00  8.61           C  
-ATOM    870  CG  TYR A 205      93.770  73.100 -37.139  1.00  9.24           C  
-ATOM    871  CD1 TYR A 205      92.459  73.314 -37.547  1.00  9.32           C  
-ATOM    872  CD2 TYR A 205      94.194  73.690 -35.959  1.00  9.56           C  
-ATOM    873  CE1 TYR A 205      91.587  74.080 -36.779  1.00  9.72           C  
-ATOM    874  CE2 TYR A 205      93.330  74.459 -35.186  1.00  8.78           C  
-ATOM    875  CZ  TYR A 205      92.033  74.655 -35.608  1.00  9.37           C  
-ATOM    876  OH  TYR A 205      91.181  75.419 -34.840  1.00  8.60           O  
-ATOM    877  N   LEU A 206      97.760  72.842 -39.486  1.00  9.65           N  
-ATOM    878  CA  LEU A 206      98.934  72.240 -40.109  1.00 13.64           C  
-ATOM    879  C   LEU A 206      99.830  71.540 -39.103  1.00 13.22           C  
-ATOM    880  O   LEU A 206     100.156  72.100 -38.048  1.00 10.67           O  
-ATOM    881  CB  LEU A 206      99.763  73.301 -40.823  1.00 11.81           C  
-ATOM    882  CG  LEU A 206     101.081  72.822 -41.452  1.00 14.64           C  
-ATOM    883  CD1 LEU A 206     100.791  71.853 -42.594  1.00 16.56           C  
-ATOM    884  CD2 LEU A 206     101.903  73.999 -41.955  1.00 12.70           C  
-ATOM    885  N   ASP A 207     100.211  70.304 -39.439  1.00 13.26           N  
-ATOM    886  CA  ASP A 207     101.324  69.638 -38.788  1.00 15.89           C  
-ATOM    887  C   ASP A 207     102.463  69.656 -39.797  1.00 16.91           C  
-ATOM    888  O   ASP A 207     102.405  68.961 -40.816  1.00 16.09           O  
-ATOM    889  CB  ASP A 207     100.983  68.185 -38.453  1.00 15.29           C  
-ATOM    890  CG  ASP A 207      99.806  68.053 -37.512  1.00 24.24           C  
-ATOM    891  OD1 ASP A 207      99.841  68.666 -36.436  1.00 21.65           O  
-ATOM    892  OD2 ASP A 207      98.856  67.311 -37.838  1.00 34.94           O  
-ATOM    893  N   ASP A 208     103.491  70.447 -39.525  1.00 13.24           N  
-ATOM    894  CA  ASP A 208     104.563  70.646 -40.493  1.00 15.15           C  
-ATOM    895  C   ASP A 208     105.303  69.334 -40.743  1.00 17.04           C  
-ATOM    896  O   ASP A 208     105.728  68.666 -39.800  1.00 17.73           O  
-ATOM    897  CB  ASP A 208     105.529  71.725 -40.005  1.00 15.28           C  
-ATOM    898  CG  ASP A 208     106.471  72.200 -41.098  1.00 22.18           C  
-ATOM    899  OD1 ASP A 208     107.446  71.479 -41.396  1.00 22.60           O  
-ATOM    900  OD2 ASP A 208     106.235  73.292 -41.659  1.00 22.75           O  
-ATOM    901  N   ARG A 209     105.448  68.955 -42.009  1.00 19.48           N  
-ATOM    902  CA  ARG A 209     106.019  67.648 -42.325  1.00 23.99           C  
-ATOM    903  C   ARG A 209     107.504  67.602 -41.983  1.00 24.50           C  
-ATOM    904  O   ARG A 209     108.077  66.522 -41.824  1.00 28.04           O  
-ATOM    905  CB  ARG A 209     105.806  67.304 -43.804  1.00 30.96           C  
-ATOM    906  CG  ARG A 209     106.712  68.080 -44.751  1.00 43.40           C  
-ATOM    907  CD  ARG A 209     106.422  67.756 -46.214  1.00 48.45           C  
-ATOM    908  NE  ARG A 209     105.168  68.350 -46.672  1.00 53.58           N  
-ATOM    909  CZ  ARG A 209     104.661  68.180 -47.889  1.00 66.24           C  
-ATOM    910  NH1 ARG A 209     105.301  67.427 -48.775  1.00 66.91           N  
-ATOM    911  NH2 ARG A 209     103.514  68.760 -48.221  1.00 63.52           N  
-ATOM    912  N   ASN A 210     108.119  68.774 -41.858  1.00 23.59           N  
-ATOM    913  CA  ASN A 210     109.554  68.867 -41.588  1.00 26.35           C  
-ATOM    914  C   ASN A 210     109.927  69.251 -40.157  1.00 28.27           C  
-ATOM    915  O   ASN A 210     110.829  68.655 -39.568  1.00 29.30           O  
-ATOM    916  CB  ASN A 210     110.223  69.822 -42.577  1.00 30.97           C  
-ATOM    917  CG  ASN A 210     110.162  69.314 -44.000  1.00 35.96           C  
-ATOM    918  OD1 ASN A 210     109.737  70.027 -44.909  1.00 40.52           O  
-ATOM    919  ND2 ASN A 210     110.573  68.067 -44.199  1.00 36.76           N  
-ATOM    920  N   THR A 211     109.246  70.249 -39.598  1.00 23.60           N  
-ATOM    921  CA  THR A 211     109.554  70.699 -38.242  1.00 20.76           C  
-ATOM    922  C   THR A 211     108.643  70.069 -37.197  1.00 17.27           C  
-ATOM    923  O   THR A 211     108.915  70.164 -36.008  1.00 20.58           O  
-ATOM    924  CB  THR A 211     109.410  72.223 -38.102  1.00 22.37           C  
-ATOM    925  OG1 THR A 211     108.026  72.580 -38.228  1.00 20.49           O  
-ATOM    926  CG2 THR A 211     110.214  72.942 -39.179  1.00 26.51           C  
-ATOM    927  N   PHE A 212     107.555  69.447 -37.643  1.00 17.72           N  
-ATOM    928  CA  PHE A 212     106.571  68.846 -36.738  1.00 15.47           C  
-ATOM    929  C   PHE A 212     105.812  69.882 -35.898  1.00 16.22           C  
-ATOM    930  O   PHE A 212     105.025  69.521 -35.024  1.00 13.98           O  
-ATOM    931  CB  PHE A 212     107.225  67.812 -35.821  1.00 21.90           C  
-ATOM    932  CG  PHE A 212     107.992  66.751 -36.562  1.00 24.17           C  
-ATOM    933  CD1 PHE A 212     107.336  65.855 -37.388  1.00 27.88           C  
-ATOM    934  CD2 PHE A 212     109.367  66.653 -36.430  1.00 32.21           C  
-ATOM    935  CE1 PHE A 212     108.039  64.880 -38.078  1.00 33.02           C  
-ATOM    936  CE2 PHE A 212     110.074  65.679 -37.112  1.00 36.66           C  
-ATOM    937  CZ  PHE A 212     109.407  64.792 -37.936  1.00 37.28           C  
-ATOM    938  N   ARG A 213     106.035  71.160 -36.170  1.00 12.75           N  
-ATOM    939  CA  ARG A 213     105.320  72.205 -35.428  1.00 11.72           C  
-ATOM    940  C   ARG A 213     103.866  72.345 -35.867  1.00 13.01           C  
-ATOM    941  O   ARG A 213     103.527  72.037 -37.007  1.00 12.43           O  
-ATOM    942  CB  ARG A 213     106.028  73.543 -35.559  1.00 14.35           C  
-ATOM    943  CG  ARG A 213     107.314  73.616 -34.772  1.00 15.00           C  
-ATOM    944  CD  ARG A 213     107.873  75.015 -34.838  1.00 15.84           C  
-ATOM    945  NE  ARG A 213     109.269  75.074 -34.417  1.00 17.32           N  
-ATOM    946  CZ  ARG A 213     109.667  75.149 -33.152  1.00 22.31           C  
-ATOM    947  NH1 ARG A 213     108.778  75.144 -32.162  1.00 13.87           N  
-ATOM    948  NH2 ARG A 213     110.961  75.220 -32.879  1.00 20.90           N  
-ATOM    949  N   HIS A 214     103.021  72.821 -34.946  1.00  7.90           N  
-ATOM    950  CA  HIS A 214     101.594  72.989 -35.197  1.00  8.50           C  
-ATOM    951  C   HIS A 214     101.291  74.447 -35.510  1.00  8.71           C  
-ATOM    952  O   HIS A 214     101.908  75.352 -34.941  1.00  8.50           O  
-ATOM    953  CB  HIS A 214     100.791  72.606 -33.951  1.00  8.38           C  
-ATOM    954  CG  HIS A 214     101.081  71.227 -33.434  1.00  6.82           C  
-ATOM    955  ND1 HIS A 214     100.817  70.854 -32.132  1.00 11.44           N  
-ATOM    956  CD2 HIS A 214     101.597  70.132 -34.046  1.00 12.07           C  
-ATOM    957  CE1 HIS A 214     101.165  69.588 -31.963  1.00 14.26           C  
-ATOM    958  NE2 HIS A 214     101.638  69.126 -33.109  1.00 11.59           N  
-ATOM    959  N   SER A 215     100.328  74.682 -36.397  1.00  7.99           N  
-ATOM    960  CA  SER A 215      99.816  76.036 -36.598  1.00  7.34           C  
-ATOM    961  C   SER A 215      98.380  75.996 -37.078  1.00  8.62           C  
-ATOM    962  O   SER A 215      97.895  74.962 -37.567  1.00  9.17           O  
-ATOM    963  CB  SER A 215     100.693  76.826 -37.588  1.00  8.95           C  
-ATOM    964  OG  SER A 215     100.792  76.138 -38.838  1.00 10.56           O  
-ATOM    965  N   VAL A 216      97.692  77.124 -36.935  1.00  7.53           N  
-ATOM    966  CA  VAL A 216      96.339  77.249 -37.460  1.00  5.94           C  
-ATOM    967  C   VAL A 216      96.286  78.497 -38.335  1.00  7.29           C  
-ATOM    968  O   VAL A 216      96.795  79.548 -37.950  1.00  7.77           O  
-ATOM    969  CB  VAL A 216      95.280  77.301 -36.327  1.00  7.42           C  
-ATOM    970  CG1 VAL A 216      95.574  78.441 -35.321  1.00  8.15           C  
-ATOM    971  CG2 VAL A 216      93.879  77.406 -36.915  1.00  9.81           C  
-ATOM    972  N   VAL A 217      95.685  78.368 -39.512  1.00  6.58           N  
-ATOM    973  CA  VAL A 217      95.734  79.445 -40.503  1.00  5.71           C  
-ATOM    974  C   VAL A 217      94.327  79.713 -41.060  1.00  9.58           C  
-ATOM    975  O   VAL A 217      93.557  78.779 -41.312  1.00  9.99           O  
-ATOM    976  CB  VAL A 217      96.756  79.119 -41.634  1.00  5.74           C  
-ATOM    977  CG1 VAL A 217      96.378  77.831 -42.349  1.00  8.58           C  
-ATOM    978  CG2 VAL A 217      96.854  80.285 -42.645  1.00  8.10           C  
-ATOM    979  N   VAL A 218      93.986  80.988 -41.220  1.00  7.88           N  
-ATOM    980  CA  VAL A 218      92.697  81.378 -41.800  1.00  9.57           C  
-ATOM    981  C   VAL A 218      92.873  82.395 -42.925  1.00  7.23           C  
-ATOM    982  O   VAL A 218      93.888  83.069 -43.004  1.00  8.57           O  
-ATOM    983  CB  VAL A 218      91.744  82.001 -40.756  1.00  6.33           C  
-ATOM    984  CG1 VAL A 218      91.358  80.963 -39.698  1.00 10.61           C  
-ATOM    985  CG2 VAL A 218      92.377  83.234 -40.112  1.00 11.01           C  
-ATOM    986  N   PRO A 219      91.882  82.490 -43.813  1.00  8.61           N  
-ATOM    987  CA  PRO A 219      91.952  83.558 -44.824  1.00  9.44           C  
-ATOM    988  C   PRO A 219      91.887  84.919 -44.145  1.00 12.14           C  
-ATOM    989  O   PRO A 219      91.164  85.091 -43.150  1.00 12.88           O  
-ATOM    990  CB  PRO A 219      90.684  83.334 -45.651  1.00 11.61           C  
-ATOM    991  CG  PRO A 219      90.368  81.872 -45.473  1.00 14.39           C  
-ATOM    992  CD  PRO A 219      90.752  81.574 -44.041  1.00 13.40           C  
-ATOM    993  N   CYS A 220      92.646  85.876 -44.662  1.00 11.06           N  
-ATOM    994  CA  CYS A 220      92.563  87.249 -44.191  1.00 14.22           C  
-ATOM    995  C   CYS A 220      91.291  87.863 -44.774  1.00 19.27           C  
-ATOM    996  O   CYS A 220      91.109  87.886 -45.994  1.00 20.91           O  
-ATOM    997  CB  CYS A 220      93.795  88.040 -44.637  1.00 12.42           C  
-ATOM    998  SG  CYS A 220      93.848  89.725 -43.964  1.00 16.61           S  
-ATOM    999  N   GLU A 221      90.398  88.332 -43.909  1.00 14.64           N  
-ATOM   1000  CA  GLU A 221      89.126  88.877 -44.375  1.00 16.18           C  
-ATOM   1001  C   GLU A 221      88.997  90.349 -44.001  1.00 13.78           C  
-ATOM   1002  O   GLU A 221      89.548  90.788 -42.995  1.00 12.06           O  
-ATOM   1003  CB  GLU A 221      87.954  88.083 -43.801  1.00 20.46           C  
-ATOM   1004  CG  GLU A 221      87.817  86.685 -44.381  1.00 30.16           C  
-ATOM   1005  CD  GLU A 221      86.935  85.797 -43.530  1.00 37.33           C  
-ATOM   1006  OE1 GLU A 221      86.431  86.283 -42.496  1.00 39.89           O  
-ATOM   1007  OE2 GLU A 221      86.751  84.612 -43.888  1.00 45.42           O  
-ATOM   1008  N   PRO A 222      88.274  91.123 -44.826  1.00 15.01           N  
-ATOM   1009  CA  PRO A 222      88.065  92.549 -44.558  1.00 12.63           C  
-ATOM   1010  C   PRO A 222      87.162  92.751 -43.346  1.00 16.03           C  
-ATOM   1011  O   PRO A 222      86.395  91.857 -42.996  1.00 18.03           O  
-ATOM   1012  CB  PRO A 222      87.352  93.051 -45.825  1.00 20.84           C  
-ATOM   1013  CG  PRO A 222      87.532  91.975 -46.847  1.00 27.59           C  
-ATOM   1014  CD  PRO A 222      87.629  90.693 -46.077  1.00 20.09           C  
-ATOM   1015  N   PRO A 223      87.261  93.915 -42.699  1.00 15.32           N  
-ATOM   1016  CA  PRO A 223      86.392  94.207 -41.553  1.00 18.16           C  
-ATOM   1017  C   PRO A 223      84.913  94.205 -41.949  1.00 17.17           C  
-ATOM   1018  O   PRO A 223      84.577  94.488 -43.095  1.00 20.55           O  
-ATOM   1019  CB  PRO A 223      86.819  95.620 -41.140  1.00 17.22           C  
-ATOM   1020  CG  PRO A 223      88.221  95.771 -41.668  1.00 14.40           C  
-ATOM   1021  CD  PRO A 223      88.245  94.980 -42.950  1.00 15.01           C  
-ATOM   1022  N   GLU A 224      84.041  93.861 -41.010  1.00 21.13           N  
-ATOM   1023  CA  GLU A 224      82.608  93.987 -41.233  1.00 19.31           C  
-ATOM   1024  C   GLU A 224      82.290  95.453 -41.519  1.00 23.66           C  
-ATOM   1025  O   GLU A 224      83.018  96.352 -41.091  1.00 19.79           O  
-ATOM   1026  CB  GLU A 224      81.842  93.525 -39.994  1.00 22.63           C  
-ATOM   1027  CG  GLU A 224      82.161  92.098 -39.575  1.00 26.76           C  
-ATOM   1028  CD  GLU A 224      81.684  91.086 -40.597  1.00 37.40           C  
-ATOM   1029  OE1 GLU A 224      80.499  91.165 -40.989  1.00 33.06           O  
-ATOM   1030  OE2 GLU A 224      82.490  90.216 -41.008  1.00 36.59           O  
-ATOM   1031  N   VAL A 225      81.202  95.698 -42.243  1.00 24.65           N  
-ATOM   1032  CA  VAL A 225      80.806  97.067 -42.543  1.00 22.58           C  
-ATOM   1033  C   VAL A 225      80.637  97.874 -41.264  1.00 21.50           C  
-ATOM   1034  O   VAL A 225      79.908  97.470 -40.350  1.00 19.81           O  
-ATOM   1035  CB  VAL A 225      79.498  97.119 -43.334  1.00 26.19           C  
-ATOM   1036  CG1 VAL A 225      79.139  98.562 -43.639  1.00 24.99           C  
-ATOM   1037  CG2 VAL A 225      79.622  96.296 -44.613  1.00 29.56           C  
-ATOM   1038  N   GLY A 226      81.320  99.012 -41.199  1.00 21.47           N  
-ATOM   1039  CA  GLY A 226      81.276  99.866 -40.029  1.00 21.62           C  
-ATOM   1040  C   GLY A 226      82.458  99.686 -39.092  1.00 27.28           C  
-ATOM   1041  O   GLY A 226      82.643 100.477 -38.169  1.00 31.34           O  
-ATOM   1042  N   SER A 227      83.255  98.644 -39.322  1.00 20.08           N  
-ATOM   1043  CA  SER A 227      84.418  98.361 -38.481  1.00 18.65           C  
-ATOM   1044  C   SER A 227      85.720  98.704 -39.198  1.00 14.60           C  
-ATOM   1045  O   SER A 227      85.772  98.745 -40.425  1.00 15.17           O  
-ATOM   1046  CB  SER A 227      84.434  96.893 -38.047  1.00 21.04           C  
-ATOM   1047  OG  SER A 227      83.375  96.614 -37.144  1.00 25.05           O  
-ATOM   1048  N   ASP A 228      86.768  98.942 -38.414  1.00 12.59           N  
-ATOM   1049  CA  ASP A 228      88.051  99.393 -38.937  1.00 16.94           C  
-ATOM   1050  C   ASP A 228      89.125  98.311 -38.904  1.00 13.72           C  
-ATOM   1051  O   ASP A 228      90.223  98.505 -39.439  1.00 15.75           O  
-ATOM   1052  CB  ASP A 228      88.534 100.612 -38.149  1.00 18.55           C  
-ATOM   1053  CG  ASP A 228      87.697 101.851 -38.416  1.00 23.50           C  
-ATOM   1054  OD1 ASP A 228      87.273 102.051 -39.572  1.00 28.50           O  
-ATOM   1055  OD2 ASP A 228      87.466 102.619 -37.461  1.00 33.24           O  
-ATOM   1056  N   CYS A 229      88.814  97.186 -38.268  1.00 11.18           N  
-ATOM   1057  CA  CYS A 229      89.757  96.074 -38.172  1.00 11.46           C  
-ATOM   1058  C   CYS A 229      89.011  94.746 -38.177  1.00 11.00           C  
-ATOM   1059  O   CYS A 229      87.789  94.708 -38.060  1.00 12.71           O  
-ATOM   1060  CB  CYS A 229      90.603  96.187 -36.892  1.00 10.80           C  
-ATOM   1061  SG  CYS A 229      89.733  95.835 -35.332  1.00 13.71           S  
-ATOM   1062  N   THR A 230      89.755  93.656 -38.332  1.00 11.88           N  
-ATOM   1063  C   THR A 230      89.614  91.603 -37.037  1.00 12.18           C  
-ATOM   1064  O   THR A 230      90.739  91.781 -36.579  1.00 10.53           O  
-ATOM   1065  CA ATHR A 230      89.158  92.329 -38.294  0.17 10.87           C  
-ATOM   1066  CB ATHR A 230      89.526  91.501 -39.536  0.17 11.17           C  
-ATOM   1067  OG1ATHR A 230      88.848  90.239 -39.492  0.17 13.36           O  
-ATOM   1068  CG2ATHR A 230      91.017  91.267 -39.588  0.17 10.23           C  
-ATOM   1069  CA BTHR A 230      89.186  92.319 -38.313  0.83 10.81           C  
-ATOM   1070  CB BTHR A 230      89.650  91.540 -39.557  0.83 11.02           C  
-ATOM   1071  OG1BTHR A 230      89.043  92.127 -40.718  0.83 10.23           O  
-ATOM   1072  CG2BTHR A 230      89.264  90.068 -39.472  0.83 13.18           C  
-ATOM   1073  N   THR A 231      88.723  90.801 -36.468  1.00  8.79           N  
-ATOM   1074  CA  THR A 231      89.050  90.115 -35.223  1.00  7.98           C  
-ATOM   1075  C   THR A 231      89.035  88.606 -35.419  1.00 11.25           C  
-ATOM   1076  O   THR A 231      88.129  88.066 -36.055  1.00 13.51           O  
-ATOM   1077  CB  THR A 231      88.093  90.537 -34.088  1.00 12.40           C  
-ATOM   1078  OG1 THR A 231      88.203  91.953 -33.879  1.00 12.65           O  
-ATOM   1079  CG2 THR A 231      88.447  89.826 -32.786  1.00 13.59           C  
-ATOM   1080  N   ILE A 232      90.064  87.933 -34.914  1.00  8.28           N  
-ATOM   1081  CA  ILE A 232      90.092  86.475 -34.928  1.00  7.92           C  
-ATOM   1082  C   ILE A 232      89.929  86.040 -33.488  1.00  8.92           C  
-ATOM   1083  O   ILE A 232      90.495  86.658 -32.587  1.00  8.69           O  
-ATOM   1084  CB  ILE A 232      91.440  85.913 -35.474  1.00  7.87           C  
-ATOM   1085  CG1 ILE A 232      91.635  86.302 -36.941  1.00 12.70           C  
-ATOM   1086  CG2 ILE A 232      91.505  84.377 -35.314  1.00 10.61           C  
-ATOM   1087  CD1 ILE A 232      92.950  85.805 -37.527  1.00 12.52           C  
-ATOM   1088  N   HIS A 233      89.134  85.000 -33.254  1.00  9.11           N  
-ATOM   1089  CA  HIS A 233      88.957  84.503 -31.889  1.00  8.60           C  
-ATOM   1090  C   HIS A 233      89.773  83.225 -31.676  1.00  9.68           C  
-ATOM   1091  O   HIS A 233      89.508  82.215 -32.313  1.00 11.22           O  
-ATOM   1092  CB  HIS A 233      87.469  84.257 -31.596  1.00  8.93           C  
-ATOM   1093  CG  HIS A 233      86.630  85.490 -31.739  1.00 11.17           C  
-ATOM   1094  ND1 HIS A 233      85.817  85.715 -32.828  1.00 21.01           N  
-ATOM   1095  CD2 HIS A 233      86.510  86.583 -30.949  1.00 14.69           C  
-ATOM   1096  CE1 HIS A 233      85.224  86.889 -32.698  1.00 18.97           C  
-ATOM   1097  NE2 HIS A 233      85.627  87.436 -31.567  1.00 16.14           N  
-ATOM   1098  N   TYR A 234      90.778  83.287 -30.802  1.00  7.34           N  
-ATOM   1099  CA  TYR A 234      91.635  82.128 -30.550  1.00  8.62           C  
-ATOM   1100  C   TYR A 234      91.258  81.459 -29.234  1.00  7.53           C  
-ATOM   1101  O   TYR A 234      90.727  82.109 -28.334  1.00  9.82           O  
-ATOM   1102  CB  TYR A 234      93.114  82.542 -30.494  1.00  7.01           C  
-ATOM   1103  CG  TYR A 234      93.719  82.944 -31.827  1.00  7.97           C  
-ATOM   1104  CD1 TYR A 234      93.995  81.987 -32.808  1.00  6.22           C  
-ATOM   1105  CD2 TYR A 234      94.027  84.272 -32.105  1.00  7.92           C  
-ATOM   1106  CE1 TYR A 234      94.560  82.353 -34.024  1.00  9.03           C  
-ATOM   1107  CE2 TYR A 234      94.588  84.645 -33.317  1.00  9.32           C  
-ATOM   1108  CZ  TYR A 234      94.854  83.673 -34.274  1.00  8.92           C  
-ATOM   1109  OH  TYR A 234      95.408  84.036 -35.483  1.00  8.41           O  
-ATOM   1110  N   ASN A 235      91.519  80.160 -29.128  1.00  6.58           N  
-ATOM   1111  CA  ASN A 235      91.442  79.459 -27.837  1.00  7.58           C  
-ATOM   1112  C   ASN A 235      92.780  78.807 -27.545  1.00  8.32           C  
-ATOM   1113  O   ASN A 235      93.408  78.263 -28.462  1.00 10.09           O  
-ATOM   1114  CB  ASN A 235      90.390  78.340 -27.850  1.00 11.62           C  
-ATOM   1115  CG  ASN A 235      88.977  78.833 -28.119  1.00 21.62           C  
-ATOM   1116  OD1 ASN A 235      88.157  78.094 -28.666  1.00 25.02           O  
-ATOM   1117  ND2 ASN A 235      88.677  80.064 -27.720  1.00 11.88           N  
-ATOM   1118  N   TYR A 236      93.197  78.826 -26.276  1.00  7.22           N  
-ATOM   1119  CA  TYR A 236      94.392  78.098 -25.838  1.00  7.81           C  
-ATOM   1120  C   TYR A 236      93.947  76.913 -24.988  1.00 10.58           C  
-ATOM   1121  O   TYR A 236      93.223  77.082 -24.006  1.00  8.89           O  
-ATOM   1122  CB  TYR A 236      95.344  79.020 -25.060  1.00  5.99           C  
-ATOM   1123  CG  TYR A 236      95.973  80.071 -25.948  1.00  7.53           C  
-ATOM   1124  CD1 TYR A 236      95.300  81.257 -26.236  1.00  8.95           C  
-ATOM   1125  CD2 TYR A 236      97.237  79.873 -26.508  1.00  6.64           C  
-ATOM   1126  CE1 TYR A 236      95.863  82.217 -27.060  1.00  9.95           C  
-ATOM   1127  CE2 TYR A 236      97.814  80.833 -27.337  1.00  9.07           C  
-ATOM   1128  CZ  TYR A 236      97.119  82.000 -27.609  1.00 10.72           C  
-ATOM   1129  OH  TYR A 236      97.667  82.966 -28.428  1.00 10.50           O  
-ATOM   1130  N   MET A 237      94.379  75.714 -25.374  1.00  8.38           N  
-ATOM   1131  CA  MET A 237      93.723  74.495 -24.912  1.00  7.05           C  
-ATOM   1132  C   MET A 237      94.500  73.727 -23.841  1.00 10.56           C  
-ATOM   1133  O   MET A 237      94.197  72.561 -23.567  1.00 11.51           O  
-ATOM   1134  CB  MET A 237      93.417  73.586 -26.113  1.00  8.30           C  
-ATOM   1135  CG  MET A 237      92.564  74.255 -27.201  1.00 10.18           C  
-ATOM   1136  SD  MET A 237      90.974  74.835 -26.563  1.00 12.72           S  
-ATOM   1137  CE  MET A 237      90.298  73.332 -25.840  1.00 13.92           C  
-ATOM   1138  N   CYS A 238      95.495  74.386 -23.251  1.00  9.31           N  
-ATOM   1139  C   CYS A 238      96.650  74.981 -21.204  1.00 10.43           C  
-ATOM   1140  O   CYS A 238      96.830  76.104 -21.666  1.00 11.47           O  
-ATOM   1141  CA ACYS A 238      96.218  73.841 -22.103  0.50 11.28           C  
-ATOM   1142  CB ACYS A 238      97.468  73.092 -22.547  0.50 12.83           C  
-ATOM   1143  SG ACYS A 238      97.275  71.315 -22.775  0.50  9.01           S  
-ATOM   1144  CA BCYS A 238      96.282  73.841 -22.149  0.50 11.30           C  
-ATOM   1145  CB BCYS A 238      97.579  73.273 -22.707  0.50 12.91           C  
-ATOM   1146  SG BCYS A 238      97.969  71.605 -22.211  0.50 10.56           S  
-ATOM   1147  N   TYR A 239      96.806  74.692 -19.905  1.00  8.39           N  
-ATOM   1148  CA  TYR A 239      97.358  75.678 -18.968  1.00  9.69           C  
-ATOM   1149  C   TYR A 239      98.871  75.775 -19.113  1.00 11.87           C  
-ATOM   1150  O   TYR A 239      99.531  74.785 -19.430  1.00 11.80           O  
-ATOM   1151  CB  TYR A 239      97.082  75.291 -17.512  1.00 12.25           C  
-ATOM   1152  CG  TYR A 239      95.655  75.439 -17.068  1.00 12.23           C  
-ATOM   1153  CD1 TYR A 239      95.082  76.698 -16.917  1.00 13.31           C  
-ATOM   1154  CD2 TYR A 239      94.887  74.323 -16.766  1.00 16.53           C  
-ATOM   1155  CE1 TYR A 239      93.778  76.839 -16.493  1.00 18.38           C  
-ATOM   1156  CE2 TYR A 239      93.576  74.454 -16.341  1.00 16.47           C  
-ATOM   1157  CZ  TYR A 239      93.028  75.709 -16.210  1.00 17.02           C  
-ATOM   1158  OH  TYR A 239      91.725  75.846 -15.796  1.00 19.18           O  
-ATOM   1159  N   SER A 240      99.435  76.951 -18.838  1.00  9.46           N  
-ATOM   1160  CA  SER A 240     100.889  77.079 -18.846  1.00  9.36           C  
-ATOM   1161  C   SER A 240     101.521  76.063 -17.897  1.00 11.22           C  
-ATOM   1162  O   SER A 240     102.632  75.580 -18.137  1.00 13.49           O  
-ATOM   1163  CB  SER A 240     101.324  78.499 -18.481  1.00 10.25           C  
-ATOM   1164  OG  SER A 240     100.982  79.406 -19.522  1.00 10.66           O  
-ATOM   1165  N   SER A 241     100.789  75.724 -16.844  1.00 10.37           N  
-ATOM   1166  CA  SER A 241     101.310  74.842 -15.807  1.00 11.20           C  
-ATOM   1167  C   SER A 241     101.190  73.352 -16.112  1.00 15.86           C  
-ATOM   1168  O   SER A 241     101.698  72.537 -15.341  1.00 14.63           O  
-ATOM   1169  CB  SER A 241     100.615  75.132 -14.476  1.00 15.07           C  
-ATOM   1170  OG  SER A 241      99.233  74.803 -14.554  1.00 15.98           O  
-ATOM   1171  N   CYS A 242     100.536  72.981 -17.212  1.00 12.19           N  
-ATOM   1172  CA  CYS A 242     100.286  71.550 -17.451  1.00 13.17           C  
-ATOM   1173  C   CYS A 242     101.550  70.668 -17.418  1.00 16.18           C  
-ATOM   1174  O   CYS A 242     102.489  70.858 -18.189  1.00 13.37           O  
-ATOM   1175  CB  CYS A 242      99.494  71.315 -18.751  1.00 12.44           C  
-ATOM   1176  SG  CYS A 242      97.706  71.623 -18.600  1.00 12.14           S  
-ATOM   1177  N   MET A 243     101.562  69.684 -16.523  1.00 14.46           N  
-ATOM   1178  CA  MET A 243     102.693  68.771 -16.443  1.00 16.06           C  
-ATOM   1179  C   MET A 243     102.818  67.907 -17.707  1.00 16.56           C  
-ATOM   1180  O   MET A 243     101.815  67.456 -18.265  1.00 12.15           O  
-ATOM   1181  CB  MET A 243     102.569  67.896 -15.186  1.00 13.91           C  
-ATOM   1182  CG  MET A 243     102.662  68.690 -13.897  1.00 25.45           C  
-ATOM   1183  SD  MET A 243     104.264  69.516 -13.757  1.00 36.43           S  
-ATOM   1184  CE  MET A 243     105.360  68.103 -13.620  1.00 33.60           C  
-ATOM   1185  N   GLY A 244     104.051  67.693 -18.168  1.00 16.46           N  
-ATOM   1186  CA  GLY A 244     104.289  66.939 -19.391  1.00 16.28           C  
-ATOM   1187  C   GLY A 244     103.974  67.726 -20.660  1.00 18.26           C  
-ATOM   1188  O   GLY A 244     104.178  67.241 -21.780  1.00 17.07           O  
-ATOM   1189  N   GLY A 245     103.463  68.942 -20.484  1.00 16.86           N  
-ATOM   1190  CA  GLY A 245     103.187  69.831 -21.603  1.00 14.60           C  
-ATOM   1191  C   GLY A 245     104.046  71.076 -21.467  1.00 14.99           C  
-ATOM   1192  O   GLY A 245     105.269  70.974 -21.360  1.00 15.40           O  
-ATOM   1193  N   MET A 246     103.424  72.254 -21.453  1.00 12.44           N  
-ATOM   1194  CA  MET A 246     104.193  73.486 -21.253  1.00 12.45           C  
-ATOM   1195  C   MET A 246     104.980  73.478 -19.936  1.00 17.06           C  
-ATOM   1196  O   MET A 246     106.068  74.040 -19.857  1.00 12.86           O  
-ATOM   1197  CB  MET A 246     103.302  74.731 -21.405  1.00 10.45           C  
-ATOM   1198  CG  MET A 246     102.955  75.013 -22.870  1.00 11.92           C  
-ATOM   1199  SD  MET A 246     101.810  76.385 -23.123  1.00 11.57           S  
-ATOM   1200  CE  MET A 246     100.258  75.698 -22.525  1.00 11.91           C  
-ATOM   1201  N   ASN A 247     104.446  72.813 -18.911  1.00 13.14           N  
-ATOM   1202  CA  ASN A 247     105.186  72.609 -17.664  1.00 16.58           C  
-ATOM   1203  C   ASN A 247     105.779  73.881 -17.066  1.00 16.73           C  
-ATOM   1204  O   ASN A 247     106.942  73.897 -16.654  1.00 16.02           O  
-ATOM   1205  CB  ASN A 247     106.299  71.571 -17.854  1.00 21.65           C  
-ATOM   1206  CG  ASN A 247     106.911  71.122 -16.523  1.00 31.06           C  
-ATOM   1207  OD1 ASN A 247     106.275  71.213 -15.471  1.00 32.43           O  
-ATOM   1208  ND2 ASN A 247     108.148  70.641 -16.568  1.00 33.54           N  
-ATOM   1209  N   ARG A 248     104.971  74.939 -17.033  1.00 12.23           N  
-ATOM   1210  CA  ARG A 248     105.333  76.233 -16.450  1.00 15.71           C  
-ATOM   1211  C   ARG A 248     106.260  77.104 -17.310  1.00 17.24           C  
-ATOM   1212  O   ARG A 248     106.636  78.201 -16.906  1.00 19.42           O  
-ATOM   1213  CB  ARG A 248     105.885  76.068 -15.024  1.00 19.67           C  
-ATOM   1214  CG  ARG A 248     104.861  75.504 -14.054  1.00 19.57           C  
-ATOM   1215  CD  ARG A 248     105.425  75.347 -12.644  1.00 30.31           C  
-ATOM   1216  NE  ARG A 248     104.387  74.924 -11.707  1.00 47.77           N  
-ATOM   1217  CZ  ARG A 248     104.615  74.526 -10.458  1.00 65.69           C  
-ATOM   1218  NH1 ARG A 248     105.856  74.485  -9.983  1.00 67.23           N  
-ATOM   1219  NH2 ARG A 248     103.602  74.163  -9.682  1.00 63.42           N  
-ATOM   1220  N   ARG A 249     106.618  76.617 -18.490  1.00 14.35           N  
-ATOM   1221  CA  ARG A 249     107.481  77.374 -19.392  1.00 10.34           C  
-ATOM   1222  C   ARG A 249     106.641  78.386 -20.168  1.00 13.78           C  
-ATOM   1223  O   ARG A 249     105.609  78.026 -20.731  1.00 14.50           O  
-ATOM   1224  CB  ARG A 249     108.174  76.417 -20.363  1.00 10.78           C  
-ATOM   1225  CG  ARG A 249     109.161  75.476 -19.680  1.00 17.21           C  
-ATOM   1226  CD  ARG A 249     109.709  74.431 -20.640  1.00 18.91           C  
-ATOM   1227  NE  ARG A 249     108.683  73.502 -21.101  1.00 14.66           N  
-ATOM   1228  CZ  ARG A 249     108.905  72.544 -21.994  1.00 13.79           C  
-ATOM   1229  NH1 ARG A 249     110.119  72.391 -22.504  1.00 15.03           N  
-ATOM   1230  NH2 ARG A 249     107.923  71.742 -22.374  1.00 14.85           N  
-ATOM   1231  N   PRO A 250     107.081  79.655 -20.207  1.00 14.82           N  
-ATOM   1232  CA  PRO A 250     106.349  80.664 -20.975  1.00 12.18           C  
-ATOM   1233  C   PRO A 250     106.453  80.404 -22.469  1.00 13.35           C  
-ATOM   1234  O   PRO A 250     107.479  79.911 -22.958  1.00 12.18           O  
-ATOM   1235  CB  PRO A 250     107.082  81.971 -20.635  1.00 13.32           C  
-ATOM   1236  CG  PRO A 250     107.840  81.678 -19.385  1.00 23.66           C  
-ATOM   1237  CD  PRO A 250     108.226  80.241 -19.491  1.00 18.84           C  
-ATOM   1238  N   ILE A 251     105.384  80.748 -23.183  1.00 10.65           N  
-ATOM   1239  CA  ILE A 251     105.358  80.656 -24.633  1.00  9.14           C  
-ATOM   1240  C   ILE A 251     105.082  82.021 -25.259  1.00  7.47           C  
-ATOM   1241  O   ILE A 251     104.643  82.963 -24.581  1.00  8.52           O  
-ATOM   1242  CB  ILE A 251     104.290  79.660 -25.137  1.00 11.10           C  
-ATOM   1243  CG1 ILE A 251     102.889  80.096 -24.688  1.00 11.76           C  
-ATOM   1244  CG2 ILE A 251     104.604  78.232 -24.648  1.00  9.08           C  
-ATOM   1245  CD1 ILE A 251     101.765  79.497 -25.534  1.00 10.84           C  
-ATOM   1246  N   LEU A 252     105.397  82.120 -26.545  1.00  7.87           N  
-ATOM   1247  CA  LEU A 252     104.990  83.256 -27.368  1.00  9.70           C  
-ATOM   1248  C   LEU A 252     104.063  82.724 -28.435  1.00  8.37           C  
-ATOM   1249  O   LEU A 252     104.243  81.604 -28.914  1.00 10.49           O  
-ATOM   1250  CB  LEU A 252     106.193  83.879 -28.082  1.00 12.22           C  
-ATOM   1251  CG  LEU A 252     107.408  84.298 -27.267  1.00 22.01           C  
-ATOM   1252  CD1 LEU A 252     108.532  84.710 -28.206  1.00 29.14           C  
-ATOM   1253  CD2 LEU A 252     107.031  85.434 -26.333  1.00 23.63           C  
-ATOM   1254  N   THR A 253     103.084  83.531 -28.830  1.00  8.10           N  
-ATOM   1255  CA  THR A 253     102.337  83.257 -30.050  1.00  7.93           C  
-ATOM   1256  C   THR A 253     102.879  84.179 -31.128  1.00  6.39           C  
-ATOM   1257  O   THR A 253     103.057  85.379 -30.895  1.00  7.89           O  
-ATOM   1258  CB  THR A 253     100.823  83.508 -29.870  1.00  7.44           C  
-ATOM   1259  OG1 THR A 253     100.311  82.587 -28.897  1.00  7.75           O  
-ATOM   1260  CG2 THR A 253     100.075  83.286 -31.184  1.00  6.32           C  
-ATOM   1261  N   ILE A 254     103.188  83.598 -32.284  1.00  6.16           N  
-ATOM   1262  CA  ILE A 254     103.646  84.349 -33.453  1.00  6.87           C  
-ATOM   1263  C   ILE A 254     102.524  84.371 -34.482  1.00  7.37           C  
-ATOM   1264  O   ILE A 254     102.024  83.317 -34.892  1.00  7.49           O  
-ATOM   1265  CB  ILE A 254     104.894  83.697 -34.093  1.00  6.96           C  
-ATOM   1266  CG1 ILE A 254     106.026  83.593 -33.071  1.00 10.92           C  
-ATOM   1267  CG2 ILE A 254     105.346  84.516 -35.333  1.00  9.79           C  
-ATOM   1268  CD1 ILE A 254     107.173  82.650 -33.494  1.00 12.39           C  
-ATOM   1269  N   ILE A 255     102.128  85.570 -34.913  1.00  7.51           N  
-ATOM   1270  CA  ILE A 255     101.093  85.689 -35.934  1.00  5.53           C  
-ATOM   1271  C   ILE A 255     101.732  86.215 -37.202  1.00  8.22           C  
-ATOM   1272  O   ILE A 255     102.352  87.286 -37.204  1.00  9.51           O  
-ATOM   1273  CB  ILE A 255      99.982  86.686 -35.533  1.00  8.09           C  
-ATOM   1274  CG1 ILE A 255      99.401  86.345 -34.160  1.00  9.80           C  
-ATOM   1275  CG2 ILE A 255      98.892  86.747 -36.620  1.00  8.15           C  
-ATOM   1276  CD1 ILE A 255      98.590  85.094 -34.115  1.00 11.58           C  
-ATOM   1277  N   THR A 256     101.579  85.466 -38.285  1.00  8.02           N  
-ATOM   1278  C   THR A 256     101.100  86.122 -40.613  1.00  7.87           C  
-ATOM   1279  O   THR A 256     100.140  85.354 -40.746  1.00  9.70           O  
-ATOM   1280  CA ATHR A 256     102.153  85.891 -39.551  0.58  8.39           C  
-ATOM   1281  CB ATHR A 256     103.212  84.898 -40.077  0.58  8.59           C  
-ATOM   1282  OG1ATHR A 256     102.701  83.561 -40.011  0.58  8.33           O  
-ATOM   1283  CG2ATHR A 256     104.462  84.987 -39.228  0.58 10.98           C  
-ATOM   1284  CA BTHR A 256     102.166  85.834 -39.566  0.42  8.40           C  
-ATOM   1285  CB BTHR A 256     103.045  84.693 -40.107  0.42  8.75           C  
-ATOM   1286  OG1BTHR A 256     103.992  84.296 -39.107  0.42 10.36           O  
-ATOM   1287  CG2BTHR A 256     103.777  85.128 -41.358  0.42  9.74           C  
-ATOM   1288  N   LEU A 257     101.290  87.207 -41.364  1.00  6.25           N  
-ATOM   1289  CA  LEU A 257     100.469  87.494 -42.521  1.00  7.58           C  
-ATOM   1290  C   LEU A 257     101.246  86.874 -43.694  1.00  7.14           C  
-ATOM   1291  O   LEU A 257     102.440  87.133 -43.835  1.00  9.39           O  
-ATOM   1292  CB  LEU A 257     100.324  89.015 -42.678  1.00  7.57           C  
-ATOM   1293  CG  LEU A 257      99.326  89.477 -43.741  1.00  9.45           C  
-ATOM   1294  CD1 LEU A 257      97.900  89.200 -43.279  1.00  9.68           C  
-ATOM   1295  CD2 LEU A 257      99.510  90.958 -44.059  1.00 10.66           C  
-ATOM   1296  N   GLU A 258     100.596  86.011 -44.474  1.00  8.46           N  
-ATOM   1297  CA  GLU A 258     101.271  85.233 -45.534  1.00  7.89           C  
-ATOM   1298  C   GLU A 258     100.574  85.414 -46.875  1.00 10.16           C  
-ATOM   1299  O   GLU A 258      99.359  85.596 -46.914  1.00 10.36           O  
-ATOM   1300  CB  GLU A 258     101.204  83.733 -45.235  1.00 11.19           C  
-ATOM   1301  CG  GLU A 258     101.885  83.267 -43.965  1.00 12.78           C  
-ATOM   1302  CD  GLU A 258     101.735  81.752 -43.772  1.00 12.65           C  
-ATOM   1303  OE1 GLU A 258     100.871  81.140 -44.441  1.00 14.24           O  
-ATOM   1304  OE2 GLU A 258     102.479  81.184 -42.949  1.00 21.69           O  
-ATOM   1305  N   ASP A 259     101.318  85.312 -47.976  1.00  8.47           N  
-ATOM   1306  CA  ASP A 259     100.648  85.249 -49.283  1.00  7.89           C  
-ATOM   1307  C   ASP A 259     100.124  83.830 -49.550  1.00 10.13           C  
-ATOM   1308  O   ASP A 259     100.240  82.952 -48.692  1.00 10.47           O  
-ATOM   1309  CB  ASP A 259     101.542  85.774 -50.424  1.00  9.08           C  
-ATOM   1310  CG  ASP A 259     102.746  84.878 -50.726  1.00 13.49           C  
-ATOM   1311  OD1 ASP A 259     102.771  83.695 -50.318  1.00 11.24           O  
-ATOM   1312  OD2 ASP A 259     103.674  85.370 -51.415  1.00 14.19           O  
-ATOM   1313  N   SER A 260      99.531  83.599 -50.725  1.00  9.27           N  
-ATOM   1314  CA  SER A 260      98.904  82.304 -50.995  1.00 10.43           C  
-ATOM   1315  C   SER A 260      99.881  81.120 -51.061  1.00 12.94           C  
-ATOM   1316  O   SER A 260      99.457  79.968 -50.949  1.00 11.67           O  
-ATOM   1317  CB  SER A 260      98.085  82.362 -52.287  1.00 12.82           C  
-ATOM   1318  OG  SER A 260      98.910  82.725 -53.381  1.00  9.65           O  
-ATOM   1319  N   SER A 261     101.167  81.408 -51.257  1.00 10.81           N  
-ATOM   1320  CA  SER A 261     102.229  80.403 -51.222  1.00 16.08           C  
-ATOM   1321  C   SER A 261     102.769  80.147 -49.829  1.00 14.16           C  
-ATOM   1322  O   SER A 261     103.564  79.233 -49.635  1.00 14.59           O  
-ATOM   1323  CB  SER A 261     103.428  80.847 -52.065  1.00 17.32           C  
-ATOM   1324  OG  SER A 261     103.170  80.743 -53.445  1.00 16.98           O  
-ATOM   1325  N   GLY A 262     102.386  80.981 -48.866  1.00 10.45           N  
-ATOM   1326  CA  GLY A 262     102.953  80.873 -47.532  1.00 11.03           C  
-ATOM   1327  C   GLY A 262     104.164  81.764 -47.292  1.00 13.10           C  
-ATOM   1328  O   GLY A 262     104.790  81.692 -46.237  1.00 14.38           O  
-ATOM   1329  N   ASN A 263     104.497  82.615 -48.262  1.00 11.03           N  
-ATOM   1330  CA  ASN A 263     105.588  83.571 -48.093  1.00 10.17           C  
-ATOM   1331  C   ASN A 263     105.227  84.693 -47.114  1.00 10.20           C  
-ATOM   1332  O   ASN A 263     104.072  85.129 -47.034  1.00 12.89           O  
-ATOM   1333  CB  ASN A 263     105.982  84.208 -49.429  1.00 12.51           C  
-ATOM   1334  CG  ASN A 263     106.412  83.189 -50.476  1.00 23.45           C  
-ATOM   1335  OD1 ASN A 263     107.271  82.344 -50.224  1.00 23.69           O  
-ATOM   1336  ND2 ASN A 263     105.826  83.286 -51.668  1.00 21.50           N  
-ATOM   1337  N   LEU A 264     106.235  85.181 -46.403  1.00 11.56           N  
-ATOM   1338  CA  LEU A 264     106.051  86.203 -45.368  1.00 11.12           C  
-ATOM   1339  C   LEU A 264     105.621  87.563 -45.910  1.00 12.64           C  
-ATOM   1340  O   LEU A 264     106.285  88.126 -46.782  1.00 12.80           O  
-ATOM   1341  CB  LEU A 264     107.356  86.376 -44.590  1.00 13.92           C  
-ATOM   1342  CG  LEU A 264     107.315  87.452 -43.501  1.00 18.24           C  
-ATOM   1343  CD1 LEU A 264     106.485  86.948 -42.347  1.00 17.85           C  
-ATOM   1344  CD2 LEU A 264     108.726  87.810 -43.028  1.00 20.71           C  
-ATOM   1345  N   LEU A 265     104.522  88.098 -45.375  1.00  9.69           N  
-ATOM   1346  CA  LEU A 265     104.116  89.478 -45.660  1.00  8.41           C  
-ATOM   1347  C   LEU A 265     104.207  90.378 -44.433  1.00  9.16           C  
-ATOM   1348  O   LEU A 265     104.373  91.580 -44.568  1.00 11.51           O  
-ATOM   1349  CB  LEU A 265     102.685  89.543 -46.189  1.00  8.64           C  
-ATOM   1350  CG  LEU A 265     102.411  88.758 -47.478  1.00  9.48           C  
-ATOM   1351  CD1 LEU A 265     100.946  88.858 -47.852  1.00 10.78           C  
-ATOM   1352  CD2 LEU A 265     103.301  89.288 -48.609  1.00 13.61           C  
-ATOM   1353  N   GLY A 266     104.072  89.799 -43.242  1.00  8.42           N  
-ATOM   1354  CA  GLY A 266     104.045  90.598 -42.025  1.00  7.58           C  
-ATOM   1355  C   GLY A 266     104.149  89.674 -40.833  1.00  7.97           C  
-ATOM   1356  O   GLY A 266     103.835  88.494 -40.954  1.00  9.68           O  
-ATOM   1357  N   ARG A 267     104.606  90.196 -39.699  1.00  6.45           N  
-ATOM   1358  CA  ARG A 267     104.742  89.352 -38.500  1.00  7.53           C  
-ATOM   1359  C   ARG A 267     104.603  90.174 -37.227  1.00  8.58           C  
-ATOM   1360  O   ARG A 267     105.066  91.307 -37.162  1.00  8.95           O  
-ATOM   1361  CB  ARG A 267     106.091  88.614 -38.490  1.00 10.98           C  
-ATOM   1362  CG  ARG A 267     106.204  87.586 -37.351  1.00 11.89           C  
-ATOM   1363  CD  ARG A 267     107.636  87.068 -37.157  1.00 16.96           C  
-ATOM   1364  NE  ARG A 267     108.139  86.341 -38.315  1.00 19.48           N  
-ATOM   1365  CZ  ARG A 267     109.045  86.813 -39.166  1.00 19.15           C  
-ATOM   1366  NH1 ARG A 267     109.559  88.021 -38.997  1.00 19.22           N  
-ATOM   1367  NH2 ARG A 267     109.440  86.070 -40.191  1.00 24.12           N  
-ATOM   1368  N   ASP A 268     103.963  89.595 -36.213  1.00  7.85           N  
-ATOM   1369  CA  ASP A 268     103.848  90.243 -34.906  1.00  7.91           C  
-ATOM   1370  C   ASP A 268     103.812  89.085 -33.904  1.00  7.18           C  
-ATOM   1371  O   ASP A 268     103.737  87.927 -34.313  1.00  8.87           O  
-ATOM   1372  CB  ASP A 268     102.578  91.101 -34.840  1.00  6.91           C  
-ATOM   1373  CG  ASP A 268     102.630  92.173 -33.748  1.00  9.62           C  
-ATOM   1374  OD1 ASP A 268     103.492  92.097 -32.840  1.00 10.58           O  
-ATOM   1375  OD2 ASP A 268     101.804  93.111 -33.808  1.00 10.18           O  
-ATOM   1376  N   SER A 269     103.893  89.382 -32.610  1.00  7.79           N  
-ATOM   1377  CA  SER A 269     103.914  88.314 -31.612  1.00  6.50           C  
-ATOM   1378  C   SER A 269     103.602  88.852 -30.222  1.00  7.33           C  
-ATOM   1379  O   SER A 269     103.645  90.061 -29.978  1.00  9.37           O  
-ATOM   1380  CB  SER A 269     105.285  87.627 -31.608  1.00  9.02           C  
-ATOM   1381  OG  SER A 269     106.313  88.537 -31.233  1.00 12.37           O  
-ATOM   1382  N   PHE A 270     103.280  87.944 -29.303  1.00  7.85           N  
-ATOM   1383  CA  PHE A 270     102.990  88.317 -27.920  1.00  7.28           C  
-ATOM   1384  C   PHE A 270     103.183  87.093 -27.037  1.00  7.41           C  
-ATOM   1385  O   PHE A 270     102.962  85.974 -27.475  1.00  7.58           O  
-ATOM   1386  CB  PHE A 270     101.556  88.861 -27.781  1.00  9.69           C  
-ATOM   1387  CG  PHE A 270     100.488  87.947 -28.347  1.00  7.66           C  
-ATOM   1388  CD1 PHE A 270     100.185  87.965 -29.704  1.00  5.64           C  
-ATOM   1389  CD2 PHE A 270      99.767  87.090 -27.517  1.00  8.18           C  
-ATOM   1390  CE1 PHE A 270      99.194  87.125 -30.230  1.00  9.50           C  
-ATOM   1391  CE2 PHE A 270      98.774  86.259 -28.030  1.00  8.84           C  
-ATOM   1392  CZ  PHE A 270      98.491  86.269 -29.386  1.00  8.30           C  
-ATOM   1393  N   GLU A 271     103.611  87.317 -25.798  1.00  7.19           N  
-ATOM   1394  CA  GLU A 271     103.723  86.232 -24.824  1.00  8.27           C  
-ATOM   1395  C   GLU A 271     102.321  85.823 -24.369  1.00  8.55           C  
-ATOM   1396  O   GLU A 271     101.386  86.627 -24.418  1.00  7.56           O  
-ATOM   1397  CB  GLU A 271     104.577  86.678 -23.619  1.00  7.20           C  
-ATOM   1398  CG  GLU A 271     104.798  85.570 -22.574  1.00 13.53           C  
-ATOM   1399  CD  GLU A 271     105.757  85.978 -21.464  1.00 18.92           C  
-ATOM   1400  OE1 GLU A 271     106.412  87.035 -21.601  1.00 18.88           O  
-ATOM   1401  OE2 GLU A 271     105.850  85.232 -20.456  1.00 17.85           O  
-ATOM   1402  N   VAL A 272     102.178  84.578 -23.918  1.00  8.22           N  
-ATOM   1403  CA  VAL A 272     100.892  84.081 -23.437  1.00  6.49           C  
-ATOM   1404  C   VAL A 272     101.094  83.307 -22.145  1.00  8.34           C  
-ATOM   1405  O   VAL A 272     102.045  82.530 -22.029  1.00 11.91           O  
-ATOM   1406  CB  VAL A 272     100.229  83.147 -24.472  1.00  9.23           C  
-ATOM   1407  CG1 VAL A 272      98.922  82.588 -23.938  1.00  9.93           C  
-ATOM   1408  CG2 VAL A 272      99.986  83.906 -25.776  1.00 11.42           C  
-ATOM   1409  N   ARG A 273     100.211  83.544 -21.177  1.00  7.36           N  
-ATOM   1410  CA  ARG A 273     100.098  82.702 -19.986  1.00  7.55           C  
-ATOM   1411  C   ARG A 273      98.657  82.248 -19.875  1.00  9.21           C  
-ATOM   1412  O   ARG A 273      97.737  83.078 -19.825  1.00  8.47           O  
-ATOM   1413  CB  ARG A 273     100.473  83.479 -18.714  1.00  7.49           C  
-ATOM   1414  CG  ARG A 273     100.160  82.721 -17.406  1.00 11.23           C  
-ATOM   1415  CD  ARG A 273     100.576  83.538 -16.189  1.00 15.07           C  
-ATOM   1416  NE  ARG A 273     100.211  82.883 -14.933  1.00 16.94           N  
-ATOM   1417  CZ  ARG A 273     100.924  81.921 -14.360  1.00 26.53           C  
-ATOM   1418  NH1 ARG A 273     102.038  81.492 -14.938  1.00 32.05           N  
-ATOM   1419  NH2 ARG A 273     100.521  81.389 -13.208  1.00 25.87           N  
-ATOM   1420  N   VAL A 274      98.461  80.933 -19.850  1.00  8.68           N  
-ATOM   1421  CA  VAL A 274      97.126  80.370 -19.717  1.00  8.97           C  
-ATOM   1422  C   VAL A 274      97.002  79.934 -18.268  1.00  9.07           C  
-ATOM   1423  O   VAL A 274      97.785  79.107 -17.798  1.00 10.63           O  
-ATOM   1424  CB  VAL A 274      96.928  79.152 -20.629  1.00  8.69           C  
-ATOM   1425  CG1 VAL A 274      95.472  78.684 -20.563  1.00 10.47           C  
-ATOM   1426  CG2 VAL A 274      97.351  79.464 -22.073  1.00  8.56           C  
-ATOM   1427  N   CYS A 275      96.045  80.518 -17.552  1.00  7.82           N  
-ATOM   1428  CA  CYS A 275      96.004  80.377 -16.099  1.00 10.65           C  
-ATOM   1429  C   CYS A 275      94.581  80.512 -15.572  1.00 13.68           C  
-ATOM   1430  O   CYS A 275      93.679  80.935 -16.293  1.00 13.10           O  
-ATOM   1431  CB  CYS A 275      96.904  81.433 -15.444  1.00 13.05           C  
-ATOM   1432  SG  CYS A 275      96.541  83.139 -15.921  1.00 14.95           S  
-ATOM   1433  N   ALA A 276      94.388  80.176 -14.299  1.00 12.83           N  
-ATOM   1434  CA  ALA A 276      93.059  80.206 -13.703  1.00 15.69           C  
-ATOM   1435  C   ALA A 276      92.529  81.615 -13.431  1.00 14.07           C  
-ATOM   1436  O   ALA A 276      91.324  81.851 -13.514  1.00 16.16           O  
-ATOM   1437  CB  ALA A 276      93.050  79.389 -12.413  1.00 16.41           C  
-ATOM   1438  N   CYS A 277      93.423  82.540 -13.085  1.00 16.22           N  
-ATOM   1439  C   CYS A 277      93.870  84.944 -13.473  1.00 14.02           C  
-ATOM   1440  O   CYS A 277      94.781  85.539 -12.891  1.00 13.79           O  
-ATOM   1441  CA ACYS A 277      93.022  83.901 -12.746  0.53 15.18           C  
-ATOM   1442  CB ACYS A 277      93.113  84.128 -11.238  0.53 15.12           C  
-ATOM   1443  SG ACYS A 277      92.251  85.605 -10.667  0.53 16.48           S  
-ATOM   1444  CA BCYS A 277      93.034  83.904 -12.732  0.47 15.18           C  
-ATOM   1445  CB BCYS A 277      93.204  84.139 -11.229  0.47 15.12           C  
-ATOM   1446  SG BCYS A 277      92.437  82.901 -10.162  0.47 22.16           S  
-ATOM   1447  N   PRO A 278      93.559  85.178 -14.750  1.00 13.33           N  
-ATOM   1448  CA  PRO A 278      94.315  86.118 -15.588  1.00 12.52           C  
-ATOM   1449  C   PRO A 278      94.407  87.523 -14.997  1.00 11.77           C  
-ATOM   1450  O   PRO A 278      95.460  88.152 -15.096  1.00 12.63           O  
-ATOM   1451  CB  PRO A 278      93.508  86.157 -16.893  1.00 11.56           C  
-ATOM   1452  CG  PRO A 278      92.755  84.882 -16.926  1.00 14.48           C  
-ATOM   1453  CD  PRO A 278      92.512  84.461 -15.501  1.00 11.93           C  
-ATOM   1454  N   GLY A 279      93.322  88.014 -14.405  1.00 12.49           N  
-ATOM   1455  CA  GLY A 279      93.318  89.355 -13.833  1.00 14.23           C  
-ATOM   1456  C   GLY A 279      94.347  89.504 -12.728  1.00 14.93           C  
-ATOM   1457  O   GLY A 279      95.139  90.451 -12.712  1.00 15.99           O  
-ATOM   1458  N   ARG A 280      94.335  88.563 -11.793  1.00 15.47           N  
-ATOM   1459  CA  ARG A 280      95.278  88.600 -10.684  1.00 16.87           C  
-ATOM   1460  C   ARG A 280      96.714  88.443 -11.174  1.00 16.12           C  
-ATOM   1461  O   ARG A 280      97.607  89.168 -10.743  1.00 17.49           O  
-ATOM   1462  CB  ARG A 280      94.945  87.515  -9.655  1.00 21.39           C  
-ATOM   1463  CG  ARG A 280      95.843  87.517  -8.425  1.00 29.05           C  
-ATOM   1464  CD  ARG A 280      95.764  86.170  -7.705  1.00 36.25           C  
-ATOM   1465  NE  ARG A 280      96.138  85.080  -8.607  1.00 41.45           N  
-ATOM   1466  CZ  ARG A 280      96.019  83.787  -8.321  1.00 45.14           C  
-ATOM   1467  NH1 ARG A 280      95.530  83.405  -7.147  1.00 40.90           N  
-ATOM   1468  NH2 ARG A 280      96.387  82.875  -9.214  1.00 38.67           N  
-ATOM   1469  N   ASP A 281      96.946  87.499 -12.078  1.00 12.60           N  
-ATOM   1470  CA  ASP A 281      98.305  87.267 -12.545  1.00 11.70           C  
-ATOM   1471  C   ASP A 281      98.837  88.461 -13.341  1.00 15.93           C  
-ATOM   1472  O   ASP A 281     100.018  88.797 -13.238  1.00 16.76           O  
-ATOM   1473  CB  ASP A 281      98.418  85.961 -13.347  1.00 12.20           C  
-ATOM   1474  CG  ASP A 281      98.268  84.723 -12.476  1.00 20.70           C  
-ATOM   1475  OD1 ASP A 281      98.285  84.862 -11.231  1.00 21.66           O  
-ATOM   1476  OD2 ASP A 281      98.137  83.612 -13.029  1.00 19.74           O  
-ATOM   1477  N   ARG A 282      97.985  89.102 -14.138  1.00 13.26           N  
-ATOM   1478  CA  ARG A 282      98.437  90.299 -14.848  1.00 11.67           C  
-ATOM   1479  C   ARG A 282      98.815  91.399 -13.852  1.00 17.44           C  
-ATOM   1480  O   ARG A 282      99.853  92.049 -13.998  1.00 15.78           O  
-ATOM   1481  CB  ARG A 282      97.380  90.822 -15.826  1.00 10.81           C  
-ATOM   1482  CG  ARG A 282      97.780  92.146 -16.481  1.00  9.82           C  
-ATOM   1483  CD  ARG A 282      96.748  92.676 -17.505  1.00  9.03           C  
-ATOM   1484  NE  ARG A 282      97.053  94.064 -17.860  1.00 10.72           N  
-ATOM   1485  CZ  ARG A 282      96.210  94.918 -18.439  1.00 11.16           C  
-ATOM   1486  NH1 ARG A 282      94.977  94.551 -18.771  1.00 10.78           N  
-ATOM   1487  NH2 ARG A 282      96.606  96.162 -18.682  1.00 13.75           N  
-ATOM   1488  N   ARG A 283      97.982  91.597 -12.832  1.00 15.14           N  
-ATOM   1489  CA  ARG A 283      98.269  92.619 -11.823  1.00 21.41           C  
-ATOM   1490  C   ARG A 283      99.601  92.344 -11.124  1.00 20.54           C  
-ATOM   1491  O   ARG A 283     100.432  93.243 -10.961  1.00 21.31           O  
-ATOM   1492  CB  ARG A 283      97.130  92.713 -10.807  1.00 18.47           C  
-ATOM   1493  CG  ARG A 283      96.044  93.721 -11.174  1.00 24.29           C  
-ATOM   1494  CD  ARG A 283      94.959  93.814 -10.091  1.00 26.96           C  
-ATOM   1495  NE  ARG A 283      93.931  92.780 -10.236  1.00 27.08           N  
-ATOM   1496  CZ  ARG A 283      93.697  91.815  -9.349  1.00 31.03           C  
-ATOM   1497  NH1 ARG A 283      94.412  91.739  -8.230  1.00 32.40           N  
-ATOM   1498  NH2 ARG A 283      92.737  90.926  -9.577  1.00 28.38           N  
-ATOM   1499  N   THR A 284      99.796  91.092 -10.728  1.00 21.06           N  
-ATOM   1500  CA  THR A 284     101.036  90.640 -10.109  1.00 19.71           C  
-ATOM   1501  C   THR A 284     102.267  90.874 -10.983  1.00 22.61           C  
-ATOM   1502  O   THR A 284     103.240  91.477 -10.535  1.00 23.55           O  
-ATOM   1503  CB  THR A 284     100.947  89.147  -9.736  1.00 22.42           C  
-ATOM   1504  OG1 THR A 284      99.912  88.963  -8.758  1.00 23.13           O  
-ATOM   1505  CG2 THR A 284     102.276  88.641  -9.179  1.00 28.63           C  
-ATOM   1506  N   GLU A 285     102.226  90.411 -12.232  1.00 18.58           N  
-ATOM   1507  CA  GLU A 285     103.391  90.531 -13.103  1.00 18.07           C  
-ATOM   1508  C   GLU A 285     103.690  91.981 -13.469  1.00 19.34           C  
-ATOM   1509  O   GLU A 285     104.854  92.345 -13.652  1.00 20.35           O  
-ATOM   1510  CB  GLU A 285     103.258  89.649 -14.357  1.00 18.71           C  
-ATOM   1511  CG  GLU A 285     103.111  88.170 -14.017  1.00 21.90           C  
-ATOM   1512  CD  GLU A 285     103.314  87.245 -15.203  1.00 22.62           C  
-ATOM   1513  OE1 GLU A 285     103.876  87.684 -16.228  1.00 18.61           O  
-ATOM   1514  OE2 GLU A 285     102.926  86.063 -15.093  1.00 21.99           O  
-ATOM   1515  N   GLU A 286     102.648  92.804 -13.567  1.00 17.20           N  
-ATOM   1516  CA  GLU A 286     102.843  94.221 -13.865  1.00 14.18           C  
-ATOM   1517  C   GLU A 286     103.463  94.916 -12.654  1.00 23.63           C  
-ATOM   1518  O   GLU A 286     104.305  95.797 -12.801  1.00 24.48           O  
-ATOM   1519  CB  GLU A 286     101.538  94.903 -14.290  1.00 16.44           C  
-ATOM   1520  CG  GLU A 286     101.069  94.477 -15.693  1.00 17.49           C  
-ATOM   1521  CD  GLU A 286      99.960  95.352 -16.279  1.00 19.48           C  
-ATOM   1522  OE1 GLU A 286      99.419  96.235 -15.570  1.00 20.93           O  
-ATOM   1523  OE2 GLU A 286      99.640  95.160 -17.473  1.00 15.26           O  
-ATOM   1524  N   GLU A 287     103.056  94.505 -11.458  1.00 23.06           N  
-ATOM   1525  CA  GLU A 287     103.638  95.078 -10.245  1.00 28.99           C  
-ATOM   1526  C   GLU A 287     105.111  94.705 -10.127  1.00 30.98           C  
-ATOM   1527  O   GLU A 287     105.953  95.560  -9.845  1.00 33.94           O  
-ATOM   1528  CB  GLU A 287     102.871  94.642  -8.996  1.00 33.39           C  
-ATOM   1529  CG  GLU A 287     103.373  95.310  -7.722  1.00 39.73           C  
-ATOM   1530  CD  GLU A 287     103.499  96.822  -7.861  1.00 45.71           C  
-ATOM   1531  OE1 GLU A 287     102.649  97.440  -8.541  1.00 48.45           O  
-ATOM   1532  OE2 GLU A 287     104.449  97.395  -7.285  1.00 56.15           O  
-ATOM   1533  N   ASN A 288     105.417  93.431 -10.357  1.00 24.76           N  
-ATOM   1534  CA  ASN A 288     106.803  92.973 -10.375  1.00 31.56           C  
-ATOM   1535  C   ASN A 288     107.661  93.802 -11.330  1.00 33.94           C  
-ATOM   1536  O   ASN A 288     108.749  94.247 -10.972  1.00 33.99           O  
-ATOM   1537  CB  ASN A 288     106.888  91.486 -10.740  1.00 24.83           C  
-ATOM   1538  CG  ASN A 288     106.360  90.576  -9.635  1.00 37.68           C  
-ATOM   1539  OD1 ASN A 288     106.017  91.034  -8.544  1.00 39.93           O  
-ATOM   1540  ND2 ASN A 288     106.298  89.279  -9.916  1.00 37.35           N  
-ATOM   1541  N   LEU A 289     107.167  94.010 -12.547  1.00 28.20           N  
-ATOM   1542  CA  LEU A 289     107.897  94.800 -13.536  1.00 28.42           C  
-ATOM   1543  C   LEU A 289     108.283  96.187 -13.003  1.00 34.07           C  
-ATOM   1544  O   LEU A 289     109.423  96.620 -13.166  1.00 34.53           O  
-ATOM   1545  CB  LEU A 289     107.094  94.916 -14.837  1.00 27.17           C  
-ATOM   1546  CG  LEU A 289     107.719  95.739 -15.967  1.00 29.13           C  
-ATOM   1547  CD1 LEU A 289     109.048  95.129 -16.393  1.00 26.03           C  
-ATOM   1548  CD2 LEU A 289     106.758  95.843 -17.151  1.00 25.62           C  
-ATOM   1549  N   ARG A 290     107.339  96.877 -12.367  1.00 32.30           N  
-ATOM   1550  CA  ARG A 290     107.627  98.180 -11.767  1.00 40.56           C  
-ATOM   1551  C   ARG A 290     108.915  98.161 -10.946  1.00 44.41           C  
-ATOM   1552  O   ARG A 290     108.967  97.572  -9.866  1.00 49.75           O  
-ATOM   1553  CB  ARG A 290     106.468  98.643 -10.884  1.00 44.35           C  
-ATOM   1554  CG  ARG A 290     105.335  99.309 -11.635  1.00 46.13           C  
-ATOM   1555  CD  ARG A 290     104.265  99.799 -10.670  1.00 54.41           C  
-ATOM   1556  NE  ARG A 290     103.200 100.523 -11.358  1.00 58.82           N  
-ATOM   1557  CZ  ARG A 290     103.128 101.849 -11.441  1.00 64.28           C  
-ATOM   1558  NH1 ARG A 290     104.057 102.610 -10.873  1.00 66.38           N  
-ATOM   1559  NH2 ARG A 290     102.120 102.415 -12.089  1.00 59.50           N  
-TER    1560      ARG A 290                                                      
-ATOM   1561  N   SER B  94     146.626  76.516 -31.350  1.00 37.79           N  
-ATOM   1562  CA  SER B  94     146.659  77.974 -31.387  1.00 33.04           C  
-ATOM   1563  C   SER B  94     146.369  78.506 -32.783  1.00 33.68           C  
-ATOM   1564  O   SER B  94     146.525  77.792 -33.779  1.00 29.68           O  
-ATOM   1565  CB  SER B  94     148.011  78.497 -30.897  1.00 27.59           C  
-ATOM   1566  OG  SER B  94     148.201  78.170 -29.533  1.00 41.10           O  
-ATOM   1567  N   SER B  95     145.943  79.765 -32.848  1.00 26.36           N  
-ATOM   1568  CA  SER B  95     145.581  80.382 -34.122  1.00 30.31           C  
-ATOM   1569  C   SER B  95     146.196  81.770 -34.249  1.00 30.64           C  
-ATOM   1570  O   SER B  95     146.449  82.429 -33.243  1.00 25.74           O  
-ATOM   1571  CB  SER B  95     144.058  80.474 -34.249  1.00 28.60           C  
-ATOM   1572  OG  SER B  95     143.467  79.199 -34.072  1.00 27.74           O  
-ATOM   1573  N   SER B  96     146.444  82.207 -35.484  1.00 28.63           N  
-ATOM   1574  CA  SER B  96     146.941  83.562 -35.725  1.00 27.87           C  
-ATOM   1575  C   SER B  96     145.980  84.582 -35.119  1.00 30.17           C  
-ATOM   1576  O   SER B  96     144.791  84.294 -34.943  1.00 29.50           O  
-ATOM   1577  CB  SER B  96     147.104  83.824 -37.226  1.00 27.07           C  
-ATOM   1578  OG  SER B  96     145.861  83.691 -37.887  1.00 29.30           O  
-ATOM   1579  N   VAL B  97     146.493  85.771 -34.813  1.00 21.12           N  
-ATOM   1580  CA  VAL B  97     145.720  86.767 -34.078  1.00 16.93           C  
-ATOM   1581  C   VAL B  97     145.230  87.882 -34.994  1.00 19.47           C  
-ATOM   1582  O   VAL B  97     146.029  88.596 -35.588  1.00 19.36           O  
-ATOM   1583  CB  VAL B  97     146.542  87.387 -32.929  1.00 16.77           C  
-ATOM   1584  CG1 VAL B  97     145.666  88.322 -32.103  1.00 19.78           C  
-ATOM   1585  CG2 VAL B  97     147.140  86.292 -32.045  1.00 18.68           C  
-ATOM   1586  N   PRO B  98     143.906  88.037 -35.104  1.00 15.56           N  
-ATOM   1587  CA  PRO B  98     143.338  89.084 -35.956  1.00 15.72           C  
-ATOM   1588  C   PRO B  98     143.702  90.456 -35.403  1.00 15.09           C  
-ATOM   1589  O   PRO B  98     143.763  90.633 -34.189  1.00 14.61           O  
-ATOM   1590  CB  PRO B  98     141.823  88.863 -35.820  1.00 17.18           C  
-ATOM   1591  CG  PRO B  98     141.666  87.498 -35.253  1.00 23.29           C  
-ATOM   1592  CD  PRO B  98     142.866  87.257 -34.413  1.00 21.10           C  
-ATOM   1593  N   SER B  99     143.923  91.423 -36.286  1.00 12.86           N  
-ATOM   1594  CA  SER B  99     144.251  92.771 -35.848  1.00 17.01           C  
-ATOM   1595  C   SER B  99     143.086  93.400 -35.100  1.00 13.72           C  
-ATOM   1596  O   SER B  99     141.930  93.157 -35.434  1.00 12.66           O  
-ATOM   1597  CB  SER B  99     144.609  93.648 -37.052  1.00 18.00           C  
-ATOM   1598  OG  SER B  99     144.708  95.006 -36.658  1.00 17.84           O  
-ATOM   1599  N   GLN B 100     143.396  94.211 -34.092  1.00 13.09           N  
-ATOM   1600  CA  GLN B 100     142.372  94.983 -33.394  1.00 14.09           C  
-ATOM   1601  C   GLN B 100     142.578  96.480 -33.606  1.00 16.62           C  
-ATOM   1602  O   GLN B 100     141.997  97.293 -32.894  1.00 16.83           O  
-ATOM   1603  CB  GLN B 100     142.384  94.671 -31.896  1.00 16.33           C  
-ATOM   1604  CG  GLN B 100     143.673  95.089 -31.191  1.00 16.72           C  
-ATOM   1605  CD  GLN B 100     143.665  94.749 -29.712  1.00 23.34           C  
-ATOM   1606  OE1 GLN B 100     144.057  93.653 -29.313  1.00 28.85           O  
-ATOM   1607  NE2 GLN B 100     143.222  95.690 -28.894  1.00 22.21           N  
-ATOM   1608  N   LYS B 101     143.399  96.847 -34.586  1.00 13.89           N  
-ATOM   1609  CA  LYS B 101     143.735  98.256 -34.798  1.00 15.10           C  
-ATOM   1610  C   LYS B 101     142.590  99.059 -35.409  1.00 13.27           C  
-ATOM   1611  O   LYS B 101     142.055  98.698 -36.457  1.00 13.51           O  
-ATOM   1612  CB  LYS B 101     144.956  98.378 -35.707  1.00 17.11           C  
-ATOM   1613  CG  LYS B 101     146.189  97.639 -35.213  1.00 26.84           C  
-ATOM   1614  CD  LYS B 101     147.027  98.504 -34.279  1.00 34.53           C  
-ATOM   1615  CE  LYS B 101     148.435  97.927 -34.117  1.00 39.24           C  
-ATOM   1616  NZ  LYS B 101     149.255  98.721 -33.156  1.00 51.23           N  
-ATOM   1617  N   THR B 102     142.245 100.173 -34.773  1.00 11.84           N  
-ATOM   1618  CA  THR B 102     141.217 101.060 -35.295  1.00 11.61           C  
-ATOM   1619  C   THR B 102     141.613 101.601 -36.663  1.00 13.59           C  
-ATOM   1620  O   THR B 102     142.742 102.053 -36.858  1.00 14.43           O  
-ATOM   1621  CB  THR B 102     140.959 102.233 -34.333  1.00 13.57           C  
-ATOM   1622  OG1 THR B 102     140.558 101.711 -33.062  1.00 15.33           O  
-ATOM   1623  CG2 THR B 102     139.861 103.133 -34.864  1.00 11.22           C  
-ATOM   1624  N   TYR B 103     140.675 101.555 -37.604  1.00  9.75           N  
-ATOM   1625  CA  TYR B 103     140.945 101.914 -38.990  1.00 11.38           C  
-ATOM   1626  C   TYR B 103     139.643 102.367 -39.641  1.00 14.11           C  
-ATOM   1627  O   TYR B 103     138.790 101.548 -39.978  1.00 11.17           O  
-ATOM   1628  CB  TYR B 103     141.536 100.704 -39.735  1.00 13.48           C  
-ATOM   1629  CG  TYR B 103     141.889 100.992 -41.183  1.00 14.08           C  
-ATOM   1630  CD1 TYR B 103     142.987 101.783 -41.500  1.00 21.92           C  
-ATOM   1631  CD2 TYR B 103     141.125 100.476 -42.222  1.00 17.95           C  
-ATOM   1632  CE1 TYR B 103     143.313 102.059 -42.815  1.00 22.79           C  
-ATOM   1633  CE2 TYR B 103     141.451 100.745 -43.552  1.00 20.40           C  
-ATOM   1634  CZ  TYR B 103     142.546 101.535 -43.833  1.00 24.92           C  
-ATOM   1635  OH  TYR B 103     142.883 101.818 -45.146  1.00 27.57           O  
-ATOM   1636  N   GLN B 104     139.467 103.676 -39.805  1.00 10.82           N  
-ATOM   1637  CA  GLN B 104     138.211 104.173 -40.360  1.00  9.78           C  
-ATOM   1638  C   GLN B 104     138.043 103.871 -41.843  1.00 13.44           C  
-ATOM   1639  O   GLN B 104     136.919 103.715 -42.321  1.00 10.84           O  
-ATOM   1640  CB  GLN B 104     138.056 105.674 -40.114  1.00 10.44           C  
-ATOM   1641  CG  GLN B 104     137.800 106.017 -38.660  1.00 12.21           C  
-ATOM   1642  CD  GLN B 104     137.064 107.340 -38.503  1.00 17.49           C  
-ATOM   1643  OE1 GLN B 104     136.953 108.119 -39.454  1.00 17.66           O  
-ATOM   1644  NE2 GLN B 104     136.546 107.592 -37.307  1.00 17.72           N  
-ATOM   1645  N   GLY B 105     139.153 103.817 -42.573  1.00 12.86           N  
-ATOM   1646  CA  GLY B 105     139.090 103.492 -43.986  1.00 14.15           C  
-ATOM   1647  C   GLY B 105     138.426 104.584 -44.808  1.00 15.30           C  
-ATOM   1648  O   GLY B 105     138.156 105.689 -44.309  1.00 12.87           O  
-ATOM   1649  N   SER B 106     138.140 104.267 -46.068  1.00 12.86           N  
-ATOM   1650  CA  SER B 106     137.660 105.259 -47.033  1.00 12.34           C  
-ATOM   1651  C   SER B 106     136.271 105.803 -46.725  1.00 14.15           C  
-ATOM   1652  O   SER B 106     135.923 106.904 -47.168  1.00 17.23           O  
-ATOM   1653  CB  SER B 106     137.646 104.656 -48.449  1.00 12.95           C  
-ATOM   1654  OG  SER B 106     138.941 104.214 -48.819  1.00 27.45           O  
-ATOM   1655  N   TYR B 107     135.473 105.030 -45.989  1.00 10.67           N  
-ATOM   1656  CA  TYR B 107     134.088 105.411 -45.720  1.00  9.59           C  
-ATOM   1657  C   TYR B 107     133.894 106.058 -44.354  1.00 10.92           C  
-ATOM   1658  O   TYR B 107     132.784 106.444 -44.018  1.00 13.45           O  
-ATOM   1659  CB  TYR B 107     133.147 104.211 -45.880  1.00 10.43           C  
-ATOM   1660  CG  TYR B 107     133.268 103.625 -47.259  1.00 12.74           C  
-ATOM   1661  CD1 TYR B 107     132.677 104.254 -48.341  1.00 13.49           C  
-ATOM   1662  CD2 TYR B 107     134.012 102.479 -47.486  1.00 14.13           C  
-ATOM   1663  CE1 TYR B 107     132.804 103.746 -49.621  1.00 14.87           C  
-ATOM   1664  CE2 TYR B 107     134.142 101.958 -48.771  1.00 16.05           C  
-ATOM   1665  CZ  TYR B 107     133.538 102.605 -49.828  1.00 17.28           C  
-ATOM   1666  OH  TYR B 107     133.657 102.101 -51.109  1.00 20.69           O  
-ATOM   1667  N   GLY B 108     134.973 106.173 -43.581  1.00  9.92           N  
-ATOM   1668  CA  GLY B 108     134.909 106.826 -42.283  1.00 11.69           C  
-ATOM   1669  C   GLY B 108     134.110 106.006 -41.291  1.00 13.84           C  
-ATOM   1670  O   GLY B 108     133.240 106.526 -40.581  1.00 10.26           O  
-ATOM   1671  N   PHE B 109     134.409 104.712 -41.253  1.00  9.34           N  
-ATOM   1672  CA  PHE B 109     133.660 103.764 -40.421  1.00  8.97           C  
-ATOM   1673  C   PHE B 109     134.061 103.809 -38.947  1.00 10.91           C  
-ATOM   1674  O   PHE B 109     135.250 103.746 -38.618  1.00  9.36           O  
-ATOM   1675  CB  PHE B 109     133.890 102.352 -40.968  1.00  8.00           C  
-ATOM   1676  CG  PHE B 109     133.280 101.265 -40.131  1.00  6.88           C  
-ATOM   1677  CD1 PHE B 109     131.912 101.059 -40.141  1.00  6.99           C  
-ATOM   1678  CD2 PHE B 109     134.082 100.430 -39.354  1.00  8.81           C  
-ATOM   1679  CE1 PHE B 109     131.346 100.043 -39.371  1.00 12.50           C  
-ATOM   1680  CE2 PHE B 109     133.525  99.415 -38.589  1.00 10.07           C  
-ATOM   1681  CZ  PHE B 109     132.163  99.221 -38.599  1.00 10.94           C  
-ATOM   1682  N   ARG B 110     133.065 103.890 -38.061  1.00  8.03           N  
-ATOM   1683  CA  ARG B 110     133.298 103.751 -36.620  1.00  8.02           C  
-ATOM   1684  C   ARG B 110     132.020 103.314 -35.906  1.00  8.02           C  
-ATOM   1685  O   ARG B 110     130.928 103.441 -36.448  1.00  9.34           O  
-ATOM   1686  CB  ARG B 110     133.819 105.061 -36.002  1.00 10.16           C  
-ATOM   1687  CG  ARG B 110     132.802 106.197 -35.931  1.00 11.22           C  
-ATOM   1688  CD  ARG B 110     132.682 106.943 -37.273  1.00  8.58           C  
-ATOM   1689  NE  ARG B 110     131.815 108.112 -37.131  1.00 10.59           N  
-ATOM   1690  CZ  ARG B 110     131.467 108.906 -38.139  1.00 16.07           C  
-ATOM   1691  NH1 ARG B 110     131.907 108.647 -39.364  1.00 13.00           N  
-ATOM   1692  NH2 ARG B 110     130.674 109.956 -37.923  1.00 15.08           N  
-ATOM   1693  N   LEU B 111     132.165 102.788 -34.687  1.00  7.29           N  
-ATOM   1694  CA  LEU B 111     131.016 102.338 -33.910  1.00  5.61           C  
-ATOM   1695  C   LEU B 111     130.413 103.439 -33.045  1.00  8.92           C  
-ATOM   1696  O   LEU B 111     131.024 104.481 -32.829  1.00 10.00           O  
-ATOM   1697  CB  LEU B 111     131.421 101.170 -33.002  1.00  5.23           C  
-ATOM   1698  CG  LEU B 111     132.062  99.993 -33.740  1.00  5.10           C  
-ATOM   1699  CD1 LEU B 111     132.555  98.973 -32.693  1.00  6.55           C  
-ATOM   1700  CD2 LEU B 111     131.073  99.362 -34.707  1.00  6.42           C  
-ATOM   1701  N   GLY B 112     129.214 103.177 -32.530  1.00  8.12           N  
-ATOM   1702  CA  GLY B 112     128.596 104.040 -31.537  1.00  8.36           C  
-ATOM   1703  C   GLY B 112     127.750 103.224 -30.580  1.00 10.41           C  
-ATOM   1704  O   GLY B 112     127.332 102.117 -30.913  1.00  8.61           O  
-ATOM   1705  N   PHE B 113     127.495 103.767 -29.390  1.00  8.58           N  
-ATOM   1706  CA  PHE B 113     126.721 103.043 -28.391  1.00  9.53           C  
-ATOM   1707  C   PHE B 113     125.693 103.975 -27.752  1.00 10.69           C  
-ATOM   1708  O   PHE B 113     125.916 105.190 -27.672  1.00 12.95           O  
-ATOM   1709  CB  PHE B 113     127.652 102.469 -27.314  1.00 10.42           C  
-ATOM   1710  CG  PHE B 113     128.684 101.522 -27.860  1.00 10.00           C  
-ATOM   1711  CD1 PHE B 113     129.858 102.008 -28.416  1.00 11.09           C  
-ATOM   1712  CD2 PHE B 113     128.468 100.149 -27.835  1.00  9.96           C  
-ATOM   1713  CE1 PHE B 113     130.812 101.139 -28.948  1.00 10.55           C  
-ATOM   1714  CE2 PHE B 113     129.416  99.271 -28.359  1.00  8.55           C  
-ATOM   1715  CZ  PHE B 113     130.589  99.765 -28.911  1.00 10.24           C  
-ATOM   1716  N   LEU B 114     124.568 103.407 -27.326  1.00 13.12           N  
-ATOM   1717  CA  LEU B 114     123.541 104.174 -26.626  1.00 14.50           C  
-ATOM   1718  C   LEU B 114     124.081 104.608 -25.281  1.00 14.99           C  
-ATOM   1719  O   LEU B 114     125.080 104.068 -24.798  1.00 14.53           O  
-ATOM   1720  CB  LEU B 114     122.280 103.329 -26.420  1.00 15.86           C  
-ATOM   1721  CG  LEU B 114     121.542 102.892 -27.686  1.00 18.99           C  
-ATOM   1722  CD1 LEU B 114     120.347 102.025 -27.327  1.00 19.65           C  
-ATOM   1723  CD2 LEU B 114     121.105 104.112 -28.488  1.00 20.70           C  
-ATOM   1724  N   HIS B 115     123.424 105.585 -24.669  1.00 13.45           N  
-ATOM   1725  CA  HIS B 115     123.766 105.976 -23.313  1.00 14.39           C  
-ATOM   1726  C   HIS B 115     122.699 105.444 -22.365  1.00 19.84           C  
-ATOM   1727  O   HIS B 115     121.671 106.085 -22.139  1.00 21.72           O  
-ATOM   1728  CB  HIS B 115     123.938 107.497 -23.232  1.00 12.32           C  
-ATOM   1729  CG  HIS B 115     125.045 108.000 -24.104  1.00 11.60           C  
-ATOM   1730  ND1 HIS B 115     124.860 108.318 -25.431  1.00 16.29           N  
-ATOM   1731  CD2 HIS B 115     126.366 108.168 -23.857  1.00 13.85           C  
-ATOM   1732  CE1 HIS B 115     126.014 108.685 -25.959  1.00 14.59           C  
-ATOM   1733  NE2 HIS B 115     126.943 108.606 -25.024  1.00 12.41           N  
-ATOM   1734  N   SER B 116     122.951 104.251 -21.828  1.00 15.27           N  
-ATOM   1735  CA  SER B 116     121.927 103.503 -21.095  1.00 16.00           C  
-ATOM   1736  C   SER B 116     121.984 103.659 -19.579  1.00 17.21           C  
-ATOM   1737  O   SER B 116     121.078 103.209 -18.880  1.00 18.50           O  
-ATOM   1738  CB  SER B 116     121.999 102.017 -21.461  1.00 18.34           C  
-ATOM   1739  OG  SER B 116     121.758 101.847 -22.848  1.00 20.87           O  
-ATOM   1740  N   GLY B 117     123.042 104.280 -19.073  1.00 15.69           N  
-ATOM   1741  CA  GLY B 117     123.170 104.508 -17.636  1.00 16.28           C  
-ATOM   1742  C   GLY B 117     123.588 103.265 -16.864  1.00 16.26           C  
-ATOM   1743  O   GLY B 117     123.948 102.245 -17.457  1.00 18.11           O  
-ATOM   1744  N   THR B 118     123.531 103.338 -15.537  1.00 15.66           N  
-ATOM   1745  CA  THR B 118     124.072 102.274 -14.704  1.00 15.97           C  
-ATOM   1746  C   THR B 118     123.097 101.791 -13.624  1.00 18.16           C  
-ATOM   1747  O   THR B 118     123.517 101.240 -12.609  1.00 20.98           O  
-ATOM   1748  CB  THR B 118     125.393 102.706 -14.036  1.00 20.41           C  
-ATOM   1749  OG1 THR B 118     125.160 103.865 -13.227  1.00 26.14           O  
-ATOM   1750  CG2 THR B 118     126.442 103.043 -15.094  1.00 21.48           C  
-ATOM   1751  N   ALA B 119     121.802 101.978 -13.862  1.00 18.61           N  
-ATOM   1752  CA  ALA B 119     120.780 101.482 -12.941  1.00 24.58           C  
-ATOM   1753  C   ALA B 119     120.889  99.968 -12.779  1.00 31.14           C  
-ATOM   1754  O   ALA B 119     121.240  99.257 -13.724  1.00 25.58           O  
-ATOM   1755  CB  ALA B 119     119.393 101.866 -13.428  1.00 24.93           C  
-ATOM   1756  N   LYS B 120     120.584  99.474 -11.581  1.00 29.37           N  
-ATOM   1757  CA  LYS B 120     120.715  98.047 -11.296  1.00 33.18           C  
-ATOM   1758  C   LYS B 120     119.994  97.173 -12.322  1.00 27.67           C  
-ATOM   1759  O   LYS B 120     120.415  96.046 -12.587  1.00 34.46           O  
-ATOM   1760  CB  LYS B 120     120.212  97.726  -9.883  1.00 36.03           C  
-ATOM   1761  CG  LYS B 120     121.052  98.341  -8.770  1.00 49.61           C  
-ATOM   1762  CD  LYS B 120     120.507  97.977  -7.395  1.00 53.58           C  
-ATOM   1763  CE  LYS B 120     121.324  98.625  -6.287  1.00 55.67           C  
-ATOM   1764  NZ  LYS B 120     120.836  98.226  -4.935  1.00 57.82           N  
-ATOM   1765  N   SER B 121     118.917  97.696 -12.903  1.00 28.59           N  
-ATOM   1766  CA  SER B 121     118.103  96.929 -13.845  1.00 25.92           C  
-ATOM   1767  C   SER B 121     118.598  96.953 -15.299  1.00 27.83           C  
-ATOM   1768  O   SER B 121     118.042  96.260 -16.151  1.00 29.71           O  
-ATOM   1769  CB  SER B 121     116.659  97.426 -13.818  1.00 28.74           C  
-ATOM   1770  OG  SER B 121     116.571  98.741 -14.341  1.00 38.70           O  
-ATOM   1771  N   VAL B 122     119.621  97.749 -15.590  1.00 22.93           N  
-ATOM   1772  CA  VAL B 122     120.082  97.882 -16.973  1.00 19.71           C  
-ATOM   1773  C   VAL B 122     120.666  96.560 -17.504  1.00 19.33           C  
-ATOM   1774  O   VAL B 122     121.379  95.847 -16.793  1.00 19.35           O  
-ATOM   1775  CB  VAL B 122     121.072  99.071 -17.133  1.00 20.35           C  
-ATOM   1776  CG1 VAL B 122     122.475  98.684 -16.697  1.00 18.22           C  
-ATOM   1777  CG2 VAL B 122     121.074  99.583 -18.566  1.00 19.65           C  
-ATOM   1778  N   THR B 123     120.349  96.242 -18.757  1.00 15.13           N  
-ATOM   1779  CA  THR B 123     120.715  94.950 -19.357  1.00 17.28           C  
-ATOM   1780  C   THR B 123     121.976  95.050 -20.210  1.00 15.96           C  
-ATOM   1781  O   THR B 123     122.661  94.054 -20.450  1.00 14.88           O  
-ATOM   1782  CB  THR B 123     119.580  94.413 -20.244  1.00 20.65           C  
-ATOM   1783  OG1 THR B 123     119.232  95.407 -21.213  1.00 20.85           O  
-ATOM   1784  CG2 THR B 123     118.352  94.075 -19.399  1.00 25.52           C  
-ATOM   1785  N   CYS B 124     122.274  96.262 -20.661  1.00 13.48           N  
-ATOM   1786  CA  CYS B 124     123.443  96.508 -21.488  1.00 11.80           C  
-ATOM   1787  C   CYS B 124     123.833  97.967 -21.324  1.00 12.96           C  
-ATOM   1788  O   CYS B 124     122.990  98.847 -21.448  1.00 15.94           O  
-ATOM   1789  CB  CYS B 124     123.120  96.204 -22.954  1.00 13.39           C  
-ATOM   1790  SG  CYS B 124     124.484  96.521 -24.111  1.00 14.37           S  
-ATOM   1791  N   THR B 125     125.103  98.223 -21.035  1.00  9.92           N  
-ATOM   1792  CA  THR B 125     125.568  99.599 -20.874  1.00  8.98           C  
-ATOM   1793  C   THR B 125     127.028  99.721 -21.312  1.00 10.25           C  
-ATOM   1794  O   THR B 125     127.825  98.822 -21.077  1.00 11.07           O  
-ATOM   1795  CB  THR B 125     125.373 100.077 -19.417  1.00 11.94           C  
-ATOM   1796  OG1 THR B 125     125.688 101.472 -19.315  1.00 12.19           O  
-ATOM   1797  CG2 THR B 125     126.248  99.276 -18.455  1.00  9.05           C  
-ATOM   1798  N   TYR B 126     127.364 100.823 -21.973  1.00  9.01           N  
-ATOM   1799  CA  TYR B 126     128.705 100.993 -22.523  1.00  8.41           C  
-ATOM   1800  C   TYR B 126     129.479 102.072 -21.763  1.00 11.20           C  
-ATOM   1801  O   TYR B 126     128.945 103.160 -21.510  1.00  9.89           O  
-ATOM   1802  CB  TYR B 126     128.622 101.363 -24.013  1.00  8.80           C  
-ATOM   1803  CG  TYR B 126     129.958 101.729 -24.611  1.00  9.57           C  
-ATOM   1804  CD1 TYR B 126     130.902 100.750 -24.908  1.00 10.04           C  
-ATOM   1805  CD2 TYR B 126     130.279 103.059 -24.886  1.00  8.80           C  
-ATOM   1806  CE1 TYR B 126     132.138 101.088 -25.438  1.00  8.66           C  
-ATOM   1807  CE2 TYR B 126     131.498 103.400 -25.425  1.00  8.65           C  
-ATOM   1808  CZ  TYR B 126     132.427 102.413 -25.696  1.00 11.81           C  
-ATOM   1809  OH  TYR B 126     133.649 102.770 -26.213  1.00 10.18           O  
-ATOM   1810  N   SER B 127     130.736 101.779 -21.429  1.00  7.62           N  
-ATOM   1811  CA  SER B 127     131.625 102.760 -20.793  1.00 10.42           C  
-ATOM   1812  C   SER B 127     132.615 103.383 -21.779  1.00  9.26           C  
-ATOM   1813  O   SER B 127     133.570 102.731 -22.206  1.00 10.14           O  
-ATOM   1814  CB  SER B 127     132.414 102.112 -19.654  1.00 11.79           C  
-ATOM   1815  OG  SER B 127     133.416 102.999 -19.165  1.00 10.26           O  
-ATOM   1816  N   PRO B 128     132.393 104.652 -22.148  1.00  9.70           N  
-ATOM   1817  CA  PRO B 128     133.372 105.284 -23.041  1.00  8.96           C  
-ATOM   1818  C   PRO B 128     134.765 105.361 -22.403  1.00  9.99           C  
-ATOM   1819  O   PRO B 128     135.768 105.181 -23.092  1.00 12.97           O  
-ATOM   1820  CB  PRO B 128     132.776 106.679 -23.289  1.00 12.69           C  
-ATOM   1821  CG  PRO B 128     131.285 106.475 -23.111  1.00 10.79           C  
-ATOM   1822  CD  PRO B 128     131.156 105.441 -22.006  1.00  7.17           C  
-ATOM   1823  N   ALA B 129     134.835 105.614 -21.096  1.00 11.94           N  
-ATOM   1824  CA  ALA B 129     136.136 105.748 -20.442  1.00 12.07           C  
-ATOM   1825  C   ALA B 129     136.974 104.470 -20.494  1.00 13.58           C  
-ATOM   1826  O   ALA B 129     138.205 104.528 -20.563  1.00 14.83           O  
-ATOM   1827  CB  ALA B 129     135.966 106.206 -19.002  1.00 13.04           C  
-ATOM   1828  N   LEU B 130     136.298 103.326 -20.458  1.00 10.61           N  
-ATOM   1829  CA  LEU B 130     136.964 102.030 -20.480  1.00 10.36           C  
-ATOM   1830  C   LEU B 130     136.962 101.392 -21.861  1.00 11.84           C  
-ATOM   1831  O   LEU B 130     137.574 100.342 -22.051  1.00 12.88           O  
-ATOM   1832  CB  LEU B 130     136.276 101.072 -19.504  1.00 10.71           C  
-ATOM   1833  CG  LEU B 130     136.389 101.475 -18.025  1.00 16.19           C  
-ATOM   1834  CD1 LEU B 130     135.397 100.706 -17.170  1.00 13.29           C  
-ATOM   1835  CD2 LEU B 130     137.811 101.278 -17.517  1.00 15.07           C  
-ATOM   1836  N   ASN B 131     136.279 102.029 -22.812  1.00 10.10           N  
-ATOM   1837  CA  ASN B 131     135.919 101.396 -24.095  1.00  9.09           C  
-ATOM   1838  C   ASN B 131     135.445  99.964 -23.885  1.00  8.93           C  
-ATOM   1839  O   ASN B 131     135.957  99.024 -24.500  1.00 10.53           O  
-ATOM   1840  CB  ASN B 131     137.066 101.442 -25.113  1.00 10.67           C  
-ATOM   1841  CG  ASN B 131     136.652 100.907 -26.482  1.00 11.63           C  
-ATOM   1842  OD1 ASN B 131     135.504 101.067 -26.911  1.00  9.64           O  
-ATOM   1843  ND2 ASN B 131     137.594 100.285 -27.179  1.00  9.30           N  
-ATOM   1844  N   LYS B 132     134.449  99.805 -23.021  1.00  7.87           N  
-ATOM   1845  CA  LYS B 132     134.027  98.484 -22.587  1.00  7.79           C  
-ATOM   1846  C   LYS B 132     132.506  98.405 -22.481  1.00  8.58           C  
-ATOM   1847  O   LYS B 132     131.864  99.243 -21.837  1.00  9.15           O  
-ATOM   1848  CB  LYS B 132     134.683  98.143 -21.241  1.00 10.58           C  
-ATOM   1849  CG  LYS B 132     134.359  96.756 -20.695  1.00  8.64           C  
-ATOM   1850  CD  LYS B 132     135.308  96.434 -19.539  1.00 14.80           C  
-ATOM   1851  CE  LYS B 132     135.093  95.026 -18.993  1.00 15.08           C  
-ATOM   1852  NZ  LYS B 132     136.066  94.782 -17.886  1.00 17.02           N  
-ATOM   1853  N   LEU B 133     131.943  97.389 -23.119  1.00  8.83           N  
-ATOM   1854  CA  LEU B 133     130.514  97.109 -23.036  1.00  7.26           C  
-ATOM   1855  C   LEU B 133     130.263  96.095 -21.918  1.00  9.19           C  
-ATOM   1856  O   LEU B 133     130.944  95.082 -21.847  1.00 10.57           O  
-ATOM   1857  CB  LEU B 133     130.031  96.525 -24.364  1.00  9.86           C  
-ATOM   1858  CG  LEU B 133     128.529  96.301 -24.517  1.00 10.99           C  
-ATOM   1859  CD1 LEU B 133     127.791  97.632 -24.526  1.00 15.66           C  
-ATOM   1860  CD2 LEU B 133     128.249  95.539 -25.815  1.00 19.44           C  
-ATOM   1861  N   PHE B 134     129.284  96.382 -21.065  1.00  8.13           N  
-ATOM   1862  CA  PHE B 134     128.862  95.479 -19.987  1.00  9.44           C  
-ATOM   1863  C   PHE B 134     127.449  94.993 -20.292  1.00 12.46           C  
-ATOM   1864  O   PHE B 134     126.556  95.799 -20.529  1.00 10.95           O  
-ATOM   1865  CB  PHE B 134     128.835  96.234 -18.646  1.00 10.26           C  
-ATOM   1866  CG  PHE B 134     130.175  96.733 -18.191  1.00  8.86           C  
-ATOM   1867  CD1 PHE B 134     130.727  97.886 -18.730  1.00  6.41           C  
-ATOM   1868  CD2 PHE B 134     130.874  96.060 -17.204  1.00 10.98           C  
-ATOM   1869  CE1 PHE B 134     131.963  98.345 -18.320  1.00  9.29           C  
-ATOM   1870  CE2 PHE B 134     132.110  96.520 -16.775  1.00 12.44           C  
-ATOM   1871  CZ  PHE B 134     132.656  97.664 -17.333  1.00 12.03           C  
-ATOM   1872  N   CYS B 135     127.222  93.684 -20.289  1.00 10.49           N  
-ATOM   1873  CA  CYS B 135     125.901  93.188 -20.649  1.00  8.90           C  
-ATOM   1874  C   CYS B 135     125.529  91.889 -19.936  1.00 11.37           C  
-ATOM   1875  O   CYS B 135     126.396  91.128 -19.522  1.00 12.10           O  
-ATOM   1876  CB  CYS B 135     125.810  92.985 -22.159  1.00 11.34           C  
-ATOM   1877  SG  CYS B 135     126.905  91.666 -22.758  1.00 13.99           S  
-ATOM   1878  N   GLN B 136     124.228  91.653 -19.793  1.00 12.92           N  
-ATOM   1879  CA  GLN B 136     123.737  90.409 -19.209  1.00 12.01           C  
-ATOM   1880  C   GLN B 136     123.765  89.296 -20.246  1.00 14.16           C  
-ATOM   1881  O   GLN B 136     123.779  89.543 -21.450  1.00 14.32           O  
-ATOM   1882  CB  GLN B 136     122.315  90.589 -18.664  1.00 12.78           C  
-ATOM   1883  CG  GLN B 136     122.252  91.505 -17.451  1.00 15.72           C  
-ATOM   1884  CD  GLN B 136     120.833  91.721 -16.950  1.00 20.97           C  
-ATOM   1885  OE1 GLN B 136     119.863  91.435 -17.653  1.00 23.32           O  
-ATOM   1886  NE2 GLN B 136     120.709  92.235 -15.728  1.00 24.40           N  
-ATOM   1887  N   LEU B 137     123.762  88.062 -19.765  1.00 12.11           N  
-ATOM   1888  CA  LEU B 137     123.777  86.894 -20.636  1.00 10.83           C  
-ATOM   1889  C   LEU B 137     122.639  86.880 -21.660  1.00 13.11           C  
-ATOM   1890  O   LEU B 137     121.459  86.971 -21.298  1.00 12.59           O  
-ATOM   1891  CB  LEU B 137     123.717  85.632 -19.765  1.00 11.20           C  
-ATOM   1892  CG  LEU B 137     123.745  84.316 -20.535  1.00 11.98           C  
-ATOM   1893  CD1 LEU B 137     125.104  84.127 -21.189  1.00 11.30           C  
-ATOM   1894  CD2 LEU B 137     123.446  83.172 -19.578  1.00 14.01           C  
-ATOM   1895  N   ALA B 138     123.011  86.798 -22.940  1.00 11.77           N  
-ATOM   1896  CA  ALA B 138     122.079  86.619 -24.051  1.00 10.53           C  
-ATOM   1897  C   ALA B 138     121.066  87.756 -24.267  1.00 14.27           C  
-ATOM   1898  O   ALA B 138     120.118  87.601 -25.021  1.00 22.02           O  
-ATOM   1899  CB  ALA B 138     121.361  85.270 -23.938  1.00 14.99           C  
-ATOM   1900  N   LYS B 139     121.264  88.890 -23.611  1.00 14.90           N  
-ATOM   1901  CA  LYS B 139     120.366  90.018 -23.793  1.00 11.80           C  
-ATOM   1902  C   LYS B 139     120.790  90.865 -24.992  1.00 16.19           C  
-ATOM   1903  O   LYS B 139     121.930  90.805 -25.438  1.00 13.83           O  
-ATOM   1904  CB  LYS B 139     120.344  90.884 -22.536  1.00 14.78           C  
-ATOM   1905  CG  LYS B 139     119.884  90.148 -21.278  1.00 20.00           C  
-ATOM   1906  CD  LYS B 139     118.395  89.877 -21.313  1.00 28.01           C  
-ATOM   1907  CE  LYS B 139     117.881  89.459 -19.935  1.00 33.32           C  
-ATOM   1908  NZ  LYS B 139     116.420  89.170 -19.957  1.00 41.59           N  
-ATOM   1909  N   THR B 140     119.859  91.657 -25.503  1.00 13.44           N  
-ATOM   1910  CA  THR B 140     120.118  92.525 -26.646  1.00 11.57           C  
-ATOM   1911  C   THR B 140     121.209  93.554 -26.374  1.00 11.36           C  
-ATOM   1912  O   THR B 140     121.123  94.312 -25.407  1.00 12.06           O  
-ATOM   1913  CB  THR B 140     118.831  93.268 -27.037  1.00 13.66           C  
-ATOM   1914  OG1 THR B 140     117.787  92.314 -27.287  1.00 16.18           O  
-ATOM   1915  CG2 THR B 140     119.062  94.137 -28.285  1.00 16.32           C  
-ATOM   1916  N   CYS B 141     122.223  93.589 -27.240  1.00  9.42           N  
-ATOM   1917  CA  CYS B 141     123.260  94.620 -27.187  1.00 10.67           C  
-ATOM   1918  C   CYS B 141     123.251  95.453 -28.469  1.00  8.56           C  
-ATOM   1919  O   CYS B 141     123.755  95.008 -29.503  1.00 11.48           O  
-ATOM   1920  CB  CYS B 141     124.646  93.990 -27.038  1.00 10.76           C  
-ATOM   1921  SG  CYS B 141     124.850  92.972 -25.567  1.00 13.18           S  
-ATOM   1922  N   PRO B 142     122.678  96.662 -28.409  1.00  9.00           N  
-ATOM   1923  CA  PRO B 142     122.660  97.505 -29.608  1.00  9.41           C  
-ATOM   1924  C   PRO B 142     124.032  98.095 -29.886  1.00 13.13           C  
-ATOM   1925  O   PRO B 142     124.646  98.702 -29.010  1.00 12.37           O  
-ATOM   1926  CB  PRO B 142     121.686  98.636 -29.236  1.00 14.17           C  
-ATOM   1927  CG  PRO B 142     120.954  98.148 -28.007  1.00 18.79           C  
-ATOM   1928  CD  PRO B 142     121.935  97.278 -27.296  1.00 15.35           C  
-ATOM   1929  N   VAL B 143     124.505  97.918 -31.110  1.00  9.19           N  
-ATOM   1930  CA  VAL B 143     125.760  98.517 -31.534  1.00  6.69           C  
-ATOM   1931  C   VAL B 143     125.488  99.318 -32.799  1.00  8.10           C  
-ATOM   1932  O   VAL B 143     124.961  98.788 -33.789  1.00  8.90           O  
-ATOM   1933  CB  VAL B 143     126.850  97.454 -31.791  1.00  8.53           C  
-ATOM   1934  CG1 VAL B 143     128.116  98.114 -32.323  1.00  9.91           C  
-ATOM   1935  CG2 VAL B 143     127.152  96.690 -30.502  1.00 10.22           C  
-ATOM   1936  N   GLN B 144     125.828 100.603 -32.762  1.00  7.30           N  
-ATOM   1937  CA  GLN B 144     125.617 101.466 -33.917  1.00  7.82           C  
-ATOM   1938  C   GLN B 144     126.768 101.421 -34.903  1.00 11.20           C  
-ATOM   1939  O   GLN B 144     127.934 101.312 -34.510  1.00  7.39           O  
-ATOM   1940  CB  GLN B 144     125.446 102.912 -33.459  1.00 10.20           C  
-ATOM   1941  CG  GLN B 144     124.274 103.103 -32.514  1.00  9.48           C  
-ATOM   1942  CD  GLN B 144     124.210 104.507 -31.978  1.00 11.84           C  
-ATOM   1943  OE1 GLN B 144     125.214 105.229 -31.954  1.00 14.04           O  
-ATOM   1944  NE2 GLN B 144     123.032 104.903 -31.529  1.00 17.76           N  
-ATOM   1945  N   LEU B 145     126.424 101.532 -36.187  1.00 10.01           N  
-ATOM   1946  CA  LEU B 145     127.405 101.688 -37.261  1.00  9.35           C  
-ATOM   1947  C   LEU B 145     127.283 103.091 -37.840  1.00  8.71           C  
-ATOM   1948  O   LEU B 145     126.200 103.486 -38.255  1.00  9.62           O  
-ATOM   1949  CB  LEU B 145     127.137 100.671 -38.375  1.00  7.54           C  
-ATOM   1950  CG  LEU B 145     127.006  99.201 -37.936  1.00 10.38           C  
-ATOM   1951  CD1 LEU B 145     126.713  98.314 -39.158  1.00 16.77           C  
-ATOM   1952  CD2 LEU B 145     128.262  98.740 -37.202  1.00 14.02           C  
-ATOM   1953  N   TRP B 146     128.392 103.827 -37.866  1.00  8.87           N  
-ATOM   1954  CA  TRP B 146     128.445 105.175 -38.446  1.00  6.95           C  
-ATOM   1955  C   TRP B 146     129.450 105.235 -39.596  1.00 11.32           C  
-ATOM   1956  O   TRP B 146     130.547 104.673 -39.496  1.00  8.98           O  
-ATOM   1957  CB  TRP B 146     128.865 106.183 -37.356  1.00 10.51           C  
-ATOM   1958  CG  TRP B 146     127.857 106.351 -36.249  1.00  8.97           C  
-ATOM   1959  CD1 TRP B 146     127.767 105.624 -35.091  1.00 10.05           C  
-ATOM   1960  CD2 TRP B 146     126.793 107.308 -36.205  1.00 10.20           C  
-ATOM   1961  NE1 TRP B 146     126.708 106.078 -34.330  1.00 12.68           N  
-ATOM   1962  CE2 TRP B 146     126.095 107.108 -34.997  1.00 12.05           C  
-ATOM   1963  CE3 TRP B 146     126.356 108.310 -37.082  1.00  9.04           C  
-ATOM   1964  CZ2 TRP B 146     124.987 107.873 -34.639  1.00 13.78           C  
-ATOM   1965  CZ3 TRP B 146     125.253 109.072 -36.721  1.00 13.29           C  
-ATOM   1966  CH2 TRP B 146     124.587 108.854 -35.512  1.00 14.76           C  
-ATOM   1967  N   VAL B 147     129.080 105.914 -40.688  1.00 10.23           N  
-ATOM   1968  CA  VAL B 147     130.014 106.164 -41.781  1.00  9.49           C  
-ATOM   1969  C   VAL B 147     129.853 107.595 -42.284  1.00 11.42           C  
-ATOM   1970  O   VAL B 147     128.798 108.191 -42.116  1.00 14.09           O  
-ATOM   1971  CB  VAL B 147     129.765 105.220 -42.980  1.00  9.27           C  
-ATOM   1972  CG1 VAL B 147     130.162 103.786 -42.628  1.00 11.20           C  
-ATOM   1973  CG2 VAL B 147     128.302 105.290 -43.424  1.00 11.72           C  
-ATOM   1974  N   ASP B 148     130.896 108.130 -42.910  1.00 11.99           N  
-ATOM   1975  CA  ASP B 148     130.820 109.455 -43.533  1.00 13.55           C  
-ATOM   1976  C   ASP B 148     130.215 109.393 -44.930  1.00 19.58           C  
-ATOM   1977  O   ASP B 148     129.642 110.372 -45.415  1.00 16.01           O  
-ATOM   1978  CB  ASP B 148     132.210 110.077 -43.624  1.00 13.61           C  
-ATOM   1979  CG  ASP B 148     132.788 110.428 -42.270  1.00 16.30           C  
-ATOM   1980  OD1 ASP B 148     132.015 110.800 -41.358  1.00 19.48           O  
-ATOM   1981  OD2 ASP B 148     134.024 110.358 -42.130  1.00 19.01           O  
-ATOM   1982  N   SER B 149     130.380 108.257 -45.597  1.00 13.81           N  
-ATOM   1983  CA  SER B 149     129.788 108.075 -46.918  1.00 17.71           C  
-ATOM   1984  C   SER B 149     129.292 106.649 -47.128  1.00 20.77           C  
-ATOM   1985  O   SER B 149     129.743 105.713 -46.458  1.00 16.16           O  
-ATOM   1986  CB  SER B 149     130.747 108.504 -48.037  1.00 25.07           C  
-ATOM   1987  OG  SER B 149     131.989 107.840 -47.945  1.00 23.37           O  
-ATOM   1988  N   THR B 150     128.350 106.508 -48.054  1.00 16.02           N  
-ATOM   1989  CA  THR B 150     127.673 105.242 -48.305  1.00 13.41           C  
-ATOM   1990  C   THR B 150     128.588 104.212 -48.954  1.00 16.46           C  
-ATOM   1991  O   THR B 150     129.106 104.436 -50.044  1.00 13.99           O  
-ATOM   1992  CB  THR B 150     126.443 105.452 -49.205  1.00 22.58           C  
-ATOM   1993  OG1 THR B 150     125.581 106.430 -48.609  1.00 26.05           O  
-ATOM   1994  CG2 THR B 150     125.675 104.146 -49.395  1.00 18.03           C  
-ATOM   1995  N   PRO B 151     128.780 103.070 -48.283  1.00 12.99           N  
-ATOM   1996  CA  PRO B 151     129.553 101.987 -48.897  1.00 10.92           C  
-ATOM   1997  C   PRO B 151     128.717 101.285 -49.968  1.00 10.63           C  
-ATOM   1998  O   PRO B 151     127.491 101.396 -49.981  1.00 13.85           O  
-ATOM   1999  CB  PRO B 151     129.845 101.035 -47.730  1.00 12.40           C  
-ATOM   2000  CG  PRO B 151     128.933 101.431 -46.618  1.00 13.72           C  
-ATOM   2001  CD  PRO B 151     128.196 102.692 -46.982  1.00 13.31           C  
-ATOM   2002  N   PRO B 152     129.382 100.564 -50.876  1.00 10.71           N  
-ATOM   2003  CA  PRO B 152     128.713  99.894 -51.996  1.00 13.32           C  
-ATOM   2004  C   PRO B 152     127.724  98.807 -51.582  1.00 10.98           C  
-ATOM   2005  O   PRO B 152     127.881  98.183 -50.523  1.00 10.32           O  
-ATOM   2006  CB  PRO B 152     129.875  99.266 -52.767  1.00 11.09           C  
-ATOM   2007  CG  PRO B 152     131.049 100.116 -52.443  1.00 14.48           C  
-ATOM   2008  CD  PRO B 152     130.847 100.520 -50.996  1.00 10.41           C  
-ATOM   2009  N   PRO B 153     126.707  98.558 -52.422  1.00 13.40           N  
-ATOM   2010  CA  PRO B 153     125.852  97.388 -52.198  1.00 13.80           C  
-ATOM   2011  C   PRO B 153     126.706  96.126 -52.099  1.00 11.32           C  
-ATOM   2012  O   PRO B 153     127.622  95.943 -52.897  1.00 11.94           O  
-ATOM   2013  CB  PRO B 153     124.974  97.340 -53.455  1.00 15.14           C  
-ATOM   2014  CG  PRO B 153     124.985  98.742 -53.990  1.00 12.77           C  
-ATOM   2015  CD  PRO B 153     126.320  99.321 -53.628  1.00 17.56           C  
-ATOM   2016  N   GLY B 154     126.428  95.284 -51.106  1.00 10.49           N  
-ATOM   2017  CA  GLY B 154     127.194  94.063 -50.929  1.00 10.36           C  
-ATOM   2018  C   GLY B 154     128.195  94.167 -49.795  1.00 10.64           C  
-ATOM   2019  O   GLY B 154     128.796  93.179 -49.395  1.00 10.99           O  
-ATOM   2020  N   THR B 155     128.373  95.373 -49.268  1.00  8.87           N  
-ATOM   2021  CA  THR B 155     129.233  95.563 -48.107  1.00  8.24           C  
-ATOM   2022  C   THR B 155     128.630  94.801 -46.929  1.00  8.25           C  
-ATOM   2023  O   THR B 155     127.408  94.745 -46.788  1.00 10.17           O  
-ATOM   2024  CB  THR B 155     129.339  97.052 -47.770  1.00  9.84           C  
-ATOM   2025  OG1 THR B 155     129.937  97.746 -48.878  1.00 10.14           O  
-ATOM   2026  CG2 THR B 155     130.197  97.266 -46.527  1.00  9.08           C  
-ATOM   2027  N   ARG B 156     129.485  94.212 -46.091  1.00  7.62           N  
-ATOM   2028  CA  ARG B 156     129.021  93.442 -44.939  1.00  6.58           C  
-ATOM   2029  C   ARG B 156     129.726  93.884 -43.653  1.00  6.67           C  
-ATOM   2030  O   ARG B 156     130.733  94.605 -43.697  1.00  7.30           O  
-ATOM   2031  CB  ARG B 156     129.238  91.945 -45.160  1.00  7.63           C  
-ATOM   2032  CG  ARG B 156     128.512  91.405 -46.380  1.00  9.62           C  
-ATOM   2033  CD  ARG B 156     128.153  89.920 -46.191  1.00  8.25           C  
-ATOM   2034  NE  ARG B 156     129.322  89.046 -46.230  1.00 11.43           N  
-ATOM   2035  CZ  ARG B 156     129.251  87.724 -46.081  1.00 11.90           C  
-ATOM   2036  NH1 ARG B 156     128.076  87.151 -45.863  1.00 10.11           N  
-ATOM   2037  NH2 ARG B 156     130.346  86.979 -46.141  1.00 11.73           N  
-ATOM   2038  N   VAL B 157     129.191  93.441 -42.514  1.00  6.47           N  
-ATOM   2039  CA  VAL B 157     129.725  93.821 -41.204  1.00  6.81           C  
-ATOM   2040  C   VAL B 157     129.917  92.545 -40.395  1.00  7.86           C  
-ATOM   2041  O   VAL B 157     128.960  91.799 -40.192  1.00  7.48           O  
-ATOM   2042  CB  VAL B 157     128.736  94.735 -40.448  1.00  6.92           C  
-ATOM   2043  CG1 VAL B 157     129.351  95.223 -39.115  1.00  9.49           C  
-ATOM   2044  CG2 VAL B 157     128.323  95.920 -41.338  1.00 11.05           C  
-ATOM   2045  N   ARG B 158     131.148  92.299 -39.946  1.00  7.25           N  
-ATOM   2046  CA  ARG B 158     131.507  91.059 -39.246  1.00  6.75           C  
-ATOM   2047  C   ARG B 158     131.899  91.343 -37.799  1.00  6.18           C  
-ATOM   2048  O   ARG B 158     132.535  92.351 -37.520  1.00  6.33           O  
-ATOM   2049  CB  ARG B 158     132.682  90.372 -39.962  1.00  5.95           C  
-ATOM   2050  CG  ARG B 158     133.116  89.049 -39.329  1.00  7.24           C  
-ATOM   2051  CD  ARG B 158     134.247  88.384 -40.101  1.00  8.56           C  
-ATOM   2052  NE  ARG B 158     133.913  88.284 -41.525  1.00  7.80           N  
-ATOM   2053  CZ  ARG B 158     133.248  87.275 -42.088  1.00  7.32           C  
-ATOM   2054  NH1 ARG B 158     132.829  86.240 -41.365  1.00  9.68           N  
-ATOM   2055  NH2 ARG B 158     132.988  87.311 -43.393  1.00  8.95           N  
-ATOM   2056  N   ALA B 159     131.503  90.461 -36.881  1.00  5.62           N  
-ATOM   2057  CA  ALA B 159     131.919  90.554 -35.481  1.00  5.37           C  
-ATOM   2058  C   ALA B 159     132.670  89.278 -35.086  1.00  5.21           C  
-ATOM   2059  O   ALA B 159     132.272  88.173 -35.467  1.00  6.37           O  
-ATOM   2060  CB  ALA B 159     130.700  90.730 -34.574  1.00  6.82           C  
-ATOM   2061  N   MET B 160     133.760  89.447 -34.342  1.00  6.96           N  
-ATOM   2062  CA  MET B 160     134.594  88.340 -33.871  1.00  8.25           C  
-ATOM   2063  C   MET B 160     135.136  88.696 -32.488  1.00  7.48           C  
-ATOM   2064  O   MET B 160     135.449  89.857 -32.225  1.00  7.75           O  
-ATOM   2065  CB  MET B 160     135.768  88.135 -34.844  1.00  9.43           C  
-ATOM   2066  CG  MET B 160     136.734  87.016 -34.455  1.00  9.87           C  
-ATOM   2067  SD  MET B 160     138.175  86.949 -35.561  1.00 12.24           S  
-ATOM   2068  CE  MET B 160     137.493  86.240 -37.069  1.00 14.42           C  
-ATOM   2069  N   ALA B 161     135.273  87.708 -31.604  1.00  7.22           N  
-ATOM   2070  CA  ALA B 161     135.854  87.955 -30.281  1.00  6.76           C  
-ATOM   2071  C   ALA B 161     137.282  87.418 -30.221  1.00  9.52           C  
-ATOM   2072  O   ALA B 161     137.578  86.389 -30.820  1.00  9.61           O  
-ATOM   2073  CB  ALA B 161     135.002  87.271 -29.192  1.00  7.28           C  
-ATOM   2074  N   ILE B 162     138.157  88.119 -29.507  1.00  7.19           N  
-ATOM   2075  CA  ILE B 162     139.496  87.609 -29.183  1.00  7.81           C  
-ATOM   2076  C   ILE B 162     139.794  87.910 -27.719  1.00  9.99           C  
-ATOM   2077  O   ILE B 162     139.206  88.823 -27.138  1.00  8.66           O  
-ATOM   2078  CB  ILE B 162     140.603  88.232 -30.071  1.00  8.82           C  
-ATOM   2079  CG1 ILE B 162     140.794  89.724 -29.764  1.00 10.48           C  
-ATOM   2080  CG2 ILE B 162     140.292  88.031 -31.566  1.00 11.40           C  
-ATOM   2081  CD1 ILE B 162     142.060  90.304 -30.381  1.00 15.85           C  
-ATOM   2082  N   TYR B 163     140.689  87.132 -27.108  1.00  9.18           N  
-ATOM   2083  CA  TYR B 163     141.119  87.440 -25.746  1.00  8.70           C  
-ATOM   2084  C   TYR B 163     142.022  88.672 -25.743  1.00 10.37           C  
-ATOM   2085  O   TYR B 163     142.834  88.859 -26.647  1.00 11.64           O  
-ATOM   2086  CB  TYR B 163     141.793  86.236 -25.058  1.00 11.30           C  
-ATOM   2087  CG  TYR B 163     140.797  85.163 -24.710  1.00  8.86           C  
-ATOM   2088  CD1 TYR B 163     139.829  85.390 -23.732  1.00  9.66           C  
-ATOM   2089  CD2 TYR B 163     140.789  83.941 -25.378  1.00  8.50           C  
-ATOM   2090  CE1 TYR B 163     138.891  84.439 -23.422  1.00  9.37           C  
-ATOM   2091  CE2 TYR B 163     139.844  82.977 -25.074  1.00  8.37           C  
-ATOM   2092  CZ  TYR B 163     138.899  83.239 -24.094  1.00  7.84           C  
-ATOM   2093  OH  TYR B 163     137.951  82.304 -23.788  1.00 11.49           O  
-ATOM   2094  N   LYS B 164     141.866  89.502 -24.716  1.00  9.55           N  
-ATOM   2095  CA  LYS B 164     142.573  90.776 -24.627  1.00 13.69           C  
-ATOM   2096  C   LYS B 164     144.031  90.604 -24.198  1.00 14.65           C  
-ATOM   2097  O   LYS B 164     144.919  91.306 -24.692  1.00 17.44           O  
-ATOM   2098  CB  LYS B 164     141.839  91.703 -23.654  1.00 12.28           C  
-ATOM   2099  CG  LYS B 164     142.639  92.950 -23.259  1.00 21.11           C  
-ATOM   2100  CD  LYS B 164     141.835  93.873 -22.351  1.00 24.33           C  
-ATOM   2101  CE  LYS B 164     142.647  95.116 -21.977  1.00 25.57           C  
-ATOM   2102  NZ  LYS B 164     141.986  95.918 -20.902  1.00 27.31           N  
-ATOM   2103  N   GLN B 165     144.264  89.674 -23.277  1.00 15.00           N  
-ATOM   2104  CA  GLN B 165     145.595  89.458 -22.701  1.00 18.33           C  
-ATOM   2105  C   GLN B 165     146.544  88.727 -23.647  1.00 19.02           C  
-ATOM   2106  O   GLN B 165     146.156  87.778 -24.330  1.00 15.16           O  
-ATOM   2107  CB  GLN B 165     145.485  88.687 -21.389  1.00 17.88           C  
-ATOM   2108  CG  GLN B 165     144.730  89.445 -20.305  1.00 20.90           C  
-ATOM   2109  CD  GLN B 165     144.300  88.544 -19.176  1.00 21.67           C  
-ATOM   2110  OE1 GLN B 165     143.442  87.680 -19.350  1.00 17.95           O  
-ATOM   2111  NE2 GLN B 165     144.900  88.736 -18.003  1.00 33.58           N  
-ATOM   2112  N   SER B 166     147.803  89.153 -23.657  1.00 25.44           N  
-ATOM   2113  CA  SER B 166     148.779  88.596 -24.587  1.00 25.04           C  
-ATOM   2114  C   SER B 166     148.926  87.081 -24.452  1.00 19.98           C  
-ATOM   2115  O   SER B 166     149.112  86.391 -25.446  1.00 18.41           O  
-ATOM   2116  CB  SER B 166     150.141  89.271 -24.412  1.00 34.91           C  
-ATOM   2117  OG  SER B 166     150.963  88.503 -23.554  1.00 34.76           O  
-ATOM   2118  N   GLN B 167     148.837  86.572 -23.224  1.00 20.06           N  
-ATOM   2119  CA  GLN B 167     148.995  85.147 -22.966  1.00 20.29           C  
-ATOM   2120  C   GLN B 167     147.845  84.314 -23.509  1.00 14.90           C  
-ATOM   2121  O   GLN B 167     147.976  83.105 -23.673  1.00 17.88           O  
-ATOM   2122  CB  GLN B 167     149.160  84.885 -21.461  1.00 24.72           C  
-ATOM   2123  CG  GLN B 167     148.375  85.847 -20.562  1.00 21.51           C  
-ATOM   2124  CD  GLN B 167     148.352  85.394 -19.117  1.00 33.17           C  
-ATOM   2125  OE1 GLN B 167     148.400  84.201 -18.834  1.00 39.16           O  
-ATOM   2126  NE2 GLN B 167     148.283  86.344 -18.195  1.00 37.20           N  
-ATOM   2127  N   HIS B 168     146.722  84.968 -23.800  1.00 14.61           N  
-ATOM   2128  CA  HIS B 168     145.517  84.255 -24.212  1.00 11.75           C  
-ATOM   2129  C   HIS B 168     145.053  84.578 -25.636  1.00 11.89           C  
-ATOM   2130  O   HIS B 168     144.148  83.920 -26.144  1.00 12.16           O  
-ATOM   2131  CB  HIS B 168     144.365  84.569 -23.250  1.00 11.72           C  
-ATOM   2132  CG  HIS B 168     144.657  84.225 -21.823  1.00 12.52           C  
-ATOM   2133  ND1 HIS B 168     145.018  82.956 -21.426  1.00 17.35           N  
-ATOM   2134  CD2 HIS B 168     144.623  84.978 -20.697  1.00 15.19           C  
-ATOM   2135  CE1 HIS B 168     145.198  82.942 -20.117  1.00 20.73           C  
-ATOM   2136  NE2 HIS B 168     144.966  84.156 -19.650  1.00 16.75           N  
-ATOM   2137  N   MET B 169     145.657  85.571 -26.277  1.00 12.42           N  
-ATOM   2138  C   MET B 169     145.166  85.015 -28.683  1.00 12.56           C  
-ATOM   2139  O   MET B 169     144.370  85.095 -29.610  1.00 13.55           O  
-ATOM   2140  CA AMET B 169     145.138  86.053 -27.558  0.50 11.82           C  
-ATOM   2141  CB AMET B 169     145.832  87.343 -27.996  0.50 15.61           C  
-ATOM   2142  CG AMET B 169     147.330  87.229 -28.169  0.50 19.08           C  
-ATOM   2143  SD AMET B 169     148.024  88.818 -28.673  0.50 22.59           S  
-ATOM   2144  CE AMET B 169     147.262  89.903 -27.471  0.50 18.87           C  
-ATOM   2145  CA BMET B 169     145.145  86.057 -27.560  0.50 11.82           C  
-ATOM   2146  CB BMET B 169     145.862  87.337 -27.994  0.50 15.61           C  
-ATOM   2147  CG BMET B 169     147.351  87.180 -28.227  0.50 19.05           C  
-ATOM   2148  SD BMET B 169     148.168  88.787 -28.361  0.50 22.81           S  
-ATOM   2149  CE BMET B 169     149.869  88.275 -28.621  0.50 20.25           C  
-ATOM   2150  N   THR B 170     146.064  84.035 -28.599  1.00 11.51           N  
-ATOM   2151  CA  THR B 170     146.105  82.980 -29.628  1.00  9.60           C  
-ATOM   2152  C   THR B 170     145.043  81.894 -29.472  1.00 14.08           C  
-ATOM   2153  O   THR B 170     144.896  81.039 -30.348  1.00 16.44           O  
-ATOM   2154  CB  THR B 170     147.493  82.309 -29.751  1.00 14.45           C  
-ATOM   2155  OG1 THR B 170     147.806  81.610 -28.539  1.00 12.96           O  
-ATOM   2156  CG2 THR B 170     148.563  83.347 -30.053  1.00 12.02           C  
-ATOM   2157  N   GLU B 171     144.310  81.911 -28.364  1.00 12.00           N  
-ATOM   2158  CA  GLU B 171     143.279  80.907 -28.121  1.00 11.65           C  
-ATOM   2159  C   GLU B 171     141.924  81.345 -28.682  1.00 12.54           C  
-ATOM   2160  O   GLU B 171     141.494  82.478 -28.447  1.00 11.05           O  
-ATOM   2161  CB  GLU B 171     143.160  80.623 -26.616  1.00 13.47           C  
-ATOM   2162  CG  GLU B 171     142.078  79.632 -26.267  1.00 15.77           C  
-ATOM   2163  CD  GLU B 171     141.967  79.358 -24.775  1.00 19.60           C  
-ATOM   2164  OE1 GLU B 171     142.967  79.539 -24.042  1.00 19.68           O  
-ATOM   2165  OE2 GLU B 171     140.872  78.955 -24.339  1.00 20.14           O  
-ATOM   2166  N   VAL B 172     141.255  80.454 -29.419  1.00  9.07           N  
-ATOM   2167  CA  VAL B 172     139.930  80.764 -29.968  1.00  7.62           C  
-ATOM   2168  C   VAL B 172     138.950  81.052 -28.828  1.00 10.92           C  
-ATOM   2169  O   VAL B 172     138.836  80.265 -27.882  1.00 10.14           O  
-ATOM   2170  CB  VAL B 172     139.379  79.595 -30.824  1.00 10.10           C  
-ATOM   2171  CG1 VAL B 172     137.917  79.849 -31.253  1.00  9.69           C  
-ATOM   2172  CG2 VAL B 172     140.266  79.364 -32.044  1.00 11.40           C  
-ATOM   2173  N   VAL B 173     138.247  82.181 -28.909  1.00  8.20           N  
-ATOM   2174  CA  VAL B 173     137.182  82.469 -27.953  1.00  7.57           C  
-ATOM   2175  C   VAL B 173     135.941  81.666 -28.343  1.00  7.98           C  
-ATOM   2176  O   VAL B 173     135.445  81.783 -29.466  1.00  7.43           O  
-ATOM   2177  CB  VAL B 173     136.814  83.962 -27.942  1.00  9.55           C  
-ATOM   2178  CG1 VAL B 173     135.648  84.198 -26.986  1.00  8.29           C  
-ATOM   2179  CG2 VAL B 173     138.020  84.805 -27.543  1.00  8.77           C  
-ATOM   2180  N   ARG B 174     135.457  80.834 -27.425  1.00  9.73           N  
-ATOM   2181  CA  ARG B 174     134.306  79.983 -27.708  1.00  8.22           C  
-ATOM   2182  C   ARG B 174     133.430  79.822 -26.467  1.00  6.01           C  
-ATOM   2183  O   ARG B 174     133.832  80.170 -25.359  1.00  9.19           O  
-ATOM   2184  CB  ARG B 174     134.790  78.603 -28.171  1.00 10.46           C  
-ATOM   2185  CG  ARG B 174     135.636  77.881 -27.114  1.00  9.70           C  
-ATOM   2186  CD  ARG B 174     135.932  76.423 -27.485  1.00 14.44           C  
-ATOM   2187  NE  ARG B 174     136.685  76.289 -28.737  1.00 13.29           N  
-ATOM   2188  CZ  ARG B 174     136.141  76.017 -29.922  1.00 12.15           C  
-ATOM   2189  NH1 ARG B 174     134.827  75.849 -30.041  1.00 12.22           N  
-ATOM   2190  NH2 ARG B 174     136.917  75.921 -30.994  1.00 13.55           N  
-ATOM   2191  N   ARG B 175     132.229  79.283 -26.656  1.00  6.37           N  
-ATOM   2192  CA  ARG B 175     131.358  79.004 -25.526  1.00  7.52           C  
-ATOM   2193  C   ARG B 175     131.897  77.867 -24.668  1.00  9.08           C  
-ATOM   2194  O   ARG B 175     132.609  76.989 -25.154  1.00  8.99           O  
-ATOM   2195  CB  ARG B 175     129.933  78.708 -25.990  1.00  7.92           C  
-ATOM   2196  CG  ARG B 175     129.231  79.939 -26.564  1.00  9.12           C  
-ATOM   2197  CD  ARG B 175     127.817  79.561 -26.928  1.00 11.19           C  
-ATOM   2198  NE  ARG B 175     126.866  79.761 -25.836  1.00 10.09           N  
-ATOM   2199  CZ  ARG B 175     125.636  79.251 -25.833  1.00  8.65           C  
-ATOM   2200  NH1 ARG B 175     125.251  78.450 -26.822  1.00 10.01           N  
-ATOM   2201  NH2 ARG B 175     124.804  79.516 -24.835  1.00 10.86           N  
-ATOM   2202  N   CYS B 176     131.538  77.903 -23.384  1.00  6.96           N  
-ATOM   2203  CA  CYS B 176     132.040  76.954 -22.394  1.00  7.79           C  
-ATOM   2204  C   CYS B 176     131.443  75.568 -22.603  1.00 11.95           C  
-ATOM   2205  O   CYS B 176     130.504  75.403 -23.378  1.00 11.04           O  
-ATOM   2206  CB  CYS B 176     131.747  77.472 -20.972  1.00  7.27           C  
-ATOM   2207  SG  CYS B 176     130.035  77.360 -20.445  1.00  9.49           S  
-ATOM   2208  N   PRO B 177     132.000  74.556 -21.912  1.00 10.17           N  
-ATOM   2209  CA  PRO B 177     131.543  73.173 -22.095  1.00 12.25           C  
-ATOM   2210  C   PRO B 177     130.084  72.973 -21.704  1.00 10.17           C  
-ATOM   2211  O   PRO B 177     129.438  72.059 -22.213  1.00 14.27           O  
-ATOM   2212  CB  PRO B 177     132.465  72.367 -21.176  1.00 14.46           C  
-ATOM   2213  CG  PRO B 177     133.676  73.211 -20.996  1.00 16.08           C  
-ATOM   2214  CD  PRO B 177     133.220  74.642 -21.092  1.00 11.51           C  
-ATOM   2215  N   HIS B 178     129.569  73.802 -20.801  1.00 12.37           N  
-ATOM   2216  CA  HIS B 178     128.153  73.742 -20.453  1.00  9.87           C  
-ATOM   2217  C   HIS B 178     127.262  74.379 -21.515  1.00 11.15           C  
-ATOM   2218  O   HIS B 178     126.322  73.761 -22.006  1.00 12.50           O  
-ATOM   2219  CB  HIS B 178     127.882  74.426 -19.108  1.00 12.28           C  
-ATOM   2220  CG  HIS B 178     126.427  74.669 -18.848  1.00 12.77           C  
-ATOM   2221  ND1 HIS B 178     125.514  73.644 -18.717  1.00 16.03           N  
-ATOM   2222  CD2 HIS B 178     125.722  75.818 -18.708  1.00 13.74           C  
-ATOM   2223  CE1 HIS B 178     124.311  74.150 -18.505  1.00 16.28           C  
-ATOM   2224  NE2 HIS B 178     124.410  75.468 -18.493  1.00 16.62           N  
-ATOM   2225  N   HIS B 179     127.540  75.634 -21.854  1.00 11.20           N  
-ATOM   2226  CA  HIS B 179     126.640  76.346 -22.758  1.00 10.97           C  
-ATOM   2227  C   HIS B 179     126.648  75.815 -24.191  1.00  9.17           C  
-ATOM   2228  O   HIS B 179     125.625  75.881 -24.890  1.00 11.22           O  
-ATOM   2229  CB  HIS B 179     126.901  77.852 -22.717  1.00 10.59           C  
-ATOM   2230  CG  HIS B 179     126.317  78.523 -21.513  1.00 10.12           C  
-ATOM   2231  ND1 HIS B 179     127.092  79.118 -20.543  1.00 11.51           N  
-ATOM   2232  CD2 HIS B 179     125.030  78.683 -21.117  1.00 13.79           C  
-ATOM   2233  CE1 HIS B 179     126.311  79.627 -19.606  1.00 11.90           C  
-ATOM   2234  NE2 HIS B 179     125.055  79.375 -19.928  1.00 12.62           N  
-ATOM   2235  N   GLU B 180     127.776  75.276 -24.640  1.00  9.71           N  
-ATOM   2236  CA  GLU B 180     127.791  74.719 -25.988  1.00 10.00           C  
-ATOM   2237  C   GLU B 180     126.875  73.505 -26.090  1.00 12.50           C  
-ATOM   2238  O   GLU B 180     126.517  73.095 -27.181  1.00 13.05           O  
-ATOM   2239  CB  GLU B 180     129.214  74.406 -26.486  1.00 11.37           C  
-ATOM   2240  CG  GLU B 180     129.866  73.195 -25.836  1.00 10.38           C  
-ATOM   2241  CD  GLU B 180     131.125  72.737 -26.566  1.00 12.34           C  
-ATOM   2242  OE1 GLU B 180     131.587  73.442 -27.485  1.00 12.27           O  
-ATOM   2243  OE2 GLU B 180     131.654  71.649 -26.239  1.00 16.58           O  
-ATOM   2244  N   ARG B 181     126.480  72.955 -24.941  1.00 13.18           N  
-ATOM   2245  CA  ARG B 181     125.657  71.746 -24.904  1.00 12.09           C  
-ATOM   2246  C   ARG B 181     124.224  71.960 -24.385  1.00 17.13           C  
-ATOM   2247  O   ARG B 181     123.531  70.992 -24.073  1.00 16.90           O  
-ATOM   2248  CB  ARG B 181     126.342  70.670 -24.047  1.00 12.76           C  
-ATOM   2249  CG  ARG B 181     127.666  70.174 -24.605  1.00 11.99           C  
-ATOM   2250  CD  ARG B 181     128.263  69.050 -23.735  1.00  9.56           C  
-ATOM   2251  NE  ARG B 181     127.481  67.812 -23.784  1.00  8.77           N  
-ATOM   2252  CZ  ARG B 181     126.879  67.252 -22.731  1.00  9.83           C  
-ATOM   2253  NH1 ARG B 181     126.926  67.831 -21.531  1.00  9.04           N  
-ATOM   2254  NH2 ARG B 181     126.216  66.109 -22.882  1.00 10.21           N  
-ATOM   2255  N  ACYS B 182     123.770  73.205 -24.280  0.53 16.49           N  
-ATOM   2256  CA ACYS B 182     122.455  73.431 -23.675  0.53 19.53           C  
-ATOM   2257  C  ACYS B 182     121.300  73.571 -24.675  0.53 20.41           C  
-ATOM   2258  O  ACYS B 182     120.203  73.986 -24.302  0.53 22.32           O  
-ATOM   2259  CB ACYS B 182     122.488  74.605 -22.685  0.53 20.01           C  
-ATOM   2260  SG ACYS B 182     122.669  76.225 -23.433  0.53 17.36           S  
-ATOM   2261  N  BCYS B 182     123.787  73.218 -24.329  0.47 16.48           N  
-ATOM   2262  CA BCYS B 182     122.495  73.579 -23.732  0.47 19.53           C  
-ATOM   2263  C  BCYS B 182     121.292  73.486 -24.662  0.47 20.42           C  
-ATOM   2264  O  BCYS B 182     120.155  73.673 -24.230  0.47 22.03           O  
-ATOM   2265  CB BCYS B 182     122.554  74.994 -23.157  0.47 20.75           C  
-ATOM   2266  SG BCYS B 182     123.209  75.062 -21.504  0.47 14.71           S  
-ATOM   2267  N   SER B 183     121.540  73.213 -25.934  1.00 21.06           N  
-ATOM   2268  CA  SER B 183     120.466  73.168 -26.937  1.00 22.53           C  
-ATOM   2269  C   SER B 183     119.708  74.489 -27.049  1.00 27.22           C  
-ATOM   2270  O   SER B 183     118.482  74.503 -27.209  1.00 26.04           O  
-ATOM   2271  CB  SER B 183     119.471  72.042 -26.622  1.00 28.85           C  
-ATOM   2272  OG  SER B 183     120.123  70.790 -26.570  1.00 34.08           O  
-ATOM   2273  N   ASP B 184     120.433  75.599 -26.964  1.00 21.68           N  
-ATOM   2274  CA  ASP B 184     119.798  76.905 -27.031  1.00 13.67           C  
-ATOM   2275  C   ASP B 184     120.066  77.602 -28.368  1.00 21.16           C  
-ATOM   2276  O   ASP B 184     119.940  78.812 -28.471  1.00 22.02           O  
-ATOM   2277  CB  ASP B 184     120.234  77.780 -25.850  1.00 14.43           C  
-ATOM   2278  CG  ASP B 184     121.698  78.159 -25.909  1.00 15.21           C  
-ATOM   2279  OD1 ASP B 184     122.367  77.827 -26.907  1.00 15.13           O  
-ATOM   2280  OD2 ASP B 184     122.167  78.808 -24.950  1.00 16.61           O  
-ATOM   2281  N   SER B 185     120.434  76.830 -29.386  1.00 24.18           N  
-ATOM   2282  CA  SER B 185     120.667  77.387 -30.719  1.00 28.04           C  
-ATOM   2283  C   SER B 185     119.360  77.862 -31.362  1.00 34.17           C  
-ATOM   2284  O   SER B 185     118.278  77.440 -30.961  1.00 37.44           O  
-ATOM   2285  CB  SER B 185     121.362  76.357 -31.615  1.00 29.15           C  
-ATOM   2286  OG  SER B 185     121.362  76.768 -32.973  1.00 38.93           O  
-ATOM   2287  N   ASP B 186     119.465  78.742 -32.354  1.00 27.87           N  
-ATOM   2288  CA  ASP B 186     118.288  79.266 -33.046  1.00 29.10           C  
-ATOM   2289  C   ASP B 186     118.139  78.658 -34.435  1.00 29.38           C  
-ATOM   2290  O   ASP B 186     117.322  79.108 -35.234  1.00 32.78           O  
-ATOM   2291  CB  ASP B 186     118.358  80.793 -33.147  1.00 34.45           C  
-ATOM   2292  CG  ASP B 186     119.606  81.281 -33.885  1.00 32.88           C  
-ATOM   2293  OD1 ASP B 186     120.458  80.449 -34.261  1.00 24.72           O  
-ATOM   2294  OD2 ASP B 186     119.732  82.505 -34.092  1.00 33.42           O  
-ATOM   2295  N   GLY B 187     118.930  77.630 -34.716  1.00 28.96           N  
-ATOM   2296  CA  GLY B 187     118.913  77.002 -36.025  1.00 32.73           C  
-ATOM   2297  C   GLY B 187     119.955  77.591 -36.955  1.00 30.09           C  
-ATOM   2298  O   GLY B 187     120.340  76.962 -37.945  1.00 36.36           O  
-ATOM   2299  N   LEU B 188     120.422  78.794 -36.633  1.00 22.98           N  
-ATOM   2300  CA  LEU B 188     121.419  79.474 -37.454  1.00 21.39           C  
-ATOM   2301  C   LEU B 188     122.790  79.475 -36.791  1.00 15.68           C  
-ATOM   2302  O   LEU B 188     123.777  79.014 -37.377  1.00 17.54           O  
-ATOM   2303  CB  LEU B 188     120.986  80.912 -37.757  1.00 27.66           C  
-ATOM   2304  CG  LEU B 188     119.856  81.084 -38.776  1.00 37.82           C  
-ATOM   2305  CD1 LEU B 188     118.528  80.600 -38.200  1.00 35.85           C  
-ATOM   2306  CD2 LEU B 188     119.756  82.536 -39.215  1.00 32.85           C  
-ATOM   2307  N   ALA B 189     122.845  79.991 -35.569  1.00 14.19           N  
-ATOM   2308  CA  ALA B 189     124.106  80.067 -34.834  1.00  8.34           C  
-ATOM   2309  C   ALA B 189     124.561  78.687 -34.359  1.00 12.36           C  
-ATOM   2310  O   ALA B 189     123.808  77.980 -33.682  1.00 12.26           O  
-ATOM   2311  CB  ALA B 189     123.969  81.007 -33.644  1.00 10.87           C  
-ATOM   2312  N   PRO B 190     125.791  78.291 -34.717  1.00 10.31           N  
-ATOM   2313  CA  PRO B 190     126.332  77.065 -34.119  1.00  9.99           C  
-ATOM   2314  C   PRO B 190     126.351  77.231 -32.601  1.00 12.46           C  
-ATOM   2315  O   PRO B 190     126.552  78.351 -32.109  1.00  9.86           O  
-ATOM   2316  CB  PRO B 190     127.763  77.009 -34.662  1.00 11.73           C  
-ATOM   2317  CG  PRO B 190     127.723  77.872 -35.932  1.00 11.96           C  
-ATOM   2318  CD  PRO B 190     126.763  78.967 -35.593  1.00  9.82           C  
-ATOM   2319  N   PRO B 191     126.151  76.135 -31.856  1.00  9.55           N  
-ATOM   2320  CA  PRO B 191     126.089  76.233 -30.393  1.00 11.69           C  
-ATOM   2321  C   PRO B 191     127.423  76.645 -29.761  1.00  9.78           C  
-ATOM   2322  O   PRO B 191     127.427  77.069 -28.607  1.00  9.95           O  
-ATOM   2323  CB  PRO B 191     125.711  74.819 -29.937  1.00  9.51           C  
-ATOM   2324  CG  PRO B 191     125.785  73.939 -31.131  1.00 11.79           C  
-ATOM   2325  CD  PRO B 191     125.904  74.774 -32.371  1.00 10.25           C  
-ATOM   2326  N   GLN B 192     128.520  76.546 -30.512  1.00  8.75           N  
-ATOM   2327  CA  GLN B 192     129.827  76.934 -29.987  1.00  8.24           C  
-ATOM   2328  C   GLN B 192     130.080  78.438 -30.040  1.00 10.20           C  
-ATOM   2329  O   GLN B 192     130.994  78.931 -29.381  1.00  7.29           O  
-ATOM   2330  CB  GLN B 192     130.956  76.245 -30.769  1.00  9.18           C  
-ATOM   2331  CG  GLN B 192     130.921  74.716 -30.756  1.00  9.70           C  
-ATOM   2332  CD  GLN B 192     130.259  74.154 -32.001  1.00 10.55           C  
-ATOM   2333  OE1 GLN B 192     129.210  74.636 -32.430  1.00 14.37           O  
-ATOM   2334  NE2 GLN B 192     130.866  73.123 -32.584  1.00 10.57           N  
-ATOM   2335  N   HIS B 193     129.302  79.162 -30.840  1.00  7.23           N  
-ATOM   2336  CA  HIS B 193     129.603  80.582 -31.079  1.00  6.60           C  
-ATOM   2337  C   HIS B 193     129.193  81.497 -29.926  1.00  6.12           C  
-ATOM   2338  O   HIS B 193     128.029  81.518 -29.522  1.00  7.85           O  
-ATOM   2339  CB  HIS B 193     128.937  81.068 -32.377  1.00  6.12           C  
-ATOM   2340  CG  HIS B 193     129.667  80.673 -33.625  1.00  7.63           C  
-ATOM   2341  ND1 HIS B 193     129.784  81.510 -34.715  1.00  6.42           N  
-ATOM   2342  CD2 HIS B 193     130.320  79.533 -33.954  1.00  8.63           C  
-ATOM   2343  CE1 HIS B 193     130.477  80.901 -35.664  1.00  8.38           C  
-ATOM   2344  NE2 HIS B 193     130.809  79.696 -35.227  1.00  9.29           N  
-ATOM   2345  N   LEU B 194     130.148  82.269 -29.411  1.00  4.53           N  
-ATOM   2346  CA  LEU B 194     129.857  83.236 -28.348  1.00  5.68           C  
-ATOM   2347  C   LEU B 194     128.914  84.343 -28.813  1.00  7.35           C  
-ATOM   2348  O   LEU B 194     127.963  84.708 -28.111  1.00  7.33           O  
-ATOM   2349  CB  LEU B 194     131.149  83.873 -27.834  1.00  6.74           C  
-ATOM   2350  CG  LEU B 194     130.905  84.964 -26.776  1.00  6.67           C  
-ATOM   2351  CD1 LEU B 194     130.375  84.345 -25.491  1.00  9.53           C  
-ATOM   2352  CD2 LEU B 194     132.167  85.781 -26.492  1.00  9.01           C  
-ATOM   2353  N   ILE B 195     129.190  84.897 -29.994  1.00  6.40           N  
-ATOM   2354  CA  ILE B 195     128.451  86.062 -30.469  1.00  6.56           C  
-ATOM   2355  C   ILE B 195     127.397  85.695 -31.505  1.00  5.44           C  
-ATOM   2356  O   ILE B 195     127.701  85.058 -32.520  1.00  6.86           O  
-ATOM   2357  CB  ILE B 195     129.389  87.100 -31.116  1.00  6.62           C  
-ATOM   2358  CG1 ILE B 195     130.509  87.502 -30.141  1.00  6.00           C  
-ATOM   2359  CG2 ILE B 195     128.584  88.327 -31.572  1.00  7.08           C  
-ATOM   2360  CD1 ILE B 195     131.507  88.537 -30.729  1.00  6.14           C  
-ATOM   2361  N   ARG B 196     126.154  86.093 -31.235  1.00  7.05           N  
-ATOM   2362  CA  ARG B 196     125.062  85.939 -32.197  1.00  8.14           C  
-ATOM   2363  C   ARG B 196     124.530  87.299 -32.623  1.00  7.95           C  
-ATOM   2364  O   ARG B 196     124.678  88.297 -31.896  1.00  8.02           O  
-ATOM   2365  CB  ARG B 196     123.901  85.153 -31.582  1.00  9.13           C  
-ATOM   2366  CG  ARG B 196     124.248  83.742 -31.180  1.00  8.11           C  
-ATOM   2367  CD  ARG B 196     123.009  82.992 -30.688  1.00 12.92           C  
-ATOM   2368  NE  ARG B 196     123.393  81.690 -30.161  1.00 11.25           N  
-ATOM   2369  CZ  ARG B 196     122.563  80.838 -29.564  1.00 14.85           C  
-ATOM   2370  NH1 ARG B 196     121.280  81.141 -29.399  1.00 14.97           N  
-ATOM   2371  NH2 ARG B 196     123.029  79.681 -29.124  1.00 15.44           N  
-ATOM   2372  N   VAL B 197     123.910  87.336 -33.800  1.00  9.85           N  
-ATOM   2373  CA  VAL B 197     123.096  88.482 -34.208  1.00  8.03           C  
-ATOM   2374  C   VAL B 197     121.625  88.144 -34.005  1.00 12.33           C  
-ATOM   2375  O   VAL B 197     121.160  87.080 -34.420  1.00 11.93           O  
-ATOM   2376  CB  VAL B 197     123.363  88.905 -35.671  1.00  9.60           C  
-ATOM   2377  CG1 VAL B 197     122.266  89.869 -36.166  1.00 13.19           C  
-ATOM   2378  CG2 VAL B 197     124.739  89.563 -35.785  1.00  9.22           C  
-ATOM   2379  N   GLU B 198     120.913  89.042 -33.337  1.00 11.11           N  
-ATOM   2380  CA  GLU B 198     119.496  88.874 -33.027  1.00 12.39           C  
-ATOM   2381  C   GLU B 198     118.641  89.519 -34.121  1.00 14.24           C  
-ATOM   2382  O   GLU B 198     118.880  90.663 -34.508  1.00 16.22           O  
-ATOM   2383  CB  GLU B 198     119.192  89.526 -31.677  1.00 14.35           C  
-ATOM   2384  CG  GLU B 198     117.739  89.502 -31.255  1.00 20.83           C  
-ATOM   2385  CD  GLU B 198     117.491  90.273 -29.969  1.00 25.11           C  
-ATOM   2386  OE1 GLU B 198     118.471  90.610 -29.267  1.00 16.84           O  
-ATOM   2387  OE2 GLU B 198     116.309  90.552 -29.664  1.00 28.99           O  
-ATOM   2388  N   GLY B 199     117.662  88.771 -34.626  1.00 15.93           N  
-ATOM   2389  CA  GLY B 199     116.638  89.326 -35.498  1.00 19.10           C  
-ATOM   2390  C   GLY B 199     117.082  89.749 -36.887  1.00 22.05           C  
-ATOM   2391  O   GLY B 199     116.677  90.805 -37.387  1.00 21.92           O  
-ATOM   2392  N   ASN B 200     117.914  88.926 -37.513  1.00 15.98           N  
-ATOM   2393  CA  ASN B 200     118.349  89.172 -38.880  1.00 16.10           C  
-ATOM   2394  C   ASN B 200     118.549  87.835 -39.588  1.00 19.68           C  
-ATOM   2395  O   ASN B 200     119.538  87.145 -39.355  1.00 15.97           O  
-ATOM   2396  CB  ASN B 200     119.643  89.984 -38.882  1.00 17.38           C  
-ATOM   2397  CG  ASN B 200     120.009  90.507 -40.265  1.00 16.30           C  
-ATOM   2398  OD1 ASN B 200     119.641  89.921 -41.286  1.00 17.27           O  
-ATOM   2399  ND2 ASN B 200     120.743  91.607 -40.300  1.00 16.00           N  
-ATOM   2400  N   LEU B 201     117.600  87.454 -40.436  1.00 19.44           N  
-ATOM   2401  CA  LEU B 201     117.684  86.156 -41.106  1.00 21.73           C  
-ATOM   2402  C   LEU B 201     118.808  86.070 -42.140  1.00 19.88           C  
-ATOM   2403  O   LEU B 201     119.097  84.994 -42.659  1.00 19.07           O  
-ATOM   2404  CB  LEU B 201     116.340  85.779 -41.738  1.00 21.88           C  
-ATOM   2405  CG  LEU B 201     115.242  85.384 -40.742  1.00 30.08           C  
-ATOM   2406  CD1 LEU B 201     113.903  85.212 -41.451  1.00 36.02           C  
-ATOM   2407  CD2 LEU B 201     115.606  84.121 -39.966  1.00 33.13           C  
-ATOM   2408  N   ARG B 202     119.446  87.199 -42.434  1.00 15.94           N  
-ATOM   2409  CA  ARG B 202     120.572  87.205 -43.355  1.00 14.13           C  
-ATOM   2410  C   ARG B 202     121.924  87.047 -42.651  1.00 13.07           C  
-ATOM   2411  O   ARG B 202     122.968  87.068 -43.295  1.00 14.35           O  
-ATOM   2412  CB  ARG B 202     120.544  88.457 -44.238  1.00 19.81           C  
-ATOM   2413  CG  ARG B 202     119.408  88.426 -45.273  1.00 23.59           C  
-ATOM   2414  CD  ARG B 202     119.591  89.479 -46.353  1.00 33.15           C  
-ATOM   2415  NE  ARG B 202     119.506  90.837 -45.818  1.00 41.14           N  
-ATOM   2416  CZ  ARG B 202     119.828  91.933 -46.500  1.00 45.91           C  
-ATOM   2417  NH1 ARG B 202     120.268  91.836 -47.750  1.00 42.54           N  
-ATOM   2418  NH2 ARG B 202     119.719  93.129 -45.929  1.00 42.21           N  
-ATOM   2419  N   ALA B 203     121.902  86.868 -41.331  1.00 14.66           N  
-ATOM   2420  CA  ALA B 203     123.137  86.599 -40.600  1.00 13.71           C  
-ATOM   2421  C   ALA B 203     123.745  85.261 -41.026  1.00 14.08           C  
-ATOM   2422  O   ALA B 203     123.038  84.261 -41.171  1.00 15.27           O  
-ATOM   2423  CB  ALA B 203     122.887  86.623 -39.069  1.00 11.60           C  
-ATOM   2424  N   GLU B 204     125.058  85.259 -41.228  1.00  8.52           N  
-ATOM   2425  CA  GLU B 204     125.817  84.055 -41.537  1.00  8.85           C  
-ATOM   2426  C   GLU B 204     126.900  83.828 -40.489  1.00 11.21           C  
-ATOM   2427  O   GLU B 204     127.514  84.775 -39.995  1.00  8.95           O  
-ATOM   2428  CB  GLU B 204     126.456  84.159 -42.918  1.00 11.44           C  
-ATOM   2429  CG  GLU B 204     125.420  84.282 -44.024  1.00 14.86           C  
-ATOM   2430  CD  GLU B 204     126.038  84.433 -45.405  1.00 19.76           C  
-ATOM   2431  OE1 GLU B 204     127.279  84.303 -45.539  1.00 17.03           O  
-ATOM   2432  OE2 GLU B 204     125.271  84.689 -46.354  1.00 21.76           O  
-ATOM   2433  N   TYR B 205     127.108  82.567 -40.140  1.00  9.64           N  
-ATOM   2434  CA  TYR B 205     128.086  82.213 -39.130  1.00  8.19           C  
-ATOM   2435  C   TYR B 205     129.243  81.471 -39.773  1.00 10.55           C  
-ATOM   2436  O   TYR B 205     129.033  80.532 -40.544  1.00 13.27           O  
-ATOM   2437  CB  TYR B 205     127.418  81.370 -38.039  1.00  8.28           C  
-ATOM   2438  CG  TYR B 205     126.434  82.188 -37.237  1.00  6.83           C  
-ATOM   2439  CD1 TYR B 205     125.136  82.412 -37.698  1.00  9.69           C  
-ATOM   2440  CD2 TYR B 205     126.813  82.771 -36.037  1.00  6.51           C  
-ATOM   2441  CE1 TYR B 205     124.240  83.194 -36.955  1.00  8.23           C  
-ATOM   2442  CE2 TYR B 205     125.935  83.538 -35.300  1.00  8.51           C  
-ATOM   2443  CZ  TYR B 205     124.655  83.754 -35.764  1.00  8.01           C  
-ATOM   2444  OH  TYR B 205     123.785  84.517 -35.010  1.00  8.18           O  
-ATOM   2445  N   LEU B 206     130.462  81.901 -39.467  1.00  7.60           N  
-ATOM   2446  CA  LEU B 206     131.653  81.286 -40.051  1.00 11.02           C  
-ATOM   2447  C   LEU B 206     132.527  80.595 -39.014  1.00  9.44           C  
-ATOM   2448  O   LEU B 206     132.839  81.175 -37.974  1.00  8.43           O  
-ATOM   2449  CB  LEU B 206     132.496  82.346 -40.754  1.00 10.16           C  
-ATOM   2450  CG  LEU B 206     133.826  81.865 -41.346  1.00  9.51           C  
-ATOM   2451  CD1 LEU B 206     133.571  80.897 -42.504  1.00 13.41           C  
-ATOM   2452  CD2 LEU B 206     134.665  83.060 -41.791  1.00 12.58           C  
-ATOM   2453  N   ASP B 207     132.925  79.360 -39.316  1.00 11.09           N  
-ATOM   2454  CA  ASP B 207     134.040  78.707 -38.630  1.00 12.81           C  
-ATOM   2455  C   ASP B 207     135.215  78.765 -39.599  1.00 11.36           C  
-ATOM   2456  O   ASP B 207     135.208  78.079 -40.618  1.00 14.10           O  
-ATOM   2457  CB  ASP B 207     133.740  77.229 -38.346  1.00 11.23           C  
-ATOM   2458  CG  ASP B 207     132.566  77.024 -37.402  1.00 22.76           C  
-ATOM   2459  OD1 ASP B 207     132.486  77.719 -36.375  1.00 15.40           O  
-ATOM   2460  OD2 ASP B 207     131.727  76.140 -37.682  1.00 28.72           O  
-ATOM   2461  N   ASP B 208     136.217  79.580 -39.301  1.00 10.04           N  
-ATOM   2462  CA  ASP B 208     137.306  79.777 -40.254  1.00 12.94           C  
-ATOM   2463  C   ASP B 208     138.067  78.464 -40.467  1.00 14.51           C  
-ATOM   2464  O   ASP B 208     138.470  77.814 -39.509  1.00 12.27           O  
-ATOM   2465  CB  ASP B 208     138.241  80.888 -39.774  1.00 11.67           C  
-ATOM   2466  CG  ASP B 208     139.215  81.333 -40.848  1.00 17.05           C  
-ATOM   2467  OD1 ASP B 208     140.169  80.579 -41.137  1.00 17.99           O  
-ATOM   2468  OD2 ASP B 208     139.029  82.438 -41.398  1.00 15.81           O  
-ATOM   2469  N   ARG B 209     138.248  78.069 -41.724  1.00 19.22           N  
-ATOM   2470  CA  ARG B 209     138.810  76.747 -42.013  1.00 20.06           C  
-ATOM   2471  C   ARG B 209     140.292  76.640 -41.660  1.00 22.93           C  
-ATOM   2472  O   ARG B 209     140.827  75.536 -41.521  1.00 21.77           O  
-ATOM   2473  CB  ARG B 209     138.578  76.362 -43.481  1.00 28.89           C  
-ATOM   2474  CG  ARG B 209     139.243  77.294 -44.472  1.00 39.65           C  
-ATOM   2475  CD  ARG B 209     138.660  77.136 -45.871  1.00 48.34           C  
-ATOM   2476  NE  ARG B 209     139.430  77.880 -46.865  1.00 56.21           N  
-ATOM   2477  CZ  ARG B 209     139.314  79.188 -47.078  1.00 60.58           C  
-ATOM   2478  NH1 ARG B 209     138.457  79.906 -46.364  1.00 54.23           N  
-ATOM   2479  NH2 ARG B 209     140.057  79.780 -48.003  1.00 61.38           N  
-ATOM   2480  N   ASN B 210     140.946  77.784 -41.498  1.00 22.03           N  
-ATOM   2481  CA  ASN B 210     142.370  77.808 -41.182  1.00 19.34           C  
-ATOM   2482  C   ASN B 210     142.676  78.170 -39.735  1.00 20.40           C  
-ATOM   2483  O   ASN B 210     143.517  77.535 -39.099  1.00 23.29           O  
-ATOM   2484  CB  ASN B 210     143.098  78.758 -42.131  1.00 23.76           C  
-ATOM   2485  CG  ASN B 210     143.031  78.295 -43.576  1.00 32.92           C  
-ATOM   2486  OD1 ASN B 210     142.730  79.075 -44.479  1.00 37.36           O  
-ATOM   2487  ND2 ASN B 210     143.301  77.015 -43.798  1.00 29.28           N  
-ATOM   2488  N   THR B 211     141.985  79.184 -39.213  1.00 18.51           N  
-ATOM   2489  CA  THR B 211     142.240  79.674 -37.859  1.00 16.78           C  
-ATOM   2490  C   THR B 211     141.283  79.092 -36.823  1.00 16.25           C  
-ATOM   2491  O   THR B 211     141.518  79.193 -35.620  1.00 17.68           O  
-ATOM   2492  CB  THR B 211     142.103  81.199 -37.794  1.00 19.61           C  
-ATOM   2493  OG1 THR B 211     140.716  81.551 -37.903  1.00 16.34           O  
-ATOM   2494  CG2 THR B 211     142.868  81.851 -38.929  1.00 18.36           C  
-ATOM   2495  N   PHE B 212     140.193  78.502 -37.295  1.00 14.47           N  
-ATOM   2496  CA  PHE B 212     139.172  77.928 -36.420  1.00 13.67           C  
-ATOM   2497  C   PHE B 212     138.421  78.980 -35.606  1.00 11.33           C  
-ATOM   2498  O   PHE B 212     137.613  78.636 -34.748  1.00 12.48           O  
-ATOM   2499  CB  PHE B 212     139.776  76.855 -35.500  1.00 16.05           C  
-ATOM   2500  CG  PHE B 212     140.644  75.867 -36.233  1.00 19.55           C  
-ATOM   2501  CD1 PHE B 212     140.089  74.989 -37.144  1.00 21.79           C  
-ATOM   2502  CD2 PHE B 212     142.015  75.836 -36.024  1.00 24.84           C  
-ATOM   2503  CE1 PHE B 212     140.886  74.082 -37.835  1.00 25.55           C  
-ATOM   2504  CE2 PHE B 212     142.814  74.930 -36.705  1.00 29.88           C  
-ATOM   2505  CZ  PHE B 212     142.247  74.054 -37.610  1.00 25.18           C  
-ATOM   2506  N   ARG B 213     138.656  80.257 -35.895  1.00  9.36           N  
-ATOM   2507  CA  ARG B 213     137.935  81.303 -35.172  1.00 10.31           C  
-ATOM   2508  C   ARG B 213     136.502  81.472 -35.675  1.00 10.47           C  
-ATOM   2509  O   ARG B 213     136.205  81.191 -36.839  1.00  9.26           O  
-ATOM   2510  CB  ARG B 213     138.689  82.623 -35.228  1.00 10.26           C  
-ATOM   2511  CG  ARG B 213     139.986  82.591 -34.454  1.00 11.98           C  
-ATOM   2512  CD  ARG B 213     140.607  83.962 -34.429  1.00 13.40           C  
-ATOM   2513  NE  ARG B 213     141.961  83.948 -33.883  1.00 13.60           N  
-ATOM   2514  CZ  ARG B 213     142.251  84.089 -32.593  1.00 13.35           C  
-ATOM   2515  NH1 ARG B 213     141.279  84.213 -31.692  1.00  9.77           N  
-ATOM   2516  NH2 ARG B 213     143.524  84.087 -32.207  1.00 12.55           N  
-ATOM   2517  N   HIS B 214     135.623  81.919 -34.778  1.00  6.69           N  
-ATOM   2518  CA  HIS B 214     134.204  82.091 -35.091  1.00  5.94           C  
-ATOM   2519  C   HIS B 214     133.908  83.544 -35.375  1.00  6.62           C  
-ATOM   2520  O   HIS B 214     134.490  84.419 -34.761  1.00  7.71           O  
-ATOM   2521  CB  HIS B 214     133.342  81.705 -33.887  1.00  5.65           C  
-ATOM   2522  CG  HIS B 214     133.624  80.336 -33.353  1.00  7.21           C  
-ATOM   2523  ND1 HIS B 214     133.333  79.975 -32.057  1.00  9.03           N  
-ATOM   2524  CD2 HIS B 214     134.171  79.244 -33.938  1.00  9.10           C  
-ATOM   2525  CE1 HIS B 214     133.692  78.719 -31.861  1.00 10.98           C  
-ATOM   2526  NE2 HIS B 214     134.208  78.254 -32.987  1.00  9.65           N  
-ATOM   2527  N   SER B 215     132.975  83.794 -36.283  1.00  6.94           N  
-ATOM   2528  CA  SER B 215     132.455  85.141 -36.486  1.00  5.08           C  
-ATOM   2529  C   SER B 215     131.034  85.086 -37.021  1.00  7.83           C  
-ATOM   2530  O   SER B 215     130.586  84.051 -37.535  1.00  7.33           O  
-ATOM   2531  CB  SER B 215     133.357  85.930 -37.446  1.00  5.37           C  
-ATOM   2532  OG  SER B 215     133.513  85.241 -38.689  1.00  7.72           O  
-ATOM   2533  N   VAL B 216     130.338  86.214 -36.917  1.00  6.98           N  
-ATOM   2534  CA  VAL B 216     128.997  86.337 -37.481  1.00  4.95           C  
-ATOM   2535  C   VAL B 216     128.967  87.602 -38.339  1.00  6.55           C  
-ATOM   2536  O   VAL B 216     129.501  88.645 -37.942  1.00  8.41           O  
-ATOM   2537  CB  VAL B 216     127.912  86.360 -36.364  1.00  7.02           C  
-ATOM   2538  CG1 VAL B 216     128.188  87.486 -35.334  1.00  7.21           C  
-ATOM   2539  CG2 VAL B 216     126.518  86.491 -36.974  1.00  9.49           C  
-ATOM   2540  N   VAL B 217     128.367  87.500 -39.521  1.00  6.67           N  
-ATOM   2541  CA  VAL B 217     128.444  88.582 -40.495  1.00  6.21           C  
-ATOM   2542  C   VAL B 217     127.051  88.855 -41.077  1.00  9.79           C  
-ATOM   2543  O   VAL B 217     126.274  87.920 -41.315  1.00  8.78           O  
-ATOM   2544  CB  VAL B 217     129.500  88.262 -41.601  1.00  5.77           C  
-ATOM   2545  CG1 VAL B 217     129.166  86.943 -42.325  1.00  6.84           C  
-ATOM   2546  CG2 VAL B 217     129.648  89.427 -42.600  1.00  7.40           C  
-ATOM   2547  N   VAL B 218     126.722  90.133 -41.244  1.00  7.31           N  
-ATOM   2548  CA  VAL B 218     125.453  90.541 -41.857  1.00  7.74           C  
-ATOM   2549  C   VAL B 218     125.678  91.565 -42.958  1.00  7.25           C  
-ATOM   2550  O   VAL B 218     126.713  92.234 -42.996  1.00  8.59           O  
-ATOM   2551  CB  VAL B 218     124.480  91.174 -40.829  1.00  6.93           C  
-ATOM   2552  CG1 VAL B 218     123.996  90.120 -39.830  1.00 11.28           C  
-ATOM   2553  CG2 VAL B 218     125.126  92.356 -40.121  1.00 10.13           C  
-ATOM   2554  N   PRO B 219     124.700  91.704 -43.862  1.00  9.04           N  
-ATOM   2555  CA  PRO B 219     124.823  92.788 -44.839  1.00  8.32           C  
-ATOM   2556  C   PRO B 219     124.785  94.146 -44.142  1.00 10.66           C  
-ATOM   2557  O   PRO B 219     124.056  94.327 -43.161  1.00 12.13           O  
-ATOM   2558  CB  PRO B 219     123.573  92.611 -45.717  1.00 12.66           C  
-ATOM   2559  CG  PRO B 219     123.186  91.179 -45.556  1.00 14.67           C  
-ATOM   2560  CD  PRO B 219     123.547  90.826 -44.135  1.00 11.06           C  
-ATOM   2561  N   CYS B 220     125.583  95.087 -44.631  1.00 10.25           N  
-ATOM   2562  CA  CYS B 220     125.513  96.453 -44.145  1.00 12.66           C  
-ATOM   2563  C   CYS B 220     124.310  97.126 -44.805  1.00 22.60           C  
-ATOM   2564  O   CYS B 220     124.242  97.226 -46.032  1.00 25.00           O  
-ATOM   2565  CB  CYS B 220     126.805  97.203 -44.474  1.00 13.36           C  
-ATOM   2566  SG  CYS B 220     126.828  98.905 -43.841  1.00 18.92           S  
-ATOM   2567  N   GLU B 221     123.350  97.559 -43.997  1.00 17.98           N  
-ATOM   2568  CA  GLU B 221     122.133  98.171 -44.526  1.00 19.93           C  
-ATOM   2569  C   GLU B 221     122.080  99.648 -44.161  1.00 18.26           C  
-ATOM   2570  O   GLU B 221     122.655 100.065 -43.158  1.00 14.40           O  
-ATOM   2571  CB  GLU B 221     120.887  97.455 -43.986  1.00 24.88           C  
-ATOM   2572  CG  GLU B 221     120.573  96.128 -44.672  1.00 31.94           C  
-ATOM   2573  CD  GLU B 221     120.157  96.302 -46.127  1.00 44.78           C  
-ATOM   2574  OE1 GLU B 221     119.301  97.169 -46.405  1.00 50.88           O  
-ATOM   2575  OE2 GLU B 221     120.690  95.575 -46.996  1.00 49.56           O  
-ATOM   2576  N   PRO B 222     121.390 100.447 -44.983  1.00 18.52           N  
-ATOM   2577  CA  PRO B 222     121.209 101.877 -44.718  1.00 16.63           C  
-ATOM   2578  C   PRO B 222     120.319 102.135 -43.507  1.00 17.76           C  
-ATOM   2579  O   PRO B 222     119.472 101.311 -43.168  1.00 19.70           O  
-ATOM   2580  CB  PRO B 222     120.510 102.385 -45.989  1.00 24.56           C  
-ATOM   2581  CG  PRO B 222     120.765 101.342 -47.022  1.00 29.27           C  
-ATOM   2582  CD  PRO B 222     120.829 100.049 -46.286  1.00 26.05           C  
-ATOM   2583  N   PRO B 223     120.513 103.282 -42.846  1.00 16.77           N  
-ATOM   2584  CA  PRO B 223     119.672 103.652 -41.707  1.00 22.67           C  
-ATOM   2585  C   PRO B 223     118.195 103.687 -42.097  1.00 25.75           C  
-ATOM   2586  O   PRO B 223     117.875 104.012 -43.237  1.00 27.75           O  
-ATOM   2587  CB  PRO B 223     120.154 105.064 -41.362  1.00 18.88           C  
-ATOM   2588  CG  PRO B 223     121.557 105.118 -41.857  1.00 17.01           C  
-ATOM   2589  CD  PRO B 223     121.588 104.259 -43.094  1.00 14.98           C  
-ATOM   2590  N   GLU B 224     117.312 103.347 -41.167  1.00 26.79           N  
-ATOM   2591  CA  GLU B 224     115.885 103.487 -41.414  1.00 31.51           C  
-ATOM   2592  C   GLU B 224     115.580 104.968 -41.607  1.00 40.69           C  
-ATOM   2593  O   GLU B 224     116.330 105.831 -41.142  1.00 30.42           O  
-ATOM   2594  CB  GLU B 224     115.076 102.933 -40.242  1.00 36.94           C  
-ATOM   2595  CG  GLU B 224     115.572 101.598 -39.703  1.00 39.15           C  
-ATOM   2596  CD  GLU B 224     115.381 100.454 -40.683  1.00 53.58           C  
-ATOM   2597  OE1 GLU B 224     115.394 100.700 -41.909  1.00 57.21           O  
-ATOM   2598  OE2 GLU B 224     115.223  99.302 -40.225  1.00 60.60           O  
-ATOM   2599  N   VAL B 225     114.489 105.269 -42.302  1.00 43.15           N  
-ATOM   2600  CA  VAL B 225     114.112 106.659 -42.517  1.00 38.14           C  
-ATOM   2601  C   VAL B 225     113.972 107.361 -41.173  1.00 34.37           C  
-ATOM   2602  O   VAL B 225     113.307 106.857 -40.268  1.00 37.65           O  
-ATOM   2603  CB  VAL B 225     112.795 106.778 -43.301  1.00 40.55           C  
-ATOM   2604  CG1 VAL B 225     112.500 108.236 -43.614  1.00 50.03           C  
-ATOM   2605  CG2 VAL B 225     112.873 105.964 -44.585  1.00 45.09           C  
-ATOM   2606  N   GLY B 226     114.618 108.515 -41.040  1.00 36.60           N  
-ATOM   2607  CA  GLY B 226     114.556 109.281 -39.809  1.00 35.62           C  
-ATOM   2608  C   GLY B 226     115.619 108.870 -38.808  1.00 42.34           C  
-ATOM   2609  O   GLY B 226     115.565 109.252 -37.635  1.00 43.19           O  
-ATOM   2610  N   SER B 227     116.584 108.082 -39.273  1.00 34.47           N  
-ATOM   2611  CA  SER B 227     117.711 107.666 -38.445  1.00 31.76           C  
-ATOM   2612  C   SER B 227     119.022 108.014 -39.152  1.00 22.18           C  
-ATOM   2613  O   SER B 227     119.075 108.052 -40.383  1.00 25.49           O  
-ATOM   2614  CB  SER B 227     117.628 106.166 -38.150  1.00 30.84           C  
-ATOM   2615  OG  SER B 227     118.660 105.763 -37.269  1.00 36.53           O  
-ATOM   2616  N   ASP B 228     120.074 108.267 -38.375  1.00 18.64           N  
-ATOM   2617  CA  ASP B 228     121.356 108.703 -38.934  1.00 19.72           C  
-ATOM   2618  C   ASP B 228     122.401 107.589 -38.946  1.00 15.66           C  
-ATOM   2619  O   ASP B 228     123.489 107.750 -39.498  1.00 15.26           O  
-ATOM   2620  CB  ASP B 228     121.901 109.895 -38.139  1.00 20.09           C  
-ATOM   2621  CG  ASP B 228     121.015 111.122 -38.240  1.00 27.87           C  
-ATOM   2622  OD1 ASP B 228     120.488 111.384 -39.339  1.00 28.50           O  
-ATOM   2623  OD2 ASP B 228     120.855 111.825 -37.219  1.00 29.91           O  
-ATOM   2624  N   CYS B 229     122.081 106.473 -38.305  1.00 16.86           N  
-ATOM   2625  CA  CYS B 229     122.999 105.346 -38.262  1.00 15.54           C  
-ATOM   2626  C   CYS B 229     122.226 104.039 -38.337  1.00 14.88           C  
-ATOM   2627  O   CYS B 229     120.996 104.022 -38.227  1.00 16.37           O  
-ATOM   2628  CB  CYS B 229     123.834 105.381 -36.977  1.00 14.17           C  
-ATOM   2629  SG  CYS B 229     122.890 105.057 -35.465  1.00 15.65           S  
-ATOM   2630  N   THR B 230     122.959 102.947 -38.524  1.00 12.07           N  
-ATOM   2631  CA  THR B 230     122.363 101.617 -38.562  1.00 12.01           C  
-ATOM   2632  C   THR B 230     122.738 100.891 -37.279  1.00 11.45           C  
-ATOM   2633  O   THR B 230     123.840 101.063 -36.758  1.00 13.64           O  
-ATOM   2634  CB  THR B 230     122.869 100.832 -39.775  1.00 12.80           C  
-ATOM   2635  OG1 THR B 230     122.423 101.485 -40.972  1.00 15.28           O  
-ATOM   2636  CG2 THR B 230     122.329  99.404 -39.772  1.00 14.56           C  
-ATOM   2637  N   THR B 231     121.812 100.099 -36.759  1.00 10.21           N  
-ATOM   2638  CA  THR B 231     122.056  99.404 -35.501  1.00  9.54           C  
-ATOM   2639  C   THR B 231     122.002  97.892 -35.734  1.00 14.04           C  
-ATOM   2640  O   THR B 231     121.131  97.399 -36.447  1.00 12.64           O  
-ATOM   2641  CB  THR B 231     121.035  99.830 -34.426  1.00 13.20           C  
-ATOM   2642  OG1 THR B 231     121.198 101.227 -34.129  1.00 16.72           O  
-ATOM   2643  CG2 THR B 231     121.226  99.022 -33.143  1.00 16.47           C  
-ATOM   2644  N   ILE B 232     122.962  97.167 -35.162  1.00 10.89           N  
-ATOM   2645  CA  ILE B 232     122.929  95.713 -35.171  1.00 10.25           C  
-ATOM   2646  C   ILE B 232     122.706  95.286 -33.730  1.00 11.07           C  
-ATOM   2647  O   ILE B 232     123.283  95.877 -32.820  1.00 11.34           O  
-ATOM   2648  CB  ILE B 232     124.269  95.114 -35.656  1.00  8.75           C  
-ATOM   2649  CG1 ILE B 232     124.561  95.548 -37.097  1.00 15.13           C  
-ATOM   2650  CG2 ILE B 232     124.242  93.579 -35.545  1.00 10.15           C  
-ATOM   2651  CD1 ILE B 232     125.888  95.013 -37.642  1.00 14.13           C  
-ATOM   2652  N   HIS B 233     121.865  94.274 -33.520  1.00  9.37           N  
-ATOM   2653  CA  HIS B 233     121.651  93.745 -32.174  1.00 10.83           C  
-ATOM   2654  C   HIS B 233     122.462  92.480 -31.974  1.00  9.35           C  
-ATOM   2655  O   HIS B 233     122.216  91.475 -32.649  1.00 10.61           O  
-ATOM   2656  CB  HIS B 233     120.169  93.432 -31.940  1.00 12.16           C  
-ATOM   2657  CG  HIS B 233     119.318  94.651 -31.772  1.00 18.70           C  
-ATOM   2658  ND1 HIS B 233     117.940  94.609 -31.788  1.00 32.20           N  
-ATOM   2659  CD2 HIS B 233     119.653  95.949 -31.580  1.00 22.16           C  
-ATOM   2660  CE1 HIS B 233     117.464  95.830 -31.613  1.00 31.76           C  
-ATOM   2661  NE2 HIS B 233     118.483  96.661 -31.490  1.00 22.91           N  
-ATOM   2662  N   TYR B 234     123.417  92.526 -31.047  1.00  9.16           N  
-ATOM   2663  CA  TYR B 234     124.241  91.358 -30.749  1.00  9.85           C  
-ATOM   2664  C   TYR B 234     123.787  90.706 -29.451  1.00  9.07           C  
-ATOM   2665  O   TYR B 234     123.215  91.371 -28.578  1.00 10.45           O  
-ATOM   2666  CB  TYR B 234     125.727  91.740 -30.641  1.00  7.84           C  
-ATOM   2667  CG  TYR B 234     126.372  92.104 -31.958  1.00  6.34           C  
-ATOM   2668  CD1 TYR B 234     126.608  91.129 -32.940  1.00  6.36           C  
-ATOM   2669  CD2 TYR B 234     126.752  93.411 -32.225  1.00 10.04           C  
-ATOM   2670  CE1 TYR B 234     127.206  91.460 -34.148  1.00  8.48           C  
-ATOM   2671  CE2 TYR B 234     127.336  93.753 -33.434  1.00  8.20           C  
-ATOM   2672  CZ  TYR B 234     127.567  92.769 -34.391  1.00  7.00           C  
-ATOM   2673  OH  TYR B 234     128.156  93.117 -35.581  1.00  7.64           O  
-ATOM   2674  N   ASN B 235     124.027  89.404 -29.343  1.00  7.29           N  
-ATOM   2675  CA  ASN B 235     123.824  88.671 -28.081  1.00  9.77           C  
-ATOM   2676  C   ASN B 235     125.124  87.953 -27.719  1.00 10.38           C  
-ATOM   2677  O   ASN B 235     125.736  87.311 -28.588  1.00 11.29           O  
-ATOM   2678  CB  ASN B 235     122.736  87.596 -28.224  1.00 10.99           C  
-ATOM   2679  CG  ASN B 235     121.357  88.146 -28.604  1.00 15.92           C  
-ATOM   2680  OD1 ASN B 235     120.557  87.423 -29.196  1.00 22.05           O  
-ATOM   2681  ND2 ASN B 235     121.062  89.391 -28.243  1.00 12.95           N  
-ATOM   2682  N   TYR B 236     125.531  88.018 -26.452  1.00  9.19           N  
-ATOM   2683  CA  TYR B 236     126.698  87.262 -25.979  1.00  7.40           C  
-ATOM   2684  C   TYR B 236     126.209  86.078 -25.154  1.00 10.18           C  
-ATOM   2685  O   TYR B 236     125.433  86.254 -24.216  1.00 10.04           O  
-ATOM   2686  CB  TYR B 236     127.644  88.166 -25.163  1.00  6.16           C  
-ATOM   2687  CG  TYR B 236     128.324  89.212 -26.026  1.00  7.23           C  
-ATOM   2688  CD1 TYR B 236     127.681  90.408 -26.338  1.00  7.15           C  
-ATOM   2689  CD2 TYR B 236     129.590  88.992 -26.559  1.00  7.53           C  
-ATOM   2690  CE1 TYR B 236     128.285  91.365 -27.157  1.00  9.55           C  
-ATOM   2691  CE2 TYR B 236     130.207  89.954 -27.378  1.00  7.73           C  
-ATOM   2692  CZ  TYR B 236     129.545  91.134 -27.668  1.00  9.51           C  
-ATOM   2693  OH  TYR B 236     130.137  92.095 -28.460  1.00  8.57           O  
-ATOM   2694  N   MET B 237     126.668  84.874 -25.493  1.00  7.05           N  
-ATOM   2695  CA  MET B 237     125.998  83.649 -25.030  1.00  7.99           C  
-ATOM   2696  C   MET B 237     126.712  82.878 -23.918  1.00 11.54           C  
-ATOM   2697  O   MET B 237     126.348  81.738 -23.633  1.00 10.26           O  
-ATOM   2698  CB  MET B 237     125.745  82.717 -26.224  1.00  8.65           C  
-ATOM   2699  CG  MET B 237     124.969  83.381 -27.370  1.00  9.55           C  
-ATOM   2700  SD  MET B 237     123.355  84.024 -26.857  1.00 12.51           S  
-ATOM   2701  CE  MET B 237     122.592  82.548 -26.180  1.00 17.70           C  
-ATOM   2702  N   CYS B 238     127.726  83.489 -23.309  1.00  8.78           N  
-ATOM   2703  CA  CYS B 238     128.351  82.977 -22.084  1.00  6.65           C  
-ATOM   2704  C   CYS B 238     128.669  84.154 -21.171  1.00  9.47           C  
-ATOM   2705  O   CYS B 238     128.866  85.264 -21.646  1.00 10.30           O  
-ATOM   2706  CB  CYS B 238     129.681  82.285 -22.395  1.00 11.81           C  
-ATOM   2707  SG  CYS B 238     129.589  80.506 -22.683  1.00 10.08           S  
-ATOM   2708  N   TYR B 239     128.735  83.899 -19.863  1.00 10.26           N  
-ATOM   2709  CA  TYR B 239     129.266  84.872 -18.912  1.00 10.96           C  
-ATOM   2710  C   TYR B 239     130.780  84.951 -19.061  1.00  9.94           C  
-ATOM   2711  O   TYR B 239     131.421  83.962 -19.419  1.00 10.37           O  
-ATOM   2712  CB  TYR B 239     128.951  84.436 -17.473  1.00  8.94           C  
-ATOM   2713  CG  TYR B 239     127.512  84.644 -17.072  1.00 12.55           C  
-ATOM   2714  CD1 TYR B 239     126.993  85.926 -16.948  1.00 15.22           C  
-ATOM   2715  CD2 TYR B 239     126.677  83.566 -16.794  1.00 15.83           C  
-ATOM   2716  CE1 TYR B 239     125.676  86.134 -16.574  1.00 18.64           C  
-ATOM   2717  CE2 TYR B 239     125.354  83.764 -16.418  1.00 15.41           C  
-ATOM   2718  CZ  TYR B 239     124.861  85.050 -16.313  1.00 19.06           C  
-ATOM   2719  OH  TYR B 239     123.553  85.270 -15.942  1.00 20.00           O  
-ATOM   2720  N   SER B 240     131.360  86.110 -18.752  1.00  8.34           N  
-ATOM   2721  CA  SER B 240     132.811  86.222 -18.706  1.00  9.35           C  
-ATOM   2722  C   SER B 240     133.412  85.179 -17.765  1.00  9.52           C  
-ATOM   2723  O   SER B 240     134.516  84.685 -17.997  1.00 11.23           O  
-ATOM   2724  CB  SER B 240     133.237  87.628 -18.271  1.00 12.17           C  
-ATOM   2725  OG  SER B 240     133.038  88.552 -19.333  1.00 11.76           O  
-ATOM   2726  N   SER B 241     132.664  84.842 -16.720  1.00  8.71           N  
-ATOM   2727  CA  SER B 241     133.140  83.929 -15.691  1.00 11.56           C  
-ATOM   2728  C   SER B 241     132.998  82.441 -16.024  1.00 14.82           C  
-ATOM   2729  O   SER B 241     133.453  81.607 -15.251  1.00 14.65           O  
-ATOM   2730  CB  SER B 241     132.392  84.202 -14.379  1.00 14.13           C  
-ATOM   2731  OG  SER B 241     131.016  83.893 -14.537  1.00 15.33           O  
-ATOM   2732  N   CYS B 242     132.375  82.093 -17.146  1.00 10.63           N  
-ATOM   2733  CA  CYS B 242     132.088  80.673 -17.407  1.00 12.52           C  
-ATOM   2734  C   CYS B 242     133.329  79.772 -17.356  1.00 14.85           C  
-ATOM   2735  O   CYS B 242     134.283  79.960 -18.106  1.00 13.26           O  
-ATOM   2736  CB  CYS B 242     131.382  80.486 -18.753  1.00 10.95           C  
-ATOM   2737  SG  CYS B 242     129.598  80.790 -18.740  1.00 11.71           S  
-ATOM   2738  N   MET B 243     133.312  78.777 -16.471  1.00 13.96           N  
-ATOM   2739  CA  MET B 243     134.453  77.877 -16.355  1.00 14.73           C  
-ATOM   2740  C   MET B 243     134.582  77.012 -17.609  1.00 11.30           C  
-ATOM   2741  O   MET B 243     133.587  76.515 -18.139  1.00 11.67           O  
-ATOM   2742  CB  MET B 243     134.324  77.005 -15.100  1.00 15.14           C  
-ATOM   2743  CG  MET B 243     134.407  77.803 -13.807  1.00 25.79           C  
-ATOM   2744  SD  MET B 243     135.950  78.746 -13.727  1.00 45.95           S  
-ATOM   2745  CE  MET B 243     137.147  77.407 -13.767  1.00 31.08           C  
-ATOM   2746  N   GLY B 244     135.809  76.837 -18.082  1.00 14.07           N  
-ATOM   2747  CA  GLY B 244     136.053  76.061 -19.284  1.00 15.54           C  
-ATOM   2748  C   GLY B 244     135.853  76.854 -20.565  1.00 16.71           C  
-ATOM   2749  O   GLY B 244     136.156  76.369 -21.660  1.00 17.91           O  
-ATOM   2750  N   GLY B 245     135.334  78.074 -20.437  1.00 14.39           N  
-ATOM   2751  CA  GLY B 245     135.200  78.970 -21.575  1.00 10.93           C  
-ATOM   2752  C   GLY B 245     136.063  80.198 -21.338  1.00 10.80           C  
-ATOM   2753  O   GLY B 245     137.275  80.076 -21.158  1.00 14.02           O  
-ATOM   2754  N   MET B 246     135.446  81.382 -21.314  1.00  9.73           N  
-ATOM   2755  CA  MET B 246     136.204  82.610 -21.054  1.00  9.14           C  
-ATOM   2756  C   MET B 246     136.946  82.571 -19.711  1.00 12.87           C  
-ATOM   2757  O   MET B 246     138.046  83.103 -19.592  1.00 12.10           O  
-ATOM   2758  CB  MET B 246     135.320  83.864 -21.209  1.00  9.00           C  
-ATOM   2759  CG  MET B 246     134.991  84.144 -22.685  1.00  9.88           C  
-ATOM   2760  SD  MET B 246     133.943  85.584 -22.946  1.00 10.70           S  
-ATOM   2761  CE  MET B 246     132.336  84.980 -22.406  1.00  9.59           C  
-ATOM   2762  N   ASN B 247     136.348  81.931 -18.710  1.00 14.42           N  
-ATOM   2763  C   ASN B 247     137.635  82.952 -16.813  1.00 17.04           C  
-ATOM   2764  O   ASN B 247     138.803  82.949 -16.405  1.00 16.35           O  
-ATOM   2765  CA AASN B 247     137.003  81.704 -17.416  0.51 16.93           C  
-ATOM   2766  CB AASN B 247     138.044  80.586 -17.508  0.51 19.23           C  
-ATOM   2767  CG AASN B 247     138.626  80.215 -16.144  0.51 24.40           C  
-ATOM   2768  OD1AASN B 247     138.039  80.514 -15.100  0.51 23.47           O  
-ATOM   2769  ND2AASN B 247     139.785  79.567 -16.151  0.51 22.28           N  
-ATOM   2770  CA BASN B 247     137.046  81.690 -17.453  0.49 16.93           C  
-ATOM   2771  CB BASN B 247     138.164  80.679 -17.702  0.49 18.88           C  
-ATOM   2772  CG BASN B 247     138.265  79.636 -16.611  0.49 25.73           C  
-ATOM   2773  OD1BASN B 247     138.149  78.439 -16.873  0.49 25.82           O  
-ATOM   2774  ND2BASN B 247     138.487  80.084 -15.379  0.49 25.24           N  
-ATOM   2775  N   ARG B 248     136.839  84.018 -16.745  1.00 13.74           N  
-ATOM   2776  CA  ARG B 248     137.226  85.294 -16.136  1.00 14.77           C  
-ATOM   2777  C   ARG B 248     138.207  86.125 -16.971  1.00 15.83           C  
-ATOM   2778  O   ARG B 248     138.648  87.197 -16.540  1.00 19.62           O  
-ATOM   2779  CB  ARG B 248     137.774  85.094 -14.712  1.00 14.28           C  
-ATOM   2780  CG  ARG B 248     137.051  84.028 -13.911  1.00 24.42           C  
-ATOM   2781  CD  ARG B 248     137.288  84.220 -12.415  1.00 27.84           C  
-ATOM   2782  NE  ARG B 248     136.414  85.266 -11.900  1.00 43.88           N  
-ATOM   2783  CZ  ARG B 248     135.229  85.038 -11.338  1.00 46.96           C  
-ATOM   2784  NH1 ARG B 248     134.784  83.794 -11.202  1.00 41.00           N  
-ATOM   2785  NH2 ARG B 248     134.492  86.052 -10.906  1.00 57.11           N  
-ATOM   2786  N   ARG B 249     138.543  85.640 -18.164  1.00 13.62           N  
-ATOM   2787  CA  ARG B 249     139.475  86.351 -19.035  1.00 13.12           C  
-ATOM   2788  C   ARG B 249     138.739  87.381 -19.881  1.00 12.59           C  
-ATOM   2789  O   ARG B 249     137.763  87.052 -20.548  1.00 13.78           O  
-ATOM   2790  CB  ARG B 249     140.209  85.371 -19.951  1.00 11.67           C  
-ATOM   2791  CG  ARG B 249     141.079  84.368 -19.199  1.00 15.62           C  
-ATOM   2792  CD  ARG B 249     141.680  83.359 -20.167  1.00 15.86           C  
-ATOM   2793  NE  ARG B 249     140.667  82.462 -20.713  1.00 13.44           N  
-ATOM   2794  CZ  ARG B 249     140.928  81.504 -21.596  1.00 15.66           C  
-ATOM   2795  NH1 ARG B 249     142.169  81.326 -22.025  1.00 14.20           N  
-ATOM   2796  NH2 ARG B 249     139.957  80.724 -22.042  1.00 15.32           N  
-ATOM   2797  N   PRO B 250     139.203  88.632 -19.853  1.00 12.00           N  
-ATOM   2798  CA  PRO B 250     138.582  89.677 -20.675  1.00 10.37           C  
-ATOM   2799  C   PRO B 250     138.734  89.419 -22.164  1.00  8.94           C  
-ATOM   2800  O   PRO B 250     139.769  88.930 -22.636  1.00  9.02           O  
-ATOM   2801  CB  PRO B 250     139.353  90.948 -20.287  1.00 14.31           C  
-ATOM   2802  CG  PRO B 250     140.612  90.456 -19.613  1.00 21.75           C  
-ATOM   2803  CD  PRO B 250     140.229  89.174 -18.945  1.00 16.10           C  
-ATOM   2804  N   ILE B 251     137.691  89.776 -22.904  1.00 10.22           N  
-ATOM   2805  CA  ILE B 251     137.723  89.692 -24.359  1.00  7.20           C  
-ATOM   2806  C   ILE B 251     137.485  91.054 -24.992  1.00  7.86           C  
-ATOM   2807  O   ILE B 251     137.063  92.004 -24.329  1.00 10.15           O  
-ATOM   2808  CB  ILE B 251     136.645  88.746 -24.899  1.00  8.67           C  
-ATOM   2809  CG1 ILE B 251     135.247  89.221 -24.458  1.00  9.59           C  
-ATOM   2810  CG2 ILE B 251     136.921  87.312 -24.439  1.00  8.15           C  
-ATOM   2811  CD1 ILE B 251     134.111  88.699 -25.331  1.00 12.12           C  
-ATOM   2812  N   LEU B 252     137.785  91.129 -26.282  1.00  7.65           N  
-ATOM   2813  CA  LEU B 252     137.426  92.261 -27.122  1.00 10.38           C  
-ATOM   2814  C   LEU B 252     136.546  91.727 -28.235  1.00  8.52           C  
-ATOM   2815  O   LEU B 252     136.737  90.592 -28.692  1.00  9.88           O  
-ATOM   2816  CB  LEU B 252     138.679  92.874 -27.753  1.00 11.80           C  
-ATOM   2817  CG  LEU B 252     139.820  93.198 -26.789  1.00 21.39           C  
-ATOM   2818  CD1 LEU B 252     141.110  93.456 -27.555  1.00 29.64           C  
-ATOM   2819  CD2 LEU B 252     139.441  94.388 -25.926  1.00 25.18           C  
-ATOM   2820  N   THR B 253     135.590  92.540 -28.680  1.00  7.66           N  
-ATOM   2821  CA  THR B 253     134.886  92.257 -29.923  1.00  5.89           C  
-ATOM   2822  C   THR B 253     135.481  93.177 -30.977  1.00  7.20           C  
-ATOM   2823  O   THR B 253     135.624  94.373 -30.739  1.00  7.36           O  
-ATOM   2824  CB  THR B 253     133.367  92.545 -29.804  1.00  5.47           C  
-ATOM   2825  OG1 THR B 253     132.796  91.677 -28.812  1.00  6.68           O  
-ATOM   2826  CG2 THR B 253     132.666  92.293 -31.139  1.00  6.88           C  
-ATOM   2827  N   ILE B 254     135.848  92.604 -32.122  1.00  5.27           N  
-ATOM   2828  CA  ILE B 254     136.352  93.360 -33.265  1.00  5.90           C  
-ATOM   2829  C   ILE B 254     135.241  93.409 -34.305  1.00  5.61           C  
-ATOM   2830  O   ILE B 254     134.702  92.372 -34.681  1.00  5.19           O  
-ATOM   2831  CB  ILE B 254     137.600  92.686 -33.863  1.00  5.76           C  
-ATOM   2832  CG1 ILE B 254     138.686  92.556 -32.784  1.00 10.71           C  
-ATOM   2833  CG2 ILE B 254     138.121  93.501 -35.071  1.00  7.65           C  
-ATOM   2834  CD1 ILE B 254     139.810  91.585 -33.136  1.00 11.71           C  
-ATOM   2835  N   ILE B 255     134.884  94.614 -34.750  1.00  5.98           N  
-ATOM   2836  CA  ILE B 255     133.867  94.764 -35.788  1.00  6.05           C  
-ATOM   2837  C   ILE B 255     134.552  95.228 -37.045  1.00  8.73           C  
-ATOM   2838  O   ILE B 255     135.242  96.245 -37.038  1.00  9.15           O  
-ATOM   2839  CB  ILE B 255     132.793  95.808 -35.414  1.00  8.36           C  
-ATOM   2840  CG1 ILE B 255     132.128  95.444 -34.094  1.00  8.97           C  
-ATOM   2841  CG2 ILE B 255     131.761  95.938 -36.542  1.00  7.49           C  
-ATOM   2842  CD1 ILE B 255     131.462  94.094 -34.078  1.00 11.44           C  
-ATOM   2843  N   THR B 256     134.387  94.468 -38.120  1.00  7.69           N  
-ATOM   2844  C   THR B 256     133.978  95.119 -40.473  1.00  9.17           C  
-ATOM   2845  O   THR B 256     133.002  94.383 -40.636  1.00  8.57           O  
-ATOM   2846  CA ATHR B 256     135.001  94.852 -39.383  0.63  7.74           C  
-ATOM   2847  CB ATHR B 256     136.021  93.810 -39.861  0.63  9.52           C  
-ATOM   2848  OG1ATHR B 256     135.417  92.516 -39.863  0.63  6.82           O  
-ATOM   2849  CG2ATHR B 256     137.210  93.784 -38.923  0.63 10.78           C  
-ATOM   2850  CA BTHR B 256     135.012  94.795 -39.399  0.37  7.76           C  
-ATOM   2851  CB BTHR B 256     135.871  93.624 -39.916  0.37  9.35           C  
-ATOM   2852  OG1BTHR B 256     136.886  93.299 -38.956  0.37  9.44           O  
-ATOM   2853  CG2BTHR B 256     136.526  93.993 -41.234  0.37 10.06           C  
-ATOM   2854  N   LEU B 257     134.203  96.210 -41.202  1.00  6.81           N  
-ATOM   2855  CA  LEU B 257     133.415  96.527 -42.383  1.00  7.65           C  
-ATOM   2856  C   LEU B 257     134.156  95.879 -43.560  1.00  8.61           C  
-ATOM   2857  O   LEU B 257     135.363  96.074 -43.711  1.00 10.60           O  
-ATOM   2858  CB  LEU B 257     133.315  98.050 -42.547  1.00  8.83           C  
-ATOM   2859  CG  LEU B 257     132.357  98.522 -43.642  1.00 10.67           C  
-ATOM   2860  CD1 LEU B 257     130.907  98.284 -43.208  1.00 10.79           C  
-ATOM   2861  CD2 LEU B 257     132.588 100.003 -43.964  1.00  9.79           C  
-ATOM   2862  N   GLU B 258     133.450  95.070 -44.349  1.00  7.24           N  
-ATOM   2863  CA  GLU B 258     134.080  94.266 -45.416  1.00  9.75           C  
-ATOM   2864  C   GLU B 258     133.401  94.485 -46.756  1.00  8.53           C  
-ATOM   2865  O   GLU B 258     132.196  94.731 -46.801  1.00  9.82           O  
-ATOM   2866  CB  GLU B 258     133.956  92.763 -45.118  1.00 10.92           C  
-ATOM   2867  CG  GLU B 258     134.734  92.254 -43.924  1.00 15.02           C  
-ATOM   2868  CD  GLU B 258     134.521  90.752 -43.708  1.00 10.76           C  
-ATOM   2869  OE1 GLU B 258     133.629  90.159 -44.367  1.00 14.28           O  
-ATOM   2870  OE2 GLU B 258     135.266  90.166 -42.899  1.00 18.42           O  
-ATOM   2871  N   ASP B 259     134.148  94.353 -47.851  1.00  9.20           N  
-ATOM   2872  CA  ASP B 259     133.496  94.277 -49.164  1.00  7.70           C  
-ATOM   2873  C   ASP B 259     132.937  92.865 -49.406  1.00  9.60           C  
-ATOM   2874  O   ASP B 259     133.032  91.986 -48.537  1.00  8.90           O  
-ATOM   2875  CB  ASP B 259     134.401  94.776 -50.315  1.00  9.51           C  
-ATOM   2876  CG  ASP B 259     135.585  93.846 -50.604  1.00 11.32           C  
-ATOM   2877  OD1 ASP B 259     135.569  92.660 -50.193  1.00 10.65           O  
-ATOM   2878  OD2 ASP B 259     136.536  94.308 -51.280  1.00 13.02           O  
-ATOM   2879  N   SER B 260     132.325  92.644 -50.566  1.00  9.82           N  
-ATOM   2880  CA  SER B 260     131.650  91.373 -50.820  1.00  8.83           C  
-ATOM   2881  C   SER B 260     132.582  90.165 -50.919  1.00 11.31           C  
-ATOM   2882  O   SER B 260     132.112  89.022 -50.824  1.00 11.32           O  
-ATOM   2883  CB  SER B 260     130.779  91.468 -52.081  1.00 11.12           C  
-ATOM   2884  OG  SER B 260     131.559  91.822 -53.218  1.00 10.19           O  
-ATOM   2885  N   SER B 261     133.881  90.412 -51.108  1.00 10.03           N  
-ATOM   2886  CA  SER B 261     134.894  89.350 -51.110  1.00 12.01           C  
-ATOM   2887  C   SER B 261     135.436  89.079 -49.712  1.00 11.04           C  
-ATOM   2888  O   SER B 261     136.160  88.108 -49.508  1.00 10.46           O  
-ATOM   2889  CB  SER B 261     136.089  89.735 -51.995  1.00 13.12           C  
-ATOM   2890  OG  SER B 261     135.740  89.778 -53.370  1.00 13.12           O  
-ATOM   2891  N   GLY B 262     135.114  89.957 -48.764  1.00 10.08           N  
-ATOM   2892  CA  GLY B 262     135.647  89.849 -47.412  1.00  8.41           C  
-ATOM   2893  C   GLY B 262     136.882  90.708 -47.171  1.00 11.63           C  
-ATOM   2894  O   GLY B 262     137.510  90.614 -46.116  1.00 12.41           O  
-ATOM   2895  N   ASN B 263     137.242  91.553 -48.137  1.00  8.94           N  
-ATOM   2896  CA  ASN B 263     138.398  92.422 -47.953  1.00 10.04           C  
-ATOM   2897  C   ASN B 263     138.080  93.538 -46.970  1.00  9.93           C  
-ATOM   2898  O   ASN B 263     136.952  94.021 -46.914  1.00 10.32           O  
-ATOM   2899  CB  ASN B 263     138.839  93.044 -49.276  1.00  9.33           C  
-ATOM   2900  CG  ASN B 263     139.255  92.006 -50.301  1.00 18.22           C  
-ATOM   2901  OD1 ASN B 263     140.075  91.135 -50.021  1.00 21.40           O  
-ATOM   2902  ND2 ASN B 263     138.691  92.100 -51.496  1.00 18.77           N  
-ATOM   2903  N   LEU B 264     139.088  93.955 -46.215  1.00 10.46           N  
-ATOM   2904  CA  LEU B 264     138.899  94.968 -45.170  1.00  9.74           C  
-ATOM   2905  C   LEU B 264     138.565  96.357 -45.717  1.00 13.45           C  
-ATOM   2906  O   LEU B 264     139.272  96.871 -46.585  1.00 16.78           O  
-ATOM   2907  CB  LEU B 264     140.159  95.062 -44.315  1.00 12.88           C  
-ATOM   2908  CG  LEU B 264     140.030  96.080 -43.177  1.00 17.61           C  
-ATOM   2909  CD1 LEU B 264     139.305  95.453 -42.013  1.00 18.25           C  
-ATOM   2910  CD2 LEU B 264     141.395  96.592 -42.752  1.00 25.00           C  
-ATOM   2911  N   LEU B 265     137.496  96.966 -45.198  1.00  8.38           N  
-ATOM   2912  CA  LEU B 265     137.180  98.364 -45.488  1.00  8.53           C  
-ATOM   2913  C   LEU B 265     137.325  99.244 -44.243  1.00 10.56           C  
-ATOM   2914  O   LEU B 265     137.616 100.424 -44.357  1.00 11.72           O  
-ATOM   2915  CB  LEU B 265     135.765  98.524 -46.040  1.00  8.68           C  
-ATOM   2916  CG  LEU B 265     135.445  97.756 -47.326  1.00 11.27           C  
-ATOM   2917  CD1 LEU B 265     133.972  97.910 -47.678  1.00 10.33           C  
-ATOM   2918  CD2 LEU B 265     136.341  98.227 -48.483  1.00 13.23           C  
-ATOM   2919  N   GLY B 266     137.124  98.664 -43.064  1.00  7.65           N  
-ATOM   2920  CA  GLY B 266     137.183  99.449 -41.832  1.00  8.17           C  
-ATOM   2921  C   GLY B 266     137.166  98.544 -40.622  1.00  7.36           C  
-ATOM   2922  O   GLY B 266     136.730  97.394 -40.714  1.00  8.97           O  
-ATOM   2923  N   ARG B 267     137.628  99.060 -39.482  1.00  7.17           N  
-ATOM   2924  CA  ARG B 267     137.759  98.225 -38.283  1.00  7.21           C  
-ATOM   2925  C   ARG B 267     137.614  99.059 -37.019  1.00  8.34           C  
-ATOM   2926  O   ARG B 267     138.093 100.193 -36.965  1.00  8.40           O  
-ATOM   2927  CB  ARG B 267     139.125  97.515 -38.275  1.00  8.56           C  
-ATOM   2928  CG  ARG B 267     139.249  96.407 -37.228  1.00 10.95           C  
-ATOM   2929  CD  ARG B 267     140.704  95.946 -37.026  1.00 14.99           C  
-ATOM   2930  NE  ARG B 267     141.313  95.339 -38.211  1.00 16.97           N  
-ATOM   2931  CZ  ARG B 267     142.303  95.883 -38.916  1.00 14.98           C  
-ATOM   2932  NH1 ARG B 267     142.793  97.070 -38.589  1.00 16.19           N  
-ATOM   2933  NH2 ARG B 267     142.796  95.242 -39.967  1.00 21.26           N  
-ATOM   2934  N   ASP B 268     136.979  98.487 -35.998  1.00  7.09           N  
-ATOM   2935  CA  ASP B 268     136.845  99.147 -34.692  1.00  8.62           C  
-ATOM   2936  C   ASP B 268     136.709  98.005 -33.689  1.00  7.10           C  
-ATOM   2937  O   ASP B 268     136.579  96.839 -34.091  1.00  7.80           O  
-ATOM   2938  CB  ASP B 268     135.614 100.061 -34.693  1.00  7.24           C  
-ATOM   2939  CG  ASP B 268     135.667 101.156 -33.619  1.00 10.08           C  
-ATOM   2940  OD1 ASP B 268     136.520 101.095 -32.705  1.00  9.59           O  
-ATOM   2941  OD2 ASP B 268     134.837 102.090 -33.705  1.00 10.39           O  
-ATOM   2942  N   SER B 269     136.761  98.307 -32.397  1.00  6.20           N  
-ATOM   2943  CA  SER B 269     136.726  97.251 -31.390  1.00  5.93           C  
-ATOM   2944  C   SER B 269     136.347  97.833 -30.038  1.00  6.90           C  
-ATOM   2945  O   SER B 269     136.459  99.041 -29.821  1.00  8.90           O  
-ATOM   2946  CB  SER B 269     138.094  96.560 -31.285  1.00  8.00           C  
-ATOM   2947  OG  SER B 269     139.077  97.459 -30.792  1.00 11.67           O  
-ATOM   2948  N   PHE B 270     135.895  96.962 -29.136  1.00  7.46           N  
-ATOM   2949  CA  PHE B 270     135.541  97.337 -27.766  1.00  6.69           C  
-ATOM   2950  C   PHE B 270     135.694  96.128 -26.849  1.00  7.62           C  
-ATOM   2951  O   PHE B 270     135.510  94.988 -27.279  1.00  7.52           O  
-ATOM   2952  CB  PHE B 270     134.099  97.888 -27.681  1.00  8.70           C  
-ATOM   2953  CG  PHE B 270     133.041  96.984 -28.300  1.00  7.39           C  
-ATOM   2954  CD1 PHE B 270     132.825  96.985 -29.674  1.00  6.50           C  
-ATOM   2955  CD2 PHE B 270     132.246  96.161 -27.505  1.00  7.16           C  
-ATOM   2956  CE1 PHE B 270     131.851  96.162 -30.253  1.00  8.06           C  
-ATOM   2957  CE2 PHE B 270     131.266  95.342 -28.065  1.00  6.97           C  
-ATOM   2958  CZ  PHE B 270     131.062  95.340 -29.445  1.00  7.17           C  
-ATOM   2959  N   GLU B 271     136.032  96.374 -25.585  1.00  6.14           N  
-ATOM   2960  CA  GLU B 271     136.093  95.283 -24.602  1.00  6.76           C  
-ATOM   2961  C   GLU B 271     134.674  94.889 -24.209  1.00  6.95           C  
-ATOM   2962  O   GLU B 271     133.760  95.704 -24.305  1.00  7.44           O  
-ATOM   2963  CB  GLU B 271     136.917  95.702 -23.370  1.00  7.03           C  
-ATOM   2964  CG  GLU B 271     137.180  94.552 -22.377  1.00 17.24           C  
-ATOM   2965  CD  GLU B 271     138.068  94.967 -21.212  1.00 23.97           C  
-ATOM   2966  OE1 GLU B 271     138.774  95.991 -21.347  1.00 19.53           O  
-ATOM   2967  OE2 GLU B 271     138.059  94.270 -20.162  1.00 21.32           O  
-ATOM   2968  N   VAL B 272     134.488  93.645 -23.766  1.00  6.35           N  
-ATOM   2969  CA  VAL B 272     133.178  93.182 -23.318  1.00  6.48           C  
-ATOM   2970  C   VAL B 272     133.294  92.406 -22.023  1.00  8.65           C  
-ATOM   2971  O   VAL B 272     134.186  91.580 -21.877  1.00 11.13           O  
-ATOM   2972  CB  VAL B 272     132.508  92.245 -24.363  1.00 10.46           C  
-ATOM   2973  CG1 VAL B 272     131.167  91.722 -23.849  1.00  9.41           C  
-ATOM   2974  CG2 VAL B 272     132.310  92.976 -25.669  1.00 10.73           C  
-ATOM   2975  N   ARG B 273     132.395  92.695 -21.085  1.00  6.56           N  
-ATOM   2976  CA  ARG B 273     132.195  91.849 -19.917  1.00  7.33           C  
-ATOM   2977  C   ARG B 273     130.738  91.427 -19.882  1.00 11.79           C  
-ATOM   2978  O   ARG B 273     129.838  92.272 -19.880  1.00  9.95           O  
-ATOM   2979  CB  ARG B 273     132.538  92.607 -18.624  1.00  8.81           C  
-ATOM   2980  CG  ARG B 273     132.205  91.828 -17.331  1.00 10.86           C  
-ATOM   2981  CD  ARG B 273     132.541  92.657 -16.106  1.00 13.58           C  
-ATOM   2982  NE  ARG B 273     132.050  92.074 -14.851  1.00 19.80           N  
-ATOM   2983  CZ  ARG B 273     132.606  91.032 -14.245  1.00 28.12           C  
-ATOM   2984  NH1 ARG B 273     133.659  90.440 -14.788  1.00 27.32           N  
-ATOM   2985  NH2 ARG B 273     132.103  90.576 -13.097  1.00 26.37           N  
-ATOM   2986  N   VAL B 274     130.507  90.117 -19.840  1.00 10.42           N  
-ATOM   2987  CA  VAL B 274     129.157  89.585 -19.739  1.00  9.60           C  
-ATOM   2988  C   VAL B 274     128.986  89.174 -18.278  1.00 10.75           C  
-ATOM   2989  O   VAL B 274     129.765  88.362 -17.771  1.00 12.56           O  
-ATOM   2990  CB  VAL B 274     128.964  88.361 -20.654  1.00  9.61           C  
-ATOM   2991  CG1 VAL B 274     127.491  87.938 -20.692  1.00 10.26           C  
-ATOM   2992  CG2 VAL B 274     129.454  88.664 -22.071  1.00 10.16           C  
-ATOM   2993  N   CYS B 275     127.998  89.765 -17.608  1.00  9.38           N  
-ATOM   2994  CA  CYS B 275     127.879  89.661 -16.150  1.00 11.79           C  
-ATOM   2995  C   CYS B 275     126.431  89.838 -15.687  1.00 13.31           C  
-ATOM   2996  O   CYS B 275     125.578  90.300 -16.440  1.00 13.69           O  
-ATOM   2997  CB  CYS B 275     128.775  90.705 -15.473  1.00 14.00           C  
-ATOM   2998  SG  CYS B 275     128.466  92.412 -15.997  1.00 15.69           S  
-ATOM   2999  N   ALA B 276     126.162  89.477 -14.435  1.00 14.98           N  
-ATOM   3000  CA  ALA B 276     124.801  89.509 -13.916  1.00 18.39           C  
-ATOM   3001  C   ALA B 276     124.290  90.931 -13.702  1.00 15.00           C  
-ATOM   3002  O   ALA B 276     123.109  91.217 -13.921  1.00 16.57           O  
-ATOM   3003  CB  ALA B 276     124.713  88.716 -12.613  1.00 16.47           C  
-ATOM   3004  N   CYS B 277     125.183  91.821 -13.281  1.00 16.36           N  
-ATOM   3005  C   CYS B 277     125.710  94.195 -13.689  1.00 15.70           C  
-ATOM   3006  O   CYS B 277     126.611  94.770 -13.075  1.00 16.48           O  
-ATOM   3007  CA ACYS B 277     124.813  93.195 -12.965  0.56 15.88           C  
-ATOM   3008  CB ACYS B 277     124.929  93.427 -11.453  0.56 17.77           C  
-ATOM   3009  SG ACYS B 277     124.022  92.243 -10.424  0.56 23.36           S  
-ATOM   3010  CA BCYS B 277     124.798  93.195 -12.988  0.44 15.89           C  
-ATOM   3011  CB BCYS B 277     124.806  93.448 -11.481  0.44 17.86           C  
-ATOM   3012  SG BCYS B 277     123.859  94.905 -10.998  0.44 20.33           S  
-ATOM   3013  N   PRO B 278     125.468  94.410 -14.992  1.00 14.48           N  
-ATOM   3014  CA  PRO B 278     126.256  95.329 -15.828  1.00 14.56           C  
-ATOM   3015  C   PRO B 278     126.362  96.739 -15.245  1.00 13.20           C  
-ATOM   3016  O   PRO B 278     127.443  97.331 -15.270  1.00 13.67           O  
-ATOM   3017  CB  PRO B 278     125.453  95.398 -17.131  1.00 15.63           C  
-ATOM   3018  CG  PRO B 278     124.673  94.161 -17.183  1.00 17.38           C  
-ATOM   3019  CD  PRO B 278     124.426  93.708 -15.761  1.00 13.20           C  
-ATOM   3020  N   GLY B 279     125.248  97.272 -14.744  1.00 14.43           N  
-ATOM   3021  CA  GLY B 279     125.229  98.620 -14.188  1.00 17.29           C  
-ATOM   3022  C   GLY B 279     126.159  98.767 -12.997  1.00 17.10           C  
-ATOM   3023  O   GLY B 279     126.966  99.699 -12.917  1.00 17.29           O  
-ATOM   3024  N   ARG B 280     126.052  97.836 -12.056  1.00 16.82           N  
-ATOM   3025  CA  ARG B 280     126.935  97.842 -10.904  1.00 18.49           C  
-ATOM   3026  C   ARG B 280     128.397  97.646 -11.303  1.00 17.15           C  
-ATOM   3027  O   ARG B 280     129.281  98.327 -10.789  1.00 19.66           O  
-ATOM   3028  CB  ARG B 280     126.506  96.774  -9.892  1.00 18.70           C  
-ATOM   3029  CG  ARG B 280     127.309  96.786  -8.604  1.00 27.74           C  
-ATOM   3030  CD  ARG B 280     127.093  95.494  -7.839  1.00 31.94           C  
-ATOM   3031  NE  ARG B 280     127.557  94.353  -8.624  1.00 44.01           N  
-ATOM   3032  CZ  ARG B 280     127.103  93.112  -8.487  1.00 42.82           C  
-ATOM   3033  NH1 ARG B 280     126.156  92.844  -7.593  1.00 41.32           N  
-ATOM   3034  NH2 ARG B 280     127.592  92.140  -9.251  1.00 38.23           N  
-ATOM   3035  N   ASP B 281     128.660  96.722 -12.224  1.00 13.90           N  
-ATOM   3036  CA  ASP B 281     130.041  96.458 -12.605  1.00 15.18           C  
-ATOM   3037  C   ASP B 281     130.660  97.628 -13.363  1.00 15.96           C  
-ATOM   3038  O   ASP B 281     131.845  97.923 -13.193  1.00 16.18           O  
-ATOM   3039  CB  ASP B 281     130.161  95.142 -13.390  1.00 14.99           C  
-ATOM   3040  CG  ASP B 281     129.981  93.915 -12.505  1.00 24.69           C  
-ATOM   3041  OD1 ASP B 281     129.902  94.082 -11.267  1.00 23.31           O  
-ATOM   3042  OD2 ASP B 281     129.925  92.784 -13.039  1.00 19.51           O  
-ATOM   3043  N   ARG B 282     129.873  98.302 -14.199  1.00 13.36           N  
-ATOM   3044  CA  ARG B 282     130.397  99.492 -14.864  1.00 14.13           C  
-ATOM   3045  C   ARG B 282     130.792 100.570 -13.844  1.00 15.15           C  
-ATOM   3046  O   ARG B 282     131.884 101.131 -13.916  1.00 17.02           O  
-ATOM   3047  CB  ARG B 282     129.405 100.060 -15.880  1.00 11.62           C  
-ATOM   3048  CG  ARG B 282     129.881 101.379 -16.480  1.00 13.84           C  
-ATOM   3049  CD  ARG B 282     128.948 101.895 -17.567  1.00 10.76           C  
-ATOM   3050  NE  ARG B 282     129.339 103.256 -17.939  1.00 11.21           N  
-ATOM   3051  CZ  ARG B 282     128.555 104.120 -18.572  1.00 10.37           C  
-ATOM   3052  NH1 ARG B 282     127.326 103.775 -18.940  1.00 11.47           N  
-ATOM   3053  NH2 ARG B 282     129.005 105.343 -18.829  1.00 15.36           N  
-ATOM   3054  N   ARG B 283     129.904 100.854 -12.898  1.00 18.18           N  
-ATOM   3055  CA  ARG B 283     130.200 101.862 -11.873  1.00 20.25           C  
-ATOM   3056  C   ARG B 283     131.469 101.521 -11.102  1.00 19.16           C  
-ATOM   3057  O   ARG B 283     132.313 102.386 -10.862  1.00 21.23           O  
-ATOM   3058  CB  ARG B 283     129.031 102.017 -10.900  1.00 22.68           C  
-ATOM   3059  CG  ARG B 283     127.771 102.588 -11.510  1.00 25.54           C  
-ATOM   3060  CD  ARG B 283     126.806 103.079 -10.429  1.00 34.18           C  
-ATOM   3061  NE  ARG B 283     126.726 102.164  -9.291  1.00 43.93           N  
-ATOM   3062  CZ  ARG B 283     125.811 101.208  -9.156  1.00 42.05           C  
-ATOM   3063  NH1 ARG B 283     124.883 101.035 -10.090  1.00 35.73           N  
-ATOM   3064  NH2 ARG B 283     125.820 100.425  -8.083  1.00 38.83           N  
-ATOM   3065  N   THR B 284     131.594 100.259 -10.708  1.00 19.97           N  
-ATOM   3066  CA  THR B 284     132.782  99.786 -10.012  1.00 21.40           C  
-ATOM   3067  C   THR B 284     134.065  99.978 -10.813  1.00 23.85           C  
-ATOM   3068  O   THR B 284     135.035 100.547 -10.314  1.00 24.37           O  
-ATOM   3069  CB  THR B 284     132.645  98.300  -9.630  1.00 27.16           C  
-ATOM   3070  OG1 THR B 284     131.563  98.150  -8.706  1.00 24.20           O  
-ATOM   3071  CG2 THR B 284     133.928  97.789  -8.996  1.00 27.42           C  
-ATOM   3072  N   GLU B 285     134.078  99.504 -12.057  1.00 20.49           N  
-ATOM   3073  CA  GLU B 285     135.291  99.591 -12.866  1.00 18.38           C  
-ATOM   3074  C   GLU B 285     135.645 101.029 -13.224  1.00 23.40           C  
-ATOM   3075  O   GLU B 285     136.823 101.353 -13.377  1.00 25.72           O  
-ATOM   3076  CB  GLU B 285     135.193  98.729 -14.138  1.00 21.03           C  
-ATOM   3077  CG  GLU B 285     135.082  97.247 -13.838  1.00 21.63           C  
-ATOM   3078  CD  GLU B 285     135.382  96.351 -15.034  1.00 24.76           C  
-ATOM   3079  OE1 GLU B 285     135.980  96.823 -16.027  1.00 17.55           O  
-ATOM   3080  OE2 GLU B 285     135.032  95.156 -14.962  1.00 21.11           O  
-ATOM   3081  N   GLU B 286     134.637 101.884 -13.368  1.00 20.38           N  
-ATOM   3082  CA  GLU B 286     134.898 103.293 -13.662  1.00 17.38           C  
-ATOM   3083  C   GLU B 286     135.421 103.987 -12.406  1.00 28.02           C  
-ATOM   3084  O   GLU B 286     136.298 104.846 -12.483  1.00 27.20           O  
-ATOM   3085  CB  GLU B 286     133.648 104.010 -14.198  1.00 19.92           C  
-ATOM   3086  CG  GLU B 286     133.286 103.634 -15.640  1.00 18.05           C  
-ATOM   3087  CD  GLU B 286     132.232 104.545 -16.257  1.00 20.45           C  
-ATOM   3088  OE1 GLU B 286     131.754 105.479 -15.566  1.00 21.24           O  
-ATOM   3089  OE2 GLU B 286     131.883 104.331 -17.445  1.00 15.10           O  
-ATOM   3090  N   GLU B 287     134.883 103.605 -11.252  1.00 28.45           N  
-ATOM   3091  CA  GLU B 287     135.356 104.158  -9.984  1.00 36.54           C  
-ATOM   3092  C   GLU B 287     136.814 103.770  -9.742  1.00 33.67           C  
-ATOM   3093  O   GLU B 287     137.613 104.583  -9.277  1.00 39.49           O  
-ATOM   3094  CB  GLU B 287     134.470 103.704  -8.820  1.00 33.46           C  
-ATOM   3095  CG  GLU B 287     134.916 104.221  -7.456  1.00 43.00           C  
-ATOM   3096  CD  GLU B 287     135.014 105.739  -7.398  1.00 54.60           C  
-ATOM   3097  OE1 GLU B 287     134.441 106.417  -8.280  1.00 55.10           O  
-ATOM   3098  OE2 GLU B 287     135.665 106.254  -6.462  1.00 61.72           O  
-ATOM   3099  N   ASN B 288     137.159 102.530 -10.074  1.00 31.69           N  
-ATOM   3100  CA  ASN B 288     138.540 102.077  -9.977  1.00 32.79           C  
-ATOM   3101  C   ASN B 288     139.461 102.893 -10.876  1.00 39.60           C  
-ATOM   3102  O   ASN B 288     140.558 103.271 -10.470  1.00 40.86           O  
-ATOM   3103  CB  ASN B 288     138.658 100.587 -10.315  1.00 30.49           C  
-ATOM   3104  CG  ASN B 288     138.062  99.692  -9.241  1.00 40.70           C  
-ATOM   3105  OD1 ASN B 288     137.853  98.497  -9.461  1.00 44.11           O  
-ATOM   3106  ND2 ASN B 288     137.786 100.264  -8.073  1.00 36.39           N  
-ATOM   3107  N   LEU B 289     139.009 103.162 -12.098  1.00 31.23           N  
-ATOM   3108  CA  LEU B 289     139.805 103.926 -13.049  1.00 36.56           C  
-ATOM   3109  C   LEU B 289     140.110 105.324 -12.508  1.00 41.22           C  
-ATOM   3110  O   LEU B 289     141.228 105.819 -12.648  1.00 42.54           O  
-ATOM   3111  CB  LEU B 289     139.093 104.009 -14.403  1.00 32.97           C  
-ATOM   3112  CG  LEU B 289     139.789 104.769 -15.535  1.00 33.48           C  
-ATOM   3113  CD1 LEU B 289     141.172 104.200 -15.817  1.00 29.81           C  
-ATOM   3114  CD2 LEU B 289     138.931 104.740 -16.786  1.00 25.33           C  
-ATOM   3115  N   ARG B 290     139.112 105.955 -11.894  1.00 37.91           N  
-ATOM   3116  CA  ARG B 290     139.314 107.247 -11.245  1.00 46.08           C  
-ATOM   3117  C   ARG B 290     140.326 107.131 -10.108  1.00 49.85           C  
-ATOM   3118  O   ARG B 290     141.133 108.035  -9.889  1.00 53.24           O  
-ATOM   3119  CB  ARG B 290     137.994 107.807 -10.707  1.00 49.87           C  
-ATOM   3120  CG  ARG B 290     137.059 108.357 -11.773  1.00 49.79           C  
-ATOM   3121  CD  ARG B 290     136.031 109.303 -11.163  1.00 58.11           C  
-ATOM   3122  NE  ARG B 290     135.412 110.164 -12.170  1.00 57.70           N  
-ATOM   3123  CZ  ARG B 290     134.668 111.231 -11.889  1.00 61.38           C  
-ATOM   3124  NH1 ARG B 290     134.448 111.575 -10.625  1.00 62.58           N  
-ATOM   3125  NH2 ARG B 290     134.145 111.958 -12.872  1.00 51.72           N  
-TER    3126      ARG B 290                                                      
-HETATM 3127  C1  P84 A 400      91.150  95.734 -44.953  0.73 11.29           C  
-HETATM 3128  C2  P84 A 400      91.511  95.543 -43.614  0.73 13.95           C  
-HETATM 3129  C3  P84 A 400      91.883  94.283 -43.152  0.73  6.56           C  
-HETATM 3130  C4  P84 A 400      90.715  97.095 -45.476  0.73 12.52           C  
-HETATM 3131  N5  P84 A 400      91.397  98.231 -44.827  0.73 10.38           N  
-HETATM 3132  C6  P84 A 400      91.896  93.176 -44.013  0.73 12.11           C  
-HETATM 3133  C8  P84 A 400      91.167  94.618 -45.816  0.73 11.98           C  
-HETATM 3134  C9  P84 A 400      92.791  98.432 -45.271  0.73 11.86           C  
-HETATM 3135  C10 P84 A 400      91.536  93.348 -45.351  0.73 10.89           C  
-HETATM 3136  I15 P84 A 400      92.385  94.074 -41.117  0.73 11.44           I  
-HETATM 3137  O16 P84 A 400      91.524  96.627 -42.780  0.73 11.95           O  
-HETATM 3138  I17 P84 A 400      91.536  91.734 -46.682  0.73 19.11           I  
-HETATM 3139  C14 P84 A 400      90.614  99.473 -44.925  0.73 23.04           C  
-HETATM 3140 ZN    ZN A1300      97.133  70.383 -20.490  1.00 11.94          ZN  
-HETATM 3141  C1  P84 B 400     124.461 105.107 -45.040  0.70 16.25           C  
-HETATM 3142  C2  P84 B 400     124.810 104.933 -43.693  0.70 19.35           C  
-HETATM 3143  C3  P84 B 400     125.116 103.661 -43.202  0.70 10.20           C  
-HETATM 3144  C4  P84 B 400     124.099 106.472 -45.600  0.70 16.19           C  
-HETATM 3145  N5  P84 B 400     124.805 107.588 -44.945  0.70 14.23           N  
-HETATM 3146  C6  P84 B 400     125.081 102.538 -44.036  0.70 14.59           C  
-HETATM 3147  C8  P84 B 400     124.420 103.970 -45.871  0.70 14.27           C  
-HETATM 3148  C9  P84 B 400     126.221 107.735 -45.354  0.70 14.63           C  
-HETATM 3149  C10 P84 B 400     124.734 102.700 -45.378  0.70 12.86           C  
-HETATM 3150  I15 P84 B 400     125.644 103.438 -41.182  0.70 13.14           I  
-HETATM 3151  O16 P84 B 400     124.842 106.032 -42.872  0.70 14.88           O  
-HETATM 3152  I17 P84 B 400     124.649 101.060 -46.674  0.70 23.30           I  
-HETATM 3153  C14 P84 B 400     124.058 108.847 -45.092  0.70 21.52           C  
-HETATM 3154 ZN    ZN B1300     129.092  79.505 -20.617  1.00 10.80          ZN  
-HETATM 3155  O   HOH A2001     112.659  72.056 -33.851  1.00 29.83           O  
-HETATM 3156  O   HOH A2002     113.699  71.325 -37.826  1.00 41.06           O  
-HETATM 3157  O   HOH A2003     111.128  75.167 -36.543  1.00 32.80           O  
-HETATM 3158  O   HOH A2004     115.953  78.408 -37.701  1.00 37.25           O  
-HETATM 3159  O   HOH A2005     115.528  82.598 -35.178  1.00 42.98           O  
-HETATM 3160  O   HOH A2006     112.336  82.997 -32.337  1.00 24.34           O  
-HETATM 3161  O   HOH A2007     107.801  82.972 -37.765  1.00 21.37           O  
-HETATM 3162  O   HOH A2008     110.836  81.795 -39.685  1.00 25.31           O  
-HETATM 3163  O   HOH A2009     114.728  87.036 -37.408  1.00 30.62           O  
-HETATM 3164  O   HOH A2010     113.682  86.292 -34.364  1.00 25.61           O  
-HETATM 3165  O   HOH A2011     107.060  89.915 -33.388  1.00 16.48           O  
-HETATM 3166  O   HOH A2012     109.649  90.202 -31.072  1.00 37.69           O  
-HETATM 3167  O   HOH A2013     112.159  84.509 -27.078  1.00 27.65           O  
-HETATM 3168  O   HOH A2014     110.595  86.723 -26.887  1.00 26.00           O  
-HETATM 3169  O   HOH A2015     111.419  94.027 -39.292  1.00 35.98           O  
-HETATM 3170  O   HOH A2016     111.035  92.363 -33.012  1.00 21.46           O  
-HETATM 3171  O   HOH A2017     111.193  95.112 -35.923  1.00 29.29           O  
-HETATM 3172  O   HOH A2018     107.756  92.123 -29.888  1.00 35.24           O  
-HETATM 3173  O   HOH A2019     105.245  94.003 -32.008  1.00 20.09           O  
-HETATM 3174  O   HOH A2020     107.368  90.795 -47.432  1.00 34.56           O  
-HETATM 3175  O   HOH A2021     108.245  96.687 -39.198  1.00 18.92           O  
-HETATM 3176  O   HOH A2022     102.360  93.686 -44.674  1.00 10.47           O  
-HETATM 3177  O   HOH A2023     101.777 101.235 -40.056  1.00 22.73           O  
-HETATM 3178  O   HOH A2024     101.710 101.389 -37.577  1.00 23.77           O  
-HETATM 3179  O   HOH A2025     104.926 100.179 -41.743  1.00 24.22           O  
-HETATM 3180  O   HOH A2026     104.134  96.287 -35.500  1.00 15.83           O  
-HETATM 3181  O   HOH A2027     106.206  97.936 -35.537  1.00 23.97           O  
-HETATM 3182  O   HOH A2028     106.423 100.407 -36.896  1.00 37.73           O  
-HETATM 3183  O   HOH A2029     108.306  96.635 -42.553  1.00 20.28           O  
-HETATM 3184  O   HOH A2030     104.310  99.584 -44.177  1.00 29.27           O  
-HETATM 3185  O   HOH A2031     105.048  92.738 -47.123  1.00 17.33           O  
-HETATM 3186  O   HOH A2032     100.548 100.035 -46.601  1.00 21.53           O  
-HETATM 3187  O   HOH A2033     103.965 100.087 -48.526  1.00 34.96           O  
-HETATM 3188  O   HOH A2034     104.691  92.720 -50.077  1.00 31.06           O  
-HETATM 3189  O   HOH A2035     103.535  95.569 -52.746  1.00 45.60           O  
-HETATM 3190  O   HOH A2036     102.549  91.758 -51.791  1.00 25.60           O  
-HETATM 3191  O   HOH A2037      98.994  94.759 -53.502  1.00 29.94           O  
-HETATM 3192  O   HOH A2038     103.784  94.004 -36.894  1.00 10.92           O  
-HETATM 3193  O   HOH A2039      96.702  99.195 -34.834  1.00 14.20           O  
-HETATM 3194  O   HOH A2040      96.012 102.520 -40.059  1.00 24.46           O  
-HETATM 3195  O   HOH A2041      92.353  97.659 -29.625  1.00 19.12           O  
-HETATM 3196  O   HOH A2042      94.353  98.746 -28.294  1.00 23.27           O  
-HETATM 3197  O   HOH A2043      92.060  91.361 -26.789  1.00 15.61           O  
-HETATM 3198  O   HOH A2044      94.997  96.019 -22.390  1.00 13.22           O  
-HETATM 3199  O   HOH A2045      92.913  93.672 -22.126  1.00 22.57           O  
-HETATM 3200  O   HOH A2046      88.157  97.382 -24.947  1.00 28.29           O  
-HETATM 3201  O   HOH A2047      88.074  98.263 -18.660  1.00 37.45           O  
-HETATM 3202  O   HOH A2048      86.077  93.035 -19.029  1.00 25.81           O  
-HETATM 3203  O   HOH A2049      88.094  93.523 -15.749  1.00 16.35           O  
-HETATM 3204  O   HOH A2050      90.952  90.743 -24.079  1.00 15.76           O  
-HETATM 3205  O   HOH A2051      87.847  89.548 -21.374  1.00 24.39           O  
-HETATM 3206  O   HOH A2052      88.062  89.828 -24.124  1.00 30.16           O  
-HETATM 3207  O   HOH A2053      86.738  93.092 -23.542  1.00 34.82           O  
-HETATM 3208  O   HOH A2054      92.846  96.996 -19.573  1.00 13.26           O  
-HETATM 3209  O   HOH A2055      90.270  96.563 -14.102  1.00 30.31           O  
-HETATM 3210  O   HOH A2056      91.503  95.296 -10.864  1.00 33.89           O  
-HETATM 3211  O   HOH A2057      95.159  96.511 -13.075  1.00 32.47           O  
-HETATM 3212  O   HOH A2058      93.401  97.365 -16.462  1.00 33.50           O  
-HETATM 3213  O   HOH A2059      85.368  90.559 -10.508  1.00 36.33           O  
-HETATM 3214  O   HOH A2060      88.701  92.019  -8.673  1.00 33.94           O  
-HETATM 3215  O   HOH A2061      90.861  86.475 -13.886  1.00 18.19           O  
-HETATM 3216  O   HOH A2062      84.264  85.148 -15.126  1.00 42.66           O  
-HETATM 3217  O   HOH A2063      86.330  83.797 -14.386  1.00 39.32           O  
-HETATM 3218  O   HOH A2064      86.303  88.246 -19.733  1.00 22.21           O  
-HETATM 3219  O   HOH A2065      86.799  85.704 -23.153  1.00 16.12           O  
-HETATM 3220  O   HOH A2066     103.024  95.582 -25.894  1.00 21.54           O  
-HETATM 3221  O   HOH A2067     100.220  97.254 -19.242  1.00 13.50           O  
-HETATM 3222  O   HOH A2068     107.419  97.818 -20.285  1.00 37.92           O  
-HETATM 3223  O   HOH A2069     106.720  89.658 -24.182  1.00 31.99           O  
-HETATM 3224  O   HOH A2070     106.588  89.493 -20.464  1.00 35.40           O  
-HETATM 3225  O   HOH A2071     107.156  89.401 -28.813  1.00 28.38           O  
-HETATM 3226  O   HOH A2072     107.584  91.072 -26.506  1.00 25.01           O  
-HETATM 3227  O   HOH A2073     116.990  85.213 -36.441  1.00 39.28           O  
-HETATM 3228  O   HOH A2074     115.269  83.332 -32.262  1.00 41.67           O  
-HETATM 3229  O   HOH A2075     108.631  79.698 -39.747  1.00 39.34           O  
-HETATM 3230  O   HOH A2076     113.702  88.942 -33.110  1.00 33.88           O  
-HETATM 3231  O   HOH A2077     103.730  82.553 -17.266  1.00 32.67           O  
-HETATM 3232  O   HOH A2078     103.870  82.794 -19.945  1.00 23.88           O  
-HETATM 3233  O   HOH A2079     110.795  96.490 -40.813  1.00 35.94           O  
-HETATM 3234  O   HOH A2080     114.480  91.522 -33.378  1.00 42.07           O  
-HETATM 3235  O   HOH A2081     108.457  97.401 -36.583  1.00 33.08           O  
-HETATM 3236  O   HOH A2082     106.887  91.188 -50.095  1.00 41.68           O  
-HETATM 3237  O   HOH A2083     100.555 103.658 -37.336  1.00 33.47           O  
-HETATM 3238  O   HOH A2084     106.707  98.221 -32.765  1.00 30.68           O  
-HETATM 3239  O   HOH A2085      95.783  93.513 -54.525  1.00 23.90           O  
-HETATM 3240  O   HOH A2086      99.498  93.392 -55.742  1.00 35.41           O  
-HETATM 3241  O   HOH A2087      91.898  80.338 -24.271  1.00  9.88           O  
-HETATM 3242  O   HOH A2088      85.316  81.739 -15.963  1.00 43.10           O  
-HETATM 3243  O   HOH A2089      89.609  79.699 -14.341  1.00 28.88           O  
-HETATM 3244  O   HOH A2090      90.585  78.326 -16.557  1.00 14.76           O  
-HETATM 3245  O   HOH A2091      88.372  77.634 -18.345  1.00 23.93           O  
-HETATM 3246  O   HOH A2092      86.356  95.655 -24.142  1.00 42.94           O  
-HETATM 3247  O   HOH A2093      87.340  99.547 -23.382  1.00 40.52           O  
-HETATM 3248  O   HOH A2094      89.468  99.423 -26.577  1.00 42.17           O  
-HETATM 3249  O   HOH A2095      90.609  98.993 -18.640  1.00 35.48           O  
-HETATM 3250  O   HOH A2096      85.111  79.609 -26.199  1.00 21.29           O  
-HETATM 3251  O   HOH A2097      85.933  77.158 -26.196  1.00 36.42           O  
-HETATM 3252  O   HOH A2098      85.899  91.759 -21.276  1.00 37.38           O  
-HETATM 3253  O   HOH A2099      85.866  92.158 -15.741  1.00 35.33           O  
-HETATM 3254  O   HOH A2100      87.721  96.226 -14.987  1.00 29.31           O  
-HETATM 3255  O   HOH A2101      82.955  80.572 -21.541  1.00 36.43           O  
-HETATM 3256  O   HOH A2102      84.748  78.793 -16.671  1.00 46.90           O  
-HETATM 3257  O   HOH A2103      90.522  93.893  -8.795  1.00 42.08           O  
-HETATM 3258  O   HOH A2104      95.648  98.236 -15.695  1.00 39.48           O  
-HETATM 3259  O   HOH A2105      82.944  84.025 -26.740  1.00 14.89           O  
-HETATM 3260  O   HOH A2106     106.182  99.773 -21.091  1.00 35.22           O  
-HETATM 3261  O   HOH A2107      87.839  93.554 -31.577  1.00 23.67           O  
-HETATM 3262  O   HOH A2108     108.284  93.385 -24.627  1.00 44.54           O  
-HETATM 3263  O   HOH A2109      89.920  77.239 -12.856  1.00 42.81           O  
-HETATM 3264  O   HOH A2110      92.796  97.680 -40.371  1.00 16.21           O  
-HETATM 3265  O   HOH A2111      93.899 100.978 -40.823  1.00 27.35           O  
-HETATM 3266  O   HOH A2112      93.231 101.653 -47.246  1.00 40.34           O  
-HETATM 3267  O   HOH A2113      99.613 103.750 -39.807  1.00 28.64           O  
-HETATM 3268  O   HOH A2114     102.113 100.979 -44.365  1.00 26.07           O  
-HETATM 3269  O   HOH A2115      85.918  91.760 -29.924  1.00 26.76           O  
-HETATM 3270  O   HOH A2116      99.423  98.372 -50.683  1.00 28.81           O  
-HETATM 3271  O   HOH A2117      96.616  97.396 -51.305  1.00 24.06           O  
-HETATM 3272  O   HOH A2118      93.565  99.814 -49.245  1.00 25.82           O  
-HETATM 3273  O   HOH A2119      94.788  94.378 -52.557  1.00 30.17           O  
-HETATM 3274  O   HOH A2120     102.037  97.646 -51.569  1.00 42.18           O  
-HETATM 3275  O   HOH A2121      93.136  96.470 -53.219  1.00 41.80           O  
-HETATM 3276  O   HOH A2122      91.367  92.800 -55.526  1.00 24.18           O  
-HETATM 3277  O   HOH A2123      90.743  91.230 -50.743  1.00 41.72           O  
-HETATM 3278  O   HOH A2124      88.701  95.519 -48.748  1.00 36.47           O  
-HETATM 3279  O   HOH A2125      88.876  91.491 -55.650  1.00 42.59           O  
-HETATM 3280  O   HOH A2126      92.274  93.423 -52.659  1.00 34.53           O  
-HETATM 3281  O   HOH A2127      92.919  86.866 -57.122  1.00 11.42           O  
-HETATM 3282  O   HOH A2128      92.537  87.842 -48.379  1.00 29.10           O  
-HETATM 3283  O   HOH A2129      91.028  83.052 -49.807  1.00 34.91           O  
-HETATM 3284  O   HOH A2130      92.756  81.473 -48.634  1.00 14.73           O  
-HETATM 3285  O   HOH A2131      95.316  86.880 -55.629  1.00  8.84           O  
-HETATM 3286  O   HOH A2132      95.950  76.886 -49.303  1.00 14.23           O  
-HETATM 3287  O   HOH A2133      91.972  79.037 -47.607  1.00 20.91           O  
-HETATM 3288  O   HOH A2134     101.166  74.914 -45.498  1.00 22.09           O  
-HETATM 3289  O   HOH A2135      90.735  86.430 -50.269  1.00 36.14           O  
-HETATM 3290  O   HOH A2136      92.434  84.546 -48.424  1.00 26.01           O  
-HETATM 3291  O   HOH A2137      95.197  81.510 -50.059  1.00 11.72           O  
-HETATM 3292  O   HOH A2138     105.512  80.109 -39.876  1.00 23.36           O  
-HETATM 3293  O   HOH A2139      90.866  84.137 -53.121  1.00 33.44           O  
-HETATM 3294  O   HOH A2140      97.037  79.364 -49.421  1.00 13.72           O  
-HETATM 3295  O   HOH A2141      99.316  81.027 -46.846  1.00 12.82           O  
-HETATM 3296  O   HOH A2142      93.073  78.865 -44.504  1.00 15.84           O  
-HETATM 3297  O   HOH A2143      97.174  75.108 -47.333  1.00 22.72           O  
-HETATM 3298  O   HOH A2144     100.428  78.474 -47.356  1.00 22.32           O  
-HETATM 3299  O   HOH A2145      99.050  75.595 -43.890  1.00 13.75           O  
-HETATM 3300  O   HOH A2146     110.804  83.657 -20.369  1.00 35.93           O  
-HETATM 3301  O   HOH A2147     113.845  84.153 -22.136  1.00 38.47           O  
-HETATM 3302  O   HOH A2148     119.077  82.968 -20.794  1.00 41.98           O  
-HETATM 3303  O   HOH A2149     117.159  72.841 -20.280  1.00 45.30           O  
-HETATM 3304  O   HOH A2150      95.302  82.049 -37.510  1.00  7.56           O  
-HETATM 3305  O   HOH A2151     102.917  82.254 -37.495  1.00 10.09           O  
-HETATM 3306  O   HOH A2152     104.286  77.614 -41.096  1.00 24.79           O  
-HETATM 3307  O   HOH A2153     102.596  77.392 -46.042  1.00 24.78           O  
-HETATM 3308  O   HOH A2154     109.353  66.989 -32.055  1.00 35.67           O  
-HETATM 3309  O   HOH A2155     103.234  66.047 -36.554  1.00 35.74           O  
-HETATM 3310  O   HOH A2156     105.409  81.171 -37.258  1.00 16.05           O  
-HETATM 3311  O   HOH A2157     101.690  75.971 -32.302  1.00  7.98           O  
-HETATM 3312  O   HOH A2158     105.983  74.894 -31.603  1.00 11.14           O  
-HETATM 3313  O   HOH A2159     109.341  76.087 -29.268  1.00 12.40           O  
-HETATM 3314  O   HOH A2160     105.384  71.052 -25.618  1.00 15.24           O  
-HETATM 3315  O   HOH A2161      90.066  64.445 -35.149  1.00 47.51           O  
-HETATM 3316  O   HOH A2162      84.634  76.034 -36.107  1.00 34.33           O  
-HETATM 3317  O   HOH A2163     110.063  78.946 -22.425  1.00 15.82           O  
-HETATM 3318  O   HOH A2164     108.537  85.097 -19.242  1.00 32.98           O  
-HETATM 3319  O   HOH A2165     107.939  87.753 -23.565  1.00 37.53           O  
-HETATM 3320  O   HOH A2166     110.155  89.771 -22.739  1.00 40.04           O  
-HETATM 3321  O   HOH A2167     115.913  80.809 -18.471  1.00 39.50           O  
-HETATM 3322  O   HOH A2168     115.962  82.989 -23.106  1.00 33.95           O  
-HETATM 3323  O   HOH A2169     116.759  76.559 -29.100  1.00 30.99           O  
-HETATM 3324  O   HOH A2170     117.146  81.978 -30.003  1.00 44.72           O  
-HETATM 3325  O   HOH A2171     118.987  84.074 -26.844  1.00 41.74           O  
-HETATM 3326  O   HOH A2172     116.854  81.402 -21.219  1.00 36.86           O  
-HETATM 3327  O   HOH A2173     120.468  81.262 -23.407  1.00 42.76           O  
-HETATM 3328  O   HOH A2174     115.798  73.813 -27.505  1.00 25.46           O  
-HETATM 3329  O   HOH A2175     115.180  71.683 -25.990  1.00 34.36           O  
-HETATM 3330  O   HOH A2176     117.590  72.421 -23.181  1.00 38.72           O  
-HETATM 3331  O   HOH A2177     116.400  75.511 -18.242  1.00 40.22           O  
-HETATM 3332  O   HOH A2178     113.338  71.629 -24.013  1.00 26.58           O  
-HETATM 3333  O   HOH A2179      91.507  75.521 -50.200  1.00 25.35           O  
-HETATM 3334  O   HOH A2180     102.264  65.131 -40.632  1.00 38.67           O  
-HETATM 3335  O   HOH A2181     117.628  70.697 -30.064  1.00 43.23           O  
-HETATM 3336  O   HOH A2182     109.410  77.023 -39.205  1.00 37.40           O  
-HETATM 3337  O   HOH A2183     105.530  68.770 -24.451  1.00 28.09           O  
-HETATM 3338  O   HOH A2184     109.727  68.508 -29.926  1.00 24.22           O  
-HETATM 3339  O   HOH A2185     106.907  68.526 -28.129  1.00 23.33           O  
-HETATM 3340  O   HOH A2186     103.553  73.801 -32.099  1.00  8.56           O  
-HETATM 3341  O   HOH A2187     100.303  72.963 -30.529  1.00  7.91           O  
-HETATM 3342  O   HOH A2188     100.776  71.975 -22.894  1.00 13.97           O  
-HETATM 3343  O   HOH A2189     107.072  66.660 -30.946  1.00 31.44           O  
-HETATM 3344  O   HOH A2190     101.093  66.043 -32.819  1.00 18.04           O  
-HETATM 3345  O   HOH A2191     100.089  66.862 -27.986  1.00 11.76           O  
-HETATM 3346  O   HOH A2192     103.691  67.200 -34.186  1.00 21.11           O  
-HETATM 3347  O   HOH A2193      87.016  97.337 -45.420  1.00 38.66           O  
-HETATM 3348  O   HOH A2194      77.653  92.193 -43.877  1.00 35.90           O  
-HETATM 3349  O   HOH A2195      75.591  88.148 -40.385  1.00 40.34           O  
-HETATM 3350  O   HOH A2196     102.211  66.006 -24.577  1.00 19.35           O  
-HETATM 3351  O   HOH A2197      91.439  66.239 -26.850  1.00 33.87           O  
-HETATM 3352  O   HOH A2198      88.270 100.272 -33.559  1.00 39.64           O  
-HETATM 3353  O   HOH A2199      97.584  68.556 -16.887  1.00 22.84           O  
-HETATM 3354  O   HOH A2200      99.478  66.448 -17.658  1.00 15.99           O  
-HETATM 3355  O   HOH A2201      83.058  87.542 -38.504  1.00 41.76           O  
-HETATM 3356  O   HOH A2202      95.824  61.283 -20.467  1.00  9.03           O  
-HETATM 3357  O   HOH A2203      99.055  61.163 -23.958  1.00 11.78           O  
-HETATM 3358  O   HOH A2204      93.489  61.901 -19.344  1.00 15.87           O  
-HETATM 3359  O   HOH A2205      90.136  68.163 -18.194  1.00 29.17           O  
-HETATM 3360  O   HOH A2206      90.887  70.857 -17.731  1.00 34.14           O  
-HETATM 3361  O   HOH A2207      88.215  75.308 -13.643  1.00 43.40           O  
-HETATM 3362  O   HOH A2208      95.593  72.182 -13.835  1.00 36.88           O  
-HETATM 3363  O   HOH A2209      95.390  75.090 -12.771  1.00 42.47           O  
-HETATM 3364  O   HOH A2210      94.173  70.722 -15.860  1.00 24.97           O  
-HETATM 3365  O   HOH A2211      91.364  63.759 -27.534  1.00 22.16           O  
-HETATM 3366  O   HOH A2212     100.900  60.887 -27.799  1.00 14.13           O  
-HETATM 3367  O   HOH A2213      90.816  59.694 -25.175  1.00 27.00           O  
-HETATM 3368  O   HOH A2214      91.198  61.111 -21.022  1.00 23.93           O  
-HETATM 3369  O   HOH A2215      88.482  61.337 -23.306  1.00 37.81           O  
-HETATM 3370  O   HOH A2216     111.023  71.844 -18.772  1.00 37.51           O  
-HETATM 3371  O   HOH A2217      85.401  66.775 -24.412  1.00 43.28           O  
-HETATM 3372  O   HOH A2218      86.515  64.978 -28.980  1.00 40.10           O  
-HETATM 3373  O   HOH A2219      90.392  60.814 -27.632  1.00 37.26           O  
-HETATM 3374  O   HOH A2220      88.336  58.622 -24.813  1.00 37.98           O  
-HETATM 3375  O   HOH A2221      90.532  67.349 -29.030  1.00 30.03           O  
-HETATM 3376  O   HOH A2222      88.677  71.417 -22.618  1.00 36.26           O  
-HETATM 3377  O   HOH A2223     108.178  82.241 -43.256  1.00 43.58           O  
-HETATM 3378  O   HOH A2224      83.745  67.782 -28.106  1.00 43.79           O  
-HETATM 3379  O   HOH A2225      89.533  64.975 -29.336  1.00 36.71           O  
-HETATM 3380  O   HOH A2226      89.382  66.957 -34.076  1.00 36.53           O  
-HETATM 3381  O   HOH A2227      89.458  69.725 -31.661  1.00 30.03           O  
-HETATM 3382  O   HOH A2228      84.244  73.422 -35.649  1.00 44.40           O  
-HETATM 3383  O   HOH A2229      88.729  74.996 -35.224  1.00 18.53           O  
-HETATM 3384  O   HOH A2230      87.135  75.824 -32.107  1.00 27.58           O  
-HETATM 3385  O   HOH A2231     102.066  84.998 -10.176  1.00 47.97           O  
-HETATM 3386  O   HOH A2232      91.456  66.648 -36.905  1.00 32.86           O  
-HETATM 3387  O   HOH A2233      92.018  69.264 -39.528  1.00 38.24           O  
-HETATM 3388  O   HOH A2234      93.288  71.072 -30.076  1.00  9.75           O  
-HETATM 3389  O   HOH A2235      95.146  64.033 -34.765  1.00 21.33           O  
-HETATM 3390  O   HOH A2236      97.350  65.370 -35.983  1.00 20.49           O  
-HETATM 3391  O   HOH A2237      98.954  67.083 -34.196  1.00 18.87           O  
-HETATM 3392  O   HOH A2238     100.437  62.512 -32.108  1.00 18.39           O  
-HETATM 3393  O   HOH A2239      98.929  94.986  -7.612  1.00 43.26           O  
-HETATM 3394  O   HOH A2240     109.297  91.749 -14.660  1.00 38.27           O  
-HETATM 3395  O   HOH A2241      97.493  75.219 -33.847  1.00  8.06           O  
-HETATM 3396  O   HOH A2242      99.186  75.190 -31.643  1.00  7.91           O  
-HETATM 3397  O   HOH A2243      87.604  75.080 -29.003  1.00 32.73           O  
-HETATM 3398  O   HOH A2244      86.930  77.234 -36.395  1.00 20.76           O  
-HETATM 3399  O   HOH A2245      84.205  83.422 -33.901  1.00 26.52           O  
-HETATM 3400  O   HOH A2246      87.534  83.557 -35.250  1.00 12.21           O  
-HETATM 3401  O   HOH A2247      84.761  76.514 -33.407  1.00 29.27           O  
-HETATM 3402  O   HOH A2248      80.765  79.928 -37.594  1.00 30.15           O  
-HETATM 3403  O   HOH A2249      85.244  81.951 -42.829  1.00 35.58           O  
-HETATM 3404  O   HOH A2250      88.768  83.994 -42.337  1.00 19.27           O  
-HETATM 3405  O   HOH A2251      88.556  83.867 -37.823  1.00 23.68           O  
-HETATM 3406  O   HOH A2252      82.634  80.109 -40.600  1.00 31.08           O  
-HETATM 3407  O   HOH A2253      85.058  73.310 -42.178  1.00 37.77           O  
-HETATM 3408  O   HOH A2254      88.528  74.337 -43.016  1.00 28.17           O  
-HETATM 3409  O   HOH A2255      89.218  79.070 -47.763  1.00 38.33           O  
-HETATM 3410  O   HOH A2256      90.680  72.207 -42.993  1.00 36.65           O  
-HETATM 3411  O   HOH A2257      93.135  76.835 -48.515  1.00 19.43           O  
-HETATM 3412  O   HOH A2258      96.438  71.419 -43.315  1.00 27.33           O  
-HETATM 3413  O   HOH A2259      92.611  71.408 -41.225  1.00 19.78           O  
-HETATM 3414  O   HOH A2260      97.068  68.277 -39.506  1.00 39.25           O  
-HETATM 3415  O   HOH A2261      94.716  69.019 -39.795  1.00 37.35           O  
-HETATM 3416  O   HOH A2262     102.801  74.414 -38.545  1.00 10.87           O  
-HETATM 3417  O   HOH A2263      98.863  68.800 -41.573  1.00 19.85           O  
-HETATM 3418  O   HOH A2264     101.191  67.139 -42.525  1.00 38.04           O  
-HETATM 3419  O   HOH A2265     104.138  66.367 -39.129  1.00 36.43           O  
-HETATM 3420  O   HOH A2266      99.916  64.849 -39.263  1.00 37.10           O  
-HETATM 3421  O   HOH A2267     108.881  72.520 -43.782  1.00 42.41           O  
-HETATM 3422  O   HOH A2268     105.283  73.100 -44.405  1.00 36.90           O  
-HETATM 3423  O   HOH A2269     105.010  75.163 -40.125  1.00 18.28           O  
-HETATM 3424  O   HOH A2270     104.341  70.577 -44.181  1.00 29.36           O  
-HETATM 3425  O   HOH A2271     102.036  69.341 -45.051  1.00 43.00           O  
-HETATM 3426  O   HOH A2272     112.778  68.767 -37.281  1.00 38.32           O  
-HETATM 3427  O   HOH A2273     107.397  75.175 -38.586  1.00 21.35           O  
-HETATM 3428  O   HOH A2274     111.071  68.383 -33.361  1.00 40.65           O  
-HETATM 3429  O   HOH A2275      90.744  87.187 -41.087  1.00 17.38           O  
-HETATM 3430  O   HOH A2276      89.514  86.664 -47.951  1.00 35.60           O  
-HETATM 3431  O   HOH A2277      92.631  89.759 -41.579  1.00 24.79           O  
-HETATM 3432  O   HOH A2278      86.369  87.656 -40.401  1.00 39.54           O  
-HETATM 3433  O   HOH A2279      85.488  90.232 -40.655  1.00 27.09           O  
-HETATM 3434  O   HOH A2280      84.722  90.236 -44.278  1.00 30.43           O  
-HETATM 3435  O   HOH A2281      84.958  96.323 -44.777  1.00 36.84           O  
-HETATM 3436  O   HOH A2282      85.158  93.493 -38.367  1.00 21.45           O  
-HETATM 3437  O   HOH A2283      81.075  96.271 -38.178  1.00 23.79           O  
-HETATM 3438  O   HOH A2284      78.379  90.750 -39.153  1.00 25.77           O  
-HETATM 3439  O   HOH A2285      79.179  93.382 -41.999  1.00 33.00           O  
-HETATM 3440  O   HOH A2286      82.732  93.957 -35.934  1.00 32.88           O  
-HETATM 3441  O   HOH A2287      86.808  98.435 -35.377  1.00 22.00           O  
-HETATM 3442  O   HOH A2288      91.137 100.860 -40.487  1.00 25.58           O  
-HETATM 3443  O   HOH A2289      85.706 104.306 -36.252  1.00 40.67           O  
-HETATM 3444  O   HOH A2290      89.830 103.923 -36.455  1.00 41.15           O  
-HETATM 3445  O   HOH A2291      88.309 102.609 -34.883  1.00 40.55           O  
-HETATM 3446  O   HOH A2292      86.747  93.615 -35.487  1.00 20.34           O  
-HETATM 3447  O   HOH A2293      86.060  90.771 -37.713  1.00 18.56           O  
-HETATM 3448  O   HOH A2294      85.175  88.669 -35.960  1.00 29.52           O  
-HETATM 3449  O   HOH A2295      88.709  86.361 -39.199  1.00 31.21           O  
-HETATM 3450  O   HOH A2296      84.800  90.164 -31.636  1.00 24.63           O  
-HETATM 3451  O   HOH A2297      89.919  73.782 -15.769  1.00 38.20           O  
-HETATM 3452  O   HOH A2298      99.028  77.952 -15.685  1.00 15.15           O  
-HETATM 3453  O   HOH A2299     103.033  78.874 -21.221  1.00 12.46           O  
-HETATM 3454  O   HOH A2300      98.431  72.375 -14.265  1.00 27.70           O  
-HETATM 3455  O   HOH A2301     103.190  72.358 -13.156  1.00 29.44           O  
-HETATM 3456  O   HOH A2302      97.435  76.494 -13.202  1.00 37.13           O  
-HETATM 3457  O   HOH A2303      99.374  69.363 -14.667  1.00 20.66           O  
-HETATM 3458  O   HOH A2304     104.697  66.281 -24.314  1.00 31.93           O  
-HETATM 3459  O   HOH A2305     106.996  69.053 -20.564  1.00 26.55           O  
-HETATM 3460  O   HOH A2306     109.923  73.985 -16.018  1.00 40.84           O  
-HETATM 3461  O   HOH A2307     109.059  69.449 -13.922  1.00 33.07           O  
-HETATM 3462  O   HOH A2308     109.175  70.247 -19.453  1.00 35.95           O  
-HETATM 3463  O   HOH A2309     102.782  77.189 -11.639  1.00 38.19           O  
-HETATM 3464  O   HOH A2310     104.462  82.041 -41.882  1.00 22.52           O  
-HETATM 3465  O   HOH A2311     106.775  83.935 -39.784  1.00 29.20           O  
-HETATM 3466  O   HOH A2312     103.672  79.056 -44.346  1.00 30.96           O  
-HETATM 3467  O   HOH A2313     100.292  77.537 -49.763  1.00 24.22           O  
-HETATM 3468  O   HOH A2314      99.232  80.693 -55.080  1.00 10.86           O  
-HETATM 3469  O   HOH A2315     106.911  79.075 -48.677  1.00 45.47           O  
-HETATM 3470  O   HOH A2316     105.232  77.045 -47.332  1.00 40.35           O  
-HETATM 3471  O   HOH A2317     101.407  79.068 -54.360  1.00 16.39           O  
-HETATM 3472  O   HOH A2318     103.316  76.805 -51.170  1.00 32.03           O  
-HETATM 3473  O   HOH A2319     106.135  79.413 -45.007  1.00 41.64           O  
-HETATM 3474  O   HOH A2320     105.497  83.179 -43.882  1.00 25.34           O  
-HETATM 3475  O   HOH A2321     108.037  79.592 -51.140  1.00 40.73           O  
-HETATM 3476  O   HOH A2322     108.769  83.953 -46.718  1.00 24.81           O  
-HETATM 3477  O   HOH A2323     108.833  83.156 -40.837  1.00 37.46           O  
-HETATM 3478  O   HOH A2324     101.923  85.008 -12.932  1.00 29.38           O  
-HETATM 3479  O   HOH A2325     102.609  78.158 -14.743  1.00 26.65           O  
-HETATM 3480  O   HOH A2326      96.591  78.673 -13.062  1.00 31.28           O  
-HETATM 3481  O   HOH A2327      96.148  82.002 -12.111  1.00 16.31           O  
-HETATM 3482  O   HOH A2328      89.559  82.490 -11.413  1.00 39.30           O  
-HETATM 3483  O   HOH A2329      99.422  86.293  -9.117  1.00 25.67           O  
-HETATM 3484  O   HOH A2330      98.005  98.201 -16.939  1.00 21.32           O  
-HETATM 3485  O   HOH A2331      99.696  95.803 -10.836  1.00 27.03           O  
-HETATM 3486  O   HOH A2332      92.182  89.195  -7.218  1.00 40.71           O  
-HETATM 3487  O   HOH A2333     106.927  90.641 -14.398  1.00 31.16           O  
-HETATM 3488  O   HOH A2334     106.418  88.854 -16.342  1.00 31.14           O  
-HETATM 3489  O   HOH A2335     104.350  97.350 -15.246  1.00 30.90           O  
-HETATM 3490  O   HOH A2336      98.081  96.234 -13.039  1.00 31.55           O  
-HETATM 3491  O   HOH A2337     101.640  98.115 -10.907  1.00 44.43           O  
-HETATM 3492  O   HOH A2338     104.098  91.645  -6.980  1.00 42.16           O  
-HETATM 3493  O   HOH A2339     107.017  88.059 -12.750  1.00 42.54           O  
-HETATM 3494  O   HOH B2001     144.778  74.936 -33.020  1.00 36.00           O  
-HETATM 3495  O   HOH B2002     143.436  77.191 -32.487  1.00 28.99           O  
-HETATM 3496  O   HOH B2003     147.391  76.683 -36.227  1.00 38.53           O  
-HETATM 3497  O   HOH B2004     145.103  77.631 -36.791  1.00 36.11           O  
-HETATM 3498  O   HOH B2005     145.983  86.394 -38.679  1.00 39.86           O  
-HETATM 3499  O   HOH B2006     148.827  86.574 -36.044  1.00 35.52           O  
-HETATM 3500  O   HOH B2007     145.100  91.913 -31.987  1.00 20.20           O  
-HETATM 3501  O   HOH B2008     140.486  91.841 -37.526  1.00 20.10           O  
-HETATM 3502  O   HOH B2009     146.253  94.752 -33.455  1.00 20.64           O  
-HETATM 3503  O   HOH B2010     139.932  98.871 -32.997  1.00 14.55           O  
-HETATM 3504  O   HOH B2011     144.671  91.034 -27.629  1.00 25.33           O  
-HETATM 3505  O   HOH B2012     144.363  93.773 -26.202  1.00 33.06           O  
-HETATM 3506  O   HOH B2013     151.257  96.037 -34.108  1.00 37.53           O  
-HETATM 3507  O   HOH B2014     143.630 100.933 -32.163  1.00 20.40           O  
-HETATM 3508  O   HOH B2015     144.725 102.828 -38.704  1.00 35.65           O  
-HETATM 3509  O   HOH B2016     144.059 104.132 -35.569  1.00 32.82           O  
-HETATM 3510  O   HOH B2017     138.292 102.967 -31.778  1.00 19.03           O  
-HETATM 3511  O   HOH B2018     142.063 102.511 -30.513  1.00 40.65           O  
-HETATM 3512  O   HOH B2019     141.546 105.474 -38.891  1.00 17.96           O  
-HETATM 3513  O   HOH B2020     135.721 102.565 -44.500  1.00 11.71           O  
-HETATM 3514  O   HOH B2021     135.348 110.278 -39.963  1.00 22.86           O  
-HETATM 3515  O   HOH B2022     138.798 108.916 -41.412  1.00 32.06           O  
-HETATM 3516  O   HOH B2023     135.231 110.443 -37.330  1.00 27.29           O  
-HETATM 3517  O   HOH B2024     137.167 105.294 -35.279  1.00 17.53           O  
-HETATM 3518  O   HOH B2025     141.782 105.203 -42.286  1.00 19.82           O  
-HETATM 3519  O   HOH B2026     137.928 108.294 -43.806  1.00 29.54           O  
-HETATM 3520  O   HOH B2027     138.555 101.566 -46.868  1.00 16.19           O  
-HETATM 3521  O   HOH B2028     134.197 109.077 -46.485  1.00 18.59           O  
-HETATM 3522  O   HOH B2029     137.535 108.965 -48.163  1.00 31.18           O  
-HETATM 3523  O   HOH B2030     138.058 101.381 -49.730  1.00 33.05           O  
-HETATM 3524  O   HOH B2031     132.481 103.761 -53.141  1.00 33.85           O  
-HETATM 3525  O   HOH B2032     135.613 100.619 -51.905  1.00 30.85           O  
-HETATM 3526  O   HOH B2033     136.968 102.857 -36.664  1.00 10.54           O  
-HETATM 3527  O   HOH B2034     130.075 108.425 -34.847  1.00 15.66           O  
-HETATM 3528  O   HOH B2035     129.365 111.791 -40.049  1.00 24.12           O  
-HETATM 3529  O   HOH B2036     125.415 106.813 -29.830  1.00 18.32           O  
-HETATM 3530  O   HOH B2037     124.570 100.487 -27.031  1.00 15.26           O  
-HETATM 3531  O   HOH B2038     125.434 102.918 -22.368  1.00 21.30           O  
-HETATM 3532  O   HOH B2039     127.536 105.262 -22.617  1.00 13.09           O  
-HETATM 3533  O   HOH B2040     120.878 106.857 -25.508  1.00 30.65           O  
-HETATM 3534  O   HOH B2041     122.543 108.344 -26.822  1.00 35.23           O  
-HETATM 3535  O   HOH B2042     120.957 108.163 -19.231  1.00 34.76           O  
-HETATM 3536  O   HOH B2043     118.397 102.399 -19.936  1.00 33.46           O  
-HETATM 3537  O   HOH B2044     120.283 102.876 -16.181  1.00 24.37           O  
-HETATM 3538  O   HOH B2045     120.263  98.679 -21.833  1.00 27.03           O  
-HETATM 3539  O   HOH B2046     119.346 102.772 -23.806  1.00 32.90           O  
-HETATM 3540  O   HOH B2047     123.318 100.001 -24.444  1.00 16.96           O  
-HETATM 3541  O   HOH B2048     125.396 106.330 -19.870  1.00 14.43           O  
-HETATM 3542  O   HOH B2049     122.347 105.895 -14.640  1.00 27.00           O  
-HETATM 3543  O   HOH B2050     123.367 104.650 -11.180  1.00 35.71           O  
-HETATM 3544  O   HOH B2051     126.972 105.766 -13.355  1.00 38.26           O  
-HETATM 3545  O   HOH B2052     122.763  96.036 -14.461  1.00 25.61           O  
-HETATM 3546  O   HOH B2053     119.880 101.297  -9.227  1.00 39.97           O  
-HETATM 3547  O   HOH B2054     118.289  97.868 -20.195  1.00 32.02           O  
-HETATM 3548  O   HOH B2055     119.147  94.572 -23.539  1.00 26.35           O  
-HETATM 3549  O   HOH B2056     135.814 104.623 -25.679  1.00 23.37           O  
-HETATM 3550  O   HOH B2057     132.770 106.388 -19.196  1.00 14.34           O  
-HETATM 3551  O   HOH B2058     139.085  98.564 -23.655  1.00 32.10           O  
-HETATM 3552  O   HOH B2059     138.800  98.519 -20.317  1.00 29.01           O  
-HETATM 3553  O   HOH B2060     139.501 102.114 -29.430  1.00 30.87           O  
-HETATM 3554  O   HOH B2061     140.005  98.613 -28.683  1.00 29.69           O  
-HETATM 3555  O   HOH B2062     140.228  99.780 -26.126  1.00 31.46           O  
-HETATM 3556  O   HOH B2063     135.484  91.476 -17.180  1.00 30.99           O  
-HETATM 3557  O   HOH B2064     136.905  92.929 -15.921  1.00 36.43           O  
-HETATM 3558  O   HOH B2065     145.085  98.828 -31.120  1.00 32.76           O  
-HETATM 3559  O   HOH B2066     143.986 105.047 -40.315  1.00 43.60           O  
-HETATM 3560  O   HOH B2067     141.633 106.276 -36.265  1.00 35.59           O  
-HETATM 3561  O   HOH B2068     143.085 105.849 -33.849  1.00 47.10           O  
-HETATM 3562  O   HOH B2069     134.143 112.887 -36.957  1.00 40.30           O  
-HETATM 3563  O   HOH B2070     139.425 106.895 -35.115  1.00 21.06           O  
-HETATM 3564  O   HOH B2071     141.822 106.372 -44.787  1.00 44.58           O  
-HETATM 3565  O   HOH B2072     124.245  89.597 -24.439  1.00 11.14           O  
-HETATM 3566  O   HOH B2073     121.369  88.998 -14.668  1.00 25.73           O  
-HETATM 3567  O   HOH B2074     122.611  87.642 -16.825  1.00 16.74           O  
-HETATM 3568  O   HOH B2075     120.375  87.077 -18.715  1.00 24.45           O  
-HETATM 3569  O   HOH B2076     120.362 109.245 -24.315  1.00 32.51           O  
-HETATM 3570  O   HOH B2077     123.358 108.281 -18.832  1.00 30.29           O  
-HETATM 3571  O   HOH B2078     117.691 101.444 -16.762  1.00 37.70           O  
-HETATM 3572  O   HOH B2079     119.805 105.494 -15.538  1.00 32.40           O  
-HETATM 3573  O   HOH B2080     119.984  98.712 -24.492  1.00 25.19           O  
-HETATM 3574  O   HOH B2081     126.009 106.632 -16.819  1.00 30.99           O  
-HETATM 3575  O   HOH B2082     115.572  91.741 -20.967  1.00 41.94           O  
-HETATM 3576  O   HOH B2083     121.096 103.669  -9.772  1.00 37.77           O  
-HETATM 3577  O   HOH B2084     128.190 107.348 -15.645  1.00 39.05           O  
-HETATM 3578  O   HOH B2085     117.074  90.723 -24.654  1.00 25.17           O  
-HETATM 3579  O   HOH B2086     115.464  90.060 -27.115  1.00 39.21           O  
-HETATM 3580  O   HOH B2087     115.458  93.577 -27.266  1.00 34.44           O  
-HETATM 3581  O   HOH B2088     116.801  93.005 -23.842  1.00 31.86           O  
-HETATM 3582  O   HOH B2089     118.345  96.685 -24.966  1.00 38.65           O  
-HETATM 3583  O   HOH B2090     120.773 102.798 -31.896  1.00 30.53           O  
-HETATM 3584  O   HOH B2091     122.062 107.952 -31.168  1.00 42.13           O  
-HETATM 3585  O   HOH B2092     141.058 101.850 -24.332  1.00 47.10           O  
-HETATM 3586  O   HOH B2093     126.185 107.024 -40.435  1.00 15.49           O  
-HETATM 3587  O   HOH B2094     127.210 110.287 -40.619  1.00 35.83           O  
-HETATM 3588  O   HOH B2095     126.795 110.585 -47.131  1.00 38.35           O  
-HETATM 3589  O   HOH B2096     129.127 112.965 -44.194  1.00 35.25           O  
-HETATM 3590  O   HOH B2097     133.012 112.567 -39.440  1.00 31.82           O  
-HETATM 3591  O   HOH B2098     130.677 113.444 -42.201  1.00 38.91           O  
-HETATM 3592  O   HOH B2099     135.815 109.860 -44.220  1.00 26.55           O  
-HETATM 3593  O   HOH B2100     118.848 101.500 -30.692  1.00 34.30           O  
-HETATM 3594  O   HOH B2101     121.169 109.440 -33.381  1.00 42.59           O  
-HETATM 3595  O   HOH B2102     133.315 107.365 -50.447  1.00 34.17           O  
-HETATM 3596  O   HOH B2103     132.259 113.861 -44.237  1.00 39.45           O  
-HETATM 3597  O   HOH B2104     135.422 115.517 -36.735  1.00 29.72           O  
-HETATM 3598  O   HOH B2105     127.486 109.120 -49.329  1.00 30.47           O  
-HETATM 3599  O   HOH B2106     130.376 106.536 -51.095  1.00 29.80           O  
-HETATM 3600  O   HOH B2107     127.524 103.745 -52.521  1.00 29.17           O  
-HETATM 3601  O   HOH B2108     129.948 103.359 -52.352  1.00 28.05           O  
-HETATM 3602  O   HOH B2109     124.932 102.812 -52.878  1.00 29.22           O  
-HETATM 3603  O   HOH B2110     128.619 102.603 -54.439  1.00 26.16           O  
-HETATM 3604  O   HOH B2111     122.859  98.903 -49.881  1.00 41.47           O  
-HETATM 3605  O   HOH B2112     122.047 104.818 -48.620  1.00 36.74           O  
-HETATM 3606  O   HOH B2113     124.572 100.846 -50.684  1.00 33.53           O  
-HETATM 3607  O   HOH B2114     123.886  92.644 -49.626  1.00 26.82           O  
-HETATM 3608  O   HOH B2115     124.692  88.332 -47.551  1.00 18.82           O  
-HETATM 3609  O   HOH B2116     133.729  83.802 -45.431  1.00 19.18           O  
-HETATM 3610  O   HOH B2117     125.212  95.569 -48.385  1.00 22.86           O  
-HETATM 3611  O   HOH B2118     138.279  89.063 -39.744  1.00 23.43           O  
-HETATM 3612  O   HOH B2119     132.078  90.094 -46.752  1.00 12.96           O  
-HETATM 3613  O   HOH B2120     129.649  88.611 -49.326  1.00 10.78           O  
-HETATM 3614  O   HOH B2121     125.579  87.998 -44.672  1.00 15.04           O  
-HETATM 3615  O   HOH B2122     128.503  85.997 -49.297  1.00 13.72           O  
-HETATM 3616  O   HOH B2123     130.009  84.258 -47.333  1.00 24.71           O  
-HETATM 3617  O   HOH B2124     131.748  84.675 -43.740  1.00 11.52           O  
-HETATM 3618  O   HOH B2125     133.060  87.485 -47.283  1.00 17.24           O  
-HETATM 3619  O   HOH B2126     128.032  91.164 -37.565  1.00  8.51           O  
-HETATM 3620  O   HOH B2127     143.776  82.431 -16.454  1.00 45.66           O  
-HETATM 3621  O   HOH B2128     135.691  91.242 -37.264  1.00  8.77           O  
-HETATM 3622  O   HOH B2129     137.118  86.597 -41.014  1.00 21.23           O  
-HETATM 3623  O   HOH B2130     135.122  86.314 -46.008  1.00 23.45           O  
-HETATM 3624  O   HOH B2131     135.988  75.116 -36.204  1.00 32.02           O  
-HETATM 3625  O   HOH B2132     138.245  90.133 -37.106  1.00 14.09           O  
-HETATM 3626  O   HOH B2133     122.443  81.113 -16.248  1.00 40.39           O  
-HETATM 3627  O   HOH B2134     134.277  85.058 -32.136  1.00  7.39           O  
-HETATM 3628  O   HOH B2135     138.430  83.955 -31.339  1.00  9.91           O  
-HETATM 3629  O   HOH B2136     121.160  71.164 -20.407  1.00 29.25           O  
-HETATM 3630  O   HOH B2137     141.758  85.111 -28.809  1.00  9.25           O  
-HETATM 3631  O   HOH B2138     137.666  80.211 -25.315  1.00 11.43           O  
-HETATM 3632  O   HOH B2139     142.344  87.910 -21.916  1.00 14.82           O  
-HETATM 3633  O   HOH B2140     140.408  96.826 -22.782  1.00 32.62           O  
-HETATM 3634  O   HOH B2141     142.858  94.416 -18.735  1.00 42.07           O  
-HETATM 3635  O   HOH B2142     140.256  94.284 -18.701  1.00 38.71           O  
-HETATM 3636  O   HOH B2143     125.214  74.000 -35.913  1.00 36.18           O  
-HETATM 3637  O   HOH B2144     142.609  86.476 -16.925  1.00 33.61           O  
-HETATM 3638  O   HOH B2145     147.518  91.092 -18.260  1.00 39.84           O  
-HETATM 3639  O   HOH B2146     148.626  91.173 -21.672  1.00 29.42           O  
-HETATM 3640  O   HOH B2147     149.051  88.886 -20.583  1.00 32.66           O  
-HETATM 3641  O   HOH B2148     145.607  80.619 -23.102  1.00 33.99           O  
-HETATM 3642  O   HOH B2149     150.189  81.501 -23.983  1.00 15.18           O  
-HETATM 3643  O   HOH B2150     146.894  81.293 -25.845  1.00 16.96           O  
-HETATM 3644  O   HOH B2151     148.622  81.789 -18.447  1.00 40.46           O  
-HETATM 3645  O   HOH B2152     147.963  83.502 -16.497  1.00 42.90           O  
-HETATM 3646  O   HOH B2153     148.572  88.795 -16.987  1.00 41.09           O  
-HETATM 3647  O   HOH B2154     117.943  94.661 -35.732  1.00 37.93           O  
-HETATM 3648  O   HOH B2155     119.042  94.820 -42.192  1.00 42.54           O  
-HETATM 3649  O   HOH B2156     145.114  84.713 -16.819  1.00 32.76           O  
-HETATM 3650  O   HOH B2157     121.997  88.003 -48.085  1.00 40.18           O  
-HETATM 3651  O   HOH B2158     130.643  78.919 -44.061  1.00 40.69           O  
-HETATM 3652  O   HOH B2159     135.112  74.238 -40.614  1.00 41.24           O  
-HETATM 3653  O   HOH B2160     134.547  78.664 -45.185  1.00 45.90           O  
-HETATM 3654  O   HOH B2161     141.867  85.700 -39.412  1.00 40.15           O  
-HETATM 3655  O   HOH B2162     137.510  77.583 -24.157  1.00 22.12           O  
-HETATM 3656  O   HOH B2163     140.642  77.116 -22.017  1.00 36.97           O  
-HETATM 3657  O   HOH B2164     142.332  77.663 -29.592  1.00 14.90           O  
-HETATM 3658  O   HOH B2165     139.237  77.396 -27.848  1.00 20.73           O  
-HETATM 3659  O   HOH B2166     132.787  82.079 -30.450  1.00  6.61           O  
-HETATM 3660  O   HOH B2167     136.039  82.917 -31.941  1.00  7.06           O  
-HETATM 3661  O   HOH B2168     132.838  81.114 -22.812  1.00 11.04           O  
-HETATM 3662  O   HOH B2169     139.729  75.619 -30.630  1.00 25.74           O  
-HETATM 3663  O   HOH B2170     133.691  75.150 -32.726  1.00 13.98           O  
-HETATM 3664  O   HOH B2171     132.486  75.995 -27.884  1.00 10.74           O  
-HETATM 3665  O   HOH B2172     136.298  76.350 -33.862  1.00 19.00           O  
-HETATM 3666  O   HOH B2173     119.455  96.922 -40.736  1.00 39.23           O  
-HETATM 3667  O   HOH B2174     134.502  75.239 -24.358  1.00 19.91           O  
-HETATM 3668  O   HOH B2175     123.692  75.426 -27.074  1.00 23.24           O  
-HETATM 3669  O   HOH B2176     131.248  75.626 -17.662  1.00 17.39           O  
-HETATM 3670  O   HOH B2177     129.433  77.617 -17.100  1.00 26.44           O  
-HETATM 3671  O   HOH B2178     131.609  70.321 -23.976  1.00 15.24           O  
-HETATM 3672  O   HOH B2179     128.076  70.384 -20.529  1.00  9.64           O  
-HETATM 3673  O   HOH B2180     117.377  99.393 -28.075  1.00 43.20           O  
-HETATM 3674  O   HOH B2181     125.602  70.893 -19.495  1.00 14.11           O  
-HETATM 3675  O   HOH B2182     122.095  77.187 -18.278  1.00 25.55           O  
-HETATM 3676  O   HOH B2183     122.870  79.816 -18.386  1.00 23.39           O  
-HETATM 3677  O   HOH B2184     123.753  72.542 -27.737  1.00 20.41           O  
-HETATM 3678  O   HOH B2185     133.482  70.035 -27.512  1.00 12.40           O  
-HETATM 3679  O   HOH B2186     123.401  68.558 -25.399  1.00 25.17           O  
-HETATM 3680  O   HOH B2187     123.546  70.135 -21.131  1.00 17.71           O  
-HETATM 3681  O   HOH B2188     119.765  73.226 -21.490  1.00 33.77           O  
-HETATM 3682  O   HOH B2189     120.804  78.841 -22.405  1.00 38.67           O  
-HETATM 3683  O   HOH B2190     120.285  76.906 -20.367  1.00 34.97           O  
-HETATM 3684  O   HOH B2191     140.401  91.391 -42.138  1.00 33.61           O  
-HETATM 3685  O   HOH B2192     121.086  68.957 -28.942  1.00 43.30           O  
-HETATM 3686  O   HOH B2193     123.327  69.898 -27.881  1.00 32.52           O  
-HETATM 3687  O   HOH B2194     122.000  74.023 -29.693  1.00 31.88           O  
-HETATM 3688  O   HOH B2195     121.331  84.205 -35.495  1.00 22.37           O  
-HETATM 3689  O   HOH B2196     119.467  84.784 -33.170  1.00 35.12           O  
-HETATM 3690  O   HOH B2197     125.015  78.324 -39.763  1.00 32.79           O  
-HETATM 3691  O   HOH B2198     124.076  75.878 -37.116  1.00 38.31           O  
-HETATM 3692  O   HOH B2199     125.776  80.147 -30.239  1.00  8.95           O  
-HETATM 3693  O   HOH B2200     130.857 101.211  -6.677  1.00 47.67           O  
-HETATM 3694  O   HOH B2201     130.118  74.479 -35.905  1.00 18.90           O  
-HETATM 3695  O   HOH B2202     127.854  73.159 -34.697  1.00 21.91           O  
-HETATM 3696  O   HOH B2203     131.582  76.182 -34.066  1.00 14.12           O  
-HETATM 3697  O   HOH B2204     130.063  84.282 -33.843  1.00  8.17           O  
-HETATM 3698  O   HOH B2205     131.691  84.294 -31.586  1.00  7.24           O  
-HETATM 3699  O   HOH B2206     119.512  83.338 -29.865  1.00 34.54           O  
-HETATM 3700  O   HOH B2207     119.528  86.628 -36.573  1.00 24.70           O  
-HETATM 3701  O   HOH B2208     120.247  92.866 -35.588  1.00 13.07           O  
-HETATM 3702  O   HOH B2209     115.711  92.841 -31.317  1.00 37.53           O  
-HETATM 3703  O   HOH B2210     114.281  88.842 -30.551  1.00 31.47           O  
-HETATM 3704  O   HOH B2211     117.115  86.213 -33.458  1.00 32.06           O  
-HETATM 3705  O   HOH B2212     118.078  91.122 -43.203  1.00 32.74           O  
-HETATM 3706  O   HOH B2213     121.416  93.254 -42.662  1.00 18.69           O  
-HETATM 3707  O   HOH B2214     121.324  93.167 -38.131  1.00 22.22           O  
-HETATM 3708  O   HOH B2215     114.515  88.614 -39.714  1.00 39.48           O  
-HETATM 3709  O   HOH B2216     121.485  83.480 -43.414  1.00 29.74           O  
-HETATM 3710  O   HOH B2217     123.158  86.926 -45.829  1.00 37.09           O  
-HETATM 3711  O   HOH B2218     122.176  90.451 -49.329  1.00 41.16           O  
-HETATM 3712  O   HOH B2219     129.420  83.309 -44.520  1.00 23.14           O  
-HETATM 3713  O   HOH B2220     125.732  85.984 -48.491  1.00 17.25           O  
-HETATM 3714  O   HOH B2221     122.322  84.551 -45.943  1.00 39.35           O  
-HETATM 3715  O   HOH B2222     125.457  80.566 -41.393  1.00 14.74           O  
-HETATM 3716  O   HOH B2223     129.245  80.769 -43.402  1.00 27.10           O  
-HETATM 3717  O   HOH B2224     135.542  83.439 -38.426  1.00  9.95           O  
-HETATM 3718  O   HOH B2225     131.628  77.884 -41.549  1.00 17.38           O  
-HETATM 3719  O   HOH B2226     133.864  76.376 -42.449  1.00 31.65           O  
-HETATM 3720  O   HOH B2227     136.795  75.540 -38.813  1.00 30.76           O  
-HETATM 3721  O   HOH B2228     132.596  73.894 -39.040  1.00 34.38           O  
-HETATM 3722  O   HOH B2229     141.596  81.748 -43.218  1.00 42.32           O  
-HETATM 3723  O   HOH B2230     137.860  84.253 -39.808  1.00 15.07           O  
-HETATM 3724  O   HOH B2231     138.218  84.401 -43.595  1.00 41.45           O  
-HETATM 3725  O   HOH B2232     137.548  81.996 -44.405  1.00 40.42           O  
-HETATM 3726  O   HOH B2233     141.380  84.154 -41.618  1.00 35.54           O  
-HETATM 3727  O   HOH B2234     137.164  79.596 -43.864  1.00 25.97           O  
-HETATM 3728  O   HOH B2235     140.260  84.203 -38.135  1.00 19.50           O  
-HETATM 3729  O   HOH B2236     123.532  96.425 -41.193  1.00 19.68           O  
-HETATM 3730  O   HOH B2237     118.704  99.557 -40.779  1.00 29.82           O  
-HETATM 3731  O   HOH B2238     117.703  99.972 -44.585  1.00 32.15           O  
-HETATM 3732  O   HOH B2239     115.837 102.779 -45.139  1.00 39.66           O  
-HETATM 3733  O   HOH B2240     118.715 105.971 -44.805  1.00 36.02           O  
-HETATM 3734  O   HOH B2241     118.293 102.639 -38.468  1.00 25.86           O  
-HETATM 3735  O   HOH B2242     117.596 111.066 -35.674  1.00 42.60           O  
-HETATM 3736  O   HOH B2243     119.869 102.923 -35.648  1.00 20.67           O  
-HETATM 3737  O   HOH B2244     119.858 108.100 -35.243  1.00 36.95           O  
-HETATM 3738  O   HOH B2245     119.185 105.457 -34.458  1.00 42.24           O  
-HETATM 3739  O   HOH B2246     120.233 114.125 -39.574  1.00 31.79           O  
-HETATM 3740  O   HOH B2247     118.634 113.275 -36.513  1.00 39.28           O  
-HETATM 3741  O   HOH B2248     122.147 111.548 -34.732  1.00 36.70           O  
-HETATM 3742  O   HOH B2249     119.138 100.171 -37.997  1.00 20.01           O  
-HETATM 3743  O   HOH B2250     121.315  95.803 -39.079  1.00 27.19           O  
-HETATM 3744  O   HOH B2251     118.148  97.613 -36.174  1.00 37.50           O  
-HETATM 3745  O   HOH B2252     117.867  99.216 -30.650  1.00 38.06           O  
-HETATM 3746  O   HOH B2253     120.183  85.557 -31.052  1.00 32.92           O  
-HETATM 3747  O   HOH B2254     117.600  87.035 -28.529  1.00 40.79           O  
-HETATM 3748  O   HOH B2255     121.552  83.428 -15.697  1.00 36.85           O  
-HETATM 3749  O   HOH B2256     130.851  87.050 -15.597  1.00 17.41           O  
-HETATM 3750  O   HOH B2257     135.160  87.931 -21.025  1.00 13.25           O  
-HETATM 3751  O   HOH B2258     130.022  81.383 -14.275  1.00 32.29           O  
-HETATM 3752  O   HOH B2259     134.917  81.516 -13.010  1.00 32.12           O  
-HETATM 3753  O   HOH B2260     128.104  85.407 -13.174  1.00 34.58           O  
-HETATM 3754  O   HOH B2261     130.945  78.544 -14.759  1.00 20.28           O  
-HETATM 3755  O   HOH B2262     138.954  78.039 -20.078  1.00 26.94           O  
-HETATM 3756  O   HOH B2263     141.601  84.439 -15.505  1.00 38.93           O  
-HETATM 3757  O   HOH B2264     141.430  78.955 -19.314  1.00 34.98           O  
-HETATM 3758  O   HOH B2265     142.575  80.808 -18.150  1.00 35.10           O  
-HETATM 3759  O   HOH B2266     137.246  90.946 -41.697  1.00 23.41           O  
-HETATM 3760  O   HOH B2267     139.666  92.991 -39.551  1.00 28.96           O  
-HETATM 3761  O   HOH B2268     136.568  88.157 -44.335  1.00 28.70           O  
-HETATM 3762  O   HOH B2269     138.736  96.133 -51.371  1.00 30.31           O  
-HETATM 3763  O   HOH B2270     132.925  86.625 -49.810  1.00 21.93           O  
-HETATM 3764  O   HOH B2271     131.623  89.738 -54.955  1.00 10.32           O  
-HETATM 3765  O   HOH B2272     137.303  85.635 -47.620  1.00 35.23           O  
-HETATM 3766  O   HOH B2273     138.884  87.762 -48.467  1.00 41.24           O  
-HETATM 3767  O   HOH B2274     133.708  88.161 -54.135  1.00 13.69           O  
-HETATM 3768  O   HOH B2275     138.487  88.205 -54.050  1.00 37.44           O  
-HETATM 3769  O   HOH B2276     135.701  85.715 -51.275  1.00 26.04           O  
-HETATM 3770  O   HOH B2277     138.357  91.979 -43.794  1.00 22.01           O  
-HETATM 3771  O   HOH B2278     141.043  88.663 -51.227  1.00 44.13           O  
-HETATM 3772  O   HOH B2279     139.848  90.678 -53.892  1.00 37.62           O  
-HETATM 3773  O   HOH B2280     141.645  92.687 -46.404  1.00 23.71           O  
-HETATM 3774  O   HOH B2281     141.683  95.711 -47.617  1.00 29.36           O  
-HETATM 3775  O   HOH B2282     140.697  99.478 -47.128  1.00 34.21           O  
-HETATM 3776  O   HOH B2283     141.981  92.558 -40.309  1.00 35.83           O  
-HETATM 3777  O   HOH B2284     139.421  97.227 -18.085  1.00 40.86           O  
-HETATM 3778  O   HOH B2285     136.021  91.670 -19.875  1.00 26.86           O  
-HETATM 3779  O   HOH B2286     133.698  94.232 -12.723  1.00 29.51           O  
-HETATM 3780  O   HOH B2287     134.486  87.237 -14.592  1.00 21.12           O  
-HETATM 3781  O   HOH B2288     127.836  91.303 -12.199  1.00 19.66           O  
-HETATM 3782  O   HOH B2289     128.526  87.857 -13.115  1.00 32.25           O  
-HETATM 3783  O   HOH B2290     128.824  99.893  -7.825  1.00 37.66           O  
-HETATM 3784  O   HOH B2291     130.960  95.294  -9.123  1.00 26.00           O  
-HETATM 3785  O   HOH B2292     128.065 107.261 -20.892  1.00 15.93           O  
-HETATM 3786  O   HOH B2293     130.295 107.449 -17.059  1.00 21.26           O  
-HETATM 3787  O   HOH B2294     131.571 105.011 -10.981  1.00 27.10           O  
-HETATM 3788  O   HOH B2295     138.834  99.775 -13.865  1.00 31.47           O  
-HETATM 3789  O   HOH B2296     138.296  97.865 -15.733  1.00 35.25           O  
-HETATM 3790  O   HOH B2297     136.347 106.310 -15.004  1.00 32.35           O  
-HETATM 3791  O   HOH B2298     130.180 105.452 -13.148  1.00 33.29           O  
-HETATM 3792  O   HOH B2299     133.824 107.534 -14.599  1.00 39.31           O  
-CONECT  633 3140                                                                
-CONECT  657 3140                                                                
-CONECT 1143 3140                                                                
-CONECT 1146 3140                                                                
-CONECT 1176 3140                                                                
-CONECT 2207 3154                                                                
-CONECT 2231 3154                                                                
-CONECT 2707 3154                                                                
-CONECT 2737 3154                                                                
-CONECT 3127 3128 3130 3133                                                      
-CONECT 3128 3127 3129 3137                                                      
-CONECT 3129 3128 3132 3136                                                      
-CONECT 3130 3127 3131                                                           
-CONECT 3131 3130 3134 3139                                                      
-CONECT 3132 3129 3135                                                           
-CONECT 3133 3127 3135                                                           
-CONECT 3134 3131                                                                
-CONECT 3135 3132 3133 3138                                                      
-CONECT 3136 3129                                                                
-CONECT 3137 3128                                                                
-CONECT 3138 3135                                                                
-CONECT 3139 3131                                                                
-CONECT 3140  633  657 1143 1146                                                 
-CONECT 3140 1176                                                                
-CONECT 3141 3142 3144 3147                                                      
-CONECT 3142 3141 3143 3151                                                      
-CONECT 3143 3142 3146 3150                                                      
-CONECT 3144 3141 3145                                                           
-CONECT 3145 3144 3148 3153                                                      
-CONECT 3146 3143 3149                                                           
-CONECT 3147 3141 3149                                                           
-CONECT 3148 3145                                                                
-CONECT 3149 3146 3147 3152                                                      
-CONECT 3150 3143                                                                
-CONECT 3151 3142                                                                
-CONECT 3152 3149                                                                
-CONECT 3153 3145                                                                
-CONECT 3154 2207 2231 2707 2737                                                 
-MASTER      541    0    4    5   22    0    6    6 3790    2   38   34          
-END                                                                             
diff --git a/plip/test/pdb/4alw.pdb b/plip/test/pdb/4alw.pdb
deleted file mode 100644
index 285ce4b..0000000
--- a/plip/test/pdb/4alw.pdb
+++ /dev/null
@@ -1,3305 +0,0 @@
-HEADER    TRANSFERASE                             05-MAR-12   4ALW              
-TITLE     BENZOFUROPYRIMIDINONE INHIBITORS OF PIM-1                             
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: PIM-1 KINASE;                                              
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 FRAGMENT: PROTEIN KINASE DOMAIN, RESIDUES 406-717;                   
-COMPND   5 EC: 2.7.1.37;                                                        
-COMPND   6 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
-SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
-KEYWDS    TRANSFERASE, PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE PIM-1     
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    T.J.STOUT,L.ADAMS                                                     
-REVDAT   1   16-JAN-13 4ALW    0                                                
-JRNL        AUTH   A.L.TSUHAKO,D.S.BROWN,E.S.KOLTUN,N.AAY,A.ARCALAS,V.CHAN,     
-JRNL        AUTH 2 H.DU,S.ENGST,M.FRANZINI,A.GALAN,P.HUANG,S.JOHNSTON,B.KANE,   
-JRNL        AUTH 3 M.H.KIM,A.D.LAIRD,R.LIN,L.MOCK,I.NGAN,M.PACK,G.STOTT,        
-JRNL        AUTH 4 T.J.STOUT,P.YU,C.ZAHARIA,W.ZHANG,P.ZHOU,J.M.NUSS,            
-JRNL        AUTH 5 P.C.KEARNEY,W.XU                                             
-JRNL        TITL   THE DESIGN, SYNTHESIS, AND BIOLOGICAL EVALUATION OF PIM      
-JRNL        TITL 2 KINASE INHIBITORS.                                           
-JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  3732 2012              
-JRNL        REFN                   ISSN 0960-894X                               
-JRNL        PMID   22542012                                                     
-JRNL        DOI    10.1016/J.BMCL.2012.04.025                                   
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.92 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
-REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.42                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.32                          
-REMARK   3   NUMBER OF REFLECTIONS             : 31220                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.15781                         
-REMARK   3   R VALUE            (WORKING SET) : 0.15516                         
-REMARK   3   FREE R VALUE                     : 0.20731                         
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
-REMARK   3   FREE R VALUE TEST SET COUNT      : 1670                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.920                        
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.970                        
-REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2214                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.36                        
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.368                        
-REMARK   3   BIN FREE R VALUE SET COUNT          : 142                          
-REMARK   3   BIN FREE R VALUE                    : 0.474                        
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 2263                                    
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 33                                      
-REMARK   3   SOLVENT ATOMS            : 337                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.685                         
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 0.00                                                 
-REMARK   3    B22 (A**2) : 0.00                                                 
-REMARK   3    B33 (A**2) : 0.00                                                 
-REMARK   3    B12 (A**2) : 0.00                                                 
-REMARK   3    B13 (A**2) : 0.00                                                 
-REMARK   3    B23 (A**2) : 0.00                                                 
-REMARK   3                                                                      
-REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
-REMARK   3   ESU BASED ON R VALUE                            (A): 0.109         
-REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
-REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
-REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.009         
-REMARK   3                                                                      
-REMARK   3  CORRELATION COEFFICIENTS.                                           
-REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
-REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
-REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2363 ; 0.031 ; 0.021       
-REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
-REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3211 ; 2.238 ; 1.962       
-REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
-REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   280 ; 6.771 ; 5.000       
-REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;33.585 ;23.065       
-REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   395 ;13.795 ;15.000       
-REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;17.316 ;15.000       
-REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   339 ; 0.191 ; 0.200       
-REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1841 ; 0.012 ; 0.020       
-REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1238 ; 0.236 ; 0.200       
-REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1614 ; 0.320 ; 0.200       
-REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   298 ; 0.231 ; 0.200       
-REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.213 ; 0.200       
-REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.278 ; 0.200       
-REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
-REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1427 ; 1.845 ; 1.500       
-REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2231 ; 2.715 ; 2.000       
-REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1141 ; 4.345 ; 3.000       
-REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   976 ; 6.036 ; 4.500       
-REMARK   3                                                                      
-REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
-REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS STATISTICS                                           
-REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
-REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
-REMARK   3   VDW PROBE RADIUS   : 1.20                                          
-REMARK   3   ION PROBE RADIUS   : 0.80                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
-REMARK   3  POSITIONS.                                                          
-REMARK   4                                                                      
-REMARK   4 4ALW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-12.                  
-REMARK 100 THE PDBE ID CODE IS EBI-51570.                                       
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 04-JAN-07                          
-REMARK 200  TEMPERATURE           (KELVIN) : 155                                
-REMARK 200  PH                             : 7.2                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : SSRL                               
-REMARK 200  BEAMLINE                       : BL11-1                             
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD (MX-325)                       
-REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
-REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33275                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.92                               
-REMARK 200  RESOLUTION RANGE LOW       (A) : 37.42                              
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
-REMARK 200  DATA REDUNDANCY                : 7.4                                
-REMARK 200  R MERGE                    (I) : 0.07                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.33                              
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : 5.92                               
-REMARK 200  R MERGE FOR SHELL          (I) : 1.28                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.60                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASER                                                
-REMARK 200 STARTING MODEL: IN-HOUSE PIM1 STRUCTURE                              
-REMARK 200                                                                      
-REMARK 200 REMARK: NONE                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 64                                        
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9                      
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -Y,X-Y,Z+2/3                                            
-REMARK 290       3555   -X+Y,-X,Z+1/3                                           
-REMARK 290       4555   -X,-Y,Z+1/2                                             
-REMARK 290       5555   Y,-X+Y,Z+1/6                                            
-REMARK 290       6555   X-Y,X,Z+5/6                                             
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.00200            
-REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       27.00100            
-REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.50150            
-REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       13.50050            
-REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       67.50250            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A   -14                                                      
-REMARK 465     HIS A   -13                                                      
-REMARK 465     HIS A   -12                                                      
-REMARK 465     HIS A   -11                                                      
-REMARK 465     HIS A   -10                                                      
-REMARK 465     HIS A    -9                                                      
-REMARK 465     HIS A    -8                                                      
-REMARK 465     GLY A    -7                                                      
-REMARK 465     GLU A    -6                                                      
-REMARK 465     ASN A    -5                                                      
-REMARK 465     LEU A    -4                                                      
-REMARK 465     TYR A    -3                                                      
-REMARK 465     PHE A    -2                                                      
-REMARK 465     GLN A    -1                                                      
-REMARK 465     GLY A     0                                                      
-REMARK 465     SER A     1                                                      
-REMARK 465     LEU A     2                                                      
-REMARK 465     LEU A     3                                                      
-REMARK 465     SER A     4                                                      
-REMARK 465     LYS A     5                                                      
-REMARK 465     ILE A     6                                                      
-REMARK 465     ASN A     7                                                      
-REMARK 465     SER A     8                                                      
-REMARK 465     LEU A     9                                                      
-REMARK 465     ALA A    10                                                      
-REMARK 465     HIS A    11                                                      
-REMARK 465     LEU A    12                                                      
-REMARK 465     ARG A    13                                                      
-REMARK 465     ALA A    14                                                      
-REMARK 465     ALA A    15                                                      
-REMARK 465     PRO A    16                                                      
-REMARK 465     CYS A    17                                                      
-REMARK 465     ASN A    18                                                      
-REMARK 465     ASP A    19                                                      
-REMARK 465     LEU A    20                                                      
-REMARK 465     HIS A    21                                                      
-REMARK 465     ALA A    22                                                      
-REMARK 465     THR A    23                                                      
-REMARK 465     LYS A    24                                                      
-REMARK 465     LEU A    25                                                      
-REMARK 465     ALA A    26                                                      
-REMARK 465     PRO A    27                                                      
-REMARK 465     GLY A    28                                                      
-REMARK 465     LYS A    29                                                      
-REMARK 465     GLU A    30                                                      
-REMARK 465     LYS A    31                                                      
-REMARK 465     GLU A    32                                                      
-REMARK 465     PRO A    33                                                      
-REMARK 465     LEU A   307                                                      
-REMARK 465     SER A   308                                                      
-REMARK 465     PRO A   309                                                      
-REMARK 465     GLY A   310                                                      
-REMARK 465     PRO A   311                                                      
-REMARK 465     SER A   312                                                      
-REMARK 465     LYS A   313                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   OD1  ASP A    72     O    HOH A  2047              2.14            
-REMARK 500   OG   SER A   222     C2   IMD A  1309              2.03            
-REMARK 500   O    HOH A  2016     O    HOH A  2336              2.17            
-REMARK 500   O    HOH A  2025     O    HOH A  2064              1.78            
-REMARK 500   O    HOH A  2026     O    HOH A  2064              1.78            
-REMARK 500   O    HOH A  2058     O    HOH A  2214              2.10            
-REMARK 500   O    HOH A  2117     O    HOH A  2123              2.11            
-REMARK 500   O    HOH A  2138     O    HOH A  2295              1.97            
-REMARK 500   O    HOH A  2194     O    HOH A  2196              2.04            
-REMARK 500   O    HOH A  2238     O    HOH A  2243              2.00            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
-REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
-REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
-REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
-REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
-REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
-REMARK 500                                                                      
-REMARK 500 DISTANCE CUTOFF:                                                     
-REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
-REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
-REMARK 500   O    HOH A  2078     O    HOH A  2289     2544     2.13            
-REMARK 500   O    HOH A  2114     O    HOH A  2270     2544     2.19            
-REMARK 500   O    HOH A  2277     O    HOH A  2325     3655     1.99            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
-REMARK 500    PHE A 147   CD1   PHE A 147   CE1     0.126                       
-REMARK 500    TYR A 207   CD1   TYR A 207   CE1     0.091                       
-REMARK 500    GLU A 262   CD    GLU A 262   OE1     0.077                       
-REMARK 500    GLU A 262   CG    GLU A 262   CD      0.120                       
-REMARK 500    TRP A 269   CG    TRP A 269   CD1     0.092                       
-REMARK 500    PHE A 281   CD1   PHE A 281   CE1     0.129                       
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    ARG A  57   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
-REMARK 500    ARG A  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
-REMARK 500    LEU A 118   CB  -  CG  -  CD1 ANGL. DEV. =  10.7 DEGREES          
-REMARK 500    ARG A 145   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
-REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
-REMARK 500    CYS A 158   CA  -  CB  -  SG  ANGL. DEV. =  -7.7 DEGREES          
-REMARK 500    ARG A 250   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
-REMARK 500    ARG A 268   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
-REMARK 500    CYS A 270   CA  -  CB  -  SG  ANGL. DEV. =  -8.3 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASP A 167       46.78   -140.86                                   
-REMARK 500    ASP A 186       81.46     71.12                                   
-REMARK 500    ASP A 202       32.20   -140.98                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
-REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
-REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
-REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
-REMARK 500                                 MODEL     OMEGA                      
-REMARK 500 GLU A   35     SER A   36                  146.50                    
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A1307                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HY7 A1308                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A1309                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 1XQZ   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF HPIM-1 KINASE AT 2.1 A                         
-REMARK 900  RESOLUTION                                                          
-REMARK 900 RELATED ID: 1XR1   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF HPIM-1 KINASE IN COMPLEX WITH                  
-REMARK 900  AMP-PNPAT 2.1 A RESOLUTION                                          
-REMARK 900 RELATED ID: 1XWS   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 KINASE DOMAIN                   
-REMARK 900 RELATED ID: 1YHS   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF PIM-1 BOUND TO STAUROSPORINE                   
-REMARK 900 RELATED ID: 1YI3   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF PIM-1 BOUND TO LY294002                        
-REMARK 900 RELATED ID: 1YI4   RELATED DB: PDB                                   
-REMARK 900  STRUCTURE OF PIM-1 BOUND TO ADENOSINE                               
-REMARK 900 RELATED ID: 1YWV   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURES OF PROTO-ONCOGENE KINASE PIM1: A                 
-REMARK 900  TARGETOF ABERRANT SOMATIC HYPERMUTATIONS IN DIFFUSE LARGE           
-REMARK 900   CELLLYMPHOMA                                                       
-REMARK 900 RELATED ID: 1YXS   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 WITH P123M MUTATION                
-REMARK 900 RELATED ID: 1YXT   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH                    
-REMARK 900  AMPPNP                                                              
-REMARK 900 RELATED ID: 1YXU   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH AMP                
-REMARK 900 RELATED ID: 1YXV   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH 3,4                
-REMARK 900  -DIHYDROXY-1-METHYLQUINOLIN-2(1H)-ONE                               
-REMARK 900 RELATED ID: 1YXX   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH (3E                
-REMARK 900  )-3-[(4-HYDROXYPHENYL)IMINO]-1H-INDOL-2(3H)-ONE                     
-REMARK 900 RELATED ID: 2BIK   RELATED DB: PDB                                   
-REMARK 900  HUMAN PIM1 PHOSPHORYLATED ON SER261                                 
-REMARK 900 RELATED ID: 2BIL   RELATED DB: PDB                                   
-REMARK 900  THE HUMAN PROTEIN KINASE PIM1 IN COMPLEX WITH ITS                   
-REMARK 900  CONSENSUS PEPTIDE PIMTIDE                                           
-REMARK 900 RELATED ID: 2BZH   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH                 
-REMARK 900  A RUTHENIUM ORGANOMETALLIC LIGAND RU1                               
-REMARK 900 RELATED ID: 2BZI   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH                 
-REMARK 900  A RUTHENIUM ORGANOMETALLIC LIGAND RU2                               
-REMARK 900 RELATED ID: 2BZJ   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH                 
-REMARK 900  A RUTHENIUM ORGANOMETALLIC LIGAND RU3                               
-REMARK 900 RELATED ID: 2BZK   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH                 
-REMARK 900  AMPPNP AND PIMTIDE                                                  
-REMARK 900 RELATED ID: 2C3I   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF HUMAN PIM1 IN COMPLEX WITH                     
-REMARK 900  IMIDAZOPYRIDAZIN I                                                  
-REMARK 900 RELATED ID: 2J2I   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF THE HUMAB PIM1 IN COMPLEX WITH                 
-REMARK 900  LY333531                                                            
-REMARK 900 RELATED ID: 2XIX   RELATED DB: PDB                                   
-REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-1 FROM                
-REMARK 900   CRYSTALLOGRAPHIC FRAGMENT SCREEN                                   
-REMARK 900 RELATED ID: 2XIY   RELATED DB: PDB                                   
-REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-2 FROM                
-REMARK 900   CRYSTALLOGRAPHIC FRAGMENT SCREEN                                   
-REMARK 900 RELATED ID: 2XIZ   RELATED DB: PDB                                   
-REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-3 FROM                
-REMARK 900   CRYSTALLOGRAPHIC FRAGMENT SCREEN                                   
-REMARK 900 RELATED ID: 2XJ0   RELATED DB: PDB                                   
-REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-4 FROM                
-REMARK 900   CRYSTALLOGRAPHIC FRAGMENT SCREEN                                   
-REMARK 900 RELATED ID: 2XJ1   RELATED DB: PDB                                   
-REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE                 
-REMARK 900  INIBITOR                                                            
-REMARK 900 RELATED ID: 2XJ2   RELATED DB: PDB                                   
-REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE                 
-REMARK 900  INHIBITOR                                                           
-REMARK 900 RELATED ID: 4A7C   RELATED DB: PDB                                   
-REMARK 900  CRYSTAL STRUCTURE OF PIM1 KINASE WITH ETP46546                      
-DBREF  4ALW A    2   313  UNP    P11309   PIM1_HUMAN       2    213             
-SEQADV 4ALW MET A  -14  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW HIS A  -13  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW HIS A  -12  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW HIS A  -11  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW HIS A  -10  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW HIS A   -9  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW HIS A   -8  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW GLY A   -7  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW GLU A   -6  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW ASN A   -5  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW LEU A   -4  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW TYR A   -3  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW PHE A   -2  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW GLN A   -1  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW GLY A    0  UNP  P11309              EXPRESSION TAG                 
-SEQADV 4ALW SER A    1  UNP  P11309              EXPRESSION TAG                 
-SEQRES   1 A  328  MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE          
-SEQRES   2 A  328  GLN GLY SER LEU LEU SER LYS ILE ASN SER LEU ALA HIS          
-SEQRES   3 A  328  LEU ARG ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS          
-SEQRES   4 A  328  LEU ALA PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN          
-SEQRES   5 A  328  TYR GLN VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY          
-SEQRES   6 A  328  SER VAL TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO          
-SEQRES   7 A  328  VAL ALA ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP          
-SEQRES   8 A  328  TRP GLY GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU          
-SEQRES   9 A  328  VAL VAL LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY          
-SEQRES  10 A  328  VAL ILE ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER          
-SEQRES  11 A  328  PHE VAL LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP          
-SEQRES  12 A  328  LEU PHE ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU          
-SEQRES  13 A  328  GLU LEU ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA          
-SEQRES  14 A  328  VAL ARG HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP          
-SEQRES  15 A  328  ILE LYS ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY          
-SEQRES  16 A  328  GLU LEU LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU          
-SEQRES  17 A  328  LYS ASP THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL          
-SEQRES  18 A  328  TYR SER PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS          
-SEQRES  19 A  328  GLY ARG SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU          
-SEQRES  20 A  328  TYR ASP MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP          
-SEQRES  21 A  328  GLU GLU ILE ILE ARG GLY GLN VAL PHE PHE ARG GLN ARG          
-SEQRES  22 A  328  VAL SER SER GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU          
-SEQRES  23 A  328  ALA LEU ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE          
-SEQRES  24 A  328  GLN ASN HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN          
-SEQRES  25 A  328  GLU THR ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY          
-SEQRES  26 A  328  PRO SER LYS                                                  
-HET    IMD  A1307       5                                                       
-HET    HY7  A1308      23                                                       
-HET    IMD  A1309       5                                                       
-HETNAM     IMD IMIDAZOLE                                                        
-HETNAM     HY7 8-BROMANYL-2-[(4-METHYLPIPERAZIN-1-YL)METHYL]                    
-HETNAM   2 HY7  -3H-[1]BENZOFURO[3,2-D]PYRIMIDIN-4-ONE                          
-FORMUL   2  IMD    2(C3 H5 N2 1+)                                               
-FORMUL   3  HY7    C16 H17 BR N4 O2                                             
-FORMUL   4  HOH   *337(H2 O)                                                    
-HELIX    1   1 ASP A   72  ILE A   74  5                                   3    
-HELIX    2   2 MET A   88  SER A   97  1                                  10    
-HELIX    3   3 LEU A  129  GLY A  137  1                                   9    
-HELIX    4   4 GLN A  140  CYS A  161  1                                  22    
-HELIX    5   5 LYS A  169  GLU A  171  5                                   3    
-HELIX    6   6 ASP A  186  GLY A  190  5                                   5    
-HELIX    7   7 THR A  204  SER A  208  5                                   5    
-HELIX    8   8 PRO A  209  HIS A  216  1                                   8    
-HELIX    9   9 HIS A  219  GLY A  238  1                                  20    
-HELIX   10  10 HIS A  244  GLY A  251  1                                   8    
-HELIX   11  11 SER A  260  LEU A  271  1                                  12    
-HELIX   12  12 ARG A  274  ARG A  278  5                                   5    
-HELIX   13  13 THR A  280  ASN A  286  1                                   7    
-HELIX   14  14 HIS A  287  GLN A  291  5                                   5    
-HELIX   15  15 LEU A  295  LEU A  304  1                                  10    
-SHEET    1  AA 5 TYR A  38  GLY A  47  0                                        
-SHEET    2  AA 5 GLY A  50  ARG A  57 -1  O  GLY A  50   N  GLY A  47           
-SHEET    3  AA 5 LEU A  62  GLU A  70 -1  O  LEU A  62   N  ARG A  57           
-SHEET    4  AA 5 SER A 115  GLU A 121 -1  O  PHE A 116   N  VAL A  69           
-SHEET    5  AA 5 LEU A 106  GLU A 111 -1  N  LEU A 107   O  ILE A 119           
-SHEET    1  AB 2 TRP A  77  GLU A  79  0                                        
-SHEET    2  AB 2 ARG A  85  PRO A  87 -1  O  VAL A  86   N  GLY A  78           
-SHEET    1  AC 3 VAL A 126  ASP A 128  0                                        
-SHEET    2  AC 3 ILE A 173  ASP A 176 -1  O  ILE A 175   N  GLN A 127           
-SHEET    3  AC 3 GLU A 181  LEU A 184 -1  O  GLU A 181   N  ASP A 176           
-SHEET    1  AD 2 VAL A 163  LEU A 164  0                                        
-SHEET    2  AD 2 ALA A 191  LEU A 192 -1  O  ALA A 191   N  LEU A 164           
-CISPEP   1 GLU A  124    PRO A  125          0         0.04                     
-SITE     1 AC1  7 PHE A 130  ILE A 133  THR A 134  ASP A 170                    
-SITE     2 AC1  7 ASP A 234  GLY A 238  ASP A 239                               
-SITE     1 AC2 13 PHE A  49  VAL A  52  ALA A  65  LYS A  67                    
-SITE     2 AC2 13 LEU A 120  GLU A 121  ASN A 172  LEU A 174                    
-SITE     3 AC2 13 ILE A 185  ASP A 186  HOH A2213  HOH A2336                    
-SITE     4 AC2 13 HOH A2337                                                     
-SITE     1 AC3  5 HIS A 219  ARG A 221  SER A 222  HOH A2249                    
-SITE     2 AC3  5 HOH A2302                                                     
-CRYST1   97.449   97.449   81.003  90.00  90.00 120.00 P 65          6          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.010262  0.005925  0.000000        0.00000                         
-SCALE2      0.000000  0.011849  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.012345        0.00000                         
-ATOM      1  N   LEU A  34       7.313 -40.565 -13.432  1.00 82.72           N  
-ATOM      2  CA  LEU A  34       6.965 -40.395 -11.961  1.00 83.44           C  
-ATOM      3  C   LEU A  34       7.884 -41.192 -10.992  1.00 83.01           C  
-ATOM      4  O   LEU A  34       8.703 -41.979 -11.452  1.00 83.89           O  
-ATOM      5  CB  LEU A  34       5.479 -40.728 -11.705  1.00 83.29           C  
-ATOM      6  CG  LEU A  34       5.078 -42.198 -11.565  1.00 83.23           C  
-ATOM      7  CD1 LEU A  34       4.052 -42.341 -10.444  1.00 83.91           C  
-ATOM      8  CD2 LEU A  34       4.568 -42.753 -12.892  1.00 82.22           C  
-ATOM      9  N   GLU A  35       7.761 -40.987  -9.671  1.00 82.39           N  
-ATOM     10  CA  GLU A  35       8.551 -41.769  -8.685  1.00 81.26           C  
-ATOM     11  C   GLU A  35       7.776 -42.994  -8.257  1.00 79.77           C  
-ATOM     12  O   GLU A  35       7.352 -43.138  -7.099  1.00 79.72           O  
-ATOM     13  CB  GLU A  35       8.952 -40.969  -7.447  1.00 82.22           C  
-ATOM     14  CG  GLU A  35       9.944 -39.814  -7.674  1.00 85.51           C  
-ATOM     15  CD  GLU A  35       9.304 -38.566  -8.350  1.00 88.82           C  
-ATOM     16  OE1 GLU A  35       8.499 -38.715  -9.312  1.00 88.93           O  
-ATOM     17  OE2 GLU A  35       9.632 -37.427  -7.923  1.00 88.92           O  
-ATOM     18  N   SER A  36       7.528 -43.830  -9.254  1.00 77.44           N  
-ATOM     19  CA  SER A  36       7.471 -45.275  -9.086  1.00 74.71           C  
-ATOM     20  C   SER A  36       8.861 -45.839  -9.500  1.00 72.05           C  
-ATOM     21  O   SER A  36       9.134 -47.036  -9.322  1.00 71.74           O  
-ATOM     22  CB  SER A  36       6.305 -45.888  -9.898  1.00 75.36           C  
-ATOM     23  OG  SER A  36       6.175 -45.291 -11.201  1.00 76.24           O  
-ATOM     24  N   GLN A  37       9.744 -44.961 -10.007  1.00 68.22           N  
-ATOM     25  CA  GLN A  37      11.112 -45.363 -10.388  1.00 64.70           C  
-ATOM     26  C   GLN A  37      12.053 -45.487  -9.202  1.00 61.12           C  
-ATOM     27  O   GLN A  37      13.144 -46.058  -9.349  1.00 60.46           O  
-ATOM     28  CB  GLN A  37      11.740 -44.397 -11.359  1.00 65.23           C  
-ATOM     29  CG  GLN A  37      10.796 -43.771 -12.337  1.00 67.99           C  
-ATOM     30  CD  GLN A  37      11.521 -42.776 -13.225  1.00 73.03           C  
-ATOM     31  OE1 GLN A  37      12.713 -42.968 -13.558  1.00 72.75           O  
-ATOM     32  NE2 GLN A  37      10.823 -41.693 -13.601  1.00 72.74           N  
-ATOM     33  N   TYR A  38      11.612 -44.988  -8.038  1.00 57.40           N  
-ATOM     34  CA  TYR A  38      12.410 -44.965  -6.810  1.00 54.24           C  
-ATOM     35  C   TYR A  38      11.716 -45.526  -5.596  1.00 53.47           C  
-ATOM     36  O   TYR A  38      10.604 -45.130  -5.296  1.00 53.03           O  
-ATOM     37  CB  TYR A  38      12.895 -43.527  -6.498  1.00 53.14           C  
-ATOM     38  CG  TYR A  38      13.722 -42.973  -7.614  1.00 49.32           C  
-ATOM     39  CD1 TYR A  38      15.036 -43.369  -7.779  1.00 48.19           C  
-ATOM     40  CD2 TYR A  38      13.185 -42.068  -8.512  1.00 48.26           C  
-ATOM     41  CE1 TYR A  38      15.793 -42.911  -8.852  1.00 48.46           C  
-ATOM     42  CE2 TYR A  38      13.939 -41.592  -9.592  1.00 48.12           C  
-ATOM     43  CZ  TYR A  38      15.227 -42.026  -9.751  1.00 47.94           C  
-ATOM     44  OH  TYR A  38      15.969 -41.535 -10.789  1.00 50.20           O  
-ATOM     45  N   GLN A  39      12.396 -46.413  -4.877  1.00 51.30           N  
-ATOM     46  CA  GLN A  39      11.944 -46.739  -3.562  1.00 51.65           C  
-ATOM     47  C   GLN A  39      12.509 -45.687  -2.555  1.00 50.48           C  
-ATOM     48  O   GLN A  39      13.736 -45.611  -2.362  1.00 50.32           O  
-ATOM     49  CB  GLN A  39      12.457 -48.106  -3.238  1.00 51.56           C  
-ATOM     50  CG  GLN A  39      11.844 -48.807  -2.095  1.00 58.61           C  
-ATOM     51  CD  GLN A  39      12.710 -50.025  -1.689  1.00 68.02           C  
-ATOM     52  OE1 GLN A  39      13.650 -49.899  -0.883  1.00 73.23           O  
-ATOM     53  NE2 GLN A  39      12.424 -51.197  -2.283  1.00 69.47           N  
-ATOM     54  N   VAL A  40      11.635 -44.916  -1.906  1.00 48.43           N  
-ATOM     55  CA  VAL A  40      12.026 -44.022  -0.832  1.00 45.82           C  
-ATOM     56  C   VAL A  40      12.453 -44.755   0.468  1.00 46.04           C  
-ATOM     57  O   VAL A  40      11.707 -45.597   0.998  1.00 44.89           O  
-ATOM     58  CB  VAL A  40      10.930 -43.012  -0.544  1.00 46.73           C  
-ATOM     59  CG1 VAL A  40      11.339 -42.041   0.548  1.00 45.57           C  
-ATOM     60  CG2 VAL A  40      10.646 -42.211  -1.771  1.00 45.82           C  
-ATOM     61  N   GLY A  41      13.634 -44.429   1.015  1.00 42.27           N  
-ATOM     62  CA  GLY A  41      14.066 -45.013   2.313  1.00 40.23           C  
-ATOM     63  C   GLY A  41      13.969 -43.912   3.361  1.00 38.17           C  
-ATOM     64  O   GLY A  41      13.176 -43.006   3.216  1.00 39.09           O  
-ATOM     65  N   PRO A  42      14.756 -43.988   4.434  1.00 37.65           N  
-ATOM     66  CA  PRO A  42      14.645 -43.047   5.571  1.00 38.13           C  
-ATOM     67  C   PRO A  42      15.018 -41.569   5.230  1.00 38.64           C  
-ATOM     68  O   PRO A  42      15.822 -41.311   4.296  1.00 37.19           O  
-ATOM     69  CB  PRO A  42      15.685 -43.556   6.551  1.00 38.55           C  
-ATOM     70  CG  PRO A  42      16.155 -44.857   6.078  1.00 39.95           C  
-ATOM     71  CD  PRO A  42      15.743 -45.057   4.659  1.00 38.97           C  
-ATOM     72  N   LEU A  43      14.408 -40.645   5.956  1.00 37.16           N  
-ATOM     73  CA  LEU A  43      14.760 -39.263   5.891  1.00 36.56           C  
-ATOM     74  C   LEU A  43      16.258 -39.157   6.287  1.00 38.01           C  
-ATOM     75  O   LEU A  43      16.628 -39.706   7.314  1.00 38.49           O  
-ATOM     76  CB  LEU A  43      13.900 -38.492   6.864  1.00 35.96           C  
-ATOM     77  CG  LEU A  43      14.065 -36.967   6.935  1.00 36.63           C  
-ATOM     78  CD1 LEU A  43      13.590 -36.305   5.658  1.00 36.69           C  
-ATOM     79  CD2 LEU A  43      13.269 -36.402   8.072  1.00 36.06           C  
-ATOM     80  N   LEU A  44      17.089 -38.444   5.511  1.00 35.66           N  
-ATOM     81  CA  LEU A  44      18.502 -38.199   5.891  1.00 34.35           C  
-ATOM     82  C   LEU A  44      18.681 -36.853   6.556  1.00 35.42           C  
-ATOM     83  O   LEU A  44      19.590 -36.688   7.329  1.00 36.50           O  
-ATOM     84  CB  LEU A  44      19.402 -38.278   4.648  1.00 34.68           C  
-ATOM     85  CG  LEU A  44      19.450 -39.666   3.999  1.00 35.01           C  
-ATOM     86  CD1 LEU A  44      20.154 -39.646   2.597  1.00 37.08           C  
-ATOM     87  CD2 LEU A  44      20.212 -40.646   4.890  1.00 35.43           C  
-ATOM     88  N   GLY A  45      17.858 -35.866   6.272  1.00 35.33           N  
-ATOM     89  CA  GLY A  45      18.041 -34.533   6.835  1.00 35.06           C  
-ATOM     90  C   GLY A  45      16.955 -33.610   6.321  1.00 36.25           C  
-ATOM     91  O   GLY A  45      16.307 -33.932   5.275  1.00 32.98           O  
-ATOM     92  N   SER A  46      16.743 -32.489   7.014  1.00 35.82           N  
-ATOM     93  CA  SER A  46      15.868 -31.463   6.497  1.00 39.50           C  
-ATOM     94  C   SER A  46      16.227 -30.064   7.026  1.00 39.81           C  
-ATOM     95  O   SER A  46      16.969 -29.952   7.986  1.00 39.77           O  
-ATOM     96  CB  SER A  46      14.432 -31.771   6.898  1.00 41.56           C  
-ATOM     97  OG  SER A  46      14.283 -31.596   8.285  1.00 45.24           O  
-ATOM     98  N   GLY A  47      15.649 -28.994   6.478  1.00 40.37           N  
-ATOM     99  CA  GLY A  47      16.050 -27.674   6.965  1.00 41.10           C  
-ATOM    100  C   GLY A  47      15.360 -26.580   6.231  1.00 42.93           C  
-ATOM    101  O   GLY A  47      14.287 -26.829   5.684  1.00 42.13           O  
-ATOM    102  N   GLY A  48      15.980 -25.383   6.168  1.00 42.41           N  
-ATOM    103  CA  GLY A  48      15.325 -24.290   5.443  1.00 43.42           C  
-ATOM    104  C   GLY A  48      14.998 -24.669   3.975  1.00 43.46           C  
-ATOM    105  O   GLY A  48      13.974 -24.244   3.417  1.00 44.50           O  
-ATOM    106  N   PHE A  49      15.868 -25.475   3.350  1.00 40.22           N  
-ATOM    107  CA  PHE A  49      15.738 -25.731   1.942  1.00 38.73           C  
-ATOM    108  C   PHE A  49      14.561 -26.666   1.609  1.00 37.94           C  
-ATOM    109  O   PHE A  49      14.027 -26.551   0.502  1.00 36.12           O  
-ATOM    110  CB  PHE A  49      16.989 -26.403   1.418  1.00 38.99           C  
-ATOM    111  CG  PHE A  49      17.157 -27.790   1.921  1.00 39.57           C  
-ATOM    112  CD1 PHE A  49      17.789 -28.012   3.144  1.00 33.86           C  
-ATOM    113  CD2 PHE A  49      16.640 -28.880   1.176  1.00 37.87           C  
-ATOM    114  CE1 PHE A  49      17.993 -29.327   3.627  1.00 39.80           C  
-ATOM    115  CE2 PHE A  49      16.814 -30.223   1.675  1.00 37.90           C  
-ATOM    116  CZ  PHE A  49      17.494 -30.425   2.882  1.00 38.08           C  
-ATOM    117  N   GLY A  50      14.245 -27.628   2.527  1.00 36.11           N  
-ATOM    118  CA  GLY A  50      13.285 -28.787   2.254  1.00 35.22           C  
-ATOM    119  C   GLY A  50      13.834 -30.028   3.007  1.00 33.94           C  
-ATOM    120  O   GLY A  50      14.359 -29.871   4.131  1.00 33.36           O  
-ATOM    121  N   SER A  51      13.813 -31.201   2.369  1.00 33.44           N  
-ATOM    122  CA  SER A  51      14.153 -32.515   3.010  1.00 32.38           C  
-ATOM    123  C   SER A  51      14.805 -33.453   2.061  1.00 31.16           C  
-ATOM    124  O   SER A  51      14.477 -33.426   0.871  1.00 32.99           O  
-ATOM    125  CB  SER A  51      12.793 -33.217   3.466  1.00 30.30           C  
-ATOM    126  OG  SER A  51      12.075 -32.353   4.342  1.00 31.61           O  
-ATOM    127  N   VAL A  52      15.646 -34.381   2.559  1.00 29.02           N  
-ATOM    128  CA  VAL A  52      16.279 -35.310   1.731  1.00 27.20           C  
-ATOM    129  C   VAL A  52      16.182 -36.668   2.319  1.00 29.34           C  
-ATOM    130  O   VAL A  52      16.292 -36.814   3.577  1.00 30.08           O  
-ATOM    131  CB  VAL A  52      17.848 -34.946   1.544  1.00 26.61           C  
-ATOM    132  CG1AVAL A  52      18.320 -35.380   0.158  0.50 27.91           C  
-ATOM    133  CG2AVAL A  52      18.005 -33.565   1.689  0.50 28.09           C  
-ATOM    134  CG1BVAL A  52      18.440 -34.489   2.889  0.50 22.94           C  
-ATOM    135  CG2BVAL A  52      18.635 -36.131   0.950  0.50 29.31           C  
-ATOM    136  N   TYR A  53      15.941 -37.637   1.423  1.00 29.85           N  
-ATOM    137  CA  TYR A  53      15.736 -39.073   1.740  1.00 30.76           C  
-ATOM    138  C   TYR A  53      16.729 -39.904   1.045  1.00 31.96           C  
-ATOM    139  O   TYR A  53      17.183 -39.565  -0.102  1.00 33.32           O  
-ATOM    140  CB  TYR A  53      14.392 -39.563   1.180  1.00 30.41           C  
-ATOM    141  CG  TYR A  53      13.201 -38.876   1.865  1.00 29.23           C  
-ATOM    142  CD1 TYR A  53      12.776 -37.609   1.465  1.00 30.63           C  
-ATOM    143  CD2 TYR A  53      12.530 -39.499   2.985  1.00 29.97           C  
-ATOM    144  CE1 TYR A  53      11.720 -36.968   2.102  1.00 29.06           C  
-ATOM    145  CE2 TYR A  53      11.408 -38.853   3.617  1.00 30.30           C  
-ATOM    146  CZ  TYR A  53      11.002 -37.620   3.162  1.00 31.70           C  
-ATOM    147  OH  TYR A  53       9.949 -36.904   3.794  1.00 31.69           O  
-ATOM    148  N   SER A  54      16.989 -41.044   1.657  1.00 29.38           N  
-ATOM    149  CA  SER A  54      17.736 -42.129   1.052  1.00 34.10           C  
-ATOM    150  C   SER A  54      16.759 -42.808   0.115  1.00 36.79           C  
-ATOM    151  O   SER A  54      15.541 -42.769   0.367  1.00 38.53           O  
-ATOM    152  CB  SER A  54      18.220 -43.080   2.136  1.00 32.31           C  
-ATOM    153  OG  SER A  54      18.977 -44.106   1.573  1.00 37.01           O  
-ATOM    154  N   GLY A  55      17.247 -43.335  -1.003  1.00 36.95           N  
-ATOM    155  CA  GLY A  55      16.376 -43.935  -1.956  1.00 38.44           C  
-ATOM    156  C   GLY A  55      17.169 -44.915  -2.753  1.00 40.12           C  
-ATOM    157  O   GLY A  55      18.402 -45.047  -2.592  1.00 36.85           O  
-ATOM    158  N   ILE A  56      16.464 -45.618  -3.624  1.00 40.93           N  
-ATOM    159  CA  ILE A  56      17.096 -46.655  -4.444  1.00 44.58           C  
-ATOM    160  C   ILE A  56      16.394 -46.597  -5.766  1.00 45.04           C  
-ATOM    161  O   ILE A  56      15.166 -46.536  -5.813  1.00 44.35           O  
-ATOM    162  CB  ILE A  56      16.935 -48.027  -3.821  1.00 44.47           C  
-ATOM    163  CG1 ILE A  56      17.941 -48.184  -2.681  1.00 47.46           C  
-ATOM    164  CG2 ILE A  56      17.111 -49.138  -4.866  1.00 47.78           C  
-ATOM    165  CD1 ILE A  56      17.788 -49.534  -1.854  1.00 47.80           C  
-ATOM    166  N   ARG A  57      17.165 -46.537  -6.838  1.00 45.68           N  
-ATOM    167  CA  ARG A  57      16.535 -46.506  -8.147  1.00 48.30           C  
-ATOM    168  C   ARG A  57      16.104 -47.934  -8.486  1.00 49.46           C  
-ATOM    169  O   ARG A  57      16.937 -48.870  -8.489  1.00 47.86           O  
-ATOM    170  CB  ARG A  57      17.489 -46.005  -9.172  1.00 48.05           C  
-ATOM    171  CG  ARG A  57      16.887 -45.882 -10.509  1.00 49.51           C  
-ATOM    172  CD  ARG A  57      18.076 -46.157 -11.457  1.00 56.12           C  
-ATOM    173  NE  ARG A  57      18.627 -44.910 -11.910  1.00 53.20           N  
-ATOM    174  CZ  ARG A  57      19.851 -44.709 -12.388  1.00 54.48           C  
-ATOM    175  NH1 ARG A  57      20.770 -45.669 -12.486  1.00 52.72           N  
-ATOM    176  NH2 ARG A  57      20.129 -43.489 -12.785  1.00 50.86           N  
-ATOM    177  N   VAL A  58      14.800 -48.061  -8.717  1.00 51.28           N  
-ATOM    178  CA  VAL A  58      14.085 -49.366  -8.807  1.00 54.00           C  
-ATOM    179  C   VAL A  58      14.662 -50.239  -9.927  1.00 55.45           C  
-ATOM    180  O   VAL A  58      15.016 -51.386  -9.694  1.00 56.42           O  
-ATOM    181  CB  VAL A  58      12.568 -49.112  -8.907  1.00 53.57           C  
-ATOM    182  CG1 VAL A  58      11.804 -50.283  -9.559  1.00 57.42           C  
-ATOM    183  CG2 VAL A  58      12.005 -48.784  -7.530  1.00 52.94           C  
-ATOM    184  N   SER A  59      14.850 -49.653 -11.107  1.00 57.12           N  
-ATOM    185  CA  SER A  59      15.355 -50.369 -12.278  1.00 57.82           C  
-ATOM    186  C   SER A  59      16.659 -51.084 -11.992  1.00 58.63           C  
-ATOM    187  O   SER A  59      16.704 -52.316 -12.037  1.00 59.28           O  
-ATOM    188  CB  SER A  59      15.519 -49.414 -13.454  1.00 58.71           C  
-ATOM    189  OG  SER A  59      16.546 -48.492 -13.172  1.00 58.93           O  
-ATOM    190  N   ASP A  60      17.718 -50.347 -11.649  1.00 57.80           N  
-ATOM    191  CA  ASP A  60      19.009 -51.009 -11.333  1.00 56.42           C  
-ATOM    192  C   ASP A  60      19.421 -51.150  -9.875  1.00 54.90           C  
-ATOM    193  O   ASP A  60      20.545 -51.567  -9.630  1.00 53.83           O  
-ATOM    194  CB  ASP A  60      20.176 -50.346 -12.074  1.00 56.39           C  
-ATOM    195  CG  ASP A  60      20.277 -48.857 -11.798  1.00 56.96           C  
-ATOM    196  OD1 ASP A  60      19.365 -48.282 -11.175  1.00 55.30           O  
-ATOM    197  OD2 ASP A  60      21.242 -48.229 -12.270  1.00 61.13           O  
-ATOM    198  N   ASN A  61      18.567 -50.805  -8.924  1.00 53.71           N  
-ATOM    199  CA  ASN A  61      19.016 -50.704  -7.508  1.00 53.91           C  
-ATOM    200  C   ASN A  61      20.141 -49.673  -7.148  1.00 51.20           C  
-ATOM    201  O   ASN A  61      20.836 -49.802  -6.138  1.00 50.71           O  
-ATOM    202  CB  ASN A  61      19.421 -52.055  -6.985  1.00 55.68           C  
-ATOM    203  CG  ASN A  61      18.226 -52.911  -6.738  1.00 61.89           C  
-ATOM    204  OD1 ASN A  61      17.206 -52.429  -6.237  1.00 66.14           O  
-ATOM    205  ND2 ASN A  61      18.305 -54.176  -7.166  1.00 67.16           N  
-ATOM    206  N   LEU A  62      20.335 -48.679  -7.982  1.00 47.38           N  
-ATOM    207  CA  LEU A  62      21.403 -47.726  -7.725  1.00 44.37           C  
-ATOM    208  C   LEU A  62      21.057 -46.971  -6.465  1.00 41.59           C  
-ATOM    209  O   LEU A  62      19.969 -46.422  -6.380  1.00 39.80           O  
-ATOM    210  CB  LEU A  62      21.456 -46.725  -8.867  1.00 45.16           C  
-ATOM    211  CG  LEU A  62      22.568 -45.702  -8.656  1.00 42.02           C  
-ATOM    212  CD1 LEU A  62      23.993 -46.420  -8.708  1.00 45.42           C  
-ATOM    213  CD2 LEU A  62      22.448 -44.504  -9.608  1.00 41.34           C  
-ATOM    214  N   PRO A  63      21.982 -46.892  -5.493  1.00 39.37           N  
-ATOM    215  CA  PRO A  63      21.674 -45.934  -4.374  1.00 38.76           C  
-ATOM    216  C   PRO A  63      21.599 -44.431  -4.801  1.00 39.28           C  
-ATOM    217  O   PRO A  63      22.474 -43.918  -5.550  1.00 39.77           O  
-ATOM    218  CB  PRO A  63      22.776 -46.173  -3.367  1.00 37.35           C  
-ATOM    219  CG  PRO A  63      23.827 -47.034  -4.079  1.00 39.72           C  
-ATOM    220  CD  PRO A  63      23.269 -47.579  -5.350  1.00 39.66           C  
-ATOM    221  N   VAL A  64      20.566 -43.735  -4.353  1.00 36.35           N  
-ATOM    222  CA  VAL A  64      20.389 -42.300  -4.665  1.00 34.56           C  
-ATOM    223  C   VAL A  64      19.944 -41.510  -3.427  1.00 34.33           C  
-ATOM    224  O   VAL A  64      19.553 -42.096  -2.365  1.00 35.69           O  
-ATOM    225  CB  VAL A  64      19.326 -42.065  -5.788  1.00 34.58           C  
-ATOM    226  CG1 VAL A  64      19.752 -42.791  -7.140  1.00 35.49           C  
-ATOM    227  CG2 VAL A  64      17.928 -42.545  -5.323  1.00 35.41           C  
-ATOM    228  N   ALA A  65      19.895 -40.197  -3.549  1.00 31.92           N  
-ATOM    229  CA  ALA A  65      19.362 -39.398  -2.451  1.00 32.34           C  
-ATOM    230  C   ALA A  65      18.289 -38.634  -3.170  1.00 31.15           C  
-ATOM    231  O   ALA A  65      18.481 -38.285  -4.321  1.00 30.96           O  
-ATOM    232  CB  ALA A  65      20.418 -38.397  -1.854  1.00 30.70           C  
-ATOM    233  N   ILE A  66      17.207 -38.309  -2.497  1.00 30.17           N  
-ATOM    234  CA  ILE A  66      16.084 -37.703  -3.135  1.00 30.95           C  
-ATOM    235  C   ILE A  66      15.813 -36.457  -2.402  1.00 30.11           C  
-ATOM    236  O   ILE A  66      15.404 -36.502  -1.218  1.00 32.75           O  
-ATOM    237  CB  ILE A  66      14.867 -38.648  -3.073  1.00 31.43           C  
-ATOM    238  CG1 ILE A  66      15.197 -39.934  -3.799  1.00 32.64           C  
-ATOM    239  CG2 ILE A  66      13.596 -37.871  -3.657  1.00 28.22           C  
-ATOM    240  CD1 ILE A  66      14.215 -41.138  -3.626  1.00 33.21           C  
-ATOM    241  N   LYS A  67      16.123 -35.327  -3.029  1.00 28.89           N  
-ATOM    242  CA  LYS A  67      16.028 -34.045  -2.354  1.00 30.15           C  
-ATOM    243  C   LYS A  67      14.842 -33.242  -2.836  1.00 32.03           C  
-ATOM    244  O   LYS A  67      14.723 -32.899  -4.062  1.00 33.17           O  
-ATOM    245  CB  LYS A  67      17.322 -33.234  -2.603  1.00 29.65           C  
-ATOM    246  CG  LYS A  67      17.238 -31.846  -2.025  1.00 29.26           C  
-ATOM    247  CD  LYS A  67      18.672 -31.147  -2.278  1.00 30.54           C  
-ATOM    248  CE  LYS A  67      18.918 -29.968  -1.322  1.00 33.75           C  
-ATOM    249  NZ  LYS A  67      20.147 -29.237  -1.840  1.00 29.98           N  
-ATOM    250  N   HIS A  68      13.997 -32.863  -1.881  1.00 31.75           N  
-ATOM    251  CA  HIS A  68      12.794 -32.067  -2.111  1.00 32.95           C  
-ATOM    252  C   HIS A  68      13.038 -30.649  -1.769  1.00 33.91           C  
-ATOM    253  O   HIS A  68      13.326 -30.353  -0.620  1.00 31.81           O  
-ATOM    254  CB  HIS A  68      11.654 -32.545  -1.215  1.00 32.12           C  
-ATOM    255  CG  HIS A  68      11.292 -33.948  -1.448  1.00 31.13           C  
-ATOM    256  ND1 HIS A  68      10.168 -34.311  -2.153  1.00 33.22           N  
-ATOM    257  CD2 HIS A  68      11.918 -35.105  -1.105  1.00 31.70           C  
-ATOM    258  CE1 HIS A  68      10.127 -35.629  -2.264  1.00 27.32           C  
-ATOM    259  NE2 HIS A  68      11.190 -36.130  -1.646  1.00 28.18           N  
-ATOM    260  N   VAL A  69      12.904 -29.765  -2.756  1.00 33.96           N  
-ATOM    261  CA  VAL A  69      13.271 -28.344  -2.609  1.00 38.00           C  
-ATOM    262  C   VAL A  69      11.930 -27.599  -2.698  1.00 40.98           C  
-ATOM    263  O   VAL A  69      11.242 -27.706  -3.728  1.00 41.22           O  
-ATOM    264  CB  VAL A  69      14.195 -27.891  -3.765  1.00 38.59           C  
-ATOM    265  CG1 VAL A  69      14.417 -26.355  -3.699  1.00 42.08           C  
-ATOM    266  CG2 VAL A  69      15.579 -28.687  -3.723  1.00 40.03           C  
-ATOM    267  N   GLU A  70      11.562 -26.918  -1.621  1.00 42.96           N  
-ATOM    268  CA  GLU A  70      10.318 -26.163  -1.545  1.00 46.58           C  
-ATOM    269  C   GLU A  70      10.477 -24.876  -2.344  1.00 45.09           C  
-ATOM    270  O   GLU A  70      11.451 -24.102  -2.159  1.00 44.48           O  
-ATOM    271  CB  GLU A  70       9.964 -25.845  -0.080  1.00 46.91           C  
-ATOM    272  CG  GLU A  70       9.228 -27.003   0.566  1.00 56.07           C  
-ATOM    273  CD  GLU A  70       7.717 -27.050   0.226  1.00 62.43           C  
-ATOM    274  OE1 GLU A  70       7.046 -25.987   0.420  1.00 68.33           O  
-ATOM    275  OE2 GLU A  70       7.194 -28.143  -0.192  1.00 62.54           O  
-ATOM    276  N   LYS A  71       9.559 -24.685  -3.266  1.00 45.67           N  
-ATOM    277  CA  LYS A  71       9.538 -23.407  -4.102  1.00 47.07           C  
-ATOM    278  C   LYS A  71       9.720 -22.082  -3.361  1.00 49.59           C  
-ATOM    279  O   LYS A  71      10.584 -21.280  -3.753  1.00 48.65           O  
-ATOM    280  CB  LYS A  71       8.323 -23.363  -4.986  1.00 46.04           C  
-ATOM    281  CG  LYS A  71       8.362 -24.515  -5.949  1.00 41.47           C  
-ATOM    282  CD  LYS A  71       7.339 -24.393  -7.065  1.00 39.26           C  
-ATOM    283  CE  LYS A  71       7.671 -25.367  -8.153  1.00 43.96           C  
-ATOM    284  NZ  LYS A  71       6.483 -25.813  -9.005  1.00 44.67           N  
-ATOM    285  N   ASP A  72       8.996 -21.888  -2.242  1.00 51.86           N  
-ATOM    286  CA  ASP A  72       8.934 -20.586  -1.629  1.00 55.13           C  
-ATOM    287  C   ASP A  72      10.189 -20.311  -0.911  1.00 56.35           C  
-ATOM    288  O   ASP A  72      10.335 -19.224  -0.362  1.00 55.99           O  
-ATOM    289  CB  ASP A  72       7.885 -20.535  -0.570  1.00 57.42           C  
-ATOM    290  CG  ASP A  72       6.749 -21.426  -0.871  1.00 65.65           C  
-ATOM    291  OD1 ASP A  72       6.941 -22.310  -1.761  1.00 72.25           O  
-ATOM    292  OD2 ASP A  72       5.677 -21.249  -0.206  1.00 72.56           O  
-ATOM    293  N   ARG A  73      11.064 -21.302  -0.814  1.00 56.95           N  
-ATOM    294  C   ARG A  73      13.477 -20.960  -1.115  1.00 58.13           C  
-ATOM    295  O   ARG A  73      14.630 -20.711  -0.722  1.00 58.54           O  
-ATOM    296  CA AARG A  73      12.327 -21.102  -0.114  0.50 58.30           C  
-ATOM    297  CB AARG A  73      12.584 -22.215   0.930  0.50 58.35           C  
-ATOM    298  CG AARG A  73      11.767 -22.088   2.233  0.50 60.52           C  
-ATOM    299  CD AARG A  73      10.604 -23.081   2.340  0.50 62.69           C  
-ATOM    300  NE AARG A  73      10.983 -24.265   3.121  0.50 65.56           N  
-ATOM    301  CZ AARG A  73      10.215 -25.345   3.275  0.50 66.70           C  
-ATOM    302  NH1AARG A  73       9.017 -25.378   2.707  0.50 65.76           N  
-ATOM    303  NH2AARG A  73      10.634 -26.392   3.992  0.50 65.70           N  
-ATOM    304  CA BARG A  73      12.324 -21.071  -0.127  0.50 57.95           C  
-ATOM    305  CB BARG A  73      12.561 -22.131   0.964  0.50 57.73           C  
-ATOM    306  CG BARG A  73      11.541 -22.057   2.111  0.50 58.46           C  
-ATOM    307  CD BARG A  73      11.607 -20.681   2.810  0.50 57.96           C  
-ATOM    308  NE BARG A  73      12.904 -20.517   3.439  0.50 55.90           N  
-ATOM    309  CZ BARG A  73      13.127 -20.728   4.725  0.50 55.37           C  
-ATOM    310  NH1BARG A  73      12.116 -21.065   5.518  0.50 55.94           N  
-ATOM    311  NH2BARG A  73      14.350 -20.578   5.213  0.50 52.65           N  
-ATOM    312  N   ILE A  74      13.160 -21.093  -2.403  1.00 58.28           N  
-ATOM    313  CA  ILE A  74      14.189 -20.975  -3.424  1.00 59.10           C  
-ATOM    314  C   ILE A  74      14.741 -19.534  -3.490  1.00 60.60           C  
-ATOM    315  O   ILE A  74      14.068 -18.630  -4.016  1.00 61.40           O  
-ATOM    316  CB  ILE A  74      13.680 -21.477  -4.787  1.00 58.93           C  
-ATOM    317  CG1 ILE A  74      13.384 -22.973  -4.709  1.00 56.78           C  
-ATOM    318  CG2 ILE A  74      14.699 -21.199  -5.898  1.00 57.75           C  
-ATOM    319  CD1 ILE A  74      12.895 -23.538  -5.970  1.00 55.76           C  
-ATOM    320  N   SER A  75      15.958 -19.313  -2.972  1.00 61.31           N  
-ATOM    321  CA  SER A  75      16.533 -17.933  -3.006  1.00 62.40           C  
-ATOM    322  C   SER A  75      16.859 -17.371  -4.419  1.00 62.87           C  
-ATOM    323  O   SER A  75      16.985 -16.146  -4.544  1.00 63.55           O  
-ATOM    324  CB  SER A  75      17.720 -17.724  -2.024  1.00 62.46           C  
-ATOM    325  OG  SER A  75      18.748 -18.729  -2.153  1.00 65.00           O  
-ATOM    326  N   ASP A  76      17.010 -18.256  -5.443  1.00 62.72           N  
-ATOM    327  CA  ASP A  76      17.332 -17.920  -6.855  1.00 60.72           C  
-ATOM    328  C   ASP A  76      16.842 -18.916  -7.914  1.00 58.95           C  
-ATOM    329  O   ASP A  76      16.990 -20.140  -7.790  1.00 56.34           O  
-ATOM    330  CB  ASP A  76      18.847 -17.757  -7.030  1.00 61.56           C  
-ATOM    331  CG  ASP A  76      19.405 -16.587  -6.219  1.00 66.63           C  
-ATOM    332  OD1 ASP A  76      18.780 -15.480  -6.263  1.00 69.46           O  
-ATOM    333  OD2 ASP A  76      20.464 -16.760  -5.521  1.00 68.92           O  
-ATOM    334  N   TRP A  77      16.312 -18.373  -8.996  1.00 56.97           N  
-ATOM    335  CA  TRP A  77      15.851 -19.187 -10.079  1.00 57.12           C  
-ATOM    336  C   TRP A  77      16.713 -18.939 -11.275  1.00 58.41           C  
-ATOM    337  O   TRP A  77      17.365 -17.904 -11.367  1.00 58.48           O  
-ATOM    338  CB  TRP A  77      14.418 -18.829 -10.448  1.00 55.41           C  
-ATOM    339  CG  TRP A  77      13.416 -19.104  -9.413  1.00 53.69           C  
-ATOM    340  CD1 TRP A  77      13.153 -18.359  -8.279  1.00 54.03           C  
-ATOM    341  CD2 TRP A  77      12.508 -20.213  -9.388  1.00 51.26           C  
-ATOM    342  NE1 TRP A  77      12.131 -18.962  -7.556  1.00 51.94           N  
-ATOM    343  CE2 TRP A  77      11.714 -20.084  -8.227  1.00 51.05           C  
-ATOM    344  CE3 TRP A  77      12.306 -21.316 -10.225  1.00 52.93           C  
-ATOM    345  CZ2 TRP A  77      10.704 -21.003  -7.905  1.00 52.07           C  
-ATOM    346  CZ3 TRP A  77      11.306 -22.240  -9.900  1.00 53.57           C  
-ATOM    347  CH2 TRP A  77      10.515 -22.070  -8.754  1.00 52.64           C  
-ATOM    348  N   GLY A  78      16.704 -19.885 -12.198  1.00 59.62           N  
-ATOM    349  CA  GLY A  78      17.488 -19.794 -13.397  1.00 62.41           C  
-ATOM    350  C   GLY A  78      16.674 -20.476 -14.433  1.00 65.42           C  
-ATOM    351  O   GLY A  78      15.483 -20.745 -14.218  1.00 65.93           O  
-ATOM    352  N   GLU A  79      17.265 -20.738 -15.585  1.00 69.01           N  
-ATOM    353  CA  GLU A  79      16.534 -21.528 -16.564  1.00 73.31           C  
-ATOM    354  C   GLU A  79      17.461 -22.277 -17.464  1.00 74.89           C  
-ATOM    355  O   GLU A  79      18.652 -21.980 -17.523  1.00 75.38           O  
-ATOM    356  CB  GLU A  79      15.535 -20.712 -17.366  1.00 73.98           C  
-ATOM    357  CG  GLU A  79      16.168 -19.846 -18.415  1.00 79.11           C  
-ATOM    358  CD  GLU A  79      15.213 -18.755 -18.854  1.00 85.37           C  
-ATOM    359  OE1 GLU A  79      13.975 -19.026 -18.920  1.00 84.99           O  
-ATOM    360  OE2 GLU A  79      15.714 -17.627 -19.113  1.00 88.07           O  
-ATOM    361  N   LEU A  80      16.895 -23.254 -18.160  1.00 77.51           N  
-ATOM    362  CA  LEU A  80      17.683 -24.313 -18.777  1.00 79.71           C  
-ATOM    363  C   LEU A  80      18.185 -23.904 -20.171  1.00 82.03           C  
-ATOM    364  O   LEU A  80      17.621 -22.947 -20.754  1.00 81.79           O  
-ATOM    365  CB  LEU A  80      16.847 -25.599 -18.809  1.00 79.36           C  
-ATOM    366  CG  LEU A  80      16.570 -26.134 -17.404  1.00 77.58           C  
-ATOM    367  CD1 LEU A  80      15.703 -27.367 -17.484  1.00 76.56           C  
-ATOM    368  CD2 LEU A  80      17.915 -26.423 -16.719  1.00 75.88           C  
-ATOM    369  N   PRO A  81      19.261 -24.588 -20.691  1.00 83.82           N  
-ATOM    370  CA  PRO A  81      19.612 -24.333 -22.116  1.00 84.88           C  
-ATOM    371  C   PRO A  81      18.350 -24.222 -23.022  1.00 85.24           C  
-ATOM    372  O   PRO A  81      18.133 -23.144 -23.586  1.00 86.01           O  
-ATOM    373  CB  PRO A  81      20.572 -25.491 -22.474  1.00 85.06           C  
-ATOM    374  CG  PRO A  81      21.319 -25.766 -21.124  1.00 85.04           C  
-ATOM    375  CD  PRO A  81      20.202 -25.557 -20.056  1.00 84.44           C  
-ATOM    376  N   ASN A  82      17.498 -25.253 -23.118  1.00 85.03           N  
-ATOM    377  CA  ASN A  82      16.175 -25.021 -23.739  1.00 84.83           C  
-ATOM    378  C   ASN A  82      15.501 -23.770 -23.119  1.00 83.63           C  
-ATOM    379  O   ASN A  82      15.140 -22.838 -23.832  1.00 83.61           O  
-ATOM    380  CB  ASN A  82      15.260 -26.276 -23.750  1.00 85.22           C  
-ATOM    381  CG  ASN A  82      14.844 -26.740 -22.333  1.00 87.09           C  
-ATOM    382  OD1 ASN A  82      15.688 -27.149 -21.518  1.00 86.95           O  
-ATOM    383  ND2 ASN A  82      13.537 -26.699 -22.053  1.00 87.09           N  
-ATOM    384  N   GLY A  83      15.399 -23.722 -21.797  1.00 82.64           N  
-ATOM    385  CA  GLY A  83      14.890 -22.531 -21.137  1.00 81.23           C  
-ATOM    386  C   GLY A  83      13.640 -22.738 -20.300  1.00 80.48           C  
-ATOM    387  O   GLY A  83      12.721 -21.903 -20.357  1.00 80.38           O  
-ATOM    388  N   THR A  84      13.612 -23.837 -19.524  1.00 78.59           N  
-ATOM    389  CA  THR A  84      12.557 -24.101 -18.497  1.00 76.59           C  
-ATOM    390  C   THR A  84      12.872 -23.425 -17.127  1.00 73.93           C  
-ATOM    391  O   THR A  84      14.029 -23.425 -16.675  1.00 74.25           O  
-ATOM    392  CB  THR A  84      12.383 -25.617 -18.254  1.00 76.83           C  
-ATOM    393  OG1 THR A  84      12.442 -26.299 -19.513  1.00 79.30           O  
-ATOM    394  CG2 THR A  84      11.064 -25.929 -17.512  1.00 76.30           C  
-ATOM    395  N   ARG A  85      11.859 -22.882 -16.458  1.00 69.93           N  
-ATOM    396  CA  ARG A  85      12.121 -22.218 -15.181  1.00 65.59           C  
-ATOM    397  C   ARG A  85      12.360 -23.194 -13.951  1.00 64.57           C  
-ATOM    398  O   ARG A  85      11.409 -23.793 -13.396  1.00 64.55           O  
-ATOM    399  CB  ARG A  85      11.074 -21.133 -14.944  1.00 66.97           C  
-ATOM    400  CG  ARG A  85      11.047 -20.534 -13.578  1.00 68.60           C  
-ATOM    401  CD  ARG A  85       9.819 -19.645 -13.491  1.00 73.68           C  
-ATOM    402  NE  ARG A  85       9.637 -19.086 -12.154  1.00 74.44           N  
-ATOM    403  CZ  ARG A  85      10.377 -18.103 -11.650  1.00 76.37           C  
-ATOM    404  NH1 ARG A  85      11.376 -17.584 -12.366  1.00 76.23           N  
-ATOM    405  NH2 ARG A  85      10.124 -17.650 -10.419  1.00 76.43           N  
-ATOM    406  N   VAL A  86      13.641 -23.347 -13.576  1.00 60.44           N  
-ATOM    407  CA  VAL A  86      14.116 -24.297 -12.542  1.00 57.31           C  
-ATOM    408  C   VAL A  86      14.882 -23.578 -11.397  1.00 51.99           C  
-ATOM    409  O   VAL A  86      15.358 -22.450 -11.569  1.00 51.59           O  
-ATOM    410  CB  VAL A  86      15.037 -25.328 -13.183  1.00 57.19           C  
-ATOM    411  CG1 VAL A  86      14.287 -26.086 -14.290  1.00 57.21           C  
-ATOM    412  CG2 VAL A  86      16.262 -24.630 -13.782  1.00 57.46           C  
-ATOM    413  N   PRO A  87      14.974 -24.206 -10.202  1.00 46.53           N  
-ATOM    414  CA  PRO A  87      15.902 -23.622  -9.254  1.00 44.26           C  
-ATOM    415  C   PRO A  87      17.313 -23.439  -9.869  1.00 40.15           C  
-ATOM    416  O   PRO A  87      17.808 -24.288 -10.638  1.00 40.09           O  
-ATOM    417  CB  PRO A  87      15.902 -24.620  -8.073  1.00 43.08           C  
-ATOM    418  CG  PRO A  87      14.689 -25.398  -8.216  1.00 44.06           C  
-ATOM    419  CD  PRO A  87      14.284 -25.376  -9.661  1.00 46.08           C  
-ATOM    420  N   MET A  88      17.945 -22.340  -9.522  1.00 38.64           N  
-ATOM    421  CA  MET A  88      19.369 -22.149  -9.863  1.00 36.71           C  
-ATOM    422  C   MET A  88      20.183 -23.402  -9.475  1.00 35.87           C  
-ATOM    423  O   MET A  88      21.099 -23.855 -10.186  1.00 35.36           O  
-ATOM    424  CB  MET A  88      19.877 -20.876  -9.178  1.00 37.76           C  
-ATOM    425  CG  MET A  88      21.345 -20.565  -9.451  1.00 42.40           C  
-ATOM    426  SD  MET A  88      21.681 -20.294 -11.237  1.00 52.99           S  
-ATOM    427  CE  MET A  88      20.390 -19.090 -11.606  1.00 46.76           C  
-ATOM    428  N   GLU A  89      19.866 -23.989  -8.344  1.00 34.65           N  
-ATOM    429  CA  GLU A  89      20.564 -25.191  -7.907  1.00 34.88           C  
-ATOM    430  C   GLU A  89      20.648 -26.239  -9.036  1.00 34.80           C  
-ATOM    431  O   GLU A  89      21.654 -26.926  -9.222  1.00 34.56           O  
-ATOM    432  CB  GLU A  89      19.721 -25.771  -6.735  1.00 35.76           C  
-ATOM    433  CG  GLU A  89      20.274 -26.982  -6.168  1.00 35.10           C  
-ATOM    434  CD  GLU A  89      19.651 -27.420  -4.828  1.00 33.27           C  
-ATOM    435  OE1 GLU A  89      18.740 -26.779  -4.249  1.00 35.93           O  
-ATOM    436  OE2 GLU A  89      20.107 -28.484  -4.338  1.00 35.19           O  
-ATOM    437  N   VAL A  90      19.529 -26.443  -9.760  1.00 34.01           N  
-ATOM    438  CA  VAL A  90      19.546 -27.376 -10.929  1.00 32.69           C  
-ATOM    439  C   VAL A  90      20.427 -26.871 -12.069  1.00 31.01           C  
-ATOM    440  O   VAL A  90      21.226 -27.623 -12.622  1.00 31.61           O  
-ATOM    441  CB  VAL A  90      18.089 -27.588 -11.430  1.00 34.57           C  
-ATOM    442  CG1 VAL A  90      18.064 -28.340 -12.777  1.00 34.42           C  
-ATOM    443  CG2 VAL A  90      17.316 -28.263 -10.336  1.00 33.20           C  
-ATOM    444  N   VAL A  91      20.398 -25.574 -12.342  1.00 30.82           N  
-ATOM    445  CA  VAL A  91      21.283 -25.080 -13.372  1.00 32.12           C  
-ATOM    446  C   VAL A  91      22.744 -25.347 -12.971  1.00 32.86           C  
-ATOM    447  O   VAL A  91      23.563 -25.797 -13.783  1.00 30.50           O  
-ATOM    448  CB  VAL A  91      21.073 -23.531 -13.539  1.00 34.16           C  
-ATOM    449  CG1 VAL A  91      22.176 -23.001 -14.394  1.00 33.76           C  
-ATOM    450  CG2 VAL A  91      19.697 -23.298 -14.240  1.00 35.36           C  
-ATOM    451  N   LEU A  92      23.071 -25.065 -11.675  1.00 31.09           N  
-ATOM    452  CA  LEU A  92      24.457 -25.185 -11.236  1.00 30.77           C  
-ATOM    453  C   LEU A  92      24.887 -26.632 -11.252  1.00 29.57           C  
-ATOM    454  O   LEU A  92      25.952 -26.931 -11.690  1.00 28.10           O  
-ATOM    455  CB  LEU A  92      24.664 -24.545  -9.831  1.00 30.81           C  
-ATOM    456  CG  LEU A  92      24.182 -23.115  -9.799  1.00 27.34           C  
-ATOM    457  CD1 LEU A  92      24.240 -22.599  -8.369  1.00 29.78           C  
-ATOM    458  CD2 LEU A  92      24.907 -22.207 -10.826  1.00 29.69           C  
-ATOM    459  N   LEU A  93      24.041 -27.547 -10.786  1.00 29.86           N  
-ATOM    460  CA  LEU A  93      24.392 -28.940 -10.770  1.00 30.72           C  
-ATOM    461  C   LEU A  93      24.657 -29.447 -12.197  1.00 31.22           C  
-ATOM    462  O   LEU A  93      25.578 -30.259 -12.410  1.00 30.78           O  
-ATOM    463  CB  LEU A  93      23.272 -29.768 -10.127  1.00 29.80           C  
-ATOM    464  CG  LEU A  93      23.262 -29.758  -8.577  1.00 30.57           C  
-ATOM    465  CD1 LEU A  93      21.877 -30.133  -8.013  1.00 30.01           C  
-ATOM    466  CD2 LEU A  93      24.281 -30.688  -8.063  1.00 27.90           C  
-ATOM    467  N   LYS A  94      23.875 -28.982 -13.170  1.00 33.09           N  
-ATOM    468  CA  LYS A  94      24.087 -29.417 -14.583  1.00 33.30           C  
-ATOM    469  C   LYS A  94      25.403 -28.902 -15.087  1.00 34.02           C  
-ATOM    470  O   LYS A  94      26.169 -29.662 -15.690  1.00 33.23           O  
-ATOM    471  CB  LYS A  94      22.977 -28.944 -15.497  1.00 35.91           C  
-ATOM    472  CG  LYS A  94      21.644 -29.721 -15.216  1.00 38.15           C  
-ATOM    473  CD  LYS A  94      20.468 -29.051 -15.976  1.00 46.08           C  
-ATOM    474  CE  LYS A  94      20.193 -29.856 -17.271  1.00 54.15           C  
-ATOM    475  NZ  LYS A  94      19.287 -31.070 -17.002  1.00 56.43           N  
-ATOM    476  N   LYS A  95      25.737 -27.652 -14.747  1.00 33.45           N  
-ATOM    477  CA  LYS A  95      27.067 -27.109 -15.206  1.00 33.29           C  
-ATOM    478  C   LYS A  95      28.223 -27.935 -14.663  1.00 31.99           C  
-ATOM    479  O   LYS A  95      29.206 -28.095 -15.344  1.00 33.94           O  
-ATOM    480  CB  LYS A  95      27.211 -25.642 -14.837  1.00 34.42           C  
-ATOM    481  CG  LYS A  95      26.259 -24.729 -15.709  1.00 37.46           C  
-ATOM    482  CD  LYS A  95      26.300 -23.244 -15.247  1.00 36.38           C  
-ATOM    483  CE  LYS A  95      27.647 -22.597 -15.417  1.00 39.74           C  
-ATOM    484  NZ  LYS A  95      28.069 -22.383 -16.851  1.00 39.74           N  
-ATOM    485  N   VAL A  96      28.115 -28.434 -13.440  1.00 32.66           N  
-ATOM    486  CA  VAL A  96      29.267 -29.139 -12.855  1.00 35.38           C  
-ATOM    487  C   VAL A  96      29.256 -30.654 -13.056  1.00 37.41           C  
-ATOM    488  O   VAL A  96      30.244 -31.356 -12.671  1.00 36.73           O  
-ATOM    489  CB  VAL A  96      29.475 -28.855 -11.339  1.00 35.07           C  
-ATOM    490  CG1 VAL A  96      29.763 -27.351 -11.095  1.00 34.70           C  
-ATOM    491  CG2 VAL A  96      28.253 -29.292 -10.567  1.00 29.57           C  
-ATOM    492  N   SER A  97      28.140 -31.167 -13.590  1.00 40.65           N  
-ATOM    493  CA  SER A  97      28.044 -32.628 -13.876  1.00 42.06           C  
-ATOM    494  C   SER A  97      29.188 -33.129 -14.757  1.00 42.74           C  
-ATOM    495  O   SER A  97      29.508 -32.567 -15.807  1.00 43.09           O  
-ATOM    496  CB  SER A  97      26.759 -32.995 -14.550  1.00 42.44           C  
-ATOM    497  OG  SER A  97      26.880 -34.410 -14.729  1.00 50.01           O  
-ATOM    498  N   SER A  98      29.880 -34.154 -14.291  1.00 44.12           N  
-ATOM    499  CA  SER A  98      30.944 -34.761 -15.120  1.00 44.70           C  
-ATOM    500  C   SER A  98      31.312 -36.084 -14.416  1.00 44.35           C  
-ATOM    501  O   SER A  98      30.722 -36.407 -13.366  1.00 44.19           O  
-ATOM    502  CB  SER A  98      32.164 -33.862 -15.197  1.00 45.66           C  
-ATOM    503  OG  SER A  98      32.942 -34.022 -14.000  1.00 46.64           O  
-ATOM    504  N   GLY A  99      32.288 -36.813 -14.957  1.00 43.76           N  
-ATOM    505  CA  GLY A  99      32.765 -38.072 -14.323  1.00 43.99           C  
-ATOM    506  C   GLY A  99      33.727 -37.793 -13.154  1.00 43.81           C  
-ATOM    507  O   GLY A  99      34.189 -38.726 -12.473  1.00 43.25           O  
-ATOM    508  N   PHE A 100      34.013 -36.499 -12.919  1.00 41.24           N  
-ATOM    509  CA  PHE A 100      34.806 -36.111 -11.768  1.00 39.64           C  
-ATOM    510  C   PHE A 100      34.046 -36.393 -10.482  1.00 39.71           C  
-ATOM    511  O   PHE A 100      33.023 -35.817 -10.259  1.00 41.56           O  
-ATOM    512  CB  PHE A 100      35.204 -34.632 -11.817  1.00 37.11           C  
-ATOM    513  CG  PHE A 100      35.965 -34.164 -10.528  1.00 36.37           C  
-ATOM    514  CD1 PHE A 100      37.135 -34.866 -10.076  1.00 31.89           C  
-ATOM    515  CD2 PHE A 100      35.545 -33.040  -9.788  1.00 36.41           C  
-ATOM    516  CE1 PHE A 100      37.877 -34.384  -8.967  1.00 32.72           C  
-ATOM    517  CE2 PHE A 100      36.294 -32.558  -8.594  1.00 32.24           C  
-ATOM    518  CZ  PHE A 100      37.436 -33.185  -8.221  1.00 31.70           C  
-ATOM    519  N   SER A 101      34.563 -37.277  -9.622  1.00 39.42           N  
-ATOM    520  CA  SER A 101      33.786 -37.710  -8.492  1.00 39.43           C  
-ATOM    521  C   SER A 101      33.780 -36.718  -7.313  1.00 38.44           C  
-ATOM    522  O   SER A 101      33.114 -37.031  -6.225  1.00 38.01           O  
-ATOM    523  CB  SER A 101      34.263 -39.087  -8.022  1.00 41.29           C  
-ATOM    524  OG  SER A 101      35.603 -39.017  -7.557  1.00 39.35           O  
-ATOM    525  N   GLY A 102      34.488 -35.553  -7.477  1.00 35.81           N  
-ATOM    526  CA  GLY A 102      34.630 -34.634  -6.317  1.00 29.65           C  
-ATOM    527  C   GLY A 102      33.437 -33.722  -6.088  1.00 28.48           C  
-ATOM    528  O   GLY A 102      33.336 -32.995  -5.065  1.00 26.79           O  
-ATOM    529  N   VAL A 103      32.544 -33.672  -7.074  1.00 27.81           N  
-ATOM    530  CA  VAL A 103      31.322 -32.902  -6.939  1.00 27.83           C  
-ATOM    531  C   VAL A 103      30.144 -33.896  -7.167  1.00 29.36           C  
-ATOM    532  O   VAL A 103      30.258 -34.769  -8.070  1.00 32.11           O  
-ATOM    533  CB  VAL A 103      31.216 -31.742  -7.914  1.00 30.07           C  
-ATOM    534  CG1 VAL A 103      29.837 -31.108  -7.778  1.00 27.44           C  
-ATOM    535  CG2 VAL A 103      32.337 -30.691  -7.583  1.00 26.10           C  
-ATOM    536  N   ILE A 104      29.088 -33.797  -6.356  1.00 26.75           N  
-ATOM    537  CA  ILE A 104      27.939 -34.738  -6.460  1.00 30.84           C  
-ATOM    538  C   ILE A 104      27.311 -34.642  -7.850  1.00 30.69           C  
-ATOM    539  O   ILE A 104      27.323 -33.535  -8.495  1.00 31.18           O  
-ATOM    540  CB  ILE A 104      26.768 -34.508  -5.454  1.00 27.33           C  
-ATOM    541  CG1AILE A 104      25.951 -35.800  -5.197  0.50 25.24           C  
-ATOM    542  CG2AILE A 104      25.918 -33.241  -5.825  0.50 25.75           C  
-ATOM    543  CD1AILE A 104      26.890 -36.859  -4.402  0.50 20.87           C  
-ATOM    544  CG1BILE A 104      26.708 -33.096  -4.953  0.50 34.41           C  
-ATOM    545  CG2BILE A 104      26.481 -35.762  -4.497  0.50 33.95           C  
-ATOM    546  CD1BILE A 104      25.969 -32.225  -5.865  0.50 31.92           C  
-ATOM    547  N   ARG A 105      26.823 -35.800  -8.334  1.00 31.97           N  
-ATOM    548  CA  ARG A 105      26.178 -35.834  -9.636  1.00 33.72           C  
-ATOM    549  C   ARG A 105      24.633 -35.767  -9.549  1.00 32.49           C  
-ATOM    550  O   ARG A 105      24.059 -36.567  -8.811  1.00 34.33           O  
-ATOM    551  CB  ARG A 105      26.551 -37.149 -10.314  1.00 34.73           C  
-ATOM    552  CG  ARG A 105      26.483 -37.011 -11.790  1.00 46.12           C  
-ATOM    553  CD  ARG A 105      27.485 -37.943 -12.439  1.00 60.19           C  
-ATOM    554  NE  ARG A 105      27.591 -37.579 -13.847  1.00 69.78           N  
-ATOM    555  CZ  ARG A 105      28.558 -37.998 -14.655  1.00 74.70           C  
-ATOM    556  NH1 ARG A 105      29.514 -38.799 -14.177  1.00 77.45           N  
-ATOM    557  NH2 ARG A 105      28.576 -37.604 -15.931  1.00 77.10           N  
-ATOM    558  N   LEU A 106      24.017 -34.813 -10.230  1.00 29.52           N  
-ATOM    559  CA  LEU A 106      22.542 -34.777 -10.418  1.00 32.73           C  
-ATOM    560  C   LEU A 106      22.171 -35.871 -11.472  1.00 33.48           C  
-ATOM    561  O   LEU A 106      22.681 -35.858 -12.615  1.00 34.00           O  
-ATOM    562  CB  LEU A 106      22.040 -33.447 -10.944  1.00 30.94           C  
-ATOM    563  CG  LEU A 106      20.516 -33.272 -11.058  1.00 31.54           C  
-ATOM    564  CD1 LEU A 106      19.785 -33.566  -9.733  1.00 30.06           C  
-ATOM    565  CD2 LEU A 106      20.248 -31.838 -11.594  1.00 31.66           C  
-ATOM    566  N   LEU A 107      21.405 -36.854 -11.064  1.00 34.91           N  
-ATOM    567  CA  LEU A 107      20.942 -37.927 -11.936  1.00 36.57           C  
-ATOM    568  C   LEU A 107      19.629 -37.604 -12.667  1.00 38.07           C  
-ATOM    569  O   LEU A 107      19.402 -38.039 -13.815  1.00 40.00           O  
-ATOM    570  CB  LEU A 107      20.763 -39.236 -11.114  1.00 36.28           C  
-ATOM    571  CG  LEU A 107      22.060 -39.726 -10.501  1.00 36.75           C  
-ATOM    572  CD1 LEU A 107      21.953 -40.971  -9.601  1.00 37.78           C  
-ATOM    573  CD2 LEU A 107      23.151 -39.918 -11.524  1.00 44.83           C  
-ATOM    574  N   ASP A 108      18.758 -36.845 -12.039  1.00 38.65           N  
-ATOM    575  CA  ASP A 108      17.481 -36.574 -12.649  1.00 39.91           C  
-ATOM    576  C   ASP A 108      16.788 -35.613 -11.781  1.00 39.26           C  
-ATOM    577  O   ASP A 108      17.249 -35.325 -10.702  1.00 38.80           O  
-ATOM    578  CB  ASP A 108      16.677 -37.885 -12.780  1.00 41.52           C  
-ATOM    579  CG  ASP A 108      15.530 -37.774 -13.818  1.00 45.70           C  
-ATOM    580  OD1 ASP A 108      15.161 -36.678 -14.294  1.00 49.10           O  
-ATOM    581  OD2 ASP A 108      14.975 -38.815 -14.114  1.00 54.18           O  
-ATOM    582  N   TRP A 109      15.685 -35.060 -12.249  1.00 39.91           N  
-ATOM    583  CA  TRP A 109      14.903 -34.116 -11.458  1.00 40.46           C  
-ATOM    584  C   TRP A 109      13.469 -34.091 -12.005  1.00 42.34           C  
-ATOM    585  O   TRP A 109      13.273 -34.414 -13.179  1.00 40.62           O  
-ATOM    586  CB  TRP A 109      15.479 -32.688 -11.461  1.00 39.42           C  
-ATOM    587  CG  TRP A 109      15.512 -31.999 -12.815  1.00 41.04           C  
-ATOM    588  CD1 TRP A 109      16.485 -32.132 -13.832  1.00 43.92           C  
-ATOM    589  CD2 TRP A 109      14.577 -31.033 -13.284  1.00 41.70           C  
-ATOM    590  NE1 TRP A 109      16.167 -31.278 -14.888  1.00 43.68           N  
-ATOM    591  CE2 TRP A 109      14.997 -30.618 -14.584  1.00 44.52           C  
-ATOM    592  CE3 TRP A 109      13.402 -30.483 -12.738  1.00 46.95           C  
-ATOM    593  CZ2 TRP A 109      14.269 -29.687 -15.346  1.00 47.16           C  
-ATOM    594  CZ3 TRP A 109      12.653 -29.517 -13.508  1.00 47.20           C  
-ATOM    595  CH2 TRP A 109      13.106 -29.143 -14.803  1.00 46.61           C  
-ATOM    596  N   PHE A 110      12.517 -33.647 -11.161  1.00 43.51           N  
-ATOM    597  CA  PHE A 110      11.051 -33.607 -11.435  1.00 44.50           C  
-ATOM    598  C   PHE A 110      10.549 -32.334 -10.851  1.00 44.80           C  
-ATOM    599  O   PHE A 110      11.104 -31.858  -9.851  1.00 43.59           O  
-ATOM    600  CB  PHE A 110      10.325 -34.796 -10.761  1.00 45.06           C  
-ATOM    601  CG  PHE A 110      10.910 -36.110 -11.141  1.00 49.35           C  
-ATOM    602  CD1 PHE A 110      10.499 -36.772 -12.333  1.00 56.67           C  
-ATOM    603  CD2 PHE A 110      11.946 -36.683 -10.388  1.00 50.52           C  
-ATOM    604  CE1 PHE A 110      11.109 -38.008 -12.733  1.00 58.32           C  
-ATOM    605  CE2 PHE A 110      12.570 -37.917 -10.776  1.00 53.02           C  
-ATOM    606  CZ  PHE A 110      12.156 -38.569 -11.949  1.00 55.73           C  
-ATOM    607  N   GLU A 111       9.537 -31.746 -11.504  1.00 43.96           N  
-ATOM    608  CA  GLU A 111       8.783 -30.659 -10.977  1.00 45.26           C  
-ATOM    609  C   GLU A 111       7.443 -31.122 -10.368  1.00 46.10           C  
-ATOM    610  O   GLU A 111       6.835 -32.077 -10.863  1.00 46.88           O  
-ATOM    611  CB  GLU A 111       8.477 -29.646 -12.066  1.00 45.62           C  
-ATOM    612  CG  GLU A 111       7.729 -28.495 -11.464  1.00 46.08           C  
-ATOM    613  CD  GLU A 111       7.803 -27.244 -12.256  1.00 48.06           C  
-ATOM    614  OE1 GLU A 111       8.312 -27.316 -13.348  1.00 49.46           O  
-ATOM    615  OE2 GLU A 111       7.361 -26.170 -11.795  1.00 50.56           O  
-ATOM    616  N   ARG A 112       7.015 -30.430  -9.304  1.00 45.88           N  
-ATOM    617  CA  ARG A 112       5.716 -30.638  -8.629  1.00 44.99           C  
-ATOM    618  C   ARG A 112       5.156 -29.269  -8.268  1.00 46.47           C  
-ATOM    619  O   ARG A 112       5.889 -28.236  -8.302  1.00 46.76           O  
-ATOM    620  CB  ARG A 112       5.876 -31.413  -7.298  1.00 43.68           C  
-ATOM    621  CG  ARG A 112       6.097 -32.902  -7.420  1.00 40.52           C  
-ATOM    622  CD  ARG A 112       6.454 -33.462  -6.064  1.00 43.52           C  
-ATOM    623  NE  ARG A 112       6.474 -34.930  -6.094  1.00 46.93           N  
-ATOM    624  CZ  ARG A 112       6.613 -35.738  -5.035  1.00 45.06           C  
-ATOM    625  NH1 ARG A 112       6.856 -35.257  -3.814  1.00 39.93           N  
-ATOM    626  NH2 ARG A 112       6.591 -37.046  -5.232  1.00 42.09           N  
-ATOM    627  N   PRO A 113       3.842 -29.210  -7.943  1.00 46.67           N  
-ATOM    628  CA  PRO A 113       3.245 -27.938  -7.656  1.00 46.16           C  
-ATOM    629  C   PRO A 113       3.992 -27.076  -6.648  1.00 46.96           C  
-ATOM    630  O   PRO A 113       4.030 -25.856  -6.856  1.00 46.27           O  
-ATOM    631  CB  PRO A 113       1.858 -28.315  -7.073  1.00 46.71           C  
-ATOM    632  CG  PRO A 113       1.581 -29.673  -7.633  1.00 46.85           C  
-ATOM    633  CD  PRO A 113       2.853 -30.316  -8.028  1.00 46.67           C  
-ATOM    634  N   ASP A 114       4.569 -27.637  -5.564  1.00 45.21           N  
-ATOM    635  CA  ASP A 114       5.163 -26.716  -4.552  1.00 46.02           C  
-ATOM    636  C   ASP A 114       6.621 -26.909  -4.337  1.00 43.52           C  
-ATOM    637  O   ASP A 114       7.243 -26.216  -3.519  1.00 45.02           O  
-ATOM    638  CB  ASP A 114       4.416 -26.742  -3.187  1.00 47.63           C  
-ATOM    639  CG  ASP A 114       3.055 -25.999  -3.259  1.00 54.33           C  
-ATOM    640  OD1 ASP A 114       2.915 -25.091  -4.136  1.00 56.21           O  
-ATOM    641  OD2 ASP A 114       2.148 -26.320  -2.438  1.00 57.73           O  
-ATOM    642  N   SER A 115       7.172 -27.824  -5.123  1.00 42.80           N  
-ATOM    643  CA  SER A 115       8.524 -28.294  -4.890  1.00 41.08           C  
-ATOM    644  C   SER A 115       9.190 -28.809  -6.217  1.00 39.61           C  
-ATOM    645  O   SER A 115       8.491 -29.177  -7.209  1.00 38.22           O  
-ATOM    646  CB  SER A 115       8.430 -29.416  -3.831  1.00 39.40           C  
-ATOM    647  OG  SER A 115       7.897 -30.593  -4.408  1.00 37.58           O  
-ATOM    648  N   PHE A 116      10.527 -28.875  -6.211  1.00 38.66           N  
-ATOM    649  CA  PHE A 116      11.202 -29.836  -7.110  1.00 37.11           C  
-ATOM    650  C   PHE A 116      11.768 -31.046  -6.424  1.00 37.67           C  
-ATOM    651  O   PHE A 116      12.101 -30.961  -5.257  1.00 36.96           O  
-ATOM    652  CB  PHE A 116      12.343 -29.116  -7.829  1.00 39.44           C  
-ATOM    653  CG  PHE A 116      11.853 -28.063  -8.797  1.00 39.54           C  
-ATOM    654  CD1 PHE A 116      11.429 -26.832  -8.341  1.00 40.96           C  
-ATOM    655  CD2 PHE A 116      11.785 -28.356 -10.182  1.00 43.25           C  
-ATOM    656  CE1 PHE A 116      10.994 -25.857  -9.278  1.00 46.87           C  
-ATOM    657  CE2 PHE A 116      11.313 -27.380 -11.099  1.00 41.46           C  
-ATOM    658  CZ  PHE A 116      10.947 -26.171 -10.646  1.00 39.92           C  
-ATOM    659  N   VAL A 117      12.037 -32.102  -7.175  1.00 35.40           N  
-ATOM    660  CA  VAL A 117      12.629 -33.264  -6.583  1.00 35.69           C  
-ATOM    661  C   VAL A 117      13.870 -33.575  -7.366  1.00 35.93           C  
-ATOM    662  O   VAL A 117      13.818 -33.828  -8.615  1.00 35.59           O  
-ATOM    663  CB  VAL A 117      11.640 -34.466  -6.531  1.00 35.93           C  
-ATOM    664  CG1 VAL A 117      12.229 -35.602  -5.778  1.00 33.66           C  
-ATOM    665  CG2 VAL A 117      10.335 -34.004  -5.803  1.00 36.43           C  
-ATOM    666  N   LEU A 118      15.005 -33.502  -6.662  1.00 33.56           N  
-ATOM    667  CA  LEU A 118      16.307 -33.783  -7.269  1.00 32.68           C  
-ATOM    668  C   LEU A 118      16.721 -35.154  -6.913  1.00 31.32           C  
-ATOM    669  O   LEU A 118      16.706 -35.501  -5.725  1.00 30.55           O  
-ATOM    670  CB  LEU A 118      17.334 -32.767  -6.756  1.00 31.02           C  
-ATOM    671  CG  LEU A 118      17.305 -31.368  -7.397  1.00 36.47           C  
-ATOM    672  CD1 LEU A 118      15.968 -30.713  -7.887  1.00 35.81           C  
-ATOM    673  CD2 LEU A 118      18.234 -30.355  -6.627  1.00 36.38           C  
-ATOM    674  N   ILE A 119      17.221 -35.902  -7.893  1.00 29.95           N  
-ATOM    675  CA  ILE A 119      17.759 -37.231  -7.656  1.00 31.00           C  
-ATOM    676  C   ILE A 119      19.274 -37.183  -7.789  1.00 31.33           C  
-ATOM    677  O   ILE A 119      19.774 -36.813  -8.882  1.00 31.05           O  
-ATOM    678  CB  ILE A 119      17.258 -38.315  -8.709  1.00 29.91           C  
-ATOM    679  CG1 ILE A 119      15.752 -38.256  -8.931  1.00 34.32           C  
-ATOM    680  CG2 ILE A 119      17.666 -39.708  -8.305  1.00 35.14           C  
-ATOM    681  CD1 ILE A 119      14.915 -38.665  -7.731  1.00 33.60           C  
-ATOM    682  N   LEU A 120      19.987 -37.563  -6.711  1.00 30.24           N  
-ATOM    683  CA  LEU A 120      21.393 -37.326  -6.650  1.00 29.10           C  
-ATOM    684  C   LEU A 120      22.025 -38.631  -6.361  1.00 31.47           C  
-ATOM    685  O   LEU A 120      21.469 -39.478  -5.695  1.00 28.99           O  
-ATOM    686  CB  LEU A 120      21.763 -36.350  -5.506  1.00 30.47           C  
-ATOM    687  CG  LEU A 120      21.164 -34.995  -5.712  1.00 27.09           C  
-ATOM    688  CD1 LEU A 120      20.714 -34.312  -4.430  1.00 30.85           C  
-ATOM    689  CD2 LEU A 120      22.133 -34.071  -6.492  1.00 32.14           C  
-ATOM    690  N   GLU A 121      23.267 -38.740  -6.800  1.00 31.19           N  
-ATOM    691  CA  GLU A 121      24.188 -39.798  -6.457  1.00 32.74           C  
-ATOM    692  C   GLU A 121      24.217 -39.987  -4.964  1.00 32.04           C  
-ATOM    693  O   GLU A 121      24.180 -39.023  -4.214  1.00 30.33           O  
-ATOM    694  CB  GLU A 121      25.549 -39.221  -6.916  1.00 33.59           C  
-ATOM    695  CG  GLU A 121      26.661 -40.028  -6.610  1.00 38.65           C  
-ATOM    696  CD  GLU A 121      28.002 -39.454  -7.163  1.00 44.57           C  
-ATOM    697  OE1 GLU A 121      28.168 -38.238  -7.510  1.00 36.26           O  
-ATOM    698  OE2 GLU A 121      28.913 -40.273  -7.167  1.00 48.00           O  
-ATOM    699  N   ARG A 122      24.377 -41.220  -4.513  1.00 31.29           N  
-ATOM    700  CA  ARG A 122      24.544 -41.473  -3.106  1.00 32.95           C  
-ATOM    701  C   ARG A 122      25.596 -42.508  -2.877  1.00 34.08           C  
-ATOM    702  O   ARG A 122      25.428 -43.678  -3.207  1.00 34.66           O  
-ATOM    703  CB  ARG A 122      23.296 -41.913  -2.408  1.00 33.09           C  
-ATOM    704  CG  ARG A 122      23.527 -42.467  -1.022  1.00 32.27           C  
-ATOM    705  CD  ARG A 122      22.111 -42.470  -0.211  1.00 33.99           C  
-ATOM    706  NE  ARG A 122      21.186 -43.573  -0.695  1.00 34.76           N  
-ATOM    707  CZ  ARG A 122      21.349 -44.891  -0.444  1.00 38.82           C  
-ATOM    708  NH1 ARG A 122      22.319 -45.357   0.363  1.00 32.36           N  
-ATOM    709  NH2 ARG A 122      20.470 -45.771  -0.924  1.00 33.50           N  
-ATOM    710  N   PRO A 123      26.727 -42.071  -2.334  1.00 35.79           N  
-ATOM    711  CA  PRO A 123      27.853 -42.992  -1.961  1.00 35.31           C  
-ATOM    712  C   PRO A 123      27.381 -43.874  -0.772  1.00 35.06           C  
-ATOM    713  O   PRO A 123      26.520 -43.487   0.017  1.00 32.73           O  
-ATOM    714  CB  PRO A 123      28.922 -42.045  -1.477  1.00 32.60           C  
-ATOM    715  CG  PRO A 123      28.502 -40.651  -1.926  1.00 36.05           C  
-ATOM    716  CD  PRO A 123      27.040 -40.639  -2.088  1.00 36.77           C  
-ATOM    717  N   GLU A 124      27.962 -45.034  -0.636  1.00 35.65           N  
-ATOM    718  CA  GLU A 124      27.506 -45.922   0.418  1.00 38.41           C  
-ATOM    719  C   GLU A 124      28.610 -46.912   0.791  1.00 37.52           C  
-ATOM    720  O   GLU A 124      29.065 -47.622  -0.073  1.00 39.61           O  
-ATOM    721  CB  GLU A 124      26.226 -46.648  -0.028  1.00 39.56           C  
-ATOM    722  CG  GLU A 124      25.920 -47.940   0.749  1.00 46.07           C  
-ATOM    723  CD  GLU A 124      25.499 -47.671   2.195  1.00 56.42           C  
-ATOM    724  OE1 GLU A 124      24.568 -46.855   2.380  1.00 65.68           O  
-ATOM    725  OE2 GLU A 124      26.065 -48.268   3.155  1.00 59.55           O  
-ATOM    726  N   PRO A 125      29.061 -46.936   2.062  1.00 35.19           N  
-ATOM    727  CA  PRO A 125      28.669 -46.159   3.184  1.00 33.83           C  
-ATOM    728  C   PRO A 125      29.240 -44.708   3.029  1.00 33.95           C  
-ATOM    729  O   PRO A 125      30.266 -44.533   2.343  1.00 32.44           O  
-ATOM    730  CB  PRO A 125      29.373 -46.862   4.327  1.00 33.97           C  
-ATOM    731  CG  PRO A 125      30.641 -47.411   3.698  1.00 34.94           C  
-ATOM    732  CD  PRO A 125      30.155 -47.889   2.394  1.00 36.85           C  
-ATOM    733  N   VAL A 126      28.543 -43.730   3.612  1.00 32.82           N  
-ATOM    734  CA  VAL A 126      28.914 -42.316   3.487  1.00 32.52           C  
-ATOM    735  C   VAL A 126      28.701 -41.691   4.854  1.00 33.44           C  
-ATOM    736  O   VAL A 126      27.868 -42.164   5.688  1.00 31.70           O  
-ATOM    737  CB  VAL A 126      28.027 -41.624   2.411  1.00 32.95           C  
-ATOM    738  CG1 VAL A 126      26.587 -41.581   2.832  1.00 33.28           C  
-ATOM    739  CG2 VAL A 126      28.489 -40.219   2.002  1.00 32.16           C  
-ATOM    740  N   GLN A 127      29.415 -40.573   5.122  1.00 29.07           N  
-ATOM    741  CA  GLN A 127      29.145 -39.795   6.300  1.00 28.55           C  
-ATOM    742  C   GLN A 127      29.575 -38.366   5.969  1.00 27.50           C  
-ATOM    743  O   GLN A 127      30.593 -38.197   5.287  1.00 24.75           O  
-ATOM    744  CB  GLN A 127      29.979 -40.286   7.483  1.00 27.16           C  
-ATOM    745  CG  GLN A 127      29.743 -39.455   8.748  1.00 32.40           C  
-ATOM    746  CD  GLN A 127      30.546 -40.025   9.910  1.00 33.10           C  
-ATOM    747  OE1 GLN A 127      31.737 -40.324   9.776  1.00 32.71           O  
-ATOM    748  NE2 GLN A 127      29.868 -40.241  11.044  1.00 39.51           N  
-ATOM    749  N   ASP A 128      28.773 -37.397   6.345  1.00 26.27           N  
-ATOM    750  CA  ASP A 128      29.159 -36.006   6.077  1.00 27.29           C  
-ATOM    751  C   ASP A 128      30.283 -35.579   7.020  1.00 26.03           C  
-ATOM    752  O   ASP A 128      30.566 -36.178   8.138  1.00 25.21           O  
-ATOM    753  CB  ASP A 128      27.939 -35.047   5.961  1.00 25.66           C  
-ATOM    754  CG  ASP A 128      27.304 -34.635   7.331  1.00 33.64           C  
-ATOM    755  OD1 ASP A 128      27.961 -34.644   8.390  1.00 30.69           O  
-ATOM    756  OD2 ASP A 128      26.161 -34.137   7.244  1.00 36.75           O  
-ATOM    757  N   LEU A 129      30.963 -34.540   6.615  1.00 25.11           N  
-ATOM    758  CA  LEU A 129      32.138 -34.211   7.343  1.00 25.33           C  
-ATOM    759  C   LEU A 129      31.803 -33.618   8.717  1.00 25.78           C  
-ATOM    760  O   LEU A 129      32.596 -33.686   9.621  1.00 25.97           O  
-ATOM    761  CB  LEU A 129      33.049 -33.254   6.534  1.00 23.08           C  
-ATOM    762  CG  LEU A 129      34.308 -32.802   7.302  1.00 23.42           C  
-ATOM    763  CD1 LEU A 129      35.411 -33.905   7.484  1.00 20.46           C  
-ATOM    764  CD2 LEU A 129      34.938 -31.745   6.310  1.00 24.99           C  
-ATOM    765  N   PHE A 130      30.652 -32.970   8.866  1.00 29.13           N  
-ATOM    766  CA  PHE A 130      30.264 -32.446  10.173  1.00 29.96           C  
-ATOM    767  C   PHE A 130      30.138 -33.584  11.204  1.00 29.66           C  
-ATOM    768  O   PHE A 130      30.637 -33.478  12.323  1.00 28.61           O  
-ATOM    769  CB  PHE A 130      28.894 -31.756  10.019  1.00 31.02           C  
-ATOM    770  CG  PHE A 130      28.397 -31.151  11.299  1.00 34.71           C  
-ATOM    771  CD1 PHE A 130      27.602 -31.924  12.182  1.00 40.18           C  
-ATOM    772  CD2 PHE A 130      28.702 -29.818  11.640  1.00 34.72           C  
-ATOM    773  CE1 PHE A 130      27.152 -31.392  13.393  1.00 40.40           C  
-ATOM    774  CE2 PHE A 130      28.233 -29.266  12.858  1.00 38.60           C  
-ATOM    775  CZ  PHE A 130      27.485 -30.090  13.735  1.00 38.86           C  
-ATOM    776  N   ASP A 131      29.497 -34.699  10.803  1.00 30.16           N  
-ATOM    777  CA  ASP A 131      29.301 -35.825  11.725  1.00 30.32           C  
-ATOM    778  C   ASP A 131      30.605 -36.553  11.982  1.00 30.52           C  
-ATOM    779  O   ASP A 131      30.894 -37.024  13.099  1.00 29.18           O  
-ATOM    780  CB  ASP A 131      28.310 -36.837  11.078  1.00 29.43           C  
-ATOM    781  CG  ASP A 131      26.887 -36.321  11.074  1.00 35.90           C  
-ATOM    782  OD1 ASP A 131      26.625 -35.350  11.774  1.00 37.73           O  
-ATOM    783  OD2 ASP A 131      26.052 -36.835  10.298  1.00 39.80           O  
-ATOM    784  N   PHE A 132      31.409 -36.658  10.934  1.00 28.53           N  
-ATOM    785  CA  PHE A 132      32.750 -37.228  11.091  1.00 27.38           C  
-ATOM    786  C   PHE A 132      33.567 -36.511  12.133  1.00 30.02           C  
-ATOM    787  O   PHE A 132      34.182 -37.134  13.040  1.00 30.75           O  
-ATOM    788  CB  PHE A 132      33.400 -37.208   9.724  1.00 26.47           C  
-ATOM    789  CG  PHE A 132      34.708 -37.930   9.669  1.00 28.90           C  
-ATOM    790  CD1 PHE A 132      34.732 -39.303   9.431  1.00 29.70           C  
-ATOM    791  CD2 PHE A 132      35.908 -37.242   9.826  1.00 29.64           C  
-ATOM    792  CE1 PHE A 132      35.969 -39.977   9.316  1.00 31.52           C  
-ATOM    793  CE2 PHE A 132      37.158 -37.913   9.755  1.00 30.60           C  
-ATOM    794  CZ  PHE A 132      37.204 -39.292   9.503  1.00 30.16           C  
-ATOM    795  N   ILE A 133      33.622 -35.180  12.027  1.00 28.28           N  
-ATOM    796  CA  ILE A 133      34.284 -34.336  13.054  1.00 27.77           C  
-ATOM    797  C   ILE A 133      33.596 -34.430  14.424  1.00 30.62           C  
-ATOM    798  O   ILE A 133      34.276 -34.504  15.403  1.00 31.56           O  
-ATOM    799  CB  ILE A 133      34.410 -32.840  12.606  1.00 26.40           C  
-ATOM    800  CG1 ILE A 133      35.422 -32.804  11.413  1.00 24.61           C  
-ATOM    801  CG2 ILE A 133      34.870 -31.926  13.826  1.00 29.10           C  
-ATOM    802  CD1 ILE A 133      35.503 -31.455  10.542  1.00 26.63           C  
-ATOM    803  N   THR A 134      32.272 -34.453  14.488  1.00 31.85           N  
-ATOM    804  CA  THR A 134      31.595 -34.653  15.797  1.00 35.11           C  
-ATOM    805  C   THR A 134      32.050 -35.938  16.439  1.00 37.09           C  
-ATOM    806  O   THR A 134      32.253 -36.000  17.610  1.00 39.29           O  
-ATOM    807  CB  THR A 134      30.062 -34.708  15.579  1.00 35.29           C  
-ATOM    808  OG1 THR A 134      29.651 -33.474  15.033  1.00 33.57           O  
-ATOM    809  CG2 THR A 134      29.284 -34.894  16.892  1.00 37.26           C  
-ATOM    810  N   GLU A 135      32.298 -36.961  15.663  1.00 38.46           N  
-ATOM    811  CA  GLU A 135      32.514 -38.259  16.209  1.00 41.85           C  
-ATOM    812  C   GLU A 135      33.978 -38.411  16.521  1.00 42.40           C  
-ATOM    813  O   GLU A 135      34.339 -38.955  17.596  1.00 43.22           O  
-ATOM    814  CB  GLU A 135      32.040 -39.190  15.140  1.00 42.25           C  
-ATOM    815  CG  GLU A 135      32.454 -40.575  15.187  1.00 50.18           C  
-ATOM    816  CD  GLU A 135      31.466 -41.402  14.346  1.00 58.63           C  
-ATOM    817  OE1 GLU A 135      30.242 -41.013  14.283  1.00 60.41           O  
-ATOM    818  OE2 GLU A 135      31.936 -42.393  13.745  1.00 60.86           O  
-ATOM    819  N   ARG A 136      34.836 -37.824  15.679  1.00 39.32           N  
-ATOM    820  CA  ARG A 136      36.258 -38.026  15.833  1.00 39.36           C  
-ATOM    821  C   ARG A 136      37.112 -36.902  16.422  1.00 37.79           C  
-ATOM    822  O   ARG A 136      38.311 -37.114  16.687  1.00 38.90           O  
-ATOM    823  CB  ARG A 136      36.849 -38.562  14.510  1.00 39.99           C  
-ATOM    824  CG  ARG A 136      36.182 -39.865  14.158  1.00 45.81           C  
-ATOM    825  CD  ARG A 136      36.689 -40.506  12.872  1.00 54.30           C  
-ATOM    826  NE  ARG A 136      38.164 -40.525  12.689  1.00 53.36           N  
-ATOM    827  CZ  ARG A 136      38.782 -41.378  11.854  1.00 48.64           C  
-ATOM    828  NH1 ARG A 136      38.053 -42.311  11.188  1.00 45.04           N  
-ATOM    829  NH2 ARG A 136      40.117 -41.325  11.699  1.00 47.92           N  
-ATOM    830  N   GLY A 137      36.499 -35.757  16.673  1.00 35.01           N  
-ATOM    831  CA  GLY A 137      37.180 -34.545  17.080  1.00 32.95           C  
-ATOM    832  C   GLY A 137      38.076 -33.954  15.994  1.00 32.78           C  
-ATOM    833  O   GLY A 137      37.942 -34.317  14.800  1.00 31.00           O  
-ATOM    834  N   ALA A 138      39.051 -33.124  16.424  1.00 31.60           N  
-ATOM    835  CA  ALA A 138      40.004 -32.500  15.553  1.00 29.42           C  
-ATOM    836  C   ALA A 138      40.753 -33.573  14.758  1.00 30.65           C  
-ATOM    837  O   ALA A 138      41.155 -34.642  15.298  1.00 29.49           O  
-ATOM    838  CB  ALA A 138      40.998 -31.688  16.381  1.00 31.08           C  
-ATOM    839  N   LEU A 139      40.962 -33.331  13.469  1.00 26.44           N  
-ATOM    840  CA  LEU A 139      41.533 -34.345  12.599  1.00 27.14           C  
-ATOM    841  C   LEU A 139      43.066 -34.238  12.637  1.00 27.80           C  
-ATOM    842  O   LEU A 139      43.601 -33.125  12.648  1.00 27.42           O  
-ATOM    843  CB  LEU A 139      41.025 -34.089  11.181  1.00 26.24           C  
-ATOM    844  CG  LEU A 139      39.494 -34.170  11.040  1.00 27.13           C  
-ATOM    845  CD1 LEU A 139      39.285 -34.159   9.540  1.00 27.40           C  
-ATOM    846  CD2 LEU A 139      38.887 -35.447  11.758  1.00 25.71           C  
-ATOM    847  N   GLN A 140      43.785 -35.376  12.614  1.00 27.62           N  
-ATOM    848  CA  GLN A 140      45.240 -35.335  12.428  1.00 29.70           C  
-ATOM    849  C   GLN A 140      45.548 -34.525  11.148  1.00 28.73           C  
-ATOM    850  O   GLN A 140      44.792 -34.611  10.157  1.00 25.59           O  
-ATOM    851  CB  GLN A 140      45.733 -36.759  12.209  1.00 29.89           C  
-ATOM    852  CG  GLN A 140      45.740 -37.655  13.494  1.00 38.19           C  
-ATOM    853  CD  GLN A 140      46.332 -39.071  13.092  1.00 38.73           C  
-ATOM    854  OE1 GLN A 140      47.198 -39.169  12.143  1.00 49.24           O  
-ATOM    855  NE2 GLN A 140      45.879 -40.141  13.794  1.00 54.11           N  
-ATOM    856  N   GLU A 141      46.676 -33.785  11.129  1.00 27.08           N  
-ATOM    857  CA  GLU A 141      46.985 -32.921   9.948  1.00 26.52           C  
-ATOM    858  C   GLU A 141      47.031 -33.680   8.660  1.00 27.40           C  
-ATOM    859  O   GLU A 141      46.584 -33.219   7.670  1.00 25.05           O  
-ATOM    860  CB  GLU A 141      48.234 -32.074  10.193  1.00 27.30           C  
-ATOM    861  CG  GLU A 141      47.956 -31.058  11.362  1.00 28.63           C  
-ATOM    862  CD  GLU A 141      49.024 -29.999  11.494  1.00 30.12           C  
-ATOM    863  OE1 GLU A 141      49.841 -29.781  10.557  1.00 27.43           O  
-ATOM    864  OE2 GLU A 141      49.098 -29.471  12.609  1.00 30.70           O  
-ATOM    865  N   GLU A 142      47.581 -34.903   8.667  1.00 26.74           N  
-ATOM    866  CA  GLU A 142      47.675 -35.621   7.408  1.00 27.41           C  
-ATOM    867  C   GLU A 142      46.313 -35.920   6.825  1.00 25.55           C  
-ATOM    868  O   GLU A 142      46.142 -35.943   5.606  1.00 23.97           O  
-ATOM    869  CB  GLU A 142      48.387 -36.985   7.693  1.00 30.08           C  
-ATOM    870  CG  GLU A 142      48.590 -37.864   6.492  1.00 28.60           C  
-ATOM    871  CD  GLU A 142      49.167 -39.294   6.914  1.00 33.18           C  
-ATOM    872  OE1 GLU A 142      48.442 -40.143   7.485  1.00 34.97           O  
-ATOM    873  OE2 GLU A 142      50.367 -39.475   6.664  1.00 35.79           O  
-ATOM    874  N   LEU A 143      45.376 -36.244   7.695  1.00 23.17           N  
-ATOM    875  CA  LEU A 143      44.006 -36.484   7.237  1.00 23.84           C  
-ATOM    876  C   LEU A 143      43.362 -35.177   6.786  1.00 24.15           C  
-ATOM    877  O   LEU A 143      42.753 -35.129   5.685  1.00 25.29           O  
-ATOM    878  CB  LEU A 143      43.144 -37.028   8.353  1.00 23.11           C  
-ATOM    879  CG  LEU A 143      41.698 -37.370   7.974  1.00 25.36           C  
-ATOM    880  CD1 LEU A 143      41.658 -38.324   6.711  1.00 25.33           C  
-ATOM    881  CD2 LEU A 143      41.097 -38.033   9.169  1.00 25.01           C  
-ATOM    882  N   ALA A 144      43.528 -34.139   7.579  1.00 22.86           N  
-ATOM    883  CA  ALA A 144      43.014 -32.795   7.157  1.00 22.68           C  
-ATOM    884  C   ALA A 144      43.597 -32.353   5.820  1.00 22.68           C  
-ATOM    885  O   ALA A 144      42.877 -31.776   5.024  1.00 23.92           O  
-ATOM    886  CB  ALA A 144      43.285 -31.747   8.141  1.00 21.64           C  
-ATOM    887  N   ARG A 145      44.919 -32.585   5.558  1.00 24.59           N  
-ATOM    888  CA  ARG A 145      45.545 -32.201   4.323  1.00 22.45           C  
-ATOM    889  C   ARG A 145      44.886 -32.916   3.160  1.00 22.52           C  
-ATOM    890  O   ARG A 145      44.567 -32.328   2.122  1.00 21.79           O  
-ATOM    891  CB  ARG A 145      47.075 -32.602   4.381  1.00 21.31           C  
-ATOM    892  CG  ARG A 145      47.857 -32.312   3.038  1.00 25.01           C  
-ATOM    893  CD  ARG A 145      49.391 -32.700   3.237  1.00 24.23           C  
-ATOM    894  NE  ARG A 145      49.951 -32.057   4.416  1.00 27.14           N  
-ATOM    895  CZ  ARG A 145      50.346 -32.652   5.530  1.00 28.55           C  
-ATOM    896  NH1 ARG A 145      50.391 -33.990   5.712  1.00 26.72           N  
-ATOM    897  NH2 ARG A 145      50.755 -31.885   6.483  1.00 33.03           N  
-ATOM    898  N   SER A 146      44.633 -34.210   3.315  1.00 23.58           N  
-ATOM    899  CA  SER A 146      44.034 -35.016   2.253  1.00 22.98           C  
-ATOM    900  C   SER A 146      42.629 -34.504   1.985  1.00 25.29           C  
-ATOM    901  O   SER A 146      42.246 -34.287   0.841  1.00 24.96           O  
-ATOM    902  CB  SER A 146      43.901 -36.478   2.747  1.00 23.14           C  
-ATOM    903  OG  SER A 146      43.324 -37.235   1.655  1.00 26.82           O  
-ATOM    904  N   PHE A 147      41.849 -34.256   3.033  1.00 23.43           N  
-ATOM    905  CA  PHE A 147      40.470 -33.831   2.836  1.00 20.83           C  
-ATOM    906  C   PHE A 147      40.463 -32.415   2.237  1.00 21.53           C  
-ATOM    907  O   PHE A 147      39.697 -32.097   1.359  1.00 23.08           O  
-ATOM    908  CB  PHE A 147      39.835 -33.768   4.207  1.00 23.16           C  
-ATOM    909  CG  PHE A 147      39.280 -35.122   4.668  1.00 25.29           C  
-ATOM    910  CD1 PHE A 147      39.541 -36.284   3.910  1.00 26.75           C  
-ATOM    911  CD2 PHE A 147      38.465 -35.178   5.801  1.00 23.55           C  
-ATOM    912  CE1 PHE A 147      38.958 -37.612   4.344  1.00 30.21           C  
-ATOM    913  CE2 PHE A 147      37.954 -36.420   6.237  1.00 27.52           C  
-ATOM    914  CZ  PHE A 147      38.152 -37.604   5.472  1.00 26.48           C  
-ATOM    915  N   PHE A 148      41.287 -31.542   2.822  1.00 21.31           N  
-ATOM    916  CA  PHE A 148      41.271 -30.136   2.327  1.00 20.47           C  
-ATOM    917  C   PHE A 148      41.678 -30.061   0.874  1.00 23.13           C  
-ATOM    918  O   PHE A 148      41.179 -29.268   0.156  1.00 22.57           O  
-ATOM    919  CB  PHE A 148      42.219 -29.305   3.184  1.00 18.27           C  
-ATOM    920  CG  PHE A 148      42.025 -27.796   3.021  1.00 22.88           C  
-ATOM    921  CD1 PHE A 148      40.765 -27.196   3.264  1.00 23.16           C  
-ATOM    922  CD2 PHE A 148      43.101 -27.012   2.633  1.00 19.06           C  
-ATOM    923  CE1 PHE A 148      40.651 -25.819   3.101  1.00 23.62           C  
-ATOM    924  CE2 PHE A 148      42.973 -25.585   2.479  1.00 20.88           C  
-ATOM    925  CZ  PHE A 148      41.759 -25.041   2.701  1.00 20.95           C  
-ATOM    926  N   TRP A 149      42.733 -30.790   0.481  1.00 22.32           N  
-ATOM    927  CA  TRP A 149      43.184 -30.865  -0.937  1.00 20.82           C  
-ATOM    928  C   TRP A 149      42.022 -31.284  -1.813  1.00 20.64           C  
-ATOM    929  O   TRP A 149      41.741 -30.667  -2.849  1.00 21.97           O  
-ATOM    930  CB  TRP A 149      44.287 -31.988  -1.031  1.00 20.43           C  
-ATOM    931  CG  TRP A 149      44.842 -32.115  -2.505  1.00 21.15           C  
-ATOM    932  CD1 TRP A 149      44.469 -33.007  -3.495  1.00 24.06           C  
-ATOM    933  CD2 TRP A 149      45.873 -31.279  -3.073  1.00 23.65           C  
-ATOM    934  NE1 TRP A 149      45.237 -32.757  -4.658  1.00 25.56           N  
-ATOM    935  CE2 TRP A 149      46.103 -31.722  -4.414  1.00 24.09           C  
-ATOM    936  CE3 TRP A 149      46.652 -30.205  -2.552  1.00 26.82           C  
-ATOM    937  CZ2 TRP A 149      47.081 -31.103  -5.263  1.00 24.33           C  
-ATOM    938  CZ3 TRP A 149      47.699 -29.615  -3.402  1.00 24.25           C  
-ATOM    939  CH2 TRP A 149      47.823 -30.035  -4.741  1.00 26.48           C  
-ATOM    940  N   GLN A 150      41.335 -32.394  -1.448  1.00 18.88           N  
-ATOM    941  CA  GLN A 150      40.228 -32.807  -2.234  1.00 20.76           C  
-ATOM    942  C   GLN A 150      39.126 -31.748  -2.328  1.00 22.67           C  
-ATOM    943  O   GLN A 150      38.431 -31.620  -3.373  1.00 21.86           O  
-ATOM    944  CB  GLN A 150      39.621 -34.113  -1.656  1.00 23.39           C  
-ATOM    945  CG  GLN A 150      40.561 -35.314  -1.910  1.00 24.59           C  
-ATOM    946  CD  GLN A 150      39.819 -36.644  -1.566  1.00 25.61           C  
-ATOM    947  OE1 GLN A 150      38.692 -36.864  -1.995  1.00 28.87           O  
-ATOM    948  NE2 GLN A 150      40.406 -37.418  -0.688  1.00 30.09           N  
-ATOM    949  N   VAL A 151      38.894 -31.026  -1.255  1.00 23.16           N  
-ATOM    950  CA  VAL A 151      37.839 -30.030  -1.365  1.00 22.31           C  
-ATOM    951  C   VAL A 151      38.307 -28.969  -2.357  1.00 23.03           C  
-ATOM    952  O   VAL A 151      37.478 -28.335  -3.018  1.00 22.95           O  
-ATOM    953  CB  VAL A 151      37.609 -29.343  -0.026  1.00 22.73           C  
-ATOM    954  CG1 VAL A 151      36.751 -27.981  -0.093  1.00 21.65           C  
-ATOM    955  CG2 VAL A 151      36.924 -30.333   1.048  1.00 19.33           C  
-ATOM    956  N   LEU A 152      39.571 -28.556  -2.245  1.00 21.56           N  
-ATOM    957  CA  LEU A 152      40.090 -27.508  -3.175  1.00 23.37           C  
-ATOM    958  C   LEU A 152      39.993 -27.959  -4.641  1.00 22.39           C  
-ATOM    959  O   LEU A 152      39.640 -27.184  -5.487  1.00 21.99           O  
-ATOM    960  CB  LEU A 152      41.648 -27.307  -2.884  1.00 24.79           C  
-ATOM    961  CG  LEU A 152      42.041 -26.090  -1.979  1.00 28.96           C  
-ATOM    962  CD1 LEU A 152      41.858 -24.692  -2.642  1.00 29.37           C  
-ATOM    963  CD2 LEU A 152      41.257 -25.913  -0.843  1.00 28.91           C  
-ATOM    964  N   GLU A 153      40.233 -29.245  -4.941  1.00 21.28           N  
-ATOM    965  CA  GLU A 153      40.091 -29.756  -6.299  1.00 21.77           C  
-ATOM    966  C   GLU A 153      38.592 -29.655  -6.729  1.00 22.81           C  
-ATOM    967  O   GLU A 153      38.313 -29.212  -7.863  1.00 21.05           O  
-ATOM    968  CB  GLU A 153      40.561 -31.252  -6.393  1.00 23.87           C  
-ATOM    969  CG  GLU A 153      42.067 -31.365  -6.293  1.00 23.88           C  
-ATOM    970  CD  GLU A 153      42.794 -30.777  -7.481  1.00 30.87           C  
-ATOM    971  OE1 GLU A 153      42.390 -31.140  -8.555  1.00 29.83           O  
-ATOM    972  OE2 GLU A 153      43.859 -30.111  -7.372  1.00 29.42           O  
-ATOM    973  N   ALA A 154      37.652 -29.977  -5.796  1.00 22.82           N  
-ATOM    974  CA  ALA A 154      36.167 -29.921  -6.077  1.00 20.17           C  
-ATOM    975  C   ALA A 154      35.744 -28.444  -6.329  1.00 22.74           C  
-ATOM    976  O   ALA A 154      34.998 -28.134  -7.240  1.00 23.12           O  
-ATOM    977  CB  ALA A 154      35.365 -30.474  -4.826  1.00 20.21           C  
-ATOM    978  N   VAL A 155      36.178 -27.522  -5.472  1.00 22.86           N  
-ATOM    979  CA  VAL A 155      35.848 -26.085  -5.677  1.00 21.95           C  
-ATOM    980  C   VAL A 155      36.427 -25.531  -6.951  1.00 22.92           C  
-ATOM    981  O   VAL A 155      35.738 -24.835  -7.697  1.00 23.13           O  
-ATOM    982  CB  VAL A 155      36.323 -25.249  -4.434  1.00 20.73           C  
-ATOM    983  CG1 VAL A 155      35.932 -23.759  -4.559  1.00 22.62           C  
-ATOM    984  CG2 VAL A 155      35.575 -25.815  -3.159  1.00 20.11           C  
-ATOM    985  N   ARG A 156      37.726 -25.781  -7.229  1.00 22.83           N  
-ATOM    986  CA  ARG A 156      38.326 -25.393  -8.546  1.00 23.82           C  
-ATOM    987  C   ARG A 156      37.513 -25.953  -9.702  1.00 25.67           C  
-ATOM    988  O   ARG A 156      37.305 -25.256 -10.704  1.00 28.03           O  
-ATOM    989  CB  ARG A 156      39.733 -25.972  -8.635  1.00 24.26           C  
-ATOM    990  CG  ARG A 156      40.717 -25.239  -7.768  1.00 23.59           C  
-ATOM    991  CD  ARG A 156      42.176 -25.863  -7.941  1.00 22.05           C  
-ATOM    992  NE  ARG A 156      42.522 -25.802  -9.349  1.00 25.12           N  
-ATOM    993  CZ  ARG A 156      43.408 -26.590  -9.980  1.00 24.97           C  
-ATOM    994  NH1 ARG A 156      44.148 -27.503  -9.307  1.00 21.71           N  
-ATOM    995  NH2 ARG A 156      43.562 -26.426 -11.300  1.00 22.49           N  
-ATOM    996  N   HIS A 157      37.100 -27.224  -9.655  1.00 25.34           N  
-ATOM    997  CA  HIS A 157      36.184 -27.738 -10.726  1.00 26.16           C  
-ATOM    998  C   HIS A 157      34.896 -26.841 -10.819  1.00 26.22           C  
-ATOM    999  O   HIS A 157      34.497 -26.455 -11.937  1.00 24.14           O  
-ATOM   1000  CB  HIS A 157      35.807 -29.220 -10.494  1.00 29.01           C  
-ATOM   1001  CG  HIS A 157      34.756 -29.752 -11.414  1.00 27.83           C  
-ATOM   1002  ND1 HIS A 157      35.060 -30.126 -12.691  1.00 28.14           N  
-ATOM   1003  CD2 HIS A 157      33.446 -30.019 -11.235  1.00 31.11           C  
-ATOM   1004  CE1 HIS A 157      33.968 -30.616 -13.264  1.00 33.40           C  
-ATOM   1005  NE2 HIS A 157      32.970 -30.530 -12.415  1.00 32.14           N  
-ATOM   1006  N   CYS A 158      34.237 -26.550  -9.702  1.00 22.79           N  
-ATOM   1007  CA  CYS A 158      33.012 -25.730  -9.753  1.00 24.22           C  
-ATOM   1008  C   CYS A 158      33.350 -24.417 -10.443  1.00 24.38           C  
-ATOM   1009  O   CYS A 158      32.645 -24.004 -11.413  1.00 23.43           O  
-ATOM   1010  CB  CYS A 158      32.531 -25.329  -8.288  1.00 24.35           C  
-ATOM   1011  SG  CYS A 158      31.771 -26.833  -7.557  1.00 28.68           S  
-ATOM   1012  N   HIS A 159      34.457 -23.800 -10.028  1.00 23.35           N  
-ATOM   1013  CA  HIS A 159      34.817 -22.439 -10.615  1.00 25.21           C  
-ATOM   1014  C   HIS A 159      35.186 -22.538 -12.084  1.00 26.01           C  
-ATOM   1015  O   HIS A 159      34.826 -21.685 -12.869  1.00 25.38           O  
-ATOM   1016  CB  HIS A 159      35.989 -21.842  -9.841  1.00 24.19           C  
-ATOM   1017  CG  HIS A 159      35.586 -21.371  -8.457  1.00 30.31           C  
-ATOM   1018  ND1 HIS A 159      36.233 -20.351  -7.816  1.00 33.32           N  
-ATOM   1019  CD2 HIS A 159      34.555 -21.727  -7.624  1.00 29.25           C  
-ATOM   1020  CE1 HIS A 159      35.655 -20.107  -6.639  1.00 39.57           C  
-ATOM   1021  NE2 HIS A 159      34.642 -20.936  -6.490  1.00 32.75           N  
-ATOM   1022  N   ASN A 160      35.737 -23.664 -12.491  1.00 26.25           N  
-ATOM   1023  CA  ASN A 160      36.197 -23.830 -13.907  1.00 29.77           C  
-ATOM   1024  C   ASN A 160      34.945 -24.014 -14.742  1.00 30.29           C  
-ATOM   1025  O   ASN A 160      34.943 -23.640 -15.911  1.00 30.77           O  
-ATOM   1026  CB  ASN A 160      36.914 -25.143 -14.134  1.00 29.48           C  
-ATOM   1027  CG AASN A 160      38.248 -25.204 -13.599  0.50 30.78           C  
-ATOM   1028  OD1AASN A 160      38.850 -24.214 -13.264  0.50 39.73           O  
-ATOM   1029  ND2AASN A 160      38.737 -26.438 -13.437  0.50 35.30           N  
-ATOM   1030  CG BASN A 160      37.768 -25.137 -15.409  0.50 25.98           C  
-ATOM   1031  OD1BASN A 160      38.453 -24.177 -15.728  0.50 22.31           O  
-ATOM   1032  ND2BASN A 160      37.730 -26.215 -16.098  0.50 21.71           N  
-ATOM   1033  N   CYS A 161      33.872 -24.554 -14.139  1.00 29.89           N  
-ATOM   1034  CA  CYS A 161      32.550 -24.762 -14.769  1.00 30.63           C  
-ATOM   1035  C   CYS A 161      31.657 -23.537 -14.670  1.00 30.60           C  
-ATOM   1036  O   CYS A 161      30.487 -23.560 -15.143  1.00 32.73           O  
-ATOM   1037  CB  CYS A 161      31.776 -26.001 -14.162  1.00 30.83           C  
-ATOM   1038  SG  CYS A 161      32.661 -27.484 -14.621  1.00 34.43           S  
-ATOM   1039  N   GLY A 162      32.201 -22.455 -14.120  1.00 30.24           N  
-ATOM   1040  CA  GLY A 162      31.432 -21.192 -14.003  1.00 27.08           C  
-ATOM   1041  C   GLY A 162      30.432 -21.194 -12.868  1.00 27.33           C  
-ATOM   1042  O   GLY A 162      29.443 -20.445 -12.936  1.00 25.45           O  
-ATOM   1043  N   VAL A 163      30.661 -22.006 -11.795  1.00 25.84           N  
-ATOM   1044  CA  VAL A 163      29.745 -22.080 -10.630  1.00 26.26           C  
-ATOM   1045  C   VAL A 163      30.514 -21.698  -9.341  1.00 24.46           C  
-ATOM   1046  O   VAL A 163      31.635 -22.181  -9.085  1.00 25.77           O  
-ATOM   1047  CB  VAL A 163      29.276 -23.505 -10.475  1.00 25.95           C  
-ATOM   1048  CG1 VAL A 163      28.470 -23.757  -9.213  1.00 22.61           C  
-ATOM   1049  CG2 VAL A 163      28.502 -23.942 -11.851  1.00 26.26           C  
-ATOM   1050  N   LEU A 164      29.899 -20.812  -8.602  1.00 26.07           N  
-ATOM   1051  CA  LEU A 164      30.280 -20.381  -7.230  1.00 25.38           C  
-ATOM   1052  C   LEU A 164      29.359 -21.088  -6.196  1.00 27.89           C  
-ATOM   1053  O   LEU A 164      28.089 -20.909  -6.214  1.00 26.98           O  
-ATOM   1054  CB  LEU A 164      30.143 -18.858  -7.208  1.00 25.80           C  
-ATOM   1055  CG  LEU A 164      30.620 -18.252  -5.882  1.00 24.34           C  
-ATOM   1056  CD1 LEU A 164      32.212 -18.378  -5.872  1.00 24.36           C  
-ATOM   1057  CD2 LEU A 164      30.222 -16.712  -5.642  1.00 22.47           C  
-ATOM   1058  N   HIS A 165      29.945 -21.894  -5.293  1.00 23.86           N  
-ATOM   1059  CA  HIS A 165      29.092 -22.696  -4.391  1.00 25.70           C  
-ATOM   1060  C   HIS A 165      28.395 -21.837  -3.286  1.00 25.03           C  
-ATOM   1061  O   HIS A 165      27.148 -22.023  -2.989  1.00 26.34           O  
-ATOM   1062  CB  HIS A 165      29.980 -23.775  -3.644  1.00 25.67           C  
-ATOM   1063  CG  HIS A 165      29.189 -24.761  -2.851  1.00 24.89           C  
-ATOM   1064  ND1 HIS A 165      28.821 -24.536  -1.541  1.00 23.45           N  
-ATOM   1065  CD2 HIS A 165      28.813 -26.038  -3.142  1.00 21.86           C  
-ATOM   1066  CE1 HIS A 165      28.161 -25.594  -1.080  1.00 24.76           C  
-ATOM   1067  NE2 HIS A 165      28.164 -26.531  -2.025  1.00 21.81           N  
-ATOM   1068  N   ARG A 166      29.162 -20.908  -2.675  1.00 21.37           N  
-ATOM   1069  CA  ARG A 166      28.708 -20.036  -1.616  1.00 24.04           C  
-ATOM   1070  C   ARG A 166      28.251 -20.647  -0.276  1.00 25.62           C  
-ATOM   1071  O   ARG A 166      27.753 -19.929   0.575  1.00 26.92           O  
-ATOM   1072  CB  ARG A 166      27.567 -19.102  -2.157  1.00 24.21           C  
-ATOM   1073  CG  ARG A 166      28.054 -18.245  -3.360  1.00 24.75           C  
-ATOM   1074  CD  ARG A 166      27.157 -16.943  -3.502  1.00 26.20           C  
-ATOM   1075  NE  ARG A 166      25.774 -17.217  -3.870  1.00 26.20           N  
-ATOM   1076  CZ  ARG A 166      24.876 -16.248  -4.146  1.00 31.72           C  
-ATOM   1077  NH1 ARG A 166      25.227 -14.922  -4.052  1.00 26.43           N  
-ATOM   1078  NH2 ARG A 166      23.632 -16.617  -4.489  1.00 31.35           N  
-ATOM   1079  N   ASP A 167      28.342 -21.966  -0.099  1.00 24.26           N  
-ATOM   1080  CA  ASP A 167      28.104 -22.493   1.268  1.00 25.13           C  
-ATOM   1081  C   ASP A 167      29.074 -23.627   1.579  1.00 24.16           C  
-ATOM   1082  O   ASP A 167      28.711 -24.715   2.027  1.00 24.64           O  
-ATOM   1083  CB  ASP A 167      26.626 -22.958   1.344  1.00 27.62           C  
-ATOM   1084  CG  ASP A 167      26.132 -23.108   2.787  1.00 32.49           C  
-ATOM   1085  OD1 ASP A 167      26.805 -22.472   3.670  1.00 29.84           O  
-ATOM   1086  OD2 ASP A 167      25.058 -23.794   2.970  1.00 30.59           O  
-ATOM   1087  N   ILE A 168      30.364 -23.431   1.286  1.00 23.39           N  
-ATOM   1088  CA  ILE A 168      31.342 -24.523   1.544  1.00 24.00           C  
-ATOM   1089  C   ILE A 168      31.432 -24.665   3.070  1.00 24.14           C  
-ATOM   1090  O   ILE A 168      31.712 -23.695   3.759  1.00 24.74           O  
-ATOM   1091  CB  ILE A 168      32.754 -24.129   0.970  1.00 23.31           C  
-ATOM   1092  CG1 ILE A 168      32.672 -23.967  -0.565  1.00 24.67           C  
-ATOM   1093  CG2 ILE A 168      33.793 -25.160   1.480  1.00 21.61           C  
-ATOM   1094  CD1 ILE A 168      33.838 -23.113  -1.130  1.00 26.98           C  
-ATOM   1095  N   LYS A 169      31.225 -25.868   3.606  1.00 24.35           N  
-ATOM   1096  CA  LYS A 169      31.291 -26.041   5.034  1.00 25.00           C  
-ATOM   1097  C   LYS A 169      31.188 -27.550   5.272  1.00 24.75           C  
-ATOM   1098  O   LYS A 169      30.830 -28.333   4.340  1.00 23.20           O  
-ATOM   1099  CB  LYS A 169      30.128 -25.308   5.743  1.00 23.48           C  
-ATOM   1100  CG  LYS A 169      28.751 -25.835   5.359  1.00 26.54           C  
-ATOM   1101  CD  LYS A 169      27.788 -25.086   6.242  1.00 31.09           C  
-ATOM   1102  CE  LYS A 169      26.404 -25.378   5.956  1.00 39.50           C  
-ATOM   1103  NZ  LYS A 169      25.749 -24.786   7.258  1.00 40.65           N  
-ATOM   1104  N   ASP A 170      31.536 -27.963   6.492  1.00 24.88           N  
-ATOM   1105  CA  ASP A 170      31.576 -29.374   6.747  1.00 25.56           C  
-ATOM   1106  C   ASP A 170      30.301 -30.142   6.421  1.00 26.80           C  
-ATOM   1107  O   ASP A 170      30.403 -31.215   5.894  1.00 26.25           O  
-ATOM   1108  CB  ASP A 170      32.132 -29.727   8.164  1.00 26.29           C  
-ATOM   1109  CG  ASP A 170      31.414 -29.020   9.300  1.00 30.62           C  
-ATOM   1110  OD1 ASP A 170      30.344 -28.350   9.092  1.00 36.77           O  
-ATOM   1111  OD2 ASP A 170      31.958 -29.176  10.439  1.00 36.67           O  
-ATOM   1112  N   GLU A 171      29.122 -29.589   6.684  1.00 26.53           N  
-ATOM   1113  CA  GLU A 171      27.865 -30.312   6.452  1.00 29.58           C  
-ATOM   1114  C   GLU A 171      27.556 -30.413   4.950  1.00 28.48           C  
-ATOM   1115  O   GLU A 171      26.697 -31.222   4.576  1.00 28.32           O  
-ATOM   1116  CB  GLU A 171      26.675 -29.505   6.917  1.00 29.87           C  
-ATOM   1117  CG  GLU A 171      26.500 -29.278   8.322  1.00 41.57           C  
-ATOM   1118  CD  GLU A 171      25.349 -28.261   8.453  1.00 51.15           C  
-ATOM   1119  OE1 GLU A 171      24.315 -28.478   7.737  1.00 43.90           O  
-ATOM   1120  OE2 GLU A 171      25.587 -27.254   9.190  1.00 55.57           O  
-ATOM   1121  N   ASN A 172      28.239 -29.639   4.114  1.00 25.88           N  
-ATOM   1122  CA  ASN A 172      28.052 -29.766   2.663  1.00 23.17           C  
-ATOM   1123  C   ASN A 172      29.193 -30.549   1.981  1.00 24.59           C  
-ATOM   1124  O   ASN A 172      29.406 -30.402   0.771  1.00 27.78           O  
-ATOM   1125  CB  ASN A 172      27.921 -28.413   2.032  1.00 22.24           C  
-ATOM   1126  CG  ASN A 172      26.575 -27.792   2.275  1.00 27.22           C  
-ATOM   1127  OD1 ASN A 172      25.613 -28.541   2.465  1.00 26.19           O  
-ATOM   1128  ND2 ASN A 172      26.496 -26.443   2.298  1.00 22.07           N  
-ATOM   1129  N   ILE A 173      29.845 -31.448   2.701  1.00 25.04           N  
-ATOM   1130  CA  ILE A 173      30.869 -32.319   2.197  1.00 22.60           C  
-ATOM   1131  C   ILE A 173      30.590 -33.764   2.634  1.00 24.04           C  
-ATOM   1132  O   ILE A 173      30.454 -34.026   3.864  1.00 24.29           O  
-ATOM   1133  CB  ILE A 173      32.247 -31.904   2.761  1.00 23.90           C  
-ATOM   1134  CG1 ILE A 173      32.658 -30.495   2.122  1.00 20.17           C  
-ATOM   1135  CG2 ILE A 173      33.336 -32.925   2.372  1.00 21.74           C  
-ATOM   1136  CD1 ILE A 173      33.854 -29.794   2.913  1.00 26.07           C  
-ATOM   1137  N   LEU A 174      30.499 -34.683   1.664  1.00 22.77           N  
-ATOM   1138  CA  LEU A 174      30.244 -36.079   2.033  1.00 25.29           C  
-ATOM   1139  C   LEU A 174      31.527 -36.844   1.927  1.00 26.90           C  
-ATOM   1140  O   LEU A 174      32.344 -36.552   1.012  1.00 28.03           O  
-ATOM   1141  CB  LEU A 174      29.156 -36.684   1.110  1.00 24.84           C  
-ATOM   1142  CG  LEU A 174      27.744 -36.104   1.085  1.00 30.57           C  
-ATOM   1143  CD1 LEU A 174      26.948 -36.963   0.060  1.00 30.70           C  
-ATOM   1144  CD2 LEU A 174      27.233 -36.147   2.542  1.00 30.28           C  
-ATOM   1145  N   ILE A 175      31.737 -37.838   2.788  1.00 27.06           N  
-ATOM   1146  CA  ILE A 175      32.902 -38.725   2.673  1.00 26.72           C  
-ATOM   1147  C   ILE A 175      32.485 -40.111   2.209  1.00 30.44           C  
-ATOM   1148  O   ILE A 175      31.644 -40.721   2.872  1.00 27.31           O  
-ATOM   1149  CB  ILE A 175      33.624 -38.858   4.040  1.00 27.41           C  
-ATOM   1150  CG1 ILE A 175      33.986 -37.511   4.674  1.00 27.02           C  
-ATOM   1151  CG2 ILE A 175      34.887 -39.770   3.843  1.00 24.32           C  
-ATOM   1152  CD1 ILE A 175      34.280 -37.637   6.256  1.00 25.65           C  
-ATOM   1153  N   ASP A 176      33.004 -40.557   1.045  1.00 30.99           N  
-ATOM   1154  CA  ASP A 176      32.759 -41.896   0.479  1.00 32.94           C  
-ATOM   1155  C   ASP A 176      33.779 -42.677   1.271  1.00 34.86           C  
-ATOM   1156  O   ASP A 176      34.983 -42.689   0.931  1.00 37.46           O  
-ATOM   1157  CB  ASP A 176      33.079 -41.782  -1.031  1.00 34.09           C  
-ATOM   1158  CG  ASP A 176      32.900 -43.118  -1.840  1.00 37.09           C  
-ATOM   1159  OD1 ASP A 176      32.970 -44.164  -1.222  1.00 36.07           O  
-ATOM   1160  OD2 ASP A 176      32.737 -43.027  -3.106  1.00 36.11           O  
-ATOM   1161  N   LEU A 177      33.344 -43.251   2.400  1.00 34.86           N  
-ATOM   1162  CA  LEU A 177      34.244 -43.948   3.324  1.00 35.99           C  
-ATOM   1163  C   LEU A 177      35.036 -45.094   2.652  1.00 37.79           C  
-ATOM   1164  O   LEU A 177      36.217 -45.236   2.931  1.00 41.08           O  
-ATOM   1165  CB  LEU A 177      33.540 -44.423   4.607  1.00 34.43           C  
-ATOM   1166  CG  LEU A 177      32.754 -43.313   5.363  1.00 35.19           C  
-ATOM   1167  CD1 LEU A 177      31.530 -43.961   6.139  1.00 29.99           C  
-ATOM   1168  CD2 LEU A 177      33.700 -42.428   6.284  1.00 29.36           C  
-ATOM   1169  N   ASN A 178      34.460 -45.846   1.725  1.00 37.88           N  
-ATOM   1170  CA  ASN A 178      35.260 -46.969   1.207  1.00 38.39           C  
-ATOM   1171  C   ASN A 178      36.454 -46.472   0.407  1.00 37.35           C  
-ATOM   1172  O   ASN A 178      37.553 -46.979   0.563  1.00 35.87           O  
-ATOM   1173  CB  ASN A 178      34.380 -47.921   0.410  1.00 38.58           C  
-ATOM   1174  CG  ASN A 178      33.609 -48.882   1.344  1.00 43.86           C  
-ATOM   1175  OD1 ASN A 178      33.938 -48.982   2.531  1.00 45.17           O  
-ATOM   1176  ND2 ASN A 178      32.587 -49.543   0.820  1.00 46.79           N  
-ATOM   1177  N   ARG A 179      36.227 -45.407  -0.362  1.00 35.16           N  
-ATOM   1178  CA  ARG A 179      37.217 -44.917  -1.332  1.00 35.60           C  
-ATOM   1179  C   ARG A 179      38.081 -43.731  -0.845  1.00 34.90           C  
-ATOM   1180  O   ARG A 179      39.049 -43.365  -1.528  1.00 36.23           O  
-ATOM   1181  CB  ARG A 179      36.462 -44.466  -2.539  1.00 35.81           C  
-ATOM   1182  CG  ARG A 179      35.624 -45.588  -3.169  1.00 37.98           C  
-ATOM   1183  CD  ARG A 179      35.336 -45.197  -4.604  1.00 37.69           C  
-ATOM   1184  NE  ARG A 179      34.711 -46.248  -5.410  1.00 44.70           N  
-ATOM   1185  CZ  ARG A 179      35.380 -47.267  -5.998  1.00 46.64           C  
-ATOM   1186  NH1 ARG A 179      36.700 -47.425  -5.875  1.00 44.32           N  
-ATOM   1187  NH2 ARG A 179      34.704 -48.129  -6.741  1.00 49.67           N  
-ATOM   1188  N   GLY A 180      37.770 -43.191   0.317  1.00 32.15           N  
-ATOM   1189  CA  GLY A 180      38.465 -41.993   0.900  1.00 31.61           C  
-ATOM   1190  C   GLY A 180      38.240 -40.702   0.044  1.00 31.12           C  
-ATOM   1191  O   GLY A 180      39.125 -39.826   0.003  1.00 32.72           O  
-ATOM   1192  N   GLU A 181      37.121 -40.638  -0.684  1.00 28.50           N  
-ATOM   1193  CA  GLU A 181      36.882 -39.574  -1.672  1.00 27.41           C  
-ATOM   1194  C   GLU A 181      35.851 -38.652  -1.076  1.00 28.88           C  
-ATOM   1195  O   GLU A 181      34.804 -39.125  -0.648  1.00 28.97           O  
-ATOM   1196  CB  GLU A 181      36.407 -40.136  -3.044  1.00 26.21           C  
-ATOM   1197  CG  GLU A 181      37.525 -40.973  -3.662  1.00 27.40           C  
-ATOM   1198  CD  GLU A 181      37.135 -41.456  -5.050  1.00 37.04           C  
-ATOM   1199  OE1 GLU A 181      35.993 -41.147  -5.493  1.00 32.70           O  
-ATOM   1200  OE2 GLU A 181      38.000 -42.127  -5.691  1.00 38.22           O  
-ATOM   1201  N   LEU A 182      36.095 -37.338  -1.100  1.00 26.52           N  
-ATOM   1202  CA  LEU A 182      35.070 -36.358  -0.645  1.00 26.68           C  
-ATOM   1203  C   LEU A 182      34.210 -35.894  -1.798  1.00 27.11           C  
-ATOM   1204  O   LEU A 182      34.701 -35.808  -2.944  1.00 28.38           O  
-ATOM   1205  CB  LEU A 182      35.829 -35.165  -0.023  1.00 28.70           C  
-ATOM   1206  CG  LEU A 182      36.060 -35.278   1.470  1.00 29.04           C  
-ATOM   1207  CD1 LEU A 182      36.659 -36.511   2.019  1.00 32.63           C  
-ATOM   1208  CD2 LEU A 182      36.963 -34.032   1.841  1.00 29.82           C  
-ATOM   1209  N   LYS A 183      32.942 -35.568  -1.535  1.00 27.11           N  
-ATOM   1210  CA  LYS A 183      32.107 -34.978  -2.547  1.00 27.27           C  
-ATOM   1211  C   LYS A 183      31.472 -33.720  -2.033  1.00 26.19           C  
-ATOM   1212  O   LYS A 183      30.860 -33.752  -0.932  1.00 25.94           O  
-ATOM   1213  CB  LYS A 183      30.953 -35.971  -2.865  1.00 26.31           C  
-ATOM   1214  CG  LYS A 183      31.437 -37.238  -3.506  1.00 34.31           C  
-ATOM   1215  CD  LYS A 183      30.232 -38.022  -4.061  1.00 41.92           C  
-ATOM   1216  CE  LYS A 183      30.452 -38.590  -5.447  1.00 47.42           C  
-ATOM   1217  NZ  LYS A 183      31.745 -39.209  -5.677  1.00 43.81           N  
-ATOM   1218  N   LEU A 184      31.473 -32.641  -2.815  1.00 24.47           N  
-ATOM   1219  CA  LEU A 184      30.791 -31.398  -2.418  1.00 23.71           C  
-ATOM   1220  C   LEU A 184      29.353 -31.560  -2.853  1.00 25.36           C  
-ATOM   1221  O   LEU A 184      29.093 -32.017  -4.039  1.00 25.64           O  
-ATOM   1222  CB  LEU A 184      31.467 -30.261  -3.210  1.00 25.53           C  
-ATOM   1223  CG  LEU A 184      31.120 -28.827  -3.038  1.00 29.08           C  
-ATOM   1224  CD1 LEU A 184      31.378 -28.408  -1.527  1.00 30.06           C  
-ATOM   1225  CD2 LEU A 184      32.108 -27.986  -3.993  1.00 29.09           C  
-ATOM   1226  N   ILE A 185      28.437 -31.205  -1.962  1.00 24.15           N  
-ATOM   1227  CA  ILE A 185      27.015 -31.296  -2.237  1.00 26.43           C  
-ATOM   1228  C   ILE A 185      26.415 -29.907  -2.046  1.00 27.47           C  
-ATOM   1229  O   ILE A 185      27.033 -29.007  -1.496  1.00 27.26           O  
-ATOM   1230  CB  ILE A 185      26.301 -32.356  -1.309  1.00 23.47           C  
-ATOM   1231  CG1 ILE A 185      26.534 -32.088   0.185  1.00 25.53           C  
-ATOM   1232  CG2 ILE A 185      26.841 -33.838  -1.566  1.00 21.78           C  
-ATOM   1233  CD1 ILE A 185      25.499 -32.726   1.142  1.00 28.98           C  
-ATOM   1234  N   ASP A 186      25.142 -29.768  -2.420  1.00 28.15           N  
-ATOM   1235  CA  ASP A 186      24.279 -28.651  -2.026  1.00 27.44           C  
-ATOM   1236  C   ASP A 186      24.607 -27.296  -2.669  1.00 27.24           C  
-ATOM   1237  O   ASP A 186      25.211 -26.365  -2.037  1.00 29.19           O  
-ATOM   1238  CB  ASP A 186      24.140 -28.497  -0.506  1.00 26.16           C  
-ATOM   1239  CG  ASP A 186      23.181 -27.366  -0.153  1.00 33.13           C  
-ATOM   1240  OD1 ASP A 186      22.357 -26.993  -1.033  1.00 31.21           O  
-ATOM   1241  OD2 ASP A 186      23.230 -26.819   0.972  1.00 32.30           O  
-ATOM   1242  N   PHE A 187      24.127 -27.124  -3.897  1.00 26.52           N  
-ATOM   1243  CA  PHE A 187      24.311 -25.856  -4.560  1.00 26.83           C  
-ATOM   1244  C   PHE A 187      23.124 -24.949  -4.362  1.00 28.73           C  
-ATOM   1245  O   PHE A 187      22.964 -23.953  -5.115  1.00 28.77           O  
-ATOM   1246  CB  PHE A 187      24.623 -26.065  -6.059  1.00 27.24           C  
-ATOM   1247  CG  PHE A 187      25.985 -26.704  -6.271  1.00 27.39           C  
-ATOM   1248  CD1 PHE A 187      26.148 -28.073  -6.126  1.00 30.55           C  
-ATOM   1249  CD2 PHE A 187      27.107 -25.928  -6.594  1.00 23.57           C  
-ATOM   1250  CE1 PHE A 187      27.423 -28.648  -6.343  1.00 29.73           C  
-ATOM   1251  CE2 PHE A 187      28.387 -26.535  -6.746  1.00 29.19           C  
-ATOM   1252  CZ  PHE A 187      28.544 -27.837  -6.575  1.00 25.95           C  
-ATOM   1253  N   GLY A 188      22.316 -25.256  -3.342  1.00 27.99           N  
-ATOM   1254  CA  GLY A 188      21.163 -24.401  -2.989  1.00 27.35           C  
-ATOM   1255  C   GLY A 188      21.381 -22.971  -2.620  1.00 29.84           C  
-ATOM   1256  O   GLY A 188      20.427 -22.192  -2.654  1.00 29.10           O  
-ATOM   1257  N   SER A 189      22.608 -22.582  -2.229  1.00 29.44           N  
-ATOM   1258  CA  SER A 189      22.936 -21.161  -2.010  1.00 30.94           C  
-ATOM   1259  C   SER A 189      23.850 -20.567  -3.097  1.00 31.10           C  
-ATOM   1260  O   SER A 189      24.330 -19.426  -2.945  1.00 27.58           O  
-ATOM   1261  CB  SER A 189      23.682 -20.981  -0.698  1.00 31.60           C  
-ATOM   1262  OG  SER A 189      22.919 -21.528   0.354  1.00 32.08           O  
-ATOM   1263  N   GLY A 190      24.080 -21.348  -4.152  1.00 29.71           N  
-ATOM   1264  CA  GLY A 190      25.133 -21.027  -5.138  1.00 29.90           C  
-ATOM   1265  C   GLY A 190      24.722 -19.971  -6.161  1.00 30.42           C  
-ATOM   1266  O   GLY A 190      23.576 -19.517  -6.153  1.00 28.93           O  
-ATOM   1267  N   ALA A 191      25.608 -19.643  -7.077  1.00 28.81           N  
-ATOM   1268  CA  ALA A 191      25.278 -18.685  -8.130  1.00 28.72           C  
-ATOM   1269  C   ALA A 191      26.207 -18.948  -9.262  1.00 29.58           C  
-ATOM   1270  O   ALA A 191      27.240 -19.644  -9.095  1.00 29.87           O  
-ATOM   1271  CB  ALA A 191      25.521 -17.227  -7.627  1.00 26.35           C  
-ATOM   1272  N   LEU A 192      25.897 -18.370 -10.444  1.00 27.58           N  
-ATOM   1273  CA  LEU A 192      26.881 -18.377 -11.514  1.00 27.73           C  
-ATOM   1274  C   LEU A 192      28.063 -17.498 -11.008  1.00 26.68           C  
-ATOM   1275  O   LEU A 192      27.859 -16.424 -10.383  1.00 24.84           O  
-ATOM   1276  CB  LEU A 192      26.253 -17.695 -12.764  1.00 29.41           C  
-ATOM   1277  CG  LEU A 192      24.979 -18.339 -13.190  1.00 31.29           C  
-ATOM   1278  CD1 LEU A 192      24.389 -17.613 -14.477  1.00 42.53           C  
-ATOM   1279  CD2 LEU A 192      25.389 -19.806 -13.515  1.00 36.02           C  
-ATOM   1280  N   LEU A 193      29.283 -17.935 -11.326  1.00 26.06           N  
-ATOM   1281  CA  LEU A 193      30.481 -17.224 -10.981  1.00 28.64           C  
-ATOM   1282  C   LEU A 193      30.573 -15.973 -11.901  1.00 30.75           C  
-ATOM   1283  O   LEU A 193      30.317 -16.068 -13.127  1.00 32.26           O  
-ATOM   1284  CB  LEU A 193      31.693 -18.127 -11.250  1.00 26.93           C  
-ATOM   1285  CG  LEU A 193      33.088 -17.593 -10.894  1.00 31.95           C  
-ATOM   1286  CD1 LEU A 193      33.149 -17.171  -9.377  1.00 27.94           C  
-ATOM   1287  CD2 LEU A 193      34.092 -18.660 -11.165  1.00 29.17           C  
-ATOM   1288  N   LYS A 194      30.960 -14.840 -11.345  1.00 31.51           N  
-ATOM   1289  CA  LYS A 194      31.122 -13.589 -12.098  1.00 30.51           C  
-ATOM   1290  C   LYS A 194      32.309 -12.850 -11.473  1.00 31.82           C  
-ATOM   1291  O   LYS A 194      32.725 -13.155 -10.315  1.00 34.00           O  
-ATOM   1292  CB  LYS A 194      29.819 -12.761 -11.991  1.00 29.31           C  
-ATOM   1293  CG  LYS A 194      29.428 -12.233 -10.575  1.00 28.12           C  
-ATOM   1294  CD  LYS A 194      28.066 -11.520 -10.579  1.00 28.11           C  
-ATOM   1295  CE  LYS A 194      27.834 -10.836  -9.336  1.00 28.85           C  
-ATOM   1296  NZ  LYS A 194      26.449 -10.245  -9.205  1.00 34.23           N  
-ATOM   1297  N   ASP A 195      32.830 -11.833 -12.164  1.00 30.15           N  
-ATOM   1298  CA  ASP A 195      34.024 -11.107 -11.683  1.00 30.55           C  
-ATOM   1299  C   ASP A 195      33.692  -9.830 -10.935  1.00 31.52           C  
-ATOM   1300  O   ASP A 195      34.594  -9.140 -10.444  1.00 32.37           O  
-ATOM   1301  CB  ASP A 195      34.865 -10.799 -12.869  1.00 31.44           C  
-ATOM   1302  CG  ASP A 195      35.357 -12.065 -13.554  1.00 38.20           C  
-ATOM   1303  OD1 ASP A 195      35.837 -12.886 -12.823  1.00 34.76           O  
-ATOM   1304  OD2 ASP A 195      35.283 -12.210 -14.766  1.00 37.96           O  
-ATOM   1305  N   THR A 196      32.399  -9.496 -10.853  1.00 31.46           N  
-ATOM   1306  CA  THR A 196      31.933  -8.274 -10.191  1.00 33.03           C  
-ATOM   1307  C   THR A 196      31.370  -8.670  -8.831  1.00 34.02           C  
-ATOM   1308  O   THR A 196      31.389  -9.878  -8.479  1.00 32.68           O  
-ATOM   1309  CB  THR A 196      30.905  -7.571 -11.111  1.00 32.79           C  
-ATOM   1310  OG1 THR A 196      29.913  -8.531 -11.468  1.00 36.58           O  
-ATOM   1311  CG2 THR A 196      31.690  -7.056 -12.423  1.00 34.00           C  
-ATOM   1312  N   VAL A 197      30.828  -7.713  -8.082  1.00 33.30           N  
-ATOM   1313  CA  VAL A 197      30.490  -7.916  -6.652  1.00 32.66           C  
-ATOM   1314  C   VAL A 197      29.153  -8.582  -6.484  1.00 32.93           C  
-ATOM   1315  O   VAL A 197      28.205  -8.350  -7.264  1.00 32.01           O  
-ATOM   1316  CB  VAL A 197      30.539  -6.553  -5.886  1.00 35.40           C  
-ATOM   1317  CG1 VAL A 197      29.268  -5.692  -6.203  1.00 39.18           C  
-ATOM   1318  CG2 VAL A 197      30.675  -6.764  -4.384  1.00 36.94           C  
-ATOM   1319  N   TYR A 198      29.057  -9.484  -5.517  1.00 29.58           N  
-ATOM   1320  CA  TYR A 198      27.760 -10.008  -5.096  1.00 31.16           C  
-ATOM   1321  C   TYR A 198      27.229  -9.169  -3.924  1.00 33.62           C  
-ATOM   1322  O   TYR A 198      28.003  -8.714  -3.096  1.00 33.68           O  
-ATOM   1323  CB  TYR A 198      27.948 -11.443  -4.599  1.00 28.29           C  
-ATOM   1324  CG  TYR A 198      28.368 -12.369  -5.700  1.00 29.52           C  
-ATOM   1325  CD1 TYR A 198      29.687 -12.502  -6.048  1.00 24.11           C  
-ATOM   1326  CD2 TYR A 198      27.392 -13.216  -6.319  1.00 23.96           C  
-ATOM   1327  CE1 TYR A 198      30.086 -13.392  -7.081  1.00 24.20           C  
-ATOM   1328  CE2 TYR A 198      27.753 -14.132  -7.358  1.00 28.83           C  
-ATOM   1329  CZ  TYR A 198      29.116 -14.266  -7.677  1.00 25.51           C  
-ATOM   1330  OH  TYR A 198      29.474 -15.086  -8.707  1.00 25.93           O  
-ATOM   1331  N   THR A 199      25.911  -8.940  -3.851  1.00 35.11           N  
-ATOM   1332  CA  THR A 199      25.333  -8.118  -2.811  1.00 36.95           C  
-ATOM   1333  C   THR A 199      24.195  -8.924  -2.193  1.00 37.80           C  
-ATOM   1334  O   THR A 199      23.507  -8.468  -1.321  1.00 37.51           O  
-ATOM   1335  CB  THR A 199      24.798  -6.829  -3.369  1.00 39.09           C  
-ATOM   1336  OG1 THR A 199      23.813  -7.148  -4.336  1.00 39.61           O  
-ATOM   1337  CG2 THR A 199      25.899  -5.980  -4.096  1.00 39.03           C  
-ATOM   1338  N   ASP A 200      24.047 -10.180  -2.587  1.00 37.56           N  
-ATOM   1339  CA  ASP A 200      23.104 -11.037  -1.952  1.00 39.28           C  
-ATOM   1340  C   ASP A 200      23.882 -12.195  -1.367  1.00 37.35           C  
-ATOM   1341  O   ASP A 200      24.914 -12.538  -1.938  1.00 36.86           O  
-ATOM   1342  CB  ASP A 200      22.126 -11.617  -3.029  1.00 41.98           C  
-ATOM   1343  CG  ASP A 200      22.827 -12.583  -4.081  1.00 46.93           C  
-ATOM   1344  OD1 ASP A 200      23.713 -12.069  -4.860  1.00 52.31           O  
-ATOM   1345  OD2 ASP A 200      22.452 -13.807  -4.160  1.00 46.98           O  
-ATOM   1346  N   PHE A 201      23.396 -12.796  -0.287  1.00 34.67           N  
-ATOM   1347  CA  PHE A 201      24.052 -13.986   0.235  1.00 35.70           C  
-ATOM   1348  C   PHE A 201      23.139 -14.733   1.142  1.00 36.10           C  
-ATOM   1349  O   PHE A 201      22.561 -14.135   1.999  1.00 38.23           O  
-ATOM   1350  CB  PHE A 201      25.265 -13.577   1.065  1.00 32.84           C  
-ATOM   1351  CG  PHE A 201      25.887 -14.712   1.800  1.00 34.82           C  
-ATOM   1352  CD1 PHE A 201      26.721 -15.625   1.129  1.00 31.36           C  
-ATOM   1353  CD2 PHE A 201      25.757 -14.822   3.177  1.00 35.09           C  
-ATOM   1354  CE1 PHE A 201      27.380 -16.703   1.824  1.00 34.67           C  
-ATOM   1355  CE2 PHE A 201      26.416 -15.856   3.887  1.00 37.38           C  
-ATOM   1356  CZ  PHE A 201      27.211 -16.817   3.185  1.00 36.58           C  
-ATOM   1357  N   ASP A 202      23.002 -16.038   1.016  1.00 36.68           N  
-ATOM   1358  C   ASP A 202      22.796 -18.068   2.269  1.00 35.25           C  
-ATOM   1359  O   ASP A 202      22.140 -19.060   2.475  1.00 35.36           O  
-ATOM   1360  CA AASP A 202      22.121 -16.756   1.939  0.50 35.94           C  
-ATOM   1361  CB AASP A 202      20.727 -17.025   1.307  0.50 37.33           C  
-ATOM   1362  CG AASP A 202      19.696 -17.559   2.324  0.50 38.82           C  
-ATOM   1363  OD1AASP A 202      19.448 -16.906   3.364  0.50 38.99           O  
-ATOM   1364  OD2AASP A 202      19.164 -18.676   2.097  0.50 42.59           O  
-ATOM   1365  CA BASP A 202      22.116 -16.771   1.882  0.50 36.07           C  
-ATOM   1366  CB BASP A 202      20.800 -17.050   1.124  0.50 37.52           C  
-ATOM   1367  CG BASP A 202      19.898 -15.819   1.069  0.50 38.99           C  
-ATOM   1368  OD1BASP A 202      19.351 -15.478   2.121  0.50 43.89           O  
-ATOM   1369  OD2BASP A 202      19.767 -15.173  -0.001  0.50 44.15           O  
-ATOM   1370  N   GLY A 203      24.130 -18.095   2.302  1.00 33.90           N  
-ATOM   1371  CA  GLY A 203      24.750 -19.338   2.778  1.00 30.96           C  
-ATOM   1372  C   GLY A 203      24.967 -19.210   4.274  1.00 32.56           C  
-ATOM   1373  O   GLY A 203      24.206 -18.530   4.961  1.00 33.14           O  
-ATOM   1374  N   THR A 204      26.040 -19.780   4.814  1.00 31.59           N  
-ATOM   1375  CA  THR A 204      26.125 -19.856   6.284  1.00 30.28           C  
-ATOM   1376  C   THR A 204      26.879 -18.618   6.884  1.00 30.69           C  
-ATOM   1377  O   THR A 204      28.096 -18.348   6.545  1.00 30.45           O  
-ATOM   1378  CB  THR A 204      26.730 -21.184   6.741  1.00 26.72           C  
-ATOM   1379  OG1 THR A 204      25.985 -22.323   6.250  1.00 30.91           O  
-ATOM   1380  CG2 THR A 204      26.837 -21.218   8.320  1.00 28.02           C  
-ATOM   1381  N   ARG A 205      26.219 -17.897   7.831  1.00 31.24           N  
-ATOM   1382  CA  ARG A 205      26.831 -16.607   8.307  1.00 33.11           C  
-ATOM   1383  C   ARG A 205      28.240 -16.817   8.936  1.00 30.52           C  
-ATOM   1384  O   ARG A 205      29.136 -16.025   8.649  1.00 32.83           O  
-ATOM   1385  CB  ARG A 205      25.970 -15.850   9.329  1.00 31.37           C  
-ATOM   1386  CG  ARG A 205      26.332 -14.375   9.434  1.00 36.04           C  
-ATOM   1387  CD  ARG A 205      25.244 -13.537  10.268  1.00 34.02           C  
-ATOM   1388  NE  ARG A 205      25.611 -12.104  10.443  1.00 34.75           N  
-ATOM   1389  CZ  ARG A 205      25.400 -11.100   9.581  1.00 39.40           C  
-ATOM   1390  NH1 ARG A 205      24.887 -11.295   8.381  1.00 40.09           N  
-ATOM   1391  NH2 ARG A 205      25.782  -9.854   9.875  1.00 38.02           N  
-ATOM   1392  N   VAL A 206      28.448 -17.861   9.749  1.00 31.45           N  
-ATOM   1393  CA  VAL A 206      29.735 -17.950  10.478  1.00 28.92           C  
-ATOM   1394  C   VAL A 206      30.868 -18.413   9.522  1.00 30.79           C  
-ATOM   1395  O   VAL A 206      32.019 -18.524   9.964  1.00 30.21           O  
-ATOM   1396  CB  VAL A 206      29.608 -18.876  11.681  1.00 32.09           C  
-ATOM   1397  CG1 VAL A 206      28.688 -18.253  12.759  1.00 28.59           C  
-ATOM   1398  CG2 VAL A 206      29.045 -20.352  11.291  1.00 26.34           C  
-ATOM   1399  N   TYR A 207      30.547 -18.720   8.239  1.00 30.09           N  
-ATOM   1400  CA  TYR A 207      31.559 -18.987   7.187  1.00 27.30           C  
-ATOM   1401  C   TYR A 207      31.734 -17.810   6.259  1.00 28.28           C  
-ATOM   1402  O   TYR A 207      32.557 -17.882   5.289  1.00 24.77           O  
-ATOM   1403  CB  TYR A 207      31.195 -20.193   6.351  1.00 28.61           C  
-ATOM   1404  CG  TYR A 207      31.479 -21.553   7.002  1.00 30.11           C  
-ATOM   1405  CD1 TYR A 207      30.648 -22.037   8.033  1.00 27.82           C  
-ATOM   1406  CD2 TYR A 207      32.648 -22.310   6.619  1.00 25.21           C  
-ATOM   1407  CE1 TYR A 207      30.881 -23.343   8.689  1.00 27.26           C  
-ATOM   1408  CE2 TYR A 207      32.897 -23.552   7.221  1.00 25.37           C  
-ATOM   1409  CZ  TYR A 207      32.024 -24.045   8.262  1.00 27.91           C  
-ATOM   1410  OH  TYR A 207      32.337 -25.334   8.713  1.00 34.67           O  
-ATOM   1411  N   SER A 208      30.890 -16.767   6.437  1.00 27.04           N  
-ATOM   1412  CA  SER A 208      30.923 -15.616   5.513  1.00 27.04           C  
-ATOM   1413  C   SER A 208      31.963 -14.549   5.996  1.00 27.63           C  
-ATOM   1414  O   SER A 208      32.288 -14.481   7.140  1.00 26.43           O  
-ATOM   1415  CB  SER A 208      29.526 -14.986   5.455  1.00 27.97           C  
-ATOM   1416  OG  SER A 208      29.362 -14.173   6.547  1.00 29.49           O  
-ATOM   1417  N   PRO A 209      32.551 -13.800   5.057  1.00 26.11           N  
-ATOM   1418  CA  PRO A 209      33.711 -13.052   5.309  1.00 27.80           C  
-ATOM   1419  C   PRO A 209      33.336 -11.674   5.855  1.00 28.61           C  
-ATOM   1420  O   PRO A 209      32.141 -11.227   5.783  1.00 29.03           O  
-ATOM   1421  CB  PRO A 209      34.340 -12.932   3.895  1.00 25.59           C  
-ATOM   1422  CG  PRO A 209      33.131 -12.807   2.982  1.00 27.07           C  
-ATOM   1423  CD  PRO A 209      32.144 -13.792   3.629  1.00 27.19           C  
-ATOM   1424  N   PRO A 210      34.335 -10.992   6.326  1.00 30.48           N  
-ATOM   1425  CA  PRO A 210      34.051  -9.750   7.039  1.00 29.56           C  
-ATOM   1426  C   PRO A 210      33.456  -8.688   6.128  1.00 31.24           C  
-ATOM   1427  O   PRO A 210      32.627  -7.895   6.604  1.00 30.70           O  
-ATOM   1428  CB  PRO A 210      35.415  -9.332   7.617  1.00 32.27           C  
-ATOM   1429  CG  PRO A 210      36.459 -10.197   6.982  1.00 31.07           C  
-ATOM   1430  CD  PRO A 210      35.777 -11.395   6.365  1.00 28.84           C  
-ATOM   1431  N   GLU A 211      33.853  -8.672   4.857  1.00 30.19           N  
-ATOM   1432  CA  GLU A 211      33.276  -7.710   3.936  1.00 31.88           C  
-ATOM   1433  C   GLU A 211      31.780  -7.991   3.736  1.00 30.44           C  
-ATOM   1434  O   GLU A 211      31.068  -7.060   3.522  1.00 34.12           O  
-ATOM   1435  CB  GLU A 211      33.964  -7.628   2.602  1.00 29.78           C  
-ATOM   1436  CG  GLU A 211      33.949  -8.980   1.755  1.00 31.45           C  
-ATOM   1437  CD  GLU A 211      35.087  -9.994   2.137  1.00 31.09           C  
-ATOM   1438  OE1 GLU A 211      35.684  -9.853   3.249  1.00 28.41           O  
-ATOM   1439  OE2 GLU A 211      35.387 -10.878   1.268  1.00 28.21           O  
-ATOM   1440  N   TRP A 212      31.313  -9.216   3.832  1.00 29.95           N  
-ATOM   1441  CA  TRP A 212      29.882  -9.454   3.806  1.00 31.71           C  
-ATOM   1442  C   TRP A 212      29.246  -8.882   5.099  1.00 34.05           C  
-ATOM   1443  O   TRP A 212      28.192  -8.159   5.050  1.00 34.57           O  
-ATOM   1444  CB  TRP A 212      29.514 -10.936   3.689  1.00 32.41           C  
-ATOM   1445  CG  TRP A 212      28.022 -11.127   3.924  1.00 29.88           C  
-ATOM   1446  CD1 TRP A 212      27.441 -11.746   5.009  1.00 36.25           C  
-ATOM   1447  CD2 TRP A 212      26.916 -10.681   3.076  1.00 32.50           C  
-ATOM   1448  NE1 TRP A 212      26.051 -11.700   4.887  1.00 35.66           N  
-ATOM   1449  CE2 TRP A 212      25.720 -11.025   3.739  1.00 34.86           C  
-ATOM   1450  CE3 TRP A 212      26.835 -10.007   1.830  1.00 27.19           C  
-ATOM   1451  CZ2 TRP A 212      24.459 -10.738   3.208  1.00 34.53           C  
-ATOM   1452  CZ3 TRP A 212      25.535  -9.714   1.301  1.00 35.80           C  
-ATOM   1453  CH2 TRP A 212      24.398 -10.114   1.982  1.00 32.98           C  
-ATOM   1454  N   ILE A 213      29.848  -9.198   6.248  1.00 32.51           N  
-ATOM   1455  CA  ILE A 213      29.247  -8.773   7.513  1.00 34.99           C  
-ATOM   1456  C   ILE A 213      29.180  -7.250   7.569  1.00 36.57           C  
-ATOM   1457  O   ILE A 213      28.154  -6.715   7.940  1.00 36.30           O  
-ATOM   1458  CB  ILE A 213      30.053  -9.285   8.724  1.00 34.48           C  
-ATOM   1459  CG1 ILE A 213      30.251 -10.790   8.620  1.00 33.77           C  
-ATOM   1460  CG2 ILE A 213      29.498  -8.752  10.089  1.00 32.73           C  
-ATOM   1461  CD1 ILE A 213      29.017 -11.620   8.878  1.00 34.29           C  
-ATOM   1462  N   ARG A 214      30.265  -6.578   7.211  1.00 37.50           N  
-ATOM   1463  CA  ARG A 214      30.312  -5.126   7.351  1.00 39.61           C  
-ATOM   1464  C   ARG A 214      29.536  -4.398   6.242  1.00 40.71           C  
-ATOM   1465  O   ARG A 214      28.830  -3.490   6.560  1.00 42.68           O  
-ATOM   1466  CB  ARG A 214      31.736  -4.642   7.254  1.00 41.30           C  
-ATOM   1467  CG  ARG A 214      32.555  -5.012   8.462  1.00 48.46           C  
-ATOM   1468  CD  ARG A 214      34.013  -4.556   8.294  1.00 58.35           C  
-ATOM   1469  NE  ARG A 214      34.213  -3.255   8.916  1.00 68.10           N  
-ATOM   1470  CZ  ARG A 214      35.214  -2.436   8.603  1.00 75.02           C  
-ATOM   1471  NH1 ARG A 214      36.100  -2.793   7.661  1.00 77.35           N  
-ATOM   1472  NH2 ARG A 214      35.328  -1.245   9.206  1.00 75.61           N  
-ATOM   1473  N   TYR A 215      29.660  -4.788   4.962  1.00 39.37           N  
-ATOM   1474  CA  TYR A 215      29.210  -3.997   3.803  1.00 38.81           C  
-ATOM   1475  C   TYR A 215      28.181  -4.686   2.929  1.00 38.22           C  
-ATOM   1476  O   TYR A 215      27.716  -4.124   1.913  1.00 37.59           O  
-ATOM   1477  CB  TYR A 215      30.379  -3.728   2.939  1.00 40.00           C  
-ATOM   1478  CG  TYR A 215      31.502  -3.108   3.699  1.00 44.33           C  
-ATOM   1479  CD1 TYR A 215      31.334  -1.871   4.338  1.00 47.59           C  
-ATOM   1480  CD2 TYR A 215      32.770  -3.714   3.744  1.00 45.27           C  
-ATOM   1481  CE1 TYR A 215      32.396  -1.264   5.033  1.00 49.39           C  
-ATOM   1482  CE2 TYR A 215      33.840  -3.128   4.467  1.00 47.34           C  
-ATOM   1483  CZ  TYR A 215      33.634  -1.910   5.094  1.00 49.06           C  
-ATOM   1484  OH  TYR A 215      34.688  -1.328   5.780  1.00 52.33           O  
-ATOM   1485  N   HIS A 216      27.851  -5.911   3.282  1.00 35.56           N  
-ATOM   1486  CA  HIS A 216      27.023  -6.655   2.417  1.00 37.76           C  
-ATOM   1487  C   HIS A 216      27.516  -6.731   0.952  1.00 36.07           C  
-ATOM   1488  O   HIS A 216      26.731  -6.604  -0.009  1.00 36.66           O  
-ATOM   1489  CB  HIS A 216      25.596  -6.078   2.576  1.00 39.21           C  
-ATOM   1490  CG  HIS A 216      24.916  -6.643   3.768  1.00 48.72           C  
-ATOM   1491  ND1 HIS A 216      23.568  -6.925   3.799  1.00 55.53           N  
-ATOM   1492  CD2 HIS A 216      25.431  -7.090   4.947  1.00 53.76           C  
-ATOM   1493  CE1 HIS A 216      23.282  -7.497   4.961  1.00 59.76           C  
-ATOM   1494  NE2 HIS A 216      24.397  -7.621   5.668  1.00 57.84           N  
-ATOM   1495  N   ARG A 217      28.834  -6.878   0.741  1.00 34.36           N  
-ATOM   1496  CA  ARG A 217      29.344  -7.018  -0.601  1.00 34.09           C  
-ATOM   1497  C   ARG A 217      30.502  -7.964  -0.489  1.00 33.19           C  
-ATOM   1498  O   ARG A 217      31.273  -7.884   0.477  1.00 29.91           O  
-ATOM   1499  CB  ARG A 217      29.942  -5.669  -1.028  1.00 32.32           C  
-ATOM   1500  CG  ARG A 217      28.829  -4.608  -1.164  1.00 40.11           C  
-ATOM   1501  CD  ARG A 217      29.436  -3.143  -1.156  1.00 42.87           C  
-ATOM   1502  NE  ARG A 217      30.375  -3.008  -2.275  1.00 50.59           N  
-ATOM   1503  CZ  ARG A 217      30.022  -2.741  -3.537  1.00 55.47           C  
-ATOM   1504  NH1 ARG A 217      28.713  -2.568  -3.884  1.00 51.41           N  
-ATOM   1505  NH2 ARG A 217      31.004  -2.688  -4.459  1.00 55.34           N  
-ATOM   1506  N   TYR A 218      30.698  -8.799  -1.497  1.00 30.45           N  
-ATOM   1507  CA  TYR A 218      31.943  -9.641  -1.534  1.00 29.48           C  
-ATOM   1508  C   TYR A 218      32.187 -10.028  -3.021  1.00 28.03           C  
-ATOM   1509  O   TYR A 218      31.292  -9.893  -3.867  1.00 29.39           O  
-ATOM   1510  CB  TYR A 218      31.775 -10.884  -0.662  1.00 28.41           C  
-ATOM   1511  CG  TYR A 218      30.590 -11.695  -1.054  1.00 30.49           C  
-ATOM   1512  CD1 TYR A 218      29.300 -11.346  -0.577  1.00 30.51           C  
-ATOM   1513  CD2 TYR A 218      30.716 -12.829  -1.920  1.00 27.99           C  
-ATOM   1514  CE1 TYR A 218      28.198 -12.095  -0.853  1.00 31.20           C  
-ATOM   1515  CE2 TYR A 218      29.561 -13.564  -2.285  1.00 26.32           C  
-ATOM   1516  CZ  TYR A 218      28.313 -13.179  -1.798  1.00 32.60           C  
-ATOM   1517  OH  TYR A 218      27.177 -13.952  -2.103  1.00 31.16           O  
-ATOM   1518  N   HIS A 219      33.397 -10.473  -3.330  1.00 27.40           N  
-ATOM   1519  CA  HIS A 219      33.691 -11.062  -4.616  1.00 27.69           C  
-ATOM   1520  C   HIS A 219      33.746 -12.582  -4.389  1.00 27.95           C  
-ATOM   1521  O   HIS A 219      34.016 -13.057  -3.281  1.00 25.79           O  
-ATOM   1522  CB  HIS A 219      35.005 -10.531  -5.138  1.00 28.43           C  
-ATOM   1523  CG  HIS A 219      34.861  -9.139  -5.726  1.00 30.38           C  
-ATOM   1524  ND1 HIS A 219      34.864  -8.012  -4.943  1.00 31.84           N  
-ATOM   1525  CD2 HIS A 219      34.616  -8.722  -6.988  1.00 31.00           C  
-ATOM   1526  CE1 HIS A 219      34.645  -6.941  -5.699  1.00 39.00           C  
-ATOM   1527  NE2 HIS A 219      34.485  -7.342  -6.947  1.00 35.03           N  
-ATOM   1528  N   GLY A 220      33.521 -13.302  -5.449  1.00 26.43           N  
-ATOM   1529  CA  GLY A 220      33.224 -14.768  -5.380  1.00 26.49           C  
-ATOM   1530  C   GLY A 220      34.412 -15.542  -4.835  1.00 24.92           C  
-ATOM   1531  O   GLY A 220      34.304 -16.212  -3.829  1.00 23.46           O  
-ATOM   1532  N   ARG A 221      35.544 -15.403  -5.510  1.00 23.30           N  
-ATOM   1533  CA  ARG A 221      36.722 -16.256  -5.201  1.00 28.19           C  
-ATOM   1534  C   ARG A 221      37.255 -15.938  -3.822  1.00 27.80           C  
-ATOM   1535  O   ARG A 221      37.497 -16.840  -3.084  1.00 24.48           O  
-ATOM   1536  CB  ARG A 221      37.750 -15.999  -6.264  1.00 26.84           C  
-ATOM   1537  CG  ARG A 221      37.211 -16.432  -7.742  1.00 33.60           C  
-ATOM   1538  CD  ARG A 221      38.117 -15.783  -8.962  1.00 34.93           C  
-ATOM   1539  NE  ARG A 221      37.632 -16.061 -10.326  1.00 39.54           N  
-ATOM   1540  CZ  ARG A 221      36.644 -15.380 -10.922  1.00 46.20           C  
-ATOM   1541  NH1 ARG A 221      36.014 -14.446 -10.213  1.00 47.27           N  
-ATOM   1542  NH2 ARG A 221      36.334 -15.593 -12.226  1.00 36.95           N  
-ATOM   1543  N   SER A 222      37.481 -14.648  -3.455  1.00 24.39           N  
-ATOM   1544  CA  SER A 222      38.019 -14.407  -2.145  1.00 24.93           C  
-ATOM   1545  C   SER A 222      37.039 -14.706  -1.022  1.00 23.57           C  
-ATOM   1546  O   SER A 222      37.431 -15.047   0.103  1.00 23.11           O  
-ATOM   1547  CB  SER A 222      38.516 -12.922  -2.071  1.00 29.88           C  
-ATOM   1548  OG  SER A 222      37.434 -12.092  -2.464  1.00 26.74           O  
-ATOM   1549  N   ALA A 223      35.730 -14.641  -1.245  1.00 23.74           N  
-ATOM   1550  CA  ALA A 223      34.796 -15.082  -0.201  1.00 23.31           C  
-ATOM   1551  C   ALA A 223      34.924 -16.639  -0.083  1.00 21.83           C  
-ATOM   1552  O   ALA A 223      34.846 -17.156   1.047  1.00 24.55           O  
-ATOM   1553  CB  ALA A 223      33.374 -14.779  -0.578  1.00 23.72           C  
-ATOM   1554  N   ALA A 224      35.097 -17.344  -1.222  1.00 23.56           N  
-ATOM   1555  CA  ALA A 224      35.254 -18.838  -1.262  1.00 21.36           C  
-ATOM   1556  C   ALA A 224      36.506 -19.152  -0.373  1.00 22.00           C  
-ATOM   1557  O   ALA A 224      36.468 -20.019   0.438  1.00 21.52           O  
-ATOM   1558  CB  ALA A 224      35.456 -19.325  -2.653  1.00 21.37           C  
-ATOM   1559  N   VAL A 225      37.569 -18.414  -0.553  1.00 20.82           N  
-ATOM   1560  CA  VAL A 225      38.823 -18.715   0.111  1.00 19.04           C  
-ATOM   1561  C   VAL A 225      38.642 -18.446   1.603  1.00 20.90           C  
-ATOM   1562  O   VAL A 225      39.084 -19.220   2.373  1.00 20.75           O  
-ATOM   1563  CB  VAL A 225      40.031 -17.857  -0.502  1.00 19.35           C  
-ATOM   1564  CG1 VAL A 225      41.225 -17.949   0.490  1.00 20.11           C  
-ATOM   1565  CG2 VAL A 225      40.398 -18.399  -1.972  1.00 19.52           C  
-ATOM   1566  N   TRP A 226      37.927 -17.375   2.052  1.00 21.33           N  
-ATOM   1567  CA  TRP A 226      37.634 -17.201   3.493  1.00 21.45           C  
-ATOM   1568  C   TRP A 226      36.945 -18.430   4.009  1.00 21.39           C  
-ATOM   1569  O   TRP A 226      37.236 -18.919   5.118  1.00 22.43           O  
-ATOM   1570  CB  TRP A 226      36.662 -15.969   3.720  1.00 22.84           C  
-ATOM   1571  CG  TRP A 226      36.343 -15.776   5.137  1.00 22.26           C  
-ATOM   1572  CD1 TRP A 226      35.298 -16.341   5.845  1.00 27.26           C  
-ATOM   1573  CD2 TRP A 226      37.032 -14.940   6.005  1.00 25.55           C  
-ATOM   1574  NE1 TRP A 226      35.324 -15.911   7.150  1.00 28.12           N  
-ATOM   1575  CE2 TRP A 226      36.373 -15.007   7.262  1.00 26.00           C  
-ATOM   1576  CE3 TRP A 226      38.133 -14.076   5.849  1.00 23.21           C  
-ATOM   1577  CZ2 TRP A 226      36.809 -14.310   8.365  1.00 26.62           C  
-ATOM   1578  CZ3 TRP A 226      38.558 -13.336   7.018  1.00 26.74           C  
-ATOM   1579  CH2 TRP A 226      37.916 -13.524   8.224  1.00 27.34           C  
-ATOM   1580  N   SER A 227      35.905 -18.879   3.317  1.00 19.60           N  
-ATOM   1581  CA  SER A 227      35.212 -20.031   3.865  1.00 19.39           C  
-ATOM   1582  C   SER A 227      36.112 -21.238   3.927  1.00 20.14           C  
-ATOM   1583  O   SER A 227      35.971 -22.083   4.864  1.00 21.35           O  
-ATOM   1584  CB  SER A 227      33.922 -20.291   3.052  1.00 21.24           C  
-ATOM   1585  OG  SER A 227      34.256 -20.809   1.744  1.00 23.90           O  
-ATOM   1586  N   LEU A 228      37.012 -21.391   2.956  1.00 21.45           N  
-ATOM   1587  CA  LEU A 228      37.995 -22.574   2.966  1.00 21.75           C  
-ATOM   1588  C   LEU A 228      38.869 -22.466   4.234  1.00 21.27           C  
-ATOM   1589  O   LEU A 228      39.250 -23.479   4.856  1.00 21.01           O  
-ATOM   1590  CB  LEU A 228      38.918 -22.558   1.729  1.00 20.39           C  
-ATOM   1591  CG  LEU A 228      37.963 -23.079   0.528  1.00 20.32           C  
-ATOM   1592  CD1 LEU A 228      38.670 -22.765  -0.840  1.00 25.25           C  
-ATOM   1593  CD2 LEU A 228      37.563 -24.573   0.656  1.00 21.62           C  
-ATOM   1594  N   GLY A 229      39.219 -21.249   4.606  1.00 19.21           N  
-ATOM   1595  CA  GLY A 229      40.037 -21.022   5.880  1.00 19.93           C  
-ATOM   1596  C   GLY A 229      39.214 -21.401   7.131  1.00 21.66           C  
-ATOM   1597  O   GLY A 229      39.744 -22.009   8.075  1.00 20.79           O  
-ATOM   1598  N   ILE A 230      37.885 -21.094   7.167  1.00 20.05           N  
-ATOM   1599  CA  ILE A 230      37.086 -21.456   8.318  1.00 19.41           C  
-ATOM   1600  C   ILE A 230      37.010 -23.013   8.292  1.00 20.85           C  
-ATOM   1601  O   ILE A 230      37.138 -23.651   9.349  1.00 20.61           O  
-ATOM   1602  CB  ILE A 230      35.594 -20.933   8.104  1.00 18.52           C  
-ATOM   1603  CG1 ILE A 230      35.611 -19.370   8.032  1.00 18.50           C  
-ATOM   1604  CG2 ILE A 230      34.667 -21.400   9.277  1.00 19.60           C  
-ATOM   1605  CD1 ILE A 230      36.214 -18.668   9.354  1.00 21.01           C  
-ATOM   1606  N   LEU A 231      36.857 -23.592   7.091  1.00 21.63           N  
-ATOM   1607  CA  LEU A 231      36.756 -25.088   7.003  1.00 20.40           C  
-ATOM   1608  C   LEU A 231      38.042 -25.740   7.459  1.00 22.51           C  
-ATOM   1609  O   LEU A 231      37.999 -26.778   8.122  1.00 22.01           O  
-ATOM   1610  CB  LEU A 231      36.544 -25.439   5.541  1.00 19.97           C  
-ATOM   1611  CG  LEU A 231      36.442 -26.962   5.307  1.00 21.52           C  
-ATOM   1612  CD1 LEU A 231      35.311 -27.621   6.089  1.00 26.40           C  
-ATOM   1613  CD2 LEU A 231      36.396 -27.250   3.827  1.00 20.28           C  
-ATOM   1614  N   LEU A 232      39.221 -25.190   7.080  1.00 20.70           N  
-ATOM   1615  CA  LEU A 232      40.438 -25.934   7.419  1.00 21.20           C  
-ATOM   1616  C   LEU A 232      40.573 -25.751   8.929  1.00 23.42           C  
-ATOM   1617  O   LEU A 232      40.978 -26.693   9.581  1.00 22.27           O  
-ATOM   1618  CB  LEU A 232      41.673 -25.305   6.758  1.00 21.92           C  
-ATOM   1619  CG  LEU A 232      43.083 -25.836   7.113  1.00 18.92           C  
-ATOM   1620  CD1 LEU A 232      43.005 -27.503   6.921  1.00 19.32           C  
-ATOM   1621  CD2 LEU A 232      44.109 -25.142   6.096  1.00 21.78           C  
-ATOM   1622  N   TYR A 233      40.329 -24.543   9.513  1.00 20.30           N  
-ATOM   1623  CA  TYR A 233      40.329 -24.441  10.993  1.00 19.08           C  
-ATOM   1624  C   TYR A 233      39.468 -25.494  11.623  1.00 22.70           C  
-ATOM   1625  O   TYR A 233      39.839 -26.166  12.591  1.00 24.07           O  
-ATOM   1626  CB  TYR A 233      39.948 -22.980  11.477  1.00 20.97           C  
-ATOM   1627  CG  TYR A 233      40.083 -22.732  13.009  1.00 20.95           C  
-ATOM   1628  CD1 TYR A 233      39.102 -23.243  13.922  1.00 25.13           C  
-ATOM   1629  CD2 TYR A 233      41.240 -22.070  13.534  1.00 23.74           C  
-ATOM   1630  CE1 TYR A 233      39.253 -23.038  15.297  1.00 28.17           C  
-ATOM   1631  CE2 TYR A 233      41.347 -21.837  14.948  1.00 24.96           C  
-ATOM   1632  CZ  TYR A 233      40.397 -22.351  15.765  1.00 25.18           C  
-ATOM   1633  OH  TYR A 233      40.457 -22.213  17.152  1.00 29.28           O  
-ATOM   1634  N   ASP A 234      38.262 -25.623  11.113  1.00 23.89           N  
-ATOM   1635  CA  ASP A 234      37.324 -26.561  11.701  1.00 25.49           C  
-ATOM   1636  C   ASP A 234      37.857 -27.954  11.662  1.00 25.42           C  
-ATOM   1637  O   ASP A 234      37.714 -28.684  12.676  1.00 25.35           O  
-ATOM   1638  CB  ASP A 234      35.998 -26.401  10.917  1.00 22.26           C  
-ATOM   1639  CG  ASP A 234      34.890 -27.359  11.365  1.00 30.82           C  
-ATOM   1640  OD1 ASP A 234      34.570 -27.443  12.583  1.00 26.64           O  
-ATOM   1641  OD2 ASP A 234      34.309 -27.973  10.428  1.00 31.57           O  
-ATOM   1642  N   MET A 235      38.582 -28.345  10.586  1.00 23.97           N  
-ATOM   1643  CA  MET A 235      39.055 -29.676  10.528  1.00 25.18           C  
-ATOM   1644  C   MET A 235      40.161 -29.896  11.563  1.00 25.17           C  
-ATOM   1645  O   MET A 235      40.200 -30.960  12.200  1.00 26.91           O  
-ATOM   1646  CB  MET A 235      39.667 -30.007   9.120  1.00 25.74           C  
-ATOM   1647  CG  MET A 235      38.508 -30.142   7.990  1.00 27.57           C  
-ATOM   1648  SD  MET A 235      39.409 -30.564   6.466  1.00 32.94           S  
-ATOM   1649  CE  MET A 235      38.363 -30.178   5.059  1.00 29.18           C  
-ATOM   1650  N   VAL A 236      41.101 -28.953  11.703  1.00 23.33           N  
-ATOM   1651  CA  VAL A 236      42.305 -29.236  12.520  1.00 22.59           C  
-ATOM   1652  C   VAL A 236      42.007 -28.897  14.008  1.00 24.86           C  
-ATOM   1653  O   VAL A 236      42.771 -29.249  14.900  1.00 25.84           O  
-ATOM   1654  CB  VAL A 236      43.581 -28.542  11.957  1.00 25.10           C  
-ATOM   1655  CG1 VAL A 236      43.953 -29.148  10.544  1.00 21.03           C  
-ATOM   1656  CG2 VAL A 236      43.487 -26.922  11.943  1.00 22.76           C  
-ATOM   1657  N   CYS A 237      40.978 -28.065  14.283  1.00 23.10           N  
-ATOM   1658  CA  CYS A 237      40.692 -27.708  15.666  1.00 25.18           C  
-ATOM   1659  C   CYS A 237      39.395 -28.368  16.162  1.00 28.23           C  
-ATOM   1660  O   CYS A 237      39.173 -28.399  17.393  1.00 28.79           O  
-ATOM   1661  CB  CYS A 237      40.554 -26.195  15.834  1.00 23.04           C  
-ATOM   1662  SG  CYS A 237      42.100 -25.365  15.688  1.00 31.24           S  
-ATOM   1663  N   GLY A 238      38.567 -28.868  15.250  1.00 26.40           N  
-ATOM   1664  CA  GLY A 238      37.370 -29.631  15.643  1.00 29.85           C  
-ATOM   1665  C   GLY A 238      36.154 -28.732  15.867  1.00 31.21           C  
-ATOM   1666  O   GLY A 238      35.106 -29.222  16.293  1.00 33.63           O  
-ATOM   1667  N   ASP A 239      36.270 -27.429  15.574  1.00 29.50           N  
-ATOM   1668  CA  ASP A 239      35.177 -26.455  15.669  1.00 31.76           C  
-ATOM   1669  C   ASP A 239      35.541 -25.230  14.852  1.00 30.05           C  
-ATOM   1670  O   ASP A 239      36.730 -24.958  14.608  1.00 27.37           O  
-ATOM   1671  CB  ASP A 239      34.910 -25.981  17.081  1.00 34.65           C  
-ATOM   1672  CG  ASP A 239      33.848 -26.829  17.743  1.00 47.06           C  
-ATOM   1673  OD1 ASP A 239      32.640 -26.759  17.313  1.00 52.18           O  
-ATOM   1674  OD2 ASP A 239      34.244 -27.640  18.654  1.00 53.23           O  
-ATOM   1675  N   ILE A 240      34.550 -24.425  14.458  1.00 29.16           N  
-ATOM   1676  CA  ILE A 240      34.859 -23.218  13.712  1.00 29.28           C  
-ATOM   1677  C   ILE A 240      35.486 -22.104  14.591  1.00 29.64           C  
-ATOM   1678  O   ILE A 240      35.311 -22.127  15.820  1.00 30.87           O  
-ATOM   1679  CB  ILE A 240      33.565 -22.710  12.985  1.00 28.70           C  
-ATOM   1680  CG1 ILE A 240      32.453 -22.484  14.022  1.00 28.80           C  
-ATOM   1681  CG2 ILE A 240      33.067 -23.753  12.025  1.00 30.42           C  
-ATOM   1682  CD1 ILE A 240      31.155 -21.723  13.458  1.00 34.32           C  
-ATOM   1683  N   PRO A 241      36.224 -21.149  13.997  1.00 27.37           N  
-ATOM   1684  CA  PRO A 241      36.895 -20.194  14.891  1.00 26.76           C  
-ATOM   1685  C   PRO A 241      36.058 -19.014  15.409  1.00 30.23           C  
-ATOM   1686  O   PRO A 241      36.431 -18.502  16.448  1.00 30.98           O  
-ATOM   1687  CB  PRO A 241      38.089 -19.670  14.053  1.00 25.35           C  
-ATOM   1688  CG  PRO A 241      37.552 -19.679  12.576  1.00 26.12           C  
-ATOM   1689  CD  PRO A 241      36.540 -20.891  12.561  1.00 25.27           C  
-ATOM   1690  N   PHE A 242      34.972 -18.625  14.708  1.00 29.79           N  
-ATOM   1691  CA  PHE A 242      34.219 -17.378  14.997  1.00 30.16           C  
-ATOM   1692  C   PHE A 242      32.773 -17.785  15.182  1.00 32.46           C  
-ATOM   1693  O   PHE A 242      32.309 -18.568  14.441  1.00 33.22           O  
-ATOM   1694  CB  PHE A 242      34.331 -16.370  13.886  1.00 27.38           C  
-ATOM   1695  CG  PHE A 242      35.732 -16.076  13.484  1.00 26.67           C  
-ATOM   1696  CD1 PHE A 242      36.752 -15.818  14.462  1.00 29.59           C  
-ATOM   1697  CD2 PHE A 242      36.078 -16.126  12.102  1.00 27.62           C  
-ATOM   1698  CE1 PHE A 242      38.098 -15.496  14.027  1.00 27.79           C  
-ATOM   1699  CE2 PHE A 242      37.422 -15.802  11.632  1.00 27.49           C  
-ATOM   1700  CZ  PHE A 242      38.423 -15.531  12.620  1.00 27.79           C  
-ATOM   1701  N   GLU A 243      32.121 -17.355  16.272  1.00 36.56           N  
-ATOM   1702  CA  GLU A 243      30.666 -17.437  16.361  1.00 39.97           C  
-ATOM   1703  C   GLU A 243      29.973 -16.080  16.143  1.00 39.54           C  
-ATOM   1704  O   GLU A 243      28.948 -16.010  15.487  1.00 41.98           O  
-ATOM   1705  CB  GLU A 243      30.288 -18.001  17.701  1.00 42.14           C  
-ATOM   1706  CG  GLU A 243      30.834 -19.407  17.930  1.00 52.79           C  
-ATOM   1707  CD  GLU A 243      30.001 -20.503  17.221  1.00 64.90           C  
-ATOM   1708  OE1 GLU A 243      28.846 -20.208  16.767  1.00 69.07           O  
-ATOM   1709  OE2 GLU A 243      30.503 -21.658  17.132  1.00 67.52           O  
-ATOM   1710  N   HIS A 244      30.538 -14.989  16.604  1.00 38.24           N  
-ATOM   1711  CA  HIS A 244      29.817 -13.684  16.556  1.00 37.76           C  
-ATOM   1712  C   HIS A 244      30.344 -12.813  15.427  1.00 35.78           C  
-ATOM   1713  O   HIS A 244      31.536 -12.947  14.989  1.00 31.05           O  
-ATOM   1714  CB  HIS A 244      29.904 -13.010  17.958  1.00 38.56           C  
-ATOM   1715  CG  HIS A 244      29.311 -13.895  19.020  1.00 47.13           C  
-ATOM   1716  ND1 HIS A 244      30.035 -14.393  20.085  1.00 53.00           N  
-ATOM   1717  CD2 HIS A 244      28.089 -14.482  19.093  1.00 51.24           C  
-ATOM   1718  CE1 HIS A 244      29.262 -15.192  20.807  1.00 55.25           C  
-ATOM   1719  NE2 HIS A 244      28.086 -15.286  20.210  1.00 54.47           N  
-ATOM   1720  N   ASP A 245      29.475 -11.941  14.926  1.00 33.38           N  
-ATOM   1721  CA  ASP A 245      29.864 -11.000  13.894  1.00 34.80           C  
-ATOM   1722  C   ASP A 245      31.122 -10.250  14.309  1.00 34.85           C  
-ATOM   1723  O   ASP A 245      31.993  -9.943  13.515  1.00 32.63           O  
-ATOM   1724  CB  ASP A 245      28.735  -9.966  13.753  1.00 35.46           C  
-ATOM   1725  CG  ASP A 245      27.547 -10.489  12.918  1.00 39.80           C  
-ATOM   1726  OD1 ASP A 245      27.405 -11.749  12.611  1.00 38.51           O  
-ATOM   1727  OD2 ASP A 245      26.732  -9.597  12.554  1.00 44.59           O  
-ATOM   1728  N   GLU A 246      31.218  -9.912  15.600  1.00 35.20           N  
-ATOM   1729  CA  GLU A 246      32.347  -9.063  16.035  1.00 35.54           C  
-ATOM   1730  C   GLU A 246      33.662  -9.857  15.857  1.00 32.96           C  
-ATOM   1731  O   GLU A 246      34.668  -9.313  15.539  1.00 33.12           O  
-ATOM   1732  CB  GLU A 246      32.176  -8.725  17.557  1.00 36.78           C  
-ATOM   1733  CG  GLU A 246      30.764  -8.066  17.892  1.00 46.59           C  
-ATOM   1734  CD  GLU A 246      29.486  -8.993  17.638  1.00 58.06           C  
-ATOM   1735  OE1 GLU A 246      29.483 -10.219  17.906  1.00 59.42           O  
-ATOM   1736  OE2 GLU A 246      28.439  -8.444  17.201  1.00 65.92           O  
-ATOM   1737  N   GLU A 247      33.613 -11.154  16.175  1.00 31.82           N  
-ATOM   1738  C   GLU A 247      35.178 -12.127  14.545  1.00 30.03           C  
-ATOM   1739  O   GLU A 247      36.365 -12.107  14.176  1.00 28.18           O  
-ATOM   1740  CA AGLU A 247      34.809 -12.009  16.021  0.50 31.10           C  
-ATOM   1741  CB AGLU A 247      34.539 -13.382  16.605  0.50 30.17           C  
-ATOM   1742  CG AGLU A 247      34.463 -13.423  18.121  0.50 30.88           C  
-ATOM   1743  CD AGLU A 247      33.567 -14.539  18.593  0.50 33.46           C  
-ATOM   1744  OE1AGLU A 247      32.827 -15.115  17.771  0.50 33.78           O  
-ATOM   1745  OE2AGLU A 247      33.606 -14.874  19.792  0.50 31.49           O  
-ATOM   1746  CA BGLU A 247      34.784 -12.037  16.017  0.50 30.91           C  
-ATOM   1747  CB BGLU A 247      34.409 -13.420  16.492  0.50 29.71           C  
-ATOM   1748  CG BGLU A 247      34.477 -13.664  17.969  0.50 29.77           C  
-ATOM   1749  CD BGLU A 247      34.468 -15.135  18.198  0.50 30.16           C  
-ATOM   1750  OE1BGLU A 247      33.360 -15.741  18.198  0.50 30.16           O  
-ATOM   1751  OE2BGLU A 247      35.578 -15.704  18.246  0.50 30.76           O  
-ATOM   1752  N   ILE A 248      34.162 -12.263  13.661  1.00 29.34           N  
-ATOM   1753  CA  ILE A 248      34.445 -12.314  12.189  1.00 28.96           C  
-ATOM   1754  C   ILE A 248      35.177 -11.069  11.735  1.00 31.47           C  
-ATOM   1755  O   ILE A 248      36.228 -11.112  11.087  1.00 29.21           O  
-ATOM   1756  CB  ILE A 248      33.167 -12.567  11.348  1.00 29.87           C  
-ATOM   1757  CG1 ILE A 248      32.617 -13.935  11.704  1.00 24.74           C  
-ATOM   1758  CG2 ILE A 248      33.490 -12.433   9.834  1.00 29.11           C  
-ATOM   1759  CD1 ILE A 248      31.161 -14.255  11.337  1.00 31.00           C  
-ATOM   1760  N   ILE A 249      34.632  -9.887  12.114  1.00 30.36           N  
-ATOM   1761  CA  ILE A 249      35.188  -8.636  11.637  1.00 33.25           C  
-ATOM   1762  C   ILE A 249      36.562  -8.371  12.218  1.00 31.60           C  
-ATOM   1763  O   ILE A 249      37.385  -7.742  11.540  1.00 34.03           O  
-ATOM   1764  CB  ILE A 249      34.226  -7.440  12.058  1.00 33.88           C  
-ATOM   1765  CG1 ILE A 249      32.939  -7.503  11.243  1.00 35.16           C  
-ATOM   1766  CG2 ILE A 249      34.926  -6.072  11.823  1.00 40.10           C  
-ATOM   1767  CD1 ILE A 249      31.880  -6.463  11.829  1.00 41.06           C  
-ATOM   1768  N   ARG A 250      36.808  -8.791  13.482  1.00 30.81           N  
-ATOM   1769  CA  ARG A 250      38.170  -8.604  14.035  1.00 31.65           C  
-ATOM   1770  C   ARG A 250      39.162  -9.609  13.361  1.00 32.37           C  
-ATOM   1771  O   ARG A 250      40.311  -9.235  13.049  1.00 32.71           O  
-ATOM   1772  CB  ARG A 250      38.174  -8.787  15.557  1.00 30.07           C  
-ATOM   1773  CG  ARG A 250      39.620  -8.591  16.182  1.00 29.41           C  
-ATOM   1774  CD  ARG A 250      39.431  -8.373  17.697  1.00 35.20           C  
-ATOM   1775  NE  ARG A 250      40.789  -8.309  18.349  1.00 33.41           N  
-ATOM   1776  CZ  ARG A 250      41.329  -9.247  19.117  1.00 34.90           C  
-ATOM   1777  NH1 ARG A 250      40.667 -10.409  19.359  1.00 27.60           N  
-ATOM   1778  NH2 ARG A 250      42.576  -9.018  19.554  1.00 35.23           N  
-ATOM   1779  N   GLY A 251      38.689 -10.843  13.059  1.00 33.51           N  
-ATOM   1780  CA  GLY A 251      39.551 -11.722  12.224  1.00 31.37           C  
-ATOM   1781  C   GLY A 251      40.761 -12.306  13.005  1.00 31.45           C  
-ATOM   1782  O   GLY A 251      41.738 -12.792  12.366  1.00 32.02           O  
-ATOM   1783  N   GLN A 252      40.706 -12.358  14.354  1.00 31.16           N  
-ATOM   1784  CA  GLN A 252      41.923 -12.732  15.146  1.00 30.03           C  
-ATOM   1785  C   GLN A 252      41.765 -14.213  15.355  1.00 30.47           C  
-ATOM   1786  O   GLN A 252      40.785 -14.622  15.947  1.00 32.64           O  
-ATOM   1787  CB  GLN A 252      41.908 -12.130  16.539  1.00 29.70           C  
-ATOM   1788  CG  GLN A 252      43.117 -12.567  17.403  1.00 34.29           C  
-ATOM   1789  CD  GLN A 252      44.449 -12.201  16.758  1.00 38.00           C  
-ATOM   1790  OE1 GLN A 252      44.609 -11.061  16.222  1.00 42.18           O  
-ATOM   1791  NE2 GLN A 252      45.408 -13.146  16.774  1.00 33.44           N  
-ATOM   1792  N   VAL A 253      42.696 -15.023  14.933  1.00 27.69           N  
-ATOM   1793  CA  VAL A 253      42.491 -16.486  15.055  1.00 28.02           C  
-ATOM   1794  C   VAL A 253      43.227 -17.032  16.270  1.00 26.37           C  
-ATOM   1795  O   VAL A 253      44.405 -16.782  16.346  1.00 27.17           O  
-ATOM   1796  CB  VAL A 253      43.133 -17.132  13.705  1.00 26.97           C  
-ATOM   1797  CG1 VAL A 253      43.073 -18.699  13.702  1.00 26.68           C  
-ATOM   1798  CG2 VAL A 253      42.419 -16.592  12.406  1.00 28.28           C  
-ATOM   1799  N   PHE A 254      42.605 -17.806  17.162  1.00 25.86           N  
-ATOM   1800  CA  PHE A 254      43.246 -18.425  18.304  1.00 27.91           C  
-ATOM   1801  C   PHE A 254      43.173 -19.942  18.042  1.00 28.98           C  
-ATOM   1802  O   PHE A 254      42.058 -20.501  17.754  1.00 28.45           O  
-ATOM   1803  CB  PHE A 254      42.438 -18.089  19.583  1.00 28.72           C  
-ATOM   1804  CG  PHE A 254      42.806 -18.949  20.765  1.00 32.21           C  
-ATOM   1805  CD1 PHE A 254      43.970 -18.655  21.565  1.00 33.32           C  
-ATOM   1806  CD2 PHE A 254      42.008 -20.075  21.104  1.00 30.22           C  
-ATOM   1807  CE1 PHE A 254      44.323 -19.536  22.727  1.00 24.56           C  
-ATOM   1808  CE2 PHE A 254      42.362 -20.954  22.242  1.00 31.72           C  
-ATOM   1809  CZ  PHE A 254      43.539 -20.651  23.017  1.00 34.00           C  
-ATOM   1810  N   PHE A 255      44.332 -20.600  18.126  1.00 29.77           N  
-ATOM   1811  CA  PHE A 255      44.370 -22.075  18.003  1.00 31.00           C  
-ATOM   1812  C   PHE A 255      44.167 -22.710  19.344  1.00 31.59           C  
-ATOM   1813  O   PHE A 255      44.874 -22.435  20.291  1.00 35.07           O  
-ATOM   1814  CB  PHE A 255      45.598 -22.544  17.268  1.00 28.75           C  
-ATOM   1815  CG  PHE A 255      45.514 -22.268  15.845  1.00 30.14           C  
-ATOM   1816  CD1 PHE A 255      45.840 -21.028  15.330  1.00 25.75           C  
-ATOM   1817  CD2 PHE A 255      44.949 -23.224  14.989  1.00 27.52           C  
-ATOM   1818  CE1 PHE A 255      45.658 -20.750  13.892  1.00 24.74           C  
-ATOM   1819  CE2 PHE A 255      44.838 -22.986  13.624  1.00 22.77           C  
-ATOM   1820  CZ  PHE A 255      45.136 -21.720  13.058  1.00 29.33           C  
-ATOM   1821  N   ARG A 256      43.103 -23.516  19.426  1.00 33.11           N  
-ATOM   1822  CA  ARG A 256      42.692 -24.127  20.665  1.00 34.58           C  
-ATOM   1823  C   ARG A 256      43.254 -25.583  20.787  1.00 34.72           C  
-ATOM   1824  O   ARG A 256      43.203 -26.170  21.910  1.00 35.38           O  
-ATOM   1825  CB  ARG A 256      41.150 -24.203  20.690  1.00 36.35           C  
-ATOM   1826  CG  ARG A 256      40.515 -24.851  19.436  1.00 35.01           C  
-ATOM   1827  CD  ARG A 256      38.936 -24.654  19.447  1.00 38.74           C  
-ATOM   1828  NE  ARG A 256      38.524 -23.363  18.854  1.00 46.04           N  
-ATOM   1829  CZ  ARG A 256      37.255 -22.919  18.903  1.00 50.68           C  
-ATOM   1830  NH1 ARG A 256      36.318 -23.663  19.521  1.00 51.37           N  
-ATOM   1831  NH2 ARG A 256      36.917 -21.760  18.372  1.00 42.28           N  
-ATOM   1832  N   GLN A 257      43.825 -26.113  19.677  1.00 31.46           N  
-ATOM   1833  CA  GLN A 257      44.485 -27.451  19.632  1.00 30.89           C  
-ATOM   1834  C   GLN A 257      45.938 -27.144  19.123  1.00 26.54           C  
-ATOM   1835  O   GLN A 257      46.213 -26.140  18.542  1.00 24.28           O  
-ATOM   1836  CB  GLN A 257      43.807 -28.347  18.560  1.00 31.47           C  
-ATOM   1837  CG  GLN A 257      42.342 -28.543  18.841  1.00 41.53           C  
-ATOM   1838  CD  GLN A 257      42.149 -29.497  19.968  1.00 52.37           C  
-ATOM   1839  OE1 GLN A 257      42.972 -30.397  20.167  1.00 54.69           O  
-ATOM   1840  NE2 GLN A 257      41.081 -29.292  20.752  1.00 56.06           N  
-ATOM   1841  N   ARG A 258      46.791 -28.112  19.259  1.00 24.66           N  
-ATOM   1842  CA  ARG A 258      48.143 -28.005  18.754  1.00 23.21           C  
-ATOM   1843  C   ARG A 258      48.011 -28.213  17.255  1.00 24.03           C  
-ATOM   1844  O   ARG A 258      47.529 -29.279  16.821  1.00 24.78           O  
-ATOM   1845  CB  ARG A 258      48.938 -29.133  19.357  1.00 20.61           C  
-ATOM   1846  CG AARG A 258      50.116 -29.551  18.534  0.50 25.17           C  
-ATOM   1847  CD AARG A 258      51.150 -28.465  18.734  0.50 22.88           C  
-ATOM   1848  NE AARG A 258      52.155 -28.554  17.673  0.50 25.23           N  
-ATOM   1849  CZ AARG A 258      53.268 -27.851  17.678  0.50 23.89           C  
-ATOM   1850  NH1AARG A 258      53.543 -27.062  18.744  0.50 15.07           N  
-ATOM   1851  NH2AARG A 258      54.131 -28.039  16.671  0.50 20.47           N  
-ATOM   1852  CG BARG A 258      50.487 -28.903  19.109  0.50 19.32           C  
-ATOM   1853  CD BARG A 258      50.844 -29.291  17.569  0.50 18.97           C  
-ATOM   1854  NE BARG A 258      52.206 -28.887  17.067  0.50 18.66           N  
-ATOM   1855  CZ BARG A 258      52.716 -29.353  15.930  0.50 21.10           C  
-ATOM   1856  NH1BARG A 258      52.017 -30.218  15.186  0.50 14.70           N  
-ATOM   1857  NH2BARG A 258      53.875 -28.918  15.519  0.50 28.51           N  
-ATOM   1858  N   VAL A 259      48.444 -27.226  16.494  1.00 21.36           N  
-ATOM   1859  CA  VAL A 259      48.401 -27.282  15.051  1.00 23.73           C  
-ATOM   1860  C   VAL A 259      49.752 -26.708  14.632  1.00 23.85           C  
-ATOM   1861  O   VAL A 259      50.256 -25.687  15.245  1.00 26.47           O  
-ATOM   1862  CB  VAL A 259      47.258 -26.317  14.543  1.00 22.49           C  
-ATOM   1863  CG1 VAL A 259      47.314 -26.116  13.026  1.00 25.62           C  
-ATOM   1864  CG2 VAL A 259      45.872 -26.918  14.964  1.00 21.99           C  
-ATOM   1865  N   SER A 260      50.309 -27.269  13.546  1.00 22.12           N  
-ATOM   1866  CA  SER A 260      51.719 -26.935  13.089  1.00 23.95           C  
-ATOM   1867  C   SER A 260      51.760 -25.507  12.616  1.00 25.13           C  
-ATOM   1868  O   SER A 260      50.749 -24.968  12.223  1.00 21.70           O  
-ATOM   1869  CB  SER A 260      52.093 -27.904  11.948  1.00 23.48           C  
-ATOM   1870  OG  SER A 260      51.268 -27.618  10.806  1.00 23.91           O  
-ATOM   1871  N   SER A 261      52.922 -24.841  12.672  1.00 24.58           N  
-ATOM   1872  CA  SER A 261      52.965 -23.447  12.283  1.00 24.82           C  
-ATOM   1873  C   SER A 261      52.667 -23.295  10.827  1.00 26.95           C  
-ATOM   1874  O   SER A 261      52.169 -22.271  10.431  1.00 25.30           O  
-ATOM   1875  CB  SER A 261      54.340 -22.814  12.563  1.00 26.89           C  
-ATOM   1876  OG  SER A 261      54.616 -22.908  13.968  1.00 27.84           O  
-ATOM   1877  N   GLU A 262      52.962 -24.295  10.020  1.00 25.76           N  
-ATOM   1878  CA  GLU A 262      52.674 -24.155   8.540  1.00 30.16           C  
-ATOM   1879  C   GLU A 262      51.174 -24.140   8.323  1.00 24.48           C  
-ATOM   1880  O   GLU A 262      50.675 -23.328   7.538  1.00 24.67           O  
-ATOM   1881  CB  GLU A 262      53.275 -25.303   7.707  1.00 28.93           C  
-ATOM   1882  CG  GLU A 262      54.778 -25.240   7.484  1.00 34.66           C  
-ATOM   1883  CD  GLU A 262      55.233 -26.588   6.679  1.00 44.00           C  
-ATOM   1884  OE1 GLU A 262      54.484 -27.685   6.727  1.00 54.71           O  
-ATOM   1885  OE2 GLU A 262      56.324 -26.541   5.986  1.00 60.34           O  
-ATOM   1886  N   CYS A 263      50.482 -25.037   8.993  1.00 24.97           N  
-ATOM   1887  CA  CYS A 263      48.985 -25.060   8.890  1.00 24.07           C  
-ATOM   1888  C   CYS A 263      48.407 -23.747   9.394  1.00 24.22           C  
-ATOM   1889  O   CYS A 263      47.480 -23.175   8.755  1.00 23.65           O  
-ATOM   1890  CB  CYS A 263      48.439 -26.247   9.650  1.00 24.66           C  
-ATOM   1891  SG  CYS A 263      46.684 -26.473   9.432  1.00 27.65           S  
-ATOM   1892  N   GLN A 264      48.885 -23.247  10.564  1.00 23.67           N  
-ATOM   1893  CA  GLN A 264      48.364 -22.008  11.138  1.00 22.73           C  
-ATOM   1894  C   GLN A 264      48.571 -20.884  10.146  1.00 23.69           C  
-ATOM   1895  O   GLN A 264      47.681 -20.068   9.967  1.00 25.71           O  
-ATOM   1896  CB  GLN A 264      49.153 -21.685  12.430  1.00 24.62           C  
-ATOM   1897  CG  GLN A 264      48.781 -22.588  13.647  1.00 22.29           C  
-ATOM   1898  CD  GLN A 264      49.184 -21.937  14.942  1.00 27.76           C  
-ATOM   1899  OE1 GLN A 264      49.459 -20.728  14.974  1.00 29.31           O  
-ATOM   1900  NE2 GLN A 264      49.221 -22.725  16.041  1.00 25.38           N  
-ATOM   1901  N   HIS A 265      49.756 -20.859   9.487  1.00 24.49           N  
-ATOM   1902  CA  HIS A 265      50.135 -19.789   8.534  1.00 26.14           C  
-ATOM   1903  C   HIS A 265      49.079 -19.819   7.349  1.00 25.77           C  
-ATOM   1904  O   HIS A 265      48.532 -18.797   6.920  1.00 22.25           O  
-ATOM   1905  CB  HIS A 265      51.505 -20.058   7.922  1.00 26.52           C  
-ATOM   1906  CG  HIS A 265      51.812 -19.095   6.804  1.00 30.55           C  
-ATOM   1907  ND1 HIS A 265      52.298 -17.803   7.039  1.00 32.39           N  
-ATOM   1908  CD2 HIS A 265      51.561 -19.168   5.476  1.00 22.79           C  
-ATOM   1909  CE1 HIS A 265      52.452 -17.178   5.869  1.00 27.85           C  
-ATOM   1910  NE2 HIS A 265      51.959 -17.952   4.916  1.00 35.61           N  
-ATOM   1911  N   LEU A 266      48.756 -21.021   6.897  1.00 23.63           N  
-ATOM   1912  CA  LEU A 266      47.837 -21.120   5.729  1.00 23.39           C  
-ATOM   1913  C   LEU A 266      46.474 -20.626   6.166  1.00 22.88           C  
-ATOM   1914  O   LEU A 266      45.783 -19.939   5.356  1.00 24.52           O  
-ATOM   1915  CB  LEU A 266      47.731 -22.581   5.229  1.00 22.42           C  
-ATOM   1916  CG  LEU A 266      46.725 -22.850   4.024  1.00 22.22           C  
-ATOM   1917  CD1 LEU A 266      46.851 -21.876   2.845  1.00 21.76           C  
-ATOM   1918  CD2 LEU A 266      46.819 -24.288   3.600  1.00 23.33           C  
-ATOM   1919  N   ILE A 267      46.038 -21.046   7.388  1.00 23.92           N  
-ATOM   1920  CA  ILE A 267      44.654 -20.714   7.853  1.00 22.08           C  
-ATOM   1921  C   ILE A 267      44.605 -19.198   7.964  1.00 24.11           C  
-ATOM   1922  O   ILE A 267      43.665 -18.580   7.522  1.00 23.09           O  
-ATOM   1923  CB  ILE A 267      44.332 -21.318   9.205  1.00 22.82           C  
-ATOM   1924  CG1 ILE A 267      44.072 -22.851   8.981  1.00 20.69           C  
-ATOM   1925  CG2 ILE A 267      43.094 -20.633   9.852  1.00 19.77           C  
-ATOM   1926  CD1 ILE A 267      44.146 -23.696  10.258  1.00 25.12           C  
-ATOM   1927  N   ARG A 268      45.617 -18.599   8.563  1.00 23.13           N  
-ATOM   1928  CA  ARG A 268      45.531 -17.133   8.842  1.00 25.50           C  
-ATOM   1929  C   ARG A 268      45.662 -16.418   7.479  1.00 24.13           C  
-ATOM   1930  O   ARG A 268      45.185 -15.291   7.325  1.00 26.48           O  
-ATOM   1931  CB  ARG A 268      46.672 -16.744   9.777  1.00 23.59           C  
-ATOM   1932  CG  ARG A 268      46.500 -17.200  11.208  1.00 24.88           C  
-ATOM   1933  CD  ARG A 268      47.433 -16.355  12.188  1.00 28.65           C  
-ATOM   1934  NE  ARG A 268      46.976 -16.547  13.584  1.00 28.83           N  
-ATOM   1935  CZ  ARG A 268      47.461 -17.504  14.371  1.00 34.20           C  
-ATOM   1936  NH1 ARG A 268      48.433 -18.225  13.882  1.00 31.34           N  
-ATOM   1937  NH2 ARG A 268      46.969 -17.709  15.606  1.00 29.96           N  
-ATOM   1938  N   TRP A 269      46.338 -17.051   6.493  1.00 24.70           N  
-ATOM   1939  CA  TRP A 269      46.364 -16.443   5.135  1.00 23.81           C  
-ATOM   1940  C   TRP A 269      44.972 -16.459   4.489  1.00 23.67           C  
-ATOM   1941  O   TRP A 269      44.487 -15.428   4.005  1.00 22.96           O  
-ATOM   1942  CB  TRP A 269      47.428 -17.101   4.269  1.00 23.08           C  
-ATOM   1943  CG  TRP A 269      47.807 -16.419   3.037  1.00 25.43           C  
-ATOM   1944  CD1 TRP A 269      47.517 -15.047   2.648  1.00 28.17           C  
-ATOM   1945  CD2 TRP A 269      48.597 -16.960   1.975  1.00 25.28           C  
-ATOM   1946  NE1 TRP A 269      48.057 -14.810   1.366  1.00 28.74           N  
-ATOM   1947  CE2 TRP A 269      48.738 -15.941   0.964  1.00 26.90           C  
-ATOM   1948  CE3 TRP A 269      49.216 -18.195   1.779  1.00 22.85           C  
-ATOM   1949  CZ2 TRP A 269      49.493 -16.137  -0.185  1.00 29.28           C  
-ATOM   1950  CZ3 TRP A 269      49.936 -18.386   0.640  1.00 26.94           C  
-ATOM   1951  CH2 TRP A 269      50.089 -17.363  -0.327  1.00 29.19           C  
-ATOM   1952  N   CYS A 270      44.317 -17.642   4.469  1.00 21.06           N  
-ATOM   1953  CA  CYS A 270      42.940 -17.722   3.944  1.00 21.50           C  
-ATOM   1954  C   CYS A 270      42.058 -16.700   4.652  1.00 21.20           C  
-ATOM   1955  O   CYS A 270      41.121 -16.209   4.041  1.00 21.71           O  
-ATOM   1956  CB  CYS A 270      42.352 -19.150   4.211  1.00 20.96           C  
-ATOM   1957  SG  CYS A 270      43.216 -20.283   3.034  1.00 25.55           S  
-ATOM   1958  N   LEU A 271      42.296 -16.404   5.967  1.00 22.35           N  
-ATOM   1959  CA  LEU A 271      41.401 -15.514   6.734  1.00 25.65           C  
-ATOM   1960  C   LEU A 271      41.978 -14.068   6.806  1.00 26.09           C  
-ATOM   1961  O   LEU A 271      41.672 -13.378   7.744  1.00 28.50           O  
-ATOM   1962  CB  LEU A 271      41.228 -15.983   8.179  1.00 23.31           C  
-ATOM   1963  CG  LEU A 271      40.547 -17.433   8.187  1.00 22.82           C  
-ATOM   1964  CD1 LEU A 271      40.389 -18.008   9.574  1.00 24.49           C  
-ATOM   1965  CD2 LEU A 271      39.102 -17.435   7.453  1.00 22.62           C  
-ATOM   1966  N   ALA A 272      42.733 -13.662   5.809  1.00 26.95           N  
-ATOM   1967  CA  ALA A 272      43.187 -12.234   5.704  1.00 28.13           C  
-ATOM   1968  C   ALA A 272      41.956 -11.351   5.657  1.00 29.23           C  
-ATOM   1969  O   ALA A 272      40.964 -11.613   4.929  1.00 27.47           O  
-ATOM   1970  CB  ALA A 272      44.031 -12.011   4.500  1.00 27.21           C  
-ATOM   1971  N   LEU A 273      41.969 -10.317   6.524  1.00 30.14           N  
-ATOM   1972  CA  LEU A 273      40.807  -9.391   6.605  1.00 30.27           C  
-ATOM   1973  C   LEU A 273      40.531  -8.751   5.221  1.00 29.36           C  
-ATOM   1974  O   LEU A 273      39.387  -8.660   4.770  1.00 28.91           O  
-ATOM   1975  CB  LEU A 273      41.093  -8.306   7.690  1.00 32.54           C  
-ATOM   1976  CG  LEU A 273      40.877  -8.745   9.134  1.00 34.75           C  
-ATOM   1977  CD1 LEU A 273      41.119  -7.604  10.161  1.00 36.69           C  
-ATOM   1978  CD2 LEU A 273      39.450  -9.243   9.285  1.00 38.63           C  
-ATOM   1979  N   ARG A 274      41.544  -8.265   4.557  1.00 28.72           N  
-ATOM   1980  CA  ARG A 274      41.375  -7.680   3.246  1.00 32.64           C  
-ATOM   1981  C   ARG A 274      41.320  -8.771   2.189  1.00 31.01           C  
-ATOM   1982  O   ARG A 274      42.277  -9.567   2.063  1.00 29.63           O  
-ATOM   1983  CB  ARG A 274      42.587  -6.821   2.882  1.00 32.57           C  
-ATOM   1984  CG  ARG A 274      42.606  -5.426   3.496  1.00 43.03           C  
-ATOM   1985  CD  ARG A 274      44.129  -4.846   3.544  1.00 42.93           C  
-ATOM   1986  NE  ARG A 274      44.676  -4.113   2.391  1.00 61.14           N  
-ATOM   1987  CZ  ARG A 274      44.474  -4.350   1.083  1.00 69.28           C  
-ATOM   1988  NH1 ARG A 274      43.700  -5.353   0.628  1.00 69.85           N  
-ATOM   1989  NH2 ARG A 274      45.090  -3.554   0.196  1.00 72.60           N  
-ATOM   1990  N   PRO A 275      40.239  -8.794   1.396  1.00 29.78           N  
-ATOM   1991  CA  PRO A 275      40.043  -9.791   0.400  1.00 30.95           C  
-ATOM   1992  C   PRO A 275      41.266  -9.995  -0.501  1.00 30.57           C  
-ATOM   1993  O   PRO A 275      41.574 -11.098  -0.858  1.00 29.07           O  
-ATOM   1994  CB  PRO A 275      38.827  -9.296  -0.398  1.00 30.86           C  
-ATOM   1995  CG  PRO A 275      38.006  -8.538   0.697  1.00 29.92           C  
-ATOM   1996  CD  PRO A 275      39.089  -7.833   1.464  1.00 30.86           C  
-ATOM   1997  N   SER A 276      41.939  -8.927  -0.913  1.00 32.19           N  
-ATOM   1998  CA  SER A 276      42.956  -9.081  -1.931  1.00 31.30           C  
-ATOM   1999  C   SER A 276      44.232  -9.616  -1.223  1.00 31.87           C  
-ATOM   2000  O   SER A 276      45.192  -9.917  -1.879  1.00 33.47           O  
-ATOM   2001  CB  SER A 276      43.235  -7.683  -2.524  1.00 33.24           C  
-ATOM   2002  OG  SER A 276      43.703  -6.795  -1.454  1.00 35.94           O  
-ATOM   2003  N   ASP A 277      44.244  -9.656   0.105  1.00 31.97           N  
-ATOM   2004  CA  ASP A 277      45.336 -10.297   0.883  1.00 31.07           C  
-ATOM   2005  C   ASP A 277      45.223 -11.832   0.992  1.00 30.73           C  
-ATOM   2006  O   ASP A 277      46.205 -12.454   1.445  1.00 31.03           O  
-ATOM   2007  CB  ASP A 277      45.383  -9.747   2.292  1.00 29.07           C  
-ATOM   2008  CG  ASP A 277      46.176  -8.357   2.325  1.00 37.49           C  
-ATOM   2009  OD1 ASP A 277      46.766  -7.981   1.299  1.00 32.25           O  
-ATOM   2010  OD2 ASP A 277      46.137  -7.713   3.343  1.00 38.70           O  
-ATOM   2011  N   ARG A 278      44.071 -12.428   0.555  1.00 26.93           N  
-ATOM   2012  CA  ARG A 278      43.961 -13.889   0.654  1.00 23.85           C  
-ATOM   2013  C   ARG A 278      44.601 -14.600  -0.522  1.00 26.41           C  
-ATOM   2014  O   ARG A 278      44.803 -14.013  -1.634  1.00 25.56           O  
-ATOM   2015  CB  ARG A 278      42.459 -14.258   0.709  1.00 24.63           C  
-ATOM   2016  CG  ARG A 278      41.790 -13.464   1.782  1.00 25.64           C  
-ATOM   2017  CD  ARG A 278      40.253 -13.807   1.883  1.00 22.52           C  
-ATOM   2018  NE  ARG A 278      39.704 -12.824   2.837  1.00 25.74           N  
-ATOM   2019  CZ  ARG A 278      38.491 -12.269   2.750  1.00 24.49           C  
-ATOM   2020  NH1 ARG A 278      37.626 -12.630   1.763  1.00 27.96           N  
-ATOM   2021  NH2 ARG A 278      38.202 -11.257   3.597  1.00 26.13           N  
-ATOM   2022  N   PRO A 279      45.032 -15.872  -0.299  1.00 24.09           N  
-ATOM   2023  CA  PRO A 279      45.730 -16.575  -1.387  1.00 23.59           C  
-ATOM   2024  C   PRO A 279      44.745 -16.916  -2.547  1.00 27.00           C  
-ATOM   2025  O   PRO A 279      43.536 -17.016  -2.294  1.00 25.49           O  
-ATOM   2026  CB  PRO A 279      46.153 -17.895  -0.684  1.00 23.81           C  
-ATOM   2027  CG  PRO A 279      45.071 -18.073   0.494  1.00 23.67           C  
-ATOM   2028  CD  PRO A 279      44.940 -16.645   0.989  1.00 20.60           C  
-ATOM   2029  N   THR A 280      45.226 -17.142  -3.774  1.00 26.15           N  
-ATOM   2030  CA  THR A 280      44.363 -17.707  -4.806  1.00 25.58           C  
-ATOM   2031  C   THR A 280      44.402 -19.236  -4.605  1.00 27.06           C  
-ATOM   2032  O   THR A 280      45.225 -19.713  -3.779  1.00 26.17           O  
-ATOM   2033  CB  THR A 280      45.028 -17.477  -6.147  1.00 25.46           C  
-ATOM   2034  OG1 THR A 280      46.331 -18.115  -6.139  1.00 26.39           O  
-ATOM   2035  CG2 THR A 280      45.173 -15.900  -6.381  1.00 26.26           C  
-ATOM   2036  N   PHE A 281      43.606 -19.983  -5.376  1.00 25.16           N  
-ATOM   2037  CA  PHE A 281      43.663 -21.522  -5.242  1.00 25.18           C  
-ATOM   2038  C   PHE A 281      45.017 -22.033  -5.482  1.00 26.49           C  
-ATOM   2039  O   PHE A 281      45.502 -22.981  -4.830  1.00 25.64           O  
-ATOM   2040  CB  PHE A 281      42.624 -22.209  -6.136  1.00 27.80           C  
-ATOM   2041  CG  PHE A 281      41.192 -21.802  -5.802  1.00 29.08           C  
-ATOM   2042  CD1 PHE A 281      40.760 -21.702  -4.501  1.00 36.55           C  
-ATOM   2043  CD2 PHE A 281      40.237 -21.609  -6.841  1.00 37.39           C  
-ATOM   2044  CE1 PHE A 281      39.348 -21.272  -4.152  1.00 34.94           C  
-ATOM   2045  CE2 PHE A 281      38.888 -21.253  -6.546  1.00 39.89           C  
-ATOM   2046  CZ  PHE A 281      38.477 -21.047  -5.145  1.00 37.37           C  
-ATOM   2047  N   GLU A 282      45.692 -21.464  -6.477  1.00 24.11           N  
-ATOM   2048  CA  GLU A 282      46.998 -21.923  -6.813  1.00 26.49           C  
-ATOM   2049  C   GLU A 282      47.925 -21.704  -5.659  1.00 25.98           C  
-ATOM   2050  O   GLU A 282      48.713 -22.611  -5.336  1.00 27.27           O  
-ATOM   2051  CB  GLU A 282      47.504 -21.187  -8.111  1.00 26.28           C  
-ATOM   2052  CG  GLU A 282      48.948 -21.692  -8.471  1.00 26.60           C  
-ATOM   2053  CD  GLU A 282      49.463 -20.942  -9.754  1.00 34.44           C  
-ATOM   2054  OE1 GLU A 282      48.859 -19.884 -10.101  1.00 36.17           O  
-ATOM   2055  OE2 GLU A 282      50.451 -21.415 -10.366  1.00 38.68           O  
-ATOM   2056  N   GLU A 283      47.888 -20.552  -5.019  1.00 23.93           N  
-ATOM   2057  CA  GLU A 283      48.755 -20.246  -3.839  1.00 25.06           C  
-ATOM   2058  C   GLU A 283      48.425 -21.153  -2.653  1.00 25.44           C  
-ATOM   2059  O   GLU A 283      49.331 -21.625  -1.929  1.00 27.97           O  
-ATOM   2060  CB  GLU A 283      48.543 -18.823  -3.413  1.00 26.49           C  
-ATOM   2061  CG  GLU A 283      49.427 -17.855  -4.307  1.00 25.65           C  
-ATOM   2062  CD  GLU A 283      49.152 -16.439  -3.969  1.00 32.85           C  
-ATOM   2063  OE1 GLU A 283      48.000 -16.060  -3.713  1.00 27.11           O  
-ATOM   2064  OE2 GLU A 283      50.131 -15.713  -3.910  1.00 32.72           O  
-ATOM   2065  N   ILE A 284      47.160 -21.502  -2.509  1.00 22.66           N  
-ATOM   2066  CA  ILE A 284      46.836 -22.479  -1.410  1.00 23.24           C  
-ATOM   2067  C   ILE A 284      47.470 -23.818  -1.786  1.00 23.06           C  
-ATOM   2068  O   ILE A 284      48.143 -24.386  -0.924  1.00 25.71           O  
-ATOM   2069  CB  ILE A 284      45.351 -22.624  -1.208  1.00 21.07           C  
-ATOM   2070  CG1 ILE A 284      44.725 -21.286  -0.729  1.00 23.60           C  
-ATOM   2071  CG2 ILE A 284      44.955 -23.870  -0.238  1.00 22.09           C  
-ATOM   2072  CD1 ILE A 284      43.165 -21.426  -0.796  1.00 22.89           C  
-ATOM   2073  N   GLN A 285      47.277 -24.315  -3.029  1.00 22.98           N  
-ATOM   2074  CA  GLN A 285      47.767 -25.694  -3.300  1.00 24.49           C  
-ATOM   2075  C   GLN A 285      49.317 -25.785  -3.416  1.00 26.08           C  
-ATOM   2076  O   GLN A 285      49.894 -26.855  -3.325  1.00 25.03           O  
-ATOM   2077  CB  GLN A 285      47.041 -26.265  -4.516  1.00 25.05           C  
-ATOM   2078  CG  GLN A 285      45.511 -26.461  -4.253  1.00 26.77           C  
-ATOM   2079  CD  GLN A 285      44.931 -27.257  -5.389  1.00 26.70           C  
-ATOM   2080  OE1 GLN A 285      44.848 -26.759  -6.494  1.00 27.34           O  
-ATOM   2081  NE2 GLN A 285      44.623 -28.547  -5.148  1.00 25.02           N  
-ATOM   2082  N   ASN A 286      49.971 -24.644  -3.592  1.00 25.87           N  
-ATOM   2083  CA  ASN A 286      51.460 -24.585  -3.521  1.00 27.92           C  
-ATOM   2084  C   ASN A 286      52.014 -24.288  -2.164  1.00 27.34           C  
-ATOM   2085  O   ASN A 286      53.278 -24.261  -1.985  1.00 27.31           O  
-ATOM   2086  CB  ASN A 286      51.998 -23.565  -4.531  1.00 28.00           C  
-ATOM   2087  CG  ASN A 286      51.806 -24.057  -5.996  1.00 30.89           C  
-ATOM   2088  OD1 ASN A 286      51.825 -25.241  -6.277  1.00 33.28           O  
-ATOM   2089  ND2 ASN A 286      51.629 -23.172  -6.869  1.00 30.20           N  
-ATOM   2090  N   HIS A 287      51.123 -24.105  -1.170  1.00 25.02           N  
-ATOM   2091  CA  HIS A 287      51.609 -23.818   0.169  1.00 25.01           C  
-ATOM   2092  C   HIS A 287      52.421 -24.970   0.741  1.00 26.14           C  
-ATOM   2093  O   HIS A 287      52.083 -26.150   0.456  1.00 27.56           O  
-ATOM   2094  CB  HIS A 287      50.437 -23.399   1.060  1.00 24.52           C  
-ATOM   2095  CG  HIS A 287      50.849 -23.015   2.429  1.00 24.25           C  
-ATOM   2096  ND1 HIS A 287      50.919 -21.700   2.860  1.00 26.11           N  
-ATOM   2097  CD2 HIS A 287      51.182 -23.788   3.490  1.00 18.69           C  
-ATOM   2098  CE1 HIS A 287      51.315 -21.667   4.124  1.00 20.62           C  
-ATOM   2099  NE2 HIS A 287      51.501 -22.933   4.519  1.00 29.24           N  
-ATOM   2100  N   PRO A 288      53.483 -24.692   1.503  1.00 27.53           N  
-ATOM   2101  CA  PRO A 288      54.277 -25.815   2.069  1.00 29.17           C  
-ATOM   2102  C   PRO A 288      53.351 -26.784   2.829  1.00 29.21           C  
-ATOM   2103  O   PRO A 288      53.652 -27.990   2.856  1.00 27.89           O  
-ATOM   2104  CB  PRO A 288      55.137 -25.128   3.115  1.00 30.22           C  
-ATOM   2105  CG  PRO A 288      55.433 -23.764   2.476  1.00 31.64           C  
-ATOM   2106  CD  PRO A 288      54.083 -23.395   1.828  1.00 29.06           C  
-ATOM   2107  N   TRP A 289      52.270 -26.305   3.483  1.00 26.19           N  
-ATOM   2108  CA  TRP A 289      51.508 -27.287   4.268  1.00 27.06           C  
-ATOM   2109  C   TRP A 289      50.857 -28.324   3.373  1.00 26.07           C  
-ATOM   2110  O   TRP A 289      50.528 -29.427   3.871  1.00 27.33           O  
-ATOM   2111  CB  TRP A 289      50.458 -26.609   5.206  1.00 26.02           C  
-ATOM   2112  CG  TRP A 289      49.791 -27.583   6.111  1.00 22.73           C  
-ATOM   2113  CD1 TRP A 289      50.342 -28.210   7.195  1.00 24.11           C  
-ATOM   2114  CD2 TRP A 289      48.459 -28.049   5.968  1.00 23.06           C  
-ATOM   2115  NE1 TRP A 289      49.360 -29.067   7.798  1.00 25.38           N  
-ATOM   2116  CE2 TRP A 289      48.220 -29.003   7.034  1.00 25.98           C  
-ATOM   2117  CE3 TRP A 289      47.430 -27.749   5.056  1.00 24.74           C  
-ATOM   2118  CZ2 TRP A 289      46.995 -29.681   7.177  1.00 27.44           C  
-ATOM   2119  CZ3 TRP A 289      46.200 -28.420   5.175  1.00 24.50           C  
-ATOM   2120  CH2 TRP A 289      46.007 -29.403   6.222  1.00 23.91           C  
-ATOM   2121  N   MET A 290      50.610 -27.980   2.108  1.00 26.29           N  
-ATOM   2122  CA  MET A 290      49.798 -28.781   1.184  1.00 27.55           C  
-ATOM   2123  C   MET A 290      50.596 -29.878   0.431  1.00 30.72           C  
-ATOM   2124  O   MET A 290      50.036 -30.540  -0.454  1.00 30.18           O  
-ATOM   2125  CB  MET A 290      49.013 -27.962   0.172  1.00 24.10           C  
-ATOM   2126  CG  MET A 290      47.916 -26.999   0.926  1.00 27.61           C  
-ATOM   2127  SD  MET A 290      46.243 -27.671   0.719  1.00 33.24           S  
-ATOM   2128  CE  MET A 290      46.430 -28.942   1.761  1.00 22.99           C  
-ATOM   2129  N   GLN A 291      51.884 -30.053   0.759  1.00 31.04           N  
-ATOM   2130  CA  GLN A 291      52.736 -30.850  -0.132  1.00 31.49           C  
-ATOM   2131  C   GLN A 291      52.605 -32.309   0.326  1.00 32.36           C  
-ATOM   2132  O   GLN A 291      52.216 -32.530   1.488  1.00 31.38           O  
-ATOM   2133  CB  GLN A 291      54.174 -30.332  -0.013  1.00 32.80           C  
-ATOM   2134  CG  GLN A 291      54.364 -28.841  -0.677  1.00 37.32           C  
-ATOM   2135  CD  GLN A 291      53.459 -28.574  -1.986  1.00 47.80           C  
-ATOM   2136  OE1 GLN A 291      53.715 -29.165  -3.048  1.00 49.95           O  
-ATOM   2137  NE2 GLN A 291      52.381 -27.714  -1.874  1.00 42.93           N  
-ATOM   2138  N   ASP A 292      52.803 -33.265  -0.603  1.00 31.67           N  
-ATOM   2139  CA  ASP A 292      52.856 -34.667  -0.235  1.00 34.37           C  
-ATOM   2140  C   ASP A 292      51.541 -35.174   0.268  1.00 33.05           C  
-ATOM   2141  O   ASP A 292      51.517 -35.908   1.251  1.00 34.01           O  
-ATOM   2142  CB  ASP A 292      53.856 -34.872   0.882  1.00 35.14           C  
-ATOM   2143  CG  ASP A 292      55.307 -34.607   0.396  1.00 46.98           C  
-ATOM   2144  OD1 ASP A 292      55.581 -34.789  -0.860  1.00 54.27           O  
-ATOM   2145  OD2 ASP A 292      56.163 -34.183   1.239  1.00 56.06           O  
-ATOM   2146  N   VAL A 293      50.460 -34.800  -0.410  1.00 30.23           N  
-ATOM   2147  CA  VAL A 293      49.131 -35.168   0.061  1.00 28.74           C  
-ATOM   2148  C   VAL A 293      48.982 -36.660  -0.217  1.00 28.48           C  
-ATOM   2149  O   VAL A 293      49.526 -37.148  -1.199  1.00 27.02           O  
-ATOM   2150  CB  VAL A 293      48.076 -34.421  -0.767  1.00 28.20           C  
-ATOM   2151  CG1 VAL A 293      48.065 -34.921  -2.272  1.00 28.79           C  
-ATOM   2152  CG2 VAL A 293      46.655 -34.559  -0.164  1.00 30.25           C  
-ATOM   2153  N   LEU A 294      48.221 -37.356   0.625  1.00 29.33           N  
-ATOM   2154  CA  LEU A 294      47.873 -38.745   0.419  1.00 29.62           C  
-ATOM   2155  C   LEU A 294      46.904 -38.874  -0.766  1.00 30.64           C  
-ATOM   2156  O   LEU A 294      46.034 -38.011  -0.992  1.00 29.76           O  
-ATOM   2157  CB  LEU A 294      47.182 -39.367   1.623  1.00 25.65           C  
-ATOM   2158  CG  LEU A 294      47.896 -39.541   2.966  1.00 26.87           C  
-ATOM   2159  CD1 LEU A 294      46.978 -40.096   4.103  1.00 26.50           C  
-ATOM   2160  CD2 LEU A 294      49.223 -40.380   2.713  1.00 29.88           C  
-ATOM   2161  N   LEU A 295      46.949 -40.060  -1.398  1.00 28.96           N  
-ATOM   2162  CA  LEU A 295      45.949 -40.363  -2.366  1.00 29.02           C  
-ATOM   2163  C   LEU A 295      44.655 -40.716  -1.642  1.00 27.52           C  
-ATOM   2164  O   LEU A 295      44.686 -41.136  -0.479  1.00 27.45           O  
-ATOM   2165  CB  LEU A 295      46.390 -41.588  -3.233  1.00 32.63           C  
-ATOM   2166  CG  LEU A 295      47.644 -41.494  -4.114  1.00 35.70           C  
-ATOM   2167  CD1 LEU A 295      47.834 -42.849  -4.887  1.00 41.04           C  
-ATOM   2168  CD2 LEU A 295      47.677 -40.362  -5.059  1.00 35.35           C  
-ATOM   2169  N   PRO A 296      43.502 -40.578  -2.294  1.00 28.83           N  
-ATOM   2170  CA  PRO A 296      42.262 -40.941  -1.519  1.00 29.41           C  
-ATOM   2171  C   PRO A 296      42.264 -42.413  -0.952  1.00 34.26           C  
-ATOM   2172  O   PRO A 296      41.956 -42.596   0.273  1.00 33.37           O  
-ATOM   2173  CB  PRO A 296      41.179 -40.811  -2.550  1.00 30.24           C  
-ATOM   2174  CG  PRO A 296      41.679 -39.684  -3.469  1.00 27.25           C  
-ATOM   2175  CD  PRO A 296      43.174 -39.989  -3.632  1.00 28.92           C  
-ATOM   2176  N   GLN A 297      42.632 -43.419  -1.805  1.00 34.44           N  
-ATOM   2177  CA  GLN A 297      42.616 -44.801  -1.316  1.00 36.31           C  
-ATOM   2178  C   GLN A 297      43.491 -44.962  -0.096  1.00 35.60           C  
-ATOM   2179  O   GLN A 297      43.042 -45.643   0.868  1.00 37.62           O  
-ATOM   2180  CB  GLN A 297      42.998 -45.886  -2.373  1.00 36.80           C  
-ATOM   2181  CG  GLN A 297      42.474 -47.385  -1.935  1.00 40.17           C  
-ATOM   2182  CD  GLN A 297      40.954 -47.381  -1.518  1.00 48.30           C  
-ATOM   2183  OE1 GLN A 297      40.083 -47.036  -2.312  1.00 53.82           O  
-ATOM   2184  NE2 GLN A 297      40.667 -47.742  -0.268  1.00 51.23           N  
-ATOM   2185  N   GLU A 298      44.708 -44.388  -0.146  1.00 34.09           N  
-ATOM   2186  CA  GLU A 298      45.639 -44.396   1.003  1.00 37.30           C  
-ATOM   2187  C   GLU A 298      45.003 -43.715   2.219  1.00 35.19           C  
-ATOM   2188  O   GLU A 298      45.159 -44.159   3.399  1.00 35.28           O  
-ATOM   2189  CB  GLU A 298      46.944 -43.650   0.771  1.00 36.82           C  
-ATOM   2190  CG  GLU A 298      47.732 -43.864  -0.479  1.00 41.71           C  
-ATOM   2191  CD  GLU A 298      48.900 -42.829  -0.502  1.00 44.09           C  
-ATOM   2192  OE1 GLU A 298      49.910 -43.058   0.180  1.00 61.60           O  
-ATOM   2193  OE2 GLU A 298      48.852 -41.764  -1.124  1.00 42.45           O  
-ATOM   2194  N   THR A 299      44.278 -42.632   1.943  1.00 31.23           N  
-ATOM   2195  CA  THR A 299      43.566 -41.960   3.001  1.00 29.91           C  
-ATOM   2196  C   THR A 299      42.533 -42.880   3.660  1.00 30.13           C  
-ATOM   2197  O   THR A 299      42.404 -42.955   4.906  1.00 29.69           O  
-ATOM   2198  CB  THR A 299      42.893 -40.620   2.439  1.00 29.25           C  
-ATOM   2199  OG1 THR A 299      43.916 -39.775   1.830  1.00 29.26           O  
-ATOM   2200  CG2 THR A 299      42.223 -39.900   3.637  1.00 30.72           C  
-ATOM   2201  N   ALA A 300      41.819 -43.623   2.840  1.00 31.42           N  
-ATOM   2202  CA  ALA A 300      40.786 -44.545   3.394  1.00 33.24           C  
-ATOM   2203  C   ALA A 300      41.465 -45.670   4.271  1.00 35.52           C  
-ATOM   2204  O   ALA A 300      41.019 -46.014   5.385  1.00 35.82           O  
-ATOM   2205  CB  ALA A 300      40.003 -45.147   2.276  1.00 33.58           C  
-ATOM   2206  N   GLU A 301      42.543 -46.211   3.724  1.00 36.21           N  
-ATOM   2207  CA  GLU A 301      43.263 -47.285   4.366  1.00 39.75           C  
-ATOM   2208  C   GLU A 301      43.873 -46.873   5.703  1.00 39.64           C  
-ATOM   2209  O   GLU A 301      43.697 -47.602   6.687  1.00 40.16           O  
-ATOM   2210  CB  GLU A 301      44.315 -47.848   3.439  1.00 39.93           C  
-ATOM   2211  CG  GLU A 301      43.670 -48.689   2.342  1.00 47.86           C  
-ATOM   2212  CD  GLU A 301      44.672 -49.005   1.228  1.00 60.63           C  
-ATOM   2213  OE1 GLU A 301      45.847 -48.521   1.333  1.00 63.40           O  
-ATOM   2214  OE2 GLU A 301      44.274 -49.707   0.245  1.00 64.67           O  
-ATOM   2215  N   ILE A 302      44.557 -45.723   5.747  1.00 37.07           N  
-ATOM   2216  CA  ILE A 302      45.143 -45.260   6.979  1.00 37.90           C  
-ATOM   2217  C   ILE A 302      44.147 -44.709   7.986  1.00 38.64           C  
-ATOM   2218  O   ILE A 302      44.263 -44.963   9.182  1.00 39.52           O  
-ATOM   2219  CB  ILE A 302      46.214 -44.223   6.657  1.00 38.45           C  
-ATOM   2220  CG1 ILE A 302      47.184 -44.814   5.580  1.00 38.77           C  
-ATOM   2221  CG2 ILE A 302      46.829 -43.690   7.963  1.00 40.86           C  
-ATOM   2222  CD1 ILE A 302      48.292 -43.892   5.066  1.00 39.14           C  
-ATOM   2223  N   HIS A 303      43.165 -43.929   7.530  1.00 37.64           N  
-ATOM   2224  CA  HIS A 303      42.389 -43.118   8.450  1.00 36.71           C  
-ATOM   2225  C   HIS A 303      40.952 -43.529   8.536  1.00 36.75           C  
-ATOM   2226  O   HIS A 303      40.244 -43.190   9.527  1.00 37.96           O  
-ATOM   2227  CB  HIS A 303      42.482 -41.645   7.995  1.00 33.44           C  
-ATOM   2228  CG  HIS A 303      43.837 -41.057   8.219  1.00 30.15           C  
-ATOM   2229  ND1 HIS A 303      44.272 -40.696   9.468  1.00 30.67           N  
-ATOM   2230  CD2 HIS A 303      44.840 -40.769   7.366  1.00 29.44           C  
-ATOM   2231  CE1 HIS A 303      45.514 -40.231   9.395  1.00 29.22           C  
-ATOM   2232  NE2 HIS A 303      45.874 -40.230   8.111  1.00 30.29           N  
-ATOM   2233  N   LEU A 304      40.440 -44.182   7.506  1.00 38.92           N  
-ATOM   2234  CA  LEU A 304      39.007 -44.457   7.539  1.00 41.57           C  
-ATOM   2235  C   LEU A 304      38.720 -45.951   7.746  1.00 48.74           C  
-ATOM   2236  O   LEU A 304      37.572 -46.315   7.944  1.00 48.50           O  
-ATOM   2237  CB  LEU A 304      38.250 -43.900   6.319  1.00 40.49           C  
-ATOM   2238  CG  LEU A 304      38.572 -42.444   5.897  1.00 33.49           C  
-ATOM   2239  CD1 LEU A 304      37.892 -42.158   4.491  1.00 33.84           C  
-ATOM   2240  CD2 LEU A 304      38.042 -41.589   6.955  1.00 35.37           C  
-ATOM   2241  N   HIS A 305      39.799 -46.734   7.793  1.00 53.89           N  
-ATOM   2242  C   HIS A 305      38.853 -48.829   6.839  1.00 59.44           C  
-ATOM   2243  O   HIS A 305      37.872 -49.541   7.200  1.00 61.16           O  
-ATOM   2244  CA AHIS A 305      39.787 -48.210   7.873  0.50 57.47           C  
-ATOM   2245  CB AHIS A 305      39.549 -48.759   9.305  0.50 57.64           C  
-ATOM   2246  CG AHIS A 305      38.329 -48.224   9.977  0.50 58.55           C  
-ATOM   2247  ND1AHIS A 305      37.088 -48.798   9.824  0.50 60.58           N  
-ATOM   2248  CD2AHIS A 305      38.160 -47.172  10.816  0.50 60.77           C  
-ATOM   2249  CE1AHIS A 305      36.200 -48.119  10.537  0.50 62.17           C  
-ATOM   2250  NE2AHIS A 305      36.825 -47.125  11.146  0.50 63.17           N  
-ATOM   2251  CA BHIS A 305      39.771 -48.198   7.896  0.50 57.68           C  
-ATOM   2252  CB BHIS A 305      39.490 -48.639   9.356  0.50 57.96           C  
-ATOM   2253  CG BHIS A 305      40.477 -48.065  10.330  0.50 59.95           C  
-ATOM   2254  ND1BHIS A 305      41.723 -48.622  10.544  0.50 61.26           N  
-ATOM   2255  CD2BHIS A 305      40.435 -46.938  11.080  0.50 62.19           C  
-ATOM   2256  CE1BHIS A 305      42.391 -47.879  11.406  0.50 63.36           C  
-ATOM   2257  NE2BHIS A 305      41.636 -46.847  11.742  0.50 64.64           N  
-ATOM   2258  N   SER A 306      39.201 -48.573   5.554  1.00 60.65           N  
-ATOM   2259  CA  SER A 306      38.369 -48.806   4.327  1.00 62.85           C  
-ATOM   2260  C   SER A 306      39.236 -48.918   3.093  1.00 62.25           C  
-ATOM   2261  O   SER A 306      40.459 -48.927   3.222  1.00 63.29           O  
-ATOM   2262  CB  SER A 306      37.406 -47.635   4.052  1.00 62.59           C  
-ATOM   2263  OG  SER A 306      36.600 -47.267   5.189  1.00 67.72           O  
-TER    2264      SER A 306                                                      
-HETATM 2265  N1  IMD A1307      31.859 -30.260  13.196  1.00 44.91           N  
-HETATM 2266  C2  IMD A1307      32.442 -29.210  13.758  1.00 42.62           C  
-HETATM 2267  N3  IMD A1307      32.238 -29.353  15.085  1.00 42.76           N  
-HETATM 2268  C4  IMD A1307      31.516 -30.469  15.340  1.00 39.06           C  
-HETATM 2269  C5  IMD A1307      31.245 -31.044  14.112  1.00 44.28           C  
-HETATM 2270  C5  HY7 A1308      21.011 -29.247   2.375  1.00 32.86           C  
-HETATM 2271  C6  HY7 A1308      21.502 -27.932   3.082  1.00 33.65           C  
-HETATM 2272  N3  HY7 A1308      22.942 -28.128   3.429  1.00 29.60           N  
-HETATM 2273  C7  HY7 A1308      23.487 -26.997   4.252  1.00 34.50           C  
-HETATM 2274  C8  HY7 A1308      23.248 -29.318   4.280  1.00 29.19           C  
-HETATM 2275  C9  HY7 A1308      22.876 -30.571   3.458  1.00 29.72           C  
-HETATM 2276  N2  HY7 A1308      21.406 -30.422   3.159  1.00 30.89           N  
-HETATM 2277  C4  HY7 A1308      20.831 -31.658   2.600  1.00 31.48           C  
-HETATM 2278  C3  HY7 A1308      21.450 -32.287   1.392  1.00 27.84           C  
-HETATM 2279  N4  HY7 A1308      21.817 -33.527   1.423  1.00 29.98           N  
-HETATM 2280  C10 HY7 A1308      22.304 -34.156   0.307  1.00 25.66           C  
-HETATM 2281  C11 HY7 A1308      22.794 -35.432   0.041  1.00 27.76           C  
-HETATM 2282  C12 HY7 A1308      22.893 -36.578   0.817  1.00 29.77           C  
-HETATM 2283  C13 HY7 A1308      23.435 -37.635   0.123  1.00 30.61           C  
-HETATM 2284 BR1  HY7 A1308      23.732 -39.255   1.085  1.00 44.83          BR  
-HETATM 2285  C14 HY7 A1308      23.841 -37.673  -1.244  1.00 27.22           C  
-HETATM 2286  C15 HY7 A1308      23.713 -36.510  -2.002  1.00 28.95           C  
-HETATM 2287  C16 HY7 A1308      23.172 -35.457  -1.301  1.00 28.95           C  
-HETATM 2288  O2  HY7 A1308      22.949 -34.208  -1.763  1.00 29.50           O  
-HETATM 2289  C1  HY7 A1308      22.373 -33.434  -0.866  1.00 28.37           C  
-HETATM 2290  C2  HY7 A1308      22.012 -32.073  -0.900  1.00 29.57           C  
-HETATM 2291  O1  HY7 A1308      22.109 -31.353  -1.906  1.00 31.12           O  
-HETATM 2292  N1  HY7 A1308      21.456 -31.581   0.237  1.00 27.98           N  
-HETATM 2293  N1  IMD A1309      37.488 -12.588  -5.602  1.00 29.42           N  
-HETATM 2294  C2  IMD A1309      37.759 -11.978  -4.461  1.00 39.74           C  
-HETATM 2295  N3  IMD A1309      38.504 -10.888  -4.620  1.00 35.95           N  
-HETATM 2296  C4  IMD A1309      38.757 -10.844  -5.994  1.00 43.18           C  
-HETATM 2297  C5  IMD A1309      38.085 -11.867  -6.597  1.00 44.12           C  
-HETATM 2298  O   HOH A2001       5.666 -41.010  -6.898  1.00 77.98           O  
-HETATM 2299  O   HOH A2002       5.446 -38.917  -7.881  1.00 71.95           O  
-HETATM 2300  O   HOH A2003       7.511 -45.949  -6.622  1.00 70.31           O  
-HETATM 2301  O   HOH A2004       6.244 -36.486  -8.673  1.00 73.72           O  
-HETATM 2302  O   HOH A2005      14.744 -45.152 -13.429  1.00 67.31           O  
-HETATM 2303  O   HOH A2006      14.612 -40.465 -12.641  1.00 64.22           O  
-HETATM 2304  O   HOH A2007      14.976 -47.147  -0.028  1.00 54.74           O  
-HETATM 2305  O   HOH A2008       8.533 -45.432  -2.086  1.00 61.98           O  
-HETATM 2306  O   HOH A2009      12.556 -41.461   7.872  1.00 38.15           O  
-HETATM 2307  O   HOH A2010      16.853 -38.406   9.592  1.00 50.98           O  
-HETATM 2308  O   HOH A2011      18.539 -41.590   8.334  1.00 59.14           O  
-HETATM 2309  O   HOH A2012      22.073 -37.871   7.834  1.00 55.19           O  
-HETATM 2310  O   HOH A2013      15.360 -33.975   9.949  1.00 43.58           O  
-HETATM 2311  O   HOH A2014      19.132 -32.483   8.977  1.00 47.38           O  
-HETATM 2312  O   HOH A2015      16.246 -28.562  10.484  1.00 64.20           O  
-HETATM 2313  O   HOH A2016      19.916 -29.131   6.527  1.00 55.51           O  
-HETATM 2314  O   HOH A2017       2.815 -43.338  -6.625  1.00 50.55           O  
-HETATM 2315  O   HOH A2018      12.287 -28.064   6.235  1.00 65.24           O  
-HETATM 2316  O   HOH A2019      14.458 -24.300   8.989  1.00 68.66           O  
-HETATM 2317  O   HOH A2020      18.717 -25.153   4.160  1.00 46.43           O  
-HETATM 2318  O   HOH A2021      18.224 -24.883   7.872  1.00 61.37           O  
-HETATM 2319  O   HOH A2022      16.417 -22.187   1.954  1.00 66.62           O  
-HETATM 2320  O   HOH A2023      14.172 -24.327  -1.048  1.00 36.00           O  
-HETATM 2321  O   HOH A2024      11.295 -29.648   4.473  1.00 37.52           O  
-HETATM 2322  O   HOH A2025      24.090 -39.409   6.080  1.00 56.67           O  
-HETATM 2323  O   HOH A2026      23.335 -37.109   5.107  1.00 54.79           O  
-HETATM 2324  O   HOH A2027      13.474 -35.312  11.581  1.00 34.94           O  
-HETATM 2325  O   HOH A2028      22.261 -34.080   9.433  1.00 65.37           O  
-HETATM 2326  O   HOH A2029      21.154 -33.328   6.071  1.00 49.39           O  
-HETATM 2327  O   HOH A2030      20.078 -26.513   6.218  1.00 48.42           O  
-HETATM 2328  O   HOH A2031      20.247 -24.375   1.779  1.00 43.51           O  
-HETATM 2329  O   HOH A2032      16.608 -24.009  -1.892  1.00 44.44           O  
-HETATM 2330  O   HOH A2033      17.233 -46.315   1.062  1.00 44.40           O  
-HETATM 2331  O   HOH A2034      20.998 -44.251   3.584  1.00 44.90           O  
-HETATM 2332  O   HOH A2035      22.988 -42.266   3.277  1.00 38.36           O  
-HETATM 2333  O   HOH A2036      23.044 -43.609 -13.993  1.00 54.83           O  
-HETATM 2334  O   HOH A2037      21.767 -41.765 -14.437  1.00 57.37           O  
-HETATM 2335  O   HOH A2038      25.402 -42.311  -9.535  1.00 55.93           O  
-HETATM 2336  O   HOH A2039      21.138 -50.302  -3.557  1.00 52.36           O  
-HETATM 2337  O   HOH A2040      24.116 -50.936  -6.521  1.00 65.40           O  
-HETATM 2338  O   HOH A2041      24.623 -43.211  -6.748  1.00 38.67           O  
-HETATM 2339  O   HOH A2042      19.986 -26.425   0.077  1.00 31.43           O  
-HETATM 2340  O   HOH A2043      18.002 -26.538  -1.863  1.00 32.13           O  
-HETATM 2341  O   HOH A2044       8.007 -32.804  -2.953  1.00 42.87           O  
-HETATM 2342  O   HOH A2045      11.062 -38.972  -1.086  1.00 44.53           O  
-HETATM 2343  O   HOH A2046      33.347 -30.974 -16.608  1.00 55.33           O  
-HETATM 2344  O   HOH A2047       6.749 -24.445  -1.782  1.00 57.35           O  
-HETATM 2345  O   HOH A2048       5.810 -29.663  -1.142  1.00 51.24           O  
-HETATM 2346  O   HOH A2049      35.751 -36.286 -16.172  1.00 53.12           O  
-HETATM 2347  O   HOH A2050      11.462 -18.918  -4.319  1.00 66.32           O  
-HETATM 2348  O   HOH A2051       4.766 -22.579  -3.994  1.00 66.59           O  
-HETATM 2349  O   HOH A2052       7.056 -21.959   2.471  1.00 66.18           O  
-HETATM 2350  O   HOH A2053      17.708 -21.502  -2.266  1.00 52.49           O  
-HETATM 2351  O   HOH A2054      11.398 -24.660   6.701  1.00 70.25           O  
-HETATM 2352  O   HOH A2055       7.824 -27.048   4.387  1.00 66.34           O  
-HETATM 2353  O   HOH A2056      20.920 -18.785  -4.496  1.00 55.33           O  
-HETATM 2354  O   HOH A2057      21.183 -17.978  -1.937  1.00 69.68           O  
-HETATM 2355  O   HOH A2058      19.661 -20.291  -0.588  1.00 51.39           O  
-HETATM 2356  O   HOH A2059      18.244 -22.808  -6.232  1.00 50.67           O  
-HETATM 2357  O   HOH A2060      22.074 -17.159  -7.499  1.00 61.17           O  
-HETATM 2358  O   HOH A2061      27.326 -51.205   1.138  1.00 70.37           O  
-HETATM 2359  O   HOH A2062      24.043 -41.926   5.941  1.00 57.64           O  
-HETATM 2360  O   HOH A2063      13.541 -18.512 -14.796  1.00 74.96           O  
-HETATM 2361  O   HOH A2064      24.830 -38.063   5.186  1.00 62.41           O  
-HETATM 2362  O   HOH A2065      20.345 -19.324 -15.668  1.00 58.59           O  
-HETATM 2363  O   HOH A2066      20.493 -23.024 -18.398  1.00 68.91           O  
-HETATM 2364  O   HOH A2067      17.930 -27.623 -21.282  1.00 77.30           O  
-HETATM 2365  O   HOH A2068      12.492 -24.612 -22.856  1.00 68.32           O  
-HETATM 2366  O   HOH A2069      10.739 -22.151 -18.735  1.00 63.67           O  
-HETATM 2367  O   HOH A2070       8.526 -23.005 -12.287  1.00 61.14           O  
-HETATM 2368  O   HOH A2071      13.814 -16.586 -13.038  1.00 65.42           O  
-HETATM 2369  O   HOH A2072      40.584 -34.949  -6.263  1.00 42.43           O  
-HETATM 2370  O   HOH A2073      35.907 -29.710 -16.750  1.00 47.21           O  
-HETATM 2371  O   HOH A2074      21.321 -21.780  -5.833  1.00 46.96           O  
-HETATM 2372  O   HOH A2075      17.272 -24.698  -4.839  1.00 49.46           O  
-HETATM 2373  O   HOH A2076      22.645 -29.179  -4.986  1.00 28.91           O  
-HETATM 2374  O   HOH A2077      41.948 -21.711 -14.588  1.00 46.96           O  
-HETATM 2375  O   HOH A2078      40.345 -25.986 -20.882  1.00 55.08           O  
-HETATM 2376  O   HOH A2079      22.931 -25.613 -16.605  1.00 47.48           O  
-HETATM 2377  O   HOH A2080      30.159 -16.707  -0.527  1.00 32.68           O  
-HETATM 2378  O   HOH A2081      26.081 -32.618 -11.130  1.00 45.21           O  
-HETATM 2379  O   HOH A2082      16.949 -31.283 -17.670  1.00 51.48           O  
-HETATM 2380  O   HOH A2083      30.503 -26.440  13.465  1.00 53.71           O  
-HETATM 2381  O   HOH A2084      19.928 -34.230 -14.986  1.00 53.32           O  
-HETATM 2382  O   HOH A2085      24.502 -27.016 -18.035  1.00 56.59           O  
-HETATM 2383  O   HOH A2086      30.765 -30.096 -16.107  1.00 51.33           O  
-HETATM 2384  O   HOH A2087      29.654 -26.123 -17.622  1.00 48.22           O  
-HETATM 2385  O   HOH A2088      30.320 -21.037 -17.506  1.00 47.87           O  
-HETATM 2386  O   HOH A2089      31.879 -33.459 -11.761  1.00 46.99           O  
-HETATM 2387  O   HOH A2090      29.292 -33.994 -11.038  1.00 50.45           O  
-HETATM 2388  O   HOH A2091      30.710 -38.006 -11.319  1.00 68.99           O  
-HETATM 2389  O   HOH A2092      35.547 -33.721 -14.825  1.00 54.04           O  
-HETATM 2390  O   HOH A2093      33.027 -36.149 -17.057  1.00 65.90           O  
-HETATM 2391  O   HOH A2094      31.697 -40.205 -10.698  1.00 59.10           O  
-HETATM 2392  O   HOH A2095      30.475 -37.526  -8.500  1.00 38.21           O  
-HETATM 2393  O   HOH A2096      37.178 -37.514  -6.528  1.00 46.50           O  
-HETATM 2394  O   HOH A2097      21.818 -16.011 -12.438  1.00 56.09           O  
-HETATM 2395  O   HOH A2098      25.997 -13.672 -13.136  1.00 47.99           O  
-HETATM 2396  O   HOH A2099      31.107 -13.628 -15.992  1.00 52.36           O  
-HETATM 2397  O   HOH A2100      38.888 -15.259 -16.010  1.00 52.29           O  
-HETATM 2398  O   HOH A2101      39.381 -11.467 -17.803  1.00 58.55           O  
-HETATM 2399  O   HOH A2102      24.312 -37.183 -14.191  1.00 57.17           O  
-HETATM 2400  O   HOH A2103      13.564 -33.653 -16.394  1.00 68.45           O  
-HETATM 2401  O   HOH A2104      11.338 -33.179 -15.422  1.00 58.91           O  
-HETATM 2402  O   HOH A2105       9.297 -31.939 -14.260  1.00 62.51           O  
-HETATM 2403  O   HOH A2106       9.048 -29.012 -15.390  1.00 67.20           O  
-HETATM 2404  O   HOH A2107       3.688 -29.483 -11.395  1.00 63.72           O  
-HETATM 2405  O   HOH A2108       1.627 -28.747  -4.197  1.00 69.69           O  
-HETATM 2406  O   HOH A2109       5.097 -30.136  -3.924  1.00 52.92           O  
-HETATM 2407  O   HOH A2110      33.971 -19.249  19.635  1.00 53.84           O  
-HETATM 2408  O   HOH A2111      38.795 -17.300  20.194  1.00 43.86           O  
-HETATM 2409  O   HOH A2112      27.315 -40.955  -9.845  1.00 57.97           O  
-HETATM 2410  O   HOH A2113      28.913 -42.122  -5.435  1.00 48.55           O  
-HETATM 2411  O   HOH A2114      31.292 -40.723  -8.089  1.00 48.09           O  
-HETATM 2412  O   HOH A2115      25.654 -14.454  17.400  1.00 62.06           O  
-HETATM 2413  O   HOH A2116      32.599  -5.169  16.289  1.00 56.24           O  
-HETATM 2414  O   HOH A2117      36.955  -5.351  15.472  1.00 50.65           O  
-HETATM 2415  O   HOH A2118      26.657 -46.174  -4.197  1.00 52.18           O  
-HETATM 2416  O   HOH A2119      26.792 -44.505  -5.705  1.00 47.40           O  
-HETATM 2417  O   HOH A2120      23.438 -48.562   0.401  1.00 65.04           O  
-HETATM 2418  O   HOH A2121      24.598 -44.108   1.669  1.00 35.37           O  
-HETATM 2419  O   HOH A2122      20.954 -48.621  -0.692  1.00 65.40           O  
-HETATM 2420  O   HOH A2123      38.250  -4.958  13.849  1.00 55.05           O  
-HETATM 2421  O   HOH A2124      45.956 -12.800  12.011  1.00 50.23           O  
-HETATM 2422  O   HOH A2125      29.880 -45.844  -2.779  1.00 41.40           O  
-HETATM 2423  O   HOH A2126      29.447 -50.833   0.251  1.00 74.60           O  
-HETATM 2424  O   HOH A2127      31.776 -45.795   0.567  1.00 38.84           O  
-HETATM 2425  O   HOH A2128      26.050 -44.834   5.033  1.00 40.56           O  
-HETATM 2426  O   HOH A2129      25.934 -41.026   8.428  1.00 65.19           O  
-HETATM 2427  O   HOH A2130      28.120 -43.673   8.464  1.00 57.07           O  
-HETATM 2428  O   HOH A2131      26.936 -39.867  11.297  1.00 55.64           O  
-HETATM 2429  O   HOH A2132      50.239 -14.535   5.515  1.00 60.08           O  
-HETATM 2430  O   HOH A2133      53.463 -16.855   1.556  1.00 57.17           O  
-HETATM 2431  O   HOH A2134      26.526 -38.122   7.995  1.00 35.14           O  
-HETATM 2432  O   HOH A2135      25.287 -33.274   9.510  1.00 44.16           O  
-HETATM 2433  O   HOH A2136      23.850 -35.802   8.037  1.00 56.51           O  
-HETATM 2434  O   HOH A2137      24.967 -33.043   5.260  1.00 37.08           O  
-HETATM 2435  O   HOH A2138      45.653 -10.119   7.258  1.00 45.97           O  
-HETATM 2436  O   HOH A2139      27.198 -34.760  14.252  1.00 53.48           O  
-HETATM 2437  O   HOH A2140      23.335 -36.689  10.164  1.00 53.94           O  
-HETATM 2438  O   HOH A2141      40.860 -15.260  -5.678  1.00 44.83           O  
-HETATM 2439  O   HOH A2142      28.405 -31.433  16.947  1.00 56.24           O  
-HETATM 2440  O   HOH A2143      52.883 -19.637  -4.095  1.00 42.40           O  
-HETATM 2441  O   HOH A2144      53.448 -19.845   0.582  1.00 48.29           O  
-HETATM 2442  O   HOH A2145      53.956 -16.475  -1.027  1.00 67.13           O  
-HETATM 2443  O   HOH A2146      35.859 -37.634  19.772  1.00 63.39           O  
-HETATM 2444  O   HOH A2147      35.083 -42.637  14.509  1.00 64.77           O  
-HETATM 2445  O   HOH A2148      40.607 -35.842  17.719  1.00 46.13           O  
-HETATM 2446  O   HOH A2149      41.035 -37.683  14.871  1.00 50.60           O  
-HETATM 2447  O   HOH A2150      42.786 -40.342  11.875  1.00 43.69           O  
-HETATM 2448  O   HOH A2151      39.185 -32.775  19.142  1.00 46.42           O  
-HETATM 2449  O   HOH A2152      44.409 -34.892  16.323  1.00 53.13           O  
-HETATM 2450  O   HOH A2153      44.555 -31.377  14.448  1.00 37.22           O  
-HETATM 2451  O   HOH A2154      42.173 -37.810  12.828  1.00 31.83           O  
-HETATM 2452  O   HOH A2155      47.593 -42.088  12.160  1.00 58.76           O  
-HETATM 2453  O   HOH A2156      43.301 -42.359  13.364  1.00 56.42           O  
-HETATM 2454  O   HOH A2157      45.767 -43.292  12.447  1.00 58.33           O  
-HETATM 2455  O   HOH A2158      49.381 -35.936  10.773  1.00 32.39           O  
-HETATM 2456  O   HOH A2159      48.061 -33.493  13.698  1.00 30.94           O  
-HETATM 2457  O   HOH A2160      51.921 -31.139   9.652  1.00 51.55           O  
-HETATM 2458  O   HOH A2161      47.193 -31.361  14.670  1.00 44.37           O  
-HETATM 2459  O   HOH A2162      49.778 -30.838  15.040  1.00 46.44           O  
-HETATM 2460  O   HOH A2163      47.742 -36.019   3.216  1.00 25.53           O  
-HETATM 2461  O   HOH A2164      51.226 -41.965   6.094  1.00 55.27           O  
-HETATM 2462  O   HOH A2165      49.299 -41.777   9.911  1.00 61.06           O  
-HETATM 2463  O   HOH A2166      51.648 -38.063   5.016  1.00 40.89           O  
-HETATM 2464  O   HOH A2167      53.513 -31.874   4.145  1.00 47.92           O  
-HETATM 2465  O   HOH A2168      50.459 -36.121   3.616  1.00 26.29           O  
-HETATM 2466  O   HOH A2169      51.663 -34.692   8.299  1.00 44.28           O  
-HETATM 2467  O   HOH A2170      43.378 -37.027  -1.064  1.00 33.87           O  
-HETATM 2468  O   HOH A2171      38.288 -33.770  -5.183  1.00 25.48           O  
-HETATM 2469  O   HOH A2172      37.147 -36.178  -4.121  1.00 28.14           O  
-HETATM 2470  O   HOH A2173      40.073 -29.731 -10.212  1.00 30.60           O  
-HETATM 2471  O   HOH A2174      39.467 -23.018 -11.026  1.00 36.14           O  
-HETATM 2472  O   HOH A2175      41.751 -23.452 -10.716  1.00 31.79           O  
-HETATM 2473  O   HOH A2176      37.003 -28.803 -14.348  1.00 44.44           O  
-HETATM 2474  O   HOH A2177      35.460 -19.659 -14.773  1.00 48.47           O  
-HETATM 2475  O   HOH A2178      38.115 -18.745  -9.633  1.00 64.61           O  
-HETATM 2476  O   HOH A2179      32.767 -21.764  -4.691  1.00 25.66           O  
-HETATM 2477  O   HOH A2180      32.674 -22.141 -17.712  1.00 59.67           O  
-HETATM 2478  O   HOH A2181      39.497 -22.100 -14.441  1.00 46.49           O  
-HETATM 2479  O   HOH A2182      39.840 -27.940 -12.077  1.00 33.57           O  
-HETATM 2480  O   HOH A2183      38.957 -26.208 -18.655  1.00 55.73           O  
-HETATM 2481  O   HOH A2184      28.878 -18.906 -15.071  1.00 41.77           O  
-HETATM 2482  O   HOH A2185      25.251 -23.765  -2.144  1.00 28.66           O  
-HETATM 2483  O   HOH A2186      31.859 -20.327  -2.481  1.00 27.58           O  
-HETATM 2484  O   HOH A2187      28.748 -19.483   3.486  1.00 33.19           O  
-HETATM 2485  O   HOH A2188      30.671 -18.508   1.464  1.00 32.47           O  
-HETATM 2486  O   HOH A2189      23.686 -17.322  -1.268  1.00 31.94           O  
-HETATM 2487  O   HOH A2190      23.942 -13.930  -6.848  1.00 57.35           O  
-HETATM 2488  O   HOH A2191      21.257 -15.470  -2.126  1.00 49.97           O  
-HETATM 2489  O   HOH A2192      31.747 -20.821   0.356  1.00 24.18           O  
-HETATM 2490  O   HOH A2193      29.342 -21.934   4.335  1.00 25.70           O  
-HETATM 2491  O   HOH A2194      22.490 -22.234   5.048  1.00 59.50           O  
-HETATM 2492  O   HOH A2195      23.145 -24.211   1.094  1.00 32.70           O  
-HETATM 2493  O   HOH A2196      23.549 -23.971   5.210  1.00 39.57           O  
-HETATM 2494  O   HOH A2197      25.861 -24.239  10.089  1.00 61.71           O  
-HETATM 2495  O   HOH A2198      23.325 -23.410   9.419  1.00 65.46           O  
-HETATM 2496  O   HOH A2199      30.635 -26.172  10.769  1.00 42.98           O  
-HETATM 2497  O   HOH A2200      22.377 -26.052   7.932  1.00 58.35           O  
-HETATM 2498  O   HOH A2201      32.094 -46.635  -2.411  1.00 52.84           O  
-HETATM 2499  O   HOH A2202      33.303 -41.134  -4.980  1.00 39.43           O  
-HETATM 2500  O   HOH A2203      37.113 -50.323   1.123  1.00 69.87           O  
-HETATM 2501  O   HOH A2204      31.706 -51.308   2.841  1.00 68.46           O  
-HETATM 2502  O   HOH A2205      34.272 -48.306   5.097  1.00 60.61           O  
-HETATM 2503  O   HOH A2206      39.458 -43.713  -4.346  1.00 37.53           O  
-HETATM 2504  O   HOH A2207      31.326 -46.661  -6.084  1.00 61.90           O  
-HETATM 2505  O   HOH A2208      38.913 -46.222  -4.763  1.00 39.01           O  
-HETATM 2506  O   HOH A2209      39.333 -48.392  -8.039  1.00 48.64           O  
-HETATM 2507  O   HOH A2210      36.814 -49.381  -8.160  1.00 54.92           O  
-HETATM 2508  O   HOH A2211      35.447 -49.593  -3.024  1.00 64.66           O  
-HETATM 2509  O   HOH A2212      39.959 -40.266  -6.818  1.00 33.07           O  
-HETATM 2510  O   HOH A2213      23.520 -31.547  -4.026  1.00 35.21           O  
-HETATM 2511  O   HOH A2214      20.726 -20.812   1.149  1.00 45.28           O  
-HETATM 2512  O   HOH A2215      23.595 -16.566 -10.346  1.00 31.53           O  
-HETATM 2513  O   HOH A2216      25.900 -14.686 -10.566  1.00 38.00           O  
-HETATM 2514  O   HOH A2217      28.655 -14.785 -14.871  1.00 47.87           O  
-HETATM 2515  O   HOH A2218      33.107 -11.943  -7.951  1.00 25.17           O  
-HETATM 2516  O   HOH A2219      24.898 -12.474  -9.083  1.00 44.60           O  
-HETATM 2517  O   HOH A2220      24.615 -10.014  -6.301  1.00 45.64           O  
-HETATM 2518  O   HOH A2221      31.514 -11.026 -14.563  1.00 37.52           O  
-HETATM 2519  O   HOH A2222      33.786 -15.489 -14.261  1.00 55.21           O  
-HETATM 2520  O   HOH A2223      38.745 -12.098 -13.095  1.00 64.47           O  
-HETATM 2521  O   HOH A2224      36.758 -13.822 -16.303  1.00 55.41           O  
-HETATM 2522  O   HOH A2225      20.904 -11.566   0.410  1.00 40.70           O  
-HETATM 2523  O   HOH A2226      23.562 -15.979   6.159  1.00 43.35           O  
-HETATM 2524  O   HOH A2227      23.692 -18.456   8.695  1.00 41.43           O  
-HETATM 2525  O   HOH A2228      25.789 -18.960  10.748  1.00 33.91           O  
-HETATM 2526  O   HOH A2229      24.255 -13.641   6.582  1.00 34.81           O  
-HETATM 2527  O   HOH A2230      23.066  -9.203   7.332  1.00 55.99           O  
-HETATM 2528  O   HOH A2231      25.760  -7.729   8.335  1.00 46.06           O  
-HETATM 2529  O   HOH A2232      33.546 -19.333  12.098  1.00 26.17           O  
-HETATM 2530  O   HOH A2233      33.366 -16.277   9.089  1.00 27.55           O  
-HETATM 2531  O   HOH A2234      32.482 -16.914   2.681  1.00 31.89           O  
-HETATM 2532  O   HOH A2235      37.098  -7.452   4.513  1.00 43.39           O  
-HETATM 2533  O   HOH A2236      35.512 -10.488  -1.258  1.00 27.84           O  
-HETATM 2534  O   HOH A2237      29.505  -4.183  11.248  1.00 61.63           O  
-HETATM 2535  O   HOH A2238      25.793  -3.096   5.066  1.00 61.61           O  
-HETATM 2536  O   HOH A2239      30.011  -0.439   7.907  1.00 57.12           O  
-HETATM 2537  O   HOH A2240      32.172  -1.215   8.919  1.00 68.49           O  
-HETATM 2538  O   HOH A2241      25.462  -4.390  -0.603  1.00 46.67           O  
-HETATM 2539  O   HOH A2242      27.968  -1.376   1.501  1.00 58.80           O  
-HETATM 2540  O   HOH A2243      25.034  -4.465   6.304  1.00 68.22           O  
-HETATM 2541  O   HOH A2244      33.641  -6.144  -0.733  1.00 44.89           O  
-HETATM 2542  O   HOH A2245      32.882  -3.721  -1.600  1.00 49.50           O  
-HETATM 2543  O   HOH A2246      30.303  -0.763   0.603  1.00 63.60           O  
-HETATM 2544  O   HOH A2247      26.182  -2.857  -2.193  1.00 57.37           O  
-HETATM 2545  O   HOH A2248      35.589  -7.778  -2.204  1.00 28.14           O  
-HETATM 2546  O   HOH A2249      35.784 -13.488  -7.598  1.00 35.25           O  
-HETATM 2547  O   HOH A2250      31.937 -17.502  -2.524  1.00 27.72           O  
-HETATM 2548  O   HOH A2251      37.991 -19.137 -12.015  1.00 56.17           O  
-HETATM 2549  O   HOH A2252      39.666 -13.653 -11.366  1.00 62.14           O  
-HETATM 2550  O   HOH A2253      34.952 -31.566  17.830  1.00 48.94           O  
-HETATM 2551  O   HOH A2254      32.092 -25.548  15.460  1.00 38.26           O  
-HETATM 2552  O   HOH A2255      33.140 -22.077  17.662  1.00 49.83           O  
-HETATM 2553  O   HOH A2256      38.510 -19.280  18.328  1.00 57.74           O  
-HETATM 2554  O   HOH A2257      39.725 -17.985  16.803  1.00 41.12           O  
-HETATM 2555  O   HOH A2258      27.690 -14.489  13.241  1.00 43.40           O  
-HETATM 2556  O   HOH A2259      30.097 -23.878  16.362  1.00 45.02           O  
-HETATM 2557  O   HOH A2260      29.000 -18.635  20.526  1.00 77.74           O  
-HETATM 2558  O   HOH A2261      26.565 -12.079  16.025  1.00 45.80           O  
-HETATM 2559  O   HOH A2262      26.946  -7.306  13.486  1.00 58.07           O  
-HETATM 2560  O   HOH A2263      35.078  -6.721  16.298  1.00 41.99           O  
-HETATM 2561  O   HOH A2264      33.663 -10.672  20.533  1.00 60.59           O  
-HETATM 2562  O   HOH A2265      38.300 -12.471  15.951  1.00 30.01           O  
-HETATM 2563  O   HOH A2266      37.849 -15.272  17.763  1.00 49.72           O  
-HETATM 2564  O   HOH A2267      37.236  -6.241   9.352  1.00 41.05           O  
-HETATM 2565  O   HOH A2268      41.026  -6.615  13.316  1.00 66.68           O  
-HETATM 2566  O   HOH A2269      38.155 -11.457  18.608  1.00 32.69           O  
-HETATM 2567  O   HOH A2270      44.374  -6.748  19.245  1.00 65.94           O  
-HETATM 2568  O   HOH A2271      42.596 -12.316  10.014  1.00 29.21           O  
-HETATM 2569  O   HOH A2272      44.340 -10.329  12.218  1.00 47.31           O  
-HETATM 2570  O   HOH A2273      40.124 -15.310  19.072  1.00 46.85           O  
-HETATM 2571  O   HOH A2274      45.206 -14.302  14.160  1.00 29.36           O  
-HETATM 2572  O   HOH A2275      44.839 -15.352  19.370  1.00 37.57           O  
-HETATM 2573  O   HOH A2276      46.852 -19.344  18.512  1.00 34.64           O  
-HETATM 2574  O   HOH A2277      44.140 -27.371  24.507  1.00 41.39           O  
-HETATM 2575  O   HOH A2278      48.573 -24.694  18.078  1.00 24.88           O  
-HETATM 2576  O   HOH A2279      46.515 -30.228  21.648  1.00 51.69           O  
-HETATM 2577  O   HOH A2280      55.950 -26.691  17.573  1.00 34.35           O  
-HETATM 2578  O   HOH A2281      55.262 -26.128  13.814  1.00 27.26           O  
-HETATM 2579  O   HOH A2282      55.357 -29.217  13.245  1.00 55.77           O  
-HETATM 2580  O   HOH A2283      53.607 -28.955   8.628  1.00 49.87           O  
-HETATM 2581  O   HOH A2284      54.962 -26.308  10.152  1.00 34.46           O  
-HETATM 2582  O   HOH A2285      52.307 -19.950  11.977  1.00 36.37           O  
-HETATM 2583  O   HOH A2286      49.510 -16.179   7.491  1.00 31.65           O  
-HETATM 2584  O   HOH A2287      50.865 -16.351   9.997  1.00 38.33           O  
-HETATM 2585  O   HOH A2288      52.007 -14.920   2.878  1.00 57.42           O  
-HETATM 2586  O   HOH A2289      55.155 -20.600   4.513  1.00 57.87           O  
-HETATM 2587  O   HOH A2290      46.892 -12.803   6.445  1.00 47.73           O  
-HETATM 2588  O   HOH A2291      44.660 -13.907   9.823  1.00 34.11           O  
-HETATM 2589  O   HOH A2292      50.457 -18.024  11.715  1.00 34.77           O  
-HETATM 2590  O   HOH A2293      50.960 -16.342  14.081  1.00 44.07           O  
-HETATM 2591  O   HOH A2294      48.778 -12.585  -0.709  1.00 37.41           O  
-HETATM 2592  O   HOH A2295      44.112  -9.862   8.463  1.00 43.87           O  
-HETATM 2593  O   HOH A2296      44.608  -8.246   5.299  1.00 35.13           O  
-HETATM 2594  O   HOH A2297      41.371  -5.918  -0.195  1.00 53.35           O  
-HETATM 2595  O   HOH A2298      47.392  -4.166  -1.291  1.00 64.46           O  
-HETATM 2596  O   HOH A2299      43.427  -3.254  -2.193  1.00 53.63           O  
-HETATM 2597  O   HOH A2300      40.425  -4.692   6.432  1.00 58.63           O  
-HETATM 2598  O   HOH A2301      42.608 -12.711  -2.857  1.00 33.97           O  
-HETATM 2599  O   HOH A2302      40.312  -9.224  -3.743  1.00 44.58           O  
-HETATM 2600  O   HOH A2303      40.313  -6.500  -2.163  1.00 43.42           O  
-HETATM 2601  O   HOH A2304      44.951 -10.359  -4.532  1.00 49.38           O  
-HETATM 2602  O   HOH A2305      48.442 -12.044   4.091  1.00 58.49           O  
-HETATM 2603  O   HOH A2306      47.051 -13.673  -3.350  1.00 40.86           O  
-HETATM 2604  O   HOH A2307      41.387 -15.266  -2.974  1.00 34.88           O  
-HETATM 2605  O   HOH A2308      48.095 -17.515  -8.260  1.00 35.15           O  
-HETATM 2606  O   HOH A2309      42.278 -18.638  -7.787  1.00 41.11           O  
-HETATM 2607  O   HOH A2310      44.347 -19.970  -8.628  1.00 28.57           O  
-HETATM 2608  O   HOH A2311      46.113 -19.163 -10.380  1.00 51.85           O  
-HETATM 2609  O   HOH A2312      50.237 -18.210 -12.005  1.00 59.34           O  
-HETATM 2610  O   HOH A2313      50.862 -18.446  -7.709  1.00 55.78           O  
-HETATM 2611  O   HOH A2314      51.859 -23.715  -9.896  1.00 43.80           O  
-HETATM 2612  O   HOH A2315      51.826 -20.566  -1.812  1.00 35.76           O  
-HETATM 2613  O   HOH A2316      52.519 -16.505  -3.548  1.00 48.47           O  
-HETATM 2614  O   HOH A2317      50.345 -13.415  -2.452  1.00 50.90           O  
-HETATM 2615  O   HOH A2318      55.318 -22.466  -1.727  1.00 49.02           O  
-HETATM 2616  O   HOH A2319      54.942 -26.348  -2.904  1.00 66.10           O  
-HETATM 2617  O   HOH A2320      56.028 -24.941  -1.080  1.00 60.24           O  
-HETATM 2618  O   HOH A2321      52.943 -25.973  -9.110  1.00 47.76           O  
-HETATM 2619  O   HOH A2322      53.100 -27.438  -5.919  1.00 54.41           O  
-HETATM 2620  O   HOH A2323      51.717 -20.194  -6.303  1.00 38.32           O  
-HETATM 2621  O   HOH A2324      56.361 -28.782   2.472  1.00 54.80           O  
-HETATM 2622  O   HOH A2325      50.952 -30.860  -3.479  1.00 51.04           O  
-HETATM 2623  O   HOH A2326      53.526 -32.283  -3.212  1.00 53.49           O  
-HETATM 2624  O   HOH A2327      52.368 -39.113   0.570  1.00 63.40           O  
-HETATM 2625  O   HOH A2328      51.049 -40.327  -1.485  1.00 56.98           O  
-HETATM 2626  O   HOH A2329      43.843 -43.745  -4.473  1.00 44.57           O  
-HETATM 2627  O   HOH A2330      52.720 -42.009   1.144  1.00 67.98           O  
-HETATM 2628  O   HOH A2331      46.263 -46.481  10.520  1.00 56.74           O  
-HETATM 2629  O   HOH A2332      38.382 -51.727   4.776  1.00 67.44           O  
-HETATM 2630  O   HOH A2333      39.162 -51.908   9.516  1.00 71.24           O  
-HETATM 2631  O   HOH A2334      34.924 -50.540  10.321  1.00 78.71           O  
-HETATM 2632  O   HOH A2335      38.322 -48.753  13.467  1.00 79.48           O  
-HETATM 2633  O   HOH A2336      20.311 -31.019   5.527  1.00 41.21           O  
-HETATM 2634  O   HOH A2337      22.622 -34.582   3.897  1.00 38.55           O  
-CONECT 2265 2266 2269                                                           
-CONECT 2266 2265 2267                                                           
-CONECT 2267 2266 2268                                                           
-CONECT 2268 2267 2269                                                           
-CONECT 2269 2265 2268                                                           
-CONECT 2270 2271 2276                                                           
-CONECT 2271 2270 2272                                                           
-CONECT 2272 2271 2273 2274                                                      
-CONECT 2273 2272                                                                
-CONECT 2274 2272 2275                                                           
-CONECT 2275 2274 2276                                                           
-CONECT 2276 2270 2275 2277                                                      
-CONECT 2277 2276 2278                                                           
-CONECT 2278 2277 2279 2292                                                      
-CONECT 2279 2278 2280                                                           
-CONECT 2280 2279 2281 2289                                                      
-CONECT 2281 2280 2282 2287                                                      
-CONECT 2282 2281 2283                                                           
-CONECT 2283 2282 2284 2285                                                      
-CONECT 2284 2283                                                                
-CONECT 2285 2283 2286                                                           
-CONECT 2286 2285 2287                                                           
-CONECT 2287 2281 2286 2288                                                      
-CONECT 2288 2287 2289                                                           
-CONECT 2289 2280 2288 2290                                                      
-CONECT 2290 2289 2291 2292                                                      
-CONECT 2291 2290                                                                
-CONECT 2292 2278 2290                                                           
-CONECT 2293 2294 2297                                                           
-CONECT 2294 2293 2295                                                           
-CONECT 2295 2294 2296                                                           
-CONECT 2296 2295 2297                                                           
-CONECT 2297 2293 2296                                                           
-MASTER      511    0    3   15   12    0    8    6 2633    1   33   26          
-END                                                                             
diff --git a/plip/test/pdb/4kya.pdb b/plip/test/pdb/4kya.pdb
deleted file mode 100644
index 3a32d70..0000000
--- a/plip/test/pdb/4kya.pdb
+++ /dev/null
@@ -1,36156 +0,0 @@
-HEADER    OXIDOREDUCTASE, TRANSFERASE/INHIBITOR   28-MAY-13   4KYA              
-TITLE     CRYSTAL STRUCTURE OF NON-CLASSICAL TS INHIBITOR 3 IN COMPLEX WITH     
-TITLE    2 TOXOPLASMA GONDII TS-DHFR                                            
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: BIFUNCTIONAL DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE; 
-COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
-COMPND   4 SYNONYM: DHFR-TS, DIHYDROFOLATE REDUCTASE, THYMIDYLATE SYNTHASE;     
-COMPND   5 EC: 1.5.1.3, 2.1.1.45;                                               
-COMPND   6 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;                              
-SOURCE   3 ORGANISM_TAXID: 5811;                                                
-SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
-KEYWDS    SYNTHASE, BIFUNCTIONAL, CHIMERA PROTEIN, OXIDOREDUCTASE, TRANSFERASE- 
-KEYWDS   2 INHIBITOR COMPLEX                                                    
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    H.SHARMA,K.S.ANDERSON                                                 
-REVDAT   1   06-AUG-14 4KYA    0                                                
-JRNL        AUTH   N.ZAWARE,H.SHARMA,J.YANG,R.K.DEVAMBATLA,S.F.QUEENER,         
-JRNL        AUTH 2 K.S.ANDERSON,A.GANGJEE                                       
-JRNL        TITL   DISCOVERY OF POTENT AND SELECTIVE INHIBITORS OF TOXOPLASMA   
-JRNL        TITL 2 GONDII THYMIDYLATE SYNTHASE FOR OPPORTUNISTIC INFECTIONS.    
-JRNL        REF    ACS MED CHEM LETT             V.   4  1148 2013              
-JRNL        REFN                                                                
-JRNL        PMID   24470841                                                     
-JRNL        DOI    10.1021/ML400208V                                            
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    3.26 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : ML                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.26                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.66                          
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
-REMARK   3   NUMBER OF REFLECTIONS             : 81456                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
-REMARK   3   R VALUE            (WORKING SET) : 0.182                           
-REMARK   3   FREE R VALUE                     : 0.241                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 4069                            
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 46.6619 -  9.9944    0.98     2683   131  0.2063 0.2464        
-REMARK   3     2  9.9944 -  7.9456    1.00     2693   136  0.1609 0.1929        
-REMARK   3     3  7.9456 -  6.9449    1.00     2706   128  0.1782 0.2658        
-REMARK   3     4  6.9449 -  6.3116    1.00     2698   155  0.1849 0.2273        
-REMARK   3     5  6.3116 -  5.8601    1.00     2654   152  0.1904 0.2312        
-REMARK   3     6  5.8601 -  5.5152    1.00     2749   118  0.1791 0.1984        
-REMARK   3     7  5.5152 -  5.2394    0.99     2705   143  0.1821 0.2527        
-REMARK   3     8  5.2394 -  5.0116    0.99     2670   131  0.1651 0.2627        
-REMARK   3     9  5.0116 -  4.8189    0.99     2609   161  0.1643 0.2076        
-REMARK   3    10  4.8189 -  4.6527    0.99     2769   156  0.1645 0.2132        
-REMARK   3    11  4.6527 -  4.5074    0.99     2595   143  0.1403 0.1887        
-REMARK   3    12  4.5074 -  4.3786    0.99     2745   147  0.1438 0.2122        
-REMARK   3    13  4.3786 -  4.2634    0.99     2679   150  0.1611 0.2026        
-REMARK   3    14  4.2634 -  4.1595    0.99     2657   138  0.1516 0.2161        
-REMARK   3    15  4.1595 -  4.0650    0.99     2646   165  0.1615 0.2394        
-REMARK   3    16  4.0650 -  3.9785    0.99     2768   108  0.1733 0.2011        
-REMARK   3    17  3.9785 -  3.8990    0.99     2669   145  0.1775 0.2338        
-REMARK   3    18  3.8990 -  3.8254    0.99     2552   143  0.1834 0.2609        
-REMARK   3    19  3.8254 -  3.7572    0.99     2745   136  0.1868 0.2633        
-REMARK   3    20  3.7572 -  3.6935    0.99     2715   152  0.1942 0.2633        
-REMARK   3    21  3.6935 -  3.6339    0.99     2685   127  0.1971 0.2485        
-REMARK   3    22  3.6339 -  3.5780    0.99     2638   154  0.1902 0.2435        
-REMARK   3    23  3.5780 -  3.5254    0.99     2691   124  0.2087 0.2606        
-REMARK   3    24  3.5254 -  3.4758    0.99     2709   153  0.2064 0.2844        
-REMARK   3    25  3.4758 -  3.4288    0.98     2669   131  0.2244 0.3336        
-REMARK   3    26  3.4288 -  3.3843    0.98     2620   134  0.2419 0.2853        
-REMARK   3    27  3.3843 -  3.3420    0.98     2596   136  0.2377 0.3155        
-REMARK   3    28  3.3420 -  3.3018    0.98     2686   138  0.2445 0.3342        
-REMARK   3    29  3.3018 -  3.2634    0.88     2386   134  0.2270 0.3093        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.11                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
-REMARK   3   K_SOL              : NULL                                          
-REMARK   3   B_SOL              : NULL                                          
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.560           
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.67                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -0.47000                                             
-REMARK   3    B22 (A**2) : -2.30000                                             
-REMARK   3    B33 (A**2) : 2.77000                                              
-REMARK   3    B12 (A**2) : -0.17000                                             
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.13000                                              
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.003          34064                                  
-REMARK   3   ANGLE     :  0.765          46292                                  
-REMARK   3   CHIRALITY :  0.029           4996                                  
-REMARK   3   PLANARITY :  0.004           5856                                  
-REMARK   3   DIHEDRAL  : 15.467          12288                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
-REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
-REMARK   4                                                                      
-REMARK   4 4KYA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-14.                  
-REMARK 100 THE RCSB ID CODE IS RCSB079946.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 13-APR-13; NULL                    
-REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
-REMARK 200  PH                             : 7.3                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y; NULL                            
-REMARK 200  RADIATION SOURCE               : NSLS; NULL                         
-REMARK 200  BEAMLINE                       : X25; NULL                          
-REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1; NULL                          
-REMARK 200  MONOCHROMATOR                  : SI 111; NULL                       
-REMARK 200  OPTICS                         : NULL; NULL                         
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
-REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M; NULL               
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
-REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81521                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.263                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 46.657                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.26                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.35                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASER                                                
-REMARK 200 STARTING MODEL: PDB ENTRY 4EIL                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 53.93                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.1 M POTASSIUM FORMATE,   
-REMARK 280  PH 7.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 6670 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 41200 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 6660 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 41270 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 3                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 6680 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 41170 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 4                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 6640 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 41200 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A     1                                                      
-REMARK 465     GLN A     2                                                      
-REMARK 465     LYS A     3                                                      
-REMARK 465     GLU A    44                                                      
-REMARK 465     GLU A    45                                                      
-REMARK 465     SER A   216                                                      
-REMARK 465     THR A   217                                                      
-REMARK 465     ALA A   218                                                      
-REMARK 465     ALA A   219                                                      
-REMARK 465     GLU A   220                                                      
-REMARK 465     LYS A   221                                                      
-REMARK 465     ASP A   222                                                      
-REMARK 465     ASN A   223                                                      
-REMARK 465     GLU A   224                                                      
-REMARK 465     LYS A   253                                                      
-REMARK 465     THR A   254                                                      
-REMARK 465     ASP A   255                                                      
-REMARK 465     ASP A   256                                                      
-REMARK 465     ALA A   257                                                      
-REMARK 465     ALA A   258                                                      
-REMARK 465     THR A   259                                                      
-REMARK 465     ALA A   260                                                      
-REMARK 465     GLU A   261                                                      
-REMARK 465     PRO A   262                                                      
-REMARK 465     SER A   263                                                      
-REMARK 465     ASN A   264                                                      
-REMARK 465     ALA A   265                                                      
-REMARK 465     MET A   266                                                      
-REMARK 465     SER A   267                                                      
-REMARK 465     SER A   268                                                      
-REMARK 465     LEU A   269                                                      
-REMARK 465     THR A   270                                                      
-REMARK 465     SER A   271                                                      
-REMARK 465     THR A   272                                                      
-REMARK 465     ARG A   273                                                      
-REMARK 465     GLU A   274                                                      
-REMARK 465     THR A   275                                                      
-REMARK 465     THR A   276                                                      
-REMARK 465     PRO A   277                                                      
-REMARK 465     VAL A   278                                                      
-REMARK 465     HIS A   279                                                      
-REMARK 465     GLY A   280                                                      
-REMARK 465     LEU A   281                                                      
-REMARK 465     GLN A   282                                                      
-REMARK 465     ALA A   283                                                      
-REMARK 465     PRO A   284                                                      
-REMARK 465     GLU A   300                                                      
-REMARK 465     ASP A   301                                                      
-REMARK 465     ARG A   302                                                      
-REMARK 465     LYS A   303                                                      
-REMARK 465     LYS A   304                                                      
-REMARK 465     ARG A   305                                                      
-REMARK 465     GLU A   306                                                      
-REMARK 465     GLN A   307                                                      
-REMARK 465     LYS A   308                                                      
-REMARK 465     GLU A   309                                                      
-REMARK 465     MET B     1                                                      
-REMARK 465     GLN B     2                                                      
-REMARK 465     THR B    67                                                      
-REMARK 465     PRO B    68                                                      
-REMARK 465     GLU B    69                                                      
-REMARK 465     GLU B    70                                                      
-REMARK 465     ALA B    71                                                      
-REMARK 465     SER B    72                                                      
-REMARK 465     ARG B    73                                                      
-REMARK 465     GLU B   108                                                      
-REMARK 465     GLU B   109                                                      
-REMARK 465     ASP B   110                                                      
-REMARK 465     ILE B   111                                                      
-REMARK 465     ALA B   112                                                      
-REMARK 465     ALA B   113                                                      
-REMARK 465     GLU B   114                                                      
-REMARK 465     LYS B   115                                                      
-REMARK 465     PRO B   116                                                      
-REMARK 465     GLN B   117                                                      
-REMARK 465     ALA B   118                                                      
-REMARK 465     GLU B   119                                                      
-REMARK 465     GLY B   120                                                      
-REMARK 465     GLN B   121                                                      
-REMARK 465     GLN B   122                                                      
-REMARK 465     ARG B   123                                                      
-REMARK 465     VAL B   124                                                      
-REMARK 465     ARG B   125                                                      
-REMARK 465     GLY B   152                                                      
-REMARK 465     SER B   216                                                      
-REMARK 465     THR B   217                                                      
-REMARK 465     ALA B   218                                                      
-REMARK 465     ALA B   219                                                      
-REMARK 465     GLU B   220                                                      
-REMARK 465     LYS B   221                                                      
-REMARK 465     ASP B   222                                                      
-REMARK 465     ASN B   223                                                      
-REMARK 465     ARG B   252                                                      
-REMARK 465     LYS B   253                                                      
-REMARK 465     THR B   254                                                      
-REMARK 465     ASP B   255                                                      
-REMARK 465     ASP B   256                                                      
-REMARK 465     ALA B   257                                                      
-REMARK 465     ALA B   258                                                      
-REMARK 465     THR B   259                                                      
-REMARK 465     ALA B   260                                                      
-REMARK 465     GLU B   261                                                      
-REMARK 465     PRO B   262                                                      
-REMARK 465     SER B   263                                                      
-REMARK 465     ASN B   264                                                      
-REMARK 465     ALA B   265                                                      
-REMARK 465     MET B   266                                                      
-REMARK 465     SER B   267                                                      
-REMARK 465     SER B   268                                                      
-REMARK 465     LEU B   269                                                      
-REMARK 465     THR B   270                                                      
-REMARK 465     SER B   271                                                      
-REMARK 465     THR B   272                                                      
-REMARK 465     ARG B   273                                                      
-REMARK 465     GLU B   274                                                      
-REMARK 465     THR B   275                                                      
-REMARK 465     THR B   276                                                      
-REMARK 465     PRO B   277                                                      
-REMARK 465     VAL B   278                                                      
-REMARK 465     HIS B   279                                                      
-REMARK 465     GLY B   280                                                      
-REMARK 465     LEU B   281                                                      
-REMARK 465     GLN B   282                                                      
-REMARK 465     ALA B   283                                                      
-REMARK 465     PRO B   284                                                      
-REMARK 465     ARG B   302                                                      
-REMARK 465     LYS B   303                                                      
-REMARK 465     LYS B   304                                                      
-REMARK 465     ARG B   305                                                      
-REMARK 465     GLU B   306                                                      
-REMARK 465     GLN B   307                                                      
-REMARK 465     MET C     1                                                      
-REMARK 465     GLN C     2                                                      
-REMARK 465     LYS C     3                                                      
-REMARK 465     GLU C    44                                                      
-REMARK 465     GLU C    45                                                      
-REMARK 465     SER C   216                                                      
-REMARK 465     THR C   217                                                      
-REMARK 465     ALA C   218                                                      
-REMARK 465     ALA C   219                                                      
-REMARK 465     GLU C   220                                                      
-REMARK 465     LYS C   221                                                      
-REMARK 465     ASP C   222                                                      
-REMARK 465     ASN C   223                                                      
-REMARK 465     GLU C   224                                                      
-REMARK 465     LYS C   253                                                      
-REMARK 465     THR C   254                                                      
-REMARK 465     ASP C   255                                                      
-REMARK 465     ASP C   256                                                      
-REMARK 465     ALA C   257                                                      
-REMARK 465     ALA C   258                                                      
-REMARK 465     THR C   259                                                      
-REMARK 465     ALA C   260                                                      
-REMARK 465     GLU C   261                                                      
-REMARK 465     PRO C   262                                                      
-REMARK 465     SER C   263                                                      
-REMARK 465     ASN C   264                                                      
-REMARK 465     ALA C   265                                                      
-REMARK 465     MET C   266                                                      
-REMARK 465     SER C   267                                                      
-REMARK 465     SER C   268                                                      
-REMARK 465     LEU C   269                                                      
-REMARK 465     THR C   270                                                      
-REMARK 465     SER C   271                                                      
-REMARK 465     THR C   272                                                      
-REMARK 465     ARG C   273                                                      
-REMARK 465     GLU C   274                                                      
-REMARK 465     THR C   275                                                      
-REMARK 465     THR C   276                                                      
-REMARK 465     PRO C   277                                                      
-REMARK 465     VAL C   278                                                      
-REMARK 465     HIS C   279                                                      
-REMARK 465     GLY C   280                                                      
-REMARK 465     LEU C   281                                                      
-REMARK 465     GLN C   282                                                      
-REMARK 465     ALA C   283                                                      
-REMARK 465     PRO C   284                                                      
-REMARK 465     GLU C   300                                                      
-REMARK 465     ASP C   301                                                      
-REMARK 465     ARG C   302                                                      
-REMARK 465     LYS C   303                                                      
-REMARK 465     LYS C   304                                                      
-REMARK 465     ARG C   305                                                      
-REMARK 465     GLU C   306                                                      
-REMARK 465     GLN C   307                                                      
-REMARK 465     LYS C   308                                                      
-REMARK 465     GLU C   309                                                      
-REMARK 465     MET D     1                                                      
-REMARK 465     GLN D     2                                                      
-REMARK 465     THR D    67                                                      
-REMARK 465     PRO D    68                                                      
-REMARK 465     GLU D    69                                                      
-REMARK 465     GLU D    70                                                      
-REMARK 465     ALA D    71                                                      
-REMARK 465     SER D    72                                                      
-REMARK 465     ARG D    73                                                      
-REMARK 465     GLU D   108                                                      
-REMARK 465     GLU D   109                                                      
-REMARK 465     ASP D   110                                                      
-REMARK 465     ILE D   111                                                      
-REMARK 465     ALA D   112                                                      
-REMARK 465     ALA D   113                                                      
-REMARK 465     GLU D   114                                                      
-REMARK 465     LYS D   115                                                      
-REMARK 465     PRO D   116                                                      
-REMARK 465     GLN D   117                                                      
-REMARK 465     ALA D   118                                                      
-REMARK 465     GLU D   119                                                      
-REMARK 465     GLY D   120                                                      
-REMARK 465     GLN D   121                                                      
-REMARK 465     GLN D   122                                                      
-REMARK 465     ARG D   123                                                      
-REMARK 465     VAL D   124                                                      
-REMARK 465     ARG D   125                                                      
-REMARK 465     GLY D   152                                                      
-REMARK 465     SER D   216                                                      
-REMARK 465     THR D   217                                                      
-REMARK 465     ALA D   218                                                      
-REMARK 465     ALA D   219                                                      
-REMARK 465     GLU D   220                                                      
-REMARK 465     LYS D   221                                                      
-REMARK 465     ASP D   222                                                      
-REMARK 465     ASN D   223                                                      
-REMARK 465     ARG D   252                                                      
-REMARK 465     LYS D   253                                                      
-REMARK 465     THR D   254                                                      
-REMARK 465     ASP D   255                                                      
-REMARK 465     ASP D   256                                                      
-REMARK 465     ALA D   257                                                      
-REMARK 465     ALA D   258                                                      
-REMARK 465     THR D   259                                                      
-REMARK 465     ALA D   260                                                      
-REMARK 465     GLU D   261                                                      
-REMARK 465     PRO D   262                                                      
-REMARK 465     SER D   263                                                      
-REMARK 465     ASN D   264                                                      
-REMARK 465     ALA D   265                                                      
-REMARK 465     MET D   266                                                      
-REMARK 465     SER D   267                                                      
-REMARK 465     SER D   268                                                      
-REMARK 465     LEU D   269                                                      
-REMARK 465     THR D   270                                                      
-REMARK 465     SER D   271                                                      
-REMARK 465     THR D   272                                                      
-REMARK 465     ARG D   273                                                      
-REMARK 465     GLU D   274                                                      
-REMARK 465     THR D   275                                                      
-REMARK 465     THR D   276                                                      
-REMARK 465     PRO D   277                                                      
-REMARK 465     VAL D   278                                                      
-REMARK 465     HIS D   279                                                      
-REMARK 465     GLY D   280                                                      
-REMARK 465     LEU D   281                                                      
-REMARK 465     GLN D   282                                                      
-REMARK 465     ALA D   283                                                      
-REMARK 465     PRO D   284                                                      
-REMARK 465     ARG D   302                                                      
-REMARK 465     LYS D   303                                                      
-REMARK 465     LYS D   304                                                      
-REMARK 465     ARG D   305                                                      
-REMARK 465     GLU D   306                                                      
-REMARK 465     GLN D   307                                                      
-REMARK 465     MET E     1                                                      
-REMARK 465     GLN E     2                                                      
-REMARK 465     LYS E     3                                                      
-REMARK 465     GLU E    44                                                      
-REMARK 465     GLU E    45                                                      
-REMARK 465     SER E   216                                                      
-REMARK 465     THR E   217                                                      
-REMARK 465     ALA E   218                                                      
-REMARK 465     ALA E   219                                                      
-REMARK 465     GLU E   220                                                      
-REMARK 465     LYS E   221                                                      
-REMARK 465     ASP E   222                                                      
-REMARK 465     ASN E   223                                                      
-REMARK 465     GLU E   224                                                      
-REMARK 465     LYS E   253                                                      
-REMARK 465     THR E   254                                                      
-REMARK 465     ASP E   255                                                      
-REMARK 465     ASP E   256                                                      
-REMARK 465     ALA E   257                                                      
-REMARK 465     ALA E   258                                                      
-REMARK 465     THR E   259                                                      
-REMARK 465     ALA E   260                                                      
-REMARK 465     GLU E   261                                                      
-REMARK 465     PRO E   262                                                      
-REMARK 465     SER E   263                                                      
-REMARK 465     ASN E   264                                                      
-REMARK 465     ALA E   265                                                      
-REMARK 465     MET E   266                                                      
-REMARK 465     SER E   267                                                      
-REMARK 465     SER E   268                                                      
-REMARK 465     LEU E   269                                                      
-REMARK 465     THR E   270                                                      
-REMARK 465     SER E   271                                                      
-REMARK 465     THR E   272                                                      
-REMARK 465     ARG E   273                                                      
-REMARK 465     GLU E   274                                                      
-REMARK 465     THR E   275                                                      
-REMARK 465     THR E   276                                                      
-REMARK 465     PRO E   277                                                      
-REMARK 465     VAL E   278                                                      
-REMARK 465     HIS E   279                                                      
-REMARK 465     GLY E   280                                                      
-REMARK 465     LEU E   281                                                      
-REMARK 465     GLN E   282                                                      
-REMARK 465     ALA E   283                                                      
-REMARK 465     PRO E   284                                                      
-REMARK 465     GLU E   300                                                      
-REMARK 465     ASP E   301                                                      
-REMARK 465     ARG E   302                                                      
-REMARK 465     LYS E   303                                                      
-REMARK 465     LYS E   304                                                      
-REMARK 465     ARG E   305                                                      
-REMARK 465     GLU E   306                                                      
-REMARK 465     GLN E   307                                                      
-REMARK 465     LYS E   308                                                      
-REMARK 465     GLU E   309                                                      
-REMARK 465     MET F     1                                                      
-REMARK 465     GLN F     2                                                      
-REMARK 465     THR F    67                                                      
-REMARK 465     PRO F    68                                                      
-REMARK 465     GLU F    69                                                      
-REMARK 465     GLU F    70                                                      
-REMARK 465     ALA F    71                                                      
-REMARK 465     SER F    72                                                      
-REMARK 465     ARG F    73                                                      
-REMARK 465     GLU F   108                                                      
-REMARK 465     GLU F   109                                                      
-REMARK 465     ASP F   110                                                      
-REMARK 465     ILE F   111                                                      
-REMARK 465     ALA F   112                                                      
-REMARK 465     ALA F   113                                                      
-REMARK 465     GLU F   114                                                      
-REMARK 465     LYS F   115                                                      
-REMARK 465     PRO F   116                                                      
-REMARK 465     GLN F   117                                                      
-REMARK 465     ALA F   118                                                      
-REMARK 465     GLU F   119                                                      
-REMARK 465     GLY F   120                                                      
-REMARK 465     GLN F   121                                                      
-REMARK 465     GLN F   122                                                      
-REMARK 465     ARG F   123                                                      
-REMARK 465     VAL F   124                                                      
-REMARK 465     ARG F   125                                                      
-REMARK 465     GLY F   152                                                      
-REMARK 465     SER F   216                                                      
-REMARK 465     THR F   217                                                      
-REMARK 465     ALA F   218                                                      
-REMARK 465     ALA F   219                                                      
-REMARK 465     GLU F   220                                                      
-REMARK 465     LYS F   221                                                      
-REMARK 465     ASP F   222                                                      
-REMARK 465     ASN F   223                                                      
-REMARK 465     ARG F   252                                                      
-REMARK 465     LYS F   253                                                      
-REMARK 465     THR F   254                                                      
-REMARK 465     ASP F   255                                                      
-REMARK 465     ASP F   256                                                      
-REMARK 465     ALA F   257                                                      
-REMARK 465     ALA F   258                                                      
-REMARK 465     THR F   259                                                      
-REMARK 465     ALA F   260                                                      
-REMARK 465     GLU F   261                                                      
-REMARK 465     PRO F   262                                                      
-REMARK 465     SER F   263                                                      
-REMARK 465     ASN F   264                                                      
-REMARK 465     ALA F   265                                                      
-REMARK 465     MET F   266                                                      
-REMARK 465     SER F   267                                                      
-REMARK 465     SER F   268                                                      
-REMARK 465     LEU F   269                                                      
-REMARK 465     THR F   270                                                      
-REMARK 465     SER F   271                                                      
-REMARK 465     THR F   272                                                      
-REMARK 465     ARG F   273                                                      
-REMARK 465     GLU F   274                                                      
-REMARK 465     THR F   275                                                      
-REMARK 465     THR F   276                                                      
-REMARK 465     PRO F   277                                                      
-REMARK 465     VAL F   278                                                      
-REMARK 465     HIS F   279                                                      
-REMARK 465     GLY F   280                                                      
-REMARK 465     LEU F   281                                                      
-REMARK 465     GLN F   282                                                      
-REMARK 465     ALA F   283                                                      
-REMARK 465     PRO F   284                                                      
-REMARK 465     ARG F   302                                                      
-REMARK 465     LYS F   303                                                      
-REMARK 465     LYS F   304                                                      
-REMARK 465     ARG F   305                                                      
-REMARK 465     GLU F   306                                                      
-REMARK 465     GLN F   307                                                      
-REMARK 465     MET G     1                                                      
-REMARK 465     GLN G     2                                                      
-REMARK 465     LYS G     3                                                      
-REMARK 465     GLU G    44                                                      
-REMARK 465     GLU G    45                                                      
-REMARK 465     SER G   216                                                      
-REMARK 465     THR G   217                                                      
-REMARK 465     ALA G   218                                                      
-REMARK 465     ALA G   219                                                      
-REMARK 465     GLU G   220                                                      
-REMARK 465     LYS G   221                                                      
-REMARK 465     ASP G   222                                                      
-REMARK 465     ASN G   223                                                      
-REMARK 465     GLU G   224                                                      
-REMARK 465     LYS G   253                                                      
-REMARK 465     THR G   254                                                      
-REMARK 465     ASP G   255                                                      
-REMARK 465     ASP G   256                                                      
-REMARK 465     ALA G   257                                                      
-REMARK 465     ALA G   258                                                      
-REMARK 465     THR G   259                                                      
-REMARK 465     ALA G   260                                                      
-REMARK 465     GLU G   261                                                      
-REMARK 465     PRO G   262                                                      
-REMARK 465     SER G   263                                                      
-REMARK 465     ASN G   264                                                      
-REMARK 465     ALA G   265                                                      
-REMARK 465     MET G   266                                                      
-REMARK 465     SER G   267                                                      
-REMARK 465     SER G   268                                                      
-REMARK 465     LEU G   269                                                      
-REMARK 465     THR G   270                                                      
-REMARK 465     SER G   271                                                      
-REMARK 465     THR G   272                                                      
-REMARK 465     ARG G   273                                                      
-REMARK 465     GLU G   274                                                      
-REMARK 465     THR G   275                                                      
-REMARK 465     THR G   276                                                      
-REMARK 465     PRO G   277                                                      
-REMARK 465     VAL G   278                                                      
-REMARK 465     HIS G   279                                                      
-REMARK 465     GLY G   280                                                      
-REMARK 465     LEU G   281                                                      
-REMARK 465     GLN G   282                                                      
-REMARK 465     ALA G   283                                                      
-REMARK 465     PRO G   284                                                      
-REMARK 465     GLU G   300                                                      
-REMARK 465     ASP G   301                                                      
-REMARK 465     ARG G   302                                                      
-REMARK 465     LYS G   303                                                      
-REMARK 465     LYS G   304                                                      
-REMARK 465     ARG G   305                                                      
-REMARK 465     GLU G   306                                                      
-REMARK 465     GLN G   307                                                      
-REMARK 465     LYS G   308                                                      
-REMARK 465     GLU G   309                                                      
-REMARK 465     MET H     1                                                      
-REMARK 465     GLN H     2                                                      
-REMARK 465     THR H    67                                                      
-REMARK 465     PRO H    68                                                      
-REMARK 465     GLU H    69                                                      
-REMARK 465     GLU H    70                                                      
-REMARK 465     ALA H    71                                                      
-REMARK 465     SER H    72                                                      
-REMARK 465     ARG H    73                                                      
-REMARK 465     GLU H   108                                                      
-REMARK 465     GLU H   109                                                      
-REMARK 465     ASP H   110                                                      
-REMARK 465     ILE H   111                                                      
-REMARK 465     ALA H   112                                                      
-REMARK 465     ALA H   113                                                      
-REMARK 465     GLU H   114                                                      
-REMARK 465     LYS H   115                                                      
-REMARK 465     PRO H   116                                                      
-REMARK 465     GLN H   117                                                      
-REMARK 465     ALA H   118                                                      
-REMARK 465     GLU H   119                                                      
-REMARK 465     GLY H   120                                                      
-REMARK 465     GLN H   121                                                      
-REMARK 465     GLN H   122                                                      
-REMARK 465     ARG H   123                                                      
-REMARK 465     VAL H   124                                                      
-REMARK 465     ARG H   125                                                      
-REMARK 465     GLY H   152                                                      
-REMARK 465     SER H   216                                                      
-REMARK 465     THR H   217                                                      
-REMARK 465     ALA H   218                                                      
-REMARK 465     ALA H   219                                                      
-REMARK 465     GLU H   220                                                      
-REMARK 465     LYS H   221                                                      
-REMARK 465     ASP H   222                                                      
-REMARK 465     ASN H   223                                                      
-REMARK 465     ARG H   252                                                      
-REMARK 465     LYS H   253                                                      
-REMARK 465     THR H   254                                                      
-REMARK 465     ASP H   255                                                      
-REMARK 465     ASP H   256                                                      
-REMARK 465     ALA H   257                                                      
-REMARK 465     ALA H   258                                                      
-REMARK 465     THR H   259                                                      
-REMARK 465     ALA H   260                                                      
-REMARK 465     GLU H   261                                                      
-REMARK 465     PRO H   262                                                      
-REMARK 465     SER H   263                                                      
-REMARK 465     ASN H   264                                                      
-REMARK 465     ALA H   265                                                      
-REMARK 465     MET H   266                                                      
-REMARK 465     SER H   267                                                      
-REMARK 465     SER H   268                                                      
-REMARK 465     LEU H   269                                                      
-REMARK 465     THR H   270                                                      
-REMARK 465     SER H   271                                                      
-REMARK 465     THR H   272                                                      
-REMARK 465     ARG H   273                                                      
-REMARK 465     GLU H   274                                                      
-REMARK 465     THR H   275                                                      
-REMARK 465     THR H   276                                                      
-REMARK 465     PRO H   277                                                      
-REMARK 465     VAL H   278                                                      
-REMARK 465     HIS H   279                                                      
-REMARK 465     GLY H   280                                                      
-REMARK 465     LEU H   281                                                      
-REMARK 465     GLN H   282                                                      
-REMARK 465     ALA H   283                                                      
-REMARK 465     PRO H   284                                                      
-REMARK 465     ARG H   302                                                      
-REMARK 465     LYS H   303                                                      
-REMARK 465     LYS H   304                                                      
-REMARK 465     ARG H   305                                                      
-REMARK 465     GLU H   306                                                      
-REMARK 465     GLN H   307                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     ASP A 191    CG   OD1  OD2                                       
-REMARK 470     ASP C 191    CG   OD1  OD2                                       
-REMARK 470     ASP E 191    CG   OD1  OD2                                       
-REMARK 470     ASP G 191    CG   OD1  OD2                                       
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   O    ALA E   313     NH2  ARG E   320              2.14            
-REMARK 500   O    ALA A   313     NH2  ARG A   320              2.16            
-REMARK 500   O    ALA C   313     NH2  ARG C   320              2.16            
-REMARK 500   O    ALA G   313     NH2  ARG G   320              2.17            
-REMARK 500   O    ALA B   313     NH1  ARG B   320              2.19            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    TYR A 141       12.48   -147.10                                   
-REMARK 500    ASP A 146      -81.62    -95.23                                   
-REMARK 500    LEU A 193      -60.78   -103.68                                   
-REMARK 500    SER A 286      -77.20    -65.50                                   
-REMARK 500    VAL A 314       75.12     23.68                                   
-REMARK 500    ARG A 320       62.43   -116.84                                   
-REMARK 500    TYR A 429      -96.71     41.46                                   
-REMARK 500    HIS A 435       51.51   -145.86                                   
-REMARK 500    LYS A 441      -80.49   -127.37                                   
-REMARK 500    ASN A 498     -154.04   -111.45                                   
-REMARK 500    GLN A 500       32.65    -90.63                                   
-REMARK 500    LEU B  94      100.50    -55.14                                   
-REMARK 500    SER B 103     -157.38   -166.39                                   
-REMARK 500    SER B 104       10.75   -148.69                                   
-REMARK 500    GLU B 139      -75.60    -59.93                                   
-REMARK 500    SER B 144      -21.62     84.66                                   
-REMARK 500    ASP B 146      -83.44    -96.81                                   
-REMARK 500    SER B 194     -168.27   -163.03                                   
-REMARK 500    VAL B 314       72.85     22.02                                   
-REMARK 500    ARG B 320       75.49   -106.06                                   
-REMARK 500    ASP B 343     -167.73   -163.42                                   
-REMARK 500    LYS B 401       44.05   -107.74                                   
-REMARK 500    TYR B 429      -96.14     36.52                                   
-REMARK 500    LYS B 441      -77.69   -104.20                                   
-REMARK 500    ASN B 465       79.56   -156.11                                   
-REMARK 500    ASN B 498     -159.98   -106.06                                   
-REMARK 500    TYR C 141       11.71   -140.94                                   
-REMARK 500    ASP C 143       -2.86     69.07                                   
-REMARK 500    ASP C 146      -84.98   -101.52                                   
-REMARK 500    SER C 286      -80.13    -66.87                                   
-REMARK 500    VAL C 314       73.19     27.44                                   
-REMARK 500    ARG C 320       64.07   -111.64                                   
-REMARK 500    TYR C 429      -94.77     42.58                                   
-REMARK 500    HIS C 435       50.50   -144.41                                   
-REMARK 500    LYS C 441      -86.08   -115.06                                   
-REMARK 500    ASN C 498     -157.43   -120.27                                   
-REMARK 500    LEU D  94      102.05    -54.41                                   
-REMARK 500    SER D 103     -154.97   -170.11                                   
-REMARK 500    GLU D 139      -74.82    -54.89                                   
-REMARK 500    TYR D 141        7.67     59.76                                   
-REMARK 500    SER D 144      -42.64     88.64                                   
-REMARK 500    ASP D 146      -82.10    -87.93                                   
-REMARK 500    GLU D 299      -65.15    -29.95                                   
-REMARK 500    VAL D 314       73.30     21.85                                   
-REMARK 500    ARG D 320       76.65   -107.31                                   
-REMARK 500    PHE D 374       81.87    -68.26                                   
-REMARK 500    LYS D 401       55.47   -109.18                                   
-REMARK 500    PRO D 427       56.32    -68.59                                   
-REMARK 500    TYR D 429      -90.62     11.94                                   
-REMARK 500    LYS D 441      -77.82   -110.64                                   
-REMARK 500                                                                      
-REMARK 500 THIS ENTRY HAS     103 RAMACHANDRAN OUTLIERS.                        
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP A 701                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UG A 702                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL A 703                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 704                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP B 701                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UG B 702                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL B 703                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 704                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP C 701                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UG C 702                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL C 703                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP C 704                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP D 701                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UG D 702                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL D 703                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP D 704                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP E 701                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UG E 702                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL E 703                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP E 704                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP F 701                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UG F 702                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL F 703                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP F 704                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP G 701                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UG G 702                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: CC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL G 703                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: DC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP G 704                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: DC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP H 701                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: DC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UG H 702                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: DC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL H 703                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: DC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP H 704                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 4EIL   RELATED DB: PDB                                   
-REMARK 900 LOOP TRUNCATED T. GONDII TS-DHFR.                                    
-REMARK 900 RELATED ID: 4KY4   RELATED DB: PDB                                   
-REMARK 900 LOOP TRUNCATED T. GONDII TS-DHFR.                                    
-DBREF  4KYA A    1    48  UNP    Q07422   DRTS_TOXGO       1     48             
-DBREF  4KYA A   74   219  UNP    Q07422   DRTS_TOXGO      74    200             
-DBREF  4KYA A  220   610  UNP    Q07422   DRTS_TOXGO     220    610             
-DBREF  4KYA B    1    73  UNP    Q07422   DRTS_TOXGO       1     48             
-DBREF  4KYA B   74   219  UNP    Q07422   DRTS_TOXGO      74    200             
-DBREF  4KYA B  220   610  UNP    Q07422   DRTS_TOXGO     220    610             
-DBREF  4KYA C    1    48  UNP    Q07422   DRTS_TOXGO       1     48             
-DBREF  4KYA C   74   219  UNP    Q07422   DRTS_TOXGO      74    200             
-DBREF  4KYA C  220   610  UNP    Q07422   DRTS_TOXGO     220    610             
-DBREF  4KYA D    1    73  UNP    Q07422   DRTS_TOXGO       1     48             
-DBREF  4KYA D   74   219  UNP    Q07422   DRTS_TOXGO      74    200             
-DBREF  4KYA D  220   610  UNP    Q07422   DRTS_TOXGO     220    610             
-DBREF  4KYA E    1    48  UNP    Q07422   DRTS_TOXGO       1     48             
-DBREF  4KYA E   74   219  UNP    Q07422   DRTS_TOXGO      74    200             
-DBREF  4KYA E  220   610  UNP    Q07422   DRTS_TOXGO     220    610             
-DBREF  4KYA F    1    73  UNP    Q07422   DRTS_TOXGO       1     48             
-DBREF  4KYA F   74   219  UNP    Q07422   DRTS_TOXGO      74    200             
-DBREF  4KYA F  220   610  UNP    Q07422   DRTS_TOXGO     220    610             
-DBREF  4KYA G    1    48  UNP    Q07422   DRTS_TOXGO       1     48             
-DBREF  4KYA G   74   219  UNP    Q07422   DRTS_TOXGO      74    200             
-DBREF  4KYA G  220   610  UNP    Q07422   DRTS_TOXGO     220    610             
-DBREF  4KYA H    1    73  UNP    Q07422   DRTS_TOXGO       1     48             
-DBREF  4KYA H   74   219  UNP    Q07422   DRTS_TOXGO      74    200             
-DBREF  4KYA H  220   610  UNP    Q07422   DRTS_TOXGO     220    610             
-SEQRES   1 A  566  MET GLN LYS PRO VAL CYS LEU VAL VAL ALA MET THR PRO          
-SEQRES   2 A  566  LYS ARG GLY ILE GLY ILE ASN ASN GLY LEU PRO TRP PRO          
-SEQRES   3 A  566  HIS LEU THR THR ASP PHE LYS HIS PHE SER ARG VAL THR          
-SEQRES   4 A  566  LYS THR THR PRO GLU GLU ALA SER ARG PHE ASN ALA VAL          
-SEQRES   5 A  566  VAL MET GLY ARG LYS THR TRP GLU SER MET PRO ARG LYS          
-SEQRES   6 A  566  PHE ARG PRO LEU VAL ASP ARG LEU ASN ILE VAL VAL SER          
-SEQRES   7 A  566  SER SER LEU LYS GLU GLU ASP ILE ALA ALA GLU LYS PRO          
-SEQRES   8 A  566  GLN ALA GLU GLY GLN GLN ARG VAL ARG VAL CYS ALA SER          
-SEQRES   9 A  566  LEU PRO ALA ALA LEU SER LEU LEU GLU GLU GLU TYR LYS          
-SEQRES  10 A  566  ASP SER VAL ASP GLN ILE PHE VAL VAL GLY GLY ALA GLY          
-SEQRES  11 A  566  LEU TYR GLU ALA ALA LEU SER LEU GLY VAL ALA SER HIS          
-SEQRES  12 A  566  LEU TYR ILE THR ARG VAL ALA ARG GLU PHE PRO CYS ASP          
-SEQRES  13 A  566  VAL PHE PHE PRO ALA PHE PRO GLY ASP ASP ILE LEU SER          
-SEQRES  14 A  566  ASN LYS SER THR ALA ALA GLU LYS ASP ASN GLU ALA THR          
-SEQRES  15 A  566  TYR ARG PRO ILE PHE ILE SER LYS THR PHE SER ASP ASN          
-SEQRES  16 A  566  GLY VAL PRO TYR ASP PHE VAL VAL LEU GLU LYS ARG ARG          
-SEQRES  17 A  566  LYS THR ASP ASP ALA ALA THR ALA GLU PRO SER ASN ALA          
-SEQRES  18 A  566  MET SER SER LEU THR SER THR ARG GLU THR THR PRO VAL          
-SEQRES  19 A  566  HIS GLY LEU GLN ALA PRO SER SER ALA ALA ALA ILE ALA          
-SEQRES  20 A  566  PRO VAL LEU ALA TRP MET ASP GLU GLU ASP ARG LYS LYS          
-SEQRES  21 A  566  ARG GLU GLN LYS GLU LEU ILE ARG ALA VAL PRO HIS VAL          
-SEQRES  22 A  566  HIS PHE ARG GLY HIS GLU GLU PHE GLN TYR LEU ASP LEU          
-SEQRES  23 A  566  ILE ALA ASP ILE ILE ASN ASN GLY ARG THR MET ASP ASP          
-SEQRES  24 A  566  ARG THR GLY VAL GLY VAL ILE SER LYS PHE GLY CYS THR          
-SEQRES  25 A  566  MET ARG TYR SER LEU ASP GLN ALA PHE PRO LEU LEU THR          
-SEQRES  26 A  566  THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU          
-SEQRES  27 A  566  LEU TRP PHE ILE ARG GLY ASP THR ASN ALA ASN HIS LEU          
-SEQRES  28 A  566  SER GLU LYS GLY VAL LYS ILE TRP ASP LYS ASN VAL THR          
-SEQRES  29 A  566  ARG GLU PHE LEU ASP SER ARG ASN LEU PRO HIS ARG GLU          
-SEQRES  30 A  566  VAL GLY ASP ILE GLY PRO GLY TYR GLY PHE GLN TRP ARG          
-SEQRES  31 A  566  HIS PHE GLY ALA ALA TYR LYS ASP MET HIS THR ASP TYR          
-SEQRES  32 A  566  THR GLY GLN GLY VAL ASP GLN LEU LYS ASN VAL ILE GLN          
-SEQRES  33 A  566  MET LEU ARG THR ASN PRO THR ASP ARG ARG MET LEU MET          
-SEQRES  34 A  566  THR ALA TRP ASN PRO ALA ALA LEU ASP GLU MET ALA LEU          
-SEQRES  35 A  566  PRO PRO CYS HIS LEU LEU CYS GLN PHE TYR VAL ASN ASP          
-SEQRES  36 A  566  GLN LYS GLU LEU SER CYS ILE MET TYR GLN ARG SER CYS          
-SEQRES  37 A  566  ASP VAL GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR          
-SEQRES  38 A  566  SER LEU LEU THR LEU MET VAL ALA HIS VAL CYS ASN LEU          
-SEQRES  39 A  566  LYS PRO LYS GLU PHE ILE HIS PHE MET GLY ASN THR HIS          
-SEQRES  40 A  566  VAL TYR THR ASN HIS VAL GLU ALA LEU LYS GLU GLN LEU          
-SEQRES  41 A  566  ARG ARG GLU PRO ARG PRO PHE PRO ILE VAL ASN ILE LEU          
-SEQRES  42 A  566  ASN LYS GLU ARG ILE LYS GLU ILE ASP ASP PHE THR ALA          
-SEQRES  43 A  566  GLU ASP PHE GLU VAL VAL GLY TYR VAL PRO HIS GLY ARG          
-SEQRES  44 A  566  ILE GLN MET GLU MET ALA VAL                                  
-SEQRES   1 B  566  MET GLN LYS PRO VAL CYS LEU VAL VAL ALA MET THR PRO          
-SEQRES   2 B  566  LYS ARG GLY ILE GLY ILE ASN ASN GLY LEU PRO TRP PRO          
-SEQRES   3 B  566  HIS LEU THR THR ASP PHE LYS HIS PHE SER ARG VAL THR          
-SEQRES   4 B  566  LYS THR THR PRO GLU GLU ALA SER ARG PHE ASN ALA VAL          
-SEQRES   5 B  566  VAL MET GLY ARG LYS THR TRP GLU SER MET PRO ARG LYS          
-SEQRES   6 B  566  PHE ARG PRO LEU VAL ASP ARG LEU ASN ILE VAL VAL SER          
-SEQRES   7 B  566  SER SER LEU LYS GLU GLU ASP ILE ALA ALA GLU LYS PRO          
-SEQRES   8 B  566  GLN ALA GLU GLY GLN GLN ARG VAL ARG VAL CYS ALA SER          
-SEQRES   9 B  566  LEU PRO ALA ALA LEU SER LEU LEU GLU GLU GLU TYR LYS          
-SEQRES  10 B  566  ASP SER VAL ASP GLN ILE PHE VAL VAL GLY GLY ALA GLY          
-SEQRES  11 B  566  LEU TYR GLU ALA ALA LEU SER LEU GLY VAL ALA SER HIS          
-SEQRES  12 B  566  LEU TYR ILE THR ARG VAL ALA ARG GLU PHE PRO CYS ASP          
-SEQRES  13 B  566  VAL PHE PHE PRO ALA PHE PRO GLY ASP ASP ILE LEU SER          
-SEQRES  14 B  566  ASN LYS SER THR ALA ALA GLU LYS ASP ASN GLU ALA THR          
-SEQRES  15 B  566  TYR ARG PRO ILE PHE ILE SER LYS THR PHE SER ASP ASN          
-SEQRES  16 B  566  GLY VAL PRO TYR ASP PHE VAL VAL LEU GLU LYS ARG ARG          
-SEQRES  17 B  566  LYS THR ASP ASP ALA ALA THR ALA GLU PRO SER ASN ALA          
-SEQRES  18 B  566  MET SER SER LEU THR SER THR ARG GLU THR THR PRO VAL          
-SEQRES  19 B  566  HIS GLY LEU GLN ALA PRO SER SER ALA ALA ALA ILE ALA          
-SEQRES  20 B  566  PRO VAL LEU ALA TRP MET ASP GLU GLU ASP ARG LYS LYS          
-SEQRES  21 B  566  ARG GLU GLN LYS GLU LEU ILE ARG ALA VAL PRO HIS VAL          
-SEQRES  22 B  566  HIS PHE ARG GLY HIS GLU GLU PHE GLN TYR LEU ASP LEU          
-SEQRES  23 B  566  ILE ALA ASP ILE ILE ASN ASN GLY ARG THR MET ASP ASP          
-SEQRES  24 B  566  ARG THR GLY VAL GLY VAL ILE SER LYS PHE GLY CYS THR          
-SEQRES  25 B  566  MET ARG TYR SER LEU ASP GLN ALA PHE PRO LEU LEU THR          
-SEQRES  26 B  566  THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU          
-SEQRES  27 B  566  LEU TRP PHE ILE ARG GLY ASP THR ASN ALA ASN HIS LEU          
-SEQRES  28 B  566  SER GLU LYS GLY VAL LYS ILE TRP ASP LYS ASN VAL THR          
-SEQRES  29 B  566  ARG GLU PHE LEU ASP SER ARG ASN LEU PRO HIS ARG GLU          
-SEQRES  30 B  566  VAL GLY ASP ILE GLY PRO GLY TYR GLY PHE GLN TRP ARG          
-SEQRES  31 B  566  HIS PHE GLY ALA ALA TYR LYS ASP MET HIS THR ASP TYR          
-SEQRES  32 B  566  THR GLY GLN GLY VAL ASP GLN LEU LYS ASN VAL ILE GLN          
-SEQRES  33 B  566  MET LEU ARG THR ASN PRO THR ASP ARG ARG MET LEU MET          
-SEQRES  34 B  566  THR ALA TRP ASN PRO ALA ALA LEU ASP GLU MET ALA LEU          
-SEQRES  35 B  566  PRO PRO CYS HIS LEU LEU CYS GLN PHE TYR VAL ASN ASP          
-SEQRES  36 B  566  GLN LYS GLU LEU SER CYS ILE MET TYR GLN ARG SER CYS          
-SEQRES  37 B  566  ASP VAL GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR          
-SEQRES  38 B  566  SER LEU LEU THR LEU MET VAL ALA HIS VAL CYS ASN LEU          
-SEQRES  39 B  566  LYS PRO LYS GLU PHE ILE HIS PHE MET GLY ASN THR HIS          
-SEQRES  40 B  566  VAL TYR THR ASN HIS VAL GLU ALA LEU LYS GLU GLN LEU          
-SEQRES  41 B  566  ARG ARG GLU PRO ARG PRO PHE PRO ILE VAL ASN ILE LEU          
-SEQRES  42 B  566  ASN LYS GLU ARG ILE LYS GLU ILE ASP ASP PHE THR ALA          
-SEQRES  43 B  566  GLU ASP PHE GLU VAL VAL GLY TYR VAL PRO HIS GLY ARG          
-SEQRES  44 B  566  ILE GLN MET GLU MET ALA VAL                                  
-SEQRES   1 C  566  MET GLN LYS PRO VAL CYS LEU VAL VAL ALA MET THR PRO          
-SEQRES   2 C  566  LYS ARG GLY ILE GLY ILE ASN ASN GLY LEU PRO TRP PRO          
-SEQRES   3 C  566  HIS LEU THR THR ASP PHE LYS HIS PHE SER ARG VAL THR          
-SEQRES   4 C  566  LYS THR THR PRO GLU GLU ALA SER ARG PHE ASN ALA VAL          
-SEQRES   5 C  566  VAL MET GLY ARG LYS THR TRP GLU SER MET PRO ARG LYS          
-SEQRES   6 C  566  PHE ARG PRO LEU VAL ASP ARG LEU ASN ILE VAL VAL SER          
-SEQRES   7 C  566  SER SER LEU LYS GLU GLU ASP ILE ALA ALA GLU LYS PRO          
-SEQRES   8 C  566  GLN ALA GLU GLY GLN GLN ARG VAL ARG VAL CYS ALA SER          
-SEQRES   9 C  566  LEU PRO ALA ALA LEU SER LEU LEU GLU GLU GLU TYR LYS          
-SEQRES  10 C  566  ASP SER VAL ASP GLN ILE PHE VAL VAL GLY GLY ALA GLY          
-SEQRES  11 C  566  LEU TYR GLU ALA ALA LEU SER LEU GLY VAL ALA SER HIS          
-SEQRES  12 C  566  LEU TYR ILE THR ARG VAL ALA ARG GLU PHE PRO CYS ASP          
-SEQRES  13 C  566  VAL PHE PHE PRO ALA PHE PRO GLY ASP ASP ILE LEU SER          
-SEQRES  14 C  566  ASN LYS SER THR ALA ALA GLU LYS ASP ASN GLU ALA THR          
-SEQRES  15 C  566  TYR ARG PRO ILE PHE ILE SER LYS THR PHE SER ASP ASN          
-SEQRES  16 C  566  GLY VAL PRO TYR ASP PHE VAL VAL LEU GLU LYS ARG ARG          
-SEQRES  17 C  566  LYS THR ASP ASP ALA ALA THR ALA GLU PRO SER ASN ALA          
-SEQRES  18 C  566  MET SER SER LEU THR SER THR ARG GLU THR THR PRO VAL          
-SEQRES  19 C  566  HIS GLY LEU GLN ALA PRO SER SER ALA ALA ALA ILE ALA          
-SEQRES  20 C  566  PRO VAL LEU ALA TRP MET ASP GLU GLU ASP ARG LYS LYS          
-SEQRES  21 C  566  ARG GLU GLN LYS GLU LEU ILE ARG ALA VAL PRO HIS VAL          
-SEQRES  22 C  566  HIS PHE ARG GLY HIS GLU GLU PHE GLN TYR LEU ASP LEU          
-SEQRES  23 C  566  ILE ALA ASP ILE ILE ASN ASN GLY ARG THR MET ASP ASP          
-SEQRES  24 C  566  ARG THR GLY VAL GLY VAL ILE SER LYS PHE GLY CYS THR          
-SEQRES  25 C  566  MET ARG TYR SER LEU ASP GLN ALA PHE PRO LEU LEU THR          
-SEQRES  26 C  566  THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU          
-SEQRES  27 C  566  LEU TRP PHE ILE ARG GLY ASP THR ASN ALA ASN HIS LEU          
-SEQRES  28 C  566  SER GLU LYS GLY VAL LYS ILE TRP ASP LYS ASN VAL THR          
-SEQRES  29 C  566  ARG GLU PHE LEU ASP SER ARG ASN LEU PRO HIS ARG GLU          
-SEQRES  30 C  566  VAL GLY ASP ILE GLY PRO GLY TYR GLY PHE GLN TRP ARG          
-SEQRES  31 C  566  HIS PHE GLY ALA ALA TYR LYS ASP MET HIS THR ASP TYR          
-SEQRES  32 C  566  THR GLY GLN GLY VAL ASP GLN LEU LYS ASN VAL ILE GLN          
-SEQRES  33 C  566  MET LEU ARG THR ASN PRO THR ASP ARG ARG MET LEU MET          
-SEQRES  34 C  566  THR ALA TRP ASN PRO ALA ALA LEU ASP GLU MET ALA LEU          
-SEQRES  35 C  566  PRO PRO CYS HIS LEU LEU CYS GLN PHE TYR VAL ASN ASP          
-SEQRES  36 C  566  GLN LYS GLU LEU SER CYS ILE MET TYR GLN ARG SER CYS          
-SEQRES  37 C  566  ASP VAL GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR          
-SEQRES  38 C  566  SER LEU LEU THR LEU MET VAL ALA HIS VAL CYS ASN LEU          
-SEQRES  39 C  566  LYS PRO LYS GLU PHE ILE HIS PHE MET GLY ASN THR HIS          
-SEQRES  40 C  566  VAL TYR THR ASN HIS VAL GLU ALA LEU LYS GLU GLN LEU          
-SEQRES  41 C  566  ARG ARG GLU PRO ARG PRO PHE PRO ILE VAL ASN ILE LEU          
-SEQRES  42 C  566  ASN LYS GLU ARG ILE LYS GLU ILE ASP ASP PHE THR ALA          
-SEQRES  43 C  566  GLU ASP PHE GLU VAL VAL GLY TYR VAL PRO HIS GLY ARG          
-SEQRES  44 C  566  ILE GLN MET GLU MET ALA VAL                                  
-SEQRES   1 D  566  MET GLN LYS PRO VAL CYS LEU VAL VAL ALA MET THR PRO          
-SEQRES   2 D  566  LYS ARG GLY ILE GLY ILE ASN ASN GLY LEU PRO TRP PRO          
-SEQRES   3 D  566  HIS LEU THR THR ASP PHE LYS HIS PHE SER ARG VAL THR          
-SEQRES   4 D  566  LYS THR THR PRO GLU GLU ALA SER ARG PHE ASN ALA VAL          
-SEQRES   5 D  566  VAL MET GLY ARG LYS THR TRP GLU SER MET PRO ARG LYS          
-SEQRES   6 D  566  PHE ARG PRO LEU VAL ASP ARG LEU ASN ILE VAL VAL SER          
-SEQRES   7 D  566  SER SER LEU LYS GLU GLU ASP ILE ALA ALA GLU LYS PRO          
-SEQRES   8 D  566  GLN ALA GLU GLY GLN GLN ARG VAL ARG VAL CYS ALA SER          
-SEQRES   9 D  566  LEU PRO ALA ALA LEU SER LEU LEU GLU GLU GLU TYR LYS          
-SEQRES  10 D  566  ASP SER VAL ASP GLN ILE PHE VAL VAL GLY GLY ALA GLY          
-SEQRES  11 D  566  LEU TYR GLU ALA ALA LEU SER LEU GLY VAL ALA SER HIS          
-SEQRES  12 D  566  LEU TYR ILE THR ARG VAL ALA ARG GLU PHE PRO CYS ASP          
-SEQRES  13 D  566  VAL PHE PHE PRO ALA PHE PRO GLY ASP ASP ILE LEU SER          
-SEQRES  14 D  566  ASN LYS SER THR ALA ALA GLU LYS ASP ASN GLU ALA THR          
-SEQRES  15 D  566  TYR ARG PRO ILE PHE ILE SER LYS THR PHE SER ASP ASN          
-SEQRES  16 D  566  GLY VAL PRO TYR ASP PHE VAL VAL LEU GLU LYS ARG ARG          
-SEQRES  17 D  566  LYS THR ASP ASP ALA ALA THR ALA GLU PRO SER ASN ALA          
-SEQRES  18 D  566  MET SER SER LEU THR SER THR ARG GLU THR THR PRO VAL          
-SEQRES  19 D  566  HIS GLY LEU GLN ALA PRO SER SER ALA ALA ALA ILE ALA          
-SEQRES  20 D  566  PRO VAL LEU ALA TRP MET ASP GLU GLU ASP ARG LYS LYS          
-SEQRES  21 D  566  ARG GLU GLN LYS GLU LEU ILE ARG ALA VAL PRO HIS VAL          
-SEQRES  22 D  566  HIS PHE ARG GLY HIS GLU GLU PHE GLN TYR LEU ASP LEU          
-SEQRES  23 D  566  ILE ALA ASP ILE ILE ASN ASN GLY ARG THR MET ASP ASP          
-SEQRES  24 D  566  ARG THR GLY VAL GLY VAL ILE SER LYS PHE GLY CYS THR          
-SEQRES  25 D  566  MET ARG TYR SER LEU ASP GLN ALA PHE PRO LEU LEU THR          
-SEQRES  26 D  566  THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU          
-SEQRES  27 D  566  LEU TRP PHE ILE ARG GLY ASP THR ASN ALA ASN HIS LEU          
-SEQRES  28 D  566  SER GLU LYS GLY VAL LYS ILE TRP ASP LYS ASN VAL THR          
-SEQRES  29 D  566  ARG GLU PHE LEU ASP SER ARG ASN LEU PRO HIS ARG GLU          
-SEQRES  30 D  566  VAL GLY ASP ILE GLY PRO GLY TYR GLY PHE GLN TRP ARG          
-SEQRES  31 D  566  HIS PHE GLY ALA ALA TYR LYS ASP MET HIS THR ASP TYR          
-SEQRES  32 D  566  THR GLY GLN GLY VAL ASP GLN LEU LYS ASN VAL ILE GLN          
-SEQRES  33 D  566  MET LEU ARG THR ASN PRO THR ASP ARG ARG MET LEU MET          
-SEQRES  34 D  566  THR ALA TRP ASN PRO ALA ALA LEU ASP GLU MET ALA LEU          
-SEQRES  35 D  566  PRO PRO CYS HIS LEU LEU CYS GLN PHE TYR VAL ASN ASP          
-SEQRES  36 D  566  GLN LYS GLU LEU SER CYS ILE MET TYR GLN ARG SER CYS          
-SEQRES  37 D  566  ASP VAL GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR          
-SEQRES  38 D  566  SER LEU LEU THR LEU MET VAL ALA HIS VAL CYS ASN LEU          
-SEQRES  39 D  566  LYS PRO LYS GLU PHE ILE HIS PHE MET GLY ASN THR HIS          
-SEQRES  40 D  566  VAL TYR THR ASN HIS VAL GLU ALA LEU LYS GLU GLN LEU          
-SEQRES  41 D  566  ARG ARG GLU PRO ARG PRO PHE PRO ILE VAL ASN ILE LEU          
-SEQRES  42 D  566  ASN LYS GLU ARG ILE LYS GLU ILE ASP ASP PHE THR ALA          
-SEQRES  43 D  566  GLU ASP PHE GLU VAL VAL GLY TYR VAL PRO HIS GLY ARG          
-SEQRES  44 D  566  ILE GLN MET GLU MET ALA VAL                                  
-SEQRES   1 E  566  MET GLN LYS PRO VAL CYS LEU VAL VAL ALA MET THR PRO          
-SEQRES   2 E  566  LYS ARG GLY ILE GLY ILE ASN ASN GLY LEU PRO TRP PRO          
-SEQRES   3 E  566  HIS LEU THR THR ASP PHE LYS HIS PHE SER ARG VAL THR          
-SEQRES   4 E  566  LYS THR THR PRO GLU GLU ALA SER ARG PHE ASN ALA VAL          
-SEQRES   5 E  566  VAL MET GLY ARG LYS THR TRP GLU SER MET PRO ARG LYS          
-SEQRES   6 E  566  PHE ARG PRO LEU VAL ASP ARG LEU ASN ILE VAL VAL SER          
-SEQRES   7 E  566  SER SER LEU LYS GLU GLU ASP ILE ALA ALA GLU LYS PRO          
-SEQRES   8 E  566  GLN ALA GLU GLY GLN GLN ARG VAL ARG VAL CYS ALA SER          
-SEQRES   9 E  566  LEU PRO ALA ALA LEU SER LEU LEU GLU GLU GLU TYR LYS          
-SEQRES  10 E  566  ASP SER VAL ASP GLN ILE PHE VAL VAL GLY GLY ALA GLY          
-SEQRES  11 E  566  LEU TYR GLU ALA ALA LEU SER LEU GLY VAL ALA SER HIS          
-SEQRES  12 E  566  LEU TYR ILE THR ARG VAL ALA ARG GLU PHE PRO CYS ASP          
-SEQRES  13 E  566  VAL PHE PHE PRO ALA PHE PRO GLY ASP ASP ILE LEU SER          
-SEQRES  14 E  566  ASN LYS SER THR ALA ALA GLU LYS ASP ASN GLU ALA THR          
-SEQRES  15 E  566  TYR ARG PRO ILE PHE ILE SER LYS THR PHE SER ASP ASN          
-SEQRES  16 E  566  GLY VAL PRO TYR ASP PHE VAL VAL LEU GLU LYS ARG ARG          
-SEQRES  17 E  566  LYS THR ASP ASP ALA ALA THR ALA GLU PRO SER ASN ALA          
-SEQRES  18 E  566  MET SER SER LEU THR SER THR ARG GLU THR THR PRO VAL          
-SEQRES  19 E  566  HIS GLY LEU GLN ALA PRO SER SER ALA ALA ALA ILE ALA          
-SEQRES  20 E  566  PRO VAL LEU ALA TRP MET ASP GLU GLU ASP ARG LYS LYS          
-SEQRES  21 E  566  ARG GLU GLN LYS GLU LEU ILE ARG ALA VAL PRO HIS VAL          
-SEQRES  22 E  566  HIS PHE ARG GLY HIS GLU GLU PHE GLN TYR LEU ASP LEU          
-SEQRES  23 E  566  ILE ALA ASP ILE ILE ASN ASN GLY ARG THR MET ASP ASP          
-SEQRES  24 E  566  ARG THR GLY VAL GLY VAL ILE SER LYS PHE GLY CYS THR          
-SEQRES  25 E  566  MET ARG TYR SER LEU ASP GLN ALA PHE PRO LEU LEU THR          
-SEQRES  26 E  566  THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU          
-SEQRES  27 E  566  LEU TRP PHE ILE ARG GLY ASP THR ASN ALA ASN HIS LEU          
-SEQRES  28 E  566  SER GLU LYS GLY VAL LYS ILE TRP ASP LYS ASN VAL THR          
-SEQRES  29 E  566  ARG GLU PHE LEU ASP SER ARG ASN LEU PRO HIS ARG GLU          
-SEQRES  30 E  566  VAL GLY ASP ILE GLY PRO GLY TYR GLY PHE GLN TRP ARG          
-SEQRES  31 E  566  HIS PHE GLY ALA ALA TYR LYS ASP MET HIS THR ASP TYR          
-SEQRES  32 E  566  THR GLY GLN GLY VAL ASP GLN LEU LYS ASN VAL ILE GLN          
-SEQRES  33 E  566  MET LEU ARG THR ASN PRO THR ASP ARG ARG MET LEU MET          
-SEQRES  34 E  566  THR ALA TRP ASN PRO ALA ALA LEU ASP GLU MET ALA LEU          
-SEQRES  35 E  566  PRO PRO CYS HIS LEU LEU CYS GLN PHE TYR VAL ASN ASP          
-SEQRES  36 E  566  GLN LYS GLU LEU SER CYS ILE MET TYR GLN ARG SER CYS          
-SEQRES  37 E  566  ASP VAL GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR          
-SEQRES  38 E  566  SER LEU LEU THR LEU MET VAL ALA HIS VAL CYS ASN LEU          
-SEQRES  39 E  566  LYS PRO LYS GLU PHE ILE HIS PHE MET GLY ASN THR HIS          
-SEQRES  40 E  566  VAL TYR THR ASN HIS VAL GLU ALA LEU LYS GLU GLN LEU          
-SEQRES  41 E  566  ARG ARG GLU PRO ARG PRO PHE PRO ILE VAL ASN ILE LEU          
-SEQRES  42 E  566  ASN LYS GLU ARG ILE LYS GLU ILE ASP ASP PHE THR ALA          
-SEQRES  43 E  566  GLU ASP PHE GLU VAL VAL GLY TYR VAL PRO HIS GLY ARG          
-SEQRES  44 E  566  ILE GLN MET GLU MET ALA VAL                                  
-SEQRES   1 F  566  MET GLN LYS PRO VAL CYS LEU VAL VAL ALA MET THR PRO          
-SEQRES   2 F  566  LYS ARG GLY ILE GLY ILE ASN ASN GLY LEU PRO TRP PRO          
-SEQRES   3 F  566  HIS LEU THR THR ASP PHE LYS HIS PHE SER ARG VAL THR          
-SEQRES   4 F  566  LYS THR THR PRO GLU GLU ALA SER ARG PHE ASN ALA VAL          
-SEQRES   5 F  566  VAL MET GLY ARG LYS THR TRP GLU SER MET PRO ARG LYS          
-SEQRES   6 F  566  PHE ARG PRO LEU VAL ASP ARG LEU ASN ILE VAL VAL SER          
-SEQRES   7 F  566  SER SER LEU LYS GLU GLU ASP ILE ALA ALA GLU LYS PRO          
-SEQRES   8 F  566  GLN ALA GLU GLY GLN GLN ARG VAL ARG VAL CYS ALA SER          
-SEQRES   9 F  566  LEU PRO ALA ALA LEU SER LEU LEU GLU GLU GLU TYR LYS          
-SEQRES  10 F  566  ASP SER VAL ASP GLN ILE PHE VAL VAL GLY GLY ALA GLY          
-SEQRES  11 F  566  LEU TYR GLU ALA ALA LEU SER LEU GLY VAL ALA SER HIS          
-SEQRES  12 F  566  LEU TYR ILE THR ARG VAL ALA ARG GLU PHE PRO CYS ASP          
-SEQRES  13 F  566  VAL PHE PHE PRO ALA PHE PRO GLY ASP ASP ILE LEU SER          
-SEQRES  14 F  566  ASN LYS SER THR ALA ALA GLU LYS ASP ASN GLU ALA THR          
-SEQRES  15 F  566  TYR ARG PRO ILE PHE ILE SER LYS THR PHE SER ASP ASN          
-SEQRES  16 F  566  GLY VAL PRO TYR ASP PHE VAL VAL LEU GLU LYS ARG ARG          
-SEQRES  17 F  566  LYS THR ASP ASP ALA ALA THR ALA GLU PRO SER ASN ALA          
-SEQRES  18 F  566  MET SER SER LEU THR SER THR ARG GLU THR THR PRO VAL          
-SEQRES  19 F  566  HIS GLY LEU GLN ALA PRO SER SER ALA ALA ALA ILE ALA          
-SEQRES  20 F  566  PRO VAL LEU ALA TRP MET ASP GLU GLU ASP ARG LYS LYS          
-SEQRES  21 F  566  ARG GLU GLN LYS GLU LEU ILE ARG ALA VAL PRO HIS VAL          
-SEQRES  22 F  566  HIS PHE ARG GLY HIS GLU GLU PHE GLN TYR LEU ASP LEU          
-SEQRES  23 F  566  ILE ALA ASP ILE ILE ASN ASN GLY ARG THR MET ASP ASP          
-SEQRES  24 F  566  ARG THR GLY VAL GLY VAL ILE SER LYS PHE GLY CYS THR          
-SEQRES  25 F  566  MET ARG TYR SER LEU ASP GLN ALA PHE PRO LEU LEU THR          
-SEQRES  26 F  566  THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU          
-SEQRES  27 F  566  LEU TRP PHE ILE ARG GLY ASP THR ASN ALA ASN HIS LEU          
-SEQRES  28 F  566  SER GLU LYS GLY VAL LYS ILE TRP ASP LYS ASN VAL THR          
-SEQRES  29 F  566  ARG GLU PHE LEU ASP SER ARG ASN LEU PRO HIS ARG GLU          
-SEQRES  30 F  566  VAL GLY ASP ILE GLY PRO GLY TYR GLY PHE GLN TRP ARG          
-SEQRES  31 F  566  HIS PHE GLY ALA ALA TYR LYS ASP MET HIS THR ASP TYR          
-SEQRES  32 F  566  THR GLY GLN GLY VAL ASP GLN LEU LYS ASN VAL ILE GLN          
-SEQRES  33 F  566  MET LEU ARG THR ASN PRO THR ASP ARG ARG MET LEU MET          
-SEQRES  34 F  566  THR ALA TRP ASN PRO ALA ALA LEU ASP GLU MET ALA LEU          
-SEQRES  35 F  566  PRO PRO CYS HIS LEU LEU CYS GLN PHE TYR VAL ASN ASP          
-SEQRES  36 F  566  GLN LYS GLU LEU SER CYS ILE MET TYR GLN ARG SER CYS          
-SEQRES  37 F  566  ASP VAL GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR          
-SEQRES  38 F  566  SER LEU LEU THR LEU MET VAL ALA HIS VAL CYS ASN LEU          
-SEQRES  39 F  566  LYS PRO LYS GLU PHE ILE HIS PHE MET GLY ASN THR HIS          
-SEQRES  40 F  566  VAL TYR THR ASN HIS VAL GLU ALA LEU LYS GLU GLN LEU          
-SEQRES  41 F  566  ARG ARG GLU PRO ARG PRO PHE PRO ILE VAL ASN ILE LEU          
-SEQRES  42 F  566  ASN LYS GLU ARG ILE LYS GLU ILE ASP ASP PHE THR ALA          
-SEQRES  43 F  566  GLU ASP PHE GLU VAL VAL GLY TYR VAL PRO HIS GLY ARG          
-SEQRES  44 F  566  ILE GLN MET GLU MET ALA VAL                                  
-SEQRES   1 G  566  MET GLN LYS PRO VAL CYS LEU VAL VAL ALA MET THR PRO          
-SEQRES   2 G  566  LYS ARG GLY ILE GLY ILE ASN ASN GLY LEU PRO TRP PRO          
-SEQRES   3 G  566  HIS LEU THR THR ASP PHE LYS HIS PHE SER ARG VAL THR          
-SEQRES   4 G  566  LYS THR THR PRO GLU GLU ALA SER ARG PHE ASN ALA VAL          
-SEQRES   5 G  566  VAL MET GLY ARG LYS THR TRP GLU SER MET PRO ARG LYS          
-SEQRES   6 G  566  PHE ARG PRO LEU VAL ASP ARG LEU ASN ILE VAL VAL SER          
-SEQRES   7 G  566  SER SER LEU LYS GLU GLU ASP ILE ALA ALA GLU LYS PRO          
-SEQRES   8 G  566  GLN ALA GLU GLY GLN GLN ARG VAL ARG VAL CYS ALA SER          
-SEQRES   9 G  566  LEU PRO ALA ALA LEU SER LEU LEU GLU GLU GLU TYR LYS          
-SEQRES  10 G  566  ASP SER VAL ASP GLN ILE PHE VAL VAL GLY GLY ALA GLY          
-SEQRES  11 G  566  LEU TYR GLU ALA ALA LEU SER LEU GLY VAL ALA SER HIS          
-SEQRES  12 G  566  LEU TYR ILE THR ARG VAL ALA ARG GLU PHE PRO CYS ASP          
-SEQRES  13 G  566  VAL PHE PHE PRO ALA PHE PRO GLY ASP ASP ILE LEU SER          
-SEQRES  14 G  566  ASN LYS SER THR ALA ALA GLU LYS ASP ASN GLU ALA THR          
-SEQRES  15 G  566  TYR ARG PRO ILE PHE ILE SER LYS THR PHE SER ASP ASN          
-SEQRES  16 G  566  GLY VAL PRO TYR ASP PHE VAL VAL LEU GLU LYS ARG ARG          
-SEQRES  17 G  566  LYS THR ASP ASP ALA ALA THR ALA GLU PRO SER ASN ALA          
-SEQRES  18 G  566  MET SER SER LEU THR SER THR ARG GLU THR THR PRO VAL          
-SEQRES  19 G  566  HIS GLY LEU GLN ALA PRO SER SER ALA ALA ALA ILE ALA          
-SEQRES  20 G  566  PRO VAL LEU ALA TRP MET ASP GLU GLU ASP ARG LYS LYS          
-SEQRES  21 G  566  ARG GLU GLN LYS GLU LEU ILE ARG ALA VAL PRO HIS VAL          
-SEQRES  22 G  566  HIS PHE ARG GLY HIS GLU GLU PHE GLN TYR LEU ASP LEU          
-SEQRES  23 G  566  ILE ALA ASP ILE ILE ASN ASN GLY ARG THR MET ASP ASP          
-SEQRES  24 G  566  ARG THR GLY VAL GLY VAL ILE SER LYS PHE GLY CYS THR          
-SEQRES  25 G  566  MET ARG TYR SER LEU ASP GLN ALA PHE PRO LEU LEU THR          
-SEQRES  26 G  566  THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU          
-SEQRES  27 G  566  LEU TRP PHE ILE ARG GLY ASP THR ASN ALA ASN HIS LEU          
-SEQRES  28 G  566  SER GLU LYS GLY VAL LYS ILE TRP ASP LYS ASN VAL THR          
-SEQRES  29 G  566  ARG GLU PHE LEU ASP SER ARG ASN LEU PRO HIS ARG GLU          
-SEQRES  30 G  566  VAL GLY ASP ILE GLY PRO GLY TYR GLY PHE GLN TRP ARG          
-SEQRES  31 G  566  HIS PHE GLY ALA ALA TYR LYS ASP MET HIS THR ASP TYR          
-SEQRES  32 G  566  THR GLY GLN GLY VAL ASP GLN LEU LYS ASN VAL ILE GLN          
-SEQRES  33 G  566  MET LEU ARG THR ASN PRO THR ASP ARG ARG MET LEU MET          
-SEQRES  34 G  566  THR ALA TRP ASN PRO ALA ALA LEU ASP GLU MET ALA LEU          
-SEQRES  35 G  566  PRO PRO CYS HIS LEU LEU CYS GLN PHE TYR VAL ASN ASP          
-SEQRES  36 G  566  GLN LYS GLU LEU SER CYS ILE MET TYR GLN ARG SER CYS          
-SEQRES  37 G  566  ASP VAL GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR          
-SEQRES  38 G  566  SER LEU LEU THR LEU MET VAL ALA HIS VAL CYS ASN LEU          
-SEQRES  39 G  566  LYS PRO LYS GLU PHE ILE HIS PHE MET GLY ASN THR HIS          
-SEQRES  40 G  566  VAL TYR THR ASN HIS VAL GLU ALA LEU LYS GLU GLN LEU          
-SEQRES  41 G  566  ARG ARG GLU PRO ARG PRO PHE PRO ILE VAL ASN ILE LEU          
-SEQRES  42 G  566  ASN LYS GLU ARG ILE LYS GLU ILE ASP ASP PHE THR ALA          
-SEQRES  43 G  566  GLU ASP PHE GLU VAL VAL GLY TYR VAL PRO HIS GLY ARG          
-SEQRES  44 G  566  ILE GLN MET GLU MET ALA VAL                                  
-SEQRES   1 H  566  MET GLN LYS PRO VAL CYS LEU VAL VAL ALA MET THR PRO          
-SEQRES   2 H  566  LYS ARG GLY ILE GLY ILE ASN ASN GLY LEU PRO TRP PRO          
-SEQRES   3 H  566  HIS LEU THR THR ASP PHE LYS HIS PHE SER ARG VAL THR          
-SEQRES   4 H  566  LYS THR THR PRO GLU GLU ALA SER ARG PHE ASN ALA VAL          
-SEQRES   5 H  566  VAL MET GLY ARG LYS THR TRP GLU SER MET PRO ARG LYS          
-SEQRES   6 H  566  PHE ARG PRO LEU VAL ASP ARG LEU ASN ILE VAL VAL SER          
-SEQRES   7 H  566  SER SER LEU LYS GLU GLU ASP ILE ALA ALA GLU LYS PRO          
-SEQRES   8 H  566  GLN ALA GLU GLY GLN GLN ARG VAL ARG VAL CYS ALA SER          
-SEQRES   9 H  566  LEU PRO ALA ALA LEU SER LEU LEU GLU GLU GLU TYR LYS          
-SEQRES  10 H  566  ASP SER VAL ASP GLN ILE PHE VAL VAL GLY GLY ALA GLY          
-SEQRES  11 H  566  LEU TYR GLU ALA ALA LEU SER LEU GLY VAL ALA SER HIS          
-SEQRES  12 H  566  LEU TYR ILE THR ARG VAL ALA ARG GLU PHE PRO CYS ASP          
-SEQRES  13 H  566  VAL PHE PHE PRO ALA PHE PRO GLY ASP ASP ILE LEU SER          
-SEQRES  14 H  566  ASN LYS SER THR ALA ALA GLU LYS ASP ASN GLU ALA THR          
-SEQRES  15 H  566  TYR ARG PRO ILE PHE ILE SER LYS THR PHE SER ASP ASN          
-SEQRES  16 H  566  GLY VAL PRO TYR ASP PHE VAL VAL LEU GLU LYS ARG ARG          
-SEQRES  17 H  566  LYS THR ASP ASP ALA ALA THR ALA GLU PRO SER ASN ALA          
-SEQRES  18 H  566  MET SER SER LEU THR SER THR ARG GLU THR THR PRO VAL          
-SEQRES  19 H  566  HIS GLY LEU GLN ALA PRO SER SER ALA ALA ALA ILE ALA          
-SEQRES  20 H  566  PRO VAL LEU ALA TRP MET ASP GLU GLU ASP ARG LYS LYS          
-SEQRES  21 H  566  ARG GLU GLN LYS GLU LEU ILE ARG ALA VAL PRO HIS VAL          
-SEQRES  22 H  566  HIS PHE ARG GLY HIS GLU GLU PHE GLN TYR LEU ASP LEU          
-SEQRES  23 H  566  ILE ALA ASP ILE ILE ASN ASN GLY ARG THR MET ASP ASP          
-SEQRES  24 H  566  ARG THR GLY VAL GLY VAL ILE SER LYS PHE GLY CYS THR          
-SEQRES  25 H  566  MET ARG TYR SER LEU ASP GLN ALA PHE PRO LEU LEU THR          
-SEQRES  26 H  566  THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU          
-SEQRES  27 H  566  LEU TRP PHE ILE ARG GLY ASP THR ASN ALA ASN HIS LEU          
-SEQRES  28 H  566  SER GLU LYS GLY VAL LYS ILE TRP ASP LYS ASN VAL THR          
-SEQRES  29 H  566  ARG GLU PHE LEU ASP SER ARG ASN LEU PRO HIS ARG GLU          
-SEQRES  30 H  566  VAL GLY ASP ILE GLY PRO GLY TYR GLY PHE GLN TRP ARG          
-SEQRES  31 H  566  HIS PHE GLY ALA ALA TYR LYS ASP MET HIS THR ASP TYR          
-SEQRES  32 H  566  THR GLY GLN GLY VAL ASP GLN LEU LYS ASN VAL ILE GLN          
-SEQRES  33 H  566  MET LEU ARG THR ASN PRO THR ASP ARG ARG MET LEU MET          
-SEQRES  34 H  566  THR ALA TRP ASN PRO ALA ALA LEU ASP GLU MET ALA LEU          
-SEQRES  35 H  566  PRO PRO CYS HIS LEU LEU CYS GLN PHE TYR VAL ASN ASP          
-SEQRES  36 H  566  GLN LYS GLU LEU SER CYS ILE MET TYR GLN ARG SER CYS          
-SEQRES  37 H  566  ASP VAL GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR          
-SEQRES  38 H  566  SER LEU LEU THR LEU MET VAL ALA HIS VAL CYS ASN LEU          
-SEQRES  39 H  566  LYS PRO LYS GLU PHE ILE HIS PHE MET GLY ASN THR HIS          
-SEQRES  40 H  566  VAL TYR THR ASN HIS VAL GLU ALA LEU LYS GLU GLN LEU          
-SEQRES  41 H  566  ARG ARG GLU PRO ARG PRO PHE PRO ILE VAL ASN ILE LEU          
-SEQRES  42 H  566  ASN LYS GLU ARG ILE LYS GLU ILE ASP ASP PHE THR ALA          
-SEQRES  43 H  566  GLU ASP PHE GLU VAL VAL GLY TYR VAL PRO HIS GLY ARG          
-SEQRES  44 H  566  ILE GLN MET GLU MET ALA VAL                                  
-HET    UMP  A 701      20                                                       
-HET    1UG  A 702      26                                                       
-HET    FOL  A 703      32                                                       
-HET    NDP  A 704      48                                                       
-HET    UMP  B 701      20                                                       
-HET    1UG  B 702      26                                                       
-HET    FOL  B 703      32                                                       
-HET    NDP  B 704      48                                                       
-HET    UMP  C 701      20                                                       
-HET    1UG  C 702      26                                                       
-HET    FOL  C 703      32                                                       
-HET    NDP  C 704      48                                                       
-HET    UMP  D 701      20                                                       
-HET    1UG  D 702      26                                                       
-HET    FOL  D 703      32                                                       
-HET    NDP  D 704      48                                                       
-HET    UMP  E 701      20                                                       
-HET    1UG  E 702      26                                                       
-HET    FOL  E 703      32                                                       
-HET    NDP  E 704      48                                                       
-HET    UMP  F 701      20                                                       
-HET    1UG  F 702      26                                                       
-HET    FOL  F 703      32                                                       
-HET    NDP  F 704      48                                                       
-HET    UMP  G 701      20                                                       
-HET    1UG  G 702      26                                                       
-HET    FOL  G 703      32                                                       
-HET    NDP  G 704      48                                                       
-HET    UMP  H 701      20                                                       
-HET    1UG  H 702      26                                                       
-HET    FOL  H 703      32                                                       
-HET    NDP  H 704      48                                                       
-HETNAM     UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE                                 
-HETNAM     1UG 2-AMINO-5-(1-NAPHTHYLSULFANYL)-3,9-DIHYDRO-4H-                   
-HETNAM   2 1UG  PYRIMIDO[4,5-B]INDOL-4-ONE                                      
-HETNAM     FOL FOLIC ACID                                                       
-HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
-HETNAM   2 NDP  PHOSPHATE                                                       
-HETSYN     UMP DUMP                                                             
-FORMUL   9  UMP    8(C9 H13 N2 O8 P)                                            
-FORMUL  10  1UG    8(C20 H14 N4 O S)                                            
-FORMUL  11  FOL    8(C19 H19 N7 O6)                                             
-FORMUL  12  NDP    8(C21 H30 N7 O17 P3)                                         
-HELIX    1   1 LEU A   28  THR A   41  1                                  14    
-HELIX    2   2 ARG A   81  MET A   87  1                                   7    
-HELIX    3   3 PRO A   88  ARG A   92  5                                   5    
-HELIX    4   4 LYS A  107  ALA A  113  1                                   7    
-HELIX    5   5 SER A  129  LYS A  142  1                                  14    
-HELIX    6   6 GLY A  153  LEU A  163  1                                  11    
-HELIX    7   7 GLY A  189  LEU A  193  5                                   5    
-HELIX    8   8 ALA A  287  ALA A  289  5                                   3    
-HELIX    9   9 ILE A  290  ASP A  298  1                                   9    
-HELIX   10  10 GLU A  324  GLY A  338  1                                  15    
-HELIX   11  11 PHE A  374  ARG A  387  1                                  14    
-HELIX   12  12 ASN A  391  GLU A  397  1                                   7    
-HELIX   13  13 TRP A  403  VAL A  407  5                                   5    
-HELIX   14  14 THR A  408  ARG A  415  1                                   8    
-HELIX   15  15 TYR A  429  PHE A  436  1                                   8    
-HELIX   16  16 ASP A  453  ASN A  465  1                                  13    
-HELIX   17  17 ALA A  480  MET A  484  5                                   5    
-HELIX   18  18 GLY A  517  CYS A  536  1                                  20    
-HELIX   19  19 HIS A  556  LEU A  564  1                                   9    
-HELIX   20  20 ASN A  578  ILE A  582  5                                   5    
-HELIX   21  21 GLU A  584  PHE A  588  5                                   5    
-HELIX   22  22 LEU B   28  THR B   39  1                                  12    
-HELIX   23  23 ARG B   81  MET B   87  1                                   7    
-HELIX   24  24 SER B  129  GLU B  140  1                                  12    
-HELIX   25  25 GLY B  155  LEU B  163  1                                   9    
-HELIX   26  26 GLY B  189  LEU B  193  5                                   5    
-HELIX   27  27 SER B  286  GLU B  300  1                                  15    
-HELIX   28  28 GLU B  324  GLY B  338  1                                  15    
-HELIX   29  29 PHE B  374  GLY B  388  1                                  15    
-HELIX   30  30 ALA B  392  GLU B  397  1                                   6    
-HELIX   31  31 TRP B  403  VAL B  407  5                                   5    
-HELIX   32  32 THR B  408  ARG B  415  1                                   8    
-HELIX   33  33 TYR B  429  PHE B  436  1                                   8    
-HELIX   34  34 ASP B  453  ASN B  465  1                                  13    
-HELIX   35  35 ALA B  480  MET B  484  5                                   5    
-HELIX   36  36 LEU B  516  CYS B  536  1                                  21    
-HELIX   37  37 HIS B  556  LEU B  564  1                                   9    
-HELIX   38  38 ASN B  578  ILE B  582  5                                   5    
-HELIX   39  39 GLU B  584  PHE B  588  5                                   5    
-HELIX   40  40 LEU C   28  THR C   41  1                                  14    
-HELIX   41  41 ARG C   81  MET C   87  1                                   7    
-HELIX   42  42 PRO C   88  ARG C   92  5                                   5    
-HELIX   43  43 LYS C  107  ALA C  113  1                                   7    
-HELIX   44  44 SER C  129  TYR C  141  1                                  13    
-HELIX   45  45 GLY C  153  GLY C  164  1                                  12    
-HELIX   46  46 GLY C  189  LEU C  193  5                                   5    
-HELIX   47  47 ALA C  287  ALA C  289  5                                   3    
-HELIX   48  48 ILE C  290  ASP C  298  1                                   9    
-HELIX   49  49 GLU C  324  GLY C  338  1                                  15    
-HELIX   50  50 PHE C  374  GLY C  388  1                                  15    
-HELIX   51  51 ASN C  391  GLU C  397  1                                   7    
-HELIX   52  52 TRP C  403  VAL C  407  5                                   5    
-HELIX   53  53 THR C  408  ARG C  415  1                                   8    
-HELIX   54  54 TYR C  429  PHE C  436  1                                   8    
-HELIX   55  55 ASP C  453  ASN C  465  1                                  13    
-HELIX   56  56 ALA C  480  MET C  484  5                                   5    
-HELIX   57  57 GLY C  517  CYS C  536  1                                  20    
-HELIX   58  58 HIS C  556  LEU C  564  1                                   9    
-HELIX   59  59 ASN C  578  ILE C  582  5                                   5    
-HELIX   60  60 GLU C  584  PHE C  588  5                                   5    
-HELIX   61  61 LEU D   28  THR D   39  1                                  12    
-HELIX   62  62 GLY D   80  MET D   87  1                                   8    
-HELIX   63  63 SER D  129  GLU D  140  1                                  12    
-HELIX   64  64 GLY D  155  LEU D  163  1                                   9    
-HELIX   65  65 GLY D  189  LEU D  193  5                                   5    
-HELIX   66  66 SER D  286  GLU D  300  1                                  15    
-HELIX   67  67 GLU D  324  GLY D  338  1                                  15    
-HELIX   68  68 PHE D  374  GLY D  388  1                                  15    
-HELIX   69  69 ALA D  392  LYS D  398  1                                   7    
-HELIX   70  70 TRP D  403  VAL D  407  5                                   5    
-HELIX   71  71 THR D  408  ARG D  415  1                                   8    
-HELIX   72  72 GLY D  428  PHE D  436  1                                   9    
-HELIX   73  73 ASP D  453  ASN D  465  1                                  13    
-HELIX   74  74 ALA D  480  MET D  484  5                                   5    
-HELIX   75  75 LEU D  516  CYS D  536  1                                  21    
-HELIX   76  76 HIS D  556  LEU D  564  1                                   9    
-HELIX   77  77 GLU D  584  PHE D  588  5                                   5    
-HELIX   78  78 LEU E   28  THR E   41  1                                  14    
-HELIX   79  79 ARG E   81  MET E   87  1                                   7    
-HELIX   80  80 PRO E   88  ARG E   92  5                                   5    
-HELIX   81  81 LYS E  107  ALA E  113  1                                   7    
-HELIX   82  82 SER E  129  TYR E  141  1                                  13    
-HELIX   83  83 GLY E  153  GLY E  164  1                                  12    
-HELIX   84  84 GLY E  189  LEU E  193  5                                   5    
-HELIX   85  85 ILE E  290  ASP E  298  1                                   9    
-HELIX   86  86 GLU E  324  GLY E  338  1                                  15    
-HELIX   87  87 PHE E  374  GLY E  388  1                                  15    
-HELIX   88  88 ASN E  391  GLU E  397  1                                   7    
-HELIX   89  89 TRP E  403  VAL E  407  5                                   5    
-HELIX   90  90 THR E  408  ARG E  415  1                                   8    
-HELIX   91  91 TYR E  429  PHE E  436  1                                   8    
-HELIX   92  92 ASP E  453  ASN E  465  1                                  13    
-HELIX   93  93 ALA E  480  MET E  484  5                                   5    
-HELIX   94  94 LEU E  516  CYS E  536  1                                  21    
-HELIX   95  95 HIS E  556  LEU E  564  1                                   9    
-HELIX   96  96 ASN E  578  ILE E  582  5                                   5    
-HELIX   97  97 GLU E  584  PHE E  588  5                                   5    
-HELIX   98  98 LEU F   28  THR F   39  1                                  12    
-HELIX   99  99 ARG F   81  MET F   87  1                                   7    
-HELIX  100 100 SER F  129  GLU F  140  1                                  12    
-HELIX  101 101 GLY F  155  LEU F  163  1                                   9    
-HELIX  102 102 GLY F  189  LEU F  193  5                                   5    
-HELIX  103 103 SER F  286  GLU F  300  1                                  15    
-HELIX  104 104 GLU F  324  GLY F  338  1                                  15    
-HELIX  105 105 PHE F  374  GLY F  388  1                                  15    
-HELIX  106 106 ALA F  392  LYS F  398  1                                   7    
-HELIX  107 107 TRP F  403  VAL F  407  5                                   5    
-HELIX  108 108 THR F  408  ARG F  415  1                                   8    
-HELIX  109 109 TYR F  429  PHE F  436  1                                   8    
-HELIX  110 110 ASP F  453  ASN F  465  1                                  13    
-HELIX  111 111 ALA F  480  MET F  484  5                                   5    
-HELIX  112 112 LEU F  516  CYS F  536  1                                  21    
-HELIX  113 113 HIS F  556  LEU F  564  1                                   9    
-HELIX  114 114 GLU F  584  PHE F  588  5                                   5    
-HELIX  115 115 LEU G   28  THR G   41  1                                  14    
-HELIX  116 116 ARG G   81  MET G   87  1                                   7    
-HELIX  117 117 PRO G   88  ARG G   92  5                                   5    
-HELIX  118 118 LYS G  107  ALA G  113  1                                   7    
-HELIX  119 119 SER G  129  TYR G  141  1                                  13    
-HELIX  120 120 GLY G  153  LEU G  163  1                                  11    
-HELIX  121 121 GLY G  189  LEU G  193  5                                   5    
-HELIX  122 122 ALA G  287  ALA G  289  5                                   3    
-HELIX  123 123 ILE G  290  ASP G  298  1                                   9    
-HELIX  124 124 GLU G  324  GLY G  338  1                                  15    
-HELIX  125 125 PHE G  374  ARG G  387  1                                  14    
-HELIX  126 126 ALA G  392  GLU G  397  1                                   6    
-HELIX  127 127 TRP G  403  VAL G  407  5                                   5    
-HELIX  128 128 THR G  408  ARG G  415  1                                   8    
-HELIX  129 129 TYR G  429  PHE G  436  1                                   8    
-HELIX  130 130 ASP G  453  ASN G  465  1                                  13    
-HELIX  131 131 ALA G  480  MET G  484  5                                   5    
-HELIX  132 132 GLY G  517  CYS G  536  1                                  20    
-HELIX  133 133 HIS G  556  LEU G  564  1                                   9    
-HELIX  134 134 ASN G  578  ILE G  582  5                                   5    
-HELIX  135 135 GLU G  584  PHE G  588  5                                   5    
-HELIX  136 136 LEU H   28  THR H   39  1                                  12    
-HELIX  137 137 GLY H   80  MET H   87  1                                   8    
-HELIX  138 138 SER H  129  GLU H  140  1                                  12    
-HELIX  139 139 GLY H  155  LEU H  163  1                                   9    
-HELIX  140 140 GLY H  189  LEU H  193  5                                   5    
-HELIX  141 141 SER H  286  GLU H  300  1                                  15    
-HELIX  142 142 GLU H  324  GLY H  338  1                                  15    
-HELIX  143 143 PHE H  374  GLY H  388  1                                  15    
-HELIX  144 144 ALA H  392  GLU H  397  1                                   6    
-HELIX  145 145 TRP H  403  VAL H  407  5                                   5    
-HELIX  146 146 THR H  408  ARG H  415  1                                   8    
-HELIX  147 147 GLY H  428  PHE H  436  1                                   9    
-HELIX  148 148 ASP H  453  ASN H  465  1                                  13    
-HELIX  149 149 ASN H  477  LEU H  481  5                                   5    
-HELIX  150 150 LEU H  516  CYS H  536  1                                  21    
-HELIX  151 151 HIS H  556  LEU H  564  1                                   9    
-HELIX  152 152 GLU H  584  PHE H  588  5                                   5    
-SHEET    1   A 8 ARG A 125  CYS A 127  0                                        
-SHEET    2   A 8 ARG A  97  VAL A 102  1  N  VAL A 101   O  ARG A 125           
-SHEET    3   A 8 PHE A  74  GLY A  80  1  N  VAL A  77   O  ILE A 100           
-SHEET    4   A 8 VAL A 145  GLY A 152  1  O  GLN A 147   N  ALA A  76           
-SHEET    5   A 8 VAL A   5  MET A  11  1  N  CYS A   6   O  ILE A 148           
-SHEET    6   A 8 ALA A 166  VAL A 174  1  O  VAL A 174   N  MET A  11           
-SHEET    7   A 8 VAL A 241  LYS A 250 -1  O  VAL A 246   N  ILE A 171           
-SHEET    8   A 8 PHE A 236  ASP A 238 -1  N  PHE A 236   O  TYR A 243           
-SHEET    1   B 9 ARG A 125  CYS A 127  0                                        
-SHEET    2   B 9 ARG A  97  VAL A 102  1  N  VAL A 101   O  ARG A 125           
-SHEET    3   B 9 PHE A  74  GLY A  80  1  N  VAL A  77   O  ILE A 100           
-SHEET    4   B 9 VAL A 145  GLY A 152  1  O  GLN A 147   N  ALA A  76           
-SHEET    5   B 9 VAL A   5  MET A  11  1  N  CYS A   6   O  ILE A 148           
-SHEET    6   B 9 ALA A 166  VAL A 174  1  O  VAL A 174   N  MET A  11           
-SHEET    7   B 9 VAL A 241  LYS A 250 -1  O  VAL A 246   N  ILE A 171           
-SHEET    8   B 9 TYR A 227  ILE A 232 -1  N  ILE A 230   O  VAL A 247           
-SHEET    9   B 9 PHE A 319  ARG A 320  1  O  PHE A 319   N  ILE A 230           
-SHEET    1   C 2 GLY A  16  GLY A  18  0                                        
-SHEET    2   C 2 VAL A 182  PHE A 183 -1  O  VAL A 182   N  ILE A  17           
-SHEET    1   D 6 ARG A 339  MET A 341  0                                        
-SHEET    2   D 6 VAL A 349  SER A 360 -1  O  VAL A 349   N  MET A 341           
-SHEET    3   D 6 LYS A 539  TYR A 553 -1  O  THR A 550   N  LYS A 352           
-SHEET    4   D 6 GLU A 502  ASP A 513  1  N  CYS A 505   O  ILE A 544           
-SHEET    5   D 6 HIS A 490  VAL A 497 -1  N  LEU A 492   O  TYR A 508           
-SHEET    6   D 6 LEU A 472  THR A 474 -1  N  MET A 473   O  CYS A 493           
-SHEET    1   E 2 ILE A 573  ILE A 576  0                                        
-SHEET    2   E 2 PHE A 593  VAL A 596 -1  O  GLU A 594   N  ASN A 575           
-SHEET    1   F 8 ARG B  97  VAL B 102  0                                        
-SHEET    2   F 8 ASN B  75  GLY B  80  1  N  VAL B  77   O  LEU B  98           
-SHEET    3   F 8 ILE B 148  VAL B 150  1  O  PHE B 149   N  VAL B  78           
-SHEET    4   F 8 VAL B   5  MET B  11  1  N  VAL B   8   O  VAL B 150           
-SHEET    5   F 8 ALA B 166  ARG B 173  1  O  TYR B 170   N  LEU B   7           
-SHEET    6   F 8 VAL B 246  ARG B 251 -1  O  VAL B 246   N  ILE B 171           
-SHEET    7   F 8 THR B 226  ILE B 232 -1  N  ILE B 230   O  VAL B 247           
-SHEET    8   F 8 PHE B 319  ARG B 320  1  O  PHE B 319   N  ILE B 232           
-SHEET    1   G 2 GLY B  16  GLY B  18  0                                        
-SHEET    2   G 2 VAL B 182  PHE B 183 -1  O  VAL B 182   N  ILE B  17           
-SHEET    1   H 2 PHE B 236  ASP B 238  0                                        
-SHEET    2   H 2 VAL B 241  TYR B 243 -1  O  TYR B 243   N  PHE B 236           
-SHEET    1   I 6 ARG B 339  MET B 341  0                                        
-SHEET    2   I 6 VAL B 349  SER B 360 -1  O  SER B 351   N  ARG B 339           
-SHEET    3   I 6 LYS B 539  TYR B 553 -1  O  MET B 547   N  CYS B 355           
-SHEET    4   I 6 GLU B 502  ASP B 513  1  N  CYS B 505   O  ILE B 544           
-SHEET    5   I 6 HIS B 490  VAL B 497 -1  N  GLN B 494   O  ILE B 506           
-SHEET    6   I 6 LEU B 472  THR B 474 -1  N  MET B 473   O  CYS B 493           
-SHEET    1   J 2 ILE B 573  ILE B 576  0                                        
-SHEET    2   J 2 PHE B 593  VAL B 596 -1  O  VAL B 596   N  ILE B 573           
-SHEET    1   K 8 ARG C 125  CYS C 127  0                                        
-SHEET    2   K 8 ARG C  97  VAL C 102  1  N  VAL C 101   O  ARG C 125           
-SHEET    3   K 8 PHE C  74  GLY C  80  1  N  MET C  79   O  VAL C 102           
-SHEET    4   K 8 VAL C 145  GLY C 152  1  O  PHE C 149   N  ALA C  76           
-SHEET    5   K 8 VAL C   5  MET C  11  1  N  CYS C   6   O  ILE C 148           
-SHEET    6   K 8 ALA C 166  VAL C 174  1  O  VAL C 174   N  MET C  11           
-SHEET    7   K 8 VAL C 241  LYS C 250 -1  O  VAL C 246   N  ILE C 171           
-SHEET    8   K 8 PHE C 236  ASP C 238 -1  N  PHE C 236   O  TYR C 243           
-SHEET    1   L 9 ARG C 125  CYS C 127  0                                        
-SHEET    2   L 9 ARG C  97  VAL C 102  1  N  VAL C 101   O  ARG C 125           
-SHEET    3   L 9 PHE C  74  GLY C  80  1  N  MET C  79   O  VAL C 102           
-SHEET    4   L 9 VAL C 145  GLY C 152  1  O  PHE C 149   N  ALA C  76           
-SHEET    5   L 9 VAL C   5  MET C  11  1  N  CYS C   6   O  ILE C 148           
-SHEET    6   L 9 ALA C 166  VAL C 174  1  O  VAL C 174   N  MET C  11           
-SHEET    7   L 9 VAL C 241  LYS C 250 -1  O  VAL C 246   N  ILE C 171           
-SHEET    8   L 9 TYR C 227  ILE C 232 -1  N  ILE C 230   O  VAL C 247           
-SHEET    9   L 9 PHE C 319  ARG C 320  1  O  PHE C 319   N  ILE C 232           
-SHEET    1   M 2 GLY C  16  GLY C  18  0                                        
-SHEET    2   M 2 VAL C 182  PHE C 183 -1  O  VAL C 182   N  ILE C  17           
-SHEET    1   N 6 ARG C 339  MET C 341  0                                        
-SHEET    2   N 6 VAL C 349  SER C 360 -1  O  SER C 351   N  ARG C 339           
-SHEET    3   N 6 LYS C 539  TYR C 553 -1  O  THR C 550   N  LYS C 352           
-SHEET    4   N 6 GLU C 502  ASP C 513  1  N  CYS C 505   O  ILE C 544           
-SHEET    5   N 6 HIS C 490  VAL C 497 -1  N  GLN C 494   O  ILE C 506           
-SHEET    6   N 6 LEU C 472  THR C 474 -1  N  MET C 473   O  CYS C 493           
-SHEET    1   O 2 ILE C 573  ILE C 576  0                                        
-SHEET    2   O 2 PHE C 593  VAL C 596 -1  O  GLU C 594   N  ASN C 575           
-SHEET    1   P 7 ARG D  97  VAL D 101  0                                        
-SHEET    2   P 7 ASN D  75  MET D  79  1  N  VAL D  77   O  LEU D  98           
-SHEET    3   P 7 ILE D 148  VAL D 150  1  O  PHE D 149   N  VAL D  78           
-SHEET    4   P 7 VAL D   5  MET D  11  1  N  VAL D   8   O  VAL D 150           
-SHEET    5   P 7 ALA D 166  VAL D 174  1  O  TYR D 170   N  LEU D   7           
-SHEET    6   P 7 VAL D 241  ARG D 251 -1  O  VAL D 246   N  ILE D 171           
-SHEET    7   P 7 PHE D 236  ASP D 238 -1  N  PHE D 236   O  TYR D 243           
-SHEET    1   Q 8 ARG D  97  VAL D 101  0                                        
-SHEET    2   Q 8 ASN D  75  MET D  79  1  N  VAL D  77   O  LEU D  98           
-SHEET    3   Q 8 ILE D 148  VAL D 150  1  O  PHE D 149   N  VAL D  78           
-SHEET    4   Q 8 VAL D   5  MET D  11  1  N  VAL D   8   O  VAL D 150           
-SHEET    5   Q 8 ALA D 166  VAL D 174  1  O  TYR D 170   N  LEU D   7           
-SHEET    6   Q 8 VAL D 241  ARG D 251 -1  O  VAL D 246   N  ILE D 171           
-SHEET    7   Q 8 THR D 226  ILE D 232 -1  N  ILE D 230   O  VAL D 247           
-SHEET    8   Q 8 PHE D 319  ARG D 320  1  O  PHE D 319   N  ILE D 232           
-SHEET    1   R 2 GLY D  16  GLY D  18  0                                        
-SHEET    2   R 2 VAL D 182  PHE D 183 -1  O  VAL D 182   N  ILE D  17           
-SHEET    1   S 6 ARG D 339  MET D 341  0                                        
-SHEET    2   S 6 VAL D 349  SER D 360 -1  O  SER D 351   N  ARG D 339           
-SHEET    3   S 6 LYS D 539  TYR D 553 -1  O  HIS D 545   N  MET D 357           
-SHEET    4   S 6 GLU D 502  ASP D 513  1  N  CYS D 505   O  ILE D 544           
-SHEET    5   S 6 HIS D 490  VAL D 497 -1  N  GLN D 494   O  ILE D 506           
-SHEET    6   S 6 LEU D 472  THR D 474 -1  N  MET D 473   O  CYS D 493           
-SHEET    1   T 2 ILE D 573  ILE D 576  0                                        
-SHEET    2   T 2 PHE D 593  VAL D 596 -1  O  VAL D 596   N  ILE D 573           
-SHEET    1   U 8 ARG E 125  CYS E 127  0                                        
-SHEET    2   U 8 ARG E  97  VAL E 102  1  N  VAL E 101   O  ARG E 125           
-SHEET    3   U 8 PHE E  74  GLY E  80  1  N  VAL E  77   O  ILE E 100           
-SHEET    4   U 8 VAL E 145  GLY E 152  1  O  PHE E 149   N  ALA E  76           
-SHEET    5   U 8 VAL E   5  MET E  11  1  N  CYS E   6   O  ILE E 148           
-SHEET    6   U 8 ALA E 166  VAL E 174  1  O  VAL E 174   N  MET E  11           
-SHEET    7   U 8 VAL E 241  LYS E 250 -1  O  VAL E 246   N  ILE E 171           
-SHEET    8   U 8 PHE E 236  ASP E 238 -1  N  PHE E 236   O  TYR E 243           
-SHEET    1   V 9 ARG E 125  CYS E 127  0                                        
-SHEET    2   V 9 ARG E  97  VAL E 102  1  N  VAL E 101   O  ARG E 125           
-SHEET    3   V 9 PHE E  74  GLY E  80  1  N  VAL E  77   O  ILE E 100           
-SHEET    4   V 9 VAL E 145  GLY E 152  1  O  PHE E 149   N  ALA E  76           
-SHEET    5   V 9 VAL E   5  MET E  11  1  N  CYS E   6   O  ILE E 148           
-SHEET    6   V 9 ALA E 166  VAL E 174  1  O  VAL E 174   N  MET E  11           
-SHEET    7   V 9 VAL E 241  LYS E 250 -1  O  VAL E 246   N  ILE E 171           
-SHEET    8   V 9 TYR E 227  ILE E 232 -1  N  ILE E 230   O  VAL E 247           
-SHEET    9   V 9 PHE E 319  ARG E 320  1  O  PHE E 319   N  ILE E 232           
-SHEET    1   W 2 GLY E  16  GLY E  18  0                                        
-SHEET    2   W 2 VAL E 182  PHE E 183 -1  O  VAL E 182   N  ILE E  17           
-SHEET    1   X 6 ARG E 339  MET E 341  0                                        
-SHEET    2   X 6 VAL E 349  SER E 360 -1  O  VAL E 349   N  MET E 341           
-SHEET    3   X 6 LYS E 539  TYR E 553 -1  O  THR E 550   N  LYS E 352           
-SHEET    4   X 6 GLU E 502  ASP E 513  1  N  CYS E 505   O  ILE E 544           
-SHEET    5   X 6 HIS E 490  VAL E 497 -1  N  GLN E 494   O  ILE E 506           
-SHEET    6   X 6 LEU E 472  THR E 474 -1  N  MET E 473   O  CYS E 493           
-SHEET    1   Y 2 ILE E 573  ILE E 576  0                                        
-SHEET    2   Y 2 PHE E 593  VAL E 596 -1  O  GLU E 594   N  ASN E 575           
-SHEET    1   Z 7 ARG F  97  VAL F 102  0                                        
-SHEET    2   Z 7 ASN F  75  GLY F  80  1  N  VAL F  77   O  LEU F  98           
-SHEET    3   Z 7 ILE F 148  VAL F 150  1  O  PHE F 149   N  VAL F  78           
-SHEET    4   Z 7 VAL F   5  MET F  11  1  N  VAL F   8   O  VAL F 150           
-SHEET    5   Z 7 ALA F 166  VAL F 174  1  O  TYR F 170   N  LEU F   7           
-SHEET    6   Z 7 VAL F 241  ARG F 251 -1  O  VAL F 246   N  ILE F 171           
-SHEET    7   Z 7 PHE F 236  ASP F 238 -1  N  PHE F 236   O  TYR F 243           
-SHEET    1  AA 8 ARG F  97  VAL F 102  0                                        
-SHEET    2  AA 8 ASN F  75  GLY F  80  1  N  VAL F  77   O  LEU F  98           
-SHEET    3  AA 8 ILE F 148  VAL F 150  1  O  PHE F 149   N  VAL F  78           
-SHEET    4  AA 8 VAL F   5  MET F  11  1  N  VAL F   8   O  VAL F 150           
-SHEET    5  AA 8 ALA F 166  VAL F 174  1  O  TYR F 170   N  LEU F   7           
-SHEET    6  AA 8 VAL F 241  ARG F 251 -1  O  VAL F 246   N  ILE F 171           
-SHEET    7  AA 8 THR F 226  ILE F 232 -1  N  ARG F 228   O  GLU F 249           
-SHEET    8  AA 8 PHE F 319  ARG F 320  1  O  PHE F 319   N  ILE F 232           
-SHEET    1  AB 2 GLY F  16  GLY F  18  0                                        
-SHEET    2  AB 2 VAL F 182  PHE F 183 -1  O  VAL F 182   N  ILE F  17           
-SHEET    1  AC 6 ARG F 339  MET F 341  0                                        
-SHEET    2  AC 6 VAL F 349  SER F 360 -1  O  SER F 351   N  ARG F 339           
-SHEET    3  AC 6 LYS F 539  TYR F 553 -1  O  MET F 547   N  CYS F 355           
-SHEET    4  AC 6 GLU F 502  ASP F 513  1  N  CYS F 505   O  ILE F 544           
-SHEET    5  AC 6 HIS F 490  VAL F 497 -1  N  GLN F 494   O  ILE F 506           
-SHEET    6  AC 6 LEU F 472  THR F 474 -1  N  MET F 473   O  CYS F 493           
-SHEET    1  AD 2 ILE F 573  ILE F 576  0                                        
-SHEET    2  AD 2 PHE F 593  VAL F 596 -1  O  VAL F 596   N  ILE F 573           
-SHEET    1  AE 8 ARG G 125  CYS G 127  0                                        
-SHEET    2  AE 8 ARG G  97  VAL G 102  1  N  VAL G 101   O  ARG G 125           
-SHEET    3  AE 8 PHE G  74  GLY G  80  1  N  MET G  79   O  VAL G 102           
-SHEET    4  AE 8 VAL G 145  GLY G 152  1  O  PHE G 149   N  ALA G  76           
-SHEET    5  AE 8 VAL G   5  MET G  11  1  N  CYS G   6   O  ILE G 148           
-SHEET    6  AE 8 ALA G 166  VAL G 174  1  O  VAL G 174   N  MET G  11           
-SHEET    7  AE 8 VAL G 241  LYS G 250 -1  O  VAL G 246   N  ILE G 171           
-SHEET    8  AE 8 PHE G 236  ASP G 238 -1  N  PHE G 236   O  TYR G 243           
-SHEET    1  AF 9 ARG G 125  CYS G 127  0                                        
-SHEET    2  AF 9 ARG G  97  VAL G 102  1  N  VAL G 101   O  ARG G 125           
-SHEET    3  AF 9 PHE G  74  GLY G  80  1  N  MET G  79   O  VAL G 102           
-SHEET    4  AF 9 VAL G 145  GLY G 152  1  O  PHE G 149   N  ALA G  76           
-SHEET    5  AF 9 VAL G   5  MET G  11  1  N  CYS G   6   O  ILE G 148           
-SHEET    6  AF 9 ALA G 166  VAL G 174  1  O  VAL G 174   N  MET G  11           
-SHEET    7  AF 9 VAL G 241  LYS G 250 -1  O  VAL G 246   N  ILE G 171           
-SHEET    8  AF 9 TYR G 227  ILE G 232 -1  N  ILE G 230   O  VAL G 247           
-SHEET    9  AF 9 PHE G 319  ARG G 320  1  O  PHE G 319   N  ILE G 232           
-SHEET    1  AG 2 GLY G  16  GLY G  18  0                                        
-SHEET    2  AG 2 VAL G 182  PHE G 183 -1  O  VAL G 182   N  ILE G  17           
-SHEET    1  AH 6 ARG G 339  MET G 341  0                                        
-SHEET    2  AH 6 VAL G 349  SER G 360 -1  O  VAL G 349   N  MET G 341           
-SHEET    3  AH 6 LYS G 539  TYR G 553 -1  O  MET G 547   N  CYS G 355           
-SHEET    4  AH 6 GLU G 502  ASP G 513  1  N  CYS G 505   O  ILE G 544           
-SHEET    5  AH 6 HIS G 490  VAL G 497 -1  N  GLN G 494   O  ILE G 506           
-SHEET    6  AH 6 LEU G 472  THR G 474 -1  N  MET G 473   O  CYS G 493           
-SHEET    1  AI 2 ILE G 573  ILE G 576  0                                        
-SHEET    2  AI 2 PHE G 593  VAL G 596 -1  O  GLU G 594   N  ASN G 575           
-SHEET    1  AJ 7 ARG H  97  VAL H 101  0                                        
-SHEET    2  AJ 7 ASN H  75  MET H  79  1  N  VAL H  77   O  LEU H  98           
-SHEET    3  AJ 7 ILE H 148  VAL H 150  1  O  PHE H 149   N  VAL H  78           
-SHEET    4  AJ 7 VAL H   5  MET H  11  1  N  VAL H   8   O  VAL H 150           
-SHEET    5  AJ 7 ALA H 166  VAL H 174  1  O  TYR H 170   N  LEU H   7           
-SHEET    6  AJ 7 VAL H 241  ARG H 251 -1  O  VAL H 246   N  ILE H 171           
-SHEET    7  AJ 7 PHE H 236  ASP H 238 -1  N  PHE H 236   O  TYR H 243           
-SHEET    1  AK 8 ARG H  97  VAL H 101  0                                        
-SHEET    2  AK 8 ASN H  75  MET H  79  1  N  VAL H  77   O  LEU H  98           
-SHEET    3  AK 8 ILE H 148  VAL H 150  1  O  PHE H 149   N  VAL H  78           
-SHEET    4  AK 8 VAL H   5  MET H  11  1  N  VAL H   8   O  VAL H 150           
-SHEET    5  AK 8 ALA H 166  VAL H 174  1  O  TYR H 170   N  LEU H   7           
-SHEET    6  AK 8 VAL H 241  ARG H 251 -1  O  VAL H 246   N  ILE H 171           
-SHEET    7  AK 8 THR H 226  ILE H 232 -1  N  ILE H 230   O  VAL H 247           
-SHEET    8  AK 8 PHE H 319  ARG H 320  1  O  PHE H 319   N  ILE H 232           
-SHEET    1  AL 2 GLY H  16  GLY H  18  0                                        
-SHEET    2  AL 2 VAL H 182  PHE H 183 -1  O  VAL H 182   N  ILE H  17           
-SHEET    1  AM 6 ARG H 339  MET H 341  0                                        
-SHEET    2  AM 6 VAL H 349  SER H 360 -1  O  SER H 351   N  ARG H 339           
-SHEET    3  AM 6 LYS H 539  TYR H 553 -1  O  MET H 547   N  CYS H 355           
-SHEET    4  AM 6 GLU H 502  ASP H 513  1  N  GLN H 509   O  GLY H 548           
-SHEET    5  AM 6 HIS H 490  VAL H 497 -1  N  GLN H 494   O  ILE H 506           
-SHEET    6  AM 6 LEU H 472  THR H 474 -1  N  MET H 473   O  CYS H 493           
-SHEET    1  AN 2 ILE H 573  ILE H 576  0                                        
-SHEET    2  AN 2 PHE H 593  VAL H 596 -1  O  VAL H 596   N  ILE H 573           
-CISPEP   1 ARG A   92    PRO A   93          0        -1.56                     
-CISPEP   2 GLY A  152    GLY A  153          0        -1.51                     
-CISPEP   3 GLU B  300    ASP B  301          0         0.54                     
-CISPEP   4 ARG C   92    PRO C   93          0        -1.74                     
-CISPEP   5 GLY C  152    GLY C  153          0        -1.31                     
-CISPEP   6 GLU D  300    ASP D  301          0         0.27                     
-CISPEP   7 ARG E   92    PRO E   93          0        -2.02                     
-CISPEP   8 GLY E  152    GLY E  153          0         0.03                     
-CISPEP   9 GLU F  300    ASP F  301          0         0.58                     
-CISPEP  10 ARG G   92    PRO G   93          0        -1.05                     
-CISPEP  11 GLY G  152    GLY G  153          0        -0.40                     
-CISPEP  12 GLU H  300    ASP H  301          0         2.12                     
-SITE     1 AC1 14 ARG A 344  CYS A 489  HIS A 490  GLN A 509                    
-SITE     2 AC1 14 ARG A 510  SER A 511  CYS A 512  ASP A 513                    
-SITE     3 AC1 14 ASN A 521  HIS A 551  TYR A 553  1UG A 702                    
-SITE     4 AC1 14 ARG B 469  ARG B 470                                          
-SITE     1 AC2  8 ILE A 402  ASN A 406  ASP A 513  LEU A 516                    
-SITE     2 AC2  8 PHE A 520  TYR A 553  ALA A 609  UMP A 701                    
-SITE     1 AC3 13 VAL A   8  VAL A   9  ALA A  10  ASP A  31                    
-SITE     2 AC3 13 PHE A  32  PHE A  35  SER A  36  PHE A  91                    
-SITE     3 AC3 13 LEU A  94  ARG A  97  VAL A 151  THR A 172                    
-SITE     4 AC3 13 NDP A 704                                                     
-SITE     1 AC4 25 VAL A   9  ALA A  10  ILE A  17  GLY A  18                    
-SITE     2 AC4 25 ASN A  21  GLY A  22  TRP A  25  GLY A  80                    
-SITE     3 AC4 25 ARG A  81  LYS A  82  THR A  83  VAL A 102                    
-SITE     4 AC4 25 SER A 103  SER A 104  SER A 105  ALA A 128                    
-SITE     5 AC4 25 VAL A 151  GLY A 152  GLY A 153  ALA A 154                    
-SITE     6 AC4 25 GLY A 155  LEU A 156  TYR A 157  VAL A 182                    
-SITE     7 AC4 25 FOL A 703                                                     
-SITE     1 AC5 13 ARG A 469  ARG A 470  CYS B 489  HIS B 490                    
-SITE     2 AC5 13 GLN B 509  ARG B 510  SER B 511  CYS B 512                    
-SITE     3 AC5 13 ASP B 513  ASN B 521  HIS B 551  TYR B 553                    
-SITE     4 AC5 13 1UG B 702                                                     
-SITE     1 AC6  9 ILE B 402  ASN B 406  ASP B 513  LEU B 516                    
-SITE     2 AC6  9 GLY B 517  PHE B 520  MET B 608  ALA B 609                    
-SITE     3 AC6  9 UMP B 701                                                     
-SITE     1 AC7 13 VAL B   8  VAL B   9  ALA B  10  ASP B  31                    
-SITE     2 AC7 13 PHE B  32  PHE B  35  SER B  36  PHE B  91                    
-SITE     3 AC7 13 LEU B  94  ARG B  97  VAL B 151  THR B 172                    
-SITE     4 AC7 13 NDP B 704                                                     
-SITE     1 AC8 16 ALA B  10  ILE B  17  GLY B  18  ASN B  21                    
-SITE     2 AC8 16 GLY B  22  ARG B  81  LYS B  82  THR B  83                    
-SITE     3 AC8 16 SER B  86  VAL B 102  SER B 103  SER B 104                    
-SITE     4 AC8 16 GLY B 153  ALA B 154  TYR B 157  FOL B 703                    
-SITE     1 AC9 14 ARG C 344  CYS C 489  HIS C 490  GLN C 509                    
-SITE     2 AC9 14 ARG C 510  SER C 511  CYS C 512  ASP C 513                    
-SITE     3 AC9 14 ASN C 521  HIS C 551  TYR C 553  1UG C 702                    
-SITE     4 AC9 14 ARG D 469  ARG D 470                                          
-SITE     1 BC1 10 GLU C 381  ILE C 402  TRP C 403  ASN C 406                    
-SITE     2 BC1 10 LEU C 486  LEU C 516  PHE C 520  MET C 608                    
-SITE     3 BC1 10 ALA C 609  UMP C 701                                          
-SITE     1 BC2 13 VAL C   8  VAL C   9  ALA C  10  ASP C  31                    
-SITE     2 BC2 13 PHE C  32  PHE C  35  SER C  36  PHE C  91                    
-SITE     3 BC2 13 LEU C  94  ARG C  97  VAL C 151  THR C 172                    
-SITE     4 BC2 13 NDP C 704                                                     
-SITE     1 BC3 26 VAL C   9  ALA C  10  ILE C  17  GLY C  18                    
-SITE     2 BC3 26 ASN C  21  GLY C  22  TRP C  25  GLY C  80                    
-SITE     3 BC3 26 ARG C  81  LYS C  82  THR C  83  SER C  86                    
-SITE     4 BC3 26 VAL C 102  SER C 103  SER C 104  SER C 105                    
-SITE     5 BC3 26 ALA C 128  VAL C 151  GLY C 152  GLY C 153                    
-SITE     6 BC3 26 ALA C 154  GLY C 155  LEU C 156  TYR C 157                    
-SITE     7 BC3 26 VAL C 182  FOL C 703                                          
-SITE     1 BC4 13 ARG C 469  ARG C 470  LEU D 486  CYS D 489                    
-SITE     2 BC4 13 HIS D 490  GLN D 509  ARG D 510  SER D 511                    
-SITE     3 BC4 13 ASP D 513  ASN D 521  HIS D 551  TYR D 553                    
-SITE     4 BC4 13 1UG D 702                                                     
-SITE     1 BC5  9 ILE D 402  ASN D 406  ASP D 513  GLY D 517                    
-SITE     2 BC5  9 PHE D 520  TYR D 553  MET D 608  ALA D 609                    
-SITE     3 BC5  9 UMP D 701                                                     
-SITE     1 BC6 12 VAL D   8  VAL D   9  ALA D  10  ASP D  31                    
-SITE     2 BC6 12 PHE D  32  PHE D  35  SER D  36  PHE D  91                    
-SITE     3 BC6 12 ARG D  97  VAL D 151  THR D 172  NDP D 704                    
-SITE     1 BC7 17 VAL D   9  ALA D  10  ILE D  17  GLY D  18                    
-SITE     2 BC7 17 ASN D  21  GLY D  22  GLY D  80  ARG D  81                    
-SITE     3 BC7 17 LYS D  82  THR D  83  SER D  86  SER D 103                    
-SITE     4 BC7 17 SER D 104  GLY D 153  ALA D 154  TYR D 157                    
-SITE     5 BC7 17 FOL D 703                                                     
-SITE     1 BC8 14 ARG E 344  CYS E 489  HIS E 490  GLN E 509                    
-SITE     2 BC8 14 ARG E 510  SER E 511  CYS E 512  ASP E 513                    
-SITE     3 BC8 14 ASN E 521  HIS E 551  TYR E 553  1UG E 702                    
-SITE     4 BC8 14 ARG F 469  ARG F 470                                          
-SITE     1 BC9  9 ILE E 402  ASN E 406  ASP E 513  LEU E 516                    
-SITE     2 BC9  9 PHE E 520  TYR E 553  MET E 608  ALA E 609                    
-SITE     3 BC9  9 UMP E 701                                                     
-SITE     1 CC1 13 VAL E   8  VAL E   9  ALA E  10  ASP E  31                    
-SITE     2 CC1 13 PHE E  32  PHE E  35  SER E  36  PHE E  91                    
-SITE     3 CC1 13 LEU E  94  ARG E  97  VAL E 151  THR E 172                    
-SITE     4 CC1 13 NDP E 704                                                     
-SITE     1 CC2 26 VAL E   9  ALA E  10  ILE E  17  GLY E  18                    
-SITE     2 CC2 26 ILE E  19  ASN E  21  GLY E  22  TRP E  25                    
-SITE     3 CC2 26 GLY E  80  ARG E  81  LYS E  82  THR E  83                    
-SITE     4 CC2 26 SER E  86  VAL E 102  SER E 103  SER E 104                    
-SITE     5 CC2 26 SER E 105  VAL E 151  GLY E 152  GLY E 153                    
-SITE     6 CC2 26 ALA E 154  GLY E 155  LEU E 156  TYR E 157                    
-SITE     7 CC2 26 VAL E 182  FOL E 703                                          
-SITE     1 CC3 12 ARG E 469  ARG E 470  CYS F 489  HIS F 490                    
-SITE     2 CC3 12 GLN F 509  ARG F 510  SER F 511  ASP F 513                    
-SITE     3 CC3 12 ASN F 521  HIS F 551  TYR F 553  1UG F 702                    
-SITE     1 CC4  9 ILE F 402  ASN F 406  ASP F 513  LEU F 516                    
-SITE     2 CC4  9 PHE F 520  TYR F 553  MET F 608  ALA F 609                    
-SITE     3 CC4  9 UMP F 701                                                     
-SITE     1 CC5 13 VAL F   8  VAL F   9  ALA F  10  ASP F  31                    
-SITE     2 CC5 13 PHE F  32  PHE F  35  SER F  36  PHE F  91                    
-SITE     3 CC5 13 LEU F  94  ARG F  97  VAL F 151  THR F 172                    
-SITE     4 CC5 13 NDP F 704                                                     
-SITE     1 CC6 19 VAL F   9  ALA F  10  ILE F  17  GLY F  18                    
-SITE     2 CC6 19 ASN F  21  GLY F  22  ARG F  81  LYS F  82                    
-SITE     3 CC6 19 THR F  83  SER F  86  VAL F 102  SER F 103                    
-SITE     4 CC6 19 SER F 104  GLY F 153  ALA F 154  GLY F 155                    
-SITE     5 CC6 19 TYR F 157  ALA F 159  FOL F 703                               
-SITE     1 CC7 15 ARG G 344  LEU G 486  CYS G 489  HIS G 490                    
-SITE     2 CC7 15 GLN G 509  ARG G 510  SER G 511  CYS G 512                    
-SITE     3 CC7 15 ASP G 513  ASN G 521  HIS G 551  TYR G 553                    
-SITE     4 CC7 15 1UG G 702  ARG H 469  ARG H 470                               
-SITE     1 CC8  9 ILE G 402  ASN G 406  ASP G 513  LEU G 516                    
-SITE     2 CC8  9 PHE G 520  TYR G 553  MET G 608  ALA G 609                    
-SITE     3 CC8  9 UMP G 701                                                     
-SITE     1 CC9 13 VAL G   8  VAL G   9  ALA G  10  ASP G  31                    
-SITE     2 CC9 13 PHE G  32  PHE G  35  SER G  36  PHE G  91                    
-SITE     3 CC9 13 LEU G  94  ARG G  97  VAL G 151  THR G 172                    
-SITE     4 CC9 13 NDP G 704                                                     
-SITE     1 DC1 27 VAL G   9  ALA G  10  ILE G  17  GLY G  18                    
-SITE     2 DC1 27 ILE G  19  ASN G  21  GLY G  22  TRP G  25                    
-SITE     3 DC1 27 GLY G  80  ARG G  81  LYS G  82  THR G  83                    
-SITE     4 DC1 27 SER G  86  VAL G 102  SER G 103  SER G 104                    
-SITE     5 DC1 27 SER G 105  ALA G 128  VAL G 151  GLY G 152                    
-SITE     6 DC1 27 GLY G 153  ALA G 154  GLY G 155  LEU G 156                    
-SITE     7 DC1 27 TYR G 157  VAL G 182  FOL G 703                               
-SITE     1 DC2 12 ARG G 469  ARG G 470  CYS H 489  HIS H 490                    
-SITE     2 DC2 12 GLN H 509  ARG H 510  SER H 511  ASP H 513                    
-SITE     3 DC2 12 ASN H 521  HIS H 551  TYR H 553  1UG H 702                    
-SITE     1 DC3 10 ILE H 402  TRP H 403  ASN H 406  ASP H 513                    
-SITE     2 DC3 10 LEU H 516  GLY H 517  PHE H 520  MET H 608                    
-SITE     3 DC3 10 ALA H 609  UMP H 701                                          
-SITE     1 DC4 12 VAL H   8  VAL H   9  ALA H  10  ASP H  31                    
-SITE     2 DC4 12 PHE H  32  PHE H  35  SER H  36  PHE H  91                    
-SITE     3 DC4 12 ARG H  97  VAL H 151  THR H 172  NDP H 704                    
-SITE     1 DC5 15 ALA H  10  ILE H  17  GLY H  18  ASN H  21                    
-SITE     2 DC5 15 GLY H  22  ARG H  81  LYS H  82  THR H  83                    
-SITE     3 DC5 15 SER H  86  SER H 103  SER H 104  GLY H 153                    
-SITE     4 DC5 15 ALA H 154  TYR H 157  FOL H 703                               
-CRYST1   53.531  145.079  176.614  90.07  89.96  90.07 P 1           8          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.018681  0.000023 -0.000013        0.00000                         
-SCALE2      0.000000  0.006893  0.000008        0.00000                         
-SCALE3      0.000000  0.000000  0.005662        0.00000                         
-ATOM      1  N   PRO A   4     -11.403 -20.329  -4.088  1.00 43.98           N  
-ATOM      2  CA  PRO A   4     -11.222 -19.808  -5.450  1.00 45.73           C  
-ATOM      3  C   PRO A   4      -9.790 -20.006  -5.950  1.00 49.86           C  
-ATOM      4  O   PRO A   4      -8.892 -19.238  -5.597  1.00 55.73           O  
-ATOM      5  CB  PRO A   4     -11.562 -18.323  -5.304  1.00 44.44           C  
-ATOM      6  CG  PRO A   4     -11.232 -18.005  -3.879  1.00 59.29           C  
-ATOM      7  CD  PRO A   4     -11.513 -19.254  -3.085  1.00 38.71           C  
-ATOM      8  N   VAL A   5      -9.588 -21.032  -6.771  1.00 41.71           N  
-ATOM      9  CA  VAL A   5      -8.247 -21.419  -7.193  1.00 45.99           C  
-ATOM     10  C   VAL A   5      -7.977 -21.055  -8.658  1.00 41.43           C  
-ATOM     11  O   VAL A   5      -8.890 -21.027  -9.485  1.00 37.97           O  
-ATOM     12  CB  VAL A   5      -8.020 -22.943  -6.980  1.00 36.34           C  
-ATOM     13  CG1 VAL A   5      -8.767 -23.761  -8.017  1.00 32.45           C  
-ATOM     14  CG2 VAL A   5      -6.545 -23.280  -7.012  1.00 43.79           C  
-ATOM     15  N   CYS A   6      -6.720 -20.748  -8.967  1.00 31.26           N  
-ATOM     16  CA  CYS A   6      -6.304 -20.489 -10.343  1.00 31.40           C  
-ATOM     17  C   CYS A   6      -5.316 -21.546 -10.821  1.00 35.06           C  
-ATOM     18  O   CYS A   6      -4.373 -21.876 -10.117  1.00 41.66           O  
-ATOM     19  CB  CYS A   6      -5.678 -19.094 -10.468  1.00 38.13           C  
-ATOM     20  SG  CYS A   6      -6.851 -17.711 -10.438  1.00 53.70           S  
-ATOM     21  N   LEU A   7      -5.536 -22.074 -12.021  1.00 30.67           N  
-ATOM     22  CA  LEU A   7      -4.614 -23.042 -12.613  1.00 21.30           C  
-ATOM     23  C   LEU A   7      -3.561 -22.323 -13.447  1.00 26.31           C  
-ATOM     24  O   LEU A   7      -3.857 -21.304 -14.069  1.00 37.31           O  
-ATOM     25  CB  LEU A   7      -5.367 -24.050 -13.484  1.00 19.57           C  
-ATOM     26  CG  LEU A   7      -5.906 -25.337 -12.856  1.00 31.64           C  
-ATOM     27  CD1 LEU A   7      -6.764 -25.053 -11.633  1.00 39.17           C  
-ATOM     28  CD2 LEU A   7      -6.696 -26.139 -13.887  1.00 31.29           C  
-ATOM     29  N   VAL A   8      -2.333 -22.837 -13.460  1.00 22.50           N  
-ATOM     30  CA  VAL A   8      -1.312 -22.255 -14.338  1.00 22.68           C  
-ATOM     31  C   VAL A   8      -0.527 -23.330 -15.104  1.00 26.86           C  
-ATOM     32  O   VAL A   8       0.039 -24.250 -14.509  1.00 23.19           O  
-ATOM     33  CB  VAL A   8      -0.335 -21.349 -13.548  1.00  9.74           C  
-ATOM     34  CG1 VAL A   8      -0.006 -21.955 -12.201  1.00 27.72           C  
-ATOM     35  CG2 VAL A   8       0.929 -21.082 -14.357  1.00 15.80           C  
-ATOM     36  N   VAL A   9      -0.500 -23.201 -16.430  1.00 26.52           N  
-ATOM     37  CA  VAL A   9       0.041 -24.243 -17.304  1.00 20.14           C  
-ATOM     38  C   VAL A   9       0.835 -23.721 -18.497  1.00 19.86           C  
-ATOM     39  O   VAL A   9       0.685 -22.572 -18.910  1.00 25.46           O  
-ATOM     40  CB  VAL A   9      -1.082 -25.125 -17.880  1.00 22.23           C  
-ATOM     41  CG1 VAL A   9      -1.590 -26.096 -16.848  1.00 24.78           C  
-ATOM     42  CG2 VAL A   9      -2.213 -24.256 -18.398  1.00 21.67           C  
-ATOM     43  N   ALA A  10       1.674 -24.593 -19.046  1.00 18.06           N  
-ATOM     44  CA  ALA A  10       2.250 -24.407 -20.371  1.00 20.02           C  
-ATOM     45  C   ALA A  10       1.844 -25.628 -21.195  1.00 28.57           C  
-ATOM     46  O   ALA A  10       1.863 -26.751 -20.687  1.00 27.37           O  
-ATOM     47  CB  ALA A  10       3.757 -24.254 -20.302  1.00 21.29           C  
-ATOM     48  N   MET A  11       1.472 -25.420 -22.455  1.00 27.87           N  
-ATOM     49  CA  MET A  11       0.715 -26.441 -23.173  1.00 18.47           C  
-ATOM     50  C   MET A  11       0.938 -26.461 -24.689  1.00 28.20           C  
-ATOM     51  O   MET A  11       0.988 -25.414 -25.339  1.00 31.70           O  
-ATOM     52  CB  MET A  11      -0.771 -26.238 -22.882  1.00 16.14           C  
-ATOM     53  CG  MET A  11      -1.629 -27.463 -23.046  1.00 21.95           C  
-ATOM     54  SD  MET A  11      -3.362 -27.064 -22.759  1.00 21.03           S  
-ATOM     55  CE  MET A  11      -3.278 -26.317 -21.136  1.00 13.54           C  
-ATOM     56  N   THR A  12       1.064 -27.662 -25.246  1.00 25.38           N  
-ATOM     57  CA  THR A  12       1.157 -27.844 -26.693  1.00 22.96           C  
-ATOM     58  C   THR A  12      -0.260 -27.834 -27.281  1.00 26.75           C  
-ATOM     59  O   THR A  12      -1.230 -27.962 -26.532  1.00 25.22           O  
-ATOM     60  CB  THR A  12       1.888 -29.157 -27.046  1.00 19.13           C  
-ATOM     61  OG1 THR A  12       1.120 -30.274 -26.588  1.00 22.02           O  
-ATOM     62  CG2 THR A  12       3.264 -29.192 -26.396  1.00 16.91           C  
-ATOM     63  N   PRO A  13      -0.396 -27.658 -28.613  1.00 24.92           N  
-ATOM     64  CA  PRO A  13      -1.745 -27.619 -29.197  1.00 21.14           C  
-ATOM     65  C   PRO A  13      -2.560 -28.880 -28.935  1.00 20.73           C  
-ATOM     66  O   PRO A  13      -3.784 -28.809 -28.840  1.00 23.24           O  
-ATOM     67  CB  PRO A  13      -1.473 -27.460 -30.694  1.00 20.43           C  
-ATOM     68  CG  PRO A  13      -0.166 -26.777 -30.757  1.00 26.94           C  
-ATOM     69  CD  PRO A  13       0.634 -27.344 -29.620  1.00 21.33           C  
-ATOM     70  N   LYS A  14      -1.887 -30.018 -28.817  1.00 19.66           N  
-ATOM     71  CA  LYS A  14      -2.564 -31.270 -28.506  1.00 21.04           C  
-ATOM     72  C   LYS A  14      -2.557 -31.524 -26.998  1.00 25.15           C  
-ATOM     73  O   LYS A  14      -2.611 -32.670 -26.547  1.00 24.40           O  
-ATOM     74  CB  LYS A  14      -1.918 -32.426 -29.274  1.00 11.89           C  
-ATOM     75  CG  LYS A  14      -2.365 -32.479 -30.732  1.00 24.61           C  
-ATOM     76  CD  LYS A  14      -1.287 -33.014 -31.666  1.00 35.25           C  
-ATOM     77  CE  LYS A  14      -1.190 -34.531 -31.625  1.00 35.97           C  
-ATOM     78  NZ  LYS A  14      -0.238 -35.040 -32.652  1.00 30.69           N  
-ATOM     79  N   ARG A  15      -2.481 -30.429 -26.241  1.00 20.31           N  
-ATOM     80  CA  ARG A  15      -2.639 -30.416 -24.785  1.00 15.73           C  
-ATOM     81  C   ARG A  15      -1.547 -31.152 -24.012  1.00 17.50           C  
-ATOM     82  O   ARG A  15      -1.732 -31.486 -22.843  1.00 16.76           O  
-ATOM     83  CB  ARG A  15      -4.009 -30.985 -24.398  1.00 16.18           C  
-ATOM     84  CG  ARG A  15      -5.154 -30.022 -24.644  1.00 17.70           C  
-ATOM     85  CD  ARG A  15      -6.485 -30.562 -24.138  1.00 23.76           C  
-ATOM     86  NE  ARG A  15      -7.033 -31.605 -25.002  1.00 19.85           N  
-ATOM     87  CZ  ARG A  15      -7.078 -32.895 -24.685  1.00 21.64           C  
-ATOM     88  NH1 ARG A  15      -7.595 -33.770 -25.538  1.00 32.85           N  
-ATOM     89  NH2 ARG A  15      -6.614 -33.314 -23.516  1.00 19.61           N  
-ATOM     90  N   GLY A  16      -0.407 -31.384 -24.654  1.00 18.04           N  
-ATOM     91  CA  GLY A  16       0.712 -32.035 -23.995  1.00 17.76           C  
-ATOM     92  C   GLY A  16       1.434 -31.095 -23.051  1.00 18.86           C  
-ATOM     93  O   GLY A  16       1.619 -29.918 -23.362  1.00 21.69           O  
-ATOM     94  N   ILE A  17       1.844 -31.607 -21.894  1.00 15.32           N  
-ATOM     95  CA  ILE A  17       2.511 -30.770 -20.900  1.00 18.63           C  
-ATOM     96  C   ILE A  17       3.834 -31.350 -20.405  1.00 23.66           C  
-ATOM     97  O   ILE A  17       4.642 -30.631 -19.813  1.00 19.64           O  
-ATOM     98  CB  ILE A  17       1.613 -30.522 -19.672  1.00 18.04           C  
-ATOM     99  CG1 ILE A  17       1.380 -31.824 -18.907  1.00 16.79           C  
-ATOM    100  CG2 ILE A  17       0.291 -29.879 -20.081  1.00 18.47           C  
-ATOM    101  CD1 ILE A  17       0.616 -31.633 -17.618  1.00 20.06           C  
-ATOM    102  N   GLY A  18       4.061 -32.640 -20.641  1.00 28.55           N  
-ATOM    103  CA  GLY A  18       5.271 -33.277 -20.149  1.00 27.73           C  
-ATOM    104  C   GLY A  18       5.683 -34.578 -20.813  1.00 22.88           C  
-ATOM    105  O   GLY A  18       4.876 -35.242 -21.467  1.00 21.31           O  
-ATOM    106  N   ILE A  19       6.953 -34.937 -20.639  1.00 23.02           N  
-ATOM    107  CA  ILE A  19       7.471 -36.222 -21.098  1.00 22.28           C  
-ATOM    108  C   ILE A  19       8.638 -36.677 -20.216  1.00 25.30           C  
-ATOM    109  O   ILE A  19       9.530 -35.887 -19.896  1.00 33.46           O  
-ATOM    110  CB  ILE A  19       7.913 -36.161 -22.578  1.00 14.24           C  
-ATOM    111  CG1 ILE A  19       8.382 -37.535 -23.053  1.00 13.89           C  
-ATOM    112  CG2 ILE A  19       8.994 -35.112 -22.787  1.00 14.65           C  
-ATOM    113  CD1 ILE A  19       7.806 -37.935 -24.383  1.00 22.13           C  
-ATOM    114  N   ASN A  20       8.610 -37.947 -19.814  1.00 19.39           N  
-ATOM    115  CA  ASN A  20       9.616 -38.521 -18.918  1.00 21.80           C  
-ATOM    116  C   ASN A  20       9.855 -37.672 -17.677  1.00 20.72           C  
-ATOM    117  O   ASN A  20      10.998 -37.364 -17.338  1.00 20.56           O  
-ATOM    118  CB  ASN A  20      10.941 -38.732 -19.655  1.00 16.61           C  
-ATOM    119  CG  ASN A  20      10.968 -40.024 -20.445  1.00 39.91           C  
-ATOM    120  OD1 ASN A  20      10.369 -41.024 -20.047  1.00 48.96           O  
-ATOM    121  ND2 ASN A  20      11.665 -40.009 -21.574  1.00 55.93           N  
-ATOM    122  N   ASN A  21       8.764 -37.296 -17.017  1.00 22.92           N  
-ATOM    123  CA  ASN A  21       8.811 -36.479 -15.809  1.00 23.63           C  
-ATOM    124  C   ASN A  21       9.620 -35.200 -16.009  1.00 21.57           C  
-ATOM    125  O   ASN A  21      10.309 -34.738 -15.101  1.00 31.58           O  
-ATOM    126  CB  ASN A  21       9.384 -37.285 -14.644  1.00 24.58           C  
-ATOM    127  CG  ASN A  21       8.802 -36.869 -13.309  1.00 38.42           C  
-ATOM    128  OD1 ASN A  21       7.646 -36.451 -13.228  1.00 31.55           O  
-ATOM    129  ND2 ASN A  21       9.601 -36.980 -12.252  1.00 47.02           N  
-ATOM    130  N   GLY A  22       9.535 -34.638 -17.210  1.00 19.05           N  
-ATOM    131  CA  GLY A  22      10.226 -33.405 -17.533  1.00 19.95           C  
-ATOM    132  C   GLY A  22       9.420 -32.602 -18.530  1.00 18.92           C  
-ATOM    133  O   GLY A  22       8.317 -33.000 -18.901  1.00 22.09           O  
-ATOM    134  N   LEU A  23       9.961 -31.469 -18.963  1.00 17.03           N  
-ATOM    135  CA  LEU A  23       9.272 -30.634 -19.938  1.00 17.39           C  
-ATOM    136  C   LEU A  23       9.580 -31.090 -21.362  1.00 16.29           C  
-ATOM    137  O   LEU A  23      10.703 -31.494 -21.661  1.00 15.11           O  
-ATOM    138  CB  LEU A  23       9.652 -29.164 -19.753  1.00 21.39           C  
-ATOM    139  CG  LEU A  23       9.256 -28.541 -18.414  1.00 15.21           C  
-ATOM    140  CD1 LEU A  23       9.536 -27.045 -18.409  1.00 21.27           C  
-ATOM    141  CD2 LEU A  23       7.795 -28.820 -18.107  1.00 24.46           C  
-ATOM    142  N   PRO A  24       8.572 -31.026 -22.244  1.00 18.68           N  
-ATOM    143  CA  PRO A  24       8.670 -31.494 -23.631  1.00 17.24           C  
-ATOM    144  C   PRO A  24       9.531 -30.603 -24.519  1.00 19.39           C  
-ATOM    145  O   PRO A  24      10.007 -31.060 -25.557  1.00 27.21           O  
-ATOM    146  CB  PRO A  24       7.212 -31.469 -24.115  1.00 18.27           C  
-ATOM    147  CG  PRO A  24       6.378 -31.317 -22.884  1.00 12.78           C  
-ATOM    148  CD  PRO A  24       7.215 -30.557 -21.926  1.00 16.41           C  
-ATOM    149  N   TRP A  25       9.723 -29.353 -24.113  1.00 19.00           N  
-ATOM    150  CA  TRP A  25      10.383 -28.353 -24.947  1.00 19.34           C  
-ATOM    151  C   TRP A  25      11.676 -27.838 -24.315  1.00 26.05           C  
-ATOM    152  O   TRP A  25      11.912 -28.052 -23.124  1.00 25.05           O  
-ATOM    153  CB  TRP A  25       9.425 -27.187 -25.198  1.00 15.79           C  
-ATOM    154  CG  TRP A  25       8.727 -26.758 -23.953  1.00 17.34           C  
-ATOM    155  CD1 TRP A  25       9.242 -26.000 -22.944  1.00 16.09           C  
-ATOM    156  CD2 TRP A  25       7.386 -27.079 -23.570  1.00 19.21           C  
-ATOM    157  NE1 TRP A  25       8.303 -25.824 -21.957  1.00 15.34           N  
-ATOM    158  CE2 TRP A  25       7.154 -26.476 -22.319  1.00 15.31           C  
-ATOM    159  CE3 TRP A  25       6.356 -27.814 -24.167  1.00 19.10           C  
-ATOM    160  CZ2 TRP A  25       5.937 -26.586 -21.654  1.00 15.12           C  
-ATOM    161  CZ3 TRP A  25       5.147 -27.921 -23.504  1.00 16.34           C  
-ATOM    162  CH2 TRP A  25       4.948 -27.309 -22.261  1.00 16.66           C  
-ATOM    163  N   PRO A  26      12.524 -27.162 -25.112  1.00 20.66           N  
-ATOM    164  CA  PRO A  26      13.671 -26.436 -24.552  1.00 20.87           C  
-ATOM    165  C   PRO A  26      13.226 -25.334 -23.588  1.00 33.94           C  
-ATOM    166  O   PRO A  26      12.035 -25.023 -23.517  1.00 37.35           O  
-ATOM    167  CB  PRO A  26      14.359 -25.851 -25.787  1.00 20.12           C  
-ATOM    168  CG  PRO A  26      13.344 -25.934 -26.885  1.00 18.92           C  
-ATOM    169  CD  PRO A  26      12.538 -27.148 -26.584  1.00 17.24           C  
-ATOM    170  N  AHIS A  27      14.170 -24.755 -22.854  0.31 49.36           N  
-ATOM    171  N  BHIS A  27      14.177 -24.755 -22.862  0.69 48.80           N  
-ATOM    172  CA AHIS A  27      13.830 -23.806 -21.798  0.31 42.72           C  
-ATOM    173  CA BHIS A  27      13.873 -23.765 -21.831  0.69 44.16           C  
-ATOM    174  C  AHIS A  27      13.204 -22.533 -22.366  0.31 45.64           C  
-ATOM    175  C  BHIS A  27      13.186 -22.533 -22.409  0.69 48.02           C  
-ATOM    176  O  AHIS A  27      13.774 -21.874 -23.237  0.31 36.31           O  
-ATOM    177  O  BHIS A  27      13.709 -21.891 -23.321  0.69 35.97           O  
-ATOM    178  CB AHIS A  27      15.067 -23.472 -20.950  0.31 37.93           C  
-ATOM    179  CB BHIS A  27      15.151 -23.351 -21.097  0.69 37.34           C  
-ATOM    180  CG AHIS A  27      16.101 -22.662 -21.666  0.31 42.90           C  
-ATOM    181  CG BHIS A  27      14.903 -22.571 -19.844  0.69 30.56           C  
-ATOM    182  ND1AHIS A  27      16.239 -21.304 -21.481  0.31 42.16           N  
-ATOM    183  ND1BHIS A  27      14.664 -23.176 -18.629  0.69 29.59           N  
-ATOM    184  CD2AHIS A  27      17.048 -23.017 -22.567  0.31 43.38           C  
-ATOM    185  CD2BHIS A  27      14.852 -21.238 -19.617  0.69 31.72           C  
-ATOM    186  CE1AHIS A  27      17.226 -20.856 -22.236  0.31 38.89           C  
-ATOM    187  CE1BHIS A  27      14.480 -22.248 -17.707  0.69 34.38           C  
-ATOM    188  NE2AHIS A  27      17.733 -21.876 -22.906  0.31 38.21           N  
-ATOM    189  NE2BHIS A  27      14.588 -21.063 -18.280  0.69 31.49           N  
-ATOM    190  N   LEU A  28      12.011 -22.212 -21.876  1.00 35.20           N  
-ATOM    191  CA  LEU A  28      11.293 -21.016 -22.292  1.00 29.34           C  
-ATOM    192  C   LEU A  28      11.390 -19.971 -21.190  1.00 31.66           C  
-ATOM    193  O   LEU A  28      10.552 -19.907 -20.287  1.00 42.41           O  
-ATOM    194  CB  LEU A  28       9.834 -21.334 -22.614  1.00 26.26           C  
-ATOM    195  CG  LEU A  28       9.591 -22.481 -23.599  1.00 33.23           C  
-ATOM    196  CD1 LEU A  28       8.107 -22.604 -23.923  1.00 23.05           C  
-ATOM    197  CD2 LEU A  28      10.413 -22.300 -24.868  1.00 27.12           C  
-ATOM    198  N   THR A  29      12.430 -19.153 -21.279  1.00 31.13           N  
-ATOM    199  CA  THR A  29      12.778 -18.210 -20.228  1.00 39.32           C  
-ATOM    200  C   THR A  29      11.657 -17.216 -19.906  1.00 33.41           C  
-ATOM    201  O   THR A  29      11.407 -16.917 -18.737  1.00 31.82           O  
-ATOM    202  CB  THR A  29      14.059 -17.432 -20.595  1.00 27.83           C  
-ATOM    203  OG1 THR A  29      14.302 -16.417 -19.614  1.00 35.98           O  
-ATOM    204  CG2 THR A  29      13.938 -16.792 -21.972  1.00 30.90           C  
-ATOM    205  N   THR A  30      10.973 -16.717 -20.931  1.00 20.93           N  
-ATOM    206  CA  THR A  30       9.909 -15.748 -20.713  1.00 21.71           C  
-ATOM    207  C   THR A  30       8.709 -16.431 -20.078  1.00 27.16           C  
-ATOM    208  O   THR A  30       7.982 -15.828 -19.290  1.00 31.66           O  
-ATOM    209  CB  THR A  30       9.492 -15.065 -22.020  1.00 20.16           C  
-ATOM    210  OG1 THR A  30      10.653 -14.545 -22.680  1.00 28.60           O  
-ATOM    211  CG2 THR A  30       8.524 -13.927 -21.743  1.00 26.77           C  
-ATOM    212  N   ASP A  31       8.508 -17.698 -20.420  1.00 27.07           N  
-ATOM    213  CA  ASP A  31       7.453 -18.482 -19.796  1.00 26.94           C  
-ATOM    214  C   ASP A  31       7.753 -18.682 -18.318  1.00 28.64           C  
-ATOM    215  O   ASP A  31       6.856 -18.602 -17.480  1.00 31.53           O  
-ATOM    216  CB  ASP A  31       7.293 -19.836 -20.482  1.00 27.97           C  
-ATOM    217  CG  ASP A  31       6.366 -20.765 -19.723  1.00 33.91           C  
-ATOM    218  OD1 ASP A  31       5.216 -20.366 -19.438  1.00 24.57           O  
-ATOM    219  OD2 ASP A  31       6.801 -21.888 -19.393  1.00 30.08           O  
-ATOM    220  N   PHE A  32       9.018 -18.941 -18.000  1.00 28.42           N  
-ATOM    221  CA  PHE A  32       9.415 -19.107 -16.607  1.00 34.58           C  
-ATOM    222  C   PHE A  32       9.245 -17.805 -15.832  1.00 33.73           C  
-ATOM    223  O   PHE A  32       8.767 -17.809 -14.695  1.00 31.04           O  
-ATOM    224  CB  PHE A  32      10.857 -19.607 -16.512  1.00 38.64           C  
-ATOM    225  CG  PHE A  32      10.967 -21.102 -16.447  1.00 32.08           C  
-ATOM    226  CD1 PHE A  32      10.857 -21.867 -17.595  1.00 47.44           C  
-ATOM    227  CD2 PHE A  32      11.167 -21.745 -15.237  1.00 36.44           C  
-ATOM    228  CE1 PHE A  32      10.950 -23.247 -17.541  1.00 52.04           C  
-ATOM    229  CE2 PHE A  32      11.261 -23.124 -15.175  1.00 44.07           C  
-ATOM    230  CZ  PHE A  32      11.152 -23.876 -16.329  1.00 43.39           C  
-ATOM    231  N   LYS A  33       9.632 -16.696 -16.455  1.00 31.02           N  
-ATOM    232  CA  LYS A  33       9.451 -15.379 -15.855  1.00 36.29           C  
-ATOM    233  C   LYS A  33       7.973 -15.144 -15.562  1.00 32.04           C  
-ATOM    234  O   LYS A  33       7.603 -14.698 -14.471  1.00 38.32           O  
-ATOM    235  CB  LYS A  33      10.001 -14.284 -16.776  1.00 28.64           C  
-ATOM    236  CG  LYS A  33       9.988 -12.896 -16.158  1.00 30.16           C  
-ATOM    237  CD  LYS A  33      10.912 -11.934 -16.893  1.00 32.32           C  
-ATOM    238  CE  LYS A  33      10.359 -11.541 -18.253  1.00 42.48           C  
-ATOM    239  NZ  LYS A  33      11.188 -10.482 -18.900  1.00 42.51           N  
-ATOM    240  N   HIS A  34       7.138 -15.466 -16.544  1.00 27.66           N  
-ATOM    241  CA  HIS A  34       5.690 -15.390 -16.398  1.00 34.10           C  
-ATOM    242  C   HIS A  34       5.218 -16.183 -15.186  1.00 28.78           C  
-ATOM    243  O   HIS A  34       4.519 -15.650 -14.330  1.00 27.51           O  
-ATOM    244  CB  HIS A  34       4.993 -15.904 -17.663  1.00 31.57           C  
-ATOM    245  CG  HIS A  34       3.540 -16.210 -17.470  1.00 28.45           C  
-ATOM    246  ND1 HIS A  34       2.556 -15.252 -17.572  1.00 32.48           N  
-ATOM    247  CD2 HIS A  34       2.905 -17.371 -17.174  1.00 28.67           C  
-ATOM    248  CE1 HIS A  34       1.377 -15.808 -17.352  1.00 26.32           C  
-ATOM    249  NE2 HIS A  34       1.563 -17.092 -17.107  1.00 24.12           N  
-ATOM    250  N   PHE A  35       5.614 -17.452 -15.122  1.00 29.14           N  
-ATOM    251  CA  PHE A  35       5.220 -18.339 -14.030  1.00 28.45           C  
-ATOM    252  C   PHE A  35       5.600 -17.760 -12.668  1.00 35.13           C  
-ATOM    253  O   PHE A  35       4.766 -17.685 -11.759  1.00 36.72           O  
-ATOM    254  CB  PHE A  35       5.855 -19.722 -14.214  1.00 25.64           C  
-ATOM    255  CG  PHE A  35       5.627 -20.655 -13.059  1.00 24.90           C  
-ATOM    256  CD1 PHE A  35       4.437 -21.352 -12.937  1.00 29.09           C  
-ATOM    257  CD2 PHE A  35       6.607 -20.840 -12.098  1.00 30.94           C  
-ATOM    258  CE1 PHE A  35       4.225 -22.213 -11.874  1.00 32.59           C  
-ATOM    259  CE2 PHE A  35       6.402 -21.699 -11.031  1.00 33.43           C  
-ATOM    260  CZ  PHE A  35       5.209 -22.387 -10.920  1.00 29.03           C  
-ATOM    261  N   SER A  36       6.859 -17.347 -12.539  1.00 35.90           N  
-ATOM    262  CA  SER A  36       7.348 -16.754 -11.300  1.00 29.83           C  
-ATOM    263  C   SER A  36       6.531 -15.532 -10.899  1.00 39.95           C  
-ATOM    264  O   SER A  36       6.031 -15.452  -9.774  1.00 43.48           O  
-ATOM    265  CB  SER A  36       8.818 -16.361 -11.432  1.00 41.42           C  
-ATOM    266  OG  SER A  36       9.258 -15.694 -10.261  1.00 48.67           O  
-ATOM    267  N   ARG A  37       6.387 -14.588 -11.824  1.00 36.60           N  
-ATOM    268  CA  ARG A  37       5.699 -13.340 -11.512  1.00 37.76           C  
-ATOM    269  C   ARG A  37       4.218 -13.543 -11.201  1.00 34.80           C  
-ATOM    270  O   ARG A  37       3.635 -12.788 -10.428  1.00 42.17           O  
-ATOM    271  CB  ARG A  37       5.846 -12.346 -12.660  1.00 41.50           C  
-ATOM    272  CG  ARG A  37       5.850 -10.903 -12.193  1.00 47.16           C  
-ATOM    273  CD  ARG A  37       7.225 -10.291 -12.376  1.00 57.78           C  
-ATOM    274  NE  ARG A  37       8.288 -11.207 -11.971  1.00 66.36           N  
-ATOM    275  CZ  ARG A  37       9.570 -11.051 -12.287  1.00 65.10           C  
-ATOM    276  NH1 ARG A  37      10.467 -11.937 -11.874  1.00 67.14           N  
-ATOM    277  NH2 ARG A  37       9.957 -10.014 -13.019  1.00 41.70           N  
-ATOM    278  N   VAL A  38       3.609 -14.556 -11.806  1.00 28.76           N  
-ATOM    279  CA  VAL A  38       2.198 -14.829 -11.567  1.00 32.54           C  
-ATOM    280  C   VAL A  38       1.997 -15.521 -10.223  1.00 33.55           C  
-ATOM    281  O   VAL A  38       1.068 -15.198  -9.483  1.00 30.24           O  
-ATOM    282  CB  VAL A  38       1.589 -15.689 -12.694  1.00 29.56           C  
-ATOM    283  CG1 VAL A  38       0.210 -16.200 -12.301  1.00 18.08           C  
-ATOM    284  CG2 VAL A  38       1.511 -14.887 -13.981  1.00 31.73           C  
-ATOM    285  N   THR A  39       2.881 -16.458  -9.895  1.00 32.21           N  
-ATOM    286  CA  THR A  39       2.725 -17.225  -8.663  1.00 34.67           C  
-ATOM    287  C   THR A  39       3.257 -16.506  -7.417  1.00 37.25           C  
-ATOM    288  O   THR A  39       2.898 -16.873  -6.298  1.00 36.83           O  
-ATOM    289  CB  THR A  39       3.412 -18.604  -8.759  1.00 27.97           C  
-ATOM    290  OG1 THR A  39       4.690 -18.470  -9.393  1.00 35.38           O  
-ATOM    291  CG2 THR A  39       2.557 -19.576  -9.564  1.00 20.59           C  
-ATOM    292  N   LYS A  40       4.098 -15.487  -7.591  1.00 37.54           N  
-ATOM    293  CA  LYS A  40       4.701 -14.832  -6.426  1.00 36.41           C  
-ATOM    294  C   LYS A  40       4.047 -13.512  -6.005  1.00 42.92           C  
-ATOM    295  O   LYS A  40       3.845 -13.278  -4.814  1.00 49.48           O  
-ATOM    296  CB  LYS A  40       6.191 -14.589  -6.671  1.00 31.42           C  
-ATOM    297  CG  LYS A  40       7.043 -15.831  -6.496  1.00 33.41           C  
-ATOM    298  CD  LYS A  40       8.477 -15.499  -6.118  1.00 34.62           C  
-ATOM    299  CE  LYS A  40       9.169 -14.700  -7.204  1.00 36.78           C  
-ATOM    300  NZ  LYS A  40      10.613 -14.501  -6.900  1.00 49.94           N  
-ATOM    301  N   THR A  41       3.723 -12.656  -6.970  1.00 37.89           N  
-ATOM    302  CA  THR A  41       3.334 -11.276  -6.670  1.00 44.30           C  
-ATOM    303  C   THR A  41       2.076 -11.132  -5.814  1.00 49.79           C  
-ATOM    304  O   THR A  41       0.989 -11.572  -6.190  1.00 42.44           O  
-ATOM    305  CB  THR A  41       3.122 -10.468  -7.958  1.00 51.33           C  
-ATOM    306  OG1 THR A  41       2.230 -11.176  -8.828  1.00 51.63           O  
-ATOM    307  CG2 THR A  41       4.450 -10.242  -8.665  1.00 43.58           C  
-ATOM    308  N   THR A  42       2.252 -10.492  -4.662  1.00 56.12           N  
-ATOM    309  CA  THR A  42       1.167 -10.184  -3.741  1.00 62.29           C  
-ATOM    310  C   THR A  42       1.143  -8.673  -3.532  1.00 70.65           C  
-ATOM    311  O   THR A  42       2.202  -8.045  -3.486  1.00 66.23           O  
-ATOM    312  CB  THR A  42       1.353 -10.911  -2.387  1.00 68.52           C  
-ATOM    313  OG1 THR A  42       1.696 -12.283  -2.618  1.00 57.70           O  
-ATOM    314  CG2 THR A  42       0.089 -10.846  -1.541  1.00 76.31           C  
-ATOM    315  N   PRO A  43      -0.059  -8.075  -3.432  1.00 77.67           N  
-ATOM    316  CA  PRO A  43      -0.150  -6.640  -3.133  1.00 83.76           C  
-ATOM    317  C   PRO A  43       0.580  -6.248  -1.849  1.00 78.30           C  
-ATOM    318  O   PRO A  43       0.466  -6.964  -0.854  1.00 68.92           O  
-ATOM    319  CB  PRO A  43      -1.663  -6.401  -2.989  1.00 80.91           C  
-ATOM    320  CG  PRO A  43      -2.284  -7.772  -2.899  1.00 77.47           C  
-ATOM    321  CD  PRO A  43      -1.386  -8.650  -3.706  1.00 72.17           C  
-ATOM    322  N   ALA A  46       2.302  -7.958   1.117  1.00 69.59           N  
-ATOM    323  CA  ALA A  46       2.529  -7.215   2.351  1.00 85.36           C  
-ATOM    324  C   ALA A  46       2.593  -8.155   3.548  1.00 78.54           C  
-ATOM    325  O   ALA A  46       3.669  -8.437   4.080  1.00 56.93           O  
-ATOM    326  CB  ALA A  46       1.436  -6.175   2.554  1.00 71.03           C  
-ATOM    327  N   SER A  47       1.428  -8.637   3.964  1.00 74.60           N  
-ATOM    328  CA  SER A  47       1.332  -9.552   5.092  1.00 74.60           C  
-ATOM    329  C   SER A  47       1.281 -11.003   4.625  1.00 72.70           C  
-ATOM    330  O   SER A  47       1.883 -11.887   5.239  1.00 45.64           O  
-ATOM    331  CB  SER A  47       0.094  -9.232   5.933  1.00 78.79           C  
-ATOM    332  OG  SER A  47      -1.092  -9.329   5.159  1.00 70.28           O  
-ATOM    333  N   ARG A  48       0.569 -11.239   3.527  1.00 75.03           N  
-ATOM    334  CA  ARG A  48       0.300 -12.595   3.064  1.00 57.53           C  
-ATOM    335  C   ARG A  48       1.208 -13.019   1.915  1.00 56.18           C  
-ATOM    336  O   ARG A  48       1.876 -12.193   1.291  1.00 60.17           O  
-ATOM    337  CB  ARG A  48      -1.162 -12.716   2.633  1.00 51.30           C  
-ATOM    338  CG  ARG A  48      -2.135 -12.013   3.566  1.00 58.74           C  
-ATOM    339  CD  ARG A  48      -3.489 -11.818   2.907  1.00 59.09           C  
-ATOM    340  NE  ARG A  48      -4.284 -13.041   2.911  1.00 63.71           N  
-ATOM    341  CZ  ARG A  48      -5.323 -13.251   3.714  1.00 62.95           C  
-ATOM    342  NH1 ARG A  48      -5.697 -12.312   4.572  1.00 55.11           N  
-ATOM    343  NH2 ARG A  48      -5.992 -14.396   3.654  1.00 61.63           N  
-ATOM    344  N   PHE A  74       1.220 -14.320   1.649  1.00 50.63           N  
-ATOM    345  CA  PHE A  74       1.941 -14.879   0.514  1.00 54.13           C  
-ATOM    346  C   PHE A  74       1.002 -15.772  -0.285  1.00 53.66           C  
-ATOM    347  O   PHE A  74      -0.119 -16.041   0.144  1.00 49.80           O  
-ATOM    348  CB  PHE A  74       3.165 -15.667   0.982  1.00 45.03           C  
-ATOM    349  CG  PHE A  74       2.913 -16.508   2.201  1.00 44.07           C  
-ATOM    350  CD1 PHE A  74       2.237 -17.713   2.104  1.00 37.83           C  
-ATOM    351  CD2 PHE A  74       3.356 -16.095   3.445  1.00 51.01           C  
-ATOM    352  CE1 PHE A  74       2.006 -18.485   3.224  1.00 37.59           C  
-ATOM    353  CE2 PHE A  74       3.128 -16.864   4.568  1.00 42.07           C  
-ATOM    354  CZ  PHE A  74       2.452 -18.060   4.457  1.00 40.32           C  
-ATOM    355  N   ASN A  75       1.453 -16.232  -1.446  1.00 42.28           N  
-ATOM    356  CA  ASN A  75       0.635 -17.119  -2.264  1.00 41.34           C  
-ATOM    357  C   ASN A  75       0.984 -18.587  -2.045  1.00 39.97           C  
-ATOM    358  O   ASN A  75       2.084 -18.919  -1.594  1.00 41.32           O  
-ATOM    359  CB  ASN A  75       0.779 -16.761  -3.742  1.00 40.97           C  
-ATOM    360  CG  ASN A  75       0.093 -15.458  -4.090  1.00 40.12           C  
-ATOM    361  OD1 ASN A  75      -1.012 -15.181  -3.621  1.00 43.62           O  
-ATOM    362  ND2 ASN A  75       0.745 -14.648  -4.913  1.00 46.97           N  
-ATOM    363  N   ALA A  76       0.043 -19.469  -2.359  1.00 33.37           N  
-ATOM    364  CA  ALA A  76       0.291 -20.895  -2.203  1.00 30.70           C  
-ATOM    365  C   ALA A  76       0.297 -21.592  -3.555  1.00 32.68           C  
-ATOM    366  O   ALA A  76      -0.540 -21.315  -4.407  1.00 31.76           O  
-ATOM    367  CB  ALA A  76      -0.749 -21.521  -1.286  1.00 33.24           C  
-ATOM    368  N   VAL A  77       1.256 -22.488  -3.752  1.00 36.21           N  
-ATOM    369  CA  VAL A  77       1.299 -23.307  -4.951  1.00 26.66           C  
-ATOM    370  C   VAL A  77       1.120 -24.779  -4.587  1.00 32.96           C  
-ATOM    371  O   VAL A  77       1.816 -25.318  -3.718  1.00 38.93           O  
-ATOM    372  CB  VAL A  77       2.616 -23.106  -5.732  1.00 17.36           C  
-ATOM    373  CG1 VAL A  77       2.610 -21.760  -6.435  1.00 25.86           C  
-ATOM    374  CG2 VAL A  77       3.814 -23.219  -4.807  1.00 23.89           C  
-ATOM    375  N   VAL A  78       0.158 -25.416  -5.244  1.00 26.50           N  
-ATOM    376  CA  VAL A  78      -0.129 -26.822  -5.003  1.00 30.23           C  
-ATOM    377  C   VAL A  78       0.261 -27.651  -6.224  1.00 35.60           C  
-ATOM    378  O   VAL A  78      -0.165 -27.366  -7.351  1.00 32.48           O  
-ATOM    379  CB  VAL A  78      -1.614 -27.050  -4.666  1.00 21.35           C  
-ATOM    380  CG1 VAL A  78      -1.873 -28.519  -4.373  1.00 15.72           C  
-ATOM    381  CG2 VAL A  78      -2.024 -26.191  -3.480  1.00 15.31           C  
-ATOM    382  N   MET A  79       1.088 -28.667  -5.991  1.00 36.31           N  
-ATOM    383  CA  MET A  79       1.585 -29.513  -7.065  1.00 24.93           C  
-ATOM    384  C   MET A  79       1.479 -30.989  -6.707  1.00 25.80           C  
-ATOM    385  O   MET A  79       1.347 -31.346  -5.538  1.00 25.47           O  
-ATOM    386  CB  MET A  79       3.035 -29.161  -7.390  1.00 25.36           C  
-ATOM    387  CG  MET A  79       4.031 -29.624  -6.343  1.00 23.75           C  
-ATOM    388  SD  MET A  79       5.594 -28.740  -6.457  1.00 30.86           S  
-ATOM    389  CE  MET A  79       5.071 -27.100  -5.963  1.00 27.13           C  
-ATOM    390  N   GLY A  80       1.531 -31.841  -7.725  1.00 29.26           N  
-ATOM    391  CA  GLY A  80       1.565 -33.275  -7.514  1.00 26.83           C  
-ATOM    392  C   GLY A  80       2.973 -33.721  -7.170  1.00 32.76           C  
-ATOM    393  O   GLY A  80       3.920 -32.939  -7.281  1.00 33.32           O  
-ATOM    394  N   ARG A  81       3.115 -34.974  -6.754  1.00 25.34           N  
-ATOM    395  CA  ARG A  81       4.413 -35.493  -6.341  1.00 27.82           C  
-ATOM    396  C   ARG A  81       5.425 -35.484  -7.485  1.00 28.36           C  
-ATOM    397  O   ARG A  81       6.580 -35.080  -7.310  1.00 36.68           O  
-ATOM    398  CB  ARG A  81       4.254 -36.908  -5.781  1.00 24.47           C  
-ATOM    399  CG  ARG A  81       5.535 -37.513  -5.240  1.00 29.18           C  
-ATOM    400  CD  ARG A  81       6.075 -38.585  -6.168  1.00 29.09           C  
-ATOM    401  NE  ARG A  81       5.145 -39.698  -6.316  1.00 29.36           N  
-ATOM    402  CZ  ARG A  81       5.282 -40.672  -7.209  1.00 31.95           C  
-ATOM    403  NH1 ARG A  81       4.384 -41.646  -7.272  1.00 41.89           N  
-ATOM    404  NH2 ARG A  81       6.314 -40.672  -8.042  1.00 23.89           N  
-ATOM    405  N   LYS A  82       4.979 -35.925  -8.656  1.00 29.69           N  
-ATOM    406  CA  LYS A  82       5.858 -36.056  -9.814  1.00 30.83           C  
-ATOM    407  C   LYS A  82       6.351 -34.705 -10.314  1.00 32.36           C  
-ATOM    408  O   LYS A  82       7.431 -34.611 -10.895  1.00 34.60           O  
-ATOM    409  CB  LYS A  82       5.153 -36.802 -10.949  1.00 30.28           C  
-ATOM    410  CG  LYS A  82       4.834 -38.249 -10.617  1.00 27.50           C  
-ATOM    411  CD  LYS A  82       4.309 -39.003 -11.827  1.00 34.63           C  
-ATOM    412  CE  LYS A  82       4.067 -40.465 -11.488  1.00 37.23           C  
-ATOM    413  NZ  LYS A  82       3.711 -41.265 -12.692  1.00 26.13           N  
-ATOM    414  N   THR A  83       5.560 -33.660 -10.096  1.00 30.89           N  
-ATOM    415  CA  THR A  83       5.960 -32.318 -10.500  1.00 25.77           C  
-ATOM    416  C   THR A  83       7.101 -31.839  -9.605  1.00 35.03           C  
-ATOM    417  O   THR A  83       8.132 -31.347 -10.080  1.00 39.64           O  
-ATOM    418  CB  THR A  83       4.776 -31.330 -10.428  1.00 24.15           C  
-ATOM    419  OG1 THR A  83       3.707 -31.787 -11.269  1.00 22.02           O  
-ATOM    420  CG2 THR A  83       5.207 -29.950 -10.872  1.00 30.26           C  
-ATOM    421  N   TRP A  84       6.893 -31.995  -8.301  1.00 33.55           N  
-ATOM    422  CA  TRP A  84       7.918 -31.729  -7.303  1.00 31.71           C  
-ATOM    423  C   TRP A  84       9.207 -32.471  -7.622  1.00 31.00           C  
-ATOM    424  O   TRP A  84      10.294 -31.904  -7.532  1.00 32.92           O  
-ATOM    425  CB  TRP A  84       7.422 -32.130  -5.913  1.00 35.40           C  
-ATOM    426  CG  TRP A  84       8.487 -32.074  -4.863  1.00 36.76           C  
-ATOM    427  CD1 TRP A  84       9.355 -33.070  -4.514  1.00 34.01           C  
-ATOM    428  CD2 TRP A  84       8.803 -30.959  -4.029  1.00 31.13           C  
-ATOM    429  NE1 TRP A  84      10.193 -32.641  -3.512  1.00 24.76           N  
-ATOM    430  CE2 TRP A  84       9.872 -31.345  -3.196  1.00 25.51           C  
-ATOM    431  CE3 TRP A  84       8.286 -29.666  -3.904  1.00 25.59           C  
-ATOM    432  CZ2 TRP A  84      10.431 -30.490  -2.255  1.00 27.83           C  
-ATOM    433  CZ3 TRP A  84       8.842 -28.817  -2.968  1.00 30.08           C  
-ATOM    434  CH2 TRP A  84       9.902 -29.232  -2.155  1.00 34.16           C  
-ATOM    435  N   GLU A  85       9.085 -33.742  -7.992  1.00 30.53           N  
-ATOM    436  CA  GLU A  85      10.261 -34.528  -8.337  1.00 31.22           C  
-ATOM    437  C   GLU A  85      10.869 -34.075  -9.661  1.00 29.45           C  
-ATOM    438  O   GLU A  85      12.062 -34.286  -9.907  1.00 31.70           O  
-ATOM    439  CB  GLU A  85       9.911 -36.015  -8.399  1.00 39.33           C  
-ATOM    440  CG  GLU A  85       9.524 -36.606  -7.055  1.00 34.28           C  
-ATOM    441  CD  GLU A  85       9.257 -38.094  -7.124  1.00 40.54           C  
-ATOM    442  OE1 GLU A  85       8.999 -38.605  -8.235  1.00 42.76           O  
-ATOM    443  OE2 GLU A  85       9.303 -38.750  -6.061  1.00 39.61           O  
-ATOM    444  N   SER A  86      10.049 -33.454 -10.507  1.00 27.84           N  
-ATOM    445  CA  SER A  86      10.504 -33.018 -11.824  1.00 30.05           C  
-ATOM    446  C   SER A  86      11.306 -31.733 -11.706  1.00 25.59           C  
-ATOM    447  O   SER A  86      12.234 -31.501 -12.473  1.00 28.74           O  
-ATOM    448  CB  SER A  86       9.323 -32.822 -12.785  1.00 34.88           C  
-ATOM    449  OG  SER A  86       8.600 -31.635 -12.495  1.00 42.68           O  
-ATOM    450  N   MET A  87      10.946 -30.902 -10.737  1.00 27.49           N  
-ATOM    451  CA  MET A  87      11.687 -29.676 -10.494  1.00 33.53           C  
-ATOM    452  C   MET A  87      13.096 -29.986  -9.992  1.00 38.36           C  
-ATOM    453  O   MET A  87      13.301 -30.948  -9.247  1.00 28.59           O  
-ATOM    454  CB  MET A  87      10.947 -28.793  -9.489  1.00 32.97           C  
-ATOM    455  CG  MET A  87       9.564 -28.351  -9.948  1.00 33.09           C  
-ATOM    456  SD  MET A  87       8.695 -27.389  -8.696  1.00 36.51           S  
-ATOM    457  CE  MET A  87       9.980 -26.239  -8.231  1.00 36.00           C  
-ATOM    458  N   PRO A  88      14.080 -29.172 -10.412  1.00 48.73           N  
-ATOM    459  CA  PRO A  88      15.468 -29.317  -9.954  1.00 47.75           C  
-ATOM    460  C   PRO A  88      15.608 -29.042  -8.458  1.00 52.48           C  
-ATOM    461  O   PRO A  88      14.809 -28.290  -7.899  1.00 51.78           O  
-ATOM    462  CB  PRO A  88      16.228 -28.267 -10.780  1.00 35.47           C  
-ATOM    463  CG  PRO A  88      15.185 -27.290 -11.213  1.00 42.90           C  
-ATOM    464  CD  PRO A  88      13.942 -28.099 -11.411  1.00 37.58           C  
-ATOM    465  N   ARG A  89      16.608 -29.653  -7.827  1.00 51.71           N  
-ATOM    466  CA  ARG A  89      16.806 -29.549  -6.382  1.00 48.46           C  
-ATOM    467  C   ARG A  89      16.920 -28.107  -5.899  1.00 45.97           C  
-ATOM    468  O   ARG A  89      16.306 -27.729  -4.903  1.00 48.68           O  
-ATOM    469  CB  ARG A  89      18.061 -30.316  -5.964  1.00 62.32           C  
-ATOM    470  CG  ARG A  89      18.006 -31.813  -6.207  1.00 77.20           C  
-ATOM    471  CD  ARG A  89      17.375 -32.552  -5.037  1.00 81.12           C  
-ATOM    472  NE  ARG A  89      17.952 -33.884  -4.877  1.00 84.78           N  
-ATOM    473  CZ  ARG A  89      17.539 -34.965  -5.532  1.00 87.55           C  
-ATOM    474  NH1 ARG A  89      16.537 -34.880  -6.396  1.00 86.56           N  
-ATOM    475  NH2 ARG A  89      18.130 -36.134  -5.322  1.00 79.12           N  
-ATOM    476  N   LYS A  90      17.707 -27.307  -6.611  1.00 46.39           N  
-ATOM    477  CA  LYS A  90      18.033 -25.956  -6.168  1.00 51.73           C  
-ATOM    478  C   LYS A  90      16.818 -25.030  -6.141  1.00 44.42           C  
-ATOM    479  O   LYS A  90      16.766 -24.088  -5.353  1.00 52.28           O  
-ATOM    480  CB  LYS A  90      19.123 -25.359  -7.065  1.00 55.84           C  
-ATOM    481  CG  LYS A  90      18.648 -24.956  -8.456  1.00 71.32           C  
-ATOM    482  CD  LYS A  90      19.600 -25.433  -9.544  1.00 81.36           C  
-ATOM    483  CE  LYS A  90      19.554 -26.946  -9.705  1.00 72.15           C  
-ATOM    484  NZ  LYS A  90      20.331 -27.400 -10.893  1.00 57.41           N  
-ATOM    485  N   PHE A  91      15.838 -25.305  -6.994  1.00 42.62           N  
-ATOM    486  CA  PHE A  91      14.698 -24.412  -7.149  1.00 47.41           C  
-ATOM    487  C   PHE A  91      13.523 -24.785  -6.253  1.00 46.24           C  
-ATOM    488  O   PHE A  91      12.560 -24.025  -6.137  1.00 45.62           O  
-ATOM    489  CB  PHE A  91      14.247 -24.387  -8.610  1.00 55.15           C  
-ATOM    490  CG  PHE A  91      14.993 -23.397  -9.459  1.00 70.71           C  
-ATOM    491  CD1 PHE A  91      15.337 -22.154  -8.953  1.00 76.34           C  
-ATOM    492  CD2 PHE A  91      15.353 -23.709 -10.761  1.00 67.92           C  
-ATOM    493  CE1 PHE A  91      16.021 -21.237  -9.729  1.00 73.97           C  
-ATOM    494  CE2 PHE A  91      16.038 -22.796 -11.543  1.00 77.06           C  
-ATOM    495  CZ  PHE A  91      16.372 -21.560 -11.026  1.00 86.99           C  
-ATOM    496  N   ARG A  92      13.596 -25.950  -5.620  1.00 43.89           N  
-ATOM    497  CA  ARG A  92      12.496 -26.403  -4.779  1.00 39.19           C  
-ATOM    498  C   ARG A  92      12.886 -26.459  -3.303  1.00 32.97           C  
-ATOM    499  O   ARG A  92      14.006 -26.835  -2.962  1.00 39.21           O  
-ATOM    500  CB  ARG A  92      11.986 -27.769  -5.249  1.00 35.84           C  
-ATOM    501  CG  ARG A  92      12.916 -28.934  -4.989  1.00 32.36           C  
-ATOM    502  CD  ARG A  92      12.371 -30.187  -5.647  1.00 35.57           C  
-ATOM    503  NE  ARG A  92      13.086 -31.388  -5.234  1.00 45.64           N  
-ATOM    504  CZ  ARG A  92      13.346 -32.414  -6.038  1.00 49.98           C  
-ATOM    505  NH1 ARG A  92      13.998 -33.471  -5.576  1.00 55.14           N  
-ATOM    506  NH2 ARG A  92      12.958 -32.382  -7.306  1.00 47.84           N  
-ATOM    507  N   PRO A  93      11.958 -26.066  -2.416  1.00 29.89           N  
-ATOM    508  CA  PRO A  93      10.619 -25.559  -2.739  1.00 30.16           C  
-ATOM    509  C   PRO A  93      10.647 -24.162  -3.357  1.00 34.97           C  
-ATOM    510  O   PRO A  93      11.604 -23.415  -3.143  1.00 43.81           O  
-ATOM    511  CB  PRO A  93       9.921 -25.533  -1.379  1.00 31.08           C  
-ATOM    512  CG  PRO A  93      11.025 -25.374  -0.399  1.00 28.12           C  
-ATOM    513  CD  PRO A  93      12.170 -26.159  -0.962  1.00 36.34           C  
-ATOM    514  N   LEU A  94       9.616 -23.834  -4.129  1.00 29.55           N  
-ATOM    515  CA  LEU A  94       9.525 -22.535  -4.779  1.00 32.57           C  
-ATOM    516  C   LEU A  94       9.529 -21.417  -3.745  1.00 34.64           C  
-ATOM    517  O   LEU A  94       8.641 -21.339  -2.896  1.00 38.84           O  
-ATOM    518  CB  LEU A  94       8.271 -22.465  -5.652  1.00 37.39           C  
-ATOM    519  CG  LEU A  94       8.336 -23.296  -6.937  1.00 27.98           C  
-ATOM    520  CD1 LEU A  94       6.967 -23.431  -7.582  1.00 25.29           C  
-ATOM    521  CD2 LEU A  94       9.330 -22.685  -7.916  1.00 31.31           C  
-ATOM    522  N   VAL A  95      10.542 -20.560  -3.822  1.00 34.89           N  
-ATOM    523  CA  VAL A  95      10.763 -19.518  -2.824  1.00 38.42           C  
-ATOM    524  C   VAL A  95       9.604 -18.530  -2.708  1.00 41.43           C  
-ATOM    525  O   VAL A  95       8.925 -18.232  -3.693  1.00 42.13           O  
-ATOM    526  CB  VAL A  95      12.047 -18.729  -3.129  1.00 37.04           C  
-ATOM    527  CG1 VAL A  95      13.273 -19.534  -2.720  1.00 47.68           C  
-ATOM    528  CG2 VAL A  95      12.104 -18.361  -4.606  1.00 36.89           C  
-ATOM    529  N   ASP A  96       9.384 -18.045  -1.487  1.00 43.10           N  
-ATOM    530  CA  ASP A  96       8.378 -17.023  -1.187  1.00 34.23           C  
-ATOM    531  C   ASP A  96       6.950 -17.466  -1.506  1.00 29.97           C  
-ATOM    532  O   ASP A  96       6.038 -16.642  -1.577  1.00 34.22           O  
-ATOM    533  CB  ASP A  96       8.703 -15.730  -1.935  1.00 33.69           C  
-ATOM    534  CG  ASP A  96      10.124 -15.260  -1.687  1.00 43.91           C  
-ATOM    535  OD1 ASP A  96      10.661 -15.540  -0.591  1.00 44.63           O  
-ATOM    536  OD2 ASP A  96      10.705 -14.617  -2.588  1.00 31.45           O  
-ATOM    537  N   ARG A  97       6.764 -18.769  -1.689  1.00 25.53           N  
-ATOM    538  CA  ARG A  97       5.443 -19.342  -1.918  1.00 25.51           C  
-ATOM    539  C   ARG A  97       5.258 -20.564  -1.033  1.00 27.90           C  
-ATOM    540  O   ARG A  97       6.171 -21.379  -0.892  1.00 26.49           O  
-ATOM    541  CB  ARG A  97       5.257 -19.728  -3.383  1.00 26.90           C  
-ATOM    542  CG  ARG A  97       5.042 -18.560  -4.328  1.00 28.51           C  
-ATOM    543  CD  ARG A  97       5.525 -18.909  -5.726  1.00 29.73           C  
-ATOM    544  NE  ARG A  97       6.977 -19.065  -5.758  1.00 34.29           N  
-ATOM    545  CZ  ARG A  97       7.694 -19.224  -6.865  1.00 30.16           C  
-ATOM    546  NH1 ARG A  97       7.098 -19.249  -8.048  1.00 31.67           N  
-ATOM    547  NH2 ARG A  97       9.012 -19.356  -6.787  1.00 34.00           N  
-ATOM    548  N   LEU A  98       4.082 -20.690  -0.428  1.00 32.02           N  
-ATOM    549  CA  LEU A  98       3.782 -21.871   0.370  1.00 29.55           C  
-ATOM    550  C   LEU A  98       3.677 -23.079  -0.544  1.00 30.97           C  
-ATOM    551  O   LEU A  98       2.827 -23.123  -1.423  1.00 29.39           O  
-ATOM    552  CB  LEU A  98       2.486 -21.692   1.162  1.00 33.93           C  
-ATOM    553  CG  LEU A  98       1.972 -22.964   1.837  1.00 34.31           C  
-ATOM    554  CD1 LEU A  98       2.977 -23.476   2.860  1.00 31.44           C  
-ATOM    555  CD2 LEU A  98       0.617 -22.725   2.481  1.00 39.77           C  
-ATOM    556  N   ASN A  99       4.543 -24.062  -0.338  1.00 28.53           N  
-ATOM    557  CA  ASN A  99       4.533 -25.247  -1.188  1.00 30.10           C  
-ATOM    558  C   ASN A  99       3.703 -26.391  -0.613  1.00 28.61           C  
-ATOM    559  O   ASN A  99       4.004 -26.916   0.463  1.00 40.01           O  
-ATOM    560  CB  ASN A  99       5.964 -25.720  -1.446  1.00 34.92           C  
-ATOM    561  CG  ASN A  99       6.654 -24.919  -2.535  1.00 30.28           C  
-ATOM    562  OD1 ASN A  99       6.886 -23.718  -2.387  1.00 35.74           O  
-ATOM    563  ND2 ASN A  99       6.993 -25.583  -3.632  1.00 18.91           N  
-ATOM    564  N   ILE A 100       2.653 -26.773  -1.334  1.00 21.58           N  
-ATOM    565  CA  ILE A 100       1.855 -27.924  -0.934  1.00 25.43           C  
-ATOM    566  C   ILE A 100       1.957 -29.026  -1.976  1.00 27.73           C  
-ATOM    567  O   ILE A 100       1.725 -28.798  -3.163  1.00 32.04           O  
-ATOM    568  CB  ILE A 100       0.372 -27.563  -0.722  1.00 24.32           C  
-ATOM    569  CG1 ILE A 100       0.227 -26.509   0.377  1.00 30.87           C  
-ATOM    570  CG2 ILE A 100      -0.429 -28.807  -0.364  1.00 21.50           C  
-ATOM    571  CD1 ILE A 100      -1.210 -26.222   0.754  1.00 20.33           C  
-ATOM    572  N   VAL A 101       2.309 -30.222  -1.522  1.00 25.49           N  
-ATOM    573  CA  VAL A 101       2.456 -31.361  -2.410  1.00 24.03           C  
-ATOM    574  C   VAL A 101       1.411 -32.424  -2.109  1.00 20.74           C  
-ATOM    575  O   VAL A 101       1.266 -32.859  -0.968  1.00 22.67           O  
-ATOM    576  CB  VAL A 101       3.859 -31.986  -2.297  1.00 21.37           C  
-ATOM    577  CG1 VAL A 101       3.971 -33.201  -3.207  1.00 23.48           C  
-ATOM    578  CG2 VAL A 101       4.932 -30.956  -2.626  1.00 18.93           C  
-ATOM    579  N   VAL A 102       0.681 -32.833  -3.140  1.00 24.00           N  
-ATOM    580  CA  VAL A 102      -0.292 -33.910  -3.011  1.00 31.94           C  
-ATOM    581  C   VAL A 102       0.358 -35.259  -3.308  1.00 36.14           C  
-ATOM    582  O   VAL A 102       0.804 -35.514  -4.427  1.00 32.53           O  
-ATOM    583  CB  VAL A 102      -1.496 -33.705  -3.949  1.00 25.59           C  
-ATOM    584  CG1 VAL A 102      -2.421 -34.908  -3.899  1.00 27.24           C  
-ATOM    585  CG2 VAL A 102      -2.241 -32.434  -3.576  1.00 24.51           C  
-ATOM    586  N   SER A 103       0.414 -36.115  -2.293  1.00 34.06           N  
-ATOM    587  CA  SER A 103       1.005 -37.441  -2.434  1.00 32.36           C  
-ATOM    588  C   SER A 103       0.554 -38.343  -1.294  1.00 37.89           C  
-ATOM    589  O   SER A 103       0.043 -37.869  -0.280  1.00 43.63           O  
-ATOM    590  CB  SER A 103       2.534 -37.350  -2.465  1.00 35.06           C  
-ATOM    591  OG  SER A 103       3.129 -38.622  -2.656  1.00 33.51           O  
-ATOM    592  N   SER A 104       0.738 -39.647  -1.465  1.00 38.16           N  
-ATOM    593  CA  SER A 104       0.428 -40.596  -0.406  1.00 34.76           C  
-ATOM    594  C   SER A 104       1.694 -41.312   0.039  1.00 40.66           C  
-ATOM    595  O   SER A 104       1.804 -41.752   1.182  1.00 56.90           O  
-ATOM    596  CB  SER A 104      -0.626 -41.599  -0.871  1.00 32.46           C  
-ATOM    597  OG  SER A 104      -1.882 -40.962  -1.044  1.00 31.79           O  
-ATOM    598  N   SER A 105       2.655 -41.411  -0.873  1.00 37.94           N  
-ATOM    599  CA  SER A 105       3.930 -42.047  -0.573  1.00 45.94           C  
-ATOM    600  C   SER A 105       4.882 -41.071   0.112  1.00 46.03           C  
-ATOM    601  O   SER A 105       5.545 -41.421   1.089  1.00 51.84           O  
-ATOM    602  CB  SER A 105       4.560 -42.607  -1.853  1.00 42.94           C  
-ATOM    603  OG  SER A 105       4.660 -41.611  -2.853  1.00 48.22           O  
-ATOM    604  N   LEU A 106       4.943 -39.846  -0.401  1.00 42.19           N  
-ATOM    605  CA  LEU A 106       5.812 -38.823   0.170  1.00 46.25           C  
-ATOM    606  C   LEU A 106       5.310 -38.313   1.516  1.00 42.59           C  
-ATOM    607  O   LEU A 106       4.104 -38.231   1.756  1.00 39.29           O  
-ATOM    608  CB  LEU A 106       5.965 -37.643  -0.793  1.00 47.38           C  
-ATOM    609  CG  LEU A 106       7.164 -37.692  -1.742  1.00 49.90           C  
-ATOM    610  CD1 LEU A 106       7.421 -36.322  -2.351  1.00 38.67           C  
-ATOM    611  CD2 LEU A 106       8.400 -38.201  -1.017  1.00 58.27           C  
-ATOM    612  N   LYS A 107       6.251 -37.971   2.390  1.00 41.55           N  
-ATOM    613  CA  LYS A 107       5.927 -37.400   3.689  1.00 46.38           C  
-ATOM    614  C   LYS A 107       6.591 -36.037   3.828  1.00 48.02           C  
-ATOM    615  O   LYS A 107       7.465 -35.687   3.036  1.00 49.57           O  
-ATOM    616  CB  LYS A 107       6.374 -38.330   4.816  1.00 59.61           C  
-ATOM    617  CG  LYS A 107       5.814 -39.738   4.713  1.00 68.23           C  
-ATOM    618  CD  LYS A 107       6.184 -40.566   5.931  1.00 65.82           C  
-ATOM    619  CE  LYS A 107       5.019 -41.443   6.358  1.00 78.76           C  
-ATOM    620  NZ  LYS A 107       3.805 -40.627   6.651  1.00 65.16           N  
-ATOM    621  N   GLU A 108       6.182 -35.272   4.834  1.00 41.99           N  
-ATOM    622  CA  GLU A 108       6.722 -33.934   5.034  1.00 37.20           C  
-ATOM    623  C   GLU A 108       8.194 -33.982   5.425  1.00 41.44           C  
-ATOM    624  O   GLU A 108       8.972 -33.110   5.049  1.00 49.17           O  
-ATOM    625  CB  GLU A 108       5.904 -33.186   6.091  1.00 40.11           C  
-ATOM    626  CG  GLU A 108       4.486 -32.877   5.650  1.00 40.04           C  
-ATOM    627  CD  GLU A 108       3.727 -32.035   6.653  1.00 40.88           C  
-ATOM    628  OE1 GLU A 108       4.323 -31.616   7.671  1.00 43.50           O  
-ATOM    629  OE2 GLU A 108       2.526 -31.792   6.417  1.00 44.94           O  
-ATOM    630  N   GLU A 109       8.572 -35.013   6.171  1.00 45.42           N  
-ATOM    631  CA  GLU A 109       9.959 -35.176   6.583  1.00 51.99           C  
-ATOM    632  C   GLU A 109      10.846 -35.663   5.446  1.00 45.26           C  
-ATOM    633  O   GLU A 109      12.061 -35.457   5.466  1.00 46.67           O  
-ATOM    634  CB  GLU A 109      10.058 -36.137   7.766  1.00 43.85           C  
-ATOM    635  CG  GLU A 109      10.131 -35.429   9.106  1.00 75.30           C  
-ATOM    636  CD  GLU A 109      11.230 -34.373   9.156  1.00 81.78           C  
-ATOM    637  OE1 GLU A 109      10.972 -33.265   9.678  1.00 67.72           O  
-ATOM    638  OE2 GLU A 109      12.350 -34.649   8.675  1.00 67.20           O  
-ATOM    639  N   ASP A 110      10.241 -36.322   4.464  1.00 39.52           N  
-ATOM    640  CA  ASP A 110      10.965 -36.707   3.262  1.00 38.40           C  
-ATOM    641  C   ASP A 110      11.463 -35.457   2.553  1.00 46.15           C  
-ATOM    642  O   ASP A 110      12.585 -35.414   2.045  1.00 45.22           O  
-ATOM    643  CB  ASP A 110      10.080 -37.540   2.332  1.00 43.30           C  
-ATOM    644  CG  ASP A 110      10.102 -39.016   2.674  1.00 54.41           C  
-ATOM    645  OD1 ASP A 110      11.138 -39.665   2.418  1.00 59.70           O  
-ATOM    646  OD2 ASP A 110       9.088 -39.529   3.193  1.00 54.49           O  
-ATOM    647  N   ILE A 111      10.617 -34.436   2.538  1.00 42.07           N  
-ATOM    648  CA  ILE A 111      10.949 -33.171   1.909  1.00 34.24           C  
-ATOM    649  C   ILE A 111      11.870 -32.349   2.804  1.00 36.11           C  
-ATOM    650  O   ILE A 111      12.804 -31.710   2.326  1.00 37.32           O  
-ATOM    651  CB  ILE A 111       9.672 -32.374   1.581  1.00 32.14           C  
-ATOM    652  CG1 ILE A 111       8.880 -33.098   0.487  1.00 33.29           C  
-ATOM    653  CG2 ILE A 111      10.021 -30.961   1.154  1.00 31.12           C  
-ATOM    654  CD1 ILE A 111       7.560 -32.450   0.144  1.00 29.34           C  
-ATOM    655  N   ALA A 112      11.614 -32.394   4.107  1.00 37.16           N  
-ATOM    656  CA  ALA A 112      12.399 -31.639   5.076  1.00 39.92           C  
-ATOM    657  C   ALA A 112      13.851 -32.104   5.101  1.00 43.20           C  
-ATOM    658  O   ALA A 112      14.766 -31.294   5.268  1.00 38.48           O  
-ATOM    659  CB  ALA A 112      11.787 -31.757   6.459  1.00 48.82           C  
-ATOM    660  N   ALA A 113      14.054 -33.408   4.935  1.00 44.60           N  
-ATOM    661  CA  ALA A 113      15.392 -33.988   4.974  1.00 41.20           C  
-ATOM    662  C   ALA A 113      16.065 -33.966   3.605  1.00 44.12           C  
-ATOM    663  O   ALA A 113      17.196 -34.429   3.455  1.00 49.01           O  
-ATOM    664  CB  ALA A 113      15.331 -35.412   5.509  1.00 35.87           C  
-ATOM    665  N   GLU A 114      15.364 -33.430   2.610  1.00 44.14           N  
-ATOM    666  CA  GLU A 114      15.901 -33.324   1.257  1.00 40.76           C  
-ATOM    667  C   GLU A 114      16.812 -32.104   1.128  1.00 38.91           C  
-ATOM    668  O   GLU A 114      17.809 -32.128   0.404  1.00 35.79           O  
-ATOM    669  CB  GLU A 114      14.760 -33.248   0.242  1.00 49.73           C  
-ATOM    670  CG  GLU A 114      15.197 -33.221  -1.211  1.00 53.98           C  
-ATOM    671  CD  GLU A 114      14.020 -33.121  -2.163  1.00 61.07           C  
-ATOM    672  OE1 GLU A 114      13.936 -32.121  -2.907  1.00 58.43           O  
-ATOM    673  OE2 GLU A 114      13.174 -34.042  -2.163  1.00 55.44           O  
-ATOM    674  N   LYS A 115      16.454 -31.042   1.843  1.00 46.55           N  
-ATOM    675  CA  LYS A 115      17.225 -29.805   1.867  1.00 45.12           C  
-ATOM    676  C   LYS A 115      16.819 -28.972   3.081  1.00 49.46           C  
-ATOM    677  O   LYS A 115      15.627 -28.832   3.367  1.00 43.99           O  
-ATOM    678  CB  LYS A 115      17.014 -29.004   0.578  1.00 36.96           C  
-ATOM    679  CG  LYS A 115      17.719 -27.656   0.559  1.00 32.68           C  
-ATOM    680  CD  LYS A 115      17.042 -26.677  -0.387  1.00 36.39           C  
-ATOM    681  CE  LYS A 115      17.149 -27.127  -1.832  1.00 36.75           C  
-ATOM    682  NZ  LYS A 115      16.623 -26.092  -2.768  1.00 40.95           N  
-ATOM    683  N   PRO A 116      17.808 -28.420   3.802  1.00 40.33           N  
-ATOM    684  CA  PRO A 116      17.527 -27.579   4.971  1.00 41.91           C  
-ATOM    685  C   PRO A 116      16.655 -26.371   4.637  1.00 48.07           C  
-ATOM    686  O   PRO A 116      16.963 -25.611   3.717  1.00 40.66           O  
-ATOM    687  CB  PRO A 116      18.923 -27.134   5.430  1.00 34.44           C  
-ATOM    688  CG  PRO A 116      19.821 -27.380   4.256  1.00 34.75           C  
-ATOM    689  CD  PRO A 116      19.253 -28.583   3.581  1.00 38.98           C  
-ATOM    690  N   GLN A 117      15.570 -26.211   5.387  1.00 48.90           N  
-ATOM    691  CA  GLN A 117      14.667 -25.084   5.209  1.00 45.07           C  
-ATOM    692  C   GLN A 117      15.375 -23.759   5.480  1.00 54.42           C  
-ATOM    693  O   GLN A 117      15.967 -23.564   6.543  1.00 50.71           O  
-ATOM    694  CB  GLN A 117      13.454 -25.232   6.126  1.00 37.70           C  
-ATOM    695  CG  GLN A 117      12.540 -24.021   6.148  1.00 53.76           C  
-ATOM    696  CD  GLN A 117      11.376 -24.194   7.103  1.00 62.91           C  
-ATOM    697  OE1 GLN A 117      10.660 -23.241   7.408  1.00 65.61           O  
-ATOM    698  NE2 GLN A 117      11.181 -25.417   7.581  1.00 66.11           N  
-ATOM    699  N   ALA A 118      15.320 -22.853   4.509  1.00 56.28           N  
-ATOM    700  CA  ALA A 118      15.933 -21.541   4.660  1.00 47.34           C  
-ATOM    701  C   ALA A 118      15.120 -20.695   5.627  1.00 48.66           C  
-ATOM    702  O   ALA A 118      13.936 -20.952   5.843  1.00 54.26           O  
-ATOM    703  CB  ALA A 118      16.054 -20.847   3.314  1.00 46.26           C  
-ATOM    704  N   GLU A 119      15.760 -19.689   6.211  1.00 50.76           N  
-ATOM    705  CA  GLU A 119      15.090 -18.817   7.166  1.00 62.02           C  
-ATOM    706  C   GLU A 119      14.069 -17.930   6.461  1.00 59.56           C  
-ATOM    707  O   GLU A 119      14.307 -17.452   5.351  1.00 50.28           O  
-ATOM    708  CB  GLU A 119      16.115 -17.964   7.924  1.00 74.07           C  
-ATOM    709  CG  GLU A 119      15.533 -17.102   9.042  1.00 72.42           C  
-ATOM    710  CD  GLU A 119      15.146 -15.708   8.573  1.00 84.66           C  
-ATOM    711  OE1 GLU A 119      14.048 -15.239   8.944  1.00 80.59           O  
-ATOM    712  OE2 GLU A 119      15.941 -15.081   7.840  1.00 73.19           O  
-ATOM    713  N   GLY A 120      12.926 -17.728   7.109  1.00 53.30           N  
-ATOM    714  CA  GLY A 120      11.886 -16.860   6.587  1.00 58.72           C  
-ATOM    715  C   GLY A 120      10.918 -17.548   5.644  1.00 51.95           C  
-ATOM    716  O   GLY A 120       9.867 -17.000   5.309  1.00 40.97           O  
-ATOM    717  N   GLN A 121      11.271 -18.754   5.213  1.00 51.86           N  
-ATOM    718  CA  GLN A 121      10.440 -19.505   4.282  1.00 48.25           C  
-ATOM    719  C   GLN A 121       9.463 -20.419   5.010  1.00 53.75           C  
-ATOM    720  O   GLN A 121       9.666 -20.764   6.174  1.00 60.51           O  
-ATOM    721  CB  GLN A 121      11.315 -20.321   3.331  1.00 45.03           C  
-ATOM    722  CG  GLN A 121      12.124 -19.471   2.371  1.00 50.44           C  
-ATOM    723  CD  GLN A 121      11.245 -18.644   1.457  1.00 53.56           C  
-ATOM    724  OE1 GLN A 121      10.256 -19.139   0.915  1.00 50.34           O  
-ATOM    725  NE2 GLN A 121      11.595 -17.374   1.287  1.00 43.45           N  
-ATOM    726  N   GLN A 122       8.397 -20.801   4.314  1.00 46.20           N  
-ATOM    727  CA  GLN A 122       7.392 -21.695   4.872  1.00 41.54           C  
-ATOM    728  C   GLN A 122       7.837 -23.144   4.746  1.00 45.05           C  
-ATOM    729  O   GLN A 122       8.551 -23.503   3.808  1.00 39.98           O  
-ATOM    730  CB  GLN A 122       6.046 -21.498   4.173  1.00 42.66           C  
-ATOM    731  CG  GLN A 122       4.970 -20.875   5.048  1.00 41.41           C  
-ATOM    732  CD  GLN A 122       5.325 -19.474   5.507  1.00 52.40           C  
-ATOM    733  OE1 GLN A 122       6.079 -18.759   4.844  1.00 51.65           O  
-ATOM    734  NE2 GLN A 122       4.781 -19.074   6.651  1.00 46.71           N  
-ATOM    735  N   ARG A 123       7.418 -23.974   5.694  1.00 46.66           N  
-ATOM    736  CA  ARG A 123       7.724 -25.393   5.625  1.00 37.31           C  
-ATOM    737  C   ARG A 123       6.813 -26.036   4.587  1.00 32.82           C  
-ATOM    738  O   ARG A 123       5.640 -25.676   4.462  1.00 35.79           O  
-ATOM    739  CB  ARG A 123       7.575 -26.059   6.999  1.00 38.78           C  
-ATOM    740  CG  ARG A 123       6.254 -26.771   7.250  1.00 54.89           C  
-ATOM    741  CD  ARG A 123       6.252 -27.445   8.613  1.00 51.11           C  
-ATOM    742  NE  ARG A 123       7.485 -28.196   8.831  1.00 71.77           N  
-ATOM    743  CZ  ARG A 123       7.622 -29.499   8.605  1.00 76.72           C  
-ATOM    744  NH1 ARG A 123       8.789 -30.090   8.828  1.00 62.54           N  
-ATOM    745  NH2 ARG A 123       6.595 -30.212   8.163  1.00 70.23           N  
-ATOM    746  N   VAL A 124       7.368 -26.965   3.817  1.00 35.29           N  
-ATOM    747  CA  VAL A 124       6.614 -27.617   2.754  1.00 32.23           C  
-ATOM    748  C   VAL A 124       5.602 -28.582   3.353  1.00 35.12           C  
-ATOM    749  O   VAL A 124       5.933 -29.378   4.232  1.00 39.26           O  
-ATOM    750  CB  VAL A 124       7.533 -28.376   1.781  1.00 26.63           C  
-ATOM    751  CG1 VAL A 124       6.741 -28.881   0.591  1.00 18.15           C  
-ATOM    752  CG2 VAL A 124       8.661 -27.480   1.316  1.00 28.51           C  
-ATOM    753  N   ARG A 125       4.364 -28.510   2.877  1.00 34.62           N  
-ATOM    754  CA  ARG A 125       3.304 -29.349   3.421  1.00 29.45           C  
-ATOM    755  C   ARG A 125       2.932 -30.473   2.460  1.00 31.27           C  
-ATOM    756  O   ARG A 125       3.124 -30.355   1.251  1.00 34.04           O  
-ATOM    757  CB  ARG A 125       2.074 -28.503   3.744  1.00 33.51           C  
-ATOM    758  CG  ARG A 125       1.324 -28.965   4.969  1.00 44.03           C  
-ATOM    759  CD  ARG A 125       2.063 -28.607   6.244  1.00 36.12           C  
-ATOM    760  NE  ARG A 125       1.255 -28.906   7.421  1.00 37.77           N  
-ATOM    761  CZ  ARG A 125       0.435 -28.036   7.999  1.00 50.07           C  
-ATOM    762  NH1 ARG A 125      -0.268 -28.390   9.067  1.00 46.62           N  
-ATOM    763  NH2 ARG A 125       0.321 -26.808   7.511  1.00 51.30           N  
-ATOM    764  N   VAL A 126       2.403 -31.566   3.003  1.00 27.86           N  
-ATOM    765  CA  VAL A 126       1.996 -32.705   2.182  1.00 28.43           C  
-ATOM    766  C   VAL A 126       0.571 -33.154   2.502  1.00 27.27           C  
-ATOM    767  O   VAL A 126       0.243 -33.432   3.654  1.00 34.24           O  
-ATOM    768  CB  VAL A 126       2.948 -33.905   2.362  1.00 24.25           C  
-ATOM    769  CG1 VAL A 126       2.430 -35.114   1.602  1.00 25.04           C  
-ATOM    770  CG2 VAL A 126       4.350 -33.545   1.901  1.00 32.12           C  
-ATOM    771  N   CYS A 127      -0.269 -33.220   1.473  1.00 23.88           N  
-ATOM    772  CA  CYS A 127      -1.651 -33.656   1.634  1.00 19.78           C  
-ATOM    773  C   CYS A 127      -1.937 -34.873   0.761  1.00 27.45           C  
-ATOM    774  O   CYS A 127      -1.214 -35.143  -0.197  1.00 29.16           O  
-ATOM    775  CB  CYS A 127      -2.611 -32.519   1.290  1.00 29.06           C  
-ATOM    776  SG  CYS A 127      -2.173 -30.933   2.038  1.00 28.00           S  
-ATOM    777  N   ALA A 128      -2.998 -35.601   1.092  1.00 34.15           N  
-ATOM    778  CA  ALA A 128      -3.315 -36.844   0.397  1.00 31.54           C  
-ATOM    779  C   ALA A 128      -4.305 -36.640  -0.744  1.00 35.77           C  
-ATOM    780  O   ALA A 128      -4.653 -37.592  -1.446  1.00 45.96           O  
-ATOM    781  CB  ALA A 128      -3.854 -37.869   1.379  1.00 26.18           C  
-ATOM    782  N   SER A 129      -4.759 -35.403  -0.920  1.00 35.41           N  
-ATOM    783  CA  SER A 129      -5.678 -35.065  -2.005  1.00 37.32           C  
-ATOM    784  C   SER A 129      -5.842 -33.558  -2.135  1.00 42.35           C  
-ATOM    785  O   SER A 129      -5.462 -32.806  -1.243  1.00 44.48           O  
-ATOM    786  CB  SER A 129      -7.044 -35.718  -1.783  1.00 39.99           C  
-ATOM    787  OG  SER A 129      -7.676 -35.193  -0.628  1.00 43.88           O  
-ATOM    788  N   LEU A 130      -6.408 -33.128  -3.256  1.00 32.52           N  
-ATOM    789  CA  LEU A 130      -6.675 -31.715  -3.481  1.00 33.67           C  
-ATOM    790  C   LEU A 130      -7.708 -31.139  -2.500  1.00 36.11           C  
-ATOM    791  O   LEU A 130      -7.500 -30.037  -1.979  1.00 45.34           O  
-ATOM    792  CB  LEU A 130      -7.128 -31.485  -4.924  1.00 29.70           C  
-ATOM    793  CG  LEU A 130      -7.197 -30.014  -5.329  1.00 30.91           C  
-ATOM    794  CD1 LEU A 130      -5.834 -29.369  -5.157  1.00 19.14           C  
-ATOM    795  CD2 LEU A 130      -7.686 -29.867  -6.754  1.00 24.31           C  
-ATOM    796  N   PRO A 131      -8.825 -31.862  -2.253  1.00 30.26           N  
-ATOM    797  CA  PRO A 131      -9.728 -31.368  -1.206  1.00 40.72           C  
-ATOM    798  C   PRO A 131      -9.045 -31.252   0.156  1.00 43.36           C  
-ATOM    799  O   PRO A 131      -9.371 -30.346   0.926  1.00 32.51           O  
-ATOM    800  CB  PRO A 131     -10.835 -32.426  -1.174  1.00 36.05           C  
-ATOM    801  CG  PRO A 131     -10.868 -32.958  -2.560  1.00 33.35           C  
-ATOM    802  CD  PRO A 131      -9.429 -32.989  -2.992  1.00 32.21           C  
-ATOM    803  N   ALA A 132      -8.109 -32.155   0.440  1.00 39.46           N  
-ATOM    804  CA  ALA A 132      -7.334 -32.086   1.675  1.00 35.85           C  
-ATOM    805  C   ALA A 132      -6.448 -30.853   1.678  1.00 44.29           C  
-ATOM    806  O   ALA A 132      -6.286 -30.199   2.707  1.00 47.44           O  
-ATOM    807  CB  ALA A 132      -6.494 -33.330   1.854  1.00 33.75           C  
-ATOM    808  N   ALA A 133      -5.868 -30.551   0.521  1.00 39.12           N  
-ATOM    809  CA  ALA A 133      -5.027 -29.373   0.357  1.00 32.73           C  
-ATOM    810  C   ALA A 133      -5.812 -28.102   0.642  1.00 41.08           C  
-ATOM    811  O   ALA A 133      -5.369 -27.251   1.415  1.00 35.85           O  
-ATOM    812  CB  ALA A 133      -4.441 -29.326  -1.046  1.00 24.06           C  
-ATOM    813  N   LEU A 134      -6.977 -27.980   0.012  1.00 43.08           N  
-ATOM    814  CA  LEU A 134      -7.828 -26.809   0.192  1.00 40.12           C  
-ATOM    815  C   LEU A 134      -8.340 -26.688   1.627  1.00 38.59           C  
-ATOM    816  O   LEU A 134      -8.388 -25.592   2.191  1.00 33.30           O  
-ATOM    817  CB  LEU A 134      -9.000 -26.863  -0.787  1.00 42.29           C  
-ATOM    818  CG  LEU A 134      -8.615 -26.925  -2.267  1.00 33.12           C  
-ATOM    819  CD1 LEU A 134      -9.854 -27.042  -3.139  1.00 27.39           C  
-ATOM    820  CD2 LEU A 134      -7.801 -25.701  -2.648  1.00 31.42           C  
-ATOM    821  N   SER A 135      -8.724 -27.822   2.206  1.00 41.83           N  
-ATOM    822  CA  SER A 135      -9.164 -27.871   3.596  1.00 40.87           C  
-ATOM    823  C   SER A 135      -8.061 -27.389   4.529  1.00 47.29           C  
-ATOM    824  O   SER A 135      -8.331 -26.681   5.498  1.00 50.77           O  
-ATOM    825  CB  SER A 135      -9.596 -29.289   3.984  1.00 41.55           C  
-ATOM    826  OG  SER A 135     -10.956 -29.522   3.658  1.00 54.99           O  
-ATOM    827  N   LEU A 136      -6.826 -27.783   4.233  1.00 45.77           N  
-ATOM    828  CA  LEU A 136      -5.670 -27.336   5.000  1.00 40.18           C  
-ATOM    829  C   LEU A 136      -5.495 -25.828   4.868  1.00 39.37           C  
-ATOM    830  O   LEU A 136      -5.338 -25.107   5.856  1.00 49.16           O  
-ATOM    831  CB  LEU A 136      -4.414 -28.070   4.527  1.00 37.24           C  
-ATOM    832  CG  LEU A 136      -3.103 -27.671   5.198  1.00 35.71           C  
-ATOM    833  CD1 LEU A 136      -2.947 -28.369   6.538  1.00 41.45           C  
-ATOM    834  CD2 LEU A 136      -1.943 -27.988   4.281  1.00 36.02           C  
-ATOM    835  N   LEU A 137      -5.541 -25.372   3.623  1.00 37.01           N  
-ATOM    836  CA  LEU A 137      -5.419 -23.961   3.286  1.00 41.25           C  
-ATOM    837  C   LEU A 137      -6.447 -23.098   4.012  1.00 45.12           C  
-ATOM    838  O   LEU A 137      -6.153 -21.965   4.386  1.00 44.82           O  
-ATOM    839  CB  LEU A 137      -5.557 -23.762   1.771  1.00 39.71           C  
-ATOM    840  CG  LEU A 137      -4.325 -23.292   0.987  1.00 31.81           C  
-ATOM    841  CD1 LEU A 137      -3.075 -23.268   1.854  1.00 35.58           C  
-ATOM    842  CD2 LEU A 137      -4.120 -24.168  -0.241  1.00 33.94           C  
-ATOM    843  N   GLU A 138      -7.650 -23.626   4.211  1.00 50.21           N  
-ATOM    844  CA  GLU A 138      -8.680 -22.874   4.918  1.00 50.90           C  
-ATOM    845  C   GLU A 138      -8.513 -22.979   6.435  1.00 53.13           C  
-ATOM    846  O   GLU A 138      -8.696 -21.998   7.159  1.00 61.77           O  
-ATOM    847  CB  GLU A 138     -10.074 -23.354   4.499  1.00 47.11           C  
-ATOM    848  CG  GLU A 138     -10.855 -22.361   3.637  1.00 60.65           C  
-ATOM    849  CD  GLU A 138     -11.277 -21.114   4.404  1.00 69.98           C  
-ATOM    850  OE1 GLU A 138     -11.468 -21.212   5.634  1.00 64.69           O  
-ATOM    851  OE2 GLU A 138     -11.414 -20.035   3.785  1.00 62.40           O  
-ATOM    852  N   GLU A 139      -8.162 -24.170   6.909  1.00 46.44           N  
-ATOM    853  CA  GLU A 139      -8.097 -24.433   8.341  1.00 48.35           C  
-ATOM    854  C   GLU A 139      -6.925 -23.743   9.032  1.00 44.01           C  
-ATOM    855  O   GLU A 139      -7.103 -23.132  10.083  1.00 55.87           O  
-ATOM    856  CB  GLU A 139      -8.038 -25.939   8.599  1.00 52.72           C  
-ATOM    857  CG  GLU A 139      -9.411 -26.584   8.722  1.00 63.26           C  
-ATOM    858  CD  GLU A 139      -9.385 -28.081   8.479  1.00 69.76           C  
-ATOM    859  OE1 GLU A 139      -8.537 -28.775   9.081  1.00 64.55           O  
-ATOM    860  OE2 GLU A 139     -10.217 -28.564   7.681  1.00 64.67           O  
-ATOM    861  N   GLU A 140      -5.730 -23.831   8.455  1.00 42.44           N  
-ATOM    862  CA  GLU A 140      -4.569 -23.234   9.108  1.00 47.05           C  
-ATOM    863  C   GLU A 140      -3.733 -22.328   8.207  1.00 49.60           C  
-ATOM    864  O   GLU A 140      -2.523 -22.204   8.399  1.00 50.88           O  
-ATOM    865  CB  GLU A 140      -3.677 -24.329   9.695  1.00 42.28           C  
-ATOM    866  CG  GLU A 140      -3.638 -25.615   8.899  1.00 40.90           C  
-ATOM    867  CD  GLU A 140      -2.909 -26.721   9.637  1.00 49.60           C  
-ATOM    868  OE1 GLU A 140      -3.541 -27.758   9.932  1.00 47.17           O  
-ATOM    869  OE2 GLU A 140      -1.706 -26.552   9.929  1.00 41.36           O  
-ATOM    870  N   TYR A 141      -4.374 -21.679   7.241  1.00 49.91           N  
-ATOM    871  CA  TYR A 141      -3.669 -20.714   6.406  1.00 52.54           C  
-ATOM    872  C   TYR A 141      -4.563 -19.560   5.965  1.00 60.96           C  
-ATOM    873  O   TYR A 141      -4.196 -18.790   5.078  1.00 60.37           O  
-ATOM    874  CB  TYR A 141      -3.064 -21.405   5.182  1.00 51.44           C  
-ATOM    875  CG  TYR A 141      -1.803 -22.184   5.485  1.00 47.32           C  
-ATOM    876  CD1 TYR A 141      -0.609 -21.530   5.767  1.00 42.79           C  
-ATOM    877  CD2 TYR A 141      -1.806 -23.571   5.488  1.00 43.95           C  
-ATOM    878  CE1 TYR A 141       0.548 -22.238   6.045  1.00 32.92           C  
-ATOM    879  CE2 TYR A 141      -0.655 -24.287   5.763  1.00 40.48           C  
-ATOM    880  CZ  TYR A 141       0.517 -23.618   6.041  1.00 31.61           C  
-ATOM    881  OH  TYR A 141       1.658 -24.337   6.315  1.00 30.28           O  
-ATOM    882  N   LYS A 142      -5.736 -19.439   6.579  1.00 68.71           N  
-ATOM    883  CA  LYS A 142      -6.563 -18.259   6.366  1.00 68.72           C  
-ATOM    884  C   LYS A 142      -5.904 -17.083   7.059  1.00 70.22           C  
-ATOM    885  O   LYS A 142      -5.270 -17.262   8.099  1.00 73.20           O  
-ATOM    886  CB  LYS A 142      -7.987 -18.472   6.878  1.00 63.50           C  
-ATOM    887  CG  LYS A 142      -8.936 -19.005   5.817  1.00 63.86           C  
-ATOM    888  CD  LYS A 142      -8.794 -18.213   4.520  1.00 83.06           C  
-ATOM    889  CE  LYS A 142      -8.252 -19.077   3.382  1.00 83.22           C  
-ATOM    890  NZ  LYS A 142      -7.620 -18.257   2.307  1.00 65.78           N  
-ATOM    891  N   ASP A 143      -6.026 -15.900   6.457  1.00 69.62           N  
-ATOM    892  CA  ASP A 143      -5.358 -14.684   6.928  1.00 79.91           C  
-ATOM    893  C   ASP A 143      -3.834 -14.823   6.755  1.00 69.16           C  
-ATOM    894  O   ASP A 143      -3.060 -13.925   7.097  1.00 65.05           O  
-ATOM    895  CB  ASP A 143      -5.773 -14.372   8.383  1.00 83.41           C  
-ATOM    896  CG  ASP A 143      -4.613 -14.403   9.362  1.00 98.80           C  
-ATOM    897  OD1 ASP A 143      -4.205 -15.502   9.798  1.00 78.66           O  
-ATOM    898  OD2 ASP A 143      -4.119 -13.310   9.709  1.00119.01           O  
-ATOM    899  N   SER A 144      -3.420 -15.939   6.162  1.00 60.33           N  
-ATOM    900  CA  SER A 144      -2.013 -16.213   5.908  1.00 52.98           C  
-ATOM    901  C   SER A 144      -1.703 -16.225   4.411  1.00 56.63           C  
-ATOM    902  O   SER A 144      -0.675 -15.702   3.979  1.00 51.55           O  
-ATOM    903  CB  SER A 144      -1.611 -17.548   6.539  1.00 56.35           C  
-ATOM    904  OG  SER A 144      -0.269 -17.879   6.232  1.00 51.90           O  
-ATOM    905  N   VAL A 145      -2.589 -16.824   3.620  1.00 63.85           N  
-ATOM    906  CA  VAL A 145      -2.372 -16.907   2.178  1.00 49.06           C  
-ATOM    907  C   VAL A 145      -3.385 -16.078   1.394  1.00 44.10           C  
-ATOM    908  O   VAL A 145      -4.527 -15.897   1.820  1.00 48.17           O  
-ATOM    909  CB  VAL A 145      -2.425 -18.366   1.675  1.00 44.75           C  
-ATOM    910  CG1 VAL A 145      -1.381 -19.211   2.388  1.00 52.55           C  
-ATOM    911  CG2 VAL A 145      -3.815 -18.957   1.863  1.00 50.25           C  
-ATOM    912  N   ASP A 146      -2.952 -15.568   0.245  1.00 43.76           N  
-ATOM    913  CA  ASP A 146      -3.832 -14.804  -0.630  1.00 50.51           C  
-ATOM    914  C   ASP A 146      -4.422 -15.713  -1.701  1.00 54.02           C  
-ATOM    915  O   ASP A 146      -5.552 -16.186  -1.573  1.00 51.05           O  
-ATOM    916  CB  ASP A 146      -3.079 -13.634  -1.277  1.00 51.56           C  
-ATOM    917  CG  ASP A 146      -4.008 -12.648  -1.981  1.00 57.30           C  
-ATOM    918  OD1 ASP A 146      -5.214 -12.943  -2.132  1.00 40.11           O  
-ATOM    919  OD2 ASP A 146      -3.525 -11.571  -2.393  1.00 62.31           O  
-ATOM    920  N   GLN A 147      -3.649 -15.957  -2.755  1.00 49.40           N  
-ATOM    921  CA  GLN A 147      -4.131 -16.746  -3.882  1.00 38.33           C  
-ATOM    922  C   GLN A 147      -3.596 -18.173  -3.871  1.00 36.89           C  
-ATOM    923  O   GLN A 147      -2.489 -18.442  -3.388  1.00 38.07           O  
-ATOM    924  CB  GLN A 147      -3.761 -16.070  -5.204  1.00 40.60           C  
-ATOM    925  CG  GLN A 147      -4.341 -14.677  -5.378  1.00 49.12           C  
-ATOM    926  CD  GLN A 147      -4.472 -14.281  -6.837  1.00 52.40           C  
-ATOM    927  OE1 GLN A 147      -3.699 -13.468  -7.344  1.00 44.30           O  
-ATOM    928  NE2 GLN A 147      -5.458 -14.853  -7.519  1.00 50.29           N  
-ATOM    929  N   ILE A 148      -4.400 -19.081  -4.414  1.00 38.01           N  
-ATOM    930  CA  ILE A 148      -4.018 -20.479  -4.536  1.00 32.60           C  
-ATOM    931  C   ILE A 148      -3.851 -20.856  -6.006  1.00 41.43           C  
-ATOM    932  O   ILE A 148      -4.763 -20.669  -6.815  1.00 49.47           O  
-ATOM    933  CB  ILE A 148      -5.057 -21.402  -3.881  1.00 29.60           C  
-ATOM    934  CG1 ILE A 148      -5.285 -20.995  -2.425  1.00 29.70           C  
-ATOM    935  CG2 ILE A 148      -4.614 -22.852  -3.978  1.00 32.26           C  
-ATOM    936  CD1 ILE A 148      -6.382 -21.775  -1.742  1.00 20.09           C  
-ATOM    937  N   PHE A 149      -2.674 -21.374  -6.344  1.00 33.46           N  
-ATOM    938  CA  PHE A 149      -2.352 -21.748  -7.713  1.00 26.70           C  
-ATOM    939  C   PHE A 149      -2.114 -23.249  -7.848  1.00 29.34           C  
-ATOM    940  O   PHE A 149      -1.218 -23.795  -7.208  1.00 29.94           O  
-ATOM    941  CB  PHE A 149      -1.106 -21.000  -8.202  1.00 27.22           C  
-ATOM    942  CG  PHE A 149      -1.271 -19.509  -8.280  1.00 29.05           C  
-ATOM    943  CD1 PHE A 149      -1.784 -18.914  -9.421  1.00 33.24           C  
-ATOM    944  CD2 PHE A 149      -0.890 -18.700  -7.223  1.00 33.16           C  
-ATOM    945  CE1 PHE A 149      -1.927 -17.537  -9.501  1.00 36.56           C  
-ATOM    946  CE2 PHE A 149      -1.031 -17.323  -7.296  1.00 38.27           C  
-ATOM    947  CZ  PHE A 149      -1.550 -16.742  -8.437  1.00 33.73           C  
-ATOM    948  N   VAL A 150      -2.912 -23.914  -8.678  1.00 31.58           N  
-ATOM    949  CA  VAL A 150      -2.620 -25.292  -9.054  1.00 28.04           C  
-ATOM    950  C   VAL A 150      -1.569 -25.272 -10.154  1.00 25.98           C  
-ATOM    951  O   VAL A 150      -1.735 -24.608 -11.190  1.00 30.49           O  
-ATOM    952  CB  VAL A 150      -3.868 -26.052  -9.527  1.00 28.48           C  
-ATOM    953  CG1 VAL A 150      -3.482 -27.430 -10.048  1.00 28.82           C  
-ATOM    954  CG2 VAL A 150      -4.866 -26.175  -8.394  1.00 24.82           C  
-ATOM    955  N   VAL A 151      -0.490 -26.011  -9.917  1.00 28.92           N  
-ATOM    956  CA  VAL A 151       0.733 -25.865 -10.693  1.00 27.97           C  
-ATOM    957  C   VAL A 151       1.071 -27.129 -11.498  1.00 31.07           C  
-ATOM    958  O   VAL A 151       1.781 -27.065 -12.503  1.00 31.66           O  
-ATOM    959  CB  VAL A 151       1.898 -25.477  -9.748  1.00 23.85           C  
-ATOM    960  CG1 VAL A 151       3.221 -25.460 -10.465  1.00 34.23           C  
-ATOM    961  CG2 VAL A 151       1.628 -24.116  -9.133  1.00 24.09           C  
-ATOM    962  N   GLY A 152       0.531 -28.270 -11.077  1.00 26.01           N  
-ATOM    963  CA  GLY A 152       0.700 -29.508 -11.820  1.00 22.01           C  
-ATOM    964  C   GLY A 152       0.577 -30.756 -10.965  1.00 25.81           C  
-ATOM    965  O   GLY A 152       0.630 -30.676  -9.743  1.00 38.72           O  
-ATOM    966  N   GLY A 153       0.407 -31.914 -11.598  1.00 24.17           N  
-ATOM    967  CA  GLY A 153       0.306 -32.009 -13.042  1.00 24.06           C  
-ATOM    968  C   GLY A 153      -1.078 -32.452 -13.469  1.00 21.85           C  
-ATOM    969  O   GLY A 153      -2.074 -31.944 -12.963  1.00 27.49           O  
-ATOM    970  N   ALA A 154      -1.136 -33.415 -14.384  1.00 19.10           N  
-ATOM    971  CA  ALA A 154      -2.396 -33.863 -14.974  1.00 21.16           C  
-ATOM    972  C   ALA A 154      -3.429 -34.279 -13.933  1.00 24.51           C  
-ATOM    973  O   ALA A 154      -4.614 -34.001 -14.088  1.00 28.15           O  
-ATOM    974  CB  ALA A 154      -2.139 -35.012 -15.936  1.00 27.92           C  
-ATOM    975  N   GLY A 155      -2.974 -34.943 -12.877  1.00 24.24           N  
-ATOM    976  CA  GLY A 155      -3.857 -35.376 -11.810  1.00 21.82           C  
-ATOM    977  C   GLY A 155      -4.509 -34.215 -11.088  1.00 27.65           C  
-ATOM    978  O   GLY A 155      -5.724 -34.200 -10.877  1.00 35.52           O  
-ATOM    979  N   LEU A 156      -3.701 -33.231 -10.711  1.00 26.00           N  
-ATOM    980  CA  LEU A 156      -4.220 -32.065 -10.006  1.00 31.85           C  
-ATOM    981  C   LEU A 156      -5.081 -31.181 -10.902  1.00 29.52           C  
-ATOM    982  O   LEU A 156      -6.051 -30.594 -10.434  1.00 25.61           O  
-ATOM    983  CB  LEU A 156      -3.085 -31.234  -9.411  1.00 24.89           C  
-ATOM    984  CG  LEU A 156      -2.407 -31.803  -8.165  1.00 25.63           C  
-ATOM    985  CD1 LEU A 156      -1.866 -30.671  -7.313  1.00 24.65           C  
-ATOM    986  CD2 LEU A 156      -3.357 -32.681  -7.365  1.00 27.32           C  
-ATOM    987  N   TYR A 157      -4.723 -31.074 -12.178  1.00 20.01           N  
-ATOM    988  CA  TYR A 157      -5.528 -30.307 -13.121  1.00 19.14           C  
-ATOM    989  C   TYR A 157      -6.888 -30.967 -13.290  1.00 26.93           C  
-ATOM    990  O   TYR A 157      -7.925 -30.303 -13.237  1.00 27.43           O  
-ATOM    991  CB  TYR A 157      -4.818 -30.187 -14.470  1.00 22.47           C  
-ATOM    992  CG  TYR A 157      -3.520 -29.412 -14.407  1.00 22.64           C  
-ATOM    993  CD1 TYR A 157      -3.405 -28.276 -13.620  1.00 19.98           C  
-ATOM    994  CD2 TYR A 157      -2.409 -29.824 -15.128  1.00 25.12           C  
-ATOM    995  CE1 TYR A 157      -2.223 -27.568 -13.559  1.00 23.82           C  
-ATOM    996  CE2 TYR A 157      -1.220 -29.129 -15.071  1.00 20.07           C  
-ATOM    997  CZ  TYR A 157      -1.133 -28.004 -14.284  1.00 21.93           C  
-ATOM    998  OH  TYR A 157       0.049 -27.309 -14.238  1.00 28.55           O  
-ATOM    999  N   GLU A 158      -6.862 -32.283 -13.486  1.00 28.08           N  
-ATOM   1000  CA  GLU A 158      -8.069 -33.095 -13.604  1.00 28.90           C  
-ATOM   1001  C   GLU A 158      -8.977 -32.924 -12.392  1.00 29.00           C  
-ATOM   1002  O   GLU A 158     -10.164 -32.632 -12.536  1.00 30.69           O  
-ATOM   1003  CB  GLU A 158      -7.701 -34.574 -13.777  1.00 27.92           C  
-ATOM   1004  CG  GLU A 158      -8.889 -35.528 -13.815  1.00 56.69           C  
-ATOM   1005  CD  GLU A 158      -9.492 -35.677 -15.204  1.00 68.73           C  
-ATOM   1006  OE1 GLU A 158      -9.933 -36.796 -15.545  1.00 87.20           O  
-ATOM   1007  OE2 GLU A 158      -9.527 -34.679 -15.956  1.00 56.52           O  
-ATOM   1008  N   ALA A 159      -8.408 -33.102 -11.202  1.00 25.00           N  
-ATOM   1009  CA  ALA A 159      -9.165 -32.976  -9.961  1.00 26.18           C  
-ATOM   1010  C   ALA A 159      -9.744 -31.575  -9.797  1.00 24.61           C  
-ATOM   1011  O   ALA A 159     -10.917 -31.418  -9.460  1.00 26.72           O  
-ATOM   1012  CB  ALA A 159      -8.288 -33.325  -8.772  1.00 34.03           C  
-ATOM   1013  N   ALA A 160      -8.912 -30.566 -10.037  1.00 22.37           N  
-ATOM   1014  CA  ALA A 160      -9.315 -29.171  -9.898  1.00 25.50           C  
-ATOM   1015  C   ALA A 160     -10.447 -28.812 -10.847  1.00 29.48           C  
-ATOM   1016  O   ALA A 160     -11.333 -28.032 -10.502  1.00 32.54           O  
-ATOM   1017  CB  ALA A 160      -8.128 -28.255 -10.132  1.00 23.50           C  
-ATOM   1018  N   LEU A 161     -10.408 -29.376 -12.048  1.00 34.00           N  
-ATOM   1019  CA  LEU A 161     -11.464 -29.145 -13.021  1.00 26.54           C  
-ATOM   1020  C   LEU A 161     -12.724 -29.902 -12.625  1.00 26.85           C  
-ATOM   1021  O   LEU A 161     -13.838 -29.449 -12.882  1.00 26.04           O  
-ATOM   1022  CB  LEU A 161     -11.003 -29.552 -14.420  1.00 29.78           C  
-ATOM   1023  CG  LEU A 161     -10.651 -28.394 -15.358  1.00 23.11           C  
-ATOM   1024  CD1 LEU A 161     -10.244 -27.159 -14.573  1.00 15.46           C  
-ATOM   1025  CD2 LEU A 161      -9.546 -28.802 -16.326  1.00 29.02           C  
-ATOM   1026  N   SER A 162     -12.539 -31.053 -11.987  1.00 31.35           N  
-ATOM   1027  CA  SER A 162     -13.660 -31.857 -11.514  1.00 33.04           C  
-ATOM   1028  C   SER A 162     -14.426 -31.128 -10.414  1.00 32.83           C  
-ATOM   1029  O   SER A 162     -15.648 -31.008 -10.474  1.00 39.34           O  
-ATOM   1030  CB  SER A 162     -13.173 -33.218 -11.011  1.00 34.81           C  
-ATOM   1031  OG  SER A 162     -12.669 -34.006 -12.077  1.00 54.36           O  
-ATOM   1032  N   LEU A 163     -13.698 -30.630  -9.420  1.00 28.96           N  
-ATOM   1033  CA  LEU A 163     -14.297 -29.920  -8.296  1.00 28.69           C  
-ATOM   1034  C   LEU A 163     -14.960 -28.616  -8.723  1.00 28.47           C  
-ATOM   1035  O   LEU A 163     -15.825 -28.100  -8.021  1.00 39.17           O  
-ATOM   1036  CB  LEU A 163     -13.240 -29.633  -7.227  1.00 26.87           C  
-ATOM   1037  CG  LEU A 163     -12.475 -30.856  -6.725  1.00 28.88           C  
-ATOM   1038  CD1 LEU A 163     -11.449 -30.463  -5.673  1.00 35.24           C  
-ATOM   1039  CD2 LEU A 163     -13.447 -31.893  -6.188  1.00 32.12           C  
-ATOM   1040  N   GLY A 164     -14.544 -28.081  -9.867  1.00 33.78           N  
-ATOM   1041  CA  GLY A 164     -15.104 -26.840 -10.370  1.00 40.77           C  
-ATOM   1042  C   GLY A 164     -14.613 -25.633  -9.595  1.00 43.54           C  
-ATOM   1043  O   GLY A 164     -15.219 -24.562  -9.636  1.00 56.34           O  
-ATOM   1044  N   VAL A 165     -13.503 -25.812  -8.888  1.00 37.15           N  
-ATOM   1045  CA  VAL A 165     -12.940 -24.762  -8.049  1.00 42.53           C  
-ATOM   1046  C   VAL A 165     -12.110 -23.770  -8.862  1.00 41.16           C  
-ATOM   1047  O   VAL A 165     -11.760 -22.692  -8.378  1.00 41.97           O  
-ATOM   1048  CB  VAL A 165     -12.066 -25.360  -6.931  1.00 38.40           C  
-ATOM   1049  CG1 VAL A 165     -12.941 -25.945  -5.836  1.00 45.27           C  
-ATOM   1050  CG2 VAL A 165     -11.139 -26.426  -7.493  1.00 29.96           C  
-ATOM   1051  N   ALA A 166     -11.806 -24.141 -10.102  1.00 34.39           N  
-ATOM   1052  CA  ALA A 166     -10.960 -23.323 -10.965  1.00 34.11           C  
-ATOM   1053  C   ALA A 166     -11.712 -22.126 -11.535  1.00 36.50           C  
-ATOM   1054  O   ALA A 166     -12.665 -22.282 -12.298  1.00 39.04           O  
-ATOM   1055  CB  ALA A 166     -10.390 -24.168 -12.089  1.00 40.72           C  
-ATOM   1056  N   SER A 167     -11.265 -20.930 -11.169  1.00 29.80           N  
-ATOM   1057  CA  SER A 167     -11.887 -19.702 -11.646  1.00 28.32           C  
-ATOM   1058  C   SER A 167     -11.200 -19.179 -12.903  1.00 34.78           C  
-ATOM   1059  O   SER A 167     -11.860 -18.722 -13.841  1.00 41.71           O  
-ATOM   1060  CB  SER A 167     -11.860 -18.636 -10.551  1.00 27.68           C  
-ATOM   1061  OG  SER A 167     -10.533 -18.343 -10.157  1.00 30.64           O  
-ATOM   1062  N   HIS A 168      -9.872 -19.248 -12.913  1.00 32.12           N  
-ATOM   1063  CA  HIS A 168      -9.083 -18.760 -14.038  1.00 29.43           C  
-ATOM   1064  C   HIS A 168      -7.989 -19.737 -14.452  1.00 30.77           C  
-ATOM   1065  O   HIS A 168      -7.401 -20.418 -13.611  1.00 33.08           O  
-ATOM   1066  CB  HIS A 168      -8.457 -17.408 -13.700  1.00 28.01           C  
-ATOM   1067  CG  HIS A 168      -9.459 -16.324 -13.459  1.00 40.48           C  
-ATOM   1068  ND1 HIS A 168     -10.000 -16.073 -12.217  1.00 50.96           N  
-ATOM   1069  CD2 HIS A 168     -10.024 -15.429 -14.304  1.00 45.39           C  
-ATOM   1070  CE1 HIS A 168     -10.851 -15.067 -12.305  1.00 51.00           C  
-ATOM   1071  NE2 HIS A 168     -10.884 -14.658 -13.561  1.00 44.59           N  
-ATOM   1072  N   LEU A 169      -7.716 -19.794 -15.752  1.00 24.76           N  
-ATOM   1073  CA  LEU A 169      -6.622 -20.612 -16.262  1.00 21.22           C  
-ATOM   1074  C   LEU A 169      -5.535 -19.742 -16.887  1.00 24.70           C  
-ATOM   1075  O   LEU A 169      -5.778 -19.056 -17.876  1.00 27.51           O  
-ATOM   1076  CB  LEU A 169      -7.127 -21.622 -17.295  1.00 15.48           C  
-ATOM   1077  CG  LEU A 169      -8.317 -22.510 -16.935  1.00 23.01           C  
-ATOM   1078  CD1 LEU A 169      -8.515 -23.578 -18.001  1.00 19.47           C  
-ATOM   1079  CD2 LEU A 169      -8.140 -23.144 -15.566  1.00 34.29           C  
-ATOM   1080  N   TYR A 170      -4.339 -19.767 -16.309  1.00 22.90           N  
-ATOM   1081  CA  TYR A 170      -3.197 -19.084 -16.908  1.00 14.83           C  
-ATOM   1082  C   TYR A 170      -2.478 -20.029 -17.858  1.00 17.90           C  
-ATOM   1083  O   TYR A 170      -1.572 -20.755 -17.452  1.00 20.76           O  
-ATOM   1084  CB  TYR A 170      -2.234 -18.580 -15.833  1.00 16.98           C  
-ATOM   1085  CG  TYR A 170      -2.780 -17.442 -15.003  1.00 25.81           C  
-ATOM   1086  CD1 TYR A 170      -3.491 -17.688 -13.835  1.00 34.37           C  
-ATOM   1087  CD2 TYR A 170      -2.583 -16.120 -15.383  1.00 26.49           C  
-ATOM   1088  CE1 TYR A 170      -3.993 -16.650 -13.072  1.00 29.32           C  
-ATOM   1089  CE2 TYR A 170      -3.081 -15.079 -14.628  1.00 24.04           C  
-ATOM   1090  CZ  TYR A 170      -3.784 -15.348 -13.475  1.00 24.57           C  
-ATOM   1091  OH  TYR A 170      -4.275 -14.306 -12.724  1.00 24.80           O  
-ATOM   1092  N   ILE A 171      -2.880 -20.024 -19.125  1.00 16.23           N  
-ATOM   1093  CA  ILE A 171      -2.342 -20.989 -20.079  1.00 14.43           C  
-ATOM   1094  C   ILE A 171      -1.275 -20.392 -20.983  1.00 16.49           C  
-ATOM   1095  O   ILE A 171      -1.503 -19.383 -21.647  1.00 14.98           O  
-ATOM   1096  CB  ILE A 171      -3.449 -21.585 -20.970  1.00 16.00           C  
-ATOM   1097  CG1 ILE A 171      -4.549 -22.218 -20.116  1.00 15.15           C  
-ATOM   1098  CG2 ILE A 171      -2.858 -22.603 -21.937  1.00 19.06           C  
-ATOM   1099  CD1 ILE A 171      -5.563 -22.995 -20.919  1.00 11.30           C  
-ATOM   1100  N   THR A 172      -0.109 -21.029 -21.006  1.00 16.19           N  
-ATOM   1101  CA  THR A 172       0.942 -20.650 -21.935  1.00 16.18           C  
-ATOM   1102  C   THR A 172       0.901 -21.568 -23.151  1.00 15.99           C  
-ATOM   1103  O   THR A 172       1.476 -22.656 -23.136  1.00 19.67           O  
-ATOM   1104  CB  THR A 172       2.339 -20.713 -21.285  1.00 22.01           C  
-ATOM   1105  OG1 THR A 172       2.370 -19.876 -20.123  1.00 18.63           O  
-ATOM   1106  CG2 THR A 172       3.405 -20.244 -22.263  1.00 24.24           C  
-ATOM   1107  N   ARG A 173       0.205 -21.125 -24.195  1.00 16.61           N  
-ATOM   1108  CA  ARG A 173       0.085 -21.896 -25.429  1.00 20.08           C  
-ATOM   1109  C   ARG A 173       1.407 -21.983 -26.167  1.00 17.94           C  
-ATOM   1110  O   ARG A 173       1.868 -20.998 -26.748  1.00 17.67           O  
-ATOM   1111  CB  ARG A 173      -0.967 -21.283 -26.355  1.00 16.58           C  
-ATOM   1112  CG  ARG A 173      -2.333 -21.140 -25.727  1.00 17.89           C  
-ATOM   1113  CD  ARG A 173      -2.982 -19.852 -26.173  1.00 19.42           C  
-ATOM   1114  NE  ARG A 173      -3.797 -20.011 -27.369  1.00 16.09           N  
-ATOM   1115  CZ  ARG A 173      -4.017 -19.043 -28.251  1.00 16.90           C  
-ATOM   1116  NH1 ARG A 173      -3.465 -17.849 -28.086  1.00 13.96           N  
-ATOM   1117  NH2 ARG A 173      -4.778 -19.274 -29.309  1.00 26.23           N  
-ATOM   1118  N   VAL A 174       2.006 -23.169 -26.124  1.00 18.24           N  
-ATOM   1119  CA  VAL A 174       3.176 -23.495 -26.926  1.00 17.02           C  
-ATOM   1120  C   VAL A 174       2.706 -23.890 -28.320  1.00 18.52           C  
-ATOM   1121  O   VAL A 174       1.848 -24.756 -28.457  1.00 23.49           O  
-ATOM   1122  CB  VAL A 174       3.987 -24.639 -26.299  1.00 18.81           C  
-ATOM   1123  CG1 VAL A 174       5.189 -24.978 -27.160  1.00 17.66           C  
-ATOM   1124  CG2 VAL A 174       4.410 -24.269 -24.881  1.00 14.39           C  
-ATOM   1125  N   ALA A 175       3.252 -23.256 -29.353  1.00 17.99           N  
-ATOM   1126  CA  ALA A 175       2.741 -23.450 -30.711  1.00 19.29           C  
-ATOM   1127  C   ALA A 175       3.235 -24.738 -31.371  1.00 17.66           C  
-ATOM   1128  O   ALA A 175       2.544 -25.309 -32.212  1.00 16.17           O  
-ATOM   1129  CB  ALA A 175       3.098 -22.254 -31.579  1.00 21.24           C  
-ATOM   1130  N   ARG A 176       4.431 -25.184 -31.000  1.00 17.26           N  
-ATOM   1131  CA  ARG A 176       5.005 -26.398 -31.575  1.00 15.13           C  
-ATOM   1132  C   ARG A 176       4.478 -27.648 -30.895  1.00 19.02           C  
-ATOM   1133  O   ARG A 176       4.111 -27.624 -29.722  1.00 23.31           O  
-ATOM   1134  CB  ARG A 176       6.525 -26.387 -31.467  1.00 22.26           C  
-ATOM   1135  CG  ARG A 176       7.209 -25.337 -32.303  1.00 22.79           C  
-ATOM   1136  CD  ARG A 176       8.712 -25.415 -32.119  1.00 22.97           C  
-ATOM   1137  NE  ARG A 176       9.228 -26.750 -32.410  1.00 23.91           N  
-ATOM   1138  CZ  ARG A 176      10.519 -27.063 -32.430  1.00 31.39           C  
-ATOM   1139  NH1 ARG A 176      10.897 -28.303 -32.703  1.00 46.89           N  
-ATOM   1140  NH2 ARG A 176      11.434 -26.135 -32.179  1.00 26.34           N  
-ATOM   1141  N   GLU A 177       4.453 -28.747 -31.635  1.00 21.88           N  
-ATOM   1142  CA  GLU A 177       4.082 -30.025 -31.056  1.00 19.92           C  
-ATOM   1143  C   GLU A 177       5.338 -30.767 -30.610  1.00 28.75           C  
-ATOM   1144  O   GLU A 177       6.347 -30.786 -31.316  1.00 39.32           O  
-ATOM   1145  CB  GLU A 177       3.281 -30.861 -32.052  1.00 27.69           C  
-ATOM   1146  CG  GLU A 177       2.438 -31.929 -31.387  1.00 32.38           C  
-ATOM   1147  CD  GLU A 177       1.672 -31.391 -30.193  1.00 35.58           C  
-ATOM   1148  OE1 GLU A 177       0.745 -30.575 -30.394  1.00 36.21           O  
-ATOM   1149  OE2 GLU A 177       2.010 -31.776 -29.053  1.00 31.28           O  
-ATOM   1150  N   PHE A 178       5.276 -31.358 -29.423  1.00 30.24           N  
-ATOM   1151  CA  PHE A 178       6.403 -32.096 -28.873  1.00 19.32           C  
-ATOM   1152  C   PHE A 178       5.952 -33.458 -28.364  1.00 23.59           C  
-ATOM   1153  O   PHE A 178       4.782 -33.636 -28.022  1.00 21.95           O  
-ATOM   1154  CB  PHE A 178       7.067 -31.303 -27.742  1.00 21.94           C  
-ATOM   1155  CG  PHE A 178       7.869 -30.125 -28.213  1.00 25.06           C  
-ATOM   1156  CD1 PHE A 178       9.197 -30.277 -28.578  1.00 32.05           C  
-ATOM   1157  CD2 PHE A 178       7.302 -28.865 -28.281  1.00 26.74           C  
-ATOM   1158  CE1 PHE A 178       9.941 -29.194 -29.008  1.00 31.84           C  
-ATOM   1159  CE2 PHE A 178       8.041 -27.779 -28.709  1.00 27.03           C  
-ATOM   1160  CZ  PHE A 178       9.361 -27.944 -29.075  1.00 30.00           C  
-ATOM   1161  N   PRO A 179       6.878 -34.429 -28.328  1.00 22.91           N  
-ATOM   1162  CA  PRO A 179       6.599 -35.737 -27.726  1.00 26.28           C  
-ATOM   1163  C   PRO A 179       6.137 -35.601 -26.277  1.00 21.76           C  
-ATOM   1164  O   PRO A 179       6.829 -34.977 -25.473  1.00 19.54           O  
-ATOM   1165  CB  PRO A 179       7.949 -36.454 -27.810  1.00 20.80           C  
-ATOM   1166  CG  PRO A 179       8.619 -35.830 -28.986  1.00 20.55           C  
-ATOM   1167  CD  PRO A 179       8.206 -34.388 -28.966  1.00 14.49           C  
-ATOM   1168  N   CYS A 180       4.981 -36.174 -25.954  1.00 21.61           N  
-ATOM   1169  CA  CYS A 180       4.408 -36.039 -24.617  1.00 24.15           C  
-ATOM   1170  C   CYS A 180       3.728 -37.312 -24.125  1.00 22.93           C  
-ATOM   1171  O   CYS A 180       3.055 -38.004 -24.887  1.00 26.72           O  
-ATOM   1172  CB  CYS A 180       3.402 -34.888 -24.592  1.00 20.99           C  
-ATOM   1173  SG  CYS A 180       4.136 -33.265 -24.827  1.00 22.06           S  
-ATOM   1174  N   ASP A 181       3.901 -37.609 -22.841  1.00 19.65           N  
-ATOM   1175  CA  ASP A 181       3.242 -38.756 -22.230  1.00 22.19           C  
-ATOM   1176  C   ASP A 181       2.239 -38.308 -21.168  1.00 23.27           C  
-ATOM   1177  O   ASP A 181       1.530 -39.126 -20.582  1.00 21.08           O  
-ATOM   1178  CB  ASP A 181       4.274 -39.720 -21.628  1.00 22.02           C  
-ATOM   1179  CG  ASP A 181       5.273 -39.026 -20.712  1.00 25.31           C  
-ATOM   1180  OD1 ASP A 181       4.914 -38.018 -20.071  1.00 36.69           O  
-ATOM   1181  OD2 ASP A 181       6.427 -39.497 -20.626  1.00 23.26           O  
-ATOM   1182  N   VAL A 182       2.189 -37.003 -20.921  1.00 21.08           N  
-ATOM   1183  CA  VAL A 182       1.249 -36.434 -19.959  1.00 22.24           C  
-ATOM   1184  C   VAL A 182       0.550 -35.215 -20.555  1.00 16.14           C  
-ATOM   1185  O   VAL A 182       1.202 -34.291 -21.039  1.00 14.46           O  
-ATOM   1186  CB  VAL A 182       1.952 -36.033 -18.645  1.00 30.04           C  
-ATOM   1187  CG1 VAL A 182       0.988 -35.296 -17.729  1.00 24.92           C  
-ATOM   1188  CG2 VAL A 182       2.520 -37.260 -17.947  1.00 25.39           C  
-ATOM   1189  N   PHE A 183      -0.779 -35.215 -20.512  1.00 16.03           N  
-ATOM   1190  CA  PHE A 183      -1.569 -34.189 -21.184  1.00 15.16           C  
-ATOM   1191  C   PHE A 183      -2.510 -33.446 -20.241  1.00 20.09           C  
-ATOM   1192  O   PHE A 183      -3.039 -34.024 -19.293  1.00 29.56           O  
-ATOM   1193  CB  PHE A 183      -2.387 -34.810 -22.319  1.00 14.54           C  
-ATOM   1194  CG  PHE A 183      -1.554 -35.433 -23.401  1.00 13.52           C  
-ATOM   1195  CD1 PHE A 183      -1.036 -36.706 -23.250  1.00 15.31           C  
-ATOM   1196  CD2 PHE A 183      -1.297 -34.748 -24.574  1.00 16.24           C  
-ATOM   1197  CE1 PHE A 183      -0.268 -37.279 -24.246  1.00 22.58           C  
-ATOM   1198  CE2 PHE A 183      -0.532 -35.314 -25.573  1.00 18.03           C  
-ATOM   1199  CZ  PHE A 183      -0.018 -36.582 -25.409  1.00 19.72           C  
-ATOM   1200  N   PHE A 184      -2.717 -32.161 -20.513  1.00 21.19           N  
-ATOM   1201  CA  PHE A 184      -3.726 -31.384 -19.806  1.00 20.83           C  
-ATOM   1202  C   PHE A 184      -5.095 -31.898 -20.235  1.00 27.52           C  
-ATOM   1203  O   PHE A 184      -5.311 -32.164 -21.417  1.00 26.34           O  
-ATOM   1204  CB  PHE A 184      -3.577 -29.889 -20.106  1.00 17.76           C  
-ATOM   1205  CG  PHE A 184      -4.404 -29.002 -19.217  1.00 23.27           C  
-ATOM   1206  CD1 PHE A 184      -3.914 -28.577 -17.992  1.00 23.65           C  
-ATOM   1207  CD2 PHE A 184      -5.668 -28.587 -19.606  1.00 22.13           C  
-ATOM   1208  CE1 PHE A 184      -4.669 -27.761 -17.171  1.00 18.54           C  
-ATOM   1209  CE2 PHE A 184      -6.427 -27.771 -18.787  1.00 20.86           C  
-ATOM   1210  CZ  PHE A 184      -5.926 -27.357 -17.568  1.00 19.51           C  
-ATOM   1211  N   PRO A 185      -6.022 -32.054 -19.276  1.00 29.37           N  
-ATOM   1212  CA  PRO A 185      -7.325 -32.658 -19.579  1.00 23.63           C  
-ATOM   1213  C   PRO A 185      -8.136 -31.873 -20.610  1.00 25.25           C  
-ATOM   1214  O   PRO A 185      -7.810 -30.726 -20.926  1.00 18.40           O  
-ATOM   1215  CB  PRO A 185      -8.033 -32.659 -18.219  1.00 19.25           C  
-ATOM   1216  CG  PRO A 185      -7.341 -31.603 -17.424  1.00 15.01           C  
-ATOM   1217  CD  PRO A 185      -5.914 -31.665 -17.859  1.00 18.74           C  
-ATOM   1218  N   ALA A 186      -9.180 -32.506 -21.136  1.00 25.90           N  
-ATOM   1219  CA  ALA A 186     -10.083 -31.846 -22.067  1.00 21.35           C  
-ATOM   1220  C   ALA A 186     -11.067 -30.985 -21.291  1.00 20.70           C  
-ATOM   1221  O   ALA A 186     -11.723 -31.459 -20.366  1.00 31.76           O  
-ATOM   1222  CB  ALA A 186     -10.818 -32.866 -22.922  1.00 22.75           C  
-ATOM   1223  N   PHE A 187     -11.158 -29.714 -21.663  1.00 23.77           N  
-ATOM   1224  CA  PHE A 187     -12.041 -28.785 -20.973  1.00 24.71           C  
-ATOM   1225  C   PHE A 187     -12.853 -27.973 -21.973  1.00 27.98           C  
-ATOM   1226  O   PHE A 187     -12.358 -27.646 -23.049  1.00 33.75           O  
-ATOM   1227  CB  PHE A 187     -11.235 -27.859 -20.060  1.00 22.82           C  
-ATOM   1228  CG  PHE A 187     -10.256 -26.983 -20.790  1.00 26.13           C  
-ATOM   1229  CD1 PHE A 187      -8.974 -27.430 -21.061  1.00 22.91           C  
-ATOM   1230  CD2 PHE A 187     -10.614 -25.706 -21.194  1.00 27.01           C  
-ATOM   1231  CE1 PHE A 187      -8.072 -26.624 -21.726  1.00 24.48           C  
-ATOM   1232  CE2 PHE A 187      -9.715 -24.898 -21.861  1.00 18.84           C  
-ATOM   1233  CZ  PHE A 187      -8.443 -25.356 -22.126  1.00 18.91           C  
-ATOM   1234  N   PRO A 188     -14.106 -27.645 -21.620  1.00 25.65           N  
-ATOM   1235  CA  PRO A 188     -14.968 -26.854 -22.506  1.00 31.78           C  
-ATOM   1236  C   PRO A 188     -14.341 -25.510 -22.862  1.00 29.30           C  
-ATOM   1237  O   PRO A 188     -14.080 -24.690 -21.981  1.00 34.44           O  
-ATOM   1238  CB  PRO A 188     -16.248 -26.665 -21.680  1.00 32.78           C  
-ATOM   1239  CG  PRO A 188     -15.845 -26.921 -20.271  1.00 28.75           C  
-ATOM   1240  CD  PRO A 188     -14.775 -27.963 -20.350  1.00 33.36           C  
-ATOM   1241  N   GLY A 189     -14.090 -25.301 -24.148  1.00 25.64           N  
-ATOM   1242  CA  GLY A 189     -13.485 -24.069 -24.608  1.00 33.79           C  
-ATOM   1243  C   GLY A 189     -12.004 -24.230 -24.880  1.00 34.32           C  
-ATOM   1244  O   GLY A 189     -11.270 -23.247 -24.913  1.00 34.58           O  
-ATOM   1245  N   ASP A 190     -11.565 -25.470 -25.086  1.00 27.94           N  
-ATOM   1246  CA  ASP A 190     -10.167 -25.746 -25.407  1.00 21.16           C  
-ATOM   1247  C   ASP A 190      -9.853 -25.452 -26.876  1.00 22.67           C  
-ATOM   1248  O   ASP A 190      -8.756 -25.732 -27.360  1.00 30.39           O  
-ATOM   1249  CB  ASP A 190      -9.821 -27.196 -25.073  1.00 21.23           C  
-ATOM   1250  CG  ASP A 190     -10.881 -28.167 -25.536  1.00 27.52           C  
-ATOM   1251  OD1 ASP A 190     -11.795 -27.743 -26.276  1.00 37.58           O  
-ATOM   1252  OD2 ASP A 190     -10.801 -29.354 -25.159  1.00 24.86           O  
-ATOM   1253  N   ASP A 191     -10.821 -24.865 -27.574  1.00 24.71           N  
-ATOM   1254  CA  ASP A 191     -10.655 -24.483 -28.972  1.00 20.80           C  
-ATOM   1255  C   ASP A 191      -9.559 -23.432 -29.148  1.00 33.15           C  
-ATOM   1256  O   ASP A 191      -9.127 -23.161 -30.267  1.00 37.02           O  
-ATOM   1257  CB  ASP A 191     -11.979 -23.961 -29.539  1.00 14.71           C  
-ATOM   1258  N   ILE A 192      -9.110 -22.843 -28.040  1.00 27.28           N  
-ATOM   1259  CA  ILE A 192      -8.001 -21.890 -28.065  1.00 27.93           C  
-ATOM   1260  C   ILE A 192      -6.658 -22.592 -28.229  1.00 27.35           C  
-ATOM   1261  O   ILE A 192      -5.615 -21.945 -28.286  1.00 30.48           O  
-ATOM   1262  CB  ILE A 192      -7.949 -21.033 -26.784  1.00 23.95           C  
-ATOM   1263  CG1 ILE A 192      -8.638 -21.753 -25.629  1.00 22.36           C  
-ATOM   1264  CG2 ILE A 192      -8.608 -19.688 -27.011  1.00 28.02           C  
-ATOM   1265  CD1 ILE A 192      -7.814 -22.844 -24.998  1.00 24.53           C  
-ATOM   1266  N   LEU A 193      -6.689 -23.918 -28.297  1.00 24.81           N  
-ATOM   1267  CA  LEU A 193      -5.475 -24.706 -28.472  1.00 21.16           C  
-ATOM   1268  C   LEU A 193      -5.346 -25.214 -29.905  1.00 22.83           C  
-ATOM   1269  O   LEU A 193      -4.382 -24.897 -30.602  1.00 31.49           O  
-ATOM   1270  CB  LEU A 193      -5.463 -25.875 -27.490  1.00 19.83           C  
-ATOM   1271  CG  LEU A 193      -5.567 -25.457 -26.021  1.00 25.47           C  
-ATOM   1272  CD1 LEU A 193      -5.923 -26.641 -25.143  1.00 24.83           C  
-ATOM   1273  CD2 LEU A 193      -4.280 -24.796 -25.543  1.00 18.81           C  
-ATOM   1274  N   SER A 194      -6.317 -26.009 -30.339  1.00 21.06           N  
-ATOM   1275  CA  SER A 194      -6.330 -26.524 -31.702  1.00 21.39           C  
-ATOM   1276  C   SER A 194      -7.759 -26.627 -32.220  1.00 28.50           C  
-ATOM   1277  O   SER A 194      -8.708 -26.254 -31.527  1.00 24.78           O  
-ATOM   1278  CB  SER A 194      -5.642 -27.889 -31.773  1.00 31.43           C  
-ATOM   1279  OG  SER A 194      -6.327 -28.853 -30.988  1.00 36.43           O  
-ATOM   1280  N   ASN A 195      -7.908 -27.126 -33.442  1.00 25.19           N  
-ATOM   1281  CA  ASN A 195      -9.227 -27.302 -34.034  1.00 17.41           C  
-ATOM   1282  C   ASN A 195      -9.906 -28.566 -33.523  1.00 21.31           C  
-ATOM   1283  O   ASN A 195      -9.255 -29.587 -33.304  1.00 25.77           O  
-ATOM   1284  CB  ASN A 195      -9.127 -27.336 -35.560  1.00 18.06           C  
-ATOM   1285  CG  ASN A 195      -8.805 -25.977 -36.154  1.00 27.45           C  
-ATOM   1286  OD1 ASN A 195      -8.531 -25.017 -35.432  1.00 28.31           O  
-ATOM   1287  ND2 ASN A 195      -8.836 -25.890 -37.478  1.00 27.82           N  
-ATOM   1288  N   LYS A 196     -11.218 -28.492 -33.330  1.00 22.53           N  
-ATOM   1289  CA  LYS A 196     -11.990 -29.646 -32.883  1.00 34.84           C  
-ATOM   1290  C   LYS A 196     -12.580 -30.415 -34.063  1.00 43.69           C  
-ATOM   1291  O   LYS A 196     -12.567 -31.649 -34.084  1.00 46.52           O  
-ATOM   1292  CB  LYS A 196     -13.105 -29.208 -31.932  1.00 36.39           C  
-ATOM   1293  CG  LYS A 196     -12.638 -28.902 -30.518  1.00 23.72           C  
-ATOM   1294  CD  LYS A 196     -11.940 -30.105 -29.906  1.00 24.32           C  
-ATOM   1295  CE  LYS A 196     -12.116 -30.136 -28.396  1.00 23.10           C  
-ATOM   1296  NZ  LYS A 196     -13.546 -30.290 -28.010  1.00 13.59           N  
-ATOM   1297  N   ALA A 225     -20.687 -25.065 -17.752  1.00 42.26           N  
-ATOM   1298  CA  ALA A 225     -19.868 -23.858 -17.691  1.00 55.78           C  
-ATOM   1299  C   ALA A 225     -18.612 -23.986 -18.550  1.00 53.67           C  
-ATOM   1300  O   ALA A 225     -17.892 -24.982 -18.469  1.00 42.03           O  
-ATOM   1301  CB  ALA A 225     -19.491 -23.550 -16.250  1.00 64.43           C  
-ATOM   1302  N   THR A 226     -18.352 -22.969 -19.368  1.00 52.30           N  
-ATOM   1303  CA  THR A 226     -17.192 -22.977 -20.254  1.00 45.04           C  
-ATOM   1304  C   THR A 226     -16.114 -21.998 -19.790  1.00 38.13           C  
-ATOM   1305  O   THR A 226     -16.392 -21.051 -19.053  1.00 40.44           O  
-ATOM   1306  CB  THR A 226     -17.589 -22.630 -21.705  1.00 44.23           C  
-ATOM   1307  OG1 THR A 226     -16.427 -22.657 -22.544  1.00 40.75           O  
-ATOM   1308  CG2 THR A 226     -18.225 -21.251 -21.771  1.00 49.46           C  
-ATOM   1309  N   TYR A 227     -14.881 -22.242 -20.226  1.00 33.82           N  
-ATOM   1310  CA  TYR A 227     -13.753 -21.378 -19.894  1.00 34.82           C  
-ATOM   1311  C   TYR A 227     -13.389 -20.482 -21.076  1.00 41.78           C  
-ATOM   1312  O   TYR A 227     -12.711 -20.923 -22.007  1.00 38.15           O  
-ATOM   1313  CB  TYR A 227     -12.541 -22.216 -19.476  1.00 31.29           C  
-ATOM   1314  CG  TYR A 227     -12.687 -22.908 -18.137  1.00 31.25           C  
-ATOM   1315  CD1 TYR A 227     -13.296 -24.152 -18.034  1.00 25.76           C  
-ATOM   1316  CD2 TYR A 227     -12.203 -22.318 -16.975  1.00 32.67           C  
-ATOM   1317  CE1 TYR A 227     -13.425 -24.786 -16.809  1.00 34.16           C  
-ATOM   1318  CE2 TYR A 227     -12.328 -22.942 -15.748  1.00 32.00           C  
-ATOM   1319  CZ  TYR A 227     -12.938 -24.175 -15.669  1.00 37.33           C  
-ATOM   1320  OH  TYR A 227     -13.062 -24.792 -14.443  1.00 36.70           O  
-ATOM   1321  N   ARG A 228     -13.831 -19.227 -21.039  1.00 40.95           N  
-ATOM   1322  CA  ARG A 228     -13.613 -18.320 -22.168  1.00 36.40           C  
-ATOM   1323  C   ARG A 228     -12.420 -17.393 -21.953  1.00 34.01           C  
-ATOM   1324  O   ARG A 228     -12.170 -16.947 -20.837  1.00 34.47           O  
-ATOM   1325  CB  ARG A 228     -14.870 -17.488 -22.441  1.00 34.98           C  
-ATOM   1326  CG  ARG A 228     -15.992 -18.259 -23.120  1.00 51.38           C  
-ATOM   1327  CD  ARG A 228     -16.919 -17.322 -23.878  1.00 53.89           C  
-ATOM   1328  NE  ARG A 228     -17.309 -16.170 -23.070  1.00 74.27           N  
-ATOM   1329  CZ  ARG A 228     -18.309 -16.176 -22.194  1.00 82.12           C  
-ATOM   1330  NH1 ARG A 228     -19.023 -17.279 -22.008  1.00 75.69           N  
-ATOM   1331  NH2 ARG A 228     -18.594 -15.080 -21.502  1.00 59.50           N  
-ATOM   1332  N   PRO A 229     -11.678 -17.099 -23.033  1.00 35.60           N  
-ATOM   1333  CA  PRO A 229     -10.506 -16.222 -22.954  1.00 27.23           C  
-ATOM   1334  C   PRO A 229     -10.878 -14.763 -22.729  1.00 31.75           C  
-ATOM   1335  O   PRO A 229     -11.896 -14.294 -23.240  1.00 30.98           O  
-ATOM   1336  CB  PRO A 229      -9.841 -16.409 -24.318  1.00 28.82           C  
-ATOM   1337  CG  PRO A 229     -10.954 -16.767 -25.222  1.00 37.36           C  
-ATOM   1338  CD  PRO A 229     -11.893 -17.602 -24.400  1.00 37.12           C  
-ATOM   1339  N   ILE A 230     -10.051 -14.057 -21.966  1.00 37.06           N  
-ATOM   1340  CA  ILE A 230     -10.293 -12.651 -21.669  1.00 32.04           C  
-ATOM   1341  C   ILE A 230      -9.012 -11.858 -21.950  1.00 31.09           C  
-ATOM   1342  O   ILE A 230      -8.987 -10.623 -21.911  1.00 34.21           O  
-ATOM   1343  CB  ILE A 230     -10.747 -12.467 -20.199  1.00 28.67           C  
-ATOM   1344  CG1 ILE A 230     -11.570 -11.189 -20.039  1.00 60.49           C  
-ATOM   1345  CG2 ILE A 230      -9.552 -12.511 -19.247  1.00 19.48           C  
-ATOM   1346  CD1 ILE A 230     -13.044 -11.432 -19.744  1.00 61.24           C  
-ATOM   1347  N   PHE A 231      -7.961 -12.605 -22.273  1.00 30.40           N  
-ATOM   1348  CA  PHE A 231      -6.605 -12.091 -22.392  1.00 25.36           C  
-ATOM   1349  C   PHE A 231      -5.872 -12.907 -23.451  1.00 28.31           C  
-ATOM   1350  O   PHE A 231      -5.780 -14.126 -23.330  1.00 32.36           O  
-ATOM   1351  CB  PHE A 231      -5.897 -12.183 -21.030  1.00 26.80           C  
-ATOM   1352  CG  PHE A 231      -4.473 -11.675 -21.018  1.00 30.95           C  
-ATOM   1353  CD1 PHE A 231      -3.451 -12.382 -21.634  1.00 25.80           C  
-ATOM   1354  CD2 PHE A 231      -4.151 -10.516 -20.335  1.00 34.56           C  
-ATOM   1355  CE1 PHE A 231      -2.150 -11.920 -21.607  1.00 26.67           C  
-ATOM   1356  CE2 PHE A 231      -2.849 -10.053 -20.295  1.00 29.79           C  
-ATOM   1357  CZ  PHE A 231      -1.848 -10.755 -20.935  1.00 29.10           C  
-ATOM   1358  N   ILE A 232      -5.362 -12.250 -24.489  1.00 27.80           N  
-ATOM   1359  CA  ILE A 232      -4.512 -12.930 -25.469  1.00 18.54           C  
-ATOM   1360  C   ILE A 232      -3.334 -12.036 -25.854  1.00 20.00           C  
-ATOM   1361  O   ILE A 232      -3.520 -10.974 -26.448  1.00 25.40           O  
-ATOM   1362  CB  ILE A 232      -5.288 -13.329 -26.743  1.00 17.35           C  
-ATOM   1363  CG1 ILE A 232      -6.461 -14.255 -26.406  1.00 13.43           C  
-ATOM   1364  CG2 ILE A 232      -4.354 -14.005 -27.737  1.00 19.60           C  
-ATOM   1365  CD1 ILE A 232      -7.281 -14.676 -27.604  1.00 14.29           C  
-ATOM   1366  N   SER A 233      -2.123 -12.475 -25.518  1.00 21.09           N  
-ATOM   1367  CA  SER A 233      -0.917 -11.661 -25.698  1.00 23.44           C  
-ATOM   1368  C   SER A 233      -0.289 -11.807 -27.079  1.00 20.20           C  
-ATOM   1369  O   SER A 233      -0.701 -12.651 -27.874  1.00 26.68           O  
-ATOM   1370  CB  SER A 233       0.125 -12.023 -24.639  1.00 22.69           C  
-ATOM   1371  OG  SER A 233       0.725 -13.275 -24.922  1.00 10.20           O  
-ATOM   1372  N   LYS A 234       0.720 -10.982 -27.354  1.00 19.01           N  
-ATOM   1373  CA  LYS A 234       1.482 -11.100 -28.592  1.00 17.78           C  
-ATOM   1374  C   LYS A 234       2.366 -12.338 -28.509  1.00 20.05           C  
-ATOM   1375  O   LYS A 234       2.645 -12.833 -27.420  1.00 24.62           O  
-ATOM   1376  CB  LYS A 234       2.324  -9.844 -28.852  1.00 13.03           C  
-ATOM   1377  CG  LYS A 234       3.785  -9.967 -28.448  1.00 20.59           C  
-ATOM   1378  CD  LYS A 234       4.035  -9.389 -27.068  1.00 36.08           C  
-ATOM   1379  CE  LYS A 234       4.358  -7.905 -27.139  1.00 31.87           C  
-ATOM   1380  NZ  LYS A 234       5.691  -7.671 -27.756  1.00 29.34           N  
-ATOM   1381  N   THR A 235       2.804 -12.842 -29.656  1.00 21.81           N  
-ATOM   1382  CA  THR A 235       3.597 -14.064 -29.677  1.00 15.73           C  
-ATOM   1383  C   THR A 235       5.055 -13.828 -29.291  1.00 22.26           C  
-ATOM   1384  O   THR A 235       5.748 -13.008 -29.895  1.00 25.76           O  
-ATOM   1385  CB  THR A 235       3.555 -14.727 -31.058  1.00 14.69           C  
-ATOM   1386  OG1 THR A 235       2.195 -15.013 -31.408  1.00 21.96           O  
-ATOM   1387  CG2 THR A 235       4.355 -16.015 -31.044  1.00 12.53           C  
-ATOM   1388  N   PHE A 236       5.502 -14.554 -28.271  1.00 20.37           N  
-ATOM   1389  CA  PHE A 236       6.904 -14.589 -27.877  1.00 18.42           C  
-ATOM   1390  C   PHE A 236       7.564 -15.827 -28.464  1.00 22.23           C  
-ATOM   1391  O   PHE A 236       6.887 -16.704 -29.000  1.00 23.08           O  
-ATOM   1392  CB  PHE A 236       7.050 -14.612 -26.356  1.00 19.28           C  
-ATOM   1393  CG  PHE A 236       6.482 -13.410 -25.664  1.00 19.27           C  
-ATOM   1394  CD1 PHE A 236       5.114 -13.261 -25.510  1.00 19.76           C  
-ATOM   1395  CD2 PHE A 236       7.319 -12.444 -25.139  1.00 23.32           C  
-ATOM   1396  CE1 PHE A 236       4.593 -12.159 -24.866  1.00 20.63           C  
-ATOM   1397  CE2 PHE A 236       6.804 -11.342 -24.490  1.00 22.36           C  
-ATOM   1398  CZ  PHE A 236       5.440 -11.200 -24.354  1.00 29.18           C  
-ATOM   1399  N   SER A 237       8.884 -15.909 -28.346  1.00 24.13           N  
-ATOM   1400  CA  SER A 237       9.602 -17.093 -28.797  1.00 19.21           C  
-ATOM   1401  C   SER A 237      10.927 -17.262 -28.067  1.00 21.50           C  
-ATOM   1402  O   SER A 237      11.629 -16.281 -27.811  1.00 22.25           O  
-ATOM   1403  CB  SER A 237       9.849 -17.031 -30.305  1.00 18.98           C  
-ATOM   1404  OG  SER A 237      10.860 -16.088 -30.610  1.00 37.74           O  
-ATOM   1405  N   ASP A 238      11.252 -18.508 -27.728  1.00 20.86           N  
-ATOM   1406  CA  ASP A 238      12.559 -18.860 -27.173  1.00 21.31           C  
-ATOM   1407  C   ASP A 238      13.017 -20.209 -27.710  1.00 21.27           C  
-ATOM   1408  O   ASP A 238      12.228 -21.152 -27.782  1.00 27.84           O  
-ATOM   1409  CB  ASP A 238      12.523 -18.896 -25.646  1.00 20.56           C  
-ATOM   1410  CG  ASP A 238      12.259 -17.540 -25.044  1.00 31.36           C  
-ATOM   1411  OD1 ASP A 238      13.117 -16.643 -25.200  1.00 37.06           O  
-ATOM   1412  OD2 ASP A 238      11.197 -17.368 -24.412  1.00 30.07           O  
-ATOM   1413  N   ASN A 239      14.292 -20.293 -28.081  1.00 19.42           N  
-ATOM   1414  CA  ASN A 239      14.879 -21.529 -28.595  1.00 22.70           C  
-ATOM   1415  C   ASN A 239      14.072 -22.166 -29.724  1.00 20.12           C  
-ATOM   1416  O   ASN A 239      13.806 -23.370 -29.707  1.00 18.96           O  
-ATOM   1417  CB  ASN A 239      15.058 -22.535 -27.458  1.00 15.99           C  
-ATOM   1418  CG  ASN A 239      16.233 -22.195 -26.561  1.00 23.55           C  
-ATOM   1419  OD1 ASN A 239      16.062 -21.894 -25.380  1.00 27.31           O  
-ATOM   1420  ND2 ASN A 239      17.437 -22.243 -27.120  1.00 24.75           N  
-ATOM   1421  N   GLY A 240      13.683 -21.352 -30.702  1.00 15.71           N  
-ATOM   1422  CA  GLY A 240      12.967 -21.846 -31.864  1.00 17.73           C  
-ATOM   1423  C   GLY A 240      11.542 -22.252 -31.552  1.00 13.93           C  
-ATOM   1424  O   GLY A 240      10.867 -22.860 -32.382  1.00 11.93           O  
-ATOM   1425  N   VAL A 241      11.089 -21.916 -30.347  1.00 17.45           N  
-ATOM   1426  CA  VAL A 241       9.739 -22.246 -29.910  1.00 19.02           C  
-ATOM   1427  C   VAL A 241       8.895 -20.994 -29.758  1.00 22.04           C  
-ATOM   1428  O   VAL A 241       9.174 -20.152 -28.907  1.00 19.79           O  
-ATOM   1429  CB  VAL A 241       9.726 -23.001 -28.565  1.00 15.15           C  
-ATOM   1430  CG1 VAL A 241       8.301 -23.376 -28.188  1.00 16.01           C  
-ATOM   1431  CG2 VAL A 241      10.608 -24.234 -28.634  1.00 19.56           C  
-ATOM   1432  N   PRO A 242       7.856 -20.872 -30.591  1.00 22.81           N  
-ATOM   1433  CA  PRO A 242       6.875 -19.791 -30.525  1.00 16.39           C  
-ATOM   1434  C   PRO A 242       5.777 -20.130 -29.533  1.00 14.28           C  
-ATOM   1435  O   PRO A 242       5.358 -21.284 -29.469  1.00 15.65           O  
-ATOM   1436  CB  PRO A 242       6.320 -19.725 -31.956  1.00 16.36           C  
-ATOM   1437  CG  PRO A 242       6.849 -20.970 -32.671  1.00 16.16           C  
-ATOM   1438  CD  PRO A 242       7.529 -21.829 -31.657  1.00 16.37           C  
-ATOM   1439  N   TYR A 243       5.321 -19.145 -28.768  1.00 14.02           N  
-ATOM   1440  CA  TYR A 243       4.259 -19.379 -27.799  1.00 15.83           C  
-ATOM   1441  C   TYR A 243       3.637 -18.066 -27.351  1.00 13.33           C  
-ATOM   1442  O   TYR A 243       4.245 -17.015 -27.505  1.00 14.00           O  
-ATOM   1443  CB  TYR A 243       4.793 -20.162 -26.590  1.00 15.75           C  
-ATOM   1444  CG  TYR A 243       5.924 -19.498 -25.842  1.00 15.92           C  
-ATOM   1445  CD1 TYR A 243       7.242 -19.699 -26.221  1.00 19.67           C  
-ATOM   1446  CD2 TYR A 243       5.674 -18.688 -24.743  1.00 17.30           C  
-ATOM   1447  CE1 TYR A 243       8.281 -19.101 -25.535  1.00 22.81           C  
-ATOM   1448  CE2 TYR A 243       6.705 -18.085 -24.051  1.00 22.82           C  
-ATOM   1449  CZ  TYR A 243       8.006 -18.295 -24.451  1.00 24.19           C  
-ATOM   1450  OH  TYR A 243       9.034 -17.698 -23.762  1.00 30.22           O  
-ATOM   1451  N   ASP A 244       2.424 -18.116 -26.808  1.00 14.28           N  
-ATOM   1452  CA  ASP A 244       1.834 -16.905 -26.231  1.00 17.96           C  
-ATOM   1453  C   ASP A 244       1.099 -17.204 -24.928  1.00 15.95           C  
-ATOM   1454  O   ASP A 244       0.973 -18.358 -24.529  1.00 17.03           O  
-ATOM   1455  CB  ASP A 244       0.894 -16.206 -27.230  1.00 19.96           C  
-ATOM   1456  CG  ASP A 244      -0.260 -17.090 -27.695  1.00 17.70           C  
-ATOM   1457  OD1 ASP A 244      -0.471 -18.178 -27.124  1.00 20.97           O  
-ATOM   1458  OD2 ASP A 244      -0.972 -16.683 -28.639  1.00 14.85           O  
-ATOM   1459  N   PHE A 245       0.618 -16.157 -24.266  1.00 15.43           N  
-ATOM   1460  CA  PHE A 245      -0.032 -16.304 -22.967  1.00 16.28           C  
-ATOM   1461  C   PHE A 245      -1.498 -15.894 -23.015  1.00 17.09           C  
-ATOM   1462  O   PHE A 245      -1.831 -14.805 -23.481  1.00 16.23           O  
-ATOM   1463  CB  PHE A 245       0.693 -15.471 -21.908  1.00 16.78           C  
-ATOM   1464  CG  PHE A 245       2.173 -15.709 -21.855  1.00 18.62           C  
-ATOM   1465  CD1 PHE A 245       3.040 -14.959 -22.637  1.00 21.16           C  
-ATOM   1466  CD2 PHE A 245       2.700 -16.671 -21.013  1.00 18.59           C  
-ATOM   1467  CE1 PHE A 245       4.402 -15.173 -22.584  1.00 17.46           C  
-ATOM   1468  CE2 PHE A 245       4.059 -16.889 -20.956  1.00 23.44           C  
-ATOM   1469  CZ  PHE A 245       4.912 -16.139 -21.743  1.00 29.68           C  
-ATOM   1470  N   VAL A 246      -2.374 -16.766 -22.527  1.00 18.64           N  
-ATOM   1471  CA  VAL A 246      -3.787 -16.427 -22.422  1.00 22.55           C  
-ATOM   1472  C   VAL A 246      -4.329 -16.671 -21.023  1.00 22.92           C  
-ATOM   1473  O   VAL A 246      -3.831 -17.522 -20.279  1.00 25.25           O  
-ATOM   1474  CB  VAL A 246      -4.653 -17.218 -23.419  1.00 14.92           C  
-ATOM   1475  CG1 VAL A 246      -4.300 -16.836 -24.847  1.00 19.04           C  
-ATOM   1476  CG2 VAL A 246      -4.510 -18.712 -23.188  1.00 14.58           C  
-ATOM   1477  N   VAL A 247      -5.356 -15.905 -20.674  1.00 20.00           N  
-ATOM   1478  CA  VAL A 247      -6.062 -16.096 -19.421  1.00 21.07           C  
-ATOM   1479  C   VAL A 247      -7.513 -16.464 -19.701  1.00 25.29           C  
-ATOM   1480  O   VAL A 247      -8.263 -15.696 -20.311  1.00 27.28           O  
-ATOM   1481  CB  VAL A 247      -6.006 -14.839 -18.534  1.00 26.46           C  
-ATOM   1482  CG1 VAL A 247      -6.691 -15.106 -17.202  1.00 32.31           C  
-ATOM   1483  CG2 VAL A 247      -4.565 -14.404 -18.320  1.00 22.24           C  
-ATOM   1484  N   LEU A 248      -7.894 -17.659 -19.266  1.00 21.93           N  
-ATOM   1485  CA  LEU A 248      -9.266 -18.114 -19.389  1.00 24.37           C  
-ATOM   1486  C   LEU A 248     -10.010 -17.857 -18.088  1.00 38.63           C  
-ATOM   1487  O   LEU A 248      -9.404 -17.791 -17.015  1.00 27.75           O  
-ATOM   1488  CB  LEU A 248      -9.325 -19.599 -19.743  1.00 23.79           C  
-ATOM   1489  CG  LEU A 248      -8.469 -20.090 -20.910  1.00 21.20           C  
-ATOM   1490  CD1 LEU A 248      -8.849 -21.515 -21.260  1.00 25.15           C  
-ATOM   1491  CD2 LEU A 248      -8.613 -19.189 -22.119  1.00 29.43           C  
-ATOM   1492  N   GLU A 249     -11.326 -17.722 -18.197  1.00 45.78           N  
-ATOM   1493  CA  GLU A 249     -12.181 -17.426 -17.059  1.00 36.32           C  
-ATOM   1494  C   GLU A 249     -13.435 -18.290 -17.120  1.00 36.30           C  
-ATOM   1495  O   GLU A 249     -13.998 -18.511 -18.198  1.00 34.98           O  
-ATOM   1496  CB  GLU A 249     -12.543 -15.940 -17.041  1.00 30.98           C  
-ATOM   1497  CG  GLU A 249     -13.539 -15.530 -15.971  1.00 40.57           C  
-ATOM   1498  CD  GLU A 249     -13.880 -14.055 -16.045  1.00 50.65           C  
-ATOM   1499  OE1 GLU A 249     -13.265 -13.265 -15.298  1.00 34.60           O  
-ATOM   1500  OE2 GLU A 249     -14.757 -13.685 -16.856  1.00 57.92           O  
-ATOM   1501  N   LYS A 250     -13.854 -18.796 -15.964  1.00 35.28           N  
-ATOM   1502  CA  LYS A 250     -15.076 -19.587 -15.875  1.00 34.22           C  
-ATOM   1503  C   LYS A 250     -16.286 -18.667 -16.012  1.00 45.04           C  
-ATOM   1504  O   LYS A 250     -16.425 -17.698 -15.265  1.00 52.13           O  
-ATOM   1505  CB  LYS A 250     -15.123 -20.357 -14.555  1.00 34.15           C  
-ATOM   1506  CG  LYS A 250     -16.170 -21.455 -14.510  1.00 42.43           C  
-ATOM   1507  CD  LYS A 250     -15.985 -22.343 -13.290  1.00 34.81           C  
-ATOM   1508  CE  LYS A 250     -16.934 -23.528 -13.327  1.00 36.21           C  
-ATOM   1509  NZ  LYS A 250     -16.699 -24.462 -12.195  1.00 30.26           N  
-ATOM   1510  N   ARG A 251     -17.160 -18.967 -16.968  1.00 46.77           N  
-ATOM   1511  CA  ARG A 251     -18.233 -18.038 -17.312  1.00 60.46           C  
-ATOM   1512  C   ARG A 251     -19.645 -18.583 -17.121  1.00 75.30           C  
-ATOM   1513  O   ARG A 251     -20.537 -17.848 -16.690  1.00 81.11           O  
-ATOM   1514  CB  ARG A 251     -18.069 -17.568 -18.762  1.00 55.05           C  
-ATOM   1515  CG  ARG A 251     -17.053 -16.453 -18.946  1.00 56.86           C  
-ATOM   1516  CD  ARG A 251     -17.314 -15.306 -17.979  1.00 68.18           C  
-ATOM   1517  NE  ARG A 251     -18.721 -14.910 -17.954  1.00 86.84           N  
-ATOM   1518  CZ  ARG A 251     -19.237 -14.033 -17.098  1.00 82.24           C  
-ATOM   1519  NH1 ARG A 251     -20.530 -13.737 -17.147  1.00 69.68           N  
-ATOM   1520  NH2 ARG A 251     -18.463 -13.453 -16.191  1.00 74.83           N  
-ATOM   1521  N   ARG A 252     -19.843 -19.856 -17.456  1.00 68.75           N  
-ATOM   1522  CA  ARG A 252     -21.169 -20.475 -17.429  1.00 67.85           C  
-ATOM   1523  C   ARG A 252     -22.156 -19.737 -18.329  1.00 67.59           C  
-ATOM   1524  O   ARG A 252     -22.166 -19.924 -19.546  1.00 63.03           O  
-ATOM   1525  CB  ARG A 252     -21.720 -20.536 -15.999  1.00 64.00           C  
-ATOM   1526  CG  ARG A 252     -23.210 -20.832 -15.931  1.00 62.25           C  
-ATOM   1527  CD  ARG A 252     -23.889 -20.042 -14.821  1.00 62.44           C  
-ATOM   1528  NE  ARG A 252     -25.014 -19.261 -15.329  1.00 66.94           N  
-ATOM   1529  CZ  ARG A 252     -26.242 -19.742 -15.499  1.00 76.53           C  
-ATOM   1530  NH1 ARG A 252     -26.508 -21.006 -15.199  1.00 70.76           N  
-ATOM   1531  NH2 ARG A 252     -27.204 -18.959 -15.970  1.00 70.26           N  
-ATOM   1532  N   SER A 285     -14.131  20.680  -8.939  1.00 85.13           N  
-ATOM   1533  CA  SER A 285     -14.230  20.650 -10.393  1.00 90.05           C  
-ATOM   1534  C   SER A 285     -12.852  20.625 -11.051  1.00 82.78           C  
-ATOM   1535  O   SER A 285     -12.475  21.558 -11.762  1.00 82.37           O  
-ATOM   1536  CB  SER A 285     -15.038  21.849 -10.893  1.00 81.23           C  
-ATOM   1537  OG  SER A 285     -14.845  22.978 -10.061  1.00 67.29           O  
-ATOM   1538  N   SER A 286     -12.105  19.552 -10.809  1.00 85.09           N  
-ATOM   1539  CA  SER A 286     -10.777  19.398 -11.393  1.00 97.80           C  
-ATOM   1540  C   SER A 286     -10.870  19.268 -12.911  1.00101.20           C  
-ATOM   1541  O   SER A 286     -10.605  20.221 -13.647  1.00 86.49           O  
-ATOM   1542  CB  SER A 286     -10.063  18.179 -10.800  1.00 80.60           C  
-ATOM   1543  OG  SER A 286      -9.917  18.301  -9.395  1.00 62.60           O  
-ATOM   1544  N   ALA A 287     -11.257  18.083 -13.369  1.00 92.20           N  
-ATOM   1545  CA  ALA A 287     -11.403  17.822 -14.793  1.00 66.20           C  
-ATOM   1546  C   ALA A 287     -12.841  17.443 -15.118  1.00 70.57           C  
-ATOM   1547  O   ALA A 287     -13.262  17.483 -16.274  1.00 78.96           O  
-ATOM   1548  CB  ALA A 287     -10.447  16.724 -15.233  1.00 68.06           C  
-ATOM   1549  N   ALA A 288     -13.591  17.087 -14.081  1.00 75.87           N  
-ATOM   1550  CA  ALA A 288     -14.948  16.575 -14.233  1.00 87.87           C  
-ATOM   1551  C   ALA A 288     -15.916  17.609 -14.806  1.00 95.52           C  
-ATOM   1552  O   ALA A 288     -16.911  17.250 -15.437  1.00 88.43           O  
-ATOM   1553  CB  ALA A 288     -15.460  16.065 -12.893  1.00 72.60           C  
-ATOM   1554  N   ALA A 289     -15.623  18.888 -14.593  1.00 91.14           N  
-ATOM   1555  CA  ALA A 289     -16.509  19.958 -15.045  1.00 96.05           C  
-ATOM   1556  C   ALA A 289     -16.346  20.247 -16.535  1.00108.81           C  
-ATOM   1557  O   ALA A 289     -16.975  21.159 -17.073  1.00106.63           O  
-ATOM   1558  CB  ALA A 289     -16.260  21.219 -14.239  1.00 86.10           C  
-ATOM   1559  N   ILE A 290     -15.501  19.466 -17.199  1.00107.37           N  
-ATOM   1560  CA  ILE A 290     -15.211  19.682 -18.610  1.00 95.62           C  
-ATOM   1561  C   ILE A 290     -15.795  18.541 -19.444  1.00 96.42           C  
-ATOM   1562  O   ILE A 290     -15.768  18.566 -20.675  1.00 91.88           O  
-ATOM   1563  CB  ILE A 290     -13.697  19.817 -18.833  1.00 86.69           C  
-ATOM   1564  CG1 ILE A 290     -13.102  20.681 -17.719  1.00 95.01           C  
-ATOM   1565  CG2 ILE A 290     -13.401  20.434 -20.192  1.00 81.42           C  
-ATOM   1566  CD1 ILE A 290     -11.714  20.288 -17.303  1.00 96.47           C  
-ATOM   1567  N   ALA A 291     -16.344  17.548 -18.752  1.00 97.88           N  
-ATOM   1568  CA  ALA A 291     -17.098  16.471 -19.387  1.00 99.53           C  
-ATOM   1569  C   ALA A 291     -18.399  16.910 -20.094  1.00100.79           C  
-ATOM   1570  O   ALA A 291     -18.870  16.200 -20.981  1.00 97.40           O  
-ATOM   1571  CB  ALA A 291     -17.412  15.392 -18.358  1.00 97.40           C  
-ATOM   1572  N   PRO A 292     -19.008  18.052 -19.697  1.00 98.55           N  
-ATOM   1573  CA  PRO A 292     -20.160  18.479 -20.506  1.00 93.22           C  
-ATOM   1574  C   PRO A 292     -19.824  18.901 -21.941  1.00 93.83           C  
-ATOM   1575  O   PRO A 292     -20.636  18.663 -22.837  1.00 91.99           O  
-ATOM   1576  CB  PRO A 292     -20.721  19.676 -19.717  1.00 94.64           C  
-ATOM   1577  CG  PRO A 292     -19.642  20.066 -18.763  1.00 83.38           C  
-ATOM   1578  CD  PRO A 292     -18.971  18.784 -18.419  1.00 94.42           C  
-ATOM   1579  N   VAL A 293     -18.670  19.525 -22.161  1.00 99.59           N  
-ATOM   1580  CA  VAL A 293     -18.269  19.881 -23.520  1.00 91.96           C  
-ATOM   1581  C   VAL A 293     -17.931  18.613 -24.291  1.00 89.11           C  
-ATOM   1582  O   VAL A 293     -18.159  18.522 -25.499  1.00 78.53           O  
-ATOM   1583  CB  VAL A 293     -17.061  20.836 -23.544  1.00 84.59           C  
-ATOM   1584  CG1 VAL A 293     -16.817  21.345 -24.957  1.00 75.04           C  
-ATOM   1585  CG2 VAL A 293     -17.291  21.996 -22.605  1.00 81.66           C  
-ATOM   1586  N   LEU A 294     -17.386  17.632 -23.579  1.00102.58           N  
-ATOM   1587  CA  LEU A 294     -17.134  16.320 -24.155  1.00105.36           C  
-ATOM   1588  C   LEU A 294     -18.445  15.631 -24.510  1.00104.68           C  
-ATOM   1589  O   LEU A 294     -18.493  14.810 -25.418  1.00102.57           O  
-ATOM   1590  CB  LEU A 294     -16.334  15.442 -23.187  1.00109.75           C  
-ATOM   1591  CG  LEU A 294     -14.866  15.784 -22.925  1.00 90.22           C  
-ATOM   1592  CD1 LEU A 294     -14.310  14.872 -21.847  1.00 88.21           C  
-ATOM   1593  CD2 LEU A 294     -14.047  15.666 -24.201  1.00 85.05           C  
-ATOM   1594  N   ALA A 295     -19.507  15.986 -23.792  1.00100.33           N  
-ATOM   1595  CA  ALA A 295     -20.784  15.285 -23.884  1.00 97.23           C  
-ATOM   1596  C   ALA A 295     -21.501  15.522 -25.213  1.00 97.67           C  
-ATOM   1597  O   ALA A 295     -22.234  14.653 -25.687  1.00 94.02           O  
-ATOM   1598  CB  ALA A 295     -21.687  15.687 -22.724  1.00 84.79           C  
-ATOM   1599  N   TRP A 296     -21.294  16.691 -25.814  1.00 93.53           N  
-ATOM   1600  CA  TRP A 296     -21.947  16.996 -27.083  1.00 96.77           C  
-ATOM   1601  C   TRP A 296     -21.031  16.735 -28.274  1.00 99.23           C  
-ATOM   1602  O   TRP A 296     -21.477  16.728 -29.422  1.00 92.56           O  
-ATOM   1603  CB  TRP A 296     -22.444  18.443 -27.103  1.00 89.26           C  
-ATOM   1604  CG  TRP A 296     -21.379  19.498 -27.170  1.00 99.88           C  
-ATOM   1605  CD1 TRP A 296     -20.785  20.133 -26.117  1.00103.84           C  
-ATOM   1606  CD2 TRP A 296     -20.808  20.067 -28.355  1.00100.04           C  
-ATOM   1607  NE1 TRP A 296     -19.870  21.054 -26.573  1.00 98.56           N  
-ATOM   1608  CE2 TRP A 296     -19.865  21.031 -27.944  1.00 94.84           C  
-ATOM   1609  CE3 TRP A 296     -20.996  19.848 -29.724  1.00 84.71           C  
-ATOM   1610  CZ2 TRP A 296     -19.116  21.776 -28.851  1.00 82.45           C  
-ATOM   1611  CZ3 TRP A 296     -20.250  20.587 -30.622  1.00 80.35           C  
-ATOM   1612  CH2 TRP A 296     -19.321  21.538 -30.183  1.00 84.35           C  
-ATOM   1613  N   MET A 297     -19.749  16.521 -28.000  1.00100.03           N  
-ATOM   1614  CA  MET A 297     -18.823  16.086 -29.036  1.00 84.75           C  
-ATOM   1615  C   MET A 297     -18.780  14.563 -29.049  1.00 83.71           C  
-ATOM   1616  O   MET A 297     -18.208  13.949 -29.949  1.00 85.74           O  
-ATOM   1617  CB  MET A 297     -17.427  16.666 -28.804  1.00 80.40           C  
-ATOM   1618  CG  MET A 297     -17.360  18.187 -28.854  1.00 84.00           C  
-ATOM   1619  SD  MET A 297     -15.661  18.792 -28.756  1.00 80.18           S  
-ATOM   1620  CE  MET A 297     -15.920  20.560 -28.639  1.00 53.26           C  
-ATOM   1621  N   ASP A 298     -19.402  13.967 -28.035  1.00 87.55           N  
-ATOM   1622  CA  ASP A 298     -19.441  12.518 -27.872  1.00 94.34           C  
-ATOM   1623  C   ASP A 298     -20.550  11.907 -28.720  1.00 97.71           C  
-ATOM   1624  O   ASP A 298     -21.555  12.561 -29.007  1.00 75.78           O  
-ATOM   1625  CB  ASP A 298     -19.636  12.151 -26.393  1.00 88.64           C  
-ATOM   1626  CG  ASP A 298     -19.567  10.656 -26.140  1.00 83.91           C  
-ATOM   1627  OD1 ASP A 298     -18.942   9.940 -26.950  1.00 84.24           O  
-ATOM   1628  OD2 ASP A 298     -20.135  10.198 -25.126  1.00 73.17           O  
-ATOM   1629  N   GLU A 299     -20.358  10.651 -29.116  1.00109.15           N  
-ATOM   1630  CA  GLU A 299     -21.343   9.925 -29.911  1.00109.15           C  
-ATOM   1631  C   GLU A 299     -21.884   8.714 -29.151  1.00 99.66           C  
-ATOM   1632  O   GLU A 299     -21.740   7.571 -29.591  1.00 81.54           O  
-ATOM   1633  CB  GLU A 299     -20.733   9.485 -31.243  1.00 88.89           C  
-ATOM   1634  CG  GLU A 299     -20.249  10.638 -32.109  1.00 73.24           C  
-ATOM   1635  CD  GLU A 299     -21.375  11.563 -32.523  1.00 79.84           C  
-ATOM   1636  OE1 GLU A 299     -22.140  11.192 -33.436  1.00 86.80           O  
-ATOM   1637  OE2 GLU A 299     -21.499  12.658 -31.933  1.00 86.56           O  
-ATOM   1638  N   LEU A 310     -21.015  -1.704 -33.610  1.00 24.95           N  
-ATOM   1639  CA  LEU A 310     -21.977  -2.801 -33.554  1.00 43.16           C  
-ATOM   1640  C   LEU A 310     -21.279  -4.155 -33.663  1.00 36.46           C  
-ATOM   1641  O   LEU A 310     -21.428  -5.012 -32.791  1.00 43.79           O  
-ATOM   1642  CB  LEU A 310     -23.019  -2.658 -34.666  1.00 49.70           C  
-ATOM   1643  CG  LEU A 310     -24.487  -2.904 -34.300  1.00 52.28           C  
-ATOM   1644  CD1 LEU A 310     -24.692  -4.288 -33.693  1.00 38.52           C  
-ATOM   1645  CD2 LEU A 310     -25.009  -1.816 -33.364  1.00 39.81           C  
-ATOM   1646  N   ILE A 311     -20.527  -4.344 -34.742  1.00 35.56           N  
-ATOM   1647  CA  ILE A 311     -19.784  -5.581 -34.952  1.00 43.33           C  
-ATOM   1648  C   ILE A 311     -18.405  -5.502 -34.300  1.00 46.51           C  
-ATOM   1649  O   ILE A 311     -17.679  -4.523 -34.479  1.00 41.60           O  
-ATOM   1650  CB  ILE A 311     -19.622  -5.904 -36.461  1.00 36.08           C  
-ATOM   1651  CG1 ILE A 311     -20.861  -6.624 -37.003  1.00 42.33           C  
-ATOM   1652  CG2 ILE A 311     -18.388  -6.762 -36.702  1.00 31.59           C  
-ATOM   1653  CD1 ILE A 311     -22.061  -5.725 -37.248  1.00 50.92           C  
-ATOM   1654  N   ARG A 312     -18.056  -6.528 -33.529  1.00 43.76           N  
-ATOM   1655  CA  ARG A 312     -16.730  -6.612 -32.931  1.00 43.70           C  
-ATOM   1656  C   ARG A 312     -16.239  -8.053 -32.872  1.00 52.66           C  
-ATOM   1657  O   ARG A 312     -16.992  -8.964 -32.525  1.00 59.11           O  
-ATOM   1658  CB  ARG A 312     -16.723  -6.004 -31.528  1.00 40.66           C  
-ATOM   1659  CG  ARG A 312     -15.351  -6.026 -30.873  1.00 41.47           C  
-ATOM   1660  CD  ARG A 312     -15.284  -5.105 -29.672  1.00 38.93           C  
-ATOM   1661  NE  ARG A 312     -13.917  -4.662 -29.414  1.00 35.38           N  
-ATOM   1662  CZ  ARG A 312     -13.379  -4.563 -28.204  1.00 46.94           C  
-ATOM   1663  NH1 ARG A 312     -14.093  -4.880 -27.132  1.00 58.70           N  
-ATOM   1664  NH2 ARG A 312     -12.126  -4.150 -28.064  1.00 28.94           N  
-ATOM   1665  N   ALA A 313     -14.972  -8.254 -33.220  1.00 45.72           N  
-ATOM   1666  CA  ALA A 313     -14.358  -9.571 -33.130  1.00 37.30           C  
-ATOM   1667  C   ALA A 313     -14.105  -9.932 -31.672  1.00 43.24           C  
-ATOM   1668  O   ALA A 313     -13.565  -9.120 -30.924  1.00 41.39           O  
-ATOM   1669  CB  ALA A 313     -13.064  -9.608 -33.919  1.00 31.95           C  
-ATOM   1670  N   VAL A 314     -14.485 -11.157 -31.300  1.00 40.19           N  
-ATOM   1671  CA  VAL A 314     -14.361 -11.712 -29.940  1.00 35.67           C  
-ATOM   1672  C   VAL A 314     -14.293 -10.674 -28.809  1.00 35.84           C  
-ATOM   1673  O   VAL A 314     -13.230 -10.435 -28.233  1.00 33.53           O  
-ATOM   1674  CB  VAL A 314     -13.126 -12.650 -29.835  1.00 29.09           C  
-ATOM   1675  CG1 VAL A 314     -13.441 -14.003 -30.453  1.00 34.31           C  
-ATOM   1676  CG2 VAL A 314     -11.896 -12.041 -30.497  1.00 31.28           C  
-ATOM   1677  N   PRO A 315     -15.446 -10.068 -28.480  1.00 38.74           N  
-ATOM   1678  CA  PRO A 315     -15.544  -8.946 -27.537  1.00 37.80           C  
-ATOM   1679  C   PRO A 315     -15.206  -9.315 -26.095  1.00 35.10           C  
-ATOM   1680  O   PRO A 315     -14.843  -8.434 -25.313  1.00 32.45           O  
-ATOM   1681  CB  PRO A 315     -17.013  -8.528 -27.649  1.00 38.49           C  
-ATOM   1682  CG  PRO A 315     -17.716  -9.773 -28.050  1.00 44.91           C  
-ATOM   1683  CD  PRO A 315     -16.770 -10.486 -28.972  1.00 39.71           C  
-ATOM   1684  N   HIS A 316     -15.328 -10.593 -25.751  1.00 34.72           N  
-ATOM   1685  CA  HIS A 316     -15.042 -11.050 -24.396  1.00 31.55           C  
-ATOM   1686  C   HIS A 316     -13.555 -10.966 -24.086  1.00 32.77           C  
-ATOM   1687  O   HIS A 316     -13.157 -10.920 -22.924  1.00 40.94           O  
-ATOM   1688  CB  HIS A 316     -15.544 -12.481 -24.196  1.00 30.63           C  
-ATOM   1689  CG  HIS A 316     -15.261 -13.388 -25.352  1.00 36.68           C  
-ATOM   1690  ND1 HIS A 316     -16.084 -13.467 -26.454  1.00 38.37           N  
-ATOM   1691  CD2 HIS A 316     -14.246 -14.257 -25.578  1.00 36.75           C  
-ATOM   1692  CE1 HIS A 316     -15.590 -14.344 -27.309  1.00 32.22           C  
-ATOM   1693  NE2 HIS A 316     -14.475 -14.837 -26.801  1.00 33.91           N  
-ATOM   1694  N   VAL A 317     -12.735 -10.949 -25.131  1.00 35.77           N  
-ATOM   1695  CA  VAL A 317     -11.293 -10.808 -24.970  1.00 39.28           C  
-ATOM   1696  C   VAL A 317     -10.932  -9.355 -24.670  1.00 38.73           C  
-ATOM   1697  O   VAL A 317     -10.917  -8.511 -25.566  1.00 40.66           O  
-ATOM   1698  CB  VAL A 317     -10.537 -11.281 -26.226  1.00 30.31           C  
-ATOM   1699  CG1 VAL A 317      -9.036 -11.126 -26.036  1.00 28.38           C  
-ATOM   1700  CG2 VAL A 317     -10.891 -12.727 -26.548  1.00 28.49           C  
-ATOM   1701  N   HIS A 318     -10.637  -9.068 -23.406  1.00 34.00           N  
-ATOM   1702  CA  HIS A 318     -10.409  -7.692 -22.979  1.00 35.78           C  
-ATOM   1703  C   HIS A 318      -8.984  -7.225 -23.249  1.00 39.24           C  
-ATOM   1704  O   HIS A 318      -8.785  -6.110 -23.730  1.00 43.42           O  
-ATOM   1705  CB  HIS A 318     -10.761  -7.531 -21.499  1.00 45.26           C  
-ATOM   1706  CG  HIS A 318     -12.235  -7.492 -21.241  1.00 66.79           C  
-ATOM   1707  ND1 HIS A 318     -12.822  -8.119 -20.163  1.00 79.89           N  
-ATOM   1708  CD2 HIS A 318     -13.244  -6.901 -21.927  1.00 70.84           C  
-ATOM   1709  CE1 HIS A 318     -14.127  -7.918 -20.196  1.00 81.98           C  
-ATOM   1710  NE2 HIS A 318     -14.409  -7.181 -21.255  1.00 82.45           N  
-ATOM   1711  N   PHE A 319      -7.988  -8.056 -22.955  1.00 40.44           N  
-ATOM   1712  CA  PHE A 319      -6.635  -7.691 -23.373  1.00 26.93           C  
-ATOM   1713  C   PHE A 319      -6.317  -8.290 -24.732  1.00 31.82           C  
-ATOM   1714  O   PHE A 319      -6.271  -9.511 -24.897  1.00 32.86           O  
-ATOM   1715  CB  PHE A 319      -5.577  -8.124 -22.367  1.00 24.63           C  
-ATOM   1716  CG  PHE A 319      -4.177  -7.776 -22.797  1.00 31.65           C  
-ATOM   1717  CD1 PHE A 319      -3.736  -6.462 -22.761  1.00 27.69           C  
-ATOM   1718  CD2 PHE A 319      -3.317  -8.752 -23.269  1.00 32.21           C  
-ATOM   1719  CE1 PHE A 319      -2.458  -6.133 -23.170  1.00 22.41           C  
-ATOM   1720  CE2 PHE A 319      -2.033  -8.431 -23.672  1.00 32.67           C  
-ATOM   1721  CZ  PHE A 319      -1.605  -7.118 -23.623  1.00 33.41           C  
-ATOM   1722  N   ARG A 320      -6.080  -7.412 -25.697  1.00 26.94           N  
-ATOM   1723  CA  ARG A 320      -5.929  -7.814 -27.085  1.00 24.96           C  
-ATOM   1724  C   ARG A 320      -4.529  -7.494 -27.596  1.00 26.76           C  
-ATOM   1725  O   ARG A 320      -4.358  -6.699 -28.521  1.00 29.13           O  
-ATOM   1726  CB  ARG A 320      -6.992  -7.122 -27.932  1.00 28.39           C  
-ATOM   1727  CG  ARG A 320      -8.351  -7.110 -27.254  1.00 26.46           C  
-ATOM   1728  CD  ARG A 320      -9.378  -6.319 -28.034  1.00 39.32           C  
-ATOM   1729  NE  ARG A 320     -10.550  -7.134 -28.319  1.00 33.17           N  
-ATOM   1730  CZ  ARG A 320     -10.989  -7.405 -29.542  1.00 34.57           C  
-ATOM   1731  NH1 ARG A 320     -10.363  -6.906 -30.599  1.00 34.80           N  
-ATOM   1732  NH2 ARG A 320     -12.060  -8.163 -29.705  1.00 34.15           N  
-ATOM   1733  N   GLY A 321      -3.531  -8.121 -26.981  1.00 25.80           N  
-ATOM   1734  CA  GLY A 321      -2.143  -7.893 -27.335  1.00 17.19           C  
-ATOM   1735  C   GLY A 321      -1.754  -8.551 -28.642  1.00 15.85           C  
-ATOM   1736  O   GLY A 321      -0.834  -8.095 -29.317  1.00 19.83           O  
-ATOM   1737  N   HIS A 322      -2.455  -9.625 -28.998  1.00 16.84           N  
-ATOM   1738  CA  HIS A 322      -2.170 -10.358 -30.227  1.00 16.75           C  
-ATOM   1739  C   HIS A 322      -2.332  -9.443 -31.435  1.00 18.17           C  
-ATOM   1740  O   HIS A 322      -3.365  -8.799 -31.602  1.00 19.12           O  
-ATOM   1741  CB  HIS A 322      -3.084 -11.578 -30.353  1.00 15.48           C  
-ATOM   1742  CG  HIS A 322      -2.588 -12.609 -31.320  1.00 17.92           C  
-ATOM   1743  ND1 HIS A 322      -2.556 -12.398 -32.682  1.00 18.43           N  
-ATOM   1744  CD2 HIS A 322      -2.109 -13.858 -31.122  1.00 22.02           C  
-ATOM   1745  CE1 HIS A 322      -2.077 -13.473 -33.280  1.00 15.55           C  
-ATOM   1746  NE2 HIS A 322      -1.798 -14.375 -32.357  1.00 18.52           N  
-ATOM   1747  N   GLU A 323      -1.305  -9.394 -32.276  1.00 16.23           N  
-ATOM   1748  CA  GLU A 323      -1.246  -8.419 -33.360  1.00 15.82           C  
-ATOM   1749  C   GLU A 323      -2.235  -8.706 -34.489  1.00 19.49           C  
-ATOM   1750  O   GLU A 323      -2.392  -7.891 -35.397  1.00 25.59           O  
-ATOM   1751  CB  GLU A 323       0.178  -8.345 -33.915  1.00 17.75           C  
-ATOM   1752  CG  GLU A 323       1.195  -7.832 -32.904  1.00 19.76           C  
-ATOM   1753  CD  GLU A 323       2.622  -7.881 -33.414  1.00 25.89           C  
-ATOM   1754  OE1 GLU A 323       2.862  -8.496 -34.477  1.00 32.54           O  
-ATOM   1755  OE2 GLU A 323       3.506  -7.303 -32.746  1.00 20.64           O  
-ATOM   1756  N   GLU A 324      -2.905  -9.854 -34.428  1.00 18.38           N  
-ATOM   1757  CA  GLU A 324      -3.921 -10.209 -35.420  1.00 20.30           C  
-ATOM   1758  C   GLU A 324      -5.205  -9.414 -35.172  1.00 27.07           C  
-ATOM   1759  O   GLU A 324      -6.044  -9.235 -36.072  1.00 31.38           O  
-ATOM   1760  CB  GLU A 324      -4.196 -11.713 -35.385  1.00 16.87           C  
-ATOM   1761  CG  GLU A 324      -5.102 -12.223 -36.490  1.00 17.10           C  
-ATOM   1762  CD  GLU A 324      -4.845 -13.681 -36.823  1.00 21.83           C  
-ATOM   1763  OE1 GLU A 324      -5.478 -14.205 -37.763  1.00 20.44           O  
-ATOM   1764  OE2 GLU A 324      -4.001 -14.304 -36.147  1.00 29.37           O  
-ATOM   1765  N   PHE A 325      -5.338  -8.921 -33.944  1.00 24.99           N  
-ATOM   1766  CA  PHE A 325      -6.463  -8.076 -33.570  1.00 21.10           C  
-ATOM   1767  C   PHE A 325      -6.471  -6.797 -34.395  1.00 23.07           C  
-ATOM   1768  O   PHE A 325      -7.499  -6.142 -34.512  1.00 27.92           O  
-ATOM   1769  CB  PHE A 325      -6.424  -7.745 -32.075  1.00 20.01           C  
-ATOM   1770  CG  PHE A 325      -6.937  -8.850 -31.194  1.00 27.33           C  
-ATOM   1771  CD1 PHE A 325      -8.269  -9.224 -31.237  1.00 25.92           C  
-ATOM   1772  CD2 PHE A 325      -6.090  -9.507 -30.318  1.00 30.82           C  
-ATOM   1773  CE1 PHE A 325      -8.747 -10.237 -30.427  1.00 23.33           C  
-ATOM   1774  CE2 PHE A 325      -6.564 -10.522 -29.504  1.00 28.61           C  
-ATOM   1775  CZ  PHE A 325      -7.894 -10.887 -29.560  1.00 20.59           C  
-ATOM   1776  N   GLN A 326      -5.321  -6.444 -34.961  1.00 20.62           N  
-ATOM   1777  CA  GLN A 326      -5.249  -5.335 -35.901  1.00 21.12           C  
-ATOM   1778  C   GLN A 326      -6.098  -5.652 -37.120  1.00 22.55           C  
-ATOM   1779  O   GLN A 326      -6.919  -4.843 -37.545  1.00 28.53           O  
-ATOM   1780  CB  GLN A 326      -3.804  -5.059 -36.316  1.00 18.02           C  
-ATOM   1781  CG  GLN A 326      -2.894  -4.658 -35.170  1.00 17.46           C  
-ATOM   1782  CD  GLN A 326      -1.482  -4.364 -35.629  1.00 20.72           C  
-ATOM   1783  OE1 GLN A 326      -1.139  -3.219 -35.921  1.00 24.28           O  
-ATOM   1784  NE2 GLN A 326      -0.653  -5.398 -35.697  1.00 25.01           N  
-ATOM   1785  N   TYR A 327      -5.896  -6.845 -37.668  1.00 20.36           N  
-ATOM   1786  CA  TYR A 327      -6.641  -7.295 -38.836  1.00 21.67           C  
-ATOM   1787  C   TYR A 327      -8.122  -7.470 -38.525  1.00 24.05           C  
-ATOM   1788  O   TYR A 327      -8.986  -6.998 -39.275  1.00 27.28           O  
-ATOM   1789  CB  TYR A 327      -6.060  -8.608 -39.365  1.00 16.45           C  
-ATOM   1790  CG  TYR A 327      -6.858  -9.217 -40.496  1.00 22.85           C  
-ATOM   1791  CD1 TYR A 327      -6.910  -8.603 -41.742  1.00 28.19           C  
-ATOM   1792  CD2 TYR A 327      -7.556 -10.404 -40.321  1.00 18.52           C  
-ATOM   1793  CE1 TYR A 327      -7.637  -9.154 -42.781  1.00 18.73           C  
-ATOM   1794  CE2 TYR A 327      -8.284 -10.964 -41.356  1.00 18.00           C  
-ATOM   1795  CZ  TYR A 327      -8.321 -10.333 -42.582  1.00 17.03           C  
-ATOM   1796  OH  TYR A 327      -9.043 -10.884 -43.613  1.00 20.47           O  
-ATOM   1797  N   LEU A 328      -8.414  -8.150 -37.421  1.00 20.36           N  
-ATOM   1798  CA  LEU A 328      -9.805  -8.372 -37.037  1.00 27.34           C  
-ATOM   1799  C   LEU A 328     -10.548  -7.048 -36.838  1.00 27.20           C  
-ATOM   1800  O   LEU A 328     -11.636  -6.837 -37.397  1.00 26.99           O  
-ATOM   1801  CB  LEU A 328      -9.879  -9.221 -35.767  1.00 37.61           C  
-ATOM   1802  CG  LEU A 328      -9.222 -10.602 -35.850  1.00 25.58           C  
-ATOM   1803  CD1 LEU A 328      -9.476 -11.396 -34.579  1.00 24.32           C  
-ATOM   1804  CD2 LEU A 328      -9.713 -11.363 -37.072  1.00 24.55           C  
-ATOM   1805  N   ASP A 329      -9.948  -6.156 -36.053  1.00 23.99           N  
-ATOM   1806  CA  ASP A 329     -10.529  -4.837 -35.812  1.00 27.01           C  
-ATOM   1807  C   ASP A 329     -10.615  -4.025 -37.097  1.00 26.77           C  
-ATOM   1808  O   ASP A 329     -11.468  -3.156 -37.221  1.00 27.45           O  
-ATOM   1809  CB  ASP A 329      -9.729  -4.054 -34.765  1.00 24.84           C  
-ATOM   1810  CG  ASP A 329      -9.882  -4.620 -33.368  1.00 33.95           C  
-ATOM   1811  OD1 ASP A 329     -10.779  -5.469 -33.165  1.00 36.66           O  
-ATOM   1812  OD2 ASP A 329      -9.112  -4.209 -32.473  1.00 28.82           O  
-ATOM   1813  N   LEU A 330      -9.721  -4.296 -38.043  1.00 24.40           N  
-ATOM   1814  CA  LEU A 330      -9.769  -3.624 -39.335  1.00 23.02           C  
-ATOM   1815  C   LEU A 330     -11.026  -4.071 -40.069  1.00 28.19           C  
-ATOM   1816  O   LEU A 330     -11.752  -3.248 -40.632  1.00 34.55           O  
-ATOM   1817  CB  LEU A 330      -8.514  -3.923 -40.164  1.00 23.83           C  
-ATOM   1818  CG  LEU A 330      -8.166  -3.033 -41.367  1.00 17.97           C  
-ATOM   1819  CD1 LEU A 330      -8.535  -3.690 -42.694  1.00 20.66           C  
-ATOM   1820  CD2 LEU A 330      -8.820  -1.664 -41.246  1.00 16.34           C  
-ATOM   1821  N   ILE A 331     -11.291  -5.375 -40.048  1.00 26.33           N  
-ATOM   1822  CA  ILE A 331     -12.513  -5.904 -40.652  1.00 24.22           C  
-ATOM   1823  C   ILE A 331     -13.760  -5.305 -40.014  1.00 20.93           C  
-ATOM   1824  O   ILE A 331     -14.634  -4.778 -40.707  1.00 20.16           O  
-ATOM   1825  CB  ILE A 331     -12.597  -7.434 -40.533  1.00 21.37           C  
-ATOM   1826  CG1 ILE A 331     -11.384  -8.090 -41.191  1.00 19.04           C  
-ATOM   1827  CG2 ILE A 331     -13.883  -7.941 -41.160  1.00 19.64           C  
-ATOM   1828  CD1 ILE A 331     -11.491  -9.587 -41.262  1.00 23.86           C  
-ATOM   1829  N   ALA A 332     -13.837  -5.393 -38.689  1.00 26.44           N  
-ATOM   1830  CA  ALA A 332     -14.993  -4.874 -37.962  1.00 26.56           C  
-ATOM   1831  C   ALA A 332     -15.201  -3.378 -38.223  1.00 32.68           C  
-ATOM   1832  O   ALA A 332     -16.334  -2.916 -38.368  1.00 35.16           O  
-ATOM   1833  CB  ALA A 332     -14.841  -5.133 -36.474  1.00 30.00           C  
-ATOM   1834  N   ASP A 333     -14.102  -2.633 -38.297  1.00 39.95           N  
-ATOM   1835  CA  ASP A 333     -14.159  -1.191 -38.513  1.00 34.20           C  
-ATOM   1836  C   ASP A 333     -14.633  -0.866 -39.922  1.00 29.01           C  
-ATOM   1837  O   ASP A 333     -15.424   0.052 -40.116  1.00 35.24           O  
-ATOM   1838  CB  ASP A 333     -12.792  -0.551 -38.254  1.00 37.78           C  
-ATOM   1839  CG  ASP A 333     -12.836   0.966 -38.302  1.00 51.48           C  
-ATOM   1840  OD1 ASP A 333     -13.946   1.544 -38.228  1.00 46.97           O  
-ATOM   1841  OD2 ASP A 333     -11.754   1.584 -38.401  1.00 54.97           O  
-ATOM   1842  N   ILE A 334     -14.146  -1.615 -40.904  1.00 28.07           N  
-ATOM   1843  CA  ILE A 334     -14.581  -1.413 -42.281  1.00 24.72           C  
-ATOM   1844  C   ILE A 334     -16.068  -1.726 -42.409  1.00 27.52           C  
-ATOM   1845  O   ILE A 334     -16.808  -1.002 -43.069  1.00 33.88           O  
-ATOM   1846  CB  ILE A 334     -13.777  -2.281 -43.267  1.00 22.51           C  
-ATOM   1847  CG1 ILE A 334     -12.353  -1.746 -43.384  1.00 20.18           C  
-ATOM   1848  CG2 ILE A 334     -14.437  -2.303 -44.632  1.00 21.52           C  
-ATOM   1849  CD1 ILE A 334     -11.511  -2.507 -44.354  1.00 21.25           C  
-ATOM   1850  N   ILE A 335     -16.513  -2.795 -41.759  1.00 33.45           N  
-ATOM   1851  CA  ILE A 335     -17.927  -3.146 -41.814  1.00 30.19           C  
-ATOM   1852  C   ILE A 335     -18.793  -2.069 -41.149  1.00 28.62           C  
-ATOM   1853  O   ILE A 335     -19.770  -1.608 -41.735  1.00 30.45           O  
-ATOM   1854  CB  ILE A 335     -18.201  -4.513 -41.156  1.00 25.66           C  
-ATOM   1855  CG1 ILE A 335     -17.601  -5.639 -42.004  1.00 23.43           C  
-ATOM   1856  CG2 ILE A 335     -19.692  -4.729 -40.993  1.00 26.76           C  
-ATOM   1857  CD1 ILE A 335     -17.862  -7.025 -41.443  1.00 35.97           C  
-ATOM   1858  N   ASN A 336     -18.427  -1.657 -39.939  1.00 34.56           N  
-ATOM   1859  CA  ASN A 336     -19.235  -0.701 -39.181  1.00 36.98           C  
-ATOM   1860  C   ASN A 336     -19.246   0.716 -39.751  1.00 34.05           C  
-ATOM   1861  O   ASN A 336     -20.302   1.337 -39.863  1.00 42.78           O  
-ATOM   1862  CB  ASN A 336     -18.759  -0.638 -37.729  1.00 28.15           C  
-ATOM   1863  CG  ASN A 336     -18.971  -1.939 -36.985  1.00 35.76           C  
-ATOM   1864  OD1 ASN A 336     -19.782  -2.775 -37.386  1.00 40.10           O  
-ATOM   1865  ND2 ASN A 336     -18.249  -2.112 -35.885  1.00 27.63           N  
-ATOM   1866  N   ASN A 337     -18.069   1.225 -40.100  1.00 31.56           N  
-ATOM   1867  CA  ASN A 337     -17.921   2.632 -40.457  1.00 32.62           C  
-ATOM   1868  C   ASN A 337     -17.652   2.877 -41.936  1.00 30.44           C  
-ATOM   1869  O   ASN A 337     -17.638   4.023 -42.388  1.00 33.36           O  
-ATOM   1870  CB  ASN A 337     -16.795   3.259 -39.632  1.00 29.30           C  
-ATOM   1871  CG  ASN A 337     -16.972   3.036 -38.145  1.00 34.17           C  
-ATOM   1872  OD1 ASN A 337     -18.094   2.929 -37.653  1.00 40.03           O  
-ATOM   1873  ND2 ASN A 337     -15.862   2.959 -37.421  1.00 39.36           N  
-ATOM   1874  N   GLY A 338     -17.437   1.805 -42.689  1.00 33.37           N  
-ATOM   1875  CA  GLY A 338     -17.129   1.932 -44.101  1.00 41.75           C  
-ATOM   1876  C   GLY A 338     -18.301   2.439 -44.918  1.00 39.44           C  
-ATOM   1877  O   GLY A 338     -19.416   2.557 -44.411  1.00 37.79           O  
-ATOM   1878  N   ARG A 339     -18.045   2.745 -46.186  1.00 34.51           N  
-ATOM   1879  CA  ARG A 339     -19.097   3.214 -47.080  1.00 32.08           C  
-ATOM   1880  C   ARG A 339     -19.356   2.202 -48.185  1.00 33.80           C  
-ATOM   1881  O   ARG A 339     -18.413   1.644 -48.748  1.00 37.99           O  
-ATOM   1882  CB  ARG A 339     -18.725   4.565 -47.688  1.00 39.19           C  
-ATOM   1883  CG  ARG A 339     -18.439   5.650 -46.670  1.00 38.74           C  
-ATOM   1884  CD  ARG A 339     -19.613   5.847 -45.731  1.00 35.33           C  
-ATOM   1885  NE  ARG A 339     -19.591   7.179 -45.136  1.00 54.18           N  
-ATOM   1886  CZ  ARG A 339     -20.206   8.234 -45.658  1.00 63.20           C  
-ATOM   1887  NH1 ARG A 339     -20.900   8.106 -46.783  1.00 47.57           N  
-ATOM   1888  NH2 ARG A 339     -20.133   9.415 -45.057  1.00 53.26           N  
-ATOM   1889  N   THR A 340     -20.627   1.962 -48.495  1.00 31.50           N  
-ATOM   1890  CA  THR A 340     -20.961   1.041 -49.574  1.00 29.76           C  
-ATOM   1891  C   THR A 340     -20.889   1.741 -50.925  1.00 38.18           C  
-ATOM   1892  O   THR A 340     -21.593   2.719 -51.174  1.00 42.05           O  
-ATOM   1893  CB  THR A 340     -22.353   0.431 -49.409  1.00 29.94           C  
-ATOM   1894  OG1 THR A 340     -22.460  -0.188 -48.122  1.00 30.18           O  
-ATOM   1895  CG2 THR A 340     -22.580  -0.612 -50.487  1.00 35.53           C  
-ATOM   1896  N   MET A 341     -20.035   1.216 -51.795  1.00 36.02           N  
-ATOM   1897  CA  MET A 341     -19.746   1.814 -53.086  1.00 32.36           C  
-ATOM   1898  C   MET A 341     -19.834   0.785 -54.204  1.00 39.07           C  
-ATOM   1899  O   MET A 341     -19.695  -0.426 -53.970  1.00 48.12           O  
-ATOM   1900  CB  MET A 341     -18.347   2.434 -53.082  1.00 38.42           C  
-ATOM   1901  CG  MET A 341     -18.063   3.366 -51.916  1.00 36.05           C  
-ATOM   1902  SD  MET A 341     -18.635   5.041 -52.234  1.00 57.31           S  
-ATOM   1903  CE  MET A 341     -17.695   5.432 -53.708  1.00 41.94           C  
-ATOM   1904  N   ASP A 342     -20.057   1.283 -55.418  1.00 46.10           N  
-ATOM   1905  CA  ASP A 342     -19.950   0.474 -56.626  1.00 52.79           C  
-ATOM   1906  C   ASP A 342     -18.482   0.172 -56.910  1.00 51.64           C  
-ATOM   1907  O   ASP A 342     -17.591   0.687 -56.233  1.00 51.01           O  
-ATOM   1908  CB  ASP A 342     -20.601   1.183 -57.815  1.00 52.57           C  
-ATOM   1909  CG  ASP A 342     -22.117   1.127 -57.765  1.00 72.15           C  
-ATOM   1910  OD1 ASP A 342     -22.657   0.077 -57.353  1.00 72.58           O  
-ATOM   1911  OD2 ASP A 342     -22.770   2.129 -58.131  1.00 71.52           O  
-ATOM   1912  N   ASP A 343     -18.223  -0.654 -57.915  1.00 45.67           N  
-ATOM   1913  CA  ASP A 343     -16.892  -1.219 -58.072  1.00 41.28           C  
-ATOM   1914  C   ASP A 343     -16.623  -1.699 -59.501  1.00 47.51           C  
-ATOM   1915  O   ASP A 343     -17.553  -2.009 -60.244  1.00 55.71           O  
-ATOM   1916  CB  ASP A 343     -16.723  -2.358 -57.059  1.00 38.73           C  
-ATOM   1917  CG  ASP A 343     -15.540  -3.243 -57.355  1.00 47.45           C  
-ATOM   1918  OD1 ASP A 343     -14.399  -2.835 -57.059  1.00 53.70           O  
-ATOM   1919  OD2 ASP A 343     -15.757  -4.353 -57.878  1.00 44.41           O  
-ATOM   1920  N   ARG A 344     -15.344  -1.736 -59.872  1.00 42.36           N  
-ATOM   1921  CA  ARG A 344     -14.898  -2.159 -61.201  1.00 44.82           C  
-ATOM   1922  C   ARG A 344     -15.441  -3.525 -61.629  1.00 48.55           C  
-ATOM   1923  O   ARG A 344     -15.693  -3.760 -62.812  1.00 49.44           O  
-ATOM   1924  CB  ARG A 344     -13.365  -2.184 -61.242  1.00 46.41           C  
-ATOM   1925  CG  ARG A 344     -12.767  -2.716 -62.537  1.00 47.42           C  
-ATOM   1926  CD  ARG A 344     -11.269  -2.950 -62.403  1.00 55.93           C  
-ATOM   1927  NE  ARG A 344     -10.952  -4.010 -61.448  1.00 43.89           N  
-ATOM   1928  CZ  ARG A 344     -10.765  -5.284 -61.778  1.00 60.68           C  
-ATOM   1929  NH1 ARG A 344     -10.865  -5.667 -63.044  1.00 60.42           N  
-ATOM   1930  NH2 ARG A 344     -10.478  -6.179 -60.842  1.00 60.32           N  
-ATOM   1931  N   THR A 345     -15.625  -4.419 -60.662  1.00 42.23           N  
-ATOM   1932  CA  THR A 345     -15.980  -5.805 -60.954  1.00 41.44           C  
-ATOM   1933  C   THR A 345     -17.485  -6.031 -61.065  1.00 41.40           C  
-ATOM   1934  O   THR A 345     -17.929  -7.007 -61.670  1.00 48.65           O  
-ATOM   1935  CB  THR A 345     -15.430  -6.751 -59.876  1.00 58.32           C  
-ATOM   1936  OG1 THR A 345     -16.202  -6.607 -58.677  1.00 63.43           O  
-ATOM   1937  CG2 THR A 345     -13.973  -6.425 -59.575  1.00 58.31           C  
-ATOM   1938  N   GLY A 346     -18.269  -5.136 -60.474  1.00 39.72           N  
-ATOM   1939  CA  GLY A 346     -19.714  -5.270 -60.494  1.00 42.67           C  
-ATOM   1940  C   GLY A 346     -20.249  -5.719 -59.151  1.00 51.49           C  
-ATOM   1941  O   GLY A 346     -21.428  -5.534 -58.845  1.00 55.19           O  
-ATOM   1942  N   VAL A 347     -19.378  -6.320 -58.348  1.00 46.08           N  
-ATOM   1943  CA  VAL A 347     -19.731  -6.692 -56.987  1.00 37.13           C  
-ATOM   1944  C   VAL A 347     -19.656  -5.445 -56.114  1.00 43.63           C  
-ATOM   1945  O   VAL A 347     -18.809  -4.583 -56.335  1.00 41.77           O  
-ATOM   1946  CB  VAL A 347     -18.800  -7.783 -56.430  1.00 44.05           C  
-ATOM   1947  CG1 VAL A 347     -19.481  -8.530 -55.295  1.00 46.35           C  
-ATOM   1948  CG2 VAL A 347     -18.393  -8.749 -57.534  1.00 46.08           C  
-ATOM   1949  N   GLY A 348     -20.550  -5.339 -55.138  1.00 46.48           N  
-ATOM   1950  CA  GLY A 348     -20.568  -4.184 -54.256  1.00 48.71           C  
-ATOM   1951  C   GLY A 348     -19.407  -4.221 -53.284  1.00 37.34           C  
-ATOM   1952  O   GLY A 348     -18.892  -5.295 -52.978  1.00 38.53           O  
-ATOM   1953  N   VAL A 349     -18.989  -3.057 -52.793  1.00 35.88           N  
-ATOM   1954  CA  VAL A 349     -17.852  -3.013 -51.875  1.00 31.63           C  
-ATOM   1955  C   VAL A 349     -18.140  -2.113 -50.677  1.00 34.93           C  
-ATOM   1956  O   VAL A 349     -18.903  -1.166 -50.785  1.00 38.58           O  
-ATOM   1957  CB  VAL A 349     -16.566  -2.540 -52.609  1.00 30.23           C  
-ATOM   1958  CG1 VAL A 349     -16.027  -1.235 -52.029  1.00 27.71           C  
-ATOM   1959  CG2 VAL A 349     -15.507  -3.629 -52.573  1.00 32.30           C  
-ATOM   1960  N   ILE A 350     -17.559  -2.432 -49.524  1.00 31.61           N  
-ATOM   1961  CA  ILE A 350     -17.598  -1.521 -48.384  1.00 28.86           C  
-ATOM   1962  C   ILE A 350     -16.177  -1.060 -48.094  1.00 29.54           C  
-ATOM   1963  O   ILE A 350     -15.327  -1.872 -47.732  1.00 35.23           O  
-ATOM   1964  CB  ILE A 350     -18.193  -2.172 -47.124  1.00 24.17           C  
-ATOM   1965  CG1 ILE A 350     -19.516  -2.866 -47.443  1.00 34.37           C  
-ATOM   1966  CG2 ILE A 350     -18.378  -1.131 -46.031  1.00 19.41           C  
-ATOM   1967  CD1 ILE A 350     -20.113  -3.597 -46.258  1.00 34.91           C  
-ATOM   1968  N   SER A 351     -15.913   0.233 -48.253  1.00 25.37           N  
-ATOM   1969  CA  SER A 351     -14.536   0.713 -48.202  1.00 23.46           C  
-ATOM   1970  C   SER A 351     -14.265   1.797 -47.162  1.00 26.78           C  
-ATOM   1971  O   SER A 351     -15.169   2.520 -46.732  1.00 27.88           O  
-ATOM   1972  CB  SER A 351     -14.113   1.227 -49.583  1.00 23.85           C  
-ATOM   1973  OG  SER A 351     -14.937   2.294 -50.012  1.00 28.25           O  
-ATOM   1974  N   LYS A 352     -12.999   1.873 -46.763  1.00 23.97           N  
-ATOM   1975  CA  LYS A 352     -12.460   2.987 -45.993  1.00 22.48           C  
-ATOM   1976  C   LYS A 352     -11.176   3.451 -46.671  1.00 26.30           C  
-ATOM   1977  O   LYS A 352     -10.660   2.774 -47.562  1.00 26.64           O  
-ATOM   1978  CB  LYS A 352     -12.188   2.590 -44.541  1.00 20.85           C  
-ATOM   1979  CG  LYS A 352     -13.432   2.222 -43.754  1.00 28.54           C  
-ATOM   1980  CD  LYS A 352     -13.179   2.310 -42.255  1.00 31.06           C  
-ATOM   1981  CE  LYS A 352     -12.726   3.706 -41.855  1.00 33.04           C  
-ATOM   1982  NZ  LYS A 352     -12.645   3.869 -40.377  1.00 34.94           N  
-ATOM   1983  N   PHE A 353     -10.652   4.597 -46.253  1.00 21.85           N  
-ATOM   1984  CA  PHE A 353      -9.470   5.155 -46.901  1.00 18.90           C  
-ATOM   1985  C   PHE A 353      -8.386   5.527 -45.893  1.00 19.03           C  
-ATOM   1986  O   PHE A 353      -8.638   6.258 -44.935  1.00 25.57           O  
-ATOM   1987  CB  PHE A 353      -9.862   6.377 -47.734  1.00 25.50           C  
-ATOM   1988  CG  PHE A 353      -8.812   6.805 -48.718  1.00 20.80           C  
-ATOM   1989  CD1 PHE A 353      -8.299   5.908 -49.638  1.00 20.85           C  
-ATOM   1990  CD2 PHE A 353      -8.353   8.111 -48.736  1.00 16.71           C  
-ATOM   1991  CE1 PHE A 353      -7.337   6.300 -50.550  1.00 20.25           C  
-ATOM   1992  CE2 PHE A 353      -7.395   8.510 -49.646  1.00 22.80           C  
-ATOM   1993  CZ  PHE A 353      -6.885   7.602 -50.555  1.00 22.39           C  
-ATOM   1994  N   GLY A 354      -7.178   5.021 -46.116  1.00 18.33           N  
-ATOM   1995  CA  GLY A 354      -6.065   5.283 -45.221  1.00 16.96           C  
-ATOM   1996  C   GLY A 354      -6.093   4.408 -43.985  1.00 16.99           C  
-ATOM   1997  O   GLY A 354      -6.628   4.801 -42.949  1.00 26.61           O  
-ATOM   1998  N   CYS A 355      -5.516   3.216 -44.095  1.00 16.51           N  
-ATOM   1999  CA  CYS A 355      -5.491   2.269 -42.986  1.00 19.76           C  
-ATOM   2000  C   CYS A 355      -4.064   1.808 -42.691  1.00 27.26           C  
-ATOM   2001  O   CYS A 355      -3.220   1.757 -43.583  1.00 20.19           O  
-ATOM   2002  CB  CYS A 355      -6.388   1.068 -43.289  1.00 21.13           C  
-ATOM   2003  SG  CYS A 355      -8.134   1.488 -43.524  1.00 38.42           S  
-ATOM   2004  N   THR A 356      -3.801   1.470 -41.434  1.00 21.58           N  
-ATOM   2005  CA  THR A 356      -2.445   1.170 -41.001  1.00 12.20           C  
-ATOM   2006  C   THR A 356      -2.386  -0.069 -40.122  1.00 17.35           C  
-ATOM   2007  O   THR A 356      -3.171  -0.211 -39.185  1.00 20.88           O  
-ATOM   2008  CB  THR A 356      -1.838   2.363 -40.231  1.00 19.14           C  
-ATOM   2009  OG1 THR A 356      -1.492   3.401 -41.155  1.00 29.14           O  
-ATOM   2010  CG2 THR A 356      -0.590   1.946 -39.460  1.00 24.91           C  
-ATOM   2011  N   MET A 357      -1.459  -0.968 -40.435  1.00 17.70           N  
-ATOM   2012  CA  MET A 357      -1.132  -2.064 -39.529  1.00 15.45           C  
-ATOM   2013  C   MET A 357       0.376  -2.176 -39.406  1.00 15.52           C  
-ATOM   2014  O   MET A 357       1.098  -1.599 -40.206  1.00 19.68           O  
-ATOM   2015  CB  MET A 357      -1.725  -3.383 -40.023  1.00 14.87           C  
-ATOM   2016  CG  MET A 357      -3.232  -3.460 -39.925  1.00 14.18           C  
-ATOM   2017  SD  MET A 357      -3.872  -5.040 -40.506  1.00 17.27           S  
-ATOM   2018  CE  MET A 357      -3.183  -5.095 -42.158  1.00 14.00           C  
-ATOM   2019  N   ARG A 358       0.856  -2.896 -38.399  1.00 13.46           N  
-ATOM   2020  CA  ARG A 358       2.273  -3.247 -38.352  1.00 19.74           C  
-ATOM   2021  C   ARG A 358       2.504  -4.487 -37.496  1.00 25.02           C  
-ATOM   2022  O   ARG A 358       1.956  -4.619 -36.400  1.00 26.67           O  
-ATOM   2023  CB  ARG A 358       3.124  -2.074 -37.848  1.00 15.27           C  
-ATOM   2024  CG  ARG A 358       2.756  -1.534 -36.484  1.00 18.30           C  
-ATOM   2025  CD  ARG A 358       3.828  -0.574 -35.989  1.00 16.71           C  
-ATOM   2026  NE  ARG A 358       3.959   0.601 -36.848  1.00 23.01           N  
-ATOM   2027  CZ  ARG A 358       5.112   1.202 -37.129  1.00 21.01           C  
-ATOM   2028  NH1 ARG A 358       6.248   0.738 -36.630  1.00 19.21           N  
-ATOM   2029  NH2 ARG A 358       5.131   2.268 -37.915  1.00 19.87           N  
-ATOM   2030  N   TYR A 359       3.318  -5.397 -38.022  1.00 20.77           N  
-ATOM   2031  CA  TYR A 359       3.551  -6.686 -37.391  1.00 19.21           C  
-ATOM   2032  C   TYR A 359       5.023  -6.884 -37.049  1.00 22.02           C  
-ATOM   2033  O   TYR A 359       5.911  -6.494 -37.811  1.00 21.92           O  
-ATOM   2034  CB  TYR A 359       3.065  -7.814 -38.302  1.00 22.11           C  
-ATOM   2035  CG  TYR A 359       1.581  -7.774 -38.581  1.00 19.17           C  
-ATOM   2036  CD1 TYR A 359       0.684  -8.441 -37.758  1.00 23.52           C  
-ATOM   2037  CD2 TYR A 359       1.074  -7.069 -39.665  1.00 18.86           C  
-ATOM   2038  CE1 TYR A 359      -0.674  -8.407 -38.008  1.00 22.25           C  
-ATOM   2039  CE2 TYR A 359      -0.284  -7.030 -39.920  1.00 18.60           C  
-ATOM   2040  CZ  TYR A 359      -1.153  -7.702 -39.087  1.00 16.23           C  
-ATOM   2041  OH  TYR A 359      -2.506  -7.673 -39.330  1.00 17.25           O  
-ATOM   2042  N   SER A 360       5.267  -7.496 -35.895  1.00 17.80           N  
-ATOM   2043  CA  SER A 360       6.620  -7.734 -35.416  1.00 17.38           C  
-ATOM   2044  C   SER A 360       7.221  -8.964 -36.078  1.00 22.16           C  
-ATOM   2045  O   SER A 360       6.529  -9.956 -36.303  1.00 23.78           O  
-ATOM   2046  CB  SER A 360       6.619  -7.898 -33.898  1.00 21.33           C  
-ATOM   2047  OG  SER A 360       5.886  -6.855 -33.281  1.00 25.38           O  
-ATOM   2048  N   LEU A 361       8.512  -8.897 -36.381  1.00 18.90           N  
-ATOM   2049  CA  LEU A 361       9.182  -9.982 -37.088  1.00 23.17           C  
-ATOM   2050  C   LEU A 361      10.340 -10.572 -36.289  1.00 32.46           C  
-ATOM   2051  O   LEU A 361      10.986 -11.520 -36.737  1.00 36.48           O  
-ATOM   2052  CB  LEU A 361       9.693  -9.492 -38.445  1.00 27.09           C  
-ATOM   2053  CG  LEU A 361       8.673  -8.831 -39.374  1.00 22.39           C  
-ATOM   2054  CD1 LEU A 361       9.337  -8.372 -40.659  1.00 15.43           C  
-ATOM   2055  CD2 LEU A 361       7.528  -9.777 -39.674  1.00 21.71           C  
-ATOM   2056  N   ASP A 362      10.602 -10.015 -35.112  1.00 30.16           N  
-ATOM   2057  CA  ASP A 362      11.755 -10.430 -34.319  1.00 25.42           C  
-ATOM   2058  C   ASP A 362      11.489 -11.697 -33.504  1.00 26.28           C  
-ATOM   2059  O   ASP A 362      12.407 -12.471 -33.237  1.00 31.29           O  
-ATOM   2060  CB  ASP A 362      12.193  -9.294 -33.393  1.00 31.05           C  
-ATOM   2061  CG  ASP A 362      11.125  -8.915 -32.385  1.00 37.41           C  
-ATOM   2062  OD1 ASP A 362      10.087  -8.355 -32.799  1.00 40.70           O  
-ATOM   2063  OD2 ASP A 362      11.326  -9.170 -31.178  1.00 32.72           O  
-ATOM   2064  N   GLN A 363      10.238 -11.911 -33.112  1.00 36.14           N  
-ATOM   2065  CA  GLN A 363       9.887 -13.079 -32.307  1.00 34.33           C  
-ATOM   2066  C   GLN A 363       9.268 -14.185 -33.157  1.00 32.01           C  
-ATOM   2067  O   GLN A 363       9.747 -15.320 -33.162  1.00 23.19           O  
-ATOM   2068  CB  GLN A 363       8.926 -12.684 -31.185  1.00 35.92           C  
-ATOM   2069  CG  GLN A 363       9.488 -11.647 -30.225  1.00 43.55           C  
-ATOM   2070  CD  GLN A 363      10.618 -12.190 -29.376  1.00 37.56           C  
-ATOM   2071  OE1 GLN A 363      10.461 -13.199 -28.687  1.00 39.89           O  
-ATOM   2072  NE2 GLN A 363      11.767 -11.523 -29.424  1.00 40.40           N  
-ATOM   2073  N   ALA A 364       8.202 -13.847 -33.876  1.00 29.09           N  
-ATOM   2074  CA  ALA A 364       7.522 -14.811 -34.731  1.00 22.27           C  
-ATOM   2075  C   ALA A 364       7.119 -14.180 -36.061  1.00 23.95           C  
-ATOM   2076  O   ALA A 364       7.470 -13.037 -36.349  1.00 29.46           O  
-ATOM   2077  CB  ALA A 364       6.308 -15.381 -34.022  1.00 16.49           C  
-ATOM   2078  N   PHE A 365       6.379 -14.933 -36.866  1.00 15.41           N  
-ATOM   2079  CA  PHE A 365       6.006 -14.496 -38.204  1.00 12.78           C  
-ATOM   2080  C   PHE A 365       4.494 -14.338 -38.300  1.00 17.84           C  
-ATOM   2081  O   PHE A 365       3.750 -15.253 -37.946  1.00 19.27           O  
-ATOM   2082  CB  PHE A 365       6.515 -15.495 -39.246  1.00 17.94           C  
-ATOM   2083  CG  PHE A 365       6.334 -15.048 -40.670  1.00 14.02           C  
-ATOM   2084  CD1 PHE A 365       5.155 -15.306 -41.350  1.00 15.71           C  
-ATOM   2085  CD2 PHE A 365       7.355 -14.399 -41.338  1.00 12.56           C  
-ATOM   2086  CE1 PHE A 365       4.992 -14.904 -42.661  1.00 14.47           C  
-ATOM   2087  CE2 PHE A 365       7.199 -13.998 -42.647  1.00 15.75           C  
-ATOM   2088  CZ  PHE A 365       6.016 -14.250 -43.310  1.00 12.79           C  
-ATOM   2089  N   PRO A 366       4.036 -13.175 -38.790  1.00 20.61           N  
-ATOM   2090  CA  PRO A 366       2.608 -12.854 -38.866  1.00 15.91           C  
-ATOM   2091  C   PRO A 366       1.878 -13.607 -39.976  1.00 21.51           C  
-ATOM   2092  O   PRO A 366       1.351 -12.985 -40.901  1.00 21.45           O  
-ATOM   2093  CB  PRO A 366       2.608 -11.351 -39.140  1.00 11.31           C  
-ATOM   2094  CG  PRO A 366       3.866 -11.119 -39.886  1.00 13.88           C  
-ATOM   2095  CD  PRO A 366       4.873 -12.088 -39.327  1.00 15.65           C  
-ATOM   2096  N   LEU A 367       1.855 -14.933 -39.887  1.00 21.85           N  
-ATOM   2097  CA  LEU A 367       0.997 -15.727 -40.753  1.00 21.99           C  
-ATOM   2098  C   LEU A 367      -0.336 -15.891 -40.033  1.00 20.28           C  
-ATOM   2099  O   LEU A 367      -0.433 -16.635 -39.058  1.00 23.79           O  
-ATOM   2100  CB  LEU A 367       1.627 -17.083 -41.080  1.00 16.33           C  
-ATOM   2101  CG  LEU A 367       1.007 -17.852 -42.251  1.00 11.94           C  
-ATOM   2102  CD1 LEU A 367       1.187 -17.085 -43.550  1.00 18.49           C  
-ATOM   2103  CD2 LEU A 367       1.597 -19.249 -42.372  1.00  9.15           C  
-ATOM   2104  N   LEU A 368      -1.349 -15.177 -40.513  1.00 13.16           N  
-ATOM   2105  CA  LEU A 368      -2.628 -15.054 -39.817  1.00 19.68           C  
-ATOM   2106  C   LEU A 368      -3.244 -16.406 -39.474  1.00 20.21           C  
-ATOM   2107  O   LEU A 368      -3.208 -17.338 -40.273  1.00 17.81           O  
-ATOM   2108  CB  LEU A 368      -3.604 -14.224 -40.653  1.00 23.04           C  
-ATOM   2109  CG  LEU A 368      -3.308 -12.720 -40.733  1.00 22.34           C  
-ATOM   2110  CD1 LEU A 368      -2.966 -12.163 -39.359  1.00 19.14           C  
-ATOM   2111  CD2 LEU A 368      -2.195 -12.403 -41.726  1.00 26.16           C  
-ATOM   2112  N   THR A 369      -3.809 -16.498 -38.273  1.00 18.75           N  
-ATOM   2113  CA  THR A 369      -4.225 -17.781 -37.720  1.00 19.16           C  
-ATOM   2114  C   THR A 369      -5.737 -17.943 -37.598  1.00 23.82           C  
-ATOM   2115  O   THR A 369      -6.230 -19.056 -37.414  1.00 26.14           O  
-ATOM   2116  CB  THR A 369      -3.606 -18.004 -36.331  1.00 19.67           C  
-ATOM   2117  OG1 THR A 369      -4.094 -17.006 -35.426  1.00 21.00           O  
-ATOM   2118  CG2 THR A 369      -2.090 -17.922 -36.407  1.00 19.24           C  
-ATOM   2119  N   THR A 370      -6.475 -16.843 -37.699  1.00 23.81           N  
-ATOM   2120  CA  THR A 370      -7.925 -16.905 -37.565  1.00 19.00           C  
-ATOM   2121  C   THR A 370      -8.558 -17.510 -38.826  1.00 24.09           C  
-ATOM   2122  O   THR A 370      -9.763 -17.756 -38.875  1.00 23.93           O  
-ATOM   2123  CB  THR A 370      -8.519 -15.514 -37.276  1.00 18.05           C  
-ATOM   2124  OG1 THR A 370      -9.866 -15.651 -36.808  1.00 37.25           O  
-ATOM   2125  CG2 THR A 370      -8.497 -14.652 -38.513  1.00 22.21           C  
-ATOM   2126  N   LYS A 371      -7.725 -17.738 -39.839  1.00 27.49           N  
-ATOM   2127  CA  LYS A 371      -8.067 -18.559 -40.999  1.00 29.24           C  
-ATOM   2128  C   LYS A 371      -6.763 -19.051 -41.622  1.00 26.92           C  
-ATOM   2129  O   LYS A 371      -5.715 -18.434 -41.432  1.00 29.45           O  
-ATOM   2130  CB  LYS A 371      -8.891 -17.781 -42.026  1.00 27.63           C  
-ATOM   2131  CG  LYS A 371      -8.050 -17.108 -43.092  1.00 37.81           C  
-ATOM   2132  CD  LYS A 371      -8.872 -16.725 -44.305  1.00 46.92           C  
-ATOM   2133  CE  LYS A 371      -7.983 -16.104 -45.370  1.00 57.44           C  
-ATOM   2134  NZ  LYS A 371      -8.753 -15.657 -46.561  1.00 60.66           N  
-ATOM   2135  N   ARG A 372      -6.816 -20.155 -42.359  1.00 25.49           N  
-ATOM   2136  CA  ARG A 372      -5.603 -20.715 -42.948  1.00 20.31           C  
-ATOM   2137  C   ARG A 372      -5.148 -19.927 -44.174  1.00 20.82           C  
-ATOM   2138  O   ARG A 372      -5.935 -19.672 -45.085  1.00 30.97           O  
-ATOM   2139  CB  ARG A 372      -5.811 -22.181 -43.322  1.00 23.78           C  
-ATOM   2140  CG  ARG A 372      -4.609 -22.800 -44.010  1.00 25.78           C  
-ATOM   2141  CD  ARG A 372      -4.776 -24.294 -44.196  1.00 36.58           C  
-ATOM   2142  NE  ARG A 372      -4.833 -25.006 -42.923  1.00 34.49           N  
-ATOM   2143  CZ  ARG A 372      -3.764 -25.340 -42.208  1.00 21.61           C  
-ATOM   2144  NH1 ARG A 372      -2.550 -25.015 -42.635  1.00 13.64           N  
-ATOM   2145  NH2 ARG A 372      -3.910 -25.991 -41.062  1.00 24.25           N  
-ATOM   2146  N   VAL A 373      -3.871 -19.552 -44.191  1.00 15.60           N  
-ATOM   2147  CA  VAL A 373      -3.310 -18.745 -45.274  1.00 16.52           C  
-ATOM   2148  C   VAL A 373      -2.438 -19.583 -46.217  1.00 24.81           C  
-ATOM   2149  O   VAL A 373      -1.677 -20.446 -45.777  1.00 21.68           O  
-ATOM   2150  CB  VAL A 373      -2.487 -17.561 -44.711  1.00 15.87           C  
-ATOM   2151  CG1 VAL A 373      -1.731 -16.837 -45.816  1.00 10.09           C  
-ATOM   2152  CG2 VAL A 373      -3.398 -16.595 -43.969  1.00 16.29           C  
-ATOM   2153  N   PHE A 374      -2.566 -19.313 -47.516  1.00 30.71           N  
-ATOM   2154  CA  PHE A 374      -1.886 -20.062 -48.573  1.00 21.20           C  
-ATOM   2155  C   PHE A 374      -0.378 -19.777 -48.634  1.00 27.98           C  
-ATOM   2156  O   PHE A 374       0.108 -19.080 -49.536  1.00 34.63           O  
-ATOM   2157  CB  PHE A 374      -2.541 -19.741 -49.920  1.00 21.08           C  
-ATOM   2158  CG  PHE A 374      -2.210 -20.719 -51.007  1.00 27.39           C  
-ATOM   2159  CD1 PHE A 374      -1.816 -22.009 -50.700  1.00 27.85           C  
-ATOM   2160  CD2 PHE A 374      -2.285 -20.344 -52.338  1.00 22.22           C  
-ATOM   2161  CE1 PHE A 374      -1.509 -22.909 -51.701  1.00 28.25           C  
-ATOM   2162  CE2 PHE A 374      -1.979 -21.235 -53.341  1.00 16.14           C  
-ATOM   2163  CZ  PHE A 374      -1.590 -22.521 -53.023  1.00 27.19           C  
-ATOM   2164  N   TRP A 375       0.358 -20.341 -47.682  1.00 19.04           N  
-ATOM   2165  CA  TRP A 375       1.781 -20.054 -47.542  1.00 22.65           C  
-ATOM   2166  C   TRP A 375       2.593 -20.476 -48.756  1.00 24.13           C  
-ATOM   2167  O   TRP A 375       3.491 -19.752 -49.189  1.00 31.05           O  
-ATOM   2168  CB  TRP A 375       2.352 -20.732 -46.298  1.00 21.72           C  
-ATOM   2169  CG  TRP A 375       3.809 -20.439 -46.123  1.00 26.71           C  
-ATOM   2170  CD1 TRP A 375       4.362 -19.265 -45.694  1.00 27.30           C  
-ATOM   2171  CD2 TRP A 375       4.901 -21.323 -46.390  1.00 22.12           C  
-ATOM   2172  NE1 TRP A 375       5.731 -19.367 -45.671  1.00 21.98           N  
-ATOM   2173  CE2 TRP A 375       6.087 -20.619 -46.096  1.00 24.88           C  
-ATOM   2174  CE3 TRP A 375       4.992 -22.642 -46.846  1.00 36.03           C  
-ATOM   2175  CZ2 TRP A 375       7.347 -21.193 -46.238  1.00 49.11           C  
-ATOM   2176  CZ3 TRP A 375       6.250 -23.211 -46.990  1.00 49.86           C  
-ATOM   2177  CH2 TRP A 375       7.409 -22.487 -46.686  1.00 51.34           C  
-ATOM   2178  N   LYS A 376       2.290 -21.657 -49.284  1.00 19.43           N  
-ATOM   2179  CA  LYS A 376       2.918 -22.139 -50.507  1.00 22.49           C  
-ATOM   2180  C   LYS A 376       2.739 -21.107 -51.610  1.00 29.16           C  
-ATOM   2181  O   LYS A 376       3.656 -20.828 -52.389  1.00 29.91           O  
-ATOM   2182  CB  LYS A 376       2.315 -23.478 -50.925  1.00 34.97           C  
-ATOM   2183  CG  LYS A 376       2.835 -24.007 -52.250  1.00 30.42           C  
-ATOM   2184  CD  LYS A 376       1.923 -25.099 -52.783  1.00 37.46           C  
-ATOM   2185  CE  LYS A 376       2.421 -25.653 -54.107  1.00 45.94           C  
-ATOM   2186  NZ  LYS A 376       3.623 -26.517 -53.947  1.00 44.98           N  
-ATOM   2187  N   GLY A 377       1.542 -20.534 -51.646  1.00 24.22           N  
-ATOM   2188  CA  GLY A 377       1.221 -19.462 -52.563  1.00 21.12           C  
-ATOM   2189  C   GLY A 377       2.094 -18.238 -52.362  1.00 24.08           C  
-ATOM   2190  O   GLY A 377       2.678 -17.738 -53.328  1.00 25.52           O  
-ATOM   2191  N   VAL A 378       2.201 -17.747 -51.125  1.00 19.54           N  
-ATOM   2192  CA  VAL A 378       2.982 -16.522 -50.908  1.00 23.74           C  
-ATOM   2193  C   VAL A 378       4.461 -16.752 -51.233  1.00 27.32           C  
-ATOM   2194  O   VAL A 378       5.124 -15.873 -51.800  1.00 26.65           O  
-ATOM   2195  CB  VAL A 378       2.816 -15.954 -49.456  1.00 19.01           C  
-ATOM   2196  CG1 VAL A 378       1.535 -16.448 -48.820  1.00 19.94           C  
-ATOM   2197  CG2 VAL A 378       4.007 -16.278 -48.568  1.00 24.10           C  
-ATOM   2198  N   LEU A 379       4.958 -17.947 -50.920  1.00 16.27           N  
-ATOM   2199  CA  LEU A 379       6.352 -18.286 -51.164  1.00 17.78           C  
-ATOM   2200  C   LEU A 379       6.641 -18.357 -52.652  1.00 20.26           C  
-ATOM   2201  O   LEU A 379       7.528 -17.668 -53.162  1.00 23.40           O  
-ATOM   2202  CB  LEU A 379       6.707 -19.617 -50.491  1.00 22.29           C  
-ATOM   2203  CG  LEU A 379       8.135 -20.112 -50.715  1.00 18.56           C  
-ATOM   2204  CD1 LEU A 379       9.143 -19.089 -50.217  1.00 18.25           C  
-ATOM   2205  CD2 LEU A 379       8.354 -21.452 -50.036  1.00 23.35           C  
-ATOM   2206  N   GLU A 380       5.881 -19.197 -53.344  1.00 18.62           N  
-ATOM   2207  CA  GLU A 380       6.077 -19.390 -54.773  1.00 26.42           C  
-ATOM   2208  C   GLU A 380       5.904 -18.082 -55.536  1.00 26.43           C  
-ATOM   2209  O   GLU A 380       6.677 -17.792 -56.447  1.00 23.22           O  
-ATOM   2210  CB  GLU A 380       5.115 -20.452 -55.314  1.00 26.66           C  
-ATOM   2211  CG  GLU A 380       5.787 -21.468 -56.217  1.00 36.81           C  
-ATOM   2212  CD  GLU A 380       6.875 -22.248 -55.500  1.00 42.55           C  
-ATOM   2213  OE1 GLU A 380       7.994 -22.362 -56.048  1.00 37.91           O  
-ATOM   2214  OE2 GLU A 380       6.608 -22.746 -54.385  1.00 28.05           O  
-ATOM   2215  N   GLU A 381       4.906 -17.287 -55.153  1.00 23.05           N  
-ATOM   2216  CA  GLU A 381       4.667 -16.014 -55.829  1.00 19.85           C  
-ATOM   2217  C   GLU A 381       5.775 -15.009 -55.534  1.00 19.75           C  
-ATOM   2218  O   GLU A 381       6.112 -14.197 -56.390  1.00 17.24           O  
-ATOM   2219  CB  GLU A 381       3.313 -15.409 -55.437  1.00 26.15           C  
-ATOM   2220  CG  GLU A 381       2.907 -14.243 -56.345  1.00 20.91           C  
-ATOM   2221  CD  GLU A 381       1.813 -13.368 -55.761  1.00 26.82           C  
-ATOM   2222  OE1 GLU A 381       0.887 -12.990 -56.511  1.00 29.01           O  
-ATOM   2223  OE2 GLU A 381       1.891 -13.037 -54.560  1.00 31.47           O  
-ATOM   2224  N   LEU A 382       6.339 -15.053 -54.329  1.00 26.81           N  
-ATOM   2225  CA  LEU A 382       7.421 -14.130 -53.993  1.00 20.76           C  
-ATOM   2226  C   LEU A 382       8.690 -14.475 -54.766  1.00 15.92           C  
-ATOM   2227  O   LEU A 382       9.338 -13.594 -55.329  1.00 20.61           O  
-ATOM   2228  CB  LEU A 382       7.695 -14.126 -52.485  1.00 17.16           C  
-ATOM   2229  CG  LEU A 382       8.709 -13.072 -52.021  1.00 18.10           C  
-ATOM   2230  CD1 LEU A 382       8.335 -11.689 -52.535  1.00 18.63           C  
-ATOM   2231  CD2 LEU A 382       8.826 -13.060 -50.506  1.00 12.47           C  
-ATOM   2232  N   LEU A 383       9.043 -15.756 -54.789  1.00 14.39           N  
-ATOM   2233  CA  LEU A 383      10.179 -16.215 -55.589  1.00 17.63           C  
-ATOM   2234  C   LEU A 383       9.975 -15.828 -57.053  1.00 21.19           C  
-ATOM   2235  O   LEU A 383      10.882 -15.316 -57.720  1.00 24.32           O  
-ATOM   2236  CB  LEU A 383      10.359 -17.731 -55.448  1.00 21.61           C  
-ATOM   2237  CG  LEU A 383      11.313 -18.236 -54.357  1.00 18.92           C  
-ATOM   2238  CD1 LEU A 383      11.317 -17.314 -53.152  1.00 21.39           C  
-ATOM   2239  CD2 LEU A 383      10.943 -19.653 -53.939  1.00 19.29           C  
-ATOM   2240  N   TRP A 384       8.755 -16.066 -57.523  1.00 20.05           N  
-ATOM   2241  CA  TRP A 384       8.301 -15.674 -58.854  1.00 22.76           C  
-ATOM   2242  C   TRP A 384       8.551 -14.191 -59.129  1.00 21.34           C  
-ATOM   2243  O   TRP A 384       9.000 -13.822 -60.215  1.00 17.64           O  
-ATOM   2244  CB  TRP A 384       6.810 -16.005 -58.995  1.00 31.64           C  
-ATOM   2245  CG  TRP A 384       6.241 -15.850 -60.367  1.00 23.45           C  
-ATOM   2246  CD1 TRP A 384       6.548 -16.588 -61.472  1.00 25.43           C  
-ATOM   2247  CD2 TRP A 384       5.230 -14.924 -60.770  1.00 19.62           C  
-ATOM   2248  NE1 TRP A 384       5.807 -16.163 -62.545  1.00 23.65           N  
-ATOM   2249  CE2 TRP A 384       4.987 -15.142 -62.140  1.00 26.25           C  
-ATOM   2250  CE3 TRP A 384       4.513 -13.924 -60.109  1.00 18.37           C  
-ATOM   2251  CZ2 TRP A 384       4.056 -14.398 -62.861  1.00 27.75           C  
-ATOM   2252  CZ3 TRP A 384       3.589 -13.186 -60.826  1.00 29.70           C  
-ATOM   2253  CH2 TRP A 384       3.369 -13.427 -62.187  1.00 29.96           C  
-ATOM   2254  N   PHE A 385       8.255 -13.350 -58.138  1.00 24.97           N  
-ATOM   2255  CA  PHE A 385       8.522 -11.915 -58.217  1.00 20.89           C  
-ATOM   2256  C   PHE A 385      10.007 -11.637 -58.360  1.00 20.44           C  
-ATOM   2257  O   PHE A 385      10.427 -10.889 -59.241  1.00 25.44           O  
-ATOM   2258  CB  PHE A 385       8.005 -11.189 -56.976  1.00 16.97           C  
-ATOM   2259  CG  PHE A 385       6.521 -11.009 -56.949  1.00 19.44           C  
-ATOM   2260  CD1 PHE A 385       5.787 -10.992 -58.123  1.00 22.38           C  
-ATOM   2261  CD2 PHE A 385       5.857 -10.850 -55.744  1.00 19.71           C  
-ATOM   2262  CE1 PHE A 385       4.417 -10.824 -58.094  1.00 20.78           C  
-ATOM   2263  CE2 PHE A 385       4.488 -10.681 -55.709  1.00 15.64           C  
-ATOM   2264  CZ  PHE A 385       3.767 -10.667 -56.885  1.00 19.84           C  
-ATOM   2265  N   ILE A 386      10.792 -12.235 -57.469  1.00 17.30           N  
-ATOM   2266  CA  ILE A 386      12.230 -11.998 -57.429  1.00 20.26           C  
-ATOM   2267  C   ILE A 386      12.897 -12.377 -58.746  1.00 23.69           C  
-ATOM   2268  O   ILE A 386      13.832 -11.710 -59.186  1.00 19.71           O  
-ATOM   2269  CB  ILE A 386      12.889 -12.771 -56.268  1.00 17.47           C  
-ATOM   2270  CG1 ILE A 386      12.293 -12.316 -54.934  1.00 15.51           C  
-ATOM   2271  CG2 ILE A 386      14.398 -12.565 -56.263  1.00 17.29           C  
-ATOM   2272  CD1 ILE A 386      13.010 -12.862 -53.739  1.00 14.61           C  
-ATOM   2273  N   ARG A 387      12.406 -13.434 -59.385  1.00 25.04           N  
-ATOM   2274  CA  ARG A 387      12.984 -13.852 -60.662  1.00 19.27           C  
-ATOM   2275  C   ARG A 387      12.655 -12.873 -61.788  1.00 24.51           C  
-ATOM   2276  O   ARG A 387      13.275 -12.909 -62.853  1.00 24.17           O  
-ATOM   2277  CB  ARG A 387      12.502 -15.249 -61.041  1.00 18.65           C  
-ATOM   2278  CG  ARG A 387      12.886 -16.325 -60.047  1.00 23.05           C  
-ATOM   2279  CD  ARG A 387      12.640 -17.706 -60.620  1.00 17.96           C  
-ATOM   2280  NE  ARG A 387      12.651 -18.722 -59.576  1.00 15.72           N  
-ATOM   2281  CZ  ARG A 387      11.561 -19.160 -58.957  1.00 21.64           C  
-ATOM   2282  NH1 ARG A 387      10.370 -18.674 -59.286  1.00 27.62           N  
-ATOM   2283  NH2 ARG A 387      11.658 -20.086 -58.015  1.00 21.39           N  
-ATOM   2284  N   GLY A 388      11.685 -11.995 -61.546  1.00 28.29           N  
-ATOM   2285  CA  GLY A 388      11.235 -11.055 -62.557  1.00 24.86           C  
-ATOM   2286  C   GLY A 388      10.373 -11.768 -63.578  1.00 35.28           C  
-ATOM   2287  O   GLY A 388      10.271 -11.351 -64.733  1.00 33.38           O  
-ATOM   2288  N   ASP A 389       9.749 -12.856 -63.140  1.00 28.53           N  
-ATOM   2289  CA  ASP A 389       8.949 -13.693 -64.024  1.00 23.74           C  
-ATOM   2290  C   ASP A 389       7.569 -13.091 -64.264  1.00 27.84           C  
-ATOM   2291  O   ASP A 389       6.910 -12.622 -63.334  1.00 25.19           O  
-ATOM   2292  CB  ASP A 389       8.819 -15.098 -63.435  1.00 29.71           C  
-ATOM   2293  CG  ASP A 389       8.434 -16.138 -64.471  1.00 29.14           C  
-ATOM   2294  OD1 ASP A 389       8.080 -15.762 -65.607  1.00 28.56           O  
-ATOM   2295  OD2 ASP A 389       8.484 -17.341 -64.140  1.00 24.77           O  
-ATOM   2296  N   THR A 390       7.137 -13.109 -65.521  1.00 33.47           N  
-ATOM   2297  CA  THR A 390       5.832 -12.576 -65.894  1.00 27.75           C  
-ATOM   2298  C   THR A 390       4.945 -13.669 -66.483  1.00 21.38           C  
-ATOM   2299  O   THR A 390       3.903 -13.393 -67.074  1.00 23.24           O  
-ATOM   2300  CB  THR A 390       5.969 -11.424 -66.904  1.00 24.26           C  
-ATOM   2301  OG1 THR A 390       6.665 -11.888 -68.067  1.00 26.21           O  
-ATOM   2302  CG2 THR A 390       6.746 -10.276 -66.286  1.00 25.01           C  
-ATOM   2303  N   ASN A 391       5.372 -14.914 -66.304  1.00 23.34           N  
-ATOM   2304  CA  ASN A 391       4.654 -16.075 -66.810  1.00 24.64           C  
-ATOM   2305  C   ASN A 391       3.833 -16.744 -65.708  1.00 32.61           C  
-ATOM   2306  O   ASN A 391       4.379 -17.477 -64.881  1.00 38.45           O  
-ATOM   2307  CB  ASN A 391       5.649 -17.068 -67.415  1.00 27.93           C  
-ATOM   2308  CG  ASN A 391       4.983 -18.126 -68.265  1.00 30.79           C  
-ATOM   2309  OD1 ASN A 391       3.898 -18.607 -67.945  1.00 42.67           O  
-ATOM   2310  ND2 ASN A 391       5.633 -18.494 -69.362  1.00 29.74           N  
-ATOM   2311  N   ALA A 392       2.526 -16.494 -65.702  1.00 28.75           N  
-ATOM   2312  CA  ALA A 392       1.653 -16.994 -64.643  1.00 27.12           C  
-ATOM   2313  C   ALA A 392       1.549 -18.513 -64.662  1.00 30.03           C  
-ATOM   2314  O   ALA A 392       1.248 -19.137 -63.646  1.00 30.02           O  
-ATOM   2315  CB  ALA A 392       0.267 -16.372 -64.758  1.00 28.70           C  
-ATOM   2316  N   ASN A 393       1.802 -19.105 -65.823  1.00 27.83           N  
-ATOM   2317  CA  ASN A 393       1.704 -20.551 -65.970  1.00 25.13           C  
-ATOM   2318  C   ASN A 393       2.744 -21.280 -65.129  1.00 36.34           C  
-ATOM   2319  O   ASN A 393       2.512 -22.406 -64.685  1.00 45.81           O  
-ATOM   2320  CB  ASN A 393       1.836 -20.942 -67.439  1.00 22.69           C  
-ATOM   2321  CG  ASN A 393       0.745 -20.335 -68.297  1.00 32.74           C  
-ATOM   2322  OD1 ASN A 393      -0.420 -20.280 -67.895  1.00 33.51           O  
-ATOM   2323  ND2 ASN A 393       1.114 -19.875 -69.486  1.00 32.89           N  
-ATOM   2324  N   HIS A 394       3.886 -20.632 -64.915  1.00 35.97           N  
-ATOM   2325  CA  HIS A 394       4.920 -21.159 -64.028  1.00 28.19           C  
-ATOM   2326  C   HIS A 394       4.400 -21.282 -62.600  1.00 34.43           C  
-ATOM   2327  O   HIS A 394       4.789 -22.187 -61.867  1.00 39.32           O  
-ATOM   2328  CB  HIS A 394       6.162 -20.269 -64.056  1.00 25.64           C  
-ATOM   2329  CG  HIS A 394       6.830 -20.216 -65.391  1.00 25.05           C  
-ATOM   2330  ND1 HIS A 394       7.761 -19.254 -65.720  1.00 27.43           N  
-ATOM   2331  CD2 HIS A 394       6.703 -21.007 -66.481  1.00 31.42           C  
-ATOM   2332  CE1 HIS A 394       8.177 -19.455 -66.957  1.00 27.72           C  
-ATOM   2333  NE2 HIS A 394       7.552 -20.513 -67.441  1.00 28.17           N  
-ATOM   2334  N   LEU A 395       3.533 -20.357 -62.204  1.00 27.65           N  
-ATOM   2335  CA  LEU A 395       2.891 -20.436 -60.900  1.00 30.14           C  
-ATOM   2336  C   LEU A 395       1.782 -21.474 -60.921  1.00 34.27           C  
-ATOM   2337  O   LEU A 395       1.557 -22.180 -59.938  1.00 34.43           O  
-ATOM   2338  CB  LEU A 395       2.319 -19.079 -60.483  1.00 31.35           C  
-ATOM   2339  CG  LEU A 395       3.272 -18.042 -59.889  1.00 33.48           C  
-ATOM   2340  CD1 LEU A 395       2.500 -16.800 -59.470  1.00 26.83           C  
-ATOM   2341  CD2 LEU A 395       4.044 -18.622 -58.713  1.00 29.23           C  
-ATOM   2342  N   SER A 396       1.091 -21.558 -62.051  1.00 38.84           N  
-ATOM   2343  CA  SER A 396      -0.093 -22.396 -62.164  1.00 37.53           C  
-ATOM   2344  C   SER A 396       0.240 -23.883 -62.119  1.00 38.79           C  
-ATOM   2345  O   SER A 396      -0.451 -24.653 -61.451  1.00 31.73           O  
-ATOM   2346  CB  SER A 396      -0.843 -22.068 -63.456  1.00 36.73           C  
-ATOM   2347  OG  SER A 396      -2.235 -22.311 -63.323  1.00 45.08           O  
-ATOM   2348  N   GLU A 397       1.292 -24.284 -62.830  1.00 41.99           N  
-ATOM   2349  CA  GLU A 397       1.656 -25.699 -62.908  1.00 45.90           C  
-ATOM   2350  C   GLU A 397       2.441 -26.150 -61.667  1.00 40.33           C  
-ATOM   2351  O   GLU A 397       2.784 -27.328 -61.523  1.00 48.34           O  
-ATOM   2352  CB  GLU A 397       2.440 -25.981 -64.202  1.00 46.92           C  
-ATOM   2353  CG  GLU A 397       3.934 -26.249 -64.053  1.00 61.05           C  
-ATOM   2354  CD  GLU A 397       4.772 -24.992 -64.130  1.00 69.55           C  
-ATOM   2355  OE1 GLU A 397       4.820 -24.369 -65.214  1.00 54.53           O  
-ATOM   2356  OE2 GLU A 397       5.385 -24.629 -63.103  1.00 68.06           O  
-ATOM   2357  N   LYS A 398       2.696 -25.214 -60.758  1.00 37.31           N  
-ATOM   2358  CA  LYS A 398       3.253 -25.557 -59.454  1.00 33.93           C  
-ATOM   2359  C   LYS A 398       2.152 -25.688 -58.405  1.00 30.10           C  
-ATOM   2360  O   LYS A 398       2.424 -26.005 -57.250  1.00 26.64           O  
-ATOM   2361  CB  LYS A 398       4.273 -24.515 -59.004  1.00 34.78           C  
-ATOM   2362  CG  LYS A 398       5.582 -24.553 -59.770  1.00 46.51           C  
-ATOM   2363  CD  LYS A 398       6.644 -23.722 -59.073  1.00 36.49           C  
-ATOM   2364  CE  LYS A 398       7.910 -23.636 -59.903  1.00 41.89           C  
-ATOM   2365  NZ  LYS A 398       7.635 -23.027 -61.233  1.00 39.38           N  
-ATOM   2366  N   GLY A 399       0.909 -25.443 -58.810  1.00 27.91           N  
-ATOM   2367  CA  GLY A 399      -0.226 -25.592 -57.916  1.00 26.03           C  
-ATOM   2368  C   GLY A 399      -0.726 -24.279 -57.350  1.00 29.08           C  
-ATOM   2369  O   GLY A 399      -1.520 -24.258 -56.408  1.00 26.21           O  
-ATOM   2370  N   VAL A 400      -0.261 -23.179 -57.932  1.00 35.59           N  
-ATOM   2371  CA  VAL A 400      -0.639 -21.844 -57.478  1.00 32.21           C  
-ATOM   2372  C   VAL A 400      -1.424 -21.117 -58.574  1.00 38.51           C  
-ATOM   2373  O   VAL A 400      -0.844 -20.451 -59.436  1.00 37.19           O  
-ATOM   2374  CB  VAL A 400       0.604 -21.026 -57.074  1.00 28.88           C  
-ATOM   2375  CG1 VAL A 400       0.202 -19.711 -56.457  1.00 30.41           C  
-ATOM   2376  CG2 VAL A 400       1.459 -21.820 -56.095  1.00 34.62           C  
-ATOM   2377  N   LYS A 401      -2.747 -21.251 -58.529  1.00 38.67           N  
-ATOM   2378  CA  LYS A 401      -3.620 -20.772 -59.601  1.00 47.06           C  
-ATOM   2379  C   LYS A 401      -4.180 -19.386 -59.322  1.00 44.47           C  
-ATOM   2380  O   LYS A 401      -5.247 -19.021 -59.813  1.00 51.07           O  
-ATOM   2381  CB  LYS A 401      -4.773 -21.753 -59.813  1.00 36.34           C  
-ATOM   2382  CG  LYS A 401      -4.341 -23.141 -60.241  1.00 37.76           C  
-ATOM   2383  CD  LYS A 401      -5.284 -24.197 -59.692  1.00 45.92           C  
-ATOM   2384  CE  LYS A 401      -5.259 -24.213 -58.168  1.00 57.65           C  
-ATOM   2385  NZ  LYS A 401      -6.119 -25.289 -57.600  1.00 46.21           N  
-ATOM   2386  N   ILE A 402      -3.440 -18.615 -58.539  1.00 39.81           N  
-ATOM   2387  CA  ILE A 402      -3.914 -17.334 -58.038  1.00 41.53           C  
-ATOM   2388  C   ILE A 402      -3.944 -16.236 -59.097  1.00 43.46           C  
-ATOM   2389  O   ILE A 402      -4.491 -15.159 -58.866  1.00 46.68           O  
-ATOM   2390  CB  ILE A 402      -3.034 -16.870 -56.879  1.00 35.20           C  
-ATOM   2391  CG1 ILE A 402      -1.698 -16.357 -57.421  1.00 39.50           C  
-ATOM   2392  CG2 ILE A 402      -2.823 -18.017 -55.909  1.00 40.22           C  
-ATOM   2393  CD1 ILE A 402      -0.632 -16.166 -56.370  1.00 31.67           C  
-ATOM   2394  N   TRP A 403      -3.353 -16.507 -60.254  1.00 42.35           N  
-ATOM   2395  CA  TRP A 403      -3.274 -15.506 -61.311  1.00 46.27           C  
-ATOM   2396  C   TRP A 403      -4.134 -15.862 -62.518  1.00 47.80           C  
-ATOM   2397  O   TRP A 403      -4.411 -15.003 -63.355  1.00 45.11           O  
-ATOM   2398  CB  TRP A 403      -1.822 -15.311 -61.757  1.00 42.10           C  
-ATOM   2399  CG  TRP A 403      -1.102 -14.226 -61.021  1.00 32.18           C  
-ATOM   2400  CD1 TRP A 403      -0.361 -14.358 -59.885  1.00 30.75           C  
-ATOM   2401  CD2 TRP A 403      -1.050 -12.840 -61.375  1.00 43.32           C  
-ATOM   2402  NE1 TRP A 403       0.149 -13.141 -59.507  1.00 35.13           N  
-ATOM   2403  CE2 TRP A 403      -0.260 -12.191 -60.406  1.00 43.36           C  
-ATOM   2404  CE3 TRP A 403      -1.597 -12.083 -62.416  1.00 46.43           C  
-ATOM   2405  CZ2 TRP A 403      -0.002 -10.824 -60.446  1.00 44.81           C  
-ATOM   2406  CZ3 TRP A 403      -1.339 -10.724 -62.455  1.00 48.18           C  
-ATOM   2407  CH2 TRP A 403      -0.549 -10.109 -61.476  1.00 47.58           C  
-ATOM   2408  N   ASP A 404      -4.558 -17.121 -62.594  1.00 52.89           N  
-ATOM   2409  CA  ASP A 404      -5.255 -17.647 -63.768  1.00 55.89           C  
-ATOM   2410  C   ASP A 404      -6.422 -16.779 -64.228  1.00 42.13           C  
-ATOM   2411  O   ASP A 404      -6.490 -16.378 -65.391  1.00 47.14           O  
-ATOM   2412  CB  ASP A 404      -5.754 -19.065 -63.484  1.00 62.25           C  
-ATOM   2413  CG  ASP A 404      -4.621 -20.055 -63.269  1.00 59.54           C  
-ATOM   2414  OD1 ASP A 404      -3.443 -19.672 -63.434  1.00 56.79           O  
-ATOM   2415  OD2 ASP A 404      -4.918 -21.223 -62.947  1.00 49.22           O  
-ATOM   2416  N   LYS A 405      -7.323 -16.471 -63.304  1.00 35.01           N  
-ATOM   2417  CA  LYS A 405      -8.516 -15.695 -63.622  1.00 41.80           C  
-ATOM   2418  C   LYS A 405      -8.221 -14.303 -64.190  1.00 43.50           C  
-ATOM   2419  O   LYS A 405      -9.116 -13.655 -64.729  1.00 43.81           O  
-ATOM   2420  CB  LYS A 405      -9.396 -15.558 -62.379  1.00 40.73           C  
-ATOM   2421  CG  LYS A 405     -10.219 -16.795 -62.059  1.00 51.07           C  
-ATOM   2422  CD  LYS A 405     -11.070 -16.571 -60.824  1.00 55.99           C  
-ATOM   2423  CE  LYS A 405     -11.846 -17.823 -60.463  1.00 54.51           C  
-ATOM   2424  NZ  LYS A 405     -12.540 -17.677 -59.156  1.00 48.10           N  
-ATOM   2425  N   ASN A 406      -6.979 -13.843 -64.078  1.00 44.47           N  
-ATOM   2426  CA  ASN A 406      -6.619 -12.524 -64.594  1.00 41.70           C  
-ATOM   2427  C   ASN A 406      -5.662 -12.598 -65.774  1.00 31.57           C  
-ATOM   2428  O   ASN A 406      -5.159 -11.578 -66.239  1.00 31.44           O  
-ATOM   2429  CB  ASN A 406      -6.007 -11.661 -63.489  1.00 44.06           C  
-ATOM   2430  CG  ASN A 406      -7.025 -11.247 -62.446  1.00 46.33           C  
-ATOM   2431  OD1 ASN A 406      -6.800 -11.403 -61.246  1.00 57.59           O  
-ATOM   2432  ND2 ASN A 406      -8.156 -10.720 -62.900  1.00 40.07           N  
-ATOM   2433  N   VAL A 407      -5.405 -13.810 -66.255  1.00 30.65           N  
-ATOM   2434  CA  VAL A 407      -4.566 -13.986 -67.437  1.00 40.04           C  
-ATOM   2435  C   VAL A 407      -5.234 -14.915 -68.447  1.00 46.50           C  
-ATOM   2436  O   VAL A 407      -4.587 -15.429 -69.362  1.00 43.49           O  
-ATOM   2437  CB  VAL A 407      -3.170 -14.538 -67.077  1.00 40.41           C  
-ATOM   2438  CG1 VAL A 407      -2.350 -13.482 -66.350  1.00 40.36           C  
-ATOM   2439  CG2 VAL A 407      -3.291 -15.806 -66.249  1.00 43.01           C  
-ATOM   2440  N   THR A 408      -6.535 -15.120 -68.274  1.00 43.96           N  
-ATOM   2441  CA  THR A 408      -7.328 -15.847 -69.254  1.00 39.87           C  
-ATOM   2442  C   THR A 408      -7.363 -15.061 -70.557  1.00 48.89           C  
-ATOM   2443  O   THR A 408      -7.156 -13.850 -70.553  1.00 54.44           O  
-ATOM   2444  CB  THR A 408      -8.772 -16.085 -68.763  1.00 44.68           C  
-ATOM   2445  OG1 THR A 408      -9.384 -14.829 -68.448  1.00 41.32           O  
-ATOM   2446  CG2 THR A 408      -8.787 -16.966 -67.531  1.00 36.03           C  
-ATOM   2447  N   ARG A 409      -7.616 -15.748 -71.666  1.00 41.19           N  
-ATOM   2448  CA  ARG A 409      -7.772 -15.086 -72.957  1.00 42.73           C  
-ATOM   2449  C   ARG A 409      -8.873 -14.028 -72.892  1.00 47.32           C  
-ATOM   2450  O   ARG A 409      -8.722 -12.917 -73.411  1.00 50.52           O  
-ATOM   2451  CB  ARG A 409      -8.078 -16.120 -74.047  1.00 36.90           C  
-ATOM   2452  CG  ARG A 409      -8.638 -15.554 -75.342  1.00 36.20           C  
-ATOM   2453  CD  ARG A 409      -7.548 -15.082 -76.293  1.00 38.08           C  
-ATOM   2454  NE  ARG A 409      -7.006 -13.777 -75.926  1.00 44.62           N  
-ATOM   2455  CZ  ARG A 409      -5.760 -13.570 -75.511  1.00 48.88           C  
-ATOM   2456  NH1 ARG A 409      -4.910 -14.583 -75.411  1.00 43.56           N  
-ATOM   2457  NH2 ARG A 409      -5.362 -12.343 -75.202  1.00 46.06           N  
-ATOM   2458  N   GLU A 410      -9.968 -14.383 -72.229  1.00 43.89           N  
-ATOM   2459  CA  GLU A 410     -11.115 -13.499 -72.084  1.00 48.55           C  
-ATOM   2460  C   GLU A 410     -10.757 -12.206 -71.354  1.00 50.29           C  
-ATOM   2461  O   GLU A 410     -11.082 -11.110 -71.823  1.00 51.12           O  
-ATOM   2462  CB  GLU A 410     -12.244 -14.229 -71.350  1.00 58.00           C  
-ATOM   2463  CG  GLU A 410     -13.637 -13.720 -71.670  1.00 75.90           C  
-ATOM   2464  CD  GLU A 410     -14.718 -14.590 -71.058  1.00 87.43           C  
-ATOM   2465  OE1 GLU A 410     -14.664 -14.832 -69.833  1.00 86.27           O  
-ATOM   2466  OE2 GLU A 410     -15.616 -15.041 -71.803  1.00 81.06           O  
-ATOM   2467  N   PHE A 411     -10.087 -12.334 -70.211  1.00 49.35           N  
-ATOM   2468  CA  PHE A 411      -9.706 -11.167 -69.415  1.00 49.69           C  
-ATOM   2469  C   PHE A 411      -8.648 -10.330 -70.126  1.00 41.17           C  
-ATOM   2470  O   PHE A 411      -8.722  -9.102 -70.134  1.00 43.85           O  
-ATOM   2471  CB  PHE A 411      -9.192 -11.590 -68.033  1.00 38.28           C  
-ATOM   2472  CG  PHE A 411      -8.992 -10.440 -67.081  1.00 40.20           C  
-ATOM   2473  CD1 PHE A 411     -10.041  -9.984 -66.297  1.00 42.75           C  
-ATOM   2474  CD2 PHE A 411      -7.763  -9.807 -66.979  1.00 41.14           C  
-ATOM   2475  CE1 PHE A 411      -9.868  -8.921 -65.423  1.00 45.68           C  
-ATOM   2476  CE2 PHE A 411      -7.582  -8.740 -66.106  1.00 44.80           C  
-ATOM   2477  CZ  PHE A 411      -8.638  -8.300 -65.328  1.00 47.46           C  
-ATOM   2478  N   LEU A 412      -7.663 -11.002 -70.714  1.00 40.80           N  
-ATOM   2479  CA  LEU A 412      -6.617 -10.330 -71.476  1.00 43.40           C  
-ATOM   2480  C   LEU A 412      -7.211  -9.530 -72.630  1.00 48.36           C  
-ATOM   2481  O   LEU A 412      -6.699  -8.467 -72.985  1.00 47.23           O  
-ATOM   2482  CB  LEU A 412      -5.596 -11.345 -72.001  1.00 38.63           C  
-ATOM   2483  CG  LEU A 412      -4.569 -11.852 -70.983  1.00 36.97           C  
-ATOM   2484  CD1 LEU A 412      -3.726 -12.985 -71.556  1.00 37.81           C  
-ATOM   2485  CD2 LEU A 412      -3.683 -10.709 -70.513  1.00 30.09           C  
-ATOM   2486  N   ASP A 413      -8.293 -10.044 -73.209  1.00 53.91           N  
-ATOM   2487  CA  ASP A 413      -8.990  -9.333 -74.274  1.00 43.97           C  
-ATOM   2488  C   ASP A 413      -9.805  -8.168 -73.721  1.00 41.11           C  
-ATOM   2489  O   ASP A 413      -9.852  -7.095 -74.324  1.00 40.58           O  
-ATOM   2490  CB  ASP A 413      -9.892 -10.289 -75.056  1.00 50.22           C  
-ATOM   2491  CG  ASP A 413      -9.117 -11.138 -76.043  1.00 51.37           C  
-ATOM   2492  OD1 ASP A 413      -8.095 -10.645 -76.568  1.00 47.26           O  
-ATOM   2493  OD2 ASP A 413      -9.527 -12.290 -76.301  1.00 46.99           O  
-ATOM   2494  N   SER A 414     -10.447  -8.378 -72.575  1.00 45.57           N  
-ATOM   2495  CA  SER A 414     -11.234  -7.320 -71.948  1.00 44.20           C  
-ATOM   2496  C   SER A 414     -10.322  -6.184 -71.491  1.00 44.42           C  
-ATOM   2497  O   SER A 414     -10.774  -5.063 -71.268  1.00 42.40           O  
-ATOM   2498  CB  SER A 414     -12.038  -7.864 -70.765  1.00 46.44           C  
-ATOM   2499  OG  SER A 414     -11.240  -7.953 -69.597  1.00 34.14           O  
-ATOM   2500  N   ARG A 415      -9.033  -6.489 -71.363  1.00 53.57           N  
-ATOM   2501  CA  ARG A 415      -8.016  -5.504 -71.007  1.00 50.56           C  
-ATOM   2502  C   ARG A 415      -7.476  -4.838 -72.277  1.00 45.68           C  
-ATOM   2503  O   ARG A 415      -6.488  -4.103 -72.239  1.00 39.48           O  
-ATOM   2504  CB  ARG A 415      -6.883  -6.173 -70.217  1.00 45.36           C  
-ATOM   2505  CG  ARG A 415      -5.922  -5.234 -69.492  1.00 43.67           C  
-ATOM   2506  CD  ARG A 415      -6.479  -4.754 -68.159  1.00 49.48           C  
-ATOM   2507  NE  ARG A 415      -5.496  -3.976 -67.407  1.00 49.52           N  
-ATOM   2508  CZ  ARG A 415      -5.451  -2.647 -67.383  1.00 52.42           C  
-ATOM   2509  NH1 ARG A 415      -4.521  -2.025 -66.672  1.00 53.44           N  
-ATOM   2510  NH2 ARG A 415      -6.340  -1.941 -68.067  1.00 52.36           N  
-ATOM   2511  N   ASN A 416      -8.148  -5.100 -73.397  1.00 46.49           N  
-ATOM   2512  CA  ASN A 416      -7.728  -4.613 -74.708  1.00 45.51           C  
-ATOM   2513  C   ASN A 416      -6.282  -5.014 -75.000  1.00 37.51           C  
-ATOM   2514  O   ASN A 416      -5.443  -4.174 -75.319  1.00 34.14           O  
-ATOM   2515  CB  ASN A 416      -7.905  -3.095 -74.800  1.00 43.14           C  
-ATOM   2516  CG  ASN A 416      -7.883  -2.590 -76.230  1.00 51.93           C  
-ATOM   2517  OD1 ASN A 416      -7.843  -3.375 -77.180  1.00 54.87           O  
-ATOM   2518  ND2 ASN A 416      -7.921  -1.273 -76.392  1.00 45.28           N  
-ATOM   2519  N   LEU A 417      -6.005  -6.308 -74.871  1.00 40.66           N  
-ATOM   2520  CA  LEU A 417      -4.674  -6.855 -75.121  1.00 40.92           C  
-ATOM   2521  C   LEU A 417      -4.739  -8.223 -75.796  1.00 40.55           C  
-ATOM   2522  O   LEU A 417      -4.406  -9.234 -75.180  1.00 41.32           O  
-ATOM   2523  CB  LEU A 417      -3.891  -6.967 -73.812  1.00 40.08           C  
-ATOM   2524  CG  LEU A 417      -2.974  -5.809 -73.431  1.00 38.77           C  
-ATOM   2525  CD1 LEU A 417      -2.519  -5.955 -71.992  1.00 32.84           C  
-ATOM   2526  CD2 LEU A 417      -1.781  -5.774 -74.369  1.00 47.63           C  
-ATOM   2527  N   PRO A 418      -5.168  -8.261 -77.068  1.00 42.46           N  
-ATOM   2528  CA  PRO A 418      -5.297  -9.537 -77.781  1.00 45.51           C  
-ATOM   2529  C   PRO A 418      -3.950 -10.149 -78.155  1.00 45.28           C  
-ATOM   2530  O   PRO A 418      -3.880 -11.344 -78.440  1.00 41.74           O  
-ATOM   2531  CB  PRO A 418      -6.087  -9.158 -79.044  1.00 48.88           C  
-ATOM   2532  CG  PRO A 418      -6.675  -7.807 -78.756  1.00 47.15           C  
-ATOM   2533  CD  PRO A 418      -5.675  -7.140 -77.874  1.00 44.93           C  
-ATOM   2534  N   HIS A 419      -2.897  -9.338 -78.147  1.00 52.11           N  
-ATOM   2535  CA  HIS A 419      -1.570  -9.797 -78.547  1.00 48.24           C  
-ATOM   2536  C   HIS A 419      -0.917 -10.676 -77.487  1.00 42.12           C  
-ATOM   2537  O   HIS A 419       0.079 -11.347 -77.754  1.00 33.78           O  
-ATOM   2538  CB  HIS A 419      -0.670  -8.598 -78.858  1.00 58.32           C  
-ATOM   2539  CG  HIS A 419      -1.010  -7.910 -80.143  1.00 97.81           C  
-ATOM   2540  ND1 HIS A 419      -0.374  -8.197 -81.332  1.00 97.22           N  
-ATOM   2541  CD2 HIS A 419      -1.926  -6.953 -80.429  1.00 92.30           C  
-ATOM   2542  CE1 HIS A 419      -0.879  -7.445 -82.293  1.00 90.13           C  
-ATOM   2543  NE2 HIS A 419      -1.822  -6.681 -81.772  1.00 90.73           N  
-ATOM   2544  N   ARG A 420      -1.487 -10.674 -76.287  1.00 41.41           N  
-ATOM   2545  CA  ARG A 420      -0.896 -11.378 -75.155  1.00 38.81           C  
-ATOM   2546  C   ARG A 420      -1.205 -12.871 -75.151  1.00 44.15           C  
-ATOM   2547  O   ARG A 420      -2.362 -13.281 -75.266  1.00 39.82           O  
-ATOM   2548  CB  ARG A 420      -1.375 -10.759 -73.843  1.00 37.15           C  
-ATOM   2549  CG  ARG A 420      -0.796  -9.384 -73.551  1.00 44.20           C  
-ATOM   2550  CD  ARG A 420       0.530  -9.479 -72.813  1.00 29.30           C  
-ATOM   2551  NE  ARG A 420       1.034  -8.160 -72.447  1.00 30.10           N  
-ATOM   2552  CZ  ARG A 420       1.914  -7.472 -73.168  1.00 35.57           C  
-ATOM   2553  NH1 ARG A 420       2.317  -6.274 -72.765  1.00 39.74           N  
-ATOM   2554  NH2 ARG A 420       2.394  -7.984 -74.292  1.00 36.12           N  
-ATOM   2555  N   GLU A 421      -0.157 -13.677 -75.014  1.00 39.06           N  
-ATOM   2556  CA  GLU A 421      -0.303 -15.112 -74.818  1.00 38.01           C  
-ATOM   2557  C   GLU A 421      -0.962 -15.368 -73.462  1.00 41.85           C  
-ATOM   2558  O   GLU A 421      -0.773 -14.594 -72.524  1.00 48.33           O  
-ATOM   2559  CB  GLU A 421       1.061 -15.800 -74.907  1.00 41.42           C  
-ATOM   2560  CG  GLU A 421       1.025 -17.320 -74.865  1.00 49.32           C  
-ATOM   2561  CD  GLU A 421       2.403 -17.933 -75.045  1.00 48.12           C  
-ATOM   2562  OE1 GLU A 421       3.297 -17.245 -75.584  1.00 34.80           O  
-ATOM   2563  OE2 GLU A 421       2.594 -19.099 -74.641  1.00 49.98           O  
-ATOM   2564  N   VAL A 422      -1.744 -16.438 -73.363  1.00 45.10           N  
-ATOM   2565  CA  VAL A 422      -2.437 -16.758 -72.116  1.00 42.99           C  
-ATOM   2566  C   VAL A 422      -1.447 -17.034 -70.991  1.00 38.47           C  
-ATOM   2567  O   VAL A 422      -0.627 -17.949 -71.082  1.00 44.71           O  
-ATOM   2568  CB  VAL A 422      -3.368 -17.977 -72.271  1.00 39.68           C  
-ATOM   2569  CG1 VAL A 422      -3.870 -18.432 -70.911  1.00 30.33           C  
-ATOM   2570  CG2 VAL A 422      -4.535 -17.644 -73.189  1.00 48.49           C  
-ATOM   2571  N   GLY A 423      -1.524 -16.231 -69.934  1.00 34.66           N  
-ATOM   2572  CA  GLY A 423      -0.635 -16.378 -68.795  1.00 40.64           C  
-ATOM   2573  C   GLY A 423       0.325 -15.215 -68.627  1.00 44.23           C  
-ATOM   2574  O   GLY A 423       0.919 -15.035 -67.562  1.00 42.06           O  
-ATOM   2575  N   ASP A 424       0.479 -14.422 -69.683  1.00 41.17           N  
-ATOM   2576  CA  ASP A 424       1.391 -13.286 -69.662  1.00 25.19           C  
-ATOM   2577  C   ASP A 424       0.756 -12.094 -68.956  1.00 27.04           C  
-ATOM   2578  O   ASP A 424      -0.175 -11.476 -69.472  1.00 36.01           O  
-ATOM   2579  CB  ASP A 424       1.801 -12.907 -71.085  1.00 27.10           C  
-ATOM   2580  CG  ASP A 424       3.059 -12.064 -71.126  1.00 34.63           C  
-ATOM   2581  OD1 ASP A 424       3.274 -11.251 -70.202  1.00 34.11           O  
-ATOM   2582  OD2 ASP A 424       3.841 -12.216 -72.087  1.00 37.49           O  
-ATOM   2583  N   ILE A 425       1.276 -11.772 -67.778  1.00 23.12           N  
-ATOM   2584  CA  ILE A 425       0.731 -10.693 -66.967  1.00 26.57           C  
-ATOM   2585  C   ILE A 425       1.207  -9.329 -67.452  1.00 29.73           C  
-ATOM   2586  O   ILE A 425       0.735  -8.294 -66.984  1.00 31.74           O  
-ATOM   2587  CB  ILE A 425       1.120 -10.857 -65.492  1.00 23.21           C  
-ATOM   2588  CG1 ILE A 425       2.593 -10.502 -65.289  1.00 25.03           C  
-ATOM   2589  CG2 ILE A 425       0.853 -12.278 -65.033  1.00 28.28           C  
-ATOM   2590  CD1 ILE A 425       2.999 -10.404 -63.837  1.00 33.12           C  
-ATOM   2591  N   GLY A 426       2.144  -9.338 -68.394  1.00 28.88           N  
-ATOM   2592  CA  GLY A 426       2.734  -8.110 -68.892  1.00 30.09           C  
-ATOM   2593  C   GLY A 426       3.845  -7.620 -67.984  1.00 26.92           C  
-ATOM   2594  O   GLY A 426       4.300  -8.352 -67.107  1.00 26.91           O  
-ATOM   2595  N   PRO A 427       4.286  -6.369 -68.182  1.00 27.40           N  
-ATOM   2596  CA  PRO A 427       5.386  -5.789 -67.406  1.00 26.57           C  
-ATOM   2597  C   PRO A 427       4.984  -5.389 -65.985  1.00 35.17           C  
-ATOM   2598  O   PRO A 427       5.003  -4.202 -65.657  1.00 34.60           O  
-ATOM   2599  CB  PRO A 427       5.764  -4.554 -68.226  1.00 25.30           C  
-ATOM   2600  CG  PRO A 427       4.498  -4.147 -68.879  1.00 27.39           C  
-ATOM   2601  CD  PRO A 427       3.770  -5.429 -69.193  1.00 33.00           C  
-ATOM   2602  N   GLY A 428       4.646  -6.367 -65.149  1.00 34.46           N  
-ATOM   2603  CA  GLY A 428       4.183  -6.082 -63.802  1.00 35.26           C  
-ATOM   2604  C   GLY A 428       5.015  -6.668 -62.675  1.00 38.57           C  
-ATOM   2605  O   GLY A 428       5.779  -7.616 -62.874  1.00 46.36           O  
-ATOM   2606  N   TYR A 429       4.848  -6.087 -61.487  1.00 39.77           N  
-ATOM   2607  CA  TYR A 429       5.527  -6.509 -60.258  1.00 33.57           C  
-ATOM   2608  C   TYR A 429       6.999  -6.866 -60.452  1.00 33.07           C  
-ATOM   2609  O   TYR A 429       7.857  -5.990 -60.456  1.00 38.23           O  
-ATOM   2610  CB  TYR A 429       4.794  -7.691 -59.629  1.00 26.24           C  
-ATOM   2611  CG  TYR A 429       3.423  -7.340 -59.102  1.00 25.17           C  
-ATOM   2612  CD1 TYR A 429       3.261  -6.359 -58.133  1.00 24.77           C  
-ATOM   2613  CD2 TYR A 429       2.293  -7.996 -59.565  1.00 34.76           C  
-ATOM   2614  CE1 TYR A 429       2.008  -6.034 -57.648  1.00 24.70           C  
-ATOM   2615  CE2 TYR A 429       1.037  -7.682 -59.084  1.00 35.03           C  
-ATOM   2616  CZ  TYR A 429       0.900  -6.702 -58.126  1.00 32.32           C  
-ATOM   2617  OH  TYR A 429      -0.353  -6.392 -57.649  1.00 43.29           O  
-ATOM   2618  N   GLY A 430       7.283  -8.156 -60.611  1.00 29.64           N  
-ATOM   2619  CA  GLY A 430       8.651  -8.626 -60.756  1.00 30.68           C  
-ATOM   2620  C   GLY A 430       9.421  -7.940 -61.867  1.00 28.53           C  
-ATOM   2621  O   GLY A 430      10.601  -7.597 -61.710  1.00 34.06           O  
-ATOM   2622  N   PHE A 431       8.744  -7.732 -62.990  1.00 24.30           N  
-ATOM   2623  CA  PHE A 431       9.367  -7.110 -64.145  1.00 30.87           C  
-ATOM   2624  C   PHE A 431       9.803  -5.688 -63.853  1.00 28.39           C  
-ATOM   2625  O   PHE A 431      10.846  -5.256 -64.330  1.00 27.26           O  
-ATOM   2626  CB  PHE A 431       8.426  -7.108 -65.344  1.00 30.62           C  
-ATOM   2627  CG  PHE A 431       9.040  -6.520 -66.585  1.00 24.62           C  
-ATOM   2628  CD1 PHE A 431       9.820  -7.297 -67.424  1.00 26.39           C  
-ATOM   2629  CD2 PHE A 431       8.844  -5.189 -66.907  1.00 21.33           C  
-ATOM   2630  CE1 PHE A 431      10.385  -6.758 -68.562  1.00 35.20           C  
-ATOM   2631  CE2 PHE A 431       9.403  -4.644 -68.043  1.00 21.70           C  
-ATOM   2632  CZ  PHE A 431      10.176  -5.428 -68.873  1.00 25.58           C  
-ATOM   2633  N   GLN A 432       9.000  -4.950 -63.094  1.00 28.00           N  
-ATOM   2634  CA  GLN A 432       9.367  -3.585 -62.747  1.00 25.65           C  
-ATOM   2635  C   GLN A 432      10.472  -3.615 -61.695  1.00 26.95           C  
-ATOM   2636  O   GLN A 432      11.412  -2.823 -61.745  1.00 31.02           O  
-ATOM   2637  CB  GLN A 432       8.145  -2.801 -62.256  1.00 28.09           C  
-ATOM   2638  CG  GLN A 432       7.055  -2.628 -63.317  1.00 28.62           C  
-ATOM   2639  CD  GLN A 432       7.542  -1.864 -64.545  1.00 33.95           C  
-ATOM   2640  OE1 GLN A 432       8.312  -0.910 -64.432  1.00 39.10           O  
-ATOM   2641  NE2 GLN A 432       7.094  -2.286 -65.723  1.00 32.68           N  
-ATOM   2642  N   TRP A 433      10.351  -4.549 -60.755  1.00 31.53           N  
-ATOM   2643  CA  TRP A 433      11.353  -4.767 -59.715  1.00 28.90           C  
-ATOM   2644  C   TRP A 433      12.758  -4.928 -60.284  1.00 28.88           C  
-ATOM   2645  O   TRP A 433      13.683  -4.216 -59.894  1.00 26.40           O  
-ATOM   2646  CB  TRP A 433      11.019  -6.016 -58.892  1.00 25.55           C  
-ATOM   2647  CG  TRP A 433       9.887  -5.880 -57.924  1.00 26.58           C  
-ATOM   2648  CD1 TRP A 433       8.924  -4.915 -57.910  1.00 23.16           C  
-ATOM   2649  CD2 TRP A 433       9.605  -6.744 -56.817  1.00 30.76           C  
-ATOM   2650  NE1 TRP A 433       8.056  -5.127 -56.869  1.00 32.32           N  
-ATOM   2651  CE2 TRP A 433       8.454  -6.244 -56.181  1.00 27.59           C  
-ATOM   2652  CE3 TRP A 433      10.216  -7.892 -56.302  1.00 27.75           C  
-ATOM   2653  CZ2 TRP A 433       7.900  -6.852 -55.056  1.00 24.11           C  
-ATOM   2654  CZ3 TRP A 433       9.666  -8.494 -55.189  1.00 22.68           C  
-ATOM   2655  CH2 TRP A 433       8.521  -7.974 -54.577  1.00 22.33           C  
-ATOM   2656  N   ARG A 434      12.905  -5.869 -61.212  1.00 29.05           N  
-ATOM   2657  CA  ARG A 434      14.222  -6.259 -61.700  1.00 27.50           C  
-ATOM   2658  C   ARG A 434      14.621  -5.521 -62.978  1.00 30.81           C  
-ATOM   2659  O   ARG A 434      15.800  -5.471 -63.339  1.00 27.29           O  
-ATOM   2660  CB  ARG A 434      14.258  -7.771 -61.935  1.00 27.30           C  
-ATOM   2661  CG  ARG A 434      13.754  -8.593 -60.756  1.00 23.83           C  
-ATOM   2662  CD  ARG A 434      14.403  -8.144 -59.458  1.00 24.55           C  
-ATOM   2663  NE  ARG A 434      15.857  -8.238 -59.521  1.00 27.86           N  
-ATOM   2664  CZ  ARG A 434      16.555  -9.279 -59.084  1.00 27.12           C  
-ATOM   2665  NH1 ARG A 434      17.876  -9.281 -59.181  1.00 20.54           N  
-ATOM   2666  NH2 ARG A 434      15.931 -10.319 -58.545  1.00 31.80           N  
-ATOM   2667  N   HIS A 435      13.634  -4.952 -63.661  1.00 21.69           N  
-ATOM   2668  CA  HIS A 435      13.879  -4.280 -64.929  1.00 24.24           C  
-ATOM   2669  C   HIS A 435      12.967  -3.078 -65.129  1.00 26.32           C  
-ATOM   2670  O   HIS A 435      12.323  -2.972 -66.169  1.00 37.14           O  
-ATOM   2671  CB  HIS A 435      13.671  -5.240 -66.105  1.00 29.57           C  
-ATOM   2672  CG  HIS A 435      14.148  -6.636 -65.851  1.00 32.29           C  
-ATOM   2673  ND1 HIS A 435      15.434  -7.047 -66.128  1.00 31.77           N  
-ATOM   2674  CD2 HIS A 435      13.506  -7.719 -65.352  1.00 30.86           C  
-ATOM   2675  CE1 HIS A 435      15.565  -8.322 -65.807  1.00 30.81           C  
-ATOM   2676  NE2 HIS A 435      14.410  -8.753 -65.334  1.00 22.55           N  
-ATOM   2677  N   PHE A 436      12.905  -2.175 -64.156  1.00 22.30           N  
-ATOM   2678  CA  PHE A 436      12.027  -1.010 -64.272  1.00 26.46           C  
-ATOM   2679  C   PHE A 436      12.288  -0.202 -65.546  1.00 29.33           C  
-ATOM   2680  O   PHE A 436      13.430   0.144 -65.855  1.00 29.44           O  
-ATOM   2681  CB  PHE A 436      12.180  -0.097 -63.054  1.00 31.15           C  
-ATOM   2682  CG  PHE A 436      11.164   1.010 -63.000  1.00 28.75           C  
-ATOM   2683  CD1 PHE A 436      11.422   2.235 -63.591  1.00 27.81           C  
-ATOM   2684  CD2 PHE A 436       9.945   0.820 -62.366  1.00 27.04           C  
-ATOM   2685  CE1 PHE A 436      10.486   3.250 -63.553  1.00 28.11           C  
-ATOM   2686  CE2 PHE A 436       9.007   1.834 -62.323  1.00 29.34           C  
-ATOM   2687  CZ  PHE A 436       9.278   3.050 -62.916  1.00 30.74           C  
-ATOM   2688  N   GLY A 437      11.220   0.091 -66.282  1.00 30.24           N  
-ATOM   2689  CA  GLY A 437      11.302   0.957 -67.444  1.00 31.83           C  
-ATOM   2690  C   GLY A 437      11.659   0.257 -68.742  1.00 24.35           C  
-ATOM   2691  O   GLY A 437      11.468   0.816 -69.823  1.00 21.70           O  
-ATOM   2692  N   ALA A 438      12.181  -0.961 -68.636  1.00 20.95           N  
-ATOM   2693  CA  ALA A 438      12.576  -1.736 -69.807  1.00 26.05           C  
-ATOM   2694  C   ALA A 438      11.394  -1.968 -70.750  1.00 35.39           C  
-ATOM   2695  O   ALA A 438      10.256  -2.120 -70.305  1.00 30.60           O  
-ATOM   2696  CB  ALA A 438      13.181  -3.062 -69.378  1.00 20.64           C  
-ATOM   2697  N   ALA A 439      11.670  -1.984 -72.051  1.00 31.10           N  
-ATOM   2698  CA  ALA A 439      10.630  -2.204 -73.051  1.00 27.29           C  
-ATOM   2699  C   ALA A 439      10.203  -3.666 -73.062  1.00 27.80           C  
-ATOM   2700  O   ALA A 439      11.017  -4.555 -73.304  1.00 36.10           O  
-ATOM   2701  CB  ALA A 439      11.116  -1.780 -74.430  1.00 46.91           C  
-ATOM   2702  N   TYR A 440       8.922  -3.907 -72.803  1.00 27.43           N  
-ATOM   2703  CA  TYR A 440       8.402  -5.266 -72.696  1.00 31.06           C  
-ATOM   2704  C   TYR A 440       8.081  -5.872 -74.062  1.00 31.27           C  
-ATOM   2705  O   TYR A 440       7.771  -5.158 -75.014  1.00 32.39           O  
-ATOM   2706  CB  TYR A 440       7.151  -5.284 -71.811  1.00 28.84           C  
-ATOM   2707  CG  TYR A 440       6.717  -6.669 -71.379  1.00 34.17           C  
-ATOM   2708  CD1 TYR A 440       7.380  -7.336 -70.356  1.00 34.08           C  
-ATOM   2709  CD2 TYR A 440       5.642  -7.306 -71.987  1.00 32.55           C  
-ATOM   2710  CE1 TYR A 440       6.989  -8.600 -69.954  1.00 31.03           C  
-ATOM   2711  CE2 TYR A 440       5.243  -8.571 -71.592  1.00 30.67           C  
-ATOM   2712  CZ  TYR A 440       5.919  -9.212 -70.575  1.00 32.01           C  
-ATOM   2713  OH  TYR A 440       5.527 -10.470 -70.180  1.00 29.49           O  
-ATOM   2714  N   LYS A 441       8.170  -7.195 -74.151  1.00 31.56           N  
-ATOM   2715  CA  LYS A 441       7.733  -7.922 -75.338  1.00 36.32           C  
-ATOM   2716  C   LYS A 441       6.765  -9.032 -74.940  1.00 38.06           C  
-ATOM   2717  O   LYS A 441       5.551  -8.878 -75.056  1.00 41.79           O  
-ATOM   2718  CB  LYS A 441       8.926  -8.499 -76.102  1.00 43.66           C  
-ATOM   2719  CG  LYS A 441       9.637  -7.499 -77.005  1.00 55.57           C  
-ATOM   2720  CD  LYS A 441      10.775  -6.790 -76.286  1.00 63.10           C  
-ATOM   2721  CE  LYS A 441      11.497  -5.827 -77.220  1.00 59.91           C  
-ATOM   2722  NZ  LYS A 441      11.999  -6.512 -78.445  1.00 46.54           N  
-ATOM   2723  N   ASP A 442       7.305 -10.153 -74.474  1.00 35.37           N  
-ATOM   2724  CA  ASP A 442       6.474 -11.213 -73.916  1.00 31.20           C  
-ATOM   2725  C   ASP A 442       7.167 -11.875 -72.730  1.00 36.06           C  
-ATOM   2726  O   ASP A 442       8.285 -11.511 -72.366  1.00 31.76           O  
-ATOM   2727  CB  ASP A 442       6.110 -12.258 -74.983  1.00 34.87           C  
-ATOM   2728  CG  ASP A 442       7.326 -12.857 -75.679  1.00 39.15           C  
-ATOM   2729  OD1 ASP A 442       8.369 -13.077 -75.027  1.00 36.12           O  
-ATOM   2730  OD2 ASP A 442       7.227 -13.124 -76.896  1.00 41.70           O  
-ATOM   2731  N   MET A 443       6.497 -12.857 -72.140  1.00 36.53           N  
-ATOM   2732  CA  MET A 443       6.998 -13.525 -70.946  1.00 31.17           C  
-ATOM   2733  C   MET A 443       8.145 -14.489 -71.237  1.00 39.36           C  
-ATOM   2734  O   MET A 443       8.719 -15.070 -70.316  1.00 43.97           O  
-ATOM   2735  CB  MET A 443       5.861 -14.276 -70.258  1.00 29.52           C  
-ATOM   2736  CG  MET A 443       5.213 -15.330 -71.131  1.00 24.86           C  
-ATOM   2737  SD  MET A 443       3.674 -15.939 -70.426  1.00 34.59           S  
-ATOM   2738  CE  MET A 443       3.127 -17.045 -71.721  1.00 44.13           C  
-ATOM   2739  N   HIS A 444       8.478 -14.659 -72.514  1.00 40.66           N  
-ATOM   2740  CA  HIS A 444       9.526 -15.596 -72.905  1.00 35.88           C  
-ATOM   2741  C   HIS A 444      10.836 -14.880 -73.213  1.00 32.04           C  
-ATOM   2742  O   HIS A 444      11.862 -15.518 -73.446  1.00 30.69           O  
-ATOM   2743  CB  HIS A 444       9.083 -16.416 -74.119  1.00 29.68           C  
-ATOM   2744  CG  HIS A 444       7.752 -17.078 -73.949  1.00 33.28           C  
-ATOM   2745  ND1 HIS A 444       7.541 -18.108 -73.058  1.00 36.86           N  
-ATOM   2746  CD2 HIS A 444       6.561 -16.857 -74.557  1.00 39.71           C  
-ATOM   2747  CE1 HIS A 444       6.278 -18.493 -73.123  1.00 44.69           C  
-ATOM   2748  NE2 HIS A 444       5.662 -17.749 -74.025  1.00 38.96           N  
-ATOM   2749  N   THR A 445      10.796 -13.551 -73.206  1.00 33.40           N  
-ATOM   2750  CA  THR A 445      11.955 -12.752 -73.588  1.00 37.86           C  
-ATOM   2751  C   THR A 445      12.964 -12.640 -72.450  1.00 46.60           C  
-ATOM   2752  O   THR A 445      12.588 -12.603 -71.278  1.00 46.32           O  
-ATOM   2753  CB  THR A 445      11.536 -11.334 -74.026  1.00 39.68           C  
-ATOM   2754  OG1 THR A 445      10.356 -11.407 -74.836  1.00 42.41           O  
-ATOM   2755  CG2 THR A 445      12.651 -10.661 -74.813  1.00 38.66           C  
-ATOM   2756  N   ASP A 446      14.247 -12.592 -72.801  1.00 47.15           N  
-ATOM   2757  CA  ASP A 446      15.301 -12.381 -71.814  1.00 49.95           C  
-ATOM   2758  C   ASP A 446      15.536 -10.885 -71.639  1.00 46.07           C  
-ATOM   2759  O   ASP A 446      15.674 -10.155 -72.620  1.00 47.37           O  
-ATOM   2760  CB  ASP A 446      16.595 -13.083 -72.234  1.00 52.13           C  
-ATOM   2761  CG  ASP A 446      17.535 -13.323 -71.065  1.00 44.66           C  
-ATOM   2762  OD1 ASP A 446      17.396 -12.630 -70.036  1.00 38.65           O  
-ATOM   2763  OD2 ASP A 446      18.413 -14.206 -71.174  1.00 44.21           O  
-ATOM   2764  N   TYR A 447      15.583 -10.433 -70.390  1.00 38.18           N  
-ATOM   2765  CA  TYR A 447      15.677  -9.006 -70.105  1.00 37.18           C  
-ATOM   2766  C   TYR A 447      16.875  -8.634 -69.241  1.00 34.58           C  
-ATOM   2767  O   TYR A 447      16.935  -7.523 -68.716  1.00 29.89           O  
-ATOM   2768  CB  TYR A 447      14.403  -8.520 -69.414  1.00 34.34           C  
-ATOM   2769  CG  TYR A 447      13.154  -8.643 -70.249  1.00 30.37           C  
-ATOM   2770  CD1 TYR A 447      12.878  -7.730 -71.256  1.00 26.84           C  
-ATOM   2771  CD2 TYR A 447      12.241  -9.663 -70.021  1.00 37.15           C  
-ATOM   2772  CE1 TYR A 447      11.733  -7.834 -72.018  1.00 36.41           C  
-ATOM   2773  CE2 TYR A 447      11.092  -9.775 -70.777  1.00 40.89           C  
-ATOM   2774  CZ  TYR A 447      10.843  -8.857 -71.774  1.00 36.30           C  
-ATOM   2775  OH  TYR A 447       9.700  -8.966 -72.531  1.00 41.52           O  
-ATOM   2776  N   THR A 448      17.820  -9.557 -69.088  1.00 41.72           N  
-ATOM   2777  CA  THR A 448      18.969  -9.317 -68.220  1.00 38.24           C  
-ATOM   2778  C   THR A 448      19.793  -8.122 -68.703  1.00 35.57           C  
-ATOM   2779  O   THR A 448      20.246  -8.082 -69.848  1.00 41.19           O  
-ATOM   2780  CB  THR A 448      19.875 -10.568 -68.113  1.00 33.73           C  
-ATOM   2781  OG1 THR A 448      21.101 -10.219 -67.458  1.00 46.15           O  
-ATOM   2782  CG2 THR A 448      20.184 -11.147 -69.488  1.00 36.25           C  
-ATOM   2783  N   GLY A 449      19.959  -7.137 -67.826  1.00 25.85           N  
-ATOM   2784  CA  GLY A 449      20.717  -5.943 -68.154  1.00 26.09           C  
-ATOM   2785  C   GLY A 449      19.845  -4.770 -68.559  1.00 30.52           C  
-ATOM   2786  O   GLY A 449      20.287  -3.619 -68.550  1.00 34.18           O  
-ATOM   2787  N   GLN A 450      18.600  -5.062 -68.918  1.00 37.30           N  
-ATOM   2788  CA  GLN A 450      17.658  -4.023 -69.317  1.00 37.87           C  
-ATOM   2789  C   GLN A 450      16.920  -3.447 -68.110  1.00 36.15           C  
-ATOM   2790  O   GLN A 450      16.514  -4.182 -67.207  1.00 37.97           O  
-ATOM   2791  CB  GLN A 450      16.648  -4.571 -70.324  1.00 27.98           C  
-ATOM   2792  CG  GLN A 450      17.261  -5.189 -71.567  1.00 25.31           C  
-ATOM   2793  CD  GLN A 450      16.207  -5.723 -72.521  1.00 37.44           C  
-ATOM   2794  OE1 GLN A 450      16.361  -6.800 -73.095  1.00 44.54           O  
-ATOM   2795  NE2 GLN A 450      15.128  -4.968 -72.694  1.00 36.94           N  
-ATOM   2796  N   GLY A 451      16.748  -2.129 -68.099  1.00 28.64           N  
-ATOM   2797  CA  GLY A 451      15.985  -1.465 -67.058  1.00 23.16           C  
-ATOM   2798  C   GLY A 451      16.717  -1.352 -65.737  1.00 23.45           C  
-ATOM   2799  O   GLY A 451      17.896  -1.693 -65.636  1.00 28.79           O  
-ATOM   2800  N   VAL A 452      16.007  -0.875 -64.719  1.00 20.08           N  
-ATOM   2801  CA  VAL A 452      16.590  -0.665 -63.397  1.00 24.24           C  
-ATOM   2802  C   VAL A 452      16.309  -1.838 -62.457  1.00 29.06           C  
-ATOM   2803  O   VAL A 452      15.162  -2.261 -62.304  1.00 27.07           O  
-ATOM   2804  CB  VAL A 452      16.059   0.632 -62.756  1.00 22.68           C  
-ATOM   2805  CG1 VAL A 452      16.654   0.832 -61.372  1.00 22.21           C  
-ATOM   2806  CG2 VAL A 452      16.363   1.825 -63.650  1.00 18.59           C  
-ATOM   2807  N   ASP A 453      17.363  -2.359 -61.831  1.00 31.21           N  
-ATOM   2808  CA  ASP A 453      17.233  -3.458 -60.875  1.00 26.08           C  
-ATOM   2809  C   ASP A 453      17.071  -2.922 -59.453  1.00 27.53           C  
-ATOM   2810  O   ASP A 453      18.021  -2.899 -58.662  1.00 31.24           O  
-ATOM   2811  CB  ASP A 453      18.443  -4.391 -60.959  1.00 28.18           C  
-ATOM   2812  CG  ASP A 453      18.199  -5.730 -60.288  1.00 29.74           C  
-ATOM   2813  OD1 ASP A 453      17.439  -5.786 -59.298  1.00 34.86           O  
-ATOM   2814  OD2 ASP A 453      18.774  -6.734 -60.755  1.00 31.95           O  
-ATOM   2815  N   GLN A 454      15.849  -2.508 -59.139  1.00 22.75           N  
-ATOM   2816  CA  GLN A 454      15.545  -1.892 -57.857  1.00 20.37           C  
-ATOM   2817  C   GLN A 454      15.890  -2.788 -56.677  1.00 23.38           C  
-ATOM   2818  O   GLN A 454      16.283  -2.294 -55.625  1.00 29.09           O  
-ATOM   2819  CB  GLN A 454      14.067  -1.512 -57.788  1.00 25.46           C  
-ATOM   2820  CG  GLN A 454      13.658  -0.410 -58.745  1.00 29.86           C  
-ATOM   2821  CD  GLN A 454      12.230   0.044 -58.523  1.00 24.28           C  
-ATOM   2822  OE1 GLN A 454      11.971   0.961 -57.742  1.00 18.03           O  
-ATOM   2823  NE2 GLN A 454      11.292  -0.600 -59.210  1.00 24.26           N  
-ATOM   2824  N   LEU A 455      15.741  -4.098 -56.846  1.00 22.24           N  
-ATOM   2825  CA  LEU A 455      15.991  -5.028 -55.750  1.00 28.85           C  
-ATOM   2826  C   LEU A 455      17.477  -5.076 -55.400  1.00 34.82           C  
-ATOM   2827  O   LEU A 455      17.862  -4.973 -54.227  1.00 29.08           O  
-ATOM   2828  CB  LEU A 455      15.473  -6.423 -56.105  1.00 26.89           C  
-ATOM   2829  CG  LEU A 455      15.371  -7.409 -54.939  1.00 30.94           C  
-ATOM   2830  CD1 LEU A 455      14.621  -6.783 -53.774  1.00 20.35           C  
-ATOM   2831  CD2 LEU A 455      14.693  -8.697 -55.377  1.00 18.41           C  
-ATOM   2832  N   LYS A 456      18.309  -5.222 -56.427  1.00 28.11           N  
-ATOM   2833  CA  LYS A 456      19.753  -5.235 -56.232  1.00 30.36           C  
-ATOM   2834  C   LYS A 456      20.217  -3.889 -55.698  1.00 35.89           C  
-ATOM   2835  O   LYS A 456      21.086  -3.826 -54.829  1.00 35.49           O  
-ATOM   2836  CB  LYS A 456      20.479  -5.575 -57.537  1.00 32.55           C  
-ATOM   2837  CG  LYS A 456      21.898  -6.083 -57.336  1.00 42.99           C  
-ATOM   2838  CD  LYS A 456      22.524  -6.503 -58.655  1.00 40.49           C  
-ATOM   2839  CE  LYS A 456      22.736  -5.319 -59.586  1.00 58.82           C  
-ATOM   2840  NZ  LYS A 456      23.188  -5.772 -60.935  1.00 55.88           N  
-ATOM   2841  N   ASN A 457      19.628  -2.815 -56.218  1.00 35.11           N  
-ATOM   2842  CA  ASN A 457      19.911  -1.474 -55.711  1.00 34.32           C  
-ATOM   2843  C   ASN A 457      19.662  -1.371 -54.208  1.00 34.20           C  
-ATOM   2844  O   ASN A 457      20.544  -0.975 -53.442  1.00 37.24           O  
-ATOM   2845  CB  ASN A 457      19.069  -0.426 -56.446  1.00 25.46           C  
-ATOM   2846  CG  ASN A 457      19.633  -0.071 -57.808  1.00 25.32           C  
-ATOM   2847  OD1 ASN A 457      20.736  -0.489 -58.168  1.00 34.98           O  
-ATOM   2848  ND2 ASN A 457      18.887   0.720 -58.566  1.00 27.39           N  
-ATOM   2849  N   VAL A 458      18.451  -1.736 -53.799  1.00 29.22           N  
-ATOM   2850  CA  VAL A 458      18.050  -1.715 -52.396  1.00 31.37           C  
-ATOM   2851  C   VAL A 458      18.981  -2.552 -51.531  1.00 28.13           C  
-ATOM   2852  O   VAL A 458      19.417  -2.112 -50.468  1.00 30.47           O  
-ATOM   2853  CB  VAL A 458      16.610  -2.230 -52.220  1.00 25.43           C  
-ATOM   2854  CG1 VAL A 458      16.343  -2.603 -50.772  1.00 18.61           C  
-ATOM   2855  CG2 VAL A 458      15.612  -1.187 -52.701  1.00 26.46           C  
-ATOM   2856  N   ILE A 459      19.291  -3.758 -51.992  1.00 26.26           N  
-ATOM   2857  CA  ILE A 459      20.140  -4.647 -51.211  1.00 29.44           C  
-ATOM   2858  C   ILE A 459      21.548  -4.087 -51.035  1.00 30.89           C  
-ATOM   2859  O   ILE A 459      22.051  -4.025 -49.914  1.00 25.93           O  
-ATOM   2860  CB  ILE A 459      20.210  -6.044 -51.841  1.00 30.69           C  
-ATOM   2861  CG1 ILE A 459      18.880  -6.766 -51.626  1.00 19.43           C  
-ATOM   2862  CG2 ILE A 459      21.344  -6.851 -51.230  1.00 22.41           C  
-ATOM   2863  CD1 ILE A 459      18.736  -8.003 -52.443  1.00 27.43           C  
-ATOM   2864  N   GLN A 460      22.178  -3.671 -52.131  1.00 41.97           N  
-ATOM   2865  CA  GLN A 460      23.521  -3.097 -52.051  1.00 40.51           C  
-ATOM   2866  C   GLN A 460      23.544  -1.857 -51.159  1.00 30.37           C  
-ATOM   2867  O   GLN A 460      24.441  -1.687 -50.328  1.00 26.59           O  
-ATOM   2868  CB  GLN A 460      24.047  -2.766 -53.451  1.00 37.09           C  
-ATOM   2869  CG  GLN A 460      24.505  -3.985 -54.229  1.00 47.61           C  
-ATOM   2870  CD  GLN A 460      24.983  -3.634 -55.626  1.00 82.18           C  
-ATOM   2871  OE1 GLN A 460      25.013  -2.463 -56.013  1.00 88.55           O  
-ATOM   2872  NE2 GLN A 460      25.358  -4.651 -56.393  1.00 79.17           N  
-ATOM   2873  N   MET A 461      22.539  -1.004 -51.324  1.00 26.95           N  
-ATOM   2874  CA  MET A 461      22.417   0.196 -50.509  1.00 29.26           C  
-ATOM   2875  C   MET A 461      22.256  -0.166 -49.035  1.00 27.67           C  
-ATOM   2876  O   MET A 461      22.700   0.572 -48.156  1.00 30.51           O  
-ATOM   2877  CB  MET A 461      21.235   1.052 -50.973  1.00 36.62           C  
-ATOM   2878  CG  MET A 461      21.166   2.423 -50.311  1.00 43.18           C  
-ATOM   2879  SD  MET A 461      22.602   3.444 -50.698  1.00 42.03           S  
-ATOM   2880  CE  MET A 461      22.371   3.682 -52.460  1.00 46.13           C  
-ATOM   2881  N   LEU A 462      21.622  -1.304 -48.769  1.00 33.07           N  
-ATOM   2882  CA  LEU A 462      21.453  -1.779 -47.399  1.00 27.06           C  
-ATOM   2883  C   LEU A 462      22.767  -2.296 -46.824  1.00 32.35           C  
-ATOM   2884  O   LEU A 462      23.066  -2.091 -45.649  1.00 33.21           O  
-ATOM   2885  CB  LEU A 462      20.388  -2.875 -47.341  1.00 19.95           C  
-ATOM   2886  CG  LEU A 462      18.927  -2.426 -47.320  1.00 16.99           C  
-ATOM   2887  CD1 LEU A 462      18.019  -3.567 -47.720  1.00 18.05           C  
-ATOM   2888  CD2 LEU A 462      18.552  -1.917 -45.949  1.00 17.86           C  
-ATOM   2889  N   ARG A 463      23.546  -2.970 -47.663  1.00 32.77           N  
-ATOM   2890  CA  ARG A 463      24.793  -3.582 -47.226  1.00 20.63           C  
-ATOM   2891  C   ARG A 463      25.915  -2.561 -47.058  1.00 26.12           C  
-ATOM   2892  O   ARG A 463      26.847  -2.784 -46.288  1.00 28.69           O  
-ATOM   2893  CB  ARG A 463      25.221  -4.667 -48.213  1.00 22.00           C  
-ATOM   2894  CG  ARG A 463      24.210  -5.795 -48.350  1.00 36.06           C  
-ATOM   2895  CD  ARG A 463      24.881  -7.128 -48.643  1.00 31.05           C  
-ATOM   2896  NE  ARG A 463      25.015  -7.397 -50.071  1.00 20.82           N  
-ATOM   2897  CZ  ARG A 463      24.654  -8.540 -50.643  1.00 19.76           C  
-ATOM   2898  NH1 ARG A 463      24.136  -9.511 -49.905  1.00 15.89           N  
-ATOM   2899  NH2 ARG A 463      24.812  -8.716 -51.947  1.00 25.05           N  
-ATOM   2900  N   THR A 464      25.819  -1.437 -47.763  1.00 32.93           N  
-ATOM   2901  CA  THR A 464      26.898  -0.453 -47.746  1.00 26.81           C  
-ATOM   2902  C   THR A 464      26.548   0.835 -46.999  1.00 29.70           C  
-ATOM   2903  O   THR A 464      27.399   1.412 -46.320  1.00 36.52           O  
-ATOM   2904  CB  THR A 464      27.329  -0.089 -49.177  1.00 27.22           C  
-ATOM   2905  OG1 THR A 464      26.322   0.719 -49.799  1.00 37.89           O  
-ATOM   2906  CG2 THR A 464      27.549  -1.349 -49.998  1.00 26.15           C  
-ATOM   2907  N   ASN A 465      25.306   1.287 -47.123  1.00 30.15           N  
-ATOM   2908  CA  ASN A 465      24.919   2.577 -46.563  1.00 33.59           C  
-ATOM   2909  C   ASN A 465      23.526   2.545 -45.933  1.00 33.50           C  
-ATOM   2910  O   ASN A 465      22.583   3.109 -46.485  1.00 38.42           O  
-ATOM   2911  CB  ASN A 465      24.980   3.646 -47.656  1.00 34.75           C  
-ATOM   2912  CG  ASN A 465      25.035   5.053 -47.099  1.00 40.57           C  
-ATOM   2913  OD1 ASN A 465      24.429   5.351 -46.071  1.00 45.17           O  
-ATOM   2914  ND2 ASN A 465      25.770   5.928 -47.777  1.00 30.26           N  
-ATOM   2915  N   PRO A 466      23.402   1.909 -44.757  1.00 33.42           N  
-ATOM   2916  CA  PRO A 466      22.104   1.609 -44.136  1.00 29.62           C  
-ATOM   2917  C   PRO A 466      21.317   2.825 -43.638  1.00 30.81           C  
-ATOM   2918  O   PRO A 466      20.211   2.650 -43.126  1.00 37.37           O  
-ATOM   2919  CB  PRO A 466      22.488   0.710 -42.956  1.00 35.95           C  
-ATOM   2920  CG  PRO A 466      23.867   1.142 -42.601  1.00 42.20           C  
-ATOM   2921  CD  PRO A 466      24.528   1.477 -43.911  1.00 40.99           C  
-ATOM   2922  N   THR A 467      21.863   4.027 -43.780  1.00 35.31           N  
-ATOM   2923  CA  THR A 467      21.167   5.224 -43.318  1.00 33.48           C  
-ATOM   2924  C   THR A 467      20.623   6.032 -44.493  1.00 29.93           C  
-ATOM   2925  O   THR A 467      20.107   7.138 -44.321  1.00 28.34           O  
-ATOM   2926  CB  THR A 467      22.083   6.116 -42.460  1.00 34.69           C  
-ATOM   2927  OG1 THR A 467      23.320   6.344 -43.147  1.00 33.73           O  
-ATOM   2928  CG2 THR A 467      22.370   5.445 -41.127  1.00 27.22           C  
-ATOM   2929  N   ASP A 468      20.741   5.466 -45.689  1.00 27.27           N  
-ATOM   2930  CA  ASP A 468      20.211   6.097 -46.890  1.00 31.87           C  
-ATOM   2931  C   ASP A 468      18.688   6.091 -46.845  1.00 30.02           C  
-ATOM   2932  O   ASP A 468      18.079   5.100 -46.446  1.00 36.05           O  
-ATOM   2933  CB  ASP A 468      20.721   5.376 -48.140  1.00 28.17           C  
-ATOM   2934  CG  ASP A 468      20.187   5.979 -49.422  1.00 27.66           C  
-ATOM   2935  OD1 ASP A 468      20.690   7.045 -49.834  1.00 28.53           O  
-ATOM   2936  OD2 ASP A 468      19.271   5.381 -50.025  1.00 30.81           O  
-ATOM   2937  N   ARG A 469      18.072   7.201 -47.239  1.00 32.31           N  
-ATOM   2938  CA  ARG A 469      16.616   7.305 -47.194  1.00 29.29           C  
-ATOM   2939  C   ARG A 469      15.989   7.187 -48.581  1.00 23.60           C  
-ATOM   2940  O   ARG A 469      14.910   7.722 -48.823  1.00 25.60           O  
-ATOM   2941  CB  ARG A 469      16.188   8.625 -46.545  1.00 26.85           C  
-ATOM   2942  CG  ARG A 469      16.839   8.919 -45.200  1.00 25.39           C  
-ATOM   2943  CD  ARG A 469      16.114  10.061 -44.503  1.00 22.50           C  
-ATOM   2944  NE  ARG A 469      17.008  10.962 -43.777  1.00 35.39           N  
-ATOM   2945  CZ  ARG A 469      17.692  11.951 -44.347  1.00 36.37           C  
-ATOM   2946  NH1 ARG A 469      17.599  12.152 -45.651  1.00 27.29           N  
-ATOM   2947  NH2 ARG A 469      18.476  12.733 -43.618  1.00 31.18           N  
-ATOM   2948  N   ARG A 470      16.666   6.489 -49.487  1.00 24.82           N  
-ATOM   2949  CA  ARG A 470      16.152   6.290 -50.840  1.00 20.63           C  
-ATOM   2950  C   ARG A 470      16.059   4.809 -51.188  1.00 25.17           C  
-ATOM   2951  O   ARG A 470      16.093   4.433 -52.361  1.00 19.25           O  
-ATOM   2952  CB  ARG A 470      17.031   7.003 -51.872  1.00 19.45           C  
-ATOM   2953  CG  ARG A 470      16.988   8.521 -51.814  1.00 19.76           C  
-ATOM   2954  CD  ARG A 470      18.000   9.074 -50.827  1.00 27.20           C  
-ATOM   2955  NE  ARG A 470      18.217  10.503 -51.025  1.00 31.32           N  
-ATOM   2956  CZ  ARG A 470      19.140  11.007 -51.837  1.00 32.34           C  
-ATOM   2957  NH1 ARG A 470      19.934  10.196 -52.525  1.00 26.33           N  
-ATOM   2958  NH2 ARG A 470      19.273  12.321 -51.960  1.00 22.56           N  
-ATOM   2959  N   MET A 471      15.945   3.971 -50.162  1.00 27.94           N  
-ATOM   2960  CA  MET A 471      15.844   2.529 -50.358  1.00 29.24           C  
-ATOM   2961  C   MET A 471      14.415   2.119 -50.688  1.00 28.06           C  
-ATOM   2962  O   MET A 471      13.683   1.636 -49.822  1.00 29.08           O  
-ATOM   2963  CB  MET A 471      16.319   1.785 -49.113  1.00 25.27           C  
-ATOM   2964  CG  MET A 471      17.658   2.249 -48.585  1.00 28.59           C  
-ATOM   2965  SD  MET A 471      18.081   1.398 -47.058  1.00 34.62           S  
-ATOM   2966  CE  MET A 471      19.567   2.263 -46.591  1.00 32.68           C  
-ATOM   2967  N   LEU A 472      14.017   2.307 -51.940  1.00 20.23           N  
-ATOM   2968  CA  LEU A 472      12.650   2.007 -52.333  1.00 21.40           C  
-ATOM   2969  C   LEU A 472      12.566   1.117 -53.564  1.00 23.71           C  
-ATOM   2970  O   LEU A 472      13.465   1.093 -54.403  1.00 22.27           O  
-ATOM   2971  CB  LEU A 472      11.872   3.299 -52.582  1.00 24.46           C  
-ATOM   2972  CG  LEU A 472      11.432   4.064 -51.335  1.00 20.15           C  
-ATOM   2973  CD1 LEU A 472      12.483   5.081 -50.903  1.00 24.32           C  
-ATOM   2974  CD2 LEU A 472      10.090   4.727 -51.577  1.00 22.26           C  
-ATOM   2975  N   MET A 473      11.461   0.388 -53.652  1.00 21.99           N  
-ATOM   2976  CA  MET A 473      11.175  -0.461 -54.791  1.00 21.88           C  
-ATOM   2977  C   MET A 473       9.743  -0.186 -55.225  1.00 25.04           C  
-ATOM   2978  O   MET A 473       8.811  -0.357 -54.441  1.00 30.60           O  
-ATOM   2979  CB  MET A 473      11.381  -1.933 -54.428  1.00 16.19           C  
-ATOM   2980  CG  MET A 473      11.544  -2.860 -55.615  1.00 19.46           C  
-ATOM   2981  SD  MET A 473      12.228  -4.456 -55.122  1.00 36.22           S  
-ATOM   2982  CE  MET A 473      10.961  -5.035 -53.995  1.00 23.08           C  
-ATOM   2983  N   THR A 474       9.566   0.265 -56.462  1.00 19.80           N  
-ATOM   2984  CA  THR A 474       8.229   0.588 -56.942  1.00 18.03           C  
-ATOM   2985  C   THR A 474       7.882  -0.203 -58.197  1.00 19.84           C  
-ATOM   2986  O   THR A 474       8.747  -0.503 -59.019  1.00 23.79           O  
-ATOM   2987  CB  THR A 474       8.075   2.098 -57.224  1.00 18.19           C  
-ATOM   2988  OG1 THR A 474       6.717   2.385 -57.581  1.00 22.18           O  
-ATOM   2989  CG2 THR A 474       9.001   2.543 -58.348  1.00 15.68           C  
-ATOM   2990  N   ALA A 475       6.608  -0.554 -58.326  1.00 21.69           N  
-ATOM   2991  CA  ALA A 475       6.124  -1.275 -59.494  1.00 21.70           C  
-ATOM   2992  C   ALA A 475       5.058  -0.457 -60.203  1.00 16.88           C  
-ATOM   2993  O   ALA A 475       4.474  -0.900 -61.190  1.00 21.28           O  
-ATOM   2994  CB  ALA A 475       5.577  -2.635 -59.095  1.00 26.70           C  
-ATOM   2995  N   TRP A 476       4.803   0.739 -59.687  1.00 16.32           N  
-ATOM   2996  CA  TRP A 476       3.823   1.626 -60.291  1.00 22.99           C  
-ATOM   2997  C   TRP A 476       4.484   2.484 -61.358  1.00 29.67           C  
-ATOM   2998  O   TRP A 476       5.014   3.557 -61.072  1.00 30.03           O  
-ATOM   2999  CB  TRP A 476       3.154   2.508 -59.235  1.00 22.72           C  
-ATOM   3000  CG  TRP A 476       1.988   3.287 -59.769  1.00 21.98           C  
-ATOM   3001  CD1 TRP A 476       1.996   4.578 -60.208  1.00 27.00           C  
-ATOM   3002  CD2 TRP A 476       0.645   2.818 -59.929  1.00 24.56           C  
-ATOM   3003  NE1 TRP A 476       0.740   4.945 -60.626  1.00 29.89           N  
-ATOM   3004  CE2 TRP A 476      -0.108   3.881 -60.466  1.00 33.74           C  
-ATOM   3005  CE3 TRP A 476       0.005   1.603 -59.668  1.00 26.12           C  
-ATOM   3006  CZ2 TRP A 476      -1.469   3.766 -60.746  1.00 36.26           C  
-ATOM   3007  CZ3 TRP A 476      -1.346   1.490 -59.948  1.00 26.39           C  
-ATOM   3008  CH2 TRP A 476      -2.068   2.565 -60.481  1.00 30.18           C  
-ATOM   3009  N   ASN A 477       4.455   1.989 -62.590  1.00 36.60           N  
-ATOM   3010  CA  ASN A 477       5.023   2.695 -63.728  1.00 28.74           C  
-ATOM   3011  C   ASN A 477       3.922   3.066 -64.718  1.00 30.29           C  
-ATOM   3012  O   ASN A 477       3.517   2.239 -65.536  1.00 32.58           O  
-ATOM   3013  CB  ASN A 477       6.097   1.835 -64.400  1.00 24.70           C  
-ATOM   3014  CG  ASN A 477       6.625   2.447 -65.681  1.00 29.25           C  
-ATOM   3015  OD1 ASN A 477       6.580   3.660 -65.869  1.00 30.61           O  
-ATOM   3016  ND2 ASN A 477       7.132   1.602 -66.574  1.00 34.84           N  
-ATOM   3017  N   PRO A 478       3.430   4.313 -64.636  1.00 25.05           N  
-ATOM   3018  CA  PRO A 478       2.327   4.845 -65.448  1.00 24.45           C  
-ATOM   3019  C   PRO A 478       2.469   4.597 -66.950  1.00 26.06           C  
-ATOM   3020  O   PRO A 478       1.464   4.553 -67.658  1.00 33.12           O  
-ATOM   3021  CB  PRO A 478       2.374   6.343 -65.143  1.00 20.41           C  
-ATOM   3022  CG  PRO A 478       2.890   6.409 -63.759  1.00 20.26           C  
-ATOM   3023  CD  PRO A 478       3.901   5.301 -63.650  1.00 21.92           C  
-ATOM   3024  N   ALA A 479       3.699   4.438 -67.425  1.00 26.02           N  
-ATOM   3025  CA  ALA A 479       3.942   4.200 -68.841  1.00 29.39           C  
-ATOM   3026  C   ALA A 479       3.487   2.807 -69.265  1.00 35.35           C  
-ATOM   3027  O   ALA A 479       2.901   2.631 -70.334  1.00 44.24           O  
-ATOM   3028  CB  ALA A 479       5.416   4.391 -69.162  1.00 33.35           C  
-ATOM   3029  N   ALA A 480       3.751   1.821 -68.414  1.00 32.64           N  
-ATOM   3030  CA  ALA A 480       3.524   0.423 -68.763  1.00 34.46           C  
-ATOM   3031  C   ALA A 480       2.231  -0.142 -68.179  1.00 31.95           C  
-ATOM   3032  O   ALA A 480       1.973  -1.339 -68.291  1.00 28.64           O  
-ATOM   3033  CB  ALA A 480       4.710  -0.419 -68.310  1.00 27.31           C  
-ATOM   3034  N   LEU A 481       1.423   0.718 -67.564  1.00 34.11           N  
-ATOM   3035  CA  LEU A 481       0.211   0.276 -66.878  1.00 26.21           C  
-ATOM   3036  C   LEU A 481      -0.793  -0.397 -67.808  1.00 30.88           C  
-ATOM   3037  O   LEU A 481      -1.340  -1.449 -67.480  1.00 29.59           O  
-ATOM   3038  CB  LEU A 481      -0.461   1.453 -66.170  1.00 21.64           C  
-ATOM   3039  CG  LEU A 481       0.178   1.912 -64.860  1.00 26.64           C  
-ATOM   3040  CD1 LEU A 481      -0.740   2.883 -64.134  1.00 26.26           C  
-ATOM   3041  CD2 LEU A 481       0.510   0.721 -63.978  1.00 33.05           C  
-ATOM   3042  N   ASP A 482      -1.035   0.208 -68.966  1.00 33.89           N  
-ATOM   3043  CA  ASP A 482      -2.020  -0.327 -69.902  1.00 36.75           C  
-ATOM   3044  C   ASP A 482      -1.543  -1.625 -70.549  1.00 30.97           C  
-ATOM   3045  O   ASP A 482      -2.336  -2.360 -71.136  1.00 29.74           O  
-ATOM   3046  CB  ASP A 482      -2.354   0.709 -70.978  1.00 32.61           C  
-ATOM   3047  CG  ASP A 482      -3.155   1.881 -70.432  1.00 36.27           C  
-ATOM   3048  OD1 ASP A 482      -3.775   1.730 -69.355  1.00 22.02           O  
-ATOM   3049  OD2 ASP A 482      -3.170   2.949 -71.081  1.00 28.15           O  
-ATOM   3050  N   GLU A 483      -0.248  -1.904 -70.434  1.00 31.79           N  
-ATOM   3051  CA  GLU A 483       0.325  -3.127 -70.984  1.00 28.62           C  
-ATOM   3052  C   GLU A 483       0.236  -4.280 -69.991  1.00 28.28           C  
-ATOM   3053  O   GLU A 483       0.430  -5.439 -70.356  1.00 26.44           O  
-ATOM   3054  CB  GLU A 483       1.781  -2.907 -71.385  1.00 31.60           C  
-ATOM   3055  CG  GLU A 483       1.989  -1.793 -72.390  1.00 41.01           C  
-ATOM   3056  CD  GLU A 483       3.457  -1.533 -72.662  1.00 50.68           C  
-ATOM   3057  OE1 GLU A 483       4.198  -2.508 -72.917  1.00 42.94           O  
-ATOM   3058  OE2 GLU A 483       3.871  -0.354 -72.610  1.00 47.28           O  
-ATOM   3059  N   MET A 484      -0.048  -3.955 -68.733  1.00 36.43           N  
-ATOM   3060  CA  MET A 484      -0.165  -4.967 -67.689  1.00 35.52           C  
-ATOM   3061  C   MET A 484      -1.558  -5.583 -67.671  1.00 34.20           C  
-ATOM   3062  O   MET A 484      -2.537  -4.942 -68.054  1.00 37.90           O  
-ATOM   3063  CB  MET A 484       0.143  -4.374 -66.315  1.00 36.76           C  
-ATOM   3064  CG  MET A 484       1.489  -3.687 -66.197  1.00 31.92           C  
-ATOM   3065  SD  MET A 484       1.755  -3.123 -64.507  1.00 41.18           S  
-ATOM   3066  CE  MET A 484       3.014  -1.875 -64.748  1.00 38.32           C  
-ATOM   3067  N   ALA A 485      -1.642  -6.828 -67.218  1.00 31.67           N  
-ATOM   3068  CA  ALA A 485      -2.926  -7.500 -67.081  1.00 35.16           C  
-ATOM   3069  C   ALA A 485      -3.728  -6.852 -65.963  1.00 38.61           C  
-ATOM   3070  O   ALA A 485      -4.943  -6.684 -66.066  1.00 44.60           O  
-ATOM   3071  CB  ALA A 485      -2.729  -8.984 -66.810  1.00 32.18           C  
-ATOM   3072  N   LEU A 486      -3.031  -6.480 -64.896  1.00 31.85           N  
-ATOM   3073  CA  LEU A 486      -3.666  -5.850 -63.749  1.00 35.75           C  
-ATOM   3074  C   LEU A 486      -2.670  -4.923 -63.060  1.00 37.48           C  
-ATOM   3075  O   LEU A 486      -1.593  -5.359 -62.650  1.00 38.46           O  
-ATOM   3076  CB  LEU A 486      -4.190  -6.913 -62.777  1.00 32.24           C  
-ATOM   3077  CG  LEU A 486      -5.464  -6.618 -61.979  1.00 42.57           C  
-ATOM   3078  CD1 LEU A 486      -6.074  -7.914 -61.469  1.00 53.99           C  
-ATOM   3079  CD2 LEU A 486      -5.194  -5.669 -60.819  1.00 50.16           C  
-ATOM   3080  N   PRO A 487      -3.025  -3.634 -62.942  1.00 32.22           N  
-ATOM   3081  CA  PRO A 487      -2.156  -2.649 -62.293  1.00 30.30           C  
-ATOM   3082  C   PRO A 487      -1.814  -3.080 -60.874  1.00 30.36           C  
-ATOM   3083  O   PRO A 487      -2.692  -3.562 -60.160  1.00 42.17           O  
-ATOM   3084  CB  PRO A 487      -3.001  -1.371 -62.298  1.00 36.87           C  
-ATOM   3085  CG  PRO A 487      -4.001  -1.574 -63.387  1.00 29.37           C  
-ATOM   3086  CD  PRO A 487      -4.296  -3.040 -63.389  1.00 33.37           C  
-ATOM   3087  N   PRO A 488      -0.545  -2.922 -60.476  1.00 28.16           N  
-ATOM   3088  CA  PRO A 488      -0.055  -3.388 -59.174  1.00 32.49           C  
-ATOM   3089  C   PRO A 488      -0.829  -2.807 -57.997  1.00 29.29           C  
-ATOM   3090  O   PRO A 488      -1.116  -1.611 -57.967  1.00 29.58           O  
-ATOM   3091  CB  PRO A 488       1.402  -2.909 -59.153  1.00 27.81           C  
-ATOM   3092  CG  PRO A 488       1.485  -1.846 -60.195  1.00 25.19           C  
-ATOM   3093  CD  PRO A 488       0.511  -2.253 -61.251  1.00 26.56           C  
-ATOM   3094  N   CYS A 489      -1.173  -3.664 -57.043  1.00 28.55           N  
-ATOM   3095  CA  CYS A 489      -1.853  -3.224 -55.837  1.00 30.68           C  
-ATOM   3096  C   CYS A 489      -0.815  -2.924 -54.759  1.00 31.99           C  
-ATOM   3097  O   CYS A 489      -0.735  -1.798 -54.267  1.00 29.23           O  
-ATOM   3098  CB  CYS A 489      -2.860  -4.276 -55.371  1.00 32.42           C  
-ATOM   3099  SG  CYS A 489      -4.220  -4.544 -56.539  1.00 73.93           S  
-ATOM   3100  N   HIS A 490      -0.014  -3.924 -54.402  1.00 33.89           N  
-ATOM   3101  CA  HIS A 490       1.173  -3.679 -53.590  1.00 25.93           C  
-ATOM   3102  C   HIS A 490       2.240  -3.087 -54.503  1.00 23.37           C  
-ATOM   3103  O   HIS A 490       2.983  -3.813 -55.160  1.00 33.97           O  
-ATOM   3104  CB  HIS A 490       1.664  -4.962 -52.906  1.00 28.90           C  
-ATOM   3105  CG  HIS A 490       1.761  -6.149 -53.815  1.00 34.16           C  
-ATOM   3106  ND1 HIS A 490       2.967  -6.702 -54.190  1.00 36.75           N  
-ATOM   3107  CD2 HIS A 490       0.803  -6.897 -54.413  1.00 39.58           C  
-ATOM   3108  CE1 HIS A 490       2.748  -7.736 -54.983  1.00 32.26           C  
-ATOM   3109  NE2 HIS A 490       1.443  -7.874 -55.135  1.00 33.81           N  
-ATOM   3110  N   LEU A 491       2.304  -1.759 -54.543  1.00 19.43           N  
-ATOM   3111  CA  LEU A 491       3.017  -1.064 -55.611  1.00 24.25           C  
-ATOM   3112  C   LEU A 491       4.350  -0.444 -55.204  1.00 24.83           C  
-ATOM   3113  O   LEU A 491       5.131  -0.035 -56.063  1.00 25.59           O  
-ATOM   3114  CB  LEU A 491       2.116   0.028 -56.193  1.00 25.98           C  
-ATOM   3115  CG  LEU A 491       1.625   1.085 -55.202  1.00 23.49           C  
-ATOM   3116  CD1 LEU A 491       2.507   2.320 -55.222  1.00 24.68           C  
-ATOM   3117  CD2 LEU A 491       0.185   1.461 -55.489  1.00 19.88           C  
-ATOM   3118  N   LEU A 492       4.607  -0.360 -53.904  1.00 28.51           N  
-ATOM   3119  CA  LEU A 492       5.785   0.348 -53.419  1.00 21.55           C  
-ATOM   3120  C   LEU A 492       6.211  -0.118 -52.032  1.00 22.49           C  
-ATOM   3121  O   LEU A 492       5.384  -0.237 -51.132  1.00 17.82           O  
-ATOM   3122  CB  LEU A 492       5.509   1.851 -53.402  1.00 17.70           C  
-ATOM   3123  CG  LEU A 492       6.581   2.782 -52.839  1.00 21.71           C  
-ATOM   3124  CD1 LEU A 492       6.806   3.938 -53.795  1.00 16.70           C  
-ATOM   3125  CD2 LEU A 492       6.174   3.298 -51.466  1.00 21.21           C  
-ATOM   3126  N   CYS A 493       7.501  -0.381 -51.854  1.00 21.28           N  
-ATOM   3127  CA  CYS A 493       8.001  -0.739 -50.531  1.00 20.79           C  
-ATOM   3128  C   CYS A 493       9.301  -0.013 -50.209  1.00 26.76           C  
-ATOM   3129  O   CYS A 493      10.122   0.235 -51.090  1.00 32.53           O  
-ATOM   3130  CB  CYS A 493       8.191  -2.255 -50.407  1.00 19.12           C  
-ATOM   3131  SG  CYS A 493       9.589  -2.951 -51.308  1.00 24.73           S  
-ATOM   3132  N   GLN A 494       9.469   0.334 -48.936  1.00 23.73           N  
-ATOM   3133  CA  GLN A 494      10.645   1.066 -48.478  1.00 25.16           C  
-ATOM   3134  C   GLN A 494      11.243   0.410 -47.237  1.00 26.23           C  
-ATOM   3135  O   GLN A 494      10.515  -0.067 -46.365  1.00 23.36           O  
-ATOM   3136  CB  GLN A 494      10.286   2.526 -48.188  1.00 18.24           C  
-ATOM   3137  CG  GLN A 494      11.446   3.368 -47.700  1.00 18.01           C  
-ATOM   3138  CD  GLN A 494      11.025   4.768 -47.319  1.00 18.17           C  
-ATOM   3139  OE1 GLN A 494       9.840   5.096 -47.336  1.00 23.20           O  
-ATOM   3140  NE2 GLN A 494      11.994   5.606 -46.972  1.00 16.24           N  
-ATOM   3141  N   PHE A 495      12.571   0.388 -47.162  1.00 26.07           N  
-ATOM   3142  CA  PHE A 495      13.262  -0.275 -46.060  1.00 24.88           C  
-ATOM   3143  C   PHE A 495      13.948   0.707 -45.113  1.00 23.34           C  
-ATOM   3144  O   PHE A 495      14.125   1.883 -45.437  1.00 22.83           O  
-ATOM   3145  CB  PHE A 495      14.278  -1.277 -46.607  1.00 19.25           C  
-ATOM   3146  CG  PHE A 495      13.648  -2.436 -47.322  1.00 20.10           C  
-ATOM   3147  CD1 PHE A 495      13.202  -3.541 -46.616  1.00 16.77           C  
-ATOM   3148  CD2 PHE A 495      13.491  -2.416 -48.698  1.00 21.64           C  
-ATOM   3149  CE1 PHE A 495      12.619  -4.609 -47.270  1.00 15.99           C  
-ATOM   3150  CE2 PHE A 495      12.908  -3.481 -49.358  1.00 21.30           C  
-ATOM   3151  CZ  PHE A 495      12.471  -4.579 -48.643  1.00 23.34           C  
-ATOM   3152  N   TYR A 496      14.338   0.205 -43.944  1.00 19.75           N  
-ATOM   3153  CA  TYR A 496      14.863   1.046 -42.876  1.00 19.28           C  
-ATOM   3154  C   TYR A 496      15.741   0.248 -41.919  1.00 23.29           C  
-ATOM   3155  O   TYR A 496      15.399  -0.866 -41.535  1.00 24.06           O  
-ATOM   3156  CB  TYR A 496      13.700   1.695 -42.125  1.00 15.00           C  
-ATOM   3157  CG  TYR A 496      14.059   2.496 -40.892  1.00 20.31           C  
-ATOM   3158  CD1 TYR A 496      14.116   1.894 -39.639  1.00 20.75           C  
-ATOM   3159  CD2 TYR A 496      14.300   3.861 -40.973  1.00 25.83           C  
-ATOM   3160  CE1 TYR A 496      14.427   2.621 -38.508  1.00 19.78           C  
-ATOM   3161  CE2 TYR A 496      14.613   4.600 -39.845  1.00 32.81           C  
-ATOM   3162  CZ  TYR A 496      14.674   3.973 -38.615  1.00 32.38           C  
-ATOM   3163  OH  TYR A 496      14.982   4.700 -37.489  1.00 36.04           O  
-ATOM   3164  N   VAL A 497      16.879   0.822 -41.542  1.00 29.47           N  
-ATOM   3165  CA  VAL A 497      17.788   0.184 -40.595  1.00 21.78           C  
-ATOM   3166  C   VAL A 497      18.130   1.149 -39.464  1.00 31.98           C  
-ATOM   3167  O   VAL A 497      18.373   2.333 -39.703  1.00 39.35           O  
-ATOM   3168  CB  VAL A 497      19.086  -0.286 -41.280  1.00 21.40           C  
-ATOM   3169  CG1 VAL A 497      20.004  -0.970 -40.279  1.00 35.20           C  
-ATOM   3170  CG2 VAL A 497      18.765  -1.225 -42.423  1.00 20.61           C  
-ATOM   3171  N   ASN A 498      18.143   0.644 -38.234  1.00 26.22           N  
-ATOM   3172  CA  ASN A 498      18.373   1.495 -37.072  1.00 31.54           C  
-ATOM   3173  C   ASN A 498      19.704   1.241 -36.373  1.00 35.57           C  
-ATOM   3174  O   ASN A 498      20.668   0.781 -36.986  1.00 32.47           O  
-ATOM   3175  CB  ASN A 498      17.234   1.326 -36.061  1.00 31.95           C  
-ATOM   3176  CG  ASN A 498      17.134  -0.092 -35.518  1.00 25.82           C  
-ATOM   3177  OD1 ASN A 498      17.892  -0.979 -35.908  1.00 21.60           O  
-ATOM   3178  ND2 ASN A 498      16.197  -0.306 -34.603  1.00 27.69           N  
-ATOM   3179  N   ASP A 499      19.733   1.559 -35.081  1.00 32.83           N  
-ATOM   3180  CA  ASP A 499      20.888   1.324 -34.224  1.00 22.72           C  
-ATOM   3181  C   ASP A 499      21.423  -0.097 -34.336  1.00 33.31           C  
-ATOM   3182  O   ASP A 499      22.562  -0.316 -34.743  1.00 33.22           O  
-ATOM   3183  CB  ASP A 499      20.523   1.609 -32.764  1.00 31.09           C  
-ATOM   3184  CG  ASP A 499      20.693   3.065 -32.391  1.00 56.29           C  
-ATOM   3185  OD1 ASP A 499      20.913   3.888 -33.305  1.00 67.33           O  
-ATOM   3186  OD2 ASP A 499      20.605   3.388 -31.185  1.00 58.43           O  
-ATOM   3187  N   GLN A 500      20.575  -1.059 -33.989  1.00 35.55           N  
-ATOM   3188  CA  GLN A 500      21.003  -2.432 -33.756  1.00 28.30           C  
-ATOM   3189  C   GLN A 500      20.957  -3.321 -34.998  1.00 20.23           C  
-ATOM   3190  O   GLN A 500      20.707  -4.523 -34.891  1.00 18.09           O  
-ATOM   3191  CB  GLN A 500      20.136  -3.047 -32.658  1.00 38.51           C  
-ATOM   3192  CG  GLN A 500      19.597  -2.035 -31.652  1.00 31.99           C  
-ATOM   3193  CD  GLN A 500      20.579  -1.729 -30.538  1.00 36.40           C  
-ATOM   3194  OE1 GLN A 500      20.357  -2.102 -29.386  1.00 45.09           O  
-ATOM   3195  NE2 GLN A 500      21.667  -1.042 -30.872  1.00 32.79           N  
-ATOM   3196  N   LYS A 501      21.207  -2.731 -36.163  1.00 23.05           N  
-ATOM   3197  CA  LYS A 501      21.183  -3.465 -37.427  1.00 24.24           C  
-ATOM   3198  C   LYS A 501      19.872  -4.227 -37.604  1.00 25.65           C  
-ATOM   3199  O   LYS A 501      19.869  -5.410 -37.944  1.00 27.12           O  
-ATOM   3200  CB  LYS A 501      22.371  -4.428 -37.511  1.00 28.50           C  
-ATOM   3201  CG  LYS A 501      23.712  -3.746 -37.736  1.00 31.20           C  
-ATOM   3202  CD  LYS A 501      24.861  -4.603 -37.218  1.00 35.80           C  
-ATOM   3203  CE  LYS A 501      24.962  -5.933 -37.949  1.00 46.19           C  
-ATOM   3204  NZ  LYS A 501      25.490  -5.778 -39.335  1.00 44.11           N  
-ATOM   3205  N   GLU A 502      18.761  -3.540 -37.362  1.00 31.17           N  
-ATOM   3206  CA  GLU A 502      17.442  -4.148 -37.473  1.00 23.50           C  
-ATOM   3207  C   GLU A 502      16.679  -3.580 -38.665  1.00 23.55           C  
-ATOM   3208  O   GLU A 502      16.599  -2.365 -38.842  1.00 26.83           O  
-ATOM   3209  CB  GLU A 502      16.649  -3.941 -36.182  1.00 15.64           C  
-ATOM   3210  CG  GLU A 502      17.421  -4.323 -34.934  1.00 21.21           C  
-ATOM   3211  CD  GLU A 502      16.586  -4.224 -33.676  1.00 30.96           C  
-ATOM   3212  OE1 GLU A 502      16.351  -5.272 -33.036  1.00 44.63           O  
-ATOM   3213  OE2 GLU A 502      16.167  -3.101 -33.323  1.00 30.24           O  
-ATOM   3214  N   LEU A 503      16.122  -4.467 -39.481  1.00 23.10           N  
-ATOM   3215  CA  LEU A 503      15.441  -4.056 -40.701  1.00 17.49           C  
-ATOM   3216  C   LEU A 503      13.935  -3.918 -40.498  1.00 24.80           C  
-ATOM   3217  O   LEU A 503      13.300  -4.753 -39.850  1.00 34.56           O  
-ATOM   3218  CB  LEU A 503      15.728  -5.053 -41.824  1.00 17.63           C  
-ATOM   3219  CG  LEU A 503      15.184  -4.720 -43.214  1.00 15.62           C  
-ATOM   3220  CD1 LEU A 503      15.936  -3.548 -43.832  1.00 19.53           C  
-ATOM   3221  CD2 LEU A 503      15.250  -5.941 -44.117  1.00 13.41           C  
-ATOM   3222  N   SER A 504      13.376  -2.850 -41.055  1.00 20.28           N  
-ATOM   3223  CA  SER A 504      11.935  -2.637 -41.072  1.00 20.07           C  
-ATOM   3224  C   SER A 504      11.488  -2.286 -42.488  1.00 21.70           C  
-ATOM   3225  O   SER A 504      12.257  -1.721 -43.268  1.00 21.65           O  
-ATOM   3226  CB  SER A 504      11.533  -1.539 -40.086  1.00 21.62           C  
-ATOM   3227  OG  SER A 504      11.812  -1.926 -38.750  1.00 29.94           O  
-ATOM   3228  N   CYS A 505      10.248  -2.623 -42.820  1.00 18.94           N  
-ATOM   3229  CA  CYS A 505       9.763  -2.452 -44.181  1.00 16.88           C  
-ATOM   3230  C   CYS A 505       8.321  -1.955 -44.232  1.00 17.76           C  
-ATOM   3231  O   CYS A 505       7.436  -2.528 -43.601  1.00 17.77           O  
-ATOM   3232  CB  CYS A 505       9.888  -3.771 -44.948  1.00 17.99           C  
-ATOM   3233  SG  CYS A 505       9.128  -3.760 -46.587  1.00 26.66           S  
-ATOM   3234  N   ILE A 506       8.098  -0.882 -44.985  1.00 18.53           N  
-ATOM   3235  CA  ILE A 506       6.751  -0.385 -45.246  1.00 15.36           C  
-ATOM   3236  C   ILE A 506       6.318  -0.769 -46.654  1.00 18.92           C  
-ATOM   3237  O   ILE A 506       7.085  -0.615 -47.600  1.00 21.12           O  
-ATOM   3238  CB  ILE A 506       6.654   1.148 -45.108  1.00 12.13           C  
-ATOM   3239  CG1 ILE A 506       7.004   1.590 -43.692  1.00 19.33           C  
-ATOM   3240  CG2 ILE A 506       5.254   1.628 -45.461  1.00 12.34           C  
-ATOM   3241  CD1 ILE A 506       7.103   3.090 -43.545  1.00 24.74           C  
-ATOM   3242  N   MET A 507       5.095  -1.267 -46.796  1.00 16.10           N  
-ATOM   3243  CA  MET A 507       4.537  -1.500 -48.118  1.00 13.74           C  
-ATOM   3244  C   MET A 507       3.237  -0.729 -48.278  1.00 16.99           C  
-ATOM   3245  O   MET A 507       2.328  -0.848 -47.459  1.00 19.50           O  
-ATOM   3246  CB  MET A 507       4.307  -2.990 -48.366  1.00 17.47           C  
-ATOM   3247  CG  MET A 507       3.785  -3.299 -49.764  1.00 19.79           C  
-ATOM   3248  SD  MET A 507       1.985  -3.335 -49.884  1.00 22.06           S  
-ATOM   3249  CE  MET A 507       1.628  -4.891 -49.075  1.00 20.35           C  
-ATOM   3250  N   TYR A 508       3.159   0.072 -49.335  1.00 19.50           N  
-ATOM   3251  CA  TYR A 508       1.950   0.825 -49.632  1.00 20.63           C  
-ATOM   3252  C   TYR A 508       1.098   0.075 -50.647  1.00 19.03           C  
-ATOM   3253  O   TYR A 508       1.575  -0.319 -51.711  1.00 22.59           O  
-ATOM   3254  CB  TYR A 508       2.285   2.228 -50.151  1.00 17.87           C  
-ATOM   3255  CG  TYR A 508       1.057   3.080 -50.375  1.00 16.38           C  
-ATOM   3256  CD1 TYR A 508       0.478   3.784 -49.326  1.00 17.48           C  
-ATOM   3257  CD2 TYR A 508       0.464   3.165 -51.629  1.00 19.17           C  
-ATOM   3258  CE1 TYR A 508      -0.652   4.554 -49.522  1.00 18.66           C  
-ATOM   3259  CE2 TYR A 508      -0.667   3.933 -51.834  1.00 18.48           C  
-ATOM   3260  CZ  TYR A 508      -1.220   4.625 -50.777  1.00 20.70           C  
-ATOM   3261  OH  TYR A 508      -2.346   5.394 -50.975  1.00 28.95           O  
-ATOM   3262  N   GLN A 509      -0.169  -0.118 -50.308  1.00 19.44           N  
-ATOM   3263  CA  GLN A 509      -1.083  -0.858 -51.162  1.00 24.30           C  
-ATOM   3264  C   GLN A 509      -2.275   0.016 -51.539  1.00 26.24           C  
-ATOM   3265  O   GLN A 509      -3.040   0.439 -50.672  1.00 22.88           O  
-ATOM   3266  CB  GLN A 509      -1.542  -2.129 -50.454  1.00 22.56           C  
-ATOM   3267  CG  GLN A 509      -2.170  -3.165 -51.356  1.00 26.85           C  
-ATOM   3268  CD  GLN A 509      -2.540  -4.421 -50.598  1.00 34.92           C  
-ATOM   3269  OE1 GLN A 509      -1.886  -4.780 -49.620  1.00 27.80           O  
-ATOM   3270  NE2 GLN A 509      -3.599  -5.090 -51.036  1.00 44.46           N  
-ATOM   3271  N   ARG A 510      -2.424   0.297 -52.831  1.00 24.79           N  
-ATOM   3272  CA  ARG A 510      -3.478   1.195 -53.292  1.00 26.83           C  
-ATOM   3273  C   ARG A 510      -4.860   0.595 -53.072  1.00 26.87           C  
-ATOM   3274  O   ARG A 510      -5.792   1.294 -52.674  1.00 26.00           O  
-ATOM   3275  CB  ARG A 510      -3.291   1.544 -54.771  1.00 22.45           C  
-ATOM   3276  CG  ARG A 510      -3.250   0.349 -55.702  1.00 23.26           C  
-ATOM   3277  CD  ARG A 510      -3.455   0.767 -57.146  1.00 31.22           C  
-ATOM   3278  NE  ARG A 510      -3.587  -0.388 -58.028  1.00 29.10           N  
-ATOM   3279  CZ  ARG A 510      -4.715  -1.069 -58.195  1.00 26.64           C  
-ATOM   3280  NH1 ARG A 510      -5.809  -0.713 -57.538  1.00 26.46           N  
-ATOM   3281  NH2 ARG A 510      -4.749  -2.108 -59.016  1.00 33.11           N  
-ATOM   3282  N   SER A 511      -4.982  -0.703 -53.329  1.00 27.49           N  
-ATOM   3283  CA  SER A 511      -6.255  -1.397 -53.205  1.00 33.28           C  
-ATOM   3284  C   SER A 511      -6.073  -2.666 -52.389  1.00 36.91           C  
-ATOM   3285  O   SER A 511      -5.123  -3.416 -52.608  1.00 41.83           O  
-ATOM   3286  CB  SER A 511      -6.827  -1.724 -54.582  1.00 32.62           C  
-ATOM   3287  OG  SER A 511      -8.145  -2.230 -54.480  1.00 41.05           O  
-ATOM   3288  N   CYS A 512      -6.983  -2.906 -51.451  1.00 30.42           N  
-ATOM   3289  CA  CYS A 512      -6.813  -4.006 -50.512  1.00 24.40           C  
-ATOM   3290  C   CYS A 512      -8.077  -4.834 -50.307  1.00 28.67           C  
-ATOM   3291  O   CYS A 512      -8.982  -4.429 -49.580  1.00 25.41           O  
-ATOM   3292  CB  CYS A 512      -6.342  -3.467 -49.162  1.00 27.49           C  
-ATOM   3293  SG  CYS A 512      -4.955  -2.313 -49.257  1.00 42.70           S  
-ATOM   3294  N   ASP A 513      -8.130  -5.999 -50.946  1.00 35.74           N  
-ATOM   3295  CA  ASP A 513      -9.155  -6.985 -50.631  1.00 32.79           C  
-ATOM   3296  C   ASP A 513      -8.859  -7.531 -49.241  1.00 24.68           C  
-ATOM   3297  O   ASP A 513      -7.991  -8.386 -49.071  1.00 24.05           O  
-ATOM   3298  CB  ASP A 513      -9.181  -8.109 -51.670  1.00 39.26           C  
-ATOM   3299  CG  ASP A 513     -10.400  -9.009 -51.532  1.00 48.85           C  
-ATOM   3300  OD1 ASP A 513     -10.997  -9.061 -50.434  1.00 39.86           O  
-ATOM   3301  OD2 ASP A 513     -10.762  -9.672 -52.529  1.00 59.93           O  
-ATOM   3302  N   VAL A 514      -9.580  -7.024 -48.249  1.00 18.17           N  
-ATOM   3303  CA  VAL A 514      -9.282  -7.324 -46.854  1.00 20.03           C  
-ATOM   3304  C   VAL A 514      -9.473  -8.792 -46.500  1.00 28.98           C  
-ATOM   3305  O   VAL A 514      -8.588  -9.411 -45.907  1.00 36.40           O  
-ATOM   3306  CB  VAL A 514     -10.143  -6.470 -45.916  1.00 17.77           C  
-ATOM   3307  CG1 VAL A 514     -10.083  -7.005 -44.496  1.00 23.12           C  
-ATOM   3308  CG2 VAL A 514      -9.671  -5.039 -45.961  1.00 26.30           C  
-ATOM   3309  N   GLY A 515     -10.622  -9.347 -46.865  1.00 26.43           N  
-ATOM   3310  CA  GLY A 515     -10.929 -10.722 -46.525  1.00 27.00           C  
-ATOM   3311  C   GLY A 515     -10.034 -11.719 -47.230  1.00 28.16           C  
-ATOM   3312  O   GLY A 515      -9.684 -12.758 -46.672  1.00 35.10           O  
-ATOM   3313  N   LEU A 516      -9.639 -11.390 -48.454  1.00 27.83           N  
-ATOM   3314  CA  LEU A 516      -8.962 -12.354 -49.310  1.00 37.80           C  
-ATOM   3315  C   LEU A 516      -7.463 -12.099 -49.472  1.00 34.86           C  
-ATOM   3316  O   LEU A 516      -6.649 -12.992 -49.244  1.00 33.46           O  
-ATOM   3317  CB  LEU A 516      -9.630 -12.372 -50.684  1.00 41.76           C  
-ATOM   3318  CG  LEU A 516      -9.538 -13.701 -51.420  1.00 43.55           C  
-ATOM   3319  CD1 LEU A 516     -10.059 -14.835 -50.546  1.00 53.23           C  
-ATOM   3320  CD2 LEU A 516     -10.292 -13.642 -52.739  1.00 62.59           C  
-ATOM   3321  N   GLY A 517      -7.102 -10.882 -49.866  1.00 29.39           N  
-ATOM   3322  CA  GLY A 517      -5.731 -10.590 -50.244  1.00 26.27           C  
-ATOM   3323  C   GLY A 517      -4.799 -10.121 -49.138  1.00 27.05           C  
-ATOM   3324  O   GLY A 517      -3.622 -10.488 -49.120  1.00 21.80           O  
-ATOM   3325  N   VAL A 518      -5.318  -9.304 -48.225  1.00 25.49           N  
-ATOM   3326  CA  VAL A 518      -4.498  -8.662 -47.196  1.00 20.34           C  
-ATOM   3327  C   VAL A 518      -3.618  -9.623 -46.386  1.00 21.86           C  
-ATOM   3328  O   VAL A 518      -2.426  -9.359 -46.239  1.00 22.86           O  
-ATOM   3329  CB  VAL A 518      -5.375  -7.833 -46.221  1.00 17.41           C  
-ATOM   3330  CG1 VAL A 518      -4.623  -7.545 -44.928  1.00 11.45           C  
-ATOM   3331  CG2 VAL A 518      -5.802  -6.545 -46.887  1.00 22.08           C  
-ATOM   3332  N   PRO A 519      -4.179 -10.738 -45.866  1.00 21.22           N  
-ATOM   3333  CA  PRO A 519      -3.283 -11.626 -45.111  1.00 18.77           C  
-ATOM   3334  C   PRO A 519      -2.132 -12.156 -45.965  1.00 17.58           C  
-ATOM   3335  O   PRO A 519      -0.982 -12.219 -45.513  1.00 17.28           O  
-ATOM   3336  CB  PRO A 519      -4.207 -12.773 -44.675  1.00 17.99           C  
-ATOM   3337  CG  PRO A 519      -5.569 -12.196 -44.713  1.00 16.72           C  
-ATOM   3338  CD  PRO A 519      -5.563 -11.248 -45.865  1.00 15.95           C  
-ATOM   3339  N   PHE A 520      -2.469 -12.526 -47.197  1.00 13.98           N  
-ATOM   3340  CA  PHE A 520      -1.503 -12.988 -48.180  1.00 14.79           C  
-ATOM   3341  C   PHE A 520      -0.404 -11.955 -48.401  1.00 19.70           C  
-ATOM   3342  O   PHE A 520       0.771 -12.305 -48.484  1.00 26.26           O  
-ATOM   3343  CB  PHE A 520      -2.203 -13.297 -49.501  1.00 24.10           C  
-ATOM   3344  CG  PHE A 520      -1.357 -14.074 -50.469  1.00 30.36           C  
-ATOM   3345  CD1 PHE A 520      -0.470 -13.429 -51.319  1.00 33.17           C  
-ATOM   3346  CD2 PHE A 520      -1.458 -15.453 -50.534  1.00 28.40           C  
-ATOM   3347  CE1 PHE A 520       0.310 -14.150 -52.206  1.00 30.75           C  
-ATOM   3348  CE2 PHE A 520      -0.688 -16.176 -51.418  1.00 35.69           C  
-ATOM   3349  CZ  PHE A 520       0.190 -15.523 -52.261  1.00 39.08           C  
-ATOM   3350  N   ASN A 521      -0.792 -10.687 -48.504  1.00 20.02           N  
-ATOM   3351  CA  ASN A 521       0.171  -9.611 -48.699  1.00 19.85           C  
-ATOM   3352  C   ASN A 521       1.082  -9.429 -47.493  1.00 18.31           C  
-ATOM   3353  O   ASN A 521       2.303  -9.314 -47.635  1.00 19.30           O  
-ATOM   3354  CB  ASN A 521      -0.552  -8.305 -49.002  1.00 21.57           C  
-ATOM   3355  CG  ASN A 521      -1.318  -8.360 -50.300  1.00 23.30           C  
-ATOM   3356  OD1 ASN A 521      -2.522  -8.118 -50.332  1.00 26.70           O  
-ATOM   3357  ND2 ASN A 521      -0.625  -8.693 -51.381  1.00 25.23           N  
-ATOM   3358  N   ILE A 522       0.472  -9.392 -46.312  1.00 15.33           N  
-ATOM   3359  CA  ILE A 522       1.204  -9.344 -45.056  1.00 18.26           C  
-ATOM   3360  C   ILE A 522       2.286 -10.411 -45.023  1.00 15.45           C  
-ATOM   3361  O   ILE A 522       3.472 -10.106 -44.870  1.00 13.20           O  
-ATOM   3362  CB  ILE A 522       0.255  -9.528 -43.853  1.00 12.77           C  
-ATOM   3363  CG1 ILE A 522      -0.760  -8.385 -43.805  1.00 15.98           C  
-ATOM   3364  CG2 ILE A 522       1.043  -9.589 -42.568  1.00 14.26           C  
-ATOM   3365  CD1 ILE A 522      -1.785  -8.535 -42.715  1.00 20.46           C  
-ATOM   3366  N   ALA A 523       1.866 -11.660 -45.196  1.00 16.13           N  
-ATOM   3367  CA  ALA A 523       2.796 -12.781 -45.230  1.00 18.89           C  
-ATOM   3368  C   ALA A 523       3.875 -12.575 -46.290  1.00 16.58           C  
-ATOM   3369  O   ALA A 523       5.057 -12.852 -46.055  1.00 14.64           O  
-ATOM   3370  CB  ALA A 523       2.051 -14.084 -45.484  1.00 16.38           C  
-ATOM   3371  N   SER A 524       3.460 -12.073 -47.448  1.00 13.63           N  
-ATOM   3372  CA  SER A 524       4.354 -11.902 -48.580  1.00 12.74           C  
-ATOM   3373  C   SER A 524       5.504 -10.953 -48.275  1.00 14.04           C  
-ATOM   3374  O   SER A 524       6.676 -11.314 -48.412  1.00 18.31           O  
-ATOM   3375  CB  SER A 524       3.571 -11.402 -49.795  1.00 12.84           C  
-ATOM   3376  OG  SER A 524       4.380 -11.439 -50.952  1.00 21.27           O  
-ATOM   3377  N   TYR A 525       5.172  -9.736 -47.865  1.00 15.41           N  
-ATOM   3378  CA  TYR A 525       6.203  -8.734 -47.634  1.00 12.75           C  
-ATOM   3379  C   TYR A 525       6.942  -8.960 -46.319  1.00 12.12           C  
-ATOM   3380  O   TYR A 525       8.080  -8.518 -46.161  1.00 14.56           O  
-ATOM   3381  CB  TYR A 525       5.604  -7.329 -47.702  1.00  9.35           C  
-ATOM   3382  CG  TYR A 525       5.473  -6.866 -49.139  1.00 15.99           C  
-ATOM   3383  CD1 TYR A 525       4.379  -7.233 -49.908  1.00 17.15           C  
-ATOM   3384  CD2 TYR A 525       6.464  -6.100 -49.736  1.00 16.58           C  
-ATOM   3385  CE1 TYR A 525       4.263  -6.837 -51.222  1.00 16.35           C  
-ATOM   3386  CE2 TYR A 525       6.360  -5.695 -51.051  1.00 18.43           C  
-ATOM   3387  CZ  TYR A 525       5.257  -6.066 -51.792  1.00 20.49           C  
-ATOM   3388  OH  TYR A 525       5.149  -5.664 -53.104  1.00 27.92           O  
-ATOM   3389  N   SER A 526       6.316  -9.669 -45.385  1.00 13.74           N  
-ATOM   3390  CA  SER A 526       7.033 -10.088 -44.185  1.00 14.26           C  
-ATOM   3391  C   SER A 526       8.136 -11.069 -44.581  1.00 15.86           C  
-ATOM   3392  O   SER A 526       9.288 -10.946 -44.142  1.00 18.12           O  
-ATOM   3393  CB  SER A 526       6.086 -10.723 -43.167  1.00 14.62           C  
-ATOM   3394  OG  SER A 526       5.054  -9.827 -42.800  1.00 19.49           O  
-ATOM   3395  N   LEU A 527       7.774 -12.034 -45.426  1.00 14.74           N  
-ATOM   3396  CA  LEU A 527       8.733 -12.994 -45.967  1.00 12.55           C  
-ATOM   3397  C   LEU A 527       9.853 -12.283 -46.721  1.00 16.16           C  
-ATOM   3398  O   LEU A 527      11.035 -12.595 -46.531  1.00 17.68           O  
-ATOM   3399  CB  LEU A 527       8.038 -13.997 -46.892  1.00 12.13           C  
-ATOM   3400  CG  LEU A 527       8.923 -15.118 -47.444  1.00 11.52           C  
-ATOM   3401  CD1 LEU A 527       9.499 -15.949 -46.310  1.00 12.47           C  
-ATOM   3402  CD2 LEU A 527       8.144 -15.998 -48.408  1.00 15.54           C  
-ATOM   3403  N   LEU A 528       9.475 -11.332 -47.576  1.00 16.14           N  
-ATOM   3404  CA  LEU A 528      10.455 -10.525 -48.302  1.00 15.04           C  
-ATOM   3405  C   LEU A 528      11.425  -9.878 -47.326  1.00 15.18           C  
-ATOM   3406  O   LEU A 528      12.636  -9.910 -47.537  1.00 17.04           O  
-ATOM   3407  CB  LEU A 528       9.777  -9.443 -49.152  1.00 14.46           C  
-ATOM   3408  CG  LEU A 528      10.727  -8.457 -49.848  1.00  7.33           C  
-ATOM   3409  CD1 LEU A 528      11.650  -9.192 -50.802  1.00  7.75           C  
-ATOM   3410  CD2 LEU A 528       9.964  -7.363 -50.581  1.00  9.73           C  
-ATOM   3411  N   THR A 529      10.884  -9.304 -46.254  1.00 12.84           N  
-ATOM   3412  CA  THR A 529      11.710  -8.660 -45.239  1.00 13.72           C  
-ATOM   3413  C   THR A 529      12.684  -9.646 -44.600  1.00 17.03           C  
-ATOM   3414  O   THR A 529      13.853  -9.319 -44.406  1.00 17.44           O  
-ATOM   3415  CB  THR A 529      10.863  -8.014 -44.130  1.00 11.04           C  
-ATOM   3416  OG1 THR A 529       9.953  -7.064 -44.700  1.00  9.12           O  
-ATOM   3417  CG2 THR A 529      11.770  -7.304 -43.137  1.00 13.86           C  
-ATOM   3418  N   LEU A 530      12.203 -10.844 -44.270  1.00 20.68           N  
-ATOM   3419  CA  LEU A 530      13.083 -11.889 -43.749  1.00 16.00           C  
-ATOM   3420  C   LEU A 530      14.239 -12.162 -44.704  1.00 16.92           C  
-ATOM   3421  O   LEU A 530      15.409 -12.107 -44.310  1.00 15.76           O  
-ATOM   3422  CB  LEU A 530      12.324 -13.193 -43.508  1.00 13.23           C  
-ATOM   3423  CG  LEU A 530      11.284 -13.277 -42.397  1.00 14.51           C  
-ATOM   3424  CD1 LEU A 530      11.045 -14.731 -42.032  1.00 16.51           C  
-ATOM   3425  CD2 LEU A 530      11.730 -12.498 -41.186  1.00 17.57           C  
-ATOM   3426  N   MET A 531      13.906 -12.452 -45.958  1.00 14.09           N  
-ATOM   3427  CA  MET A 531      14.920 -12.803 -46.946  1.00 22.33           C  
-ATOM   3428  C   MET A 531      15.956 -11.692 -47.127  1.00 23.29           C  
-ATOM   3429  O   MET A 531      17.165 -11.937 -47.031  1.00 26.57           O  
-ATOM   3430  CB  MET A 531      14.248 -13.140 -48.276  1.00 15.03           C  
-ATOM   3431  CG  MET A 531      13.230 -14.258 -48.160  1.00 12.24           C  
-ATOM   3432  SD  MET A 531      12.165 -14.379 -49.601  1.00 25.10           S  
-ATOM   3433  CE  MET A 531      13.328 -14.948 -50.833  1.00 21.76           C  
-ATOM   3434  N   VAL A 532      15.476 -10.478 -47.381  1.00 16.32           N  
-ATOM   3435  CA  VAL A 532      16.355  -9.322 -47.514  1.00 14.84           C  
-ATOM   3436  C   VAL A 532      17.259  -9.177 -46.293  1.00 18.89           C  
-ATOM   3437  O   VAL A 532      18.465  -8.979 -46.427  1.00 18.69           O  
-ATOM   3438  CB  VAL A 532      15.553  -8.020 -47.712  1.00 14.13           C  
-ATOM   3439  CG1 VAL A 532      16.450  -6.810 -47.558  1.00 13.11           C  
-ATOM   3440  CG2 VAL A 532      14.888  -8.019 -49.073  1.00 20.36           C  
-ATOM   3441  N   ALA A 533      16.674  -9.301 -45.104  1.00 20.25           N  
-ATOM   3442  CA  ALA A 533      17.429  -9.148 -43.863  1.00 18.17           C  
-ATOM   3443  C   ALA A 533      18.546 -10.182 -43.761  1.00 22.44           C  
-ATOM   3444  O   ALA A 533      19.675  -9.848 -43.391  1.00 19.37           O  
-ATOM   3445  CB  ALA A 533      16.506  -9.251 -42.660  1.00 17.73           C  
-ATOM   3446  N   HIS A 534      18.234 -11.435 -44.083  1.00 23.74           N  
-ATOM   3447  CA  HIS A 534      19.251 -12.481 -44.049  1.00 23.69           C  
-ATOM   3448  C   HIS A 534      20.360 -12.213 -45.060  1.00 22.47           C  
-ATOM   3449  O   HIS A 534      21.537 -12.413 -44.765  1.00 23.13           O  
-ATOM   3450  CB  HIS A 534      18.650 -13.855 -44.321  1.00 17.19           C  
-ATOM   3451  CG  HIS A 534      19.677 -14.892 -44.655  1.00 19.86           C  
-ATOM   3452  ND1 HIS A 534      20.493 -15.462 -43.703  1.00 19.68           N  
-ATOM   3453  CD2 HIS A 534      20.045 -15.434 -45.840  1.00 24.49           C  
-ATOM   3454  CE1 HIS A 534      21.307 -16.326 -44.284  1.00 26.74           C  
-ATOM   3455  NE2 HIS A 534      21.056 -16.327 -45.581  1.00 28.12           N  
-ATOM   3456  N   VAL A 535      19.979 -11.767 -46.253  1.00 23.80           N  
-ATOM   3457  CA  VAL A 535      20.952 -11.512 -47.309  1.00 16.14           C  
-ATOM   3458  C   VAL A 535      21.830 -10.299 -46.967  1.00 18.85           C  
-ATOM   3459  O   VAL A 535      22.971 -10.199 -47.421  1.00 22.94           O  
-ATOM   3460  CB  VAL A 535      20.234 -11.330 -48.678  1.00 20.16           C  
-ATOM   3461  CG1 VAL A 535      21.079 -10.551 -49.671  1.00 28.76           C  
-ATOM   3462  CG2 VAL A 535      19.860 -12.690 -49.254  1.00 22.01           C  
-ATOM   3463  N   CYS A 536      21.321  -9.406 -46.124  1.00 20.79           N  
-ATOM   3464  CA  CYS A 536      22.060  -8.194 -45.770  1.00 17.85           C  
-ATOM   3465  C   CYS A 536      22.692  -8.238 -44.377  1.00 19.96           C  
-ATOM   3466  O   CYS A 536      23.148  -7.213 -43.872  1.00 20.06           O  
-ATOM   3467  CB  CYS A 536      21.142  -6.977 -45.863  1.00 15.85           C  
-ATOM   3468  SG  CYS A 536      20.490  -6.671 -47.514  1.00 32.32           S  
-ATOM   3469  N   ASN A 537      22.725  -9.422 -43.770  1.00 27.32           N  
-ATOM   3470  CA  ASN A 537      23.212  -9.599 -42.398  1.00 31.73           C  
-ATOM   3471  C   ASN A 537      22.513  -8.691 -41.392  1.00 29.54           C  
-ATOM   3472  O   ASN A 537      23.166  -8.008 -40.602  1.00 32.88           O  
-ATOM   3473  CB  ASN A 537      24.722  -9.369 -42.320  1.00 31.28           C  
-ATOM   3474  CG  ASN A 537      25.513 -10.657 -42.397  1.00 47.92           C  
-ATOM   3475  OD1 ASN A 537      25.557 -11.430 -41.438  1.00 52.83           O  
-ATOM   3476  ND2 ASN A 537      26.155 -10.891 -43.536  1.00 48.33           N  
-ATOM   3477  N   LEU A 538      21.185  -8.694 -41.420  1.00 25.62           N  
-ATOM   3478  CA  LEU A 538      20.401  -7.861 -40.515  1.00 28.35           C  
-ATOM   3479  C   LEU A 538      19.352  -8.682 -39.769  1.00 25.48           C  
-ATOM   3480  O   LEU A 538      19.043  -9.810 -40.152  1.00 25.03           O  
-ATOM   3481  CB  LEU A 538      19.724  -6.727 -41.288  1.00 27.55           C  
-ATOM   3482  CG  LEU A 538      20.645  -5.792 -42.073  1.00 18.63           C  
-ATOM   3483  CD1 LEU A 538      19.840  -4.885 -42.992  1.00 11.84           C  
-ATOM   3484  CD2 LEU A 538      21.500  -4.973 -41.121  1.00 22.55           C  
-ATOM   3485  N   LYS A 539      18.812  -8.108 -38.700  1.00 16.89           N  
-ATOM   3486  CA  LYS A 539      17.747  -8.750 -37.943  1.00 25.12           C  
-ATOM   3487  C   LYS A 539      16.388  -8.191 -38.353  1.00 30.56           C  
-ATOM   3488  O   LYS A 539      16.192  -6.977 -38.370  1.00 36.72           O  
-ATOM   3489  CB  LYS A 539      17.966  -8.558 -36.441  1.00 32.38           C  
-ATOM   3490  CG  LYS A 539      18.924  -9.555 -35.807  1.00 41.51           C  
-ATOM   3491  CD  LYS A 539      18.208 -10.825 -35.351  1.00 59.87           C  
-ATOM   3492  CE  LYS A 539      17.328 -10.582 -34.124  1.00 71.11           C  
-ATOM   3493  NZ  LYS A 539      15.975 -10.041 -34.457  1.00 50.80           N  
-ATOM   3494  N   PRO A 540      15.443  -9.077 -38.696  1.00 27.61           N  
-ATOM   3495  CA  PRO A 540      14.097  -8.610 -39.040  1.00 22.28           C  
-ATOM   3496  C   PRO A 540      13.371  -8.056 -37.824  1.00 23.94           C  
-ATOM   3497  O   PRO A 540      13.289  -8.733 -36.800  1.00 29.05           O  
-ATOM   3498  CB  PRO A 540      13.410  -9.872 -39.565  1.00 21.42           C  
-ATOM   3499  CG  PRO A 540      14.137 -10.995 -38.915  1.00 25.31           C  
-ATOM   3500  CD  PRO A 540      15.564 -10.541 -38.789  1.00 33.84           C  
-ATOM   3501  N   LYS A 541      12.855  -6.838 -37.935  1.00 24.48           N  
-ATOM   3502  CA  LYS A 541      12.202  -6.195 -36.804  1.00 22.62           C  
-ATOM   3503  C   LYS A 541      10.704  -6.019 -37.015  1.00 26.48           C  
-ATOM   3504  O   LYS A 541       9.902  -6.396 -36.157  1.00 28.10           O  
-ATOM   3505  CB  LYS A 541      12.831  -4.832 -36.524  1.00 20.15           C  
-ATOM   3506  CG  LYS A 541      12.206  -4.106 -35.342  1.00 31.23           C  
-ATOM   3507  CD  LYS A 541      13.177  -4.007 -34.179  1.00 35.75           C  
-ATOM   3508  CE  LYS A 541      12.451  -3.819 -32.859  1.00 42.31           C  
-ATOM   3509  NZ  LYS A 541      11.702  -5.048 -32.469  1.00 53.14           N  
-ATOM   3510  N   GLU A 542      10.322  -5.458 -38.158  1.00 25.51           N  
-ATOM   3511  CA  GLU A 542       8.953  -4.991 -38.320  1.00 24.58           C  
-ATOM   3512  C   GLU A 542       8.515  -4.845 -39.777  1.00 25.64           C  
-ATOM   3513  O   GLU A 542       9.250  -4.306 -40.604  1.00 23.36           O  
-ATOM   3514  CB  GLU A 542       8.807  -3.652 -37.604  1.00 18.52           C  
-ATOM   3515  CG  GLU A 542       7.427  -3.358 -37.078  1.00 23.77           C  
-ATOM   3516  CD  GLU A 542       7.398  -2.074 -36.281  1.00 39.01           C  
-ATOM   3517  OE1 GLU A 542       6.573  -1.965 -35.347  1.00 25.99           O  
-ATOM   3518  OE2 GLU A 542       8.206  -1.171 -36.592  1.00 42.18           O  
-ATOM   3519  N   PHE A 543       7.314  -5.329 -40.086  1.00 20.45           N  
-ATOM   3520  CA  PHE A 543       6.691  -5.039 -41.375  1.00 19.24           C  
-ATOM   3521  C   PHE A 543       5.529  -4.077 -41.178  1.00 20.91           C  
-ATOM   3522  O   PHE A 543       4.649  -4.318 -40.352  1.00 19.54           O  
-ATOM   3523  CB  PHE A 543       6.196  -6.308 -42.069  1.00 15.40           C  
-ATOM   3524  CG  PHE A 543       5.107  -6.049 -43.071  1.00 14.52           C  
-ATOM   3525  CD1 PHE A 543       5.381  -5.384 -44.254  1.00 15.68           C  
-ATOM   3526  CD2 PHE A 543       3.804  -6.449 -42.820  1.00 20.54           C  
-ATOM   3527  CE1 PHE A 543       4.375  -5.130 -45.173  1.00 21.03           C  
-ATOM   3528  CE2 PHE A 543       2.794  -6.199 -43.737  1.00 14.24           C  
-ATOM   3529  CZ  PHE A 543       3.081  -5.539 -44.913  1.00 13.20           C  
-ATOM   3530  N   ILE A 544       5.518  -2.994 -41.945  1.00 19.78           N  
-ATOM   3531  CA  ILE A 544       4.495  -1.972 -41.780  1.00 12.83           C  
-ATOM   3532  C   ILE A 544       3.591  -1.885 -43.004  1.00 16.55           C  
-ATOM   3533  O   ILE A 544       4.054  -1.722 -44.131  1.00 20.54           O  
-ATOM   3534  CB  ILE A 544       5.126  -0.605 -41.503  1.00 12.55           C  
-ATOM   3535  CG1 ILE A 544       6.151  -0.730 -40.373  1.00 16.85           C  
-ATOM   3536  CG2 ILE A 544       4.053   0.408 -41.152  1.00 14.06           C  
-ATOM   3537  CD1 ILE A 544       6.919   0.534 -40.088  1.00 18.61           C  
-ATOM   3538  N   HIS A 545       2.290  -1.997 -42.764  1.00 18.04           N  
-ATOM   3539  CA  HIS A 545       1.304  -2.049 -43.831  1.00 14.96           C  
-ATOM   3540  C   HIS A 545       0.512  -0.749 -43.965  1.00 15.25           C  
-ATOM   3541  O   HIS A 545      -0.317  -0.415 -43.109  1.00 21.70           O  
-ATOM   3542  CB  HIS A 545       0.350  -3.218 -43.597  1.00 15.56           C  
-ATOM   3543  CG  HIS A 545      -0.280  -3.737 -44.851  1.00 18.82           C  
-ATOM   3544  ND1 HIS A 545      -0.174  -3.079 -46.055  1.00 21.49           N  
-ATOM   3545  CD2 HIS A 545      -1.011  -4.850 -45.087  1.00 20.85           C  
-ATOM   3546  CE1 HIS A 545      -0.821  -3.764 -46.983  1.00 24.75           C  
-ATOM   3547  NE2 HIS A 545      -1.336  -4.841 -46.426  1.00 23.60           N  
-ATOM   3548  N   PHE A 546       0.789  -0.023 -45.046  1.00 13.07           N  
-ATOM   3549  CA  PHE A 546       0.064   1.197 -45.395  1.00 18.41           C  
-ATOM   3550  C   PHE A 546      -0.956   0.914 -46.492  1.00 22.92           C  
-ATOM   3551  O   PHE A 546      -0.606   0.427 -47.566  1.00 21.85           O  
-ATOM   3552  CB  PHE A 546       1.030   2.293 -45.851  1.00 20.10           C  
-ATOM   3553  CG  PHE A 546       1.715   3.007 -44.724  1.00 22.33           C  
-ATOM   3554  CD1 PHE A 546       1.406   2.713 -43.406  1.00 18.77           C  
-ATOM   3555  CD2 PHE A 546       2.658   3.986 -44.983  1.00 19.30           C  
-ATOM   3556  CE1 PHE A 546       2.033   3.372 -42.371  1.00 14.19           C  
-ATOM   3557  CE2 PHE A 546       3.287   4.650 -43.950  1.00 18.47           C  
-ATOM   3558  CZ  PHE A 546       2.974   4.342 -42.643  1.00 15.14           C  
-ATOM   3559  N   MET A 547      -2.216   1.235 -46.224  1.00 20.49           N  
-ATOM   3560  CA  MET A 547      -3.307   0.820 -47.096  1.00 17.29           C  
-ATOM   3561  C   MET A 547      -4.136   1.996 -47.607  1.00 17.68           C  
-ATOM   3562  O   MET A 547      -4.642   2.799 -46.827  1.00 14.65           O  
-ATOM   3563  CB  MET A 547      -4.203  -0.168 -46.352  1.00 16.44           C  
-ATOM   3564  CG  MET A 547      -3.443  -0.996 -45.328  1.00 24.38           C  
-ATOM   3565  SD  MET A 547      -4.453  -2.195 -44.449  1.00 30.12           S  
-ATOM   3566  CE  MET A 547      -4.877  -3.290 -45.794  1.00 23.83           C  
-ATOM   3567  N   GLY A 548      -4.271   2.090 -48.925  1.00 24.49           N  
-ATOM   3568  CA  GLY A 548      -5.062   3.141 -49.540  1.00 22.07           C  
-ATOM   3569  C   GLY A 548      -6.542   2.821 -49.521  1.00 20.32           C  
-ATOM   3570  O   GLY A 548      -7.193   2.936 -48.483  1.00 22.32           O  
-ATOM   3571  N   ASN A 549      -7.079   2.425 -50.671  1.00 15.52           N  
-ATOM   3572  CA  ASN A 549      -8.470   2.002 -50.745  1.00 16.20           C  
-ATOM   3573  C   ASN A 549      -8.634   0.644 -50.076  1.00 22.00           C  
-ATOM   3574  O   ASN A 549      -8.357  -0.391 -50.680  1.00 34.15           O  
-ATOM   3575  CB  ASN A 549      -8.947   1.943 -52.198  1.00 19.59           C  
-ATOM   3576  CG  ASN A 549     -10.460   1.854 -52.315  1.00 23.38           C  
-ATOM   3577  OD1 ASN A 549     -11.061   0.825 -52.007  1.00 28.80           O  
-ATOM   3578  ND2 ASN A 549     -11.082   2.932 -52.775  1.00 22.52           N  
-ATOM   3579  N   THR A 550      -9.072   0.657 -48.821  1.00 16.58           N  
-ATOM   3580  CA  THR A 550      -9.207  -0.566 -48.038  1.00 24.12           C  
-ATOM   3581  C   THR A 550     -10.668  -1.004 -47.988  1.00 24.64           C  
-ATOM   3582  O   THR A 550     -11.526  -0.275 -47.493  1.00 25.46           O  
-ATOM   3583  CB  THR A 550      -8.665  -0.369 -46.611  1.00 26.48           C  
-ATOM   3584  OG1 THR A 550      -7.420   0.336 -46.668  1.00 22.42           O  
-ATOM   3585  CG2 THR A 550      -8.443  -1.704 -45.934  1.00 29.12           C  
-ATOM   3586  N   HIS A 551     -10.948  -2.200 -48.494  1.00 23.70           N  
-ATOM   3587  CA  HIS A 551     -12.326  -2.608 -48.734  1.00 25.34           C  
-ATOM   3588  C   HIS A 551     -12.581  -4.093 -48.506  1.00 24.34           C  
-ATOM   3589  O   HIS A 551     -11.674  -4.917 -48.622  1.00 29.25           O  
-ATOM   3590  CB  HIS A 551     -12.718  -2.253 -50.167  1.00 21.80           C  
-ATOM   3591  CG  HIS A 551     -11.887  -2.946 -51.201  1.00 25.74           C  
-ATOM   3592  ND1 HIS A 551     -10.679  -2.449 -51.641  1.00 27.13           N  
-ATOM   3593  CD2 HIS A 551     -12.081  -4.108 -51.869  1.00 34.20           C  
-ATOM   3594  CE1 HIS A 551     -10.169  -3.271 -52.541  1.00 33.73           C  
-ATOM   3595  NE2 HIS A 551     -11.000  -4.285 -52.698  1.00 37.10           N  
-ATOM   3596  N   VAL A 552     -13.826  -4.425 -48.184  1.00 22.85           N  
-ATOM   3597  CA  VAL A 552     -14.271  -5.813 -48.187  1.00 35.62           C  
-ATOM   3598  C   VAL A 552     -15.399  -5.962 -49.210  1.00 40.24           C  
-ATOM   3599  O   VAL A 552     -16.186  -5.035 -49.424  1.00 33.00           O  
-ATOM   3600  CB  VAL A 552     -14.741  -6.283 -46.787  1.00 28.96           C  
-ATOM   3601  CG1 VAL A 552     -13.738  -5.862 -45.726  1.00 21.90           C  
-ATOM   3602  CG2 VAL A 552     -16.125  -5.742 -46.452  1.00 27.24           C  
-ATOM   3603  N   TYR A 553     -15.459  -7.114 -49.869  1.00 28.58           N  
-ATOM   3604  CA  TYR A 553     -16.507  -7.347 -50.851  1.00 32.38           C  
-ATOM   3605  C   TYR A 553     -17.773  -7.816 -50.154  1.00 36.19           C  
-ATOM   3606  O   TYR A 553     -17.713  -8.502 -49.136  1.00 41.20           O  
-ATOM   3607  CB  TYR A 553     -16.054  -8.356 -51.908  1.00 35.68           C  
-ATOM   3608  CG  TYR A 553     -15.079  -7.768 -52.902  1.00 43.36           C  
-ATOM   3609  CD1 TYR A 553     -15.518  -6.929 -53.918  1.00 41.66           C  
-ATOM   3610  CD2 TYR A 553     -13.720  -8.037 -52.816  1.00 47.65           C  
-ATOM   3611  CE1 TYR A 553     -14.633  -6.378 -54.824  1.00 47.22           C  
-ATOM   3612  CE2 TYR A 553     -12.825  -7.492 -53.719  1.00 51.55           C  
-ATOM   3613  CZ  TYR A 553     -13.287  -6.662 -54.720  1.00 52.43           C  
-ATOM   3614  OH  TYR A 553     -12.404  -6.117 -55.623  1.00 56.52           O  
-ATOM   3615  N   THR A 554     -18.918  -7.427 -50.702  1.00 43.71           N  
-ATOM   3616  CA  THR A 554     -20.204  -7.704 -50.076  1.00 41.95           C  
-ATOM   3617  C   THR A 554     -20.516  -9.197 -49.991  1.00 44.17           C  
-ATOM   3618  O   THR A 554     -21.277  -9.623 -49.123  1.00 41.45           O  
-ATOM   3619  CB  THR A 554     -21.348  -6.999 -50.822  1.00 44.82           C  
-ATOM   3620  OG1 THR A 554     -21.132  -7.106 -52.235  1.00 47.16           O  
-ATOM   3621  CG2 THR A 554     -21.409  -5.527 -50.435  1.00 35.38           C  
-ATOM   3622  N   ASN A 555     -19.927  -9.990 -50.882  1.00 42.17           N  
-ATOM   3623  CA  ASN A 555     -20.125 -11.436 -50.852  1.00 45.00           C  
-ATOM   3624  C   ASN A 555     -19.174 -12.128 -49.875  1.00 40.52           C  
-ATOM   3625  O   ASN A 555     -19.080 -13.356 -49.852  1.00 40.86           O  
-ATOM   3626  CB  ASN A 555     -19.960 -12.032 -52.254  1.00 46.08           C  
-ATOM   3627  CG  ASN A 555     -18.671 -11.601 -52.929  1.00 51.61           C  
-ATOM   3628  OD1 ASN A 555     -18.233 -10.462 -52.785  1.00 54.04           O  
-ATOM   3629  ND2 ASN A 555     -18.058 -12.515 -53.675  1.00 44.65           N  
-ATOM   3630  N   HIS A 556     -18.478 -11.331 -49.069  1.00 40.51           N  
-ATOM   3631  CA  HIS A 556     -17.544 -11.852 -48.074  1.00 36.98           C  
-ATOM   3632  C   HIS A 556     -18.002 -11.572 -46.650  1.00 42.14           C  
-ATOM   3633  O   HIS A 556     -17.512 -12.185 -45.706  1.00 43.62           O  
-ATOM   3634  CB  HIS A 556     -16.156 -11.245 -48.271  1.00 28.88           C  
-ATOM   3635  CG  HIS A 556     -15.492 -11.653 -49.545  1.00 35.61           C  
-ATOM   3636  ND1 HIS A 556     -14.309 -11.093 -49.978  1.00 53.58           N  
-ATOM   3637  CD2 HIS A 556     -15.840 -12.567 -50.481  1.00 46.57           C  
-ATOM   3638  CE1 HIS A 556     -13.959 -11.643 -51.127  1.00 57.56           C  
-ATOM   3639  NE2 HIS A 556     -14.870 -12.541 -51.454  1.00 59.71           N  
-ATOM   3640  N   VAL A 557     -18.937 -10.638 -46.511  1.00 33.02           N  
-ATOM   3641  CA  VAL A 557     -19.304 -10.077 -45.212  1.00 34.94           C  
-ATOM   3642  C   VAL A 557     -19.758 -11.125 -44.200  1.00 43.11           C  
-ATOM   3643  O   VAL A 557     -19.369 -11.074 -43.031  1.00 44.47           O  
-ATOM   3644  CB  VAL A 557     -20.420  -9.029 -45.361  1.00 46.13           C  
-ATOM   3645  CG1 VAL A 557     -20.725  -8.390 -44.021  1.00 29.81           C  
-ATOM   3646  CG2 VAL A 557     -20.013  -7.978 -46.379  1.00 49.07           C  
-ATOM   3647  N  AGLU A 558     -20.580 -12.062 -44.659  0.47 46.62           N  
-ATOM   3648  N  BGLU A 558     -20.594 -12.062 -44.644  0.53 46.26           N  
-ATOM   3649  CA AGLU A 558     -21.072 -13.145 -43.819  0.47 43.94           C  
-ATOM   3650  CA BGLU A 558     -21.073 -13.138 -43.778  0.53 44.62           C  
-ATOM   3651  C  AGLU A 558     -19.919 -13.991 -43.291  0.47 43.78           C  
-ATOM   3652  C  BGLU A 558     -19.914 -13.999 -43.282  0.53 44.28           C  
-ATOM   3653  O  AGLU A 558     -19.839 -14.285 -42.095  0.47 39.25           O  
-ATOM   3654  O  BGLU A 558     -19.824 -14.317 -42.094  0.53 39.59           O  
-ATOM   3655  CB AGLU A 558     -22.052 -14.022 -44.604  0.47 44.67           C  
-ATOM   3656  CB BGLU A 558     -22.095 -14.011 -44.510  0.53 44.61           C  
-ATOM   3657  CG AGLU A 558     -23.136 -13.248 -45.343  0.47 46.77           C  
-ATOM   3658  CG BGLU A 558     -22.578 -15.209 -43.689  0.53 48.16           C  
-ATOM   3659  CD AGLU A 558     -22.780 -12.964 -46.793  0.47 46.23           C  
-ATOM   3660  CD BGLU A 558     -23.386 -16.196 -44.510  0.53 47.50           C  
-ATOM   3661  OE1AGLU A 558     -21.852 -12.163 -47.045  0.47 37.89           O  
-ATOM   3662  OE1BGLU A 558     -23.873 -15.801 -45.590  0.53 46.46           O  
-ATOM   3663  OE2AGLU A 558     -23.435 -13.547 -47.683  0.47 42.28           O  
-ATOM   3664  OE2BGLU A 558     -23.530 -17.362 -44.082  0.53 40.22           O  
-ATOM   3665  N   ALA A 559     -19.030 -14.371 -44.203  1.00 40.91           N  
-ATOM   3666  CA  ALA A 559     -17.878 -15.196 -43.876  1.00 42.49           C  
-ATOM   3667  C   ALA A 559     -16.925 -14.490 -42.919  1.00 43.38           C  
-ATOM   3668  O   ALA A 559     -16.340 -15.119 -42.045  1.00 47.21           O  
-ATOM   3669  CB  ALA A 559     -17.150 -15.595 -45.150  1.00 42.42           C  
-ATOM   3670  N   LEU A 560     -16.772 -13.182 -43.087  1.00 41.57           N  
-ATOM   3671  CA  LEU A 560     -15.900 -12.406 -42.217  1.00 36.41           C  
-ATOM   3672  C   LEU A 560     -16.514 -12.296 -40.834  1.00 31.27           C  
-ATOM   3673  O   LEU A 560     -15.814 -12.373 -39.826  1.00 31.72           O  
-ATOM   3674  CB  LEU A 560     -15.646 -11.020 -42.810  1.00 33.11           C  
-ATOM   3675  CG  LEU A 560     -14.948 -11.040 -44.174  1.00 31.94           C  
-ATOM   3676  CD1 LEU A 560     -14.712  -9.632 -44.703  1.00 31.66           C  
-ATOM   3677  CD2 LEU A 560     -13.647 -11.823 -44.097  1.00 27.60           C  
-ATOM   3678  N   LYS A 561     -17.829 -12.111 -40.805  1.00 30.60           N  
-ATOM   3679  CA  LYS A 561     -18.589 -12.131 -39.563  1.00 35.83           C  
-ATOM   3680  C   LYS A 561     -18.368 -13.452 -38.840  1.00 44.48           C  
-ATOM   3681  O   LYS A 561     -18.239 -13.485 -37.614  1.00 33.99           O  
-ATOM   3682  CB  LYS A 561     -20.080 -11.921 -39.835  1.00 47.23           C  
-ATOM   3683  CG  LYS A 561     -20.477 -10.486 -40.128  1.00 38.96           C  
-ATOM   3684  CD  LYS A 561     -21.901 -10.416 -40.666  1.00 44.63           C  
-ATOM   3685  CE  LYS A 561     -22.388  -8.978 -40.760  1.00 53.58           C  
-ATOM   3686  NZ  LYS A 561     -22.491  -8.348 -39.414  1.00 54.59           N  
-ATOM   3687  N   GLU A 562     -18.340 -14.538 -39.609  1.00 51.02           N  
-ATOM   3688  CA  GLU A 562     -18.024 -15.851 -39.064  1.00 43.63           C  
-ATOM   3689  C   GLU A 562     -16.607 -15.851 -38.490  1.00 39.51           C  
-ATOM   3690  O   GLU A 562     -16.372 -16.328 -37.382  1.00 34.17           O  
-ATOM   3691  CB  GLU A 562     -18.168 -16.932 -40.141  1.00 39.16           C  
-ATOM   3692  CG  GLU A 562     -19.602 -17.376 -40.427  1.00 58.61           C  
-ATOM   3693  CD  GLU A 562     -20.020 -18.590 -39.611  1.00 67.75           C  
-ATOM   3694  OE1 GLU A 562     -20.182 -18.456 -38.378  1.00 65.24           O  
-ATOM   3695  OE2 GLU A 562     -20.185 -19.679 -40.205  1.00 59.71           O  
-ATOM   3696  N   GLN A 563     -15.676 -15.283 -39.252  1.00 35.92           N  
-ATOM   3697  CA  GLN A 563     -14.257 -15.277 -38.919  1.00 35.27           C  
-ATOM   3698  C   GLN A 563     -13.966 -14.496 -37.638  1.00 30.94           C  
-ATOM   3699  O   GLN A 563     -13.020 -14.805 -36.915  1.00 24.39           O  
-ATOM   3700  CB  GLN A 563     -13.454 -14.697 -40.094  1.00 26.31           C  
-ATOM   3701  CG  GLN A 563     -11.938 -14.862 -40.000  1.00 13.41           C  
-ATOM   3702  CD  GLN A 563     -11.232 -14.529 -41.309  1.00 22.58           C  
-ATOM   3703  OE1 GLN A 563     -11.863 -14.435 -42.363  1.00 40.91           O  
-ATOM   3704  NE2 GLN A 563      -9.920 -14.353 -41.247  1.00 17.62           N  
-ATOM   3705  N   LEU A 564     -14.785 -13.490 -37.355  1.00 29.57           N  
-ATOM   3706  CA  LEU A 564     -14.545 -12.634 -36.202  1.00 25.91           C  
-ATOM   3707  C   LEU A 564     -14.937 -13.299 -34.887  1.00 29.38           C  
-ATOM   3708  O   LEU A 564     -14.639 -12.780 -33.813  1.00 30.44           O  
-ATOM   3709  CB  LEU A 564     -15.296 -11.311 -36.355  1.00 33.97           C  
-ATOM   3710  CG  LEU A 564     -14.846 -10.397 -37.497  1.00 33.26           C  
-ATOM   3711  CD1 LEU A 564     -15.572  -9.059 -37.437  1.00 33.77           C  
-ATOM   3712  CD2 LEU A 564     -13.340 -10.197 -37.475  1.00 35.28           C  
-ATOM   3713  N   ARG A 565     -15.610 -14.442 -34.965  1.00 37.84           N  
-ATOM   3714  CA  ARG A 565     -15.978 -15.173 -33.757  1.00 39.71           C  
-ATOM   3715  C   ARG A 565     -14.813 -16.023 -33.263  1.00 28.03           C  
-ATOM   3716  O   ARG A 565     -14.840 -16.550 -32.152  1.00 20.68           O  
-ATOM   3717  CB  ARG A 565     -17.210 -16.047 -34.008  1.00 39.55           C  
-ATOM   3718  CG  ARG A 565     -18.528 -15.334 -33.750  1.00 39.97           C  
-ATOM   3719  CD  ARG A 565     -19.725 -16.183 -34.152  1.00 46.22           C  
-ATOM   3720  NE  ARG A 565     -20.152 -15.907 -35.522  1.00 70.34           N  
-ATOM   3721  CZ  ARG A 565     -21.037 -14.971 -35.855  1.00 70.37           C  
-ATOM   3722  NH1 ARG A 565     -21.594 -14.217 -34.915  1.00 54.11           N  
-ATOM   3723  NH2 ARG A 565     -21.368 -14.787 -37.127  1.00 52.29           N  
-ATOM   3724  N   ARG A 566     -13.788 -16.141 -34.100  1.00 28.81           N  
-ATOM   3725  CA  ARG A 566     -12.612 -16.939 -33.782  1.00 21.67           C  
-ATOM   3726  C   ARG A 566     -11.534 -16.094 -33.115  1.00 24.35           C  
-ATOM   3727  O   ARG A 566     -11.149 -15.048 -33.637  1.00 37.42           O  
-ATOM   3728  CB  ARG A 566     -12.045 -17.585 -35.049  1.00 18.69           C  
-ATOM   3729  CG  ARG A 566     -13.057 -18.344 -35.893  1.00 19.82           C  
-ATOM   3730  CD  ARG A 566     -12.428 -18.812 -37.197  1.00 20.66           C  
-ATOM   3731  NE  ARG A 566     -13.300 -19.702 -37.959  1.00 24.01           N  
-ATOM   3732  CZ  ARG A 566     -12.964 -20.257 -39.119  1.00 27.11           C  
-ATOM   3733  NH1 ARG A 566     -13.812 -21.057 -39.750  1.00 29.45           N  
-ATOM   3734  NH2 ARG A 566     -11.776 -20.012 -39.650  1.00 36.47           N  
-ATOM   3735  N   GLU A 567     -11.046 -16.544 -31.965  1.00 20.67           N  
-ATOM   3736  CA  GLU A 567      -9.891 -15.906 -31.344  1.00 29.43           C  
-ATOM   3737  C   GLU A 567      -8.608 -16.464 -31.958  1.00 24.96           C  
-ATOM   3738  O   GLU A 567      -8.513 -17.662 -32.220  1.00 26.44           O  
-ATOM   3739  CB  GLU A 567      -9.897 -16.106 -29.827  1.00 25.25           C  
-ATOM   3740  CG  GLU A 567     -10.221 -17.517 -29.389  1.00 30.67           C  
-ATOM   3741  CD  GLU A 567     -11.704 -17.738 -29.205  1.00 35.68           C  
-ATOM   3742  OE1 GLU A 567     -12.355 -16.877 -28.578  1.00 37.08           O  
-ATOM   3743  OE2 GLU A 567     -12.219 -18.765 -29.692  1.00 52.39           O  
-ATOM   3744  N   PRO A 568      -7.618 -15.590 -32.195  1.00 20.71           N  
-ATOM   3745  CA  PRO A 568      -6.388 -15.972 -32.896  1.00 20.27           C  
-ATOM   3746  C   PRO A 568      -5.499 -16.928 -32.109  1.00 18.59           C  
-ATOM   3747  O   PRO A 568      -5.609 -17.031 -30.888  1.00 18.10           O  
-ATOM   3748  CB  PRO A 568      -5.678 -14.632 -33.102  1.00 18.35           C  
-ATOM   3749  CG  PRO A 568      -6.170 -13.782 -31.989  1.00 22.45           C  
-ATOM   3750  CD  PRO A 568      -7.605 -14.171 -31.801  1.00 20.25           C  
-ATOM   3751  N   ARG A 569      -4.622 -17.618 -32.830  1.00 19.53           N  
-ATOM   3752  CA  ARG A 569      -3.677 -18.554 -32.237  1.00 17.66           C  
-ATOM   3753  C   ARG A 569      -2.268 -17.966 -32.306  1.00 18.97           C  
-ATOM   3754  O   ARG A 569      -2.043 -16.998 -33.036  1.00 24.79           O  
-ATOM   3755  CB  ARG A 569      -3.751 -19.903 -32.958  1.00 17.66           C  
-ATOM   3756  CG  ARG A 569      -5.144 -20.506 -32.970  1.00 21.24           C  
-ATOM   3757  CD  ARG A 569      -5.192 -21.844 -32.249  1.00 18.00           C  
-ATOM   3758  NE  ARG A 569      -6.556 -22.361 -32.171  1.00 24.29           N  
-ATOM   3759  CZ  ARG A 569      -7.159 -23.037 -33.146  1.00 21.81           C  
-ATOM   3760  NH1 ARG A 569      -8.402 -23.468 -32.987  1.00 17.06           N  
-ATOM   3761  NH2 ARG A 569      -6.521 -23.282 -34.283  1.00 17.97           N  
-ATOM   3762  N   PRO A 570      -1.319 -18.527 -31.534  1.00 16.71           N  
-ATOM   3763  CA  PRO A 570       0.062 -18.036 -31.606  1.00 16.84           C  
-ATOM   3764  C   PRO A 570       0.629 -18.035 -33.025  1.00 15.55           C  
-ATOM   3765  O   PRO A 570       0.482 -19.015 -33.758  1.00 18.02           O  
-ATOM   3766  CB  PRO A 570       0.837 -19.017 -30.709  1.00 10.88           C  
-ATOM   3767  CG  PRO A 570      -0.112 -20.133 -30.398  1.00 11.23           C  
-ATOM   3768  CD  PRO A 570      -1.474 -19.531 -30.469  1.00 14.53           C  
-ATOM   3769  N   PHE A 571       1.250 -16.923 -33.405  1.00 12.84           N  
-ATOM   3770  CA  PHE A 571       1.920 -16.819 -34.691  1.00 10.81           C  
-ATOM   3771  C   PHE A 571       3.003 -17.881 -34.790  1.00 13.50           C  
-ATOM   3772  O   PHE A 571       3.651 -18.199 -33.796  1.00 18.98           O  
-ATOM   3773  CB  PHE A 571       2.525 -15.426 -34.880  1.00 17.86           C  
-ATOM   3774  CG  PHE A 571       1.549 -14.400 -35.381  1.00 20.94           C  
-ATOM   3775  CD1 PHE A 571       0.480 -14.772 -36.180  1.00 17.81           C  
-ATOM   3776  CD2 PHE A 571       1.704 -13.059 -35.057  1.00 21.86           C  
-ATOM   3777  CE1 PHE A 571      -0.420 -13.829 -36.645  1.00 20.79           C  
-ATOM   3778  CE2 PHE A 571       0.810 -12.110 -35.520  1.00 21.77           C  
-ATOM   3779  CZ  PHE A 571      -0.255 -12.496 -36.315  1.00 20.58           C  
-ATOM   3780  N   PRO A 572       3.191 -18.451 -35.987  1.00 14.70           N  
-ATOM   3781  CA  PRO A 572       4.249 -19.444 -36.180  1.00 18.31           C  
-ATOM   3782  C   PRO A 572       5.618 -18.792 -36.358  1.00 19.35           C  
-ATOM   3783  O   PRO A 572       5.730 -17.568 -36.324  1.00 15.67           O  
-ATOM   3784  CB  PRO A 572       3.818 -20.159 -37.459  1.00 17.53           C  
-ATOM   3785  CG  PRO A 572       3.119 -19.094 -38.237  1.00 14.75           C  
-ATOM   3786  CD  PRO A 572       2.404 -18.245 -37.216  1.00 18.24           C  
-ATOM   3787  N   ILE A 573       6.645 -19.613 -36.538  1.00 19.84           N  
-ATOM   3788  CA  ILE A 573       7.989 -19.126 -36.814  1.00 19.24           C  
-ATOM   3789  C   ILE A 573       8.419 -19.584 -38.197  1.00 18.66           C  
-ATOM   3790  O   ILE A 573       8.311 -20.763 -38.520  1.00 19.70           O  
-ATOM   3791  CB  ILE A 573       9.009 -19.627 -35.769  1.00 18.23           C  
-ATOM   3792  CG1 ILE A 573       8.938 -18.782 -34.497  1.00 18.86           C  
-ATOM   3793  CG2 ILE A 573      10.419 -19.583 -36.329  1.00 16.42           C  
-ATOM   3794  CD1 ILE A 573       9.885 -19.246 -33.413  1.00 11.18           C  
-ATOM   3795  N   VAL A 574       8.896 -18.654 -39.019  1.00 22.63           N  
-ATOM   3796  CA  VAL A 574       9.399 -19.014 -40.339  1.00 22.67           C  
-ATOM   3797  C   VAL A 574      10.921 -19.060 -40.337  1.00 19.36           C  
-ATOM   3798  O   VAL A 574      11.585 -18.027 -40.273  1.00 28.27           O  
-ATOM   3799  CB  VAL A 574       8.915 -18.036 -41.423  1.00 19.42           C  
-ATOM   3800  CG1 VAL A 574       9.614 -18.325 -42.742  1.00 22.21           C  
-ATOM   3801  CG2 VAL A 574       7.408 -18.139 -41.587  1.00 15.46           C  
-ATOM   3802  N   ASN A 575      11.467 -20.271 -40.396  1.00 20.39           N  
-ATOM   3803  CA  ASN A 575      12.908 -20.463 -40.386  1.00 15.98           C  
-ATOM   3804  C   ASN A 575      13.476 -20.566 -41.792  1.00 21.34           C  
-ATOM   3805  O   ASN A 575      12.910 -21.235 -42.661  1.00 20.27           O  
-ATOM   3806  CB  ASN A 575      13.281 -21.717 -39.589  1.00 20.27           C  
-ATOM   3807  CG  ASN A 575      13.082 -21.543 -38.096  1.00 23.63           C  
-ATOM   3808  OD1 ASN A 575      12.634 -22.460 -37.409  1.00 28.26           O  
-ATOM   3809  ND2 ASN A 575      13.414 -20.361 -37.587  1.00 16.98           N  
-ATOM   3810  N   ILE A 576      14.598 -19.889 -42.009  1.00 26.32           N  
-ATOM   3811  CA  ILE A 576      15.332 -20.016 -43.256  1.00 20.08           C  
-ATOM   3812  C   ILE A 576      16.343 -21.145 -43.129  1.00 19.58           C  
-ATOM   3813  O   ILE A 576      17.244 -21.097 -42.293  1.00 20.20           O  
-ATOM   3814  CB  ILE A 576      16.064 -18.719 -43.642  1.00 14.95           C  
-ATOM   3815  CG1 ILE A 576      15.062 -17.591 -43.885  1.00 19.03           C  
-ATOM   3816  CG2 ILE A 576      16.908 -18.947 -44.885  1.00 20.95           C  
-ATOM   3817  CD1 ILE A 576      15.701 -16.297 -44.346  1.00 18.07           C  
-ATOM   3818  N   LEU A 577      16.181 -22.166 -43.959  1.00 18.99           N  
-ATOM   3819  CA  LEU A 577      17.086 -23.302 -43.945  1.00 19.81           C  
-ATOM   3820  C   LEU A 577      18.255 -23.045 -44.889  1.00 29.47           C  
-ATOM   3821  O   LEU A 577      18.140 -22.242 -45.816  1.00 31.46           O  
-ATOM   3822  CB  LEU A 577      16.349 -24.579 -44.348  1.00 24.78           C  
-ATOM   3823  CG  LEU A 577      14.944 -24.760 -43.772  1.00 18.64           C  
-ATOM   3824  CD1 LEU A 577      14.260 -25.974 -44.379  1.00 19.48           C  
-ATOM   3825  CD2 LEU A 577      15.003 -24.877 -42.262  1.00 20.87           C  
-ATOM   3826  N   ASN A 578      19.374 -23.724 -44.640  1.00 32.79           N  
-ATOM   3827  CA  ASN A 578      20.552 -23.658 -45.507  1.00 28.10           C  
-ATOM   3828  C   ASN A 578      21.128 -22.252 -45.659  1.00 32.13           C  
-ATOM   3829  O   ASN A 578      21.567 -21.861 -46.744  1.00 28.07           O  
-ATOM   3830  CB  ASN A 578      20.216 -24.217 -46.887  1.00 21.15           C  
-ATOM   3831  CG  ASN A 578      19.319 -25.432 -46.818  1.00 19.07           C  
-ATOM   3832  OD1 ASN A 578      19.428 -26.252 -45.905  1.00 26.74           O  
-ATOM   3833  ND2 ASN A 578      18.417 -25.550 -47.781  1.00 19.65           N  
-ATOM   3834  N   LYS A 579      21.135 -21.503 -44.561  1.00 32.70           N  
-ATOM   3835  CA  LYS A 579      21.625 -20.131 -44.566  1.00 28.31           C  
-ATOM   3836  C   LYS A 579      23.022 -20.007 -45.163  1.00 29.04           C  
-ATOM   3837  O   LYS A 579      23.292 -19.080 -45.925  1.00 31.36           O  
-ATOM   3838  CB  LYS A 579      21.619 -19.563 -43.148  1.00 34.82           C  
-ATOM   3839  CG  LYS A 579      20.236 -19.433 -42.541  1.00 30.74           C  
-ATOM   3840  CD  LYS A 579      20.205 -18.322 -41.504  1.00 28.49           C  
-ATOM   3841  CE  LYS A 579      18.784 -17.853 -41.259  1.00 20.66           C  
-ATOM   3842  NZ  LYS A 579      18.760 -16.586 -40.486  1.00 34.62           N  
-ATOM   3843  N   GLU A 580      23.897 -20.949 -44.814  1.00 34.86           N  
-ATOM   3844  CA  GLU A 580      25.281 -20.952 -45.282  1.00 30.04           C  
-ATOM   3845  C   GLU A 580      25.361 -20.947 -46.804  1.00 30.73           C  
-ATOM   3846  O   GLU A 580      26.294 -20.391 -47.380  1.00 35.35           O  
-ATOM   3847  CB  GLU A 580      26.037 -22.165 -44.725  1.00 32.56           C  
-ATOM   3848  CG  GLU A 580      25.366 -22.833 -43.531  1.00 44.32           C  
-ATOM   3849  CD  GLU A 580      24.284 -23.824 -43.942  1.00 58.20           C  
-ATOM   3850  OE1 GLU A 580      24.341 -24.338 -45.081  1.00 47.75           O  
-ATOM   3851  OE2 GLU A 580      23.375 -24.087 -43.125  1.00 52.75           O  
-ATOM   3852  N   ARG A 581      24.375 -21.560 -47.451  1.00 32.33           N  
-ATOM   3853  CA  ARG A 581      24.357 -21.635 -48.907  1.00 25.73           C  
-ATOM   3854  C   ARG A 581      23.845 -20.339 -49.515  1.00 22.50           C  
-ATOM   3855  O   ARG A 581      24.194 -19.987 -50.642  1.00 28.59           O  
-ATOM   3856  CB  ARG A 581      23.491 -22.806 -49.382  1.00 19.73           C  
-ATOM   3857  CG  ARG A 581      23.797 -23.262 -50.794  1.00 16.20           C  
-ATOM   3858  CD  ARG A 581      22.679 -24.106 -51.378  1.00 22.11           C  
-ATOM   3859  NE  ARG A 581      21.544 -23.292 -51.806  1.00 29.93           N  
-ATOM   3860  CZ  ARG A 581      20.337 -23.330 -51.251  1.00 22.94           C  
-ATOM   3861  NH1 ARG A 581      19.368 -22.550 -51.714  1.00 19.80           N  
-ATOM   3862  NH2 ARG A 581      20.095 -24.148 -50.236  1.00 29.90           N  
-ATOM   3863  N   ILE A 582      23.018 -19.629 -48.758  1.00 21.25           N  
-ATOM   3864  CA  ILE A 582      22.311 -18.470 -49.283  1.00 22.80           C  
-ATOM   3865  C   ILE A 582      23.042 -17.168 -48.982  1.00 30.71           C  
-ATOM   3866  O   ILE A 582      23.122 -16.741 -47.829  1.00 31.83           O  
-ATOM   3867  CB  ILE A 582      20.881 -18.404 -48.717  1.00 21.22           C  
-ATOM   3868  CG1 ILE A 582      20.126 -19.691 -49.065  1.00 25.49           C  
-ATOM   3869  CG2 ILE A 582      20.155 -17.177 -49.244  1.00 18.71           C  
-ATOM   3870  CD1 ILE A 582      18.789 -19.831 -48.380  1.00 25.58           C  
-ATOM   3871  N   LYS A 583      23.578 -16.544 -50.028  1.00 28.09           N  
-ATOM   3872  CA  LYS A 583      24.343 -15.312 -49.882  1.00 18.67           C  
-ATOM   3873  C   LYS A 583      23.699 -14.154 -50.635  1.00 23.20           C  
-ATOM   3874  O   LYS A 583      23.904 -12.988 -50.292  1.00 23.49           O  
-ATOM   3875  CB  LYS A 583      25.775 -15.521 -50.368  1.00 20.32           C  
-ATOM   3876  CG  LYS A 583      26.620 -16.367 -49.435  1.00 31.33           C  
-ATOM   3877  CD  LYS A 583      27.818 -16.963 -50.154  1.00 40.83           C  
-ATOM   3878  CE  LYS A 583      28.879 -17.387 -49.157  1.00 61.22           C  
-ATOM   3879  NZ  LYS A 583      28.271 -17.959 -47.922  1.00 48.80           N  
-ATOM   3880  N   GLU A 584      22.923 -14.477 -51.664  1.00 27.31           N  
-ATOM   3881  CA  GLU A 584      22.249 -13.455 -52.456  1.00 30.67           C  
-ATOM   3882  C   GLU A 584      20.748 -13.721 -52.553  1.00 26.31           C  
-ATOM   3883  O   GLU A 584      20.292 -14.846 -52.346  1.00 24.02           O  
-ATOM   3884  CB  GLU A 584      22.867 -13.374 -53.855  1.00 32.75           C  
-ATOM   3885  CG  GLU A 584      24.388 -13.214 -53.866  1.00 32.62           C  
-ATOM   3886  CD  GLU A 584      24.856 -11.822 -53.459  1.00 33.91           C  
-ATOM   3887  OE1 GLU A 584      24.008 -10.965 -53.129  1.00 32.81           O  
-ATOM   3888  OE2 GLU A 584      26.083 -11.584 -53.476  1.00 32.53           O  
-ATOM   3889  N   ILE A 585      19.990 -12.678 -52.878  1.00 29.19           N  
-ATOM   3890  CA  ILE A 585      18.532 -12.755 -52.887  1.00 24.44           C  
-ATOM   3891  C   ILE A 585      18.011 -13.794 -53.881  1.00 24.38           C  
-ATOM   3892  O   ILE A 585      16.955 -14.392 -53.672  1.00 23.41           O  
-ATOM   3893  CB  ILE A 585      17.907 -11.375 -53.207  1.00 21.78           C  
-ATOM   3894  CG1 ILE A 585      16.382 -11.416 -53.056  1.00 20.06           C  
-ATOM   3895  CG2 ILE A 585      18.323 -10.895 -54.595  1.00 24.78           C  
-ATOM   3896  CD1 ILE A 585      15.918 -11.779 -51.660  1.00 18.23           C  
-ATOM   3897  N   ASP A 586      18.769 -14.027 -54.947  1.00 22.84           N  
-ATOM   3898  CA  ASP A 586      18.357 -14.973 -55.975  1.00 20.63           C  
-ATOM   3899  C   ASP A 586      18.682 -16.412 -55.592  1.00 28.94           C  
-ATOM   3900  O   ASP A 586      18.229 -17.350 -56.247  1.00 33.73           O  
-ATOM   3901  CB  ASP A 586      19.018 -14.626 -57.309  1.00 22.90           C  
-ATOM   3902  CG  ASP A 586      18.627 -13.253 -57.811  1.00 32.81           C  
-ATOM   3903  OD1 ASP A 586      17.483 -13.102 -58.292  1.00 36.16           O  
-ATOM   3904  OD2 ASP A 586      19.464 -12.328 -57.729  1.00 28.58           O  
-ATOM   3905  N   ASP A 587      19.460 -16.584 -54.526  1.00 30.41           N  
-ATOM   3906  CA  ASP A 587      19.896 -17.916 -54.108  1.00 32.17           C  
-ATOM   3907  C   ASP A 587      18.779 -18.730 -53.452  1.00 32.67           C  
-ATOM   3908  O   ASP A 587      18.887 -19.950 -53.324  1.00 30.59           O  
-ATOM   3909  CB  ASP A 587      21.088 -17.809 -53.151  1.00 24.18           C  
-ATOM   3910  CG  ASP A 587      22.368 -17.402 -53.858  1.00 35.67           C  
-ATOM   3911  OD1 ASP A 587      22.285 -16.900 -55.000  1.00 43.69           O  
-ATOM   3912  OD2 ASP A 587      23.458 -17.583 -53.275  1.00 30.72           O  
-ATOM   3913  N   PHE A 588      17.709 -18.055 -53.042  1.00 27.73           N  
-ATOM   3914  CA  PHE A 588      16.590 -18.718 -52.381  1.00 23.12           C  
-ATOM   3915  C   PHE A 588      15.836 -19.669 -53.305  1.00 23.97           C  
-ATOM   3916  O   PHE A 588      15.656 -19.391 -54.489  1.00 24.11           O  
-ATOM   3917  CB  PHE A 588      15.616 -17.683 -51.821  1.00 23.91           C  
-ATOM   3918  CG  PHE A 588      16.092 -17.014 -50.565  1.00 23.11           C  
-ATOM   3919  CD1 PHE A 588      15.874 -17.600 -49.330  1.00 17.99           C  
-ATOM   3920  CD2 PHE A 588      16.747 -15.794 -50.617  1.00 19.52           C  
-ATOM   3921  CE1 PHE A 588      16.305 -16.986 -48.169  1.00 15.47           C  
-ATOM   3922  CE2 PHE A 588      17.178 -15.175 -49.460  1.00 18.46           C  
-ATOM   3923  CZ  PHE A 588      16.958 -15.773 -48.234  1.00 14.07           C  
-ATOM   3924  N   THR A 589      15.399 -20.796 -52.753  1.00 24.69           N  
-ATOM   3925  CA  THR A 589      14.521 -21.710 -53.475  1.00 22.39           C  
-ATOM   3926  C   THR A 589      13.291 -22.015 -52.628  1.00 28.89           C  
-ATOM   3927  O   THR A 589      13.155 -21.508 -51.512  1.00 30.11           O  
-ATOM   3928  CB  THR A 589      15.222 -23.024 -53.838  1.00 21.01           C  
-ATOM   3929  OG1 THR A 589      15.394 -23.813 -52.657  1.00 27.11           O  
-ATOM   3930  CG2 THR A 589      16.579 -22.751 -54.469  1.00 27.83           C  
-ATOM   3931  N   ALA A 590      12.403 -22.852 -53.155  1.00 21.20           N  
-ATOM   3932  CA  ALA A 590      11.141 -23.146 -52.487  1.00 18.91           C  
-ATOM   3933  C   ALA A 590      11.328 -24.025 -51.250  1.00 28.61           C  
-ATOM   3934  O   ALA A 590      10.491 -24.025 -50.347  1.00 28.07           O  
-ATOM   3935  CB  ALA A 590      10.181 -23.806 -53.458  1.00 23.86           C  
-ATOM   3936  N   GLU A 591      12.431 -24.767 -51.209  1.00 31.17           N  
-ATOM   3937  CA  GLU A 591      12.678 -25.707 -50.119  1.00 26.89           C  
-ATOM   3938  C   GLU A 591      13.588 -25.139 -49.042  1.00 22.45           C  
-ATOM   3939  O   GLU A 591      14.044 -25.865 -48.159  1.00 26.22           O  
-ATOM   3940  CB  GLU A 591      13.284 -27.003 -50.662  1.00 27.79           C  
-ATOM   3941  CG  GLU A 591      12.290 -27.906 -51.367  1.00 36.11           C  
-ATOM   3942  CD  GLU A 591      11.871 -27.365 -52.715  1.00 43.86           C  
-ATOM   3943  OE1 GLU A 591      10.759 -27.706 -53.173  1.00 43.89           O  
-ATOM   3944  OE2 GLU A 591      12.658 -26.600 -53.315  1.00 38.87           O  
-ATOM   3945  N   ASP A 592      13.852 -23.841 -49.111  1.00 21.62           N  
-ATOM   3946  CA  ASP A 592      14.773 -23.217 -48.173  1.00 25.64           C  
-ATOM   3947  C   ASP A 592      14.042 -22.579 -47.000  1.00 25.24           C  
-ATOM   3948  O   ASP A 592      14.606 -21.753 -46.280  1.00 22.20           O  
-ATOM   3949  CB  ASP A 592      15.630 -22.174 -48.890  1.00 27.76           C  
-ATOM   3950  CG  ASP A 592      16.557 -22.793 -49.914  1.00 28.40           C  
-ATOM   3951  OD1 ASP A 592      17.180 -23.831 -49.602  1.00 23.51           O  
-ATOM   3952  OD2 ASP A 592      16.658 -22.246 -51.032  1.00 30.73           O  
-ATOM   3953  N   PHE A 593      12.788 -22.971 -46.803  1.00 30.56           N  
-ATOM   3954  CA  PHE A 593      11.975 -22.387 -45.742  1.00 29.21           C  
-ATOM   3955  C   PHE A 593      11.290 -23.446 -44.890  1.00 21.78           C  
-ATOM   3956  O   PHE A 593      11.160 -24.602 -45.296  1.00 20.39           O  
-ATOM   3957  CB  PHE A 593      10.936 -21.437 -46.336  1.00 23.62           C  
-ATOM   3958  CG  PHE A 593      11.537 -20.245 -47.014  1.00 15.51           C  
-ATOM   3959  CD1 PHE A 593      11.898 -20.300 -48.350  1.00 15.25           C  
-ATOM   3960  CD2 PHE A 593      11.760 -19.075 -46.312  1.00 17.25           C  
-ATOM   3961  CE1 PHE A 593      12.462 -19.205 -48.973  1.00 21.20           C  
-ATOM   3962  CE2 PHE A 593      12.323 -17.975 -46.930  1.00 20.32           C  
-ATOM   3963  CZ  PHE A 593      12.673 -18.039 -48.262  1.00 18.33           C  
-ATOM   3964  N   GLU A 594      10.856 -23.038 -43.703  1.00 24.84           N  
-ATOM   3965  CA  GLU A 594      10.232 -23.956 -42.762  1.00 22.96           C  
-ATOM   3966  C   GLU A 594       9.255 -23.235 -41.835  1.00 23.49           C  
-ATOM   3967  O   GLU A 594       9.669 -22.474 -40.963  1.00 21.00           O  
-ATOM   3968  CB  GLU A 594      11.304 -24.669 -41.938  1.00 23.64           C  
-ATOM   3969  CG  GLU A 594      10.763 -25.736 -41.008  1.00 27.97           C  
-ATOM   3970  CD  GLU A 594      11.779 -26.166 -39.970  1.00 42.22           C  
-ATOM   3971  OE1 GLU A 594      12.283 -25.289 -39.236  1.00 44.89           O  
-ATOM   3972  OE2 GLU A 594      12.077 -27.377 -39.891  1.00 48.08           O  
-ATOM   3973  N   VAL A 595       7.961 -23.469 -42.024  1.00 25.07           N  
-ATOM   3974  CA  VAL A 595       6.961 -22.904 -41.125  1.00 15.71           C  
-ATOM   3975  C   VAL A 595       6.793 -23.817 -39.922  1.00 14.09           C  
-ATOM   3976  O   VAL A 595       6.603 -25.022 -40.067  1.00 12.50           O  
-ATOM   3977  CB  VAL A 595       5.604 -22.705 -41.812  1.00 15.34           C  
-ATOM   3978  CG1 VAL A 595       4.604 -22.115 -40.833  1.00 16.51           C  
-ATOM   3979  CG2 VAL A 595       5.755 -21.800 -43.008  1.00 16.99           C  
-ATOM   3980  N   VAL A 596       6.858 -23.230 -38.734  1.00 17.27           N  
-ATOM   3981  CA  VAL A 596       6.934 -23.998 -37.501  1.00 19.25           C  
-ATOM   3982  C   VAL A 596       5.925 -23.522 -36.457  1.00 22.56           C  
-ATOM   3983  O   VAL A 596       5.953 -22.366 -36.031  1.00 17.57           O  
-ATOM   3984  CB  VAL A 596       8.353 -23.925 -36.901  1.00 18.64           C  
-ATOM   3985  CG1 VAL A 596       8.383 -24.566 -35.541  1.00 15.19           C  
-ATOM   3986  CG2 VAL A 596       9.358 -24.588 -37.829  1.00 21.24           C  
-ATOM   3987  N   GLY A 597       5.038 -24.424 -36.046  1.00 17.30           N  
-ATOM   3988  CA  GLY A 597       4.062 -24.119 -35.016  1.00 15.07           C  
-ATOM   3989  C   GLY A 597       2.848 -23.383 -35.548  1.00 17.00           C  
-ATOM   3990  O   GLY A 597       2.177 -22.660 -34.813  1.00 17.71           O  
-ATOM   3991  N   TYR A 598       2.560 -23.563 -36.830  1.00 16.51           N  
-ATOM   3992  CA  TYR A 598       1.390 -22.933 -37.428  1.00 20.25           C  
-ATOM   3993  C   TYR A 598       0.139 -23.738 -37.114  1.00 19.58           C  
-ATOM   3994  O   TYR A 598      -0.088 -24.798 -37.697  1.00 16.76           O  
-ATOM   3995  CB  TYR A 598       1.564 -22.792 -38.942  1.00 22.08           C  
-ATOM   3996  CG  TYR A 598       0.507 -21.944 -39.617  1.00 15.25           C  
-ATOM   3997  CD1 TYR A 598       0.102 -20.736 -39.065  1.00 17.46           C  
-ATOM   3998  CD2 TYR A 598      -0.066 -22.339 -40.820  1.00 14.34           C  
-ATOM   3999  CE1 TYR A 598      -0.855 -19.953 -39.682  1.00 19.05           C  
-ATOM   4000  CE2 TYR A 598      -1.022 -21.561 -41.446  1.00 15.91           C  
-ATOM   4001  CZ  TYR A 598      -1.413 -20.369 -40.872  1.00 17.64           C  
-ATOM   4002  OH  TYR A 598      -2.364 -19.586 -41.486  1.00 16.26           O  
-ATOM   4003  N   VAL A 599      -0.667 -23.232 -36.184  1.00 21.37           N  
-ATOM   4004  CA  VAL A 599      -1.920 -23.885 -35.819  1.00 18.03           C  
-ATOM   4005  C   VAL A 599      -3.106 -22.964 -36.083  1.00 17.09           C  
-ATOM   4006  O   VAL A 599      -3.608 -22.326 -35.160  1.00 20.47           O  
-ATOM   4007  CB  VAL A 599      -1.935 -24.300 -34.337  1.00 16.27           C  
-ATOM   4008  CG1 VAL A 599      -2.974 -25.387 -34.105  1.00 21.75           C  
-ATOM   4009  CG2 VAL A 599      -0.559 -24.778 -33.903  1.00 19.68           C  
-ATOM   4010  N   PRO A 600      -3.553 -22.885 -37.346  1.00 15.02           N  
-ATOM   4011  CA  PRO A 600      -4.639 -21.980 -37.729  1.00 18.47           C  
-ATOM   4012  C   PRO A 600      -6.017 -22.627 -37.656  1.00 26.06           C  
-ATOM   4013  O   PRO A 600      -6.122 -23.850 -37.537  1.00 30.87           O  
-ATOM   4014  CB  PRO A 600      -4.294 -21.639 -39.171  1.00 13.68           C  
-ATOM   4015  CG  PRO A 600      -3.698 -22.901 -39.685  1.00 14.76           C  
-ATOM   4016  CD  PRO A 600      -2.957 -23.534 -38.526  1.00 14.25           C  
-ATOM   4017  N   HIS A 601      -7.062 -21.808 -37.726  1.00 21.86           N  
-ATOM   4018  CA  HIS A 601      -8.421 -22.321 -37.817  1.00 26.12           C  
-ATOM   4019  C   HIS A 601      -8.668 -22.860 -39.219  1.00 36.97           C  
-ATOM   4020  O   HIS A 601      -7.796 -22.779 -40.084  1.00 50.69           O  
-ATOM   4021  CB  HIS A 601      -9.440 -21.234 -37.479  1.00 26.30           C  
-ATOM   4022  CG  HIS A 601      -9.443 -20.834 -36.037  1.00 21.71           C  
-ATOM   4023  ND1 HIS A 601     -10.390 -21.285 -35.142  1.00 22.14           N  
-ATOM   4024  CD2 HIS A 601      -8.615 -20.027 -35.335  1.00 20.43           C  
-ATOM   4025  CE1 HIS A 601     -10.145 -20.770 -33.950  1.00 21.64           C  
-ATOM   4026  NE2 HIS A 601      -9.074 -20.004 -34.039  1.00 21.31           N  
-ATOM   4027  N   GLY A 602      -9.857 -23.408 -39.444  1.00 36.30           N  
-ATOM   4028  CA  GLY A 602     -10.193 -23.974 -40.737  1.00 47.56           C  
-ATOM   4029  C   GLY A 602     -10.255 -22.928 -41.835  1.00 54.56           C  
-ATOM   4030  O   GLY A 602     -10.371 -21.733 -41.559  1.00 46.24           O  
-ATOM   4031  N   ARG A 603     -10.171 -23.374 -43.084  1.00 60.12           N  
-ATOM   4032  CA  ARG A 603     -10.284 -22.466 -44.220  1.00 60.55           C  
-ATOM   4033  C   ARG A 603     -11.701 -21.911 -44.342  1.00 70.39           C  
-ATOM   4034  O   ARG A 603     -12.678 -22.585 -44.006  1.00 65.68           O  
-ATOM   4035  CB  ARG A 603      -9.892 -23.165 -45.523  1.00 57.01           C  
-ATOM   4036  CG  ARG A 603      -8.394 -23.318 -45.742  1.00 60.04           C  
-ATOM   4037  CD  ARG A 603      -8.112 -23.840 -47.146  1.00 62.69           C  
-ATOM   4038  NE  ARG A 603      -6.685 -23.997 -47.415  1.00 73.37           N  
-ATOM   4039  CZ  ARG A 603      -5.919 -23.066 -47.977  1.00 73.27           C  
-ATOM   4040  NH1 ARG A 603      -6.441 -21.897 -48.332  1.00 55.07           N  
-ATOM   4041  NH2 ARG A 603      -4.629 -23.303 -48.185  1.00 42.25           N  
-ATOM   4042  N   ILE A 604     -11.802 -20.675 -44.818  1.00 67.03           N  
-ATOM   4043  CA  ILE A 604     -13.095 -20.059 -45.082  1.00 65.15           C  
-ATOM   4044  C   ILE A 604     -13.215 -19.718 -46.561  1.00 71.16           C  
-ATOM   4045  O   ILE A 604     -12.440 -18.919 -47.088  1.00 73.21           O  
-ATOM   4046  CB  ILE A 604     -13.306 -18.787 -44.243  1.00 62.43           C  
-ATOM   4047  CG1 ILE A 604     -13.530 -19.148 -42.773  1.00 68.31           C  
-ATOM   4048  CG2 ILE A 604     -14.490 -17.999 -44.768  1.00 54.91           C  
-ATOM   4049  CD1 ILE A 604     -13.860 -17.958 -41.896  1.00 51.22           C  
-ATOM   4050  N   GLN A 605     -14.186 -20.336 -47.226  1.00 71.95           N  
-ATOM   4051  CA  GLN A 605     -14.376 -20.143 -48.658  1.00 69.26           C  
-ATOM   4052  C   GLN A 605     -14.835 -18.728 -48.992  1.00 75.31           C  
-ATOM   4053  O   GLN A 605     -15.877 -18.271 -48.523  1.00 67.87           O  
-ATOM   4054  CB  GLN A 605     -15.380 -21.159 -49.206  1.00 62.74           C  
-ATOM   4055  CG  GLN A 605     -14.739 -22.379 -49.851  1.00 67.76           C  
-ATOM   4056  CD  GLN A 605     -14.027 -22.048 -51.153  1.00 79.85           C  
-ATOM   4057  OE1 GLN A 605     -14.283 -21.012 -51.770  1.00 79.51           O  
-ATOM   4058  NE2 GLN A 605     -13.128 -22.930 -51.577  1.00 69.40           N  
-ATOM   4059  N   MET A 606     -14.039 -18.042 -49.806  1.00 72.29           N  
-ATOM   4060  CA  MET A 606     -14.384 -16.713 -50.293  1.00 68.93           C  
-ATOM   4061  C   MET A 606     -13.975 -16.571 -51.752  1.00 68.92           C  
-ATOM   4062  O   MET A 606     -12.787 -16.555 -52.074  1.00 67.82           O  
-ATOM   4063  CB  MET A 606     -13.716 -15.628 -49.447  1.00 67.97           C  
-ATOM   4064  CG  MET A 606     -14.357 -15.416 -48.085  1.00 65.49           C  
-ATOM   4065  SD  MET A 606     -13.493 -14.176 -47.100  1.00 67.97           S  
-ATOM   4066  CE  MET A 606     -11.919 -14.992 -46.857  1.00 56.98           C  
-ATOM   4067  N   GLU A 607     -14.967 -16.474 -52.631  1.00 77.64           N  
-ATOM   4068  CA  GLU A 607     -14.721 -16.361 -54.064  1.00 74.52           C  
-ATOM   4069  C   GLU A 607     -14.050 -15.040 -54.414  1.00 72.99           C  
-ATOM   4070  O   GLU A 607     -14.392 -13.990 -53.869  1.00 77.24           O  
-ATOM   4071  CB  GLU A 607     -16.027 -16.500 -54.844  1.00 72.92           C  
-ATOM   4072  CG  GLU A 607     -16.699 -17.854 -54.694  1.00 83.27           C  
-ATOM   4073  CD  GLU A 607     -18.046 -17.912 -55.384  1.00102.68           C  
-ATOM   4074  OE1 GLU A 607     -18.676 -18.990 -55.367  1.00102.52           O  
-ATOM   4075  OE2 GLU A 607     -18.477 -16.879 -55.942  1.00102.61           O  
-ATOM   4076  N   MET A 608     -13.090 -15.101 -55.329  1.00 75.74           N  
-ATOM   4077  CA  MET A 608     -12.385 -13.909 -55.775  1.00 83.10           C  
-ATOM   4078  C   MET A 608     -13.289 -13.040 -56.640  1.00 85.29           C  
-ATOM   4079  O   MET A 608     -13.887 -13.522 -57.604  1.00 77.51           O  
-ATOM   4080  CB  MET A 608     -11.124 -14.290 -56.555  1.00 86.62           C  
-ATOM   4081  CG  MET A 608     -10.245 -13.107 -56.934  1.00 77.12           C  
-ATOM   4082  SD  MET A 608      -9.214 -13.432 -58.377  1.00 73.55           S  
-ATOM   4083  CE  MET A 608      -8.436 -14.973 -57.905  1.00 85.67           C  
-ATOM   4084  N   ALA A 609     -13.395 -11.762 -56.289  1.00 80.61           N  
-ATOM   4085  CA  ALA A 609     -14.092 -10.808 -57.141  1.00 74.98           C  
-ATOM   4086  C   ALA A 609     -13.337 -10.690 -58.459  1.00 79.57           C  
-ATOM   4087  O   ALA A 609     -12.239 -10.133 -58.515  1.00 84.94           O  
-ATOM   4088  CB  ALA A 609     -14.216  -9.461 -56.462  1.00 67.77           C  
-ATOM   4089  N   VAL A 610     -13.943 -11.228 -59.511  1.00 78.88           N  
-ATOM   4090  CA  VAL A 610     -13.296 -11.414 -60.807  1.00 77.64           C  
-ATOM   4091  C   VAL A 610     -12.835 -10.118 -61.473  1.00 71.53           C  
-ATOM   4092  O   VAL A 610     -12.248 -10.141 -62.555  1.00 72.75           O  
-ATOM   4093  CB  VAL A 610     -14.243 -12.148 -61.774  1.00 87.69           C  
-ATOM   4094  CG1 VAL A 610     -13.534 -13.330 -62.414  1.00 76.99           C  
-ATOM   4095  CG2 VAL A 610     -15.497 -12.610 -61.036  1.00 90.08           C  
-ATOM   4096  OXT VAL A 610     -13.031  -9.018 -60.963  1.00 70.73           O  
-TER    4097      VAL A 610                                                      
-ATOM   4098  N   LYS B   3     -19.061  27.421  -4.109  1.00 80.00           N  
-ATOM   4099  CA  LYS B   3     -19.581  28.553  -4.871  1.00 84.98           C  
-ATOM   4100  C   LYS B   3     -18.749  28.886  -6.118  1.00 91.73           C  
-ATOM   4101  O   LYS B   3     -18.379  30.046  -6.317  1.00 82.74           O  
-ATOM   4102  CB  LYS B   3     -19.649  29.790  -3.972  1.00 82.81           C  
-ATOM   4103  CG  LYS B   3     -20.184  29.522  -2.572  1.00 79.28           C  
-ATOM   4104  CD  LYS B   3     -19.339  30.219  -1.515  1.00 80.61           C  
-ATOM   4105  CE  LYS B   3     -18.061  29.446  -1.223  1.00 72.71           C  
-ATOM   4106  NZ  LYS B   3     -18.355  28.129  -0.588  1.00 62.64           N  
-ATOM   4107  N   PRO B   4     -18.455  27.885  -6.970  1.00 90.27           N  
-ATOM   4108  CA  PRO B   4     -17.595  28.196  -8.118  1.00 80.37           C  
-ATOM   4109  C   PRO B   4     -18.343  28.925  -9.234  1.00 74.46           C  
-ATOM   4110  O   PRO B   4     -19.564  28.810  -9.342  1.00 69.35           O  
-ATOM   4111  CB  PRO B   4     -17.122  26.811  -8.591  1.00 77.99           C  
-ATOM   4112  CG  PRO B   4     -17.564  25.836  -7.512  1.00 72.82           C  
-ATOM   4113  CD  PRO B   4     -18.788  26.453  -6.930  1.00 70.68           C  
-ATOM   4114  N   VAL B   5     -17.606  29.668 -10.053  1.00 75.47           N  
-ATOM   4115  CA  VAL B   5     -18.188  30.440 -11.147  1.00 58.85           C  
-ATOM   4116  C   VAL B   5     -17.469  30.113 -12.458  1.00 60.99           C  
-ATOM   4117  O   VAL B   5     -16.270  29.834 -12.456  1.00 58.62           O  
-ATOM   4118  CB  VAL B   5     -18.102  31.959 -10.867  1.00 58.27           C  
-ATOM   4119  CG1 VAL B   5     -18.832  32.754 -11.936  1.00 55.90           C  
-ATOM   4120  CG2 VAL B   5     -18.660  32.278  -9.489  1.00 64.55           C  
-ATOM   4121  N   CYS B   6     -18.201  30.135 -13.569  1.00 60.06           N  
-ATOM   4122  CA  CYS B   6     -17.603  29.905 -14.884  1.00 55.69           C  
-ATOM   4123  C   CYS B   6     -18.065  30.937 -15.909  1.00 49.14           C  
-ATOM   4124  O   CYS B   6     -19.243  31.285 -15.960  1.00 53.24           O  
-ATOM   4125  CB  CYS B   6     -17.932  28.498 -15.385  1.00 51.09           C  
-ATOM   4126  SG  CYS B   6     -17.087  27.178 -14.489  1.00 67.51           S  
-ATOM   4127  N   LEU B   7     -17.131  31.421 -16.723  1.00 44.64           N  
-ATOM   4128  CA  LEU B   7     -17.456  32.376 -17.778  1.00 38.93           C  
-ATOM   4129  C   LEU B   7     -17.572  31.673 -19.126  1.00 37.73           C  
-ATOM   4130  O   LEU B   7     -16.743  30.831 -19.466  1.00 38.84           O  
-ATOM   4131  CB  LEU B   7     -16.401  33.483 -17.861  1.00 27.23           C  
-ATOM   4132  CG  LEU B   7     -16.065  34.257 -16.584  1.00 40.68           C  
-ATOM   4133  CD1 LEU B   7     -15.187  35.465 -16.895  1.00 34.33           C  
-ATOM   4134  CD2 LEU B   7     -17.325  34.681 -15.859  1.00 39.06           C  
-ATOM   4135  N   VAL B   8     -18.607  32.018 -19.887  1.00 35.24           N  
-ATOM   4136  CA  VAL B   8     -18.805  31.454 -21.220  1.00 36.49           C  
-ATOM   4137  C   VAL B   8     -18.796  32.564 -22.270  1.00 40.08           C  
-ATOM   4138  O   VAL B   8     -19.631  33.469 -22.237  1.00 41.58           O  
-ATOM   4139  CB  VAL B   8     -20.124  30.662 -21.314  1.00 37.27           C  
-ATOM   4140  CG1 VAL B   8     -20.303  30.096 -22.713  1.00 38.25           C  
-ATOM   4141  CG2 VAL B   8     -20.147  29.547 -20.281  1.00 35.48           C  
-ATOM   4142  N   VAL B   9     -17.851  32.487 -23.204  1.00 39.25           N  
-ATOM   4143  CA  VAL B   9     -17.612  33.581 -24.144  1.00 32.61           C  
-ATOM   4144  C   VAL B   9     -17.307  33.133 -25.570  1.00 38.41           C  
-ATOM   4145  O   VAL B   9     -16.921  31.990 -25.815  1.00 41.45           O  
-ATOM   4146  CB  VAL B   9     -16.432  34.456 -23.689  1.00 27.93           C  
-ATOM   4147  CG1 VAL B   9     -16.852  35.402 -22.589  1.00 35.61           C  
-ATOM   4148  CG2 VAL B   9     -15.286  33.581 -23.230  1.00 28.39           C  
-ATOM   4149  N   ALA B  10     -17.479  34.065 -26.503  1.00 35.99           N  
-ATOM   4150  CA  ALA B  10     -17.020  33.905 -27.876  1.00 29.22           C  
-ATOM   4151  C   ALA B  10     -16.348  35.202 -28.312  1.00 34.98           C  
-ATOM   4152  O   ALA B  10     -17.013  36.223 -28.490  1.00 40.83           O  
-ATOM   4153  CB  ALA B  10     -18.174  33.553 -28.800  1.00 31.43           C  
-ATOM   4154  N   MET B  11     -15.029  35.166 -28.473  1.00 28.11           N  
-ATOM   4155  CA  MET B  11     -14.276  36.385 -28.745  1.00 21.82           C  
-ATOM   4156  C   MET B  11     -13.287  36.248 -29.905  1.00 28.81           C  
-ATOM   4157  O   MET B  11     -12.798  35.157 -30.203  1.00 33.07           O  
-ATOM   4158  CB  MET B  11     -13.530  36.825 -27.485  1.00 22.20           C  
-ATOM   4159  CG  MET B  11     -12.397  35.896 -27.083  1.00 27.63           C  
-ATOM   4160  SD  MET B  11     -11.578  36.402 -25.560  1.00 34.24           S  
-ATOM   4161  CE  MET B  11     -12.745  35.831 -24.332  1.00 27.77           C  
-ATOM   4162  N   THR B  12     -13.006  37.376 -30.551  1.00 25.10           N  
-ATOM   4163  CA  THR B  12     -12.025  37.459 -31.629  1.00 23.82           C  
-ATOM   4164  C   THR B  12     -10.612  37.347 -31.042  1.00 29.46           C  
-ATOM   4165  O   THR B  12     -10.465  37.293 -29.821  1.00 29.33           O  
-ATOM   4166  CB  THR B  12     -12.187  38.780 -32.410  1.00 21.17           C  
-ATOM   4167  OG1 THR B  12     -11.652  39.865 -31.643  1.00 24.10           O  
-ATOM   4168  CG2 THR B  12     -13.656  39.044 -32.706  1.00 25.31           C  
-ATOM   4169  N   PRO B  13      -9.566  37.288 -31.894  1.00 27.57           N  
-ATOM   4170  CA  PRO B  13      -8.230  37.286 -31.282  1.00 25.70           C  
-ATOM   4171  C   PRO B  13      -7.930  38.569 -30.510  1.00 21.42           C  
-ATOM   4172  O   PRO B  13      -7.140  38.543 -29.568  1.00 17.15           O  
-ATOM   4173  CB  PRO B  13      -7.293  37.150 -32.485  1.00 27.59           C  
-ATOM   4174  CG  PRO B  13      -8.108  36.472 -33.513  1.00 25.61           C  
-ATOM   4175  CD  PRO B  13      -9.494  37.016 -33.341  1.00 20.58           C  
-ATOM   4176  N   LYS B  14      -8.562  39.670 -30.905  1.00 23.18           N  
-ATOM   4177  CA  LYS B  14      -8.384  40.947 -30.223  1.00 20.38           C  
-ATOM   4178  C   LYS B  14      -9.378  41.107 -29.076  1.00 25.17           C  
-ATOM   4179  O   LYS B  14      -9.636  42.224 -28.624  1.00 21.26           O  
-ATOM   4180  CB  LYS B  14      -8.534  42.109 -31.205  1.00 19.77           C  
-ATOM   4181  CG  LYS B  14      -7.405  42.240 -32.212  1.00 22.05           C  
-ATOM   4182  CD  LYS B  14      -7.615  43.460 -33.097  1.00 29.36           C  
-ATOM   4183  CE  LYS B  14      -6.471  43.654 -34.076  1.00 28.90           C  
-ATOM   4184  NZ  LYS B  14      -6.674  44.866 -34.914  1.00 31.12           N  
-ATOM   4185  N   ARG B  15      -9.936  39.983 -28.629  1.00 24.31           N  
-ATOM   4186  CA  ARG B  15     -10.841  39.925 -27.479  1.00 25.68           C  
-ATOM   4187  C   ARG B  15     -12.148  40.695 -27.686  1.00 28.84           C  
-ATOM   4188  O   ARG B  15     -12.825  41.048 -26.720  1.00 33.46           O  
-ATOM   4189  CB  ARG B  15     -10.131  40.437 -26.221  1.00 24.62           C  
-ATOM   4190  CG  ARG B  15      -8.852  39.692 -25.895  1.00 25.07           C  
-ATOM   4191  CD  ARG B  15      -8.256  40.131 -24.564  1.00 34.65           C  
-ATOM   4192  NE  ARG B  15      -7.339  41.257 -24.709  1.00 37.13           N  
-ATOM   4193  CZ  ARG B  15      -7.661  42.524 -24.469  1.00 38.95           C  
-ATOM   4194  NH1 ARG B  15      -6.757  43.480 -24.632  1.00 42.21           N  
-ATOM   4195  NH2 ARG B  15      -8.884  42.834 -24.063  1.00 35.88           N  
-ATOM   4196  N   GLY B  16     -12.505  40.945 -28.941  1.00 22.84           N  
-ATOM   4197  CA  GLY B  16     -13.753  41.621 -29.250  1.00 22.92           C  
-ATOM   4198  C   GLY B  16     -14.931  40.677 -29.118  1.00 26.94           C  
-ATOM   4199  O   GLY B  16     -14.843  39.519 -29.524  1.00 33.15           O  
-ATOM   4200  N   ILE B  17     -16.036  41.159 -28.552  1.00 33.40           N  
-ATOM   4201  CA  ILE B  17     -17.195  40.297 -28.323  1.00 24.34           C  
-ATOM   4202  C   ILE B  17     -18.514  40.876 -28.824  1.00 30.71           C  
-ATOM   4203  O   ILE B  17     -19.519  40.168 -28.873  1.00 39.05           O  
-ATOM   4204  CB  ILE B  17     -17.363  39.969 -26.829  1.00 24.10           C  
-ATOM   4205  CG1 ILE B  17     -17.517  41.253 -26.014  1.00 29.60           C  
-ATOM   4206  CG2 ILE B  17     -16.186  39.152 -26.328  1.00 34.73           C  
-ATOM   4207  CD1 ILE B  17     -17.726  41.013 -24.529  1.00 40.44           C  
-ATOM   4208  N   GLY B  18     -18.525  42.152 -29.191  1.00 37.31           N  
-ATOM   4209  CA  GLY B  18     -19.763  42.770 -29.631  1.00 36.74           C  
-ATOM   4210  C   GLY B  18     -19.642  44.117 -30.315  1.00 33.12           C  
-ATOM   4211  O   GLY B  18     -18.612  44.788 -30.235  1.00 30.95           O  
-ATOM   4212  N   ILE B  19     -20.715  44.508 -30.996  1.00 38.66           N  
-ATOM   4213  CA  ILE B  19     -20.799  45.820 -31.621  1.00 38.76           C  
-ATOM   4214  C   ILE B  19     -22.264  46.190 -31.860  1.00 35.87           C  
-ATOM   4215  O   ILE B  19     -23.061  45.362 -32.309  1.00 31.37           O  
-ATOM   4216  CB  ILE B  19     -19.999  45.872 -32.947  1.00 23.65           C  
-ATOM   4217  CG1 ILE B  19     -20.050  47.275 -33.554  1.00 21.06           C  
-ATOM   4218  CG2 ILE B  19     -20.493  44.819 -33.930  1.00 21.23           C  
-ATOM   4219  CD1 ILE B  19     -19.158  47.445 -34.754  1.00 17.99           C  
-ATOM   4220  N   ASN B  20     -22.609  47.434 -31.533  1.00 27.51           N  
-ATOM   4221  CA  ASN B  20     -23.984  47.920 -31.616  1.00 33.38           C  
-ATOM   4222  C   ASN B  20     -24.952  47.015 -30.862  1.00 41.60           C  
-ATOM   4223  O   ASN B  20     -26.021  46.670 -31.371  1.00 34.83           O  
-ATOM   4224  CB  ASN B  20     -24.421  48.058 -33.076  1.00 30.97           C  
-ATOM   4225  CG  ASN B  20     -23.716  49.193 -33.789  1.00 31.35           C  
-ATOM   4226  OD1 ASN B  20     -23.400  50.219 -33.186  1.00 41.85           O  
-ATOM   4227  ND2 ASN B  20     -23.465  49.016 -35.081  1.00 29.32           N  
-ATOM   4228  N   ASN B  21     -24.555  46.634 -29.649  1.00 43.29           N  
-ATOM   4229  CA  ASN B  21     -25.349  45.762 -28.789  1.00 33.03           C  
-ATOM   4230  C   ASN B  21     -25.777  44.480 -29.498  1.00 35.28           C  
-ATOM   4231  O   ASN B  21     -26.933  44.064 -29.412  1.00 47.92           O  
-ATOM   4232  CB  ASN B  21     -26.576  46.509 -28.266  1.00 39.62           C  
-ATOM   4233  CG  ASN B  21     -26.960  46.081 -26.869  1.00 54.82           C  
-ATOM   4234  OD1 ASN B  21     -26.271  46.403 -25.902  1.00 56.04           O  
-ATOM   4235  ND2 ASN B  21     -28.067  45.355 -26.751  1.00 59.28           N  
-ATOM   4236  N   GLY B  22     -24.834  43.865 -30.203  1.00 31.74           N  
-ATOM   4237  CA  GLY B  22     -25.095  42.640 -30.932  1.00 31.97           C  
-ATOM   4238  C   GLY B  22     -23.817  41.866 -31.173  1.00 27.84           C  
-ATOM   4239  O   GLY B  22     -22.793  42.138 -30.549  1.00 27.50           O  
-ATOM   4240  N   LEU B  23     -23.870  40.904 -32.087  1.00 23.66           N  
-ATOM   4241  CA  LEU B  23     -22.711  40.068 -32.371  1.00 22.27           C  
-ATOM   4242  C   LEU B  23     -21.950  40.557 -33.597  1.00 17.80           C  
-ATOM   4243  O   LEU B  23     -22.553  40.908 -34.610  1.00 18.09           O  
-ATOM   4244  CB  LEU B  23     -23.142  38.614 -32.557  1.00 29.12           C  
-ATOM   4245  CG  LEU B  23     -23.804  38.008 -31.319  1.00 20.03           C  
-ATOM   4246  CD1 LEU B  23     -24.208  36.563 -31.561  1.00 28.93           C  
-ATOM   4247  CD2 LEU B  23     -22.875  38.122 -30.121  1.00 22.34           C  
-ATOM   4248  N   PRO B  24     -20.613  40.578 -33.500  1.00 18.13           N  
-ATOM   4249  CA  PRO B  24     -19.705  41.059 -34.546  1.00 25.22           C  
-ATOM   4250  C   PRO B  24     -19.701  40.161 -35.777  1.00 27.00           C  
-ATOM   4251  O   PRO B  24     -19.570  40.646 -36.902  1.00 24.13           O  
-ATOM   4252  CB  PRO B  24     -18.332  41.031 -33.864  1.00 25.27           C  
-ATOM   4253  CG  PRO B  24     -18.606  40.880 -32.407  1.00 21.36           C  
-ATOM   4254  CD  PRO B  24     -19.878  40.121 -32.312  1.00 22.65           C  
-ATOM   4255  N   TRP B  25     -19.843  38.860 -35.549  1.00 26.23           N  
-ATOM   4256  CA  TRP B  25     -19.753  37.862 -36.608  1.00 24.31           C  
-ATOM   4257  C   TRP B  25     -21.123  37.287 -36.957  1.00 24.41           C  
-ATOM   4258  O   TRP B  25     -22.034  37.306 -36.130  1.00 24.77           O  
-ATOM   4259  CB  TRP B  25     -18.802  36.742 -36.179  1.00 26.99           C  
-ATOM   4260  CG  TRP B  25     -18.619  36.679 -34.692  1.00 33.71           C  
-ATOM   4261  CD1 TRP B  25     -17.591  37.217 -33.968  1.00 39.69           C  
-ATOM   4262  CD2 TRP B  25     -19.494  36.063 -33.745  1.00 26.66           C  
-ATOM   4263  NE1 TRP B  25     -17.770  36.966 -32.629  1.00 26.23           N  
-ATOM   4264  CE2 TRP B  25     -18.934  36.258 -32.465  1.00 34.43           C  
-ATOM   4265  CE3 TRP B  25     -20.699  35.359 -33.851  1.00 33.06           C  
-ATOM   4266  CZ2 TRP B  25     -19.532  35.777 -31.305  1.00 50.75           C  
-ATOM   4267  CZ3 TRP B  25     -21.293  34.880 -32.695  1.00 49.26           C  
-ATOM   4268  CH2 TRP B  25     -20.710  35.091 -31.441  1.00 61.27           C  
-ATOM   4269  N   PRO B  26     -21.277  36.782 -38.192  1.00 17.62           N  
-ATOM   4270  CA  PRO B  26     -22.502  36.072 -38.574  1.00 14.60           C  
-ATOM   4271  C   PRO B  26     -22.738  34.835 -37.710  1.00 28.27           C  
-ATOM   4272  O   PRO B  26     -21.845  34.421 -36.969  1.00 36.45           O  
-ATOM   4273  CB  PRO B  26     -22.248  35.685 -40.034  1.00 15.47           C  
-ATOM   4274  CG  PRO B  26     -20.772  35.805 -40.224  1.00 25.38           C  
-ATOM   4275  CD  PRO B  26     -20.348  36.915 -39.325  1.00 22.04           C  
-ATOM   4276  N   HIS B  27     -23.929  34.254 -37.819  1.00 27.88           N  
-ATOM   4277  CA  HIS B  27     -24.377  33.203 -36.909  1.00 29.45           C  
-ATOM   4278  C   HIS B  27     -23.438  31.998 -36.850  1.00 37.70           C  
-ATOM   4279  O   HIS B  27     -23.090  31.419 -37.881  1.00 33.89           O  
-ATOM   4280  CB  HIS B  27     -25.779  32.738 -37.306  1.00 27.76           C  
-ATOM   4281  CG  HIS B  27     -26.513  32.029 -36.212  1.00 26.43           C  
-ATOM   4282  ND1 HIS B  27     -26.436  30.666 -36.024  1.00 27.67           N  
-ATOM   4283  CD2 HIS B  27     -27.338  32.496 -35.245  1.00 27.71           C  
-ATOM   4284  CE1 HIS B  27     -27.183  30.323 -34.990  1.00 36.64           C  
-ATOM   4285  NE2 HIS B  27     -27.742  31.415 -34.500  1.00 34.22           N  
-ATOM   4286  N   LEU B  28     -23.033  31.630 -35.635  1.00 42.03           N  
-ATOM   4287  CA  LEU B  28     -22.184  30.458 -35.417  1.00 32.92           C  
-ATOM   4288  C   LEU B  28     -22.975  29.313 -34.775  1.00 33.71           C  
-ATOM   4289  O   LEU B  28     -23.048  29.191 -33.546  1.00 37.80           O  
-ATOM   4290  CB  LEU B  28     -20.977  30.823 -34.551  1.00 25.94           C  
-ATOM   4291  CG  LEU B  28     -20.092  31.972 -35.043  1.00 26.56           C  
-ATOM   4292  CD1 LEU B  28     -18.929  32.194 -34.089  1.00 25.43           C  
-ATOM   4293  CD2 LEU B  28     -19.588  31.716 -36.454  1.00 25.42           C  
-ATOM   4294  N   THR B  29     -23.556  28.478 -35.632  1.00 32.86           N  
-ATOM   4295  CA  THR B  29     -24.441  27.391 -35.226  1.00 36.26           C  
-ATOM   4296  C   THR B  29     -23.818  26.474 -34.179  1.00 36.33           C  
-ATOM   4297  O   THR B  29     -24.378  26.289 -33.093  1.00 48.06           O  
-ATOM   4298  CB  THR B  29     -24.850  26.536 -36.436  1.00 35.93           C  
-ATOM   4299  OG1 THR B  29     -25.334  27.385 -37.484  1.00 36.76           O  
-ATOM   4300  CG2 THR B  29     -25.926  25.541 -36.042  1.00 36.69           C  
-ATOM   4301  N   THR B  30     -22.666  25.899 -34.515  1.00 26.43           N  
-ATOM   4302  CA  THR B  30     -21.982  24.972 -33.623  1.00 26.72           C  
-ATOM   4303  C   THR B  30     -21.643  25.640 -32.299  1.00 27.52           C  
-ATOM   4304  O   THR B  30     -21.722  25.019 -31.242  1.00 32.56           O  
-ATOM   4305  CB  THR B  30     -20.697  24.416 -34.269  1.00 28.03           C  
-ATOM   4306  OG1 THR B  30     -21.040  23.656 -35.434  1.00 35.53           O  
-ATOM   4307  CG2 THR B  30     -19.943  23.521 -33.298  1.00 29.48           C  
-ATOM   4308  N   ASP B  31     -21.277  26.915 -32.359  1.00 37.05           N  
-ATOM   4309  CA  ASP B  31     -21.005  27.676 -31.146  1.00 36.07           C  
-ATOM   4310  C   ASP B  31     -22.251  27.775 -30.280  1.00 33.34           C  
-ATOM   4311  O   ASP B  31     -22.172  27.662 -29.059  1.00 38.90           O  
-ATOM   4312  CB  ASP B  31     -20.495  29.075 -31.480  1.00 32.93           C  
-ATOM   4313  CG  ASP B  31     -20.356  29.953 -30.253  1.00 30.49           C  
-ATOM   4314  OD1 ASP B  31     -19.756  29.501 -29.256  1.00 20.96           O  
-ATOM   4315  OD2 ASP B  31     -20.860  31.095 -30.286  1.00 42.85           O  
-ATOM   4316  N   PHE B  32     -23.403  27.983 -30.912  1.00 37.67           N  
-ATOM   4317  CA  PHE B  32     -24.651  28.068 -30.161  1.00 39.19           C  
-ATOM   4318  C   PHE B  32     -25.027  26.726 -29.543  1.00 33.88           C  
-ATOM   4319  O   PHE B  32     -25.497  26.673 -28.406  1.00 34.52           O  
-ATOM   4320  CB  PHE B  32     -25.784  28.586 -31.046  1.00 41.05           C  
-ATOM   4321  CG  PHE B  32     -25.927  30.079 -31.016  1.00 44.40           C  
-ATOM   4322  CD1 PHE B  32     -26.453  30.710 -29.901  1.00 59.07           C  
-ATOM   4323  CD2 PHE B  32     -25.529  30.853 -32.091  1.00 42.99           C  
-ATOM   4324  CE1 PHE B  32     -26.582  32.086 -29.860  1.00 54.95           C  
-ATOM   4325  CE2 PHE B  32     -25.657  32.232 -32.058  1.00 53.20           C  
-ATOM   4326  CZ  PHE B  32     -26.185  32.848 -30.939  1.00 46.61           C  
-ATOM   4327  N   LYS B  33     -24.824  25.645 -30.290  1.00 39.75           N  
-ATOM   4328  CA  LYS B  33     -25.066  24.308 -29.758  1.00 47.49           C  
-ATOM   4329  C   LYS B  33     -24.173  24.054 -28.547  1.00 45.81           C  
-ATOM   4330  O   LYS B  33     -24.614  23.511 -27.538  1.00 56.84           O  
-ATOM   4331  CB  LYS B  33     -24.827  23.244 -30.833  1.00 39.24           C  
-ATOM   4332  CG  LYS B  33     -25.916  23.176 -31.897  1.00 48.10           C  
-ATOM   4333  CD  LYS B  33     -25.538  22.205 -33.007  1.00 47.85           C  
-ATOM   4334  CE  LYS B  33     -26.577  22.207 -34.118  1.00 56.00           C  
-ATOM   4335  NZ  LYS B  33     -26.107  21.453 -35.314  1.00 43.28           N  
-ATOM   4336  N   HIS B  34     -22.915  24.466 -28.666  1.00 46.07           N  
-ATOM   4337  CA  HIS B  34     -21.939  24.373 -27.585  1.00 51.74           C  
-ATOM   4338  C   HIS B  34     -22.399  25.138 -26.347  1.00 48.74           C  
-ATOM   4339  O   HIS B  34     -22.348  24.614 -25.234  1.00 49.56           O  
-ATOM   4340  CB  HIS B  34     -20.579  24.903 -28.053  1.00 49.26           C  
-ATOM   4341  CG  HIS B  34     -19.633  25.224 -26.936  1.00 50.26           C  
-ATOM   4342  ND1 HIS B  34     -18.838  24.272 -26.335  1.00 54.17           N  
-ATOM   4343  CD2 HIS B  34     -19.351  26.395 -26.316  1.00 44.93           C  
-ATOM   4344  CE1 HIS B  34     -18.109  24.842 -25.392  1.00 55.29           C  
-ATOM   4345  NE2 HIS B  34     -18.401  26.130 -25.359  1.00 52.83           N  
-ATOM   4346  N   PHE B  35     -22.843  26.376 -26.549  1.00 40.72           N  
-ATOM   4347  CA  PHE B  35     -23.332  27.217 -25.461  1.00 37.34           C  
-ATOM   4348  C   PHE B  35     -24.512  26.559 -24.755  1.00 46.68           C  
-ATOM   4349  O   PHE B  35     -24.505  26.383 -23.533  1.00 50.88           O  
-ATOM   4350  CB  PHE B  35     -23.732  28.595 -26.000  1.00 31.78           C  
-ATOM   4351  CG  PHE B  35     -24.346  29.504 -24.969  1.00 39.36           C  
-ATOM   4352  CD1 PHE B  35     -23.549  30.259 -24.125  1.00 43.53           C  
-ATOM   4353  CD2 PHE B  35     -25.723  29.613 -24.852  1.00 49.31           C  
-ATOM   4354  CE1 PHE B  35     -24.110  31.097 -23.180  1.00 42.48           C  
-ATOM   4355  CE2 PHE B  35     -26.293  30.451 -23.906  1.00 48.24           C  
-ATOM   4356  CZ  PHE B  35     -25.485  31.194 -23.070  1.00 41.30           C  
-ATOM   4357  N   SER B  36     -25.516  26.189 -25.543  1.00 51.42           N  
-ATOM   4358  CA  SER B  36     -26.750  25.619 -25.018  1.00 57.51           C  
-ATOM   4359  C   SER B  36     -26.495  24.306 -24.288  1.00 60.53           C  
-ATOM   4360  O   SER B  36     -27.142  24.015 -23.286  1.00 72.69           O  
-ATOM   4361  CB  SER B  36     -27.761  25.404 -26.148  1.00 63.40           C  
-ATOM   4362  OG  SER B  36     -29.094  25.504 -25.670  1.00 62.28           O  
-ATOM   4363  N   ARG B  37     -25.553  23.518 -24.791  1.00 51.93           N  
-ATOM   4364  CA  ARG B  37     -25.221  22.247 -24.159  1.00 52.57           C  
-ATOM   4365  C   ARG B  37     -24.465  22.448 -22.853  1.00 48.38           C  
-ATOM   4366  O   ARG B  37     -24.791  21.834 -21.838  1.00 51.51           O  
-ATOM   4367  CB  ARG B  37     -24.403  21.378 -25.110  1.00 56.36           C  
-ATOM   4368  CG  ARG B  37     -25.128  20.130 -25.563  1.00 71.28           C  
-ATOM   4369  CD  ARG B  37     -26.458  20.467 -26.213  1.00 79.08           C  
-ATOM   4370  NE  ARG B  37     -26.618  19.774 -27.487  1.00 85.11           N  
-ATOM   4371  CZ  ARG B  37     -26.963  18.496 -27.604  1.00 87.81           C  
-ATOM   4372  NH1 ARG B  37     -27.081  17.948 -28.806  1.00 90.92           N  
-ATOM   4373  NH2 ARG B  37     -27.188  17.763 -26.521  1.00 73.05           N  
-ATOM   4374  N   VAL B  38     -23.454  23.310 -22.887  1.00 52.20           N  
-ATOM   4375  CA  VAL B  38     -22.649  23.598 -21.706  1.00 51.36           C  
-ATOM   4376  C   VAL B  38     -23.489  24.181 -20.575  1.00 50.64           C  
-ATOM   4377  O   VAL B  38     -23.363  23.771 -19.422  1.00 57.80           O  
-ATOM   4378  CB  VAL B  38     -21.498  24.576 -22.033  1.00 44.02           C  
-ATOM   4379  CG1 VAL B  38     -20.941  25.206 -20.763  1.00 41.97           C  
-ATOM   4380  CG2 VAL B  38     -20.401  23.865 -22.806  1.00 46.74           C  
-ATOM   4381  N   THR B  39     -24.365  25.121 -20.910  1.00 47.23           N  
-ATOM   4382  CA  THR B  39     -25.091  25.861 -19.886  1.00 51.12           C  
-ATOM   4383  C   THR B  39     -26.175  25.050 -19.173  1.00 62.92           C  
-ATOM   4384  O   THR B  39     -26.809  25.556 -18.247  1.00 71.34           O  
-ATOM   4385  CB  THR B  39     -25.738  27.127 -20.468  1.00 55.55           C  
-ATOM   4386  OG1 THR B  39     -26.217  26.862 -21.792  1.00 63.29           O  
-ATOM   4387  CG2 THR B  39     -24.726  28.262 -20.522  1.00 42.00           C  
-ATOM   4388  N   LYS B  40     -26.392  23.800 -19.577  1.00 63.77           N  
-ATOM   4389  CA  LYS B  40     -27.385  22.979 -18.887  1.00 67.64           C  
-ATOM   4390  C   LYS B  40     -26.933  21.540 -18.629  1.00 73.86           C  
-ATOM   4391  O   LYS B  40     -26.345  20.886 -19.495  1.00 64.37           O  
-ATOM   4392  CB  LYS B  40     -28.703  22.972 -19.667  1.00 72.26           C  
-ATOM   4393  CG  LYS B  40     -28.628  22.362 -21.053  1.00 73.41           C  
-ATOM   4394  CD  LYS B  40     -29.914  21.621 -21.387  1.00 77.50           C  
-ATOM   4395  CE  LYS B  40     -30.137  21.529 -22.888  1.00 68.89           C  
-ATOM   4396  NZ  LYS B  40     -28.972  20.942 -23.608  1.00 73.30           N  
-ATOM   4397  N   THR B  41     -27.208  21.068 -17.415  1.00100.18           N  
-ATOM   4398  CA  THR B  41     -27.000  19.673 -17.031  1.00107.49           C  
-ATOM   4399  C   THR B  41     -27.781  19.346 -15.758  1.00 96.85           C  
-ATOM   4400  O   THR B  41     -27.524  19.909 -14.690  1.00 83.86           O  
-ATOM   4401  CB  THR B  41     -25.505  19.336 -16.801  1.00 91.24           C  
-ATOM   4402  OG1 THR B  41     -24.708  20.520 -16.941  1.00 85.78           O  
-ATOM   4403  CG2 THR B  41     -25.038  18.291 -17.804  1.00 75.39           C  
-ATOM   4404  N   PHE B  74     -31.428  22.280 -11.793  1.00 55.60           N  
-ATOM   4405  CA  PHE B  74     -31.084  23.007 -13.010  1.00 66.44           C  
-ATOM   4406  C   PHE B  74     -29.801  23.821 -12.853  1.00 77.93           C  
-ATOM   4407  O   PHE B  74     -29.198  23.853 -11.780  1.00 81.14           O  
-ATOM   4408  CB  PHE B  74     -32.235  23.929 -13.421  1.00 69.71           C  
-ATOM   4409  CG  PHE B  74     -32.850  24.682 -12.273  1.00 81.57           C  
-ATOM   4410  CD1 PHE B  74     -32.126  25.642 -11.584  1.00 72.92           C  
-ATOM   4411  CD2 PHE B  74     -34.158  24.436 -11.890  1.00 88.78           C  
-ATOM   4412  CE1 PHE B  74     -32.689  26.334 -10.530  1.00 77.66           C  
-ATOM   4413  CE2 PHE B  74     -34.729  25.128 -10.837  1.00 87.05           C  
-ATOM   4414  CZ  PHE B  74     -33.992  26.078 -10.157  1.00 88.80           C  
-ATOM   4415  N   ASN B  75     -29.396  24.483 -13.933  1.00 71.80           N  
-ATOM   4416  CA  ASN B  75     -28.239  25.370 -13.907  1.00 65.71           C  
-ATOM   4417  C   ASN B  75     -28.663  26.834 -13.933  1.00 64.34           C  
-ATOM   4418  O   ASN B  75     -29.827  27.147 -14.184  1.00 68.23           O  
-ATOM   4419  CB  ASN B  75     -27.305  25.068 -15.081  1.00 62.81           C  
-ATOM   4420  CG  ASN B  75     -26.232  24.057 -14.725  1.00 67.36           C  
-ATOM   4421  OD1 ASN B  75     -25.602  24.153 -13.673  1.00 72.17           O  
-ATOM   4422  ND2 ASN B  75     -26.019  23.082 -15.600  1.00 65.12           N  
-ATOM   4423  N   ALA B  76     -27.719  27.732 -13.672  1.00 56.70           N  
-ATOM   4424  CA  ALA B  76     -28.033  29.155 -13.625  1.00 65.63           C  
-ATOM   4425  C   ALA B  76     -27.154  29.971 -14.567  1.00 66.20           C  
-ATOM   4426  O   ALA B  76     -25.955  29.721 -14.690  1.00 61.52           O  
-ATOM   4427  CB  ALA B  76     -27.900  29.676 -12.202  1.00 67.40           C  
-ATOM   4428  N   VAL B  77     -27.766  30.948 -15.229  1.00 64.29           N  
-ATOM   4429  CA  VAL B  77     -27.046  31.870 -16.098  1.00 54.14           C  
-ATOM   4430  C   VAL B  77     -27.220  33.313 -15.620  1.00 51.69           C  
-ATOM   4431  O   VAL B  77     -28.315  33.727 -15.228  1.00 57.49           O  
-ATOM   4432  CB  VAL B  77     -27.512  31.746 -17.565  1.00 42.88           C  
-ATOM   4433  CG1 VAL B  77     -27.099  30.400 -18.141  1.00 43.49           C  
-ATOM   4434  CG2 VAL B  77     -29.018  31.934 -17.673  1.00 41.82           C  
-ATOM   4435  N   VAL B  78     -26.127  34.070 -15.642  1.00 39.57           N  
-ATOM   4436  CA  VAL B  78     -26.144  35.458 -15.198  1.00 44.51           C  
-ATOM   4437  C   VAL B  78     -25.658  36.381 -16.308  1.00 53.81           C  
-ATOM   4438  O   VAL B  78     -24.573  36.190 -16.858  1.00 57.84           O  
-ATOM   4439  CB  VAL B  78     -25.275  35.665 -13.948  1.00 40.30           C  
-ATOM   4440  CG1 VAL B  78     -25.355  37.111 -13.484  1.00 46.46           C  
-ATOM   4441  CG2 VAL B  78     -25.710  34.723 -12.840  1.00 41.10           C  
-ATOM   4442  N   MET B  79     -26.468  37.384 -16.630  1.00 52.09           N  
-ATOM   4443  CA  MET B  79     -26.183  38.275 -17.746  1.00 49.69           C  
-ATOM   4444  C   MET B  79     -26.417  39.738 -17.395  1.00 53.12           C  
-ATOM   4445  O   MET B  79     -27.200  40.064 -16.498  1.00 59.91           O  
-ATOM   4446  CB  MET B  79     -27.036  37.888 -18.952  1.00 53.23           C  
-ATOM   4447  CG  MET B  79     -28.520  37.779 -18.633  1.00 66.15           C  
-ATOM   4448  SD  MET B  79     -29.394  36.632 -19.714  1.00 60.26           S  
-ATOM   4449  CE  MET B  79     -29.058  37.368 -21.307  1.00 62.80           C  
-ATOM   4450  N   GLY B  80     -25.731  40.618 -18.115  1.00 59.48           N  
-ATOM   4451  CA  GLY B  80     -25.848  42.045 -17.883  1.00 66.18           C  
-ATOM   4452  C   GLY B  80     -27.150  42.601 -18.424  1.00 69.32           C  
-ATOM   4453  O   GLY B  80     -27.947  41.866 -19.013  1.00 55.03           O  
-ATOM   4454  N   ARG B  81     -27.361  43.900 -18.222  1.00 81.16           N  
-ATOM   4455  CA  ARG B  81     -28.594  44.556 -18.637  1.00 88.17           C  
-ATOM   4456  C   ARG B  81     -28.763  44.510 -20.149  1.00 82.81           C  
-ATOM   4457  O   ARG B  81     -29.762  44.008 -20.657  1.00 76.63           O  
-ATOM   4458  CB  ARG B  81     -28.625  46.009 -18.149  1.00 90.49           C  
-ATOM   4459  CG  ARG B  81     -29.933  46.745 -18.498  1.00 89.54           C  
-ATOM   4460  CD  ARG B  81     -29.865  48.229 -18.145  1.00 75.56           C  
-ATOM   4461  NE  ARG B  81     -29.047  48.959 -19.106  1.00 86.75           N  
-ATOM   4462  CZ  ARG B  81     -29.509  49.471 -20.245  1.00 92.18           C  
-ATOM   4463  NH1 ARG B  81     -30.792  49.341 -20.573  1.00 88.03           N  
-ATOM   4464  NH2 ARG B  81     -28.685  50.116 -21.060  1.00 87.83           N  
-ATOM   4465  N   LYS B  82     -27.773  45.029 -20.862  1.00 73.69           N  
-ATOM   4466  CA  LYS B  82     -27.839  45.117 -22.315  1.00 66.60           C  
-ATOM   4467  C   LYS B  82     -27.788  43.740 -22.983  1.00 71.72           C  
-ATOM   4468  O   LYS B  82     -28.353  43.538 -24.061  1.00 71.14           O  
-ATOM   4469  CB  LYS B  82     -26.706  46.010 -22.830  1.00 67.53           C  
-ATOM   4470  CG  LYS B  82     -26.946  47.497 -22.598  1.00 78.24           C  
-ATOM   4471  CD  LYS B  82     -25.735  48.178 -21.976  1.00 76.33           C  
-ATOM   4472  CE  LYS B  82     -24.671  48.502 -23.012  1.00 68.84           C  
-ATOM   4473  NZ  LYS B  82     -23.555  49.295 -22.424  1.00 52.53           N  
-ATOM   4474  N   THR B  83     -27.119  42.796 -22.326  1.00 71.74           N  
-ATOM   4475  CA  THR B  83     -26.977  41.436 -22.843  1.00 66.08           C  
-ATOM   4476  C   THR B  83     -28.338  40.750 -22.962  1.00 68.25           C  
-ATOM   4477  O   THR B  83     -28.570  39.959 -23.878  1.00 67.29           O  
-ATOM   4478  CB  THR B  83     -26.053  40.582 -21.944  1.00 62.08           C  
-ATOM   4479  OG1 THR B  83     -24.810  41.266 -21.741  1.00 62.64           O  
-ATOM   4480  CG2 THR B  83     -25.786  39.228 -22.577  1.00 47.07           C  
-ATOM   4481  N   TRP B  84     -29.232  41.060 -22.028  1.00 74.11           N  
-ATOM   4482  CA  TRP B  84     -30.590  40.531 -22.050  1.00 78.09           C  
-ATOM   4483  C   TRP B  84     -31.352  41.090 -23.247  1.00 76.34           C  
-ATOM   4484  O   TRP B  84     -32.162  40.396 -23.867  1.00 70.90           O  
-ATOM   4485  CB  TRP B  84     -31.304  40.866 -20.738  1.00 80.31           C  
-ATOM   4486  CG  TRP B  84     -32.786  40.650 -20.754  1.00 81.22           C  
-ATOM   4487  CD1 TRP B  84     -33.741  41.576 -21.055  1.00 79.89           C  
-ATOM   4488  CD2 TRP B  84     -33.487  39.439 -20.439  1.00 67.80           C  
-ATOM   4489  NE1 TRP B  84     -34.990  41.018 -20.956  1.00 74.59           N  
-ATOM   4490  CE2 TRP B  84     -34.863  39.706 -20.578  1.00 61.78           C  
-ATOM   4491  CE3 TRP B  84     -33.087  38.154 -20.060  1.00 75.26           C  
-ATOM   4492  CZ2 TRP B  84     -35.840  38.739 -20.351  1.00 65.29           C  
-ATOM   4493  CZ3 TRP B  84     -34.059  37.197 -19.830  1.00 67.39           C  
-ATOM   4494  CH2 TRP B  84     -35.418  37.493 -19.979  1.00 60.05           C  
-ATOM   4495  N   GLU B  85     -31.074  42.347 -23.577  1.00 69.90           N  
-ATOM   4496  CA  GLU B  85     -31.735  43.003 -24.695  1.00 72.49           C  
-ATOM   4497  C   GLU B  85     -31.186  42.517 -26.030  1.00 76.05           C  
-ATOM   4498  O   GLU B  85     -31.891  42.523 -27.036  1.00 75.24           O  
-ATOM   4499  CB  GLU B  85     -31.589  44.520 -24.578  1.00 80.66           C  
-ATOM   4500  CG  GLU B  85     -32.352  45.114 -23.406  1.00 91.70           C  
-ATOM   4501  CD  GLU B  85     -31.983  46.561 -23.142  1.00 92.15           C  
-ATOM   4502  OE1 GLU B  85     -31.003  47.045 -23.747  1.00 84.08           O  
-ATOM   4503  OE2 GLU B  85     -32.672  47.211 -22.326  1.00 86.82           O  
-ATOM   4504  N   SER B  86     -29.927  42.092 -26.033  1.00 79.70           N  
-ATOM   4505  CA  SER B  86     -29.292  41.600 -27.251  1.00 62.67           C  
-ATOM   4506  C   SER B  86     -30.012  40.372 -27.802  1.00 57.35           C  
-ATOM   4507  O   SER B  86     -30.063  40.163 -29.012  1.00 67.28           O  
-ATOM   4508  CB  SER B  86     -27.818  41.274 -26.993  1.00 55.26           C  
-ATOM   4509  OG  SER B  86     -27.065  42.450 -26.748  1.00 66.49           O  
-ATOM   4510  N   MET B  87     -30.582  39.570 -26.909  1.00 58.56           N  
-ATOM   4511  CA  MET B  87     -31.267  38.343 -27.304  1.00 66.21           C  
-ATOM   4512  C   MET B  87     -32.665  38.603 -27.859  1.00 73.63           C  
-ATOM   4513  O   MET B  87     -33.410  39.419 -27.313  1.00 72.69           O  
-ATOM   4514  CB  MET B  87     -31.370  37.384 -26.116  1.00 73.71           C  
-ATOM   4515  CG  MET B  87     -30.038  36.905 -25.566  1.00 70.92           C  
-ATOM   4516  SD  MET B  87     -30.272  35.758 -24.193  1.00 73.96           S  
-ATOM   4517  CE  MET B  87     -31.412  34.589 -24.926  1.00 70.31           C  
-ATOM   4518  N   PRO B  88     -33.017  37.915 -28.959  1.00 75.95           N  
-ATOM   4519  CA  PRO B  88     -34.388  37.867 -29.480  1.00 82.73           C  
-ATOM   4520  C   PRO B  88     -35.398  37.532 -28.384  1.00 90.58           C  
-ATOM   4521  O   PRO B  88     -35.084  36.747 -27.488  1.00 89.08           O  
-ATOM   4522  CB  PRO B  88     -34.334  36.746 -30.521  1.00 68.77           C  
-ATOM   4523  CG  PRO B  88     -32.887  36.613 -30.899  1.00 65.70           C  
-ATOM   4524  CD  PRO B  88     -32.041  37.383 -29.924  1.00 68.64           C  
-ATOM   4525  N   ARG B  89     -36.591  38.114 -28.464  1.00 90.65           N  
-ATOM   4526  CA  ARG B  89     -37.607  37.951 -27.428  1.00 86.65           C  
-ATOM   4527  C   ARG B  89     -38.032  36.498 -27.246  1.00 82.61           C  
-ATOM   4528  O   ARG B  89     -38.346  36.070 -26.135  1.00 79.49           O  
-ATOM   4529  CB  ARG B  89     -38.835  38.806 -27.750  1.00 83.91           C  
-ATOM   4530  CG  ARG B  89     -38.502  40.220 -28.185  1.00 82.86           C  
-ATOM   4531  CD  ARG B  89     -38.814  40.444 -29.659  1.00 97.37           C  
-ATOM   4532  NE  ARG B  89     -38.289  39.382 -30.513  1.00 94.73           N  
-ATOM   4533  CZ  ARG B  89     -38.195  39.468 -31.836  1.00 82.88           C  
-ATOM   4534  NH1 ARG B  89     -38.582  40.574 -32.456  1.00 67.91           N  
-ATOM   4535  NH2 ARG B  89     -37.708  38.452 -32.538  1.00 70.10           N  
-ATOM   4536  N   LYS B  90     -38.039  35.744 -28.340  1.00 77.32           N  
-ATOM   4537  CA  LYS B  90     -38.481  34.354 -28.307  1.00 81.86           C  
-ATOM   4538  C   LYS B  90     -37.496  33.463 -27.555  1.00 81.43           C  
-ATOM   4539  O   LYS B  90     -37.842  32.357 -27.137  1.00 70.54           O  
-ATOM   4540  CB  LYS B  90     -38.683  33.825 -29.729  1.00 90.93           C  
-ATOM   4541  CG  LYS B  90     -37.429  33.847 -30.586  1.00 83.12           C  
-ATOM   4542  CD  LYS B  90     -37.700  33.279 -31.968  1.00 82.17           C  
-ATOM   4543  CE  LYS B  90     -36.432  33.232 -32.802  1.00 64.94           C  
-ATOM   4544  NZ  LYS B  90     -36.682  32.668 -34.155  1.00 57.94           N  
-ATOM   4545  N   PHE B  91     -36.272  33.952 -27.385  1.00 87.14           N  
-ATOM   4546  CA  PHE B  91     -35.230  33.203 -26.692  1.00 89.86           C  
-ATOM   4547  C   PHE B  91     -34.964  33.717 -25.282  1.00 83.93           C  
-ATOM   4548  O   PHE B  91     -34.407  32.993 -24.456  1.00 74.71           O  
-ATOM   4549  CB  PHE B  91     -33.921  33.245 -27.483  1.00 87.93           C  
-ATOM   4550  CG  PHE B  91     -33.859  32.266 -28.618  1.00 92.09           C  
-ATOM   4551  CD1 PHE B  91     -33.877  30.901 -28.375  1.00 90.67           C  
-ATOM   4552  CD2 PHE B  91     -33.750  32.709 -29.925  1.00 80.54           C  
-ATOM   4553  CE1 PHE B  91     -33.809  29.997 -29.418  1.00 89.34           C  
-ATOM   4554  CE2 PHE B  91     -33.680  31.811 -30.972  1.00 72.51           C  
-ATOM   4555  CZ  PHE B  91     -33.709  30.453 -30.719  1.00 81.10           C  
-ATOM   4556  N   ARG B  92     -35.362  34.962 -25.019  1.00 85.29           N  
-ATOM   4557  CA  ARG B  92     -34.951  35.683 -23.811  1.00 82.37           C  
-ATOM   4558  C   ARG B  92     -35.084  34.872 -22.512  1.00 93.08           C  
-ATOM   4559  O   ARG B  92     -34.138  34.824 -21.726  1.00 98.06           O  
-ATOM   4560  CB  ARG B  92     -35.722  37.005 -23.692  1.00 74.46           C  
-ATOM   4561  CG  ARG B  92     -35.173  38.118 -24.578  1.00 78.33           C  
-ATOM   4562  CD  ARG B  92     -35.360  39.484 -23.934  1.00 78.86           C  
-ATOM   4563  NE  ARG B  92     -36.539  40.188 -24.430  1.00 89.47           N  
-ATOM   4564  CZ  ARG B  92     -36.493  41.334 -25.101  1.00 89.17           C  
-ATOM   4565  NH1 ARG B  92     -37.614  41.909 -25.518  1.00 78.80           N  
-ATOM   4566  NH2 ARG B  92     -35.324  41.910 -25.351  1.00 84.73           N  
-ATOM   4567  N   PRO B  93     -36.238  34.222 -22.278  1.00 86.63           N  
-ATOM   4568  CA  PRO B  93     -36.166  33.317 -21.126  1.00 72.33           C  
-ATOM   4569  C   PRO B  93     -35.392  32.052 -21.485  1.00 78.40           C  
-ATOM   4570  O   PRO B  93     -35.992  31.099 -21.987  1.00 78.89           O  
-ATOM   4571  CB  PRO B  93     -37.637  32.997 -20.824  1.00 71.23           C  
-ATOM   4572  CG  PRO B  93     -38.437  34.012 -21.598  1.00 89.53           C  
-ATOM   4573  CD  PRO B  93     -37.610  34.330 -22.802  1.00 86.65           C  
-ATOM   4574  N   LEU B  94     -34.081  32.057 -21.251  1.00 76.01           N  
-ATOM   4575  CA  LEU B  94     -33.233  30.906 -21.555  1.00 76.19           C  
-ATOM   4576  C   LEU B  94     -33.762  29.652 -20.868  1.00 71.73           C  
-ATOM   4577  O   LEU B  94     -33.543  29.446 -19.674  1.00 65.55           O  
-ATOM   4578  CB  LEU B  94     -31.784  31.178 -21.140  1.00 70.06           C  
-ATOM   4579  CG  LEU B  94     -30.981  32.047 -22.113  1.00 66.43           C  
-ATOM   4580  CD1 LEU B  94     -29.667  32.494 -21.492  1.00 60.78           C  
-ATOM   4581  CD2 LEU B  94     -30.732  31.299 -23.417  1.00 61.77           C  
-ATOM   4582  N   VAL B  95     -34.460  28.825 -21.641  1.00 73.80           N  
-ATOM   4583  CA  VAL B  95     -35.215  27.695 -21.107  1.00 78.23           C  
-ATOM   4584  C   VAL B  95     -34.356  26.662 -20.377  1.00 69.87           C  
-ATOM   4585  O   VAL B  95     -33.206  26.415 -20.750  1.00 54.52           O  
-ATOM   4586  CB  VAL B  95     -36.002  26.977 -22.228  1.00 77.90           C  
-ATOM   4587  CG1 VAL B  95     -37.079  27.895 -22.796  1.00 63.73           C  
-ATOM   4588  CG2 VAL B  95     -35.059  26.498 -23.326  1.00 62.13           C  
-ATOM   4589  N   ASP B  96     -34.943  26.080 -19.330  1.00 81.17           N  
-ATOM   4590  CA  ASP B  96     -34.315  25.051 -18.496  1.00 77.82           C  
-ATOM   4591  C   ASP B  96     -33.107  25.567 -17.713  1.00 71.15           C  
-ATOM   4592  O   ASP B  96     -32.248  24.788 -17.295  1.00 58.97           O  
-ATOM   4593  CB  ASP B  96     -33.912  23.845 -19.350  1.00 57.09           C  
-ATOM   4594  CG  ASP B  96     -35.049  23.348 -20.219  1.00 70.97           C  
-ATOM   4595  OD1 ASP B  96     -35.870  22.547 -19.723  1.00 73.06           O  
-ATOM   4596  OD2 ASP B  96     -35.126  23.763 -21.396  1.00 75.06           O  
-ATOM   4597  N   ARG B  97     -33.056  26.880 -17.506  1.00 57.65           N  
-ATOM   4598  CA  ARG B  97     -31.984  27.503 -16.738  1.00 53.51           C  
-ATOM   4599  C   ARG B  97     -32.499  28.729 -15.998  1.00 55.84           C  
-ATOM   4600  O   ARG B  97     -33.253  29.526 -16.555  1.00 53.27           O  
-ATOM   4601  CB  ARG B  97     -30.819  27.900 -17.647  1.00 62.74           C  
-ATOM   4602  CG  ARG B  97     -29.953  26.741 -18.114  1.00 64.49           C  
-ATOM   4603  CD  ARG B  97     -29.292  27.059 -19.441  1.00 54.63           C  
-ATOM   4604  NE  ARG B  97     -30.263  27.120 -20.527  1.00 61.07           N  
-ATOM   4605  CZ  ARG B  97     -30.002  27.610 -21.734  1.00 66.06           C  
-ATOM   4606  NH1 ARG B  97     -28.797  28.089 -22.009  1.00 62.45           N  
-ATOM   4607  NH2 ARG B  97     -30.947  27.626 -22.663  1.00 74.83           N  
-ATOM   4608  N   LEU B  98     -32.092  28.877 -14.742  1.00 56.64           N  
-ATOM   4609  CA  LEU B  98     -32.463  30.046 -13.952  1.00 63.11           C  
-ATOM   4610  C   LEU B  98     -31.765  31.279 -14.517  1.00 60.93           C  
-ATOM   4611  O   LEU B  98     -30.541  31.333 -14.565  1.00 59.91           O  
-ATOM   4612  CB  LEU B  98     -32.096  29.834 -12.477  1.00 67.05           C  
-ATOM   4613  CG  LEU B  98     -32.702  30.728 -11.388  1.00 68.52           C  
-ATOM   4614  CD1 LEU B  98     -31.954  32.048 -11.241  1.00 49.41           C  
-ATOM   4615  CD2 LEU B  98     -34.183  30.973 -11.652  1.00 66.60           C  
-ATOM   4616  N   ASN B  99     -32.542  32.267 -14.951  1.00 49.43           N  
-ATOM   4617  CA  ASN B  99     -31.963  33.478 -15.522  1.00 49.26           C  
-ATOM   4618  C   ASN B  99     -31.796  34.591 -14.491  1.00 52.27           C  
-ATOM   4619  O   ASN B  99     -32.656  34.789 -13.632  1.00 65.40           O  
-ATOM   4620  CB  ASN B  99     -32.815  33.980 -16.691  1.00 61.18           C  
-ATOM   4621  CG  ASN B  99     -32.680  33.108 -17.929  1.00 69.64           C  
-ATOM   4622  OD1 ASN B  99     -32.507  31.893 -17.832  1.00 59.64           O  
-ATOM   4623  ND2 ASN B  99     -32.750  33.731 -19.103  1.00 63.87           N  
-ATOM   4624  N   ILE B 100     -30.677  35.307 -14.577  1.00 52.97           N  
-ATOM   4625  CA  ILE B 100     -30.423  36.450 -13.704  1.00 62.78           C  
-ATOM   4626  C   ILE B 100     -29.871  37.644 -14.479  1.00 60.95           C  
-ATOM   4627  O   ILE B 100     -28.688  37.684 -14.816  1.00 58.99           O  
-ATOM   4628  CB  ILE B 100     -29.427  36.103 -12.573  1.00 60.27           C  
-ATOM   4629  CG1 ILE B 100     -29.980  34.992 -11.682  1.00 60.04           C  
-ATOM   4630  CG2 ILE B 100     -29.125  37.334 -11.727  1.00 51.97           C  
-ATOM   4631  CD1 ILE B 100     -29.071  34.631 -10.528  1.00 69.17           C  
-ATOM   4632  N   VAL B 101     -30.731  38.614 -14.764  1.00 52.76           N  
-ATOM   4633  CA  VAL B 101     -30.286  39.872 -15.347  1.00 55.39           C  
-ATOM   4634  C   VAL B 101     -29.814  40.783 -14.225  1.00 54.32           C  
-ATOM   4635  O   VAL B 101     -30.422  40.815 -13.158  1.00 59.62           O  
-ATOM   4636  CB  VAL B 101     -31.409  40.562 -16.145  1.00 61.28           C  
-ATOM   4637  CG1 VAL B 101     -30.922  41.877 -16.743  1.00 73.95           C  
-ATOM   4638  CG2 VAL B 101     -31.915  39.643 -17.232  1.00 58.69           C  
-ATOM   4639  N   VAL B 102     -28.726  41.512 -14.444  1.00 57.58           N  
-ATOM   4640  CA  VAL B 102     -28.296  42.475 -13.440  1.00 59.30           C  
-ATOM   4641  C   VAL B 102     -28.358  43.908 -13.971  1.00 73.22           C  
-ATOM   4642  O   VAL B 102     -27.840  44.216 -15.046  1.00 85.53           O  
-ATOM   4643  CB  VAL B 102     -26.875  42.157 -12.925  1.00 57.78           C  
-ATOM   4644  CG1 VAL B 102     -26.885  40.849 -12.145  1.00 57.63           C  
-ATOM   4645  CG2 VAL B 102     -25.883  42.090 -14.072  1.00 71.13           C  
-ATOM   4646  N   SER B 103     -29.017  44.775 -13.208  1.00 77.64           N  
-ATOM   4647  CA  SER B 103     -29.169  46.179 -13.576  1.00 93.36           C  
-ATOM   4648  C   SER B 103     -29.662  46.996 -12.387  1.00 88.56           C  
-ATOM   4649  O   SER B 103     -29.490  46.605 -11.234  1.00 78.14           O  
-ATOM   4650  CB  SER B 103     -30.138  46.329 -14.754  1.00 85.88           C  
-ATOM   4651  OG  SER B 103     -30.364  47.690 -15.067  1.00 82.59           O  
-ATOM   4652  N   SER B 104     -30.273  48.138 -12.677  1.00 89.99           N  
-ATOM   4653  CA  SER B 104     -30.872  48.972 -11.644  1.00 84.05           C  
-ATOM   4654  C   SER B 104     -32.079  49.709 -12.205  1.00 88.25           C  
-ATOM   4655  O   SER B 104     -32.623  50.608 -11.566  1.00 90.67           O  
-ATOM   4656  CB  SER B 104     -29.848  49.967 -11.088  1.00 85.67           C  
-ATOM   4657  OG  SER B 104     -29.364  50.828 -12.105  1.00 78.83           O  
-ATOM   4658  N   SER B 105     -32.498  49.314 -13.402  1.00 84.37           N  
-ATOM   4659  CA  SER B 105     -33.564  50.019 -14.102  1.00 90.51           C  
-ATOM   4660  C   SER B 105     -34.771  49.133 -14.419  1.00 83.22           C  
-ATOM   4661  O   SER B 105     -35.912  49.594 -14.383  1.00 89.71           O  
-ATOM   4662  CB  SER B 105     -33.019  50.630 -15.397  1.00 91.49           C  
-ATOM   4663  OG  SER B 105     -31.958  51.535 -15.133  1.00 83.95           O  
-ATOM   4664  N   LEU B 106     -34.521  47.862 -14.718  1.00 70.01           N  
-ATOM   4665  CA  LEU B 106     -35.562  46.997 -15.271  1.00 71.91           C  
-ATOM   4666  C   LEU B 106     -36.434  46.298 -14.229  1.00 67.96           C  
-ATOM   4667  O   LEU B 106     -36.182  46.376 -13.027  1.00 68.13           O  
-ATOM   4668  CB  LEU B 106     -34.928  45.948 -16.186  1.00 79.98           C  
-ATOM   4669  CG  LEU B 106     -34.107  46.515 -17.346  1.00 97.46           C  
-ATOM   4670  CD1 LEU B 106     -33.744  45.417 -18.334  1.00 80.77           C  
-ATOM   4671  CD2 LEU B 106     -34.850  47.650 -18.041  1.00 93.42           C  
-ATOM   4672  N   LYS B 107     -37.461  45.609 -14.723  1.00 68.12           N  
-ATOM   4673  CA  LYS B 107     -38.452  44.940 -13.885  1.00 65.96           C  
-ATOM   4674  C   LYS B 107     -37.824  43.856 -13.013  1.00 57.97           C  
-ATOM   4675  O   LYS B 107     -38.450  42.834 -12.725  1.00 48.27           O  
-ATOM   4676  CB  LYS B 107     -39.555  44.331 -14.759  1.00 60.66           C  
-ATOM   4677  CG  LYS B 107     -40.931  44.308 -14.112  1.00 62.83           C  
-ATOM   4678  CD  LYS B 107     -41.816  43.240 -14.734  1.00 58.68           C  
-ATOM   4679  CE  LYS B 107     -41.943  42.032 -13.816  1.00 60.91           C  
-ATOM   4680  NZ  LYS B 107     -40.620  41.543 -13.330  1.00 41.43           N  
-ATOM   4681  N   VAL B 126     -33.500  39.281 -10.918  1.00 28.11           N  
-ATOM   4682  CA  VAL B 126     -32.959  40.585 -11.287  1.00 54.12           C  
-ATOM   4683  C   VAL B 126     -32.271  41.253 -10.101  1.00 48.76           C  
-ATOM   4684  O   VAL B 126     -32.927  41.786  -9.206  1.00 56.97           O  
-ATOM   4685  CB  VAL B 126     -34.057  41.518 -11.828  1.00 49.92           C  
-ATOM   4686  CG1 VAL B 126     -33.464  42.866 -12.230  1.00 32.53           C  
-ATOM   4687  CG2 VAL B 126     -34.765  40.867 -13.005  1.00 43.78           C  
-ATOM   4688  N   CYS B 127     -30.942  41.224 -10.106  1.00 42.48           N  
-ATOM   4689  CA  CYS B 127     -30.155  41.769  -9.007  1.00 48.82           C  
-ATOM   4690  C   CYS B 127     -29.480  43.078  -9.405  1.00 61.95           C  
-ATOM   4691  O   CYS B 127     -29.451  43.435 -10.582  1.00 71.07           O  
-ATOM   4692  CB  CYS B 127     -29.118  40.746  -8.553  1.00 56.21           C  
-ATOM   4693  SG  CYS B 127     -29.830  39.109  -8.269  1.00 75.26           S  
-ATOM   4694  N   ALA B 128     -28.942  43.791  -8.419  1.00 57.93           N  
-ATOM   4695  CA  ALA B 128     -28.383  45.119  -8.653  1.00 71.08           C  
-ATOM   4696  C   ALA B 128     -26.870  45.086  -8.849  1.00 74.04           C  
-ATOM   4697  O   ALA B 128     -26.249  46.110  -9.141  1.00 65.33           O  
-ATOM   4698  CB  ALA B 128     -28.744  46.049  -7.504  1.00 78.12           C  
-ATOM   4699  N   SER B 129     -26.285  43.906  -8.681  1.00 77.09           N  
-ATOM   4700  CA  SER B 129     -24.859  43.714  -8.903  1.00 77.40           C  
-ATOM   4701  C   SER B 129     -24.561  42.228  -9.011  1.00 76.38           C  
-ATOM   4702  O   SER B 129     -25.413  41.394  -8.708  1.00 70.77           O  
-ATOM   4703  CB  SER B 129     -24.035  44.337  -7.775  1.00 74.63           C  
-ATOM   4704  OG  SER B 129     -24.215  43.623  -6.566  1.00 74.78           O  
-ATOM   4705  N   LEU B 130     -23.351  41.901  -9.447  1.00 70.30           N  
-ATOM   4706  CA  LEU B 130     -22.922  40.510  -9.525  1.00 69.65           C  
-ATOM   4707  C   LEU B 130     -22.794  39.856  -8.142  1.00 75.67           C  
-ATOM   4708  O   LEU B 130     -23.240  38.718  -7.967  1.00 69.67           O  
-ATOM   4709  CB  LEU B 130     -21.600  40.399 -10.287  1.00 69.50           C  
-ATOM   4710  CG  LEU B 130     -21.076  38.981 -10.510  1.00 58.68           C  
-ATOM   4711  CD1 LEU B 130     -22.096  38.141 -11.261  1.00 55.88           C  
-ATOM   4712  CD2 LEU B 130     -19.766  39.031 -11.263  1.00 61.77           C  
-ATOM   4713  N   PRO B 131     -22.182  40.555  -7.158  1.00 81.57           N  
-ATOM   4714  CA  PRO B 131     -22.182  39.951  -5.820  1.00 76.50           C  
-ATOM   4715  C   PRO B 131     -23.590  39.691  -5.294  1.00 76.08           C  
-ATOM   4716  O   PRO B 131     -23.822  38.665  -4.653  1.00 71.09           O  
-ATOM   4717  CB  PRO B 131     -21.468  40.999  -4.961  1.00 71.97           C  
-ATOM   4718  CG  PRO B 131     -20.597  41.714  -5.901  1.00 65.95           C  
-ATOM   4719  CD  PRO B 131     -21.355  41.778  -7.191  1.00 67.62           C  
-ATOM   4720  N   ALA B 132     -24.508  40.615  -5.560  1.00 75.68           N  
-ATOM   4721  CA  ALA B 132     -25.899  40.433  -5.174  1.00 77.58           C  
-ATOM   4722  C   ALA B 132     -26.487  39.222  -5.886  1.00 75.68           C  
-ATOM   4723  O   ALA B 132     -27.250  38.457  -5.302  1.00 68.74           O  
-ATOM   4724  CB  ALA B 132     -26.708  41.686  -5.485  1.00 64.74           C  
-ATOM   4725  N   ALA B 133     -26.114  39.055  -7.150  1.00 80.73           N  
-ATOM   4726  CA  ALA B 133     -26.578  37.932  -7.953  1.00 78.85           C  
-ATOM   4727  C   ALA B 133     -26.107  36.615  -7.364  1.00 78.39           C  
-ATOM   4728  O   ALA B 133     -26.825  35.617  -7.407  1.00 70.66           O  
-ATOM   4729  CB  ALA B 133     -26.101  38.069  -9.390  1.00 78.95           C  
-ATOM   4730  N   LEU B 134     -24.898  36.617  -6.815  1.00 75.83           N  
-ATOM   4731  CA  LEU B 134     -24.360  35.423  -6.184  1.00 73.05           C  
-ATOM   4732  C   LEU B 134     -25.055  35.164  -4.851  1.00 77.01           C  
-ATOM   4733  O   LEU B 134     -25.357  34.021  -4.505  1.00 70.97           O  
-ATOM   4734  CB  LEU B 134     -22.852  35.564  -5.991  1.00 73.29           C  
-ATOM   4735  CG  LEU B 134     -22.050  35.751  -7.282  1.00 59.05           C  
-ATOM   4736  CD1 LEU B 134     -20.565  35.877  -6.983  1.00 54.50           C  
-ATOM   4737  CD2 LEU B 134     -22.314  34.603  -8.238  1.00 53.56           C  
-ATOM   4738  N   SER B 135     -25.308  36.238  -4.109  1.00 77.23           N  
-ATOM   4739  CA  SER B 135     -25.999  36.149  -2.829  1.00 76.31           C  
-ATOM   4740  C   SER B 135     -27.394  35.560  -3.004  1.00 78.26           C  
-ATOM   4741  O   SER B 135     -27.837  34.743  -2.200  1.00 80.31           O  
-ATOM   4742  CB  SER B 135     -26.089  37.526  -2.169  1.00 70.22           C  
-ATOM   4743  OG  SER B 135     -24.800  38.063  -1.917  1.00 65.58           O  
-ATOM   4744  N   LEU B 136     -28.075  35.978  -4.068  1.00 75.85           N  
-ATOM   4745  CA  LEU B 136     -29.406  35.474  -4.393  1.00 86.36           C  
-ATOM   4746  C   LEU B 136     -29.353  33.992  -4.752  1.00 83.29           C  
-ATOM   4747  O   LEU B 136     -30.356  33.282  -4.665  1.00 72.82           O  
-ATOM   4748  CB  LEU B 136     -30.016  36.279  -5.546  1.00 85.32           C  
-ATOM   4749  CG  LEU B 136     -31.005  37.390  -5.183  1.00 90.31           C  
-ATOM   4750  CD1 LEU B 136     -32.389  36.821  -4.899  1.00 77.85           C  
-ATOM   4751  CD2 LEU B 136     -30.503  38.189  -3.989  1.00 90.23           C  
-ATOM   4752  N   LEU B 137     -28.173  33.535  -5.156  1.00 85.78           N  
-ATOM   4753  CA  LEU B 137     -27.969  32.134  -5.496  1.00 85.06           C  
-ATOM   4754  C   LEU B 137     -27.599  31.318  -4.263  1.00 80.91           C  
-ATOM   4755  O   LEU B 137     -27.847  30.115  -4.213  1.00 70.99           O  
-ATOM   4756  CB  LEU B 137     -26.885  31.993  -6.567  1.00 94.58           C  
-ATOM   4757  CG  LEU B 137     -27.236  32.432  -7.991  1.00 91.67           C  
-ATOM   4758  CD1 LEU B 137     -26.008  32.352  -8.883  1.00 85.63           C  
-ATOM   4759  CD2 LEU B 137     -28.373  31.591  -8.562  1.00 88.91           C  
-ATOM   4760  N   GLU B 138     -27.006  31.972  -3.270  1.00 89.54           N  
-ATOM   4761  CA  GLU B 138     -26.606  31.284  -2.049  1.00 91.02           C  
-ATOM   4762  C   GLU B 138     -27.764  31.157  -1.068  1.00 92.85           C  
-ATOM   4763  O   GLU B 138     -28.005  30.079  -0.524  1.00 85.97           O  
-ATOM   4764  CB  GLU B 138     -25.439  32.008  -1.384  1.00 81.99           C  
-ATOM   4765  CG  GLU B 138     -24.156  31.194  -1.353  1.00 85.45           C  
-ATOM   4766  CD  GLU B 138     -22.977  31.987  -0.824  1.00 96.25           C  
-ATOM   4767  OE1 GLU B 138     -23.095  32.569   0.274  1.00 93.96           O  
-ATOM   4768  OE2 GLU B 138     -21.935  32.037  -1.510  1.00 90.29           O  
-ATOM   4769  N   GLU B 139     -28.470  32.262  -0.838  1.00 90.65           N  
-ATOM   4770  CA  GLU B 139     -29.612  32.260   0.073  1.00 89.11           C  
-ATOM   4771  C   GLU B 139     -30.672  31.279  -0.411  1.00 94.33           C  
-ATOM   4772  O   GLU B 139     -30.819  30.192   0.146  1.00 90.20           O  
-ATOM   4773  CB  GLU B 139     -30.210  33.662   0.215  1.00 79.84           C  
-ATOM   4774  CG  GLU B 139     -31.511  33.707   1.022  1.00 94.40           C  
-ATOM   4775  CD  GLU B 139     -31.307  33.504   2.517  1.00104.95           C  
-ATOM   4776  OE1 GLU B 139     -31.539  34.469   3.275  1.00 97.31           O  
-ATOM   4777  OE2 GLU B 139     -30.935  32.386   2.940  1.00 97.97           O  
-ATOM   4778  N   GLU B 140     -31.409  31.662  -1.447  1.00 92.49           N  
-ATOM   4779  CA  GLU B 140     -32.360  30.750  -2.064  1.00 76.33           C  
-ATOM   4780  C   GLU B 140     -31.690  30.035  -3.225  1.00 91.06           C  
-ATOM   4781  O   GLU B 140     -30.546  30.339  -3.569  1.00 89.42           O  
-ATOM   4782  CB  GLU B 140     -33.612  31.488  -2.533  1.00 62.50           C  
-ATOM   4783  CG  GLU B 140     -33.333  32.793  -3.249  1.00 76.21           C  
-ATOM   4784  CD  GLU B 140     -34.076  33.958  -2.627  1.00 77.58           C  
-ATOM   4785  OE1 GLU B 140     -33.444  34.728  -1.872  1.00 79.53           O  
-ATOM   4786  OE2 GLU B 140     -35.290  34.103  -2.886  1.00 60.23           O  
-ATOM   4787  N   TYR B 141     -32.407  29.079  -3.812  1.00 91.55           N  
-ATOM   4788  CA  TYR B 141     -31.887  28.214  -4.870  1.00 76.29           C  
-ATOM   4789  C   TYR B 141     -30.703  27.364  -4.417  1.00 83.78           C  
-ATOM   4790  O   TYR B 141     -30.083  26.700  -5.243  1.00 84.17           O  
-ATOM   4791  CB  TYR B 141     -31.449  29.020  -6.098  1.00 70.11           C  
-ATOM   4792  CG  TYR B 141     -32.448  30.014  -6.631  1.00 71.37           C  
-ATOM   4793  CD1 TYR B 141     -33.481  29.613  -7.467  1.00 60.53           C  
-ATOM   4794  CD2 TYR B 141     -32.335  31.365  -6.329  1.00 79.21           C  
-ATOM   4795  CE1 TYR B 141     -34.388  30.529  -7.969  1.00 59.04           C  
-ATOM   4796  CE2 TYR B 141     -33.234  32.287  -6.824  1.00 66.84           C  
-ATOM   4797  CZ  TYR B 141     -34.258  31.865  -7.644  1.00 60.91           C  
-ATOM   4798  OH  TYR B 141     -35.154  32.785  -8.138  1.00 49.25           O  
-ATOM   4799  N   LYS B 142     -30.382  27.387  -3.123  1.00 88.00           N  
-ATOM   4800  CA  LYS B 142     -29.232  26.646  -2.604  1.00 87.92           C  
-ATOM   4801  C   LYS B 142     -29.332  25.178  -2.997  1.00 83.19           C  
-ATOM   4802  O   LYS B 142     -28.331  24.529  -3.304  1.00 69.13           O  
-ATOM   4803  CB  LYS B 142     -29.131  26.779  -1.084  1.00 86.94           C  
-ATOM   4804  CG  LYS B 142     -27.936  26.051  -0.484  1.00 86.20           C  
-ATOM   4805  CD  LYS B 142     -26.633  26.788  -0.772  1.00 92.19           C  
-ATOM   4806  CE  LYS B 142     -25.433  25.861  -0.632  1.00 75.60           C  
-ATOM   4807  NZ  LYS B 142     -25.446  25.114   0.656  1.00 58.10           N  
-ATOM   4808  N   ASP B 143     -30.557  24.668  -2.987  1.00 91.26           N  
-ATOM   4809  CA  ASP B 143     -30.850  23.374  -3.577  1.00 91.95           C  
-ATOM   4810  C   ASP B 143     -31.386  23.609  -4.985  1.00 94.77           C  
-ATOM   4811  O   ASP B 143     -31.953  24.669  -5.262  1.00 91.21           O  
-ATOM   4812  CB  ASP B 143     -31.855  22.597  -2.727  1.00 92.58           C  
-ATOM   4813  CG  ASP B 143     -31.462  22.549  -1.261  1.00 92.29           C  
-ATOM   4814  OD1 ASP B 143     -30.828  23.514  -0.784  1.00 90.50           O  
-ATOM   4815  OD2 ASP B 143     -31.789  21.551  -0.584  1.00 84.51           O  
-ATOM   4816  N   SER B 144     -31.168  22.619  -5.852  1.00 97.54           N  
-ATOM   4817  CA  SER B 144     -31.599  22.587  -7.259  1.00 94.65           C  
-ATOM   4818  C   SER B 144     -30.635  23.289  -8.219  1.00 86.17           C  
-ATOM   4819  O   SER B 144     -30.652  23.005  -9.418  1.00 87.63           O  
-ATOM   4820  CB  SER B 144     -33.005  23.174  -7.435  1.00 92.11           C  
-ATOM   4821  OG  SER B 144     -33.947  22.493  -6.624  1.00100.29           O  
-ATOM   4822  N   VAL B 145     -29.798  24.197  -7.721  1.00 82.33           N  
-ATOM   4823  CA  VAL B 145     -28.795  24.797  -8.597  1.00 75.70           C  
-ATOM   4824  C   VAL B 145     -27.516  23.960  -8.544  1.00 83.92           C  
-ATOM   4825  O   VAL B 145     -27.106  23.484  -7.483  1.00 97.78           O  
-ATOM   4826  CB  VAL B 145     -28.500  26.285  -8.246  1.00 70.35           C  
-ATOM   4827  CG1 VAL B 145     -27.579  26.414  -7.040  1.00 75.51           C  
-ATOM   4828  CG2 VAL B 145     -27.889  26.992  -9.445  1.00 71.78           C  
-ATOM   4829  N   ASP B 146     -26.915  23.748  -9.709  1.00 71.04           N  
-ATOM   4830  CA  ASP B 146     -25.709  22.937  -9.820  1.00 66.00           C  
-ATOM   4831  C   ASP B 146     -24.475  23.829  -9.827  1.00 64.41           C  
-ATOM   4832  O   ASP B 146     -23.833  24.037  -8.798  1.00 63.48           O  
-ATOM   4833  CB  ASP B 146     -25.757  22.079 -11.090  1.00 65.07           C  
-ATOM   4834  CG  ASP B 146     -24.469  21.308 -11.330  1.00 70.81           C  
-ATOM   4835  OD1 ASP B 146     -23.782  20.958 -10.346  1.00 66.21           O  
-ATOM   4836  OD2 ASP B 146     -24.145  21.052 -12.510  1.00 69.10           O  
-ATOM   4837  N   GLN B 147     -24.154  24.346 -11.005  1.00 67.43           N  
-ATOM   4838  CA  GLN B 147     -23.058  25.283 -11.178  1.00 61.11           C  
-ATOM   4839  C   GLN B 147     -23.603  26.535 -11.843  1.00 59.04           C  
-ATOM   4840  O   GLN B 147     -24.672  26.502 -12.452  1.00 53.31           O  
-ATOM   4841  CB  GLN B 147     -21.942  24.662 -12.017  1.00 62.74           C  
-ATOM   4842  CG  GLN B 147     -22.459  23.828 -13.177  1.00 58.23           C  
-ATOM   4843  CD  GLN B 147     -21.376  23.463 -14.169  1.00 46.36           C  
-ATOM   4844  OE1 GLN B 147     -20.186  23.588 -13.884  1.00 45.65           O  
-ATOM   4845  NE2 GLN B 147     -21.785  23.016 -15.349  1.00 52.19           N  
-ATOM   4846  N   ILE B 148     -22.878  27.640 -11.732  1.00 57.25           N  
-ATOM   4847  CA  ILE B 148     -23.360  28.880 -12.317  1.00 56.67           C  
-ATOM   4848  C   ILE B 148     -22.541  29.272 -13.541  1.00 61.52           C  
-ATOM   4849  O   ILE B 148     -21.432  28.776 -13.753  1.00 64.84           O  
-ATOM   4850  CB  ILE B 148     -23.349  30.037 -11.293  1.00 58.52           C  
-ATOM   4851  CG1 ILE B 148     -22.073  30.873 -11.409  1.00 58.67           C  
-ATOM   4852  CG2 ILE B 148     -23.536  29.503  -9.878  1.00 43.10           C  
-ATOM   4853  CD1 ILE B 148     -22.279  32.319 -11.026  1.00 63.90           C  
-ATOM   4854  N   PHE B 149     -23.113  30.152 -14.354  1.00 60.01           N  
-ATOM   4855  CA  PHE B 149     -22.443  30.666 -15.536  1.00 50.35           C  
-ATOM   4856  C   PHE B 149     -22.638  32.174 -15.646  1.00 54.90           C  
-ATOM   4857  O   PHE B 149     -23.618  32.721 -15.140  1.00 58.53           O  
-ATOM   4858  CB  PHE B 149     -22.968  29.978 -16.797  1.00 47.56           C  
-ATOM   4859  CG  PHE B 149     -22.612  28.522 -16.894  1.00 49.10           C  
-ATOM   4860  CD1 PHE B 149     -21.312  28.131 -17.159  1.00 50.66           C  
-ATOM   4861  CD2 PHE B 149     -23.583  27.544 -16.744  1.00 55.61           C  
-ATOM   4862  CE1 PHE B 149     -20.981  26.793 -17.259  1.00 54.88           C  
-ATOM   4863  CE2 PHE B 149     -23.257  26.203 -16.843  1.00 47.99           C  
-ATOM   4864  CZ  PHE B 149     -21.956  25.828 -17.101  1.00 44.98           C  
-ATOM   4865  N   VAL B 150     -21.694  32.844 -16.298  1.00 55.90           N  
-ATOM   4866  CA  VAL B 150     -21.840  34.259 -16.617  1.00 52.24           C  
-ATOM   4867  C   VAL B 150     -21.668  34.454 -18.122  1.00 47.76           C  
-ATOM   4868  O   VAL B 150     -20.645  34.076 -18.694  1.00 48.55           O  
-ATOM   4869  CB  VAL B 150     -20.829  35.130 -15.853  1.00 44.73           C  
-ATOM   4870  CG1 VAL B 150     -21.014  36.597 -16.212  1.00 39.60           C  
-ATOM   4871  CG2 VAL B 150     -20.976  34.922 -14.352  1.00 47.63           C  
-ATOM   4872  N   VAL B 151     -22.678  35.039 -18.760  1.00 44.97           N  
-ATOM   4873  CA  VAL B 151     -22.725  35.109 -20.217  1.00 35.16           C  
-ATOM   4874  C   VAL B 151     -22.900  36.533 -20.747  1.00 29.63           C  
-ATOM   4875  O   VAL B 151     -22.447  37.503 -20.136  1.00 23.72           O  
-ATOM   4876  CB  VAL B 151     -23.868  34.237 -20.762  1.00 37.29           C  
-ATOM   4877  CG1 VAL B 151     -23.777  32.834 -20.187  1.00 34.16           C  
-ATOM   4878  CG2 VAL B 151     -25.210  34.856 -20.418  1.00 41.15           C  
-ATOM   4879  N   GLY B 153     -22.417  40.059 -20.448  1.00 31.01           N  
-ATOM   4880  CA  GLY B 153     -21.572  40.833 -21.341  1.00 52.43           C  
-ATOM   4881  C   GLY B 153     -20.374  41.428 -20.624  1.00 56.36           C  
-ATOM   4882  O   GLY B 153     -20.129  41.112 -19.461  1.00 50.57           O  
-ATOM   4883  N   ALA B 154     -19.625  42.286 -21.313  1.00 55.29           N  
-ATOM   4884  CA  ALA B 154     -18.457  42.929 -20.714  1.00 47.67           C  
-ATOM   4885  C   ALA B 154     -18.886  43.797 -19.545  1.00 60.60           C  
-ATOM   4886  O   ALA B 154     -20.018  44.277 -19.499  1.00 68.28           O  
-ATOM   4887  CB  ALA B 154     -17.706  43.754 -21.739  1.00 43.26           C  
-ATOM   4888  N   GLY B 155     -17.983  43.999 -18.596  1.00 60.83           N  
-ATOM   4889  CA  GLY B 155     -18.353  44.678 -17.373  1.00 70.30           C  
-ATOM   4890  C   GLY B 155     -18.799  43.659 -16.347  1.00 58.68           C  
-ATOM   4891  O   GLY B 155     -18.419  43.734 -15.185  1.00 67.59           O  
-ATOM   4892  N   LEU B 156     -19.617  42.706 -16.779  1.00 50.61           N  
-ATOM   4893  CA  LEU B 156     -19.979  41.581 -15.933  1.00 57.54           C  
-ATOM   4894  C   LEU B 156     -18.805  40.616 -15.881  1.00 59.26           C  
-ATOM   4895  O   LEU B 156     -18.477  40.072 -14.829  1.00 62.54           O  
-ATOM   4896  CB  LEU B 156     -21.234  40.882 -16.453  1.00 49.49           C  
-ATOM   4897  CG  LEU B 156     -22.043  40.186 -15.360  1.00 50.75           C  
-ATOM   4898  CD1 LEU B 156     -22.435  41.208 -14.311  1.00 57.39           C  
-ATOM   4899  CD2 LEU B 156     -23.269  39.509 -15.943  1.00 41.65           C  
-ATOM   4900  N   TYR B 157     -18.180  40.414 -17.037  1.00 50.66           N  
-ATOM   4901  CA  TYR B 157     -16.953  39.634 -17.132  1.00 43.08           C  
-ATOM   4902  C   TYR B 157     -15.856  40.263 -16.287  1.00 49.88           C  
-ATOM   4903  O   TYR B 157     -15.174  39.574 -15.531  1.00 55.90           O  
-ATOM   4904  CB  TYR B 157     -16.489  39.522 -18.588  1.00 45.72           C  
-ATOM   4905  CG  TYR B 157     -17.412  38.719 -19.479  1.00 46.08           C  
-ATOM   4906  CD1 TYR B 157     -17.961  37.519 -19.045  1.00 43.72           C  
-ATOM   4907  CD2 TYR B 157     -17.734  39.163 -20.755  1.00 45.45           C  
-ATOM   4908  CE1 TYR B 157     -18.800  36.783 -19.858  1.00 38.92           C  
-ATOM   4909  CE2 TYR B 157     -18.574  38.435 -21.574  1.00 36.16           C  
-ATOM   4910  CZ  TYR B 157     -19.107  37.249 -21.119  1.00 36.99           C  
-ATOM   4911  OH  TYR B 157     -19.942  36.517 -21.930  1.00 37.11           O  
-ATOM   4912  N   GLU B 158     -15.690  41.577 -16.418  1.00 50.94           N  
-ATOM   4913  CA  GLU B 158     -14.634  42.282 -15.699  1.00 63.31           C  
-ATOM   4914  C   GLU B 158     -14.955  42.362 -14.211  1.00 65.69           C  
-ATOM   4915  O   GLU B 158     -14.050  42.451 -13.379  1.00 61.10           O  
-ATOM   4916  CB  GLU B 158     -14.418  43.686 -16.276  1.00 65.31           C  
-ATOM   4917  CG  GLU B 158     -15.345  44.758 -15.735  1.00 75.91           C  
-ATOM   4918  CD  GLU B 158     -15.301  46.032 -16.559  1.00 83.24           C  
-ATOM   4919  OE1 GLU B 158     -14.415  46.144 -17.432  1.00 83.48           O  
-ATOM   4920  OE2 GLU B 158     -16.156  46.917 -16.340  1.00 71.69           O  
-ATOM   4921  N   ALA B 159     -16.242  42.329 -13.881  1.00 56.33           N  
-ATOM   4922  CA  ALA B 159     -16.662  42.296 -12.488  1.00 50.53           C  
-ATOM   4923  C   ALA B 159     -16.286  40.959 -11.886  1.00 55.89           C  
-ATOM   4924  O   ALA B 159     -15.709  40.893 -10.804  1.00 70.37           O  
-ATOM   4925  CB  ALA B 159     -18.157  42.530 -12.364  1.00 52.30           C  
-ATOM   4926  N   ALA B 160     -16.617  39.896 -12.612  1.00 49.43           N  
-ATOM   4927  CA  ALA B 160     -16.329  38.532 -12.192  1.00 43.60           C  
-ATOM   4928  C   ALA B 160     -14.830  38.287 -12.074  1.00 51.82           C  
-ATOM   4929  O   ALA B 160     -14.382  37.506 -11.234  1.00 46.03           O  
-ATOM   4930  CB  ALA B 160     -16.947  37.545 -13.165  1.00 42.62           C  
-ATOM   4931  N   LEU B 161     -14.059  38.959 -12.921  1.00 55.99           N  
-ATOM   4932  CA  LEU B 161     -12.610  38.805 -12.918  1.00 48.92           C  
-ATOM   4933  C   LEU B 161     -11.955  39.604 -11.797  1.00 53.53           C  
-ATOM   4934  O   LEU B 161     -11.068  39.100 -11.108  1.00 60.76           O  
-ATOM   4935  CB  LEU B 161     -12.030  39.220 -14.270  1.00 54.16           C  
-ATOM   4936  CG  LEU B 161     -12.224  38.212 -15.405  1.00 42.49           C  
-ATOM   4937  CD1 LEU B 161     -11.688  38.760 -16.719  1.00 38.66           C  
-ATOM   4938  CD2 LEU B 161     -11.559  36.889 -15.060  1.00 37.06           C  
-ATOM   4939  N   SER B 162     -12.389  40.849 -11.618  1.00 50.65           N  
-ATOM   4940  CA  SER B 162     -11.843  41.694 -10.561  1.00 49.19           C  
-ATOM   4941  C   SER B 162     -12.199  41.138  -9.186  1.00 50.17           C  
-ATOM   4942  O   SER B 162     -11.397  41.200  -8.255  1.00 66.42           O  
-ATOM   4943  CB  SER B 162     -12.349  43.131 -10.699  1.00 50.84           C  
-ATOM   4944  OG  SER B 162     -13.756  43.191 -10.552  1.00 66.17           O  
-ATOM   4945  N   LEU B 163     -13.404  40.589  -9.069  1.00 44.12           N  
-ATOM   4946  CA  LEU B 163     -13.845  39.960  -7.827  1.00 43.76           C  
-ATOM   4947  C   LEU B 163     -13.261  38.559  -7.698  1.00 50.21           C  
-ATOM   4948  O   LEU B 163     -13.472  37.880  -6.692  1.00 52.03           O  
-ATOM   4949  CB  LEU B 163     -15.374  39.906  -7.760  1.00 45.78           C  
-ATOM   4950  CG  LEU B 163     -16.095  41.255  -7.695  1.00 58.82           C  
-ATOM   4951  CD1 LEU B 163     -17.593  41.077  -7.902  1.00 62.11           C  
-ATOM   4952  CD2 LEU B 163     -15.812  41.958  -6.376  1.00 66.12           C  
-ATOM   4953  N   GLY B 164     -12.538  38.134  -8.732  1.00 52.94           N  
-ATOM   4954  CA  GLY B 164     -11.807  36.878  -8.723  1.00 50.67           C  
-ATOM   4955  C   GLY B 164     -12.614  35.658  -8.328  1.00 52.07           C  
-ATOM   4956  O   GLY B 164     -12.173  34.860  -7.501  1.00 59.38           O  
-ATOM   4957  N   VAL B 165     -13.794  35.506  -8.919  1.00 50.15           N  
-ATOM   4958  CA  VAL B 165     -14.669  34.387  -8.585  1.00 58.51           C  
-ATOM   4959  C   VAL B 165     -14.756  33.367  -9.719  1.00 62.00           C  
-ATOM   4960  O   VAL B 165     -15.208  32.240  -9.516  1.00 68.21           O  
-ATOM   4961  CB  VAL B 165     -16.085  34.873  -8.233  1.00 50.49           C  
-ATOM   4962  CG1 VAL B 165     -16.064  35.643  -6.922  1.00 51.88           C  
-ATOM   4963  CG2 VAL B 165     -16.647  35.731  -9.355  1.00 46.16           C  
-ATOM   4964  N   ALA B 166     -14.321  33.765 -10.910  1.00 55.93           N  
-ATOM   4965  CA  ALA B 166     -14.348  32.880 -12.068  1.00 46.78           C  
-ATOM   4966  C   ALA B 166     -13.181  31.898 -12.027  1.00 55.72           C  
-ATOM   4967  O   ALA B 166     -12.021  32.297 -12.129  1.00 63.72           O  
-ATOM   4968  CB  ALA B 166     -14.319  33.689 -13.352  1.00 47.35           C  
-ATOM   4969  N   SER B 167     -13.495  30.615 -11.877  1.00 48.76           N  
-ATOM   4970  CA  SER B 167     -12.473  29.577 -11.789  1.00 50.72           C  
-ATOM   4971  C   SER B 167     -12.110  29.026 -13.165  1.00 48.09           C  
-ATOM   4972  O   SER B 167     -10.941  28.718 -13.437  1.00 50.37           O  
-ATOM   4973  CB  SER B 167     -12.947  28.441 -10.883  1.00 56.38           C  
-ATOM   4974  OG  SER B 167     -14.171  27.899 -11.349  1.00 58.78           O  
-ATOM   4975  N   HIS B 168     -13.120  28.907 -14.023  1.00 47.05           N  
-ATOM   4976  CA  HIS B 168     -12.942  28.373 -15.369  1.00 41.13           C  
-ATOM   4977  C   HIS B 168     -13.456  29.323 -16.446  1.00 38.22           C  
-ATOM   4978  O   HIS B 168     -14.402  30.076 -16.220  1.00 46.05           O  
-ATOM   4979  CB  HIS B 168     -13.650  27.025 -15.507  1.00 38.37           C  
-ATOM   4980  CG  HIS B 168     -13.290  26.042 -14.440  1.00 46.90           C  
-ATOM   4981  ND1 HIS B 168     -12.038  25.476 -14.340  1.00 56.27           N  
-ATOM   4982  CD2 HIS B 168     -14.022  25.519 -13.428  1.00 58.70           C  
-ATOM   4983  CE1 HIS B 168     -12.012  24.649 -13.310  1.00 61.61           C  
-ATOM   4984  NE2 HIS B 168     -13.203  24.657 -12.740  1.00 72.30           N  
-ATOM   4985  N   LEU B 169     -12.833  29.273 -17.621  1.00 32.55           N  
-ATOM   4986  CA  LEU B 169     -13.262  30.088 -18.756  1.00 36.26           C  
-ATOM   4987  C   LEU B 169     -13.589  29.235 -19.980  1.00 37.40           C  
-ATOM   4988  O   LEU B 169     -12.708  28.590 -20.541  1.00 34.37           O  
-ATOM   4989  CB  LEU B 169     -12.185  31.109 -19.131  1.00 27.64           C  
-ATOM   4990  CG  LEU B 169     -11.698  32.110 -18.085  1.00 28.97           C  
-ATOM   4991  CD1 LEU B 169     -10.883  33.203 -18.754  1.00 27.54           C  
-ATOM   4992  CD2 LEU B 169     -12.858  32.706 -17.324  1.00 32.62           C  
-ATOM   4993  N   TYR B 170     -14.852  29.238 -20.396  1.00 34.10           N  
-ATOM   4994  CA  TYR B 170     -15.248  28.552 -21.625  1.00 31.81           C  
-ATOM   4995  C   TYR B 170     -15.204  29.514 -22.805  1.00 27.87           C  
-ATOM   4996  O   TYR B 170     -16.191  30.180 -23.112  1.00 27.41           O  
-ATOM   4997  CB  TYR B 170     -16.648  27.950 -21.493  1.00 48.38           C  
-ATOM   4998  CG  TYR B 170     -16.723  26.760 -20.564  1.00 55.16           C  
-ATOM   4999  CD1 TYR B 170     -16.840  26.934 -19.190  1.00 55.67           C  
-ATOM   5000  CD2 TYR B 170     -16.686  25.464 -21.060  1.00 41.66           C  
-ATOM   5001  CE1 TYR B 170     -16.912  25.850 -18.336  1.00 54.92           C  
-ATOM   5002  CE2 TYR B 170     -16.757  24.375 -20.213  1.00 50.97           C  
-ATOM   5003  CZ  TYR B 170     -16.870  24.573 -18.854  1.00 56.87           C  
-ATOM   5004  OH  TYR B 170     -16.941  23.486 -18.012  1.00 66.04           O  
-ATOM   5005  N   ILE B 171     -14.055  29.578 -23.467  1.00 37.87           N  
-ATOM   5006  CA  ILE B 171     -13.839  30.545 -24.536  1.00 27.89           C  
-ATOM   5007  C   ILE B 171     -13.989  29.937 -25.928  1.00 31.83           C  
-ATOM   5008  O   ILE B 171     -13.387  28.908 -26.238  1.00 27.29           O  
-ATOM   5009  CB  ILE B 171     -12.440  31.187 -24.432  1.00 20.72           C  
-ATOM   5010  CG1 ILE B 171     -12.241  31.828 -23.057  1.00 26.33           C  
-ATOM   5011  CG2 ILE B 171     -12.236  32.209 -25.539  1.00 27.74           C  
-ATOM   5012  CD1 ILE B 171     -10.931  32.560 -22.914  1.00 25.51           C  
-ATOM   5013  N   THR B 172     -14.802  30.584 -26.760  1.00 34.97           N  
-ATOM   5014  CA  THR B 172     -14.886  30.251 -28.177  1.00 29.12           C  
-ATOM   5015  C   THR B 172     -13.973  31.180 -28.970  1.00 30.55           C  
-ATOM   5016  O   THR B 172     -14.275  32.362 -29.140  1.00 36.56           O  
-ATOM   5017  CB  THR B 172     -16.325  30.369 -28.716  1.00 26.92           C  
-ATOM   5018  OG1 THR B 172     -17.226  29.659 -27.858  1.00 35.55           O  
-ATOM   5019  CG2 THR B 172     -16.417  29.803 -30.125  1.00 22.79           C  
-ATOM   5020  N   ARG B 173     -12.853  30.648 -29.446  1.00 25.25           N  
-ATOM   5021  CA  ARG B 173     -11.879  31.460 -30.165  1.00 24.05           C  
-ATOM   5022  C   ARG B 173     -12.293  31.711 -31.608  1.00 22.74           C  
-ATOM   5023  O   ARG B 173     -11.959  30.929 -32.495  1.00 23.22           O  
-ATOM   5024  CB  ARG B 173     -10.507  30.793 -30.149  1.00 20.00           C  
-ATOM   5025  CG  ARG B 173      -9.981  30.480 -28.771  1.00 23.25           C  
-ATOM   5026  CD  ARG B 173      -9.104  29.252 -28.824  1.00 29.70           C  
-ATOM   5027  NE  ARG B 173      -7.683  29.576 -28.842  1.00 30.64           N  
-ATOM   5028  CZ  ARG B 173      -6.729  28.707 -29.162  1.00 32.94           C  
-ATOM   5029  NH1 ARG B 173      -7.049  27.466 -29.507  1.00 23.98           N  
-ATOM   5030  NH2 ARG B 173      -5.457  29.081 -29.148  1.00 34.58           N  
-ATOM   5031  N   VAL B 174     -13.013  32.799 -31.844  1.00 18.03           N  
-ATOM   5032  CA  VAL B 174     -13.282  33.233 -33.207  1.00 21.39           C  
-ATOM   5033  C   VAL B 174     -11.960  33.640 -33.850  1.00 22.94           C  
-ATOM   5034  O   VAL B 174     -11.286  34.541 -33.360  1.00 21.34           O  
-ATOM   5035  CB  VAL B 174     -14.273  34.404 -33.245  1.00 22.75           C  
-ATOM   5036  CG1 VAL B 174     -14.589  34.787 -34.682  1.00 18.90           C  
-ATOM   5037  CG2 VAL B 174     -15.541  34.036 -32.493  1.00 29.06           C  
-ATOM   5038  N   ALA B 175     -11.584  32.965 -34.933  1.00 17.38           N  
-ATOM   5039  CA  ALA B 175     -10.268  33.168 -35.537  1.00 14.37           C  
-ATOM   5040  C   ALA B 175     -10.184  34.456 -36.353  1.00 22.73           C  
-ATOM   5041  O   ALA B 175      -9.115  35.059 -36.455  1.00 22.97           O  
-ATOM   5042  CB  ALA B 175      -9.900  31.979 -36.404  1.00 15.90           C  
-ATOM   5043  N   ARG B 176     -11.307  34.868 -36.936  1.00 26.12           N  
-ATOM   5044  CA  ARG B 176     -11.373  36.114 -37.697  1.00 20.72           C  
-ATOM   5045  C   ARG B 176     -11.560  37.326 -36.799  1.00 21.01           C  
-ATOM   5046  O   ARG B 176     -12.255  37.258 -35.786  1.00 21.51           O  
-ATOM   5047  CB  ARG B 176     -12.520  36.078 -38.701  1.00 21.12           C  
-ATOM   5048  CG  ARG B 176     -12.336  35.134 -39.858  1.00 21.40           C  
-ATOM   5049  CD  ARG B 176     -13.552  35.192 -40.768  1.00 23.51           C  
-ATOM   5050  NE  ARG B 176     -13.831  36.552 -41.221  1.00 21.56           N  
-ATOM   5051  CZ  ARG B 176     -14.805  36.872 -42.068  1.00 29.89           C  
-ATOM   5052  NH1 ARG B 176     -14.988  38.136 -42.423  1.00 43.65           N  
-ATOM   5053  NH2 ARG B 176     -15.594  35.928 -42.562  1.00 25.77           N  
-ATOM   5054  N   GLU B 177     -10.949  38.442 -37.178  1.00 22.46           N  
-ATOM   5055  CA  GLU B 177     -11.226  39.703 -36.506  1.00 28.89           C  
-ATOM   5056  C   GLU B 177     -12.422  40.383 -37.152  1.00 27.78           C  
-ATOM   5057  O   GLU B 177     -12.639  40.276 -38.360  1.00 23.03           O  
-ATOM   5058  CB  GLU B 177     -10.013  40.634 -36.538  1.00 34.12           C  
-ATOM   5059  CG  GLU B 177      -9.135  40.568 -35.297  1.00 38.79           C  
-ATOM   5060  CD  GLU B 177      -7.798  39.895 -35.558  1.00 66.07           C  
-ATOM   5061  OE1 GLU B 177      -7.752  38.939 -36.365  1.00 64.97           O  
-ATOM   5062  OE2 GLU B 177      -6.789  40.327 -34.959  1.00 66.19           O  
-ATOM   5063  N   PHE B 178     -13.197  41.077 -36.331  1.00 30.12           N  
-ATOM   5064  CA  PHE B 178     -14.361  41.808 -36.799  1.00 22.31           C  
-ATOM   5065  C   PHE B 178     -14.412  43.171 -36.126  1.00 22.26           C  
-ATOM   5066  O   PHE B 178     -13.847  43.349 -35.045  1.00 24.40           O  
-ATOM   5067  CB  PHE B 178     -15.645  41.025 -36.510  1.00 21.01           C  
-ATOM   5068  CG  PHE B 178     -15.818  39.796 -37.355  1.00 22.75           C  
-ATOM   5069  CD1 PHE B 178     -16.430  39.876 -38.595  1.00 27.97           C  
-ATOM   5070  CD2 PHE B 178     -15.386  38.557 -36.905  1.00 25.99           C  
-ATOM   5071  CE1 PHE B 178     -16.600  38.745 -39.376  1.00 32.73           C  
-ATOM   5072  CE2 PHE B 178     -15.556  37.424 -37.680  1.00 23.21           C  
-ATOM   5073  CZ  PHE B 178     -16.162  37.519 -38.916  1.00 29.22           C  
-ATOM   5074  N   PRO B 179     -15.069  44.145 -36.773  1.00 22.33           N  
-ATOM   5075  CA  PRO B 179     -15.324  45.437 -36.130  1.00 22.89           C  
-ATOM   5076  C   PRO B 179     -16.046  45.264 -34.799  1.00 23.45           C  
-ATOM   5077  O   PRO B 179     -17.065  44.574 -34.737  1.00 25.70           O  
-ATOM   5078  CB  PRO B 179     -16.205  46.163 -37.147  1.00 15.46           C  
-ATOM   5079  CG  PRO B 179     -15.801  45.587 -38.454  1.00 17.30           C  
-ATOM   5080  CD  PRO B 179     -15.485  44.142 -38.186  1.00 19.59           C  
-ATOM   5081  N   CYS B 180     -15.511  45.873 -33.747  1.00 22.44           N  
-ATOM   5082  CA  CYS B 180     -16.095  45.760 -32.417  1.00 24.44           C  
-ATOM   5083  C   CYS B 180     -15.957  47.055 -31.629  1.00 28.73           C  
-ATOM   5084  O   CYS B 180     -15.046  47.849 -31.868  1.00 36.45           O  
-ATOM   5085  CB  CYS B 180     -15.441  44.617 -31.637  1.00 26.93           C  
-ATOM   5086  SG  CYS B 180     -15.731  42.975 -32.309  1.00 23.44           S  
-ATOM   5087  N   ASP B 181     -16.866  47.259 -30.684  1.00 28.77           N  
-ATOM   5088  CA  ASP B 181     -16.778  48.394 -29.777  1.00 33.90           C  
-ATOM   5089  C   ASP B 181     -16.844  47.919 -28.326  1.00 27.12           C  
-ATOM   5090  O   ASP B 181     -16.806  48.724 -27.398  1.00 40.13           O  
-ATOM   5091  CB  ASP B 181     -17.886  49.415 -30.072  1.00 38.54           C  
-ATOM   5092  CG  ASP B 181     -19.270  48.784 -30.152  1.00 35.20           C  
-ATOM   5093  OD1 ASP B 181     -19.519  47.781 -29.451  1.00 39.78           O  
-ATOM   5094  OD2 ASP B 181     -20.116  49.299 -30.916  1.00 24.62           O  
-ATOM   5095  N   VAL B 182     -16.947  46.607 -28.140  1.00 23.25           N  
-ATOM   5096  CA  VAL B 182     -17.003  46.018 -26.805  1.00 27.74           C  
-ATOM   5097  C   VAL B 182     -16.079  44.807 -26.706  1.00 26.33           C  
-ATOM   5098  O   VAL B 182     -16.221  43.841 -27.454  1.00 23.31           O  
-ATOM   5099  CB  VAL B 182     -18.438  45.597 -26.428  1.00 27.35           C  
-ATOM   5100  CG1 VAL B 182     -18.426  44.746 -25.174  1.00 39.93           C  
-ATOM   5101  CG2 VAL B 182     -19.318  46.819 -26.233  1.00 27.22           C  
-ATOM   5102  N   PHE B 183     -15.140  44.863 -25.767  1.00 29.52           N  
-ATOM   5103  CA  PHE B 183     -14.087  43.856 -25.679  1.00 27.70           C  
-ATOM   5104  C   PHE B 183     -14.064  43.109 -24.350  1.00 34.01           C  
-ATOM   5105  O   PHE B 183     -14.365  43.674 -23.299  1.00 32.37           O  
-ATOM   5106  CB  PHE B 183     -12.721  44.507 -25.909  1.00 25.15           C  
-ATOM   5107  CG  PHE B 183     -12.549  45.093 -27.279  1.00 22.22           C  
-ATOM   5108  CD1 PHE B 183     -13.049  46.348 -27.579  1.00 23.27           C  
-ATOM   5109  CD2 PHE B 183     -11.876  44.393 -28.264  1.00 27.12           C  
-ATOM   5110  CE1 PHE B 183     -12.890  46.889 -28.838  1.00 29.00           C  
-ATOM   5111  CE2 PHE B 183     -11.711  44.927 -29.525  1.00 27.16           C  
-ATOM   5112  CZ  PHE B 183     -12.219  46.178 -29.814  1.00 32.44           C  
-ATOM   5113  N   PHE B 184     -13.690  41.834 -24.413  1.00 37.81           N  
-ATOM   5114  CA  PHE B 184     -13.444  41.036 -23.218  1.00 36.83           C  
-ATOM   5115  C   PHE B 184     -12.149  41.510 -22.567  1.00 37.52           C  
-ATOM   5116  O   PHE B 184     -11.152  41.728 -23.255  1.00 36.81           O  
-ATOM   5117  CB  PHE B 184     -13.366  39.545 -23.566  1.00 32.79           C  
-ATOM   5118  CG  PHE B 184     -13.331  38.639 -22.365  1.00 40.21           C  
-ATOM   5119  CD1 PHE B 184     -14.506  38.188 -21.784  1.00 35.46           C  
-ATOM   5120  CD2 PHE B 184     -12.123  38.235 -21.818  1.00 37.67           C  
-ATOM   5121  CE1 PHE B 184     -14.477  37.354 -20.681  1.00 24.19           C  
-ATOM   5122  CE2 PHE B 184     -12.088  37.399 -20.715  1.00 31.31           C  
-ATOM   5123  CZ  PHE B 184     -13.267  36.960 -20.147  1.00 24.45           C  
-ATOM   5124  N   PRO B 185     -12.161  41.677 -21.236  1.00 37.89           N  
-ATOM   5125  CA  PRO B 185     -11.018  42.220 -20.493  1.00 35.88           C  
-ATOM   5126  C   PRO B 185      -9.735  41.427 -20.708  1.00 34.54           C  
-ATOM   5127  O   PRO B 185      -9.790  40.222 -20.948  1.00 37.66           O  
-ATOM   5128  CB  PRO B 185     -11.471  42.119 -19.034  1.00 43.99           C  
-ATOM   5129  CG  PRO B 185     -12.954  42.107 -19.102  1.00 47.76           C  
-ATOM   5130  CD  PRO B 185     -13.289  41.355 -20.347  1.00 37.62           C  
-ATOM   5131  N   ALA B 186      -8.595  42.105 -20.635  1.00 38.49           N  
-ATOM   5132  CA  ALA B 186      -7.307  41.431 -20.720  1.00 42.96           C  
-ATOM   5133  C   ALA B 186      -7.089  40.603 -19.459  1.00 43.66           C  
-ATOM   5134  O   ALA B 186      -7.586  40.952 -18.388  1.00 43.21           O  
-ATOM   5135  CB  ALA B 186      -6.182  42.435 -20.911  1.00 32.31           C  
-ATOM   5136  N   PHE B 187      -6.352  39.505 -19.588  1.00 44.56           N  
-ATOM   5137  CA  PHE B 187      -6.146  38.598 -18.465  1.00 49.00           C  
-ATOM   5138  C   PHE B 187      -4.922  37.711 -18.686  1.00 54.67           C  
-ATOM   5139  O   PHE B 187      -4.531  37.467 -19.829  1.00 49.18           O  
-ATOM   5140  CB  PHE B 187      -7.393  37.734 -18.246  1.00 39.22           C  
-ATOM   5141  CG  PHE B 187      -7.732  36.847 -19.411  1.00 38.99           C  
-ATOM   5142  CD1 PHE B 187      -7.257  35.547 -19.470  1.00 37.14           C  
-ATOM   5143  CD2 PHE B 187      -8.527  37.311 -20.445  1.00 38.05           C  
-ATOM   5144  CE1 PHE B 187      -7.565  34.730 -20.540  1.00 31.96           C  
-ATOM   5145  CE2 PHE B 187      -8.839  36.498 -21.517  1.00 36.07           C  
-ATOM   5146  CZ  PHE B 187      -8.357  35.206 -21.563  1.00 34.42           C  
-ATOM   5147  N   PRO B 188      -4.307  37.236 -17.588  1.00 45.12           N  
-ATOM   5148  CA  PRO B 188      -3.188  36.292 -17.665  1.00 43.25           C  
-ATOM   5149  C   PRO B 188      -3.610  34.978 -18.301  1.00 46.27           C  
-ATOM   5150  O   PRO B 188      -4.376  34.221 -17.704  1.00 47.21           O  
-ATOM   5151  CB  PRO B 188      -2.798  36.082 -16.200  1.00 46.94           C  
-ATOM   5152  CG  PRO B 188      -3.277  37.283 -15.514  1.00 48.57           C  
-ATOM   5153  CD  PRO B 188      -4.552  37.662 -16.201  1.00 43.95           C  
-ATOM   5154  N   GLY B 189      -3.105  34.716 -19.500  1.00 42.51           N  
-ATOM   5155  CA  GLY B 189      -3.516  33.562 -20.274  1.00 41.27           C  
-ATOM   5156  C   GLY B 189      -3.901  34.033 -21.659  1.00 48.11           C  
-ATOM   5157  O   GLY B 189      -4.150  33.231 -22.566  1.00 57.04           O  
-ATOM   5158  N   ASP B 190      -3.921  35.354 -21.819  1.00 47.19           N  
-ATOM   5159  CA  ASP B 190      -4.254  36.004 -23.083  1.00 36.10           C  
-ATOM   5160  C   ASP B 190      -3.497  35.415 -24.272  1.00 38.37           C  
-ATOM   5161  O   ASP B 190      -3.945  35.518 -25.415  1.00 39.24           O  
-ATOM   5162  CB  ASP B 190      -3.978  37.507 -22.978  1.00 38.40           C  
-ATOM   5163  CG  ASP B 190      -5.233  38.338 -23.134  1.00 55.69           C  
-ATOM   5164  OD1 ASP B 190      -6.325  37.740 -23.220  1.00 62.74           O  
-ATOM   5165  OD2 ASP B 190      -5.130  39.583 -23.168  1.00 64.56           O  
-ATOM   5166  N   ASP B 191      -2.359  34.790 -23.983  1.00 38.49           N  
-ATOM   5167  CA  ASP B 191      -1.555  34.088 -24.977  1.00 39.26           C  
-ATOM   5168  C   ASP B 191      -2.359  33.143 -25.864  1.00 40.27           C  
-ATOM   5169  O   ASP B 191      -1.955  32.865 -26.991  1.00 45.49           O  
-ATOM   5170  CB  ASP B 191      -0.444  33.297 -24.284  1.00 43.25           C  
-ATOM   5171  CG  ASP B 191       0.897  33.994 -24.351  1.00 72.66           C  
-ATOM   5172  OD1 ASP B 191       0.929  35.213 -24.631  1.00 91.93           O  
-ATOM   5173  OD2 ASP B 191       1.921  33.317 -24.120  1.00 69.41           O  
-ATOM   5174  N   ILE B 192      -3.487  32.646 -25.359  1.00 36.40           N  
-ATOM   5175  CA  ILE B 192      -4.284  31.665 -26.101  1.00 35.55           C  
-ATOM   5176  C   ILE B 192      -5.071  32.304 -27.257  1.00 33.38           C  
-ATOM   5177  O   ILE B 192      -5.542  31.610 -28.160  1.00 34.28           O  
-ATOM   5178  CB  ILE B 192      -5.242  30.914 -25.146  1.00 33.55           C  
-ATOM   5179  CG1 ILE B 192      -4.457  30.429 -23.928  1.00 64.71           C  
-ATOM   5180  CG2 ILE B 192      -5.898  29.728 -25.834  1.00 31.75           C  
-ATOM   5181  CD1 ILE B 192      -5.318  29.874 -22.834  1.00 71.84           C  
-ATOM   5182  N   LEU B 193      -5.195  33.628 -27.243  1.00 29.14           N  
-ATOM   5183  CA  LEU B 193      -5.918  34.325 -28.304  1.00 23.81           C  
-ATOM   5184  C   LEU B 193      -4.994  34.804 -29.424  1.00 30.65           C  
-ATOM   5185  O   LEU B 193      -5.300  34.633 -30.605  1.00 31.47           O  
-ATOM   5186  CB  LEU B 193      -6.692  35.500 -27.720  1.00 20.31           C  
-ATOM   5187  CG  LEU B 193      -7.678  35.089 -26.627  1.00 22.52           C  
-ATOM   5188  CD1 LEU B 193      -8.056  36.287 -25.788  1.00 30.57           C  
-ATOM   5189  CD2 LEU B 193      -8.920  34.427 -27.212  1.00 13.52           C  
-ATOM   5190  N   SER B 194      -3.867  35.404 -29.054  1.00 27.92           N  
-ATOM   5191  CA  SER B 194      -2.881  35.850 -30.033  1.00 28.34           C  
-ATOM   5192  C   SER B 194      -1.538  36.109 -29.353  1.00 41.08           C  
-ATOM   5193  O   SER B 194      -1.342  35.731 -28.197  1.00 41.42           O  
-ATOM   5194  CB  SER B 194      -3.370  37.101 -30.767  1.00 29.19           C  
-ATOM   5195  OG  SER B 194      -3.909  38.046 -29.860  1.00 41.86           O  
-ATOM   5196  N   ASN B 195      -0.616  36.746 -30.070  1.00 46.05           N  
-ATOM   5197  CA  ASN B 195       0.751  36.918 -29.579  1.00 40.05           C  
-ATOM   5198  C   ASN B 195       0.945  38.166 -28.714  1.00 43.76           C  
-ATOM   5199  O   ASN B 195       2.071  38.640 -28.549  1.00 41.71           O  
-ATOM   5200  CB  ASN B 195       1.727  36.951 -30.760  1.00 31.44           C  
-ATOM   5201  CG  ASN B 195       1.716  35.659 -31.559  1.00 26.28           C  
-ATOM   5202  OD1 ASN B 195       1.155  34.656 -31.123  1.00 29.85           O  
-ATOM   5203  ND2 ASN B 195       2.346  35.675 -32.727  1.00 27.68           N  
-ATOM   5204  N   LYS B 196      -0.151  38.684 -28.161  1.00 54.74           N  
-ATOM   5205  CA  LYS B 196      -0.101  39.871 -27.306  1.00 62.57           C  
-ATOM   5206  C   LYS B 196       0.857  39.668 -26.136  1.00 50.51           C  
-ATOM   5207  O   LYS B 196       2.020  40.064 -26.205  1.00 40.31           O  
-ATOM   5208  CB  LYS B 196      -1.497  40.229 -26.777  1.00 71.79           C  
-ATOM   5209  CG  LYS B 196      -2.247  41.269 -27.601  1.00 87.54           C  
-ATOM   5210  CD  LYS B 196      -2.556  40.753 -28.991  1.00 83.31           C  
-ATOM   5211  CE  LYS B 196      -3.425  41.726 -29.764  1.00 74.71           C  
-ATOM   5212  NZ  LYS B 196      -3.809  41.166 -31.087  1.00 51.24           N  
-ATOM   5213  N   GLU B 224       0.932  34.986  -8.250  1.00 85.26           N  
-ATOM   5214  CA  GLU B 224       0.169  35.559  -9.351  1.00 83.61           C  
-ATOM   5215  C   GLU B 224      -0.781  34.525  -9.947  1.00 91.36           C  
-ATOM   5216  O   GLU B 224      -0.377  33.399 -10.242  1.00 87.34           O  
-ATOM   5217  CB  GLU B 224       1.107  36.096 -10.433  1.00 84.56           C  
-ATOM   5218  CG  GLU B 224       0.471  37.135 -11.340  1.00 85.88           C  
-ATOM   5219  CD  GLU B 224       0.221  38.447 -10.624  1.00 94.02           C  
-ATOM   5220  OE1 GLU B 224      -0.938  38.704 -10.234  1.00 82.90           O  
-ATOM   5221  OE2 GLU B 224       1.188  39.219 -10.448  1.00 88.06           O  
-ATOM   5222  N   ALA B 225      -2.041  34.910 -10.123  1.00 84.23           N  
-ATOM   5223  CA  ALA B 225      -3.043  34.007 -10.681  1.00 70.63           C  
-ATOM   5224  C   ALA B 225      -3.034  34.052 -12.206  1.00 68.61           C  
-ATOM   5225  O   ALA B 225      -2.920  35.121 -12.805  1.00 74.05           O  
-ATOM   5226  CB  ALA B 225      -4.422  34.352 -10.149  1.00 53.87           C  
-ATOM   5227  N   THR B 226      -3.158  32.885 -12.829  1.00 63.14           N  
-ATOM   5228  CA  THR B 226      -3.129  32.797 -14.283  1.00 58.14           C  
-ATOM   5229  C   THR B 226      -4.025  31.675 -14.804  1.00 50.18           C  
-ATOM   5230  O   THR B 226      -4.223  30.658 -14.137  1.00 42.71           O  
-ATOM   5231  CB  THR B 226      -1.695  32.582 -14.801  1.00 59.70           C  
-ATOM   5232  OG1 THR B 226      -1.708  32.490 -16.232  1.00 58.16           O  
-ATOM   5233  CG2 THR B 226      -1.101  31.308 -14.216  1.00 62.89           C  
-ATOM   5234  N   TYR B 227      -4.561  31.872 -16.003  1.00 45.16           N  
-ATOM   5235  CA  TYR B 227      -5.493  30.924 -16.601  1.00 35.79           C  
-ATOM   5236  C   TYR B 227      -4.805  29.986 -17.584  1.00 41.40           C  
-ATOM   5237  O   TYR B 227      -4.463  30.380 -18.700  1.00 44.67           O  
-ATOM   5238  CB  TYR B 227      -6.625  31.673 -17.306  1.00 28.57           C  
-ATOM   5239  CG  TYR B 227      -7.568  32.385 -16.365  1.00 35.93           C  
-ATOM   5240  CD1 TYR B 227      -8.677  31.733 -15.844  1.00 42.48           C  
-ATOM   5241  CD2 TYR B 227      -7.352  33.707 -15.996  1.00 41.38           C  
-ATOM   5242  CE1 TYR B 227      -9.544  32.374 -14.984  1.00 40.86           C  
-ATOM   5243  CE2 TYR B 227      -8.216  34.358 -15.134  1.00 40.81           C  
-ATOM   5244  CZ  TYR B 227      -9.310  33.684 -14.630  1.00 42.43           C  
-ATOM   5245  OH  TYR B 227     -10.180  34.317 -13.772  1.00 53.33           O  
-ATOM   5246  N   ARG B 228      -4.609  28.740 -17.167  1.00 42.09           N  
-ATOM   5247  CA  ARG B 228      -3.995  27.740 -18.031  1.00 41.59           C  
-ATOM   5248  C   ARG B 228      -5.071  26.953 -18.773  1.00 44.46           C  
-ATOM   5249  O   ARG B 228      -6.072  26.553 -18.178  1.00 47.35           O  
-ATOM   5250  CB  ARG B 228      -3.103  26.797 -17.218  1.00 45.76           C  
-ATOM   5251  CG  ARG B 228      -1.687  26.638 -17.765  1.00 47.61           C  
-ATOM   5252  CD  ARG B 228      -0.652  26.769 -16.654  1.00 55.97           C  
-ATOM   5253  NE  ARG B 228      -0.914  25.848 -15.550  1.00 72.81           N  
-ATOM   5254  CZ  ARG B 228      -0.258  24.709 -15.350  1.00 65.72           C  
-ATOM   5255  NH1 ARG B 228       0.715  24.346 -16.177  1.00 59.73           N  
-ATOM   5256  NH2 ARG B 228      -0.569  23.934 -14.319  1.00 46.32           N  
-ATOM   5257  N   PRO B 229      -4.873  26.742 -20.083  1.00 43.47           N  
-ATOM   5258  CA  PRO B 229      -5.809  25.949 -20.884  1.00 31.89           C  
-ATOM   5259  C   PRO B 229      -5.712  24.460 -20.559  1.00 44.67           C  
-ATOM   5260  O   PRO B 229      -4.633  23.963 -20.227  1.00 46.72           O  
-ATOM   5261  CB  PRO B 229      -5.369  26.233 -22.319  1.00 31.98           C  
-ATOM   5262  CG  PRO B 229      -3.924  26.550 -22.207  1.00 38.44           C  
-ATOM   5263  CD  PRO B 229      -3.753  27.256 -20.891  1.00 43.63           C  
-ATOM   5264  N   ILE B 230      -6.836  23.761 -20.664  1.00 38.43           N  
-ATOM   5265  CA  ILE B 230      -6.927  22.369 -20.246  1.00 35.44           C  
-ATOM   5266  C   ILE B 230      -7.657  21.566 -21.324  1.00 37.41           C  
-ATOM   5267  O   ILE B 230      -7.528  20.337 -21.428  1.00 39.91           O  
-ATOM   5268  CB  ILE B 230      -7.661  22.261 -18.887  1.00 29.91           C  
-ATOM   5269  CG1 ILE B 230      -6.890  21.373 -17.912  1.00 51.29           C  
-ATOM   5270  CG2 ILE B 230      -9.102  21.810 -19.068  1.00 28.22           C  
-ATOM   5271  CD1 ILE B 230      -5.906  22.134 -17.042  1.00 52.99           C  
-ATOM   5272  N   PHE B 231      -8.405  22.302 -22.138  1.00 32.34           N  
-ATOM   5273  CA  PHE B 231      -9.250  21.751 -23.182  1.00 30.56           C  
-ATOM   5274  C   PHE B 231      -9.039  22.570 -24.444  1.00 29.93           C  
-ATOM   5275  O   PHE B 231      -9.225  23.779 -24.427  1.00 35.95           O  
-ATOM   5276  CB  PHE B 231     -10.719  21.784 -22.742  1.00 31.26           C  
-ATOM   5277  CG  PHE B 231     -11.688  21.293 -23.781  1.00 33.20           C  
-ATOM   5278  CD1 PHE B 231     -12.132  22.123 -24.798  1.00 31.64           C  
-ATOM   5279  CD2 PHE B 231     -12.184  20.007 -23.719  1.00 48.26           C  
-ATOM   5280  CE1 PHE B 231     -13.026  21.663 -25.744  1.00 35.04           C  
-ATOM   5281  CE2 PHE B 231     -13.076  19.543 -24.658  1.00 50.22           C  
-ATOM   5282  CZ  PHE B 231     -13.500  20.371 -25.672  1.00 34.45           C  
-ATOM   5283  N   ILE B 232      -8.633  21.928 -25.532  1.00 29.57           N  
-ATOM   5284  CA  ILE B 232      -8.547  22.621 -26.816  1.00 26.58           C  
-ATOM   5285  C   ILE B 232      -9.151  21.742 -27.901  1.00 27.54           C  
-ATOM   5286  O   ILE B 232      -8.708  20.613 -28.109  1.00 25.86           O  
-ATOM   5287  CB  ILE B 232      -7.098  22.989 -27.190  1.00 28.78           C  
-ATOM   5288  CG1 ILE B 232      -6.511  23.970 -26.172  1.00 22.74           C  
-ATOM   5289  CG2 ILE B 232      -7.049  23.598 -28.587  1.00 25.81           C  
-ATOM   5290  CD1 ILE B 232      -5.118  24.434 -26.508  1.00 25.38           C  
-ATOM   5291  N   SER B 233     -10.158  22.270 -28.594  1.00 29.16           N  
-ATOM   5292  CA  SER B 233     -10.979  21.464 -29.493  1.00 29.56           C  
-ATOM   5293  C   SER B 233     -10.540  21.497 -30.952  1.00 26.36           C  
-ATOM   5294  O   SER B 233      -9.675  22.279 -31.346  1.00 29.59           O  
-ATOM   5295  CB  SER B 233     -12.438  21.918 -29.413  1.00 36.46           C  
-ATOM   5296  OG  SER B 233     -12.634  23.130 -30.124  1.00 28.50           O  
-ATOM   5297  N   LYS B 234     -11.163  20.629 -31.742  1.00 22.06           N  
-ATOM   5298  CA  LYS B 234     -11.007  20.626 -33.189  1.00 27.17           C  
-ATOM   5299  C   LYS B 234     -11.549  21.939 -33.744  1.00 31.31           C  
-ATOM   5300  O   LYS B 234     -12.447  22.538 -33.153  1.00 36.41           O  
-ATOM   5301  CB  LYS B 234     -11.738  19.423 -33.792  1.00 33.69           C  
-ATOM   5302  CG  LYS B 234     -11.788  19.374 -35.308  1.00 39.88           C  
-ATOM   5303  CD  LYS B 234     -13.178  18.965 -35.780  1.00 51.25           C  
-ATOM   5304  CE  LYS B 234     -13.695  17.753 -35.012  1.00 46.36           C  
-ATOM   5305  NZ  LYS B 234     -15.116  17.442 -35.337  1.00 37.13           N  
-ATOM   5306  N   THR B 235     -11.000  22.401 -34.862  1.00 30.20           N  
-ATOM   5307  CA  THR B 235     -11.462  23.647 -35.463  1.00 26.88           C  
-ATOM   5308  C   THR B 235     -12.784  23.460 -36.206  1.00 24.42           C  
-ATOM   5309  O   THR B 235     -12.905  22.598 -37.078  1.00 25.10           O  
-ATOM   5310  CB  THR B 235     -10.420  24.226 -36.437  1.00 22.72           C  
-ATOM   5311  OG1 THR B 235      -9.168  24.394 -35.759  1.00 22.97           O  
-ATOM   5312  CG2 THR B 235     -10.885  25.569 -36.964  1.00 22.59           C  
-ATOM   5313  N   PHE B 236     -13.776  24.270 -35.848  1.00 23.56           N  
-ATOM   5314  CA  PHE B 236     -15.065  24.249 -36.529  1.00 24.58           C  
-ATOM   5315  C   PHE B 236     -15.211  25.490 -37.394  1.00 25.78           C  
-ATOM   5316  O   PHE B 236     -14.388  26.398 -37.319  1.00 25.97           O  
-ATOM   5317  CB  PHE B 236     -16.211  24.159 -35.522  1.00 22.86           C  
-ATOM   5318  CG  PHE B 236     -16.208  22.892 -34.724  1.00 28.60           C  
-ATOM   5319  CD1 PHE B 236     -16.794  21.743 -35.227  1.00 31.42           C  
-ATOM   5320  CD2 PHE B 236     -15.610  22.844 -33.476  1.00 27.46           C  
-ATOM   5321  CE1 PHE B 236     -16.787  20.572 -34.502  1.00 30.66           C  
-ATOM   5322  CE2 PHE B 236     -15.601  21.674 -32.744  1.00 33.33           C  
-ATOM   5323  CZ  PHE B 236     -16.191  20.535 -33.259  1.00 38.02           C  
-ATOM   5324  N   SER B 237     -16.250  25.528 -38.220  1.00 30.47           N  
-ATOM   5325  CA  SER B 237     -16.475  26.682 -39.085  1.00 24.13           C  
-ATOM   5326  C   SER B 237     -17.943  26.864 -39.446  1.00 35.49           C  
-ATOM   5327  O   SER B 237     -18.639  25.894 -39.759  1.00 37.70           O  
-ATOM   5328  CB  SER B 237     -15.660  26.557 -40.368  1.00 20.26           C  
-ATOM   5329  OG  SER B 237     -16.242  25.605 -41.241  1.00 33.38           O  
-ATOM   5330  N   ASP B 238     -18.401  28.114 -39.410  1.00 33.80           N  
-ATOM   5331  CA  ASP B 238     -19.749  28.457 -39.851  1.00 28.85           C  
-ATOM   5332  C   ASP B 238     -19.763  29.809 -40.558  1.00 24.56           C  
-ATOM   5333  O   ASP B 238     -19.176  30.777 -40.073  1.00 26.30           O  
-ATOM   5334  CB  ASP B 238     -20.719  28.459 -38.670  1.00 32.34           C  
-ATOM   5335  CG  ASP B 238     -21.205  27.069 -38.322  1.00 38.56           C  
-ATOM   5336  OD1 ASP B 238     -21.638  26.337 -39.240  1.00 37.11           O  
-ATOM   5337  OD2 ASP B 238     -21.144  26.702 -37.131  1.00 33.99           O  
-ATOM   5338  N   ASN B 239     -20.437  29.855 -41.705  1.00 23.11           N  
-ATOM   5339  CA  ASN B 239     -20.544  31.059 -42.527  1.00 23.28           C  
-ATOM   5340  C   ASN B 239     -19.195  31.705 -42.823  1.00 21.15           C  
-ATOM   5341  O   ASN B 239     -19.071  32.931 -42.826  1.00 20.79           O  
-ATOM   5342  CB  ASN B 239     -21.466  32.081 -41.861  1.00 24.45           C  
-ATOM   5343  CG  ASN B 239     -22.899  31.593 -41.752  1.00 25.91           C  
-ATOM   5344  OD1 ASN B 239     -23.604  31.470 -42.754  1.00 27.46           O  
-ATOM   5345  ND2 ASN B 239     -23.339  31.317 -40.530  1.00 30.87           N  
-ATOM   5346  N   GLY B 240     -18.189  30.876 -43.075  1.00 21.89           N  
-ATOM   5347  CA  GLY B 240     -16.870  31.367 -43.427  1.00 32.85           C  
-ATOM   5348  C   GLY B 240     -16.096  31.886 -42.230  1.00 32.04           C  
-ATOM   5349  O   GLY B 240     -15.135  32.644 -42.379  1.00 26.50           O  
-ATOM   5350  N   VAL B 241     -16.524  31.476 -41.039  1.00 30.06           N  
-ATOM   5351  CA  VAL B 241     -15.846  31.846 -39.804  1.00 21.00           C  
-ATOM   5352  C   VAL B 241     -15.343  30.608 -39.077  1.00 24.77           C  
-ATOM   5353  O   VAL B 241     -16.138  29.778 -38.633  1.00 29.24           O  
-ATOM   5354  CB  VAL B 241     -16.767  32.635 -38.860  1.00 22.69           C  
-ATOM   5355  CG1 VAL B 241     -16.005  33.052 -37.606  1.00 23.36           C  
-ATOM   5356  CG2 VAL B 241     -17.342  33.844 -39.577  1.00 30.68           C  
-ATOM   5357  N   PRO B 242     -14.014  30.475 -38.968  1.00 20.07           N  
-ATOM   5358  CA  PRO B 242     -13.371  29.399 -38.211  1.00 20.71           C  
-ATOM   5359  C   PRO B 242     -13.299  29.716 -36.720  1.00 20.82           C  
-ATOM   5360  O   PRO B 242     -13.033  30.862 -36.364  1.00 22.17           O  
-ATOM   5361  CB  PRO B 242     -11.971  29.341 -38.820  1.00 15.01           C  
-ATOM   5362  CG  PRO B 242     -11.709  30.744 -39.240  1.00 11.78           C  
-ATOM   5363  CD  PRO B 242     -13.032  31.283 -39.714  1.00 15.38           C  
-ATOM   5364  N   TYR B 243     -13.534  28.728 -35.862  1.00 21.43           N  
-ATOM   5365  CA  TYR B 243     -13.371  28.943 -34.430  1.00 26.59           C  
-ATOM   5366  C   TYR B 243     -13.030  27.675 -33.653  1.00 26.51           C  
-ATOM   5367  O   TYR B 243     -13.099  26.562 -34.177  1.00 27.78           O  
-ATOM   5368  CB  TYR B 243     -14.623  29.601 -33.832  1.00 25.86           C  
-ATOM   5369  CG  TYR B 243     -15.953  28.966 -34.183  1.00 25.48           C  
-ATOM   5370  CD1 TYR B 243     -16.593  29.264 -35.379  1.00 25.32           C  
-ATOM   5371  CD2 TYR B 243     -16.593  28.106 -33.296  1.00 27.03           C  
-ATOM   5372  CE1 TYR B 243     -17.818  28.702 -35.696  1.00 27.95           C  
-ATOM   5373  CE2 TYR B 243     -17.820  27.541 -33.607  1.00 25.58           C  
-ATOM   5374  CZ  TYR B 243     -18.425  27.845 -34.808  1.00 22.54           C  
-ATOM   5375  OH  TYR B 243     -19.641  27.293 -35.127  1.00 22.78           O  
-ATOM   5376  N   ASP B 244     -12.645  27.874 -32.396  1.00 28.53           N  
-ATOM   5377  CA  ASP B 244     -12.230  26.797 -31.508  1.00 24.33           C  
-ATOM   5378  C   ASP B 244     -13.069  26.781 -30.241  1.00 32.65           C  
-ATOM   5379  O   ASP B 244     -13.908  27.655 -30.025  1.00 36.16           O  
-ATOM   5380  CB  ASP B 244     -10.755  26.949 -31.134  1.00 22.67           C  
-ATOM   5381  CG  ASP B 244      -9.862  25.967 -31.858  1.00 32.16           C  
-ATOM   5382  OD1 ASP B 244     -10.370  25.214 -32.717  1.00 32.49           O  
-ATOM   5383  OD2 ASP B 244      -8.646  25.954 -31.571  1.00 33.55           O  
-ATOM   5384  N   PHE B 245     -12.829  25.780 -29.405  1.00 37.51           N  
-ATOM   5385  CA  PHE B 245     -13.405  25.746 -28.070  1.00 28.47           C  
-ATOM   5386  C   PHE B 245     -12.317  25.411 -27.066  1.00 28.48           C  
-ATOM   5387  O   PHE B 245     -11.745  24.321 -27.099  1.00 25.28           O  
-ATOM   5388  CB  PHE B 245     -14.541  24.730 -27.983  1.00 22.14           C  
-ATOM   5389  CG  PHE B 245     -15.705  25.051 -28.867  1.00 31.12           C  
-ATOM   5390  CD1 PHE B 245     -16.509  26.146 -28.603  1.00 25.55           C  
-ATOM   5391  CD2 PHE B 245     -16.004  24.253 -29.959  1.00 39.76           C  
-ATOM   5392  CE1 PHE B 245     -17.585  26.444 -29.415  1.00 31.94           C  
-ATOM   5393  CE2 PHE B 245     -17.081  24.544 -30.775  1.00 34.84           C  
-ATOM   5394  CZ  PHE B 245     -17.872  25.642 -30.503  1.00 29.63           C  
-ATOM   5395  N   VAL B 246     -12.019  26.357 -26.184  1.00 28.85           N  
-ATOM   5396  CA  VAL B 246     -11.040  26.112 -25.137  1.00 28.79           C  
-ATOM   5397  C   VAL B 246     -11.643  26.310 -23.757  1.00 24.86           C  
-ATOM   5398  O   VAL B 246     -12.574  27.093 -23.581  1.00 29.01           O  
-ATOM   5399  CB  VAL B 246      -9.804  27.017 -25.279  1.00 19.27           C  
-ATOM   5400  CG1 VAL B 246      -8.990  26.603 -26.493  1.00 27.14           C  
-ATOM   5401  CG2 VAL B 246     -10.213  28.473 -25.366  1.00 19.40           C  
-ATOM   5402  N   VAL B 247     -11.117  25.574 -22.786  1.00 24.49           N  
-ATOM   5403  CA  VAL B 247     -11.510  25.738 -21.396  1.00 26.57           C  
-ATOM   5404  C   VAL B 247     -10.271  26.032 -20.559  1.00 31.96           C  
-ATOM   5405  O   VAL B 247      -9.297  25.280 -20.587  1.00 28.67           O  
-ATOM   5406  CB  VAL B 247     -12.232  24.492 -20.847  1.00 32.41           C  
-ATOM   5407  CG1 VAL B 247     -12.771  24.767 -19.451  1.00 40.45           C  
-ATOM   5408  CG2 VAL B 247     -13.357  24.075 -21.778  1.00 28.52           C  
-ATOM   5409  N   LEU B 248     -10.313  27.138 -19.827  1.00 29.17           N  
-ATOM   5410  CA  LEU B 248      -9.186  27.580 -19.015  1.00 26.36           C  
-ATOM   5411  C   LEU B 248      -9.510  27.394 -17.544  1.00 34.44           C  
-ATOM   5412  O   LEU B 248     -10.678  27.378 -17.169  1.00 42.73           O  
-ATOM   5413  CB  LEU B 248      -8.858  29.049 -19.294  1.00 30.35           C  
-ATOM   5414  CG  LEU B 248      -8.044  29.450 -20.527  1.00 29.41           C  
-ATOM   5415  CD1 LEU B 248      -8.641  28.910 -21.814  1.00 30.57           C  
-ATOM   5416  CD2 LEU B 248      -7.944  30.963 -20.595  1.00 31.20           C  
-ATOM   5417  N   GLU B 249      -8.483  27.252 -16.713  1.00 38.36           N  
-ATOM   5418  CA  GLU B 249      -8.688  27.185 -15.269  1.00 41.02           C  
-ATOM   5419  C   GLU B 249      -7.635  28.008 -14.535  1.00 46.74           C  
-ATOM   5420  O   GLU B 249      -6.523  28.193 -15.035  1.00 53.31           O  
-ATOM   5421  CB  GLU B 249      -8.663  25.735 -14.777  1.00 38.42           C  
-ATOM   5422  CG  GLU B 249      -7.282  25.092 -14.756  1.00 49.35           C  
-ATOM   5423  CD  GLU B 249      -7.280  23.751 -14.043  1.00 68.20           C  
-ATOM   5424  OE1 GLU B 249      -8.368  23.310 -13.609  1.00 64.42           O  
-ATOM   5425  OE2 GLU B 249      -6.196  23.140 -13.912  1.00 59.26           O  
-ATOM   5426  N   LYS B 250      -7.992  28.508 -13.354  1.00 39.80           N  
-ATOM   5427  CA  LYS B 250      -7.041  29.266 -12.542  1.00 38.47           C  
-ATOM   5428  C   LYS B 250      -5.980  28.373 -11.899  1.00 47.70           C  
-ATOM   5429  O   LYS B 250      -6.288  27.310 -11.359  1.00 52.42           O  
-ATOM   5430  CB  LYS B 250      -7.769  30.056 -11.454  1.00 41.07           C  
-ATOM   5431  CG  LYS B 250      -8.346  31.378 -11.927  1.00 48.05           C  
-ATOM   5432  CD  LYS B 250      -8.755  32.258 -10.753  1.00 49.22           C  
-ATOM   5433  CE  LYS B 250      -9.796  31.575  -9.881  1.00 54.23           C  
-ATOM   5434  NZ  LYS B 250     -10.276  32.472  -8.796  1.00 53.36           N  
-ATOM   5435  N   ARG B 251      -4.729  28.821 -11.958  1.00 43.44           N  
-ATOM   5436  CA  ARG B 251      -3.613  28.096 -11.358  1.00 55.48           C  
-ATOM   5437  C   ARG B 251      -2.536  29.051 -10.848  1.00 62.89           C  
-ATOM   5438  O   ARG B 251      -2.836  30.136 -10.350  1.00 54.92           O  
-ATOM   5439  CB  ARG B 251      -3.005  27.112 -12.361  1.00 56.61           C  
-ATOM   5440  CG  ARG B 251      -3.621  25.721 -12.323  1.00 63.67           C  
-ATOM   5441  CD  ARG B 251      -3.522  25.106 -10.927  1.00 81.42           C  
-ATOM   5442  NE  ARG B 251      -2.155  25.132 -10.406  1.00 91.04           N  
-ATOM   5443  CZ  ARG B 251      -1.812  25.591  -9.204  1.00 90.71           C  
-ATOM   5444  NH1 ARG B 251      -0.540  25.573  -8.826  1.00 85.40           N  
-ATOM   5445  NH2 ARG B 251      -2.735  26.068  -8.378  1.00 69.73           N  
-ATOM   5446  N   SER B 285     -12.740  -8.346 -10.887  1.00 57.66           N  
-ATOM   5447  CA  SER B 285     -12.488  -9.783 -10.861  1.00 66.72           C  
-ATOM   5448  C   SER B 285     -11.570 -10.205 -12.005  1.00 55.01           C  
-ATOM   5449  O   SER B 285     -10.518 -10.803 -11.780  1.00 55.13           O  
-ATOM   5450  CB  SER B 285     -13.804 -10.565 -10.932  1.00 71.50           C  
-ATOM   5451  OG  SER B 285     -14.606 -10.346  -9.782  1.00 75.47           O  
-ATOM   5452  N   SER B 286     -11.978  -9.886 -13.231  1.00 55.71           N  
-ATOM   5453  CA  SER B 286     -11.227 -10.271 -14.423  1.00 55.30           C  
-ATOM   5454  C   SER B 286     -10.073  -9.317 -14.699  1.00 55.83           C  
-ATOM   5455  O   SER B 286      -9.164  -9.639 -15.460  1.00 53.63           O  
-ATOM   5456  CB  SER B 286     -12.145 -10.327 -15.645  1.00 35.43           C  
-ATOM   5457  OG  SER B 286     -12.539  -9.028 -16.035  1.00 51.88           O  
-ATOM   5458  N   ALA B 287     -10.124  -8.134 -14.100  1.00 55.86           N  
-ATOM   5459  CA  ALA B 287      -9.038  -7.178 -14.237  1.00 51.33           C  
-ATOM   5460  C   ALA B 287      -7.908  -7.569 -13.294  1.00 50.83           C  
-ATOM   5461  O   ALA B 287      -6.729  -7.388 -13.597  1.00 49.69           O  
-ATOM   5462  CB  ALA B 287      -9.529  -5.767 -13.948  1.00 49.07           C  
-ATOM   5463  N   ALA B 288      -8.291  -8.123 -12.149  1.00 53.23           N  
-ATOM   5464  CA  ALA B 288      -7.338  -8.553 -11.138  1.00 55.47           C  
-ATOM   5465  C   ALA B 288      -6.562  -9.771 -11.618  1.00 51.76           C  
-ATOM   5466  O   ALA B 288      -5.371  -9.900 -11.344  1.00 48.06           O  
-ATOM   5467  CB  ALA B 288      -8.048  -8.859  -9.835  1.00 58.17           C  
-ATOM   5468  N   ALA B 289      -7.241 -10.664 -12.332  1.00 39.54           N  
-ATOM   5469  CA  ALA B 289      -6.586 -11.844 -12.883  1.00 36.50           C  
-ATOM   5470  C   ALA B 289      -5.597 -11.452 -13.975  1.00 37.60           C  
-ATOM   5471  O   ALA B 289      -4.544 -12.068 -14.129  1.00 39.79           O  
-ATOM   5472  CB  ALA B 289      -7.620 -12.824 -13.424  1.00 33.93           C  
-ATOM   5473  N   ILE B 290      -5.946 -10.415 -14.725  1.00 38.89           N  
-ATOM   5474  CA  ILE B 290      -5.132  -9.960 -15.843  1.00 34.32           C  
-ATOM   5475  C   ILE B 290      -3.912  -9.172 -15.364  1.00 38.84           C  
-ATOM   5476  O   ILE B 290      -2.819  -9.305 -15.915  1.00 33.70           O  
-ATOM   5477  CB  ILE B 290      -5.976  -9.100 -16.813  1.00 49.46           C  
-ATOM   5478  CG1 ILE B 290      -6.931  -9.994 -17.606  1.00 49.29           C  
-ATOM   5479  CG2 ILE B 290      -5.093  -8.303 -17.758  1.00 43.01           C  
-ATOM   5480  CD1 ILE B 290      -7.850  -9.237 -18.539  1.00 47.86           C  
-ATOM   5481  N   ALA B 291      -4.109  -8.389 -14.307  1.00 43.92           N  
-ATOM   5482  CA  ALA B 291      -3.115  -7.441 -13.795  1.00 43.50           C  
-ATOM   5483  C   ALA B 291      -1.677  -7.969 -13.654  1.00 40.63           C  
-ATOM   5484  O   ALA B 291      -0.748  -7.344 -14.170  1.00 39.22           O  
-ATOM   5485  CB  ALA B 291      -3.592  -6.888 -12.450  1.00 42.62           C  
-ATOM   5486  N   PRO B 292      -1.478  -9.112 -12.965  1.00 38.07           N  
-ATOM   5487  CA  PRO B 292      -0.084  -9.501 -12.714  1.00 34.49           C  
-ATOM   5488  C   PRO B 292       0.678  -9.931 -13.966  1.00 36.11           C  
-ATOM   5489  O   PRO B 292       1.888 -10.135 -13.885  1.00 44.57           O  
-ATOM   5490  CB  PRO B 292      -0.223 -10.676 -11.743  1.00 31.74           C  
-ATOM   5491  CG  PRO B 292      -1.536 -11.267 -12.070  1.00 32.85           C  
-ATOM   5492  CD  PRO B 292      -2.420 -10.105 -12.414  1.00 39.75           C  
-ATOM   5493  N   VAL B 293      -0.010 -10.068 -15.096  1.00 33.31           N  
-ATOM   5494  CA  VAL B 293       0.653 -10.411 -16.350  1.00 35.72           C  
-ATOM   5495  C   VAL B 293       1.054  -9.137 -17.085  1.00 38.48           C  
-ATOM   5496  O   VAL B 293       2.186  -9.005 -17.569  1.00 34.05           O  
-ATOM   5497  CB  VAL B 293      -0.248 -11.276 -17.249  1.00 36.26           C  
-ATOM   5498  CG1 VAL B 293       0.505 -11.709 -18.494  1.00 29.84           C  
-ATOM   5499  CG2 VAL B 293      -0.748 -12.489 -16.482  1.00 29.56           C  
-ATOM   5500  N   LEU B 294       0.112  -8.200 -17.154  1.00 41.79           N  
-ATOM   5501  CA  LEU B 294       0.380  -6.861 -17.656  1.00 34.87           C  
-ATOM   5502  C   LEU B 294       1.556  -6.247 -16.919  1.00 38.76           C  
-ATOM   5503  O   LEU B 294       2.367  -5.535 -17.509  1.00 49.59           O  
-ATOM   5504  CB  LEU B 294      -0.850  -5.969 -17.499  1.00 32.71           C  
-ATOM   5505  CG  LEU B 294      -2.054  -6.306 -18.375  1.00 38.12           C  
-ATOM   5506  CD1 LEU B 294      -3.138  -5.256 -18.205  1.00 51.39           C  
-ATOM   5507  CD2 LEU B 294      -1.629  -6.410 -19.824  1.00 35.48           C  
-ATOM   5508  N   ALA B 295       1.637  -6.537 -15.623  1.00 37.44           N  
-ATOM   5509  CA  ALA B 295       2.723  -6.048 -14.783  1.00 46.97           C  
-ATOM   5510  C   ALA B 295       4.085  -6.419 -15.365  1.00 51.41           C  
-ATOM   5511  O   ALA B 295       4.855  -5.543 -15.766  1.00 55.50           O  
-ATOM   5512  CB  ALA B 295       2.586  -6.593 -13.368  1.00 40.13           C  
-ATOM   5513  N   TRP B 296       4.371  -7.718 -15.427  1.00 47.66           N  
-ATOM   5514  CA  TRP B 296       5.679  -8.179 -15.880  1.00 46.45           C  
-ATOM   5515  C   TRP B 296       5.891  -7.907 -17.361  1.00 40.00           C  
-ATOM   5516  O   TRP B 296       7.027  -7.760 -17.808  1.00 48.74           O  
-ATOM   5517  CB  TRP B 296       5.875  -9.673 -15.585  1.00 46.54           C  
-ATOM   5518  CG  TRP B 296       5.147 -10.636 -16.491  1.00 40.18           C  
-ATOM   5519  CD1 TRP B 296       3.971 -11.275 -16.230  1.00 41.98           C  
-ATOM   5520  CD2 TRP B 296       5.571 -11.094 -17.785  1.00 36.62           C  
-ATOM   5521  NE1 TRP B 296       3.627 -12.088 -17.284  1.00 31.05           N  
-ATOM   5522  CE2 TRP B 296       4.592 -11.994 -18.251  1.00 32.36           C  
-ATOM   5523  CE3 TRP B 296       6.678 -10.822 -18.596  1.00 34.68           C  
-ATOM   5524  CZ2 TRP B 296       4.686 -12.623 -19.489  1.00 33.80           C  
-ATOM   5525  CZ3 TRP B 296       6.768 -11.445 -19.827  1.00 30.68           C  
-ATOM   5526  CH2 TRP B 296       5.777 -12.335 -20.261  1.00 34.19           C  
-ATOM   5527  N   MET B 297       4.808  -7.839 -18.127  1.00 35.97           N  
-ATOM   5528  CA  MET B 297       4.943  -7.521 -19.543  1.00 39.93           C  
-ATOM   5529  C   MET B 297       5.336  -6.061 -19.746  1.00 49.23           C  
-ATOM   5530  O   MET B 297       5.996  -5.723 -20.728  1.00 46.52           O  
-ATOM   5531  CB  MET B 297       3.650  -7.836 -20.290  1.00 42.62           C  
-ATOM   5532  CG  MET B 297       3.535  -9.292 -20.693  1.00 27.98           C  
-ATOM   5533  SD  MET B 297       1.932  -9.702 -21.394  1.00 30.60           S  
-ATOM   5534  CE  MET B 297       2.191 -11.426 -21.800  1.00 33.32           C  
-ATOM   5535  N   ASP B 298       4.942  -5.198 -18.812  1.00 58.14           N  
-ATOM   5536  CA  ASP B 298       5.272  -3.781 -18.921  1.00 65.50           C  
-ATOM   5537  C   ASP B 298       6.625  -3.447 -18.297  1.00 61.15           C  
-ATOM   5538  O   ASP B 298       7.329  -2.567 -18.790  1.00 65.95           O  
-ATOM   5539  CB  ASP B 298       4.188  -2.914 -18.277  1.00 51.07           C  
-ATOM   5540  CG  ASP B 298       4.436  -1.431 -18.491  1.00 66.77           C  
-ATOM   5541  OD1 ASP B 298       4.959  -1.069 -19.568  1.00 81.15           O  
-ATOM   5542  OD2 ASP B 298       4.118  -0.628 -17.590  1.00 80.47           O  
-ATOM   5543  N   GLU B 299       6.963  -4.150 -17.215  1.00 62.56           N  
-ATOM   5544  CA  GLU B 299       8.190  -3.921 -16.439  1.00 64.89           C  
-ATOM   5545  C   GLU B 299       9.404  -3.518 -17.271  1.00 69.13           C  
-ATOM   5546  O   GLU B 299       9.972  -2.442 -17.082  1.00 72.52           O  
-ATOM   5547  CB  GLU B 299       8.540  -5.175 -15.635  1.00 58.58           C  
-ATOM   5548  CG  GLU B 299       7.699  -5.379 -14.391  1.00 71.61           C  
-ATOM   5549  CD  GLU B 299       8.058  -6.659 -13.663  1.00 74.25           C  
-ATOM   5550  OE1 GLU B 299       9.066  -7.295 -14.045  1.00 59.83           O  
-ATOM   5551  OE2 GLU B 299       7.332  -7.030 -12.716  1.00 63.35           O  
-ATOM   5552  N   GLU B 300       9.797  -4.393 -18.188  1.00 70.68           N  
-ATOM   5553  CA  GLU B 300      10.895  -4.109 -19.101  1.00 81.80           C  
-ATOM   5554  C   GLU B 300      10.349  -3.845 -20.502  1.00 80.91           C  
-ATOM   5555  O   GLU B 300       9.771  -4.736 -21.126  1.00 79.08           O  
-ATOM   5556  CB  GLU B 300      11.897  -5.268 -19.109  1.00 87.71           C  
-ATOM   5557  CG  GLU B 300      12.736  -5.388 -20.373  1.00 93.17           C  
-ATOM   5558  CD  GLU B 300      12.321  -6.571 -21.232  1.00 85.46           C  
-ATOM   5559  OE1 GLU B 300      12.801  -6.671 -22.383  1.00 66.36           O  
-ATOM   5560  OE2 GLU B 300      11.519  -7.403 -20.755  1.00 83.69           O  
-ATOM   5561  N   ASP B 301      10.511  -2.616 -20.985  1.00 73.01           N  
-ATOM   5562  CA  ASP B 301      11.186  -1.563 -20.231  1.00 71.16           C  
-ATOM   5563  C   ASP B 301      10.173  -0.638 -19.561  1.00 56.21           C  
-ATOM   5564  O   ASP B 301       9.088  -0.397 -20.095  1.00 38.34           O  
-ATOM   5565  CB  ASP B 301      12.112  -0.759 -21.151  1.00 90.51           C  
-ATOM   5566  CG  ASP B 301      13.336  -0.219 -20.428  1.00 90.90           C  
-ATOM   5567  OD1 ASP B 301      14.356  -0.939 -20.369  1.00 81.94           O  
-ATOM   5568  OD2 ASP B 301      13.282   0.925 -19.927  1.00 75.74           O  
-ATOM   5569  N   LYS B 308      14.522   9.161 -20.836  1.00 58.49           N  
-ATOM   5570  CA  LYS B 308      14.638   9.146 -19.384  1.00 62.31           C  
-ATOM   5571  C   LYS B 308      13.551  10.010 -18.753  1.00 57.46           C  
-ATOM   5572  O   LYS B 308      12.777   9.543 -17.917  1.00 45.85           O  
-ATOM   5573  CB  LYS B 308      16.027   9.623 -18.955  1.00 56.28           C  
-ATOM   5574  CG  LYS B 308      16.593   8.880 -17.755  1.00 58.48           C  
-ATOM   5575  CD  LYS B 308      16.729   7.390 -18.042  1.00 64.75           C  
-ATOM   5576  CE  LYS B 308      15.780   6.563 -17.184  1.00 63.28           C  
-ATOM   5577  NZ  LYS B 308      15.893   5.109 -17.486  1.00 68.22           N  
-ATOM   5578  N   GLU B 309      13.506  11.275 -19.160  1.00 50.12           N  
-ATOM   5579  CA  GLU B 309      12.422  12.169 -18.769  1.00 59.74           C  
-ATOM   5580  C   GLU B 309      11.632  12.591 -20.006  1.00 60.70           C  
-ATOM   5581  O   GLU B 309      12.101  13.389 -20.819  1.00 51.63           O  
-ATOM   5582  CB  GLU B 309      12.961  13.392 -18.023  1.00 66.11           C  
-ATOM   5583  CG  GLU B 309      12.382  13.557 -16.623  1.00 71.31           C  
-ATOM   5584  CD  GLU B 309      12.949  14.759 -15.890  1.00 81.12           C  
-ATOM   5585  OE1 GLU B 309      14.148  14.735 -15.536  1.00 74.21           O  
-ATOM   5586  OE2 GLU B 309      12.193  15.729 -15.668  1.00 81.11           O  
-ATOM   5587  N   LEU B 310      10.432  12.034 -20.135  1.00 61.24           N  
-ATOM   5588  CA  LEU B 310       9.589  12.227 -21.308  1.00 49.33           C  
-ATOM   5589  C   LEU B 310       9.188  13.681 -21.505  1.00 45.21           C  
-ATOM   5590  O   LEU B 310       8.620  14.299 -20.605  1.00 55.22           O  
-ATOM   5591  CB  LEU B 310       8.329  11.367 -21.194  1.00 52.13           C  
-ATOM   5592  CG  LEU B 310       8.514   9.908 -20.783  1.00 37.11           C  
-ATOM   5593  CD1 LEU B 310       7.314   9.432 -19.979  1.00 42.46           C  
-ATOM   5594  CD2 LEU B 310       8.727   9.029 -22.005  1.00 28.99           C  
-ATOM   5595  N   ILE B 311       9.479  14.224 -22.684  1.00 45.51           N  
-ATOM   5596  CA  ILE B 311       8.974  15.542 -23.046  1.00 47.10           C  
-ATOM   5597  C   ILE B 311       7.569  15.371 -23.615  1.00 41.37           C  
-ATOM   5598  O   ILE B 311       7.224  14.304 -24.128  1.00 31.20           O  
-ATOM   5599  CB  ILE B 311       9.889  16.268 -24.067  1.00 42.31           C  
-ATOM   5600  CG1 ILE B 311       9.526  15.902 -25.507  1.00 39.49           C  
-ATOM   5601  CG2 ILE B 311      11.352  15.964 -23.792  1.00 47.47           C  
-ATOM   5602  CD1 ILE B 311       8.928  17.051 -26.295  1.00 38.39           C  
-ATOM   5603  N   ARG B 312       6.753  16.413 -23.514  1.00 37.41           N  
-ATOM   5604  CA  ARG B 312       5.374  16.323 -23.971  1.00 34.85           C  
-ATOM   5605  C   ARG B 312       4.825  17.692 -24.349  1.00 38.45           C  
-ATOM   5606  O   ARG B 312       5.102  18.689 -23.682  1.00 37.73           O  
-ATOM   5607  CB  ARG B 312       4.504  15.673 -22.892  1.00 37.07           C  
-ATOM   5608  CG  ARG B 312       3.039  15.525 -23.262  1.00 42.91           C  
-ATOM   5609  CD  ARG B 312       2.369  14.466 -22.403  1.00 49.76           C  
-ATOM   5610  NE  ARG B 312       0.911  14.505 -22.494  1.00 55.02           N  
-ATOM   5611  CZ  ARG B 312       0.200  13.906 -23.445  1.00 59.95           C  
-ATOM   5612  NH1 ARG B 312      -1.123  13.995 -23.438  1.00 53.48           N  
-ATOM   5613  NH2 ARG B 312       0.809  13.223 -24.407  1.00 55.97           N  
-ATOM   5614  N   ALA B 313       4.055  17.734 -25.431  1.00 35.41           N  
-ATOM   5615  CA  ALA B 313       3.439  18.973 -25.886  1.00 36.11           C  
-ATOM   5616  C   ALA B 313       2.386  19.450 -24.898  1.00 34.37           C  
-ATOM   5617  O   ALA B 313       1.439  18.720 -24.608  1.00 31.11           O  
-ATOM   5618  CB  ALA B 313       2.822  18.786 -27.257  1.00 33.52           C  
-ATOM   5619  N   VAL B 314       2.560  20.684 -24.420  1.00 31.06           N  
-ATOM   5620  CA  VAL B 314       1.694  21.336 -23.429  1.00 27.39           C  
-ATOM   5621  C   VAL B 314       0.875  20.371 -22.568  1.00 35.08           C  
-ATOM   5622  O   VAL B 314      -0.339  20.256 -22.736  1.00 37.94           O  
-ATOM   5623  CB  VAL B 314       0.735  22.346 -24.110  1.00 28.27           C  
-ATOM   5624  CG1 VAL B 314       1.481  23.626 -24.441  1.00 32.09           C  
-ATOM   5625  CG2 VAL B 314       0.100  21.757 -25.369  1.00 27.25           C  
-ATOM   5626  N   PRO B 315       1.547  19.680 -21.633  1.00 36.27           N  
-ATOM   5627  CA  PRO B 315       0.959  18.599 -20.829  1.00 42.48           C  
-ATOM   5628  C   PRO B 315      -0.247  19.027 -19.995  1.00 31.27           C  
-ATOM   5629  O   PRO B 315      -1.065  18.183 -19.627  1.00 27.69           O  
-ATOM   5630  CB  PRO B 315       2.118  18.173 -19.918  1.00 37.85           C  
-ATOM   5631  CG  PRO B 315       3.009  19.360 -19.862  1.00 35.27           C  
-ATOM   5632  CD  PRO B 315       2.927  19.981 -21.220  1.00 33.23           C  
-ATOM   5633  N   HIS B 316      -0.356  20.318 -19.708  1.00 29.89           N  
-ATOM   5634  CA  HIS B 316      -1.469  20.832 -18.917  1.00 37.57           C  
-ATOM   5635  C   HIS B 316      -2.796  20.723 -19.664  1.00 37.20           C  
-ATOM   5636  O   HIS B 316      -3.862  20.819 -19.064  1.00 44.94           O  
-ATOM   5637  CB  HIS B 316      -1.212  22.285 -18.515  1.00 43.77           C  
-ATOM   5638  CG  HIS B 316      -0.790  23.160 -19.653  1.00 46.26           C  
-ATOM   5639  ND1 HIS B 316       0.531  23.442 -19.926  1.00 42.40           N  
-ATOM   5640  CD2 HIS B 316      -1.515  23.815 -20.591  1.00 43.32           C  
-ATOM   5641  CE1 HIS B 316       0.602  24.233 -20.981  1.00 41.32           C  
-ATOM   5642  NE2 HIS B 316      -0.626  24.475 -21.404  1.00 39.04           N  
-ATOM   5643  N   VAL B 317      -2.729  20.524 -20.974  1.00 37.48           N  
-ATOM   5644  CA  VAL B 317      -3.933  20.343 -21.774  1.00 39.31           C  
-ATOM   5645  C   VAL B 317      -4.331  18.874 -21.798  1.00 42.09           C  
-ATOM   5646  O   VAL B 317      -3.748  18.080 -22.534  1.00 42.04           O  
-ATOM   5647  CB  VAL B 317      -3.742  20.841 -23.217  1.00 42.73           C  
-ATOM   5648  CG1 VAL B 317      -5.024  20.650 -24.020  1.00 40.86           C  
-ATOM   5649  CG2 VAL B 317      -3.314  22.299 -23.223  1.00 31.76           C  
-ATOM   5650  N   HIS B 318      -5.325  18.516 -20.992  1.00 51.08           N  
-ATOM   5651  CA  HIS B 318      -5.761  17.126 -20.903  1.00 53.37           C  
-ATOM   5652  C   HIS B 318      -6.634  16.716 -22.083  1.00 44.68           C  
-ATOM   5653  O   HIS B 318      -6.472  15.626 -22.626  1.00 48.11           O  
-ATOM   5654  CB  HIS B 318      -6.501  16.877 -19.587  1.00 59.85           C  
-ATOM   5655  CG  HIS B 318      -5.652  16.231 -18.537  1.00 69.98           C  
-ATOM   5656  ND1 HIS B 318      -5.425  14.872 -18.498  1.00 73.83           N  
-ATOM   5657  CD2 HIS B 318      -4.973  16.756 -17.489  1.00 65.97           C  
-ATOM   5658  CE1 HIS B 318      -4.645  14.587 -17.471  1.00 78.19           C  
-ATOM   5659  NE2 HIS B 318      -4.357  15.713 -16.842  1.00 73.09           N  
-ATOM   5660  N   PHE B 319      -7.559  17.583 -22.482  1.00 46.23           N  
-ATOM   5661  CA  PHE B 319      -8.443  17.251 -23.598  1.00 47.61           C  
-ATOM   5662  C   PHE B 319      -7.959  17.901 -24.893  1.00 41.48           C  
-ATOM   5663  O   PHE B 319      -8.211  19.078 -25.151  1.00 37.17           O  
-ATOM   5664  CB  PHE B 319      -9.880  17.663 -23.281  1.00 47.97           C  
-ATOM   5665  CG  PHE B 319     -10.348  17.215 -21.924  1.00 69.64           C  
-ATOM   5666  CD1 PHE B 319     -10.720  15.898 -21.704  1.00 73.30           C  
-ATOM   5667  CD2 PHE B 319     -10.404  18.108 -20.864  1.00 65.63           C  
-ATOM   5668  CE1 PHE B 319     -11.143  15.480 -20.453  1.00 68.86           C  
-ATOM   5669  CE2 PHE B 319     -10.828  17.696 -19.613  1.00 67.81           C  
-ATOM   5670  CZ  PHE B 319     -11.198  16.381 -19.408  1.00 72.91           C  
-ATOM   5671  N   ARG B 320      -7.272  17.103 -25.705  1.00 34.87           N  
-ATOM   5672  CA  ARG B 320      -6.522  17.602 -26.850  1.00 30.28           C  
-ATOM   5673  C   ARG B 320      -7.201  17.294 -28.180  1.00 24.19           C  
-ATOM   5674  O   ARG B 320      -6.765  16.412 -28.918  1.00 21.60           O  
-ATOM   5675  CB  ARG B 320      -5.116  17.005 -26.831  1.00 30.48           C  
-ATOM   5676  CG  ARG B 320      -4.338  17.346 -25.571  1.00 31.50           C  
-ATOM   5677  CD  ARG B 320      -3.368  16.245 -25.190  1.00 31.77           C  
-ATOM   5678  NE  ARG B 320      -2.032  16.772 -24.934  1.00 33.07           N  
-ATOM   5679  CZ  ARG B 320      -1.008  16.642 -25.771  1.00 35.40           C  
-ATOM   5680  NH1 ARG B 320       0.174  17.152 -25.459  1.00 33.47           N  
-ATOM   5681  NH2 ARG B 320      -1.164  15.993 -26.917  1.00 33.47           N  
-ATOM   5682  N   GLY B 321      -8.258  18.039 -28.487  1.00 25.27           N  
-ATOM   5683  CA  GLY B 321      -9.042  17.801 -29.686  1.00 24.47           C  
-ATOM   5684  C   GLY B 321      -8.447  18.394 -30.948  1.00 19.81           C  
-ATOM   5685  O   GLY B 321      -8.776  17.963 -32.052  1.00 24.28           O  
-ATOM   5686  N   HIS B 322      -7.575  19.385 -30.790  1.00 16.67           N  
-ATOM   5687  CA  HIS B 322      -6.945  20.040 -31.931  1.00 21.35           C  
-ATOM   5688  C   HIS B 322      -6.129  19.039 -32.742  1.00 25.85           C  
-ATOM   5689  O   HIS B 322      -5.427  18.201 -32.178  1.00 34.29           O  
-ATOM   5690  CB  HIS B 322      -6.057  21.195 -31.466  1.00 24.28           C  
-ATOM   5691  CG  HIS B 322      -5.864  22.263 -32.497  1.00 30.51           C  
-ATOM   5692  ND1 HIS B 322      -5.201  22.040 -33.685  1.00 21.58           N  
-ATOM   5693  CD2 HIS B 322      -6.246  23.562 -32.517  1.00 26.34           C  
-ATOM   5694  CE1 HIS B 322      -5.185  23.156 -34.393  1.00 18.20           C  
-ATOM   5695  NE2 HIS B 322      -5.812  24.094 -33.706  1.00 19.36           N  
-ATOM   5696  N   GLU B 323      -6.222  19.128 -34.065  1.00 20.84           N  
-ATOM   5697  CA  GLU B 323      -5.573  18.156 -34.939  1.00 19.92           C  
-ATOM   5698  C   GLU B 323      -4.065  18.395 -35.071  1.00 25.59           C  
-ATOM   5699  O   GLU B 323      -3.343  17.535 -35.575  1.00 26.29           O  
-ATOM   5700  CB  GLU B 323      -6.236  18.164 -36.321  1.00 24.29           C  
-ATOM   5701  CG  GLU B 323      -7.651  17.589 -36.325  1.00 21.63           C  
-ATOM   5702  CD  GLU B 323      -8.296  17.588 -37.703  1.00 27.00           C  
-ATOM   5703  OE1 GLU B 323      -9.446  17.112 -37.818  1.00 27.60           O  
-ATOM   5704  OE2 GLU B 323      -7.661  18.062 -38.669  1.00 25.38           O  
-ATOM   5705  N   GLU B 324      -3.593  19.551 -34.608  1.00 20.45           N  
-ATOM   5706  CA  GLU B 324      -2.165  19.875 -34.636  1.00 16.30           C  
-ATOM   5707  C   GLU B 324      -1.407  19.071 -33.573  1.00 27.11           C  
-ATOM   5708  O   GLU B 324      -0.181  18.873 -33.653  1.00 34.44           O  
-ATOM   5709  CB  GLU B 324      -1.961  21.379 -34.434  1.00 14.28           C  
-ATOM   5710  CG  GLU B 324      -0.511  21.834 -34.477  1.00 12.83           C  
-ATOM   5711  CD  GLU B 324      -0.368  23.296 -34.854  1.00 18.38           C  
-ATOM   5712  OE1 GLU B 324       0.774  23.804 -34.870  1.00 15.54           O  
-ATOM   5713  OE2 GLU B 324      -1.399  23.936 -35.145  1.00 21.90           O  
-ATOM   5714  N   PHE B 325      -2.155  18.592 -32.584  1.00 24.48           N  
-ATOM   5715  CA  PHE B 325      -1.602  17.730 -31.551  1.00 19.75           C  
-ATOM   5716  C   PHE B 325      -1.050  16.446 -32.155  1.00 23.39           C  
-ATOM   5717  O   PHE B 325      -0.229  15.776 -31.540  1.00 30.16           O  
-ATOM   5718  CB  PHE B 325      -2.657  17.405 -30.492  1.00 25.20           C  
-ATOM   5719  CG  PHE B 325      -2.863  18.497 -29.484  1.00 24.31           C  
-ATOM   5720  CD1 PHE B 325      -1.842  18.858 -28.622  1.00 22.19           C  
-ATOM   5721  CD2 PHE B 325      -4.078  19.153 -29.388  1.00 24.32           C  
-ATOM   5722  CE1 PHE B 325      -2.025  19.861 -27.687  1.00 28.72           C  
-ATOM   5723  CE2 PHE B 325      -4.270  20.156 -28.454  1.00 28.75           C  
-ATOM   5724  CZ  PHE B 325      -3.242  20.511 -27.602  1.00 32.00           C  
-ATOM   5725  N   GLN B 326      -1.510  16.100 -33.353  1.00 19.84           N  
-ATOM   5726  CA  GLN B 326      -0.919  14.993 -34.090  1.00 23.44           C  
-ATOM   5727  C   GLN B 326       0.547  15.296 -34.351  1.00 22.66           C  
-ATOM   5728  O   GLN B 326       1.428  14.478 -34.080  1.00 27.51           O  
-ATOM   5729  CB  GLN B 326      -1.651  14.753 -35.411  1.00 21.95           C  
-ATOM   5730  CG  GLN B 326      -3.083  14.283 -35.264  1.00 12.71           C  
-ATOM   5731  CD  GLN B 326      -3.691  13.883 -36.593  1.00 18.75           C  
-ATOM   5732  OE1 GLN B 326      -3.407  12.808 -37.122  1.00 16.48           O  
-ATOM   5733  NE2 GLN B 326      -4.527  14.753 -37.146  1.00 29.19           N  
-ATOM   5734  N   TYR B 327       0.790  16.493 -34.872  1.00 18.56           N  
-ATOM   5735  CA  TYR B 327       2.135  16.947 -35.194  1.00 17.04           C  
-ATOM   5736  C   TYR B 327       2.995  17.106 -33.947  1.00 22.81           C  
-ATOM   5737  O   TYR B 327       4.123  16.603 -33.890  1.00 25.22           O  
-ATOM   5738  CB  TYR B 327       2.068  18.269 -35.961  1.00 12.48           C  
-ATOM   5739  CG  TYR B 327       3.412  18.881 -36.262  1.00 14.52           C  
-ATOM   5740  CD1 TYR B 327       4.194  18.407 -37.308  1.00 20.94           C  
-ATOM   5741  CD2 TYR B 327       3.898  19.939 -35.507  1.00 14.15           C  
-ATOM   5742  CE1 TYR B 327       5.424  18.964 -37.589  1.00 17.83           C  
-ATOM   5743  CE2 TYR B 327       5.127  20.504 -35.782  1.00 18.76           C  
-ATOM   5744  CZ  TYR B 327       5.885  20.013 -36.823  1.00 20.24           C  
-ATOM   5745  OH  TYR B 327       7.108  20.577 -37.099  1.00 31.80           O  
-ATOM   5746  N   LEU B 328       2.463  17.806 -32.950  1.00 20.10           N  
-ATOM   5747  CA  LEU B 328       3.207  18.015 -31.712  1.00 21.92           C  
-ATOM   5748  C   LEU B 328       3.573  16.690 -31.035  1.00 26.42           C  
-ATOM   5749  O   LEU B 328       4.736  16.470 -30.671  1.00 32.85           O  
-ATOM   5750  CB  LEU B 328       2.404  18.898 -30.762  1.00 21.18           C  
-ATOM   5751  CG  LEU B 328       2.112  20.302 -31.291  1.00 15.12           C  
-ATOM   5752  CD1 LEU B 328       1.261  21.082 -30.309  1.00 21.41           C  
-ATOM   5753  CD2 LEU B 328       3.406  21.040 -31.584  1.00 17.05           C  
-ATOM   5754  N   ASP B 329       2.589  15.806 -30.883  1.00 23.66           N  
-ATOM   5755  CA  ASP B 329       2.833  14.488 -30.303  1.00 22.32           C  
-ATOM   5756  C   ASP B 329       3.766  13.661 -31.169  1.00 26.45           C  
-ATOM   5757  O   ASP B 329       4.431  12.761 -30.671  1.00 32.10           O  
-ATOM   5758  CB  ASP B 329       1.530  13.713 -30.097  1.00 30.17           C  
-ATOM   5759  CG  ASP B 329       0.682  14.280 -28.982  1.00 40.56           C  
-ATOM   5760  OD1 ASP B 329       1.154  15.209 -28.292  1.00 41.17           O  
-ATOM   5761  OD2 ASP B 329      -0.465  13.810 -28.811  1.00 31.64           O  
-ATOM   5762  N   LEU B 330       3.786  13.936 -32.469  1.00 25.85           N  
-ATOM   5763  CA  LEU B 330       4.721  13.261 -33.359  1.00 23.17           C  
-ATOM   5764  C   LEU B 330       6.134  13.678 -33.001  1.00 24.82           C  
-ATOM   5765  O   LEU B 330       7.019  12.838 -32.846  1.00 31.52           O  
-ATOM   5766  CB  LEU B 330       4.421  13.578 -34.828  1.00 22.81           C  
-ATOM   5767  CG  LEU B 330       5.454  13.072 -35.840  1.00 23.04           C  
-ATOM   5768  CD1 LEU B 330       5.659  11.569 -35.712  1.00 18.94           C  
-ATOM   5769  CD2 LEU B 330       5.043  13.442 -37.259  1.00 16.99           C  
-ATOM   5770  N   ILE B 331       6.333  14.985 -32.860  1.00 23.67           N  
-ATOM   5771  CA  ILE B 331       7.631  15.516 -32.459  1.00 25.70           C  
-ATOM   5772  C   ILE B 331       8.077  14.902 -31.138  1.00 26.18           C  
-ATOM   5773  O   ILE B 331       9.196  14.383 -31.024  1.00 21.66           O  
-ATOM   5774  CB  ILE B 331       7.605  17.051 -32.314  1.00 27.82           C  
-ATOM   5775  CG1 ILE B 331       7.204  17.703 -33.639  1.00 29.36           C  
-ATOM   5776  CG2 ILE B 331       8.958  17.560 -31.839  1.00 23.94           C  
-ATOM   5777  CD1 ILE B 331       7.732  19.120 -33.812  1.00 24.85           C  
-ATOM   5778  N   ALA B 332       7.186  14.949 -30.150  1.00 32.18           N  
-ATOM   5779  CA  ALA B 332       7.472  14.382 -28.838  1.00 28.98           C  
-ATOM   5780  C   ALA B 332       7.850  12.908 -28.938  1.00 33.04           C  
-ATOM   5781  O   ALA B 332       8.833  12.475 -28.343  1.00 37.47           O  
-ATOM   5782  CB  ALA B 332       6.279  14.560 -27.914  1.00 30.69           C  
-ATOM   5783  N   ASP B 333       7.071  12.146 -29.700  1.00 31.32           N  
-ATOM   5784  CA  ASP B 333       7.290  10.711 -29.833  1.00 37.52           C  
-ATOM   5785  C   ASP B 333       8.626  10.413 -30.495  1.00 38.37           C  
-ATOM   5786  O   ASP B 333       9.284   9.432 -30.162  1.00 42.40           O  
-ATOM   5787  CB  ASP B 333       6.160  10.053 -30.630  1.00 37.09           C  
-ATOM   5788  CG  ASP B 333       6.328   8.545 -30.738  1.00 57.76           C  
-ATOM   5789  OD1 ASP B 333       6.604   7.899 -29.702  1.00 50.01           O  
-ATOM   5790  OD2 ASP B 333       6.195   8.008 -31.859  1.00 59.80           O  
-ATOM   5791  N   ILE B 334       9.023  11.255 -31.440  1.00 29.99           N  
-ATOM   5792  CA  ILE B 334      10.293  11.053 -32.118  1.00 24.37           C  
-ATOM   5793  C   ILE B 334      11.447  11.374 -31.177  1.00 29.37           C  
-ATOM   5794  O   ILE B 334      12.429  10.635 -31.120  1.00 33.15           O  
-ATOM   5795  CB  ILE B 334      10.399  11.911 -33.392  1.00 26.42           C  
-ATOM   5796  CG1 ILE B 334       9.380  11.434 -34.421  1.00 22.16           C  
-ATOM   5797  CG2 ILE B 334      11.797  11.834 -33.974  1.00 19.81           C  
-ATOM   5798  CD1 ILE B 334       9.319  12.291 -35.648  1.00 20.58           C  
-ATOM   5799  N   ILE B 335      11.324  12.466 -30.429  1.00 34.63           N  
-ATOM   5800  CA  ILE B 335      12.393  12.859 -29.514  1.00 33.20           C  
-ATOM   5801  C   ILE B 335      12.558  11.842 -28.380  1.00 32.45           C  
-ATOM   5802  O   ILE B 335      13.679  11.517 -27.990  1.00 38.86           O  
-ATOM   5803  CB  ILE B 335      12.145  14.269 -28.935  1.00 26.40           C  
-ATOM   5804  CG1 ILE B 335      12.442  15.329 -30.000  1.00 22.03           C  
-ATOM   5805  CG2 ILE B 335      13.011  14.515 -27.715  1.00 23.19           C  
-ATOM   5806  CD1 ILE B 335      12.251  16.751 -29.522  1.00 24.03           C  
-ATOM   5807  N   ASN B 336      11.445  11.316 -27.879  1.00 35.05           N  
-ATOM   5808  CA  ASN B 336      11.476  10.386 -26.753  1.00 29.23           C  
-ATOM   5809  C   ASN B 336      11.768   8.937 -27.139  1.00 30.97           C  
-ATOM   5810  O   ASN B 336      12.397   8.206 -26.376  1.00 40.89           O  
-ATOM   5811  CB  ASN B 336      10.149  10.439 -25.990  1.00 25.40           C  
-ATOM   5812  CG  ASN B 336       9.914  11.778 -25.316  1.00 34.34           C  
-ATOM   5813  OD1 ASN B 336      10.856  12.462 -24.919  1.00 39.85           O  
-ATOM   5814  ND2 ASN B 336       8.649  12.158 -25.183  1.00 30.38           N  
-ATOM   5815  N   ASN B 337      11.315   8.521 -28.318  1.00 32.99           N  
-ATOM   5816  CA  ASN B 337      11.360   7.108 -28.691  1.00 35.33           C  
-ATOM   5817  C   ASN B 337      12.075   6.806 -30.007  1.00 32.78           C  
-ATOM   5818  O   ASN B 337      12.025   5.678 -30.500  1.00 32.85           O  
-ATOM   5819  CB  ASN B 337       9.937   6.556 -28.760  1.00 33.02           C  
-ATOM   5820  CG  ASN B 337       9.141   6.848 -27.506  1.00 42.16           C  
-ATOM   5821  OD1 ASN B 337       9.654   6.745 -26.391  1.00 35.82           O  
-ATOM   5822  ND2 ASN B 337       7.881   7.227 -27.681  1.00 49.19           N  
-ATOM   5823  N   GLY B 338      12.741   7.805 -30.574  1.00 32.65           N  
-ATOM   5824  CA  GLY B 338      13.450   7.611 -31.825  1.00 29.20           C  
-ATOM   5825  C   GLY B 338      14.862   7.113 -31.595  1.00 38.86           C  
-ATOM   5826  O   GLY B 338      15.323   7.048 -30.455  1.00 45.31           O  
-ATOM   5827  N   ARG B 339      15.548   6.753 -32.676  1.00 46.29           N  
-ATOM   5828  CA  ARG B 339      16.945   6.333 -32.593  1.00 39.70           C  
-ATOM   5829  C   ARG B 339      17.848   7.406 -33.187  1.00 36.11           C  
-ATOM   5830  O   ARG B 339      17.504   8.019 -34.195  1.00 34.84           O  
-ATOM   5831  CB  ARG B 339      17.163   5.000 -33.318  1.00 35.97           C  
-ATOM   5832  CG  ARG B 339      16.480   3.800 -32.680  1.00 31.67           C  
-ATOM   5833  CD  ARG B 339      17.043   3.489 -31.300  1.00 39.91           C  
-ATOM   5834  NE  ARG B 339      16.265   4.110 -30.231  1.00 71.33           N  
-ATOM   5835  CZ  ARG B 339      16.561   4.011 -28.939  1.00 88.36           C  
-ATOM   5836  NH1 ARG B 339      17.624   3.317 -28.552  1.00 71.66           N  
-ATOM   5837  NH2 ARG B 339      15.796   4.608 -28.032  1.00 86.89           N  
-ATOM   5838  N   THR B 340      19.000   7.632 -32.565  1.00 27.28           N  
-ATOM   5839  CA  THR B 340      19.953   8.612 -33.072  1.00 32.04           C  
-ATOM   5840  C   THR B 340      20.798   8.022 -34.199  1.00 40.04           C  
-ATOM   5841  O   THR B 340      21.566   7.085 -33.985  1.00 37.97           O  
-ATOM   5842  CB  THR B 340      20.873   9.125 -31.959  1.00 36.29           C  
-ATOM   5843  OG1 THR B 340      20.085   9.769 -30.952  1.00 30.84           O  
-ATOM   5844  CG2 THR B 340      21.890  10.111 -32.521  1.00 31.29           C  
-ATOM   5845  N   MET B 341      20.651   8.581 -35.396  1.00 38.90           N  
-ATOM   5846  CA  MET B 341      21.302   8.051 -36.588  1.00 39.61           C  
-ATOM   5847  C   MET B 341      22.106   9.116 -37.321  1.00 36.84           C  
-ATOM   5848  O   MET B 341      21.985  10.310 -37.037  1.00 36.40           O  
-ATOM   5849  CB  MET B 341      20.264   7.464 -37.546  1.00 37.41           C  
-ATOM   5850  CG  MET B 341      19.245   6.548 -36.896  1.00 36.04           C  
-ATOM   5851  SD  MET B 341      19.960   4.966 -36.431  1.00 40.83           S  
-ATOM   5852  CE  MET B 341      20.595   4.417 -38.013  1.00 42.64           C  
-ATOM   5853  N   ASP B 342      22.921   8.668 -38.272  1.00 39.31           N  
-ATOM   5854  CA  ASP B 342      23.599   9.565 -39.201  1.00 42.59           C  
-ATOM   5855  C   ASP B 342      22.752   9.712 -40.461  1.00 49.33           C  
-ATOM   5856  O   ASP B 342      21.672   9.128 -40.558  1.00 49.54           O  
-ATOM   5857  CB  ASP B 342      24.990   9.038 -39.558  1.00 40.59           C  
-ATOM   5858  CG  ASP B 342      25.872   8.845 -38.341  1.00 49.08           C  
-ATOM   5859  OD1 ASP B 342      25.790   9.671 -37.406  1.00 52.65           O  
-ATOM   5860  OD2 ASP B 342      26.649   7.866 -38.320  1.00 44.79           O  
-ATOM   5861  N   ASP B 343      23.244  10.485 -41.425  1.00 58.50           N  
-ATOM   5862  CA  ASP B 343      22.555  10.635 -42.703  1.00 55.13           C  
-ATOM   5863  C   ASP B 343      23.461  11.217 -43.787  1.00 50.73           C  
-ATOM   5864  O   ASP B 343      24.680  11.296 -43.625  1.00 56.77           O  
-ATOM   5865  CB  ASP B 343      21.315  11.515 -42.544  1.00 40.73           C  
-ATOM   5866  CG  ASP B 343      21.648  12.904 -42.047  1.00 45.06           C  
-ATOM   5867  OD1 ASP B 343      22.491  13.022 -41.134  1.00 46.66           O  
-ATOM   5868  OD2 ASP B 343      21.071  13.878 -42.575  1.00 49.63           O  
-ATOM   5869  N   ARG B 344      22.845  11.617 -44.894  1.00 41.26           N  
-ATOM   5870  CA  ARG B 344      23.552  12.188 -46.034  1.00 51.32           C  
-ATOM   5871  C   ARG B 344      24.182  13.538 -45.694  1.00 48.63           C  
-ATOM   5872  O   ARG B 344      25.278  13.863 -46.157  1.00 53.49           O  
-ATOM   5873  CB  ARG B 344      22.586  12.328 -47.220  1.00 59.11           C  
-ATOM   5874  CG  ARG B 344      22.728  13.612 -48.027  1.00 58.50           C  
-ATOM   5875  CD  ARG B 344      23.559  13.408 -49.286  1.00 67.38           C  
-ATOM   5876  NE  ARG B 344      24.887  12.866 -49.007  1.00 83.89           N  
-ATOM   5877  CZ  ARG B 344      25.387  11.779 -49.588  1.00 84.56           C  
-ATOM   5878  NH1 ARG B 344      24.670  11.115 -50.486  1.00 83.71           N  
-ATOM   5879  NH2 ARG B 344      26.606  11.360 -49.273  1.00 67.95           N  
-ATOM   5880  N   THR B 345      23.485  14.314 -44.871  1.00 42.93           N  
-ATOM   5881  CA  THR B 345      23.894  15.680 -44.574  1.00 43.59           C  
-ATOM   5882  C   THR B 345      25.056  15.736 -43.585  1.00 49.70           C  
-ATOM   5883  O   THR B 345      25.817  16.705 -43.562  1.00 49.82           O  
-ATOM   5884  CB  THR B 345      22.720  16.497 -44.003  1.00 41.63           C  
-ATOM   5885  OG1 THR B 345      22.447  16.073 -42.662  1.00 34.93           O  
-ATOM   5886  CG2 THR B 345      21.471  16.303 -44.854  1.00 45.28           C  
-ATOM   5887  N   GLY B 346      25.185  14.697 -42.766  1.00 54.03           N  
-ATOM   5888  CA  GLY B 346      26.221  14.649 -41.748  1.00 49.86           C  
-ATOM   5889  C   GLY B 346      25.828  15.407 -40.494  1.00 45.15           C  
-ATOM   5890  O   GLY B 346      26.611  15.516 -39.550  1.00 44.65           O  
-ATOM   5891  N   VAL B 347      24.609  15.935 -40.487  1.00 39.90           N  
-ATOM   5892  CA  VAL B 347      24.106  16.694 -39.350  1.00 36.01           C  
-ATOM   5893  C   VAL B 347      23.694  15.750 -38.224  1.00 42.11           C  
-ATOM   5894  O   VAL B 347      23.918  16.035 -37.046  1.00 43.99           O  
-ATOM   5895  CB  VAL B 347      22.913  17.585 -39.755  1.00 37.24           C  
-ATOM   5896  CG1 VAL B 347      22.344  18.306 -38.545  1.00 45.66           C  
-ATOM   5897  CG2 VAL B 347      23.339  18.585 -40.819  1.00 38.30           C  
-ATOM   5898  N   GLY B 348      23.109  14.615 -38.595  1.00 33.82           N  
-ATOM   5899  CA  GLY B 348      22.658  13.636 -37.624  1.00 36.40           C  
-ATOM   5900  C   GLY B 348      21.211  13.866 -37.234  1.00 40.45           C  
-ATOM   5901  O   GLY B 348      20.796  15.007 -37.020  1.00 40.46           O  
-ATOM   5902  N   VAL B 349      20.438  12.786 -37.142  1.00 37.48           N  
-ATOM   5903  CA  VAL B 349      19.013  12.906 -36.846  1.00 28.63           C  
-ATOM   5904  C   VAL B 349      18.562  11.982 -35.724  1.00 32.17           C  
-ATOM   5905  O   VAL B 349      19.300  11.102 -35.293  1.00 34.43           O  
-ATOM   5906  CB  VAL B 349      18.146  12.595 -38.085  1.00 25.49           C  
-ATOM   5907  CG1 VAL B 349      18.604  13.404 -39.278  1.00 36.47           C  
-ATOM   5908  CG2 VAL B 349      18.192  11.111 -38.405  1.00 29.10           C  
-ATOM   5909  N   ILE B 350      17.341  12.206 -35.251  1.00 29.67           N  
-ATOM   5910  CA  ILE B 350      16.646  11.256 -34.392  1.00 28.88           C  
-ATOM   5911  C   ILE B 350      15.422  10.778 -35.164  1.00 32.25           C  
-ATOM   5912  O   ILE B 350      14.560  11.580 -35.515  1.00 33.38           O  
-ATOM   5913  CB  ILE B 350      16.222  11.881 -33.052  1.00 25.03           C  
-ATOM   5914  CG1 ILE B 350      17.433  12.487 -32.342  1.00 27.59           C  
-ATOM   5915  CG2 ILE B 350      15.537  10.844 -32.178  1.00 25.43           C  
-ATOM   5916  CD1 ILE B 350      17.097  13.175 -31.039  1.00 28.68           C  
-ATOM   5917  N   SER B 351      15.346   9.484 -35.451  1.00 28.06           N  
-ATOM   5918  CA  SER B 351      14.367   9.016 -36.424  1.00 23.81           C  
-ATOM   5919  C   SER B 351      13.490   7.864 -35.952  1.00 29.28           C  
-ATOM   5920  O   SER B 351      13.856   7.102 -35.053  1.00 32.41           O  
-ATOM   5921  CB  SER B 351      15.080   8.596 -37.707  1.00 27.95           C  
-ATOM   5922  OG  SER B 351      15.815   7.404 -37.501  1.00 34.33           O  
-ATOM   5923  N   LYS B 352      12.319   7.770 -36.577  1.00 29.11           N  
-ATOM   5924  CA  LYS B 352      11.428   6.624 -36.457  1.00 26.99           C  
-ATOM   5925  C   LYS B 352      11.025   6.203 -37.864  1.00 31.25           C  
-ATOM   5926  O   LYS B 352      11.280   6.930 -38.826  1.00 31.84           O  
-ATOM   5927  CB  LYS B 352      10.190   6.957 -35.621  1.00 21.53           C  
-ATOM   5928  CG  LYS B 352      10.495   7.430 -34.215  1.00 30.72           C  
-ATOM   5929  CD  LYS B 352       9.257   7.372 -33.329  1.00 36.52           C  
-ATOM   5930  CE  LYS B 352       8.805   5.937 -33.110  1.00 46.64           C  
-ATOM   5931  NZ  LYS B 352       7.749   5.834 -32.061  1.00 45.91           N  
-ATOM   5932  N   PHE B 353      10.394   5.040 -37.988  1.00 24.64           N  
-ATOM   5933  CA  PHE B 353       9.958   4.558 -39.293  1.00 16.47           C  
-ATOM   5934  C   PHE B 353       8.477   4.193 -39.274  1.00 19.95           C  
-ATOM   5935  O   PHE B 353       8.014   3.478 -38.383  1.00 24.33           O  
-ATOM   5936  CB  PHE B 353      10.796   3.354 -39.727  1.00 12.51           C  
-ATOM   5937  CG  PHE B 353      10.712   3.054 -41.197  1.00 16.77           C  
-ATOM   5938  CD1 PHE B 353      11.002   4.033 -42.132  1.00 20.83           C  
-ATOM   5939  CD2 PHE B 353      10.359   1.791 -41.645  1.00 16.99           C  
-ATOM   5940  CE1 PHE B 353      10.932   3.765 -43.488  1.00 20.72           C  
-ATOM   5941  CE2 PHE B 353      10.297   1.514 -43.002  1.00 19.50           C  
-ATOM   5942  CZ  PHE B 353      10.580   2.503 -43.924  1.00 19.56           C  
-ATOM   5943  N   GLY B 354       7.738   4.690 -40.261  1.00 16.38           N  
-ATOM   5944  CA  GLY B 354       6.315   4.417 -40.355  1.00 18.34           C  
-ATOM   5945  C   GLY B 354       5.490   5.247 -39.392  1.00 19.70           C  
-ATOM   5946  O   GLY B 354       5.174   4.808 -38.285  1.00 21.93           O  
-ATOM   5947  N   CYS B 355       5.143   6.456 -39.815  1.00 16.18           N  
-ATOM   5948  CA  CYS B 355       4.344   7.353 -38.994  1.00 15.08           C  
-ATOM   5949  C   CYS B 355       3.157   7.869 -39.792  1.00 20.72           C  
-ATOM   5950  O   CYS B 355       3.210   7.945 -41.018  1.00 18.05           O  
-ATOM   5951  CB  CYS B 355       5.198   8.510 -38.474  1.00 15.54           C  
-ATOM   5952  SG  CYS B 355       6.518   7.991 -37.344  1.00 17.76           S  
-ATOM   5953  N   THR B 356       2.088   8.222 -39.089  1.00 25.78           N  
-ATOM   5954  CA  THR B 356       0.821   8.531 -39.737  1.00 15.91           C  
-ATOM   5955  C   THR B 356       0.129   9.739 -39.123  1.00 19.61           C  
-ATOM   5956  O   THR B 356       0.030   9.862 -37.900  1.00 17.28           O  
-ATOM   5957  CB  THR B 356      -0.127   7.312 -39.676  1.00 18.82           C  
-ATOM   5958  OG1 THR B 356       0.179   6.425 -40.758  1.00 38.61           O  
-ATOM   5959  CG2 THR B 356      -1.593   7.731 -39.775  1.00 20.32           C  
-ATOM   5960  N   MET B 357      -0.339  10.639 -39.982  1.00 20.65           N  
-ATOM   5961  CA  MET B 357      -1.229  11.707 -39.546  1.00 18.44           C  
-ATOM   5962  C   MET B 357      -2.410  11.813 -40.499  1.00 18.42           C  
-ATOM   5963  O   MET B 357      -2.392  11.228 -41.575  1.00 16.24           O  
-ATOM   5964  CB  MET B 357      -0.493  13.042 -39.474  1.00 17.40           C  
-ATOM   5965  CG  MET B 357       0.496  13.156 -38.333  1.00 18.68           C  
-ATOM   5966  SD  MET B 357       1.298  14.770 -38.305  1.00 30.16           S  
-ATOM   5967  CE  MET B 357       1.975  14.846 -39.962  1.00 17.91           C  
-ATOM   5968  N   ARG B 358      -3.443  12.544 -40.097  1.00 15.10           N  
-ATOM   5969  CA  ARG B 358      -4.533  12.863 -41.010  1.00 17.17           C  
-ATOM   5970  C   ARG B 358      -5.293  14.096 -40.533  1.00 23.49           C  
-ATOM   5971  O   ARG B 358      -5.608  14.234 -39.348  1.00 18.39           O  
-ATOM   5972  CB  ARG B 358      -5.483  11.672 -41.184  1.00 15.21           C  
-ATOM   5973  CG  ARG B 358      -6.054  11.096 -39.907  1.00 19.56           C  
-ATOM   5974  CD  ARG B 358      -7.207  10.157 -40.228  1.00 20.15           C  
-ATOM   5975  NE  ARG B 358      -6.777   8.989 -40.993  1.00 25.25           N  
-ATOM   5976  CZ  ARG B 358      -7.557   8.318 -41.837  1.00 25.48           C  
-ATOM   5977  NH1 ARG B 358      -8.809   8.706 -42.040  1.00 22.27           N  
-ATOM   5978  NH2 ARG B 358      -7.082   7.262 -42.484  1.00 20.36           N  
-ATOM   5979  N   TYR B 359      -5.575  14.996 -41.470  1.00 19.94           N  
-ATOM   5980  CA  TYR B 359      -6.177  16.280 -41.143  1.00 16.83           C  
-ATOM   5981  C   TYR B 359      -7.478  16.495 -41.903  1.00 18.18           C  
-ATOM   5982  O   TYR B 359      -7.557  16.251 -43.107  1.00 16.97           O  
-ATOM   5983  CB  TYR B 359      -5.190  17.414 -41.437  1.00 20.00           C  
-ATOM   5984  CG  TYR B 359      -3.934  17.348 -40.595  1.00 17.24           C  
-ATOM   5985  CD1 TYR B 359      -3.827  18.071 -39.415  1.00 19.05           C  
-ATOM   5986  CD2 TYR B 359      -2.862  16.551 -40.971  1.00 13.59           C  
-ATOM   5987  CE1 TYR B 359      -2.684  18.007 -38.639  1.00 16.60           C  
-ATOM   5988  CE2 TYR B 359      -1.718  16.480 -40.202  1.00 12.30           C  
-ATOM   5989  CZ  TYR B 359      -1.633  17.210 -39.039  1.00 14.05           C  
-ATOM   5990  OH  TYR B 359      -0.495  17.142 -38.271  1.00 19.28           O  
-ATOM   5991  N   SER B 360      -8.498  16.952 -41.185  1.00 19.93           N  
-ATOM   5992  CA  SER B 360      -9.803  17.196 -41.780  1.00 19.78           C  
-ATOM   5993  C   SER B 360      -9.793  18.465 -42.631  1.00 26.18           C  
-ATOM   5994  O   SER B 360      -9.094  19.428 -42.311  1.00 33.03           O  
-ATOM   5995  CB  SER B 360     -10.870  17.292 -40.690  1.00 19.45           C  
-ATOM   5996  OG  SER B 360     -12.162  17.400 -41.259  1.00 49.99           O  
-ATOM   5997  N   LEU B 361     -10.574  18.464 -43.709  1.00 24.05           N  
-ATOM   5998  CA  LEU B 361     -10.564  19.575 -44.658  1.00 23.98           C  
-ATOM   5999  C   LEU B 361     -11.925  20.242 -44.862  1.00 28.23           C  
-ATOM   6000  O   LEU B 361     -12.026  21.229 -45.592  1.00 22.50           O  
-ATOM   6001  CB  LEU B 361     -10.038  19.097 -46.013  1.00 13.97           C  
-ATOM   6002  CG  LEU B 361      -8.631  18.501 -46.037  1.00 18.08           C  
-ATOM   6003  CD1 LEU B 361      -8.212  18.185 -47.463  1.00 16.03           C  
-ATOM   6004  CD2 LEU B 361      -7.644  19.448 -45.383  1.00 19.28           C  
-ATOM   6005  N   ASP B 362     -12.967  19.714 -44.227  1.00 31.64           N  
-ATOM   6006  CA  ASP B 362     -14.321  20.209 -44.468  1.00 21.88           C  
-ATOM   6007  C   ASP B 362     -14.642  21.476 -43.679  1.00 21.41           C  
-ATOM   6008  O   ASP B 362     -15.427  22.308 -44.128  1.00 20.64           O  
-ATOM   6009  CB  ASP B 362     -15.352  19.128 -44.138  1.00 18.16           C  
-ATOM   6010  CG  ASP B 362     -15.324  18.723 -42.681  1.00 24.18           C  
-ATOM   6011  OD1 ASP B 362     -14.219  18.512 -42.141  1.00 26.68           O  
-ATOM   6012  OD2 ASP B 362     -16.410  18.623 -42.072  1.00 26.30           O  
-ATOM   6013  N   GLN B 363     -14.041  21.620 -42.502  1.00 24.70           N  
-ATOM   6014  CA  GLN B 363     -14.311  22.778 -41.658  1.00 18.60           C  
-ATOM   6015  C   GLN B 363     -13.238  23.845 -41.841  1.00 14.62           C  
-ATOM   6016  O   GLN B 363     -13.547  25.009 -42.086  1.00  8.64           O  
-ATOM   6017  CB  GLN B 363     -14.401  22.366 -40.187  1.00 27.87           C  
-ATOM   6018  CG  GLN B 363     -15.502  21.353 -39.878  1.00 35.66           C  
-ATOM   6019  CD  GLN B 363     -16.866  21.994 -39.685  1.00 34.39           C  
-ATOM   6020  OE1 GLN B 363     -17.027  22.914 -38.881  1.00 24.89           O  
-ATOM   6021  NE2 GLN B 363     -17.858  21.505 -40.420  1.00 39.16           N  
-ATOM   6022  N   ALA B 364     -11.974  23.445 -41.735  1.00 19.34           N  
-ATOM   6023  CA  ALA B 364     -10.873  24.397 -41.844  1.00 15.86           C  
-ATOM   6024  C   ALA B 364      -9.685  23.821 -42.603  1.00 15.30           C  
-ATOM   6025  O   ALA B 364      -9.761  22.726 -43.161  1.00 19.48           O  
-ATOM   6026  CB  ALA B 364     -10.439  24.855 -40.465  1.00 15.33           C  
-ATOM   6027  N   PHE B 365      -8.588  24.573 -42.614  1.00 16.58           N  
-ATOM   6028  CA  PHE B 365      -7.382  24.182 -43.337  1.00 18.21           C  
-ATOM   6029  C   PHE B 365      -6.218  24.000 -42.370  1.00 15.94           C  
-ATOM   6030  O   PHE B 365      -5.959  24.867 -41.537  1.00 16.27           O  
-ATOM   6031  CB  PHE B 365      -7.035  25.225 -44.406  1.00 14.18           C  
-ATOM   6032  CG  PHE B 365      -5.925  24.809 -45.328  1.00 11.31           C  
-ATOM   6033  CD1 PHE B 365      -4.605  25.099 -45.021  1.00 18.32           C  
-ATOM   6034  CD2 PHE B 365      -6.201  24.140 -46.508  1.00 10.90           C  
-ATOM   6035  CE1 PHE B 365      -3.580  24.720 -45.869  1.00 14.42           C  
-ATOM   6036  CE2 PHE B 365      -5.179  23.759 -47.360  1.00 15.19           C  
-ATOM   6037  CZ  PHE B 365      -3.867  24.050 -47.039  1.00 13.58           C  
-ATOM   6038  N   PRO B 366      -5.506  22.869 -42.483  1.00 16.67           N  
-ATOM   6039  CA  PRO B 366      -4.409  22.551 -41.567  1.00 11.66           C  
-ATOM   6040  C   PRO B 366      -3.153  23.380 -41.819  1.00 16.78           C  
-ATOM   6041  O   PRO B 366      -2.096  22.818 -42.105  1.00 31.71           O  
-ATOM   6042  CB  PRO B 366      -4.146  21.071 -41.848  1.00 12.47           C  
-ATOM   6043  CG  PRO B 366      -4.529  20.898 -43.272  1.00 13.60           C  
-ATOM   6044  CD  PRO B 366      -5.707  21.810 -43.488  1.00 14.75           C  
-ATOM   6045  N   LEU B 367      -3.269  24.700 -41.720  1.00 15.63           N  
-ATOM   6046  CA  LEU B 367      -2.092  25.557 -41.735  1.00 16.75           C  
-ATOM   6047  C   LEU B 367      -1.623  25.741 -40.296  1.00 18.07           C  
-ATOM   6048  O   LEU B 367      -2.260  26.444 -39.512  1.00 20.34           O  
-ATOM   6049  CB  LEU B 367      -2.396  26.902 -42.395  1.00 12.78           C  
-ATOM   6050  CG  LEU B 367      -1.184  27.742 -42.806  1.00 12.77           C  
-ATOM   6051  CD1 LEU B 367      -0.302  26.981 -43.784  1.00 13.67           C  
-ATOM   6052  CD2 LEU B 367      -1.631  29.061 -43.408  1.00 15.44           C  
-ATOM   6053  N   LEU B 368      -0.509  25.096 -39.962  1.00 13.42           N  
-ATOM   6054  CA  LEU B 368      -0.035  24.975 -38.581  1.00 20.29           C  
-ATOM   6055  C   LEU B 368       0.070  26.316 -37.851  1.00 24.19           C  
-ATOM   6056  O   LEU B 368       0.377  27.341 -38.459  1.00 26.45           O  
-ATOM   6057  CB  LEU B 368       1.322  24.263 -38.558  1.00 29.11           C  
-ATOM   6058  CG  LEU B 368       1.343  22.762 -38.889  1.00 34.63           C  
-ATOM   6059  CD1 LEU B 368       0.385  21.988 -37.993  1.00 18.79           C  
-ATOM   6060  CD2 LEU B 368       1.043  22.478 -40.363  1.00 43.93           C  
-ATOM   6061  N   THR B 369      -0.186  26.300 -36.545  1.00 23.66           N  
-ATOM   6062  CA  THR B 369      -0.285  27.537 -35.774  1.00 23.74           C  
-ATOM   6063  C   THR B 369       0.789  27.705 -34.700  1.00 24.06           C  
-ATOM   6064  O   THR B 369       1.010  28.815 -34.217  1.00 31.65           O  
-ATOM   6065  CB  THR B 369      -1.662  27.656 -35.088  1.00 20.61           C  
-ATOM   6066  OG1 THR B 369      -1.911  26.485 -34.301  1.00 20.78           O  
-ATOM   6067  CG2 THR B 369      -2.759  27.805 -36.123  1.00 24.19           C  
-ATOM   6068  N   THR B 370       1.455  26.617 -34.320  1.00 19.94           N  
-ATOM   6069  CA  THR B 370       2.505  26.699 -33.305  1.00 23.38           C  
-ATOM   6070  C   THR B 370       3.743  27.404 -33.855  1.00 28.26           C  
-ATOM   6071  O   THR B 370       4.670  27.730 -33.112  1.00 25.80           O  
-ATOM   6072  CB  THR B 370       2.904  25.311 -32.776  1.00 23.50           C  
-ATOM   6073  OG1 THR B 370       3.235  24.452 -33.875  1.00 30.02           O  
-ATOM   6074  CG2 THR B 370       1.760  24.698 -31.979  1.00 18.58           C  
-ATOM   6075  N   LYS B 371       3.749  27.626 -35.164  1.00 27.95           N  
-ATOM   6076  CA  LYS B 371       4.756  28.451 -35.816  1.00 26.22           C  
-ATOM   6077  C   LYS B 371       4.200  28.902 -37.159  1.00 32.58           C  
-ATOM   6078  O   LYS B 371       3.349  28.229 -37.742  1.00 40.44           O  
-ATOM   6079  CB  LYS B 371       6.074  27.690 -35.992  1.00 28.75           C  
-ATOM   6080  CG  LYS B 371       6.158  26.849 -37.256  1.00 34.37           C  
-ATOM   6081  CD  LYS B 371       7.376  25.937 -37.242  1.00 40.80           C  
-ATOM   6082  CE  LYS B 371       8.194  26.076 -38.517  1.00 42.07           C  
-ATOM   6083  NZ  LYS B 371       9.194  24.980 -38.644  1.00 45.04           N  
-ATOM   6084  N   ARG B 372       4.665  30.045 -37.647  1.00 37.51           N  
-ATOM   6085  CA  ARG B 372       4.170  30.564 -38.914  1.00 29.66           C  
-ATOM   6086  C   ARG B 372       4.708  29.738 -40.080  1.00 29.48           C  
-ATOM   6087  O   ARG B 372       5.917  29.560 -40.226  1.00 35.08           O  
-ATOM   6088  CB  ARG B 372       4.545  32.038 -39.080  1.00 29.91           C  
-ATOM   6089  CG  ARG B 372       4.056  32.647 -40.382  1.00 29.69           C  
-ATOM   6090  CD  ARG B 372       4.169  34.161 -40.376  1.00 33.03           C  
-ATOM   6091  NE  ARG B 372       3.205  34.786 -39.474  1.00 32.22           N  
-ATOM   6092  CZ  ARG B 372       1.947  35.066 -39.804  1.00 32.48           C  
-ATOM   6093  NH1 ARG B 372       1.493  34.769 -41.015  1.00 30.40           N  
-ATOM   6094  NH2 ARG B 372       1.139  35.638 -38.921  1.00 29.70           N  
-ATOM   6095  N   VAL B 373       3.796  29.227 -40.900  1.00 22.92           N  
-ATOM   6096  CA  VAL B 373       4.156  28.427 -42.065  1.00 22.82           C  
-ATOM   6097  C   VAL B 373       4.239  29.299 -43.317  1.00 21.31           C  
-ATOM   6098  O   VAL B 373       3.410  30.188 -43.517  1.00 23.08           O  
-ATOM   6099  CB  VAL B 373       3.141  27.280 -42.279  1.00 25.45           C  
-ATOM   6100  CG1 VAL B 373       3.392  26.556 -43.599  1.00 19.37           C  
-ATOM   6101  CG2 VAL B 373       3.196  26.308 -41.109  1.00 25.54           C  
-ATOM   6102  N   PHE B 374       5.249  29.052 -44.148  1.00 22.89           N  
-ATOM   6103  CA  PHE B 374       5.456  29.841 -45.363  1.00 26.93           C  
-ATOM   6104  C   PHE B 374       4.399  29.546 -46.432  1.00 22.16           C  
-ATOM   6105  O   PHE B 374       4.635  28.799 -47.391  1.00 26.72           O  
-ATOM   6106  CB  PHE B 374       6.855  29.595 -45.927  1.00 28.43           C  
-ATOM   6107  CG  PHE B 374       7.289  30.621 -46.928  1.00 23.30           C  
-ATOM   6108  CD1 PHE B 374       6.742  31.893 -46.918  1.00 19.59           C  
-ATOM   6109  CD2 PHE B 374       8.229  30.309 -47.893  1.00 29.15           C  
-ATOM   6110  CE1 PHE B 374       7.133  32.838 -47.845  1.00 25.31           C  
-ATOM   6111  CE2 PHE B 374       8.624  31.247 -48.825  1.00 28.16           C  
-ATOM   6112  CZ  PHE B 374       8.076  32.515 -48.802  1.00 25.32           C  
-ATOM   6113  N   TRP B 375       3.236  30.164 -46.262  1.00 17.43           N  
-ATOM   6114  CA  TRP B 375       2.099  29.931 -47.140  1.00 16.23           C  
-ATOM   6115  C   TRP B 375       2.384  30.265 -48.597  1.00 19.31           C  
-ATOM   6116  O   TRP B 375       2.099  29.463 -49.484  1.00 25.81           O  
-ATOM   6117  CB  TRP B 375       0.893  30.739 -46.674  1.00 15.30           C  
-ATOM   6118  CG  TRP B 375      -0.186  30.760 -47.696  1.00 12.24           C  
-ATOM   6119  CD1 TRP B 375      -0.522  31.796 -48.516  1.00 10.45           C  
-ATOM   6120  CD2 TRP B 375      -1.057  29.681 -48.036  1.00 15.23           C  
-ATOM   6121  NE1 TRP B 375      -1.561  31.434 -49.337  1.00  9.29           N  
-ATOM   6122  CE2 TRP B 375      -1.907  30.136 -49.063  1.00 14.66           C  
-ATOM   6123  CE3 TRP B 375      -1.206  28.372 -47.567  1.00 14.86           C  
-ATOM   6124  CZ2 TRP B 375      -2.894  29.333 -49.626  1.00 19.81           C  
-ATOM   6125  CZ3 TRP B 375      -2.186  27.575 -48.128  1.00 17.54           C  
-ATOM   6126  CH2 TRP B 375      -3.018  28.058 -49.146  1.00 20.79           C  
-ATOM   6127  N   LYS B 376       2.921  31.457 -48.839  1.00 14.97           N  
-ATOM   6128  CA  LYS B 376       3.249  31.888 -50.192  1.00 15.44           C  
-ATOM   6129  C   LYS B 376       4.159  30.864 -50.857  1.00 16.60           C  
-ATOM   6130  O   LYS B 376       3.966  30.501 -52.014  1.00 18.60           O  
-ATOM   6131  CB  LYS B 376       3.918  33.264 -50.176  1.00 23.35           C  
-ATOM   6132  CG  LYS B 376       3.955  33.945 -51.535  1.00 33.45           C  
-ATOM   6133  CD  LYS B 376       5.329  34.522 -51.838  1.00 30.71           C  
-ATOM   6134  CE  LYS B 376       5.757  35.538 -50.791  1.00 39.65           C  
-ATOM   6135  NZ  LYS B 376       7.109  36.096 -51.088  1.00 36.22           N  
-ATOM   6136  N   GLY B 377       5.141  30.389 -50.101  1.00 18.45           N  
-ATOM   6137  CA  GLY B 377       6.033  29.346 -50.568  1.00 19.93           C  
-ATOM   6138  C   GLY B 377       5.270  28.094 -50.949  1.00 19.31           C  
-ATOM   6139  O   GLY B 377       5.502  27.523 -52.014  1.00 20.83           O  
-ATOM   6140  N   VAL B 378       4.354  27.670 -50.079  1.00 18.89           N  
-ATOM   6141  CA  VAL B 378       3.505  26.510 -50.363  1.00 23.05           C  
-ATOM   6142  C   VAL B 378       2.779  26.656 -51.701  1.00 22.34           C  
-ATOM   6143  O   VAL B 378       2.942  25.828 -52.610  1.00 30.32           O  
-ATOM   6144  CB  VAL B 378       2.456  26.291 -49.247  1.00 18.42           C  
-ATOM   6145  CG1 VAL B 378       1.429  25.249 -49.667  1.00 17.59           C  
-ATOM   6146  CG2 VAL B 378       3.130  25.894 -47.951  1.00 17.27           C  
-ATOM   6147  N   LEU B 379       1.993  27.722 -51.804  1.00 16.88           N  
-ATOM   6148  CA  LEU B 379       1.184  28.015 -52.978  1.00 20.49           C  
-ATOM   6149  C   LEU B 379       1.996  28.081 -54.269  1.00 21.94           C  
-ATOM   6150  O   LEU B 379       1.689  27.396 -55.245  1.00 21.48           O  
-ATOM   6151  CB  LEU B 379       0.433  29.335 -52.751  1.00 21.63           C  
-ATOM   6152  CG  LEU B 379      -0.468  29.828 -53.884  1.00 23.79           C  
-ATOM   6153  CD1 LEU B 379      -1.399  28.725 -54.363  1.00 21.64           C  
-ATOM   6154  CD2 LEU B 379      -1.258  31.038 -53.417  1.00 17.49           C  
-ATOM   6155  N   GLU B 380       3.035  28.907 -54.263  1.00 21.84           N  
-ATOM   6156  CA  GLU B 380       3.878  29.082 -55.439  1.00 22.54           C  
-ATOM   6157  C   GLU B 380       4.576  27.792 -55.841  1.00 23.65           C  
-ATOM   6158  O   GLU B 380       4.650  27.475 -57.029  1.00 29.57           O  
-ATOM   6159  CB  GLU B 380       4.918  30.181 -55.200  1.00 25.38           C  
-ATOM   6160  CG  GLU B 380       4.330  31.578 -55.048  1.00 33.69           C  
-ATOM   6161  CD  GLU B 380       3.834  32.173 -56.362  1.00 38.99           C  
-ATOM   6162  OE1 GLU B 380       3.924  31.497 -57.411  1.00 35.30           O  
-ATOM   6163  OE2 GLU B 380       3.359  33.331 -56.343  1.00 30.86           O  
-ATOM   6164  N   GLU B 381       5.088  27.048 -54.863  1.00 18.52           N  
-ATOM   6165  CA  GLU B 381       5.738  25.779 -55.172  1.00 18.27           C  
-ATOM   6166  C   GLU B 381       4.745  24.791 -55.778  1.00 20.74           C  
-ATOM   6167  O   GLU B 381       5.097  24.010 -56.666  1.00 19.09           O  
-ATOM   6168  CB  GLU B 381       6.385  25.166 -53.928  1.00 19.59           C  
-ATOM   6169  CG  GLU B 381       7.322  24.006 -54.242  1.00 20.12           C  
-ATOM   6170  CD  GLU B 381       7.467  23.039 -53.084  1.00 35.59           C  
-ATOM   6171  OE1 GLU B 381       6.467  22.814 -52.369  1.00 42.85           O  
-ATOM   6172  OE2 GLU B 381       8.579  22.500 -52.891  1.00 35.69           O  
-ATOM   6173  N   LEU B 382       3.503  24.820 -55.300  1.00 23.41           N  
-ATOM   6174  CA  LEU B 382       2.493  23.908 -55.830  1.00 20.22           C  
-ATOM   6175  C   LEU B 382       2.092  24.276 -57.257  1.00 19.74           C  
-ATOM   6176  O   LEU B 382       1.951  23.403 -58.110  1.00 23.20           O  
-ATOM   6177  CB  LEU B 382       1.255  23.872 -54.927  1.00 16.68           C  
-ATOM   6178  CG  LEU B 382       0.132  22.923 -55.370  1.00 19.92           C  
-ATOM   6179  CD1 LEU B 382       0.682  21.558 -55.762  1.00 16.22           C  
-ATOM   6180  CD2 LEU B 382      -0.914  22.783 -54.268  1.00 21.82           C  
-ATOM   6181  N   LEU B 383       1.902  25.565 -57.514  1.00 18.19           N  
-ATOM   6182  CA  LEU B 383       1.574  26.018 -58.863  1.00 15.99           C  
-ATOM   6183  C   LEU B 383       2.708  25.666 -59.820  1.00 22.05           C  
-ATOM   6184  O   LEU B 383       2.478  25.241 -60.950  1.00 22.89           O  
-ATOM   6185  CB  LEU B 383       1.306  27.522 -58.877  1.00 16.46           C  
-ATOM   6186  CG  LEU B 383       0.018  27.956 -58.177  1.00 12.92           C  
-ATOM   6187  CD1 LEU B 383      -0.119  29.466 -58.188  1.00 21.98           C  
-ATOM   6188  CD2 LEU B 383      -1.183  27.306 -58.833  1.00 16.06           C  
-ATOM   6189  N   TRP B 384       3.931  25.860 -59.339  1.00 25.23           N  
-ATOM   6190  CA  TRP B 384       5.152  25.403 -59.994  1.00 23.46           C  
-ATOM   6191  C   TRP B 384       5.037  23.929 -60.406  1.00 23.19           C  
-ATOM   6192  O   TRP B 384       5.140  23.583 -61.595  1.00 21.31           O  
-ATOM   6193  CB  TRP B 384       6.328  25.632 -59.032  1.00 19.75           C  
-ATOM   6194  CG  TRP B 384       7.705  25.571 -59.608  1.00 17.48           C  
-ATOM   6195  CD1 TRP B 384       8.228  26.373 -60.580  1.00 20.26           C  
-ATOM   6196  CD2 TRP B 384       8.761  24.698 -59.198  1.00 20.17           C  
-ATOM   6197  NE1 TRP B 384       9.536  26.030 -60.824  1.00 18.73           N  
-ATOM   6198  CE2 TRP B 384       9.889  25.003 -59.985  1.00 21.65           C  
-ATOM   6199  CE3 TRP B 384       8.860  23.674 -58.250  1.00 17.34           C  
-ATOM   6200  CZ2 TRP B 384      11.098  24.324 -59.856  1.00 22.47           C  
-ATOM   6201  CZ3 TRP B 384      10.058  23.002 -58.122  1.00 21.68           C  
-ATOM   6202  CH2 TRP B 384      11.162  23.329 -58.919  1.00 22.54           C  
-ATOM   6203  N   PHE B 385       4.810  23.076 -59.408  1.00 22.08           N  
-ATOM   6204  CA  PHE B 385       4.616  21.645 -59.625  1.00 21.37           C  
-ATOM   6205  C   PHE B 385       3.612  21.366 -60.729  1.00 22.91           C  
-ATOM   6206  O   PHE B 385       3.894  20.606 -61.654  1.00 23.63           O  
-ATOM   6207  CB  PHE B 385       4.146  20.962 -58.336  1.00 17.08           C  
-ATOM   6208  CG  PHE B 385       5.219  20.799 -57.307  1.00 26.87           C  
-ATOM   6209  CD1 PHE B 385       6.555  20.898 -57.657  1.00 35.14           C  
-ATOM   6210  CD2 PHE B 385       4.892  20.541 -55.986  1.00 28.07           C  
-ATOM   6211  CE1 PHE B 385       7.551  20.746 -56.706  1.00 33.00           C  
-ATOM   6212  CE2 PHE B 385       5.883  20.386 -55.026  1.00 34.15           C  
-ATOM   6213  CZ  PHE B 385       7.214  20.489 -55.389  1.00 34.96           C  
-ATOM   6214  N   ILE B 386       2.444  21.989 -60.622  1.00 21.00           N  
-ATOM   6215  CA  ILE B 386       1.362  21.756 -61.571  1.00 17.56           C  
-ATOM   6216  C   ILE B 386       1.741  22.174 -62.989  1.00 20.51           C  
-ATOM   6217  O   ILE B 386       1.421  21.474 -63.951  1.00 26.69           O  
-ATOM   6218  CB  ILE B 386       0.079  22.489 -61.133  1.00 15.70           C  
-ATOM   6219  CG1 ILE B 386      -0.378  21.953 -59.776  1.00 19.65           C  
-ATOM   6220  CG2 ILE B 386      -1.017  22.307 -62.166  1.00 14.67           C  
-ATOM   6221  CD1 ILE B 386      -1.629  22.595 -59.260  1.00 21.94           C  
-ATOM   6222  N   ARG B 387       2.429  23.304 -63.124  1.00 29.79           N  
-ATOM   6223  CA  ARG B 387       2.922  23.713 -64.435  1.00 22.91           C  
-ATOM   6224  C   ARG B 387       3.941  22.696 -64.935  1.00 25.12           C  
-ATOM   6225  O   ARG B 387       4.129  22.532 -66.140  1.00 28.22           O  
-ATOM   6226  CB  ARG B 387       3.549  25.108 -64.387  1.00 27.12           C  
-ATOM   6227  CG  ARG B 387       2.591  26.216 -63.978  1.00 30.74           C  
-ATOM   6228  CD  ARG B 387       3.249  27.586 -64.063  1.00 26.42           C  
-ATOM   6229  NE  ARG B 387       2.604  28.549 -63.174  1.00 34.55           N  
-ATOM   6230  CZ  ARG B 387       3.162  29.031 -62.067  1.00 33.33           C  
-ATOM   6231  NH1 ARG B 387       4.381  28.649 -61.715  1.00 30.13           N  
-ATOM   6232  NH2 ARG B 387       2.505  29.904 -61.316  1.00 38.33           N  
-ATOM   6233  N   GLY B 388       4.585  22.001 -64.003  1.00 29.96           N  
-ATOM   6234  CA  GLY B 388       5.579  21.008 -64.370  1.00 24.60           C  
-ATOM   6235  C   GLY B 388       6.880  21.711 -64.677  1.00 24.89           C  
-ATOM   6236  O   GLY B 388       7.663  21.284 -65.522  1.00 20.77           O  
-ATOM   6237  N   ASP B 389       7.090  22.817 -63.977  1.00 21.34           N  
-ATOM   6238  CA  ASP B 389       8.287  23.618 -64.122  1.00 16.14           C  
-ATOM   6239  C   ASP B 389       9.424  22.978 -63.338  1.00 19.31           C  
-ATOM   6240  O   ASP B 389       9.225  22.520 -62.215  1.00 19.93           O  
-ATOM   6241  CB  ASP B 389       8.014  25.037 -63.631  1.00 21.56           C  
-ATOM   6242  CG  ASP B 389       9.029  26.038 -64.124  1.00 26.31           C  
-ATOM   6243  OD1 ASP B 389      10.068  25.627 -64.685  1.00 25.12           O  
-ATOM   6244  OD2 ASP B 389       8.782  27.249 -63.939  1.00 25.52           O  
-ATOM   6245  N   THR B 390      10.610  22.932 -63.935  1.00 33.12           N  
-ATOM   6246  CA  THR B 390      11.783  22.377 -63.267  1.00 25.84           C  
-ATOM   6247  C   THR B 390      12.847  23.455 -63.086  1.00 24.68           C  
-ATOM   6248  O   THR B 390      14.018  23.162 -62.847  1.00 29.06           O  
-ATOM   6249  CB  THR B 390      12.375  21.189 -64.052  1.00 23.37           C  
-ATOM   6250  OG1 THR B 390      12.723  21.611 -65.378  1.00 24.79           O  
-ATOM   6251  CG2 THR B 390      11.365  20.061 -64.140  1.00 21.78           C  
-ATOM   6252  N   ASN B 391      12.419  24.706 -63.204  1.00 23.03           N  
-ATOM   6253  CA  ASN B 391      13.302  25.852 -63.056  1.00 21.87           C  
-ATOM   6254  C   ASN B 391      13.086  26.505 -61.693  1.00 28.20           C  
-ATOM   6255  O   ASN B 391      12.054  27.131 -61.458  1.00 34.24           O  
-ATOM   6256  CB  ASN B 391      13.053  26.854 -64.189  1.00 23.87           C  
-ATOM   6257  CG  ASN B 391      14.145  27.900 -64.304  1.00 24.44           C  
-ATOM   6258  OD1 ASN B 391      14.673  28.378 -63.304  1.00 25.83           O  
-ATOM   6259  ND2 ASN B 391      14.493  28.255 -65.534  1.00 33.10           N  
-ATOM   6260  N   ALA B 392      14.057  26.356 -60.797  1.00 22.94           N  
-ATOM   6261  CA  ALA B 392      13.922  26.865 -59.435  1.00 24.83           C  
-ATOM   6262  C   ALA B 392      14.077  28.383 -59.362  1.00 28.45           C  
-ATOM   6263  O   ALA B 392      13.695  29.007 -58.373  1.00 35.92           O  
-ATOM   6264  CB  ALA B 392      14.932  26.191 -58.522  1.00 27.11           C  
-ATOM   6265  N   ASN B 393      14.639  28.974 -60.410  1.00 26.05           N  
-ATOM   6266  CA  ASN B 393      14.826  30.418 -60.453  1.00 23.65           C  
-ATOM   6267  C   ASN B 393      13.493  31.137 -60.574  1.00 30.79           C  
-ATOM   6268  O   ASN B 393      13.358  32.287 -60.161  1.00 39.95           O  
-ATOM   6269  CB  ASN B 393      15.742  30.807 -61.612  1.00 25.40           C  
-ATOM   6270  CG  ASN B 393      17.090  30.125 -61.538  1.00 25.13           C  
-ATOM   6271  OD1 ASN B 393      17.708  30.058 -60.477  1.00 26.80           O  
-ATOM   6272  ND2 ASN B 393      17.551  29.608 -62.668  1.00 39.80           N  
-ATOM   6273  N   HIS B 394      12.508  30.449 -61.142  1.00 28.14           N  
-ATOM   6274  CA  HIS B 394      11.154  30.986 -61.232  1.00 31.04           C  
-ATOM   6275  C   HIS B 394      10.519  31.071 -59.850  1.00 25.99           C  
-ATOM   6276  O   HIS B 394       9.647  31.901 -59.599  1.00 24.39           O  
-ATOM   6277  CB  HIS B 394      10.298  30.125 -62.157  1.00 33.43           C  
-ATOM   6278  CG  HIS B 394      10.733  30.166 -63.588  1.00 24.24           C  
-ATOM   6279  ND1 HIS B 394      10.191  29.347 -64.555  1.00 24.17           N  
-ATOM   6280  CD2 HIS B 394      11.653  30.934 -64.218  1.00 25.99           C  
-ATOM   6281  CE1 HIS B 394      10.760  29.606 -65.718  1.00 28.05           C  
-ATOM   6282  NE2 HIS B 394      11.650  30.566 -65.542  1.00 33.70           N  
-ATOM   6283  N   LEU B 395      10.966  30.193 -58.960  1.00 29.62           N  
-ATOM   6284  CA  LEU B 395      10.528  30.199 -57.573  1.00 27.66           C  
-ATOM   6285  C   LEU B 395      11.302  31.247 -56.782  1.00 29.94           C  
-ATOM   6286  O   LEU B 395      10.743  31.948 -55.941  1.00 25.78           O  
-ATOM   6287  CB  LEU B 395      10.717  28.812 -56.951  1.00 20.96           C  
-ATOM   6288  CG  LEU B 395       9.485  28.097 -56.398  1.00 19.21           C  
-ATOM   6289  CD1 LEU B 395       8.299  28.238 -57.339  1.00 19.77           C  
-ATOM   6290  CD2 LEU B 395       9.808  26.631 -56.159  1.00 19.08           C  
-ATOM   6291  N   SER B 396      12.595  31.347 -57.070  1.00 35.33           N  
-ATOM   6292  CA  SER B 396      13.492  32.231 -56.341  1.00 32.51           C  
-ATOM   6293  C   SER B 396      13.210  33.699 -56.661  1.00 33.94           C  
-ATOM   6294  O   SER B 396      13.417  34.574 -55.822  1.00 33.96           O  
-ATOM   6295  CB  SER B 396      14.948  31.881 -56.662  1.00 32.90           C  
-ATOM   6296  OG  SER B 396      15.828  32.379 -55.670  1.00 45.57           O  
-ATOM   6297  N  AGLU B 397      12.744  33.949 -57.882  0.42 40.58           N  
-ATOM   6298  N  BGLU B 397      12.729  33.968 -57.871  0.58 38.86           N  
-ATOM   6299  CA AGLU B 397      12.403  35.294 -58.332  0.42 30.73           C  
-ATOM   6300  CA BGLU B 397      12.444  35.342 -58.276  0.58 31.03           C  
-ATOM   6301  C  AGLU B 397      11.236  35.847 -57.523  0.42 32.23           C  
-ATOM   6302  C  BGLU B 397      11.130  35.858 -57.691  0.58 32.31           C  
-ATOM   6303  O  AGLU B 397      11.164  37.046 -57.250  0.42 32.22           O  
-ATOM   6304  O  BGLU B 397      10.847  37.055 -57.751  0.58 33.04           O  
-ATOM   6305  CB AGLU B 397      12.067  35.287 -59.829  0.42 30.26           C  
-ATOM   6306  CB BGLU B 397      12.431  35.455 -59.801  0.58 30.02           C  
-ATOM   6307  CG AGLU B 397      11.430  36.569 -60.357  0.42 32.64           C  
-ATOM   6308  CG BGLU B 397      13.796  35.781 -60.386  0.58 29.51           C  
-ATOM   6309  CD AGLU B 397       9.915  36.486 -60.430  0.42 29.18           C  
-ATOM   6310  CD BGLU B 397      14.107  34.984 -61.635  0.58 29.28           C  
-ATOM   6311  OE1AGLU B 397       9.249  37.521 -60.216  0.42 24.32           O  
-ATOM   6312  OE1BGLU B 397      13.164  34.665 -62.389  0.58 23.26           O  
-ATOM   6313  OE2AGLU B 397       9.391  35.386 -60.707  0.42 26.85           O  
-ATOM   6314  OE2BGLU B 397      15.297  34.670 -61.855  0.58 22.34           O  
-ATOM   6315  N   LYS B 398      10.333  34.957 -57.125  1.00 33.53           N  
-ATOM   6316  CA  LYS B 398       9.127  35.355 -56.407  1.00 28.08           C  
-ATOM   6317  C   LYS B 398       9.376  35.409 -54.902  1.00 30.27           C  
-ATOM   6318  O   LYS B 398       8.444  35.576 -54.115  1.00 30.85           O  
-ATOM   6319  CB  LYS B 398       7.975  34.397 -56.707  1.00 25.22           C  
-ATOM   6320  CG  LYS B 398       7.693  34.199 -58.184  1.00 28.64           C  
-ATOM   6321  CD  LYS B 398       6.405  33.420 -58.396  1.00 18.51           C  
-ATOM   6322  CE  LYS B 398       6.291  32.929 -59.828  1.00 22.42           C  
-ATOM   6323  NZ  LYS B 398       6.492  34.029 -60.809  1.00 21.56           N  
-ATOM   6324  N   GLY B 399      10.635  35.262 -54.505  1.00 30.65           N  
-ATOM   6325  CA  GLY B 399      11.000  35.339 -53.103  1.00 36.23           C  
-ATOM   6326  C   GLY B 399      10.896  34.004 -52.394  1.00 41.54           C  
-ATOM   6327  O   GLY B 399      11.094  33.921 -51.181  1.00 48.21           O  
-ATOM   6328  N   VAL B 400      10.579  32.959 -53.152  1.00 35.98           N  
-ATOM   6329  CA  VAL B 400      10.484  31.611 -52.605  1.00 34.11           C  
-ATOM   6330  C   VAL B 400      11.757  30.836 -52.910  1.00 27.39           C  
-ATOM   6331  O   VAL B 400      11.875  30.214 -53.963  1.00 27.42           O  
-ATOM   6332  CB  VAL B 400       9.269  30.846 -53.173  1.00 30.57           C  
-ATOM   6333  CG1 VAL B 400       9.165  29.463 -52.546  1.00 27.68           C  
-ATOM   6334  CG2 VAL B 400       7.988  31.632 -52.941  1.00 26.77           C  
-ATOM   6335  N   LYS B 401      12.710  30.874 -51.984  1.00 28.54           N  
-ATOM   6336  CA  LYS B 401      14.015  30.264 -52.224  1.00 35.54           C  
-ATOM   6337  C   LYS B 401      14.241  28.983 -51.432  1.00 32.83           C  
-ATOM   6338  O   LYS B 401      15.316  28.771 -50.878  1.00 52.69           O  
-ATOM   6339  CB  LYS B 401      15.127  31.271 -51.918  1.00 44.50           C  
-ATOM   6340  CG  LYS B 401      14.721  32.420 -51.013  1.00 45.72           C  
-ATOM   6341  CD  LYS B 401      15.532  33.664 -51.356  1.00 53.19           C  
-ATOM   6342  CE  LYS B 401      15.929  34.455 -50.118  1.00 67.72           C  
-ATOM   6343  NZ  LYS B 401      14.774  35.130 -49.462  1.00 63.20           N  
-ATOM   6344  N   ILE B 402      13.231  28.122 -51.400  1.00 31.73           N  
-ATOM   6345  CA  ILE B 402      13.325  26.862 -50.669  1.00 29.28           C  
-ATOM   6346  C   ILE B 402      14.149  25.824 -51.418  1.00 39.02           C  
-ATOM   6347  O   ILE B 402      14.496  24.785 -50.862  1.00 50.65           O  
-ATOM   6348  CB  ILE B 402      11.938  26.260 -50.390  1.00 29.08           C  
-ATOM   6349  CG1 ILE B 402      11.214  25.961 -51.706  1.00 30.19           C  
-ATOM   6350  CG2 ILE B 402      11.119  27.195 -49.521  1.00 42.94           C  
-ATOM   6351  CD1 ILE B 402       9.813  25.422 -51.534  1.00 28.65           C  
-ATOM   6352  N   TRP B 403      14.461  26.104 -52.678  1.00 36.23           N  
-ATOM   6353  CA  TRP B 403      15.150  25.135 -53.523  1.00 35.90           C  
-ATOM   6354  C   TRP B 403      16.607  25.490 -53.781  1.00 39.82           C  
-ATOM   6355  O   TRP B 403      17.390  24.632 -54.181  1.00 48.00           O  
-ATOM   6356  CB  TRP B 403      14.422  24.995 -54.860  1.00 35.09           C  
-ATOM   6357  CG  TRP B 403      13.368  23.943 -54.872  1.00 38.00           C  
-ATOM   6358  CD1 TRP B 403      12.023  24.129 -54.757  1.00 36.97           C  
-ATOM   6359  CD2 TRP B 403      13.570  22.533 -55.013  1.00 46.86           C  
-ATOM   6360  NE1 TRP B 403      11.373  22.921 -54.819  1.00 43.63           N  
-ATOM   6361  CE2 TRP B 403      12.301  21.925 -54.976  1.00 52.49           C  
-ATOM   6362  CE3 TRP B 403      14.701  21.725 -55.167  1.00 58.77           C  
-ATOM   6363  CZ2 TRP B 403      12.129  20.548 -55.086  1.00 58.54           C  
-ATOM   6364  CZ3 TRP B 403      14.528  20.354 -55.277  1.00 65.41           C  
-ATOM   6365  CH2 TRP B 403      13.251  19.781 -55.236  1.00 63.63           C  
-ATOM   6366  N   ASP B 404      16.961  26.749 -53.545  1.00 45.70           N  
-ATOM   6367  CA  ASP B 404      18.262  27.286 -53.942  1.00 54.19           C  
-ATOM   6368  C   ASP B 404      19.460  26.449 -53.490  1.00 48.98           C  
-ATOM   6369  O   ASP B 404      20.322  26.103 -54.302  1.00 36.97           O  
-ATOM   6370  CB  ASP B 404      18.412  28.717 -53.423  1.00 49.79           C  
-ATOM   6371  CG  ASP B 404      17.590  29.715 -54.220  1.00 61.54           C  
-ATOM   6372  OD1 ASP B 404      16.998  29.323 -55.250  1.00 61.58           O  
-ATOM   6373  OD2 ASP B 404      17.551  30.897 -53.824  1.00 64.11           O  
-ATOM   6374  N   LYS B 405      19.502  26.111 -52.204  1.00 42.58           N  
-ATOM   6375  CA  LYS B 405      20.632  25.380 -51.637  1.00 37.93           C  
-ATOM   6376  C   LYS B 405      20.807  23.993 -52.258  1.00 41.40           C  
-ATOM   6377  O   LYS B 405      21.851  23.366 -52.088  1.00 40.60           O  
-ATOM   6378  CB  LYS B 405      20.475  25.255 -50.118  1.00 36.41           C  
-ATOM   6379  CG  LYS B 405      20.459  26.586 -49.389  1.00 48.48           C  
-ATOM   6380  CD  LYS B 405      20.430  26.393 -47.885  1.00 39.21           C  
-ATOM   6381  CE  LYS B 405      20.314  27.724 -47.172  1.00 29.88           C  
-ATOM   6382  NZ  LYS B 405      20.327  27.561 -45.695  1.00 39.70           N  
-ATOM   6383  N   ASN B 406      19.793  23.521 -52.981  1.00 37.14           N  
-ATOM   6384  CA  ASN B 406      19.853  22.210 -53.622  1.00 34.04           C  
-ATOM   6385  C   ASN B 406      19.995  22.308 -55.138  1.00 30.83           C  
-ATOM   6386  O   ASN B 406      19.970  21.297 -55.836  1.00 29.22           O  
-ATOM   6387  CB  ASN B 406      18.613  21.386 -53.265  1.00 38.79           C  
-ATOM   6388  CG  ASN B 406      18.589  20.974 -51.804  1.00 44.85           C  
-ATOM   6389  OD1 ASN B 406      17.675  21.329 -51.061  1.00 54.23           O  
-ATOM   6390  ND2 ASN B 406      19.599  20.219 -51.384  1.00 40.10           N  
-ATOM   6391  N   VAL B 407      20.137  23.528 -55.647  1.00 33.41           N  
-ATOM   6392  CA  VAL B 407      20.337  23.731 -57.083  1.00 34.15           C  
-ATOM   6393  C   VAL B 407      21.544  24.621 -57.367  1.00 40.74           C  
-ATOM   6394  O   VAL B 407      21.667  25.195 -58.451  1.00 35.05           O  
-ATOM   6395  CB  VAL B 407      19.095  24.349 -57.758  1.00 31.98           C  
-ATOM   6396  CG1 VAL B 407      17.927  23.377 -57.709  1.00 29.86           C  
-ATOM   6397  CG2 VAL B 407      18.734  25.673 -57.105  1.00 32.97           C  
-ATOM   6398  N   THR B 408      22.433  24.729 -56.386  1.00 49.34           N  
-ATOM   6399  CA  THR B 408      23.686  25.448 -56.569  1.00 33.03           C  
-ATOM   6400  C   THR B 408      24.660  24.614 -57.390  1.00 44.03           C  
-ATOM   6401  O   THR B 408      24.524  23.390 -57.476  1.00 46.45           O  
-ATOM   6402  CB  THR B 408      24.350  25.804 -55.224  1.00 31.78           C  
-ATOM   6403  OG1 THR B 408      24.681  24.603 -54.516  1.00 33.18           O  
-ATOM   6404  CG2 THR B 408      23.422  26.646 -54.372  1.00 39.07           C  
-ATOM   6405  N   ARG B 409      25.640  25.285 -57.989  1.00 49.40           N  
-ATOM   6406  CA  ARG B 409      26.685  24.618 -58.758  1.00 41.78           C  
-ATOM   6407  C   ARG B 409      27.383  23.544 -57.927  1.00 44.20           C  
-ATOM   6408  O   ARG B 409      27.671  22.454 -58.423  1.00 42.83           O  
-ATOM   6409  CB  ARG B 409      27.705  25.641 -59.262  1.00 30.87           C  
-ATOM   6410  CG  ARG B 409      28.919  25.048 -59.952  1.00 29.56           C  
-ATOM   6411  CD  ARG B 409      28.732  24.970 -61.458  1.00 40.03           C  
-ATOM   6412  NE  ARG B 409      28.096  23.728 -61.888  1.00 47.93           N  
-ATOM   6413  CZ  ARG B 409      26.831  23.632 -62.281  1.00 41.58           C  
-ATOM   6414  NH1 ARG B 409      26.058  24.709 -62.300  1.00 48.03           N  
-ATOM   6415  NH2 ARG B 409      26.339  22.459 -62.660  1.00 27.21           N  
-ATOM   6416  N   GLU B 410      27.637  23.856 -56.659  1.00 39.69           N  
-ATOM   6417  CA  GLU B 410      28.331  22.937 -55.768  1.00 39.17           C  
-ATOM   6418  C   GLU B 410      27.532  21.657 -55.531  1.00 43.42           C  
-ATOM   6419  O   GLU B 410      28.083  20.555 -55.583  1.00 40.95           O  
-ATOM   6420  CB  GLU B 410      28.637  23.626 -54.435  1.00 46.68           C  
-ATOM   6421  CG  GLU B 410      29.628  22.867 -53.564  1.00 67.38           C  
-ATOM   6422  CD  GLU B 410      30.065  23.661 -52.347  1.00 72.09           C  
-ATOM   6423  OE1 GLU B 410      31.288  23.853 -52.167  1.00 72.57           O  
-ATOM   6424  OE2 GLU B 410      29.186  24.090 -51.570  1.00 62.32           O  
-ATOM   6425  N   PHE B 411      26.236  21.808 -55.275  1.00 43.36           N  
-ATOM   6426  CA  PHE B 411      25.374  20.664 -54.989  1.00 40.57           C  
-ATOM   6427  C   PHE B 411      25.131  19.833 -56.241  1.00 40.41           C  
-ATOM   6428  O   PHE B 411      25.138  18.601 -56.189  1.00 43.71           O  
-ATOM   6429  CB  PHE B 411      24.037  21.125 -54.399  1.00 32.14           C  
-ATOM   6430  CG  PHE B 411      23.276  20.034 -53.698  1.00 35.87           C  
-ATOM   6431  CD1 PHE B 411      22.393  19.222 -54.393  1.00 39.22           C  
-ATOM   6432  CD2 PHE B 411      23.450  19.815 -52.341  1.00 49.40           C  
-ATOM   6433  CE1 PHE B 411      21.695  18.213 -53.744  1.00 40.20           C  
-ATOM   6434  CE2 PHE B 411      22.757  18.811 -51.687  1.00 50.82           C  
-ATOM   6435  CZ  PHE B 411      21.878  18.009 -52.389  1.00 42.93           C  
-ATOM   6436  N   LEU B 412      24.908  20.512 -57.363  1.00 36.33           N  
-ATOM   6437  CA  LEU B 412      24.735  19.833 -58.640  1.00 32.38           C  
-ATOM   6438  C   LEU B 412      25.981  19.033 -58.985  1.00 33.52           C  
-ATOM   6439  O   LEU B 412      25.892  17.917 -59.497  1.00 33.54           O  
-ATOM   6440  CB  LEU B 412      24.427  20.839 -59.750  1.00 31.74           C  
-ATOM   6441  CG  LEU B 412      23.059  21.520 -59.685  1.00 29.88           C  
-ATOM   6442  CD1 LEU B 412      22.924  22.542 -60.798  1.00 33.52           C  
-ATOM   6443  CD2 LEU B 412      21.945  20.491 -59.760  1.00 35.16           C  
-ATOM   6444  N   ASP B 413      27.141  19.613 -58.697  1.00 30.48           N  
-ATOM   6445  CA  ASP B 413      28.408  18.936 -58.930  1.00 30.23           C  
-ATOM   6446  C   ASP B 413      28.584  17.758 -57.976  1.00 36.69           C  
-ATOM   6447  O   ASP B 413      29.169  16.739 -58.342  1.00 37.69           O  
-ATOM   6448  CB  ASP B 413      29.573  19.917 -58.789  1.00 42.62           C  
-ATOM   6449  CG  ASP B 413      29.671  20.873 -59.959  1.00 35.19           C  
-ATOM   6450  OD1 ASP B 413      28.724  20.917 -60.770  1.00 33.68           O  
-ATOM   6451  OD2 ASP B 413      30.690  21.587 -60.063  1.00 42.68           O  
-ATOM   6452  N   SER B 414      28.079  17.898 -56.754  1.00 43.44           N  
-ATOM   6453  CA  SER B 414      28.116  16.800 -55.794  1.00 37.85           C  
-ATOM   6454  C   SER B 414      27.199  15.668 -56.253  1.00 45.05           C  
-ATOM   6455  O   SER B 414      27.417  14.504 -55.918  1.00 50.00           O  
-ATOM   6456  CB  SER B 414      27.712  17.280 -54.398  1.00 28.89           C  
-ATOM   6457  OG  SER B 414      26.325  17.555 -54.326  1.00 36.98           O  
-ATOM   6458  N   ARG B 415      26.178  16.020 -57.028  1.00 46.26           N  
-ATOM   6459  CA  ARG B 415      25.236  15.045 -57.571  1.00 42.06           C  
-ATOM   6460  C   ARG B 415      25.706  14.470 -58.907  1.00 38.36           C  
-ATOM   6461  O   ARG B 415      24.934  13.815 -59.610  1.00 41.78           O  
-ATOM   6462  CB  ARG B 415      23.855  15.685 -57.739  1.00 32.84           C  
-ATOM   6463  CG  ARG B 415      23.078  15.843 -56.445  1.00 34.93           C  
-ATOM   6464  CD  ARG B 415      22.585  14.498 -55.932  1.00 44.46           C  
-ATOM   6465  NE  ARG B 415      21.530  13.944 -56.776  1.00 36.61           N  
-ATOM   6466  CZ  ARG B 415      20.976  12.749 -56.591  1.00 39.54           C  
-ATOM   6467  NH1 ARG B 415      20.020  12.326 -57.406  1.00 39.29           N  
-ATOM   6468  NH2 ARG B 415      21.381  11.976 -55.595  1.00 41.08           N  
-ATOM   6469  N   ASN B 416      26.972  14.712 -59.238  1.00 39.06           N  
-ATOM   6470  CA  ASN B 416      27.541  14.325 -60.528  1.00 37.26           C  
-ATOM   6471  C   ASN B 416      26.729  14.870 -61.698  1.00 33.47           C  
-ATOM   6472  O   ASN B 416      26.454  14.158 -62.661  1.00 30.47           O  
-ATOM   6473  CB  ASN B 416      27.657  12.803 -60.637  1.00 31.43           C  
-ATOM   6474  CG  ASN B 416      28.627  12.219 -59.633  1.00 36.09           C  
-ATOM   6475  OD1 ASN B 416      28.229  11.759 -58.564  1.00 45.05           O  
-ATOM   6476  ND2 ASN B 416      29.911  12.233 -59.973  1.00 30.24           N  
-ATOM   6477  N   LEU B 417      26.341  16.137 -61.600  1.00 32.59           N  
-ATOM   6478  CA  LEU B 417      25.582  16.795 -62.658  1.00 33.42           C  
-ATOM   6479  C   LEU B 417      26.191  18.142 -63.040  1.00 39.17           C  
-ATOM   6480  O   LEU B 417      25.530  19.175 -62.922  1.00 35.76           O  
-ATOM   6481  CB  LEU B 417      24.129  16.996 -62.223  1.00 34.99           C  
-ATOM   6482  CG  LEU B 417      23.278  15.756 -61.951  1.00 36.46           C  
-ATOM   6483  CD1 LEU B 417      22.058  16.123 -61.119  1.00 27.21           C  
-ATOM   6484  CD2 LEU B 417      22.859  15.100 -63.259  1.00 33.26           C  
-ATOM   6485  N   PRO B 418      27.450  18.141 -63.513  1.00 38.61           N  
-ATOM   6486  CA  PRO B 418      28.099  19.420 -63.815  1.00 32.45           C  
-ATOM   6487  C   PRO B 418      27.512  20.094 -65.049  1.00 29.01           C  
-ATOM   6488  O   PRO B 418      27.768  21.272 -65.279  1.00 32.68           O  
-ATOM   6489  CB  PRO B 418      29.555  19.018 -64.054  1.00 29.52           C  
-ATOM   6490  CG  PRO B 418      29.460  17.644 -64.601  1.00 28.31           C  
-ATOM   6491  CD  PRO B 418      28.300  16.996 -63.887  1.00 34.48           C  
-ATOM   6492  N   HIS B 419      26.728  19.349 -65.822  1.00 28.89           N  
-ATOM   6493  CA  HIS B 419      26.168  19.851 -67.070  1.00 30.41           C  
-ATOM   6494  C   HIS B 419      24.803  20.502 -66.864  1.00 37.59           C  
-ATOM   6495  O   HIS B 419      24.113  20.834 -67.830  1.00 31.72           O  
-ATOM   6496  CB  HIS B 419      26.056  18.718 -68.091  1.00 35.89           C  
-ATOM   6497  CG  HIS B 419      25.228  17.562 -67.624  1.00 38.17           C  
-ATOM   6498  ND1 HIS B 419      25.778  16.429 -67.065  1.00 40.92           N  
-ATOM   6499  CD2 HIS B 419      23.887  17.363 -67.633  1.00 31.32           C  
-ATOM   6500  CE1 HIS B 419      24.815  15.582 -66.749  1.00 40.37           C  
-ATOM   6501  NE2 HIS B 419      23.658  16.126 -67.083  1.00 34.64           N  
-ATOM   6502  N   ARG B 420      24.417  20.680 -65.605  1.00 41.56           N  
-ATOM   6503  CA  ARG B 420      23.143  21.313 -65.284  1.00 40.55           C  
-ATOM   6504  C   ARG B 420      23.312  22.807 -65.049  1.00 41.85           C  
-ATOM   6505  O   ARG B 420      24.289  23.244 -64.438  1.00 37.69           O  
-ATOM   6506  CB  ARG B 420      22.514  20.666 -64.051  1.00 30.54           C  
-ATOM   6507  CG  ARG B 420      21.874  19.316 -64.309  1.00 35.21           C  
-ATOM   6508  CD  ARG B 420      20.384  19.445 -64.588  1.00 29.31           C  
-ATOM   6509  NE  ARG B 420      19.733  18.138 -64.602  1.00 39.83           N  
-ATOM   6510  CZ  ARG B 420      19.535  17.413 -65.698  1.00 37.55           C  
-ATOM   6511  NH1 ARG B 420      18.938  16.231 -65.613  1.00 34.67           N  
-ATOM   6512  NH2 ARG B 420      19.931  17.869 -66.880  1.00 23.99           N  
-ATOM   6513  N   GLU B 421      22.356  23.587 -65.543  1.00 42.60           N  
-ATOM   6514  CA  GLU B 421      22.314  25.016 -65.269  1.00 37.68           C  
-ATOM   6515  C   GLU B 421      21.916  25.227 -63.813  1.00 33.36           C  
-ATOM   6516  O   GLU B 421      21.229  24.389 -63.228  1.00 38.24           O  
-ATOM   6517  CB  GLU B 421      21.329  25.718 -66.206  1.00 33.14           C  
-ATOM   6518  CG  GLU B 421      21.798  27.073 -66.713  1.00 35.45           C  
-ATOM   6519  CD  GLU B 421      20.793  27.721 -67.647  1.00 44.79           C  
-ATOM   6520  OE1 GLU B 421      20.562  28.942 -67.518  1.00 42.32           O  
-ATOM   6521  OE2 GLU B 421      20.232  27.010 -68.509  1.00 42.75           O  
-ATOM   6522  N   VAL B 422      22.358  26.333 -63.222  1.00 33.59           N  
-ATOM   6523  CA  VAL B 422      21.977  26.651 -61.851  1.00 27.70           C  
-ATOM   6524  C   VAL B 422      20.478  26.910 -61.771  1.00 29.92           C  
-ATOM   6525  O   VAL B 422      19.958  27.797 -62.446  1.00 32.68           O  
-ATOM   6526  CB  VAL B 422      22.731  27.876 -61.316  1.00 23.26           C  
-ATOM   6527  CG1 VAL B 422      22.160  28.297 -59.970  1.00 31.85           C  
-ATOM   6528  CG2 VAL B 422      24.214  27.575 -61.205  1.00 28.14           C  
-ATOM   6529  N   GLY B 423      19.788  26.121 -60.954  1.00 31.39           N  
-ATOM   6530  CA  GLY B 423      18.351  26.250 -60.797  1.00 30.00           C  
-ATOM   6531  C   GLY B 423      17.593  25.045 -61.319  1.00 29.37           C  
-ATOM   6532  O   GLY B 423      16.470  24.778 -60.899  1.00 30.00           O  
-ATOM   6533  N   ASP B 424      18.211  24.312 -62.239  1.00 26.67           N  
-ATOM   6534  CA  ASP B 424      17.571  23.158 -62.856  1.00 18.83           C  
-ATOM   6535  C   ASP B 424      17.515  21.973 -61.898  1.00 28.11           C  
-ATOM   6536  O   ASP B 424      18.541  21.358 -61.601  1.00 40.59           O  
-ATOM   6537  CB  ASP B 424      18.314  22.769 -64.134  1.00 20.86           C  
-ATOM   6538  CG  ASP B 424      17.467  21.933 -65.072  1.00 34.29           C  
-ATOM   6539  OD1 ASP B 424      16.668  21.105 -64.587  1.00 37.45           O  
-ATOM   6540  OD2 ASP B 424      17.599  22.108 -66.302  1.00 32.92           O  
-ATOM   6541  N   ILE B 425      16.313  21.646 -61.426  1.00 25.54           N  
-ATOM   6542  CA  ILE B 425      16.135  20.540 -60.488  1.00 31.57           C  
-ATOM   6543  C   ILE B 425      16.075  19.189 -61.199  1.00 32.63           C  
-ATOM   6544  O   ILE B 425      15.877  18.153 -60.563  1.00 33.53           O  
-ATOM   6545  CB  ILE B 425      14.852  20.703 -59.645  1.00 25.09           C  
-ATOM   6546  CG1 ILE B 425      13.611  20.410 -60.490  1.00 30.34           C  
-ATOM   6547  CG2 ILE B 425      14.779  22.095 -59.044  1.00 25.30           C  
-ATOM   6548  CD1 ILE B 425      12.380  20.117 -59.666  1.00 27.13           C  
-ATOM   6549  N   GLY B 426      16.247  19.205 -62.516  1.00 25.15           N  
-ATOM   6550  CA  GLY B 426      16.171  17.988 -63.302  1.00 27.04           C  
-ATOM   6551  C   GLY B 426      14.743  17.494 -63.427  1.00 28.48           C  
-ATOM   6552  O   GLY B 426      13.809  18.195 -63.041  1.00 27.06           O  
-ATOM   6553  N   PRO B 427      14.564  16.277 -63.963  1.00 26.53           N  
-ATOM   6554  CA  PRO B 427      13.241  15.679 -64.178  1.00 25.48           C  
-ATOM   6555  C   PRO B 427      12.555  15.242 -62.883  1.00 24.94           C  
-ATOM   6556  O   PRO B 427      12.282  14.052 -62.712  1.00 26.07           O  
-ATOM   6557  CB  PRO B 427      13.555  14.465 -65.053  1.00 23.88           C  
-ATOM   6558  CG  PRO B 427      14.937  14.084 -64.662  1.00 24.63           C  
-ATOM   6559  CD  PRO B 427      15.647  15.384 -64.411  1.00 25.93           C  
-ATOM   6560  N   GLY B 428      12.270  16.190 -61.995  1.00 21.27           N  
-ATOM   6561  CA  GLY B 428      11.679  15.872 -60.708  1.00 17.70           C  
-ATOM   6562  C   GLY B 428      10.286  16.431 -60.483  1.00 23.93           C  
-ATOM   6563  O   GLY B 428       9.832  17.307 -61.218  1.00 40.39           O  
-ATOM   6564  N   TYR B 429       9.623  15.907 -59.452  1.00 28.79           N  
-ATOM   6565  CA  TYR B 429       8.271  16.302 -59.034  1.00 25.78           C  
-ATOM   6566  C   TYR B 429       7.312  16.646 -60.179  1.00 29.29           C  
-ATOM   6567  O   TYR B 429       6.691  15.760 -60.766  1.00 34.49           O  
-ATOM   6568  CB  TYR B 429       8.350  17.481 -58.060  1.00 22.15           C  
-ATOM   6569  CG  TYR B 429       8.910  17.109 -56.701  1.00 29.48           C  
-ATOM   6570  CD1 TYR B 429       8.282  16.160 -55.907  1.00 33.33           C  
-ATOM   6571  CD2 TYR B 429      10.060  17.713 -56.211  1.00 41.78           C  
-ATOM   6572  CE1 TYR B 429       8.787  15.816 -54.664  1.00 38.53           C  
-ATOM   6573  CE2 TYR B 429      10.574  17.379 -54.969  1.00 39.19           C  
-ATOM   6574  CZ  TYR B 429       9.933  16.431 -54.198  1.00 44.07           C  
-ATOM   6575  OH  TYR B 429      10.442  16.097 -52.962  1.00 42.66           O  
-ATOM   6576  N   GLY B 430       7.195  17.933 -60.487  1.00 29.88           N  
-ATOM   6577  CA  GLY B 430       6.278  18.397 -61.516  1.00 31.04           C  
-ATOM   6578  C   GLY B 430       6.467  17.752 -62.877  1.00 31.50           C  
-ATOM   6579  O   GLY B 430       5.493  17.402 -63.556  1.00 34.30           O  
-ATOM   6580  N   PHE B 431       7.725  17.597 -63.280  1.00 22.78           N  
-ATOM   6581  CA  PHE B 431       8.035  17.008 -64.573  1.00 28.48           C  
-ATOM   6582  C   PHE B 431       7.543  15.575 -64.662  1.00 30.01           C  
-ATOM   6583  O   PHE B 431       7.147  15.119 -65.733  1.00 30.94           O  
-ATOM   6584  CB  PHE B 431       9.536  17.046 -64.854  1.00 25.18           C  
-ATOM   6585  CG  PHE B 431       9.912  16.405 -66.159  1.00 23.71           C  
-ATOM   6586  CD1 PHE B 431       9.778  17.098 -67.349  1.00 28.65           C  
-ATOM   6587  CD2 PHE B 431      10.373  15.102 -66.200  1.00 20.94           C  
-ATOM   6588  CE1 PHE B 431      10.112  16.508 -68.553  1.00 27.49           C  
-ATOM   6589  CE2 PHE B 431      10.710  14.507 -67.400  1.00 22.81           C  
-ATOM   6590  CZ  PHE B 431      10.579  15.211 -68.579  1.00 20.99           C  
-ATOM   6591  N   GLN B 432       7.584  14.858 -63.544  1.00 25.53           N  
-ATOM   6592  CA  GLN B 432       7.073  13.498 -63.523  1.00 26.06           C  
-ATOM   6593  C   GLN B 432       5.552  13.535 -63.526  1.00 24.65           C  
-ATOM   6594  O   GLN B 432       4.912  12.782 -64.259  1.00 32.76           O  
-ATOM   6595  CB  GLN B 432       7.616  12.729 -62.314  1.00 24.90           C  
-ATOM   6596  CG  GLN B 432       9.119  12.476 -62.380  1.00 24.59           C  
-ATOM   6597  CD  GLN B 432       9.531  11.697 -63.624  1.00 28.05           C  
-ATOM   6598  OE1 GLN B 432       8.799  10.826 -64.095  1.00 32.15           O  
-ATOM   6599  NE2 GLN B 432      10.707  12.008 -64.159  1.00 27.61           N  
-ATOM   6600  N   TRP B 433       4.995  14.431 -62.713  1.00 21.98           N  
-ATOM   6601  CA  TRP B 433       3.553  14.669 -62.640  1.00 22.65           C  
-ATOM   6602  C   TRP B 433       2.907  14.823 -64.011  1.00 25.20           C  
-ATOM   6603  O   TRP B 433       1.943  14.129 -64.337  1.00 26.63           O  
-ATOM   6604  CB  TRP B 433       3.250  15.934 -61.826  1.00 24.37           C  
-ATOM   6605  CG  TRP B 433       3.320  15.793 -60.340  1.00 30.40           C  
-ATOM   6606  CD1 TRP B 433       3.951  14.813 -59.634  1.00 32.09           C  
-ATOM   6607  CD2 TRP B 433       2.725  16.664 -59.375  1.00 27.23           C  
-ATOM   6608  NE1 TRP B 433       3.791  15.022 -58.287  1.00 30.78           N  
-ATOM   6609  CE2 TRP B 433       3.041  16.155 -58.101  1.00 24.67           C  
-ATOM   6610  CE3 TRP B 433       1.956  17.830 -59.463  1.00 23.73           C  
-ATOM   6611  CZ2 TRP B 433       2.615  16.767 -56.925  1.00 29.02           C  
-ATOM   6612  CZ3 TRP B 433       1.536  18.436 -58.298  1.00 30.60           C  
-ATOM   6613  CH2 TRP B 433       1.864  17.905 -57.045  1.00 30.67           C  
-ATOM   6614  N   ARG B 434       3.446  15.740 -64.809  1.00 24.92           N  
-ATOM   6615  CA  ARG B 434       2.812  16.110 -66.068  1.00 22.70           C  
-ATOM   6616  C   ARG B 434       3.375  15.340 -67.260  1.00 26.07           C  
-ATOM   6617  O   ARG B 434       2.683  15.141 -68.259  1.00 26.70           O  
-ATOM   6618  CB  ARG B 434       2.953  17.618 -66.301  1.00 26.64           C  
-ATOM   6619  CG  ARG B 434       2.492  18.491 -65.134  1.00 24.39           C  
-ATOM   6620  CD  ARG B 434       1.130  18.063 -64.602  1.00 18.74           C  
-ATOM   6621  NE  ARG B 434       0.108  18.060 -65.644  1.00 29.03           N  
-ATOM   6622  CZ  ARG B 434      -0.741  19.058 -65.866  1.00 27.47           C  
-ATOM   6623  NH1 ARG B 434      -1.638  18.962 -66.838  1.00 20.42           N  
-ATOM   6624  NH2 ARG B 434      -0.699  20.150 -65.116  1.00 28.65           N  
-ATOM   6625  N   HIS B 435       4.629  14.914 -67.154  1.00 29.69           N  
-ATOM   6626  CA  HIS B 435       5.278  14.200 -68.248  1.00 33.50           C  
-ATOM   6627  C   HIS B 435       6.117  13.027 -67.758  1.00 25.92           C  
-ATOM   6628  O   HIS B 435       7.310  12.966 -68.037  1.00 29.34           O  
-ATOM   6629  CB  HIS B 435       6.169  15.146 -69.056  1.00 36.28           C  
-ATOM   6630  CG  HIS B 435       5.582  16.508 -69.259  1.00 36.32           C  
-ATOM   6631  ND1 HIS B 435       4.493  16.733 -70.074  1.00 35.17           N  
-ATOM   6632  CD2 HIS B 435       5.928  17.712 -68.751  1.00 32.62           C  
-ATOM   6633  CE1 HIS B 435       4.195  18.019 -70.059  1.00 41.97           C  
-ATOM   6634  NE2 HIS B 435       5.050  18.638 -69.265  1.00 34.04           N  
-ATOM   6635  N   PHE B 436       5.497  12.099 -67.035  1.00 20.61           N  
-ATOM   6636  CA  PHE B 436       6.196  10.904 -66.567  1.00 21.01           C  
-ATOM   6637  C   PHE B 436       6.850  10.124 -67.709  1.00 25.21           C  
-ATOM   6638  O   PHE B 436       6.248   9.919 -68.763  1.00 22.79           O  
-ATOM   6639  CB  PHE B 436       5.235   9.986 -65.812  1.00 19.18           C  
-ATOM   6640  CG  PHE B 436       5.915   8.848 -65.105  1.00 24.10           C  
-ATOM   6641  CD1 PHE B 436       6.167   7.654 -65.762  1.00 19.86           C  
-ATOM   6642  CD2 PHE B 436       6.299   8.970 -63.778  1.00 23.72           C  
-ATOM   6643  CE1 PHE B 436       6.796   6.610 -65.112  1.00 25.79           C  
-ATOM   6644  CE2 PHE B 436       6.924   7.927 -63.123  1.00 21.51           C  
-ATOM   6645  CZ  PHE B 436       7.173   6.746 -63.789  1.00 23.77           C  
-ATOM   6646  N   GLY B 437       8.088   9.694 -67.488  1.00 27.49           N  
-ATOM   6647  CA  GLY B 437       8.786   8.833 -68.427  1.00 29.12           C  
-ATOM   6648  C   GLY B 437       9.349   9.532 -69.649  1.00 28.32           C  
-ATOM   6649  O   GLY B 437       9.925   8.888 -70.528  1.00 25.33           O  
-ATOM   6650  N   ALA B 438       9.186  10.849 -69.710  1.00 28.93           N  
-ATOM   6651  CA  ALA B 438       9.679  11.623 -70.842  1.00 22.54           C  
-ATOM   6652  C   ALA B 438      11.179  11.856 -70.727  1.00 17.53           C  
-ATOM   6653  O   ALA B 438      11.717  11.949 -69.625  1.00 17.34           O  
-ATOM   6654  CB  ALA B 438       8.940  12.947 -70.940  1.00 24.08           C  
-ATOM   6655  N   ALA B 439      11.850  11.942 -71.870  1.00 18.82           N  
-ATOM   6656  CA  ALA B 439      13.281  12.218 -71.895  1.00 21.47           C  
-ATOM   6657  C   ALA B 439      13.539  13.676 -71.531  1.00 29.49           C  
-ATOM   6658  O   ALA B 439      13.054  14.584 -72.205  1.00 33.35           O  
-ATOM   6659  CB  ALA B 439      13.862  11.896 -73.263  1.00 26.85           C  
-ATOM   6660  N   TYR B 440      14.300  13.897 -70.463  1.00 28.45           N  
-ATOM   6661  CA  TYR B 440      14.564  15.249 -69.981  1.00 21.66           C  
-ATOM   6662  C   TYR B 440      15.800  15.859 -70.637  1.00 28.71           C  
-ATOM   6663  O   TYR B 440      16.847  15.220 -70.731  1.00 31.02           O  
-ATOM   6664  CB  TYR B 440      14.729  15.252 -68.458  1.00 21.22           C  
-ATOM   6665  CG  TYR B 440      14.784  16.640 -67.855  1.00 25.51           C  
-ATOM   6666  CD1 TYR B 440      13.621  17.359 -67.620  1.00 27.97           C  
-ATOM   6667  CD2 TYR B 440      15.996  17.230 -67.521  1.00 29.67           C  
-ATOM   6668  CE1 TYR B 440      13.662  18.627 -67.072  1.00 27.34           C  
-ATOM   6669  CE2 TYR B 440      16.048  18.499 -66.971  1.00 26.37           C  
-ATOM   6670  CZ  TYR B 440      14.877  19.192 -66.749  1.00 28.63           C  
-ATOM   6671  OH  TYR B 440      14.920  20.453 -66.204  1.00 28.15           O  
-ATOM   6672  N   LYS B 441      15.667  17.103 -71.088  1.00 28.66           N  
-ATOM   6673  CA  LYS B 441      16.792  17.843 -71.650  1.00 23.33           C  
-ATOM   6674  C   LYS B 441      17.297  18.876 -70.650  1.00 26.81           C  
-ATOM   6675  O   LYS B 441      18.318  18.671 -69.994  1.00 36.69           O  
-ATOM   6676  CB  LYS B 441      16.394  18.523 -72.961  1.00 26.87           C  
-ATOM   6677  CG  LYS B 441      16.677  17.702 -74.215  1.00 46.11           C  
-ATOM   6678  CD  LYS B 441      15.860  16.419 -74.258  1.00 54.04           C  
-ATOM   6679  CE  LYS B 441      16.086  15.667 -75.561  1.00 49.37           C  
-ATOM   6680  NZ  LYS B 441      15.711  16.488 -76.748  1.00 54.74           N  
-ATOM   6681  N   ASP B 442      16.575  19.987 -70.540  1.00 30.72           N  
-ATOM   6682  CA  ASP B 442      16.896  21.019 -69.560  1.00 33.98           C  
-ATOM   6683  C   ASP B 442      15.641  21.802 -69.174  1.00 32.94           C  
-ATOM   6684  O   ASP B 442      14.559  21.558 -69.708  1.00 29.41           O  
-ATOM   6685  CB  ASP B 442      17.977  21.962 -70.098  1.00 28.08           C  
-ATOM   6686  CG  ASP B 442      17.515  22.761 -71.301  1.00 34.32           C  
-ATOM   6687  OD1 ASP B 442      16.568  22.321 -71.988  1.00 32.47           O  
-ATOM   6688  OD2 ASP B 442      18.105  23.832 -71.561  1.00 38.05           O  
-ATOM   6689  N   MET B 443      15.792  22.750 -68.254  1.00 28.73           N  
-ATOM   6690  CA  MET B 443      14.652  23.475 -67.699  1.00 28.85           C  
-ATOM   6691  C   MET B 443      14.065  24.510 -68.655  1.00 28.72           C  
-ATOM   6692  O   MET B 443      13.188  25.285 -68.273  1.00 38.60           O  
-ATOM   6693  CB  MET B 443      15.055  24.166 -66.397  1.00 27.48           C  
-ATOM   6694  CG  MET B 443      16.138  25.212 -66.573  1.00 24.20           C  
-ATOM   6695  SD  MET B 443      16.683  25.913 -65.010  1.00 34.05           S  
-ATOM   6696  CE  MET B 443      17.893  27.107 -65.570  1.00 37.29           C  
-ATOM   6697  N   HIS B 444      14.546  24.526 -69.893  1.00 26.13           N  
-ATOM   6698  CA  HIS B 444      14.057  25.478 -70.882  1.00 34.47           C  
-ATOM   6699  C   HIS B 444      13.322  24.769 -72.012  1.00 34.89           C  
-ATOM   6700  O   HIS B 444      12.756  25.411 -72.899  1.00 32.47           O  
-ATOM   6701  CB  HIS B 444      15.211  26.308 -71.444  1.00 32.91           C  
-ATOM   6702  CG  HIS B 444      15.938  27.107 -70.409  1.00 30.32           C  
-ATOM   6703  ND1 HIS B 444      15.321  28.076 -69.648  1.00 31.62           N  
-ATOM   6704  CD2 HIS B 444      17.232  27.083 -70.011  1.00 28.93           C  
-ATOM   6705  CE1 HIS B 444      16.202  28.613 -68.824  1.00 41.44           C  
-ATOM   6706  NE2 HIS B 444      17.370  28.028 -69.024  1.00 32.86           N  
-ATOM   6707  N   THR B 445      13.331  23.441 -71.970  1.00 33.10           N  
-ATOM   6708  CA  THR B 445      12.738  22.634 -73.029  1.00 33.60           C  
-ATOM   6709  C   THR B 445      11.229  22.491 -72.855  1.00 31.45           C  
-ATOM   6710  O   THR B 445      10.741  22.283 -71.745  1.00 36.48           O  
-ATOM   6711  CB  THR B 445      13.377  21.234 -73.080  1.00 31.91           C  
-ATOM   6712  OG1 THR B 445      14.804  21.361 -73.107  1.00 29.18           O  
-ATOM   6713  CG2 THR B 445      12.912  20.472 -74.313  1.00 35.45           C  
-ATOM   6714  N   ASP B 446      10.497  22.606 -73.959  1.00 34.86           N  
-ATOM   6715  CA  ASP B 446       9.048  22.448 -73.946  1.00 37.40           C  
-ATOM   6716  C   ASP B 446       8.666  20.980 -74.116  1.00 41.59           C  
-ATOM   6717  O   ASP B 446       8.744  20.432 -75.216  1.00 38.56           O  
-ATOM   6718  CB  ASP B 446       8.408  23.291 -75.049  1.00 46.89           C  
-ATOM   6719  CG  ASP B 446       6.895  23.296 -74.974  1.00 51.03           C  
-ATOM   6720  OD1 ASP B 446       6.357  23.368 -73.849  1.00 60.65           O  
-ATOM   6721  OD2 ASP B 446       6.245  23.226 -76.039  1.00 37.22           O  
-ATOM   6722  N   TYR B 447       8.248  20.349 -73.024  1.00 45.92           N  
-ATOM   6723  CA  TYR B 447       7.937  18.924 -73.035  1.00 35.92           C  
-ATOM   6724  C   TYR B 447       6.456  18.645 -73.257  1.00 43.87           C  
-ATOM   6725  O   TYR B 447       5.970  17.572 -72.898  1.00 44.58           O  
-ATOM   6726  CB  TYR B 447       8.374  18.271 -71.721  1.00 28.10           C  
-ATOM   6727  CG  TYR B 447       9.829  18.472 -71.383  1.00 25.00           C  
-ATOM   6728  CD1 TYR B 447      10.810  17.672 -71.951  1.00 29.96           C  
-ATOM   6729  CD2 TYR B 447      10.223  19.455 -70.488  1.00 27.58           C  
-ATOM   6730  CE1 TYR B 447      12.144  17.851 -71.642  1.00 31.07           C  
-ATOM   6731  CE2 TYR B 447      11.554  19.641 -70.172  1.00 34.97           C  
-ATOM   6732  CZ  TYR B 447      12.511  18.837 -70.752  1.00 31.06           C  
-ATOM   6733  OH  TYR B 447      13.839  19.020 -70.440  1.00 35.36           O  
-ATOM   6734  N   THR B 448       5.740  19.599 -73.845  1.00 49.58           N  
-ATOM   6735  CA  THR B 448       4.294  19.456 -73.991  1.00 52.58           C  
-ATOM   6736  C   THR B 448       3.952  18.279 -74.910  1.00 47.35           C  
-ATOM   6737  O   THR B 448       4.627  18.036 -75.915  1.00 40.56           O  
-ATOM   6738  CB  THR B 448       3.636  20.762 -74.513  1.00 43.12           C  
-ATOM   6739  OG1 THR B 448       2.218  20.694 -74.319  1.00 43.24           O  
-ATOM   6740  CG2 THR B 448       3.942  20.999 -75.989  1.00 45.47           C  
-ATOM   6741  N   GLY B 449       2.924  17.526 -74.529  1.00 39.50           N  
-ATOM   6742  CA  GLY B 449       2.507  16.358 -75.282  1.00 33.87           C  
-ATOM   6743  C   GLY B 449       3.282  15.097 -74.941  1.00 37.28           C  
-ATOM   6744  O   GLY B 449       2.811  13.986 -75.186  1.00 43.89           O  
-ATOM   6745  N   GLN B 450       4.472  15.264 -74.374  1.00 37.37           N  
-ATOM   6746  CA  GLN B 450       5.337  14.131 -74.056  1.00 33.78           C  
-ATOM   6747  C   GLN B 450       4.992  13.484 -72.715  1.00 39.86           C  
-ATOM   6748  O   GLN B 450       4.496  14.147 -71.803  1.00 44.57           O  
-ATOM   6749  CB  GLN B 450       6.802  14.565 -74.042  1.00 29.53           C  
-ATOM   6750  CG  GLN B 450       7.303  15.145 -75.352  1.00 33.74           C  
-ATOM   6751  CD  GLN B 450       8.768  15.529 -75.285  1.00 40.08           C  
-ATOM   6752  OE1 GLN B 450       9.636  14.681 -75.074  1.00 39.77           O  
-ATOM   6753  NE2 GLN B 450       9.050  16.815 -75.454  1.00 41.12           N  
-ATOM   6754  N   GLY B 451       5.265  12.186 -72.606  1.00 38.63           N  
-ATOM   6755  CA  GLY B 451       5.078  11.455 -71.365  1.00 26.99           C  
-ATOM   6756  C   GLY B 451       3.629  11.297 -70.949  1.00 27.51           C  
-ATOM   6757  O   GLY B 451       2.716  11.659 -71.690  1.00 26.14           O  
-ATOM   6758  N   VAL B 452       3.422  10.754 -69.754  1.00 25.01           N  
-ATOM   6759  CA  VAL B 452       2.080  10.547 -69.220  1.00 23.08           C  
-ATOM   6760  C   VAL B 452       1.664  11.719 -68.334  1.00 25.04           C  
-ATOM   6761  O   VAL B 452       2.434  12.169 -67.487  1.00 23.68           O  
-ATOM   6762  CB  VAL B 452       1.992   9.239 -68.412  1.00 14.57           C  
-ATOM   6763  CG1 VAL B 452       0.588   9.037 -67.856  1.00 14.88           C  
-ATOM   6764  CG2 VAL B 452       2.399   8.060 -69.281  1.00 13.55           C  
-ATOM   6765  N   ASP B 453       0.450  12.219 -68.538  1.00 26.77           N  
-ATOM   6766  CA  ASP B 453      -0.073  13.293 -67.701  1.00 22.17           C  
-ATOM   6767  C   ASP B 453      -0.907  12.726 -66.555  1.00 27.15           C  
-ATOM   6768  O   ASP B 453      -2.135  12.681 -66.621  1.00 27.31           O  
-ATOM   6769  CB  ASP B 453      -0.898  14.274 -68.530  1.00 29.29           C  
-ATOM   6770  CG  ASP B 453      -1.101  15.603 -67.828  1.00 30.69           C  
-ATOM   6771  OD1 ASP B 453      -1.049  15.642 -66.579  1.00 25.66           O  
-ATOM   6772  OD2 ASP B 453      -1.320  16.612 -68.528  1.00 29.17           O  
-ATOM   6773  N   GLN B 454      -0.216  12.310 -65.499  1.00 29.29           N  
-ATOM   6774  CA  GLN B 454      -0.848  11.685 -64.344  1.00 20.83           C  
-ATOM   6775  C   GLN B 454      -1.906  12.569 -63.702  1.00 26.73           C  
-ATOM   6776  O   GLN B 454      -2.931  12.071 -63.248  1.00 34.33           O  
-ATOM   6777  CB  GLN B 454       0.198  11.322 -63.297  1.00 16.22           C  
-ATOM   6778  CG  GLN B 454       1.252  10.356 -63.789  1.00 17.63           C  
-ATOM   6779  CD  GLN B 454       2.154   9.875 -62.675  1.00 24.75           C  
-ATOM   6780  OE1 GLN B 454       1.801   8.963 -61.926  1.00 26.74           O  
-ATOM   6781  NE2 GLN B 454       3.326  10.487 -62.556  1.00 27.46           N  
-ATOM   6782  N   LEU B 455      -1.654  13.874 -63.654  1.00 26.68           N  
-ATOM   6783  CA  LEU B 455      -2.602  14.803 -63.049  1.00 26.32           C  
-ATOM   6784  C   LEU B 455      -3.902  14.844 -63.844  1.00 24.54           C  
-ATOM   6785  O   LEU B 455      -4.999  14.711 -63.289  1.00 19.54           O  
-ATOM   6786  CB  LEU B 455      -1.982  16.200 -62.950  1.00 17.82           C  
-ATOM   6787  CG  LEU B 455      -2.731  17.239 -62.115  1.00 15.38           C  
-ATOM   6788  CD1 LEU B 455      -2.932  16.746 -60.697  1.00 14.89           C  
-ATOM   6789  CD2 LEU B 455      -1.978  18.556 -62.109  1.00 16.75           C  
-ATOM   6790  N   LYS B 456      -3.764  15.019 -65.153  1.00 28.46           N  
-ATOM   6791  CA  LYS B 456      -4.918  15.093 -66.039  1.00 32.84           C  
-ATOM   6792  C   LYS B 456      -5.693  13.788 -66.033  1.00 27.16           C  
-ATOM   6793  O   LYS B 456      -6.918  13.792 -66.073  1.00 22.81           O  
-ATOM   6794  CB  LYS B 456      -4.493  15.439 -67.470  1.00 29.59           C  
-ATOM   6795  CG  LYS B 456      -5.641  15.895 -68.352  1.00 33.86           C  
-ATOM   6796  CD  LYS B 456      -5.171  16.171 -69.772  1.00 49.56           C  
-ATOM   6797  CE  LYS B 456      -5.521  15.022 -70.706  1.00 63.49           C  
-ATOM   6798  NZ  LYS B 456      -4.893  13.742 -70.279  1.00 72.36           N  
-ATOM   6799  N   ASN B 457      -4.973  12.672 -65.983  1.00 23.08           N  
-ATOM   6800  CA  ASN B 457      -5.611  11.364 -65.941  1.00 25.96           C  
-ATOM   6801  C   ASN B 457      -6.376  11.163 -64.636  1.00 28.34           C  
-ATOM   6802  O   ASN B 457      -7.499  10.657 -64.637  1.00 29.81           O  
-ATOM   6803  CB  ASN B 457      -4.574  10.249 -66.129  1.00 24.07           C  
-ATOM   6804  CG  ASN B 457      -3.901  10.298 -67.487  1.00 29.03           C  
-ATOM   6805  OD1 ASN B 457      -4.325  11.036 -68.378  1.00 25.09           O  
-ATOM   6806  ND2 ASN B 457      -2.847   9.504 -67.655  1.00 29.57           N  
-ATOM   6807  N   VAL B 458      -5.760  11.565 -63.528  1.00 23.05           N  
-ATOM   6808  CA  VAL B 458      -6.386  11.466 -62.218  1.00 21.90           C  
-ATOM   6809  C   VAL B 458      -7.667  12.284 -62.176  1.00 21.49           C  
-ATOM   6810  O   VAL B 458      -8.705  11.803 -61.729  1.00 27.10           O  
-ATOM   6811  CB  VAL B 458      -5.439  11.937 -61.096  1.00 20.25           C  
-ATOM   6812  CG1 VAL B 458      -6.230  12.346 -59.866  1.00 18.95           C  
-ATOM   6813  CG2 VAL B 458      -4.443  10.842 -60.750  1.00 15.84           C  
-ATOM   6814  N   ILE B 459      -7.591  13.519 -62.657  1.00 22.97           N  
-ATOM   6815  CA  ILE B 459      -8.766  14.379 -62.710  1.00 24.44           C  
-ATOM   6816  C   ILE B 459      -9.854  13.787 -63.606  1.00 22.90           C  
-ATOM   6817  O   ILE B 459     -11.026  13.761 -63.228  1.00 22.72           O  
-ATOM   6818  CB  ILE B 459      -8.403  15.790 -63.205  1.00 22.12           C  
-ATOM   6819  CG1 ILE B 459      -7.599  16.522 -62.133  1.00 20.86           C  
-ATOM   6820  CG2 ILE B 459      -9.656  16.577 -63.546  1.00 18.17           C  
-ATOM   6821  CD1 ILE B 459      -7.176  17.908 -62.540  1.00 29.32           C  
-ATOM   6822  N   GLN B 460      -9.463  13.299 -64.781  1.00 21.13           N  
-ATOM   6823  CA  GLN B 460     -10.414  12.696 -65.712  1.00 25.53           C  
-ATOM   6824  C   GLN B 460     -11.157  11.530 -65.074  1.00 25.61           C  
-ATOM   6825  O   GLN B 460     -12.386  11.473 -65.102  1.00 25.30           O  
-ATOM   6826  CB  GLN B 460      -9.700  12.229 -66.985  1.00 32.39           C  
-ATOM   6827  CG  GLN B 460     -10.574  11.405 -67.927  1.00 40.06           C  
-ATOM   6828  CD  GLN B 460     -11.568  12.246 -68.710  1.00 41.64           C  
-ATOM   6829  OE1 GLN B 460     -11.696  13.454 -68.493  1.00 39.66           O  
-ATOM   6830  NE2 GLN B 460     -12.276  11.607 -69.635  1.00 32.67           N  
-ATOM   6831  N   MET B 461     -10.399  10.609 -64.491  1.00 29.64           N  
-ATOM   6832  CA  MET B 461     -10.979   9.443 -63.840  1.00 24.97           C  
-ATOM   6833  C   MET B 461     -11.840   9.858 -62.655  1.00 19.73           C  
-ATOM   6834  O   MET B 461     -12.819   9.199 -62.337  1.00 28.71           O  
-ATOM   6835  CB  MET B 461      -9.881   8.469 -63.391  1.00 33.73           C  
-ATOM   6836  CG  MET B 461     -10.410   7.141 -62.863  1.00 41.30           C  
-ATOM   6837  SD  MET B 461     -11.392   6.233 -64.076  1.00 45.26           S  
-ATOM   6838  CE  MET B 461     -10.119   5.733 -65.236  1.00 43.37           C  
-ATOM   6839  N   LEU B 462     -11.474  10.955 -62.003  1.00 20.10           N  
-ATOM   6840  CA  LEU B 462     -12.280  11.473 -60.904  1.00 18.19           C  
-ATOM   6841  C   LEU B 462     -13.629  11.972 -61.402  1.00 19.94           C  
-ATOM   6842  O   LEU B 462     -14.658  11.748 -60.764  1.00 19.83           O  
-ATOM   6843  CB  LEU B 462     -11.547  12.601 -60.173  1.00 15.12           C  
-ATOM   6844  CG  LEU B 462     -10.562  12.181 -59.080  1.00 22.21           C  
-ATOM   6845  CD1 LEU B 462      -9.781  13.374 -58.563  1.00 23.08           C  
-ATOM   6846  CD2 LEU B 462     -11.290  11.498 -57.943  1.00 19.19           C  
-ATOM   6847  N   ARG B 463     -13.620  12.640 -62.551  1.00 19.28           N  
-ATOM   6848  CA  ARG B 463     -14.823  13.279 -63.067  1.00 14.99           C  
-ATOM   6849  C   ARG B 463     -15.725  12.320 -63.841  1.00 17.39           C  
-ATOM   6850  O   ARG B 463     -16.916  12.584 -64.003  1.00 18.05           O  
-ATOM   6851  CB  ARG B 463     -14.446  14.476 -63.946  1.00 12.32           C  
-ATOM   6852  CG  ARG B 463     -13.686  15.557 -63.187  1.00 16.20           C  
-ATOM   6853  CD  ARG B 463     -13.846  16.947 -63.790  1.00 16.69           C  
-ATOM   6854  NE  ARG B 463     -12.964  17.182 -64.929  1.00 22.14           N  
-ATOM   6855  CZ  ARG B 463     -12.470  18.374 -65.255  1.00 19.66           C  
-ATOM   6856  NH1 ARG B 463     -12.760  19.439 -64.521  1.00 11.40           N  
-ATOM   6857  NH2 ARG B 463     -11.679  18.501 -66.312  1.00 20.44           N  
-ATOM   6858  N   THR B 464     -15.173  11.204 -64.307  1.00 20.93           N  
-ATOM   6859  CA  THR B 464     -15.970  10.256 -65.081  1.00 17.73           C  
-ATOM   6860  C   THR B 464     -16.325   8.992 -64.301  1.00 18.81           C  
-ATOM   6861  O   THR B 464     -17.393   8.418 -64.498  1.00 29.83           O  
-ATOM   6862  CB  THR B 464     -15.251   9.839 -66.378  1.00 16.35           C  
-ATOM   6863  OG1 THR B 464     -14.107   9.037 -66.061  1.00 28.90           O  
-ATOM   6864  CG2 THR B 464     -14.813  11.065 -67.167  1.00 16.51           C  
-ATOM   6865  N   ASN B 465     -15.432   8.562 -63.415  1.00 20.12           N  
-ATOM   6866  CA  ASN B 465     -15.600   7.291 -62.718  1.00 22.80           C  
-ATOM   6867  C   ASN B 465     -14.843   7.250 -61.389  1.00 26.82           C  
-ATOM   6868  O   ASN B 465     -13.760   6.669 -61.301  1.00 28.48           O  
-ATOM   6869  CB  ASN B 465     -15.139   6.148 -63.622  1.00 24.71           C  
-ATOM   6870  CG  ASN B 465     -15.345   4.788 -62.997  1.00 35.03           C  
-ATOM   6871  OD1 ASN B 465     -16.317   4.563 -62.277  1.00 32.29           O  
-ATOM   6872  ND2 ASN B 465     -14.422   3.870 -63.261  1.00 39.24           N  
-ATOM   6873  N   PRO B 466     -15.417   7.863 -60.344  1.00 26.68           N  
-ATOM   6874  CA  PRO B 466     -14.732   8.064 -59.060  1.00 36.85           C  
-ATOM   6875  C   PRO B 466     -14.526   6.794 -58.228  1.00 33.02           C  
-ATOM   6876  O   PRO B 466     -13.867   6.859 -57.189  1.00 31.23           O  
-ATOM   6877  CB  PRO B 466     -15.663   9.035 -58.324  1.00 30.24           C  
-ATOM   6878  CG  PRO B 466     -17.009   8.736 -58.876  1.00 28.77           C  
-ATOM   6879  CD  PRO B 466     -16.784   8.413 -60.327  1.00 30.63           C  
-ATOM   6880  N   THR B 467     -15.071   5.665 -58.664  1.00 26.82           N  
-ATOM   6881  CA  THR B 467     -14.936   4.429 -57.897  1.00 34.49           C  
-ATOM   6882  C   THR B 467     -13.687   3.648 -58.301  1.00 36.83           C  
-ATOM   6883  O   THR B 467     -13.380   2.604 -57.722  1.00 32.14           O  
-ATOM   6884  CB  THR B 467     -16.173   3.522 -58.056  1.00 37.09           C  
-ATOM   6885  OG1 THR B 467     -16.344   3.176 -59.436  1.00 45.89           O  
-ATOM   6886  CG2 THR B 467     -17.419   4.232 -57.555  1.00 30.02           C  
-ATOM   6887  N   ASP B 468     -12.970   4.160 -59.296  1.00 32.76           N  
-ATOM   6888  CA  ASP B 468     -11.741   3.527 -59.761  1.00 34.50           C  
-ATOM   6889  C   ASP B 468     -10.644   3.648 -58.708  1.00 34.48           C  
-ATOM   6890  O   ASP B 468     -10.444   4.713 -58.127  1.00 41.66           O  
-ATOM   6891  CB  ASP B 468     -11.287   4.150 -61.083  1.00 33.72           C  
-ATOM   6892  CG  ASP B 468      -9.927   3.650 -61.529  1.00 33.53           C  
-ATOM   6893  OD1 ASP B 468      -9.865   2.579 -62.166  1.00 37.87           O  
-ATOM   6894  OD2 ASP B 468      -8.920   4.333 -61.252  1.00 35.24           O  
-ATOM   6895  N   ARG B 469      -9.937   2.549 -58.460  1.00 44.33           N  
-ATOM   6896  CA  ARG B 469      -8.910   2.522 -57.424  1.00 41.82           C  
-ATOM   6897  C   ARG B 469      -7.506   2.614 -58.008  1.00 34.53           C  
-ATOM   6898  O   ARG B 469      -6.539   2.165 -57.394  1.00 33.76           O  
-ATOM   6899  CB  ARG B 469      -9.046   1.254 -56.580  1.00 31.70           C  
-ATOM   6900  CG  ARG B 469     -10.339   1.191 -55.792  1.00 29.65           C  
-ATOM   6901  CD  ARG B 469     -10.597  -0.201 -55.248  1.00 37.16           C  
-ATOM   6902  NE  ARG B 469     -10.755  -1.181 -56.318  1.00 54.61           N  
-ATOM   6903  CZ  ARG B 469     -11.599  -2.206 -56.272  1.00 45.96           C  
-ATOM   6904  NH1 ARG B 469     -12.372  -2.382 -55.209  1.00 34.00           N  
-ATOM   6905  NH2 ARG B 469     -11.678  -3.052 -57.291  1.00 40.47           N  
-ATOM   6906  N   ARG B 470      -7.404   3.198 -59.198  1.00 36.47           N  
-ATOM   6907  CA  ARG B 470      -6.115   3.398 -59.852  1.00 33.63           C  
-ATOM   6908  C   ARG B 470      -5.845   4.883 -60.069  1.00 28.22           C  
-ATOM   6909  O   ARG B 470      -5.182   5.267 -61.034  1.00 23.35           O  
-ATOM   6910  CB  ARG B 470      -6.060   2.660 -61.194  1.00 24.82           C  
-ATOM   6911  CG  ARG B 470      -6.087   1.143 -61.102  1.00 22.94           C  
-ATOM   6912  CD  ARG B 470      -7.486   0.589 -61.331  1.00 31.44           C  
-ATOM   6913  NE  ARG B 470      -7.478  -0.864 -61.487  1.00 46.41           N  
-ATOM   6914  CZ  ARG B 470      -7.672  -1.503 -62.639  1.00 50.88           C  
-ATOM   6915  NH1 ARG B 470      -7.907  -0.823 -63.754  1.00 48.61           N  
-ATOM   6916  NH2 ARG B 470      -7.641  -2.829 -62.674  1.00 42.63           N  
-ATOM   6917  N   MET B 471      -6.364   5.715 -59.171  1.00 22.01           N  
-ATOM   6918  CA  MET B 471      -6.218   7.161 -59.297  1.00 23.40           C  
-ATOM   6919  C   MET B 471      -4.991   7.667 -58.541  1.00 22.21           C  
-ATOM   6920  O   MET B 471      -5.110   8.392 -57.553  1.00 18.19           O  
-ATOM   6921  CB  MET B 471      -7.485   7.861 -58.803  1.00 20.76           C  
-ATOM   6922  CG  MET B 471      -8.743   7.398 -59.523  1.00 22.34           C  
-ATOM   6923  SD  MET B 471     -10.221   8.317 -59.062  1.00 21.91           S  
-ATOM   6924  CE  MET B 471     -10.360   7.901 -57.325  1.00 25.67           C  
-ATOM   6925  N   LEU B 472      -3.812   7.282 -59.020  1.00 29.03           N  
-ATOM   6926  CA  LEU B 472      -2.561   7.614 -58.346  1.00 22.50           C  
-ATOM   6927  C   LEU B 472      -1.646   8.509 -59.172  1.00 20.90           C  
-ATOM   6928  O   LEU B 472      -1.636   8.456 -60.402  1.00 20.38           O  
-ATOM   6929  CB  LEU B 472      -1.800   6.339 -57.973  1.00 26.99           C  
-ATOM   6930  CG  LEU B 472      -2.278   5.544 -56.758  1.00 27.63           C  
-ATOM   6931  CD1 LEU B 472      -3.432   4.615 -57.112  1.00 28.14           C  
-ATOM   6932  CD2 LEU B 472      -1.116   4.771 -56.158  1.00 36.05           C  
-ATOM   6933  N   MET B 473      -0.865   9.319 -58.469  1.00 24.95           N  
-ATOM   6934  CA  MET B 473       0.150  10.157 -59.083  1.00 26.39           C  
-ATOM   6935  C   MET B 473       1.488   9.877 -58.405  1.00 24.89           C  
-ATOM   6936  O   MET B 473       1.642  10.102 -57.202  1.00 31.92           O  
-ATOM   6937  CB  MET B 473      -0.231  11.634 -58.968  1.00 18.23           C  
-ATOM   6938  CG  MET B 473       0.609  12.567 -59.816  1.00 20.97           C  
-ATOM   6939  SD  MET B 473      -0.133  14.207 -59.953  1.00 41.63           S  
-ATOM   6940  CE  MET B 473      -0.142  14.740 -58.245  1.00 19.52           C  
-ATOM   6941  N   THR B 474       2.444   9.359 -59.170  1.00 15.72           N  
-ATOM   6942  CA  THR B 474       3.749   9.018 -58.614  1.00 17.77           C  
-ATOM   6943  C   THR B 474       4.834   9.939 -59.154  1.00 21.98           C  
-ATOM   6944  O   THR B 474       4.744  10.430 -60.280  1.00 28.86           O  
-ATOM   6945  CB  THR B 474       4.135   7.559 -58.918  1.00 22.60           C  
-ATOM   6946  OG1 THR B 474       5.428   7.277 -58.367  1.00 20.22           O  
-ATOM   6947  CG2 THR B 474       4.172   7.314 -60.417  1.00 29.13           C  
-ATOM   6948  N   ALA B 475       5.857  10.176 -58.339  1.00 20.08           N  
-ATOM   6949  CA  ALA B 475       6.988  10.999 -58.748  1.00 20.22           C  
-ATOM   6950  C   ALA B 475       8.271  10.177 -58.747  1.00 18.42           C  
-ATOM   6951  O   ALA B 475       9.325  10.654 -59.165  1.00 23.16           O  
-ATOM   6952  CB  ALA B 475       7.128  12.205 -57.832  1.00 21.47           C  
-ATOM   6953  N   TRP B 476       8.169   8.936 -58.284  1.00 13.51           N  
-ATOM   6954  CA  TRP B 476       9.334   8.076 -58.134  1.00 16.67           C  
-ATOM   6955  C   TRP B 476       9.647   7.318 -59.420  1.00 19.74           C  
-ATOM   6956  O   TRP B 476       9.075   6.262 -59.685  1.00 27.62           O  
-ATOM   6957  CB  TRP B 476       9.120   7.096 -56.976  1.00 20.09           C  
-ATOM   6958  CG  TRP B 476      10.384   6.455 -56.495  1.00 22.24           C  
-ATOM   6959  CD1 TRP B 476      10.814   5.190 -56.762  1.00 26.57           C  
-ATOM   6960  CD2 TRP B 476      11.389   7.056 -55.670  1.00 25.68           C  
-ATOM   6961  NE1 TRP B 476      12.024   4.963 -56.150  1.00 27.92           N  
-ATOM   6962  CE2 TRP B 476      12.399   6.095 -55.474  1.00 25.56           C  
-ATOM   6963  CE3 TRP B 476      11.533   8.314 -55.077  1.00 19.95           C  
-ATOM   6964  CZ2 TRP B 476      13.536   6.351 -54.711  1.00 22.40           C  
-ATOM   6965  CZ3 TRP B 476      12.660   8.566 -54.320  1.00 16.71           C  
-ATOM   6966  CH2 TRP B 476      13.647   7.589 -54.143  1.00 18.67           C  
-ATOM   6967  N   ASN B 477      10.559   7.869 -60.215  1.00 17.52           N  
-ATOM   6968  CA  ASN B 477      10.990   7.239 -61.457  1.00 21.25           C  
-ATOM   6969  C   ASN B 477      12.456   6.825 -61.382  1.00 28.73           C  
-ATOM   6970  O   ASN B 477      13.345   7.639 -61.633  1.00 34.15           O  
-ATOM   6971  CB  ASN B 477      10.771   8.186 -62.641  1.00 23.88           C  
-ATOM   6972  CG  ASN B 477      11.069   7.536 -63.988  1.00 32.85           C  
-ATOM   6973  OD1 ASN B 477      11.577   6.418 -64.061  1.00 36.16           O  
-ATOM   6974  ND2 ASN B 477      10.755   8.249 -65.067  1.00 31.68           N  
-ATOM   6975  N   PRO B 478      12.708   5.552 -61.039  1.00 29.19           N  
-ATOM   6976  CA  PRO B 478      14.048   4.960 -60.937  1.00 25.95           C  
-ATOM   6977  C   PRO B 478      14.950   5.253 -62.138  1.00 28.47           C  
-ATOM   6978  O   PRO B 478      16.163   5.365 -61.973  1.00 34.61           O  
-ATOM   6979  CB  PRO B 478      13.753   3.462 -60.837  1.00 24.71           C  
-ATOM   6980  CG  PRO B 478      12.439   3.408 -60.145  1.00 32.76           C  
-ATOM   6981  CD  PRO B 478      11.658   4.596 -60.646  1.00 29.81           C  
-ATOM   6982  N   ALA B 479      14.360   5.383 -63.323  1.00 27.17           N  
-ATOM   6983  CA  ALA B 479      15.124   5.622 -64.544  1.00 26.29           C  
-ATOM   6984  C   ALA B 479      15.528   7.088 -64.703  1.00 32.03           C  
-ATOM   6985  O   ALA B 479      16.165   7.458 -65.689  1.00 33.10           O  
-ATOM   6986  CB  ALA B 479      14.326   5.169 -65.758  1.00 23.28           C  
-ATOM   6987  N   ALA B 480      15.160   7.918 -63.732  1.00 31.75           N  
-ATOM   6988  CA  ALA B 480      15.428   9.349 -63.817  1.00 29.01           C  
-ATOM   6989  C   ALA B 480      16.012   9.906 -62.518  1.00 31.11           C  
-ATOM   6990  O   ALA B 480      16.412  11.070 -62.460  1.00 29.90           O  
-ATOM   6991  CB  ALA B 480      14.152  10.094 -64.187  1.00 29.65           C  
-ATOM   6992  N   LEU B 481      16.070   9.067 -61.487  1.00 32.65           N  
-ATOM   6993  CA  LEU B 481      16.519   9.489 -60.163  1.00 27.63           C  
-ATOM   6994  C   LEU B 481      17.867  10.204 -60.206  1.00 31.04           C  
-ATOM   6995  O   LEU B 481      17.987  11.346 -59.759  1.00 32.41           O  
-ATOM   6996  CB  LEU B 481      16.596   8.286 -59.219  1.00 33.06           C  
-ATOM   6997  CG  LEU B 481      15.287   7.660 -58.727  1.00 28.50           C  
-ATOM   6998  CD1 LEU B 481      15.583   6.423 -57.897  1.00 41.10           C  
-ATOM   6999  CD2 LEU B 481      14.472   8.650 -57.920  1.00 18.32           C  
-ATOM   7000  N   ASP B 482      18.868   9.536 -60.772  1.00 31.89           N  
-ATOM   7001  CA  ASP B 482      20.219  10.081 -60.854  1.00 30.31           C  
-ATOM   7002  C   ASP B 482      20.276  11.407 -61.611  1.00 29.24           C  
-ATOM   7003  O   ASP B 482      21.222  12.175 -61.448  1.00 29.14           O  
-ATOM   7004  CB  ASP B 482      21.161   9.071 -61.519  1.00 44.86           C  
-ATOM   7005  CG  ASP B 482      21.313   7.790 -60.714  1.00 47.86           C  
-ATOM   7006  OD1 ASP B 482      20.850   7.757 -59.553  1.00 38.13           O  
-ATOM   7007  OD2 ASP B 482      21.904   6.819 -61.240  1.00 27.15           O  
-ATOM   7008  N   GLU B 483      19.264  11.672 -62.434  1.00 29.12           N  
-ATOM   7009  CA  GLU B 483      19.239  12.883 -63.248  1.00 25.61           C  
-ATOM   7010  C   GLU B 483      18.667  14.069 -62.490  1.00 29.32           C  
-ATOM   7011  O   GLU B 483      18.709  15.198 -62.972  1.00 27.56           O  
-ATOM   7012  CB  GLU B 483      18.427  12.652 -64.519  1.00 22.58           C  
-ATOM   7013  CG  GLU B 483      18.901  11.463 -65.322  1.00 34.09           C  
-ATOM   7014  CD  GLU B 483      17.938  11.092 -66.426  1.00 37.66           C  
-ATOM   7015  OE1 GLU B 483      18.036   9.957 -66.936  1.00 33.43           O  
-ATOM   7016  OE2 GLU B 483      17.087  11.935 -66.783  1.00 37.92           O  
-ATOM   7017  N   MET B 484      18.127  13.812 -61.304  1.00 35.31           N  
-ATOM   7018  CA  MET B 484      17.483  14.868 -60.531  1.00 32.74           C  
-ATOM   7019  C   MET B 484      18.394  15.424 -59.447  1.00 27.61           C  
-ATOM   7020  O   MET B 484      19.269  14.725 -58.936  1.00 30.29           O  
-ATOM   7021  CB  MET B 484      16.190  14.354 -59.903  1.00 28.83           C  
-ATOM   7022  CG  MET B 484      15.231  13.729 -60.895  1.00 35.33           C  
-ATOM   7023  SD  MET B 484      13.853  12.933 -60.055  1.00 34.39           S  
-ATOM   7024  CE  MET B 484      14.734  12.145 -58.721  1.00 32.46           C  
-ATOM   7025  N   ALA B 485      18.175  16.688 -59.102  1.00 26.94           N  
-ATOM   7026  CA  ALA B 485      18.934  17.341 -58.047  1.00 26.86           C  
-ATOM   7027  C   ALA B 485      18.717  16.619 -56.725  1.00 30.06           C  
-ATOM   7028  O   ALA B 485      19.669  16.275 -56.026  1.00 37.81           O  
-ATOM   7029  CB  ALA B 485      18.537  18.803 -57.933  1.00 26.05           C  
-ATOM   7030  N   LEU B 486      17.452  16.389 -56.395  1.00 30.45           N  
-ATOM   7031  CA  LEU B 486      17.089  15.642 -55.199  1.00 29.50           C  
-ATOM   7032  C   LEU B 486      15.965  14.653 -55.490  1.00 32.14           C  
-ATOM   7033  O   LEU B 486      14.938  15.027 -56.059  1.00 32.03           O  
-ATOM   7034  CB  LEU B 486      16.668  16.590 -54.073  1.00 28.17           C  
-ATOM   7035  CG  LEU B 486      17.739  16.939 -53.039  1.00 28.43           C  
-ATOM   7036  CD1 LEU B 486      17.137  17.723 -51.878  1.00 42.43           C  
-ATOM   7037  CD2 LEU B 486      18.421  15.678 -52.541  1.00 22.17           C  
-ATOM   7038  N   PRO B 487      16.165  13.381 -55.113  1.00 26.90           N  
-ATOM   7039  CA  PRO B 487      15.104  12.372 -55.166  1.00 24.61           C  
-ATOM   7040  C   PRO B 487      13.866  12.846 -54.417  1.00 24.83           C  
-ATOM   7041  O   PRO B 487      14.003  13.404 -53.330  1.00 31.05           O  
-ATOM   7042  CB  PRO B 487      15.740  11.163 -54.481  1.00 24.80           C  
-ATOM   7043  CG  PRO B 487      17.189  11.318 -54.746  1.00 25.48           C  
-ATOM   7044  CD  PRO B 487      17.456  12.797 -54.712  1.00 29.54           C  
-ATOM   7045  N   PRO B 488      12.672  12.629 -54.987  1.00 20.63           N  
-ATOM   7046  CA  PRO B 488      11.449  13.195 -54.408  1.00 30.07           C  
-ATOM   7047  C   PRO B 488      11.124  12.640 -53.023  1.00 27.33           C  
-ATOM   7048  O   PRO B 488      11.176  11.429 -52.808  1.00 25.90           O  
-ATOM   7049  CB  PRO B 488      10.369  12.799 -55.419  1.00 24.11           C  
-ATOM   7050  CG  PRO B 488      10.895  11.580 -56.066  1.00 22.73           C  
-ATOM   7051  CD  PRO B 488      12.383  11.759 -56.139  1.00 19.05           C  
-ATOM   7052  N   CYS B 489      10.801  13.529 -52.090  1.00 27.26           N  
-ATOM   7053  CA  CYS B 489      10.394  13.104 -50.760  1.00 32.18           C  
-ATOM   7054  C   CYS B 489       8.928  12.689 -50.801  1.00 34.44           C  
-ATOM   7055  O   CYS B 489       8.605  11.519 -50.596  1.00 29.59           O  
-ATOM   7056  CB  CYS B 489      10.633  14.213 -49.734  1.00 28.94           C  
-ATOM   7057  SG  CYS B 489      12.380  14.457 -49.318  1.00 56.95           S  
-ATOM   7058  N   HIS B 490       8.042  13.640 -51.079  1.00 30.26           N  
-ATOM   7059  CA  HIS B 490       6.652  13.296 -51.336  1.00 27.02           C  
-ATOM   7060  C   HIS B 490       6.556  12.699 -52.738  1.00 28.38           C  
-ATOM   7061  O   HIS B 490       6.512  13.423 -53.734  1.00 33.06           O  
-ATOM   7062  CB  HIS B 490       5.735  14.515 -51.172  1.00 30.49           C  
-ATOM   7063  CG  HIS B 490       6.277  15.781 -51.758  1.00 30.05           C  
-ATOM   7064  ND1 HIS B 490       5.775  16.343 -52.912  1.00 34.79           N  
-ATOM   7065  CD2 HIS B 490       7.262  16.611 -51.335  1.00 33.83           C  
-ATOM   7066  CE1 HIS B 490       6.430  17.459 -53.180  1.00 31.31           C  
-ATOM   7067  NE2 HIS B 490       7.341  17.641 -52.239  1.00 35.25           N  
-ATOM   7068  N   LEU B 491       6.532  11.371 -52.805  1.00 23.24           N  
-ATOM   7069  CA  LEU B 491       6.709  10.672 -54.072  1.00 26.15           C  
-ATOM   7070  C   LEU B 491       5.441  10.029 -54.627  1.00 20.05           C  
-ATOM   7071  O   LEU B 491       5.459   9.482 -55.730  1.00 20.20           O  
-ATOM   7072  CB  LEU B 491       7.798   9.603 -53.923  1.00 28.72           C  
-ATOM   7073  CG  LEU B 491       7.739   8.656 -52.719  1.00 20.64           C  
-ATOM   7074  CD1 LEU B 491       6.760   7.510 -52.935  1.00 24.50           C  
-ATOM   7075  CD2 LEU B 491       9.124   8.118 -52.410  1.00 16.04           C  
-ATOM   7076  N   LEU B 492       4.347  10.084 -53.875  1.00 26.61           N  
-ATOM   7077  CA  LEU B 492       3.123   9.418 -54.305  1.00 20.24           C  
-ATOM   7078  C   LEU B 492       1.872   9.969 -53.629  1.00 21.14           C  
-ATOM   7079  O   LEU B 492       1.870  10.246 -52.431  1.00 19.01           O  
-ATOM   7080  CB  LEU B 492       3.229   7.917 -54.040  1.00 16.06           C  
-ATOM   7081  CG  LEU B 492       2.140   7.044 -54.661  1.00 21.51           C  
-ATOM   7082  CD1 LEU B 492       2.777   5.877 -55.388  1.00 16.86           C  
-ATOM   7083  CD2 LEU B 492       1.163   6.555 -53.600  1.00 28.89           C  
-ATOM   7084  N   CYS B 493       0.804  10.127 -54.404  1.00 20.32           N  
-ATOM   7085  CA  CYS B 493      -0.481  10.492 -53.821  1.00 23.82           C  
-ATOM   7086  C   CYS B 493      -1.623   9.732 -54.484  1.00 25.49           C  
-ATOM   7087  O   CYS B 493      -1.575   9.442 -55.676  1.00 24.89           O  
-ATOM   7088  CB  CYS B 493      -0.719  12.000 -53.921  1.00 29.20           C  
-ATOM   7089  SG  CYS B 493      -0.966  12.623 -55.591  1.00 31.14           S  
-ATOM   7090  N   GLN B 494      -2.642   9.403 -53.695  1.00 23.83           N  
-ATOM   7091  CA  GLN B 494      -3.797   8.659 -54.190  1.00 23.18           C  
-ATOM   7092  C   GLN B 494      -5.088   9.317 -53.720  1.00 22.45           C  
-ATOM   7093  O   GLN B 494      -5.195   9.729 -52.565  1.00 18.58           O  
-ATOM   7094  CB  GLN B 494      -3.744   7.203 -53.724  1.00 23.32           C  
-ATOM   7095  CG  GLN B 494      -4.940   6.371 -54.157  1.00 25.72           C  
-ATOM   7096  CD  GLN B 494      -4.905   4.968 -53.594  1.00 26.67           C  
-ATOM   7097  OE1 GLN B 494      -3.954   4.584 -52.915  1.00 24.02           O  
-ATOM   7098  NE2 GLN B 494      -5.944   4.192 -53.872  1.00 27.76           N  
-ATOM   7099  N   PHE B 495      -6.066   9.416 -54.616  1.00 22.35           N  
-ATOM   7100  CA  PHE B 495      -7.313  10.104 -54.301  1.00 21.35           C  
-ATOM   7101  C   PHE B 495      -8.481   9.135 -54.146  1.00 19.91           C  
-ATOM   7102  O   PHE B 495      -8.460   8.028 -54.687  1.00 14.46           O  
-ATOM   7103  CB  PHE B 495      -7.620  11.149 -55.374  1.00 18.14           C  
-ATOM   7104  CG  PHE B 495      -6.639  12.285 -55.399  1.00 20.44           C  
-ATOM   7105  CD1 PHE B 495      -6.875  13.433 -54.663  1.00 17.52           C  
-ATOM   7106  CD2 PHE B 495      -5.475  12.200 -56.147  1.00 20.53           C  
-ATOM   7107  CE1 PHE B 495      -5.973  14.479 -54.678  1.00 20.00           C  
-ATOM   7108  CE2 PHE B 495      -4.570  13.242 -56.166  1.00 13.61           C  
-ATOM   7109  CZ  PHE B 495      -4.819  14.383 -55.431  1.00 18.18           C  
-ATOM   7110  N   TYR B 496      -9.497   9.565 -53.402  1.00 20.65           N  
-ATOM   7111  CA  TYR B 496     -10.601   8.692 -53.019  1.00 21.51           C  
-ATOM   7112  C   TYR B 496     -11.907   9.462 -52.871  1.00 21.74           C  
-ATOM   7113  O   TYR B 496     -11.957  10.494 -52.203  1.00 28.11           O  
-ATOM   7114  CB  TYR B 496     -10.256   7.976 -51.712  1.00 22.58           C  
-ATOM   7115  CG  TYR B 496     -11.367   7.155 -51.089  1.00 25.36           C  
-ATOM   7116  CD1 TYR B 496     -11.574   5.834 -51.462  1.00 22.08           C  
-ATOM   7117  CD2 TYR B 496     -12.185   7.691 -50.101  1.00 27.08           C  
-ATOM   7118  CE1 TYR B 496     -12.577   5.078 -50.886  1.00 25.03           C  
-ATOM   7119  CE2 TYR B 496     -13.189   6.942 -49.519  1.00 20.49           C  
-ATOM   7120  CZ  TYR B 496     -13.380   5.638 -49.915  1.00 19.11           C  
-ATOM   7121  OH  TYR B 496     -14.377   4.890 -49.336  1.00 20.73           O  
-ATOM   7122  N   VAL B 497     -12.965   8.960 -53.496  1.00 16.70           N  
-ATOM   7123  CA  VAL B 497     -14.277   9.581 -53.369  1.00 20.15           C  
-ATOM   7124  C   VAL B 497     -15.245   8.601 -52.727  1.00 20.34           C  
-ATOM   7125  O   VAL B 497     -15.166   7.396 -52.962  1.00 27.32           O  
-ATOM   7126  CB  VAL B 497     -14.841  10.036 -54.735  1.00 17.52           C  
-ATOM   7127  CG1 VAL B 497     -15.971  11.037 -54.543  1.00 12.79           C  
-ATOM   7128  CG2 VAL B 497     -13.749  10.645 -55.581  1.00 21.38           C  
-ATOM   7129  N   ASN B 498     -16.151   9.117 -51.904  1.00 17.82           N  
-ATOM   7130  CA  ASN B 498     -17.196   8.287 -51.326  1.00 20.67           C  
-ATOM   7131  C   ASN B 498     -18.540   8.573 -51.991  1.00 32.34           C  
-ATOM   7132  O   ASN B 498     -18.592   9.112 -53.097  1.00 32.57           O  
-ATOM   7133  CB  ASN B 498     -17.283   8.499 -49.813  1.00 21.23           C  
-ATOM   7134  CG  ASN B 498     -17.598   9.933 -49.440  1.00 18.76           C  
-ATOM   7135  OD1 ASN B 498     -17.519  10.834 -50.272  1.00 18.72           O  
-ATOM   7136  ND2 ASN B 498     -17.945  10.154 -48.178  1.00 18.59           N  
-ATOM   7137  N   ASP B 499     -19.626   8.213 -51.316  1.00 35.35           N  
-ATOM   7138  CA  ASP B 499     -20.961   8.385 -51.876  1.00 30.11           C  
-ATOM   7139  C   ASP B 499     -21.505   9.798 -51.668  1.00 32.41           C  
-ATOM   7140  O   ASP B 499     -22.584  10.131 -52.158  1.00 35.44           O  
-ATOM   7141  CB  ASP B 499     -21.917   7.356 -51.268  1.00 45.98           C  
-ATOM   7142  CG  ASP B 499     -21.741   7.210 -49.765  1.00 46.83           C  
-ATOM   7143  OD1 ASP B 499     -20.732   7.714 -49.227  1.00 32.05           O  
-ATOM   7144  OD2 ASP B 499     -22.606   6.577 -49.122  1.00 50.76           O  
-ATOM   7145  N   GLN B 500     -20.756  10.626 -50.948  1.00 32.48           N  
-ATOM   7146  CA  GLN B 500     -21.188  11.988 -50.655  1.00 29.50           C  
-ATOM   7147  C   GLN B 500     -20.406  13.011 -51.475  1.00 25.59           C  
-ATOM   7148  O   GLN B 500     -20.375  14.195 -51.130  1.00 26.08           O  
-ATOM   7149  CB  GLN B 500     -21.029  12.296 -49.165  1.00 33.16           C  
-ATOM   7150  CG  GLN B 500     -21.594  11.234 -48.238  1.00 30.39           C  
-ATOM   7151  CD  GLN B 500     -23.072  10.995 -48.458  1.00 46.28           C  
-ATOM   7152  OE1 GLN B 500     -23.492   9.876 -48.756  1.00 55.02           O  
-ATOM   7153  NE2 GLN B 500     -23.872  12.045 -48.306  1.00 45.55           N  
-ATOM   7154  N   LYS B 501     -19.780  12.544 -52.554  1.00 20.59           N  
-ATOM   7155  CA  LYS B 501     -18.938  13.381 -53.409  1.00 20.47           C  
-ATOM   7156  C   LYS B 501     -17.822  14.062 -52.618  1.00 27.05           C  
-ATOM   7157  O   LYS B 501     -17.404  15.172 -52.954  1.00 26.78           O  
-ATOM   7158  CB  LYS B 501     -19.777  14.437 -54.130  1.00 14.94           C  
-ATOM   7159  CG  LYS B 501     -20.905  13.873 -54.974  1.00 18.25           C  
-ATOM   7160  CD  LYS B 501     -20.659  14.112 -56.455  1.00 19.38           C  
-ATOM   7161  CE  LYS B 501     -21.848  13.655 -57.278  1.00 27.78           C  
-ATOM   7162  NZ  LYS B 501     -23.106  14.303 -56.813  1.00 33.27           N  
-ATOM   7163  N   GLU B 502     -17.345  13.393 -51.570  1.00 26.68           N  
-ATOM   7164  CA  GLU B 502     -16.276  13.929 -50.733  1.00 21.26           C  
-ATOM   7165  C   GLU B 502     -14.917  13.360 -51.129  1.00 23.10           C  
-ATOM   7166  O   GLU B 502     -14.713  12.145 -51.125  1.00 21.57           O  
-ATOM   7167  CB  GLU B 502     -16.550  13.642 -49.258  1.00 17.20           C  
-ATOM   7168  CG  GLU B 502     -17.717  14.416 -48.675  1.00 24.69           C  
-ATOM   7169  CD  GLU B 502     -17.994  14.045 -47.229  1.00 47.82           C  
-ATOM   7170  OE1 GLU B 502     -18.004  12.836 -46.911  1.00 46.12           O  
-ATOM   7171  OE2 GLU B 502     -18.199  14.964 -46.408  1.00 55.83           O  
-ATOM   7172  N   LEU B 503     -13.989  14.250 -51.465  1.00 20.62           N  
-ATOM   7173  CA  LEU B 503     -12.656  13.850 -51.896  1.00 17.97           C  
-ATOM   7174  C   LEU B 503     -11.681  13.758 -50.726  1.00 21.29           C  
-ATOM   7175  O   LEU B 503     -11.690  14.597 -49.825  1.00 19.53           O  
-ATOM   7176  CB  LEU B 503     -12.122  14.833 -52.939  1.00 20.16           C  
-ATOM   7177  CG  LEU B 503     -10.719  14.548 -53.479  1.00 22.72           C  
-ATOM   7178  CD1 LEU B 503     -10.727  13.337 -54.403  1.00 19.93           C  
-ATOM   7179  CD2 LEU B 503     -10.155  15.772 -54.185  1.00 20.71           C  
-ATOM   7180  N   SER B 504     -10.842  12.727 -50.750  1.00 23.93           N  
-ATOM   7181  CA  SER B 504      -9.790  12.552 -49.757  1.00 18.91           C  
-ATOM   7182  C   SER B 504      -8.490  12.182 -50.460  1.00 23.51           C  
-ATOM   7183  O   SER B 504      -8.508  11.566 -51.530  1.00 19.94           O  
-ATOM   7184  CB  SER B 504     -10.171  11.477 -48.736  1.00 18.04           C  
-ATOM   7185  OG  SER B 504     -11.398  11.785 -48.096  1.00 23.59           O  
-ATOM   7186  N   CYS B 505      -7.365  12.554 -49.858  1.00 22.65           N  
-ATOM   7187  CA  CYS B 505      -6.066  12.317 -50.475  1.00 18.08           C  
-ATOM   7188  C   CYS B 505      -5.050  11.722 -49.505  1.00 17.63           C  
-ATOM   7189  O   CYS B 505      -4.857  12.227 -48.400  1.00 19.36           O  
-ATOM   7190  CB  CYS B 505      -5.512  13.618 -51.060  1.00 18.11           C  
-ATOM   7191  SG  CYS B 505      -3.856  13.467 -51.776  1.00 36.71           S  
-ATOM   7192  N   ILE B 506      -4.411  10.639 -49.936  1.00 20.70           N  
-ATOM   7193  CA  ILE B 506      -3.274  10.060 -49.230  1.00 19.89           C  
-ATOM   7194  C   ILE B 506      -1.983  10.513 -49.899  1.00 21.29           C  
-ATOM   7195  O   ILE B 506      -1.891  10.528 -51.123  1.00 22.14           O  
-ATOM   7196  CB  ILE B 506      -3.329   8.514 -49.219  1.00 21.79           C  
-ATOM   7197  CG1 ILE B 506      -4.326   8.016 -48.177  1.00 20.15           C  
-ATOM   7198  CG2 ILE B 506      -1.960   7.918 -48.925  1.00 22.02           C  
-ATOM   7199  CD1 ILE B 506      -4.482   6.514 -48.167  1.00 20.49           C  
-ATOM   7200  N   MET B 507      -0.991  10.892 -49.103  1.00 20.64           N  
-ATOM   7201  CA  MET B 507       0.321  11.199 -49.650  1.00 20.25           C  
-ATOM   7202  C   MET B 507       1.404  10.442 -48.890  1.00 19.69           C  
-ATOM   7203  O   MET B 507       1.523  10.565 -47.671  1.00 19.59           O  
-ATOM   7204  CB  MET B 507       0.588  12.703 -49.608  1.00 17.42           C  
-ATOM   7205  CG  MET B 507       1.873  13.116 -50.306  1.00 19.47           C  
-ATOM   7206  SD  MET B 507       3.312  13.089 -49.223  1.00 23.53           S  
-ATOM   7207  CE  MET B 507       3.117  14.641 -48.352  1.00 20.52           C  
-ATOM   7208  N   TYR B 508       2.187   9.652 -49.616  1.00 23.27           N  
-ATOM   7209  CA  TYR B 508       3.290   8.922 -49.008  1.00 20.30           C  
-ATOM   7210  C   TYR B 508       4.590   9.702 -49.148  1.00 18.61           C  
-ATOM   7211  O   TYR B 508       4.906  10.221 -50.219  1.00 23.27           O  
-ATOM   7212  CB  TYR B 508       3.440   7.534 -49.633  1.00 20.17           C  
-ATOM   7213  CG  TYR B 508       4.532   6.705 -48.993  1.00 19.26           C  
-ATOM   7214  CD1 TYR B 508       4.295   5.991 -47.826  1.00 19.34           C  
-ATOM   7215  CD2 TYR B 508       5.802   6.643 -49.552  1.00 21.96           C  
-ATOM   7216  CE1 TYR B 508       5.292   5.235 -47.235  1.00 24.06           C  
-ATOM   7217  CE2 TYR B 508       6.805   5.890 -48.968  1.00 20.51           C  
-ATOM   7218  CZ  TYR B 508       6.544   5.189 -47.811  1.00 19.72           C  
-ATOM   7219  OH  TYR B 508       7.538   4.440 -47.225  1.00 21.40           O  
-ATOM   7220  N   GLN B 509       5.341   9.779 -48.057  1.00 16.94           N  
-ATOM   7221  CA  GLN B 509       6.591  10.524 -48.042  1.00 24.35           C  
-ATOM   7222  C   GLN B 509       7.723   9.654 -47.499  1.00 24.02           C  
-ATOM   7223  O   GLN B 509       7.650   9.155 -46.376  1.00 29.15           O  
-ATOM   7224  CB  GLN B 509       6.435  11.796 -47.209  1.00 20.77           C  
-ATOM   7225  CG  GLN B 509       7.522  12.832 -47.422  1.00 20.56           C  
-ATOM   7226  CD  GLN B 509       7.249  14.109 -46.655  1.00 24.87           C  
-ATOM   7227  OE1 GLN B 509       6.115  14.378 -46.264  1.00 19.57           O  
-ATOM   7228  NE2 GLN B 509       8.289  14.900 -46.428  1.00 33.60           N  
-ATOM   7229  N   ARG B 510       8.765   9.470 -48.303  1.00 17.21           N  
-ATOM   7230  CA  ARG B 510       9.865   8.583 -47.940  1.00 21.48           C  
-ATOM   7231  C   ARG B 510      10.740   9.157 -46.830  1.00 27.33           C  
-ATOM   7232  O   ARG B 510      11.355   8.411 -46.065  1.00 23.50           O  
-ATOM   7233  CB  ARG B 510      10.736   8.287 -49.162  1.00 19.40           C  
-ATOM   7234  CG  ARG B 510      11.400   9.517 -49.757  1.00 19.70           C  
-ATOM   7235  CD  ARG B 510      12.489   9.143 -50.741  1.00 21.92           C  
-ATOM   7236  NE  ARG B 510      13.143  10.319 -51.307  1.00 21.82           N  
-ATOM   7237  CZ  ARG B 510      14.135  10.978 -50.717  1.00 30.56           C  
-ATOM   7238  NH1 ARG B 510      14.674  12.036 -51.307  1.00 33.18           N  
-ATOM   7239  NH2 ARG B 510      14.589  10.580 -49.536  1.00 29.68           N  
-ATOM   7240  N   SER B 511      10.794  10.481 -46.748  1.00 25.40           N  
-ATOM   7241  CA  SER B 511      11.723  11.153 -45.852  1.00 21.81           C  
-ATOM   7242  C   SER B 511      11.134  12.467 -45.369  1.00 26.00           C  
-ATOM   7243  O   SER B 511      10.728  13.303 -46.174  1.00 35.07           O  
-ATOM   7244  CB  SER B 511      13.056  11.393 -46.559  1.00 26.19           C  
-ATOM   7245  OG  SER B 511      13.976  12.036 -45.703  1.00 35.13           O  
-ATOM   7246  N   CYS B 512      11.094  12.655 -44.054  1.00 26.15           N  
-ATOM   7247  CA  CYS B 512      10.375  13.790 -43.491  1.00 26.95           C  
-ATOM   7248  C   CYS B 512      11.179  14.598 -42.475  1.00 36.59           C  
-ATOM   7249  O   CYS B 512      11.390  14.157 -41.344  1.00 36.74           O  
-ATOM   7250  CB  CYS B 512       9.082  13.304 -42.836  1.00 29.05           C  
-ATOM   7251  SG  CYS B 512       8.101  12.190 -43.867  1.00 31.56           S  
-ATOM   7252  N   ASP B 513      11.614  15.788 -42.881  1.00 39.17           N  
-ATOM   7253  CA  ASP B 513      12.168  16.755 -41.944  1.00 26.12           C  
-ATOM   7254  C   ASP B 513      11.023  17.300 -41.100  1.00 25.62           C  
-ATOM   7255  O   ASP B 513      10.354  18.257 -41.490  1.00 29.65           O  
-ATOM   7256  CB  ASP B 513      12.891  17.887 -42.680  1.00 33.50           C  
-ATOM   7257  CG  ASP B 513      13.710  18.770 -41.749  1.00 39.62           C  
-ATOM   7258  OD1 ASP B 513      13.445  18.783 -40.528  1.00 42.51           O  
-ATOM   7259  OD2 ASP B 513      14.626  19.458 -42.246  1.00 43.61           O  
-ATOM   7260  N   VAL B 514      10.802  16.678 -39.947  1.00 22.08           N  
-ATOM   7261  CA  VAL B 514       9.680  17.019 -39.080  1.00 20.96           C  
-ATOM   7262  C   VAL B 514       9.685  18.484 -38.672  1.00 24.44           C  
-ATOM   7263  O   VAL B 514       8.640  19.133 -38.645  1.00 29.45           O  
-ATOM   7264  CB  VAL B 514       9.678  16.144 -37.819  1.00 23.27           C  
-ATOM   7265  CG1 VAL B 514       8.556  16.554 -36.874  1.00 23.41           C  
-ATOM   7266  CG2 VAL B 514       9.550  14.690 -38.208  1.00 23.97           C  
-ATOM   7267  N   GLY B 515      10.868  19.006 -38.371  1.00 31.35           N  
-ATOM   7268  CA  GLY B 515      10.992  20.379 -37.926  1.00 26.55           C  
-ATOM   7269  C   GLY B 515      10.663  21.396 -39.002  1.00 33.90           C  
-ATOM   7270  O   GLY B 515       9.987  22.390 -38.740  1.00 42.87           O  
-ATOM   7271  N   LEU B 516      11.125  21.140 -40.221  1.00 31.98           N  
-ATOM   7272  CA  LEU B 516      11.073  22.152 -41.268  1.00 38.32           C  
-ATOM   7273  C   LEU B 516      10.076  21.834 -42.380  1.00 38.12           C  
-ATOM   7274  O   LEU B 516       9.236  22.666 -42.722  1.00 51.09           O  
-ATOM   7275  CB  LEU B 516      12.470  22.344 -41.864  1.00 50.71           C  
-ATOM   7276  CG  LEU B 516      12.764  23.688 -42.531  1.00 56.71           C  
-ATOM   7277  CD1 LEU B 516      12.455  24.835 -41.583  1.00 50.82           C  
-ATOM   7278  CD2 LEU B 516      14.215  23.744 -42.980  1.00 50.68           C  
-ATOM   7279  N   GLY B 517      10.169  20.631 -42.938  1.00 34.34           N  
-ATOM   7280  CA  GLY B 517       9.431  20.289 -44.143  1.00 37.59           C  
-ATOM   7281  C   GLY B 517       7.997  19.811 -43.977  1.00 37.68           C  
-ATOM   7282  O   GLY B 517       7.149  20.099 -44.823  1.00 37.07           O  
-ATOM   7283  N   VAL B 518       7.726  19.081 -42.898  1.00 32.01           N  
-ATOM   7284  CA  VAL B 518       6.429  18.434 -42.697  1.00 25.20           C  
-ATOM   7285  C   VAL B 518       5.214  19.372 -42.708  1.00 25.04           C  
-ATOM   7286  O   VAL B 518       4.239  19.083 -43.408  1.00 30.02           O  
-ATOM   7287  CB  VAL B 518       6.428  17.619 -41.375  1.00 19.78           C  
-ATOM   7288  CG1 VAL B 518       5.007  17.281 -40.942  1.00 18.37           C  
-ATOM   7289  CG2 VAL B 518       7.249  16.368 -41.547  1.00 23.91           C  
-ATOM   7290  N   PRO B 519       5.253  20.486 -41.947  1.00 20.09           N  
-ATOM   7291  CA  PRO B 519       4.083  21.371 -41.998  1.00 23.29           C  
-ATOM   7292  C   PRO B 519       3.829  21.880 -43.411  1.00 25.28           C  
-ATOM   7293  O   PRO B 519       2.691  21.912 -43.895  1.00 26.44           O  
-ATOM   7294  CB  PRO B 519       4.473  22.527 -41.061  1.00 27.34           C  
-ATOM   7295  CG  PRO B 519       5.507  21.956 -40.166  1.00 21.05           C  
-ATOM   7296  CD  PRO B 519       6.280  21.013 -41.028  1.00 19.47           C  
-ATOM   7297  N   PHE B 520       4.923  22.271 -44.054  1.00 27.65           N  
-ATOM   7298  CA  PHE B 520       4.919  22.713 -45.435  1.00 26.24           C  
-ATOM   7299  C   PHE B 520       4.242  21.681 -46.330  1.00 26.64           C  
-ATOM   7300  O   PHE B 520       3.412  22.030 -47.163  1.00 23.20           O  
-ATOM   7301  CB  PHE B 520       6.347  22.970 -45.905  1.00 23.73           C  
-ATOM   7302  CG  PHE B 520       6.440  23.805 -47.148  1.00 26.10           C  
-ATOM   7303  CD1 PHE B 520       6.492  23.212 -48.397  1.00 21.29           C  
-ATOM   7304  CD2 PHE B 520       6.505  25.186 -47.063  1.00 29.98           C  
-ATOM   7305  CE1 PHE B 520       6.592  23.985 -49.535  1.00 26.36           C  
-ATOM   7306  CE2 PHE B 520       6.610  25.958 -48.195  1.00 20.66           C  
-ATOM   7307  CZ  PHE B 520       6.652  25.359 -49.432  1.00 22.24           C  
-ATOM   7308  N   ASN B 521       4.588  20.411 -46.143  1.00 27.00           N  
-ATOM   7309  CA  ASN B 521       4.020  19.339 -46.952  1.00 25.58           C  
-ATOM   7310  C   ASN B 521       2.526  19.144 -46.702  1.00 21.79           C  
-ATOM   7311  O   ASN B 521       1.741  18.998 -47.652  1.00 29.37           O  
-ATOM   7312  CB  ASN B 521       4.766  18.031 -46.695  1.00 28.72           C  
-ATOM   7313  CG  ASN B 521       6.177  18.042 -47.257  1.00 29.19           C  
-ATOM   7314  OD1 ASN B 521       7.148  17.852 -46.528  1.00 29.66           O  
-ATOM   7315  ND2 ASN B 521       6.295  18.271 -48.560  1.00 26.97           N  
-ATOM   7316  N   ILE B 522       2.144  19.137 -45.425  1.00 16.66           N  
-ATOM   7317  CA  ILE B 522       0.738  19.085 -45.034  1.00 15.95           C  
-ATOM   7318  C   ILE B 522      -0.049  20.153 -45.778  1.00 16.31           C  
-ATOM   7319  O   ILE B 522      -1.019  19.848 -46.483  1.00 15.97           O  
-ATOM   7320  CB  ILE B 522       0.562  19.277 -43.507  1.00 14.22           C  
-ATOM   7321  CG1 ILE B 522       1.269  18.157 -42.741  1.00 17.16           C  
-ATOM   7322  CG2 ILE B 522      -0.908  19.324 -43.137  1.00  9.26           C  
-ATOM   7323  CD1 ILE B 522       1.120  18.262 -41.245  1.00 14.30           C  
-ATOM   7324  N   ALA B 523       0.401  21.398 -45.642  1.00 19.13           N  
-ATOM   7325  CA  ALA B 523      -0.239  22.527 -46.311  1.00 17.72           C  
-ATOM   7326  C   ALA B 523      -0.305  22.322 -47.821  1.00 19.81           C  
-ATOM   7327  O   ALA B 523      -1.344  22.561 -48.450  1.00 26.84           O  
-ATOM   7328  CB  ALA B 523       0.496  23.821 -45.990  1.00 21.19           C  
-ATOM   7329  N   SER B 524       0.806  21.870 -48.390  1.00 15.55           N  
-ATOM   7330  CA  SER B 524       0.912  21.653 -49.825  1.00 16.48           C  
-ATOM   7331  C   SER B 524      -0.132  20.685 -50.367  1.00 18.93           C  
-ATOM   7332  O   SER B 524      -0.902  21.027 -51.267  1.00 21.62           O  
-ATOM   7333  CB  SER B 524       2.313  21.149 -50.174  1.00 17.21           C  
-ATOM   7334  OG  SER B 524       2.390  20.832 -51.547  1.00 30.49           O  
-ATOM   7335  N   TYR B 525      -0.158  19.472 -49.829  1.00 19.85           N  
-ATOM   7336  CA  TYR B 525      -1.055  18.462 -50.378  1.00 17.65           C  
-ATOM   7337  C   TYR B 525      -2.505  18.663 -49.943  1.00 19.89           C  
-ATOM   7338  O   TYR B 525      -3.426  18.242 -50.648  1.00 27.79           O  
-ATOM   7339  CB  TYR B 525      -0.565  17.060 -50.020  1.00 14.96           C  
-ATOM   7340  CG  TYR B 525       0.502  16.599 -50.991  1.00 18.04           C  
-ATOM   7341  CD1 TYR B 525       1.839  16.885 -50.767  1.00 14.85           C  
-ATOM   7342  CD2 TYR B 525       0.164  15.916 -52.151  1.00 24.91           C  
-ATOM   7343  CE1 TYR B 525       2.810  16.487 -51.655  1.00 14.74           C  
-ATOM   7344  CE2 TYR B 525       1.130  15.510 -53.049  1.00 24.43           C  
-ATOM   7345  CZ  TYR B 525       2.453  15.798 -52.797  1.00 17.88           C  
-ATOM   7346  OH  TYR B 525       3.423  15.395 -53.688  1.00 22.32           O  
-ATOM   7347  N   SER B 526      -2.723  19.317 -48.806  1.00 18.40           N  
-ATOM   7348  CA  SER B 526      -4.085  19.700 -48.447  1.00 19.43           C  
-ATOM   7349  C   SER B 526      -4.605  20.703 -49.476  1.00 22.14           C  
-ATOM   7350  O   SER B 526      -5.738  20.595 -49.958  1.00 27.31           O  
-ATOM   7351  CB  SER B 526      -4.140  20.290 -47.038  1.00 15.77           C  
-ATOM   7352  OG  SER B 526      -3.738  19.338 -46.069  1.00 13.76           O  
-ATOM   7353  N   LEU B 527      -3.759  21.674 -49.814  1.00 17.64           N  
-ATOM   7354  CA  LEU B 527      -4.092  22.657 -50.838  1.00 21.18           C  
-ATOM   7355  C   LEU B 527      -4.388  21.986 -52.175  1.00 22.91           C  
-ATOM   7356  O   LEU B 527      -5.387  22.306 -52.833  1.00 22.05           O  
-ATOM   7357  CB  LEU B 527      -2.954  23.666 -50.999  1.00 17.53           C  
-ATOM   7358  CG  LEU B 527      -3.205  24.846 -51.939  1.00 13.51           C  
-ATOM   7359  CD1 LEU B 527      -4.435  25.622 -51.505  1.00 15.29           C  
-ATOM   7360  CD2 LEU B 527      -1.990  25.756 -51.982  1.00 18.13           C  
-ATOM   7361  N   LEU B 528      -3.514  21.062 -52.577  1.00 19.23           N  
-ATOM   7362  CA  LEU B 528      -3.728  20.301 -53.808  1.00 17.46           C  
-ATOM   7363  C   LEU B 528      -5.085  19.614 -53.784  1.00 19.45           C  
-ATOM   7364  O   LEU B 528      -5.814  19.630 -54.781  1.00 21.58           O  
-ATOM   7365  CB  LEU B 528      -2.631  19.253 -54.021  1.00 20.54           C  
-ATOM   7366  CG  LEU B 528      -2.868  18.251 -55.163  1.00 16.22           C  
-ATOM   7367  CD1 LEU B 528      -2.846  18.942 -56.519  1.00 13.21           C  
-ATOM   7368  CD2 LEU B 528      -1.853  17.117 -55.125  1.00 20.65           C  
-ATOM   7369  N   THR B 529      -5.416  19.013 -52.642  1.00 14.32           N  
-ATOM   7370  CA  THR B 529      -6.711  18.362 -52.470  1.00 14.59           C  
-ATOM   7371  C   THR B 529      -7.855  19.346 -52.667  1.00 16.69           C  
-ATOM   7372  O   THR B 529      -8.826  19.036 -53.347  1.00 17.00           O  
-ATOM   7373  CB  THR B 529      -6.848  17.711 -51.084  1.00 14.95           C  
-ATOM   7374  OG1 THR B 529      -5.797  16.757 -50.904  1.00 19.15           O  
-ATOM   7375  CG2 THR B 529      -8.192  17.005 -50.960  1.00 12.83           C  
-ATOM   7376  N   LEU B 530      -7.732  20.530 -52.075  1.00 17.16           N  
-ATOM   7377  CA  LEU B 530      -8.732  21.579 -52.255  1.00 14.96           C  
-ATOM   7378  C   LEU B 530      -8.937  21.913 -53.731  1.00 18.90           C  
-ATOM   7379  O   LEU B 530     -10.074  21.964 -54.213  1.00 20.14           O  
-ATOM   7380  CB  LEU B 530      -8.330  22.842 -51.492  1.00 16.59           C  
-ATOM   7381  CG  LEU B 530      -9.072  23.131 -50.190  1.00 18.01           C  
-ATOM   7382  CD1 LEU B 530      -8.951  21.957 -49.239  1.00 17.29           C  
-ATOM   7383  CD2 LEU B 530      -8.544  24.405 -49.546  1.00 16.31           C  
-ATOM   7384  N   MET B 531      -7.833  22.131 -54.444  1.00 21.59           N  
-ATOM   7385  CA  MET B 531      -7.889  22.496 -55.859  1.00 18.35           C  
-ATOM   7386  C   MET B 531      -8.535  21.408 -56.724  1.00 18.57           C  
-ATOM   7387  O   MET B 531      -9.474  21.681 -57.494  1.00 17.62           O  
-ATOM   7388  CB  MET B 531      -6.480  22.811 -56.362  1.00 16.64           C  
-ATOM   7389  CG  MET B 531      -5.797  23.930 -55.580  1.00 18.99           C  
-ATOM   7390  SD  MET B 531      -4.031  24.102 -55.917  1.00 20.48           S  
-ATOM   7391  CE  MET B 531      -4.062  24.607 -57.628  1.00 15.06           C  
-ATOM   7392  N   VAL B 532      -8.033  20.182 -56.595  1.00 19.25           N  
-ATOM   7393  CA  VAL B 532      -8.594  19.046 -57.323  1.00 22.12           C  
-ATOM   7394  C   VAL B 532     -10.092  18.889 -57.035  1.00 24.08           C  
-ATOM   7395  O   VAL B 532     -10.909  18.728 -57.954  1.00 16.35           O  
-ATOM   7396  CB  VAL B 532      -7.860  17.735 -56.969  1.00 11.90           C  
-ATOM   7397  CG1 VAL B 532      -8.639  16.548 -57.465  1.00 14.57           C  
-ATOM   7398  CG2 VAL B 532      -6.461  17.735 -57.559  1.00 14.29           C  
-ATOM   7399  N   ALA B 533     -10.442  18.954 -55.752  1.00 22.15           N  
-ATOM   7400  CA  ALA B 533     -11.833  18.885 -55.323  1.00 17.89           C  
-ATOM   7401  C   ALA B 533     -12.659  19.961 -56.009  1.00 18.98           C  
-ATOM   7402  O   ALA B 533     -13.792  19.706 -56.418  1.00 25.61           O  
-ATOM   7403  CB  ALA B 533     -11.943  19.019 -53.811  1.00 18.44           C  
-ATOM   7404  N   HIS B 534     -12.102  21.161 -56.150  1.00 17.95           N  
-ATOM   7405  CA  HIS B 534     -12.850  22.211 -56.833  1.00 29.52           C  
-ATOM   7406  C   HIS B 534     -13.051  21.904 -58.311  1.00 25.52           C  
-ATOM   7407  O   HIS B 534     -14.172  22.004 -58.813  1.00 23.04           O  
-ATOM   7408  CB  HIS B 534     -12.177  23.573 -56.705  1.00 25.41           C  
-ATOM   7409  CG  HIS B 534     -12.873  24.644 -57.486  1.00 23.06           C  
-ATOM   7410  ND1 HIS B 534     -12.390  25.129 -58.683  1.00 22.22           N  
-ATOM   7411  CD2 HIS B 534     -14.043  25.289 -57.264  1.00 24.45           C  
-ATOM   7412  CE1 HIS B 534     -13.220  26.045 -59.151  1.00 25.63           C  
-ATOM   7413  NE2 HIS B 534     -14.231  26.160 -58.310  1.00 31.06           N  
-ATOM   7414  N   VAL B 535     -11.982  21.537 -59.017  1.00 26.29           N  
-ATOM   7415  CA  VAL B 535     -12.132  21.299 -60.454  1.00 21.39           C  
-ATOM   7416  C   VAL B 535     -12.891  20.003 -60.761  1.00 27.83           C  
-ATOM   7417  O   VAL B 535     -13.221  19.739 -61.918  1.00 28.27           O  
-ATOM   7418  CB  VAL B 535     -10.772  21.268 -61.190  1.00 18.19           C  
-ATOM   7419  CG1 VAL B 535     -10.153  22.656 -61.226  1.00 17.91           C  
-ATOM   7420  CG2 VAL B 535      -9.820  20.256 -60.561  1.00 16.12           C  
-ATOM   7421  N   CYS B 536     -13.185  19.201 -59.738  1.00 27.00           N  
-ATOM   7422  CA  CYS B 536     -13.948  17.971 -59.955  1.00 22.54           C  
-ATOM   7423  C   CYS B 536     -15.369  18.028 -59.390  1.00 23.09           C  
-ATOM   7424  O   CYS B 536     -16.067  17.013 -59.363  1.00 30.91           O  
-ATOM   7425  CB  CYS B 536     -13.208  16.778 -59.347  1.00 23.64           C  
-ATOM   7426  SG  CYS B 536     -11.654  16.347 -60.162  1.00 28.99           S  
-ATOM   7427  N   ASN B 537     -15.791  19.213 -58.953  1.00 27.75           N  
-ATOM   7428  CA  ASN B 537     -17.085  19.395 -58.292  1.00 31.84           C  
-ATOM   7429  C   ASN B 537     -17.233  18.513 -57.057  1.00 25.79           C  
-ATOM   7430  O   ASN B 537     -18.314  17.997 -56.776  1.00 24.82           O  
-ATOM   7431  CB  ASN B 537     -18.240  19.119 -59.261  1.00 30.10           C  
-ATOM   7432  CG  ASN B 537     -18.314  20.133 -60.381  1.00 49.16           C  
-ATOM   7433  OD1 ASN B 537     -17.746  19.932 -61.455  1.00 63.37           O  
-ATOM   7434  ND2 ASN B 537     -19.017  21.231 -60.136  1.00 40.49           N  
-ATOM   7435  N   LEU B 538     -16.138  18.344 -56.324  1.00 22.72           N  
-ATOM   7436  CA  LEU B 538     -16.144  17.532 -55.115  1.00 19.93           C  
-ATOM   7437  C   LEU B 538     -15.869  18.385 -53.886  1.00 19.55           C  
-ATOM   7438  O   LEU B 538     -15.278  19.461 -53.984  1.00 20.20           O  
-ATOM   7439  CB  LEU B 538     -15.112  16.409 -55.217  1.00 15.60           C  
-ATOM   7440  CG  LEU B 538     -15.230  15.527 -56.460  1.00 15.84           C  
-ATOM   7441  CD1 LEU B 538     -14.090  14.525 -56.521  1.00 16.45           C  
-ATOM   7442  CD2 LEU B 538     -16.574  14.820 -56.474  1.00 17.59           C  
-ATOM   7443  N   LYS B 539     -16.308  17.902 -52.730  1.00 18.59           N  
-ATOM   7444  CA  LYS B 539     -16.077  18.602 -51.474  1.00 22.22           C  
-ATOM   7445  C   LYS B 539     -14.877  18.002 -50.754  1.00 29.89           C  
-ATOM   7446  O   LYS B 539     -14.864  16.805 -50.460  1.00 32.70           O  
-ATOM   7447  CB  LYS B 539     -17.321  18.536 -50.586  1.00 23.17           C  
-ATOM   7448  CG  LYS B 539     -18.521  19.295 -51.137  1.00 25.67           C  
-ATOM   7449  CD  LYS B 539     -19.822  18.838 -50.489  1.00 20.54           C  
-ATOM   7450  CE  LYS B 539     -20.353  17.553 -51.118  1.00 23.03           C  
-ATOM   7451  NZ  LYS B 539     -21.479  16.985 -50.313  1.00 30.36           N  
-ATOM   7452  N   PRO B 540     -13.857  18.827 -50.478  1.00 18.18           N  
-ATOM   7453  CA  PRO B 540     -12.673  18.330 -49.775  1.00 15.63           C  
-ATOM   7454  C   PRO B 540     -13.046  17.805 -48.397  1.00 24.86           C  
-ATOM   7455  O   PRO B 540     -13.854  18.419 -47.702  1.00 31.04           O  
-ATOM   7456  CB  PRO B 540     -11.770  19.563 -49.685  1.00 17.89           C  
-ATOM   7457  CG  PRO B 540     -12.689  20.724 -49.821  1.00 17.96           C  
-ATOM   7458  CD  PRO B 540     -13.765  20.268 -50.760  1.00 24.83           C  
-ATOM   7459  N   LYS B 541     -12.472  16.669 -48.019  1.00 23.16           N  
-ATOM   7460  CA  LYS B 541     -12.843  16.013 -46.775  1.00 21.76           C  
-ATOM   7461  C   LYS B 541     -11.648  15.774 -45.863  1.00 22.43           C  
-ATOM   7462  O   LYS B 541     -11.690  16.103 -44.679  1.00 25.86           O  
-ATOM   7463  CB  LYS B 541     -13.537  14.681 -47.067  1.00 27.84           C  
-ATOM   7464  CG  LYS B 541     -13.899  13.882 -45.823  1.00 25.35           C  
-ATOM   7465  CD  LYS B 541     -14.413  12.497 -46.189  1.00 27.21           C  
-ATOM   7466  CE  LYS B 541     -14.626  11.641 -44.953  1.00 28.03           C  
-ATOM   7467  NZ  LYS B 541     -15.637  12.247 -44.047  1.00 38.86           N  
-ATOM   7468  N   GLU B 542     -10.580  15.210 -46.415  1.00 21.37           N  
-ATOM   7469  CA  GLU B 542      -9.487  14.731 -45.583  1.00 19.27           C  
-ATOM   7470  C   GLU B 542      -8.166  14.615 -46.338  1.00 19.52           C  
-ATOM   7471  O   GLU B 542      -8.136  14.226 -47.506  1.00 17.71           O  
-ATOM   7472  CB  GLU B 542      -9.865  13.372 -44.990  1.00 28.79           C  
-ATOM   7473  CG  GLU B 542      -9.090  12.963 -43.753  1.00 33.05           C  
-ATOM   7474  CD  GLU B 542      -9.678  11.727 -43.092  1.00 39.94           C  
-ATOM   7475  OE1 GLU B 542      -9.551  11.592 -41.856  1.00 32.49           O  
-ATOM   7476  OE2 GLU B 542     -10.273  10.896 -43.813  1.00 29.07           O  
-ATOM   7477  N   PHE B 543      -7.076  14.963 -45.663  1.00 19.99           N  
-ATOM   7478  CA  PHE B 543      -5.741  14.663 -46.165  1.00 16.57           C  
-ATOM   7479  C   PHE B 543      -5.061  13.650 -45.261  1.00 14.56           C  
-ATOM   7480  O   PHE B 543      -4.880  13.894 -44.070  1.00 16.98           O  
-ATOM   7481  CB  PHE B 543      -4.878  15.919 -46.261  1.00 15.76           C  
-ATOM   7482  CG  PHE B 543      -3.404  15.627 -46.346  1.00 14.71           C  
-ATOM   7483  CD1 PHE B 543      -2.883  14.943 -47.433  1.00 15.28           C  
-ATOM   7484  CD2 PHE B 543      -2.543  16.028 -45.338  1.00 13.10           C  
-ATOM   7485  CE1 PHE B 543      -1.530  14.666 -47.513  1.00 14.22           C  
-ATOM   7486  CE2 PHE B 543      -1.188  15.755 -45.414  1.00 12.15           C  
-ATOM   7487  CZ  PHE B 543      -0.682  15.073 -46.502  1.00 13.84           C  
-ATOM   7488  N   ILE B 544      -4.678  12.514 -45.828  1.00 12.42           N  
-ATOM   7489  CA  ILE B 544      -4.015  11.485 -45.046  1.00 15.31           C  
-ATOM   7490  C   ILE B 544      -2.524  11.451 -45.359  1.00 17.40           C  
-ATOM   7491  O   ILE B 544      -2.112  11.292 -46.507  1.00 16.86           O  
-ATOM   7492  CB  ILE B 544      -4.642  10.109 -45.294  1.00 18.61           C  
-ATOM   7493  CG1 ILE B 544      -6.156  10.192 -45.095  1.00 20.32           C  
-ATOM   7494  CG2 ILE B 544      -4.029   9.068 -44.369  1.00 13.90           C  
-ATOM   7495  CD1 ILE B 544      -6.885   8.908 -45.387  1.00 21.82           C  
-ATOM   7496  N   HIS B 545      -1.723  11.607 -44.313  1.00 13.48           N  
-ATOM   7497  CA  HIS B 545      -0.282  11.747 -44.439  1.00 14.90           C  
-ATOM   7498  C   HIS B 545       0.459  10.493 -43.977  1.00 19.36           C  
-ATOM   7499  O   HIS B 545       0.506  10.188 -42.776  1.00 23.49           O  
-ATOM   7500  CB  HIS B 545       0.186  12.961 -43.636  1.00 20.37           C  
-ATOM   7501  CG  HIS B 545       1.538  13.464 -44.027  1.00 20.39           C  
-ATOM   7502  ND1 HIS B 545       2.310  12.855 -44.996  1.00 17.69           N  
-ATOM   7503  CD2 HIS B 545       2.259  14.519 -43.584  1.00 18.27           C  
-ATOM   7504  CE1 HIS B 545       3.445  13.512 -45.127  1.00 15.99           C  
-ATOM   7505  NE2 HIS B 545       3.441  14.529 -44.283  1.00 18.55           N  
-ATOM   7506  N   PHE B 546       1.033   9.777 -44.941  1.00 14.27           N  
-ATOM   7507  CA  PHE B 546       1.836   8.589 -44.667  1.00 16.17           C  
-ATOM   7508  C   PHE B 546       3.326   8.904 -44.761  1.00 17.87           C  
-ATOM   7509  O   PHE B 546       3.792   9.454 -45.758  1.00 18.49           O  
-ATOM   7510  CB  PHE B 546       1.476   7.462 -45.634  1.00 18.84           C  
-ATOM   7511  CG  PHE B 546       0.197   6.755 -45.291  1.00 26.82           C  
-ATOM   7512  CD1 PHE B 546      -0.436   6.986 -44.078  1.00 23.32           C  
-ATOM   7513  CD2 PHE B 546      -0.366   5.847 -46.174  1.00 22.42           C  
-ATOM   7514  CE1 PHE B 546      -1.609   6.332 -43.758  1.00 15.84           C  
-ATOM   7515  CE2 PHE B 546      -1.539   5.190 -45.858  1.00 17.73           C  
-ATOM   7516  CZ  PHE B 546      -2.160   5.432 -44.648  1.00 18.48           C  
-ATOM   7517  N   MET B 547       4.071   8.549 -43.719  1.00 19.09           N  
-ATOM   7518  CA  MET B 547       5.474   8.939 -43.612  1.00 15.26           C  
-ATOM   7519  C   MET B 547       6.385   7.740 -43.376  1.00 20.32           C  
-ATOM   7520  O   MET B 547       6.117   6.910 -42.509  1.00 24.50           O  
-ATOM   7521  CB  MET B 547       5.646   9.952 -42.482  1.00 15.94           C  
-ATOM   7522  CG  MET B 547       4.482  10.926 -42.365  1.00 28.00           C  
-ATOM   7523  SD  MET B 547       4.517  11.977 -40.904  1.00 27.58           S  
-ATOM   7524  CE  MET B 547       5.811  13.122 -41.344  1.00 17.40           C  
-ATOM   7525  N   GLY B 548       7.463   7.653 -44.147  1.00 21.64           N  
-ATOM   7526  CA  GLY B 548       8.431   6.581 -43.989  1.00 21.71           C  
-ATOM   7527  C   GLY B 548       9.489   6.921 -42.956  1.00 22.95           C  
-ATOM   7528  O   GLY B 548       9.256   6.797 -41.753  1.00 19.99           O  
-ATOM   7529  N   ASN B 549      10.660   7.345 -43.423  1.00 21.76           N  
-ATOM   7530  CA  ASN B 549      11.712   7.801 -42.520  1.00 23.09           C  
-ATOM   7531  C   ASN B 549      11.342   9.156 -41.927  1.00 23.32           C  
-ATOM   7532  O   ASN B 549      11.502  10.193 -42.570  1.00 28.42           O  
-ATOM   7533  CB  ASN B 549      13.059   7.882 -43.248  1.00 27.34           C  
-ATOM   7534  CG  ASN B 549      14.239   7.997 -42.292  1.00 24.85           C  
-ATOM   7535  OD1 ASN B 549      14.308   8.911 -41.470  1.00 26.94           O  
-ATOM   7536  ND2 ASN B 549      15.171   7.057 -42.393  1.00 18.64           N  
-ATOM   7537  N   THR B 550      10.834   9.139 -40.700  1.00 17.70           N  
-ATOM   7538  CA  THR B 550      10.397  10.358 -40.034  1.00 23.68           C  
-ATOM   7539  C   THR B 550      11.440  10.782 -39.009  1.00 28.99           C  
-ATOM   7540  O   THR B 550      11.630  10.110 -37.996  1.00 33.98           O  
-ATOM   7541  CB  THR B 550       9.033  10.165 -39.344  1.00 25.65           C  
-ATOM   7542  OG1 THR B 550       8.207   9.312 -40.146  1.00 27.65           O  
-ATOM   7543  CG2 THR B 550       8.337  11.499 -39.147  1.00 25.45           C  
-ATOM   7544  N   HIS B 551      12.114  11.899 -39.269  1.00 23.87           N  
-ATOM   7545  CA  HIS B 551      13.279  12.273 -38.473  1.00 24.85           C  
-ATOM   7546  C   HIS B 551      13.303  13.735 -38.049  1.00 24.30           C  
-ATOM   7547  O   HIS B 551      12.785  14.607 -38.744  1.00 30.58           O  
-ATOM   7548  CB  HIS B 551      14.557  11.961 -39.252  1.00 34.66           C  
-ATOM   7549  CG  HIS B 551      14.594  12.577 -40.615  1.00 30.50           C  
-ATOM   7550  ND1 HIS B 551      14.256  11.879 -41.754  1.00 27.22           N  
-ATOM   7551  CD2 HIS B 551      14.918  13.828 -41.023  1.00 29.67           C  
-ATOM   7552  CE1 HIS B 551      14.374  12.671 -42.805  1.00 28.62           C  
-ATOM   7553  NE2 HIS B 551      14.775  13.859 -42.388  1.00 28.75           N  
-ATOM   7554  N   VAL B 552      13.925  13.984 -36.901  1.00 28.23           N  
-ATOM   7555  CA  VAL B 552      14.166  15.333 -36.407  1.00 22.05           C  
-ATOM   7556  C   VAL B 552      15.669  15.597 -36.351  1.00 30.18           C  
-ATOM   7557  O   VAL B 552      16.409  14.852 -35.705  1.00 30.23           O  
-ATOM   7558  CB  VAL B 552      13.554  15.542 -35.009  1.00 13.31           C  
-ATOM   7559  CG1 VAL B 552      14.159  16.760 -34.336  1.00 20.73           C  
-ATOM   7560  CG2 VAL B 552      12.045  15.669 -35.103  1.00 18.65           C  
-ATOM   7561  N   TYR B 553      16.121  16.647 -37.032  1.00 31.47           N  
-ATOM   7562  CA  TYR B 553      17.543  16.981 -37.042  1.00 32.03           C  
-ATOM   7563  C   TYR B 553      17.995  17.468 -35.670  1.00 33.11           C  
-ATOM   7564  O   TYR B 553      17.299  18.243 -35.011  1.00 29.35           O  
-ATOM   7565  CB  TYR B 553      17.850  18.025 -38.120  1.00 26.42           C  
-ATOM   7566  CG  TYR B 553      17.878  17.434 -39.511  1.00 32.76           C  
-ATOM   7567  CD1 TYR B 553      19.008  16.781 -39.983  1.00 35.40           C  
-ATOM   7568  CD2 TYR B 553      16.770  17.509 -40.344  1.00 35.36           C  
-ATOM   7569  CE1 TYR B 553      19.037  16.226 -41.250  1.00 35.38           C  
-ATOM   7570  CE2 TYR B 553      16.790  16.957 -41.614  1.00 33.84           C  
-ATOM   7571  CZ  TYR B 553      17.926  16.315 -42.060  1.00 31.59           C  
-ATOM   7572  OH  TYR B 553      17.955  15.763 -43.320  1.00 28.95           O  
-ATOM   7573  N   THR B 554      19.163  16.993 -35.247  1.00 32.43           N  
-ATOM   7574  CA  THR B 554      19.698  17.279 -33.919  1.00 34.10           C  
-ATOM   7575  C   THR B 554      19.825  18.773 -33.620  1.00 33.94           C  
-ATOM   7576  O   THR B 554      19.739  19.187 -32.465  1.00 27.10           O  
-ATOM   7577  CB  THR B 554      21.078  16.618 -33.732  1.00 35.00           C  
-ATOM   7578  OG1 THR B 554      21.838  16.755 -34.939  1.00 38.07           O  
-ATOM   7579  CG2 THR B 554      20.921  15.140 -33.412  1.00 31.97           C  
-ATOM   7580  N   ASN B 555      20.024  19.579 -34.658  1.00 33.72           N  
-ATOM   7581  CA  ASN B 555      20.153  21.019 -34.478  1.00 25.32           C  
-ATOM   7582  C   ASN B 555      18.805  21.733 -34.573  1.00 32.85           C  
-ATOM   7583  O   ASN B 555      18.747  22.946 -34.775  1.00 42.99           O  
-ATOM   7584  CB  ASN B 555      21.136  21.599 -35.500  1.00 29.10           C  
-ATOM   7585  CG  ASN B 555      20.670  21.415 -36.934  1.00 31.52           C  
-ATOM   7586  OD1 ASN B 555      19.923  20.490 -37.245  1.00 42.08           O  
-ATOM   7587  ND2 ASN B 555      21.121  22.296 -37.817  1.00 30.29           N  
-ATOM   7588  N   HIS B 556      17.725  20.971 -34.426  1.00 33.82           N  
-ATOM   7589  CA  HIS B 556      16.379  21.533 -34.416  1.00 39.97           C  
-ATOM   7590  C   HIS B 556      15.706  21.280 -33.076  1.00 37.81           C  
-ATOM   7591  O   HIS B 556      14.698  21.905 -32.747  1.00 36.59           O  
-ATOM   7592  CB  HIS B 556      15.526  20.933 -35.535  1.00 35.18           C  
-ATOM   7593  CG  HIS B 556      15.948  21.346 -36.910  1.00 30.54           C  
-ATOM   7594  ND1 HIS B 556      15.247  20.982 -38.039  1.00 37.20           N  
-ATOM   7595  CD2 HIS B 556      16.994  22.089 -37.339  1.00 33.94           C  
-ATOM   7596  CE1 HIS B 556      15.844  21.483 -39.105  1.00 45.83           C  
-ATOM   7597  NE2 HIS B 556      16.907  22.159 -38.708  1.00 47.80           N  
-ATOM   7598  N   VAL B 557      16.281  20.354 -32.315  1.00 28.76           N  
-ATOM   7599  CA  VAL B 557      15.663  19.813 -31.109  1.00 29.67           C  
-ATOM   7600  C   VAL B 557      15.217  20.865 -30.099  1.00 37.76           C  
-ATOM   7601  O   VAL B 557      14.089  20.817 -29.603  1.00 33.95           O  
-ATOM   7602  CB  VAL B 557      16.622  18.840 -30.401  1.00 35.51           C  
-ATOM   7603  CG1 VAL B 557      16.059  18.426 -29.052  1.00 24.41           C  
-ATOM   7604  CG2 VAL B 557      16.881  17.623 -31.279  1.00 38.29           C  
-ATOM   7605  N   GLU B 558      16.103  21.808 -29.798  1.00 47.87           N  
-ATOM   7606  CA  GLU B 558      15.810  22.832 -28.806  1.00 42.26           C  
-ATOM   7607  C   GLU B 558      14.674  23.737 -29.276  1.00 43.81           C  
-ATOM   7608  O   GLU B 558      13.742  24.013 -28.520  1.00 47.56           O  
-ATOM   7609  CB  GLU B 558      17.069  23.649 -28.496  1.00 40.46           C  
-ATOM   7610  CG  GLU B 558      17.094  24.216 -27.093  1.00 60.45           C  
-ATOM   7611  CD  GLU B 558      17.216  23.133 -26.029  1.00 66.14           C  
-ATOM   7612  OE1 GLU B 558      17.628  22.003 -26.371  1.00 48.95           O  
-ATOM   7613  OE2 GLU B 558      16.908  23.407 -24.848  1.00 75.02           O  
-ATOM   7614  N   ALA B 559      14.750  24.176 -30.529  1.00 39.01           N  
-ATOM   7615  CA  ALA B 559      13.723  25.030 -31.112  1.00 31.87           C  
-ATOM   7616  C   ALA B 559      12.372  24.324 -31.101  1.00 33.58           C  
-ATOM   7617  O   ALA B 559      11.340  24.937 -30.825  1.00 32.06           O  
-ATOM   7618  CB  ALA B 559      14.104  25.428 -32.526  1.00 23.75           C  
-ATOM   7619  N   LEU B 560      12.390  23.029 -31.395  1.00 36.85           N  
-ATOM   7620  CA  LEU B 560      11.177  22.227 -31.376  1.00 28.52           C  
-ATOM   7621  C   LEU B 560      10.630  22.108 -29.966  1.00 31.39           C  
-ATOM   7622  O   LEU B 560       9.419  22.090 -29.765  1.00 36.93           O  
-ATOM   7623  CB  LEU B 560      11.440  20.839 -31.953  1.00 23.01           C  
-ATOM   7624  CG  LEU B 560      11.617  20.801 -33.467  1.00 20.17           C  
-ATOM   7625  CD1 LEU B 560      11.774  19.381 -33.960  1.00 22.28           C  
-ATOM   7626  CD2 LEU B 560      10.434  21.467 -34.129  1.00 26.10           C  
-ATOM   7627  N   LYS B 561      11.529  22.016 -28.993  1.00 31.71           N  
-ATOM   7628  CA  LYS B 561      11.126  21.926 -27.598  1.00 32.34           C  
-ATOM   7629  C   LYS B 561      10.525  23.248 -27.155  1.00 35.87           C  
-ATOM   7630  O   LYS B 561       9.708  23.297 -26.237  1.00 32.24           O  
-ATOM   7631  CB  LYS B 561      12.314  21.537 -26.718  1.00 36.60           C  
-ATOM   7632  CG  LYS B 561      12.622  20.050 -26.762  1.00 39.32           C  
-ATOM   7633  CD  LYS B 561      14.049  19.728 -26.343  1.00 46.72           C  
-ATOM   7634  CE  LYS B 561      14.309  20.061 -24.883  1.00 60.42           C  
-ATOM   7635  NZ  LYS B 561      15.710  19.725 -24.498  1.00 48.50           N  
-ATOM   7636  N   GLU B 562      10.937  24.320 -27.820  1.00 36.14           N  
-ATOM   7637  CA  GLU B 562      10.317  25.615 -27.612  1.00 34.94           C  
-ATOM   7638  C   GLU B 562       8.920  25.603 -28.217  1.00 32.16           C  
-ATOM   7639  O   GLU B 562       7.969  26.087 -27.609  1.00 30.58           O  
-ATOM   7640  CB  GLU B 562      11.163  26.734 -28.229  1.00 36.56           C  
-ATOM   7641  CG  GLU B 562      12.272  27.278 -27.334  1.00 51.79           C  
-ATOM   7642  CD  GLU B 562      11.786  28.337 -26.354  1.00 60.48           C  
-ATOM   7643  OE1 GLU B 562      10.740  28.124 -25.702  1.00 49.56           O  
-ATOM   7644  OE2 GLU B 562      12.452  29.390 -26.241  1.00 59.13           O  
-ATOM   7645  N   GLN B 563       8.806  25.034 -29.414  1.00 37.32           N  
-ATOM   7646  CA  GLN B 563       7.539  24.989 -30.136  1.00 26.49           C  
-ATOM   7647  C   GLN B 563       6.496  24.163 -29.389  1.00 26.21           C  
-ATOM   7648  O   GLN B 563       5.304  24.458 -29.440  1.00 34.09           O  
-ATOM   7649  CB  GLN B 563       7.748  24.423 -31.547  1.00 21.51           C  
-ATOM   7650  CG  GLN B 563       6.526  24.548 -32.460  1.00 24.60           C  
-ATOM   7651  CD  GLN B 563       6.790  24.077 -33.886  1.00 29.38           C  
-ATOM   7652  OE1 GLN B 563       7.925  23.773 -34.256  1.00 27.03           O  
-ATOM   7653  NE2 GLN B 563       5.736  24.017 -34.692  1.00 17.74           N  
-ATOM   7654  N   LEU B 564       6.956  23.137 -28.682  1.00 24.22           N  
-ATOM   7655  CA  LEU B 564       6.061  22.194 -28.022  1.00 23.18           C  
-ATOM   7656  C   LEU B 564       5.445  22.784 -26.762  1.00 25.94           C  
-ATOM   7657  O   LEU B 564       4.564  22.177 -26.156  1.00 35.70           O  
-ATOM   7658  CB  LEU B 564       6.801  20.898 -27.676  1.00 32.73           C  
-ATOM   7659  CG  LEU B 564       7.059  19.840 -28.759  1.00 27.61           C  
-ATOM   7660  CD1 LEU B 564       6.253  18.588 -28.469  1.00 24.16           C  
-ATOM   7661  CD2 LEU B 564       6.755  20.347 -30.161  1.00 29.61           C  
-ATOM   7662  N   ARG B 565       5.917  23.962 -26.364  1.00 26.85           N  
-ATOM   7663  CA  ARG B 565       5.344  24.661 -25.218  1.00 32.71           C  
-ATOM   7664  C   ARG B 565       4.203  25.569 -25.660  1.00 29.81           C  
-ATOM   7665  O   ARG B 565       3.552  26.222 -24.840  1.00 24.41           O  
-ATOM   7666  CB  ARG B 565       6.409  25.478 -24.489  1.00 29.57           C  
-ATOM   7667  CG  ARG B 565       7.390  24.645 -23.688  1.00 36.39           C  
-ATOM   7668  CD  ARG B 565       8.293  25.531 -22.849  1.00 34.00           C  
-ATOM   7669  NE  ARG B 565       9.385  24.776 -22.241  1.00 59.72           N  
-ATOM   7670  CZ  ARG B 565      10.564  24.575 -22.820  1.00 64.16           C  
-ATOM   7671  NH1 ARG B 565      10.804  25.073 -24.026  1.00 49.94           N  
-ATOM   7672  NH2 ARG B 565      11.504  23.877 -22.196  1.00 57.74           N  
-ATOM   7673  N   ARG B 566       3.967  25.599 -26.967  1.00 28.29           N  
-ATOM   7674  CA  ARG B 566       2.947  26.460 -27.545  1.00 25.73           C  
-ATOM   7675  C   ARG B 566       1.648  25.703 -27.785  1.00 21.05           C  
-ATOM   7676  O   ARG B 566       1.631  24.681 -28.467  1.00 22.01           O  
-ATOM   7677  CB  ARG B 566       3.448  27.073 -28.856  1.00 22.13           C  
-ATOM   7678  CG  ARG B 566       4.709  27.915 -28.719  1.00 23.91           C  
-ATOM   7679  CD  ARG B 566       5.134  28.492 -30.059  1.00 30.59           C  
-ATOM   7680  NE  ARG B 566       6.273  29.400 -29.944  1.00 35.25           N  
-ATOM   7681  CZ  ARG B 566       6.795  30.072 -30.966  1.00 40.29           C  
-ATOM   7682  NH1 ARG B 566       7.830  30.880 -30.776  1.00 41.58           N  
-ATOM   7683  NH2 ARG B 566       6.283  29.936 -32.181  1.00 36.59           N  
-ATOM   7684  N   GLU B 567       0.564  26.213 -27.213  1.00 20.99           N  
-ATOM   7685  CA  GLU B 567      -0.761  25.667 -27.468  1.00 21.59           C  
-ATOM   7686  C   GLU B 567      -1.284  26.164 -28.809  1.00 19.57           C  
-ATOM   7687  O   GLU B 567      -1.231  27.358 -29.101  1.00 20.27           O  
-ATOM   7688  CB  GLU B 567      -1.732  26.042 -26.348  1.00 21.62           C  
-ATOM   7689  CG  GLU B 567      -1.415  27.362 -25.679  1.00 30.36           C  
-ATOM   7690  CD  GLU B 567      -0.557  27.187 -24.445  1.00 35.24           C  
-ATOM   7691  OE1 GLU B 567       0.466  27.894 -24.320  1.00 34.14           O  
-ATOM   7692  OE2 GLU B 567      -0.912  26.340 -23.598  1.00 30.79           O  
-ATOM   7693  N   PRO B 568      -1.796  25.240 -29.630  1.00 17.89           N  
-ATOM   7694  CA  PRO B 568      -2.264  25.539 -30.985  1.00 18.30           C  
-ATOM   7695  C   PRO B 568      -3.430  26.518 -31.007  1.00 24.20           C  
-ATOM   7696  O   PRO B 568      -4.229  26.560 -30.069  1.00 25.47           O  
-ATOM   7697  CB  PRO B 568      -2.706  24.171 -31.515  1.00 19.99           C  
-ATOM   7698  CG  PRO B 568      -2.013  23.175 -30.646  1.00 23.27           C  
-ATOM   7699  CD  PRO B 568      -1.942  23.814 -29.302  1.00 20.33           C  
-ATOM   7700  N   ARG B 569      -3.514  27.298 -32.079  1.00 31.63           N  
-ATOM   7701  CA  ARG B 569      -4.623  28.221 -32.290  1.00 27.57           C  
-ATOM   7702  C   ARG B 569      -5.577  27.640 -33.340  1.00 25.11           C  
-ATOM   7703  O   ARG B 569      -5.224  26.678 -34.024  1.00 28.24           O  
-ATOM   7704  CB  ARG B 569      -4.094  29.592 -32.720  1.00 22.70           C  
-ATOM   7705  CG  ARG B 569      -3.062  30.176 -31.767  1.00 30.10           C  
-ATOM   7706  CD  ARG B 569      -3.441  31.578 -31.309  1.00 29.43           C  
-ATOM   7707  NE  ARG B 569      -2.474  32.112 -30.355  1.00 27.09           N  
-ATOM   7708  CZ  ARG B 569      -1.351  32.733 -30.699  1.00 25.02           C  
-ATOM   7709  NH1 ARG B 569      -0.527  33.184 -29.765  1.00 28.20           N  
-ATOM   7710  NH2 ARG B 569      -1.051  32.901 -31.980  1.00 26.43           N  
-ATOM   7711  N   PRO B 570      -6.795  28.198 -33.455  1.00 17.98           N  
-ATOM   7712  CA  PRO B 570      -7.727  27.745 -34.492  1.00 17.57           C  
-ATOM   7713  C   PRO B 570      -7.118  27.700 -35.891  1.00 16.63           C  
-ATOM   7714  O   PRO B 570      -6.435  28.638 -36.299  1.00 18.93           O  
-ATOM   7715  CB  PRO B 570      -8.838  28.792 -34.433  1.00 16.78           C  
-ATOM   7716  CG  PRO B 570      -8.856  29.219 -33.023  1.00 20.80           C  
-ATOM   7717  CD  PRO B 570      -7.439  29.141 -32.522  1.00 20.86           C  
-ATOM   7718  N   PHE B 571      -7.352  26.604 -36.604  1.00 16.91           N  
-ATOM   7719  CA  PHE B 571      -6.977  26.514 -38.006  1.00 15.54           C  
-ATOM   7720  C   PHE B 571      -7.725  27.576 -38.800  1.00 17.87           C  
-ATOM   7721  O   PHE B 571      -8.886  27.867 -38.515  1.00 15.64           O  
-ATOM   7722  CB  PHE B 571      -7.286  25.125 -38.568  1.00 18.85           C  
-ATOM   7723  CG  PHE B 571      -6.221  24.103 -38.293  1.00 16.65           C  
-ATOM   7724  CD1 PHE B 571      -4.893  24.476 -38.173  1.00 19.07           C  
-ATOM   7725  CD2 PHE B 571      -6.549  22.765 -38.161  1.00 20.97           C  
-ATOM   7726  CE1 PHE B 571      -3.913  23.532 -37.924  1.00 19.16           C  
-ATOM   7727  CE2 PHE B 571      -5.576  21.818 -37.912  1.00 22.82           C  
-ATOM   7728  CZ  PHE B 571      -4.256  22.201 -37.794  1.00 20.33           C  
-ATOM   7729  N   PRO B 572      -7.056  28.173 -39.795  1.00 23.88           N  
-ATOM   7730  CA  PRO B 572      -7.723  29.115 -40.700  1.00 23.95           C  
-ATOM   7731  C   PRO B 572      -8.541  28.365 -41.744  1.00 19.82           C  
-ATOM   7732  O   PRO B 572      -8.422  27.144 -41.833  1.00 22.80           O  
-ATOM   7733  CB  PRO B 572      -6.555  29.857 -41.351  1.00 18.95           C  
-ATOM   7734  CG  PRO B 572      -5.464  28.840 -41.376  1.00 21.51           C  
-ATOM   7735  CD  PRO B 572      -5.622  28.033 -40.107  1.00 16.68           C  
-ATOM   7736  N   ILE B 573      -9.368  29.063 -42.514  1.00 19.79           N  
-ATOM   7737  CA  ILE B 573      -9.977  28.423 -43.674  1.00 20.01           C  
-ATOM   7738  C   ILE B 573      -9.354  29.034 -44.920  1.00 19.85           C  
-ATOM   7739  O   ILE B 573      -9.081  30.232 -44.969  1.00 18.42           O  
-ATOM   7740  CB  ILE B 573     -11.531  28.557 -43.706  1.00 14.00           C  
-ATOM   7741  CG1 ILE B 573     -11.982  29.820 -44.437  1.00 19.00           C  
-ATOM   7742  CG2 ILE B 573     -12.119  28.494 -42.308  1.00 13.89           C  
-ATOM   7743  CD1 ILE B 573     -13.480  29.907 -44.624  1.00 42.38           C  
-ATOM   7744  N   VAL B 574      -9.086  28.195 -45.912  1.00 17.59           N  
-ATOM   7745  CA  VAL B 574      -8.529  28.671 -47.170  1.00 14.48           C  
-ATOM   7746  C   VAL B 574      -9.625  28.738 -48.221  1.00 11.58           C  
-ATOM   7747  O   VAL B 574     -10.222  27.721 -48.574  1.00 11.46           O  
-ATOM   7748  CB  VAL B 574      -7.383  27.768 -47.668  1.00 14.87           C  
-ATOM   7749  CG1 VAL B 574      -7.041  28.082 -49.115  1.00 18.73           C  
-ATOM   7750  CG2 VAL B 574      -6.163  27.929 -46.779  1.00 11.78           C  
-ATOM   7751  N   ASN B 575      -9.899  29.940 -48.712  1.00 13.63           N  
-ATOM   7752  CA  ASN B 575     -10.916  30.110 -49.739  1.00 18.34           C  
-ATOM   7753  C   ASN B 575     -10.314  30.226 -51.131  1.00 21.59           C  
-ATOM   7754  O   ASN B 575      -9.297  30.895 -51.331  1.00 22.29           O  
-ATOM   7755  CB  ASN B 575     -11.779  31.336 -49.442  1.00 16.06           C  
-ATOM   7756  CG  ASN B 575     -12.664  31.139 -48.235  1.00 16.87           C  
-ATOM   7757  OD1 ASN B 575     -13.181  30.046 -48.008  1.00 18.13           O  
-ATOM   7758  ND2 ASN B 575     -12.839  32.193 -47.448  1.00 16.87           N  
-ATOM   7759  N   ILE B 576     -10.942  29.552 -52.087  1.00 16.37           N  
-ATOM   7760  CA  ILE B 576     -10.591  29.720 -53.483  1.00 14.70           C  
-ATOM   7761  C   ILE B 576     -11.412  30.870 -54.039  1.00 16.44           C  
-ATOM   7762  O   ILE B 576     -12.641  30.825 -54.024  1.00 15.82           O  
-ATOM   7763  CB  ILE B 576     -10.852  28.449 -54.309  1.00 14.13           C  
-ATOM   7764  CG1 ILE B 576     -10.019  27.285 -53.778  1.00 14.32           C  
-ATOM   7765  CG2 ILE B 576     -10.539  28.697 -55.777  1.00 19.65           C  
-ATOM   7766  CD1 ILE B 576     -10.183  26.022 -54.588  1.00 20.25           C  
-ATOM   7767  N   LEU B 577     -10.732  31.906 -54.513  1.00 13.63           N  
-ATOM   7768  CA  LEU B 577     -11.406  33.044 -55.122  1.00 19.09           C  
-ATOM   7769  C   LEU B 577     -11.635  32.794 -56.610  1.00 33.93           C  
-ATOM   7770  O   LEU B 577     -10.930  31.985 -57.219  1.00 34.36           O  
-ATOM   7771  CB  LEU B 577     -10.588  34.317 -54.914  1.00 18.52           C  
-ATOM   7772  CG  LEU B 577     -10.106  34.545 -53.479  1.00 20.72           C  
-ATOM   7773  CD1 LEU B 577      -9.063  35.653 -53.427  1.00 28.00           C  
-ATOM   7774  CD2 LEU B 577     -11.276  34.862 -52.562  1.00 20.95           C  
-ATOM   7775  N   ASN B 578     -12.623  33.476 -57.187  1.00 29.54           N  
-ATOM   7776  CA  ASN B 578     -12.912  33.377 -58.621  1.00 29.73           C  
-ATOM   7777  C   ASN B 578     -13.210  31.958 -59.095  1.00 27.80           C  
-ATOM   7778  O   ASN B 578     -12.798  31.568 -60.190  1.00 27.00           O  
-ATOM   7779  CB  ASN B 578     -11.745  33.934 -59.440  1.00 29.47           C  
-ATOM   7780  CG  ASN B 578     -11.219  35.244 -58.891  1.00 26.21           C  
-ATOM   7781  OD1 ASN B 578     -11.970  36.201 -58.701  1.00 31.99           O  
-ATOM   7782  ND2 ASN B 578      -9.919  35.292 -58.630  1.00 19.66           N  
-ATOM   7783  N   LYS B 579     -13.921  31.194 -58.271  1.00 27.91           N  
-ATOM   7784  CA  LYS B 579     -14.249  29.807 -58.592  1.00 32.82           C  
-ATOM   7785  C   LYS B 579     -14.899  29.680 -59.967  1.00 26.69           C  
-ATOM   7786  O   LYS B 579     -14.576  28.774 -60.736  1.00 27.52           O  
-ATOM   7787  CB  LYS B 579     -15.170  29.207 -57.518  1.00 28.76           C  
-ATOM   7788  CG  LYS B 579     -15.325  30.053 -56.260  1.00 41.69           C  
-ATOM   7789  CD  LYS B 579     -16.585  30.905 -56.317  1.00 65.32           C  
-ATOM   7790  CE  LYS B 579     -16.600  31.935 -55.201  1.00 49.73           C  
-ATOM   7791  NZ  LYS B 579     -15.551  32.977 -55.397  1.00 39.11           N  
-ATOM   7792  N   GLU B 580     -15.806  30.606 -60.261  1.00 29.57           N  
-ATOM   7793  CA  GLU B 580     -16.526  30.629 -61.527  1.00 32.21           C  
-ATOM   7794  C   GLU B 580     -15.576  30.612 -62.721  1.00 29.44           C  
-ATOM   7795  O   GLU B 580     -15.864  30.002 -63.748  1.00 28.27           O  
-ATOM   7796  CB  GLU B 580     -17.440  31.862 -61.587  1.00 32.94           C  
-ATOM   7797  CG  GLU B 580     -18.115  32.105 -62.930  1.00 46.40           C  
-ATOM   7798  CD  GLU B 580     -19.240  31.130 -63.222  1.00 58.96           C  
-ATOM   7799  OE1 GLU B 580     -19.812  31.206 -64.330  1.00 62.39           O  
-ATOM   7800  OE2 GLU B 580     -19.558  30.293 -62.350  1.00 60.84           O  
-ATOM   7801  N   ARG B 581     -14.430  31.265 -62.570  1.00 26.32           N  
-ATOM   7802  CA  ARG B 581     -13.466  31.363 -63.657  1.00 24.27           C  
-ATOM   7803  C   ARG B 581     -12.614  30.102 -63.779  1.00 25.37           C  
-ATOM   7804  O   ARG B 581     -12.068  29.812 -64.842  1.00 25.96           O  
-ATOM   7805  CB  ARG B 581     -12.565  32.590 -63.462  1.00 24.14           C  
-ATOM   7806  CG  ARG B 581     -11.661  32.876 -64.645  1.00 19.42           C  
-ATOM   7807  CD  ARG B 581     -10.718  34.029 -64.377  1.00 28.32           C  
-ATOM   7808  NE  ARG B 581      -9.965  33.856 -63.138  1.00 29.01           N  
-ATOM   7809  CZ  ARG B 581      -8.937  33.026 -62.995  1.00 31.79           C  
-ATOM   7810  NH1 ARG B 581      -8.541  32.270 -64.011  1.00 30.12           N  
-ATOM   7811  NH2 ARG B 581      -8.309  32.945 -61.830  1.00 23.69           N  
-ATOM   7812  N   ILE B 582     -12.508  29.348 -62.691  1.00 29.56           N  
-ATOM   7813  CA  ILE B 582     -11.593  28.212 -62.655  1.00 21.98           C  
-ATOM   7814  C   ILE B 582     -12.295  26.893 -62.955  1.00 25.27           C  
-ATOM   7815  O   ILE B 582     -13.142  26.438 -62.186  1.00 20.31           O  
-ATOM   7816  CB  ILE B 582     -10.884  28.123 -61.292  1.00 15.64           C  
-ATOM   7817  CG1 ILE B 582     -10.116  29.418 -61.027  1.00 18.46           C  
-ATOM   7818  CG2 ILE B 582      -9.950  26.922 -61.249  1.00 18.89           C  
-ATOM   7819  CD1 ILE B 582      -9.440  29.471 -59.685  1.00 30.34           C  
-ATOM   7820  N   LYS B 583     -11.939  26.289 -64.085  1.00 23.84           N  
-ATOM   7821  CA  LYS B 583     -12.581  25.059 -64.535  1.00 24.41           C  
-ATOM   7822  C   LYS B 583     -11.601  23.894 -64.661  1.00 25.49           C  
-ATOM   7823  O   LYS B 583     -11.986  22.732 -64.516  1.00 20.55           O  
-ATOM   7824  CB  LYS B 583     -13.281  25.291 -65.874  1.00 24.18           C  
-ATOM   7825  CG  LYS B 583     -14.372  26.353 -65.828  1.00 24.52           C  
-ATOM   7826  CD  LYS B 583     -15.038  26.509 -67.190  1.00 55.03           C  
-ATOM   7827  CE  LYS B 583     -16.189  27.507 -67.147  1.00 62.10           C  
-ATOM   7828  NZ  LYS B 583     -16.811  27.693 -68.492  1.00 55.07           N  
-ATOM   7829  N   GLU B 584     -10.340  24.205 -64.946  1.00 25.49           N  
-ATOM   7830  CA  GLU B 584      -9.305  23.180 -65.033  1.00 18.89           C  
-ATOM   7831  C   GLU B 584      -8.168  23.474 -64.058  1.00 15.39           C  
-ATOM   7832  O   GLU B 584      -7.988  24.610 -63.624  1.00 20.17           O  
-ATOM   7833  CB  GLU B 584      -8.773  23.070 -66.465  1.00 20.39           C  
-ATOM   7834  CG  GLU B 584      -9.852  22.912 -67.534  1.00 22.15           C  
-ATOM   7835  CD  GLU B 584     -10.599  21.595 -67.437  1.00 23.31           C  
-ATOM   7836  OE1 GLU B 584     -10.108  20.680 -66.744  1.00 25.21           O  
-ATOM   7837  OE2 GLU B 584     -11.680  21.474 -68.055  1.00 32.04           O  
-ATOM   7838  N   ILE B 585      -7.404  22.442 -63.720  1.00 17.92           N  
-ATOM   7839  CA  ILE B 585      -6.352  22.558 -62.715  1.00 22.54           C  
-ATOM   7840  C   ILE B 585      -5.263  23.557 -63.126  1.00 22.25           C  
-ATOM   7841  O   ILE B 585      -4.560  24.107 -62.277  1.00 22.67           O  
-ATOM   7842  CB  ILE B 585      -5.710  21.179 -62.426  1.00 19.57           C  
-ATOM   7843  CG1 ILE B 585      -4.802  21.243 -61.196  1.00 17.15           C  
-ATOM   7844  CG2 ILE B 585      -4.962  20.661 -63.648  1.00 20.65           C  
-ATOM   7845  CD1 ILE B 585      -5.520  21.651 -59.931  1.00 15.62           C  
-ATOM   7846  N   ASP B 586      -5.144  23.805 -64.428  1.00 19.34           N  
-ATOM   7847  CA  ASP B 586      -4.145  24.734 -64.948  1.00 19.88           C  
-ATOM   7848  C   ASP B 586      -4.572  26.190 -64.772  1.00 23.62           C  
-ATOM   7849  O   ASP B 586      -3.756  27.105 -64.900  1.00 21.15           O  
-ATOM   7850  CB  ASP B 586      -3.877  24.449 -66.427  1.00 30.46           C  
-ATOM   7851  CG  ASP B 586      -3.174  23.127 -66.646  1.00 39.81           C  
-ATOM   7852  OD1 ASP B 586      -2.209  22.839 -65.906  1.00 37.83           O  
-ATOM   7853  OD2 ASP B 586      -3.591  22.375 -67.553  1.00 37.67           O  
-ATOM   7854  N   ASP B 587      -5.850  26.396 -64.469  1.00 19.02           N  
-ATOM   7855  CA  ASP B 587      -6.420  27.739 -64.427  1.00 16.20           C  
-ATOM   7856  C   ASP B 587      -6.134  28.489 -63.124  1.00 18.91           C  
-ATOM   7857  O   ASP B 587      -6.391  29.688 -63.025  1.00 20.15           O  
-ATOM   7858  CB  ASP B 587      -7.931  27.667 -64.664  1.00 20.58           C  
-ATOM   7859  CG  ASP B 587      -8.280  27.270 -66.088  1.00 25.65           C  
-ATOM   7860  OD1 ASP B 587      -7.529  27.648 -67.013  1.00 26.35           O  
-ATOM   7861  OD2 ASP B 587      -9.305  26.582 -66.284  1.00 30.05           O  
-ATOM   7862  N   PHE B 588      -5.601  27.787 -62.129  1.00 20.05           N  
-ATOM   7863  CA  PHE B 588      -5.273  28.414 -60.852  1.00 20.66           C  
-ATOM   7864  C   PHE B 588      -4.078  29.349 -60.974  1.00 20.26           C  
-ATOM   7865  O   PHE B 588      -3.107  29.041 -61.665  1.00 22.06           O  
-ATOM   7866  CB  PHE B 588      -4.979  27.355 -59.790  1.00 26.93           C  
-ATOM   7867  CG  PHE B 588      -6.206  26.697 -59.225  1.00 23.67           C  
-ATOM   7868  CD1 PHE B 588      -6.886  27.267 -58.163  1.00 18.18           C  
-ATOM   7869  CD2 PHE B 588      -6.668  25.499 -59.742  1.00 20.51           C  
-ATOM   7870  CE1 PHE B 588      -8.009  26.661 -57.636  1.00 15.92           C  
-ATOM   7871  CE2 PHE B 588      -7.788  24.888 -59.217  1.00 16.38           C  
-ATOM   7872  CZ  PHE B 588      -8.460  25.471 -58.163  1.00 12.98           C  
-ATOM   7873  N   THR B 589      -4.156  30.494 -60.303  1.00 22.74           N  
-ATOM   7874  CA  THR B 589      -3.016  31.399 -60.188  1.00 21.40           C  
-ATOM   7875  C   THR B 589      -2.738  31.700 -58.716  1.00 23.43           C  
-ATOM   7876  O   THR B 589      -3.475  31.260 -57.834  1.00 22.04           O  
-ATOM   7877  CB  THR B 589      -3.242  32.719 -60.950  1.00 24.21           C  
-ATOM   7878  OG1 THR B 589      -4.274  33.478 -60.307  1.00 28.77           O  
-ATOM   7879  CG2 THR B 589      -3.639  32.442 -62.390  1.00 21.93           C  
-ATOM   7880  N   ALA B 590      -1.682  32.465 -58.457  1.00 28.37           N  
-ATOM   7881  CA  ALA B 590      -1.259  32.753 -57.089  1.00 20.88           C  
-ATOM   7882  C   ALA B 590      -2.155  33.783 -56.413  1.00 19.15           C  
-ATOM   7883  O   ALA B 590      -1.913  34.168 -55.270  1.00 26.02           O  
-ATOM   7884  CB  ALA B 590       0.186  33.231 -57.076  1.00 24.09           C  
-ATOM   7885  N   GLU B 591      -3.191  34.222 -57.119  1.00 17.09           N  
-ATOM   7886  CA  GLU B 591      -4.075  35.261 -56.607  1.00 18.30           C  
-ATOM   7887  C   GLU B 591      -5.493  34.748 -56.379  1.00 25.32           C  
-ATOM   7888  O   GLU B 591      -6.395  35.522 -56.054  1.00 24.40           O  
-ATOM   7889  CB  GLU B 591      -4.105  36.448 -57.569  1.00 22.45           C  
-ATOM   7890  CG  GLU B 591      -2.741  36.848 -58.106  1.00 32.92           C  
-ATOM   7891  CD  GLU B 591      -1.812  37.374 -57.029  1.00 31.64           C  
-ATOM   7892  OE1 GLU B 591      -0.582  37.228 -57.188  1.00 29.99           O  
-ATOM   7893  OE2 GLU B 591      -2.310  37.942 -56.032  1.00 31.94           O  
-ATOM   7894  N   ASP B 592      -5.688  33.444 -56.548  1.00 25.61           N  
-ATOM   7895  CA  ASP B 592      -7.016  32.853 -56.411  1.00 25.61           C  
-ATOM   7896  C   ASP B 592      -7.232  32.202 -55.047  1.00 19.92           C  
-ATOM   7897  O   ASP B 592      -8.049  31.292 -54.908  1.00 19.58           O  
-ATOM   7898  CB  ASP B 592      -7.252  31.820 -57.514  1.00 22.58           C  
-ATOM   7899  CG  ASP B 592      -7.137  32.415 -58.900  1.00 28.02           C  
-ATOM   7900  OD1 ASP B 592      -8.001  33.241 -59.264  1.00 32.77           O  
-ATOM   7901  OD2 ASP B 592      -6.189  32.052 -59.627  1.00 33.19           O  
-ATOM   7902  N   PHE B 593      -6.503  32.670 -54.041  1.00 17.93           N  
-ATOM   7903  CA  PHE B 593      -6.623  32.109 -52.702  1.00 18.03           C  
-ATOM   7904  C   PHE B 593      -6.604  33.190 -51.638  1.00 20.14           C  
-ATOM   7905  O   PHE B 593      -5.868  34.170 -51.752  1.00 25.23           O  
-ATOM   7906  CB  PHE B 593      -5.494  31.116 -52.423  1.00 16.64           C  
-ATOM   7907  CG  PHE B 593      -5.472  29.938 -53.350  1.00 17.60           C  
-ATOM   7908  CD1 PHE B 593      -6.184  28.790 -53.049  1.00 17.63           C  
-ATOM   7909  CD2 PHE B 593      -4.724  29.972 -54.513  1.00 15.68           C  
-ATOM   7910  CE1 PHE B 593      -6.159  27.702 -53.898  1.00 15.83           C  
-ATOM   7911  CE2 PHE B 593      -4.695  28.890 -55.367  1.00 17.46           C  
-ATOM   7912  CZ  PHE B 593      -5.411  27.752 -55.058  1.00 21.29           C  
-ATOM   7913  N   GLU B 594      -7.414  33.009 -50.600  1.00 20.37           N  
-ATOM   7914  CA  GLU B 594      -7.278  33.828 -49.406  1.00 23.22           C  
-ATOM   7915  C   GLU B 594      -7.172  32.931 -48.178  1.00 21.34           C  
-ATOM   7916  O   GLU B 594      -7.842  31.899 -48.080  1.00 15.61           O  
-ATOM   7917  CB  GLU B 594      -8.441  34.816 -49.266  1.00 23.38           C  
-ATOM   7918  CG  GLU B 594      -9.780  34.217 -48.867  1.00 30.67           C  
-ATOM   7919  CD  GLU B 594     -10.839  35.283 -48.631  1.00 34.75           C  
-ATOM   7920  OE1 GLU B 594     -12.043  34.948 -48.641  1.00 28.38           O  
-ATOM   7921  OE2 GLU B 594     -10.463  36.460 -48.438  1.00 24.96           O  
-ATOM   7922  N   VAL B 595      -6.297  33.319 -47.258  1.00 19.72           N  
-ATOM   7923  CA  VAL B 595      -6.123  32.587 -46.015  1.00 13.56           C  
-ATOM   7924  C   VAL B 595      -6.808  33.352 -44.894  1.00 16.02           C  
-ATOM   7925  O   VAL B 595      -6.312  34.372 -44.422  1.00 18.07           O  
-ATOM   7926  CB  VAL B 595      -4.642  32.369 -45.690  1.00 15.68           C  
-ATOM   7927  CG1 VAL B 595      -4.492  31.698 -44.334  1.00 23.58           C  
-ATOM   7928  CG2 VAL B 595      -3.993  31.536 -46.780  1.00 13.83           C  
-ATOM   7929  N   VAL B 596      -7.958  32.840 -44.478  1.00 18.49           N  
-ATOM   7930  CA  VAL B 596      -8.855  33.549 -43.579  1.00 16.55           C  
-ATOM   7931  C   VAL B 596      -8.754  33.060 -42.134  1.00 28.71           C  
-ATOM   7932  O   VAL B 596      -8.951  31.875 -41.852  1.00 32.30           O  
-ATOM   7933  CB  VAL B 596     -10.314  33.411 -44.067  1.00 12.83           C  
-ATOM   7934  CG1 VAL B 596     -11.290  33.667 -42.943  1.00 15.74           C  
-ATOM   7935  CG2 VAL B 596     -10.571  34.346 -45.238  1.00 14.81           C  
-ATOM   7936  N   GLY B 597      -8.445  33.983 -41.224  1.00 21.10           N  
-ATOM   7937  CA  GLY B 597      -8.427  33.690 -39.801  1.00 20.31           C  
-ATOM   7938  C   GLY B 597      -7.167  33.003 -39.311  1.00 23.36           C  
-ATOM   7939  O   GLY B 597      -7.212  32.191 -38.387  1.00 26.62           O  
-ATOM   7940  N   TYR B 598      -6.035  33.331 -39.922  1.00 22.93           N  
-ATOM   7941  CA  TYR B 598      -4.769  32.711 -39.551  1.00 22.36           C  
-ATOM   7942  C   TYR B 598      -4.071  33.512 -38.461  1.00 18.63           C  
-ATOM   7943  O   TYR B 598      -3.541  34.590 -38.719  1.00 18.87           O  
-ATOM   7944  CB  TYR B 598      -3.865  32.579 -40.779  1.00 27.57           C  
-ATOM   7945  CG  TYR B 598      -2.651  31.700 -40.581  1.00 18.99           C  
-ATOM   7946  CD1 TYR B 598      -2.756  30.471 -39.943  1.00 26.26           C  
-ATOM   7947  CD2 TYR B 598      -1.405  32.088 -41.053  1.00 17.40           C  
-ATOM   7948  CE1 TYR B 598      -1.651  29.657 -39.768  1.00 25.09           C  
-ATOM   7949  CE2 TYR B 598      -0.294  31.283 -40.883  1.00 25.98           C  
-ATOM   7950  CZ  TYR B 598      -0.422  30.067 -40.240  1.00 28.49           C  
-ATOM   7951  OH  TYR B 598       0.679  29.258 -40.067  1.00 23.97           O  
-ATOM   7952  N   VAL B 599      -4.083  32.981 -37.240  1.00 22.27           N  
-ATOM   7953  CA  VAL B 599      -3.435  33.635 -36.105  1.00 18.62           C  
-ATOM   7954  C   VAL B 599      -2.397  32.712 -35.463  1.00 23.96           C  
-ATOM   7955  O   VAL B 599      -2.680  32.056 -34.462  1.00 31.32           O  
-ATOM   7956  CB  VAL B 599      -4.461  34.058 -35.033  1.00 14.80           C  
-ATOM   7957  CG1 VAL B 599      -3.817  34.991 -34.018  1.00 26.27           C  
-ATOM   7958  CG2 VAL B 599      -5.662  34.724 -35.679  1.00 19.47           C  
-ATOM   7959  N   PRO B 600      -1.189  32.652 -36.045  1.00 24.55           N  
-ATOM   7960  CA  PRO B 600      -0.151  31.738 -35.562  1.00 26.70           C  
-ATOM   7961  C   PRO B 600       0.817  32.378 -34.573  1.00 24.56           C  
-ATOM   7962  O   PRO B 600       0.831  33.599 -34.423  1.00 28.29           O  
-ATOM   7963  CB  PRO B 600       0.579  31.357 -36.846  1.00 24.56           C  
-ATOM   7964  CG  PRO B 600       0.506  32.602 -37.672  1.00 20.64           C  
-ATOM   7965  CD  PRO B 600      -0.799  33.291 -37.315  1.00 27.40           C  
-ATOM   7966  N   HIS B 601       1.617  31.552 -33.906  1.00 25.73           N  
-ATOM   7967  CA  HIS B 601       2.693  32.056 -33.064  1.00 29.16           C  
-ATOM   7968  C   HIS B 601       3.814  32.592 -33.946  1.00 36.06           C  
-ATOM   7969  O   HIS B 601       3.747  32.496 -35.172  1.00 35.77           O  
-ATOM   7970  CB  HIS B 601       3.222  30.966 -32.129  1.00 26.24           C  
-ATOM   7971  CG  HIS B 601       2.238  30.524 -31.091  1.00 27.25           C  
-ATOM   7972  ND1 HIS B 601       2.135  31.129 -29.856  1.00 31.63           N  
-ATOM   7973  CD2 HIS B 601       1.316  29.533 -31.101  1.00 24.02           C  
-ATOM   7974  CE1 HIS B 601       1.191  30.531 -29.152  1.00 28.06           C  
-ATOM   7975  NE2 HIS B 601       0.678  29.559 -29.885  1.00 23.22           N  
-ATOM   7976  N   GLY B 602       4.843  33.150 -33.319  1.00 38.53           N  
-ATOM   7977  CA  GLY B 602       5.951  33.736 -34.052  1.00 49.39           C  
-ATOM   7978  C   GLY B 602       6.753  32.716 -34.837  1.00 49.96           C  
-ATOM   7979  O   GLY B 602       6.714  31.522 -34.539  1.00 47.66           O  
-ATOM   7980  N   ARG B 603       7.482  33.188 -35.843  1.00 57.19           N  
-ATOM   7981  CA  ARG B 603       8.324  32.315 -36.653  1.00 45.97           C  
-ATOM   7982  C   ARG B 603       9.434  31.705 -35.809  1.00 37.83           C  
-ATOM   7983  O   ARG B 603      10.051  32.390 -34.994  1.00 35.66           O  
-ATOM   7984  CB  ARG B 603       8.934  33.081 -37.829  1.00 52.51           C  
-ATOM   7985  CG  ARG B 603       8.000  34.084 -38.485  1.00 61.53           C  
-ATOM   7986  CD  ARG B 603       8.591  34.603 -39.787  1.00 50.34           C  
-ATOM   7987  NE  ARG B 603       8.368  33.669 -40.888  1.00 78.31           N  
-ATOM   7988  CZ  ARG B 603       7.558  33.906 -41.916  1.00 74.26           C  
-ATOM   7989  NH1 ARG B 603       7.409  32.996 -42.871  1.00 45.05           N  
-ATOM   7990  NH2 ARG B 603       6.903  35.058 -41.994  1.00 60.43           N  
-ATOM   7991  N   ILE B 604       9.681  30.414 -36.000  1.00 44.71           N  
-ATOM   7992  CA  ILE B 604      10.798  29.752 -35.339  1.00 54.94           C  
-ATOM   7993  C   ILE B 604      11.838  29.337 -36.373  1.00 53.97           C  
-ATOM   7994  O   ILE B 604      11.624  28.402 -37.145  1.00 48.63           O  
-ATOM   7995  CB  ILE B 604      10.351  28.516 -34.542  1.00 49.24           C  
-ATOM   7996  CG1 ILE B 604       9.257  28.888 -33.539  1.00 45.38           C  
-ATOM   7997  CG2 ILE B 604      11.541  27.893 -33.828  1.00 40.92           C  
-ATOM   7998  CD1 ILE B 604       8.798  27.724 -32.683  1.00 35.05           C  
-ATOM   7999  N   GLN B 605      12.965  30.041 -36.378  1.00 53.20           N  
-ATOM   8000  CA  GLN B 605      13.994  29.848 -37.392  1.00 57.80           C  
-ATOM   8001  C   GLN B 605      14.715  28.512 -37.235  1.00 57.53           C  
-ATOM   8002  O   GLN B 605      15.201  28.175 -36.155  1.00 44.51           O  
-ATOM   8003  CB  GLN B 605      15.001  31.002 -37.342  1.00 59.56           C  
-ATOM   8004  CG  GLN B 605      15.772  31.226 -38.638  1.00 64.00           C  
-ATOM   8005  CD  GLN B 605      17.107  30.507 -38.664  1.00 59.62           C  
-ATOM   8006  OE1 GLN B 605      17.664  30.168 -37.618  1.00 51.52           O  
-ATOM   8007  NE2 GLN B 605      17.631  30.274 -39.864  1.00 37.00           N  
-ATOM   8008  N   MET B 606      14.769  27.753 -38.327  1.00 58.18           N  
-ATOM   8009  CA  MET B 606      15.490  26.483 -38.364  1.00 60.69           C  
-ATOM   8010  C   MET B 606      16.284  26.359 -39.661  1.00 54.57           C  
-ATOM   8011  O   MET B 606      15.722  26.454 -40.754  1.00 61.53           O  
-ATOM   8012  CB  MET B 606      14.526  25.302 -38.223  1.00 54.76           C  
-ATOM   8013  CG  MET B 606      13.759  25.279 -36.913  1.00 52.58           C  
-ATOM   8014  SD  MET B 606      12.555  23.942 -36.829  1.00 48.57           S  
-ATOM   8015  CE  MET B 606      11.457  24.569 -35.562  1.00 32.91           C  
-ATOM   8016  N   GLU B 607      17.591  26.152 -39.536  1.00 45.99           N  
-ATOM   8017  CA  GLU B 607      18.462  26.058 -40.701  1.00 57.70           C  
-ATOM   8018  C   GLU B 607      18.246  24.747 -41.446  1.00 56.32           C  
-ATOM   8019  O   GLU B 607      18.056  23.694 -40.837  1.00 43.19           O  
-ATOM   8020  CB  GLU B 607      19.934  26.202 -40.295  1.00 61.86           C  
-ATOM   8021  CG  GLU B 607      20.409  25.201 -39.254  1.00 71.27           C  
-ATOM   8022  CD  GLU B 607      20.027  25.599 -37.839  1.00 85.97           C  
-ATOM   8023  OE1 GLU B 607      20.910  26.085 -37.099  1.00 87.57           O  
-ATOM   8024  OE2 GLU B 607      18.844  25.427 -37.469  1.00 73.22           O  
-ATOM   8025  N   MET B 608      18.278  24.823 -42.772  1.00 71.12           N  
-ATOM   8026  CA  MET B 608      18.052  23.656 -43.613  1.00 59.47           C  
-ATOM   8027  C   MET B 608      19.333  22.849 -43.795  1.00 49.70           C  
-ATOM   8028  O   MET B 608      20.305  23.332 -44.378  1.00 42.91           O  
-ATOM   8029  CB  MET B 608      17.502  24.075 -44.979  1.00 55.75           C  
-ATOM   8030  CG  MET B 608      16.874  22.938 -45.768  1.00 58.55           C  
-ATOM   8031  SD  MET B 608      17.419  22.866 -47.487  1.00 52.57           S  
-ATOM   8032  CE  MET B 608      17.164  24.557 -48.013  1.00 59.39           C  
-ATOM   8033  N   ALA B 609      19.326  21.620 -43.289  1.00 52.27           N  
-ATOM   8034  CA  ALA B 609      20.450  20.712 -43.473  1.00 47.67           C  
-ATOM   8035  C   ALA B 609      20.566  20.318 -44.941  1.00 48.28           C  
-ATOM   8036  O   ALA B 609      19.782  19.512 -45.443  1.00 53.75           O  
-ATOM   8037  CB  ALA B 609      20.290  19.480 -42.600  1.00 40.87           C  
-ATOM   8038  N   VAL B 610      21.547  20.897 -45.624  1.00 50.03           N  
-ATOM   8039  CA  VAL B 610      21.711  20.686 -47.056  1.00 64.54           C  
-ATOM   8040  C   VAL B 610      22.266  19.295 -47.356  1.00 61.84           C  
-ATOM   8041  O   VAL B 610      21.764  18.592 -48.235  1.00 63.56           O  
-ATOM   8042  CB  VAL B 610      22.640  21.753 -47.676  1.00 61.19           C  
-ATOM   8043  CG1 VAL B 610      22.718  21.579 -49.185  1.00 56.14           C  
-ATOM   8044  CG2 VAL B 610      22.153  23.151 -47.321  1.00 43.54           C  
-ATOM   8045  OXT VAL B 610      23.221  18.839 -46.723  1.00 45.57           O  
-TER    8046      VAL B 610                                                      
-ATOM   8047  N   PRO C   4     -13.817  22.576 -92.516  1.00 47.72           N  
-ATOM   8048  CA  PRO C   4     -14.005  21.896 -93.804  1.00 45.12           C  
-ATOM   8049  C   PRO C   4     -15.431  22.064 -94.330  1.00 52.07           C  
-ATOM   8050  O   PRO C   4     -16.303  21.240 -94.048  1.00 49.98           O  
-ATOM   8051  CB  PRO C   4     -13.703  20.434 -93.474  1.00 41.79           C  
-ATOM   8052  CG  PRO C   4     -14.054  20.303 -92.023  1.00 63.13           C  
-ATOM   8053  CD  PRO C   4     -13.739  21.631 -91.387  1.00 34.18           C  
-ATOM   8054  N   VAL C   5     -15.653  23.127 -95.098  1.00 47.38           N  
-ATOM   8055  CA  VAL C   5     -16.997  23.503 -95.524  1.00 45.98           C  
-ATOM   8056  C   VAL C   5     -17.273  23.124 -96.983  1.00 39.45           C  
-ATOM   8057  O   VAL C   5     -16.356  23.037 -97.801  1.00 41.08           O  
-ATOM   8058  CB  VAL C   5     -17.226  25.027 -95.330  1.00 36.73           C  
-ATOM   8059  CG1 VAL C   5     -16.516  25.825 -96.408  1.00 32.95           C  
-ATOM   8060  CG2 VAL C   5     -18.703  25.357 -95.322  1.00 46.75           C  
-ATOM   8061  N   CYS C   6     -18.542  22.877 -97.298  1.00 33.84           N  
-ATOM   8062  CA  CYS C   6     -18.957  22.623 -98.675  1.00 36.68           C  
-ATOM   8063  C   CYS C   6     -19.941  23.686 -99.152  1.00 38.62           C  
-ATOM   8064  O   CYS C   6     -20.855  24.055 -98.428  1.00 43.84           O  
-ATOM   8065  CB  CYS C   6     -19.586  21.232 -98.805  1.00 38.61           C  
-ATOM   8066  SG  CYS C   6     -18.424  19.851 -98.656  1.00 56.89           S  
-ATOM   8067  N   LEU C   7     -19.750  24.176-100.373  1.00 34.82           N  
-ATOM   8068  CA  LEU C   7     -20.663  25.152-100.966  1.00 22.54           C  
-ATOM   8069  C   LEU C   7     -21.688  24.451-101.849  1.00 28.30           C  
-ATOM   8070  O   LEU C   7     -21.351  23.498-102.550  1.00 34.59           O  
-ATOM   8071  CB  LEU C   7     -19.896  26.190-101.789  1.00 19.89           C  
-ATOM   8072  CG  LEU C   7     -19.337  27.442-101.109  1.00 30.95           C  
-ATOM   8073  CD1 LEU C   7     -18.449  27.099 -99.920  1.00 40.29           C  
-ATOM   8074  CD2 LEU C   7     -18.572  28.294-102.117  1.00 29.91           C  
-ATOM   8075  N   VAL C   8     -22.938  24.910-101.818  1.00 29.88           N  
-ATOM   8076  CA  VAL C   8     -23.956  24.331-102.701  1.00 27.93           C  
-ATOM   8077  C   VAL C   8     -24.731  25.406-103.478  1.00 30.79           C  
-ATOM   8078  O   VAL C   8     -25.349  26.295-102.887  1.00 26.23           O  
-ATOM   8079  CB  VAL C   8     -24.944  23.437-101.910  1.00 13.59           C  
-ATOM   8080  CG1 VAL C   8     -25.217  24.019-100.538  1.00 27.39           C  
-ATOM   8081  CG2 VAL C   8     -26.235  23.232-102.693  1.00 21.42           C  
-ATOM   8082  N   VAL C   9     -24.696  25.308-104.807  1.00 26.03           N  
-ATOM   8083  CA  VAL C   9     -25.226  26.353-105.686  1.00 23.45           C  
-ATOM   8084  C   VAL C   9     -26.034  25.840-106.873  1.00 23.92           C  
-ATOM   8085  O   VAL C   9     -25.838  24.718-107.339  1.00 32.71           O  
-ATOM   8086  CB  VAL C   9     -24.091  27.219-106.274  1.00 28.90           C  
-ATOM   8087  CG1 VAL C   9     -23.848  28.442-105.429  1.00 29.00           C  
-ATOM   8088  CG2 VAL C   9     -22.820  26.396-106.429  1.00 32.22           C  
-ATOM   8089  N   ALA C  10     -26.937  26.686-107.357  1.00 23.45           N  
-ATOM   8090  CA  ALA C  10     -27.551  26.515-108.669  1.00 23.26           C  
-ATOM   8091  C   ALA C  10     -27.184  27.749-109.490  1.00 28.91           C  
-ATOM   8092  O   ALA C  10     -27.259  28.872-108.989  1.00 31.01           O  
-ATOM   8093  CB  ALA C  10     -29.053  26.345-108.557  1.00 25.23           C  
-ATOM   8094  N   MET C  11     -26.786  27.551-110.743  1.00 24.85           N  
-ATOM   8095  CA  MET C  11     -26.030  28.584-111.446  1.00 18.24           C  
-ATOM   8096  C   MET C  11     -26.223  28.595-112.966  1.00 26.81           C  
-ATOM   8097  O   MET C  11     -26.263  27.543-113.608  1.00 34.50           O  
-ATOM   8098  CB  MET C  11     -24.550  28.399-111.120  1.00 16.92           C  
-ATOM   8099  CG  MET C  11     -23.671  29.587-111.388  1.00 21.32           C  
-ATOM   8100  SD  MET C  11     -21.951  29.161-111.059  1.00 28.61           S  
-ATOM   8101  CE  MET C  11     -22.072  28.455-109.417  1.00 20.38           C  
-ATOM   8102  N   THR C  12     -26.332  29.792-113.537  1.00 21.51           N  
-ATOM   8103  CA  THR C  12     -26.407  29.955-114.989  1.00 25.71           C  
-ATOM   8104  C   THR C  12     -24.989  29.919-115.580  1.00 31.39           C  
-ATOM   8105  O   THR C  12     -24.014  30.004-114.830  1.00 33.37           O  
-ATOM   8106  CB  THR C  12     -27.119  31.273-115.367  1.00 18.19           C  
-ATOM   8107  OG1 THR C  12     -26.330  32.389-114.941  1.00 24.61           O  
-ATOM   8108  CG2 THR C  12     -28.488  31.345-114.712  1.00 18.17           C  
-ATOM   8109  N   PRO C  13     -24.859  29.765-116.915  1.00 22.68           N  
-ATOM   8110  CA  PRO C  13     -23.512  29.742-117.503  1.00 17.22           C  
-ATOM   8111  C   PRO C  13     -22.710  31.015-117.245  1.00 18.60           C  
-ATOM   8112  O   PRO C  13     -21.481  30.963-117.196  1.00 20.12           O  
-ATOM   8113  CB  PRO C  13     -23.788  29.580-118.999  1.00 17.72           C  
-ATOM   8114  CG  PRO C  13     -25.080  28.871-119.056  1.00 22.62           C  
-ATOM   8115  CD  PRO C  13     -25.886  29.415-117.913  1.00 20.83           C  
-ATOM   8116  N   LYS C  14     -23.397  32.140-117.085  1.00 19.08           N  
-ATOM   8117  CA  LYS C  14     -22.725  33.396-116.773  1.00 23.85           C  
-ATOM   8118  C   LYS C  14     -22.737  33.649-115.268  1.00 27.17           C  
-ATOM   8119  O   LYS C  14     -22.729  34.795-114.816  1.00 26.02           O  
-ATOM   8120  CB  LYS C  14     -23.373  34.553-117.538  1.00 13.95           C  
-ATOM   8121  CG  LYS C  14     -22.858  34.670-118.967  1.00 23.95           C  
-ATOM   8122  CD  LYS C  14     -23.946  35.050-119.959  1.00 31.93           C  
-ATOM   8123  CE  LYS C  14     -24.173  36.552-120.011  1.00 34.71           C  
-ATOM   8124  NZ  LYS C  14     -25.079  36.922-121.134  1.00 25.03           N  
-ATOM   8125  N   ARG C  15     -22.762  32.552-114.511  1.00 23.36           N  
-ATOM   8126  CA  ARG C  15     -22.621  32.557-113.055  1.00 16.99           C  
-ATOM   8127  C   ARG C  15     -23.723  33.309-112.311  1.00 19.40           C  
-ATOM   8128  O   ARG C  15     -23.551  33.671-111.149  1.00 18.25           O  
-ATOM   8129  CB  ARG C  15     -21.253  33.126-112.662  1.00 16.80           C  
-ATOM   8130  CG  ARG C  15     -20.124  32.117-112.774  1.00 18.60           C  
-ATOM   8131  CD  ARG C  15     -18.774  32.704-112.380  1.00 19.55           C  
-ATOM   8132  NE  ARG C  15     -18.286  33.672-113.358  1.00 19.25           N  
-ATOM   8133  CZ  ARG C  15     -18.230  34.984-113.149  1.00 24.30           C  
-ATOM   8134  NH1 ARG C  15     -17.773  35.787-114.100  1.00 27.77           N  
-ATOM   8135  NH2 ARG C  15     -18.623  35.493-111.989  1.00 23.91           N  
-ATOM   8136  N   GLY C  16     -24.856  33.525-112.972  1.00 19.77           N  
-ATOM   8137  CA  GLY C  16     -25.985  34.190-112.345  1.00 16.87           C  
-ATOM   8138  C   GLY C  16     -26.712  33.261-111.396  1.00 20.64           C  
-ATOM   8139  O   GLY C  16     -26.914  32.086-111.706  1.00 25.58           O  
-ATOM   8140  N   ILE C  17     -27.104  33.777-110.234  1.00 20.94           N  
-ATOM   8141  CA  ILE C  17     -27.763  32.945-109.231  1.00 23.75           C  
-ATOM   8142  C   ILE C  17     -29.087  33.523-108.727  1.00 25.64           C  
-ATOM   8143  O   ILE C  17     -29.901  32.799-108.150  1.00 24.20           O  
-ATOM   8144  CB  ILE C  17     -26.852  32.702-108.010  1.00 19.49           C  
-ATOM   8145  CG1 ILE C  17     -26.578  34.014-107.278  1.00 19.27           C  
-ATOM   8146  CG2 ILE C  17     -25.551  32.029-108.427  1.00 17.31           C  
-ATOM   8147  CD1 ILE C  17     -25.755  33.842-106.022  1.00 20.62           C  
-ATOM   8148  N   GLY C  18     -29.308  34.818-108.936  1.00 25.21           N  
-ATOM   8149  CA  GLY C  18     -30.527  35.438-108.445  1.00 28.06           C  
-ATOM   8150  C   GLY C  18     -30.957  36.737-109.100  1.00 23.16           C  
-ATOM   8151  O   GLY C  18     -30.166  37.402-109.771  1.00 23.10           O  
-ATOM   8152  N   ILE C  19     -32.226  37.093-108.899  1.00 20.62           N  
-ATOM   8153  CA  ILE C  19     -32.754  38.380-109.343  1.00 20.67           C  
-ATOM   8154  C   ILE C  19     -33.927  38.830-108.462  1.00 28.11           C  
-ATOM   8155  O   ILE C  19     -34.817  38.038-108.139  1.00 34.31           O  
-ATOM   8156  CB  ILE C  19     -33.189  38.331-110.824  1.00 14.14           C  
-ATOM   8157  CG1 ILE C  19     -33.625  39.715-111.299  1.00 12.27           C  
-ATOM   8158  CG2 ILE C  19     -34.285  37.297-111.045  1.00 15.28           C  
-ATOM   8159  CD1 ILE C  19     -33.141  40.048-112.681  1.00 17.11           C  
-ATOM   8160  N   ASN C  20     -33.906  40.103-108.067  1.00 21.76           N  
-ATOM   8161  CA  ASN C  20     -34.908  40.675-107.163  1.00 25.22           C  
-ATOM   8162  C   ASN C  20     -35.111  39.839-105.907  1.00 26.81           C  
-ATOM   8163  O   ASN C  20     -36.244  39.581-105.499  1.00 28.30           O  
-ATOM   8164  CB  ASN C  20     -36.246  40.855-107.882  1.00 21.92           C  
-ATOM   8165  CG  ASN C  20     -36.305  42.131-108.694  1.00 40.92           C  
-ATOM   8166  OD1 ASN C  20     -35.862  43.189-108.245  1.00 44.36           O  
-ATOM   8167  ND2 ASN C  20     -36.846  42.038-109.902  1.00 57.71           N  
-ATOM   8168  N   ASN C  21     -34.000  39.421-105.307  1.00 27.93           N  
-ATOM   8169  CA  ASN C  21     -34.015  38.593-104.107  1.00 26.73           C  
-ATOM   8170  C   ASN C  21     -34.844  37.327-104.308  1.00 26.11           C  
-ATOM   8171  O   ASN C  21     -35.516  36.855-103.391  1.00 38.58           O  
-ATOM   8172  CB  ASN C  21     -34.542  39.391-102.915  1.00 23.41           C  
-ATOM   8173  CG  ASN C  21     -33.989  38.898-101.597  1.00 36.63           C  
-ATOM   8174  OD1 ASN C  21     -32.784  38.962-101.359  1.00 38.98           O  
-ATOM   8175  ND2 ASN C  21     -34.867  38.411-100.728  1.00 41.60           N  
-ATOM   8176  N   GLY C  22     -34.789  36.785-105.520  1.00 21.75           N  
-ATOM   8177  CA  GLY C  22     -35.488  35.557-105.850  1.00 21.90           C  
-ATOM   8178  C   GLY C  22     -34.665  34.730-106.816  1.00 19.64           C  
-ATOM   8179  O   GLY C  22     -33.510  35.053-107.083  1.00 24.59           O  
-ATOM   8180  N   LEU C  23     -35.253  33.662-107.340  1.00 17.62           N  
-ATOM   8181  CA  LEU C  23     -34.552  32.814-108.295  1.00 17.24           C  
-ATOM   8182  C   LEU C  23     -34.879  33.225-109.727  1.00 20.52           C  
-ATOM   8183  O   LEU C  23     -36.013  33.596-110.031  1.00 26.04           O  
-ATOM   8184  CB  LEU C  23     -34.900  31.344-108.065  1.00 20.39           C  
-ATOM   8185  CG  LEU C  23     -34.512  30.802-106.689  1.00 20.57           C  
-ATOM   8186  CD1 LEU C  23     -34.870  29.329-106.566  1.00 29.44           C  
-ATOM   8187  CD2 LEU C  23     -33.031  31.027-106.423  1.00 22.63           C  
-ATOM   8188  N   PRO C  24     -33.874  33.166-110.612  1.00 20.00           N  
-ATOM   8189  CA  PRO C  24     -33.993  33.608-112.006  1.00 18.21           C  
-ATOM   8190  C   PRO C  24     -34.868  32.693-112.861  1.00 23.42           C  
-ATOM   8191  O   PRO C  24     -35.464  33.147-113.838  1.00 27.14           O  
-ATOM   8192  CB  PRO C  24     -32.542  33.579-112.506  1.00 15.72           C  
-ATOM   8193  CG  PRO C  24     -31.693  33.496-111.275  1.00 17.34           C  
-ATOM   8194  CD  PRO C  24     -32.504  32.738-110.291  1.00 19.61           C  
-ATOM   8195  N   TRP C  25     -34.944  31.422-112.484  1.00 25.89           N  
-ATOM   8196  CA  TRP C  25     -35.612  30.401-113.285  1.00 20.50           C  
-ATOM   8197  C   TRP C  25     -36.926  29.935-112.656  1.00 28.05           C  
-ATOM   8198  O   TRP C  25     -37.176  30.190-111.478  1.00 28.50           O  
-ATOM   8199  CB  TRP C  25     -34.672  29.209-113.467  1.00 17.34           C  
-ATOM   8200  CG  TRP C  25     -33.990  28.826-112.191  1.00 21.43           C  
-ATOM   8201  CD1 TRP C  25     -34.514  28.089-111.169  1.00 20.67           C  
-ATOM   8202  CD2 TRP C  25     -32.660  29.177-111.791  1.00 22.87           C  
-ATOM   8203  NE1 TRP C  25     -33.590  27.954-110.160  1.00 17.33           N  
-ATOM   8204  CE2 TRP C  25     -32.444  28.612-110.518  1.00 19.48           C  
-ATOM   8205  CE3 TRP C  25     -31.629  29.910-112.388  1.00 19.77           C  
-ATOM   8206  CZ2 TRP C  25     -31.241  28.758-109.832  1.00 18.48           C  
-ATOM   8207  CZ3 TRP C  25     -30.434  30.053-111.704  1.00 18.60           C  
-ATOM   8208  CH2 TRP C  25     -30.251  29.479-110.440  1.00 17.42           C  
-ATOM   8209  N   PRO C  26     -37.776  29.253-113.444  1.00 23.27           N  
-ATOM   8210  CA  PRO C  26     -38.933  28.553-112.873  1.00 25.85           C  
-ATOM   8211  C   PRO C  26     -38.500  27.441-111.915  1.00 39.92           C  
-ATOM   8212  O   PRO C  26     -37.312  27.115-111.850  1.00 37.72           O  
-ATOM   8213  CB  PRO C  26     -39.650  27.987-114.102  1.00 19.84           C  
-ATOM   8214  CG  PRO C  26     -38.644  28.041-115.207  1.00 19.71           C  
-ATOM   8215  CD  PRO C  26     -37.792  29.225-114.915  1.00 19.47           C  
-ATOM   8216  N  AHIS C  27     -39.450  26.869-111.181  0.31 57.48           N  
-ATOM   8217  N  BHIS C  27     -39.457  26.872-111.187  0.69 54.23           N  
-ATOM   8218  CA AHIS C  27     -39.124  25.919-110.120  0.31 48.68           C  
-ATOM   8219  CA BHIS C  27     -39.158  25.886-110.150  0.69 49.89           C  
-ATOM   8220  C  AHIS C  27     -38.485  24.644-110.671  0.31 50.31           C  
-ATOM   8221  C  BHIS C  27     -38.463  24.651-110.715  0.69 49.81           C  
-ATOM   8222  O  AHIS C  27     -39.033  23.988-111.559  0.31 40.79           O  
-ATOM   8223  O  BHIS C  27     -38.959  24.022-111.651  0.69 39.74           O  
-ATOM   8224  CB AHIS C  27     -40.373  25.581-109.291  0.31 39.29           C  
-ATOM   8225  CB BHIS C  27     -40.441  25.474-109.423  0.69 38.64           C  
-ATOM   8226  CG AHIS C  27     -41.415  24.808-110.039  0.31 43.76           C  
-ATOM   8227  CG BHIS C  27     -40.203  24.657-108.191  0.69 32.62           C  
-ATOM   8228  ND1AHIS C  27     -41.421  23.431-110.094  0.31 44.19           N  
-ATOM   8229  ND1BHIS C  27     -39.875  25.224-106.979  0.69 29.63           N  
-ATOM   8230  CD2AHIS C  27     -42.487  25.218-110.758  0.31 42.31           C  
-ATOM   8231  CD2BHIS C  27     -40.239  23.321-107.986  0.69 33.77           C  
-ATOM   8232  CE1AHIS C  27     -42.450  23.026-110.815  0.31 37.07           C  
-ATOM   8233  CE1BHIS C  27     -39.723  24.270-106.078  0.69 30.51           C  
-ATOM   8234  NE2AHIS C  27     -43.113  24.091-111.230  0.31 35.86           N  
-ATOM   8235  NE2BHIS C  27     -39.938  23.105-106.662  0.69 28.58           N  
-ATOM   8236  N   LEU C  28     -37.311  24.317-110.144  1.00 38.42           N  
-ATOM   8237  CA  LEU C  28     -36.580  23.121-110.543  1.00 27.97           C  
-ATOM   8238  C   LEU C  28     -36.682  22.076-109.438  1.00 32.91           C  
-ATOM   8239  O   LEU C  28     -35.827  21.987-108.555  1.00 40.62           O  
-ATOM   8240  CB  LEU C  28     -35.118  23.446-110.846  1.00 27.20           C  
-ATOM   8241  CG  LEU C  28     -34.854  24.619-111.795  1.00 39.16           C  
-ATOM   8242  CD1 LEU C  28     -33.359  24.774-112.047  1.00 24.89           C  
-ATOM   8243  CD2 LEU C  28     -35.612  24.456-113.106  1.00 32.39           C  
-ATOM   8244  N   THR C  29     -37.747  21.289-109.503  1.00 35.66           N  
-ATOM   8245  CA  THR C  29     -38.081  20.333-108.459  1.00 41.33           C  
-ATOM   8246  C   THR C  29     -36.951  19.348-108.152  1.00 33.75           C  
-ATOM   8247  O   THR C  29     -36.690  19.044-106.985  1.00 34.13           O  
-ATOM   8248  CB  THR C  29     -39.352  19.545-108.834  1.00 36.23           C  
-ATOM   8249  OG1 THR C  29     -39.499  18.429-107.948  1.00 48.86           O  
-ATOM   8250  CG2 THR C  29     -39.280  19.044-110.271  1.00 32.68           C  
-ATOM   8251  N   THR C  30     -36.273  18.863-109.188  1.00 21.76           N  
-ATOM   8252  CA  THR C  30     -35.185  17.913-108.998  1.00 24.49           C  
-ATOM   8253  C   THR C  30     -34.002  18.595-108.330  1.00 25.99           C  
-ATOM   8254  O   THR C  30     -33.311  17.994-107.512  1.00 25.96           O  
-ATOM   8255  CB  THR C  30     -34.747  17.291-110.330  1.00 19.19           C  
-ATOM   8256  OG1 THR C  30     -35.844  16.566-110.899  1.00 21.04           O  
-ATOM   8257  CG2 THR C  30     -33.576  16.344-110.129  1.00 19.87           C  
-ATOM   8258  N   ASP C  31     -33.774  19.855-108.682  1.00 27.84           N  
-ATOM   8259  CA  ASP C  31     -32.719  20.631-108.048  1.00 24.86           C  
-ATOM   8260  C   ASP C  31     -33.025  20.807-106.572  1.00 27.96           C  
-ATOM   8261  O   ASP C  31     -32.132  20.714-105.733  1.00 33.82           O  
-ATOM   8262  CB  ASP C  31     -32.561  21.993-108.717  1.00 29.62           C  
-ATOM   8263  CG  ASP C  31     -31.573  22.886-107.992  1.00 37.44           C  
-ATOM   8264  OD1 ASP C  31     -30.465  22.413-107.655  1.00 31.80           O  
-ATOM   8265  OD2 ASP C  31     -31.919  24.061-107.751  1.00 30.44           O  
-ATOM   8266  N   PHE C  32     -34.294  21.051-106.255  1.00 33.74           N  
-ATOM   8267  CA  PHE C  32     -34.700  21.194-104.861  1.00 34.17           C  
-ATOM   8268  C   PHE C  32     -34.540  19.882-104.101  1.00 33.62           C  
-ATOM   8269  O   PHE C  32     -34.127  19.881-102.943  1.00 33.67           O  
-ATOM   8270  CB  PHE C  32     -36.140  21.698-104.763  1.00 34.65           C  
-ATOM   8271  CG  PHE C  32     -36.249  23.194-104.765  1.00 34.27           C  
-ATOM   8272  CD1 PHE C  32     -36.273  23.904-103.575  1.00 43.71           C  
-ATOM   8273  CD2 PHE C  32     -36.299  23.894-105.957  1.00 47.67           C  
-ATOM   8274  CE1 PHE C  32     -36.361  25.286-103.577  1.00 54.21           C  
-ATOM   8275  CE2 PHE C  32     -36.387  25.277-105.966  1.00 54.85           C  
-ATOM   8276  CZ  PHE C  32     -36.417  25.973-104.774  1.00 52.65           C  
-ATOM   8277  N   LYS C  33     -34.857  18.769-104.756  1.00 33.68           N  
-ATOM   8278  CA  LYS C  33     -34.668  17.457-104.147  1.00 38.19           C  
-ATOM   8279  C   LYS C  33     -33.187  17.224-103.859  1.00 35.47           C  
-ATOM   8280  O   LYS C  33     -32.819  16.729-102.791  1.00 40.94           O  
-ATOM   8281  CB  LYS C  33     -35.218  16.348-105.050  1.00 27.57           C  
-ATOM   8282  CG  LYS C  33     -35.187  14.966-104.410  1.00 27.92           C  
-ATOM   8283  CD  LYS C  33     -36.146  13.993-105.087  1.00 31.91           C  
-ATOM   8284  CE  LYS C  33     -35.625  13.519-106.433  1.00 43.76           C  
-ATOM   8285  NZ  LYS C  33     -36.439  12.387-106.966  1.00 43.95           N  
-ATOM   8286  N   HIS C  34     -32.349  17.594-104.822  1.00 30.18           N  
-ATOM   8287  CA  HIS C  34     -30.899  17.517-104.685  1.00 35.77           C  
-ATOM   8288  C   HIS C  34     -30.422  18.305-103.472  1.00 31.89           C  
-ATOM   8289  O   HIS C  34     -29.743  17.763-102.603  1.00 33.59           O  
-ATOM   8290  CB  HIS C  34     -30.214  18.036-105.956  1.00 32.92           C  
-ATOM   8291  CG  HIS C  34     -28.757  18.339-105.782  1.00 28.65           C  
-ATOM   8292  ND1 HIS C  34     -27.781  17.369-105.839  1.00 35.44           N  
-ATOM   8293  CD2 HIS C  34     -28.112  19.508-105.554  1.00 30.81           C  
-ATOM   8294  CE1 HIS C  34     -26.597  17.926-105.653  1.00 31.97           C  
-ATOM   8295  NE2 HIS C  34     -26.771  19.223-105.477  1.00 29.10           N  
-ATOM   8296  N   PHE C  35     -30.788  19.582-103.422  1.00 32.61           N  
-ATOM   8297  CA  PHE C  35     -30.415  20.466-102.318  1.00 32.45           C  
-ATOM   8298  C   PHE C  35     -30.843  19.883-100.969  1.00 35.05           C  
-ATOM   8299  O   PHE C  35     -30.037  19.787-100.038  1.00 38.03           O  
-ATOM   8300  CB  PHE C  35     -31.030  21.856-102.532  1.00 31.96           C  
-ATOM   8301  CG  PHE C  35     -30.840  22.798-101.375  1.00 30.24           C  
-ATOM   8302  CD1 PHE C  35     -29.669  23.522-101.236  1.00 30.84           C  
-ATOM   8303  CD2 PHE C  35     -31.844  22.971-100.437  1.00 30.97           C  
-ATOM   8304  CE1 PHE C  35     -29.496  24.393-100.175  1.00 30.43           C  
-ATOM   8305  CE2 PHE C  35     -31.678  23.839 -99.373  1.00 34.34           C  
-ATOM   8306  CZ  PHE C  35     -30.502  24.552 -99.242  1.00 29.95           C  
-ATOM   8307  N   SER C  36     -32.111  19.485-100.885  1.00 34.88           N  
-ATOM   8308  CA  SER C  36     -32.662  18.879 -99.678  1.00 33.77           C  
-ATOM   8309  C   SER C  36     -31.863  17.665 -99.219  1.00 38.32           C  
-ATOM   8310  O   SER C  36     -31.398  17.617 -98.075  1.00 43.16           O  
-ATOM   8311  CB  SER C  36     -34.114  18.468 -99.900  1.00 42.94           C  
-ATOM   8312  OG  SER C  36     -34.551  17.647 -98.830  1.00 47.89           O  
-ATOM   8313  N   ARG C  37     -31.700  16.690-100.109  1.00 36.63           N  
-ATOM   8314  CA  ARG C  37     -30.986  15.469 -99.757  1.00 40.39           C  
-ATOM   8315  C   ARG C  37     -29.552  15.761 -99.321  1.00 38.28           C  
-ATOM   8316  O   ARG C  37     -29.115  15.307 -98.261  1.00 47.52           O  
-ATOM   8317  CB  ARG C  37     -30.992  14.488-100.927  1.00 41.52           C  
-ATOM   8318  CG  ARG C  37     -31.014  13.042-100.476  1.00 55.20           C  
-ATOM   8319  CD  ARG C  37     -32.380  12.411-100.705  1.00 57.66           C  
-ATOM   8320  NE  ARG C  37     -33.477  13.315-100.370  1.00 56.40           N  
-ATOM   8321  CZ  ARG C  37     -34.747  13.113-100.710  1.00 61.41           C  
-ATOM   8322  NH1 ARG C  37     -35.671  13.996-100.358  1.00 68.74           N  
-ATOM   8323  NH2 ARG C  37     -35.097  12.036-101.404  1.00 41.04           N  
-ATOM   8324  N   VAL C  38     -28.836  16.535-100.132  1.00 32.49           N  
-ATOM   8325  CA  VAL C  38     -27.443  16.873 -99.851  1.00 31.01           C  
-ATOM   8326  C   VAL C  38     -27.274  17.567 -98.503  1.00 29.58           C  
-ATOM   8327  O   VAL C  38     -26.392  17.205 -97.727  1.00 31.91           O  
-ATOM   8328  CB  VAL C  38     -26.846  17.772-100.954  1.00 32.74           C  
-ATOM   8329  CG1 VAL C  38     -25.503  18.341-100.518  1.00 21.44           C  
-ATOM   8330  CG2 VAL C  38     -26.697  16.986-102.243  1.00 36.04           C  
-ATOM   8331  N   THR C  39     -28.127  18.546 -98.215  1.00 30.39           N  
-ATOM   8332  CA  THR C  39     -27.990  19.304 -96.976  1.00 32.66           C  
-ATOM   8333  C   THR C  39     -28.539  18.561 -95.751  1.00 37.11           C  
-ATOM   8334  O   THR C  39     -28.189  18.901 -94.618  1.00 36.32           O  
-ATOM   8335  CB  THR C  39     -28.684  20.684 -97.071  1.00 26.72           C  
-ATOM   8336  OG1 THR C  39     -29.994  20.539 -97.633  1.00 33.28           O  
-ATOM   8337  CG2 THR C  39     -27.872  21.641 -97.938  1.00 19.40           C  
-ATOM   8338  N   LYS C  40     -29.383  17.551 -95.960  1.00 34.24           N  
-ATOM   8339  CA  LYS C  40     -29.995  16.863 -94.819  1.00 34.00           C  
-ATOM   8340  C   LYS C  40     -29.331  15.540 -94.431  1.00 40.79           C  
-ATOM   8341  O   LYS C  40     -29.102  15.291 -93.247  1.00 40.98           O  
-ATOM   8342  CB  LYS C  40     -31.480  16.615 -95.081  1.00 25.10           C  
-ATOM   8343  CG  LYS C  40     -32.344  17.847 -94.883  1.00 33.59           C  
-ATOM   8344  CD  LYS C  40     -33.741  17.497 -94.388  1.00 35.01           C  
-ATOM   8345  CE  LYS C  40     -34.477  16.590 -95.358  1.00 37.98           C  
-ATOM   8346  NZ  LYS C  40     -35.862  16.294 -94.895  1.00 41.46           N  
-ATOM   8347  N   THR C  41     -29.022  14.699 -95.415  1.00 42.15           N  
-ATOM   8348  CA  THR C  41     -28.600  13.325 -95.131  1.00 43.93           C  
-ATOM   8349  C   THR C  41     -27.318  13.208 -94.305  1.00 45.37           C  
-ATOM   8350  O   THR C  41     -26.242  13.645 -94.717  1.00 36.59           O  
-ATOM   8351  CB  THR C  41     -28.403  12.513 -96.427  1.00 55.36           C  
-ATOM   8352  OG1 THR C  41     -27.482  13.189 -97.293  1.00 56.49           O  
-ATOM   8353  CG2 THR C  41     -29.733  12.320 -97.146  1.00 50.88           C  
-ATOM   8354  N   THR C  42     -27.470  12.600 -93.133  1.00 53.45           N  
-ATOM   8355  CA  THR C  42     -26.376  12.314 -92.216  1.00 57.63           C  
-ATOM   8356  C   THR C  42     -26.370  10.813 -91.938  1.00 65.86           C  
-ATOM   8357  O   THR C  42     -27.437  10.221 -91.767  1.00 64.50           O  
-ATOM   8358  CB  THR C  42     -26.532  13.108 -90.894  1.00 63.97           C  
-ATOM   8359  OG1 THR C  42     -26.442  14.512 -91.164  1.00 55.63           O  
-ATOM   8360  CG2 THR C  42     -25.463  12.722 -89.881  1.00 77.80           C  
-ATOM   8361  N   PRO C  43     -25.178  10.188 -91.913  1.00 65.39           N  
-ATOM   8362  CA  PRO C  43     -25.065   8.757 -91.600  1.00 70.35           C  
-ATOM   8363  C   PRO C  43     -25.754   8.368 -90.291  1.00 80.43           C  
-ATOM   8364  O   PRO C  43     -25.454   8.949 -89.248  1.00 71.11           O  
-ATOM   8365  CB  PRO C  43     -23.547   8.535 -91.500  1.00 61.52           C  
-ATOM   8366  CG  PRO C  43     -22.941   9.911 -91.433  1.00 68.03           C  
-ATOM   8367  CD  PRO C  43     -23.865  10.776 -92.223  1.00 61.79           C  
-ATOM   8368  N   ALA C  46     -27.161   9.949 -87.266  1.00 70.80           N  
-ATOM   8369  CA  ALA C  46     -27.541   9.262 -86.037  1.00 84.21           C  
-ATOM   8370  C   ALA C  46     -27.633  10.238 -84.873  1.00 71.97           C  
-ATOM   8371  O   ALA C  46     -28.725  10.592 -84.424  1.00 59.19           O  
-ATOM   8372  CB  ALA C  46     -26.546   8.154 -85.718  1.00 72.58           C  
-ATOM   8373  N   SER C  47     -26.473  10.672 -84.394  1.00 67.10           N  
-ATOM   8374  CA  SER C  47     -26.397  11.572 -83.251  1.00 74.99           C  
-ATOM   8375  C   SER C  47     -26.397  13.038 -83.673  1.00 73.39           C  
-ATOM   8376  O   SER C  47     -26.930  13.897 -82.967  1.00 52.85           O  
-ATOM   8377  CB  SER C  47     -25.142  11.271 -82.427  1.00 77.75           C  
-ATOM   8378  OG  SER C  47     -23.971  11.338 -83.228  1.00 54.65           O  
-ATOM   8379  N   ARG C  48     -25.804  13.318 -84.830  1.00 73.67           N  
-ATOM   8380  CA  ARG C  48     -25.569  14.695 -85.253  1.00 55.69           C  
-ATOM   8381  C   ARG C  48     -26.479  15.131 -86.396  1.00 57.70           C  
-ATOM   8382  O   ARG C  48     -27.192  14.322 -86.989  1.00 63.64           O  
-ATOM   8383  CB  ARG C  48     -24.106  14.865 -85.667  1.00 48.26           C  
-ATOM   8384  CG  ARG C  48     -23.130  14.123 -84.769  1.00 59.20           C  
-ATOM   8385  CD  ARG C  48     -21.764  13.996 -85.419  1.00 58.10           C  
-ATOM   8386  NE  ARG C  48     -20.950  15.191 -85.225  1.00 63.72           N  
-ATOM   8387  CZ  ARG C  48     -19.875  15.242 -84.444  1.00 58.76           C  
-ATOM   8388  NH1 ARG C  48     -19.478  14.159 -83.790  1.00 57.88           N  
-ATOM   8389  NH2 ARG C  48     -19.191  16.372 -84.324  1.00 59.57           N  
-ATOM   8390  N   PHE C  74     -26.441  16.426 -86.692  1.00 51.72           N  
-ATOM   8391  CA  PHE C  74     -27.177  16.995 -87.814  1.00 47.90           C  
-ATOM   8392  C   PHE C  74     -26.253  17.899 -88.621  1.00 50.73           C  
-ATOM   8393  O   PHE C  74     -25.129  18.171 -88.204  1.00 48.08           O  
-ATOM   8394  CB  PHE C  74     -28.398  17.774 -87.325  1.00 43.99           C  
-ATOM   8395  CG  PHE C  74     -28.131  18.618 -86.110  1.00 41.86           C  
-ATOM   8396  CD1 PHE C  74     -27.430  19.808 -86.213  1.00 36.31           C  
-ATOM   8397  CD2 PHE C  74     -28.589  18.223 -84.864  1.00 49.53           C  
-ATOM   8398  CE1 PHE C  74     -27.187  20.583 -85.097  1.00 38.21           C  
-ATOM   8399  CE2 PHE C  74     -28.348  18.996 -83.745  1.00 40.06           C  
-ATOM   8400  CZ  PHE C  74     -27.646  20.176 -83.862  1.00 37.79           C  
-ATOM   8401  N   ASN C  75     -26.724  18.364 -89.773  1.00 50.55           N  
-ATOM   8402  CA  ASN C  75     -25.924  19.253 -90.608  1.00 43.81           C  
-ATOM   8403  C   ASN C  75     -26.282  20.720 -90.396  1.00 39.90           C  
-ATOM   8404  O   ASN C  75     -27.384  21.048 -89.953  1.00 41.52           O  
-ATOM   8405  CB  ASN C  75     -26.082  18.885 -92.084  1.00 39.06           C  
-ATOM   8406  CG  ASN C  75     -25.374  17.595 -92.440  1.00 40.36           C  
-ATOM   8407  OD1 ASN C  75     -24.259  17.339 -91.983  1.00 45.91           O  
-ATOM   8408  ND2 ASN C  75     -26.020  16.772 -93.257  1.00 46.93           N  
-ATOM   8409  N   ALA C  76     -25.341  21.601 -90.711  1.00 34.76           N  
-ATOM   8410  CA  ALA C  76     -25.561  23.031 -90.557  1.00 35.02           C  
-ATOM   8411  C   ALA C  76     -25.550  23.730 -91.910  1.00 35.57           C  
-ATOM   8412  O   ALA C  76     -24.686  23.473 -92.749  1.00 37.17           O  
-ATOM   8413  CB  ALA C  76     -24.511  23.637 -89.635  1.00 36.36           C  
-ATOM   8414  N   VAL C  77     -26.524  24.606 -92.120  1.00 33.88           N  
-ATOM   8415  CA  VAL C  77     -26.567  25.419 -93.325  1.00 25.77           C  
-ATOM   8416  C   VAL C  77     -26.374  26.892 -92.970  1.00 28.42           C  
-ATOM   8417  O   VAL C  77     -27.114  27.453 -92.161  1.00 30.65           O  
-ATOM   8418  CB  VAL C  77     -27.888  25.226 -94.097  1.00 16.53           C  
-ATOM   8419  CG1 VAL C  77     -27.851  23.924 -94.875  1.00 26.45           C  
-ATOM   8420  CG2 VAL C  77     -29.076  25.245 -93.149  1.00 21.63           C  
-ATOM   8421  N   VAL C  78     -25.359  27.507 -93.565  1.00 26.83           N  
-ATOM   8422  CA  VAL C  78     -25.067  28.911 -93.314  1.00 24.59           C  
-ATOM   8423  C   VAL C  78     -25.464  29.758 -94.520  1.00 32.42           C  
-ATOM   8424  O   VAL C  78     -25.065  29.469 -95.650  1.00 28.91           O  
-ATOM   8425  CB  VAL C  78     -23.579  29.129 -92.995  1.00 20.29           C  
-ATOM   8426  CG1 VAL C  78     -23.336  30.568 -92.577  1.00 20.02           C  
-ATOM   8427  CG2 VAL C  78     -23.131  28.174 -91.902  1.00 15.43           C  
-ATOM   8428  N   MET C  79     -26.256  30.798 -94.277  1.00 34.88           N  
-ATOM   8429  CA  MET C  79     -26.749  31.639 -95.359  1.00 24.20           C  
-ATOM   8430  C   MET C  79     -26.677  33.121 -95.014  1.00 26.89           C  
-ATOM   8431  O   MET C  79     -26.544  33.491 -93.847  1.00 24.48           O  
-ATOM   8432  CB  MET C  79     -28.186  31.259 -95.713  1.00 23.29           C  
-ATOM   8433  CG  MET C  79     -29.213  31.722 -94.702  1.00 21.38           C  
-ATOM   8434  SD  MET C  79     -30.782  30.857 -94.882  1.00 29.21           S  
-ATOM   8435  CE  MET C  79     -30.329  29.232 -94.279  1.00 21.97           C  
-ATOM   8436  N   GLY C  80     -26.758  33.962 -96.041  1.00 30.58           N  
-ATOM   8437  CA  GLY C  80     -26.812  35.400 -95.855  1.00 28.93           C  
-ATOM   8438  C   GLY C  80     -28.224  35.855 -95.535  1.00 36.93           C  
-ATOM   8439  O   GLY C  80     -29.184  35.107 -95.743  1.00 36.01           O  
-ATOM   8440  N   ARG C  81     -28.355  37.079 -95.032  1.00 25.74           N  
-ATOM   8441  CA  ARG C  81     -29.651  37.596 -94.607  1.00 25.84           C  
-ATOM   8442  C   ARG C  81     -30.664  37.633 -95.750  1.00 28.51           C  
-ATOM   8443  O   ARG C  81     -31.838  37.294 -95.572  1.00 38.10           O  
-ATOM   8444  CB  ARG C  81     -29.482  38.991 -94.004  1.00 25.83           C  
-ATOM   8445  CG  ARG C  81     -30.744  39.570 -93.393  1.00 31.78           C  
-ATOM   8446  CD  ARG C  81     -31.308  40.680 -94.255  1.00 28.65           C  
-ATOM   8447  NE  ARG C  81     -30.335  41.745 -94.467  1.00 26.98           N  
-ATOM   8448  CZ  ARG C  81     -30.475  42.716 -95.363  1.00 26.67           C  
-ATOM   8449  NH1 ARG C  81     -29.536  43.642 -95.487  1.00 31.99           N  
-ATOM   8450  NH2 ARG C  81     -31.553  42.758 -96.136  1.00 24.84           N  
-ATOM   8451  N   LYS C  82     -30.197  38.039 -96.926  1.00 31.02           N  
-ATOM   8452  CA  LYS C  82     -31.067  38.179 -98.087  1.00 32.94           C  
-ATOM   8453  C   LYS C  82     -31.557  36.828 -98.598  1.00 34.56           C  
-ATOM   8454  O   LYS C  82     -32.634  36.736 -99.185  1.00 42.40           O  
-ATOM   8455  CB  LYS C  82     -30.351  38.936 -99.209  1.00 30.80           C  
-ATOM   8456  CG  LYS C  82     -30.070  40.391 -98.872  1.00 26.01           C  
-ATOM   8457  CD  LYS C  82     -29.541  41.160-100.071  1.00 32.74           C  
-ATOM   8458  CE  LYS C  82     -29.374  42.633 -99.725  1.00 34.87           C  
-ATOM   8459  NZ  LYS C  82     -28.939  43.446-100.892  1.00 34.14           N  
-ATOM   8460  N   THR C  83     -30.768  35.782 -98.381  1.00 29.12           N  
-ATOM   8461  CA  THR C  83     -31.180  34.444 -98.783  1.00 26.76           C  
-ATOM   8462  C   THR C  83     -32.311  33.969 -97.875  1.00 33.18           C  
-ATOM   8463  O   THR C  83     -33.334  33.449 -98.339  1.00 41.31           O  
-ATOM   8464  CB  THR C  83     -30.000  33.450 -98.735  1.00 28.88           C  
-ATOM   8465  OG1 THR C  83     -29.001  33.840 -99.686  1.00 25.35           O  
-ATOM   8466  CG2 THR C  83     -30.469  32.047 -99.057  1.00 29.42           C  
-ATOM   8467  N   TRP C  84     -32.114  34.163 -96.575  1.00 31.91           N  
-ATOM   8468  CA  TRP C  84     -33.143  33.894 -95.581  1.00 31.51           C  
-ATOM   8469  C   TRP C  84     -34.430  34.637 -95.905  1.00 28.03           C  
-ATOM   8470  O   TRP C  84     -35.518  34.074 -95.809  1.00 29.61           O  
-ATOM   8471  CB  TRP C  84     -32.659  34.288 -94.185  1.00 29.96           C  
-ATOM   8472  CG  TRP C  84     -33.734  34.214 -93.143  1.00 33.16           C  
-ATOM   8473  CD1 TRP C  84     -34.595  35.210 -92.775  1.00 31.10           C  
-ATOM   8474  CD2 TRP C  84     -34.070  33.081 -92.344  1.00 29.56           C  
-ATOM   8475  NE1 TRP C  84     -35.444  34.764 -91.792  1.00 25.99           N  
-ATOM   8476  CE2 TRP C  84     -35.140  33.456 -91.508  1.00 25.28           C  
-ATOM   8477  CE3 TRP C  84     -33.569  31.778 -92.249  1.00 22.30           C  
-ATOM   8478  CZ2 TRP C  84     -35.717  32.583 -90.594  1.00 28.83           C  
-ATOM   8479  CZ3 TRP C  84     -34.143  30.911 -91.340  1.00 26.73           C  
-ATOM   8480  CH2 TRP C  84     -35.203  31.316 -90.525  1.00 34.99           C  
-ATOM   8481  N   GLU C  85     -34.303  35.904 -96.285  1.00 28.60           N  
-ATOM   8482  CA  GLU C  85     -35.476  36.696 -96.625  1.00 32.08           C  
-ATOM   8483  C   GLU C  85     -36.078  36.258 -97.956  1.00 31.01           C  
-ATOM   8484  O   GLU C  85     -37.258  36.510 -98.226  1.00 34.01           O  
-ATOM   8485  CB  GLU C  85     -35.123  38.185 -96.662  1.00 36.01           C  
-ATOM   8486  CG  GLU C  85     -34.762  38.757 -95.298  1.00 35.17           C  
-ATOM   8487  CD  GLU C  85     -34.492  40.249 -95.335  1.00 44.85           C  
-ATOM   8488  OE1 GLU C  85     -34.284  40.797 -96.440  1.00 41.95           O  
-ATOM   8489  OE2 GLU C  85     -34.484  40.873 -94.251  1.00 44.22           O  
-ATOM   8490  N   SER C  86     -35.267  35.602 -98.784  1.00 29.65           N  
-ATOM   8491  CA  SER C  86     -35.721  35.165-100.100  1.00 31.32           C  
-ATOM   8492  C   SER C  86     -36.530  33.881 -99.990  1.00 27.30           C  
-ATOM   8493  O   SER C  86     -37.495  33.686-100.721  1.00 34.40           O  
-ATOM   8494  CB  SER C  86     -34.536  34.970-101.057  1.00 38.17           C  
-ATOM   8495  OG  SER C  86     -33.762  33.829-100.718  1.00 52.88           O  
-ATOM   8496  N   MET C  87     -36.132  33.011 -99.068  1.00 28.82           N  
-ATOM   8497  CA  MET C  87     -36.865  31.774 -98.833  1.00 34.47           C  
-ATOM   8498  C   MET C  87     -38.285  32.065 -98.351  1.00 41.92           C  
-ATOM   8499  O   MET C  87     -38.514  33.037 -97.628  1.00 42.49           O  
-ATOM   8500  CB  MET C  87     -36.133  30.897 -97.816  1.00 32.41           C  
-ATOM   8501  CG  MET C  87     -34.798  30.351 -98.304  1.00 35.26           C  
-ATOM   8502  SD  MET C  87     -33.941  29.389 -97.040  1.00 37.52           S  
-ATOM   8503  CE  MET C  87     -35.262  28.312 -96.501  1.00 34.51           C  
-ATOM   8504  N   PRO C  88     -39.250  31.225 -98.763  1.00 45.52           N  
-ATOM   8505  CA  PRO C  88     -40.643  31.369 -98.325  1.00 49.62           C  
-ATOM   8506  C   PRO C  88     -40.797  31.127 -96.824  1.00 51.97           C  
-ATOM   8507  O   PRO C  88     -40.008  30.382 -96.243  1.00 50.14           O  
-ATOM   8508  CB  PRO C  88     -41.382  30.296 -99.138  1.00 39.69           C  
-ATOM   8509  CG  PRO C  88     -40.326  29.310 -99.515  1.00 41.63           C  
-ATOM   8510  CD  PRO C  88     -39.089  30.121 -99.723  1.00 37.37           C  
-ATOM   8511  N   ARG C  89     -41.797  31.758 -96.214  1.00 54.46           N  
-ATOM   8512  CA  ARG C  89     -42.008  31.684 -94.770  1.00 51.77           C  
-ATOM   8513  C   ARG C  89     -42.147  30.252 -94.262  1.00 51.84           C  
-ATOM   8514  O   ARG C  89     -41.491  29.861 -93.297  1.00 50.88           O  
-ATOM   8515  CB  ARG C  89     -43.257  32.477 -94.378  1.00 60.19           C  
-ATOM   8516  CG  ARG C  89     -43.201  33.963 -94.696  1.00 75.14           C  
-ATOM   8517  CD  ARG C  89     -42.633  34.768 -93.536  1.00 85.26           C  
-ATOM   8518  NE  ARG C  89     -43.202  36.113 -93.486  1.00 86.19           N  
-ATOM   8519  CZ  ARG C  89     -42.697  37.168 -94.117  1.00 85.77           C  
-ATOM   8520  NH1 ARG C  89     -41.601  37.043 -94.853  1.00 82.34           N  
-ATOM   8521  NH2 ARG C  89     -43.288  38.350 -94.013  1.00 81.49           N  
-ATOM   8522  N   LYS C  90     -43.001  29.476 -94.922  1.00 54.66           N  
-ATOM   8523  CA  LYS C  90     -43.369  28.145 -94.447  1.00 54.43           C  
-ATOM   8524  C   LYS C  90     -42.201  27.162 -94.450  1.00 49.21           C  
-ATOM   8525  O   LYS C  90     -42.214  26.171 -93.722  1.00 56.93           O  
-ATOM   8526  CB  LYS C  90     -44.514  27.585 -95.297  1.00 59.27           C  
-ATOM   8527  CG  LYS C  90     -44.096  27.132 -96.690  1.00 74.76           C  
-ATOM   8528  CD  LYS C  90     -44.978  27.738 -97.774  1.00 90.80           C  
-ATOM   8529  CE  LYS C  90     -44.742  29.236 -97.920  1.00 81.12           C  
-ATOM   8530  NZ  LYS C  90     -45.436  29.790 -99.118  1.00 66.52           N  
-ATOM   8531  N   PHE C  91     -41.193  27.438 -95.269  1.00 48.05           N  
-ATOM   8532  CA  PHE C  91     -40.074  26.519 -95.430  1.00 48.90           C  
-ATOM   8533  C   PHE C  91     -38.901  26.855 -94.517  1.00 48.23           C  
-ATOM   8534  O   PHE C  91     -38.009  26.030 -94.317  1.00 47.37           O  
-ATOM   8535  CB  PHE C  91     -39.610  26.506 -96.888  1.00 58.43           C  
-ATOM   8536  CG  PHE C  91     -40.294  25.468 -97.732  1.00 77.87           C  
-ATOM   8537  CD1 PHE C  91     -40.541  24.202 -97.226  1.00 87.11           C  
-ATOM   8538  CD2 PHE C  91     -40.691  25.757 -99.028  1.00 72.73           C  
-ATOM   8539  CE1 PHE C  91     -41.167  23.241 -97.997  1.00 81.28           C  
-ATOM   8540  CE2 PHE C  91     -41.319  24.798 -99.805  1.00 83.75           C  
-ATOM   8541  CZ  PHE C  91     -41.557  23.539 -99.287  1.00 84.04           C  
-ATOM   8542  N   ARG C  92     -38.900  28.062 -93.961  1.00 45.80           N  
-ATOM   8543  CA  ARG C  92     -37.778  28.496 -93.138  1.00 36.69           C  
-ATOM   8544  C   ARG C  92     -38.142  28.545 -91.657  1.00 34.17           C  
-ATOM   8545  O   ARG C  92     -39.259  28.912 -91.297  1.00 46.31           O  
-ATOM   8546  CB  ARG C  92     -37.265  29.860 -93.608  1.00 38.31           C  
-ATOM   8547  CG  ARG C  92     -38.149  31.038 -93.256  1.00 37.68           C  
-ATOM   8548  CD  ARG C  92     -37.715  32.275 -94.021  1.00 37.23           C  
-ATOM   8549  NE  ARG C  92     -38.405  33.475 -93.562  1.00 45.23           N  
-ATOM   8550  CZ  ARG C  92     -38.584  34.563 -94.304  1.00 47.73           C  
-ATOM   8551  NH1 ARG C  92     -39.220  35.611 -93.801  1.00 58.57           N  
-ATOM   8552  NH2 ARG C  92     -38.134  34.602 -95.550  1.00 43.84           N  
-ATOM   8553  N   PRO C  93     -37.196  28.157 -90.787  1.00 33.73           N  
-ATOM   8554  CA  PRO C  93     -35.859  27.657 -91.126  1.00 33.80           C  
-ATOM   8555  C   PRO C  93     -35.892  26.262 -91.745  1.00 39.10           C  
-ATOM   8556  O   PRO C  93     -36.872  25.537 -91.566  1.00 50.15           O  
-ATOM   8557  CB  PRO C  93     -35.147  27.630 -89.774  1.00 31.51           C  
-ATOM   8558  CG  PRO C  93     -36.241  27.444 -88.788  1.00 30.54           C  
-ATOM   8559  CD  PRO C  93     -37.397  28.230 -89.330  1.00 39.10           C  
-ATOM   8560  N   LEU C  94     -34.845  25.909 -92.481  1.00 32.61           N  
-ATOM   8561  CA  LEU C  94     -34.761  24.598 -93.108  1.00 39.26           C  
-ATOM   8562  C   LEU C  94     -34.789  23.504 -92.046  1.00 35.84           C  
-ATOM   8563  O   LEU C  94     -33.933  23.461 -91.163  1.00 38.19           O  
-ATOM   8564  CB  LEU C  94     -33.497  24.498 -93.967  1.00 46.35           C  
-ATOM   8565  CG  LEU C  94     -33.499  25.316 -95.263  1.00 30.97           C  
-ATOM   8566  CD1 LEU C  94     -32.122  25.334 -95.908  1.00 27.17           C  
-ATOM   8567  CD2 LEU C  94     -34.534  24.776 -96.240  1.00 33.74           C  
-ATOM   8568  N   VAL C  95     -35.789  22.632 -92.134  1.00 35.16           N  
-ATOM   8569  CA  VAL C  95     -36.018  21.602 -91.122  1.00 42.32           C  
-ATOM   8570  C   VAL C  95     -34.869  20.600 -91.004  1.00 44.65           C  
-ATOM   8571  O   VAL C  95     -34.219  20.263 -91.996  1.00 43.49           O  
-ATOM   8572  CB  VAL C  95     -37.315  20.824 -91.408  1.00 35.32           C  
-ATOM   8573  CG1 VAL C  95     -38.529  21.689 -91.104  1.00 36.83           C  
-ATOM   8574  CG2 VAL C  95     -37.337  20.341 -92.851  1.00 36.33           C  
-ATOM   8575  N   ASP C  96     -34.632  20.138 -89.777  1.00 43.60           N  
-ATOM   8576  CA  ASP C  96     -33.615  19.129 -89.473  1.00 33.77           C  
-ATOM   8577  C   ASP C  96     -32.207  19.576 -89.861  1.00 31.84           C  
-ATOM   8578  O   ASP C  96     -31.330  18.748 -90.108  1.00 34.83           O  
-ATOM   8579  CB  ASP C  96     -33.955  17.807 -90.163  1.00 33.33           C  
-ATOM   8580  CG  ASP C  96     -35.334  17.299 -89.791  1.00 45.69           C  
-ATOM   8581  OD1 ASP C  96     -35.776  17.559 -88.649  1.00 43.68           O  
-ATOM   8582  OD2 ASP C  96     -35.978  16.646 -90.639  1.00 40.38           O  
-ATOM   8583  N   ARG C  97     -32.003  20.889 -89.906  1.00 31.45           N  
-ATOM   8584  CA  ARG C  97     -30.693  21.474 -90.172  1.00 28.68           C  
-ATOM   8585  C   ARG C  97     -30.502  22.716 -89.314  1.00 28.50           C  
-ATOM   8586  O   ARG C  97     -31.403  23.547 -89.202  1.00 26.35           O  
-ATOM   8587  CB  ARG C  97     -30.538  21.832 -91.650  1.00 25.62           C  
-ATOM   8588  CG  ARG C  97     -30.317  20.642 -92.571  1.00 27.35           C  
-ATOM   8589  CD  ARG C  97     -30.804  20.946 -93.978  1.00 27.47           C  
-ATOM   8590  NE  ARG C  97     -32.257  21.100 -94.021  1.00 37.16           N  
-ATOM   8591  CZ  ARG C  97     -32.964  21.286 -95.131  1.00 29.66           C  
-ATOM   8592  NH1 ARG C  97     -32.357  21.345 -96.308  1.00 29.21           N  
-ATOM   8593  NH2 ARG C  97     -34.283  21.414 -95.062  1.00 26.11           N  
-ATOM   8594  N   LEU C  98     -29.334  22.840 -88.699  1.00 29.52           N  
-ATOM   8595  CA  LEU C  98     -29.027  24.032 -87.925  1.00 26.69           C  
-ATOM   8596  C   LEU C  98     -28.891  25.220 -88.861  1.00 29.02           C  
-ATOM   8597  O   LEU C  98     -28.000  25.254 -89.707  1.00 30.10           O  
-ATOM   8598  CB  LEU C  98     -27.746  23.849 -87.113  1.00 30.94           C  
-ATOM   8599  CG  LEU C  98     -27.225  25.129 -86.458  1.00 33.89           C  
-ATOM   8600  CD1 LEU C  98     -28.180  25.602 -85.373  1.00 33.42           C  
-ATOM   8601  CD2 LEU C  98     -25.824  24.929 -85.902  1.00 36.59           C  
-ATOM   8602  N   ASN C  99     -29.781  26.192 -88.717  1.00 26.88           N  
-ATOM   8603  CA  ASN C  99     -29.713  27.387 -89.546  1.00 26.45           C  
-ATOM   8604  C   ASN C  99     -28.888  28.502 -88.909  1.00 29.75           C  
-ATOM   8605  O   ASN C  99     -29.169  28.953 -87.793  1.00 35.88           O  
-ATOM   8606  CB  ASN C  99     -31.119  27.900 -89.868  1.00 31.11           C  
-ATOM   8607  CG  ASN C  99     -31.843  27.023 -90.873  1.00 31.71           C  
-ATOM   8608  OD1 ASN C  99     -31.842  25.797 -90.761  1.00 39.53           O  
-ATOM   8609  ND2 ASN C  99     -32.457  27.649 -91.870  1.00 21.13           N  
-ATOM   8610  N   ILE C 100     -27.860  28.934 -89.629  1.00 23.13           N  
-ATOM   8611  CA  ILE C 100     -27.068  30.080 -89.215  1.00 24.95           C  
-ATOM   8612  C   ILE C 100     -27.192  31.172 -90.261  1.00 26.10           C  
-ATOM   8613  O   ILE C 100     -26.959  30.937 -91.444  1.00 30.22           O  
-ATOM   8614  CB  ILE C 100     -25.584  29.717 -89.014  1.00 21.80           C  
-ATOM   8615  CG1 ILE C 100     -25.433  28.680 -87.900  1.00 22.76           C  
-ATOM   8616  CG2 ILE C 100     -24.770  30.963 -88.696  1.00 23.56           C  
-ATOM   8617  CD1 ILE C 100     -23.997  28.365 -87.563  1.00 16.50           C  
-ATOM   8618  N   VAL C 101     -27.572  32.366 -89.822  1.00 27.22           N  
-ATOM   8619  CA  VAL C 101     -27.719  33.492 -90.727  1.00 22.79           C  
-ATOM   8620  C   VAL C 101     -26.664  34.550 -90.442  1.00 23.01           C  
-ATOM   8621  O   VAL C 101     -26.516  35.003 -89.309  1.00 22.23           O  
-ATOM   8622  CB  VAL C 101     -29.113  34.132 -90.620  1.00 19.02           C  
-ATOM   8623  CG1 VAL C 101     -29.283  35.199 -91.689  1.00 23.83           C  
-ATOM   8624  CG2 VAL C 101     -30.200  33.072 -90.739  1.00 17.20           C  
-ATOM   8625  N   VAL C 102     -25.925  34.930 -91.479  1.00 28.09           N  
-ATOM   8626  CA  VAL C 102     -24.937  35.994 -91.369  1.00 27.00           C  
-ATOM   8627  C   VAL C 102     -25.592  37.340 -91.650  1.00 35.57           C  
-ATOM   8628  O   VAL C 102     -26.040  37.601 -92.767  1.00 32.44           O  
-ATOM   8629  CB  VAL C 102     -23.757  35.784 -92.337  1.00 24.50           C  
-ATOM   8630  CG1 VAL C 102     -22.808  36.970 -92.286  1.00 24.87           C  
-ATOM   8631  CG2 VAL C 102     -23.029  34.491 -92.009  1.00 24.78           C  
-ATOM   8632  N   SER C 103     -25.654  38.184 -90.626  1.00 40.24           N  
-ATOM   8633  CA  SER C 103     -26.279  39.496 -90.746  1.00 35.58           C  
-ATOM   8634  C   SER C 103     -25.853  40.409 -89.603  1.00 41.36           C  
-ATOM   8635  O   SER C 103     -25.369  39.942 -88.571  1.00 45.84           O  
-ATOM   8636  CB  SER C 103     -27.804  39.363 -90.771  1.00 33.15           C  
-ATOM   8637  OG  SER C 103     -28.426  40.626 -90.918  1.00 35.10           O  
-ATOM   8638  N   SER C 104     -26.031  41.712 -89.792  1.00 38.33           N  
-ATOM   8639  CA  SER C 104     -25.739  42.678 -88.741  1.00 40.46           C  
-ATOM   8640  C   SER C 104     -27.000  43.439 -88.357  1.00 45.84           C  
-ATOM   8641  O   SER C 104     -27.075  44.051 -87.290  1.00 59.43           O  
-ATOM   8642  CB  SER C 104     -24.642  43.644 -89.186  1.00 38.58           C  
-ATOM   8643  OG  SER C 104     -23.394  42.978 -89.282  1.00 43.41           O  
-ATOM   8644  N   SER C 105     -27.995  43.386 -89.236  1.00 37.08           N  
-ATOM   8645  CA  SER C 105     -29.272  44.042 -88.991  1.00 45.98           C  
-ATOM   8646  C   SER C 105     -30.263  43.094 -88.316  1.00 47.28           C  
-ATOM   8647  O   SER C 105     -30.999  43.493 -87.412  1.00 44.87           O  
-ATOM   8648  CB  SER C 105     -29.851  44.585 -90.303  1.00 40.02           C  
-ATOM   8649  OG  SER C 105     -30.006  43.556 -91.261  1.00 35.00           O  
-ATOM   8650  N   LEU C 106     -30.273  41.838 -88.756  1.00 39.90           N  
-ATOM   8651  CA  LEU C 106     -31.171  40.835 -88.190  1.00 40.81           C  
-ATOM   8652  C   LEU C 106     -30.687  40.324 -86.836  1.00 43.68           C  
-ATOM   8653  O   LEU C 106     -29.496  40.369 -86.532  1.00 44.72           O  
-ATOM   8654  CB  LEU C 106     -31.337  39.656 -89.152  1.00 42.71           C  
-ATOM   8655  CG  LEU C 106     -32.523  39.738 -90.112  1.00 45.56           C  
-ATOM   8656  CD1 LEU C 106     -32.833  38.369 -90.696  1.00 36.61           C  
-ATOM   8657  CD2 LEU C 106     -33.742  40.306 -89.405  1.00 45.88           C  
-ATOM   8658  N   LYS C 107     -31.623  39.839 -86.027  1.00 36.68           N  
-ATOM   8659  CA  LYS C 107     -31.296  39.294 -84.715  1.00 39.43           C  
-ATOM   8660  C   LYS C 107     -31.978  37.958 -84.471  1.00 42.58           C  
-ATOM   8661  O   LYS C 107     -32.997  37.643 -85.089  1.00 46.80           O  
-ATOM   8662  CB  LYS C 107     -31.683  40.282 -83.610  1.00 51.25           C  
-ATOM   8663  CG  LYS C 107     -30.872  41.548 -83.597  1.00 57.42           C  
-ATOM   8664  CD  LYS C 107     -31.146  42.327 -82.333  1.00 56.20           C  
-ATOM   8665  CE  LYS C 107     -29.920  43.118 -81.931  1.00 73.11           C  
-ATOM   8666  NZ  LYS C 107     -28.764  42.220 -81.654  1.00 57.09           N  
-ATOM   8667  N   GLU C 108     -31.412  37.187 -83.551  1.00 32.32           N  
-ATOM   8668  CA  GLU C 108     -31.946  35.878 -83.210  1.00 32.79           C  
-ATOM   8669  C   GLU C 108     -33.398  35.952 -82.746  1.00 37.02           C  
-ATOM   8670  O   GLU C 108     -34.171  35.019 -82.967  1.00 46.81           O  
-ATOM   8671  CB  GLU C 108     -31.085  35.221 -82.138  1.00 39.20           C  
-ATOM   8672  CG  GLU C 108     -29.668  34.960 -82.601  1.00 43.50           C  
-ATOM   8673  CD  GLU C 108     -28.892  34.102 -81.629  1.00 47.18           C  
-ATOM   8674  OE1 GLU C 108     -29.456  33.714 -80.581  1.00 45.07           O  
-ATOM   8675  OE2 GLU C 108     -27.713  33.815 -81.920  1.00 45.89           O  
-ATOM   8676  N   GLU C 109     -33.770  37.058 -82.109  1.00 40.65           N  
-ATOM   8677  CA  GLU C 109     -35.156  37.249 -81.699  1.00 48.84           C  
-ATOM   8678  C   GLU C 109     -36.011  37.780 -82.839  1.00 41.31           C  
-ATOM   8679  O   GLU C 109     -37.223  37.558 -82.869  1.00 47.67           O  
-ATOM   8680  CB  GLU C 109     -35.240  38.184 -80.491  1.00 48.66           C  
-ATOM   8681  CG  GLU C 109     -35.407  37.452 -79.174  1.00 70.24           C  
-ATOM   8682  CD  GLU C 109     -36.548  36.440 -79.202  1.00 77.63           C  
-ATOM   8683  OE1 GLU C 109     -36.349  35.303 -78.717  1.00 67.21           O  
-ATOM   8684  OE2 GLU C 109     -37.643  36.778 -79.706  1.00 63.03           O  
-ATOM   8685  N   ASP C 110     -35.381  38.495 -83.763  1.00 36.10           N  
-ATOM   8686  CA  ASP C 110     -36.063  38.912 -84.976  1.00 34.64           C  
-ATOM   8687  C   ASP C 110     -36.528  37.674 -85.730  1.00 41.15           C  
-ATOM   8688  O   ASP C 110     -37.641  37.626 -86.249  1.00 41.52           O  
-ATOM   8689  CB  ASP C 110     -35.150  39.777 -85.853  1.00 36.67           C  
-ATOM   8690  CG  ASP C 110     -35.105  41.222 -85.399  1.00 44.45           C  
-ATOM   8691  OD1 ASP C 110     -36.159  41.726 -84.963  1.00 53.24           O  
-ATOM   8692  OD2 ASP C 110     -34.026  41.848 -85.475  1.00 40.68           O  
-ATOM   8693  N   ILE C 111     -35.672  36.660 -85.765  1.00 40.95           N  
-ATOM   8694  CA  ILE C 111     -36.013  35.413 -86.442  1.00 37.08           C  
-ATOM   8695  C   ILE C 111     -36.948  34.559 -85.582  1.00 34.76           C  
-ATOM   8696  O   ILE C 111     -37.873  33.927 -86.096  1.00 31.87           O  
-ATOM   8697  CB  ILE C 111     -34.733  34.616 -86.820  1.00 34.31           C  
-ATOM   8698  CG1 ILE C 111     -34.017  35.313 -87.980  1.00 31.68           C  
-ATOM   8699  CG2 ILE C 111     -35.067  33.184 -87.196  1.00 23.74           C  
-ATOM   8700  CD1 ILE C 111     -32.754  34.607 -88.448  1.00 30.04           C  
-ATOM   8701  N   ALA C 112     -36.719  34.563 -84.272  1.00 35.07           N  
-ATOM   8702  CA  ALA C 112     -37.513  33.755 -83.351  1.00 34.41           C  
-ATOM   8703  C   ALA C 112     -38.974  34.192 -83.304  1.00 42.81           C  
-ATOM   8704  O   ALA C 112     -39.874  33.356 -83.217  1.00 42.97           O  
-ATOM   8705  CB  ALA C 112     -36.913  33.805 -81.962  1.00 40.03           C  
-ATOM   8706  N   ALA C 113     -39.207  35.500 -83.364  1.00 42.23           N  
-ATOM   8707  CA  ALA C 113     -40.563  36.039 -83.285  1.00 43.87           C  
-ATOM   8708  C   ALA C 113     -41.258  36.035 -84.645  1.00 45.57           C  
-ATOM   8709  O   ALA C 113     -42.364  36.559 -84.790  1.00 51.42           O  
-ATOM   8710  CB  ALA C 113     -40.538  37.446 -82.709  1.00 35.88           C  
-ATOM   8711  N   GLU C 114     -40.603  35.441 -85.636  1.00 43.71           N  
-ATOM   8712  CA  GLU C 114     -41.159  35.340 -86.979  1.00 45.90           C  
-ATOM   8713  C   GLU C 114     -42.073  34.119 -87.097  1.00 49.06           C  
-ATOM   8714  O   GLU C 114     -43.124  34.173 -87.737  1.00 42.19           O  
-ATOM   8715  CB  GLU C 114     -40.031  35.271 -88.008  1.00 48.38           C  
-ATOM   8716  CG  GLU C 114     -40.485  35.167 -89.451  1.00 47.78           C  
-ATOM   8717  CD  GLU C 114     -39.316  35.126 -90.416  1.00 52.71           C  
-ATOM   8718  OE1 GLU C 114     -39.214  34.150 -91.189  1.00 53.97           O  
-ATOM   8719  OE2 GLU C 114     -38.497  36.070 -90.398  1.00 51.34           O  
-ATOM   8720  N   LYS C 115     -41.662  33.021 -86.468  1.00 52.29           N  
-ATOM   8721  CA  LYS C 115     -42.437  31.785 -86.449  1.00 43.89           C  
-ATOM   8722  C   LYS C 115     -42.045  30.949 -85.233  1.00 43.65           C  
-ATOM   8723  O   LYS C 115     -40.858  30.794 -84.944  1.00 37.48           O  
-ATOM   8724  CB  LYS C 115     -42.219  30.984 -87.737  1.00 40.79           C  
-ATOM   8725  CG  LYS C 115     -42.892  29.619 -87.745  1.00 33.71           C  
-ATOM   8726  CD  LYS C 115     -42.234  28.668 -88.734  1.00 31.55           C  
-ATOM   8727  CE  LYS C 115     -42.439  29.119 -90.169  1.00 36.01           C  
-ATOM   8728  NZ  LYS C 115     -41.918  28.113 -91.136  1.00 43.48           N  
-ATOM   8729  N   PRO C 116     -43.046  30.412 -84.514  1.00 39.03           N  
-ATOM   8730  CA  PRO C 116     -42.814  29.575 -83.332  1.00 41.37           C  
-ATOM   8731  C   PRO C 116     -41.916  28.371 -83.612  1.00 46.87           C  
-ATOM   8732  O   PRO C 116     -42.218  27.554 -84.484  1.00 41.43           O  
-ATOM   8733  CB  PRO C 116     -44.227  29.118 -82.939  1.00 39.82           C  
-ATOM   8734  CG  PRO C 116     -45.085  29.398 -84.137  1.00 34.79           C  
-ATOM   8735  CD  PRO C 116     -44.482  30.604 -84.770  1.00 38.61           C  
-ATOM   8736  N   GLN C 117     -40.819  28.277 -82.866  1.00 46.08           N  
-ATOM   8737  CA  GLN C 117     -39.877  27.174 -83.006  1.00 45.07           C  
-ATOM   8738  C   GLN C 117     -40.549  25.823 -82.766  1.00 54.69           C  
-ATOM   8739  O   GLN C 117     -41.081  25.564 -81.685  1.00 49.22           O  
-ATOM   8740  CB  GLN C 117     -38.707  27.359 -82.040  1.00 39.13           C  
-ATOM   8741  CG  GLN C 117     -37.832  26.131 -81.881  1.00 58.75           C  
-ATOM   8742  CD  GLN C 117     -36.678  26.364 -80.927  1.00 59.94           C  
-ATOM   8743  OE1 GLN C 117     -36.226  25.445 -80.244  1.00 58.25           O  
-ATOM   8744  NE2 GLN C 117     -36.193  27.599 -80.878  1.00 60.69           N  
-ATOM   8745  N   ALA C 118     -40.527  24.969 -83.784  1.00 58.56           N  
-ATOM   8746  CA  ALA C 118     -41.114  23.639 -83.679  1.00 50.06           C  
-ATOM   8747  C   ALA C 118     -40.297  22.780 -82.727  1.00 53.75           C  
-ATOM   8748  O   ALA C 118     -39.084  22.950 -82.609  1.00 61.81           O  
-ATOM   8749  CB  ALA C 118     -41.205  22.983 -85.046  1.00 47.11           C  
-ATOM   8750  N   GLU C 119     -40.965  21.857 -82.045  1.00 55.71           N  
-ATOM   8751  CA  GLU C 119     -40.298  21.010 -81.067  1.00 61.93           C  
-ATOM   8752  C   GLU C 119     -39.343  20.038 -81.752  1.00 56.86           C  
-ATOM   8753  O   GLU C 119     -39.703  19.386 -82.732  1.00 49.95           O  
-ATOM   8754  CB  GLU C 119     -41.328  20.251 -80.225  1.00 75.40           C  
-ATOM   8755  CG  GLU C 119     -40.736  19.445 -79.076  1.00 78.69           C  
-ATOM   8756  CD  GLU C 119     -40.407  18.015 -79.469  1.00 91.25           C  
-ATOM   8757  OE1 GLU C 119     -39.390  17.481 -78.976  1.00 79.50           O  
-ATOM   8758  OE2 GLU C 119     -41.170  17.425 -80.266  1.00 84.62           O  
-ATOM   8759  N   GLY C 120     -38.122  19.957 -81.231  1.00 51.95           N  
-ATOM   8760  CA  GLY C 120     -37.115  19.058 -81.767  1.00 58.58           C  
-ATOM   8761  C   GLY C 120     -36.148  19.734 -82.720  1.00 55.30           C  
-ATOM   8762  O   GLY C 120     -35.110  19.172 -83.071  1.00 49.14           O  
-ATOM   8763  N   GLN C 121     -36.487  20.947 -83.138  1.00 55.52           N  
-ATOM   8764  CA  GLN C 121     -35.670  21.680 -84.095  1.00 52.54           C  
-ATOM   8765  C   GLN C 121     -34.736  22.659 -83.395  1.00 55.62           C  
-ATOM   8766  O   GLN C 121     -35.072  23.215 -82.349  1.00 59.31           O  
-ATOM   8767  CB  GLN C 121     -36.561  22.421 -85.093  1.00 58.90           C  
-ATOM   8768  CG  GLN C 121     -37.382  21.500 -85.977  1.00 55.11           C  
-ATOM   8769  CD  GLN C 121     -36.522  20.702 -86.933  1.00 56.23           C  
-ATOM   8770  OE1 GLN C 121     -35.591  21.233 -87.541  1.00 53.20           O  
-ATOM   8771  NE2 GLN C 121     -36.824  19.416 -87.069  1.00 48.28           N  
-ATOM   8772  N   GLN C 122     -33.558  22.858 -83.978  1.00 53.38           N  
-ATOM   8773  CA  GLN C 122     -32.570  23.781 -83.434  1.00 44.01           C  
-ATOM   8774  C   GLN C 122     -33.043  25.221 -83.560  1.00 43.44           C  
-ATOM   8775  O   GLN C 122     -33.762  25.567 -84.498  1.00 41.44           O  
-ATOM   8776  CB  GLN C 122     -31.227  23.609 -84.147  1.00 39.92           C  
-ATOM   8777  CG  GLN C 122     -30.140  22.969 -83.298  1.00 43.75           C  
-ATOM   8778  CD  GLN C 122     -30.506  21.577 -82.818  1.00 54.00           C  
-ATOM   8779  OE1 GLN C 122     -31.263  20.857 -83.472  1.00 53.11           O  
-ATOM   8780  NE2 GLN C 122     -29.969  21.192 -81.667  1.00 44.19           N  
-ATOM   8781  N   ARG C 123     -32.643  26.060 -82.612  1.00 42.36           N  
-ATOM   8782  CA  ARG C 123     -32.961  27.476 -82.697  1.00 36.16           C  
-ATOM   8783  C   ARG C 123     -32.040  28.113 -83.731  1.00 31.57           C  
-ATOM   8784  O   ARG C 123     -30.878  27.726 -83.868  1.00 29.85           O  
-ATOM   8785  CB  ARG C 123     -32.830  28.158 -81.330  1.00 38.37           C  
-ATOM   8786  CG  ARG C 123     -31.485  28.807 -81.050  1.00 51.60           C  
-ATOM   8787  CD  ARG C 123     -31.487  29.498 -79.698  1.00 40.58           C  
-ATOM   8788  NE  ARG C 123     -32.732  30.230 -79.482  1.00 63.57           N  
-ATOM   8789  CZ  ARG C 123     -32.909  31.516 -79.769  1.00 74.24           C  
-ATOM   8790  NH1 ARG C 123     -34.083  32.090 -79.541  1.00 63.98           N  
-ATOM   8791  NH2 ARG C 123     -31.914  32.229 -80.281  1.00 69.30           N  
-ATOM   8792  N   VAL C 124     -32.573  29.071 -84.481  1.00 39.58           N  
-ATOM   8793  CA  VAL C 124     -31.808  29.713 -85.541  1.00 31.59           C  
-ATOM   8794  C   VAL C 124     -30.790  30.676 -84.951  1.00 30.01           C  
-ATOM   8795  O   VAL C 124     -31.130  31.526 -84.128  1.00 33.36           O  
-ATOM   8796  CB  VAL C 124     -32.717  30.472 -86.523  1.00 27.17           C  
-ATOM   8797  CG1 VAL C 124     -31.897  31.053 -87.657  1.00 21.86           C  
-ATOM   8798  CG2 VAL C 124     -33.787  29.549 -87.068  1.00 29.95           C  
-ATOM   8799  N   ARG C 125     -29.537  30.541 -85.371  1.00 36.49           N  
-ATOM   8800  CA  ARG C 125     -28.478  31.395 -84.846  1.00 37.87           C  
-ATOM   8801  C   ARG C 125     -28.130  32.513 -85.825  1.00 32.62           C  
-ATOM   8802  O   ARG C 125     -28.318  32.372 -87.031  1.00 31.04           O  
-ATOM   8803  CB  ARG C 125     -27.233  30.568 -84.530  1.00 35.58           C  
-ATOM   8804  CG  ARG C 125     -26.525  30.999 -83.270  1.00 42.51           C  
-ATOM   8805  CD  ARG C 125     -27.288  30.579 -82.030  1.00 33.92           C  
-ATOM   8806  NE  ARG C 125     -26.565  30.954 -80.821  1.00 38.12           N  
-ATOM   8807  CZ  ARG C 125     -25.595  30.225 -80.280  1.00 44.06           C  
-ATOM   8808  NH1 ARG C 125     -24.985  30.641 -79.178  1.00 43.34           N  
-ATOM   8809  NH2 ARG C 125     -25.237  29.078 -80.840  1.00 47.42           N  
-ATOM   8810  N   VAL C 126     -27.625  33.626 -85.302  1.00 27.75           N  
-ATOM   8811  CA  VAL C 126     -27.228  34.751 -86.146  1.00 26.37           C  
-ATOM   8812  C   VAL C 126     -25.808  35.216 -85.830  1.00 26.02           C  
-ATOM   8813  O   VAL C 126     -25.474  35.485 -84.677  1.00 30.02           O  
-ATOM   8814  CB  VAL C 126     -28.191  35.944 -85.994  1.00 24.61           C  
-ATOM   8815  CG1 VAL C 126     -27.712  37.125 -86.823  1.00 25.89           C  
-ATOM   8816  CG2 VAL C 126     -29.598  35.543 -86.405  1.00 32.85           C  
-ATOM   8817  N   CYS C 127     -24.977  35.309 -86.863  1.00 24.64           N  
-ATOM   8818  CA  CYS C 127     -23.593  35.739 -86.699  1.00 22.59           C  
-ATOM   8819  C   CYS C 127     -23.285  36.966 -87.555  1.00 26.67           C  
-ATOM   8820  O   CYS C 127     -23.922  37.194 -88.582  1.00 27.46           O  
-ATOM   8821  CB  CYS C 127     -22.639  34.595 -87.051  1.00 30.61           C  
-ATOM   8822  SG  CYS C 127     -22.982  33.046 -86.172  1.00 22.71           S  
-ATOM   8823  N   ALA C 128     -22.303  37.751 -87.126  1.00 29.13           N  
-ATOM   8824  CA  ALA C 128     -21.953  38.986 -87.821  1.00 29.71           C  
-ATOM   8825  C   ALA C 128     -21.047  38.735 -89.023  1.00 33.96           C  
-ATOM   8826  O   ALA C 128     -20.816  39.635 -89.832  1.00 42.96           O  
-ATOM   8827  CB  ALA C 128     -21.289  39.957 -86.862  1.00 31.01           C  
-ATOM   8828  N   SER C 129     -20.531  37.516 -89.133  1.00 32.39           N  
-ATOM   8829  CA  SER C 129     -19.649  37.165 -90.240  1.00 31.09           C  
-ATOM   8830  C   SER C 129     -19.489  35.658 -90.369  1.00 36.24           C  
-ATOM   8831  O   SER C 129     -19.884  34.903 -89.483  1.00 39.24           O  
-ATOM   8832  CB  SER C 129     -18.278  37.823 -90.060  1.00 33.35           C  
-ATOM   8833  OG  SER C 129     -17.632  37.344 -88.893  1.00 27.72           O  
-ATOM   8834  N   LEU C 130     -18.911  35.234 -91.486  1.00 28.01           N  
-ATOM   8835  CA  LEU C 130     -18.634  33.825 -91.722  1.00 28.49           C  
-ATOM   8836  C   LEU C 130     -17.584  33.254 -90.758  1.00 31.45           C  
-ATOM   8837  O   LEU C 130     -17.773  32.149 -90.243  1.00 38.41           O  
-ATOM   8838  CB  LEU C 130     -18.196  33.611 -93.173  1.00 29.09           C  
-ATOM   8839  CG  LEU C 130     -18.029  32.155 -93.608  1.00 28.40           C  
-ATOM   8840  CD1 LEU C 130     -19.326  31.396 -93.407  1.00 17.68           C  
-ATOM   8841  CD2 LEU C 130     -17.585  32.085 -95.054  1.00 19.61           C  
-ATOM   8842  N   PRO C 131     -16.471  33.986 -90.516  1.00 30.99           N  
-ATOM   8843  CA  PRO C 131     -15.556  33.491 -89.481  1.00 37.15           C  
-ATOM   8844  C   PRO C 131     -16.234  33.355 -88.120  1.00 37.08           C  
-ATOM   8845  O   PRO C 131     -15.877  32.464 -87.344  1.00 36.83           O  
-ATOM   8846  CB  PRO C 131     -14.459  34.561 -89.441  1.00 34.17           C  
-ATOM   8847  CG  PRO C 131     -14.449  35.125 -90.806  1.00 33.41           C  
-ATOM   8848  CD  PRO C 131     -15.889  35.137 -91.236  1.00 35.75           C  
-ATOM   8849  N   ALA C 132     -17.196  34.229 -87.841  1.00 31.47           N  
-ATOM   8850  CA  ALA C 132     -17.971  34.142 -86.610  1.00 33.25           C  
-ATOM   8851  C   ALA C 132     -18.854  32.908 -86.624  1.00 39.06           C  
-ATOM   8852  O   ALA C 132     -19.038  32.256 -85.598  1.00 42.56           O  
-ATOM   8853  CB  ALA C 132     -18.814  35.387 -86.416  1.00 27.97           C  
-ATOM   8854  N   ALA C 133     -19.407  32.600 -87.793  1.00 31.26           N  
-ATOM   8855  CA  ALA C 133     -20.242  31.420 -87.963  1.00 25.06           C  
-ATOM   8856  C   ALA C 133     -19.447  30.155 -87.674  1.00 39.21           C  
-ATOM   8857  O   ALA C 133     -19.890  29.288 -86.917  1.00 40.78           O  
-ATOM   8858  CB  ALA C 133     -20.818  31.372 -89.369  1.00 21.52           C  
-ATOM   8859  N   LEU C 134     -18.268  30.061 -88.282  1.00 42.47           N  
-ATOM   8860  CA  LEU C 134     -17.395  28.907 -88.108  1.00 33.56           C  
-ATOM   8861  C   LEU C 134     -16.889  28.786 -86.672  1.00 40.56           C  
-ATOM   8862  O   LEU C 134     -16.846  27.689 -86.106  1.00 36.16           O  
-ATOM   8863  CB  LEU C 134     -16.220  28.999 -89.080  1.00 34.69           C  
-ATOM   8864  CG  LEU C 134     -16.601  29.087 -90.560  1.00 31.63           C  
-ATOM   8865  CD1 LEU C 134     -15.369  29.313 -91.425  1.00 34.01           C  
-ATOM   8866  CD2 LEU C 134     -17.340  27.831 -90.987  1.00 31.21           C  
-ATOM   8867  N   SER C 135     -16.505  29.920 -86.093  1.00 42.76           N  
-ATOM   8868  CA  SER C 135     -16.048  29.965 -84.709  1.00 41.33           C  
-ATOM   8869  C   SER C 135     -17.145  29.492 -83.762  1.00 44.80           C  
-ATOM   8870  O   SER C 135     -16.872  28.788 -82.791  1.00 48.09           O  
-ATOM   8871  CB  SER C 135     -15.600  31.380 -84.331  1.00 42.83           C  
-ATOM   8872  OG  SER C 135     -14.549  31.831 -85.169  1.00 47.30           O  
-ATOM   8873  N   LEU C 136     -18.382  29.888 -84.051  1.00 36.41           N  
-ATOM   8874  CA  LEU C 136     -19.536  29.446 -83.277  1.00 39.56           C  
-ATOM   8875  C   LEU C 136     -19.726  27.939 -83.409  1.00 40.22           C  
-ATOM   8876  O   LEU C 136     -19.892  27.222 -82.418  1.00 48.86           O  
-ATOM   8877  CB  LEU C 136     -20.793  30.186 -83.739  1.00 38.88           C  
-ATOM   8878  CG  LEU C 136     -22.116  29.776 -83.095  1.00 34.05           C  
-ATOM   8879  CD1 LEU C 136     -22.310  30.462 -81.751  1.00 29.03           C  
-ATOM   8880  CD2 LEU C 136     -23.259  30.088 -84.036  1.00 35.19           C  
-ATOM   8881  N   LEU C 137     -19.694  27.480 -84.654  1.00 36.43           N  
-ATOM   8882  CA  LEU C 137     -19.836  26.068 -84.981  1.00 38.98           C  
-ATOM   8883  C   LEU C 137     -18.802  25.205 -84.266  1.00 46.73           C  
-ATOM   8884  O   LEU C 137     -19.093  24.072 -83.888  1.00 49.23           O  
-ATOM   8885  CB  LEU C 137     -19.726  25.861 -86.495  1.00 41.47           C  
-ATOM   8886  CG  LEU C 137     -20.972  25.390 -87.254  1.00 35.10           C  
-ATOM   8887  CD1 LEU C 137     -22.210  25.402 -86.370  1.00 33.37           C  
-ATOM   8888  CD2 LEU C 137     -21.184  26.241 -88.498  1.00 31.39           C  
-ATOM   8889  N   GLU C 138     -17.597  25.735 -84.083  1.00 52.26           N  
-ATOM   8890  CA  GLU C 138     -16.558  24.995 -83.376  1.00 51.28           C  
-ATOM   8891  C   GLU C 138     -16.731  25.099 -81.862  1.00 48.92           C  
-ATOM   8892  O   GLU C 138     -16.490  24.136 -81.132  1.00 58.50           O  
-ATOM   8893  CB  GLU C 138     -15.169  25.494 -83.786  1.00 51.56           C  
-ATOM   8894  CG  GLU C 138     -14.441  24.591 -84.778  1.00 62.79           C  
-ATOM   8895  CD  GLU C 138     -14.024  23.258 -84.170  1.00 72.52           C  
-ATOM   8896  OE1 GLU C 138     -13.661  23.236 -82.975  1.00 64.58           O  
-ATOM   8897  OE2 GLU C 138     -14.064  22.230 -84.881  1.00 67.43           O  
-ATOM   8898  N   GLU C 139     -17.152  26.270 -81.397  1.00 47.02           N  
-ATOM   8899  CA  GLU C 139     -17.237  26.530 -79.966  1.00 47.11           C  
-ATOM   8900  C   GLU C 139     -18.381  25.782 -79.295  1.00 38.20           C  
-ATOM   8901  O   GLU C 139     -18.169  25.099 -78.298  1.00 46.22           O  
-ATOM   8902  CB  GLU C 139     -17.366  28.031 -79.706  1.00 53.29           C  
-ATOM   8903  CG  GLU C 139     -16.024  28.713 -79.474  1.00 65.96           C  
-ATOM   8904  CD  GLU C 139     -16.003  30.153 -79.946  1.00 72.86           C  
-ATOM   8905  OE1 GLU C 139     -17.082  30.783 -80.000  1.00 64.59           O  
-ATOM   8906  OE2 GLU C 139     -14.905  30.653 -80.270  1.00 72.38           O  
-ATOM   8907  N   GLU C 140     -19.590  25.898 -79.833  1.00 44.33           N  
-ATOM   8908  CA  GLU C 140     -20.735  25.269 -79.181  1.00 48.38           C  
-ATOM   8909  C   GLU C 140     -21.511  24.296 -80.062  1.00 49.98           C  
-ATOM   8910  O   GLU C 140     -22.681  24.023 -79.798  1.00 51.93           O  
-ATOM   8911  CB  GLU C 140     -21.690  26.341 -78.650  1.00 42.51           C  
-ATOM   8912  CG  GLU C 140     -21.509  27.714 -79.261  1.00 35.11           C  
-ATOM   8913  CD  GLU C 140     -22.317  28.766 -78.531  1.00 42.52           C  
-ATOM   8914  OE1 GLU C 140     -21.762  29.844 -78.230  1.00 37.66           O  
-ATOM   8915  OE2 GLU C 140     -23.508  28.511 -78.249  1.00 39.77           O  
-ATOM   8916  N   TYR C 141     -20.868  23.761 -81.093  1.00 53.03           N  
-ATOM   8917  CA  TYR C 141     -21.543  22.790 -81.946  1.00 51.87           C  
-ATOM   8918  C   TYR C 141     -20.641  21.643 -82.391  1.00 60.16           C  
-ATOM   8919  O   TYR C 141     -21.007  20.874 -83.279  1.00 61.35           O  
-ATOM   8920  CB  TYR C 141     -22.142  23.481 -83.171  1.00 43.17           C  
-ATOM   8921  CG  TYR C 141     -23.430  24.219 -82.883  1.00 44.02           C  
-ATOM   8922  CD1 TYR C 141     -24.621  23.529 -82.683  1.00 36.60           C  
-ATOM   8923  CD2 TYR C 141     -23.458  25.605 -82.819  1.00 43.53           C  
-ATOM   8924  CE1 TYR C 141     -25.803  24.202 -82.423  1.00 30.95           C  
-ATOM   8925  CE2 TYR C 141     -24.633  26.285 -82.561  1.00 38.63           C  
-ATOM   8926  CZ  TYR C 141     -25.801  25.582 -82.364  1.00 30.77           C  
-ATOM   8927  OH  TYR C 141     -26.967  26.267 -82.108  1.00 31.64           O  
-ATOM   8928  N   LYS C 142     -19.466  21.522 -81.784  1.00 62.93           N  
-ATOM   8929  CA  LYS C 142     -18.678  20.312 -81.964  1.00 63.71           C  
-ATOM   8930  C   LYS C 142     -19.376  19.202 -81.204  1.00 66.32           C  
-ATOM   8931  O   LYS C 142     -20.060  19.476 -80.215  1.00 75.70           O  
-ATOM   8932  CB  LYS C 142     -17.238  20.500 -81.485  1.00 69.93           C  
-ATOM   8933  CG  LYS C 142     -16.297  20.986 -82.577  1.00 73.31           C  
-ATOM   8934  CD  LYS C 142     -16.409  20.107 -83.823  1.00 84.91           C  
-ATOM   8935  CE  LYS C 142     -17.024  20.859 -85.004  1.00 79.61           C  
-ATOM   8936  NZ  LYS C 142     -17.454  19.937 -86.095  1.00 50.51           N  
-ATOM   8937  N   ASP C 143     -19.244  17.968 -81.696  1.00 62.39           N  
-ATOM   8938  CA  ASP C 143     -19.953  16.811 -81.140  1.00 78.19           C  
-ATOM   8939  C   ASP C 143     -21.463  16.933 -81.435  1.00 65.92           C  
-ATOM   8940  O   ASP C 143     -22.252  16.027 -81.159  1.00 61.01           O  
-ATOM   8941  CB  ASP C 143     -19.643  16.677 -79.632  1.00 85.41           C  
-ATOM   8942  CG  ASP C 143     -20.686  15.888 -78.870  1.00104.34           C  
-ATOM   8943  OD1 ASP C 143     -21.624  16.513 -78.328  1.00 99.89           O  
-ATOM   8944  OD2 ASP C 143     -20.562  14.647 -78.805  1.00105.70           O  
-ATOM   8945  N   SER C 144     -21.845  18.044 -82.058  1.00 55.72           N  
-ATOM   8946  CA  SER C 144     -23.242  18.321 -82.363  1.00 45.14           C  
-ATOM   8947  C   SER C 144     -23.531  18.303 -83.867  1.00 51.69           C  
-ATOM   8948  O   SER C 144     -24.549  17.762 -84.300  1.00 46.36           O  
-ATOM   8949  CB  SER C 144     -23.645  19.673 -81.772  1.00 49.72           C  
-ATOM   8950  OG  SER C 144     -24.963  20.029 -82.150  1.00 53.23           O  
-ATOM   8951  N   VAL C 145     -22.643  18.895 -84.661  1.00 59.11           N  
-ATOM   8952  CA  VAL C 145     -22.860  18.973 -86.104  1.00 46.53           C  
-ATOM   8953  C   VAL C 145     -21.871  18.114 -86.887  1.00 43.30           C  
-ATOM   8954  O   VAL C 145     -20.765  17.831 -86.423  1.00 43.62           O  
-ATOM   8955  CB  VAL C 145     -22.769  20.426 -86.617  1.00 45.82           C  
-ATOM   8956  CG1 VAL C 145     -23.755  21.315 -85.872  1.00 52.67           C  
-ATOM   8957  CG2 VAL C 145     -21.351  20.961 -86.479  1.00 49.70           C  
-ATOM   8958  N   ASP C 146     -22.284  17.700 -88.081  1.00 44.55           N  
-ATOM   8959  CA  ASP C 146     -21.434  16.895 -88.949  1.00 54.66           C  
-ATOM   8960  C   ASP C 146     -20.815  17.756 -90.048  1.00 59.25           C  
-ATOM   8961  O   ASP C 146     -19.691  18.239 -89.909  1.00 64.03           O  
-ATOM   8962  CB  ASP C 146     -22.231  15.735 -89.560  1.00 53.74           C  
-ATOM   8963  CG  ASP C 146     -21.358  14.776 -90.357  1.00 55.86           C  
-ATOM   8964  OD1 ASP C 146     -20.115  14.835 -90.226  1.00 44.14           O  
-ATOM   8965  OD2 ASP C 146     -21.918  13.951 -91.109  1.00 56.50           O  
-ATOM   8966  N   GLN C 147     -21.553  17.948 -91.137  1.00 50.98           N  
-ATOM   8967  CA  GLN C 147     -21.057  18.731 -92.262  1.00 42.51           C  
-ATOM   8968  C   GLN C 147     -21.575  20.164 -92.225  1.00 42.16           C  
-ATOM   8969  O   GLN C 147     -22.650  20.432 -91.690  1.00 40.61           O  
-ATOM   8970  CB  GLN C 147     -21.446  18.075 -93.588  1.00 40.40           C  
-ATOM   8971  CG  GLN C 147     -20.948  16.653 -93.752  1.00 46.82           C  
-ATOM   8972  CD  GLN C 147     -20.832  16.243 -95.208  1.00 53.71           C  
-ATOM   8973  OE1 GLN C 147     -21.649  15.477 -95.718  1.00 47.85           O  
-ATOM   8974  NE2 GLN C 147     -19.809  16.754 -95.887  1.00 45.51           N  
-ATOM   8975  N   ILE C 148     -20.805  21.080 -92.803  1.00 43.25           N  
-ATOM   8976  CA  ILE C 148     -21.201  22.481 -92.870  1.00 38.78           C  
-ATOM   8977  C   ILE C 148     -21.401  22.915 -94.320  1.00 37.49           C  
-ATOM   8978  O   ILE C 148     -20.508  22.748 -95.156  1.00 39.62           O  
-ATOM   8979  CB  ILE C 148     -20.158  23.394 -92.198  1.00 37.14           C  
-ATOM   8980  CG1 ILE C 148     -19.987  23.009 -90.727  1.00 35.24           C  
-ATOM   8981  CG2 ILE C 148     -20.568  24.850 -92.324  1.00 34.08           C  
-ATOM   8982  CD1 ILE C 148     -18.947  23.830 -90.001  1.00 23.43           C  
-ATOM   8983  N   PHE C 149     -22.577  23.464 -94.612  1.00 35.92           N  
-ATOM   8984  CA  PHE C 149     -22.924  23.862 -95.973  1.00 29.38           C  
-ATOM   8985  C   PHE C 149     -23.158  25.366 -96.107  1.00 28.12           C  
-ATOM   8986  O   PHE C 149     -24.049  25.921 -95.463  1.00 30.34           O  
-ATOM   8987  CB  PHE C 149     -24.179  23.120 -96.447  1.00 31.14           C  
-ATOM   8988  CG  PHE C 149     -23.997  21.635 -96.601  1.00 35.05           C  
-ATOM   8989  CD1 PHE C 149     -23.489  21.103 -97.775  1.00 33.05           C  
-ATOM   8990  CD2 PHE C 149     -24.355  20.770 -95.579  1.00 33.25           C  
-ATOM   8991  CE1 PHE C 149     -23.329  19.735 -97.921  1.00 35.67           C  
-ATOM   8992  CE2 PHE C 149     -24.199  19.403 -95.720  1.00 31.26           C  
-ATOM   8993  CZ  PHE C 149     -23.685  18.885 -96.892  1.00 30.45           C  
-ATOM   8994  N   VAL C 150     -22.355  26.021 -96.941  1.00 26.46           N  
-ATOM   8995  CA  VAL C 150     -22.642  27.388 -97.352  1.00 25.11           C  
-ATOM   8996  C   VAL C 150     -23.652  27.345 -98.494  1.00 29.04           C  
-ATOM   8997  O   VAL C 150     -23.461  26.651 -99.506  1.00 35.99           O  
-ATOM   8998  CB  VAL C 150     -21.379  28.152 -97.786  1.00 31.24           C  
-ATOM   8999  CG1 VAL C 150     -21.756  29.519 -98.343  1.00 28.98           C  
-ATOM   9000  CG2 VAL C 150     -20.426  28.300 -96.614  1.00 24.39           C  
-ATOM   9001  N   VAL C 151     -24.724  28.108 -98.314  1.00 29.49           N  
-ATOM   9002  CA  VAL C 151     -25.944  27.945 -99.087  1.00 29.55           C  
-ATOM   9003  C   VAL C 151     -26.288  29.203 -99.893  1.00 35.87           C  
-ATOM   9004  O   VAL C 151     -26.938  29.125-100.940  1.00 42.42           O  
-ATOM   9005  CB  VAL C 151     -27.098  27.554 -98.135  1.00 25.87           C  
-ATOM   9006  CG1 VAL C 151     -28.448  27.715 -98.783  1.00 31.91           C  
-ATOM   9007  CG2 VAL C 151     -26.903  26.127 -97.654  1.00 25.24           C  
-ATOM   9008  N   GLY C 152     -25.817  30.356 -99.426  1.00 25.92           N  
-ATOM   9009  CA  GLY C 152     -25.994  31.600-100.157  1.00 23.00           C  
-ATOM   9010  C   GLY C 152     -25.825  32.840 -99.297  1.00 28.34           C  
-ATOM   9011  O   GLY C 152     -25.871  32.757 -98.074  1.00 35.15           O  
-ATOM   9012  N   GLY C 153     -25.626  33.995 -99.927  1.00 26.72           N  
-ATOM   9013  CA  GLY C 153     -25.540  34.096-101.371  1.00 23.30           C  
-ATOM   9014  C   GLY C 153     -24.160  34.551-101.794  1.00 24.52           C  
-ATOM   9015  O   GLY C 153     -23.163  34.053-101.280  1.00 29.93           O  
-ATOM   9016  N   ALA C 154     -24.105  35.512-102.712  1.00 22.08           N  
-ATOM   9017  CA  ALA C 154     -22.846  35.978-103.296  1.00 20.03           C  
-ATOM   9018  C   ALA C 154     -21.807  36.386-102.254  1.00 26.55           C  
-ATOM   9019  O   ALA C 154     -20.622  36.111-102.415  1.00 26.59           O  
-ATOM   9020  CB  ALA C 154     -23.111  37.138-104.237  1.00 29.53           C  
-ATOM   9021  N   GLY C 155     -22.259  37.041-101.190  1.00 30.07           N  
-ATOM   9022  CA  GLY C 155     -21.373  37.468-100.123  1.00 24.90           C  
-ATOM   9023  C   GLY C 155     -20.734  36.301 -99.399  1.00 31.29           C  
-ATOM   9024  O   GLY C 155     -19.519  36.276 -99.188  1.00 36.12           O  
-ATOM   9025  N   LEU C 156     -21.553  35.326 -99.020  1.00 30.75           N  
-ATOM   9026  CA  LEU C 156     -21.050  34.150 -98.318  1.00 29.91           C  
-ATOM   9027  C   LEU C 156     -20.166  33.282 -99.204  1.00 24.86           C  
-ATOM   9028  O   LEU C 156     -19.173  32.739 -98.734  1.00 22.15           O  
-ATOM   9029  CB  LEU C 156     -22.200  33.308 -97.762  1.00 25.91           C  
-ATOM   9030  CG  LEU C 156     -22.868  33.796 -96.474  1.00 24.55           C  
-ATOM   9031  CD1 LEU C 156     -23.261  32.606 -95.615  1.00 18.19           C  
-ATOM   9032  CD2 LEU C 156     -21.974  34.759 -95.702  1.00 25.52           C  
-ATOM   9033  N   TYR C 157     -20.532  33.141-100.475  1.00 22.32           N  
-ATOM   9034  CA  TYR C 157     -19.714  32.390-101.424  1.00 20.78           C  
-ATOM   9035  C   TYR C 157     -18.359  33.064-101.589  1.00 24.63           C  
-ATOM   9036  O   TYR C 157     -17.317  32.407-101.548  1.00 25.43           O  
-ATOM   9037  CB  TYR C 157     -20.415  32.271-102.780  1.00 23.89           C  
-ATOM   9038  CG  TYR C 157     -21.715  31.499-102.737  1.00 23.34           C  
-ATOM   9039  CD1 TYR C 157     -21.819  30.314-102.022  1.00 22.79           C  
-ATOM   9040  CD2 TYR C 157     -22.839  31.958-103.410  1.00 30.15           C  
-ATOM   9041  CE1 TYR C 157     -23.006  29.609-101.981  1.00 26.64           C  
-ATOM   9042  CE2 TYR C 157     -24.031  31.265-103.369  1.00 24.16           C  
-ATOM   9043  CZ  TYR C 157     -24.109  30.093-102.653  1.00 25.13           C  
-ATOM   9044  OH  TYR C 157     -25.296  29.402-102.627  1.00 30.23           O  
-ATOM   9045  N   GLU C 158     -18.391  34.381-101.774  1.00 25.33           N  
-ATOM   9046  CA  GLU C 158     -17.182  35.186-101.909  1.00 29.77           C  
-ATOM   9047  C   GLU C 158     -16.265  35.029-100.703  1.00 28.48           C  
-ATOM   9048  O   GLU C 158     -15.075  34.761-100.854  1.00 30.52           O  
-ATOM   9049  CB  GLU C 158     -17.544  36.664-102.103  1.00 36.43           C  
-ATOM   9050  CG  GLU C 158     -16.350  37.607-102.171  1.00 63.40           C  
-ATOM   9051  CD  GLU C 158     -15.753  37.713-103.567  1.00 67.27           C  
-ATOM   9052  OE1 GLU C 158     -15.342  38.828-103.955  1.00 77.24           O  
-ATOM   9053  OE2 GLU C 158     -15.689  36.687-104.276  1.00 67.46           O  
-ATOM   9054  N   ALA C 159     -16.828  35.197 -99.510  1.00 28.01           N  
-ATOM   9055  CA  ALA C 159     -16.059  35.095 -98.274  1.00 27.38           C  
-ATOM   9056  C   ALA C 159     -15.483  33.697 -98.080  1.00 26.47           C  
-ATOM   9057  O   ALA C 159     -14.315  33.542 -97.735  1.00 30.12           O  
-ATOM   9058  CB  ALA C 159     -16.924  35.474 -97.085  1.00 31.15           C  
-ATOM   9059  N   ALA C 160     -16.315  32.685 -98.307  1.00 27.33           N  
-ATOM   9060  CA  ALA C 160     -15.917  31.290 -98.141  1.00 32.03           C  
-ATOM   9061  C   ALA C 160     -14.823  30.897 -99.122  1.00 32.86           C  
-ATOM   9062  O   ALA C 160     -13.964  30.073 -98.808  1.00 38.50           O  
-ATOM   9063  CB  ALA C 160     -17.120  30.376 -98.303  1.00 31.68           C  
-ATOM   9064  N   LEU C 161     -14.865  31.481-100.314  1.00 35.72           N  
-ATOM   9065  CA  LEU C 161     -13.837  31.233-101.313  1.00 30.53           C  
-ATOM   9066  C   LEU C 161     -12.567  31.991-100.958  1.00 25.55           C  
-ATOM   9067  O   LEU C 161     -11.462  31.545-101.255  1.00 28.12           O  
-ATOM   9068  CB  LEU C 161     -14.334  31.629-102.704  1.00 32.05           C  
-ATOM   9069  CG  LEU C 161     -14.583  30.473-103.676  1.00 19.80           C  
-ATOM   9070  CD1 LEU C 161     -15.021  29.226-102.934  1.00 15.14           C  
-ATOM   9071  CD2 LEU C 161     -15.626  30.870-104.710  1.00 19.29           C  
-ATOM   9072  N   SER C 162     -12.736  33.138-100.309  1.00 32.55           N  
-ATOM   9073  CA  SER C 162     -11.605  33.944 -99.869  1.00 35.49           C  
-ATOM   9074  C   SER C 162     -10.823  33.226 -98.775  1.00 38.07           C  
-ATOM   9075  O   SER C 162      -9.604  33.090 -98.864  1.00 44.36           O  
-ATOM   9076  CB  SER C 162     -12.078  35.313 -99.376  1.00 36.57           C  
-ATOM   9077  OG  SER C 162     -12.562  36.103-100.450  1.00 64.22           O  
-ATOM   9078  N   LEU C 163     -11.534  32.759 -97.753  1.00 31.82           N  
-ATOM   9079  CA  LEU C 163     -10.925  32.030 -96.648  1.00 28.38           C  
-ATOM   9080  C   LEU C 163     -10.268  30.742 -97.124  1.00 32.87           C  
-ATOM   9081  O   LEU C 163      -9.318  30.260 -96.509  1.00 35.52           O  
-ATOM   9082  CB  LEU C 163     -11.970  31.713 -95.579  1.00 20.63           C  
-ATOM   9083  CG  LEU C 163     -12.726  32.919 -95.026  1.00 29.02           C  
-ATOM   9084  CD1 LEU C 163     -13.677  32.506 -93.911  1.00 36.21           C  
-ATOM   9085  CD2 LEU C 163     -11.748  33.978 -94.548  1.00 32.75           C  
-ATOM   9086  N   GLY C 164     -10.780  30.187 -98.218  1.00 34.23           N  
-ATOM   9087  CA  GLY C 164     -10.239  28.961 -98.771  1.00 36.56           C  
-ATOM   9088  C   GLY C 164     -10.698  27.747 -97.992  1.00 39.19           C  
-ATOM   9089  O   GLY C 164     -10.093  26.679 -98.067  1.00 53.86           O  
-ATOM   9090  N   VAL C 165     -11.779  27.917 -97.240  1.00 35.95           N  
-ATOM   9091  CA  VAL C 165     -12.319  26.850 -96.408  1.00 39.39           C  
-ATOM   9092  C   VAL C 165     -13.156  25.869 -97.226  1.00 37.38           C  
-ATOM   9093  O   VAL C 165     -13.506  24.787 -96.751  1.00 36.73           O  
-ATOM   9094  CB  VAL C 165     -13.174  27.422 -95.262  1.00 38.69           C  
-ATOM   9095  CG1 VAL C 165     -12.281  28.019 -94.189  1.00 46.56           C  
-ATOM   9096  CG2 VAL C 165     -14.143  28.468 -95.790  1.00 30.02           C  
-ATOM   9097  N   ALA C 166     -13.465  26.253 -98.460  1.00 34.66           N  
-ATOM   9098  CA  ALA C 166     -14.290  25.433 -99.340  1.00 33.63           C  
-ATOM   9099  C   ALA C 166     -13.512  24.251 -99.905  1.00 36.98           C  
-ATOM   9100  O   ALA C 166     -12.544  24.428-100.644  1.00 43.87           O  
-ATOM   9101  CB  ALA C 166     -14.853  26.276-100.468  1.00 35.05           C  
-ATOM   9102  N   SER C 167     -13.948  23.044 -99.560  1.00 30.36           N  
-ATOM   9103  CA  SER C 167     -13.297  21.829-100.034  1.00 28.93           C  
-ATOM   9104  C   SER C 167     -14.001  21.266-101.263  1.00 33.81           C  
-ATOM   9105  O   SER C 167     -13.357  20.751-102.182  1.00 41.86           O  
-ATOM   9106  CB  SER C 167     -13.264  20.778 -98.925  1.00 29.27           C  
-ATOM   9107  OG  SER C 167     -14.572  20.367 -98.573  1.00 27.68           O  
-ATOM   9108  N   HIS C 168     -15.327  21.366-101.268  1.00 31.40           N  
-ATOM   9109  CA  HIS C 168     -16.137  20.851-102.366  1.00 30.40           C  
-ATOM   9110  C   HIS C 168     -17.209  21.842-102.804  1.00 33.27           C  
-ATOM   9111  O   HIS C 168     -17.752  22.584-101.987  1.00 37.71           O  
-ATOM   9112  CB  HIS C 168     -16.792  19.528-101.968  1.00 31.16           C  
-ATOM   9113  CG  HIS C 168     -15.814  18.426-101.705  1.00 44.73           C  
-ATOM   9114  ND1 HIS C 168     -15.321  18.154-100.447  1.00 52.68           N  
-ATOM   9115  CD2 HIS C 168     -15.237  17.529-102.538  1.00 43.59           C  
-ATOM   9116  CE1 HIS C 168     -14.485  17.134-100.517  1.00 53.68           C  
-ATOM   9117  NE2 HIS C 168     -14.415  16.736-101.774  1.00 41.83           N  
-ATOM   9118  N   LEU C 169     -17.513  21.842-104.098  1.00 29.31           N  
-ATOM   9119  CA  LEU C 169     -18.580  22.681-104.630  1.00 25.24           C  
-ATOM   9120  C   LEU C 169     -19.691  21.837-105.248  1.00 29.19           C  
-ATOM   9121  O   LEU C 169     -19.469  21.135-106.232  1.00 29.23           O  
-ATOM   9122  CB  LEU C 169     -18.034  23.654-105.677  1.00 21.04           C  
-ATOM   9123  CG  LEU C 169     -16.882  24.573-105.279  1.00 25.59           C  
-ATOM   9124  CD1 LEU C 169     -16.589  25.562-106.398  1.00 24.99           C  
-ATOM   9125  CD2 LEU C 169     -17.196  25.301-103.986  1.00 28.62           C  
-ATOM   9126  N   TYR C 170     -20.886  21.903-104.671  1.00 27.37           N  
-ATOM   9127  CA  TYR C 170     -22.046  21.238-105.256  1.00 20.11           C  
-ATOM   9128  C   TYR C 170     -22.762  22.185-106.209  1.00 20.59           C  
-ATOM   9129  O   TYR C 170     -23.701  22.878-105.819  1.00 25.77           O  
-ATOM   9130  CB  TYR C 170     -23.005  20.752-104.169  1.00 20.10           C  
-ATOM   9131  CG  TYR C 170     -22.484  19.579-103.371  1.00 27.65           C  
-ATOM   9132  CD1 TYR C 170     -21.670  19.775-102.262  1.00 36.17           C  
-ATOM   9133  CD2 TYR C 170     -22.808  18.274-103.722  1.00 28.27           C  
-ATOM   9134  CE1 TYR C 170     -21.192  18.705-101.529  1.00 33.23           C  
-ATOM   9135  CE2 TYR C 170     -22.335  17.200-102.996  1.00 21.35           C  
-ATOM   9136  CZ  TYR C 170     -21.529  17.420-101.902  1.00 24.64           C  
-ATOM   9137  OH  TYR C 170     -21.061  16.347-101.180  1.00 29.57           O  
-ATOM   9138  N   ILE C 171     -22.319  22.215-107.460  1.00 16.15           N  
-ATOM   9139  CA  ILE C 171     -22.861  23.171-108.416  1.00 16.99           C  
-ATOM   9140  C   ILE C 171     -23.931  22.552-109.298  1.00 17.87           C  
-ATOM   9141  O   ILE C 171     -23.701  21.529-109.940  1.00 17.56           O  
-ATOM   9142  CB  ILE C 171     -21.763  23.759-109.321  1.00 23.64           C  
-ATOM   9143  CG1 ILE C 171     -20.652  24.395-108.481  1.00 19.14           C  
-ATOM   9144  CG2 ILE C 171     -22.360  24.774-110.285  1.00 21.61           C  
-ATOM   9145  CD1 ILE C 171     -19.613  25.118-109.303  1.00 12.53           C  
-ATOM   9146  N   THR C 172     -25.100  23.182-109.323  1.00 18.33           N  
-ATOM   9147  CA  THR C 172     -26.160  22.787-110.238  1.00 17.03           C  
-ATOM   9148  C   THR C 172     -26.131  23.699-111.458  1.00 15.94           C  
-ATOM   9149  O   THR C 172     -26.702  24.790-111.440  1.00 18.10           O  
-ATOM   9150  CB  THR C 172     -27.550  22.849-109.575  1.00 22.12           C  
-ATOM   9151  OG1 THR C 172     -27.555  22.045-108.389  1.00 21.73           O  
-ATOM   9152  CG2 THR C 172     -28.622  22.340-110.527  1.00 25.99           C  
-ATOM   9153  N   ARG C 173     -25.451  23.251-112.510  1.00 19.86           N  
-ATOM   9154  CA  ARG C 173     -25.346  24.018-113.747  1.00 21.75           C  
-ATOM   9155  C   ARG C 173     -26.673  24.096-114.472  1.00 19.22           C  
-ATOM   9156  O   ARG C 173     -27.141  23.104-115.034  1.00 19.86           O  
-ATOM   9157  CB  ARG C 173     -24.301  23.410-114.684  1.00 19.46           C  
-ATOM   9158  CG  ARG C 173     -22.920  23.288-114.085  1.00 19.54           C  
-ATOM   9159  CD  ARG C 173     -22.277  21.996-114.527  1.00 21.49           C  
-ATOM   9160  NE  ARG C 173     -21.452  22.145-115.718  1.00 17.09           N  
-ATOM   9161  CZ  ARG C 173     -21.243  21.176-116.602  1.00 19.51           C  
-ATOM   9162  NH1 ARG C 173     -21.816  19.990-116.445  1.00 15.31           N  
-ATOM   9163  NH2 ARG C 173     -20.471  21.397-117.653  1.00 29.90           N  
-ATOM   9164  N   VAL C 174     -27.273  25.281-114.438  1.00 18.26           N  
-ATOM   9165  CA  VAL C 174     -28.424  25.600-115.267  1.00 16.26           C  
-ATOM   9166  C   VAL C 174     -27.899  25.968-116.648  1.00 18.64           C  
-ATOM   9167  O   VAL C 174     -26.956  26.745-116.758  1.00 24.19           O  
-ATOM   9168  CB  VAL C 174     -29.244  26.760-114.677  1.00 15.28           C  
-ATOM   9169  CG1 VAL C 174     -30.429  27.088-115.564  1.00 14.32           C  
-ATOM   9170  CG2 VAL C 174     -29.695  26.420-113.259  1.00 13.13           C  
-ATOM   9171  N   ALA C 175     -28.480  25.403-117.701  1.00 14.79           N  
-ATOM   9172  CA  ALA C 175     -27.952  25.628-119.046  1.00 14.13           C  
-ATOM   9173  C   ALA C 175     -28.479  26.917-119.684  1.00 15.43           C  
-ATOM   9174  O   ALA C 175     -27.766  27.572-120.441  1.00 15.58           O  
-ATOM   9175  CB  ALA C 175     -28.261  24.440-119.936  1.00 18.68           C  
-ATOM   9176  N   ARG C 176     -29.725  27.272-119.384  1.00 15.25           N  
-ATOM   9177  CA  ARG C 176     -30.320  28.499-119.909  1.00 12.79           C  
-ATOM   9178  C   ARG C 176     -29.769  29.739-119.222  1.00 18.20           C  
-ATOM   9179  O   ARG C 176     -29.336  29.685-118.072  1.00 25.46           O  
-ATOM   9180  CB  ARG C 176     -31.836  28.481-119.746  1.00 20.77           C  
-ATOM   9181  CG  ARG C 176     -32.564  27.564-120.697  1.00 24.85           C  
-ATOM   9182  CD  ARG C 176     -34.069  27.625-120.470  1.00 24.93           C  
-ATOM   9183  NE  ARG C 176     -34.601  28.980-120.594  1.00 21.39           N  
-ATOM   9184  CZ  ARG C 176     -35.897  29.275-120.592  1.00 28.35           C  
-ATOM   9185  NH1 ARG C 176     -36.291  30.535-120.708  1.00 41.47           N  
-ATOM   9186  NH2 ARG C 176     -36.802  28.311-120.477  1.00 22.99           N  
-ATOM   9187  N   GLU C 177     -29.799  30.861-119.928  1.00 20.12           N  
-ATOM   9188  CA  GLU C 177     -29.387  32.127-119.346  1.00 15.31           C  
-ATOM   9189  C   GLU C 177     -30.618  32.931-118.943  1.00 24.94           C  
-ATOM   9190  O   GLU C 177     -31.562  33.078-119.719  1.00 34.05           O  
-ATOM   9191  CB  GLU C 177     -28.517  32.915-120.324  1.00 21.25           C  
-ATOM   9192  CG  GLU C 177     -27.715  34.018-119.666  1.00 24.61           C  
-ATOM   9193  CD  GLU C 177     -26.935  33.522-118.465  1.00 31.78           C  
-ATOM   9194  OE1 GLU C 177     -25.953  32.772-118.655  1.00 36.49           O  
-ATOM   9195  OE2 GLU C 177     -27.313  33.879-117.329  1.00 34.23           O  
-ATOM   9196  N   PHE C 178     -30.611  33.436-117.716  1.00 28.83           N  
-ATOM   9197  CA  PHE C 178     -31.737  34.199-117.198  1.00 19.02           C  
-ATOM   9198  C   PHE C 178     -31.285  35.571-116.718  1.00 20.03           C  
-ATOM   9199  O   PHE C 178     -30.110  35.760-116.397  1.00 19.45           O  
-ATOM   9200  CB  PHE C 178     -32.418  33.437-116.058  1.00 21.36           C  
-ATOM   9201  CG  PHE C 178     -33.173  32.224-116.507  1.00 19.45           C  
-ATOM   9202  CD1 PHE C 178     -32.546  30.995-116.593  1.00 21.61           C  
-ATOM   9203  CD2 PHE C 178     -34.512  32.314-116.844  1.00 25.66           C  
-ATOM   9204  CE1 PHE C 178     -33.240  29.877-117.005  1.00 26.62           C  
-ATOM   9205  CE2 PHE C 178     -35.212  31.198-117.260  1.00 32.14           C  
-ATOM   9206  CZ  PHE C 178     -34.574  29.978-117.342  1.00 26.89           C  
-ATOM   9207  N   PRO C 179     -32.215  36.538-116.685  1.00 18.95           N  
-ATOM   9208  CA  PRO C 179     -31.935  37.848-116.089  1.00 24.63           C  
-ATOM   9209  C   PRO C 179     -31.478  37.718-114.637  1.00 20.62           C  
-ATOM   9210  O   PRO C 179     -32.191  37.130-113.824  1.00 19.06           O  
-ATOM   9211  CB  PRO C 179     -33.282  38.568-116.181  1.00 25.78           C  
-ATOM   9212  CG  PRO C 179     -33.960  37.934-117.346  1.00 23.65           C  
-ATOM   9213  CD  PRO C 179     -33.547  36.493-117.313  1.00 15.84           C  
-ATOM   9214  N   CYS C 180     -30.304  38.256-114.323  1.00 17.86           N  
-ATOM   9215  CA  CYS C 180     -29.749  38.145-112.978  1.00 20.18           C  
-ATOM   9216  C   CYS C 180     -29.108  39.446-112.504  1.00 23.34           C  
-ATOM   9217  O   CYS C 180     -28.549  40.200-113.301  1.00 31.08           O  
-ATOM   9218  CB  CYS C 180     -28.717  37.018-112.921  1.00 25.78           C  
-ATOM   9219  SG  CYS C 180     -29.393  35.372-113.210  1.00 23.24           S  
-ATOM   9220  N   ASP C 181     -29.189  39.701-111.202  1.00 21.37           N  
-ATOM   9221  CA  ASP C 181     -28.548  40.871-110.614  1.00 20.49           C  
-ATOM   9222  C   ASP C 181     -27.530  40.458-109.555  1.00 22.57           C  
-ATOM   9223  O   ASP C 181     -26.811  41.294-109.009  1.00 26.49           O  
-ATOM   9224  CB  ASP C 181     -29.593  41.823-110.016  1.00 18.96           C  
-ATOM   9225  CG  ASP C 181     -30.542  41.133-109.044  1.00 25.74           C  
-ATOM   9226  OD1 ASP C 181     -30.163  40.100-108.455  1.00 33.49           O  
-ATOM   9227  OD2 ASP C 181     -31.673  41.634-108.860  1.00 24.58           O  
-ATOM   9228  N   VAL C 182     -27.480  39.162-109.265  1.00 21.89           N  
-ATOM   9229  CA  VAL C 182     -26.531  38.621-108.295  1.00 23.86           C  
-ATOM   9230  C   VAL C 182     -25.835  37.391-108.872  1.00 17.70           C  
-ATOM   9231  O   VAL C 182     -26.490  36.476-109.374  1.00 13.30           O  
-ATOM   9232  CB  VAL C 182     -27.224  38.251-106.966  1.00 28.37           C  
-ATOM   9233  CG1 VAL C 182     -26.255  37.536-106.037  1.00 26.78           C  
-ATOM   9234  CG2 VAL C 182     -27.792  39.495-106.293  1.00 19.29           C  
-ATOM   9235  N   PHE C 183     -24.507  37.372-108.796  1.00 17.59           N  
-ATOM   9236  CA  PHE C 183     -23.716  36.335-109.454  1.00 16.77           C  
-ATOM   9237  C   PHE C 183     -22.800  35.583-108.495  1.00 19.29           C  
-ATOM   9238  O   PHE C 183     -22.338  36.135-107.497  1.00 31.18           O  
-ATOM   9239  CB  PHE C 183     -22.871  36.947-110.575  1.00 16.07           C  
-ATOM   9240  CG  PHE C 183     -23.679  37.614-111.649  1.00 15.93           C  
-ATOM   9241  CD1 PHE C 183     -24.134  38.912-111.489  1.00 15.91           C  
-ATOM   9242  CD2 PHE C 183     -23.975  36.947-112.826  1.00 17.69           C  
-ATOM   9243  CE1 PHE C 183     -24.878  39.526-112.478  1.00 27.18           C  
-ATOM   9244  CE2 PHE C 183     -24.717  37.554-113.818  1.00 17.12           C  
-ATOM   9245  CZ  PHE C 183     -25.169  38.845-113.645  1.00 23.63           C  
-ATOM   9246  N   PHE C 184     -22.542  34.318-108.810  1.00 19.98           N  
-ATOM   9247  CA  PHE C 184     -21.546  33.535-108.088  1.00 22.10           C  
-ATOM   9248  C   PHE C 184     -20.168  34.047-108.489  1.00 28.64           C  
-ATOM   9249  O   PHE C 184     -19.921  34.296-109.670  1.00 27.13           O  
-ATOM   9250  CB  PHE C 184     -21.691  32.042-108.400  1.00 21.28           C  
-ATOM   9251  CG  PHE C 184     -20.859  31.149-107.521  1.00 26.68           C  
-ATOM   9252  CD1 PHE C 184     -21.340  30.722-106.294  1.00 31.95           C  
-ATOM   9253  CD2 PHE C 184     -19.600  30.732-107.921  1.00 26.03           C  
-ATOM   9254  CE1 PHE C 184     -20.582  29.897-105.481  1.00 22.33           C  
-ATOM   9255  CE2 PHE C 184     -18.836  29.909-107.111  1.00 23.93           C  
-ATOM   9256  CZ  PHE C 184     -19.329  29.492-105.889  1.00 22.04           C  
-ATOM   9257  N   PRO C 185     -19.268  34.217-107.508  1.00 27.28           N  
-ATOM   9258  CA  PRO C 185     -17.951  34.806-107.779  1.00 25.62           C  
-ATOM   9259  C   PRO C 185     -17.123  34.005-108.783  1.00 28.45           C  
-ATOM   9260  O   PRO C 185     -17.387  32.823-109.008  1.00 22.56           O  
-ATOM   9261  CB  PRO C 185     -17.280  34.811-106.402  1.00 20.78           C  
-ATOM   9262  CG  PRO C 185     -18.014  33.781-105.610  1.00 20.66           C  
-ATOM   9263  CD  PRO C 185     -19.427  33.849-106.091  1.00 19.83           C  
-ATOM   9264  N   ALA C 186     -16.135  34.659-109.386  1.00 30.28           N  
-ATOM   9265  CA  ALA C 186     -15.231  33.989-110.311  1.00 24.40           C  
-ATOM   9266  C   ALA C 186     -14.256  33.111-109.537  1.00 22.84           C  
-ATOM   9267  O   ALA C 186     -13.655  33.554-108.559  1.00 30.80           O  
-ATOM   9268  CB  ALA C 186     -14.483  35.007-111.160  1.00 23.52           C  
-ATOM   9269  N   PHE C 187     -14.108  31.865-109.972  1.00 25.08           N  
-ATOM   9270  CA  PHE C 187     -13.227  30.923-109.291  1.00 27.00           C  
-ATOM   9271  C   PHE C 187     -12.404  30.122-110.291  1.00 29.67           C  
-ATOM   9272  O   PHE C 187     -12.879  29.822-111.385  1.00 30.58           O  
-ATOM   9273  CB  PHE C 187     -14.039  29.981-108.396  1.00 27.17           C  
-ATOM   9274  CG  PHE C 187     -14.987  29.090-109.149  1.00 24.51           C  
-ATOM   9275  CD1 PHE C 187     -16.255  29.532-109.482  1.00 23.14           C  
-ATOM   9276  CD2 PHE C 187     -14.614  27.806-109.514  1.00 24.87           C  
-ATOM   9277  CE1 PHE C 187     -17.129  28.715-110.171  1.00 22.95           C  
-ATOM   9278  CE2 PHE C 187     -15.485  26.986-110.202  1.00 19.28           C  
-ATOM   9279  CZ  PHE C 187     -16.744  27.442-110.531  1.00 18.52           C  
-ATOM   9280  N   PRO C 188     -11.162  29.773-109.919  1.00 30.63           N  
-ATOM   9281  CA  PRO C 188     -10.297  28.968-110.788  1.00 32.45           C  
-ATOM   9282  C   PRO C 188     -10.941  27.640-111.173  1.00 32.50           C  
-ATOM   9283  O   PRO C 188     -11.227  26.811-110.307  1.00 33.08           O  
-ATOM   9284  CB  PRO C 188      -9.042  28.744-109.931  1.00 33.93           C  
-ATOM   9285  CG  PRO C 188      -9.466  29.044-108.528  1.00 33.30           C  
-ATOM   9286  CD  PRO C 188     -10.498  30.115-108.652  1.00 31.28           C  
-ATOM   9287  N   GLY C 189     -11.179  27.455-112.467  1.00 33.01           N  
-ATOM   9288  CA  GLY C 189     -11.789  26.236-112.959  1.00 33.87           C  
-ATOM   9289  C   GLY C 189     -13.275  26.390-113.211  1.00 30.42           C  
-ATOM   9290  O   GLY C 189     -14.024  25.418-113.136  1.00 31.10           O  
-ATOM   9291  N   ASP C 190     -13.703  27.612-113.515  1.00 24.27           N  
-ATOM   9292  CA  ASP C 190     -15.102  27.879-113.833  1.00 20.81           C  
-ATOM   9293  C   ASP C 190     -15.401  27.594-115.305  1.00 21.76           C  
-ATOM   9294  O   ASP C 190     -16.467  27.940-115.816  1.00 25.46           O  
-ATOM   9295  CB  ASP C 190     -15.462  29.323-113.488  1.00 23.65           C  
-ATOM   9296  CG  ASP C 190     -14.370  30.297-113.867  1.00 31.40           C  
-ATOM   9297  OD1 ASP C 190     -13.472  29.906-114.643  1.00 39.49           O  
-ATOM   9298  OD2 ASP C 190     -14.407  31.448-113.385  1.00 27.10           O  
-ATOM   9299  N   ASP C 191     -14.456  26.943-115.975  1.00 26.11           N  
-ATOM   9300  CA  ASP C 191     -14.618  26.553-117.371  1.00 23.28           C  
-ATOM   9301  C   ASP C 191     -15.727  25.513-117.536  1.00 34.05           C  
-ATOM   9302  O   ASP C 191     -16.139  25.207-118.655  1.00 36.19           O  
-ATOM   9303  CB  ASP C 191     -13.299  26.012-117.930  1.00 14.06           C  
-ATOM   9304  N   ILE C 192     -16.204  24.970-116.417  1.00 26.58           N  
-ATOM   9305  CA  ILE C 192     -17.330  24.040-116.432  1.00 29.17           C  
-ATOM   9306  C   ILE C 192     -18.651  24.781-116.599  1.00 26.78           C  
-ATOM   9307  O   ILE C 192     -19.707  24.164-116.728  1.00 31.03           O  
-ATOM   9308  CB  ILE C 192     -17.396  23.191-115.145  1.00 21.57           C  
-ATOM   9309  CG1 ILE C 192     -16.674  23.898-114.000  1.00 20.48           C  
-ATOM   9310  CG2 ILE C 192     -16.785  21.822-115.372  1.00 22.64           C  
-ATOM   9311  CD1 ILE C 192     -17.471  25.007-113.367  1.00 23.55           C  
-ATOM   9312  N   LEU C 193     -18.588  26.108-116.594  1.00 22.50           N  
-ATOM   9313  CA  LEU C 193     -19.783  26.926-116.755  1.00 20.64           C  
-ATOM   9314  C   LEU C 193     -19.914  27.446-118.182  1.00 21.92           C  
-ATOM   9315  O   LEU C 193     -20.920  27.207-118.849  1.00 28.75           O  
-ATOM   9316  CB  LEU C 193     -19.763  28.086-115.764  1.00 19.84           C  
-ATOM   9317  CG  LEU C 193     -19.759  27.617-114.309  1.00 20.90           C  
-ATOM   9318  CD1 LEU C 193     -19.325  28.735-113.383  1.00 28.26           C  
-ATOM   9319  CD2 LEU C 193     -21.125  27.075-113.908  1.00 18.29           C  
-ATOM   9320  N   SER C 194     -18.895  28.160-118.645  1.00 20.17           N  
-ATOM   9321  CA  SER C 194     -18.876  28.658-120.014  1.00 20.91           C  
-ATOM   9322  C   SER C 194     -17.441  28.776-120.512  1.00 27.63           C  
-ATOM   9323  O   SER C 194     -16.501  28.354-119.835  1.00 20.73           O  
-ATOM   9324  CB  SER C 194     -19.587  30.009-120.114  1.00 28.77           C  
-ATOM   9325  OG  SER C 194     -18.937  31.002-119.335  1.00 32.95           O  
-ATOM   9326  N   ASN C 195     -17.277  29.345-121.700  1.00 27.91           N  
-ATOM   9327  CA  ASN C 195     -15.954  29.516-122.280  1.00 19.77           C  
-ATOM   9328  C   ASN C 195     -15.306  30.814-121.815  1.00 24.58           C  
-ATOM   9329  O   ASN C 195     -15.993  31.796-121.533  1.00 30.06           O  
-ATOM   9330  CB  ASN C 195     -16.037  29.480-123.805  1.00 22.60           C  
-ATOM   9331  CG  ASN C 195     -16.504  28.136-124.331  1.00 29.20           C  
-ATOM   9332  OD1 ASN C 195     -16.835  27.235-123.558  1.00 28.53           O  
-ATOM   9333  ND2 ASN C 195     -16.538  27.995-125.651  1.00 30.00           N  
-ATOM   9334  N   LYS C 196     -13.980  30.812-121.730  1.00 26.16           N  
-ATOM   9335  CA  LYS C 196     -13.241  32.001-121.322  1.00 38.49           C  
-ATOM   9336  C   LYS C 196     -12.745  32.794-122.530  1.00 42.01           C  
-ATOM   9337  O   LYS C 196     -12.775  34.027-122.533  1.00 38.52           O  
-ATOM   9338  CB  LYS C 196     -12.062  31.616-120.425  1.00 37.88           C  
-ATOM   9339  CG  LYS C 196     -12.459  31.215-119.014  1.00 28.66           C  
-ATOM   9340  CD  LYS C 196     -13.285  32.308-118.357  1.00 27.65           C  
-ATOM   9341  CE  LYS C 196     -13.286  32.163-116.848  1.00 25.78           C  
-ATOM   9342  NZ  LYS C 196     -11.905  32.226-116.297  1.00 18.48           N  
-ATOM   9343  N   ALA C 225      -4.578  27.093-105.984  1.00 41.27           N  
-ATOM   9344  CA  ALA C 225      -5.396  25.885-106.046  1.00 55.60           C  
-ATOM   9345  C   ALA C 225      -6.616  26.070-106.948  1.00 51.17           C  
-ATOM   9346  O   ALA C 225      -7.272  27.111-106.913  1.00 42.45           O  
-ATOM   9347  CB  ALA C 225      -5.834  25.474-104.648  1.00 60.54           C  
-ATOM   9348  N   THR C 226      -6.918  25.053-107.750  1.00 53.15           N  
-ATOM   9349  CA  THR C 226      -8.079  25.094-108.632  1.00 43.01           C  
-ATOM   9350  C   THR C 226      -9.158  24.115-108.168  1.00 38.72           C  
-ATOM   9351  O   THR C 226      -8.872  23.152-107.453  1.00 34.63           O  
-ATOM   9352  CB  THR C 226      -7.695  24.772-110.094  1.00 37.87           C  
-ATOM   9353  OG1 THR C 226      -8.832  24.960-110.947  1.00 37.86           O  
-ATOM   9354  CG2 THR C 226      -7.206  23.339-110.218  1.00 43.27           C  
-ATOM   9355  N   TYR C 227     -10.399  24.377-108.569  1.00 36.82           N  
-ATOM   9356  CA  TYR C 227     -11.525  23.518-108.217  1.00 32.98           C  
-ATOM   9357  C   TYR C 227     -11.917  22.635-109.399  1.00 39.05           C  
-ATOM   9358  O   TYR C 227     -12.611  23.086-110.311  1.00 39.97           O  
-ATOM   9359  CB  TYR C 227     -12.721  24.361-107.763  1.00 30.86           C  
-ATOM   9360  CG  TYR C 227     -12.535  25.030-106.417  1.00 34.54           C  
-ATOM   9361  CD1 TYR C 227     -11.849  26.233-106.304  1.00 34.41           C  
-ATOM   9362  CD2 TYR C 227     -13.056  24.462-105.259  1.00 29.52           C  
-ATOM   9363  CE1 TYR C 227     -11.680  26.846-105.074  1.00 43.31           C  
-ATOM   9364  CE2 TYR C 227     -12.892  25.068-104.027  1.00 27.90           C  
-ATOM   9365  CZ  TYR C 227     -12.204  26.260-103.939  1.00 43.45           C  
-ATOM   9366  OH  TYR C 227     -12.040  26.865-102.711  1.00 39.73           O  
-ATOM   9367  N   ARG C 228     -11.478  21.378-109.377  1.00 40.08           N  
-ATOM   9368  CA  ARG C 228     -11.690  20.476-110.510  1.00 34.81           C  
-ATOM   9369  C   ARG C 228     -12.852  19.508-110.298  1.00 33.34           C  
-ATOM   9370  O   ARG C 228     -13.057  19.011-109.195  1.00 36.02           O  
-ATOM   9371  CB  ARG C 228     -10.415  19.682-110.807  1.00 36.75           C  
-ATOM   9372  CG  ARG C 228      -9.328  20.485-111.500  1.00 54.10           C  
-ATOM   9373  CD  ARG C 228      -8.368  19.571-112.244  1.00 54.04           C  
-ATOM   9374  NE  ARG C 228      -7.943  18.446-111.416  1.00 69.96           N  
-ATOM   9375  CZ  ARG C 228      -6.951  18.502-110.533  1.00 81.38           C  
-ATOM   9376  NH1 ARG C 228      -6.279  19.633-110.358  1.00 74.69           N  
-ATOM   9377  NH2 ARG C 228      -6.632  17.427-109.822  1.00 65.75           N  
-ATOM   9378  N   PRO C 229     -13.611  19.230-111.372  1.00 30.63           N  
-ATOM   9379  CA  PRO C 229     -14.763  18.324-111.318  1.00 26.01           C  
-ATOM   9380  C   PRO C 229     -14.376  16.873-111.067  1.00 29.94           C  
-ATOM   9381  O   PRO C 229     -13.343  16.407-111.549  1.00 28.19           O  
-ATOM   9382  CB  PRO C 229     -15.394  18.481-112.703  1.00 27.07           C  
-ATOM   9383  CG  PRO C 229     -14.277  18.898-113.574  1.00 32.55           C  
-ATOM   9384  CD  PRO C 229     -13.416  19.782-112.723  1.00 28.78           C  
-ATOM   9385  N   ILE C 230     -15.215  16.172-110.313  1.00 35.07           N  
-ATOM   9386  CA  ILE C 230     -14.985  14.770-109.992  1.00 28.77           C  
-ATOM   9387  C   ILE C 230     -16.261  13.984-110.306  1.00 30.71           C  
-ATOM   9388  O   ILE C 230     -16.291  12.748-110.286  1.00 35.25           O  
-ATOM   9389  CB  ILE C 230     -14.588  14.601-108.506  1.00 32.28           C  
-ATOM   9390  CG1 ILE C 230     -13.750  13.340-108.303  1.00 62.99           C  
-ATOM   9391  CG2 ILE C 230     -15.821  14.623-107.603  1.00 20.75           C  
-ATOM   9392  CD1 ILE C 230     -12.259  13.607-108.139  1.00 64.46           C  
-ATOM   9393  N   PHE C 231     -17.305  14.739-110.631  1.00 28.36           N  
-ATOM   9394  CA  PHE C 231     -18.663  14.235-110.759  1.00 25.88           C  
-ATOM   9395  C   PHE C 231     -19.393  15.050-111.818  1.00 29.18           C  
-ATOM   9396  O   PHE C 231     -19.514  16.265-111.686  1.00 27.40           O  
-ATOM   9397  CB  PHE C 231     -19.380  14.331-109.403  1.00 28.05           C  
-ATOM   9398  CG  PHE C 231     -20.803  13.821-109.402  1.00 30.67           C  
-ATOM   9399  CD1 PHE C 231     -21.826  14.533-110.013  1.00 24.69           C  
-ATOM   9400  CD2 PHE C 231     -21.124  12.653-108.734  1.00 35.67           C  
-ATOM   9401  CE1 PHE C 231     -23.127  14.066-109.992  1.00 27.97           C  
-ATOM   9402  CE2 PHE C 231     -22.424  12.186-108.701  1.00 34.15           C  
-ATOM   9403  CZ  PHE C 231     -23.426  12.892-109.335  1.00 28.93           C  
-ATOM   9404  N   ILE C 232     -19.875  14.397-112.869  1.00 30.09           N  
-ATOM   9405  CA  ILE C 232     -20.762  15.066-113.818  1.00 19.35           C  
-ATOM   9406  C   ILE C 232     -21.925  14.142-114.162  1.00 22.17           C  
-ATOM   9407  O   ILE C 232     -21.719  13.034-114.656  1.00 27.00           O  
-ATOM   9408  CB  ILE C 232     -20.036  15.487-115.115  1.00 22.22           C  
-ATOM   9409  CG1 ILE C 232     -18.798  16.336-114.805  1.00 17.79           C  
-ATOM   9410  CG2 ILE C 232     -20.987  16.257-116.023  1.00 19.31           C  
-ATOM   9411  CD1 ILE C 232     -18.039  16.795-116.035  1.00 13.98           C  
-ATOM   9412  N   SER C 233     -23.146  14.605-113.901  1.00 20.01           N  
-ATOM   9413  CA  SER C 233     -24.342  13.779-114.062  1.00 20.63           C  
-ATOM   9414  C   SER C 233     -24.960  13.898-115.449  1.00 20.30           C  
-ATOM   9415  O   SER C 233     -24.492  14.672-116.285  1.00 25.42           O  
-ATOM   9416  CB  SER C 233     -25.388  14.155-113.014  1.00 24.61           C  
-ATOM   9417  OG  SER C 233     -25.947  15.429-113.287  1.00 13.49           O  
-ATOM   9418  N   LYS C 234     -26.019  13.128-115.686  1.00 19.73           N  
-ATOM   9419  CA  LYS C 234     -26.778  13.244-116.926  1.00 20.35           C  
-ATOM   9420  C   LYS C 234     -27.649  14.493-116.852  1.00 19.42           C  
-ATOM   9421  O   LYS C 234     -27.885  15.024-115.769  1.00 19.78           O  
-ATOM   9422  CB  LYS C 234     -27.634  11.996-117.176  1.00 17.79           C  
-ATOM   9423  CG  LYS C 234     -29.076  12.120-116.711  1.00 22.73           C  
-ATOM   9424  CD  LYS C 234     -29.284  11.474-115.354  1.00 34.10           C  
-ATOM   9425  CE  LYS C 234     -29.577   9.990-115.487  1.00 27.12           C  
-ATOM   9426  NZ  LYS C 234     -30.887   9.760-116.152  1.00 27.29           N  
-ATOM   9427  N   THR C 235     -28.122  14.966-117.998  1.00 21.43           N  
-ATOM   9428  CA  THR C 235     -28.917  16.186-118.023  1.00 18.98           C  
-ATOM   9429  C   THR C 235     -30.368  15.944-117.608  1.00 24.81           C  
-ATOM   9430  O   THR C 235     -31.046  15.067-118.145  1.00 24.25           O  
-ATOM   9431  CB  THR C 235     -28.902  16.836-119.413  1.00 12.70           C  
-ATOM   9432  OG1 THR C 235     -27.549  17.114-119.795  1.00 16.64           O  
-ATOM   9433  CG2 THR C 235     -29.694  18.128-119.393  1.00 10.29           C  
-ATOM   9434  N   PHE C 236     -30.825  16.730-116.636  1.00 21.51           N  
-ATOM   9435  CA  PHE C 236     -32.219  16.744-116.211  1.00 18.82           C  
-ATOM   9436  C   PHE C 236     -32.900  17.981-116.768  1.00 20.62           C  
-ATOM   9437  O   PHE C 236     -32.234  18.873-117.294  1.00 23.65           O  
-ATOM   9438  CB  PHE C 236     -32.332  16.750-114.689  1.00 20.76           C  
-ATOM   9439  CG  PHE C 236     -31.719  15.558-114.023  1.00 20.03           C  
-ATOM   9440  CD1 PHE C 236     -30.352  15.479-113.832  1.00 21.25           C  
-ATOM   9441  CD2 PHE C 236     -32.516  14.527-113.564  1.00 24.54           C  
-ATOM   9442  CE1 PHE C 236     -29.791  14.385-113.212  1.00 27.97           C  
-ATOM   9443  CE2 PHE C 236     -31.962  13.432-112.942  1.00 26.48           C  
-ATOM   9444  CZ  PHE C 236     -30.598  13.360-112.763  1.00 32.48           C  
-ATOM   9445  N   SER C 237     -34.220  18.053-116.636  1.00 23.90           N  
-ATOM   9446  CA  SER C 237     -34.939  19.259-117.030  1.00 22.89           C  
-ATOM   9447  C   SER C 237     -36.322  19.353-116.401  1.00 23.78           C  
-ATOM   9448  O   SER C 237     -37.069  18.374-116.360  1.00 24.23           O  
-ATOM   9449  CB  SER C 237     -35.070  19.333-118.551  1.00 18.15           C  
-ATOM   9450  OG  SER C 237     -36.058  18.432-119.012  1.00 35.79           O  
-ATOM   9451  N   ASP C 238     -36.645  20.546-115.912  1.00 22.27           N  
-ATOM   9452  CA  ASP C 238     -37.987  20.870-115.444  1.00 26.01           C  
-ATOM   9453  C   ASP C 238     -38.380  22.235-115.995  1.00 24.25           C  
-ATOM   9454  O   ASP C 238     -37.530  23.123-116.121  1.00 28.38           O  
-ATOM   9455  CB  ASP C 238     -38.060  20.866-113.915  1.00 20.73           C  
-ATOM   9456  CG  ASP C 238     -37.572  19.564-113.312  1.00 29.59           C  
-ATOM   9457  OD1 ASP C 238     -38.287  18.546-113.431  1.00 29.42           O  
-ATOM   9458  OD2 ASP C 238     -36.474  19.558-112.718  1.00 32.62           O  
-ATOM   9459  N   ASN C 239     -39.657  22.384-116.340  1.00 20.27           N  
-ATOM   9460  CA  ASN C 239     -40.196  23.643-116.857  1.00 20.48           C  
-ATOM   9461  C   ASN C 239     -39.366  24.276-117.971  1.00 17.82           C  
-ATOM   9462  O   ASN C 239     -39.083  25.476-117.937  1.00 11.29           O  
-ATOM   9463  CB  ASN C 239     -40.361  24.646-115.717  1.00 16.30           C  
-ATOM   9464  CG  ASN C 239     -41.561  24.341-114.845  1.00 19.32           C  
-ATOM   9465  OD1 ASN C 239     -41.421  24.049-113.659  1.00 29.64           O  
-ATOM   9466  ND2 ASN C 239     -42.751  24.410-115.430  1.00 16.36           N  
-ATOM   9467  N   GLY C 240     -38.980  23.463-118.951  1.00 14.59           N  
-ATOM   9468  CA  GLY C 240     -38.253  23.947-120.111  1.00 11.83           C  
-ATOM   9469  C   GLY C 240     -36.848  24.419-119.798  1.00 11.99           C  
-ATOM   9470  O   GLY C 240     -36.236  25.136-120.590  1.00  7.03           O  
-ATOM   9471  N   VAL C 241     -36.333  24.021-118.639  1.00 18.73           N  
-ATOM   9472  CA  VAL C 241     -34.983  24.400-118.243  1.00 15.82           C  
-ATOM   9473  C   VAL C 241     -34.097  23.168-118.107  1.00 21.72           C  
-ATOM   9474  O   VAL C 241     -34.305  22.361-117.205  1.00 20.92           O  
-ATOM   9475  CB  VAL C 241     -34.970  25.168-116.901  1.00 18.23           C  
-ATOM   9476  CG1 VAL C 241     -33.581  25.704-116.610  1.00 18.73           C  
-ATOM   9477  CG2 VAL C 241     -35.990  26.293-116.908  1.00 20.58           C  
-ATOM   9478  N   PRO C 242     -33.103  23.019-119.001  1.00 22.36           N  
-ATOM   9479  CA  PRO C 242     -32.110  21.945-118.895  1.00 17.13           C  
-ATOM   9480  C   PRO C 242     -31.013  22.266-117.893  1.00 15.44           C  
-ATOM   9481  O   PRO C 242     -30.513  23.391-117.874  1.00 21.09           O  
-ATOM   9482  CB  PRO C 242     -31.520  21.883-120.300  1.00 15.39           C  
-ATOM   9483  CG  PRO C 242     -31.567  23.304-120.751  1.00 14.19           C  
-ATOM   9484  CD  PRO C 242     -32.851  23.867-120.181  1.00 15.04           C  
-ATOM   9485  N   TYR C 243     -30.620  21.282-117.094  1.00 13.96           N  
-ATOM   9486  CA  TYR C 243     -29.550  21.489-116.126  1.00 17.15           C  
-ATOM   9487  C   TYR C 243     -28.937  20.180-115.642  1.00 14.17           C  
-ATOM   9488  O   TYR C 243     -29.577  19.139-115.708  1.00 15.59           O  
-ATOM   9489  CB  TYR C 243     -30.076  22.292-114.935  1.00 17.62           C  
-ATOM   9490  CG  TYR C 243     -31.199  21.635-114.168  1.00 18.43           C  
-ATOM   9491  CD1 TYR C 243     -32.520  21.803-114.556  1.00 19.87           C  
-ATOM   9492  CD2 TYR C 243     -30.939  20.867-113.040  1.00 17.69           C  
-ATOM   9493  CE1 TYR C 243     -33.553  21.214-113.849  1.00 23.54           C  
-ATOM   9494  CE2 TYR C 243     -31.964  20.274-112.327  1.00 18.42           C  
-ATOM   9495  CZ  TYR C 243     -33.269  20.453-112.736  1.00 19.73           C  
-ATOM   9496  OH  TYR C 243     -34.296  19.870-112.035  1.00 20.66           O  
-ATOM   9497  N   ASP C 244     -27.699  20.228-115.152  1.00 15.45           N  
-ATOM   9498  CA  ASP C 244     -27.097  19.028-114.561  1.00 20.61           C  
-ATOM   9499  C   ASP C 244     -26.360  19.327-113.256  1.00 18.82           C  
-ATOM   9500  O   ASP C 244     -26.214  20.483-112.867  1.00 18.09           O  
-ATOM   9501  CB  ASP C 244     -26.147  18.330-115.553  1.00 22.72           C  
-ATOM   9502  CG  ASP C 244     -24.959  19.197-115.966  1.00 20.02           C  
-ATOM   9503  OD1 ASP C 244     -24.815  20.326-115.455  1.00 20.49           O  
-ATOM   9504  OD2 ASP C 244     -24.155  18.739-116.806  1.00 17.32           O  
-ATOM   9505  N   PHE C 245     -25.897  18.277-112.587  1.00 19.60           N  
-ATOM   9506  CA  PHE C 245     -25.235  18.421-111.294  1.00 19.22           C  
-ATOM   9507  C   PHE C 245     -23.766  18.032-111.368  1.00 19.23           C  
-ATOM   9508  O   PHE C 245     -23.426  16.956-111.858  1.00 23.22           O  
-ATOM   9509  CB  PHE C 245     -25.936  17.568-110.233  1.00 17.25           C  
-ATOM   9510  CG  PHE C 245     -27.416  17.790-110.159  1.00 19.39           C  
-ATOM   9511  CD1 PHE C 245     -28.288  17.008-110.900  1.00 21.85           C  
-ATOM   9512  CD2 PHE C 245     -27.939  18.776-109.344  1.00 25.13           C  
-ATOM   9513  CE1 PHE C 245     -29.652  17.211-110.831  1.00 19.25           C  
-ATOM   9514  CE2 PHE C 245     -29.299  18.983-109.271  1.00 27.06           C  
-ATOM   9515  CZ  PHE C 245     -30.157  18.200-110.016  1.00 25.89           C  
-ATOM   9516  N   VAL C 246     -22.896  18.910-110.880  1.00 17.59           N  
-ATOM   9517  CA  VAL C 246     -21.480  18.587-110.787  1.00 22.43           C  
-ATOM   9518  C   VAL C 246     -20.935  18.843-109.390  1.00 20.72           C  
-ATOM   9519  O   VAL C 246     -21.419  19.715-108.662  1.00 24.96           O  
-ATOM   9520  CB  VAL C 246     -20.629  19.387-111.791  1.00 15.86           C  
-ATOM   9521  CG1 VAL C 246     -20.970  18.989-113.218  1.00 18.35           C  
-ATOM   9522  CG2 VAL C 246     -20.800  20.880-111.568  1.00 16.43           C  
-ATOM   9523  N   VAL C 247     -19.923  18.065-109.027  1.00 17.84           N  
-ATOM   9524  CA  VAL C 247     -19.218  18.260-107.776  1.00 18.45           C  
-ATOM   9525  C   VAL C 247     -17.761  18.586-108.067  1.00 23.51           C  
-ATOM   9526  O   VAL C 247     -17.042  17.799-108.691  1.00 24.72           O  
-ATOM   9527  CB  VAL C 247     -19.306  17.020-106.865  1.00 23.14           C  
-ATOM   9528  CG1 VAL C 247     -18.588  17.281-105.549  1.00 30.65           C  
-ATOM   9529  CG2 VAL C 247     -20.759  16.641-106.619  1.00 17.58           C  
-ATOM   9530  N   LEU C 248     -17.339  19.765-107.627  1.00 22.51           N  
-ATOM   9531  CA  LEU C 248     -15.955  20.181-107.764  1.00 23.64           C  
-ATOM   9532  C   LEU C 248     -15.213  19.935-106.458  1.00 35.79           C  
-ATOM   9533  O   LEU C 248     -15.821  19.859-105.387  1.00 24.61           O  
-ATOM   9534  CB  LEU C 248     -15.861  21.656-108.157  1.00 25.14           C  
-ATOM   9535  CG  LEU C 248     -16.738  22.149-109.311  1.00 21.92           C  
-ATOM   9536  CD1 LEU C 248     -16.337  23.557-109.704  1.00 27.27           C  
-ATOM   9537  CD2 LEU C 248     -16.659  21.226-110.508  1.00 24.02           C  
-ATOM   9538  N   GLU C 249     -13.894  19.818-106.561  1.00 40.64           N  
-ATOM   9539  CA  GLU C 249     -13.044  19.507-105.424  1.00 30.04           C  
-ATOM   9540  C   GLU C 249     -11.804  20.391-105.459  1.00 28.30           C  
-ATOM   9541  O   GLU C 249     -11.290  20.709-106.534  1.00 29.22           O  
-ATOM   9542  CB  GLU C 249     -12.659  18.026-105.444  1.00 34.74           C  
-ATOM   9543  CG  GLU C 249     -11.794  17.556-104.288  1.00 43.71           C  
-ATOM   9544  CD  GLU C 249     -11.428  16.088-104.412  1.00 53.97           C  
-ATOM   9545  OE1 GLU C 249     -11.999  15.264-103.664  1.00 37.52           O  
-ATOM   9546  OE2 GLU C 249     -10.576  15.758-105.265  1.00 53.79           O  
-ATOM   9547  N   LYS C 250     -11.341  20.808-104.285  1.00 36.33           N  
-ATOM   9548  CA  LYS C 250     -10.115  21.593-104.188  1.00 40.46           C  
-ATOM   9549  C   LYS C 250      -8.911  20.673-104.385  1.00 52.60           C  
-ATOM   9550  O   LYS C 250      -8.800  19.639-103.724  1.00 59.22           O  
-ATOM   9551  CB  LYS C 250     -10.039  22.313-102.842  1.00 36.47           C  
-ATOM   9552  CG  LYS C 250      -9.061  23.477-102.818  1.00 48.13           C  
-ATOM   9553  CD  LYS C 250      -9.298  24.377-101.616  1.00 41.62           C  
-ATOM   9554  CE  LYS C 250      -8.478  25.651-101.721  1.00 43.98           C  
-ATOM   9555  NZ  LYS C 250      -8.787  26.607-100.627  1.00 42.54           N  
-ATOM   9556  N   ARG C 251      -8.013  21.042-105.294  1.00 50.33           N  
-ATOM   9557  CA  ARG C 251      -6.958  20.119-105.705  1.00 60.48           C  
-ATOM   9558  C   ARG C 251      -5.530  20.654-105.598  1.00 77.16           C  
-ATOM   9559  O   ARG C 251      -4.607  19.892-105.294  1.00 81.30           O  
-ATOM   9560  CB  ARG C 251      -7.212  19.657-107.144  1.00 54.21           C  
-ATOM   9561  CG  ARG C 251      -8.282  18.586-107.266  1.00 58.12           C  
-ATOM   9562  CD  ARG C 251      -8.039  17.467-106.263  1.00 65.36           C  
-ATOM   9563  NE  ARG C 251      -6.668  16.965-106.316  1.00 88.28           N  
-ATOM   9564  CZ  ARG C 251      -6.115  16.199-105.380  1.00 80.55           C  
-ATOM   9565  NH1 ARG C 251      -4.859  15.790-105.511  1.00 59.23           N  
-ATOM   9566  NH2 ARG C 251      -6.816  15.843-104.312  1.00 69.97           N  
-ATOM   9567  N   ARG C 252      -5.350  21.947-105.861  1.00 65.54           N  
-ATOM   9568  CA  ARG C 252      -4.023  22.564-105.864  1.00 65.61           C  
-ATOM   9569  C   ARG C 252      -3.074  21.876-106.843  1.00 68.14           C  
-ATOM   9570  O   ARG C 252      -2.991  22.249-108.014  1.00 60.76           O  
-ATOM   9571  CB  ARG C 252      -3.414  22.555-104.457  1.00 62.98           C  
-ATOM   9572  CG  ARG C 252      -1.914  22.808-104.435  1.00 66.83           C  
-ATOM   9573  CD  ARG C 252      -1.287  22.362-103.122  1.00 74.97           C  
-ATOM   9574  NE  ARG C 252      -0.082  21.567-103.346  1.00 84.91           N  
-ATOM   9575  CZ  ARG C 252       1.138  22.077-103.486  1.00 87.67           C  
-ATOM   9576  NH1 ARG C 252       1.323  23.388-103.421  1.00 79.36           N  
-ATOM   9577  NH2 ARG C 252       2.174  21.274-103.692  1.00 83.91           N  
-ATOM   9578  N   SER C 285     -11.290 -18.679 -97.109  1.00 72.52           N  
-ATOM   9579  CA  SER C 285     -11.114 -18.390 -98.528  1.00 92.19           C  
-ATOM   9580  C   SER C 285     -12.449 -18.378 -99.269  1.00 83.95           C  
-ATOM   9581  O   SER C 285     -12.808 -19.346 -99.940  1.00 79.47           O  
-ATOM   9582  CB  SER C 285     -10.164 -19.407 -99.163  1.00 84.43           C  
-ATOM   9583  OG  SER C 285     -10.364 -20.700 -98.620  1.00 77.30           O  
-ATOM   9584  N   SER C 286     -13.178 -17.273 -99.144  1.00 89.40           N  
-ATOM   9585  CA  SER C 286     -14.476 -17.130 -99.795  1.00 98.19           C  
-ATOM   9586  C   SER C 286     -14.320 -17.084-101.313  1.00 96.38           C  
-ATOM   9587  O   SER C 286     -14.524 -18.086-102.002  1.00 79.35           O  
-ATOM   9588  CB  SER C 286     -15.192 -15.870 -99.298  1.00 81.16           C  
-ATOM   9589  OG  SER C 286     -15.358 -15.893 -97.890  1.00 59.77           O  
-ATOM   9590  N   ALA C 287     -13.952 -15.915-101.825  1.00 91.27           N  
-ATOM   9591  CA  ALA C 287     -13.764 -15.734-103.257  1.00 76.18           C  
-ATOM   9592  C   ALA C 287     -12.340 -15.286-103.552  1.00 75.97           C  
-ATOM   9593  O   ALA C 287     -11.918 -15.228-104.707  1.00 82.05           O  
-ATOM   9594  CB  ALA C 287     -14.767 -14.729-103.802  1.00 73.90           C  
-ATOM   9595  N   ALA C 288     -11.602 -14.982-102.490  1.00 76.18           N  
-ATOM   9596  CA  ALA C 288     -10.251 -14.448-102.604  1.00 86.51           C  
-ATOM   9597  C   ALA C 288      -9.259 -15.471-103.156  1.00 93.13           C  
-ATOM   9598  O   ALA C 288      -8.236 -15.102-103.733  1.00 82.60           O  
-ATOM   9599  CB  ALA C 288      -9.779 -13.938-101.250  1.00 67.51           C  
-ATOM   9600  N   ALA C 289      -9.565 -16.754-102.983  1.00 89.57           N  
-ATOM   9601  CA  ALA C 289      -8.670 -17.817-103.431  1.00 95.51           C  
-ATOM   9602  C   ALA C 289      -8.848 -18.115-104.918  1.00103.36           C  
-ATOM   9603  O   ALA C 289      -8.241 -19.043-105.454  1.00100.85           O  
-ATOM   9604  CB  ALA C 289      -8.897 -19.075-102.613  1.00 88.26           C  
-ATOM   9605  N   ILE C 290      -9.682 -17.321-105.581  1.00104.07           N  
-ATOM   9606  CA  ILE C 290      -9.987 -17.536-106.989  1.00 94.51           C  
-ATOM   9607  C   ILE C 290      -9.417 -16.388-107.827  1.00 92.88           C  
-ATOM   9608  O   ILE C 290      -9.451 -16.412-109.058  1.00 88.65           O  
-ATOM   9609  CB  ILE C 290     -11.504 -17.683-107.195  1.00 84.32           C  
-ATOM   9610  CG1 ILE C 290     -12.069 -18.611-106.116  1.00 92.44           C  
-ATOM   9611  CG2 ILE C 290     -11.817 -18.234-108.580  1.00 75.01           C  
-ATOM   9612  CD1 ILE C 290     -13.459 -18.267-105.665  1.00 93.92           C  
-ATOM   9613  N   ALA C 291      -8.867 -15.394-107.137  1.00 98.05           N  
-ATOM   9614  CA  ALA C 291      -8.117 -14.317-107.775  1.00 97.85           C  
-ATOM   9615  C   ALA C 291      -6.805 -14.751-108.466  1.00 96.24           C  
-ATOM   9616  O   ALA C 291      -6.317 -14.029-109.335  1.00 92.89           O  
-ATOM   9617  CB  ALA C 291      -7.820 -13.226-106.752  1.00 95.29           C  
-ATOM   9618  N   PRO C 292      -6.205 -15.899-108.076  1.00 91.47           N  
-ATOM   9619  CA  PRO C 292      -5.061 -16.329-108.894  1.00 92.03           C  
-ATOM   9620  C   PRO C 292      -5.418 -16.758-110.322  1.00 96.22           C  
-ATOM   9621  O   PRO C 292      -4.612 -16.549-111.230  1.00 89.12           O  
-ATOM   9622  CB  PRO C 292      -4.492 -17.523-108.107  1.00 94.14           C  
-ATOM   9623  CG  PRO C 292      -5.566 -17.914-107.144  1.00 83.86           C  
-ATOM   9624  CD  PRO C 292      -6.233 -16.629-106.796  1.00 89.98           C  
-ATOM   9625  N   VAL C 293      -6.588 -17.360-110.518  1.00100.94           N  
-ATOM   9626  CA  VAL C 293      -7.024 -17.713-111.866  1.00 92.58           C  
-ATOM   9627  C   VAL C 293      -7.359 -16.441-112.632  1.00 89.92           C  
-ATOM   9628  O   VAL C 293      -7.148 -16.353-113.842  1.00 81.50           O  
-ATOM   9629  CB  VAL C 293      -8.248 -18.646-111.861  1.00 82.92           C  
-ATOM   9630  CG1 VAL C 293      -8.515 -19.170-113.263  1.00 73.74           C  
-ATOM   9631  CG2 VAL C 293      -8.026 -19.797-110.905  1.00 83.49           C  
-ATOM   9632  N   LEU C 294      -7.884 -15.455-111.913  1.00 99.10           N  
-ATOM   9633  CA  LEU C 294      -8.126 -14.141-112.488  1.00103.07           C  
-ATOM   9634  C   LEU C 294      -6.810 -13.484-112.881  1.00107.95           C  
-ATOM   9635  O   LEU C 294      -6.759 -12.708-113.824  1.00105.90           O  
-ATOM   9636  CB  LEU C 294      -8.885 -13.245-111.501  1.00110.05           C  
-ATOM   9637  CG  LEU C 294     -10.342 -13.584-111.172  1.00 94.04           C  
-ATOM   9638  CD1 LEU C 294     -10.869 -12.653-110.091  1.00 86.52           C  
-ATOM   9639  CD2 LEU C 294     -11.212 -13.507-112.418  1.00 91.09           C  
-ATOM   9640  N   ALA C 295      -5.746 -13.820-112.157  1.00106.35           N  
-ATOM   9641  CA  ALA C 295      -4.460 -13.136-112.279  1.00 99.64           C  
-ATOM   9642  C   ALA C 295      -3.792 -13.358-113.634  1.00102.32           C  
-ATOM   9643  O   ALA C 295      -3.126 -12.461-114.154  1.00 99.58           O  
-ATOM   9644  CB  ALA C 295      -3.524 -13.576-111.159  1.00 81.18           C  
-ATOM   9645  N   TRP C 296      -3.968 -14.545-114.207  1.00 97.03           N  
-ATOM   9646  CA  TRP C 296      -3.334 -14.852-115.484  1.00102.37           C  
-ATOM   9647  C   TRP C 296      -4.274 -14.610-116.662  1.00 98.55           C  
-ATOM   9648  O   TRP C 296      -3.857 -14.663-117.820  1.00 92.52           O  
-ATOM   9649  CB  TRP C 296      -2.825 -16.293-115.498  1.00 96.97           C  
-ATOM   9650  CG  TRP C 296      -3.888 -17.349-115.542  1.00103.68           C  
-ATOM   9651  CD1 TRP C 296      -4.503 -17.942-114.476  1.00103.97           C  
-ATOM   9652  CD2 TRP C 296      -4.439 -17.960-116.715  1.00103.42           C  
-ATOM   9653  NE1 TRP C 296      -5.412 -18.878-114.915  1.00 95.24           N  
-ATOM   9654  CE2 TRP C 296      -5.391 -18.907-116.285  1.00 96.84           C  
-ATOM   9655  CE3 TRP C 296      -4.223 -17.794-118.087  1.00 89.76           C  
-ATOM   9656  CZ2 TRP C 296      -6.123 -19.684-117.178  1.00 84.42           C  
-ATOM   9657  CZ3 TRP C 296      -4.953 -18.564-118.971  1.00 84.18           C  
-ATOM   9658  CH2 TRP C 296      -5.893 -19.497-118.513  1.00 85.08           C  
-ATOM   9659  N   MET C 297      -5.540 -14.343-116.363  1.00 97.99           N  
-ATOM   9660  CA  MET C 297      -6.493 -13.957-117.396  1.00 85.60           C  
-ATOM   9661  C   MET C 297      -6.592 -12.436-117.460  1.00 82.09           C  
-ATOM   9662  O   MET C 297      -7.169 -11.875-118.391  1.00 84.49           O  
-ATOM   9663  CB  MET C 297      -7.869 -14.571-117.129  1.00 85.20           C  
-ATOM   9664  CG  MET C 297      -7.914 -16.094-117.201  1.00 84.60           C  
-ATOM   9665  SD  MET C 297      -9.599 -16.725-117.028  1.00 82.58           S  
-ATOM   9666  CE  MET C 297      -9.326 -18.495-117.036  1.00 56.71           C  
-ATOM   9667  N   ASP C 298      -6.012 -11.780-116.460  1.00 90.33           N  
-ATOM   9668  CA  ASP C 298      -6.059 -10.326-116.333  1.00 96.91           C  
-ATOM   9669  C   ASP C 298      -4.886  -9.679-117.057  1.00 97.02           C  
-ATOM   9670  O   ASP C 298      -3.838 -10.301-117.240  1.00 80.01           O  
-ATOM   9671  CB  ASP C 298      -6.059  -9.917-114.851  1.00 90.75           C  
-ATOM   9672  CG  ASP C 298      -6.130  -8.413-114.650  1.00 91.22           C  
-ATOM   9673  OD1 ASP C 298      -6.703  -7.719-115.516  1.00 93.83           O  
-ATOM   9674  OD2 ASP C 298      -5.612  -7.925-113.622  1.00 79.21           O  
-ATOM   9675  N   GLU C 299      -5.074  -8.429-117.470  1.00104.20           N  
-ATOM   9676  CA  GLU C 299      -4.018  -7.654-118.109  1.00107.85           C  
-ATOM   9677  C   GLU C 299      -3.671  -6.412-117.288  1.00 94.35           C  
-ATOM   9678  O   GLU C 299      -3.624  -5.298-117.811  1.00 78.48           O  
-ATOM   9679  CB  GLU C 299      -4.431  -7.253-119.528  1.00 94.68           C  
-ATOM   9680  CG  GLU C 299      -4.690  -8.425-120.466  1.00 83.74           C  
-ATOM   9681  CD  GLU C 299      -3.417  -9.015-121.048  1.00 88.72           C  
-ATOM   9682  OE1 GLU C 299      -3.447  -9.430-122.226  1.00 85.84           O  
-ATOM   9683  OE2 GLU C 299      -2.390  -9.069-120.337  1.00 83.45           O  
-ATOM   9684  N   LEU C 310      -4.324   3.923-121.944  1.00 22.72           N  
-ATOM   9685  CA  LEU C 310      -3.265   4.927-121.985  1.00 45.11           C  
-ATOM   9686  C   LEU C 310      -3.840   6.328-122.187  1.00 31.86           C  
-ATOM   9687  O   LEU C 310      -3.378   7.294-121.578  1.00 28.17           O  
-ATOM   9688  CB  LEU C 310      -2.260   4.602-123.094  1.00 51.92           C  
-ATOM   9689  CG  LEU C 310      -0.767   4.719-122.764  1.00 52.84           C  
-ATOM   9690  CD1 LEU C 310      -0.411   6.113-122.255  1.00 38.77           C  
-ATOM   9691  CD2 LEU C 310      -0.329   3.644-121.770  1.00 34.85           C  
-ATOM   9692  N   ILE C 311      -4.842   6.434-123.054  1.00 32.64           N  
-ATOM   9693  CA  ILE C 311      -5.536   7.698-123.269  1.00 40.05           C  
-ATOM   9694  C   ILE C 311      -6.921   7.650-122.632  1.00 42.12           C  
-ATOM   9695  O   ILE C 311      -7.694   6.722-122.875  1.00 39.97           O  
-ATOM   9696  CB  ILE C 311      -5.675   8.038-124.776  1.00 36.04           C  
-ATOM   9697  CG1 ILE C 311      -4.385   8.657-125.319  1.00 41.07           C  
-ATOM   9698  CG2 ILE C 311      -6.835   8.993-125.008  1.00 29.46           C  
-ATOM   9699  CD1 ILE C 311      -3.300   7.654-125.665  1.00 49.39           C  
-ATOM   9700  N   ARG C 312      -7.226   8.646-121.805  1.00 38.81           N  
-ATOM   9701  CA  ARG C 312      -8.547   8.747-121.198  1.00 38.39           C  
-ATOM   9702  C   ARG C 312      -9.041  10.188-121.177  1.00 45.23           C  
-ATOM   9703  O   ARG C 312      -8.280  11.115-120.900  1.00 50.52           O  
-ATOM   9704  CB  ARG C 312      -8.537   8.176-119.777  1.00 39.69           C  
-ATOM   9705  CG  ARG C 312      -9.909   8.170-119.116  1.00 38.49           C  
-ATOM   9706  CD  ARG C 312      -9.979   7.153-117.994  1.00 35.70           C  
-ATOM   9707  NE  ARG C 312     -11.352   6.734-117.725  1.00 37.08           N  
-ATOM   9708  CZ  ARG C 312     -11.913   6.741-116.521  1.00 48.58           C  
-ATOM   9709  NH1 ARG C 312     -11.218   7.144-115.465  1.00 57.41           N  
-ATOM   9710  NH2 ARG C 312     -13.170   6.344-116.371  1.00 26.49           N  
-ATOM   9711  N   ALA C 313     -10.323  10.366-121.479  1.00 42.94           N  
-ATOM   9712  CA  ALA C 313     -10.950  11.678-121.424  1.00 40.49           C  
-ATOM   9713  C   ALA C 313     -11.221  12.070-119.978  1.00 39.14           C  
-ATOM   9714  O   ALA C 313     -11.834  11.302-119.240  1.00 36.45           O  
-ATOM   9715  CB  ALA C 313     -12.237  11.684-122.226  1.00 32.76           C  
-ATOM   9716  N   VAL C 314     -10.784  13.275-119.606  1.00 31.49           N  
-ATOM   9717  CA  VAL C 314     -10.899  13.833-118.248  1.00 30.59           C  
-ATOM   9718  C   VAL C 314     -10.941  12.785-117.126  1.00 38.17           C  
-ATOM   9719  O   VAL C 314     -11.987  12.553-116.516  1.00 36.33           O  
-ATOM   9720  CB  VAL C 314     -12.144  14.761-118.120  1.00 22.10           C  
-ATOM   9721  CG1 VAL C 314     -11.867  16.110-118.766  1.00 27.36           C  
-ATOM   9722  CG2 VAL C 314     -13.393  14.132-118.727  1.00 27.22           C  
-ATOM   9723  N   PRO C 315      -9.785  12.162-116.843  1.00 34.71           N  
-ATOM   9724  CA  PRO C 315      -9.664  11.039-115.904  1.00 30.68           C  
-ATOM   9725  C   PRO C 315     -10.048  11.397-114.472  1.00 31.35           C  
-ATOM   9726  O   PRO C 315     -10.475  10.519-113.720  1.00 30.05           O  
-ATOM   9727  CB  PRO C 315      -8.178  10.678-115.985  1.00 35.57           C  
-ATOM   9728  CG  PRO C 315      -7.514  11.938-116.406  1.00 35.23           C  
-ATOM   9729  CD  PRO C 315      -8.473  12.588-117.357  1.00 35.35           C  
-ATOM   9730  N   HIS C 316      -9.898  12.667-114.108  1.00 33.42           N  
-ATOM   9731  CA  HIS C 316     -10.194  13.118-112.753  1.00 34.05           C  
-ATOM   9732  C   HIS C 316     -11.687  13.068-112.456  1.00 33.44           C  
-ATOM   9733  O   HIS C 316     -12.093  13.041-111.296  1.00 39.53           O  
-ATOM   9734  CB  HIS C 316      -9.662  14.535-112.533  1.00 31.99           C  
-ATOM   9735  CG  HIS C 316      -9.937  15.466-113.672  1.00 36.54           C  
-ATOM   9736  ND1 HIS C 316      -9.165  15.491-114.813  1.00 34.99           N  
-ATOM   9737  CD2 HIS C 316     -10.896  16.407-113.845  1.00 34.10           C  
-ATOM   9738  CE1 HIS C 316      -9.637  16.406-115.641  1.00 31.40           C  
-ATOM   9739  NE2 HIS C 316     -10.687  16.976-115.078  1.00 33.59           N  
-ATOM   9740  N   VAL C 317     -12.501  13.058-113.506  1.00 33.42           N  
-ATOM   9741  CA  VAL C 317     -13.945  12.951-113.337  1.00 40.78           C  
-ATOM   9742  C   VAL C 317     -14.337  11.503-113.055  1.00 35.48           C  
-ATOM   9743  O   VAL C 317     -14.425  10.682-113.967  1.00 29.86           O  
-ATOM   9744  CB  VAL C 317     -14.701  13.460-114.575  1.00 31.57           C  
-ATOM   9745  CG1 VAL C 317     -16.203  13.380-114.348  1.00 26.96           C  
-ATOM   9746  CG2 VAL C 317     -14.286  14.887-114.900  1.00 28.31           C  
-ATOM   9747  N   HIS C 318     -14.575  11.198-111.783  1.00 35.93           N  
-ATOM   9748  CA  HIS C 318     -14.835   9.824-111.370  1.00 34.26           C  
-ATOM   9749  C   HIS C 318     -16.255   9.378-111.695  1.00 34.97           C  
-ATOM   9750  O   HIS C 318     -16.442   8.306-112.270  1.00 36.25           O  
-ATOM   9751  CB  HIS C 318     -14.538   9.654-109.879  1.00 39.77           C  
-ATOM   9752  CG  HIS C 318     -13.074   9.582-109.570  1.00 59.75           C  
-ATOM   9753  ND1 HIS C 318     -12.487  10.309-108.558  1.00 71.35           N  
-ATOM   9754  CD2 HIS C 318     -12.076   8.868-110.147  1.00 59.38           C  
-ATOM   9755  CE1 HIS C 318     -11.192  10.047-108.523  1.00 69.12           C  
-ATOM   9756  NE2 HIS C 318     -10.917   9.175-109.476  1.00 70.15           N  
-ATOM   9757  N   PHE C 319     -17.261  10.177-111.350  1.00 41.65           N  
-ATOM   9758  CA  PHE C 319     -18.616   9.800-111.757  1.00 31.11           C  
-ATOM   9759  C   PHE C 319     -18.977  10.394-113.110  1.00 30.61           C  
-ATOM   9760  O   PHE C 319     -19.080  11.614-113.271  1.00 35.23           O  
-ATOM   9761  CB  PHE C 319     -19.666  10.211-110.730  1.00 26.56           C  
-ATOM   9762  CG  PHE C 319     -21.065   9.822-111.128  1.00 35.22           C  
-ATOM   9763  CD1 PHE C 319     -21.476   8.499-111.059  1.00 28.28           C  
-ATOM   9764  CD2 PHE C 319     -21.956  10.769-111.604  1.00 38.86           C  
-ATOM   9765  CE1 PHE C 319     -22.754   8.133-111.440  1.00 18.55           C  
-ATOM   9766  CE2 PHE C 319     -23.239  10.410-111.980  1.00 36.24           C  
-ATOM   9767  CZ  PHE C 319     -23.636   9.089-111.899  1.00 31.01           C  
-ATOM   9768  N   ARG C 320     -19.189   9.508-114.076  1.00 22.53           N  
-ATOM   9769  CA  ARG C 320     -19.407   9.906-115.457  1.00 27.84           C  
-ATOM   9770  C   ARG C 320     -20.835   9.624-115.902  1.00 27.00           C  
-ATOM   9771  O   ARG C 320     -21.073   8.811-116.796  1.00 25.90           O  
-ATOM   9772  CB  ARG C 320     -18.415   9.181-116.361  1.00 25.04           C  
-ATOM   9773  CG  ARG C 320     -17.008   9.189-115.801  1.00 25.15           C  
-ATOM   9774  CD  ARG C 320     -16.021   8.549-116.751  1.00 27.24           C  
-ATOM   9775  NE  ARG C 320     -14.753   9.263-116.720  1.00 22.13           N  
-ATOM   9776  CZ  ARG C 320     -14.102   9.671-117.802  1.00 30.72           C  
-ATOM   9777  NH1 ARG C 320     -14.590   9.420-119.009  1.00 31.39           N  
-ATOM   9778  NH2 ARG C 320     -12.957  10.321-117.673  1.00 38.74           N  
-ATOM   9779  N   GLY C 321     -21.784  10.304-115.269  1.00 20.04           N  
-ATOM   9780  CA  GLY C 321     -23.186  10.129-115.588  1.00 18.96           C  
-ATOM   9781  C   GLY C 321     -23.547  10.743-116.925  1.00 24.25           C  
-ATOM   9782  O   GLY C 321     -24.453  10.267-117.608  1.00 24.94           O  
-ATOM   9783  N   HIS C 322     -22.832  11.801-117.300  1.00 19.43           N  
-ATOM   9784  CA  HIS C 322     -23.115  12.516-118.537  1.00 19.32           C  
-ATOM   9785  C   HIS C 322     -22.974  11.586-119.734  1.00 20.10           C  
-ATOM   9786  O   HIS C 322     -21.954  10.921-119.898  1.00 20.24           O  
-ATOM   9787  CB  HIS C 322     -22.192  13.725-118.689  1.00 17.37           C  
-ATOM   9788  CG  HIS C 322     -22.694  14.745-119.662  1.00 16.21           C  
-ATOM   9789  ND1 HIS C 322     -22.862  14.477-121.003  1.00 15.92           N  
-ATOM   9790  CD2 HIS C 322     -23.066  16.035-119.488  1.00 18.62           C  
-ATOM   9791  CE1 HIS C 322     -23.315  15.557-121.613  1.00 15.45           C  
-ATOM   9792  NE2 HIS C 322     -23.447  16.517-120.716  1.00 16.02           N  
-ATOM   9793  N   GLU C 323     -24.004  11.554-120.572  1.00 16.85           N  
-ATOM   9794  CA  GLU C 323     -24.082  10.587-121.659  1.00 16.10           C  
-ATOM   9795  C   GLU C 323     -23.090  10.872-122.791  1.00 22.42           C  
-ATOM   9796  O   GLU C 323     -22.947  10.060-123.705  1.00 28.66           O  
-ATOM   9797  CB  GLU C 323     -25.512  10.535-122.204  1.00 16.33           C  
-ATOM   9798  CG  GLU C 323     -26.541  10.100-121.162  1.00 21.68           C  
-ATOM   9799  CD  GLU C 323     -27.967  10.081-121.689  1.00 23.73           C  
-ATOM   9800  OE1 GLU C 323     -28.243  10.746-122.712  1.00 28.25           O  
-ATOM   9801  OE2 GLU C 323     -28.813   9.398-121.072  1.00 18.37           O  
-ATOM   9802  N   GLU C 324     -22.399  12.010-122.724  1.00 18.08           N  
-ATOM   9803  CA  GLU C 324     -21.381  12.362-123.718  1.00 19.58           C  
-ATOM   9804  C   GLU C 324     -20.096  11.563-123.478  1.00 29.08           C  
-ATOM   9805  O   GLU C 324     -19.245  11.407-124.373  1.00 34.59           O  
-ATOM   9806  CB  GLU C 324     -21.101  13.866-123.682  1.00 15.27           C  
-ATOM   9807  CG  GLU C 324     -20.192  14.370-124.789  1.00 15.98           C  
-ATOM   9808  CD  GLU C 324     -20.441  15.830-125.128  1.00 25.20           C  
-ATOM   9809  OE1 GLU C 324     -19.863  16.326-126.120  1.00 22.80           O  
-ATOM   9810  OE2 GLU C 324     -21.222  16.482-124.404  1.00 29.72           O  
-ATOM   9811  N   PHE C 325     -19.972  11.041-122.262  1.00 21.41           N  
-ATOM   9812  CA  PHE C 325     -18.843  10.197-121.909  1.00 20.27           C  
-ATOM   9813  C   PHE C 325     -18.848   8.922-122.739  1.00 23.65           C  
-ATOM   9814  O   PHE C 325     -17.825   8.266-122.869  1.00 31.01           O  
-ATOM   9815  CB  PHE C 325     -18.858   9.865-120.416  1.00 23.26           C  
-ATOM   9816  CG  PHE C 325     -18.362  10.980-119.544  1.00 27.01           C  
-ATOM   9817  CD1 PHE C 325     -17.030  11.357-119.572  1.00 26.72           C  
-ATOM   9818  CD2 PHE C 325     -19.224  11.648-118.692  1.00 26.45           C  
-ATOM   9819  CE1 PHE C 325     -16.567  12.383-118.767  1.00 27.00           C  
-ATOM   9820  CE2 PHE C 325     -18.768  12.674-117.884  1.00 29.05           C  
-ATOM   9821  CZ  PHE C 325     -17.437  13.042-117.924  1.00 21.32           C  
-ATOM   9822  N   GLN C 326     -20.002   8.576-123.300  1.00 23.52           N  
-ATOM   9823  CA  GLN C 326     -20.074   7.481-124.257  1.00 22.82           C  
-ATOM   9824  C   GLN C 326     -19.203   7.809-125.456  1.00 21.72           C  
-ATOM   9825  O   GLN C 326     -18.373   7.006-125.872  1.00 26.93           O  
-ATOM   9826  CB  GLN C 326     -21.517   7.229-124.700  1.00 19.57           C  
-ATOM   9827  CG  GLN C 326     -22.434   6.767-123.585  1.00 17.39           C  
-ATOM   9828  CD  GLN C 326     -23.845   6.516-124.069  1.00 21.69           C  
-ATOM   9829  OE1 GLN C 326     -24.215   5.385-124.380  1.00 24.89           O  
-ATOM   9830  NE2 GLN C 326     -24.644   7.574-124.137  1.00 24.05           N  
-ATOM   9831  N   TYR C 327     -19.394   9.008-125.991  1.00 20.73           N  
-ATOM   9832  CA  TYR C 327     -18.638   9.477-127.143  1.00 22.14           C  
-ATOM   9833  C   TYR C 327     -17.158   9.650-126.824  1.00 23.92           C  
-ATOM   9834  O   TYR C 327     -16.291   9.180-127.572  1.00 25.44           O  
-ATOM   9835  CB  TYR C 327     -19.221  10.796-127.654  1.00 18.11           C  
-ATOM   9836  CG  TYR C 327     -18.461  11.401-128.811  1.00 25.63           C  
-ATOM   9837  CD1 TYR C 327     -18.512  10.830-130.076  1.00 31.33           C  
-ATOM   9838  CD2 TYR C 327     -17.697  12.547-128.641  1.00 20.32           C  
-ATOM   9839  CE1 TYR C 327     -17.822  11.380-131.138  1.00 25.70           C  
-ATOM   9840  CE2 TYR C 327     -17.004  13.106-129.700  1.00 21.97           C  
-ATOM   9841  CZ  TYR C 327     -17.070  12.518-130.945  1.00 23.30           C  
-ATOM   9842  OH  TYR C 327     -16.383  13.071-132.000  1.00 28.11           O  
-ATOM   9843  N   LEU C 328     -16.867  10.324-125.717  1.00 21.31           N  
-ATOM   9844  CA  LEU C 328     -15.475  10.547-125.339  1.00 26.27           C  
-ATOM   9845  C   LEU C 328     -14.731   9.225-125.127  1.00 25.32           C  
-ATOM   9846  O   LEU C 328     -13.636   9.017-125.673  1.00 26.18           O  
-ATOM   9847  CB  LEU C 328     -15.396  11.411-124.080  1.00 37.78           C  
-ATOM   9848  CG  LEU C 328     -16.045  12.795-124.182  1.00 28.39           C  
-ATOM   9849  CD1 LEU C 328     -15.829  13.591-122.904  1.00 31.43           C  
-ATOM   9850  CD2 LEU C 328     -15.518  13.556-125.389  1.00 25.10           C  
-ATOM   9851  N   ASP C 329     -15.338   8.330-124.349  1.00 22.37           N  
-ATOM   9852  CA  ASP C 329     -14.745   7.019-124.088  1.00 23.95           C  
-ATOM   9853  C   ASP C 329     -14.673   6.181-125.359  1.00 27.18           C  
-ATOM   9854  O   ASP C 329     -13.835   5.293-125.469  1.00 29.41           O  
-ATOM   9855  CB  ASP C 329     -15.525   6.255-123.012  1.00 23.91           C  
-ATOM   9856  CG  ASP C 329     -15.421   6.902-121.643  1.00 33.76           C  
-ATOM   9857  OD1 ASP C 329     -14.519   7.746-121.453  1.00 39.24           O  
-ATOM   9858  OD2 ASP C 329     -16.236   6.561-120.758  1.00 24.26           O  
-ATOM   9859  N   LEU C 330     -15.560   6.455-126.311  1.00 25.01           N  
-ATOM   9860  CA  LEU C 330     -15.510   5.779-127.601  1.00 22.33           C  
-ATOM   9861  C   LEU C 330     -14.251   6.226-128.331  1.00 30.03           C  
-ATOM   9862  O   LEU C 330     -13.518   5.401-128.877  1.00 37.67           O  
-ATOM   9863  CB  LEU C 330     -16.763   6.075-128.436  1.00 23.14           C  
-ATOM   9864  CG  LEU C 330     -17.037   5.288-129.727  1.00 18.32           C  
-ATOM   9865  CD1 LEU C 330     -16.526   6.020-130.963  1.00 20.49           C  
-ATOM   9866  CD2 LEU C 330     -16.445   3.890-129.648  1.00 19.77           C  
-ATOM   9867  N   ILE C 331     -13.996   7.533-128.327  1.00 27.65           N  
-ATOM   9868  CA  ILE C 331     -12.777   8.063-128.937  1.00 23.60           C  
-ATOM   9869  C   ILE C 331     -11.522   7.479-128.297  1.00 25.43           C  
-ATOM   9870  O   ILE C 331     -10.634   6.974-128.991  1.00 27.07           O  
-ATOM   9871  CB  ILE C 331     -12.708   9.596-128.838  1.00 20.26           C  
-ATOM   9872  CG1 ILE C 331     -13.884  10.229-129.582  1.00 22.67           C  
-ATOM   9873  CG2 ILE C 331     -11.390  10.100-129.397  1.00 17.54           C  
-ATOM   9874  CD1 ILE C 331     -13.792  11.729-129.676  1.00 24.53           C  
-ATOM   9875  N   ALA C 332     -11.454   7.552-126.971  1.00 29.59           N  
-ATOM   9876  CA  ALA C 332     -10.306   7.013-126.244  1.00 25.80           C  
-ATOM   9877  C   ALA C 332     -10.118   5.522-126.529  1.00 31.97           C  
-ATOM   9878  O   ALA C 332      -8.989   5.046-126.667  1.00 35.18           O  
-ATOM   9879  CB  ALA C 332     -10.463   7.250-124.754  1.00 27.11           C  
-ATOM   9880  N   ASP C 333     -11.230   4.796-126.631  1.00 34.74           N  
-ATOM   9881  CA  ASP C 333     -11.188   3.357-126.876  1.00 32.69           C  
-ATOM   9882  C   ASP C 333     -10.647   3.062-128.268  1.00 29.65           C  
-ATOM   9883  O   ASP C 333      -9.831   2.162-128.444  1.00 35.23           O  
-ATOM   9884  CB  ASP C 333     -12.577   2.735-126.708  1.00 38.34           C  
-ATOM   9885  CG  ASP C 333     -12.532   1.219-126.578  1.00 50.77           C  
-ATOM   9886  OD1 ASP C 333     -11.483   0.603-126.873  1.00 48.74           O  
-ATOM   9887  OD2 ASP C 333     -13.561   0.637-126.179  1.00 50.36           O  
-ATOM   9888  N   ILE C 334     -11.111   3.815-129.258  1.00 29.01           N  
-ATOM   9889  CA  ILE C 334     -10.635   3.632-130.622  1.00 25.08           C  
-ATOM   9890  C   ILE C 334      -9.146   3.948-130.714  1.00 30.01           C  
-ATOM   9891  O   ILE C 334      -8.385   3.210-131.333  1.00 33.41           O  
-ATOM   9892  CB  ILE C 334     -11.412   4.509-131.616  1.00 25.67           C  
-ATOM   9893  CG1 ILE C 334     -12.860   4.036-131.709  1.00 22.48           C  
-ATOM   9894  CG2 ILE C 334     -10.764   4.472-132.987  1.00 23.46           C  
-ATOM   9895  CD1 ILE C 334     -13.650   4.749-132.756  1.00 22.90           C  
-ATOM   9896  N   ILE C 335      -8.724   5.038-130.083  1.00 36.61           N  
-ATOM   9897  CA  ILE C 335      -7.311   5.402-130.124  1.00 35.57           C  
-ATOM   9898  C   ILE C 335      -6.440   4.342-129.434  1.00 31.08           C  
-ATOM   9899  O   ILE C 335      -5.403   3.948-129.964  1.00 34.85           O  
-ATOM   9900  CB  ILE C 335      -7.063   6.783-129.483  1.00 28.92           C  
-ATOM   9901  CG1 ILE C 335      -7.768   7.878-130.289  1.00 26.30           C  
-ATOM   9902  CG2 ILE C 335      -5.577   7.074-129.410  1.00 30.67           C  
-ATOM   9903  CD1 ILE C 335      -7.560   9.275-129.730  1.00 38.55           C  
-ATOM   9904  N   ASN C 336      -6.869   3.868-128.267  1.00 27.84           N  
-ATOM   9905  CA  ASN C 336      -6.076   2.906-127.504  1.00 32.49           C  
-ATOM   9906  C   ASN C 336      -6.033   1.502-128.106  1.00 33.84           C  
-ATOM   9907  O   ASN C 336      -4.960   0.920-128.262  1.00 47.88           O  
-ATOM   9908  CB  ASN C 336      -6.598   2.805-126.070  1.00 29.47           C  
-ATOM   9909  CG  ASN C 336      -6.365   4.071-125.272  1.00 36.16           C  
-ATOM   9910  OD1 ASN C 336      -5.531   4.903-125.630  1.00 41.07           O  
-ATOM   9911  ND2 ASN C 336      -7.097   4.217-124.174  1.00 21.99           N  
-ATOM   9912  N   ASN C 337      -7.202   0.962-128.435  1.00 31.76           N  
-ATOM   9913  CA  ASN C 337      -7.322  -0.446-128.803  1.00 36.96           C  
-ATOM   9914  C   ASN C 337      -7.586  -0.689-130.284  1.00 41.38           C  
-ATOM   9915  O   ASN C 337      -7.537  -1.830-130.748  1.00 49.84           O  
-ATOM   9916  CB  ASN C 337      -8.435  -1.102-127.984  1.00 34.25           C  
-ATOM   9917  CG  ASN C 337      -8.226  -0.952-126.491  1.00 37.48           C  
-ATOM   9918  OD1 ASN C 337      -7.095  -0.954-126.010  1.00 40.43           O  
-ATOM   9919  ND2 ASN C 337      -9.320  -0.815-125.750  1.00 36.20           N  
-ATOM   9920  N   GLY C 338      -7.872   0.376-131.023  1.00 38.50           N  
-ATOM   9921  CA  GLY C 338      -8.192   0.244-132.432  1.00 40.83           C  
-ATOM   9922  C   GLY C 338      -7.004  -0.209-133.257  1.00 39.85           C  
-ATOM   9923  O   GLY C 338      -5.865  -0.174-132.790  1.00 42.74           O  
-ATOM   9924  N   ARG C 339      -7.272  -0.641-134.485  1.00 35.16           N  
-ATOM   9925  CA  ARG C 339      -6.208  -1.081-135.380  1.00 33.58           C  
-ATOM   9926  C   ARG C 339      -5.947  -0.040-136.456  1.00 36.53           C  
-ATOM   9927  O   ARG C 339      -6.884   0.577-136.964  1.00 38.59           O  
-ATOM   9928  CB  ARG C 339      -6.565  -2.420-136.022  1.00 35.18           C  
-ATOM   9929  CG  ARG C 339      -6.851  -3.528-135.030  1.00 41.14           C  
-ATOM   9930  CD  ARG C 339      -5.673  -3.760-134.101  1.00 37.34           C  
-ATOM   9931  NE  ARG C 339      -5.735  -5.089-133.502  1.00 57.73           N  
-ATOM   9932  CZ  ARG C 339      -5.216  -6.178-134.059  1.00 67.69           C  
-ATOM   9933  NH1 ARG C 339      -4.588  -6.090-135.225  1.00 52.91           N  
-ATOM   9934  NH2 ARG C 339      -5.321  -7.355-133.452  1.00 51.69           N  
-ATOM   9935  N   THR C 340      -4.679   0.159-136.801  1.00 33.65           N  
-ATOM   9936  CA  THR C 340      -4.340   1.100-137.861  1.00 33.45           C  
-ATOM   9937  C   THR C 340      -4.462   0.442-139.228  1.00 37.87           C  
-ATOM   9938  O   THR C 340      -3.754  -0.514-139.537  1.00 46.92           O  
-ATOM   9939  CB  THR C 340      -2.927   1.659-137.714  1.00 37.09           C  
-ATOM   9940  OG1 THR C 340      -2.774   2.245-136.415  1.00 39.91           O  
-ATOM   9941  CG2 THR C 340      -2.687   2.714-138.778  1.00 39.05           C  
-ATOM   9942  N   MET C 341      -5.362   0.974-140.045  1.00 36.52           N  
-ATOM   9943  CA  MET C 341      -5.674   0.397-141.340  1.00 37.82           C  
-ATOM   9944  C   MET C 341      -5.577   1.434-142.448  1.00 36.80           C  
-ATOM   9945  O   MET C 341      -5.658   2.645-142.196  1.00 42.24           O  
-ATOM   9946  CB  MET C 341      -7.081  -0.208-141.326  1.00 44.54           C  
-ATOM   9947  CG  MET C 341      -7.338  -1.195-140.200  1.00 41.53           C  
-ATOM   9948  SD  MET C 341      -6.575  -2.799-140.499  1.00 61.37           S  
-ATOM   9949  CE  MET C 341      -7.429  -3.295-141.994  1.00 46.60           C  
-ATOM   9950  N   ASP C 342      -5.407   0.942-143.673  1.00 45.17           N  
-ATOM   9951  CA  ASP C 342      -5.501   1.770-144.869  1.00 52.92           C  
-ATOM   9952  C   ASP C 342      -6.960   2.109-145.156  1.00 50.53           C  
-ATOM   9953  O   ASP C 342      -7.866   1.610-144.488  1.00 56.94           O  
-ATOM   9954  CB  ASP C 342      -4.869   1.066-146.069  1.00 54.18           C  
-ATOM   9955  CG  ASP C 342      -3.376   1.311-146.166  1.00 74.86           C  
-ATOM   9956  OD1 ASP C 342      -2.789   1.827-145.189  1.00 71.17           O  
-ATOM   9957  OD2 ASP C 342      -2.788   0.985-147.219  1.00 79.34           O  
-ATOM   9958  N   ASP C 343      -7.191   2.942-146.162  1.00 47.37           N  
-ATOM   9959  CA  ASP C 343      -8.508   3.533-146.339  1.00 40.72           C  
-ATOM   9960  C   ASP C 343      -8.752   3.986-147.780  1.00 47.35           C  
-ATOM   9961  O   ASP C 343      -7.808   4.251-148.524  1.00 52.40           O  
-ATOM   9962  CB  ASP C 343      -8.658   4.697-145.353  1.00 40.21           C  
-ATOM   9963  CG  ASP C 343      -9.850   5.571-145.648  1.00 49.09           C  
-ATOM   9964  OD1 ASP C 343     -10.992   5.133-145.400  1.00 55.98           O  
-ATOM   9965  OD2 ASP C 343      -9.642   6.704-146.123  1.00 43.93           O  
-ATOM   9966  N   ARG C 344     -10.025   4.049-148.165  1.00 38.91           N  
-ATOM   9967  CA  ARG C 344     -10.437   4.464-149.505  1.00 40.40           C  
-ATOM   9968  C   ARG C 344      -9.822   5.793-149.948  1.00 44.55           C  
-ATOM   9969  O   ARG C 344      -9.465   5.963-151.114  1.00 45.61           O  
-ATOM   9970  CB  ARG C 344     -11.966   4.562-149.569  1.00 42.95           C  
-ATOM   9971  CG  ARG C 344     -12.509   5.128-150.873  1.00 44.88           C  
-ATOM   9972  CD  ARG C 344     -14.016   5.330-150.808  1.00 47.73           C  
-ATOM   9973  NE  ARG C 344     -14.400   6.361-149.847  1.00 40.34           N  
-ATOM   9974  CZ  ARG C 344     -14.600   7.638-150.159  1.00 61.18           C  
-ATOM   9975  NH1 ARG C 344     -14.450   8.050-151.412  1.00 63.53           N  
-ATOM   9976  NH2 ARG C 344     -14.949   8.506-149.219  1.00 63.25           N  
-ATOM   9977  N   THR C 345      -9.696   6.726-149.010  1.00 44.81           N  
-ATOM   9978  CA  THR C 345      -9.246   8.081-149.319  1.00 48.64           C  
-ATOM   9979  C   THR C 345      -7.731   8.185-149.478  1.00 47.75           C  
-ATOM   9980  O   THR C 345      -7.234   9.016-150.239  1.00 52.45           O  
-ATOM   9981  CB  THR C 345      -9.680   9.071-148.226  1.00 60.37           C  
-ATOM   9982  OG1 THR C 345      -8.894   8.857-147.046  1.00 59.56           O  
-ATOM   9983  CG2 THR C 345     -11.152   8.880-147.889  1.00 63.52           C  
-ATOM   9984  N   GLY C 346      -7.001   7.347-148.752  1.00 41.02           N  
-ATOM   9985  CA  GLY C 346      -5.551   7.401-148.766  1.00 39.57           C  
-ATOM   9986  C   GLY C 346      -5.014   7.849-147.423  1.00 53.57           C  
-ATOM   9987  O   GLY C 346      -3.864   7.576-147.077  1.00 55.28           O  
-ATOM   9988  N   VAL C 347      -5.852   8.551-146.667  1.00 48.97           N  
-ATOM   9989  CA  VAL C 347      -5.507   8.940-145.309  1.00 42.24           C  
-ATOM   9990  C   VAL C 347      -5.619   7.711-144.416  1.00 45.89           C  
-ATOM   9991  O   VAL C 347      -6.479   6.860-144.635  1.00 39.28           O  
-ATOM   9992  CB  VAL C 347      -6.422  10.062-144.782  1.00 49.71           C  
-ATOM   9993  CG1 VAL C 347      -5.790  10.743-143.579  1.00 47.17           C  
-ATOM   9994  CG2 VAL C 347      -6.700  11.077-145.881  1.00 52.94           C  
-ATOM   9995  N   GLY C 348      -4.742   7.609-143.424  1.00 49.49           N  
-ATOM   9996  CA  GLY C 348      -4.741   6.465-142.530  1.00 49.48           C  
-ATOM   9997  C   GLY C 348      -5.951   6.464-141.617  1.00 35.49           C  
-ATOM   9998  O   GLY C 348      -6.586   7.501-141.426  1.00 40.03           O  
-ATOM   9999  N   VAL C 349      -6.277   5.306-141.053  1.00 35.20           N  
-ATOM  10000  CA  VAL C 349      -7.422   5.219-140.153  1.00 32.67           C  
-ATOM  10001  C   VAL C 349      -7.089   4.362-138.935  1.00 32.45           C  
-ATOM  10002  O   VAL C 349      -6.243   3.480-139.006  1.00 35.58           O  
-ATOM  10003  CB  VAL C 349      -8.670   4.655-140.891  1.00 33.34           C  
-ATOM  10004  CG1 VAL C 349      -9.132   3.327-140.294  1.00 29.25           C  
-ATOM  10005  CG2 VAL C 349      -9.797   5.678-140.893  1.00 30.35           C  
-ATOM  10006  N   ILE C 350      -7.723   4.656-137.805  1.00 29.31           N  
-ATOM  10007  CA  ILE C 350      -7.673   3.765-136.651  1.00 31.35           C  
-ATOM  10008  C   ILE C 350      -9.096   3.318-136.349  1.00 30.25           C  
-ATOM  10009  O   ILE C 350      -9.943   4.141-136.010  1.00 30.65           O  
-ATOM  10010  CB  ILE C 350      -7.065   4.439-135.412  1.00 26.66           C  
-ATOM  10011  CG1 ILE C 350      -5.774   5.173-135.776  1.00 35.12           C  
-ATOM  10012  CG2 ILE C 350      -6.817   3.410-134.323  1.00 22.20           C  
-ATOM  10013  CD1 ILE C 350      -5.161   5.932-134.618  1.00 33.84           C  
-ATOM  10014  N   SER C 351      -9.367   2.023-136.479  1.00 26.09           N  
-ATOM  10015  CA  SER C 351     -10.751   1.561-136.437  1.00 26.51           C  
-ATOM  10016  C   SER C 351     -11.029   0.425-135.457  1.00 24.84           C  
-ATOM  10017  O   SER C 351     -10.135  -0.336-135.077  1.00 28.27           O  
-ATOM  10018  CB  SER C 351     -11.195   1.130-137.840  1.00 27.12           C  
-ATOM  10019  OG  SER C 351     -10.401   0.067-138.331  1.00 38.71           O  
-ATOM  10020  N   LYS C 352     -12.292   0.346-135.050  1.00 22.66           N  
-ATOM  10021  CA  LYS C 352     -12.831  -0.785-134.309  1.00 24.42           C  
-ATOM  10022  C   LYS C 352     -14.097  -1.256-135.016  1.00 28.17           C  
-ATOM  10023  O   LYS C 352     -14.592  -0.583-135.921  1.00 26.51           O  
-ATOM  10024  CB  LYS C 352     -13.136  -0.411-132.858  1.00 24.24           C  
-ATOM  10025  CG  LYS C 352     -11.920  -0.003-132.049  1.00 31.33           C  
-ATOM  10026  CD  LYS C 352     -12.181  -0.169-130.558  1.00 34.67           C  
-ATOM  10027  CE  LYS C 352     -12.540  -1.611-130.228  1.00 45.19           C  
-ATOM  10028  NZ  LYS C 352     -12.734  -1.831-128.768  1.00 49.29           N  
-ATOM  10029  N   PHE C 353     -14.628  -2.401-134.603  1.00 25.70           N  
-ATOM  10030  CA  PHE C 353     -15.808  -2.958-135.256  1.00 23.38           C  
-ATOM  10031  C   PHE C 353     -16.899  -3.313-134.250  1.00 25.13           C  
-ATOM  10032  O   PHE C 353     -16.653  -4.022-133.274  1.00 30.66           O  
-ATOM  10033  CB  PHE C 353     -15.421  -4.188-136.075  1.00 29.80           C  
-ATOM  10034  CG  PHE C 353     -16.467  -4.618-137.064  1.00 27.63           C  
-ATOM  10035  CD1 PHE C 353     -16.981  -3.721-137.986  1.00 26.83           C  
-ATOM  10036  CD2 PHE C 353     -16.915  -5.928-137.088  1.00 23.15           C  
-ATOM  10037  CE1 PHE C 353     -17.936  -4.119-138.904  1.00 26.17           C  
-ATOM  10038  CE2 PHE C 353     -17.865  -6.334-138.005  1.00 28.92           C  
-ATOM  10039  CZ  PHE C 353     -18.378  -5.428-138.915  1.00 28.13           C  
-ATOM  10040  N   GLY C 354     -18.106  -2.816-134.496  1.00 23.23           N  
-ATOM  10041  CA  GLY C 354     -19.221  -3.050-133.596  1.00 21.21           C  
-ATOM  10042  C   GLY C 354     -19.149  -2.181-132.359  1.00 20.39           C  
-ATOM  10043  O   GLY C 354     -18.557  -2.566-131.352  1.00 27.45           O  
-ATOM  10044  N   CYS C 355     -19.752  -0.999-132.435  1.00 18.82           N  
-ATOM  10045  CA  CYS C 355     -19.744  -0.064-131.314  1.00 26.56           C  
-ATOM  10046  C   CYS C 355     -21.152   0.452-131.014  1.00 32.96           C  
-ATOM  10047  O   CYS C 355     -21.959   0.652-131.919  1.00 23.56           O  
-ATOM  10048  CB  CYS C 355     -18.796   1.103-131.597  1.00 26.75           C  
-ATOM  10049  SG  CYS C 355     -17.047   0.631-131.677  1.00 44.25           S  
-ATOM  10050  N   THR C 356     -21.442   0.669-129.736  1.00 28.46           N  
-ATOM  10051  CA  THR C 356     -22.802   0.975-129.317  1.00 15.36           C  
-ATOM  10052  C   THR C 356     -22.879   2.210-128.433  1.00 18.14           C  
-ATOM  10053  O   THR C 356     -22.094   2.366-127.499  1.00 22.22           O  
-ATOM  10054  CB  THR C 356     -23.420  -0.226-128.569  1.00 20.77           C  
-ATOM  10055  OG1 THR C 356     -23.825  -1.219-129.518  1.00 27.53           O  
-ATOM  10056  CG2 THR C 356     -24.631   0.196-127.744  1.00 28.18           C  
-ATOM  10057  N   MET C 357     -23.826   3.090-128.745  1.00 19.48           N  
-ATOM  10058  CA  MET C 357     -24.165   4.198-127.858  1.00 19.15           C  
-ATOM  10059  C   MET C 357     -25.679   4.314-127.738  1.00 18.33           C  
-ATOM  10060  O   MET C 357     -26.405   3.691-128.502  1.00 20.37           O  
-ATOM  10061  CB  MET C 357     -23.569   5.511-128.369  1.00 18.02           C  
-ATOM  10062  CG  MET C 357     -22.059   5.590-128.262  1.00 18.88           C  
-ATOM  10063  SD  MET C 357     -21.398   7.186-128.781  1.00 20.52           S  
-ATOM  10064  CE  MET C 357     -22.040   7.293-130.449  1.00 18.97           C  
-ATOM  10065  N   ARG C 358     -26.151   5.092-126.769  1.00 18.19           N  
-ATOM  10066  CA  ARG C 358     -27.569   5.438-126.696  1.00 18.55           C  
-ATOM  10067  C   ARG C 358     -27.794   6.668-125.819  1.00 20.28           C  
-ATOM  10068  O   ARG C 358     -27.234   6.786-124.727  1.00 18.11           O  
-ATOM  10069  CB  ARG C 358     -28.409   4.258-126.188  1.00 16.42           C  
-ATOM  10070  CG  ARG C 358     -28.008   3.711-124.835  1.00 25.10           C  
-ATOM  10071  CD  ARG C 358     -29.065   2.752-124.306  1.00 20.08           C  
-ATOM  10072  NE  ARG C 358     -29.161   1.532-125.101  1.00 21.67           N  
-ATOM  10073  CZ  ARG C 358     -30.306   0.936-125.424  1.00 27.75           C  
-ATOM  10074  NH1 ARG C 358     -31.461   1.451-125.028  1.00 21.41           N  
-ATOM  10075  NH2 ARG C 358     -30.297  -0.175-126.147  1.00 30.32           N  
-ATOM  10076  N   TYR C 359     -28.619   7.582-126.320  1.00 18.81           N  
-ATOM  10077  CA  TYR C 359     -28.862   8.862-125.670  1.00 19.23           C  
-ATOM  10078  C   TYR C 359     -30.338   9.052-125.333  1.00 20.77           C  
-ATOM  10079  O   TYR C 359     -31.220   8.679-126.111  1.00 19.92           O  
-ATOM  10080  CB  TYR C 359     -28.373  10.006-126.563  1.00 23.65           C  
-ATOM  10081  CG  TYR C 359     -26.891   9.953-126.850  1.00 19.06           C  
-ATOM  10082  CD1 TYR C 359     -25.981  10.564-126.001  1.00 19.69           C  
-ATOM  10083  CD2 TYR C 359     -26.401   9.283-127.964  1.00 19.48           C  
-ATOM  10084  CE1 TYR C 359     -24.624  10.513-126.254  1.00 20.95           C  
-ATOM  10085  CE2 TYR C 359     -25.044   9.226-128.224  1.00 18.11           C  
-ATOM  10086  CZ  TYR C 359     -24.161   9.844-127.365  1.00 21.58           C  
-ATOM  10087  OH  TYR C 359     -22.808   9.798-127.613  1.00 27.46           O  
-ATOM  10088  N   SER C 360     -30.595   9.637-124.168  1.00 15.08           N  
-ATOM  10089  CA  SER C 360     -31.955   9.862-123.704  1.00 18.04           C  
-ATOM  10090  C   SER C 360     -32.546  11.114-124.336  1.00 21.94           C  
-ATOM  10091  O   SER C 360     -31.846  12.105-124.535  1.00 22.33           O  
-ATOM  10092  CB  SER C 360     -31.981   9.975-122.183  1.00 20.11           C  
-ATOM  10093  OG  SER C 360     -31.317   8.872-121.592  1.00 22.43           O  
-ATOM  10094  N   LEU C 361     -33.838  11.069-124.644  1.00 22.24           N  
-ATOM  10095  CA  LEU C 361     -34.484  12.177-125.336  1.00 23.96           C  
-ATOM  10096  C   LEU C 361     -35.637  12.782-124.543  1.00 28.99           C  
-ATOM  10097  O   LEU C 361     -36.273  13.731-125.001  1.00 33.42           O  
-ATOM  10098  CB  LEU C 361     -35.000  11.722-126.703  1.00 27.25           C  
-ATOM  10099  CG  LEU C 361     -34.017  11.017-127.640  1.00 22.36           C  
-ATOM  10100  CD1 LEU C 361     -34.665  10.765-128.988  1.00 16.73           C  
-ATOM  10101  CD2 LEU C 361     -32.743  11.822-127.803  1.00 19.31           C  
-ATOM  10102  N   ASP C 362     -35.910  12.237-123.362  1.00 28.07           N  
-ATOM  10103  CA  ASP C 362     -37.053  12.690-122.576  1.00 28.17           C  
-ATOM  10104  C   ASP C 362     -36.733  13.933-121.745  1.00 29.30           C  
-ATOM  10105  O   ASP C 362     -37.612  14.754-121.486  1.00 26.94           O  
-ATOM  10106  CB  ASP C 362     -37.550  11.567-121.666  1.00 28.07           C  
-ATOM  10107  CG  ASP C 362     -36.481  11.070-120.715  1.00 34.35           C  
-ATOM  10108  OD1 ASP C 362     -35.628  10.268-121.149  1.00 38.52           O  
-ATOM  10109  OD2 ASP C 362     -36.496  11.480-119.534  1.00 28.47           O  
-ATOM  10110  N   GLN C 363     -35.480  14.071-121.328  1.00 32.23           N  
-ATOM  10111  CA  GLN C 363     -35.076  15.230-120.538  1.00 28.07           C  
-ATOM  10112  C   GLN C 363     -34.501  16.328-121.426  1.00 23.25           C  
-ATOM  10113  O   GLN C 363     -35.018  17.444-121.464  1.00 17.37           O  
-ATOM  10114  CB  GLN C 363     -34.058  14.826-119.471  1.00 35.50           C  
-ATOM  10115  CG  GLN C 363     -34.600  13.857-118.430  1.00 42.58           C  
-ATOM  10116  CD  GLN C 363     -35.759  14.435-117.645  1.00 34.41           C  
-ATOM  10117  OE1 GLN C 363     -35.571  15.283-116.771  1.00 36.01           O  
-ATOM  10118  NE2 GLN C 363     -36.969  13.979-117.955  1.00 36.31           N  
-ATOM  10119  N   ALA C 364     -33.432  16.005-122.145  1.00 22.03           N  
-ATOM  10120  CA  ALA C 364     -32.801  16.970-123.034  1.00 18.77           C  
-ATOM  10121  C   ALA C 364     -32.438  16.337-124.375  1.00 20.82           C  
-ATOM  10122  O   ALA C 364     -32.885  15.236-124.696  1.00 24.21           O  
-ATOM  10123  CB  ALA C 364     -31.574  17.563-122.374  1.00 14.31           C  
-ATOM  10124  N   PHE C 365     -31.627  17.042-125.155  1.00 15.53           N  
-ATOM  10125  CA  PHE C 365     -31.288  16.606-126.503  1.00 15.36           C  
-ATOM  10126  C   PHE C 365     -29.779  16.452-126.636  1.00 21.94           C  
-ATOM  10127  O   PHE C 365     -29.028  17.360-126.274  1.00 23.86           O  
-ATOM  10128  CB  PHE C 365     -31.824  17.605-127.532  1.00 16.21           C  
-ATOM  10129  CG  PHE C 365     -31.638  17.175-128.958  1.00 14.81           C  
-ATOM  10130  CD1 PHE C 365     -30.479  17.490-129.647  1.00 17.87           C  
-ATOM  10131  CD2 PHE C 365     -32.633  16.477-129.616  1.00 15.56           C  
-ATOM  10132  CE1 PHE C 365     -30.310  17.101-130.962  1.00 16.60           C  
-ATOM  10133  CE2 PHE C 365     -32.471  16.088-130.930  1.00 18.52           C  
-ATOM  10134  CZ  PHE C 365     -31.307  16.399-131.604  1.00 13.41           C  
-ATOM  10135  N   PRO C 366     -29.330  15.301-127.163  1.00 21.37           N  
-ATOM  10136  CA  PRO C 366     -27.900  14.990-127.243  1.00 15.40           C  
-ATOM  10137  C   PRO C 366     -27.176  15.752-128.351  1.00 23.21           C  
-ATOM  10138  O   PRO C 366     -26.613  15.138-129.259  1.00 25.89           O  
-ATOM  10139  CB  PRO C 366     -27.891  13.488-127.521  1.00 11.13           C  
-ATOM  10140  CG  PRO C 366     -29.144  13.255-128.278  1.00 15.05           C  
-ATOM  10141  CD  PRO C 366     -30.160  14.225-127.732  1.00 13.85           C  
-ATOM  10142  N   LEU C 367     -27.200  17.079-128.281  1.00 22.16           N  
-ATOM  10143  CA  LEU C 367     -26.337  17.890-129.125  1.00 22.61           C  
-ATOM  10144  C   LEU C 367     -25.020  18.057-128.376  1.00 22.56           C  
-ATOM  10145  O   LEU C 367     -24.944  18.811-127.406  1.00 24.94           O  
-ATOM  10146  CB  LEU C 367     -26.974  19.244-129.444  1.00 16.90           C  
-ATOM  10147  CG  LEU C 367     -26.355  20.042-130.596  1.00 13.15           C  
-ATOM  10148  CD1 LEU C 367     -26.555  19.324-131.920  1.00 19.28           C  
-ATOM  10149  CD2 LEU C 367     -26.926  21.449-130.662  1.00 11.50           C  
-ATOM  10150  N   LEU C 368     -23.996  17.335-128.822  1.00 15.03           N  
-ATOM  10151  CA  LEU C 368     -22.733  17.230-128.096  1.00 18.33           C  
-ATOM  10152  C   LEU C 368     -22.148  18.592-127.748  1.00 20.75           C  
-ATOM  10153  O   LEU C 368     -22.270  19.545-128.515  1.00 19.13           O  
-ATOM  10154  CB  LEU C 368     -21.723  16.411-128.901  1.00 21.94           C  
-ATOM  10155  CG  LEU C 368     -22.003  14.905-128.988  1.00 23.92           C  
-ATOM  10156  CD1 LEU C 368     -22.422  14.349-127.634  1.00 19.54           C  
-ATOM  10157  CD2 LEU C 368     -23.054  14.585-130.041  1.00 36.50           C  
-ATOM  10158  N   THR C 369     -21.520  18.672-126.579  1.00 19.64           N  
-ATOM  10159  CA  THR C 369     -21.103  19.953-126.021  1.00 22.56           C  
-ATOM  10160  C   THR C 369     -19.592  20.106-125.905  1.00 23.61           C  
-ATOM  10161  O   THR C 369     -19.091  21.212-125.698  1.00 24.85           O  
-ATOM  10162  CB  THR C 369     -21.711  20.168-124.626  1.00 20.11           C  
-ATOM  10163  OG1 THR C 369     -21.170  19.202-123.717  1.00 19.19           O  
-ATOM  10164  CG2 THR C 369     -23.224  20.026-124.677  1.00 19.73           C  
-ATOM  10165  N   THR C 370     -18.863  19.004-126.035  1.00 20.09           N  
-ATOM  10166  CA  THR C 370     -17.415  19.046-125.881  1.00 19.58           C  
-ATOM  10167  C   THR C 370     -16.771  19.659-127.129  1.00 22.69           C  
-ATOM  10168  O   THR C 370     -15.567  19.910-127.165  1.00 21.47           O  
-ATOM  10169  CB  THR C 370     -16.842  17.643-125.599  1.00 20.12           C  
-ATOM  10170  OG1 THR C 370     -15.526  17.759-125.046  1.00 36.50           O  
-ATOM  10171  CG2 THR C 370     -16.794  16.819-126.861  1.00 24.94           C  
-ATOM  10172  N   LYS C 371     -17.597  19.892-128.146  1.00 25.78           N  
-ATOM  10173  CA  LYS C 371     -17.236  20.688-129.317  1.00 27.72           C  
-ATOM  10174  C   LYS C 371     -18.534  21.172-129.968  1.00 31.14           C  
-ATOM  10175  O   LYS C 371     -19.576  20.534-129.815  1.00 34.24           O  
-ATOM  10176  CB  LYS C 371     -16.395  19.881-130.307  1.00 23.11           C  
-ATOM  10177  CG  LYS C 371     -17.140  19.521-131.577  1.00 34.87           C  
-ATOM  10178  CD  LYS C 371     -16.258  18.823-132.587  1.00 51.27           C  
-ATOM  10179  CE  LYS C 371     -17.053  18.531-133.846  1.00 63.26           C  
-ATOM  10180  NZ  LYS C 371     -16.477  17.422-134.647  1.00 61.04           N  
-ATOM  10181  N   ARG C 372     -18.487  22.293-130.682  1.00 31.49           N  
-ATOM  10182  CA  ARG C 372     -19.703  22.844-131.279  1.00 27.23           C  
-ATOM  10183  C   ARG C 372     -20.161  22.068-132.516  1.00 28.18           C  
-ATOM  10184  O   ARG C 372     -19.391  21.863-133.455  1.00 29.75           O  
-ATOM  10185  CB  ARG C 372     -19.504  24.316-131.640  1.00 33.93           C  
-ATOM  10186  CG  ARG C 372     -20.720  24.942-132.300  1.00 28.56           C  
-ATOM  10187  CD  ARG C 372     -20.547  26.437-132.490  1.00 40.07           C  
-ATOM  10188  NE  ARG C 372     -20.434  27.142-131.217  1.00 35.03           N  
-ATOM  10189  CZ  ARG C 372     -21.473  27.547-130.495  1.00 27.19           C  
-ATOM  10190  NH1 ARG C 372     -22.708  27.308-130.918  1.00 16.47           N  
-ATOM  10191  NH2 ARG C 372     -21.276  28.184-129.348  1.00 21.49           N  
-ATOM  10192  N   VAL C 373     -21.426  21.655-132.512  1.00 24.10           N  
-ATOM  10193  CA  VAL C 373     -21.998  20.872-133.606  1.00 19.68           C  
-ATOM  10194  C   VAL C 373     -22.847  21.740-134.542  1.00 25.16           C  
-ATOM  10195  O   VAL C 373     -23.576  22.626-134.095  1.00 25.96           O  
-ATOM  10196  CB  VAL C 373     -22.851  19.702-133.057  1.00 15.03           C  
-ATOM  10197  CG1 VAL C 373     -23.587  18.979-134.178  1.00  9.42           C  
-ATOM  10198  CG2 VAL C 373     -21.972  18.733-132.285  1.00 19.07           C  
-ATOM  10199  N   PHE C 374     -22.735  21.475-135.843  1.00 24.50           N  
-ATOM  10200  CA  PHE C 374     -23.412  22.249-136.883  1.00 23.62           C  
-ATOM  10201  C   PHE C 374     -24.923  21.973-136.946  1.00 27.84           C  
-ATOM  10202  O   PHE C 374     -25.416  21.304-137.865  1.00 33.25           O  
-ATOM  10203  CB  PHE C 374     -22.768  21.945-138.238  1.00 26.30           C  
-ATOM  10204  CG  PHE C 374     -23.088  22.950-139.303  1.00 28.97           C  
-ATOM  10205  CD1 PHE C 374     -23.366  24.262-138.965  1.00 29.30           C  
-ATOM  10206  CD2 PHE C 374     -23.119  22.583-140.640  1.00 23.19           C  
-ATOM  10207  CE1 PHE C 374     -23.666  25.194-139.941  1.00 33.10           C  
-ATOM  10208  CE2 PHE C 374     -23.418  23.507-141.616  1.00 22.80           C  
-ATOM  10209  CZ  PHE C 374     -23.692  24.813-141.268  1.00 30.78           C  
-ATOM  10210  N   TRP C 375     -25.659  22.518-135.983  1.00 18.98           N  
-ATOM  10211  CA  TRP C 375     -27.079  22.211-135.840  1.00 22.77           C  
-ATOM  10212  C   TRP C 375     -27.910  22.664-137.033  1.00 24.90           C  
-ATOM  10213  O   TRP C 375     -28.838  21.968-137.450  1.00 30.32           O  
-ATOM  10214  CB  TRP C 375     -27.644  22.839-134.568  1.00 23.26           C  
-ATOM  10215  CG  TRP C 375     -29.089  22.501-134.380  1.00 28.32           C  
-ATOM  10216  CD1 TRP C 375     -29.604  21.310-133.948  1.00 24.85           C  
-ATOM  10217  CD2 TRP C 375     -30.209  23.352-134.638  1.00 22.34           C  
-ATOM  10218  NE1 TRP C 375     -30.977  21.372-133.914  1.00 21.61           N  
-ATOM  10219  CE2 TRP C 375     -31.372  22.614-134.335  1.00 30.00           C  
-ATOM  10220  CE3 TRP C 375     -30.342  24.669-135.092  1.00 34.42           C  
-ATOM  10221  CZ2 TRP C 375     -32.650  23.152-134.466  1.00 42.48           C  
-ATOM  10222  CZ3 TRP C 375     -31.615  25.201-135.225  1.00 43.46           C  
-ATOM  10223  CH2 TRP C 375     -32.750  24.444-134.913  1.00 47.89           C  
-ATOM  10224  N   LYS C 376     -27.587  23.840-137.560  1.00 19.21           N  
-ATOM  10225  CA  LYS C 376     -28.223  24.345-138.769  1.00 24.99           C  
-ATOM  10226  C   LYS C 376     -28.062  23.320-139.885  1.00 27.99           C  
-ATOM  10227  O   LYS C 376     -28.990  23.047-140.654  1.00 25.19           O  
-ATOM  10228  CB  LYS C 376     -27.607  25.684-139.169  1.00 30.04           C  
-ATOM  10229  CG  LYS C 376     -28.143  26.261-140.464  1.00 26.25           C  
-ATOM  10230  CD  LYS C 376     -27.200  27.334-140.983  1.00 36.31           C  
-ATOM  10231  CE  LYS C 376     -27.634  27.865-142.340  1.00 44.33           C  
-ATOM  10232  NZ  LYS C 376     -28.790  28.798-142.240  1.00 45.31           N  
-ATOM  10233  N   GLY C 377     -26.867  22.743-139.942  1.00 21.76           N  
-ATOM  10234  CA  GLY C 377     -26.556  21.684-140.876  1.00 22.42           C  
-ATOM  10235  C   GLY C 377     -27.408  20.445-140.674  1.00 25.82           C  
-ATOM  10236  O   GLY C 377     -27.993  19.942-141.639  1.00 27.81           O  
-ATOM  10237  N   VAL C 378     -27.495  19.942-139.442  1.00 19.60           N  
-ATOM  10238  CA  VAL C 378     -28.267  18.709-139.242  1.00 25.34           C  
-ATOM  10239  C   VAL C 378     -29.750  18.943-139.544  1.00 27.19           C  
-ATOM  10240  O   VAL C 378     -30.405  18.084-140.148  1.00 29.38           O  
-ATOM  10241  CB  VAL C 378     -28.086  18.102-137.805  1.00 19.44           C  
-ATOM  10242  CG1 VAL C 378     -27.021  18.836-137.022  1.00 20.11           C  
-ATOM  10243  CG2 VAL C 378     -29.402  18.049-137.031  1.00 19.64           C  
-ATOM  10244  N   LEU C 379     -30.265  20.114-139.173  1.00 16.46           N  
-ATOM  10245  CA  LEU C 379     -31.666  20.439-139.422  1.00 17.16           C  
-ATOM  10246  C   LEU C 379     -31.955  20.534-140.913  1.00 20.12           C  
-ATOM  10247  O   LEU C 379     -32.860  19.872-141.422  1.00 23.16           O  
-ATOM  10248  CB  LEU C 379     -32.052  21.751-138.724  1.00 24.35           C  
-ATOM  10249  CG  LEU C 379     -33.465  22.266-139.016  1.00 20.93           C  
-ATOM  10250  CD1 LEU C 379     -34.520  21.255-138.589  1.00 17.30           C  
-ATOM  10251  CD2 LEU C 379     -33.708  23.608-138.344  1.00 19.38           C  
-ATOM  10252  N   GLU C 380     -31.182  21.364-141.604  1.00 18.75           N  
-ATOM  10253  CA  GLU C 380     -31.381  21.573-143.033  1.00 23.99           C  
-ATOM  10254  C   GLU C 380     -31.242  20.268-143.803  1.00 25.97           C  
-ATOM  10255  O   GLU C 380     -32.054  19.968-144.677  1.00 23.96           O  
-ATOM  10256  CB  GLU C 380     -30.392  22.615-143.569  1.00 23.76           C  
-ATOM  10257  CG  GLU C 380     -31.012  23.578-144.556  1.00 31.18           C  
-ATOM  10258  CD  GLU C 380     -32.195  24.321-143.966  1.00 37.77           C  
-ATOM  10259  OE1 GLU C 380     -33.328  24.137-144.463  1.00 38.16           O  
-ATOM  10260  OE2 GLU C 380     -31.992  25.084-142.998  1.00 28.92           O  
-ATOM  10261  N   GLU C 381     -30.222  19.486-143.461  1.00 24.24           N  
-ATOM  10262  CA  GLU C 381     -29.992  18.213-144.136  1.00 27.59           C  
-ATOM  10263  C   GLU C 381     -31.114  17.215-143.858  1.00 25.44           C  
-ATOM  10264  O   GLU C 381     -31.478  16.432-144.733  1.00 22.27           O  
-ATOM  10265  CB  GLU C 381     -28.649  17.599-143.725  1.00 35.61           C  
-ATOM  10266  CG  GLU C 381     -28.241  16.418-144.607  1.00 26.59           C  
-ATOM  10267  CD  GLU C 381     -27.206  15.518-143.962  1.00 34.16           C  
-ATOM  10268  OE1 GLU C 381     -26.369  14.948-144.693  1.00 38.04           O  
-ATOM  10269  OE2 GLU C 381     -27.242  15.367-142.724  1.00 41.22           O  
-ATOM  10270  N   LEU C 382     -31.660  17.235-142.644  1.00 23.53           N  
-ATOM  10271  CA  LEU C 382     -32.746  16.317-142.314  1.00 19.75           C  
-ATOM  10272  C   LEU C 382     -34.014  16.687-143.074  1.00 19.41           C  
-ATOM  10273  O   LEU C 382     -34.692  15.816-143.622  1.00 21.99           O  
-ATOM  10274  CB  LEU C 382     -33.015  16.298-140.804  1.00 17.48           C  
-ATOM  10275  CG  LEU C 382     -34.053  15.264-140.347  1.00 18.51           C  
-ATOM  10276  CD1 LEU C 382     -33.694  13.868-140.840  1.00 21.08           C  
-ATOM  10277  CD2 LEU C 382     -34.201  15.271-138.834  1.00 11.53           C  
-ATOM  10278  N   LEU C 383     -34.330  17.978-143.103  1.00 18.62           N  
-ATOM  10279  CA  LEU C 383     -35.478  18.457-143.871  1.00 18.53           C  
-ATOM  10280  C   LEU C 383     -35.317  18.081-145.337  1.00 22.22           C  
-ATOM  10281  O   LEU C 383     -36.267  17.671-145.998  1.00 25.21           O  
-ATOM  10282  CB  LEU C 383     -35.636  19.973-143.720  1.00 23.79           C  
-ATOM  10283  CG  LEU C 383     -36.590  20.455-142.623  1.00 18.81           C  
-ATOM  10284  CD1 LEU C 383     -36.684  19.442-141.500  1.00 21.72           C  
-ATOM  10285  CD2 LEU C 383     -36.134  21.801-142.088  1.00 23.88           C  
-ATOM  10286  N   TRP C 384     -34.089  18.227-145.821  1.00 20.36           N  
-ATOM  10287  CA  TRP C 384     -33.682  17.810-147.158  1.00 25.79           C  
-ATOM  10288  C   TRP C 384     -34.030  16.336-147.413  1.00 22.54           C  
-ATOM  10289  O   TRP C 384     -34.721  16.003-148.390  1.00 18.92           O  
-ATOM  10290  CB  TRP C 384     -32.174  18.069-147.316  1.00 28.51           C  
-ATOM  10291  CG  TRP C 384     -31.625  17.974-148.707  1.00 21.77           C  
-ATOM  10292  CD1 TRP C 384     -31.974  18.733-149.785  1.00 27.61           C  
-ATOM  10293  CD2 TRP C 384     -30.585  17.098-149.153  1.00 21.55           C  
-ATOM  10294  NE1 TRP C 384     -31.234  18.363-150.883  1.00 29.40           N  
-ATOM  10295  CE2 TRP C 384     -30.373  17.362-150.519  1.00 23.96           C  
-ATOM  10296  CE3 TRP C 384     -29.823  16.106-148.531  1.00 26.91           C  
-ATOM  10297  CZ2 TRP C 384     -29.428  16.671-151.274  1.00 26.49           C  
-ATOM  10298  CZ3 TRP C 384     -28.886  15.421-149.281  1.00 28.24           C  
-ATOM  10299  CH2 TRP C 384     -28.696  15.707-150.637  1.00 28.94           C  
-ATOM  10300  N   PHE C 385     -33.548  15.468-146.524  1.00 22.25           N  
-ATOM  10301  CA  PHE C 385     -33.859  14.041-146.560  1.00 21.04           C  
-ATOM  10302  C   PHE C 385     -35.353  13.785-146.648  1.00 21.91           C  
-ATOM  10303  O   PHE C 385     -35.806  13.004-147.481  1.00 25.10           O  
-ATOM  10304  CB  PHE C 385     -33.315  13.333-145.317  1.00 20.97           C  
-ATOM  10305  CG  PHE C 385     -31.829  13.173-145.306  1.00 22.33           C  
-ATOM  10306  CD1 PHE C 385     -31.104  13.202-146.485  1.00 23.92           C  
-ATOM  10307  CD2 PHE C 385     -31.153  12.987-144.112  1.00 21.71           C  
-ATOM  10308  CE1 PHE C 385     -29.731  13.053-146.473  1.00 25.93           C  
-ATOM  10309  CE2 PHE C 385     -29.776  12.836-144.092  1.00 20.80           C  
-ATOM  10310  CZ  PHE C 385     -29.066  12.869-145.273  1.00 28.22           C  
-ATOM  10311  N   ILE C 386     -36.108  14.436-145.770  1.00 18.54           N  
-ATOM  10312  CA  ILE C 386     -37.551  14.246-145.718  1.00 21.86           C  
-ATOM  10313  C   ILE C 386     -38.210  14.645-147.032  1.00 25.55           C  
-ATOM  10314  O   ILE C 386     -39.095  13.942-147.526  1.00 23.96           O  
-ATOM  10315  CB  ILE C 386     -38.173  15.039-144.549  1.00 21.97           C  
-ATOM  10316  CG1 ILE C 386     -37.694  14.453-143.218  1.00 18.50           C  
-ATOM  10317  CG2 ILE C 386     -39.692  15.012-144.623  1.00 20.82           C  
-ATOM  10318  CD1 ILE C 386     -38.331  15.077-142.014  1.00 14.10           C  
-ATOM  10319  N   ARG C 387     -37.769  15.762-147.605  1.00 31.44           N  
-ATOM  10320  CA  ARG C 387     -38.260  16.173-148.917  1.00 23.60           C  
-ATOM  10321  C   ARG C 387     -37.881  15.136-149.968  1.00 25.22           C  
-ATOM  10322  O   ARG C 387     -38.561  14.984-150.979  1.00 22.49           O  
-ATOM  10323  CB  ARG C 387     -37.712  17.547-149.308  1.00 19.99           C  
-ATOM  10324  CG  ARG C 387     -38.207  18.685-148.429  1.00 26.21           C  
-ATOM  10325  CD  ARG C 387     -37.802  20.047-148.977  1.00 15.11           C  
-ATOM  10326  NE  ARG C 387     -37.895  21.081-147.951  1.00 18.60           N  
-ATOM  10327  CZ  ARG C 387     -36.897  21.409-147.137  1.00 30.13           C  
-ATOM  10328  NH1 ARG C 387     -35.730  20.786-147.232  1.00 30.38           N  
-ATOM  10329  NH2 ARG C 387     -37.062  22.361-146.228  1.00 31.79           N  
-ATOM  10330  N   GLY C 388     -36.799  14.409-149.710  1.00 32.43           N  
-ATOM  10331  CA  GLY C 388     -36.349  13.380-150.630  1.00 24.63           C  
-ATOM  10332  C   GLY C 388     -35.587  14.035-151.758  1.00 29.57           C  
-ATOM  10333  O   GLY C 388     -35.501  13.512-152.868  1.00 29.69           O  
-ATOM  10334  N   ASP C 389     -35.038  15.204-151.455  1.00 25.81           N  
-ATOM  10335  CA  ASP C 389     -34.285  15.990-152.415  1.00 23.86           C  
-ATOM  10336  C   ASP C 389     -32.901  15.385-152.619  1.00 24.81           C  
-ATOM  10337  O   ASP C 389     -32.280  14.905-151.672  1.00 23.61           O  
-ATOM  10338  CB  ASP C 389     -34.183  17.433-151.926  1.00 33.36           C  
-ATOM  10339  CG  ASP C 389     -33.787  18.403-153.017  1.00 34.45           C  
-ATOM  10340  OD1 ASP C 389     -33.429  17.965-154.131  1.00 30.90           O  
-ATOM  10341  OD2 ASP C 389     -33.832  19.621-152.746  1.00 32.75           O  
-ATOM  10342  N   THR C 390     -32.427  15.403-153.859  1.00 30.55           N  
-ATOM  10343  CA  THR C 390     -31.117  14.852-154.182  1.00 25.41           C  
-ATOM  10344  C   THR C 390     -30.211  15.940-154.749  1.00 22.71           C  
-ATOM  10345  O   THR C 390     -29.112  15.666-155.230  1.00 24.11           O  
-ATOM  10346  CB  THR C 390     -31.231  13.690-155.181  1.00 21.40           C  
-ATOM  10347  OG1 THR C 390     -31.857  14.152-156.384  1.00 23.99           O  
-ATOM  10348  CG2 THR C 390     -32.069  12.569-154.587  1.00 25.58           C  
-ATOM  10349  N   ASN C 391     -30.687  17.178-154.676  1.00 25.14           N  
-ATOM  10350  CA  ASN C 391     -29.939  18.332-155.157  1.00 25.37           C  
-ATOM  10351  C   ASN C 391     -29.144  18.980-154.028  1.00 30.57           C  
-ATOM  10352  O   ASN C 391     -29.706  19.688-153.194  1.00 39.86           O  
-ATOM  10353  CB  ASN C 391     -30.894  19.348-155.790  1.00 27.02           C  
-ATOM  10354  CG  ASN C 391     -30.176  20.405-156.604  1.00 29.39           C  
-ATOM  10355  OD1 ASN C 391     -29.030  20.753-156.324  1.00 37.35           O  
-ATOM  10356  ND2 ASN C 391     -30.849  20.921-157.626  1.00 31.03           N  
-ATOM  10357  N   ALA C 392     -27.836  18.742-154.009  1.00 24.78           N  
-ATOM  10358  CA  ALA C 392     -26.985  19.239-152.935  1.00 25.00           C  
-ATOM  10359  C   ALA C 392     -26.848  20.758-152.965  1.00 29.18           C  
-ATOM  10360  O   ALA C 392     -26.466  21.373-151.971  1.00 34.90           O  
-ATOM  10361  CB  ALA C 392     -25.612  18.585-153.008  1.00 36.81           C  
-ATOM  10362  N   ASN C 393     -27.157  21.360-154.107  1.00 28.02           N  
-ATOM  10363  CA  ASN C 393     -27.058  22.807-154.245  1.00 29.32           C  
-ATOM  10364  C   ASN C 393     -28.092  23.526-153.390  1.00 39.14           C  
-ATOM  10365  O   ASN C 393     -27.862  24.648-152.939  1.00 43.48           O  
-ATOM  10366  CB  ASN C 393     -27.207  23.213-155.709  1.00 23.52           C  
-ATOM  10367  CG  ASN C 393     -26.145  22.592-156.591  1.00 32.63           C  
-ATOM  10368  OD1 ASN C 393     -24.978  22.493-156.205  1.00 31.57           O  
-ATOM  10369  ND2 ASN C 393     -26.544  22.166-157.783  1.00 37.00           N  
-ATOM  10370  N   HIS C 394     -29.231  22.875-153.170  1.00 35.24           N  
-ATOM  10371  CA  HIS C 394     -30.260  23.406-152.283  1.00 27.05           C  
-ATOM  10372  C   HIS C 394     -29.731  23.516-150.857  1.00 33.74           C  
-ATOM  10373  O   HIS C 394     -30.140  24.392-150.099  1.00 38.60           O  
-ATOM  10374  CB  HIS C 394     -31.509  22.528-152.318  1.00 26.14           C  
-ATOM  10375  CG  HIS C 394     -32.151  22.448-153.667  1.00 25.19           C  
-ATOM  10376  ND1 HIS C 394     -33.007  21.430-154.025  1.00 26.04           N  
-ATOM  10377  CD2 HIS C 394     -32.064  23.263-154.744  1.00 30.42           C  
-ATOM  10378  CE1 HIS C 394     -33.419  21.620-155.265  1.00 24.34           C  
-ATOM  10379  NE2 HIS C 394     -32.862  22.726-155.724  1.00 28.29           N  
-ATOM  10380  N   LEU C 395     -28.826  22.613-150.495  1.00 31.02           N  
-ATOM  10381  CA  LEU C 395     -28.172  22.670-149.195  1.00 32.59           C  
-ATOM  10382  C   LEU C 395     -27.043  23.688-149.208  1.00 38.67           C  
-ATOM  10383  O   LEU C 395     -26.804  24.381-148.220  1.00 37.79           O  
-ATOM  10384  CB  LEU C 395     -27.622  21.299-148.798  1.00 29.28           C  
-ATOM  10385  CG  LEU C 395     -28.593  20.277-148.213  1.00 29.65           C  
-ATOM  10386  CD1 LEU C 395     -27.859  18.982-147.906  1.00 31.79           C  
-ATOM  10387  CD2 LEU C 395     -29.259  20.829-146.963  1.00 30.99           C  
-ATOM  10388  N   SER C 396     -26.351  23.766-150.339  1.00 42.99           N  
-ATOM  10389  CA  SER C 396     -25.156  24.586-150.459  1.00 39.60           C  
-ATOM  10390  C   SER C 396     -25.473  26.076-150.438  1.00 38.74           C  
-ATOM  10391  O   SER C 396     -24.725  26.862-149.856  1.00 31.77           O  
-ATOM  10392  CB  SER C 396     -24.401  24.231-151.741  1.00 38.90           C  
-ATOM  10393  OG  SER C 396     -23.060  24.691-151.695  1.00 47.50           O  
-ATOM  10394  N   GLU C 397     -26.578  26.463-151.071  1.00 44.90           N  
-ATOM  10395  CA  GLU C 397     -26.938  27.877-151.167  1.00 47.15           C  
-ATOM  10396  C   GLU C 397     -27.685  28.353-149.915  1.00 39.61           C  
-ATOM  10397  O   GLU C 397     -27.991  29.540-149.770  1.00 46.73           O  
-ATOM  10398  CB  GLU C 397     -27.759  28.137-152.442  1.00 48.17           C  
-ATOM  10399  CG  GLU C 397     -29.243  28.415-152.243  1.00 54.47           C  
-ATOM  10400  CD  GLU C 397     -30.105  27.183-152.413  1.00 64.63           C  
-ATOM  10401  OE1 GLU C 397     -30.115  26.608-153.524  1.00 49.36           O  
-ATOM  10402  OE2 GLU C 397     -30.775  26.792-151.433  1.00 72.36           O  
-ATOM  10403  N   LYS C 398     -27.950  27.428-148.998  1.00 39.23           N  
-ATOM  10404  CA  LYS C 398     -28.503  27.789-147.698  1.00 35.69           C  
-ATOM  10405  C   LYS C 398     -27.402  27.941-146.651  1.00 32.97           C  
-ATOM  10406  O   LYS C 398     -27.671  28.308-145.509  1.00 32.51           O  
-ATOM  10407  CB  LYS C 398     -29.520  26.751-147.230  1.00 33.41           C  
-ATOM  10408  CG  LYS C 398     -30.827  26.767-148.001  1.00 40.59           C  
-ATOM  10409  CD  LYS C 398     -31.890  25.961-147.276  1.00 33.70           C  
-ATOM  10410  CE  LYS C 398     -33.152  25.833-148.108  1.00 34.30           C  
-ATOM  10411  NZ  LYS C 398     -32.883  25.102-149.374  1.00 34.81           N  
-ATOM  10412  N   GLY C 399     -26.163  27.657-147.043  1.00 30.16           N  
-ATOM  10413  CA  GLY C 399     -25.029  27.818-146.150  1.00 30.73           C  
-ATOM  10414  C   GLY C 399     -24.492  26.507-145.613  1.00 36.15           C  
-ATOM  10415  O   GLY C 399     -23.623  26.494-144.739  1.00 28.16           O  
-ATOM  10416  N   VAL C 400     -25.010  25.400-146.140  1.00 42.03           N  
-ATOM  10417  CA  VAL C 400     -24.583  24.068-145.716  1.00 39.55           C  
-ATOM  10418  C   VAL C 400     -23.840  23.356-146.847  1.00 42.11           C  
-ATOM  10419  O   VAL C 400     -24.456  22.770-147.739  1.00 41.48           O  
-ATOM  10420  CB  VAL C 400     -25.781  23.206-145.265  1.00 26.76           C  
-ATOM  10421  CG1 VAL C 400     -25.303  21.875-144.726  1.00 31.76           C  
-ATOM  10422  CG2 VAL C 400     -26.590  23.937-144.208  1.00 30.58           C  
-ATOM  10423  N   LYS C 401     -22.512  23.406-146.802  1.00 34.59           N  
-ATOM  10424  CA  LYS C 401     -21.692  22.891-147.895  1.00 40.62           C  
-ATOM  10425  C   LYS C 401     -21.108  21.521-147.584  1.00 46.49           C  
-ATOM  10426  O   LYS C 401     -20.056  21.153-148.104  1.00 53.00           O  
-ATOM  10427  CB  LYS C 401     -20.563  23.871-148.210  1.00 32.48           C  
-ATOM  10428  CG  LYS C 401     -21.035  25.249-148.628  1.00 33.47           C  
-ATOM  10429  CD  LYS C 401     -20.120  26.328-148.078  1.00 39.22           C  
-ATOM  10430  CE  LYS C 401     -20.141  26.340-146.552  1.00 61.58           C  
-ATOM  10431  NZ  LYS C 401     -19.251  27.391-145.976  1.00 44.91           N  
-ATOM  10432  N   ILE C 402     -21.805  20.766-146.746  1.00 44.79           N  
-ATOM  10433  CA  ILE C 402     -21.299  19.489-146.263  1.00 48.55           C  
-ATOM  10434  C   ILE C 402     -21.314  18.399-147.333  1.00 49.22           C  
-ATOM  10435  O   ILE C 402     -20.742  17.327-147.142  1.00 57.19           O  
-ATOM  10436  CB  ILE C 402     -22.109  19.006-145.053  1.00 41.51           C  
-ATOM  10437  CG1 ILE C 402     -23.490  18.526-145.501  1.00 48.30           C  
-ATOM  10438  CG2 ILE C 402     -22.243  20.125-144.038  1.00 46.19           C  
-ATOM  10439  CD1 ILE C 402     -24.354  18.010-144.377  1.00 42.98           C  
-ATOM  10440  N   TRP C 403     -21.963  18.677-148.460  1.00 42.46           N  
-ATOM  10441  CA  TRP C 403     -22.076  17.697-149.535  1.00 46.43           C  
-ATOM  10442  C   TRP C 403     -21.235  18.050-150.758  1.00 49.65           C  
-ATOM  10443  O   TRP C 403     -20.948  17.187-151.587  1.00 47.94           O  
-ATOM  10444  CB  TRP C 403     -23.538  17.541-149.955  1.00 42.82           C  
-ATOM  10445  CG  TRP C 403     -24.275  16.500-149.185  1.00 40.91           C  
-ATOM  10446  CD1 TRP C 403     -25.007  16.684-148.051  1.00 39.72           C  
-ATOM  10447  CD2 TRP C 403     -24.357  15.104-149.496  1.00 49.96           C  
-ATOM  10448  NE1 TRP C 403     -25.541  15.490-147.633  1.00 41.39           N  
-ATOM  10449  CE2 TRP C 403     -25.157  14.504-148.504  1.00 45.92           C  
-ATOM  10450  CE3 TRP C 403     -23.832  14.304-150.516  1.00 53.98           C  
-ATOM  10451  CZ2 TRP C 403     -25.446  13.142-148.502  1.00 48.58           C  
-ATOM  10452  CZ3 TRP C 403     -24.121  12.949-150.512  1.00 50.94           C  
-ATOM  10453  CH2 TRP C 403     -24.920  12.383-149.512  1.00 55.18           C  
-ATOM  10454  N   ASP C 404     -20.841  19.315-150.856  1.00 47.73           N  
-ATOM  10455  CA  ASP C 404     -20.173  19.843-152.043  1.00 46.12           C  
-ATOM  10456  C   ASP C 404     -18.983  19.006-152.511  1.00 40.64           C  
-ATOM  10457  O   ASP C 404     -18.906  18.614-153.678  1.00 46.07           O  
-ATOM  10458  CB  ASP C 404     -19.727  21.280-151.773  1.00 56.02           C  
-ATOM  10459  CG  ASP C 404     -20.901  22.222-151.547  1.00 53.27           C  
-ATOM  10460  OD1 ASP C 404     -22.042  21.738-151.375  1.00 53.96           O  
-ATOM  10461  OD2 ASP C 404     -20.677  23.450-151.537  1.00 35.28           O  
-ATOM  10462  N   LYS C 405     -18.074  18.711-151.589  1.00 38.53           N  
-ATOM  10463  CA  LYS C 405     -16.866  17.957-151.909  1.00 42.92           C  
-ATOM  10464  C   LYS C 405     -17.133  16.558-152.476  1.00 39.35           C  
-ATOM  10465  O   LYS C 405     -16.216  15.906-152.966  1.00 35.37           O  
-ATOM  10466  CB  LYS C 405     -15.979  17.839-150.667  1.00 41.04           C  
-ATOM  10467  CG  LYS C 405     -15.217  19.105-150.323  1.00 50.73           C  
-ATOM  10468  CD  LYS C 405     -14.327  18.892-149.114  1.00 55.74           C  
-ATOM  10469  CE  LYS C 405     -13.574  20.161-148.770  1.00 69.25           C  
-ATOM  10470  NZ  LYS C 405     -12.765  20.013-147.530  1.00 68.26           N  
-ATOM  10471  N   ASN C 406     -18.380  16.099-152.417  1.00 49.83           N  
-ATOM  10472  CA  ASN C 406     -18.727  14.774-152.929  1.00 46.00           C  
-ATOM  10473  C   ASN C 406     -19.691  14.838-154.106  1.00 37.70           C  
-ATOM  10474  O   ASN C 406     -20.214  13.818-154.547  1.00 39.90           O  
-ATOM  10475  CB  ASN C 406     -19.325  13.911-151.817  1.00 42.75           C  
-ATOM  10476  CG  ASN C 406     -18.306  13.541-150.760  1.00 51.33           C  
-ATOM  10477  OD1 ASN C 406     -18.402  13.971-149.612  1.00 70.29           O  
-ATOM  10478  ND2 ASN C 406     -17.322  12.738-151.144  1.00 49.10           N  
-ATOM  10479  N   VAL C 407     -19.933  16.045-154.605  1.00 39.56           N  
-ATOM  10480  CA  VAL C 407     -20.774  16.220-155.787  1.00 45.87           C  
-ATOM  10481  C   VAL C 407     -20.116  17.154-156.798  1.00 48.83           C  
-ATOM  10482  O   VAL C 407     -20.780  17.693-157.686  1.00 45.44           O  
-ATOM  10483  CB  VAL C 407     -22.172  16.768-155.424  1.00 44.50           C  
-ATOM  10484  CG1 VAL C 407     -22.997  15.704-154.711  1.00 40.59           C  
-ATOM  10485  CG2 VAL C 407     -22.053  18.027-154.583  1.00 41.83           C  
-ATOM  10486  N   THR C 408     -18.807  17.337-156.658  1.00 47.47           N  
-ATOM  10487  CA  THR C 408     -18.033  18.081-157.643  1.00 41.79           C  
-ATOM  10488  C   THR C 408     -18.003  17.304-158.952  1.00 49.66           C  
-ATOM  10489  O   THR C 408     -18.244  16.098-158.963  1.00 50.05           O  
-ATOM  10490  CB  THR C 408     -16.586  18.333-157.170  1.00 36.93           C  
-ATOM  10491  OG1 THR C 408     -15.901  17.083-157.031  1.00 36.05           O  
-ATOM  10492  CG2 THR C 408     -16.572  19.057-155.842  1.00 37.93           C  
-ATOM  10493  N   ARG C 409     -17.713  17.992-160.051  1.00 46.61           N  
-ATOM  10494  CA  ARG C 409     -17.558  17.332-161.342  1.00 45.56           C  
-ATOM  10495  C   ARG C 409     -16.449  16.283-161.269  1.00 49.38           C  
-ATOM  10496  O   ARG C 409     -16.586  15.175-161.793  1.00 52.59           O  
-ATOM  10497  CB  ARG C 409     -17.260  18.364-162.435  1.00 39.37           C  
-ATOM  10498  CG  ARG C 409     -16.659  17.799-163.714  1.00 45.59           C  
-ATOM  10499  CD  ARG C 409     -17.719  17.381-164.720  1.00 45.73           C  
-ATOM  10500  NE  ARG C 409     -18.341  16.103-164.390  1.00 51.50           N  
-ATOM  10501  CZ  ARG C 409     -19.564  15.974-163.885  1.00 61.26           C  
-ATOM  10502  NH1 ARG C 409     -20.304  17.050-163.649  1.00 58.74           N  
-ATOM  10503  NH2 ARG C 409     -20.050  14.769-163.618  1.00 56.86           N  
-ATOM  10504  N   GLU C 410     -15.362  16.640-160.592  1.00 47.10           N  
-ATOM  10505  CA  GLU C 410     -14.206  15.766-160.451  1.00 44.74           C  
-ATOM  10506  C   GLU C 410     -14.549  14.477-159.707  1.00 45.57           C  
-ATOM  10507  O   GLU C 410     -14.165  13.384-160.131  1.00 45.03           O  
-ATOM  10508  CB  GLU C 410     -13.074  16.510-159.734  1.00 44.32           C  
-ATOM  10509  CG  GLU C 410     -11.726  15.811-159.796  1.00 67.63           C  
-ATOM  10510  CD  GLU C 410     -10.621  16.618-159.138  1.00 81.33           C  
-ATOM  10511  OE1 GLU C 410     -10.696  16.838-157.910  1.00 85.88           O  
-ATOM  10512  OE2 GLU C 410      -9.678  17.034-159.846  1.00 75.64           O  
-ATOM  10513  N   PHE C 411     -15.276  14.608-158.600  1.00 50.28           N  
-ATOM  10514  CA  PHE C 411     -15.646  13.448-157.791  1.00 54.70           C  
-ATOM  10515  C   PHE C 411     -16.699  12.597-158.488  1.00 46.10           C  
-ATOM  10516  O   PHE C 411     -16.597  11.370-158.510  1.00 44.67           O  
-ATOM  10517  CB  PHE C 411     -16.159  13.877-156.411  1.00 39.77           C  
-ATOM  10518  CG  PHE C 411     -16.353  12.731-155.455  1.00 41.56           C  
-ATOM  10519  CD1 PHE C 411     -15.304  12.290-154.663  1.00 47.72           C  
-ATOM  10520  CD2 PHE C 411     -17.577  12.088-155.356  1.00 42.95           C  
-ATOM  10521  CE1 PHE C 411     -15.473  11.231-153.785  1.00 52.49           C  
-ATOM  10522  CE2 PHE C 411     -17.752  11.027-154.479  1.00 46.89           C  
-ATOM  10523  CZ  PHE C 411     -16.698  10.601-153.694  1.00 47.45           C  
-ATOM  10524  N   LEU C 412     -17.712  13.252-159.048  1.00 41.85           N  
-ATOM  10525  CA  LEU C 412     -18.753  12.560-159.800  1.00 42.76           C  
-ATOM  10526  C   LEU C 412     -18.151  11.770-160.957  1.00 51.41           C  
-ATOM  10527  O   LEU C 412     -18.624  10.682-161.290  1.00 51.37           O  
-ATOM  10528  CB  LEU C 412     -19.797  13.553-160.321  1.00 43.59           C  
-ATOM  10529  CG  LEU C 412     -20.786  14.112-159.293  1.00 47.66           C  
-ATOM  10530  CD1 LEU C 412     -21.677  15.177-159.917  1.00 46.56           C  
-ATOM  10531  CD2 LEU C 412     -21.626  12.996-158.686  1.00 38.64           C  
-ATOM  10532  N   ASP C 413     -17.104  12.322-161.563  1.00 55.29           N  
-ATOM  10533  CA  ASP C 413     -16.394  11.633-162.634  1.00 46.00           C  
-ATOM  10534  C   ASP C 413     -15.563  10.475-162.092  1.00 44.92           C  
-ATOM  10535  O   ASP C 413     -15.529   9.398-162.687  1.00 47.46           O  
-ATOM  10536  CB  ASP C 413     -15.507  12.611-163.404  1.00 47.28           C  
-ATOM  10537  CG  ASP C 413     -16.290  13.430-164.409  1.00 55.88           C  
-ATOM  10538  OD1 ASP C 413     -17.238  12.878-165.004  1.00 60.49           O  
-ATOM  10539  OD2 ASP C 413     -15.962  14.619-164.608  1.00 51.80           O  
-ATOM  10540  N   SER C 414     -14.900  10.696-160.960  1.00 43.23           N  
-ATOM  10541  CA  SER C 414     -14.099   9.650-160.330  1.00 41.71           C  
-ATOM  10542  C   SER C 414     -14.985   8.494-159.875  1.00 45.97           C  
-ATOM  10543  O   SER C 414     -14.506   7.387-159.635  1.00 48.77           O  
-ATOM  10544  CB  SER C 414     -13.317  10.208-159.140  1.00 49.34           C  
-ATOM  10545  OG  SER C 414     -14.060  10.076-157.939  1.00 47.89           O  
-ATOM  10546  N   ARG C 415     -16.280   8.770-159.757  1.00 52.56           N  
-ATOM  10547  CA  ARG C 415     -17.275   7.774-159.372  1.00 48.93           C  
-ATOM  10548  C   ARG C 415     -17.850   7.102-160.623  1.00 51.29           C  
-ATOM  10549  O   ARG C 415     -18.846   6.379-160.556  1.00 42.86           O  
-ATOM  10550  CB  ARG C 415     -18.386   8.435-158.547  1.00 44.12           C  
-ATOM  10551  CG  ARG C 415     -19.323   7.490-157.805  1.00 49.30           C  
-ATOM  10552  CD  ARG C 415     -18.744   7.021-156.482  1.00 47.34           C  
-ATOM  10553  NE  ARG C 415     -19.724   6.258-155.713  1.00 47.00           N  
-ATOM  10554  CZ  ARG C 415     -19.874   4.941-155.793  1.00 52.01           C  
-ATOM  10555  NH1 ARG C 415     -20.794   4.329-155.058  1.00 57.46           N  
-ATOM  10556  NH2 ARG C 415     -19.102   4.233-156.606  1.00 55.20           N  
-ATOM  10557  N   ASN C 416     -17.203   7.347-161.761  1.00 51.40           N  
-ATOM  10558  CA  ASN C 416     -17.655   6.843-163.055  1.00 43.32           C  
-ATOM  10559  C   ASN C 416     -19.098   7.261-163.332  1.00 37.55           C  
-ATOM  10560  O   ASN C 416     -19.959   6.426-163.601  1.00 34.58           O  
-ATOM  10561  CB  ASN C 416     -17.514   5.319-163.122  1.00 42.79           C  
-ATOM  10562  CG  ASN C 416     -17.446   4.798-164.547  1.00 55.71           C  
-ATOM  10563  OD1 ASN C 416     -17.807   5.494-165.497  1.00 58.22           O  
-ATOM  10564  ND2 ASN C 416     -16.981   3.563-164.701  1.00 56.12           N  
-ATOM  10565  N   LEU C 417     -19.352   8.564-163.253  1.00 43.55           N  
-ATOM  10566  CA  LEU C 417     -20.687   9.113-163.475  1.00 47.97           C  
-ATOM  10567  C   LEU C 417     -20.642  10.496-164.120  1.00 48.46           C  
-ATOM  10568  O   LEU C 417     -20.981  11.491-163.480  1.00 42.10           O  
-ATOM  10569  CB  LEU C 417     -21.453   9.186-162.154  1.00 42.40           C  
-ATOM  10570  CG  LEU C 417     -22.414   8.039-161.849  1.00 42.56           C  
-ATOM  10571  CD1 LEU C 417     -22.906   8.135-160.418  1.00 34.23           C  
-ATOM  10572  CD2 LEU C 417     -23.580   8.072-162.822  1.00 50.87           C  
-ATOM  10573  N   PRO C 418     -20.227  10.565-165.395  1.00 51.48           N  
-ATOM  10574  CA  PRO C 418     -20.108  11.857-166.078  1.00 51.55           C  
-ATOM  10575  C   PRO C 418     -21.458  12.480-166.415  1.00 48.55           C  
-ATOM  10576  O   PRO C 418     -21.537  13.687-166.633  1.00 55.95           O  
-ATOM  10577  CB  PRO C 418     -19.340  11.509-167.364  1.00 54.62           C  
-ATOM  10578  CG  PRO C 418     -18.763  10.141-167.127  1.00 54.27           C  
-ATOM  10579  CD  PRO C 418     -19.750   9.461-166.242  1.00 51.21           C  
-ATOM  10580  N   HIS C 419     -22.505  11.662-166.446  1.00 49.08           N  
-ATOM  10581  CA  HIS C 419     -23.831  12.123-166.846  1.00 51.46           C  
-ATOM  10582  C   HIS C 419     -24.514  12.955-165.764  1.00 42.94           C  
-ATOM  10583  O   HIS C 419     -25.543  13.584-166.009  1.00 31.90           O  
-ATOM  10584  CB  HIS C 419     -24.708  10.926-167.222  1.00 66.73           C  
-ATOM  10585  CG  HIS C 419     -24.292  10.254-168.495  1.00 97.23           C  
-ATOM  10586  ND1 HIS C 419     -24.914  10.494-169.701  1.00 99.18           N  
-ATOM  10587  CD2 HIS C 419     -23.310   9.357-168.751  1.00 90.65           C  
-ATOM  10588  CE1 HIS C 419     -24.337   9.771-170.644  1.00 86.58           C  
-ATOM  10589  NE2 HIS C 419     -23.361   9.072-170.094  1.00 91.38           N  
-ATOM  10590  N   ARG C 420     -23.933  12.958-164.569  1.00 45.35           N  
-ATOM  10591  CA  ARG C 420     -24.516  13.663-163.434  1.00 36.07           C  
-ATOM  10592  C   ARG C 420     -24.192  15.150-163.447  1.00 43.41           C  
-ATOM  10593  O   ARG C 420     -23.030  15.544-163.558  1.00 40.24           O  
-ATOM  10594  CB  ARG C 420     -24.030  13.051-162.119  1.00 36.56           C  
-ATOM  10595  CG  ARG C 420     -24.587  11.669-161.825  1.00 45.00           C  
-ATOM  10596  CD  ARG C 420     -25.909  11.743-161.078  1.00 28.03           C  
-ATOM  10597  NE  ARG C 420     -26.417  10.412-160.757  1.00 34.35           N  
-ATOM  10598  CZ  ARG C 420     -27.311   9.756-161.492  1.00 42.55           C  
-ATOM  10599  NH1 ARG C 420     -27.716   8.546-161.129  1.00 41.03           N  
-ATOM  10600  NH2 ARG C 420     -27.802  10.312-162.590  1.00 40.07           N  
-ATOM  10601  N   GLU C 421     -25.231  15.971-163.331  1.00 41.10           N  
-ATOM  10602  CA  GLU C 421     -25.066  17.406-163.151  1.00 35.94           C  
-ATOM  10603  C   GLU C 421     -24.410  17.665-161.795  1.00 42.32           C  
-ATOM  10604  O   GLU C 421     -24.574  16.876-160.867  1.00 55.85           O  
-ATOM  10605  CB  GLU C 421     -26.422  18.107-163.253  1.00 35.50           C  
-ATOM  10606  CG  GLU C 421     -26.369  19.624-163.299  1.00 51.22           C  
-ATOM  10607  CD  GLU C 421     -27.731  20.233-163.579  1.00 57.45           C  
-ATOM  10608  OE1 GLU C 421     -28.403  19.773-164.529  1.00 47.35           O  
-ATOM  10609  OE2 GLU C 421     -28.134  21.159-162.844  1.00 50.70           O  
-ATOM  10610  N   VAL C 422     -23.657  18.755-161.683  1.00 46.59           N  
-ATOM  10611  CA  VAL C 422     -22.953  19.063-160.438  1.00 46.28           C  
-ATOM  10612  C   VAL C 422     -23.929  19.328-159.295  1.00 38.16           C  
-ATOM  10613  O   VAL C 422     -24.713  20.277-159.340  1.00 37.80           O  
-ATOM  10614  CB  VAL C 422     -22.023  20.281-160.592  1.00 44.71           C  
-ATOM  10615  CG1 VAL C 422     -21.403  20.644-159.252  1.00 33.67           C  
-ATOM  10616  CG2 VAL C 422     -20.940  19.996-161.623  1.00 52.03           C  
-ATOM  10617  N   GLY C 423     -23.877  18.479-158.272  1.00 38.01           N  
-ATOM  10618  CA  GLY C 423     -24.747  18.614-157.117  1.00 39.97           C  
-ATOM  10619  C   GLY C 423     -25.703  17.447-156.946  1.00 41.53           C  
-ATOM  10620  O   GLY C 423     -26.340  17.299-155.901  1.00 36.30           O  
-ATOM  10621  N   ASP C 424     -25.804  16.616-157.979  1.00 41.94           N  
-ATOM  10622  CA  ASP C 424     -26.706  15.471-157.964  1.00 26.65           C  
-ATOM  10623  C   ASP C 424     -26.068  14.288-157.244  1.00 27.87           C  
-ATOM  10624  O   ASP C 424     -25.126  13.678-157.745  1.00 42.33           O  
-ATOM  10625  CB  ASP C 424     -27.093  15.083-159.392  1.00 29.39           C  
-ATOM  10626  CG  ASP C 424     -28.374  14.273-159.453  1.00 37.00           C  
-ATOM  10627  OD1 ASP C 424     -28.662  13.527-158.493  1.00 34.10           O  
-ATOM  10628  OD2 ASP C 424     -29.097  14.384-160.467  1.00 37.54           O  
-ATOM  10629  N   ILE C 425     -26.595  13.968-156.068  1.00 26.47           N  
-ATOM  10630  CA  ILE C 425     -26.067  12.880-155.255  1.00 25.19           C  
-ATOM  10631  C   ILE C 425     -26.563  11.526-155.743  1.00 27.20           C  
-ATOM  10632  O   ILE C 425     -26.159  10.485-155.226  1.00 31.68           O  
-ATOM  10633  CB  ILE C 425     -26.461  13.042-153.781  1.00 26.60           C  
-ATOM  10634  CG1 ILE C 425     -27.950  12.740-153.598  1.00 24.67           C  
-ATOM  10635  CG2 ILE C 425     -26.140  14.446-153.302  1.00 32.72           C  
-ATOM  10636  CD1 ILE C 425     -28.374  12.609-152.156  1.00 26.44           C  
-ATOM  10637  N   GLY C 426     -27.443  11.548-156.738  1.00 29.57           N  
-ATOM  10638  CA  GLY C 426     -28.053  10.336-157.246  1.00 29.73           C  
-ATOM  10639  C   GLY C 426     -29.169   9.859-156.338  1.00 28.86           C  
-ATOM  10640  O   GLY C 426     -29.623  10.599-155.468  1.00 31.12           O  
-ATOM  10641  N   PRO C 427     -29.616   8.610-156.532  1.00 33.32           N  
-ATOM  10642  CA  PRO C 427     -30.706   8.027-155.742  1.00 30.44           C  
-ATOM  10643  C   PRO C 427     -30.280   7.623-154.329  1.00 35.37           C  
-ATOM  10644  O   PRO C 427     -30.254   6.432-154.021  1.00 34.37           O  
-ATOM  10645  CB  PRO C 427     -31.097   6.794-156.560  1.00 28.81           C  
-ATOM  10646  CG  PRO C 427     -29.842   6.397-157.244  1.00 32.21           C  
-ATOM  10647  CD  PRO C 427     -29.125   7.681-157.564  1.00 34.45           C  
-ATOM  10648  N   GLY C 428     -29.970   8.597-153.479  1.00 33.97           N  
-ATOM  10649  CA  GLY C 428     -29.493   8.298-152.139  1.00 37.08           C  
-ATOM  10650  C   GLY C 428     -30.313   8.881-150.999  1.00 44.65           C  
-ATOM  10651  O   GLY C 428     -31.075   9.832-151.187  1.00 48.78           O  
-ATOM  10652  N   TYR C 429     -30.137   8.293-149.815  1.00 39.57           N  
-ATOM  10653  CA  TYR C 429     -30.795   8.719-148.577  1.00 28.02           C  
-ATOM  10654  C   TYR C 429     -32.275   9.070-148.742  1.00 29.33           C  
-ATOM  10655  O   TYR C 429     -33.137   8.197-148.683  1.00 37.11           O  
-ATOM  10656  CB  TYR C 429     -30.050   9.909-147.970  1.00 29.11           C  
-ATOM  10657  CG  TYR C 429     -28.693   9.562-147.397  1.00 31.42           C  
-ATOM  10658  CD1 TYR C 429     -28.560   8.591-146.413  1.00 27.97           C  
-ATOM  10659  CD2 TYR C 429     -27.549  10.221-147.825  1.00 39.23           C  
-ATOM  10660  CE1 TYR C 429     -27.322   8.274-145.883  1.00 29.21           C  
-ATOM  10661  CE2 TYR C 429     -26.306   9.915-147.298  1.00 43.35           C  
-ATOM  10662  CZ  TYR C 429     -26.199   8.942-146.327  1.00 40.42           C  
-ATOM  10663  OH  TYR C 429     -24.962   8.640-145.806  1.00 43.81           O  
-ATOM  10664  N   GLY C 430     -32.560  10.352-148.941  1.00 26.68           N  
-ATOM  10665  CA  GLY C 430     -33.929  10.820-149.070  1.00 27.30           C  
-ATOM  10666  C   GLY C 430     -34.713  10.149-150.181  1.00 26.48           C  
-ATOM  10667  O   GLY C 430     -35.887   9.803-150.012  1.00 28.98           O  
-ATOM  10668  N   PHE C 431     -34.057   9.964-151.322  1.00 26.49           N  
-ATOM  10669  CA  PHE C 431     -34.701   9.357-152.478  1.00 30.73           C  
-ATOM  10670  C   PHE C 431     -35.131   7.928-152.203  1.00 28.02           C  
-ATOM  10671  O   PHE C 431     -36.141   7.474-152.733  1.00 26.79           O  
-ATOM  10672  CB  PHE C 431     -33.780   9.377-153.696  1.00 30.89           C  
-ATOM  10673  CG  PHE C 431     -34.397   8.767-154.927  1.00 32.09           C  
-ATOM  10674  CD1 PHE C 431     -35.221   9.517-155.749  1.00 31.86           C  
-ATOM  10675  CD2 PHE C 431     -34.163   7.441-155.253  1.00 22.78           C  
-ATOM  10676  CE1 PHE C 431     -35.791   8.959-156.877  1.00 32.37           C  
-ATOM  10677  CE2 PHE C 431     -34.729   6.877-156.380  1.00 21.87           C  
-ATOM  10678  CZ  PHE C 431     -35.545   7.636-157.194  1.00 25.56           C  
-ATOM  10679  N   GLN C 432     -34.356   7.211-151.398  1.00 29.61           N  
-ATOM  10680  CA  GLN C 432     -34.716   5.844-151.055  1.00 28.94           C  
-ATOM  10681  C   GLN C 432     -35.793   5.865-149.979  1.00 27.36           C  
-ATOM  10682  O   GLN C 432     -36.730   5.071-150.015  1.00 34.12           O  
-ATOM  10683  CB  GLN C 432     -33.482   5.053-150.603  1.00 35.89           C  
-ATOM  10684  CG  GLN C 432     -32.417   4.891-151.692  1.00 33.45           C  
-ATOM  10685  CD  GLN C 432     -32.908   4.080-152.888  1.00 32.95           C  
-ATOM  10686  OE1 GLN C 432     -33.824   3.264-152.770  1.00 33.54           O  
-ATOM  10687  NE2 GLN C 432     -32.294   4.301-154.044  1.00 34.65           N  
-ATOM  10688  N   TRP C 433     -35.654   6.796-149.039  1.00 29.28           N  
-ATOM  10689  CA  TRP C 433     -36.642   7.012-147.984  1.00 31.88           C  
-ATOM  10690  C   TRP C 433     -38.053   7.187-148.533  1.00 28.81           C  
-ATOM  10691  O   TRP C 433     -38.991   6.524-148.090  1.00 26.65           O  
-ATOM  10692  CB  TRP C 433     -36.289   8.251-147.153  1.00 24.57           C  
-ATOM  10693  CG  TRP C 433     -35.188   8.075-146.161  1.00 26.10           C  
-ATOM  10694  CD1 TRP C 433     -34.267   7.070-146.118  1.00 24.24           C  
-ATOM  10695  CD2 TRP C 433     -34.897   8.933-145.054  1.00 30.80           C  
-ATOM  10696  NE1 TRP C 433     -33.416   7.252-145.057  1.00 29.94           N  
-ATOM  10697  CE2 TRP C 433     -33.782   8.389-144.387  1.00 33.76           C  
-ATOM  10698  CE3 TRP C 433     -35.471  10.109-144.562  1.00 25.74           C  
-ATOM  10699  CZ2 TRP C 433     -33.231   8.983-143.252  1.00 25.78           C  
-ATOM  10700  CZ3 TRP C 433     -34.924  10.695-143.441  1.00 27.01           C  
-ATOM  10701  CH2 TRP C 433     -33.816  10.132-142.797  1.00 21.64           C  
-ATOM  10702  N   ARG C 434     -38.190   8.086-149.503  1.00 28.72           N  
-ATOM  10703  CA  ARG C 434     -39.503   8.480-149.994  1.00 26.67           C  
-ATOM  10704  C   ARG C 434     -39.900   7.733-151.266  1.00 29.48           C  
-ATOM  10705  O   ARG C 434     -41.081   7.666-151.614  1.00 26.97           O  
-ATOM  10706  CB  ARG C 434     -39.533   9.992-150.238  1.00 21.74           C  
-ATOM  10707  CG  ARG C 434     -39.023  10.825-149.067  1.00 26.43           C  
-ATOM  10708  CD  ARG C 434     -39.645  10.383-147.750  1.00 24.80           C  
-ATOM  10709  NE  ARG C 434     -41.101  10.454-147.790  1.00 28.06           N  
-ATOM  10710  CZ  ARG C 434     -41.805  11.522-147.433  1.00 28.06           C  
-ATOM  10711  NH1 ARG C 434     -43.127  11.497-147.504  1.00 25.17           N  
-ATOM  10712  NH2 ARG C 434     -41.188  12.615-147.002  1.00 29.35           N  
-ATOM  10713  N   HIS C 435     -38.912   7.175-151.958  1.00 21.58           N  
-ATOM  10714  CA  HIS C 435     -39.166   6.495-153.220  1.00 23.34           C  
-ATOM  10715  C   HIS C 435     -38.272   5.283-153.422  1.00 25.87           C  
-ATOM  10716  O   HIS C 435     -37.653   5.157-154.474  1.00 34.44           O  
-ATOM  10717  CB  HIS C 435     -38.954   7.444-154.401  1.00 26.93           C  
-ATOM  10718  CG  HIS C 435     -39.476   8.828-154.178  1.00 27.69           C  
-ATOM  10719  ND1 HIS C 435     -40.785   9.180-154.424  1.00 35.21           N  
-ATOM  10720  CD2 HIS C 435     -38.861   9.949-153.733  1.00 30.45           C  
-ATOM  10721  CE1 HIS C 435     -40.955  10.459-154.138  1.00 36.90           C  
-ATOM  10722  NE2 HIS C 435     -39.804  10.949-153.717  1.00 26.85           N  
-ATOM  10723  N   PHE C 436     -38.200   4.393-152.437  1.00 23.42           N  
-ATOM  10724  CA  PHE C 436     -37.339   3.216-152.555  1.00 31.04           C  
-ATOM  10725  C   PHE C 436     -37.616   2.402-153.824  1.00 31.83           C  
-ATOM  10726  O   PHE C 436     -38.755   2.027-154.102  1.00 31.98           O  
-ATOM  10727  CB  PHE C 436     -37.490   2.307-151.334  1.00 29.59           C  
-ATOM  10728  CG  PHE C 436     -36.508   1.170-151.308  1.00 26.77           C  
-ATOM  10729  CD1 PHE C 436     -35.260   1.326-150.728  1.00 28.62           C  
-ATOM  10730  CD2 PHE C 436     -36.826  -0.049-151.881  1.00 27.10           C  
-ATOM  10731  CE1 PHE C 436     -34.351   0.283-150.714  1.00 30.53           C  
-ATOM  10732  CE2 PHE C 436     -35.921  -1.093-151.875  1.00 28.94           C  
-ATOM  10733  CZ  PHE C 436     -34.683  -0.928-151.287  1.00 30.02           C  
-ATOM  10734  N   GLY C 437     -36.562   2.137-154.591  1.00 28.75           N  
-ATOM  10735  CA  GLY C 437     -36.651   1.261-155.746  1.00 29.34           C  
-ATOM  10736  C   GLY C 437     -36.991   1.948-157.054  1.00 31.33           C  
-ATOM  10737  O   GLY C 437     -36.786   1.381-158.128  1.00 33.96           O  
-ATOM  10738  N   ALA C 438     -37.513   3.167-156.968  1.00 27.01           N  
-ATOM  10739  CA  ALA C 438     -37.903   3.920-158.154  1.00 28.04           C  
-ATOM  10740  C   ALA C 438     -36.715   4.156-159.088  1.00 34.86           C  
-ATOM  10741  O   ALA C 438     -35.571   4.247-158.642  1.00 26.76           O  
-ATOM  10742  CB  ALA C 438     -38.531   5.242-157.750  1.00 21.86           C  
-ATOM  10743  N   ALA C 439     -36.993   4.244-160.386  1.00 36.53           N  
-ATOM  10744  CA  ALA C 439     -35.952   4.490-161.378  1.00 35.13           C  
-ATOM  10745  C   ALA C 439     -35.535   5.955-161.362  1.00 31.03           C  
-ATOM  10746  O   ALA C 439     -36.364   6.848-161.537  1.00 37.68           O  
-ATOM  10747  CB  ALA C 439     -36.428   4.086-162.765  1.00 49.59           C  
-ATOM  10748  N   TYR C 440     -34.245   6.195-161.157  1.00 29.67           N  
-ATOM  10749  CA  TYR C 440     -33.729   7.551-161.017  1.00 30.97           C  
-ATOM  10750  C   TYR C 440     -33.341   8.160-162.361  1.00 33.46           C  
-ATOM  10751  O   TYR C 440     -32.812   7.476-163.235  1.00 39.69           O  
-ATOM  10752  CB  TYR C 440     -32.524   7.559-160.074  1.00 32.20           C  
-ATOM  10753  CG  TYR C 440     -32.095   8.940-159.630  1.00 36.33           C  
-ATOM  10754  CD1 TYR C 440     -32.744   9.586-158.586  1.00 33.28           C  
-ATOM  10755  CD2 TYR C 440     -31.039   9.596-160.250  1.00 38.59           C  
-ATOM  10756  CE1 TYR C 440     -32.356  10.846-158.174  1.00 29.70           C  
-ATOM  10757  CE2 TYR C 440     -30.643  10.858-159.845  1.00 31.49           C  
-ATOM  10758  CZ  TYR C 440     -31.306  11.476-158.806  1.00 30.49           C  
-ATOM  10759  OH  TYR C 440     -30.917  12.730-158.399  1.00 31.27           O  
-ATOM  10760  N   LYS C 441     -33.615   9.450-162.521  1.00 35.93           N  
-ATOM  10761  CA  LYS C 441     -33.182  10.189-163.702  1.00 33.88           C  
-ATOM  10762  C   LYS C 441     -32.179  11.263-163.295  1.00 34.43           C  
-ATOM  10763  O   LYS C 441     -30.971  11.042-163.338  1.00 36.36           O  
-ATOM  10764  CB  LYS C 441     -34.375  10.814-164.430  1.00 40.18           C  
-ATOM  10765  CG  LYS C 441     -35.151   9.850-165.320  1.00 44.77           C  
-ATOM  10766  CD  LYS C 441     -36.149   9.019-164.528  1.00 59.61           C  
-ATOM  10767  CE  LYS C 441     -36.878   8.028-165.426  1.00 65.26           C  
-ATOM  10768  NZ  LYS C 441     -37.569   8.711-166.555  1.00 68.20           N  
-ATOM  10769  N   ASP C 442     -32.685  12.427-162.903  1.00 36.94           N  
-ATOM  10770  CA  ASP C 442     -31.835  13.464-162.332  1.00 35.00           C  
-ATOM  10771  C   ASP C 442     -32.507  14.089-161.115  1.00 35.66           C  
-ATOM  10772  O   ASP C 442     -33.601  13.684-160.720  1.00 33.20           O  
-ATOM  10773  CB  ASP C 442     -31.489  14.539-163.373  1.00 36.53           C  
-ATOM  10774  CG  ASP C 442     -32.716  15.155-164.034  1.00 38.35           C  
-ATOM  10775  OD1 ASP C 442     -33.764  15.316-163.372  1.00 34.90           O  
-ATOM  10776  OD2 ASP C 442     -32.621  15.495-165.232  1.00 43.20           O  
-ATOM  10777  N   MET C 443     -31.850  15.083-160.531  1.00 33.32           N  
-ATOM  10778  CA  MET C 443     -32.351  15.727-159.325  1.00 27.45           C  
-ATOM  10779  C   MET C 443     -33.480  16.710-159.612  1.00 32.82           C  
-ATOM  10780  O   MET C 443     -34.029  17.313-158.691  1.00 42.36           O  
-ATOM  10781  CB  MET C 443     -31.214  16.447-158.608  1.00 27.63           C  
-ATOM  10782  CG  MET C 443     -30.544  17.513-159.448  1.00 26.21           C  
-ATOM  10783  SD  MET C 443     -29.020  18.089-158.688  1.00 36.99           S  
-ATOM  10784  CE  MET C 443     -28.388  19.171-159.966  1.00 46.88           C  
-ATOM  10785  N   HIS C 444     -33.821  16.874-160.886  1.00 38.32           N  
-ATOM  10786  CA  HIS C 444     -34.871  17.808-161.275  1.00 34.17           C  
-ATOM  10787  C   HIS C 444     -36.190  17.089-161.529  1.00 30.49           C  
-ATOM  10788  O   HIS C 444     -37.224  17.726-161.730  1.00 24.47           O  
-ATOM  10789  CB  HIS C 444     -34.453  18.593-162.520  1.00 27.31           C  
-ATOM  10790  CG  HIS C 444     -33.126  19.272-162.387  1.00 29.05           C  
-ATOM  10791  ND1 HIS C 444     -32.883  20.253-161.451  1.00 35.09           N  
-ATOM  10792  CD2 HIS C 444     -31.969  19.109-163.072  1.00 42.99           C  
-ATOM  10793  CE1 HIS C 444     -31.633  20.666-161.564  1.00 44.98           C  
-ATOM  10794  NE2 HIS C 444     -31.056  19.988-162.540  1.00 43.57           N  
-ATOM  10795  N   THR C 445     -36.150  15.761-161.508  1.00 35.75           N  
-ATOM  10796  CA  THR C 445     -37.316  14.955-161.851  1.00 41.36           C  
-ATOM  10797  C   THR C 445     -38.308  14.850-160.695  1.00 43.49           C  
-ATOM  10798  O   THR C 445     -37.915  14.782-159.530  1.00 39.05           O  
-ATOM  10799  CB  THR C 445     -36.905  13.532-162.280  1.00 38.82           C  
-ATOM  10800  OG1 THR C 445     -35.719  13.594-163.080  1.00 43.51           O  
-ATOM  10801  CG2 THR C 445     -38.022  12.861-163.071  1.00 32.54           C  
-ATOM  10802  N   ASP C 446     -39.596  14.842-161.028  1.00 45.08           N  
-ATOM  10803  CA  ASP C 446     -40.646  14.627-160.039  1.00 42.89           C  
-ATOM  10804  C   ASP C 446     -40.895  13.130-159.896  1.00 44.72           C  
-ATOM  10805  O   ASP C 446     -41.140  12.439-160.885  1.00 47.17           O  
-ATOM  10806  CB  ASP C 446     -41.933  15.353-160.441  1.00 42.21           C  
-ATOM  10807  CG  ASP C 446     -42.863  15.597-159.262  1.00 46.25           C  
-ATOM  10808  OD1 ASP C 446     -42.728  14.898-158.236  1.00 38.73           O  
-ATOM  10809  OD2 ASP C 446     -43.731  16.492-159.363  1.00 45.34           O  
-ATOM  10810  N   TYR C 447     -40.828  12.632-158.666  1.00 37.77           N  
-ATOM  10811  CA  TYR C 447     -40.966  11.200-158.423  1.00 37.21           C  
-ATOM  10812  C   TYR C 447     -42.180  10.861-157.570  1.00 33.53           C  
-ATOM  10813  O   TYR C 447     -42.260   9.764-157.016  1.00 30.65           O  
-ATOM  10814  CB  TYR C 447     -39.713  10.651-157.744  1.00 33.02           C  
-ATOM  10815  CG  TYR C 447     -38.445  10.826-158.538  1.00 30.23           C  
-ATOM  10816  CD1 TYR C 447     -38.108   9.935-159.546  1.00 31.97           C  
-ATOM  10817  CD2 TYR C 447     -37.574  11.872-158.268  1.00 41.86           C  
-ATOM  10818  CE1 TYR C 447     -36.943  10.086-160.271  1.00 41.27           C  
-ATOM  10819  CE2 TYR C 447     -36.406  12.032-158.987  1.00 47.67           C  
-ATOM  10820  CZ  TYR C 447     -36.095  11.135-159.986  1.00 40.86           C  
-ATOM  10821  OH  TYR C 447     -34.933  11.295-160.704  1.00 40.35           O  
-ATOM  10822  N   THR C 448     -43.118  11.796-157.458  1.00 34.13           N  
-ATOM  10823  CA  THR C 448     -44.265  11.599-156.580  1.00 37.29           C  
-ATOM  10824  C   THR C 448     -45.121  10.419-157.046  1.00 33.32           C  
-ATOM  10825  O   THR C 448     -45.592  10.381-158.185  1.00 25.73           O  
-ATOM  10826  CB  THR C 448     -45.130  12.885-156.473  1.00 32.33           C  
-ATOM  10827  OG1 THR C 448     -46.302  12.613-155.695  1.00 36.81           O  
-ATOM  10828  CG2 THR C 448     -45.538  13.402-157.850  1.00 40.53           C  
-ATOM  10829  N   GLY C 449     -45.288   9.441-156.160  1.00 28.78           N  
-ATOM  10830  CA  GLY C 449     -46.061   8.251-156.466  1.00 23.76           C  
-ATOM  10831  C   GLY C 449     -45.213   7.066-156.894  1.00 30.74           C  
-ATOM  10832  O   GLY C 449     -45.703   5.939-156.995  1.00 33.98           O  
-ATOM  10833  N   GLN C 450     -43.934   7.320-157.150  1.00 37.09           N  
-ATOM  10834  CA  GLN C 450     -43.016   6.270-157.576  1.00 31.43           C  
-ATOM  10835  C   GLN C 450     -42.239   5.701-156.388  1.00 35.11           C  
-ATOM  10836  O   GLN C 450     -41.806   6.444-155.505  1.00 33.50           O  
-ATOM  10837  CB  GLN C 450     -42.044   6.804-158.628  1.00 26.58           C  
-ATOM  10838  CG  GLN C 450     -42.716   7.393-159.860  1.00 24.17           C  
-ATOM  10839  CD  GLN C 450     -41.734   8.103-160.777  1.00 30.31           C  
-ATOM  10840  OE1 GLN C 450     -42.052   9.137-161.360  1.00 33.63           O  
-ATOM  10841  NE2 GLN C 450     -40.533   7.548-160.908  1.00 30.65           N  
-ATOM  10842  N   GLY C 451     -42.071   4.382-156.369  1.00 32.44           N  
-ATOM  10843  CA  GLY C 451     -41.297   3.724-155.332  1.00 23.17           C  
-ATOM  10844  C   GLY C 451     -42.032   3.599-154.013  1.00 24.12           C  
-ATOM  10845  O   GLY C 451     -43.200   3.970-153.902  1.00 23.37           O  
-ATOM  10846  N   VAL C 452     -41.340   3.074-153.006  1.00 25.45           N  
-ATOM  10847  CA  VAL C 452     -41.931   2.874-151.688  1.00 23.45           C  
-ATOM  10848  C   VAL C 452     -41.654   4.066-150.775  1.00 28.19           C  
-ATOM  10849  O   VAL C 452     -40.512   4.512-150.662  1.00 30.76           O  
-ATOM  10850  CB  VAL C 452     -41.396   1.594-151.022  1.00 22.04           C  
-ATOM  10851  CG1 VAL C 452     -42.055   1.381-149.669  1.00 27.33           C  
-ATOM  10852  CG2 VAL C 452     -41.624   0.390-151.928  1.00 19.46           C  
-ATOM  10853  N   ASP C 453     -42.699   4.584-150.133  1.00 30.73           N  
-ATOM  10854  CA  ASP C 453     -42.545   5.687-149.186  1.00 26.75           C  
-ATOM  10855  C   ASP C 453     -42.379   5.145-147.768  1.00 29.28           C  
-ATOM  10856  O   ASP C 453     -43.326   5.124-146.971  1.00 37.22           O  
-ATOM  10857  CB  ASP C 453     -43.736   6.644-149.261  1.00 33.57           C  
-ATOM  10858  CG  ASP C 453     -43.458   7.981-148.590  1.00 36.95           C  
-ATOM  10859  OD1 ASP C 453     -42.800   8.003-147.526  1.00 34.84           O  
-ATOM  10860  OD2 ASP C 453     -43.901   9.016-149.130  1.00 33.74           O  
-ATOM  10861  N   GLN C 454     -41.157   4.721-147.469  1.00 20.11           N  
-ATOM  10862  CA  GLN C 454     -40.832   4.102-146.195  1.00 20.81           C  
-ATOM  10863  C   GLN C 454     -41.175   4.984-145.003  1.00 23.76           C  
-ATOM  10864  O   GLN C 454     -41.595   4.482-143.966  1.00 24.01           O  
-ATOM  10865  CB  GLN C 454     -39.350   3.740-146.144  1.00 27.08           C  
-ATOM  10866  CG  GLN C 454     -38.932   2.658-147.121  1.00 25.95           C  
-ATOM  10867  CD  GLN C 454     -37.505   2.207-146.897  1.00 25.17           C  
-ATOM  10868  OE1 GLN C 454     -37.240   1.326-146.075  1.00 19.83           O  
-ATOM  10869  NE2 GLN C 454     -36.573   2.812-147.625  1.00 24.17           N  
-ATOM  10870  N   LEU C 455     -40.989   6.293-145.145  1.00 24.98           N  
-ATOM  10871  CA  LEU C 455     -41.255   7.210-144.042  1.00 25.84           C  
-ATOM  10872  C   LEU C 455     -42.747   7.240-143.711  1.00 33.08           C  
-ATOM  10873  O   LEU C 455     -43.142   7.161-142.540  1.00 31.23           O  
-ATOM  10874  CB  LEU C 455     -40.747   8.614-144.379  1.00 22.90           C  
-ATOM  10875  CG  LEU C 455     -40.670   9.610-143.218  1.00 24.84           C  
-ATOM  10876  CD1 LEU C 455     -39.839   9.045-142.076  1.00 19.07           C  
-ATOM  10877  CD2 LEU C 455     -40.100  10.940-143.686  1.00 19.03           C  
-ATOM  10878  N   LYS C 456     -43.572   7.337-144.749  1.00 30.05           N  
-ATOM  10879  CA  LYS C 456     -45.018   7.355-144.568  1.00 30.39           C  
-ATOM  10880  C   LYS C 456     -45.500   6.020-144.018  1.00 38.95           C  
-ATOM  10881  O   LYS C 456     -46.349   5.981-143.128  1.00 34.60           O  
-ATOM  10882  CB  LYS C 456     -45.731   7.679-145.884  1.00 28.65           C  
-ATOM  10883  CG  LYS C 456     -47.123   8.266-145.694  1.00 34.03           C  
-ATOM  10884  CD  LYS C 456     -47.763   8.618-147.028  1.00 38.66           C  
-ATOM  10885  CE  LYS C 456     -48.053   7.377-147.856  1.00 59.94           C  
-ATOM  10886  NZ  LYS C 456     -48.610   7.734-149.193  1.00 61.76           N  
-ATOM  10887  N   ASN C 457     -44.951   4.930-144.547  1.00 39.31           N  
-ATOM  10888  CA  ASN C 457     -45.260   3.596-144.031  1.00 41.96           C  
-ATOM  10889  C   ASN C 457     -44.977   3.497-142.533  1.00 33.15           C  
-ATOM  10890  O   ASN C 457     -45.836   3.084-141.750  1.00 34.23           O  
-ATOM  10891  CB  ASN C 457     -44.466   2.525-144.787  1.00 25.71           C  
-ATOM  10892  CG  ASN C 457     -45.069   2.199-146.140  1.00 32.40           C  
-ATOM  10893  OD1 ASN C 457     -45.924   2.927-146.647  1.00 32.70           O  
-ATOM  10894  ND2 ASN C 457     -44.623   1.098-146.733  1.00 41.26           N  
-ATOM  10895  N   VAL C 458     -43.765   3.885-142.151  1.00 25.79           N  
-ATOM  10896  CA  VAL C 458     -43.339   3.891-140.757  1.00 24.89           C  
-ATOM  10897  C   VAL C 458     -44.273   4.717-139.884  1.00 27.24           C  
-ATOM  10898  O   VAL C 458     -44.698   4.270-138.818  1.00 28.90           O  
-ATOM  10899  CB  VAL C 458     -41.904   4.439-140.616  1.00 20.44           C  
-ATOM  10900  CG1 VAL C 458     -41.637   4.893-139.193  1.00 21.44           C  
-ATOM  10901  CG2 VAL C 458     -40.889   3.390-141.047  1.00 22.30           C  
-ATOM  10902  N   ILE C 459     -44.602   5.920-140.340  1.00 27.56           N  
-ATOM  10903  CA  ILE C 459     -45.446   6.801-139.543  1.00 32.67           C  
-ATOM  10904  C   ILE C 459     -46.854   6.241-139.363  1.00 31.15           C  
-ATOM  10905  O   ILE C 459     -47.340   6.156-138.236  1.00 27.45           O  
-ATOM  10906  CB  ILE C 459     -45.521   8.209-140.155  1.00 29.72           C  
-ATOM  10907  CG1 ILE C 459     -44.165   8.902-140.014  1.00 18.49           C  
-ATOM  10908  CG2 ILE C 459     -46.599   9.029-139.469  1.00 23.11           C  
-ATOM  10909  CD1 ILE C 459     -44.165  10.323-140.480  1.00 30.46           C  
-ATOM  10910  N   GLN C 460     -47.500   5.851-140.459  1.00 38.49           N  
-ATOM  10911  CA  GLN C 460     -48.842   5.273-140.373  1.00 39.79           C  
-ATOM  10912  C   GLN C 460     -48.851   4.036-139.477  1.00 31.74           C  
-ATOM  10913  O   GLN C 460     -49.731   3.877-138.627  1.00 29.50           O  
-ATOM  10914  CB  GLN C 460     -49.376   4.930-141.768  1.00 45.89           C  
-ATOM  10915  CG  GLN C 460     -49.829   6.141-142.567  1.00 58.00           C  
-ATOM  10916  CD  GLN C 460     -50.485   5.759-143.884  1.00 79.33           C  
-ATOM  10917  OE1 GLN C 460     -51.017   4.657-144.032  1.00 81.77           O  
-ATOM  10918  NE2 GLN C 460     -50.449   6.672-144.849  1.00 62.67           N  
-ATOM  10919  N   MET C 461     -47.853   3.178-139.660  1.00 31.26           N  
-ATOM  10920  CA  MET C 461     -47.713   1.982-138.840  1.00 31.96           C  
-ATOM  10921  C   MET C 461     -47.552   2.348-137.369  1.00 29.05           C  
-ATOM  10922  O   MET C 461     -48.004   1.617-136.491  1.00 36.02           O  
-ATOM  10923  CB  MET C 461     -46.523   1.138-139.307  1.00 37.26           C  
-ATOM  10924  CG  MET C 461     -46.456  -0.246-138.672  1.00 41.71           C  
-ATOM  10925  SD  MET C 461     -47.923  -1.226-139.036  1.00 45.53           S  
-ATOM  10926  CE  MET C 461     -47.813  -1.328-140.821  1.00 43.36           C  
-ATOM  10927  N   LEU C 462     -46.907   3.479-137.103  1.00 36.37           N  
-ATOM  10928  CA  LEU C 462     -46.747   3.952-135.731  1.00 29.53           C  
-ATOM  10929  C   LEU C 462     -48.065   4.453-135.156  1.00 27.70           C  
-ATOM  10930  O   LEU C 462     -48.359   4.251-133.981  1.00 29.87           O  
-ATOM  10931  CB  LEU C 462     -45.695   5.060-135.665  1.00 23.70           C  
-ATOM  10932  CG  LEU C 462     -44.230   4.622-135.663  1.00 19.55           C  
-ATOM  10933  CD1 LEU C 462     -43.341   5.767-136.086  1.00 15.82           C  
-ATOM  10934  CD2 LEU C 462     -43.837   4.131-134.290  1.00 16.63           C  
-ATOM  10935  N   ARG C 463     -48.858   5.107-135.997  1.00 35.93           N  
-ATOM  10936  CA  ARG C 463     -50.114   5.698-135.559  1.00 27.85           C  
-ATOM  10937  C   ARG C 463     -51.205   4.653-135.346  1.00 25.71           C  
-ATOM  10938  O   ARG C 463     -52.089   4.834-134.510  1.00 23.40           O  
-ATOM  10939  CB  ARG C 463     -50.586   6.742-136.572  1.00 26.04           C  
-ATOM  10940  CG  ARG C 463     -49.578   7.854-136.819  1.00 30.35           C  
-ATOM  10941  CD  ARG C 463     -50.259   9.196-137.028  1.00 24.59           C  
-ATOM  10942  NE  ARG C 463     -50.380   9.554-138.438  1.00 18.14           N  
-ATOM  10943  CZ  ARG C 463     -49.930  10.693-138.953  1.00 19.35           C  
-ATOM  10944  NH1 ARG C 463     -49.332  11.580-138.171  1.00 18.50           N  
-ATOM  10945  NH2 ARG C 463     -50.083  10.952-140.243  1.00 20.33           N  
-ATOM  10946  N   THR C 464     -51.132   3.554-136.090  1.00 32.61           N  
-ATOM  10947  CA  THR C 464     -52.203   2.563-136.069  1.00 31.59           C  
-ATOM  10948  C   THR C 464     -51.844   1.269-135.334  1.00 31.17           C  
-ATOM  10949  O   THR C 464     -52.706   0.646-134.714  1.00 29.02           O  
-ATOM  10950  CB  THR C 464     -52.636   2.206-137.501  1.00 30.39           C  
-ATOM  10951  OG1 THR C 464     -51.644   1.373-138.114  1.00 36.13           O  
-ATOM  10952  CG2 THR C 464     -52.813   3.469-138.324  1.00 31.71           C  
-ATOM  10953  N   ASN C 465     -50.581   0.866-135.404  1.00 32.00           N  
-ATOM  10954  CA  ASN C 465     -50.174  -0.436-134.885  1.00 32.52           C  
-ATOM  10955  C   ASN C 465     -48.793  -0.400-134.233  1.00 37.79           C  
-ATOM  10956  O   ASN C 465     -47.843  -0.977-134.763  1.00 40.39           O  
-ATOM  10957  CB  ASN C 465     -50.188  -1.464-136.019  1.00 38.80           C  
-ATOM  10958  CG  ASN C 465     -50.276  -2.890-135.518  1.00 43.13           C  
-ATOM  10959  OD1 ASN C 465     -49.975  -3.175-134.359  1.00 37.21           O  
-ATOM  10960  ND2 ASN C 465     -50.693  -3.799-136.395  1.00 34.46           N  
-ATOM  10961  N   PRO C 466     -48.685   0.254-133.065  1.00 33.23           N  
-ATOM  10962  CA  PRO C 466     -47.388   0.560-132.442  1.00 25.35           C  
-ATOM  10963  C   PRO C 466     -46.600  -0.653-131.934  1.00 30.47           C  
-ATOM  10964  O   PRO C 466     -45.475  -0.478-131.466  1.00 41.15           O  
-ATOM  10965  CB  PRO C 466     -47.775   1.466-131.270  1.00 28.81           C  
-ATOM  10966  CG  PRO C 466     -49.165   1.060-130.928  1.00 41.54           C  
-ATOM  10967  CD  PRO C 466     -49.816   0.707-132.236  1.00 34.20           C  
-ATOM  10968  N   THR C 467     -47.165  -1.853-132.025  1.00 30.40           N  
-ATOM  10969  CA  THR C 467     -46.473  -3.051-131.558  1.00 26.94           C  
-ATOM  10970  C   THR C 467     -45.932  -3.862-132.729  1.00 26.36           C  
-ATOM  10971  O   THR C 467     -45.466  -4.990-132.559  1.00 29.46           O  
-ATOM  10972  CB  THR C 467     -47.393  -3.940-130.705  1.00 34.90           C  
-ATOM  10973  OG1 THR C 467     -48.619  -4.181-131.407  1.00 35.27           O  
-ATOM  10974  CG2 THR C 467     -47.700  -3.262-129.382  1.00 29.96           C  
-ATOM  10975  N   ASP C 468     -46.002  -3.280-133.920  1.00 25.24           N  
-ATOM  10976  CA  ASP C 468     -45.460  -3.915-135.110  1.00 28.64           C  
-ATOM  10977  C   ASP C 468     -43.939  -3.935-135.019  1.00 30.87           C  
-ATOM  10978  O   ASP C 468     -43.336  -3.022-134.454  1.00 33.68           O  
-ATOM  10979  CB  ASP C 468     -45.926  -3.179-136.367  1.00 28.82           C  
-ATOM  10980  CG  ASP C 468     -45.431  -3.827-137.642  1.00 32.44           C  
-ATOM  10981  OD1 ASP C 468     -46.077  -4.786-138.115  1.00 38.19           O  
-ATOM  10982  OD2 ASP C 468     -44.401  -3.371-138.179  1.00 31.18           O  
-ATOM  10983  N   ARG C 469     -43.317  -4.979-135.556  1.00 35.62           N  
-ATOM  10984  CA  ARG C 469     -41.862  -5.091-135.499  1.00 33.47           C  
-ATOM  10985  C   ARG C 469     -41.223  -4.973-136.880  1.00 26.65           C  
-ATOM  10986  O   ARG C 469     -40.121  -5.471-137.101  1.00 27.17           O  
-ATOM  10987  CB  ARG C 469     -41.443  -6.415-134.852  1.00 24.82           C  
-ATOM  10988  CG  ARG C 469     -42.097  -6.707-133.511  1.00 23.87           C  
-ATOM  10989  CD  ARG C 469     -41.389  -7.864-132.826  1.00 28.54           C  
-ATOM  10990  NE  ARG C 469     -42.291  -8.730-132.072  1.00 36.60           N  
-ATOM  10991  CZ  ARG C 469     -42.956  -9.751-132.603  1.00 37.02           C  
-ATOM  10992  NH1 ARG C 469     -42.827 -10.023-133.893  1.00 29.38           N  
-ATOM  10993  NH2 ARG C 469     -43.751 -10.498-131.851  1.00 38.28           N  
-ATOM  10994  N   ARG C 470     -41.915  -4.319-137.807  1.00 26.72           N  
-ATOM  10995  CA  ARG C 470     -41.383  -4.118-139.152  1.00 23.46           C  
-ATOM  10996  C   ARG C 470     -41.337  -2.635-139.505  1.00 24.81           C  
-ATOM  10997  O   ARG C 470     -41.412  -2.263-140.677  1.00 21.67           O  
-ATOM  10998  CB  ARG C 470     -42.214  -4.876-140.192  1.00 21.67           C  
-ATOM  10999  CG  ARG C 470     -42.177  -6.391-140.065  1.00 20.05           C  
-ATOM  11000  CD  ARG C 470     -43.241  -6.897-139.106  1.00 30.83           C  
-ATOM  11001  NE  ARG C 470     -43.494  -8.325-139.273  1.00 34.83           N  
-ATOM  11002  CZ  ARG C 470     -44.401  -8.828-140.104  1.00 35.96           C  
-ATOM  11003  NH1 ARG C 470     -45.145  -8.018-140.847  1.00 30.29           N  
-ATOM  11004  NH2 ARG C 470     -44.567 -10.140-140.193  1.00 30.62           N  
-ATOM  11005  N   MET C 471     -41.217  -1.795-138.483  1.00 25.60           N  
-ATOM  11006  CA  MET C 471     -41.126  -0.354-138.682  1.00 29.53           C  
-ATOM  11007  C   MET C 471     -39.697   0.062-139.003  1.00 28.30           C  
-ATOM  11008  O   MET C 471     -38.985   0.586-138.143  1.00 23.16           O  
-ATOM  11009  CB  MET C 471     -41.611   0.392-137.443  1.00 29.03           C  
-ATOM  11010  CG  MET C 471     -42.934  -0.097-136.900  1.00 25.78           C  
-ATOM  11011  SD  MET C 471     -43.395   0.831-135.430  1.00 31.14           S  
-ATOM  11012  CE  MET C 471     -44.783  -0.123-134.843  1.00 36.38           C  
-ATOM  11013  N   LEU C 472     -39.278  -0.168-140.241  1.00 22.70           N  
-ATOM  11014  CA  LEU C 472     -37.913   0.144-140.629  1.00 19.82           C  
-ATOM  11015  C   LEU C 472     -37.840   1.022-141.869  1.00 24.54           C  
-ATOM  11016  O   LEU C 472     -38.715   0.989-142.735  1.00 19.99           O  
-ATOM  11017  CB  LEU C 472     -37.117  -1.141-140.857  1.00 19.93           C  
-ATOM  11018  CG  LEU C 472     -36.759  -1.926-139.595  1.00 19.95           C  
-ATOM  11019  CD1 LEU C 472     -37.798  -2.998-139.288  1.00 27.08           C  
-ATOM  11020  CD2 LEU C 472     -35.372  -2.526-139.719  1.00 21.43           C  
-ATOM  11021  N   MET C 473     -36.776   1.811-141.933  1.00 24.91           N  
-ATOM  11022  CA  MET C 473     -36.498   2.658-143.076  1.00 23.94           C  
-ATOM  11023  C   MET C 473     -35.056   2.410-143.497  1.00 26.92           C  
-ATOM  11024  O   MET C 473     -34.129   2.641-142.719  1.00 27.23           O  
-ATOM  11025  CB  MET C 473     -36.737   4.128-142.726  1.00 14.60           C  
-ATOM  11026  CG  MET C 473     -36.809   5.056-143.923  1.00 23.02           C  
-ATOM  11027  SD  MET C 473     -37.511   6.662-143.490  1.00 46.19           S  
-ATOM  11028  CE  MET C 473     -36.342   7.227-142.253  1.00 24.45           C  
-ATOM  11029  N   THR C 474     -34.867   1.911-144.714  1.00 21.22           N  
-ATOM  11030  CA  THR C 474     -33.523   1.615-145.194  1.00 17.96           C  
-ATOM  11031  C   THR C 474     -33.198   2.400-146.459  1.00 22.29           C  
-ATOM  11032  O   THR C 474     -34.073   2.660-147.286  1.00 25.56           O  
-ATOM  11033  CB  THR C 474     -33.332   0.110-145.464  1.00 14.63           C  
-ATOM  11034  OG1 THR C 474     -31.988  -0.133-145.900  1.00 18.77           O  
-ATOM  11035  CG2 THR C 474     -34.304  -0.379-146.527  1.00 17.52           C  
-ATOM  11036  N   ALA C 475     -31.935   2.788-146.592  1.00 23.90           N  
-ATOM  11037  CA  ALA C 475     -31.477   3.511-147.770  1.00 20.44           C  
-ATOM  11038  C   ALA C 475     -30.411   2.705-148.491  1.00 21.55           C  
-ATOM  11039  O   ALA C 475     -29.857   3.146-149.495  1.00 29.44           O  
-ATOM  11040  CB  ALA C 475     -30.945   4.878-147.385  1.00 30.92           C  
-ATOM  11041  N   TRP C 476     -30.124   1.520-147.964  1.00 20.53           N  
-ATOM  11042  CA  TRP C 476     -29.153   0.632-148.583  1.00 24.16           C  
-ATOM  11043  C   TRP C 476     -29.834  -0.208-149.653  1.00 30.79           C  
-ATOM  11044  O   TRP C 476     -30.426  -1.247-149.362  1.00 38.19           O  
-ATOM  11045  CB  TRP C 476     -28.488  -0.262-147.536  1.00 23.83           C  
-ATOM  11046  CG  TRP C 476     -27.322  -1.036-148.069  1.00 22.05           C  
-ATOM  11047  CD1 TRP C 476     -27.305  -2.352-148.426  1.00 26.06           C  
-ATOM  11048  CD2 TRP C 476     -26.001  -0.539-148.310  1.00 23.41           C  
-ATOM  11049  NE1 TRP C 476     -26.055  -2.707-148.872  1.00 32.27           N  
-ATOM  11050  CE2 TRP C 476     -25.235  -1.609-148.811  1.00 33.40           C  
-ATOM  11051  CE3 TRP C 476     -25.390   0.708-148.150  1.00 24.73           C  
-ATOM  11052  CZ2 TRP C 476     -23.891  -1.472-149.153  1.00 33.19           C  
-ATOM  11053  CZ3 TRP C 476     -24.056   0.844-148.492  1.00 24.47           C  
-ATOM  11054  CH2 TRP C 476     -23.322  -0.240-148.987  1.00 27.44           C  
-ATOM  11055  N   ASN C 477     -29.751   0.261-150.893  1.00 29.75           N  
-ATOM  11056  CA  ASN C 477     -30.364  -0.418-152.024  1.00 28.49           C  
-ATOM  11057  C   ASN C 477     -29.301  -0.824-153.042  1.00 29.30           C  
-ATOM  11058  O   ASN C 477     -28.940  -0.034-153.914  1.00 30.31           O  
-ATOM  11059  CB  ASN C 477     -31.422   0.483-152.667  1.00 31.65           C  
-ATOM  11060  CG  ASN C 477     -32.051  -0.134-153.900  1.00 31.56           C  
-ATOM  11061  OD1 ASN C 477     -32.031  -1.350-154.081  1.00 31.47           O  
-ATOM  11062  ND2 ASN C 477     -32.618   0.710-154.757  1.00 27.23           N  
-ATOM  11063  N   PRO C 478     -28.799  -2.065-152.927  1.00 25.48           N  
-ATOM  11064  CA  PRO C 478     -27.702  -2.628-153.724  1.00 22.92           C  
-ATOM  11065  C   PRO C 478     -27.843  -2.427-155.234  1.00 25.86           C  
-ATOM  11066  O   PRO C 478     -26.840  -2.463-155.947  1.00 28.24           O  
-ATOM  11067  CB  PRO C 478     -27.757  -4.117-153.374  1.00 21.40           C  
-ATOM  11068  CG  PRO C 478     -28.282  -4.142-151.993  1.00 21.86           C  
-ATOM  11069  CD  PRO C 478     -29.289  -3.027-151.923  1.00 23.26           C  
-ATOM  11070  N   ALA C 479     -29.066  -2.212-155.708  1.00 27.21           N  
-ATOM  11071  CA  ALA C 479     -29.312  -2.032-157.133  1.00 27.04           C  
-ATOM  11072  C   ALA C 479     -28.920  -0.635-157.606  1.00 31.62           C  
-ATOM  11073  O   ALA C 479     -28.549  -0.444-158.765  1.00 32.78           O  
-ATOM  11074  CB  ALA C 479     -30.774  -2.300-157.448  1.00 30.63           C  
-ATOM  11075  N   ALA C 480     -28.997   0.336-156.703  1.00 32.87           N  
-ATOM  11076  CA  ALA C 480     -28.790   1.733-157.066  1.00 34.81           C  
-ATOM  11077  C   ALA C 480     -27.506   2.317-156.480  1.00 31.62           C  
-ATOM  11078  O   ALA C 480     -27.265   3.518-156.586  1.00 32.97           O  
-ATOM  11079  CB  ALA C 480     -29.991   2.564-156.627  1.00 28.78           C  
-ATOM  11080  N   LEU C 481     -26.684   1.467-155.873  1.00 28.91           N  
-ATOM  11081  CA  LEU C 481     -25.474   1.923-155.194  1.00 28.83           C  
-ATOM  11082  C   LEU C 481     -24.476   2.590-156.133  1.00 34.17           C  
-ATOM  11083  O   LEU C 481     -23.915   3.635-155.806  1.00 25.03           O  
-ATOM  11084  CB  LEU C 481     -24.796   0.756-154.478  1.00 25.21           C  
-ATOM  11085  CG  LEU C 481     -25.498   0.254-153.218  1.00 27.63           C  
-ATOM  11086  CD1 LEU C 481     -24.636  -0.777-152.510  1.00 29.88           C  
-ATOM  11087  CD2 LEU C 481     -25.830   1.412-152.293  1.00 27.99           C  
-ATOM  11088  N   ASP C 482     -24.256   1.986-157.296  1.00 43.11           N  
-ATOM  11089  CA  ASP C 482     -23.296   2.521-158.258  1.00 37.88           C  
-ATOM  11090  C   ASP C 482     -23.775   3.838-158.861  1.00 30.79           C  
-ATOM  11091  O   ASP C 482     -22.981   4.606-159.402  1.00 29.46           O  
-ATOM  11092  CB  ASP C 482     -23.023   1.503-159.369  1.00 35.27           C  
-ATOM  11093  CG  ASP C 482     -22.251   0.291-158.875  1.00 42.52           C  
-ATOM  11094  OD1 ASP C 482     -21.542   0.410-157.850  1.00 24.82           O  
-ATOM  11095  OD2 ASP C 482     -22.350  -0.778-159.516  1.00 31.43           O  
-ATOM  11096  N   GLU C 483     -25.075   4.096-158.760  1.00 31.60           N  
-ATOM  11097  CA  GLU C 483     -25.655   5.323-159.294  1.00 32.32           C  
-ATOM  11098  C   GLU C 483     -25.544   6.477-158.304  1.00 33.39           C  
-ATOM  11099  O   GLU C 483     -25.685   7.640-158.681  1.00 30.55           O  
-ATOM  11100  CB  GLU C 483     -27.119   5.105-159.666  1.00 35.63           C  
-ATOM  11101  CG  GLU C 483     -27.346   3.986-160.660  1.00 45.80           C  
-ATOM  11102  CD  GLU C 483     -28.818   3.746-160.928  1.00 55.68           C  
-ATOM  11103  OE1 GLU C 483     -29.531   4.721-161.253  1.00 47.43           O  
-ATOM  11104  OE2 GLU C 483     -29.263   2.585-160.804  1.00 52.85           O  
-ATOM  11105  N   MET C 484     -25.300   6.152-157.038  1.00 36.38           N  
-ATOM  11106  CA  MET C 484     -25.166   7.172-156.003  1.00 35.33           C  
-ATOM  11107  C   MET C 484     -23.770   7.781-156.005  1.00 34.73           C  
-ATOM  11108  O   MET C 484     -22.798   7.139-156.402  1.00 34.03           O  
-ATOM  11109  CB  MET C 484     -25.463   6.591-154.619  1.00 38.08           C  
-ATOM  11110  CG  MET C 484     -26.805   5.898-154.485  1.00 37.00           C  
-ATOM  11111  SD  MET C 484     -27.023   5.249-152.816  1.00 35.67           S  
-ATOM  11112  CE  MET C 484     -28.340   4.064-153.067  1.00 34.35           C  
-ATOM  11113  N   ALA C 485     -23.677   9.025-155.550  1.00 34.27           N  
-ATOM  11114  CA  ALA C 485     -22.391   9.692-155.427  1.00 35.82           C  
-ATOM  11115  C   ALA C 485     -21.585   9.050-154.309  1.00 37.77           C  
-ATOM  11116  O   ALA C 485     -20.363   8.935-154.394  1.00 46.92           O  
-ATOM  11117  CB  ALA C 485     -22.582  11.176-155.168  1.00 40.63           C  
-ATOM  11118  N   LEU C 486     -22.282   8.627-153.261  1.00 32.21           N  
-ATOM  11119  CA  LEU C 486     -21.639   7.978-152.128  1.00 39.92           C  
-ATOM  11120  C   LEU C 486     -22.635   7.066-151.417  1.00 38.53           C  
-ATOM  11121  O   LEU C 486     -23.707   7.512-151.005  1.00 31.62           O  
-ATOM  11122  CB  LEU C 486     -21.072   9.025-151.162  1.00 35.60           C  
-ATOM  11123  CG  LEU C 486     -19.871   8.641-150.290  1.00 44.85           C  
-ATOM  11124  CD1 LEU C 486     -19.085   9.882-149.902  1.00 58.34           C  
-ATOM  11125  CD2 LEU C 486     -20.299   7.881-149.043  1.00 49.60           C  
-ATOM  11126  N   PRO C 487     -22.283   5.778-151.280  1.00 33.33           N  
-ATOM  11127  CA  PRO C 487     -23.141   4.798-150.608  1.00 28.54           C  
-ATOM  11128  C   PRO C 487     -23.488   5.253-149.197  1.00 31.17           C  
-ATOM  11129  O   PRO C 487     -22.607   5.728-148.481  1.00 43.25           O  
-ATOM  11130  CB  PRO C 487     -22.281   3.531-150.587  1.00 37.45           C  
-ATOM  11131  CG  PRO C 487     -21.300   3.718-151.696  1.00 31.65           C  
-ATOM  11132  CD  PRO C 487     -21.013   5.184-151.730  1.00 34.18           C  
-ATOM  11133  N   PRO C 488     -24.763   5.124-148.806  1.00 31.06           N  
-ATOM  11134  CA  PRO C 488     -25.248   5.632-147.518  1.00 37.75           C  
-ATOM  11135  C   PRO C 488     -24.513   5.037-146.321  1.00 32.51           C  
-ATOM  11136  O   PRO C 488     -24.299   3.827-146.253  1.00 28.47           O  
-ATOM  11137  CB  PRO C 488     -26.726   5.220-147.512  1.00 32.78           C  
-ATOM  11138  CG  PRO C 488     -26.828   4.117-148.505  1.00 24.64           C  
-ATOM  11139  CD  PRO C 488     -25.828   4.449-149.564  1.00 29.29           C  
-ATOM  11140  N   CYS C 489     -24.121   5.898-145.390  1.00 28.37           N  
-ATOM  11141  CA  CYS C 489     -23.446   5.450-144.184  1.00 30.70           C  
-ATOM  11142  C   CYS C 489     -24.491   5.139-143.114  1.00 33.77           C  
-ATOM  11143  O   CYS C 489     -24.580   4.006-142.641  1.00 32.24           O  
-ATOM  11144  CB  CYS C 489     -22.440   6.499-143.704  1.00 38.59           C  
-ATOM  11145  SG  CYS C 489     -21.057   6.794-144.846  1.00 71.61           S  
-ATOM  11146  N   HIS C 490     -25.287   6.136-142.738  1.00 36.38           N  
-ATOM  11147  CA  HIS C 490     -26.459   5.875-141.909  1.00 28.68           C  
-ATOM  11148  C   HIS C 490     -27.542   5.290-142.806  1.00 29.36           C  
-ATOM  11149  O   HIS C 490     -28.305   6.022-143.432  1.00 40.19           O  
-ATOM  11150  CB  HIS C 490     -26.944   7.144-141.195  1.00 35.11           C  
-ATOM  11151  CG  HIS C 490     -27.053   8.348-142.079  1.00 37.22           C  
-ATOM  11152  ND1 HIS C 490     -28.264   8.890-142.453  1.00 38.51           N  
-ATOM  11153  CD2 HIS C 490     -26.102   9.129-142.645  1.00 43.29           C  
-ATOM  11154  CE1 HIS C 490     -28.055   9.948-143.217  1.00 35.53           C  
-ATOM  11155  NE2 HIS C 490     -26.751  10.113-143.351  1.00 44.75           N  
-ATOM  11156  N   LEU C 491     -27.600   3.963-142.867  1.00 27.05           N  
-ATOM  11157  CA  LEU C 491     -28.344   3.283-143.924  1.00 29.85           C  
-ATOM  11158  C   LEU C 491     -29.689   2.698-143.500  1.00 29.39           C  
-ATOM  11159  O   LEU C 491     -30.541   2.431-144.346  1.00 30.31           O  
-ATOM  11160  CB  LEU C 491     -27.478   2.168-144.517  1.00 26.64           C  
-ATOM  11161  CG  LEU C 491     -26.867   1.187-143.514  1.00 23.58           C  
-ATOM  11162  CD1 LEU C 491     -27.756  -0.023-143.291  1.00 26.07           C  
-ATOM  11163  CD2 LEU C 491     -25.492   0.750-143.971  1.00 23.38           C  
-ATOM  11164  N   LEU C 492     -29.875   2.488-142.203  1.00 24.46           N  
-ATOM  11165  CA  LEU C 492     -31.075   1.818-141.713  1.00 20.75           C  
-ATOM  11166  C   LEU C 492     -31.493   2.307-140.330  1.00 24.81           C  
-ATOM  11167  O   LEU C 492     -30.658   2.474-139.445  1.00 18.23           O  
-ATOM  11168  CB  LEU C 492     -30.848   0.307-141.685  1.00 15.90           C  
-ATOM  11169  CG  LEU C 492     -31.893  -0.584-141.014  1.00 18.78           C  
-ATOM  11170  CD1 LEU C 492     -32.231  -1.748-141.922  1.00 20.87           C  
-ATOM  11171  CD2 LEU C 492     -31.386  -1.090-139.671  1.00 18.41           C  
-ATOM  11172  N   CYS C 493     -32.788   2.536-140.143  1.00 22.82           N  
-ATOM  11173  CA  CYS C 493     -33.287   2.892-138.822  1.00 22.13           C  
-ATOM  11174  C   CYS C 493     -34.595   2.175-138.509  1.00 25.14           C  
-ATOM  11175  O   CYS C 493     -35.410   1.933-139.395  1.00 27.10           O  
-ATOM  11176  CB  CYS C 493     -33.463   4.410-138.691  1.00 22.09           C  
-ATOM  11177  SG  CYS C 493     -34.756   5.143-139.711  1.00 32.62           S  
-ATOM  11178  N   GLN C 494     -34.774   1.827-137.239  1.00 28.30           N  
-ATOM  11179  CA  GLN C 494     -35.957   1.107-136.786  1.00 27.41           C  
-ATOM  11180  C   GLN C 494     -36.552   1.771-135.545  1.00 26.75           C  
-ATOM  11181  O   GLN C 494     -35.821   2.225-134.663  1.00 19.49           O  
-ATOM  11182  CB  GLN C 494     -35.611  -0.356-136.498  1.00 17.95           C  
-ATOM  11183  CG  GLN C 494     -36.774  -1.185-135.992  1.00 22.36           C  
-ATOM  11184  CD  GLN C 494     -36.361  -2.592-135.616  1.00 22.47           C  
-ATOM  11185  OE1 GLN C 494     -35.224  -2.997-135.847  1.00 24.57           O  
-ATOM  11186  NE2 GLN C 494     -37.286  -3.344-135.032  1.00 16.92           N  
-ATOM  11187  N   PHE C 495     -37.880   1.828-135.484  1.00 26.65           N  
-ATOM  11188  CA  PHE C 495     -38.570   2.492-134.382  1.00 23.84           C  
-ATOM  11189  C   PHE C 495     -39.244   1.499-133.440  1.00 25.33           C  
-ATOM  11190  O   PHE C 495     -39.402   0.322-133.768  1.00 22.20           O  
-ATOM  11191  CB  PHE C 495     -39.597   3.488-134.924  1.00 18.71           C  
-ATOM  11192  CG  PHE C 495     -38.983   4.641-135.664  1.00 21.77           C  
-ATOM  11193  CD1 PHE C 495     -38.526   5.757-134.980  1.00 20.70           C  
-ATOM  11194  CD2 PHE C 495     -38.849   4.606-137.042  1.00 17.45           C  
-ATOM  11195  CE1 PHE C 495     -37.954   6.819-135.657  1.00 16.68           C  
-ATOM  11196  CE2 PHE C 495     -38.279   5.664-137.725  1.00 16.24           C  
-ATOM  11197  CZ  PHE C 495     -37.831   6.772-137.032  1.00 17.93           C  
-ATOM  11198  N   TYR C 496     -39.643   1.989-132.269  1.00 25.78           N  
-ATOM  11199  CA  TYR C 496     -40.176   1.131-131.218  1.00 20.98           C  
-ATOM  11200  C   TYR C 496     -41.042   1.920-130.242  1.00 23.54           C  
-ATOM  11201  O   TYR C 496     -40.657   2.994-129.791  1.00 25.11           O  
-ATOM  11202  CB  TYR C 496     -39.020   0.449-130.487  1.00 16.09           C  
-ATOM  11203  CG  TYR C 496     -39.383  -0.337-129.244  1.00 25.09           C  
-ATOM  11204  CD1 TYR C 496     -39.400   0.271-127.993  1.00 26.03           C  
-ATOM  11205  CD2 TYR C 496     -39.669  -1.695-129.316  1.00 26.23           C  
-ATOM  11206  CE1 TYR C 496     -39.714  -0.443-126.854  1.00 23.37           C  
-ATOM  11207  CE2 TYR C 496     -39.984  -2.419-128.179  1.00 30.61           C  
-ATOM  11208  CZ  TYR C 496     -40.004  -1.786-126.952  1.00 30.15           C  
-ATOM  11209  OH  TYR C 496     -40.314  -2.495-125.815  1.00 36.09           O  
-ATOM  11210  N   VAL C 497     -42.215   1.385-129.921  1.00 27.43           N  
-ATOM  11211  CA  VAL C 497     -43.113   2.021-128.961  1.00 22.99           C  
-ATOM  11212  C   VAL C 497     -43.446   1.042-127.837  1.00 33.26           C  
-ATOM  11213  O   VAL C 497     -43.582  -0.160-128.073  1.00 35.22           O  
-ATOM  11214  CB  VAL C 497     -44.409   2.514-129.640  1.00 22.36           C  
-ATOM  11215  CG1 VAL C 497     -45.327   3.191-128.635  1.00 32.22           C  
-ATOM  11216  CG2 VAL C 497     -44.075   3.471-130.762  1.00 21.85           C  
-ATOM  11217  N   ASN C 498     -43.570   1.555-126.616  1.00 28.71           N  
-ATOM  11218  CA  ASN C 498     -43.767   0.704-125.448  1.00 34.93           C  
-ATOM  11219  C   ASN C 498     -45.061   0.976-124.685  1.00 36.54           C  
-ATOM  11220  O   ASN C 498     -46.021   1.518-125.232  1.00 30.02           O  
-ATOM  11221  CB  ASN C 498     -42.579   0.852-124.495  1.00 34.12           C  
-ATOM  11222  CG  ASN C 498     -42.491   2.239-123.884  1.00 25.09           C  
-ATOM  11223  OD1 ASN C 498     -43.094   3.188-124.381  1.00 21.83           O  
-ATOM  11224  ND2 ASN C 498     -41.734   2.361-122.802  1.00 28.79           N  
-ATOM  11225  N   ASP C 499     -45.062   0.586-123.412  1.00 38.17           N  
-ATOM  11226  CA  ASP C 499     -46.195   0.782-122.514  1.00 33.89           C  
-ATOM  11227  C   ASP C 499     -46.727   2.208-122.520  1.00 40.59           C  
-ATOM  11228  O   ASP C 499     -47.917   2.439-122.729  1.00 39.73           O  
-ATOM  11229  CB  ASP C 499     -45.802   0.410-121.081  1.00 32.73           C  
-ATOM  11230  CG  ASP C 499     -45.977  -1.062-120.792  1.00 56.51           C  
-ATOM  11231  OD1 ASP C 499     -46.657  -1.744-121.589  1.00 69.08           O  
-ATOM  11232  OD2 ASP C 499     -45.447  -1.535-119.762  1.00 60.75           O  
-ATOM  11233  N   GLN C 500     -45.828   3.160-122.302  1.00 35.88           N  
-ATOM  11234  CA  GLN C 500     -46.214   4.530-121.994  1.00 29.43           C  
-ATOM  11235  C   GLN C 500     -46.200   5.460-123.206  1.00 28.20           C  
-ATOM  11236  O   GLN C 500     -45.974   6.664-123.062  1.00 24.66           O  
-ATOM  11237  CB  GLN C 500     -45.285   5.083-120.915  1.00 32.92           C  
-ATOM  11238  CG  GLN C 500     -44.820   4.042-119.904  1.00 31.83           C  
-ATOM  11239  CD  GLN C 500     -45.761   3.904-118.723  1.00 42.48           C  
-ATOM  11240  OE1 GLN C 500     -45.411   4.255-117.596  1.00 48.80           O  
-ATOM  11241  NE2 GLN C 500     -46.960   3.386-118.973  1.00 40.67           N  
-ATOM  11242  N   LYS C 501     -46.453   4.903-124.388  1.00 24.62           N  
-ATOM  11243  CA  LYS C 501     -46.459   5.679-125.627  1.00 22.87           C  
-ATOM  11244  C   LYS C 501     -45.147   6.437-125.822  1.00 24.46           C  
-ATOM  11245  O   LYS C 501     -45.147   7.621-126.159  1.00 23.29           O  
-ATOM  11246  CB  LYS C 501     -47.641   6.655-125.645  1.00 24.39           C  
-ATOM  11247  CG  LYS C 501     -48.999   5.994-125.840  1.00 33.84           C  
-ATOM  11248  CD  LYS C 501     -50.136   6.919-125.419  1.00 37.94           C  
-ATOM  11249  CE  LYS C 501     -50.207   8.173-126.281  1.00 41.79           C  
-ATOM  11250  NZ  LYS C 501     -50.665   7.877-127.668  1.00 37.06           N  
-ATOM  11251  N   GLU C 502     -44.032   5.746-125.605  1.00 29.31           N  
-ATOM  11252  CA  GLU C 502     -42.713   6.354-125.733  1.00 20.33           C  
-ATOM  11253  C   GLU C 502     -41.951   5.785-126.926  1.00 21.23           C  
-ATOM  11254  O   GLU C 502     -41.804   4.570-127.059  1.00 24.37           O  
-ATOM  11255  CB  GLU C 502     -41.904   6.153-124.453  1.00 15.90           C  
-ATOM  11256  CG  GLU C 502     -42.675   6.463-123.187  1.00 23.54           C  
-ATOM  11257  CD  GLU C 502     -41.801   6.419-121.951  1.00 36.57           C  
-ATOM  11258  OE1 GLU C 502     -41.351   7.497-121.506  1.00 54.35           O  
-ATOM  11259  OE2 GLU C 502     -41.565   5.311-121.425  1.00 26.84           O  
-ATOM  11260  N   LEU C 503     -41.464   6.668-127.790  1.00 23.35           N  
-ATOM  11261  CA  LEU C 503     -40.775   6.243-129.001  1.00 22.52           C  
-ATOM  11262  C   LEU C 503     -39.265   6.135-128.803  1.00 29.50           C  
-ATOM  11263  O   LEU C 503     -38.635   7.019-128.220  1.00 33.86           O  
-ATOM  11264  CB  LEU C 503     -41.077   7.205-130.150  1.00 20.32           C  
-ATOM  11265  CG  LEU C 503     -40.430   6.879-131.496  1.00 17.88           C  
-ATOM  11266  CD1 LEU C 503     -41.070   5.646-132.125  1.00 22.17           C  
-ATOM  11267  CD2 LEU C 503     -40.507   8.075-132.433  1.00 14.02           C  
-ATOM  11268  N   SER C 504     -38.700   5.035-129.289  1.00 24.80           N  
-ATOM  11269  CA  SER C 504     -37.260   4.830-129.303  1.00 21.82           C  
-ATOM  11270  C   SER C 504     -36.809   4.488-130.720  1.00 24.78           C  
-ATOM  11271  O   SER C 504     -37.573   3.913-131.499  1.00 29.61           O  
-ATOM  11272  CB  SER C 504     -36.853   3.727-128.321  1.00 27.23           C  
-ATOM  11273  OG  SER C 504     -37.032   4.142-126.975  1.00 35.67           O  
-ATOM  11274  N   CYS C 505     -35.572   4.844-131.049  1.00 22.83           N  
-ATOM  11275  CA  CYS C 505     -35.069   4.678-132.406  1.00 17.02           C  
-ATOM  11276  C   CYS C 505     -33.645   4.123-132.444  1.00 18.44           C  
-ATOM  11277  O   CYS C 505     -32.758   4.611-131.748  1.00 16.47           O  
-ATOM  11278  CB  CYS C 505     -35.129   6.017-133.146  1.00 16.33           C  
-ATOM  11279  SG  CYS C 505     -34.335   6.026-134.768  1.00 23.60           S  
-ATOM  11280  N   ILE C 506     -33.438   3.093-133.259  1.00 22.15           N  
-ATOM  11281  CA  ILE C 506     -32.104   2.561-133.514  1.00 17.86           C  
-ATOM  11282  C   ILE C 506     -31.666   2.945-134.917  1.00 19.42           C  
-ATOM  11283  O   ILE C 506     -32.437   2.814-135.859  1.00 21.85           O  
-ATOM  11284  CB  ILE C 506     -32.047   1.024-133.385  1.00 18.78           C  
-ATOM  11285  CG1 ILE C 506     -32.309   0.585-131.947  1.00 23.58           C  
-ATOM  11286  CG2 ILE C 506     -30.692   0.496-133.845  1.00 15.57           C  
-ATOM  11287  CD1 ILE C 506     -32.398  -0.914-131.794  1.00 24.39           C  
-ATOM  11288  N   MET C 507     -30.435   3.422-135.058  1.00 17.93           N  
-ATOM  11289  CA  MET C 507     -29.873   3.655-136.380  1.00 16.39           C  
-ATOM  11290  C   MET C 507     -28.567   2.889-136.536  1.00 18.54           C  
-ATOM  11291  O   MET C 507     -27.675   2.990-135.696  1.00 18.99           O  
-ATOM  11292  CB  MET C 507     -29.653   5.147-136.629  1.00 18.79           C  
-ATOM  11293  CG  MET C 507     -29.180   5.467-138.042  1.00 21.41           C  
-ATOM  11294  SD  MET C 507     -27.385   5.465-138.231  1.00 19.83           S  
-ATOM  11295  CE  MET C 507     -26.957   6.987-137.395  1.00 20.22           C  
-ATOM  11296  N   TYR C 508     -28.466   2.115-137.610  1.00 20.43           N  
-ATOM  11297  CA  TYR C 508     -27.250   1.369-137.898  1.00 19.67           C  
-ATOM  11298  C   TYR C 508     -26.402   2.104-138.932  1.00 22.47           C  
-ATOM  11299  O   TYR C 508     -26.885   2.480-140.001  1.00 26.18           O  
-ATOM  11300  CB  TYR C 508     -27.577  -0.047-138.384  1.00 17.66           C  
-ATOM  11301  CG  TYR C 508     -26.344  -0.888-138.622  1.00 19.82           C  
-ATOM  11302  CD1 TYR C 508     -25.705  -1.530-137.568  1.00 19.97           C  
-ATOM  11303  CD2 TYR C 508     -25.809  -1.027-139.896  1.00 20.38           C  
-ATOM  11304  CE1 TYR C 508     -24.571  -2.291-137.781  1.00 21.86           C  
-ATOM  11305  CE2 TYR C 508     -24.676  -1.785-140.116  1.00 18.88           C  
-ATOM  11306  CZ  TYR C 508     -24.062  -2.416-139.056  1.00 19.88           C  
-ATOM  11307  OH  TYR C 508     -22.935  -3.175-139.271  1.00 24.07           O  
-ATOM  11308  N   GLN C 509     -25.132   2.304-138.602  1.00 18.31           N  
-ATOM  11309  CA  GLN C 509     -24.224   3.044-139.465  1.00 22.56           C  
-ATOM  11310  C   GLN C 509     -23.032   2.172-139.848  1.00 26.83           C  
-ATOM  11311  O   GLN C 509     -22.264   1.748-138.985  1.00 26.58           O  
-ATOM  11312  CB  GLN C 509     -23.760   4.319-138.764  1.00 23.32           C  
-ATOM  11313  CG  GLN C 509     -23.093   5.333-139.668  1.00 28.37           C  
-ATOM  11314  CD  GLN C 509     -22.731   6.602-138.924  1.00 34.59           C  
-ATOM  11315  OE1 GLN C 509     -23.377   6.959-137.939  1.00 29.90           O  
-ATOM  11316  NE2 GLN C 509     -21.690   7.285-139.383  1.00 43.12           N  
-ATOM  11317  N   ARG C 510     -22.889   1.898-141.142  1.00 29.33           N  
-ATOM  11318  CA  ARG C 510     -21.843   0.998-141.622  1.00 26.18           C  
-ATOM  11319  C   ARG C 510     -20.452   1.584-141.434  1.00 23.36           C  
-ATOM  11320  O   ARG C 510     -19.501   0.860-141.136  1.00 22.73           O  
-ATOM  11321  CB  ARG C 510     -22.059   0.656-143.099  1.00 23.80           C  
-ATOM  11322  CG  ARG C 510     -22.067   1.859-144.024  1.00 26.10           C  
-ATOM  11323  CD  ARG C 510     -21.871   1.447-145.472  1.00 29.87           C  
-ATOM  11324  NE  ARG C 510     -21.753   2.604-146.354  1.00 29.31           N  
-ATOM  11325  CZ  ARG C 510     -20.632   3.295-146.533  1.00 24.64           C  
-ATOM  11326  NH1 ARG C 510     -19.529   2.950-145.885  1.00 27.32           N  
-ATOM  11327  NH2 ARG C 510     -20.614   4.333-147.356  1.00 26.95           N  
-ATOM  11328  N   SER C 511     -20.339   2.895-141.614  1.00 24.33           N  
-ATOM  11329  CA  SER C 511     -19.060   3.581-141.510  1.00 33.78           C  
-ATOM  11330  C   SER C 511     -19.223   4.859-140.706  1.00 36.53           C  
-ATOM  11331  O   SER C 511     -20.133   5.646-140.965  1.00 45.24           O  
-ATOM  11332  CB  SER C 511     -18.501   3.891-142.897  1.00 35.20           C  
-ATOM  11333  OG  SER C 511     -17.204   4.453-142.807  1.00 38.38           O  
-ATOM  11334  N   CYS C 512     -18.342   5.069-139.734  1.00 28.85           N  
-ATOM  11335  CA  CYS C 512     -18.515   6.174-138.802  1.00 29.24           C  
-ATOM  11336  C   CYS C 512     -17.256   7.010-138.601  1.00 29.21           C  
-ATOM  11337  O   CYS C 512     -16.359   6.623-137.852  1.00 29.46           O  
-ATOM  11338  CB  CYS C 512     -18.987   5.642-137.448  1.00 32.13           C  
-ATOM  11339  SG  CYS C 512     -20.368   4.476-137.538  1.00 39.00           S  
-ATOM  11340  N   ASP C 513     -17.197   8.158-139.268  1.00 35.38           N  
-ATOM  11341  CA  ASP C 513     -16.176   9.154-138.970  1.00 29.81           C  
-ATOM  11342  C   ASP C 513     -16.456   9.700-137.576  1.00 24.81           C  
-ATOM  11343  O   ASP C 513     -17.339  10.537-137.389  1.00 24.88           O  
-ATOM  11344  CB  ASP C 513     -16.176  10.275-140.011  1.00 42.44           C  
-ATOM  11345  CG  ASP C 513     -14.969  11.192-139.889  1.00 47.85           C  
-ATOM  11346  OD1 ASP C 513     -14.296  11.173-138.834  1.00 42.55           O  
-ATOM  11347  OD2 ASP C 513     -14.696  11.940-140.853  1.00 51.22           O  
-ATOM  11348  N   VAL C 514     -15.696   9.218-136.601  1.00 22.28           N  
-ATOM  11349  CA  VAL C 514     -15.983   9.492-135.198  1.00 20.68           C  
-ATOM  11350  C   VAL C 514     -15.792  10.951-134.808  1.00 23.87           C  
-ATOM  11351  O   VAL C 514     -16.666  11.548-134.179  1.00 28.90           O  
-ATOM  11352  CB  VAL C 514     -15.119   8.614-134.289  1.00 14.88           C  
-ATOM  11353  CG1 VAL C 514     -15.155   9.123-132.862  1.00 23.02           C  
-ATOM  11354  CG2 VAL C 514     -15.611   7.189-134.354  1.00 22.44           C  
-ATOM  11355  N   GLY C 515     -14.658  11.527-135.185  1.00 27.27           N  
-ATOM  11356  CA  GLY C 515     -14.352  12.896-134.817  1.00 31.38           C  
-ATOM  11357  C   GLY C 515     -15.245  13.924-135.482  1.00 35.79           C  
-ATOM  11358  O   GLY C 515     -15.530  14.974-134.905  1.00 45.97           O  
-ATOM  11359  N   LEU C 516     -15.705  13.616-136.690  1.00 30.41           N  
-ATOM  11360  CA  LEU C 516     -16.391  14.604-137.514  1.00 36.74           C  
-ATOM  11361  C   LEU C 516     -17.878  14.314-137.723  1.00 32.71           C  
-ATOM  11362  O   LEU C 516     -18.720  15.188-137.515  1.00 36.30           O  
-ATOM  11363  CB  LEU C 516     -15.687  14.709-138.868  1.00 42.29           C  
-ATOM  11364  CG  LEU C 516     -16.104  15.829-139.814  1.00 50.14           C  
-ATOM  11365  CD1 LEU C 516     -16.240  17.148-139.068  1.00 57.18           C  
-ATOM  11366  CD2 LEU C 516     -15.077  15.945-140.928  1.00 60.64           C  
-ATOM  11367  N   GLY C 517     -18.202  13.091-138.129  1.00 26.24           N  
-ATOM  11368  CA  GLY C 517     -19.558  12.767-138.536  1.00 30.72           C  
-ATOM  11369  C   GLY C 517     -20.500  12.291-137.442  1.00 29.70           C  
-ATOM  11370  O   GLY C 517     -21.677  12.662-137.425  1.00 27.61           O  
-ATOM  11371  N   VAL C 518     -19.985  11.462-136.538  1.00 24.03           N  
-ATOM  11372  CA  VAL C 518     -20.801  10.822-135.507  1.00 23.35           C  
-ATOM  11373  C   VAL C 518     -21.684  11.781-134.695  1.00 20.79           C  
-ATOM  11374  O   VAL C 518     -22.877  11.521-134.558  1.00 21.03           O  
-ATOM  11375  CB  VAL C 518     -19.914   9.999-134.535  1.00 18.15           C  
-ATOM  11376  CG1 VAL C 518     -20.672   9.665-133.256  1.00 11.95           C  
-ATOM  11377  CG2 VAL C 518     -19.445   8.738-135.219  1.00 22.95           C  
-ATOM  11378  N   PRO C 519     -21.121  12.890-134.167  1.00 18.09           N  
-ATOM  11379  CA  PRO C 519     -22.004  13.770-133.388  1.00 20.08           C  
-ATOM  11380  C   PRO C 519     -23.164  14.312-134.222  1.00 19.58           C  
-ATOM  11381  O   PRO C 519     -24.310  14.379-133.762  1.00 19.21           O  
-ATOM  11382  CB  PRO C 519     -21.071  14.910-132.955  1.00 22.71           C  
-ATOM  11383  CG  PRO C 519     -19.704  14.344-133.055  1.00 16.07           C  
-ATOM  11384  CD  PRO C 519     -19.747  13.420-134.218  1.00 13.85           C  
-ATOM  11385  N   PHE C 520     -22.834  14.685-135.453  1.00 15.64           N  
-ATOM  11386  CA  PHE C 520     -23.793  15.159-136.434  1.00 13.33           C  
-ATOM  11387  C   PHE C 520     -24.895  14.134-136.674  1.00 20.88           C  
-ATOM  11388  O   PHE C 520     -26.071  14.487-136.733  1.00 30.08           O  
-ATOM  11389  CB  PHE C 520     -23.071  15.476-137.740  1.00 22.57           C  
-ATOM  11390  CG  PHE C 520     -23.875  16.295-138.706  1.00 30.77           C  
-ATOM  11391  CD1 PHE C 520     -24.542  15.692-139.759  1.00 30.50           C  
-ATOM  11392  CD2 PHE C 520     -23.940  17.673-138.580  1.00 30.98           C  
-ATOM  11393  CE1 PHE C 520     -25.267  16.444-140.659  1.00 31.33           C  
-ATOM  11394  CE2 PHE C 520     -24.659  18.429-139.478  1.00 36.75           C  
-ATOM  11395  CZ  PHE C 520     -25.322  17.814-140.521  1.00 40.46           C  
-ATOM  11396  N   ASN C 521     -24.513  12.868-136.815  1.00 23.47           N  
-ATOM  11397  CA  ASN C 521     -25.491  11.802-137.011  1.00 25.07           C  
-ATOM  11398  C   ASN C 521     -26.394  11.618-135.793  1.00 22.29           C  
-ATOM  11399  O   ASN C 521     -27.617  11.506-135.927  1.00 18.60           O  
-ATOM  11400  CB  ASN C 521     -24.786  10.489-137.337  1.00 24.96           C  
-ATOM  11401  CG  ASN C 521     -24.028  10.550-138.640  1.00 28.87           C  
-ATOM  11402  OD1 ASN C 521     -22.815  10.354-138.673  1.00 31.86           O  
-ATOM  11403  ND2 ASN C 521     -24.739  10.834-139.725  1.00 31.19           N  
-ATOM  11404  N   ILE C 522     -25.777  11.579-134.614  1.00 18.13           N  
-ATOM  11405  CA  ILE C 522     -26.501  11.528-133.351  1.00 15.14           C  
-ATOM  11406  C   ILE C 522     -27.587  12.594-133.311  1.00 15.84           C  
-ATOM  11407  O   ILE C 522     -28.775  12.286-133.157  1.00 16.82           O  
-ATOM  11408  CB  ILE C 522     -25.547  11.719-132.155  1.00 12.44           C  
-ATOM  11409  CG1 ILE C 522     -24.530  10.578-132.100  1.00 14.98           C  
-ATOM  11410  CG2 ILE C 522     -26.328  11.785-130.866  1.00 16.73           C  
-ATOM  11411  CD1 ILE C 522     -23.503  10.737-131.008  1.00 21.16           C  
-ATOM  11412  N   ALA C 523     -27.165  13.844-133.475  1.00 16.22           N  
-ATOM  11413  CA  ALA C 523     -28.088  14.972-133.506  1.00 17.89           C  
-ATOM  11414  C   ALA C 523     -29.179  14.762-134.549  1.00 16.71           C  
-ATOM  11415  O   ALA C 523     -30.362  15.012-134.288  1.00 12.74           O  
-ATOM  11416  CB  ALA C 523     -27.338  16.265-133.786  1.00 16.93           C  
-ATOM  11417  N   SER C 524     -28.774  14.289-135.723  1.00 15.37           N  
-ATOM  11418  CA  SER C 524     -29.685  14.119-136.844  1.00 15.02           C  
-ATOM  11419  C   SER C 524     -30.825  13.160-136.536  1.00 14.01           C  
-ATOM  11420  O   SER C 524     -31.996  13.523-136.638  1.00 21.16           O  
-ATOM  11421  CB  SER C 524     -28.915  13.639-138.077  1.00 12.84           C  
-ATOM  11422  OG  SER C 524     -29.758  13.634-139.211  1.00 19.34           O  
-ATOM  11423  N   TYR C 525     -30.485  11.933-136.166  1.00 12.44           N  
-ATOM  11424  CA  TYR C 525     -31.515  10.926-135.942  1.00 12.03           C  
-ATOM  11425  C   TYR C 525     -32.253  11.139-134.626  1.00 13.38           C  
-ATOM  11426  O   TYR C 525     -33.389  10.690-134.472  1.00 13.95           O  
-ATOM  11427  CB  TYR C 525     -30.916   9.520-136.016  1.00 11.36           C  
-ATOM  11428  CG  TYR C 525     -30.791   9.058-137.452  1.00 14.52           C  
-ATOM  11429  CD1 TYR C 525     -29.686   9.401-138.216  1.00 15.58           C  
-ATOM  11430  CD2 TYR C 525     -31.796   8.316-138.053  1.00 13.93           C  
-ATOM  11431  CE1 TYR C 525     -29.576   9.004-139.530  1.00 17.55           C  
-ATOM  11432  CE2 TYR C 525     -31.697   7.911-139.366  1.00 20.73           C  
-ATOM  11433  CZ  TYR C 525     -30.586   8.258-140.103  1.00 20.75           C  
-ATOM  11434  OH  TYR C 525     -30.487   7.852-141.415  1.00 22.88           O  
-ATOM  11435  N   SER C 526     -31.629  11.841-133.684  1.00 16.64           N  
-ATOM  11436  CA  SER C 526     -32.349  12.240-132.478  1.00 13.17           C  
-ATOM  11437  C   SER C 526     -33.444  13.241-132.851  1.00 13.19           C  
-ATOM  11438  O   SER C 526     -34.583  13.150-132.372  1.00 16.48           O  
-ATOM  11439  CB  SER C 526     -31.397  12.838-131.443  1.00 15.14           C  
-ATOM  11440  OG  SER C 526     -30.358  11.930-131.123  1.00 20.97           O  
-ATOM  11441  N   LEU C 527     -33.091  14.187-133.720  1.00 14.51           N  
-ATOM  11442  CA  LEU C 527     -34.051  15.153-134.250  1.00 11.14           C  
-ATOM  11443  C   LEU C 527     -35.177  14.450-134.998  1.00 15.49           C  
-ATOM  11444  O   LEU C 527     -36.354  14.766-134.798  1.00 16.78           O  
-ATOM  11445  CB  LEU C 527     -33.361  16.156-135.179  1.00 10.68           C  
-ATOM  11446  CG  LEU C 527     -34.251  17.292-135.692  1.00 10.37           C  
-ATOM  11447  CD1 LEU C 527     -34.768  18.129-134.535  1.00 12.79           C  
-ATOM  11448  CD2 LEU C 527     -33.507  18.164-136.688  1.00 19.27           C  
-ATOM  11449  N   LEU C 528     -34.809  13.500-135.859  1.00 16.55           N  
-ATOM  11450  CA  LEU C 528     -35.794  12.699-136.587  1.00 15.81           C  
-ATOM  11451  C   LEU C 528     -36.747  12.035-135.606  1.00 15.57           C  
-ATOM  11452  O   LEU C 528     -37.959  12.032-135.814  1.00 15.37           O  
-ATOM  11453  CB  LEU C 528     -35.122  11.633-137.461  1.00 15.05           C  
-ATOM  11454  CG  LEU C 528     -36.076  10.722-138.247  1.00  8.09           C  
-ATOM  11455  CD1 LEU C 528     -36.841  11.524-139.283  1.00  7.81           C  
-ATOM  11456  CD2 LEU C 528     -35.341   9.561-138.903  1.00  5.76           C  
-ATOM  11457  N   THR C 529     -36.189  11.483-134.531  1.00 13.74           N  
-ATOM  11458  CA  THR C 529     -36.995  10.845-133.497  1.00 14.48           C  
-ATOM  11459  C   THR C 529     -37.974  11.832-132.870  1.00 16.62           C  
-ATOM  11460  O   THR C 529     -39.142  11.504-132.677  1.00 20.39           O  
-ATOM  11461  CB  THR C 529     -36.128  10.235-132.380  1.00 11.52           C  
-ATOM  11462  OG1 THR C 529     -35.144   9.357-132.944  1.00  8.89           O  
-ATOM  11463  CG2 THR C 529     -37.003   9.455-131.412  1.00 14.40           C  
-ATOM  11464  N   LEU C 530     -37.496  13.034-132.552  1.00 16.15           N  
-ATOM  11465  CA  LEU C 530     -38.372  14.080-132.026  1.00 17.38           C  
-ATOM  11466  C   LEU C 530     -39.540  14.343-132.966  1.00 17.50           C  
-ATOM  11467  O   LEU C 530     -40.704  14.299-132.558  1.00 14.00           O  
-ATOM  11468  CB  LEU C 530     -37.608  15.384-131.803  1.00 14.82           C  
-ATOM  11469  CG  LEU C 530     -36.572  15.445-130.687  1.00 15.96           C  
-ATOM  11470  CD1 LEU C 530     -36.210  16.889-130.384  1.00 15.45           C  
-ATOM  11471  CD2 LEU C 530     -37.092  14.761-129.447  1.00 15.80           C  
-ATOM  11472  N   MET C 531     -39.220  14.611-134.229  1.00 17.14           N  
-ATOM  11473  CA  MET C 531     -40.236  14.959-135.215  1.00 24.78           C  
-ATOM  11474  C   MET C 531     -41.270  13.848-135.404  1.00 24.58           C  
-ATOM  11475  O   MET C 531     -42.480  14.094-135.322  1.00 28.12           O  
-ATOM  11476  CB  MET C 531     -39.563  15.304-136.542  1.00 13.11           C  
-ATOM  11477  CG  MET C 531     -38.559  16.433-136.417  1.00 11.30           C  
-ATOM  11478  SD  MET C 531     -37.504  16.591-137.861  1.00 27.73           S  
-ATOM  11479  CE  MET C 531     -38.689  17.122-139.090  1.00 22.43           C  
-ATOM  11480  N   VAL C 532     -40.791  12.633-135.652  1.00 15.84           N  
-ATOM  11481  CA  VAL C 532     -41.671  11.477-135.774  1.00 13.90           C  
-ATOM  11482  C   VAL C 532     -42.569  11.340-134.547  1.00 19.06           C  
-ATOM  11483  O   VAL C 532     -43.781  11.170-134.672  1.00 18.50           O  
-ATOM  11484  CB  VAL C 532     -40.871  10.177-135.962  1.00 11.62           C  
-ATOM  11485  CG1 VAL C 532     -41.777   8.973-135.834  1.00  9.96           C  
-ATOM  11486  CG2 VAL C 532     -40.172  10.186-137.307  1.00 17.91           C  
-ATOM  11487  N   ALA C 533     -41.966  11.439-133.366  1.00 24.43           N  
-ATOM  11488  CA  ALA C 533     -42.699  11.308-132.109  1.00 22.67           C  
-ATOM  11489  C   ALA C 533     -43.825  12.333-132.012  1.00 29.00           C  
-ATOM  11490  O   ALA C 533     -44.955  11.989-131.658  1.00 23.33           O  
-ATOM  11491  CB  ALA C 533     -41.756  11.450-130.925  1.00 18.53           C  
-ATOM  11492  N   HIS C 534     -43.514  13.591-132.323  1.00 31.13           N  
-ATOM  11493  CA  HIS C 534     -44.528  14.639-132.289  1.00 29.27           C  
-ATOM  11494  C   HIS C 534     -45.649  14.351-133.278  1.00 26.18           C  
-ATOM  11495  O   HIS C 534     -46.826  14.476-132.942  1.00 28.17           O  
-ATOM  11496  CB  HIS C 534     -43.926  16.009-132.595  1.00 23.28           C  
-ATOM  11497  CG  HIS C 534     -44.952  17.037-132.960  1.00 22.83           C  
-ATOM  11498  ND1 HIS C 534     -45.797  17.606-132.032  1.00 26.21           N  
-ATOM  11499  CD2 HIS C 534     -45.291  17.573-134.156  1.00 22.34           C  
-ATOM  11500  CE1 HIS C 534     -46.601  18.462-132.639  1.00 28.85           C  
-ATOM  11501  NE2 HIS C 534     -46.315  18.460-133.928  1.00 25.38           N  
-ATOM  11502  N   VAL C 535     -45.278  13.966-134.496  1.00 24.77           N  
-ATOM  11503  CA  VAL C 535     -46.259  13.720-135.548  1.00 20.57           C  
-ATOM  11504  C   VAL C 535     -47.149  12.512-135.216  1.00 25.22           C  
-ATOM  11505  O   VAL C 535     -48.294  12.430-135.665  1.00 25.19           O  
-ATOM  11506  CB  VAL C 535     -45.545  13.542-136.920  1.00 23.18           C  
-ATOM  11507  CG1 VAL C 535     -46.272  12.563-137.827  1.00 34.64           C  
-ATOM  11508  CG2 VAL C 535     -45.388  14.893-137.605  1.00 23.80           C  
-ATOM  11509  N   CYS C 536     -46.643  11.603-134.387  1.00 29.31           N  
-ATOM  11510  CA  CYS C 536     -47.407  10.410-134.025  1.00 21.52           C  
-ATOM  11511  C   CYS C 536     -47.992  10.464-132.613  1.00 22.98           C  
-ATOM  11512  O   CYS C 536     -48.420   9.442-132.080  1.00 29.38           O  
-ATOM  11513  CB  CYS C 536     -46.528   9.167-134.162  1.00 20.17           C  
-ATOM  11514  SG  CYS C 536     -45.852   8.925-135.817  1.00 40.44           S  
-ATOM  11515  N   ASN C 537     -48.017  11.655-132.020  1.00 29.42           N  
-ATOM  11516  CA  ASN C 537     -48.488  11.841-130.644  1.00 33.47           C  
-ATOM  11517  C   ASN C 537     -47.808  10.916-129.641  1.00 30.90           C  
-ATOM  11518  O   ASN C 537     -48.466  10.315-128.792  1.00 29.15           O  
-ATOM  11519  CB  ASN C 537     -50.005  11.649-130.561  1.00 29.44           C  
-ATOM  11520  CG  ASN C 537     -50.768  12.938-130.781  1.00 51.07           C  
-ATOM  11521  OD1 ASN C 537     -50.912  13.751-129.866  1.00 56.27           O  
-ATOM  11522  ND2 ASN C 537     -51.271  13.130-131.996  1.00 49.31           N  
-ATOM  11523  N   LEU C 538     -46.489  10.806-129.744  1.00 29.20           N  
-ATOM  11524  CA  LEU C 538     -45.724   9.957-128.841  1.00 26.97           C  
-ATOM  11525  C   LEU C 538     -44.693  10.772-128.069  1.00 26.12           C  
-ATOM  11526  O   LEU C 538     -44.453  11.939-128.376  1.00 29.32           O  
-ATOM  11527  CB  LEU C 538     -45.037   8.834-129.618  1.00 27.84           C  
-ATOM  11528  CG  LEU C 538     -45.970   7.900-130.388  1.00 19.92           C  
-ATOM  11529  CD1 LEU C 538     -45.187   7.022-131.354  1.00 18.02           C  
-ATOM  11530  CD2 LEU C 538     -46.782   7.053-129.421  1.00 22.84           C  
-ATOM  11531  N   LYS C 539     -44.089  10.153-127.062  1.00 15.03           N  
-ATOM  11532  CA  LYS C 539     -43.059  10.808-126.271  1.00 26.11           C  
-ATOM  11533  C   LYS C 539     -41.672  10.304-126.660  1.00 30.67           C  
-ATOM  11534  O   LYS C 539     -41.409   9.105-126.607  1.00 36.15           O  
-ATOM  11535  CB  LYS C 539     -43.305  10.578-124.778  1.00 32.94           C  
-ATOM  11536  CG  LYS C 539     -44.214  11.603-124.116  1.00 29.42           C  
-ATOM  11537  CD  LYS C 539     -43.470  12.895-123.783  1.00 55.29           C  
-ATOM  11538  CE  LYS C 539     -42.431  12.698-122.677  1.00 63.37           C  
-ATOM  11539  NZ  LYS C 539     -41.099  12.250-123.187  1.00 42.24           N  
-ATOM  11540  N   PRO C 540     -40.778  11.220-127.058  1.00 27.80           N  
-ATOM  11541  CA  PRO C 540     -39.404  10.822-127.378  1.00 24.45           C  
-ATOM  11542  C   PRO C 540     -38.689  10.259-126.159  1.00 26.29           C  
-ATOM  11543  O   PRO C 540     -38.638  10.912-125.117  1.00 30.99           O  
-ATOM  11544  CB  PRO C 540     -38.755  12.129-127.842  1.00 24.13           C  
-ATOM  11545  CG  PRO C 540     -39.584  13.206-127.236  1.00 32.66           C  
-ATOM  11546  CD  PRO C 540     -40.984  12.669-127.208  1.00 38.02           C  
-ATOM  11547  N   LYS C 541     -38.147   9.055-126.292  1.00 28.79           N  
-ATOM  11548  CA  LYS C 541     -37.542   8.367-125.162  1.00 27.12           C  
-ATOM  11549  C   LYS C 541     -36.041   8.183-125.333  1.00 27.43           C  
-ATOM  11550  O   LYS C 541     -35.265   8.495-124.428  1.00 28.68           O  
-ATOM  11551  CB  LYS C 541     -38.202   7.003-124.956  1.00 26.92           C  
-ATOM  11552  CG  LYS C 541     -37.701   6.245-123.735  1.00 34.96           C  
-ATOM  11553  CD  LYS C 541     -38.181   6.890-122.442  1.00 40.59           C  
-ATOM  11554  CE  LYS C 541     -37.585   6.203-121.224  1.00 50.34           C  
-ATOM  11555  NZ  LYS C 541     -36.109   6.410-121.135  1.00 58.37           N  
-ATOM  11556  N   GLU C 542     -35.630   7.689-126.496  1.00 27.71           N  
-ATOM  11557  CA  GLU C 542     -34.262   7.215-126.645  1.00 26.44           C  
-ATOM  11558  C   GLU C 542     -33.812   7.050-128.095  1.00 23.53           C  
-ATOM  11559  O   GLU C 542     -34.516   6.453-128.909  1.00 18.13           O  
-ATOM  11560  CB  GLU C 542     -34.127   5.883-125.913  1.00 22.63           C  
-ATOM  11561  CG  GLU C 542     -32.735   5.532-125.464  1.00 23.65           C  
-ATOM  11562  CD  GLU C 542     -32.717   4.219-124.718  1.00 37.43           C  
-ATOM  11563  OE1 GLU C 542     -31.887   4.063-123.797  1.00 31.12           O  
-ATOM  11564  OE2 GLU C 542     -33.544   3.342-125.054  1.00 36.85           O  
-ATOM  11565  N   PHE C 543     -32.634   7.580-128.413  1.00 21.24           N  
-ATOM  11566  CA  PHE C 543     -31.991   7.279-129.686  1.00 17.31           C  
-ATOM  11567  C   PHE C 543     -30.865   6.284-129.453  1.00 20.29           C  
-ATOM  11568  O   PHE C 543     -30.051   6.467-128.552  1.00 22.78           O  
-ATOM  11569  CB  PHE C 543     -31.443   8.537-130.359  1.00 13.10           C  
-ATOM  11570  CG  PHE C 543     -30.361   8.252-131.363  1.00 15.36           C  
-ATOM  11571  CD1 PHE C 543     -30.661   7.642-132.570  1.00 15.94           C  
-ATOM  11572  CD2 PHE C 543     -29.041   8.578-131.095  1.00 20.35           C  
-ATOM  11573  CE1 PHE C 543     -29.665   7.368-133.492  1.00 18.82           C  
-ATOM  11574  CE2 PHE C 543     -28.040   8.306-132.014  1.00 14.72           C  
-ATOM  11575  CZ  PHE C 543     -28.353   7.700-133.213  1.00 14.16           C  
-ATOM  11576  N   ILE C 544     -30.815   5.233-130.262  1.00 19.36           N  
-ATOM  11577  CA  ILE C 544     -29.806   4.201-130.075  1.00 15.26           C  
-ATOM  11578  C   ILE C 544     -28.894   4.091-131.291  1.00 16.56           C  
-ATOM  11579  O   ILE C 544     -29.351   3.887-132.414  1.00 19.53           O  
-ATOM  11580  CB  ILE C 544     -30.453   2.840-129.783  1.00 14.52           C  
-ATOM  11581  CG1 ILE C 544     -31.380   2.955-128.571  1.00 17.11           C  
-ATOM  11582  CG2 ILE C 544     -29.386   1.788-129.543  1.00 11.82           C  
-ATOM  11583  CD1 ILE C 544     -32.183   1.711-128.286  1.00 19.35           C  
-ATOM  11584  N   HIS C 545     -27.597   4.232-131.050  1.00 17.02           N  
-ATOM  11585  CA  HIS C 545     -26.608   4.263-132.118  1.00 16.22           C  
-ATOM  11586  C   HIS C 545     -25.850   2.944-132.252  1.00 15.86           C  
-ATOM  11587  O   HIS C 545     -25.068   2.567-131.372  1.00 23.74           O  
-ATOM  11588  CB  HIS C 545     -25.625   5.408-131.879  1.00 15.68           C  
-ATOM  11589  CG  HIS C 545     -25.002   5.938-133.132  1.00 19.73           C  
-ATOM  11590  ND1 HIS C 545     -25.062   5.264-134.331  1.00 24.73           N  
-ATOM  11591  CD2 HIS C 545     -24.317   7.080-133.373  1.00 21.50           C  
-ATOM  11592  CE1 HIS C 545     -24.433   5.965-135.259  1.00 25.67           C  
-ATOM  11593  NE2 HIS C 545     -23.973   7.070-134.705  1.00 29.30           N  
-ATOM  11594  N   PHE C 546     -26.099   2.249-133.359  1.00 12.99           N  
-ATOM  11595  CA  PHE C 546     -25.385   1.021-133.697  1.00 16.82           C  
-ATOM  11596  C   PHE C 546     -24.375   1.287-134.806  1.00 20.64           C  
-ATOM  11597  O   PHE C 546     -24.737   1.740-135.890  1.00 25.79           O  
-ATOM  11598  CB  PHE C 546     -26.360  -0.079-134.122  1.00 19.09           C  
-ATOM  11599  CG  PHE C 546     -27.007  -0.790-132.969  1.00 22.80           C  
-ATOM  11600  CD1 PHE C 546     -26.611  -0.528-131.668  1.00 17.49           C  
-ATOM  11601  CD2 PHE C 546     -28.000  -1.729-133.186  1.00 18.26           C  
-ATOM  11602  CE1 PHE C 546     -27.198  -1.181-130.607  1.00 12.98           C  
-ATOM  11603  CE2 PHE C 546     -28.591  -2.386-132.126  1.00 18.14           C  
-ATOM  11604  CZ  PHE C 546     -28.189  -2.111-130.835  1.00 14.53           C  
-ATOM  11605  N   MET C 547     -23.108   0.996-134.533  1.00 19.30           N  
-ATOM  11606  CA  MET C 547     -22.021   1.398-135.418  1.00 17.01           C  
-ATOM  11607  C   MET C 547     -21.212   0.206-135.910  1.00 17.15           C  
-ATOM  11608  O   MET C 547     -20.808  -0.648-135.123  1.00 19.24           O  
-ATOM  11609  CB  MET C 547     -21.109   2.388-134.696  1.00 17.87           C  
-ATOM  11610  CG  MET C 547     -21.867   3.307-133.748  1.00 28.22           C  
-ATOM  11611  SD  MET C 547     -20.827   4.369-132.732  1.00 26.00           S  
-ATOM  11612  CE  MET C 547     -20.237   5.520-133.964  1.00 29.31           C  
-ATOM  11613  N   GLY C 548     -20.978   0.157-137.217  1.00 20.82           N  
-ATOM  11614  CA  GLY C 548     -20.207  -0.916-137.819  1.00 23.47           C  
-ATOM  11615  C   GLY C 548     -18.722  -0.621-137.810  1.00 21.03           C  
-ATOM  11616  O   GLY C 548     -18.057  -0.785-136.787  1.00 22.76           O  
-ATOM  11617  N   ASN C 549     -18.197  -0.190-138.953  1.00 17.65           N  
-ATOM  11618  CA  ASN C 549     -16.806   0.238-139.030  1.00 18.22           C  
-ATOM  11619  C   ASN C 549     -16.639   1.584-138.332  1.00 21.85           C  
-ATOM  11620  O   ASN C 549     -16.937   2.630-138.908  1.00 29.85           O  
-ATOM  11621  CB  ASN C 549     -16.344   0.330-140.487  1.00 19.87           C  
-ATOM  11622  CG  ASN C 549     -14.831   0.361-140.622  1.00 25.85           C  
-ATOM  11623  OD1 ASN C 549     -14.185   1.355-140.293  1.00 29.90           O  
-ATOM  11624  ND2 ASN C 549     -14.261  -0.727-141.124  1.00 27.44           N  
-ATOM  11625  N   THR C 550     -16.174   1.550-137.087  1.00 19.14           N  
-ATOM  11626  CA  THR C 550     -16.053   2.756-136.272  1.00 23.77           C  
-ATOM  11627  C   THR C 550     -14.602   3.229-136.210  1.00 27.45           C  
-ATOM  11628  O   THR C 550     -13.753   2.578-135.602  1.00 30.52           O  
-ATOM  11629  CB  THR C 550     -16.579   2.515-134.848  1.00 24.10           C  
-ATOM  11630  OG1 THR C 550     -17.816   1.797-134.911  1.00 25.59           O  
-ATOM  11631  CG2 THR C 550     -16.806   3.831-134.133  1.00 28.48           C  
-ATOM  11632  N   HIS C 551     -14.326   4.373-136.826  1.00 22.69           N  
-ATOM  11633  CA  HIS C 551     -12.949   4.784-137.072  1.00 25.24           C  
-ATOM  11634  C   HIS C 551     -12.690   6.268-136.836  1.00 29.29           C  
-ATOM  11635  O   HIS C 551     -13.594   7.095-136.950  1.00 36.52           O  
-ATOM  11636  CB  HIS C 551     -12.572   4.441-138.510  1.00 22.41           C  
-ATOM  11637  CG  HIS C 551     -13.409   5.147-139.527  1.00 22.65           C  
-ATOM  11638  ND1 HIS C 551     -14.636   4.673-139.940  1.00 27.34           N  
-ATOM  11639  CD2 HIS C 551     -13.209   6.306-140.199  1.00 30.82           C  
-ATOM  11640  CE1 HIS C 551     -15.150   5.503-140.830  1.00 34.35           C  
-ATOM  11641  NE2 HIS C 551     -14.304   6.501-141.006  1.00 38.04           N  
-ATOM  11642  N   VAL C 552     -11.443   6.598-136.515  1.00 30.16           N  
-ATOM  11643  CA  VAL C 552     -10.999   7.987-136.523  1.00 38.62           C  
-ATOM  11644  C   VAL C 552      -9.881   8.132-137.555  1.00 41.85           C  
-ATOM  11645  O   VAL C 552      -9.111   7.196-137.792  1.00 38.04           O  
-ATOM  11646  CB  VAL C 552     -10.514   8.462-135.129  1.00 30.34           C  
-ATOM  11647  CG1 VAL C 552     -11.445   7.949-134.042  1.00 25.86           C  
-ATOM  11648  CG2 VAL C 552      -9.081   8.021-134.855  1.00 27.38           C  
-ATOM  11649  N   TYR C 553      -9.809   9.294-138.195  1.00 33.61           N  
-ATOM  11650  CA  TYR C 553      -8.770   9.530-139.186  1.00 34.97           C  
-ATOM  11651  C   TYR C 553      -7.492   9.980-138.494  1.00 36.74           C  
-ATOM  11652  O   TYR C 553      -7.536  10.663-137.474  1.00 41.86           O  
-ATOM  11653  CB  TYR C 553      -9.231  10.555-140.224  1.00 32.49           C  
-ATOM  11654  CG  TYR C 553     -10.256   9.995-141.184  1.00 40.80           C  
-ATOM  11655  CD1 TYR C 553      -9.894   9.050-142.137  1.00 43.36           C  
-ATOM  11656  CD2 TYR C 553     -11.583  10.397-141.132  1.00 36.15           C  
-ATOM  11657  CE1 TYR C 553     -10.824   8.523-143.013  1.00 41.15           C  
-ATOM  11658  CE2 TYR C 553     -12.523   9.877-142.005  1.00 39.99           C  
-ATOM  11659  CZ  TYR C 553     -12.136   8.939-142.943  1.00 43.83           C  
-ATOM  11660  OH  TYR C 553     -13.061   8.416-143.817  1.00 48.78           O  
-ATOM  11661  N   THR C 554      -6.355   9.575-139.047  1.00 44.16           N  
-ATOM  11662  CA  THR C 554      -5.063   9.835-138.423  1.00 38.82           C  
-ATOM  11663  C   THR C 554      -4.732  11.323-138.347  1.00 44.44           C  
-ATOM  11664  O   THR C 554      -3.932  11.737-137.511  1.00 44.50           O  
-ATOM  11665  CB  THR C 554      -3.931   9.112-139.167  1.00 42.40           C  
-ATOM  11666  OG1 THR C 554      -4.162   9.190-140.580  1.00 52.63           O  
-ATOM  11667  CG2 THR C 554      -3.872   7.649-138.750  1.00 34.81           C  
-ATOM  11668  N   ASN C 555      -5.347  12.125-139.211  1.00 45.36           N  
-ATOM  11669  CA  ASN C 555      -5.157  13.571-139.160  1.00 45.38           C  
-ATOM  11670  C   ASN C 555      -6.183  14.243-138.247  1.00 40.05           C  
-ATOM  11671  O   ASN C 555      -6.467  15.435-138.383  1.00 37.85           O  
-ATOM  11672  CB  ASN C 555      -5.221  14.171-140.568  1.00 49.12           C  
-ATOM  11673  CG  ASN C 555      -6.441  13.717-141.346  1.00 50.01           C  
-ATOM  11674  OD1 ASN C 555      -7.066  12.713-141.011  1.00 54.70           O  
-ATOM  11675  ND2 ASN C 555      -6.778  14.452-142.401  1.00 46.17           N  
-ATOM  11676  N   HIS C 556      -6.727  13.465-137.314  1.00 45.27           N  
-ATOM  11677  CA  HIS C 556      -7.699  13.958-136.341  1.00 42.30           C  
-ATOM  11678  C   HIS C 556      -7.258  13.682-134.911  1.00 42.39           C  
-ATOM  11679  O   HIS C 556      -7.779  14.277-133.973  1.00 40.51           O  
-ATOM  11680  CB  HIS C 556      -9.068  13.314-136.565  1.00 34.92           C  
-ATOM  11681  CG  HIS C 556      -9.770  13.787-137.798  1.00 42.49           C  
-ATOM  11682  ND1 HIS C 556     -10.972  13.257-138.215  1.00 53.25           N  
-ATOM  11683  CD2 HIS C 556      -9.444  14.740-138.702  1.00 53.53           C  
-ATOM  11684  CE1 HIS C 556     -11.356  13.862-139.325  1.00 63.43           C  
-ATOM  11685  NE2 HIS C 556     -10.446  14.766-139.642  1.00 65.78           N  
-ATOM  11686  N   VAL C 557      -6.303  12.769-134.758  1.00 37.10           N  
-ATOM  11687  CA  VAL C 557      -5.926  12.232-133.450  1.00 37.32           C  
-ATOM  11688  C   VAL C 557      -5.487  13.301-132.453  1.00 46.71           C  
-ATOM  11689  O   VAL C 557      -5.870  13.261-131.280  1.00 47.79           O  
-ATOM  11690  CB  VAL C 557      -4.792  11.199-133.584  1.00 47.11           C  
-ATOM  11691  CG1 VAL C 557      -4.444  10.620-132.227  1.00 37.67           C  
-ATOM  11692  CG2 VAL C 557      -5.195  10.103-134.556  1.00 48.32           C  
-ATOM  11693  N  AGLU C 558      -4.682  14.245-132.931  0.47 52.16           N  
-ATOM  11694  N  BGLU C 558      -4.675  14.249-132.916  0.53 52.44           N  
-ATOM  11695  CA AGLU C 558      -4.217  15.355-132.112  0.47 49.65           C  
-ATOM  11696  CA BGLU C 558      -4.215  15.345-132.067  0.53 50.76           C  
-ATOM  11697  C  AGLU C 558      -5.393  16.172-131.593  0.47 47.11           C  
-ATOM  11698  C  BGLU C 558      -5.392  16.190-131.584  0.53 48.39           C  
-ATOM  11699  O  AGLU C 558      -5.509  16.434-130.391  0.47 42.78           O  
-ATOM  11700  O  BGLU C 558      -5.510  16.490-130.393  0.53 44.22           O  
-ATOM  11701  CB AGLU C 558      -3.269  16.249-132.915  0.47 48.79           C  
-ATOM  11702  CB BGLU C 558      -3.208  16.224-132.815  0.53 48.92           C  
-ATOM  11703  CG AGLU C 558      -2.155  15.501-133.634  0.47 51.77           C  
-ATOM  11704  CG BGLU C 558      -2.683  17.400-131.993  0.53 49.90           C  
-ATOM  11705  CD AGLU C 558      -2.464  15.248-135.098  0.47 51.48           C  
-ATOM  11706  CD BGLU C 558      -1.743  18.289-132.784  0.53 51.46           C  
-ATOM  11707  OE1AGLU C 558      -3.464  14.557-135.396  0.47 45.51           O  
-ATOM  11708  OE1BGLU C 558      -1.250  17.832-133.835  0.53 49.64           O  
-ATOM  11709  OE2AGLU C 558      -1.702  15.748-135.952  0.47 45.44           O  
-ATOM  11710  OE2BGLU C 558      -1.501  19.441-132.359  0.53 46.70           O  
-ATOM  11711  N   ALA C 559      -6.265  16.561-132.517  1.00 44.18           N  
-ATOM  11712  CA  ALA C 559      -7.433  17.371-132.203  1.00 46.46           C  
-ATOM  11713  C   ALA C 559      -8.381  16.660-131.242  1.00 44.72           C  
-ATOM  11714  O   ALA C 559      -8.988  17.292-130.383  1.00 47.91           O  
-ATOM  11715  CB  ALA C 559      -8.163  17.748-133.485  1.00 44.41           C  
-ATOM  11716  N   LEU C 560      -8.503  15.347-131.388  1.00 40.26           N  
-ATOM  11717  CA  LEU C 560      -9.365  14.565-130.513  1.00 36.48           C  
-ATOM  11718  C   LEU C 560      -8.762  14.478-129.125  1.00 32.72           C  
-ATOM  11719  O   LEU C 560      -9.474  14.558-128.126  1.00 29.72           O  
-ATOM  11720  CB  LEU C 560      -9.592  13.165-131.084  1.00 28.36           C  
-ATOM  11721  CG  LEU C 560     -10.374  13.123-132.398  1.00 33.77           C  
-ATOM  11722  CD1 LEU C 560     -10.636  11.689-132.832  1.00 37.34           C  
-ATOM  11723  CD2 LEU C 560     -11.671  13.904-132.271  1.00 35.32           C  
-ATOM  11724  N   LYS C 561      -7.446  14.308-129.070  1.00 31.82           N  
-ATOM  11725  CA  LYS C 561      -6.734  14.311-127.801  1.00 36.13           C  
-ATOM  11726  C   LYS C 561      -6.926  15.648-127.100  1.00 45.17           C  
-ATOM  11727  O   LYS C 561      -7.007  15.712-125.870  1.00 36.99           O  
-ATOM  11728  CB  LYS C 561      -5.246  14.024-128.011  1.00 50.45           C  
-ATOM  11729  CG  LYS C 561      -4.948  12.565-128.314  1.00 49.64           C  
-ATOM  11730  CD  LYS C 561      -3.450  12.286-128.365  1.00 56.33           C  
-ATOM  11731  CE  LYS C 561      -3.167  10.818-128.660  1.00 54.05           C  
-ATOM  11732  NZ  LYS C 561      -1.707  10.520-128.618  1.00 50.85           N  
-ATOM  11733  N   GLU C 562      -6.987  16.714-127.893  1.00 51.68           N  
-ATOM  11734  CA  GLU C 562      -7.304  18.033-127.367  1.00 42.75           C  
-ATOM  11735  C   GLU C 562      -8.728  18.032-126.811  1.00 40.17           C  
-ATOM  11736  O   GLU C 562      -8.976  18.511-125.707  1.00 34.31           O  
-ATOM  11737  CB  GLU C 562      -7.149  19.104-128.452  1.00 39.94           C  
-ATOM  11738  CG  GLU C 562      -5.709  19.530-128.745  1.00 57.65           C  
-ATOM  11739  CD  GLU C 562      -5.304  20.797-128.005  1.00 71.08           C  
-ATOM  11740  OE1 GLU C 562      -5.240  20.769-126.757  1.00 72.27           O  
-ATOM  11741  OE2 GLU C 562      -5.049  21.823-128.674  1.00 66.76           O  
-ATOM  11742  N   GLN C 563      -9.649  17.463-127.583  1.00 40.19           N  
-ATOM  11743  CA  GLN C 563     -11.073  17.454-127.266  1.00 31.79           C  
-ATOM  11744  C   GLN C 563     -11.372  16.661-125.998  1.00 29.25           C  
-ATOM  11745  O   GLN C 563     -12.366  16.916-125.321  1.00 25.73           O  
-ATOM  11746  CB  GLN C 563     -11.866  16.885-128.452  1.00 25.18           C  
-ATOM  11747  CG  GLN C 563     -13.388  16.991-128.340  1.00 17.77           C  
-ATOM  11748  CD  GLN C 563     -14.091  16.687-129.657  1.00 26.09           C  
-ATOM  11749  OE1 GLN C 563     -13.483  16.748-130.726  1.00 41.47           O  
-ATOM  11750  NE2 GLN C 563     -15.374  16.358-129.585  1.00 18.38           N  
-ATOM  11751  N   LEU C 564     -10.509  15.705-125.676  1.00 27.93           N  
-ATOM  11752  CA  LEU C 564     -10.746  14.841-124.528  1.00 24.35           C  
-ATOM  11753  C   LEU C 564     -10.358  15.506-123.213  1.00 24.25           C  
-ATOM  11754  O   LEU C 564     -10.719  15.020-122.143  1.00 23.21           O  
-ATOM  11755  CB  LEU C 564      -9.989  13.520-124.681  1.00 34.31           C  
-ATOM  11756  CG  LEU C 564     -10.432  12.593-125.815  1.00 32.38           C  
-ATOM  11757  CD1 LEU C 564      -9.649  11.285-125.778  1.00 34.95           C  
-ATOM  11758  CD2 LEU C 564     -11.929  12.332-125.753  1.00 37.24           C  
-ATOM  11759  N   ARG C 565      -9.619  16.608-123.285  1.00 32.96           N  
-ATOM  11760  CA  ARG C 565      -9.254  17.342-122.075  1.00 36.26           C  
-ATOM  11761  C   ARG C 565     -10.429  18.171-121.572  1.00 24.28           C  
-ATOM  11762  O   ARG C 565     -10.448  18.613-120.423  1.00 17.82           O  
-ATOM  11763  CB  ARG C 565      -8.039  18.237-122.327  1.00 37.68           C  
-ATOM  11764  CG  ARG C 565      -6.714  17.499-122.258  1.00 41.96           C  
-ATOM  11765  CD  ARG C 565      -5.542  18.405-122.591  1.00 48.84           C  
-ATOM  11766  NE  ARG C 565      -5.011  18.132-123.924  1.00 72.79           N  
-ATOM  11767  CZ  ARG C 565      -4.123  17.179-124.194  1.00 76.80           C  
-ATOM  11768  NH1 ARG C 565      -3.664  16.400-123.221  1.00 65.66           N  
-ATOM  11769  NH2 ARG C 565      -3.695  17.001-125.437  1.00 55.38           N  
-ATOM  11770  N   ARG C 566     -11.408  18.373-122.447  1.00 25.83           N  
-ATOM  11771  CA  ARG C 566     -12.603  19.136-122.119  1.00 17.69           C  
-ATOM  11772  C   ARG C 566     -13.644  18.261-121.432  1.00 21.51           C  
-ATOM  11773  O   ARG C 566     -13.895  17.134-121.858  1.00 29.21           O  
-ATOM  11774  CB  ARG C 566     -13.204  19.753-123.385  1.00 14.98           C  
-ATOM  11775  CG  ARG C 566     -12.213  20.508-124.261  1.00 19.35           C  
-ATOM  11776  CD  ARG C 566     -12.861  20.944-125.568  1.00 22.39           C  
-ATOM  11777  NE  ARG C 566     -12.022  21.857-126.343  1.00 28.71           N  
-ATOM  11778  CZ  ARG C 566     -12.385  22.392-127.505  1.00 27.78           C  
-ATOM  11779  NH1 ARG C 566     -11.569  23.215-128.150  1.00 26.77           N  
-ATOM  11780  NH2 ARG C 566     -13.569  22.104-128.024  1.00 30.93           N  
-ATOM  11781  N   GLU C 567     -14.248  18.779-120.368  1.00 19.54           N  
-ATOM  11782  CA  GLU C 567     -15.382  18.109-119.744  1.00 22.74           C  
-ATOM  11783  C   GLU C 567     -16.679  18.634-120.349  1.00 20.76           C  
-ATOM  11784  O   GLU C 567     -16.802  19.828-120.615  1.00 28.91           O  
-ATOM  11785  CB  GLU C 567     -15.376  18.308-118.228  1.00 23.28           C  
-ATOM  11786  CG  GLU C 567     -15.059  19.722-117.795  1.00 29.50           C  
-ATOM  11787  CD  GLU C 567     -13.581  19.932-117.564  1.00 34.90           C  
-ATOM  11788  OE1 GLU C 567     -12.912  18.973-117.127  1.00 30.64           O  
-ATOM  11789  OE2 GLU C 567     -13.089  21.050-117.823  1.00 51.89           O  
-ATOM  11790  N   PRO C 568     -17.653  17.740-120.570  1.00 18.18           N  
-ATOM  11791  CA  PRO C 568     -18.901  18.096-121.253  1.00 18.06           C  
-ATOM  11792  C   PRO C 568     -19.775  19.058-120.459  1.00 17.80           C  
-ATOM  11793  O   PRO C 568     -19.614  19.196-119.247  1.00 16.94           O  
-ATOM  11794  CB  PRO C 568     -19.603  16.746-121.418  1.00 18.94           C  
-ATOM  11795  CG  PRO C 568     -19.064  15.911-120.311  1.00 22.88           C  
-ATOM  11796  CD  PRO C 568     -17.632  16.324-120.166  1.00 21.61           C  
-ATOM  11797  N   ARG C 569     -20.696  19.713-121.156  1.00 21.35           N  
-ATOM  11798  CA  ARG C 569     -21.624  20.653-120.541  1.00 17.16           C  
-ATOM  11799  C   ARG C 569     -23.037  20.076-120.589  1.00 16.72           C  
-ATOM  11800  O   ARG C 569     -23.276  19.100-121.303  1.00 20.78           O  
-ATOM  11801  CB  ARG C 569     -21.552  22.005-121.255  1.00 16.67           C  
-ATOM  11802  CG  ARG C 569     -20.146  22.582-121.322  1.00 19.75           C  
-ATOM  11803  CD  ARG C 569     -20.009  23.849-120.494  1.00 17.45           C  
-ATOM  11804  NE  ARG C 569     -18.626  24.321-120.458  1.00 21.93           N  
-ATOM  11805  CZ  ARG C 569     -18.068  25.082-121.394  1.00 19.02           C  
-ATOM  11806  NH1 ARG C 569     -16.804  25.461-121.274  1.00 15.76           N  
-ATOM  11807  NH2 ARG C 569     -18.771  25.464-122.452  1.00 16.20           N  
-ATOM  11808  N   PRO C 570     -23.974  20.652-119.815  1.00 15.40           N  
-ATOM  11809  CA  PRO C 570     -25.356  20.168-119.891  1.00 15.46           C  
-ATOM  11810  C   PRO C 570     -25.923  20.210-121.308  1.00 16.33           C  
-ATOM  11811  O   PRO C 570     -25.773  21.211-122.010  1.00 17.75           O  
-ATOM  11812  CB  PRO C 570     -26.122  21.129-118.966  1.00 11.24           C  
-ATOM  11813  CG  PRO C 570     -25.178  22.246-118.658  1.00 13.36           C  
-ATOM  11814  CD  PRO C 570     -23.814  21.651-118.747  1.00 15.84           C  
-ATOM  11815  N   PHE C 571     -26.545  19.111-121.721  1.00 13.21           N  
-ATOM  11816  CA  PHE C 571     -27.203  19.041-123.017  1.00 11.84           C  
-ATOM  11817  C   PHE C 571     -28.284  20.108-123.115  1.00 14.23           C  
-ATOM  11818  O   PHE C 571     -28.934  20.432-122.122  1.00 18.28           O  
-ATOM  11819  CB  PHE C 571     -27.809  17.654-123.242  1.00 15.29           C  
-ATOM  11820  CG  PHE C 571     -26.822  16.628-123.723  1.00 18.38           C  
-ATOM  11821  CD1 PHE C 571     -25.704  17.007-124.448  1.00 21.22           C  
-ATOM  11822  CD2 PHE C 571     -27.016  15.282-123.454  1.00 22.16           C  
-ATOM  11823  CE1 PHE C 571     -24.795  16.062-124.896  1.00 21.17           C  
-ATOM  11824  CE2 PHE C 571     -26.113  14.333-123.899  1.00 20.19           C  
-ATOM  11825  CZ  PHE C 571     -25.000  14.725-124.620  1.00 17.58           C  
-ATOM  11826  N   PRO C 572     -28.471  20.676-124.312  1.00 15.46           N  
-ATOM  11827  CA  PRO C 572     -29.543  21.653-124.497  1.00 17.41           C  
-ATOM  11828  C   PRO C 572     -30.902  20.979-124.644  1.00 20.30           C  
-ATOM  11829  O   PRO C 572     -30.992  19.753-124.612  1.00 17.33           O  
-ATOM  11830  CB  PRO C 572     -29.145  22.358-125.793  1.00 19.68           C  
-ATOM  11831  CG  PRO C 572     -28.439  21.297-126.569  1.00 14.69           C  
-ATOM  11832  CD  PRO C 572     -27.685  20.487-125.544  1.00 21.93           C  
-ATOM  11833  N   ILE C 573     -31.945  21.785-124.795  1.00 21.59           N  
-ATOM  11834  CA  ILE C 573     -33.280  21.291-125.087  1.00 20.81           C  
-ATOM  11835  C   ILE C 573     -33.680  21.747-126.481  1.00 26.40           C  
-ATOM  11836  O   ILE C 573     -33.544  22.924-126.813  1.00 25.40           O  
-ATOM  11837  CB  ILE C 573     -34.320  21.797-124.069  1.00 19.79           C  
-ATOM  11838  CG1 ILE C 573     -34.105  21.141-122.707  1.00 22.97           C  
-ATOM  11839  CG2 ILE C 573     -35.729  21.519-124.560  1.00 19.23           C  
-ATOM  11840  CD1 ILE C 573     -35.100  21.586-121.663  1.00 12.93           C  
-ATOM  11841  N   VAL C 574     -34.154  20.815-127.302  1.00 27.64           N  
-ATOM  11842  CA  VAL C 574     -34.662  21.169-128.620  1.00 25.39           C  
-ATOM  11843  C   VAL C 574     -36.184  21.237-128.591  1.00 24.01           C  
-ATOM  11844  O   VAL C 574     -36.860  20.219-128.448  1.00 30.01           O  
-ATOM  11845  CB  VAL C 574     -34.204  20.170-129.698  1.00 23.90           C  
-ATOM  11846  CG1 VAL C 574     -34.975  20.397-130.989  1.00 29.42           C  
-ATOM  11847  CG2 VAL C 574     -32.708  20.300-129.938  1.00 15.82           C  
-ATOM  11848  N   ASN C 575     -36.715  22.449-128.712  1.00 26.05           N  
-ATOM  11849  CA  ASN C 575     -38.155  22.660-128.700  1.00 24.27           C  
-ATOM  11850  C   ASN C 575     -38.731  22.781-130.104  1.00 23.55           C  
-ATOM  11851  O   ASN C 575     -38.164  23.454-130.971  1.00 18.92           O  
-ATOM  11852  CB  ASN C 575     -38.513  23.909-127.888  1.00 22.32           C  
-ATOM  11853  CG  ASN C 575     -38.373  23.694-126.392  1.00 30.65           C  
-ATOM  11854  OD1 ASN C 575     -37.950  24.590-125.661  1.00 33.87           O  
-ATOM  11855  ND2 ASN C 575     -38.728  22.500-125.929  1.00 21.28           N  
-ATOM  11856  N   ILE C 576     -39.859  22.113-130.317  1.00 24.93           N  
-ATOM  11857  CA  ILE C 576     -40.601  22.243-131.560  1.00 23.30           C  
-ATOM  11858  C   ILE C 576     -41.628  23.356-131.430  1.00 22.18           C  
-ATOM  11859  O   ILE C 576     -42.581  23.253-130.658  1.00 21.41           O  
-ATOM  11860  CB  ILE C 576     -41.318  20.939-131.950  1.00 20.33           C  
-ATOM  11861  CG1 ILE C 576     -40.306  19.819-132.183  1.00 23.50           C  
-ATOM  11862  CG2 ILE C 576     -42.158  21.160-133.198  1.00 19.33           C  
-ATOM  11863  CD1 ILE C 576     -40.927  18.534-132.686  1.00 20.37           C  
-ATOM  11864  N   LEU C 577     -41.423  24.427-132.184  1.00 18.88           N  
-ATOM  11865  CA  LEU C 577     -42.357  25.540-132.192  1.00 18.03           C  
-ATOM  11866  C   LEU C 577     -43.515  25.221-133.127  1.00 23.16           C  
-ATOM  11867  O   LEU C 577     -43.398  24.338-133.978  1.00 32.09           O  
-ATOM  11868  CB  LEU C 577     -41.657  26.824-132.631  1.00 24.40           C  
-ATOM  11869  CG  LEU C 577     -40.238  27.021-132.098  1.00 20.39           C  
-ATOM  11870  CD1 LEU C 577     -39.539  28.165-132.818  1.00 21.19           C  
-ATOM  11871  CD2 LEU C 577     -40.266  27.262-130.600  1.00 27.40           C  
-ATOM  11872  N   ASN C 578     -44.628  25.931-132.958  1.00 22.78           N  
-ATOM  11873  CA  ASN C 578     -45.771  25.829-133.866  1.00 23.83           C  
-ATOM  11874  C   ASN C 578     -46.358  24.423-133.987  1.00 26.12           C  
-ATOM  11875  O   ASN C 578     -46.835  24.027-135.054  1.00 25.83           O  
-ATOM  11876  CB  ASN C 578     -45.373  26.328-135.252  1.00 17.90           C  
-ATOM  11877  CG  ASN C 578     -44.577  27.614-135.200  1.00 16.41           C  
-ATOM  11878  OD1 ASN C 578     -44.810  28.474-134.349  1.00 21.60           O  
-ATOM  11879  ND2 ASN C 578     -43.626  27.752-136.113  1.00 14.86           N  
-ATOM  11880  N   LYS C 579     -46.333  23.680-132.885  1.00 27.98           N  
-ATOM  11881  CA  LYS C 579     -46.842  22.314-132.861  1.00 27.61           C  
-ATOM  11882  C   LYS C 579     -48.238  22.185-133.460  1.00 29.95           C  
-ATOM  11883  O   LYS C 579     -48.495  21.268-134.240  1.00 30.48           O  
-ATOM  11884  CB  LYS C 579     -46.858  21.779-131.430  1.00 37.82           C  
-ATOM  11885  CG  LYS C 579     -45.491  21.432-130.873  1.00 33.07           C  
-ATOM  11886  CD  LYS C 579     -45.617  20.389-129.774  1.00 30.63           C  
-ATOM  11887  CE  LYS C 579     -44.261  19.817-129.404  1.00 25.93           C  
-ATOM  11888  NZ  LYS C 579     -44.403  18.618-128.536  1.00 33.66           N  
-ATOM  11889  N   GLU C 580     -49.126  23.108-133.094  1.00 32.86           N  
-ATOM  11890  CA  GLU C 580     -50.521  23.082-133.534  1.00 30.97           C  
-ATOM  11891  C   GLU C 580     -50.650  23.119-135.053  1.00 31.03           C  
-ATOM  11892  O   GLU C 580     -51.636  22.636-135.605  1.00 31.62           O  
-ATOM  11893  CB  GLU C 580     -51.303  24.250-132.920  1.00 36.45           C  
-ATOM  11894  CG  GLU C 580     -50.621  24.914-131.736  1.00 40.78           C  
-ATOM  11895  CD  GLU C 580     -49.599  25.959-132.160  1.00 60.36           C  
-ATOM  11896  OE1 GLU C 580     -49.794  26.593-133.222  1.00 52.39           O  
-ATOM  11897  OE2 GLU C 580     -48.600  26.147-131.433  1.00 58.35           O  
-ATOM  11898  N   ARG C 581     -49.652  23.689-135.723  1.00 30.67           N  
-ATOM  11899  CA  ARG C 581     -49.666  23.766-137.181  1.00 21.16           C  
-ATOM  11900  C   ARG C 581     -49.146  22.480-137.806  1.00 17.56           C  
-ATOM  11901  O   ARG C 581     -49.527  22.117-138.917  1.00 20.32           O  
-ATOM  11902  CB  ARG C 581     -48.827  24.950-137.673  1.00 20.67           C  
-ATOM  11903  CG  ARG C 581     -49.090  25.326-139.117  1.00 15.96           C  
-ATOM  11904  CD  ARG C 581     -47.981  26.181-139.698  1.00 21.00           C  
-ATOM  11905  NE  ARG C 581     -46.816  25.385-140.072  1.00 29.65           N  
-ATOM  11906  CZ  ARG C 581     -45.607  25.520-139.536  1.00 22.88           C  
-ATOM  11907  NH1 ARG C 581     -44.609  24.749-139.949  1.00 18.75           N  
-ATOM  11908  NH2 ARG C 581     -45.394  26.426-138.591  1.00 30.41           N  
-ATOM  11909  N   ILE C 582     -48.274  21.793-137.081  1.00 24.63           N  
-ATOM  11910  CA  ILE C 582     -47.580  20.633-137.619  1.00 23.71           C  
-ATOM  11911  C   ILE C 582     -48.317  19.334-137.314  1.00 31.14           C  
-ATOM  11912  O   ILE C 582     -48.384  18.902-136.162  1.00 30.08           O  
-ATOM  11913  CB  ILE C 582     -46.146  20.550-137.066  1.00 21.38           C  
-ATOM  11914  CG1 ILE C 582     -45.385  21.838-137.391  1.00 22.95           C  
-ATOM  11915  CG2 ILE C 582     -45.432  19.335-137.627  1.00 19.40           C  
-ATOM  11916  CD1 ILE C 582     -44.043  21.950-136.714  1.00 21.20           C  
-ATOM  11917  N   LYS C 583     -48.876  18.723-138.355  1.00 33.25           N  
-ATOM  11918  CA  LYS C 583     -49.645  17.492-138.207  1.00 23.23           C  
-ATOM  11919  C   LYS C 583     -49.015  16.331-138.968  1.00 25.82           C  
-ATOM  11920  O   LYS C 583     -49.244  15.166-138.640  1.00 33.59           O  
-ATOM  11921  CB  LYS C 583     -51.083  17.709-138.677  1.00 25.48           C  
-ATOM  11922  CG  LYS C 583     -51.942  18.477-137.687  1.00 35.49           C  
-ATOM  11923  CD  LYS C 583     -53.184  19.054-138.347  1.00 42.85           C  
-ATOM  11924  CE  LYS C 583     -54.204  19.467-137.299  1.00 71.92           C  
-ATOM  11925  NZ  LYS C 583     -53.554  20.079-136.102  1.00 59.02           N  
-ATOM  11926  N   GLU C 584     -48.224  16.650-139.986  1.00 27.57           N  
-ATOM  11927  CA  GLU C 584     -47.542  15.622-140.765  1.00 33.74           C  
-ATOM  11928  C   GLU C 584     -46.044  15.897-140.858  1.00 27.27           C  
-ATOM  11929  O   GLU C 584     -45.594  17.015-140.614  1.00 22.40           O  
-ATOM  11930  CB  GLU C 584     -48.156  15.518-142.164  1.00 31.17           C  
-ATOM  11931  CG  GLU C 584     -49.676  15.353-142.177  1.00 32.81           C  
-ATOM  11932  CD  GLU C 584     -50.147  13.986-141.691  1.00 32.36           C  
-ATOM  11933  OE1 GLU C 584     -49.302  13.136-141.336  1.00 26.73           O  
-ATOM  11934  OE2 GLU C 584     -51.376  13.762-141.669  1.00 35.24           O  
-ATOM  11935  N   ILE C 585     -45.279  14.871-141.217  1.00 30.01           N  
-ATOM  11936  CA  ILE C 585     -43.822  14.961-141.230  1.00 24.89           C  
-ATOM  11937  C   ILE C 585     -43.312  15.990-142.241  1.00 25.24           C  
-ATOM  11938  O   ILE C 585     -42.240  16.571-142.065  1.00 20.21           O  
-ATOM  11939  CB  ILE C 585     -43.185  13.583-141.529  1.00 19.30           C  
-ATOM  11940  CG1 ILE C 585     -41.664  13.633-141.354  1.00 21.84           C  
-ATOM  11941  CG2 ILE C 585     -43.579  13.087-142.917  1.00 20.85           C  
-ATOM  11942  CD1 ILE C 585     -41.229  14.041-139.963  1.00 22.35           C  
-ATOM  11943  N   ASP C 586     -44.094  16.234-143.287  1.00 29.15           N  
-ATOM  11944  CA  ASP C 586     -43.696  17.173-144.327  1.00 21.89           C  
-ATOM  11945  C   ASP C 586     -44.047  18.613-143.962  1.00 27.48           C  
-ATOM  11946  O   ASP C 586     -43.692  19.545-144.683  1.00 30.26           O  
-ATOM  11947  CB  ASP C 586     -44.350  16.800-145.657  1.00 23.55           C  
-ATOM  11948  CG  ASP C 586     -44.035  15.380-146.079  1.00 35.48           C  
-ATOM  11949  OD1 ASP C 586     -42.885  15.126-146.499  1.00 39.87           O  
-ATOM  11950  OD2 ASP C 586     -44.940  14.520-145.994  1.00 28.05           O  
-ATOM  11951  N   ASP C 587     -44.738  18.791-142.840  1.00 29.26           N  
-ATOM  11952  CA  ASP C 587     -45.185  20.119-142.425  1.00 32.37           C  
-ATOM  11953  C   ASP C 587     -44.071  20.936-141.767  1.00 29.68           C  
-ATOM  11954  O   ASP C 587     -44.123  22.167-141.760  1.00 24.70           O  
-ATOM  11955  CB  ASP C 587     -46.383  20.009-141.475  1.00 27.99           C  
-ATOM  11956  CG  ASP C 587     -47.637  19.504-142.173  1.00 36.75           C  
-ATOM  11957  OD1 ASP C 587     -47.608  19.354-143.413  1.00 46.19           O  
-ATOM  11958  OD2 ASP C 587     -48.656  19.270-141.488  1.00 28.03           O  
-ATOM  11959  N   PHE C 588     -43.070  20.252-141.218  1.00 22.62           N  
-ATOM  11960  CA  PHE C 588     -41.940  20.919-140.576  1.00 18.43           C  
-ATOM  11961  C   PHE C 588     -41.189  21.842-141.530  1.00 20.01           C  
-ATOM  11962  O   PHE C 588     -41.026  21.531-142.709  1.00 21.43           O  
-ATOM  11963  CB  PHE C 588     -40.962  19.891-140.008  1.00 21.97           C  
-ATOM  11964  CG  PHE C 588     -41.433  19.226-138.748  1.00 23.26           C  
-ATOM  11965  CD1 PHE C 588     -41.195  19.807-137.514  1.00 16.13           C  
-ATOM  11966  CD2 PHE C 588     -42.095  18.011-138.795  1.00 21.89           C  
-ATOM  11967  CE1 PHE C 588     -41.617  19.192-136.350  1.00 15.05           C  
-ATOM  11968  CE2 PHE C 588     -42.518  17.391-137.634  1.00 16.60           C  
-ATOM  11969  CZ  PHE C 588     -42.281  17.984-136.411  1.00 12.72           C  
-ATOM  11970  N   THR C 589     -40.736  22.981-141.017  1.00 22.81           N  
-ATOM  11971  CA  THR C 589     -39.877  23.874-141.786  1.00 18.90           C  
-ATOM  11972  C   THR C 589     -38.626  24.206-140.985  1.00 22.76           C  
-ATOM  11973  O   THR C 589     -38.423  23.679-139.891  1.00 30.30           O  
-ATOM  11974  CB  THR C 589     -40.588  25.180-142.172  1.00 19.89           C  
-ATOM  11975  OG1 THR C 589     -40.836  25.955-140.994  1.00 27.01           O  
-ATOM  11976  CG2 THR C 589     -41.904  24.889-142.882  1.00 24.34           C  
-ATOM  11977  N   ALA C 590     -37.794  25.088-141.529  1.00 16.79           N  
-ATOM  11978  CA  ALA C 590     -36.510  25.403-140.916  1.00 16.24           C  
-ATOM  11979  C   ALA C 590     -36.661  26.274-139.669  1.00 32.77           C  
-ATOM  11980  O   ALA C 590     -35.758  26.335-138.833  1.00 30.55           O  
-ATOM  11981  CB  ALA C 590     -35.607  26.084-141.926  1.00 19.17           C  
-ATOM  11982  N   GLU C 591     -37.807  26.937-139.544  1.00 34.81           N  
-ATOM  11983  CA  GLU C 591     -38.039  27.865-138.440  1.00 25.59           C  
-ATOM  11984  C   GLU C 591     -38.918  27.283-137.345  1.00 19.56           C  
-ATOM  11985  O   GLU C 591     -39.325  27.993-136.427  1.00 30.22           O  
-ATOM  11986  CB  GLU C 591     -38.673  29.159-138.956  1.00 24.60           C  
-ATOM  11987  CG  GLU C 591     -37.698  30.102-139.622  1.00 34.21           C  
-ATOM  11988  CD  GLU C 591     -37.246  29.605-140.973  1.00 39.28           C  
-ATOM  11989  OE1 GLU C 591     -36.123  29.963-141.390  1.00 42.69           O  
-ATOM  11990  OE2 GLU C 591     -38.019  28.859-141.615  1.00 37.35           O  
-ATOM  11991  N   ASP C 592     -39.211  25.995-137.437  1.00 17.12           N  
-ATOM  11992  CA  ASP C 592     -40.106  25.371-136.475  1.00 21.70           C  
-ATOM  11993  C   ASP C 592     -39.342  24.723-135.327  1.00 23.47           C  
-ATOM  11994  O   ASP C 592     -39.868  23.851-134.635  1.00 22.32           O  
-ATOM  11995  CB  ASP C 592     -40.992  24.341-137.175  1.00 24.73           C  
-ATOM  11996  CG  ASP C 592     -41.913  24.971-138.200  1.00 24.22           C  
-ATOM  11997  OD1 ASP C 592     -42.544  26.002-137.883  1.00 21.83           O  
-ATOM  11998  OD2 ASP C 592     -42.002  24.440-139.325  1.00 25.81           O  
-ATOM  11999  N   PHE C 593     -38.102  25.159-135.123  1.00 30.60           N  
-ATOM  12000  CA  PHE C 593     -37.256  24.573-134.088  1.00 29.85           C  
-ATOM  12001  C   PHE C 593     -36.549  25.624-133.243  1.00 20.28           C  
-ATOM  12002  O   PHE C 593     -36.421  26.781-133.645  1.00 21.97           O  
-ATOM  12003  CB  PHE C 593     -36.231  23.632-134.719  1.00 23.83           C  
-ATOM  12004  CG  PHE C 593     -36.842  22.424-135.355  1.00 16.22           C  
-ATOM  12005  CD1 PHE C 593     -37.264  22.456-136.673  1.00 16.02           C  
-ATOM  12006  CD2 PHE C 593     -37.013  21.260-134.627  1.00 16.26           C  
-ATOM  12007  CE1 PHE C 593     -37.837  21.345-137.257  1.00 21.38           C  
-ATOM  12008  CE2 PHE C 593     -37.585  20.145-135.205  1.00 23.07           C  
-ATOM  12009  CZ  PHE C 593     -37.996  20.186-136.521  1.00 20.83           C  
-ATOM  12010  N   GLU C 594     -36.088  25.206-132.068  1.00 21.41           N  
-ATOM  12011  CA  GLU C 594     -35.463  26.120-131.123  1.00 21.95           C  
-ATOM  12012  C   GLU C 594     -34.486  25.399-130.192  1.00 24.86           C  
-ATOM  12013  O   GLU C 594     -34.899  24.624-129.331  1.00 26.68           O  
-ATOM  12014  CB  GLU C 594     -36.543  26.829-130.304  1.00 28.32           C  
-ATOM  12015  CG  GLU C 594     -36.017  27.851-129.318  1.00 32.67           C  
-ATOM  12016  CD  GLU C 594     -37.063  28.254-128.298  1.00 45.23           C  
-ATOM  12017  OE1 GLU C 594     -37.529  27.368-127.549  1.00 43.80           O  
-ATOM  12018  OE2 GLU C 594     -37.426  29.449-128.250  1.00 49.96           O  
-ATOM  12019  N   VAL C 595     -33.191  25.649-130.365  1.00 19.91           N  
-ATOM  12020  CA  VAL C 595     -32.193  25.085-129.461  1.00 17.15           C  
-ATOM  12021  C   VAL C 595     -32.037  25.990-128.248  1.00 19.17           C  
-ATOM  12022  O   VAL C 595     -31.890  27.204-128.381  1.00 17.50           O  
-ATOM  12023  CB  VAL C 595     -30.828  24.898-130.143  1.00 16.59           C  
-ATOM  12024  CG1 VAL C 595     -29.822  24.313-129.167  1.00 15.75           C  
-ATOM  12025  CG2 VAL C 595     -30.970  23.997-131.339  1.00 20.42           C  
-ATOM  12026  N   VAL C 596     -32.065  25.390-127.063  1.00 22.20           N  
-ATOM  12027  CA  VAL C 596     -32.164  26.149-125.824  1.00 23.83           C  
-ATOM  12028  C   VAL C 596     -31.179  25.668-124.756  1.00 23.67           C  
-ATOM  12029  O   VAL C 596     -31.217  24.512-124.337  1.00 17.44           O  
-ATOM  12030  CB  VAL C 596     -33.601  26.076-125.265  1.00 20.67           C  
-ATOM  12031  CG1 VAL C 596     -33.642  26.549-123.840  1.00 13.42           C  
-ATOM  12032  CG2 VAL C 596     -34.548  26.893-126.132  1.00 22.94           C  
-ATOM  12033  N   GLY C 597     -30.301  26.564-124.316  1.00 20.44           N  
-ATOM  12034  CA  GLY C 597     -29.340  26.241-123.277  1.00 14.23           C  
-ATOM  12035  C   GLY C 597     -28.109  25.532-123.808  1.00 16.77           C  
-ATOM  12036  O   GLY C 597     -27.440  24.797-123.083  1.00 15.06           O  
-ATOM  12037  N   TYR C 598     -27.806  25.751-125.082  1.00 17.47           N  
-ATOM  12038  CA  TYR C 598     -26.629  25.146-125.687  1.00 19.47           C  
-ATOM  12039  C   TYR C 598     -25.387  25.959-125.351  1.00 18.76           C  
-ATOM  12040  O   TYR C 598     -25.212  27.073-125.844  1.00 14.34           O  
-ATOM  12041  CB  TYR C 598     -26.798  25.031-127.203  1.00 21.89           C  
-ATOM  12042  CG  TYR C 598     -25.761  24.162-127.880  1.00 14.84           C  
-ATOM  12043  CD1 TYR C 598     -25.353  22.965-127.310  1.00 18.98           C  
-ATOM  12044  CD2 TYR C 598     -25.208  24.529-129.100  1.00 14.90           C  
-ATOM  12045  CE1 TYR C 598     -24.412  22.163-127.929  1.00 21.87           C  
-ATOM  12046  CE2 TYR C 598     -24.270  23.733-129.728  1.00 16.31           C  
-ATOM  12047  CZ  TYR C 598     -23.875  22.551-129.137  1.00 21.10           C  
-ATOM  12048  OH  TYR C 598     -22.941  21.750-129.752  1.00 22.64           O  
-ATOM  12049  N   VAL C 599     -24.536  25.398-124.496  1.00 23.63           N  
-ATOM  12050  CA  VAL C 599     -23.288  26.047-124.109  1.00 17.17           C  
-ATOM  12051  C   VAL C 599     -22.098  25.140-124.397  1.00 15.51           C  
-ATOM  12052  O   VAL C 599     -21.537  24.549-123.478  1.00 18.34           O  
-ATOM  12053  CB  VAL C 599     -23.275  26.416-122.611  1.00 14.75           C  
-ATOM  12054  CG1 VAL C 599     -22.498  27.705-122.391  1.00 19.50           C  
-ATOM  12055  CG2 VAL C 599     -24.692  26.549-122.078  1.00 15.74           C  
-ATOM  12056  N   PRO C 600     -21.709  25.022-125.677  1.00 16.25           N  
-ATOM  12057  CA  PRO C 600     -20.620  24.116-126.055  1.00 21.70           C  
-ATOM  12058  C   PRO C 600     -19.237  24.748-125.931  1.00 28.64           C  
-ATOM  12059  O   PRO C 600     -19.124  25.956-125.705  1.00 31.60           O  
-ATOM  12060  CB  PRO C 600     -20.930  23.810-127.517  1.00 17.16           C  
-ATOM  12061  CG  PRO C 600     -21.538  25.075-128.013  1.00 16.26           C  
-ATOM  12062  CD  PRO C 600     -22.322  25.655-126.857  1.00 15.03           C  
-ATOM  12063  N   HIS C 601     -18.198  23.932-126.074  1.00 21.16           N  
-ATOM  12064  CA  HIS C 601     -16.838  24.445-126.152  1.00 26.39           C  
-ATOM  12065  C   HIS C 601     -16.580  24.987-127.551  1.00 37.49           C  
-ATOM  12066  O   HIS C 601     -17.440  24.894-128.427  1.00 52.35           O  
-ATOM  12067  CB  HIS C 601     -15.822  23.358-125.809  1.00 23.54           C  
-ATOM  12068  CG  HIS C 601     -15.813  22.976-124.362  1.00 19.58           C  
-ATOM  12069  ND1 HIS C 601     -14.851  23.420-123.482  1.00 17.71           N  
-ATOM  12070  CD2 HIS C 601     -16.650  22.194-123.642  1.00 19.73           C  
-ATOM  12071  CE1 HIS C 601     -15.095  22.926-122.281  1.00 21.05           C  
-ATOM  12072  NE2 HIS C 601     -16.181  22.179-122.351  1.00 16.08           N  
-ATOM  12073  N   GLY C 602     -15.394  25.549-127.759  1.00 32.33           N  
-ATOM  12074  CA  GLY C 602     -15.039  26.117-129.047  1.00 49.17           C  
-ATOM  12075  C   GLY C 602     -15.005  25.083-130.157  1.00 61.11           C  
-ATOM  12076  O   GLY C 602     -14.898  23.885-129.896  1.00 56.36           O  
-ATOM  12077  N   ARG C 603     -15.104  25.544-131.400  1.00 71.11           N  
-ATOM  12078  CA  ARG C 603     -15.012  24.646-132.544  1.00 65.38           C  
-ATOM  12079  C   ARG C 603     -13.605  24.068-132.670  1.00 67.08           C  
-ATOM  12080  O   ARG C 603     -12.622  24.701-132.279  1.00 58.09           O  
-ATOM  12081  CB  ARG C 603     -15.396  25.365-133.840  1.00 63.36           C  
-ATOM  12082  CG  ARG C 603     -16.895  25.531-134.057  1.00 65.48           C  
-ATOM  12083  CD  ARG C 603     -17.184  26.014-135.474  1.00 65.87           C  
-ATOM  12084  NE  ARG C 603     -18.613  26.177-135.738  1.00 75.97           N  
-ATOM  12085  CZ  ARG C 603     -19.399  25.224-136.231  1.00 74.84           C  
-ATOM  12086  NH1 ARG C 603     -18.901  24.026-136.513  1.00 54.25           N  
-ATOM  12087  NH2 ARG C 603     -20.687  25.468-136.442  1.00 54.79           N  
-ATOM  12088  N   ILE C 604     -13.521  22.857-133.208  1.00 67.16           N  
-ATOM  12089  CA  ILE C 604     -12.237  22.226-133.482  1.00 69.14           C  
-ATOM  12090  C   ILE C 604     -12.098  21.950-134.972  1.00 68.06           C  
-ATOM  12091  O   ILE C 604     -12.892  21.209-135.552  1.00 69.76           O  
-ATOM  12092  CB  ILE C 604     -12.065  20.911-132.702  1.00 63.36           C  
-ATOM  12093  CG1 ILE C 604     -11.866  21.196-131.213  1.00 58.06           C  
-ATOM  12094  CG2 ILE C 604     -10.881  20.128-133.241  1.00 56.60           C  
-ATOM  12095  CD1 ILE C 604     -11.548  19.963-130.397  1.00 46.09           C  
-ATOM  12096  N   GLN C 605     -11.089  22.556-135.587  1.00 65.35           N  
-ATOM  12097  CA  GLN C 605     -10.862  22.385-137.015  1.00 73.88           C  
-ATOM  12098  C   GLN C 605     -10.408  20.969-137.347  1.00 74.49           C  
-ATOM  12099  O   GLN C 605      -9.339  20.529-136.926  1.00 68.80           O  
-ATOM  12100  CB  GLN C 605      -9.835  23.400-137.522  1.00 66.13           C  
-ATOM  12101  CG  GLN C 605     -10.457  24.615-138.190  1.00 66.15           C  
-ATOM  12102  CD  GLN C 605     -11.250  24.252-139.434  1.00 80.00           C  
-ATOM  12103  OE1 GLN C 605     -10.952  23.265-140.110  1.00 81.41           O  
-ATOM  12104  NE2 GLN C 605     -12.270  25.047-139.740  1.00 69.99           N  
-ATOM  12105  N   MET C 606     -11.240  20.261-138.102  1.00 68.97           N  
-ATOM  12106  CA  MET C 606     -10.907  18.925-138.578  1.00 65.10           C  
-ATOM  12107  C   MET C 606     -11.328  18.772-140.033  1.00 70.69           C  
-ATOM  12108  O   MET C 606     -12.517  18.789-140.353  1.00 70.76           O  
-ATOM  12109  CB  MET C 606     -11.570  17.855-137.709  1.00 62.95           C  
-ATOM  12110  CG  MET C 606     -10.909  17.667-136.350  1.00 77.04           C  
-ATOM  12111  SD  MET C 606     -11.745  16.452-135.311  1.00 74.02           S  
-ATOM  12112  CE  MET C 606     -13.264  17.322-134.947  1.00 64.84           C  
-ATOM  12113  N   GLU C 607     -10.342  18.631-140.913  1.00 73.80           N  
-ATOM  12114  CA  GLU C 607     -10.598  18.527-142.344  1.00 72.46           C  
-ATOM  12115  C   GLU C 607     -11.284  17.216-142.702  1.00 76.44           C  
-ATOM  12116  O   GLU C 607     -11.049  16.183-142.073  1.00 72.07           O  
-ATOM  12117  CB  GLU C 607      -9.295  18.664-143.132  1.00 72.22           C  
-ATOM  12118  CG  GLU C 607      -8.643  20.031-143.017  1.00 81.03           C  
-ATOM  12119  CD  GLU C 607      -7.412  20.162-143.892  1.00 95.05           C  
-ATOM  12120  OE1 GLU C 607      -6.833  21.267-143.942  1.00 94.78           O  
-ATOM  12121  OE2 GLU C 607      -7.025  19.159-144.530  1.00 91.84           O  
-ATOM  12122  N   MET C 608     -12.133  17.269-143.721  1.00 82.70           N  
-ATOM  12123  CA  MET C 608     -12.860  16.094-144.179  1.00 84.46           C  
-ATOM  12124  C   MET C 608     -11.975  15.196-145.036  1.00 78.48           C  
-ATOM  12125  O   MET C 608     -11.356  15.657-145.997  1.00 68.96           O  
-ATOM  12126  CB  MET C 608     -14.102  16.512-144.973  1.00 84.05           C  
-ATOM  12127  CG  MET C 608     -15.023  15.362-145.346  1.00 72.59           C  
-ATOM  12128  SD  MET C 608     -16.034  15.723-146.796  1.00 86.08           S  
-ATOM  12129  CE  MET C 608     -16.733  17.309-146.344  1.00 93.11           C  
-ATOM  12130  N   ALA C 609     -11.908  13.917-144.680  1.00 76.86           N  
-ATOM  12131  CA  ALA C 609     -11.254  12.936-145.535  1.00 72.48           C  
-ATOM  12132  C   ALA C 609     -12.049  12.823-146.831  1.00 81.30           C  
-ATOM  12133  O   ALA C 609     -13.163  12.296-146.849  1.00 85.83           O  
-ATOM  12134  CB  ALA C 609     -11.147  11.593-144.841  1.00 60.59           C  
-ATOM  12135  N   VAL C 610     -11.458  13.331-147.907  1.00 79.67           N  
-ATOM  12136  CA  VAL C 610     -12.140  13.532-149.182  1.00 76.10           C  
-ATOM  12137  C   VAL C 610     -12.571  12.244-149.886  1.00 79.43           C  
-ATOM  12138  O   VAL C 610     -12.809  12.243-151.095  1.00 79.06           O  
-ATOM  12139  CB  VAL C 610     -11.244  14.334-150.147  1.00 83.46           C  
-ATOM  12140  CG1 VAL C 610     -11.975  15.568-150.646  1.00 76.39           C  
-ATOM  12141  CG2 VAL C 610      -9.938  14.724-149.458  1.00 86.33           C  
-ATOM  12142  OXT VAL C 610     -12.699  11.178-149.291  1.00 77.01           O  
-TER   12143      VAL C 610                                                      
-ATOM  12144  N   LYS D   3      -6.612 -25.449 -92.372  1.00 80.44           N  
-ATOM  12145  CA  LYS D   3      -5.938 -26.456 -93.188  1.00 89.23           C  
-ATOM  12146  C   LYS D   3      -6.717 -26.798 -94.463  1.00 89.35           C  
-ATOM  12147  O   LYS D   3      -7.097 -27.953 -94.665  1.00 69.39           O  
-ATOM  12148  CB  LYS D   3      -5.719 -27.730 -92.368  1.00 84.50           C  
-ATOM  12149  CG  LYS D   3      -5.213 -27.490 -90.953  1.00 68.09           C  
-ATOM  12150  CD  LYS D   3      -6.098 -28.180 -89.924  1.00 74.63           C  
-ATOM  12151  CE  LYS D   3      -7.403 -27.428 -89.717  1.00 71.98           C  
-ATOM  12152  NZ  LYS D   3      -7.175 -26.090 -89.100  1.00 66.16           N  
-ATOM  12153  N   PRO D   4      -6.954 -25.800 -95.335  1.00 91.53           N  
-ATOM  12154  CA  PRO D   4      -7.747 -26.063 -96.542  1.00 78.79           C  
-ATOM  12155  C   PRO D   4      -6.957 -26.800 -97.627  1.00 77.20           C  
-ATOM  12156  O   PRO D   4      -5.731 -26.699 -97.686  1.00 70.70           O  
-ATOM  12157  CB  PRO D   4      -8.140 -24.657 -97.025  1.00 73.00           C  
-ATOM  12158  CG  PRO D   4      -7.692 -23.701 -95.937  1.00 71.90           C  
-ATOM  12159  CD  PRO D   4      -6.560 -24.386 -95.251  1.00 77.31           C  
-ATOM  12160  N   VAL D   5      -7.668 -27.537 -98.475  1.00 77.25           N  
-ATOM  12161  CA  VAL D   5      -7.060 -28.304 -99.559  1.00 63.24           C  
-ATOM  12162  C   VAL D   5      -7.788 -28.026-100.875  1.00 69.80           C  
-ATOM  12163  O   VAL D   5      -9.012 -27.889-100.892  1.00 69.99           O  
-ATOM  12164  CB  VAL D   5      -7.095 -29.822 -99.263  1.00 55.33           C  
-ATOM  12165  CG1 VAL D   5      -6.385 -30.604-100.355  1.00 56.57           C  
-ATOM  12166  CG2 VAL D   5      -6.486 -30.119 -97.903  1.00 60.96           C  
-ATOM  12167  N   CYS D   6      -7.040 -27.936-101.973  1.00 59.57           N  
-ATOM  12168  CA  CYS D   6      -7.640 -27.728-103.289  1.00 56.45           C  
-ATOM  12169  C   CYS D   6      -7.195 -28.790-104.290  1.00 52.96           C  
-ATOM  12170  O   CYS D   6      -6.014 -29.132-104.356  1.00 51.18           O  
-ATOM  12171  CB  CYS D   6      -7.294 -26.338-103.824  1.00 60.42           C  
-ATOM  12172  SG  CYS D   6      -8.009 -24.975-102.880  1.00 74.38           S  
-ATOM  12173  N   LEU D   7      -8.143 -29.308-105.068  1.00 48.78           N  
-ATOM  12174  CA  LEU D   7      -7.831 -30.295-106.098  1.00 39.62           C  
-ATOM  12175  C   LEU D   7      -7.693 -29.632-107.463  1.00 44.50           C  
-ATOM  12176  O   LEU D   7      -8.567 -28.873-107.881  1.00 46.11           O  
-ATOM  12177  CB  LEU D   7      -8.907 -31.382-106.160  1.00 32.35           C  
-ATOM  12178  CG  LEU D   7      -9.247 -32.156-104.885  1.00 37.49           C  
-ATOM  12179  CD1 LEU D   7     -10.109 -33.371-105.208  1.00 29.33           C  
-ATOM  12180  CD2 LEU D   7      -7.988 -32.570-104.148  1.00 45.49           C  
-ATOM  12181  N   VAL D   8      -6.595 -29.920-108.155  1.00 44.87           N  
-ATOM  12182  CA  VAL D   8      -6.369 -29.384-109.496  1.00 35.93           C  
-ATOM  12183  C   VAL D   8      -6.412 -30.507-110.530  1.00 43.89           C  
-ATOM  12184  O   VAL D   8      -5.581 -31.417-110.509  1.00 43.43           O  
-ATOM  12185  CB  VAL D   8      -5.025 -28.640-109.593  1.00 31.41           C  
-ATOM  12186  CG1 VAL D   8      -4.868 -28.005-110.964  1.00 40.77           C  
-ATOM  12187  CG2 VAL D   8      -4.930 -27.581-108.508  1.00 39.39           C  
-ATOM  12188  N   VAL D   9      -7.385 -30.435-111.436  1.00 46.86           N  
-ATOM  12189  CA  VAL D   9      -7.657 -31.529-112.367  1.00 38.75           C  
-ATOM  12190  C   VAL D   9      -7.947 -31.071-113.792  1.00 32.15           C  
-ATOM  12191  O   VAL D   9      -8.297 -29.915-114.032  1.00 38.21           O  
-ATOM  12192  CB  VAL D   9      -8.865 -32.365-111.904  1.00 34.05           C  
-ATOM  12193  CG1 VAL D   9      -8.486 -33.277-110.759  1.00 38.27           C  
-ATOM  12194  CG2 VAL D   9     -10.002 -31.451-111.504  1.00 32.28           C  
-ATOM  12195  N   ALA D  10      -7.806 -32.004-114.729  1.00 30.62           N  
-ATOM  12196  CA  ALA D  10      -8.240 -31.812-116.108  1.00 30.95           C  
-ATOM  12197  C   ALA D  10      -8.908 -33.093-116.596  1.00 35.49           C  
-ATOM  12198  O   ALA D  10      -8.235 -34.092-116.854  1.00 38.63           O  
-ATOM  12199  CB  ALA D  10      -7.068 -31.438-117.001  1.00 32.65           C  
-ATOM  12200  N   MET D  11     -10.232 -33.066-116.716  1.00 29.38           N  
-ATOM  12201  CA  MET D  11     -10.986 -34.279-117.014  1.00 23.11           C  
-ATOM  12202  C   MET D  11     -11.953 -34.133-118.192  1.00 29.44           C  
-ATOM  12203  O   MET D  11     -12.423 -33.037-118.502  1.00 33.63           O  
-ATOM  12204  CB  MET D  11     -11.758 -34.725-115.771  1.00 21.07           C  
-ATOM  12205  CG  MET D  11     -12.877 -33.780-115.365  1.00 26.92           C  
-ATOM  12206  SD  MET D  11     -13.698 -34.267-113.835  1.00 37.87           S  
-ATOM  12207  CE  MET D  11     -12.520 -33.706-112.611  1.00 22.63           C  
-ATOM  12208  N   THR D  12     -12.236 -35.260-118.840  1.00 29.11           N  
-ATOM  12209  CA  THR D  12     -13.223 -35.348-119.913  1.00 22.71           C  
-ATOM  12210  C   THR D  12     -14.637 -35.242-119.325  1.00 26.28           C  
-ATOM  12211  O   THR D  12     -14.784 -35.174-118.104  1.00 28.62           O  
-ATOM  12212  CB  THR D  12     -13.062 -36.672-120.692  1.00 21.95           C  
-ATOM  12213  OG1 THR D  12     -13.539 -37.764-119.896  1.00 23.45           O  
-ATOM  12214  CG2 THR D  12     -11.603 -36.905-121.047  1.00 25.38           C  
-ATOM  12215  N   PRO D  13     -15.683 -35.202-120.176  1.00 25.61           N  
-ATOM  12216  CA  PRO D  13     -17.018 -35.203-119.562  1.00 23.52           C  
-ATOM  12217  C   PRO D  13     -17.329 -36.489-118.800  1.00 21.83           C  
-ATOM  12218  O   PRO D  13     -18.113 -36.459-117.854  1.00 20.50           O  
-ATOM  12219  CB  PRO D  13     -17.957 -35.050-120.760  1.00 24.65           C  
-ATOM  12220  CG  PRO D  13     -17.143 -34.355-121.778  1.00 30.00           C  
-ATOM  12221  CD  PRO D  13     -15.755 -34.902-121.618  1.00 23.37           C  
-ATOM  12222  N   LYS D  14     -16.717 -37.598-119.205  1.00 26.35           N  
-ATOM  12223  CA  LYS D  14     -16.914 -38.871-118.519  1.00 21.49           C  
-ATOM  12224  C   LYS D  14     -15.923 -39.035-117.368  1.00 25.15           C  
-ATOM  12225  O   LYS D  14     -15.646 -40.154-116.935  1.00 22.77           O  
-ATOM  12226  CB  LYS D  14     -16.776 -40.040-119.495  1.00 22.61           C  
-ATOM  12227  CG  LYS D  14     -17.889 -40.144-120.529  1.00 26.10           C  
-ATOM  12228  CD  LYS D  14     -17.658 -41.339-121.448  1.00 34.49           C  
-ATOM  12229  CE  LYS D  14     -18.777 -41.501-122.464  1.00 35.49           C  
-ATOM  12230  NZ  LYS D  14     -18.549 -42.679-123.347  1.00 26.96           N  
-ATOM  12231  N   ARG D  15     -15.391 -37.909-116.893  1.00 24.15           N  
-ATOM  12232  CA  ARG D  15     -14.476 -37.857-115.751  1.00 24.93           C  
-ATOM  12233  C   ARG D  15     -13.167 -38.617-115.977  1.00 33.00           C  
-ATOM  12234  O   ARG D  15     -12.490 -38.990-115.018  1.00 37.27           O  
-ATOM  12235  CB  ARG D  15     -15.166 -38.390-114.490  1.00 22.37           C  
-ATOM  12236  CG  ARG D  15     -16.414 -37.629-114.099  1.00 21.17           C  
-ATOM  12237  CD  ARG D  15     -16.920 -38.044-112.725  1.00 24.68           C  
-ATOM  12238  NE  ARG D  15     -17.954 -39.072-112.797  1.00 29.48           N  
-ATOM  12239  CZ  ARG D  15     -17.734 -40.374-112.645  1.00 33.88           C  
-ATOM  12240  NH1 ARG D  15     -18.744 -41.231-112.727  1.00 34.65           N  
-ATOM  12241  NH2 ARG D  15     -16.509 -40.822-112.408  1.00 30.07           N  
-ATOM  12242  N   GLY D  16     -12.807 -38.837-117.237  1.00 25.53           N  
-ATOM  12243  CA  GLY D  16     -11.562 -39.513-117.554  1.00 24.49           C  
-ATOM  12244  C   GLY D  16     -10.380 -38.577-117.413  1.00 24.15           C  
-ATOM  12245  O   GLY D  16     -10.455 -37.424-117.831  1.00 29.81           O  
-ATOM  12246  N   ILE D  17      -9.287 -39.060-116.827  1.00 30.24           N  
-ATOM  12247  CA  ILE D  17      -8.124 -38.203-116.600  1.00 24.59           C  
-ATOM  12248  C   ILE D  17      -6.808 -38.775-117.123  1.00 25.79           C  
-ATOM  12249  O   ILE D  17      -5.816 -38.055-117.215  1.00 36.27           O  
-ATOM  12250  CB  ILE D  17      -7.937 -37.893-115.105  1.00 23.56           C  
-ATOM  12251  CG1 ILE D  17      -7.729 -39.182-114.313  1.00 28.71           C  
-ATOM  12252  CG2 ILE D  17      -9.127 -37.116-114.567  1.00 31.01           C  
-ATOM  12253  CD1 ILE D  17      -7.370 -38.952-112.859  1.00 37.12           C  
-ATOM  12254  N   GLY D  18      -6.786 -40.059-117.461  1.00 29.97           N  
-ATOM  12255  CA  GLY D  18      -5.550 -40.667-117.920  1.00 35.26           C  
-ATOM  12256  C   GLY D  18      -5.664 -42.005-118.624  1.00 33.31           C  
-ATOM  12257  O   GLY D  18      -6.703 -42.665-118.584  1.00 29.83           O  
-ATOM  12258  N   ILE D  19      -4.574 -42.403-119.274  1.00 39.38           N  
-ATOM  12259  CA  ILE D  19      -4.493 -43.699-119.934  1.00 40.06           C  
-ATOM  12260  C   ILE D  19      -3.027 -44.076-120.179  1.00 38.79           C  
-ATOM  12261  O   ILE D  19      -2.225 -43.248-120.619  1.00 30.51           O  
-ATOM  12262  CB  ILE D  19      -5.291 -43.707-121.261  1.00 23.93           C  
-ATOM  12263  CG1 ILE D  19      -5.254 -45.093-121.907  1.00 22.79           C  
-ATOM  12264  CG2 ILE D  19      -4.791 -42.623-122.210  1.00 23.62           C  
-ATOM  12265  CD1 ILE D  19      -6.152 -45.223-123.110  1.00 21.21           C  
-ATOM  12266  N   ASN D  20      -2.690 -45.326-119.868  1.00 34.65           N  
-ATOM  12267  CA  ASN D  20      -1.316 -45.822-119.949  1.00 35.68           C  
-ATOM  12268  C   ASN D  20      -0.336 -44.931-119.190  1.00 39.82           C  
-ATOM  12269  O   ASN D  20       0.748 -44.619-119.688  1.00 30.60           O  
-ATOM  12270  CB  ASN D  20      -0.879 -45.962-121.410  1.00 33.19           C  
-ATOM  12271  CG  ASN D  20      -1.550 -47.129-122.108  1.00 35.65           C  
-ATOM  12272  OD1 ASN D  20      -1.876 -48.136-121.481  1.00 48.19           O  
-ATOM  12273  ND2 ASN D  20      -1.757 -47.000-123.414  1.00 33.39           N  
-ATOM  12274  N   ASN D  21      -0.737 -44.531-117.985  1.00 41.42           N  
-ATOM  12275  CA  ASN D  21       0.049 -43.639-117.138  1.00 36.26           C  
-ATOM  12276  C   ASN D  21       0.481 -42.369-117.871  1.00 42.13           C  
-ATOM  12277  O   ASN D  21       1.629 -41.933-117.769  1.00 45.43           O  
-ATOM  12278  CB  ASN D  21       1.272 -44.371-116.588  1.00 36.26           C  
-ATOM  12279  CG  ASN D  21       1.507 -44.080-115.123  1.00 51.68           C  
-ATOM  12280  OD1 ASN D  21       0.773 -44.563-114.261  1.00 58.13           O  
-ATOM  12281  ND2 ASN D  21       2.534 -43.290-114.832  1.00 59.03           N  
-ATOM  12282  N   GLY D  22      -0.455 -41.784-118.612  1.00 37.04           N  
-ATOM  12283  CA  GLY D  22      -0.201 -40.564-119.352  1.00 36.49           C  
-ATOM  12284  C   GLY D  22      -1.485 -39.791-119.577  1.00 32.69           C  
-ATOM  12285  O   GLY D  22      -2.529 -40.137-119.030  1.00 26.51           O  
-ATOM  12286  N   LEU D  23      -1.410 -38.743-120.388  1.00 28.16           N  
-ATOM  12287  CA  LEU D  23      -2.572 -37.907-120.652  1.00 26.86           C  
-ATOM  12288  C   LEU D  23      -3.346 -38.414-121.863  1.00 25.39           C  
-ATOM  12289  O   LEU D  23      -2.747 -38.827-122.856  1.00 25.11           O  
-ATOM  12290  CB  LEU D  23      -2.143 -36.454-120.858  1.00 36.13           C  
-ATOM  12291  CG  LEU D  23      -1.451 -35.826-119.648  1.00 25.88           C  
-ATOM  12292  CD1 LEU D  23      -1.040 -34.392-119.941  1.00 35.87           C  
-ATOM  12293  CD2 LEU D  23      -2.357 -35.893-118.429  1.00 25.42           C  
-ATOM  12294  N   PRO D  24      -4.685 -38.383-121.779  1.00 22.19           N  
-ATOM  12295  CA  PRO D  24      -5.586 -38.884-122.821  1.00 26.31           C  
-ATOM  12296  C   PRO D  24      -5.605 -37.987-124.052  1.00 28.17           C  
-ATOM  12297  O   PRO D  24      -5.749 -38.468-125.176  1.00 26.69           O  
-ATOM  12298  CB  PRO D  24      -6.960 -38.877-122.138  1.00 23.94           C  
-ATOM  12299  CG  PRO D  24      -6.692 -38.633-120.684  1.00 25.22           C  
-ATOM  12300  CD  PRO D  24      -5.434 -37.847-120.633  1.00 24.27           C  
-ATOM  12301  N   TRP D  25      -5.459 -36.688-123.825  1.00 25.40           N  
-ATOM  12302  CA  TRP D  25      -5.582 -35.691-124.878  1.00 23.64           C  
-ATOM  12303  C   TRP D  25      -4.227 -35.088-125.230  1.00 24.88           C  
-ATOM  12304  O   TRP D  25      -3.315 -35.089-124.403  1.00 23.18           O  
-ATOM  12305  CB  TRP D  25      -6.556 -34.595-124.439  1.00 29.62           C  
-ATOM  12306  CG  TRP D  25      -6.738 -34.547-122.950  1.00 38.08           C  
-ATOM  12307  CD1 TRP D  25      -7.761 -35.097-122.229  1.00 37.33           C  
-ATOM  12308  CD2 TRP D  25      -5.865 -33.933-121.999  1.00 32.66           C  
-ATOM  12309  NE1 TRP D  25      -7.582 -34.857-120.889  1.00 23.15           N  
-ATOM  12310  CE2 TRP D  25      -6.422 -34.142-120.721  1.00 35.08           C  
-ATOM  12311  CE3 TRP D  25      -4.663 -33.221-122.101  1.00 32.87           C  
-ATOM  12312  CZ2 TRP D  25      -5.826 -33.669-119.558  1.00 53.60           C  
-ATOM  12313  CZ3 TRP D  25      -4.070 -32.749-120.943  1.00 44.49           C  
-ATOM  12314  CH2 TRP D  25      -4.652 -32.975-119.689  1.00 64.40           C  
-ATOM  12315  N   PRO D  26      -4.085 -34.579-126.465  1.00 22.96           N  
-ATOM  12316  CA  PRO D  26      -2.869 -33.862-126.863  1.00 19.50           C  
-ATOM  12317  C   PRO D  26      -2.611 -32.636-125.991  1.00 35.42           C  
-ATOM  12318  O   PRO D  26      -3.480 -32.238-125.212  1.00 41.80           O  
-ATOM  12319  CB  PRO D  26      -3.153 -33.456-128.313  1.00 18.90           C  
-ATOM  12320  CG  PRO D  26      -4.630 -33.588-128.479  1.00 25.66           C  
-ATOM  12321  CD  PRO D  26      -5.030 -34.710-127.585  1.00 25.74           C  
-ATOM  12322  N   HIS D  27      -1.428 -32.047-126.136  1.00 31.70           N  
-ATOM  12323  CA  HIS D  27      -0.961 -30.995-125.236  1.00 33.47           C  
-ATOM  12324  C   HIS D  27      -1.917 -29.805-125.145  1.00 36.75           C  
-ATOM  12325  O   HIS D  27      -2.287 -29.213-126.160  1.00 35.11           O  
-ATOM  12326  CB  HIS D  27       0.420 -30.514-125.680  1.00 35.79           C  
-ATOM  12327  CG  HIS D  27       1.218 -29.877-124.586  1.00 28.46           C  
-ATOM  12328  ND1 HIS D  27       1.232 -28.516-124.370  1.00 27.23           N  
-ATOM  12329  CD2 HIS D  27       2.026 -30.417-123.645  1.00 32.26           C  
-ATOM  12330  CE1 HIS D  27       2.017 -28.245-123.343  1.00 40.58           C  
-ATOM  12331  NE2 HIS D  27       2.512 -29.380-122.885  1.00 40.19           N  
-ATOM  12332  N   LEU D  28      -2.315 -29.465-123.921  1.00 37.82           N  
-ATOM  12333  CA  LEU D  28      -3.174 -28.309-123.679  1.00 32.03           C  
-ATOM  12334  C   LEU D  28      -2.381 -27.163-123.045  1.00 37.97           C  
-ATOM  12335  O   LEU D  28      -2.290 -27.038-121.817  1.00 42.04           O  
-ATOM  12336  CB  LEU D  28      -4.361 -28.697-122.799  1.00 28.34           C  
-ATOM  12337  CG  LEU D  28      -5.220 -29.848-123.329  1.00 28.93           C  
-ATOM  12338  CD1 LEU D  28      -6.438 -30.062-122.447  1.00 27.11           C  
-ATOM  12339  CD2 LEU D  28      -5.637 -29.593-124.767  1.00 26.77           C  
-ATOM  12340  N   THR D  29      -1.815 -26.329-123.914  1.00 36.26           N  
-ATOM  12341  CA  THR D  29      -0.909 -25.255-123.526  1.00 34.56           C  
-ATOM  12342  C   THR D  29      -1.504 -24.321-122.478  1.00 38.85           C  
-ATOM  12343  O   THR D  29      -0.903 -24.106-121.422  1.00 47.16           O  
-ATOM  12344  CB  THR D  29      -0.496 -24.416-124.748  1.00 30.67           C  
-ATOM  12345  OG1 THR D  29       0.061 -25.272-125.754  1.00 27.29           O  
-ATOM  12346  CG2 THR D  29       0.525 -23.364-124.350  1.00 31.53           C  
-ATOM  12347  N   THR D  30      -2.677 -23.767-122.772  1.00 29.22           N  
-ATOM  12348  CA  THR D  30      -3.325 -22.828-121.864  1.00 30.44           C  
-ATOM  12349  C   THR D  30      -3.650 -23.497-120.535  1.00 34.01           C  
-ATOM  12350  O   THR D  30      -3.574 -22.871-119.479  1.00 38.77           O  
-ATOM  12351  CB  THR D  30      -4.614 -22.250-122.477  1.00 29.89           C  
-ATOM  12352  OG1 THR D  30      -4.315 -21.628-123.733  1.00 45.93           O  
-ATOM  12353  CG2 THR D  30      -5.244 -21.227-121.548  1.00 36.46           C  
-ATOM  12354  N   ASP D  31      -4.005 -24.776-120.595  1.00 38.96           N  
-ATOM  12355  CA  ASP D  31      -4.281 -25.545-119.389  1.00 32.44           C  
-ATOM  12356  C   ASP D  31      -3.026 -25.659-118.538  1.00 37.21           C  
-ATOM  12357  O   ASP D  31      -3.097 -25.577-117.313  1.00 46.15           O  
-ATOM  12358  CB  ASP D  31      -4.809 -26.935-119.734  1.00 33.90           C  
-ATOM  12359  CG  ASP D  31      -4.970 -27.820-118.511  1.00 34.42           C  
-ATOM  12360  OD1 ASP D  31      -5.576 -27.370-117.516  1.00 27.49           O  
-ATOM  12361  OD2 ASP D  31      -4.480 -28.967-118.546  1.00 43.81           O  
-ATOM  12362  N   PHE D  32      -1.875 -25.837-119.181  1.00 40.92           N  
-ATOM  12363  CA  PHE D  32      -0.620 -25.895-118.433  1.00 41.81           C  
-ATOM  12364  C   PHE D  32      -0.251 -24.538-117.842  1.00 37.51           C  
-ATOM  12365  O   PHE D  32       0.187 -24.455-116.691  1.00 37.90           O  
-ATOM  12366  CB  PHE D  32       0.515 -26.421-119.310  1.00 43.77           C  
-ATOM  12367  CG  PHE D  32       0.637 -27.915-119.288  1.00 47.41           C  
-ATOM  12368  CD1 PHE D  32       1.018 -28.568-118.129  1.00 57.99           C  
-ATOM  12369  CD2 PHE D  32       0.358 -28.669-120.415  1.00 49.57           C  
-ATOM  12370  CE1 PHE D  32       1.125 -29.946-118.093  1.00 53.25           C  
-ATOM  12371  CE2 PHE D  32       0.465 -30.052-120.386  1.00 54.43           C  
-ATOM  12372  CZ  PHE D  32       0.850 -30.689-119.222  1.00 42.33           C  
-ATOM  12373  N   LYS D  33      -0.431 -23.480-118.628  1.00 41.30           N  
-ATOM  12374  CA  LYS D  33      -0.210 -22.119-118.143  1.00 51.01           C  
-ATOM  12375  C   LYS D  33      -1.122 -21.808-116.961  1.00 48.10           C  
-ATOM  12376  O   LYS D  33      -0.795 -20.986-116.107  1.00 58.04           O  
-ATOM  12377  CB  LYS D  33      -0.446 -21.095-119.256  1.00 51.01           C  
-ATOM  12378  CG  LYS D  33       0.626 -21.055-120.335  1.00 55.71           C  
-ATOM  12379  CD  LYS D  33       0.293 -19.995-121.377  1.00 55.01           C  
-ATOM  12380  CE  LYS D  33       1.263 -20.020-122.546  1.00 65.49           C  
-ATOM  12381  NZ  LYS D  33       0.829 -19.090-123.627  1.00 44.01           N  
-ATOM  12382  N   HIS D  34      -2.271 -22.475-116.930  1.00 46.58           N  
-ATOM  12383  CA  HIS D  34      -3.257 -22.307-115.871  1.00 50.06           C  
-ATOM  12384  C   HIS D  34      -2.833 -23.057-114.615  1.00 46.73           C  
-ATOM  12385  O   HIS D  34      -2.895 -22.517-113.510  1.00 53.48           O  
-ATOM  12386  CB  HIS D  34      -4.628 -22.788-116.356  1.00 48.21           C  
-ATOM  12387  CG  HIS D  34      -5.588 -23.116-115.255  1.00 44.37           C  
-ATOM  12388  ND1 HIS D  34      -6.354 -22.159-114.626  1.00 46.83           N  
-ATOM  12389  CD2 HIS D  34      -5.915 -24.298-114.683  1.00 42.12           C  
-ATOM  12390  CE1 HIS D  34      -7.109 -22.738-113.709  1.00 52.44           C  
-ATOM  12391  NE2 HIS D  34      -6.862 -24.035-113.723  1.00 53.51           N  
-ATOM  12392  N   PHE D  35      -2.407 -24.304-114.800  1.00 37.75           N  
-ATOM  12393  CA  PHE D  35      -1.882 -25.135-113.721  1.00 38.00           C  
-ATOM  12394  C   PHE D  35      -0.722 -24.440-113.015  1.00 46.17           C  
-ATOM  12395  O   PHE D  35      -0.725 -24.271-111.791  1.00 53.34           O  
-ATOM  12396  CB  PHE D  35      -1.434 -26.491-114.285  1.00 33.64           C  
-ATOM  12397  CG  PHE D  35      -0.824 -27.418-113.266  1.00 39.99           C  
-ATOM  12398  CD1 PHE D  35       0.549 -27.452-113.065  1.00 46.08           C  
-ATOM  12399  CD2 PHE D  35      -1.623 -28.270-112.522  1.00 39.79           C  
-ATOM  12400  CE1 PHE D  35       1.110 -28.310-112.128  1.00 40.21           C  
-ATOM  12401  CE2 PHE D  35      -1.069 -29.128-111.589  1.00 38.01           C  
-ATOM  12402  CZ  PHE D  35       0.299 -29.149-111.391  1.00 37.64           C  
-ATOM  12403  N   SER D  36       0.261 -24.031-113.810  1.00 48.99           N  
-ATOM  12404  CA  SER D  36       1.475 -23.407-113.299  1.00 61.33           C  
-ATOM  12405  C   SER D  36       1.159 -22.153-112.492  1.00 63.30           C  
-ATOM  12406  O   SER D  36       1.717 -21.947-111.415  1.00 71.47           O  
-ATOM  12407  CB  SER D  36       2.426 -23.067-114.450  1.00 62.59           C  
-ATOM  12408  OG  SER D  36       3.779 -23.134-114.029  1.00 62.91           O  
-ATOM  12409  N   ARG D  37       0.255 -21.325-113.007  1.00 50.34           N  
-ATOM  12410  CA  ARG D  37      -0.127 -20.093-112.324  1.00 47.74           C  
-ATOM  12411  C   ARG D  37      -0.884 -20.360-111.030  1.00 51.07           C  
-ATOM  12412  O   ARG D  37      -0.536 -19.826-109.976  1.00 56.37           O  
-ATOM  12413  CB  ARG D  37      -0.975 -19.217-113.245  1.00 52.13           C  
-ATOM  12414  CG  ARG D  37      -0.211 -18.067-113.871  1.00 72.29           C  
-ATOM  12415  CD  ARG D  37       1.054 -18.549-114.560  1.00 76.67           C  
-ATOM  12416  NE  ARG D  37       1.255 -17.876-115.839  1.00 77.26           N  
-ATOM  12417  CZ  ARG D  37       1.737 -16.645-115.969  1.00 86.89           C  
-ATOM  12418  NH1 ARG D  37       1.883 -16.115-117.176  1.00 96.69           N  
-ATOM  12419  NH2 ARG D  37       2.070 -15.941-114.894  1.00 73.87           N  
-ATOM  12420  N   VAL D  38      -1.924 -21.182-111.121  1.00 55.04           N  
-ATOM  12421  CA  VAL D  38      -2.739 -21.529-109.963  1.00 53.47           C  
-ATOM  12422  C   VAL D  38      -1.899 -22.109-108.830  1.00 54.61           C  
-ATOM  12423  O   VAL D  38      -2.053 -21.722-107.673  1.00 60.26           O  
-ATOM  12424  CB  VAL D  38      -3.849 -22.539-110.344  1.00 48.78           C  
-ATOM  12425  CG1 VAL D  38      -4.377 -23.262-109.111  1.00 52.73           C  
-ATOM  12426  CG2 VAL D  38      -4.972 -21.833-111.088  1.00 48.76           C  
-ATOM  12427  N   THR D  39      -0.987 -23.014-109.168  1.00 51.90           N  
-ATOM  12428  CA  THR D  39      -0.248 -23.740-108.141  1.00 56.52           C  
-ATOM  12429  C   THR D  39       0.817 -22.908-107.414  1.00 62.37           C  
-ATOM  12430  O   THR D  39       1.412 -23.390-106.452  1.00 55.42           O  
-ATOM  12431  CB  THR D  39       0.430 -24.996-108.722  1.00 57.27           C  
-ATOM  12432  OG1 THR D  39       0.897 -24.728-110.050  1.00 61.09           O  
-ATOM  12433  CG2 THR D  39      -0.553 -26.158-108.762  1.00 40.61           C  
-ATOM  12434  N   LYS D  40       1.059 -21.670-107.841  1.00 69.56           N  
-ATOM  12435  CA  LYS D  40       2.043 -20.847-107.136  1.00 72.16           C  
-ATOM  12436  C   LYS D  40       1.639 -19.381-106.961  1.00 76.37           C  
-ATOM  12437  O   LYS D  40       1.142 -18.737-107.887  1.00 57.13           O  
-ATOM  12438  CB  LYS D  40       3.399 -20.916-107.846  1.00 72.15           C  
-ATOM  12439  CG  LYS D  40       3.402 -20.395-109.270  1.00 71.06           C  
-ATOM  12440  CD  LYS D  40       4.716 -19.704-109.595  1.00 77.03           C  
-ATOM  12441  CE  LYS D  40       4.973 -19.682-111.093  1.00 66.51           C  
-ATOM  12442  NZ  LYS D  40       3.843 -19.081-111.854  1.00 70.37           N  
-ATOM  12443  N   THR D  41       1.855 -18.875-105.749  1.00 96.80           N  
-ATOM  12444  CA  THR D  41       1.708 -17.454-105.441  1.00 97.77           C  
-ATOM  12445  C   THR D  41       2.455 -17.100-104.156  1.00 83.59           C  
-ATOM  12446  O   THR D  41       2.211 -17.685-103.097  1.00 79.55           O  
-ATOM  12447  CB  THR D  41       0.226 -17.031-105.290  1.00 87.08           C  
-ATOM  12448  OG1 THR D  41      -0.634 -18.143-105.569  1.00 82.80           O  
-ATOM  12449  CG2 THR D  41      -0.095 -15.889-106.246  1.00 73.76           C  
-ATOM  12450  N   PHE D  74       5.926 -19.995-100.163  1.00 78.88           N  
-ATOM  12451  CA  PHE D  74       5.690 -20.840-101.329  1.00 81.90           C  
-ATOM  12452  C   PHE D  74       4.492 -21.764-101.125  1.00 87.48           C  
-ATOM  12453  O   PHE D  74       4.035 -21.963 -99.999  1.00 90.39           O  
-ATOM  12454  CB  PHE D  74       6.939 -21.666-101.650  1.00 80.38           C  
-ATOM  12455  CG  PHE D  74       7.551 -22.335-100.450  1.00 84.68           C  
-ATOM  12456  CD1 PHE D  74       6.983 -23.477 -99.908  1.00 78.78           C  
-ATOM  12457  CD2 PHE D  74       8.701 -21.825 -99.871  1.00 85.28           C  
-ATOM  12458  CE1 PHE D  74       7.546 -24.093 -98.807  1.00 84.64           C  
-ATOM  12459  CE2 PHE D  74       9.270 -22.438 -98.771  1.00 86.87           C  
-ATOM  12460  CZ  PHE D  74       8.692 -23.573 -98.238  1.00 93.65           C  
-ATOM  12461  N   ASN D  75       3.993 -22.329-102.220  1.00 81.29           N  
-ATOM  12462  CA  ASN D  75       2.860 -23.247-102.165  1.00 69.34           C  
-ATOM  12463  C   ASN D  75       3.302 -24.708-102.174  1.00 70.54           C  
-ATOM  12464  O   ASN D  75       4.469 -25.013-102.426  1.00 75.15           O  
-ATOM  12465  CB  ASN D  75       1.904 -22.979-103.329  1.00 66.39           C  
-ATOM  12466  CG  ASN D  75       0.904 -21.879-103.021  1.00 67.30           C  
-ATOM  12467  OD1 ASN D  75       0.302 -21.858-101.950  1.00 73.29           O  
-ATOM  12468  ND2 ASN D  75       0.723 -20.960-103.961  1.00 65.91           N  
-ATOM  12469  N   ALA D  76       2.364 -25.608-101.898  1.00 60.84           N  
-ATOM  12470  CA  ALA D  76       2.676 -27.032-101.837  1.00 69.58           C  
-ATOM  12471  C   ALA D  76       1.820 -27.847-102.801  1.00 71.14           C  
-ATOM  12472  O   ALA D  76       0.615 -27.624-102.922  1.00 64.39           O  
-ATOM  12473  CB  ALA D  76       2.502 -27.548-100.416  1.00 66.83           C  
-ATOM  12474  N   VAL D  77       2.456 -28.792-103.486  1.00 66.35           N  
-ATOM  12475  CA  VAL D  77       1.757 -29.713-104.372  1.00 58.46           C  
-ATOM  12476  C   VAL D  77       1.963 -31.161-103.920  1.00 57.88           C  
-ATOM  12477  O   VAL D  77       3.068 -31.563-103.540  1.00 61.73           O  
-ATOM  12478  CB  VAL D  77       2.214 -29.553-105.842  1.00 55.97           C  
-ATOM  12479  CG1 VAL D  77       1.813 -28.186-106.376  1.00 50.70           C  
-ATOM  12480  CG2 VAL D  77       3.716 -29.760-105.974  1.00 51.50           C  
-ATOM  12481  N   VAL D  78       0.884 -31.936-103.948  1.00 46.43           N  
-ATOM  12482  CA  VAL D  78       0.929 -33.331-103.528  1.00 49.48           C  
-ATOM  12483  C   VAL D  78       0.462 -34.235-104.661  1.00 57.82           C  
-ATOM  12484  O   VAL D  78      -0.582 -33.994-105.268  1.00 61.71           O  
-ATOM  12485  CB  VAL D  78       0.060 -33.579-102.283  1.00 45.14           C  
-ATOM  12486  CG1 VAL D  78       0.277 -34.990-101.760  1.00 53.05           C  
-ATOM  12487  CG2 VAL D  78       0.374 -32.557-101.206  1.00 40.86           C  
-ATOM  12488  N   MET D  79       1.237 -35.276-104.943  1.00 62.05           N  
-ATOM  12489  CA  MET D  79       0.952 -36.151-106.074  1.00 59.47           C  
-ATOM  12490  C   MET D  79       1.167 -37.623-105.742  1.00 63.27           C  
-ATOM  12491  O   MET D  79       1.956 -37.968-104.859  1.00 65.96           O  
-ATOM  12492  CB  MET D  79       1.815 -35.752-107.272  1.00 60.68           C  
-ATOM  12493  CG  MET D  79       3.306 -35.721-106.974  1.00 65.97           C  
-ATOM  12494  SD  MET D  79       4.211 -34.588-108.047  1.00 65.13           S  
-ATOM  12495  CE  MET D  79       3.659 -35.148-109.653  1.00 70.53           C  
-ATOM  12496  N   GLY D  80       0.456 -38.487-106.460  1.00 67.62           N  
-ATOM  12497  CA  GLY D  80       0.550 -39.920-106.247  1.00 71.55           C  
-ATOM  12498  C   GLY D  80       1.847 -40.487-106.787  1.00 70.68           C  
-ATOM  12499  O   GLY D  80       2.654 -39.754-107.362  1.00 61.38           O  
-ATOM  12500  N   ARG D  81       2.050 -41.789-106.604  1.00 77.00           N  
-ATOM  12501  CA  ARG D  81       3.287 -42.426-107.041  1.00 84.39           C  
-ATOM  12502  C   ARG D  81       3.436 -42.357-108.554  1.00 80.43           C  
-ATOM  12503  O   ARG D  81       4.423 -41.833-109.067  1.00 73.58           O  
-ATOM  12504  CB  ARG D  81       3.353 -43.887-106.579  1.00 87.53           C  
-ATOM  12505  CG  ARG D  81       4.658 -44.582-106.983  1.00 85.18           C  
-ATOM  12506  CD  ARG D  81       4.685 -46.049-106.580  1.00 75.89           C  
-ATOM  12507  NE  ARG D  81       3.809 -46.863-107.416  1.00 77.16           N  
-ATOM  12508  CZ  ARG D  81       4.156 -47.359-108.601  1.00 76.11           C  
-ATOM  12509  NH1 ARG D  81       5.364 -47.120-109.102  1.00 76.76           N  
-ATOM  12510  NH2 ARG D  81       3.292 -48.091-109.290  1.00 72.74           N  
-ATOM  12511  N   LYS D  82       2.442 -42.878-109.262  1.00 74.84           N  
-ATOM  12512  CA  LYS D  82       2.496 -42.950-110.716  1.00 70.96           C  
-ATOM  12513  C   LYS D  82       2.449 -41.571-111.376  1.00 73.09           C  
-ATOM  12514  O   LYS D  82       2.999 -41.376-112.461  1.00 77.37           O  
-ATOM  12515  CB  LYS D  82       1.354 -43.831-111.234  1.00 67.76           C  
-ATOM  12516  CG  LYS D  82       1.638 -45.324-111.124  1.00 76.11           C  
-ATOM  12517  CD  LYS D  82       0.541 -46.059-110.370  1.00 71.01           C  
-ATOM  12518  CE  LYS D  82      -0.641 -46.382-111.268  1.00 64.06           C  
-ATOM  12519  NZ  LYS D  82      -1.637 -47.245-110.575  1.00 47.32           N  
-ATOM  12520  N   THR D  83       1.801 -40.617-110.714  1.00 72.46           N  
-ATOM  12521  CA  THR D  83       1.678 -39.262-111.245  1.00 66.85           C  
-ATOM  12522  C   THR D  83       3.044 -38.589-111.365  1.00 71.45           C  
-ATOM  12523  O   THR D  83       3.308 -37.859-112.323  1.00 66.78           O  
-ATOM  12524  CB  THR D  83       0.763 -38.386-110.363  1.00 64.64           C  
-ATOM  12525  OG1 THR D  83      -0.494 -39.047-110.165  1.00 68.65           O  
-ATOM  12526  CG2 THR D  83       0.525 -37.035-111.016  1.00 46.87           C  
-ATOM  12527  N   TRP D  84       3.907 -38.843-110.386  1.00 77.24           N  
-ATOM  12528  CA  TRP D  84       5.268 -38.318-110.389  1.00 79.29           C  
-ATOM  12529  C   TRP D  84       6.059 -38.903-111.556  1.00 78.01           C  
-ATOM  12530  O   TRP D  84       6.897 -38.227-112.159  1.00 72.03           O  
-ATOM  12531  CB  TRP D  84       5.952 -38.627-109.054  1.00 80.37           C  
-ATOM  12532  CG  TRP D  84       7.441 -38.447-109.051  1.00 79.10           C  
-ATOM  12533  CD1 TRP D  84       8.378 -39.404-109.308  1.00 77.58           C  
-ATOM  12534  CD2 TRP D  84       8.166 -37.246-108.760  1.00 63.54           C  
-ATOM  12535  NE1 TRP D  84       9.638 -38.874-109.204  1.00 68.24           N  
-ATOM  12536  CE2 TRP D  84       9.536 -37.548-108.866  1.00 59.26           C  
-ATOM  12537  CE3 TRP D  84       7.790 -35.941-108.425  1.00 72.66           C  
-ATOM  12538  CZ2 TRP D  84      10.533 -36.598-108.652  1.00 66.25           C  
-ATOM  12539  CZ3 TRP D  84       8.782 -35.000-108.206  1.00 67.14           C  
-ATOM  12540  CH2 TRP D  84      10.135 -35.333-108.324  1.00 60.16           C  
-ATOM  12541  N   GLU D  85       5.776 -40.160-111.877  1.00 71.36           N  
-ATOM  12542  CA  GLU D  85       6.447 -40.833-112.980  1.00 75.69           C  
-ATOM  12543  C   GLU D  85       5.937 -40.339-114.329  1.00 77.92           C  
-ATOM  12544  O   GLU D  85       6.690 -40.288-115.299  1.00 77.90           O  
-ATOM  12545  CB  GLU D  85       6.267 -42.347-112.863  1.00 79.30           C  
-ATOM  12546  CG  GLU D  85       7.009 -42.961-111.686  1.00 84.77           C  
-ATOM  12547  CD  GLU D  85       6.585 -44.390-111.407  1.00 85.97           C  
-ATOM  12548  OE1 GLU D  85       5.468 -44.769-111.818  1.00 80.74           O  
-ATOM  12549  OE2 GLU D  85       7.368 -45.134-110.778  1.00 75.38           O  
-ATOM  12550  N   SER D  86       4.660 -39.971-114.383  1.00 78.80           N  
-ATOM  12551  CA  SER D  86       4.054 -39.482-115.619  1.00 68.68           C  
-ATOM  12552  C   SER D  86       4.779 -38.249-116.152  1.00 67.56           C  
-ATOM  12553  O   SER D  86       4.888 -38.057-117.362  1.00 58.72           O  
-ATOM  12554  CB  SER D  86       2.573 -39.163-115.402  1.00 57.80           C  
-ATOM  12555  OG  SER D  86       1.797 -40.348-115.337  1.00 68.66           O  
-ATOM  12556  N   MET D  87       5.283 -37.423-115.242  1.00 65.98           N  
-ATOM  12557  CA  MET D  87       6.004 -36.215-115.623  1.00 64.31           C  
-ATOM  12558  C   MET D  87       7.381 -36.529-116.198  1.00 69.91           C  
-ATOM  12559  O   MET D  87       8.094 -37.391-115.680  1.00 65.15           O  
-ATOM  12560  CB  MET D  87       6.162 -35.279-114.423  1.00 71.42           C  
-ATOM  12561  CG  MET D  87       4.858 -34.798-113.814  1.00 68.40           C  
-ATOM  12562  SD  MET D  87       5.147 -33.608-112.488  1.00 68.17           S  
-ATOM  12563  CE  MET D  87       6.099 -32.364-113.356  1.00 69.40           C  
-ATOM  12564  N   PRO D  88       7.758 -35.830-117.278  1.00 76.13           N  
-ATOM  12565  CA  PRO D  88       9.131 -35.880-117.792  1.00 78.38           C  
-ATOM  12566  C   PRO D  88      10.133 -35.429-116.724  1.00 82.21           C  
-ATOM  12567  O   PRO D  88       9.788 -34.612-115.869  1.00 83.03           O  
-ATOM  12568  CB  PRO D  88       9.098 -34.919-118.990  1.00 66.83           C  
-ATOM  12569  CG  PRO D  88       7.844 -34.099-118.808  1.00 66.29           C  
-ATOM  12570  CD  PRO D  88       6.879 -35.005-118.123  1.00 68.91           C  
-ATOM  12571  N   ARG D  89      11.349 -35.966-116.775  1.00 83.19           N  
-ATOM  12572  CA  ARG D  89      12.335 -35.751-115.717  1.00 81.41           C  
-ATOM  12573  C   ARG D  89      12.730 -34.283-115.565  1.00 80.42           C  
-ATOM  12574  O   ARG D  89      12.982 -33.812-114.455  1.00 75.49           O  
-ATOM  12575  CB  ARG D  89      13.584 -36.594-115.978  1.00 75.82           C  
-ATOM  12576  CG  ARG D  89      13.294 -37.958-116.579  1.00 74.34           C  
-ATOM  12577  CD  ARG D  89      13.956 -38.102-117.941  1.00 88.31           C  
-ATOM  12578  NE  ARG D  89      13.553 -37.044-118.865  1.00 95.62           N  
-ATOM  12579  CZ  ARG D  89      12.774 -37.232-119.926  1.00 79.75           C  
-ATOM  12580  NH1 ARG D  89      12.318 -38.444-120.209  1.00 68.62           N  
-ATOM  12581  NH2 ARG D  89      12.458 -36.209-120.710  1.00 70.95           N  
-ATOM  12582  N   LYS D  90      12.775 -33.561-116.679  1.00 77.56           N  
-ATOM  12583  CA  LYS D  90      13.194 -32.162-116.664  1.00 80.23           C  
-ATOM  12584  C   LYS D  90      12.197 -31.284-115.911  1.00 85.34           C  
-ATOM  12585  O   LYS D  90      12.536 -30.188-115.464  1.00 85.96           O  
-ATOM  12586  CB  LYS D  90      13.376 -31.641-118.091  1.00 86.32           C  
-ATOM  12587  CG  LYS D  90      12.114 -31.672-118.935  1.00 84.21           C  
-ATOM  12588  CD  LYS D  90      12.374 -31.128-120.329  1.00 83.50           C  
-ATOM  12589  CE  LYS D  90      11.101 -31.095-121.156  1.00 64.91           C  
-ATOM  12590  NZ  LYS D  90      11.345 -30.548-122.518  1.00 53.67           N  
-ATOM  12591  N   PHE D  91      10.971 -31.778-115.770  1.00 88.97           N  
-ATOM  12592  CA  PHE D  91       9.918 -31.048-115.074  1.00 91.68           C  
-ATOM  12593  C   PHE D  91       9.641 -31.592-113.676  1.00 90.59           C  
-ATOM  12594  O   PHE D  91       8.996 -30.919-112.871  1.00 84.08           O  
-ATOM  12595  CB  PHE D  91       8.620 -31.083-115.883  1.00 84.14           C  
-ATOM  12596  CG  PHE D  91       8.528 -30.019-116.937  1.00 92.06           C  
-ATOM  12597  CD1 PHE D  91       8.552 -28.678-116.589  1.00 88.61           C  
-ATOM  12598  CD2 PHE D  91       8.384 -30.358-118.273  1.00 83.98           C  
-ATOM  12599  CE1 PHE D  91       8.456 -27.695-117.555  1.00 77.99           C  
-ATOM  12600  CE2 PHE D  91       8.287 -29.379-119.244  1.00 77.27           C  
-ATOM  12601  CZ  PHE D  91       8.322 -28.046-118.884  1.00 79.26           C  
-ATOM  12602  N   ARG D  92      10.128 -32.802-113.396  1.00 85.74           N  
-ATOM  12603  CA  ARG D  92       9.723 -33.545-112.199  1.00 77.61           C  
-ATOM  12604  C   ARG D  92       9.828 -32.739-110.897  1.00 91.05           C  
-ATOM  12605  O   ARG D  92       8.854 -32.669-110.147  1.00 96.01           O  
-ATOM  12606  CB  ARG D  92      10.521 -34.851-112.082  1.00 69.37           C  
-ATOM  12607  CG  ARG D  92       9.914 -36.013-112.855  1.00 76.29           C  
-ATOM  12608  CD  ARG D  92      10.211 -37.341-112.175  1.00 72.81           C  
-ATOM  12609  NE  ARG D  92      11.233 -38.118-112.869  1.00 86.56           N  
-ATOM  12610  CZ  ARG D  92      10.982 -39.213-113.580  1.00 85.90           C  
-ATOM  12611  NH1 ARG D  92      11.972 -39.861-114.178  1.00 78.11           N  
-ATOM  12612  NH2 ARG D  92       9.739 -39.663-113.687  1.00 78.75           N  
-ATOM  12613  N   PRO D  93      10.988 -32.117-110.617  1.00 87.18           N  
-ATOM  12614  CA  PRO D  93      10.894 -31.224-109.458  1.00 74.76           C  
-ATOM  12615  C   PRO D  93      10.116 -29.961-109.814  1.00 76.31           C  
-ATOM  12616  O   PRO D  93      10.707 -29.012-110.331  1.00 74.50           O  
-ATOM  12617  CB  PRO D  93      12.358 -30.898-109.131  1.00 72.09           C  
-ATOM  12618  CG  PRO D  93      13.172 -31.917-109.880  1.00 86.06           C  
-ATOM  12619  CD  PRO D  93      12.373 -32.232-111.105  1.00 88.24           C  
-ATOM  12620  N   LEU D  94       8.808 -29.969-109.560  1.00 71.53           N  
-ATOM  12621  CA  LEU D  94       7.952 -28.820-109.849  1.00 73.69           C  
-ATOM  12622  C   LEU D  94       8.495 -27.562-109.185  1.00 66.21           C  
-ATOM  12623  O   LEU D  94       8.329 -27.361-107.982  1.00 57.14           O  
-ATOM  12624  CB  LEU D  94       6.515 -29.089-109.394  1.00 70.50           C  
-ATOM  12625  CG  LEU D  94       5.671 -29.922-110.363  1.00 68.79           C  
-ATOM  12626  CD1 LEU D  94       4.366 -30.361-109.716  1.00 63.24           C  
-ATOM  12627  CD2 LEU D  94       5.402 -29.139-111.642  1.00 60.46           C  
-ATOM  12628  N   VAL D  95       9.144 -26.724-109.988  1.00 70.58           N  
-ATOM  12629  CA  VAL D  95       9.901 -25.582-109.485  1.00 77.29           C  
-ATOM  12630  C   VAL D  95       9.051 -24.552-108.741  1.00 73.94           C  
-ATOM  12631  O   VAL D  95       7.889 -24.319-109.085  1.00 61.63           O  
-ATOM  12632  CB  VAL D  95      10.648 -24.869-110.636  1.00 75.85           C  
-ATOM  12633  CG1 VAL D  95      11.730 -25.777-111.212  1.00 54.77           C  
-ATOM  12634  CG2 VAL D  95       9.672 -24.433-111.719  1.00 66.94           C  
-ATOM  12635  N   ASP D  96       9.657 -23.958-107.712  1.00 82.53           N  
-ATOM  12636  CA  ASP D  96       9.049 -22.912-106.883  1.00 74.60           C  
-ATOM  12637  C   ASP D  96       7.849 -23.397-106.068  1.00 66.06           C  
-ATOM  12638  O   ASP D  96       7.018 -22.597-105.637  1.00 60.29           O  
-ATOM  12639  CB  ASP D  96       8.640 -21.716-107.748  1.00 67.49           C  
-ATOM  12640  CG  ASP D  96       9.788 -21.189-108.586  1.00 86.05           C  
-ATOM  12641  OD1 ASP D  96      10.667 -20.500-108.023  1.00 87.19           O  
-ATOM  12642  OD2 ASP D  96       9.814 -21.463-109.806  1.00 89.33           O  
-ATOM  12643  N   ARG D  97       7.772 -24.705-105.847  1.00 57.78           N  
-ATOM  12644  CA  ARG D  97       6.712 -25.290-105.033  1.00 54.55           C  
-ATOM  12645  C   ARG D  97       7.232 -26.504-104.281  1.00 57.71           C  
-ATOM  12646  O   ARG D  97       8.043 -27.266-104.807  1.00 53.19           O  
-ATOM  12647  CB  ARG D  97       5.515 -25.686-105.898  1.00 63.46           C  
-ATOM  12648  CG  ARG D  97       4.653 -24.522-106.361  1.00 70.16           C  
-ATOM  12649  CD  ARG D  97       3.961 -24.847-107.671  1.00 53.16           C  
-ATOM  12650  NE  ARG D  97       4.907 -24.902-108.780  1.00 58.75           N  
-ATOM  12651  CZ  ARG D  97       4.631 -25.424-109.970  1.00 70.47           C  
-ATOM  12652  NH1 ARG D  97       3.435 -25.944-110.205  1.00 68.08           N  
-ATOM  12653  NH2 ARG D  97       5.552 -25.432-110.923  1.00 76.48           N  
-ATOM  12654  N   LEU D  98       6.768 -26.682-103.049  1.00 59.54           N  
-ATOM  12655  CA  LEU D  98       7.129 -27.858-102.267  1.00 67.14           C  
-ATOM  12656  C   LEU D  98       6.475 -29.080-102.902  1.00 61.99           C  
-ATOM  12657  O   LEU D  98       5.297 -29.044-103.235  1.00 59.86           O  
-ATOM  12658  CB  LEU D  98       6.693 -27.691-100.806  1.00 72.47           C  
-ATOM  12659  CG  LEU D  98       7.321 -28.560 -99.710  1.00 71.88           C  
-ATOM  12660  CD1 LEU D  98       6.717 -29.959 -99.663  1.00 52.24           C  
-ATOM  12661  CD2 LEU D  98       8.834 -28.631 -99.879  1.00 73.86           C  
-ATOM  12662  N   ASN D  99       7.237 -30.154-103.082  1.00 49.00           N  
-ATOM  12663  CA  ASN D  99       6.696 -31.358-103.705  1.00 54.17           C  
-ATOM  12664  C   ASN D  99       6.520 -32.505-102.715  1.00 54.08           C  
-ATOM  12665  O   ASN D  99       7.399 -32.765-101.894  1.00 67.19           O  
-ATOM  12666  CB  ASN D  99       7.591 -31.810-104.862  1.00 63.74           C  
-ATOM  12667  CG  ASN D  99       7.492 -30.896-106.073  1.00 68.94           C  
-ATOM  12668  OD1 ASN D  99       7.325 -29.683-105.939  1.00 57.30           O  
-ATOM  12669  ND2 ASN D  99       7.585 -31.480-107.264  1.00 65.43           N  
-ATOM  12670  N   ILE D 100       5.378 -33.184-102.790  1.00 54.83           N  
-ATOM  12671  CA  ILE D 100       5.130 -34.354-101.949  1.00 66.08           C  
-ATOM  12672  C   ILE D 100       4.574 -35.532-102.745  1.00 67.89           C  
-ATOM  12673  O   ILE D 100       3.375 -35.599-103.019  1.00 71.30           O  
-ATOM  12674  CB  ILE D 100       4.146 -34.041-100.799  1.00 61.68           C  
-ATOM  12675  CG1 ILE D 100       4.671 -32.900 -99.930  1.00 63.07           C  
-ATOM  12676  CG2 ILE D 100       3.916 -35.277 -99.938  1.00 54.08           C  
-ATOM  12677  CD1 ILE D 100       3.819 -32.622 -98.712  1.00 71.67           C  
-ATOM  12678  N   VAL D 101       5.451 -36.459-103.119  1.00 54.66           N  
-ATOM  12679  CA  VAL D 101       5.018 -37.712-103.723  1.00 55.55           C  
-ATOM  12680  C   VAL D 101       4.575 -38.645-102.608  1.00 55.09           C  
-ATOM  12681  O   VAL D 101       5.185 -38.664-101.541  1.00 61.15           O  
-ATOM  12682  CB  VAL D 101       6.137 -38.378-104.545  1.00 60.94           C  
-ATOM  12683  CG1 VAL D 101       5.598 -39.575-105.315  1.00 68.13           C  
-ATOM  12684  CG2 VAL D 101       6.758 -37.376-105.493  1.00 61.53           C  
-ATOM  12685  N   VAL D 102       3.512 -39.407-102.832  1.00 54.63           N  
-ATOM  12686  CA  VAL D 102       3.079 -40.352-101.812  1.00 59.09           C  
-ATOM  12687  C   VAL D 102       3.106 -41.793-102.319  1.00 72.99           C  
-ATOM  12688  O   VAL D 102       2.587 -42.104-103.393  1.00 83.52           O  
-ATOM  12689  CB  VAL D 102       1.668 -39.999-101.283  1.00 54.14           C  
-ATOM  12690  CG1 VAL D 102       1.702 -38.658-100.566  1.00 59.26           C  
-ATOM  12691  CG2 VAL D 102       0.654 -39.972-102.413  1.00 64.38           C  
-ATOM  12692  N   SER D 103       3.738 -42.665-101.539  1.00 75.59           N  
-ATOM  12693  CA  SER D 103       3.840 -44.083-101.876  1.00 91.07           C  
-ATOM  12694  C   SER D 103       4.396 -44.881-100.704  1.00 83.34           C  
-ATOM  12695  O   SER D 103       4.279 -44.480 -99.546  1.00 70.37           O  
-ATOM  12696  CB  SER D 103       4.724 -44.290-103.111  1.00 81.87           C  
-ATOM  12697  OG  SER D 103       4.848 -45.662-103.432  1.00 81.05           O  
-ATOM  12698  N   SER D 104       5.006 -46.017-101.020  1.00 84.83           N  
-ATOM  12699  CA  SER D 104       5.631 -46.861-100.015  1.00 76.11           C  
-ATOM  12700  C   SER D 104       6.838 -47.582-100.602  1.00 79.42           C  
-ATOM  12701  O   SER D 104       7.401 -48.476 -99.971  1.00 77.95           O  
-ATOM  12702  CB  SER D 104       4.623 -47.873 -99.462  1.00 80.23           C  
-ATOM  12703  OG  SER D 104       4.144 -48.730-100.486  1.00 67.72           O  
-ATOM  12704  N   SER D 105       7.238 -47.186-101.808  1.00 79.27           N  
-ATOM  12705  CA  SER D 105       8.289 -47.903-102.522  1.00 86.14           C  
-ATOM  12706  C   SER D 105       9.407 -47.009-103.069  1.00 77.96           C  
-ATOM  12707  O   SER D 105      10.362 -47.509-103.668  1.00 79.78           O  
-ATOM  12708  CB  SER D 105       7.675 -48.707-103.673  1.00 88.20           C  
-ATOM  12709  OG  SER D 105       6.779 -49.696-103.190  1.00 81.04           O  
-ATOM  12710  N   LEU D 106       9.309 -45.700-102.861  1.00 64.88           N  
-ATOM  12711  CA  LEU D 106      10.278 -44.785-103.464  1.00 70.98           C  
-ATOM  12712  C   LEU D 106      11.208 -44.102-102.462  1.00 67.09           C  
-ATOM  12713  O   LEU D 106      10.995 -44.160-101.250  1.00 63.23           O  
-ATOM  12714  CB  LEU D 106       9.550 -43.725-104.293  1.00 80.14           C  
-ATOM  12715  CG  LEU D 106       8.764 -44.268-105.490  1.00 95.34           C  
-ATOM  12716  CD1 LEU D 106       8.355 -43.139-106.426  1.00 71.67           C  
-ATOM  12717  CD2 LEU D 106       9.559 -45.333-106.237  1.00 86.46           C  
-ATOM  12718  N   LYS D 107      12.242 -43.456-102.997  1.00 72.91           N  
-ATOM  12719  CA  LYS D 107      13.286 -42.815-102.202  1.00 68.49           C  
-ATOM  12720  C   LYS D 107      12.725 -41.704-101.318  1.00 67.27           C  
-ATOM  12721  O   LYS D 107      13.322 -40.632-101.195  1.00 53.90           O  
-ATOM  12722  CB  LYS D 107      14.377 -42.251-103.119  1.00 65.37           C  
-ATOM  12723  CG  LYS D 107      15.760 -42.184-102.489  1.00 68.66           C  
-ATOM  12724  CD  LYS D 107      16.632 -41.150-103.182  1.00 62.90           C  
-ATOM  12725  CE  LYS D 107      16.807 -39.912-102.312  1.00 67.23           C  
-ATOM  12726  NZ  LYS D 107      15.507 -39.392-101.799  1.00 47.22           N  
-ATOM  12727  N   VAL D 126       8.283 -37.081 -99.286  1.00 23.52           N  
-ATOM  12728  CA  VAL D 126       7.715 -38.372 -99.659  1.00 47.81           C  
-ATOM  12729  C   VAL D 126       7.033 -39.040 -98.469  1.00 48.35           C  
-ATOM  12730  O   VAL D 126       7.695 -39.583 -97.585  1.00 57.19           O  
-ATOM  12731  CB  VAL D 126       8.789 -39.320-100.224  1.00 51.22           C  
-ATOM  12732  CG1 VAL D 126       8.166 -40.656-100.617  1.00 38.43           C  
-ATOM  12733  CG2 VAL D 126       9.485 -38.675-101.413  1.00 45.86           C  
-ATOM  12734  N   CYS D 127       5.705 -39.000 -98.459  1.00 45.05           N  
-ATOM  12735  CA  CYS D 127       4.928 -39.537 -97.349  1.00 43.44           C  
-ATOM  12736  C   CYS D 127       4.258 -40.855 -97.724  1.00 54.03           C  
-ATOM  12737  O   CYS D 127       4.225 -41.229 -98.895  1.00 63.30           O  
-ATOM  12738  CB  CYS D 127       3.887 -38.514 -96.901  1.00 55.69           C  
-ATOM  12739  SG  CYS D 127       4.579 -36.859 -96.681  1.00 74.66           S  
-ATOM  12740  N   ALA D 128       3.725 -41.553 -96.725  1.00 49.29           N  
-ATOM  12741  CA  ALA D 128       3.171 -42.887 -96.931  1.00 53.57           C  
-ATOM  12742  C   ALA D 128       1.669 -42.852 -97.194  1.00 63.58           C  
-ATOM  12743  O   ALA D 128       1.069 -43.864 -97.558  1.00 60.42           O  
-ATOM  12744  CB  ALA D 128       3.474 -43.771 -95.731  1.00 58.10           C  
-ATOM  12745  N   SER D 129       1.068 -41.685 -97.001  1.00 70.03           N  
-ATOM  12746  CA  SER D 129      -0.349 -41.496 -97.279  1.00 73.66           C  
-ATOM  12747  C   SER D 129      -0.665 -40.012 -97.347  1.00 75.84           C  
-ATOM  12748  O   SER D 129       0.166 -39.174 -96.999  1.00 68.66           O  
-ATOM  12749  CB  SER D 129      -1.218 -42.169 -96.212  1.00 76.25           C  
-ATOM  12750  OG  SER D 129      -1.074 -41.527 -94.956  1.00 74.79           O  
-ATOM  12751  N   LEU D 130      -1.874 -39.695 -97.797  1.00 71.33           N  
-ATOM  12752  CA  LEU D 130      -2.329 -38.310 -97.857  1.00 71.10           C  
-ATOM  12753  C   LEU D 130      -2.464 -37.671 -96.466  1.00 80.04           C  
-ATOM  12754  O   LEU D 130      -2.021 -36.533 -96.270  1.00 71.53           O  
-ATOM  12755  CB  LEU D 130      -3.658 -38.216 -98.614  1.00 67.29           C  
-ATOM  12756  CG  LEU D 130      -4.240 -36.811 -98.766  1.00 61.68           C  
-ATOM  12757  CD1 LEU D 130      -3.269 -35.905 -99.506  1.00 58.94           C  
-ATOM  12758  CD2 LEU D 130      -5.568 -36.884 -99.488  1.00 64.23           C  
-ATOM  12759  N   PRO D 131      -3.073 -38.388 -95.494  1.00 85.72           N  
-ATOM  12760  CA  PRO D 131      -3.066 -37.795 -94.152  1.00 75.20           C  
-ATOM  12761  C   PRO D 131      -1.655 -37.577 -93.620  1.00 73.02           C  
-ATOM  12762  O   PRO D 131      -1.406 -36.584 -92.940  1.00 70.06           O  
-ATOM  12763  CB  PRO D 131      -3.813 -38.832 -93.305  1.00 75.53           C  
-ATOM  12764  CG  PRO D 131      -4.681 -39.540 -94.264  1.00 72.91           C  
-ATOM  12765  CD  PRO D 131      -3.890 -39.617 -95.532  1.00 70.14           C  
-ATOM  12766  N   ALA D 132      -0.753 -38.505 -93.923  1.00 74.03           N  
-ATOM  12767  CA  ALA D 132       0.642 -38.369 -93.533  1.00 72.17           C  
-ATOM  12768  C   ALA D 132       1.266 -37.136 -94.180  1.00 76.30           C  
-ATOM  12769  O   ALA D 132       2.093 -36.459 -93.571  1.00 68.12           O  
-ATOM  12770  CB  ALA D 132       1.423 -39.627 -93.903  1.00 60.25           C  
-ATOM  12771  N   ALA D 133       0.861 -36.852 -95.413  1.00 83.52           N  
-ATOM  12772  CA  ALA D 133       1.358 -35.688 -96.127  1.00 82.53           C  
-ATOM  12773  C   ALA D 133       0.868 -34.409 -95.463  1.00 82.13           C  
-ATOM  12774  O   ALA D 133       1.634 -33.467 -95.259  1.00 79.07           O  
-ATOM  12775  CB  ALA D 133       0.931 -35.744 -97.587  1.00 75.07           C  
-ATOM  12776  N   LEU D 134      -0.412 -34.395 -95.112  1.00 74.42           N  
-ATOM  12777  CA  LEU D 134      -0.994 -33.255 -94.424  1.00 76.10           C  
-ATOM  12778  C   LEU D 134      -0.292 -33.027 -93.094  1.00 82.07           C  
-ATOM  12779  O   LEU D 134      -0.049 -31.888 -92.695  1.00 70.88           O  
-ATOM  12780  CB  LEU D 134      -2.489 -33.471 -94.207  1.00 78.71           C  
-ATOM  12781  CG  LEU D 134      -3.315 -33.679 -95.477  1.00 70.30           C  
-ATOM  12782  CD1 LEU D 134      -4.770 -33.934 -95.128  1.00 70.86           C  
-ATOM  12783  CD2 LEU D 134      -3.185 -32.480 -96.394  1.00 57.35           C  
-ATOM  12784  N   SER D 135       0.034 -34.125 -92.419  1.00 81.96           N  
-ATOM  12785  CA  SER D 135       0.755 -34.067 -91.155  1.00 73.17           C  
-ATOM  12786  C   SER D 135       2.149 -33.490 -91.358  1.00 77.21           C  
-ATOM  12787  O   SER D 135       2.610 -32.676 -90.561  1.00 79.25           O  
-ATOM  12788  CB  SER D 135       0.851 -35.456 -90.521  1.00 64.47           C  
-ATOM  12789  OG  SER D 135      -0.434 -36.018 -90.311  1.00 62.88           O  
-ATOM  12790  N   LEU D 136       2.815 -33.917 -92.427  1.00 78.71           N  
-ATOM  12791  CA  LEU D 136       4.138 -33.409 -92.767  1.00 85.34           C  
-ATOM  12792  C   LEU D 136       4.072 -31.928 -93.117  1.00 81.01           C  
-ATOM  12793  O   LEU D 136       5.053 -31.198 -92.977  1.00 67.69           O  
-ATOM  12794  CB  LEU D 136       4.737 -34.207 -93.929  1.00 82.90           C  
-ATOM  12795  CG  LEU D 136       5.753 -35.305 -93.599  1.00 87.09           C  
-ATOM  12796  CD1 LEU D 136       7.162 -34.735 -93.532  1.00 76.28           C  
-ATOM  12797  CD2 LEU D 136       5.395 -36.011 -92.300  1.00 89.03           C  
-ATOM  12798  N   LEU D 137       2.905 -31.493 -93.573  1.00 87.31           N  
-ATOM  12799  CA  LEU D 137       2.688 -30.099 -93.911  1.00 84.34           C  
-ATOM  12800  C   LEU D 137       2.376 -29.271 -92.666  1.00 79.00           C  
-ATOM  12801  O   LEU D 137       2.650 -28.072 -92.620  1.00 65.75           O  
-ATOM  12802  CB  LEU D 137       1.557 -29.975 -94.932  1.00 92.77           C  
-ATOM  12803  CG  LEU D 137       1.878 -30.360 -96.382  1.00 88.23           C  
-ATOM  12804  CD1 LEU D 137       0.649 -30.264 -97.281  1.00 83.38           C  
-ATOM  12805  CD2 LEU D 137       3.018 -29.514 -96.945  1.00 85.06           C  
-ATOM  12806  N   GLU D 138       1.802 -29.914 -91.656  1.00 88.43           N  
-ATOM  12807  CA  GLU D 138       1.418 -29.215 -90.437  1.00 87.29           C  
-ATOM  12808  C   GLU D 138       2.576 -29.094 -89.450  1.00 88.13           C  
-ATOM  12809  O   GLU D 138       2.861 -28.003 -88.954  1.00 84.48           O  
-ATOM  12810  CB  GLU D 138       0.238 -29.922 -89.773  1.00 76.34           C  
-ATOM  12811  CG  GLU D 138      -0.998 -29.041 -89.644  1.00 84.32           C  
-ATOM  12812  CD  GLU D 138      -2.177 -29.765 -89.020  1.00 89.28           C  
-ATOM  12813  OE1 GLU D 138      -1.974 -30.492 -88.026  1.00 81.74           O  
-ATOM  12814  OE2 GLU D 138      -3.309 -29.612 -89.523  1.00 79.87           O  
-ATOM  12815  N   GLU D 139       3.229 -30.219 -89.164  1.00 83.46           N  
-ATOM  12816  CA  GLU D 139       4.364 -30.251 -88.243  1.00 81.89           C  
-ATOM  12817  C   GLU D 139       5.438 -29.259 -88.674  1.00 92.86           C  
-ATOM  12818  O   GLU D 139       5.593 -28.199 -88.068  1.00 88.39           O  
-ATOM  12819  CB  GLU D 139       4.950 -31.663 -88.153  1.00 73.22           C  
-ATOM  12820  CG  GLU D 139       6.255 -31.753 -87.369  1.00 85.18           C  
-ATOM  12821  CD  GLU D 139       6.071 -31.547 -85.877  1.00 96.59           C  
-ATOM  12822  OE1 GLU D 139       5.986 -32.559 -85.150  1.00 94.71           O  
-ATOM  12823  OE2 GLU D 139       6.026 -30.381 -85.427  1.00 91.06           O  
-ATOM  12824  N   GLU D 140       6.176 -29.602 -89.723  1.00 92.52           N  
-ATOM  12825  CA  GLU D 140       7.122 -28.666 -90.308  1.00 75.13           C  
-ATOM  12826  C   GLU D 140       6.431 -27.901 -91.424  1.00 90.51           C  
-ATOM  12827  O   GLU D 140       5.263 -28.155 -91.723  1.00 90.42           O  
-ATOM  12828  CB  GLU D 140       8.365 -29.385 -90.830  1.00 58.39           C  
-ATOM  12829  CG  GLU D 140       8.075 -30.685 -91.550  1.00 72.06           C  
-ATOM  12830  CD  GLU D 140       8.708 -31.879 -90.862  1.00 74.64           C  
-ATOM  12831  OE1 GLU D 140       8.014 -32.539 -90.059  1.00 73.96           O  
-ATOM  12832  OE2 GLU D 140       9.900 -32.155 -91.122  1.00 47.12           O  
-ATOM  12833  N   TYR D 141       7.156 -26.961 -92.023  1.00 90.56           N  
-ATOM  12834  CA  TYR D 141       6.623 -26.076 -93.059  1.00 81.07           C  
-ATOM  12835  C   TYR D 141       5.443 -25.229 -92.586  1.00 83.52           C  
-ATOM  12836  O   TYR D 141       4.818 -24.561 -93.402  1.00 76.83           O  
-ATOM  12837  CB  TYR D 141       6.170 -26.861 -94.294  1.00 73.02           C  
-ATOM  12838  CG  TYR D 141       7.151 -27.867 -94.843  1.00 69.53           C  
-ATOM  12839  CD1 TYR D 141       8.190 -27.474 -95.676  1.00 61.13           C  
-ATOM  12840  CD2 TYR D 141       7.012 -29.218 -94.560  1.00 76.93           C  
-ATOM  12841  CE1 TYR D 141       9.079 -28.399 -96.192  1.00 63.31           C  
-ATOM  12842  CE2 TYR D 141       7.892 -30.150 -95.069  1.00 65.08           C  
-ATOM  12843  CZ  TYR D 141       8.924 -29.738 -95.885  1.00 65.54           C  
-ATOM  12844  OH  TYR D 141       9.801 -30.669 -96.392  1.00 51.63           O  
-ATOM  12845  N   LYS D 142       5.132 -25.258 -91.291  1.00 86.64           N  
-ATOM  12846  CA  LYS D 142       3.966 -24.541 -90.770  1.00 87.33           C  
-ATOM  12847  C   LYS D 142       4.033 -23.067 -91.152  1.00 86.83           C  
-ATOM  12848  O   LYS D 142       3.012 -22.429 -91.415  1.00 65.95           O  
-ATOM  12849  CB  LYS D 142       3.863 -24.684 -89.251  1.00 84.15           C  
-ATOM  12850  CG  LYS D 142       2.582 -24.099 -88.671  1.00 86.97           C  
-ATOM  12851  CD  LYS D 142       1.400 -25.041 -88.871  1.00 85.42           C  
-ATOM  12852  CE  LYS D 142       0.076 -24.295 -88.788  1.00 77.40           C  
-ATOM  12853  NZ  LYS D 142      -0.016 -23.429 -87.580  1.00 61.37           N  
-ATOM  12854  N   ASP D 143       5.251 -22.537 -91.180  1.00 98.67           N  
-ATOM  12855  CA  ASP D 143       5.504 -21.229 -91.757  1.00 94.58           C  
-ATOM  12856  C   ASP D 143       5.970 -21.425 -93.196  1.00 97.32           C  
-ATOM  12857  O   ASP D 143       6.560 -22.460 -93.517  1.00 92.54           O  
-ATOM  12858  CB  ASP D 143       6.546 -20.462 -90.942  1.00 98.77           C  
-ATOM  12859  CG  ASP D 143       6.235 -20.457 -89.456  1.00 98.31           C  
-ATOM  12860  OD1 ASP D 143       5.627 -21.435 -88.973  1.00101.94           O  
-ATOM  12861  OD2 ASP D 143       6.599 -19.478 -88.769  1.00 83.88           O  
-ATOM  12862  N   SER D 144       5.667 -20.431 -94.033  1.00101.80           N  
-ATOM  12863  CA  SER D 144       6.006 -20.354 -95.466  1.00103.94           C  
-ATOM  12864  C   SER D 144       4.957 -20.988 -96.384  1.00 92.70           C  
-ATOM  12865  O   SER D 144       4.637 -20.414 -97.427  1.00 84.60           O  
-ATOM  12866  CB  SER D 144       7.378 -20.972 -95.766  1.00 97.10           C  
-ATOM  12867  OG  SER D 144       8.408 -20.282 -95.081  1.00 95.84           O  
-ATOM  12868  N   VAL D 145       4.422 -22.153 -96.026  1.00 91.13           N  
-ATOM  12869  CA  VAL D 145       3.430 -22.774 -96.901  1.00 74.64           C  
-ATOM  12870  C   VAL D 145       2.132 -21.967 -96.848  1.00 80.67           C  
-ATOM  12871  O   VAL D 145       1.619 -21.636 -95.777  1.00 94.12           O  
-ATOM  12872  CB  VAL D 145       3.171 -24.273 -96.558  1.00 75.65           C  
-ATOM  12873  CG1 VAL D 145       2.404 -24.443 -95.253  1.00 84.44           C  
-ATOM  12874  CG2 VAL D 145       2.421 -24.945 -97.695  1.00 75.93           C  
-ATOM  12875  N   ASP D 146       1.633 -21.606 -98.024  1.00 72.29           N  
-ATOM  12876  CA  ASP D 146       0.426 -20.796 -98.129  1.00 72.99           C  
-ATOM  12877  C   ASP D 146      -0.800 -21.697 -98.142  1.00 73.19           C  
-ATOM  12878  O   ASP D 146      -1.455 -21.899 -97.118  1.00 68.31           O  
-ATOM  12879  CB  ASP D 146       0.473 -19.925 -99.390  1.00 68.07           C  
-ATOM  12880  CG  ASP D 146      -0.796 -19.115 -99.593  1.00 73.51           C  
-ATOM  12881  OD1 ASP D 146      -1.470 -18.793 -98.592  1.00 74.54           O  
-ATOM  12882  OD2 ASP D 146      -1.117 -18.796-100.759  1.00 69.42           O  
-ATOM  12883  N   GLN D 147      -1.102 -22.231 -99.318  1.00 73.11           N  
-ATOM  12884  CA  GLN D 147      -2.170 -23.202 -99.487  1.00 64.74           C  
-ATOM  12885  C   GLN D 147      -1.598 -24.432-100.170  1.00 60.25           C  
-ATOM  12886  O   GLN D 147      -0.550 -24.359-100.811  1.00 61.17           O  
-ATOM  12887  CB  GLN D 147      -3.319 -22.610-100.302  1.00 64.45           C  
-ATOM  12888  CG  GLN D 147      -2.853 -21.781-101.488  1.00 61.24           C  
-ATOM  12889  CD  GLN D 147      -3.969 -21.478-102.466  1.00 59.36           C  
-ATOM  12890  OE1 GLN D 147      -5.145 -21.684-102.169  1.00 54.79           O  
-ATOM  12891  NE2 GLN D 147      -3.603 -20.992-103.645  1.00 61.65           N  
-ATOM  12892  N   ILE D 148      -2.279 -25.563-100.038  1.00 53.68           N  
-ATOM  12893  CA  ILE D 148      -1.779 -26.797-100.627  1.00 58.66           C  
-ATOM  12894  C   ILE D 148      -2.592 -27.200-101.852  1.00 66.31           C  
-ATOM  12895  O   ILE D 148      -3.681 -26.674-102.091  1.00 75.32           O  
-ATOM  12896  CB  ILE D 148      -1.787 -27.952 -99.609  1.00 55.84           C  
-ATOM  12897  CG1 ILE D 148      -3.122 -28.697 -99.642  1.00 55.90           C  
-ATOM  12898  CG2 ILE D 148      -1.482 -27.432 -98.211  1.00 46.91           C  
-ATOM  12899  CD1 ILE D 148      -3.035 -30.095 -99.088  1.00 65.73           C  
-ATOM  12900  N   PHE D 149      -2.049 -28.131-102.629  1.00 63.53           N  
-ATOM  12901  CA  PHE D 149      -2.727 -28.636-103.815  1.00 48.73           C  
-ATOM  12902  C   PHE D 149      -2.539 -30.143-103.966  1.00 49.32           C  
-ATOM  12903  O   PHE D 149      -1.525 -30.698-103.545  1.00 57.77           O  
-ATOM  12904  CB  PHE D 149      -2.215 -27.926-105.069  1.00 50.02           C  
-ATOM  12905  CG  PHE D 149      -2.616 -26.483-105.159  1.00 46.79           C  
-ATOM  12906  CD1 PHE D 149      -3.925 -26.135-105.440  1.00 47.21           C  
-ATOM  12907  CD2 PHE D 149      -1.682 -25.476-104.982  1.00 50.84           C  
-ATOM  12908  CE1 PHE D 149      -4.298 -24.809-105.533  1.00 55.93           C  
-ATOM  12909  CE2 PHE D 149      -2.050 -24.147-105.074  1.00 50.41           C  
-ATOM  12910  CZ  PHE D 149      -3.359 -23.814-105.350  1.00 49.55           C  
-ATOM  12911  N   VAL D 150      -3.526 -30.799-104.566  1.00 47.78           N  
-ATOM  12912  CA  VAL D 150      -3.412 -32.213-104.907  1.00 43.60           C  
-ATOM  12913  C   VAL D 150      -3.595 -32.387-106.413  1.00 47.61           C  
-ATOM  12914  O   VAL D 150      -4.640 -32.039-106.964  1.00 50.05           O  
-ATOM  12915  CB  VAL D 150      -4.444 -33.072-104.157  1.00 39.08           C  
-ATOM  12916  CG1 VAL D 150      -4.198 -34.548-104.429  1.00 36.00           C  
-ATOM  12917  CG2 VAL D 150      -4.391 -32.785-102.664  1.00 47.96           C  
-ATOM  12918  N   VAL D 151      -2.574 -32.926-107.073  1.00 51.24           N  
-ATOM  12919  CA  VAL D 151      -2.556 -32.995-108.532  1.00 38.88           C  
-ATOM  12920  C   VAL D 151      -2.364 -34.417-109.062  1.00 29.52           C  
-ATOM  12921  O   VAL D 151      -2.850 -35.387-108.478  1.00 27.47           O  
-ATOM  12922  CB  VAL D 151      -1.442 -32.104-109.104  1.00 40.54           C  
-ATOM  12923  CG1 VAL D 151      -1.530 -30.705-108.511  1.00 34.11           C  
-ATOM  12924  CG2 VAL D 151      -0.081 -32.712-108.815  1.00 44.81           C  
-ATOM  12925  N   GLY D 153      -2.795 -37.861-108.718  1.00 32.82           N  
-ATOM  12926  CA  GLY D 153      -3.687 -38.537-109.643  1.00 48.09           C  
-ATOM  12927  C   GLY D 153      -4.873 -39.165-108.937  1.00 53.84           C  
-ATOM  12928  O   GLY D 153      -5.135 -38.869-107.771  1.00 57.17           O  
-ATOM  12929  N   ALA D 154      -5.592 -40.034-109.643  1.00 52.67           N  
-ATOM  12930  CA  ALA D 154      -6.763 -40.693-109.075  1.00 48.55           C  
-ATOM  12931  C   ALA D 154      -6.355 -41.588-107.918  1.00 58.27           C  
-ATOM  12932  O   ALA D 154      -5.224 -42.071-107.860  1.00 61.15           O  
-ATOM  12933  CB  ALA D 154      -7.496 -41.494-110.131  1.00 45.23           C  
-ATOM  12934  N   GLY D 155      -7.280 -41.809-106.994  1.00 60.91           N  
-ATOM  12935  CA  GLY D 155      -6.949 -42.522-105.778  1.00 71.20           C  
-ATOM  12936  C   GLY D 155      -6.503 -41.539-104.716  1.00 59.10           C  
-ATOM  12937  O   GLY D 155      -6.944 -41.610-103.570  1.00 67.05           O  
-ATOM  12938  N   LEU D 156      -5.619 -40.622-105.093  1.00 48.55           N  
-ATOM  12939  CA  LEU D 156      -5.274 -39.515-104.222  1.00 54.94           C  
-ATOM  12940  C   LEU D 156      -6.467 -38.580-104.160  1.00 59.12           C  
-ATOM  12941  O   LEU D 156      -6.800 -38.046-103.107  1.00 65.68           O  
-ATOM  12942  CB  LEU D 156      -4.026 -38.788-104.724  1.00 46.30           C  
-ATOM  12943  CG  LEU D 156      -3.200 -38.121-103.623  1.00 53.21           C  
-ATOM  12944  CD1 LEU D 156      -2.841 -39.158-102.579  1.00 64.26           C  
-ATOM  12945  CD2 LEU D 156      -1.952 -37.487-104.205  1.00 45.91           C  
-ATOM  12946  N   TYR D 157      -7.103 -38.396-105.312  1.00 51.62           N  
-ATOM  12947  CA  TYR D 157      -8.336 -37.623-105.413  1.00 44.73           C  
-ATOM  12948  C   TYR D 157      -9.448 -38.243-104.579  1.00 56.92           C  
-ATOM  12949  O   TYR D 157     -10.106 -37.553-103.802  1.00 57.15           O  
-ATOM  12950  CB  TYR D 157      -8.793 -37.512-106.872  1.00 44.07           C  
-ATOM  12951  CG  TYR D 157      -7.880 -36.685-107.744  1.00 46.42           C  
-ATOM  12952  CD1 TYR D 157      -7.296 -35.518-107.266  1.00 42.39           C  
-ATOM  12953  CD2 TYR D 157      -7.604 -37.069-109.049  1.00 45.33           C  
-ATOM  12954  CE1 TYR D 157      -6.467 -34.760-108.065  1.00 39.15           C  
-ATOM  12955  CE2 TYR D 157      -6.774 -36.317-109.853  1.00 40.35           C  
-ATOM  12956  CZ  TYR D 157      -6.206 -35.166-109.356  1.00 41.27           C  
-ATOM  12957  OH  TYR D 157      -5.379 -34.408-110.154  1.00 42.93           O  
-ATOM  12958  N   GLU D 158      -9.662 -39.545-104.752  1.00 60.46           N  
-ATOM  12959  CA  GLU D 158     -10.732 -40.234-104.037  1.00 62.65           C  
-ATOM  12960  C   GLU D 158     -10.427 -40.295-102.546  1.00 61.66           C  
-ATOM  12961  O   GLU D 158     -11.340 -40.344-101.720  1.00 60.14           O  
-ATOM  12962  CB  GLU D 158     -10.952 -41.644-104.601  1.00 56.31           C  
-ATOM  12963  CG  GLU D 158     -10.015 -42.706-104.062  1.00 72.07           C  
-ATOM  12964  CD  GLU D 158      -9.891 -43.894-104.995  1.00 72.21           C  
-ATOM  12965  OE1 GLU D 158     -10.319 -43.778-106.163  1.00 63.29           O  
-ATOM  12966  OE2 GLU D 158      -9.357 -44.940-104.565  1.00 61.97           O  
-ATOM  12967  N   ALA D 159      -9.142 -40.290-102.204  1.00 54.56           N  
-ATOM  12968  CA  ALA D 159      -8.739 -40.239-100.809  1.00 53.18           C  
-ATOM  12969  C   ALA D 159      -9.092 -38.888-100.231  1.00 55.57           C  
-ATOM  12970  O   ALA D 159      -9.661 -38.793 -99.151  1.00 63.29           O  
-ATOM  12971  CB  ALA D 159      -7.251 -40.502-100.665  1.00 58.53           C  
-ATOM  12972  N   ALA D 160      -8.752 -37.847-100.982  1.00 53.26           N  
-ATOM  12973  CA  ALA D 160      -8.985 -36.463-100.588  1.00 47.35           C  
-ATOM  12974  C   ALA D 160     -10.472 -36.166-100.462  1.00 53.28           C  
-ATOM  12975  O   ALA D 160     -10.884 -35.296 -99.690  1.00 52.33           O  
-ATOM  12976  CB  ALA D 160      -8.349 -35.522-101.590  1.00 49.42           C  
-ATOM  12977  N   LEU D 161     -11.272 -36.894-101.233  1.00 49.01           N  
-ATOM  12978  CA  LEU D 161     -12.714 -36.717-101.224  1.00 47.75           C  
-ATOM  12979  C   LEU D 161     -13.378 -37.506-100.100  1.00 59.27           C  
-ATOM  12980  O   LEU D 161     -14.249 -36.983 -99.405  1.00 65.17           O  
-ATOM  12981  CB  LEU D 161     -13.302 -37.124-102.575  1.00 51.30           C  
-ATOM  12982  CG  LEU D 161     -13.136 -36.101-103.701  1.00 44.52           C  
-ATOM  12983  CD1 LEU D 161     -13.661 -36.653-105.016  1.00 43.85           C  
-ATOM  12984  CD2 LEU D 161     -13.836 -34.797-103.346  1.00 39.48           C  
-ATOM  12985  N   SER D 162     -12.974 -38.760 -99.921  1.00 58.94           N  
-ATOM  12986  CA  SER D 162     -13.547 -39.588 -98.864  1.00 54.81           C  
-ATOM  12987  C   SER D 162     -13.131 -39.083 -97.483  1.00 49.00           C  
-ATOM  12988  O   SER D 162     -13.862 -39.243 -96.508  1.00 61.40           O  
-ATOM  12989  CB  SER D 162     -13.142 -41.053 -99.043  1.00 51.72           C  
-ATOM  12990  OG  SER D 162     -11.737 -41.196 -99.118  1.00 78.22           O  
-ATOM  12991  N   LEU D 163     -11.955 -38.467 -97.412  1.00 42.18           N  
-ATOM  12992  CA  LEU D 163     -11.474 -37.863 -96.173  1.00 42.17           C  
-ATOM  12993  C   LEU D 163     -12.039 -36.456 -96.019  1.00 46.88           C  
-ATOM  12994  O   LEU D 163     -11.801 -35.789 -95.012  1.00 46.78           O  
-ATOM  12995  CB  LEU D 163      -9.943 -37.828 -96.137  1.00 50.00           C  
-ATOM  12996  CG  LEU D 163      -9.225 -39.178 -96.050  1.00 60.54           C  
-ATOM  12997  CD1 LEU D 163      -7.724 -39.015 -96.270  1.00 56.69           C  
-ATOM  12998  CD2 LEU D 163      -9.503 -39.856 -94.717  1.00 68.26           C  
-ATOM  12999  N   GLY D 164     -12.776 -36.016 -97.036  1.00 54.72           N  
-ATOM  13000  CA  GLY D 164     -13.498 -34.756 -96.999  1.00 57.97           C  
-ATOM  13001  C   GLY D 164     -12.676 -33.543 -96.614  1.00 56.00           C  
-ATOM  13002  O   GLY D 164     -13.122 -32.712 -95.823  1.00 62.41           O  
-ATOM  13003  N   VAL D 165     -11.477 -33.433 -97.175  1.00 50.71           N  
-ATOM  13004  CA  VAL D 165     -10.579 -32.335 -96.834  1.00 59.83           C  
-ATOM  13005  C   VAL D 165     -10.454 -31.311 -97.961  1.00 67.52           C  
-ATOM  13006  O   VAL D 165      -9.838 -30.261 -97.785  1.00 67.64           O  
-ATOM  13007  CB  VAL D 165      -9.175 -32.854 -96.474  1.00 55.04           C  
-ATOM  13008  CG1 VAL D 165      -9.195 -33.528 -95.110  1.00 57.82           C  
-ATOM  13009  CG2 VAL D 165      -8.672 -33.810 -97.544  1.00 50.83           C  
-ATOM  13010  N   ALA D 166     -11.041 -31.617 -99.114  1.00 61.17           N  
-ATOM  13011  CA  ALA D 166     -10.966 -30.726-100.266  1.00 52.56           C  
-ATOM  13012  C   ALA D 166     -12.100 -29.705-100.248  1.00 57.46           C  
-ATOM  13013  O   ALA D 166     -13.266 -30.056-100.423  1.00 64.30           O  
-ATOM  13014  CB  ALA D 166     -10.995 -31.528-101.558  1.00 51.61           C  
-ATOM  13015  N   SER D 167     -11.750 -28.440-100.037  1.00 49.79           N  
-ATOM  13016  CA  SER D 167     -12.744 -27.375 -99.964  1.00 48.57           C  
-ATOM  13017  C   SER D 167     -13.103 -26.838-101.347  1.00 49.93           C  
-ATOM  13018  O   SER D 167     -14.248 -26.445-101.594  1.00 56.29           O  
-ATOM  13019  CB  SER D 167     -12.239 -26.236 -99.077  1.00 53.40           C  
-ATOM  13020  OG  SER D 167     -11.017 -25.710 -99.566  1.00 56.43           O  
-ATOM  13021  N   HIS D 168     -12.117 -26.827-102.241  1.00 48.92           N  
-ATOM  13022  CA  HIS D 168     -12.294 -26.293-103.587  1.00 45.14           C  
-ATOM  13023  C   HIS D 168     -11.827 -27.271-104.663  1.00 45.60           C  
-ATOM  13024  O   HIS D 168     -10.964 -28.114-104.416  1.00 50.19           O  
-ATOM  13025  CB  HIS D 168     -11.540 -24.970-103.739  1.00 45.17           C  
-ATOM  13026  CG  HIS D 168     -11.930 -23.931-102.735  1.00 43.90           C  
-ATOM  13027  ND1 HIS D 168     -13.180 -23.351-102.711  1.00 45.58           N  
-ATOM  13028  CD2 HIS D 168     -11.231 -23.362-101.725  1.00 53.93           C  
-ATOM  13029  CE1 HIS D 168     -13.236 -22.473-101.726  1.00 55.01           C  
-ATOM  13030  NE2 HIS D 168     -12.067 -22.460-101.112  1.00 72.58           N  
-ATOM  13031  N   LEU D 169     -12.402 -27.142-105.857  1.00 38.04           N  
-ATOM  13032  CA  LEU D 169     -12.011 -27.953-107.007  1.00 41.17           C  
-ATOM  13033  C   LEU D 169     -11.653 -27.078-108.207  1.00 40.67           C  
-ATOM  13034  O   LEU D 169     -12.513 -26.392-108.752  1.00 39.54           O  
-ATOM  13035  CB  LEU D 169     -13.133 -28.920-107.400  1.00 30.97           C  
-ATOM  13036  CG  LEU D 169     -13.626 -29.942-106.376  1.00 28.25           C  
-ATOM  13037  CD1 LEU D 169     -14.569 -30.935-107.031  1.00 30.14           C  
-ATOM  13038  CD2 LEU D 169     -12.464 -30.666-105.738  1.00 35.84           C  
-ATOM  13039  N   TYR D 170     -10.387 -27.098-108.615  1.00 37.26           N  
-ATOM  13040  CA  TYR D 170      -9.975 -26.422-109.844  1.00 34.22           C  
-ATOM  13041  C   TYR D 170     -10.021 -27.401-111.010  1.00 30.64           C  
-ATOM  13042  O   TYR D 170      -9.099 -28.192-111.204  1.00 33.50           O  
-ATOM  13043  CB  TYR D 170      -8.571 -25.831-109.706  1.00 47.52           C  
-ATOM  13044  CG  TYR D 170      -8.496 -24.614-108.813  1.00 54.82           C  
-ATOM  13045  CD1 TYR D 170      -8.659 -23.336-109.332  1.00 49.36           C  
-ATOM  13046  CD2 TYR D 170      -8.258 -24.742-107.450  1.00 63.67           C  
-ATOM  13047  CE1 TYR D 170      -8.591 -22.221-108.517  1.00 64.30           C  
-ATOM  13048  CE2 TYR D 170      -8.187 -23.633-106.628  1.00 65.68           C  
-ATOM  13049  CZ  TYR D 170      -8.354 -22.375-107.166  1.00 68.15           C  
-ATOM  13050  OH  TYR D 170      -8.284 -21.268-106.349  1.00 69.18           O  
-ATOM  13051  N   ILE D 171     -11.096 -27.343-111.789  1.00 38.29           N  
-ATOM  13052  CA  ILE D 171     -11.327 -28.328-112.840  1.00 34.28           C  
-ATOM  13053  C   ILE D 171     -11.214 -27.751-114.247  1.00 31.67           C  
-ATOM  13054  O   ILE D 171     -11.855 -26.752-114.574  1.00 31.46           O  
-ATOM  13055  CB  ILE D 171     -12.720 -28.979-112.697  1.00 25.15           C  
-ATOM  13056  CG1 ILE D 171     -12.922 -29.510-111.276  1.00 28.54           C  
-ATOM  13057  CG2 ILE D 171     -12.903 -30.081-113.730  1.00 25.48           C  
-ATOM  13058  CD1 ILE D 171     -14.188 -30.308-111.100  1.00 24.49           C  
-ATOM  13059  N   THR D 172     -10.394 -28.396-115.073  1.00 34.27           N  
-ATOM  13060  CA  THR D 172     -10.307 -28.073-116.494  1.00 34.39           C  
-ATOM  13061  C   THR D 172     -11.220 -28.994-117.301  1.00 33.20           C  
-ATOM  13062  O   THR D 172     -10.898 -30.161-117.521  1.00 32.39           O  
-ATOM  13063  CB  THR D 172      -8.869 -28.203-117.028  1.00 24.14           C  
-ATOM  13064  OG1 THR D 172      -7.978 -27.437-116.211  1.00 32.55           O  
-ATOM  13065  CG2 THR D 172      -8.786 -27.706-118.463  1.00 24.73           C  
-ATOM  13066  N   ARG D 173     -12.359 -28.468-117.738  1.00 26.17           N  
-ATOM  13067  CA  ARG D 173     -13.333 -29.269-118.471  1.00 23.81           C  
-ATOM  13068  C   ARG D 173     -12.925 -29.502-119.913  1.00 23.80           C  
-ATOM  13069  O   ARG D 173     -13.179 -28.668-120.774  1.00 24.53           O  
-ATOM  13070  CB  ARG D 173     -14.705 -28.601-118.445  1.00 24.23           C  
-ATOM  13071  CG  ARG D 173     -15.256 -28.368-117.064  1.00 24.58           C  
-ATOM  13072  CD  ARG D 173     -16.131 -27.141-117.054  1.00 28.27           C  
-ATOM  13073  NE  ARG D 173     -17.548 -27.466-117.124  1.00 25.16           N  
-ATOM  13074  CZ  ARG D 173     -18.494 -26.581-117.414  1.00 32.05           C  
-ATOM  13075  NH1 ARG D 173     -18.164 -25.323-117.677  1.00 24.81           N  
-ATOM  13076  NH2 ARG D 173     -19.765 -26.954-117.455  1.00 37.32           N  
-ATOM  13077  N   VAL D 174     -12.304 -30.644-120.174  1.00 21.12           N  
-ATOM  13078  CA  VAL D 174     -12.050 -31.073-121.544  1.00 20.91           C  
-ATOM  13079  C   VAL D 174     -13.377 -31.457-122.195  1.00 22.57           C  
-ATOM  13080  O   VAL D 174     -14.087 -32.325-121.693  1.00 22.57           O  
-ATOM  13081  CB  VAL D 174     -11.075 -32.262-121.594  1.00 20.73           C  
-ATOM  13082  CG1 VAL D 174     -10.803 -32.674-123.027  1.00 20.27           C  
-ATOM  13083  CG2 VAL D 174      -9.783 -31.898-120.887  1.00 29.54           C  
-ATOM  13084  N   ALA D 175     -13.720 -30.805-123.301  1.00 19.45           N  
-ATOM  13085  CA  ALA D 175     -15.027 -31.013-123.926  1.00 21.19           C  
-ATOM  13086  C   ALA D 175     -15.101 -32.310-124.732  1.00 27.01           C  
-ATOM  13087  O   ALA D 175     -16.165 -32.923-124.827  1.00 26.07           O  
-ATOM  13088  CB  ALA D 175     -15.381 -29.831-124.810  1.00 19.60           C  
-ATOM  13089  N   ARG D 176     -13.977 -32.716-125.317  1.00 22.46           N  
-ATOM  13090  CA  ARG D 176     -13.908 -33.971-126.061  1.00 22.62           C  
-ATOM  13091  C   ARG D 176     -13.732 -35.166-125.139  1.00 22.58           C  
-ATOM  13092  O   ARG D 176     -13.041 -35.080-124.126  1.00 25.23           O  
-ATOM  13093  CB  ARG D 176     -12.754 -33.947-127.061  1.00 20.20           C  
-ATOM  13094  CG  ARG D 176     -12.958 -33.043-128.250  1.00 22.36           C  
-ATOM  13095  CD  ARG D 176     -11.737 -33.077-129.155  1.00 23.46           C  
-ATOM  13096  NE  ARG D 176     -11.461 -34.420-129.657  1.00 23.93           N  
-ATOM  13097  CZ  ARG D 176     -10.445 -34.720-130.459  1.00 31.29           C  
-ATOM  13098  NH1 ARG D 176     -10.263 -35.969-130.867  1.00 40.03           N  
-ATOM  13099  NH2 ARG D 176      -9.607 -33.771-130.851  1.00 29.98           N  
-ATOM  13100  N   GLU D 177     -14.353 -36.284-125.495  1.00 22.07           N  
-ATOM  13101  CA  GLU D 177     -14.073 -37.538-124.813  1.00 25.15           C  
-ATOM  13102  C   GLU D 177     -12.856 -38.197-125.440  1.00 27.00           C  
-ATOM  13103  O   GLU D 177     -12.595 -38.041-126.634  1.00 32.06           O  
-ATOM  13104  CB  GLU D 177     -15.270 -38.488-124.870  1.00 35.63           C  
-ATOM  13105  CG  GLU D 177     -16.115 -38.524-123.605  1.00 35.59           C  
-ATOM  13106  CD  GLU D 177     -17.371 -37.677-123.711  1.00 61.18           C  
-ATOM  13107  OE1 GLU D 177     -17.323 -36.610-124.363  1.00 71.67           O  
-ATOM  13108  OE2 GLU D 177     -18.410 -38.086-123.150  1.00 60.20           O  
-ATOM  13109  N   PHE D 178     -12.112 -38.929-124.624  1.00 29.83           N  
-ATOM  13110  CA  PHE D 178     -10.944 -39.655-125.092  1.00 23.34           C  
-ATOM  13111  C   PHE D 178     -10.906 -41.023-124.428  1.00 21.37           C  
-ATOM  13112  O   PHE D 178     -11.485 -41.207-123.358  1.00 22.08           O  
-ATOM  13113  CB  PHE D 178      -9.660 -38.879-124.786  1.00 25.39           C  
-ATOM  13114  CG  PHE D 178      -9.463 -37.656-125.638  1.00 24.58           C  
-ATOM  13115  CD1 PHE D 178      -8.798 -37.743-126.849  1.00 32.54           C  
-ATOM  13116  CD2 PHE D 178      -9.924 -36.417-125.221  1.00 25.21           C  
-ATOM  13117  CE1 PHE D 178      -8.603 -36.621-127.635  1.00 35.72           C  
-ATOM  13118  CE2 PHE D 178      -9.732 -35.290-126.001  1.00 23.40           C  
-ATOM  13119  CZ  PHE D 178      -9.071 -35.393-127.209  1.00 29.92           C  
-ATOM  13120  N   PRO D 179     -10.243 -41.995-125.072  1.00 24.62           N  
-ATOM  13121  CA  PRO D 179     -10.001 -43.289-124.429  1.00 30.54           C  
-ATOM  13122  C   PRO D 179      -9.266 -43.125-123.101  1.00 26.18           C  
-ATOM  13123  O   PRO D 179      -8.245 -42.439-123.046  1.00 24.85           O  
-ATOM  13124  CB  PRO D 179      -9.137 -44.030-125.452  1.00 24.82           C  
-ATOM  13125  CG  PRO D 179      -9.527 -43.438-126.759  1.00 22.33           C  
-ATOM  13126  CD  PRO D 179      -9.813 -41.989-126.481  1.00 22.24           C  
-ATOM  13127  N   CYS D 180      -9.792 -43.739-122.046  1.00 26.23           N  
-ATOM  13128  CA  CYS D 180      -9.198 -43.631-120.718  1.00 28.07           C  
-ATOM  13129  C   CYS D 180      -9.312 -44.934-119.937  1.00 31.03           C  
-ATOM  13130  O   CYS D 180     -10.224 -45.729-120.163  1.00 35.51           O  
-ATOM  13131  CB  CYS D 180      -9.857 -42.502-119.925  1.00 25.30           C  
-ATOM  13132  SG  CYS D 180      -9.538 -40.852-120.562  1.00 29.58           S  
-ATOM  13133  N   ASP D 181      -8.383 -45.143-119.012  1.00 28.07           N  
-ATOM  13134  CA  ASP D 181      -8.457 -46.282-118.107  1.00 30.48           C  
-ATOM  13135  C   ASP D 181      -8.363 -45.820-116.652  1.00 31.37           C  
-ATOM  13136  O   ASP D 181      -8.328 -46.637-115.733  1.00 44.58           O  
-ATOM  13137  CB  ASP D 181      -7.359 -47.307-118.427  1.00 37.24           C  
-ATOM  13138  CG  ASP D 181      -5.966 -46.692-118.489  1.00 35.13           C  
-ATOM  13139  OD1 ASP D 181      -5.704 -45.705-117.770  1.00 39.41           O  
-ATOM  13140  OD2 ASP D 181      -5.123 -47.206-119.257  1.00 25.64           O  
-ATOM  13141  N   VAL D 182      -8.316 -44.506-116.454  1.00 24.11           N  
-ATOM  13142  CA  VAL D 182      -8.256 -43.927-115.114  1.00 26.97           C  
-ATOM  13143  C   VAL D 182      -9.179 -42.716-115.017  1.00 30.58           C  
-ATOM  13144  O   VAL D 182      -9.048 -41.761-115.782  1.00 31.48           O  
-ATOM  13145  CB  VAL D 182      -6.820 -43.512-114.733  1.00 25.37           C  
-ATOM  13146  CG1 VAL D 182      -6.833 -42.624-113.505  1.00 34.77           C  
-ATOM  13147  CG2 VAL D 182      -5.956 -44.737-114.493  1.00 25.01           C  
-ATOM  13148  N   PHE D 183     -10.106 -42.757-114.065  1.00 30.70           N  
-ATOM  13149  CA  PHE D 183     -11.154 -41.745-113.985  1.00 27.70           C  
-ATOM  13150  C   PHE D 183     -11.180 -40.996-112.658  1.00 34.59           C  
-ATOM  13151  O   PHE D 183     -10.791 -41.531-111.618  1.00 28.07           O  
-ATOM  13152  CB  PHE D 183     -12.522 -42.389-114.226  1.00 24.91           C  
-ATOM  13153  CG  PHE D 183     -12.696 -42.950-115.608  1.00 22.48           C  
-ATOM  13154  CD1 PHE D 183     -12.163 -44.183-115.945  1.00 22.76           C  
-ATOM  13155  CD2 PHE D 183     -13.404 -42.250-116.567  1.00 21.61           C  
-ATOM  13156  CE1 PHE D 183     -12.324 -44.701-117.214  1.00 19.03           C  
-ATOM  13157  CE2 PHE D 183     -13.569 -42.761-117.838  1.00 21.80           C  
-ATOM  13158  CZ  PHE D 183     -13.029 -43.989-118.162  1.00 19.77           C  
-ATOM  13159  N   PHE D 184     -11.652 -39.752-112.710  1.00 36.29           N  
-ATOM  13160  CA  PHE D 184     -11.897 -38.958-111.512  1.00 28.78           C  
-ATOM  13161  C   PHE D 184     -13.189 -39.439-110.857  1.00 36.38           C  
-ATOM  13162  O   PHE D 184     -14.179 -39.685-111.546  1.00 34.28           O  
-ATOM  13163  CB  PHE D 184     -11.981 -37.466-111.855  1.00 21.40           C  
-ATOM  13164  CG  PHE D 184     -11.998 -36.562-110.651  1.00 34.90           C  
-ATOM  13165  CD1 PHE D 184     -10.814 -36.106-110.093  1.00 32.47           C  
-ATOM  13166  CD2 PHE D 184     -13.197 -36.168-110.076  1.00 35.27           C  
-ATOM  13167  CE1 PHE D 184     -10.825 -35.277-108.985  1.00 24.56           C  
-ATOM  13168  CE2 PHE D 184     -13.215 -35.338-108.969  1.00 23.35           C  
-ATOM  13169  CZ  PHE D 184     -12.028 -34.892-108.424  1.00 24.03           C  
-ATOM  13170  N   PRO D 185     -13.180 -39.585-109.523  1.00 37.44           N  
-ATOM  13171  CA  PRO D 185     -14.322 -40.108-108.764  1.00 30.22           C  
-ATOM  13172  C   PRO D 185     -15.598 -39.300-108.964  1.00 26.87           C  
-ATOM  13173  O   PRO D 185     -15.536 -38.076-109.067  1.00 27.48           O  
-ATOM  13174  CB  PRO D 185     -13.852 -40.006-107.311  1.00 35.80           C  
-ATOM  13175  CG  PRO D 185     -12.373 -40.008-107.393  1.00 39.53           C  
-ATOM  13176  CD  PRO D 185     -12.037 -39.277-108.647  1.00 37.38           C  
-ATOM  13177  N   ALA D 186     -16.737 -39.984-109.020  1.00 33.28           N  
-ATOM  13178  CA  ALA D 186     -18.031 -39.313-109.095  1.00 36.45           C  
-ATOM  13179  C   ALA D 186     -18.269 -38.530-107.810  1.00 40.05           C  
-ATOM  13180  O   ALA D 186     -17.861 -38.959-106.732  1.00 45.32           O  
-ATOM  13181  CB  ALA D 186     -19.150 -40.319-109.329  1.00 23.71           C  
-ATOM  13182  N   PHE D 187     -18.922 -37.380-107.925  1.00 39.27           N  
-ATOM  13183  CA  PHE D 187     -19.116 -36.506-106.774  1.00 42.30           C  
-ATOM  13184  C   PHE D 187     -20.353 -35.631-106.950  1.00 52.24           C  
-ATOM  13185  O   PHE D 187     -20.787 -35.394-108.077  1.00 51.45           O  
-ATOM  13186  CB  PHE D 187     -17.877 -35.631-106.562  1.00 35.09           C  
-ATOM  13187  CG  PHE D 187     -17.589 -34.700-107.705  1.00 33.87           C  
-ATOM  13188  CD1 PHE D 187     -16.837 -35.123-108.788  1.00 31.14           C  
-ATOM  13189  CD2 PHE D 187     -18.070 -33.401-107.697  1.00 40.69           C  
-ATOM  13190  CE1 PHE D 187     -16.572 -34.270-109.842  1.00 31.01           C  
-ATOM  13191  CE2 PHE D 187     -17.810 -32.543-108.749  1.00 36.14           C  
-ATOM  13192  CZ  PHE D 187     -17.059 -32.978-109.822  1.00 28.93           C  
-ATOM  13193  N   PRO D 188     -20.932 -35.155-105.834  1.00 43.87           N  
-ATOM  13194  CA  PRO D 188     -22.043 -34.201-105.912  1.00 41.53           C  
-ATOM  13195  C   PRO D 188     -21.618 -32.903-106.591  1.00 48.23           C  
-ATOM  13196  O   PRO D 188     -20.741 -32.203-106.084  1.00 50.67           O  
-ATOM  13197  CB  PRO D 188     -22.403 -33.956-104.444  1.00 45.37           C  
-ATOM  13198  CG  PRO D 188     -21.918 -35.165-103.735  1.00 55.59           C  
-ATOM  13199  CD  PRO D 188     -20.662 -35.563-104.446  1.00 45.32           C  
-ATOM  13200  N   GLY D 189     -22.238 -32.591-107.723  1.00 46.85           N  
-ATOM  13201  CA  GLY D 189     -21.838 -31.450-108.525  1.00 40.79           C  
-ATOM  13202  C   GLY D 189     -21.429 -31.940-109.896  1.00 43.54           C  
-ATOM  13203  O   GLY D 189     -21.158 -31.151-110.806  1.00 52.52           O  
-ATOM  13204  N   ASP D 190     -21.410 -33.263-110.041  1.00 44.34           N  
-ATOM  13205  CA  ASP D 190     -21.055 -33.926-111.293  1.00 36.30           C  
-ATOM  13206  C   ASP D 190     -21.805 -33.346-112.489  1.00 40.91           C  
-ATOM  13207  O   ASP D 190     -21.340 -33.425-113.625  1.00 39.01           O  
-ATOM  13208  CB  ASP D 190     -21.325 -35.428-111.180  1.00 40.55           C  
-ATOM  13209  CG  ASP D 190     -20.150 -36.264-111.629  1.00 55.56           C  
-ATOM  13210  OD1 ASP D 190     -19.071 -35.681-111.863  1.00 64.23           O  
-ATOM  13211  OD2 ASP D 190     -20.300 -37.499-111.740  1.00 61.74           O  
-ATOM  13212  N   ASP D 191     -22.960 -32.749-112.211  1.00 40.35           N  
-ATOM  13213  CA  ASP D 191     -23.785 -32.085-113.211  1.00 36.86           C  
-ATOM  13214  C   ASP D 191     -23.016 -31.091-114.081  1.00 38.96           C  
-ATOM  13215  O   ASP D 191     -23.466 -30.746-115.173  1.00 43.89           O  
-ATOM  13216  CB  ASP D 191     -24.944 -31.361-112.524  1.00 46.02           C  
-ATOM  13217  CG  ASP D 191     -26.296 -31.888-112.953  1.00 70.25           C  
-ATOM  13218  OD1 ASP D 191     -26.360 -33.031-113.457  1.00 74.07           O  
-ATOM  13219  OD2 ASP D 191     -27.296 -31.160-112.781  1.00 69.00           O  
-ATOM  13220  N   ILE D 192     -21.863 -30.629-113.601  1.00 37.56           N  
-ATOM  13221  CA  ILE D 192     -21.091 -29.620-114.325  1.00 36.78           C  
-ATOM  13222  C   ILE D 192     -20.288 -30.225-115.486  1.00 31.42           C  
-ATOM  13223  O   ILE D 192     -19.809 -29.507-116.364  1.00 36.73           O  
-ATOM  13224  CB  ILE D 192     -20.154 -28.864-113.359  1.00 34.04           C  
-ATOM  13225  CG1 ILE D 192     -20.954 -28.386-112.148  1.00 63.37           C  
-ATOM  13226  CG2 ILE D 192     -19.504 -27.664-114.035  1.00 32.66           C  
-ATOM  13227  CD1 ILE D 192     -20.113 -27.758-111.079  1.00 75.60           C  
-ATOM  13228  N   LEU D 193     -20.162 -31.548-115.508  1.00 26.37           N  
-ATOM  13229  CA  LEU D 193     -19.416 -32.211-116.575  1.00 23.91           C  
-ATOM  13230  C   LEU D 193     -20.320 -32.674-117.714  1.00 30.49           C  
-ATOM  13231  O   LEU D 193     -20.030 -32.430-118.885  1.00 35.35           O  
-ATOM  13232  CB  LEU D 193     -18.637 -33.392-116.010  1.00 19.52           C  
-ATOM  13233  CG  LEU D 193     -17.676 -32.999-114.890  1.00 19.94           C  
-ATOM  13234  CD1 LEU D 193     -17.168 -34.229-114.184  1.00 26.04           C  
-ATOM  13235  CD2 LEU D 193     -16.521 -32.172-115.427  1.00 14.66           C  
-ATOM  13236  N   SER D 194     -21.411 -33.350-117.368  1.00 30.56           N  
-ATOM  13237  CA  SER D 194     -22.405 -33.759-118.355  1.00 35.88           C  
-ATOM  13238  C   SER D 194     -23.739 -34.044-117.672  1.00 44.31           C  
-ATOM  13239  O   SER D 194     -23.892 -33.794-116.476  1.00 52.53           O  
-ATOM  13240  CB  SER D 194     -21.924 -34.980-119.144  1.00 37.96           C  
-ATOM  13241  OG  SER D 194     -21.162 -35.850-118.325  1.00 50.68           O  
-ATOM  13242  N   ASN D 195     -24.700 -34.563-118.430  1.00 40.02           N  
-ATOM  13243  CA  ASN D 195     -26.071 -34.699-117.944  1.00 39.05           C  
-ATOM  13244  C   ASN D 195     -26.316 -35.931-117.071  1.00 48.58           C  
-ATOM  13245  O   ASN D 195     -27.462 -36.366-116.924  1.00 45.73           O  
-ATOM  13246  CB  ASN D 195     -27.043 -34.719-119.128  1.00 35.56           C  
-ATOM  13247  CG  ASN D 195     -27.023 -33.425-119.920  1.00 33.75           C  
-ATOM  13248  OD1 ASN D 195     -26.512 -32.409-119.453  1.00 37.55           O  
-ATOM  13249  ND2 ASN D 195     -27.589 -33.454-121.121  1.00 30.43           N  
-ATOM  13250  N   LYS D 196     -25.244 -36.476-116.494  1.00 56.56           N  
-ATOM  13251  CA  LYS D 196     -25.323 -37.674-115.654  1.00 60.20           C  
-ATOM  13252  C   LYS D 196     -26.407 -37.555-114.586  1.00 49.94           C  
-ATOM  13253  O   LYS D 196     -27.515 -38.061-114.759  1.00 37.08           O  
-ATOM  13254  CB  LYS D 196     -23.972 -37.961-114.982  1.00 61.74           C  
-ATOM  13255  CG  LYS D 196     -23.056 -38.902-115.753  1.00 85.37           C  
-ATOM  13256  CD  LYS D 196     -22.672 -38.323-117.099  1.00 77.18           C  
-ATOM  13257  CE  LYS D 196     -21.682 -39.214-117.825  1.00 77.35           C  
-ATOM  13258  NZ  LYS D 196     -21.259 -38.607-119.115  1.00 62.03           N  
-ATOM  13259  N   GLU D 224     -26.242 -32.739 -96.629  1.00 83.48           N  
-ATOM  13260  CA  GLU D 224     -25.502 -33.413 -97.689  1.00 84.26           C  
-ATOM  13261  C   GLU D 224     -24.550 -32.447 -98.388  1.00 92.16           C  
-ATOM  13262  O   GLU D 224     -24.981 -31.447 -98.965  1.00 91.67           O  
-ATOM  13263  CB  GLU D 224     -26.464 -34.032 -98.706  1.00 75.59           C  
-ATOM  13264  CG  GLU D 224     -25.836 -35.103 -99.581  1.00 86.32           C  
-ATOM  13265  CD  GLU D 224     -25.489 -36.357 -98.801  1.00 90.89           C  
-ATOM  13266  OE1 GLU D 224     -24.383 -36.414 -98.220  1.00 76.31           O  
-ATOM  13267  OE2 GLU D 224     -26.326 -37.285 -98.766  1.00 75.83           O  
-ATOM  13268  N   ALA D 225     -23.256 -32.750 -98.333  1.00 78.77           N  
-ATOM  13269  CA  ALA D 225     -22.240 -31.885 -98.928  1.00 66.79           C  
-ATOM  13270  C   ALA D 225     -22.259 -31.961-100.453  1.00 78.71           C  
-ATOM  13271  O   ALA D 225     -22.455 -33.031-101.031  1.00 82.15           O  
-ATOM  13272  CB  ALA D 225     -20.863 -32.248 -98.398  1.00 49.76           C  
-ATOM  13273  N   THR D 226     -22.050 -30.817-101.096  1.00 71.08           N  
-ATOM  13274  CA  THR D 226     -22.047 -30.742-102.551  1.00 56.94           C  
-ATOM  13275  C   THR D 226     -21.142 -29.620-103.047  1.00 52.19           C  
-ATOM  13276  O   THR D 226     -20.896 -28.642-102.338  1.00 48.27           O  
-ATOM  13277  CB  THR D 226     -23.465 -30.523-103.108  1.00 52.54           C  
-ATOM  13278  OG1 THR D 226     -23.404 -30.389-104.534  1.00 49.34           O  
-ATOM  13279  CG2 THR D 226     -24.079 -29.268-102.512  1.00 62.77           C  
-ATOM  13280  N   TYR D 227     -20.654 -29.768-104.274  1.00 46.33           N  
-ATOM  13281  CA  TYR D 227     -19.719 -28.814-104.855  1.00 37.78           C  
-ATOM  13282  C   TYR D 227     -20.395 -27.879-105.848  1.00 45.55           C  
-ATOM  13283  O   TYR D 227     -20.703 -28.271-106.975  1.00 48.02           O  
-ATOM  13284  CB  TYR D 227     -18.571 -29.552-105.543  1.00 34.70           C  
-ATOM  13285  CG  TYR D 227     -17.636 -30.250-104.588  1.00 38.16           C  
-ATOM  13286  CD1 TYR D 227     -16.529 -29.593-104.070  1.00 40.77           C  
-ATOM  13287  CD2 TYR D 227     -17.860 -31.565-104.200  1.00 44.27           C  
-ATOM  13288  CE1 TYR D 227     -15.669 -30.225-103.196  1.00 45.84           C  
-ATOM  13289  CE2 TYR D 227     -17.004 -32.205-103.324  1.00 42.12           C  
-ATOM  13290  CZ  TYR D 227     -15.911 -31.529-102.825  1.00 47.32           C  
-ATOM  13291  OH  TYR D 227     -15.050 -32.156-101.952  1.00 55.71           O  
-ATOM  13292  N   ARG D 228     -20.612 -26.637-105.429  1.00 44.16           N  
-ATOM  13293  CA  ARG D 228     -21.232 -25.645-106.299  1.00 44.00           C  
-ATOM  13294  C   ARG D 228     -20.167 -24.821-107.015  1.00 42.82           C  
-ATOM  13295  O   ARG D 228     -19.180 -24.409-106.405  1.00 43.72           O  
-ATOM  13296  CB  ARG D 228     -22.168 -24.737-105.497  1.00 47.20           C  
-ATOM  13297  CG  ARG D 228     -23.595 -24.672-106.037  1.00 52.01           C  
-ATOM  13298  CD  ARG D 228     -24.616 -24.766-104.908  1.00 68.58           C  
-ATOM  13299  NE  ARG D 228     -24.339 -23.819-103.830  1.00 77.48           N  
-ATOM  13300  CZ  ARG D 228     -24.997 -22.678-103.641  1.00 69.16           C  
-ATOM  13301  NH1 ARG D 228     -25.988 -22.334-104.454  1.00 53.95           N  
-ATOM  13302  NH2 ARG D 228     -24.668 -21.883-102.631  1.00 57.57           N  
-ATOM  13303  N   PRO D 229     -20.360 -24.587-108.322  1.00 48.18           N  
-ATOM  13304  CA  PRO D 229     -19.430 -23.778-109.114  1.00 34.79           C  
-ATOM  13305  C   PRO D 229     -19.535 -22.294-108.778  1.00 39.06           C  
-ATOM  13306  O   PRO D 229     -20.599 -21.817-108.382  1.00 45.69           O  
-ATOM  13307  CB  PRO D 229     -19.869 -24.051-110.554  1.00 34.57           C  
-ATOM  13308  CG  PRO D 229     -21.311 -24.368-110.447  1.00 41.44           C  
-ATOM  13309  CD  PRO D 229     -21.486 -25.084-109.133  1.00 51.67           C  
-ATOM  13310  N   ILE D 230     -18.433 -21.573-108.948  1.00 36.67           N  
-ATOM  13311  CA  ILE D 230     -18.348 -20.182-108.529  1.00 35.46           C  
-ATOM  13312  C   ILE D 230     -17.610 -19.381-109.605  1.00 35.51           C  
-ATOM  13313  O   ILE D 230     -17.693 -18.148-109.678  1.00 38.40           O  
-ATOM  13314  CB  ILE D 230     -17.627 -20.077-107.164  1.00 25.38           C  
-ATOM  13315  CG1 ILE D 230     -18.344 -19.105-106.229  1.00 50.46           C  
-ATOM  13316  CG2 ILE D 230     -16.158 -19.739-107.342  1.00 27.98           C  
-ATOM  13317  CD1 ILE D 230     -19.265 -19.787-105.226  1.00 53.76           C  
-ATOM  13318  N   PHE D 231     -16.909 -20.126-110.452  1.00 27.26           N  
-ATOM  13319  CA  PHE D 231     -16.064 -19.583-111.499  1.00 28.81           C  
-ATOM  13320  C   PHE D 231     -16.278 -20.404-112.760  1.00 32.06           C  
-ATOM  13321  O   PHE D 231     -16.108 -21.617-112.738  1.00 39.06           O  
-ATOM  13322  CB  PHE D 231     -14.594 -19.620-111.061  1.00 36.08           C  
-ATOM  13323  CG  PHE D 231     -13.623 -19.146-112.109  1.00 40.94           C  
-ATOM  13324  CD1 PHE D 231     -13.171 -19.997-113.105  1.00 34.65           C  
-ATOM  13325  CD2 PHE D 231     -13.138 -17.854-112.077  1.00 51.09           C  
-ATOM  13326  CE1 PHE D 231     -12.276 -19.553-114.059  1.00 40.53           C  
-ATOM  13327  CE2 PHE D 231     -12.245 -17.405-113.025  1.00 51.41           C  
-ATOM  13328  CZ  PHE D 231     -11.812 -18.255-114.018  1.00 38.19           C  
-ATOM  13329  N   ILE D 232     -16.670 -19.755-113.851  1.00 31.82           N  
-ATOM  13330  CA  ILE D 232     -16.756 -20.434-115.144  1.00 28.54           C  
-ATOM  13331  C   ILE D 232     -16.156 -19.545-116.224  1.00 24.90           C  
-ATOM  13332  O   ILE D 232     -16.602 -18.416-116.423  1.00 27.53           O  
-ATOM  13333  CB  ILE D 232     -18.204 -20.798-115.525  1.00 27.91           C  
-ATOM  13334  CG1 ILE D 232     -18.778 -21.824-114.548  1.00 21.55           C  
-ATOM  13335  CG2 ILE D 232     -18.254 -21.356-116.941  1.00 25.36           C  
-ATOM  13336  CD1 ILE D 232     -20.174 -22.269-114.892  1.00 24.80           C  
-ATOM  13337  N   SER D 233     -15.154 -20.066-116.926  1.00 26.55           N  
-ATOM  13338  CA  SER D 233     -14.343 -19.256-117.828  1.00 27.19           C  
-ATOM  13339  C   SER D 233     -14.772 -19.320-119.289  1.00 25.07           C  
-ATOM  13340  O   SER D 233     -15.648 -20.096-119.670  1.00 23.43           O  
-ATOM  13341  CB  SER D 233     -12.875 -19.677-117.729  1.00 34.76           C  
-ATOM  13342  OG  SER D 233     -12.659 -20.926-118.366  1.00 25.80           O  
-ATOM  13343  N   LYS D 234     -14.128 -18.483-120.096  1.00 28.52           N  
-ATOM  13344  CA  LYS D 234     -14.258 -18.514-121.546  1.00 28.55           C  
-ATOM  13345  C   LYS D 234     -13.755 -19.859-122.065  1.00 31.71           C  
-ATOM  13346  O   LYS D 234     -12.923 -20.500-121.424  1.00 35.65           O  
-ATOM  13347  CB  LYS D 234     -13.471 -17.353-122.162  1.00 32.39           C  
-ATOM  13348  CG  LYS D 234     -13.405 -17.323-123.678  1.00 42.02           C  
-ATOM  13349  CD  LYS D 234     -12.013 -16.910-124.137  1.00 51.17           C  
-ATOM  13350  CE  LYS D 234     -11.509 -15.697-123.364  1.00 49.51           C  
-ATOM  13351  NZ  LYS D 234     -10.073 -15.413-123.642  1.00 52.72           N  
-ATOM  13352  N   THR D 235     -14.268 -20.301-123.209  1.00 30.75           N  
-ATOM  13353  CA  THR D 235     -13.816 -21.557-123.795  1.00 24.16           C  
-ATOM  13354  C   THR D 235     -12.503 -21.378-124.556  1.00 24.94           C  
-ATOM  13355  O   THR D 235     -12.407 -20.550-125.463  1.00 25.33           O  
-ATOM  13356  CB  THR D 235     -14.869 -22.148-124.746  1.00 22.12           C  
-ATOM  13357  OG1 THR D 235     -16.110 -22.310-124.048  1.00 21.00           O  
-ATOM  13358  CG2 THR D 235     -14.407 -23.496-125.272  1.00 28.46           C  
-ATOM  13359  N   PHE D 236     -11.493 -22.156-124.179  1.00 22.89           N  
-ATOM  13360  CA  PHE D 236     -10.208 -22.122-124.874  1.00 26.29           C  
-ATOM  13361  C   PHE D 236     -10.063 -23.352-125.759  1.00 27.52           C  
-ATOM  13362  O   PHE D 236     -10.896 -24.252-125.713  1.00 27.24           O  
-ATOM  13363  CB  PHE D 236      -9.052 -22.042-123.877  1.00 30.66           C  
-ATOM  13364  CG  PHE D 236      -9.065 -20.800-123.040  1.00 29.46           C  
-ATOM  13365  CD1 PHE D 236      -8.404 -19.660-123.463  1.00 38.64           C  
-ATOM  13366  CD2 PHE D 236      -9.744 -20.768-121.835  1.00 26.33           C  
-ATOM  13367  CE1 PHE D 236      -8.418 -18.513-122.700  1.00 37.00           C  
-ATOM  13368  CE2 PHE D 236      -9.761 -19.622-121.066  1.00 34.02           C  
-ATOM  13369  CZ  PHE D 236      -9.097 -18.493-121.500  1.00 39.64           C  
-ATOM  13370  N   SER D 237      -9.011 -23.393-126.568  1.00 31.64           N  
-ATOM  13371  CA  SER D 237      -8.791 -24.543-127.438  1.00 26.69           C  
-ATOM  13372  C   SER D 237      -7.331 -24.723-127.813  1.00 31.66           C  
-ATOM  13373  O   SER D 237      -6.646 -23.762-128.163  1.00 34.72           O  
-ATOM  13374  CB  SER D 237      -9.616 -24.416-128.714  1.00 22.79           C  
-ATOM  13375  OG  SER D 237      -9.043 -23.452-129.581  1.00 33.58           O  
-ATOM  13376  N   ASP D 238      -6.864 -25.965-127.748  1.00 27.90           N  
-ATOM  13377  CA  ASP D 238      -5.531 -26.299-128.228  1.00 27.36           C  
-ATOM  13378  C   ASP D 238      -5.533 -27.661-128.910  1.00 25.95           C  
-ATOM  13379  O   ASP D 238      -6.096 -28.626-128.388  1.00 26.00           O  
-ATOM  13380  CB  ASP D 238      -4.515 -26.278-127.086  1.00 32.29           C  
-ATOM  13381  CG  ASP D 238      -4.140 -24.870-126.668  1.00 35.81           C  
-ATOM  13382  OD1 ASP D 238      -3.348 -24.222-127.388  1.00 31.62           O  
-ATOM  13383  OD2 ASP D 238      -4.631 -24.411-125.615  1.00 38.07           O  
-ATOM  13384  N   ASN D 239      -4.909 -27.717-130.083  1.00 22.03           N  
-ATOM  13385  CA  ASN D 239      -4.784 -28.948-130.856  1.00 23.27           C  
-ATOM  13386  C   ASN D 239      -6.128 -29.604-131.158  1.00 23.43           C  
-ATOM  13387  O   ASN D 239      -6.233 -30.831-131.206  1.00 24.86           O  
-ATOM  13388  CB  ASN D 239      -3.874 -29.938-130.127  1.00 27.93           C  
-ATOM  13389  CG  ASN D 239      -2.439 -29.452-130.034  1.00 32.76           C  
-ATOM  13390  OD1 ASN D 239      -1.863 -28.991-131.019  1.00 34.28           O  
-ATOM  13391  ND2 ASN D 239      -1.856 -29.550-128.844  1.00 36.03           N  
-ATOM  13392  N   GLY D 240      -7.150 -28.783-131.369  1.00 17.60           N  
-ATOM  13393  CA  GLY D 240      -8.468 -29.289-131.706  1.00 31.09           C  
-ATOM  13394  C   GLY D 240      -9.237 -29.767-130.490  1.00 34.17           C  
-ATOM  13395  O   GLY D 240     -10.260 -30.447-130.612  1.00 27.42           O  
-ATOM  13396  N   VAL D 241      -8.734 -29.412-129.311  1.00 35.24           N  
-ATOM  13397  CA  VAL D 241      -9.395 -29.750-128.058  1.00 23.48           C  
-ATOM  13398  C   VAL D 241      -9.900 -28.493-127.372  1.00 25.40           C  
-ATOM  13399  O   VAL D 241      -9.105 -27.654-126.946  1.00 32.73           O  
-ATOM  13400  CB  VAL D 241      -8.457 -30.496-127.093  1.00 24.72           C  
-ATOM  13401  CG1 VAL D 241      -9.211 -30.895-125.831  1.00 22.84           C  
-ATOM  13402  CG2 VAL D 241      -7.848 -31.709-127.773  1.00 33.38           C  
-ATOM  13403  N   PRO D 242     -11.229 -28.352-127.281  1.00 21.59           N  
-ATOM  13404  CA  PRO D 242     -11.871 -27.258-126.550  1.00 20.70           C  
-ATOM  13405  C   PRO D 242     -11.963 -27.558-125.060  1.00 19.86           C  
-ATOM  13406  O   PRO D 242     -12.300 -28.681-124.696  1.00 20.74           O  
-ATOM  13407  CB  PRO D 242     -13.261 -27.194-127.180  1.00 16.45           C  
-ATOM  13408  CG  PRO D 242     -13.534 -28.600-127.593  1.00 12.70           C  
-ATOM  13409  CD  PRO D 242     -12.209 -29.185-128.000  1.00 18.75           C  
-ATOM  13410  N   TYR D 243     -11.664 -26.583-124.208  1.00 20.79           N  
-ATOM  13411  CA  TYR D 243     -11.819 -26.806-122.776  1.00 29.24           C  
-ATOM  13412  C   TYR D 243     -12.191 -25.565-121.967  1.00 28.18           C  
-ATOM  13413  O   TYR D 243     -12.120 -24.431-122.447  1.00 30.04           O  
-ATOM  13414  CB  TYR D 243     -10.551 -27.443-122.187  1.00 26.79           C  
-ATOM  13415  CG  TYR D 243      -9.235 -26.785-122.536  1.00 22.11           C  
-ATOM  13416  CD1 TYR D 243      -8.619 -27.028-123.755  1.00 26.20           C  
-ATOM  13417  CD2 TYR D 243      -8.583 -25.960-121.625  1.00 25.07           C  
-ATOM  13418  CE1 TYR D 243      -7.406 -26.447-124.071  1.00 30.32           C  
-ATOM  13419  CE2 TYR D 243      -7.367 -25.375-121.935  1.00 22.85           C  
-ATOM  13420  CZ  TYR D 243      -6.785 -25.625-123.159  1.00 24.01           C  
-ATOM  13421  OH  TYR D 243      -5.579 -25.053-123.481  1.00 26.57           O  
-ATOM  13422  N   ASP D 244     -12.601 -25.815-120.727  1.00 28.00           N  
-ATOM  13423  CA  ASP D 244     -13.084 -24.776-119.829  1.00 25.38           C  
-ATOM  13424  C   ASP D 244     -12.300 -24.767-118.528  1.00 34.89           C  
-ATOM  13425  O   ASP D 244     -11.579 -25.714-118.223  1.00 31.41           O  
-ATOM  13426  CB  ASP D 244     -14.567 -24.987-119.529  1.00 23.19           C  
-ATOM  13427  CG  ASP D 244     -15.417 -23.803-119.921  1.00 31.86           C  
-ATOM  13428  OD1 ASP D 244     -14.978 -23.014-120.784  1.00 38.92           O  
-ATOM  13429  OD2 ASP D 244     -16.529 -23.668-119.369  1.00 34.11           O  
-ATOM  13430  N   PHE D 245     -12.454 -23.693-117.762  1.00 37.11           N  
-ATOM  13431  CA  PHE D 245     -11.900 -23.628-116.416  1.00 29.23           C  
-ATOM  13432  C   PHE D 245     -12.992 -23.298-115.416  1.00 28.06           C  
-ATOM  13433  O   PHE D 245     -13.603 -22.233-115.486  1.00 28.52           O  
-ATOM  13434  CB  PHE D 245     -10.783 -22.588-116.321  1.00 23.18           C  
-ATOM  13435  CG  PHE D 245      -9.590 -22.899-117.169  1.00 31.51           C  
-ATOM  13436  CD1 PHE D 245      -8.839 -24.037-116.937  1.00 27.09           C  
-ATOM  13437  CD2 PHE D 245      -9.206 -22.040-118.184  1.00 33.88           C  
-ATOM  13438  CE1 PHE D 245      -7.735 -24.320-117.713  1.00 32.90           C  
-ATOM  13439  CE2 PHE D 245      -8.103 -22.315-118.962  1.00 32.18           C  
-ATOM  13440  CZ  PHE D 245      -7.365 -23.458-118.728  1.00 32.73           C  
-ATOM  13441  N   VAL D 246     -13.239 -24.209-114.482  1.00 32.22           N  
-ATOM  13442  CA  VAL D 246     -14.211 -23.947-113.432  1.00 31.82           C  
-ATOM  13443  C   VAL D 246     -13.601 -24.138-112.057  1.00 27.35           C  
-ATOM  13444  O   VAL D 246     -12.648 -24.896-111.887  1.00 28.52           O  
-ATOM  13445  CB  VAL D 246     -15.456 -24.846-113.550  1.00 22.54           C  
-ATOM  13446  CG1 VAL D 246     -16.267 -24.467-114.780  1.00 27.19           C  
-ATOM  13447  CG2 VAL D 246     -15.058 -26.311-113.575  1.00 21.24           C  
-ATOM  13448  N   VAL D 247     -14.152 -23.424-111.082  1.00 27.87           N  
-ATOM  13449  CA  VAL D 247     -13.766 -23.585-109.691  1.00 28.23           C  
-ATOM  13450  C   VAL D 247     -15.011 -23.887-108.865  1.00 30.14           C  
-ATOM  13451  O   VAL D 247     -15.992 -23.146-108.907  1.00 29.55           O  
-ATOM  13452  CB  VAL D 247     -13.055 -22.331-109.144  1.00 33.34           C  
-ATOM  13453  CG1 VAL D 247     -12.559 -22.579-107.728  1.00 42.84           C  
-ATOM  13454  CG2 VAL D 247     -11.901 -21.936-110.050  1.00 30.32           C  
-ATOM  13455  N   LEU D 248     -14.968 -24.992-108.130  1.00 27.35           N  
-ATOM  13456  CA  LEU D 248     -16.090 -25.424-107.308  1.00 28.77           C  
-ATOM  13457  C   LEU D 248     -15.740 -25.267-105.836  1.00 39.27           C  
-ATOM  13458  O   LEU D 248     -14.566 -25.260-105.474  1.00 46.52           O  
-ATOM  13459  CB  LEU D 248     -16.455 -26.881-107.607  1.00 31.61           C  
-ATOM  13460  CG  LEU D 248     -17.310 -27.249-108.822  1.00 31.18           C  
-ATOM  13461  CD1 LEU D 248     -16.730 -26.719-110.124  1.00 33.07           C  
-ATOM  13462  CD2 LEU D 248     -17.450 -28.759-108.891  1.00 37.93           C  
-ATOM  13463  N   GLU D 249     -16.754 -25.140-104.987  1.00 40.19           N  
-ATOM  13464  CA  GLU D 249     -16.525 -25.099-103.548  1.00 38.49           C  
-ATOM  13465  C   GLU D 249     -17.549 -25.955-102.814  1.00 42.38           C  
-ATOM  13466  O   GLU D 249     -18.659 -26.168-103.307  1.00 52.16           O  
-ATOM  13467  CB  GLU D 249     -16.568 -23.661-103.027  1.00 37.59           C  
-ATOM  13468  CG  GLU D 249     -17.954 -23.034-103.004  1.00 46.73           C  
-ATOM  13469  CD  GLU D 249     -17.976 -21.717-102.250  1.00 58.68           C  
-ATOM  13470  OE1 GLU D 249     -16.899 -21.283-101.785  1.00 53.18           O  
-ATOM  13471  OE2 GLU D 249     -19.067 -21.118-102.119  1.00 53.78           O  
-ATOM  13472  N   LYS D 250     -17.169 -26.452-101.640  1.00 36.67           N  
-ATOM  13473  CA  LYS D 250     -18.101 -27.204-100.804  1.00 38.51           C  
-ATOM  13474  C   LYS D 250     -19.143 -26.289-100.166  1.00 51.47           C  
-ATOM  13475  O   LYS D 250     -18.810 -25.238 -99.615  1.00 54.77           O  
-ATOM  13476  CB  LYS D 250     -17.358 -27.973 -99.712  1.00 44.49           C  
-ATOM  13477  CG  LYS D 250     -16.902 -29.359-100.128  1.00 48.80           C  
-ATOM  13478  CD  LYS D 250     -16.588 -30.224 -98.918  1.00 49.05           C  
-ATOM  13479  CE  LYS D 250     -15.483 -29.617 -98.069  1.00 55.62           C  
-ATOM  13480  NZ  LYS D 250     -15.165 -30.471 -96.891  1.00 47.13           N  
-ATOM  13481  N   ARG D 251     -20.406 -26.696-100.244  1.00 50.15           N  
-ATOM  13482  CA  ARG D 251     -21.496 -25.937 -99.642  1.00 57.06           C  
-ATOM  13483  C   ARG D 251     -22.512 -26.853 -98.965  1.00 57.31           C  
-ATOM  13484  O   ARG D 251     -22.307 -28.061 -98.864  1.00 50.01           O  
-ATOM  13485  CB  ARG D 251     -22.193 -25.067-100.692  1.00 55.37           C  
-ATOM  13486  CG  ARG D 251     -21.684 -23.634-100.747  1.00 63.27           C  
-ATOM  13487  CD  ARG D 251     -21.816 -22.944 -99.390  1.00 82.95           C  
-ATOM  13488  NE  ARG D 251     -23.159 -23.087 -98.828  1.00 92.60           N  
-ATOM  13489  CZ  ARG D 251     -23.424 -23.571 -97.616  1.00 87.47           C  
-ATOM  13490  NH1 ARG D 251     -24.681 -23.663 -97.200  1.00 80.29           N  
-ATOM  13491  NH2 ARG D 251     -22.437 -23.960 -96.818  1.00 64.29           N  
-ATOM  13492  N   SER D 285     -12.495  10.506 -99.243  1.00 67.48           N  
-ATOM  13493  CA  SER D 285     -12.749  11.943 -99.252  1.00 70.95           C  
-ATOM  13494  C   SER D 285     -13.743  12.328-100.342  1.00 59.56           C  
-ATOM  13495  O   SER D 285     -14.814  12.862-100.055  1.00 58.95           O  
-ATOM  13496  CB  SER D 285     -11.444  12.722 -99.440  1.00 73.52           C  
-ATOM  13497  OG  SER D 285     -10.606  12.610 -98.302  1.00 80.74           O  
-ATOM  13498  N   SER D 286     -13.381  12.055-101.592  1.00 58.40           N  
-ATOM  13499  CA  SER D 286     -14.227  12.407-102.726  1.00 52.98           C  
-ATOM  13500  C   SER D 286     -15.412  11.454-102.859  1.00 52.18           C  
-ATOM  13501  O   SER D 286     -16.489  11.851-103.300  1.00 52.56           O  
-ATOM  13502  CB  SER D 286     -13.412  12.415-104.019  1.00 40.32           C  
-ATOM  13503  OG  SER D 286     -12.944  11.119-104.320  1.00 53.50           O  
-ATOM  13504  N   ALA D 287     -15.207  10.195-102.483  1.00 56.04           N  
-ATOM  13505  CA  ALA D 287     -16.280   9.207-102.529  1.00 48.50           C  
-ATOM  13506  C   ALA D 287     -17.387   9.591-101.554  1.00 48.66           C  
-ATOM  13507  O   ALA D 287     -18.572   9.383-101.821  1.00 46.47           O  
-ATOM  13508  CB  ALA D 287     -15.742   7.816-102.213  1.00 36.66           C  
-ATOM  13509  N   ALA D 288     -16.984  10.166-100.425  1.00 52.98           N  
-ATOM  13510  CA  ALA D 288     -17.924  10.595 -99.399  1.00 55.65           C  
-ATOM  13511  C   ALA D 288     -18.706  11.816 -99.862  1.00 51.53           C  
-ATOM  13512  O   ALA D 288     -19.893  11.945 -99.576  1.00 51.01           O  
-ATOM  13513  CB  ALA D 288     -17.193  10.892 -98.101  1.00 64.28           C  
-ATOM  13514  N   ALA D 289     -18.033  12.711-100.577  1.00 43.70           N  
-ATOM  13515  CA  ALA D 289     -18.684  13.896-101.123  1.00 37.12           C  
-ATOM  13516  C   ALA D 289     -19.660  13.520-102.229  1.00 36.41           C  
-ATOM  13517  O   ALA D 289     -20.710  14.143-102.386  1.00 41.58           O  
-ATOM  13518  CB  ALA D 289     -17.647  14.878-101.645  1.00 34.37           C  
-ATOM  13519  N   ILE D 290     -19.306  12.493-102.992  1.00 38.63           N  
-ATOM  13520  CA  ILE D 290     -20.109  12.063-104.130  1.00 43.23           C  
-ATOM  13521  C   ILE D 290     -21.334  11.269-103.676  1.00 44.48           C  
-ATOM  13522  O   ILE D 290     -22.426  11.420-104.229  1.00 41.29           O  
-ATOM  13523  CB  ILE D 290     -19.256  11.218-105.117  1.00 51.59           C  
-ATOM  13524  CG1 ILE D 290     -18.245  12.114-105.836  1.00 46.54           C  
-ATOM  13525  CG2 ILE D 290     -20.125  10.500-106.133  1.00 44.93           C  
-ATOM  13526  CD1 ILE D 290     -17.313  11.362-106.769  1.00 47.30           C  
-ATOM  13527  N   ALA D 291     -21.140  10.454-102.644  1.00 47.18           N  
-ATOM  13528  CA  ALA D 291     -22.141   9.503-102.155  1.00 48.74           C  
-ATOM  13529  C   ALA D 291     -23.581  10.032-102.011  1.00 49.12           C  
-ATOM  13530  O   ALA D 291     -24.509   9.410-102.532  1.00 45.86           O  
-ATOM  13531  CB  ALA D 291     -21.672   8.921-100.819  1.00 47.38           C  
-ATOM  13532  N   PRO D 292     -23.783  11.172-101.316  1.00 42.50           N  
-ATOM  13533  CA  PRO D 292     -25.180  11.556-101.075  1.00 37.84           C  
-ATOM  13534  C   PRO D 292     -25.934  11.993-102.329  1.00 37.65           C  
-ATOM  13535  O   PRO D 292     -27.151  12.151-102.267  1.00 44.45           O  
-ATOM  13536  CB  PRO D 292     -25.054  12.723-100.094  1.00 38.24           C  
-ATOM  13537  CG  PRO D 292     -23.729  13.311-100.389  1.00 41.28           C  
-ATOM  13538  CD  PRO D 292     -22.846  12.145-100.725  1.00 42.41           C  
-ATOM  13539  N   VAL D 293     -25.230  12.187-103.440  1.00 37.24           N  
-ATOM  13540  CA  VAL D 293     -25.883  12.545-104.695  1.00 41.53           C  
-ATOM  13541  C   VAL D 293     -26.304  11.275-105.427  1.00 42.40           C  
-ATOM  13542  O   VAL D 293     -27.444  11.152-105.895  1.00 41.15           O  
-ATOM  13543  CB  VAL D 293     -24.965  13.391-105.593  1.00 35.67           C  
-ATOM  13544  CG1 VAL D 293     -25.734  13.910-106.791  1.00 32.08           C  
-ATOM  13545  CG2 VAL D 293     -24.376  14.548-104.804  1.00 33.60           C  
-ATOM  13546  N   LEU D 294     -25.369  10.333-105.511  1.00 43.67           N  
-ATOM  13547  CA  LEU D 294     -25.650   8.993-106.006  1.00 35.37           C  
-ATOM  13548  C   LEU D 294     -26.828   8.388-105.259  1.00 43.91           C  
-ATOM  13549  O   LEU D 294     -27.625   7.650-105.837  1.00 55.13           O  
-ATOM  13550  CB  LEU D 294     -24.426   8.090-105.855  1.00 31.13           C  
-ATOM  13551  CG  LEU D 294     -23.165   8.486-106.617  1.00 35.59           C  
-ATOM  13552  CD1 LEU D 294     -22.083   7.436-106.430  1.00 41.47           C  
-ATOM  13553  CD2 LEU D 294     -23.473   8.682-108.087  1.00 33.40           C  
-ATOM  13554  N   ALA D 295     -26.928   8.711-103.971  1.00 40.40           N  
-ATOM  13555  CA  ALA D 295     -28.013   8.222-103.130  1.00 41.53           C  
-ATOM  13556  C   ALA D 295     -29.380   8.597-103.697  1.00 45.07           C  
-ATOM  13557  O   ALA D 295     -30.168   7.721-104.061  1.00 45.96           O  
-ATOM  13558  CB  ALA D 295     -27.865   8.756-101.713  1.00 37.75           C  
-ATOM  13559  N   TRP D 296     -29.655   9.896-103.782  1.00 43.55           N  
-ATOM  13560  CA  TRP D 296     -30.960  10.359-104.241  1.00 43.57           C  
-ATOM  13561  C   TRP D 296     -31.161  10.076-105.722  1.00 44.61           C  
-ATOM  13562  O   TRP D 296     -32.294   9.927-106.177  1.00 53.89           O  
-ATOM  13563  CB  TRP D 296     -31.154  11.856-103.959  1.00 39.78           C  
-ATOM  13564  CG  TRP D 296     -30.420  12.806-104.873  1.00 40.94           C  
-ATOM  13565  CD1 TRP D 296     -29.241  13.441-104.616  1.00 44.73           C  
-ATOM  13566  CD2 TRP D 296     -30.838  13.251-106.173  1.00 37.98           C  
-ATOM  13567  NE1 TRP D 296     -28.890  14.241-105.678  1.00 32.85           N  
-ATOM  13568  CE2 TRP D 296     -29.854  14.141-106.646  1.00 32.70           C  
-ATOM  13569  CE3 TRP D 296     -31.943  12.975-106.986  1.00 38.59           C  
-ATOM  13570  CZ2 TRP D 296     -29.941  14.756-107.891  1.00 36.09           C  
-ATOM  13571  CZ3 TRP D 296     -32.026  13.584-108.223  1.00 26.76           C  
-ATOM  13572  CH2 TRP D 296     -31.031  14.464-108.664  1.00 36.35           C  
-ATOM  13573  N   MET D 297     -30.070   9.999-106.477  1.00 36.69           N  
-ATOM  13574  CA  MET D 297     -30.184   9.681-107.895  1.00 36.28           C  
-ATOM  13575  C   MET D 297     -30.588   8.224-108.105  1.00 45.60           C  
-ATOM  13576  O   MET D 297     -31.272   7.899-109.076  1.00 51.12           O  
-ATOM  13577  CB  MET D 297     -28.875   9.979-108.622  1.00 41.51           C  
-ATOM  13578  CG  MET D 297     -28.649  11.459-108.866  1.00 31.00           C  
-ATOM  13579  SD  MET D 297     -27.246  11.787-109.939  1.00 29.89           S  
-ATOM  13580  CE  MET D 297     -27.355  13.569-110.075  1.00 32.23           C  
-ATOM  13581  N   ASP D 298     -30.174   7.352-107.189  1.00 54.80           N  
-ATOM  13582  CA  ASP D 298     -30.507   5.933-107.284  1.00 67.42           C  
-ATOM  13583  C   ASP D 298     -31.893   5.649-106.706  1.00 64.42           C  
-ATOM  13584  O   ASP D 298     -32.658   4.879-107.288  1.00 62.52           O  
-ATOM  13585  CB  ASP D 298     -29.451   5.079-106.570  1.00 56.22           C  
-ATOM  13586  CG  ASP D 298     -29.512   3.610-106.971  1.00 65.72           C  
-ATOM  13587  OD1 ASP D 298     -30.541   3.171-107.531  1.00 79.75           O  
-ATOM  13588  OD2 ASP D 298     -28.526   2.887-106.722  1.00 70.29           O  
-ATOM  13589  N   GLU D 299     -32.193   6.278-105.568  1.00 55.40           N  
-ATOM  13590  CA  GLU D 299     -33.436   6.075-104.811  1.00 58.08           C  
-ATOM  13591  C   GLU D 299     -34.649   5.695-105.655  1.00 64.71           C  
-ATOM  13592  O   GLU D 299     -35.183   4.592-105.534  1.00 64.37           O  
-ATOM  13593  CB  GLU D 299     -33.769   7.335-104.010  1.00 53.95           C  
-ATOM  13594  CG  GLU D 299     -32.995   7.464-102.713  1.00 69.86           C  
-ATOM  13595  CD  GLU D 299     -33.323   8.743-101.971  1.00 75.26           C  
-ATOM  13596  OE1 GLU D 299     -34.282   9.437-102.377  1.00 60.55           O  
-ATOM  13597  OE2 GLU D 299     -32.620   9.054-100.985  1.00 65.52           O  
-ATOM  13598  N   GLU D 300     -35.074   6.615-106.511  1.00 68.70           N  
-ATOM  13599  CA  GLU D 300     -36.182   6.360-107.419  1.00 80.43           C  
-ATOM  13600  C   GLU D 300     -35.668   6.162-108.844  1.00 81.22           C  
-ATOM  13601  O   GLU D 300     -35.109   7.083-109.440  1.00 83.60           O  
-ATOM  13602  CB  GLU D 300     -37.194   7.506-107.361  1.00 90.96           C  
-ATOM  13603  CG  GLU D 300     -38.123   7.587-108.559  1.00 95.39           C  
-ATOM  13604  CD  GLU D 300     -37.811   8.775-109.449  1.00 93.50           C  
-ATOM  13605  OE1 GLU D 300     -37.934   8.645-110.687  1.00 74.69           O  
-ATOM  13606  OE2 GLU D 300     -37.448   9.842-108.908  1.00 95.63           O  
-ATOM  13607  N   ASP D 301     -35.843   4.957-109.382  1.00 71.09           N  
-ATOM  13608  CA  ASP D 301     -36.497   3.868-108.663  1.00 69.70           C  
-ATOM  13609  C   ASP D 301     -35.470   2.917-108.051  1.00 55.72           C  
-ATOM  13610  O   ASP D 301     -34.507   2.518-108.707  1.00 36.11           O  
-ATOM  13611  CB  ASP D 301     -37.437   3.102-109.598  1.00 88.16           C  
-ATOM  13612  CG  ASP D 301     -38.597   2.450-108.862  1.00 94.18           C  
-ATOM  13613  OD1 ASP D 301     -39.230   3.126-108.022  1.00 73.53           O  
-ATOM  13614  OD2 ASP D 301     -38.875   1.260-109.125  1.00 89.30           O  
-ATOM  13615  N   LYS D 308     -39.899  -7.236-109.038  1.00 59.70           N  
-ATOM  13616  CA  LYS D 308     -39.877  -7.115-107.586  1.00 71.11           C  
-ATOM  13617  C   LYS D 308     -38.758  -7.970-107.000  1.00 61.15           C  
-ATOM  13618  O   LYS D 308     -37.971  -7.505-106.175  1.00 49.64           O  
-ATOM  13619  CB  LYS D 308     -41.231  -7.517-106.994  1.00 68.98           C  
-ATOM  13620  CG  LYS D 308     -41.653  -6.700-105.779  1.00 65.29           C  
-ATOM  13621  CD  LYS D 308     -41.986  -5.258-106.154  1.00 65.15           C  
-ATOM  13622  CE  LYS D 308     -40.903  -4.286-105.701  1.00 63.11           C  
-ATOM  13623  NZ  LYS D 308     -41.238  -2.882-106.071  1.00 58.77           N  
-ATOM  13624  N   GLU D 309     -38.701  -9.226-107.434  1.00 53.60           N  
-ATOM  13625  CA  GLU D 309     -37.595 -10.113-107.092  1.00 63.44           C  
-ATOM  13626  C   GLU D 309     -36.830 -10.497-108.354  1.00 63.28           C  
-ATOM  13627  O   GLU D 309     -37.285 -11.324-109.148  1.00 51.91           O  
-ATOM  13628  CB  GLU D 309     -38.098 -11.360-106.361  1.00 64.27           C  
-ATOM  13629  CG  GLU D 309     -37.852 -11.329-104.859  1.00 77.07           C  
-ATOM  13630  CD  GLU D 309     -38.549 -12.460-104.127  1.00 88.58           C  
-ATOM  13631  OE1 GLU D 309     -39.785 -12.390-103.965  1.00 82.86           O  
-ATOM  13632  OE2 GLU D 309     -37.863 -13.419-103.714  1.00 92.02           O  
-ATOM  13633  N   LEU D 310     -35.667  -9.877-108.527  1.00 58.26           N  
-ATOM  13634  CA  LEU D 310     -34.852 -10.048-109.722  1.00 45.30           C  
-ATOM  13635  C   LEU D 310     -34.408 -11.490-109.908  1.00 40.20           C  
-ATOM  13636  O   LEU D 310     -33.747 -12.055-109.038  1.00 50.53           O  
-ATOM  13637  CB  LEU D 310     -33.619  -9.142-109.655  1.00 51.38           C  
-ATOM  13638  CG  LEU D 310     -33.826  -7.682-109.254  1.00 40.72           C  
-ATOM  13639  CD1 LEU D 310     -32.800  -7.283-108.206  1.00 45.44           C  
-ATOM  13640  CD2 LEU D 310     -33.742  -6.767-110.467  1.00 28.62           C  
-ATOM  13641  N   ILE D 311     -34.770 -12.084-111.041  1.00 39.77           N  
-ATOM  13642  CA  ILE D 311     -34.256 -13.402-111.388  1.00 44.43           C  
-ATOM  13643  C   ILE D 311     -32.853 -13.236-111.964  1.00 45.12           C  
-ATOM  13644  O   ILE D 311     -32.524 -12.191-112.531  1.00 32.77           O  
-ATOM  13645  CB  ILE D 311     -35.170 -14.146-112.393  1.00 38.80           C  
-ATOM  13646  CG1 ILE D 311     -34.981 -13.619-113.815  1.00 40.67           C  
-ATOM  13647  CG2 ILE D 311     -36.624 -14.037-111.977  1.00 51.97           C  
-ATOM  13648  CD1 ILE D 311     -34.344 -14.624-114.753  1.00 42.22           C  
-ATOM  13649  N   ARG D 312     -32.022 -14.260-111.808  1.00 39.24           N  
-ATOM  13650  CA  ARG D 312     -30.636 -14.171-112.246  1.00 35.58           C  
-ATOM  13651  C   ARG D 312     -30.074 -15.538-112.612  1.00 40.38           C  
-ATOM  13652  O   ARG D 312     -30.339 -16.531-111.936  1.00 46.22           O  
-ATOM  13653  CB  ARG D 312     -29.779 -13.519-111.158  1.00 39.55           C  
-ATOM  13654  CG  ARG D 312     -28.297 -13.447-111.486  1.00 45.49           C  
-ATOM  13655  CD  ARG D 312     -27.584 -12.446-110.594  1.00 57.30           C  
-ATOM  13656  NE  ARG D 312     -26.148 -12.393-110.855  1.00 60.34           N  
-ATOM  13657  CZ  ARG D 312     -25.590 -11.702-111.846  1.00 66.27           C  
-ATOM  13658  NH1 ARG D 312     -24.273 -11.710-112.001  1.00 54.86           N  
-ATOM  13659  NH2 ARG D 312     -26.346 -11.004-112.684  1.00 67.08           N  
-ATOM  13660  N   ALA D 313     -29.304 -15.580-113.695  1.00 35.63           N  
-ATOM  13661  CA  ALA D 313     -28.664 -16.813-114.133  1.00 39.35           C  
-ATOM  13662  C   ALA D 313     -27.648 -17.290-113.106  1.00 42.10           C  
-ATOM  13663  O   ALA D 313     -26.727 -16.548-112.762  1.00 41.46           O  
-ATOM  13664  CB  ALA D 313     -27.995 -16.612-115.479  1.00 34.11           C  
-ATOM  13665  N   VAL D 314     -27.824 -18.534-112.653  1.00 37.46           N  
-ATOM  13666  CA  VAL D 314     -26.976 -19.202-111.656  1.00 33.02           C  
-ATOM  13667  C   VAL D 314     -26.176 -18.250-110.762  1.00 34.15           C  
-ATOM  13668  O   VAL D 314     -24.961 -18.121-110.908  1.00 33.48           O  
-ATOM  13669  CB  VAL D 314     -25.999 -20.199-112.337  1.00 33.93           C  
-ATOM  13670  CG1 VAL D 314     -26.727 -21.485-112.693  1.00 31.08           C  
-ATOM  13671  CG2 VAL D 314     -25.353 -19.590-113.580  1.00 29.60           C  
-ATOM  13672  N   PRO D 315     -26.867 -17.584-109.823  1.00 37.58           N  
-ATOM  13673  CA  PRO D 315     -26.301 -16.513-108.990  1.00 44.54           C  
-ATOM  13674  C   PRO D 315     -25.127 -16.947-108.113  1.00 34.16           C  
-ATOM  13675  O   PRO D 315     -24.405 -16.095-107.596  1.00 37.99           O  
-ATOM  13676  CB  PRO D 315     -27.491 -16.085-108.120  1.00 38.74           C  
-ATOM  13677  CG  PRO D 315     -28.384 -17.272-108.094  1.00 37.54           C  
-ATOM  13678  CD  PRO D 315     -28.259 -17.888-109.453  1.00 37.40           C  
-ATOM  13679  N   HIS D 316     -24.938 -18.251-107.948  1.00 35.28           N  
-ATOM  13680  CA  HIS D 316     -23.828 -18.761-107.153  1.00 41.17           C  
-ATOM  13681  C   HIS D 316     -22.501 -18.632-107.896  1.00 37.75           C  
-ATOM  13682  O   HIS D 316     -21.435 -18.729-107.296  1.00 40.10           O  
-ATOM  13683  CB  HIS D 316     -24.075 -20.218-106.766  1.00 35.54           C  
-ATOM  13684  CG  HIS D 316     -24.497 -21.082-107.911  1.00 39.33           C  
-ATOM  13685  ND1 HIS D 316     -25.818 -21.261-108.260  1.00 45.28           N  
-ATOM  13686  CD2 HIS D 316     -23.773 -21.813-108.792  1.00 43.97           C  
-ATOM  13687  CE1 HIS D 316     -25.891 -22.068-109.304  1.00 46.40           C  
-ATOM  13688  NE2 HIS D 316     -24.664 -22.417-109.646  1.00 42.01           N  
-ATOM  13689  N   VAL D 317     -22.568 -18.414-109.203  1.00 37.46           N  
-ATOM  13690  CA  VAL D 317     -21.361 -18.229-109.996  1.00 35.24           C  
-ATOM  13691  C   VAL D 317     -20.996 -16.753-110.056  1.00 40.21           C  
-ATOM  13692  O   VAL D 317     -21.619 -15.981-110.783  1.00 38.03           O  
-ATOM  13693  CB  VAL D 317     -21.526 -18.770-111.426  1.00 40.36           C  
-ATOM  13694  CG1 VAL D 317     -20.259 -18.528-112.237  1.00 40.12           C  
-ATOM  13695  CG2 VAL D 317     -21.875 -20.251-111.398  1.00 27.18           C  
-ATOM  13696  N   HIS D 318     -19.981 -16.367-109.287  1.00 53.28           N  
-ATOM  13697  CA  HIS D 318     -19.561 -14.970-109.223  1.00 56.19           C  
-ATOM  13698  C   HIS D 318     -18.684 -14.567-110.404  1.00 47.39           C  
-ATOM  13699  O   HIS D 318     -18.887 -13.509-110.995  1.00 46.67           O  
-ATOM  13700  CB  HIS D 318     -18.834 -14.691-107.905  1.00 57.76           C  
-ATOM  13701  CG  HIS D 318     -19.694 -14.022-106.880  1.00 78.83           C  
-ATOM  13702  ND1 HIS D 318     -19.910 -12.661-106.866  1.00 80.08           N  
-ATOM  13703  CD2 HIS D 318     -20.394 -14.525-105.835  1.00 72.74           C  
-ATOM  13704  CE1 HIS D 318     -20.704 -12.353-105.856  1.00 76.19           C  
-ATOM  13705  NE2 HIS D 318     -21.012 -13.466-105.214  1.00 80.25           N  
-ATOM  13706  N   PHE D 319     -17.709 -15.401-110.750  1.00 49.64           N  
-ATOM  13707  CA  PHE D 319     -16.826 -15.070-111.869  1.00 52.57           C  
-ATOM  13708  C   PHE D 319     -17.308 -15.737-113.156  1.00 42.62           C  
-ATOM  13709  O   PHE D 319     -17.051 -16.916-113.401  1.00 42.29           O  
-ATOM  13710  CB  PHE D 319     -15.381 -15.463-111.552  1.00 54.48           C  
-ATOM  13711  CG  PHE D 319     -14.903 -14.970-110.213  1.00 69.36           C  
-ATOM  13712  CD1 PHE D 319     -14.618 -13.627-110.015  1.00 67.52           C  
-ATOM  13713  CD2 PHE D 319     -14.748 -15.847-109.150  1.00 65.38           C  
-ATOM  13714  CE1 PHE D 319     -14.186 -13.169-108.782  1.00 64.09           C  
-ATOM  13715  CE2 PHE D 319     -14.314 -15.395-107.916  1.00 69.31           C  
-ATOM  13716  CZ  PHE D 319     -14.034 -14.054-107.732  1.00 71.67           C  
-ATOM  13717  N   ARG D 320     -17.999 -14.953-113.977  1.00 34.38           N  
-ATOM  13718  CA  ARG D 320     -18.748 -15.470-115.116  1.00 31.47           C  
-ATOM  13719  C   ARG D 320     -18.082 -15.146-116.450  1.00 25.43           C  
-ATOM  13720  O   ARG D 320     -18.526 -14.255-117.175  1.00 22.87           O  
-ATOM  13721  CB  ARG D 320     -20.165 -14.900-115.083  1.00 32.57           C  
-ATOM  13722  CG  ARG D 320     -20.793 -14.962-113.701  1.00 30.95           C  
-ATOM  13723  CD  ARG D 320     -21.942 -13.987-113.550  1.00 30.53           C  
-ATOM  13724  NE  ARG D 320     -23.216 -14.677-113.377  1.00 35.68           N  
-ATOM  13725  CZ  ARG D 320     -24.253 -14.543-114.195  1.00 36.33           C  
-ATOM  13726  NH1 ARG D 320     -25.373 -15.211-113.960  1.00 32.25           N  
-ATOM  13727  NH2 ARG D 320     -24.172 -13.736-115.245  1.00 35.20           N  
-ATOM  13728  N   GLY D 321     -17.024 -15.884-116.774  1.00 25.16           N  
-ATOM  13729  CA  GLY D 321     -16.252 -15.632-117.978  1.00 24.72           C  
-ATOM  13730  C   GLY D 321     -16.831 -16.249-119.238  1.00 22.96           C  
-ATOM  13731  O   GLY D 321     -16.459 -15.863-120.346  1.00 25.70           O  
-ATOM  13732  N   HIS D 322     -17.735 -17.210-119.074  1.00 20.44           N  
-ATOM  13733  CA  HIS D 322     -18.353 -17.874-120.217  1.00 26.04           C  
-ATOM  13734  C   HIS D 322     -19.164 -16.872-121.027  1.00 26.88           C  
-ATOM  13735  O   HIS D 322     -19.839 -16.014-120.461  1.00 30.26           O  
-ATOM  13736  CB  HIS D 322     -19.242 -19.032-119.758  1.00 28.89           C  
-ATOM  13737  CG  HIS D 322     -19.420 -20.103-120.790  1.00 33.70           C  
-ATOM  13738  ND1 HIS D 322     -20.010 -19.869-122.014  1.00 24.16           N  
-ATOM  13739  CD2 HIS D 322     -19.089 -21.415-120.776  1.00 26.77           C  
-ATOM  13740  CE1 HIS D 322     -20.032 -20.992-122.709  1.00 22.65           C  
-ATOM  13741  NE2 HIS D 322     -19.480 -21.945-121.981  1.00 22.63           N  
-ATOM  13742  N   GLU D 323     -19.097 -16.982-122.351  1.00 25.48           N  
-ATOM  13743  CA  GLU D 323     -19.751 -16.014-123.223  1.00 22.33           C  
-ATOM  13744  C   GLU D 323     -21.251 -16.284-123.370  1.00 27.62           C  
-ATOM  13745  O   GLU D 323     -21.976 -15.468-123.937  1.00 29.84           O  
-ATOM  13746  CB  GLU D 323     -19.074 -15.995-124.597  1.00 20.00           C  
-ATOM  13747  CG  GLU D 323     -17.632 -15.493-124.561  1.00 24.01           C  
-ATOM  13748  CD  GLU D 323     -16.992 -15.405-125.937  1.00 26.09           C  
-ATOM  13749  OE1 GLU D 323     -15.764 -15.185-126.008  1.00 30.97           O  
-ATOM  13750  OE2 GLU D 323     -17.711 -15.553-126.947  1.00 26.30           O  
-ATOM  13751  N   GLU D 324     -21.713 -17.420-122.847  1.00 23.11           N  
-ATOM  13752  CA  GLU D 324     -23.136 -17.764-122.861  1.00 19.73           C  
-ATOM  13753  C   GLU D 324     -23.894 -16.966-121.795  1.00 28.89           C  
-ATOM  13754  O   GLU D 324     -25.121 -16.770-121.872  1.00 32.92           O  
-ATOM  13755  CB  GLU D 324     -23.315 -19.271-122.648  1.00 18.65           C  
-ATOM  13756  CG  GLU D 324     -24.753 -19.759-122.738  1.00 20.61           C  
-ATOM  13757  CD  GLU D 324     -24.854 -21.208-123.181  1.00 24.59           C  
-ATOM  13758  OE1 GLU D 324     -25.982 -21.740-123.261  1.00 19.00           O  
-ATOM  13759  OE2 GLU D 324     -23.800 -21.815-123.463  1.00 33.63           O  
-ATOM  13760  N   PHE D 325     -23.142 -16.492-120.806  1.00 26.05           N  
-ATOM  13761  CA  PHE D 325     -23.683 -15.621-119.774  1.00 22.33           C  
-ATOM  13762  C   PHE D 325     -24.219 -14.329-120.379  1.00 27.79           C  
-ATOM  13763  O   PHE D 325     -25.036 -13.650-119.767  1.00 35.42           O  
-ATOM  13764  CB  PHE D 325     -22.621 -15.306-118.717  1.00 25.66           C  
-ATOM  13765  CG  PHE D 325     -22.421 -16.401-117.711  1.00 25.61           C  
-ATOM  13766  CD1 PHE D 325     -23.440 -16.752-116.844  1.00 26.88           C  
-ATOM  13767  CD2 PHE D 325     -21.211 -17.068-117.622  1.00 31.58           C  
-ATOM  13768  CE1 PHE D 325     -23.262 -17.757-115.909  1.00 31.34           C  
-ATOM  13769  CE2 PHE D 325     -21.024 -18.074-116.687  1.00 35.06           C  
-ATOM  13770  CZ  PHE D 325     -22.052 -18.417-115.830  1.00 32.28           C  
-ATOM  13771  N   GLN D 326     -23.748 -13.990-121.576  1.00 21.79           N  
-ATOM  13772  CA  GLN D 326     -24.325 -12.883-122.324  1.00 23.71           C  
-ATOM  13773  C   GLN D 326     -25.795 -13.161-122.592  1.00 25.94           C  
-ATOM  13774  O   GLN D 326     -26.664 -12.331-122.316  1.00 27.53           O  
-ATOM  13775  CB  GLN D 326     -23.588 -12.669-123.645  1.00 20.92           C  
-ATOM  13776  CG  GLN D 326     -22.152 -12.219-123.498  1.00 18.38           C  
-ATOM  13777  CD  GLN D 326     -21.572 -11.742-124.812  1.00 21.93           C  
-ATOM  13778  OE1 GLN D 326     -21.847 -10.627-125.258  1.00 22.31           O  
-ATOM  13779  NE2 GLN D 326     -20.774 -12.589-125.448  1.00 31.94           N  
-ATOM  13780  N   TYR D 327     -26.056 -14.348-123.129  1.00 23.41           N  
-ATOM  13781  CA  TYR D 327     -27.404 -14.778-123.469  1.00 20.50           C  
-ATOM  13782  C   TYR D 327     -28.276 -14.940-122.230  1.00 21.06           C  
-ATOM  13783  O   TYR D 327     -29.410 -14.448-122.188  1.00 21.90           O  
-ATOM  13784  CB  TYR D 327     -27.349 -16.090-124.255  1.00 15.58           C  
-ATOM  13785  CG  TYR D 327     -28.697 -16.695-124.558  1.00 15.72           C  
-ATOM  13786  CD1 TYR D 327     -29.496 -16.186-125.573  1.00 16.24           C  
-ATOM  13787  CD2 TYR D 327     -29.165 -17.783-123.836  1.00 16.78           C  
-ATOM  13788  CE1 TYR D 327     -30.729 -16.739-125.855  1.00 15.12           C  
-ATOM  13789  CE2 TYR D 327     -30.395 -18.344-124.112  1.00 20.07           C  
-ATOM  13790  CZ  TYR D 327     -31.172 -17.819-125.121  1.00 20.90           C  
-ATOM  13791  OH  TYR D 327     -32.397 -18.381-125.394  1.00 30.55           O  
-ATOM  13792  N   LEU D 328     -27.746 -15.627-121.223  1.00 20.13           N  
-ATOM  13793  CA  LEU D 328     -28.497 -15.828-119.988  1.00 25.75           C  
-ATOM  13794  C   LEU D 328     -28.857 -14.495-119.323  1.00 27.86           C  
-ATOM  13795  O   LEU D 328     -30.014 -14.274-118.940  1.00 32.76           O  
-ATOM  13796  CB  LEU D 328     -27.708 -16.708-119.021  1.00 23.09           C  
-ATOM  13797  CG  LEU D 328     -27.428 -18.128-119.516  1.00 22.06           C  
-ATOM  13798  CD1 LEU D 328     -26.741 -18.955-118.439  1.00 24.03           C  
-ATOM  13799  CD2 LEU D 328     -28.713 -18.798-119.977  1.00 20.38           C  
-ATOM  13800  N   ASP D 329     -27.875 -13.606-119.203  1.00 23.75           N  
-ATOM  13801  CA  ASP D 329     -28.114 -12.288-118.623  1.00 25.74           C  
-ATOM  13802  C   ASP D 329     -29.038 -11.453-119.494  1.00 26.92           C  
-ATOM  13803  O   ASP D 329     -29.693 -10.542-119.002  1.00 31.58           O  
-ATOM  13804  CB  ASP D 329     -26.805 -11.528-118.404  1.00 36.99           C  
-ATOM  13805  CG  ASP D 329     -25.988 -12.086-117.260  1.00 40.00           C  
-ATOM  13806  OD1 ASP D 329     -26.485 -12.994-116.561  1.00 39.15           O  
-ATOM  13807  OD2 ASP D 329     -24.838 -11.629-117.077  1.00 32.18           O  
-ATOM  13808  N   LEU D 330     -29.066 -11.740-120.792  1.00 26.78           N  
-ATOM  13809  CA  LEU D 330     -30.002 -11.068-121.683  1.00 20.89           C  
-ATOM  13810  C   LEU D 330     -31.417 -11.499-121.338  1.00 23.93           C  
-ATOM  13811  O   LEU D 330     -32.318 -10.669-121.228  1.00 25.42           O  
-ATOM  13812  CB  LEU D 330     -29.691 -11.373-123.150  1.00 19.23           C  
-ATOM  13813  CG  LEU D 330     -30.709 -10.834-124.160  1.00 22.75           C  
-ATOM  13814  CD1 LEU D 330     -30.896  -9.331-123.998  1.00 20.30           C  
-ATOM  13815  CD2 LEU D 330     -30.287 -11.177-125.583  1.00 22.25           C  
-ATOM  13816  N   ILE D 331     -31.601 -12.804-121.161  1.00 26.19           N  
-ATOM  13817  CA  ILE D 331     -32.900 -13.341-120.765  1.00 26.89           C  
-ATOM  13818  C   ILE D 331     -33.360 -12.724-119.448  1.00 24.55           C  
-ATOM  13819  O   ILE D 331     -34.480 -12.208-119.342  1.00 20.68           O  
-ATOM  13820  CB  ILE D 331     -32.865 -14.877-120.617  1.00 25.46           C  
-ATOM  13821  CG1 ILE D 331     -32.552 -15.546-121.957  1.00 24.95           C  
-ATOM  13822  CG2 ILE D 331     -34.189 -15.385-120.074  1.00 25.86           C  
-ATOM  13823  CD1 ILE D 331     -32.853 -17.043-121.975  1.00 21.50           C  
-ATOM  13824  N   ALA D 332     -32.479 -12.769-118.452  1.00 30.03           N  
-ATOM  13825  CA  ALA D 332     -32.777 -12.205-117.140  1.00 27.61           C  
-ATOM  13826  C   ALA D 332     -33.128 -10.723-117.229  1.00 30.82           C  
-ATOM  13827  O   ALA D 332     -34.115 -10.280-116.645  1.00 34.05           O  
-ATOM  13828  CB  ALA D 332     -31.604 -12.412-116.196  1.00 30.98           C  
-ATOM  13829  N   ASP D 333     -32.322  -9.964-117.966  1.00 32.72           N  
-ATOM  13830  CA  ASP D 333     -32.526  -8.523-118.091  1.00 34.84           C  
-ATOM  13831  C   ASP D 333     -33.848  -8.208-118.782  1.00 37.53           C  
-ATOM  13832  O   ASP D 333     -34.512  -7.227-118.451  1.00 40.40           O  
-ATOM  13833  CB  ASP D 333     -31.366  -7.876-118.854  1.00 31.50           C  
-ATOM  13834  CG  ASP D 333     -31.516  -6.369-118.982  1.00 50.76           C  
-ATOM  13835  OD1 ASP D 333     -31.360  -5.664-117.962  1.00 52.46           O  
-ATOM  13836  OD2 ASP D 333     -31.783  -5.891-120.105  1.00 56.77           O  
-ATOM  13837  N   ILE D 334     -34.226  -9.044-119.742  1.00 31.96           N  
-ATOM  13838  CA  ILE D 334     -35.486  -8.860-120.446  1.00 24.52           C  
-ATOM  13839  C   ILE D 334     -36.663  -9.151-119.525  1.00 26.25           C  
-ATOM  13840  O   ILE D 334     -37.627  -8.388-119.484  1.00 32.82           O  
-ATOM  13841  CB  ILE D 334     -35.568  -9.754-121.692  1.00 30.98           C  
-ATOM  13842  CG1 ILE D 334     -34.642  -9.213-122.778  1.00 28.70           C  
-ATOM  13843  CG2 ILE D 334     -36.991  -9.822-122.213  1.00 22.64           C  
-ATOM  13844  CD1 ILE D 334     -34.578 -10.079-123.990  1.00 21.85           C  
-ATOM  13845  N   ILE D 335     -36.582 -10.249-118.781  1.00 31.27           N  
-ATOM  13846  CA  ILE D 335     -37.671 -10.615-117.879  1.00 32.90           C  
-ATOM  13847  C   ILE D 335     -37.840  -9.582-116.761  1.00 35.51           C  
-ATOM  13848  O   ILE D 335     -38.963  -9.201-116.423  1.00 36.79           O  
-ATOM  13849  CB  ILE D 335     -37.450 -12.018-117.271  1.00 29.16           C  
-ATOM  13850  CG1 ILE D 335     -37.661 -13.094-118.339  1.00 20.72           C  
-ATOM  13851  CG2 ILE D 335     -38.391 -12.255-116.103  1.00 27.07           C  
-ATOM  13852  CD1 ILE D 335     -37.455 -14.506-117.834  1.00 17.50           C  
-ATOM  13853  N   ASN D 336     -36.725  -9.109-116.210  1.00 34.42           N  
-ATOM  13854  CA  ASN D 336     -36.759  -8.182-115.080  1.00 30.43           C  
-ATOM  13855  C   ASN D 336     -37.063  -6.733-115.463  1.00 28.91           C  
-ATOM  13856  O   ASN D 336     -37.776  -6.037-114.742  1.00 35.26           O  
-ATOM  13857  CB  ASN D 336     -35.430  -8.223-114.322  1.00 25.54           C  
-ATOM  13858  CG  ASN D 336     -35.119  -9.598-113.759  1.00 36.42           C  
-ATOM  13859  OD1 ASN D 336     -36.017 -10.405-113.520  1.00 39.98           O  
-ATOM  13860  ND2 ASN D 336     -33.839  -9.870-113.542  1.00 32.13           N  
-ATOM  13861  N   ASN D 337     -36.525  -6.279-116.592  1.00 31.01           N  
-ATOM  13862  CA  ASN D 337     -36.600  -4.865-116.955  1.00 30.71           C  
-ATOM  13863  C   ASN D 337     -37.419  -4.562-118.211  1.00 35.06           C  
-ATOM  13864  O   ASN D 337     -37.525  -3.406-118.625  1.00 33.59           O  
-ATOM  13865  CB  ASN D 337     -35.186  -4.310-117.134  1.00 24.24           C  
-ATOM  13866  CG  ASN D 337     -34.282  -4.641-115.965  1.00 34.34           C  
-ATOM  13867  OD1 ASN D 337     -34.720  -4.673-114.815  1.00 32.53           O  
-ATOM  13868  ND2 ASN D 337     -33.013  -4.897-116.254  1.00 39.29           N  
-ATOM  13869  N   GLY D 338     -38.002  -5.592-118.813  1.00 33.22           N  
-ATOM  13870  CA  GLY D 338     -38.741  -5.412-120.050  1.00 28.00           C  
-ATOM  13871  C   GLY D 338     -40.156  -4.919-119.829  1.00 38.67           C  
-ATOM  13872  O   GLY D 338     -40.627  -4.857-118.693  1.00 52.48           O  
-ATOM  13873  N   ARG D 339     -40.831  -4.562-120.919  1.00 43.84           N  
-ATOM  13874  CA  ARG D 339     -42.228  -4.135-120.866  1.00 38.89           C  
-ATOM  13875  C   ARG D 339     -43.125  -5.207-121.476  1.00 37.59           C  
-ATOM  13876  O   ARG D 339     -42.808  -5.755-122.529  1.00 40.88           O  
-ATOM  13877  CB  ARG D 339     -42.422  -2.808-121.607  1.00 36.47           C  
-ATOM  13878  CG  ARG D 339     -41.656  -1.626-121.032  1.00 37.64           C  
-ATOM  13879  CD  ARG D 339     -42.195  -1.221-119.670  1.00 44.57           C  
-ATOM  13880  NE  ARG D 339     -41.374  -1.732-118.577  1.00 64.42           N  
-ATOM  13881  CZ  ARG D 339     -41.776  -1.809-117.312  1.00 80.92           C  
-ATOM  13882  NH1 ARG D 339     -43.000  -1.417-116.977  1.00 72.16           N  
-ATOM  13883  NH2 ARG D 339     -40.958  -2.286-116.382  1.00 77.79           N  
-ATOM  13884  N   THR D 340     -44.242  -5.504-120.822  1.00 26.10           N  
-ATOM  13885  CA  THR D 340     -45.182  -6.489-121.348  1.00 29.35           C  
-ATOM  13886  C   THR D 340     -46.036  -5.892-122.466  1.00 35.42           C  
-ATOM  13887  O   THR D 340     -46.779  -4.936-122.248  1.00 33.76           O  
-ATOM  13888  CB  THR D 340     -46.095  -7.034-120.243  1.00 31.98           C  
-ATOM  13889  OG1 THR D 340     -45.295  -7.650-119.226  1.00 30.54           O  
-ATOM  13890  CG2 THR D 340     -47.070  -8.057-120.812  1.00 27.16           C  
-ATOM  13891  N   MET D 341     -45.926  -6.463-123.663  1.00 36.26           N  
-ATOM  13892  CA  MET D 341     -46.593  -5.923-124.843  1.00 39.99           C  
-ATOM  13893  C   MET D 341     -47.411  -6.977-125.581  1.00 38.02           C  
-ATOM  13894  O   MET D 341     -47.339  -8.166-125.269  1.00 36.39           O  
-ATOM  13895  CB  MET D 341     -45.567  -5.323-125.808  1.00 33.93           C  
-ATOM  13896  CG  MET D 341     -44.598  -4.343-125.175  1.00 31.60           C  
-ATOM  13897  SD  MET D 341     -45.421  -2.853-124.592  1.00 51.16           S  
-ATOM  13898  CE  MET D 341     -46.230  -2.316-126.097  1.00 50.65           C  
-ATOM  13899  N   ASP D 342     -48.183  -6.525-126.565  1.00 45.54           N  
-ATOM  13900  CA  ASP D 342     -48.881  -7.419-127.484  1.00 51.39           C  
-ATOM  13901  C   ASP D 342     -48.056  -7.581-128.755  1.00 49.57           C  
-ATOM  13902  O   ASP D 342     -46.986  -6.985-128.881  1.00 48.06           O  
-ATOM  13903  CB  ASP D 342     -50.272  -6.882-127.823  1.00 53.98           C  
-ATOM  13904  CG  ASP D 342     -51.118  -6.634-126.593  1.00 51.88           C  
-ATOM  13905  OD1 ASP D 342     -50.981  -7.396-125.611  1.00 52.30           O  
-ATOM  13906  OD2 ASP D 342     -51.921  -5.677-126.608  1.00 46.07           O  
-ATOM  13907  N   ASP D 343     -48.555  -8.374-129.698  1.00 52.65           N  
-ATOM  13908  CA  ASP D 343     -47.858  -8.562-130.965  1.00 53.43           C  
-ATOM  13909  C   ASP D 343     -48.734  -9.195-132.041  1.00 46.85           C  
-ATOM  13910  O   ASP D 343     -49.923  -9.443-131.835  1.00 50.46           O  
-ATOM  13911  CB  ASP D 343     -46.604  -9.417-130.763  1.00 43.46           C  
-ATOM  13912  CG  ASP D 343     -46.923 -10.817-130.282  1.00 44.61           C  
-ATOM  13913  OD1 ASP D 343     -47.793 -10.962-129.397  1.00 50.76           O  
-ATOM  13914  OD2 ASP D 343     -46.305 -11.774-130.794  1.00 46.64           O  
-ATOM  13915  N   ARG D 344     -48.114  -9.442-133.190  1.00 41.55           N  
-ATOM  13916  CA  ARG D 344     -48.753 -10.067-134.342  1.00 50.09           C  
-ATOM  13917  C   ARG D 344     -49.462 -11.373-133.997  1.00 52.49           C  
-ATOM  13918  O   ARG D 344     -50.577 -11.632-134.455  1.00 53.53           O  
-ATOM  13919  CB  ARG D 344     -47.701 -10.321-135.428  1.00 55.22           C  
-ATOM  13920  CG  ARG D 344     -48.107 -11.321-136.498  1.00 48.37           C  
-ATOM  13921  CD  ARG D 344     -48.749 -10.641-137.695  1.00 57.71           C  
-ATOM  13922  NE  ARG D 344     -50.068 -10.092-137.392  1.00 84.13           N  
-ATOM  13923  CZ  ARG D 344     -50.769  -9.332-138.228  1.00 80.76           C  
-ATOM  13924  NH1 ARG D 344     -50.273  -9.025-139.420  1.00 69.39           N  
-ATOM  13925  NH2 ARG D 344     -51.961  -8.873-137.871  1.00 68.45           N  
-ATOM  13926  N   THR D 345     -48.805 -12.188-133.179  1.00 50.52           N  
-ATOM  13927  CA  THR D 345     -49.273 -13.535-132.884  1.00 47.60           C  
-ATOM  13928  C   THR D 345     -50.444 -13.556-131.904  1.00 49.58           C  
-ATOM  13929  O   THR D 345     -51.252 -14.486-131.908  1.00 48.44           O  
-ATOM  13930  CB  THR D 345     -48.132 -14.395-132.307  1.00 45.12           C  
-ATOM  13931  OG1 THR D 345     -47.792 -13.927-130.996  1.00 31.77           O  
-ATOM  13932  CG2 THR D 345     -46.900 -14.312-133.199  1.00 52.25           C  
-ATOM  13933  N   GLY D 346     -50.531 -12.529-131.065  1.00 48.77           N  
-ATOM  13934  CA  GLY D 346     -51.562 -12.465-130.043  1.00 48.71           C  
-ATOM  13935  C   GLY D 346     -51.165 -13.229-128.794  1.00 50.27           C  
-ATOM  13936  O   GLY D 346     -51.942 -13.337-127.844  1.00 45.57           O  
-ATOM  13937  N   VAL D 347     -49.947 -13.763-128.801  1.00 48.00           N  
-ATOM  13938  CA  VAL D 347     -49.429 -14.524-127.672  1.00 40.67           C  
-ATOM  13939  C   VAL D 347     -49.022 -13.585-126.539  1.00 40.63           C  
-ATOM  13940  O   VAL D 347     -49.259 -13.874-125.364  1.00 48.19           O  
-ATOM  13941  CB  VAL D 347     -48.227 -15.398-128.090  1.00 39.65           C  
-ATOM  13942  CG1 VAL D 347     -47.584 -16.048-126.878  1.00 44.55           C  
-ATOM  13943  CG2 VAL D 347     -48.664 -16.455-129.096  1.00 38.26           C  
-ATOM  13944  N   GLY D 348     -48.428 -12.451-126.901  1.00 23.93           N  
-ATOM  13945  CA  GLY D 348     -47.981 -11.479-125.920  1.00 34.63           C  
-ATOM  13946  C   GLY D 348     -46.533 -11.705-125.530  1.00 42.40           C  
-ATOM  13947  O   GLY D 348     -46.102 -12.846-125.358  1.00 45.42           O  
-ATOM  13948  N   VAL D 349     -45.775 -10.619-125.390  1.00 38.33           N  
-ATOM  13949  CA  VAL D 349     -44.345 -10.728-125.116  1.00 28.81           C  
-ATOM  13950  C   VAL D 349     -43.894  -9.839-123.963  1.00 34.79           C  
-ATOM  13951  O   VAL D 349     -44.665  -9.035-123.444  1.00 37.31           O  
-ATOM  13952  CB  VAL D 349     -43.500 -10.357-126.354  1.00 26.56           C  
-ATOM  13953  CG1 VAL D 349     -43.933 -11.159-127.566  1.00 31.32           C  
-ATOM  13954  CG2 VAL D 349     -43.605  -8.868-126.637  1.00 29.49           C  
-ATOM  13955  N   ILE D 350     -42.637 -10.007-123.567  1.00 25.29           N  
-ATOM  13956  CA  ILE D 350     -41.962  -9.078-122.668  1.00 23.98           C  
-ATOM  13957  C   ILE D 350     -40.725  -8.572-123.397  1.00 28.07           C  
-ATOM  13958  O   ILE D 350     -39.775  -9.322-123.603  1.00 35.10           O  
-ATOM  13959  CB  ILE D 350     -41.557  -9.737-121.336  1.00 24.91           C  
-ATOM  13960  CG1 ILE D 350     -42.773 -10.365-120.655  1.00 23.05           C  
-ATOM  13961  CG2 ILE D 350     -40.888  -8.722-120.423  1.00 27.09           C  
-ATOM  13962  CD1 ILE D 350     -42.441 -11.101-119.378  1.00 25.17           C  
-ATOM  13963  N   SER D 351     -40.733  -7.308-123.802  1.00 26.95           N  
-ATOM  13964  CA  SER D 351     -39.731  -6.840-124.750  1.00 26.44           C  
-ATOM  13965  C   SER D 351     -38.833  -5.727-124.233  1.00 25.35           C  
-ATOM  13966  O   SER D 351     -39.172  -5.014-123.287  1.00 32.17           O  
-ATOM  13967  CB  SER D 351     -40.416  -6.367-126.034  1.00 29.51           C  
-ATOM  13968  OG  SER D 351     -41.129  -5.165-125.812  1.00 30.66           O  
-ATOM  13969  N   LYS D 352     -37.674  -5.613-124.873  1.00 24.29           N  
-ATOM  13970  CA  LYS D 352     -36.776  -4.475-124.731  1.00 25.17           C  
-ATOM  13971  C   LYS D 352     -36.354  -4.044-126.130  1.00 32.09           C  
-ATOM  13972  O   LYS D 352     -36.646  -4.738-127.106  1.00 36.35           O  
-ATOM  13973  CB  LYS D 352     -35.553  -4.824-123.883  1.00 22.69           C  
-ATOM  13974  CG  LYS D 352     -35.857  -5.087-122.422  1.00 29.74           C  
-ATOM  13975  CD  LYS D 352     -34.579  -5.128-121.599  1.00 31.24           C  
-ATOM  13976  CE  LYS D 352     -33.822  -3.814-121.701  1.00 37.45           C  
-ATOM  13977  NZ  LYS D 352     -32.577  -3.813-120.881  1.00 40.96           N  
-ATOM  13978  N   PHE D 353     -35.666  -2.912-126.235  1.00 28.79           N  
-ATOM  13979  CA  PHE D 353     -35.248  -2.410-127.541  1.00 19.23           C  
-ATOM  13980  C   PHE D 353     -33.774  -2.010-127.547  1.00 24.25           C  
-ATOM  13981  O   PHE D 353     -33.319  -1.252-126.689  1.00 28.13           O  
-ATOM  13982  CB  PHE D 353     -36.120  -1.224-127.954  1.00 14.44           C  
-ATOM  13983  CG  PHE D 353     -36.014  -0.869-129.408  1.00 16.63           C  
-ATOM  13984  CD1 PHE D 353     -36.260  -1.819-130.384  1.00 18.77           C  
-ATOM  13985  CD2 PHE D 353     -35.684   0.417-129.801  1.00 18.30           C  
-ATOM  13986  CE1 PHE D 353     -36.168  -1.498-131.727  1.00 21.85           C  
-ATOM  13987  CE2 PHE D 353     -35.597   0.747-131.140  1.00 20.73           C  
-ATOM  13988  CZ  PHE D 353     -35.837  -0.213-132.105  1.00 19.85           C  
-ATOM  13989  N   GLY D 354     -33.032  -2.527-128.520  1.00 18.75           N  
-ATOM  13990  CA  GLY D 354     -31.613  -2.241-128.624  1.00 21.09           C  
-ATOM  13991  C   GLY D 354     -30.785  -3.079-127.671  1.00 28.24           C  
-ATOM  13992  O   GLY D 354     -30.533  -2.679-126.534  1.00 30.70           O  
-ATOM  13993  N   CYS D 355     -30.362  -4.249-128.137  1.00 19.67           N  
-ATOM  13994  CA  CYS D 355     -29.575  -5.156-127.314  1.00 16.10           C  
-ATOM  13995  C   CYS D 355     -28.375  -5.676-128.089  1.00 20.17           C  
-ATOM  13996  O   CYS D 355     -28.424  -5.809-129.309  1.00 21.61           O  
-ATOM  13997  CB  CYS D 355     -30.440  -6.312-126.815  1.00 16.67           C  
-ATOM  13998  SG  CYS D 355     -31.727  -5.797-125.650  1.00 27.01           S  
-ATOM  13999  N   THR D 356     -27.299  -5.970-127.369  1.00 25.32           N  
-ATOM  14000  CA  THR D 356     -26.026  -6.301-127.995  1.00 17.16           C  
-ATOM  14001  C   THR D 356     -25.388  -7.550-127.403  1.00 21.63           C  
-ATOM  14002  O   THR D 356     -25.325  -7.712-126.182  1.00 18.35           O  
-ATOM  14003  CB  THR D 356     -25.034  -5.120-127.872  1.00 19.99           C  
-ATOM  14004  OG1 THR D 356     -25.345  -4.139-128.866  1.00 36.93           O  
-ATOM  14005  CG2 THR D 356     -23.589  -5.578-128.058  1.00 20.89           C  
-ATOM  14006  N   MET D 357     -24.926  -8.438-128.278  1.00 23.40           N  
-ATOM  14007  CA  MET D 357     -24.067  -9.539-127.854  1.00 18.15           C  
-ATOM  14008  C   MET D 357     -22.884  -9.659-128.800  1.00 18.78           C  
-ATOM  14009  O   MET D 357     -22.917  -9.121-129.897  1.00 16.65           O  
-ATOM  14010  CB  MET D 357     -24.837 -10.855-127.812  1.00 15.42           C  
-ATOM  14011  CG  MET D 357     -25.850 -10.953-126.695  1.00 17.93           C  
-ATOM  14012  SD  MET D 357     -26.633 -12.575-126.663  1.00 22.72           S  
-ATOM  14013  CE  MET D 357     -27.270 -12.681-128.334  1.00 18.17           C  
-ATOM  14014  N   ARG D 358     -21.833 -10.348-128.374  1.00 17.00           N  
-ATOM  14015  CA  ARG D 358     -20.747 -10.680-129.288  1.00 16.34           C  
-ATOM  14016  C   ARG D 358     -20.002 -11.928-128.824  1.00 16.76           C  
-ATOM  14017  O   ARG D 358     -19.682 -12.079-127.645  1.00 14.09           O  
-ATOM  14018  CB  ARG D 358     -19.781  -9.500-129.460  1.00 16.25           C  
-ATOM  14019  CG  ARG D 358     -19.212  -8.916-128.185  1.00 18.98           C  
-ATOM  14020  CD  ARG D 358     -18.075  -7.955-128.511  1.00 22.79           C  
-ATOM  14021  NE  ARG D 358     -18.522  -6.808-129.299  1.00 34.74           N  
-ATOM  14022  CZ  ARG D 358     -17.754  -6.144-130.160  1.00 33.68           C  
-ATOM  14023  NH1 ARG D 358     -16.497  -6.518-130.358  1.00 30.98           N  
-ATOM  14024  NH2 ARG D 358     -18.244  -5.109-130.830  1.00 25.11           N  
-ATOM  14025  N   TYR D 359     -19.741 -12.823-129.771  1.00 17.50           N  
-ATOM  14026  CA  TYR D 359     -19.144 -14.115-129.465  1.00 16.83           C  
-ATOM  14027  C   TYR D 359     -17.851 -14.335-130.241  1.00 18.49           C  
-ATOM  14028  O   TYR D 359     -17.812 -14.198-131.462  1.00 17.00           O  
-ATOM  14029  CB  TYR D 359     -20.140 -15.242-129.757  1.00 21.39           C  
-ATOM  14030  CG  TYR D 359     -21.378 -15.189-128.888  1.00 17.58           C  
-ATOM  14031  CD1 TYR D 359     -22.445 -14.361-129.212  1.00 17.41           C  
-ATOM  14032  CD2 TYR D 359     -21.476 -15.960-127.740  1.00 17.77           C  
-ATOM  14033  CE1 TYR D 359     -23.576 -14.304-128.418  1.00 15.69           C  
-ATOM  14034  CE2 TYR D 359     -22.604 -15.911-126.940  1.00 20.59           C  
-ATOM  14035  CZ  TYR D 359     -23.649 -15.082-127.284  1.00 16.66           C  
-ATOM  14036  OH  TYR D 359     -24.769 -15.031-126.489  1.00 19.82           O  
-ATOM  14037  N   SER D 360     -16.793 -14.678-129.515  1.00 20.94           N  
-ATOM  14038  CA  SER D 360     -15.489 -14.928-130.116  1.00 20.81           C  
-ATOM  14039  C   SER D 360     -15.478 -16.224-130.928  1.00 24.73           C  
-ATOM  14040  O   SER D 360     -16.112 -17.206-130.544  1.00 24.75           O  
-ATOM  14041  CB  SER D 360     -14.415 -14.976-129.030  1.00 20.54           C  
-ATOM  14042  OG  SER D 360     -13.399 -15.901-129.369  1.00 54.73           O  
-ATOM  14043  N   LEU D 361     -14.743 -16.225-132.039  1.00 24.23           N  
-ATOM  14044  CA  LEU D 361     -14.742 -17.363-132.956  1.00 21.00           C  
-ATOM  14045  C   LEU D 361     -13.369 -17.999-133.181  1.00 27.98           C  
-ATOM  14046  O   LEU D 361     -13.236 -18.892-134.018  1.00 27.23           O  
-ATOM  14047  CB  LEU D 361     -15.310 -16.940-134.312  1.00 15.35           C  
-ATOM  14048  CG  LEU D 361     -16.738 -16.404-134.344  1.00 19.73           C  
-ATOM  14049  CD1 LEU D 361     -17.131 -16.041-135.763  1.00 19.46           C  
-ATOM  14050  CD2 LEU D 361     -17.694 -17.425-133.771  1.00 19.59           C  
-ATOM  14051  N   ASP D 362     -12.352 -17.549-132.451  1.00 28.48           N  
-ATOM  14052  CA  ASP D 362     -10.990 -18.013-132.708  1.00 19.58           C  
-ATOM  14053  C   ASP D 362     -10.645 -19.280-131.935  1.00 18.67           C  
-ATOM  14054  O   ASP D 362      -9.807 -20.069-132.367  1.00 22.02           O  
-ATOM  14055  CB  ASP D 362      -9.979 -16.918-132.371  1.00 18.18           C  
-ATOM  14056  CG  ASP D 362      -9.995 -16.545-130.907  1.00 24.90           C  
-ATOM  14057  OD1 ASP D 362     -11.100 -16.347-130.361  1.00 26.26           O  
-ATOM  14058  OD2 ASP D 362      -8.906 -16.459-130.299  1.00 27.88           O  
-ATOM  14059  N   GLN D 363     -11.283 -19.471-130.787  1.00 19.29           N  
-ATOM  14060  CA  GLN D 363     -11.002 -20.635-129.959  1.00 18.19           C  
-ATOM  14061  C   GLN D 363     -12.065 -21.710-130.152  1.00 16.38           C  
-ATOM  14062  O   GLN D 363     -11.747 -22.878-130.350  1.00 12.48           O  
-ATOM  14063  CB  GLN D 363     -10.916 -20.239-128.485  1.00 28.98           C  
-ATOM  14064  CG  GLN D 363      -9.795 -19.258-128.161  1.00 35.35           C  
-ATOM  14065  CD  GLN D 363      -8.427 -19.912-128.140  1.00 41.14           C  
-ATOM  14066  OE1 GLN D 363      -8.089 -20.645-127.207  1.00 31.43           O  
-ATOM  14067  NE2 GLN D 363      -7.630 -19.649-129.171  1.00 44.52           N  
-ATOM  14068  N   ALA D 364     -13.332 -21.312-130.104  1.00 20.69           N  
-ATOM  14069  CA  ALA D 364     -14.423 -22.274-130.204  1.00 16.89           C  
-ATOM  14070  C   ALA D 364     -15.610 -21.708-130.972  1.00 17.53           C  
-ATOM  14071  O   ALA D 364     -15.544 -20.604-131.514  1.00 18.38           O  
-ATOM  14072  CB  ALA D 364     -14.857 -22.718-128.818  1.00 15.04           C  
-ATOM  14073  N   PHE D 365     -16.692 -22.481-131.014  1.00 18.58           N  
-ATOM  14074  CA  PHE D 365     -17.908 -22.076-131.710  1.00 18.81           C  
-ATOM  14075  C   PHE D 365     -19.049 -21.894-130.714  1.00 17.91           C  
-ATOM  14076  O   PHE D 365     -19.292 -22.762-129.876  1.00 18.50           O  
-ATOM  14077  CB  PHE D 365     -18.290 -23.105-132.781  1.00 14.62           C  
-ATOM  14078  CG  PHE D 365     -19.414 -22.664-133.676  1.00 13.47           C  
-ATOM  14079  CD1 PHE D 365     -20.731 -22.943-133.347  1.00 16.57           C  
-ATOM  14080  CD2 PHE D 365     -19.153 -21.972-134.847  1.00 13.15           C  
-ATOM  14081  CE1 PHE D 365     -21.768 -22.537-134.167  1.00 14.97           C  
-ATOM  14082  CE2 PHE D 365     -20.185 -21.563-135.672  1.00 15.78           C  
-ATOM  14083  CZ  PHE D 365     -21.494 -21.846-135.331  1.00 15.72           C  
-ATOM  14084  N   PRO D 366     -19.756 -20.759-130.807  1.00 14.92           N  
-ATOM  14085  CA  PRO D 366     -20.827 -20.436-129.864  1.00 14.59           C  
-ATOM  14086  C   PRO D 366     -22.098 -21.238-130.113  1.00 20.43           C  
-ATOM  14087  O   PRO D 366     -23.141 -20.656-130.415  1.00 31.58           O  
-ATOM  14088  CB  PRO D 366     -21.066 -18.946-130.113  1.00 17.42           C  
-ATOM  14089  CG  PRO D 366     -20.708 -18.754-131.540  1.00 17.53           C  
-ATOM  14090  CD  PRO D 366     -19.564 -19.696-131.808  1.00 14.52           C  
-ATOM  14091  N   LEU D 367     -22.009 -22.558-129.993  1.00 18.68           N  
-ATOM  14092  CA  LEU D 367     -23.202 -23.395-130.004  1.00 22.10           C  
-ATOM  14093  C   LEU D 367     -23.703 -23.538-128.571  1.00 19.30           C  
-ATOM  14094  O   LEU D 367     -23.084 -24.221-127.757  1.00 23.26           O  
-ATOM  14095  CB  LEU D 367     -22.911 -24.762-130.626  1.00 16.15           C  
-ATOM  14096  CG  LEU D 367     -24.128 -25.564-131.093  1.00 15.73           C  
-ATOM  14097  CD1 LEU D 367     -24.965 -24.763-132.083  1.00 15.19           C  
-ATOM  14098  CD2 LEU D 367     -23.690 -26.881-131.712  1.00 16.75           C  
-ATOM  14099  N   LEU D 368     -24.822 -22.880-128.277  1.00 13.87           N  
-ATOM  14100  CA  LEU D 368     -25.348 -22.758-126.914  1.00 26.17           C  
-ATOM  14101  C   LEU D 368     -25.460 -24.099-126.185  1.00 26.76           C  
-ATOM  14102  O   LEU D 368     -25.852 -25.106-126.774  1.00 23.87           O  
-ATOM  14103  CB  LEU D 368     -26.715 -22.065-126.944  1.00 34.87           C  
-ATOM  14104  CG  LEU D 368     -26.752 -20.546-127.171  1.00 37.91           C  
-ATOM  14105  CD1 LEU D 368     -25.951 -19.816-126.107  1.00 24.25           C  
-ATOM  14106  CD2 LEU D 368     -26.270 -20.146-128.567  1.00 48.93           C  
-ATOM  14107  N   THR D 369     -25.115 -24.105-124.899  1.00 23.86           N  
-ATOM  14108  CA  THR D 369     -24.999 -25.354-124.151  1.00 25.02           C  
-ATOM  14109  C   THR D 369     -26.058 -25.543-123.063  1.00 24.83           C  
-ATOM  14110  O   THR D 369     -26.263 -26.661-122.593  1.00 28.17           O  
-ATOM  14111  CB  THR D 369     -23.611 -25.477-123.490  1.00 20.67           C  
-ATOM  14112  OG1 THR D 369     -23.409 -24.387-122.583  1.00 25.33           O  
-ATOM  14113  CG2 THR D 369     -22.519 -25.462-124.541  1.00 19.96           C  
-ATOM  14114  N   THR D 370     -26.726 -24.466-122.660  1.00 21.08           N  
-ATOM  14115  CA  THR D 370     -27.770 -24.569-121.640  1.00 24.89           C  
-ATOM  14116  C   THR D 370     -29.007 -25.280-122.191  1.00 25.44           C  
-ATOM  14117  O   THR D 370     -29.891 -25.686-121.438  1.00 23.92           O  
-ATOM  14118  CB  THR D 370     -28.181 -23.189-121.094  1.00 25.93           C  
-ATOM  14119  OG1 THR D 370     -28.609 -22.348-122.174  1.00 32.22           O  
-ATOM  14120  CG2 THR D 370     -27.014 -22.533-120.371  1.00 21.42           C  
-ATOM  14121  N   LYS D 371     -29.061 -25.414-123.511  1.00 24.89           N  
-ATOM  14122  CA  LYS D 371     -30.071 -26.229-124.173  1.00 22.12           C  
-ATOM  14123  C   LYS D 371     -29.497 -26.711-125.496  1.00 25.30           C  
-ATOM  14124  O   LYS D 371     -28.650 -26.044-126.092  1.00 30.48           O  
-ATOM  14125  CB  LYS D 371     -31.368 -25.444-124.395  1.00 25.29           C  
-ATOM  14126  CG  LYS D 371     -31.356 -24.542-125.621  1.00 29.23           C  
-ATOM  14127  CD  LYS D 371     -32.538 -23.583-125.633  1.00 34.82           C  
-ATOM  14128  CE  LYS D 371     -33.546 -23.941-126.714  1.00 43.64           C  
-ATOM  14129  NZ  LYS D 371     -34.522 -22.836-126.936  1.00 52.05           N  
-ATOM  14130  N   ARG D 372     -29.941 -27.875-125.951  1.00 29.25           N  
-ATOM  14131  CA  ARG D 372     -29.447 -28.411-127.211  1.00 26.87           C  
-ATOM  14132  C   ARG D 372     -29.976 -27.586-128.384  1.00 29.22           C  
-ATOM  14133  O   ARG D 372     -31.184 -27.390-128.526  1.00 31.44           O  
-ATOM  14134  CB  ARG D 372     -29.838 -29.881-127.366  1.00 26.85           C  
-ATOM  14135  CG  ARG D 372     -29.422 -30.481-128.696  1.00 26.51           C  
-ATOM  14136  CD  ARG D 372     -29.530 -31.996-128.697  1.00 34.42           C  
-ATOM  14137  NE  ARG D 372     -28.537 -32.621-127.829  1.00 32.30           N  
-ATOM  14138  CZ  ARG D 372     -27.275 -32.849-128.182  1.00 33.94           C  
-ATOM  14139  NH1 ARG D 372     -26.844 -32.493-129.386  1.00 25.01           N  
-ATOM  14140  NH2 ARG D 372     -26.440 -33.426-127.329  1.00 31.82           N  
-ATOM  14141  N   VAL D 373     -29.061 -27.094-129.212  1.00 20.67           N  
-ATOM  14142  CA  VAL D 373     -29.421 -26.287-130.371  1.00 20.03           C  
-ATOM  14143  C   VAL D 373     -29.494 -27.145-131.633  1.00 21.97           C  
-ATOM  14144  O   VAL D 373     -28.634 -27.994-131.865  1.00 21.13           O  
-ATOM  14145  CB  VAL D 373     -28.417 -25.129-130.571  1.00 19.95           C  
-ATOM  14146  CG1 VAL D 373     -28.607 -24.463-131.930  1.00 21.05           C  
-ATOM  14147  CG2 VAL D 373     -28.563 -24.113-129.450  1.00 24.80           C  
-ATOM  14148  N   PHE D 374     -30.533 -26.927-132.435  1.00 23.07           N  
-ATOM  14149  CA  PHE D 374     -30.737 -27.696-133.660  1.00 24.91           C  
-ATOM  14150  C   PHE D 374     -29.675 -27.388-134.718  1.00 20.31           C  
-ATOM  14151  O   PHE D 374     -29.898 -26.605-135.646  1.00 27.21           O  
-ATOM  14152  CB  PHE D 374     -32.133 -27.439-134.229  1.00 34.37           C  
-ATOM  14153  CG  PHE D 374     -32.582 -28.480-135.211  1.00 28.79           C  
-ATOM  14154  CD1 PHE D 374     -32.023 -29.747-135.201  1.00 22.69           C  
-ATOM  14155  CD2 PHE D 374     -33.553 -28.188-136.151  1.00 28.88           C  
-ATOM  14156  CE1 PHE D 374     -32.431 -30.705-136.106  1.00 26.42           C  
-ATOM  14157  CE2 PHE D 374     -33.964 -29.140-137.060  1.00 34.28           C  
-ATOM  14158  CZ  PHE D 374     -33.402 -30.403-137.037  1.00 30.11           C  
-ATOM  14159  N   TRP D 375     -28.523 -28.032-134.575  1.00 16.99           N  
-ATOM  14160  CA  TRP D 375     -27.386 -27.782-135.449  1.00 16.29           C  
-ATOM  14161  C   TRP D 375     -27.660 -28.107-136.913  1.00 20.21           C  
-ATOM  14162  O   TRP D 375     -27.325 -27.321-137.799  1.00 26.07           O  
-ATOM  14163  CB  TRP D 375     -26.174 -28.581-134.978  1.00 15.43           C  
-ATOM  14164  CG  TRP D 375     -25.084 -28.605-135.994  1.00 13.16           C  
-ATOM  14165  CD1 TRP D 375     -24.690 -29.668-136.749  1.00 12.52           C  
-ATOM  14166  CD2 TRP D 375     -24.265 -27.504-136.392  1.00 15.96           C  
-ATOM  14167  NE1 TRP D 375     -23.665 -29.301-137.585  1.00 12.24           N  
-ATOM  14168  CE2 TRP D 375     -23.386 -27.975-137.387  1.00 14.30           C  
-ATOM  14169  CE3 TRP D 375     -24.185 -26.164-136.000  1.00 16.98           C  
-ATOM  14170  CZ2 TRP D 375     -22.436 -27.156-137.993  1.00 16.86           C  
-ATOM  14171  CZ3 TRP D 375     -23.242 -25.350-136.604  1.00 20.09           C  
-ATOM  14172  CH2 TRP D 375     -22.379 -25.849-137.589  1.00 19.53           C  
-ATOM  14173  N   LYS D 376     -28.249 -29.272-137.163  1.00 17.84           N  
-ATOM  14174  CA  LYS D 376     -28.568 -29.681-138.525  1.00 19.61           C  
-ATOM  14175  C   LYS D 376     -29.508 -28.668-139.162  1.00 19.20           C  
-ATOM  14176  O   LYS D 376     -29.360 -28.320-140.329  1.00 16.38           O  
-ATOM  14177  CB  LYS D 376     -29.197 -31.075-138.546  1.00 24.51           C  
-ATOM  14178  CG  LYS D 376     -29.227 -31.712-139.927  1.00 36.22           C  
-ATOM  14179  CD  LYS D 376     -30.604 -32.260-140.266  1.00 33.71           C  
-ATOM  14180  CE  LYS D 376     -31.017 -33.373-139.314  1.00 46.51           C  
-ATOM  14181  NZ  LYS D 376     -32.366 -33.913-139.650  1.00 38.16           N  
-ATOM  14182  N   GLY D 377     -30.467 -28.190-138.379  1.00 19.29           N  
-ATOM  14183  CA  GLY D 377     -31.372 -27.150-138.825  1.00 18.46           C  
-ATOM  14184  C   GLY D 377     -30.625 -25.886-139.199  1.00 16.53           C  
-ATOM  14185  O   GLY D 377     -30.874 -25.303-140.253  1.00 19.33           O  
-ATOM  14186  N   VAL D 378     -29.705 -25.466-138.334  1.00 16.27           N  
-ATOM  14187  CA  VAL D 378     -28.868 -24.296-138.606  1.00 20.26           C  
-ATOM  14188  C   VAL D 378     -28.134 -24.426-139.940  1.00 24.38           C  
-ATOM  14189  O   VAL D 378     -28.290 -23.592-140.842  1.00 27.11           O  
-ATOM  14190  CB  VAL D 378     -27.828 -24.073-137.481  1.00 16.51           C  
-ATOM  14191  CG1 VAL D 378     -26.795 -23.042-137.899  1.00 18.96           C  
-ATOM  14192  CG2 VAL D 378     -28.513 -23.658-136.193  1.00 19.46           C  
-ATOM  14193  N   LEU D 379     -27.342 -25.487-140.048  1.00 19.71           N  
-ATOM  14194  CA  LEU D 379     -26.534 -25.768-141.225  1.00 17.56           C  
-ATOM  14195  C   LEU D 379     -27.353 -25.833-142.512  1.00 19.07           C  
-ATOM  14196  O   LEU D 379     -27.061 -25.132-143.481  1.00 21.61           O  
-ATOM  14197  CB  LEU D 379     -25.770 -27.082-141.011  1.00 17.58           C  
-ATOM  14198  CG  LEU D 379     -24.887 -27.575-142.157  1.00 20.92           C  
-ATOM  14199  CD1 LEU D 379     -23.948 -26.480-142.637  1.00 22.77           C  
-ATOM  14200  CD2 LEU D 379     -24.103 -28.801-141.717  1.00 15.68           C  
-ATOM  14201  N   GLU D 380     -28.374 -26.681-142.512  1.00 20.49           N  
-ATOM  14202  CA  GLU D 380     -29.223 -26.858-143.683  1.00 21.59           C  
-ATOM  14203  C   GLU D 380     -29.927 -25.569-144.079  1.00 24.29           C  
-ATOM  14204  O   GLU D 380     -30.034 -25.265-145.266  1.00 31.56           O  
-ATOM  14205  CB  GLU D 380     -30.263 -27.959-143.442  1.00 21.68           C  
-ATOM  14206  CG  GLU D 380     -29.684 -29.359-143.322  1.00 31.29           C  
-ATOM  14207  CD  GLU D 380     -29.196 -29.929-144.647  1.00 39.63           C  
-ATOM  14208  OE1 GLU D 380     -29.292 -29.235-145.686  1.00 34.56           O  
-ATOM  14209  OE2 GLU D 380     -28.719 -31.085-144.643  1.00 32.77           O  
-ATOM  14210  N   GLU D 381     -30.409 -24.815-143.093  1.00 18.50           N  
-ATOM  14211  CA  GLU D 381     -31.070 -23.552-143.397  1.00 17.85           C  
-ATOM  14212  C   GLU D 381     -30.084 -22.559-144.002  1.00 23.90           C  
-ATOM  14213  O   GLU D 381     -30.447 -21.783-144.886  1.00 21.59           O  
-ATOM  14214  CB  GLU D 381     -31.718 -22.946-142.152  1.00 18.18           C  
-ATOM  14215  CG  GLU D 381     -32.667 -21.797-142.468  1.00 23.46           C  
-ATOM  14216  CD  GLU D 381     -32.741 -20.770-141.356  1.00 31.80           C  
-ATOM  14217  OE1 GLU D 381     -31.729 -20.590-140.645  1.00 33.96           O  
-ATOM  14218  OE2 GLU D 381     -33.807 -20.137-141.200  1.00 26.44           O  
-ATOM  14219  N   LEU D 382     -28.838 -22.582-143.530  1.00 28.93           N  
-ATOM  14220  CA  LEU D 382     -27.823 -21.671-144.059  1.00 20.28           C  
-ATOM  14221  C   LEU D 382     -27.441 -22.019-145.496  1.00 19.29           C  
-ATOM  14222  O   LEU D 382     -27.350 -21.137-146.352  1.00 22.27           O  
-ATOM  14223  CB  LEU D 382     -26.574 -21.666-143.168  1.00 16.90           C  
-ATOM  14224  CG  LEU D 382     -25.427 -20.753-143.623  1.00 22.38           C  
-ATOM  14225  CD1 LEU D 382     -25.930 -19.358-143.978  1.00 21.26           C  
-ATOM  14226  CD2 LEU D 382     -24.341 -20.674-142.552  1.00 22.76           C  
-ATOM  14227  N   LEU D 383     -27.212 -23.301-145.759  1.00 19.43           N  
-ATOM  14228  CA  LEU D 383     -26.909 -23.746-147.116  1.00 19.27           C  
-ATOM  14229  C   LEU D 383     -28.068 -23.388-148.043  1.00 26.55           C  
-ATOM  14230  O   LEU D 383     -27.873 -22.894-149.158  1.00 31.98           O  
-ATOM  14231  CB  LEU D 383     -26.635 -25.252-147.135  1.00 19.92           C  
-ATOM  14232  CG  LEU D 383     -25.365 -25.679-146.388  1.00 15.29           C  
-ATOM  14233  CD1 LEU D 383     -25.367 -27.172-146.110  1.00 21.28           C  
-ATOM  14234  CD2 LEU D 383     -24.123 -25.284-147.172  1.00 19.78           C  
-ATOM  14235  N   TRP D 384     -29.274 -23.630-147.541  1.00 27.22           N  
-ATOM  14236  CA  TRP D 384     -30.518 -23.228-148.187  1.00 27.28           C  
-ATOM  14237  C   TRP D 384     -30.493 -21.752-148.578  1.00 27.09           C  
-ATOM  14238  O   TRP D 384     -30.813 -21.401-149.715  1.00 29.52           O  
-ATOM  14239  CB  TRP D 384     -31.695 -23.516-147.250  1.00 24.04           C  
-ATOM  14240  CG  TRP D 384     -33.050 -23.384-147.860  1.00 19.61           C  
-ATOM  14241  CD1 TRP D 384     -33.564 -24.125-148.882  1.00 21.73           C  
-ATOM  14242  CD2 TRP D 384     -34.085 -22.483-147.456  1.00 20.24           C  
-ATOM  14243  NE1 TRP D 384     -34.849 -23.725-149.154  1.00 22.02           N  
-ATOM  14244  CE2 TRP D 384     -35.193 -22.719-148.291  1.00 23.25           C  
-ATOM  14245  CE3 TRP D 384     -34.179 -21.491-146.475  1.00 21.63           C  
-ATOM  14246  CZ2 TRP D 384     -36.381 -22.001-148.175  1.00 25.86           C  
-ATOM  14247  CZ3 TRP D 384     -35.358 -20.780-146.361  1.00 25.35           C  
-ATOM  14248  CH2 TRP D 384     -36.444 -21.039-147.206  1.00 24.32           C  
-ATOM  14249  N   PHE D 385     -30.112 -20.899-147.630  1.00 25.08           N  
-ATOM  14250  CA  PHE D 385     -29.966 -19.470-147.888  1.00 21.43           C  
-ATOM  14251  C   PHE D 385     -29.000 -19.216-149.029  1.00 23.44           C  
-ATOM  14252  O   PHE D 385     -29.323 -18.510-149.985  1.00 27.01           O  
-ATOM  14253  CB  PHE D 385     -29.466 -18.735-146.646  1.00 22.09           C  
-ATOM  14254  CG  PHE D 385     -30.493 -18.590-145.569  1.00 32.54           C  
-ATOM  14255  CD1 PHE D 385     -31.844 -18.687-145.859  1.00 33.67           C  
-ATOM  14256  CD2 PHE D 385     -30.105 -18.348-144.261  1.00 28.03           C  
-ATOM  14257  CE1 PHE D 385     -32.791 -18.549-144.862  1.00 34.99           C  
-ATOM  14258  CE2 PHE D 385     -31.045 -18.210-143.260  1.00 31.00           C  
-ATOM  14259  CZ  PHE D 385     -32.391 -18.309-143.561  1.00 42.08           C  
-ATOM  14260  N   ILE D 386     -27.813 -19.802-148.914  1.00 23.17           N  
-ATOM  14261  CA  ILE D 386     -26.729 -19.539-149.853  1.00 23.93           C  
-ATOM  14262  C   ILE D 386     -27.071 -19.965-151.282  1.00 25.16           C  
-ATOM  14263  O   ILE D 386     -26.670 -19.305-152.239  1.00 27.22           O  
-ATOM  14264  CB  ILE D 386     -25.432 -20.233-149.387  1.00 24.51           C  
-ATOM  14265  CG1 ILE D 386     -25.014 -19.672-148.024  1.00 20.81           C  
-ATOM  14266  CG2 ILE D 386     -24.314 -20.040-150.401  1.00 17.43           C  
-ATOM  14267  CD1 ILE D 386     -23.767 -20.290-147.471  1.00 20.55           C  
-ATOM  14268  N   ARG D 387     -27.827 -21.047-151.432  1.00 34.26           N  
-ATOM  14269  CA  ARG D 387     -28.229 -21.481-152.770  1.00 25.85           C  
-ATOM  14270  C   ARG D 387     -29.199 -20.487-153.413  1.00 27.96           C  
-ATOM  14271  O   ARG D 387     -29.362 -20.469-154.635  1.00 33.78           O  
-ATOM  14272  CB  ARG D 387     -28.873 -22.865-152.726  1.00 31.12           C  
-ATOM  14273  CG  ARG D 387     -27.968 -23.958-152.186  1.00 34.21           C  
-ATOM  14274  CD  ARG D 387     -28.591 -25.327-152.389  1.00 28.85           C  
-ATOM  14275  NE  ARG D 387     -28.005 -26.317-151.494  1.00 34.58           N  
-ATOM  14276  CZ  ARG D 387     -28.624 -26.818-150.430  1.00 35.07           C  
-ATOM  14277  NH1 ARG D 387     -29.856 -26.428-150.133  1.00 35.31           N  
-ATOM  14278  NH2 ARG D 387     -28.015 -27.715-149.668  1.00 39.73           N  
-ATOM  14279  N   GLY D 388     -29.832 -19.658-152.587  1.00 26.22           N  
-ATOM  14280  CA  GLY D 388     -30.840 -18.728-153.066  1.00 25.08           C  
-ATOM  14281  C   GLY D 388     -32.166 -19.443-153.215  1.00 27.08           C  
-ATOM  14282  O   GLY D 388     -33.008 -19.067-154.029  1.00 22.63           O  
-ATOM  14283  N   ASP D 389     -32.342 -20.490-152.418  1.00 22.81           N  
-ATOM  14284  CA  ASP D 389     -33.542 -21.309-152.472  1.00 16.39           C  
-ATOM  14285  C   ASP D 389     -34.673 -20.667-151.674  1.00 25.29           C  
-ATOM  14286  O   ASP D 389     -34.454 -20.149-150.577  1.00 22.39           O  
-ATOM  14287  CB  ASP D 389     -33.239 -22.707-151.937  1.00 21.27           C  
-ATOM  14288  CG  ASP D 389     -34.285 -23.727-152.331  1.00 27.60           C  
-ATOM  14289  OD1 ASP D 389     -35.344 -23.334-152.865  1.00 29.77           O  
-ATOM  14290  OD2 ASP D 389     -34.044 -24.931-152.097  1.00 25.07           O  
-ATOM  14291  N   THR D 390     -35.881 -20.700-152.232  1.00 36.26           N  
-ATOM  14292  CA  THR D 390     -37.058 -20.164-151.553  1.00 22.66           C  
-ATOM  14293  C   THR D 390     -38.113 -21.246-151.340  1.00 22.34           C  
-ATOM  14294  O   THR D 390     -39.270 -20.951-151.044  1.00 28.37           O  
-ATOM  14295  CB  THR D 390     -37.684 -18.999-152.341  1.00 20.73           C  
-ATOM  14296  OG1 THR D 390     -38.011 -19.433-153.667  1.00 23.23           O  
-ATOM  14297  CG2 THR D 390     -36.714 -17.835-152.421  1.00 20.74           C  
-ATOM  14298  N   ASN D 391     -37.701 -22.500-151.491  1.00 21.61           N  
-ATOM  14299  CA  ASN D 391     -38.588 -23.641-151.302  1.00 20.30           C  
-ATOM  14300  C   ASN D 391     -38.379 -24.260-149.922  1.00 23.06           C  
-ATOM  14301  O   ASN D 391     -37.342 -24.865-149.663  1.00 28.29           O  
-ATOM  14302  CB  ASN D 391     -38.343 -24.680-152.401  1.00 22.87           C  
-ATOM  14303  CG  ASN D 391     -39.452 -25.710-152.497  1.00 23.84           C  
-ATOM  14304  OD1 ASN D 391     -40.167 -25.966-151.532  1.00 27.34           O  
-ATOM  14305  ND2 ASN D 391     -39.600 -26.307-153.673  1.00 25.82           N  
-ATOM  14306  N   ALA D 392     -39.363 -24.110-149.040  1.00 22.94           N  
-ATOM  14307  CA  ALA D 392     -39.241 -24.606-147.669  1.00 26.02           C  
-ATOM  14308  C   ALA D 392     -39.432 -26.119-147.588  1.00 29.62           C  
-ATOM  14309  O   ALA D 392     -39.098 -26.746-146.579  1.00 33.44           O  
-ATOM  14310  CB  ALA D 392     -40.238 -23.904-146.764  1.00 24.67           C  
-ATOM  14311  N   ASN D 393     -39.972 -26.700-148.653  1.00 24.11           N  
-ATOM  14312  CA  ASN D 393     -40.174 -28.140-148.708  1.00 24.65           C  
-ATOM  14313  C   ASN D 393     -38.842 -28.868-148.814  1.00 27.98           C  
-ATOM  14314  O   ASN D 393     -38.707 -30.008-148.369  1.00 29.40           O  
-ATOM  14315  CB  ASN D 393     -41.082 -28.506-149.880  1.00 32.71           C  
-ATOM  14316  CG  ASN D 393     -42.453 -27.868-149.773  1.00 31.42           C  
-ATOM  14317  OD1 ASN D 393     -43.141 -28.009-148.761  1.00 27.78           O  
-ATOM  14318  ND2 ASN D 393     -42.853 -27.149-150.814  1.00 38.64           N  
-ATOM  14319  N   HIS D 394     -37.856 -28.197-149.403  1.00 25.49           N  
-ATOM  14320  CA  HIS D 394     -36.503 -28.735-149.475  1.00 25.46           C  
-ATOM  14321  C   HIS D 394     -35.899 -28.841-148.079  1.00 23.05           C  
-ATOM  14322  O   HIS D 394     -35.080 -29.717-147.804  1.00 20.69           O  
-ATOM  14323  CB  HIS D 394     -35.626 -27.863-150.372  1.00 24.76           C  
-ATOM  14324  CG  HIS D 394     -36.038 -27.873-151.811  1.00 21.16           C  
-ATOM  14325  ND1 HIS D 394     -35.516 -27.001-152.741  1.00 21.35           N  
-ATOM  14326  CD2 HIS D 394     -36.919 -28.653-152.481  1.00 25.56           C  
-ATOM  14327  CE1 HIS D 394     -36.059 -27.241-153.921  1.00 24.75           C  
-ATOM  14328  NE2 HIS D 394     -36.914 -28.240-153.791  1.00 26.54           N  
-ATOM  14329  N   LEU D 395     -36.316 -27.934-147.202  1.00 27.03           N  
-ATOM  14330  CA  LEU D 395     -35.904 -27.959-145.806  1.00 25.92           C  
-ATOM  14331  C   LEU D 395     -36.680 -29.020-145.034  1.00 26.27           C  
-ATOM  14332  O   LEU D 395     -36.122 -29.736-144.203  1.00 23.69           O  
-ATOM  14333  CB  LEU D 395     -36.108 -26.583-145.170  1.00 18.40           C  
-ATOM  14334  CG  LEU D 395     -34.854 -25.871-144.667  1.00 19.91           C  
-ATOM  14335  CD1 LEU D 395     -33.706 -26.043-145.648  1.00 20.50           C  
-ATOM  14336  CD2 LEU D 395     -35.147 -24.397-144.432  1.00 21.95           C  
-ATOM  14337  N   SER D 396     -37.974 -29.113-145.319  1.00 27.22           N  
-ATOM  14338  CA  SER D 396     -38.857 -30.036-144.621  1.00 25.86           C  
-ATOM  14339  C   SER D 396     -38.504 -31.496-144.913  1.00 27.06           C  
-ATOM  14340  O   SER D 396     -38.603 -32.352-144.035  1.00 25.34           O  
-ATOM  14341  CB  SER D 396     -40.313 -29.755-145.003  1.00 27.95           C  
-ATOM  14342  OG  SER D 396     -41.209 -30.426-144.135  1.00 40.31           O  
-ATOM  14343  N  AGLU D 397     -38.100 -31.761-146.153  0.42 32.69           N  
-ATOM  14344  N  BGLU D 397     -38.085 -31.778-146.143  0.58 36.15           N  
-ATOM  14345  CA AGLU D 397     -37.739 -33.103-146.598  0.42 27.57           C  
-ATOM  14346  CA BGLU D 397     -37.780 -33.150-146.540  0.58 26.28           C  
-ATOM  14347  C  AGLU D 397     -36.555 -33.644-145.804  0.42 27.47           C  
-ATOM  14348  C  BGLU D 397     -36.472 -33.660-145.935  0.58 27.73           C  
-ATOM  14349  O  AGLU D 397     -36.470 -34.842-145.532  0.42 27.97           O  
-ATOM  14350  O  BGLU D 397     -36.212 -34.863-145.934  0.58 28.69           O  
-ATOM  14351  CB AGLU D 397     -37.421 -33.094-148.100  0.42 24.80           C  
-ATOM  14352  CB BGLU D 397     -37.742 -33.263-148.065  0.58 24.66           C  
-ATOM  14353  CG AGLU D 397     -36.854 -34.399-148.651  0.42 27.18           C  
-ATOM  14354  CG BGLU D 397     -39.115 -33.484-148.679  0.58 24.98           C  
-ATOM  14355  CD AGLU D 397     -35.337 -34.396-148.728  0.42 25.49           C  
-ATOM  14356  CD BGLU D 397     -39.321 -32.699-149.957  0.58 28.12           C  
-ATOM  14357  OE1AGLU D 397     -34.729 -35.471-148.544  0.42 19.52           O  
-ATOM  14358  OE1BGLU D 397     -38.320 -32.408-150.646  0.58 23.54           O  
-ATOM  14359  OE2AGLU D 397     -34.755 -33.320-148.979  0.42 25.83           O  
-ATOM  14360  OE2BGLU D 397     -40.487 -32.366-150.266  0.58 21.71           O  
-ATOM  14361  N   LYS D 398     -35.652 -32.747-145.420  1.00 26.12           N  
-ATOM  14362  CA  LYS D 398     -34.439 -33.137-144.707  1.00 24.47           C  
-ATOM  14363  C   LYS D 398     -34.668 -33.170-143.198  1.00 30.96           C  
-ATOM  14364  O   LYS D 398     -33.724 -33.330-142.424  1.00 35.10           O  
-ATOM  14365  CB  LYS D 398     -33.286 -32.187-145.031  1.00 22.67           C  
-ATOM  14366  CG  LYS D 398     -32.986 -32.029-146.509  1.00 23.58           C  
-ATOM  14367  CD  LYS D 398     -31.690 -31.261-146.714  1.00 18.60           C  
-ATOM  14368  CE  LYS D 398     -31.632 -30.629-148.093  1.00 21.39           C  
-ATOM  14369  NZ  LYS D 398     -31.867 -31.625-149.174  1.00 25.74           N  
-ATOM  14370  N   GLY D 399     -35.920 -33.009-142.783  1.00 26.70           N  
-ATOM  14371  CA  GLY D 399     -36.261 -33.071-141.374  1.00 25.76           C  
-ATOM  14372  C   GLY D 399     -36.212 -31.720-140.692  1.00 33.83           C  
-ATOM  14373  O   GLY D 399     -36.534 -31.601-139.510  1.00 47.19           O  
-ATOM  14374  N   VAL D 400     -35.806 -30.697-141.437  1.00 32.28           N  
-ATOM  14375  CA  VAL D 400     -35.758 -29.340-140.907  1.00 31.13           C  
-ATOM  14376  C   VAL D 400     -37.044 -28.595-141.235  1.00 29.09           C  
-ATOM  14377  O   VAL D 400     -37.156 -27.972-142.287  1.00 27.71           O  
-ATOM  14378  CB  VAL D 400     -34.558 -28.550-141.469  1.00 27.49           C  
-ATOM  14379  CG1 VAL D 400     -34.481 -27.172-140.832  1.00 23.73           C  
-ATOM  14380  CG2 VAL D 400     -33.265 -29.315-141.238  1.00 30.18           C  
-ATOM  14381  N   LYS D 401     -38.018 -28.660-140.334  1.00 32.15           N  
-ATOM  14382  CA  LYS D 401     -39.296 -27.999-140.572  1.00 38.26           C  
-ATOM  14383  C   LYS D 401     -39.495 -26.783-139.677  1.00 36.86           C  
-ATOM  14384  O   LYS D 401     -40.488 -26.679-138.962  1.00 48.35           O  
-ATOM  14385  CB  LYS D 401     -40.448 -28.990-140.390  1.00 48.42           C  
-ATOM  14386  CG  LYS D 401     -40.226 -30.046-139.326  1.00 53.98           C  
-ATOM  14387  CD  LYS D 401     -41.065 -31.280-139.632  1.00 61.08           C  
-ATOM  14388  CE  LYS D 401     -41.331 -32.115-138.388  1.00 83.48           C  
-ATOM  14389  NZ  LYS D 401     -40.085 -32.669-137.787  1.00 74.49           N  
-ATOM  14390  N   ILE D 402     -38.543 -25.859-139.735  1.00 36.58           N  
-ATOM  14391  CA  ILE D 402     -38.630 -24.622-138.973  1.00 37.52           C  
-ATOM  14392  C   ILE D 402     -39.451 -23.585-139.721  1.00 42.95           C  
-ATOM  14393  O   ILE D 402     -39.808 -22.550-139.166  1.00 52.03           O  
-ATOM  14394  CB  ILE D 402     -37.241 -24.028-138.683  1.00 38.66           C  
-ATOM  14395  CG1 ILE D 402     -36.521 -23.697-139.993  1.00 37.62           C  
-ATOM  14396  CG2 ILE D 402     -36.417 -24.985-137.845  1.00 43.73           C  
-ATOM  14397  CD1 ILE D 402     -35.109 -23.195-139.813  1.00 31.73           C  
-ATOM  14398  N   TRP D 403     -39.756 -23.871-140.983  1.00 37.44           N  
-ATOM  14399  CA  TRP D 403     -40.435 -22.906-141.837  1.00 40.16           C  
-ATOM  14400  C   TRP D 403     -41.890 -23.255-142.115  1.00 40.60           C  
-ATOM  14401  O   TRP D 403     -42.663 -22.399-142.537  1.00 44.21           O  
-ATOM  14402  CB  TRP D 403     -39.688 -22.773-143.163  1.00 36.10           C  
-ATOM  14403  CG  TRP D 403     -38.642 -21.719-143.157  1.00 41.23           C  
-ATOM  14404  CD1 TRP D 403     -37.293 -21.903-143.104  1.00 39.84           C  
-ATOM  14405  CD2 TRP D 403     -38.856 -20.304-143.205  1.00 45.85           C  
-ATOM  14406  NE1 TRP D 403     -36.651 -20.689-143.120  1.00 48.26           N  
-ATOM  14407  CE2 TRP D 403     -37.588 -19.692-143.181  1.00 57.44           C  
-ATOM  14408  CE3 TRP D 403     -39.996 -19.496-143.266  1.00 55.43           C  
-ATOM  14409  CZ2 TRP D 403     -37.428 -18.309-143.217  1.00 60.25           C  
-ATOM  14410  CZ3 TRP D 403     -39.833 -18.121-143.302  1.00 61.44           C  
-ATOM  14411  CH2 TRP D 403     -38.559 -17.543-143.278  1.00 63.44           C  
-ATOM  14412  N   ASP D 404     -42.254 -24.509-141.872  1.00 46.35           N  
-ATOM  14413  CA  ASP D 404     -43.554 -25.035-142.283  1.00 56.57           C  
-ATOM  14414  C   ASP D 404     -44.750 -24.195-141.827  1.00 54.17           C  
-ATOM  14415  O   ASP D 404     -45.623 -23.861-142.633  1.00 45.62           O  
-ATOM  14416  CB  ASP D 404     -43.711 -26.471-141.780  1.00 54.18           C  
-ATOM  14417  CG  ASP D 404     -42.873 -27.460-142.572  1.00 59.14           C  
-ATOM  14418  OD1 ASP D 404     -42.199 -27.042-143.541  1.00 52.97           O  
-ATOM  14419  OD2 ASP D 404     -42.904 -28.661-142.237  1.00 58.58           O  
-ATOM  14420  N   LYS D 405     -44.779 -23.842-140.546  1.00 48.36           N  
-ATOM  14421  CA  LYS D 405     -45.904 -23.101-139.983  1.00 41.78           C  
-ATOM  14422  C   LYS D 405     -46.069 -21.711-140.603  1.00 37.60           C  
-ATOM  14423  O   LYS D 405     -47.090 -21.061-140.399  1.00 38.78           O  
-ATOM  14424  CB  LYS D 405     -45.751 -22.985-138.464  1.00 34.12           C  
-ATOM  14425  CG  LYS D 405     -45.848 -24.314-137.738  1.00 34.76           C  
-ATOM  14426  CD  LYS D 405     -45.734 -24.133-136.238  1.00 34.98           C  
-ATOM  14427  CE  LYS D 405     -45.703 -25.473-135.530  1.00 30.02           C  
-ATOM  14428  NZ  LYS D 405     -45.607 -25.316-134.053  1.00 29.61           N  
-ATOM  14429  N   ASN D 406     -45.074 -21.264-141.365  1.00 38.26           N  
-ATOM  14430  CA  ASN D 406     -45.142 -19.962-142.027  1.00 35.28           C  
-ATOM  14431  C   ASN D 406     -45.276 -20.084-143.542  1.00 34.48           C  
-ATOM  14432  O   ASN D 406     -45.193 -19.092-144.262  1.00 29.01           O  
-ATOM  14433  CB  ASN D 406     -43.910 -19.122-141.681  1.00 32.83           C  
-ATOM  14434  CG  ASN D 406     -43.797 -18.841-140.197  1.00 45.03           C  
-ATOM  14435  OD1 ASN D 406     -43.043 -19.503-139.486  1.00 57.55           O  
-ATOM  14436  ND2 ASN D 406     -44.556 -17.861-139.718  1.00 40.52           N  
-ATOM  14437  N   VAL D 407     -45.474 -21.308-144.024  1.00 36.01           N  
-ATOM  14438  CA  VAL D 407     -45.674 -21.542-145.454  1.00 30.27           C  
-ATOM  14439  C   VAL D 407     -46.879 -22.440-145.715  1.00 35.97           C  
-ATOM  14440  O   VAL D 407     -47.029 -22.998-146.803  1.00 37.77           O  
-ATOM  14441  CB  VAL D 407     -44.433 -22.177-146.112  1.00 32.89           C  
-ATOM  14442  CG1 VAL D 407     -43.251 -21.224-146.051  1.00 33.76           C  
-ATOM  14443  CG2 VAL D 407     -44.102 -23.503-145.452  1.00 36.57           C  
-ATOM  14444  N   THR D 408     -47.735 -22.576-144.710  1.00 45.44           N  
-ATOM  14445  CA  THR D 408     -48.992 -23.291-144.873  1.00 33.85           C  
-ATOM  14446  C   THR D 408     -49.968 -22.454-145.690  1.00 41.89           C  
-ATOM  14447  O   THR D 408     -49.820 -21.233-145.788  1.00 44.96           O  
-ATOM  14448  CB  THR D 408     -49.638 -23.640-143.514  1.00 35.84           C  
-ATOM  14449  OG1 THR D 408     -49.865 -22.442-142.760  1.00 37.38           O  
-ATOM  14450  CG2 THR D 408     -48.738 -24.562-142.720  1.00 33.10           C  
-ATOM  14451  N   ARG D 409     -50.958 -23.118-146.279  1.00 47.91           N  
-ATOM  14452  CA  ARG D 409     -52.000 -22.446-147.048  1.00 49.04           C  
-ATOM  14453  C   ARG D 409     -52.690 -21.361-146.224  1.00 46.20           C  
-ATOM  14454  O   ARG D 409     -52.947 -20.264-146.718  1.00 45.09           O  
-ATOM  14455  CB  ARG D 409     -53.028 -23.467-147.547  1.00 42.53           C  
-ATOM  14456  CG  ARG D 409     -54.265 -22.867-148.185  1.00 35.20           C  
-ATOM  14457  CD  ARG D 409     -54.141 -22.792-149.697  1.00 35.65           C  
-ATOM  14458  NE  ARG D 409     -53.391 -21.622-150.144  1.00 47.40           N  
-ATOM  14459  CZ  ARG D 409     -52.129 -21.653-150.557  1.00 44.47           C  
-ATOM  14460  NH1 ARG D 409     -51.466 -22.801-150.581  1.00 49.85           N  
-ATOM  14461  NH2 ARG D 409     -51.531 -20.535-150.950  1.00 34.82           N  
-ATOM  14462  N   GLU D 410     -52.973 -21.678-144.965  1.00 39.34           N  
-ATOM  14463  CA  GLU D 410     -53.666 -20.759-144.075  1.00 44.23           C  
-ATOM  14464  C   GLU D 410     -52.867 -19.480-143.850  1.00 46.36           C  
-ATOM  14465  O   GLU D 410     -53.398 -18.376-143.984  1.00 45.55           O  
-ATOM  14466  CB  GLU D 410     -53.960 -21.445-142.738  1.00 51.94           C  
-ATOM  14467  CG  GLU D 410     -54.922 -20.678-141.846  1.00 67.73           C  
-ATOM  14468  CD  GLU D 410     -55.265 -21.438-140.580  1.00 76.51           C  
-ATOM  14469  OE1 GLU D 410     -56.468 -21.669-140.324  1.00 81.56           O  
-ATOM  14470  OE2 GLU D 410     -54.329 -21.803-139.838  1.00 65.15           O  
-ATOM  14471  N   PHE D 411     -51.590 -19.635-143.514  1.00 44.86           N  
-ATOM  14472  CA  PHE D 411     -50.726 -18.491-143.241  1.00 46.15           C  
-ATOM  14473  C   PHE D 411     -50.473 -17.676-144.502  1.00 46.47           C  
-ATOM  14474  O   PHE D 411     -50.475 -16.444-144.463  1.00 47.65           O  
-ATOM  14475  CB  PHE D 411     -49.392 -18.944-142.642  1.00 39.61           C  
-ATOM  14476  CG  PHE D 411     -48.636 -17.843-141.948  1.00 39.13           C  
-ATOM  14477  CD1 PHE D 411     -47.810 -16.988-142.660  1.00 38.17           C  
-ATOM  14478  CD2 PHE D 411     -48.760 -17.659-140.581  1.00 48.69           C  
-ATOM  14479  CE1 PHE D 411     -47.120 -15.971-142.018  1.00 45.61           C  
-ATOM  14480  CE2 PHE D 411     -48.073 -16.648-139.934  1.00 44.01           C  
-ATOM  14481  CZ  PHE D 411     -47.253 -15.803-140.653  1.00 44.32           C  
-ATOM  14482  N   LEU D 412     -50.243 -18.369-145.614  1.00 37.84           N  
-ATOM  14483  CA  LEU D 412     -50.035 -17.706-146.895  1.00 33.38           C  
-ATOM  14484  C   LEU D 412     -51.258 -16.894-147.284  1.00 38.90           C  
-ATOM  14485  O   LEU D 412     -51.139 -15.820-147.876  1.00 38.03           O  
-ATOM  14486  CB  LEU D 412     -49.710 -18.726-147.985  1.00 39.42           C  
-ATOM  14487  CG  LEU D 412     -48.291 -19.297-147.975  1.00 34.84           C  
-ATOM  14488  CD1 LEU D 412     -48.160 -20.392-149.015  1.00 34.53           C  
-ATOM  14489  CD2 LEU D 412     -47.276 -18.194-148.222  1.00 36.84           C  
-ATOM  14490  N   ASP D 413     -52.434 -17.415-146.952  1.00 41.56           N  
-ATOM  14491  CA  ASP D 413     -53.674 -16.697-147.200  1.00 36.64           C  
-ATOM  14492  C   ASP D 413     -53.811 -15.516-146.244  1.00 39.15           C  
-ATOM  14493  O   ASP D 413     -54.372 -14.483-146.603  1.00 39.16           O  
-ATOM  14494  CB  ASP D 413     -54.875 -17.637-147.077  1.00 45.29           C  
-ATOM  14495  CG  ASP D 413     -54.927 -18.658-148.194  1.00 40.36           C  
-ATOM  14496  OD1 ASP D 413     -54.233 -18.452-149.212  1.00 40.71           O  
-ATOM  14497  OD2 ASP D 413     -55.659 -19.661-148.057  1.00 39.45           O  
-ATOM  14498  N   SER D 414     -53.292 -15.672-145.029  1.00 45.26           N  
-ATOM  14499  CA  SER D 414     -53.307 -14.591-144.048  1.00 40.79           C  
-ATOM  14500  C   SER D 414     -52.390 -13.457-144.494  1.00 46.15           C  
-ATOM  14501  O   SER D 414     -52.604 -12.296-144.142  1.00 42.26           O  
-ATOM  14502  CB  SER D 414     -52.886 -15.101-142.666  1.00 40.74           C  
-ATOM  14503  OG  SER D 414     -51.489 -15.336-142.603  1.00 42.19           O  
-ATOM  14504  N   ARG D 415     -51.369 -13.807-145.271  1.00 45.53           N  
-ATOM  14505  CA  ARG D 415     -50.445 -12.826-145.827  1.00 42.15           C  
-ATOM  14506  C   ARG D 415     -50.927 -12.300-147.176  1.00 37.16           C  
-ATOM  14507  O   ARG D 415     -50.175 -11.640-147.895  1.00 36.29           O  
-ATOM  14508  CB  ARG D 415     -49.048 -13.436-145.974  1.00 35.90           C  
-ATOM  14509  CG  ARG D 415     -48.257 -13.525-144.678  1.00 40.41           C  
-ATOM  14510  CD  ARG D 415     -47.740 -12.159-144.242  1.00 42.53           C  
-ATOM  14511  NE  ARG D 415     -46.750 -11.622-145.171  1.00 36.83           N  
-ATOM  14512  CZ  ARG D 415     -46.214 -10.409-145.076  1.00 40.83           C  
-ATOM  14513  NH1 ARG D 415     -45.320 -10.005-145.967  1.00 40.02           N  
-ATOM  14514  NH2 ARG D 415     -46.575  -9.596-144.093  1.00 45.39           N  
-ATOM  14515  N   ASN D 416     -52.183 -12.595-147.504  1.00 39.26           N  
-ATOM  14516  CA  ASN D 416     -52.780 -12.206-148.779  1.00 40.00           C  
-ATOM  14517  C   ASN D 416     -51.978 -12.724-149.969  1.00 33.62           C  
-ATOM  14518  O   ASN D 416     -51.730 -11.999-150.931  1.00 25.77           O  
-ATOM  14519  CB  ASN D 416     -52.928 -10.684-148.862  1.00 39.08           C  
-ATOM  14520  CG  ASN D 416     -53.924 -10.140-147.858  1.00 36.03           C  
-ATOM  14521  OD1 ASN D 416     -53.621 -10.012-146.672  1.00 42.97           O  
-ATOM  14522  ND2 ASN D 416     -55.117  -9.806-148.332  1.00 34.70           N  
-ATOM  14523  N   LEU D 417     -51.569 -13.986-149.886  1.00 37.16           N  
-ATOM  14524  CA  LEU D 417     -50.836 -14.635-150.966  1.00 28.48           C  
-ATOM  14525  C   LEU D 417     -51.467 -15.973-151.340  1.00 34.03           C  
-ATOM  14526  O   LEU D 417     -50.845 -17.021-151.160  1.00 33.51           O  
-ATOM  14527  CB  LEU D 417     -49.374 -14.853-150.567  1.00 31.74           C  
-ATOM  14528  CG  LEU D 417     -48.506 -13.633-150.259  1.00 33.44           C  
-ATOM  14529  CD1 LEU D 417     -47.326 -14.030-149.383  1.00 25.24           C  
-ATOM  14530  CD2 LEU D 417     -48.021 -12.987-151.547  1.00 32.89           C  
-ATOM  14531  N   PRO D 418     -52.703 -15.948-151.867  1.00 38.79           N  
-ATOM  14532  CA  PRO D 418     -53.360 -17.212-152.212  1.00 34.08           C  
-ATOM  14533  C   PRO D 418     -52.714 -17.895-153.413  1.00 29.34           C  
-ATOM  14534  O   PRO D 418     -52.895 -19.094-153.605  1.00 34.31           O  
-ATOM  14535  CB  PRO D 418     -54.793 -16.780-152.532  1.00 28.07           C  
-ATOM  14536  CG  PRO D 418     -54.649 -15.393-153.031  1.00 25.42           C  
-ATOM  14537  CD  PRO D 418     -53.536 -14.784-152.219  1.00 31.19           C  
-ATOM  14538  N   HIS D 419     -51.964 -17.132-154.201  1.00 28.00           N  
-ATOM  14539  CA  HIS D 419     -51.352 -17.642-155.422  1.00 28.60           C  
-ATOM  14540  C   HIS D 419     -50.014 -18.327-155.162  1.00 34.74           C  
-ATOM  14541  O   HIS D 419     -49.340 -18.760-156.098  1.00 30.52           O  
-ATOM  14542  CB  HIS D 419     -51.166 -16.506-156.429  1.00 36.47           C  
-ATOM  14543  CG  HIS D 419     -50.446 -15.317-155.873  1.00 41.21           C  
-ATOM  14544  ND1 HIS D 419     -51.099 -14.274-155.252  1.00 34.74           N  
-ATOM  14545  CD2 HIS D 419     -49.127 -15.005-155.843  1.00 33.80           C  
-ATOM  14546  CE1 HIS D 419     -50.215 -13.372-154.864  1.00 31.85           C  
-ATOM  14547  NE2 HIS D 419     -49.012 -13.791-155.211  1.00 35.21           N  
-ATOM  14548  N   ARG D 420     -49.635 -18.424-153.892  1.00 41.09           N  
-ATOM  14549  CA  ARG D 420     -48.383 -19.072-153.514  1.00 41.34           C  
-ATOM  14550  C   ARG D 420     -48.586 -20.555-153.226  1.00 44.06           C  
-ATOM  14551  O   ARG D 420     -49.539 -20.938-152.546  1.00 44.71           O  
-ATOM  14552  CB  ARG D 420     -47.774 -18.392-152.287  1.00 31.18           C  
-ATOM  14553  CG  ARG D 420     -47.121 -17.050-152.567  1.00 33.78           C  
-ATOM  14554  CD  ARG D 420     -45.681 -17.210-153.029  1.00 32.58           C  
-ATOM  14555  NE  ARG D 420     -44.989 -15.925-153.080  1.00 39.50           N  
-ATOM  14556  CZ  ARG D 420     -44.920 -15.154-154.161  1.00 38.05           C  
-ATOM  14557  NH1 ARG D 420     -44.271 -13.998-154.113  1.00 31.16           N  
-ATOM  14558  NH2 ARG D 420     -45.497 -15.540-155.291  1.00 35.01           N  
-ATOM  14559  N   GLU D 421     -47.689 -21.387-153.750  1.00 40.75           N  
-ATOM  14560  CA  GLU D 421     -47.671 -22.806-153.411  1.00 38.20           C  
-ATOM  14561  C   GLU D 421     -47.319 -22.981-151.943  1.00 37.23           C  
-ATOM  14562  O   GLU D 421     -46.632 -22.141-151.362  1.00 39.95           O  
-ATOM  14563  CB  GLU D 421     -46.662 -23.569-154.268  1.00 30.67           C  
-ATOM  14564  CG  GLU D 421     -47.246 -24.239-155.494  1.00 30.09           C  
-ATOM  14565  CD  GLU D 421     -46.296 -25.258-156.093  1.00 46.09           C  
-ATOM  14566  OE1 GLU D 421     -45.942 -26.228-155.387  1.00 38.24           O  
-ATOM  14567  OE2 GLU D 421     -45.897 -25.087-157.265  1.00 52.55           O  
-ATOM  14568  N   VAL D 422     -47.787 -24.070-151.343  1.00 34.48           N  
-ATOM  14569  CA  VAL D 422     -47.371 -24.413-149.990  1.00 29.14           C  
-ATOM  14570  C   VAL D 422     -45.874 -24.698-149.984  1.00 26.83           C  
-ATOM  14571  O   VAL D 422     -45.399 -25.577-150.702  1.00 26.03           O  
-ATOM  14572  CB  VAL D 422     -48.133 -25.632-149.442  1.00 25.14           C  
-ATOM  14573  CG1 VAL D 422     -47.496 -26.114-148.147  1.00 27.58           C  
-ATOM  14574  CG2 VAL D 422     -49.597 -25.292-149.227  1.00 32.10           C  
-ATOM  14575  N   GLY D 423     -45.134 -23.937-149.186  1.00 26.70           N  
-ATOM  14576  CA  GLY D 423     -43.697 -24.104-149.092  1.00 28.45           C  
-ATOM  14577  C   GLY D 423     -42.929 -22.916-149.637  1.00 27.30           C  
-ATOM  14578  O   GLY D 423     -41.774 -22.698-149.279  1.00 30.72           O  
-ATOM  14579  N   ASP D 424     -43.572 -22.143-150.505  1.00 28.11           N  
-ATOM  14580  CA  ASP D 424     -42.925 -20.993-151.125  1.00 20.42           C  
-ATOM  14581  C   ASP D 424     -42.875 -19.806-150.167  1.00 29.59           C  
-ATOM  14582  O   ASP D 424     -43.908 -19.228-149.824  1.00 36.64           O  
-ATOM  14583  CB  ASP D 424     -43.654 -20.605-152.412  1.00 21.24           C  
-ATOM  14584  CG  ASP D 424     -42.789 -19.785-153.348  1.00 30.90           C  
-ATOM  14585  OD1 ASP D 424     -41.936 -19.014-152.859  1.00 34.09           O  
-ATOM  14586  OD2 ASP D 424     -42.959 -19.913-154.579  1.00 30.86           O  
-ATOM  14587  N   ILE D 425     -41.667 -19.438-149.747  1.00 27.04           N  
-ATOM  14588  CA  ILE D 425     -41.488 -18.337-148.805  1.00 35.62           C  
-ATOM  14589  C   ILE D 425     -41.441 -16.981-149.508  1.00 33.73           C  
-ATOM  14590  O   ILE D 425     -41.231 -15.948-148.868  1.00 30.95           O  
-ATOM  14591  CB  ILE D 425     -40.198 -18.505-147.975  1.00 28.46           C  
-ATOM  14592  CG1 ILE D 425     -38.966 -18.191-148.826  1.00 29.88           C  
-ATOM  14593  CG2 ILE D 425     -40.111 -19.906-147.399  1.00 24.41           C  
-ATOM  14594  CD1 ILE D 425     -37.732 -17.897-148.009  1.00 26.25           C  
-ATOM  14595  N   GLY D 426     -41.639 -16.987-150.822  1.00 26.80           N  
-ATOM  14596  CA  GLY D 426     -41.553 -15.771-151.608  1.00 29.74           C  
-ATOM  14597  C   GLY D 426     -40.116 -15.302-151.744  1.00 29.88           C  
-ATOM  14598  O   GLY D 426     -39.196 -16.005-151.331  1.00 29.08           O  
-ATOM  14599  N   PRO D 427     -39.913 -14.106-152.317  1.00 27.67           N  
-ATOM  14600  CA  PRO D 427     -38.571 -13.542-152.514  1.00 28.83           C  
-ATOM  14601  C   PRO D 427     -37.874 -13.150-151.209  1.00 32.13           C  
-ATOM  14602  O   PRO D 427     -37.462 -11.997-151.064  1.00 30.44           O  
-ATOM  14603  CB  PRO D 427     -38.842 -12.301-153.370  1.00 19.89           C  
-ATOM  14604  CG  PRO D 427     -40.236 -11.918-153.036  1.00 23.65           C  
-ATOM  14605  CD  PRO D 427     -40.963 -13.215-152.839  1.00 22.99           C  
-ATOM  14606  N   GLY D 428     -37.731 -14.097-150.285  1.00 25.12           N  
-ATOM  14607  CA  GLY D 428     -37.130 -13.824-148.992  1.00 16.62           C  
-ATOM  14608  C   GLY D 428     -35.656 -14.175-148.894  1.00 24.90           C  
-ATOM  14609  O   GLY D 428     -35.069 -14.677-149.852  1.00 34.41           O  
-ATOM  14610  N   TYR D 429     -35.086 -13.904-147.718  1.00 31.21           N  
-ATOM  14611  CA  TYR D 429     -33.669 -14.109-147.371  1.00 31.97           C  
-ATOM  14612  C   TYR D 429     -32.702 -14.417-148.521  1.00 29.80           C  
-ATOM  14613  O   TYR D 429     -32.130 -13.508-149.123  1.00 29.59           O  
-ATOM  14614  CB  TYR D 429     -33.559 -15.224-146.324  1.00 25.38           C  
-ATOM  14615  CG  TYR D 429     -34.186 -14.880-144.986  1.00 35.24           C  
-ATOM  14616  CD1 TYR D 429     -33.632 -13.904-144.168  1.00 41.94           C  
-ATOM  14617  CD2 TYR D 429     -35.323 -15.539-144.538  1.00 46.46           C  
-ATOM  14618  CE1 TYR D 429     -34.198 -13.589-142.943  1.00 40.48           C  
-ATOM  14619  CE2 TYR D 429     -35.897 -15.232-143.316  1.00 45.60           C  
-ATOM  14620  CZ  TYR D 429     -35.331 -14.258-142.522  1.00 48.47           C  
-ATOM  14621  OH  TYR D 429     -35.906 -13.955-141.307  1.00 42.93           O  
-ATOM  14622  N   GLY D 430     -32.524 -15.701-148.813  1.00 33.80           N  
-ATOM  14623  CA  GLY D 430     -31.585 -16.142-149.833  1.00 30.81           C  
-ATOM  14624  C   GLY D 430     -31.782 -15.521-151.204  1.00 31.60           C  
-ATOM  14625  O   GLY D 430     -30.813 -15.163-151.882  1.00 36.97           O  
-ATOM  14626  N   PHE D 431     -33.040 -15.399-151.615  1.00 25.18           N  
-ATOM  14627  CA  PHE D 431     -33.360 -14.808-152.906  1.00 27.16           C  
-ATOM  14628  C   PHE D 431     -32.871 -13.372-152.990  1.00 30.90           C  
-ATOM  14629  O   PHE D 431     -32.478 -12.913-154.060  1.00 25.63           O  
-ATOM  14630  CB  PHE D 431     -34.863 -14.848-153.177  1.00 23.21           C  
-ATOM  14631  CG  PHE D 431     -35.255 -14.182-154.466  1.00 24.39           C  
-ATOM  14632  CD1 PHE D 431     -35.211 -14.877-155.662  1.00 26.71           C  
-ATOM  14633  CD2 PHE D 431     -35.648 -12.854-154.485  1.00 23.54           C  
-ATOM  14634  CE1 PHE D 431     -35.563 -14.263-156.851  1.00 24.85           C  
-ATOM  14635  CE2 PHE D 431     -36.001 -12.235-155.669  1.00 26.02           C  
-ATOM  14636  CZ  PHE D 431     -35.959 -12.941-156.854  1.00 20.02           C  
-ATOM  14637  N   GLN D 432     -32.912 -12.660-151.868  1.00 29.62           N  
-ATOM  14638  CA  GLN D 432     -32.407 -11.297-151.833  1.00 24.36           C  
-ATOM  14639  C   GLN D 432     -30.886 -11.321-151.815  1.00 23.17           C  
-ATOM  14640  O   GLN D 432     -30.242 -10.549-152.524  1.00 33.38           O  
-ATOM  14641  CB  GLN D 432     -32.972 -10.540-150.626  1.00 21.93           C  
-ATOM  14642  CG  GLN D 432     -34.468 -10.271-150.732  1.00 25.22           C  
-ATOM  14643  CD  GLN D 432     -34.828  -9.467-151.975  1.00 25.85           C  
-ATOM  14644  OE1 GLN D 432     -34.093  -8.566-152.378  1.00 30.20           O  
-ATOM  14645  NE2 GLN D 432     -35.962  -9.791-152.587  1.00 30.17           N  
-ATOM  14646  N   TRP D 433     -30.334 -12.226-151.009  1.00 23.25           N  
-ATOM  14647  CA  TRP D 433     -28.892 -12.457-150.910  1.00 20.32           C  
-ATOM  14648  C   TRP D 433     -28.223 -12.593-152.271  1.00 23.90           C  
-ATOM  14649  O   TRP D 433     -27.257 -11.891-152.573  1.00 27.01           O  
-ATOM  14650  CB  TRP D 433     -28.600 -13.730-150.108  1.00 24.18           C  
-ATOM  14651  CG  TRP D 433     -28.661 -13.597-148.623  1.00 27.92           C  
-ATOM  14652  CD1 TRP D 433     -29.273 -12.611-147.908  1.00 32.05           C  
-ATOM  14653  CD2 TRP D 433     -28.076 -14.484-147.665  1.00 24.17           C  
-ATOM  14654  NE1 TRP D 433     -29.112 -12.831-146.563  1.00 36.47           N  
-ATOM  14655  CE2 TRP D 433     -28.379 -13.975-146.388  1.00 29.75           C  
-ATOM  14656  CE3 TRP D 433     -27.328 -15.659-147.763  1.00 23.18           C  
-ATOM  14657  CZ2 TRP D 433     -27.958 -14.603-145.218  1.00 34.28           C  
-ATOM  14658  CZ3 TRP D 433     -26.912 -16.278-146.606  1.00 29.33           C  
-ATOM  14659  CH2 TRP D 433     -27.226 -15.751-145.349  1.00 28.39           C  
-ATOM  14660  N   ARG D 434     -28.744 -13.504-153.087  1.00 23.53           N  
-ATOM  14661  CA  ARG D 434     -28.102 -13.842-154.348  1.00 21.43           C  
-ATOM  14662  C   ARG D 434     -28.671 -13.055-155.524  1.00 26.28           C  
-ATOM  14663  O   ARG D 434     -27.974 -12.818-156.511  1.00 25.94           O  
-ATOM  14664  CB  ARG D 434     -28.226 -15.345-154.610  1.00 21.62           C  
-ATOM  14665  CG  ARG D 434     -27.786 -16.228-153.447  1.00 21.78           C  
-ATOM  14666  CD  ARG D 434     -26.424 -15.815-152.905  1.00 21.25           C  
-ATOM  14667  NE  ARG D 434     -25.400 -15.796-153.945  1.00 33.31           N  
-ATOM  14668  CZ  ARG D 434     -24.560 -16.797-154.190  1.00 31.31           C  
-ATOM  14669  NH1 ARG D 434     -23.659 -16.686-155.157  1.00 20.54           N  
-ATOM  14670  NH2 ARG D 434     -24.614 -17.907-153.466  1.00 36.56           N  
-ATOM  14671  N   HIS D 435     -29.936 -12.659-155.422  1.00 29.10           N  
-ATOM  14672  CA  HIS D 435     -30.586 -11.921-156.500  1.00 32.89           C  
-ATOM  14673  C   HIS D 435     -31.421 -10.762-155.977  1.00 24.75           C  
-ATOM  14674  O   HIS D 435     -32.627 -10.729-156.196  1.00 28.06           O  
-ATOM  14675  CB  HIS D 435     -31.486 -12.844-157.328  1.00 31.90           C  
-ATOM  14676  CG  HIS D 435     -30.934 -14.222-157.520  1.00 34.59           C  
-ATOM  14677  ND1 HIS D 435     -29.846 -14.483-158.324  1.00 30.50           N  
-ATOM  14678  CD2 HIS D 435     -31.320 -15.414-157.009  1.00 26.78           C  
-ATOM  14679  CE1 HIS D 435     -29.584 -15.778-158.299  1.00 40.56           C  
-ATOM  14680  NE2 HIS D 435     -30.465 -16.366-157.508  1.00 33.19           N  
-ATOM  14681  N   PHE D 436     -30.789  -9.813-155.293  1.00 23.65           N  
-ATOM  14682  CA  PHE D 436     -31.497  -8.626-154.818  1.00 21.04           C  
-ATOM  14683  C   PHE D 436     -32.139  -7.845-155.966  1.00 22.37           C  
-ATOM  14684  O   PHE D 436     -31.503  -7.581-156.986  1.00 24.15           O  
-ATOM  14685  CB  PHE D 436     -30.551  -7.707-154.044  1.00 20.44           C  
-ATOM  14686  CG  PHE D 436     -31.249  -6.580-153.330  1.00 21.67           C  
-ATOM  14687  CD1 PHE D 436     -31.550  -5.399-153.990  1.00 21.08           C  
-ATOM  14688  CD2 PHE D 436     -31.600  -6.702-151.996  1.00 23.85           C  
-ATOM  14689  CE1 PHE D 436     -32.197  -4.367-153.335  1.00 27.08           C  
-ATOM  14690  CE2 PHE D 436     -32.242  -5.671-151.336  1.00 24.55           C  
-ATOM  14691  CZ  PHE D 436     -32.540  -4.504-152.005  1.00 21.81           C  
-ATOM  14692  N   GLY D 437     -33.404  -7.479-155.787  1.00 28.40           N  
-ATOM  14693  CA  GLY D 437     -34.101  -6.619-156.729  1.00 33.34           C  
-ATOM  14694  C   GLY D 437     -34.707  -7.316-157.934  1.00 29.36           C  
-ATOM  14695  O   GLY D 437     -35.388  -6.684-158.743  1.00 26.25           O  
-ATOM  14696  N   ALA D 438     -34.462  -8.616-158.058  1.00 32.30           N  
-ATOM  14697  CA  ALA D 438     -34.974  -9.383-159.187  1.00 22.33           C  
-ATOM  14698  C   ALA D 438     -36.476  -9.606-159.054  1.00 26.93           C  
-ATOM  14699  O   ALA D 438     -37.008  -9.660-157.945  1.00 24.89           O  
-ATOM  14700  CB  ALA D 438     -34.243 -10.713-159.298  1.00 21.84           C  
-ATOM  14701  N   ALA D 439     -37.155  -9.725-160.191  1.00 26.75           N  
-ATOM  14702  CA  ALA D 439     -38.589  -9.986-160.200  1.00 25.09           C  
-ATOM  14703  C   ALA D 439     -38.859 -11.444-159.848  1.00 35.35           C  
-ATOM  14704  O   ALA D 439     -38.367 -12.350-160.520  1.00 36.46           O  
-ATOM  14705  CB  ALA D 439     -39.185  -9.643-161.557  1.00 35.40           C  
-ATOM  14706  N   TYR D 440     -39.635 -11.667-158.791  1.00 30.95           N  
-ATOM  14707  CA  TYR D 440     -39.913 -13.018-158.315  1.00 23.16           C  
-ATOM  14708  C   TYR D 440     -41.124 -13.630-159.011  1.00 33.77           C  
-ATOM  14709  O   TYR D 440     -42.134 -12.959-159.227  1.00 36.72           O  
-ATOM  14710  CB  TYR D 440     -40.136 -13.013-156.801  1.00 23.11           C  
-ATOM  14711  CG  TYR D 440     -40.164 -14.393-156.177  1.00 28.20           C  
-ATOM  14712  CD1 TYR D 440     -38.986 -15.043-155.838  1.00 31.02           C  
-ATOM  14713  CD2 TYR D 440     -41.365 -15.041-155.922  1.00 30.48           C  
-ATOM  14714  CE1 TYR D 440     -39.001 -16.301-155.266  1.00 27.85           C  
-ATOM  14715  CE2 TYR D 440     -41.391 -16.301-155.350  1.00 28.44           C  
-ATOM  14716  CZ  TYR D 440     -40.205 -16.924-155.025  1.00 27.07           C  
-ATOM  14717  OH  TYR D 440     -40.220 -18.175-154.457  1.00 25.92           O  
-ATOM  14718  N   LYS D 441     -41.015 -14.909-159.361  1.00 32.36           N  
-ATOM  14719  CA  LYS D 441     -42.132 -15.649-159.939  1.00 24.15           C  
-ATOM  14720  C   LYS D 441     -42.632 -16.695-158.949  1.00 27.35           C  
-ATOM  14721  O   LYS D 441     -43.654 -16.503-158.291  1.00 31.62           O  
-ATOM  14722  CB  LYS D 441     -41.727 -16.313-161.258  1.00 25.22           C  
-ATOM  14723  CG  LYS D 441     -41.903 -15.435-162.495  1.00 46.28           C  
-ATOM  14724  CD  LYS D 441     -40.920 -14.273-162.518  1.00 55.43           C  
-ATOM  14725  CE  LYS D 441     -41.112 -13.405-163.753  1.00 49.73           C  
-ATOM  14726  NZ  LYS D 441     -40.916 -14.179-165.010  1.00 55.42           N  
-ATOM  14727  N   ASP D 442     -41.903 -17.801-158.849  1.00 32.57           N  
-ATOM  14728  CA  ASP D 442     -42.216 -18.839-157.874  1.00 33.21           C  
-ATOM  14729  C   ASP D 442     -40.953 -19.605-157.486  1.00 28.66           C  
-ATOM  14730  O   ASP D 442     -39.871 -19.339-158.009  1.00 23.99           O  
-ATOM  14731  CB  ASP D 442     -43.284 -19.793-158.417  1.00 32.46           C  
-ATOM  14732  CG  ASP D 442     -42.843 -20.511-159.676  1.00 36.05           C  
-ATOM  14733  OD1 ASP D 442     -41.927 -20.011-160.361  1.00 36.23           O  
-ATOM  14734  OD2 ASP D 442     -43.420 -21.577-159.981  1.00 39.80           O  
-ATOM  14735  N   MET D 443     -41.096 -20.559-156.573  1.00 28.59           N  
-ATOM  14736  CA  MET D 443     -39.946 -21.260-156.010  1.00 30.78           C  
-ATOM  14737  C   MET D 443     -39.328 -22.271-156.970  1.00 28.19           C  
-ATOM  14738  O   MET D 443     -38.378 -22.969-156.615  1.00 40.34           O  
-ATOM  14739  CB  MET D 443     -40.345 -21.968-154.714  1.00 29.25           C  
-ATOM  14740  CG  MET D 443     -41.410 -23.033-154.898  1.00 27.30           C  
-ATOM  14741  SD  MET D 443     -41.987 -23.714-153.335  1.00 35.63           S  
-ATOM  14742  CE  MET D 443     -43.197 -24.905-153.905  1.00 33.65           C  
-ATOM  14743  N   HIS D 444     -39.865 -22.354-158.182  1.00 27.43           N  
-ATOM  14744  CA  HIS D 444     -39.355 -23.301-159.166  1.00 36.13           C  
-ATOM  14745  C   HIS D 444     -38.611 -22.584-160.286  1.00 32.84           C  
-ATOM  14746  O   HIS D 444     -37.924 -23.213-161.090  1.00 28.88           O  
-ATOM  14747  CB  HIS D 444     -40.496 -24.141-159.739  1.00 30.90           C  
-ATOM  14748  CG  HIS D 444     -41.290 -24.864-158.697  1.00 33.26           C  
-ATOM  14749  ND1 HIS D 444     -40.732 -25.800-157.854  1.00 36.11           N  
-ATOM  14750  CD2 HIS D 444     -42.599 -24.785-158.359  1.00 31.25           C  
-ATOM  14751  CE1 HIS D 444     -41.663 -26.268-157.043  1.00 37.58           C  
-ATOM  14752  NE2 HIS D 444     -42.805 -25.669-157.329  1.00 30.26           N  
-ATOM  14753  N   THR D 445     -38.747 -21.263-160.327  1.00 33.52           N  
-ATOM  14754  CA  THR D 445     -38.126 -20.465-161.374  1.00 29.26           C  
-ATOM  14755  C   THR D 445     -36.627 -20.307-161.134  1.00 27.49           C  
-ATOM  14756  O   THR D 445     -36.185 -20.098-160.005  1.00 31.36           O  
-ATOM  14757  CB  THR D 445     -38.775 -19.070-161.478  1.00 28.91           C  
-ATOM  14758  OG1 THR D 445     -40.200 -19.209-161.538  1.00 29.41           O  
-ATOM  14759  CG2 THR D 445     -38.288 -18.341-162.721  1.00 32.01           C  
-ATOM  14760  N   ASP D 446     -35.854 -20.416-162.209  1.00 31.21           N  
-ATOM  14761  CA  ASP D 446     -34.412 -20.224-162.154  1.00 34.62           C  
-ATOM  14762  C   ASP D 446     -34.065 -18.748-162.342  1.00 36.97           C  
-ATOM  14763  O   ASP D 446     -34.326 -18.172-163.398  1.00 37.85           O  
-ATOM  14764  CB  ASP D 446     -33.726 -21.077-163.221  1.00 36.99           C  
-ATOM  14765  CG  ASP D 446     -32.223 -20.909-163.227  1.00 44.35           C  
-ATOM  14766  OD1 ASP D 446     -31.622 -20.873-162.132  1.00 55.56           O  
-ATOM  14767  OD2 ASP D 446     -31.644 -20.812-164.329  1.00 35.64           O  
-ATOM  14768  N   TYR D 447     -33.477 -18.137-161.319  1.00 39.17           N  
-ATOM  14769  CA  TYR D 447     -33.185 -16.707-161.359  1.00 36.38           C  
-ATOM  14770  C   TYR D 447     -31.704 -16.410-161.556  1.00 37.73           C  
-ATOM  14771  O   TYR D 447     -31.249 -15.313-161.228  1.00 33.71           O  
-ATOM  14772  CB  TYR D 447     -33.662 -16.025-160.074  1.00 30.34           C  
-ATOM  14773  CG  TYR D 447     -35.121 -16.242-159.759  1.00 25.57           C  
-ATOM  14774  CD1 TYR D 447     -36.109 -15.529-160.424  1.00 25.03           C  
-ATOM  14775  CD2 TYR D 447     -35.511 -17.153-158.787  1.00 25.11           C  
-ATOM  14776  CE1 TYR D 447     -37.446 -15.725-160.136  1.00 27.40           C  
-ATOM  14777  CE2 TYR D 447     -36.844 -17.354-158.491  1.00 30.18           C  
-ATOM  14778  CZ  TYR D 447     -37.808 -16.638-159.167  1.00 30.39           C  
-ATOM  14779  OH  TYR D 447     -39.139 -16.840-158.873  1.00 32.69           O  
-ATOM  14780  N   THR D 448     -30.953 -17.371-162.086  1.00 43.25           N  
-ATOM  14781  CA  THR D 448     -29.509 -17.195-162.212  1.00 48.49           C  
-ATOM  14782  C   THR D 448     -29.177 -16.019-163.136  1.00 40.66           C  
-ATOM  14783  O   THR D 448     -29.827 -15.810-164.163  1.00 39.60           O  
-ATOM  14784  CB  THR D 448     -28.812 -18.485-162.716  1.00 36.99           C  
-ATOM  14785  OG1 THR D 448     -27.391 -18.326-162.626  1.00 45.84           O  
-ATOM  14786  CG2 THR D 448     -29.196 -18.804-164.154  1.00 42.24           C  
-ATOM  14787  N   GLY D 449     -28.185 -15.229-162.735  1.00 39.33           N  
-ATOM  14788  CA  GLY D 449     -27.776 -14.067-163.502  1.00 41.18           C  
-ATOM  14789  C   GLY D 449     -28.597 -12.822-163.218  1.00 37.03           C  
-ATOM  14790  O   GLY D 449     -28.177 -11.708-163.533  1.00 43.54           O  
-ATOM  14791  N   GLN D 450     -29.770 -13.006-162.622  1.00 33.94           N  
-ATOM  14792  CA  GLN D 450     -30.661 -11.887-162.328  1.00 38.18           C  
-ATOM  14793  C   GLN D 450     -30.348 -11.239-160.980  1.00 43.64           C  
-ATOM  14794  O   GLN D 450     -29.854 -11.898-160.063  1.00 41.48           O  
-ATOM  14795  CB  GLN D 450     -32.119 -12.346-162.346  1.00 31.30           C  
-ATOM  14796  CG  GLN D 450     -32.569 -12.980-163.648  1.00 36.17           C  
-ATOM  14797  CD  GLN D 450     -34.012 -13.442-163.592  1.00 40.15           C  
-ATOM  14798  OE1 GLN D 450     -34.895 -12.706-163.149  1.00 37.05           O  
-ATOM  14799  NE2 GLN D 450     -34.258 -14.670-164.031  1.00 42.95           N  
-ATOM  14800  N   GLY D 451     -30.644  -9.946-160.867  1.00 40.01           N  
-ATOM  14801  CA  GLY D 451     -30.466  -9.216-159.624  1.00 26.86           C  
-ATOM  14802  C   GLY D 451     -29.013  -9.042-159.231  1.00 30.96           C  
-ATOM  14803  O   GLY D 451     -28.109  -9.372-159.997  1.00 34.97           O  
-ATOM  14804  N   VAL D 452     -28.791  -8.523-158.027  1.00 24.51           N  
-ATOM  14805  CA  VAL D 452     -27.440  -8.313-157.515  1.00 23.48           C  
-ATOM  14806  C   VAL D 452     -27.007  -9.478-156.631  1.00 26.55           C  
-ATOM  14807  O   VAL D 452     -27.751  -9.903-155.747  1.00 26.36           O  
-ATOM  14808  CB  VAL D 452     -27.341  -7.003-156.712  1.00 17.30           C  
-ATOM  14809  CG1 VAL D 452     -25.944  -6.828-156.131  1.00 18.92           C  
-ATOM  14810  CG2 VAL D 452     -27.705  -5.820-157.593  1.00 16.33           C  
-ATOM  14811  N   ASP D 453     -25.807  -9.998-156.872  1.00 25.66           N  
-ATOM  14812  CA  ASP D 453     -25.272 -11.069-156.039  1.00 22.09           C  
-ATOM  14813  C   ASP D 453     -24.437 -10.508-154.891  1.00 27.49           C  
-ATOM  14814  O   ASP D 453     -23.207 -10.482-154.948  1.00 30.26           O  
-ATOM  14815  CB  ASP D 453     -24.443 -12.040-156.878  1.00 28.11           C  
-ATOM  14816  CG  ASP D 453     -24.200 -13.358-156.171  1.00 30.46           C  
-ATOM  14817  OD1 ASP D 453     -24.270 -13.400-154.923  1.00 27.84           O  
-ATOM  14818  OD2 ASP D 453     -23.931 -14.357-156.868  1.00 31.92           O  
-ATOM  14819  N   GLN D 454     -25.129 -10.076-153.842  1.00 27.97           N  
-ATOM  14820  CA  GLN D 454     -24.496  -9.460-152.684  1.00 18.32           C  
-ATOM  14821  C   GLN D 454     -23.426 -10.339-152.064  1.00 22.63           C  
-ATOM  14822  O   GLN D 454     -22.399  -9.839-151.620  1.00 27.53           O  
-ATOM  14823  CB  GLN D 454     -25.535  -9.124-151.623  1.00 15.58           C  
-ATOM  14824  CG  GLN D 454     -26.590  -8.148-152.082  1.00 17.98           C  
-ATOM  14825  CD  GLN D 454     -27.474  -7.689-150.946  1.00 22.56           C  
-ATOM  14826  OE1 GLN D 454     -27.180  -6.699-150.277  1.00 23.35           O  
-ATOM  14827  NE2 GLN D 454     -28.564  -8.410-150.718  1.00 25.47           N  
-ATOM  14828  N   LEU D 455     -23.670 -11.646-152.024  1.00 21.85           N  
-ATOM  14829  CA  LEU D 455     -22.725 -12.572-151.410  1.00 28.74           C  
-ATOM  14830  C   LEU D 455     -21.416 -12.618-152.194  1.00 25.50           C  
-ATOM  14831  O   LEU D 455     -20.323 -12.472-151.629  1.00 19.79           O  
-ATOM  14832  CB  LEU D 455     -23.347 -13.967-151.310  1.00 19.94           C  
-ATOM  14833  CG  LEU D 455     -22.612 -15.006-150.463  1.00 20.16           C  
-ATOM  14834  CD1 LEU D 455     -22.406 -14.499-149.049  1.00 20.19           C  
-ATOM  14835  CD2 LEU D 455     -23.385 -16.312-150.447  1.00 19.43           C  
-ATOM  14836  N   LYS D 456     -21.542 -12.814-153.501  1.00 26.91           N  
-ATOM  14837  CA  LYS D 456     -20.382 -12.879-154.380  1.00 31.72           C  
-ATOM  14838  C   LYS D 456     -19.625 -11.562-154.372  1.00 28.79           C  
-ATOM  14839  O   LYS D 456     -18.398 -11.546-154.417  1.00 24.95           O  
-ATOM  14840  CB  LYS D 456     -20.796 -13.234-155.811  1.00 30.40           C  
-ATOM  14841  CG  LYS D 456     -19.629 -13.602-156.710  1.00 36.02           C  
-ATOM  14842  CD  LYS D 456     -20.077 -13.812-158.148  1.00 43.19           C  
-ATOM  14843  CE  LYS D 456     -19.950 -12.535-158.970  1.00 63.26           C  
-ATOM  14844  NZ  LYS D 456     -20.835 -11.440-158.477  1.00 60.11           N  
-ATOM  14845  N   ASN D 457     -20.363 -10.458-154.315  1.00 24.65           N  
-ATOM  14846  CA  ASN D 457     -19.746  -9.141-154.228  1.00 25.94           C  
-ATOM  14847  C   ASN D 457     -18.952  -8.984-152.934  1.00 28.11           C  
-ATOM  14848  O   ASN D 457     -17.812  -8.524-152.953  1.00 28.98           O  
-ATOM  14849  CB  ASN D 457     -20.805  -8.035-154.335  1.00 23.33           C  
-ATOM  14850  CG  ASN D 457     -21.483  -8.005-155.688  1.00 28.20           C  
-ATOM  14851  OD1 ASN D 457     -21.082  -8.714-156.613  1.00 28.67           O  
-ATOM  14852  ND2 ASN D 457     -22.516  -7.175-155.815  1.00 25.21           N  
-ATOM  14853  N   VAL D 458     -19.563  -9.370-151.818  1.00 23.92           N  
-ATOM  14854  CA  VAL D 458     -18.927  -9.278-150.510  1.00 23.81           C  
-ATOM  14855  C   VAL D 458     -17.647 -10.096-150.467  1.00 22.91           C  
-ATOM  14856  O   VAL D 458     -16.615  -9.624-149.995  1.00 25.09           O  
-ATOM  14857  CB  VAL D 458     -19.870  -9.753-149.385  1.00 22.16           C  
-ATOM  14858  CG1 VAL D 458     -19.077 -10.121-148.142  1.00 21.05           C  
-ATOM  14859  CG2 VAL D 458     -20.895  -8.679-149.066  1.00 20.74           C  
-ATOM  14860  N   ILE D 459     -17.715 -11.322-150.971  1.00 23.92           N  
-ATOM  14861  CA  ILE D 459     -16.532 -12.172-151.013  1.00 23.98           C  
-ATOM  14862  C   ILE D 459     -15.455 -11.585-151.924  1.00 24.10           C  
-ATOM  14863  O   ILE D 459     -14.276 -11.578-151.566  1.00 25.19           O  
-ATOM  14864  CB  ILE D 459     -16.882 -13.596-151.474  1.00 19.23           C  
-ATOM  14865  CG1 ILE D 459     -17.785 -14.265-150.440  1.00 21.33           C  
-ATOM  14866  CG2 ILE D 459     -15.617 -14.416-151.687  1.00 15.15           C  
-ATOM  14867  CD1 ILE D 459     -18.123 -15.699-150.765  1.00 30.83           C  
-ATOM  14868  N   GLN D 460     -15.858 -11.083-153.090  1.00 21.85           N  
-ATOM  14869  CA  GLN D 460     -14.909 -10.485-154.027  1.00 24.00           C  
-ATOM  14870  C   GLN D 460     -14.169  -9.315-153.398  1.00 21.61           C  
-ATOM  14871  O   GLN D 460     -12.948  -9.216-153.494  1.00 20.48           O  
-ATOM  14872  CB  GLN D 460     -15.619 -10.025-155.305  1.00 39.33           C  
-ATOM  14873  CG  GLN D 460     -14.730  -9.221-156.258  1.00 46.90           C  
-ATOM  14874  CD  GLN D 460     -13.745 -10.087-157.029  1.00 39.95           C  
-ATOM  14875  OE1 GLN D 460     -13.680 -11.304-156.838  1.00 42.89           O  
-ATOM  14876  NE2 GLN D 460     -12.976  -9.459-157.911  1.00 27.52           N  
-ATOM  14877  N   MET D 461     -14.924  -8.435-152.751  1.00 28.85           N  
-ATOM  14878  CA  MET D 461     -14.352  -7.269-152.090  1.00 26.45           C  
-ATOM  14879  C   MET D 461     -13.478  -7.686-150.917  1.00 22.84           C  
-ATOM  14880  O   MET D 461     -12.489  -7.033-150.615  1.00 27.76           O  
-ATOM  14881  CB  MET D 461     -15.459  -6.313-151.620  1.00 30.91           C  
-ATOM  14882  CG  MET D 461     -14.946  -4.972-151.108  1.00 42.66           C  
-ATOM  14883  SD  MET D 461     -14.058  -4.005-152.351  1.00 52.47           S  
-ATOM  14884  CE  MET D 461     -15.376  -3.634-153.508  1.00 39.84           C  
-ATOM  14885  N   LEU D 462     -13.843  -8.780-150.261  1.00 23.80           N  
-ATOM  14886  CA  LEU D 462     -13.038  -9.302-149.162  1.00 17.45           C  
-ATOM  14887  C   LEU D 462     -11.692  -9.804-149.661  1.00 19.93           C  
-ATOM  14888  O   LEU D 462     -10.666  -9.600-149.012  1.00 21.12           O  
-ATOM  14889  CB  LEU D 462     -13.773 -10.430-148.433  1.00 15.61           C  
-ATOM  14890  CG  LEU D 462     -14.748 -10.006-147.333  1.00 21.68           C  
-ATOM  14891  CD1 LEU D 462     -15.478 -11.205-146.765  1.00 27.32           C  
-ATOM  14892  CD2 LEU D 462     -14.022  -9.267-146.233  1.00 10.13           C  
-ATOM  14893  N   ARG D 463     -11.702 -10.453-150.820  1.00 21.57           N  
-ATOM  14894  CA  ARG D 463     -10.493 -11.062-151.360  1.00 19.79           C  
-ATOM  14895  C   ARG D 463      -9.583 -10.060-152.069  1.00 18.31           C  
-ATOM  14896  O   ARG D 463      -8.362 -10.214-152.053  1.00 20.44           O  
-ATOM  14897  CB  ARG D 463     -10.859 -12.205-152.312  1.00 16.54           C  
-ATOM  14898  CG  ARG D 463     -11.572 -13.360-151.623  1.00 18.66           C  
-ATOM  14899  CD  ARG D 463     -11.366 -14.686-152.342  1.00 15.73           C  
-ATOM  14900  NE  ARG D 463     -12.397 -14.958-153.339  1.00 15.55           N  
-ATOM  14901  CZ  ARG D 463     -12.952 -16.152-153.527  1.00 20.86           C  
-ATOM  14902  NH1 ARG D 463     -12.582 -17.184-152.783  1.00 12.76           N  
-ATOM  14903  NH2 ARG D 463     -13.880 -16.316-154.459  1.00 30.44           N  
-ATOM  14904  N   THR D 464     -10.166  -9.033-152.679  1.00 16.92           N  
-ATOM  14905  CA  THR D 464      -9.371  -8.075-153.443  1.00 15.48           C  
-ATOM  14906  C   THR D 464      -9.005  -6.825-152.646  1.00 18.71           C  
-ATOM  14907  O   THR D 464      -7.925  -6.269-152.822  1.00 32.34           O  
-ATOM  14908  CB  THR D 464     -10.100  -7.632-154.725  1.00 18.63           C  
-ATOM  14909  OG1 THR D 464     -11.257  -6.861-154.381  1.00 25.86           O  
-ATOM  14910  CG2 THR D 464     -10.519  -8.842-155.552  1.00 21.30           C  
-ATOM  14911  N   ASN D 465      -9.906  -6.389-151.772  1.00 21.71           N  
-ATOM  14912  CA  ASN D 465      -9.738  -5.119-151.072  1.00 26.72           C  
-ATOM  14913  C   ASN D 465     -10.473  -5.094-149.731  1.00 29.90           C  
-ATOM  14914  O   ASN D 465     -11.568  -4.543-149.627  1.00 32.94           O  
-ATOM  14915  CB  ASN D 465     -10.226  -3.976-151.964  1.00 26.49           C  
-ATOM  14916  CG  ASN D 465     -10.030  -2.617-151.333  1.00 34.17           C  
-ATOM  14917  OD1 ASN D 465      -9.119  -2.418-150.531  1.00 33.97           O  
-ATOM  14918  ND2 ASN D 465     -10.893  -1.672-151.688  1.00 36.80           N  
-ATOM  14919  N   PRO D 466      -9.863  -5.690-148.695  1.00 27.57           N  
-ATOM  14920  CA  PRO D 466     -10.528  -5.925-147.406  1.00 33.32           C  
-ATOM  14921  C   PRO D 466     -10.765  -4.671-146.563  1.00 38.11           C  
-ATOM  14922  O   PRO D 466     -11.495  -4.746-145.573  1.00 43.13           O  
-ATOM  14923  CB  PRO D 466      -9.558  -6.869-146.688  1.00 29.46           C  
-ATOM  14924  CG  PRO D 466      -8.229  -6.504-147.239  1.00 38.77           C  
-ATOM  14925  CD  PRO D 466      -8.469  -6.165-148.686  1.00 35.02           C  
-ATOM  14926  N   THR D 467     -10.166  -3.546-146.937  1.00 30.19           N  
-ATOM  14927  CA  THR D 467     -10.311  -2.324-146.149  1.00 41.97           C  
-ATOM  14928  C   THR D 467     -11.535  -1.515-146.566  1.00 37.83           C  
-ATOM  14929  O   THR D 467     -11.801  -0.446-146.013  1.00 36.90           O  
-ATOM  14930  CB  THR D 467      -9.066  -1.424-146.258  1.00 42.95           C  
-ATOM  14931  OG1 THR D 467      -8.821  -1.106-147.634  1.00 51.48           O  
-ATOM  14932  CG2 THR D 467      -7.852  -2.127-145.678  1.00 37.02           C  
-ATOM  14933  N   ASP D 468     -12.278  -2.027-147.541  1.00 29.30           N  
-ATOM  14934  CA  ASP D 468     -13.486  -1.359-148.010  1.00 32.53           C  
-ATOM  14935  C   ASP D 468     -14.588  -1.446-146.960  1.00 37.02           C  
-ATOM  14936  O   ASP D 468     -14.772  -2.484-146.327  1.00 49.46           O  
-ATOM  14937  CB  ASP D 468     -13.957  -1.968-149.329  1.00 32.66           C  
-ATOM  14938  CG  ASP D 468     -15.305  -1.437-149.766  1.00 33.07           C  
-ATOM  14939  OD1 ASP D 468     -15.356  -0.321-150.324  1.00 40.65           O  
-ATOM  14940  OD2 ASP D 468     -16.315  -2.140-149.554  1.00 31.44           O  
-ATOM  14941  N   ARG D 469     -15.319  -0.352-146.778  1.00 44.41           N  
-ATOM  14942  CA  ARG D 469     -16.349  -0.287-145.746  1.00 42.01           C  
-ATOM  14943  C   ARG D 469     -17.757  -0.404-146.322  1.00 36.79           C  
-ATOM  14944  O   ARG D 469     -18.725   0.037-145.704  1.00 33.86           O  
-ATOM  14945  CB  ARG D 469     -16.217   1.013-144.950  1.00 35.20           C  
-ATOM  14946  CG  ARG D 469     -14.909   1.137-144.184  1.00 36.54           C  
-ATOM  14947  CD  ARG D 469     -14.818   2.467-143.450  1.00 36.55           C  
-ATOM  14948  NE  ARG D 469     -14.722   3.595-144.373  1.00 49.69           N  
-ATOM  14949  CZ  ARG D 469     -13.721   4.470-144.384  1.00 42.31           C  
-ATOM  14950  NH1 ARG D 469     -12.727   4.354-143.513  1.00 28.95           N  
-ATOM  14951  NH2 ARG D 469     -13.714   5.464-145.262  1.00 38.32           N  
-ATOM  14952  N   ARG D 470     -17.864  -0.999-147.506  1.00 40.80           N  
-ATOM  14953  CA  ARG D 470     -19.159  -1.207-148.147  1.00 35.30           C  
-ATOM  14954  C   ARG D 470     -19.443  -2.693-148.339  1.00 28.44           C  
-ATOM  14955  O   ARG D 470     -20.143  -3.083-149.275  1.00 23.51           O  
-ATOM  14956  CB  ARG D 470     -19.223  -0.490-149.501  1.00 24.17           C  
-ATOM  14957  CG  ARG D 470     -19.209   1.030-149.436  1.00 23.22           C  
-ATOM  14958  CD  ARG D 470     -17.793   1.590-149.511  1.00 32.17           C  
-ATOM  14959  NE  ARG D 470     -17.786   3.032-149.749  1.00 43.31           N  
-ATOM  14960  CZ  ARG D 470     -17.516   3.602-150.921  1.00 47.07           C  
-ATOM  14961  NH1 ARG D 470     -17.214   2.855-151.975  1.00 46.15           N  
-ATOM  14962  NH2 ARG D 470     -17.539   4.923-151.037  1.00 41.28           N  
-ATOM  14963  N   MET D 471     -18.899  -3.516-147.449  1.00 23.56           N  
-ATOM  14964  CA  MET D 471     -19.044  -4.964-147.554  1.00 22.44           C  
-ATOM  14965  C   MET D 471     -20.277  -5.468-146.802  1.00 22.13           C  
-ATOM  14966  O   MET D 471     -20.163  -6.213-145.828  1.00 19.96           O  
-ATOM  14967  CB  MET D 471     -17.781  -5.654-147.036  1.00 21.25           C  
-ATOM  14968  CG  MET D 471     -16.504  -5.143-147.690  1.00 21.80           C  
-ATOM  14969  SD  MET D 471     -15.022  -6.066-147.236  1.00 20.79           S  
-ATOM  14970  CE  MET D 471     -14.857  -5.649-145.502  1.00 30.14           C  
-ATOM  14971  N   LEU D 472     -21.456  -5.063-147.268  1.00 30.76           N  
-ATOM  14972  CA  LEU D 472     -22.708  -5.415-146.604  1.00 26.06           C  
-ATOM  14973  C   LEU D 472     -23.601  -6.323-147.445  1.00 22.68           C  
-ATOM  14974  O   LEU D 472     -23.503  -6.363-148.670  1.00 25.60           O  
-ATOM  14975  CB  LEU D 472     -23.494  -4.155-146.232  1.00 27.38           C  
-ATOM  14976  CG  LEU D 472     -22.928  -3.240-145.146  1.00 29.75           C  
-ATOM  14977  CD1 LEU D 472     -21.932  -2.239-145.721  1.00 30.39           C  
-ATOM  14978  CD2 LEU D 472     -24.063  -2.531-144.427  1.00 34.81           C  
-ATOM  14979  N   MET D 473     -24.482  -7.040-146.760  1.00 26.87           N  
-ATOM  14980  CA  MET D 473     -25.473  -7.889-147.399  1.00 27.41           C  
-ATOM  14981  C   MET D 473     -26.813  -7.668-146.707  1.00 27.85           C  
-ATOM  14982  O   MET D 473     -26.959  -7.946-145.513  1.00 36.17           O  
-ATOM  14983  CB  MET D 473     -25.049  -9.359-147.334  1.00 22.24           C  
-ATOM  14984  CG  MET D 473     -25.883 -10.293-148.190  1.00 19.23           C  
-ATOM  14985  SD  MET D 473     -25.130 -11.926-148.343  1.00 35.78           S  
-ATOM  14986  CE  MET D 473     -25.208 -12.516-146.655  1.00 18.64           C  
-ATOM  14987  N   THR D 474     -27.782  -7.144-147.450  1.00 18.56           N  
-ATOM  14988  CA  THR D 474     -29.079  -6.813-146.871  1.00 20.39           C  
-ATOM  14989  C   THR D 474     -30.175  -7.741-147.376  1.00 25.74           C  
-ATOM  14990  O   THR D 474     -30.120  -8.232-148.504  1.00 33.06           O  
-ATOM  14991  CB  THR D 474     -29.480  -5.354-147.172  1.00 20.92           C  
-ATOM  14992  OG1 THR D 474     -30.741  -5.066-146.557  1.00 28.45           O  
-ATOM  14993  CG2 THR D 474     -29.595  -5.123-148.668  1.00 24.82           C  
-ATOM  14994  N   ALA D 475     -31.169  -7.984-146.528  1.00 25.92           N  
-ATOM  14995  CA  ALA D 475     -32.311  -8.810-146.898  1.00 25.62           C  
-ATOM  14996  C   ALA D 475     -33.591  -7.982-146.887  1.00 22.22           C  
-ATOM  14997  O   ALA D 475     -34.664  -8.475-147.233  1.00 23.37           O  
-ATOM  14998  CB  ALA D 475     -32.435 -10.000-145.956  1.00 24.15           C  
-ATOM  14999  N   TRP D 476     -33.468  -6.719-146.490  1.00 17.70           N  
-ATOM  15000  CA  TRP D 476     -34.624  -5.845-146.363  1.00 16.37           C  
-ATOM  15001  C   TRP D 476     -34.916  -5.104-147.663  1.00 21.37           C  
-ATOM  15002  O   TRP D 476     -34.289  -4.089-147.969  1.00 26.86           O  
-ATOM  15003  CB  TRP D 476     -34.419  -4.848-145.218  1.00 17.03           C  
-ATOM  15004  CG  TRP D 476     -35.692  -4.196-144.782  1.00 16.02           C  
-ATOM  15005  CD1 TRP D 476     -36.114  -2.937-145.085  1.00 19.20           C  
-ATOM  15006  CD2 TRP D 476     -36.724  -4.783-143.981  1.00 20.50           C  
-ATOM  15007  NE1 TRP D 476     -37.341  -2.698-144.516  1.00 21.41           N  
-ATOM  15008  CE2 TRP D 476     -37.738  -3.818-143.833  1.00 23.22           C  
-ATOM  15009  CE3 TRP D 476     -36.888  -6.031-143.372  1.00 16.58           C  
-ATOM  15010  CZ2 TRP D 476     -38.899  -4.060-143.101  1.00 23.32           C  
-ATOM  15011  CZ3 TRP D 476     -38.038  -6.270-142.647  1.00 14.99           C  
-ATOM  15012  CH2 TRP D 476     -39.029  -5.289-142.517  1.00 19.94           C  
-ATOM  15013  N   ASN D 477     -35.871  -5.626-148.425  1.00 21.34           N  
-ATOM  15014  CA  ASN D 477     -36.316  -4.987-149.655  1.00 23.69           C  
-ATOM  15015  C   ASN D 477     -37.777  -4.564-149.541  1.00 31.20           C  
-ATOM  15016  O   ASN D 477     -38.678  -5.385-149.714  1.00 38.57           O  
-ATOM  15017  CB  ASN D 477     -36.127  -5.929-150.848  1.00 25.76           C  
-ATOM  15018  CG  ASN D 477     -36.408  -5.258-152.186  1.00 30.12           C  
-ATOM  15019  OD1 ASN D 477     -36.997  -4.180-152.248  1.00 31.12           O  
-ATOM  15020  ND2 ASN D 477     -35.990  -5.906-153.269  1.00 35.36           N  
-ATOM  15021  N   PRO D 478     -38.012  -3.277-149.247  1.00 31.79           N  
-ATOM  15022  CA  PRO D 478     -39.349  -2.680-149.143  1.00 29.10           C  
-ATOM  15023  C   PRO D 478     -40.255  -2.991-150.336  1.00 34.13           C  
-ATOM  15024  O   PRO D 478     -41.472  -3.077-150.170  1.00 39.39           O  
-ATOM  15025  CB  PRO D 478     -39.049  -1.181-149.069  1.00 27.40           C  
-ATOM  15026  CG  PRO D 478     -37.721  -1.114-148.407  1.00 30.73           C  
-ATOM  15027  CD  PRO D 478     -36.953  -2.316-148.890  1.00 28.64           C  
-ATOM  15028  N   ALA D 479     -39.665  -3.169-151.515  1.00 30.73           N  
-ATOM  15029  CA  ALA D 479     -40.432  -3.398-152.737  1.00 27.69           C  
-ATOM  15030  C   ALA D 479     -40.815  -4.864-152.928  1.00 35.77           C  
-ATOM  15031  O   ALA D 479     -41.340  -5.239-153.977  1.00 37.29           O  
-ATOM  15032  CB  ALA D 479     -39.647  -2.908-153.944  1.00 25.36           C  
-ATOM  15033  N   ALA D 480     -40.557  -5.690-151.919  1.00 37.43           N  
-ATOM  15034  CA  ALA D 480     -40.825  -7.120-152.032  1.00 38.27           C  
-ATOM  15035  C   ALA D 480     -41.373  -7.711-150.734  1.00 31.89           C  
-ATOM  15036  O   ALA D 480     -41.762  -8.879-150.697  1.00 25.39           O  
-ATOM  15037  CB  ALA D 480     -39.557  -7.855-152.456  1.00 34.54           C  
-ATOM  15038  N   LEU D 481     -41.409  -6.898-149.682  1.00 29.79           N  
-ATOM  15039  CA  LEU D 481     -41.852  -7.349-148.365  1.00 25.53           C  
-ATOM  15040  C   LEU D 481     -43.213  -8.032-148.424  1.00 29.09           C  
-ATOM  15041  O   LEU D 481     -43.373  -9.165-147.965  1.00 29.90           O  
-ATOM  15042  CB  LEU D 481     -41.904  -6.173-147.388  1.00 26.43           C  
-ATOM  15043  CG  LEU D 481     -40.590  -5.514-146.961  1.00 29.11           C  
-ATOM  15044  CD1 LEU D 481     -40.884  -4.312-146.082  1.00 45.93           C  
-ATOM  15045  CD2 LEU D 481     -39.696  -6.496-146.229  1.00 17.93           C  
-ATOM  15046  N   ASP D 482     -44.181  -7.342-149.017  1.00 29.01           N  
-ATOM  15047  CA  ASP D 482     -45.546  -7.842-149.127  1.00 30.84           C  
-ATOM  15048  C   ASP D 482     -45.631  -9.176-149.870  1.00 31.96           C  
-ATOM  15049  O   ASP D 482     -46.608  -9.909-149.723  1.00 31.31           O  
-ATOM  15050  CB  ASP D 482     -46.428  -6.803-149.827  1.00 44.62           C  
-ATOM  15051  CG  ASP D 482     -46.682  -5.574-148.968  1.00 41.48           C  
-ATOM  15052  OD1 ASP D 482     -45.942  -5.369-147.981  1.00 32.13           O  
-ATOM  15053  OD2 ASP D 482     -47.622  -4.810-149.286  1.00 24.30           O  
-ATOM  15054  N   GLU D 483     -44.610  -9.487-150.663  1.00 32.48           N  
-ATOM  15055  CA  GLU D 483     -44.612 -10.708-151.463  1.00 27.10           C  
-ATOM  15056  C   GLU D 483     -44.029 -11.888-150.703  1.00 30.29           C  
-ATOM  15057  O   GLU D 483     -44.074 -13.019-151.176  1.00 30.79           O  
-ATOM  15058  CB  GLU D 483     -43.830 -10.497-152.756  1.00 23.30           C  
-ATOM  15059  CG  GLU D 483     -44.282  -9.294-153.549  1.00 31.51           C  
-ATOM  15060  CD  GLU D 483     -43.350  -8.982-154.694  1.00 33.11           C  
-ATOM  15061  OE1 GLU D 483     -43.368  -7.831-155.178  1.00 34.30           O  
-ATOM  15062  OE2 GLU D 483     -42.600  -9.889-155.109  1.00 33.93           O  
-ATOM  15063  N   MET D 484     -43.476 -11.624-149.526  1.00 34.81           N  
-ATOM  15064  CA  MET D 484     -42.812 -12.676-148.767  1.00 34.26           C  
-ATOM  15065  C   MET D 484     -43.682 -13.186-147.630  1.00 31.39           C  
-ATOM  15066  O   MET D 484     -44.484 -12.440-147.067  1.00 39.13           O  
-ATOM  15067  CB  MET D 484     -41.476 -12.173-148.221  1.00 33.90           C  
-ATOM  15068  CG  MET D 484     -40.590 -11.526-149.267  1.00 33.78           C  
-ATOM  15069  SD  MET D 484     -39.154 -10.734-148.522  1.00 34.29           S  
-ATOM  15070  CE  MET D 484     -39.918 -10.009-147.081  1.00 36.71           C  
-ATOM  15071  N   ALA D 485     -43.516 -14.463-147.302  1.00 29.33           N  
-ATOM  15072  CA  ALA D 485     -44.282 -15.094-146.236  1.00 31.71           C  
-ATOM  15073  C   ALA D 485     -44.014 -14.409-144.903  1.00 37.89           C  
-ATOM  15074  O   ALA D 485     -44.935 -14.128-144.136  1.00 42.06           O  
-ATOM  15075  CB  ALA D 485     -43.948 -16.573-146.152  1.00 31.41           C  
-ATOM  15076  N   LEU D 486     -42.741 -14.144-144.639  1.00 37.77           N  
-ATOM  15077  CA  LEU D 486     -42.332 -13.435-143.436  1.00 38.55           C  
-ATOM  15078  C   LEU D 486     -41.221 -12.440-143.743  1.00 39.08           C  
-ATOM  15079  O   LEU D 486     -40.197 -12.808-144.318  1.00 39.08           O  
-ATOM  15080  CB  LEU D 486     -41.865 -14.416-142.357  1.00 40.97           C  
-ATOM  15081  CG  LEU D 486     -42.874 -14.787-141.270  1.00 40.64           C  
-ATOM  15082  CD1 LEU D 486     -42.200 -15.592-140.169  1.00 48.91           C  
-ATOM  15083  CD2 LEU D 486     -43.528 -13.539-140.701  1.00 33.16           C  
-ATOM  15084  N   PRO D 487     -41.430 -11.168-143.370  1.00 35.23           N  
-ATOM  15085  CA  PRO D 487     -40.378 -10.150-143.449  1.00 32.57           C  
-ATOM  15086  C   PRO D 487     -39.144 -10.584-142.668  1.00 27.33           C  
-ATOM  15087  O   PRO D 487     -39.281 -11.081-141.552  1.00 30.53           O  
-ATOM  15088  CB  PRO D 487     -41.033  -8.922-142.816  1.00 28.34           C  
-ATOM  15089  CG  PRO D 487     -42.485  -9.118-143.052  1.00 28.17           C  
-ATOM  15090  CD  PRO D 487     -42.716 -10.596-142.940  1.00 33.27           C  
-ATOM  15091  N   PRO D 488     -37.951 -10.395-143.246  1.00 19.63           N  
-ATOM  15092  CA  PRO D 488     -36.720 -10.946-142.669  1.00 27.37           C  
-ATOM  15093  C   PRO D 488     -36.389 -10.388-141.287  1.00 29.74           C  
-ATOM  15094  O   PRO D 488     -36.421  -9.174-141.078  1.00 30.50           O  
-ATOM  15095  CB  PRO D 488     -35.650 -10.543-143.688  1.00 25.65           C  
-ATOM  15096  CG  PRO D 488     -36.194  -9.335-144.340  1.00 24.73           C  
-ATOM  15097  CD  PRO D 488     -37.676  -9.547-144.417  1.00 19.60           C  
-ATOM  15098  N   CYS D 489     -36.082 -11.280-140.351  1.00 25.66           N  
-ATOM  15099  CA  CYS D 489     -35.676 -10.869-139.016  1.00 25.80           C  
-ATOM  15100  C   CYS D 489     -34.211 -10.449-139.047  1.00 30.59           C  
-ATOM  15101  O   CYS D 489     -33.886  -9.288-138.798  1.00 27.55           O  
-ATOM  15102  CB  CYS D 489     -35.911 -11.993-138.006  1.00 26.52           C  
-ATOM  15103  SG  CYS D 489     -37.661 -12.358-137.702  1.00 54.72           S  
-ATOM  15104  N   HIS D 490     -33.330 -11.391-139.363  1.00 33.67           N  
-ATOM  15105  CA  HIS D 490     -31.937 -11.056-139.622  1.00 29.54           C  
-ATOM  15106  C   HIS D 490     -31.837 -10.468-141.027  1.00 32.91           C  
-ATOM  15107  O   HIS D 490     -31.769 -11.199-142.017  1.00 38.19           O  
-ATOM  15108  CB  HIS D 490     -31.034 -12.285-139.459  1.00 30.90           C  
-ATOM  15109  CG  HIS D 490     -31.583 -13.536-140.073  1.00 32.22           C  
-ATOM  15110  ND1 HIS D 490     -31.088 -14.071-141.242  1.00 36.55           N  
-ATOM  15111  CD2 HIS D 490     -32.576 -14.366-139.671  1.00 33.56           C  
-ATOM  15112  CE1 HIS D 490     -31.753 -15.175-141.537  1.00 36.16           C  
-ATOM  15113  NE2 HIS D 490     -32.665 -15.372-140.601  1.00 39.76           N  
-ATOM  15114  N   LEU D 491     -31.842  -9.140-141.106  1.00 26.04           N  
-ATOM  15115  CA  LEU D 491     -32.010  -8.456-142.384  1.00 27.90           C  
-ATOM  15116  C   LEU D 491     -30.734  -7.828-142.941  1.00 26.41           C  
-ATOM  15117  O   LEU D 491     -30.723  -7.363-144.081  1.00 22.91           O  
-ATOM  15118  CB  LEU D 491     -33.091  -7.378-142.253  1.00 26.69           C  
-ATOM  15119  CG  LEU D 491     -33.038  -6.438-141.045  1.00 22.76           C  
-ATOM  15120  CD1 LEU D 491     -32.023  -5.319-141.232  1.00 27.97           C  
-ATOM  15121  CD2 LEU D 491     -34.417  -5.866-140.778  1.00 19.69           C  
-ATOM  15122  N   LEU D 492     -29.667  -7.803-142.149  1.00 28.94           N  
-ATOM  15123  CA  LEU D 492     -28.429  -7.183-142.605  1.00 22.64           C  
-ATOM  15124  C   LEU D 492     -27.190  -7.770-141.937  1.00 24.98           C  
-ATOM  15125  O   LEU D 492     -27.206  -8.104-140.752  1.00 21.31           O  
-ATOM  15126  CB  LEU D 492     -28.480  -5.674-142.364  1.00 19.39           C  
-ATOM  15127  CG  LEU D 492     -27.351  -4.855-142.991  1.00 23.63           C  
-ATOM  15128  CD1 LEU D 492     -27.919  -3.612-143.642  1.00 24.92           C  
-ATOM  15129  CD2 LEU D 492     -26.301  -4.482-141.952  1.00 30.43           C  
-ATOM  15130  N   CYS D 493     -26.114  -7.899-142.706  1.00 25.82           N  
-ATOM  15131  CA  CYS D 493     -24.836  -8.302-142.133  1.00 24.32           C  
-ATOM  15132  C   CYS D 493     -23.681  -7.563-142.794  1.00 26.65           C  
-ATOM  15133  O   CYS D 493     -23.717  -7.286-143.990  1.00 25.49           O  
-ATOM  15134  CB  CYS D 493     -24.636  -9.814-142.253  1.00 27.88           C  
-ATOM  15135  SG  CYS D 493     -24.458 -10.421-143.938  1.00 29.93           S  
-ATOM  15136  N   GLN D 494     -22.662  -7.239-142.004  1.00 26.75           N  
-ATOM  15137  CA  GLN D 494     -21.495  -6.519-142.507  1.00 28.38           C  
-ATOM  15138  C   GLN D 494     -20.211  -7.186-142.029  1.00 26.38           C  
-ATOM  15139  O   GLN D 494     -20.131  -7.648-140.894  1.00 19.34           O  
-ATOM  15140  CB  GLN D 494     -21.529  -5.054-142.063  1.00 28.22           C  
-ATOM  15141  CG  GLN D 494     -20.361  -4.228-142.572  1.00 23.74           C  
-ATOM  15142  CD  GLN D 494     -20.364  -2.817-142.027  1.00 29.01           C  
-ATOM  15143  OE1 GLN D 494     -21.255  -2.434-141.270  1.00 26.93           O  
-ATOM  15144  NE2 GLN D 494     -19.365  -2.034-142.410  1.00 36.46           N  
-ATOM  15145  N   PHE D 495     -19.206  -7.235-142.898  1.00 28.98           N  
-ATOM  15146  CA  PHE D 495     -17.957  -7.914-142.572  1.00 28.34           C  
-ATOM  15147  C   PHE D 495     -16.801  -6.932-142.413  1.00 24.71           C  
-ATOM  15148  O   PHE D 495     -16.838  -5.820-142.943  1.00 18.16           O  
-ATOM  15149  CB  PHE D 495     -17.637  -8.961-143.638  1.00 22.80           C  
-ATOM  15150  CG  PHE D 495     -18.643 -10.075-143.701  1.00 29.21           C  
-ATOM  15151  CD1 PHE D 495     -18.470 -11.223-142.947  1.00 27.55           C  
-ATOM  15152  CD2 PHE D 495     -19.770  -9.966-144.502  1.00 25.16           C  
-ATOM  15153  CE1 PHE D 495     -19.396 -12.247-142.996  1.00 29.65           C  
-ATOM  15154  CE2 PHE D 495     -20.700 -10.986-144.555  1.00 17.11           C  
-ATOM  15155  CZ  PHE D 495     -20.513 -12.127-143.801  1.00 26.32           C  
-ATOM  15156  N   TYR D 496     -15.776  -7.355-141.678  1.00 26.07           N  
-ATOM  15157  CA  TYR D 496     -14.674  -6.473-141.314  1.00 23.08           C  
-ATOM  15158  C   TYR D 496     -13.367  -7.241-141.166  1.00 26.83           C  
-ATOM  15159  O   TYR D 496     -13.306  -8.246-140.461  1.00 36.29           O  
-ATOM  15160  CB  TYR D 496     -15.010  -5.742-140.013  1.00 22.74           C  
-ATOM  15161  CG  TYR D 496     -13.890  -4.919-139.408  1.00 29.41           C  
-ATOM  15162  CD1 TYR D 496     -13.724  -3.583-139.744  1.00 27.52           C  
-ATOM  15163  CD2 TYR D 496     -13.019  -5.473-138.476  1.00 30.79           C  
-ATOM  15164  CE1 TYR D 496     -12.711  -2.826-139.186  1.00 24.52           C  
-ATOM  15165  CE2 TYR D 496     -12.005  -4.726-137.914  1.00 24.12           C  
-ATOM  15166  CZ  TYR D 496     -11.856  -3.404-138.271  1.00 22.89           C  
-ATOM  15167  OH  TYR D 496     -10.847  -2.661-137.708  1.00 27.18           O  
-ATOM  15168  N   VAL D 497     -12.320  -6.763-141.827  1.00 24.26           N  
-ATOM  15169  CA  VAL D 497     -11.010  -7.387-141.703  1.00 25.62           C  
-ATOM  15170  C   VAL D 497     -10.030  -6.418-141.062  1.00 21.81           C  
-ATOM  15171  O   VAL D 497     -10.045  -5.225-141.361  1.00 29.51           O  
-ATOM  15172  CB  VAL D 497     -10.451  -7.839-143.069  1.00 21.14           C  
-ATOM  15173  CG1 VAL D 497      -9.307  -8.820-142.876  1.00 19.74           C  
-ATOM  15174  CG2 VAL D 497     -11.538  -8.469-143.901  1.00 19.93           C  
-ATOM  15175  N   ASN D 498      -9.187  -6.930-140.174  1.00 21.35           N  
-ATOM  15176  CA  ASN D 498      -8.126  -6.118-139.595  1.00 25.10           C  
-ATOM  15177  C   ASN D 498      -6.790  -6.424-140.269  1.00 31.70           C  
-ATOM  15178  O   ASN D 498      -6.754  -7.005-141.355  1.00 31.58           O  
-ATOM  15179  CB  ASN D 498      -8.037  -6.339-138.083  1.00 25.00           C  
-ATOM  15180  CG  ASN D 498      -7.743  -7.779-137.718  1.00 21.81           C  
-ATOM  15181  OD1 ASN D 498      -7.787  -8.667-138.567  1.00 22.96           O  
-ATOM  15182  ND2 ASN D 498      -7.450  -8.019-136.445  1.00 19.27           N  
-ATOM  15183  N   ASP D 499      -5.696  -6.037-139.626  1.00 33.04           N  
-ATOM  15184  CA  ASP D 499      -4.374  -6.211-140.213  1.00 30.53           C  
-ATOM  15185  C   ASP D 499      -3.795  -7.600-139.945  1.00 30.23           C  
-ATOM  15186  O   ASP D 499      -2.714  -7.933-140.430  1.00 28.79           O  
-ATOM  15187  CB  ASP D 499      -3.423  -5.133-139.693  1.00 39.21           C  
-ATOM  15188  CG  ASP D 499      -3.462  -5.001-138.183  1.00 49.26           C  
-ATOM  15189  OD1 ASP D 499      -4.467  -5.418-137.569  1.00 31.48           O  
-ATOM  15190  OD2 ASP D 499      -2.486  -4.472-137.610  1.00 64.97           O  
-ATOM  15191  N   GLN D 500      -4.518  -8.409-139.178  1.00 27.79           N  
-ATOM  15192  CA  GLN D 500      -4.083  -9.770-138.885  1.00 28.20           C  
-ATOM  15193  C   GLN D 500      -4.872 -10.781-139.712  1.00 28.64           C  
-ATOM  15194  O   GLN D 500      -4.912 -11.968-139.379  1.00 29.79           O  
-ATOM  15195  CB  GLN D 500      -4.239 -10.079-137.396  1.00 32.86           C  
-ATOM  15196  CG  GLN D 500      -3.641  -9.030-136.473  1.00 36.88           C  
-ATOM  15197  CD  GLN D 500      -2.152  -8.845-136.683  1.00 49.26           C  
-ATOM  15198  OE1 GLN D 500      -1.673  -7.723-136.846  1.00 61.74           O  
-ATOM  15199  NE2 GLN D 500      -1.410  -9.947-136.672  1.00 46.55           N  
-ATOM  15200  N   LYS D 501      -5.494 -10.297-140.786  1.00 25.52           N  
-ATOM  15201  CA  LYS D 501      -6.332 -11.118-141.660  1.00 24.27           C  
-ATOM  15202  C   LYS D 501      -7.465 -11.802-140.897  1.00 26.95           C  
-ATOM  15203  O   LYS D 501      -7.893 -12.897-141.264  1.00 28.75           O  
-ATOM  15204  CB  LYS D 501      -5.487 -12.171-142.382  1.00 20.83           C  
-ATOM  15205  CG  LYS D 501      -4.418 -11.607-143.299  1.00 19.36           C  
-ATOM  15206  CD  LYS D 501      -4.805 -11.778-144.759  1.00 25.03           C  
-ATOM  15207  CE  LYS D 501      -3.667 -11.377-145.678  1.00 31.11           C  
-ATOM  15208  NZ  LYS D 501      -2.442 -12.178-145.409  1.00 30.73           N  
-ATOM  15209  N   GLU D 502      -7.946 -11.156-139.838  1.00 25.35           N  
-ATOM  15210  CA  GLU D 502      -9.021 -11.717-139.023  1.00 27.83           C  
-ATOM  15211  C   GLU D 502     -10.382 -11.156-139.429  1.00 29.29           C  
-ATOM  15212  O   GLU D 502     -10.587  -9.942-139.438  1.00 29.70           O  
-ATOM  15213  CB  GLU D 502      -8.770 -11.449-137.539  1.00 21.12           C  
-ATOM  15214  CG  GLU D 502      -7.575 -12.181-136.958  1.00 27.99           C  
-ATOM  15215  CD  GLU D 502      -7.312 -11.798-135.513  1.00 43.76           C  
-ATOM  15216  OE1 GLU D 502      -7.392 -10.593-135.192  1.00 42.56           O  
-ATOM  15217  OE2 GLU D 502      -7.031 -12.702-134.697  1.00 44.62           O  
-ATOM  15218  N   LEU D 503     -11.310 -12.050-139.757  1.00 26.99           N  
-ATOM  15219  CA  LEU D 503     -12.640 -11.649-140.196  1.00 24.33           C  
-ATOM  15220  C   LEU D 503     -13.617 -11.547-139.028  1.00 29.64           C  
-ATOM  15221  O   LEU D 503     -13.623 -12.392-138.132  1.00 25.09           O  
-ATOM  15222  CB  LEU D 503     -13.178 -12.635-141.234  1.00 25.39           C  
-ATOM  15223  CG  LEU D 503     -14.579 -12.351-141.781  1.00 20.69           C  
-ATOM  15224  CD1 LEU D 503     -14.566 -11.113-142.661  1.00 22.80           C  
-ATOM  15225  CD2 LEU D 503     -15.126 -13.552-142.539  1.00 17.60           C  
-ATOM  15226  N   SER D 504     -14.437 -10.500-139.050  1.00 30.53           N  
-ATOM  15227  CA  SER D 504     -15.501 -10.312-138.071  1.00 22.91           C  
-ATOM  15228  C   SER D 504     -16.804  -9.995-138.794  1.00 28.08           C  
-ATOM  15229  O   SER D 504     -16.789  -9.419-139.884  1.00 24.08           O  
-ATOM  15230  CB  SER D 504     -15.151  -9.192-137.087  1.00 24.53           C  
-ATOM  15231  OG  SER D 504     -14.004  -9.513-136.318  1.00 36.10           O  
-ATOM  15232  N   CYS D 505     -17.928 -10.370-138.189  1.00 31.57           N  
-ATOM  15233  CA  CYS D 505     -19.229 -10.151-138.813  1.00 24.61           C  
-ATOM  15234  C   CYS D 505     -20.264  -9.586-137.845  1.00 21.33           C  
-ATOM  15235  O   CYS D 505     -20.479 -10.128-136.762  1.00 23.87           O  
-ATOM  15236  CB  CYS D 505     -19.759 -11.452-139.418  1.00 24.26           C  
-ATOM  15237  SG  CYS D 505     -21.477 -11.341-139.988  1.00 46.10           S  
-ATOM  15238  N   ILE D 506     -20.893  -8.489-138.255  1.00 26.57           N  
-ATOM  15239  CA  ILE D 506     -22.027  -7.900-137.549  1.00 21.66           C  
-ATOM  15240  C   ILE D 506     -23.324  -8.341-138.209  1.00 20.69           C  
-ATOM  15241  O   ILE D 506     -23.421  -8.357-139.432  1.00 26.47           O  
-ATOM  15242  CB  ILE D 506     -21.965  -6.352-137.546  1.00 23.21           C  
-ATOM  15243  CG1 ILE D 506     -20.932  -5.851-136.543  1.00 20.85           C  
-ATOM  15244  CG2 ILE D 506     -23.320  -5.746-137.206  1.00 20.16           C  
-ATOM  15245  CD1 ILE D 506     -20.791  -4.350-136.532  1.00 20.38           C  
-ATOM  15246  N   MET D 507     -24.316  -8.707-137.407  1.00 17.54           N  
-ATOM  15247  CA  MET D 507     -25.634  -9.008-137.944  1.00 16.36           C  
-ATOM  15248  C   MET D 507     -26.699  -8.217-137.201  1.00 19.18           C  
-ATOM  15249  O   MET D 507     -26.789  -8.280-135.976  1.00 26.61           O  
-ATOM  15250  CB  MET D 507     -25.928 -10.506-137.860  1.00 18.49           C  
-ATOM  15251  CG  MET D 507     -27.240 -10.909-138.514  1.00 20.19           C  
-ATOM  15252  SD  MET D 507     -28.641 -10.899-137.381  1.00 28.47           S  
-ATOM  15253  CE  MET D 507     -28.412 -12.460-136.536  1.00 23.84           C  
-ATOM  15254  N   TYR D 508     -27.500  -7.461-137.943  1.00 22.58           N  
-ATOM  15255  CA  TYR D 508     -28.602  -6.724-137.340  1.00 19.74           C  
-ATOM  15256  C   TYR D 508     -29.901  -7.506-137.472  1.00 19.67           C  
-ATOM  15257  O   TYR D 508     -30.249  -7.979-138.553  1.00 24.98           O  
-ATOM  15258  CB  TYR D 508     -28.753  -5.340-137.972  1.00 19.24           C  
-ATOM  15259  CG  TYR D 508     -29.847  -4.514-137.334  1.00 22.26           C  
-ATOM  15260  CD1 TYR D 508     -29.616  -3.810-136.159  1.00 21.93           C  
-ATOM  15261  CD2 TYR D 508     -31.115  -4.448-137.898  1.00 23.57           C  
-ATOM  15262  CE1 TYR D 508     -30.616  -3.058-135.568  1.00 23.86           C  
-ATOM  15263  CE2 TYR D 508     -32.120  -3.700-137.313  1.00 20.73           C  
-ATOM  15264  CZ  TYR D 508     -31.865  -3.007-136.150  1.00 20.16           C  
-ATOM  15265  OH  TYR D 508     -32.862  -2.262-135.563  1.00 26.69           O  
-ATOM  15266  N   GLN D 509     -30.614  -7.636-136.361  1.00 18.73           N  
-ATOM  15267  CA  GLN D 509     -31.861  -8.386-136.337  1.00 23.52           C  
-ATOM  15268  C   GLN D 509     -32.999  -7.521-135.800  1.00 23.01           C  
-ATOM  15269  O   GLN D 509     -32.949  -7.050-134.663  1.00 24.82           O  
-ATOM  15270  CB  GLN D 509     -31.696  -9.651-135.494  1.00 20.73           C  
-ATOM  15271  CG  GLN D 509     -32.826 -10.651-135.631  1.00 23.88           C  
-ATOM  15272  CD  GLN D 509     -32.522 -11.955-134.924  1.00 26.93           C  
-ATOM  15273  OE1 GLN D 509     -31.413 -12.161-134.435  1.00 21.19           O  
-ATOM  15274  NE2 GLN D 509     -33.505 -12.844-134.866  1.00 33.82           N  
-ATOM  15275  N   ARG D 510     -34.020  -7.307-136.626  1.00 18.91           N  
-ATOM  15276  CA  ARG D 510     -35.127  -6.427-136.267  1.00 21.56           C  
-ATOM  15277  C   ARG D 510     -36.012  -7.022-135.178  1.00 22.87           C  
-ATOM  15278  O   ARG D 510     -36.593  -6.294-134.373  1.00 23.48           O  
-ATOM  15279  CB  ARG D 510     -35.982  -6.110-137.497  1.00 21.84           C  
-ATOM  15280  CG  ARG D 510     -36.651  -7.323-138.119  1.00 20.22           C  
-ATOM  15281  CD  ARG D 510     -37.775  -6.917-139.053  1.00 22.93           C  
-ATOM  15282  NE  ARG D 510     -38.447  -8.074-139.637  1.00 22.92           N  
-ATOM  15283  CZ  ARG D 510     -39.444  -8.731-139.053  1.00 27.07           C  
-ATOM  15284  NH1 ARG D 510     -39.998  -9.770-139.661  1.00 31.65           N  
-ATOM  15285  NH2 ARG D 510     -39.889  -8.351-137.862  1.00 25.89           N  
-ATOM  15286  N   SER D 511     -36.114  -8.345-135.160  1.00 24.51           N  
-ATOM  15287  CA  SER D 511     -37.022  -9.028-134.252  1.00 23.81           C  
-ATOM  15288  C   SER D 511     -36.378 -10.299-133.722  1.00 27.32           C  
-ATOM  15289  O   SER D 511     -35.880 -11.118-134.495  1.00 28.38           O  
-ATOM  15290  CB  SER D 511     -38.338  -9.347-134.960  1.00 30.20           C  
-ATOM  15291  OG  SER D 511     -39.282  -9.893-134.058  1.00 36.49           O  
-ATOM  15292  N   CYS D 512     -36.390 -10.466-132.404  1.00 27.52           N  
-ATOM  15293  CA  CYS D 512     -35.678 -11.576-131.786  1.00 26.09           C  
-ATOM  15294  C   CYS D 512     -36.531 -12.386-130.818  1.00 35.41           C  
-ATOM  15295  O   CYS D 512     -36.925 -11.890-129.762  1.00 40.07           O  
-ATOM  15296  CB  CYS D 512     -34.443 -11.058-131.051  1.00 26.54           C  
-ATOM  15297  SG  CYS D 512     -33.454  -9.890-132.001  1.00 35.11           S  
-ATOM  15298  N   ASP D 513     -36.806 -13.635-131.179  1.00 41.38           N  
-ATOM  15299  CA  ASP D 513     -37.384 -14.586-130.239  1.00 31.00           C  
-ATOM  15300  C   ASP D 513     -36.254 -15.149-129.387  1.00 29.65           C  
-ATOM  15301  O   ASP D 513     -35.600 -16.120-129.768  1.00 31.32           O  
-ATOM  15302  CB  ASP D 513     -38.130 -15.707-130.965  1.00 33.86           C  
-ATOM  15303  CG  ASP D 513     -38.969 -16.560-130.026  1.00 38.08           C  
-ATOM  15304  OD1 ASP D 513     -38.720 -16.543-128.802  1.00 38.51           O  
-ATOM  15305  OD2 ASP D 513     -39.883 -17.255-130.516  1.00 46.54           O  
-ATOM  15306  N   VAL D 514     -36.033 -14.523-128.237  1.00 23.30           N  
-ATOM  15307  CA  VAL D 514     -34.924 -14.869-127.357  1.00 25.54           C  
-ATOM  15308  C   VAL D 514     -34.956 -16.331-126.935  1.00 28.60           C  
-ATOM  15309  O   VAL D 514     -33.925 -17.003-126.916  1.00 30.98           O  
-ATOM  15310  CB  VAL D 514     -34.924 -13.979-126.106  1.00 23.58           C  
-ATOM  15311  CG1 VAL D 514     -33.848 -14.422-125.127  1.00 23.13           C  
-ATOM  15312  CG2 VAL D 514     -34.724 -12.535-126.509  1.00 21.33           C  
-ATOM  15313  N   GLY D 515     -36.146 -16.823-126.614  1.00 33.14           N  
-ATOM  15314  CA  GLY D 515     -36.300 -18.193-126.168  1.00 28.79           C  
-ATOM  15315  C   GLY D 515     -35.976 -19.217-127.238  1.00 38.55           C  
-ATOM  15316  O   GLY D 515     -35.322 -20.223-126.965  1.00 52.37           O  
-ATOM  15317  N   LEU D 516     -36.416 -18.957-128.464  1.00 36.25           N  
-ATOM  15318  CA  LEU D 516     -36.378 -19.978-129.503  1.00 36.54           C  
-ATOM  15319  C   LEU D 516     -35.377 -19.689-130.620  1.00 34.73           C  
-ATOM  15320  O   LEU D 516     -34.549 -20.538-130.946  1.00 46.07           O  
-ATOM  15321  CB  LEU D 516     -37.778 -20.154-130.097  1.00 49.40           C  
-ATOM  15322  CG  LEU D 516     -38.104 -21.502-130.738  1.00 56.44           C  
-ATOM  15323  CD1 LEU D 516     -37.853 -22.640-129.762  1.00 56.64           C  
-ATOM  15324  CD2 LEU D 516     -39.547 -21.519-131.217  1.00 54.25           C  
-ATOM  15325  N   GLY D 517     -35.451 -18.494-131.197  1.00 31.93           N  
-ATOM  15326  CA  GLY D 517     -34.711 -18.185-132.409  1.00 39.09           C  
-ATOM  15327  C   GLY D 517     -33.292 -17.660-132.260  1.00 38.19           C  
-ATOM  15328  O   GLY D 517     -32.453 -17.899-133.129  1.00 34.88           O  
-ATOM  15329  N   VAL D 518     -33.021 -16.945-131.172  1.00 30.92           N  
-ATOM  15330  CA  VAL D 518     -31.734 -16.272-130.991  1.00 23.28           C  
-ATOM  15331  C   VAL D 518     -30.514 -17.202-131.000  1.00 24.90           C  
-ATOM  15332  O   VAL D 518     -29.551 -16.917-131.714  1.00 32.27           O  
-ATOM  15333  CB  VAL D 518     -31.727 -15.433-129.686  1.00 22.20           C  
-ATOM  15334  CG1 VAL D 518     -30.303 -15.102-129.258  1.00 19.73           C  
-ATOM  15335  CG2 VAL D 518     -32.536 -14.172-129.884  1.00 29.44           C  
-ATOM  15336  N   PRO D 519     -30.537 -18.308-130.223  1.00 23.74           N  
-ATOM  15337  CA  PRO D 519     -29.365 -19.192-130.291  1.00 26.98           C  
-ATOM  15338  C   PRO D 519     -29.123 -19.697-131.709  1.00 28.31           C  
-ATOM  15339  O   PRO D 519     -27.987 -19.717-132.206  1.00 28.65           O  
-ATOM  15340  CB  PRO D 519     -29.745 -20.350-129.358  1.00 26.42           C  
-ATOM  15341  CG  PRO D 519     -30.749 -19.777-128.436  1.00 18.84           C  
-ATOM  15342  CD  PRO D 519     -31.537 -18.819-129.267  1.00 20.58           C  
-ATOM  15343  N   PHE D 520     -30.221 -20.096-132.341  1.00 28.62           N  
-ATOM  15344  CA  PHE D 520     -30.229 -20.528-133.725  1.00 27.32           C  
-ATOM  15345  C   PHE D 520     -29.533 -19.503-134.613  1.00 28.59           C  
-ATOM  15346  O   PHE D 520     -28.675 -19.855-135.420  1.00 27.96           O  
-ATOM  15347  CB  PHE D 520     -31.663 -20.757-134.197  1.00 25.02           C  
-ATOM  15348  CG  PHE D 520     -31.769 -21.598-135.434  1.00 25.61           C  
-ATOM  15349  CD1 PHE D 520     -31.739 -21.019-136.691  1.00 21.12           C  
-ATOM  15350  CD2 PHE D 520     -31.919 -22.971-135.338  1.00 27.80           C  
-ATOM  15351  CE1 PHE D 520     -31.848 -21.798-137.824  1.00 23.85           C  
-ATOM  15352  CE2 PHE D 520     -32.032 -23.751-136.464  1.00 19.15           C  
-ATOM  15353  CZ  PHE D 520     -31.997 -23.166-137.708  1.00 22.01           C  
-ATOM  15354  N   ASN D 521     -29.892 -18.233-134.449  1.00 25.17           N  
-ATOM  15355  CA  ASN D 521     -29.318 -17.170-135.267  1.00 26.51           C  
-ATOM  15356  C   ASN D 521     -27.828 -16.975-135.004  1.00 25.70           C  
-ATOM  15357  O   ASN D 521     -27.037 -16.842-135.948  1.00 34.44           O  
-ATOM  15358  CB  ASN D 521     -30.065 -15.859-135.034  1.00 28.71           C  
-ATOM  15359  CG  ASN D 521     -31.477 -15.883-135.595  1.00 34.30           C  
-ATOM  15360  OD1 ASN D 521     -32.447 -15.630-134.879  1.00 35.76           O  
-ATOM  15361  ND2 ASN D 521     -31.598 -16.196-136.882  1.00 22.17           N  
-ATOM  15362  N   ILE D 522     -27.456 -16.956-133.725  1.00 15.99           N  
-ATOM  15363  CA  ILE D 522     -26.053 -16.889-133.329  1.00 13.95           C  
-ATOM  15364  C   ILE D 522     -25.251 -17.943-134.070  1.00 18.95           C  
-ATOM  15365  O   ILE D 522     -24.299 -17.620-134.790  1.00 24.91           O  
-ATOM  15366  CB  ILE D 522     -25.873 -17.091-131.808  1.00 17.82           C  
-ATOM  15367  CG1 ILE D 522     -26.601 -15.993-131.029  1.00 22.58           C  
-ATOM  15368  CG2 ILE D 522     -24.401 -17.114-131.449  1.00 13.29           C  
-ATOM  15369  CD1 ILE D 522     -26.474 -16.133-129.532  1.00 16.35           C  
-ATOM  15370  N   ALA D 523     -25.665 -19.198-133.912  1.00 18.48           N  
-ATOM  15371  CA  ALA D 523     -24.995 -20.318-134.568  1.00 20.92           C  
-ATOM  15372  C   ALA D 523     -24.944 -20.132-136.083  1.00 23.22           C  
-ATOM  15373  O   ALA D 523     -23.908 -20.370-136.717  1.00 26.17           O  
-ATOM  15374  CB  ALA D 523     -25.688 -21.626-134.223  1.00 25.24           C  
-ATOM  15375  N   SER D 524     -26.063 -19.697-136.651  1.00 16.78           N  
-ATOM  15376  CA  SER D 524     -26.166 -19.498-138.088  1.00 20.17           C  
-ATOM  15377  C   SER D 524     -25.126 -18.523-138.632  1.00 23.17           C  
-ATOM  15378  O   SER D 524     -24.323 -18.879-139.496  1.00 21.31           O  
-ATOM  15379  CB  SER D 524     -27.576 -19.018-138.446  1.00 20.71           C  
-ATOM  15380  OG  SER D 524     -27.709 -18.880-139.847  1.00 31.50           O  
-ATOM  15381  N   TYR D 525     -25.140 -17.294-138.129  1.00 24.51           N  
-ATOM  15382  CA  TYR D 525     -24.252 -16.270-138.673  1.00 21.34           C  
-ATOM  15383  C   TYR D 525     -22.799 -16.471-138.246  1.00 24.58           C  
-ATOM  15384  O   TYR D 525     -21.880 -16.041-138.950  1.00 29.11           O  
-ATOM  15385  CB  TYR D 525     -24.746 -14.870-138.295  1.00 16.72           C  
-ATOM  15386  CG  TYR D 525     -25.814 -14.394-139.259  1.00 20.08           C  
-ATOM  15387  CD1 TYR D 525     -27.152 -14.679-139.039  1.00 16.39           C  
-ATOM  15388  CD2 TYR D 525     -25.475 -13.697-140.412  1.00 28.27           C  
-ATOM  15389  CE1 TYR D 525     -28.124 -14.268-139.924  1.00 17.71           C  
-ATOM  15390  CE2 TYR D 525     -26.439 -13.278-141.307  1.00 18.57           C  
-ATOM  15391  CZ  TYR D 525     -27.764 -13.565-141.060  1.00 22.64           C  
-ATOM  15392  OH  TYR D 525     -28.729 -13.149-141.949  1.00 34.31           O  
-ATOM  15393  N   SER D 526     -22.578 -17.136-137.115  1.00 22.75           N  
-ATOM  15394  CA  SER D 526     -21.215 -17.518-136.754  1.00 20.37           C  
-ATOM  15395  C   SER D 526     -20.682 -18.505-137.790  1.00 24.89           C  
-ATOM  15396  O   SER D 526     -19.558 -18.361-138.291  1.00 27.58           O  
-ATOM  15397  CB  SER D 526     -21.168 -18.129-135.355  1.00 14.95           C  
-ATOM  15398  OG  SER D 526     -21.568 -17.188-134.376  1.00 17.14           O  
-ATOM  15399  N   LEU D 527     -21.506 -19.501-138.112  1.00 24.61           N  
-ATOM  15400  CA  LEU D 527     -21.170 -20.476-139.143  1.00 27.35           C  
-ATOM  15401  C   LEU D 527     -20.864 -19.793-140.469  1.00 22.35           C  
-ATOM  15402  O   LEU D 527     -19.849 -20.088-141.109  1.00 22.85           O  
-ATOM  15403  CB  LEU D 527     -22.309 -21.480-139.325  1.00 23.04           C  
-ATOM  15404  CG  LEU D 527     -22.055 -22.643-140.288  1.00 18.36           C  
-ATOM  15405  CD1 LEU D 527     -20.822 -23.427-139.869  1.00 16.16           C  
-ATOM  15406  CD2 LEU D 527     -23.269 -23.554-140.356  1.00 23.53           C  
-ATOM  15407  N   LEU D 528     -21.749 -18.883-140.876  1.00 20.87           N  
-ATOM  15408  CA  LEU D 528     -21.537 -18.109-142.097  1.00 20.84           C  
-ATOM  15409  C   LEU D 528     -20.184 -17.416-142.062  1.00 19.67           C  
-ATOM  15410  O   LEU D 528     -19.448 -17.431-143.049  1.00 25.11           O  
-ATOM  15411  CB  LEU D 528     -22.642 -17.066-142.300  1.00 25.27           C  
-ATOM  15412  CG  LEU D 528     -22.469 -16.130-143.507  1.00 15.03           C  
-ATOM  15413  CD1 LEU D 528     -22.464 -16.913-144.809  1.00 15.41           C  
-ATOM  15414  CD2 LEU D 528     -23.548 -15.057-143.536  1.00 18.03           C  
-ATOM  15415  N   THR D 529     -19.861 -16.814-140.918  1.00 16.06           N  
-ATOM  15416  CA  THR D 529     -18.567 -16.159-140.743  1.00 17.07           C  
-ATOM  15417  C   THR D 529     -17.422 -17.135-140.969  1.00 17.98           C  
-ATOM  15418  O   THR D 529     -16.464 -16.814-141.669  1.00 20.58           O  
-ATOM  15419  CB  THR D 529     -18.417 -15.537-139.344  1.00 18.00           C  
-ATOM  15420  OG1 THR D 529     -19.496 -14.627-139.105  1.00 18.74           O  
-ATOM  15421  CG2 THR D 529     -17.096 -14.785-139.239  1.00 18.77           C  
-ATOM  15422  N   LEU D 530     -17.528 -18.325-140.383  1.00 19.00           N  
-ATOM  15423  CA  LEU D 530     -16.519 -19.366-140.576  1.00 17.31           C  
-ATOM  15424  C   LEU D 530     -16.317 -19.693-142.057  1.00 18.39           C  
-ATOM  15425  O   LEU D 530     -15.182 -19.716-142.552  1.00 22.30           O  
-ATOM  15426  CB  LEU D 530     -16.904 -20.638-139.815  1.00 17.87           C  
-ATOM  15427  CG  LEU D 530     -16.260 -20.888-138.449  1.00 21.12           C  
-ATOM  15428  CD1 LEU D 530     -16.548 -19.743-137.500  1.00 19.14           C  
-ATOM  15429  CD2 LEU D 530     -16.753 -22.204-137.869  1.00 19.42           C  
-ATOM  15430  N   MET D 531     -17.423 -19.933-142.757  1.00 19.32           N  
-ATOM  15431  CA  MET D 531     -17.375 -20.294-144.173  1.00 14.55           C  
-ATOM  15432  C   MET D 531     -16.748 -19.199-145.042  1.00 17.84           C  
-ATOM  15433  O   MET D 531     -15.814 -19.458-145.821  1.00 21.48           O  
-ATOM  15434  CB  MET D 531     -18.785 -20.621-144.662  1.00 13.48           C  
-ATOM  15435  CG  MET D 531     -19.444 -21.741-143.869  1.00 15.22           C  
-ATOM  15436  SD  MET D 531     -21.213 -21.911-144.174  1.00 18.00           S  
-ATOM  15437  CE  MET D 531     -21.222 -22.271-145.924  1.00 11.94           C  
-ATOM  15438  N   VAL D 532     -17.264 -17.979-144.903  1.00 18.16           N  
-ATOM  15439  CA  VAL D 532     -16.729 -16.837-145.640  1.00 20.57           C  
-ATOM  15440  C   VAL D 532     -15.232 -16.654-145.361  1.00 23.66           C  
-ATOM  15441  O   VAL D 532     -14.438 -16.436-146.286  1.00 18.34           O  
-ATOM  15442  CB  VAL D 532     -17.477 -15.533-145.293  1.00 15.10           C  
-ATOM  15443  CG1 VAL D 532     -16.813 -14.362-145.962  1.00 16.44           C  
-ATOM  15444  CG2 VAL D 532     -18.936 -15.622-145.714  1.00 14.01           C  
-ATOM  15445  N   ALA D 533     -14.852 -16.753-144.087  1.00 19.62           N  
-ATOM  15446  CA  ALA D 533     -13.449 -16.656-143.702  1.00 17.40           C  
-ATOM  15447  C   ALA D 533     -12.617 -17.699-144.437  1.00 18.87           C  
-ATOM  15448  O   ALA D 533     -11.552 -17.386-144.990  1.00 29.41           O  
-ATOM  15449  CB  ALA D 533     -13.292 -16.812-142.195  1.00 18.41           C  
-ATOM  15450  N   HIS D 534     -13.107 -18.936-144.467  1.00 16.60           N  
-ATOM  15451  CA  HIS D 534     -12.360 -19.984-145.155  1.00 28.42           C  
-ATOM  15452  C   HIS D 534     -12.205 -19.690-146.644  1.00 29.31           C  
-ATOM  15453  O   HIS D 534     -11.100 -19.814-147.182  1.00 22.45           O  
-ATOM  15454  CB  HIS D 534     -13.010 -21.354-144.986  1.00 22.02           C  
-ATOM  15455  CG  HIS D 534     -12.289 -22.441-145.722  1.00 23.69           C  
-ATOM  15456  ND1 HIS D 534     -12.800 -23.045-146.851  1.00 28.27           N  
-ATOM  15457  CD2 HIS D 534     -11.073 -22.999-145.516  1.00 26.13           C  
-ATOM  15458  CE1 HIS D 534     -11.940 -23.945-147.295  1.00 30.05           C  
-ATOM  15459  NE2 HIS D 534     -10.883 -23.936-146.502  1.00 36.25           N  
-ATOM  15460  N   VAL D 535     -13.288 -19.296-147.316  1.00 29.48           N  
-ATOM  15461  CA  VAL D 535     -13.183 -19.058-148.758  1.00 26.79           C  
-ATOM  15462  C   VAL D 535     -12.424 -17.762-149.071  1.00 25.91           C  
-ATOM  15463  O   VAL D 535     -12.068 -17.511-150.221  1.00 27.28           O  
-ATOM  15464  CB  VAL D 535     -14.568 -19.020-149.452  1.00 20.35           C  
-ATOM  15465  CG1 VAL D 535     -15.244 -20.379-149.371  1.00 17.78           C  
-ATOM  15466  CG2 VAL D 535     -15.460 -17.935-148.864  1.00 19.59           C  
-ATOM  15467  N   CYS D 536     -12.167 -16.947-148.052  1.00 26.01           N  
-ATOM  15468  CA  CYS D 536     -11.405 -15.718-148.257  1.00 23.04           C  
-ATOM  15469  C   CYS D 536      -9.996 -15.793-147.681  1.00 25.18           C  
-ATOM  15470  O   CYS D 536      -9.268 -14.800-147.707  1.00 28.36           O  
-ATOM  15471  CB  CYS D 536     -12.132 -14.523-147.641  1.00 22.10           C  
-ATOM  15472  SG  CYS D 536     -13.689 -14.075-148.433  1.00 31.68           S  
-ATOM  15473  N   ASN D 537      -9.625 -16.961-147.156  1.00 31.61           N  
-ATOM  15474  CA  ASN D 537      -8.307 -17.174-146.551  1.00 35.86           C  
-ATOM  15475  C   ASN D 537      -8.106 -16.295-145.325  1.00 30.65           C  
-ATOM  15476  O   ASN D 537      -6.988 -15.879-145.017  1.00 31.04           O  
-ATOM  15477  CB  ASN D 537      -7.185 -16.920-147.563  1.00 29.87           C  
-ATOM  15478  CG  ASN D 537      -6.976 -18.084-148.506  1.00 41.17           C  
-ATOM  15479  OD1 ASN D 537      -7.624 -18.181-149.550  1.00 53.26           O  
-ATOM  15480  ND2 ASN D 537      -6.063 -18.978-148.144  1.00 29.39           N  
-ATOM  15481  N   LEU D 538      -9.202 -16.019-144.628  1.00 23.86           N  
-ATOM  15482  CA  LEU D 538      -9.159 -15.239-143.402  1.00 24.85           C  
-ATOM  15483  C   LEU D 538      -9.411 -16.143-142.205  1.00 24.21           C  
-ATOM  15484  O   LEU D 538      -9.930 -17.249-142.353  1.00 23.67           O  
-ATOM  15485  CB  LEU D 538     -10.190 -14.114-143.451  1.00 20.29           C  
-ATOM  15486  CG  LEU D 538     -10.104 -13.234-144.697  1.00 17.01           C  
-ATOM  15487  CD1 LEU D 538     -11.272 -12.269-144.765  1.00 17.06           C  
-ATOM  15488  CD2 LEU D 538      -8.785 -12.486-144.698  1.00 20.73           C  
-ATOM  15489  N   LYS D 539      -9.031 -15.675-141.022  1.00 25.47           N  
-ATOM  15490  CA  LYS D 539      -9.283 -16.421-139.796  1.00 24.72           C  
-ATOM  15491  C   LYS D 539     -10.487 -15.829-139.081  1.00 29.32           C  
-ATOM  15492  O   LYS D 539     -10.517 -14.629-138.807  1.00 34.23           O  
-ATOM  15493  CB  LYS D 539      -8.058 -16.398-138.880  1.00 27.65           C  
-ATOM  15494  CG  LYS D 539      -6.756 -16.776-139.570  1.00 32.03           C  
-ATOM  15495  CD  LYS D 539      -5.558 -16.371-138.728  1.00 32.99           C  
-ATOM  15496  CE  LYS D 539      -4.565 -15.553-139.541  1.00 37.43           C  
-ATOM  15497  NZ  LYS D 539      -3.604 -14.822-138.665  1.00 40.72           N  
-ATOM  15498  N   PRO D 540     -11.494 -16.665-138.790  1.00 24.53           N  
-ATOM  15499  CA  PRO D 540     -12.672 -16.179-138.070  1.00 25.10           C  
-ATOM  15500  C   PRO D 540     -12.291 -15.661-136.689  1.00 24.93           C  
-ATOM  15501  O   PRO D 540     -11.526 -16.307-135.974  1.00 28.93           O  
-ATOM  15502  CB  PRO D 540     -13.570 -17.417-137.979  1.00 24.52           C  
-ATOM  15503  CG  PRO D 540     -12.651 -18.576-138.164  1.00 25.19           C  
-ATOM  15504  CD  PRO D 540     -11.591 -18.099-139.107  1.00 27.07           C  
-ATOM  15505  N   LYS D 541     -12.810 -14.493-136.331  1.00 23.50           N  
-ATOM  15506  CA  LYS D 541     -12.448 -13.856-135.074  1.00 26.68           C  
-ATOM  15507  C   LYS D 541     -13.651 -13.645-134.165  1.00 25.40           C  
-ATOM  15508  O   LYS D 541     -13.639 -14.060-133.007  1.00 23.85           O  
-ATOM  15509  CB  LYS D 541     -11.761 -12.514-135.338  1.00 30.62           C  
-ATOM  15510  CG  LYS D 541     -11.412 -11.736-134.078  1.00 25.08           C  
-ATOM  15511  CD  LYS D 541     -10.884 -10.349-134.412  1.00 27.71           C  
-ATOM  15512  CE  LYS D 541     -10.647  -9.530-133.155  1.00 33.92           C  
-ATOM  15513  NZ  LYS D 541      -9.654 -10.184-132.259  1.00 40.76           N  
-ATOM  15514  N   GLU D 542     -14.691 -13.008-134.691  1.00 23.13           N  
-ATOM  15515  CA  GLU D 542     -15.792 -12.565-133.848  1.00 23.11           C  
-ATOM  15516  C   GLU D 542     -17.107 -12.429-134.609  1.00 23.68           C  
-ATOM  15517  O   GLU D 542     -17.126 -12.032-135.774  1.00 23.82           O  
-ATOM  15518  CB  GLU D 542     -15.428 -11.227-133.201  1.00 36.51           C  
-ATOM  15519  CG  GLU D 542     -16.122 -10.936-131.883  1.00 39.06           C  
-ATOM  15520  CD  GLU D 542     -15.583  -9.682-131.216  1.00 50.28           C  
-ATOM  15521  OE1 GLU D 542     -15.693  -9.570-129.976  1.00 41.84           O  
-ATOM  15522  OE2 GLU D 542     -15.047  -8.810-131.936  1.00 45.98           O  
-ATOM  15523  N   PHE D 543     -18.205 -12.767-133.942  1.00 20.66           N  
-ATOM  15524  CA  PHE D 543     -19.535 -12.467-134.453  1.00 15.66           C  
-ATOM  15525  C   PHE D 543     -20.224 -11.449-133.558  1.00 15.75           C  
-ATOM  15526  O   PHE D 543     -20.426 -11.690-132.369  1.00 18.38           O  
-ATOM  15527  CB  PHE D 543     -20.397 -13.722-134.552  1.00 13.39           C  
-ATOM  15528  CG  PHE D 543     -21.868 -13.430-134.650  1.00 13.09           C  
-ATOM  15529  CD1 PHE D 543     -22.380 -12.752-135.744  1.00 17.39           C  
-ATOM  15530  CD2 PHE D 543     -22.737 -13.826-133.649  1.00 13.83           C  
-ATOM  15531  CE1 PHE D 543     -23.731 -12.474-135.838  1.00 16.18           C  
-ATOM  15532  CE2 PHE D 543     -24.091 -13.554-133.738  1.00 15.79           C  
-ATOM  15533  CZ  PHE D 543     -24.588 -12.876-134.835  1.00 16.49           C  
-ATOM  15534  N   ILE D 544     -20.590 -10.315-134.138  1.00 16.58           N  
-ATOM  15535  CA  ILE D 544     -21.256  -9.266-133.385  1.00 16.07           C  
-ATOM  15536  C   ILE D 544     -22.750  -9.250-133.694  1.00 18.48           C  
-ATOM  15537  O   ILE D 544     -23.166  -9.134-134.846  1.00 17.74           O  
-ATOM  15538  CB  ILE D 544     -20.636  -7.895-133.681  1.00 17.02           C  
-ATOM  15539  CG1 ILE D 544     -19.124  -7.957-133.456  1.00 24.42           C  
-ATOM  15540  CG2 ILE D 544     -21.270  -6.821-132.813  1.00 16.71           C  
-ATOM  15541  CD1 ILE D 544     -18.392  -6.697-133.838  1.00 33.26           C  
-ATOM  15542  N   HIS D 545     -23.549  -9.376-132.643  1.00 15.65           N  
-ATOM  15543  CA  HIS D 545     -24.990  -9.529-132.762  1.00 15.93           C  
-ATOM  15544  C   HIS D 545     -25.745  -8.292-132.283  1.00 19.75           C  
-ATOM  15545  O   HIS D 545     -25.813  -8.011-131.076  1.00 23.00           O  
-ATOM  15546  CB  HIS D 545     -25.444 -10.758-131.973  1.00 19.50           C  
-ATOM  15547  CG  HIS D 545     -26.831 -11.207-132.296  1.00 19.39           C  
-ATOM  15548  ND1 HIS D 545     -27.612 -10.588-133.253  1.00 18.74           N  
-ATOM  15549  CD2 HIS D 545     -27.582 -12.215-131.797  1.00 17.56           C  
-ATOM  15550  CE1 HIS D 545     -28.780 -11.194-133.321  1.00 17.86           C  
-ATOM  15551  NE2 HIS D 545     -28.790 -12.187-132.449  1.00 21.16           N  
-ATOM  15552  N   PHE D 546     -26.313  -7.564-133.242  1.00 14.46           N  
-ATOM  15553  CA  PHE D 546     -27.122  -6.383-132.961  1.00 18.58           C  
-ATOM  15554  C   PHE D 546     -28.612  -6.703-133.047  1.00 18.49           C  
-ATOM  15555  O   PHE D 546     -29.088  -7.229-134.052  1.00 21.11           O  
-ATOM  15556  CB  PHE D 546     -26.771  -5.251-133.926  1.00 21.03           C  
-ATOM  15557  CG  PHE D 546     -25.493  -4.539-133.585  1.00 23.75           C  
-ATOM  15558  CD1 PHE D 546     -24.813  -4.829-132.412  1.00 18.77           C  
-ATOM  15559  CD2 PHE D 546     -24.979  -3.568-134.428  1.00 24.15           C  
-ATOM  15560  CE1 PHE D 546     -23.643  -4.170-132.094  1.00 16.58           C  
-ATOM  15561  CE2 PHE D 546     -23.808  -2.906-134.114  1.00 19.73           C  
-ATOM  15562  CZ  PHE D 546     -23.140  -3.208-132.944  1.00 16.30           C  
-ATOM  15563  N   MET D 547     -29.348  -6.374-131.990  1.00 17.11           N  
-ATOM  15564  CA  MET D 547     -30.748  -6.770-131.876  1.00 14.97           C  
-ATOM  15565  C   MET D 547     -31.669  -5.572-131.656  1.00 22.63           C  
-ATOM  15566  O   MET D 547     -31.413  -4.732-130.794  1.00 28.01           O  
-ATOM  15567  CB  MET D 547     -30.906  -7.774-130.735  1.00 14.31           C  
-ATOM  15568  CG  MET D 547     -29.887  -8.910-130.798  1.00 28.02           C  
-ATOM  15569  SD  MET D 547     -29.693  -9.865-129.280  1.00 27.15           S  
-ATOM  15570  CE  MET D 547     -31.184 -10.853-129.313  1.00 26.27           C  
-ATOM  15571  N   GLY D 548     -32.740  -5.494-132.440  1.00 21.70           N  
-ATOM  15572  CA  GLY D 548     -33.707  -4.416-132.311  1.00 22.23           C  
-ATOM  15573  C   GLY D 548     -34.785  -4.727-131.289  1.00 23.29           C  
-ATOM  15574  O   GLY D 548     -34.583  -4.546-130.087  1.00 20.63           O  
-ATOM  15575  N   ASN D 549     -35.940  -5.188-131.762  1.00 21.60           N  
-ATOM  15576  CA  ASN D 549     -37.000  -5.630-130.863  1.00 21.22           C  
-ATOM  15577  C   ASN D 549     -36.627  -6.967-130.242  1.00 24.99           C  
-ATOM  15578  O   ASN D 549     -36.715  -8.010-130.890  1.00 29.28           O  
-ATOM  15579  CB  ASN D 549     -38.338  -5.744-131.599  1.00 26.22           C  
-ATOM  15580  CG  ASN D 549     -39.516  -5.907-130.651  1.00 25.53           C  
-ATOM  15581  OD1 ASN D 549     -39.737  -6.981-130.091  1.00 25.53           O  
-ATOM  15582  ND2 ASN D 549     -40.284  -4.837-130.476  1.00 21.12           N  
-ATOM  15583  N   THR D 550     -36.201  -6.932-128.986  1.00 17.70           N  
-ATOM  15584  CA  THR D 550     -35.735  -8.133-128.309  1.00 21.18           C  
-ATOM  15585  C   THR D 550     -36.767  -8.595-127.287  1.00 25.90           C  
-ATOM  15586  O   THR D 550     -36.934  -7.973-126.239  1.00 36.80           O  
-ATOM  15587  CB  THR D 550     -34.385  -7.889-127.620  1.00 20.99           C  
-ATOM  15588  OG1 THR D 550     -33.544  -7.112-128.481  1.00 25.80           O  
-ATOM  15589  CG2 THR D 550     -33.702  -9.203-127.313  1.00 24.97           C  
-ATOM  15590  N   HIS D 551     -37.456  -9.689-127.592  1.00 19.80           N  
-ATOM  15591  CA  HIS D 551     -38.609 -10.094-126.799  1.00 21.09           C  
-ATOM  15592  C   HIS D 551     -38.575 -11.548-126.354  1.00 23.93           C  
-ATOM  15593  O   HIS D 551     -37.969 -12.399-127.001  1.00 34.64           O  
-ATOM  15594  CB  HIS D 551     -39.893  -9.846-127.591  1.00 30.67           C  
-ATOM  15595  CG  HIS D 551     -39.885 -10.465-128.954  1.00 33.18           C  
-ATOM  15596  ND1 HIS D 551     -39.701  -9.728-130.104  1.00 28.38           N  
-ATOM  15597  CD2 HIS D 551     -40.027 -11.752-129.352  1.00 29.98           C  
-ATOM  15598  CE1 HIS D 551     -39.734 -10.533-131.151  1.00 30.11           C  
-ATOM  15599  NE2 HIS D 551     -39.932 -11.766-130.721  1.00 30.06           N  
-ATOM  15600  N   VAL D 552     -39.245 -11.812-125.238  1.00 28.93           N  
-ATOM  15601  CA  VAL D 552     -39.453 -13.161-124.737  1.00 21.32           C  
-ATOM  15602  C   VAL D 552     -40.952 -13.438-124.685  1.00 28.03           C  
-ATOM  15603  O   VAL D 552     -41.703 -12.687-124.058  1.00 26.87           O  
-ATOM  15604  CB  VAL D 552     -38.837 -13.349-123.339  1.00 15.83           C  
-ATOM  15605  CG1 VAL D 552     -39.409 -14.581-122.664  1.00 25.79           C  
-ATOM  15606  CG2 VAL D 552     -37.324 -13.430-123.429  1.00 16.42           C  
-ATOM  15607  N   TYR D 553     -41.392 -14.502-125.352  1.00 31.26           N  
-ATOM  15608  CA  TYR D 553     -42.813 -14.834-125.374  1.00 32.58           C  
-ATOM  15609  C   TYR D 553     -43.272 -15.319-124.004  1.00 28.40           C  
-ATOM  15610  O   TYR D 553     -42.572 -16.079-123.333  1.00 27.61           O  
-ATOM  15611  CB  TYR D 553     -43.114 -15.876-126.457  1.00 30.48           C  
-ATOM  15612  CG  TYR D 553     -43.145 -15.275-127.844  1.00 32.03           C  
-ATOM  15613  CD1 TYR D 553     -44.253 -14.566-128.285  1.00 35.51           C  
-ATOM  15614  CD2 TYR D 553     -42.062 -15.397-128.704  1.00 31.53           C  
-ATOM  15615  CE1 TYR D 553     -44.288 -14.001-129.546  1.00 37.02           C  
-ATOM  15616  CE2 TYR D 553     -42.087 -14.835-129.969  1.00 38.19           C  
-ATOM  15617  CZ  TYR D 553     -43.203 -14.136-130.383  1.00 33.98           C  
-ATOM  15618  OH  TYR D 553     -43.242 -13.573-131.638  1.00 27.55           O  
-ATOM  15619  N   THR D 554     -44.448 -14.855-123.595  1.00 29.75           N  
-ATOM  15620  CA  THR D 554     -44.981 -15.129-122.264  1.00 34.47           C  
-ATOM  15621  C   THR D 554     -45.088 -16.624-121.950  1.00 34.54           C  
-ATOM  15622  O   THR D 554     -44.916 -17.035-120.802  1.00 29.72           O  
-ATOM  15623  CB  THR D 554     -46.368 -14.477-122.084  1.00 31.38           C  
-ATOM  15624  OG1 THR D 554     -47.159 -14.701-123.258  1.00 32.74           O  
-ATOM  15625  CG2 THR D 554     -46.226 -12.978-121.864  1.00 24.11           C  
-ATOM  15626  N   ASN D 555     -45.363 -17.436-122.966  1.00 33.41           N  
-ATOM  15627  CA  ASN D 555     -45.456 -18.877-122.770  1.00 25.83           C  
-ATOM  15628  C   ASN D 555     -44.091 -19.562-122.872  1.00 29.47           C  
-ATOM  15629  O   ASN D 555     -44.007 -20.768-123.107  1.00 32.24           O  
-ATOM  15630  CB  ASN D 555     -46.439 -19.489-123.775  1.00 27.94           C  
-ATOM  15631  CG  ASN D 555     -46.013 -19.286-125.220  1.00 34.38           C  
-ATOM  15632  OD1 ASN D 555     -45.389 -18.282-125.565  1.00 42.03           O  
-ATOM  15633  ND2 ASN D 555     -46.357 -20.241-126.076  1.00 29.34           N  
-ATOM  15634  N   HIS D 556     -43.026 -18.786-122.691  1.00 30.26           N  
-ATOM  15635  CA  HIS D 556     -41.667 -19.320-122.692  1.00 37.60           C  
-ATOM  15636  C   HIS D 556     -40.983 -19.065-121.357  1.00 35.35           C  
-ATOM  15637  O   HIS D 556     -39.958 -19.670-121.044  1.00 33.09           O  
-ATOM  15638  CB  HIS D 556     -40.836 -18.696-123.815  1.00 33.50           C  
-ATOM  15639  CG  HIS D 556     -41.225 -19.152-125.185  1.00 32.53           C  
-ATOM  15640  ND1 HIS D 556     -40.487 -18.839-126.306  1.00 42.09           N  
-ATOM  15641  CD2 HIS D 556     -42.270 -19.896-125.618  1.00 33.38           C  
-ATOM  15642  CE1 HIS D 556     -41.061 -19.370-127.371  1.00 48.43           C  
-ATOM  15643  NE2 HIS D 556     -42.145 -20.016-126.980  1.00 50.38           N  
-ATOM  15644  N   VAL D 557     -41.568 -18.159-120.581  1.00 27.28           N  
-ATOM  15645  CA  VAL D 557     -40.945 -17.623-119.378  1.00 26.41           C  
-ATOM  15646  C   VAL D 557     -40.504 -18.678-118.369  1.00 33.80           C  
-ATOM  15647  O   VAL D 557     -39.381 -18.628-117.862  1.00 35.68           O  
-ATOM  15648  CB  VAL D 557     -41.898 -16.645-118.669  1.00 37.25           C  
-ATOM  15649  CG1 VAL D 557     -41.303 -16.191-117.346  1.00 24.23           C  
-ATOM  15650  CG2 VAL D 557     -42.205 -15.458-119.574  1.00 33.38           C  
-ATOM  15651  N   GLU D 558     -41.389 -19.625-118.078  1.00 44.00           N  
-ATOM  15652  CA  GLU D 558     -41.096 -20.658-117.094  1.00 41.41           C  
-ATOM  15653  C   GLU D 558     -39.961 -21.557-117.574  1.00 43.79           C  
-ATOM  15654  O   GLU D 558     -39.032 -21.852-116.819  1.00 48.46           O  
-ATOM  15655  CB  GLU D 558     -42.349 -21.485-116.796  1.00 35.21           C  
-ATOM  15656  CG  GLU D 558     -42.387 -22.039-115.391  1.00 54.36           C  
-ATOM  15657  CD  GLU D 558     -42.526 -20.943-114.346  1.00 61.33           C  
-ATOM  15658  OE1 GLU D 558     -42.998 -19.842-114.702  1.00 43.51           O  
-ATOM  15659  OE2 GLU D 558     -42.170 -21.179-113.170  1.00 62.67           O  
-ATOM  15660  N   ALA D 559     -40.038 -21.973-118.835  1.00 38.04           N  
-ATOM  15661  CA  ALA D 559     -39.010 -22.812-119.434  1.00 33.44           C  
-ATOM  15662  C   ALA D 559     -37.658 -22.112-119.391  1.00 31.90           C  
-ATOM  15663  O   ALA D 559     -36.637 -22.730-119.092  1.00 28.89           O  
-ATOM  15664  CB  ALA D 559     -39.382 -23.168-120.865  1.00 29.67           C  
-ATOM  15665  N   LEU D 560     -37.662 -20.816-119.686  1.00 36.87           N  
-ATOM  15666  CA  LEU D 560     -36.445 -20.021-119.641  1.00 28.04           C  
-ATOM  15667  C   LEU D 560     -35.923 -19.907-118.222  1.00 35.35           C  
-ATOM  15668  O   LEU D 560     -34.714 -19.850-118.004  1.00 42.68           O  
-ATOM  15669  CB  LEU D 560     -36.688 -18.629-120.218  1.00 20.72           C  
-ATOM  15670  CG  LEU D 560     -36.887 -18.589-121.729  1.00 21.42           C  
-ATOM  15671  CD1 LEU D 560     -37.016 -17.165-122.217  1.00 23.65           C  
-ATOM  15672  CD2 LEU D 560     -35.734 -19.287-122.417  1.00 29.17           C  
-ATOM  15673  N   LYS D 561     -36.836 -19.863-117.258  1.00 32.58           N  
-ATOM  15674  CA  LYS D 561     -36.444 -19.795-115.860  1.00 31.50           C  
-ATOM  15675  C   LYS D 561     -35.824 -21.117-115.439  1.00 38.85           C  
-ATOM  15676  O   LYS D 561     -34.987 -21.165-114.537  1.00 41.74           O  
-ATOM  15677  CB  LYS D 561     -37.642 -19.435-114.980  1.00 36.34           C  
-ATOM  15678  CG  LYS D 561     -37.866 -17.934-114.872  1.00 44.21           C  
-ATOM  15679  CD  LYS D 561     -39.298 -17.564-114.513  1.00 45.71           C  
-ATOM  15680  CE  LYS D 561     -39.668 -18.001-113.105  1.00 53.17           C  
-ATOM  15681  NZ  LYS D 561     -41.056 -17.580-112.758  1.00 45.94           N  
-ATOM  15682  N   GLU D 562     -36.233 -22.188-116.107  1.00 39.31           N  
-ATOM  15683  CA  GLU D 562     -35.594 -23.478-115.914  1.00 42.35           C  
-ATOM  15684  C   GLU D 562     -34.198 -23.459-116.530  1.00 37.66           C  
-ATOM  15685  O   GLU D 562     -33.245 -23.957-115.937  1.00 34.99           O  
-ATOM  15686  CB  GLU D 562     -36.436 -24.603-116.523  1.00 40.73           C  
-ATOM  15687  CG  GLU D 562     -37.452 -25.230-115.575  1.00 51.53           C  
-ATOM  15688  CD  GLU D 562     -36.833 -26.248-114.631  1.00 64.02           C  
-ATOM  15689  OE1 GLU D 562     -35.935 -25.875-113.846  1.00 61.12           O  
-ATOM  15690  OE2 GLU D 562     -37.243 -27.427-114.679  1.00 64.23           O  
-ATOM  15691  N   GLN D 563     -34.085 -22.869-117.716  1.00 38.97           N  
-ATOM  15692  CA  GLN D 563     -32.816 -22.809-118.436  1.00 31.62           C  
-ATOM  15693  C   GLN D 563     -31.783 -21.981-117.679  1.00 28.54           C  
-ATOM  15694  O   GLN D 563     -30.591 -22.277-117.717  1.00 38.01           O  
-ATOM  15695  CB  GLN D 563     -33.023 -22.232-119.844  1.00 25.81           C  
-ATOM  15696  CG  GLN D 563     -31.810 -22.386-120.768  1.00 25.16           C  
-ATOM  15697  CD  GLN D 563     -32.091 -21.950-122.201  1.00 28.49           C  
-ATOM  15698  OE1 GLN D 563     -33.236 -21.689-122.573  1.00 32.10           O  
-ATOM  15699  NE2 GLN D 563     -31.041 -21.870-123.011  1.00 19.95           N  
-ATOM  15700  N   LEU D 564     -32.247 -20.953-116.980  1.00 27.18           N  
-ATOM  15701  CA  LEU D 564     -31.351 -20.023-116.300  1.00 31.24           C  
-ATOM  15702  C   LEU D 564     -30.719 -20.646-115.061  1.00 37.70           C  
-ATOM  15703  O   LEU D 564     -29.795 -20.077-114.478  1.00 45.08           O  
-ATOM  15704  CB  LEU D 564     -32.094 -18.739-115.915  1.00 35.79           C  
-ATOM  15705  CG  LEU D 564     -32.302 -17.639-116.965  1.00 28.91           C  
-ATOM  15706  CD1 LEU D 564     -31.423 -16.446-116.655  1.00 33.24           C  
-ATOM  15707  CD2 LEU D 564     -32.036 -18.126-118.381  1.00 33.75           C  
-ATOM  15708  N   ARG D 565     -31.221 -21.810-114.659  1.00 33.19           N  
-ATOM  15709  CA  ARG D 565     -30.654 -22.530-113.523  1.00 37.31           C  
-ATOM  15710  C   ARG D 565     -29.554 -23.484-113.980  1.00 36.76           C  
-ATOM  15711  O   ARG D 565     -28.955 -24.200-113.174  1.00 30.53           O  
-ATOM  15712  CB  ARG D 565     -31.739 -23.299-112.771  1.00 34.27           C  
-ATOM  15713  CG  ARG D 565     -32.738 -22.407-112.059  1.00 44.31           C  
-ATOM  15714  CD  ARG D 565     -33.679 -23.219-111.186  1.00 48.71           C  
-ATOM  15715  NE  ARG D 565     -34.716 -22.386-110.584  1.00 67.79           N  
-ATOM  15716  CZ  ARG D 565     -35.908 -22.166-111.131  1.00 70.05           C  
-ATOM  15717  NH1 ARG D 565     -36.216 -22.720-112.295  1.00 61.47           N  
-ATOM  15718  NH2 ARG D 565     -36.794 -21.395-110.513  1.00 56.51           N  
-ATOM  15719  N   ARG D 566     -29.292 -23.481-115.283  1.00 33.74           N  
-ATOM  15720  CA  ARG D 566     -28.283 -24.352-115.870  1.00 27.83           C  
-ATOM  15721  C   ARG D 566     -26.972 -23.612-116.103  1.00 23.62           C  
-ATOM  15722  O   ARG D 566     -26.932 -22.600-116.802  1.00 20.00           O  
-ATOM  15723  CB  ARG D 566     -28.789 -24.942-117.189  1.00 24.00           C  
-ATOM  15724  CG  ARG D 566     -30.053 -25.780-117.067  1.00 28.57           C  
-ATOM  15725  CD  ARG D 566     -30.433 -26.388-118.409  1.00 32.77           C  
-ATOM  15726  NE  ARG D 566     -31.623 -27.233-118.332  1.00 35.56           N  
-ATOM  15727  CZ  ARG D 566     -32.144 -27.880-119.370  1.00 33.93           C  
-ATOM  15728  NH1 ARG D 566     -33.228 -28.629-119.215  1.00 31.40           N  
-ATOM  15729  NH2 ARG D 566     -31.582 -27.778-120.565  1.00 35.04           N  
-ATOM  15730  N   GLU D 567     -25.900 -24.126-115.512  1.00 25.34           N  
-ATOM  15731  CA  GLU D 567     -24.570 -23.578-115.740  1.00 24.02           C  
-ATOM  15732  C   GLU D 567     -24.006 -24.087-117.060  1.00 19.39           C  
-ATOM  15733  O   GLU D 567     -24.011 -25.289-117.323  1.00 21.55           O  
-ATOM  15734  CB  GLU D 567     -23.630 -23.934-114.587  1.00 24.83           C  
-ATOM  15735  CG  GLU D 567     -23.945 -25.262-113.925  1.00 41.34           C  
-ATOM  15736  CD  GLU D 567     -24.636 -25.089-112.588  1.00 40.42           C  
-ATOM  15737  OE1 GLU D 567     -25.564 -25.870-112.286  1.00 34.76           O  
-ATOM  15738  OE2 GLU D 567     -24.244 -24.171-111.837  1.00 35.33           O  
-ATOM  15739  N   PRO D 568     -23.515 -23.163-117.895  1.00 17.97           N  
-ATOM  15740  CA  PRO D 568     -23.013 -23.461-119.240  1.00 19.44           C  
-ATOM  15741  C   PRO D 568     -21.836 -24.430-119.244  1.00 24.71           C  
-ATOM  15742  O   PRO D 568     -21.085 -24.508-118.270  1.00 24.91           O  
-ATOM  15743  CB  PRO D 568     -22.576 -22.088-119.763  1.00 17.91           C  
-ATOM  15744  CG  PRO D 568     -23.328 -21.104-118.933  1.00 25.62           C  
-ATOM  15745  CD  PRO D 568     -23.428 -21.727-117.583  1.00 18.69           C  
-ATOM  15746  N   ARG D 569     -21.688 -25.161-120.343  1.00 29.53           N  
-ATOM  15747  CA  ARG D 569     -20.545 -26.046-120.539  1.00 27.08           C  
-ATOM  15748  C   ARG D 569     -19.651 -25.482-121.645  1.00 24.59           C  
-ATOM  15749  O   ARG D 569     -20.074 -24.587-122.378  1.00 27.62           O  
-ATOM  15750  CB  ARG D 569     -21.016 -27.462-120.879  1.00 24.65           C  
-ATOM  15751  CG  ARG D 569     -21.982 -28.043-119.860  1.00 29.26           C  
-ATOM  15752  CD  ARG D 569     -21.779 -29.539-119.675  1.00 30.12           C  
-ATOM  15753  NE  ARG D 569     -22.704 -30.086-118.687  1.00 28.09           N  
-ATOM  15754  CZ  ARG D 569     -23.883 -30.621-118.984  1.00 30.97           C  
-ATOM  15755  NH1 ARG D 569     -24.663 -31.090-118.019  1.00 29.80           N  
-ATOM  15756  NH2 ARG D 569     -24.280 -30.690-120.247  1.00 31.04           N  
-ATOM  15757  N   PRO D 570     -18.404 -25.974-121.747  1.00 19.54           N  
-ATOM  15758  CA  PRO D 570     -17.488 -25.548-122.809  1.00 16.78           C  
-ATOM  15759  C   PRO D 570     -18.130 -25.507-124.192  1.00 17.48           C  
-ATOM  15760  O   PRO D 570     -18.829 -26.443-124.578  1.00 19.59           O  
-ATOM  15761  CB  PRO D 570     -16.390 -26.617-122.773  1.00 18.25           C  
-ATOM  15762  CG  PRO D 570     -16.498 -27.277-121.422  1.00 22.85           C  
-ATOM  15763  CD  PRO D 570     -17.691 -26.724-120.700  1.00 23.18           C  
-ATOM  15764  N   PHE D 571     -17.907 -24.416-124.915  1.00 19.48           N  
-ATOM  15765  CA  PHE D 571     -18.297 -24.340-126.313  1.00 14.91           C  
-ATOM  15766  C   PHE D 571     -17.547 -25.404-127.102  1.00 18.31           C  
-ATOM  15767  O   PHE D 571     -16.382 -25.684-126.823  1.00 14.38           O  
-ATOM  15768  CB  PHE D 571     -18.006 -22.953-126.888  1.00 18.70           C  
-ATOM  15769  CG  PHE D 571     -19.051 -21.926-126.562  1.00 18.64           C  
-ATOM  15770  CD1 PHE D 571     -20.361 -22.302-126.317  1.00 20.02           C  
-ATOM  15771  CD2 PHE D 571     -18.723 -20.583-126.509  1.00 20.84           C  
-ATOM  15772  CE1 PHE D 571     -21.323 -21.355-126.022  1.00 18.25           C  
-ATOM  15773  CE2 PHE D 571     -19.679 -19.633-126.215  1.00 21.29           C  
-ATOM  15774  CZ  PHE D 571     -20.981 -20.020-125.971  1.00 20.93           C  
-ATOM  15775  N   PRO D 572     -18.218 -26.015-128.085  1.00 24.09           N  
-ATOM  15776  CA  PRO D 572     -17.541 -26.965-128.969  1.00 17.74           C  
-ATOM  15777  C   PRO D 572     -16.734 -26.215-130.020  1.00 21.22           C  
-ATOM  15778  O   PRO D 572     -16.875 -24.996-130.124  1.00 21.33           O  
-ATOM  15779  CB  PRO D 572     -18.699 -27.728-129.609  1.00 16.61           C  
-ATOM  15780  CG  PRO D 572     -19.794 -26.716-129.670  1.00 16.42           C  
-ATOM  15781  CD  PRO D 572     -19.645 -25.868-128.427  1.00 18.35           C  
-ATOM  15782  N   ILE D 573     -15.895 -26.911-130.780  1.00 25.34           N  
-ATOM  15783  CA  ILE D 573     -15.291 -26.282-131.948  1.00 21.71           C  
-ATOM  15784  C   ILE D 573     -15.952 -26.866-133.188  1.00 14.38           C  
-ATOM  15785  O   ILE D 573     -16.283 -28.049-133.230  1.00 11.68           O  
-ATOM  15786  CB  ILE D 573     -13.745 -26.465-132.011  1.00 15.58           C  
-ATOM  15787  CG1 ILE D 573     -13.358 -27.822-132.591  1.00 21.40           C  
-ATOM  15788  CG2 ILE D 573     -13.108 -26.255-130.646  1.00 11.72           C  
-ATOM  15789  CD1 ILE D 573     -11.870 -27.981-132.810  1.00 40.84           C  
-ATOM  15790  N   VAL D 574     -16.188 -26.022-134.183  1.00 14.58           N  
-ATOM  15791  CA  VAL D 574     -16.752 -26.491-135.440  1.00 14.25           C  
-ATOM  15792  C   VAL D 574     -15.660 -26.531-136.497  1.00 13.55           C  
-ATOM  15793  O   VAL D 574     -15.059 -25.506-136.820  1.00 13.53           O  
-ATOM  15794  CB  VAL D 574     -17.913 -25.602-135.922  1.00 14.15           C  
-ATOM  15795  CG1 VAL D 574     -18.228 -25.878-137.380  1.00 17.34           C  
-ATOM  15796  CG2 VAL D 574     -19.142 -25.826-135.058  1.00 13.07           C  
-ATOM  15797  N   ASN D 575     -15.394 -27.720-137.024  1.00 15.32           N  
-ATOM  15798  CA  ASN D 575     -14.379 -27.871-138.059  1.00 20.66           C  
-ATOM  15799  C   ASN D 575     -14.982 -28.005-139.449  1.00 16.54           C  
-ATOM  15800  O   ASN D 575     -15.962 -28.727-139.651  1.00 17.65           O  
-ATOM  15801  CB  ASN D 575     -13.491 -29.080-137.768  1.00 23.39           C  
-ATOM  15802  CG  ASN D 575     -12.682 -28.911-136.507  1.00 16.66           C  
-ATOM  15803  OD1 ASN D 575     -12.170 -27.828-136.228  1.00 16.29           O  
-ATOM  15804  ND2 ASN D 575     -12.567 -29.979-135.729  1.00 16.58           N  
-ATOM  15805  N   ILE D 576     -14.391 -27.297-140.403  1.00 13.47           N  
-ATOM  15806  CA  ILE D 576     -14.736 -27.475-141.800  1.00 13.12           C  
-ATOM  15807  C   ILE D 576     -13.909 -28.628-142.346  1.00 11.67           C  
-ATOM  15808  O   ILE D 576     -12.682 -28.613-142.268  1.00 10.95           O  
-ATOM  15809  CB  ILE D 576     -14.483 -26.201-142.629  1.00 11.52           C  
-ATOM  15810  CG1 ILE D 576     -15.269 -25.029-142.049  1.00  9.48           C  
-ATOM  15811  CG2 ILE D 576     -14.866 -26.424-144.083  1.00 14.94           C  
-ATOM  15812  CD1 ILE D 576     -15.115 -23.761-142.839  1.00 15.32           C  
-ATOM  15813  N   LEU D 577     -14.586 -29.635-142.882  1.00 12.06           N  
-ATOM  15814  CA  LEU D 577     -13.909 -30.789-143.460  1.00 20.16           C  
-ATOM  15815  C   LEU D 577     -13.659 -30.565-144.949  1.00 28.40           C  
-ATOM  15816  O   LEU D 577     -14.360 -29.774-145.584  1.00 28.56           O  
-ATOM  15817  CB  LEU D 577     -14.738 -32.056-143.233  1.00 20.76           C  
-ATOM  15818  CG  LEU D 577     -15.124 -32.315-141.773  1.00 17.92           C  
-ATOM  15819  CD1 LEU D 577     -16.369 -33.181-141.678  1.00 19.81           C  
-ATOM  15820  CD2 LEU D 577     -13.968 -32.957-141.026  1.00 14.84           C  
-ATOM  15821  N   ASN D 578     -12.658 -31.252-145.494  1.00 25.41           N  
-ATOM  15822  CA  ASN D 578     -12.325 -31.151-146.916  1.00 33.53           C  
-ATOM  15823  C   ASN D 578     -12.056 -29.714-147.352  1.00 31.36           C  
-ATOM  15824  O   ASN D 578     -12.604 -29.246-148.352  1.00 31.72           O  
-ATOM  15825  CB  ASN D 578     -13.448 -31.745-147.770  1.00 30.26           C  
-ATOM  15826  CG  ASN D 578     -14.027 -33.009-147.170  1.00 27.53           C  
-ATOM  15827  OD1 ASN D 578     -13.303 -33.960-146.877  1.00 34.45           O  
-ATOM  15828  ND2 ASN D 578     -15.340 -33.021-146.973  1.00 23.18           N  
-ATOM  15829  N   LYS D 579     -11.214 -29.020-146.593  1.00 31.25           N  
-ATOM  15830  CA  LYS D 579     -10.897 -27.622-146.873  1.00 35.99           C  
-ATOM  15831  C   LYS D 579     -10.204 -27.458-148.221  1.00 32.24           C  
-ATOM  15832  O   LYS D 579     -10.294 -26.406-148.849  1.00 34.93           O  
-ATOM  15833  CB  LYS D 579     -10.022 -27.031-145.759  1.00 31.55           C  
-ATOM  15834  CG  LYS D 579      -9.810 -27.946-144.562  1.00 48.33           C  
-ATOM  15835  CD  LYS D 579      -8.577 -28.829-144.735  1.00 60.26           C  
-ATOM  15836  CE  LYS D 579      -8.490 -29.881-143.640  1.00 39.84           C  
-ATOM  15837  NZ  LYS D 579      -9.628 -30.844-143.700  1.00 37.50           N  
-ATOM  15838  N   GLU D 580      -9.511 -28.505-148.654  1.00 32.26           N  
-ATOM  15839  CA  GLU D 580      -8.792 -28.478-149.922  1.00 32.77           C  
-ATOM  15840  C   GLU D 580      -9.749 -28.359-151.103  1.00 28.38           C  
-ATOM  15841  O   GLU D 580      -9.454 -27.686-152.090  1.00 30.33           O  
-ATOM  15842  CB  GLU D 580      -7.924 -29.734-150.065  1.00 36.24           C  
-ATOM  15843  CG  GLU D 580      -7.284 -29.924-151.436  1.00 53.45           C  
-ATOM  15844  CD  GLU D 580      -6.153 -28.949-151.715  1.00 67.13           C  
-ATOM  15845  OE1 GLU D 580      -5.640 -28.948-152.856  1.00 67.11           O  
-ATOM  15846  OE2 GLU D 580      -5.770 -28.188-150.801  1.00 73.23           O  
-ATOM  15847  N   ARG D 581     -10.903 -29.004-150.987  1.00 28.28           N  
-ATOM  15848  CA  ARG D 581     -11.868 -29.058-152.079  1.00 28.11           C  
-ATOM  15849  C   ARG D 581     -12.719 -27.795-152.165  1.00 29.12           C  
-ATOM  15850  O   ARG D 581     -13.170 -27.408-153.245  1.00 27.53           O  
-ATOM  15851  CB  ARG D 581     -12.773 -30.282-151.922  1.00 27.83           C  
-ATOM  15852  CG  ARG D 581     -13.803 -30.430-153.025  1.00 25.03           C  
-ATOM  15853  CD  ARG D 581     -14.707 -31.628-152.803  1.00 26.64           C  
-ATOM  15854  NE  ARG D 581     -15.392 -31.582-151.514  1.00 26.13           N  
-ATOM  15855  CZ  ARG D 581     -16.453 -30.824-151.256  1.00 30.31           C  
-ATOM  15856  NH1 ARG D 581     -16.951 -30.029-152.195  1.00 34.88           N  
-ATOM  15857  NH2 ARG D 581     -17.015 -30.854-150.056  1.00 26.08           N  
-ATOM  15858  N   ILE D 582     -12.935 -27.153-151.022  1.00 29.85           N  
-ATOM  15859  CA  ILE D 582     -13.839 -26.012-150.948  1.00 25.50           C  
-ATOM  15860  C   ILE D 582     -13.128 -24.692-151.238  1.00 27.55           C  
-ATOM  15861  O   ILE D 582     -12.349 -24.200-150.421  1.00 27.44           O  
-ATOM  15862  CB  ILE D 582     -14.512 -25.943-149.571  1.00 22.77           C  
-ATOM  15863  CG1 ILE D 582     -15.181 -27.283-149.257  1.00 22.46           C  
-ATOM  15864  CG2 ILE D 582     -15.518 -24.806-149.526  1.00 21.91           C  
-ATOM  15865  CD1 ILE D 582     -15.737 -27.387-147.857  1.00 23.52           C  
-ATOM  15866  N   LYS D 583     -13.407 -24.124-152.407  1.00 28.20           N  
-ATOM  15867  CA  LYS D 583     -12.759 -22.889-152.837  1.00 29.69           C  
-ATOM  15868  C   LYS D 583     -13.733 -21.716-152.952  1.00 27.97           C  
-ATOM  15869  O   LYS D 583     -13.342 -20.562-152.779  1.00 26.11           O  
-ATOM  15870  CB  LYS D 583     -12.056 -23.100-154.176  1.00 31.34           C  
-ATOM  15871  CG  LYS D 583     -10.937 -24.129-154.143  1.00 26.91           C  
-ATOM  15872  CD  LYS D 583     -10.335 -24.301-155.529  1.00 55.89           C  
-ATOM  15873  CE  LYS D 583      -9.150 -25.256-155.528  1.00 58.72           C  
-ATOM  15874  NZ  LYS D 583      -8.597 -25.438-156.904  1.00 50.45           N  
-ATOM  15875  N   GLU D 584     -14.993 -22.009-153.259  1.00 23.76           N  
-ATOM  15876  CA  GLU D 584     -16.015 -20.970-153.325  1.00 17.31           C  
-ATOM  15877  C   GLU D 584     -17.157 -21.272-152.359  1.00 20.16           C  
-ATOM  15878  O   GLU D 584     -17.334 -22.412-151.929  1.00 26.98           O  
-ATOM  15879  CB  GLU D 584     -16.543 -20.820-154.753  1.00 19.98           C  
-ATOM  15880  CG  GLU D 584     -15.461 -20.583-155.805  1.00 32.67           C  
-ATOM  15881  CD  GLU D 584     -14.812 -19.214-155.698  1.00 33.27           C  
-ATOM  15882  OE1 GLU D 584     -15.287 -18.384-154.893  1.00 36.12           O  
-ATOM  15883  OE2 GLU D 584     -13.826 -18.965-156.425  1.00 29.00           O  
-ATOM  15884  N   ILE D 585     -17.927 -20.244-152.022  1.00 21.07           N  
-ATOM  15885  CA  ILE D 585     -18.965 -20.357-151.001  1.00 22.98           C  
-ATOM  15886  C   ILE D 585     -20.058 -21.360-151.386  1.00 23.10           C  
-ATOM  15887  O   ILE D 585     -20.754 -21.892-150.521  1.00 28.17           O  
-ATOM  15888  CB  ILE D 585     -19.606 -18.977-150.712  1.00 24.05           C  
-ATOM  15889  CG1 ILE D 585     -20.480 -19.027-149.454  1.00 19.94           C  
-ATOM  15890  CG2 ILE D 585     -20.384 -18.474-151.923  1.00 24.04           C  
-ATOM  15891  CD1 ILE D 585     -19.706 -19.296-148.181  1.00 12.53           C  
-ATOM  15892  N   ASP D 586     -20.193 -21.631-152.680  1.00 19.81           N  
-ATOM  15893  CA  ASP D 586     -21.204 -22.568-153.160  1.00 18.10           C  
-ATOM  15894  C   ASP D 586     -20.754 -24.021-153.013  1.00 25.97           C  
-ATOM  15895  O   ASP D 586     -21.560 -24.945-153.142  1.00 26.27           O  
-ATOM  15896  CB  ASP D 586     -21.544 -22.272-154.620  1.00 27.07           C  
-ATOM  15897  CG  ASP D 586     -22.266 -20.950-154.792  1.00 42.72           C  
-ATOM  15898  OD1 ASP D 586     -23.313 -20.757-154.138  1.00 33.76           O  
-ATOM  15899  OD2 ASP D 586     -21.782 -20.101-155.572  1.00 47.80           O  
-ATOM  15900  N   ASP D 587     -19.469 -24.216-152.729  1.00 24.80           N  
-ATOM  15901  CA  ASP D 587     -18.884 -25.554-152.689  1.00 17.97           C  
-ATOM  15902  C   ASP D 587     -19.170 -26.301-151.385  1.00 19.69           C  
-ATOM  15903  O   ASP D 587     -18.944 -27.508-151.295  1.00 24.98           O  
-ATOM  15904  CB  ASP D 587     -17.373 -25.468-152.918  1.00 19.10           C  
-ATOM  15905  CG  ASP D 587     -17.022 -24.963-154.305  1.00 27.16           C  
-ATOM  15906  OD1 ASP D 587     -17.812 -25.200-155.245  1.00 31.86           O  
-ATOM  15907  OD2 ASP D 587     -15.956 -24.330-154.459  1.00 34.22           O  
-ATOM  15908  N   PHE D 588     -19.661 -25.587-150.378  1.00 18.95           N  
-ATOM  15909  CA  PHE D 588     -19.995 -26.209-149.101  1.00 17.99           C  
-ATOM  15910  C   PHE D 588     -21.176 -27.161-149.240  1.00 19.87           C  
-ATOM  15911  O   PHE D 588     -22.123 -26.884-149.977  1.00 22.30           O  
-ATOM  15912  CB  PHE D 588     -20.318 -25.146-148.050  1.00 21.87           C  
-ATOM  15913  CG  PHE D 588     -19.111 -24.437-147.503  1.00 21.54           C  
-ATOM  15914  CD1 PHE D 588     -18.434 -24.942-146.407  1.00 17.82           C  
-ATOM  15915  CD2 PHE D 588     -18.665 -23.257-148.072  1.00 18.84           C  
-ATOM  15916  CE1 PHE D 588     -17.329 -24.291-145.896  1.00 12.27           C  
-ATOM  15917  CE2 PHE D 588     -17.562 -22.601-147.562  1.00 16.82           C  
-ATOM  15918  CZ  PHE D 588     -16.893 -23.120-146.475  1.00  9.82           C  
-ATOM  15919  N   THR D 589     -21.115 -28.288-148.536  1.00 21.22           N  
-ATOM  15920  CA  THR D 589     -22.262 -29.184-148.430  1.00 19.64           C  
-ATOM  15921  C   THR D 589     -22.589 -29.428-146.959  1.00 17.95           C  
-ATOM  15922  O   THR D 589     -21.939 -28.880-146.070  1.00 17.64           O  
-ATOM  15923  CB  THR D 589     -22.018 -30.534-149.130  1.00 20.30           C  
-ATOM  15924  OG1 THR D 589     -21.160 -31.350-148.323  1.00 21.76           O  
-ATOM  15925  CG2 THR D 589     -21.386 -30.323-150.499  1.00 23.84           C  
-ATOM  15926  N   ALA D 590     -23.594 -30.257-146.704  1.00 20.35           N  
-ATOM  15927  CA  ALA D 590     -24.024 -30.527-145.338  1.00 21.34           C  
-ATOM  15928  C   ALA D 590     -23.111 -31.541-144.661  1.00 20.29           C  
-ATOM  15929  O   ALA D 590     -23.313 -31.892-143.499  1.00 23.89           O  
-ATOM  15930  CB  ALA D 590     -25.462 -31.020-145.323  1.00 25.79           C  
-ATOM  15931  N   GLU D 591     -22.101 -32.002-145.392  1.00 19.50           N  
-ATOM  15932  CA  GLU D 591     -21.214 -33.048-144.900  1.00 16.91           C  
-ATOM  15933  C   GLU D 591     -19.789 -32.546-144.688  1.00 21.70           C  
-ATOM  15934  O   GLU D 591     -18.886 -33.330-144.393  1.00 21.24           O  
-ATOM  15935  CB  GLU D 591     -21.204 -34.230-145.872  1.00 19.63           C  
-ATOM  15936  CG  GLU D 591     -22.580 -34.642-146.373  1.00 28.12           C  
-ATOM  15937  CD  GLU D 591     -23.465 -35.211-145.279  1.00 31.40           C  
-ATOM  15938  OE1 GLU D 591     -24.698 -35.032-145.365  1.00 26.62           O  
-ATOM  15939  OE2 GLU D 591     -22.930 -35.845-144.342  1.00 31.04           O  
-ATOM  15940  N   ASP D 592     -19.585 -31.241-144.839  1.00 23.24           N  
-ATOM  15941  CA  ASP D 592     -18.250 -30.668-144.702  1.00 20.64           C  
-ATOM  15942  C   ASP D 592     -18.030 -30.022-143.339  1.00 18.66           C  
-ATOM  15943  O   ASP D 592     -17.220 -29.106-143.202  1.00 16.75           O  
-ATOM  15944  CB  ASP D 592     -18.000 -29.638-145.803  1.00 16.39           C  
-ATOM  15945  CG  ASP D 592     -18.175 -30.216-147.186  1.00 20.79           C  
-ATOM  15946  OD1 ASP D 592     -17.374 -31.094-147.571  1.00 25.39           O  
-ATOM  15947  OD2 ASP D 592     -19.108 -29.788-147.893  1.00 29.91           O  
-ATOM  15948  N   PHE D 593     -18.750 -30.502-142.332  1.00 19.28           N  
-ATOM  15949  CA  PHE D 593     -18.637 -29.949-140.989  1.00 18.26           C  
-ATOM  15950  C   PHE D 593     -18.651 -31.035-139.930  1.00 18.17           C  
-ATOM  15951  O   PHE D 593     -19.383 -32.018-140.048  1.00 26.76           O  
-ATOM  15952  CB  PHE D 593     -19.774 -28.964-140.708  1.00 16.48           C  
-ATOM  15953  CG  PHE D 593     -19.811 -27.791-141.640  1.00 16.47           C  
-ATOM  15954  CD1 PHE D 593     -19.064 -26.656-141.377  1.00 17.76           C  
-ATOM  15955  CD2 PHE D 593     -20.605 -27.819-142.773  1.00 15.20           C  
-ATOM  15956  CE1 PHE D 593     -19.103 -25.572-142.234  1.00 18.08           C  
-ATOM  15957  CE2 PHE D 593     -20.647 -26.740-143.633  1.00 16.25           C  
-ATOM  15958  CZ  PHE D 593     -19.898 -25.614-143.363  1.00 17.88           C  
-ATOM  15959  N   GLU D 594     -17.839 -30.854-138.895  1.00 18.01           N  
-ATOM  15960  CA  GLU D 594     -17.967 -31.675-137.701  1.00 17.81           C  
-ATOM  15961  C   GLU D 594     -18.062 -30.779-136.474  1.00 16.03           C  
-ATOM  15962  O   GLU D 594     -17.317 -29.805-136.334  1.00 13.58           O  
-ATOM  15963  CB  GLU D 594     -16.804 -32.664-137.568  1.00 20.41           C  
-ATOM  15964  CG  GLU D 594     -15.438 -32.052-137.293  1.00 28.78           C  
-ATOM  15965  CD  GLU D 594     -14.390 -33.106-136.976  1.00 34.35           C  
-ATOM  15966  OE1 GLU D 594     -13.183 -32.776-136.976  1.00 19.72           O  
-ATOM  15967  OE2 GLU D 594     -14.781 -34.268-136.725  1.00 23.68           O  
-ATOM  15968  N   VAL D 595     -19.015 -31.096-135.607  1.00 15.79           N  
-ATOM  15969  CA  VAL D 595     -19.162 -30.387-134.347  1.00 11.08           C  
-ATOM  15970  C   VAL D 595     -18.491 -31.201-133.259  1.00 12.73           C  
-ATOM  15971  O   VAL D 595     -18.925 -32.303-132.935  1.00 17.85           O  
-ATOM  15972  CB  VAL D 595     -20.629 -30.142-133.990  1.00 12.52           C  
-ATOM  15973  CG1 VAL D 595     -20.732 -29.582-132.585  1.00 21.58           C  
-ATOM  15974  CG2 VAL D 595     -21.262 -29.197-134.998  1.00 11.93           C  
-ATOM  15975  N   VAL D 596     -17.424 -30.647-132.700  1.00 16.89           N  
-ATOM  15976  CA  VAL D 596     -16.529 -31.400-131.837  1.00 15.47           C  
-ATOM  15977  C   VAL D 596     -16.567 -30.903-130.393  1.00 24.42           C  
-ATOM  15978  O   VAL D 596     -16.301 -29.729-130.118  1.00 28.13           O  
-ATOM  15979  CB  VAL D 596     -15.082 -31.335-132.379  1.00 11.26           C  
-ATOM  15980  CG1 VAL D 596     -14.076 -31.595-131.285  1.00 18.13           C  
-ATOM  15981  CG2 VAL D 596     -14.903 -32.314-133.528  1.00 10.55           C  
-ATOM  15982  N   GLY D 597     -16.908 -31.808-129.478  1.00 17.43           N  
-ATOM  15983  CA  GLY D 597     -16.906 -31.512-128.057  1.00 18.59           C  
-ATOM  15984  C   GLY D 597     -18.180 -30.858-127.556  1.00 23.66           C  
-ATOM  15985  O   GLY D 597     -18.168 -30.157-126.544  1.00 26.58           O  
-ATOM  15986  N   TYR D 598     -19.285 -31.089-128.257  1.00 23.64           N  
-ATOM  15987  CA  TYR D 598     -20.559 -30.486-127.881  1.00 23.21           C  
-ATOM  15988  C   TYR D 598     -21.265 -31.310-126.812  1.00 19.96           C  
-ATOM  15989  O   TYR D 598     -21.830 -32.363-127.104  1.00 18.72           O  
-ATOM  15990  CB  TYR D 598     -21.455 -30.331-129.111  1.00 24.39           C  
-ATOM  15991  CG  TYR D 598     -22.677 -29.467-128.895  1.00 18.18           C  
-ATOM  15992  CD1 TYR D 598     -22.598 -28.285-128.169  1.00 21.98           C  
-ATOM  15993  CD2 TYR D 598     -23.905 -29.822-129.439  1.00 17.28           C  
-ATOM  15994  CE1 TYR D 598     -23.712 -27.487-127.979  1.00 22.56           C  
-ATOM  15995  CE2 TYR D 598     -25.024 -29.032-129.254  1.00 19.41           C  
-ATOM  15996  CZ  TYR D 598     -24.922 -27.865-128.524  1.00 23.86           C  
-ATOM  15997  OH  TYR D 598     -26.033 -27.072-128.336  1.00 18.22           O  
-ATOM  15998  N   VAL D 599     -21.223 -30.826-125.574  1.00 21.18           N  
-ATOM  15999  CA  VAL D 599     -21.882 -31.497-124.457  1.00 20.35           C  
-ATOM  16000  C   VAL D 599     -22.895 -30.565-123.787  1.00 24.53           C  
-ATOM  16001  O   VAL D 599     -22.589 -29.932-122.778  1.00 27.58           O  
-ATOM  16002  CB  VAL D 599     -20.861 -31.980-123.404  1.00 17.73           C  
-ATOM  16003  CG1 VAL D 599     -21.532 -32.902-122.393  1.00 28.56           C  
-ATOM  16004  CG2 VAL D 599     -19.698 -32.688-124.076  1.00 18.29           C  
-ATOM  16005  N   PRO D 600     -24.108 -30.473-124.355  1.00 22.67           N  
-ATOM  16006  CA  PRO D 600     -25.141 -29.567-123.848  1.00 23.81           C  
-ATOM  16007  C   PRO D 600     -26.094 -30.220-122.852  1.00 29.45           C  
-ATOM  16008  O   PRO D 600     -26.070 -31.439-122.675  1.00 31.04           O  
-ATOM  16009  CB  PRO D 600     -25.893 -29.179-125.116  1.00 20.77           C  
-ATOM  16010  CG  PRO D 600     -25.839 -30.426-125.943  1.00 20.15           C  
-ATOM  16011  CD  PRO D 600     -24.519 -31.102-125.623  1.00 22.48           C  
-ATOM  16012  N   HIS D 601     -26.926 -29.408-122.209  1.00 26.42           N  
-ATOM  16013  CA  HIS D 601     -27.996 -29.937-121.377  1.00 27.42           C  
-ATOM  16014  C   HIS D 601     -29.113 -30.442-122.278  1.00 33.04           C  
-ATOM  16015  O   HIS D 601     -29.046 -30.299-123.499  1.00 34.95           O  
-ATOM  16016  CB  HIS D 601     -28.522 -28.876-120.410  1.00 27.69           C  
-ATOM  16017  CG  HIS D 601     -27.527 -28.451-119.376  1.00 26.23           C  
-ATOM  16018  ND1 HIS D 601     -27.393 -29.093-118.164  1.00 31.09           N  
-ATOM  16019  CD2 HIS D 601     -26.618 -27.447-119.373  1.00 27.25           C  
-ATOM  16020  CE1 HIS D 601     -26.444 -28.503-117.459  1.00 30.08           C  
-ATOM  16021  NE2 HIS D 601     -25.958 -27.502-118.170  1.00 21.90           N  
-ATOM  16022  N   GLY D 602     -30.141 -31.030-121.675  1.00 32.68           N  
-ATOM  16023  CA  GLY D 602     -31.242 -31.594-122.434  1.00 49.42           C  
-ATOM  16024  C   GLY D 602     -32.039 -30.551-123.195  1.00 48.05           C  
-ATOM  16025  O   GLY D 602     -32.004 -29.367-122.861  1.00 42.00           O  
-ATOM  16026  N   ARG D 603     -32.759 -30.994-124.222  1.00 47.76           N  
-ATOM  16027  CA  ARG D 603     -33.598 -30.098-125.011  1.00 39.97           C  
-ATOM  16028  C   ARG D 603     -34.713 -29.513-124.154  1.00 39.15           C  
-ATOM  16029  O   ARG D 603     -35.344 -30.228-123.376  1.00 36.69           O  
-ATOM  16030  CB  ARG D 603     -34.198 -30.833-126.212  1.00 48.84           C  
-ATOM  16031  CG  ARG D 603     -33.219 -31.717-126.968  1.00 61.86           C  
-ATOM  16032  CD  ARG D 603     -33.840 -32.258-128.246  1.00 56.67           C  
-ATOM  16033  NE  ARG D 603     -33.701 -31.323-129.361  1.00 85.29           N  
-ATOM  16034  CZ  ARG D 603     -32.933 -31.539-130.426  1.00 84.28           C  
-ATOM  16035  NH1 ARG D 603     -32.863 -30.631-131.393  1.00 49.97           N  
-ATOM  16036  NH2 ARG D 603     -32.241 -32.667-130.530  1.00 79.42           N  
-ATOM  16037  N   ILE D 604     -34.948 -28.212-124.293  1.00 42.85           N  
-ATOM  16038  CA  ILE D 604     -36.068 -27.568-123.618  1.00 44.26           C  
-ATOM  16039  C   ILE D 604     -37.133 -27.176-124.635  1.00 44.49           C  
-ATOM  16040  O   ILE D 604     -36.911 -26.307-125.478  1.00 43.71           O  
-ATOM  16041  CB  ILE D 604     -35.634 -26.321-122.832  1.00 45.92           C  
-ATOM  16042  CG1 ILE D 604     -34.495 -26.658-121.869  1.00 45.83           C  
-ATOM  16043  CG2 ILE D 604     -36.820 -25.739-122.077  1.00 47.19           C  
-ATOM  16044  CD1 ILE D 604     -34.051 -25.483-121.022  1.00 33.75           C  
-ATOM  16045  N   GLN D 605     -38.292 -27.818-124.542  1.00 48.64           N  
-ATOM  16046  CA  GLN D 605     -39.345 -27.657-125.538  1.00 59.95           C  
-ATOM  16047  C   GLN D 605     -40.045 -26.304-125.433  1.00 58.01           C  
-ATOM  16048  O   GLN D 605     -40.528 -25.921-124.366  1.00 44.71           O  
-ATOM  16049  CB  GLN D 605     -40.368 -28.789-125.407  1.00 59.95           C  
-ATOM  16050  CG  GLN D 605     -41.119 -29.110-126.692  1.00 63.12           C  
-ATOM  16051  CD  GLN D 605     -42.478 -28.442-126.765  1.00 63.89           C  
-ATOM  16052  OE1 GLN D 605     -43.085 -28.128-125.740  1.00 53.20           O  
-ATOM  16053  NE2 GLN D 605     -42.966 -28.226-127.983  1.00 51.61           N  
-ATOM  16054  N   MET D 606     -40.086 -25.585-126.552  1.00 56.01           N  
-ATOM  16055  CA  MET D 606     -40.788 -24.306-126.638  1.00 60.93           C  
-ATOM  16056  C   MET D 606     -41.549 -24.198-127.957  1.00 58.08           C  
-ATOM  16057  O   MET D 606     -40.955 -24.279-129.033  1.00 57.79           O  
-ATOM  16058  CB  MET D 606     -39.812 -23.136-126.505  1.00 61.89           C  
-ATOM  16059  CG  MET D 606     -39.033 -23.110-125.204  1.00 53.18           C  
-ATOM  16060  SD  MET D 606     -37.832 -21.770-125.155  1.00 47.34           S  
-ATOM  16061  CE  MET D 606     -36.671 -22.414-123.952  1.00 41.04           C  
-ATOM  16062  N   GLU D 607     -42.862 -24.010-127.870  1.00 53.17           N  
-ATOM  16063  CA  GLU D 607     -43.699 -23.922-129.061  1.00 63.26           C  
-ATOM  16064  C   GLU D 607     -43.520 -22.585-129.770  1.00 62.89           C  
-ATOM  16065  O   GLU D 607     -43.375 -21.541-129.133  1.00 55.45           O  
-ATOM  16066  CB  GLU D 607     -45.176 -24.138-128.709  1.00 67.04           C  
-ATOM  16067  CG  GLU D 607     -45.751 -23.142-127.712  1.00 78.56           C  
-ATOM  16068  CD  GLU D 607     -45.354 -23.447-126.278  1.00 97.15           C  
-ATOM  16069  OE1 GLU D 607     -46.214 -23.935-125.512  1.00 98.56           O  
-ATOM  16070  OE2 GLU D 607     -44.182 -23.200-125.919  1.00 85.63           O  
-ATOM  16071  N   MET D 608     -43.533 -22.631-131.097  1.00 71.72           N  
-ATOM  16072  CA  MET D 608     -43.336 -21.440-131.911  1.00 60.75           C  
-ATOM  16073  C   MET D 608     -44.625 -20.639-132.041  1.00 50.26           C  
-ATOM  16074  O   MET D 608     -45.638 -21.148-132.521  1.00 41.17           O  
-ATOM  16075  CB  MET D 608     -42.817 -21.823-133.300  1.00 61.75           C  
-ATOM  16076  CG  MET D 608     -42.277 -20.656-134.110  1.00 65.11           C  
-ATOM  16077  SD  MET D 608     -42.869 -20.633-135.816  1.00 61.64           S  
-ATOM  16078  CE  MET D 608     -42.519 -22.307-136.344  1.00 57.16           C  
-ATOM  16079  N   ALA D 609     -44.582 -19.384-131.608  1.00 56.41           N  
-ATOM  16080  CA  ALA D 609     -45.705 -18.479-131.805  1.00 58.18           C  
-ATOM  16081  C   ALA D 609     -45.852 -18.168-133.291  1.00 60.92           C  
-ATOM  16082  O   ALA D 609     -45.079 -17.390-133.852  1.00 65.73           O  
-ATOM  16083  CB  ALA D 609     -45.514 -17.203-131.002  1.00 44.66           C  
-ATOM  16084  N   VAL D 610     -46.843 -18.788-133.922  1.00 61.22           N  
-ATOM  16085  CA  VAL D 610     -47.032 -18.665-135.363  1.00 69.53           C  
-ATOM  16086  C   VAL D 610     -47.471 -17.256-135.750  1.00 63.73           C  
-ATOM  16087  O   VAL D 610     -46.904 -16.651-136.662  1.00 64.11           O  
-ATOM  16088  CB  VAL D 610     -48.070 -19.682-135.881  1.00 62.58           C  
-ATOM  16089  CG1 VAL D 610     -48.188 -19.601-137.396  1.00 50.55           C  
-ATOM  16090  CG2 VAL D 610     -47.688 -21.090-135.451  1.00 49.31           C  
-ATOM  16091  OXT VAL D 610     -48.390 -16.690-135.156  1.00 47.17           O  
-TER   16092      VAL D 610                                                      
-ATOM  16093  N   PRO E   4      13.227 -92.666 -85.106  1.00 52.20           N  
-ATOM  16094  CA  PRO E   4      12.933 -92.227 -83.738  1.00 51.43           C  
-ATOM  16095  C   PRO E   4      11.492 -92.531 -83.331  1.00 56.13           C  
-ATOM  16096  O   PRO E   4      10.551 -92.035 -83.956  1.00 58.04           O  
-ATOM  16097  CB  PRO E   4      13.185 -90.718 -83.799  1.00 46.36           C  
-ATOM  16098  CG  PRO E   4      13.009 -90.345 -85.275  1.00 64.53           C  
-ATOM  16099  CD  PRO E   4      12.910 -91.617 -86.089  1.00 43.43           C  
-ATOM  16100  N   VAL E   5      11.325 -93.337 -82.287  1.00 45.02           N  
-ATOM  16101  CA  VAL E   5       9.998 -93.792 -81.889  1.00 44.18           C  
-ATOM  16102  C   VAL E   5       9.677 -93.426 -80.436  1.00 39.70           C  
-ATOM  16103  O   VAL E   5      10.575 -93.248 -79.612  1.00 39.46           O  
-ATOM  16104  CB  VAL E   5       9.859 -95.325 -82.087  1.00 32.73           C  
-ATOM  16105  CG1 VAL E   5      10.320 -96.082 -80.856  1.00 35.27           C  
-ATOM  16106  CG2 VAL E   5       8.431 -95.690 -82.416  1.00 40.75           C  
-ATOM  16107  N   CYS E   6       8.388 -93.293 -80.135  1.00 31.08           N  
-ATOM  16108  CA  CYS E   6       7.940 -93.010 -78.774  1.00 30.95           C  
-ATOM  16109  C   CYS E   6       6.958 -94.067 -78.285  1.00 35.79           C  
-ATOM  16110  O   CYS E   6       5.983 -94.365 -78.957  1.00 40.89           O  
-ATOM  16111  CB  CYS E   6       7.294 -91.623 -78.695  1.00 34.16           C  
-ATOM  16112  SG  CYS E   6       8.451 -90.232 -78.755  1.00 57.18           S  
-ATOM  16113  N   LEU E   7       7.215 -94.629 -77.109  1.00 35.32           N  
-ATOM  16114  CA  LEU E   7       6.302 -95.598 -76.506  1.00 24.50           C  
-ATOM  16115  C   LEU E   7       5.284 -94.878 -75.630  1.00 28.16           C  
-ATOM  16116  O   LEU E   7       5.624 -93.896 -74.972  1.00 35.97           O  
-ATOM  16117  CB  LEU E   7       7.070 -96.628 -75.674  1.00 22.10           C  
-ATOM  16118  CG  LEU E   7       7.668 -97.870 -76.342  1.00 31.21           C  
-ATOM  16119  CD1 LEU E   7       8.558 -97.517 -77.525  1.00 40.57           C  
-ATOM  16120  CD2 LEU E   7       8.444 -98.693 -75.320  1.00 24.50           C  
-ATOM  16121  N   VAL E   8       4.040 -95.350 -75.618  1.00 25.06           N  
-ATOM  16122  CA  VAL E   8       3.044 -94.751 -74.723  1.00 24.55           C  
-ATOM  16123  C   VAL E   8       2.248 -95.812 -73.948  1.00 25.57           C  
-ATOM  16124  O   VAL E   8       1.648 -96.714 -74.538  1.00 20.04           O  
-ATOM  16125  CB  VAL E   8       2.077 -93.820 -75.500  1.00  9.79           C  
-ATOM  16126  CG1 VAL E   8       1.841 -94.337 -76.903  1.00 24.06           C  
-ATOM  16127  CG2 VAL E   8       0.766 -93.641 -74.742  1.00 15.50           C  
-ATOM  16128  N   VAL E   9       2.253 -95.692 -72.619  1.00 26.23           N  
-ATOM  16129  CA  VAL E   9       1.712 -96.727 -71.735  1.00 18.60           C  
-ATOM  16130  C   VAL E   9       0.870 -96.212 -70.577  1.00 20.21           C  
-ATOM  16131  O   VAL E   9       0.993 -95.063 -70.157  1.00 30.12           O  
-ATOM  16132  CB  VAL E   9       2.840 -97.568 -71.101  1.00 19.92           C  
-ATOM  16133  CG1 VAL E   9       3.034 -98.864 -71.846  1.00 27.77           C  
-ATOM  16134  CG2 VAL E   9       4.133 -96.765 -71.036  1.00 24.78           C  
-ATOM  16135  N   ALA E  10       0.017 -97.092 -70.064  1.00 19.20           N  
-ATOM  16136  CA  ALA E  10      -0.592 -96.926 -68.752  1.00 20.14           C  
-ATOM  16137  C   ALA E  10      -0.200 -98.155 -67.936  1.00 23.21           C  
-ATOM  16138  O   ALA E  10      -0.211 -99.272 -68.455  1.00 24.15           O  
-ATOM  16139  CB  ALA E  10      -2.095 -96.779 -68.855  1.00 24.49           C  
-ATOM  16140  N   MET E  11       0.152 -97.960 -66.668  1.00 21.57           N  
-ATOM  16141  CA  MET E  11       0.930 -98.973 -65.964  1.00 14.72           C  
-ATOM  16142  C   MET E  11       0.740 -98.991 -64.443  1.00 22.99           C  
-ATOM  16143  O   MET E  11       0.714 -97.943 -63.792  1.00 30.27           O  
-ATOM  16144  CB  MET E  11       2.405 -98.756 -66.291  1.00 15.50           C  
-ATOM  16145  CG  MET E  11       3.297 -99.941 -66.062  1.00 21.25           C  
-ATOM  16146  SD  MET E  11       5.007 -99.497 -66.411  1.00 26.53           S  
-ATOM  16147  CE  MET E  11       4.853 -98.779 -68.044  1.00 15.37           C  
-ATOM  16148  N   THR E  12       0.620-100.192 -63.882  1.00 15.96           N  
-ATOM  16149  CA  THR E  12       0.546-100.371 -62.433  1.00 18.80           C  
-ATOM  16150  C   THR E  12       1.955-100.271 -61.835  1.00 24.78           C  
-ATOM  16151  O   THR E  12       2.933-100.266 -62.582  1.00 27.35           O  
-ATOM  16152  CB  THR E  12      -0.093-101.726 -62.073  1.00 16.33           C  
-ATOM  16153  OG1 THR E  12       0.720-102.787 -62.582  1.00 23.19           O  
-ATOM  16154  CG2 THR E  12      -1.489-101.830 -62.665  1.00 15.70           C  
-ATOM  16155  N   PRO E  13       2.072-100.171 -60.494  1.00 23.19           N  
-ATOM  16156  CA  PRO E  13       3.426-100.110 -59.924  1.00 18.62           C  
-ATOM  16157  C   PRO E  13       4.253-101.362 -60.194  1.00 15.75           C  
-ATOM  16158  O   PRO E  13       5.481-101.292 -60.188  1.00 17.05           O  
-ATOM  16159  CB  PRO E  13       3.169 -99.955 -58.422  1.00 20.50           C  
-ATOM  16160  CG  PRO E  13       1.837 -99.324 -58.338  1.00 23.53           C  
-ATOM  16161  CD  PRO E  13       1.046 -99.913 -59.468  1.00 18.94           C  
-ATOM  16162  N   LYS E  14       3.587-102.488 -60.423  1.00 19.71           N  
-ATOM  16163  CA  LYS E  14       4.280-103.732 -60.737  1.00 26.22           C  
-ATOM  16164  C   LYS E  14       4.269-103.992 -62.242  1.00 23.29           C  
-ATOM  16165  O   LYS E  14       4.302-105.139 -62.689  1.00 20.30           O  
-ATOM  16166  CB  LYS E  14       3.656-104.898 -59.966  1.00 10.94           C  
-ATOM  16167  CG  LYS E  14       4.089-104.928 -58.506  1.00 18.25           C  
-ATOM  16168  CD  LYS E  14       3.023-105.506 -57.586  1.00 33.02           C  
-ATOM  16169  CE  LYS E  14       2.922-107.017 -57.707  1.00 37.05           C  
-ATOM  16170  NZ  LYS E  14       1.971-107.579 -56.708  1.00 27.26           N  
-ATOM  16171  N   ARG E  15       4.216-102.901 -63.004  1.00 20.90           N  
-ATOM  16172  CA  ARG E  15       4.350-102.912 -64.460  1.00 16.38           C  
-ATOM  16173  C   ARG E  15       3.252-103.685 -65.189  1.00 20.32           C  
-ATOM  16174  O   ARG E  15       3.419-104.055 -66.351  1.00 21.28           O  
-ATOM  16175  CB  ARG E  15       5.723-103.465 -64.857  1.00 17.89           C  
-ATOM  16176  CG  ARG E  15       6.862-102.510 -64.551  1.00 18.32           C  
-ATOM  16177  CD  ARG E  15       8.210-103.043 -65.016  1.00 23.95           C  
-ATOM  16178  NE  ARG E  15       8.744-104.062 -64.116  1.00 25.08           N  
-ATOM  16179  CZ  ARG E  15       8.779-105.363 -64.390  1.00 31.92           C  
-ATOM  16180  NH1 ARG E  15       9.285-106.212 -63.506  1.00 33.96           N  
-ATOM  16181  NH2 ARG E  15       8.316-105.816 -65.548  1.00 27.41           N  
-ATOM  16182  N   GLY E  16       2.126-103.907 -64.517  1.00 17.81           N  
-ATOM  16183  CA  GLY E  16       0.993-104.577 -65.133  1.00 16.01           C  
-ATOM  16184  C   GLY E  16       0.235-103.646 -66.057  1.00 17.68           C  
-ATOM  16185  O   GLY E  16      -0.014-102.492 -65.710  1.00 20.46           O  
-ATOM  16186  N   ILE E  17      -0.132-104.138 -67.236  1.00 19.15           N  
-ATOM  16187  CA  ILE E  17      -0.789-103.293 -68.229  1.00 22.56           C  
-ATOM  16188  C   ILE E  17      -2.120-103.853 -68.734  1.00 23.46           C  
-ATOM  16189  O   ILE E  17      -2.927-103.115 -69.302  1.00 19.80           O  
-ATOM  16190  CB  ILE E  17       0.120-103.050 -69.455  1.00 20.88           C  
-ATOM  16191  CG1 ILE E  17       0.340-104.349 -70.228  1.00 16.98           C  
-ATOM  16192  CG2 ILE E  17       1.448-102.432 -69.036  1.00 16.59           C  
-ATOM  16193  CD1 ILE E  17       1.099-104.156 -71.519  1.00 22.53           C  
-ATOM  16194  N   GLY E  18      -2.353-105.147 -68.535  1.00 25.15           N  
-ATOM  16195  CA  GLY E  18      -3.571-105.762 -69.034  1.00 26.02           C  
-ATOM  16196  C   GLY E  18      -3.991-107.060 -68.370  1.00 24.89           C  
-ATOM  16197  O   GLY E  18      -3.192-107.719 -67.703  1.00 22.19           O  
-ATOM  16198  N   ILE E  19      -5.259-107.420 -68.556  1.00 24.30           N  
-ATOM  16199  CA  ILE E  19      -5.781-108.705 -68.100  1.00 23.39           C  
-ATOM  16200  C   ILE E  19      -6.948-109.158 -68.984  1.00 30.41           C  
-ATOM  16201  O   ILE E  19      -7.833-108.363 -69.317  1.00 34.68           O  
-ATOM  16202  CB  ILE E  19      -6.224-108.645 -66.623  1.00 13.39           C  
-ATOM  16203  CG1 ILE E  19      -6.736-110.008 -66.160  1.00 12.80           C  
-ATOM  16204  CG2 ILE E  19      -7.276-107.571 -66.414  1.00 16.15           C  
-ATOM  16205  CD1 ILE E  19      -6.265-110.386 -64.784  1.00 19.55           C  
-ATOM  16206  N   ASN E  20      -6.928-110.433 -69.375  1.00 19.78           N  
-ATOM  16207  CA  ASN E  20      -7.940-111.009 -70.262  1.00 21.64           C  
-ATOM  16208  C   ASN E  20      -8.131-110.207 -71.541  1.00 22.10           C  
-ATOM  16209  O   ASN E  20      -9.260-109.983 -71.978  1.00 18.05           O  
-ATOM  16210  CB  ASN E  20      -9.283-111.140 -69.539  1.00 17.54           C  
-ATOM  16211  CG  ASN E  20      -9.411-112.442 -68.782  1.00 33.04           C  
-ATOM  16212  OD1 ASN E  20      -8.978-113.494 -69.253  1.00 41.97           O  
-ATOM  16213  ND2 ASN E  20     -10.005-112.380 -67.596  1.00 55.41           N  
-ATOM  16214  N   ASN E  21      -7.017-109.780 -72.128  1.00 23.30           N  
-ATOM  16215  CA  ASN E  21      -7.028-108.977 -73.345  1.00 23.64           C  
-ATOM  16216  C   ASN E  21      -7.868-107.714 -73.164  1.00 21.84           C  
-ATOM  16217  O   ASN E  21      -8.546-107.259 -74.086  1.00 31.52           O  
-ATOM  16218  CB  ASN E  21      -7.540-109.805 -74.524  1.00 25.96           C  
-ATOM  16219  CG  ASN E  21      -7.092-109.255 -75.861  1.00 35.58           C  
-ATOM  16220  OD1 ASN E  21      -5.897-109.126 -76.121  1.00 33.23           O  
-ATOM  16221  ND2 ASN E  21      -8.052-108.939 -76.725  1.00 40.16           N  
-ATOM  16222  N   GLY E  22      -7.817-107.155 -71.961  1.00 19.30           N  
-ATOM  16223  CA  GLY E  22      -8.519-105.925 -71.646  1.00 16.87           C  
-ATOM  16224  C   GLY E  22      -7.722-105.127 -70.636  1.00 17.25           C  
-ATOM  16225  O   GLY E  22      -6.615-105.518 -70.269  1.00 20.32           O  
-ATOM  16226  N   LEU E  23      -8.276-104.010 -70.182  1.00 14.80           N  
-ATOM  16227  CA  LEU E  23      -7.585-103.173 -69.209  1.00 16.21           C  
-ATOM  16228  C   LEU E  23      -7.895-103.612 -67.777  1.00 17.26           C  
-ATOM  16229  O   LEU E  23      -9.023-103.998 -67.468  1.00 15.17           O  
-ATOM  16230  CB  LEU E  23      -7.958-101.704 -69.412  1.00 20.35           C  
-ATOM  16231  CG  LEU E  23      -7.568-101.122 -70.771  1.00 14.39           C  
-ATOM  16232  CD1 LEU E  23      -8.014 -99.673 -70.883  1.00 22.81           C  
-ATOM  16233  CD2 LEU E  23      -6.070-101.246 -70.989  1.00 17.06           C  
-ATOM  16234  N   PRO E  24      -6.883-103.557 -66.899  1.00 16.40           N  
-ATOM  16235  CA  PRO E  24      -6.981-104.017 -65.508  1.00 17.93           C  
-ATOM  16236  C   PRO E  24      -7.860-103.129 -64.631  1.00 25.15           C  
-ATOM  16237  O   PRO E  24      -8.404-103.599 -63.632  1.00 26.39           O  
-ATOM  16238  CB  PRO E  24      -5.526-103.968 -65.018  1.00 16.57           C  
-ATOM  16239  CG  PRO E  24      -4.690-103.849 -66.246  1.00 16.03           C  
-ATOM  16240  CD  PRO E  24      -5.522-103.107 -67.228  1.00 15.31           C  
-ATOM  16241  N   TRP E  25      -7.991-101.862 -65.010  1.00 24.93           N  
-ATOM  16242  CA  TRP E  25      -8.656-100.862 -64.182  1.00 18.08           C  
-ATOM  16243  C   TRP E  25      -9.969-100.375 -64.797  1.00 24.75           C  
-ATOM  16244  O   TRP E  25     -10.238-100.627 -65.973  1.00 19.62           O  
-ATOM  16245  CB  TRP E  25      -7.712 -99.680 -63.964  1.00 12.40           C  
-ATOM  16246  CG  TRP E  25      -7.015 -99.273 -65.221  1.00 17.17           C  
-ATOM  16247  CD1 TRP E  25      -7.534 -98.536 -66.244  1.00 17.58           C  
-ATOM  16248  CD2 TRP E  25      -5.671 -99.594 -65.599  1.00 19.61           C  
-ATOM  16249  NE1 TRP E  25      -6.596 -98.373 -67.235  1.00 15.04           N  
-ATOM  16250  CE2 TRP E  25      -5.443 -99.012 -66.861  1.00 14.48           C  
-ATOM  16251  CE3 TRP E  25      -4.637-100.313 -64.990  1.00 18.14           C  
-ATOM  16252  CZ2 TRP E  25      -4.227 -99.129 -67.526  1.00 12.84           C  
-ATOM  16253  CZ3 TRP E  25      -3.428-100.425 -65.652  1.00 12.81           C  
-ATOM  16254  CH2 TRP E  25      -3.234 -99.836 -66.906  1.00 12.81           C  
-ATOM  16255  N   PRO E  26     -10.800 -99.683 -63.997  1.00 23.43           N  
-ATOM  16256  CA  PRO E  26     -11.948 -98.961 -64.557  1.00 24.23           C  
-ATOM  16257  C   PRO E  26     -11.506 -97.866 -65.531  1.00 33.91           C  
-ATOM  16258  O   PRO E  26     -10.313 -97.565 -65.618  1.00 33.29           O  
-ATOM  16259  CB  PRO E  26     -12.634 -98.366 -63.322  1.00 18.55           C  
-ATOM  16260  CG  PRO E  26     -11.622 -98.455 -62.222  1.00 16.09           C  
-ATOM  16261  CD  PRO E  26     -10.811 -99.666 -62.525  1.00 15.99           C  
-ATOM  16262  N  AHIS E  27     -12.454 -97.282 -66.254  0.31 46.98           N  
-ATOM  16263  N  BHIS E  27     -12.461 -97.285 -66.248  0.69 48.01           N  
-ATOM  16264  CA AHIS E  27     -12.120 -96.334 -67.314  0.31 38.28           C  
-ATOM  16265  CA BHIS E  27     -12.158 -96.298 -67.281  0.69 37.25           C  
-ATOM  16266  C  AHIS E  27     -11.504 -95.057 -66.745  0.31 41.58           C  
-ATOM  16267  C  BHIS E  27     -11.480 -95.064 -66.700  0.69 43.36           C  
-ATOM  16268  O  AHIS E  27     -12.054 -94.433 -65.836  0.31 34.86           O  
-ATOM  16269  O  BHIS E  27     -11.976 -94.464 -65.744  0.69 34.50           O  
-ATOM  16270  CB AHIS E  27     -13.360 -96.008 -68.161  0.31 34.21           C  
-ATOM  16271  CB BHIS E  27     -13.434 -95.892 -68.022  0.69 33.78           C  
-ATOM  16272  CG AHIS E  27     -14.393 -95.194 -67.448  0.31 39.81           C  
-ATOM  16273  CG BHIS E  27     -13.185 -95.085 -69.257  0.69 28.15           C  
-ATOM  16274  ND1AHIS E  27     -14.518 -93.833 -67.626  0.31 39.63           N  
-ATOM  16275  ND1BHIS E  27     -12.871 -95.663 -70.468  0.69 28.89           N  
-ATOM  16276  CD2AHIS E  27     -15.352 -95.547 -66.559  0.31 39.85           C  
-ATOM  16277  CD2BHIS E  27     -13.198 -93.749 -69.468  0.69 29.54           C  
-ATOM  16278  CE1AHIS E  27     -15.508 -93.382 -66.876  0.31 37.52           C  
-ATOM  16279  CE1BHIS E  27     -12.705 -94.716 -71.373  0.69 30.26           C  
-ATOM  16280  NE2AHIS E  27     -16.030 -94.402 -66.219  0.31 36.51           N  
-ATOM  16281  NE2BHIS E  27     -12.898 -93.545 -70.794  0.69 28.83           N  
-ATOM  16282  N   LEU E  28     -10.341 -94.692 -67.278  1.00 35.96           N  
-ATOM  16283  CA  LEU E  28      -9.630 -93.493 -66.854  1.00 26.14           C  
-ATOM  16284  C   LEU E  28      -9.710 -92.446 -67.957  1.00 31.14           C  
-ATOM  16285  O   LEU E  28      -8.862 -92.383 -68.849  1.00 43.13           O  
-ATOM  16286  CB  LEU E  28      -8.176 -93.813 -66.510  1.00 23.55           C  
-ATOM  16287  CG  LEU E  28      -7.950 -94.997 -65.566  1.00 29.83           C  
-ATOM  16288  CD1 LEU E  28      -6.469 -95.150 -65.245  1.00 23.20           C  
-ATOM  16289  CD2 LEU E  28      -8.767 -94.847 -64.292  1.00 24.26           C  
-ATOM  16290  N   THR E  29     -10.750 -91.626 -67.879  1.00 30.47           N  
-ATOM  16291  CA  THR E  29     -11.084 -90.685 -68.936  1.00 37.27           C  
-ATOM  16292  C   THR E  29      -9.969 -89.676 -69.231  1.00 34.56           C  
-ATOM  16293  O   THR E  29      -9.701 -89.375 -70.395  1.00 34.77           O  
-ATOM  16294  CB  THR E  29     -12.380 -89.922 -68.596  1.00 28.49           C  
-ATOM  16295  OG1 THR E  29     -12.572 -88.863 -69.541  1.00 40.97           O  
-ATOM  16296  CG2 THR E  29     -12.322 -89.342 -67.191  1.00 30.33           C  
-ATOM  16297  N   THR E  30      -9.313 -89.167 -68.192  1.00 21.85           N  
-ATOM  16298  CA  THR E  30      -8.248 -88.193 -68.390  1.00 21.48           C  
-ATOM  16299  C   THR E  30      -7.063 -88.866 -69.064  1.00 23.67           C  
-ATOM  16300  O   THR E  30      -6.385 -88.262 -69.896  1.00 33.16           O  
-ATOM  16301  CB  THR E  30      -7.808 -87.552 -67.063  1.00 23.72           C  
-ATOM  16302  OG1 THR E  30      -8.936 -86.935 -66.429  1.00 25.85           O  
-ATOM  16303  CG2 THR E  30      -6.735 -86.504 -67.301  1.00 23.51           C  
-ATOM  16304  N   ASP E  31      -6.824 -90.124 -68.708  1.00 25.30           N  
-ATOM  16305  CA  ASP E  31      -5.779 -90.908 -69.356  1.00 27.93           C  
-ATOM  16306  C   ASP E  31      -6.093 -91.096 -70.830  1.00 26.92           C  
-ATOM  16307  O   ASP E  31      -5.210 -90.984 -71.677  1.00 31.88           O  
-ATOM  16308  CB  ASP E  31      -5.617 -92.271 -68.686  1.00 31.96           C  
-ATOM  16309  CG  ASP E  31      -4.704 -93.201 -69.466  1.00 38.08           C  
-ATOM  16310  OD1 ASP E  31      -3.590 -92.778 -69.843  1.00 27.82           O  
-ATOM  16311  OD2 ASP E  31      -5.115 -94.354 -69.715  1.00 34.51           O  
-ATOM  16312  N   PHE E  32      -7.355 -91.382 -71.137  1.00 24.93           N  
-ATOM  16313  CA  PHE E  32      -7.757 -91.560 -72.527  1.00 36.64           C  
-ATOM  16314  C   PHE E  32      -7.595 -90.263 -73.312  1.00 34.02           C  
-ATOM  16315  O   PHE E  32      -7.169 -90.277 -74.470  1.00 30.41           O  
-ATOM  16316  CB  PHE E  32      -9.195 -92.069 -72.611  1.00 38.69           C  
-ATOM  16317  CG  PHE E  32      -9.294 -93.565 -72.685  1.00 34.83           C  
-ATOM  16318  CD1 PHE E  32      -9.183 -94.335 -71.541  1.00 40.82           C  
-ATOM  16319  CD2 PHE E  32      -9.480 -94.203 -73.901  1.00 37.48           C  
-ATOM  16320  CE1 PHE E  32      -9.264 -95.716 -71.605  1.00 45.85           C  
-ATOM  16321  CE2 PHE E  32      -9.564 -95.582 -73.969  1.00 42.60           C  
-ATOM  16322  CZ  PHE E  32      -9.455 -96.339 -72.820  1.00 36.70           C  
-ATOM  16323  N   LYS E  33      -7.924 -89.147 -72.671  1.00 33.27           N  
-ATOM  16324  CA  LYS E  33      -7.737 -87.834 -73.272  1.00 35.01           C  
-ATOM  16325  C   LYS E  33      -6.261 -87.618 -73.581  1.00 31.16           C  
-ATOM  16326  O   LYS E  33      -5.900 -87.175 -74.674  1.00 36.93           O  
-ATOM  16327  CB  LYS E  33      -8.264 -86.733 -72.346  1.00 21.43           C  
-ATOM  16328  CG  LYS E  33      -8.304 -85.355 -72.982  1.00 24.71           C  
-ATOM  16329  CD  LYS E  33      -9.205 -84.403 -72.209  1.00 29.98           C  
-ATOM  16330  CE  LYS E  33      -8.669 -84.126 -70.812  1.00 48.63           C  
-ATOM  16331  NZ  LYS E  33      -9.507 -83.129 -70.083  1.00 49.48           N  
-ATOM  16332  N   HIS E  34      -5.417 -87.953 -72.608  1.00 25.41           N  
-ATOM  16333  CA  HIS E  34      -3.966 -87.877 -72.758  1.00 32.71           C  
-ATOM  16334  C   HIS E  34      -3.490 -88.666 -73.972  1.00 31.04           C  
-ATOM  16335  O   HIS E  34      -2.786 -88.133 -74.828  1.00 30.04           O  
-ATOM  16336  CB  HIS E  34      -3.271 -88.389 -71.492  1.00 27.30           C  
-ATOM  16337  CG  HIS E  34      -1.815 -88.685 -71.674  1.00 25.99           C  
-ATOM  16338  ND1 HIS E  34      -0.836 -87.725 -71.541  1.00 32.35           N  
-ATOM  16339  CD2 HIS E  34      -1.172 -89.837 -71.979  1.00 27.35           C  
-ATOM  16340  CE1 HIS E  34       0.347 -88.272 -71.755  1.00 26.33           C  
-ATOM  16341  NE2 HIS E  34       0.171 -89.553 -72.024  1.00 26.65           N  
-ATOM  16342  N   PHE E  35      -3.884 -89.936 -74.038  1.00 34.33           N  
-ATOM  16343  CA  PHE E  35      -3.514 -90.816 -75.147  1.00 33.00           C  
-ATOM  16344  C   PHE E  35      -3.934 -90.221 -76.491  1.00 35.26           C  
-ATOM  16345  O   PHE E  35      -3.119 -90.110 -77.415  1.00 32.97           O  
-ATOM  16346  CB  PHE E  35      -4.142 -92.202 -74.956  1.00 22.41           C  
-ATOM  16347  CG  PHE E  35      -3.879 -93.154 -76.088  1.00 24.17           C  
-ATOM  16348  CD1 PHE E  35      -2.727 -93.921 -76.115  1.00 28.03           C  
-ATOM  16349  CD2 PHE E  35      -4.793 -93.291 -77.121  1.00 29.89           C  
-ATOM  16350  CE1 PHE E  35      -2.486 -94.801 -77.156  1.00 33.81           C  
-ATOM  16351  CE2 PHE E  35      -4.557 -94.169 -78.166  1.00 25.97           C  
-ATOM  16352  CZ  PHE E  35      -3.403 -94.925 -78.183  1.00 25.59           C  
-ATOM  16353  N   SER E  36      -5.206 -89.840 -76.584  1.00 36.15           N  
-ATOM  16354  CA  SER E  36      -5.748 -89.237 -77.796  1.00 31.99           C  
-ATOM  16355  C   SER E  36      -4.928 -88.035 -78.246  1.00 41.53           C  
-ATOM  16356  O   SER E  36      -4.448 -87.995 -79.384  1.00 46.09           O  
-ATOM  16357  CB  SER E  36      -7.198 -88.810 -77.586  1.00 44.49           C  
-ATOM  16358  OG  SER E  36      -7.631 -88.004 -78.672  1.00 43.43           O  
-ATOM  16359  N   ARG E  37      -4.758 -87.065 -77.351  1.00 40.23           N  
-ATOM  16360  CA  ARG E  37      -4.024 -85.854 -77.692  1.00 38.66           C  
-ATOM  16361  C   ARG E  37      -2.589 -86.157 -78.125  1.00 34.94           C  
-ATOM  16362  O   ARG E  37      -2.146 -85.701 -79.179  1.00 42.47           O  
-ATOM  16363  CB  ARG E  37      -4.024 -84.883 -76.514  1.00 40.92           C  
-ATOM  16364  CG  ARG E  37      -4.070 -83.435 -76.951  1.00 56.83           C  
-ATOM  16365  CD  ARG E  37      -5.447 -82.830 -76.718  1.00 61.18           C  
-ATOM  16366  NE  ARG E  37      -6.526 -83.767 -77.017  1.00 59.73           N  
-ATOM  16367  CZ  ARG E  37      -7.802 -83.569 -76.697  1.00 61.41           C  
-ATOM  16368  NH1 ARG E  37      -8.710 -84.481 -77.012  1.00 63.36           N  
-ATOM  16369  NH2 ARG E  37      -8.172 -82.463 -76.061  1.00 38.76           N  
-ATOM  16370  N   VAL E  38      -1.878 -86.938 -77.316  1.00 30.45           N  
-ATOM  16371  CA  VAL E  38      -0.483 -87.275 -77.597  1.00 28.54           C  
-ATOM  16372  C   VAL E  38      -0.312 -87.967 -78.946  1.00 27.59           C  
-ATOM  16373  O   VAL E  38       0.579 -87.612 -79.716  1.00 28.97           O  
-ATOM  16374  CB  VAL E  38       0.117 -88.176 -76.494  1.00 30.09           C  
-ATOM  16375  CG1 VAL E  38       1.457 -88.748 -76.935  1.00 19.68           C  
-ATOM  16376  CG2 VAL E  38       0.274 -87.392 -75.205  1.00 31.42           C  
-ATOM  16377  N   THR E  39      -1.167 -88.941 -79.243  1.00 32.23           N  
-ATOM  16378  CA  THR E  39      -1.027 -89.685 -80.490  1.00 31.89           C  
-ATOM  16379  C   THR E  39      -1.592 -88.944 -81.708  1.00 29.57           C  
-ATOM  16380  O   THR E  39      -1.261 -89.288 -82.843  1.00 28.53           O  
-ATOM  16381  CB  THR E  39      -1.701 -91.074 -80.405  1.00 25.14           C  
-ATOM  16382  OG1 THR E  39      -3.039 -90.939 -79.911  1.00 36.09           O  
-ATOM  16383  CG2 THR E  39      -0.917 -92.002 -79.484  1.00 16.46           C  
-ATOM  16384  N   LYS E  40      -2.431 -87.931 -81.491  1.00 31.50           N  
-ATOM  16385  CA  LYS E  40      -3.052 -87.241 -82.626  1.00 32.38           C  
-ATOM  16386  C   LYS E  40      -2.401 -85.907 -83.007  1.00 34.56           C  
-ATOM  16387  O   LYS E  40      -2.192 -85.643 -84.189  1.00 39.18           O  
-ATOM  16388  CB  LYS E  40      -4.543 -87.014 -82.360  1.00 21.72           C  
-ATOM  16389  CG  LYS E  40      -5.382 -88.269 -82.530  1.00 29.64           C  
-ATOM  16390  CD  LYS E  40      -6.791 -87.967 -83.018  1.00 27.87           C  
-ATOM  16391  CE  LYS E  40      -7.559 -87.113 -82.027  1.00 35.62           C  
-ATOM  16392  NZ  LYS E  40      -8.965 -86.885 -82.465  1.00 44.76           N  
-ATOM  16393  N   THR E  41      -2.079 -85.075 -82.020  1.00 33.75           N  
-ATOM  16394  CA  THR E  41      -1.642 -83.704 -82.292  1.00 37.51           C  
-ATOM  16395  C   THR E  41      -0.378 -83.601 -83.145  1.00 44.86           C  
-ATOM  16396  O   THR E  41       0.679 -84.133 -82.798  1.00 38.29           O  
-ATOM  16397  CB  THR E  41      -1.399 -82.916 -80.988  1.00 52.71           C  
-ATOM  16398  OG1 THR E  41      -0.497 -83.637 -80.138  1.00 50.90           O  
-ATOM  16399  CG2 THR E  41      -2.712 -82.677 -80.253  1.00 41.51           C  
-ATOM  16400  N   THR E  42      -0.516 -82.896 -84.264  1.00 57.17           N  
-ATOM  16401  CA  THR E  42       0.572 -82.648 -85.201  1.00 57.75           C  
-ATOM  16402  C   THR E  42       0.568 -81.168 -85.577  1.00 66.52           C  
-ATOM  16403  O   THR E  42      -0.502 -80.583 -85.757  1.00 60.88           O  
-ATOM  16404  CB  THR E  42       0.427 -83.510 -86.478  1.00 57.56           C  
-ATOM  16405  OG1 THR E  42      -0.002 -84.832 -86.125  1.00 53.89           O  
-ATOM  16406  CG2 THR E  42       1.741 -83.590 -87.243  1.00 59.77           C  
-ATOM  16407  N   PRO E  43       1.758 -80.553 -85.681  1.00 66.90           N  
-ATOM  16408  CA  PRO E  43       1.839 -79.159 -86.134  1.00 77.40           C  
-ATOM  16409  C   PRO E  43       1.233 -78.952 -87.523  1.00 76.72           C  
-ATOM  16410  O   PRO E  43       1.736 -79.514 -88.495  1.00 60.96           O  
-ATOM  16411  CB  PRO E  43       3.348 -78.879 -86.149  1.00 71.75           C  
-ATOM  16412  CG  PRO E  43       4.003 -80.229 -86.102  1.00 74.77           C  
-ATOM  16413  CD  PRO E  43       3.077 -81.077 -85.294  1.00 60.55           C  
-ATOM  16414  N   ALA E  46      -0.786 -80.276 -90.168  1.00 76.07           N  
-ATOM  16415  CA  ALA E  46      -0.930 -79.573 -91.438  1.00 87.09           C  
-ATOM  16416  C   ALA E  46      -0.900 -80.543 -92.612  1.00 77.28           C  
-ATOM  16417  O   ALA E  46      -1.943 -80.946 -93.131  1.00 64.14           O  
-ATOM  16418  CB  ALA E  46       0.165 -78.526 -91.593  1.00 78.20           C  
-ATOM  16419  N   SER E  47       0.306 -80.916 -93.021  1.00 74.35           N  
-ATOM  16420  CA  SER E  47       0.493 -81.800 -94.163  1.00 73.49           C  
-ATOM  16421  C   SER E  47       0.469 -83.273 -93.766  1.00 75.13           C  
-ATOM  16422  O   SER E  47      -0.067 -84.112 -94.493  1.00 55.45           O  
-ATOM  16423  CB  SER E  47       1.815 -81.477 -94.864  1.00 73.66           C  
-ATOM  16424  OG  SER E  47       2.896 -81.476 -93.944  1.00 50.40           O  
-ATOM  16425  N   ARG E  48       1.041 -83.581 -92.605  1.00 77.01           N  
-ATOM  16426  CA  ARG E  48       1.272 -84.965 -92.210  1.00 55.65           C  
-ATOM  16427  C   ARG E  48       0.404 -85.408 -91.038  1.00 53.32           C  
-ATOM  16428  O   ARG E  48      -0.271 -84.597 -90.403  1.00 57.19           O  
-ATOM  16429  CB  ARG E  48       2.749 -85.158 -91.863  1.00 48.82           C  
-ATOM  16430  CG  ARG E  48       3.684 -84.444 -92.823  1.00 59.78           C  
-ATOM  16431  CD  ARG E  48       5.085 -84.315 -92.259  1.00 57.12           C  
-ATOM  16432  NE  ARG E  48       5.834 -85.564 -92.349  1.00 66.03           N  
-ATOM  16433  CZ  ARG E  48       7.109 -85.639 -92.715  1.00 65.03           C  
-ATOM  16434  NH1 ARG E  48       7.774 -84.535 -93.024  1.00 66.85           N  
-ATOM  16435  NH2 ARG E  48       7.720 -86.815 -92.771  1.00 64.02           N  
-ATOM  16436  N   PHE E  74       0.431 -86.709 -90.768  1.00 48.28           N  
-ATOM  16437  CA  PHE E  74      -0.273 -87.287 -89.631  1.00 47.27           C  
-ATOM  16438  C   PHE E  74       0.681 -88.169 -88.834  1.00 46.99           C  
-ATOM  16439  O   PHE E  74       1.829 -88.364 -89.231  1.00 47.71           O  
-ATOM  16440  CB  PHE E  74      -1.489 -88.090 -90.096  1.00 42.68           C  
-ATOM  16441  CG  PHE E  74      -1.227 -88.945 -91.305  1.00 39.39           C  
-ATOM  16442  CD1 PHE E  74      -0.575 -90.160 -91.184  1.00 35.99           C  
-ATOM  16443  CD2 PHE E  74      -1.638 -88.534 -92.562  1.00 48.87           C  
-ATOM  16444  CE1 PHE E  74      -0.335 -90.946 -92.295  1.00 39.47           C  
-ATOM  16445  CE2 PHE E  74      -1.400 -89.317 -93.676  1.00 38.15           C  
-ATOM  16446  CZ  PHE E  74      -0.747 -90.523 -93.542  1.00 40.01           C  
-ATOM  16447  N   ASN E  75       0.211 -88.696 -87.709  1.00 44.32           N  
-ATOM  16448  CA  ASN E  75       1.035 -89.575 -86.886  1.00 40.20           C  
-ATOM  16449  C   ASN E  75       0.727 -91.045 -87.144  1.00 40.14           C  
-ATOM  16450  O   ASN E  75      -0.351 -91.389 -87.633  1.00 40.70           O  
-ATOM  16451  CB  ASN E  75       0.844 -89.253 -85.405  1.00 36.71           C  
-ATOM  16452  CG  ASN E  75       1.468 -87.933 -85.012  1.00 36.09           C  
-ATOM  16453  OD1 ASN E  75       2.583 -87.614 -85.426  1.00 41.27           O  
-ATOM  16454  ND2 ASN E  75       0.751 -87.154 -84.210  1.00 37.01           N  
-ATOM  16455  N   ALA E  76       1.676 -91.914 -86.819  1.00 39.46           N  
-ATOM  16456  CA  ALA E  76       1.459 -93.344 -86.991  1.00 32.70           C  
-ATOM  16457  C   ALA E  76       1.452 -94.053 -85.643  1.00 34.65           C  
-ATOM  16458  O   ALA E  76       2.333 -93.836 -84.819  1.00 29.67           O  
-ATOM  16459  CB  ALA E  76       2.522 -93.941 -87.902  1.00 35.55           C  
-ATOM  16460  N   VAL E  77       0.446 -94.889 -85.417  1.00 36.95           N  
-ATOM  16461  CA  VAL E  77       0.405 -95.720 -84.223  1.00 26.88           C  
-ATOM  16462  C   VAL E  77       0.581 -97.190 -84.599  1.00 31.24           C  
-ATOM  16463  O   VAL E  77      -0.115 -97.719 -85.471  1.00 33.12           O  
-ATOM  16464  CB  VAL E  77      -0.907 -95.529 -83.433  1.00 15.98           C  
-ATOM  16465  CG1 VAL E  77      -0.892 -94.197 -82.708  1.00 24.08           C  
-ATOM  16466  CG2 VAL E  77      -2.112 -95.623 -84.353  1.00 25.42           C  
-ATOM  16467  N   VAL E  78       1.540 -97.834 -83.946  1.00 27.39           N  
-ATOM  16468  CA  VAL E  78       1.819 -99.243 -84.165  1.00 26.70           C  
-ATOM  16469  C   VAL E  78       1.415-100.042 -82.929  1.00 28.39           C  
-ATOM  16470  O   VAL E  78       1.775 -99.691 -81.801  1.00 23.63           O  
-ATOM  16471  CB  VAL E  78       3.307 -99.485 -84.484  1.00 20.49           C  
-ATOM  16472  CG1 VAL E  78       3.550-100.950 -84.818  1.00 18.69           C  
-ATOM  16473  CG2 VAL E  78       3.750 -98.597 -85.633  1.00 13.97           C  
-ATOM  16474  N   MET E  79       0.653-101.109 -83.148  1.00 33.28           N  
-ATOM  16475  CA  MET E  79       0.157-101.925 -82.051  1.00 29.02           C  
-ATOM  16476  C   MET E  79       0.284-103.416 -82.343  1.00 26.15           C  
-ATOM  16477  O   MET E  79       0.556-103.818 -83.474  1.00 23.63           O  
-ATOM  16478  CB  MET E  79      -1.301-101.578 -81.750  1.00 23.83           C  
-ATOM  16479  CG  MET E  79      -2.284-102.087 -82.788  1.00 24.39           C  
-ATOM  16480  SD  MET E  79      -3.877-101.256 -82.675  1.00 29.35           S  
-ATOM  16481  CE  MET E  79      -3.420 -99.610 -83.207  1.00 27.55           C  
-ATOM  16482  N   GLY E  80       0.091-104.227 -81.308  1.00 29.99           N  
-ATOM  16483  CA  GLY E  80       0.069-105.669 -81.459  1.00 28.45           C  
-ATOM  16484  C   GLY E  80      -1.324-106.145 -81.820  1.00 33.28           C  
-ATOM  16485  O   GLY E  80      -2.301-105.413 -81.639  1.00 32.19           O  
-ATOM  16486  N   ARG E  81      -1.417-107.369 -82.331  1.00 24.75           N  
-ATOM  16487  CA  ARG E  81      -2.690-107.911 -82.788  1.00 25.70           C  
-ATOM  16488  C   ARG E  81      -3.718-107.980 -81.661  1.00 28.94           C  
-ATOM  16489  O   ARG E  81      -4.893-107.654 -81.853  1.00 35.56           O  
-ATOM  16490  CB  ARG E  81      -2.473-109.295 -83.402  1.00 22.87           C  
-ATOM  16491  CG  ARG E  81      -3.690-109.872 -84.094  1.00 28.16           C  
-ATOM  16492  CD  ARG E  81      -4.340-110.954 -83.258  1.00 28.80           C  
-ATOM  16493  NE  ARG E  81      -3.395-112.007 -82.908  1.00 27.49           N  
-ATOM  16494  CZ  ARG E  81      -3.626-112.943 -81.995  1.00 28.83           C  
-ATOM  16495  NH1 ARG E  81      -2.704-113.861 -81.740  1.00 34.82           N  
-ATOM  16496  NH2 ARG E  81      -4.776-112.960 -81.335  1.00 28.16           N  
-ATOM  16497  N   LYS E  82      -3.260-108.394 -80.484  1.00 29.61           N  
-ATOM  16498  CA  LYS E  82      -4.139-108.553 -79.330  1.00 30.80           C  
-ATOM  16499  C   LYS E  82      -4.639-107.208 -78.816  1.00 33.52           C  
-ATOM  16500  O   LYS E  82      -5.728-107.118 -78.249  1.00 36.72           O  
-ATOM  16501  CB  LYS E  82      -3.426-109.309 -78.206  1.00 28.52           C  
-ATOM  16502  CG  LYS E  82      -3.080-110.745 -78.570  1.00 34.78           C  
-ATOM  16503  CD  LYS E  82      -2.563-111.534 -77.375  1.00 34.52           C  
-ATOM  16504  CE  LYS E  82      -2.316-112.986 -77.761  1.00 35.22           C  
-ATOM  16505  NZ  LYS E  82      -1.950-113.830 -76.591  1.00 36.55           N  
-ATOM  16506  N   THR E  83      -3.843-106.162 -79.010  1.00 31.09           N  
-ATOM  16507  CA  THR E  83      -4.254-104.825 -78.606  1.00 26.47           C  
-ATOM  16508  C   THR E  83      -5.370-104.339 -79.528  1.00 38.11           C  
-ATOM  16509  O   THR E  83      -6.395-103.809 -79.075  1.00 42.78           O  
-ATOM  16510  CB  THR E  83      -3.068-103.839 -78.635  1.00 26.06           C  
-ATOM  16511  OG1 THR E  83      -2.060-104.269 -77.709  1.00 22.72           O  
-ATOM  16512  CG2 THR E  83      -3.524-102.446 -78.264  1.00 32.73           C  
-ATOM  16513  N   TRP E  84      -5.154-104.533 -80.825  1.00 32.92           N  
-ATOM  16514  CA  TRP E  84      -6.168-104.257 -81.832  1.00 31.49           C  
-ATOM  16515  C   TRP E  84      -7.465-104.992 -81.529  1.00 28.99           C  
-ATOM  16516  O   TRP E  84      -8.548-104.425 -81.654  1.00 26.60           O  
-ATOM  16517  CB  TRP E  84      -5.673-104.655 -83.221  1.00 28.28           C  
-ATOM  16518  CG  TRP E  84      -6.748-104.583 -84.260  1.00 31.37           C  
-ATOM  16519  CD1 TRP E  84      -7.604-105.581 -84.633  1.00 31.18           C  
-ATOM  16520  CD2 TRP E  84      -7.094-103.444 -85.049  1.00 29.81           C  
-ATOM  16521  NE1 TRP E  84      -8.459-105.132 -85.611  1.00 27.86           N  
-ATOM  16522  CE2 TRP E  84      -8.164-103.821 -85.886  1.00 25.57           C  
-ATOM  16523  CE3 TRP E  84      -6.600-102.139 -85.135  1.00 22.72           C  
-ATOM  16524  CZ2 TRP E  84      -8.747-102.944 -86.790  1.00 26.92           C  
-ATOM  16525  CZ3 TRP E  84      -7.180-101.269 -86.035  1.00 28.04           C  
-ATOM  16526  CH2 TRP E  84      -8.241-101.674 -86.851  1.00 35.20           C  
-ATOM  16527  N   GLU E  85      -7.354-106.257 -81.139  1.00 28.58           N  
-ATOM  16528  CA  GLU E  85      -8.539-107.035 -80.809  1.00 26.83           C  
-ATOM  16529  C   GLU E  85      -9.160-106.565 -79.498  1.00 28.87           C  
-ATOM  16530  O   GLU E  85     -10.360-106.763 -79.264  1.00 29.94           O  
-ATOM  16531  CB  GLU E  85      -8.196-108.523 -80.735  1.00 30.20           C  
-ATOM  16532  CG  GLU E  85      -7.798-109.120 -82.075  1.00 32.31           C  
-ATOM  16533  CD  GLU E  85      -7.482-110.600 -81.992  1.00 42.67           C  
-ATOM  16534  OE1 GLU E  85      -7.205-111.095 -80.876  1.00 34.12           O  
-ATOM  16535  OE2 GLU E  85      -7.508-111.266 -83.050  1.00 39.53           O  
-ATOM  16536  N   SER E  86      -8.343-105.944 -78.648  1.00 27.52           N  
-ATOM  16537  CA  SER E  86      -8.803-105.494 -77.337  1.00 29.64           C  
-ATOM  16538  C   SER E  86      -9.608-104.208 -77.459  1.00 29.82           C  
-ATOM  16539  O   SER E  86     -10.580-104.008 -76.738  1.00 30.49           O  
-ATOM  16540  CB  SER E  86      -7.621-105.293 -76.379  1.00 36.61           C  
-ATOM  16541  OG  SER E  86      -6.951-104.065 -76.619  1.00 49.33           O  
-ATOM  16542  N   MET E  87      -9.197-103.340 -78.377  1.00 35.29           N  
-ATOM  16543  CA  MET E  87      -9.929-102.105 -78.628  1.00 33.58           C  
-ATOM  16544  C   MET E  87     -11.340-102.396 -79.133  1.00 41.11           C  
-ATOM  16545  O   MET E  87     -11.551-103.337 -79.902  1.00 39.13           O  
-ATOM  16546  CB  MET E  87      -9.183-101.231 -79.638  1.00 29.58           C  
-ATOM  16547  CG  MET E  87      -7.838-100.711 -79.154  1.00 34.99           C  
-ATOM  16548  SD  MET E  87      -6.967 -99.788 -80.437  1.00 34.98           S  
-ATOM  16549  CE  MET E  87      -8.280 -98.716 -81.004  1.00 33.72           C  
-ATOM  16550  N   PRO E  88     -12.317-101.586 -78.694  1.00 49.11           N  
-ATOM  16551  CA  PRO E  88     -13.707-101.717 -79.149  1.00 46.78           C  
-ATOM  16552  C   PRO E  88     -13.837-101.489 -80.654  1.00 44.44           C  
-ATOM  16553  O   PRO E  88     -13.034-100.757 -81.233  1.00 43.65           O  
-ATOM  16554  CB  PRO E  88     -14.446-100.626 -78.357  1.00 36.51           C  
-ATOM  16555  CG  PRO E  88     -13.378 -99.679 -77.907  1.00 38.66           C  
-ATOM  16556  CD  PRO E  88     -12.171-100.528 -77.681  1.00 39.90           C  
-ATOM  16557  N   ARG E  89     -14.831-102.122 -81.272  1.00 45.92           N  
-ATOM  16558  CA  ARG E  89     -15.025-102.046 -82.718  1.00 46.07           C  
-ATOM  16559  C   ARG E  89     -15.180-100.612 -83.212  1.00 45.85           C  
-ATOM  16560  O   ARG E  89     -14.577-100.223 -84.213  1.00 45.67           O  
-ATOM  16561  CB  ARG E  89     -16.254-102.856 -83.131  1.00 56.23           C  
-ATOM  16562  CG  ARG E  89     -16.172-104.342 -82.831  1.00 69.32           C  
-ATOM  16563  CD  ARG E  89     -15.673-105.132 -84.030  1.00 73.31           C  
-ATOM  16564  NE  ARG E  89     -16.253-106.473 -84.064  1.00 67.76           N  
-ATOM  16565  CZ  ARG E  89     -15.763-107.520 -83.408  1.00 80.90           C  
-ATOM  16566  NH1 ARG E  89     -14.674-107.392 -82.661  1.00 75.27           N  
-ATOM  16567  NH2 ARG E  89     -16.362-108.700 -83.499  1.00 78.17           N  
-ATOM  16568  N   LYS E  90     -15.987 -99.829 -82.503  1.00 45.03           N  
-ATOM  16569  CA  LYS E  90     -16.355 -98.490 -82.954  1.00 44.31           C  
-ATOM  16570  C   LYS E  90     -15.181 -97.514 -82.958  1.00 38.13           C  
-ATOM  16571  O   LYS E  90     -15.191 -96.525 -83.688  1.00 44.17           O  
-ATOM  16572  CB  LYS E  90     -17.484 -97.936 -82.079  1.00 43.99           C  
-ATOM  16573  CG  LYS E  90     -17.044 -97.514 -80.684  1.00 67.90           C  
-ATOM  16574  CD  LYS E  90     -17.964 -98.069 -79.605  1.00 71.68           C  
-ATOM  16575  CE  LYS E  90     -17.824 -99.579 -79.473  1.00 61.18           C  
-ATOM  16576  NZ  LYS E  90     -18.517-100.088 -78.257  1.00 48.92           N  
-ATOM  16577  N   PHE E  91     -14.170 -97.793 -82.145  1.00 39.79           N  
-ATOM  16578  CA  PHE E  91     -13.053 -96.871 -81.989  1.00 45.61           C  
-ATOM  16579  C   PHE E  91     -11.873 -97.221 -82.887  1.00 45.96           C  
-ATOM  16580  O   PHE E  91     -10.953 -96.419 -83.053  1.00 45.36           O  
-ATOM  16581  CB  PHE E  91     -12.605 -96.833 -80.526  1.00 56.83           C  
-ATOM  16582  CG  PHE E  91     -13.363 -95.843 -79.687  1.00 75.50           C  
-ATOM  16583  CD1 PHE E  91     -13.745 -94.620 -80.216  1.00 74.45           C  
-ATOM  16584  CD2 PHE E  91     -13.698 -96.135 -78.374  1.00 74.07           C  
-ATOM  16585  CE1 PHE E  91     -14.441 -93.704 -79.451  1.00 69.45           C  
-ATOM  16586  CE2 PHE E  91     -14.394 -95.221 -77.603  1.00 75.20           C  
-ATOM  16587  CZ  PHE E  91     -14.766 -94.005 -78.143  1.00 77.47           C  
-ATOM  16588  N   ARG E  92     -11.902 -98.414 -83.472  1.00 40.25           N  
-ATOM  16589  CA  ARG E  92     -10.796 -98.856 -84.310  1.00 37.16           C  
-ATOM  16590  C   ARG E  92     -11.184 -98.903 -85.787  1.00 32.86           C  
-ATOM  16591  O   ARG E  92     -12.307 -99.271 -86.128  1.00 39.69           O  
-ATOM  16592  CB  ARG E  92     -10.285-100.224 -83.846  1.00 33.54           C  
-ATOM  16593  CG  ARG E  92     -11.168-101.400 -84.205  1.00 33.64           C  
-ATOM  16594  CD  ARG E  92     -10.757-102.627 -83.416  1.00 33.14           C  
-ATOM  16595  NE  ARG E  92     -11.412-103.838 -83.898  1.00 41.02           N  
-ATOM  16596  CZ  ARG E  92     -11.651-104.905 -83.143  1.00 45.78           C  
-ATOM  16597  NH1 ARG E  92     -12.248-105.967 -83.665  1.00 50.91           N  
-ATOM  16598  NH2 ARG E  92     -11.300-104.907 -81.865  1.00 47.58           N  
-ATOM  16599  N   PRO E  93     -10.256 -98.507 -86.672  1.00 30.54           N  
-ATOM  16600  CA  PRO E  93      -8.918 -97.994 -86.351  1.00 31.33           C  
-ATOM  16601  C   PRO E  93      -8.952 -96.603 -85.722  1.00 33.90           C  
-ATOM  16602  O   PRO E  93      -9.909 -95.857 -85.934  1.00 43.00           O  
-ATOM  16603  CB  PRO E  93      -8.225 -97.953 -87.715  1.00 27.73           C  
-ATOM  16604  CG  PRO E  93      -9.332 -97.806 -88.690  1.00 30.77           C  
-ATOM  16605  CD  PRO E  93     -10.467 -98.606 -88.126  1.00 38.30           C  
-ATOM  16606  N   LEU E  94      -7.928 -96.279 -84.940  1.00 28.38           N  
-ATOM  16607  CA  LEU E  94      -7.837 -94.975 -84.299  1.00 35.62           C  
-ATOM  16608  C   LEU E  94      -7.844 -93.869 -85.349  1.00 32.47           C  
-ATOM  16609  O   LEU E  94      -6.982 -93.825 -86.225  1.00 38.42           O  
-ATOM  16610  CB  LEU E  94      -6.580 -94.894 -83.429  1.00 42.50           C  
-ATOM  16611  CG  LEU E  94      -6.590 -95.729 -82.144  1.00 25.69           C  
-ATOM  16612  CD1 LEU E  94      -5.198 -95.831 -81.548  1.00 24.25           C  
-ATOM  16613  CD2 LEU E  94      -7.559 -95.148 -81.127  1.00 23.78           C  
-ATOM  16614  N   VAL E  95      -8.834 -92.986 -85.257  1.00 31.31           N  
-ATOM  16615  CA  VAL E  95      -9.046 -91.948 -86.262  1.00 37.94           C  
-ATOM  16616  C   VAL E  95      -7.865 -90.989 -86.398  1.00 39.41           C  
-ATOM  16617  O   VAL E  95      -7.138 -90.740 -85.435  1.00 35.25           O  
-ATOM  16618  CB  VAL E  95     -10.308 -91.127 -85.948  1.00 34.99           C  
-ATOM  16619  CG1 VAL E  95     -11.557 -91.925 -86.289  1.00 31.86           C  
-ATOM  16620  CG2 VAL E  95     -10.314 -90.705 -84.486  1.00 39.30           C  
-ATOM  16621  N   ASP E  96      -7.678 -90.479 -87.615  1.00 44.99           N  
-ATOM  16622  CA  ASP E  96      -6.664 -89.468 -87.923  1.00 35.11           C  
-ATOM  16623  C   ASP E  96      -5.234 -89.943 -87.669  1.00 32.45           C  
-ATOM  16624  O   ASP E  96      -4.294 -89.147 -87.701  1.00 37.64           O  
-ATOM  16625  CB  ASP E  96      -6.938 -88.192 -87.125  1.00 33.67           C  
-ATOM  16626  CG  ASP E  96      -8.348 -87.676 -87.328  1.00 44.01           C  
-ATOM  16627  OD1 ASP E  96      -8.812 -87.656 -88.490  1.00 50.63           O  
-ATOM  16628  OD2 ASP E  96      -8.997 -87.302 -86.327  1.00 33.74           O  
-ATOM  16629  N   ARG E  97      -5.073 -91.240 -87.430  1.00 30.60           N  
-ATOM  16630  CA  ARG E  97      -3.759 -91.827 -87.197  1.00 27.88           C  
-ATOM  16631  C   ARG E  97      -3.565 -93.053 -88.077  1.00 29.84           C  
-ATOM  16632  O   ARG E  97      -4.461 -93.889 -88.198  1.00 28.73           O  
-ATOM  16633  CB  ARG E  97      -3.590 -92.204 -85.725  1.00 25.57           C  
-ATOM  16634  CG  ARG E  97      -3.464 -91.015 -84.788  1.00 26.32           C  
-ATOM  16635  CD  ARG E  97      -3.901 -91.372 -83.376  1.00 27.32           C  
-ATOM  16636  NE  ARG E  97      -5.346 -91.571 -83.295  1.00 32.87           N  
-ATOM  16637  CZ  ARG E  97      -6.026 -91.695 -82.159  1.00 26.44           C  
-ATOM  16638  NH1 ARG E  97      -5.396 -91.639 -80.995  1.00 30.42           N  
-ATOM  16639  NH2 ARG E  97      -7.339 -91.872 -82.188  1.00 26.58           N  
-ATOM  16640  N   LEU E  98      -2.398 -93.156 -88.704  1.00 29.20           N  
-ATOM  16641  CA  LEU E  98      -2.088 -94.327 -89.512  1.00 25.23           C  
-ATOM  16642  C   LEU E  98      -1.957 -95.541 -88.609  1.00 32.84           C  
-ATOM  16643  O   LEU E  98      -1.066 -95.603 -87.769  1.00 30.19           O  
-ATOM  16644  CB  LEU E  98      -0.803 -94.122 -90.312  1.00 30.86           C  
-ATOM  16645  CG  LEU E  98      -0.265 -95.387 -90.981  1.00 31.20           C  
-ATOM  16646  CD1 LEU E  98      -1.196 -95.850 -92.092  1.00 31.18           C  
-ATOM  16647  CD2 LEU E  98       1.145 -95.172 -91.506  1.00 34.33           C  
-ATOM  16648  N   ASN E  99      -2.849 -96.507 -88.781  1.00 28.49           N  
-ATOM  16649  CA  ASN E  99      -2.821 -97.704 -87.952  1.00 27.75           C  
-ATOM  16650  C   ASN E  99      -1.977 -98.827 -88.548  1.00 31.50           C  
-ATOM  16651  O   ASN E  99      -2.252 -99.320 -89.647  1.00 36.72           O  
-ATOM  16652  CB  ASN E  99      -4.245 -98.200 -87.699  1.00 30.35           C  
-ATOM  16653  CG  ASN E  99      -4.956 -97.400 -86.625  1.00 35.71           C  
-ATOM  16654  OD1 ASN E  99      -5.238 -96.214 -86.799  1.00 43.20           O  
-ATOM  16655  ND2 ASN E  99      -5.256 -98.050 -85.508  1.00 24.24           N  
-ATOM  16656  N   ILE E 100      -0.939 -99.220 -87.817  1.00 23.40           N  
-ATOM  16657  CA  ILE E 100      -0.129-100.364 -88.210  1.00 26.03           C  
-ATOM  16658  C   ILE E 100      -0.232-101.454 -87.155  1.00 27.13           C  
-ATOM  16659  O   ILE E 100       0.019-101.215 -85.976  1.00 29.26           O  
-ATOM  16660  CB  ILE E 100       1.353 -99.986 -88.416  1.00 27.13           C  
-ATOM  16661  CG1 ILE E 100       1.487 -98.892 -89.476  1.00 26.28           C  
-ATOM  16662  CG2 ILE E 100       2.162-101.214 -88.817  1.00 25.15           C  
-ATOM  16663  CD1 ILE E 100       2.921 -98.546 -89.807  1.00 20.00           C  
-ATOM  16664  N   VAL E 101      -0.613-102.649 -87.587  1.00 27.91           N  
-ATOM  16665  CA  VAL E 101      -0.740-103.779 -86.683  1.00 23.80           C  
-ATOM  16666  C   VAL E 101       0.315-104.828 -86.987  1.00 20.26           C  
-ATOM  16667  O   VAL E 101       0.476-105.245 -88.133  1.00 22.12           O  
-ATOM  16668  CB  VAL E 101      -2.134-104.424 -86.774  1.00 19.42           C  
-ATOM  16669  CG1 VAL E 101      -2.248-105.573 -85.782  1.00 20.59           C  
-ATOM  16670  CG2 VAL E 101      -3.218-103.386 -86.529  1.00 17.03           C  
-ATOM  16671  N   VAL E 102       1.037-105.245 -85.954  1.00 23.75           N  
-ATOM  16672  CA  VAL E 102       2.023-106.308 -86.090  1.00 30.29           C  
-ATOM  16673  C   VAL E 102       1.384-107.669 -85.829  1.00 39.54           C  
-ATOM  16674  O   VAL E 102       0.936-107.957 -84.717  1.00 33.72           O  
-ATOM  16675  CB  VAL E 102       3.210-106.106 -85.132  1.00 26.55           C  
-ATOM  16676  CG1 VAL E 102       4.137-107.309 -85.171  1.00 27.49           C  
-ATOM  16677  CG2 VAL E 102       3.961-104.834 -85.491  1.00 26.41           C  
-ATOM  16678  N   SER E 103       1.339-108.500 -86.866  1.00 40.89           N  
-ATOM  16679  CA  SER E 103       0.731-109.822 -86.767  1.00 38.75           C  
-ATOM  16680  C   SER E 103       1.201-110.723 -87.902  1.00 40.62           C  
-ATOM  16681  O   SER E 103       1.778-110.255 -88.884  1.00 45.02           O  
-ATOM  16682  CB  SER E 103      -0.796-109.713 -86.783  1.00 36.14           C  
-ATOM  16683  OG  SER E 103      -1.407-110.983 -86.633  1.00 37.18           O  
-ATOM  16684  N   SER E 104       0.957-112.020 -87.757  1.00 39.99           N  
-ATOM  16685  CA  SER E 104       1.283-112.979 -88.804  1.00 39.63           C  
-ATOM  16686  C   SER E 104       0.046-113.782 -89.180  1.00 43.89           C  
-ATOM  16687  O   SER E 104      -0.009-114.403 -90.242  1.00 51.70           O  
-ATOM  16688  CB  SER E 104       2.410-113.906 -88.354  1.00 39.09           C  
-ATOM  16689  OG  SER E 104       3.628-113.191 -88.223  1.00 39.28           O  
-ATOM  16690  N   SER E 105      -0.947-113.760 -88.297  1.00 41.68           N  
-ATOM  16691  CA  SER E 105      -2.213-114.433 -88.549  1.00 45.17           C  
-ATOM  16692  C   SER E 105      -3.198-113.484 -89.227  1.00 47.70           C  
-ATOM  16693  O   SER E 105      -3.845-113.847 -90.210  1.00 50.61           O  
-ATOM  16694  CB  SER E 105      -2.800-114.984 -87.244  1.00 43.23           C  
-ATOM  16695  OG  SER E 105      -3.043-113.952 -86.306  1.00 44.73           O  
-ATOM  16696  N   LEU E 106      -3.304-112.267 -88.700  1.00 43.91           N  
-ATOM  16697  CA  LEU E 106      -4.175-111.255 -89.288  1.00 47.52           C  
-ATOM  16698  C   LEU E 106      -3.645-110.753 -90.625  1.00 46.27           C  
-ATOM  16699  O   LEU E 106      -2.435-110.648 -90.830  1.00 47.99           O  
-ATOM  16700  CB  LEU E 106      -4.356-110.070 -88.336  1.00 47.69           C  
-ATOM  16701  CG  LEU E 106      -5.547-110.127 -87.376  1.00 51.25           C  
-ATOM  16702  CD1 LEU E 106      -5.830-108.750 -86.791  1.00 38.60           C  
-ATOM  16703  CD2 LEU E 106      -6.780-110.682 -88.075  1.00 54.41           C  
-ATOM  16704  N   LYS E 107      -4.564-110.442 -91.531  1.00 41.72           N  
-ATOM  16705  CA  LYS E 107      -4.205-109.859 -92.817  1.00 51.67           C  
-ATOM  16706  C   LYS E 107      -4.880-108.502 -92.962  1.00 47.57           C  
-ATOM  16707  O   LYS E 107      -5.787-108.175 -92.198  1.00 48.91           O  
-ATOM  16708  CB  LYS E 107      -4.604-110.784 -93.967  1.00 57.82           C  
-ATOM  16709  CG  LYS E 107      -4.043-112.192 -93.847  1.00 69.68           C  
-ATOM  16710  CD  LYS E 107      -4.327-113.011 -95.095  1.00 74.65           C  
-ATOM  16711  CE  LYS E 107      -3.064-113.704 -95.584  1.00 82.13           C  
-ATOM  16712  NZ  LYS E 107      -1.982-112.722 -95.887  1.00 57.65           N  
-ATOM  16713  N   GLU E 108      -4.440-107.716 -93.938  1.00 36.34           N  
-ATOM  16714  CA  GLU E 108      -4.982-106.378 -94.128  1.00 32.25           C  
-ATOM  16715  C   GLU E 108      -6.445-106.434 -94.550  1.00 36.99           C  
-ATOM  16716  O   GLU E 108      -7.236-105.567 -94.189  1.00 48.95           O  
-ATOM  16717  CB  GLU E 108      -4.147-105.609 -95.155  1.00 37.52           C  
-ATOM  16718  CG  GLU E 108      -2.712-105.385 -94.715  1.00 36.85           C  
-ATOM  16719  CD  GLU E 108      -1.946-104.462 -95.639  1.00 43.05           C  
-ATOM  16720  OE1 GLU E 108      -2.520-103.998 -96.650  1.00 45.23           O  
-ATOM  16721  OE2 GLU E 108      -0.762-104.200 -95.345  1.00 46.45           O  
-ATOM  16722  N   GLU E 109      -6.803-107.468 -95.301  1.00 40.91           N  
-ATOM  16723  CA  GLU E 109      -8.182-107.640 -95.733  1.00 46.07           C  
-ATOM  16724  C   GLU E 109      -9.090-108.098 -94.600  1.00 39.16           C  
-ATOM  16725  O   GLU E 109     -10.298-107.857 -94.631  1.00 49.49           O  
-ATOM  16726  CB  GLU E 109      -8.264-108.632 -96.891  1.00 45.36           C  
-ATOM  16727  CG  GLU E 109      -8.435-107.970 -98.248  1.00 76.84           C  
-ATOM  16728  CD  GLU E 109      -9.637-107.031 -98.309  1.00 79.41           C  
-ATOM  16729  OE1 GLU E 109      -9.552-106.000 -99.012  1.00 78.08           O  
-ATOM  16730  OE2 GLU E 109     -10.667-107.321 -97.662  1.00 63.50           O  
-ATOM  16731  N   ASP E 110      -8.512-108.767 -93.609  1.00 34.35           N  
-ATOM  16732  CA  ASP E 110      -9.267-109.158 -92.428  1.00 32.34           C  
-ATOM  16733  C   ASP E 110      -9.748-107.917 -91.685  1.00 40.63           C  
-ATOM  16734  O   ASP E 110     -10.838-107.898 -91.114  1.00 36.64           O  
-ATOM  16735  CB  ASP E 110      -8.422-110.043 -91.508  1.00 40.23           C  
-ATOM  16736  CG  ASP E 110      -8.380-111.485 -91.968  1.00 49.78           C  
-ATOM  16737  OD1 ASP E 110      -9.444-112.139 -91.957  1.00 61.70           O  
-ATOM  16738  OD2 ASP E 110      -7.288-111.968 -92.332  1.00 47.90           O  
-ATOM  16739  N   ILE E 111      -8.925-106.878 -91.711  1.00 39.14           N  
-ATOM  16740  CA  ILE E 111      -9.257-105.625 -91.059  1.00 36.49           C  
-ATOM  16741  C   ILE E 111     -10.148-104.777 -91.961  1.00 35.75           C  
-ATOM  16742  O   ILE E 111     -11.073-104.118 -91.492  1.00 35.76           O  
-ATOM  16743  CB  ILE E 111      -7.980-104.850 -90.677  1.00 33.76           C  
-ATOM  16744  CG1 ILE E 111      -7.215-105.619 -89.595  1.00 31.63           C  
-ATOM  16745  CG2 ILE E 111      -8.326-103.448 -90.204  1.00 29.68           C  
-ATOM  16746  CD1 ILE E 111      -5.908-104.978 -89.186  1.00 31.58           C  
-ATOM  16747  N   ALA E 112      -9.878-104.820 -93.261  1.00 34.08           N  
-ATOM  16748  CA  ALA E 112     -10.652-104.061 -94.235  1.00 31.15           C  
-ATOM  16749  C   ALA E 112     -12.106-104.519 -94.257  1.00 37.63           C  
-ATOM  16750  O   ALA E 112     -13.020-103.705 -94.409  1.00 37.03           O  
-ATOM  16751  CB  ALA E 112     -10.038-104.194 -95.616  1.00 37.24           C  
-ATOM  16752  N   ALA E 113     -12.312-105.824 -94.102  1.00 39.21           N  
-ATOM  16753  CA  ALA E 113     -13.652-106.399 -94.148  1.00 43.44           C  
-ATOM  16754  C   ALA E 113     -14.335-106.381 -92.781  1.00 47.21           C  
-ATOM  16755  O   ALA E 113     -15.457-106.867 -92.635  1.00 52.57           O  
-ATOM  16756  CB  ALA E 113     -13.592-107.820 -94.691  1.00 32.66           C  
-ATOM  16757  N   GLU E 114     -13.652-105.823 -91.786  1.00 44.37           N  
-ATOM  16758  CA  GLU E 114     -14.203-105.716 -90.438  1.00 45.90           C  
-ATOM  16759  C   GLU E 114     -15.115-104.494 -90.316  1.00 45.89           C  
-ATOM  16760  O   GLU E 114     -16.115-104.515 -89.594  1.00 38.95           O  
-ATOM  16761  CB  GLU E 114     -13.070-105.643 -89.412  1.00 49.41           C  
-ATOM  16762  CG  GLU E 114     -13.519-105.562 -87.964  1.00 47.03           C  
-ATOM  16763  CD  GLU E 114     -12.351-105.413 -87.008  1.00 50.35           C  
-ATOM  16764  OE1 GLU E 114     -12.250-104.357 -86.348  1.00 52.09           O  
-ATOM  16765  OE2 GLU E 114     -11.528-106.350 -86.921  1.00 53.53           O  
-ATOM  16766  N   LYS E 115     -14.757-103.434 -91.035  1.00 48.34           N  
-ATOM  16767  CA  LYS E 115     -15.521-102.191 -91.048  1.00 43.69           C  
-ATOM  16768  C   LYS E 115     -15.127-101.357 -92.264  1.00 46.85           C  
-ATOM  16769  O   LYS E 115     -13.940-101.227 -92.568  1.00 46.94           O  
-ATOM  16770  CB  LYS E 115     -15.287-101.395 -89.760  1.00 37.49           C  
-ATOM  16771  CG  LYS E 115     -15.879 -99.994 -89.771  1.00 34.07           C  
-ATOM  16772  CD  LYS E 115     -15.234 -99.102 -88.722  1.00 33.36           C  
-ATOM  16773  CE  LYS E 115     -15.560 -99.564 -87.313  1.00 30.45           C  
-ATOM  16774  NZ  LYS E 115     -15.001 -98.632 -86.294  1.00 38.53           N  
-ATOM  16775  N   PRO E 116     -16.122-100.792 -92.967  1.00 39.14           N  
-ATOM  16776  CA  PRO E 116     -15.852 -99.956 -94.142  1.00 38.92           C  
-ATOM  16777  C   PRO E 116     -14.961 -98.756 -93.829  1.00 47.85           C  
-ATOM  16778  O   PRO E 116     -15.278 -97.951 -92.950  1.00 44.49           O  
-ATOM  16779  CB  PRO E 116     -17.250 -99.498 -94.579  1.00 31.75           C  
-ATOM  16780  CG  PRO E 116     -18.126 -99.717 -93.386  1.00 32.35           C  
-ATOM  16781  CD  PRO E 116     -17.566-100.924 -92.711  1.00 37.36           C  
-ATOM  16782  N   GLN E 117     -13.850 -98.655 -94.552  1.00 46.64           N  
-ATOM  16783  CA  GLN E 117     -12.914 -97.550 -94.394  1.00 45.85           C  
-ATOM  16784  C   GLN E 117     -13.591 -96.201 -94.627  1.00 52.87           C  
-ATOM  16785  O   GLN E 117     -14.143 -95.948 -95.699  1.00 54.79           O  
-ATOM  16786  CB  GLN E 117     -11.739 -97.723 -95.355  1.00 45.25           C  
-ATOM  16787  CG  GLN E 117     -10.771 -96.556 -95.374  1.00 54.68           C  
-ATOM  16788  CD  GLN E 117      -9.676 -96.735 -96.407  1.00 60.24           C  
-ATOM  16789  OE1 GLN E 117      -8.842 -95.854 -96.605  1.00 58.22           O  
-ATOM  16790  NE2 GLN E 117      -9.674 -97.884 -97.072  1.00 67.50           N  
-ATOM  16791  N   ALA E 118     -13.554 -95.343 -93.613  1.00 50.71           N  
-ATOM  16792  CA  ALA E 118     -14.151 -94.017 -93.715  1.00 49.23           C  
-ATOM  16793  C   ALA E 118     -13.348 -93.147 -94.670  1.00 50.62           C  
-ATOM  16794  O   ALA E 118     -12.138 -93.323 -94.811  1.00 61.17           O  
-ATOM  16795  CB  ALA E 118     -14.242 -93.364 -92.346  1.00 50.72           C  
-ATOM  16796  N   GLU E 119     -14.024 -92.210 -95.326  1.00 44.26           N  
-ATOM  16797  CA  GLU E 119     -13.368 -91.330 -96.285  1.00 54.72           C  
-ATOM  16798  C   GLU E 119     -12.396 -90.387 -95.583  1.00 55.44           C  
-ATOM  16799  O   GLU E 119     -12.694 -89.858 -94.512  1.00 50.60           O  
-ATOM  16800  CB  GLU E 119     -14.409 -90.534 -97.079  1.00 65.45           C  
-ATOM  16801  CG  GLU E 119     -13.835 -89.669 -98.198  1.00 74.46           C  
-ATOM  16802  CD  GLU E 119     -13.455 -88.274 -97.730  1.00 87.66           C  
-ATOM  16803  OE1 GLU E 119     -12.408 -87.760 -98.181  1.00 79.82           O  
-ATOM  16804  OE2 GLU E 119     -14.205 -87.692 -96.915  1.00 72.29           O  
-ATOM  16805  N   GLY E 120     -11.230 -90.190 -96.191  1.00 55.78           N  
-ATOM  16806  CA  GLY E 120     -10.222 -89.296 -95.649  1.00 59.73           C  
-ATOM  16807  C   GLY E 120      -9.274 -89.975 -94.680  1.00 53.80           C  
-ATOM  16808  O   GLY E 120      -8.285 -89.384 -94.247  1.00 47.84           O  
-ATOM  16809  N   GLN E 121      -9.574 -91.222 -94.338  1.00 52.52           N  
-ATOM  16810  CA  GLN E 121      -8.762 -91.964 -93.384  1.00 45.53           C  
-ATOM  16811  C   GLN E 121      -7.816 -92.933 -94.084  1.00 53.60           C  
-ATOM  16812  O   GLN E 121      -8.093 -93.401 -95.189  1.00 56.41           O  
-ATOM  16813  CB  GLN E 121      -9.658 -92.717 -92.400  1.00 44.49           C  
-ATOM  16814  CG  GLN E 121     -10.378 -91.813 -91.416  1.00 47.85           C  
-ATOM  16815  CD  GLN E 121      -9.424 -91.120 -90.464  1.00 50.25           C  
-ATOM  16816  OE1 GLN E 121      -8.424 -91.700 -90.036  1.00 49.06           O  
-ATOM  16817  NE2 GLN E 121      -9.723 -89.869 -90.131  1.00 39.13           N  
-ATOM  16818  N   GLN E 122      -6.694 -93.223 -93.432  1.00 49.79           N  
-ATOM  16819  CA  GLN E 122      -5.695 -94.134 -93.974  1.00 38.67           C  
-ATOM  16820  C   GLN E 122      -6.152 -95.580 -93.859  1.00 37.75           C  
-ATOM  16821  O   GLN E 122      -6.914 -95.930 -92.957  1.00 36.54           O  
-ATOM  16822  CB  GLN E 122      -4.359 -93.951 -93.252  1.00 43.54           C  
-ATOM  16823  CG  GLN E 122      -3.235 -93.422 -94.132  1.00 48.34           C  
-ATOM  16824  CD  GLN E 122      -3.517 -92.037 -94.683  1.00 50.69           C  
-ATOM  16825  OE1 GLN E 122      -4.293 -91.269 -94.111  1.00 51.65           O  
-ATOM  16826  NE2 GLN E 122      -2.884 -91.711 -95.805  1.00 42.13           N  
-ATOM  16827  N   ARG E 123      -5.688 -96.421 -94.776  1.00 40.54           N  
-ATOM  16828  CA  ARG E 123      -6.010 -97.837 -94.712  1.00 37.15           C  
-ATOM  16829  C   ARG E 123      -5.110 -98.501 -93.676  1.00 37.01           C  
-ATOM  16830  O   ARG E 123      -3.936 -98.148 -93.539  1.00 39.40           O  
-ATOM  16831  CB  ARG E 123      -5.865 -98.498 -96.088  1.00 35.82           C  
-ATOM  16832  CG  ARG E 123      -4.521 -99.154 -96.364  1.00 49.15           C  
-ATOM  16833  CD  ARG E 123      -4.528 -99.851 -97.713  1.00 44.80           C  
-ATOM  16834  NE  ARG E 123      -5.746-100.636 -97.895  1.00 61.91           N  
-ATOM  16835  CZ  ARG E 123      -5.830-101.950 -97.713  1.00 70.62           C  
-ATOM  16836  NH1 ARG E 123      -6.988-102.571 -97.897  1.00 58.67           N  
-ATOM  16837  NH2 ARG E 123      -4.759-102.646 -97.353  1.00 67.31           N  
-ATOM  16838  N   VAL E 124      -5.671 -99.443 -92.927  1.00 38.14           N  
-ATOM  16839  CA  VAL E 124      -4.922-100.111 -91.870  1.00 36.56           C  
-ATOM  16840  C   VAL E 124      -3.904-101.071 -92.468  1.00 35.96           C  
-ATOM  16841  O   VAL E 124      -4.241-101.907 -93.307  1.00 39.49           O  
-ATOM  16842  CB  VAL E 124      -5.847-100.879 -90.914  1.00 33.02           C  
-ATOM  16843  CG1 VAL E 124      -5.047-101.467 -89.768  1.00 22.98           C  
-ATOM  16844  CG2 VAL E 124      -6.930 -99.962 -90.382  1.00 28.78           C  
-ATOM  16845  N   ARG E 125      -2.655-100.949 -92.032  1.00 37.16           N  
-ATOM  16846  CA  ARG E 125      -1.585-101.777 -92.578  1.00 38.59           C  
-ATOM  16847  C   ARG E 125      -1.184-102.881 -91.604  1.00 35.00           C  
-ATOM  16848  O   ARG E 125      -1.302-102.719 -90.393  1.00 37.48           O  
-ATOM  16849  CB  ARG E 125      -0.373-100.913 -92.923  1.00 36.69           C  
-ATOM  16850  CG  ARG E 125       0.349-101.352 -94.170  1.00 47.04           C  
-ATOM  16851  CD  ARG E 125      -0.412-100.958 -95.421  1.00 39.92           C  
-ATOM  16852  NE  ARG E 125       0.341-101.304 -96.621  1.00 40.22           N  
-ATOM  16853  CZ  ARG E 125       1.280-100.532 -97.156  1.00 46.70           C  
-ATOM  16854  NH1 ARG E 125       1.921-100.922 -98.249  1.00 45.39           N  
-ATOM  16855  NH2 ARG E 125       1.577 -99.367 -96.596  1.00 45.25           N  
-ATOM  16856  N   VAL E 126      -0.710-104.003 -92.137  1.00 31.64           N  
-ATOM  16857  CA  VAL E 126      -0.291-105.126 -91.299  1.00 30.04           C  
-ATOM  16858  C   VAL E 126       1.136-105.569 -91.621  1.00 28.21           C  
-ATOM  16859  O   VAL E 126       1.472-105.814 -92.779  1.00 31.90           O  
-ATOM  16860  CB  VAL E 126      -1.237-106.335 -91.452  1.00 26.24           C  
-ATOM  16861  CG1 VAL E 126      -0.738-107.510 -90.632  1.00 30.20           C  
-ATOM  16862  CG2 VAL E 126      -2.650-105.959 -91.037  1.00 31.24           C  
-ATOM  16863  N   CYS E 127       1.970-105.666 -90.590  1.00 26.80           N  
-ATOM  16864  CA  CYS E 127       3.358-106.083 -90.759  1.00 22.40           C  
-ATOM  16865  C   CYS E 127       3.679-107.296 -89.893  1.00 24.89           C  
-ATOM  16866  O   CYS E 127       3.041-107.518 -88.865  1.00 24.25           O  
-ATOM  16867  CB  CYS E 127       4.304-104.927 -90.426  1.00 29.03           C  
-ATOM  16868  SG  CYS E 127       3.965-103.405 -91.343  1.00 30.29           S  
-ATOM  16869  N   ALA E 128       4.675-108.071 -90.309  1.00 28.49           N  
-ATOM  16870  CA  ALA E 128       5.025-109.305 -89.613  1.00 27.07           C  
-ATOM  16871  C   ALA E 128       5.959-109.069 -88.429  1.00 32.48           C  
-ATOM  16872  O   ALA E 128       6.239-109.991 -87.662  1.00 41.74           O  
-ATOM  16873  CB  ALA E 128       5.652-110.290 -90.581  1.00 23.49           C  
-ATOM  16874  N   SER E 129       6.444-107.840 -88.286  1.00 31.55           N  
-ATOM  16875  CA  SER E 129       7.330-107.497 -87.178  1.00 30.31           C  
-ATOM  16876  C   SER E 129       7.504-105.991 -87.043  1.00 35.77           C  
-ATOM  16877  O   SER E 129       7.076-105.227 -87.905  1.00 39.91           O  
-ATOM  16878  CB  SER E 129       8.695-108.163 -87.356  1.00 32.16           C  
-ATOM  16879  OG  SER E 129       9.319-107.723 -88.550  1.00 41.00           O  
-ATOM  16880  N   LEU E 130       8.136-105.575 -85.952  1.00 26.51           N  
-ATOM  16881  CA  LEU E 130       8.406-104.166 -85.708  1.00 29.78           C  
-ATOM  16882  C   LEU E 130       9.445-103.577 -86.672  1.00 32.16           C  
-ATOM  16883  O   LEU E 130       9.253-102.461 -87.168  1.00 44.46           O  
-ATOM  16884  CB  LEU E 130       8.851-103.958 -84.258  1.00 31.60           C  
-ATOM  16885  CG  LEU E 130       8.967-102.497 -83.830  1.00 30.17           C  
-ATOM  16886  CD1 LEU E 130       7.668-101.773 -84.128  1.00 23.17           C  
-ATOM  16887  CD2 LEU E 130       9.306-102.403 -82.359  1.00 22.33           C  
-ATOM  16888  N   PRO E 131      10.553-104.307 -86.935  1.00 28.95           N  
-ATOM  16889  CA  PRO E 131      11.443-103.817 -87.993  1.00 36.69           C  
-ATOM  16890  C   PRO E 131      10.726-103.681 -89.332  1.00 37.14           C  
-ATOM  16891  O   PRO E 131      11.065-102.796 -90.119  1.00 37.07           O  
-ATOM  16892  CB  PRO E 131      12.532-104.895 -88.061  1.00 34.79           C  
-ATOM  16893  CG  PRO E 131      12.578-105.452 -86.692  1.00 31.33           C  
-ATOM  16894  CD  PRO E 131      11.152-105.452 -86.221  1.00 35.89           C  
-ATOM  16895  N   ALA E 132       9.752-104.553 -89.580  1.00 30.22           N  
-ATOM  16896  CA  ALA E 132       8.948-104.481 -90.793  1.00 31.93           C  
-ATOM  16897  C   ALA E 132       8.068-103.241 -90.782  1.00 39.16           C  
-ATOM  16898  O   ALA E 132       7.901-102.582 -91.808  1.00 40.93           O  
-ATOM  16899  CB  ALA E 132       8.095-105.727 -90.946  1.00 26.52           C  
-ATOM  16900  N   ALA E 133       7.502-102.935 -89.619  1.00 33.25           N  
-ATOM  16901  CA  ALA E 133       6.669-101.752 -89.457  1.00 26.49           C  
-ATOM  16902  C   ALA E 133       7.469-100.491 -89.740  1.00 39.89           C  
-ATOM  16903  O   ALA E 133       7.017 -99.607 -90.471  1.00 40.12           O  
-ATOM  16904  CB  ALA E 133       6.082-101.703 -88.056  1.00 21.98           C  
-ATOM  16905  N   LEU E 134       8.662-100.417 -89.159  1.00 41.57           N  
-ATOM  16906  CA  LEU E 134       9.537 -99.264 -89.337  1.00 33.18           C  
-ATOM  16907  C   LEU E 134      10.040 -99.133 -90.773  1.00 40.75           C  
-ATOM  16908  O   LEU E 134      10.107 -98.029 -91.322  1.00 35.68           O  
-ATOM  16909  CB  LEU E 134      10.718 -99.356 -88.373  1.00 32.87           C  
-ATOM  16910  CG  LEU E 134      10.343 -99.397 -86.891  1.00 37.66           C  
-ATOM  16911  CD1 LEU E 134      11.587 -99.525 -86.024  1.00 37.65           C  
-ATOM  16912  CD2 LEU E 134       9.543 -98.161 -86.517  1.00 33.51           C  
-ATOM  16913  N   SER E 135      10.397-100.266 -91.371  1.00 39.75           N  
-ATOM  16914  CA  SER E 135      10.860-100.292 -92.751  1.00 35.78           C  
-ATOM  16915  C   SER E 135       9.759 -99.829 -93.695  1.00 42.81           C  
-ATOM  16916  O   SER E 135      10.024 -99.107 -94.655  1.00 50.16           O  
-ATOM  16917  CB  SER E 135      11.337-101.693 -93.142  1.00 36.16           C  
-ATOM  16918  OG  SER E 135      12.516-102.049 -92.443  1.00 49.68           O  
-ATOM  16919  N   LEU E 136       8.528-100.252 -93.420  1.00 35.87           N  
-ATOM  16920  CA  LEU E 136       7.372 -99.804 -94.187  1.00 37.62           C  
-ATOM  16921  C   LEU E 136       7.183 -98.301 -94.036  1.00 39.97           C  
-ATOM  16922  O   LEU E 136       7.022 -97.567 -95.015  1.00 46.55           O  
-ATOM  16923  CB  LEU E 136       6.115-100.547 -93.730  1.00 33.16           C  
-ATOM  16924  CG  LEU E 136       4.796-100.087 -94.347  1.00 28.83           C  
-ATOM  16925  CD1 LEU E 136       4.590-100.706 -95.720  1.00 26.52           C  
-ATOM  16926  CD2 LEU E 136       3.649-100.426 -93.419  1.00 34.70           C  
-ATOM  16927  N   LEU E 137       7.217 -97.866 -92.783  1.00 33.81           N  
-ATOM  16928  CA  LEU E 137       7.038 -96.471 -92.419  1.00 35.28           C  
-ATOM  16929  C   LEU E 137       8.049 -95.568 -93.116  1.00 42.17           C  
-ATOM  16930  O   LEU E 137       7.727 -94.441 -93.487  1.00 39.85           O  
-ATOM  16931  CB  LEU E 137       7.145 -96.310 -90.899  1.00 33.38           C  
-ATOM  16932  CG  LEU E 137       5.989 -95.606 -90.180  1.00 32.84           C  
-ATOM  16933  CD1 LEU E 137       4.741 -95.579 -91.044  1.00 30.58           C  
-ATOM  16934  CD2 LEU E 137       5.703 -96.290 -88.851  1.00 28.67           C  
-ATOM  16935  N   GLU E 138       9.270 -96.059 -93.298  1.00 47.60           N  
-ATOM  16936  CA  GLU E 138      10.290 -95.273 -93.981  1.00 52.80           C  
-ATOM  16937  C   GLU E 138      10.169 -95.380 -95.501  1.00 48.45           C  
-ATOM  16938  O   GLU E 138      10.418 -94.412 -96.222  1.00 56.67           O  
-ATOM  16939  CB  GLU E 138      11.688 -95.705 -93.528  1.00 54.07           C  
-ATOM  16940  CG  GLU E 138      12.344 -94.765 -92.520  1.00 59.29           C  
-ATOM  16941  CD  GLU E 138      12.862 -93.481 -93.156  1.00 70.23           C  
-ATOM  16942  OE1 GLU E 138      13.161 -93.495 -94.369  1.00 63.01           O  
-ATOM  16943  OE2 GLU E 138      12.970 -92.457 -92.447  1.00 66.73           O  
-ATOM  16944  N   GLU E 139       9.782 -96.555 -95.984  1.00 38.94           N  
-ATOM  16945  CA  GLU E 139       9.741 -96.805 -97.419  1.00 42.34           C  
-ATOM  16946  C   GLU E 139       8.590 -96.083 -98.107  1.00 35.21           C  
-ATOM  16947  O   GLU E 139       8.800 -95.401 -99.104  1.00 42.17           O  
-ATOM  16948  CB  GLU E 139       9.660 -98.306 -97.700  1.00 51.46           C  
-ATOM  16949  CG  GLU E 139      11.013 -98.934 -98.009  1.00 62.79           C  
-ATOM  16950  CD  GLU E 139      11.054-100.421 -97.711  1.00 73.82           C  
-ATOM  16951  OE1 GLU E 139       9.983-101.066 -97.721  1.00 68.39           O  
-ATOM  16952  OE2 GLU E 139      12.161-100.944 -97.459  1.00 73.05           O  
-ATOM  16953  N   GLU E 140       7.377 -96.221 -97.584  1.00 38.06           N  
-ATOM  16954  CA  GLU E 140       6.235 -95.607 -98.255  1.00 43.29           C  
-ATOM  16955  C   GLU E 140       5.399 -94.688 -97.370  1.00 45.17           C  
-ATOM  16956  O   GLU E 140       4.225 -94.449 -97.655  1.00 48.49           O  
-ATOM  16957  CB  GLU E 140       5.337 -96.689 -98.857  1.00 43.05           C  
-ATOM  16958  CG  GLU E 140       5.302 -97.991 -98.090  1.00 37.49           C  
-ATOM  16959  CD  GLU E 140       4.539 -99.066 -98.837  1.00 45.63           C  
-ATOM  16960  OE1 GLU E 140       5.121-100.139 -99.098  1.00 43.11           O  
-ATOM  16961  OE2 GLU E 140       3.358 -98.833 -99.172  1.00 37.01           O  
-ATOM  16962  N   TYR E 141       5.998 -94.155 -96.311  1.00 47.88           N  
-ATOM  16963  CA  TYR E 141       5.301 -93.176 -95.486  1.00 48.49           C  
-ATOM  16964  C   TYR E 141       6.213 -92.031 -95.055  1.00 58.52           C  
-ATOM  16965  O   TYR E 141       5.851 -91.238 -94.188  1.00 54.84           O  
-ATOM  16966  CB  TYR E 141       4.685 -93.845 -94.257  1.00 42.91           C  
-ATOM  16967  CG  TYR E 141       3.437 -94.645 -94.554  1.00 41.33           C  
-ATOM  16968  CD1 TYR E 141       2.222 -94.014 -94.792  1.00 36.13           C  
-ATOM  16969  CD2 TYR E 141       3.473 -96.031 -94.587  1.00 40.72           C  
-ATOM  16970  CE1 TYR E 141       1.076 -94.746 -95.061  1.00 35.40           C  
-ATOM  16971  CE2 TYR E 141       2.335 -96.770 -94.854  1.00 36.85           C  
-ATOM  16972  CZ  TYR E 141       1.141 -96.125 -95.090  1.00 35.05           C  
-ATOM  16973  OH  TYR E 141       0.010 -96.866 -95.355  1.00 36.95           O  
-ATOM  16974  N   LYS E 142       7.394 -91.944 -95.659  1.00 66.10           N  
-ATOM  16975  CA  LYS E 142       8.241 -90.778 -95.456  1.00 59.77           C  
-ATOM  16976  C   LYS E 142       7.593 -89.588 -96.140  1.00 64.07           C  
-ATOM  16977  O   LYS E 142       6.952 -89.749 -97.180  1.00 73.91           O  
-ATOM  16978  CB  LYS E 142       9.656 -91.015 -95.988  1.00 58.00           C  
-ATOM  16979  CG  LYS E 142      10.656 -91.402 -94.908  1.00 61.20           C  
-ATOM  16980  CD  LYS E 142      10.583 -90.440 -93.722  1.00 78.93           C  
-ATOM  16981  CE  LYS E 142      10.033 -91.118 -92.467  1.00 82.29           C  
-ATOM  16982  NZ  LYS E 142       9.482 -90.134 -91.488  1.00 57.97           N  
-ATOM  16983  N   ASP E 143       7.732 -88.412 -95.526  1.00 61.65           N  
-ATOM  16984  CA  ASP E 143       7.085 -87.179 -95.985  1.00 78.27           C  
-ATOM  16985  C   ASP E 143       5.561 -87.272 -95.779  1.00 66.69           C  
-ATOM  16986  O   ASP E 143       4.822 -86.309 -95.999  1.00 58.90           O  
-ATOM  16987  CB  ASP E 143       7.469 -86.885 -97.452  1.00 81.72           C  
-ATOM  16988  CG  ASP E 143       6.269 -86.705 -98.364  1.00100.18           C  
-ATOM  16989  OD1 ASP E 143       5.664 -87.720 -98.778  1.00 91.50           O  
-ATOM  16990  OD2 ASP E 143       5.941 -85.540 -98.675  1.00113.27           O  
-ATOM  16991  N   SER E 144       5.112 -88.428 -95.297  1.00 58.12           N  
-ATOM  16992  CA  SER E 144       3.699 -88.676 -95.043  1.00 52.10           C  
-ATOM  16993  C   SER E 144       3.381 -88.691 -93.547  1.00 52.49           C  
-ATOM  16994  O   SER E 144       2.340 -88.187 -93.123  1.00 42.01           O  
-ATOM  16995  CB  SER E 144       3.276 -90.001 -95.682  1.00 51.73           C  
-ATOM  16996  OG  SER E 144       1.961 -90.364 -95.299  1.00 52.98           O  
-ATOM  16997  N   VAL E 145       4.273 -89.269 -92.748  1.00 62.30           N  
-ATOM  16998  CA  VAL E 145       4.049 -89.347 -91.307  1.00 44.46           C  
-ATOM  16999  C   VAL E 145       5.064 -88.519 -90.524  1.00 41.97           C  
-ATOM  17000  O   VAL E 145       6.201 -88.330 -90.957  1.00 44.62           O  
-ATOM  17001  CB  VAL E 145       4.095 -90.804 -90.799  1.00 41.58           C  
-ATOM  17002  CG1 VAL E 145       3.046 -91.644 -91.509  1.00 48.29           C  
-ATOM  17003  CG2 VAL E 145       5.483 -91.401 -90.987  1.00 47.08           C  
-ATOM  17004  N   ASP E 146       4.639 -88.026 -89.365  1.00 46.65           N  
-ATOM  17005  CA  ASP E 146       5.510 -87.232 -88.506  1.00 53.01           C  
-ATOM  17006  C   ASP E 146       6.112 -88.089 -87.394  1.00 52.38           C  
-ATOM  17007  O   ASP E 146       7.271 -88.499 -87.475  1.00 48.10           O  
-ATOM  17008  CB  ASP E 146       4.742 -86.047 -87.910  1.00 48.40           C  
-ATOM  17009  CG  ASP E 146       5.636 -85.108 -87.117  1.00 55.59           C  
-ATOM  17010  OD1 ASP E 146       6.871 -85.147 -87.308  1.00 43.49           O  
-ATOM  17011  OD2 ASP E 146       5.100 -84.324 -86.306  1.00 57.13           O  
-ATOM  17012  N   GLN E 147       5.323 -88.357 -86.359  1.00 46.51           N  
-ATOM  17013  CA  GLN E 147       5.800 -89.147 -85.229  1.00 39.98           C  
-ATOM  17014  C   GLN E 147       5.284 -90.584 -85.257  1.00 41.42           C  
-ATOM  17015  O   GLN E 147       4.204 -90.870 -85.789  1.00 41.54           O  
-ATOM  17016  CB  GLN E 147       5.409 -88.481 -83.908  1.00 41.35           C  
-ATOM  17017  CG  GLN E 147       6.117 -87.165 -83.636  1.00 47.20           C  
-ATOM  17018  CD  GLN E 147       6.039 -86.753 -82.176  1.00 49.57           C  
-ATOM  17019  OE1 GLN E 147       5.220 -85.917 -81.796  1.00 40.59           O  
-ATOM  17020  NE2 GLN E 147       6.896 -87.343 -81.348  1.00 45.82           N  
-ATOM  17021  N   ILE E 148       6.076 -91.483 -84.679  1.00 41.89           N  
-ATOM  17022  CA  ILE E 148       5.723 -92.893 -84.599  1.00 35.86           C  
-ATOM  17023  C   ILE E 148       5.571 -93.318 -83.142  1.00 35.45           C  
-ATOM  17024  O   ILE E 148       6.491 -93.163 -82.337  1.00 40.96           O  
-ATOM  17025  CB  ILE E 148       6.776 -93.778 -85.286  1.00 30.42           C  
-ATOM  17026  CG1 ILE E 148       7.055 -93.269 -86.702  1.00 30.82           C  
-ATOM  17027  CG2 ILE E 148       6.320 -95.229 -85.303  1.00 33.90           C  
-ATOM  17028  CD1 ILE E 148       8.126 -94.048 -87.431  1.00 22.50           C  
-ATOM  17029  N   PHE E 149       4.398 -93.849 -82.812  1.00 34.10           N  
-ATOM  17030  CA  PHE E 149       4.066 -94.238 -81.446  1.00 31.48           C  
-ATOM  17031  C   PHE E 149       3.828 -95.739 -81.312  1.00 28.58           C  
-ATOM  17032  O   PHE E 149       2.930 -96.282 -81.946  1.00 27.97           O  
-ATOM  17033  CB  PHE E 149       2.814 -93.498 -80.961  1.00 24.82           C  
-ATOM  17034  CG  PHE E 149       2.956 -92.004 -80.918  1.00 29.09           C  
-ATOM  17035  CD1 PHE E 149       3.529 -91.380 -79.822  1.00 34.46           C  
-ATOM  17036  CD2 PHE E 149       2.491 -91.219 -81.961  1.00 33.56           C  
-ATOM  17037  CE1 PHE E 149       3.651 -90.000 -79.773  1.00 38.36           C  
-ATOM  17038  CE2 PHE E 149       2.608 -89.840 -81.919  1.00 36.28           C  
-ATOM  17039  CZ  PHE E 149       3.190 -89.230 -80.823  1.00 30.81           C  
-ATOM  17040  N   VAL E 150       4.622 -96.404 -80.479  1.00 28.64           N  
-ATOM  17041  CA  VAL E 150       4.322 -97.775 -80.086  1.00 30.14           C  
-ATOM  17042  C   VAL E 150       3.289 -97.746 -78.962  1.00 31.14           C  
-ATOM  17043  O   VAL E 150       3.479 -97.087 -77.925  1.00 33.49           O  
-ATOM  17044  CB  VAL E 150       5.574 -98.541 -79.636  1.00 33.41           C  
-ATOM  17045  CG1 VAL E 150       5.187 -99.895 -79.059  1.00 29.18           C  
-ATOM  17046  CG2 VAL E 150       6.530 -98.709 -80.805  1.00 28.93           C  
-ATOM  17047  N   VAL E 151       2.199 -98.474 -79.182  1.00 31.50           N  
-ATOM  17048  CA  VAL E 151       0.984 -98.315 -78.396  1.00 25.38           C  
-ATOM  17049  C   VAL E 151       0.653 -99.570 -77.574  1.00 27.97           C  
-ATOM  17050  O   VAL E 151      -0.020 -99.493 -76.543  1.00 31.43           O  
-ATOM  17051  CB  VAL E 151      -0.185 -97.932 -79.340  1.00 25.29           C  
-ATOM  17052  CG1 VAL E 151      -1.532 -98.138 -78.694  1.00 39.07           C  
-ATOM  17053  CG2 VAL E 151      -0.029 -96.488 -79.799  1.00 25.59           C  
-ATOM  17054  N   GLY E 152       1.160-100.719 -78.008  1.00 23.32           N  
-ATOM  17055  CA  GLY E 152       0.995-101.948 -77.251  1.00 22.17           C  
-ATOM  17056  C   GLY E 152       1.049-103.201 -78.107  1.00 27.36           C  
-ATOM  17057  O   GLY E 152       0.920-103.126 -79.324  1.00 35.15           O  
-ATOM  17058  N   GLY E 153       1.239-104.358 -77.478  1.00 24.07           N  
-ATOM  17059  CA  GLY E 153       1.390-104.444 -76.039  1.00 23.41           C  
-ATOM  17060  C   GLY E 153       2.779-104.905 -75.650  1.00 24.32           C  
-ATOM  17061  O   GLY E 153       3.769-104.410 -76.184  1.00 28.79           O  
-ATOM  17062  N   ALA E 154       2.844-105.867 -74.733  1.00 19.53           N  
-ATOM  17063  CA  ALA E 154       4.105-106.339 -74.162  1.00 20.20           C  
-ATOM  17064  C   ALA E 154       5.135-106.749 -75.212  1.00 28.50           C  
-ATOM  17065  O   ALA E 154       6.324-106.482 -75.056  1.00 27.24           O  
-ATOM  17066  CB  ALA E 154       3.843-107.501 -73.220  1.00 22.06           C  
-ATOM  17067  N   GLY E 155       4.673-107.401 -76.274  1.00 22.30           N  
-ATOM  17068  CA  GLY E 155       5.551-107.836 -77.343  1.00 19.84           C  
-ATOM  17069  C   GLY E 155       6.223-106.669 -78.035  1.00 31.77           C  
-ATOM  17070  O   GLY E 155       7.444-106.643 -78.190  1.00 39.89           O  
-ATOM  17071  N   LEU E 156       5.421-105.693 -78.444  1.00 30.37           N  
-ATOM  17072  CA  LEU E 156       5.949-104.519 -79.129  1.00 29.84           C  
-ATOM  17073  C   LEU E 156       6.806-103.652 -78.218  1.00 26.45           C  
-ATOM  17074  O   LEU E 156       7.794-103.083 -78.667  1.00 25.45           O  
-ATOM  17075  CB  LEU E 156       4.819-103.674 -79.717  1.00 25.87           C  
-ATOM  17076  CG  LEU E 156       4.083-104.241 -80.930  1.00 27.03           C  
-ATOM  17077  CD1 LEU E 156       3.638-103.104 -81.833  1.00 22.69           C  
-ATOM  17078  CD2 LEU E 156       4.943-105.243 -81.689  1.00 31.63           C  
-ATOM  17079  N   TYR E 157       6.424-103.538 -76.950  1.00 21.62           N  
-ATOM  17080  CA  TYR E 157       7.220-102.784 -75.987  1.00 23.58           C  
-ATOM  17081  C   TYR E 157       8.589-103.432 -75.826  1.00 33.79           C  
-ATOM  17082  O   TYR E 157       9.620-102.764 -75.929  1.00 29.63           O  
-ATOM  17083  CB  TYR E 157       6.503-102.697 -74.637  1.00 22.46           C  
-ATOM  17084  CG  TYR E 157       5.235-101.870 -74.676  1.00 23.49           C  
-ATOM  17085  CD1 TYR E 157       5.188-100.670 -75.368  1.00 22.34           C  
-ATOM  17086  CD2 TYR E 157       4.086-102.295 -74.025  1.00 27.96           C  
-ATOM  17087  CE1 TYR E 157       4.035 -99.914 -75.406  1.00 24.05           C  
-ATOM  17088  CE2 TYR E 157       2.925-101.550 -74.062  1.00 20.33           C  
-ATOM  17089  CZ  TYR E 157       2.906-100.362 -74.755  1.00 20.14           C  
-ATOM  17090  OH  TYR E 157       1.752 -99.618 -74.783  1.00 27.36           O  
-ATOM  17091  N   GLU E 158       8.579-104.740 -75.582  1.00 32.11           N  
-ATOM  17092  CA  GLU E 158       9.796-105.539 -75.471  1.00 33.78           C  
-ATOM  17093  C   GLU E 158      10.702-105.375 -76.688  1.00 31.82           C  
-ATOM  17094  O   GLU E 158      11.888-105.079 -76.549  1.00 34.46           O  
-ATOM  17095  CB  GLU E 158       9.440-107.019 -75.280  1.00 40.37           C  
-ATOM  17096  CG  GLU E 158      10.627-107.968 -75.337  1.00 64.44           C  
-ATOM  17097  CD  GLU E 158      11.392-108.044 -74.026  1.00 74.46           C  
-ATOM  17098  OE1 GLU E 158      12.352-108.842 -73.944  1.00 83.19           O  
-ATOM  17099  OE2 GLU E 158      11.033-107.315 -73.076  1.00 69.38           O  
-ATOM  17100  N   ALA E 159      10.132-105.564 -77.875  1.00 29.21           N  
-ATOM  17101  CA  ALA E 159      10.883-105.458 -79.123  1.00 30.65           C  
-ATOM  17102  C   ALA E 159      11.478-104.067 -79.308  1.00 30.42           C  
-ATOM  17103  O   ALA E 159      12.663-103.926 -79.607  1.00 33.91           O  
-ATOM  17104  CB  ALA E 159       9.991-105.805 -80.304  1.00 33.81           C  
-ATOM  17105  N   ALA E 160      10.645-103.048 -79.127  1.00 31.33           N  
-ATOM  17106  CA  ALA E 160      11.060-101.659 -79.290  1.00 31.08           C  
-ATOM  17107  C   ALA E 160      12.154-101.279 -78.302  1.00 31.63           C  
-ATOM  17108  O   ALA E 160      13.017-100.459 -78.608  1.00 34.66           O  
-ATOM  17109  CB  ALA E 160       9.867-100.731 -79.134  1.00 26.51           C  
-ATOM  17110  N   LEU E 161      12.110-101.874 -77.116  1.00 36.38           N  
-ATOM  17111  CA  LEU E 161      13.136-101.631 -76.113  1.00 32.02           C  
-ATOM  17112  C   LEU E 161      14.413-102.381 -76.466  1.00 27.93           C  
-ATOM  17113  O   LEU E 161      15.513-101.942 -76.138  1.00 22.66           O  
-ATOM  17114  CB  LEU E 161      12.635-102.036 -74.727  1.00 33.24           C  
-ATOM  17115  CG  LEU E 161      12.416-100.872 -73.757  1.00 23.11           C  
-ATOM  17116  CD1 LEU E 161      12.023 -99.610 -74.506  1.00 15.66           C  
-ATOM  17117  CD2 LEU E 161      11.359-101.229 -72.720  1.00 33.69           C  
-ATOM  17118  N   SER E 162      14.257-103.512 -77.148  1.00 33.62           N  
-ATOM  17119  CA  SER E 162      15.398-104.294 -77.608  1.00 32.02           C  
-ATOM  17120  C   SER E 162      16.158-103.549 -78.701  1.00 34.30           C  
-ATOM  17121  O   SER E 162      17.372-103.377 -78.615  1.00 34.84           O  
-ATOM  17122  CB  SER E 162      14.941-105.664 -78.114  1.00 30.56           C  
-ATOM  17123  OG  SER E 162      14.487-106.476 -77.044  1.00 56.78           O  
-ATOM  17124  N   LEU E 163      15.430-103.093 -79.716  1.00 34.56           N  
-ATOM  17125  CA  LEU E 163      16.015-102.371 -80.841  1.00 28.91           C  
-ATOM  17126  C   LEU E 163      16.655-101.059 -80.407  1.00 31.34           C  
-ATOM  17127  O   LEU E 163      17.539-100.540 -81.087  1.00 35.90           O  
-ATOM  17128  CB  LEU E 163      14.950-102.100 -81.903  1.00 23.28           C  
-ATOM  17129  CG  LEU E 163      14.174-103.330 -82.367  1.00 30.00           C  
-ATOM  17130  CD1 LEU E 163      13.078-102.943 -83.346  1.00 40.11           C  
-ATOM  17131  CD2 LEU E 163      15.119-104.349 -82.979  1.00 36.13           C  
-ATOM  17132  N   GLY E 164      16.199-100.523 -79.280  1.00 33.45           N  
-ATOM  17133  CA  GLY E 164      16.736 -99.278 -78.763  1.00 39.04           C  
-ATOM  17134  C   GLY E 164      16.282 -98.081 -79.572  1.00 39.46           C  
-ATOM  17135  O   GLY E 164      16.915 -97.027 -79.551  1.00 56.17           O  
-ATOM  17136  N   VAL E 165      15.175 -98.246 -80.287  1.00 34.97           N  
-ATOM  17137  CA  VAL E 165      14.633 -97.185 -81.126  1.00 36.13           C  
-ATOM  17138  C   VAL E 165      13.789 -96.208 -80.310  1.00 37.13           C  
-ATOM  17139  O   VAL E 165      13.383 -95.156 -80.808  1.00 45.27           O  
-ATOM  17140  CB  VAL E 165      13.781 -97.763 -82.273  1.00 36.94           C  
-ATOM  17141  CG1 VAL E 165      14.662 -98.529 -83.246  1.00 42.13           C  
-ATOM  17142  CG2 VAL E 165      12.688 -98.666 -81.726  1.00 27.89           C  
-ATOM  17143  N   ALA E 166      13.538 -96.558 -79.052  1.00 33.63           N  
-ATOM  17144  CA  ALA E 166      12.690 -95.751 -78.182  1.00 35.61           C  
-ATOM  17145  C   ALA E 166      13.446 -94.572 -77.584  1.00 35.67           C  
-ATOM  17146  O   ALA E 166      14.408 -94.751 -76.839  1.00 42.55           O  
-ATOM  17147  CB  ALA E 166      12.102 -96.612 -77.079  1.00 37.65           C  
-ATOM  17148  N   SER E 167      12.994 -93.366 -77.909  1.00 28.81           N  
-ATOM  17149  CA  SER E 167      13.618 -92.150 -77.405  1.00 31.11           C  
-ATOM  17150  C   SER E 167      12.900 -91.628 -76.164  1.00 35.83           C  
-ATOM  17151  O   SER E 167      13.536 -91.167 -75.211  1.00 39.63           O  
-ATOM  17152  CB  SER E 167      13.632 -91.074 -78.490  1.00 31.01           C  
-ATOM  17153  OG  SER E 167      12.316 -90.710 -78.861  1.00 28.49           O  
-ATOM  17154  N   HIS E 168      11.572 -91.702 -76.189  1.00 36.48           N  
-ATOM  17155  CA  HIS E 168      10.751 -91.207 -75.091  1.00 31.87           C  
-ATOM  17156  C   HIS E 168       9.660 -92.188 -74.675  1.00 31.16           C  
-ATOM  17157  O   HIS E 168       9.050 -92.849 -75.516  1.00 34.33           O  
-ATOM  17158  CB  HIS E 168      10.115 -89.871 -75.469  1.00 28.25           C  
-ATOM  17159  CG  HIS E 168      11.110 -88.784 -75.729  1.00 39.12           C  
-ATOM  17160  ND1 HIS E 168      11.571 -88.485 -76.992  1.00 49.79           N  
-ATOM  17161  CD2 HIS E 168      11.736 -87.929 -74.887  1.00 40.69           C  
-ATOM  17162  CE1 HIS E 168      12.435 -87.488 -76.918  1.00 52.80           C  
-ATOM  17163  NE2 HIS E 168      12.553 -87.132 -75.651  1.00 45.45           N  
-ATOM  17164  N   LEU E 169       9.414 -92.267 -73.371  1.00 23.59           N  
-ATOM  17165  CA  LEU E 169       8.332 -93.094 -72.850  1.00 22.27           C  
-ATOM  17166  C   LEU E 169       7.238 -92.236 -72.221  1.00 27.58           C  
-ATOM  17167  O   LEU E 169       7.472 -91.568 -71.216  1.00 28.12           O  
-ATOM  17168  CB  LEU E 169       8.858 -94.089 -71.816  1.00 14.98           C  
-ATOM  17169  CG  LEU E 169      10.033 -94.980 -72.212  1.00 22.36           C  
-ATOM  17170  CD1 LEU E 169      10.326 -95.985 -71.110  1.00 23.12           C  
-ATOM  17171  CD2 LEU E 169       9.748 -95.689 -73.518  1.00 32.94           C  
-ATOM  17172  N   TYR E 170       6.048 -92.249 -72.813  1.00 25.97           N  
-ATOM  17173  CA  TYR E 170       4.899 -91.580 -72.210  1.00 15.74           C  
-ATOM  17174  C   TYR E 170       4.192 -92.544 -71.272  1.00 18.42           C  
-ATOM  17175  O   TYR E 170       3.324 -93.306 -71.694  1.00 22.22           O  
-ATOM  17176  CB  TYR E 170       3.925 -91.073 -73.275  1.00 15.80           C  
-ATOM  17177  CG  TYR E 170       4.449 -89.916 -74.094  1.00 28.13           C  
-ATOM  17178  CD1 TYR E 170       4.339 -88.608 -73.637  1.00 32.38           C  
-ATOM  17179  CD2 TYR E 170       5.048 -90.130 -75.330  1.00 41.51           C  
-ATOM  17180  CE1 TYR E 170       4.817 -87.548 -74.382  1.00 23.32           C  
-ATOM  17181  CE2 TYR E 170       5.528 -89.075 -76.082  1.00 37.78           C  
-ATOM  17182  CZ  TYR E 170       5.409 -87.786 -75.602  1.00 29.58           C  
-ATOM  17183  OH  TYR E 170       5.881 -86.728 -76.344  1.00 32.05           O  
-ATOM  17184  N   ILE E 171       4.563 -92.513 -69.998  1.00 14.96           N  
-ATOM  17185  CA  ILE E 171       4.019 -93.473 -69.048  1.00 16.39           C  
-ATOM  17186  C   ILE E 171       2.950 -92.869 -68.157  1.00 17.79           C  
-ATOM  17187  O   ILE E 171       3.179 -91.862 -67.487  1.00 19.16           O  
-ATOM  17188  CB  ILE E 171       5.114 -94.068 -68.145  1.00 21.11           C  
-ATOM  17189  CG1 ILE E 171       6.227 -94.695 -68.989  1.00 15.41           C  
-ATOM  17190  CG2 ILE E 171       4.506 -95.089 -67.188  1.00 17.98           C  
-ATOM  17191  CD1 ILE E 171       7.233 -95.479 -68.180  1.00 10.97           C  
-ATOM  17192  N   THR E 172       1.780 -93.497 -68.154  1.00 16.06           N  
-ATOM  17193  CA  THR E 172       0.739 -93.148 -67.204  1.00 15.93           C  
-ATOM  17194  C   THR E 172       0.835 -94.091 -66.013  1.00 16.67           C  
-ATOM  17195  O   THR E 172       0.402 -95.241 -66.087  1.00 19.10           O  
-ATOM  17196  CB  THR E 172      -0.668 -93.229 -67.825  1.00 19.88           C  
-ATOM  17197  OG1 THR E 172      -0.745 -92.363 -68.963  1.00 20.92           O  
-ATOM  17198  CG2 THR E 172      -1.722 -92.813 -66.813  1.00 22.07           C  
-ATOM  17199  N   ARG E 173       1.425 -93.603 -64.925  1.00 19.08           N  
-ATOM  17200  CA  ARG E 173       1.566 -94.387 -63.703  1.00 17.22           C  
-ATOM  17201  C   ARG E 173       0.253 -94.497 -62.959  1.00 14.49           C  
-ATOM  17202  O   ARG E 173      -0.203 -93.525 -62.352  1.00 18.31           O  
-ATOM  17203  CB  ARG E 173       2.616 -93.773 -62.777  1.00 14.43           C  
-ATOM  17204  CG  ARG E 173       3.984 -93.636 -63.402  1.00 17.50           C  
-ATOM  17205  CD  ARG E 173       4.654 -92.373 -62.927  1.00 17.83           C  
-ATOM  17206  NE  ARG E 173       5.477 -92.578 -61.745  1.00 11.54           N  
-ATOM  17207  CZ  ARG E 173       5.752 -91.626 -60.862  1.00 13.83           C  
-ATOM  17208  NH1 ARG E 173       5.252 -90.407 -61.014  1.00  9.29           N  
-ATOM  17209  NH2 ARG E 173       6.517 -91.895 -59.818  1.00 32.09           N  
-ATOM  17210  N   VAL E 174      -0.342 -95.686 -63.023  1.00 13.58           N  
-ATOM  17211  CA  VAL E 174      -1.504 -96.039 -62.216  1.00 15.52           C  
-ATOM  17212  C   VAL E 174      -1.033 -96.445 -60.821  1.00 15.46           C  
-ATOM  17213  O   VAL E 174      -0.241 -97.373 -60.678  1.00 14.33           O  
-ATOM  17214  CB  VAL E 174      -2.302 -97.186 -62.856  1.00 13.16           C  
-ATOM  17215  CG1 VAL E 174      -3.532 -97.507 -62.036  1.00 12.36           C  
-ATOM  17216  CG2 VAL E 174      -2.681 -96.824 -64.287  1.00 12.45           C  
-ATOM  17217  N   ALA E 175      -1.506 -95.746 -59.794  1.00 13.48           N  
-ATOM  17218  CA  ALA E 175      -0.971 -95.932 -58.445  1.00 15.91           C  
-ATOM  17219  C   ALA E 175      -1.496 -97.191 -57.750  1.00 18.42           C  
-ATOM  17220  O   ALA E 175      -0.863 -97.700 -56.825  1.00 18.89           O  
-ATOM  17221  CB  ALA E 175      -1.268 -94.708 -57.594  1.00 16.57           C  
-ATOM  17222  N   ARG E 176      -2.650 -97.684 -58.189  1.00 14.48           N  
-ATOM  17223  CA  ARG E 176      -3.234 -98.893 -57.613  1.00 11.67           C  
-ATOM  17224  C   ARG E 176      -2.721-100.147 -58.300  1.00 16.20           C  
-ATOM  17225  O   ARG E 176      -2.370-100.125 -59.478  1.00 19.81           O  
-ATOM  17226  CB  ARG E 176      -4.755 -98.863 -57.713  1.00 20.86           C  
-ATOM  17227  CG  ARG E 176      -5.432 -97.905 -56.766  1.00 21.01           C  
-ATOM  17228  CD  ARG E 176      -6.935 -97.921 -56.984  1.00 23.41           C  
-ATOM  17229  NE  ARG E 176      -7.493 -99.268 -56.897  1.00 19.53           N  
-ATOM  17230  CZ  ARG E 176      -8.795 -99.533 -56.863  1.00 26.20           C  
-ATOM  17231  NH1 ARG E 176      -9.215-100.787 -56.786  1.00 41.43           N  
-ATOM  17232  NH2 ARG E 176      -9.678 -98.543 -56.901  1.00 20.67           N  
-ATOM  17233  N   GLU E 177      -2.692-101.249 -57.561  1.00 19.70           N  
-ATOM  17234  CA  GLU E 177      -2.308-102.526 -58.138  1.00 15.94           C  
-ATOM  17235  C   GLU E 177      -3.559-103.306 -58.534  1.00 24.61           C  
-ATOM  17236  O   GLU E 177      -4.518-103.400 -57.767  1.00 29.28           O  
-ATOM  17237  CB  GLU E 177      -1.451-103.327 -57.158  1.00 17.98           C  
-ATOM  17238  CG  GLU E 177      -0.678-104.452 -57.814  1.00 25.49           C  
-ATOM  17239  CD  GLU E 177       0.070-103.990 -59.049  1.00 32.23           C  
-ATOM  17240  OE1 GLU E 177       0.994-103.158 -58.914  1.00 31.12           O  
-ATOM  17241  OE2 GLU E 177      -0.278-104.455 -60.156  1.00 32.87           O  
-ATOM  17242  N   PHE E 178      -3.551-103.843 -59.749  1.00 26.02           N  
-ATOM  17243  CA  PHE E 178      -4.683-104.606 -60.258  1.00 19.22           C  
-ATOM  17244  C   PHE E 178      -4.231-105.977 -60.743  1.00 23.48           C  
-ATOM  17245  O   PHE E 178      -3.058-106.164 -61.072  1.00 23.99           O  
-ATOM  17246  CB  PHE E 178      -5.378-103.847 -61.394  1.00 17.73           C  
-ATOM  17247  CG  PHE E 178      -6.134-102.634 -60.941  1.00 18.55           C  
-ATOM  17248  CD1 PHE E 178      -7.460-102.733 -60.555  1.00 24.08           C  
-ATOM  17249  CD2 PHE E 178      -5.521-101.393 -60.905  1.00 22.76           C  
-ATOM  17250  CE1 PHE E 178      -8.161-101.616 -60.137  1.00 31.37           C  
-ATOM  17251  CE2 PHE E 178      -6.215-100.273 -60.490  1.00 21.37           C  
-ATOM  17252  CZ  PHE E 178      -7.536-100.384 -60.104  1.00 29.05           C  
-ATOM  17253  N   PRO E 179      -5.159-106.946 -60.770  1.00 19.43           N  
-ATOM  17254  CA  PRO E 179      -4.883-108.256 -61.367  1.00 23.27           C  
-ATOM  17255  C   PRO E 179      -4.447-108.123 -62.823  1.00 21.79           C  
-ATOM  17256  O   PRO E 179      -5.187-107.565 -63.633  1.00 20.09           O  
-ATOM  17257  CB  PRO E 179      -6.225-108.979 -61.253  1.00 23.26           C  
-ATOM  17258  CG  PRO E 179      -6.871-108.359 -60.064  1.00 18.87           C  
-ATOM  17259  CD  PRO E 179      -6.470-106.915 -60.098  1.00 14.55           C  
-ATOM  17260  N   CYS E 180      -3.257-108.625 -63.141  1.00 20.67           N  
-ATOM  17261  CA  CYS E 180      -2.702-108.499 -64.485  1.00 24.02           C  
-ATOM  17262  C   CYS E 180      -2.039-109.787 -64.964  1.00 22.57           C  
-ATOM  17263  O   CYS E 180      -1.427-110.510 -64.179  1.00 30.15           O  
-ATOM  17264  CB  CYS E 180      -1.690-107.354 -64.531  1.00 27.60           C  
-ATOM  17265  SG  CYS E 180      -2.389-105.726 -64.195  1.00 27.24           S  
-ATOM  17266  N   ASP E 181      -2.159-110.068 -66.258  1.00 20.21           N  
-ATOM  17267  CA  ASP E 181      -1.500-111.227 -66.848  1.00 21.22           C  
-ATOM  17268  C   ASP E 181      -0.518-110.802 -67.937  1.00 24.57           C  
-ATOM  17269  O   ASP E 181       0.198-111.629 -68.501  1.00 25.47           O  
-ATOM  17270  CB  ASP E 181      -2.532-112.216 -67.407  1.00 21.97           C  
-ATOM  17271  CG  ASP E 181      -3.533-111.563 -68.352  1.00 26.99           C  
-ATOM  17272  OD1 ASP E 181      -3.188-110.555 -69.002  1.00 37.60           O  
-ATOM  17273  OD2 ASP E 181      -4.672-112.067 -68.453  1.00 27.11           O  
-ATOM  17274  N   VAL E 182      -0.497-109.506 -68.232  1.00 23.25           N  
-ATOM  17275  CA  VAL E 182       0.430-108.953 -69.215  1.00 21.13           C  
-ATOM  17276  C   VAL E 182       1.140-107.732 -68.639  1.00 18.28           C  
-ATOM  17277  O   VAL E 182       0.495-106.808 -68.145  1.00 16.14           O  
-ATOM  17278  CB  VAL E 182      -0.288-108.563 -70.520  1.00 24.97           C  
-ATOM  17279  CG1 VAL E 182       0.663-107.837 -71.453  1.00 26.87           C  
-ATOM  17280  CG2 VAL E 182      -0.868-109.796 -71.198  1.00 24.30           C  
-ATOM  17281  N   PHE E 183       2.469-107.731 -68.708  1.00 17.21           N  
-ATOM  17282  CA  PHE E 183       3.270-106.702 -68.050  1.00 17.51           C  
-ATOM  17283  C   PHE E 183       4.177-105.931 -69.002  1.00 20.00           C  
-ATOM  17284  O   PHE E 183       4.679-106.480 -69.982  1.00 28.30           O  
-ATOM  17285  CB  PHE E 183       4.130-107.327 -66.949  1.00 15.27           C  
-ATOM  17286  CG  PHE E 183       3.339-107.982 -65.858  1.00 13.27           C  
-ATOM  17287  CD1 PHE E 183       2.908-109.289 -65.985  1.00 16.25           C  
-ATOM  17288  CD2 PHE E 183       3.034-107.292 -64.699  1.00 14.96           C  
-ATOM  17289  CE1 PHE E 183       2.179-109.893 -64.979  1.00 24.81           C  
-ATOM  17290  CE2 PHE E 183       2.307-107.887 -63.690  1.00 16.98           C  
-ATOM  17291  CZ  PHE E 183       1.879-109.190 -63.828  1.00 22.36           C  
-ATOM  17292  N   PHE E 184       4.389-104.654 -68.700  1.00 19.64           N  
-ATOM  17293  CA  PHE E 184       5.391-103.860 -69.399  1.00 20.72           C  
-ATOM  17294  C   PHE E 184       6.766-104.356 -68.964  1.00 29.03           C  
-ATOM  17295  O   PHE E 184       6.989-104.598 -67.777  1.00 28.59           O  
-ATOM  17296  CB  PHE E 184       5.219-102.369 -69.094  1.00 20.37           C  
-ATOM  17297  CG  PHE E 184       6.082-101.469 -69.933  1.00 25.46           C  
-ATOM  17298  CD1 PHE E 184       5.661-101.055 -71.186  1.00 27.41           C  
-ATOM  17299  CD2 PHE E 184       7.313-101.034 -69.468  1.00 26.88           C  
-ATOM  17300  CE1 PHE E 184       6.450-100.224 -71.962  1.00 19.64           C  
-ATOM  17301  CE2 PHE E 184       8.107-100.205 -70.241  1.00 24.97           C  
-ATOM  17302  CZ  PHE E 184       7.674 -99.800 -71.489  1.00 19.08           C  
-ATOM  17303  N   PRO E 185       7.691-104.519 -69.922  1.00 25.02           N  
-ATOM  17304  CA  PRO E 185       9.002-105.110 -69.625  1.00 23.32           C  
-ATOM  17305  C   PRO E 185       9.808-104.320 -68.596  1.00 29.09           C  
-ATOM  17306  O   PRO E 185       9.517-103.151 -68.338  1.00 26.67           O  
-ATOM  17307  CB  PRO E 185       9.705-105.098 -70.985  1.00 20.78           C  
-ATOM  17308  CG  PRO E 185       9.004-104.041 -71.770  1.00 21.66           C  
-ATOM  17309  CD  PRO E 185       7.576-104.119 -71.334  1.00 21.30           C  
-ATOM  17310  N   ALA E 186      10.807-104.969 -68.008  1.00 27.61           N  
-ATOM  17311  CA  ALA E 186      11.705-104.299 -67.079  1.00 24.39           C  
-ATOM  17312  C   ALA E 186      12.688-103.438 -67.861  1.00 24.39           C  
-ATOM  17313  O   ALA E 186      13.274-103.890 -68.843  1.00 33.70           O  
-ATOM  17314  CB  ALA E 186      12.442-105.311 -66.215  1.00 23.94           C  
-ATOM  17315  N   PHE E 187      12.858-102.193 -67.434  1.00 28.23           N  
-ATOM  17316  CA  PHE E 187      13.739-101.272 -68.140  1.00 33.59           C  
-ATOM  17317  C   PHE E 187      14.563-100.445 -67.162  1.00 31.34           C  
-ATOM  17318  O   PHE E 187      14.084-100.100 -66.084  1.00 33.29           O  
-ATOM  17319  CB  PHE E 187      12.929-100.355 -69.064  1.00 31.58           C  
-ATOM  17320  CG  PHE E 187      11.965 -99.456 -68.343  1.00 28.04           C  
-ATOM  17321  CD1 PHE E 187      10.698 -99.902 -68.010  1.00 27.08           C  
-ATOM  17322  CD2 PHE E 187      12.320 -98.159 -68.011  1.00 28.81           C  
-ATOM  17323  CE1 PHE E 187       9.807 -99.075 -67.353  1.00 26.85           C  
-ATOM  17324  CE2 PHE E 187      11.434 -97.330 -67.353  1.00 21.27           C  
-ATOM  17325  CZ  PHE E 187      10.175 -97.788 -67.024  1.00 18.94           C  
-ATOM  17326  N   PRO E 188      15.812-100.128 -67.536  1.00 30.16           N  
-ATOM  17327  CA  PRO E 188      16.689 -99.309 -66.694  1.00 35.60           C  
-ATOM  17328  C   PRO E 188      16.049 -97.970 -66.346  1.00 35.98           C  
-ATOM  17329  O   PRO E 188      15.784 -97.158 -67.234  1.00 40.39           O  
-ATOM  17330  CB  PRO E 188      17.940 -99.115 -67.565  1.00 38.53           C  
-ATOM  17331  CG  PRO E 188      17.505 -99.446 -68.955  1.00 32.13           C  
-ATOM  17332  CD  PRO E 188      16.467-100.504 -68.799  1.00 37.51           C  
-ATOM  17333  N   GLY E 189      15.786 -97.761 -65.062  1.00 33.13           N  
-ATOM  17334  CA  GLY E 189      15.175 -96.530 -64.606  1.00 33.07           C  
-ATOM  17335  C   GLY E 189      13.691 -96.686 -64.345  1.00 29.21           C  
-ATOM  17336  O   GLY E 189      12.947 -95.709 -64.392  1.00 33.98           O  
-ATOM  17337  N   ASP E 190      13.257 -97.912 -64.067  1.00 25.04           N  
-ATOM  17338  CA  ASP E 190      11.855 -98.163 -63.741  1.00 24.64           C  
-ATOM  17339  C   ASP E 190      11.565 -97.907 -62.258  1.00 23.91           C  
-ATOM  17340  O   ASP E 190      10.487 -98.227 -61.753  1.00 21.51           O  
-ATOM  17341  CB  ASP E 190      11.466 -99.591 -64.122  1.00 23.12           C  
-ATOM  17342  CG  ASP E 190      12.489-100.610 -63.676  1.00 31.15           C  
-ATOM  17343  OD1 ASP E 190      13.413-100.237 -62.921  1.00 39.02           O  
-ATOM  17344  OD2 ASP E 190      12.367-101.784 -64.082  1.00 30.68           O  
-ATOM  17345  N   ASP E 191      12.528 -97.302 -61.571  1.00 26.78           N  
-ATOM  17346  CA  ASP E 191      12.369 -96.953 -60.165  1.00 20.97           C  
-ATOM  17347  C   ASP E 191      11.281 -95.898 -59.971  1.00 29.99           C  
-ATOM  17348  O   ASP E 191      10.906 -95.590 -58.842  1.00 35.50           O  
-ATOM  17349  CB  ASP E 191      13.695 -96.454 -59.586  1.00 16.39           C  
-ATOM  17350  N   ILE E 192      10.778 -95.345 -61.074  1.00 24.82           N  
-ATOM  17351  CA  ILE E 192       9.663 -94.400 -61.022  1.00 26.49           C  
-ATOM  17352  C   ILE E 192       8.330 -95.119 -60.862  1.00 25.30           C  
-ATOM  17353  O   ILE E 192       7.283 -94.485 -60.768  1.00 29.56           O  
-ATOM  17354  CB  ILE E 192       9.591 -93.517 -62.285  1.00 21.18           C  
-ATOM  17355  CG1 ILE E 192      10.258 -94.217 -63.467  1.00 19.34           C  
-ATOM  17356  CG2 ILE E 192      10.247 -92.175 -62.037  1.00 23.13           C  
-ATOM  17357  CD1 ILE E 192       9.407 -95.274 -64.120  1.00 21.10           C  
-ATOM  17358  N   LEU E 193       8.374 -96.445 -60.842  1.00 22.96           N  
-ATOM  17359  CA  LEU E 193       7.165 -97.244 -60.689  1.00 19.39           C  
-ATOM  17360  C   LEU E 193       7.022 -97.766 -59.265  1.00 21.71           C  
-ATOM  17361  O   LEU E 193       6.001 -97.546 -58.613  1.00 30.04           O  
-ATOM  17362  CB  LEU E 193       7.174 -98.403 -61.683  1.00 20.65           C  
-ATOM  17363  CG  LEU E 193       7.223 -97.959 -63.147  1.00 25.90           C  
-ATOM  17364  CD1 LEU E 193       7.581 -99.116 -64.059  1.00 22.63           C  
-ATOM  17365  CD2 LEU E 193       5.904 -97.321 -63.569  1.00 22.03           C  
-ATOM  17366  N   SER E 194       8.048 -98.459 -58.787  1.00 18.90           N  
-ATOM  17367  CA  SER E 194       8.057 -98.965 -57.421  1.00 19.22           C  
-ATOM  17368  C   SER E 194       9.490 -99.113 -56.922  1.00 25.11           C  
-ATOM  17369  O   SER E 194      10.437 -98.729 -57.609  1.00 25.20           O  
-ATOM  17370  CB  SER E 194       7.320-100.302 -57.332  1.00 23.18           C  
-ATOM  17371  OG  SER E 194       7.944-101.287 -58.138  1.00 37.01           O  
-ATOM  17372  N   ASN E 195       9.649 -99.661 -55.722  1.00 25.11           N  
-ATOM  17373  CA  ASN E 195      10.976 -99.854 -55.155  1.00 18.86           C  
-ATOM  17374  C   ASN E 195      11.623-101.130 -55.684  1.00 26.70           C  
-ATOM  17375  O   ASN E 195      10.932-102.081 -56.050  1.00 28.99           O  
-ATOM  17376  CB  ASN E 195      10.903 -99.885 -53.627  1.00 24.40           C  
-ATOM  17377  CG  ASN E 195      10.443 -98.562 -53.037  1.00 34.68           C  
-ATOM  17378  OD1 ASN E 195      10.062 -97.642 -53.764  1.00 31.80           O  
-ATOM  17379  ND2 ASN E 195      10.472 -98.461 -51.713  1.00 30.07           N  
-ATOM  17380  N   LYS E 196      12.951-101.144 -55.732  1.00 30.59           N  
-ATOM  17381  CA  LYS E 196      13.685-102.318 -56.193  1.00 39.36           C  
-ATOM  17382  C   LYS E 196      14.206-103.151 -55.023  1.00 46.48           C  
-ATOM  17383  O   LYS E 196      14.208-104.384 -55.075  1.00 44.90           O  
-ATOM  17384  CB  LYS E 196      14.847-101.904 -57.098  1.00 42.33           C  
-ATOM  17385  CG  LYS E 196      14.438-101.554 -58.521  1.00 35.06           C  
-ATOM  17386  CD  LYS E 196      13.649-102.692 -59.151  1.00 37.77           C  
-ATOM  17387  CE  LYS E 196      13.604-102.567 -60.662  1.00 32.21           C  
-ATOM  17388  NZ  LYS E 196      14.965-102.664 -61.253  1.00 25.30           N  
-ATOM  17389  N   ALA E 225      22.252 -97.539 -71.425  1.00 45.23           N  
-ATOM  17390  CA  ALA E 225      21.474 -96.304 -71.410  1.00 59.27           C  
-ATOM  17391  C   ALA E 225      20.248 -96.422 -70.506  1.00 48.45           C  
-ATOM  17392  O   ALA E 225      19.535 -97.425 -70.541  1.00 39.51           O  
-ATOM  17393  CB  ALA E 225      21.053 -95.929 -72.822  1.00 64.70           C  
-ATOM  17394  N   THR E 226      20.005 -95.392 -69.700  1.00 52.29           N  
-ATOM  17395  CA  THR E 226      18.859 -95.381 -68.796  1.00 42.07           C  
-ATOM  17396  C   THR E 226      17.777 -94.408 -69.265  1.00 38.48           C  
-ATOM  17397  O   THR E 226      18.066 -93.423 -69.947  1.00 42.56           O  
-ATOM  17398  CB  THR E 226      19.275 -95.010 -67.356  1.00 35.90           C  
-ATOM  17399  OG1 THR E 226      18.117 -94.977 -66.513  1.00 43.07           O  
-ATOM  17400  CG2 THR E 226      19.954 -93.651 -67.326  1.00 41.55           C  
-ATOM  17401  N   TYR E 227      16.531 -94.700 -68.902  1.00 34.55           N  
-ATOM  17402  CA  TYR E 227      15.401 -93.838 -69.238  1.00 34.70           C  
-ATOM  17403  C   TYR E 227      15.028 -92.952 -68.052  1.00 40.70           C  
-ATOM  17404  O   TYR E 227      14.362 -93.404 -67.120  1.00 40.83           O  
-ATOM  17405  CB  TYR E 227      14.194 -94.676 -69.669  1.00 31.00           C  
-ATOM  17406  CG  TYR E 227      14.368 -95.389 -70.994  1.00 32.35           C  
-ATOM  17407  CD1 TYR E 227      15.033 -96.605 -71.070  1.00 32.59           C  
-ATOM  17408  CD2 TYR E 227      13.855 -94.849 -72.167  1.00 32.23           C  
-ATOM  17409  CE1 TYR E 227      15.190 -97.260 -72.279  1.00 36.66           C  
-ATOM  17410  CE2 TYR E 227      14.007 -95.495 -73.379  1.00 30.81           C  
-ATOM  17411  CZ  TYR E 227      14.675 -96.700 -73.431  1.00 37.82           C  
-ATOM  17412  OH  TYR E 227      14.827 -97.343 -74.640  1.00 39.84           O  
-ATOM  17413  N   ARG E 228      15.449 -91.690 -68.091  1.00 41.36           N  
-ATOM  17414  CA  ARG E 228      15.242 -90.789 -66.957  1.00 37.90           C  
-ATOM  17415  C   ARG E 228      14.078 -89.823 -67.170  1.00 32.45           C  
-ATOM  17416  O   ARG E 228      13.886 -89.310 -68.268  1.00 32.73           O  
-ATOM  17417  CB  ARG E 228      16.520 -89.997 -66.660  1.00 37.84           C  
-ATOM  17418  CG  ARG E 228      17.633 -90.822 -66.036  1.00 49.84           C  
-ATOM  17419  CD  ARG E 228      18.611 -89.936 -65.279  1.00 52.52           C  
-ATOM  17420  NE  ARG E 228      19.041 -88.792 -66.078  1.00 69.94           N  
-ATOM  17421  CZ  ARG E 228      20.018 -88.834 -66.978  1.00 79.43           C  
-ATOM  17422  NH1 ARG E 228      20.669 -89.970 -67.200  1.00 69.80           N  
-ATOM  17423  NH2 ARG E 228      20.344 -87.742 -67.658  1.00 66.50           N  
-ATOM  17424  N   PRO E 229      13.302 -89.566 -66.103  1.00 30.51           N  
-ATOM  17425  CA  PRO E 229      12.136 -88.678 -66.154  1.00 22.41           C  
-ATOM  17426  C   PRO E 229      12.505 -87.216 -66.362  1.00 29.16           C  
-ATOM  17427  O   PRO E 229      13.487 -86.734 -65.796  1.00 31.35           O  
-ATOM  17428  CB  PRO E 229      11.486 -88.880 -64.784  1.00 26.44           C  
-ATOM  17429  CG  PRO E 229      12.604 -89.277 -63.902  1.00 35.46           C  
-ATOM  17430  CD  PRO E 229      13.509 -90.117 -64.753  1.00 30.30           C  
-ATOM  17431  N   ILE E 230      11.711 -86.522 -67.169  1.00 36.06           N  
-ATOM  17432  CA  ILE E 230      11.943 -85.113 -67.462  1.00 32.00           C  
-ATOM  17433  C   ILE E 230      10.659 -84.323 -67.171  1.00 35.92           C  
-ATOM  17434  O   ILE E 230      10.643 -83.086 -67.156  1.00 41.03           O  
-ATOM  17435  CB  ILE E 230      12.386 -84.922 -68.935  1.00 26.32           C  
-ATOM  17436  CG1 ILE E 230      13.200 -83.639 -69.097  1.00 61.50           C  
-ATOM  17437  CG2 ILE E 230      11.186 -84.960 -69.879  1.00 17.72           C  
-ATOM  17438  CD1 ILE E 230      14.663 -83.872 -69.449  1.00 74.11           C  
-ATOM  17439  N   PHE E 231       9.594 -85.073 -66.906  1.00 25.57           N  
-ATOM  17440  CA  PHE E 231       8.245 -84.545 -66.757  1.00 22.97           C  
-ATOM  17441  C   PHE E 231       7.519 -85.368 -65.701  1.00 29.66           C  
-ATOM  17442  O   PHE E 231       7.410 -86.583 -65.840  1.00 29.58           O  
-ATOM  17443  CB  PHE E 231       7.511 -84.608 -68.106  1.00 28.08           C  
-ATOM  17444  CG  PHE E 231       6.071 -84.142 -68.068  1.00 30.92           C  
-ATOM  17445  CD1 PHE E 231       5.075 -84.919 -67.490  1.00 26.44           C  
-ATOM  17446  CD2 PHE E 231       5.708 -82.950 -68.668  1.00 32.34           C  
-ATOM  17447  CE1 PHE E 231       3.761 -84.492 -67.475  1.00 24.10           C  
-ATOM  17448  CE2 PHE E 231       4.394 -82.524 -68.664  1.00 28.10           C  
-ATOM  17449  CZ  PHE E 231       3.421 -83.293 -68.063  1.00 25.96           C  
-ATOM  17450  N   ILE E 232       7.029 -84.723 -64.646  1.00 30.70           N  
-ATOM  17451  CA  ILE E 232       6.179 -85.412 -63.673  1.00 20.06           C  
-ATOM  17452  C   ILE E 232       5.006 -84.519 -63.267  1.00 24.66           C  
-ATOM  17453  O   ILE E 232       5.195 -83.492 -62.614  1.00 29.73           O  
-ATOM  17454  CB  ILE E 232       6.955 -85.833 -62.407  1.00 20.50           C  
-ATOM  17455  CG1 ILE E 232       8.125 -86.756 -62.759  1.00 15.04           C  
-ATOM  17456  CG2 ILE E 232       6.022 -86.523 -61.420  1.00 21.55           C  
-ATOM  17457  CD1 ILE E 232       8.922 -87.219 -61.560  1.00 20.54           C  
-ATOM  17458  N   SER E 233       3.797 -84.926 -63.649  1.00 27.60           N  
-ATOM  17459  CA  SER E 233       2.595 -84.115 -63.452  1.00 23.13           C  
-ATOM  17460  C   SER E 233       1.995 -84.258 -62.059  1.00 21.30           C  
-ATOM  17461  O   SER E 233       2.458 -85.066 -61.254  1.00 27.32           O  
-ATOM  17462  CB  SER E 233       1.536 -84.488 -64.486  1.00 24.01           C  
-ATOM  17463  OG  SER E 233       1.016 -85.783 -64.233  1.00 14.22           O  
-ATOM  17464  N   LYS E 234       0.955 -83.473 -61.782  1.00 20.90           N  
-ATOM  17465  CA  LYS E 234       0.215 -83.607 -60.532  1.00 19.13           C  
-ATOM  17466  C   LYS E 234      -0.666 -84.846 -60.619  1.00 21.06           C  
-ATOM  17467  O   LYS E 234      -0.933 -85.342 -61.710  1.00 20.39           O  
-ATOM  17468  CB  LYS E 234      -0.628 -82.360 -60.241  1.00 16.23           C  
-ATOM  17469  CG  LYS E 234      -2.068 -82.449 -60.719  1.00 21.92           C  
-ATOM  17470  CD  LYS E 234      -2.243 -81.805 -62.083  1.00 42.19           C  
-ATOM  17471  CE  LYS E 234      -2.725 -80.368 -61.961  1.00 31.37           C  
-ATOM  17472  NZ  LYS E 234      -4.106 -80.313 -61.414  1.00 25.80           N  
-ATOM  17473  N   THR E 235      -1.112 -85.349 -59.475  1.00 27.16           N  
-ATOM  17474  CA  THR E 235      -1.910 -86.568 -59.457  1.00 18.46           C  
-ATOM  17475  C   THR E 235      -3.364 -86.316 -59.854  1.00 25.55           C  
-ATOM  17476  O   THR E 235      -4.043 -85.468 -59.273  1.00 22.47           O  
-ATOM  17477  CB  THR E 235      -1.879 -87.235 -58.072  1.00 13.94           C  
-ATOM  17478  OG1 THR E 235      -0.523 -87.539 -57.721  1.00 17.77           O  
-ATOM  17479  CG2 THR E 235      -2.696 -88.513 -58.082  1.00 10.78           C  
-ATOM  17480  N   PHE E 236      -3.821 -87.053 -60.863  1.00 22.08           N  
-ATOM  17481  CA  PHE E 236      -5.224 -87.078 -61.254  1.00 18.04           C  
-ATOM  17482  C   PHE E 236      -5.868 -88.333 -60.692  1.00 18.05           C  
-ATOM  17483  O   PHE E 236      -5.177 -89.212 -60.181  1.00 19.25           O  
-ATOM  17484  CB  PHE E 236      -5.379 -87.062 -62.773  1.00 19.94           C  
-ATOM  17485  CG  PHE E 236      -4.770 -85.866 -63.439  1.00 20.53           C  
-ATOM  17486  CD1 PHE E 236      -3.404 -85.792 -63.653  1.00 20.98           C  
-ATOM  17487  CD2 PHE E 236      -5.569 -84.826 -63.880  1.00 27.18           C  
-ATOM  17488  CE1 PHE E 236      -2.846 -84.695 -64.274  1.00 25.73           C  
-ATOM  17489  CE2 PHE E 236      -5.017 -83.728 -64.503  1.00 28.21           C  
-ATOM  17490  CZ  PHE E 236      -3.654 -83.663 -64.701  1.00 30.85           C  
-ATOM  17491  N   SER E 237      -7.187 -88.431 -60.797  1.00 20.54           N  
-ATOM  17492  CA  SER E 237      -7.874 -89.644 -60.371  1.00 19.98           C  
-ATOM  17493  C   SER E 237      -9.215 -89.811 -61.067  1.00 22.14           C  
-ATOM  17494  O   SER E 237      -9.940 -88.835 -61.275  1.00 19.29           O  
-ATOM  17495  CB  SER E 237      -8.080 -89.646 -58.856  1.00 16.39           C  
-ATOM  17496  OG  SER E 237      -9.146 -88.788 -58.490  1.00 38.75           O  
-ATOM  17497  N   ASP E 238      -9.532 -91.054 -61.427  1.00 20.57           N  
-ATOM  17498  CA  ASP E 238     -10.845 -91.402 -61.966  1.00 19.65           C  
-ATOM  17499  C   ASP E 238     -11.322 -92.740 -61.412  1.00 21.36           C  
-ATOM  17500  O   ASP E 238     -10.548 -93.697 -61.327  1.00 22.53           O  
-ATOM  17501  CB  ASP E 238     -10.816 -91.447 -63.492  1.00 17.24           C  
-ATOM  17502  CG  ASP E 238     -10.646 -90.079 -64.102  1.00 27.59           C  
-ATOM  17503  OD1 ASP E 238     -11.592 -89.267 -64.011  1.00 33.96           O  
-ATOM  17504  OD2 ASP E 238      -9.569 -89.813 -64.673  1.00 32.90           O  
-ATOM  17505  N   ASN E 239     -12.598 -92.790 -61.036  1.00 23.71           N  
-ATOM  17506  CA  ASN E 239     -13.210 -93.995 -60.482  1.00 25.09           C  
-ATOM  17507  C   ASN E 239     -12.406 -94.618 -59.344  1.00 20.95           C  
-ATOM  17508  O   ASN E 239     -12.187 -95.831 -59.320  1.00 22.53           O  
-ATOM  17509  CB  ASN E 239     -13.428 -95.029 -61.586  1.00 17.42           C  
-ATOM  17510  CG  ASN E 239     -14.596 -94.678 -62.487  1.00 22.41           C  
-ATOM  17511  OD1 ASN E 239     -14.428 -94.457 -63.686  1.00 30.94           O  
-ATOM  17512  ND2 ASN E 239     -15.791 -94.621 -61.909  1.00 15.61           N  
-ATOM  17513  N   GLY E 240     -11.969 -93.783 -58.407  1.00 10.60           N  
-ATOM  17514  CA  GLY E 240     -11.248 -94.263 -57.242  1.00 16.96           C  
-ATOM  17515  C   GLY E 240      -9.857 -94.765 -57.572  1.00 14.62           C  
-ATOM  17516  O   GLY E 240      -9.235 -95.468 -56.774  1.00  9.65           O  
-ATOM  17517  N   VAL E 241      -9.374 -94.407 -58.758  1.00 20.35           N  
-ATOM  17518  CA  VAL E 241      -8.033 -94.774 -59.191  1.00 17.59           C  
-ATOM  17519  C   VAL E 241      -7.185 -93.532 -59.388  1.00 21.45           C  
-ATOM  17520  O   VAL E 241      -7.443 -92.740 -60.296  1.00 21.51           O  
-ATOM  17521  CB  VAL E 241      -8.037 -95.569 -60.510  1.00 16.39           C  
-ATOM  17522  CG1 VAL E 241      -6.622 -96.001 -60.858  1.00 18.76           C  
-ATOM  17523  CG2 VAL E 241      -8.964 -96.768 -60.414  1.00 18.22           C  
-ATOM  17524  N   PRO E 242      -6.173 -93.357 -58.528  1.00 21.16           N  
-ATOM  17525  CA  PRO E 242      -5.198 -92.273 -58.639  1.00 16.26           C  
-ATOM  17526  C   PRO E 242      -4.103 -92.632 -59.626  1.00 12.81           C  
-ATOM  17527  O   PRO E 242      -3.697 -93.791 -59.688  1.00 15.60           O  
-ATOM  17528  CB  PRO E 242      -4.641 -92.161 -57.220  1.00 13.33           C  
-ATOM  17529  CG  PRO E 242      -4.696 -93.563 -56.713  1.00 15.61           C  
-ATOM  17530  CD  PRO E 242      -5.931 -94.187 -57.334  1.00 19.60           C  
-ATOM  17531  N   TYR E 243      -3.633 -91.653 -60.388  1.00 11.98           N  
-ATOM  17532  CA  TYR E 243      -2.560 -91.886 -61.345  1.00 13.75           C  
-ATOM  17533  C   TYR E 243      -1.918 -90.571 -61.758  1.00 11.79           C  
-ATOM  17534  O   TYR E 243      -2.493 -89.513 -61.544  1.00 13.92           O  
-ATOM  17535  CB  TYR E 243      -3.085 -92.642 -62.576  1.00 14.13           C  
-ATOM  17536  CG  TYR E 243      -4.213 -91.963 -63.316  1.00 15.09           C  
-ATOM  17537  CD1 TYR E 243      -5.533 -92.181 -62.950  1.00 19.21           C  
-ATOM  17538  CD2 TYR E 243      -3.960 -91.126 -64.394  1.00 13.93           C  
-ATOM  17539  CE1 TYR E 243      -6.570 -91.573 -63.627  1.00 19.61           C  
-ATOM  17540  CE2 TYR E 243      -4.991 -90.513 -65.077  1.00 17.95           C  
-ATOM  17541  CZ  TYR E 243      -6.293 -90.742 -64.689  1.00 20.59           C  
-ATOM  17542  OH  TYR E 243      -7.324 -90.137 -65.364  1.00 26.00           O  
-ATOM  17543  N   ASP E 244      -0.723 -90.627 -62.337  1.00 12.49           N  
-ATOM  17544  CA  ASP E 244      -0.139 -89.405 -62.893  1.00 16.44           C  
-ATOM  17545  C   ASP E 244       0.590 -89.684 -64.201  1.00 17.77           C  
-ATOM  17546  O   ASP E 244       0.670 -90.826 -64.642  1.00 17.07           O  
-ATOM  17547  CB  ASP E 244       0.805 -88.717 -61.887  1.00 19.05           C  
-ATOM  17548  CG  ASP E 244       1.963 -89.605 -61.440  1.00 18.96           C  
-ATOM  17549  OD1 ASP E 244       2.164 -90.690 -62.022  1.00 19.07           O  
-ATOM  17550  OD2 ASP E 244       2.686 -89.206 -60.500  1.00 15.81           O  
-ATOM  17551  N   PHE E 245       1.115 -88.634 -64.820  1.00 16.42           N  
-ATOM  17552  CA  PHE E 245       1.764 -88.767 -66.117  1.00 15.42           C  
-ATOM  17553  C   PHE E 245       3.234 -88.393 -66.041  1.00 17.55           C  
-ATOM  17554  O   PHE E 245       3.588 -87.328 -65.535  1.00 19.24           O  
-ATOM  17555  CB  PHE E 245       1.063 -87.898 -67.162  1.00 16.25           C  
-ATOM  17556  CG  PHE E 245      -0.412 -88.148 -67.266  1.00 19.34           C  
-ATOM  17557  CD1 PHE E 245      -1.310 -87.426 -66.494  1.00 20.48           C  
-ATOM  17558  CD2 PHE E 245      -0.903 -89.100 -68.142  1.00 20.50           C  
-ATOM  17559  CE1 PHE E 245      -2.669 -87.653 -66.590  1.00 18.37           C  
-ATOM  17560  CE2 PHE E 245      -2.260 -89.331 -68.243  1.00 25.95           C  
-ATOM  17561  CZ  PHE E 245      -3.144 -88.606 -67.466  1.00 29.49           C  
-ATOM  17562  N   VAL E 246       4.091 -89.273 -66.544  1.00 19.73           N  
-ATOM  17563  CA  VAL E 246       5.508 -88.955 -66.643  1.00 21.93           C  
-ATOM  17564  C   VAL E 246       6.041 -89.204 -68.045  1.00 19.60           C  
-ATOM  17565  O   VAL E 246       5.541 -90.059 -68.780  1.00 20.75           O  
-ATOM  17566  CB  VAL E 246       6.358 -89.761 -65.644  1.00 13.36           C  
-ATOM  17567  CG1 VAL E 246       6.014 -89.366 -64.221  1.00 15.92           C  
-ATOM  17568  CG2 VAL E 246       6.180 -91.252 -65.866  1.00 12.74           C  
-ATOM  17569  N   VAL E 247       7.058 -88.434 -68.410  1.00 16.32           N  
-ATOM  17570  CA  VAL E 247       7.747 -88.632 -69.670  1.00 21.20           C  
-ATOM  17571  C   VAL E 247       9.202 -88.985 -69.396  1.00 25.12           C  
-ATOM  17572  O   VAL E 247       9.924 -88.236 -68.732  1.00 26.24           O  
-ATOM  17573  CB  VAL E 247       7.668 -87.386 -70.569  1.00 24.82           C  
-ATOM  17574  CG1 VAL E 247       8.235 -87.696 -71.946  1.00 26.94           C  
-ATOM  17575  CG2 VAL E 247       6.231 -86.903 -70.678  1.00 16.29           C  
-ATOM  17576  N   LEU E 248       9.619 -90.143 -69.897  1.00 23.91           N  
-ATOM  17577  CA  LEU E 248      10.993 -90.590 -69.747  1.00 25.41           C  
-ATOM  17578  C   LEU E 248      11.759 -90.340 -71.036  1.00 33.53           C  
-ATOM  17579  O   LEU E 248      11.176 -90.323 -72.120  1.00 29.02           O  
-ATOM  17580  CB  LEU E 248      11.047 -92.073 -69.375  1.00 25.17           C  
-ATOM  17581  CG  LEU E 248      10.146 -92.544 -68.231  1.00 19.88           C  
-ATOM  17582  CD1 LEU E 248      10.504 -93.963 -67.835  1.00 22.38           C  
-ATOM  17583  CD2 LEU E 248      10.239 -91.621 -67.034  1.00 22.08           C  
-ATOM  17584  N   GLU E 249      13.068 -90.148 -70.907  1.00 40.30           N  
-ATOM  17585  CA  GLU E 249      13.926 -89.844 -72.042  1.00 31.02           C  
-ATOM  17586  C   GLU E 249      15.171 -90.723 -72.007  1.00 32.16           C  
-ATOM  17587  O   GLU E 249      15.694 -91.030 -70.933  1.00 37.00           O  
-ATOM  17588  CB  GLU E 249      14.310 -88.363 -72.033  1.00 32.40           C  
-ATOM  17589  CG  GLU E 249      15.202 -87.911 -73.177  1.00 44.30           C  
-ATOM  17590  CD  GLU E 249      15.567 -86.442 -73.072  1.00 57.92           C  
-ATOM  17591  OE1 GLU E 249      15.055 -85.638 -73.881  1.00 42.43           O  
-ATOM  17592  OE2 GLU E 249      16.362 -86.091 -72.173  1.00 58.40           O  
-ATOM  17593  N   LYS E 250      15.627 -91.144 -73.181  1.00 32.92           N  
-ATOM  17594  CA  LYS E 250      16.850 -91.934 -73.290  1.00 40.18           C  
-ATOM  17595  C   LYS E 250      18.074 -91.029 -73.148  1.00 52.90           C  
-ATOM  17596  O   LYS E 250      18.204 -90.036 -73.867  1.00 54.01           O  
-ATOM  17597  CB  LYS E 250      16.881 -92.680 -74.623  1.00 39.06           C  
-ATOM  17598  CG  LYS E 250      17.777 -93.905 -74.639  1.00 39.67           C  
-ATOM  17599  CD  LYS E 250      17.596 -94.692 -75.928  1.00 30.66           C  
-ATOM  17600  CE  LYS E 250      18.369 -95.996 -75.894  1.00 40.56           C  
-ATOM  17601  NZ  LYS E 250      18.152 -96.781 -77.136  1.00 44.23           N  
-ATOM  17602  N   ARG E 251      18.975 -91.369 -72.229  1.00 49.95           N  
-ATOM  17603  CA  ARG E 251      20.050 -90.446 -71.870  1.00 68.11           C  
-ATOM  17604  C   ARG E 251      21.470 -91.005 -71.975  1.00 84.05           C  
-ATOM  17605  O   ARG E 251      22.414 -90.245 -72.209  1.00 79.84           O  
-ATOM  17606  CB  ARG E 251      19.824 -89.922 -70.447  1.00 62.14           C  
-ATOM  17607  CG  ARG E 251      18.788 -88.812 -70.352  1.00 62.45           C  
-ATOM  17608  CD  ARG E 251      19.045 -87.731 -71.395  1.00 67.90           C  
-ATOM  17609  NE  ARG E 251      20.426 -87.252 -71.370  1.00 87.64           N  
-ATOM  17610  CZ  ARG E 251      20.976 -86.506 -72.323  1.00 82.71           C  
-ATOM  17611  NH1 ARG E 251      22.240 -86.117 -72.219  1.00 65.91           N  
-ATOM  17612  NH2 ARG E 251      20.263 -86.150 -73.384  1.00 82.24           N  
-ATOM  17613  N   ARG E 252      21.619 -92.314 -71.788  1.00 75.00           N  
-ATOM  17614  CA  ARG E 252      22.931 -92.962 -71.838  1.00 68.59           C  
-ATOM  17615  C   ARG E 252      23.913 -92.354 -70.839  1.00 62.44           C  
-ATOM  17616  O   ARG E 252      23.734 -92.462 -69.628  1.00 63.66           O  
-ATOM  17617  CB  ARG E 252      23.521 -92.886 -73.252  1.00 71.41           C  
-ATOM  17618  CG  ARG E 252      24.972 -93.330 -73.343  1.00 73.40           C  
-ATOM  17619  CD  ARG E 252      25.674 -92.712 -74.547  1.00 66.74           C  
-ATOM  17620  NE  ARG E 252      26.819 -91.900 -74.142  1.00 71.39           N  
-ATOM  17621  CZ  ARG E 252      28.050 -92.373 -73.972  1.00 72.11           C  
-ATOM  17622  NH1 ARG E 252      28.302 -93.659 -74.178  1.00 61.32           N  
-ATOM  17623  NH2 ARG E 252      29.030 -91.562 -73.598  1.00 64.73           N  
-ATOM  17624  N   SER E 285      15.920 -51.982 -80.106  1.00 85.04           N  
-ATOM  17625  CA  SER E 285      15.951 -51.944 -78.648  1.00 96.06           C  
-ATOM  17626  C   SER E 285      14.546 -51.959 -78.049  1.00 85.94           C  
-ATOM  17627  O   SER E 285      14.134 -51.007 -77.385  1.00 80.06           O  
-ATOM  17628  CB  SER E 285      16.720 -50.711 -78.168  1.00 84.19           C  
-ATOM  17629  OG  SER E 285      16.646 -49.664 -79.119  1.00 71.57           O  
-ATOM  17630  N   SER E 286      13.815 -53.045 -78.286  1.00 87.01           N  
-ATOM  17631  CA  SER E 286      12.465 -53.191 -77.754  1.00 95.38           C  
-ATOM  17632  C   SER E 286      12.496 -53.243 -76.229  1.00 97.78           C  
-ATOM  17633  O   SER E 286      12.101 -52.290 -75.554  1.00 79.85           O  
-ATOM  17634  CB  SER E 286      11.794 -54.448 -78.315  1.00 85.31           C  
-ATOM  17635  OG  SER E 286      11.730 -54.410 -79.730  1.00 68.79           O  
-ATOM  17636  N   ALA E 287      12.977 -54.360 -75.696  1.00 92.10           N  
-ATOM  17637  CA  ALA E 287      13.095 -54.534 -74.256  1.00 74.29           C  
-ATOM  17638  C   ALA E 287      14.507 -54.981 -73.908  1.00 74.49           C  
-ATOM  17639  O   ALA E 287      14.880 -55.065 -72.738  1.00 81.97           O  
-ATOM  17640  CB  ALA E 287      12.073 -55.538 -73.754  1.00 74.23           C  
-ATOM  17641  N   ALA E 288      15.291 -55.256 -74.945  1.00 76.49           N  
-ATOM  17642  CA  ALA E 288      16.639 -55.786 -74.787  1.00 91.22           C  
-ATOM  17643  C   ALA E 288      17.612 -54.763 -74.197  1.00 99.03           C  
-ATOM  17644  O   ALA E 288      18.665 -55.131 -73.671  1.00 82.85           O  
-ATOM  17645  CB  ALA E 288      17.156 -56.290 -76.128  1.00 68.21           C  
-ATOM  17646  N   ALA E 289      17.257 -53.483 -74.279  1.00 94.71           N  
-ATOM  17647  CA  ALA E 289      18.131 -52.413 -73.805  1.00 98.62           C  
-ATOM  17648  C   ALA E 289      17.944 -52.147 -72.315  1.00107.24           C  
-ATOM  17649  O   ALA E 289      18.433 -51.149 -71.786  1.00 97.78           O  
-ATOM  17650  CB  ALA E 289      17.883 -51.143 -74.597  1.00 90.26           C  
-ATOM  17651  N   ILE E 290      17.231 -53.042 -71.641  1.00107.48           N  
-ATOM  17652  CA  ILE E 290      16.938 -52.875 -70.225  1.00 89.80           C  
-ATOM  17653  C   ILE E 290      17.587 -54.011 -69.435  1.00 92.53           C  
-ATOM  17654  O   ILE E 290      17.777 -53.926 -68.219  1.00 94.01           O  
-ATOM  17655  CB  ILE E 290      15.421 -52.820 -69.993  1.00 77.20           C  
-ATOM  17656  CG1 ILE E 290      14.782 -51.887 -71.026  1.00 88.59           C  
-ATOM  17657  CG2 ILE E 290      15.114 -52.352 -68.584  1.00 69.21           C  
-ATOM  17658  CD1 ILE E 290      13.423 -52.325 -71.491  1.00 92.33           C  
-ATOM  17659  N   ALA E 291      17.949 -55.065 -70.159  1.00 96.39           N  
-ATOM  17660  CA  ALA E 291      18.773 -56.147 -69.632  1.00 99.42           C  
-ATOM  17661  C   ALA E 291      20.099 -55.682 -69.008  1.00101.34           C  
-ATOM  17662  O   ALA E 291      20.633 -56.375 -68.150  1.00 96.02           O  
-ATOM  17663  CB  ALA E 291      19.047 -57.166 -70.733  1.00 96.59           C  
-ATOM  17664  N   PRO E 292      20.659 -54.536 -69.454  1.00 95.02           N  
-ATOM  17665  CA  PRO E 292      21.782 -53.994 -68.677  1.00 94.39           C  
-ATOM  17666  C   PRO E 292      21.402 -53.571 -67.252  1.00 93.61           C  
-ATOM  17667  O   PRO E 292      22.152 -53.878 -66.322  1.00 85.34           O  
-ATOM  17668  CB  PRO E 292      22.233 -52.776 -69.505  1.00 92.06           C  
-ATOM  17669  CG  PRO E 292      21.148 -52.555 -70.524  1.00 85.21           C  
-ATOM  17670  CD  PRO E 292      20.601 -53.911 -70.786  1.00 87.56           C  
-ATOM  17671  N   VAL E 293      20.277 -52.882 -67.073  1.00 96.64           N  
-ATOM  17672  CA  VAL E 293      19.833 -52.548 -65.723  1.00 92.21           C  
-ATOM  17673  C   VAL E 293      19.473 -53.828 -64.980  1.00 92.42           C  
-ATOM  17674  O   VAL E 293      19.663 -53.924 -63.768  1.00 80.95           O  
-ATOM  17675  CB  VAL E 293      18.629 -51.587 -65.721  1.00 83.41           C  
-ATOM  17676  CG1 VAL E 293      18.281 -51.177 -64.297  1.00 72.66           C  
-ATOM  17677  CG2 VAL E 293      18.938 -50.368 -66.543  1.00 70.44           C  
-ATOM  17678  N   LEU E 294      18.961 -54.814 -65.711  1.00102.12           N  
-ATOM  17679  CA  LEU E 294      18.705 -56.121 -65.120  1.00100.93           C  
-ATOM  17680  C   LEU E 294      20.008 -56.745 -64.625  1.00102.99           C  
-ATOM  17681  O   LEU E 294      20.021 -57.454 -63.621  1.00103.60           O  
-ATOM  17682  CB  LEU E 294      18.025 -57.060 -66.123  1.00105.17           C  
-ATOM  17683  CG  LEU E 294      16.498 -57.021 -66.225  1.00 93.78           C  
-ATOM  17684  CD1 LEU E 294      15.979 -57.996 -67.277  1.00 89.33           C  
-ATOM  17685  CD2 LEU E 294      15.856 -57.304 -64.872  1.00 87.68           C  
-ATOM  17686  N   ALA E 295      21.104 -56.438 -65.316  1.00101.56           N  
-ATOM  17687  CA  ALA E 295      22.364 -57.162 -65.166  1.00101.16           C  
-ATOM  17688  C   ALA E 295      23.078 -56.919 -63.836  1.00101.28           C  
-ATOM  17689  O   ALA E 295      23.861 -57.757 -63.390  1.00 91.38           O  
-ATOM  17690  CB  ALA E 295      23.294 -56.814 -66.321  1.00 79.13           C  
-ATOM  17691  N   TRP E 296      22.820 -55.779 -63.204  1.00 96.94           N  
-ATOM  17692  CA  TRP E 296      23.496 -55.468 -61.950  1.00102.56           C  
-ATOM  17693  C   TRP E 296      22.591 -55.693 -60.741  1.00100.68           C  
-ATOM  17694  O   TRP E 296      23.046 -55.641 -59.597  1.00 89.89           O  
-ATOM  17695  CB  TRP E 296      24.023 -54.033 -61.961  1.00 96.36           C  
-ATOM  17696  CG  TRP E 296      22.976 -52.961 -61.966  1.00103.75           C  
-ATOM  17697  CD1 TRP E 296      22.405 -52.373 -63.059  1.00101.88           C  
-ATOM  17698  CD2 TRP E 296      22.399 -52.325 -60.821  1.00103.35           C  
-ATOM  17699  NE1 TRP E 296      21.497 -51.417 -62.663  1.00 97.00           N  
-ATOM  17700  CE2 TRP E 296      21.476 -51.369 -61.292  1.00 95.96           C  
-ATOM  17701  CE3 TRP E 296      22.568 -52.475 -59.440  1.00 90.32           C  
-ATOM  17702  CZ2 TRP E 296      20.727 -50.568 -60.435  1.00 85.88           C  
-ATOM  17703  CZ3 TRP E 296      21.823 -51.680 -58.591  1.00 86.75           C  
-ATOM  17704  CH2 TRP E 296      20.914 -50.740 -59.090  1.00 87.84           C  
-ATOM  17705  N   MET E 297      21.313 -55.947 -60.994  1.00101.47           N  
-ATOM  17706  CA  MET E 297      20.408 -56.376 -59.936  1.00 90.10           C  
-ATOM  17707  C   MET E 297      20.359 -57.899 -59.928  1.00 90.31           C  
-ATOM  17708  O   MET E 297      19.922 -58.520 -58.957  1.00 89.77           O  
-ATOM  17709  CB  MET E 297      19.010 -55.789 -60.132  1.00 78.91           C  
-ATOM  17710  CG  MET E 297      18.952 -54.267 -60.092  1.00 87.39           C  
-ATOM  17711  SD  MET E 297      17.252 -53.654 -60.083  1.00 71.14           S  
-ATOM  17712  CE  MET E 297      17.515 -51.896 -60.308  1.00 64.19           C  
-ATOM  17713  N   ASP E 298      20.822 -58.486 -61.029  1.00 88.72           N  
-ATOM  17714  CA  ASP E 298      20.842 -59.933 -61.209  1.00 92.26           C  
-ATOM  17715  C   ASP E 298      22.020 -60.552 -60.464  1.00 93.82           C  
-ATOM  17716  O   ASP E 298      23.045 -59.899 -60.258  1.00 72.84           O  
-ATOM  17717  CB  ASP E 298      20.907 -60.281 -62.703  1.00 84.99           C  
-ATOM  17718  CG  ASP E 298      20.886 -61.777 -62.963  1.00 81.70           C  
-ATOM  17719  OD1 ASP E 298      20.274 -62.513 -62.161  1.00 89.74           O  
-ATOM  17720  OD2 ASP E 298      21.479 -62.216 -63.972  1.00 69.00           O  
-ATOM  17721  N   GLU E 299      21.864 -61.810 -60.060  1.00101.26           N  
-ATOM  17722  CA  GLU E 299      22.920 -62.544 -59.368  1.00102.69           C  
-ATOM  17723  C   GLU E 299      23.402 -63.734 -60.196  1.00 94.29           C  
-ATOM  17724  O   GLU E 299      23.275 -64.888 -59.782  1.00 83.03           O  
-ATOM  17725  CB  GLU E 299      22.434 -63.020 -57.996  1.00 84.87           C  
-ATOM  17726  CG  GLU E 299      22.008 -61.894 -57.067  1.00 77.55           C  
-ATOM  17727  CD  GLU E 299      23.138 -60.929 -56.768  1.00 80.74           C  
-ATOM  17728  OE1 GLU E 299      24.286 -61.391 -56.597  1.00 77.12           O  
-ATOM  17729  OE2 GLU E 299      22.880 -59.708 -56.711  1.00 75.32           O  
-ATOM  17730  N   LEU E 310      22.474 -74.105 -55.619  1.00 29.07           N  
-ATOM  17731  CA  LEU E 310      23.474 -75.167 -55.555  1.00 55.10           C  
-ATOM  17732  C   LEU E 310      22.814 -76.540 -55.474  1.00 39.08           C  
-ATOM  17733  O   LEU E 310      22.914 -77.344 -56.402  1.00 47.88           O  
-ATOM  17734  CB  LEU E 310      24.404 -74.957 -54.355  1.00 51.93           C  
-ATOM  17735  CG  LEU E 310      25.904 -75.203 -54.563  1.00 55.54           C  
-ATOM  17736  CD1 LEU E 310      26.188 -76.642 -54.978  1.00 51.83           C  
-ATOM  17737  CD2 LEU E 310      26.483 -74.219 -55.577  1.00 40.47           C  
-ATOM  17738  N   ILE E 311      22.146 -76.803 -54.357  1.00 38.15           N  
-ATOM  17739  CA  ILE E 311      21.443 -78.065 -54.162  1.00 44.87           C  
-ATOM  17740  C   ILE E 311      20.045 -78.005 -54.775  1.00 45.08           C  
-ATOM  17741  O   ILE E 311      19.290 -77.064 -54.528  1.00 40.03           O  
-ATOM  17742  CB  ILE E 311      21.330 -78.431 -52.660  1.00 37.95           C  
-ATOM  17743  CG1 ILE E 311      22.642 -79.028 -52.144  1.00 39.72           C  
-ATOM  17744  CG2 ILE E 311      20.193 -79.415 -52.425  1.00 32.99           C  
-ATOM  17745  CD1 ILE E 311      23.697 -78.003 -51.769  1.00 52.32           C  
-ATOM  17746  N   ARG E 312      19.710 -79.003 -55.588  1.00 38.16           N  
-ATOM  17747  CA  ARG E 312      18.371 -79.097 -56.151  1.00 40.35           C  
-ATOM  17748  C   ARG E 312      17.896 -80.543 -56.226  1.00 44.21           C  
-ATOM  17749  O   ARG E 312      18.659 -81.441 -56.582  1.00 54.02           O  
-ATOM  17750  CB  ARG E 312      18.316 -78.459 -57.541  1.00 47.24           C  
-ATOM  17751  CG  ARG E 312      16.902 -78.364 -58.091  1.00 44.99           C  
-ATOM  17752  CD  ARG E 312      16.836 -77.585 -59.388  1.00 35.87           C  
-ATOM  17753  NE  ARG E 312      15.473 -77.135 -59.654  1.00 38.57           N  
-ATOM  17754  CZ  ARG E 312      14.961 -76.968 -60.869  1.00 46.04           C  
-ATOM  17755  NH1 ARG E 312      15.697 -77.218 -61.943  1.00 59.55           N  
-ATOM  17756  NH2 ARG E 312      13.708 -76.555 -61.008  1.00 23.64           N  
-ATOM  17757  N   ALA E 313      16.631 -80.759 -55.884  1.00 40.66           N  
-ATOM  17758  CA  ALA E 313      16.023 -82.078 -55.994  1.00 36.75           C  
-ATOM  17759  C   ALA E 313      15.764 -82.415 -57.457  1.00 43.28           C  
-ATOM  17760  O   ALA E 313      15.235 -81.584 -58.192  1.00 40.96           O  
-ATOM  17761  CB  ALA E 313      14.734 -82.137 -55.198  1.00 31.17           C  
-ATOM  17762  N   VAL E 314      16.127 -83.640 -57.850  1.00 37.18           N  
-ATOM  17763  CA  VAL E 314      16.008 -84.167 -59.222  1.00 31.00           C  
-ATOM  17764  C   VAL E 314      15.931 -83.113 -60.335  1.00 40.43           C  
-ATOM  17765  O   VAL E 314      14.864 -82.877 -60.907  1.00 37.26           O  
-ATOM  17766  CB  VAL E 314      14.778 -85.107 -59.354  1.00 24.94           C  
-ATOM  17767  CG1 VAL E 314      15.108 -86.489 -58.812  1.00 33.08           C  
-ATOM  17768  CG2 VAL E 314      13.558 -84.535 -58.646  1.00 31.64           C  
-ATOM  17769  N   PRO E 315      17.077 -82.491 -60.657  1.00 40.37           N  
-ATOM  17770  CA  PRO E 315      17.160 -81.371 -61.604  1.00 34.68           C  
-ATOM  17771  C   PRO E 315      16.809 -81.750 -63.041  1.00 32.13           C  
-ATOM  17772  O   PRO E 315      16.380 -80.888 -63.808  1.00 32.08           O  
-ATOM  17773  CB  PRO E 315      18.626 -80.943 -61.506  1.00 40.49           C  
-ATOM  17774  CG  PRO E 315      19.342 -82.179 -61.090  1.00 44.35           C  
-ATOM  17775  CD  PRO E 315      18.405 -82.887 -60.158  1.00 35.91           C  
-ATOM  17776  N   HIS E 316      16.991 -83.018 -63.397  1.00 30.82           N  
-ATOM  17777  CA  HIS E 316      16.697 -83.482 -64.749  1.00 31.30           C  
-ATOM  17778  C   HIS E 316      15.203 -83.445 -65.038  1.00 34.55           C  
-ATOM  17779  O   HIS E 316      14.788 -83.432 -66.195  1.00 39.58           O  
-ATOM  17780  CB  HIS E 316      17.238 -84.896 -64.961  1.00 32.34           C  
-ATOM  17781  CG  HIS E 316      16.962 -85.825 -63.822  1.00 38.21           C  
-ATOM  17782  ND1 HIS E 316      17.762 -85.884 -62.702  1.00 37.87           N  
-ATOM  17783  CD2 HIS E 316      15.976 -86.734 -63.629  1.00 33.39           C  
-ATOM  17784  CE1 HIS E 316      17.282 -86.789 -61.868  1.00 36.40           C  
-ATOM  17785  NE2 HIS E 316      16.198 -87.319 -62.407  1.00 35.81           N  
-ATOM  17786  N   VAL E 317      14.400 -83.434 -63.980  1.00 38.82           N  
-ATOM  17787  CA  VAL E 317      12.953 -83.313 -64.118  1.00 45.20           C  
-ATOM  17788  C   VAL E 317      12.579 -81.859 -64.400  1.00 43.34           C  
-ATOM  17789  O   VAL E 317      12.517 -81.034 -63.487  1.00 35.68           O  
-ATOM  17790  CB  VAL E 317      12.218 -83.804 -62.856  1.00 31.18           C  
-ATOM  17791  CG1 VAL E 317      10.712 -83.767 -63.068  1.00 25.25           C  
-ATOM  17792  CG2 VAL E 317      12.670 -85.211 -62.491  1.00 28.91           C  
-ATOM  17793  N   HIS E 318      12.332 -81.547 -65.668  1.00 37.67           N  
-ATOM  17794  CA  HIS E 318      12.105 -80.164 -66.070  1.00 37.08           C  
-ATOM  17795  C   HIS E 318      10.683 -79.698 -65.780  1.00 41.66           C  
-ATOM  17796  O   HIS E 318      10.494 -78.594 -65.267  1.00 41.98           O  
-ATOM  17797  CB  HIS E 318      12.450 -79.979 -67.550  1.00 42.48           C  
-ATOM  17798  CG  HIS E 318      13.923 -79.920 -67.813  1.00 66.11           C  
-ATOM  17799  ND1 HIS E 318      14.529 -80.624 -68.831  1.00 83.57           N  
-ATOM  17800  CD2 HIS E 318      14.913 -79.239 -67.186  1.00 64.59           C  
-ATOM  17801  CE1 HIS E 318      15.828 -80.382 -68.820  1.00 82.21           C  
-ATOM  17802  NE2 HIS E 318      16.087 -79.543 -67.833  1.00 80.74           N  
-ATOM  17803  N   PHE E 319       9.678 -80.515 -66.087  1.00 41.72           N  
-ATOM  17804  CA  PHE E 319       8.325 -80.134 -65.680  1.00 29.55           C  
-ATOM  17805  C   PHE E 319       7.965 -80.736 -64.330  1.00 30.89           C  
-ATOM  17806  O   PHE E 319       7.863 -81.956 -64.177  1.00 37.64           O  
-ATOM  17807  CB  PHE E 319       7.272 -80.535 -66.709  1.00 28.16           C  
-ATOM  17808  CG  PHE E 319       5.873 -80.162 -66.295  1.00 34.81           C  
-ATOM  17809  CD1 PHE E 319       5.439 -78.848 -66.378  1.00 28.62           C  
-ATOM  17810  CD2 PHE E 319       5.005 -81.115 -65.786  1.00 37.81           C  
-ATOM  17811  CE1 PHE E 319       4.163 -78.495 -65.982  1.00 20.67           C  
-ATOM  17812  CE2 PHE E 319       3.725 -80.770 -65.394  1.00 37.46           C  
-ATOM  17813  CZ  PHE E 319       3.305 -79.458 -65.491  1.00 33.19           C  
-ATOM  17814  N   ARG E 320       7.752 -79.857 -63.359  1.00 28.27           N  
-ATOM  17815  CA  ARG E 320       7.531 -80.261 -61.980  1.00 27.14           C  
-ATOM  17816  C   ARG E 320       6.105 -79.966 -61.532  1.00 28.82           C  
-ATOM  17817  O   ARG E 320       5.881 -79.147 -60.639  1.00 27.92           O  
-ATOM  17818  CB  ARG E 320       8.528 -79.550 -61.072  1.00 23.94           C  
-ATOM  17819  CG  ARG E 320       9.926 -79.507 -61.652  1.00 26.16           C  
-ATOM  17820  CD  ARG E 320      10.910 -78.896 -60.681  1.00 30.85           C  
-ATOM  17821  NE  ARG E 320      12.151 -79.657 -60.655  1.00 24.19           N  
-ATOM  17822  CZ  ARG E 320      12.813 -79.959 -59.547  1.00 28.34           C  
-ATOM  17823  NH1 ARG E 320      12.358 -79.558 -58.369  1.00 33.47           N  
-ATOM  17824  NH2 ARG E 320      13.932 -80.660 -59.619  1.00 34.69           N  
-ATOM  17825  N   GLY E 321       5.145 -80.637 -62.157  1.00 21.88           N  
-ATOM  17826  CA  GLY E 321       3.747 -80.446 -61.826  1.00 17.62           C  
-ATOM  17827  C   GLY E 321       3.387 -81.066 -60.493  1.00 17.30           C  
-ATOM  17828  O   GLY E 321       2.492 -80.583 -59.801  1.00 21.02           O  
-ATOM  17829  N   HIS E 322       4.090 -82.138 -60.133  1.00 18.28           N  
-ATOM  17830  CA  HIS E 322       3.825 -82.860 -58.892  1.00 19.23           C  
-ATOM  17831  C   HIS E 322       3.971 -81.937 -57.688  1.00 19.38           C  
-ATOM  17832  O   HIS E 322       5.009 -81.304 -57.502  1.00 20.61           O  
-ATOM  17833  CB  HIS E 322       4.762 -84.061 -58.758  1.00 17.59           C  
-ATOM  17834  CG  HIS E 322       4.274 -85.103 -57.801  1.00 15.32           C  
-ATOM  17835  ND1 HIS E 322       4.130 -84.863 -56.451  1.00 17.47           N  
-ATOM  17836  CD2 HIS E 322       3.895 -86.386 -57.998  1.00 20.91           C  
-ATOM  17837  CE1 HIS E 322       3.685 -85.956 -55.858  1.00 18.33           C  
-ATOM  17838  NE2 HIS E 322       3.534 -86.896 -56.773  1.00 21.05           N  
-ATOM  17839  N   GLU E 323       2.927 -81.878 -56.868  1.00 15.28           N  
-ATOM  17840  CA  GLU E 323       2.856 -80.909 -55.781  1.00 15.43           C  
-ATOM  17841  C   GLU E 323       3.838 -81.202 -54.645  1.00 19.94           C  
-ATOM  17842  O   GLU E 323       3.955 -80.411 -53.711  1.00 25.55           O  
-ATOM  17843  CB  GLU E 323       1.425 -80.840 -55.235  1.00 20.31           C  
-ATOM  17844  CG  GLU E 323       0.401 -80.379 -56.269  1.00 23.41           C  
-ATOM  17845  CD  GLU E 323      -1.014 -80.293 -55.722  1.00 23.21           C  
-ATOM  17846  OE1 GLU E 323      -1.276 -80.841 -54.629  1.00 27.81           O  
-ATOM  17847  OE2 GLU E 323      -1.866 -79.673 -56.393  1.00 20.33           O  
-ATOM  17848  N   GLU E 324       4.548 -82.326 -54.731  1.00 18.70           N  
-ATOM  17849  CA  GLU E 324       5.559 -82.691 -53.735  1.00 20.47           C  
-ATOM  17850  C   GLU E 324       6.851 -81.903 -53.966  1.00 24.77           C  
-ATOM  17851  O   GLU E 324       7.695 -81.751 -53.064  1.00 34.54           O  
-ATOM  17852  CB  GLU E 324       5.826 -84.198 -53.780  1.00 18.25           C  
-ATOM  17853  CG  GLU E 324       6.761 -84.715 -52.703  1.00 20.71           C  
-ATOM  17854  CD  GLU E 324       6.500 -86.170 -52.364  1.00 27.84           C  
-ATOM  17855  OE1 GLU E 324       7.203 -86.724 -51.492  1.00 26.06           O  
-ATOM  17856  OE2 GLU E 324       5.580 -86.759 -52.968  1.00 35.19           O  
-ATOM  17857  N   PHE E 325       6.991 -81.389 -55.183  1.00 20.34           N  
-ATOM  17858  CA  PHE E 325       8.126 -80.552 -55.536  1.00 20.37           C  
-ATOM  17859  C   PHE E 325       8.127 -79.274 -54.709  1.00 24.83           C  
-ATOM  17860  O   PHE E 325       9.154 -78.619 -54.584  1.00 33.41           O  
-ATOM  17861  CB  PHE E 325       8.114 -80.223 -57.031  1.00 19.72           C  
-ATOM  17862  CG  PHE E 325       8.600 -81.344 -57.901  1.00 23.64           C  
-ATOM  17863  CD1 PHE E 325       9.929 -81.732 -57.870  1.00 27.12           C  
-ATOM  17864  CD2 PHE E 325       7.734 -82.006 -58.753  1.00 23.06           C  
-ATOM  17865  CE1 PHE E 325      10.385 -82.763 -58.669  1.00 21.96           C  
-ATOM  17866  CE2 PHE E 325       8.185 -83.038 -59.557  1.00 28.23           C  
-ATOM  17867  CZ  PHE E 325       9.513 -83.416 -59.513  1.00 24.40           C  
-ATOM  17868  N   GLN E 326       6.974 -78.921 -54.151  1.00 19.90           N  
-ATOM  17869  CA  GLN E 326       6.897 -77.810 -53.215  1.00 19.93           C  
-ATOM  17870  C   GLN E 326       7.748 -78.124 -51.999  1.00 20.27           C  
-ATOM  17871  O   GLN E 326       8.565 -77.313 -51.572  1.00 25.94           O  
-ATOM  17872  CB  GLN E 326       5.450 -77.541 -52.798  1.00 21.88           C  
-ATOM  17873  CG  GLN E 326       4.553 -77.091 -53.936  1.00 20.94           C  
-ATOM  17874  CD  GLN E 326       3.147 -76.784 -53.473  1.00 21.57           C  
-ATOM  17875  OE1 GLN E 326       2.813 -75.634 -53.187  1.00 25.00           O  
-ATOM  17876  NE2 GLN E 326       2.314 -77.814 -53.390  1.00 22.33           N  
-ATOM  17877  N   TYR E 327       7.552 -79.321 -51.458  1.00 18.65           N  
-ATOM  17878  CA  TYR E 327       8.301 -79.781 -50.299  1.00 19.82           C  
-ATOM  17879  C   TYR E 327       9.779 -79.976 -50.615  1.00 20.49           C  
-ATOM  17880  O   TYR E 327      10.649 -79.512 -49.868  1.00 22.12           O  
-ATOM  17881  CB  TYR E 327       7.704 -81.086 -49.770  1.00 16.11           C  
-ATOM  17882  CG  TYR E 327       8.486 -81.702 -48.633  1.00 26.36           C  
-ATOM  17883  CD1 TYR E 327       8.413 -81.175 -47.349  1.00 27.45           C  
-ATOM  17884  CD2 TYR E 327       9.294 -82.811 -48.841  1.00 19.42           C  
-ATOM  17885  CE1 TYR E 327       9.125 -81.735 -46.305  1.00 20.25           C  
-ATOM  17886  CE2 TYR E 327      10.008 -83.379 -47.802  1.00 18.14           C  
-ATOM  17887  CZ  TYR E 327       9.920 -82.837 -46.538  1.00 19.38           C  
-ATOM  17888  OH  TYR E 327      10.628 -83.402 -45.502  1.00 29.63           O  
-ATOM  17889  N   LEU E 328      10.064 -80.665 -51.715  1.00 17.67           N  
-ATOM  17890  CA  LEU E 328      11.453 -80.904 -52.098  1.00 24.18           C  
-ATOM  17891  C   LEU E 328      12.214 -79.589 -52.293  1.00 24.86           C  
-ATOM  17892  O   LEU E 328      13.310 -79.391 -51.739  1.00 21.48           O  
-ATOM  17893  CB  LEU E 328      11.516 -81.749 -53.370  1.00 32.49           C  
-ATOM  17894  CG  LEU E 328      10.876 -83.137 -53.283  1.00 24.09           C  
-ATOM  17895  CD1 LEU E 328      11.113 -83.924 -54.563  1.00 21.97           C  
-ATOM  17896  CD2 LEU E 328      11.404 -83.897 -52.076  1.00 22.31           C  
-ATOM  17897  N   ASP E 329      11.620 -78.687 -53.071  1.00 22.97           N  
-ATOM  17898  CA  ASP E 329      12.216 -77.377 -53.311  1.00 22.92           C  
-ATOM  17899  C   ASP E 329      12.266 -76.548 -52.037  1.00 22.94           C  
-ATOM  17900  O   ASP E 329      13.085 -75.647 -51.920  1.00 24.21           O  
-ATOM  17901  CB  ASP E 329      11.453 -76.607 -54.393  1.00 20.77           C  
-ATOM  17902  CG  ASP E 329      11.627 -77.211 -55.770  1.00 30.17           C  
-ATOM  17903  OD1 ASP E 329      12.611 -77.957 -55.968  1.00 35.00           O  
-ATOM  17904  OD2 ASP E 329      10.784 -76.935 -56.652  1.00 23.42           O  
-ATOM  17905  N   LEU E 330      11.385 -76.844 -51.088  1.00 21.75           N  
-ATOM  17906  CA  LEU E 330      11.435 -76.173 -49.797  1.00 19.33           C  
-ATOM  17907  C   LEU E 330      12.709 -76.608 -49.089  1.00 26.54           C  
-ATOM  17908  O   LEU E 330      13.450 -75.777 -48.563  1.00 33.51           O  
-ATOM  17909  CB  LEU E 330      10.198 -76.495 -48.951  1.00 19.83           C  
-ATOM  17910  CG  LEU E 330       9.806 -75.542 -47.813  1.00 18.27           C  
-ATOM  17911  CD1 LEU E 330      10.200 -76.093 -46.448  1.00 18.07           C  
-ATOM  17912  CD2 LEU E 330      10.407 -74.160 -48.029  1.00 16.43           C  
-ATOM  17913  N   ILE E 331      12.972 -77.913 -49.097  1.00 27.39           N  
-ATOM  17914  CA  ILE E 331      14.203 -78.434 -48.503  1.00 22.97           C  
-ATOM  17915  C   ILE E 331      15.442 -77.828 -49.152  1.00 23.71           C  
-ATOM  17916  O   ILE E 331      16.313 -77.287 -48.462  1.00 22.15           O  
-ATOM  17917  CB  ILE E 331      14.290 -79.968 -48.614  1.00 18.99           C  
-ATOM  17918  CG1 ILE E 331      13.139 -80.624 -47.850  1.00 20.20           C  
-ATOM  17919  CG2 ILE E 331      15.625 -80.455 -48.086  1.00 17.94           C  
-ATOM  17920  CD1 ILE E 331      13.268 -82.124 -47.743  1.00 19.15           C  
-ATOM  17921  N   ALA E 332      15.519 -77.919 -50.477  1.00 28.90           N  
-ATOM  17922  CA  ALA E 332      16.664 -77.371 -51.204  1.00 26.05           C  
-ATOM  17923  C   ALA E 332      16.853 -75.879 -50.915  1.00 27.53           C  
-ATOM  17924  O   ALA E 332      17.972 -75.421 -50.662  1.00 33.63           O  
-ATOM  17925  CB  ALA E 332      16.504 -77.603 -52.694  1.00 28.27           C  
-ATOM  17926  N   ASP E 333      15.752 -75.133 -50.935  1.00 33.83           N  
-ATOM  17927  CA  ASP E 333      15.787 -73.694 -50.691  1.00 35.22           C  
-ATOM  17928  C   ASP E 333      16.319 -73.385 -49.298  1.00 28.11           C  
-ATOM  17929  O   ASP E 333      17.169 -72.517 -49.135  1.00 31.39           O  
-ATOM  17930  CB  ASP E 333      14.395 -73.082 -50.868  1.00 33.58           C  
-ATOM  17931  CG  ASP E 333      14.425 -71.565 -50.962  1.00 43.93           C  
-ATOM  17932  OD1 ASP E 333      15.502 -70.955 -50.768  1.00 46.38           O  
-ATOM  17933  OD2 ASP E 333      13.357 -70.976 -51.227  1.00 47.85           O  
-ATOM  17934  N   ILE E 334      15.808 -74.092 -48.297  1.00 24.62           N  
-ATOM  17935  CA  ILE E 334      16.256 -73.890 -46.926  1.00 23.88           C  
-ATOM  17936  C   ILE E 334      17.743 -74.200 -46.793  1.00 27.78           C  
-ATOM  17937  O   ILE E 334      18.488 -73.444 -46.176  1.00 27.27           O  
-ATOM  17938  CB  ILE E 334      15.461 -74.759 -45.934  1.00 23.72           C  
-ATOM  17939  CG1 ILE E 334      14.033 -74.238 -45.816  1.00 22.26           C  
-ATOM  17940  CG2 ILE E 334      16.132 -74.772 -44.572  1.00 20.56           C  
-ATOM  17941  CD1 ILE E 334      13.209 -75.001 -44.830  1.00 23.75           C  
-ATOM  17942  N   ILE E 335      18.181 -75.306 -47.386  1.00 35.33           N  
-ATOM  17943  CA  ILE E 335      19.590 -75.676 -47.295  1.00 28.95           C  
-ATOM  17944  C   ILE E 335      20.486 -74.626 -47.970  1.00 25.48           C  
-ATOM  17945  O   ILE E 335      21.540 -74.275 -47.443  1.00 28.77           O  
-ATOM  17946  CB  ILE E 335      19.847 -77.074 -47.906  1.00 22.18           C  
-ATOM  17947  CG1 ILE E 335      19.161 -78.156 -47.061  1.00 16.46           C  
-ATOM  17948  CG2 ILE E 335      21.336 -77.356 -47.999  1.00 26.13           C  
-ATOM  17949  CD1 ILE E 335      19.410 -79.572 -47.559  1.00 24.99           C  
-ATOM  17950  N   ASN E 336      20.060 -74.108 -49.118  1.00 30.43           N  
-ATOM  17951  CA  ASN E 336      20.876 -73.137 -49.846  1.00 32.57           C  
-ATOM  17952  C   ASN E 336      20.901 -71.744 -49.216  1.00 34.45           C  
-ATOM  17953  O   ASN E 336      21.971 -71.192 -48.960  1.00 47.03           O  
-ATOM  17954  CB  ASN E 336      20.395 -73.016 -51.291  1.00 25.51           C  
-ATOM  17955  CG  ASN E 336      20.490 -74.322 -52.052  1.00 30.02           C  
-ATOM  17956  OD1 ASN E 336      21.273 -75.205 -51.704  1.00 35.78           O  
-ATOM  17957  ND2 ASN E 336      19.691 -74.449 -53.103  1.00 30.52           N  
-ATOM  17958  N   ASN E 337      19.724 -71.180 -48.969  1.00 31.79           N  
-ATOM  17959  CA  ASN E 337      19.610 -69.777 -48.583  1.00 36.13           C  
-ATOM  17960  C   ASN E 337      19.351 -69.544 -47.096  1.00 33.41           C  
-ATOM  17961  O   ASN E 337      19.481 -68.419 -46.610  1.00 39.50           O  
-ATOM  17962  CB  ASN E 337      18.500 -69.111 -49.396  1.00 34.94           C  
-ATOM  17963  CG  ASN E 337      18.615 -69.401 -50.876  1.00 38.05           C  
-ATOM  17964  OD1 ASN E 337      19.715 -69.555 -51.405  1.00 37.66           O  
-ATOM  17965  ND2 ASN E 337      17.476 -69.487 -51.554  1.00 43.90           N  
-ATOM  17966  N   GLY E 338      18.984 -70.601 -46.379  1.00 32.40           N  
-ATOM  17967  CA  GLY E 338      18.690 -70.491 -44.961  1.00 35.17           C  
-ATOM  17968  C   GLY E 338      19.895 -70.083 -44.134  1.00 36.67           C  
-ATOM  17969  O   GLY E 338      21.027 -70.113 -44.616  1.00 38.38           O  
-ATOM  17970  N   ARG E 339      19.654 -69.697 -42.886  1.00 30.78           N  
-ATOM  17971  CA  ARG E 339      20.741 -69.273 -42.009  1.00 32.05           C  
-ATOM  17972  C   ARG E 339      20.997 -70.303 -40.920  1.00 37.08           C  
-ATOM  17973  O   ARG E 339      20.055 -70.889 -40.383  1.00 37.09           O  
-ATOM  17974  CB  ARG E 339      20.426 -67.917 -41.377  1.00 33.25           C  
-ATOM  17975  CG  ARG E 339      20.157 -66.815 -42.378  1.00 37.74           C  
-ATOM  17976  CD  ARG E 339      21.319 -66.642 -43.338  1.00 35.08           C  
-ATOM  17977  NE  ARG E 339      21.212 -65.380 -44.060  1.00 44.90           N  
-ATOM  17978  CZ  ARG E 339      21.686 -64.224 -43.607  1.00 60.68           C  
-ATOM  17979  NH1 ARG E 339      22.308 -64.177 -42.436  1.00 52.49           N  
-ATOM  17980  NH2 ARG E 339      21.541 -63.117 -44.323  1.00 59.77           N  
-ATOM  17981  N   THR E 340      22.269 -70.525 -40.595  1.00 31.27           N  
-ATOM  17982  CA  THR E 340      22.613 -71.459 -39.530  1.00 29.94           C  
-ATOM  17983  C   THR E 340      22.532 -70.786 -38.165  1.00 31.83           C  
-ATOM  17984  O   THR E 340      23.250 -69.829 -37.882  1.00 38.02           O  
-ATOM  17985  CB  THR E 340      24.012 -72.047 -39.704  1.00 34.64           C  
-ATOM  17986  OG1 THR E 340      24.106 -72.699 -40.977  1.00 26.63           O  
-ATOM  17987  CG2 THR E 340      24.282 -73.055 -38.600  1.00 39.82           C  
-ATOM  17988  N   MET E 341      21.656 -71.312 -37.319  1.00 33.19           N  
-ATOM  17989  CA  MET E 341      21.365 -70.735 -36.021  1.00 36.42           C  
-ATOM  17990  C   MET E 341      21.453 -71.777 -34.919  1.00 38.58           C  
-ATOM  17991  O   MET E 341      21.281 -72.982 -35.163  1.00 49.17           O  
-ATOM  17992  CB  MET E 341      19.963 -70.116 -36.015  1.00 43.88           C  
-ATOM  17993  CG  MET E 341      19.660 -69.207 -37.191  1.00 40.14           C  
-ATOM  17994  SD  MET E 341      20.287 -67.539 -36.938  1.00 56.08           S  
-ATOM  17995  CE  MET E 341      19.378 -67.073 -35.467  1.00 46.71           C  
-ATOM  17996  N   ASP E 342      21.716 -71.296 -33.706  1.00 43.47           N  
-ATOM  17997  CA  ASP E 342      21.568 -72.097 -32.500  1.00 50.65           C  
-ATOM  17998  C   ASP E 342      20.090 -72.368 -32.250  1.00 51.41           C  
-ATOM  17999  O   ASP E 342      19.223 -71.807 -32.921  1.00 59.03           O  
-ATOM  18000  CB  ASP E 342      22.197 -71.397 -31.295  1.00 53.83           C  
-ATOM  18001  CG  ASP E 342      23.710 -71.497 -31.291  1.00 67.39           C  
-ATOM  18002  OD1 ASP E 342      24.236 -72.553 -31.705  1.00 62.70           O  
-ATOM  18003  OD2 ASP E 342      24.373 -70.523 -30.875  1.00 69.07           O  
-ATOM  18004  N   ASP E 343      19.799 -73.215 -31.273  1.00 46.45           N  
-ATOM  18005  CA  ASP E 343      18.449 -73.731 -31.123  1.00 40.17           C  
-ATOM  18006  C   ASP E 343      18.212 -74.278 -29.715  1.00 44.43           C  
-ATOM  18007  O   ASP E 343      19.159 -74.655 -29.025  1.00 53.95           O  
-ATOM  18008  CB  ASP E 343      18.208 -74.799 -32.200  1.00 41.85           C  
-ATOM  18009  CG  ASP E 343      17.184 -75.828 -31.795  1.00 48.37           C  
-ATOM  18010  OD1 ASP E 343      15.981 -75.609 -32.047  1.00 53.32           O  
-ATOM  18011  OD2 ASP E 343      17.589 -76.863 -31.230  1.00 45.04           O  
-ATOM  18012  N   ARG E 344      16.947 -74.294 -29.296  1.00 37.85           N  
-ATOM  18013  CA  ARG E 344      16.542 -74.751 -27.965  1.00 38.71           C  
-ATOM  18014  C   ARG E 344      17.157 -76.089 -27.549  1.00 40.18           C  
-ATOM  18015  O   ARG E 344      17.521 -76.279 -26.388  1.00 38.27           O  
-ATOM  18016  CB  ARG E 344      15.013 -74.857 -27.898  1.00 38.88           C  
-ATOM  18017  CG  ARG E 344      14.480 -75.425 -26.591  1.00 39.73           C  
-ATOM  18018  CD  ARG E 344      12.974 -75.639 -26.638  1.00 47.07           C  
-ATOM  18019  NE  ARG E 344      12.581 -76.665 -27.602  1.00 48.50           N  
-ATOM  18020  CZ  ARG E 344      12.420 -77.952 -27.304  1.00 61.90           C  
-ATOM  18021  NH1 ARG E 344      12.622 -78.381 -26.064  1.00 54.82           N  
-ATOM  18022  NH2 ARG E 344      12.057 -78.812 -28.246  1.00 56.19           N  
-ATOM  18023  N   THR E 345      17.281 -77.005 -28.505  1.00 38.05           N  
-ATOM  18024  CA  THR E 345      17.703 -78.373 -28.218  1.00 43.56           C  
-ATOM  18025  C   THR E 345      19.217 -78.525 -28.077  1.00 46.50           C  
-ATOM  18026  O   THR E 345      19.696 -79.424 -27.385  1.00 44.36           O  
-ATOM  18027  CB  THR E 345      17.227 -79.336 -29.317  1.00 55.38           C  
-ATOM  18028  OG1 THR E 345      18.045 -79.172 -30.484  1.00 59.44           O  
-ATOM  18029  CG2 THR E 345      15.778 -79.051 -29.680  1.00 53.82           C  
-ATOM  18030  N   GLY E 346      19.967 -77.653 -28.741  1.00 41.55           N  
-ATOM  18031  CA  GLY E 346      21.416 -77.738 -28.726  1.00 40.99           C  
-ATOM  18032  C   GLY E 346      21.946 -78.206 -30.066  1.00 55.48           C  
-ATOM  18033  O   GLY E 346      23.119 -78.011 -30.388  1.00 59.84           O  
-ATOM  18034  N   VAL E 347      21.074 -78.837 -30.845  1.00 53.66           N  
-ATOM  18035  CA  VAL E 347      21.409 -79.223 -32.208  1.00 45.68           C  
-ATOM  18036  C   VAL E 347      21.279 -77.993 -33.100  1.00 46.11           C  
-ATOM  18037  O   VAL E 347      20.373 -77.181 -32.914  1.00 42.93           O  
-ATOM  18038  CB  VAL E 347      20.496 -80.352 -32.724  1.00 50.06           C  
-ATOM  18039  CG1 VAL E 347      21.067 -80.956 -33.996  1.00 52.34           C  
-ATOM  18040  CG2 VAL E 347      20.319 -81.425 -31.657  1.00 45.40           C  
-ATOM  18041  N   GLY E 348      22.191 -77.843 -34.055  1.00 48.52           N  
-ATOM  18042  CA  GLY E 348      22.175 -76.692 -34.942  1.00 54.46           C  
-ATOM  18043  C   GLY E 348      21.016 -76.739 -35.918  1.00 40.93           C  
-ATOM  18044  O   GLY E 348      20.483 -77.813 -36.198  1.00 42.25           O  
-ATOM  18045  N   VAL E 349      20.619 -75.582 -36.443  1.00 38.17           N  
-ATOM  18046  CA  VAL E 349      19.492 -75.539 -37.373  1.00 30.88           C  
-ATOM  18047  C   VAL E 349      19.783 -74.627 -38.561  1.00 34.90           C  
-ATOM  18048  O   VAL E 349      20.490 -73.640 -38.425  1.00 38.70           O  
-ATOM  18049  CB  VAL E 349      18.192 -75.078 -36.649  1.00 31.86           C  
-ATOM  18050  CG1 VAL E 349      17.582 -73.840 -37.302  1.00 29.15           C  
-ATOM  18051  CG2 VAL E 349      17.185 -76.213 -36.593  1.00 30.94           C  
-ATOM  18052  N   ILE E 350      19.264 -74.974 -39.734  1.00 30.11           N  
-ATOM  18053  CA  ILE E 350      19.281 -74.049 -40.862  1.00 27.44           C  
-ATOM  18054  C   ILE E 350      17.852 -73.597 -41.132  1.00 28.18           C  
-ATOM  18055  O   ILE E 350      17.012 -74.403 -41.527  1.00 34.92           O  
-ATOM  18056  CB  ILE E 350      19.866 -74.681 -42.131  1.00 26.25           C  
-ATOM  18057  CG1 ILE E 350      21.130 -75.475 -41.808  1.00 35.78           C  
-ATOM  18058  CG2 ILE E 350      20.151 -73.608 -43.167  1.00 16.68           C  
-ATOM  18059  CD1 ILE E 350      21.718 -76.182 -43.010  1.00 36.31           C  
-ATOM  18060  N   SER E 351      17.570 -72.315 -40.916  1.00 19.53           N  
-ATOM  18061  CA  SER E 351      16.184 -71.857 -40.937  1.00 20.02           C  
-ATOM  18062  C   SER E 351      15.889 -70.740 -41.932  1.00 19.81           C  
-ATOM  18063  O   SER E 351      16.777 -69.983 -42.334  1.00 24.72           O  
-ATOM  18064  CB  SER E 351      15.767 -71.402 -39.534  1.00 22.93           C  
-ATOM  18065  OG  SER E 351      16.545 -70.303 -39.097  1.00 35.54           O  
-ATOM  18066  N   LYS E 352      14.619 -70.670 -42.324  1.00 16.65           N  
-ATOM  18067  CA  LYS E 352      14.071 -69.555 -43.085  1.00 19.72           C  
-ATOM  18068  C   LYS E 352      12.786 -69.092 -42.407  1.00 22.48           C  
-ATOM  18069  O   LYS E 352      12.244 -69.793 -41.550  1.00 21.08           O  
-ATOM  18070  CB  LYS E 352      13.794 -69.948 -44.539  1.00 20.36           C  
-ATOM  18071  CG  LYS E 352      15.033 -70.297 -45.340  1.00 27.21           C  
-ATOM  18072  CD  LYS E 352      14.777 -70.163 -46.836  1.00 28.36           C  
-ATOM  18073  CE  LYS E 352      14.387 -68.737 -47.202  1.00 36.22           C  
-ATOM  18074  NZ  LYS E 352      14.362 -68.518 -48.677  1.00 36.09           N  
-ATOM  18075  N   PHE E 353      12.290 -67.922 -42.794  1.00 18.09           N  
-ATOM  18076  CA  PHE E 353      11.106 -67.360 -42.155  1.00 17.24           C  
-ATOM  18077  C   PHE E 353      10.028 -67.000 -43.175  1.00 21.71           C  
-ATOM  18078  O   PHE E 353      10.283 -66.272 -44.134  1.00 25.14           O  
-ATOM  18079  CB  PHE E 353      11.492 -66.129 -41.335  1.00 24.07           C  
-ATOM  18080  CG  PHE E 353      10.451 -65.706 -40.336  1.00 24.28           C  
-ATOM  18081  CD1 PHE E 353       9.949 -66.609 -39.412  1.00 24.30           C  
-ATOM  18082  CD2 PHE E 353       9.996 -64.397 -40.303  1.00 18.53           C  
-ATOM  18083  CE1 PHE E 353       8.998 -66.218 -38.484  1.00 23.30           C  
-ATOM  18084  CE2 PHE E 353       9.050 -63.999 -39.375  1.00 23.27           C  
-ATOM  18085  CZ  PHE E 353       8.550 -64.911 -38.464  1.00 23.81           C  
-ATOM  18086  N   GLY E 354       8.822 -67.515 -42.959  1.00 24.91           N  
-ATOM  18087  CA  GLY E 354       7.708 -67.249 -43.852  1.00 24.65           C  
-ATOM  18088  C   GLY E 354       7.727 -68.104 -45.103  1.00 24.94           C  
-ATOM  18089  O   GLY E 354       8.224 -67.682 -46.146  1.00 32.62           O  
-ATOM  18090  N   CYS E 355       7.181 -69.311 -44.999  1.00 22.39           N  
-ATOM  18091  CA  CYS E 355       7.160 -70.237 -46.126  1.00 24.23           C  
-ATOM  18092  C   CYS E 355       5.740 -70.731 -46.400  1.00 29.09           C  
-ATOM  18093  O   CYS E 355       4.901 -70.762 -45.504  1.00 23.06           O  
-ATOM  18094  CB  CYS E 355       8.100 -71.413 -45.865  1.00 30.88           C  
-ATOM  18095  SG  CYS E 355       9.826 -70.921 -45.613  1.00 44.31           S  
-ATOM  18096  N   THR E 356       5.474 -71.117 -47.642  1.00 32.92           N  
-ATOM  18097  CA  THR E 356       4.110 -71.407 -48.062  1.00 18.85           C  
-ATOM  18098  C   THR E 356       4.026 -72.609 -48.988  1.00 18.15           C  
-ATOM  18099  O   THR E 356       4.792 -72.721 -49.943  1.00 21.52           O  
-ATOM  18100  CB  THR E 356       3.487 -70.183 -48.771  1.00 22.50           C  
-ATOM  18101  OG1 THR E 356       3.114 -69.205 -47.793  1.00 26.80           O  
-ATOM  18102  CG2 THR E 356       2.256 -70.577 -49.578  1.00 28.12           C  
-ATOM  18103  N   MET E 357       3.096 -73.511 -48.693  1.00 19.14           N  
-ATOM  18104  CA  MET E 357       2.759 -74.587 -49.619  1.00 17.31           C  
-ATOM  18105  C   MET E 357       1.248 -74.700 -49.742  1.00 16.58           C  
-ATOM  18106  O   MET E 357       0.520 -74.108 -48.954  1.00 18.09           O  
-ATOM  18107  CB  MET E 357       3.353 -75.917 -49.154  1.00 17.27           C  
-ATOM  18108  CG  MET E 357       4.866 -75.956 -49.159  1.00 19.27           C  
-ATOM  18109  SD  MET E 357       5.510 -77.540 -48.591  1.00 19.78           S  
-ATOM  18110  CE  MET E 357       4.765 -77.643 -46.969  1.00 16.87           C  
-ATOM  18111  N   ARG E 358       0.774 -75.446 -50.733  1.00 14.26           N  
-ATOM  18112  CA  ARG E 358      -0.644 -75.786 -50.795  1.00 20.00           C  
-ATOM  18113  C   ARG E 358      -0.880 -77.023 -51.657  1.00 27.18           C  
-ATOM  18114  O   ARG E 358      -0.363 -77.138 -52.771  1.00 22.16           O  
-ATOM  18115  CB  ARG E 358      -1.477 -74.603 -51.306  1.00 19.38           C  
-ATOM  18116  CG  ARG E 358      -1.042 -74.033 -52.639  1.00 26.09           C  
-ATOM  18117  CD  ARG E 358      -2.089 -73.068 -53.165  1.00 20.06           C  
-ATOM  18118  NE  ARG E 358      -2.282 -71.929 -52.274  1.00 19.83           N  
-ATOM  18119  CZ  ARG E 358      -3.451 -71.332 -52.062  1.00 24.84           C  
-ATOM  18120  NH1 ARG E 358      -4.545 -71.767 -52.670  1.00 20.09           N  
-ATOM  18121  NH2 ARG E 358      -3.528 -70.297 -51.239  1.00 28.99           N  
-ATOM  18122  N   TYR E 359      -1.667 -77.948 -51.117  1.00 23.06           N  
-ATOM  18123  CA  TYR E 359      -1.900 -79.238 -51.750  1.00 20.75           C  
-ATOM  18124  C   TYR E 359      -3.369 -79.431 -52.101  1.00 22.28           C  
-ATOM  18125  O   TYR E 359      -4.261 -79.031 -51.348  1.00 19.88           O  
-ATOM  18126  CB  TYR E 359      -1.420 -80.366 -50.836  1.00 21.25           C  
-ATOM  18127  CG  TYR E 359       0.063 -80.315 -50.560  1.00 18.46           C  
-ATOM  18128  CD1 TYR E 359       0.963 -80.947 -51.403  1.00 21.79           C  
-ATOM  18129  CD2 TYR E 359       0.565 -79.621 -49.466  1.00 18.40           C  
-ATOM  18130  CE1 TYR E 359       2.321 -80.897 -51.162  1.00 22.01           C  
-ATOM  18131  CE2 TYR E 359       1.925 -79.565 -49.219  1.00 17.31           C  
-ATOM  18132  CZ  TYR E 359       2.797 -80.207 -50.072  1.00 17.62           C  
-ATOM  18133  OH  TYR E 359       4.152 -80.165 -49.842  1.00 22.95           O  
-ATOM  18134  N   SER E 360      -3.606 -80.046 -53.254  1.00 15.85           N  
-ATOM  18135  CA  SER E 360      -4.955 -80.280 -53.740  1.00 14.36           C  
-ATOM  18136  C   SER E 360      -5.561 -81.497 -53.060  1.00 19.60           C  
-ATOM  18137  O   SER E 360      -4.862 -82.468 -52.776  1.00 21.15           O  
-ATOM  18138  CB  SER E 360      -4.945 -80.466 -55.255  1.00 18.30           C  
-ATOM  18139  OG  SER E 360      -4.275 -79.391 -55.889  1.00 16.85           O  
-ATOM  18140  N   LEU E 361      -6.864 -81.445 -52.803  1.00 19.77           N  
-ATOM  18141  CA  LEU E 361      -7.536 -82.520 -52.088  1.00 18.23           C  
-ATOM  18142  C   LEU E 361      -8.698 -83.121 -52.873  1.00 24.67           C  
-ATOM  18143  O   LEU E 361      -9.360 -84.040 -52.393  1.00 33.72           O  
-ATOM  18144  CB  LEU E 361      -8.044 -82.017 -50.735  1.00 25.52           C  
-ATOM  18145  CG  LEU E 361      -7.021 -81.373 -49.798  1.00 22.30           C  
-ATOM  18146  CD1 LEU E 361      -7.681 -80.949 -48.499  1.00 15.84           C  
-ATOM  18147  CD2 LEU E 361      -5.870 -82.320 -49.526  1.00 18.77           C  
-ATOM  18148  N   ASP E 362      -8.950 -82.607 -54.073  1.00 25.88           N  
-ATOM  18149  CA  ASP E 362     -10.095 -83.063 -54.855  1.00 21.98           C  
-ATOM  18150  C   ASP E 362      -9.775 -84.295 -55.702  1.00 24.36           C  
-ATOM  18151  O   ASP E 362     -10.649 -85.123 -55.954  1.00 31.19           O  
-ATOM  18152  CB  ASP E 362     -10.613 -81.934 -55.750  1.00 25.69           C  
-ATOM  18153  CG  ASP E 362      -9.580 -81.464 -56.757  1.00 27.64           C  
-ATOM  18154  OD1 ASP E 362      -8.647 -80.738 -56.354  1.00 27.76           O  
-ATOM  18155  OD2 ASP E 362      -9.704 -81.816 -57.950  1.00 21.69           O  
-ATOM  18156  N   GLN E 363      -8.526 -84.421 -56.139  1.00 33.03           N  
-ATOM  18157  CA  GLN E 363      -8.128 -85.565 -56.955  1.00 27.80           C  
-ATOM  18158  C   GLN E 363      -7.514 -86.676 -56.104  1.00 25.74           C  
-ATOM  18159  O   GLN E 363      -7.923 -87.831 -56.193  1.00 21.73           O  
-ATOM  18160  CB  GLN E 363      -7.145 -85.132 -58.044  1.00 37.25           C  
-ATOM  18161  CG  GLN E 363      -7.725 -84.139 -59.044  1.00 38.75           C  
-ATOM  18162  CD  GLN E 363      -8.846 -84.732 -59.874  1.00 34.66           C  
-ATOM  18163  OE1 GLN E 363      -8.628 -85.645 -60.673  1.00 33.39           O  
-ATOM  18164  NE2 GLN E 363     -10.056 -84.216 -59.687  1.00 41.52           N  
-ATOM  18165  N   ALA E 364      -6.535 -86.322 -55.276  1.00 24.68           N  
-ATOM  18166  CA  ALA E 364      -5.887 -87.297 -54.405  1.00 19.92           C  
-ATOM  18167  C   ALA E 364      -5.515 -86.685 -53.054  1.00 25.48           C  
-ATOM  18168  O   ALA E 364      -5.948 -85.582 -52.721  1.00 26.47           O  
-ATOM  18169  CB  ALA E 364      -4.657 -87.873 -55.084  1.00 13.95           C  
-ATOM  18170  N   PHE E 365      -4.714 -87.409 -52.281  1.00 18.18           N  
-ATOM  18171  CA  PHE E 365      -4.350 -86.981 -50.936  1.00 14.98           C  
-ATOM  18172  C   PHE E 365      -2.838 -86.841 -50.828  1.00 21.57           C  
-ATOM  18173  O   PHE E 365      -2.103 -87.757 -51.198  1.00 23.38           O  
-ATOM  18174  CB  PHE E 365      -4.877 -87.978 -49.900  1.00 19.31           C  
-ATOM  18175  CG  PHE E 365      -4.680 -87.546 -48.474  1.00 15.77           C  
-ATOM  18176  CD1 PHE E 365      -3.507 -87.839 -47.797  1.00 17.84           C  
-ATOM  18177  CD2 PHE E 365      -5.683 -86.874 -47.800  1.00 16.05           C  
-ATOM  18178  CE1 PHE E 365      -3.332 -87.450 -46.483  1.00 16.28           C  
-ATOM  18179  CE2 PHE E 365      -5.515 -86.486 -46.487  1.00 18.74           C  
-ATOM  18180  CZ  PHE E 365      -4.338 -86.773 -45.827  1.00 13.35           C  
-ATOM  18181  N   PRO E 366      -2.371 -85.694 -50.312  1.00 24.71           N  
-ATOM  18182  CA  PRO E 366      -0.941 -85.378 -50.249  1.00 17.70           C  
-ATOM  18183  C   PRO E 366      -0.201 -86.124 -49.140  1.00 25.34           C  
-ATOM  18184  O   PRO E 366       0.324 -85.503 -48.215  1.00 32.00           O  
-ATOM  18185  CB  PRO E 366      -0.933 -83.873 -49.989  1.00 14.33           C  
-ATOM  18186  CG  PRO E 366      -2.181 -83.631 -49.224  1.00 16.71           C  
-ATOM  18187  CD  PRO E 366      -3.198 -84.616 -49.741  1.00 16.83           C  
-ATOM  18188  N   LEU E 367      -0.167 -87.448 -49.233  1.00 21.24           N  
-ATOM  18189  CA  LEU E 367       0.707 -88.238 -48.381  1.00 22.50           C  
-ATOM  18190  C   LEU E 367       2.038 -88.373 -49.116  1.00 21.43           C  
-ATOM  18191  O   LEU E 367       2.125 -89.065 -50.130  1.00 27.98           O  
-ATOM  18192  CB  LEU E 367       0.089 -89.604 -48.070  1.00 17.34           C  
-ATOM  18193  CG  LEU E 367       0.659 -90.390 -46.886  1.00 12.56           C  
-ATOM  18194  CD1 LEU E 367       0.496 -89.612 -45.592  1.00 17.68           C  
-ATOM  18195  CD2 LEU E 367      -0.008 -91.751 -46.773  1.00 11.28           C  
-ATOM  18196  N   LEU E 368       3.061 -87.691 -48.611  1.00 16.71           N  
-ATOM  18197  CA  LEU E 368       4.335 -87.554 -49.315  1.00 23.62           C  
-ATOM  18198  C   LEU E 368       4.935 -88.904 -49.692  1.00 21.08           C  
-ATOM  18199  O   LEU E 368       4.869 -89.859 -48.923  1.00 20.00           O  
-ATOM  18200  CB  LEU E 368       5.327 -86.750 -48.468  1.00 28.77           C  
-ATOM  18201  CG  LEU E 368       5.066 -85.242 -48.353  1.00 29.90           C  
-ATOM  18202  CD1 LEU E 368       4.798 -84.631 -49.720  1.00 23.56           C  
-ATOM  18203  CD2 LEU E 368       3.918 -84.926 -47.401  1.00 33.25           C  
-ATOM  18204  N   THR E 369       5.516 -88.974 -50.887  1.00 20.54           N  
-ATOM  18205  CA  THR E 369       5.935 -90.250 -51.457  1.00 20.50           C  
-ATOM  18206  C   THR E 369       7.446 -90.408 -51.590  1.00 23.83           C  
-ATOM  18207  O   THR E 369       7.932 -91.501 -51.881  1.00 24.80           O  
-ATOM  18208  CB  THR E 369       5.312 -90.461 -52.848  1.00 18.50           C  
-ATOM  18209  OG1 THR E 369       5.833 -89.487 -53.761  1.00 17.58           O  
-ATOM  18210  CG2 THR E 369       3.798 -90.331 -52.777  1.00 21.71           C  
-ATOM  18211  N   THR E 370       8.192 -89.330 -51.380  1.00 22.30           N  
-ATOM  18212  CA  THR E 370       9.643 -89.400 -51.505  1.00 20.64           C  
-ATOM  18213  C   THR E 370      10.256 -90.046 -50.259  1.00 24.84           C  
-ATOM  18214  O   THR E 370      11.456 -90.320 -50.211  1.00 21.62           O  
-ATOM  18215  CB  THR E 370      10.257 -88.011 -51.739  1.00 18.42           C  
-ATOM  18216  OG1 THR E 370      11.637 -88.150 -52.096  1.00 36.05           O  
-ATOM  18217  CG2 THR E 370      10.139 -87.164 -50.498  1.00 20.85           C  
-ATOM  18218  N   LYS E 371       9.411 -90.278 -49.257  1.00 24.00           N  
-ATOM  18219  CA  LYS E 371       9.746 -91.094 -48.094  1.00 27.12           C  
-ATOM  18220  C   LYS E 371       8.438 -91.613 -47.498  1.00 29.21           C  
-ATOM  18221  O   LYS E 371       7.386 -91.009 -47.700  1.00 35.66           O  
-ATOM  18222  CB  LYS E 371      10.538 -90.299 -47.054  1.00 23.41           C  
-ATOM  18223  CG  LYS E 371       9.706 -89.861 -45.864  1.00 32.95           C  
-ATOM  18224  CD  LYS E 371      10.556 -89.323 -44.734  1.00 46.31           C  
-ATOM  18225  CE  LYS E 371       9.674 -88.924 -43.563  1.00 59.43           C  
-ATOM  18226  NZ  LYS E 371      10.435 -88.274 -42.466  1.00 52.78           N  
-ATOM  18227  N   ARG E 372       8.491 -92.728 -46.776  1.00 28.44           N  
-ATOM  18228  CA  ARG E 372       7.277 -93.293 -46.193  1.00 19.34           C  
-ATOM  18229  C   ARG E 372       6.818 -92.509 -44.964  1.00 25.31           C  
-ATOM  18230  O   ARG E 372       7.586 -92.303 -44.023  1.00 28.43           O  
-ATOM  18231  CB  ARG E 372       7.488 -94.760 -45.824  1.00 30.20           C  
-ATOM  18232  CG  ARG E 372       6.287 -95.396 -45.146  1.00 29.45           C  
-ATOM  18233  CD  ARG E 372       6.464 -96.896 -44.985  1.00 40.95           C  
-ATOM  18234  NE  ARG E 372       6.565 -97.581 -46.271  1.00 29.46           N  
-ATOM  18235  CZ  ARG E 372       5.518 -97.935 -47.009  1.00 23.81           C  
-ATOM  18236  NH1 ARG E 372       4.289 -97.659 -46.592  1.00 16.32           N  
-ATOM  18237  NH2 ARG E 372       5.701 -98.556 -48.167  1.00 19.95           N  
-ATOM  18238  N   VAL E 373       5.559 -92.080 -44.981  1.00 23.32           N  
-ATOM  18239  CA  VAL E 373       4.992 -91.279 -43.897  1.00 19.45           C  
-ATOM  18240  C   VAL E 373       4.149 -92.138 -42.948  1.00 22.62           C  
-ATOM  18241  O   VAL E 373       3.421 -93.029 -43.383  1.00 22.03           O  
-ATOM  18242  CB  VAL E 373       4.138 -90.116 -44.457  1.00 14.72           C  
-ATOM  18243  CG1 VAL E 373       3.461 -89.338 -43.335  1.00  9.02           C  
-ATOM  18244  CG2 VAL E 373       5.002 -89.190 -45.296  1.00 14.32           C  
-ATOM  18245  N   PHE E 374       4.265 -91.858 -41.651  1.00 25.11           N  
-ATOM  18246  CA  PHE E 374       3.596 -92.624 -40.600  1.00 21.68           C  
-ATOM  18247  C   PHE E 374       2.095 -92.324 -40.509  1.00 24.73           C  
-ATOM  18248  O   PHE E 374       1.628 -91.643 -39.586  1.00 29.61           O  
-ATOM  18249  CB  PHE E 374       4.276 -92.346 -39.256  1.00 22.84           C  
-ATOM  18250  CG  PHE E 374       3.901 -93.315 -38.174  1.00 22.93           C  
-ATOM  18251  CD1 PHE E 374       3.551 -94.616 -38.484  1.00 24.96           C  
-ATOM  18252  CD2 PHE E 374       3.896 -92.921 -36.845  1.00 15.75           C  
-ATOM  18253  CE1 PHE E 374       3.206 -95.509 -37.489  1.00 26.63           C  
-ATOM  18254  CE2 PHE E 374       3.551 -93.807 -35.847  1.00 17.03           C  
-ATOM  18255  CZ  PHE E 374       3.205 -95.105 -36.170  1.00 26.04           C  
-ATOM  18256  N   TRP E 375       1.343 -92.860 -41.465  1.00 20.37           N  
-ATOM  18257  CA  TRP E 375      -0.070 -92.534 -41.596  1.00 24.00           C  
-ATOM  18258  C   TRP E 375      -0.899 -93.001 -40.411  1.00 27.84           C  
-ATOM  18259  O   TRP E 375      -1.824 -92.308 -39.987  1.00 34.94           O  
-ATOM  18260  CB  TRP E 375      -0.645 -93.132 -42.877  1.00 22.83           C  
-ATOM  18261  CG  TRP E 375      -2.091 -92.790 -43.051  1.00 26.68           C  
-ATOM  18262  CD1 TRP E 375      -2.609 -91.581 -43.423  1.00 27.88           C  
-ATOM  18263  CD2 TRP E 375      -3.209 -93.656 -42.838  1.00 20.36           C  
-ATOM  18264  NE1 TRP E 375      -3.982 -91.644 -43.463  1.00 20.92           N  
-ATOM  18265  CE2 TRP E 375      -4.374 -92.908 -43.107  1.00 27.38           C  
-ATOM  18266  CE3 TRP E 375      -3.339 -94.995 -42.452  1.00 31.95           C  
-ATOM  18267  CZ2 TRP E 375      -5.651 -93.455 -43.006  1.00 43.45           C  
-ATOM  18268  CZ3 TRP E 375      -4.612 -95.537 -42.348  1.00 47.72           C  
-ATOM  18269  CH2 TRP E 375      -5.749 -94.768 -42.625  1.00 51.56           C  
-ATOM  18270  N   LYS E 376      -0.581 -94.185 -39.898  1.00 16.54           N  
-ATOM  18271  CA  LYS E 376      -1.221 -94.695 -38.693  1.00 22.56           C  
-ATOM  18272  C   LYS E 376      -1.067 -93.679 -37.568  1.00 26.90           C  
-ATOM  18273  O   LYS E 376      -2.001 -93.411 -36.805  1.00 23.11           O  
-ATOM  18274  CB  LYS E 376      -0.610 -96.035 -38.290  1.00 32.65           C  
-ATOM  18275  CG  LYS E 376      -1.126 -96.578 -36.968  1.00 29.69           C  
-ATOM  18276  CD  LYS E 376      -0.252 -97.725 -36.490  1.00 42.05           C  
-ATOM  18277  CE  LYS E 376      -0.641 -98.189 -35.094  1.00 44.52           C  
-ATOM  18278  NZ  LYS E 376      -1.911 -98.963 -35.080  1.00 39.96           N  
-ATOM  18279  N   GLY E 377       0.128 -93.105 -37.494  1.00 21.73           N  
-ATOM  18280  CA  GLY E 377       0.432 -92.056 -36.544  1.00 21.20           C  
-ATOM  18281  C   GLY E 377      -0.400 -90.808 -36.766  1.00 24.73           C  
-ATOM  18282  O   GLY E 377      -0.960 -90.265 -35.808  1.00 26.53           O  
-ATOM  18283  N   VAL E 378      -0.496 -90.341 -38.012  1.00 20.31           N  
-ATOM  18284  CA  VAL E 378      -1.266 -89.116 -38.253  1.00 25.32           C  
-ATOM  18285  C   VAL E 378      -2.746 -89.332 -37.898  1.00 25.09           C  
-ATOM  18286  O   VAL E 378      -3.385 -88.455 -37.298  1.00 26.99           O  
-ATOM  18287  CB  VAL E 378      -1.119 -88.590 -39.726  1.00 20.04           C  
-ATOM  18288  CG1 VAL E 378       0.192 -89.032 -40.338  1.00 20.61           C  
-ATOM  18289  CG2 VAL E 378      -2.273 -89.012 -40.617  1.00 26.15           C  
-ATOM  18290  N   LEU E 379      -3.268 -90.515 -38.219  1.00 16.01           N  
-ATOM  18291  CA  LEU E 379      -4.670 -90.832 -37.976  1.00 19.42           C  
-ATOM  18292  C   LEU E 379      -4.956 -90.922 -36.488  1.00 22.57           C  
-ATOM  18293  O   LEU E 379      -5.875 -90.278 -35.981  1.00 23.41           O  
-ATOM  18294  CB  LEU E 379      -5.054 -92.146 -38.670  1.00 21.05           C  
-ATOM  18295  CG  LEU E 379      -6.469 -92.658 -38.393  1.00 18.08           C  
-ATOM  18296  CD1 LEU E 379      -7.514 -91.663 -38.872  1.00 16.61           C  
-ATOM  18297  CD2 LEU E 379      -6.694 -94.019 -39.028  1.00 19.95           C  
-ATOM  18298  N   GLU E 380      -4.162 -91.729 -35.794  1.00 21.87           N  
-ATOM  18299  CA  GLU E 380      -4.352 -91.931 -34.365  1.00 24.91           C  
-ATOM  18300  C   GLU E 380      -4.204 -90.620 -33.608  1.00 24.58           C  
-ATOM  18301  O   GLU E 380      -5.016 -90.310 -32.736  1.00 25.02           O  
-ATOM  18302  CB  GLU E 380      -3.364 -92.969 -33.824  1.00 25.53           C  
-ATOM  18303  CG  GLU E 380      -4.002 -93.985 -32.893  1.00 33.50           C  
-ATOM  18304  CD  GLU E 380      -5.113 -94.770 -33.565  1.00 35.51           C  
-ATOM  18305  OE1 GLU E 380      -6.181 -94.947 -32.942  1.00 37.36           O  
-ATOM  18306  OE2 GLU E 380      -4.920 -95.209 -34.719  1.00 28.17           O  
-ATOM  18307  N   GLU E 381      -3.177 -89.843 -33.951  1.00 21.21           N  
-ATOM  18308  CA  GLU E 381      -2.956 -88.563 -33.283  1.00 19.31           C  
-ATOM  18309  C   GLU E 381      -4.093 -87.587 -33.561  1.00 18.95           C  
-ATOM  18310  O   GLU E 381      -4.478 -86.820 -32.684  1.00 15.69           O  
-ATOM  18311  CB  GLU E 381      -1.623 -87.930 -33.705  1.00 25.44           C  
-ATOM  18312  CG  GLU E 381      -1.212 -86.762 -32.808  1.00 21.39           C  
-ATOM  18313  CD  GLU E 381      -0.151 -85.871 -33.426  1.00 24.73           C  
-ATOM  18314  OE1 GLU E 381       0.794 -85.482 -32.707  1.00 31.91           O  
-ATOM  18315  OE2 GLU E 381      -0.270 -85.540 -34.625  1.00 29.13           O  
-ATOM  18316  N   LEU E 382      -4.625 -87.608 -34.781  1.00 24.05           N  
-ATOM  18317  CA  LEU E 382      -5.724 -86.704 -35.118  1.00 18.52           C  
-ATOM  18318  C   LEU E 382      -7.000 -87.066 -34.362  1.00 13.18           C  
-ATOM  18319  O   LEU E 382      -7.677 -86.191 -33.822  1.00 14.62           O  
-ATOM  18320  CB  LEU E 382      -5.991 -86.700 -36.627  1.00 18.90           C  
-ATOM  18321  CG  LEU E 382      -7.076 -85.713 -37.080  1.00 22.13           C  
-ATOM  18322  CD1 LEU E 382      -6.811 -84.317 -36.531  1.00 21.92           C  
-ATOM  18323  CD2 LEU E 382      -7.177 -85.678 -38.596  1.00 14.61           C  
-ATOM  18324  N   LEU E 383      -7.326 -88.354 -34.329  1.00 12.99           N  
-ATOM  18325  CA  LEU E 383      -8.489 -88.825 -33.580  1.00 13.13           C  
-ATOM  18326  C   LEU E 383      -8.336 -88.472 -32.106  1.00 17.63           C  
-ATOM  18327  O   LEU E 383      -9.292 -88.081 -31.440  1.00 24.07           O  
-ATOM  18328  CB  LEU E 383      -8.669 -90.335 -33.759  1.00 20.00           C  
-ATOM  18329  CG  LEU E 383      -9.601 -90.799 -34.883  1.00 21.59           C  
-ATOM  18330  CD1 LEU E 383      -9.548 -89.850 -36.064  1.00 21.54           C  
-ATOM  18331  CD2 LEU E 383      -9.238 -92.208 -35.323  1.00 23.69           C  
-ATOM  18332  N   TRP E 384      -7.108 -88.613 -31.622  1.00 15.62           N  
-ATOM  18333  CA  TRP E 384      -6.704 -88.201 -30.282  1.00 17.20           C  
-ATOM  18334  C   TRP E 384      -7.053 -86.728 -30.021  1.00 15.98           C  
-ATOM  18335  O   TRP E 384      -7.761 -86.401 -29.056  1.00 14.04           O  
-ATOM  18336  CB  TRP E 384      -5.197 -88.461 -30.132  1.00 24.86           C  
-ATOM  18337  CG  TRP E 384      -4.623 -88.342 -28.759  1.00 17.75           C  
-ATOM  18338  CD1 TRP E 384      -4.906 -89.120 -27.677  1.00 23.26           C  
-ATOM  18339  CD2 TRP E 384      -3.612 -87.422 -28.338  1.00 17.63           C  
-ATOM  18340  NE1 TRP E 384      -4.156 -88.720 -26.598  1.00 26.51           N  
-ATOM  18341  CE2 TRP E 384      -3.352 -87.679 -26.980  1.00 22.69           C  
-ATOM  18342  CE3 TRP E 384      -2.913 -86.395 -28.977  1.00 21.57           C  
-ATOM  18343  CZ2 TRP E 384      -2.421 -86.946 -26.248  1.00 27.77           C  
-ATOM  18344  CZ3 TRP E 384      -1.990 -85.669 -28.250  1.00 27.07           C  
-ATOM  18345  CH2 TRP E 384      -1.751 -85.948 -26.901  1.00 31.26           C  
-ATOM  18346  N   PHE E 385      -6.554 -85.855 -30.894  1.00 19.20           N  
-ATOM  18347  CA  PHE E 385      -6.869 -84.428 -30.859  1.00 18.68           C  
-ATOM  18348  C   PHE E 385      -8.362 -84.180 -30.774  1.00 19.41           C  
-ATOM  18349  O   PHE E 385      -8.824 -83.438 -29.911  1.00 25.76           O  
-ATOM  18350  CB  PHE E 385      -6.329 -83.716 -32.102  1.00 19.01           C  
-ATOM  18351  CG  PHE E 385      -4.846 -83.542 -32.114  1.00 20.88           C  
-ATOM  18352  CD1 PHE E 385      -4.111 -83.642 -30.946  1.00 24.07           C  
-ATOM  18353  CD2 PHE E 385      -4.184 -83.271 -33.298  1.00 17.54           C  
-ATOM  18354  CE1 PHE E 385      -2.740 -83.479 -30.959  1.00 25.23           C  
-ATOM  18355  CE2 PHE E 385      -2.810 -83.107 -33.319  1.00 16.00           C  
-ATOM  18356  CZ  PHE E 385      -2.089 -83.210 -32.150  1.00 21.32           C  
-ATOM  18357  N   ILE E 386      -9.106 -84.792 -31.690  1.00 15.64           N  
-ATOM  18358  CA  ILE E 386     -10.548 -84.600 -31.759  1.00 19.21           C  
-ATOM  18359  C   ILE E 386     -11.226 -85.011 -30.458  1.00 21.03           C  
-ATOM  18360  O   ILE E 386     -12.121 -84.317 -29.972  1.00 19.97           O  
-ATOM  18361  CB  ILE E 386     -11.157 -85.380 -32.942  1.00 19.39           C  
-ATOM  18362  CG1 ILE E 386     -10.652 -84.792 -34.262  1.00 13.76           C  
-ATOM  18363  CG2 ILE E 386     -12.681 -85.346 -32.890  1.00 23.39           C  
-ATOM  18364  CD1 ILE E 386     -11.271 -85.413 -35.474  1.00 13.57           C  
-ATOM  18365  N   ARG E 387     -10.787 -86.128 -29.886  1.00 23.07           N  
-ATOM  18366  CA  ARG E 387     -11.295 -86.550 -28.585  1.00 21.56           C  
-ATOM  18367  C   ARG E 387     -10.907 -85.539 -27.512  1.00 22.75           C  
-ATOM  18368  O   ARG E 387     -11.562 -85.435 -26.476  1.00 20.49           O  
-ATOM  18369  CB  ARG E 387     -10.777 -87.943 -28.218  1.00 17.79           C  
-ATOM  18370  CG  ARG E 387     -11.289 -89.051 -29.124  1.00 22.72           C  
-ATOM  18371  CD  ARG E 387     -10.926 -90.433 -28.598  1.00 14.18           C  
-ATOM  18372  NE  ARG E 387     -10.942 -91.427 -29.666  1.00 14.76           N  
-ATOM  18373  CZ  ARG E 387      -9.871 -91.770 -30.374  1.00 25.80           C  
-ATOM  18374  NH1 ARG E 387      -8.699 -91.202 -30.120  1.00 28.24           N  
-ATOM  18375  NH2 ARG E 387      -9.966 -92.682 -31.333  1.00 24.61           N  
-ATOM  18376  N   GLY E 388      -9.845 -84.784 -27.776  1.00 28.19           N  
-ATOM  18377  CA  GLY E 388      -9.399 -83.765 -26.843  1.00 24.34           C  
-ATOM  18378  C   GLY E 388      -8.632 -84.422 -25.720  1.00 32.86           C  
-ATOM  18379  O   GLY E 388      -8.584 -83.924 -24.596  1.00 35.94           O  
-ATOM  18380  N   ASP E 389      -8.034 -85.562 -26.041  1.00 25.05           N  
-ATOM  18381  CA  ASP E 389      -7.281 -86.346 -25.081  1.00 20.26           C  
-ATOM  18382  C   ASP E 389      -5.922 -85.706 -24.836  1.00 23.40           C  
-ATOM  18383  O   ASP E 389      -5.308 -85.164 -25.754  1.00 23.49           O  
-ATOM  18384  CB  ASP E 389      -7.125 -87.775 -25.595  1.00 23.93           C  
-ATOM  18385  CG  ASP E 389      -6.705 -88.751 -24.516  1.00 29.04           C  
-ATOM  18386  OD1 ASP E 389      -6.272 -88.314 -23.429  1.00 31.45           O  
-ATOM  18387  OD2 ASP E 389      -6.804 -89.970 -24.769  1.00 25.67           O  
-ATOM  18388  N   THR E 390      -5.459 -85.763 -23.594  1.00 31.43           N  
-ATOM  18389  CA  THR E 390      -4.163 -85.199 -23.237  1.00 29.39           C  
-ATOM  18390  C   THR E 390      -3.258 -86.287 -22.664  1.00 27.29           C  
-ATOM  18391  O   THR E 390      -2.185 -86.008 -22.130  1.00 26.92           O  
-ATOM  18392  CB  THR E 390      -4.314 -84.047 -22.227  1.00 25.98           C  
-ATOM  18393  OG1 THR E 390      -5.030 -84.509 -21.075  1.00 28.77           O  
-ATOM  18394  CG2 THR E 390      -5.084 -82.897 -22.854  1.00 26.61           C  
-ATOM  18395  N   ASN E 391      -3.707 -87.531 -22.791  1.00 30.00           N  
-ATOM  18396  CA  ASN E 391      -2.962 -88.685 -22.308  1.00 26.42           C  
-ATOM  18397  C   ASN E 391      -2.163 -89.334 -23.436  1.00 32.44           C  
-ATOM  18398  O   ASN E 391      -2.725 -90.033 -24.280  1.00 38.51           O  
-ATOM  18399  CB  ASN E 391      -3.922 -89.699 -21.679  1.00 28.27           C  
-ATOM  18400  CG  ASN E 391      -3.210 -90.742 -20.843  1.00 37.04           C  
-ATOM  18401  OD1 ASN E 391      -2.085 -91.137 -21.146  1.00 46.56           O  
-ATOM  18402  ND2 ASN E 391      -3.866 -91.194 -19.780  1.00 31.92           N  
-ATOM  18403  N   ALA E 392      -0.853 -89.105 -23.443  1.00 29.04           N  
-ATOM  18404  CA  ALA E 392       0.007 -89.598 -24.514  1.00 29.45           C  
-ATOM  18405  C   ALA E 392       0.140 -91.117 -24.488  1.00 36.02           C  
-ATOM  18406  O   ALA E 392       0.501 -91.735 -25.489  1.00 38.88           O  
-ATOM  18407  CB  ALA E 392       1.380 -88.946 -24.425  1.00 34.48           C  
-ATOM  18408  N   ASN E 393      -0.154 -91.716 -23.339  1.00 30.78           N  
-ATOM  18409  CA  ASN E 393      -0.053 -93.161 -23.194  1.00 29.59           C  
-ATOM  18410  C   ASN E 393      -1.091 -93.888 -24.039  1.00 39.83           C  
-ATOM  18411  O   ASN E 393      -0.859 -95.012 -24.485  1.00 44.33           O  
-ATOM  18412  CB  ASN E 393      -0.192 -93.556 -21.726  1.00 24.38           C  
-ATOM  18413  CG  ASN E 393       0.885 -92.942 -20.859  1.00 37.21           C  
-ATOM  18414  OD1 ASN E 393       2.060 -92.912 -21.233  1.00 37.47           O  
-ATOM  18415  ND2 ASN E 393       0.492 -92.446 -19.693  1.00 39.11           N  
-ATOM  18416  N   HIS E 394      -2.234 -93.243 -24.257  1.00 38.84           N  
-ATOM  18417  CA  HIS E 394      -3.271 -93.794 -25.124  1.00 28.80           C  
-ATOM  18418  C   HIS E 394      -2.761 -93.901 -26.557  1.00 36.55           C  
-ATOM  18419  O   HIS E 394      -3.172 -94.785 -27.308  1.00 40.37           O  
-ATOM  18420  CB  HIS E 394      -4.537 -92.937 -25.075  1.00 26.24           C  
-ATOM  18421  CG  HIS E 394      -5.126 -92.809 -23.705  1.00 25.89           C  
-ATOM  18422  ND1 HIS E 394      -6.191 -91.980 -23.429  1.00 23.33           N  
-ATOM  18423  CD2 HIS E 394      -4.798 -93.403 -22.534  1.00 25.12           C  
-ATOM  18424  CE1 HIS E 394      -6.495 -92.069 -22.147  1.00 24.54           C  
-ATOM  18425  NE2 HIS E 394      -5.665 -92.926 -21.581  1.00 27.50           N  
-ATOM  18426  N   LEU E 395      -1.871 -92.988 -26.934  1.00 31.14           N  
-ATOM  18427  CA  LEU E 395      -1.227 -93.040 -28.240  1.00 30.29           C  
-ATOM  18428  C   LEU E 395      -0.091 -94.051 -28.240  1.00 37.30           C  
-ATOM  18429  O   LEU E 395       0.139 -94.740 -29.233  1.00 37.44           O  
-ATOM  18430  CB  LEU E 395      -0.691 -91.664 -28.643  1.00 25.61           C  
-ATOM  18431  CG  LEU E 395      -1.659 -90.667 -29.279  1.00 28.57           C  
-ATOM  18432  CD1 LEU E 395      -0.937 -89.365 -29.593  1.00 32.15           C  
-ATOM  18433  CD2 LEU E 395      -2.289 -91.251 -30.533  1.00 27.01           C  
-ATOM  18434  N   SER E 396       0.619 -94.130 -27.120  1.00 38.45           N  
-ATOM  18435  CA  SER E 396       1.802 -94.971 -27.022  1.00 35.93           C  
-ATOM  18436  C   SER E 396       1.456 -96.454 -27.056  1.00 38.49           C  
-ATOM  18437  O   SER E 396       2.154 -97.241 -27.694  1.00 34.79           O  
-ATOM  18438  CB  SER E 396       2.578 -94.644 -25.744  1.00 37.47           C  
-ATOM  18439  OG  SER E 396       3.870 -95.229 -25.762  1.00 48.19           O  
-ATOM  18440  N   GLU E 397       0.381 -96.835 -26.372  1.00 41.36           N  
-ATOM  18441  CA  GLU E 397       0.002 -98.243 -26.294  1.00 41.52           C  
-ATOM  18442  C   GLU E 397      -0.670 -98.716 -27.587  1.00 42.31           C  
-ATOM  18443  O   GLU E 397      -0.815 -99.919 -27.819  1.00 57.42           O  
-ATOM  18444  CB  GLU E 397      -0.907 -98.489 -25.081  1.00 40.48           C  
-ATOM  18445  CG  GLU E 397      -2.347 -98.864 -25.404  1.00 52.70           C  
-ATOM  18446  CD  GLU E 397      -3.291 -97.684 -25.323  1.00 63.77           C  
-ATOM  18447  OE1 GLU E 397      -3.230 -96.941 -24.319  1.00 59.65           O  
-ATOM  18448  OE2 GLU E 397      -4.094 -97.500 -26.263  1.00 60.34           O  
-ATOM  18449  N   LYS E 398      -1.060 -97.770 -28.435  1.00 37.02           N  
-ATOM  18450  CA  LYS E 398      -1.594 -98.110 -29.749  1.00 33.83           C  
-ATOM  18451  C   LYS E 398      -0.476 -98.257 -30.777  1.00 32.11           C  
-ATOM  18452  O   LYS E 398      -0.731 -98.574 -31.937  1.00 33.22           O  
-ATOM  18453  CB  LYS E 398      -2.593 -97.057 -30.221  1.00 35.10           C  
-ATOM  18454  CG  LYS E 398      -3.924 -97.092 -29.490  1.00 46.33           C  
-ATOM  18455  CD  LYS E 398      -4.951 -96.209 -30.176  1.00 36.14           C  
-ATOM  18456  CE  LYS E 398      -6.273 -96.210 -29.429  1.00 40.09           C  
-ATOM  18457  NZ  LYS E 398      -6.117 -95.678 -28.048  1.00 41.17           N  
-ATOM  18458  N   GLY E 399       0.761 -98.024 -30.351  1.00 28.70           N  
-ATOM  18459  CA  GLY E 399       1.908 -98.190 -31.225  1.00 27.99           C  
-ATOM  18460  C   GLY E 399       2.425 -96.889 -31.803  1.00 31.17           C  
-ATOM  18461  O   GLY E 399       3.272 -96.894 -32.699  1.00 27.47           O  
-ATOM  18462  N   VAL E 400       1.915 -95.772 -31.290  1.00 33.93           N  
-ATOM  18463  CA  VAL E 400       2.340 -94.451 -31.747  1.00 34.34           C  
-ATOM  18464  C   VAL E 400       3.093 -93.716 -30.640  1.00 38.99           C  
-ATOM  18465  O   VAL E 400       2.485 -93.095 -29.765  1.00 37.67           O  
-ATOM  18466  CB  VAL E 400       1.144 -93.591 -32.205  1.00 24.60           C  
-ATOM  18467  CG1 VAL E 400       1.631 -92.398 -33.005  1.00 24.59           C  
-ATOM  18468  CG2 VAL E 400       0.179 -94.420 -33.037  1.00 31.24           C  
-ATOM  18469  N   LYS E 401       4.420 -93.783 -30.687  1.00 39.00           N  
-ATOM  18470  CA  LYS E 401       5.254 -93.263 -29.607  1.00 42.55           C  
-ATOM  18471  C   LYS E 401       5.832 -91.891 -29.917  1.00 45.90           C  
-ATOM  18472  O   LYS E 401       6.856 -91.502 -29.356  1.00 50.80           O  
-ATOM  18473  CB  LYS E 401       6.395 -94.238 -29.310  1.00 29.21           C  
-ATOM  18474  CG  LYS E 401       5.945 -95.602 -28.828  1.00 33.03           C  
-ATOM  18475  CD  LYS E 401       6.882 -96.689 -29.326  1.00 38.94           C  
-ATOM  18476  CE  LYS E 401       6.822 -96.814 -30.846  1.00 60.60           C  
-ATOM  18477  NZ  LYS E 401       7.774 -97.837 -31.373  1.00 53.94           N  
-ATOM  18478  N   ILE E 402       5.170 -91.157 -30.802  1.00 45.63           N  
-ATOM  18479  CA  ILE E 402       5.690 -89.880 -31.278  1.00 47.31           C  
-ATOM  18480  C   ILE E 402       5.694 -88.791 -30.206  1.00 50.27           C  
-ATOM  18481  O   ILE E 402       6.316 -87.744 -30.383  1.00 60.40           O  
-ATOM  18482  CB  ILE E 402       4.885 -89.378 -32.485  1.00 39.24           C  
-ATOM  18483  CG1 ILE E 402       3.507 -88.892 -32.038  1.00 41.10           C  
-ATOM  18484  CG2 ILE E 402       4.748 -90.480 -33.519  1.00 43.15           C  
-ATOM  18485  CD1 ILE E 402       2.648 -88.378 -33.169  1.00 35.52           C  
-ATOM  18486  N   TRP E 403       5.005 -89.038 -29.096  1.00 42.48           N  
-ATOM  18487  CA  TRP E 403       4.904 -88.050 -28.026  1.00 43.54           C  
-ATOM  18488  C   TRP E 403       5.758 -88.397 -26.810  1.00 47.15           C  
-ATOM  18489  O   TRP E 403       6.071 -87.525 -26.000  1.00 45.32           O  
-ATOM  18490  CB  TRP E 403       3.446 -87.889 -27.590  1.00 41.44           C  
-ATOM  18491  CG  TRP E 403       2.704 -86.818 -28.319  1.00 35.66           C  
-ATOM  18492  CD1 TRP E 403       1.971 -86.959 -29.460  1.00 37.52           C  
-ATOM  18493  CD2 TRP E 403       2.611 -85.437 -27.950  1.00 46.49           C  
-ATOM  18494  NE1 TRP E 403       1.430 -85.751 -29.827  1.00 41.38           N  
-ATOM  18495  CE2 TRP E 403       1.808 -84.800 -28.916  1.00 49.34           C  
-ATOM  18496  CE3 TRP E 403       3.131 -84.677 -26.897  1.00 50.65           C  
-ATOM  18497  CZ2 TRP E 403       1.512 -83.440 -28.862  1.00 48.37           C  
-ATOM  18498  CZ3 TRP E 403       2.836 -83.325 -26.845  1.00 48.62           C  
-ATOM  18499  CH2 TRP E 403       2.034 -82.721 -27.821  1.00 49.55           C  
-ATOM  18500  N   ASP E 404       6.133 -89.667 -26.698  1.00 48.74           N  
-ATOM  18501  CA  ASP E 404       6.786 -90.201 -25.503  1.00 47.64           C  
-ATOM  18502  C   ASP E 404       7.962 -89.367 -24.996  1.00 44.75           C  
-ATOM  18503  O   ASP E 404       8.003 -88.988 -23.823  1.00 50.23           O  
-ATOM  18504  CB  ASP E 404       7.248 -91.634 -25.775  1.00 54.43           C  
-ATOM  18505  CG  ASP E 404       6.086 -92.591 -25.990  1.00 56.46           C  
-ATOM  18506  OD1 ASP E 404       4.959 -92.121 -26.264  1.00 50.50           O  
-ATOM  18507  OD2 ASP E 404       6.305 -93.816 -25.886  1.00 43.31           O  
-ATOM  18508  N   LYS E 405       8.902 -89.065 -25.885  1.00 40.77           N  
-ATOM  18509  CA  LYS E 405      10.101 -88.318 -25.514  1.00 47.98           C  
-ATOM  18510  C   LYS E 405       9.812 -86.949 -24.888  1.00 49.07           C  
-ATOM  18511  O   LYS E 405      10.675 -86.380 -24.221  1.00 45.45           O  
-ATOM  18512  CB  LYS E 405      11.007 -88.135 -26.733  1.00 41.57           C  
-ATOM  18513  CG  LYS E 405      11.872 -89.340 -27.057  1.00 49.15           C  
-ATOM  18514  CD  LYS E 405      12.792 -89.044 -28.227  1.00 47.42           C  
-ATOM  18515  CE  LYS E 405      13.560 -90.284 -28.641  1.00 47.62           C  
-ATOM  18516  NZ  LYS E 405      14.257 -90.093 -29.940  1.00 50.43           N  
-ATOM  18517  N   ASN E 406       8.608 -86.423 -25.097  1.00 53.42           N  
-ATOM  18518  CA  ASN E 406       8.256 -85.110 -24.559  1.00 44.71           C  
-ATOM  18519  C   ASN E 406       7.296 -85.186 -23.378  1.00 39.11           C  
-ATOM  18520  O   ASN E 406       6.790 -84.166 -22.918  1.00 39.62           O  
-ATOM  18521  CB  ASN E 406       7.653 -84.229 -25.654  1.00 42.13           C  
-ATOM  18522  CG  ASN E 406       8.656 -83.876 -26.731  1.00 51.11           C  
-ATOM  18523  OD1 ASN E 406       8.391 -84.038 -27.921  1.00 67.94           O  
-ATOM  18524  ND2 ASN E 406       9.823 -83.397 -26.316  1.00 46.32           N  
-ATOM  18525  N   VAL E 407       7.042 -86.396 -22.893  1.00 41.31           N  
-ATOM  18526  CA  VAL E 407       6.199 -86.564 -21.712  1.00 52.10           C  
-ATOM  18527  C   VAL E 407       6.859 -87.484 -20.690  1.00 52.17           C  
-ATOM  18528  O   VAL E 407       6.204 -87.990 -19.775  1.00 43.54           O  
-ATOM  18529  CB  VAL E 407       4.803 -87.117 -22.074  1.00 50.40           C  
-ATOM  18530  CG1 VAL E 407       3.967 -86.044 -22.754  1.00 45.45           C  
-ATOM  18531  CG2 VAL E 407       4.924 -88.355 -22.948  1.00 42.48           C  
-ATOM  18532  N   THR E 408       8.162 -87.692 -20.850  1.00 49.84           N  
-ATOM  18533  CA  THR E 408       8.942 -88.425 -19.863  1.00 47.07           C  
-ATOM  18534  C   THR E 408       9.006 -87.626 -18.569  1.00 51.06           C  
-ATOM  18535  O   THR E 408       8.801 -86.415 -18.578  1.00 53.65           O  
-ATOM  18536  CB  THR E 408      10.376 -88.707 -20.360  1.00 37.82           C  
-ATOM  18537  OG1 THR E 408      11.044 -87.467 -20.625  1.00 39.27           O  
-ATOM  18538  CG2 THR E 408      10.350 -89.536 -21.627  1.00 31.99           C  
-ATOM  18539  N   ARG E 409       9.276 -88.307 -17.460  1.00 42.58           N  
-ATOM  18540  CA  ARG E 409       9.443 -87.640 -16.172  1.00 46.51           C  
-ATOM  18541  C   ARG E 409      10.550 -86.588 -16.247  1.00 47.84           C  
-ATOM  18542  O   ARG E 409      10.408 -85.473 -15.734  1.00 46.44           O  
-ATOM  18543  CB  ARG E 409       9.745 -88.674 -15.080  1.00 32.66           C  
-ATOM  18544  CG  ARG E 409      10.339 -88.108 -13.802  1.00 36.80           C  
-ATOM  18545  CD  ARG E 409       9.273 -87.636 -12.822  1.00 39.48           C  
-ATOM  18546  NE  ARG E 409       8.659 -86.372 -13.218  1.00 45.24           N  
-ATOM  18547  CZ  ARG E 409       7.382 -86.233 -13.564  1.00 52.97           C  
-ATOM  18548  NH1 ARG E 409       6.569 -87.281 -13.561  1.00 47.30           N  
-ATOM  18549  NH2 ARG E 409       6.917 -85.040 -13.909  1.00 52.41           N  
-ATOM  18550  N   GLU E 410      11.642 -86.950 -16.912  1.00 44.16           N  
-ATOM  18551  CA  GLU E 410      12.788 -86.066 -17.069  1.00 48.12           C  
-ATOM  18552  C   GLU E 410      12.422 -84.771 -17.790  1.00 50.46           C  
-ATOM  18553  O   GLU E 410      12.786 -83.679 -17.345  1.00 47.76           O  
-ATOM  18554  CB  GLU E 410      13.908 -86.793 -17.821  1.00 56.31           C  
-ATOM  18555  CG  GLU E 410      15.209 -86.015 -17.916  1.00 66.00           C  
-ATOM  18556  CD  GLU E 410      16.289 -86.781 -18.655  1.00 78.12           C  
-ATOM  18557  OE1 GLU E 410      16.156 -86.961 -19.885  1.00 71.27           O  
-ATOM  18558  OE2 GLU E 410      17.267 -87.209 -18.006  1.00 83.32           O  
-ATOM  18559  N   PHE E 411      11.698 -84.894 -18.899  1.00 57.06           N  
-ATOM  18560  CA  PHE E 411      11.320 -83.727 -19.693  1.00 53.66           C  
-ATOM  18561  C   PHE E 411      10.258 -82.894 -18.984  1.00 44.07           C  
-ATOM  18562  O   PHE E 411      10.317 -81.663 -18.992  1.00 42.51           O  
-ATOM  18563  CB  PHE E 411      10.814 -84.147 -21.076  1.00 39.97           C  
-ATOM  18564  CG  PHE E 411      10.618 -82.996 -22.023  1.00 42.10           C  
-ATOM  18565  CD1 PHE E 411      11.696 -82.453 -22.704  1.00 41.27           C  
-ATOM  18566  CD2 PHE E 411       9.360 -82.451 -22.224  1.00 38.62           C  
-ATOM  18567  CE1 PHE E 411      11.524 -81.390 -23.573  1.00 38.32           C  
-ATOM  18568  CE2 PHE E 411       9.181 -81.387 -23.094  1.00 37.75           C  
-ATOM  18569  CZ  PHE E 411      10.265 -80.857 -23.768  1.00 37.18           C  
-ATOM  18570  N   LEU E 412       9.289 -83.572 -18.376  1.00 42.44           N  
-ATOM  18571  CA  LEU E 412       8.250 -82.905 -17.600  1.00 47.30           C  
-ATOM  18572  C   LEU E 412       8.858 -82.091 -16.462  1.00 52.33           C  
-ATOM  18573  O   LEU E 412       8.352 -81.023 -16.113  1.00 49.45           O  
-ATOM  18574  CB  LEU E 412       7.249 -83.925 -17.049  1.00 41.54           C  
-ATOM  18575  CG  LEU E 412       6.187 -84.444 -18.023  1.00 43.93           C  
-ATOM  18576  CD1 LEU E 412       5.318 -85.513 -17.371  1.00 39.82           C  
-ATOM  18577  CD2 LEU E 412       5.332 -83.296 -18.540  1.00 37.76           C  
-ATOM  18578  N   ASP E 413       9.946 -82.600 -15.890  1.00 57.80           N  
-ATOM  18579  CA  ASP E 413      10.660 -81.880 -14.842  1.00 47.47           C  
-ATOM  18580  C   ASP E 413      11.496 -80.741 -15.421  1.00 43.10           C  
-ATOM  18581  O   ASP E 413      11.617 -79.677 -14.813  1.00 46.31           O  
-ATOM  18582  CB  ASP E 413      11.546 -82.839 -14.044  1.00 51.00           C  
-ATOM  18583  CG  ASP E 413      10.748 -83.709 -13.092  1.00 51.60           C  
-ATOM  18584  OD1 ASP E 413       9.739 -83.215 -12.547  1.00 53.71           O  
-ATOM  18585  OD2 ASP E 413      11.124 -84.883 -12.886  1.00 43.81           O  
-ATOM  18586  N   SER E 414      12.069 -80.964 -16.600  1.00 46.30           N  
-ATOM  18587  CA  SER E 414      12.864 -79.935 -17.262  1.00 48.25           C  
-ATOM  18588  C   SER E 414      11.969 -78.785 -17.717  1.00 48.22           C  
-ATOM  18589  O   SER E 414      12.447 -77.690 -18.013  1.00 45.75           O  
-ATOM  18590  CB  SER E 414      13.622 -80.519 -18.455  1.00 52.70           C  
-ATOM  18591  OG  SER E 414      12.948 -80.245 -19.671  1.00 48.29           O  
-ATOM  18592  N   ARG E 415      10.668 -79.051 -17.774  1.00 52.14           N  
-ATOM  18593  CA  ARG E 415       9.674 -78.044 -18.132  1.00 53.12           C  
-ATOM  18594  C   ARG E 415       9.143 -77.373 -16.859  1.00 49.66           C  
-ATOM  18595  O   ARG E 415       8.189 -76.593 -16.899  1.00 40.11           O  
-ATOM  18596  CB  ARG E 415       8.534 -78.689 -18.932  1.00 47.25           C  
-ATOM  18597  CG  ARG E 415       7.567 -77.726 -19.619  1.00 51.34           C  
-ATOM  18598  CD  ARG E 415       8.031 -77.336 -21.012  1.00 46.73           C  
-ATOM  18599  NE  ARG E 415       7.039 -76.512 -21.699  1.00 50.15           N  
-ATOM  18600  CZ  ARG E 415       7.058 -75.183 -21.724  1.00 56.77           C  
-ATOM  18601  NH1 ARG E 415       6.112 -74.515 -22.373  1.00 63.69           N  
-ATOM  18602  NH2 ARG E 415       8.024 -74.520 -21.105  1.00 53.79           N  
-ATOM  18603  N   ASN E 416       9.788 -77.679 -15.734  1.00 49.58           N  
-ATOM  18604  CA  ASN E 416       9.358 -77.218 -14.415  1.00 46.42           C  
-ATOM  18605  C   ASN E 416       7.906 -77.609 -14.147  1.00 38.37           C  
-ATOM  18606  O   ASN E 416       7.069 -76.764 -13.833  1.00 32.51           O  
-ATOM  18607  CB  ASN E 416       9.541 -75.704 -14.279  1.00 48.39           C  
-ATOM  18608  CG  ASN E 416       9.591 -75.248 -12.830  1.00 57.86           C  
-ATOM  18609  OD1 ASN E 416       9.236 -75.995 -11.915  1.00 52.12           O  
-ATOM  18610  ND2 ASN E 416      10.030 -74.013 -12.615  1.00 57.01           N  
-ATOM  18611  N   LEU E 417       7.621 -78.901 -14.282  1.00 44.25           N  
-ATOM  18612  CA  LEU E 417       6.283 -79.438 -14.049  1.00 45.92           C  
-ATOM  18613  C   LEU E 417       6.330 -80.801 -13.363  1.00 43.98           C  
-ATOM  18614  O   LEU E 417       5.965 -81.810 -13.964  1.00 38.83           O  
-ATOM  18615  CB  LEU E 417       5.521 -79.552 -15.369  1.00 44.92           C  
-ATOM  18616  CG  LEU E 417       4.556 -78.425 -15.727  1.00 42.60           C  
-ATOM  18617  CD1 LEU E 417       4.075 -78.583 -17.156  1.00 31.40           C  
-ATOM  18618  CD2 LEU E 417       3.382 -78.426 -14.763  1.00 52.23           C  
-ATOM  18619  N   PRO E 418       6.777 -80.836 -12.096  1.00 51.97           N  
-ATOM  18620  CA  PRO E 418       6.908 -82.108 -11.379  1.00 53.54           C  
-ATOM  18621  C   PRO E 418       5.564 -82.728 -11.016  1.00 48.72           C  
-ATOM  18622  O   PRO E 418       5.493 -83.929 -10.764  1.00 44.65           O  
-ATOM  18623  CB  PRO E 418       7.681 -81.720 -10.108  1.00 52.00           C  
-ATOM  18624  CG  PRO E 418       8.259 -80.367 -10.392  1.00 51.45           C  
-ATOM  18625  CD  PRO E 418       7.264 -79.710 -11.285  1.00 49.85           C  
-ATOM  18626  N   HIS E 419       4.512 -81.915 -10.999  1.00 54.89           N  
-ATOM  18627  CA  HIS E 419       3.189 -82.373 -10.585  1.00 47.47           C  
-ATOM  18628  C   HIS E 419       2.490 -83.189 -11.667  1.00 45.29           C  
-ATOM  18629  O   HIS E 419       1.397 -83.712 -11.451  1.00 33.78           O  
-ATOM  18630  CB  HIS E 419       2.324 -81.175 -10.186  1.00 54.31           C  
-ATOM  18631  CG  HIS E 419       2.781 -80.498  -8.932  1.00 91.46           C  
-ATOM  18632  ND1 HIS E 419       2.163 -80.691  -7.714  1.00 92.71           N  
-ATOM  18633  CD2 HIS E 419       3.805 -79.642  -8.702  1.00 87.38           C  
-ATOM  18634  CE1 HIS E 419       2.782 -79.977  -6.791  1.00 83.96           C  
-ATOM  18635  NE2 HIS E 419       3.782 -79.332  -7.364  1.00 87.86           N  
-ATOM  18636  N   ARG E 420       3.127 -83.299 -12.827  1.00 44.26           N  
-ATOM  18637  CA  ARG E 420       2.539 -84.002 -13.960  1.00 35.03           C  
-ATOM  18638  C   ARG E 420       2.826 -85.497 -13.925  1.00 45.94           C  
-ATOM  18639  O   ARG E 420       3.949 -85.922 -13.649  1.00 53.80           O  
-ATOM  18640  CB  ARG E 420       3.054 -83.416 -15.273  1.00 37.02           C  
-ATOM  18641  CG  ARG E 420       2.526 -82.027 -15.588  1.00 43.94           C  
-ATOM  18642  CD  ARG E 420       1.247 -82.087 -16.406  1.00 31.09           C  
-ATOM  18643  NE  ARG E 420       0.753 -80.752 -16.727  1.00 30.88           N  
-ATOM  18644  CZ  ARG E 420      -0.174 -80.112 -16.022  1.00 40.30           C  
-ATOM  18645  NH1 ARG E 420      -0.565 -78.896 -16.382  1.00 46.40           N  
-ATOM  18646  NH2 ARG E 420      -0.714 -80.690 -14.958  1.00 38.17           N  
-ATOM  18647  N   GLU E 421       1.800 -86.292 -14.207  1.00 41.60           N  
-ATOM  18648  CA  GLU E 421       1.965 -87.728 -14.376  1.00 39.45           C  
-ATOM  18649  C   GLU E 421       2.632 -87.985 -15.725  1.00 41.38           C  
-ATOM  18650  O   GLU E 421       2.474 -87.195 -16.655  1.00 48.10           O  
-ATOM  18651  CB  GLU E 421       0.612 -88.434 -14.278  1.00 44.35           C  
-ATOM  18652  CG  GLU E 421       0.678 -89.950 -14.189  1.00 52.18           C  
-ATOM  18653  CD  GLU E 421      -0.663 -90.559 -13.823  1.00 59.30           C  
-ATOM  18654  OE1 GLU E 421      -1.259 -90.124 -12.813  1.00 48.53           O  
-ATOM  18655  OE2 GLU E 421      -1.127 -91.464 -14.549  1.00 57.58           O  
-ATOM  18656  N   VAL E 422       3.388 -89.073 -15.832  1.00 44.91           N  
-ATOM  18657  CA  VAL E 422       4.098 -89.377 -17.074  1.00 45.82           C  
-ATOM  18658  C   VAL E 422       3.121 -89.685 -18.205  1.00 40.45           C  
-ATOM  18659  O   VAL E 422       2.376 -90.663 -18.149  1.00 42.94           O  
-ATOM  18660  CB  VAL E 422       5.064 -90.565 -16.905  1.00 39.07           C  
-ATOM  18661  CG1 VAL E 422       5.700 -90.919 -18.238  1.00 31.49           C  
-ATOM  18662  CG2 VAL E 422       6.135 -90.238 -15.874  1.00 44.93           C  
-ATOM  18663  N   GLY E 423       3.128 -88.837 -19.230  1.00 40.96           N  
-ATOM  18664  CA  GLY E 423       2.236 -88.996 -20.365  1.00 42.47           C  
-ATOM  18665  C   GLY E 423       1.268 -87.837 -20.507  1.00 42.05           C  
-ATOM  18666  O   GLY E 423       0.577 -87.710 -21.520  1.00 38.19           O  
-ATOM  18667  N   ASP E 424       1.222 -86.987 -19.485  1.00 39.44           N  
-ATOM  18668  CA  ASP E 424       0.315 -85.846 -19.466  1.00 28.83           C  
-ATOM  18669  C   ASP E 424       0.929 -84.650 -20.186  1.00 33.06           C  
-ATOM  18670  O   ASP E 424       1.826 -83.988 -19.665  1.00 45.60           O  
-ATOM  18671  CB  ASP E 424      -0.041 -85.477 -18.024  1.00 30.10           C  
-ATOM  18672  CG  ASP E 424      -1.310 -84.653 -17.925  1.00 38.52           C  
-ATOM  18673  OD1 ASP E 424      -1.607 -83.888 -18.868  1.00 34.57           O  
-ATOM  18674  OD2 ASP E 424      -2.014 -84.772 -16.900  1.00 37.56           O  
-ATOM  18675  N   ILE E 425       0.429 -84.372 -21.384  1.00 28.03           N  
-ATOM  18676  CA  ILE E 425       0.951 -83.287 -22.203  1.00 24.86           C  
-ATOM  18677  C   ILE E 425       0.480 -81.927 -21.704  1.00 29.71           C  
-ATOM  18678  O   ILE E 425       0.916 -80.889 -22.201  1.00 34.32           O  
-ATOM  18679  CB  ILE E 425       0.528 -83.448 -23.668  1.00 25.39           C  
-ATOM  18680  CG1 ILE E 425      -0.960 -83.129 -23.824  1.00 24.94           C  
-ATOM  18681  CG2 ILE E 425       0.820 -84.858 -24.147  1.00 30.22           C  
-ATOM  18682  CD1 ILE E 425      -1.394 -82.925 -25.256  1.00 26.97           C  
-ATOM  18683  N   GLY E 426      -0.413 -81.939 -20.719  1.00 28.89           N  
-ATOM  18684  CA  GLY E 426      -1.011 -80.717 -20.220  1.00 30.04           C  
-ATOM  18685  C   GLY E 426      -2.141 -80.253 -21.120  1.00 30.61           C  
-ATOM  18686  O   GLY E 426      -2.617 -81.012 -21.963  1.00 32.39           O  
-ATOM  18687  N   PRO E 427      -2.574 -78.997 -20.952  1.00 27.35           N  
-ATOM  18688  CA  PRO E 427      -3.683 -78.436 -21.729  1.00 26.87           C  
-ATOM  18689  C   PRO E 427      -3.278 -78.025 -23.145  1.00 35.23           C  
-ATOM  18690  O   PRO E 427      -3.309 -76.837 -23.467  1.00 36.68           O  
-ATOM  18691  CB  PRO E 427      -4.090 -77.214 -20.906  1.00 24.82           C  
-ATOM  18692  CG  PRO E 427      -2.829 -76.780 -20.254  1.00 30.17           C  
-ATOM  18693  CD  PRO E 427      -2.056 -78.039 -19.959  1.00 32.05           C  
-ATOM  18694  N   GLY E 428      -2.922 -78.994 -23.983  1.00 33.51           N  
-ATOM  18695  CA  GLY E 428      -2.464 -78.698 -25.329  1.00 34.39           C  
-ATOM  18696  C   GLY E 428      -3.335 -79.233 -26.453  1.00 39.35           C  
-ATOM  18697  O   GLY E 428      -4.168 -80.118 -26.245  1.00 46.21           O  
-ATOM  18698  N   TYR E 429      -3.122 -78.677 -27.647  1.00 39.62           N  
-ATOM  18699  CA  TYR E 429      -3.823 -79.047 -28.882  1.00 26.84           C  
-ATOM  18700  C   TYR E 429      -5.301 -79.392 -28.697  1.00 27.58           C  
-ATOM  18701  O   TYR E 429      -6.155 -78.509 -28.689  1.00 30.14           O  
-ATOM  18702  CB  TYR E 429      -3.110 -80.218 -29.559  1.00 26.50           C  
-ATOM  18703  CG  TYR E 429      -1.742 -79.868 -30.101  1.00 29.74           C  
-ATOM  18704  CD1 TYR E 429      -1.581 -78.854 -31.037  1.00 24.14           C  
-ATOM  18705  CD2 TYR E 429      -0.614 -80.560 -29.685  1.00 37.45           C  
-ATOM  18706  CE1 TYR E 429      -0.330 -78.533 -31.535  1.00 21.27           C  
-ATOM  18707  CE2 TYR E 429       0.640 -80.250 -30.180  1.00 34.21           C  
-ATOM  18708  CZ  TYR E 429       0.777 -79.237 -31.104  1.00 29.41           C  
-ATOM  18709  OH  TYR E 429       2.028 -78.932 -31.593  1.00 37.31           O  
-ATOM  18710  N   GLY E 430      -5.594 -80.681 -28.553  1.00 27.70           N  
-ATOM  18711  CA  GLY E 430      -6.965 -81.145 -28.421  1.00 29.24           C  
-ATOM  18712  C   GLY E 430      -7.736 -80.498 -27.288  1.00 27.74           C  
-ATOM  18713  O   GLY E 430      -8.919 -80.165 -27.429  1.00 30.53           O  
-ATOM  18714  N   PHE E 431      -7.060 -80.317 -26.158  1.00 25.71           N  
-ATOM  18715  CA  PHE E 431      -7.689 -79.726 -24.989  1.00 32.01           C  
-ATOM  18716  C   PHE E 431      -8.149 -78.307 -25.262  1.00 29.17           C  
-ATOM  18717  O   PHE E 431      -9.195 -77.895 -24.770  1.00 26.22           O  
-ATOM  18718  CB  PHE E 431      -6.744 -79.729 -23.792  1.00 30.66           C  
-ATOM  18719  CG  PHE E 431      -7.370 -79.194 -22.532  1.00 27.10           C  
-ATOM  18720  CD1 PHE E 431      -8.146 -80.010 -21.727  1.00 26.13           C  
-ATOM  18721  CD2 PHE E 431      -7.189 -77.874 -22.159  1.00 21.64           C  
-ATOM  18722  CE1 PHE E 431      -8.721 -79.522 -20.570  1.00 29.33           C  
-ATOM  18723  CE2 PHE E 431      -7.760 -77.379 -21.004  1.00 21.93           C  
-ATOM  18724  CZ  PHE E 431      -8.529 -78.204 -20.208  1.00 23.73           C  
-ATOM  18725  N   GLN E 432      -7.363 -77.556 -26.026  1.00 34.21           N  
-ATOM  18726  CA  GLN E 432      -7.749 -76.198 -26.378  1.00 28.80           C  
-ATOM  18727  C   GLN E 432      -8.853 -76.249 -27.428  1.00 27.20           C  
-ATOM  18728  O   GLN E 432      -9.810 -75.479 -27.370  1.00 36.08           O  
-ATOM  18729  CB  GLN E 432      -6.538 -75.397 -26.872  1.00 31.29           C  
-ATOM  18730  CG  GLN E 432      -5.429 -75.246 -25.826  1.00 30.00           C  
-ATOM  18731  CD  GLN E 432      -5.902 -74.530 -24.564  1.00 35.57           C  
-ATOM  18732  OE1 GLN E 432      -6.785 -73.672 -24.614  1.00 36.86           O  
-ATOM  18733  NE2 GLN E 432      -5.312 -74.881 -23.427  1.00 39.37           N  
-ATOM  18734  N   TRP E 433      -8.714 -77.180 -28.370  1.00 28.94           N  
-ATOM  18735  CA  TRP E 433      -9.710 -77.414 -29.415  1.00 29.68           C  
-ATOM  18736  C   TRP E 433     -11.119 -77.586 -28.859  1.00 27.59           C  
-ATOM  18737  O   TRP E 433     -12.052 -76.912 -29.292  1.00 29.07           O  
-ATOM  18738  CB  TRP E 433      -9.356 -78.662 -30.235  1.00 24.59           C  
-ATOM  18739  CG  TRP E 433      -8.249 -78.494 -31.224  1.00 22.60           C  
-ATOM  18740  CD1 TRP E 433      -7.335 -77.485 -31.274  1.00 21.69           C  
-ATOM  18741  CD2 TRP E 433      -7.946 -79.366 -32.316  1.00 29.12           C  
-ATOM  18742  NE1 TRP E 433      -6.475 -77.677 -32.326  1.00 30.14           N  
-ATOM  18743  CE2 TRP E 433      -6.830 -78.826 -32.982  1.00 29.12           C  
-ATOM  18744  CE3 TRP E 433      -8.509 -80.553 -32.794  1.00 27.36           C  
-ATOM  18745  CZ2 TRP E 433      -6.267 -79.431 -34.102  1.00 25.44           C  
-ATOM  18746  CZ3 TRP E 433      -7.952 -81.150 -33.902  1.00 25.03           C  
-ATOM  18747  CH2 TRP E 433      -6.842 -80.591 -34.545  1.00 30.05           C  
-ATOM  18748  N   ARG E 434     -11.263 -78.490 -27.894  1.00 29.70           N  
-ATOM  18749  CA  ARG E 434     -12.582 -78.867 -27.401  1.00 27.79           C  
-ATOM  18750  C   ARG E 434     -12.972 -78.123 -26.123  1.00 32.81           C  
-ATOM  18751  O   ARG E 434     -14.149 -78.078 -25.753  1.00 27.21           O  
-ATOM  18752  CB  ARG E 434     -12.636 -80.381 -27.163  1.00 21.77           C  
-ATOM  18753  CG  ARG E 434     -12.110 -81.220 -28.323  1.00 25.80           C  
-ATOM  18754  CD  ARG E 434     -12.696 -80.768 -29.650  1.00 26.45           C  
-ATOM  18755  NE  ARG E 434     -14.154 -80.799 -29.634  1.00 26.89           N  
-ATOM  18756  CZ  ARG E 434     -14.881 -81.847 -30.002  1.00 25.95           C  
-ATOM  18757  NH1 ARG E 434     -16.203 -81.784 -29.955  1.00 22.90           N  
-ATOM  18758  NH2 ARG E 434     -14.286 -82.958 -30.421  1.00 28.85           N  
-ATOM  18759  N   HIS E 435     -11.983 -77.548 -25.448  1.00 23.52           N  
-ATOM  18760  CA  HIS E 435     -12.223 -76.914 -24.161  1.00 21.97           C  
-ATOM  18761  C   HIS E 435     -11.350 -75.691 -23.938  1.00 27.00           C  
-ATOM  18762  O   HIS E 435     -10.774 -75.549 -22.865  1.00 35.51           O  
-ATOM  18763  CB  HIS E 435     -11.967 -77.899 -23.019  1.00 24.02           C  
-ATOM  18764  CG  HIS E 435     -12.503 -79.274 -23.266  1.00 30.36           C  
-ATOM  18765  ND1 HIS E 435     -13.823 -79.608 -23.052  1.00 34.12           N  
-ATOM  18766  CD2 HIS E 435     -11.897 -80.399 -23.713  1.00 32.02           C  
-ATOM  18767  CE1 HIS E 435     -14.006 -80.881 -23.357  1.00 34.63           C  
-ATOM  18768  NE2 HIS E 435     -12.854 -81.384 -23.761  1.00 25.67           N  
-ATOM  18769  N   PHE E 436     -11.251 -74.810 -24.929  1.00 22.97           N  
-ATOM  18770  CA  PHE E 436     -10.386 -73.633 -24.809  1.00 29.98           C  
-ATOM  18771  C   PHE E 436     -10.666 -72.804 -23.551  1.00 30.41           C  
-ATOM  18772  O   PHE E 436     -11.785 -72.343 -23.330  1.00 29.37           O  
-ATOM  18773  CB  PHE E 436     -10.527 -72.733 -26.038  1.00 30.02           C  
-ATOM  18774  CG  PHE E 436      -9.547 -71.592 -26.067  1.00 27.09           C  
-ATOM  18775  CD1 PHE E 436      -8.292 -71.749 -26.636  1.00 28.91           C  
-ATOM  18776  CD2 PHE E 436      -9.877 -70.363 -25.519  1.00 23.84           C  
-ATOM  18777  CE1 PHE E 436      -7.388 -70.702 -26.658  1.00 26.98           C  
-ATOM  18778  CE2 PHE E 436      -8.976 -69.315 -25.535  1.00 28.67           C  
-ATOM  18779  CZ  PHE E 436      -7.731 -69.484 -26.109  1.00 29.03           C  
-ATOM  18780  N   GLY E 437      -9.636 -72.620 -22.731  1.00 26.87           N  
-ATOM  18781  CA  GLY E 437      -9.722 -71.751 -21.571  1.00 26.33           C  
-ATOM  18782  C   GLY E 437     -10.092 -72.444 -20.274  1.00 25.20           C  
-ATOM  18783  O   GLY E 437      -9.964 -71.861 -19.197  1.00 19.24           O  
-ATOM  18784  N   ALA E 438     -10.555 -73.685 -20.375  1.00 23.25           N  
-ATOM  18785  CA  ALA E 438     -10.940 -74.452 -19.197  1.00 23.51           C  
-ATOM  18786  C   ALA E 438      -9.747 -74.677 -18.268  1.00 31.73           C  
-ATOM  18787  O   ALA E 438      -8.613 -74.825 -18.726  1.00 27.48           O  
-ATOM  18788  CB  ALA E 438     -11.549 -75.780 -19.612  1.00 19.24           C  
-ATOM  18789  N   ALA E 439     -10.006 -74.688 -16.964  1.00 34.62           N  
-ATOM  18790  CA  ALA E 439      -8.956 -74.919 -15.978  1.00 30.14           C  
-ATOM  18791  C   ALA E 439      -8.516 -76.377 -16.003  1.00 29.60           C  
-ATOM  18792  O   ALA E 439      -9.324 -77.281 -15.790  1.00 29.72           O  
-ATOM  18793  CB  ALA E 439      -9.432 -74.529 -14.586  1.00 41.38           C  
-ATOM  18794  N   TYR E 440      -7.232 -76.600 -16.263  1.00 32.61           N  
-ATOM  18795  CA  TYR E 440      -6.697 -77.950 -16.396  1.00 30.57           C  
-ATOM  18796  C   TYR E 440      -6.300 -78.545 -15.047  1.00 32.49           C  
-ATOM  18797  O   TYR E 440      -5.811 -77.841 -14.165  1.00 37.10           O  
-ATOM  18798  CB  TYR E 440      -5.491 -77.948 -17.339  1.00 29.46           C  
-ATOM  18799  CG  TYR E 440      -5.038 -79.326 -17.775  1.00 35.26           C  
-ATOM  18800  CD1 TYR E 440      -5.635 -79.964 -18.855  1.00 34.12           C  
-ATOM  18801  CD2 TYR E 440      -4.009 -79.986 -17.113  1.00 33.71           C  
-ATOM  18802  CE1 TYR E 440      -5.225 -81.221 -19.260  1.00 31.86           C  
-ATOM  18803  CE2 TYR E 440      -3.593 -81.244 -17.511  1.00 30.79           C  
-ATOM  18804  CZ  TYR E 440      -4.204 -81.855 -18.585  1.00 31.92           C  
-ATOM  18805  OH  TYR E 440      -3.792 -83.105 -18.983  1.00 33.27           O  
-ATOM  18806  N   LYS E 441      -6.519 -79.847 -14.894  1.00 32.44           N  
-ATOM  18807  CA  LYS E 441      -6.064 -80.573 -13.713  1.00 37.74           C  
-ATOM  18808  C   LYS E 441      -5.085 -81.669 -14.123  1.00 38.26           C  
-ATOM  18809  O   LYS E 441      -3.871 -81.500 -14.022  1.00 35.13           O  
-ATOM  18810  CB  LYS E 441      -7.245 -81.174 -12.946  1.00 46.46           C  
-ATOM  18811  CG  LYS E 441      -8.050 -80.173 -12.128  1.00 51.43           C  
-ATOM  18812  CD  LYS E 441      -9.119 -79.484 -12.961  1.00 57.93           C  
-ATOM  18813  CE  LYS E 441      -9.971 -78.557 -12.104  1.00 67.33           C  
-ATOM  18814  NZ  LYS E 441     -10.640 -79.290 -10.992  1.00 58.05           N  
-ATOM  18815  N   ASP E 442      -5.620 -82.796 -14.583  1.00 37.15           N  
-ATOM  18816  CA  ASP E 442      -4.791 -83.851 -15.151  1.00 33.27           C  
-ATOM  18817  C   ASP E 442      -5.469 -84.472 -16.367  1.00 36.14           C  
-ATOM  18818  O   ASP E 442      -6.562 -84.064 -16.760  1.00 33.85           O  
-ATOM  18819  CB  ASP E 442      -4.466 -84.930 -14.108  1.00 35.87           C  
-ATOM  18820  CG  ASP E 442      -5.706 -85.527 -13.453  1.00 40.32           C  
-ATOM  18821  OD1 ASP E 442      -6.796 -85.518 -14.065  1.00 37.05           O  
-ATOM  18822  OD2 ASP E 442      -5.581 -86.022 -12.312  1.00 43.50           O  
-ATOM  18823  N   MET E 443      -4.817 -85.470 -16.952  1.00 33.47           N  
-ATOM  18824  CA  MET E 443      -5.315 -86.117 -18.158  1.00 26.19           C  
-ATOM  18825  C   MET E 443      -6.475 -87.068 -17.881  1.00 30.72           C  
-ATOM  18826  O   MET E 443      -7.057 -87.626 -18.810  1.00 36.72           O  
-ATOM  18827  CB  MET E 443      -4.181 -86.874 -18.843  1.00 29.14           C  
-ATOM  18828  CG  MET E 443      -3.530 -87.920 -17.962  1.00 26.68           C  
-ATOM  18829  SD  MET E 443      -1.976 -88.508 -18.650  1.00 36.60           S  
-ATOM  18830  CE  MET E 443      -1.437 -89.622 -17.358  1.00 43.72           C  
-ATOM  18831  N   HIS E 444      -6.807 -87.252 -16.607  1.00 41.73           N  
-ATOM  18832  CA  HIS E 444      -7.869 -88.177 -16.224  1.00 39.46           C  
-ATOM  18833  C   HIS E 444      -9.181 -87.451 -15.950  1.00 34.49           C  
-ATOM  18834  O   HIS E 444     -10.210 -88.082 -15.710  1.00 32.52           O  
-ATOM  18835  CB  HIS E 444      -7.457 -88.984 -14.991  1.00 31.91           C  
-ATOM  18836  CG  HIS E 444      -6.125 -89.654 -15.124  1.00 35.98           C  
-ATOM  18837  ND1 HIS E 444      -5.833 -90.535 -16.142  1.00 41.89           N  
-ATOM  18838  CD2 HIS E 444      -5.007 -89.575 -14.363  1.00 47.27           C  
-ATOM  18839  CE1 HIS E 444      -4.593 -90.968 -16.006  1.00 51.35           C  
-ATOM  18840  NE2 HIS E 444      -4.070 -90.401 -14.933  1.00 44.96           N  
-ATOM  18841  N   THR E 445      -9.141 -86.123 -15.996  1.00 35.27           N  
-ATOM  18842  CA  THR E 445     -10.294 -85.309 -15.627  1.00 37.85           C  
-ATOM  18843  C   THR E 445     -11.305 -85.186 -16.766  1.00 43.26           C  
-ATOM  18844  O   THR E 445     -10.927 -85.059 -17.931  1.00 45.95           O  
-ATOM  18845  CB  THR E 445      -9.857 -83.897 -15.196  1.00 39.96           C  
-ATOM  18846  OG1 THR E 445      -8.672 -83.984 -14.395  1.00 40.50           O  
-ATOM  18847  CG2 THR E 445     -10.960 -83.211 -14.402  1.00 40.98           C  
-ATOM  18848  N   ASP E 446     -12.590 -85.228 -16.423  1.00 43.28           N  
-ATOM  18849  CA  ASP E 446     -13.652 -85.037 -17.407  1.00 44.75           C  
-ATOM  18850  C   ASP E 446     -13.936 -83.547 -17.557  1.00 44.58           C  
-ATOM  18851  O   ASP E 446     -14.199 -82.856 -16.572  1.00 49.09           O  
-ATOM  18852  CB  ASP E 446     -14.921 -85.792 -16.997  1.00 46.93           C  
-ATOM  18853  CG  ASP E 446     -15.862 -86.041 -18.168  1.00 46.19           C  
-ATOM  18854  OD1 ASP E 446     -15.863 -85.235 -19.123  1.00 45.43           O  
-ATOM  18855  OD2 ASP E 446     -16.603 -87.048 -18.132  1.00 41.25           O  
-ATOM  18856  N   TYR E 447     -13.881 -83.057 -18.790  1.00 38.46           N  
-ATOM  18857  CA  TYR E 447     -13.999 -81.626 -19.044  1.00 40.76           C  
-ATOM  18858  C   TYR E 447     -15.223 -81.257 -19.869  1.00 39.28           C  
-ATOM  18859  O   TYR E 447     -15.306 -80.141 -20.382  1.00 35.23           O  
-ATOM  18860  CB  TYR E 447     -12.753 -81.111 -19.763  1.00 33.17           C  
-ATOM  18861  CG  TYR E 447     -11.473 -81.247 -18.979  1.00 31.54           C  
-ATOM  18862  CD1 TYR E 447     -11.176 -80.373 -17.944  1.00 29.20           C  
-ATOM  18863  CD2 TYR E 447     -10.549 -82.237 -19.287  1.00 42.38           C  
-ATOM  18864  CE1 TYR E 447     -10.001 -80.488 -17.229  1.00 37.63           C  
-ATOM  18865  CE2 TYR E 447      -9.370 -82.358 -18.577  1.00 41.75           C  
-ATOM  18866  CZ  TYR E 447      -9.101 -81.481 -17.551  1.00 34.04           C  
-ATOM  18867  OH  TYR E 447      -7.930 -81.599 -16.840  1.00 37.92           O  
-ATOM  18868  N   THR E 448     -16.164 -82.185 -20.006  1.00 44.11           N  
-ATOM  18869  CA  THR E 448     -17.308 -81.956 -20.882  1.00 45.99           C  
-ATOM  18870  C   THR E 448     -18.133 -80.763 -20.388  1.00 39.71           C  
-ATOM  18871  O   THR E 448     -18.532 -80.697 -19.223  1.00 31.08           O  
-ATOM  18872  CB  THR E 448     -18.194 -83.230 -21.016  1.00 35.08           C  
-ATOM  18873  OG1 THR E 448     -19.245 -82.991 -21.960  1.00 46.62           O  
-ATOM  18874  CG2 THR E 448     -18.787 -83.656 -19.673  1.00 39.39           C  
-ATOM  18875  N   GLY E 449     -18.340 -79.797 -21.278  1.00 35.35           N  
-ATOM  18876  CA  GLY E 449     -19.083 -78.596 -20.942  1.00 29.63           C  
-ATOM  18877  C   GLY E 449     -18.217 -77.462 -20.423  1.00 32.55           C  
-ATOM  18878  O   GLY E 449     -18.719 -76.389 -20.086  1.00 35.34           O  
-ATOM  18879  N   GLN E 450     -16.911 -77.697 -20.353  1.00 40.08           N  
-ATOM  18880  CA  GLN E 450     -15.979 -76.667 -19.907  1.00 37.61           C  
-ATOM  18881  C   GLN E 450     -15.233 -76.053 -21.088  1.00 32.33           C  
-ATOM  18882  O   GLN E 450     -14.808 -76.763 -22.001  1.00 36.40           O  
-ATOM  18883  CB  GLN E 450     -14.979 -77.240 -18.903  1.00 34.38           C  
-ATOM  18884  CG  GLN E 450     -15.596 -77.776 -17.622  1.00 27.63           C  
-ATOM  18885  CD  GLN E 450     -14.552 -78.340 -16.673  1.00 35.61           C  
-ATOM  18886  OE1 GLN E 450     -14.699 -79.447 -16.160  1.00 42.75           O  
-ATOM  18887  NE2 GLN E 450     -13.490 -77.577 -16.436  1.00 34.09           N  
-ATOM  18888  N   GLY E 451     -15.079 -74.732 -21.068  1.00 22.56           N  
-ATOM  18889  CA  GLY E 451     -14.336 -74.032 -22.100  1.00 22.51           C  
-ATOM  18890  C   GLY E 451     -15.053 -73.976 -23.435  1.00 24.00           C  
-ATOM  18891  O   GLY E 451     -16.195 -74.420 -23.557  1.00 30.47           O  
-ATOM  18892  N   VAL E 452     -14.372 -73.435 -24.442  1.00 21.31           N  
-ATOM  18893  CA  VAL E 452     -14.958 -73.264 -25.770  1.00 23.89           C  
-ATOM  18894  C   VAL E 452     -14.663 -74.451 -26.690  1.00 33.00           C  
-ATOM  18895  O   VAL E 452     -13.509 -74.854 -26.845  1.00 32.15           O  
-ATOM  18896  CB  VAL E 452     -14.444 -71.977 -26.442  1.00 20.80           C  
-ATOM  18897  CG1 VAL E 452     -15.061 -71.811 -27.820  1.00 20.75           C  
-ATOM  18898  CG2 VAL E 452     -14.742 -70.766 -25.568  1.00 22.60           C  
-ATOM  18899  N   ASP E 453     -15.712 -75.004 -27.297  1.00 31.24           N  
-ATOM  18900  CA  ASP E 453     -15.566 -76.099 -28.255  1.00 20.72           C  
-ATOM  18901  C   ASP E 453     -15.397 -75.549 -29.668  1.00 25.18           C  
-ATOM  18902  O   ASP E 453     -16.342 -75.523 -30.466  1.00 30.09           O  
-ATOM  18903  CB  ASP E 453     -16.769 -77.043 -28.187  1.00 30.81           C  
-ATOM  18904  CG  ASP E 453     -16.518 -78.369 -28.888  1.00 32.75           C  
-ATOM  18905  OD1 ASP E 453     -15.859 -78.386 -29.951  1.00 30.54           O  
-ATOM  18906  OD2 ASP E 453     -16.989 -79.404 -28.371  1.00 29.66           O  
-ATOM  18907  N   GLN E 454     -14.175 -75.124 -29.967  1.00 21.98           N  
-ATOM  18908  CA  GLN E 454     -13.855 -74.503 -31.241  1.00 18.89           C  
-ATOM  18909  C   GLN E 454     -14.200 -75.389 -32.430  1.00 22.49           C  
-ATOM  18910  O   GLN E 454     -14.607 -74.889 -33.474  1.00 29.40           O  
-ATOM  18911  CB  GLN E 454     -12.373 -74.138 -31.293  1.00 23.52           C  
-ATOM  18912  CG  GLN E 454     -11.944 -73.121 -30.251  1.00 24.22           C  
-ATOM  18913  CD  GLN E 454     -10.537 -72.614 -30.487  1.00 25.20           C  
-ATOM  18914  OE1 GLN E 454     -10.317 -71.705 -31.292  1.00 22.23           O  
-ATOM  18915  NE2 GLN E 454      -9.573 -73.202 -29.788  1.00 23.30           N  
-ATOM  18916  N   LEU E 455     -14.038 -76.699 -32.275  1.00 21.76           N  
-ATOM  18917  CA  LEU E 455     -14.305 -77.622 -33.372  1.00 27.53           C  
-ATOM  18918  C   LEU E 455     -15.793 -77.644 -33.717  1.00 30.97           C  
-ATOM  18919  O   LEU E 455     -16.172 -77.529 -34.888  1.00 26.23           O  
-ATOM  18920  CB  LEU E 455     -13.812 -79.028 -33.023  1.00 24.19           C  
-ATOM  18921  CG  LEU E 455     -13.726 -80.008 -34.195  1.00 22.68           C  
-ATOM  18922  CD1 LEU E 455     -12.921 -79.403 -35.333  1.00 13.91           C  
-ATOM  18923  CD2 LEU E 455     -13.116 -81.331 -33.755  1.00 16.37           C  
-ATOM  18924  N   LYS E 456     -16.631 -77.780 -32.694  1.00 26.26           N  
-ATOM  18925  CA  LYS E 456     -18.075 -77.800 -32.891  1.00 28.46           C  
-ATOM  18926  C   LYS E 456     -18.558 -76.458 -33.419  1.00 34.03           C  
-ATOM  18927  O   LYS E 456     -19.429 -76.399 -34.288  1.00 36.29           O  
-ATOM  18928  CB  LYS E 456     -18.798 -78.156 -31.589  1.00 30.95           C  
-ATOM  18929  CG  LYS E 456     -20.208 -78.691 -31.794  1.00 41.80           C  
-ATOM  18930  CD  LYS E 456     -20.808 -79.155 -30.477  1.00 43.77           C  
-ATOM  18931  CE  LYS E 456     -21.003 -77.989 -29.523  1.00 56.58           C  
-ATOM  18932  NZ  LYS E 456     -20.871 -78.419 -28.100  1.00 48.82           N  
-ATOM  18933  N   ASN E 457     -17.983 -75.381 -32.890  1.00 35.64           N  
-ATOM  18934  CA  ASN E 457     -18.276 -74.040 -33.394  1.00 36.39           C  
-ATOM  18935  C   ASN E 457     -18.006 -73.934 -34.892  1.00 29.85           C  
-ATOM  18936  O   ASN E 457     -18.881 -73.545 -35.669  1.00 32.71           O  
-ATOM  18937  CB  ASN E 457     -17.457 -72.984 -32.640  1.00 30.48           C  
-ATOM  18938  CG  ASN E 457     -17.981 -72.725 -31.239  1.00 33.85           C  
-ATOM  18939  OD1 ASN E 457     -18.808 -73.478 -30.718  1.00 34.33           O  
-ATOM  18940  ND2 ASN E 457     -17.496 -71.657 -30.619  1.00 32.11           N  
-ATOM  18941  N   VAL E 458     -16.785 -74.289 -35.280  1.00 22.76           N  
-ATOM  18942  CA  VAL E 458     -16.364 -74.274 -36.676  1.00 26.98           C  
-ATOM  18943  C   VAL E 458     -17.289 -75.104 -37.555  1.00 24.84           C  
-ATOM  18944  O   VAL E 458     -17.701 -74.667 -38.630  1.00 27.16           O  
-ATOM  18945  CB  VAL E 458     -14.923 -74.801 -36.829  1.00 21.50           C  
-ATOM  18946  CG1 VAL E 458     -14.647 -75.196 -38.268  1.00 17.40           C  
-ATOM  18947  CG2 VAL E 458     -13.921 -73.759 -36.355  1.00 19.19           C  
-ATOM  18948  N   ILE E 459     -17.625 -76.301 -37.089  1.00 24.81           N  
-ATOM  18949  CA  ILE E 459     -18.465 -77.196 -37.873  1.00 29.31           C  
-ATOM  18950  C   ILE E 459     -19.872 -76.644 -38.072  1.00 30.24           C  
-ATOM  18951  O   ILE E 459     -20.354 -76.579 -39.202  1.00 26.90           O  
-ATOM  18952  CB  ILE E 459     -18.546 -78.589 -37.229  1.00 26.54           C  
-ATOM  18953  CG1 ILE E 459     -17.192 -79.288 -37.346  1.00 18.96           C  
-ATOM  18954  CG2 ILE E 459     -19.622 -79.423 -37.900  1.00 21.02           C  
-ATOM  18955  CD1 ILE E 459     -17.192 -80.682 -36.807  1.00 30.98           C  
-ATOM  18956  N   GLN E 460     -20.526 -76.239 -36.987  1.00 32.56           N  
-ATOM  18957  CA  GLN E 460     -21.879 -75.699 -37.096  1.00 36.34           C  
-ATOM  18958  C   GLN E 460     -21.905 -74.434 -37.951  1.00 28.49           C  
-ATOM  18959  O   GLN E 460     -22.808 -74.244 -38.772  1.00 21.19           O  
-ATOM  18960  CB  GLN E 460     -22.463 -75.427 -35.708  1.00 36.64           C  
-ATOM  18961  CG  GLN E 460     -22.995 -76.675 -35.026  1.00 42.19           C  
-ATOM  18962  CD  GLN E 460     -23.545 -76.397 -33.640  1.00 74.84           C  
-ATOM  18963  OE1 GLN E 460     -23.945 -75.273 -33.329  1.00 88.22           O  
-ATOM  18964  NE2 GLN E 460     -23.564 -77.421 -32.796  1.00 68.07           N  
-ATOM  18965  N   MET E 461     -20.898 -73.586 -37.768  1.00 27.48           N  
-ATOM  18966  CA  MET E 461     -20.760 -72.386 -38.583  1.00 26.01           C  
-ATOM  18967  C   MET E 461     -20.614 -72.755 -40.055  1.00 24.74           C  
-ATOM  18968  O   MET E 461     -21.125 -72.059 -40.928  1.00 28.85           O  
-ATOM  18969  CB  MET E 461     -19.562 -71.548 -38.125  1.00 29.39           C  
-ATOM  18970  CG  MET E 461     -19.471 -70.173 -38.784  1.00 39.93           C  
-ATOM  18971  SD  MET E 461     -20.886 -69.112 -38.416  1.00 52.84           S  
-ATOM  18972  CE  MET E 461     -20.756 -68.971 -36.633  1.00 41.29           C  
-ATOM  18973  N   LEU E 462     -19.918 -73.854 -40.324  1.00 30.78           N  
-ATOM  18974  CA  LEU E 462     -19.755 -74.335 -41.693  1.00 25.01           C  
-ATOM  18975  C   LEU E 462     -21.074 -74.836 -42.273  1.00 29.10           C  
-ATOM  18976  O   LEU E 462     -21.375 -74.611 -43.444  1.00 30.03           O  
-ATOM  18977  CB  LEU E 462     -18.706 -75.448 -41.749  1.00 18.57           C  
-ATOM  18978  CG  LEU E 462     -17.236 -75.030 -41.805  1.00 16.09           C  
-ATOM  18979  CD1 LEU E 462     -16.346 -76.167 -41.355  1.00 19.06           C  
-ATOM  18980  CD2 LEU E 462     -16.864 -74.599 -43.205  1.00 14.53           C  
-ATOM  18981  N   ARG E 463     -21.859 -75.514 -41.444  1.00 34.20           N  
-ATOM  18982  CA  ARG E 463     -23.106 -76.120 -41.897  1.00 28.01           C  
-ATOM  18983  C   ARG E 463     -24.236 -75.106 -42.059  1.00 27.48           C  
-ATOM  18984  O   ARG E 463     -25.174 -75.336 -42.824  1.00 20.54           O  
-ATOM  18985  CB  ARG E 463     -23.536 -77.223 -40.928  1.00 24.34           C  
-ATOM  18986  CG  ARG E 463     -22.486 -78.307 -40.742  1.00 32.58           C  
-ATOM  18987  CD  ARG E 463     -23.106 -79.660 -40.446  1.00 27.96           C  
-ATOM  18988  NE  ARG E 463     -23.355 -79.873 -39.024  1.00 19.81           N  
-ATOM  18989  CZ  ARG E 463     -23.043 -80.993 -38.382  1.00 16.14           C  
-ATOM  18990  NH1 ARG E 463     -22.470 -81.990 -39.039  1.00 12.57           N  
-ATOM  18991  NH2 ARG E 463     -23.303 -81.121 -37.089  1.00 20.07           N  
-ATOM  18992  N   THR E 464     -24.145 -73.984 -41.351  1.00 32.42           N  
-ATOM  18993  CA  THR E 464     -25.250 -73.031 -41.328  1.00 24.57           C  
-ATOM  18994  C   THR E 464     -24.927 -71.665 -41.933  1.00 25.60           C  
-ATOM  18995  O   THR E 464     -25.830 -70.866 -42.169  1.00 28.19           O  
-ATOM  18996  CB  THR E 464     -25.744 -72.811 -39.889  1.00 27.33           C  
-ATOM  18997  OG1 THR E 464     -24.791 -72.023 -39.165  1.00 34.75           O  
-ATOM  18998  CG2 THR E 464     -25.937 -74.148 -39.187  1.00 27.53           C  
-ATOM  18999  N   ASN E 465     -23.650 -71.395 -42.184  1.00 28.50           N  
-ATOM  19000  CA  ASN E 465     -23.241 -70.073 -42.652  1.00 26.65           C  
-ATOM  19001  C   ASN E 465     -21.840 -70.081 -43.260  1.00 29.45           C  
-ATOM  19002  O   ASN E 465     -20.925 -69.470 -42.712  1.00 34.91           O  
-ATOM  19003  CB  ASN E 465     -23.300 -69.076 -41.490  1.00 32.62           C  
-ATOM  19004  CG  ASN E 465     -23.366 -67.635 -41.953  1.00 43.00           C  
-ATOM  19005  OD1 ASN E 465     -23.002 -67.315 -43.084  1.00 41.24           O  
-ATOM  19006  ND2 ASN E 465     -23.832 -66.753 -41.073  1.00 38.47           N  
-ATOM  19007  N   PRO E 466     -21.675 -70.752 -44.411  1.00 30.49           N  
-ATOM  19008  CA  PRO E 466     -20.347 -71.009 -44.987  1.00 28.08           C  
-ATOM  19009  C   PRO E 466     -19.583 -69.767 -45.463  1.00 28.88           C  
-ATOM  19010  O   PRO E 466     -18.429 -69.897 -45.867  1.00 38.07           O  
-ATOM  19011  CB  PRO E 466     -20.660 -71.925 -46.175  1.00 33.05           C  
-ATOM  19012  CG  PRO E 466     -22.048 -71.565 -46.566  1.00 42.50           C  
-ATOM  19013  CD  PRO E 466     -22.756 -71.254 -45.277  1.00 38.45           C  
-ATOM  19014  N   THR E 467     -20.201 -68.592 -45.414  1.00 31.52           N  
-ATOM  19015  CA  THR E 467     -19.538 -67.374 -45.870  1.00 30.18           C  
-ATOM  19016  C   THR E 467     -18.994 -66.565 -44.695  1.00 27.49           C  
-ATOM  19017  O   THR E 467     -18.471 -65.463 -44.871  1.00 27.97           O  
-ATOM  19018  CB  THR E 467     -20.486 -66.491 -46.701  1.00 33.68           C  
-ATOM  19019  OG1 THR E 467     -21.690 -66.248 -45.962  1.00 38.23           O  
-ATOM  19020  CG2 THR E 467     -20.835 -67.178 -48.010  1.00 27.36           C  
-ATOM  19021  N   ASP E 468     -19.120 -67.121 -43.496  1.00 24.91           N  
-ATOM  19022  CA  ASP E 468     -18.586 -66.482 -42.301  1.00 29.82           C  
-ATOM  19023  C   ASP E 468     -17.064 -66.479 -42.361  1.00 28.50           C  
-ATOM  19024  O   ASP E 468     -16.456 -67.425 -42.860  1.00 35.59           O  
-ATOM  19025  CB  ASP E 468     -19.082 -67.197 -41.043  1.00 31.46           C  
-ATOM  19026  CG  ASP E 468     -18.550 -66.576 -39.768  1.00 30.26           C  
-ATOM  19027  OD1 ASP E 468     -19.028 -65.485 -39.391  1.00 32.69           O  
-ATOM  19028  OD2 ASP E 468     -17.661 -67.183 -39.136  1.00 31.80           O  
-ATOM  19029  N   ARG E 469     -16.446 -65.411 -41.866  1.00 32.70           N  
-ATOM  19030  CA  ARG E 469     -14.991 -65.296 -41.920  1.00 33.06           C  
-ATOM  19031  C   ARG E 469     -14.352 -65.387 -40.537  1.00 26.04           C  
-ATOM  19032  O   ARG E 469     -13.297 -64.802 -40.300  1.00 27.14           O  
-ATOM  19033  CB  ARG E 469     -14.578 -63.984 -42.593  1.00 24.80           C  
-ATOM  19034  CG  ARG E 469     -15.209 -63.745 -43.955  1.00 26.22           C  
-ATOM  19035  CD  ARG E 469     -14.521 -62.592 -44.667  1.00 27.41           C  
-ATOM  19036  NE  ARG E 469     -15.455 -61.703 -45.354  1.00 37.32           N  
-ATOM  19037  CZ  ARG E 469     -16.088 -60.691 -44.766  1.00 38.33           C  
-ATOM  19038  NH1 ARG E 469     -15.893 -60.448 -43.479  1.00 28.22           N  
-ATOM  19039  NH2 ARG E 469     -16.918 -59.925 -45.460  1.00 37.11           N  
-ATOM  19040  N   ARG E 470     -14.991 -66.117 -39.630  1.00 25.62           N  
-ATOM  19041  CA  ARG E 470     -14.454 -66.304 -38.285  1.00 23.82           C  
-ATOM  19042  C   ARG E 470     -14.383 -67.782 -37.921  1.00 24.08           C  
-ATOM  19043  O   ARG E 470     -14.436 -68.144 -36.745  1.00 20.38           O  
-ATOM  19044  CB  ARG E 470     -15.297 -65.561 -37.245  1.00 23.19           C  
-ATOM  19045  CG  ARG E 470     -15.263 -64.046 -37.349  1.00 18.97           C  
-ATOM  19046  CD  ARG E 470     -16.311 -63.530 -38.317  1.00 28.93           C  
-ATOM  19047  NE  ARG E 470     -16.620 -62.125 -38.078  1.00 33.28           N  
-ATOM  19048  CZ  ARG E 470     -17.592 -61.705 -37.275  1.00 36.40           C  
-ATOM  19049  NH1 ARG E 470     -18.353 -62.583 -36.634  1.00 31.54           N  
-ATOM  19050  NH2 ARG E 470     -17.805 -60.406 -37.114  1.00 33.85           N  
-ATOM  19051  N   MET E 471     -14.267 -68.633 -38.934  1.00 29.11           N  
-ATOM  19052  CA  MET E 471     -14.182 -70.071 -38.715  1.00 30.82           C  
-ATOM  19053  C   MET E 471     -12.751 -70.492 -38.402  1.00 27.91           C  
-ATOM  19054  O   MET E 471     -12.032 -70.986 -39.273  1.00 27.99           O  
-ATOM  19055  CB  MET E 471     -14.690 -70.830 -39.938  1.00 23.23           C  
-ATOM  19056  CG  MET E 471     -15.982 -70.286 -40.505  1.00 24.24           C  
-ATOM  19057  SD  MET E 471     -16.606 -71.331 -41.828  1.00 32.88           S  
-ATOM  19058  CE  MET E 471     -17.862 -70.275 -42.526  1.00 33.04           C  
-ATOM  19059  N   LEU E 472     -12.340 -70.298 -37.155  1.00 17.11           N  
-ATOM  19060  CA  LEU E 472     -10.972 -70.602 -36.772  1.00 18.07           C  
-ATOM  19061  C   LEU E 472     -10.881 -71.496 -35.545  1.00 25.11           C  
-ATOM  19062  O   LEU E 472     -11.756 -71.496 -34.679  1.00 23.43           O  
-ATOM  19063  CB  LEU E 472     -10.190 -69.313 -36.521  1.00 18.44           C  
-ATOM  19064  CG  LEU E 472      -9.743 -68.559 -37.772  1.00 17.98           C  
-ATOM  19065  CD1 LEU E 472     -10.787 -67.541 -38.216  1.00 26.70           C  
-ATOM  19066  CD2 LEU E 472      -8.397 -67.900 -37.537  1.00 20.35           C  
-ATOM  19067  N   MET E 473      -9.799 -72.260 -35.493  1.00 25.27           N  
-ATOM  19068  CA  MET E 473      -9.487 -73.100 -34.356  1.00 22.74           C  
-ATOM  19069  C   MET E 473      -8.052 -72.805 -33.949  1.00 27.58           C  
-ATOM  19070  O   MET E 473      -7.126 -72.961 -34.751  1.00 31.26           O  
-ATOM  19071  CB  MET E 473      -9.682 -74.576 -34.707  1.00 17.88           C  
-ATOM  19072  CG  MET E 473      -9.834 -75.491 -33.511  1.00 21.82           C  
-ATOM  19073  SD  MET E 473     -10.568 -77.070 -33.978  1.00 37.73           S  
-ATOM  19074  CE  MET E 473      -9.357 -77.676 -35.153  1.00 22.29           C  
-ATOM  19075  N   THR E 474      -7.872 -72.348 -32.715  1.00 20.88           N  
-ATOM  19076  CA  THR E 474      -6.540 -72.021 -32.227  1.00 20.38           C  
-ATOM  19077  C   THR E 474      -6.214 -72.794 -30.957  1.00 22.89           C  
-ATOM  19078  O   THR E 474      -7.089 -73.054 -30.130  1.00 24.90           O  
-ATOM  19079  CB  THR E 474      -6.386 -70.512 -31.958  1.00 14.45           C  
-ATOM  19080  OG1 THR E 474      -5.067 -70.246 -31.463  1.00 13.68           O  
-ATOM  19081  CG2 THR E 474      -7.412 -70.036 -30.942  1.00 15.97           C  
-ATOM  19082  N   ALA E 475      -4.950 -73.173 -30.818  1.00 23.26           N  
-ATOM  19083  CA  ALA E 475      -4.489 -73.882 -29.634  1.00 21.14           C  
-ATOM  19084  C   ALA E 475      -3.437 -73.055 -28.919  1.00 19.92           C  
-ATOM  19085  O   ALA E 475      -2.873 -73.483 -27.914  1.00 27.54           O  
-ATOM  19086  CB  ALA E 475      -3.937 -75.247 -30.006  1.00 23.87           C  
-ATOM  19087  N   TRP E 476      -3.173 -71.865 -29.448  1.00 17.21           N  
-ATOM  19088  CA  TRP E 476      -2.206 -70.969 -28.837  1.00 20.05           C  
-ATOM  19089  C   TRP E 476      -2.882 -70.135 -27.757  1.00 23.92           C  
-ATOM  19090  O   TRP E 476      -3.472 -69.091 -28.035  1.00 31.80           O  
-ATOM  19091  CB  TRP E 476      -1.555 -70.067 -29.889  1.00 20.82           C  
-ATOM  19092  CG  TRP E 476      -0.380 -69.299 -29.363  1.00 23.09           C  
-ATOM  19093  CD1 TRP E 476      -0.367 -67.997 -28.956  1.00 24.80           C  
-ATOM  19094  CD2 TRP E 476       0.953 -69.791 -29.174  1.00 24.18           C  
-ATOM  19095  NE1 TRP E 476       0.892 -67.645 -28.530  1.00 29.81           N  
-ATOM  19096  CE2 TRP E 476       1.721 -68.731 -28.653  1.00 29.52           C  
-ATOM  19097  CE3 TRP E 476       1.572 -71.025 -29.396  1.00 19.75           C  
-ATOM  19098  CZ2 TRP E 476       3.074 -68.865 -28.353  1.00 28.28           C  
-ATOM  19099  CZ3 TRP E 476       2.915 -71.157 -29.095  1.00 20.94           C  
-ATOM  19100  CH2 TRP E 476       3.652 -70.084 -28.580  1.00 25.49           C  
-ATOM  19101  N   ASN E 477      -2.800 -70.618 -26.522  1.00 24.51           N  
-ATOM  19102  CA  ASN E 477      -3.382 -69.928 -25.381  1.00 25.54           C  
-ATOM  19103  C   ASN E 477      -2.294 -69.537 -24.386  1.00 26.79           C  
-ATOM  19104  O   ASN E 477      -1.908 -70.342 -23.540  1.00 30.74           O  
-ATOM  19105  CB  ASN E 477      -4.439 -70.810 -24.712  1.00 25.97           C  
-ATOM  19106  CG  ASN E 477      -5.010 -70.192 -23.451  1.00 30.85           C  
-ATOM  19107  OD1 ASN E 477      -4.945 -68.979 -23.254  1.00 27.39           O  
-ATOM  19108  ND2 ASN E 477      -5.575 -71.028 -22.587  1.00 33.25           N  
-ATOM  19109  N   PRO E 478      -1.799 -68.292 -24.491  1.00 22.00           N  
-ATOM  19110  CA  PRO E 478      -0.693 -67.744 -23.695  1.00 21.34           C  
-ATOM  19111  C   PRO E 478      -0.836 -67.948 -22.185  1.00 27.49           C  
-ATOM  19112  O   PRO E 478       0.163 -67.894 -21.467  1.00 32.11           O  
-ATOM  19113  CB  PRO E 478      -0.732 -66.254 -24.041  1.00 17.44           C  
-ATOM  19114  CG  PRO E 478      -1.274 -66.216 -25.419  1.00 16.01           C  
-ATOM  19115  CD  PRO E 478      -2.295 -67.316 -25.477  1.00 18.71           C  
-ATOM  19116  N   ALA E 479      -2.057 -68.178 -21.713  1.00 28.11           N  
-ATOM  19117  CA  ALA E 479      -2.293 -68.392 -20.291  1.00 30.27           C  
-ATOM  19118  C   ALA E 479      -1.819 -69.773 -19.847  1.00 31.97           C  
-ATOM  19119  O   ALA E 479      -1.245 -69.927 -18.768  1.00 33.50           O  
-ATOM  19120  CB  ALA E 479      -3.768 -68.211 -19.971  1.00 29.62           C  
-ATOM  19121  N   ALA E 480      -2.051 -70.772 -20.691  1.00 31.84           N  
-ATOM  19122  CA  ALA E 480      -1.790 -72.160 -20.327  1.00 32.83           C  
-ATOM  19123  C   ALA E 480      -0.518 -72.722 -20.961  1.00 33.71           C  
-ATOM  19124  O   ALA E 480      -0.283 -73.928 -20.917  1.00 34.69           O  
-ATOM  19125  CB  ALA E 480      -2.984 -73.025 -20.707  1.00 29.41           C  
-ATOM  19126  N   LEU E 481       0.302 -71.851 -21.542  1.00 34.53           N  
-ATOM  19127  CA  LEU E 481       1.510 -72.286 -22.237  1.00 27.62           C  
-ATOM  19128  C   LEU E 481       2.517 -72.955 -21.307  1.00 36.05           C  
-ATOM  19129  O   LEU E 481       3.114 -73.971 -21.660  1.00 35.36           O  
-ATOM  19130  CB  LEU E 481       2.173 -71.106 -22.947  1.00 25.21           C  
-ATOM  19131  CG  LEU E 481       1.501 -70.643 -24.240  1.00 27.11           C  
-ATOM  19132  CD1 LEU E 481       2.353 -69.598 -24.944  1.00 24.57           C  
-ATOM  19133  CD2 LEU E 481       1.229 -71.826 -25.154  1.00 30.82           C  
-ATOM  19134  N   ASP E 482       2.703 -72.388 -20.120  1.00 41.01           N  
-ATOM  19135  CA  ASP E 482       3.659 -72.939 -19.164  1.00 40.38           C  
-ATOM  19136  C   ASP E 482       3.155 -74.247 -18.565  1.00 33.46           C  
-ATOM  19137  O   ASP E 482       3.920 -74.998 -17.960  1.00 35.29           O  
-ATOM  19138  CB  ASP E 482       3.953 -71.928 -18.052  1.00 33.18           C  
-ATOM  19139  CG  ASP E 482       4.719 -70.716 -18.554  1.00 43.52           C  
-ATOM  19140  OD1 ASP E 482       5.384 -70.823 -19.609  1.00 32.53           O  
-ATOM  19141  OD2 ASP E 482       4.661 -69.659 -17.889  1.00 37.90           O  
-ATOM  19142  N   GLU E 483       1.867 -74.518 -18.740  1.00 32.62           N  
-ATOM  19143  CA  GLU E 483       1.262 -75.733 -18.210  1.00 31.93           C  
-ATOM  19144  C   GLU E 483       1.362 -76.883 -19.204  1.00 29.40           C  
-ATOM  19145  O   GLU E 483       1.107 -78.035 -18.856  1.00 29.56           O  
-ATOM  19146  CB  GLU E 483      -0.201 -75.485 -17.847  1.00 33.08           C  
-ATOM  19147  CG  GLU E 483      -0.404 -74.348 -16.865  1.00 43.75           C  
-ATOM  19148  CD  GLU E 483      -1.866 -73.992 -16.684  1.00 52.53           C  
-ATOM  19149  OE1 GLU E 483      -2.721 -74.897 -16.805  1.00 39.01           O  
-ATOM  19150  OE2 GLU E 483      -2.160 -72.805 -16.428  1.00 61.05           O  
-ATOM  19151  N   MET E 484       1.733 -76.567 -20.441  1.00 31.50           N  
-ATOM  19152  CA  MET E 484       1.861 -77.586 -21.479  1.00 37.51           C  
-ATOM  19153  C   MET E 484       3.255 -78.205 -21.497  1.00 35.92           C  
-ATOM  19154  O   MET E 484       4.242 -77.559 -21.141  1.00 38.03           O  
-ATOM  19155  CB  MET E 484       1.551 -76.999 -22.857  1.00 39.75           C  
-ATOM  19156  CG  MET E 484       0.199 -76.323 -22.971  1.00 35.52           C  
-ATOM  19157  SD  MET E 484      -0.104 -75.762 -24.656  1.00 37.22           S  
-ATOM  19158  CE  MET E 484      -1.324 -74.481 -24.381  1.00 38.66           C  
-ATOM  19159  N   ALA E 485       3.330 -79.460 -21.922  1.00 32.80           N  
-ATOM  19160  CA  ALA E 485       4.609 -80.140 -22.062  1.00 33.48           C  
-ATOM  19161  C   ALA E 485       5.400 -79.511 -23.199  1.00 38.79           C  
-ATOM  19162  O   ALA E 485       6.628 -79.443 -23.155  1.00 43.93           O  
-ATOM  19163  CB  ALA E 485       4.402 -81.625 -22.309  1.00 34.14           C  
-ATOM  19164  N   LEU E 486       4.683 -79.044 -24.214  1.00 36.39           N  
-ATOM  19165  CA  LEU E 486       5.310 -78.413 -25.366  1.00 38.85           C  
-ATOM  19166  C   LEU E 486       4.315 -77.495 -26.065  1.00 38.53           C  
-ATOM  19167  O   LEU E 486       3.237 -77.936 -26.469  1.00 29.84           O  
-ATOM  19168  CB  LEU E 486       5.841 -79.474 -26.336  1.00 35.84           C  
-ATOM  19169  CG  LEU E 486       7.100 -79.149 -27.146  1.00 47.62           C  
-ATOM  19170  CD1 LEU E 486       7.729 -80.429 -27.672  1.00 58.22           C  
-ATOM  19171  CD2 LEU E 486       6.806 -78.193 -28.294  1.00 47.27           C  
-ATOM  19172  N   PRO E 487       4.675 -76.210 -26.203  1.00 38.49           N  
-ATOM  19173  CA  PRO E 487       3.829 -75.216 -26.870  1.00 33.18           C  
-ATOM  19174  C   PRO E 487       3.449 -75.670 -28.273  1.00 27.51           C  
-ATOM  19175  O   PRO E 487       4.300 -76.191 -28.992  1.00 37.63           O  
-ATOM  19176  CB  PRO E 487       4.717 -73.969 -26.914  1.00 31.66           C  
-ATOM  19177  CG  PRO E 487       5.686 -74.158 -25.800  1.00 33.04           C  
-ATOM  19178  CD  PRO E 487       5.949 -75.629 -25.745  1.00 34.89           C  
-ATOM  19179  N   PRO E 488       2.177 -75.490 -28.650  1.00 23.38           N  
-ATOM  19180  CA  PRO E 488       1.672 -75.960 -29.943  1.00 29.64           C  
-ATOM  19181  C   PRO E 488       2.463 -75.414 -31.125  1.00 28.16           C  
-ATOM  19182  O   PRO E 488       2.719 -74.212 -31.206  1.00 28.66           O  
-ATOM  19183  CB  PRO E 488       0.226 -75.444 -29.966  1.00 29.39           C  
-ATOM  19184  CG  PRO E 488       0.167 -74.380 -28.923  1.00 23.54           C  
-ATOM  19185  CD  PRO E 488       1.133 -74.809 -27.870  1.00 23.88           C  
-ATOM  19186  N   CYS E 489       2.862 -76.304 -32.024  1.00 29.32           N  
-ATOM  19187  CA  CYS E 489       3.567 -75.894 -33.226  1.00 32.19           C  
-ATOM  19188  C   CYS E 489       2.541 -75.572 -34.308  1.00 29.53           C  
-ATOM  19189  O   CYS E 489       2.433 -74.424 -34.736  1.00 24.66           O  
-ATOM  19190  CB  CYS E 489       4.548 -76.977 -33.676  1.00 36.00           C  
-ATOM  19191  SG  CYS E 489       5.920 -77.250 -32.519  1.00 63.16           S  
-ATOM  19192  N   HIS E 490       1.775 -76.572 -34.738  1.00 33.19           N  
-ATOM  19193  CA  HIS E 490       0.611 -76.297 -35.573  1.00 27.00           C  
-ATOM  19194  C   HIS E 490      -0.448 -75.641 -34.695  1.00 25.34           C  
-ATOM  19195  O   HIS E 490      -1.250 -76.320 -34.061  1.00 32.30           O  
-ATOM  19196  CB  HIS E 490       0.076 -77.570 -36.244  1.00 29.45           C  
-ATOM  19197  CG  HIS E 490      -0.079 -78.740 -35.321  1.00 31.65           C  
-ATOM  19198  ND1 HIS E 490      -1.310 -79.246 -34.960  1.00 30.67           N  
-ATOM  19199  CD2 HIS E 490       0.841 -79.519 -34.707  1.00 39.09           C  
-ATOM  19200  CE1 HIS E 490      -1.141 -80.279 -34.154  1.00 29.66           C  
-ATOM  19201  NE2 HIS E 490       0.156 -80.466 -33.984  1.00 34.17           N  
-ATOM  19202  N   LEU E 491      -0.436 -74.312 -34.657  1.00 22.98           N  
-ATOM  19203  CA  LEU E 491      -1.193 -73.575 -33.651  1.00 23.71           C  
-ATOM  19204  C   LEU E 491      -2.528 -73.023 -34.138  1.00 24.28           C  
-ATOM  19205  O   LEU E 491      -3.434 -72.804 -33.334  1.00 21.14           O  
-ATOM  19206  CB  LEU E 491      -0.344 -72.425 -33.105  1.00 29.06           C  
-ATOM  19207  CG  LEU E 491       0.108 -71.374 -34.120  1.00 23.22           C  
-ATOM  19208  CD1 LEU E 491      -0.833 -70.183 -34.150  1.00 27.07           C  
-ATOM  19209  CD2 LEU E 491       1.509 -70.920 -33.802  1.00 20.30           C  
-ATOM  19210  N   LEU E 492      -2.651 -72.769 -35.437  1.00 25.50           N  
-ATOM  19211  CA  LEU E 492      -3.892 -72.166 -35.925  1.00 20.40           C  
-ATOM  19212  C   LEU E 492      -4.437 -72.840 -37.180  1.00 20.93           C  
-ATOM  19213  O   LEU E 492      -3.674 -73.331 -37.998  1.00 18.13           O  
-ATOM  19214  CB  LEU E 492      -3.667 -70.679 -36.196  1.00 22.42           C  
-ATOM  19215  CG  LEU E 492      -4.901 -69.851 -36.542  1.00 21.07           C  
-ATOM  19216  CD1 LEU E 492      -5.188 -68.840 -35.446  1.00 18.30           C  
-ATOM  19217  CD2 LEU E 492      -4.707 -69.163 -37.880  1.00 21.35           C  
-ATOM  19218  N   CYS E 493      -5.756 -72.872 -37.337  1.00 21.59           N  
-ATOM  19219  CA  CYS E 493      -6.321 -73.327 -38.606  1.00 21.76           C  
-ATOM  19220  C   CYS E 493      -7.640 -72.631 -38.918  1.00 26.19           C  
-ATOM  19221  O   CYS E 493      -8.468 -72.415 -38.036  1.00 28.10           O  
-ATOM  19222  CB  CYS E 493      -6.500 -74.852 -38.619  1.00 21.78           C  
-ATOM  19223  SG  CYS E 493      -7.904 -75.500 -37.692  1.00 31.10           S  
-ATOM  19224  N   GLN E 494      -7.814 -72.267 -40.185  1.00 24.43           N  
-ATOM  19225  CA  GLN E 494      -8.997 -71.545 -40.636  1.00 23.94           C  
-ATOM  19226  C   GLN E 494      -9.588 -72.198 -41.885  1.00 26.54           C  
-ATOM  19227  O   GLN E 494      -8.856 -72.683 -42.751  1.00 21.28           O  
-ATOM  19228  CB  GLN E 494      -8.655 -70.082 -40.916  1.00 17.15           C  
-ATOM  19229  CG  GLN E 494      -9.831 -69.245 -41.368  1.00 20.54           C  
-ATOM  19230  CD  GLN E 494      -9.413 -67.879 -41.855  1.00 17.69           C  
-ATOM  19231  OE1 GLN E 494      -8.226 -67.560 -41.886  1.00 19.39           O  
-ATOM  19232  NE2 GLN E 494     -10.386 -67.063 -42.242  1.00 14.14           N  
-ATOM  19233  N   PHE E 495     -10.916 -72.207 -41.973  1.00 26.40           N  
-ATOM  19234  CA  PHE E 495     -11.604 -72.859 -43.084  1.00 28.04           C  
-ATOM  19235  C   PHE E 495     -12.282 -71.864 -44.027  1.00 25.09           C  
-ATOM  19236  O   PHE E 495     -12.457 -70.690 -43.694  1.00 22.22           O  
-ATOM  19237  CB  PHE E 495     -12.627 -73.862 -42.548  1.00 19.91           C  
-ATOM  19238  CG  PHE E 495     -12.005 -75.023 -41.828  1.00 20.10           C  
-ATOM  19239  CD1 PHE E 495     -11.612 -76.155 -42.524  1.00 19.20           C  
-ATOM  19240  CD2 PHE E 495     -11.797 -74.978 -40.460  1.00 19.77           C  
-ATOM  19241  CE1 PHE E 495     -11.033 -77.224 -41.868  1.00 16.71           C  
-ATOM  19242  CE2 PHE E 495     -11.218 -76.043 -39.798  1.00 20.83           C  
-ATOM  19243  CZ  PHE E 495     -10.836 -77.168 -40.503  1.00 25.47           C  
-ATOM  19244  N   TYR E 496     -12.664 -72.351 -45.205  1.00 19.78           N  
-ATOM  19245  CA  TYR E 496     -13.219 -71.498 -46.248  1.00 17.77           C  
-ATOM  19246  C   TYR E 496     -14.079 -72.301 -47.218  1.00 19.52           C  
-ATOM  19247  O   TYR E 496     -13.718 -73.405 -47.611  1.00 20.52           O  
-ATOM  19248  CB  TYR E 496     -12.082 -70.792 -46.986  1.00 14.82           C  
-ATOM  19249  CG  TYR E 496     -12.471 -69.997 -48.214  1.00 17.72           C  
-ATOM  19250  CD1 TYR E 496     -12.527 -70.598 -49.465  1.00 20.77           C  
-ATOM  19251  CD2 TYR E 496     -12.742 -68.638 -48.129  1.00 21.24           C  
-ATOM  19252  CE1 TYR E 496     -12.866 -69.880 -50.589  1.00 21.65           C  
-ATOM  19253  CE2 TYR E 496     -13.082 -67.908 -49.251  1.00 28.81           C  
-ATOM  19254  CZ  TYR E 496     -13.141 -68.536 -50.478  1.00 29.78           C  
-ATOM  19255  OH  TYR E 496     -13.477 -67.823 -51.604  1.00 38.27           O  
-ATOM  19256  N   VAL E 497     -15.226 -71.743 -47.594  1.00 22.55           N  
-ATOM  19257  CA  VAL E 497     -16.113 -72.388 -48.557  1.00 21.67           C  
-ATOM  19258  C   VAL E 497     -16.434 -71.419 -49.689  1.00 32.94           C  
-ATOM  19259  O   VAL E 497     -16.534 -70.211 -49.468  1.00 38.92           O  
-ATOM  19260  CB  VAL E 497     -17.422 -72.866 -47.899  1.00 23.38           C  
-ATOM  19261  CG1 VAL E 497     -18.209 -73.749 -48.855  1.00 32.13           C  
-ATOM  19262  CG2 VAL E 497     -17.125 -73.622 -46.625  1.00 20.06           C  
-ATOM  19263  N   ASN E 498     -16.593 -71.948 -50.899  1.00 26.08           N  
-ATOM  19264  CA  ASN E 498     -16.780 -71.105 -52.073  1.00 33.36           C  
-ATOM  19265  C   ASN E 498     -18.085 -71.359 -52.821  1.00 35.34           C  
-ATOM  19266  O   ASN E 498     -19.053 -71.872 -52.259  1.00 34.74           O  
-ATOM  19267  CB  ASN E 498     -15.604 -71.289 -53.034  1.00 32.28           C  
-ATOM  19268  CG  ASN E 498     -15.529 -72.697 -53.599  1.00 26.27           C  
-ATOM  19269  OD1 ASN E 498     -16.176 -73.613 -53.099  1.00 25.40           O  
-ATOM  19270  ND2 ASN E 498     -14.730 -72.874 -54.643  1.00 27.19           N  
-ATOM  19271  N   ASP E 499     -18.084 -70.984 -54.098  1.00 31.80           N  
-ATOM  19272  CA  ASP E 499     -19.220 -71.178 -54.992  1.00 27.49           C  
-ATOM  19273  C   ASP E 499     -19.776 -72.596 -54.963  1.00 39.22           C  
-ATOM  19274  O   ASP E 499     -20.977 -72.799 -54.793  1.00 41.92           O  
-ATOM  19275  CB  ASP E 499     -18.815 -70.830 -56.427  1.00 35.01           C  
-ATOM  19276  CG  ASP E 499     -19.123 -69.394 -56.787  1.00 59.10           C  
-ATOM  19277  OD1 ASP E 499     -19.555 -68.640 -55.890  1.00 66.75           O  
-ATOM  19278  OD2 ASP E 499     -18.930 -69.021 -57.965  1.00 58.75           O  
-ATOM  19279  N   GLN E 500     -18.890 -73.573 -55.115  1.00 33.27           N  
-ATOM  19280  CA  GLN E 500     -19.296 -74.945 -55.389  1.00 28.12           C  
-ATOM  19281  C   GLN E 500     -19.288 -75.841 -54.153  1.00 22.73           C  
-ATOM  19282  O   GLN E 500     -19.078 -77.051 -54.262  1.00 22.19           O  
-ATOM  19283  CB  GLN E 500     -18.381 -75.536 -56.461  1.00 33.91           C  
-ATOM  19284  CG  GLN E 500     -17.875 -74.517 -57.477  1.00 30.10           C  
-ATOM  19285  CD  GLN E 500     -18.851 -74.277 -58.613  1.00 38.84           C  
-ATOM  19286  OE1 GLN E 500     -18.647 -74.758 -59.728  1.00 48.00           O  
-ATOM  19287  NE2 GLN E 500     -19.913 -73.528 -58.338  1.00 40.58           N  
-ATOM  19288  N   LYS E 501     -19.531 -75.248 -52.987  1.00 24.79           N  
-ATOM  19289  CA  LYS E 501     -19.513 -75.983 -51.723  1.00 26.10           C  
-ATOM  19290  C   LYS E 501     -18.215 -76.769 -51.550  1.00 23.96           C  
-ATOM  19291  O   LYS E 501     -18.237 -77.959 -51.238  1.00 27.76           O  
-ATOM  19292  CB  LYS E 501     -20.719 -76.925 -51.630  1.00 27.62           C  
-ATOM  19293  CG  LYS E 501     -22.020 -76.248 -51.218  1.00 28.81           C  
-ATOM  19294  CD  LYS E 501     -23.234 -77.034 -51.709  1.00 38.22           C  
-ATOM  19295  CE  LYS E 501     -23.288 -78.446 -51.135  1.00 35.63           C  
-ATOM  19296  NZ  LYS E 501     -23.765 -78.479 -49.724  1.00 28.43           N  
-ATOM  19297  N   GLU E 502     -17.088 -76.098 -51.762  1.00 28.12           N  
-ATOM  19298  CA  GLU E 502     -15.781 -76.737 -51.646  1.00 21.87           C  
-ATOM  19299  C   GLU E 502     -14.985 -76.156 -50.482  1.00 22.67           C  
-ATOM  19300  O   GLU E 502     -14.845 -74.939 -50.356  1.00 24.83           O  
-ATOM  19301  CB  GLU E 502     -14.996 -76.591 -52.948  1.00 15.95           C  
-ATOM  19302  CG  GLU E 502     -15.831 -76.842 -54.187  1.00 25.66           C  
-ATOM  19303  CD  GLU E 502     -14.997 -76.928 -55.446  1.00 34.26           C  
-ATOM  19304  OE1 GLU E 502     -14.799 -78.055 -55.948  1.00 48.64           O  
-ATOM  19305  OE2 GLU E 502     -14.544 -75.870 -55.934  1.00 25.52           O  
-ATOM  19306  N   LEU E 503     -14.461 -77.035 -49.636  1.00 23.73           N  
-ATOM  19307  CA  LEU E 503     -13.773 -76.614 -48.424  1.00 17.78           C  
-ATOM  19308  C   LEU E 503     -12.265 -76.502 -48.619  1.00 24.95           C  
-ATOM  19309  O   LEU E 503     -11.626 -77.403 -49.166  1.00 27.63           O  
-ATOM  19310  CB  LEU E 503     -14.073 -77.586 -47.283  1.00 16.64           C  
-ATOM  19311  CG  LEU E 503     -13.461 -77.263 -45.921  1.00 15.38           C  
-ATOM  19312  CD1 LEU E 503     -14.128 -76.042 -45.304  1.00 19.76           C  
-ATOM  19313  CD2 LEU E 503     -13.565 -78.466 -44.998  1.00 13.44           C  
-ATOM  19314  N   SER E 504     -11.710 -75.383 -48.166  1.00 22.26           N  
-ATOM  19315  CA  SER E 504     -10.269 -75.183 -48.135  1.00 19.07           C  
-ATOM  19316  C   SER E 504      -9.835 -74.852 -46.713  1.00 18.96           C  
-ATOM  19317  O   SER E 504     -10.616 -74.308 -45.928  1.00 19.21           O  
-ATOM  19318  CB  SER E 504      -9.846 -74.075 -49.101  1.00 22.96           C  
-ATOM  19319  OG  SER E 504     -10.031 -74.472 -50.451  1.00 32.76           O  
-ATOM  19320  N   CYS E 505      -8.590 -75.181 -46.386  1.00 20.94           N  
-ATOM  19321  CA  CYS E 505      -8.096 -75.025 -45.026  1.00 16.64           C  
-ATOM  19322  C   CYS E 505      -6.667 -74.485 -44.986  1.00 16.89           C  
-ATOM  19323  O   CYS E 505      -5.784 -74.978 -45.686  1.00 15.98           O  
-ATOM  19324  CB  CYS E 505      -8.172 -76.365 -44.290  1.00 15.79           C  
-ATOM  19325  SG  CYS E 505      -7.543 -76.332 -42.599  1.00 22.66           S  
-ATOM  19326  N   ILE E 506      -6.455 -73.459 -44.167  1.00 18.04           N  
-ATOM  19327  CA  ILE E 506      -5.121 -72.924 -43.922  1.00 13.21           C  
-ATOM  19328  C   ILE E 506      -4.680 -73.288 -42.518  1.00 16.62           C  
-ATOM  19329  O   ILE E 506      -5.440 -73.117 -41.571  1.00 15.44           O  
-ATOM  19330  CB  ILE E 506      -5.064 -71.389 -44.062  1.00 14.21           C  
-ATOM  19331  CG1 ILE E 506      -5.401 -70.951 -45.484  1.00 19.99           C  
-ATOM  19332  CG2 ILE E 506      -3.687 -70.871 -43.679  1.00 14.21           C  
-ATOM  19333  CD1 ILE E 506      -5.477 -69.449 -45.641  1.00 19.04           C  
-ATOM  19334  N   MET E 507      -3.457 -73.783 -42.376  1.00 17.70           N  
-ATOM  19335  CA  MET E 507      -2.908 -74.019 -41.050  1.00 14.00           C  
-ATOM  19336  C   MET E 507      -1.643 -73.198 -40.838  1.00 15.19           C  
-ATOM  19337  O   MET E 507      -0.715 -73.252 -41.641  1.00 18.97           O  
-ATOM  19338  CB  MET E 507      -2.622 -75.504 -40.839  1.00 14.30           C  
-ATOM  19339  CG  MET E 507      -2.239 -75.855 -39.409  1.00 18.93           C  
-ATOM  19340  SD  MET E 507      -0.467 -75.768 -39.093  1.00 22.35           S  
-ATOM  19341  CE  MET E 507       0.088 -77.236 -39.956  1.00 21.63           C  
-ATOM  19342  N   TYR E 508      -1.617 -72.422 -39.759  1.00 17.15           N  
-ATOM  19343  CA  TYR E 508      -0.416 -71.691 -39.384  1.00 20.64           C  
-ATOM  19344  C   TYR E 508       0.344 -72.421 -38.284  1.00 19.97           C  
-ATOM  19345  O   TYR E 508      -0.204 -72.743 -37.212  1.00 26.39           O  
-ATOM  19346  CB  TYR E 508      -0.736 -70.264 -38.933  1.00 24.56           C  
-ATOM  19347  CG  TYR E 508       0.519 -69.444 -38.728  1.00 21.09           C  
-ATOM  19348  CD1 TYR E 508       1.111 -68.769 -39.788  1.00 17.26           C  
-ATOM  19349  CD2 TYR E 508       1.130 -69.372 -37.482  1.00 21.20           C  
-ATOM  19350  CE1 TYR E 508       2.269 -68.033 -39.606  1.00 19.40           C  
-ATOM  19351  CE2 TYR E 508       2.284 -68.643 -37.293  1.00 18.59           C  
-ATOM  19352  CZ  TYR E 508       2.849 -67.974 -38.355  1.00 21.33           C  
-ATOM  19353  OH  TYR E 508       3.999 -67.243 -38.158  1.00 29.47           O  
-ATOM  19354  N   GLN E 509       1.619 -72.656 -38.579  1.00 16.92           N  
-ATOM  19355  CA  GLN E 509       2.528 -73.411 -37.737  1.00 23.90           C  
-ATOM  19356  C   GLN E 509       3.766 -72.567 -37.435  1.00 25.87           C  
-ATOM  19357  O   GLN E 509       4.502 -72.189 -38.347  1.00 20.38           O  
-ATOM  19358  CB  GLN E 509       2.910 -74.720 -38.432  1.00 24.86           C  
-ATOM  19359  CG  GLN E 509       3.799 -75.644 -37.626  1.00 31.73           C  
-ATOM  19360  CD  GLN E 509       4.213 -76.870 -38.419  1.00 33.53           C  
-ATOM  19361  OE1 GLN E 509       3.663 -77.143 -39.484  1.00 25.98           O  
-ATOM  19362  NE2 GLN E 509       5.191 -77.607 -37.910  1.00 46.30           N  
-ATOM  19363  N   ARG E 510       3.985 -72.264 -36.158  1.00 25.60           N  
-ATOM  19364  CA  ARG E 510       5.072 -71.372 -35.759  1.00 26.52           C  
-ATOM  19365  C   ARG E 510       6.450 -71.969 -36.012  1.00 24.19           C  
-ATOM  19366  O   ARG E 510       7.367 -71.270 -36.444  1.00 24.48           O  
-ATOM  19367  CB  ARG E 510       4.949 -71.002 -34.280  1.00 25.76           C  
-ATOM  19368  CG  ARG E 510       4.833 -72.199 -33.352  1.00 27.61           C  
-ATOM  19369  CD  ARG E 510       5.047 -71.806 -31.903  1.00 28.44           C  
-ATOM  19370  NE  ARG E 510       5.239 -72.975 -31.050  1.00 28.32           N  
-ATOM  19371  CZ  ARG E 510       6.402 -73.597 -30.894  1.00 25.33           C  
-ATOM  19372  NH1 ARG E 510       7.476 -73.163 -31.535  1.00 26.81           N  
-ATOM  19373  NH2 ARG E 510       6.492 -74.654 -30.099  1.00 31.58           N  
-ATOM  19374  N   SER E 511       6.592 -73.259 -35.727  1.00 24.69           N  
-ATOM  19375  CA  SER E 511       7.874 -73.934 -35.849  1.00 30.31           C  
-ATOM  19376  C   SER E 511       7.720 -75.190 -36.685  1.00 31.15           C  
-ATOM  19377  O   SER E 511       6.778 -75.957 -36.491  1.00 40.47           O  
-ATOM  19378  CB  SER E 511       8.433 -74.279 -34.471  1.00 32.24           C  
-ATOM  19379  OG  SER E 511       9.737 -74.823 -34.573  1.00 42.16           O  
-ATOM  19380  N   CYS E 512       8.645 -75.404 -37.613  1.00 26.07           N  
-ATOM  19381  CA  CYS E 512       8.495 -76.489 -38.570  1.00 26.13           C  
-ATOM  19382  C   CYS E 512       9.764 -77.308 -38.772  1.00 32.42           C  
-ATOM  19383  O   CYS E 512      10.702 -76.864 -39.435  1.00 34.90           O  
-ATOM  19384  CB  CYS E 512       8.035 -75.929 -39.917  1.00 26.47           C  
-ATOM  19385  SG  CYS E 512       6.579 -74.862 -39.823  1.00 37.12           S  
-ATOM  19386  N   ASP E 513       9.784 -78.506 -38.198  1.00 36.60           N  
-ATOM  19387  CA  ASP E 513      10.807 -79.489 -38.526  1.00 30.01           C  
-ATOM  19388  C   ASP E 513      10.511 -80.013 -39.925  1.00 23.13           C  
-ATOM  19389  O   ASP E 513       9.625 -80.846 -40.112  1.00 23.29           O  
-ATOM  19390  CB  ASP E 513      10.828 -80.628 -37.504  1.00 40.59           C  
-ATOM  19391  CG  ASP E 513      12.050 -81.522 -37.644  1.00 52.35           C  
-ATOM  19392  OD1 ASP E 513      12.694 -81.500 -38.716  1.00 43.22           O  
-ATOM  19393  OD2 ASP E 513      12.364 -82.252 -36.679  1.00 56.48           O  
-ATOM  19394  N   VAL E 514      11.251 -79.511 -40.906  1.00 21.20           N  
-ATOM  19395  CA  VAL E 514      10.959 -79.795 -42.306  1.00 23.09           C  
-ATOM  19396  C   VAL E 514      11.174 -81.257 -42.674  1.00 29.05           C  
-ATOM  19397  O   VAL E 514      10.341 -81.860 -43.350  1.00 33.43           O  
-ATOM  19398  CB  VAL E 514      11.806 -78.913 -43.231  1.00 19.50           C  
-ATOM  19399  CG1 VAL E 514      11.706 -79.391 -44.668  1.00 24.49           C  
-ATOM  19400  CG2 VAL E 514      11.347 -77.480 -43.122  1.00 21.87           C  
-ATOM  19401  N   GLY E 515      12.282 -81.829 -42.219  1.00 31.76           N  
-ATOM  19402  CA  GLY E 515      12.612 -83.199 -42.558  1.00 28.92           C  
-ATOM  19403  C   GLY E 515      11.680 -84.219 -41.935  1.00 32.71           C  
-ATOM  19404  O   GLY E 515      11.305 -85.200 -42.577  1.00 43.65           O  
-ATOM  19405  N   LEU E 516      11.288 -83.975 -40.689  1.00 25.40           N  
-ATOM  19406  CA  LEU E 516      10.570 -84.977 -39.910  1.00 37.15           C  
-ATOM  19407  C   LEU E 516       9.079 -84.676 -39.734  1.00 33.05           C  
-ATOM  19408  O   LEU E 516       8.233 -85.525 -40.014  1.00 34.00           O  
-ATOM  19409  CB  LEU E 516      11.232 -85.126 -38.539  1.00 40.81           C  
-ATOM  19410  CG  LEU E 516      10.826 -86.324 -37.685  1.00 51.60           C  
-ATOM  19411  CD1 LEU E 516      10.787 -87.591 -38.523  1.00 57.68           C  
-ATOM  19412  CD2 LEU E 516      11.803 -86.477 -36.534  1.00 68.85           C  
-ATOM  19413  N   GLY E 517       8.760 -83.471 -39.275  1.00 29.85           N  
-ATOM  19414  CA  GLY E 517       7.400 -83.150 -38.875  1.00 32.89           C  
-ATOM  19415  C   GLY E 517       6.457 -82.664 -39.964  1.00 30.08           C  
-ATOM  19416  O   GLY E 517       5.268 -83.005 -39.962  1.00 22.42           O  
-ATOM  19417  N   VAL E 518       6.980 -81.861 -40.886  1.00 24.06           N  
-ATOM  19418  CA  VAL E 518       6.158 -81.212 -41.907  1.00 21.12           C  
-ATOM  19419  C   VAL E 518       5.276 -82.169 -42.723  1.00 20.68           C  
-ATOM  19420  O   VAL E 518       4.083 -81.908 -42.860  1.00 22.74           O  
-ATOM  19421  CB  VAL E 518       7.036 -80.372 -42.870  1.00 17.34           C  
-ATOM  19422  CG1 VAL E 518       6.274 -80.038 -44.146  1.00 12.37           C  
-ATOM  19423  CG2 VAL E 518       7.489 -79.111 -42.174  1.00 20.13           C  
-ATOM  19424  N   PRO E 519       5.836 -83.278 -43.254  1.00 19.74           N  
-ATOM  19425  CA  PRO E 519       4.939 -84.166 -44.009  1.00 18.01           C  
-ATOM  19426  C   PRO E 519       3.787 -84.702 -43.158  1.00 15.81           C  
-ATOM  19427  O   PRO E 519       2.638 -84.780 -43.611  1.00 14.37           O  
-ATOM  19428  CB  PRO E 519       5.866 -85.309 -44.448  1.00 20.71           C  
-ATOM  19429  CG  PRO E 519       7.230 -84.730 -44.406  1.00 15.07           C  
-ATOM  19430  CD  PRO E 519       7.219 -83.791 -43.252  1.00 15.52           C  
-ATOM  19431  N   PHE E 520       4.124 -85.059 -41.923  1.00 14.52           N  
-ATOM  19432  CA  PHE E 520       3.170 -85.531 -40.932  1.00 16.22           C  
-ATOM  19433  C   PHE E 520       2.062 -84.508 -40.699  1.00 20.90           C  
-ATOM  19434  O   PHE E 520       0.888 -84.866 -40.610  1.00 25.12           O  
-ATOM  19435  CB  PHE E 520       3.899 -85.835 -39.623  1.00 22.59           C  
-ATOM  19436  CG  PHE E 520       3.096 -86.641 -38.643  1.00 28.11           C  
-ATOM  19437  CD1 PHE E 520       2.335 -86.017 -37.667  1.00 29.52           C  
-ATOM  19438  CD2 PHE E 520       3.127 -88.025 -38.679  1.00 25.18           C  
-ATOM  19439  CE1 PHE E 520       1.608 -86.760 -36.757  1.00 26.37           C  
-ATOM  19440  CE2 PHE E 520       2.407 -88.771 -37.770  1.00 27.89           C  
-ATOM  19441  CZ  PHE E 520       1.647 -88.137 -36.808  1.00 31.44           C  
-ATOM  19442  N   ASN E 521       2.439 -83.236 -40.602  1.00 22.05           N  
-ATOM  19443  CA  ASN E 521       1.464 -82.170 -40.401  1.00 21.71           C  
-ATOM  19444  C   ASN E 521       0.569 -81.962 -41.618  1.00 20.73           C  
-ATOM  19445  O   ASN E 521      -0.649 -81.806 -41.486  1.00 22.88           O  
-ATOM  19446  CB  ASN E 521       2.171 -80.864 -40.051  1.00 25.08           C  
-ATOM  19447  CG  ASN E 521       2.881 -80.931 -38.720  1.00 29.91           C  
-ATOM  19448  OD1 ASN E 521       4.088 -80.718 -38.637  1.00 30.70           O  
-ATOM  19449  ND2 ASN E 521       2.134 -81.241 -37.668  1.00 29.61           N  
-ATOM  19450  N   ILE E 522       1.187 -81.949 -42.796  1.00 15.14           N  
-ATOM  19451  CA  ILE E 522       0.463 -81.881 -44.057  1.00 15.34           C  
-ATOM  19452  C   ILE E 522      -0.622 -82.945 -44.112  1.00 16.94           C  
-ATOM  19453  O   ILE E 522      -1.809 -82.639 -44.280  1.00 16.41           O  
-ATOM  19454  CB  ILE E 522       1.414 -82.060 -45.257  1.00 12.75           C  
-ATOM  19455  CG1 ILE E 522       2.432 -80.922 -45.303  1.00 14.83           C  
-ATOM  19456  CG2 ILE E 522       0.629 -82.117 -46.547  1.00 15.82           C  
-ATOM  19457  CD1 ILE E 522       3.466 -81.085 -46.387  1.00 18.77           C  
-ATOM  19458  N   ALA E 523      -0.203 -84.196 -43.949  1.00 17.18           N  
-ATOM  19459  CA  ALA E 523      -1.132 -85.318 -43.925  1.00 17.72           C  
-ATOM  19460  C   ALA E 523      -2.206 -85.120 -42.861  1.00 16.41           C  
-ATOM  19461  O   ALA E 523      -3.387 -85.397 -43.095  1.00 16.50           O  
-ATOM  19462  CB  ALA E 523      -0.387 -86.620 -43.684  1.00 16.55           C  
-ATOM  19463  N   SER E 524      -1.789 -84.625 -41.700  1.00 13.68           N  
-ATOM  19464  CA  SER E 524      -2.693 -84.443 -40.573  1.00 15.65           C  
-ATOM  19465  C   SER E 524      -3.843 -83.495 -40.889  1.00 15.02           C  
-ATOM  19466  O   SER E 524      -5.013 -83.868 -40.792  1.00 19.71           O  
-ATOM  19467  CB  SER E 524      -1.918 -83.934 -39.356  1.00 13.17           C  
-ATOM  19468  OG  SER E 524      -2.708 -84.034 -38.188  1.00 20.29           O  
-ATOM  19469  N   TYR E 525      -3.512 -82.266 -41.261  1.00 13.52           N  
-ATOM  19470  CA  TYR E 525      -4.546 -81.267 -41.497  1.00 12.23           C  
-ATOM  19471  C   TYR E 525      -5.285 -81.495 -42.813  1.00 15.58           C  
-ATOM  19472  O   TYR E 525      -6.426 -81.058 -42.965  1.00 16.87           O  
-ATOM  19473  CB  TYR E 525      -3.948 -79.860 -41.437  1.00  9.04           C  
-ATOM  19474  CG  TYR E 525      -3.797 -79.387 -40.006  1.00 15.61           C  
-ATOM  19475  CD1 TYR E 525      -2.670 -79.709 -39.263  1.00 16.26           C  
-ATOM  19476  CD2 TYR E 525      -4.797 -78.648 -39.390  1.00 14.46           C  
-ATOM  19477  CE1 TYR E 525      -2.537 -79.298 -37.954  1.00 15.99           C  
-ATOM  19478  CE2 TYR E 525      -4.673 -78.229 -38.082  1.00 18.69           C  
-ATOM  19479  CZ  TYR E 525      -3.541 -78.557 -37.366  1.00 20.88           C  
-ATOM  19480  OH  TYR E 525      -3.416 -78.140 -36.059  1.00 31.12           O  
-ATOM  19481  N   SER E 526      -4.658 -82.194 -43.754  1.00 17.89           N  
-ATOM  19482  CA  SER E 526      -5.373 -82.600 -44.961  1.00 13.89           C  
-ATOM  19483  C   SER E 526      -6.462 -83.611 -44.592  1.00 17.95           C  
-ATOM  19484  O   SER E 526      -7.607 -83.518 -45.059  1.00 19.12           O  
-ATOM  19485  CB  SER E 526      -4.414 -83.191 -45.992  1.00 15.36           C  
-ATOM  19486  OG  SER E 526      -3.376 -82.278 -46.299  1.00 18.95           O  
-ATOM  19487  N   LEU E 527      -6.097 -84.568 -43.740  1.00 14.73           N  
-ATOM  19488  CA  LEU E 527      -7.051 -85.540 -43.212  1.00 12.32           C  
-ATOM  19489  C   LEU E 527      -8.181 -84.843 -42.460  1.00 16.18           C  
-ATOM  19490  O   LEU E 527      -9.359 -85.164 -42.656  1.00 17.49           O  
-ATOM  19491  CB  LEU E 527      -6.352 -86.541 -42.289  1.00 13.63           C  
-ATOM  19492  CG  LEU E 527      -7.238 -87.643 -41.702  1.00 13.41           C  
-ATOM  19493  CD1 LEU E 527      -7.885 -88.461 -42.806  1.00 14.58           C  
-ATOM  19494  CD2 LEU E 527      -6.440 -88.543 -40.773  1.00 20.66           C  
-ATOM  19495  N   LEU E 528      -7.815 -83.893 -41.599  1.00 16.84           N  
-ATOM  19496  CA  LEU E 528      -8.804 -83.101 -40.869  1.00 15.72           C  
-ATOM  19497  C   LEU E 528      -9.766 -82.445 -41.846  1.00 15.04           C  
-ATOM  19498  O   LEU E 528     -10.978 -82.467 -41.641  1.00 14.96           O  
-ATOM  19499  CB  LEU E 528      -8.138 -82.029 -39.999  1.00 12.70           C  
-ATOM  19500  CG  LEU E 528      -9.100 -81.098 -39.249  1.00  6.81           C  
-ATOM  19501  CD1 LEU E 528      -9.928 -81.892 -38.258  1.00  6.18           C  
-ATOM  19502  CD2 LEU E 528      -8.358 -79.971 -38.546  1.00  7.94           C  
-ATOM  19503  N   THR E 529      -9.217 -81.869 -42.913  1.00 13.36           N  
-ATOM  19504  CA  THR E 529     -10.036 -81.231 -43.935  1.00 15.06           C  
-ATOM  19505  C   THR E 529     -11.010 -82.223 -44.562  1.00 14.81           C  
-ATOM  19506  O   THR E 529     -12.182 -81.903 -44.749  1.00 18.01           O  
-ATOM  19507  CB  THR E 529      -9.182 -80.602 -45.051  1.00 12.74           C  
-ATOM  19508  OG1 THR E 529      -8.227 -79.696 -44.484  1.00  8.81           O  
-ATOM  19509  CG2 THR E 529     -10.075 -79.845 -46.023  1.00 13.74           C  
-ATOM  19510  N   LEU E 530     -10.524 -83.420 -44.885  1.00 13.17           N  
-ATOM  19511  CA  LEU E 530     -11.398 -84.469 -45.408  1.00 11.68           C  
-ATOM  19512  C   LEU E 530     -12.560 -84.740 -44.463  1.00 15.99           C  
-ATOM  19513  O   LEU E 530     -13.727 -84.703 -44.869  1.00 13.05           O  
-ATOM  19514  CB  LEU E 530     -10.633 -85.772 -45.637  1.00 12.63           C  
-ATOM  19515  CG  LEU E 530      -9.616 -85.875 -46.768  1.00 16.72           C  
-ATOM  19516  CD1 LEU E 530      -9.335 -87.336 -47.066  1.00 16.60           C  
-ATOM  19517  CD2 LEU E 530     -10.104 -85.167 -48.011  1.00 16.64           C  
-ATOM  19518  N   MET E 531     -12.234 -85.010 -43.201  1.00 17.95           N  
-ATOM  19519  CA  MET E 531     -13.249 -85.365 -42.214  1.00 22.43           C  
-ATOM  19520  C   MET E 531     -14.287 -84.260 -42.033  1.00 21.21           C  
-ATOM  19521  O   MET E 531     -15.494 -84.506 -42.135  1.00 23.48           O  
-ATOM  19522  CB  MET E 531     -12.582 -85.694 -40.880  1.00 15.45           C  
-ATOM  19523  CG  MET E 531     -11.532 -86.781 -40.984  1.00 11.23           C  
-ATOM  19524  SD  MET E 531     -10.511 -86.874 -39.508  1.00 32.18           S  
-ATOM  19525  CE  MET E 531     -11.670 -87.565 -38.335  1.00 22.08           C  
-ATOM  19526  N   VAL E 532     -13.810 -83.050 -41.763  1.00 15.71           N  
-ATOM  19527  CA  VAL E 532     -14.684 -81.892 -41.633  1.00 15.51           C  
-ATOM  19528  C   VAL E 532     -15.590 -81.749 -42.853  1.00 18.51           C  
-ATOM  19529  O   VAL E 532     -16.799 -81.560 -42.716  1.00 20.39           O  
-ATOM  19530  CB  VAL E 532     -13.876 -80.593 -41.448  1.00 14.20           C  
-ATOM  19531  CG1 VAL E 532     -14.781 -79.388 -41.556  1.00 11.51           C  
-ATOM  19532  CG2 VAL E 532     -13.158 -80.605 -40.110  1.00 20.51           C  
-ATOM  19533  N   ALA E 533     -15.005 -81.864 -44.044  1.00 18.42           N  
-ATOM  19534  CA  ALA E 533     -15.762 -81.716 -45.285  1.00 19.25           C  
-ATOM  19535  C   ALA E 533     -16.867 -82.764 -45.390  1.00 24.22           C  
-ATOM  19536  O   ALA E 533     -17.991 -82.448 -45.790  1.00 20.00           O  
-ATOM  19537  CB  ALA E 533     -14.839 -81.800 -46.490  1.00 14.95           C  
-ATOM  19538  N   HIS E 534     -16.552 -84.009 -45.037  1.00 24.22           N  
-ATOM  19539  CA  HIS E 534     -17.562 -85.063 -45.067  1.00 26.46           C  
-ATOM  19540  C   HIS E 534     -18.682 -84.780 -44.075  1.00 25.09           C  
-ATOM  19541  O   HIS E 534     -19.858 -84.951 -44.395  1.00 27.92           O  
-ATOM  19542  CB  HIS E 534     -16.956 -86.432 -44.765  1.00 20.56           C  
-ATOM  19543  CG  HIS E 534     -17.980 -87.469 -44.417  1.00 23.01           C  
-ATOM  19544  ND1 HIS E 534     -18.871 -87.974 -45.340  1.00 30.90           N  
-ATOM  19545  CD2 HIS E 534     -18.276 -88.071 -43.241  1.00 22.78           C  
-ATOM  19546  CE1 HIS E 534     -19.660 -88.855 -44.751  1.00 27.91           C  
-ATOM  19547  NE2 HIS E 534     -19.321 -88.933 -43.477  1.00 26.26           N  
-ATOM  19548  N   VAL E 535     -18.312 -84.352 -42.872  1.00 25.30           N  
-ATOM  19549  CA  VAL E 535     -19.291 -84.088 -41.823  1.00 17.79           C  
-ATOM  19550  C   VAL E 535     -20.180 -82.890 -42.184  1.00 22.20           C  
-ATOM  19551  O   VAL E 535     -21.334 -82.811 -41.762  1.00 24.13           O  
-ATOM  19552  CB  VAL E 535     -18.582 -83.862 -40.457  1.00 22.38           C  
-ATOM  19553  CG1 VAL E 535     -19.530 -83.286 -39.421  1.00 32.84           C  
-ATOM  19554  CG2 VAL E 535     -17.982 -85.169 -39.955  1.00 25.18           C  
-ATOM  19555  N   CYS E 536     -19.658 -81.981 -43.002  1.00 25.33           N  
-ATOM  19556  CA  CYS E 536     -20.404 -80.779 -43.368  1.00 22.21           C  
-ATOM  19557  C   CYS E 536     -21.010 -80.836 -44.772  1.00 23.72           C  
-ATOM  19558  O   CYS E 536     -21.448 -79.815 -45.301  1.00 27.37           O  
-ATOM  19559  CB  CYS E 536     -19.499 -79.551 -43.255  1.00 22.97           C  
-ATOM  19560  SG  CYS E 536     -18.828 -79.269 -41.599  1.00 34.80           S  
-ATOM  19561  N   ASN E 537     -21.040 -82.028 -45.361  1.00 31.91           N  
-ATOM  19562  CA  ASN E 537     -21.526 -82.222 -46.730  1.00 36.06           C  
-ATOM  19563  C   ASN E 537     -20.851 -81.305 -47.743  1.00 32.70           C  
-ATOM  19564  O   ASN E 537     -21.517 -80.685 -48.573  1.00 35.34           O  
-ATOM  19565  CB  ASN E 537     -23.042 -82.027 -46.801  1.00 32.78           C  
-ATOM  19566  CG  ASN E 537     -23.805 -83.324 -46.621  1.00 55.86           C  
-ATOM  19567  OD1 ASN E 537     -23.882 -84.142 -47.539  1.00 64.61           O  
-ATOM  19568  ND2 ASN E 537     -24.381 -83.516 -45.438  1.00 42.96           N  
-ATOM  19569  N   LEU E 538     -19.527 -81.223 -47.671  1.00 30.07           N  
-ATOM  19570  CA  LEU E 538     -18.763 -80.376 -48.579  1.00 28.00           C  
-ATOM  19571  C   LEU E 538     -17.705 -81.181 -49.322  1.00 27.36           C  
-ATOM  19572  O   LEU E 538     -17.431 -82.331 -48.981  1.00 28.23           O  
-ATOM  19573  CB  LEU E 538     -18.108 -79.228 -47.812  1.00 27.04           C  
-ATOM  19574  CG  LEU E 538     -19.070 -78.326 -47.041  1.00 23.54           C  
-ATOM  19575  CD1 LEU E 538     -18.313 -77.351 -46.149  1.00 15.44           C  
-ATOM  19576  CD2 LEU E 538     -19.983 -77.588 -48.008  1.00 22.68           C  
-ATOM  19577  N   LYS E 539     -17.115 -80.569 -50.342  1.00 16.71           N  
-ATOM  19578  CA  LYS E 539     -16.065 -81.212 -51.119  1.00 22.23           C  
-ATOM  19579  C   LYS E 539     -14.691 -80.669 -50.735  1.00 25.89           C  
-ATOM  19580  O   LYS E 539     -14.461 -79.464 -50.790  1.00 28.26           O  
-ATOM  19581  CB  LYS E 539     -16.312 -81.007 -52.615  1.00 30.72           C  
-ATOM  19582  CG  LYS E 539     -17.350 -81.935 -53.224  1.00 37.31           C  
-ATOM  19583  CD  LYS E 539     -16.711 -83.194 -53.804  1.00 61.99           C  
-ATOM  19584  CE  LYS E 539     -15.791 -82.879 -54.984  1.00 72.67           C  
-ATOM  19585  NZ  LYS E 539     -14.377 -82.610 -54.576  1.00 50.29           N  
-ATOM  19586  N   PRO E 540     -13.771 -81.558 -50.338  1.00 23.05           N  
-ATOM  19587  CA  PRO E 540     -12.405 -81.119 -50.036  1.00 19.53           C  
-ATOM  19588  C   PRO E 540     -11.700 -80.573 -51.272  1.00 22.02           C  
-ATOM  19589  O   PRO E 540     -11.606 -81.266 -52.284  1.00 22.52           O  
-ATOM  19590  CB  PRO E 540     -11.724 -82.396 -49.534  1.00 14.58           C  
-ATOM  19591  CG  PRO E 540     -12.533 -83.508 -50.099  1.00 21.76           C  
-ATOM  19592  CD  PRO E 540     -13.943 -83.006 -50.136  1.00 27.12           C  
-ATOM  19593  N   LYS E 541     -11.216 -79.339 -51.183  1.00 24.73           N  
-ATOM  19594  CA  LYS E 541     -10.572 -78.686 -52.315  1.00 22.35           C  
-ATOM  19595  C   LYS E 541      -9.067 -78.542 -52.120  1.00 25.72           C  
-ATOM  19596  O   LYS E 541      -8.281 -78.945 -52.980  1.00 24.97           O  
-ATOM  19597  CB  LYS E 541     -11.181 -77.305 -52.553  1.00 24.92           C  
-ATOM  19598  CG  LYS E 541     -10.539 -76.535 -53.701  1.00 33.96           C  
-ATOM  19599  CD  LYS E 541     -11.336 -76.692 -54.987  1.00 46.00           C  
-ATOM  19600  CE  LYS E 541     -10.501 -76.341 -56.208  1.00 53.77           C  
-ATOM  19601  NZ  LYS E 541      -9.476 -77.386 -56.497  1.00 48.82           N  
-ATOM  19602  N   GLU E 542      -8.665 -77.977 -50.986  1.00 28.20           N  
-ATOM  19603  CA  GLU E 542      -7.279 -77.561 -50.818  1.00 27.21           C  
-ATOM  19604  C   GLU E 542      -6.848 -77.432 -49.357  1.00 24.57           C  
-ATOM  19605  O   GLU E 542      -7.605 -76.947 -48.516  1.00 22.02           O  
-ATOM  19606  CB  GLU E 542      -7.075 -76.227 -51.535  1.00 19.83           C  
-ATOM  19607  CG  GLU E 542      -5.660 -75.955 -51.980  1.00 25.86           C  
-ATOM  19608  CD  GLU E 542      -5.550 -74.647 -52.732  1.00 39.17           C  
-ATOM  19609  OE1 GLU E 542      -4.804 -74.592 -53.733  1.00 26.78           O  
-ATOM  19610  OE2 GLU E 542      -6.215 -73.670 -52.319  1.00 43.69           O  
-ATOM  19611  N   PHE E 543      -5.629 -77.875 -49.060  1.00 18.43           N  
-ATOM  19612  CA  PHE E 543      -5.008 -77.587 -47.771  1.00 18.26           C  
-ATOM  19613  C   PHE E 543      -3.854 -76.614 -47.965  1.00 19.31           C  
-ATOM  19614  O   PHE E 543      -2.983 -76.838 -48.803  1.00 19.88           O  
-ATOM  19615  CB  PHE E 543      -4.504 -78.857 -47.087  1.00 14.12           C  
-ATOM  19616  CG  PHE E 543      -3.418 -78.601 -46.079  1.00 14.09           C  
-ATOM  19617  CD1 PHE E 543      -3.701 -77.958 -44.886  1.00 14.27           C  
-ATOM  19618  CD2 PHE E 543      -2.111 -78.987 -46.331  1.00 16.25           C  
-ATOM  19619  CE1 PHE E 543      -2.703 -77.711 -43.961  1.00 14.41           C  
-ATOM  19620  CE2 PHE E 543      -1.109 -78.743 -45.407  1.00 12.26           C  
-ATOM  19621  CZ  PHE E 543      -1.406 -78.106 -44.223  1.00 13.69           C  
-ATOM  19622  N   ILE E 544      -3.841 -75.538 -47.186  1.00 15.56           N  
-ATOM  19623  CA  ILE E 544      -2.820 -74.512 -47.349  1.00 14.03           C  
-ATOM  19624  C   ILE E 544      -1.910 -74.424 -46.129  1.00 16.57           C  
-ATOM  19625  O   ILE E 544      -2.366 -74.215 -45.006  1.00 18.43           O  
-ATOM  19626  CB  ILE E 544      -3.456 -73.142 -47.622  1.00 14.85           C  
-ATOM  19627  CG1 ILE E 544      -4.428 -73.247 -48.800  1.00 18.06           C  
-ATOM  19628  CG2 ILE E 544      -2.382 -72.104 -47.897  1.00 12.07           C  
-ATOM  19629  CD1 ILE E 544      -5.262 -72.012 -49.031  1.00 17.12           C  
-ATOM  19630  N   HIS E 545      -0.613 -74.585 -46.367  1.00 17.60           N  
-ATOM  19631  CA  HIS E 545       0.374 -74.644 -45.299  1.00 14.15           C  
-ATOM  19632  C   HIS E 545       1.165 -73.345 -45.154  1.00 16.39           C  
-ATOM  19633  O   HIS E 545       2.023 -73.027 -45.985  1.00 23.83           O  
-ATOM  19634  CB  HIS E 545       1.332 -75.808 -45.545  1.00 13.43           C  
-ATOM  19635  CG  HIS E 545       1.974 -76.331 -44.301  1.00 24.25           C  
-ATOM  19636  ND1 HIS E 545       1.824 -75.719 -43.074  1.00 26.16           N  
-ATOM  19637  CD2 HIS E 545       2.761 -77.412 -44.086  1.00 21.42           C  
-ATOM  19638  CE1 HIS E 545       2.496 -76.395 -42.162  1.00 24.23           C  
-ATOM  19639  NE2 HIS E 545       3.073 -77.429 -42.748  1.00 23.43           N  
-ATOM  19640  N   PHE E 546       0.859 -72.600 -44.094  1.00 14.86           N  
-ATOM  19641  CA  PHE E 546       1.575 -71.373 -43.752  1.00 18.40           C  
-ATOM  19642  C   PHE E 546       2.574 -71.635 -42.631  1.00 21.65           C  
-ATOM  19643  O   PHE E 546       2.202 -72.086 -41.548  1.00 26.47           O  
-ATOM  19644  CB  PHE E 546       0.602 -70.268 -43.336  1.00 20.79           C  
-ATOM  19645  CG  PHE E 546      -0.072 -69.585 -44.491  1.00 21.52           C  
-ATOM  19646  CD1 PHE E 546       0.312 -69.855 -45.794  1.00 19.17           C  
-ATOM  19647  CD2 PHE E 546      -1.078 -68.661 -44.273  1.00 18.28           C  
-ATOM  19648  CE1 PHE E 546      -0.304 -69.225 -46.856  1.00 15.37           C  
-ATOM  19649  CE2 PHE E 546      -1.696 -68.029 -45.331  1.00 18.72           C  
-ATOM  19650  CZ  PHE E 546      -1.308 -68.311 -46.624  1.00 14.46           C  
-ATOM  19651  N   MET E 547       3.842 -71.339 -42.892  1.00 21.79           N  
-ATOM  19652  CA  MET E 547       4.924 -71.735 -41.999  1.00 19.05           C  
-ATOM  19653  C   MET E 547       5.744 -70.546 -41.512  1.00 17.98           C  
-ATOM  19654  O   MET E 547       6.169 -69.704 -42.302  1.00 15.99           O  
-ATOM  19655  CB  MET E 547       5.830 -72.741 -42.707  1.00 17.62           C  
-ATOM  19656  CG  MET E 547       5.110 -73.520 -43.795  1.00 23.84           C  
-ATOM  19657  SD  MET E 547       6.131 -74.750 -44.615  1.00 28.04           S  
-ATOM  19658  CE  MET E 547       6.338 -75.926 -43.287  1.00 21.88           C  
-ATOM  19659  N   GLY E 548       5.965 -70.488 -40.202  1.00 23.16           N  
-ATOM  19660  CA  GLY E 548       6.741 -69.419 -39.600  1.00 28.17           C  
-ATOM  19661  C   GLY E 548       8.227 -69.713 -39.610  1.00 22.06           C  
-ATOM  19662  O   GLY E 548       8.894 -69.535 -40.629  1.00 23.89           O  
-ATOM  19663  N   ASN E 549       8.752 -70.161 -38.475  1.00 17.19           N  
-ATOM  19664  CA  ASN E 549      10.149 -70.559 -38.407  1.00 17.45           C  
-ATOM  19665  C   ASN E 549      10.337 -71.911 -39.083  1.00 24.80           C  
-ATOM  19666  O   ASN E 549      10.153 -72.957 -38.462  1.00 30.58           O  
-ATOM  19667  CB  ASN E 549      10.632 -70.609 -36.958  1.00 18.19           C  
-ATOM  19668  CG  ASN E 549      12.145 -70.626 -36.847  1.00 21.65           C  
-ATOM  19669  OD1 ASN E 549      12.819 -71.447 -37.467  1.00 26.45           O  
-ATOM  19670  ND2 ASN E 549      12.688 -69.706 -36.058  1.00 28.97           N  
-ATOM  19671  N   THR E 550      10.696 -71.876 -40.363  1.00 21.25           N  
-ATOM  19672  CA  THR E 550      10.835 -73.082 -41.173  1.00 21.85           C  
-ATOM  19673  C   THR E 550      12.294 -73.525 -41.232  1.00 22.96           C  
-ATOM  19674  O   THR E 550      13.142 -72.821 -41.777  1.00 25.32           O  
-ATOM  19675  CB  THR E 550      10.306 -72.849 -42.598  1.00 27.53           C  
-ATOM  19676  OG1 THR E 550       9.041 -72.180 -42.536  1.00 28.18           O  
-ATOM  19677  CG2 THR E 550      10.133 -74.161 -43.325  1.00 34.20           C  
-ATOM  19678  N   HIS E 551      12.581 -74.700 -40.681  1.00 21.60           N  
-ATOM  19679  CA  HIS E 551      13.962 -75.102 -40.440  1.00 24.96           C  
-ATOM  19680  C   HIS E 551      14.218 -76.587 -40.666  1.00 30.57           C  
-ATOM  19681  O   HIS E 551      13.307 -77.407 -40.558  1.00 41.33           O  
-ATOM  19682  CB  HIS E 551      14.349 -74.746 -39.006  1.00 23.85           C  
-ATOM  19683  CG  HIS E 551      13.523 -75.449 -37.975  1.00 25.25           C  
-ATOM  19684  ND1 HIS E 551      12.346 -74.929 -37.482  1.00 28.50           N  
-ATOM  19685  CD2 HIS E 551      13.693 -76.643 -37.359  1.00 32.38           C  
-ATOM  19686  CE1 HIS E 551      11.832 -75.766 -36.599  1.00 31.84           C  
-ATOM  19687  NE2 HIS E 551      12.630 -76.814 -36.506  1.00 35.44           N  
-ATOM  19688  N   VAL E 552      15.466 -76.928 -40.973  1.00 30.66           N  
-ATOM  19689  CA  VAL E 552      15.897 -78.321 -40.965  1.00 43.02           C  
-ATOM  19690  C   VAL E 552      17.050 -78.472 -39.969  1.00 40.44           C  
-ATOM  19691  O   VAL E 552      17.866 -77.560 -39.801  1.00 30.33           O  
-ATOM  19692  CB  VAL E 552      16.323 -78.816 -42.374  1.00 38.44           C  
-ATOM  19693  CG1 VAL E 552      15.422 -78.213 -43.442  1.00 25.80           C  
-ATOM  19694  CG2 VAL E 552      17.784 -78.493 -42.666  1.00 32.69           C  
-ATOM  19695  N   TYR E 553      17.097 -79.608 -39.282  1.00 34.50           N  
-ATOM  19696  CA  TYR E 553      18.148 -79.839 -38.300  1.00 34.12           C  
-ATOM  19697  C   TYR E 553      19.420 -80.288 -39.000  1.00 38.24           C  
-ATOM  19698  O   TYR E 553      19.371 -80.952 -40.033  1.00 42.98           O  
-ATOM  19699  CB  TYR E 553      17.705 -80.864 -37.252  1.00 38.59           C  
-ATOM  19700  CG  TYR E 553      16.695 -80.308 -36.270  1.00 46.43           C  
-ATOM  19701  CD1 TYR E 553      17.088 -79.435 -35.264  1.00 48.55           C  
-ATOM  19702  CD2 TYR E 553      15.351 -80.646 -36.356  1.00 44.47           C  
-ATOM  19703  CE1 TYR E 553      16.172 -78.913 -34.370  1.00 52.10           C  
-ATOM  19704  CE2 TYR E 553      14.426 -80.131 -35.464  1.00 44.60           C  
-ATOM  19705  CZ  TYR E 553      14.842 -79.265 -34.474  1.00 50.22           C  
-ATOM  19706  OH  TYR E 553      13.931 -78.748 -33.582  1.00 52.44           O  
-ATOM  19707  N   THR E 554      20.560 -79.904 -38.436  1.00 48.82           N  
-ATOM  19708  CA  THR E 554      21.854 -80.157 -39.058  1.00 41.27           C  
-ATOM  19709  C   THR E 554      22.198 -81.644 -39.136  1.00 45.51           C  
-ATOM  19710  O   THR E 554      23.004 -82.052 -39.971  1.00 40.97           O  
-ATOM  19711  CB  THR E 554      22.979 -79.426 -38.307  1.00 41.22           C  
-ATOM  19712  OG1 THR E 554      22.750 -79.523 -36.896  1.00 40.26           O  
-ATOM  19713  CG2 THR E 554      23.015 -77.959 -38.704  1.00 35.60           C  
-ATOM  19714  N   ASN E 555      21.589 -82.451 -38.272  1.00 44.72           N  
-ATOM  19715  CA  ASN E 555      21.808 -83.893 -38.303  1.00 44.84           C  
-ATOM  19716  C   ASN E 555      20.831 -84.596 -39.246  1.00 39.78           C  
-ATOM  19717  O   ASN E 555      20.700 -85.821 -39.221  1.00 41.31           O  
-ATOM  19718  CB  ASN E 555      21.702 -84.483 -36.893  1.00 50.97           C  
-ATOM  19719  CG  ASN E 555      20.434 -84.064 -36.174  1.00 50.67           C  
-ATOM  19720  OD1 ASN E 555      19.931 -82.960 -36.371  1.00 54.20           O  
-ATOM  19721  ND2 ASN E 555      19.913 -84.948 -35.328  1.00 42.55           N  
-ATOM  19722  N   HIS E 556      20.155 -83.809 -40.079  1.00 44.36           N  
-ATOM  19723  CA  HIS E 556      19.215 -84.335 -41.064  1.00 38.98           C  
-ATOM  19724  C   HIS E 556      19.689 -84.086 -42.488  1.00 41.36           C  
-ATOM  19725  O   HIS E 556      19.196 -84.703 -43.428  1.00 41.77           O  
-ATOM  19726  CB  HIS E 556      17.835 -83.702 -40.887  1.00 35.32           C  
-ATOM  19727  CG  HIS E 556      17.135 -84.113 -39.631  1.00 38.93           C  
-ATOM  19728  ND1 HIS E 556      15.930 -83.567 -39.243  1.00 47.55           N  
-ATOM  19729  CD2 HIS E 556      17.465 -85.016 -38.680  1.00 48.09           C  
-ATOM  19730  CE1 HIS E 556      15.550 -84.115 -38.103  1.00 63.69           C  
-ATOM  19731  NE2 HIS E 556      16.463 -84.998 -37.739  1.00 60.85           N  
-ATOM  19732  N   VAL E 557      20.645 -83.172 -42.631  1.00 32.79           N  
-ATOM  19733  CA  VAL E 557      21.024 -82.621 -43.931  1.00 37.75           C  
-ATOM  19734  C   VAL E 557      21.480 -83.673 -44.940  1.00 46.90           C  
-ATOM  19735  O   VAL E 557      21.109 -83.612 -46.114  1.00 46.36           O  
-ATOM  19736  CB  VAL E 557      22.139 -81.573 -43.776  1.00 47.97           C  
-ATOM  19737  CG1 VAL E 557      22.427 -80.910 -45.109  1.00 31.27           C  
-ATOM  19738  CG2 VAL E 557      21.740 -80.538 -42.736  1.00 48.46           C  
-ATOM  19739  N  AGLU E 558      22.283 -84.624 -44.473  0.47 50.45           N  
-ATOM  19740  N  BGLU E 558      22.292 -84.627 -44.491  0.53 51.04           N  
-ATOM  19741  CA AGLU E 558      22.756 -85.720 -45.308  0.47 46.95           C  
-ATOM  19742  CA BGLU E 558      22.753 -85.704 -45.364  0.53 48.28           C  
-ATOM  19743  C  AGLU E 558      21.582 -86.527 -45.847  0.47 46.00           C  
-ATOM  19744  C  BGLU E 558      21.577 -86.540 -45.859  0.53 47.78           C  
-ATOM  19745  O  AGLU E 558      21.473 -86.772 -47.052  0.47 43.80           O  
-ATOM  19746  O  BGLU E 558      21.462 -86.822 -47.053  0.53 45.83           O  
-ATOM  19747  CB AGLU E 558      23.696 -86.631 -44.514  0.47 48.92           C  
-ATOM  19748  CB BGLU E 558      23.763 -86.601 -44.644  0.53 48.90           C  
-ATOM  19749  CG AGLU E 558      24.733 -85.895 -43.676  0.47 49.18           C  
-ATOM  19750  CG BGLU E 558      24.251 -87.773 -45.496  0.53 50.79           C  
-ATOM  19751  CD AGLU E 558      24.310 -85.727 -42.227  0.47 49.33           C  
-ATOM  19752  CD BGLU E 558      25.093 -88.762 -44.713  0.53 48.96           C  
-ATOM  19753  OE1AGLU E 558      23.319 -85.010 -41.965  0.47 43.23           O  
-ATOM  19754  OE1BGLU E 558      25.738 -88.342 -43.730  0.53 47.15           O  
-ATOM  19755  OE2AGLU E 558      24.974 -86.318 -41.348  0.47 48.21           O  
-ATOM  19756  OE2BGLU E 558      25.105 -89.959 -45.077  0.53 37.32           O  
-ATOM  19757  N   ALA E 559      20.705 -86.925 -44.933  1.00 44.36           N  
-ATOM  19758  CA  ALA E 559      19.536 -87.730 -45.258  1.00 47.38           C  
-ATOM  19759  C   ALA E 559      18.588 -87.011 -46.212  1.00 47.27           C  
-ATOM  19760  O   ALA E 559      17.995 -87.635 -47.085  1.00 45.31           O  
-ATOM  19761  CB  ALA E 559      18.805 -88.121 -43.982  1.00 39.88           C  
-ATOM  19762  N   LEU E 560      18.449 -85.701 -46.040  1.00 41.62           N  
-ATOM  19763  CA  LEU E 560      17.583 -84.911 -46.905  1.00 36.45           C  
-ATOM  19764  C   LEU E 560      18.196 -84.797 -48.290  1.00 33.82           C  
-ATOM  19765  O   LEU E 560      17.495 -84.884 -49.299  1.00 31.57           O  
-ATOM  19766  CB  LEU E 560      17.341 -83.525 -46.307  1.00 28.36           C  
-ATOM  19767  CG  LEU E 560      16.632 -83.537 -44.951  1.00 31.14           C  
-ATOM  19768  CD1 LEU E 560      16.403 -82.123 -44.433  1.00 36.70           C  
-ATOM  19769  CD2 LEU E 560      15.325 -84.308 -45.037  1.00 29.28           C  
-ATOM  19770  N   LYS E 561      19.511 -84.601 -48.324  1.00 33.53           N  
-ATOM  19771  CA  LYS E 561      20.262 -84.591 -49.572  1.00 35.76           C  
-ATOM  19772  C   LYS E 561      20.052 -85.900 -50.323  1.00 46.03           C  
-ATOM  19773  O   LYS E 561      19.918 -85.911 -51.548  1.00 37.72           O  
-ATOM  19774  CB  LYS E 561      21.752 -84.367 -49.304  1.00 46.96           C  
-ATOM  19775  CG  LYS E 561      22.129 -82.926 -49.005  1.00 43.13           C  
-ATOM  19776  CD  LYS E 561      23.559 -82.832 -48.490  1.00 48.18           C  
-ATOM  19777  CE  LYS E 561      24.009 -81.385 -48.370  1.00 49.83           C  
-ATOM  19778  NZ  LYS E 561      24.106 -80.728 -49.703  1.00 42.30           N  
-ATOM  19779  N   GLU E 562      20.036 -87.001 -49.576  1.00 49.73           N  
-ATOM  19780  CA  GLU E 562      19.715 -88.306 -50.139  1.00 42.72           C  
-ATOM  19781  C   GLU E 562      18.296 -88.297 -50.704  1.00 40.83           C  
-ATOM  19782  O   GLU E 562      18.068 -88.687 -51.848  1.00 36.38           O  
-ATOM  19783  CB  GLU E 562      19.858 -89.400 -49.077  1.00 44.21           C  
-ATOM  19784  CG  GLU E 562      21.294 -89.810 -48.765  1.00 61.93           C  
-ATOM  19785  CD  GLU E 562      21.707 -91.089 -49.475  1.00 62.33           C  
-ATOM  19786  OE1 GLU E 562      21.714 -91.104 -50.725  1.00 58.57           O  
-ATOM  19787  OE2 GLU E 562      22.019 -92.081 -48.780  1.00 55.97           O  
-ATOM  19788  N   GLN E 563      17.359 -87.823 -49.888  1.00 38.55           N  
-ATOM  19789  CA  GLN E 563      15.935 -87.804 -50.208  1.00 31.23           C  
-ATOM  19790  C   GLN E 563      15.629 -87.022 -51.483  1.00 29.06           C  
-ATOM  19791  O   GLN E 563      14.689 -87.346 -52.207  1.00 23.63           O  
-ATOM  19792  CB  GLN E 563      15.154 -87.219 -49.024  1.00 24.26           C  
-ATOM  19793  CG  GLN E 563      13.634 -87.329 -49.119  1.00 16.78           C  
-ATOM  19794  CD  GLN E 563      12.951 -86.982 -47.804  1.00 22.92           C  
-ATOM  19795  OE1 GLN E 563      13.555 -87.080 -46.735  1.00 35.63           O  
-ATOM  19796  NE2 GLN E 563      11.693 -86.569 -47.876  1.00 16.44           N  
-ATOM  19797  N   LEU E 564      16.429 -85.999 -51.761  1.00 28.88           N  
-ATOM  19798  CA  LEU E 564      16.182 -85.149 -52.918  1.00 26.44           C  
-ATOM  19799  C   LEU E 564      16.550 -85.819 -54.239  1.00 25.10           C  
-ATOM  19800  O   LEU E 564      16.199 -85.321 -55.307  1.00 25.15           O  
-ATOM  19801  CB  LEU E 564      16.944 -83.830 -52.784  1.00 32.76           C  
-ATOM  19802  CG  LEU E 564      16.527 -82.925 -51.625  1.00 28.72           C  
-ATOM  19803  CD1 LEU E 564      17.240 -81.580 -51.705  1.00 31.25           C  
-ATOM  19804  CD2 LEU E 564      15.019 -82.740 -51.600  1.00 27.74           C  
-ATOM  19805  N   ARG E 565      17.259 -86.942 -54.172  1.00 34.02           N  
-ATOM  19806  CA  ARG E 565      17.631 -87.667 -55.385  1.00 39.08           C  
-ATOM  19807  C   ARG E 565      16.473 -88.524 -55.880  1.00 26.07           C  
-ATOM  19808  O   ARG E 565      16.504 -89.053 -56.992  1.00 17.33           O  
-ATOM  19809  CB  ARG E 565      18.864 -88.539 -55.142  1.00 41.59           C  
-ATOM  19810  CG  ARG E 565      20.126 -87.749 -54.862  1.00 50.33           C  
-ATOM  19811  CD  ARG E 565      21.326 -88.659 -54.668  1.00 54.66           C  
-ATOM  19812  NE  ARG E 565      22.011 -88.377 -53.409  1.00 72.67           N  
-ATOM  19813  CZ  ARG E 565      22.903 -87.405 -53.240  1.00 72.51           C  
-ATOM  19814  NH1 ARG E 565      23.226 -86.611 -54.254  1.00 55.10           N  
-ATOM  19815  NH2 ARG E 565      23.471 -87.225 -52.055  1.00 55.34           N  
-ATOM  19816  N   ARG E 566      15.453 -88.653 -55.040  1.00 25.79           N  
-ATOM  19817  CA  ARG E 566      14.273 -89.436 -55.371  1.00 19.83           C  
-ATOM  19818  C   ARG E 566      13.206 -88.565 -56.022  1.00 24.29           C  
-ATOM  19819  O   ARG E 566      12.840 -87.520 -55.487  1.00 35.52           O  
-ATOM  19820  CB  ARG E 566      13.701 -90.098 -54.113  1.00 17.36           C  
-ATOM  19821  CG  ARG E 566      14.713 -90.866 -53.272  1.00 21.21           C  
-ATOM  19822  CD  ARG E 566      14.100 -91.295 -51.946  1.00 22.61           C  
-ATOM  19823  NE  ARG E 566      14.940 -92.233 -51.204  1.00 24.13           N  
-ATOM  19824  CZ  ARG E 566      14.622 -92.730 -50.011  1.00 30.70           C  
-ATOM  19825  NH1 ARG E 566      15.435 -93.581 -49.400  1.00 30.92           N  
-ATOM  19826  NH2 ARG E 566      13.488 -92.374 -49.427  1.00 34.12           N  
-ATOM  19827  N   GLU E 567      12.709 -88.992 -57.177  1.00 20.27           N  
-ATOM  19828  CA  GLU E 567      11.550 -88.345 -57.777  1.00 26.04           C  
-ATOM  19829  C   GLU E 567      10.281 -88.895 -57.136  1.00 21.84           C  
-ATOM  19830  O   GLU E 567      10.221 -90.072 -56.789  1.00 27.06           O  
-ATOM  19831  CB  GLU E 567      11.525 -88.551 -59.292  1.00 27.77           C  
-ATOM  19832  CG  GLU E 567      11.864 -89.959 -59.726  1.00 30.97           C  
-ATOM  19833  CD  GLU E 567      13.341 -90.142 -59.975  1.00 33.90           C  
-ATOM  19834  OE1 GLU E 567      13.972 -89.195 -60.487  1.00 29.49           O  
-ATOM  19835  OE2 GLU E 567      13.873 -91.224 -59.652  1.00 54.01           O  
-ATOM  19836  N   PRO E 568       9.260 -88.041 -56.971  1.00 21.08           N  
-ATOM  19837  CA  PRO E 568       8.041 -88.444 -56.263  1.00 19.76           C  
-ATOM  19838  C   PRO E 568       7.241 -89.497 -57.018  1.00 17.24           C  
-ATOM  19839  O   PRO E 568       7.498 -89.755 -58.194  1.00 22.07           O  
-ATOM  19840  CB  PRO E 568       7.237 -87.139 -56.160  1.00 20.40           C  
-ATOM  19841  CG  PRO E 568       8.199 -86.043 -56.493  1.00 23.96           C  
-ATOM  19842  CD  PRO E 568       9.189 -86.646 -57.432  1.00 23.07           C  
-ATOM  19843  N   ARG E 569       6.278 -90.095 -56.328  1.00 15.92           N  
-ATOM  19844  CA  ARG E 569       5.360 -91.047 -56.936  1.00 16.70           C  
-ATOM  19845  C   ARG E 569       3.952 -90.467 -56.865  1.00 19.15           C  
-ATOM  19846  O   ARG E 569       3.726 -89.504 -56.131  1.00 24.03           O  
-ATOM  19847  CB  ARG E 569       5.448 -92.401 -56.229  1.00 15.65           C  
-ATOM  19848  CG  ARG E 569       6.845 -92.993 -56.237  1.00 17.98           C  
-ATOM  19849  CD  ARG E 569       6.869 -94.380 -56.851  1.00 16.72           C  
-ATOM  19850  NE  ARG E 569       8.234 -94.883 -56.978  1.00 24.39           N  
-ATOM  19851  CZ  ARG E 569       8.876 -95.557 -56.029  1.00 21.03           C  
-ATOM  19852  NH1 ARG E 569      10.117 -95.973 -56.235  1.00 18.28           N  
-ATOM  19853  NH2 ARG E 569       8.280 -95.819 -54.874  1.00 17.87           N  
-ATOM  19854  N   PRO E 570       3.007 -91.020 -57.647  1.00 16.51           N  
-ATOM  19855  CA  PRO E 570       1.633 -90.513 -57.570  1.00 16.46           C  
-ATOM  19856  C   PRO E 570       1.063 -90.559 -56.154  1.00 17.20           C  
-ATOM  19857  O   PRO E 570       1.259 -91.540 -55.433  1.00 15.93           O  
-ATOM  19858  CB  PRO E 570       0.853 -91.451 -58.507  1.00 11.03           C  
-ATOM  19859  CG  PRO E 570       1.777 -92.588 -58.813  1.00 12.02           C  
-ATOM  19860  CD  PRO E 570       3.153 -92.023 -58.713  1.00 13.45           C  
-ATOM  19861  N   PHE E 571       0.391 -89.483 -55.760  1.00 14.56           N  
-ATOM  19862  CA  PHE E 571      -0.266 -89.424 -54.465  1.00 12.53           C  
-ATOM  19863  C   PHE E 571      -1.341 -90.496 -54.379  1.00 16.29           C  
-ATOM  19864  O   PHE E 571      -1.966 -90.833 -55.384  1.00 20.39           O  
-ATOM  19865  CB  PHE E 571      -0.875 -88.041 -54.231  1.00 17.45           C  
-ATOM  19866  CG  PHE E 571       0.116 -87.010 -53.774  1.00 21.67           C  
-ATOM  19867  CD1 PHE E 571       1.240 -87.381 -53.054  1.00 21.09           C  
-ATOM  19868  CD2 PHE E 571      -0.078 -85.667 -54.063  1.00 25.89           C  
-ATOM  19869  CE1 PHE E 571       2.154 -86.432 -52.631  1.00 24.67           C  
-ATOM  19870  CE2 PHE E 571       0.830 -84.715 -53.643  1.00 24.08           C  
-ATOM  19871  CZ  PHE E 571       1.949 -85.098 -52.926  1.00 23.79           C  
-ATOM  19872  N   PRO E 572      -1.547 -91.054 -53.178  1.00 16.21           N  
-ATOM  19873  CA  PRO E 572      -2.613 -92.038 -52.981  1.00 19.23           C  
-ATOM  19874  C   PRO E 572      -3.973 -91.377 -52.780  1.00 23.38           C  
-ATOM  19875  O   PRO E 572      -4.077 -90.149 -52.783  1.00 20.83           O  
-ATOM  19876  CB  PRO E 572      -2.174 -92.770 -51.715  1.00 20.09           C  
-ATOM  19877  CG  PRO E 572      -1.449 -91.725 -50.936  1.00 18.27           C  
-ATOM  19878  CD  PRO E 572      -0.745 -90.863 -51.956  1.00 19.94           C  
-ATOM  19879  N   ILE E 573      -5.005 -92.196 -52.613  1.00 19.81           N  
-ATOM  19880  CA  ILE E 573      -6.346 -91.712 -52.325  1.00 19.45           C  
-ATOM  19881  C   ILE E 573      -6.761 -92.161 -50.935  1.00 23.07           C  
-ATOM  19882  O   ILE E 573      -6.703 -93.348 -50.624  1.00 23.33           O  
-ATOM  19883  CB  ILE E 573      -7.376 -92.230 -53.346  1.00 19.01           C  
-ATOM  19884  CG1 ILE E 573      -7.163 -91.576 -54.710  1.00 23.23           C  
-ATOM  19885  CG2 ILE E 573      -8.790 -91.966 -52.857  1.00 21.63           C  
-ATOM  19886  CD1 ILE E 573      -8.218 -91.947 -55.727  1.00 13.88           C  
-ATOM  19887  N   VAL E 574      -7.171 -91.215 -50.096  1.00 28.61           N  
-ATOM  19888  CA  VAL E 574      -7.676 -91.558 -48.772  1.00 26.03           C  
-ATOM  19889  C   VAL E 574      -9.198 -91.608 -48.791  1.00 21.35           C  
-ATOM  19890  O   VAL E 574      -9.859 -90.586 -48.961  1.00 24.71           O  
-ATOM  19891  CB  VAL E 574      -7.206 -90.562 -47.698  1.00 21.33           C  
-ATOM  19892  CG1 VAL E 574      -7.934 -90.821 -46.390  1.00 25.85           C  
-ATOM  19893  CG2 VAL E 574      -5.703 -90.667 -47.503  1.00 15.50           C  
-ATOM  19894  N   ASN E 575      -9.744 -92.809 -48.627  1.00 24.87           N  
-ATOM  19895  CA  ASN E 575     -11.187 -93.004 -48.654  1.00 19.60           C  
-ATOM  19896  C   ASN E 575     -11.774 -93.148 -47.261  1.00 19.15           C  
-ATOM  19897  O   ASN E 575     -11.220 -93.846 -46.407  1.00 21.93           O  
-ATOM  19898  CB  ASN E 575     -11.548 -94.236 -49.488  1.00 18.93           C  
-ATOM  19899  CG  ASN E 575     -11.355 -94.012 -50.971  1.00 19.83           C  
-ATOM  19900  OD1 ASN E 575     -10.808 -94.863 -51.672  1.00 23.45           O  
-ATOM  19901  ND2 ASN E 575     -11.801 -92.860 -51.459  1.00 16.47           N  
-ATOM  19902  N   ILE E 576     -12.898 -92.477 -47.038  1.00 17.13           N  
-ATOM  19903  CA  ILE E 576     -13.636 -92.628 -45.796  1.00 19.04           C  
-ATOM  19904  C   ILE E 576     -14.644 -93.757 -45.943  1.00 19.67           C  
-ATOM  19905  O   ILE E 576     -15.527 -93.711 -46.799  1.00 20.46           O  
-ATOM  19906  CB  ILE E 576     -14.369 -91.338 -45.389  1.00 17.86           C  
-ATOM  19907  CG1 ILE E 576     -13.368 -90.211 -45.134  1.00 18.88           C  
-ATOM  19908  CG2 ILE E 576     -15.215 -91.583 -44.148  1.00 19.05           C  
-ATOM  19909  CD1 ILE E 576     -14.007 -88.930 -44.646  1.00 18.14           C  
-ATOM  19910  N   LEU E 577     -14.497 -94.778 -45.110  1.00 20.81           N  
-ATOM  19911  CA  LEU E 577     -15.401 -95.914 -45.134  1.00 19.58           C  
-ATOM  19912  C   LEU E 577     -16.583 -95.648 -44.210  1.00 26.50           C  
-ATOM  19913  O   LEU E 577     -16.484 -94.825 -43.297  1.00 28.74           O  
-ATOM  19914  CB  LEU E 577     -14.669 -97.188 -44.712  1.00 20.25           C  
-ATOM  19915  CG  LEU E 577     -13.255 -97.356 -45.270  1.00 19.08           C  
-ATOM  19916  CD1 LEU E 577     -12.535 -98.514 -44.594  1.00 24.48           C  
-ATOM  19917  CD2 LEU E 577     -13.295 -97.552 -46.774  1.00 18.36           C  
-ATOM  19918  N   ASN E 578     -17.695 -96.337 -44.459  1.00 27.05           N  
-ATOM  19919  CA  ASN E 578     -18.872 -96.271 -43.593  1.00 25.98           C  
-ATOM  19920  C   ASN E 578     -19.452 -94.865 -43.454  1.00 30.48           C  
-ATOM  19921  O   ASN E 578     -19.905 -94.471 -42.375  1.00 28.29           O  
-ATOM  19922  CB  ASN E 578     -18.531 -96.819 -42.209  1.00 18.44           C  
-ATOM  19923  CG  ASN E 578     -17.658 -98.052 -42.274  1.00 17.02           C  
-ATOM  19924  OD1 ASN E 578     -17.824 -98.906 -43.147  1.00 22.71           O  
-ATOM  19925  ND2 ASN E 578     -16.712 -98.149 -41.349  1.00 15.15           N  
-ATOM  19926  N   LYS E 579     -19.445 -94.121 -44.556  1.00 31.47           N  
-ATOM  19927  CA  LYS E 579     -19.931 -92.747 -44.565  1.00 26.10           C  
-ATOM  19928  C   LYS E 579     -21.328 -92.609 -43.972  1.00 28.35           C  
-ATOM  19929  O   LYS E 579     -21.584 -91.682 -43.205  1.00 34.75           O  
-ATOM  19930  CB  LYS E 579     -19.929 -92.190 -45.988  1.00 29.13           C  
-ATOM  19931  CG  LYS E 579     -18.554 -91.851 -46.525  1.00 25.00           C  
-ATOM  19932  CD  LYS E 579     -18.643 -90.753 -47.572  1.00 25.76           C  
-ATOM  19933  CE  LYS E 579     -17.272 -90.187 -47.896  1.00 21.42           C  
-ATOM  19934  NZ  LYS E 579     -17.393 -88.916 -48.661  1.00 33.96           N  
-ATOM  19935  N   GLU E 580     -22.217 -93.535 -44.329  1.00 31.35           N  
-ATOM  19936  CA  GLU E 580     -23.606 -93.515 -43.872  1.00 29.62           C  
-ATOM  19937  C   GLU E 580     -23.707 -93.528 -42.349  1.00 32.60           C  
-ATOM  19938  O   GLU E 580     -24.661 -93.000 -41.780  1.00 33.95           O  
-ATOM  19939  CB  GLU E 580     -24.380 -94.702 -44.456  1.00 28.67           C  
-ATOM  19940  CG  GLU E 580     -23.608 -95.505 -45.497  1.00 39.22           C  
-ATOM  19941  CD  GLU E 580     -22.654 -96.521 -44.876  1.00 52.97           C  
-ATOM  19942  OE1 GLU E 580     -22.873 -96.915 -43.709  1.00 46.82           O  
-ATOM  19943  OE2 GLU E 580     -21.687 -96.929 -45.556  1.00 41.94           O  
-ATOM  19944  N   ARG E 581     -22.716 -94.124 -41.694  1.00 29.94           N  
-ATOM  19945  CA  ARG E 581     -22.707 -94.196 -40.238  1.00 23.27           C  
-ATOM  19946  C   ARG E 581     -22.182 -92.908 -39.624  1.00 20.26           C  
-ATOM  19947  O   ARG E 581     -22.543 -92.548 -38.505  1.00 25.40           O  
-ATOM  19948  CB  ARG E 581     -21.854 -95.372 -39.757  1.00 20.53           C  
-ATOM  19949  CG  ARG E 581     -22.116 -95.774 -38.319  1.00 15.12           C  
-ATOM  19950  CD  ARG E 581     -20.991 -96.623 -37.755  1.00 22.65           C  
-ATOM  19951  NE  ARG E 581     -19.829 -95.817 -37.390  1.00 26.93           N  
-ATOM  19952  CZ  ARG E 581     -18.621 -95.950 -37.928  1.00 20.50           C  
-ATOM  19953  NH1 ARG E 581     -17.627 -95.169 -37.527  1.00 16.68           N  
-ATOM  19954  NH2 ARG E 581     -18.407 -96.864 -38.863  1.00 30.90           N  
-ATOM  19955  N   ILE E 582     -21.327 -92.217 -40.368  1.00 23.84           N  
-ATOM  19956  CA  ILE E 582     -20.622 -91.057 -39.844  1.00 22.40           C  
-ATOM  19957  C   ILE E 582     -21.361 -89.759 -40.150  1.00 29.01           C  
-ATOM  19958  O   ILE E 582     -21.519 -89.380 -41.311  1.00 30.59           O  
-ATOM  19959  CB  ILE E 582     -19.197 -90.991 -40.412  1.00 20.11           C  
-ATOM  19960  CG1 ILE E 582     -18.429 -92.264 -40.042  1.00 24.05           C  
-ATOM  19961  CG2 ILE E 582     -18.479 -89.758 -39.900  1.00 19.69           C  
-ATOM  19962  CD1 ILE E 582     -17.137 -92.453 -40.799  1.00 25.62           C  
-ATOM  19963  N   LYS E 583     -21.821 -89.085 -39.099  1.00 27.75           N  
-ATOM  19964  CA  LYS E 583     -22.590 -87.855 -39.253  1.00 21.23           C  
-ATOM  19965  C   LYS E 583     -21.974 -86.692 -38.484  1.00 26.34           C  
-ATOM  19966  O   LYS E 583     -22.208 -85.528 -38.810  1.00 31.03           O  
-ATOM  19967  CB  LYS E 583     -24.032 -88.076 -38.801  1.00 24.07           C  
-ATOM  19968  CG  LYS E 583     -24.877 -88.831 -39.811  1.00 34.03           C  
-ATOM  19969  CD  LYS E 583     -26.127 -89.415 -39.178  1.00 39.77           C  
-ATOM  19970  CE  LYS E 583     -27.079 -89.919 -40.247  1.00 70.95           C  
-ATOM  19971  NZ  LYS E 583     -26.344 -90.567 -41.373  1.00 51.37           N  
-ATOM  19972  N   GLU E 584     -21.186 -87.009 -37.461  1.00 29.23           N  
-ATOM  19973  CA  GLU E 584     -20.506 -85.980 -36.685  1.00 32.97           C  
-ATOM  19974  C   GLU E 584     -19.007 -86.250 -36.618  1.00 25.61           C  
-ATOM  19975  O   GLU E 584     -18.556 -87.356 -36.907  1.00 22.41           O  
-ATOM  19976  CB  GLU E 584     -21.100 -85.890 -35.276  1.00 32.01           C  
-ATOM  19977  CG  GLU E 584     -22.621 -85.759 -35.240  1.00 35.75           C  
-ATOM  19978  CD  GLU E 584     -23.129 -84.413 -35.740  1.00 33.47           C  
-ATOM  19979  OE1 GLU E 584     -22.305 -83.525 -36.050  1.00 31.75           O  
-ATOM  19980  OE2 GLU E 584     -24.364 -84.241 -35.816  1.00 31.84           O  
-ATOM  19981  N   ILE E 585     -18.243 -85.235 -36.230  1.00 30.90           N  
-ATOM  19982  CA  ILE E 585     -16.788 -85.324 -36.223  1.00 23.50           C  
-ATOM  19983  C   ILE E 585     -16.284 -86.382 -35.240  1.00 20.12           C  
-ATOM  19984  O   ILE E 585     -15.223 -86.974 -35.439  1.00 17.27           O  
-ATOM  19985  CB  ILE E 585     -16.153 -83.952 -35.885  1.00 20.85           C  
-ATOM  19986  CG1 ILE E 585     -14.629 -83.991 -36.052  1.00 21.40           C  
-ATOM  19987  CG2 ILE E 585     -16.560 -83.490 -34.488  1.00 22.54           C  
-ATOM  19988  CD1 ILE E 585     -14.177 -84.212 -37.481  1.00 19.78           C  
-ATOM  19989  N   ASP E 586     -17.063 -86.637 -34.195  1.00 23.84           N  
-ATOM  19990  CA  ASP E 586     -16.668 -87.592 -33.169  1.00 22.48           C  
-ATOM  19991  C   ASP E 586     -17.017 -89.025 -33.553  1.00 26.41           C  
-ATOM  19992  O   ASP E 586     -16.589 -89.972 -32.893  1.00 32.09           O  
-ATOM  19993  CB  ASP E 586     -17.325 -87.240 -31.833  1.00 23.09           C  
-ATOM  19994  CG  ASP E 586     -16.946 -85.858 -31.345  1.00 31.54           C  
-ATOM  19995  OD1 ASP E 586     -15.771 -85.665 -30.963  1.00 28.37           O  
-ATOM  19996  OD2 ASP E 586     -17.825 -84.968 -31.340  1.00 29.30           O  
-ATOM  19997  N   ASP E 587     -17.791 -89.180 -34.623  1.00 24.52           N  
-ATOM  19998  CA  ASP E 587     -18.243 -90.502 -35.049  1.00 28.55           C  
-ATOM  19999  C   ASP E 587     -17.130 -91.326 -35.697  1.00 26.67           C  
-ATOM  20000  O   ASP E 587     -17.207 -92.553 -35.740  1.00 27.13           O  
-ATOM  20001  CB  ASP E 587     -19.427 -90.378 -36.015  1.00 28.27           C  
-ATOM  20002  CG  ASP E 587     -20.701 -89.921 -35.321  1.00 37.05           C  
-ATOM  20003  OD1 ASP E 587     -20.714 -89.872 -34.072  1.00 45.62           O  
-ATOM  20004  OD2 ASP E 587     -21.694 -89.623 -36.020  1.00 28.57           O  
-ATOM  20005  N   PHE E 588     -16.099 -90.650 -36.196  1.00 23.19           N  
-ATOM  20006  CA  PHE E 588     -14.973 -91.325 -36.834  1.00 18.69           C  
-ATOM  20007  C   PHE E 588     -14.240 -92.270 -35.887  1.00 19.06           C  
-ATOM  20008  O   PHE E 588     -14.124 -92.002 -34.692  1.00 19.58           O  
-ATOM  20009  CB  PHE E 588     -13.980 -90.303 -37.385  1.00 19.50           C  
-ATOM  20010  CG  PHE E 588     -14.438 -89.618 -38.638  1.00 20.93           C  
-ATOM  20011  CD1 PHE E 588     -14.187 -90.178 -39.880  1.00 17.97           C  
-ATOM  20012  CD2 PHE E 588     -15.100 -88.403 -38.578  1.00 19.34           C  
-ATOM  20013  CE1 PHE E 588     -14.598 -89.545 -41.038  1.00 15.32           C  
-ATOM  20014  CE2 PHE E 588     -15.510 -87.765 -39.732  1.00 18.34           C  
-ATOM  20015  CZ  PHE E 588     -15.260 -88.337 -40.964  1.00 13.77           C  
-ATOM  20016  N   THR E 589     -13.749 -93.380 -36.429  1.00 21.06           N  
-ATOM  20017  CA  THR E 589     -12.891 -94.288 -35.675  1.00 20.28           C  
-ATOM  20018  C   THR E 589     -11.625 -94.579 -36.471  1.00 25.48           C  
-ATOM  20019  O   THR E 589     -11.419 -94.016 -37.548  1.00 29.20           O  
-ATOM  20020  CB  THR E 589     -13.592 -95.612 -35.342  1.00 21.43           C  
-ATOM  20021  OG1 THR E 589     -13.776 -96.369 -36.543  1.00 25.91           O  
-ATOM  20022  CG2 THR E 589     -14.941 -95.357 -34.684  1.00 23.80           C  
-ATOM  20023  N   ALA E 590     -10.786 -95.465 -35.945  1.00 20.14           N  
-ATOM  20024  CA  ALA E 590      -9.500 -95.761 -36.566  1.00 17.85           C  
-ATOM  20025  C   ALA E 590      -9.642 -96.637 -37.811  1.00 29.42           C  
-ATOM  20026  O   ALA E 590      -8.760 -96.657 -38.669  1.00 28.16           O  
-ATOM  20027  CB  ALA E 590      -8.578 -96.425 -35.562  1.00 20.78           C  
-ATOM  20028  N   GLU E 591     -10.757 -97.355 -37.907  1.00 32.01           N  
-ATOM  20029  CA  GLU E 591     -10.972 -98.291 -39.006  1.00 25.01           C  
-ATOM  20030  C   GLU E 591     -11.860 -97.718 -40.100  1.00 21.64           C  
-ATOM  20031  O   GLU E 591     -12.288 -98.438 -41.001  1.00 29.91           O  
-ATOM  20032  CB  GLU E 591     -11.584 -99.594 -38.483  1.00 23.73           C  
-ATOM  20033  CG  GLU E 591     -10.584-100.539 -37.850  1.00 33.59           C  
-ATOM  20034  CD  GLU E 591     -10.042-100.019 -36.539  1.00 40.65           C  
-ATOM  20035  OE1 GLU E 591      -8.893-100.366 -36.190  1.00 36.98           O  
-ATOM  20036  OE2 GLU E 591     -10.770 -99.265 -35.856  1.00 44.21           O  
-ATOM  20037  N   ASP E 592     -12.133 -96.424 -40.024  1.00 16.58           N  
-ATOM  20038  CA  ASP E 592     -13.052 -95.804 -40.966  1.00 22.48           C  
-ATOM  20039  C   ASP E 592     -12.327 -95.169 -42.145  1.00 23.19           C  
-ATOM  20040  O   ASP E 592     -12.899 -94.351 -42.867  1.00 21.33           O  
-ATOM  20041  CB  ASP E 592     -13.912 -94.762 -40.253  1.00 26.70           C  
-ATOM  20042  CG  ASP E 592     -14.884 -95.388 -39.277  1.00 24.75           C  
-ATOM  20043  OD1 ASP E 592     -15.480 -96.432 -39.617  1.00 22.88           O  
-ATOM  20044  OD2 ASP E 592     -15.048 -94.839 -38.169  1.00 27.09           O  
-ATOM  20045  N   PHE E 593     -11.072 -95.553 -42.345  1.00 30.69           N  
-ATOM  20046  CA  PHE E 593     -10.275 -94.976 -43.421  1.00 27.46           C  
-ATOM  20047  C   PHE E 593      -9.589 -96.036 -44.271  1.00 18.29           C  
-ATOM  20048  O   PHE E 593      -9.502 -97.202 -43.885  1.00 19.26           O  
-ATOM  20049  CB  PHE E 593      -9.239 -94.011 -42.848  1.00 23.49           C  
-ATOM  20050  CG  PHE E 593      -9.843 -92.802 -42.204  1.00 17.72           C  
-ATOM  20051  CD1 PHE E 593     -10.077 -91.657 -42.942  1.00 17.33           C  
-ATOM  20052  CD2 PHE E 593     -10.198 -92.817 -40.866  1.00 18.05           C  
-ATOM  20053  CE1 PHE E 593     -10.644 -90.544 -42.356  1.00 24.71           C  
-ATOM  20054  CE2 PHE E 593     -10.765 -91.707 -40.274  1.00 21.87           C  
-ATOM  20055  CZ  PHE E 593     -10.986 -90.567 -41.020  1.00 19.23           C  
-ATOM  20056  N   GLU E 594      -9.108 -95.618 -45.436  1.00 19.16           N  
-ATOM  20057  CA  GLU E 594      -8.478 -96.534 -46.372  1.00 20.13           C  
-ATOM  20058  C   GLU E 594      -7.506 -95.803 -47.295  1.00 23.59           C  
-ATOM  20059  O   GLU E 594      -7.922 -95.018 -48.146  1.00 23.09           O  
-ATOM  20060  CB  GLU E 594      -9.546 -97.257 -47.196  1.00 26.46           C  
-ATOM  20061  CG  GLU E 594      -8.999 -98.317 -48.134  1.00 30.66           C  
-ATOM  20062  CD  GLU E 594      -9.991 -98.705 -49.214  1.00 42.74           C  
-ATOM  20063  OE1 GLU E 594     -10.544 -97.794 -49.869  1.00 41.67           O  
-ATOM  20064  OE2 GLU E 594     -10.221 -99.918 -49.407  1.00 52.69           O  
-ATOM  20065  N   VAL E 595      -6.212 -96.054 -47.123  1.00 22.07           N  
-ATOM  20066  CA  VAL E 595      -5.214 -95.478 -48.016  1.00 14.61           C  
-ATOM  20067  C   VAL E 595      -5.049 -96.373 -49.234  1.00 17.77           C  
-ATOM  20068  O   VAL E 595      -4.820 -97.574 -49.105  1.00 19.66           O  
-ATOM  20069  CB  VAL E 595      -3.855 -95.293 -47.328  1.00 13.96           C  
-ATOM  20070  CG1 VAL E 595      -2.854 -94.700 -48.302  1.00 16.32           C  
-ATOM  20071  CG2 VAL E 595      -4.001 -94.403 -46.118  1.00 17.19           C  
-ATOM  20072  N   VAL E 596      -5.163 -95.780 -50.416  1.00 21.03           N  
-ATOM  20073  CA  VAL E 596      -5.242 -96.546 -51.653  1.00 19.79           C  
-ATOM  20074  C   VAL E 596      -4.254 -96.060 -52.712  1.00 24.99           C  
-ATOM  20075  O   VAL E 596      -4.338 -94.926 -53.181  1.00 19.53           O  
-ATOM  20076  CB  VAL E 596      -6.666 -96.490 -52.240  1.00 17.75           C  
-ATOM  20077  CG1 VAL E 596      -6.721 -97.233 -53.542  1.00 15.53           C  
-ATOM  20078  CG2 VAL E 596      -7.670 -97.063 -51.256  1.00 22.54           C  
-ATOM  20079  N   GLY E 597      -3.323 -96.927 -53.093  1.00 20.67           N  
-ATOM  20080  CA  GLY E 597      -2.350 -96.590 -54.116  1.00 15.85           C  
-ATOM  20081  C   GLY E 597      -1.136 -95.869 -53.565  1.00 17.91           C  
-ATOM  20082  O   GLY E 597      -0.472 -95.117 -54.277  1.00 17.68           O  
-ATOM  20083  N   TYR E 598      -0.842 -96.092 -52.289  1.00 19.55           N  
-ATOM  20084  CA  TYR E 598       0.344 -95.504 -51.684  1.00 18.76           C  
-ATOM  20085  C   TYR E 598       1.574 -96.306 -52.075  1.00 18.19           C  
-ATOM  20086  O   TYR E 598       1.761 -97.429 -51.608  1.00 14.85           O  
-ATOM  20087  CB  TYR E 598       0.216 -95.452 -50.160  1.00 20.21           C  
-ATOM  20088  CG  TYR E 598       1.213 -94.530 -49.493  1.00 15.15           C  
-ATOM  20089  CD1 TYR E 598       1.674 -93.392 -50.141  1.00 22.64           C  
-ATOM  20090  CD2 TYR E 598       1.700 -94.801 -48.221  1.00 14.38           C  
-ATOM  20091  CE1 TYR E 598       2.586 -92.544 -49.538  1.00 20.16           C  
-ATOM  20092  CE2 TYR E 598       2.614 -93.961 -47.611  1.00 16.90           C  
-ATOM  20093  CZ  TYR E 598       3.052 -92.834 -48.275  1.00 16.96           C  
-ATOM  20094  OH  TYR E 598       3.958 -91.990 -47.679  1.00 17.71           O  
-ATOM  20095  N   VAL E 599       2.402 -95.732 -52.944  1.00 21.39           N  
-ATOM  20096  CA  VAL E 599       3.655 -96.365 -53.343  1.00 18.29           C  
-ATOM  20097  C   VAL E 599       4.836 -95.445 -53.044  1.00 16.30           C  
-ATOM  20098  O   VAL E 599       5.363 -94.801 -53.949  1.00 21.17           O  
-ATOM  20099  CB  VAL E 599       3.666 -96.721 -54.845  1.00 16.65           C  
-ATOM  20100  CG1 VAL E 599       4.765 -97.728 -55.142  1.00 18.32           C  
-ATOM  20101  CG2 VAL E 599       2.315 -97.269 -55.276  1.00 20.71           C  
-ATOM  20102  N   PRO E 600       5.251 -95.373 -51.769  1.00 14.01           N  
-ATOM  20103  CA  PRO E 600       6.339 -94.479 -51.365  1.00 18.66           C  
-ATOM  20104  C   PRO E 600       7.716 -95.126 -51.464  1.00 26.61           C  
-ATOM  20105  O   PRO E 600       7.815 -96.345 -51.615  1.00 34.41           O  
-ATOM  20106  CB  PRO E 600       6.001 -94.176 -49.910  1.00 18.51           C  
-ATOM  20107  CG  PRO E 600       5.383 -95.443 -49.428  1.00 17.18           C  
-ATOM  20108  CD  PRO E 600       4.638 -96.036 -50.605  1.00 14.80           C  
-ATOM  20109  N   HIS E 601       8.766 -94.315 -51.376  1.00 20.70           N  
-ATOM  20110  CA  HIS E 601      10.121 -94.844 -51.318  1.00 24.56           C  
-ATOM  20111  C   HIS E 601      10.398 -95.397 -49.926  1.00 38.75           C  
-ATOM  20112  O   HIS E 601       9.512 -95.418 -49.072  1.00 54.76           O  
-ATOM  20113  CB  HIS E 601      11.145 -93.768 -51.675  1.00 25.28           C  
-ATOM  20114  CG  HIS E 601      11.132 -93.378 -53.120  1.00 25.25           C  
-ATOM  20115  ND1 HIS E 601      12.035 -93.878 -54.033  1.00 22.37           N  
-ATOM  20116  CD2 HIS E 601      10.325 -92.539 -53.809  1.00 21.52           C  
-ATOM  20117  CE1 HIS E 601      11.785 -93.361 -55.223  1.00 25.23           C  
-ATOM  20118  NE2 HIS E 601      10.752 -92.546 -55.115  1.00 16.52           N  
-ATOM  20119  N   GLY E 602      11.628 -95.842 -49.698  1.00 35.17           N  
-ATOM  20120  CA  GLY E 602      11.996 -96.409 -48.414  1.00 52.83           C  
-ATOM  20121  C   GLY E 602      11.967 -95.385 -47.295  1.00 60.31           C  
-ATOM  20122  O   GLY E 602      12.020 -94.181 -47.546  1.00 49.82           O  
-ATOM  20123  N   ARG E 603      11.874 -95.858 -46.056  1.00 66.25           N  
-ATOM  20124  CA  ARG E 603      11.952 -94.965 -44.906  1.00 57.71           C  
-ATOM  20125  C   ARG E 603      13.365 -94.410 -44.757  1.00 59.05           C  
-ATOM  20126  O   ARG E 603      14.341 -95.050 -45.155  1.00 53.84           O  
-ATOM  20127  CB  ARG E 603      11.533 -95.681 -43.620  1.00 55.02           C  
-ATOM  20128  CG  ARG E 603      10.029 -95.790 -43.408  1.00 58.79           C  
-ATOM  20129  CD  ARG E 603       9.719 -96.292 -42.002  1.00 61.23           C  
-ATOM  20130  NE  ARG E 603       8.290 -96.489 -41.769  1.00 69.83           N  
-ATOM  20131  CZ  ARG E 603       7.490 -95.596 -41.192  1.00 69.78           C  
-ATOM  20132  NH1 ARG E 603       7.976 -94.428 -40.787  1.00 56.93           N  
-ATOM  20133  NH2 ARG E 603       6.202 -95.869 -41.019  1.00 39.83           N  
-ATOM  20134  N   ILE E 604      13.466 -93.214 -44.189  1.00 60.89           N  
-ATOM  20135  CA  ILE E 604      14.758 -92.603 -43.915  1.00 61.87           C  
-ATOM  20136  C   ILE E 604      14.883 -92.269 -42.436  1.00 65.72           C  
-ATOM  20137  O   ILE E 604      14.122 -91.458 -41.907  1.00 66.14           O  
-ATOM  20138  CB  ILE E 604      14.974 -91.325 -44.742  1.00 61.20           C  
-ATOM  20139  CG1 ILE E 604      15.122 -91.670 -46.225  1.00 66.62           C  
-ATOM  20140  CG2 ILE E 604      16.204 -90.583 -44.253  1.00 51.53           C  
-ATOM  20141  CD1 ILE E 604      15.463 -90.480 -47.097  1.00 49.73           C  
-ATOM  20142  N   GLN E 605      15.842 -92.905 -41.773  1.00 64.81           N  
-ATOM  20143  CA  GLN E 605      16.046 -92.701 -40.346  1.00 67.43           C  
-ATOM  20144  C   GLN E 605      16.496 -91.279 -40.031  1.00 68.06           C  
-ATOM  20145  O   GLN E 605      17.540 -90.824 -40.499  1.00 61.05           O  
-ATOM  20146  CB  GLN E 605      17.067 -93.704 -39.803  1.00 55.30           C  
-ATOM  20147  CG  GLN E 605      16.442 -94.924 -39.146  1.00 60.64           C  
-ATOM  20148  CD  GLN E 605      15.699 -94.580 -37.865  1.00 82.71           C  
-ATOM  20149  OE1 GLN E 605      15.985 -93.571 -37.217  1.00 81.38           O  
-ATOM  20150  NE2 GLN E 605      14.736 -95.419 -37.495  1.00 70.47           N  
-ATOM  20151  N   MET E 606      15.690 -90.580 -39.238  1.00 65.78           N  
-ATOM  20152  CA  MET E 606      16.036 -89.245 -38.767  1.00 69.79           C  
-ATOM  20153  C   MET E 606      15.657 -89.085 -37.299  1.00 73.18           C  
-ATOM  20154  O   MET E 606      14.476 -89.079 -36.948  1.00 72.04           O  
-ATOM  20155  CB  MET E 606      15.350 -88.173 -39.618  1.00 62.53           C  
-ATOM  20156  CG  MET E 606      15.968 -87.991 -40.996  1.00 65.93           C  
-ATOM  20157  SD  MET E 606      15.147 -86.722 -41.979  1.00 76.35           S  
-ATOM  20158  CE  MET E 606      13.543 -87.476 -42.216  1.00 59.24           C  
-ATOM  20159  N   GLU E 607      16.671 -88.961 -36.448  1.00 73.44           N  
-ATOM  20160  CA  GLU E 607      16.468 -88.844 -35.008  1.00 71.84           C  
-ATOM  20161  C   GLU E 607      15.742 -87.556 -34.641  1.00 77.51           C  
-ATOM  20162  O   GLU E 607      15.934 -86.518 -35.274  1.00 81.94           O  
-ATOM  20163  CB  GLU E 607      17.806 -88.906 -34.272  1.00 73.33           C  
-ATOM  20164  CG  GLU E 607      18.522 -90.240 -34.395  1.00 86.07           C  
-ATOM  20165  CD  GLU E 607      19.829 -90.269 -33.628  1.00105.38           C  
-ATOM  20166  OE1 GLU E 607      20.395 -91.370 -33.461  1.00106.24           O  
-ATOM  20167  OE2 GLU E 607      20.290 -89.191 -33.193  1.00 98.94           O  
-ATOM  20168  N   MET E 608      14.907 -87.631 -33.611  1.00 76.36           N  
-ATOM  20169  CA  MET E 608      14.173 -86.463 -33.149  1.00 84.34           C  
-ATOM  20170  C   MET E 608      15.064 -85.553 -32.314  1.00 81.70           C  
-ATOM  20171  O   MET E 608      15.666 -85.991 -31.332  1.00 69.20           O  
-ATOM  20172  CB  MET E 608      12.949 -86.882 -32.332  1.00 85.16           C  
-ATOM  20173  CG  MET E 608      12.012 -85.732 -31.992  1.00 76.64           C  
-ATOM  20174  SD  MET E 608      11.100 -85.985 -30.456  1.00 66.30           S  
-ATOM  20175  CE  MET E 608      10.472 -87.647 -30.679  1.00 84.55           C  
-ATOM  20176  N   ALA E 609      15.150 -84.288 -32.712  1.00 85.33           N  
-ATOM  20177  CA  ALA E 609      15.796 -83.281 -31.883  1.00 77.06           C  
-ATOM  20178  C   ALA E 609      14.978 -83.118 -30.606  1.00 80.19           C  
-ATOM  20179  O   ALA E 609      13.896 -82.527 -30.618  1.00 79.28           O  
-ATOM  20180  CB  ALA E 609      15.920 -81.966 -32.624  1.00 67.99           C  
-ATOM  20181  N   VAL E 610      15.510 -83.654 -29.512  1.00 77.94           N  
-ATOM  20182  CA  VAL E 610      14.774 -83.807 -28.259  1.00 76.37           C  
-ATOM  20183  C   VAL E 610      14.402 -82.488 -27.582  1.00 69.24           C  
-ATOM  20184  O   VAL E 610      14.015 -82.476 -26.412  1.00 61.12           O  
-ATOM  20185  CB  VAL E 610      15.583 -84.655 -27.255  1.00 81.23           C  
-ATOM  20186  CG1 VAL E 610      14.754 -85.831 -26.770  1.00 63.05           C  
-ATOM  20187  CG2 VAL E 610      16.882 -85.140 -27.894  1.00 91.95           C  
-ATOM  20188  OXT VAL E 610      14.468 -81.410 -28.165  1.00 69.14           O  
-TER   20189      VAL E 610                                                      
-ATOM  20190  N   LYS F   3      20.403 -44.855 -85.083  1.00 91.11           N  
-ATOM  20191  CA  LYS F   3      21.056 -43.814 -84.295  1.00 90.81           C  
-ATOM  20192  C   LYS F   3      20.244 -43.427 -83.053  1.00 93.40           C  
-ATOM  20193  O   LYS F   3      19.896 -42.257 -82.884  1.00 80.29           O  
-ATOM  20194  CB  LYS F   3      21.290 -42.572 -85.159  1.00 88.95           C  
-ATOM  20195  CG  LYS F   3      21.873 -42.859 -86.536  1.00 72.43           C  
-ATOM  20196  CD  LYS F   3      21.043 -42.206 -87.633  1.00 68.18           C  
-ATOM  20197  CE  LYS F   3      19.729 -42.940 -87.847  1.00 68.65           C  
-ATOM  20198  NZ  LYS F   3      19.947 -44.307 -88.399  1.00 60.28           N  
-ATOM  20199  N   PRO F   4      19.948 -44.401 -82.173  1.00 94.15           N  
-ATOM  20200  CA  PRO F   4      19.095 -44.108 -81.017  1.00 77.81           C  
-ATOM  20201  C   PRO F   4      19.863 -43.461 -79.864  1.00 71.92           C  
-ATOM  20202  O   PRO F   4      21.077 -43.630 -79.755  1.00 67.89           O  
-ATOM  20203  CB  PRO F   4      18.562 -45.493 -80.612  1.00 75.03           C  
-ATOM  20204  CG  PRO F   4      19.259 -46.504 -81.530  1.00 70.05           C  
-ATOM  20205  CD  PRO F   4      20.417 -45.794 -82.149  1.00 74.28           C  
-ATOM  20206  N   VAL F   5      19.152 -42.723 -79.016  1.00 73.01           N  
-ATOM  20207  CA  VAL F   5      19.763 -42.021 -77.889  1.00 62.49           C  
-ATOM  20208  C   VAL F   5      19.041 -42.367 -76.584  1.00 66.22           C  
-ATOM  20209  O   VAL F   5      17.837 -42.631 -76.588  1.00 62.64           O  
-ATOM  20210  CB  VAL F   5      19.735 -40.489 -78.100  1.00 54.23           C  
-ATOM  20211  CG1 VAL F   5      20.589 -39.781 -77.061  1.00 52.06           C  
-ATOM  20212  CG2 VAL F   5      20.203 -40.134 -79.502  1.00 65.54           C  
-ATOM  20213  N   CYS F   6      19.778 -42.377 -75.474  1.00 59.30           N  
-ATOM  20214  CA  CYS F   6      19.189 -42.612 -74.157  1.00 49.55           C  
-ATOM  20215  C   CYS F   6      19.632 -41.554 -73.149  1.00 46.72           C  
-ATOM  20216  O   CYS F   6      20.806 -41.191 -73.102  1.00 48.25           O  
-ATOM  20217  CB  CYS F   6      19.560 -44.002 -73.640  1.00 50.23           C  
-ATOM  20218  SG  CYS F   6      18.797 -45.365 -74.548  1.00 70.77           S  
-ATOM  20219  N   LEU F   7      18.690 -41.062 -72.347  1.00 48.45           N  
-ATOM  20220  CA  LEU F   7      19.003 -40.080 -71.312  1.00 41.39           C  
-ATOM  20221  C   LEU F   7      19.156 -40.749 -69.949  1.00 41.88           C  
-ATOM  20222  O   LEU F   7      18.305 -41.537 -69.538  1.00 43.30           O  
-ATOM  20223  CB  LEU F   7      17.923 -38.998 -71.238  1.00 29.97           C  
-ATOM  20224  CG  LEU F   7      17.591 -38.210 -72.507  1.00 38.82           C  
-ATOM  20225  CD1 LEU F   7      16.735 -36.991 -72.179  1.00 35.47           C  
-ATOM  20226  CD2 LEU F   7      18.853 -37.798 -73.237  1.00 43.06           C  
-ATOM  20227  N   VAL F   8      20.246 -40.437 -69.254  1.00 37.64           N  
-ATOM  20228  CA  VAL F   8      20.488 -40.984 -67.923  1.00 32.97           C  
-ATOM  20229  C   VAL F   8      20.457 -39.869 -66.883  1.00 44.74           C  
-ATOM  20230  O   VAL F   8      21.325 -38.995 -66.869  1.00 45.79           O  
-ATOM  20231  CB  VAL F   8      21.835 -41.722 -67.844  1.00 32.64           C  
-ATOM  20232  CG1 VAL F   8      22.013 -42.344 -66.470  1.00 42.09           C  
-ATOM  20233  CG2 VAL F   8      21.918 -42.788 -68.923  1.00 41.19           C  
-ATOM  20234  N   VAL F   9      19.452 -39.907 -66.011  1.00 46.54           N  
-ATOM  20235  CA  VAL F   9      19.203 -38.815 -65.073  1.00 34.29           C  
-ATOM  20236  C   VAL F   9      18.924 -39.278 -63.646  1.00 33.90           C  
-ATOM  20237  O   VAL F   9      18.635 -40.450 -63.397  1.00 38.55           O  
-ATOM  20238  CB  VAL F   9      18.002 -37.964 -65.517  1.00 27.50           C  
-ATOM  20239  CG1 VAL F   9      18.307 -37.236 -66.804  1.00 37.88           C  
-ATOM  20240  CG2 VAL F   9      16.787 -38.842 -65.692  1.00 26.42           C  
-ATOM  20241  N   ALA F  10      19.006 -38.332 -62.716  1.00 30.78           N  
-ATOM  20242  CA  ALA F  10      18.586 -38.539 -61.336  1.00 28.10           C  
-ATOM  20243  C   ALA F  10      17.910 -37.267 -60.837  1.00 36.96           C  
-ATOM  20244  O   ALA F  10      18.581 -36.283 -60.526  1.00 42.23           O  
-ATOM  20245  CB  ALA F  10      19.769 -38.907 -60.456  1.00 31.00           C  
-ATOM  20246  N   MET F  11      16.582 -37.286 -60.769  1.00 26.17           N  
-ATOM  20247  CA  MET F  11      15.832 -36.074 -60.463  1.00 20.07           C  
-ATOM  20248  C   MET F  11      14.857 -36.227 -59.294  1.00 26.52           C  
-ATOM  20249  O   MET F  11      14.358 -37.318 -59.016  1.00 35.08           O  
-ATOM  20250  CB  MET F  11      15.069 -35.610 -61.705  1.00 17.57           C  
-ATOM  20251  CG  MET F  11      13.927 -36.523 -62.108  1.00 24.77           C  
-ATOM  20252  SD  MET F  11      13.080 -35.977 -63.604  1.00 36.47           S  
-ATOM  20253  CE  MET F  11      14.117 -36.684 -64.878  1.00 20.72           C  
-ATOM  20254  N   THR F  12      14.601 -35.111 -58.615  1.00 25.19           N  
-ATOM  20255  CA  THR F  12      13.610 -35.029 -57.545  1.00 23.54           C  
-ATOM  20256  C   THR F  12      12.201 -35.118 -58.147  1.00 26.21           C  
-ATOM  20257  O   THR F  12      12.063 -35.144 -59.370  1.00 26.13           O  
-ATOM  20258  CB  THR F  12      13.780 -33.716 -56.749  1.00 20.71           C  
-ATOM  20259  OG1 THR F  12      13.285 -32.615 -57.521  1.00 25.29           O  
-ATOM  20260  CG2 THR F  12      15.244 -33.482 -56.419  1.00 20.85           C  
-ATOM  20261  N   PRO F  13      11.146 -35.187 -57.307  1.00 26.81           N  
-ATOM  20262  CA  PRO F  13       9.818 -35.193 -57.937  1.00 24.50           C  
-ATOM  20263  C   PRO F  13       9.492 -33.885 -58.653  1.00 22.29           C  
-ATOM  20264  O   PRO F  13       8.666 -33.880 -59.562  1.00 23.21           O  
-ATOM  20265  CB  PRO F  13       8.867 -35.411 -56.757  1.00 25.11           C  
-ATOM  20266  CG  PRO F  13       9.693 -36.075 -55.725  1.00 29.91           C  
-ATOM  20267  CD  PRO F  13      11.057 -35.471 -55.863  1.00 25.41           C  
-ATOM  20268  N   LYS F  14      10.135 -32.794 -58.248  1.00 22.73           N  
-ATOM  20269  CA  LYS F  14       9.944 -31.509 -58.909  1.00 21.35           C  
-ATOM  20270  C   LYS F  14      10.934 -31.330 -60.057  1.00 23.32           C  
-ATOM  20271  O   LYS F  14      11.196 -30.206 -60.489  1.00 24.17           O  
-ATOM  20272  CB  LYS F  14      10.086 -30.359 -57.912  1.00 21.92           C  
-ATOM  20273  CG  LYS F  14       8.934 -30.220 -56.932  1.00 20.13           C  
-ATOM  20274  CD  LYS F  14       9.155 -29.022 -56.018  1.00 26.03           C  
-ATOM  20275  CE  LYS F  14       8.020 -28.844 -55.027  1.00 22.07           C  
-ATOM  20276  NZ  LYS F  14       8.270 -27.682 -54.133  1.00 19.26           N  
-ATOM  20277  N   ARG F  15      11.484 -32.449 -60.526  1.00 23.09           N  
-ATOM  20278  CA  ARG F  15      12.398 -32.492 -61.671  1.00 27.83           C  
-ATOM  20279  C   ARG F  15      13.710 -31.737 -61.443  1.00 30.38           C  
-ATOM  20280  O   ARG F  15      14.422 -31.422 -62.397  1.00 32.16           O  
-ATOM  20281  CB  ARG F  15      11.704 -31.953 -62.928  1.00 21.84           C  
-ATOM  20282  CG  ARG F  15      10.441 -32.702 -63.297  1.00 21.87           C  
-ATOM  20283  CD  ARG F  15       9.909 -32.286 -64.661  1.00 25.69           C  
-ATOM  20284  NE  ARG F  15       8.917 -31.219 -64.572  1.00 26.14           N  
-ATOM  20285  CZ  ARG F  15       9.172 -29.934 -64.790  1.00 30.11           C  
-ATOM  20286  NH1 ARG F  15       8.201 -29.037 -64.686  1.00 32.78           N  
-ATOM  20287  NH2 ARG F  15      10.396 -29.542 -65.115  1.00 28.25           N  
-ATOM  20288  N   GLY F  16      14.031 -31.458 -60.184  1.00 22.49           N  
-ATOM  20289  CA  GLY F  16      15.283 -30.801 -59.856  1.00 22.80           C  
-ATOM  20290  C   GLY F  16      16.451 -31.756 -60.004  1.00 24.87           C  
-ATOM  20291  O   GLY F  16      16.334 -32.931 -59.660  1.00 32.44           O  
-ATOM  20292  N   ILE F  17      17.577 -31.265 -60.516  1.00 31.73           N  
-ATOM  20293  CA  ILE F  17      18.735 -32.129 -60.743  1.00 23.64           C  
-ATOM  20294  C   ILE F  17      20.052 -31.559 -60.223  1.00 26.45           C  
-ATOM  20295  O   ILE F  17      21.026 -32.294 -60.069  1.00 29.20           O  
-ATOM  20296  CB  ILE F  17      18.916 -32.444 -62.240  1.00 21.67           C  
-ATOM  20297  CG1 ILE F  17      19.068 -31.154 -63.045  1.00 25.96           C  
-ATOM  20298  CG2 ILE F  17      17.746 -33.260 -62.757  1.00 31.32           C  
-ATOM  20299  CD1 ILE F  17      19.329 -31.382 -64.521  1.00 32.12           C  
-ATOM  20300  N   GLY F  18      20.093 -30.258 -59.956  1.00 27.22           N  
-ATOM  20301  CA  GLY F  18      21.334 -29.645 -59.519  1.00 29.42           C  
-ATOM  20302  C   GLY F  18      21.216 -28.306 -58.820  1.00 31.60           C  
-ATOM  20303  O   GLY F  18      20.185 -27.634 -58.892  1.00 29.00           O  
-ATOM  20304  N   ILE F  19      22.290 -27.920 -58.139  1.00 38.93           N  
-ATOM  20305  CA  ILE F  19      22.360 -26.626 -57.475  1.00 35.05           C  
-ATOM  20306  C   ILE F  19      23.821 -26.240 -57.225  1.00 33.16           C  
-ATOM  20307  O   ILE F  19      24.623 -27.055 -56.760  1.00 26.85           O  
-ATOM  20308  CB  ILE F  19      21.554 -26.626 -56.151  1.00 22.27           C  
-ATOM  20309  CG1 ILE F  19      21.559 -25.237 -55.513  1.00 21.55           C  
-ATOM  20310  CG2 ILE F  19      22.068 -27.694 -55.190  1.00 21.09           C  
-ATOM  20311  CD1 ILE F  19      20.575 -25.092 -54.381  1.00 19.77           C  
-ATOM  20312  N   ASN F  20      24.156 -24.995 -57.560  1.00 31.17           N  
-ATOM  20313  CA  ASN F  20      25.528 -24.496 -57.493  1.00 35.26           C  
-ATOM  20314  C   ASN F  20      26.499 -25.414 -58.228  1.00 37.63           C  
-ATOM  20315  O   ASN F  20      27.568 -25.746 -57.712  1.00 33.35           O  
-ATOM  20316  CB  ASN F  20      25.969 -24.316 -56.039  1.00 35.08           C  
-ATOM  20317  CG  ASN F  20      25.216 -23.205 -55.337  1.00 31.57           C  
-ATOM  20318  OD1 ASN F  20      24.793 -22.234 -55.964  1.00 32.32           O  
-ATOM  20319  ND2 ASN F  20      25.044 -23.342 -54.027  1.00 29.30           N  
-ATOM  20320  N   ASN F  21      26.105 -25.819 -59.433  1.00 39.77           N  
-ATOM  20321  CA  ASN F  21      26.897 -26.712 -60.273  1.00 37.23           C  
-ATOM  20322  C   ASN F  21      27.313 -27.986 -59.544  1.00 38.20           C  
-ATOM  20323  O   ASN F  21      28.462 -28.421 -59.630  1.00 47.40           O  
-ATOM  20324  CB  ASN F  21      28.132 -25.986 -60.804  1.00 34.68           C  
-ATOM  20325  CG  ASN F  21      28.413 -26.314 -62.251  1.00 46.87           C  
-ATOM  20326  OD1 ASN F  21      27.694 -25.871 -63.145  1.00 52.19           O  
-ATOM  20327  ND2 ASN F  21      29.465 -27.089 -62.492  1.00 60.84           N  
-ATOM  20328  N   GLY F  22      26.365 -28.574 -58.822  1.00 31.14           N  
-ATOM  20329  CA  GLY F  22      26.614 -29.794 -58.082  1.00 33.11           C  
-ATOM  20330  C   GLY F  22      25.330 -30.566 -57.865  1.00 27.14           C  
-ATOM  20331  O   GLY F  22      24.304 -30.256 -58.465  1.00 26.45           O  
-ATOM  20332  N   LEU F  23      25.385 -31.571 -57.000  1.00 18.91           N  
-ATOM  20333  CA  LEU F  23      24.219 -32.398 -56.731  1.00 20.56           C  
-ATOM  20334  C   LEU F  23      23.441 -31.887 -55.523  1.00 21.45           C  
-ATOM  20335  O   LEU F  23      24.033 -31.479 -54.524  1.00 22.52           O  
-ATOM  20336  CB  LEU F  23      24.641 -33.851 -56.518  1.00 28.36           C  
-ATOM  20337  CG  LEU F  23      25.283 -34.504 -57.742  1.00 22.38           C  
-ATOM  20338  CD1 LEU F  23      25.777 -35.904 -57.414  1.00 30.01           C  
-ATOM  20339  CD2 LEU F  23      24.300 -34.532 -58.900  1.00 21.44           C  
-ATOM  20340  N   PRO F  24      22.104 -31.911 -55.618  1.00 20.80           N  
-ATOM  20341  CA  PRO F  24      21.194 -31.432 -54.575  1.00 25.79           C  
-ATOM  20342  C   PRO F  24      21.198 -32.338 -53.352  1.00 26.86           C  
-ATOM  20343  O   PRO F  24      21.044 -31.869 -52.223  1.00 23.44           O  
-ATOM  20344  CB  PRO F  24      19.822 -31.465 -55.260  1.00 22.29           C  
-ATOM  20345  CG  PRO F  24      20.100 -31.653 -56.717  1.00 22.29           C  
-ATOM  20346  CD  PRO F  24      21.368 -32.420 -56.784  1.00 25.90           C  
-ATOM  20347  N   TRP F  25      21.376 -33.633 -53.593  1.00 22.79           N  
-ATOM  20348  CA  TRP F  25      21.285 -34.646 -52.550  1.00 25.27           C  
-ATOM  20349  C   TRP F  25      22.656 -35.213 -52.193  1.00 25.85           C  
-ATOM  20350  O   TRP F  25      23.568 -35.197 -53.019  1.00 25.27           O  
-ATOM  20351  CB  TRP F  25      20.346 -35.768 -53.002  1.00 26.75           C  
-ATOM  20352  CG  TRP F  25      20.182 -35.830 -54.492  1.00 32.27           C  
-ATOM  20353  CD1 TRP F  25      19.169 -35.283 -55.231  1.00 34.89           C  
-ATOM  20354  CD2 TRP F  25      21.060 -36.462 -55.426  1.00 27.99           C  
-ATOM  20355  NE1 TRP F  25      19.360 -35.540 -56.566  1.00 23.97           N  
-ATOM  20356  CE2 TRP F  25      20.518 -36.263 -56.713  1.00 35.06           C  
-ATOM  20357  CE3 TRP F  25      22.256 -37.180 -55.302  1.00 32.52           C  
-ATOM  20358  CZ2 TRP F  25      21.125 -36.755 -57.865  1.00 50.73           C  
-ATOM  20359  CZ3 TRP F  25      22.859 -37.671 -56.449  1.00 46.23           C  
-ATOM  20360  CH2 TRP F  25      22.294 -37.455 -57.712  1.00 58.37           C  
-ATOM  20361  N   PRO F  26      22.807 -35.712 -50.955  1.00 18.70           N  
-ATOM  20362  CA  PRO F  26      24.039 -36.400 -50.558  1.00 15.11           C  
-ATOM  20363  C   PRO F  26      24.299 -37.633 -51.416  1.00 26.51           C  
-ATOM  20364  O   PRO F  26      23.421 -38.051 -52.171  1.00 37.28           O  
-ATOM  20365  CB  PRO F  26      23.775 -36.789 -49.100  1.00 19.63           C  
-ATOM  20366  CG  PRO F  26      22.292 -36.723 -48.940  1.00 28.91           C  
-ATOM  20367  CD  PRO F  26      21.853 -35.616 -49.839  1.00 23.48           C  
-ATOM  20368  N   HIS F  27      25.491 -38.206 -51.287  1.00 27.77           N  
-ATOM  20369  CA  HIS F  27      25.957 -39.255 -52.190  1.00 29.67           C  
-ATOM  20370  C   HIS F  27      25.010 -40.452 -52.271  1.00 36.21           C  
-ATOM  20371  O   HIS F  27      24.629 -41.024 -51.249  1.00 33.77           O  
-ATOM  20372  CB  HIS F  27      27.348 -39.725 -51.761  1.00 28.69           C  
-ATOM  20373  CG  HIS F  27      28.129 -40.373 -52.860  1.00 25.64           C  
-ATOM  20374  ND1 HIS F  27      28.202 -41.740 -53.016  1.00 28.16           N  
-ATOM  20375  CD2 HIS F  27      28.868 -39.840 -53.861  1.00 28.70           C  
-ATOM  20376  CE1 HIS F  27      28.955 -42.022 -54.063  1.00 38.49           C  
-ATOM  20377  NE2 HIS F  27      29.372 -40.887 -54.594  1.00 42.75           N  
-ATOM  20378  N   LEU F  28      24.633 -40.818 -53.496  1.00 37.20           N  
-ATOM  20379  CA  LEU F  28      23.770 -41.975 -53.734  1.00 29.07           C  
-ATOM  20380  C   LEU F  28      24.551 -43.126 -54.371  1.00 34.96           C  
-ATOM  20381  O   LEU F  28      24.625 -43.250 -55.599  1.00 39.76           O  
-ATOM  20382  CB  LEU F  28      22.582 -41.592 -54.616  1.00 25.61           C  
-ATOM  20383  CG  LEU F  28      21.658 -40.487 -54.101  1.00 25.31           C  
-ATOM  20384  CD1 LEU F  28      20.493 -40.284 -55.057  1.00 22.46           C  
-ATOM  20385  CD2 LEU F  28      21.156 -40.799 -52.701  1.00 23.84           C  
-ATOM  20386  N   THR F  29      25.119 -43.966 -53.509  1.00 32.94           N  
-ATOM  20387  CA  THR F  29      25.991 -45.067 -53.904  1.00 32.66           C  
-ATOM  20388  C   THR F  29      25.373 -45.978 -54.959  1.00 38.70           C  
-ATOM  20389  O   THR F  29      25.953 -46.179 -56.035  1.00 43.66           O  
-ATOM  20390  CB  THR F  29      26.369 -45.927 -52.688  1.00 25.99           C  
-ATOM  20391  OG1 THR F  29      26.915 -45.091 -51.660  1.00 29.29           O  
-ATOM  20392  CG2 THR F  29      27.385 -46.987 -53.079  1.00 25.11           C  
-ATOM  20393  N   THR F  30      24.204 -46.532 -54.646  1.00 25.05           N  
-ATOM  20394  CA  THR F  30      23.534 -47.465 -55.544  1.00 29.04           C  
-ATOM  20395  C   THR F  30      23.189 -46.801 -56.866  1.00 34.26           C  
-ATOM  20396  O   THR F  30      23.238 -47.432 -57.919  1.00 40.42           O  
-ATOM  20397  CB  THR F  30      22.251 -48.034 -54.915  1.00 28.92           C  
-ATOM  20398  OG1 THR F  30      22.571 -48.685 -53.679  1.00 41.92           O  
-ATOM  20399  CG2 THR F  30      21.587 -49.031 -55.850  1.00 37.05           C  
-ATOM  20400  N   ASP F  31      22.842 -45.520 -56.805  1.00 37.40           N  
-ATOM  20401  CA  ASP F  31      22.560 -44.757 -58.014  1.00 32.23           C  
-ATOM  20402  C   ASP F  31      23.810 -44.631 -58.871  1.00 33.10           C  
-ATOM  20403  O   ASP F  31      23.731 -44.695 -60.096  1.00 42.14           O  
-ATOM  20404  CB  ASP F  31      22.021 -43.369 -57.673  1.00 33.02           C  
-ATOM  20405  CG  ASP F  31      21.857 -42.487 -58.898  1.00 30.73           C  
-ATOM  20406  OD1 ASP F  31      21.234 -42.933 -59.883  1.00 19.85           O  
-ATOM  20407  OD2 ASP F  31      22.361 -41.346 -58.875  1.00 40.88           O  
-ATOM  20408  N   PHE F  32      24.964 -44.459 -58.232  1.00 38.34           N  
-ATOM  20409  CA  PHE F  32      26.215 -44.374 -58.982  1.00 45.01           C  
-ATOM  20410  C   PHE F  32      26.605 -45.715 -59.595  1.00 40.45           C  
-ATOM  20411  O   PHE F  32      27.086 -45.766 -60.734  1.00 37.46           O  
-ATOM  20412  CB  PHE F  32      27.346 -43.845 -58.100  1.00 39.44           C  
-ATOM  20413  CG  PHE F  32      27.490 -42.356 -58.150  1.00 42.12           C  
-ATOM  20414  CD1 PHE F  32      27.918 -41.733 -59.310  1.00 55.14           C  
-ATOM  20415  CD2 PHE F  32      27.185 -41.576 -57.049  1.00 44.23           C  
-ATOM  20416  CE1 PHE F  32      28.046 -40.358 -59.368  1.00 58.06           C  
-ATOM  20417  CE2 PHE F  32      27.312 -40.200 -57.099  1.00 52.51           C  
-ATOM  20418  CZ  PHE F  32      27.743 -39.590 -58.261  1.00 50.42           C  
-ATOM  20419  N   LYS F  33      26.406 -46.793 -58.843  1.00 41.09           N  
-ATOM  20420  CA  LYS F  33      26.628 -48.129 -59.381  1.00 48.03           C  
-ATOM  20421  C   LYS F  33      25.745 -48.339 -60.606  1.00 48.46           C  
-ATOM  20422  O   LYS F  33      26.190 -48.847 -61.630  1.00 61.45           O  
-ATOM  20423  CB  LYS F  33      26.347 -49.199 -58.322  1.00 45.40           C  
-ATOM  20424  CG  LYS F  33      27.389 -49.281 -57.215  1.00 52.62           C  
-ATOM  20425  CD  LYS F  33      26.996 -50.325 -56.178  1.00 50.51           C  
-ATOM  20426  CE  LYS F  33      27.966 -50.337 -55.009  1.00 61.94           C  
-ATOM  20427  NZ  LYS F  33      27.463 -51.171 -53.881  1.00 36.11           N  
-ATOM  20428  N   HIS F  34      24.489 -47.922 -60.481  1.00 48.27           N  
-ATOM  20429  CA  HIS F  34      23.513 -47.987 -61.564  1.00 53.18           C  
-ATOM  20430  C   HIS F  34      23.989 -47.231 -62.802  1.00 46.79           C  
-ATOM  20431  O   HIS F  34      23.973 -47.776 -63.904  1.00 52.95           O  
-ATOM  20432  CB  HIS F  34      22.165 -47.425 -61.101  1.00 52.20           C  
-ATOM  20433  CG  HIS F  34      21.229 -47.091 -62.222  1.00 49.88           C  
-ATOM  20434  ND1 HIS F  34      20.438 -48.035 -62.840  1.00 52.38           N  
-ATOM  20435  CD2 HIS F  34      20.953 -45.913 -62.831  1.00 47.91           C  
-ATOM  20436  CE1 HIS F  34      19.716 -47.454 -63.782  1.00 59.16           C  
-ATOM  20437  NE2 HIS F  34      20.010 -46.167 -63.798  1.00 55.77           N  
-ATOM  20438  N   PHE F  35      24.398 -45.979 -62.611  1.00 37.93           N  
-ATOM  20439  CA  PHE F  35      24.909 -45.146 -63.696  1.00 40.36           C  
-ATOM  20440  C   PHE F  35      26.073 -45.829 -64.403  1.00 47.09           C  
-ATOM  20441  O   PHE F  35      26.044 -46.038 -65.624  1.00 50.42           O  
-ATOM  20442  CB  PHE F  35      25.342 -43.781 -63.148  1.00 40.67           C  
-ATOM  20443  CG  PHE F  35      25.975 -42.873 -64.175  1.00 43.19           C  
-ATOM  20444  CD1 PHE F  35      27.352 -42.848 -64.347  1.00 50.94           C  
-ATOM  20445  CD2 PHE F  35      25.197 -42.029 -64.950  1.00 41.87           C  
-ATOM  20446  CE1 PHE F  35      27.937 -42.010 -65.286  1.00 48.80           C  
-ATOM  20447  CE2 PHE F  35      25.774 -41.191 -65.886  1.00 41.96           C  
-ATOM  20448  CZ  PHE F  35      27.145 -41.180 -66.055  1.00 45.05           C  
-ATOM  20449  N   SER F  36      27.090 -46.179 -63.618  1.00 48.89           N  
-ATOM  20450  CA  SER F  36      28.314 -46.770 -64.146  1.00 61.58           C  
-ATOM  20451  C   SER F  36      28.050 -48.076 -64.882  1.00 64.97           C  
-ATOM  20452  O   SER F  36      28.707 -48.379 -65.873  1.00 70.38           O  
-ATOM  20453  CB  SER F  36      29.323 -47.000 -63.016  1.00 67.71           C  
-ATOM  20454  OG  SER F  36      30.627 -47.237 -63.534  1.00 63.80           O  
-ATOM  20455  N   ARG F  37      27.089 -48.849 -64.391  1.00 56.05           N  
-ATOM  20456  CA  ARG F  37      26.738 -50.114 -65.022  1.00 52.46           C  
-ATOM  20457  C   ARG F  37      26.010 -49.898 -66.340  1.00 50.91           C  
-ATOM  20458  O   ARG F  37      26.363 -50.489 -67.360  1.00 52.14           O  
-ATOM  20459  CB  ARG F  37      25.879 -50.957 -64.083  1.00 46.52           C  
-ATOM  20460  CG  ARG F  37      26.572 -52.204 -63.582  1.00 70.96           C  
-ATOM  20461  CD  ARG F  37      27.934 -51.884 -62.991  1.00 80.17           C  
-ATOM  20462  NE  ARG F  37      28.166 -52.613 -61.748  1.00 85.62           N  
-ATOM  20463  CZ  ARG F  37      28.496 -53.899 -61.683  1.00 89.13           C  
-ATOM  20464  NH1 ARG F  37      28.684 -54.476 -60.503  1.00 98.95           N  
-ATOM  20465  NH2 ARG F  37      28.636 -54.611 -62.794  1.00 78.00           N  
-ATOM  20466  N   VAL F  38      24.991 -49.046 -66.309  1.00 52.26           N  
-ATOM  20467  CA  VAL F  38      24.202 -48.743 -67.495  1.00 48.07           C  
-ATOM  20468  C   VAL F  38      25.058 -48.164 -68.619  1.00 52.24           C  
-ATOM  20469  O   VAL F  38      24.925 -48.564 -69.774  1.00 62.34           O  
-ATOM  20470  CB  VAL F  38      23.061 -47.754 -67.172  1.00 46.52           C  
-ATOM  20471  CG1 VAL F  38      22.467 -47.178 -68.449  1.00 42.83           C  
-ATOM  20472  CG2 VAL F  38      21.989 -48.437 -66.341  1.00 47.05           C  
-ATOM  20473  N   THR F  39      25.952 -47.242 -68.281  1.00 51.20           N  
-ATOM  20474  CA  THR F  39      26.690 -46.524 -69.314  1.00 55.08           C  
-ATOM  20475  C   THR F  39      27.762 -47.360 -70.019  1.00 64.33           C  
-ATOM  20476  O   THR F  39      28.430 -46.862 -70.926  1.00 69.12           O  
-ATOM  20477  CB  THR F  39      27.360 -45.262 -68.748  1.00 61.00           C  
-ATOM  20478  OG1 THR F  39      27.816 -45.512 -67.413  1.00 71.07           O  
-ATOM  20479  CG2 THR F  39      26.375 -44.102 -68.734  1.00 46.27           C  
-ATOM  20480  N   LYS F  40      27.929 -48.621 -69.628  1.00 68.29           N  
-ATOM  20481  CA  LYS F  40      28.900 -49.470 -70.313  1.00 65.75           C  
-ATOM  20482  C   LYS F  40      28.465 -50.933 -70.430  1.00 72.11           C  
-ATOM  20483  O   LYS F  40      28.025 -51.550 -69.459  1.00 71.27           O  
-ATOM  20484  CB  LYS F  40      30.262 -49.389 -69.617  1.00 70.46           C  
-ATOM  20485  CG  LYS F  40      30.300 -49.919 -68.194  1.00 72.59           C  
-ATOM  20486  CD  LYS F  40      31.538 -50.775 -67.974  1.00 83.55           C  
-ATOM  20487  CE  LYS F  40      31.858 -50.930 -66.496  1.00 73.70           C  
-ATOM  20488  NZ  LYS F  40      30.739 -51.554 -65.738  1.00 79.96           N  
-ATOM  20489  N   THR F  41      28.585 -51.466 -71.644  1.00 92.69           N  
-ATOM  20490  CA  THR F  41      28.382 -52.888 -71.921  1.00102.01           C  
-ATOM  20491  C   THR F  41      28.906 -53.240 -73.312  1.00 83.14           C  
-ATOM  20492  O   THR F  41      28.227 -53.030 -74.318  1.00 59.94           O  
-ATOM  20493  CB  THR F  41      26.895 -53.307 -71.827  1.00 93.02           C  
-ATOM  20494  OG1 THR F  41      26.068 -52.148 -71.660  1.00 86.08           O  
-ATOM  20495  CG2 THR F  41      26.683 -54.254 -70.653  1.00 69.86           C  
-ATOM  20496  N   PHE F  74      32.901 -50.209 -77.323  1.00 70.00           N  
-ATOM  20497  CA  PHE F  74      32.597 -49.428 -76.129  1.00 73.92           C  
-ATOM  20498  C   PHE F  74      31.345 -48.574 -76.309  1.00 84.19           C  
-ATOM  20499  O   PHE F  74      30.798 -48.478 -77.407  1.00 85.78           O  
-ATOM  20500  CB  PHE F  74      33.786 -48.537 -75.759  1.00 75.10           C  
-ATOM  20501  CG  PHE F  74      34.426 -47.856 -76.937  1.00 83.44           C  
-ATOM  20502  CD1 PHE F  74      33.752 -46.868 -77.639  1.00 78.77           C  
-ATOM  20503  CD2 PHE F  74      35.707 -48.196 -77.336  1.00 89.97           C  
-ATOM  20504  CE1 PHE F  74      34.339 -46.241 -78.721  1.00 88.26           C  
-ATOM  20505  CE2 PHE F  74      36.302 -47.571 -78.416  1.00 94.33           C  
-ATOM  20506  CZ  PHE F  74      35.617 -46.592 -79.109  1.00 99.93           C  
-ATOM  20507  N   ASN F  75      30.902 -47.950 -75.221  1.00 80.43           N  
-ATOM  20508  CA  ASN F  75      29.766 -47.037 -75.265  1.00 68.74           C  
-ATOM  20509  C   ASN F  75      30.215 -45.580 -75.245  1.00 69.51           C  
-ATOM  20510  O   ASN F  75      31.387 -45.282 -75.002  1.00 73.84           O  
-ATOM  20511  CB  ASN F  75      28.813 -47.312 -74.100  1.00 60.78           C  
-ATOM  20512  CG  ASN F  75      27.822 -48.421 -74.405  1.00 68.64           C  
-ATOM  20513  OD1 ASN F  75      27.239 -48.465 -75.486  1.00 76.48           O  
-ATOM  20514  ND2 ASN F  75      27.627 -49.323 -73.451  1.00 66.24           N  
-ATOM  20515  N   ALA F  76      29.281 -44.671 -75.504  1.00 62.73           N  
-ATOM  20516  CA  ALA F  76      29.605 -43.250 -75.542  1.00 69.91           C  
-ATOM  20517  C   ALA F  76      28.737 -42.444 -74.583  1.00 68.94           C  
-ATOM  20518  O   ALA F  76      27.544 -42.705 -74.437  1.00 67.34           O  
-ATOM  20519  CB  ALA F  76      29.461 -42.715 -76.961  1.00 63.55           C  
-ATOM  20520  N   VAL F  77      29.352 -41.467 -73.926  1.00 64.53           N  
-ATOM  20521  CA  VAL F  77      28.642 -40.546 -73.050  1.00 56.54           C  
-ATOM  20522  C   VAL F  77      28.834 -39.105 -73.528  1.00 54.23           C  
-ATOM  20523  O   VAL F  77      29.941 -38.694 -73.890  1.00 60.78           O  
-ATOM  20524  CB  VAL F  77      29.110 -40.682 -71.583  1.00 49.45           C  
-ATOM  20525  CG1 VAL F  77      28.704 -42.036 -71.018  1.00 47.28           C  
-ATOM  20526  CG2 VAL F  77      30.614 -40.487 -71.471  1.00 41.23           C  
-ATOM  20527  N   VAL F  78      27.743 -38.345 -73.546  1.00 38.90           N  
-ATOM  20528  CA  VAL F  78      27.778 -36.960 -73.998  1.00 44.73           C  
-ATOM  20529  C   VAL F  78      27.280 -36.031 -72.895  1.00 56.09           C  
-ATOM  20530  O   VAL F  78      26.158 -36.179 -72.412  1.00 60.10           O  
-ATOM  20531  CB  VAL F  78      26.926 -36.753 -75.264  1.00 42.60           C  
-ATOM  20532  CG1 VAL F  78      27.153 -35.360 -75.832  1.00 51.59           C  
-ATOM  20533  CG2 VAL F  78      27.248 -37.813 -76.302  1.00 41.27           C  
-ATOM  20534  N   MET F  79      28.115 -35.074 -72.503  1.00 56.58           N  
-ATOM  20535  CA  MET F  79      27.790 -34.194 -71.385  1.00 56.45           C  
-ATOM  20536  C   MET F  79      27.996 -32.721 -71.713  1.00 55.79           C  
-ATOM  20537  O   MET F  79      28.802 -32.371 -72.575  1.00 64.75           O  
-ATOM  20538  CB  MET F  79      28.624 -34.575 -70.160  1.00 60.71           C  
-ATOM  20539  CG  MET F  79      30.126 -34.577 -70.405  1.00 67.17           C  
-ATOM  20540  SD  MET F  79      31.013 -35.638 -69.245  1.00 74.19           S  
-ATOM  20541  CE  MET F  79      30.365 -35.035 -67.691  1.00 73.92           C  
-ATOM  20542  N   GLY F  80      27.262 -31.862 -71.014  1.00 56.33           N  
-ATOM  20543  CA  GLY F  80      27.353 -30.429 -71.229  1.00 63.52           C  
-ATOM  20544  C   GLY F  80      28.642 -29.849 -70.682  1.00 73.39           C  
-ATOM  20545  O   GLY F  80      29.462 -30.575 -70.114  1.00 59.92           O  
-ATOM  20546  N   ARG F  81      28.819 -28.540 -70.851  1.00 82.29           N  
-ATOM  20547  CA  ARG F  81      30.045 -27.874 -70.428  1.00 84.80           C  
-ATOM  20548  C   ARG F  81      30.232 -27.964 -68.922  1.00 79.62           C  
-ATOM  20549  O   ARG F  81      31.196 -28.556 -68.440  1.00 72.93           O  
-ATOM  20550  CB  ARG F  81      30.050 -26.405 -70.869  1.00 86.30           C  
-ATOM  20551  CG  ARG F  81      31.343 -25.668 -70.486  1.00 90.34           C  
-ATOM  20552  CD  ARG F  81      31.294 -24.187 -70.841  1.00 75.32           C  
-ATOM  20553  NE  ARG F  81      30.546 -23.428 -69.847  1.00 81.43           N  
-ATOM  20554  CZ  ARG F  81      31.074 -22.953 -68.722  1.00 88.16           C  
-ATOM  20555  NH1 ARG F  81      32.359 -23.156 -68.443  1.00 85.38           N  
-ATOM  20556  NH2 ARG F  81      30.316 -22.273 -67.870  1.00 78.50           N  
-ATOM  20557  N   LYS F  82      29.293 -27.384 -68.184  1.00 75.47           N  
-ATOM  20558  CA  LYS F  82      29.385 -27.331 -66.731  1.00 71.41           C  
-ATOM  20559  C   LYS F  82      29.340 -28.721 -66.092  1.00 72.13           C  
-ATOM  20560  O   LYS F  82      29.926 -28.947 -65.032  1.00 71.08           O  
-ATOM  20561  CB  LYS F  82      28.265 -26.450 -66.167  1.00 71.24           C  
-ATOM  20562  CG  LYS F  82      28.557 -24.956 -66.222  1.00 79.16           C  
-ATOM  20563  CD  LYS F  82      27.612 -24.235 -67.170  1.00 73.13           C  
-ATOM  20564  CE  LYS F  82      26.232 -24.056 -66.558  1.00 64.52           C  
-ATOM  20565  NZ  LYS F  82      25.361 -23.191 -67.401  1.00 50.32           N  
-ATOM  20566  N   THR F  83      28.653 -29.650 -66.751  1.00 73.28           N  
-ATOM  20567  CA  THR F  83      28.518 -31.015 -66.250  1.00 68.38           C  
-ATOM  20568  C   THR F  83      29.880 -31.697 -66.142  1.00 68.29           C  
-ATOM  20569  O   THR F  83      30.125 -32.481 -65.224  1.00 62.26           O  
-ATOM  20570  CB  THR F  83      27.600 -31.864 -67.154  1.00 59.12           C  
-ATOM  20571  OG1 THR F  83      26.377 -31.158 -67.398  1.00 60.77           O  
-ATOM  20572  CG2 THR F  83      27.292 -33.197 -66.498  1.00 49.02           C  
-ATOM  20573  N   TRP F  84      30.760 -31.389 -67.089  1.00 75.83           N  
-ATOM  20574  CA  TRP F  84      32.119 -31.917 -67.087  1.00 80.02           C  
-ATOM  20575  C   TRP F  84      32.902 -31.357 -65.904  1.00 80.56           C  
-ATOM  20576  O   TRP F  84      33.773 -32.026 -65.342  1.00 77.05           O  
-ATOM  20577  CB  TRP F  84      32.817 -31.583 -68.408  1.00 79.56           C  
-ATOM  20578  CG  TRP F  84      34.302 -31.773 -68.392  1.00 80.02           C  
-ATOM  20579  CD1 TRP F  84      35.244 -30.824 -68.126  1.00 77.89           C  
-ATOM  20580  CD2 TRP F  84      35.019 -32.984 -68.665  1.00 69.28           C  
-ATOM  20581  NE1 TRP F  84      36.501 -31.368 -68.210  1.00 74.33           N  
-ATOM  20582  CE2 TRP F  84      36.391 -32.692 -68.541  1.00 65.29           C  
-ATOM  20583  CE3 TRP F  84      34.635 -34.286 -68.998  1.00 74.39           C  
-ATOM  20584  CZ2 TRP F  84      37.380 -33.654 -68.737  1.00 68.63           C  
-ATOM  20585  CZ3 TRP F  84      35.619 -35.237 -69.197  1.00 67.91           C  
-ATOM  20586  CH2 TRP F  84      36.975 -34.917 -69.063  1.00 64.33           C  
-ATOM  20587  N   GLU F  85      32.576 -30.127 -65.523  1.00 76.05           N  
-ATOM  20588  CA  GLU F  85      33.254 -29.468 -64.415  1.00 79.91           C  
-ATOM  20589  C   GLU F  85      32.727 -29.950 -63.068  1.00 81.55           C  
-ATOM  20590  O   GLU F  85      33.449 -29.930 -62.073  1.00 76.27           O  
-ATOM  20591  CB  GLU F  85      33.108 -27.951 -64.535  1.00 82.76           C  
-ATOM  20592  CG  GLU F  85      33.896 -27.359 -65.691  1.00 82.77           C  
-ATOM  20593  CD  GLU F  85      33.464 -25.947 -66.033  1.00 89.64           C  
-ATOM  20594  OE1 GLU F  85      32.394 -25.517 -65.551  1.00 80.88           O  
-ATOM  20595  OE2 GLU F  85      34.195 -25.268 -66.787  1.00 83.89           O  
-ATOM  20596  N   SER F  86      31.472 -30.388 -63.042  1.00 84.04           N  
-ATOM  20597  CA  SER F  86      30.878 -30.913 -61.817  1.00 75.64           C  
-ATOM  20598  C   SER F  86      31.630 -32.145 -61.325  1.00 75.55           C  
-ATOM  20599  O   SER F  86      31.766 -32.359 -60.122  1.00 72.85           O  
-ATOM  20600  CB  SER F  86      29.400 -31.250 -62.033  1.00 60.86           C  
-ATOM  20601  OG  SER F  86      28.578 -30.118 -61.807  1.00 64.71           O  
-ATOM  20602  N   MET F  87      32.125 -32.948 -62.260  1.00 68.97           N  
-ATOM  20603  CA  MET F  87      32.868 -34.153 -61.910  1.00 63.96           C  
-ATOM  20604  C   MET F  87      34.247 -33.823 -61.349  1.00 74.49           C  
-ATOM  20605  O   MET F  87      34.986 -33.033 -61.940  1.00 70.12           O  
-ATOM  20606  CB  MET F  87      33.022 -35.066 -63.128  1.00 78.59           C  
-ATOM  20607  CG  MET F  87      31.715 -35.559 -63.726  1.00 81.07           C  
-ATOM  20608  SD  MET F  87      32.004 -36.747 -65.054  1.00 67.60           S  
-ATOM  20609  CE  MET F  87      32.943 -37.998 -64.183  1.00 70.78           C  
-ATOM  20610  N   PRO F  88      34.594 -34.429 -60.202  1.00 81.26           N  
-ATOM  20611  CA  PRO F  88      35.960 -34.374 -59.669  1.00 80.73           C  
-ATOM  20612  C   PRO F  88      36.974 -34.863 -60.701  1.00 82.64           C  
-ATOM  20613  O   PRO F  88      36.663 -35.760 -61.486  1.00 82.71           O  
-ATOM  20614  CB  PRO F  88      35.906 -35.306 -58.449  1.00 68.96           C  
-ATOM  20615  CG  PRO F  88      34.611 -36.072 -58.582  1.00 65.11           C  
-ATOM  20616  CD  PRO F  88      33.683 -35.161 -59.309  1.00 68.32           C  
-ATOM  20617  N   ARG F  89      38.166 -34.273 -60.689  1.00 82.99           N  
-ATOM  20618  CA  ARG F  89      39.166 -34.496 -61.733  1.00 79.40           C  
-ATOM  20619  C   ARG F  89      39.598 -35.954 -61.863  1.00 77.35           C  
-ATOM  20620  O   ARG F  89      39.898 -36.423 -62.961  1.00 80.04           O  
-ATOM  20621  CB  ARG F  89      40.398 -33.628 -61.474  1.00 72.82           C  
-ATOM  20622  CG  ARG F  89      40.085 -32.266 -60.882  1.00 83.59           C  
-ATOM  20623  CD  ARG F  89      40.828 -32.071 -59.568  1.00 94.72           C  
-ATOM  20624  NE  ARG F  89      40.497 -33.109 -58.594  1.00 93.00           N  
-ATOM  20625  CZ  ARG F  89      39.772 -32.903 -57.499  1.00 75.53           C  
-ATOM  20626  NH1 ARG F  89      39.308 -31.691 -57.227  1.00 65.65           N  
-ATOM  20627  NH2 ARG F  89      39.519 -33.908 -56.670  1.00 65.92           N  
-ATOM  20628  N   LYS F  90      39.633 -36.665 -60.742  1.00 69.47           N  
-ATOM  20629  CA  LYS F  90      40.061 -38.060 -60.738  1.00 75.02           C  
-ATOM  20630  C   LYS F  90      39.057 -38.952 -61.464  1.00 77.49           C  
-ATOM  20631  O   LYS F  90      39.373 -40.081 -61.840  1.00 66.97           O  
-ATOM  20632  CB  LYS F  90      40.262 -38.557 -59.305  1.00 86.22           C  
-ATOM  20633  CG  LYS F  90      38.995 -38.570 -58.465  1.00 78.16           C  
-ATOM  20634  CD  LYS F  90      39.259 -39.161 -57.090  1.00 70.20           C  
-ATOM  20635  CE  LYS F  90      37.979 -39.263 -56.280  1.00 53.03           C  
-ATOM  20636  NZ  LYS F  90      38.229 -39.844 -54.933  1.00 52.93           N  
-ATOM  20637  N   PHE F  91      37.850 -38.433 -61.662  1.00 84.06           N  
-ATOM  20638  CA  PHE F  91      36.790 -39.171 -62.339  1.00 86.38           C  
-ATOM  20639  C   PHE F  91      36.499 -38.650 -63.744  1.00 82.11           C  
-ATOM  20640  O   PHE F  91      35.878 -39.353 -64.543  1.00 68.80           O  
-ATOM  20641  CB  PHE F  91      35.499 -39.123 -61.519  1.00 80.89           C  
-ATOM  20642  CG  PHE F  91      35.389 -40.210 -60.491  1.00 83.64           C  
-ATOM  20643  CD1 PHE F  91      35.430 -41.543 -60.867  1.00 85.41           C  
-ATOM  20644  CD2 PHE F  91      35.214 -39.901 -59.152  1.00 78.67           C  
-ATOM  20645  CE1 PHE F  91      35.320 -42.548 -59.926  1.00 83.74           C  
-ATOM  20646  CE2 PHE F  91      35.101 -40.901 -58.205  1.00 77.07           C  
-ATOM  20647  CZ  PHE F  91      35.154 -42.226 -58.592  1.00 82.75           C  
-ATOM  20648  N   ARG F  92      36.949 -37.429 -64.037  1.00 81.65           N  
-ATOM  20649  CA  ARG F  92      36.504 -36.697 -65.227  1.00 79.13           C  
-ATOM  20650  C   ARG F  92      36.588 -37.501 -66.534  1.00 92.28           C  
-ATOM  20651  O   ARG F  92      35.601 -37.573 -67.266  1.00101.16           O  
-ATOM  20652  CB  ARG F  92      37.276 -35.377 -65.362  1.00 72.50           C  
-ATOM  20653  CG  ARG F  92      36.701 -34.246 -64.519  1.00 79.76           C  
-ATOM  20654  CD  ARG F  92      36.926 -32.892 -65.177  1.00 80.30           C  
-ATOM  20655  NE  ARG F  92      38.148 -32.236 -64.720  1.00 95.55           N  
-ATOM  20656  CZ  ARG F  92      38.169 -31.096 -64.035  1.00 97.95           C  
-ATOM  20657  NH1 ARG F  92      39.325 -30.565 -63.658  1.00 82.66           N  
-ATOM  20658  NH2 ARG F  92      37.032 -30.484 -63.732  1.00 95.54           N  
-ATOM  20659  N   PRO F  93      37.746 -38.117 -66.838  1.00 83.15           N  
-ATOM  20660  CA  PRO F  93      37.642 -39.017 -67.991  1.00 69.62           C  
-ATOM  20661  C   PRO F  93      36.881 -40.287 -67.620  1.00 74.92           C  
-ATOM  20662  O   PRO F  93      37.476 -41.208 -67.057  1.00 75.75           O  
-ATOM  20663  CB  PRO F  93      39.103 -39.331 -68.338  1.00 71.13           C  
-ATOM  20664  CG  PRO F  93      39.915 -38.290 -67.623  1.00 85.96           C  
-ATOM  20665  CD  PRO F  93      39.140 -37.973 -66.384  1.00 82.32           C  
-ATOM  20666  N   LEU F  94      35.583 -40.321 -67.913  1.00 68.74           N  
-ATOM  20667  CA  LEU F  94      34.755 -41.489 -67.623  1.00 70.24           C  
-ATOM  20668  C   LEU F  94      35.312 -42.728 -68.314  1.00 63.69           C  
-ATOM  20669  O   LEU F  94      35.140 -42.910 -69.518  1.00 62.04           O  
-ATOM  20670  CB  LEU F  94      33.306 -41.243 -68.050  1.00 65.76           C  
-ATOM  20671  CG  LEU F  94      32.461 -40.442 -67.055  1.00 66.13           C  
-ATOM  20672  CD1 LEU F  94      31.133 -40.029 -67.671  1.00 61.75           C  
-ATOM  20673  CD2 LEU F  94      32.236 -41.247 -65.781  1.00 64.26           C  
-ATOM  20674  N   VAL F  95      35.978 -43.574 -67.533  1.00 65.66           N  
-ATOM  20675  CA  VAL F  95      36.746 -44.696 -68.065  1.00 75.15           C  
-ATOM  20676  C   VAL F  95      35.902 -45.740 -68.799  1.00 75.47           C  
-ATOM  20677  O   VAL F  95      34.743 -45.981 -68.451  1.00 59.26           O  
-ATOM  20678  CB  VAL F  95      37.534 -45.402 -66.940  1.00 79.21           C  
-ATOM  20679  CG1 VAL F  95      38.581 -44.462 -66.355  1.00 64.64           C  
-ATOM  20680  CG2 VAL F  95      36.590 -45.903 -65.857  1.00 64.29           C  
-ATOM  20681  N   ASP F  96      36.512 -46.342 -69.821  1.00 88.54           N  
-ATOM  20682  CA  ASP F  96      35.896 -47.377 -70.658  1.00 80.66           C  
-ATOM  20683  C   ASP F  96      34.688 -46.868 -71.443  1.00 72.03           C  
-ATOM  20684  O   ASP F  96      33.839 -47.652 -71.872  1.00 60.76           O  
-ATOM  20685  CB  ASP F  96      35.498 -48.585 -69.807  1.00 68.08           C  
-ATOM  20686  CG  ASP F  96      36.664 -49.148 -69.021  1.00 87.40           C  
-ATOM  20687  OD1 ASP F  96      37.502 -49.852 -69.625  1.00 87.37           O  
-ATOM  20688  OD2 ASP F  96      36.746 -48.885 -67.801  1.00 87.08           O  
-ATOM  20689  N   ARG F  97      34.627 -45.555 -71.640  1.00 60.97           N  
-ATOM  20690  CA  ARG F  97      33.550 -44.929 -72.397  1.00 55.32           C  
-ATOM  20691  C   ARG F  97      34.072 -43.709 -73.144  1.00 58.78           C  
-ATOM  20692  O   ARG F  97      34.852 -42.928 -72.599  1.00 52.93           O  
-ATOM  20693  CB  ARG F  97      32.399 -44.523 -71.473  1.00 63.32           C  
-ATOM  20694  CG  ARG F  97      31.563 -45.684 -70.958  1.00 62.35           C  
-ATOM  20695  CD  ARG F  97      30.890 -45.334 -69.646  1.00 50.91           C  
-ATOM  20696  NE  ARG F  97      31.851 -45.221 -68.554  1.00 68.78           N  
-ATOM  20697  CZ  ARG F  97      31.546 -44.794 -67.333  1.00 73.66           C  
-ATOM  20698  NH1 ARG F  97      30.303 -44.433 -67.047  1.00 70.15           N  
-ATOM  20699  NH2 ARG F  97      32.485 -44.723 -66.399  1.00 72.70           N  
-ATOM  20700  N   LEU F  98      33.646 -43.549 -74.392  1.00 61.60           N  
-ATOM  20701  CA  LEU F  98      34.027 -42.382 -75.179  1.00 65.21           C  
-ATOM  20702  C   LEU F  98      33.361 -41.146 -74.583  1.00 61.75           C  
-ATOM  20703  O   LEU F  98      32.154 -41.133 -74.384  1.00 57.76           O  
-ATOM  20704  CB  LEU F  98      33.628 -42.569 -76.648  1.00 72.01           C  
-ATOM  20705  CG  LEU F  98      34.296 -41.732 -77.748  1.00 72.78           C  
-ATOM  20706  CD1 LEU F  98      33.756 -40.306 -77.807  1.00 55.65           C  
-ATOM  20707  CD2 LEU F  98      35.809 -41.730 -77.576  1.00 79.03           C  
-ATOM  20708  N   ASN F  99      34.142 -40.112 -74.291  1.00 56.30           N  
-ATOM  20709  CA  ASN F  99      33.581 -38.899 -73.703  1.00 56.60           C  
-ATOM  20710  C   ASN F  99      33.399 -37.782 -74.723  1.00 49.31           C  
-ATOM  20711  O   ASN F  99      34.265 -37.555 -75.566  1.00 65.57           O  
-ATOM  20712  CB  ASN F  99      34.459 -38.406 -72.550  1.00 66.57           C  
-ATOM  20713  CG  ASN F  99      34.353 -39.286 -71.317  1.00 71.80           C  
-ATOM  20714  OD1 ASN F  99      34.164 -40.499 -71.419  1.00 59.34           O  
-ATOM  20715  ND2 ASN F  99      34.464 -38.674 -70.141  1.00 63.00           N  
-ATOM  20716  N   ILE F 100      32.264 -37.092 -74.645  1.00 52.52           N  
-ATOM  20717  CA  ILE F 100      32.007 -35.940 -75.506  1.00 69.91           C  
-ATOM  20718  C   ILE F 100      31.450 -34.757 -74.717  1.00 65.99           C  
-ATOM  20719  O   ILE F 100      30.260 -34.707 -74.408  1.00 70.49           O  
-ATOM  20720  CB  ILE F 100      31.020 -36.279 -76.647  1.00 63.97           C  
-ATOM  20721  CG1 ILE F 100      31.572 -37.401 -77.527  1.00 58.16           C  
-ATOM  20722  CG2 ILE F 100      30.741 -35.047 -77.500  1.00 57.87           C  
-ATOM  20723  CD1 ILE F 100      30.706 -37.713 -78.727  1.00 65.83           C  
-ATOM  20724  N   VAL F 101      32.321 -33.810 -74.387  1.00 57.79           N  
-ATOM  20725  CA  VAL F 101      31.892 -32.561 -73.769  1.00 61.57           C  
-ATOM  20726  C   VAL F 101      31.378 -31.637 -74.865  1.00 55.42           C  
-ATOM  20727  O   VAL F 101      31.932 -31.615 -75.962  1.00 60.38           O  
-ATOM  20728  CB  VAL F 101      33.040 -31.876 -73.001  1.00 64.63           C  
-ATOM  20729  CG1 VAL F 101      32.549 -30.613 -72.308  1.00 70.25           C  
-ATOM  20730  CG2 VAL F 101      33.649 -32.835 -71.994  1.00 61.29           C  
-ATOM  20731  N   VAL F 102      30.318 -30.886 -74.589  1.00 56.10           N  
-ATOM  20732  CA  VAL F 102      29.818 -29.943 -75.581  1.00 57.67           C  
-ATOM  20733  C   VAL F 102      29.844 -28.501 -75.075  1.00 73.82           C  
-ATOM  20734  O   VAL F 102      29.306 -28.185 -74.012  1.00 87.41           O  
-ATOM  20735  CB  VAL F 102      28.384 -30.318 -76.037  1.00 53.39           C  
-ATOM  20736  CG1 VAL F 102      28.414 -31.581 -76.885  1.00 58.37           C  
-ATOM  20737  CG2 VAL F 102      27.463 -30.495 -74.843  1.00 72.14           C  
-ATOM  20738  N   SER F 103      30.492 -27.633 -75.846  1.00 79.72           N  
-ATOM  20739  CA  SER F 103      30.584 -26.207 -75.523  1.00 93.30           C  
-ATOM  20740  C   SER F 103      31.125 -25.440 -76.725  1.00 87.21           C  
-ATOM  20741  O   SER F 103      31.011 -25.887 -77.863  1.00 80.30           O  
-ATOM  20742  CB  SER F 103      31.480 -25.971 -74.300  1.00 79.82           C  
-ATOM  20743  OG  SER F 103      31.555 -24.602 -73.966  1.00 73.26           O  
-ATOM  20744  N   SER F 104      31.714 -24.279 -76.463  1.00 85.71           N  
-ATOM  20745  CA  SER F 104      32.334 -23.482 -77.512  1.00 75.75           C  
-ATOM  20746  C   SER F 104      33.529 -22.719 -76.960  1.00 81.09           C  
-ATOM  20747  O   SER F 104      34.062 -21.825 -77.617  1.00 80.65           O  
-ATOM  20748  CB  SER F 104      31.318 -22.514 -78.125  1.00 76.90           C  
-ATOM  20749  OG  SER F 104      30.811 -21.616 -77.151  1.00 69.75           O  
-ATOM  20750  N   SER F 105      33.952 -23.083 -75.754  1.00 79.39           N  
-ATOM  20751  CA  SER F 105      35.005 -22.344 -75.069  1.00 89.14           C  
-ATOM  20752  C   SER F 105      36.201 -23.211 -74.666  1.00 85.10           C  
-ATOM  20753  O   SER F 105      37.325 -22.715 -74.566  1.00 93.66           O  
-ATOM  20754  CB  SER F 105      34.431 -21.654 -73.828  1.00 89.33           C  
-ATOM  20755  OG  SER F 105      33.403 -20.741 -74.180  1.00 82.14           O  
-ATOM  20756  N   LEU F 106      35.966 -24.501 -74.446  1.00 64.84           N  
-ATOM  20757  CA  LEU F 106      36.988 -25.360 -73.851  1.00 71.51           C  
-ATOM  20758  C   LEU F 106      37.899 -26.065 -74.856  1.00 66.23           C  
-ATOM  20759  O   LEU F 106      37.681 -26.010 -76.067  1.00 65.94           O  
-ATOM  20760  CB  LEU F 106      36.327 -26.403 -72.949  1.00 81.29           C  
-ATOM  20761  CG  LEU F 106      35.577 -25.828 -71.745  1.00 95.37           C  
-ATOM  20762  CD1 LEU F 106      35.195 -26.931 -70.770  1.00 79.38           C  
-ATOM  20763  CD2 LEU F 106      36.399 -24.749 -71.051  1.00 87.75           C  
-ATOM  20764  N   LYS F 107      38.920 -26.731 -74.321  1.00 62.80           N  
-ATOM  20765  CA  LYS F 107      39.954 -27.392 -75.113  1.00 58.44           C  
-ATOM  20766  C   LYS F 107      39.380 -28.501 -75.990  1.00 57.01           C  
-ATOM  20767  O   LYS F 107      40.028 -29.524 -76.220  1.00 50.98           O  
-ATOM  20768  CB  LYS F 107      41.035 -27.966 -74.189  1.00 63.17           C  
-ATOM  20769  CG  LYS F 107      42.430 -28.003 -74.792  1.00 69.22           C  
-ATOM  20770  CD  LYS F 107      43.297 -29.046 -74.103  1.00 66.37           C  
-ATOM  20771  CE  LYS F 107      43.497 -30.265 -74.992  1.00 69.65           C  
-ATOM  20772  NZ  LYS F 107      42.218 -30.745 -75.594  1.00 46.12           N  
-ATOM  20773  N   VAL F 126      35.156 -33.136 -78.241  1.00 25.26           N  
-ATOM  20774  CA  VAL F 126      34.539 -31.874 -77.844  1.00 55.47           C  
-ATOM  20775  C   VAL F 126      33.859 -31.193 -79.028  1.00 51.19           C  
-ATOM  20776  O   VAL F 126      34.523 -30.687 -79.932  1.00 51.02           O  
-ATOM  20777  CB  VAL F 126      35.570 -30.908 -77.230  1.00 50.20           C  
-ATOM  20778  CG1 VAL F 126      34.910 -29.581 -76.871  1.00 33.93           C  
-ATOM  20779  CG2 VAL F 126      36.219 -31.538 -76.008  1.00 40.75           C  
-ATOM  20780  N   CYS F 127      32.530 -31.180 -79.012  1.00 48.75           N  
-ATOM  20781  CA  CYS F 127      31.755 -30.622 -80.112  1.00 50.11           C  
-ATOM  20782  C   CYS F 127      31.083 -29.314 -79.707  1.00 59.88           C  
-ATOM  20783  O   CYS F 127      31.082 -28.946 -78.532  1.00 64.56           O  
-ATOM  20784  CB  CYS F 127      30.716 -31.634 -80.586  1.00 55.80           C  
-ATOM  20785  SG  CYS F 127      31.406 -33.283 -80.855  1.00 71.29           S  
-ATOM  20786  N   ALA F 128      30.513 -28.616 -80.685  1.00 58.94           N  
-ATOM  20787  CA  ALA F 128      29.934 -27.297 -80.448  1.00 65.92           C  
-ATOM  20788  C   ALA F 128      28.422 -27.357 -80.256  1.00 68.59           C  
-ATOM  20789  O   ALA F 128      27.785 -26.348 -79.946  1.00 65.79           O  
-ATOM  20790  CB  ALA F 128      30.284 -26.357 -81.593  1.00 68.91           C  
-ATOM  20791  N   SER F 129      27.855 -28.542 -80.444  1.00 68.30           N  
-ATOM  20792  CA  SER F 129      26.428 -28.756 -80.236  1.00 69.88           C  
-ATOM  20793  C   SER F 129      26.139 -30.245 -80.154  1.00 72.87           C  
-ATOM  20794  O   SER F 129      26.989 -31.069 -80.488  1.00 66.89           O  
-ATOM  20795  CB  SER F 129      25.608 -28.122 -81.361  1.00 68.48           C  
-ATOM  20796  OG  SER F 129      25.785 -28.827 -82.576  1.00 65.70           O  
-ATOM  20797  N   LEU F 130      24.937 -30.586 -79.704  1.00 73.40           N  
-ATOM  20798  CA  LEU F 130      24.517 -31.980 -79.631  1.00 71.06           C  
-ATOM  20799  C   LEU F 130      24.360 -32.628 -81.014  1.00 76.79           C  
-ATOM  20800  O   LEU F 130      24.793 -33.769 -81.200  1.00 67.07           O  
-ATOM  20801  CB  LEU F 130      23.211 -32.105 -78.839  1.00 64.09           C  
-ATOM  20802  CG  LEU F 130      22.707 -33.530 -78.604  1.00 56.28           C  
-ATOM  20803  CD1 LEU F 130      23.772 -34.375 -77.925  1.00 53.84           C  
-ATOM  20804  CD2 LEU F 130      21.440 -33.501 -77.777  1.00 58.10           C  
-ATOM  20805  N   PRO F 131      23.737 -31.922 -81.985  1.00 83.46           N  
-ATOM  20806  CA  PRO F 131      23.720 -32.518 -83.327  1.00 80.35           C  
-ATOM  20807  C   PRO F 131      25.121 -32.764 -83.874  1.00 76.11           C  
-ATOM  20808  O   PRO F 131      25.350 -33.775 -84.537  1.00 69.04           O  
-ATOM  20809  CB  PRO F 131      22.987 -31.469 -84.170  1.00 76.39           C  
-ATOM  20810  CG  PRO F 131      22.129 -30.760 -83.210  1.00 69.27           C  
-ATOM  20811  CD  PRO F 131      22.906 -30.703 -81.931  1.00 65.69           C  
-ATOM  20812  N   ALA F 132      26.038 -31.842 -83.602  1.00 72.80           N  
-ATOM  20813  CA  ALA F 132      27.427 -32.010 -84.002  1.00 76.00           C  
-ATOM  20814  C   ALA F 132      28.036 -33.217 -83.299  1.00 78.68           C  
-ATOM  20815  O   ALA F 132      28.833 -33.948 -83.882  1.00 72.82           O  
-ATOM  20816  CB  ALA F 132      28.228 -30.752 -83.696  1.00 61.76           C  
-ATOM  20817  N   ALA F 133      27.649 -33.418 -82.044  1.00 79.27           N  
-ATOM  20818  CA  ALA F 133      28.139 -34.541 -81.257  1.00 78.15           C  
-ATOM  20819  C   ALA F 133      27.668 -35.857 -81.850  1.00 78.20           C  
-ATOM  20820  O   ALA F 133      28.397 -36.849 -81.840  1.00 71.14           O  
-ATOM  20821  CB  ALA F 133      27.685 -34.416 -79.812  1.00 78.77           C  
-ATOM  20822  N   LEU F 134      26.443 -35.860 -82.363  1.00 73.97           N  
-ATOM  20823  CA  LEU F 134      25.895 -37.038 -83.017  1.00 75.84           C  
-ATOM  20824  C   LEU F 134      26.601 -37.280 -84.347  1.00 83.33           C  
-ATOM  20825  O   LEU F 134      26.918 -38.417 -84.702  1.00 72.47           O  
-ATOM  20826  CB  LEU F 134      24.390 -36.876 -83.226  1.00 77.89           C  
-ATOM  20827  CG  LEU F 134      23.565 -36.697 -81.949  1.00 64.26           C  
-ATOM  20828  CD1 LEU F 134      22.116 -36.386 -82.281  1.00 59.38           C  
-ATOM  20829  CD2 LEU F 134      23.663 -37.936 -81.080  1.00 54.15           C  
-ATOM  20830  N   SER F 135      26.848 -36.193 -85.072  1.00 81.59           N  
-ATOM  20831  CA  SER F 135      27.534 -36.253 -86.356  1.00 71.86           C  
-ATOM  20832  C   SER F 135      28.933 -36.834 -86.196  1.00 79.36           C  
-ATOM  20833  O   SER F 135      29.377 -37.633 -87.016  1.00 83.82           O  
-ATOM  20834  CB  SER F 135      27.612 -34.862 -86.989  1.00 63.58           C  
-ATOM  20835  OG  SER F 135      26.320 -34.313 -87.185  1.00 56.07           O  
-ATOM  20836  N   LEU F 136      29.616 -36.433 -85.127  1.00 79.49           N  
-ATOM  20837  CA  LEU F 136      30.954 -36.930 -84.821  1.00 88.17           C  
-ATOM  20838  C   LEU F 136      30.927 -38.415 -84.472  1.00 85.89           C  
-ATOM  20839  O   LEU F 136      31.951 -39.097 -84.523  1.00 75.55           O  
-ATOM  20840  CB  LEU F 136      31.570 -36.129 -83.669  1.00 80.30           C  
-ATOM  20841  CG  LEU F 136      32.543 -35.004 -84.030  1.00 90.02           C  
-ATOM  20842  CD1 LEU F 136      33.894 -35.567 -84.451  1.00 84.45           C  
-ATOM  20843  CD2 LEU F 136      31.968 -34.120 -85.126  1.00 86.87           C  
-ATOM  20844  N   LEU F 137      29.747 -38.908 -84.113  1.00 84.66           N  
-ATOM  20845  CA  LEU F 137      29.579 -40.311 -83.765  1.00 81.81           C  
-ATOM  20846  C   LEU F 137      29.158 -41.133 -84.977  1.00 79.53           C  
-ATOM  20847  O   LEU F 137      29.384 -42.341 -85.024  1.00 70.31           O  
-ATOM  20848  CB  LEU F 137      28.555 -40.464 -82.641  1.00 92.44           C  
-ATOM  20849  CG  LEU F 137      28.983 -39.997 -81.248  1.00 92.20           C  
-ATOM  20850  CD1 LEU F 137      27.789 -39.989 -80.311  1.00 86.24           C  
-ATOM  20851  CD2 LEU F 137      30.099 -40.874 -80.691  1.00 83.24           C  
-ATOM  20852  N   GLU F 138      28.542 -40.477 -85.954  1.00 88.15           N  
-ATOM  20853  CA  GLU F 138      28.150 -41.156 -87.184  1.00 89.93           C  
-ATOM  20854  C   GLU F 138      29.318 -41.246 -88.156  1.00 90.06           C  
-ATOM  20855  O   GLU F 138      29.574 -42.305 -88.731  1.00 84.90           O  
-ATOM  20856  CB  GLU F 138      26.976 -40.440 -87.846  1.00 80.78           C  
-ATOM  20857  CG  GLU F 138      25.672 -41.211 -87.773  1.00 89.80           C  
-ATOM  20858  CD  GLU F 138      24.522 -40.470 -88.423  1.00 97.68           C  
-ATOM  20859  OE1 GLU F 138      24.641 -40.108 -89.613  1.00 89.81           O  
-ATOM  20860  OE2 GLU F 138      23.502 -40.243 -87.741  1.00 93.57           O  
-ATOM  20861  N   GLU F 139      30.013 -40.126 -88.338  1.00 87.68           N  
-ATOM  20862  CA  GLU F 139      31.176 -40.063 -89.216  1.00 84.70           C  
-ATOM  20863  C   GLU F 139      32.222 -41.078 -88.776  1.00 90.48           C  
-ATOM  20864  O   GLU F 139      32.324 -42.162 -89.349  1.00 85.67           O  
-ATOM  20865  CB  GLU F 139      31.774 -38.652 -89.226  1.00 75.20           C  
-ATOM  20866  CG  GLU F 139      33.046 -38.515 -90.060  1.00 83.78           C  
-ATOM  20867  CD  GLU F 139      32.786 -38.576 -91.555  1.00101.52           C  
-ATOM  20868  OE1 GLU F 139      32.487 -37.517 -92.147  1.00 96.38           O  
-ATOM  20869  OE2 GLU F 139      32.892 -39.676 -92.140  1.00 95.10           O  
-ATOM  20870  N   GLU F 140      32.995 -40.727 -87.756  1.00 88.10           N  
-ATOM  20871  CA  GLU F 140      33.938 -41.667 -87.175  1.00 71.55           C  
-ATOM  20872  C   GLU F 140      33.252 -42.431 -86.057  1.00 88.18           C  
-ATOM  20873  O   GLU F 140      32.089 -42.167 -85.743  1.00 90.68           O  
-ATOM  20874  CB  GLU F 140      35.184 -40.948 -86.660  1.00 63.46           C  
-ATOM  20875  CG  GLU F 140      34.894 -39.640 -85.949  1.00 76.22           C  
-ATOM  20876  CD  GLU F 140      35.820 -38.524 -86.393  1.00 72.82           C  
-ATOM  20877  OE1 GLU F 140      35.362 -37.642 -87.149  1.00 68.18           O  
-ATOM  20878  OE2 GLU F 140      37.004 -38.529 -85.990  1.00 52.37           O  
-ATOM  20879  N   TYR F 141      33.974 -43.387 -85.478  1.00 90.14           N  
-ATOM  20880  CA  TYR F 141      33.457 -44.264 -84.428  1.00 84.99           C  
-ATOM  20881  C   TYR F 141      32.294 -45.143 -84.884  1.00 86.53           C  
-ATOM  20882  O   TYR F 141      31.745 -45.882 -84.073  1.00 79.38           O  
-ATOM  20883  CB  TYR F 141      32.997 -43.462 -83.205  1.00 77.23           C  
-ATOM  20884  CG  TYR F 141      34.005 -42.492 -82.640  1.00 76.00           C  
-ATOM  20885  CD1 TYR F 141      35.040 -42.930 -81.824  1.00 67.61           C  
-ATOM  20886  CD2 TYR F 141      33.900 -41.131 -82.894  1.00 81.37           C  
-ATOM  20887  CE1 TYR F 141      35.956 -42.039 -81.294  1.00 65.01           C  
-ATOM  20888  CE2 TYR F 141      34.809 -40.233 -82.371  1.00 68.38           C  
-ATOM  20889  CZ  TYR F 141      35.835 -40.691 -81.571  1.00 68.25           C  
-ATOM  20890  OH  TYR F 141      36.740 -39.797 -81.048  1.00 57.36           O  
-ATOM  20891  N   LYS F 142      31.920 -45.068 -86.162  1.00 90.52           N  
-ATOM  20892  CA  LYS F 142      30.774 -45.823 -86.680  1.00 90.89           C  
-ATOM  20893  C   LYS F 142      30.885 -47.299 -86.312  1.00 88.84           C  
-ATOM  20894  O   LYS F 142      29.883 -47.975 -86.075  1.00 74.86           O  
-ATOM  20895  CB  LYS F 142      30.654 -45.669 -88.197  1.00 85.49           C  
-ATOM  20896  CG  LYS F 142      29.423 -46.350 -88.786  1.00 86.93           C  
-ATOM  20897  CD  LYS F 142      28.145 -45.603 -88.423  1.00 91.01           C  
-ATOM  20898  CE  LYS F 142      26.921 -46.502 -88.544  1.00 75.19           C  
-ATOM  20899  NZ  LYS F 142      26.850 -47.192 -89.862  1.00 63.34           N  
-ATOM  20900  N   ASP F 143      32.119 -47.786 -86.263  1.00 95.28           N  
-ATOM  20901  CA  ASP F 143      32.408 -49.067 -85.644  1.00 91.97           C  
-ATOM  20902  C   ASP F 143      32.971 -48.810 -84.251  1.00 92.15           C  
-ATOM  20903  O   ASP F 143      33.657 -47.808 -84.037  1.00 87.14           O  
-ATOM  20904  CB  ASP F 143      33.388 -49.878 -86.490  1.00 93.83           C  
-ATOM  20905  CG  ASP F 143      32.903 -50.074 -87.913  1.00 91.17           C  
-ATOM  20906  OD1 ASP F 143      32.303 -49.130 -88.470  1.00 92.85           O  
-ATOM  20907  OD2 ASP F 143      33.114 -51.170 -88.474  1.00 83.08           O  
-ATOM  20908  N   SER F 144      32.634 -49.713 -83.328  1.00 96.80           N  
-ATOM  20909  CA  SER F 144      33.075 -49.745 -81.922  1.00103.70           C  
-ATOM  20910  C   SER F 144      32.165 -48.975 -80.959  1.00 93.06           C  
-ATOM  20911  O   SER F 144      32.257 -49.171 -79.747  1.00 92.20           O  
-ATOM  20912  CB  SER F 144      34.515 -49.238 -81.761  1.00 99.73           C  
-ATOM  20913  OG  SER F 144      35.425 -50.037 -82.497  1.00105.10           O  
-ATOM  20914  N   VAL F 145      31.293 -48.106 -81.467  1.00 87.71           N  
-ATOM  20915  CA  VAL F 145      30.318 -47.485 -80.574  1.00 72.28           C  
-ATOM  20916  C   VAL F 145      29.003 -48.266 -80.640  1.00 76.15           C  
-ATOM  20917  O   VAL F 145      28.455 -48.524 -81.714  1.00 87.84           O  
-ATOM  20918  CB  VAL F 145      30.093 -45.970 -80.882  1.00 73.99           C  
-ATOM  20919  CG1 VAL F 145      29.349 -45.749 -82.192  1.00 84.95           C  
-ATOM  20920  CG2 VAL F 145      29.348 -45.308 -79.733  1.00 73.65           C  
-ATOM  20921  N   ASP F 146      28.531 -48.688 -79.473  1.00 68.50           N  
-ATOM  20922  CA  ASP F 146      27.304 -49.465 -79.378  1.00 65.16           C  
-ATOM  20923  C   ASP F 146      26.104 -48.531 -79.351  1.00 66.66           C  
-ATOM  20924  O   ASP F 146      25.530 -48.200 -80.389  1.00 62.16           O  
-ATOM  20925  CB  ASP F 146      27.323 -50.354 -78.129  1.00 62.21           C  
-ATOM  20926  CG  ASP F 146      26.031 -51.133 -77.941  1.00 69.25           C  
-ATOM  20927  OD1 ASP F 146      25.364 -51.439 -78.953  1.00 62.64           O  
-ATOM  20928  OD2 ASP F 146      25.681 -51.438 -76.780  1.00 71.46           O  
-ATOM  20929  N   GLN F 147      25.736 -48.112 -78.146  1.00 71.26           N  
-ATOM  20930  CA  GLN F 147      24.665 -47.150 -77.946  1.00 66.14           C  
-ATOM  20931  C   GLN F 147      25.228 -45.919 -77.254  1.00 60.33           C  
-ATOM  20932  O   GLN F 147      26.264 -45.993 -76.590  1.00 52.66           O  
-ATOM  20933  CB  GLN F 147      23.534 -47.762 -77.120  1.00 60.80           C  
-ATOM  20934  CG  GLN F 147      24.005 -48.422 -75.835  1.00 56.83           C  
-ATOM  20935  CD  GLN F 147      22.857 -48.876 -74.957  1.00 52.30           C  
-ATOM  20936  OE1 GLN F 147      21.688 -48.714 -75.309  1.00 46.05           O  
-ATOM  20937  NE2 GLN F 147      23.185 -49.446 -73.804  1.00 56.74           N  
-ATOM  20938  N   ILE F 148      24.553 -44.787 -77.405  1.00 56.69           N  
-ATOM  20939  CA  ILE F 148      25.041 -43.555 -76.807  1.00 58.80           C  
-ATOM  20940  C   ILE F 148      24.187 -43.143 -75.613  1.00 64.39           C  
-ATOM  20941  O   ILE F 148      23.081 -43.649 -75.420  1.00 68.31           O  
-ATOM  20942  CB  ILE F 148      25.079 -42.403 -77.830  1.00 57.35           C  
-ATOM  20943  CG1 ILE F 148      23.767 -41.620 -77.819  1.00 60.26           C  
-ATOM  20944  CG2 ILE F 148      25.389 -42.934 -79.224  1.00 47.01           C  
-ATOM  20945  CD1 ILE F 148      23.912 -40.222 -78.351  1.00 67.79           C  
-ATOM  20946  N   PHE F 149      24.720 -42.229 -74.810  1.00 63.88           N  
-ATOM  20947  CA  PHE F 149      24.023 -41.723 -73.637  1.00 51.69           C  
-ATOM  20948  C   PHE F 149      24.214 -40.217 -73.500  1.00 51.26           C  
-ATOM  20949  O   PHE F 149      25.198 -39.660 -73.986  1.00 55.68           O  
-ATOM  20950  CB  PHE F 149      24.517 -42.422 -72.369  1.00 46.63           C  
-ATOM  20951  CG  PHE F 149      24.137 -43.870 -72.280  1.00 45.08           C  
-ATOM  20952  CD1 PHE F 149      22.828 -44.238 -72.029  1.00 45.45           C  
-ATOM  20953  CD2 PHE F 149      25.092 -44.864 -72.423  1.00 51.44           C  
-ATOM  20954  CE1 PHE F 149      22.474 -45.568 -71.934  1.00 55.46           C  
-ATOM  20955  CE2 PHE F 149      24.744 -46.198 -72.329  1.00 48.71           C  
-ATOM  20956  CZ  PHE F 149      23.433 -46.549 -72.084  1.00 52.20           C  
-ATOM  20957  N   VAL F 150      23.263 -39.562 -72.841  1.00 47.36           N  
-ATOM  20958  CA  VAL F 150      23.400 -38.153 -72.494  1.00 44.14           C  
-ATOM  20959  C   VAL F 150      23.241 -37.992 -70.984  1.00 47.56           C  
-ATOM  20960  O   VAL F 150      22.206 -38.347 -70.419  1.00 48.65           O  
-ATOM  20961  CB  VAL F 150      22.370 -37.273 -73.226  1.00 37.00           C  
-ATOM  20962  CG1 VAL F 150      22.620 -35.803 -72.925  1.00 37.90           C  
-ATOM  20963  CG2 VAL F 150      22.421 -37.527 -74.723  1.00 47.03           C  
-ATOM  20964  N   VAL F 151      24.272 -37.458 -70.336  1.00 46.78           N  
-ATOM  20965  CA  VAL F 151      24.320 -37.416 -68.879  1.00 36.87           C  
-ATOM  20966  C   VAL F 151      24.386 -35.991 -68.329  1.00 31.30           C  
-ATOM  20967  O   VAL F 151      24.187 -35.017 -69.057  1.00 28.80           O  
-ATOM  20968  CB  VAL F 151      25.528 -38.208 -68.354  1.00 38.51           C  
-ATOM  20969  CG1 VAL F 151      25.566 -39.589 -68.991  1.00 34.78           C  
-ATOM  20970  CG2 VAL F 151      26.815 -37.462 -68.648  1.00 42.38           C  
-ATOM  20971  N   GLY F 153      24.035 -32.352 -68.621  1.00 28.40           N  
-ATOM  20972  CA  GLY F 153      23.135 -31.636 -67.734  1.00 46.15           C  
-ATOM  20973  C   GLY F 153      21.940 -31.056 -68.467  1.00 57.70           C  
-ATOM  20974  O   GLY F 153      21.706 -31.375 -69.633  1.00 56.55           O  
-ATOM  20975  N   ALA F 154      21.180 -30.205 -67.783  1.00 54.60           N  
-ATOM  20976  CA  ALA F 154      20.006 -29.580 -68.384  1.00 47.39           C  
-ATOM  20977  C   ALA F 154      20.422 -28.688 -69.538  1.00 60.21           C  
-ATOM  20978  O   ALA F 154      21.538 -28.169 -69.565  1.00 68.68           O  
-ATOM  20979  CB  ALA F 154      19.230 -28.787 -67.352  1.00 45.67           C  
-ATOM  20980  N   GLY F 155      19.523 -28.509 -70.496  1.00 62.99           N  
-ATOM  20981  CA  GLY F 155      19.873 -27.800 -71.709  1.00 69.30           C  
-ATOM  20982  C   GLY F 155      20.339 -28.789 -72.755  1.00 58.79           C  
-ATOM  20983  O   GLY F 155      19.950 -28.701 -73.915  1.00 68.63           O  
-ATOM  20984  N   LEU F 156      21.184 -29.729 -72.346  1.00 50.27           N  
-ATOM  20985  CA  LEU F 156      21.552 -30.840 -73.209  1.00 58.78           C  
-ATOM  20986  C   LEU F 156      20.393 -31.821 -73.241  1.00 61.92           C  
-ATOM  20987  O   LEU F 156      20.071 -32.390 -74.282  1.00 63.85           O  
-ATOM  20988  CB  LEU F 156      22.831 -31.522 -72.721  1.00 47.99           C  
-ATOM  20989  CG  LEU F 156      23.613 -32.229 -73.828  1.00 51.46           C  
-ATOM  20990  CD1 LEU F 156      23.946 -31.226 -74.916  1.00 63.49           C  
-ATOM  20991  CD2 LEU F 156      24.873 -32.864 -73.270  1.00 46.33           C  
-ATOM  20992  N   TYR F 157      19.774 -32.009 -72.081  1.00 54.75           N  
-ATOM  20993  CA  TYR F 157      18.551 -32.791 -71.974  1.00 46.63           C  
-ATOM  20994  C   TYR F 157      17.454 -32.177 -72.828  1.00 51.70           C  
-ATOM  20995  O   TYR F 157      16.795 -32.873 -73.598  1.00 50.83           O  
-ATOM  20996  CB  TYR F 157      18.083 -32.881 -70.517  1.00 45.45           C  
-ATOM  20997  CG  TYR F 157      18.980 -33.703 -69.618  1.00 42.96           C  
-ATOM  20998  CD1 TYR F 157      19.592 -34.859 -70.081  1.00 45.17           C  
-ATOM  20999  CD2 TYR F 157      19.207 -33.323 -68.302  1.00 38.26           C  
-ATOM  21000  CE1 TYR F 157      20.404 -35.612 -69.260  1.00 40.69           C  
-ATOM  21001  CE2 TYR F 157      20.018 -34.070 -67.473  1.00 35.01           C  
-ATOM  21002  CZ  TYR F 157      20.617 -35.210 -67.958  1.00 36.71           C  
-ATOM  21003  OH  TYR F 157      21.424 -35.960 -67.135  1.00 36.82           O  
-ATOM  21004  N   GLU F 158      17.260 -30.868 -72.684  1.00 58.43           N  
-ATOM  21005  CA  GLU F 158      16.198 -30.175 -73.408  1.00 68.30           C  
-ATOM  21006  C   GLU F 158      16.505 -30.094 -74.898  1.00 66.02           C  
-ATOM  21007  O   GLU F 158      15.591 -30.017 -75.720  1.00 60.58           O  
-ATOM  21008  CB  GLU F 158      15.972 -28.770 -72.835  1.00 68.79           C  
-ATOM  21009  CG  GLU F 158      16.846 -27.683 -73.429  1.00 82.70           C  
-ATOM  21010  CD  GLU F 158      16.894 -26.442 -72.559  1.00 84.25           C  
-ATOM  21011  OE1 GLU F 158      16.363 -26.491 -71.430  1.00 78.43           O  
-ATOM  21012  OE2 GLU F 158      17.465 -25.421 -73.000  1.00 76.66           O  
-ATOM  21013  N   ALA F 159      17.789 -30.107 -75.244  1.00 56.99           N  
-ATOM  21014  CA  ALA F 159      18.184 -30.136 -76.643  1.00 55.47           C  
-ATOM  21015  C   ALA F 159      17.843 -31.488 -77.231  1.00 59.67           C  
-ATOM  21016  O   ALA F 159      17.261 -31.583 -78.304  1.00 68.79           O  
-ATOM  21017  CB  ALA F 159      19.668 -29.850 -76.795  1.00 63.01           C  
-ATOM  21018  N   ALA F 160      18.209 -32.532 -76.496  1.00 53.84           N  
-ATOM  21019  CA  ALA F 160      17.953 -33.913 -76.887  1.00 47.46           C  
-ATOM  21020  C   ALA F 160      16.460 -34.186 -77.021  1.00 55.11           C  
-ATOM  21021  O   ALA F 160      16.038 -34.988 -77.854  1.00 49.80           O  
-ATOM  21022  CB  ALA F 160      18.568 -34.862 -75.879  1.00 44.26           C  
-ATOM  21023  N   LEU F 161      15.667 -33.516 -76.192  1.00 53.77           N  
-ATOM  21024  CA  LEU F 161      14.222 -33.690 -76.205  1.00 47.36           C  
-ATOM  21025  C   LEU F 161      13.563 -32.898 -77.330  1.00 56.88           C  
-ATOM  21026  O   LEU F 161      12.699 -33.420 -78.037  1.00 56.40           O  
-ATOM  21027  CB  LEU F 161      13.629 -33.283 -74.856  1.00 47.11           C  
-ATOM  21028  CG  LEU F 161      13.752 -34.325 -73.741  1.00 42.75           C  
-ATOM  21029  CD1 LEU F 161      13.226 -33.785 -72.419  1.00 41.01           C  
-ATOM  21030  CD2 LEU F 161      13.022 -35.601 -74.128  1.00 41.18           C  
-ATOM  21031  N   SER F 162      13.965 -31.640 -77.492  1.00 54.81           N  
-ATOM  21032  CA  SER F 162      13.393 -30.796 -78.538  1.00 54.67           C  
-ATOM  21033  C   SER F 162      13.766 -31.311 -79.927  1.00 60.51           C  
-ATOM  21034  O   SER F 162      12.983 -31.203 -80.870  1.00 71.88           O  
-ATOM  21035  CB  SER F 162      13.844 -29.345 -78.367  1.00 52.41           C  
-ATOM  21036  OG  SER F 162      15.252 -29.254 -78.266  1.00 71.45           O  
-ATOM  21037  N   LEU F 163      14.961 -31.882 -80.044  1.00 54.48           N  
-ATOM  21038  CA  LEU F 163      15.414 -32.481 -81.295  1.00 44.79           C  
-ATOM  21039  C   LEU F 163      14.855 -33.891 -81.446  1.00 47.91           C  
-ATOM  21040  O   LEU F 163      15.116 -34.567 -82.442  1.00 51.94           O  
-ATOM  21041  CB  LEU F 163      16.944 -32.505 -81.363  1.00 55.39           C  
-ATOM  21042  CG  LEU F 163      17.635 -31.138 -81.368  1.00 67.82           C  
-ATOM  21043  CD1 LEU F 163      19.143 -31.291 -81.212  1.00 67.61           C  
-ATOM  21044  CD2 LEU F 163      17.294 -30.354 -82.627  1.00 73.65           C  
-ATOM  21045  N   GLY F 164      14.095 -34.324 -80.442  1.00 56.53           N  
-ATOM  21046  CA  GLY F 164      13.362 -35.579 -80.486  1.00 58.38           C  
-ATOM  21047  C   GLY F 164      14.167 -36.804 -80.872  1.00 59.61           C  
-ATOM  21048  O   GLY F 164      13.725 -37.607 -81.693  1.00 61.69           O  
-ATOM  21049  N   VAL F 165      15.345 -36.955 -80.276  1.00 58.00           N  
-ATOM  21050  CA  VAL F 165      16.227 -38.067 -80.613  1.00 61.75           C  
-ATOM  21051  C   VAL F 165      16.348 -39.084 -79.478  1.00 67.97           C  
-ATOM  21052  O   VAL F 165      16.893 -40.172 -79.666  1.00 71.13           O  
-ATOM  21053  CB  VAL F 165      17.631 -37.565 -80.989  1.00 54.69           C  
-ATOM  21054  CG1 VAL F 165      17.586 -36.826 -82.318  1.00 60.13           C  
-ATOM  21055  CG2 VAL F 165      18.185 -36.669 -79.893  1.00 49.24           C  
-ATOM  21056  N   ALA F 166      15.838 -38.729 -78.303  1.00 59.40           N  
-ATOM  21057  CA  ALA F 166      15.902 -39.615 -77.145  1.00 51.53           C  
-ATOM  21058  C   ALA F 166      14.762 -40.629 -77.174  1.00 54.37           C  
-ATOM  21059  O   ALA F 166      13.592 -40.261 -77.061  1.00 57.88           O  
-ATOM  21060  CB  ALA F 166      15.866 -38.807 -75.857  1.00 53.94           C  
-ATOM  21061  N   SER F 167      15.108 -41.904 -77.324  1.00 47.02           N  
-ATOM  21062  CA  SER F 167      14.107 -42.963 -77.406  1.00 50.53           C  
-ATOM  21063  C   SER F 167      13.745 -43.508 -76.028  1.00 51.26           C  
-ATOM  21064  O   SER F 167      12.591 -43.873 -75.778  1.00 56.56           O  
-ATOM  21065  CB  SER F 167      14.603 -44.100 -78.301  1.00 51.32           C  
-ATOM  21066  OG  SER F 167      15.775 -44.693 -77.771  1.00 57.60           O  
-ATOM  21067  N   HIS F 168      14.736 -43.556 -75.139  1.00 48.28           N  
-ATOM  21068  CA  HIS F 168      14.547 -44.088 -73.792  1.00 41.98           C  
-ATOM  21069  C   HIS F 168      15.031 -43.123 -72.710  1.00 40.02           C  
-ATOM  21070  O   HIS F 168      15.911 -42.296 -72.953  1.00 48.91           O  
-ATOM  21071  CB  HIS F 168      15.273 -45.426 -73.640  1.00 43.15           C  
-ATOM  21072  CG  HIS F 168      14.901 -46.436 -74.679  1.00 48.76           C  
-ATOM  21073  ND1 HIS F 168      13.617 -46.914 -74.826  1.00 55.56           N  
-ATOM  21074  CD2 HIS F 168      15.645 -47.064 -75.620  1.00 59.27           C  
-ATOM  21075  CE1 HIS F 168      13.585 -47.789 -75.815  1.00 59.13           C  
-ATOM  21076  NE2 HIS F 168      14.803 -47.898 -76.313  1.00 70.26           N  
-ATOM  21077  N   LEU F 169      14.456 -43.240 -71.516  1.00 37.54           N  
-ATOM  21078  CA  LEU F 169      14.852 -42.409 -70.378  1.00 38.45           C  
-ATOM  21079  C   LEU F 169      15.190 -43.251 -69.148  1.00 37.02           C  
-ATOM  21080  O   LEU F 169      14.315 -43.900 -68.581  1.00 37.08           O  
-ATOM  21081  CB  LEU F 169      13.742 -41.416 -70.016  1.00 26.69           C  
-ATOM  21082  CG  LEU F 169      13.245 -40.418 -71.061  1.00 27.81           C  
-ATOM  21083  CD1 LEU F 169      12.334 -39.396 -70.409  1.00 27.75           C  
-ATOM  21084  CD2 LEU F 169      14.402 -39.729 -71.744  1.00 39.88           C  
-ATOM  21085  N   TYR F 170      16.453 -43.235 -68.733  1.00 34.09           N  
-ATOM  21086  CA  TYR F 170      16.856 -43.912 -67.502  1.00 33.35           C  
-ATOM  21087  C   TYR F 170      16.803 -42.949 -66.322  1.00 30.17           C  
-ATOM  21088  O   TYR F 170      17.786 -42.282 -66.006  1.00 30.55           O  
-ATOM  21089  CB  TYR F 170      18.259 -44.505 -67.636  1.00 45.05           C  
-ATOM  21090  CG  TYR F 170      18.327 -45.697 -68.561  1.00 49.92           C  
-ATOM  21091  CD1 TYR F 170      18.495 -45.530 -69.929  1.00 62.44           C  
-ATOM  21092  CD2 TYR F 170      18.221 -46.989 -68.067  1.00 44.00           C  
-ATOM  21093  CE1 TYR F 170      18.557 -46.617 -70.781  1.00 60.89           C  
-ATOM  21094  CE2 TYR F 170      18.280 -48.080 -68.912  1.00 58.78           C  
-ATOM  21095  CZ  TYR F 170      18.449 -47.891 -70.265  1.00 60.67           C  
-ATOM  21096  OH  TYR F 170      18.508 -48.982 -71.102  1.00 67.63           O  
-ATOM  21097  N   ILE F 171      15.647 -42.885 -65.672  1.00 33.21           N  
-ATOM  21098  CA  ILE F 171      15.421 -41.926 -64.601  1.00 27.57           C  
-ATOM  21099  C   ILE F 171      15.577 -42.537 -63.212  1.00 33.58           C  
-ATOM  21100  O   ILE F 171      14.930 -43.532 -62.886  1.00 30.97           O  
-ATOM  21101  CB  ILE F 171      14.014 -41.302 -64.699  1.00 21.11           C  
-ATOM  21102  CG1 ILE F 171      13.792 -40.685 -66.080  1.00 26.19           C  
-ATOM  21103  CG2 ILE F 171      13.808 -40.273 -63.599  1.00 25.14           C  
-ATOM  21104  CD1 ILE F 171      12.482 -39.952 -66.211  1.00 26.41           C  
-ATOM  21105  N   THR F 172      16.440 -41.931 -62.399  1.00 36.39           N  
-ATOM  21106  CA  THR F 172      16.522 -42.260 -60.980  1.00 31.19           C  
-ATOM  21107  C   THR F 172      15.593 -41.343 -60.187  1.00 29.22           C  
-ATOM  21108  O   THR F 172      15.883 -40.162 -60.000  1.00 29.46           O  
-ATOM  21109  CB  THR F 172      17.953 -42.127 -60.432  1.00 27.71           C  
-ATOM  21110  OG1 THR F 172      18.850 -42.913 -61.224  1.00 29.90           O  
-ATOM  21111  CG2 THR F 172      18.016 -42.597 -58.985  1.00 23.94           C  
-ATOM  21112  N   ARG F 173      14.471 -41.888 -59.730  1.00 24.42           N  
-ATOM  21113  CA  ARG F 173      13.481 -41.097 -59.010  1.00 24.64           C  
-ATOM  21114  C   ARG F 173      13.876 -40.860 -57.569  1.00 24.98           C  
-ATOM  21115  O   ARG F 173      13.619 -41.694 -56.711  1.00 30.18           O  
-ATOM  21116  CB  ARG F 173      12.117 -41.779 -59.044  1.00 23.53           C  
-ATOM  21117  CG  ARG F 173      11.561 -41.984 -60.424  1.00 23.57           C  
-ATOM  21118  CD  ARG F 173      10.699 -43.215 -60.454  1.00 27.13           C  
-ATOM  21119  NE  ARG F 173       9.281 -42.903 -60.356  1.00 29.53           N  
-ATOM  21120  CZ  ARG F 173       8.362 -43.772 -59.953  1.00 35.77           C  
-ATOM  21121  NH1 ARG F 173       8.723 -44.998 -59.597  1.00 23.27           N  
-ATOM  21122  NH2 ARG F 173       7.086 -43.414 -59.895  1.00 35.52           N  
-ATOM  21123  N   VAL F 174      14.491 -39.716 -57.306  1.00 20.72           N  
-ATOM  21124  CA  VAL F 174      14.761 -39.297 -55.937  1.00 23.53           C  
-ATOM  21125  C   VAL F 174      13.445 -38.904 -55.272  1.00 24.96           C  
-ATOM  21126  O   VAL F 174      12.751 -38.011 -55.751  1.00 23.54           O  
-ATOM  21127  CB  VAL F 174      15.748 -38.118 -55.888  1.00 22.17           C  
-ATOM  21128  CG1 VAL F 174      16.077 -37.755 -54.454  1.00 18.72           C  
-ATOM  21129  CG2 VAL F 174      17.010 -38.468 -56.653  1.00 28.82           C  
-ATOM  21130  N   ALA F 175      13.095 -39.577 -54.181  1.00 20.68           N  
-ATOM  21131  CA  ALA F 175      11.796 -39.358 -53.544  1.00 17.80           C  
-ATOM  21132  C   ALA F 175      11.754 -38.077 -52.712  1.00 23.98           C  
-ATOM  21133  O   ALA F 175      10.695 -37.463 -52.570  1.00 28.18           O  
-ATOM  21134  CB  ALA F 175      11.426 -40.552 -52.682  1.00 17.42           C  
-ATOM  21135  N   ARG F 176      12.898 -37.681 -52.159  1.00 24.55           N  
-ATOM  21136  CA  ARG F 176      12.993 -36.446 -51.384  1.00 21.75           C  
-ATOM  21137  C   ARG F 176      13.146 -35.229 -52.281  1.00 24.27           C  
-ATOM  21138  O   ARG F 176      13.769 -35.301 -53.340  1.00 21.07           O  
-ATOM  21139  CB  ARG F 176      14.176 -36.497 -50.422  1.00 20.98           C  
-ATOM  21140  CG  ARG F 176      14.003 -37.423 -49.243  1.00 25.65           C  
-ATOM  21141  CD  ARG F 176      15.205 -37.317 -48.317  1.00 24.72           C  
-ATOM  21142  NE  ARG F 176      15.438 -35.944 -47.878  1.00 24.07           N  
-ATOM  21143  CZ  ARG F 176      16.424 -35.575 -47.067  1.00 31.03           C  
-ATOM  21144  NH1 ARG F 176      16.562 -34.302 -46.723  1.00 44.58           N  
-ATOM  21145  NH2 ARG F 176      17.273 -36.479 -46.599  1.00 27.53           N  
-ATOM  21146  N   GLU F 177      12.579 -34.107 -51.854  1.00 27.35           N  
-ATOM  21147  CA  GLU F 177      12.825 -32.841 -52.530  1.00 30.38           C  
-ATOM  21148  C   GLU F 177      14.032 -32.153 -51.916  1.00 26.72           C  
-ATOM  21149  O   GLU F 177      14.294 -32.276 -50.720  1.00 28.14           O  
-ATOM  21150  CB  GLU F 177      11.608 -31.920 -52.455  1.00 36.35           C  
-ATOM  21151  CG  GLU F 177      10.811 -31.820 -53.747  1.00 37.58           C  
-ATOM  21152  CD  GLU F 177       9.598 -32.732 -53.757  1.00 61.15           C  
-ATOM  21153  OE1 GLU F 177       9.664 -33.825 -53.153  1.00 65.91           O  
-ATOM  21154  OE2 GLU F 177       8.573 -32.348 -54.361  1.00 67.44           O  
-ATOM  21155  N   PHE F 178      14.767 -31.430 -52.749  1.00 28.07           N  
-ATOM  21156  CA  PHE F 178      15.923 -30.679 -52.294  1.00 23.25           C  
-ATOM  21157  C   PHE F 178      15.945 -29.320 -52.974  1.00 23.44           C  
-ATOM  21158  O   PHE F 178      15.384 -29.161 -54.059  1.00 21.46           O  
-ATOM  21159  CB  PHE F 178      17.219 -31.441 -52.588  1.00 22.40           C  
-ATOM  21160  CG  PHE F 178      17.383 -32.701 -51.787  1.00 23.61           C  
-ATOM  21161  CD1 PHE F 178      17.910 -32.657 -50.507  1.00 33.88           C  
-ATOM  21162  CD2 PHE F 178      17.026 -33.931 -52.319  1.00 24.20           C  
-ATOM  21163  CE1 PHE F 178      18.070 -33.816 -49.766  1.00 39.04           C  
-ATOM  21164  CE2 PHE F 178      17.184 -35.092 -51.584  1.00 24.63           C  
-ATOM  21165  CZ  PHE F 178      17.707 -35.035 -50.307  1.00 34.81           C  
-ATOM  21166  N   PRO F 179      16.571 -28.327 -52.325  1.00 24.15           N  
-ATOM  21167  CA  PRO F 179      16.826 -27.039 -52.973  1.00 26.20           C  
-ATOM  21168  C   PRO F 179      17.560 -27.214 -54.300  1.00 24.17           C  
-ATOM  21169  O   PRO F 179      18.578 -27.906 -54.355  1.00 19.45           O  
-ATOM  21170  CB  PRO F 179      17.694 -26.305 -51.952  1.00 18.01           C  
-ATOM  21171  CG  PRO F 179      17.261 -26.864 -50.645  1.00 16.51           C  
-ATOM  21172  CD  PRO F 179      16.945 -28.310 -50.900  1.00 18.18           C  
-ATOM  21173  N   CYS F 180      17.033 -26.602 -55.356  1.00 24.96           N  
-ATOM  21174  CA  CYS F 180      17.620 -26.717 -56.685  1.00 24.85           C  
-ATOM  21175  C   CYS F 180      17.503 -25.415 -57.466  1.00 30.61           C  
-ATOM  21176  O   CYS F 180      16.597 -24.615 -57.228  1.00 36.10           O  
-ATOM  21177  CB  CYS F 180      16.950 -27.844 -57.473  1.00 24.09           C  
-ATOM  21178  SG  CYS F 180      17.236 -29.498 -56.826  1.00 21.60           S  
-ATOM  21179  N   ASP F 181      18.423 -25.212 -58.403  1.00 30.65           N  
-ATOM  21180  CA  ASP F 181      18.341 -24.082 -59.317  1.00 29.31           C  
-ATOM  21181  C   ASP F 181      18.466 -24.555 -60.764  1.00 23.66           C  
-ATOM  21182  O   ASP F 181      18.545 -23.747 -61.686  1.00 28.98           O  
-ATOM  21183  CB  ASP F 181      19.414 -23.033 -58.990  1.00 37.91           C  
-ATOM  21184  CG  ASP F 181      20.820 -23.618 -58.917  1.00 34.59           C  
-ATOM  21185  OD1 ASP F 181      21.097 -24.623 -59.605  1.00 32.04           O  
-ATOM  21186  OD2 ASP F 181      21.656 -23.061 -58.172  1.00 24.62           O  
-ATOM  21187  N   VAL F 182      18.495 -25.871 -60.951  1.00 20.53           N  
-ATOM  21188  CA  VAL F 182      18.564 -26.465 -62.284  1.00 26.96           C  
-ATOM  21189  C   VAL F 182      17.598 -27.640 -62.383  1.00 25.17           C  
-ATOM  21190  O   VAL F 182      17.659 -28.570 -61.581  1.00 23.51           O  
-ATOM  21191  CB  VAL F 182      19.992 -26.943 -62.631  1.00 27.47           C  
-ATOM  21192  CG1 VAL F 182      19.986 -27.738 -63.923  1.00 33.48           C  
-ATOM  21193  CG2 VAL F 182      20.944 -25.764 -62.739  1.00 26.57           C  
-ATOM  21194  N   PHE F 183      16.711 -27.599 -63.373  1.00 28.50           N  
-ATOM  21195  CA  PHE F 183      15.639 -28.585 -63.471  1.00 26.21           C  
-ATOM  21196  C   PHE F 183      15.600 -29.320 -64.807  1.00 33.34           C  
-ATOM  21197  O   PHE F 183      15.906 -28.750 -65.855  1.00 28.63           O  
-ATOM  21198  CB  PHE F 183      14.286 -27.913 -63.229  1.00 22.62           C  
-ATOM  21199  CG  PHE F 183      14.123 -27.356 -61.845  1.00 20.04           C  
-ATOM  21200  CD1 PHE F 183      14.649 -26.119 -61.514  1.00 19.82           C  
-ATOM  21201  CD2 PHE F 183      13.435 -28.066 -60.878  1.00 24.23           C  
-ATOM  21202  CE1 PHE F 183      14.499 -25.605 -60.241  1.00 23.86           C  
-ATOM  21203  CE2 PHE F 183      13.281 -27.558 -59.602  1.00 26.06           C  
-ATOM  21204  CZ  PHE F 183      13.813 -26.325 -59.284  1.00 27.91           C  
-ATOM  21205  N   PHE F 184      15.213 -30.592 -64.752  1.00 40.39           N  
-ATOM  21206  CA  PHE F 184      14.987 -31.397 -65.948  1.00 31.82           C  
-ATOM  21207  C   PHE F 184      13.694 -30.945 -66.619  1.00 33.99           C  
-ATOM  21208  O   PHE F 184      12.697 -30.699 -65.941  1.00 37.42           O  
-ATOM  21209  CB  PHE F 184      14.921 -32.888 -65.594  1.00 28.37           C  
-ATOM  21210  CG  PHE F 184      14.895 -33.801 -66.791  1.00 35.34           C  
-ATOM  21211  CD1 PHE F 184      16.072 -34.291 -67.332  1.00 31.25           C  
-ATOM  21212  CD2 PHE F 184      13.693 -34.170 -67.375  1.00 32.60           C  
-ATOM  21213  CE1 PHE F 184      16.051 -35.127 -68.433  1.00 23.95           C  
-ATOM  21214  CE2 PHE F 184      13.667 -35.008 -68.474  1.00 24.78           C  
-ATOM  21215  CZ  PHE F 184      14.847 -35.487 -69.003  1.00 24.57           C  
-ATOM  21216  N   PRO F 185      13.711 -30.827 -67.955  1.00 33.40           N  
-ATOM  21217  CA  PRO F 185      12.565 -30.350 -68.738  1.00 32.29           C  
-ATOM  21218  C   PRO F 185      11.281 -31.126 -68.471  1.00 29.18           C  
-ATOM  21219  O   PRO F 185      11.329 -32.324 -68.198  1.00 29.35           O  
-ATOM  21220  CB  PRO F 185      13.022 -30.559 -70.183  1.00 39.59           C  
-ATOM  21221  CG  PRO F 185      14.499 -30.501 -70.116  1.00 41.17           C  
-ATOM  21222  CD  PRO F 185      14.873 -31.122 -68.811  1.00 33.93           C  
-ATOM  21223  N   ALA F 186      10.145 -30.441 -68.541  1.00 34.90           N  
-ATOM  21224  CA  ALA F 186       8.852 -31.104 -68.441  1.00 36.90           C  
-ATOM  21225  C   ALA F 186       8.610 -31.913 -69.709  1.00 42.26           C  
-ATOM  21226  O   ALA F 186       8.983 -31.489 -70.802  1.00 44.88           O  
-ATOM  21227  CB  ALA F 186       7.737 -30.091 -68.225  1.00 30.81           C  
-ATOM  21228  N   PHE F 187       7.994 -33.080 -69.562  1.00 47.89           N  
-ATOM  21229  CA  PHE F 187       7.779 -33.970 -70.696  1.00 47.58           C  
-ATOM  21230  C   PHE F 187       6.535 -34.831 -70.493  1.00 52.82           C  
-ATOM  21231  O   PHE F 187       6.135 -35.083 -69.356  1.00 56.19           O  
-ATOM  21232  CB  PHE F 187       9.008 -34.859 -70.912  1.00 37.74           C  
-ATOM  21233  CG  PHE F 187       9.334 -35.741 -69.739  1.00 36.03           C  
-ATOM  21234  CD1 PHE F 187      10.137 -35.281 -68.709  1.00 33.03           C  
-ATOM  21235  CD2 PHE F 187       8.839 -37.032 -69.669  1.00 38.95           C  
-ATOM  21236  CE1 PHE F 187      10.437 -36.090 -67.631  1.00 31.28           C  
-ATOM  21237  CE2 PHE F 187       9.135 -37.845 -68.591  1.00 33.86           C  
-ATOM  21238  CZ  PHE F 187       9.935 -37.374 -67.573  1.00 28.40           C  
-ATOM  21239  N   PRO F 188       5.913 -35.279 -71.598  1.00 47.13           N  
-ATOM  21240  CA  PRO F 188       4.774 -36.200 -71.507  1.00 47.75           C  
-ATOM  21241  C   PRO F 188       5.168 -37.510 -70.835  1.00 50.02           C  
-ATOM  21242  O   PRO F 188       6.003 -38.248 -71.362  1.00 52.32           O  
-ATOM  21243  CB  PRO F 188       4.391 -36.438 -72.971  1.00 52.48           C  
-ATOM  21244  CG  PRO F 188       4.923 -35.269 -73.697  1.00 59.27           C  
-ATOM  21245  CD  PRO F 188       6.191 -34.897 -72.992  1.00 53.26           C  
-ATOM  21246  N   GLY F 189       4.569 -37.789 -69.683  1.00 47.70           N  
-ATOM  21247  CA  GLY F 189       4.941 -38.941 -68.886  1.00 48.13           C  
-ATOM  21248  C   GLY F 189       5.349 -38.463 -67.510  1.00 51.24           C  
-ATOM  21249  O   GLY F 189       5.585 -39.259 -66.598  1.00 57.57           O  
-ATOM  21250  N   ASP F 190       5.407 -37.141 -67.367  1.00 48.23           N  
-ATOM  21251  CA  ASP F 190       5.775 -36.479 -66.118  1.00 35.14           C  
-ATOM  21252  C   ASP F 190       5.058 -37.060 -64.903  1.00 38.64           C  
-ATOM  21253  O   ASP F 190       5.545 -36.957 -63.777  1.00 42.74           O  
-ATOM  21254  CB  ASP F 190       5.486 -34.981 -66.224  1.00 41.47           C  
-ATOM  21255  CG  ASP F 190       6.738 -34.140 -66.104  1.00 57.98           C  
-ATOM  21256  OD1 ASP F 190       7.840 -34.725 -66.059  1.00 64.97           O  
-ATOM  21257  OD2 ASP F 190       6.621 -32.896 -66.060  1.00 68.80           O  
-ATOM  21258  N   ASP F 191       3.906 -37.678 -65.151  1.00 41.84           N  
-ATOM  21259  CA  ASP F 191       3.121 -38.353 -64.127  1.00 41.44           C  
-ATOM  21260  C   ASP F 191       3.931 -39.309 -63.255  1.00 41.98           C  
-ATOM  21261  O   ASP F 191       3.551 -39.580 -62.118  1.00 47.99           O  
-ATOM  21262  CB  ASP F 191       1.974 -39.123 -64.780  1.00 47.84           C  
-ATOM  21263  CG  ASP F 191       0.633 -38.458 -64.566  1.00 72.61           C  
-ATOM  21264  OD1 ASP F 191       0.606 -37.247 -64.253  1.00 76.49           O  
-ATOM  21265  OD2 ASP F 191      -0.396 -39.151 -64.714  1.00 75.93           O  
-ATOM  21266  N   ILE F 192       5.040 -39.821 -63.781  1.00 41.72           N  
-ATOM  21267  CA  ILE F 192       5.839 -40.801 -63.045  1.00 40.36           C  
-ATOM  21268  C   ILE F 192       6.616 -40.161 -61.885  1.00 35.51           C  
-ATOM  21269  O   ILE F 192       7.068 -40.853 -60.971  1.00 35.12           O  
-ATOM  21270  CB  ILE F 192       6.807 -41.538 -63.996  1.00 33.91           C  
-ATOM  21271  CG1 ILE F 192       6.038 -42.029 -65.221  1.00 60.59           C  
-ATOM  21272  CG2 ILE F 192       7.470 -42.721 -63.307  1.00 33.01           C  
-ATOM  21273  CD1 ILE F 192       6.906 -42.660 -66.261  1.00 70.37           C  
-ATOM  21274  N   LEU F 193       6.745 -38.838 -61.904  1.00 30.30           N  
-ATOM  21275  CA  LEU F 193       7.473 -38.142 -60.845  1.00 25.91           C  
-ATOM  21276  C   LEU F 193       6.558 -37.693 -59.708  1.00 29.01           C  
-ATOM  21277  O   LEU F 193       6.842 -37.942 -58.536  1.00 29.02           O  
-ATOM  21278  CB  LEU F 193       8.217 -36.943 -61.422  1.00 21.92           C  
-ATOM  21279  CG  LEU F 193       9.156 -37.319 -62.567  1.00 20.30           C  
-ATOM  21280  CD1 LEU F 193       9.574 -36.079 -63.314  1.00 23.89           C  
-ATOM  21281  CD2 LEU F 193      10.371 -38.079 -62.057  1.00 13.23           C  
-ATOM  21282  N   SER F 194       5.465 -37.024 -60.058  1.00 29.13           N  
-ATOM  21283  CA  SER F 194       4.458 -36.634 -59.078  1.00 29.05           C  
-ATOM  21284  C   SER F 194       3.120 -36.386 -59.768  1.00 40.61           C  
-ATOM  21285  O   SER F 194       2.951 -36.722 -60.940  1.00 47.31           O  
-ATOM  21286  CB  SER F 194       4.906 -35.398 -58.297  1.00 29.14           C  
-ATOM  21287  OG  SER F 194       5.618 -34.499 -59.127  1.00 42.22           O  
-ATOM  21288  N   ASN F 195       2.174 -35.799 -59.040  1.00 40.97           N  
-ATOM  21289  CA  ASN F 195       0.791 -35.707 -59.508  1.00 39.91           C  
-ATOM  21290  C   ASN F 195       0.497 -34.517 -60.421  1.00 49.61           C  
-ATOM  21291  O   ASN F 195      -0.671 -34.169 -60.615  1.00 48.32           O  
-ATOM  21292  CB  ASN F 195      -0.157 -35.663 -58.307  1.00 33.47           C  
-ATOM  21293  CG  ASN F 195      -0.101 -36.928 -57.476  1.00 27.12           C  
-ATOM  21294  OD1 ASN F 195       0.433 -37.945 -57.915  1.00 32.50           O  
-ATOM  21295  ND2 ASN F 195      -0.661 -36.877 -56.274  1.00 22.92           N  
-ATOM  21296  N   LYS F 196       1.553 -33.920 -60.979  1.00 55.13           N  
-ATOM  21297  CA  LYS F 196       1.456 -32.728 -61.834  1.00 54.37           C  
-ATOM  21298  C   LYS F 196       0.278 -32.775 -62.803  1.00 47.31           C  
-ATOM  21299  O   LYS F 196      -0.792 -32.235 -62.515  1.00 33.12           O  
-ATOM  21300  CB  LYS F 196       2.755 -32.529 -62.632  1.00 57.14           C  
-ATOM  21301  CG  LYS F 196       3.775 -31.609 -61.976  1.00 77.10           C  
-ATOM  21302  CD  LYS F 196       4.189 -32.138 -60.619  1.00 74.33           C  
-ATOM  21303  CE  LYS F 196       5.193 -31.226 -59.941  1.00 79.58           C  
-ATOM  21304  NZ  LYS F 196       5.522 -31.714 -58.574  1.00 68.06           N  
-ATOM  21305  N   GLU F 224       0.393 -37.428 -80.518  1.00 82.35           N  
-ATOM  21306  CA  GLU F 224       1.226 -36.828 -79.483  1.00 88.05           C  
-ATOM  21307  C   GLU F 224       2.217 -37.847 -78.928  1.00 94.32           C  
-ATOM  21308  O   GLU F 224       1.827 -38.934 -78.498  1.00 82.02           O  
-ATOM  21309  CB  GLU F 224       0.356 -36.265 -78.356  1.00 77.39           C  
-ATOM  21310  CG  GLU F 224       1.025 -35.168 -77.546  1.00 79.01           C  
-ATOM  21311  CD  GLU F 224       1.254 -33.907 -78.358  1.00 91.02           C  
-ATOM  21312  OE1 GLU F 224       2.374 -33.730 -78.883  1.00 83.80           O  
-ATOM  21313  OE2 GLU F 224       0.310 -33.095 -78.473  1.00 73.30           O  
-ATOM  21314  N   ALA F 225       3.499 -37.495 -78.942  1.00 82.77           N  
-ATOM  21315  CA  ALA F 225       4.543 -38.398 -78.469  1.00 63.38           C  
-ATOM  21316  C   ALA F 225       4.646 -38.368 -76.950  1.00 69.51           C  
-ATOM  21317  O   ALA F 225       4.781 -37.302 -76.349  1.00 74.35           O  
-ATOM  21318  CB  ALA F 225       5.879 -38.042 -79.099  1.00 50.55           C  
-ATOM  21319  N   THR F 226       4.581 -39.543 -76.333  1.00 63.76           N  
-ATOM  21320  CA  THR F 226       4.641 -39.642 -74.881  1.00 56.80           C  
-ATOM  21321  C   THR F 226       5.597 -40.737 -74.416  1.00 54.78           C  
-ATOM  21322  O   THR F 226       5.846 -41.714 -75.128  1.00 51.38           O  
-ATOM  21323  CB  THR F 226       3.248 -39.910 -74.279  1.00 53.12           C  
-ATOM  21324  OG1 THR F 226       3.355 -40.026 -72.854  1.00 56.27           O  
-ATOM  21325  CG2 THR F 226       2.660 -41.192 -74.845  1.00 64.39           C  
-ATOM  21326  N   TYR F 227       6.126 -40.559 -73.210  1.00 50.94           N  
-ATOM  21327  CA  TYR F 227       7.070 -41.501 -72.621  1.00 39.11           C  
-ATOM  21328  C   TYR F 227       6.395 -42.423 -71.614  1.00 44.74           C  
-ATOM  21329  O   TYR F 227       6.037 -42.000 -70.513  1.00 46.22           O  
-ATOM  21330  CB  TYR F 227       8.214 -40.750 -71.941  1.00 31.00           C  
-ATOM  21331  CG  TYR F 227       9.158 -40.061 -72.894  1.00 36.58           C  
-ATOM  21332  CD1 TYR F 227      10.280 -40.717 -73.381  1.00 39.24           C  
-ATOM  21333  CD2 TYR F 227       8.935 -38.753 -73.303  1.00 44.32           C  
-ATOM  21334  CE1 TYR F 227      11.152 -40.094 -74.249  1.00 41.00           C  
-ATOM  21335  CE2 TYR F 227       9.803 -38.120 -74.174  1.00 45.92           C  
-ATOM  21336  CZ  TYR F 227      10.910 -38.797 -74.645  1.00 42.97           C  
-ATOM  21337  OH  TYR F 227      11.785 -38.184 -75.512  1.00 47.57           O  
-ATOM  21338  N   ARG F 228       6.230 -43.686 -71.988  1.00 42.97           N  
-ATOM  21339  CA  ARG F 228       5.606 -44.657 -71.100  1.00 42.61           C  
-ATOM  21340  C   ARG F 228       6.677 -45.452 -70.359  1.00 42.80           C  
-ATOM  21341  O   ARG F 228       7.690 -45.830 -70.948  1.00 47.30           O  
-ATOM  21342  CB  ARG F 228       4.685 -45.592 -71.890  1.00 45.94           C  
-ATOM  21343  CG  ARG F 228       3.331 -45.855 -71.238  1.00 48.11           C  
-ATOM  21344  CD  ARG F 228       2.209 -45.808 -72.272  1.00 61.03           C  
-ATOM  21345  NE  ARG F 228       2.517 -46.614 -73.452  1.00 76.69           N  
-ATOM  21346  CZ  ARG F 228       1.908 -47.755 -73.766  1.00 69.02           C  
-ATOM  21347  NH1 ARG F 228       0.941 -48.231 -72.992  1.00 59.34           N  
-ATOM  21348  NH2 ARG F 228       2.262 -48.416 -74.861  1.00 53.62           N  
-ATOM  21349  N   PRO F 229       6.465 -45.692 -69.055  1.00 42.75           N  
-ATOM  21350  CA  PRO F 229       7.406 -46.502 -68.278  1.00 32.46           C  
-ATOM  21351  C   PRO F 229       7.320 -47.978 -68.653  1.00 40.03           C  
-ATOM  21352  O   PRO F 229       6.273 -48.443 -69.106  1.00 41.80           O  
-ATOM  21353  CB  PRO F 229       6.958 -46.271 -66.834  1.00 33.25           C  
-ATOM  21354  CG  PRO F 229       5.512 -45.963 -66.939  1.00 44.22           C  
-ATOM  21355  CD  PRO F 229       5.335 -45.218 -68.237  1.00 48.90           C  
-ATOM  21356  N   ILE F 230       8.415 -48.705 -68.456  1.00 34.81           N  
-ATOM  21357  CA  ILE F 230       8.505 -50.090 -68.896  1.00 31.50           C  
-ATOM  21358  C   ILE F 230       9.247 -50.915 -67.840  1.00 33.53           C  
-ATOM  21359  O   ILE F 230       9.145 -52.149 -67.779  1.00 38.44           O  
-ATOM  21360  CB  ILE F 230       9.218 -50.169 -70.270  1.00 27.55           C  
-ATOM  21361  CG1 ILE F 230       8.502 -51.135 -71.211  1.00 50.25           C  
-ATOM  21362  CG2 ILE F 230      10.695 -50.500 -70.113  1.00 27.35           C  
-ATOM  21363  CD1 ILE F 230       7.468 -50.467 -72.103  1.00 50.27           C  
-ATOM  21364  N   PHE F 231       9.972 -50.193 -66.993  1.00 28.55           N  
-ATOM  21365  CA  PHE F 231      10.806 -50.760 -65.949  1.00 27.42           C  
-ATOM  21366  C   PHE F 231      10.601 -49.937 -64.690  1.00 30.18           C  
-ATOM  21367  O   PHE F 231      10.774 -48.725 -64.717  1.00 37.46           O  
-ATOM  21368  CB  PHE F 231      12.278 -50.749 -66.379  1.00 28.10           C  
-ATOM  21369  CG  PHE F 231      13.236 -51.204 -65.312  1.00 31.69           C  
-ATOM  21370  CD1 PHE F 231      13.712 -50.325 -64.353  1.00 35.18           C  
-ATOM  21371  CD2 PHE F 231      13.684 -52.507 -65.290  1.00 48.80           C  
-ATOM  21372  CE1 PHE F 231      14.596 -50.754 -63.380  1.00 41.37           C  
-ATOM  21373  CE2 PHE F 231      14.565 -52.942 -64.325  1.00 50.95           C  
-ATOM  21374  CZ  PHE F 231      15.023 -52.065 -63.368  1.00 39.91           C  
-ATOM  21375  N   ILE F 232      10.213 -50.578 -63.594  1.00 30.88           N  
-ATOM  21376  CA  ILE F 232      10.137 -49.885 -62.310  1.00 26.62           C  
-ATOM  21377  C   ILE F 232      10.745 -50.766 -61.232  1.00 26.46           C  
-ATOM  21378  O   ILE F 232      10.276 -51.880 -60.997  1.00 28.30           O  
-ATOM  21379  CB  ILE F 232       8.693 -49.515 -61.920  1.00 29.90           C  
-ATOM  21380  CG1 ILE F 232       8.110 -48.502 -62.906  1.00 21.20           C  
-ATOM  21381  CG2 ILE F 232       8.655 -48.940 -60.510  1.00 24.54           C  
-ATOM  21382  CD1 ILE F 232       6.719 -48.051 -62.556  1.00 22.05           C  
-ATOM  21383  N   SER F 233      11.781 -50.257 -60.573  1.00 26.91           N  
-ATOM  21384  CA  SER F 233      12.594 -51.068 -59.672  1.00 24.87           C  
-ATOM  21385  C   SER F 233      12.145 -51.022 -58.218  1.00 23.32           C  
-ATOM  21386  O   SER F 233      11.230 -50.287 -57.849  1.00 24.92           O  
-ATOM  21387  CB  SER F 233      14.058 -50.628 -59.750  1.00 34.58           C  
-ATOM  21388  OG  SER F 233      14.267 -49.419 -59.037  1.00 25.89           O  
-ATOM  21389  N   LYS F 234      12.814 -51.828 -57.401  1.00 25.58           N  
-ATOM  21390  CA  LYS F 234      12.643 -51.807 -55.956  1.00 28.22           C  
-ATOM  21391  C   LYS F 234      13.113 -50.456 -55.426  1.00 34.73           C  
-ATOM  21392  O   LYS F 234      13.920 -49.786 -56.069  1.00 41.48           O  
-ATOM  21393  CB  LYS F 234      13.430 -52.957 -55.319  1.00 26.14           C  
-ATOM  21394  CG  LYS F 234      13.371 -53.040 -53.805  1.00 37.49           C  
-ATOM  21395  CD  LYS F 234      14.735 -53.414 -53.245  1.00 53.21           C  
-ATOM  21396  CE  LYS F 234      15.335 -54.600 -53.991  1.00 55.75           C  
-ATOM  21397  NZ  LYS F 234      16.769 -54.810 -53.649  1.00 48.78           N  
-ATOM  21398  N   THR F 235      12.602 -50.043 -54.271  1.00 31.00           N  
-ATOM  21399  CA  THR F 235      13.035 -48.786 -53.673  1.00 22.12           C  
-ATOM  21400  C   THR F 235      14.348 -48.962 -52.911  1.00 24.36           C  
-ATOM  21401  O   THR F 235      14.443 -49.784 -51.998  1.00 24.07           O  
-ATOM  21402  CB  THR F 235      11.968 -48.216 -52.724  1.00 18.32           C  
-ATOM  21403  OG1 THR F 235      10.729 -48.069 -53.427  1.00 19.19           O  
-ATOM  21404  CG2 THR F 235      12.404 -46.864 -52.195  1.00 26.18           C  
-ATOM  21405  N   PHE F 236      15.362 -48.192 -53.299  1.00 22.19           N  
-ATOM  21406  CA  PHE F 236      16.648 -48.219 -52.607  1.00 24.36           C  
-ATOM  21407  C   PHE F 236      16.782 -46.971 -51.746  1.00 26.27           C  
-ATOM  21408  O   PHE F 236      15.946 -46.078 -51.825  1.00 25.05           O  
-ATOM  21409  CB  PHE F 236      17.805 -48.312 -53.603  1.00 24.18           C  
-ATOM  21410  CG  PHE F 236      17.796 -49.568 -54.421  1.00 25.55           C  
-ATOM  21411  CD1 PHE F 236      17.070 -49.641 -55.597  1.00 24.91           C  
-ATOM  21412  CD2 PHE F 236      18.511 -50.680 -54.011  1.00 34.73           C  
-ATOM  21413  CE1 PHE F 236      17.058 -50.799 -56.349  1.00 33.77           C  
-ATOM  21414  CE2 PHE F 236      18.502 -51.840 -54.757  1.00 39.11           C  
-ATOM  21415  CZ  PHE F 236      17.775 -51.900 -55.927  1.00 41.50           C  
-ATOM  21416  N   SER F 237      17.821 -46.905 -50.921  1.00 29.43           N  
-ATOM  21417  CA  SER F 237      18.024 -45.727 -50.081  1.00 24.16           C  
-ATOM  21418  C   SER F 237      19.462 -45.571 -49.610  1.00 30.91           C  
-ATOM  21419  O   SER F 237      20.086 -46.534 -49.159  1.00 32.70           O  
-ATOM  21420  CB  SER F 237      17.108 -45.773 -48.860  1.00 20.77           C  
-ATOM  21421  OG  SER F 237      17.613 -46.674 -47.891  1.00 35.54           O  
-ATOM  21422  N   ASP F 238      19.979 -44.349 -49.706  1.00 31.54           N  
-ATOM  21423  CA  ASP F 238      21.303 -44.038 -49.179  1.00 27.88           C  
-ATOM  21424  C   ASP F 238      21.328 -42.672 -48.502  1.00 21.63           C  
-ATOM  21425  O   ASP F 238      20.765 -41.702 -49.014  1.00 25.89           O  
-ATOM  21426  CB  ASP F 238      22.353 -44.096 -50.286  1.00 26.54           C  
-ATOM  21427  CG  ASP F 238      22.640 -45.512 -50.736  1.00 32.32           C  
-ATOM  21428  OD1 ASP F 238      23.329 -46.246 -49.995  1.00 28.15           O  
-ATOM  21429  OD2 ASP F 238      22.178 -45.893 -51.832  1.00 34.05           O  
-ATOM  21430  N   ASN F 239      21.990 -42.616 -47.349  1.00 19.32           N  
-ATOM  21431  CA  ASN F 239      22.094 -41.402 -46.545  1.00 23.03           C  
-ATOM  21432  C   ASN F 239      20.744 -40.754 -46.257  1.00 19.98           C  
-ATOM  21433  O   ASN F 239      20.633 -39.528 -46.204  1.00 18.87           O  
-ATOM  21434  CB  ASN F 239      23.018 -40.389 -47.224  1.00 23.15           C  
-ATOM  21435  CG  ASN F 239      24.460 -40.854 -47.269  1.00 24.15           C  
-ATOM  21436  OD1 ASN F 239      25.127 -40.948 -46.238  1.00 21.22           O  
-ATOM  21437  ND2 ASN F 239      24.951 -41.141 -48.469  1.00 29.30           N  
-ATOM  21438  N   GLY F 240      19.723 -41.583 -46.067  1.00 17.13           N  
-ATOM  21439  CA  GLY F 240      18.400 -41.091 -45.729  1.00 33.35           C  
-ATOM  21440  C   GLY F 240      17.632 -40.585 -46.935  1.00 26.99           C  
-ATOM  21441  O   GLY F 240      16.634 -39.873 -46.797  1.00 20.70           O  
-ATOM  21442  N   VAL F 241      18.107 -40.951 -48.121  1.00 28.26           N  
-ATOM  21443  CA  VAL F 241      17.446 -40.583 -49.366  1.00 20.37           C  
-ATOM  21444  C   VAL F 241      16.954 -41.826 -50.088  1.00 20.99           C  
-ATOM  21445  O   VAL F 241      17.759 -42.644 -50.534  1.00 24.23           O  
-ATOM  21446  CB  VAL F 241      18.380 -39.801 -50.307  1.00 22.08           C  
-ATOM  21447  CG1 VAL F 241      17.575 -39.141 -51.419  1.00 19.77           C  
-ATOM  21448  CG2 VAL F 241      19.180 -38.772 -49.528  1.00 27.46           C  
-ATOM  21449  N   PRO F 242      15.627 -41.979 -50.189  1.00 17.94           N  
-ATOM  21450  CA  PRO F 242      15.002 -43.069 -50.942  1.00 19.94           C  
-ATOM  21451  C   PRO F 242      14.912 -42.757 -52.431  1.00 20.27           C  
-ATOM  21452  O   PRO F 242      14.634 -41.614 -52.789  1.00 22.50           O  
-ATOM  21453  CB  PRO F 242      13.608 -43.159 -50.323  1.00 14.45           C  
-ATOM  21454  CG  PRO F 242      13.317 -41.760 -49.903  1.00 13.50           C  
-ATOM  21455  CD  PRO F 242      14.630 -41.174 -49.461  1.00 16.86           C  
-ATOM  21456  N   TYR F 243      15.143 -43.747 -53.287  1.00 18.57           N  
-ATOM  21457  CA  TYR F 243      14.991 -43.527 -54.720  1.00 26.28           C  
-ATOM  21458  C   TYR F 243      14.636 -44.781 -55.521  1.00 29.25           C  
-ATOM  21459  O   TYR F 243      14.744 -45.910 -55.033  1.00 28.30           O  
-ATOM  21460  CB  TYR F 243      16.257 -42.883 -55.301  1.00 22.25           C  
-ATOM  21461  CG  TYR F 243      17.569 -43.532 -54.924  1.00 21.59           C  
-ATOM  21462  CD1 TYR F 243      18.177 -43.253 -53.707  1.00 20.82           C  
-ATOM  21463  CD2 TYR F 243      18.226 -44.387 -55.803  1.00 28.00           C  
-ATOM  21464  CE1 TYR F 243      19.386 -43.827 -53.364  1.00 25.56           C  
-ATOM  21465  CE2 TYR F 243      19.439 -44.965 -55.466  1.00 24.36           C  
-ATOM  21466  CZ  TYR F 243      20.012 -44.679 -54.246  1.00 23.01           C  
-ATOM  21467  OH  TYR F 243      21.215 -45.244 -53.901  1.00 26.02           O  
-ATOM  21468  N   ASP F 244      14.194 -44.550 -56.755  1.00 29.08           N  
-ATOM  21469  CA  ASP F 244      13.782 -45.615 -57.663  1.00 25.58           C  
-ATOM  21470  C   ASP F 244      14.587 -45.586 -58.948  1.00 32.43           C  
-ATOM  21471  O   ASP F 244      15.299 -44.624 -59.225  1.00 33.86           O  
-ATOM  21472  CB  ASP F 244      12.294 -45.492 -58.002  1.00 25.00           C  
-ATOM  21473  CG  ASP F 244      11.452 -46.556 -57.335  1.00 31.67           C  
-ATOM  21474  OD1 ASP F 244      11.975 -47.255 -56.443  1.00 36.79           O  
-ATOM  21475  OD2 ASP F 244      10.264 -46.687 -57.698  1.00 33.73           O  
-ATOM  21476  N   PHE F 245      14.458 -46.647 -59.735  1.00 35.43           N  
-ATOM  21477  CA  PHE F 245      15.009 -46.676 -61.082  1.00 27.57           C  
-ATOM  21478  C   PHE F 245      13.912 -47.025 -62.070  1.00 26.23           C  
-ATOM  21479  O   PHE F 245      13.313 -48.096 -61.986  1.00 25.28           O  
-ATOM  21480  CB  PHE F 245      16.156 -47.681 -61.193  1.00 22.45           C  
-ATOM  21481  CG  PHE F 245      17.312 -47.381 -60.293  1.00 32.49           C  
-ATOM  21482  CD1 PHE F 245      18.114 -46.278 -60.521  1.00 30.00           C  
-ATOM  21483  CD2 PHE F 245      17.607 -48.210 -59.226  1.00 41.20           C  
-ATOM  21484  CE1 PHE F 245      19.185 -46.002 -59.693  1.00 36.74           C  
-ATOM  21485  CE2 PHE F 245      18.676 -47.943 -58.395  1.00 40.16           C  
-ATOM  21486  CZ  PHE F 245      19.467 -46.836 -58.628  1.00 33.58           C  
-ATOM  21487  N   VAL F 246      13.644 -46.120 -63.004  1.00 25.05           N  
-ATOM  21488  CA  VAL F 246      12.659 -46.394 -64.040  1.00 30.44           C  
-ATOM  21489  C   VAL F 246      13.237 -46.179 -65.427  1.00 27.34           C  
-ATOM  21490  O   VAL F 246      14.110 -45.337 -65.624  1.00 28.50           O  
-ATOM  21491  CB  VAL F 246      11.397 -45.525 -63.887  1.00 20.81           C  
-ATOM  21492  CG1 VAL F 246      10.618 -45.944 -62.651  1.00 27.31           C  
-ATOM  21493  CG2 VAL F 246      11.760 -44.052 -63.838  1.00 21.21           C  
-ATOM  21494  N   VAL F 247      12.752 -46.962 -66.383  1.00 26.14           N  
-ATOM  21495  CA  VAL F 247      13.136 -46.799 -67.775  1.00 27.16           C  
-ATOM  21496  C   VAL F 247      11.894 -46.495 -68.605  1.00 32.31           C  
-ATOM  21497  O   VAL F 247      10.930 -47.262 -68.610  1.00 31.14           O  
-ATOM  21498  CB  VAL F 247      13.848 -48.050 -68.324  1.00 28.26           C  
-ATOM  21499  CG1 VAL F 247      14.415 -47.772 -69.708  1.00 33.48           C  
-ATOM  21500  CG2 VAL F 247      14.951 -48.488 -67.378  1.00 27.80           C  
-ATOM  21501  N   LEU F 248      11.920 -45.360 -69.292  1.00 25.34           N  
-ATOM  21502  CA  LEU F 248      10.800 -44.925 -70.111  1.00 27.16           C  
-ATOM  21503  C   LEU F 248      11.141 -45.103 -71.580  1.00 37.71           C  
-ATOM  21504  O   LEU F 248      12.314 -45.149 -71.941  1.00 39.56           O  
-ATOM  21505  CB  LEU F 248      10.457 -43.461 -69.831  1.00 30.48           C  
-ATOM  21506  CG  LEU F 248       9.610 -43.087 -68.615  1.00 26.58           C  
-ATOM  21507  CD1 LEU F 248      10.261 -43.526 -67.315  1.00 31.33           C  
-ATOM  21508  CD2 LEU F 248       9.378 -41.587 -68.607  1.00 28.93           C  
-ATOM  21509  N   GLU F 249      10.119 -45.206 -72.424  1.00 40.37           N  
-ATOM  21510  CA  GLU F 249      10.337 -45.244 -73.866  1.00 38.39           C  
-ATOM  21511  C   GLU F 249       9.300 -44.393 -74.588  1.00 42.23           C  
-ATOM  21512  O   GLU F 249       8.190 -44.199 -74.087  1.00 51.61           O  
-ATOM  21513  CB  GLU F 249      10.299 -46.682 -74.390  1.00 37.69           C  
-ATOM  21514  CG  GLU F 249       8.916 -47.320 -74.397  1.00 48.61           C  
-ATOM  21515  CD  GLU F 249       8.909 -48.668 -75.095  1.00 65.84           C  
-ATOM  21516  OE1 GLU F 249       9.989 -49.102 -75.553  1.00 60.45           O  
-ATOM  21517  OE2 GLU F 249       7.828 -49.291 -75.189  1.00 64.63           O  
-ATOM  21518  N   LYS F 250       9.668 -43.874 -75.756  1.00 36.16           N  
-ATOM  21519  CA  LYS F 250       8.718 -43.132 -76.581  1.00 39.96           C  
-ATOM  21520  C   LYS F 250       7.677 -44.059 -77.200  1.00 51.86           C  
-ATOM  21521  O   LYS F 250       7.987 -45.185 -77.594  1.00 59.52           O  
-ATOM  21522  CB  LYS F 250       9.437 -42.359 -77.687  1.00 44.33           C  
-ATOM  21523  CG  LYS F 250       9.883 -40.969 -77.278  1.00 51.24           C  
-ATOM  21524  CD  LYS F 250      10.206 -40.104 -78.487  1.00 50.37           C  
-ATOM  21525  CE  LYS F 250      11.338 -40.693 -79.313  1.00 59.03           C  
-ATOM  21526  NZ  LYS F 250      11.736 -39.785 -80.425  1.00 49.37           N  
-ATOM  21527  N   ARG F 251       6.440 -43.580 -77.283  1.00 48.68           N  
-ATOM  21528  CA  ARG F 251       5.373 -44.333 -77.932  1.00 61.59           C  
-ATOM  21529  C   ARG F 251       4.393 -43.412 -78.653  1.00 62.33           C  
-ATOM  21530  O   ARG F 251       3.933 -42.415 -78.100  1.00 59.97           O  
-ATOM  21531  CB  ARG F 251       4.629 -45.200 -76.915  1.00 61.51           C  
-ATOM  21532  CG  ARG F 251       5.132 -46.635 -76.840  1.00 58.96           C  
-ATOM  21533  CD  ARG F 251       4.991 -47.341 -78.187  1.00 80.19           C  
-ATOM  21534  NE  ARG F 251       3.621 -47.278 -78.692  1.00 92.42           N  
-ATOM  21535  CZ  ARG F 251       3.266 -46.737 -79.856  1.00 87.64           C  
-ATOM  21536  NH1 ARG F 251       1.989 -46.730 -80.216  1.00 77.40           N  
-ATOM  21537  NH2 ARG F 251       4.179 -46.208 -80.662  1.00 68.81           N  
-ATOM  21538  N   SER F 285      14.364 -80.725 -78.139  1.00 61.61           N  
-ATOM  21539  CA  SER F 285      14.116 -82.160 -78.242  1.00 69.58           C  
-ATOM  21540  C   SER F 285      13.171 -82.636 -77.145  1.00 56.89           C  
-ATOM  21541  O   SER F 285      12.128 -83.226 -77.427  1.00 52.19           O  
-ATOM  21542  CB  SER F 285      15.430 -82.945 -78.172  1.00 78.04           C  
-ATOM  21543  OG  SER F 285      16.270 -82.657 -79.278  1.00 77.68           O  
-ATOM  21544  N   SER F 286      13.546 -82.381 -75.895  1.00 57.96           N  
-ATOM  21545  CA  SER F 286      12.735 -82.786 -74.752  1.00 56.12           C  
-ATOM  21546  C   SER F 286      11.537 -81.858 -74.565  1.00 55.04           C  
-ATOM  21547  O   SER F 286      10.466 -82.293 -74.140  1.00 53.36           O  
-ATOM  21548  CB  SER F 286      13.581 -82.815 -73.481  1.00 39.55           C  
-ATOM  21549  OG  SER F 286      14.039 -81.519 -73.160  1.00 55.65           O  
-ATOM  21550  N   ALA F 287      11.722 -80.579 -74.878  1.00 56.45           N  
-ATOM  21551  CA  ALA F 287      10.632 -79.613 -74.798  1.00 46.53           C  
-ATOM  21552  C   ALA F 287       9.543 -79.970 -75.804  1.00 48.77           C  
-ATOM  21553  O   ALA F 287       8.353 -79.764 -75.556  1.00 38.99           O  
-ATOM  21554  CB  ALA F 287      11.149 -78.201 -75.042  1.00 33.71           C  
-ATOM  21555  N   ALA F 288       9.966 -80.515 -76.939  1.00 51.45           N  
-ATOM  21556  CA  ALA F 288       9.042 -80.935 -77.982  1.00 49.94           C  
-ATOM  21557  C   ALA F 288       8.250 -82.152 -77.525  1.00 50.44           C  
-ATOM  21558  O   ALA F 288       7.060 -82.267 -77.807  1.00 50.38           O  
-ATOM  21559  CB  ALA F 288       9.789 -81.237 -79.267  1.00 54.91           C  
-ATOM  21560  N   ALA F 289       8.917 -83.058 -76.817  1.00 45.63           N  
-ATOM  21561  CA  ALA F 289       8.259 -84.245 -76.283  1.00 40.19           C  
-ATOM  21562  C   ALA F 289       7.295 -83.881 -75.163  1.00 36.92           C  
-ATOM  21563  O   ALA F 289       6.280 -84.546 -74.963  1.00 42.10           O  
-ATOM  21564  CB  ALA F 289       9.291 -85.245 -75.785  1.00 34.23           C  
-ATOM  21565  N   ILE F 290       7.621 -82.821 -74.433  1.00 42.33           N  
-ATOM  21566  CA  ILE F 290       6.813 -82.396 -73.295  1.00 40.95           C  
-ATOM  21567  C   ILE F 290       5.582 -81.620 -73.762  1.00 37.28           C  
-ATOM  21568  O   ILE F 290       4.495 -81.750 -73.194  1.00 30.38           O  
-ATOM  21569  CB  ILE F 290       7.656 -81.537 -72.313  1.00 48.03           C  
-ATOM  21570  CG1 ILE F 290       8.694 -82.414 -71.608  1.00 44.88           C  
-ATOM  21571  CG2 ILE F 290       6.781 -80.840 -71.289  1.00 37.79           C  
-ATOM  21572  CD1 ILE F 290       9.605 -81.650 -70.663  1.00 51.51           C  
-ATOM  21573  N   ALA F 291       5.769 -80.845 -74.825  1.00 44.45           N  
-ATOM  21574  CA  ALA F 291       4.767 -79.911 -75.342  1.00 51.35           C  
-ATOM  21575  C   ALA F 291       3.333 -80.453 -75.478  1.00 50.08           C  
-ATOM  21576  O   ALA F 291       2.400 -79.829 -74.968  1.00 44.90           O  
-ATOM  21577  CB  ALA F 291       5.239 -79.361 -76.691  1.00 50.55           C  
-ATOM  21578  N   PRO F 292       3.143 -81.607 -76.154  1.00 44.81           N  
-ATOM  21579  CA  PRO F 292       1.753 -82.011 -76.400  1.00 37.86           C  
-ATOM  21580  C   PRO F 292       0.994 -82.417 -75.139  1.00 37.92           C  
-ATOM  21581  O   PRO F 292      -0.227 -82.563 -75.196  1.00 44.48           O  
-ATOM  21582  CB  PRO F 292       1.901 -83.208 -77.341  1.00 35.99           C  
-ATOM  21583  CG  PRO F 292       3.223 -83.775 -77.007  1.00 34.60           C  
-ATOM  21584  CD  PRO F 292       4.094 -82.592 -76.703  1.00 41.86           C  
-ATOM  21585  N   VAL F 293       1.699 -82.597 -74.026  1.00 36.78           N  
-ATOM  21586  CA  VAL F 293       1.052 -82.949 -72.769  1.00 35.71           C  
-ATOM  21587  C   VAL F 293       0.636 -81.680 -72.033  1.00 40.69           C  
-ATOM  21588  O   VAL F 293      -0.502 -81.557 -71.564  1.00 40.97           O  
-ATOM  21589  CB  VAL F 293       1.974 -83.799 -71.876  1.00 31.20           C  
-ATOM  21590  CG1 VAL F 293       1.219 -84.293 -70.661  1.00 30.42           C  
-ATOM  21591  CG2 VAL F 293       2.537 -84.974 -72.661  1.00 22.91           C  
-ATOM  21592  N   LEU F 294       1.573 -80.738 -71.947  1.00 36.15           N  
-ATOM  21593  CA  LEU F 294       1.291 -79.404 -71.436  1.00 30.33           C  
-ATOM  21594  C   LEU F 294       0.120 -78.784 -72.180  1.00 39.95           C  
-ATOM  21595  O   LEU F 294      -0.677 -78.053 -71.595  1.00 49.96           O  
-ATOM  21596  CB  LEU F 294       2.516 -78.500 -71.568  1.00 28.14           C  
-ATOM  21597  CG  LEU F 294       3.753 -78.872 -70.755  1.00 32.45           C  
-ATOM  21598  CD1 LEU F 294       4.803 -77.780 -70.864  1.00 27.26           C  
-ATOM  21599  CD2 LEU F 294       3.380 -79.115 -69.308  1.00 34.26           C  
-ATOM  21600  N   ALA F 295       0.027 -79.083 -73.474  1.00 38.06           N  
-ATOM  21601  CA  ALA F 295      -1.049 -78.569 -74.313  1.00 38.93           C  
-ATOM  21602  C   ALA F 295      -2.422 -78.938 -73.757  1.00 44.01           C  
-ATOM  21603  O   ALA F 295      -3.215 -78.058 -73.417  1.00 51.75           O  
-ATOM  21604  CB  ALA F 295      -0.900 -79.083 -75.739  1.00 40.66           C  
-ATOM  21605  N   TRP F 296      -2.696 -80.236 -73.651  1.00 43.14           N  
-ATOM  21606  CA  TRP F 296      -4.006 -80.691 -73.197  1.00 43.70           C  
-ATOM  21607  C   TRP F 296      -4.204 -80.409 -71.715  1.00 41.26           C  
-ATOM  21608  O   TRP F 296      -5.330 -80.199 -71.268  1.00 44.49           O  
-ATOM  21609  CB  TRP F 296      -4.211 -82.185 -73.486  1.00 40.62           C  
-ATOM  21610  CG  TRP F 296      -3.468 -83.150 -72.593  1.00 41.65           C  
-ATOM  21611  CD1 TRP F 296      -2.298 -83.793 -72.876  1.00 43.71           C  
-ATOM  21612  CD2 TRP F 296      -3.869 -83.606 -71.290  1.00 37.84           C  
-ATOM  21613  NE1 TRP F 296      -1.936 -84.606 -71.828  1.00 32.85           N  
-ATOM  21614  CE2 TRP F 296      -2.883 -84.509 -70.843  1.00 34.71           C  
-ATOM  21615  CE3 TRP F 296      -4.958 -83.330 -70.457  1.00 31.53           C  
-ATOM  21616  CZ2 TRP F 296      -2.954 -85.136 -69.602  1.00 32.43           C  
-ATOM  21617  CZ3 TRP F 296      -5.025 -83.950 -69.226  1.00 24.87           C  
-ATOM  21618  CH2 TRP F 296      -4.029 -84.843 -68.809  1.00 31.67           C  
-ATOM  21619  N   MET F 297      -3.115 -80.398 -70.953  1.00 36.43           N  
-ATOM  21620  CA  MET F 297      -3.216 -80.078 -69.533  1.00 36.80           C  
-ATOM  21621  C   MET F 297      -3.596 -78.616 -69.312  1.00 51.11           C  
-ATOM  21622  O   MET F 297      -4.213 -78.277 -68.303  1.00 55.98           O  
-ATOM  21623  CB  MET F 297      -1.906 -80.393 -68.816  1.00 38.95           C  
-ATOM  21624  CG  MET F 297      -1.687 -81.872 -68.577  1.00 30.38           C  
-ATOM  21625  SD  MET F 297      -0.229 -82.206 -67.584  1.00 26.74           S  
-ATOM  21626  CE  MET F 297      -0.372 -83.982 -67.407  1.00 39.51           C  
-ATOM  21627  N   ASP F 298      -3.235 -77.753 -70.258  1.00 58.29           N  
-ATOM  21628  CA  ASP F 298      -3.528 -76.327 -70.135  1.00 66.28           C  
-ATOM  21629  C   ASP F 298      -4.863 -75.953 -70.778  1.00 66.91           C  
-ATOM  21630  O   ASP F 298      -5.533 -75.028 -70.317  1.00 71.75           O  
-ATOM  21631  CB  ASP F 298      -2.405 -75.487 -70.750  1.00 54.90           C  
-ATOM  21632  CG  ASP F 298      -2.604 -73.998 -70.521  1.00 74.07           C  
-ATOM  21633  OD1 ASP F 298      -3.252 -73.632 -69.515  1.00 82.26           O  
-ATOM  21634  OD2 ASP F 298      -2.115 -73.191 -71.340  1.00 86.01           O  
-ATOM  21635  N   GLU F 299      -5.227 -76.674 -71.838  1.00 61.09           N  
-ATOM  21636  CA  GLU F 299      -6.447 -76.422 -72.613  1.00 61.92           C  
-ATOM  21637  C   GLU F 299      -7.646 -76.008 -71.767  1.00 69.55           C  
-ATOM  21638  O   GLU F 299      -8.101 -74.865 -71.833  1.00 67.96           O  
-ATOM  21639  CB  GLU F 299      -6.819 -77.664 -73.424  1.00 55.44           C  
-ATOM  21640  CG  GLU F 299      -6.079 -77.793 -74.741  1.00 68.82           C  
-ATOM  21641  CD  GLU F 299      -6.441 -79.066 -75.478  1.00 70.32           C  
-ATOM  21642  OE1 GLU F 299      -7.323 -79.806 -74.989  1.00 60.92           O  
-ATOM  21643  OE2 GLU F 299      -5.845 -79.329 -76.544  1.00 66.51           O  
-ATOM  21644  N   GLU F 300      -8.154 -76.944 -70.976  1.00 74.51           N  
-ATOM  21645  CA  GLU F 300      -9.255 -76.658 -70.067  1.00 83.06           C  
-ATOM  21646  C   GLU F 300      -8.729 -76.431 -68.652  1.00 79.79           C  
-ATOM  21647  O   GLU F 300      -8.194 -77.348 -68.027  1.00 77.75           O  
-ATOM  21648  CB  GLU F 300     -10.278 -77.798 -70.092  1.00 91.38           C  
-ATOM  21649  CG  GLU F 300     -11.175 -77.872 -68.868  1.00 90.34           C  
-ATOM  21650  CD  GLU F 300     -10.805 -79.026 -67.954  1.00 89.78           C  
-ATOM  21651  OE1 GLU F 300     -10.862 -78.853 -66.717  1.00 72.86           O  
-ATOM  21652  OE2 GLU F 300     -10.459 -80.107 -68.477  1.00 89.39           O  
-ATOM  21653  N   ASP F 301      -8.867 -75.203 -68.155  1.00 71.66           N  
-ATOM  21654  CA  ASP F 301      -9.498 -74.123 -68.907  1.00 66.96           C  
-ATOM  21655  C   ASP F 301      -8.464 -73.090 -69.345  1.00 53.32           C  
-ATOM  21656  O   ASP F 301      -7.443 -72.900 -68.683  1.00 40.00           O  
-ATOM  21657  CB  ASP F 301     -10.593 -73.456 -68.067  1.00 84.58           C  
-ATOM  21658  CG  ASP F 301     -11.777 -72.993 -68.903  1.00 81.21           C  
-ATOM  21659  OD1 ASP F 301     -12.678 -73.819 -69.162  1.00 63.72           O  
-ATOM  21660  OD2 ASP F 301     -11.812 -71.805 -69.292  1.00 61.07           O  
-ATOM  21661  N   LYS F 308     -13.056 -63.190 -68.280  1.00 56.00           N  
-ATOM  21662  CA  LYS F 308     -13.057 -63.328 -69.732  1.00 69.98           C  
-ATOM  21663  C   LYS F 308     -11.933 -62.504 -70.349  1.00 64.10           C  
-ATOM  21664  O   LYS F 308     -11.088 -63.030 -71.074  1.00 59.01           O  
-ATOM  21665  CB  LYS F 308     -14.410 -62.906 -70.310  1.00 69.59           C  
-ATOM  21666  CG  LYS F 308     -14.829 -63.691 -71.543  1.00 65.65           C  
-ATOM  21667  CD  LYS F 308     -15.119 -65.147 -71.200  1.00 66.60           C  
-ATOM  21668  CE  LYS F 308     -14.070 -66.087 -71.778  1.00 63.91           C  
-ATOM  21669  NZ  LYS F 308     -14.382 -67.510 -71.468  1.00 64.71           N  
-ATOM  21670  N   GLU F 309     -11.937 -61.207 -70.058  1.00 51.31           N  
-ATOM  21671  CA  GLU F 309     -10.846 -60.325 -70.457  1.00 65.04           C  
-ATOM  21672  C   GLU F 309     -10.052 -59.892 -69.227  1.00 61.84           C  
-ATOM  21673  O   GLU F 309     -10.509 -59.067 -68.435  1.00 57.31           O  
-ATOM  21674  CB  GLU F 309     -11.377 -59.107 -71.219  1.00 71.80           C  
-ATOM  21675  CG  GLU F 309     -10.923 -59.047 -72.672  1.00 81.02           C  
-ATOM  21676  CD  GLU F 309     -11.491 -57.851 -73.417  1.00 92.42           C  
-ATOM  21677  OE1 GLU F 309     -12.730 -57.693 -73.438  1.00 82.64           O  
-ATOM  21678  OE2 GLU F 309     -10.696 -57.068 -73.981  1.00 89.24           O  
-ATOM  21679  N   LEU F 310      -8.863 -60.467 -69.081  1.00 58.15           N  
-ATOM  21680  CA  LEU F 310      -8.024 -60.273 -67.904  1.00 44.89           C  
-ATOM  21681  C   LEU F 310      -7.644 -58.816 -67.681  1.00 39.55           C  
-ATOM  21682  O   LEU F 310      -7.157 -58.151 -68.594  1.00 52.05           O  
-ATOM  21683  CB  LEU F 310      -6.752 -61.115 -68.027  1.00 50.26           C  
-ATOM  21684  CG  LEU F 310      -6.924 -62.603 -68.328  1.00 35.22           C  
-ATOM  21685  CD1 LEU F 310      -5.662 -63.157 -68.966  1.00 43.51           C  
-ATOM  21686  CD2 LEU F 310      -7.268 -63.374 -67.063  1.00 27.10           C  
-ATOM  21687  N   ILE F 311      -7.865 -58.326 -66.465  1.00 45.42           N  
-ATOM  21688  CA  ILE F 311      -7.378 -57.006 -66.082  1.00 49.91           C  
-ATOM  21689  C   ILE F 311      -5.971 -57.152 -65.509  1.00 48.13           C  
-ATOM  21690  O   ILE F 311      -5.606 -58.215 -65.000  1.00 35.48           O  
-ATOM  21691  CB  ILE F 311      -8.303 -56.310 -65.055  1.00 39.89           C  
-ATOM  21692  CG1 ILE F 311      -8.052 -56.828 -63.640  1.00 35.64           C  
-ATOM  21693  CG2 ILE F 311      -9.760 -56.490 -65.433  1.00 46.67           C  
-ATOM  21694  CD1 ILE F 311      -7.506 -55.773 -62.704  1.00 39.20           C  
-ATOM  21695  N   ARG F 312      -5.179 -56.090 -65.596  1.00 36.08           N  
-ATOM  21696  CA  ARG F 312      -3.787 -56.162 -65.177  1.00 34.68           C  
-ATOM  21697  C   ARG F 312      -3.240 -54.790 -64.808  1.00 37.72           C  
-ATOM  21698  O   ARG F 312      -3.521 -53.798 -65.478  1.00 44.50           O  
-ATOM  21699  CB  ARG F 312      -2.940 -56.794 -66.284  1.00 44.56           C  
-ATOM  21700  CG  ARG F 312      -1.452 -56.846 -65.988  1.00 51.07           C  
-ATOM  21701  CD  ARG F 312      -0.748 -57.822 -66.913  1.00 50.78           C  
-ATOM  21702  NE  ARG F 312       0.697 -57.841 -66.702  1.00 48.66           N  
-ATOM  21703  CZ  ARG F 312       1.303 -58.500 -65.718  1.00 59.77           C  
-ATOM  21704  NH1 ARG F 312       2.624 -58.462 -65.611  1.00 54.19           N  
-ATOM  21705  NH2 ARG F 312       0.591 -59.191 -64.835  1.00 63.20           N  
-ATOM  21706  N   ALA F 313      -2.459 -54.741 -63.733  1.00 34.20           N  
-ATOM  21707  CA  ALA F 313      -1.859 -53.492 -63.280  1.00 34.98           C  
-ATOM  21708  C   ALA F 313      -0.794 -53.006 -64.253  1.00 32.60           C  
-ATOM  21709  O   ALA F 313       0.170 -53.721 -64.520  1.00 32.95           O  
-ATOM  21710  CB  ALA F 313      -1.264 -53.666 -61.899  1.00 34.57           C  
-ATOM  21711  N   VAL F 314      -0.976 -51.777 -64.742  1.00 32.24           N  
-ATOM  21712  CA  VAL F 314      -0.112 -51.128 -65.739  1.00 28.62           C  
-ATOM  21713  C   VAL F 314       0.681 -52.096 -66.620  1.00 33.99           C  
-ATOM  21714  O   VAL F 314       1.898 -52.213 -66.486  1.00 37.00           O  
-ATOM  21715  CB  VAL F 314       0.877 -50.138 -65.066  1.00 32.61           C  
-ATOM  21716  CG1 VAL F 314       0.168 -48.837 -64.728  1.00 33.96           C  
-ATOM  21717  CG2 VAL F 314       1.521 -50.743 -63.817  1.00 29.59           C  
-ATOM  21718  N   PRO F 315      -0.015 -52.782 -67.540  1.00 34.97           N  
-ATOM  21719  CA  PRO F 315       0.554 -53.862 -68.357  1.00 40.12           C  
-ATOM  21720  C   PRO F 315       1.742 -53.439 -69.221  1.00 36.37           C  
-ATOM  21721  O   PRO F 315       2.511 -54.296 -69.657  1.00 38.12           O  
-ATOM  21722  CB  PRO F 315      -0.625 -54.290 -69.239  1.00 42.28           C  
-ATOM  21723  CG  PRO F 315      -1.521 -53.105 -69.271  1.00 43.43           C  
-ATOM  21724  CD  PRO F 315      -1.408 -52.489 -67.915  1.00 35.04           C  
-ATOM  21725  N   HIS F 316       1.891 -52.141 -69.463  1.00 39.19           N  
-ATOM  21726  CA  HIS F 316       3.006 -51.645 -70.262  1.00 41.96           C  
-ATOM  21727  C   HIS F 316       4.334 -51.809 -69.530  1.00 38.01           C  
-ATOM  21728  O   HIS F 316       5.393 -51.842 -70.151  1.00 44.71           O  
-ATOM  21729  CB  HIS F 316       2.788 -50.178 -70.638  1.00 34.98           C  
-ATOM  21730  CG  HIS F 316       2.355 -49.317 -69.493  1.00 40.82           C  
-ATOM  21731  ND1 HIS F 316       1.030 -49.078 -69.201  1.00 45.59           N  
-ATOM  21732  CD2 HIS F 316       3.072 -48.637 -68.567  1.00 45.66           C  
-ATOM  21733  CE1 HIS F 316       0.948 -48.288 -68.145  1.00 42.26           C  
-ATOM  21734  NE2 HIS F 316       2.174 -48.006 -67.741  1.00 37.86           N  
-ATOM  21735  N   VAL F 317       4.276 -51.917 -68.208  1.00 36.91           N  
-ATOM  21736  CA  VAL F 317       5.482 -52.102 -67.413  1.00 37.11           C  
-ATOM  21737  C   VAL F 317       5.874 -53.572 -67.360  1.00 43.71           C  
-ATOM  21738  O   VAL F 317       5.315 -54.343 -66.580  1.00 42.94           O  
-ATOM  21739  CB  VAL F 317       5.304 -51.578 -65.981  1.00 39.97           C  
-ATOM  21740  CG1 VAL F 317       6.585 -51.781 -65.177  1.00 39.49           C  
-ATOM  21741  CG2 VAL F 317       4.907 -50.111 -66.001  1.00 30.42           C  
-ATOM  21742  N   HIS F 318       6.841 -53.952 -68.190  1.00 52.51           N  
-ATOM  21743  CA  HIS F 318       7.294 -55.337 -68.253  1.00 55.34           C  
-ATOM  21744  C   HIS F 318       8.130 -55.727 -67.041  1.00 45.84           C  
-ATOM  21745  O   HIS F 318       7.890 -56.767 -66.429  1.00 44.73           O  
-ATOM  21746  CB  HIS F 318       8.084 -55.585 -69.538  1.00 59.46           C  
-ATOM  21747  CG  HIS F 318       7.304 -56.311 -70.590  1.00 74.97           C  
-ATOM  21748  ND1 HIS F 318       7.063 -57.667 -70.532  1.00 75.69           N  
-ATOM  21749  CD2 HIS F 318       6.713 -55.872 -71.726  1.00 75.39           C  
-ATOM  21750  CE1 HIS F 318       6.356 -58.032 -71.587  1.00 77.25           C  
-ATOM  21751  NE2 HIS F 318       6.131 -56.961 -72.328  1.00 83.73           N  
-ATOM  21752  N   PHE F 319       9.110 -54.901 -66.690  1.00 44.86           N  
-ATOM  21753  CA  PHE F 319       9.988 -55.245 -65.570  1.00 45.99           C  
-ATOM  21754  C   PHE F 319       9.521 -54.596 -64.268  1.00 42.68           C  
-ATOM  21755  O   PHE F 319       9.794 -53.424 -64.002  1.00 39.34           O  
-ATOM  21756  CB  PHE F 319      11.431 -54.856 -65.887  1.00 45.16           C  
-ATOM  21757  CG  PHE F 319      11.927 -55.400 -67.198  1.00 66.86           C  
-ATOM  21758  CD1 PHE F 319      12.245 -56.742 -67.329  1.00 73.13           C  
-ATOM  21759  CD2 PHE F 319      12.067 -54.572 -68.301  1.00 67.81           C  
-ATOM  21760  CE1 PHE F 319      12.696 -57.249 -68.537  1.00 70.77           C  
-ATOM  21761  CE2 PHE F 319      12.518 -55.073 -69.509  1.00 68.77           C  
-ATOM  21762  CZ  PHE F 319      12.833 -56.413 -69.626  1.00 69.58           C  
-ATOM  21763  N   ARG F 320       8.829 -55.389 -63.456  1.00 37.04           N  
-ATOM  21764  CA  ARG F 320       8.116 -54.890 -62.287  1.00 30.13           C  
-ATOM  21765  C   ARG F 320       8.826 -55.209 -60.973  1.00 24.64           C  
-ATOM  21766  O   ARG F 320       8.433 -56.128 -60.254  1.00 22.82           O  
-ATOM  21767  CB  ARG F 320       6.704 -55.473 -62.272  1.00 28.55           C  
-ATOM  21768  CG  ARG F 320       5.882 -55.097 -63.494  1.00 29.80           C  
-ATOM  21769  CD  ARG F 320       4.908 -56.196 -63.873  1.00 31.29           C  
-ATOM  21770  NE  ARG F 320       3.567 -55.674 -64.114  1.00 29.92           N  
-ATOM  21771  CZ  ARG F 320       2.553 -55.803 -63.264  1.00 32.40           C  
-ATOM  21772  NH1 ARG F 320       1.366 -55.297 -63.563  1.00 31.57           N  
-ATOM  21773  NH2 ARG F 320       2.724 -56.444 -62.117  1.00 34.44           N  
-ATOM  21774  N   GLY F 321       9.858 -54.435 -60.655  1.00 23.84           N  
-ATOM  21775  CA  GLY F 321      10.654 -54.672 -59.464  1.00 21.08           C  
-ATOM  21776  C   GLY F 321      10.064 -54.090 -58.193  1.00 17.97           C  
-ATOM  21777  O   GLY F 321      10.409 -54.523 -57.094  1.00 24.95           O  
-ATOM  21778  N   HIS F 322       9.182 -53.107 -58.341  1.00 18.20           N  
-ATOM  21779  CA  HIS F 322       8.550 -52.458 -57.197  1.00 22.69           C  
-ATOM  21780  C   HIS F 322       7.735 -53.469 -56.400  1.00 26.71           C  
-ATOM  21781  O   HIS F 322       7.060 -54.320 -56.978  1.00 29.66           O  
-ATOM  21782  CB  HIS F 322       7.657 -51.303 -57.656  1.00 26.42           C  
-ATOM  21783  CG  HIS F 322       7.448 -50.246 -56.615  1.00 33.25           C  
-ATOM  21784  ND1 HIS F 322       6.766 -50.479 -55.440  1.00 23.18           N  
-ATOM  21785  CD2 HIS F 322       7.827 -48.947 -56.578  1.00 28.95           C  
-ATOM  21786  CE1 HIS F 322       6.738 -49.370 -54.722  1.00 20.84           C  
-ATOM  21787  NE2 HIS F 322       7.374 -48.425 -55.391  1.00 23.59           N  
-ATOM  21788  N   GLU F 323       7.797 -53.373 -55.076  1.00 24.86           N  
-ATOM  21789  CA  GLU F 323       7.140 -54.349 -54.213  1.00 19.62           C  
-ATOM  21790  C   GLU F 323       5.629 -54.124 -54.112  1.00 23.26           C  
-ATOM  21791  O   GLU F 323       4.902 -55.001 -53.651  1.00 29.34           O  
-ATOM  21792  CB  GLU F 323       7.771 -54.333 -52.817  1.00 23.11           C  
-ATOM  21793  CG  GLU F 323       9.197 -54.880 -52.781  1.00 22.50           C  
-ATOM  21794  CD  GLU F 323       9.814 -54.865 -51.391  1.00 27.65           C  
-ATOM  21795  OE1 GLU F 323      10.949 -55.367 -51.245  1.00 23.92           O  
-ATOM  21796  OE2 GLU F 323       9.174 -54.352 -50.447  1.00 30.65           O  
-ATOM  21797  N   GLU F 324       5.159 -52.959 -54.551  1.00 23.36           N  
-ATOM  21798  CA  GLU F 324       3.730 -52.637 -54.530  1.00 20.89           C  
-ATOM  21799  C   GLU F 324       2.971 -53.439 -55.594  1.00 29.92           C  
-ATOM  21800  O   GLU F 324       1.747 -53.643 -55.508  1.00 34.75           O  
-ATOM  21801  CB  GLU F 324       3.526 -51.132 -54.734  1.00 18.64           C  
-ATOM  21802  CG  GLU F 324       2.073 -50.681 -54.728  1.00 17.14           C  
-ATOM  21803  CD  GLU F 324       1.909 -49.230 -54.314  1.00 25.03           C  
-ATOM  21804  OE1 GLU F 324       0.768 -48.724 -54.337  1.00 17.63           O  
-ATOM  21805  OE2 GLU F 324       2.923 -48.598 -53.952  1.00 34.04           O  
-ATOM  21806  N   PHE F 325       3.715 -53.908 -56.591  1.00 25.29           N  
-ATOM  21807  CA  PHE F 325       3.166 -54.776 -57.621  1.00 20.00           C  
-ATOM  21808  C   PHE F 325       2.628 -56.072 -57.020  1.00 22.67           C  
-ATOM  21809  O   PHE F 325       1.818 -56.754 -57.641  1.00 31.08           O  
-ATOM  21810  CB  PHE F 325       4.222 -55.086 -58.686  1.00 25.99           C  
-ATOM  21811  CG  PHE F 325       4.434 -53.974 -59.673  1.00 24.55           C  
-ATOM  21812  CD1 PHE F 325       3.423 -53.608 -60.545  1.00 26.33           C  
-ATOM  21813  CD2 PHE F 325       5.646 -53.306 -59.741  1.00 24.07           C  
-ATOM  21814  CE1 PHE F 325       3.611 -52.590 -61.463  1.00 25.55           C  
-ATOM  21815  CE2 PHE F 325       5.841 -52.286 -60.660  1.00 25.31           C  
-ATOM  21816  CZ  PHE F 325       4.822 -51.929 -61.521  1.00 24.01           C  
-ATOM  21817  N   GLN F 326       3.085 -56.414 -55.819  1.00 17.82           N  
-ATOM  21818  CA  GLN F 326       2.499 -57.524 -55.083  1.00 19.26           C  
-ATOM  21819  C   GLN F 326       1.030 -57.233 -54.825  1.00 21.81           C  
-ATOM  21820  O   GLN F 326       0.154 -58.051 -55.114  1.00 24.67           O  
-ATOM  21821  CB  GLN F 326       3.225 -57.755 -53.757  1.00 20.37           C  
-ATOM  21822  CG  GLN F 326       4.652 -58.243 -53.885  1.00 13.38           C  
-ATOM  21823  CD  GLN F 326       5.232 -58.652 -52.547  1.00 17.22           C  
-ATOM  21824  OE1 GLN F 326       5.047 -59.782 -52.095  1.00 19.89           O  
-ATOM  21825  NE2 GLN F 326       5.930 -57.729 -51.898  1.00 23.79           N  
-ATOM  21826  N   TYR F 327       0.781 -56.047 -54.282  1.00 21.57           N  
-ATOM  21827  CA  TYR F 327      -0.564 -55.601 -53.949  1.00 21.36           C  
-ATOM  21828  C   TYR F 327      -1.425 -55.422 -55.193  1.00 20.60           C  
-ATOM  21829  O   TYR F 327      -2.567 -55.889 -55.240  1.00 22.38           O  
-ATOM  21830  CB  TYR F 327      -0.497 -54.294 -53.155  1.00 13.18           C  
-ATOM  21831  CG  TYR F 327      -1.835 -53.662 -52.868  1.00 13.10           C  
-ATOM  21832  CD1 TYR F 327      -2.683 -54.190 -51.904  1.00 16.88           C  
-ATOM  21833  CD2 TYR F 327      -2.246 -52.527 -53.553  1.00 13.84           C  
-ATOM  21834  CE1 TYR F 327      -3.907 -53.609 -51.636  1.00 19.17           C  
-ATOM  21835  CE2 TYR F 327      -3.466 -51.939 -53.292  1.00 15.93           C  
-ATOM  21836  CZ  TYR F 327      -4.293 -52.484 -52.333  1.00 20.37           C  
-ATOM  21837  OH  TYR F 327      -5.510 -51.898 -52.070  1.00 26.44           O  
-ATOM  21838  N   LEU F 328      -0.879 -54.750 -56.201  1.00 16.14           N  
-ATOM  21839  CA  LEU F 328      -1.622 -54.532 -57.437  1.00 19.61           C  
-ATOM  21840  C   LEU F 328      -1.995 -55.854 -58.115  1.00 23.98           C  
-ATOM  21841  O   LEU F 328      -3.159 -56.071 -58.481  1.00 28.07           O  
-ATOM  21842  CB  LEU F 328      -0.814 -53.652 -58.386  1.00 22.32           C  
-ATOM  21843  CG  LEU F 328      -0.476 -52.262 -57.844  1.00 21.08           C  
-ATOM  21844  CD1 LEU F 328       0.294 -51.450 -58.872  1.00 25.57           C  
-ATOM  21845  CD2 LEU F 328      -1.741 -51.535 -57.416  1.00 17.55           C  
-ATOM  21846  N   ASP F 329      -1.013 -56.740 -58.267  1.00 21.50           N  
-ATOM  21847  CA  ASP F 329      -1.259 -58.056 -58.849  1.00 20.55           C  
-ATOM  21848  C   ASP F 329      -2.188 -58.888 -57.977  1.00 24.25           C  
-ATOM  21849  O   ASP F 329      -2.836 -59.805 -58.465  1.00 29.73           O  
-ATOM  21850  CB  ASP F 329       0.049 -58.817 -59.069  1.00 30.19           C  
-ATOM  21851  CG  ASP F 329       0.869 -58.254 -60.214  1.00 41.07           C  
-ATOM  21852  OD1 ASP F 329       0.282 -57.615 -61.115  1.00 43.68           O  
-ATOM  21853  OD2 ASP F 329       2.102 -58.463 -60.212  1.00 25.85           O  
-ATOM  21854  N   LEU F 330      -2.234 -58.582 -56.685  1.00 24.93           N  
-ATOM  21855  CA  LEU F 330      -3.178 -59.241 -55.794  1.00 17.67           C  
-ATOM  21856  C   LEU F 330      -4.589 -58.799 -56.145  1.00 20.99           C  
-ATOM  21857  O   LEU F 330      -5.494 -59.624 -56.265  1.00 24.68           O  
-ATOM  21858  CB  LEU F 330      -2.865 -58.933 -54.329  1.00 19.28           C  
-ATOM  21859  CG  LEU F 330      -3.908 -59.413 -53.316  1.00 21.91           C  
-ATOM  21860  CD1 LEU F 330      -4.122 -60.916 -53.427  1.00 17.75           C  
-ATOM  21861  CD2 LEU F 330      -3.498 -59.027 -51.903  1.00 19.72           C  
-ATOM  21862  N   ILE F 331      -4.764 -57.490 -56.310  1.00 21.29           N  
-ATOM  21863  CA  ILE F 331      -6.041 -56.934 -56.752  1.00 23.97           C  
-ATOM  21864  C   ILE F 331      -6.496 -57.605 -58.038  1.00 24.18           C  
-ATOM  21865  O   ILE F 331      -7.593 -58.172 -58.113  1.00 17.69           O  
-ATOM  21866  CB  ILE F 331      -5.956 -55.411 -57.000  1.00 24.27           C  
-ATOM  21867  CG1 ILE F 331      -5.498 -54.682 -55.733  1.00 24.07           C  
-ATOM  21868  CG2 ILE F 331      -7.288 -54.883 -57.521  1.00 22.90           C  
-ATOM  21869  CD1 ILE F 331      -6.497 -53.685 -55.187  1.00 24.61           C  
-ATOM  21870  N   ALA F 332      -5.628 -57.544 -59.044  1.00 29.41           N  
-ATOM  21871  CA  ALA F 332      -5.912 -58.134 -60.346  1.00 26.27           C  
-ATOM  21872  C   ALA F 332      -6.275 -59.610 -60.232  1.00 31.19           C  
-ATOM  21873  O   ALA F 332      -7.267 -60.052 -60.806  1.00 35.76           O  
-ATOM  21874  CB  ALA F 332      -4.725 -57.956 -61.276  1.00 28.37           C  
-ATOM  21875  N   ASP F 333      -5.475 -60.366 -59.486  1.00 34.56           N  
-ATOM  21876  CA  ASP F 333      -5.683 -61.805 -59.358  1.00 37.14           C  
-ATOM  21877  C   ASP F 333      -7.008 -62.119 -58.680  1.00 39.18           C  
-ATOM  21878  O   ASP F 333      -7.670 -63.096 -59.021  1.00 46.04           O  
-ATOM  21879  CB  ASP F 333      -4.534 -62.452 -58.581  1.00 34.68           C  
-ATOM  21880  CG  ASP F 333      -4.679 -63.958 -58.472  1.00 54.42           C  
-ATOM  21881  OD1 ASP F 333      -4.457 -64.654 -59.485  1.00 47.06           O  
-ATOM  21882  OD2 ASP F 333      -5.012 -64.447 -57.371  1.00 65.09           O  
-ATOM  21883  N   ILE F 334      -7.392 -61.289 -57.718  1.00 31.89           N  
-ATOM  21884  CA  ILE F 334      -8.655 -61.494 -57.024  1.00 26.64           C  
-ATOM  21885  C   ILE F 334      -9.831 -61.183 -57.941  1.00 28.26           C  
-ATOM  21886  O   ILE F 334     -10.803 -61.934 -57.985  1.00 27.14           O  
-ATOM  21887  CB  ILE F 334      -8.747 -60.636 -55.755  1.00 29.70           C  
-ATOM  21888  CG1 ILE F 334      -7.767 -61.154 -54.707  1.00 22.75           C  
-ATOM  21889  CG2 ILE F 334     -10.156 -60.657 -55.198  1.00 22.54           C  
-ATOM  21890  CD1 ILE F 334      -7.818 -60.399 -53.417  1.00 21.58           C  
-ATOM  21891  N   ILE F 335      -9.742 -60.080 -58.680  1.00 37.06           N  
-ATOM  21892  CA  ILE F 335     -10.835 -59.704 -59.573  1.00 35.62           C  
-ATOM  21893  C   ILE F 335     -10.996 -60.717 -60.711  1.00 37.18           C  
-ATOM  21894  O   ILE F 335     -12.116 -61.052 -61.100  1.00 45.10           O  
-ATOM  21895  CB  ILE F 335     -10.628 -58.295 -60.160  1.00 28.42           C  
-ATOM  21896  CG1 ILE F 335     -10.625 -57.253 -59.039  1.00 19.16           C  
-ATOM  21897  CG2 ILE F 335     -11.716 -57.969 -61.168  1.00 25.86           C  
-ATOM  21898  CD1 ILE F 335     -10.516 -55.828 -59.532  1.00 16.55           C  
-ATOM  21899  N   ASN F 336      -9.878 -61.224 -61.221  1.00 31.59           N  
-ATOM  21900  CA  ASN F 336      -9.902 -62.165 -62.338  1.00 32.07           C  
-ATOM  21901  C   ASN F 336     -10.250 -63.602 -61.944  1.00 30.46           C  
-ATOM  21902  O   ASN F 336     -10.984 -64.280 -62.661  1.00 38.52           O  
-ATOM  21903  CB  ASN F 336      -8.552 -62.160 -63.059  1.00 28.97           C  
-ATOM  21904  CG  ASN F 336      -8.284 -60.859 -63.793  1.00 35.74           C  
-ATOM  21905  OD1 ASN F 336      -9.204 -60.214 -64.293  1.00 44.77           O  
-ATOM  21906  ND2 ASN F 336      -7.019 -60.467 -63.861  1.00 27.62           N  
-ATOM  21907  N   ASN F 337      -9.733 -64.063 -60.808  1.00 32.65           N  
-ATOM  21908  CA  ASN F 337      -9.808 -65.481 -60.459  1.00 32.18           C  
-ATOM  21909  C   ASN F 337     -10.590 -65.799 -59.186  1.00 33.84           C  
-ATOM  21910  O   ASN F 337     -10.726 -66.965 -58.808  1.00 34.10           O  
-ATOM  21911  CB  ASN F 337      -8.393 -66.041 -60.327  1.00 29.55           C  
-ATOM  21912  CG  ASN F 337      -7.501 -65.631 -61.476  1.00 34.82           C  
-ATOM  21913  OD1 ASN F 337      -7.869 -65.769 -62.642  1.00 33.13           O  
-ATOM  21914  ND2 ASN F 337      -6.327 -65.106 -61.153  1.00 43.41           N  
-ATOM  21915  N   GLY F 338     -11.101 -64.769 -58.522  1.00 37.22           N  
-ATOM  21916  CA  GLY F 338     -11.824 -64.966 -57.279  1.00 29.94           C  
-ATOM  21917  C   GLY F 338     -13.236 -65.464 -57.513  1.00 34.68           C  
-ATOM  21918  O   GLY F 338     -13.699 -65.519 -58.651  1.00 42.56           O  
-ATOM  21919  N   ARG F 339     -13.918 -65.835 -56.434  1.00 40.39           N  
-ATOM  21920  CA  ARG F 339     -15.311 -66.266 -56.517  1.00 35.09           C  
-ATOM  21921  C   ARG F 339     -16.223 -65.204 -55.911  1.00 36.24           C  
-ATOM  21922  O   ARG F 339     -15.898 -64.621 -54.878  1.00 35.20           O  
-ATOM  21923  CB  ARG F 339     -15.510 -67.607 -55.802  1.00 33.03           C  
-ATOM  21924  CG  ARG F 339     -14.721 -68.770 -56.389  1.00 35.30           C  
-ATOM  21925  CD  ARG F 339     -15.351 -69.292 -57.675  1.00 44.98           C  
-ATOM  21926  NE  ARG F 339     -14.523 -69.026 -58.848  1.00 62.19           N  
-ATOM  21927  CZ  ARG F 339     -14.988 -68.563 -60.005  1.00 78.38           C  
-ATOM  21928  NH1 ARG F 339     -16.283 -68.310 -60.153  1.00 61.99           N  
-ATOM  21929  NH2 ARG F 339     -14.155 -68.352 -61.017  1.00 83.00           N  
-ATOM  21930  N   THR F 340     -17.359 -64.951 -56.552  1.00 26.63           N  
-ATOM  21931  CA  THR F 340     -18.299 -63.954 -56.051  1.00 29.41           C  
-ATOM  21932  C   THR F 340     -19.160 -64.532 -54.930  1.00 36.20           C  
-ATOM  21933  O   THR F 340     -19.917 -65.479 -55.142  1.00 32.73           O  
-ATOM  21934  CB  THR F 340     -19.203 -63.425 -57.170  1.00 32.83           C  
-ATOM  21935  OG1 THR F 340     -18.392 -62.902 -58.229  1.00 27.92           O  
-ATOM  21936  CG2 THR F 340     -20.120 -62.330 -56.641  1.00 29.15           C  
-ATOM  21937  N   MET F 341     -19.043 -63.955 -53.739  1.00 37.28           N  
-ATOM  21938  CA  MET F 341     -19.701 -64.492 -52.554  1.00 36.57           C  
-ATOM  21939  C   MET F 341     -20.534 -63.446 -51.823  1.00 35.32           C  
-ATOM  21940  O   MET F 341     -20.466 -62.255 -52.130  1.00 36.49           O  
-ATOM  21941  CB  MET F 341     -18.663 -65.068 -51.588  1.00 35.19           C  
-ATOM  21942  CG  MET F 341     -17.649 -66.001 -52.225  1.00 33.27           C  
-ATOM  21943  SD  MET F 341     -18.389 -67.550 -52.760  1.00 51.31           S  
-ATOM  21944  CE  MET F 341     -19.193 -68.066 -51.246  1.00 43.06           C  
-ATOM  21945  N   ASP F 342     -21.316 -63.909 -50.851  1.00 41.66           N  
-ATOM  21946  CA  ASP F 342     -22.015 -63.024 -49.923  1.00 48.26           C  
-ATOM  21947  C   ASP F 342     -21.199 -62.894 -48.639  1.00 52.39           C  
-ATOM  21948  O   ASP F 342     -20.145 -63.519 -48.506  1.00 53.08           O  
-ATOM  21949  CB  ASP F 342     -23.415 -63.553 -49.608  1.00 45.78           C  
-ATOM  21950  CG  ASP F 342     -24.275 -63.708 -50.847  1.00 56.69           C  
-ATOM  21951  OD1 ASP F 342     -24.085 -62.931 -51.808  1.00 63.02           O  
-ATOM  21952  OD2 ASP F 342     -25.144 -64.606 -50.858  1.00 52.50           O  
-ATOM  21953  N   ASP F 343     -21.685 -62.094 -47.694  1.00 49.44           N  
-ATOM  21954  CA  ASP F 343     -20.989 -61.928 -46.422  1.00 52.19           C  
-ATOM  21955  C   ASP F 343     -21.864 -61.321 -45.330  1.00 47.50           C  
-ATOM  21956  O   ASP F 343     -23.064 -61.109 -45.511  1.00 49.25           O  
-ATOM  21957  CB  ASP F 343     -19.741 -61.062 -46.606  1.00 43.03           C  
-ATOM  21958  CG  ASP F 343     -20.069 -59.660 -47.078  1.00 38.99           C  
-ATOM  21959  OD1 ASP F 343     -20.917 -59.518 -47.984  1.00 44.39           O  
-ATOM  21960  OD2 ASP F 343     -19.481 -58.700 -46.536  1.00 41.28           O  
-ATOM  21961  N   ARG F 344     -21.231 -61.051 -44.193  1.00 37.73           N  
-ATOM  21962  CA  ARG F 344     -21.878 -60.433 -43.043  1.00 48.24           C  
-ATOM  21963  C   ARG F 344     -22.582 -59.123 -43.385  1.00 47.53           C  
-ATOM  21964  O   ARG F 344     -23.712 -58.880 -42.954  1.00 46.89           O  
-ATOM  21965  CB  ARG F 344     -20.841 -60.183 -41.944  1.00 59.32           C  
-ATOM  21966  CG  ARG F 344     -21.212 -59.078 -40.966  1.00 54.88           C  
-ATOM  21967  CD  ARG F 344     -21.895 -59.624 -39.717  1.00 68.87           C  
-ATOM  21968  NE  ARG F 344     -23.147 -60.310 -40.023  1.00 89.91           N  
-ATOM  21969  CZ  ARG F 344     -23.866 -60.995 -39.140  1.00 80.85           C  
-ATOM  21970  NH1 ARG F 344     -23.467 -61.096 -37.877  1.00 74.27           N  
-ATOM  21971  NH2 ARG F 344     -24.989 -61.584 -39.525  1.00 67.22           N  
-ATOM  21972  N   THR F 345     -21.902 -58.287 -44.161  1.00 50.00           N  
-ATOM  21973  CA  THR F 345     -22.370 -56.937 -44.452  1.00 48.89           C  
-ATOM  21974  C   THR F 345     -23.548 -56.908 -45.428  1.00 51.08           C  
-ATOM  21975  O   THR F 345     -24.414 -56.034 -45.345  1.00 43.22           O  
-ATOM  21976  CB  THR F 345     -21.226 -56.079 -45.029  1.00 47.84           C  
-ATOM  21977  OG1 THR F 345     -20.927 -56.508 -46.365  1.00 36.50           O  
-ATOM  21978  CG2 THR F 345     -19.976 -56.219 -44.173  1.00 50.79           C  
-ATOM  21979  N   GLY F 346     -23.576 -57.864 -46.351  1.00 55.23           N  
-ATOM  21980  CA  GLY F 346     -24.618 -57.920 -47.360  1.00 50.17           C  
-ATOM  21981  C   GLY F 346     -24.239 -57.138 -48.602  1.00 52.76           C  
-ATOM  21982  O   GLY F 346     -25.058 -56.943 -49.500  1.00 49.23           O  
-ATOM  21983  N   VAL F 347     -22.990 -56.686 -48.649  1.00 49.18           N  
-ATOM  21984  CA  VAL F 347     -22.498 -55.913 -49.781  1.00 42.55           C  
-ATOM  21985  C   VAL F 347     -22.079 -56.845 -50.915  1.00 40.64           C  
-ATOM  21986  O   VAL F 347     -22.292 -56.546 -52.092  1.00 42.10           O  
-ATOM  21987  CB  VAL F 347     -21.315 -55.009 -49.374  1.00 40.38           C  
-ATOM  21988  CG1 VAL F 347     -20.783 -54.247 -50.576  1.00 48.18           C  
-ATOM  21989  CG2 VAL F 347     -21.743 -54.042 -48.280  1.00 41.20           C  
-ATOM  21990  N   GLY F 348     -21.503 -57.987 -50.553  1.00 27.18           N  
-ATOM  21991  CA  GLY F 348     -21.054 -58.959 -51.533  1.00 33.39           C  
-ATOM  21992  C   GLY F 348     -19.601 -58.741 -51.904  1.00 41.95           C  
-ATOM  21993  O   GLY F 348     -19.157 -57.601 -52.052  1.00 45.68           O  
-ATOM  21994  N   VAL F 349     -18.852 -59.831 -52.053  1.00 35.77           N  
-ATOM  21995  CA  VAL F 349     -17.421 -59.726 -52.322  1.00 27.09           C  
-ATOM  21996  C   VAL F 349     -16.971 -60.607 -53.476  1.00 33.90           C  
-ATOM  21997  O   VAL F 349     -17.741 -61.405 -54.004  1.00 39.80           O  
-ATOM  21998  CB  VAL F 349     -16.578 -60.112 -51.090  1.00 24.07           C  
-ATOM  21999  CG1 VAL F 349     -16.988 -59.300 -49.878  1.00 33.85           C  
-ATOM  22000  CG2 VAL F 349     -16.713 -61.599 -50.807  1.00 26.36           C  
-ATOM  22001  N   ILE F 350     -15.712 -60.435 -53.863  1.00 27.57           N  
-ATOM  22002  CA  ILE F 350     -15.017 -61.372 -54.737  1.00 27.93           C  
-ATOM  22003  C   ILE F 350     -13.791 -61.852 -53.971  1.00 32.37           C  
-ATOM  22004  O   ILE F 350     -12.890 -61.067 -53.688  1.00 34.82           O  
-ATOM  22005  CB  ILE F 350     -14.593 -60.732 -56.070  1.00 23.12           C  
-ATOM  22006  CG1 ILE F 350     -15.792 -60.079 -56.756  1.00 23.43           C  
-ATOM  22007  CG2 ILE F 350     -13.949 -61.769 -56.974  1.00 25.27           C  
-ATOM  22008  CD1 ILE F 350     -15.451 -59.395 -58.058  1.00 29.32           C  
-ATOM  22009  N   SER F 351     -13.757 -63.129 -53.613  1.00 27.26           N  
-ATOM  22010  CA  SER F 351     -12.759 -63.579 -52.654  1.00 24.06           C  
-ATOM  22011  C   SER F 351     -11.869 -64.707 -53.151  1.00 26.14           C  
-ATOM  22012  O   SER F 351     -12.224 -65.449 -54.070  1.00 28.93           O  
-ATOM  22013  CB  SER F 351     -13.447 -64.018 -51.360  1.00 32.21           C  
-ATOM  22014  OG  SER F 351     -14.251 -65.162 -51.575  1.00 39.72           O  
-ATOM  22015  N   LYS F 352     -10.697 -64.799 -52.530  1.00 26.59           N  
-ATOM  22016  CA  LYS F 352      -9.792 -65.929 -52.670  1.00 22.99           C  
-ATOM  22017  C   LYS F 352      -9.354 -66.349 -51.274  1.00 35.10           C  
-ATOM  22018  O   LYS F 352      -9.620 -65.640 -50.300  1.00 37.89           O  
-ATOM  22019  CB  LYS F 352      -8.581 -65.575 -53.531  1.00 14.28           C  
-ATOM  22020  CG  LYS F 352      -8.931 -65.169 -54.946  1.00 33.98           C  
-ATOM  22021  CD  LYS F 352      -7.702 -65.175 -55.844  1.00 38.68           C  
-ATOM  22022  CE  LYS F 352      -7.134 -66.576 -55.991  1.00 41.05           C  
-ATOM  22023  NZ  LYS F 352      -6.015 -66.620 -56.974  1.00 42.36           N  
-ATOM  22024  N   PHE F 353      -8.684 -67.492 -51.168  1.00 26.47           N  
-ATOM  22025  CA  PHE F 353      -8.259 -67.990 -49.864  1.00 17.15           C  
-ATOM  22026  C   PHE F 353      -6.788 -68.388 -49.876  1.00 22.50           C  
-ATOM  22027  O   PHE F 353      -6.345 -69.150 -50.737  1.00 29.73           O  
-ATOM  22028  CB  PHE F 353      -9.124 -69.177 -49.441  1.00 16.68           C  
-ATOM  22029  CG  PHE F 353      -9.047 -69.493 -47.975  1.00 16.93           C  
-ATOM  22030  CD1 PHE F 353      -9.290 -68.510 -47.034  1.00 18.13           C  
-ATOM  22031  CD2 PHE F 353      -8.748 -70.773 -47.539  1.00 17.56           C  
-ATOM  22032  CE1 PHE F 353      -9.227 -68.790 -45.680  1.00 21.82           C  
-ATOM  22033  CE2 PHE F 353      -8.692 -71.063 -46.186  1.00 21.87           C  
-ATOM  22034  CZ  PHE F 353      -8.928 -70.068 -45.255  1.00 19.88           C  
-ATOM  22035  N   GLY F 354      -6.033 -67.869 -48.915  1.00 19.64           N  
-ATOM  22036  CA  GLY F 354      -4.614 -68.154 -48.832  1.00 18.03           C  
-ATOM  22037  C   GLY F 354      -3.812 -67.307 -49.797  1.00 20.73           C  
-ATOM  22038  O   GLY F 354      -3.526 -67.723 -50.921  1.00 22.47           O  
-ATOM  22039  N   CYS F 355      -3.456 -66.106 -49.357  1.00 18.33           N  
-ATOM  22040  CA  CYS F 355      -2.663 -65.200 -50.173  1.00 15.14           C  
-ATOM  22041  C   CYS F 355      -1.477 -64.692 -49.371  1.00 18.83           C  
-ATOM  22042  O   CYS F 355      -1.524 -64.640 -48.144  1.00 18.17           O  
-ATOM  22043  CB  CYS F 355      -3.519 -64.040 -50.677  1.00 14.60           C  
-ATOM  22044  SG  CYS F 355      -4.818 -64.554 -51.825  1.00 20.16           S  
-ATOM  22045  N   THR F 356      -0.412 -64.318 -50.069  1.00 23.47           N  
-ATOM  22046  CA  THR F 356       0.848 -64.000 -49.414  1.00 16.37           C  
-ATOM  22047  C   THR F 356       1.526 -62.775 -50.009  1.00 21.57           C  
-ATOM  22048  O   THR F 356       1.632 -62.639 -51.230  1.00 22.31           O  
-ATOM  22049  CB  THR F 356       1.813 -65.202 -49.491  1.00 18.68           C  
-ATOM  22050  OG1 THR F 356       1.446 -66.163 -48.495  1.00 35.02           O  
-ATOM  22051  CG2 THR F 356       3.260 -64.773 -49.262  1.00 22.91           C  
-ATOM  22052  N   MET F 357       1.977 -61.877 -49.139  1.00 21.60           N  
-ATOM  22053  CA  MET F 357       2.840 -60.784 -49.571  1.00 20.14           C  
-ATOM  22054  C   MET F 357       4.039 -60.667 -48.642  1.00 20.53           C  
-ATOM  22055  O   MET F 357       4.014 -61.183 -47.533  1.00 19.74           O  
-ATOM  22056  CB  MET F 357       2.073 -59.465 -49.607  1.00 17.61           C  
-ATOM  22057  CG  MET F 357       1.046 -59.375 -50.714  1.00 18.81           C  
-ATOM  22058  SD  MET F 357       0.178 -57.797 -50.694  1.00 26.36           S  
-ATOM  22059  CE  MET F 357      -0.444 -57.768 -49.014  1.00 17.06           C  
-ATOM  22060  N   ARG F 358       5.095 -60.006 -49.100  1.00 17.20           N  
-ATOM  22061  CA  ARG F 358       6.212 -59.693 -48.218  1.00 19.79           C  
-ATOM  22062  C   ARG F 358       6.919 -58.417 -48.666  1.00 24.71           C  
-ATOM  22063  O   ARG F 358       7.263 -58.254 -49.838  1.00 22.22           O  
-ATOM  22064  CB  ARG F 358       7.199 -60.866 -48.136  1.00 21.58           C  
-ATOM  22065  CG  ARG F 358       7.711 -61.387 -49.464  1.00 32.67           C  
-ATOM  22066  CD  ARG F 358       8.836 -62.398 -49.255  1.00 35.72           C  
-ATOM  22067  NE  ARG F 358       8.397 -63.574 -48.506  1.00 37.72           N  
-ATOM  22068  CZ  ARG F 358       8.951 -63.994 -47.372  1.00 31.00           C  
-ATOM  22069  NH1 ARG F 358       9.974 -63.337 -46.846  1.00 24.39           N  
-ATOM  22070  NH2 ARG F 358       8.484 -65.078 -46.764  1.00 28.85           N  
-ATOM  22071  N   TYR F 359       7.120 -57.509 -47.715  1.00 21.00           N  
-ATOM  22072  CA  TYR F 359       7.700 -56.207 -48.010  1.00 16.49           C  
-ATOM  22073  C   TYR F 359       8.966 -55.991 -47.195  1.00 21.18           C  
-ATOM  22074  O   TYR F 359       8.959 -56.121 -45.972  1.00 24.64           O  
-ATOM  22075  CB  TYR F 359       6.680 -55.095 -47.736  1.00 21.67           C  
-ATOM  22076  CG  TYR F 359       5.444 -55.185 -48.607  1.00 20.49           C  
-ATOM  22077  CD1 TYR F 359       5.360 -54.482 -49.800  1.00 23.39           C  
-ATOM  22078  CD2 TYR F 359       4.368 -55.985 -48.244  1.00 15.89           C  
-ATOM  22079  CE1 TYR F 359       4.238 -54.567 -50.604  1.00 19.52           C  
-ATOM  22080  CE2 TYR F 359       3.243 -56.077 -49.042  1.00 13.84           C  
-ATOM  22081  CZ  TYR F 359       3.184 -55.366 -50.221  1.00 14.84           C  
-ATOM  22082  OH  TYR F 359       2.068 -55.451 -51.022  1.00 17.22           O  
-ATOM  22083  N   SER F 360      10.056 -55.668 -47.882  1.00 24.03           N  
-ATOM  22084  CA  SER F 360      11.347 -55.480 -47.229  1.00 24.59           C  
-ATOM  22085  C   SER F 360      11.404 -54.152 -46.475  1.00 28.45           C  
-ATOM  22086  O   SER F 360      10.805 -53.164 -46.902  1.00 27.55           O  
-ATOM  22087  CB  SER F 360      12.474 -55.555 -48.258  1.00 22.23           C  
-ATOM  22088  OG  SER F 360      13.193 -54.337 -48.307  1.00 49.20           O  
-ATOM  22089  N   LEU F 361      12.138 -54.129 -45.364  1.00 27.38           N  
-ATOM  22090  CA  LEU F 361      12.151 -52.965 -44.480  1.00 23.60           C  
-ATOM  22091  C   LEU F 361      13.514 -52.289 -44.306  1.00 26.12           C  
-ATOM  22092  O   LEU F 361      13.616 -51.284 -43.602  1.00 25.87           O  
-ATOM  22093  CB  LEU F 361      11.626 -53.361 -43.099  1.00 16.11           C  
-ATOM  22094  CG  LEU F 361      10.242 -54.003 -43.032  1.00 22.41           C  
-ATOM  22095  CD1 LEU F 361       9.801 -54.149 -41.585  1.00 18.10           C  
-ATOM  22096  CD2 LEU F 361       9.233 -53.195 -43.828  1.00 22.42           C  
-ATOM  22097  N   ASP F 362      14.556 -52.826 -44.933  1.00 27.84           N  
-ATOM  22098  CA  ASP F 362      15.909 -52.326 -44.688  1.00 22.90           C  
-ATOM  22099  C   ASP F 362      16.228 -51.045 -45.460  1.00 20.34           C  
-ATOM  22100  O   ASP F 362      17.001 -50.211 -44.992  1.00 13.98           O  
-ATOM  22101  CB  ASP F 362      16.943 -53.399 -45.030  1.00 19.70           C  
-ATOM  22102  CG  ASP F 362      16.906 -53.800 -46.489  1.00 29.30           C  
-ATOM  22103  OD1 ASP F 362      15.808 -54.120 -46.991  1.00 27.32           O  
-ATOM  22104  OD2 ASP F 362      17.976 -53.783 -47.135  1.00 30.05           O  
-ATOM  22105  N   GLN F 363      15.641 -50.893 -46.642  1.00 22.36           N  
-ATOM  22106  CA  GLN F 363      15.914 -49.727 -47.473  1.00 18.45           C  
-ATOM  22107  C   GLN F 363      14.853 -48.650 -47.277  1.00 16.85           C  
-ATOM  22108  O   GLN F 363      15.174 -47.489 -47.033  1.00  9.05           O  
-ATOM  22109  CB  GLN F 363      15.993 -50.129 -48.947  1.00 24.50           C  
-ATOM  22110  CG  GLN F 363      17.113 -51.109 -49.266  1.00 30.90           C  
-ATOM  22111  CD  GLN F 363      18.456 -50.429 -49.443  1.00 34.38           C  
-ATOM  22112  OE1 GLN F 363      18.633 -49.602 -50.339  1.00 26.41           O  
-ATOM  22113  NE2 GLN F 363      19.412 -50.775 -48.587  1.00 41.29           N  
-ATOM  22114  N   ALA F 364      13.586 -49.040 -47.375  1.00 24.60           N  
-ATOM  22115  CA  ALA F 364      12.489 -48.086 -47.264  1.00 18.96           C  
-ATOM  22116  C   ALA F 364      11.314 -48.665 -46.485  1.00 17.86           C  
-ATOM  22117  O   ALA F 364      11.405 -49.759 -45.924  1.00 15.43           O  
-ATOM  22118  CB  ALA F 364      12.039 -47.641 -48.646  1.00 13.89           C  
-ATOM  22119  N   PHE F 365      10.214 -47.917 -46.458  1.00 18.13           N  
-ATOM  22120  CA  PHE F 365       9.010 -48.321 -45.739  1.00 16.80           C  
-ATOM  22121  C   PHE F 365       7.846 -48.498 -46.709  1.00 17.56           C  
-ATOM  22122  O   PHE F 365       7.580 -47.622 -47.531  1.00 20.26           O  
-ATOM  22123  CB  PHE F 365       8.654 -47.291 -44.660  1.00 15.34           C  
-ATOM  22124  CG  PHE F 365       7.512 -47.705 -43.773  1.00 14.13           C  
-ATOM  22125  CD1 PHE F 365       6.202 -47.419 -44.126  1.00 17.22           C  
-ATOM  22126  CD2 PHE F 365       7.749 -48.374 -42.582  1.00 10.98           C  
-ATOM  22127  CE1 PHE F 365       5.150 -47.800 -43.314  1.00 14.91           C  
-ATOM  22128  CE2 PHE F 365       6.702 -48.756 -41.766  1.00 12.19           C  
-ATOM  22129  CZ  PHE F 365       5.401 -48.469 -42.132  1.00 14.91           C  
-ATOM  22130  N   PRO F 366       7.141 -49.634 -46.607  1.00 15.14           N  
-ATOM  22131  CA  PRO F 366       6.055 -49.955 -47.536  1.00 16.46           C  
-ATOM  22132  C   PRO F 366       4.787 -49.139 -47.294  1.00 22.62           C  
-ATOM  22133  O   PRO F 366       3.738 -49.711 -46.993  1.00 31.62           O  
-ATOM  22134  CB  PRO F 366       5.804 -51.440 -47.271  1.00 17.74           C  
-ATOM  22135  CG  PRO F 366       6.190 -51.627 -45.849  1.00 17.61           C  
-ATOM  22136  CD  PRO F 366       7.353 -50.702 -45.615  1.00 13.14           C  
-ATOM  22137  N   LEU F 367       4.884 -47.819 -47.425  1.00 17.87           N  
-ATOM  22138  CA  LEU F 367       3.697 -46.973 -47.418  1.00 19.86           C  
-ATOM  22139  C   LEU F 367       3.206 -46.806 -48.852  1.00 19.93           C  
-ATOM  22140  O   LEU F 367       3.832 -46.112 -49.651  1.00 26.14           O  
-ATOM  22141  CB  LEU F 367       3.992 -45.616 -46.780  1.00 14.96           C  
-ATOM  22142  CG  LEU F 367       2.764 -44.793 -46.384  1.00 13.50           C  
-ATOM  22143  CD1 LEU F 367       1.895 -45.554 -45.392  1.00 13.03           C  
-ATOM  22144  CD2 LEU F 367       3.183 -43.452 -45.806  1.00 15.44           C  
-ATOM  22145  N   LEU F 368       2.083 -47.447 -49.163  1.00 14.22           N  
-ATOM  22146  CA  LEU F 368       1.588 -47.572 -50.536  1.00 23.39           C  
-ATOM  22147  C   LEU F 368       1.488 -46.234 -51.274  1.00 26.98           C  
-ATOM  22148  O   LEU F 368       1.192 -45.203 -50.672  1.00 27.12           O  
-ATOM  22149  CB  LEU F 368       0.224 -48.270 -50.536  1.00 32.45           C  
-ATOM  22150  CG  LEU F 368       0.212 -49.782 -50.265  1.00 34.28           C  
-ATOM  22151  CD1 LEU F 368       1.132 -50.514 -51.228  1.00 21.58           C  
-ATOM  22152  CD2 LEU F 368       0.579 -50.121 -48.819  1.00 49.56           C  
-ATOM  22153  N   THR F 369       1.737 -46.261 -52.582  1.00 26.44           N  
-ATOM  22154  CA  THR F 369       1.869 -45.028 -53.356  1.00 26.44           C  
-ATOM  22155  C   THR F 369       0.802 -44.839 -54.433  1.00 26.46           C  
-ATOM  22156  O   THR F 369       0.615 -43.726 -54.925  1.00 32.14           O  
-ATOM  22157  CB  THR F 369       3.252 -44.945 -54.038  1.00 21.86           C  
-ATOM  22158  OG1 THR F 369       3.447 -46.088 -54.881  1.00 25.34           O  
-ATOM  22159  CG2 THR F 369       4.355 -44.896 -52.997  1.00 21.78           C  
-ATOM  22160  N   THR F 370       0.106 -45.909 -54.807  1.00 22.09           N  
-ATOM  22161  CA  THR F 370      -0.945 -45.800 -55.818  1.00 21.98           C  
-ATOM  22162  C   THR F 370      -2.168 -45.085 -55.251  1.00 22.42           C  
-ATOM  22163  O   THR F 370      -3.070 -44.693 -55.988  1.00 22.97           O  
-ATOM  22164  CB  THR F 370      -1.368 -47.176 -56.368  1.00 25.04           C  
-ATOM  22165  OG1 THR F 370      -1.679 -48.058 -55.282  1.00 27.96           O  
-ATOM  22166  CG2 THR F 370      -0.252 -47.780 -57.211  1.00 21.73           C  
-ATOM  22167  N   LYS F 371      -2.192 -44.929 -53.933  1.00 25.62           N  
-ATOM  22168  CA  LYS F 371      -3.202 -44.122 -53.266  1.00 20.94           C  
-ATOM  22169  C   LYS F 371      -2.634 -43.647 -51.937  1.00 25.32           C  
-ATOM  22170  O   LYS F 371      -1.777 -44.307 -51.348  1.00 30.36           O  
-ATOM  22171  CB  LYS F 371      -4.496 -44.912 -53.058  1.00 21.65           C  
-ATOM  22172  CG  LYS F 371      -4.537 -45.717 -51.769  1.00 27.58           C  
-ATOM  22173  CD  LYS F 371      -5.617 -46.788 -51.804  1.00 34.46           C  
-ATOM  22174  CE  LYS F 371      -6.712 -46.520 -50.786  1.00 37.30           C  
-ATOM  22175  NZ  LYS F 371      -7.559 -47.727 -50.580  1.00 51.53           N  
-ATOM  22176  N   ARG F 372      -3.100 -42.496 -51.470  1.00 33.51           N  
-ATOM  22177  CA  ARG F 372      -2.619 -41.954 -50.208  1.00 29.11           C  
-ATOM  22178  C   ARG F 372      -3.134 -42.789 -49.036  1.00 26.67           C  
-ATOM  22179  O   ARG F 372      -4.334 -43.040 -48.917  1.00 25.70           O  
-ATOM  22180  CB  ARG F 372      -3.036 -40.491 -50.055  1.00 26.51           C  
-ATOM  22181  CG  ARG F 372      -2.595 -39.863 -48.747  1.00 30.72           C  
-ATOM  22182  CD  ARG F 372      -2.716 -38.350 -48.781  1.00 34.96           C  
-ATOM  22183  NE  ARG F 372      -1.727 -37.740 -49.665  1.00 30.50           N  
-ATOM  22184  CZ  ARG F 372      -0.473 -37.478 -49.311  1.00 36.36           C  
-ATOM  22185  NH1 ARG F 372      -0.050 -37.778 -48.089  1.00 32.27           N  
-ATOM  22186  NH2 ARG F 372       0.360 -36.918 -50.178  1.00 30.20           N  
-ATOM  22187  N   VAL F 373      -2.216 -43.226 -48.181  1.00 24.10           N  
-ATOM  22188  CA  VAL F 373      -2.563 -44.047 -47.027  1.00 24.19           C  
-ATOM  22189  C   VAL F 373      -2.663 -43.200 -45.757  1.00 21.15           C  
-ATOM  22190  O   VAL F 373      -1.833 -42.323 -45.521  1.00 18.00           O  
-ATOM  22191  CB  VAL F 373      -1.530 -45.178 -46.827  1.00 21.38           C  
-ATOM  22192  CG1 VAL F 373      -1.804 -45.946 -45.538  1.00 21.98           C  
-ATOM  22193  CG2 VAL F 373      -1.542 -46.114 -48.024  1.00 22.43           C  
-ATOM  22194  N   PHE F 374      -3.687 -43.462 -44.946  1.00 24.42           N  
-ATOM  22195  CA  PHE F 374      -3.913 -42.702 -43.718  1.00 27.07           C  
-ATOM  22196  C   PHE F 374      -2.847 -42.989 -42.658  1.00 18.32           C  
-ATOM  22197  O   PHE F 374      -3.069 -43.750 -41.710  1.00 19.61           O  
-ATOM  22198  CB  PHE F 374      -5.306 -42.992 -43.155  1.00 26.75           C  
-ATOM  22199  CG  PHE F 374      -5.769 -41.981 -42.148  1.00 23.78           C  
-ATOM  22200  CD1 PHE F 374      -5.230 -40.705 -42.134  1.00 20.15           C  
-ATOM  22201  CD2 PHE F 374      -6.731 -42.309 -41.209  1.00 25.02           C  
-ATOM  22202  CE1 PHE F 374      -5.649 -39.773 -41.205  1.00 31.10           C  
-ATOM  22203  CE2 PHE F 374      -7.153 -41.383 -40.276  1.00 25.46           C  
-ATOM  22204  CZ  PHE F 374      -6.612 -40.112 -40.274  1.00 29.08           C  
-ATOM  22205  N   TRP F 375      -1.695 -42.351 -42.822  1.00 18.15           N  
-ATOM  22206  CA  TRP F 375      -0.546 -42.594 -41.961  1.00 16.51           C  
-ATOM  22207  C   TRP F 375      -0.798 -42.241 -40.501  1.00 19.77           C  
-ATOM  22208  O   TRP F 375      -0.440 -43.008 -39.605  1.00 25.64           O  
-ATOM  22209  CB  TRP F 375       0.667 -41.815 -42.460  1.00 13.41           C  
-ATOM  22210  CG  TRP F 375       1.758 -41.759 -41.448  1.00 12.01           C  
-ATOM  22211  CD1 TRP F 375       2.135 -40.679 -40.707  1.00 12.79           C  
-ATOM  22212  CD2 TRP F 375       2.603 -42.839 -41.042  1.00 15.20           C  
-ATOM  22213  NE1 TRP F 375       3.172 -41.017 -39.871  1.00 10.88           N  
-ATOM  22214  CE2 TRP F 375       3.476 -42.339 -40.057  1.00 12.68           C  
-ATOM  22215  CE3 TRP F 375       2.708 -44.180 -41.420  1.00 17.14           C  
-ATOM  22216  CZ2 TRP F 375       4.445 -43.132 -39.447  1.00 17.61           C  
-ATOM  22217  CZ3 TRP F 375       3.671 -44.967 -40.811  1.00 17.61           C  
-ATOM  22218  CH2 TRP F 375       4.526 -44.441 -39.836  1.00 16.85           C  
-ATOM  22219  N   LYS F 376      -1.390 -41.075 -40.262  1.00 17.21           N  
-ATOM  22220  CA  LYS F 376      -1.695 -40.651 -38.902  1.00 17.67           C  
-ATOM  22221  C   LYS F 376      -2.600 -41.677 -38.233  1.00 15.49           C  
-ATOM  22222  O   LYS F 376      -2.407 -42.033 -37.075  1.00 14.72           O  
-ATOM  22223  CB  LYS F 376      -2.355 -39.271 -38.893  1.00 23.37           C  
-ATOM  22224  CG  LYS F 376      -2.267 -38.568 -37.546  1.00 37.65           C  
-ATOM  22225  CD  LYS F 376      -3.601 -37.986 -37.109  1.00 29.23           C  
-ATOM  22226  CE  LYS F 376      -4.085 -36.904 -38.061  1.00 47.04           C  
-ATOM  22227  NZ  LYS F 376      -5.407 -36.357 -37.640  1.00 37.42           N  
-ATOM  22228  N   GLY F 377      -3.579 -42.163 -38.986  1.00 17.28           N  
-ATOM  22229  CA  GLY F 377      -4.454 -43.218 -38.518  1.00 14.88           C  
-ATOM  22230  C   GLY F 377      -3.680 -44.471 -38.160  1.00 17.16           C  
-ATOM  22231  O   GLY F 377      -3.930 -45.077 -37.119  1.00 19.04           O  
-ATOM  22232  N   VAL F 378      -2.743 -44.862 -39.023  1.00 16.29           N  
-ATOM  22233  CA  VAL F 378      -1.888 -46.019 -38.751  1.00 18.29           C  
-ATOM  22234  C   VAL F 378      -1.168 -45.867 -37.414  1.00 22.47           C  
-ATOM  22235  O   VAL F 378      -1.328 -46.694 -36.503  1.00 28.89           O  
-ATOM  22236  CB  VAL F 378      -0.836 -46.228 -39.864  1.00 13.88           C  
-ATOM  22237  CG1 VAL F 378       0.149 -47.315 -39.472  1.00 17.80           C  
-ATOM  22238  CG2 VAL F 378      -1.506 -46.564 -41.179  1.00 17.20           C  
-ATOM  22239  N   LEU F 379      -0.389 -44.795 -37.313  1.00 17.72           N  
-ATOM  22240  CA  LEU F 379       0.403 -44.485 -36.132  1.00 19.28           C  
-ATOM  22241  C   LEU F 379      -0.422 -44.463 -34.849  1.00 20.20           C  
-ATOM  22242  O   LEU F 379      -0.107 -45.157 -33.882  1.00 23.42           O  
-ATOM  22243  CB  LEU F 379       1.107 -43.137 -36.339  1.00 19.33           C  
-ATOM  22244  CG  LEU F 379       2.098 -42.701 -35.259  1.00 22.57           C  
-ATOM  22245  CD1 LEU F 379       3.062 -43.827 -34.928  1.00 25.99           C  
-ATOM  22246  CD2 LEU F 379       2.852 -41.464 -35.715  1.00 17.62           C  
-ATOM  22247  N   GLU F 380      -1.483 -43.666 -34.854  1.00 19.20           N  
-ATOM  22248  CA  GLU F 380      -2.337 -43.516 -33.682  1.00 22.78           C  
-ATOM  22249  C   GLU F 380      -3.018 -44.822 -33.295  1.00 25.26           C  
-ATOM  22250  O   GLU F 380      -3.125 -45.136 -32.108  1.00 25.83           O  
-ATOM  22251  CB  GLU F 380      -3.398 -42.432 -33.916  1.00 24.91           C  
-ATOM  22252  CG  GLU F 380      -2.835 -41.024 -34.109  1.00 28.15           C  
-ATOM  22253  CD  GLU F 380      -2.263 -40.419 -32.832  1.00 34.41           C  
-ATOM  22254  OE1 GLU F 380      -2.353 -41.064 -31.764  1.00 34.73           O  
-ATOM  22255  OE2 GLU F 380      -1.728 -39.289 -32.896  1.00 27.09           O  
-ATOM  22256  N   GLU F 381      -3.478 -45.584 -34.285  1.00 20.68           N  
-ATOM  22257  CA  GLU F 381      -4.117 -46.863 -33.988  1.00 20.79           C  
-ATOM  22258  C   GLU F 381      -3.119 -47.844 -33.379  1.00 25.79           C  
-ATOM  22259  O   GLU F 381      -3.473 -48.627 -32.493  1.00 23.73           O  
-ATOM  22260  CB  GLU F 381      -4.749 -47.481 -35.238  1.00 19.77           C  
-ATOM  22261  CG  GLU F 381      -5.680 -48.651 -34.931  1.00 18.30           C  
-ATOM  22262  CD  GLU F 381      -5.821 -49.613 -36.096  1.00 36.61           C  
-ATOM  22263  OE1 GLU F 381      -4.860 -49.739 -36.887  1.00 39.71           O  
-ATOM  22264  OE2 GLU F 381      -6.890 -50.250 -36.219  1.00 35.77           O  
-ATOM  22265  N   LEU F 382      -1.876 -47.811 -33.856  1.00 25.18           N  
-ATOM  22266  CA  LEU F 382      -0.855 -48.705 -33.315  1.00 18.60           C  
-ATOM  22267  C   LEU F 382      -0.475 -48.321 -31.887  1.00 20.62           C  
-ATOM  22268  O   LEU F 382      -0.323 -49.185 -31.025  1.00 24.33           O  
-ATOM  22269  CB  LEU F 382       0.394 -48.720 -34.202  1.00 18.27           C  
-ATOM  22270  CG  LEU F 382       1.520 -49.648 -33.730  1.00 16.76           C  
-ATOM  22271  CD1 LEU F 382       0.976 -51.024 -33.385  1.00 16.23           C  
-ATOM  22272  CD2 LEU F 382       2.606 -49.756 -34.790  1.00 19.97           C  
-ATOM  22273  N   LEU F 383      -0.318 -47.026 -31.641  1.00 21.36           N  
-ATOM  22274  CA  LEU F 383      -0.023 -46.547 -30.294  1.00 17.26           C  
-ATOM  22275  C   LEU F 383      -1.144 -46.938 -29.339  1.00 20.10           C  
-ATOM  22276  O   LEU F 383      -0.899 -47.388 -28.223  1.00 26.24           O  
-ATOM  22277  CB  LEU F 383       0.179 -45.033 -30.301  1.00 16.05           C  
-ATOM  22278  CG  LEU F 383       1.496 -44.566 -30.921  1.00 12.44           C  
-ATOM  22279  CD1 LEU F 383       1.498 -43.063 -31.093  1.00 21.50           C  
-ATOM  22280  CD2 LEU F 383       2.670 -45.004 -30.066  1.00 17.92           C  
-ATOM  22281  N   TRP F 384      -2.373 -46.752 -29.807  1.00 22.05           N  
-ATOM  22282  CA  TRP F 384      -3.587 -47.234 -29.153  1.00 25.20           C  
-ATOM  22283  C   TRP F 384      -3.455 -48.708 -28.747  1.00 24.48           C  
-ATOM  22284  O   TRP F 384      -3.571 -49.067 -27.561  1.00 22.36           O  
-ATOM  22285  CB  TRP F 384      -4.766 -47.020 -30.115  1.00 21.46           C  
-ATOM  22286  CG  TRP F 384      -6.136 -47.094 -29.530  1.00 15.71           C  
-ATOM  22287  CD1 TRP F 384      -6.650 -46.318 -28.535  1.00 17.43           C  
-ATOM  22288  CD2 TRP F 384      -7.194 -47.958 -29.952  1.00 17.54           C  
-ATOM  22289  NE1 TRP F 384      -7.954 -46.668 -28.289  1.00 19.08           N  
-ATOM  22290  CE2 TRP F 384      -8.313 -47.674 -29.149  1.00 21.09           C  
-ATOM  22291  CE3 TRP F 384      -7.299 -48.959 -30.922  1.00 19.81           C  
-ATOM  22292  CZ2 TRP F 384      -9.523 -48.352 -29.285  1.00 28.85           C  
-ATOM  22293  CZ3 TRP F 384      -8.497 -49.629 -31.058  1.00 21.31           C  
-ATOM  22294  CH2 TRP F 384      -9.594 -49.324 -30.245  1.00 22.99           C  
-ATOM  22295  N   PHE F 385      -3.207 -49.548 -29.749  1.00 21.19           N  
-ATOM  22296  CA  PHE F 385      -2.967 -50.970 -29.545  1.00 22.76           C  
-ATOM  22297  C   PHE F 385      -1.981 -51.229 -28.419  1.00 24.89           C  
-ATOM  22298  O   PHE F 385      -2.279 -51.971 -27.487  1.00 27.70           O  
-ATOM  22299  CB  PHE F 385      -2.442 -51.615 -30.830  1.00 22.47           C  
-ATOM  22300  CG  PHE F 385      -3.480 -51.793 -31.891  1.00 28.45           C  
-ATOM  22301  CD1 PHE F 385      -4.829 -51.743 -31.580  1.00 34.69           C  
-ATOM  22302  CD2 PHE F 385      -3.107 -52.020 -33.205  1.00 25.51           C  
-ATOM  22303  CE1 PHE F 385      -5.790 -51.912 -32.562  1.00 30.22           C  
-ATOM  22304  CE2 PHE F 385      -4.064 -52.191 -34.195  1.00 27.39           C  
-ATOM  22305  CZ  PHE F 385      -5.406 -52.138 -33.871  1.00 33.76           C  
-ATOM  22306  N   ILE F 386      -0.810 -50.607 -28.516  1.00 23.33           N  
-ATOM  22307  CA  ILE F 386       0.264 -50.840 -27.557  1.00 22.58           C  
-ATOM  22308  C   ILE F 386      -0.106 -50.404 -26.140  1.00 18.63           C  
-ATOM  22309  O   ILE F 386       0.230 -51.087 -25.172  1.00 21.95           O  
-ATOM  22310  CB  ILE F 386       1.558 -50.128 -28.002  1.00 19.53           C  
-ATOM  22311  CG1 ILE F 386       1.984 -50.650 -29.374  1.00 16.73           C  
-ATOM  22312  CG2 ILE F 386       2.672 -50.353 -26.993  1.00 16.26           C  
-ATOM  22313  CD1 ILE F 386       3.242 -50.026 -29.889  1.00 18.31           C  
-ATOM  22314  N   ARG F 387      -0.800 -49.278 -26.014  1.00 25.93           N  
-ATOM  22315  CA  ARG F 387      -1.300 -48.865 -24.708  1.00 23.91           C  
-ATOM  22316  C   ARG F 387      -2.301 -49.895 -24.198  1.00 28.86           C  
-ATOM  22317  O   ARG F 387      -2.473 -50.069 -22.990  1.00 22.85           O  
-ATOM  22318  CB  ARG F 387      -1.958 -47.486 -24.770  1.00 24.71           C  
-ATOM  22319  CG  ARG F 387      -1.044 -46.359 -25.215  1.00 23.43           C  
-ATOM  22320  CD  ARG F 387      -1.739 -45.014 -25.080  1.00 20.03           C  
-ATOM  22321  NE  ARG F 387      -1.120 -43.988 -25.915  1.00 29.42           N  
-ATOM  22322  CZ  ARG F 387      -1.673 -43.490 -27.017  1.00 31.63           C  
-ATOM  22323  NH1 ARG F 387      -2.863 -43.919 -27.417  1.00 30.43           N  
-ATOM  22324  NH2 ARG F 387      -1.040 -42.557 -27.717  1.00 31.52           N  
-ATOM  22325  N   GLY F 388      -2.953 -50.588 -25.128  1.00 28.94           N  
-ATOM  22326  CA  GLY F 388      -3.936 -51.590 -24.756  1.00 24.88           C  
-ATOM  22327  C   GLY F 388      -5.237 -50.895 -24.431  1.00 29.44           C  
-ATOM  22328  O   GLY F 388      -5.992 -51.313 -23.555  1.00 26.81           O  
-ATOM  22329  N   ASP F 389      -5.479 -49.808 -25.151  1.00 22.57           N  
-ATOM  22330  CA  ASP F 389      -6.672 -49.005 -24.978  1.00 15.55           C  
-ATOM  22331  C   ASP F 389      -7.822 -49.614 -25.771  1.00 26.46           C  
-ATOM  22332  O   ASP F 389      -7.645 -50.025 -26.918  1.00 24.66           O  
-ATOM  22333  CB  ASP F 389      -6.392 -47.575 -25.431  1.00 19.15           C  
-ATOM  22334  CG  ASP F 389      -7.444 -46.595 -24.973  1.00 25.17           C  
-ATOM  22335  OD1 ASP F 389      -8.485 -47.029 -24.433  1.00 23.66           O  
-ATOM  22336  OD2 ASP F 389      -7.223 -45.380 -25.164  1.00 26.21           O  
-ATOM  22337  N   THR F 390      -8.998 -49.681 -25.156  1.00 38.19           N  
-ATOM  22338  CA  THR F 390     -10.174 -50.235 -25.820  1.00 25.73           C  
-ATOM  22339  C   THR F 390     -11.237 -49.160 -26.015  1.00 23.96           C  
-ATOM  22340  O   THR F 390     -12.414 -49.459 -26.220  1.00 22.60           O  
-ATOM  22341  CB  THR F 390     -10.766 -51.409 -25.025  1.00 22.75           C  
-ATOM  22342  OG1 THR F 390     -11.050 -50.987 -23.685  1.00 27.02           O  
-ATOM  22343  CG2 THR F 390      -9.780 -52.556 -24.980  1.00 23.84           C  
-ATOM  22344  N   ASN F 391     -10.804 -47.906 -25.948  1.00 24.73           N  
-ATOM  22345  CA  ASN F 391     -11.690 -46.760 -26.104  1.00 20.30           C  
-ATOM  22346  C   ASN F 391     -11.492 -46.113 -27.469  1.00 21.86           C  
-ATOM  22347  O   ASN F 391     -10.453 -45.510 -27.730  1.00 27.93           O  
-ATOM  22348  CB  ASN F 391     -11.436 -45.745 -24.985  1.00 20.95           C  
-ATOM  22349  CG  ASN F 391     -12.522 -44.692 -24.886  1.00 21.62           C  
-ATOM  22350  OD1 ASN F 391     -13.064 -44.240 -25.891  1.00 22.21           O  
-ATOM  22351  ND2 ASN F 391     -12.850 -44.300 -23.661  1.00 31.39           N  
-ATOM  22352  N   ALA F 392     -12.491 -46.236 -28.337  1.00 20.91           N  
-ATOM  22353  CA  ALA F 392     -12.383 -45.723 -29.699  1.00 25.15           C  
-ATOM  22354  C   ALA F 392     -12.521 -44.203 -29.760  1.00 29.78           C  
-ATOM  22355  O   ALA F 392     -12.137 -43.580 -30.748  1.00 34.08           O  
-ATOM  22356  CB  ALA F 392     -13.424 -46.378 -30.592  1.00 27.56           C  
-ATOM  22357  N   ASN F 393     -13.073 -43.608 -28.707  1.00 24.77           N  
-ATOM  22358  CA  ASN F 393     -13.245 -42.161 -28.671  1.00 27.08           C  
-ATOM  22359  C   ASN F 393     -11.903 -41.454 -28.567  1.00 29.89           C  
-ATOM  22360  O   ASN F 393     -11.758 -40.308 -28.993  1.00 32.84           O  
-ATOM  22361  CB  ASN F 393     -14.151 -41.748 -27.509  1.00 33.94           C  
-ATOM  22362  CG  ASN F 393     -15.553 -42.305 -27.640  1.00 30.65           C  
-ATOM  22363  OD1 ASN F 393     -16.352 -41.827 -28.447  1.00 27.61           O  
-ATOM  22364  ND2 ASN F 393     -15.864 -43.317 -26.839  1.00 33.92           N  
-ATOM  22365  N   HIS F 394     -10.922 -42.149 -28.000  1.00 29.86           N  
-ATOM  22366  CA  HIS F 394      -9.560 -41.634 -27.922  1.00 26.63           C  
-ATOM  22367  C   HIS F 394      -8.949 -41.537 -29.316  1.00 23.99           C  
-ATOM  22368  O   HIS F 394      -8.087 -40.699 -29.576  1.00 24.09           O  
-ATOM  22369  CB  HIS F 394      -8.704 -42.523 -27.021  1.00 21.78           C  
-ATOM  22370  CG  HIS F 394      -9.151 -42.537 -25.592  1.00 21.66           C  
-ATOM  22371  ND1 HIS F 394      -8.591 -43.365 -24.643  1.00 24.43           N  
-ATOM  22372  CD2 HIS F 394     -10.102 -41.820 -24.950  1.00 24.86           C  
-ATOM  22373  CE1 HIS F 394      -9.178 -43.158 -23.479  1.00 17.70           C  
-ATOM  22374  NE2 HIS F 394     -10.099 -42.225 -23.637  1.00 22.19           N  
-ATOM  22375  N   LEU F 395      -9.410 -42.407 -30.207  1.00 24.73           N  
-ATOM  22376  CA  LEU F 395      -8.992 -42.391 -31.601  1.00 26.24           C  
-ATOM  22377  C   LEU F 395      -9.775 -41.339 -32.383  1.00 29.22           C  
-ATOM  22378  O   LEU F 395      -9.222 -40.630 -33.223  1.00 24.66           O  
-ATOM  22379  CB  LEU F 395      -9.188 -43.774 -32.226  1.00 23.35           C  
-ATOM  22380  CG  LEU F 395      -7.952 -44.526 -32.719  1.00 20.26           C  
-ATOM  22381  CD1 LEU F 395      -6.749 -44.270 -31.824  1.00 17.88           C  
-ATOM  22382  CD2 LEU F 395      -8.258 -46.013 -32.791  1.00 22.73           C  
-ATOM  22383  N   SER F 396     -11.068 -41.247 -32.089  1.00 37.06           N  
-ATOM  22384  CA  SER F 396     -11.970 -40.345 -32.789  1.00 33.40           C  
-ATOM  22385  C   SER F 396     -11.638 -38.880 -32.507  1.00 31.08           C  
-ATOM  22386  O   SER F 396     -11.747 -38.032 -33.392  1.00 32.11           O  
-ATOM  22387  CB  SER F 396     -13.420 -40.648 -32.396  1.00 29.60           C  
-ATOM  22388  OG  SER F 396     -14.335 -39.935 -33.211  1.00 42.96           O  
-ATOM  22389  N  AGLU F 397     -11.240 -38.601 -31.269  0.42 32.13           N  
-ATOM  22390  N  BGLU F 397     -11.226 -38.584 -31.279  0.58 33.74           N  
-ATOM  22391  CA AGLU F 397     -10.883 -37.254 -30.838  0.42 35.24           C  
-ATOM  22392  CA BGLU F 397     -10.924 -37.207 -30.899  0.58 32.00           C  
-ATOM  22393  C  AGLU F 397      -9.693 -36.724 -31.629  0.42 36.50           C  
-ATOM  22394  C  BGLU F 397      -9.628 -36.698 -31.531  0.58 40.15           C  
-ATOM  22395  O  AGLU F 397      -9.629 -35.540 -31.959  0.42 35.13           O  
-ATOM  22396  O  BGLU F 397      -9.424 -35.489 -31.644  0.58 35.66           O  
-ATOM  22397  CB AGLU F 397     -10.576 -37.242 -29.334  0.42 29.82           C  
-ATOM  22398  CB BGLU F 397     -10.859 -37.076 -29.376  0.58 29.76           C  
-ATOM  22399  CG AGLU F 397     -10.006 -35.931 -28.803  0.42 31.76           C  
-ATOM  22400  CG BGLU F 397     -12.202 -36.740 -28.747  0.58 28.54           C  
-ATOM  22401  CD AGLU F 397      -8.490 -35.940 -28.721  0.42 28.22           C  
-ATOM  22402  CD BGLU F 397     -12.559 -37.659 -27.599  0.58 27.83           C  
-ATOM  22403  OE1AGLU F 397      -7.882 -34.851 -28.802  0.42 23.01           O  
-ATOM  22404  OE1BGLU F 397     -11.633 -38.209 -26.966  0.58 23.44           O  
-ATOM  22405  OE2AGLU F 397      -7.907 -37.034 -28.571  0.42 25.82           O  
-ATOM  22406  OE2BGLU F 397     -13.769 -37.837 -27.336  0.58 22.42           O  
-ATOM  22407  N   LYS F 398      -8.759 -37.616 -31.945  1.00 33.45           N  
-ATOM  22408  CA  LYS F 398      -7.543 -37.235 -32.656  1.00 25.53           C  
-ATOM  22409  C   LYS F 398      -7.776 -37.161 -34.163  1.00 28.52           C  
-ATOM  22410  O   LYS F 398      -6.836 -36.966 -34.935  1.00 33.84           O  
-ATOM  22411  CB  LYS F 398      -6.408 -38.215 -32.359  1.00 21.56           C  
-ATOM  22412  CG  LYS F 398      -6.052 -38.342 -30.890  1.00 24.16           C  
-ATOM  22413  CD  LYS F 398      -4.712 -39.040 -30.712  1.00 18.34           C  
-ATOM  22414  CE  LYS F 398      -4.599 -39.680 -29.337  1.00 24.41           C  
-ATOM  22415  NZ  LYS F 398      -4.921 -38.728 -28.235  1.00 18.33           N  
-ATOM  22416  N   GLY F 399      -9.027 -37.323 -34.580  1.00 28.50           N  
-ATOM  22417  CA  GLY F 399      -9.376 -37.231 -35.986  1.00 28.53           C  
-ATOM  22418  C   GLY F 399      -9.302 -38.563 -36.704  1.00 32.27           C  
-ATOM  22419  O   GLY F 399      -9.489 -38.636 -37.918  1.00 39.40           O  
-ATOM  22420  N   VAL F 400      -9.025 -39.621 -35.949  1.00 35.18           N  
-ATOM  22421  CA  VAL F 400      -8.956 -40.967 -36.504  1.00 30.09           C  
-ATOM  22422  C   VAL F 400     -10.243 -41.726 -36.209  1.00 28.15           C  
-ATOM  22423  O   VAL F 400     -10.355 -42.389 -35.181  1.00 29.54           O  
-ATOM  22424  CB  VAL F 400      -7.756 -41.750 -35.932  1.00 26.72           C  
-ATOM  22425  CG1 VAL F 400      -7.631 -43.103 -36.607  1.00 28.16           C  
-ATOM  22426  CG2 VAL F 400      -6.472 -40.951 -36.097  1.00 26.20           C  
-ATOM  22427  N   LYS F 401     -11.217 -41.626 -37.108  1.00 30.94           N  
-ATOM  22428  CA  LYS F 401     -12.528 -42.234 -36.876  1.00 39.25           C  
-ATOM  22429  C   LYS F 401     -12.731 -43.518 -37.664  1.00 35.03           C  
-ATOM  22430  O   LYS F 401     -13.801 -43.761 -38.216  1.00 49.37           O  
-ATOM  22431  CB  LYS F 401     -13.639 -41.235 -37.204  1.00 42.81           C  
-ATOM  22432  CG  LYS F 401     -13.276 -40.199 -38.247  1.00 44.12           C  
-ATOM  22433  CD  LYS F 401     -13.978 -38.887 -37.934  1.00 51.62           C  
-ATOM  22434  CE  LYS F 401     -14.232 -38.060 -39.185  1.00 67.14           C  
-ATOM  22435  NZ  LYS F 401     -12.980 -37.553 -39.813  1.00 52.13           N  
-ATOM  22436  N   ILE F 402     -11.695 -44.345 -37.691  1.00 34.96           N  
-ATOM  22437  CA  ILE F 402     -11.705 -45.577 -38.464  1.00 32.34           C  
-ATOM  22438  C   ILE F 402     -12.441 -46.688 -37.730  1.00 39.05           C  
-ATOM  22439  O   ILE F 402     -12.636 -47.775 -38.270  1.00 45.08           O  
-ATOM  22440  CB  ILE F 402     -10.277 -46.045 -38.773  1.00 28.56           C  
-ATOM  22441  CG1 ILE F 402      -9.675 -46.748 -37.554  1.00 36.00           C  
-ATOM  22442  CG2 ILE F 402      -9.420 -44.863 -39.174  1.00 39.07           C  
-ATOM  22443  CD1 ILE F 402      -8.220 -47.111 -37.705  1.00 30.79           C  
-ATOM  22444  N   TRP F 403     -12.849 -46.407 -36.497  1.00 32.02           N  
-ATOM  22445  CA  TRP F 403     -13.487 -47.406 -35.650  1.00 32.15           C  
-ATOM  22446  C   TRP F 403     -14.946 -47.088 -35.357  1.00 36.21           C  
-ATOM  22447  O   TRP F 403     -15.706 -47.967 -34.962  1.00 39.85           O  
-ATOM  22448  CB  TRP F 403     -12.726 -47.537 -34.332  1.00 36.87           C  
-ATOM  22449  CG  TRP F 403     -11.695 -48.604 -34.332  1.00 36.10           C  
-ATOM  22450  CD1 TRP F 403     -10.345 -48.441 -34.419  1.00 39.22           C  
-ATOM  22451  CD2 TRP F 403     -11.926 -50.012 -34.234  1.00 44.88           C  
-ATOM  22452  NE1 TRP F 403      -9.719 -49.663 -34.381  1.00 48.87           N  
-ATOM  22453  CE2 TRP F 403     -10.669 -50.645 -34.268  1.00 54.18           C  
-ATOM  22454  CE3 TRP F 403     -13.075 -50.802 -34.123  1.00 54.51           C  
-ATOM  22455  CZ2 TRP F 403     -10.526 -52.027 -34.194  1.00 55.88           C  
-ATOM  22456  CZ3 TRP F 403     -12.931 -52.177 -34.050  1.00 62.52           C  
-ATOM  22457  CH2 TRP F 403     -11.665 -52.774 -34.085  1.00 60.73           C  
-ATOM  22458  N   ASP F 404     -15.324 -45.830 -35.557  1.00 48.58           N  
-ATOM  22459  CA  ASP F 404     -16.619 -45.320 -35.110  1.00 57.53           C  
-ATOM  22460  C   ASP F 404     -17.819 -46.151 -35.570  1.00 51.02           C  
-ATOM  22461  O   ASP F 404     -18.686 -46.493 -34.762  1.00 39.13           O  
-ATOM  22462  CB  ASP F 404     -16.791 -43.869 -35.569  1.00 55.92           C  
-ATOM  22463  CG  ASP F 404     -15.972 -42.895 -34.737  1.00 67.10           C  
-ATOM  22464  OD1 ASP F 404     -15.423 -43.308 -33.691  1.00 62.02           O  
-ATOM  22465  OD2 ASP F 404     -15.891 -41.710 -35.121  1.00 65.33           O  
-ATOM  22466  N   LYS F 405     -17.859 -46.489 -36.856  1.00 47.62           N  
-ATOM  22467  CA  LYS F 405     -18.988 -47.224 -37.423  1.00 39.29           C  
-ATOM  22468  C   LYS F 405     -19.160 -48.617 -36.813  1.00 35.35           C  
-ATOM  22469  O   LYS F 405     -20.173 -49.273 -37.042  1.00 33.31           O  
-ATOM  22470  CB  LYS F 405     -18.835 -47.338 -38.942  1.00 37.50           C  
-ATOM  22471  CG  LYS F 405     -18.813 -46.006 -39.666  1.00 42.05           C  
-ATOM  22472  CD  LYS F 405     -18.737 -46.202 -41.168  1.00 44.24           C  
-ATOM  22473  CE  LYS F 405     -18.638 -44.872 -41.886  1.00 43.92           C  
-ATOM  22474  NZ  LYS F 405     -18.613 -45.049 -43.363  1.00 41.52           N  
-ATOM  22475  N   ASN F 406     -18.174 -49.062 -36.037  1.00 37.09           N  
-ATOM  22476  CA  ASN F 406     -18.234 -50.372 -35.393  1.00 33.46           C  
-ATOM  22477  C   ASN F 406     -18.390 -50.270 -33.879  1.00 29.20           C  
-ATOM  22478  O   ASN F 406     -18.394 -51.280 -33.179  1.00 32.23           O  
-ATOM  22479  CB  ASN F 406     -16.985 -51.188 -35.735  1.00 31.83           C  
-ATOM  22480  CG  ASN F 406     -16.914 -51.547 -37.207  1.00 43.84           C  
-ATOM  22481  OD1 ASN F 406     -16.054 -51.056 -37.935  1.00 56.29           O  
-ATOM  22482  ND2 ASN F 406     -17.824 -52.405 -37.653  1.00 40.95           N  
-ATOM  22483  N   VAL F 407     -18.515 -49.046 -33.375  1.00 30.83           N  
-ATOM  22484  CA  VAL F 407     -18.718 -48.833 -31.942  1.00 30.97           C  
-ATOM  22485  C   VAL F 407     -19.923 -47.936 -31.682  1.00 35.38           C  
-ATOM  22486  O   VAL F 407     -20.048 -47.332 -30.615  1.00 28.21           O  
-ATOM  22487  CB  VAL F 407     -17.479 -48.213 -31.269  1.00 31.26           C  
-ATOM  22488  CG1 VAL F 407     -16.305 -49.177 -31.335  1.00 28.49           C  
-ATOM  22489  CG2 VAL F 407     -17.130 -46.883 -31.916  1.00 36.74           C  
-ATOM  22490  N   THR F 408     -20.808 -47.855 -32.670  1.00 46.07           N  
-ATOM  22491  CA  THR F 408     -22.068 -47.142 -32.513  1.00 35.57           C  
-ATOM  22492  C   THR F 408     -23.061 -47.985 -31.720  1.00 43.17           C  
-ATOM  22493  O   THR F 408     -22.922 -49.209 -31.634  1.00 41.94           O  
-ATOM  22494  CB  THR F 408     -22.695 -46.777 -33.875  1.00 30.82           C  
-ATOM  22495  OG1 THR F 408     -22.910 -47.965 -34.649  1.00 31.32           O  
-ATOM  22496  CG2 THR F 408     -21.784 -45.844 -34.646  1.00 30.64           C  
-ATOM  22497  N   ARG F 409     -24.054 -47.319 -31.138  1.00 47.21           N  
-ATOM  22498  CA  ARG F 409     -25.100 -47.988 -30.371  1.00 45.67           C  
-ATOM  22499  C   ARG F 409     -25.781 -49.081 -31.190  1.00 47.76           C  
-ATOM  22500  O   ARG F 409     -25.997 -50.189 -30.701  1.00 46.34           O  
-ATOM  22501  CB  ARG F 409     -26.132 -46.965 -29.886  1.00 33.80           C  
-ATOM  22502  CG  ARG F 409     -27.319 -47.553 -29.151  1.00 32.00           C  
-ATOM  22503  CD  ARG F 409     -27.087 -47.606 -27.650  1.00 37.53           C  
-ATOM  22504  NE  ARG F 409     -26.426 -48.836 -27.225  1.00 52.51           N  
-ATOM  22505  CZ  ARG F 409     -25.155 -48.915 -26.846  1.00 44.87           C  
-ATOM  22506  NH1 ARG F 409     -24.392 -47.830 -26.834  1.00 43.20           N  
-ATOM  22507  NH2 ARG F 409     -24.647 -50.083 -26.473  1.00 33.54           N  
-ATOM  22508  N   GLU F 410     -26.099 -48.764 -32.441  1.00 39.15           N  
-ATOM  22509  CA  GLU F 410     -26.788 -49.698 -33.321  1.00 42.24           C  
-ATOM  22510  C   GLU F 410     -25.970 -50.963 -33.564  1.00 47.02           C  
-ATOM  22511  O   GLU F 410     -26.492 -52.076 -33.472  1.00 47.85           O  
-ATOM  22512  CB  GLU F 410     -27.118 -49.020 -34.653  1.00 57.39           C  
-ATOM  22513  CG  GLU F 410     -28.068 -49.814 -35.538  1.00 67.40           C  
-ATOM  22514  CD  GLU F 410     -28.446 -49.064 -36.802  1.00 68.49           C  
-ATOM  22515  OE1 GLU F 410     -29.647 -48.771 -36.990  1.00 74.49           O  
-ATOM  22516  OE2 GLU F 410     -27.537 -48.769 -37.607  1.00 47.33           O  
-ATOM  22517  N   PHE F 411     -24.688 -50.787 -33.868  1.00 49.38           N  
-ATOM  22518  CA  PHE F 411     -23.814 -51.919 -34.161  1.00 47.15           C  
-ATOM  22519  C   PHE F 411     -23.567 -52.753 -32.911  1.00 46.70           C  
-ATOM  22520  O   PHE F 411     -23.580 -53.985 -32.967  1.00 48.41           O  
-ATOM  22521  CB  PHE F 411     -22.480 -51.445 -34.745  1.00 35.22           C  
-ATOM  22522  CG  PHE F 411     -21.680 -52.543 -35.392  1.00 35.47           C  
-ATOM  22523  CD1 PHE F 411     -20.828 -53.338 -34.642  1.00 35.26           C  
-ATOM  22524  CD2 PHE F 411     -21.787 -52.782 -36.752  1.00 50.39           C  
-ATOM  22525  CE1 PHE F 411     -20.095 -54.351 -35.238  1.00 41.36           C  
-ATOM  22526  CE2 PHE F 411     -21.056 -53.792 -37.355  1.00 48.61           C  
-ATOM  22527  CZ  PHE F 411     -20.209 -54.577 -36.597  1.00 42.30           C  
-ATOM  22528  N   LEU F 412     -23.333 -52.077 -31.791  1.00 39.17           N  
-ATOM  22529  CA  LEU F 412     -23.125 -52.756 -30.519  1.00 36.95           C  
-ATOM  22530  C   LEU F 412     -24.351 -53.572 -30.139  1.00 40.17           C  
-ATOM  22531  O   LEU F 412     -24.234 -54.659 -29.570  1.00 38.65           O  
-ATOM  22532  CB  LEU F 412     -22.794 -51.749 -29.416  1.00 36.38           C  
-ATOM  22533  CG  LEU F 412     -21.396 -51.128 -29.472  1.00 34.54           C  
-ATOM  22534  CD1 LEU F 412     -21.268 -50.017 -28.447  1.00 37.81           C  
-ATOM  22535  CD2 LEU F 412     -20.328 -52.189 -29.255  1.00 38.81           C  
-ATOM  22536  N   ASP F 413     -25.526 -53.041 -30.459  1.00 38.96           N  
-ATOM  22537  CA  ASP F 413     -26.770 -53.750 -30.204  1.00 36.75           C  
-ATOM  22538  C   ASP F 413     -26.931 -54.920 -31.172  1.00 40.45           C  
-ATOM  22539  O   ASP F 413     -27.516 -55.945 -30.823  1.00 41.94           O  
-ATOM  22540  CB  ASP F 413     -27.965 -52.798 -30.302  1.00 43.70           C  
-ATOM  22541  CG  ASP F 413     -27.971 -51.759 -29.197  1.00 40.21           C  
-ATOM  22542  OD1 ASP F 413     -27.178 -51.904 -28.244  1.00 35.85           O  
-ATOM  22543  OD2 ASP F 413     -28.769 -50.801 -29.279  1.00 54.88           O  
-ATOM  22544  N   SER F 414     -26.410 -54.765 -32.386  1.00 43.79           N  
-ATOM  22545  CA  SER F 414     -26.433 -55.848 -33.365  1.00 44.07           C  
-ATOM  22546  C   SER F 414     -25.491 -56.968 -32.931  1.00 49.28           C  
-ATOM  22547  O   SER F 414     -25.668 -58.127 -33.313  1.00 48.96           O  
-ATOM  22548  CB  SER F 414     -26.050 -55.335 -34.757  1.00 43.38           C  
-ATOM  22549  OG  SER F 414     -24.663 -55.058 -34.846  1.00 41.74           O  
-ATOM  22550  N   ARG F 415     -24.493 -56.609 -32.129  1.00 42.29           N  
-ATOM  22551  CA  ARG F 415     -23.543 -57.573 -31.585  1.00 41.78           C  
-ATOM  22552  C   ARG F 415     -24.011 -58.133 -30.242  1.00 40.47           C  
-ATOM  22553  O   ARG F 415     -23.235 -58.763 -29.521  1.00 40.49           O  
-ATOM  22554  CB  ARG F 415     -22.163 -56.929 -31.426  1.00 34.14           C  
-ATOM  22555  CG  ARG F 415     -21.389 -56.766 -32.725  1.00 41.44           C  
-ATOM  22556  CD  ARG F 415     -20.889 -58.106 -33.247  1.00 46.55           C  
-ATOM  22557  NE  ARG F 415     -19.886 -58.703 -32.368  1.00 41.32           N  
-ATOM  22558  CZ  ARG F 415     -19.386 -59.925 -32.526  1.00 43.58           C  
-ATOM  22559  NH1 ARG F 415     -18.476 -60.388 -31.679  1.00 42.45           N  
-ATOM  22560  NH2 ARG F 415     -19.797 -60.687 -33.529  1.00 43.81           N  
-ATOM  22561  N   ASN F 416     -25.282 -57.901 -29.923  1.00 39.01           N  
-ATOM  22562  CA  ASN F 416     -25.863 -58.297 -28.641  1.00 37.93           C  
-ATOM  22563  C   ASN F 416     -25.074 -57.751 -27.456  1.00 32.68           C  
-ATOM  22564  O   ASN F 416     -24.839 -58.455 -26.474  1.00 29.68           O  
-ATOM  22565  CB  ASN F 416     -25.967 -59.821 -28.542  1.00 37.48           C  
-ATOM  22566  CG  ASN F 416     -26.985 -60.398 -29.502  1.00 38.97           C  
-ATOM  22567  OD1 ASN F 416     -26.644 -60.823 -30.605  1.00 47.52           O  
-ATOM  22568  ND2 ASN F 416     -28.245 -60.418 -29.087  1.00 35.14           N  
-ATOM  22569  N   LEU F 417     -24.666 -56.492 -27.561  1.00 27.91           N  
-ATOM  22570  CA  LEU F 417     -23.938 -55.826 -26.488  1.00 30.27           C  
-ATOM  22571  C   LEU F 417     -24.569 -54.481 -26.134  1.00 40.73           C  
-ATOM  22572  O   LEU F 417     -23.945 -53.435 -26.321  1.00 36.11           O  
-ATOM  22573  CB  LEU F 417     -22.474 -55.620 -26.884  1.00 32.61           C  
-ATOM  22574  CG  LEU F 417     -21.615 -56.864 -27.108  1.00 32.07           C  
-ATOM  22575  CD1 LEU F 417     -20.386 -56.522 -27.933  1.00 26.23           C  
-ATOM  22576  CD2 LEU F 417     -21.210 -57.474 -25.776  1.00 30.42           C  
-ATOM  22577  N   PRO F 418     -25.808 -54.500 -25.610  1.00 40.49           N  
-ATOM  22578  CA  PRO F 418     -26.488 -53.241 -25.296  1.00 30.86           C  
-ATOM  22579  C   PRO F 418     -25.913 -52.569 -24.054  1.00 30.17           C  
-ATOM  22580  O   PRO F 418     -26.244 -51.422 -23.768  1.00 35.81           O  
-ATOM  22581  CB  PRO F 418     -27.932 -53.681 -25.063  1.00 25.43           C  
-ATOM  22582  CG  PRO F 418     -27.801 -55.052 -24.519  1.00 20.31           C  
-ATOM  22583  CD  PRO F 418     -26.622 -55.669 -25.227  1.00 29.54           C  
-ATOM  22584  N   HIS F 419     -25.058 -53.285 -23.332  1.00 30.48           N  
-ATOM  22585  CA  HIS F 419     -24.466 -52.776 -22.103  1.00 32.28           C  
-ATOM  22586  C   HIS F 419     -23.102 -52.136 -22.352  1.00 37.40           C  
-ATOM  22587  O   HIS F 419     -22.366 -51.834 -21.411  1.00 36.03           O  
-ATOM  22588  CB  HIS F 419     -24.336 -53.903 -21.078  1.00 36.60           C  
-ATOM  22589  CG  HIS F 419     -23.589 -55.096 -21.587  1.00 37.79           C  
-ATOM  22590  ND1 HIS F 419     -24.215 -56.159 -22.203  1.00 34.65           N  
-ATOM  22591  CD2 HIS F 419     -22.268 -55.392 -21.579  1.00 33.30           C  
-ATOM  22592  CE1 HIS F 419     -23.313 -57.059 -22.549  1.00 36.24           C  
-ATOM  22593  NE2 HIS F 419     -22.123 -56.618 -22.181  1.00 37.29           N  
-ATOM  22594  N   ARG F 420     -22.770 -51.932 -23.623  1.00 40.46           N  
-ATOM  22595  CA  ARG F 420     -21.501 -51.314 -23.994  1.00 39.28           C  
-ATOM  22596  C   ARG F 420     -21.671 -49.829 -24.291  1.00 38.12           C  
-ATOM  22597  O   ARG F 420     -22.569 -49.436 -25.038  1.00 34.28           O  
-ATOM  22598  CB  ARG F 420     -20.896 -52.016 -25.210  1.00 31.35           C  
-ATOM  22599  CG  ARG F 420     -20.262 -53.365 -24.910  1.00 39.76           C  
-ATOM  22600  CD  ARG F 420     -18.812 -53.220 -24.468  1.00 33.55           C  
-ATOM  22601  NE  ARG F 420     -18.122 -54.506 -24.468  1.00 34.26           N  
-ATOM  22602  CZ  ARG F 420     -17.979 -55.280 -23.397  1.00 33.61           C  
-ATOM  22603  NH1 ARG F 420     -17.339 -56.438 -23.495  1.00 33.39           N  
-ATOM  22604  NH2 ARG F 420     -18.473 -54.896 -22.228  1.00 28.97           N  
-ATOM  22605  N   GLU F 421     -20.809 -49.007 -23.698  1.00 42.65           N  
-ATOM  22606  CA  GLU F 421     -20.760 -47.585 -24.023  1.00 35.35           C  
-ATOM  22607  C   GLU F 421     -20.398 -47.408 -25.485  1.00 32.83           C  
-ATOM  22608  O   GLU F 421     -19.727 -48.259 -26.069  1.00 37.80           O  
-ATOM  22609  CB  GLU F 421     -19.738 -46.848 -23.158  1.00 30.00           C  
-ATOM  22610  CG  GLU F 421     -20.291 -46.253 -21.879  1.00 33.00           C  
-ATOM  22611  CD  GLU F 421     -19.363 -45.208 -21.290  1.00 40.22           C  
-ATOM  22612  OE1 GLU F 421     -19.068 -44.213 -21.989  1.00 31.81           O  
-ATOM  22613  OE2 GLU F 421     -18.922 -45.383 -20.135  1.00 45.56           O  
-ATOM  22614  N   VAL F 422     -20.842 -46.305 -26.077  1.00 32.07           N  
-ATOM  22615  CA  VAL F 422     -20.406 -45.957 -27.419  1.00 23.80           C  
-ATOM  22616  C   VAL F 422     -18.907 -45.695 -27.388  1.00 25.10           C  
-ATOM  22617  O   VAL F 422     -18.436 -44.834 -26.645  1.00 21.88           O  
-ATOM  22618  CB  VAL F 422     -21.141 -44.724 -27.968  1.00 23.06           C  
-ATOM  22619  CG1 VAL F 422     -20.522 -44.286 -29.286  1.00 33.66           C  
-ATOM  22620  CG2 VAL F 422     -22.619 -45.024 -28.143  1.00 27.65           C  
-ATOM  22621  N   GLY F 423     -18.162 -46.459 -28.180  1.00 30.70           N  
-ATOM  22622  CA  GLY F 423     -16.719 -46.326 -28.239  1.00 30.69           C  
-ATOM  22623  C   GLY F 423     -15.990 -47.557 -27.735  1.00 25.22           C  
-ATOM  22624  O   GLY F 423     -14.872 -47.842 -28.158  1.00 28.44           O  
-ATOM  22625  N   ASP F 424     -16.625 -48.293 -26.829  1.00 21.86           N  
-ATOM  22626  CA  ASP F 424     -16.002 -49.460 -26.219  1.00 18.53           C  
-ATOM  22627  C   ASP F 424     -15.942 -50.634 -27.190  1.00 26.35           C  
-ATOM  22628  O   ASP F 424     -16.967 -51.243 -27.502  1.00 34.44           O  
-ATOM  22629  CB  ASP F 424     -16.764 -49.859 -24.954  1.00 23.13           C  
-ATOM  22630  CG  ASP F 424     -15.922 -50.684 -23.998  1.00 32.10           C  
-ATOM  22631  OD1 ASP F 424     -15.077 -51.476 -24.466  1.00 33.33           O  
-ATOM  22632  OD2 ASP F 424     -16.104 -50.536 -22.772  1.00 32.24           O  
-ATOM  22633  N   ILE F 425     -14.736 -50.958 -27.654  1.00 23.83           N  
-ATOM  22634  CA  ILE F 425     -14.552 -52.054 -28.603  1.00 31.92           C  
-ATOM  22635  C   ILE F 425     -14.489 -53.409 -27.902  1.00 28.62           C  
-ATOM  22636  O   ILE F 425     -14.194 -54.431 -28.526  1.00 29.99           O  
-ATOM  22637  CB  ILE F 425     -13.269 -51.874 -29.444  1.00 24.53           C  
-ATOM  22638  CG1 ILE F 425     -12.025 -52.178 -28.607  1.00 28.18           C  
-ATOM  22639  CG2 ILE F 425     -13.201 -50.471 -30.018  1.00 25.02           C  
-ATOM  22640  CD1 ILE F 425     -10.813 -52.511 -29.442  1.00 24.03           C  
-ATOM  22641  N   GLY F 426     -14.775 -53.415 -26.605  1.00 23.87           N  
-ATOM  22642  CA  GLY F 426     -14.697 -54.631 -25.819  1.00 31.67           C  
-ATOM  22643  C   GLY F 426     -13.259 -55.079 -25.645  1.00 31.37           C  
-ATOM  22644  O   GLY F 426     -12.334 -54.322 -25.931  1.00 29.30           O  
-ATOM  22645  N   PRO F 427     -13.061 -56.323 -25.189  1.00 30.77           N  
-ATOM  22646  CA  PRO F 427     -11.719 -56.858 -24.943  1.00 29.17           C  
-ATOM  22647  C   PRO F 427     -11.022 -57.325 -26.220  1.00 29.98           C  
-ATOM  22648  O   PRO F 427     -10.661 -58.499 -26.327  1.00 29.86           O  
-ATOM  22649  CB  PRO F 427     -11.980 -58.037 -23.999  1.00 28.79           C  
-ATOM  22650  CG  PRO F 427     -13.444 -58.379 -24.151  1.00 29.41           C  
-ATOM  22651  CD  PRO F 427     -14.108 -57.342 -25.008  1.00 27.29           C  
-ATOM  22652  N   GLY F 428     -10.831 -56.410 -27.168  1.00 26.37           N  
-ATOM  22653  CA  GLY F 428     -10.197 -56.736 -28.433  1.00 19.08           C  
-ATOM  22654  C   GLY F 428      -8.767 -56.243 -28.566  1.00 22.98           C  
-ATOM  22655  O   GLY F 428      -8.252 -55.563 -27.679  1.00 32.21           O  
-ATOM  22656  N   TYR F 429      -8.148 -56.602 -29.691  1.00 27.97           N  
-ATOM  22657  CA  TYR F 429      -6.765 -56.258 -30.060  1.00 26.79           C  
-ATOM  22658  C   TYR F 429      -5.813 -55.930 -28.905  1.00 27.76           C  
-ATOM  22659  O   TYR F 429      -5.283 -56.831 -28.256  1.00 28.74           O  
-ATOM  22660  CB  TYR F 429      -6.774 -55.091 -31.051  1.00 23.70           C  
-ATOM  22661  CG  TYR F 429      -7.347 -55.451 -32.407  1.00 31.52           C  
-ATOM  22662  CD1 TYR F 429      -6.729 -56.395 -33.216  1.00 34.19           C  
-ATOM  22663  CD2 TYR F 429      -8.502 -54.843 -32.879  1.00 42.55           C  
-ATOM  22664  CE1 TYR F 429      -7.248 -56.728 -34.456  1.00 37.37           C  
-ATOM  22665  CE2 TYR F 429      -9.029 -55.167 -34.119  1.00 42.87           C  
-ATOM  22666  CZ  TYR F 429      -8.398 -56.109 -34.904  1.00 41.13           C  
-ATOM  22667  OH  TYR F 429      -8.920 -56.435 -36.136  1.00 37.42           O  
-ATOM  22668  N   GLY F 430      -5.598 -54.640 -28.661  1.00 30.16           N  
-ATOM  22669  CA  GLY F 430      -4.666 -54.188 -27.638  1.00 29.66           C  
-ATOM  22670  C   GLY F 430      -4.852 -54.812 -26.266  1.00 33.44           C  
-ATOM  22671  O   GLY F 430      -3.878 -55.154 -25.585  1.00 38.14           O  
-ATOM  22672  N   PHE F 431      -6.108 -54.958 -25.857  1.00 28.60           N  
-ATOM  22673  CA  PHE F 431      -6.420 -55.539 -24.560  1.00 28.41           C  
-ATOM  22674  C   PHE F 431      -5.957 -56.984 -24.470  1.00 31.33           C  
-ATOM  22675  O   PHE F 431      -5.562 -57.441 -23.400  1.00 31.54           O  
-ATOM  22676  CB  PHE F 431      -7.916 -55.469 -24.267  1.00 22.89           C  
-ATOM  22677  CG  PHE F 431      -8.302 -56.129 -22.974  1.00 24.57           C  
-ATOM  22678  CD1 PHE F 431      -8.164 -55.461 -21.770  1.00 25.95           C  
-ATOM  22679  CD2 PHE F 431      -8.780 -57.426 -22.959  1.00 22.82           C  
-ATOM  22680  CE1 PHE F 431      -8.509 -56.072 -20.578  1.00 23.74           C  
-ATOM  22681  CE2 PHE F 431      -9.128 -58.041 -21.772  1.00 22.02           C  
-ATOM  22682  CZ  PHE F 431      -8.992 -57.363 -20.580  1.00 18.11           C  
-ATOM  22683  N   GLN F 432      -6.026 -57.709 -25.581  1.00 25.71           N  
-ATOM  22684  CA  GLN F 432      -5.534 -59.078 -25.594  1.00 27.86           C  
-ATOM  22685  C   GLN F 432      -4.012 -59.060 -25.619  1.00 25.36           C  
-ATOM  22686  O   GLN F 432      -3.364 -59.836 -24.916  1.00 31.42           O  
-ATOM  22687  CB  GLN F 432      -6.110 -59.854 -26.783  1.00 25.04           C  
-ATOM  22688  CG  GLN F 432      -7.592 -60.178 -26.630  1.00 23.96           C  
-ATOM  22689  CD  GLN F 432      -7.889 -60.953 -25.349  1.00 35.80           C  
-ATOM  22690  OE1 GLN F 432      -7.154 -61.869 -24.983  1.00 37.90           O  
-ATOM  22691  NE2 GLN F 432      -8.967 -60.585 -24.664  1.00 34.35           N  
-ATOM  22692  N   TRP F 433      -3.464 -58.152 -26.425  1.00 21.11           N  
-ATOM  22693  CA  TRP F 433      -2.024 -57.910 -26.519  1.00 23.35           C  
-ATOM  22694  C   TRP F 433      -1.353 -57.778 -25.156  1.00 25.39           C  
-ATOM  22695  O   TRP F 433      -0.398 -58.493 -24.851  1.00 24.12           O  
-ATOM  22696  CB  TRP F 433      -1.742 -56.629 -27.314  1.00 24.52           C  
-ATOM  22697  CG  TRP F 433      -1.744 -56.763 -28.800  1.00 27.61           C  
-ATOM  22698  CD1 TRP F 433      -2.318 -57.754 -29.538  1.00 33.01           C  
-ATOM  22699  CD2 TRP F 433      -1.130 -55.871 -29.734  1.00 26.19           C  
-ATOM  22700  NE1 TRP F 433      -2.105 -57.533 -30.875  1.00 34.34           N  
-ATOM  22701  CE2 TRP F 433      -1.376 -56.382 -31.023  1.00 27.98           C  
-ATOM  22702  CE3 TRP F 433      -0.396 -54.687 -29.607  1.00 24.87           C  
-ATOM  22703  CZ2 TRP F 433      -0.915 -55.752 -32.176  1.00 35.00           C  
-ATOM  22704  CZ3 TRP F 433       0.061 -54.064 -30.750  1.00 30.56           C  
-ATOM  22705  CH2 TRP F 433      -0.199 -54.595 -32.018  1.00 31.76           C  
-ATOM  22706  N   ARG F 434      -1.859 -56.856 -24.342  1.00 27.03           N  
-ATOM  22707  CA  ARG F 434      -1.207 -56.521 -23.083  1.00 23.93           C  
-ATOM  22708  C   ARG F 434      -1.779 -57.295 -21.897  1.00 28.86           C  
-ATOM  22709  O   ARG F 434      -1.082 -57.523 -20.907  1.00 27.65           O  
-ATOM  22710  CB  ARG F 434      -1.308 -55.014 -22.825  1.00 24.46           C  
-ATOM  22711  CG  ARG F 434      -0.869 -54.134 -23.993  1.00 21.03           C  
-ATOM  22712  CD  ARG F 434       0.490 -54.543 -24.539  1.00 18.75           C  
-ATOM  22713  NE  ARG F 434       1.517 -54.578 -23.503  1.00 30.89           N  
-ATOM  22714  CZ  ARG F 434       2.334 -53.568 -23.218  1.00 29.80           C  
-ATOM  22715  NH1 ARG F 434       3.240 -53.698 -22.259  1.00 20.60           N  
-ATOM  22716  NH2 ARG F 434       2.250 -52.429 -23.892  1.00 33.54           N  
-ATOM  22717  N   HIS F 435      -3.044 -57.694 -21.999  1.00 27.57           N  
-ATOM  22718  CA  HIS F 435      -3.707 -58.398 -20.906  1.00 32.46           C  
-ATOM  22719  C   HIS F 435      -4.524 -59.591 -21.382  1.00 22.52           C  
-ATOM  22720  O   HIS F 435      -5.706 -59.682 -21.070  1.00 29.91           O  
-ATOM  22721  CB  HIS F 435      -4.632 -57.452 -20.135  1.00 32.03           C  
-ATOM  22722  CG  HIS F 435      -4.051 -56.095 -19.895  1.00 32.66           C  
-ATOM  22723  ND1 HIS F 435      -3.075 -55.861 -18.949  1.00 31.91           N  
-ATOM  22724  CD2 HIS F 435      -4.309 -54.900 -20.474  1.00 28.44           C  
-ATOM  22725  CE1 HIS F 435      -2.756 -54.580 -18.959  1.00 40.73           C  
-ATOM  22726  NE2 HIS F 435      -3.490 -53.973 -19.873  1.00 33.37           N  
-ATOM  22727  N   PHE F 436      -3.905 -60.503 -22.125  1.00 20.94           N  
-ATOM  22728  CA  PHE F 436      -4.592 -61.716 -22.571  1.00 22.15           C  
-ATOM  22729  C   PHE F 436      -5.204 -62.504 -21.408  1.00 21.76           C  
-ATOM  22730  O   PHE F 436      -4.560 -62.733 -20.385  1.00 18.35           O  
-ATOM  22731  CB  PHE F 436      -3.631 -62.621 -23.344  1.00 18.81           C  
-ATOM  22732  CG  PHE F 436      -4.307 -63.765 -24.049  1.00 19.11           C  
-ATOM  22733  CD1 PHE F 436      -4.582 -64.948 -23.380  1.00 18.33           C  
-ATOM  22734  CD2 PHE F 436      -4.660 -63.660 -25.384  1.00 22.86           C  
-ATOM  22735  CE1 PHE F 436      -5.208 -65.998 -24.027  1.00 23.30           C  
-ATOM  22736  CE2 PHE F 436      -5.282 -64.708 -26.036  1.00 25.44           C  
-ATOM  22737  CZ  PHE F 436      -5.556 -65.878 -25.357  1.00 23.83           C  
-ATOM  22738  N   GLY F 437      -6.458 -62.914 -21.576  1.00 27.45           N  
-ATOM  22739  CA  GLY F 437      -7.126 -63.772 -20.613  1.00 25.13           C  
-ATOM  22740  C   GLY F 437      -7.785 -63.057 -19.448  1.00 27.74           C  
-ATOM  22741  O   GLY F 437      -8.536 -63.667 -18.686  1.00 23.09           O  
-ATOM  22742  N   ALA F 438      -7.507 -61.765 -19.307  1.00 29.87           N  
-ATOM  22743  CA  ALA F 438      -8.031 -60.989 -18.189  1.00 22.48           C  
-ATOM  22744  C   ALA F 438      -9.528 -60.749 -18.332  1.00 23.01           C  
-ATOM  22745  O   ALA F 438     -10.049 -60.656 -19.444  1.00 20.83           O  
-ATOM  22746  CB  ALA F 438      -7.292 -59.666 -18.072  1.00 21.33           C  
-ATOM  22747  N   ALA F 439     -10.214 -60.657 -17.196  1.00 20.66           N  
-ATOM  22748  CA  ALA F 439     -11.643 -60.373 -17.180  1.00 20.93           C  
-ATOM  22749  C   ALA F 439     -11.894 -58.918 -17.559  1.00 29.58           C  
-ATOM  22750  O   ALA F 439     -11.345 -58.007 -16.941  1.00 36.13           O  
-ATOM  22751  CB  ALA F 439     -12.228 -60.677 -15.812  1.00 35.69           C  
-ATOM  22752  N   TYR F 440     -12.724 -58.705 -18.576  1.00 26.02           N  
-ATOM  22753  CA  TYR F 440     -12.982 -57.362 -19.084  1.00 21.71           C  
-ATOM  22754  C   TYR F 440     -14.240 -56.747 -18.475  1.00 26.92           C  
-ATOM  22755  O   TYR F 440     -15.292 -57.385 -18.420  1.00 25.10           O  
-ATOM  22756  CB  TYR F 440     -13.100 -57.387 -20.610  1.00 26.93           C  
-ATOM  22757  CG  TYR F 440     -13.183 -56.014 -21.243  1.00 27.04           C  
-ATOM  22758  CD1 TYR F 440     -12.040 -55.254 -21.445  1.00 31.53           C  
-ATOM  22759  CD2 TYR F 440     -14.402 -55.482 -21.640  1.00 27.16           C  
-ATOM  22760  CE1 TYR F 440     -12.108 -54.000 -22.021  1.00 28.28           C  
-ATOM  22761  CE2 TYR F 440     -14.480 -54.228 -22.218  1.00 26.71           C  
-ATOM  22762  CZ  TYR F 440     -13.330 -53.493 -22.406  1.00 28.60           C  
-ATOM  22763  OH  TYR F 440     -13.401 -52.245 -22.978  1.00 28.32           O  
-ATOM  22764  N   LYS F 441     -14.119 -55.501 -18.022  1.00 29.36           N  
-ATOM  22765  CA  LYS F 441     -15.255 -54.757 -17.487  1.00 24.60           C  
-ATOM  22766  C   LYS F 441     -15.732 -53.723 -18.503  1.00 29.12           C  
-ATOM  22767  O   LYS F 441     -16.718 -53.942 -19.208  1.00 34.71           O  
-ATOM  22768  CB  LYS F 441     -14.889 -54.078 -16.164  1.00 21.25           C  
-ATOM  22769  CG  LYS F 441     -15.146 -54.925 -14.919  1.00 42.46           C  
-ATOM  22770  CD  LYS F 441     -14.307 -56.197 -14.903  1.00 47.66           C  
-ATOM  22771  CE  LYS F 441     -14.569 -57.022 -13.652  1.00 46.90           C  
-ATOM  22772  NZ  LYS F 441     -14.203 -56.285 -12.409  1.00 59.29           N  
-ATOM  22773  N   ASP F 442     -15.028 -52.597 -18.574  1.00 29.86           N  
-ATOM  22774  CA  ASP F 442     -15.306 -51.587 -19.590  1.00 32.54           C  
-ATOM  22775  C   ASP F 442     -14.026 -50.872 -20.023  1.00 31.46           C  
-ATOM  22776  O   ASP F 442     -12.929 -51.230 -19.595  1.00 28.14           O  
-ATOM  22777  CB  ASP F 442     -16.342 -50.572 -19.091  1.00 28.40           C  
-ATOM  22778  CG  ASP F 442     -15.922 -49.875 -17.808  1.00 31.97           C  
-ATOM  22779  OD1 ASP F 442     -14.792 -50.105 -17.329  1.00 34.36           O  
-ATOM  22780  OD2 ASP F 442     -16.731 -49.081 -17.281  1.00 35.18           O  
-ATOM  22781  N   MET F 443     -14.178 -49.855 -20.865  1.00 32.20           N  
-ATOM  22782  CA  MET F 443     -13.037 -49.145 -21.433  1.00 30.46           C  
-ATOM  22783  C   MET F 443     -12.456 -48.103 -20.483  1.00 28.41           C  
-ATOM  22784  O   MET F 443     -11.522 -47.385 -20.840  1.00 42.03           O  
-ATOM  22785  CB  MET F 443     -13.440 -48.469 -22.743  1.00 28.47           C  
-ATOM  22786  CG  MET F 443     -14.504 -47.402 -22.574  1.00 24.87           C  
-ATOM  22787  SD  MET F 443     -15.038 -46.698 -24.140  1.00 32.31           S  
-ATOM  22788  CE  MET F 443     -16.244 -45.500 -23.578  1.00 36.11           C  
-ATOM  22789  N   HIS F 444     -13.011 -48.013 -19.279  1.00 26.98           N  
-ATOM  22790  CA  HIS F 444     -12.520 -47.061 -18.289  1.00 37.64           C  
-ATOM  22791  C   HIS F 444     -11.803 -47.783 -17.155  1.00 36.83           C  
-ATOM  22792  O   HIS F 444     -11.309 -47.155 -16.217  1.00 31.68           O  
-ATOM  22793  CB  HIS F 444     -13.670 -46.219 -17.731  1.00 34.77           C  
-ATOM  22794  CG  HIS F 444     -14.399 -45.430 -18.772  1.00 36.17           C  
-ATOM  22795  ND1 HIS F 444     -13.793 -44.442 -19.518  1.00 39.30           N  
-ATOM  22796  CD2 HIS F 444     -15.686 -45.482 -19.190  1.00 33.04           C  
-ATOM  22797  CE1 HIS F 444     -14.675 -43.920 -20.352  1.00 46.49           C  
-ATOM  22798  NE2 HIS F 444     -15.832 -44.534 -20.173  1.00 34.52           N  
-ATOM  22799  N   THR F 445     -11.749 -49.107 -17.250  1.00 32.58           N  
-ATOM  22800  CA  THR F 445     -11.173 -49.923 -16.191  1.00 29.80           C  
-ATOM  22801  C   THR F 445      -9.665 -50.074 -16.353  1.00 27.92           C  
-ATOM  22802  O   THR F 445      -9.172 -50.345 -17.446  1.00 34.49           O  
-ATOM  22803  CB  THR F 445     -11.817 -51.320 -16.152  1.00 26.63           C  
-ATOM  22804  OG1 THR F 445     -13.244 -51.189 -16.139  1.00 27.69           O  
-ATOM  22805  CG2 THR F 445     -11.368 -52.081 -14.913  1.00 35.02           C  
-ATOM  22806  N   ASP F 446      -8.940 -49.892 -15.255  1.00 30.51           N  
-ATOM  22807  CA  ASP F 446      -7.498 -50.095 -15.239  1.00 33.90           C  
-ATOM  22808  C   ASP F 446      -7.185 -51.580 -15.071  1.00 37.69           C  
-ATOM  22809  O   ASP F 446      -7.512 -52.176 -14.045  1.00 41.47           O  
-ATOM  22810  CB  ASP F 446      -6.858 -49.282 -14.113  1.00 41.95           C  
-ATOM  22811  CG  ASP F 446      -5.345 -49.362 -14.120  1.00 48.22           C  
-ATOM  22812  OD1 ASP F 446      -4.747 -49.293 -15.215  1.00 56.62           O  
-ATOM  22813  OD2 ASP F 446      -4.755 -49.492 -13.026  1.00 43.71           O  
-ATOM  22814  N   TYR F 447      -6.557 -52.177 -16.078  1.00 37.62           N  
-ATOM  22815  CA  TYR F 447      -6.283 -53.610 -16.055  1.00 32.85           C  
-ATOM  22816  C   TYR F 447      -4.814 -53.932 -15.813  1.00 39.89           C  
-ATOM  22817  O   TYR F 447      -4.388 -55.065 -16.044  1.00 38.46           O  
-ATOM  22818  CB  TYR F 447      -6.715 -54.262 -17.369  1.00 30.42           C  
-ATOM  22819  CG  TYR F 447      -8.180 -54.116 -17.693  1.00 26.76           C  
-ATOM  22820  CD1 TYR F 447      -9.135 -54.891 -17.048  1.00 26.67           C  
-ATOM  22821  CD2 TYR F 447      -8.609 -53.219 -18.662  1.00 26.65           C  
-ATOM  22822  CE1 TYR F 447     -10.477 -54.764 -17.349  1.00 28.36           C  
-ATOM  22823  CE2 TYR F 447      -9.948 -53.088 -18.970  1.00 30.37           C  
-ATOM  22824  CZ  TYR F 447     -10.878 -53.862 -18.311  1.00 30.49           C  
-ATOM  22825  OH  TYR F 447     -12.215 -53.729 -18.617  1.00 33.32           O  
-ATOM  22826  N   THR F 448      -4.041 -52.952 -15.354  1.00 42.91           N  
-ATOM  22827  CA  THR F 448      -2.597 -53.139 -15.236  1.00 48.72           C  
-ATOM  22828  C   THR F 448      -2.262 -54.280 -14.268  1.00 47.00           C  
-ATOM  22829  O   THR F 448      -2.828 -54.383 -13.177  1.00 47.18           O  
-ATOM  22830  CB  THR F 448      -1.882 -51.830 -14.803  1.00 38.49           C  
-ATOM  22831  OG1 THR F 448      -0.463 -52.010 -14.882  1.00 41.95           O  
-ATOM  22832  CG2 THR F 448      -2.270 -51.414 -13.387  1.00 41.05           C  
-ATOM  22833  N   GLY F 449      -1.366 -55.161 -14.702  1.00 39.60           N  
-ATOM  22834  CA  GLY F 449      -0.972 -56.308 -13.905  1.00 37.07           C  
-ATOM  22835  C   GLY F 449      -1.775 -57.565 -14.190  1.00 38.03           C  
-ATOM  22836  O   GLY F 449      -1.345 -58.672 -13.865  1.00 40.89           O  
-ATOM  22837  N   GLN F 450      -2.944 -57.400 -14.799  1.00 36.61           N  
-ATOM  22838  CA  GLN F 450      -3.815 -58.535 -15.093  1.00 36.54           C  
-ATOM  22839  C   GLN F 450      -3.494 -59.182 -16.443  1.00 46.31           C  
-ATOM  22840  O   GLN F 450      -3.096 -58.503 -17.392  1.00 46.82           O  
-ATOM  22841  CB  GLN F 450      -5.281 -58.099 -15.070  1.00 31.69           C  
-ATOM  22842  CG  GLN F 450      -5.744 -57.507 -13.750  1.00 35.93           C  
-ATOM  22843  CD  GLN F 450      -7.177 -57.011 -13.807  1.00 37.49           C  
-ATOM  22844  OE1 GLN F 450      -8.086 -57.742 -14.200  1.00 35.15           O  
-ATOM  22845  NE2 GLN F 450      -7.384 -55.758 -13.424  1.00 46.43           N  
-ATOM  22846  N   GLY F 451      -3.672 -60.498 -16.519  1.00 39.77           N  
-ATOM  22847  CA  GLY F 451      -3.485 -61.231 -17.759  1.00 23.37           C  
-ATOM  22848  C   GLY F 451      -2.035 -61.350 -18.181  1.00 24.09           C  
-ATOM  22849  O   GLY F 451      -1.129 -60.992 -17.430  1.00 29.61           O  
-ATOM  22850  N   VAL F 452      -1.818 -61.855 -19.392  1.00 22.84           N  
-ATOM  22851  CA  VAL F 452      -0.473 -62.037 -19.927  1.00 18.27           C  
-ATOM  22852  C   VAL F 452      -0.072 -60.862 -20.813  1.00 20.43           C  
-ATOM  22853  O   VAL F 452      -0.845 -60.426 -21.664  1.00 19.47           O  
-ATOM  22854  CB  VAL F 452      -0.364 -63.342 -20.737  1.00 12.96           C  
-ATOM  22855  CG1 VAL F 452       1.027 -63.493 -21.338  1.00 14.85           C  
-ATOM  22856  CG2 VAL F 452      -0.701 -64.533 -19.859  1.00 12.68           C  
-ATOM  22857  N   ASP F 453       1.135 -60.345 -20.604  1.00 23.63           N  
-ATOM  22858  CA  ASP F 453       1.653 -59.271 -21.445  1.00 20.34           C  
-ATOM  22859  C   ASP F 453       2.487 -59.840 -22.592  1.00 26.84           C  
-ATOM  22860  O   ASP F 453       3.716 -59.887 -22.524  1.00 27.49           O  
-ATOM  22861  CB  ASP F 453       2.481 -58.290 -20.618  1.00 29.09           C  
-ATOM  22862  CG  ASP F 453       2.690 -56.966 -21.325  1.00 30.65           C  
-ATOM  22863  OD1 ASP F 453       2.601 -56.929 -22.570  1.00 31.01           O  
-ATOM  22864  OD2 ASP F 453       2.950 -55.961 -20.632  1.00 30.48           O  
-ATOM  22865  N   GLN F 454       1.797 -60.259 -23.649  1.00 27.21           N  
-ATOM  22866  CA  GLN F 454       2.431 -60.894 -24.796  1.00 17.14           C  
-ATOM  22867  C   GLN F 454       3.493 -60.017 -25.438  1.00 23.61           C  
-ATOM  22868  O   GLN F 454       4.535 -60.515 -25.852  1.00 29.71           O  
-ATOM  22869  CB  GLN F 454       1.389 -61.261 -25.845  1.00 14.60           C  
-ATOM  22870  CG  GLN F 454       0.340 -62.234 -25.360  1.00 15.91           C  
-ATOM  22871  CD  GLN F 454      -0.598 -62.657 -26.467  1.00 24.79           C  
-ATOM  22872  OE1 GLN F 454      -0.316 -63.599 -27.208  1.00 27.94           O  
-ATOM  22873  NE2 GLN F 454      -1.721 -61.961 -26.589  1.00 28.05           N  
-ATOM  22874  N   LEU F 455       3.224 -58.718 -25.527  1.00 23.99           N  
-ATOM  22875  CA  LEU F 455       4.158 -57.786 -26.153  1.00 28.03           C  
-ATOM  22876  C   LEU F 455       5.471 -57.721 -25.375  1.00 26.25           C  
-ATOM  22877  O   LEU F 455       6.563 -57.866 -25.943  1.00 19.97           O  
-ATOM  22878  CB  LEU F 455       3.516 -56.398 -26.260  1.00 17.36           C  
-ATOM  22879  CG  LEU F 455       4.241 -55.301 -27.042  1.00 17.80           C  
-ATOM  22880  CD1 LEU F 455       4.537 -55.727 -28.470  1.00 13.04           C  
-ATOM  22881  CD2 LEU F 455       3.410 -54.031 -27.032  1.00 19.18           C  
-ATOM  22882  N   LYS F 456       5.347 -57.518 -24.068  1.00 25.84           N  
-ATOM  22883  CA  LYS F 456       6.507 -57.440 -23.191  1.00 29.79           C  
-ATOM  22884  C   LYS F 456       7.276 -58.751 -23.184  1.00 24.54           C  
-ATOM  22885  O   LYS F 456       8.502 -58.751 -23.175  1.00 20.41           O  
-ATOM  22886  CB  LYS F 456       6.093 -57.074 -21.763  1.00 29.19           C  
-ATOM  22887  CG  LYS F 456       7.263 -56.716 -20.862  1.00 31.95           C  
-ATOM  22888  CD  LYS F 456       6.822 -56.514 -19.421  1.00 40.92           C  
-ATOM  22889  CE  LYS F 456       6.970 -57.791 -18.605  1.00 55.01           C  
-ATOM  22890  NZ  LYS F 456       6.090 -58.890 -19.091  1.00 51.19           N  
-ATOM  22891  N   ASN F 457       6.551 -59.865 -23.184  1.00 19.07           N  
-ATOM  22892  CA  ASN F 457       7.187 -61.174 -23.230  1.00 22.61           C  
-ATOM  22893  C   ASN F 457       7.978 -61.359 -24.523  1.00 27.63           C  
-ATOM  22894  O   ASN F 457       9.106 -61.854 -24.506  1.00 30.36           O  
-ATOM  22895  CB  ASN F 457       6.146 -62.290 -23.082  1.00 24.25           C  
-ATOM  22896  CG  ASN F 457       5.510 -62.316 -21.708  1.00 24.20           C  
-ATOM  22897  OD1 ASN F 457       5.950 -61.617 -20.794  1.00 21.12           O  
-ATOM  22898  ND2 ASN F 457       4.472 -63.133 -21.552  1.00 22.35           N  
-ATOM  22899  N   VAL F 458       7.378 -60.952 -25.637  1.00 24.80           N  
-ATOM  22900  CA  VAL F 458       8.023 -61.032 -26.940  1.00 22.14           C  
-ATOM  22901  C   VAL F 458       9.301 -60.212 -26.954  1.00 21.49           C  
-ATOM  22902  O   VAL F 458      10.341 -60.682 -27.405  1.00 25.17           O  
-ATOM  22903  CB  VAL F 458       7.091 -60.546 -28.069  1.00 21.11           C  
-ATOM  22904  CG1 VAL F 458       7.894 -60.185 -29.311  1.00 20.57           C  
-ATOM  22905  CG2 VAL F 458       6.056 -61.609 -28.393  1.00 22.74           C  
-ATOM  22906  N   ILE F 459       9.223 -58.988 -26.445  1.00 23.84           N  
-ATOM  22907  CA  ILE F 459      10.399 -58.127 -26.394  1.00 22.97           C  
-ATOM  22908  C   ILE F 459      11.494 -58.724 -25.510  1.00 23.29           C  
-ATOM  22909  O   ILE F 459      12.666 -58.738 -25.893  1.00 25.11           O  
-ATOM  22910  CB  ILE F 459      10.042 -56.720 -25.891  1.00 19.58           C  
-ATOM  22911  CG1 ILE F 459       9.159 -56.011 -26.916  1.00 18.03           C  
-ATOM  22912  CG2 ILE F 459      11.302 -55.908 -25.630  1.00 16.00           C  
-ATOM  22913  CD1 ILE F 459       8.805 -54.601 -26.529  1.00 25.91           C  
-ATOM  22914  N   GLN F 460      11.110 -59.226 -24.339  1.00 23.12           N  
-ATOM  22915  CA  GLN F 460      12.063 -59.841 -23.418  1.00 25.93           C  
-ATOM  22916  C   GLN F 460      12.779 -61.020 -24.062  1.00 25.05           C  
-ATOM  22917  O   GLN F 460      14.004 -61.108 -24.023  1.00 23.25           O  
-ATOM  22918  CB  GLN F 460      11.362 -60.296 -22.134  1.00 35.05           C  
-ATOM  22919  CG  GLN F 460      12.238 -61.137 -21.203  1.00 48.90           C  
-ATOM  22920  CD  GLN F 460      13.228 -60.308 -20.398  1.00 48.40           C  
-ATOM  22921  OE1 GLN F 460      13.419 -59.116 -20.653  1.00 42.60           O  
-ATOM  22922  NE2 GLN F 460      13.859 -60.940 -19.413  1.00 33.24           N  
-ATOM  22923  N   MET F 461      12.006 -61.921 -24.658  1.00 28.22           N  
-ATOM  22924  CA  MET F 461      12.574 -63.085 -25.325  1.00 25.48           C  
-ATOM  22925  C   MET F 461      13.464 -62.665 -26.489  1.00 22.66           C  
-ATOM  22926  O   MET F 461      14.473 -63.301 -26.764  1.00 28.74           O  
-ATOM  22927  CB  MET F 461      11.468 -64.026 -25.816  1.00 32.02           C  
-ATOM  22928  CG  MET F 461      11.990 -65.350 -26.357  1.00 40.43           C  
-ATOM  22929  SD  MET F 461      12.970 -66.269 -25.148  1.00 46.31           S  
-ATOM  22930  CE  MET F 461      11.704 -66.746 -23.971  1.00 39.40           C  
-ATOM  22931  N   LEU F 462      13.089 -61.586 -27.166  1.00 26.93           N  
-ATOM  22932  CA  LEU F 462      13.894 -61.059 -28.263  1.00 20.50           C  
-ATOM  22933  C   LEU F 462      15.242 -60.554 -27.767  1.00 22.98           C  
-ATOM  22934  O   LEU F 462      16.267 -60.770 -28.412  1.00 22.06           O  
-ATOM  22935  CB  LEU F 462      13.154 -59.932 -28.988  1.00 14.59           C  
-ATOM  22936  CG  LEU F 462      12.157 -60.355 -30.068  1.00 19.79           C  
-ATOM  22937  CD1 LEU F 462      11.334 -59.171 -30.537  1.00 24.74           C  
-ATOM  22938  CD2 LEU F 462      12.876 -60.987 -31.237  1.00 13.75           C  
-ATOM  22939  N   ARG F 463      15.236 -59.889 -26.616  1.00 21.17           N  
-ATOM  22940  CA  ARG F 463      16.447 -59.262 -26.095  1.00 18.20           C  
-ATOM  22941  C   ARG F 463      17.361 -60.239 -25.352  1.00 19.02           C  
-ATOM  22942  O   ARG F 463      18.572 -60.028 -25.290  1.00 14.14           O  
-ATOM  22943  CB  ARG F 463      16.079 -58.087 -25.181  1.00 17.54           C  
-ATOM  22944  CG  ARG F 463      15.374 -56.950 -25.911  1.00 17.98           C  
-ATOM  22945  CD  ARG F 463      15.563 -55.598 -25.229  1.00 19.78           C  
-ATOM  22946  NE  ARG F 463      14.644 -55.388 -24.113  1.00 18.65           N  
-ATOM  22947  CZ  ARG F 463      14.060 -54.224 -23.837  1.00 18.15           C  
-ATOM  22948  NH1 ARG F 463      14.292 -53.164 -24.601  1.00  9.77           N  
-ATOM  22949  NH2 ARG F 463      13.242 -54.120 -22.800  1.00 22.52           N  
-ATOM  22950  N   THR F 464      16.791 -61.309 -24.804  1.00 21.02           N  
-ATOM  22951  CA  THR F 464      17.579 -62.260 -24.022  1.00 16.84           C  
-ATOM  22952  C   THR F 464      17.971 -63.507 -24.809  1.00 16.83           C  
-ATOM  22953  O   THR F 464      19.059 -64.047 -24.623  1.00 27.31           O  
-ATOM  22954  CB  THR F 464      16.826 -62.713 -22.757  1.00 20.19           C  
-ATOM  22955  OG1 THR F 464      15.683 -63.493 -23.127  1.00 23.65           O  
-ATOM  22956  CG2 THR F 464      16.380 -61.511 -21.931  1.00 23.95           C  
-ATOM  22957  N   ASN F 465      17.082 -63.960 -25.685  1.00 22.30           N  
-ATOM  22958  CA  ASN F 465      17.267 -65.229 -26.383  1.00 25.35           C  
-ATOM  22959  C   ASN F 465      16.500 -65.271 -27.704  1.00 28.94           C  
-ATOM  22960  O   ASN F 465      15.408 -65.835 -27.779  1.00 31.34           O  
-ATOM  22961  CB  ASN F 465      16.827 -66.380 -25.477  1.00 27.10           C  
-ATOM  22962  CG  ASN F 465      17.006 -67.735 -26.124  1.00 31.63           C  
-ATOM  22963  OD1 ASN F 465      17.932 -67.946 -26.905  1.00 31.35           O  
-ATOM  22964  ND2 ASN F 465      16.111 -68.663 -25.805  1.00 28.85           N  
-ATOM  22965  N   PRO F 466      17.075 -64.674 -28.758  1.00 32.95           N  
-ATOM  22966  CA  PRO F 466      16.367 -64.463 -30.026  1.00 32.27           C  
-ATOM  22967  C   PRO F 466      16.141 -65.731 -30.850  1.00 29.04           C  
-ATOM  22968  O   PRO F 466      15.435 -65.675 -31.857  1.00 31.68           O  
-ATOM  22969  CB  PRO F 466      17.293 -63.500 -30.777  1.00 32.67           C  
-ATOM  22970  CG  PRO F 466      18.649 -63.834 -30.269  1.00 36.77           C  
-ATOM  22971  CD  PRO F 466      18.462 -64.181 -28.814  1.00 41.52           C  
-ATOM  22972  N   THR F 467      16.725 -66.851 -30.438  1.00 26.92           N  
-ATOM  22973  CA  THR F 467      16.602 -68.084 -31.209  1.00 37.14           C  
-ATOM  22974  C   THR F 467      15.367 -68.885 -30.801  1.00 36.56           C  
-ATOM  22975  O   THR F 467      15.068 -69.923 -31.393  1.00 36.42           O  
-ATOM  22976  CB  THR F 467      17.850 -68.976 -31.058  1.00 41.16           C  
-ATOM  22977  OG1 THR F 467      17.961 -69.425 -29.702  1.00 51.00           O  
-ATOM  22978  CG2 THR F 467      19.102 -68.205 -31.439  1.00 36.62           C  
-ATOM  22979  N   ASP F 468      14.654 -68.399 -29.790  1.00 29.66           N  
-ATOM  22980  CA  ASP F 468      13.434 -69.053 -29.328  1.00 29.91           C  
-ATOM  22981  C   ASP F 468      12.324 -68.915 -30.364  1.00 34.81           C  
-ATOM  22982  O   ASP F 468      12.071 -67.824 -30.873  1.00 41.53           O  
-ATOM  22983  CB  ASP F 468      12.987 -68.470 -27.988  1.00 35.09           C  
-ATOM  22984  CG  ASP F 468      11.601 -68.931 -27.585  1.00 35.96           C  
-ATOM  22985  OD1 ASP F 468      11.478 -70.056 -27.056  1.00 42.13           O  
-ATOM  22986  OD2 ASP F 468      10.635 -68.167 -27.790  1.00 30.14           O  
-ATOM  22987  N   ARG F 469      11.661 -70.025 -30.671  1.00 41.55           N  
-ATOM  22988  CA  ARG F 469      10.660 -70.046 -31.733  1.00 37.88           C  
-ATOM  22989  C   ARG F 469       9.236 -69.894 -31.210  1.00 31.70           C  
-ATOM  22990  O   ARG F 469       8.280 -70.268 -31.888  1.00 31.27           O  
-ATOM  22991  CB  ARG F 469      10.778 -71.341 -32.540  1.00 28.88           C  
-ATOM  22992  CG  ARG F 469      12.093 -71.483 -33.284  1.00 29.57           C  
-ATOM  22993  CD  ARG F 469      12.181 -72.814 -34.011  1.00 32.81           C  
-ATOM  22994  NE  ARG F 469      12.276 -73.939 -33.085  1.00 51.02           N  
-ATOM  22995  CZ  ARG F 469      13.224 -74.870 -33.135  1.00 45.74           C  
-ATOM  22996  NH1 ARG F 469      14.160 -74.816 -34.073  1.00 29.87           N  
-ATOM  22997  NH2 ARG F 469      13.235 -75.858 -32.250  1.00 45.46           N  
-ATOM  22998  N   ARG F 470       9.098 -69.345 -30.007  1.00 31.97           N  
-ATOM  22999  CA  ARG F 470       7.782 -69.147 -29.408  1.00 30.32           C  
-ATOM  23000  C   ARG F 470       7.496 -67.669 -29.182  1.00 28.15           C  
-ATOM  23001  O   ARG F 470       6.766 -67.302 -28.259  1.00 21.00           O  
-ATOM  23002  CB  ARG F 470       7.668 -69.908 -28.086  1.00 23.91           C  
-ATOM  23003  CG  ARG F 470       7.747 -71.416 -28.222  1.00 24.83           C  
-ATOM  23004  CD  ARG F 470       8.997 -71.955 -27.553  1.00 28.87           C  
-ATOM  23005  NE  ARG F 470       8.987 -73.411 -27.454  1.00 44.38           N  
-ATOM  23006  CZ  ARG F 470       9.495 -74.092 -26.431  1.00 50.80           C  
-ATOM  23007  NH1 ARG F 470      10.052 -73.448 -25.414  1.00 44.35           N  
-ATOM  23008  NH2 ARG F 470       9.444 -75.418 -26.422  1.00 42.28           N  
-ATOM  23009  N   MET F 471       8.075 -66.826 -30.031  1.00 22.24           N  
-ATOM  23010  CA  MET F 471       7.917 -65.383 -29.906  1.00 19.78           C  
-ATOM  23011  C   MET F 471       6.673 -64.896 -30.650  1.00 21.01           C  
-ATOM  23012  O   MET F 471       6.769 -64.205 -31.665  1.00 21.40           O  
-ATOM  23013  CB  MET F 471       9.173 -64.677 -30.419  1.00 21.83           C  
-ATOM  23014  CG  MET F 471      10.443 -65.150 -29.722  1.00 24.16           C  
-ATOM  23015  SD  MET F 471      11.919 -64.220 -30.164  1.00 18.08           S  
-ATOM  23016  CE  MET F 471      12.117 -64.675 -31.884  1.00 27.50           C  
-ATOM  23017  N   LEU F 472       5.504 -65.261 -30.131  1.00 27.63           N  
-ATOM  23018  CA  LEU F 472       4.240 -64.931 -30.780  1.00 24.58           C  
-ATOM  23019  C   LEU F 472       3.349 -64.014 -29.952  1.00 22.85           C  
-ATOM  23020  O   LEU F 472       3.426 -63.980 -28.725  1.00 29.68           O  
-ATOM  23021  CB  LEU F 472       3.457 -66.203 -31.112  1.00 25.22           C  
-ATOM  23022  CG  LEU F 472       3.933 -67.040 -32.297  1.00 25.03           C  
-ATOM  23023  CD1 LEU F 472       4.938 -68.096 -31.861  1.00 23.65           C  
-ATOM  23024  CD2 LEU F 472       2.738 -67.670 -32.985  1.00 38.15           C  
-ATOM  23025  N   MET F 473       2.493 -63.283 -30.654  1.00 23.54           N  
-ATOM  23026  CA  MET F 473       1.471 -62.459 -30.037  1.00 22.11           C  
-ATOM  23027  C   MET F 473       0.154 -62.702 -30.763  1.00 24.68           C  
-ATOM  23028  O   MET F 473       0.033 -62.440 -31.967  1.00 30.11           O  
-ATOM  23029  CB  MET F 473       1.863 -60.982 -30.082  1.00 20.27           C  
-ATOM  23030  CG  MET F 473       0.932 -60.068 -29.306  1.00 17.68           C  
-ATOM  23031  SD  MET F 473       1.658 -58.441 -29.024  1.00 40.14           S  
-ATOM  23032  CE  MET F 473       1.951 -57.884 -30.701  1.00 18.75           C  
-ATOM  23033  N   THR F 474      -0.823 -63.228 -30.034  1.00 18.65           N  
-ATOM  23034  CA  THR F 474      -2.121 -63.538 -30.614  1.00 19.80           C  
-ATOM  23035  C   THR F 474      -3.192 -62.599 -30.075  1.00 26.82           C  
-ATOM  23036  O   THR F 474      -3.065 -62.062 -28.974  1.00 31.09           O  
-ATOM  23037  CB  THR F 474      -2.534 -64.993 -30.333  1.00 22.79           C  
-ATOM  23038  OG1 THR F 474      -3.779 -65.275 -30.982  1.00 27.31           O  
-ATOM  23039  CG2 THR F 474      -2.683 -65.227 -28.838  1.00 25.04           C  
-ATOM  23040  N   ALA F 475      -4.243 -62.395 -30.862  1.00 24.44           N  
-ATOM  23041  CA  ALA F 475      -5.364 -61.566 -30.441  1.00 19.70           C  
-ATOM  23042  C   ALA F 475      -6.654 -62.374 -30.456  1.00 19.21           C  
-ATOM  23043  O   ALA F 475      -7.719 -61.870 -30.102  1.00 23.68           O  
-ATOM  23044  CB  ALA F 475      -5.489 -60.347 -31.335  1.00 21.09           C  
-ATOM  23045  N   TRP F 476      -6.546 -63.635 -30.865  1.00 16.07           N  
-ATOM  23046  CA  TRP F 476      -7.710 -64.497 -31.008  1.00 15.21           C  
-ATOM  23047  C   TRP F 476      -7.997 -65.262 -29.724  1.00 20.82           C  
-ATOM  23048  O   TRP F 476      -7.384 -66.293 -29.453  1.00 30.72           O  
-ATOM  23049  CB  TRP F 476      -7.513 -65.472 -32.171  1.00 17.24           C  
-ATOM  23050  CG  TRP F 476      -8.781 -66.134 -32.604  1.00 20.83           C  
-ATOM  23051  CD1 TRP F 476      -9.190 -67.399 -32.303  1.00 24.21           C  
-ATOM  23052  CD2 TRP F 476      -9.817 -65.558 -33.408  1.00 26.67           C  
-ATOM  23053  NE1 TRP F 476     -10.414 -67.651 -32.875  1.00 22.70           N  
-ATOM  23054  CE2 TRP F 476     -10.822 -66.534 -33.559  1.00 23.54           C  
-ATOM  23055  CE3 TRP F 476      -9.993 -64.311 -34.016  1.00 18.54           C  
-ATOM  23056  CZ2 TRP F 476     -11.983 -66.304 -34.292  1.00 19.87           C  
-ATOM  23057  CZ3 TRP F 476     -11.144 -64.084 -34.743  1.00 17.62           C  
-ATOM  23058  CH2 TRP F 476     -12.124 -65.075 -34.876  1.00 19.12           C  
-ATOM  23059  N   ASN F 477      -8.933 -64.740 -28.938  1.00 21.31           N  
-ATOM  23060  CA  ASN F 477      -9.355 -65.380 -27.699  1.00 24.28           C  
-ATOM  23061  C   ASN F 477     -10.813 -65.811 -27.789  1.00 29.67           C  
-ATOM  23062  O   ASN F 477     -11.714 -65.007 -27.546  1.00 34.08           O  
-ATOM  23063  CB  ASN F 477      -9.155 -64.433 -26.512  1.00 27.51           C  
-ATOM  23064  CG  ASN F 477      -9.456 -65.088 -25.170  1.00 31.72           C  
-ATOM  23065  OD1 ASN F 477      -9.943 -66.216 -25.104  1.00 30.78           O  
-ATOM  23066  ND2 ASN F 477      -9.171 -64.369 -24.089  1.00 33.29           N  
-ATOM  23067  N   PRO F 478     -11.045 -67.085 -28.138  1.00 29.65           N  
-ATOM  23068  CA  PRO F 478     -12.378 -67.691 -28.255  1.00 25.76           C  
-ATOM  23069  C   PRO F 478     -13.297 -67.402 -27.065  1.00 29.65           C  
-ATOM  23070  O   PRO F 478     -14.514 -67.337 -27.238  1.00 34.71           O  
-ATOM  23071  CB  PRO F 478     -12.065 -69.186 -28.345  1.00 25.96           C  
-ATOM  23072  CG  PRO F 478     -10.738 -69.230 -29.015  1.00 31.26           C  
-ATOM  23073  CD  PRO F 478      -9.979 -68.028 -28.519  1.00 25.88           C  
-ATOM  23074  N   ALA F 479     -12.716 -67.222 -25.882  1.00 28.16           N  
-ATOM  23075  CA  ALA F 479     -13.488 -66.997 -24.663  1.00 25.92           C  
-ATOM  23076  C   ALA F 479     -13.944 -65.547 -24.517  1.00 32.25           C  
-ATOM  23077  O   ALA F 479     -14.683 -65.214 -23.589  1.00 34.53           O  
-ATOM  23078  CB  ALA F 479     -12.672 -67.409 -23.448  1.00 24.69           C  
-ATOM  23079  N   ALA F 480     -13.506 -64.688 -25.431  1.00 30.99           N  
-ATOM  23080  CA  ALA F 480     -13.808 -63.264 -25.337  1.00 35.22           C  
-ATOM  23081  C   ALA F 480     -14.393 -62.707 -26.635  1.00 39.60           C  
-ATOM  23082  O   ALA F 480     -14.807 -61.545 -26.687  1.00 36.54           O  
-ATOM  23083  CB  ALA F 480     -12.554 -62.492 -24.950  1.00 34.06           C  
-ATOM  23084  N   LEU F 481     -14.434 -63.542 -27.671  1.00 32.06           N  
-ATOM  23085  CA  LEU F 481     -14.882 -63.120 -28.995  1.00 25.75           C  
-ATOM  23086  C   LEU F 481     -16.239 -62.423 -28.955  1.00 32.23           C  
-ATOM  23087  O   LEU F 481     -16.378 -61.282 -29.402  1.00 30.03           O  
-ATOM  23088  CB  LEU F 481     -14.943 -64.319 -29.945  1.00 28.30           C  
-ATOM  23089  CG  LEU F 481     -13.634 -64.914 -30.473  1.00 24.12           C  
-ATOM  23090  CD1 LEU F 481     -13.931 -66.178 -31.261  1.00 38.10           C  
-ATOM  23091  CD2 LEU F 481     -12.886 -63.922 -31.341  1.00 16.48           C  
-ATOM  23092  N   ASP F 482     -17.227 -63.108 -28.388  1.00 36.50           N  
-ATOM  23093  CA  ASP F 482     -18.591 -62.598 -28.301  1.00 35.69           C  
-ATOM  23094  C   ASP F 482     -18.689 -61.263 -27.566  1.00 35.82           C  
-ATOM  23095  O   ASP F 482     -19.688 -60.556 -27.691  1.00 37.95           O  
-ATOM  23096  CB  ASP F 482     -19.490 -63.628 -27.610  1.00 51.35           C  
-ATOM  23097  CG  ASP F 482     -19.730 -64.863 -28.462  1.00 53.96           C  
-ATOM  23098  OD1 ASP F 482     -19.046 -65.017 -29.498  1.00 38.32           O  
-ATOM  23099  OD2 ASP F 482     -20.599 -65.681 -28.090  1.00 34.78           O  
-ATOM  23100  N   GLU F 483     -17.653 -60.923 -26.803  1.00 35.75           N  
-ATOM  23101  CA  GLU F 483     -17.660 -59.698 -26.009  1.00 30.79           C  
-ATOM  23102  C   GLU F 483     -17.060 -58.516 -26.753  1.00 32.57           C  
-ATOM  23103  O   GLU F 483     -17.111 -57.386 -26.273  1.00 27.45           O  
-ATOM  23104  CB  GLU F 483     -16.900 -59.912 -24.705  1.00 26.78           C  
-ATOM  23105  CG  GLU F 483     -17.439 -61.053 -23.877  1.00 38.49           C  
-ATOM  23106  CD  GLU F 483     -16.516 -61.420 -22.741  1.00 42.03           C  
-ATOM  23107  OE1 GLU F 483     -16.652 -62.538 -22.203  1.00 48.83           O  
-ATOM  23108  OE2 GLU F 483     -15.654 -60.587 -22.387  1.00 38.47           O  
-ATOM  23109  N   MET F 484     -16.488 -58.773 -27.924  1.00 36.80           N  
-ATOM  23110  CA  MET F 484     -15.823 -57.713 -28.672  1.00 32.37           C  
-ATOM  23111  C   MET F 484     -16.710 -57.155 -29.776  1.00 28.08           C  
-ATOM  23112  O   MET F 484     -17.534 -57.870 -30.347  1.00 32.13           O  
-ATOM  23113  CB  MET F 484     -14.511 -58.222 -29.264  1.00 30.48           C  
-ATOM  23114  CG  MET F 484     -13.579 -58.848 -28.245  1.00 37.29           C  
-ATOM  23115  SD  MET F 484     -12.193 -59.680 -29.037  1.00 31.90           S  
-ATOM  23116  CE  MET F 484     -13.059 -60.467 -30.380  1.00 30.65           C  
-ATOM  23117  N   ALA F 485     -16.529 -55.871 -30.066  1.00 26.68           N  
-ATOM  23118  CA  ALA F 485     -17.288 -55.193 -31.108  1.00 30.66           C  
-ATOM  23119  C   ALA F 485     -17.069 -55.877 -32.449  1.00 33.07           C  
-ATOM  23120  O   ALA F 485     -18.012 -56.111 -33.205  1.00 41.94           O  
-ATOM  23121  CB  ALA F 485     -16.892 -53.727 -31.184  1.00 28.71           C  
-ATOM  23122  N   LEU F 486     -15.812 -56.195 -32.731  1.00 33.38           N  
-ATOM  23123  CA  LEU F 486     -15.452 -56.940 -33.927  1.00 37.01           C  
-ATOM  23124  C   LEU F 486     -14.370 -57.964 -33.614  1.00 35.09           C  
-ATOM  23125  O   LEU F 486     -13.353 -57.630 -33.005  1.00 32.85           O  
-ATOM  23126  CB  LEU F 486     -14.971 -56.000 -35.035  1.00 36.53           C  
-ATOM  23127  CG  LEU F 486     -15.980 -55.620 -36.120  1.00 35.74           C  
-ATOM  23128  CD1 LEU F 486     -15.270 -55.014 -37.326  1.00 55.44           C  
-ATOM  23129  CD2 LEU F 486     -16.808 -56.824 -36.531  1.00 26.01           C  
-ATOM  23130  N   PRO F 487     -14.594 -59.223 -34.018  1.00 32.03           N  
-ATOM  23131  CA  PRO F 487     -13.543 -60.240 -33.949  1.00 30.25           C  
-ATOM  23132  C   PRO F 487     -12.313 -59.782 -34.722  1.00 31.49           C  
-ATOM  23133  O   PRO F 487     -12.459 -59.273 -35.832  1.00 33.07           O  
-ATOM  23134  CB  PRO F 487     -14.192 -61.461 -34.602  1.00 27.02           C  
-ATOM  23135  CG  PRO F 487     -15.646 -61.272 -34.370  1.00 30.48           C  
-ATOM  23136  CD  PRO F 487     -15.880 -59.791 -34.456  1.00 32.25           C  
-ATOM  23137  N   PRO F 488     -11.115 -59.960 -34.146  1.00 26.71           N  
-ATOM  23138  CA  PRO F 488      -9.903 -59.377 -34.729  1.00 32.74           C  
-ATOM  23139  C   PRO F 488      -9.559 -59.950 -36.103  1.00 31.91           C  
-ATOM  23140  O   PRO F 488      -9.633 -61.163 -36.310  1.00 25.65           O  
-ATOM  23141  CB  PRO F 488      -8.822 -59.728 -33.704  1.00 24.89           C  
-ATOM  23142  CG  PRO F 488      -9.313 -60.966 -33.062  1.00 26.08           C  
-ATOM  23143  CD  PRO F 488     -10.809 -60.834 -33.001  1.00 22.45           C  
-ATOM  23144  N   CYS F 489      -9.196 -59.074 -37.034  1.00 28.84           N  
-ATOM  23145  CA  CYS F 489      -8.785 -59.509 -38.361  1.00 34.28           C  
-ATOM  23146  C   CYS F 489      -7.317 -59.908 -38.325  1.00 32.12           C  
-ATOM  23147  O   CYS F 489      -6.987 -61.086 -38.458  1.00 25.66           O  
-ATOM  23148  CB  CYS F 489      -9.036 -58.414 -39.398  1.00 29.97           C  
-ATOM  23149  SG  CYS F 489     -10.780 -58.202 -39.823  1.00 50.27           S  
-ATOM  23150  N   HIS F 490      -6.434 -58.935 -38.131  1.00 30.12           N  
-ATOM  23151  CA  HIS F 490      -5.036 -59.259 -37.890  1.00 27.40           C  
-ATOM  23152  C   HIS F 490      -4.920 -59.886 -36.504  1.00 28.66           C  
-ATOM  23153  O   HIS F 490      -4.780 -59.187 -35.501  1.00 32.66           O  
-ATOM  23154  CB  HIS F 490      -4.141 -58.020 -38.027  1.00 32.14           C  
-ATOM  23155  CG  HIS F 490      -4.692 -56.783 -37.388  1.00 31.21           C  
-ATOM  23156  ND1 HIS F 490      -4.163 -56.240 -36.237  1.00 31.32           N  
-ATOM  23157  CD2 HIS F 490      -5.711 -55.967 -37.754  1.00 29.71           C  
-ATOM  23158  CE1 HIS F 490      -4.836 -55.148 -35.916  1.00 32.73           C  
-ATOM  23159  NE2 HIS F 490      -5.783 -54.965 -36.819  1.00 36.29           N  
-ATOM  23160  N   LEU F 491      -4.990 -61.213 -36.458  1.00 25.70           N  
-ATOM  23161  CA  LEU F 491      -5.094 -61.921 -35.188  1.00 22.13           C  
-ATOM  23162  C   LEU F 491      -3.792 -62.552 -34.717  1.00 22.31           C  
-ATOM  23163  O   LEU F 491      -3.696 -62.959 -33.558  1.00 20.08           O  
-ATOM  23164  CB  LEU F 491      -6.180 -62.999 -35.273  1.00 26.19           C  
-ATOM  23165  CG  LEU F 491      -6.122 -64.028 -36.404  1.00 21.06           C  
-ATOM  23166  CD1 LEU F 491      -5.212 -65.197 -36.062  1.00 22.71           C  
-ATOM  23167  CD2 LEU F 491      -7.523 -64.517 -36.703  1.00 20.43           C  
-ATOM  23168  N   LEU F 492      -2.795 -62.660 -35.591  1.00 26.95           N  
-ATOM  23169  CA  LEU F 492      -1.538 -63.245 -35.123  1.00 18.24           C  
-ATOM  23170  C   LEU F 492      -0.293 -62.532 -35.638  1.00 21.23           C  
-ATOM  23171  O   LEU F 492      -0.280 -62.020 -36.750  1.00 21.60           O  
-ATOM  23172  CB  LEU F 492      -1.474 -64.722 -35.508  1.00 19.07           C  
-ATOM  23173  CG  LEU F 492      -0.417 -65.500 -34.727  1.00 23.06           C  
-ATOM  23174  CD1 LEU F 492      -1.065 -66.575 -33.872  1.00 18.99           C  
-ATOM  23175  CD2 LEU F 492       0.626 -66.092 -35.660  1.00 25.57           C  
-ATOM  23176  N   CYS F 493       0.755 -62.487 -34.821  1.00 23.15           N  
-ATOM  23177  CA  CYS F 493       2.049 -62.037 -35.324  1.00 20.20           C  
-ATOM  23178  C   CYS F 493       3.192 -62.766 -34.634  1.00 22.95           C  
-ATOM  23179  O   CYS F 493       3.151 -63.011 -33.433  1.00 24.16           O  
-ATOM  23180  CB  CYS F 493       2.209 -60.523 -35.165  1.00 24.56           C  
-ATOM  23181  SG  CYS F 493       2.430 -59.947 -33.479  1.00 25.01           S  
-ATOM  23182  N   GLN F 494       4.205 -63.127 -35.415  1.00 25.25           N  
-ATOM  23183  CA  GLN F 494       5.364 -63.851 -34.908  1.00 23.63           C  
-ATOM  23184  C   GLN F 494       6.642 -63.175 -35.387  1.00 21.46           C  
-ATOM  23185  O   GLN F 494       6.715 -62.714 -36.525  1.00 17.71           O  
-ATOM  23186  CB  GLN F 494       5.329 -65.312 -35.360  1.00 23.33           C  
-ATOM  23187  CG  GLN F 494       6.497 -66.144 -34.863  1.00 25.52           C  
-ATOM  23188  CD  GLN F 494       6.511 -67.538 -35.453  1.00 27.38           C  
-ATOM  23189  OE1 GLN F 494       5.712 -67.861 -36.330  1.00 26.49           O  
-ATOM  23190  NE2 GLN F 494       7.423 -68.374 -34.972  1.00 25.89           N  
-ATOM  23191  N   PHE F 495       7.647 -63.115 -34.518  1.00 24.28           N  
-ATOM  23192  CA  PHE F 495       8.892 -62.426 -34.844  1.00 24.94           C  
-ATOM  23193  C   PHE F 495      10.073 -63.385 -34.989  1.00 21.95           C  
-ATOM  23194  O   PHE F 495      10.064 -64.492 -34.445  1.00 16.75           O  
-ATOM  23195  CB  PHE F 495       9.192 -61.364 -33.785  1.00 18.18           C  
-ATOM  23196  CG  PHE F 495       8.181 -60.255 -33.748  1.00 20.73           C  
-ATOM  23197  CD1 PHE F 495       8.361 -59.113 -34.511  1.00 18.09           C  
-ATOM  23198  CD2 PHE F 495       7.045 -60.357 -32.961  1.00 19.86           C  
-ATOM  23199  CE1 PHE F 495       7.432 -58.091 -34.484  1.00 18.76           C  
-ATOM  23200  CE2 PHE F 495       6.112 -59.339 -32.931  1.00 14.11           C  
-ATOM  23201  CZ  PHE F 495       6.305 -58.205 -33.693  1.00 15.48           C  
-ATOM  23202  N   TYR F 496      11.089 -62.944 -35.726  1.00 18.99           N  
-ATOM  23203  CA  TYR F 496      12.208 -63.802 -36.095  1.00 21.11           C  
-ATOM  23204  C   TYR F 496      13.508 -63.015 -36.196  1.00 24.68           C  
-ATOM  23205  O   TYR F 496      13.536 -61.912 -36.740  1.00 27.39           O  
-ATOM  23206  CB  TYR F 496      11.902 -64.498 -37.422  1.00 21.05           C  
-ATOM  23207  CG  TYR F 496      13.016 -65.341 -38.009  1.00 23.29           C  
-ATOM  23208  CD1 TYR F 496      13.116 -66.695 -37.716  1.00 22.40           C  
-ATOM  23209  CD2 TYR F 496      13.943 -64.791 -38.887  1.00 20.19           C  
-ATOM  23210  CE1 TYR F 496      14.121 -67.472 -38.260  1.00 19.55           C  
-ATOM  23211  CE2 TYR F 496      14.950 -65.559 -39.434  1.00 22.26           C  
-ATOM  23212  CZ  TYR F 496      15.034 -66.898 -39.119  1.00 19.45           C  
-ATOM  23213  OH  TYR F 496      16.035 -67.666 -39.664  1.00 19.90           O  
-ATOM  23214  N   VAL F 497      14.584 -63.586 -35.666  1.00 23.98           N  
-ATOM  23215  CA  VAL F 497      15.896 -62.960 -35.761  1.00 20.50           C  
-ATOM  23216  C   VAL F 497      16.870 -63.926 -36.416  1.00 18.87           C  
-ATOM  23217  O   VAL F 497      16.763 -65.139 -36.238  1.00 23.08           O  
-ATOM  23218  CB  VAL F 497      16.445 -62.541 -34.376  1.00 14.90           C  
-ATOM  23219  CG1 VAL F 497      17.522 -61.481 -34.531  1.00 15.01           C  
-ATOM  23220  CG2 VAL F 497      15.334 -62.022 -33.496  1.00 15.86           C  
-ATOM  23221  N   ASN F 498      17.813 -63.388 -37.181  1.00 18.40           N  
-ATOM  23222  CA  ASN F 498      18.863 -64.207 -37.768  1.00 19.44           C  
-ATOM  23223  C   ASN F 498      20.220 -63.888 -37.144  1.00 28.32           C  
-ATOM  23224  O   ASN F 498      20.296 -63.265 -36.082  1.00 25.63           O  
-ATOM  23225  CB  ASN F 498      18.909 -64.019 -39.286  1.00 20.17           C  
-ATOM  23226  CG  ASN F 498      19.211 -62.591 -39.691  1.00 19.05           C  
-ATOM  23227  OD1 ASN F 498      19.162 -61.677 -38.868  1.00 15.98           O  
-ATOM  23228  ND2 ASN F 498      19.518 -62.389 -40.968  1.00 19.10           N  
-ATOM  23229  N   ASP F 499      21.290 -64.314 -37.805  1.00 29.20           N  
-ATOM  23230  CA  ASP F 499      22.635 -64.129 -37.274  1.00 29.08           C  
-ATOM  23231  C   ASP F 499      23.161 -62.710 -37.490  1.00 28.81           C  
-ATOM  23232  O   ASP F 499      24.215 -62.346 -36.967  1.00 30.92           O  
-ATOM  23233  CB  ASP F 499      23.588 -65.144 -37.906  1.00 42.46           C  
-ATOM  23234  CG  ASP F 499      23.468 -65.193 -39.418  1.00 42.95           C  
-ATOM  23235  OD1 ASP F 499      22.360 -64.942 -39.938  1.00 24.99           O  
-ATOM  23236  OD2 ASP F 499      24.481 -65.486 -40.086  1.00 56.07           O  
-ATOM  23237  N   GLN F 500      22.425 -61.910 -38.255  1.00 25.86           N  
-ATOM  23238  CA  GLN F 500      22.836 -60.541 -38.544  1.00 25.78           C  
-ATOM  23239  C   GLN F 500      22.071 -59.536 -37.684  1.00 25.77           C  
-ATOM  23240  O   GLN F 500      22.059 -58.340 -37.984  1.00 26.40           O  
-ATOM  23241  CB  GLN F 500      22.628 -60.218 -40.024  1.00 31.76           C  
-ATOM  23242  CG  GLN F 500      23.192 -61.257 -40.979  1.00 35.80           C  
-ATOM  23243  CD  GLN F 500      24.688 -61.438 -40.829  1.00 46.07           C  
-ATOM  23244  OE1 GLN F 500      25.155 -62.492 -40.394  1.00 57.12           O  
-ATOM  23245  NE2 GLN F 500      25.450 -60.414 -41.196  1.00 39.41           N  
-ATOM  23246  N   LYS F 501      21.441 -60.030 -36.620  1.00 23.84           N  
-ATOM  23247  CA  LYS F 501      20.608 -59.210 -35.740  1.00 23.48           C  
-ATOM  23248  C   LYS F 501      19.485 -58.515 -36.507  1.00 24.93           C  
-ATOM  23249  O   LYS F 501      19.112 -57.388 -36.181  1.00 31.12           O  
-ATOM  23250  CB  LYS F 501      21.454 -58.166 -35.005  1.00 23.31           C  
-ATOM  23251  CG  LYS F 501      22.524 -58.741 -34.095  1.00 24.97           C  
-ATOM  23252  CD  LYS F 501      22.193 -58.493 -32.633  1.00 24.65           C  
-ATOM  23253  CE  LYS F 501      23.279 -59.047 -31.728  1.00 36.17           C  
-ATOM  23254  NZ  LYS F 501      24.608 -58.457 -32.048  1.00 44.58           N  
-ATOM  23255  N   GLU F 502      18.950 -59.189 -37.523  1.00 23.11           N  
-ATOM  23256  CA  GLU F 502      17.878 -58.622 -38.337  1.00 22.48           C  
-ATOM  23257  C   GLU F 502      16.515 -59.198 -37.959  1.00 23.25           C  
-ATOM  23258  O   GLU F 502      16.343 -60.414 -37.872  1.00 21.57           O  
-ATOM  23259  CB  GLU F 502      18.151 -58.855 -39.822  1.00 19.90           C  
-ATOM  23260  CG  GLU F 502      19.330 -58.071 -40.367  1.00 25.43           C  
-ATOM  23261  CD  GLU F 502      19.645 -58.424 -41.807  1.00 39.39           C  
-ATOM  23262  OE1 GLU F 502      19.450 -59.598 -42.191  1.00 37.14           O  
-ATOM  23263  OE2 GLU F 502      20.085 -57.526 -42.557  1.00 47.98           O  
-ATOM  23264  N   LEU F 503      15.548 -58.311 -37.744  1.00 24.78           N  
-ATOM  23265  CA  LEU F 503      14.213 -58.706 -37.310  1.00 22.21           C  
-ATOM  23266  C   LEU F 503      13.237 -58.831 -38.479  1.00 23.86           C  
-ATOM  23267  O   LEU F 503      13.252 -58.022 -39.407  1.00 20.64           O  
-ATOM  23268  CB  LEU F 503      13.672 -57.702 -36.291  1.00 21.98           C  
-ATOM  23269  CG  LEU F 503      12.281 -57.988 -35.720  1.00 21.00           C  
-ATOM  23270  CD1 LEU F 503      12.310 -59.233 -34.847  1.00 20.05           C  
-ATOM  23271  CD2 LEU F 503      11.753 -56.787 -34.944  1.00 19.94           C  
-ATOM  23272  N   SER F 504      12.392 -59.856 -38.422  1.00 24.10           N  
-ATOM  23273  CA  SER F 504      11.338 -60.054 -39.408  1.00 18.35           C  
-ATOM  23274  C   SER F 504      10.037 -60.390 -38.691  1.00 22.23           C  
-ATOM  23275  O   SER F 504      10.051 -60.991 -37.614  1.00 20.22           O  
-ATOM  23276  CB  SER F 504      11.708 -61.165 -40.394  1.00 18.43           C  
-ATOM  23277  OG  SER F 504      12.911 -60.868 -41.082  1.00 26.40           O  
-ATOM  23278  N   CYS F 505       8.914 -60.002 -39.287  1.00 24.50           N  
-ATOM  23279  CA  CYS F 505       7.615 -60.220 -38.662  1.00 17.87           C  
-ATOM  23280  C   CYS F 505       6.591 -60.818 -39.621  1.00 19.13           C  
-ATOM  23281  O   CYS F 505       6.352 -60.287 -40.704  1.00 21.63           O  
-ATOM  23282  CB  CYS F 505       7.076 -58.909 -38.090  1.00 15.12           C  
-ATOM  23283  SG  CYS F 505       5.399 -59.031 -37.427  1.00 34.85           S  
-ATOM  23284  N   ILE F 506       5.998 -61.935 -39.209  1.00 21.01           N  
-ATOM  23285  CA  ILE F 506       4.875 -62.545 -39.911  1.00 17.10           C  
-ATOM  23286  C   ILE F 506       3.574 -62.121 -39.252  1.00 20.90           C  
-ATOM  23287  O   ILE F 506       3.452 -62.178 -38.034  1.00 20.70           O  
-ATOM  23288  CB  ILE F 506       4.958 -64.087 -39.903  1.00 18.68           C  
-ATOM  23289  CG1 ILE F 506       6.002 -64.578 -40.899  1.00 19.99           C  
-ATOM  23290  CG2 ILE F 506       3.607 -64.710 -40.235  1.00 18.09           C  
-ATOM  23291  CD1 ILE F 506       6.196 -66.071 -40.867  1.00 18.83           C  
-ATOM  23292  N   MET F 507       2.600 -61.697 -40.047  1.00 19.09           N  
-ATOM  23293  CA  MET F 507       1.290 -61.386 -39.498  1.00 15.98           C  
-ATOM  23294  C   MET F 507       0.197 -62.180 -40.205  1.00 15.92           C  
-ATOM  23295  O   MET F 507       0.042 -62.093 -41.422  1.00 20.55           O  
-ATOM  23296  CB  MET F 507       1.011 -59.887 -39.595  1.00 15.30           C  
-ATOM  23297  CG  MET F 507      -0.262 -59.451 -38.892  1.00 22.95           C  
-ATOM  23298  SD  MET F 507      -1.716 -59.483 -39.955  1.00 26.05           S  
-ATOM  23299  CE  MET F 507      -1.535 -57.937 -40.839  1.00 18.56           C  
-ATOM  23300  N   TYR F 508      -0.551 -62.966 -39.438  1.00 18.09           N  
-ATOM  23301  CA  TYR F 508      -1.696 -63.680 -39.979  1.00 17.53           C  
-ATOM  23302  C   TYR F 508      -2.988 -62.919 -39.718  1.00 21.04           C  
-ATOM  23303  O   TYR F 508      -3.325 -62.582 -38.565  1.00 30.86           O  
-ATOM  23304  CB  TYR F 508      -1.809 -65.089 -39.401  1.00 17.60           C  
-ATOM  23305  CG  TYR F 508      -2.901 -65.890 -40.068  1.00 17.64           C  
-ATOM  23306  CD1 TYR F 508      -2.650 -66.605 -41.233  1.00 22.74           C  
-ATOM  23307  CD2 TYR F 508      -4.190 -65.911 -39.551  1.00 18.67           C  
-ATOM  23308  CE1 TYR F 508      -3.650 -67.329 -41.855  1.00 23.24           C  
-ATOM  23309  CE2 TYR F 508      -5.193 -66.627 -40.166  1.00 19.68           C  
-ATOM  23310  CZ  TYR F 508      -4.919 -67.337 -41.314  1.00 21.17           C  
-ATOM  23311  OH  TYR F 508      -5.924 -68.053 -41.923  1.00 25.09           O  
-ATOM  23312  N   GLN F 509      -3.702 -62.677 -40.815  1.00 18.37           N  
-ATOM  23313  CA  GLN F 509      -4.949 -61.929 -40.829  1.00 25.60           C  
-ATOM  23314  C   GLN F 509      -6.058 -62.769 -41.464  1.00 23.51           C  
-ATOM  23315  O   GLN F 509      -5.960 -63.162 -42.625  1.00 26.83           O  
-ATOM  23316  CB  GLN F 509      -4.759 -60.615 -41.588  1.00 18.88           C  
-ATOM  23317  CG  GLN F 509      -5.982 -59.730 -41.638  1.00 20.24           C  
-ATOM  23318  CD  GLN F 509      -5.699 -58.415 -42.330  1.00 24.64           C  
-ATOM  23319  OE1 GLN F 509      -4.630 -58.227 -42.906  1.00 20.20           O  
-ATOM  23320  NE2 GLN F 509      -6.652 -57.494 -42.271  1.00 33.64           N  
-ATOM  23321  N   ARG F 510      -7.105 -63.045 -40.692  1.00 20.20           N  
-ATOM  23322  CA  ARG F 510      -8.178 -63.934 -41.130  1.00 21.71           C  
-ATOM  23323  C   ARG F 510      -9.018 -63.360 -42.267  1.00 22.97           C  
-ATOM  23324  O   ARG F 510      -9.563 -64.102 -43.083  1.00 25.99           O  
-ATOM  23325  CB  ARG F 510      -9.100 -64.268 -39.956  1.00 21.13           C  
-ATOM  23326  CG  ARG F 510      -9.749 -63.045 -39.326  1.00 26.37           C  
-ATOM  23327  CD  ARG F 510     -10.849 -63.428 -38.357  1.00 24.15           C  
-ATOM  23328  NE  ARG F 510     -11.507 -62.258 -37.782  1.00 23.50           N  
-ATOM  23329  CZ  ARG F 510     -12.494 -61.591 -38.372  1.00 28.19           C  
-ATOM  23330  NH1 ARG F 510     -13.037 -60.540 -37.773  1.00 34.98           N  
-ATOM  23331  NH2 ARG F 510     -12.939 -61.971 -39.562  1.00 26.18           N  
-ATOM  23332  N   SER F 511      -9.130 -62.038 -42.311  1.00 25.35           N  
-ATOM  23333  CA  SER F 511     -10.045 -61.386 -43.233  1.00 22.07           C  
-ATOM  23334  C   SER F 511      -9.466 -60.066 -43.717  1.00 26.57           C  
-ATOM  23335  O   SER F 511      -9.124 -59.198 -42.914  1.00 32.74           O  
-ATOM  23336  CB  SER F 511     -11.398 -61.164 -42.558  1.00 26.53           C  
-ATOM  23337  OG  SER F 511     -12.341 -60.633 -43.467  1.00 34.60           O  
-ATOM  23338  N   CYS F 512      -9.368 -59.913 -45.033  1.00 23.42           N  
-ATOM  23339  CA  CYS F 512      -8.673 -58.768 -45.605  1.00 25.99           C  
-ATOM  23340  C   CYS F 512      -9.509 -57.979 -46.609  1.00 35.10           C  
-ATOM  23341  O   CYS F 512      -9.784 -58.455 -47.712  1.00 34.07           O  
-ATOM  23342  CB  CYS F 512      -7.385 -59.234 -46.283  1.00 30.12           C  
-ATOM  23343  SG  CYS F 512      -6.479 -60.496 -45.365  1.00 40.98           S  
-ATOM  23344  N   ASP F 513      -9.902 -56.768 -46.225  1.00 36.00           N  
-ATOM  23345  CA  ASP F 513     -10.489 -55.825 -47.167  1.00 26.09           C  
-ATOM  23346  C   ASP F 513      -9.370 -55.266 -48.040  1.00 28.19           C  
-ATOM  23347  O   ASP F 513      -8.719 -54.288 -47.674  1.00 30.77           O  
-ATOM  23348  CB  ASP F 513     -11.223 -54.701 -46.434  1.00 26.71           C  
-ATOM  23349  CG  ASP F 513     -12.087 -53.859 -47.358  1.00 33.84           C  
-ATOM  23350  OD1 ASP F 513     -11.855 -53.868 -48.585  1.00 38.29           O  
-ATOM  23351  OD2 ASP F 513     -13.003 -53.180 -46.850  1.00 43.02           O  
-ATOM  23352  N   VAL F 514      -9.153 -55.899 -49.188  1.00 22.19           N  
-ATOM  23353  CA  VAL F 514      -8.046 -55.550 -50.072  1.00 23.19           C  
-ATOM  23354  C   VAL F 514      -8.073 -54.087 -50.492  1.00 29.82           C  
-ATOM  23355  O   VAL F 514      -7.039 -53.419 -50.514  1.00 33.77           O  
-ATOM  23356  CB  VAL F 514      -8.047 -56.434 -51.327  1.00 24.87           C  
-ATOM  23357  CG1 VAL F 514      -6.965 -55.992 -52.304  1.00 21.05           C  
-ATOM  23358  CG2 VAL F 514      -7.856 -57.880 -50.931  1.00 24.27           C  
-ATOM  23359  N   GLY F 515      -9.261 -53.587 -50.808  1.00 33.03           N  
-ATOM  23360  CA  GLY F 515      -9.400 -52.212 -51.245  1.00 32.75           C  
-ATOM  23361  C   GLY F 515      -9.073 -51.211 -50.155  1.00 37.99           C  
-ATOM  23362  O   GLY F 515      -8.423 -50.197 -50.405  1.00 50.92           O  
-ATOM  23363  N   LEU F 516      -9.505 -51.507 -48.934  1.00 29.87           N  
-ATOM  23364  CA  LEU F 516      -9.481 -50.516 -47.866  1.00 31.74           C  
-ATOM  23365  C   LEU F 516      -8.443 -50.807 -46.786  1.00 37.08           C  
-ATOM  23366  O   LEU F 516      -7.541 -50.003 -46.551  1.00 51.24           O  
-ATOM  23367  CB  LEU F 516     -10.872 -50.415 -47.236  1.00 42.24           C  
-ATOM  23368  CG  LEU F 516     -11.375 -49.026 -46.844  1.00 37.48           C  
-ATOM  23369  CD1 LEU F 516     -10.953 -47.984 -47.866  1.00 40.01           C  
-ATOM  23370  CD2 LEU F 516     -12.889 -49.049 -46.710  1.00 34.52           C  
-ATOM  23371  N   GLY F 517      -8.574 -51.958 -46.136  1.00 34.93           N  
-ATOM  23372  CA  GLY F 517      -7.786 -52.267 -44.956  1.00 34.67           C  
-ATOM  23373  C   GLY F 517      -6.350 -52.714 -45.171  1.00 32.13           C  
-ATOM  23374  O   GLY F 517      -5.473 -52.355 -44.387  1.00 31.00           O  
-ATOM  23375  N   VAL F 518      -6.109 -53.496 -46.221  1.00 22.92           N  
-ATOM  23376  CA  VAL F 518      -4.808 -54.130 -46.444  1.00 19.18           C  
-ATOM  23377  C   VAL F 518      -3.601 -53.179 -46.423  1.00 23.07           C  
-ATOM  23378  O   VAL F 518      -2.636 -53.452 -45.705  1.00 24.21           O  
-ATOM  23379  CB  VAL F 518      -4.809 -54.927 -47.779  1.00 21.02           C  
-ATOM  23380  CG1 VAL F 518      -3.386 -55.191 -48.262  1.00 19.20           C  
-ATOM  23381  CG2 VAL F 518      -5.570 -56.221 -47.603  1.00 27.73           C  
-ATOM  23382  N   PRO F 519      -3.640 -52.066 -47.190  1.00 23.17           N  
-ATOM  23383  CA  PRO F 519      -2.471 -51.179 -47.137  1.00 24.98           C  
-ATOM  23384  C   PRO F 519      -2.211 -50.669 -45.723  1.00 26.22           C  
-ATOM  23385  O   PRO F 519      -1.070 -50.650 -45.240  1.00 25.93           O  
-ATOM  23386  CB  PRO F 519      -2.865 -50.023 -48.069  1.00 24.24           C  
-ATOM  23387  CG  PRO F 519      -3.889 -50.598 -48.969  1.00 19.19           C  
-ATOM  23388  CD  PRO F 519      -4.664 -51.541 -48.112  1.00 19.56           C  
-ATOM  23389  N   PHE F 520      -3.300 -50.267 -45.077  1.00 28.20           N  
-ATOM  23390  CA  PHE F 520      -3.290 -49.812 -43.698  1.00 26.64           C  
-ATOM  23391  C   PHE F 520      -2.624 -50.835 -42.781  1.00 27.90           C  
-ATOM  23392  O   PHE F 520      -1.802 -50.476 -41.939  1.00 25.40           O  
-ATOM  23393  CB  PHE F 520      -4.719 -49.533 -43.234  1.00 24.16           C  
-ATOM  23394  CG  PHE F 520      -4.805 -48.643 -42.033  1.00 23.25           C  
-ATOM  23395  CD1 PHE F 520      -4.861 -47.267 -42.181  1.00 20.19           C  
-ATOM  23396  CD2 PHE F 520      -4.847 -49.179 -40.757  1.00 21.05           C  
-ATOM  23397  CE1 PHE F 520      -4.952 -46.444 -41.084  1.00 14.88           C  
-ATOM  23398  CE2 PHE F 520      -4.935 -48.355 -39.653  1.00 25.02           C  
-ATOM  23399  CZ  PHE F 520      -4.992 -46.988 -39.819  1.00 19.74           C  
-ATOM  23400  N   ASN F 521      -2.971 -52.108 -42.954  1.00 29.49           N  
-ATOM  23401  CA  ASN F 521      -2.419 -53.172 -42.121  1.00 28.03           C  
-ATOM  23402  C   ASN F 521      -0.933 -53.393 -42.382  1.00 20.81           C  
-ATOM  23403  O   ASN F 521      -0.144 -53.550 -41.439  1.00 26.27           O  
-ATOM  23404  CB  ASN F 521      -3.191 -54.473 -42.340  1.00 26.31           C  
-ATOM  23405  CG  ASN F 521      -4.600 -54.417 -41.775  1.00 24.88           C  
-ATOM  23406  OD1 ASN F 521      -5.580 -54.461 -42.515  1.00 21.93           O  
-ATOM  23407  ND2 ASN F 521      -4.704 -54.315 -40.455  1.00 29.30           N  
-ATOM  23408  N   ILE F 522      -0.563 -53.407 -43.661  1.00 16.10           N  
-ATOM  23409  CA  ILE F 522       0.837 -53.472 -44.062  1.00 15.22           C  
-ATOM  23410  C   ILE F 522       1.637 -52.405 -43.332  1.00 17.60           C  
-ATOM  23411  O   ILE F 522       2.626 -52.712 -42.655  1.00 21.86           O  
-ATOM  23412  CB  ILE F 522       1.005 -53.291 -45.588  1.00 15.39           C  
-ATOM  23413  CG1 ILE F 522       0.307 -54.426 -46.341  1.00 16.49           C  
-ATOM  23414  CG2 ILE F 522       2.473 -53.237 -45.959  1.00 13.18           C  
-ATOM  23415  CD1 ILE F 522       0.407 -54.305 -47.839  1.00 13.41           C  
-ATOM  23416  N   ALA F 523       1.182 -51.160 -43.450  1.00 16.71           N  
-ATOM  23417  CA  ALA F 523       1.846 -50.038 -42.791  1.00 20.68           C  
-ATOM  23418  C   ALA F 523       1.918 -50.242 -41.282  1.00 20.67           C  
-ATOM  23419  O   ALA F 523       2.955 -49.994 -40.656  1.00 19.47           O  
-ATOM  23420  CB  ALA F 523       1.133 -48.733 -43.109  1.00 23.40           C  
-ATOM  23421  N   SER F 524       0.811 -50.702 -40.709  1.00 19.42           N  
-ATOM  23422  CA  SER F 524       0.711 -50.904 -39.271  1.00 18.17           C  
-ATOM  23423  C   SER F 524       1.747 -51.882 -38.727  1.00 21.95           C  
-ATOM  23424  O   SER F 524       2.503 -51.552 -37.810  1.00 24.21           O  
-ATOM  23425  CB  SER F 524      -0.695 -51.386 -38.908  1.00 18.67           C  
-ATOM  23426  OG  SER F 524      -0.824 -51.521 -37.506  1.00 35.27           O  
-ATOM  23427  N   TYR F 525       1.781 -53.088 -39.282  1.00 22.61           N  
-ATOM  23428  CA  TYR F 525       2.683 -54.104 -38.747  1.00 18.78           C  
-ATOM  23429  C   TYR F 525       4.129 -53.903 -39.199  1.00 21.43           C  
-ATOM  23430  O   TYR F 525       5.059 -54.329 -38.506  1.00 26.86           O  
-ATOM  23431  CB  TYR F 525       2.184 -55.504 -39.104  1.00 15.00           C  
-ATOM  23432  CG  TYR F 525       1.111 -55.961 -38.139  1.00 18.24           C  
-ATOM  23433  CD1 TYR F 525      -0.227 -55.707 -38.389  1.00 13.51           C  
-ATOM  23434  CD2 TYR F 525       1.442 -56.616 -36.958  1.00 28.65           C  
-ATOM  23435  CE1 TYR F 525      -1.206 -56.104 -37.507  1.00 17.88           C  
-ATOM  23436  CE2 TYR F 525       0.469 -57.022 -36.065  1.00 22.74           C  
-ATOM  23437  CZ  TYR F 525      -0.856 -56.762 -36.344  1.00 23.99           C  
-ATOM  23438  OH  TYR F 525      -1.835 -57.162 -35.461  1.00 25.89           O  
-ATOM  23439  N   SER F 526       4.333 -53.244 -40.337  1.00 19.17           N  
-ATOM  23440  CA  SER F 526       5.688 -52.845 -40.710  1.00 20.34           C  
-ATOM  23441  C   SER F 526       6.220 -51.862 -39.667  1.00 22.44           C  
-ATOM  23442  O   SER F 526       7.351 -51.995 -39.179  1.00 27.93           O  
-ATOM  23443  CB  SER F 526       5.720 -52.217 -42.104  1.00 18.06           C  
-ATOM  23444  OG  SER F 526       5.328 -53.146 -43.100  1.00 14.67           O  
-ATOM  23445  N   LEU F 527       5.388 -50.881 -39.326  1.00 17.82           N  
-ATOM  23446  CA  LEU F 527       5.732 -49.909 -38.296  1.00 22.85           C  
-ATOM  23447  C   LEU F 527       6.022 -50.594 -36.968  1.00 22.93           C  
-ATOM  23448  O   LEU F 527       7.009 -50.274 -36.299  1.00 22.73           O  
-ATOM  23449  CB  LEU F 527       4.608 -48.889 -38.118  1.00 20.68           C  
-ATOM  23450  CG  LEU F 527       4.859 -47.783 -37.090  1.00 13.99           C  
-ATOM  23451  CD1 LEU F 527       6.081 -46.965 -37.467  1.00 14.36           C  
-ATOM  23452  CD2 LEU F 527       3.638 -46.893 -36.964  1.00 20.07           C  
-ATOM  23453  N   LEU F 528       5.155 -51.532 -36.589  1.00 18.33           N  
-ATOM  23454  CA  LEU F 528       5.364 -52.301 -35.363  1.00 21.01           C  
-ATOM  23455  C   LEU F 528       6.731 -52.966 -35.382  1.00 21.75           C  
-ATOM  23456  O   LEU F 528       7.466 -52.915 -34.391  1.00 26.31           O  
-ATOM  23457  CB  LEU F 528       4.280 -53.368 -35.174  1.00 22.66           C  
-ATOM  23458  CG  LEU F 528       4.464 -54.282 -33.952  1.00 12.83           C  
-ATOM  23459  CD1 LEU F 528       4.461 -53.465 -32.675  1.00 14.16           C  
-ATOM  23460  CD2 LEU F 528       3.390 -55.356 -33.896  1.00 18.45           C  
-ATOM  23461  N   THR F 529       7.065 -53.587 -36.512  1.00 16.00           N  
-ATOM  23462  CA  THR F 529       8.370 -54.222 -36.674  1.00 16.01           C  
-ATOM  23463  C   THR F 529       9.494 -53.219 -36.464  1.00 17.51           C  
-ATOM  23464  O   THR F 529      10.459 -53.511 -35.765  1.00 22.46           O  
-ATOM  23465  CB  THR F 529       8.532 -54.865 -38.061  1.00 19.76           C  
-ATOM  23466  OG1 THR F 529       7.466 -55.793 -38.284  1.00 20.24           O  
-ATOM  23467  CG2 THR F 529       9.862 -55.602 -38.150  1.00 17.47           C  
-ATOM  23468  N   LEU F 530       9.362 -52.041 -37.067  1.00 16.06           N  
-ATOM  23469  CA  LEU F 530      10.338 -50.970 -36.875  1.00 18.14           C  
-ATOM  23470  C   LEU F 530      10.551 -50.644 -35.394  1.00 22.16           C  
-ATOM  23471  O   LEU F 530      11.689 -50.632 -34.902  1.00 19.86           O  
-ATOM  23472  CB  LEU F 530       9.901 -49.709 -37.622  1.00 15.68           C  
-ATOM  23473  CG  LEU F 530      10.670 -49.339 -38.888  1.00 16.01           C  
-ATOM  23474  CD1 LEU F 530      10.622 -50.478 -39.882  1.00 16.61           C  
-ATOM  23475  CD2 LEU F 530      10.100 -48.068 -39.494  1.00 15.60           C  
-ATOM  23476  N   MET F 531       9.450 -50.388 -34.691  1.00 21.39           N  
-ATOM  23477  CA  MET F 531       9.504 -50.021 -33.278  1.00 18.96           C  
-ATOM  23478  C   MET F 531      10.152 -51.108 -32.417  1.00 20.77           C  
-ATOM  23479  O   MET F 531      11.092 -50.835 -31.654  1.00 23.84           O  
-ATOM  23480  CB  MET F 531       8.095 -49.712 -32.772  1.00 19.82           C  
-ATOM  23481  CG  MET F 531       7.392 -48.625 -33.574  1.00 21.05           C  
-ATOM  23482  SD  MET F 531       5.627 -48.484 -33.232  1.00 20.33           S  
-ATOM  23483  CE  MET F 531       5.652 -47.924 -31.536  1.00 13.50           C  
-ATOM  23484  N   VAL F 532       9.650 -52.334 -32.544  1.00 21.77           N  
-ATOM  23485  CA  VAL F 532      10.194 -53.460 -31.788  1.00 21.89           C  
-ATOM  23486  C   VAL F 532      11.692 -53.649 -32.068  1.00 24.58           C  
-ATOM  23487  O   VAL F 532      12.492 -53.835 -31.138  1.00 17.37           O  
-ATOM  23488  CB  VAL F 532       9.442 -54.767 -32.104  1.00 15.34           C  
-ATOM  23489  CG1 VAL F 532      10.081 -55.924 -31.382  1.00 18.23           C  
-ATOM  23490  CG2 VAL F 532       7.978 -54.646 -31.714  1.00 11.63           C  
-ATOM  23491  N   ALA F 533      12.064 -53.588 -33.346  1.00 21.03           N  
-ATOM  23492  CA  ALA F 533      13.464 -53.687 -33.742  1.00 18.32           C  
-ATOM  23493  C   ALA F 533      14.292 -52.627 -33.031  1.00 20.83           C  
-ATOM  23494  O   ALA F 533      15.371 -52.921 -32.498  1.00 28.61           O  
-ATOM  23495  CB  ALA F 533      13.609 -53.552 -35.252  1.00 19.33           C  
-ATOM  23496  N   HIS F 534      13.783 -51.396 -33.000  1.00 20.53           N  
-ATOM  23497  CA  HIS F 534      14.518 -50.333 -32.322  1.00 27.10           C  
-ATOM  23498  C   HIS F 534      14.680 -50.600 -30.831  1.00 23.67           C  
-ATOM  23499  O   HIS F 534      15.785 -50.467 -30.302  1.00 24.02           O  
-ATOM  23500  CB  HIS F 534      13.857 -48.971 -32.499  1.00 21.94           C  
-ATOM  23501  CG  HIS F 534      14.540 -47.886 -31.726  1.00 22.47           C  
-ATOM  23502  ND1 HIS F 534      14.023 -47.358 -30.562  1.00 31.96           N  
-ATOM  23503  CD2 HIS F 534      15.731 -47.269 -31.921  1.00 23.34           C  
-ATOM  23504  CE1 HIS F 534      14.852 -46.443 -30.088  1.00 30.99           C  
-ATOM  23505  NE2 HIS F 534      15.895 -46.371 -30.894  1.00 34.17           N  
-ATOM  23506  N   VAL F 535      13.599 -50.971 -30.144  1.00 24.51           N  
-ATOM  23507  CA  VAL F 535      13.715 -51.200 -28.701  1.00 22.37           C  
-ATOM  23508  C   VAL F 535      14.430 -52.514 -28.381  1.00 23.93           C  
-ATOM  23509  O   VAL F 535      14.663 -52.826 -27.215  1.00 20.64           O  
-ATOM  23510  CB  VAL F 535      12.341 -51.194 -27.988  1.00 19.37           C  
-ATOM  23511  CG1 VAL F 535      11.675 -49.838 -28.126  1.00 18.32           C  
-ATOM  23512  CG2 VAL F 535      11.438 -52.305 -28.513  1.00 19.04           C  
-ATOM  23513  N   CYS F 536      14.784 -53.279 -29.410  1.00 25.23           N  
-ATOM  23514  CA  CYS F 536      15.537 -54.512 -29.195  1.00 25.21           C  
-ATOM  23515  C   CYS F 536      16.941 -54.466 -29.792  1.00 23.31           C  
-ATOM  23516  O   CYS F 536      17.659 -55.467 -29.760  1.00 26.96           O  
-ATOM  23517  CB  CYS F 536      14.783 -55.707 -29.774  1.00 20.85           C  
-ATOM  23518  SG  CYS F 536      13.245 -56.109 -28.926  1.00 22.52           S  
-ATOM  23519  N   ASN F 537      17.316 -53.310 -30.339  1.00 30.54           N  
-ATOM  23520  CA  ASN F 537      18.627 -53.119 -30.967  1.00 36.62           C  
-ATOM  23521  C   ASN F 537      18.809 -54.027 -32.175  1.00 33.13           C  
-ATOM  23522  O   ASN F 537      19.928 -54.412 -32.517  1.00 32.24           O  
-ATOM  23523  CB  ASN F 537      19.762 -53.356 -29.966  1.00 38.22           C  
-ATOM  23524  CG  ASN F 537      19.775 -52.337 -28.848  1.00 59.08           C  
-ATOM  23525  OD1 ASN F 537      19.141 -52.528 -27.810  1.00 69.91           O  
-ATOM  23526  ND2 ASN F 537      20.504 -51.246 -29.053  1.00 47.28           N  
-ATOM  23527  N   LEU F 538      17.696 -54.366 -32.813  1.00 25.23           N  
-ATOM  23528  CA  LEU F 538      17.724 -55.157 -34.030  1.00 21.13           C  
-ATOM  23529  C   LEU F 538      17.449 -54.260 -35.224  1.00 21.93           C  
-ATOM  23530  O   LEU F 538      16.863 -53.186 -35.080  1.00 24.39           O  
-ATOM  23531  CB  LEU F 538      16.698 -56.286 -33.962  1.00 20.20           C  
-ATOM  23532  CG  LEU F 538      16.801 -57.181 -32.728  1.00 18.80           C  
-ATOM  23533  CD1 LEU F 538      15.614 -58.123 -32.650  1.00 16.01           C  
-ATOM  23534  CD2 LEU F 538      18.106 -57.957 -32.763  1.00 19.72           C  
-ATOM  23535  N   LYS F 539      17.884 -54.697 -36.399  1.00 21.66           N  
-ATOM  23536  CA  LYS F 539      17.641 -53.951 -37.624  1.00 19.23           C  
-ATOM  23537  C   LYS F 539      16.436 -54.537 -38.341  1.00 24.72           C  
-ATOM  23538  O   LYS F 539      16.385 -55.744 -38.584  1.00 27.95           O  
-ATOM  23539  CB  LYS F 539      18.874 -53.983 -38.527  1.00 21.06           C  
-ATOM  23540  CG  LYS F 539      20.143 -53.482 -37.850  1.00 24.71           C  
-ATOM  23541  CD  LYS F 539      21.391 -53.873 -38.630  1.00 29.19           C  
-ATOM  23542  CE  LYS F 539      22.082 -55.087 -38.018  1.00 27.50           C  
-ATOM  23543  NZ  LYS F 539      23.170 -55.599 -38.904  1.00 27.86           N  
-ATOM  23544  N   PRO F 540      15.450 -53.690 -38.667  1.00 17.05           N  
-ATOM  23545  CA  PRO F 540      14.267 -54.180 -39.375  1.00 15.42           C  
-ATOM  23546  C   PRO F 540      14.648 -54.718 -40.746  1.00 21.17           C  
-ATOM  23547  O   PRO F 540      15.409 -54.077 -41.470  1.00 26.56           O  
-ATOM  23548  CB  PRO F 540      13.378 -52.939 -39.482  1.00 16.04           C  
-ATOM  23549  CG  PRO F 540      14.311 -51.788 -39.365  1.00 15.52           C  
-ATOM  23550  CD  PRO F 540      15.390 -52.239 -38.428  1.00 21.31           C  
-ATOM  23551  N   LYS F 541      14.139 -55.897 -41.083  1.00 20.36           N  
-ATOM  23552  CA  LYS F 541      14.507 -56.550 -42.331  1.00 26.92           C  
-ATOM  23553  C   LYS F 541      13.308 -56.781 -43.242  1.00 26.43           C  
-ATOM  23554  O   LYS F 541      13.358 -56.461 -44.429  1.00 26.24           O  
-ATOM  23555  CB  LYS F 541      15.205 -57.884 -42.048  1.00 30.41           C  
-ATOM  23556  CG  LYS F 541      15.561 -58.680 -43.299  1.00 25.47           C  
-ATOM  23557  CD  LYS F 541      16.160 -60.034 -42.943  1.00 30.61           C  
-ATOM  23558  CE  LYS F 541      16.269 -60.938 -44.163  1.00 38.98           C  
-ATOM  23559  NZ  LYS F 541      17.183 -60.375 -45.191  1.00 45.35           N  
-ATOM  23560  N   GLU F 542      12.228 -57.324 -42.690  1.00 22.35           N  
-ATOM  23561  CA  GLU F 542      11.120 -57.763 -43.528  1.00 22.01           C  
-ATOM  23562  C   GLU F 542       9.796 -57.870 -42.782  1.00 21.92           C  
-ATOM  23563  O   GLU F 542       9.758 -58.208 -41.599  1.00 18.00           O  
-ATOM  23564  CB  GLU F 542      11.464 -59.116 -44.152  1.00 35.31           C  
-ATOM  23565  CG  GLU F 542      10.766 -59.412 -45.465  1.00 34.84           C  
-ATOM  23566  CD  GLU F 542      11.293 -60.676 -46.113  1.00 48.29           C  
-ATOM  23567  OE1 GLU F 542      11.167 -60.813 -47.349  1.00 46.52           O  
-ATOM  23568  OE2 GLU F 542      11.833 -61.535 -45.380  1.00 37.98           O  
-ATOM  23569  N   PHE F 543       8.710 -57.575 -43.490  1.00 23.48           N  
-ATOM  23570  CA  PHE F 543       7.370 -57.863 -43.000  1.00 16.35           C  
-ATOM  23571  C   PHE F 543       6.688 -58.880 -43.900  1.00 16.35           C  
-ATOM  23572  O   PHE F 543       6.494 -58.638 -45.092  1.00 16.87           O  
-ATOM  23573  CB  PHE F 543       6.516 -56.602 -42.926  1.00 11.92           C  
-ATOM  23574  CG  PHE F 543       5.048 -56.887 -42.786  1.00 11.69           C  
-ATOM  23575  CD1 PHE F 543       4.565 -57.549 -41.670  1.00 15.16           C  
-ATOM  23576  CD2 PHE F 543       4.152 -56.504 -43.769  1.00 12.93           C  
-ATOM  23577  CE1 PHE F 543       3.218 -57.823 -41.534  1.00 14.46           C  
-ATOM  23578  CE2 PHE F 543       2.801 -56.773 -43.638  1.00 12.99           C  
-ATOM  23579  CZ  PHE F 543       2.334 -57.434 -42.519  1.00 14.36           C  
-ATOM  23580  N   ILE F 544       6.319 -60.016 -43.320  1.00 15.15           N  
-ATOM  23581  CA  ILE F 544       5.638 -61.062 -44.065  1.00 14.13           C  
-ATOM  23582  C   ILE F 544       4.147 -61.073 -43.742  1.00 17.43           C  
-ATOM  23583  O   ILE F 544       3.741 -61.216 -42.588  1.00 15.05           O  
-ATOM  23584  CB  ILE F 544       6.247 -62.438 -43.772  1.00 16.61           C  
-ATOM  23585  CG1 ILE F 544       7.763 -62.385 -43.969  1.00 21.93           C  
-ATOM  23586  CG2 ILE F 544       5.611 -63.502 -44.658  1.00 13.37           C  
-ATOM  23587  CD1 ILE F 544       8.486 -63.639 -43.544  1.00 25.99           C  
-ATOM  23588  N   HIS F 545       3.341 -60.917 -44.784  1.00 15.13           N  
-ATOM  23589  CA  HIS F 545       1.900 -60.781 -44.653  1.00 14.44           C  
-ATOM  23590  C   HIS F 545       1.170 -62.034 -45.131  1.00 19.23           C  
-ATOM  23591  O   HIS F 545       1.128 -62.324 -46.336  1.00 25.27           O  
-ATOM  23592  CB  HIS F 545       1.425 -59.560 -45.439  1.00 16.75           C  
-ATOM  23593  CG  HIS F 545       0.049 -59.100 -45.079  1.00 20.97           C  
-ATOM  23594  ND1 HIS F 545      -0.748 -59.765 -44.167  1.00 16.82           N  
-ATOM  23595  CD2 HIS F 545      -0.677 -58.040 -45.503  1.00 19.66           C  
-ATOM  23596  CE1 HIS F 545      -1.899 -59.135 -44.051  1.00 17.39           C  
-ATOM  23597  NE2 HIS F 545      -1.884 -58.082 -44.851  1.00 19.36           N  
-ATOM  23598  N   PHE F 546       0.603 -62.768 -44.176  1.00 12.53           N  
-ATOM  23599  CA  PHE F 546      -0.190 -63.959 -44.465  1.00 14.25           C  
-ATOM  23600  C   PHE F 546      -1.683 -63.652 -44.394  1.00 16.73           C  
-ATOM  23601  O   PHE F 546      -2.173 -63.142 -43.388  1.00 19.85           O  
-ATOM  23602  CB  PHE F 546       0.161 -65.087 -43.495  1.00 18.43           C  
-ATOM  23603  CG  PHE F 546       1.423 -65.819 -43.849  1.00 24.88           C  
-ATOM  23604  CD1 PHE F 546       2.095 -65.536 -45.026  1.00 24.27           C  
-ATOM  23605  CD2 PHE F 546       1.928 -66.802 -43.014  1.00 22.17           C  
-ATOM  23606  CE1 PHE F 546       3.251 -66.212 -45.358  1.00 21.99           C  
-ATOM  23607  CE2 PHE F 546       3.084 -67.482 -43.342  1.00 15.72           C  
-ATOM  23608  CZ  PHE F 546       3.745 -67.187 -44.516  1.00 18.38           C  
-ATOM  23609  N   MET F 547      -2.402 -63.971 -45.466  1.00 17.20           N  
-ATOM  23610  CA  MET F 547      -3.800 -63.573 -45.596  1.00 13.86           C  
-ATOM  23611  C   MET F 547      -4.722 -64.771 -45.818  1.00 19.78           C  
-ATOM  23612  O   MET F 547      -4.465 -65.609 -46.681  1.00 24.30           O  
-ATOM  23613  CB  MET F 547      -3.945 -62.580 -46.748  1.00 14.79           C  
-ATOM  23614  CG  MET F 547      -2.802 -61.574 -46.813  1.00 26.43           C  
-ATOM  23615  SD  MET F 547      -2.765 -60.566 -48.306  1.00 24.06           S  
-ATOM  23616  CE  MET F 547      -4.191 -59.525 -48.033  1.00 24.52           C  
-ATOM  23617  N   GLY F 548      -5.795 -64.848 -45.035  1.00 21.51           N  
-ATOM  23618  CA  GLY F 548      -6.756 -65.932 -45.155  1.00 21.78           C  
-ATOM  23619  C   GLY F 548      -7.840 -65.648 -46.179  1.00 24.53           C  
-ATOM  23620  O   GLY F 548      -7.647 -65.858 -47.378  1.00 20.15           O  
-ATOM  23621  N   ASN F 549      -8.993 -65.181 -45.708  1.00 21.96           N  
-ATOM  23622  CA  ASN F 549     -10.061 -64.763 -46.609  1.00 25.70           C  
-ATOM  23623  C   ASN F 549      -9.717 -63.413 -47.228  1.00 24.20           C  
-ATOM  23624  O   ASN F 549      -9.891 -62.368 -46.602  1.00 30.12           O  
-ATOM  23625  CB  ASN F 549     -11.402 -64.695 -45.870  1.00 30.01           C  
-ATOM  23626  CG  ASN F 549     -12.591 -64.578 -46.814  1.00 30.24           C  
-ATOM  23627  OD1 ASN F 549     -12.644 -63.690 -47.665  1.00 29.05           O  
-ATOM  23628  ND2 ASN F 549     -13.552 -65.483 -46.665  1.00 25.81           N  
-ATOM  23629  N   THR F 550      -9.220 -63.444 -48.459  1.00 15.86           N  
-ATOM  23630  CA  THR F 550      -8.774 -62.232 -49.133  1.00 20.28           C  
-ATOM  23631  C   THR F 550      -9.823 -61.766 -50.134  1.00 27.72           C  
-ATOM  23632  O   THR F 550      -9.953 -62.335 -51.217  1.00 40.15           O  
-ATOM  23633  CB  THR F 550      -7.435 -62.463 -49.849  1.00 19.85           C  
-ATOM  23634  OG1 THR F 550      -6.600 -63.297 -49.036  1.00 26.44           O  
-ATOM  23635  CG2 THR F 550      -6.731 -61.147 -50.103  1.00 20.48           C  
-ATOM  23636  N   HIS F 551     -10.568 -60.726 -49.775  1.00 19.92           N  
-ATOM  23637  CA  HIS F 551     -11.726 -60.327 -50.567  1.00 23.39           C  
-ATOM  23638  C   HIS F 551     -11.689 -58.879 -51.040  1.00 26.62           C  
-ATOM  23639  O   HIS F 551     -11.103 -58.012 -50.394  1.00 32.20           O  
-ATOM  23640  CB  HIS F 551     -13.005 -60.557 -49.763  1.00 26.55           C  
-ATOM  23641  CG  HIS F 551     -12.992 -59.903 -48.417  1.00 30.14           C  
-ATOM  23642  ND1 HIS F 551     -12.549 -60.547 -47.283  1.00 27.88           N  
-ATOM  23643  CD2 HIS F 551     -13.355 -58.658 -48.026  1.00 30.03           C  
-ATOM  23644  CE1 HIS F 551     -12.643 -59.729 -46.250  1.00 25.93           C  
-ATOM  23645  NE2 HIS F 551     -13.130 -58.577 -46.673  1.00 23.46           N  
-ATOM  23646  N   VAL F 552     -12.332 -58.638 -52.178  1.00 27.11           N  
-ATOM  23647  CA  VAL F 552     -12.537 -57.297 -52.702  1.00 19.76           C  
-ATOM  23648  C   VAL F 552     -14.034 -57.012 -52.760  1.00 26.12           C  
-ATOM  23649  O   VAL F 552     -14.783 -57.749 -53.405  1.00 26.57           O  
-ATOM  23650  CB  VAL F 552     -11.922 -57.135 -54.104  1.00 12.06           C  
-ATOM  23651  CG1 VAL F 552     -12.469 -55.898 -54.785  1.00 17.59           C  
-ATOM  23652  CG2 VAL F 552     -10.409 -57.082 -54.018  1.00 15.30           C  
-ATOM  23653  N   TYR F 553     -14.472 -55.958 -52.078  1.00 29.05           N  
-ATOM  23654  CA  TYR F 553     -15.892 -55.620 -52.049  1.00 30.21           C  
-ATOM  23655  C   TYR F 553     -16.351 -55.124 -53.412  1.00 29.13           C  
-ATOM  23656  O   TYR F 553     -15.646 -54.369 -54.082  1.00 32.35           O  
-ATOM  23657  CB  TYR F 553     -16.184 -54.583 -50.960  1.00 28.80           C  
-ATOM  23658  CG  TYR F 553     -16.232 -55.194 -49.578  1.00 33.47           C  
-ATOM  23659  CD1 TYR F 553     -17.345 -55.908 -49.158  1.00 38.04           C  
-ATOM  23660  CD2 TYR F 553     -15.160 -55.078 -48.704  1.00 31.27           C  
-ATOM  23661  CE1 TYR F 553     -17.395 -56.483 -47.902  1.00 36.31           C  
-ATOM  23662  CE2 TYR F 553     -15.201 -55.650 -47.444  1.00 31.64           C  
-ATOM  23663  CZ  TYR F 553     -16.322 -56.352 -47.050  1.00 27.74           C  
-ATOM  23664  OH  TYR F 553     -16.377 -56.926 -45.802  1.00 24.40           O  
-ATOM  23665  N   THR F 554     -17.536 -55.570 -53.814  1.00 31.35           N  
-ATOM  23666  CA  THR F 554     -18.070 -55.290 -55.143  1.00 40.01           C  
-ATOM  23667  C   THR F 554     -18.161 -53.797 -55.465  1.00 35.86           C  
-ATOM  23668  O   THR F 554     -17.966 -53.395 -56.611  1.00 35.53           O  
-ATOM  23669  CB  THR F 554     -19.467 -55.920 -55.317  1.00 39.98           C  
-ATOM  23670  OG1 THR F 554     -20.245 -55.691 -54.136  1.00 39.85           O  
-ATOM  23671  CG2 THR F 554     -19.351 -57.418 -55.550  1.00 29.11           C  
-ATOM  23672  N   ASN F 555     -18.449 -52.978 -54.458  1.00 31.58           N  
-ATOM  23673  CA  ASN F 555     -18.577 -51.541 -54.673  1.00 26.61           C  
-ATOM  23674  C   ASN F 555     -17.227 -50.819 -54.667  1.00 34.79           C  
-ATOM  23675  O   ASN F 555     -17.175 -49.588 -54.680  1.00 41.79           O  
-ATOM  23676  CB  ASN F 555     -19.510 -50.930 -53.621  1.00 36.49           C  
-ATOM  23677  CG  ASN F 555     -19.004 -51.117 -52.200  1.00 37.93           C  
-ATOM  23678  OD1 ASN F 555     -18.205 -52.010 -51.921  1.00 47.64           O  
-ATOM  23679  ND2 ASN F 555     -19.478 -50.275 -51.290  1.00 29.55           N  
-ATOM  23680  N   HIS F 556     -16.141 -51.588 -54.660  1.00 33.96           N  
-ATOM  23681  CA  HIS F 556     -14.789 -51.031 -54.676  1.00 36.80           C  
-ATOM  23682  C   HIS F 556     -14.091 -51.273 -56.008  1.00 32.95           C  
-ATOM  23683  O   HIS F 556     -13.077 -50.643 -56.314  1.00 30.28           O  
-ATOM  23684  CB  HIS F 556     -13.942 -51.634 -53.554  1.00 28.27           C  
-ATOM  23685  CG  HIS F 556     -14.340 -51.185 -52.184  1.00 28.63           C  
-ATOM  23686  ND1 HIS F 556     -13.643 -51.552 -51.053  1.00 40.44           N  
-ATOM  23687  CD2 HIS F 556     -15.357 -50.399 -51.762  1.00 31.67           C  
-ATOM  23688  CE1 HIS F 556     -14.215 -51.012 -49.992  1.00 46.44           C  
-ATOM  23689  NE2 HIS F 556     -15.258 -50.308 -50.394  1.00 50.86           N  
-ATOM  23690  N   VAL F 557     -14.648 -52.195 -56.786  1.00 25.76           N  
-ATOM  23691  CA  VAL F 557     -13.995 -52.733 -57.973  1.00 26.25           C  
-ATOM  23692  C   VAL F 557     -13.585 -51.682 -59.002  1.00 32.70           C  
-ATOM  23693  O   VAL F 557     -12.477 -51.730 -59.540  1.00 35.78           O  
-ATOM  23694  CB  VAL F 557     -14.906 -53.767 -58.658  1.00 32.51           C  
-ATOM  23695  CG1 VAL F 557     -14.300 -54.221 -59.974  1.00 23.09           C  
-ATOM  23696  CG2 VAL F 557     -15.151 -54.948 -57.729  1.00 26.62           C  
-ATOM  23697  N   GLU F 558     -14.475 -50.735 -59.272  1.00 38.50           N  
-ATOM  23698  CA  GLU F 558     -14.198 -49.702 -60.259  1.00 38.20           C  
-ATOM  23699  C   GLU F 558     -13.049 -48.808 -59.798  1.00 39.68           C  
-ATOM  23700  O   GLU F 558     -12.113 -48.545 -60.555  1.00 44.08           O  
-ATOM  23701  CB  GLU F 558     -15.454 -48.871 -60.528  1.00 37.07           C  
-ATOM  23702  CG  GLU F 558     -15.559 -48.373 -61.952  1.00 59.90           C  
-ATOM  23703  CD  GLU F 558     -15.585 -49.511 -62.959  1.00 65.85           C  
-ATOM  23704  OE1 GLU F 558     -16.519 -50.340 -62.894  1.00 53.25           O  
-ATOM  23705  OE2 GLU F 558     -14.669 -49.585 -63.807  1.00 67.46           O  
-ATOM  23706  N   ALA F 559     -13.126 -48.357 -58.550  1.00 34.60           N  
-ATOM  23707  CA  ALA F 559     -12.091 -47.516 -57.966  1.00 31.10           C  
-ATOM  23708  C   ALA F 559     -10.745 -48.232 -57.983  1.00 37.98           C  
-ATOM  23709  O   ALA F 559      -9.714 -47.626 -58.276  1.00 38.40           O  
-ATOM  23710  CB  ALA F 559     -12.467 -47.122 -56.550  1.00 30.97           C  
-ATOM  23711  N   LEU F 560     -10.765 -49.524 -57.672  1.00 40.27           N  
-ATOM  23712  CA  LEU F 560      -9.559 -50.337 -57.714  1.00 30.73           C  
-ATOM  23713  C   LEU F 560      -9.022 -50.436 -59.130  1.00 32.17           C  
-ATOM  23714  O   LEU F 560      -7.811 -50.482 -59.341  1.00 36.98           O  
-ATOM  23715  CB  LEU F 560      -9.832 -51.733 -57.160  1.00 21.51           C  
-ATOM  23716  CG  LEU F 560     -10.083 -51.772 -55.655  1.00 21.30           C  
-ATOM  23717  CD1 LEU F 560     -10.232 -53.196 -55.171  1.00 24.36           C  
-ATOM  23718  CD2 LEU F 560      -8.956 -51.075 -54.924  1.00 28.82           C  
-ATOM  23719  N   LYS F 561      -9.930 -50.473 -60.099  1.00 31.24           N  
-ATOM  23720  CA  LYS F 561      -9.544 -50.542 -61.500  1.00 31.75           C  
-ATOM  23721  C   LYS F 561      -8.913 -49.227 -61.928  1.00 38.20           C  
-ATOM  23722  O   LYS F 561      -8.074 -49.190 -62.828  1.00 36.51           O  
-ATOM  23723  CB  LYS F 561     -10.753 -50.884 -62.373  1.00 33.66           C  
-ATOM  23724  CG  LYS F 561     -11.112 -52.360 -62.333  1.00 37.75           C  
-ATOM  23725  CD  LYS F 561     -12.537 -52.640 -62.790  1.00 49.75           C  
-ATOM  23726  CE  LYS F 561     -12.702 -52.473 -64.291  1.00 57.74           C  
-ATOM  23727  NZ  LYS F 561     -14.086 -52.834 -64.718  1.00 44.76           N  
-ATOM  23728  N   GLU F 562      -9.322 -48.148 -61.271  1.00 37.15           N  
-ATOM  23729  CA  GLU F 562      -8.671 -46.864 -61.466  1.00 40.26           C  
-ATOM  23730  C   GLU F 562      -7.273 -46.909 -60.861  1.00 38.03           C  
-ATOM  23731  O   GLU F 562      -6.308 -46.447 -61.469  1.00 32.93           O  
-ATOM  23732  CB  GLU F 562      -9.492 -45.731 -60.841  1.00 35.96           C  
-ATOM  23733  CG  GLU F 562     -10.669 -45.248 -61.683  1.00 54.04           C  
-ATOM  23734  CD  GLU F 562     -10.266 -44.240 -62.750  1.00 64.53           C  
-ATOM  23735  OE1 GLU F 562      -9.135 -44.329 -63.274  1.00 64.51           O  
-ATOM  23736  OE2 GLU F 562     -11.088 -43.351 -63.064  1.00 61.04           O  
-ATOM  23737  N   GLN F 563      -7.175 -47.482 -59.664  1.00 42.25           N  
-ATOM  23738  CA  GLN F 563      -5.914 -47.561 -58.936  1.00 31.56           C  
-ATOM  23739  C   GLN F 563      -4.883 -48.409 -59.675  1.00 29.59           C  
-ATOM  23740  O   GLN F 563      -3.682 -48.169 -59.572  1.00 34.39           O  
-ATOM  23741  CB  GLN F 563      -6.146 -48.126 -57.529  1.00 23.78           C  
-ATOM  23742  CG  GLN F 563      -4.956 -47.956 -56.585  1.00 23.19           C  
-ATOM  23743  CD  GLN F 563      -5.231 -48.476 -55.181  1.00 24.80           C  
-ATOM  23744  OE1 GLN F 563      -6.371 -48.784 -54.828  1.00 24.94           O  
-ATOM  23745  NE2 GLN F 563      -4.182 -48.575 -54.374  1.00 18.24           N  
-ATOM  23746  N   LEU F 564      -5.355 -49.397 -60.427  1.00 26.19           N  
-ATOM  23747  CA  LEU F 564      -4.460 -50.327 -61.105  1.00 24.27           C  
-ATOM  23748  C   LEU F 564      -3.816 -49.702 -62.334  1.00 33.50           C  
-ATOM  23749  O   LEU F 564      -2.881 -50.267 -62.901  1.00 47.82           O  
-ATOM  23750  CB  LEU F 564      -5.205 -51.604 -61.503  1.00 32.27           C  
-ATOM  23751  CG  LEU F 564      -5.473 -52.674 -60.439  1.00 28.82           C  
-ATOM  23752  CD1 LEU F 564      -4.796 -53.975 -60.827  1.00 30.80           C  
-ATOM  23753  CD2 LEU F 564      -5.026 -52.239 -59.051  1.00 32.53           C  
-ATOM  23754  N   ARG F 565      -4.317 -48.542 -62.748  1.00 33.58           N  
-ATOM  23755  CA  ARG F 565      -3.738 -47.827 -63.882  1.00 35.72           C  
-ATOM  23756  C   ARG F 565      -2.628 -46.886 -63.427  1.00 30.89           C  
-ATOM  23757  O   ARG F 565      -2.060 -46.139 -64.228  1.00 28.41           O  
-ATOM  23758  CB  ARG F 565      -4.810 -47.038 -64.632  1.00 34.08           C  
-ATOM  23759  CG  ARG F 565      -5.823 -47.898 -65.363  1.00 39.78           C  
-ATOM  23760  CD  ARG F 565      -6.748 -47.039 -66.210  1.00 43.53           C  
-ATOM  23761  NE  ARG F 565      -7.827 -47.819 -66.810  1.00 70.30           N  
-ATOM  23762  CZ  ARG F 565      -9.023 -47.987 -66.255  1.00 70.40           C  
-ATOM  23763  NH1 ARG F 565      -9.296 -47.428 -65.083  1.00 49.49           N  
-ATOM  23764  NH2 ARG F 565      -9.948 -48.711 -66.871  1.00 68.31           N  
-ATOM  23765  N   ARG F 566      -2.323 -46.932 -62.135  1.00 27.01           N  
-ATOM  23766  CA  ARG F 566      -1.335 -46.040 -61.547  1.00 22.36           C  
-ATOM  23767  C   ARG F 566       0.004 -46.734 -61.323  1.00 23.46           C  
-ATOM  23768  O   ARG F 566       0.095 -47.713 -60.583  1.00 23.52           O  
-ATOM  23769  CB  ARG F 566      -1.856 -45.476 -60.223  1.00 20.44           C  
-ATOM  23770  CG  ARG F 566      -3.162 -44.709 -60.344  1.00 23.32           C  
-ATOM  23771  CD  ARG F 566      -3.546 -44.071 -59.021  1.00 27.98           C  
-ATOM  23772  NE  ARG F 566      -4.728 -43.219 -59.130  1.00 31.20           N  
-ATOM  23773  CZ  ARG F 566      -5.245 -42.530 -58.118  1.00 29.45           C  
-ATOM  23774  NH1 ARG F 566      -6.322 -41.779 -58.302  1.00 28.53           N  
-ATOM  23775  NH2 ARG F 566      -4.688 -42.594 -56.917  1.00 26.31           N  
-ATOM  23776  N   GLU F 567       1.041 -46.215 -61.970  1.00 25.78           N  
-ATOM  23777  CA  GLU F 567       2.397 -46.707 -61.765  1.00 24.93           C  
-ATOM  23778  C   GLU F 567       2.927 -46.267 -60.406  1.00 23.46           C  
-ATOM  23779  O   GLU F 567       2.917 -45.079 -60.084  1.00 26.90           O  
-ATOM  23780  CB  GLU F 567       3.323 -46.215 -62.876  1.00 25.89           C  
-ATOM  23781  CG  GLU F 567       2.870 -44.920 -63.525  1.00 37.66           C  
-ATOM  23782  CD  GLU F 567       2.118 -45.159 -64.819  1.00 40.56           C  
-ATOM  23783  OE1 GLU F 567       1.220 -44.356 -65.149  1.00 31.40           O  
-ATOM  23784  OE2 GLU F 567       2.433 -46.151 -65.510  1.00 42.28           O  
-ATOM  23785  N   PRO F 568       3.396 -47.233 -59.607  1.00 20.13           N  
-ATOM  23786  CA  PRO F 568       3.868 -46.991 -58.240  1.00 21.57           C  
-ATOM  23787  C   PRO F 568       5.033 -46.008 -58.173  1.00 27.31           C  
-ATOM  23788  O   PRO F 568       5.855 -45.943 -59.089  1.00 28.23           O  
-ATOM  23789  CB  PRO F 568       4.311 -48.381 -57.772  1.00 21.45           C  
-ATOM  23790  CG  PRO F 568       3.571 -49.331 -58.647  1.00 23.44           C  
-ATOM  23791  CD  PRO F 568       3.490 -48.654 -59.974  1.00 19.27           C  
-ATOM  23792  N   ARG F 569       5.089 -45.248 -57.084  1.00 29.04           N  
-ATOM  23793  CA  ARG F 569       6.179 -44.312 -56.843  1.00 23.65           C  
-ATOM  23794  C   ARG F 569       7.131 -44.882 -55.787  1.00 24.66           C  
-ATOM  23795  O   ARG F 569       6.788 -45.851 -55.108  1.00 25.72           O  
-ATOM  23796  CB  ARG F 569       5.618 -42.955 -56.408  1.00 25.10           C  
-ATOM  23797  CG  ARG F 569       4.640 -42.356 -57.403  1.00 31.74           C  
-ATOM  23798  CD  ARG F 569       5.039 -40.945 -57.814  1.00 25.13           C  
-ATOM  23799  NE  ARG F 569       4.105 -40.388 -58.788  1.00 25.81           N  
-ATOM  23800  CZ  ARG F 569       2.944 -39.826 -58.470  1.00 25.17           C  
-ATOM  23801  NH1 ARG F 569       2.152 -39.346 -59.419  1.00 24.54           N  
-ATOM  23802  NH2 ARG F 569       2.573 -39.745 -57.200  1.00 27.41           N  
-ATOM  23803  N   PRO F 570       8.339 -44.305 -55.663  1.00 20.27           N  
-ATOM  23804  CA  PRO F 570       9.274 -44.759 -54.629  1.00 18.22           C  
-ATOM  23805  C   PRO F 570       8.674 -44.772 -53.228  1.00 16.21           C  
-ATOM  23806  O   PRO F 570       8.063 -43.790 -52.812  1.00 17.62           O  
-ATOM  23807  CB  PRO F 570      10.404 -43.733 -54.710  1.00 19.73           C  
-ATOM  23808  CG  PRO F 570      10.398 -43.293 -56.113  1.00 23.45           C  
-ATOM  23809  CD  PRO F 570       8.972 -43.346 -56.586  1.00 24.07           C  
-ATOM  23810  N   PHE F 571       8.837 -45.888 -52.526  1.00 20.39           N  
-ATOM  23811  CA  PHE F 571       8.489 -45.960 -51.115  1.00 16.70           C  
-ATOM  23812  C   PHE F 571       9.242 -44.879 -50.354  1.00 18.75           C  
-ATOM  23813  O   PHE F 571      10.393 -44.577 -50.672  1.00 18.43           O  
-ATOM  23814  CB  PHE F 571       8.825 -47.338 -50.536  1.00 19.61           C  
-ATOM  23815  CG  PHE F 571       7.807 -48.398 -50.845  1.00 18.85           C  
-ATOM  23816  CD1 PHE F 571       6.474 -48.071 -51.027  1.00 21.07           C  
-ATOM  23817  CD2 PHE F 571       8.185 -49.726 -50.947  1.00 22.20           C  
-ATOM  23818  CE1 PHE F 571       5.536 -49.049 -51.308  1.00 19.73           C  
-ATOM  23819  CE2 PHE F 571       7.255 -50.707 -51.227  1.00 28.03           C  
-ATOM  23820  CZ  PHE F 571       5.928 -50.368 -51.409  1.00 26.57           C  
-ATOM  23821  N   PRO F 572       8.588 -44.276 -49.355  1.00 22.50           N  
-ATOM  23822  CA  PRO F 572       9.279 -43.341 -48.464  1.00 21.18           C  
-ATOM  23823  C   PRO F 572      10.070 -44.109 -47.414  1.00 20.24           C  
-ATOM  23824  O   PRO F 572       9.912 -45.326 -47.317  1.00 22.26           O  
-ATOM  23825  CB  PRO F 572       8.132 -42.563 -47.823  1.00 21.14           C  
-ATOM  23826  CG  PRO F 572       7.028 -43.563 -47.762  1.00 22.04           C  
-ATOM  23827  CD  PRO F 572       7.159 -44.399 -49.018  1.00 19.00           C  
-ATOM  23828  N   ILE F 573      10.915 -43.431 -46.646  1.00 21.31           N  
-ATOM  23829  CA  ILE F 573      11.512 -44.078 -45.487  1.00 20.07           C  
-ATOM  23830  C   ILE F 573      10.880 -43.479 -44.238  1.00 18.65           C  
-ATOM  23831  O   ILE F 573      10.561 -42.291 -44.195  1.00 12.43           O  
-ATOM  23832  CB  ILE F 573      13.062 -43.941 -45.443  1.00 15.64           C  
-ATOM  23833  CG1 ILE F 573      13.498 -42.682 -44.699  1.00 23.54           C  
-ATOM  23834  CG2 ILE F 573      13.661 -43.982 -46.839  1.00 17.00           C  
-ATOM  23835  CD1 ILE F 573      14.996 -42.576 -44.528  1.00 46.03           C  
-ATOM  23836  N   VAL F 574      10.657 -44.321 -43.238  1.00 18.92           N  
-ATOM  23837  CA  VAL F 574      10.089 -43.863 -41.979  1.00 12.03           C  
-ATOM  23838  C   VAL F 574      11.180 -43.812 -40.924  1.00 11.10           C  
-ATOM  23839  O   VAL F 574      11.772 -44.835 -40.581  1.00 10.40           O  
-ATOM  23840  CB  VAL F 574       8.944 -44.774 -41.499  1.00 10.31           C  
-ATOM  23841  CG1 VAL F 574       8.596 -44.477 -40.053  1.00 16.01           C  
-ATOM  23842  CG2 VAL F 574       7.725 -44.599 -42.386  1.00 12.55           C  
-ATOM  23843  N   ASN F 575      11.456 -42.615 -40.419  1.00 13.10           N  
-ATOM  23844  CA  ASN F 575      12.466 -42.456 -39.382  1.00 18.13           C  
-ATOM  23845  C   ASN F 575      11.863 -42.330 -37.990  1.00 19.56           C  
-ATOM  23846  O   ASN F 575      10.872 -41.622 -37.787  1.00 18.23           O  
-ATOM  23847  CB  ASN F 575      13.344 -41.239 -39.672  1.00 17.89           C  
-ATOM  23848  CG  ASN F 575      14.200 -41.426 -40.898  1.00 17.18           C  
-ATOM  23849  OD1 ASN F 575      14.684 -42.526 -41.165  1.00 14.24           O  
-ATOM  23850  ND2 ASN F 575      14.390 -40.355 -41.658  1.00 21.34           N  
-ATOM  23851  N   ILE F 576      12.465 -43.032 -37.037  1.00 15.08           N  
-ATOM  23852  CA  ILE F 576      12.124 -42.857 -35.638  1.00 14.49           C  
-ATOM  23853  C   ILE F 576      12.963 -41.716 -35.083  1.00 19.68           C  
-ATOM  23854  O   ILE F 576      14.192 -41.756 -35.137  1.00 16.16           O  
-ATOM  23855  CB  ILE F 576      12.364 -44.137 -34.818  1.00 12.06           C  
-ATOM  23856  CG1 ILE F 576      11.534 -45.289 -35.377  1.00 12.03           C  
-ATOM  23857  CG2 ILE F 576      12.021 -43.905 -33.354  1.00 18.15           C  
-ATOM  23858  CD1 ILE F 576      11.679 -46.563 -34.587  1.00 21.02           C  
-ATOM  23859  N   LEU F 577      12.293 -40.693 -34.565  1.00 17.18           N  
-ATOM  23860  CA  LEU F 577      12.977 -39.548 -33.974  1.00 22.67           C  
-ATOM  23861  C   LEU F 577      13.221 -39.785 -32.485  1.00 32.35           C  
-ATOM  23862  O   LEU F 577      12.536 -40.601 -31.865  1.00 31.19           O  
-ATOM  23863  CB  LEU F 577      12.159 -38.274 -34.192  1.00 19.60           C  
-ATOM  23864  CG  LEU F 577      11.832 -37.960 -35.653  1.00 19.08           C  
-ATOM  23865  CD1 LEU F 577      10.658 -36.999 -35.755  1.00 26.97           C  
-ATOM  23866  CD2 LEU F 577      13.053 -37.389 -36.356  1.00 21.70           C  
-ATOM  23867  N   ASN F 578      14.199 -39.079 -31.922  1.00 26.49           N  
-ATOM  23868  CA  ASN F 578      14.521 -39.185 -30.498  1.00 30.72           C  
-ATOM  23869  C   ASN F 578      14.804 -40.619 -30.066  1.00 26.97           C  
-ATOM  23870  O   ASN F 578      14.298 -41.075 -29.039  1.00 32.42           O  
-ATOM  23871  CB  ASN F 578      13.383 -38.616 -29.647  1.00 29.71           C  
-ATOM  23872  CG  ASN F 578      12.809 -37.336 -30.219  1.00 26.91           C  
-ATOM  23873  OD1 ASN F 578      13.543 -36.411 -30.567  1.00 28.93           O  
-ATOM  23874  ND2 ASN F 578      11.487 -37.280 -30.328  1.00 22.16           N  
-ATOM  23875  N   LYS F 579      15.609 -41.326 -30.854  1.00 27.57           N  
-ATOM  23876  CA  LYS F 579      15.920 -42.727 -30.575  1.00 32.66           C  
-ATOM  23877  C   LYS F 579      16.638 -42.888 -29.241  1.00 28.34           C  
-ATOM  23878  O   LYS F 579      16.550 -43.935 -28.603  1.00 30.50           O  
-ATOM  23879  CB  LYS F 579      16.769 -43.333 -31.705  1.00 27.85           C  
-ATOM  23880  CG  LYS F 579      16.973 -42.427 -32.908  1.00 46.07           C  
-ATOM  23881  CD  LYS F 579      18.231 -41.577 -32.763  1.00 65.18           C  
-ATOM  23882  CE  LYS F 579      18.274 -40.467 -33.801  1.00 45.41           C  
-ATOM  23883  NZ  LYS F 579      17.163 -39.490 -33.612  1.00 41.52           N  
-ATOM  23884  N   GLU F 580      17.347 -41.845 -28.827  1.00 26.98           N  
-ATOM  23885  CA  GLU F 580      18.073 -41.866 -27.565  1.00 34.30           C  
-ATOM  23886  C   GLU F 580      17.116 -41.949 -26.380  1.00 31.78           C  
-ATOM  23887  O   GLU F 580      17.394 -42.620 -25.386  1.00 33.73           O  
-ATOM  23888  CB  GLU F 580      18.963 -40.624 -27.444  1.00 35.44           C  
-ATOM  23889  CG  GLU F 580      19.574 -40.400 -26.065  1.00 51.50           C  
-ATOM  23890  CD  GLU F 580      20.654 -41.409 -25.710  1.00 57.17           C  
-ATOM  23891  OE1 GLU F 580      21.127 -41.383 -24.553  1.00 52.95           O  
-ATOM  23892  OE2 GLU F 580      21.035 -42.222 -26.580  1.00 59.50           O  
-ATOM  23893  N   ARG F 581      15.980 -41.274 -26.501  1.00 28.52           N  
-ATOM  23894  CA  ARG F 581      15.021 -41.193 -25.409  1.00 26.30           C  
-ATOM  23895  C   ARG F 581      14.180 -42.460 -25.283  1.00 24.95           C  
-ATOM  23896  O   ARG F 581      13.725 -42.811 -24.193  1.00 25.97           O  
-ATOM  23897  CB  ARG F 581      14.108 -39.980 -25.601  1.00 23.28           C  
-ATOM  23898  CG  ARG F 581      13.153 -39.750 -24.448  1.00 24.00           C  
-ATOM  23899  CD  ARG F 581      12.230 -38.572 -24.699  1.00 28.91           C  
-ATOM  23900  NE  ARG F 581      11.482 -38.710 -25.946  1.00 29.87           N  
-ATOM  23901  CZ  ARG F 581      10.434 -39.512 -26.106  1.00 32.66           C  
-ATOM  23902  NH1 ARG F 581      10.010 -40.267 -25.100  1.00 36.25           N  
-ATOM  23903  NH2 ARG F 581       9.814 -39.566 -27.276  1.00 25.12           N  
-ATOM  23904  N   ILE F 582      13.983 -43.148 -26.403  1.00 26.25           N  
-ATOM  23905  CA  ILE F 582      13.082 -44.294 -26.451  1.00 24.20           C  
-ATOM  23906  C   ILE F 582      13.802 -45.613 -26.176  1.00 28.37           C  
-ATOM  23907  O   ILE F 582      14.597 -46.083 -26.993  1.00 27.24           O  
-ATOM  23908  CB  ILE F 582      12.377 -44.373 -27.815  1.00 19.73           C  
-ATOM  23909  CG1 ILE F 582      11.658 -43.053 -28.103  1.00 19.29           C  
-ATOM  23910  CG2 ILE F 582      11.407 -45.542 -27.848  1.00 20.42           C  
-ATOM  23911  CD1 ILE F 582      11.015 -42.981 -29.467  1.00 23.13           C  
-ATOM  23912  N   LYS F 583      13.512 -46.209 -25.022  1.00 22.20           N  
-ATOM  23913  CA  LYS F 583      14.177 -47.439 -24.603  1.00 25.06           C  
-ATOM  23914  C   LYS F 583      13.220 -48.623 -24.483  1.00 22.62           C  
-ATOM  23915  O   LYS F 583      13.639 -49.778 -24.575  1.00 16.99           O  
-ATOM  23916  CB  LYS F 583      14.889 -47.225 -23.268  1.00 30.25           C  
-ATOM  23917  CG  LYS F 583      15.991 -46.179 -23.308  1.00 27.16           C  
-ATOM  23918  CD  LYS F 583      16.661 -46.055 -21.949  1.00 52.81           C  
-ATOM  23919  CE  LYS F 583      17.860 -45.118 -21.991  1.00 62.76           C  
-ATOM  23920  NZ  LYS F 583      18.519 -45.000 -20.657  1.00 53.50           N  
-ATOM  23921  N   GLU F 584      11.941 -48.335 -24.259  1.00 25.68           N  
-ATOM  23922  CA  GLU F 584      10.928 -49.380 -24.154  1.00 18.55           C  
-ATOM  23923  C   GLU F 584       9.774 -49.088 -25.107  1.00 18.61           C  
-ATOM  23924  O   GLU F 584       9.583 -47.948 -25.532  1.00 24.33           O  
-ATOM  23925  CB  GLU F 584      10.422 -49.502 -22.714  1.00 21.47           C  
-ATOM  23926  CG  GLU F 584      11.517 -49.685 -21.666  1.00 25.01           C  
-ATOM  23927  CD  GLU F 584      12.142 -51.066 -21.697  1.00 28.29           C  
-ATOM  23928  OE1 GLU F 584      11.617 -51.941 -22.416  1.00 33.72           O  
-ATOM  23929  OE2 GLU F 584      13.157 -51.277 -20.999  1.00 31.19           O  
-ATOM  23930  N   ILE F 585       9.004 -50.120 -25.438  1.00 20.91           N  
-ATOM  23931  CA  ILE F 585       7.949 -50.002 -26.443  1.00 23.16           C  
-ATOM  23932  C   ILE F 585       6.866 -49.000 -26.034  1.00 24.04           C  
-ATOM  23933  O   ILE F 585       6.178 -48.436 -26.887  1.00 21.58           O  
-ATOM  23934  CB  ILE F 585       7.299 -51.378 -26.727  1.00 21.48           C  
-ATOM  23935  CG1 ILE F 585       6.406 -51.317 -27.970  1.00 20.67           C  
-ATOM  23936  CG2 ILE F 585       6.532 -51.881 -25.510  1.00 20.25           C  
-ATOM  23937  CD1 ILE F 585       7.156 -51.026 -29.251  1.00 15.92           C  
-ATOM  23938  N   ASP F 586       6.731 -48.764 -24.732  1.00 20.19           N  
-ATOM  23939  CA  ASP F 586       5.727 -47.835 -24.226  1.00 19.77           C  
-ATOM  23940  C   ASP F 586       6.162 -46.381 -24.394  1.00 25.34           C  
-ATOM  23941  O   ASP F 586       5.343 -45.466 -24.297  1.00 24.14           O  
-ATOM  23942  CB  ASP F 586       5.435 -48.120 -22.752  1.00 27.23           C  
-ATOM  23943  CG  ASP F 586       4.744 -49.452 -22.541  1.00 44.62           C  
-ATOM  23944  OD1 ASP F 586       3.879 -49.812 -23.368  1.00 33.23           O  
-ATOM  23945  OD2 ASP F 586       5.066 -50.140 -21.547  1.00 55.15           O  
-ATOM  23946  N   ASP F 587       7.449 -46.177 -24.659  1.00 22.95           N  
-ATOM  23947  CA  ASP F 587       8.028 -44.836 -24.675  1.00 19.19           C  
-ATOM  23948  C   ASP F 587       7.755 -44.070 -25.970  1.00 18.38           C  
-ATOM  23949  O   ASP F 587       8.019 -42.870 -26.053  1.00 21.57           O  
-ATOM  23950  CB  ASP F 587       9.538 -44.917 -24.426  1.00 21.57           C  
-ATOM  23951  CG  ASP F 587       9.874 -45.320 -22.997  1.00 29.44           C  
-ATOM  23952  OD1 ASP F 587       9.095 -44.980 -22.080  1.00 28.40           O  
-ATOM  23953  OD2 ASP F 587      10.918 -45.973 -22.789  1.00 34.35           O  
-ATOM  23954  N   PHE F 588       7.227 -44.760 -26.976  1.00 19.57           N  
-ATOM  23955  CA  PHE F 588       6.899 -44.118 -28.245  1.00 19.26           C  
-ATOM  23956  C   PHE F 588       5.706 -43.177 -28.108  1.00 18.10           C  
-ATOM  23957  O   PHE F 588       4.739 -43.486 -27.413  1.00 18.76           O  
-ATOM  23958  CB  PHE F 588       6.593 -45.164 -29.317  1.00 24.81           C  
-ATOM  23959  CG  PHE F 588       7.811 -45.837 -29.888  1.00 25.96           C  
-ATOM  23960  CD1 PHE F 588       8.493 -45.275 -30.953  1.00 22.20           C  
-ATOM  23961  CD2 PHE F 588       8.256 -47.046 -29.378  1.00 25.71           C  
-ATOM  23962  CE1 PHE F 588       9.604 -45.896 -31.490  1.00 18.43           C  
-ATOM  23963  CE2 PHE F 588       9.366 -47.672 -29.914  1.00 22.20           C  
-ATOM  23964  CZ  PHE F 588      10.041 -47.096 -30.970  1.00 15.77           C  
-ATOM  23965  N   THR F 589       5.780 -42.026 -28.771  1.00 18.62           N  
-ATOM  23966  CA  THR F 589       4.626 -41.140 -28.895  1.00 19.52           C  
-ATOM  23967  C   THR F 589       4.343 -40.877 -30.373  1.00 16.56           C  
-ATOM  23968  O   THR F 589       5.074 -41.348 -31.242  1.00 16.00           O  
-ATOM  23969  CB  THR F 589       4.837 -39.801 -28.164  1.00 21.67           C  
-ATOM  23970  OG1 THR F 589       5.765 -38.992 -28.897  1.00 28.15           O  
-ATOM  23971  CG2 THR F 589       5.362 -40.035 -26.756  1.00 18.33           C  
-ATOM  23972  N   ALA F 590       3.291 -40.118 -30.656  1.00 18.00           N  
-ATOM  23973  CA  ALA F 590       2.877 -39.872 -32.035  1.00 17.83           C  
-ATOM  23974  C   ALA F 590       3.758 -38.838 -32.722  1.00 18.48           C  
-ATOM  23975  O   ALA F 590       3.532 -38.494 -33.881  1.00 19.82           O  
-ATOM  23976  CB  ALA F 590       1.424 -39.429 -32.077  1.00 22.35           C  
-ATOM  23977  N   GLU F 591       4.765 -38.348 -32.008  1.00 20.10           N  
-ATOM  23978  CA  GLU F 591       5.625 -37.297 -32.533  1.00 22.11           C  
-ATOM  23979  C   GLU F 591       7.047 -37.791 -32.789  1.00 26.03           C  
-ATOM  23980  O   GLU F 591       7.918 -37.017 -33.187  1.00 28.94           O  
-ATOM  23981  CB  GLU F 591       5.653 -36.110 -31.569  1.00 21.38           C  
-ATOM  23982  CG  GLU F 591       4.286 -35.714 -31.029  1.00 32.64           C  
-ATOM  23983  CD  GLU F 591       3.348 -35.194 -32.104  1.00 32.78           C  
-ATOM  23984  OE1 GLU F 591       2.122 -35.392 -31.966  1.00 26.52           O  
-ATOM  23985  OE2 GLU F 591       3.832 -34.577 -33.078  1.00 31.97           O  
-ATOM  23986  N   ASP F 592       7.280 -39.080 -32.565  1.00 25.94           N  
-ATOM  23987  CA  ASP F 592       8.618 -39.645 -32.712  1.00 25.90           C  
-ATOM  23988  C   ASP F 592       8.830 -40.307 -34.069  1.00 19.85           C  
-ATOM  23989  O   ASP F 592       9.670 -41.196 -34.209  1.00 14.86           O  
-ATOM  23990  CB  ASP F 592       8.891 -40.657 -31.601  1.00 20.39           C  
-ATOM  23991  CG  ASP F 592       8.694 -40.071 -30.223  1.00 23.80           C  
-ATOM  23992  OD1 ASP F 592       9.522 -39.233 -29.809  1.00 29.83           O  
-ATOM  23993  OD2 ASP F 592       7.715 -40.454 -29.551  1.00 30.28           O  
-ATOM  23994  N   PHE F 593       8.069 -39.873 -35.065  1.00 20.51           N  
-ATOM  23995  CA  PHE F 593       8.189 -40.433 -36.404  1.00 20.54           C  
-ATOM  23996  C   PHE F 593       8.146 -39.350 -37.468  1.00 20.45           C  
-ATOM  23997  O   PHE F 593       7.361 -38.407 -37.373  1.00 22.88           O  
-ATOM  23998  CB  PHE F 593       7.075 -41.446 -36.672  1.00 17.42           C  
-ATOM  23999  CG  PHE F 593       7.078 -42.617 -35.736  1.00 16.64           C  
-ATOM  24000  CD1 PHE F 593       7.822 -43.749 -36.023  1.00 18.80           C  
-ATOM  24001  CD2 PHE F 593       6.326 -42.592 -34.575  1.00 14.86           C  
-ATOM  24002  CE1 PHE F 593       7.822 -44.832 -35.165  1.00 15.52           C  
-ATOM  24003  CE2 PHE F 593       6.320 -43.670 -33.714  1.00 18.60           C  
-ATOM  24004  CZ  PHE F 593       7.068 -44.793 -34.010  1.00 19.35           C  
-ATOM  24005  N   GLU F 594       8.996 -39.486 -38.480  1.00 20.23           N  
-ATOM  24006  CA  GLU F 594       8.876 -38.652 -39.666  1.00 19.95           C  
-ATOM  24007  C   GLU F 594       8.789 -39.535 -40.900  1.00 17.27           C  
-ATOM  24008  O   GLU F 594       9.525 -40.516 -41.035  1.00 14.30           O  
-ATOM  24009  CB  GLU F 594      10.042 -37.661 -39.779  1.00 19.56           C  
-ATOM  24010  CG  GLU F 594      11.408 -38.270 -40.057  1.00 28.20           C  
-ATOM  24011  CD  GLU F 594      12.449 -37.214 -40.395  1.00 34.69           C  
-ATOM  24012  OE1 GLU F 594      13.658 -37.538 -40.414  1.00 24.25           O  
-ATOM  24013  OE2 GLU F 594      12.051 -36.055 -40.643  1.00 26.69           O  
-ATOM  24014  N   VAL F 595       7.858 -39.198 -41.784  1.00 17.18           N  
-ATOM  24015  CA  VAL F 595       7.717 -39.906 -43.045  1.00 15.81           C  
-ATOM  24016  C   VAL F 595       8.399 -39.102 -44.141  1.00 17.16           C  
-ATOM  24017  O   VAL F 595       7.973 -38.002 -44.478  1.00 16.05           O  
-ATOM  24018  CB  VAL F 595       6.249 -40.151 -43.401  1.00 14.21           C  
-ATOM  24019  CG1 VAL F 595       6.135 -40.697 -44.814  1.00 19.70           C  
-ATOM  24020  CG2 VAL F 595       5.626 -41.104 -42.395  1.00 12.95           C  
-ATOM  24021  N   VAL F 596       9.464 -39.671 -44.689  1.00 21.41           N  
-ATOM  24022  CA  VAL F 596      10.371 -38.944 -45.563  1.00 18.70           C  
-ATOM  24023  C   VAL F 596      10.308 -39.437 -47.008  1.00 28.26           C  
-ATOM  24024  O   VAL F 596      10.550 -40.613 -47.285  1.00 32.04           O  
-ATOM  24025  CB  VAL F 596      11.822 -39.060 -45.044  1.00 16.82           C  
-ATOM  24026  CG1 VAL F 596      12.814 -38.662 -46.113  1.00 20.62           C  
-ATOM  24027  CG2 VAL F 596      12.004 -38.223 -43.788  1.00 16.30           C  
-ATOM  24028  N   GLY F 597       9.982 -38.528 -47.924  1.00 21.44           N  
-ATOM  24029  CA  GLY F 597       9.980 -38.834 -49.344  1.00 21.63           C  
-ATOM  24030  C   GLY F 597       8.725 -39.538 -49.825  1.00 23.97           C  
-ATOM  24031  O   GLY F 597       8.776 -40.358 -50.738  1.00 27.09           O  
-ATOM  24032  N   TYR F 598       7.592 -39.212 -49.215  1.00 25.25           N  
-ATOM  24033  CA  TYR F 598       6.325 -39.832 -49.584  1.00 22.10           C  
-ATOM  24034  C   TYR F 598       5.614 -39.016 -50.656  1.00 17.49           C  
-ATOM  24035  O   TYR F 598       5.056 -37.959 -50.370  1.00 17.44           O  
-ATOM  24036  CB  TYR F 598       5.434 -39.987 -48.347  1.00 26.66           C  
-ATOM  24037  CG  TYR F 598       4.198 -40.834 -48.552  1.00 18.88           C  
-ATOM  24038  CD1 TYR F 598       4.269 -42.059 -49.201  1.00 24.18           C  
-ATOM  24039  CD2 TYR F 598       2.965 -40.420 -48.069  1.00 17.15           C  
-ATOM  24040  CE1 TYR F 598       3.144 -42.841 -49.381  1.00 23.41           C  
-ATOM  24041  CE2 TYR F 598       1.833 -41.195 -48.242  1.00 24.26           C  
-ATOM  24042  CZ  TYR F 598       1.928 -42.406 -48.899  1.00 28.79           C  
-ATOM  24043  OH  TYR F 598       0.804 -43.184 -49.074  1.00 24.55           O  
-ATOM  24044  N   VAL F 599       5.643 -39.512 -51.891  1.00 17.81           N  
-ATOM  24045  CA  VAL F 599       4.983 -38.843 -53.012  1.00 18.81           C  
-ATOM  24046  C   VAL F 599       3.943 -39.756 -53.666  1.00 21.58           C  
-ATOM  24047  O   VAL F 599       4.209 -40.359 -54.704  1.00 30.19           O  
-ATOM  24048  CB  VAL F 599       6.000 -38.395 -54.083  1.00 15.74           C  
-ATOM  24049  CG1 VAL F 599       5.353 -37.421 -55.058  1.00 23.82           C  
-ATOM  24050  CG2 VAL F 599       7.217 -37.762 -53.432  1.00 20.00           C  
-ATOM  24051  N   PRO F 600       2.752 -39.862 -53.057  1.00 21.77           N  
-ATOM  24052  CA  PRO F 600       1.721 -40.783 -53.544  1.00 24.28           C  
-ATOM  24053  C   PRO F 600       0.770 -40.154 -54.553  1.00 25.09           C  
-ATOM  24054  O   PRO F 600       0.768 -38.935 -54.726  1.00 29.70           O  
-ATOM  24055  CB  PRO F 600       0.969 -41.144 -52.268  1.00 21.62           C  
-ATOM  24056  CG  PRO F 600       1.024 -39.884 -51.466  1.00 21.39           C  
-ATOM  24057  CD  PRO F 600       2.353 -39.228 -51.788  1.00 25.46           C  
-ATOM  24058  N   HIS F 601      -0.031 -40.985 -55.211  1.00 22.56           N  
-ATOM  24059  CA  HIS F 601      -1.094 -40.485 -56.069  1.00 23.90           C  
-ATOM  24060  C   HIS F 601      -2.218 -39.950 -55.195  1.00 30.57           C  
-ATOM  24061  O   HIS F 601      -2.169 -40.072 -53.970  1.00 34.44           O  
-ATOM  24062  CB  HIS F 601      -1.614 -41.578 -57.002  1.00 25.61           C  
-ATOM  24063  CG  HIS F 601      -0.626 -42.007 -58.042  1.00 26.56           C  
-ATOM  24064  ND1 HIS F 601      -0.626 -41.497 -59.323  1.00 29.46           N  
-ATOM  24065  CD2 HIS F 601       0.393 -42.895 -57.990  1.00 26.02           C  
-ATOM  24066  CE1 HIS F 601       0.351 -42.055 -60.015  1.00 31.05           C  
-ATOM  24067  NE2 HIS F 601       0.985 -42.906 -59.230  1.00 22.78           N  
-ATOM  24068  N   GLY F 602      -3.228 -39.360 -55.824  1.00 29.39           N  
-ATOM  24069  CA  GLY F 602      -4.339 -38.777 -55.094  1.00 38.20           C  
-ATOM  24070  C   GLY F 602      -5.134 -39.808 -54.316  1.00 41.83           C  
-ATOM  24071  O   GLY F 602      -5.076 -41.001 -54.613  1.00 40.40           O  
-ATOM  24072  N   ARG F 603      -5.878 -39.348 -53.315  1.00 43.05           N  
-ATOM  24073  CA  ARG F 603      -6.713 -40.241 -52.521  1.00 42.38           C  
-ATOM  24074  C   ARG F 603      -7.815 -40.843 -53.384  1.00 34.39           C  
-ATOM  24075  O   ARG F 603      -8.408 -40.152 -54.213  1.00 26.46           O  
-ATOM  24076  CB  ARG F 603      -7.327 -39.499 -51.329  1.00 54.82           C  
-ATOM  24077  CG  ARG F 603      -6.348 -38.629 -50.557  1.00 65.22           C  
-ATOM  24078  CD  ARG F 603      -6.974 -38.092 -49.278  1.00 64.73           C  
-ATOM  24079  NE  ARG F 603      -6.785 -39.002 -48.150  1.00 89.99           N  
-ATOM  24080  CZ  ARG F 603      -6.026 -38.732 -47.091  1.00 85.17           C  
-ATOM  24081  NH1 ARG F 603      -5.908 -39.621 -46.112  1.00 54.74           N  
-ATOM  24082  NH2 ARG F 603      -5.390 -37.570 -47.006  1.00 68.24           N  
-ATOM  24083  N   ILE F 604      -8.077 -42.132 -53.195  1.00 36.45           N  
-ATOM  24084  CA  ILE F 604      -9.193 -42.784 -53.871  1.00 43.75           C  
-ATOM  24085  C   ILE F 604     -10.261 -43.184 -52.860  1.00 45.17           C  
-ATOM  24086  O   ILE F 604     -10.082 -44.130 -52.092  1.00 44.56           O  
-ATOM  24087  CB  ILE F 604      -8.751 -44.029 -54.656  1.00 45.88           C  
-ATOM  24088  CG1 ILE F 604      -7.672 -43.668 -55.677  1.00 44.55           C  
-ATOM  24089  CG2 ILE F 604      -9.945 -44.659 -55.354  1.00 43.16           C  
-ATOM  24090  CD1 ILE F 604      -7.225 -44.844 -56.522  1.00 29.71           C  
-ATOM  24091  N   GLN F 605     -11.374 -42.459 -52.875  1.00 44.42           N  
-ATOM  24092  CA  GLN F 605     -12.432 -42.637 -51.888  1.00 61.52           C  
-ATOM  24093  C   GLN F 605     -13.122 -43.997 -52.008  1.00 61.07           C  
-ATOM  24094  O   GLN F 605     -13.594 -44.375 -53.081  1.00 49.10           O  
-ATOM  24095  CB  GLN F 605     -13.459 -41.508 -52.020  1.00 62.15           C  
-ATOM  24096  CG  GLN F 605     -14.278 -41.246 -50.764  1.00 70.34           C  
-ATOM  24097  CD  GLN F 605     -15.559 -42.054 -50.715  1.00 70.27           C  
-ATOM  24098  OE1 GLN F 605     -16.113 -42.425 -51.752  1.00 53.33           O  
-ATOM  24099  NE2 GLN F 605     -16.039 -42.330 -49.506  1.00 53.94           N  
-ATOM  24100  N   MET F 606     -13.162 -44.728 -50.896  1.00 59.36           N  
-ATOM  24101  CA  MET F 606     -13.854 -46.013 -50.828  1.00 57.11           C  
-ATOM  24102  C   MET F 606     -14.659 -46.122 -49.536  1.00 58.70           C  
-ATOM  24103  O   MET F 606     -14.119 -45.948 -48.442  1.00 63.20           O  
-ATOM  24104  CB  MET F 606     -12.863 -47.175 -50.919  1.00 53.75           C  
-ATOM  24105  CG  MET F 606     -12.030 -47.196 -52.186  1.00 56.10           C  
-ATOM  24106  SD  MET F 606     -10.844 -48.552 -52.188  1.00 47.84           S  
-ATOM  24107  CE  MET F 606      -9.626 -47.923 -53.342  1.00 43.33           C  
-ATOM  24108  N   GLU F 607     -15.950 -46.413 -49.666  1.00 56.73           N  
-ATOM  24109  CA  GLU F 607     -16.832 -46.507 -48.508  1.00 56.25           C  
-ATOM  24110  C   GLU F 607     -16.687 -47.852 -47.805  1.00 51.09           C  
-ATOM  24111  O   GLU F 607     -16.629 -48.902 -48.446  1.00 44.08           O  
-ATOM  24112  CB  GLU F 607     -18.293 -46.278 -48.915  1.00 59.27           C  
-ATOM  24113  CG  GLU F 607     -18.823 -47.227 -49.980  1.00 77.40           C  
-ATOM  24114  CD  GLU F 607     -18.372 -46.850 -51.380  1.00 93.97           C  
-ATOM  24115  OE1 GLU F 607     -19.200 -46.312 -52.147  1.00100.81           O  
-ATOM  24116  OE2 GLU F 607     -17.191 -47.092 -51.712  1.00 78.56           O  
-ATOM  24117  N   MET F 608     -16.629 -47.806 -46.479  1.00 61.99           N  
-ATOM  24118  CA  MET F 608     -16.455 -49.007 -45.671  1.00 53.83           C  
-ATOM  24119  C   MET F 608     -17.756 -49.785 -45.530  1.00 45.56           C  
-ATOM  24120  O   MET F 608     -18.771 -49.244 -45.089  1.00 44.18           O  
-ATOM  24121  CB  MET F 608     -15.921 -48.650 -44.281  1.00 54.72           C  
-ATOM  24122  CG  MET F 608     -15.650 -49.862 -43.403  1.00 60.61           C  
-ATOM  24123  SD  MET F 608     -15.758 -49.514 -41.635  1.00 55.07           S  
-ATOM  24124  CE  MET F 608     -14.607 -48.155 -41.478  1.00 62.27           C  
-ATOM  24125  N   ALA F 609     -17.720 -51.059 -45.904  1.00 52.03           N  
-ATOM  24126  CA  ALA F 609     -18.851 -51.949 -45.681  1.00 48.84           C  
-ATOM  24127  C   ALA F 609     -18.994 -52.231 -44.190  1.00 50.85           C  
-ATOM  24128  O   ALA F 609     -18.248 -53.032 -43.626  1.00 55.66           O  
-ATOM  24129  CB  ALA F 609     -18.678 -53.244 -46.458  1.00 38.95           C  
-ATOM  24130  N   VAL F 610     -19.950 -51.560 -43.555  1.00 55.48           N  
-ATOM  24131  CA  VAL F 610     -20.133 -51.672 -42.114  1.00 66.27           C  
-ATOM  24132  C   VAL F 610     -20.593 -53.072 -41.722  1.00 67.60           C  
-ATOM  24133  O   VAL F 610     -20.000 -53.704 -40.845  1.00 67.64           O  
-ATOM  24134  CB  VAL F 610     -21.152 -50.636 -41.592  1.00 61.94           C  
-ATOM  24135  CG1 VAL F 610     -21.307 -50.756 -40.083  1.00 61.79           C  
-ATOM  24136  CG2 VAL F 610     -20.721 -49.228 -41.976  1.00 38.44           C  
-ATOM  24137  OXT VAL F 610     -21.557 -53.605 -42.278  1.00 54.48           O  
-TER   24138      VAL F 610                                                      
-ATOM  24139  N   PRO G   4      15.240  94.778   3.276  1.00 50.23           N  
-ATOM  24140  CA  PRO G   4      15.456  94.196   4.608  1.00 46.69           C  
-ATOM  24141  C   PRO G   4      16.878  94.441   5.114  1.00 56.41           C  
-ATOM  24142  O   PRO G   4      17.802  93.699   4.769  1.00 56.33           O  
-ATOM  24143  CB  PRO G   4      15.194  92.706   4.382  1.00 46.07           C  
-ATOM  24144  CG  PRO G   4      15.541  92.482   2.943  1.00 58.16           C  
-ATOM  24145  CD  PRO G   4      15.187  93.754   2.217  1.00 41.23           C  
-ATOM  24146  N   VAL G   5      17.045  95.474   5.934  1.00 48.68           N  
-ATOM  24147  CA  VAL G   5      18.372  95.905   6.360  1.00 47.06           C  
-ATOM  24148  C   VAL G   5      18.649  95.528   7.818  1.00 43.11           C  
-ATOM  24149  O   VAL G   5      17.726  95.377   8.621  1.00 41.63           O  
-ATOM  24150  CB  VAL G   5      18.544  97.435   6.172  1.00 33.47           C  
-ATOM  24151  CG1 VAL G   5      17.924  98.201   7.325  1.00 33.32           C  
-ATOM  24152  CG2 VAL G   5      20.005  97.799   6.032  1.00 41.95           C  
-ATOM  24153  N   CYS G   6      19.926  95.356   8.147  1.00 32.40           N  
-ATOM  24154  CA  CYS G   6      20.341  95.059   9.515  1.00 35.18           C  
-ATOM  24155  C   CYS G   6      21.361  96.077  10.021  1.00 37.74           C  
-ATOM  24156  O   CYS G   6      22.366  96.328   9.369  1.00 43.41           O  
-ATOM  24157  CB  CYS G   6      20.925  93.643   9.607  1.00 38.59           C  
-ATOM  24158  SG  CYS G   6      19.718  92.298   9.454  1.00 58.55           S  
-ATOM  24159  N   LEU G   7      21.098  96.654  11.189  1.00 26.92           N  
-ATOM  24160  CA  LEU G   7      22.023  97.605  11.802  1.00 17.35           C  
-ATOM  24161  C   LEU G   7      23.045  96.874  12.663  1.00 25.09           C  
-ATOM  24162  O   LEU G   7      22.715  95.870  13.294  1.00 32.00           O  
-ATOM  24163  CB  LEU G   7      21.264  98.628  12.653  1.00 22.47           C  
-ATOM  24164  CG  LEU G   7      20.685  99.891  12.009  1.00 32.35           C  
-ATOM  24165  CD1 LEU G   7      19.782  99.571  10.828  1.00 36.82           C  
-ATOM  24166  CD2 LEU G   7      19.928 100.710  13.049  1.00 29.51           C  
-ATOM  24167  N   VAL G   8      24.282  97.364  12.692  1.00 24.99           N  
-ATOM  24168  CA  VAL G   8      25.289  96.762  13.574  1.00 22.69           C  
-ATOM  24169  C   VAL G   8      26.092  97.823  14.340  1.00 21.86           C  
-ATOM  24170  O   VAL G   8      26.641  98.753  13.747  1.00 18.08           O  
-ATOM  24171  CB  VAL G   8      26.248  95.840  12.784  1.00 10.71           C  
-ATOM  24172  CG1 VAL G   8      26.489  96.387  11.395  1.00 26.49           C  
-ATOM  24173  CG2 VAL G   8      27.558  95.646  13.534  1.00 17.65           C  
-ATOM  24174  N   VAL G   9      26.153  97.674  15.663  1.00 23.09           N  
-ATOM  24175  CA  VAL G   9      26.687  98.719  16.539  1.00 22.49           C  
-ATOM  24176  C   VAL G   9      27.485  98.206  17.733  1.00 22.80           C  
-ATOM  24177  O   VAL G   9      27.307  97.074  18.181  1.00 36.45           O  
-ATOM  24178  CB  VAL G   9      25.553  99.592  17.115  1.00 27.37           C  
-ATOM  24179  CG1 VAL G   9      25.098 100.621  16.113  1.00 38.26           C  
-ATOM  24180  CG2 VAL G   9      24.391  98.717  17.547  1.00 25.21           C  
-ATOM  24181  N   ALA G  10      28.359  99.064  18.246  1.00 19.85           N  
-ATOM  24182  CA  ALA G  10      28.936  98.891  19.574  1.00 22.16           C  
-ATOM  24183  C   ALA G  10      28.526 100.114  20.391  1.00 27.44           C  
-ATOM  24184  O   ALA G  10      28.544 101.236  19.880  1.00 30.33           O  
-ATOM  24185  CB  ALA G  10      30.442  98.743  19.506  1.00 23.51           C  
-ATOM  24186  N   MET G  11      28.151  99.909  21.651  1.00 22.05           N  
-ATOM  24187  CA  MET G  11      27.378 100.924  22.361  1.00 17.47           C  
-ATOM  24188  C   MET G  11      27.575 100.931  23.883  1.00 25.28           C  
-ATOM  24189  O   MET G  11      27.585  99.879  24.527  1.00 31.29           O  
-ATOM  24190  CB  MET G  11      25.898 100.718  22.039  1.00 13.53           C  
-ATOM  24191  CG  MET G  11      25.028 101.930  22.218  1.00 19.26           C  
-ATOM  24192  SD  MET G  11      23.302 101.529  21.891  1.00 25.32           S  
-ATOM  24193  CE  MET G  11      23.414 100.808  20.260  1.00 18.81           C  
-ATOM  24194  N   THR G  12      27.722 102.125  24.451  1.00 19.08           N  
-ATOM  24195  CA  THR G  12      27.803 102.296  25.901  1.00 21.04           C  
-ATOM  24196  C   THR G  12      26.390 102.228  26.497  1.00 27.31           C  
-ATOM  24197  O   THR G  12      25.414 102.239  25.746  1.00 32.27           O  
-ATOM  24198  CB  THR G  12      28.479 103.633  26.266  1.00 16.11           C  
-ATOM  24199  OG1 THR G  12      27.649 104.722  25.849  1.00 20.17           O  
-ATOM  24200  CG2 THR G  12      29.836 103.745  25.591  1.00 16.74           C  
-ATOM  24201  N   PRO G  13      26.264 102.133  27.838  1.00 21.24           N  
-ATOM  24202  CA  PRO G  13      24.904 102.088  28.392  1.00 17.90           C  
-ATOM  24203  C   PRO G  13      24.092 103.347  28.114  1.00 16.98           C  
-ATOM  24204  O   PRO G  13      22.867 103.276  28.052  1.00 17.57           O  
-ATOM  24205  CB  PRO G  13      25.143 101.929  29.896  1.00 21.69           C  
-ATOM  24206  CG  PRO G  13      26.463 101.277  29.993  1.00 24.31           C  
-ATOM  24207  CD  PRO G  13      27.275 101.863  28.876  1.00 21.57           C  
-ATOM  24208  N   LYS G  14      24.768 104.480  27.949  1.00 19.12           N  
-ATOM  24209  CA  LYS G  14      24.090 105.731  27.631  1.00 20.43           C  
-ATOM  24210  C   LYS G  14      24.089 105.975  26.123  1.00 24.23           C  
-ATOM  24211  O   LYS G  14      24.075 107.119  25.664  1.00 22.12           O  
-ATOM  24212  CB  LYS G  14      24.739 106.896  28.384  1.00  9.51           C  
-ATOM  24213  CG  LYS G  14      24.280 106.978  29.838  1.00 20.39           C  
-ATOM  24214  CD  LYS G  14      25.341 107.546  30.770  1.00 26.07           C  
-ATOM  24215  CE  LYS G  14      25.329 109.066  30.799  1.00 30.14           C  
-ATOM  24216  NZ  LYS G  14      26.260 109.595  31.836  1.00 26.57           N  
-ATOM  24217  N   ARG G  15      24.110 104.875  25.372  1.00 21.14           N  
-ATOM  24218  CA  ARG G  15      23.960 104.868  23.917  1.00 14.89           C  
-ATOM  24219  C   ARG G  15      25.059 105.618  23.166  1.00 19.58           C  
-ATOM  24220  O   ARG G  15      24.894 105.956  21.994  1.00 21.02           O  
-ATOM  24221  CB  ARG G  15      22.591 105.435  23.528  1.00 19.54           C  
-ATOM  24222  CG  ARG G  15      21.433 104.518  23.884  1.00 22.48           C  
-ATOM  24223  CD  ARG G  15      20.095 105.050  23.382  1.00 25.45           C  
-ATOM  24224  NE  ARG G  15      19.563 106.110  24.235  1.00 22.14           N  
-ATOM  24225  CZ  ARG G  15      19.581 107.402  23.927  1.00 25.86           C  
-ATOM  24226  NH1 ARG G  15      19.074 108.293  24.769  1.00 24.42           N  
-ATOM  24227  NH2 ARG G  15      20.102 107.806  22.775  1.00 27.20           N  
-ATOM  24228  N   GLY G  16      26.182 105.862  23.833  1.00 21.24           N  
-ATOM  24229  CA  GLY G  16      27.308 106.529  23.203  1.00 16.26           C  
-ATOM  24230  C   GLY G  16      28.032 105.596  22.257  1.00 17.13           C  
-ATOM  24231  O   GLY G  16      28.227 104.422  22.570  1.00 22.16           O  
-ATOM  24232  N   ILE G  17      28.427 106.105  21.094  1.00 17.78           N  
-ATOM  24233  CA  ILE G  17      29.084 105.262  20.099  1.00 21.11           C  
-ATOM  24234  C   ILE G  17      30.420 105.826  19.616  1.00 22.69           C  
-ATOM  24235  O   ILE G  17      31.252 105.086  19.089  1.00 19.64           O  
-ATOM  24236  CB  ILE G  17      28.183 105.032  18.865  1.00 17.74           C  
-ATOM  24237  CG1 ILE G  17      27.986 106.334  18.091  1.00 15.22           C  
-ATOM  24238  CG2 ILE G  17      26.843 104.430  19.274  1.00 16.81           C  
-ATOM  24239  CD1 ILE G  17      27.197 106.167  16.817  1.00 17.96           C  
-ATOM  24240  N   GLY G  18      30.631 107.128  19.792  1.00 23.54           N  
-ATOM  24241  CA  GLY G  18      31.848 107.750  19.299  1.00 26.54           C  
-ATOM  24242  C   GLY G  18      32.254 109.063  19.942  1.00 25.69           C  
-ATOM  24243  O   GLY G  18      31.442 109.737  20.579  1.00 25.08           O  
-ATOM  24244  N   ILE G  19      33.526 109.419  19.772  1.00 23.55           N  
-ATOM  24245  CA  ILE G  19      34.040 110.712  20.215  1.00 25.47           C  
-ATOM  24246  C   ILE G  19      35.206 111.163  19.326  1.00 31.43           C  
-ATOM  24247  O   ILE G  19      36.080 110.363  18.981  1.00 37.83           O  
-ATOM  24248  CB  ILE G  19      34.482 110.671  21.695  1.00 15.30           C  
-ATOM  24249  CG1 ILE G  19      34.914 112.060  22.162  1.00 16.13           C  
-ATOM  24250  CG2 ILE G  19      35.592 109.652  21.905  1.00 16.25           C  
-ATOM  24251  CD1 ILE G  19      34.485 112.385  23.568  1.00 22.03           C  
-ATOM  24252  N   ASN G  20      35.197 112.441  18.946  1.00 20.25           N  
-ATOM  24253  CA  ASN G  20      36.217 113.017  18.068  1.00 19.68           C  
-ATOM  24254  C   ASN G  20      36.438 112.197  16.803  1.00 26.69           C  
-ATOM  24255  O   ASN G  20      37.578 111.935  16.416  1.00 25.01           O  
-ATOM  24256  CB  ASN G  20      37.546 113.173  18.811  1.00 16.35           C  
-ATOM  24257  CG  ASN G  20      37.703 114.541  19.443  1.00 35.82           C  
-ATOM  24258  OD1 ASN G  20      37.304 115.555  18.870  1.00 43.93           O  
-ATOM  24259  ND2 ASN G  20      38.288 114.575  20.634  1.00 53.88           N  
-ATOM  24260  N   ASN G  21      35.336 111.797  16.176  1.00 28.55           N  
-ATOM  24261  CA  ASN G  21      35.366 110.979  14.969  1.00 26.10           C  
-ATOM  24262  C   ASN G  21      36.192 109.708  15.162  1.00 25.90           C  
-ATOM  24263  O   ASN G  21      36.877 109.253  14.248  1.00 33.21           O  
-ATOM  24264  CB  ASN G  21      35.908 111.784  13.788  1.00 23.02           C  
-ATOM  24265  CG  ASN G  21      35.297 111.364  12.468  1.00 39.47           C  
-ATOM  24266  OD1 ASN G  21      34.104 111.066  12.393  1.00 34.27           O  
-ATOM  24267  ND2 ASN G  21      36.113 111.330  11.418  1.00 46.13           N  
-ATOM  24268  N   GLY G  22      36.125 109.147  16.364  1.00 22.52           N  
-ATOM  24269  CA  GLY G  22      36.820 107.914  16.681  1.00 18.43           C  
-ATOM  24270  C   GLY G  22      36.006 107.114  17.674  1.00 17.99           C  
-ATOM  24271  O   GLY G  22      34.890 107.501  18.013  1.00 22.84           O  
-ATOM  24272  N   LEU G  23      36.554 105.999  18.140  1.00 18.38           N  
-ATOM  24273  CA  LEU G  23      35.855 105.174  19.118  1.00 18.03           C  
-ATOM  24274  C   LEU G  23      36.179 105.633  20.536  1.00 19.73           C  
-ATOM  24275  O   LEU G  23      37.295 106.072  20.813  1.00 20.33           O  
-ATOM  24276  CB  LEU G  23      36.213 103.698  18.933  1.00 21.34           C  
-ATOM  24277  CG  LEU G  23      35.833 103.095  17.578  1.00 17.21           C  
-ATOM  24278  CD1 LEU G  23      36.172 101.612  17.524  1.00 18.91           C  
-ATOM  24279  CD2 LEU G  23      34.359 103.324  17.285  1.00 22.51           C  
-ATOM  24280  N   PRO G  24      35.193 105.540  21.439  1.00 18.02           N  
-ATOM  24281  CA  PRO G  24      35.327 106.011  22.822  1.00 19.06           C  
-ATOM  24282  C   PRO G  24      36.216 105.116  23.684  1.00 23.21           C  
-ATOM  24283  O   PRO G  24      36.824 105.595  24.640  1.00 27.64           O  
-ATOM  24284  CB  PRO G  24      33.882 105.987  23.342  1.00 17.77           C  
-ATOM  24285  CG  PRO G  24      33.015 105.838  22.125  1.00 16.50           C  
-ATOM  24286  CD  PRO G  24      33.830 105.067  21.154  1.00 15.78           C  
-ATOM  24287  N   TRP G  25      36.289 103.836  23.336  1.00 24.33           N  
-ATOM  24288  CA  TRP G  25      36.972 102.836  24.152  1.00 22.70           C  
-ATOM  24289  C   TRP G  25      38.297 102.384  23.537  1.00 28.51           C  
-ATOM  24290  O   TRP G  25      38.571 102.674  22.371  1.00 29.85           O  
-ATOM  24291  CB  TRP G  25      36.052 101.630  24.346  1.00 16.64           C  
-ATOM  24292  CG  TRP G  25      35.349 101.249  23.084  1.00 21.43           C  
-ATOM  24293  CD1 TRP G  25      35.858 100.520  22.049  1.00 21.58           C  
-ATOM  24294  CD2 TRP G  25      34.010 101.593  22.712  1.00 23.01           C  
-ATOM  24295  NE1 TRP G  25      34.917 100.385  21.057  1.00 19.38           N  
-ATOM  24296  CE2 TRP G  25      33.774 101.034  21.441  1.00 18.18           C  
-ATOM  24297  CE3 TRP G  25      32.986 102.316  23.332  1.00 19.98           C  
-ATOM  24298  CZ2 TRP G  25      32.557 101.176  20.780  1.00 15.10           C  
-ATOM  24299  CZ3 TRP G  25      31.779 102.455  22.673  1.00 14.94           C  
-ATOM  24300  CH2 TRP G  25      31.575 101.888  21.411  1.00 15.83           C  
-ATOM  24301  N   PRO G  26      39.131 101.678  24.322  1.00 22.33           N  
-ATOM  24302  CA  PRO G  26      40.288 100.987  23.740  1.00 23.18           C  
-ATOM  24303  C   PRO G  26      39.852  99.890  22.766  1.00 37.93           C  
-ATOM  24304  O   PRO G  26      38.661  99.587  22.677  1.00 42.80           O  
-ATOM  24305  CB  PRO G  26      41.005 100.400  24.959  1.00 22.45           C  
-ATOM  24306  CG  PRO G  26      40.003 100.439  26.067  1.00 22.44           C  
-ATOM  24307  CD  PRO G  26      39.149 101.628  25.793  1.00 18.93           C  
-ATOM  24308  N  AHIS G  27      40.803  99.306  22.045  0.31 49.24           N  
-ATOM  24309  N  BHIS G  27      40.811  99.308  22.051  0.69 49.98           N  
-ATOM  24310  CA AHIS G  27      40.471  98.365  20.979  0.31 53.11           C  
-ATOM  24311  CA BHIS G  27      40.512  98.326  21.011  0.69 52.54           C  
-ATOM  24312  C  AHIS G  27      39.852  97.082  21.533  0.31 51.37           C  
-ATOM  24313  C  BHIS G  27      39.829  97.086  21.579  0.69 51.56           C  
-ATOM  24314  O  AHIS G  27      40.404  96.442  22.430  0.31 40.57           O  
-ATOM  24315  O  BHIS G  27      40.324  96.472  22.526  0.69 40.55           O  
-ATOM  24316  CB AHIS G  27      41.711  98.049  20.131  0.31 40.45           C  
-ATOM  24317  CB BHIS G  27      41.791  97.923  20.273  0.69 40.11           C  
-ATOM  24318  CG AHIS G  27      42.738  97.219  20.835  0.31 45.02           C  
-ATOM  24319  CG BHIS G  27      41.546  97.142  19.020  0.69 33.03           C  
-ATOM  24320  ND1AHIS G  27      42.930  95.883  20.557  0.31 45.17           N  
-ATOM  24321  ND1BHIS G  27      41.279  97.745  17.810  0.69 29.45           N  
-ATOM  24322  CD2AHIS G  27      43.630  97.533  21.805  0.31 45.68           C  
-ATOM  24323  CD2BHIS G  27      41.520  95.808  18.790  0.69 32.40           C  
-ATOM  24324  CE1AHIS G  27      43.895  95.410  21.324  0.31 41.28           C  
-ATOM  24325  CE1BHIS G  27      41.104  96.816  16.887  0.69 30.37           C  
-ATOM  24326  NE2AHIS G  27      44.337  96.391  22.091  0.31 40.49           N  
-ATOM  24327  NE2BHIS G  27      41.244  95.632  17.456  0.69 31.19           N  
-ATOM  24328  N   LEU G  28      38.688  96.728  21.000  1.00 42.24           N  
-ATOM  24329  CA  LEU G  28      37.969  95.530  21.413  1.00 30.19           C  
-ATOM  24330  C   LEU G  28      38.060  94.482  20.312  1.00 32.50           C  
-ATOM  24331  O   LEU G  28      37.203  94.399  19.429  1.00 39.79           O  
-ATOM  24332  CB  LEU G  28      36.510  95.851  21.733  1.00 31.03           C  
-ATOM  24333  CG  LEU G  28      36.256  97.018  22.691  1.00 38.04           C  
-ATOM  24334  CD1 LEU G  28      34.763  97.186  22.940  1.00 24.54           C  
-ATOM  24335  CD2 LEU G  28      37.008  96.826  23.999  1.00 30.68           C  
-ATOM  24336  N   THR G  29      39.117  93.684  20.379  1.00 30.72           N  
-ATOM  24337  CA  THR G  29      39.445  92.734  19.330  1.00 38.33           C  
-ATOM  24338  C   THR G  29      38.317  91.741  19.031  1.00 31.61           C  
-ATOM  24339  O   THR G  29      38.041  91.448  17.867  1.00 34.68           O  
-ATOM  24340  CB  THR G  29      40.732  91.957  19.686  1.00 32.44           C  
-ATOM  24341  OG1 THR G  29      40.936  90.907  18.733  1.00 49.62           O  
-ATOM  24342  CG2 THR G  29      40.649  91.363  21.084  1.00 32.97           C  
-ATOM  24343  N   THR G  30      37.655  91.240  20.069  1.00 19.13           N  
-ATOM  24344  CA  THR G  30      36.574  90.284  19.874  1.00 21.32           C  
-ATOM  24345  C   THR G  30      35.394  90.971  19.205  1.00 26.35           C  
-ATOM  24346  O   THR G  30      34.689  90.369  18.397  1.00 25.90           O  
-ATOM  24347  CB  THR G  30      36.127  89.658  21.200  1.00 17.65           C  
-ATOM  24348  OG1 THR G  30      37.268  89.129  21.887  1.00 22.72           O  
-ATOM  24349  CG2 THR G  30      35.124  88.542  20.958  1.00 17.69           C  
-ATOM  24350  N   ASP G  31      35.188  92.237  19.548  1.00 27.86           N  
-ATOM  24351  CA  ASP G  31      34.132  93.025  18.929  1.00 26.38           C  
-ATOM  24352  C   ASP G  31      34.424  93.204  17.448  1.00 27.56           C  
-ATOM  24353  O   ASP G  31      33.523  93.125  16.613  1.00 27.36           O  
-ATOM  24354  CB  ASP G  31      33.997  94.385  19.610  1.00 28.40           C  
-ATOM  24355  CG  ASP G  31      32.983  95.280  18.931  1.00 35.22           C  
-ATOM  24356  OD1 ASP G  31      31.849  94.821  18.677  1.00 29.53           O  
-ATOM  24357  OD2 ASP G  31      33.332  96.444  18.642  1.00 30.59           O  
-ATOM  24358  N   PHE G  32      35.692  93.438  17.124  1.00 30.07           N  
-ATOM  24359  CA  PHE G  32      36.083  93.596  15.728  1.00 33.47           C  
-ATOM  24360  C   PHE G  32      35.929  92.290  14.961  1.00 34.12           C  
-ATOM  24361  O   PHE G  32      35.529  92.292  13.798  1.00 33.77           O  
-ATOM  24362  CB  PHE G  32      37.516  94.120  15.625  1.00 35.12           C  
-ATOM  24363  CG  PHE G  32      37.596  95.614  15.548  1.00 32.55           C  
-ATOM  24364  CD1 PHE G  32      37.359  96.387  16.671  1.00 43.08           C  
-ATOM  24365  CD2 PHE G  32      37.888  96.250  14.352  1.00 36.77           C  
-ATOM  24366  CE1 PHE G  32      37.420  97.766  16.609  1.00 46.02           C  
-ATOM  24367  CE2 PHE G  32      37.951  97.630  14.286  1.00 42.25           C  
-ATOM  24368  CZ  PHE G  32      37.716  98.388  15.417  1.00 43.11           C  
-ATOM  24369  N   LYS G  33      36.236  91.176  15.617  1.00 31.64           N  
-ATOM  24370  CA  LYS G  33      36.045  89.864  15.011  1.00 36.63           C  
-ATOM  24371  C   LYS G  33      34.563  89.648  14.723  1.00 34.84           C  
-ATOM  24372  O   LYS G  33      34.186  89.175  13.645  1.00 39.13           O  
-ATOM  24373  CB  LYS G  33      36.584  88.757  15.922  1.00 27.67           C  
-ATOM  24374  CG  LYS G  33      36.705  87.402  15.241  1.00 26.84           C  
-ATOM  24375  CD  LYS G  33      37.581  86.439  16.031  1.00 28.29           C  
-ATOM  24376  CE  LYS G  33      36.881  85.939  17.284  1.00 47.07           C  
-ATOM  24377  NZ  LYS G  33      37.689  84.904  17.988  1.00 45.04           N  
-ATOM  24378  N   HIS G  34      33.732  90.011  15.696  1.00 28.17           N  
-ATOM  24379  CA  HIS G  34      32.281  89.954  15.559  1.00 35.33           C  
-ATOM  24380  C   HIS G  34      31.812  90.741  14.341  1.00 31.84           C  
-ATOM  24381  O   HIS G  34      31.109  90.208  13.486  1.00 28.29           O  
-ATOM  24382  CB  HIS G  34      31.607  90.485  16.831  1.00 28.43           C  
-ATOM  24383  CG  HIS G  34      30.135  90.716  16.688  1.00 25.31           C  
-ATOM  24384  ND1 HIS G  34      29.199  89.731  16.915  1.00 31.65           N  
-ATOM  24385  CD2 HIS G  34      29.436  91.825  16.344  1.00 30.24           C  
-ATOM  24386  CE1 HIS G  34      27.988  90.221  16.717  1.00 28.74           C  
-ATOM  24387  NE2 HIS G  34      28.105  91.490  16.369  1.00 29.22           N  
-ATOM  24388  N   PHE G  35      32.216  92.007  14.266  1.00 34.15           N  
-ATOM  24389  CA  PHE G  35      31.852  92.878  13.148  1.00 30.88           C  
-ATOM  24390  C   PHE G  35      32.267  92.268  11.807  1.00 34.04           C  
-ATOM  24391  O   PHE G  35      31.451  92.155  10.885  1.00 38.52           O  
-ATOM  24392  CB  PHE G  35      32.486  94.265  13.328  1.00 27.51           C  
-ATOM  24393  CG  PHE G  35      32.279  95.190  12.160  1.00 29.47           C  
-ATOM  24394  CD1 PHE G  35      31.111  95.923  12.036  1.00 34.78           C  
-ATOM  24395  CD2 PHE G  35      33.259  95.334  11.193  1.00 32.14           C  
-ATOM  24396  CE1 PHE G  35      30.921  96.778  10.961  1.00 36.77           C  
-ATOM  24397  CE2 PHE G  35      33.076  96.187  10.117  1.00 29.91           C  
-ATOM  24398  CZ  PHE G  35      31.906  96.909  10.000  1.00 24.74           C  
-ATOM  24399  N   SER G  36      33.535  91.869  11.716  1.00 35.12           N  
-ATOM  24400  CA  SER G  36      34.074  91.253  10.508  1.00 34.42           C  
-ATOM  24401  C   SER G  36      33.251  90.052  10.060  1.00 41.06           C  
-ATOM  24402  O   SER G  36      32.765  90.012   8.924  1.00 45.93           O  
-ATOM  24403  CB  SER G  36      35.522  90.818  10.722  1.00 47.08           C  
-ATOM  24404  OG  SER G  36      35.969  90.048   9.617  1.00 47.90           O  
-ATOM  24405  N   ARG G  37      33.089  89.080  10.953  1.00 37.85           N  
-ATOM  24406  CA  ARG G  37      32.364  87.865  10.607  1.00 39.39           C  
-ATOM  24407  C   ARG G  37      30.920  88.163  10.199  1.00 32.36           C  
-ATOM  24408  O   ARG G  37      30.463  87.719   9.144  1.00 39.17           O  
-ATOM  24409  CB  ARG G  37      32.393  86.879  11.772  1.00 43.79           C  
-ATOM  24410  CG  ARG G  37      32.512  85.438  11.322  1.00 50.69           C  
-ATOM  24411  CD  ARG G  37      33.903  84.888  11.595  1.00 56.37           C  
-ATOM  24412  NE  ARG G  37      34.954  85.853  11.287  1.00 57.08           N  
-ATOM  24413  CZ  ARG G  37      36.242  85.674  11.567  1.00 57.96           C  
-ATOM  24414  NH1 ARG G  37      37.125  86.611  11.248  1.00 56.66           N  
-ATOM  24415  NH2 ARG G  37      36.650  84.560  12.165  1.00 36.35           N  
-ATOM  24416  N   VAL G  38      30.218  88.931  11.029  1.00 24.58           N  
-ATOM  24417  CA  VAL G  38      28.822  89.272  10.769  1.00 30.98           C  
-ATOM  24418  C   VAL G  38      28.631  89.960   9.420  1.00 26.37           C  
-ATOM  24419  O   VAL G  38      27.721  89.609   8.669  1.00 22.48           O  
-ATOM  24420  CB  VAL G  38      28.245  90.178  11.880  1.00 31.15           C  
-ATOM  24421  CG1 VAL G  38      26.904  90.763  11.458  1.00 19.06           C  
-ATOM  24422  CG2 VAL G  38      28.096  89.392  13.167  1.00 32.86           C  
-ATOM  24423  N   THR G  39      29.494  90.919   9.100  1.00 31.16           N  
-ATOM  24424  CA  THR G  39      29.337  91.662   7.853  1.00 35.50           C  
-ATOM  24425  C   THR G  39      29.872  90.912   6.626  1.00 32.41           C  
-ATOM  24426  O   THR G  39      29.496  91.234   5.497  1.00 30.53           O  
-ATOM  24427  CB  THR G  39      30.026  93.046   7.918  1.00 26.21           C  
-ATOM  24428  OG1 THR G  39      31.389  92.898   8.331  1.00 35.40           O  
-ATOM  24429  CG2 THR G  39      29.302  93.966   8.896  1.00 19.08           C  
-ATOM  24430  N   LYS G  40      30.734  89.917   6.830  1.00 33.49           N  
-ATOM  24431  CA  LYS G  40      31.343  89.232   5.687  1.00 33.61           C  
-ATOM  24432  C   LYS G  40      30.692  87.897   5.313  1.00 42.74           C  
-ATOM  24433  O   LYS G  40      30.484  87.629   4.130  1.00 43.34           O  
-ATOM  24434  CB  LYS G  40      32.836  89.009   5.934  1.00 26.09           C  
-ATOM  24435  CG  LYS G  40      33.672  90.268   5.773  1.00 34.85           C  
-ATOM  24436  CD  LYS G  40      35.107  89.954   5.376  1.00 39.22           C  
-ATOM  24437  CE  LYS G  40      35.811  89.100   6.419  1.00 37.65           C  
-ATOM  24438  NZ  LYS G  40      37.227  88.831   6.041  1.00 39.00           N  
-ATOM  24439  N   THR G  41      30.368  87.070   6.305  1.00 40.72           N  
-ATOM  24440  CA  THR G  41      29.930  85.697   6.037  1.00 41.55           C  
-ATOM  24441  C   THR G  41      28.679  85.585   5.167  1.00 47.62           C  
-ATOM  24442  O   THR G  41      27.608  86.091   5.509  1.00 41.99           O  
-ATOM  24443  CB  THR G  41      29.665  84.918   7.342  1.00 52.23           C  
-ATOM  24444  OG1 THR G  41      28.740  85.640   8.165  1.00 52.59           O  
-ATOM  24445  CG2 THR G  41      30.965  84.691   8.105  1.00 48.08           C  
-ATOM  24446  N   THR G  42      28.846  84.902   4.039  1.00 60.60           N  
-ATOM  24447  CA  THR G  42      27.770  84.620   3.099  1.00 64.63           C  
-ATOM  24448  C   THR G  42      27.764  83.119   2.818  1.00 72.35           C  
-ATOM  24449  O   THR G  42      28.834  82.513   2.728  1.00 64.38           O  
-ATOM  24450  CB  THR G  42      27.956  85.410   1.783  1.00 67.46           C  
-ATOM  24451  OG1 THR G  42      28.250  86.780   2.084  1.00 59.65           O  
-ATOM  24452  CG2 THR G  42      26.709  85.342   0.912  1.00 70.15           C  
-ATOM  24453  N   PRO G  43      26.567  82.512   2.712  1.00 76.49           N  
-ATOM  24454  CA  PRO G  43      26.401  81.095   2.362  1.00 73.87           C  
-ATOM  24455  C   PRO G  43      27.313  80.631   1.226  1.00 80.41           C  
-ATOM  24456  O   PRO G  43      27.197  81.141   0.112  1.00 76.57           O  
-ATOM  24457  CB  PRO G  43      24.928  81.010   1.933  1.00 65.63           C  
-ATOM  24458  CG  PRO G  43      24.334  82.396   2.171  1.00 72.12           C  
-ATOM  24459  CD  PRO G  43      25.276  83.112   3.080  1.00 68.70           C  
-ATOM  24460  N   ALA G  46      28.628  82.483  -1.786  1.00 71.93           N  
-ATOM  24461  CA  ALA G  46      29.066  81.763  -2.977  1.00 88.32           C  
-ATOM  24462  C   ALA G  46      29.150  82.697  -4.178  1.00 79.36           C  
-ATOM  24463  O   ALA G  46      30.239  83.064  -4.623  1.00 71.99           O  
-ATOM  24464  CB  ALA G  46      28.125  80.604  -3.274  1.00 80.14           C  
-ATOM  24465  N   SER G  47      27.988  83.078  -4.696  1.00 71.75           N  
-ATOM  24466  CA  SER G  47      27.912  83.951  -5.858  1.00 75.01           C  
-ATOM  24467  C   SER G  47      27.867  85.421  -5.455  1.00 73.88           C  
-ATOM  24468  O   SER G  47      28.332  86.292  -6.193  1.00 57.89           O  
-ATOM  24469  CB  SER G  47      26.681  83.607  -6.698  1.00 81.29           C  
-ATOM  24470  OG  SER G  47      25.494  83.696  -5.925  1.00 67.48           O  
-ATOM  24471  N   ARG G  48      27.315  85.688  -4.276  1.00 73.90           N  
-ATOM  24472  CA  ARG G  48      27.023  87.055  -3.861  1.00 56.14           C  
-ATOM  24473  C   ARG G  48      27.835  87.498  -2.647  1.00 54.73           C  
-ATOM  24474  O   ARG G  48      28.384  86.676  -1.912  1.00 57.82           O  
-ATOM  24475  CB  ARG G  48      25.528  87.190  -3.566  1.00 51.54           C  
-ATOM  24476  CG  ARG G  48      24.650  86.570  -4.642  1.00 61.39           C  
-ATOM  24477  CD  ARG G  48      23.224  86.364  -4.168  1.00 53.74           C  
-ATOM  24478  NE  ARG G  48      22.478  87.615  -4.104  1.00 54.66           N  
-ATOM  24479  CZ  ARG G  48      21.215  87.748  -4.494  1.00 58.52           C  
-ATOM  24480  NH1 ARG G  48      20.558  86.703  -4.980  1.00 60.52           N  
-ATOM  24481  NH2 ARG G  48      20.608  88.924  -4.402  1.00 64.07           N  
-ATOM  24482  N   PHE G  74      27.903  88.810  -2.453  1.00 49.71           N  
-ATOM  24483  CA  PHE G  74      28.597  89.398  -1.315  1.00 49.07           C  
-ATOM  24484  C   PHE G  74      27.644  90.292  -0.533  1.00 46.21           C  
-ATOM  24485  O   PHE G  74      26.528  90.554  -0.979  1.00 43.28           O  
-ATOM  24486  CB  PHE G  74      29.815  90.195  -1.782  1.00 40.74           C  
-ATOM  24487  CG  PHE G  74      29.568  90.998  -3.028  1.00 39.93           C  
-ATOM  24488  CD1 PHE G  74      28.821  92.163  -2.983  1.00 36.28           C  
-ATOM  24489  CD2 PHE G  74      30.083  90.587  -4.245  1.00 47.14           C  
-ATOM  24490  CE1 PHE G  74      28.592  92.901  -4.126  1.00 36.61           C  
-ATOM  24491  CE2 PHE G  74      29.857  91.321  -5.392  1.00 42.01           C  
-ATOM  24492  CZ  PHE G  74      29.110  92.479  -5.332  1.00 40.70           C  
-ATOM  24493  N   ASN G  75      28.081  90.760   0.630  1.00 38.94           N  
-ATOM  24494  CA  ASN G  75      27.261  91.655   1.438  1.00 38.46           C  
-ATOM  24495  C   ASN G  75      27.597  93.122   1.190  1.00 38.29           C  
-ATOM  24496  O   ASN G  75      28.681  93.450   0.705  1.00 34.08           O  
-ATOM  24497  CB  ASN G  75      27.417  91.325   2.923  1.00 34.91           C  
-ATOM  24498  CG  ASN G  75      26.748  90.024   3.302  1.00 37.02           C  
-ATOM  24499  OD1 ASN G  75      25.654  89.715   2.829  1.00 41.65           O  
-ATOM  24500  ND2 ASN G  75      27.403  89.248   4.156  1.00 46.64           N  
-ATOM  24501  N   ALA G  76      26.662  94.005   1.519  1.00 37.61           N  
-ATOM  24502  CA  ALA G  76      26.896  95.431   1.347  1.00 30.97           C  
-ATOM  24503  C   ALA G  76      26.909  96.141   2.693  1.00 31.35           C  
-ATOM  24504  O   ALA G  76      26.034  95.919   3.525  1.00 27.00           O  
-ATOM  24505  CB  ALA G  76      25.842  96.039   0.434  1.00 33.99           C  
-ATOM  24506  N   VAL G  77      27.909  96.989   2.908  1.00 34.78           N  
-ATOM  24507  CA  VAL G  77      27.953  97.816   4.107  1.00 27.16           C  
-ATOM  24508  C   VAL G  77      27.720  99.284   3.754  1.00 32.30           C  
-ATOM  24509  O   VAL G  77      28.402  99.851   2.898  1.00 33.47           O  
-ATOM  24510  CB  VAL G  77      29.293  97.664   4.861  1.00 15.86           C  
-ATOM  24511  CG1 VAL G  77      29.304  96.373   5.655  1.00 22.67           C  
-ATOM  24512  CG2 VAL G  77      30.465  97.707   3.895  1.00 22.18           C  
-ATOM  24513  N   VAL G  78      26.735  99.887   4.410  1.00 24.92           N  
-ATOM  24514  CA  VAL G  78      26.413 101.287   4.187  1.00 28.62           C  
-ATOM  24515  C   VAL G  78      26.806 102.118   5.405  1.00 30.46           C  
-ATOM  24516  O   VAL G  78      26.414 101.811   6.537  1.00 25.93           O  
-ATOM  24517  CB  VAL G  78      24.920 101.483   3.886  1.00 23.73           C  
-ATOM  24518  CG1 VAL G  78      24.647 102.931   3.521  1.00 20.45           C  
-ATOM  24519  CG2 VAL G  78      24.484 100.557   2.760  1.00 13.90           C  
-ATOM  24520  N   MET G  79      27.597 103.160   5.161  1.00 36.11           N  
-ATOM  24521  CA  MET G  79      28.114 104.005   6.228  1.00 27.81           C  
-ATOM  24522  C   MET G  79      28.032 105.484   5.869  1.00 27.05           C  
-ATOM  24523  O   MET G  79      27.859 105.845   4.704  1.00 23.39           O  
-ATOM  24524  CB  MET G  79      29.561 103.629   6.549  1.00 24.29           C  
-ATOM  24525  CG  MET G  79      30.558 104.086   5.503  1.00 21.95           C  
-ATOM  24526  SD  MET G  79      32.159 103.282   5.679  1.00 29.06           S  
-ATOM  24527  CE  MET G  79      31.750 101.619   5.161  1.00 28.20           C  
-ATOM  24528  N   GLY G  80      28.150 106.336   6.882  1.00 32.72           N  
-ATOM  24529  CA  GLY G  80      28.200 107.770   6.672  1.00 28.97           C  
-ATOM  24530  C   GLY G  80      29.608 108.227   6.332  1.00 35.77           C  
-ATOM  24531  O   GLY G  80      30.565 107.459   6.461  1.00 38.35           O  
-ATOM  24532  N   ARG G  81      29.738 109.477   5.900  1.00 23.38           N  
-ATOM  24533  CA  ARG G  81      31.032 110.009   5.493  1.00 22.07           C  
-ATOM  24534  C   ARG G  81      32.036 110.010   6.642  1.00 26.35           C  
-ATOM  24535  O   ARG G  81      33.203 109.639   6.472  1.00 36.77           O  
-ATOM  24536  CB  ARG G  81      30.857 111.423   4.933  1.00 22.92           C  
-ATOM  24537  CG  ARG G  81      32.116 112.034   4.348  1.00 27.53           C  
-ATOM  24538  CD  ARG G  81      32.691 113.101   5.259  1.00 28.48           C  
-ATOM  24539  NE  ARG G  81      31.720 114.149   5.558  1.00 28.97           N  
-ATOM  24540  CZ  ARG G  81      31.918 115.118   6.444  1.00 28.31           C  
-ATOM  24541  NH1 ARG G  81      30.976 116.028   6.653  1.00 37.76           N  
-ATOM  24542  NH2 ARG G  81      33.055 115.178   7.123  1.00 21.40           N  
-ATOM  24543  N   LYS G  82      31.568 110.421   7.815  1.00 29.24           N  
-ATOM  24544  CA  LYS G  82      32.435 110.562   8.979  1.00 31.26           C  
-ATOM  24545  C   LYS G  82      32.925 109.215   9.494  1.00 31.74           C  
-ATOM  24546  O   LYS G  82      34.000 109.129  10.083  1.00 37.10           O  
-ATOM  24547  CB  LYS G  82      31.718 111.316  10.103  1.00 34.81           C  
-ATOM  24548  CG  LYS G  82      31.404 112.762   9.758  1.00 36.25           C  
-ATOM  24549  CD  LYS G  82      30.895 113.539  10.961  1.00 37.29           C  
-ATOM  24550  CE  LYS G  82      30.601 114.982  10.578  1.00 34.90           C  
-ATOM  24551  NZ  LYS G  82      30.167 115.782  11.751  1.00 28.52           N  
-ATOM  24552  N   THR G  83      32.140 108.166   9.281  1.00 27.80           N  
-ATOM  24553  CA  THR G  83      32.554 106.833   9.701  1.00 25.83           C  
-ATOM  24554  C   THR G  83      33.690 106.351   8.801  1.00 35.67           C  
-ATOM  24555  O   THR G  83      34.719 105.847   9.273  1.00 39.88           O  
-ATOM  24556  CB  THR G  83      31.378 105.834   9.657  1.00 25.79           C  
-ATOM  24557  OG1 THR G  83      30.304 106.310  10.480  1.00 22.88           O  
-ATOM  24558  CG2 THR G  83      31.814 104.471  10.150  1.00 32.50           C  
-ATOM  24559  N   TRP G  84      33.486 106.519   7.498  1.00 34.24           N  
-ATOM  24560  CA  TRP G  84      34.510 106.243   6.501  1.00 34.25           C  
-ATOM  24561  C   TRP G  84      35.803 106.981   6.816  1.00 29.78           C  
-ATOM  24562  O   TRP G  84      36.884 106.401   6.752  1.00 30.11           O  
-ATOM  24563  CB  TRP G  84      34.016 106.634   5.106  1.00 30.66           C  
-ATOM  24564  CG  TRP G  84      35.080 106.561   4.054  1.00 34.90           C  
-ATOM  24565  CD1 TRP G  84      35.943 107.555   3.685  1.00 34.75           C  
-ATOM  24566  CD2 TRP G  84      35.400 105.433   3.241  1.00 30.11           C  
-ATOM  24567  NE1 TRP G  84      36.780 107.111   2.689  1.00 30.92           N  
-ATOM  24568  CE2 TRP G  84      36.464 105.808   2.397  1.00 23.97           C  
-ATOM  24569  CE3 TRP G  84      34.888 104.136   3.140  1.00 26.64           C  
-ATOM  24570  CZ2 TRP G  84      37.024 104.939   1.469  1.00 27.48           C  
-ATOM  24571  CZ3 TRP G  84      35.446 103.272   2.216  1.00 31.77           C  
-ATOM  24572  CH2 TRP G  84      36.501 103.677   1.393  1.00 31.40           C  
-ATOM  24573  N   GLU G  85      35.689 108.260   7.157  1.00 30.51           N  
-ATOM  24574  CA  GLU G  85      36.868 109.040   7.504  1.00 31.90           C  
-ATOM  24575  C   GLU G  85      37.462 108.588   8.835  1.00 35.11           C  
-ATOM  24576  O   GLU G  85      38.658 108.782   9.087  1.00 36.57           O  
-ATOM  24577  CB  GLU G  85      36.527 110.530   7.552  1.00 38.68           C  
-ATOM  24578  CG  GLU G  85      36.123 111.106   6.205  1.00 37.45           C  
-ATOM  24579  CD  GLU G  85      35.880 112.599   6.254  1.00 41.48           C  
-ATOM  24580  OE1 GLU G  85      35.687 113.137   7.367  1.00 39.96           O  
-ATOM  24581  OE2 GLU G  85      35.881 113.233   5.176  1.00 38.69           O  
-ATOM  24582  N   SER G  86      36.626 107.989   9.682  1.00 33.55           N  
-ATOM  24583  CA  SER G  86      37.065 107.555  11.005  1.00 32.28           C  
-ATOM  24584  C   SER G  86      37.883 106.278  10.902  1.00 29.14           C  
-ATOM  24585  O   SER G  86      38.815 106.068  11.670  1.00 35.44           O  
-ATOM  24586  CB  SER G  86      35.871 107.347  11.944  1.00 41.08           C  
-ATOM  24587  OG  SER G  86      35.182 106.141  11.649  1.00 44.35           O  
-ATOM  24588  N   MET G  87      37.533 105.428   9.944  1.00 35.61           N  
-ATOM  24589  CA  MET G  87      38.286 104.203   9.717  1.00 37.85           C  
-ATOM  24590  C   MET G  87      39.701 104.505   9.224  1.00 41.62           C  
-ATOM  24591  O   MET G  87      39.921 105.480   8.500  1.00 34.46           O  
-ATOM  24592  CB  MET G  87      37.558 103.305   8.716  1.00 33.81           C  
-ATOM  24593  CG  MET G  87      36.192 102.835   9.190  1.00 33.29           C  
-ATOM  24594  SD  MET G  87      35.344 101.837   7.954  1.00 35.04           S  
-ATOM  24595  CE  MET G  87      36.670 100.742   7.466  1.00 39.52           C  
-ATOM  24596  N   PRO G  88      40.673 103.669   9.628  1.00 50.03           N  
-ATOM  24597  CA  PRO G  88      42.062 103.801   9.172  1.00 50.15           C  
-ATOM  24598  C   PRO G  88      42.195 103.552   7.669  1.00 51.93           C  
-ATOM  24599  O   PRO G  88      41.374 102.836   7.095  1.00 51.53           O  
-ATOM  24600  CB  PRO G  88      42.804 102.723   9.977  1.00 41.21           C  
-ATOM  24601  CG  PRO G  88      41.745 101.746  10.373  1.00 37.92           C  
-ATOM  24602  CD  PRO G  88      40.518 102.569  10.595  1.00 37.77           C  
-ATOM  24603  N   ARG G  89      43.212 104.143   7.048  1.00 52.94           N  
-ATOM  24604  CA  ARG G  89      43.401 104.056   5.601  1.00 52.56           C  
-ATOM  24605  C   ARG G  89      43.543 102.619   5.106  1.00 54.00           C  
-ATOM  24606  O   ARG G  89      42.922 102.230   4.117  1.00 51.90           O  
-ATOM  24607  CB  ARG G  89      44.636 104.855   5.181  1.00 60.43           C  
-ATOM  24608  CG  ARG G  89      44.574 106.340   5.496  1.00 77.08           C  
-ATOM  24609  CD  ARG G  89      44.005 107.138   4.333  1.00 87.38           C  
-ATOM  24610  NE  ARG G  89      44.548 108.494   4.296  1.00 86.11           N  
-ATOM  24611  CZ  ARG G  89      44.025 109.531   4.942  1.00 86.53           C  
-ATOM  24612  NH1 ARG G  89      42.935 109.378   5.681  1.00 76.63           N  
-ATOM  24613  NH2 ARG G  89      44.592 110.726   4.847  1.00 85.20           N  
-ATOM  24614  N   LYS G  90      44.362 101.835   5.801  1.00 56.01           N  
-ATOM  24615  CA  LYS G  90      44.717 100.492   5.349  1.00 56.23           C  
-ATOM  24616  C   LYS G  90      43.537  99.523   5.378  1.00 48.05           C  
-ATOM  24617  O   LYS G  90      43.544  98.506   4.687  1.00 54.19           O  
-ATOM  24618  CB  LYS G  90      45.861  99.939   6.203  1.00 60.25           C  
-ATOM  24619  CG  LYS G  90      45.429  99.430   7.573  1.00 72.14           C  
-ATOM  24620  CD  LYS G  90      46.373  99.891   8.675  1.00 73.69           C  
-ATOM  24621  CE  LYS G  90      46.251 101.388   8.923  1.00 63.25           C  
-ATOM  24622  NZ  LYS G  90      47.028 101.817  10.119  1.00 47.05           N  
-ATOM  24623  N   PHE G  91      42.525  99.841   6.177  1.00 44.15           N  
-ATOM  24624  CA  PHE G  91      41.395  98.942   6.363  1.00 49.24           C  
-ATOM  24625  C   PHE G  91      40.209  99.292   5.470  1.00 52.04           C  
-ATOM  24626  O   PHE G  91      39.257  98.517   5.361  1.00 48.06           O  
-ATOM  24627  CB  PHE G  91      40.958  98.943   7.829  1.00 57.56           C  
-ATOM  24628  CG  PHE G  91      41.621  97.883   8.662  1.00 69.74           C  
-ATOM  24629  CD1 PHE G  91      41.901  96.638   8.124  1.00 80.81           C  
-ATOM  24630  CD2 PHE G  91      41.963  98.130   9.982  1.00 72.21           C  
-ATOM  24631  CE1 PHE G  91      42.509  95.656   8.887  1.00 77.34           C  
-ATOM  24632  CE2 PHE G  91      42.570  97.152  10.751  1.00 77.16           C  
-ATOM  24633  CZ  PHE G  91      42.843  95.914  10.202  1.00 73.86           C  
-ATOM  24634  N   ARG G  92      40.261 100.457   4.832  1.00 49.86           N  
-ATOM  24635  CA  ARG G  92      39.150 100.887   3.993  1.00 39.57           C  
-ATOM  24636  C   ARG G  92      39.539 100.948   2.518  1.00 34.89           C  
-ATOM  24637  O   ARG G  92      40.661 101.324   2.180  1.00 45.50           O  
-ATOM  24638  CB  ARG G  92      38.613 102.242   4.461  1.00 38.30           C  
-ATOM  24639  CG  ARG G  92      39.493 103.434   4.149  1.00 36.43           C  
-ATOM  24640  CD  ARG G  92      38.904 104.691   4.763  1.00 38.93           C  
-ATOM  24641  NE  ARG G  92      39.617 105.896   4.355  1.00 43.64           N  
-ATOM  24642  CZ  ARG G  92      39.830 106.941   5.148  1.00 48.51           C  
-ATOM  24643  NH1 ARG G  92      40.485 107.998   4.689  1.00 55.02           N  
-ATOM  24644  NH2 ARG G  92      39.392 106.929   6.400  1.00 48.03           N  
-ATOM  24645  N   PRO G  93      38.611 100.562   1.629  1.00 33.80           N  
-ATOM  24646  CA  PRO G  93      37.264 100.066   1.940  1.00 29.92           C  
-ATOM  24647  C   PRO G  93      37.276  98.677   2.571  1.00 31.17           C  
-ATOM  24648  O   PRO G  93      38.244  97.935   2.402  1.00 43.89           O  
-ATOM  24649  CB  PRO G  93      36.582 100.032   0.573  1.00 32.25           C  
-ATOM  24650  CG  PRO G  93      37.697  99.858  -0.395  1.00 33.03           C  
-ATOM  24651  CD  PRO G  93      38.845 100.636   0.176  1.00 42.33           C  
-ATOM  24652  N   LEU G  94      36.222  98.348   3.308  1.00 30.18           N  
-ATOM  24653  CA  LEU G  94      36.121  97.047   3.951  1.00 33.58           C  
-ATOM  24654  C   LEU G  94      36.145  95.945   2.900  1.00 33.88           C  
-ATOM  24655  O   LEU G  94      35.303  95.906   2.003  1.00 39.57           O  
-ATOM  24656  CB  LEU G  94      34.853  96.970   4.806  1.00 38.33           C  
-ATOM  24657  CG  LEU G  94      34.881  97.819   6.082  1.00 27.67           C  
-ATOM  24658  CD1 LEU G  94      33.495  97.951   6.689  1.00 29.10           C  
-ATOM  24659  CD2 LEU G  94      35.855  97.238   7.099  1.00 26.23           C  
-ATOM  24660  N   VAL G  95      37.132  95.063   3.013  1.00 34.12           N  
-ATOM  24661  CA  VAL G  95      37.372  94.025   2.016  1.00 41.43           C  
-ATOM  24662  C   VAL G  95      36.204  93.053   1.864  1.00 42.73           C  
-ATOM  24663  O   VAL G  95      35.503  92.751   2.831  1.00 43.57           O  
-ATOM  24664  CB  VAL G  95      38.638  93.221   2.358  1.00 38.82           C  
-ATOM  24665  CG1 VAL G  95      39.883  94.037   2.045  1.00 37.09           C  
-ATOM  24666  CG2 VAL G  95      38.618  92.803   3.822  1.00 43.28           C  
-ATOM  24667  N   ASP G  96      36.001  92.585   0.633  1.00 44.66           N  
-ATOM  24668  CA  ASP G  96      34.995  91.570   0.310  1.00 38.71           C  
-ATOM  24669  C   ASP G  96      33.568  92.018   0.620  1.00 29.62           C  
-ATOM  24670  O   ASP G  96      32.644  91.204   0.636  1.00 34.59           O  
-ATOM  24671  CB  ASP G  96      35.304  90.265   1.048  1.00 35.82           C  
-ATOM  24672  CG  ASP G  96      36.711  89.766   0.780  1.00 44.29           C  
-ATOM  24673  OD1 ASP G  96      37.209  89.970  -0.350  1.00 44.18           O  
-ATOM  24674  OD2 ASP G  96      37.321  89.178   1.698  1.00 38.49           O  
-ATOM  24675  N   ARG G  97      33.394  93.313   0.857  1.00 28.91           N  
-ATOM  24676  CA  ARG G  97      32.076  93.884   1.102  1.00 30.22           C  
-ATOM  24677  C   ARG G  97      31.871  95.109   0.224  1.00 28.03           C  
-ATOM  24678  O   ARG G  97      32.767  95.943   0.087  1.00 24.76           O  
-ATOM  24679  CB  ARG G  97      31.908  94.258   2.574  1.00 28.06           C  
-ATOM  24680  CG  ARG G  97      31.739  93.073   3.509  1.00 24.52           C  
-ATOM  24681  CD  ARG G  97      32.185  93.420   4.921  1.00 24.01           C  
-ATOM  24682  NE  ARG G  97      33.634  93.584   4.999  1.00 33.38           N  
-ATOM  24683  CZ  ARG G  97      34.315  93.740   6.130  1.00 27.45           C  
-ATOM  24684  NH1 ARG G  97      33.683  93.755   7.293  1.00 32.21           N  
-ATOM  24685  NH2 ARG G  97      35.633  93.880   6.098  1.00 30.82           N  
-ATOM  24686  N   LEU G  98      30.694  95.211  -0.381  1.00 27.42           N  
-ATOM  24687  CA  LEU G  98      30.366  96.379  -1.182  1.00 28.40           C  
-ATOM  24688  C   LEU G  98      30.221  97.590  -0.276  1.00 31.71           C  
-ATOM  24689  O   LEU G  98      29.322  97.645   0.562  1.00 28.73           O  
-ATOM  24690  CB  LEU G  98      29.083  96.155  -1.983  1.00 29.96           C  
-ATOM  24691  CG  LEU G  98      28.505  97.407  -2.645  1.00 36.65           C  
-ATOM  24692  CD1 LEU G  98      29.500  98.014  -3.624  1.00 37.73           C  
-ATOM  24693  CD2 LEU G  98      27.189  97.092  -3.335  1.00 37.59           C  
-ATOM  24694  N   ASN G  99      31.114  98.557  -0.438  1.00 30.94           N  
-ATOM  24695  CA  ASN G  99      31.068  99.757   0.387  1.00 31.68           C  
-ATOM  24696  C   ASN G  99      30.245 100.878  -0.238  1.00 33.51           C  
-ATOM  24697  O   ASN G  99      30.534 101.347  -1.344  1.00 43.85           O  
-ATOM  24698  CB  ASN G  99      32.483 100.260   0.683  1.00 32.32           C  
-ATOM  24699  CG  ASN G  99      33.197  99.416   1.723  1.00 32.94           C  
-ATOM  24700  OD1 ASN G  99      33.200  98.187   1.648  1.00 38.35           O  
-ATOM  24701  ND2 ASN G  99      33.798 100.074   2.707  1.00 22.42           N  
-ATOM  24702  N   ILE G 100      29.212 101.300   0.481  1.00 25.07           N  
-ATOM  24703  CA  ILE G 100      28.423 102.451   0.076  1.00 27.73           C  
-ATOM  24704  C   ILE G 100      28.535 103.537   1.131  1.00 29.60           C  
-ATOM  24705  O   ILE G 100      28.237 103.310   2.301  1.00 34.55           O  
-ATOM  24706  CB  ILE G 100      26.939 102.096  -0.139  1.00 24.50           C  
-ATOM  24707  CG1 ILE G 100      26.783 101.106  -1.294  1.00 25.64           C  
-ATOM  24708  CG2 ILE G 100      26.130 103.354  -0.411  1.00 25.76           C  
-ATOM  24709  CD1 ILE G 100      25.342 100.808  -1.643  1.00 17.15           C  
-ATOM  24710  N   VAL G 101      28.976 104.715   0.710  1.00 27.80           N  
-ATOM  24711  CA  VAL G 101      29.119 105.841   1.614  1.00 22.69           C  
-ATOM  24712  C   VAL G 101      28.079 106.903   1.297  1.00 25.91           C  
-ATOM  24713  O   VAL G 101      27.911 107.297   0.144  1.00 26.89           O  
-ATOM  24714  CB  VAL G 101      30.525 106.460   1.530  1.00 19.52           C  
-ATOM  24715  CG1 VAL G 101      30.666 107.590   2.538  1.00 24.32           C  
-ATOM  24716  CG2 VAL G 101      31.590 105.395   1.757  1.00 16.83           C  
-ATOM  24717  N   VAL G 102      27.374 107.351   2.330  1.00 27.07           N  
-ATOM  24718  CA  VAL G 102      26.372 108.397   2.183  1.00 25.03           C  
-ATOM  24719  C   VAL G 102      26.976 109.761   2.487  1.00 31.34           C  
-ATOM  24720  O   VAL G 102      27.381 110.035   3.617  1.00 27.06           O  
-ATOM  24721  CB  VAL G 102      25.160 108.157   3.102  1.00 24.52           C  
-ATOM  24722  CG1 VAL G 102      24.207 109.339   3.049  1.00 26.69           C  
-ATOM  24723  CG2 VAL G 102      24.453 106.870   2.713  1.00 26.59           C  
-ATOM  24724  N   SER G 103      27.036 110.610   1.468  1.00 42.52           N  
-ATOM  24725  CA  SER G 103      27.614 111.940   1.608  1.00 38.30           C  
-ATOM  24726  C   SER G 103      27.168 112.842   0.464  1.00 38.64           C  
-ATOM  24727  O   SER G 103      26.680 112.365  -0.560  1.00 42.07           O  
-ATOM  24728  CB  SER G 103      29.143 111.856   1.652  1.00 34.09           C  
-ATOM  24729  OG  SER G 103      29.725 113.132   1.845  1.00 34.83           O  
-ATOM  24730  N   SER G 104      27.332 114.148   0.644  1.00 38.68           N  
-ATOM  24731  CA  SER G 104      27.027 115.099  -0.417  1.00 41.75           C  
-ATOM  24732  C   SER G 104      28.269 115.901  -0.781  1.00 47.41           C  
-ATOM  24733  O   SER G 104      28.323 116.543  -1.831  1.00 56.09           O  
-ATOM  24734  CB  SER G 104      25.888 116.028  -0.001  1.00 35.88           C  
-ATOM  24735  OG  SER G 104      24.648 115.341  -0.016  1.00 39.18           O  
-ATOM  24736  N   SER G 105      29.270 115.851   0.092  1.00 37.77           N  
-ATOM  24737  CA  SER G 105      30.540 116.518  -0.160  1.00 42.04           C  
-ATOM  24738  C   SER G 105      31.528 115.559  -0.821  1.00 47.40           C  
-ATOM  24739  O   SER G 105      32.211 115.925  -1.779  1.00 51.92           O  
-ATOM  24740  CB  SER G 105      31.120 117.082   1.141  1.00 41.98           C  
-ATOM  24741  OG  SER G 105      31.231 116.082   2.137  1.00 42.09           O  
-ATOM  24742  N   LEU G 106      31.596 114.333  -0.311  1.00 39.42           N  
-ATOM  24743  CA  LEU G 106      32.462 113.314  -0.895  1.00 45.81           C  
-ATOM  24744  C   LEU G 106      31.938 112.834  -2.243  1.00 42.54           C  
-ATOM  24745  O   LEU G 106      30.729 112.766  -2.464  1.00 42.84           O  
-ATOM  24746  CB  LEU G 106      32.613 112.118   0.049  1.00 47.97           C  
-ATOM  24747  CG  LEU G 106      33.793 112.131   1.024  1.00 45.60           C  
-ATOM  24748  CD1 LEU G 106      34.037 110.735   1.577  1.00 34.54           C  
-ATOM  24749  CD2 LEU G 106      35.049 112.672   0.356  1.00 47.00           C  
-ATOM  24750  N   LYS G 107      32.860 112.501  -3.140  1.00 39.61           N  
-ATOM  24751  CA  LYS G 107      32.497 111.955  -4.441  1.00 48.62           C  
-ATOM  24752  C   LYS G 107      33.174 110.606  -4.633  1.00 51.05           C  
-ATOM  24753  O   LYS G 107      34.058 110.237  -3.859  1.00 53.24           O  
-ATOM  24754  CB  LYS G 107      32.886 112.917  -5.565  1.00 57.76           C  
-ATOM  24755  CG  LYS G 107      32.401 114.343  -5.352  1.00 69.66           C  
-ATOM  24756  CD  LYS G 107      32.505 115.162  -6.626  1.00 71.78           C  
-ATOM  24757  CE  LYS G 107      31.158 115.769  -6.987  1.00 83.64           C  
-ATOM  24758  NZ  LYS G 107      30.103 114.724  -7.129  1.00 64.43           N  
-ATOM  24759  N   GLU G 108      32.761 109.871  -5.660  1.00 37.89           N  
-ATOM  24760  CA  GLU G 108      33.290 108.534  -5.892  1.00 34.89           C  
-ATOM  24761  C   GLU G 108      34.766 108.569  -6.269  1.00 39.58           C  
-ATOM  24762  O   GLU G 108      35.531 107.686  -5.889  1.00 48.77           O  
-ATOM  24763  CB  GLU G 108      32.475 107.822  -6.974  1.00 42.90           C  
-ATOM  24764  CG  GLU G 108      31.057 107.486  -6.542  1.00 41.55           C  
-ATOM  24765  CD  GLU G 108      30.312 106.646  -7.560  1.00 44.80           C  
-ATOM  24766  OE1 GLU G 108      30.865 106.387  -8.652  1.00 40.35           O  
-ATOM  24767  OE2 GLU G 108      29.167 106.245  -7.263  1.00 45.80           O  
-ATOM  24768  N   GLU G 109      35.167 109.599  -7.005  1.00 43.29           N  
-ATOM  24769  CA  GLU G 109      36.562 109.744  -7.401  1.00 49.91           C  
-ATOM  24770  C   GLU G 109      37.437 110.220  -6.250  1.00 40.61           C  
-ATOM  24771  O   GLU G 109      38.652 110.018  -6.261  1.00 43.49           O  
-ATOM  24772  CB  GLU G 109      36.689 110.704  -8.583  1.00 51.63           C  
-ATOM  24773  CG  GLU G 109      36.697 110.004  -9.930  1.00 79.04           C  
-ATOM  24774  CD  GLU G 109      37.774 108.931 -10.031  1.00 78.92           C  
-ATOM  24775  OE1 GLU G 109      37.491 107.852 -10.596  1.00 73.88           O  
-ATOM  24776  OE2 GLU G 109      38.903 109.166  -9.547  1.00 62.39           O  
-ATOM  24777  N   ASP G 110      36.818 110.863  -5.268  1.00 39.31           N  
-ATOM  24778  CA  ASP G 110      37.525 111.258  -4.059  1.00 38.07           C  
-ATOM  24779  C   ASP G 110      38.028 110.019  -3.333  1.00 43.29           C  
-ATOM  24780  O   ASP G 110      39.126 110.008  -2.778  1.00 47.26           O  
-ATOM  24781  CB  ASP G 110      36.618 112.089  -3.148  1.00 42.99           C  
-ATOM  24782  CG  ASP G 110      36.552 113.544  -3.563  1.00 53.40           C  
-ATOM  24783  OD1 ASP G 110      37.617 114.116  -3.877  1.00 60.72           O  
-ATOM  24784  OD2 ASP G 110      35.440 114.113  -3.580  1.00 45.73           O  
-ATOM  24785  N   ILE G 111      37.214 108.972  -3.357  1.00 40.60           N  
-ATOM  24786  CA  ILE G 111      37.564 107.711  -2.725  1.00 35.11           C  
-ATOM  24787  C   ILE G 111      38.455 106.882  -3.641  1.00 32.79           C  
-ATOM  24788  O   ILE G 111      39.397 106.235  -3.189  1.00 37.83           O  
-ATOM  24789  CB  ILE G 111      36.299 106.916  -2.346  1.00 32.57           C  
-ATOM  24790  CG1 ILE G 111      35.581 107.608  -1.185  1.00 29.57           C  
-ATOM  24791  CG2 ILE G 111      36.649 105.482  -1.985  1.00 31.86           C  
-ATOM  24792  CD1 ILE G 111      34.275 106.960  -0.795  1.00 28.12           C  
-ATOM  24793  N   ALA G 112      38.162 106.927  -4.936  1.00 36.77           N  
-ATOM  24794  CA  ALA G 112      38.935 106.189  -5.929  1.00 39.19           C  
-ATOM  24795  C   ALA G 112      40.396 106.626  -5.930  1.00 40.24           C  
-ATOM  24796  O   ALA G 112      41.299 105.796  -6.044  1.00 35.80           O  
-ATOM  24797  CB  ALA G 112      38.331 106.372  -7.311  1.00 40.81           C  
-ATOM  24798  N   ALA G 113      40.620 107.930  -5.793  1.00 43.45           N  
-ATOM  24799  CA  ALA G 113      41.970 108.483  -5.838  1.00 43.66           C  
-ATOM  24800  C   ALA G 113      42.670 108.406  -4.484  1.00 48.21           C  
-ATOM  24801  O   ALA G 113      43.846 108.754  -4.368  1.00 58.15           O  
-ATOM  24802  CB  ALA G 113      41.929 109.923  -6.329  1.00 35.41           C  
-ATOM  24803  N   GLU G 114      41.947 107.953  -3.465  1.00 44.08           N  
-ATOM  24804  CA  GLU G 114      42.503 107.836  -2.120  1.00 47.20           C  
-ATOM  24805  C   GLU G 114      43.417 106.616  -2.003  1.00 52.82           C  
-ATOM  24806  O   GLU G 114      44.421 106.641  -1.288  1.00 54.04           O  
-ATOM  24807  CB  GLU G 114      41.377 107.757  -1.087  1.00 52.13           C  
-ATOM  24808  CG  GLU G 114      41.845 107.660   0.355  1.00 55.49           C  
-ATOM  24809  CD  GLU G 114      40.688 107.576   1.332  1.00 63.70           C  
-ATOM  24810  OE1 GLU G 114      40.725 106.705   2.227  1.00 61.63           O  
-ATOM  24811  OE2 GLU G 114      39.740 108.381   1.204  1.00 59.50           O  
-ATOM  24812  N   LYS G 115      43.058 105.553  -2.717  1.00 49.34           N  
-ATOM  24813  CA  LYS G 115      43.826 104.313  -2.725  1.00 46.08           C  
-ATOM  24814  C   LYS G 115      43.424 103.467  -3.929  1.00 52.15           C  
-ATOM  24815  O   LYS G 115      42.233 103.312  -4.208  1.00 49.27           O  
-ATOM  24816  CB  LYS G 115      43.607 103.527  -1.428  1.00 41.90           C  
-ATOM  24817  CG  LYS G 115      44.233 102.141  -1.424  1.00 41.14           C  
-ATOM  24818  CD  LYS G 115      43.558 101.221  -0.417  1.00 43.79           C  
-ATOM  24819  CE  LYS G 115      43.751 101.710   1.007  1.00 37.60           C  
-ATOM  24820  NZ  LYS G 115      43.235 100.725   1.999  1.00 42.91           N  
-ATOM  24821  N   PRO G 116      44.416 102.921  -4.650  1.00 45.75           N  
-ATOM  24822  CA  PRO G 116      44.145 102.077  -5.819  1.00 38.91           C  
-ATOM  24823  C   PRO G 116      43.241 100.892  -5.495  1.00 47.09           C  
-ATOM  24824  O   PRO G 116      43.509 100.141  -4.555  1.00 46.27           O  
-ATOM  24825  CB  PRO G 116      45.541 101.600  -6.243  1.00 33.29           C  
-ATOM  24826  CG  PRO G 116      46.423 101.852  -5.057  1.00 34.46           C  
-ATOM  24827  CD  PRO G 116      45.860 103.069  -4.406  1.00 42.83           C  
-ATOM  24828  N   GLN G 117      42.174 100.741  -6.270  1.00 52.14           N  
-ATOM  24829  CA  GLN G 117      41.251  99.630  -6.097  1.00 50.79           C  
-ATOM  24830  C   GLN G 117      41.948  98.292  -6.329  1.00 57.53           C  
-ATOM  24831  O   GLN G 117      42.560  98.072  -7.375  1.00 50.80           O  
-ATOM  24832  CB  GLN G 117      40.063  99.774  -7.047  1.00 46.25           C  
-ATOM  24833  CG  GLN G 117      39.145  98.566  -7.072  1.00 61.79           C  
-ATOM  24834  CD  GLN G 117      38.027  98.709  -8.085  1.00 70.61           C  
-ATOM  24835  OE1 GLN G 117      37.427  97.721  -8.508  1.00 66.64           O  
-ATOM  24836  NE2 GLN G 117      37.739  99.944  -8.478  1.00 78.45           N  
-ATOM  24837  N   ALA G 118      41.861  97.405  -5.344  1.00 63.40           N  
-ATOM  24838  CA  ALA G 118      42.446  96.078  -5.468  1.00 50.44           C  
-ATOM  24839  C   ALA G 118      41.630  95.246  -6.443  1.00 53.30           C  
-ATOM  24840  O   ALA G 118      40.436  95.482  -6.623  1.00 62.37           O  
-ATOM  24841  CB  ALA G 118      42.523  95.393  -4.113  1.00 46.07           C  
-ATOM  24842  N   GLU G 119      42.278  94.276  -7.077  1.00 58.61           N  
-ATOM  24843  CA  GLU G 119      41.598  93.414  -8.033  1.00 64.85           C  
-ATOM  24844  C   GLU G 119      40.610  92.496  -7.320  1.00 60.01           C  
-ATOM  24845  O   GLU G 119      40.896  91.975  -6.241  1.00 47.47           O  
-ATOM  24846  CB  GLU G 119      42.616  92.598  -8.836  1.00 71.48           C  
-ATOM  24847  CG  GLU G 119      42.010  91.694  -9.903  1.00 74.70           C  
-ATOM  24848  CD  GLU G 119      41.780  90.275  -9.410  1.00 91.66           C  
-ATOM  24849  OE1 GLU G 119      40.657  89.756  -9.591  1.00 82.11           O  
-ATOM  24850  OE2 GLU G 119      42.723  89.679  -8.845  1.00 79.59           O  
-ATOM  24851  N   GLY G 120      39.441  92.316  -7.926  1.00 57.91           N  
-ATOM  24852  CA  GLY G 120      38.422  91.435  -7.387  1.00 66.16           C  
-ATOM  24853  C   GLY G 120      37.500  92.114  -6.393  1.00 56.29           C  
-ATOM  24854  O   GLY G 120      36.503  91.536  -5.961  1.00 50.87           O  
-ATOM  24855  N   GLN G 121      37.833  93.347  -6.029  1.00 51.68           N  
-ATOM  24856  CA  GLN G 121      37.047  94.092  -5.056  1.00 46.99           C  
-ATOM  24857  C   GLN G 121      36.074  95.045  -5.742  1.00 56.17           C  
-ATOM  24858  O   GLN G 121      36.306  95.482  -6.870  1.00 60.74           O  
-ATOM  24859  CB  GLN G 121      37.967  94.864  -4.111  1.00 48.97           C  
-ATOM  24860  CG  GLN G 121      38.836  93.974  -3.241  1.00 48.80           C  
-ATOM  24861  CD  GLN G 121      38.028  93.192  -2.226  1.00 47.98           C  
-ATOM  24862  OE1 GLN G 121      37.113  93.727  -1.600  1.00 48.74           O  
-ATOM  24863  NE2 GLN G 121      38.359  91.917  -2.060  1.00 40.80           N  
-ATOM  24864  N   GLN G 122      34.981  95.355  -5.053  1.00 54.69           N  
-ATOM  24865  CA  GLN G 122      33.964  96.257  -5.578  1.00 47.92           C  
-ATOM  24866  C   GLN G 122      34.423  97.704  -5.514  1.00 46.73           C  
-ATOM  24867  O   GLN G 122      35.150  98.094  -4.600  1.00 46.34           O  
-ATOM  24868  CB  GLN G 122      32.656  96.096  -4.802  1.00 46.83           C  
-ATOM  24869  CG  GLN G 122      31.498  95.583  -5.635  1.00 51.17           C  
-ATOM  24870  CD  GLN G 122      31.778  94.225  -6.240  1.00 54.81           C  
-ATOM  24871  OE1 GLN G 122      32.502  93.410  -5.665  1.00 49.42           O  
-ATOM  24872  NE2 GLN G 122      31.205  93.973  -7.411  1.00 54.90           N  
-ATOM  24873  N   ARG G 123      34.000  98.503  -6.486  1.00 47.45           N  
-ATOM  24874  CA  ARG G 123      34.291  99.924  -6.443  1.00 39.89           C  
-ATOM  24875  C   ARG G 123      33.374 100.560  -5.403  1.00 35.68           C  
-ATOM  24876  O   ARG G 123      32.202 100.196  -5.283  1.00 36.62           O  
-ATOM  24877  CB  ARG G 123      34.124 100.570  -7.825  1.00 41.48           C  
-ATOM  24878  CG  ARG G 123      32.768 101.201  -8.102  1.00 58.85           C  
-ATOM  24879  CD  ARG G 123      32.737 101.845  -9.478  1.00 58.94           C  
-ATOM  24880  NE  ARG G 123      33.965 102.589  -9.747  1.00 76.08           N  
-ATOM  24881  CZ  ARG G 123      34.119 103.892  -9.531  1.00 81.75           C  
-ATOM  24882  NH1 ARG G 123      35.280 104.476  -9.803  1.00 71.11           N  
-ATOM  24883  NH2 ARG G 123      33.116 104.613  -9.046  1.00 78.83           N  
-ATOM  24884  N   VAL G 124      33.924 101.484  -4.625  1.00 41.47           N  
-ATOM  24885  CA  VAL G 124      33.164 102.132  -3.564  1.00 34.00           C  
-ATOM  24886  C   VAL G 124      32.157 103.105  -4.157  1.00 32.58           C  
-ATOM  24887  O   VAL G 124      32.503 103.929  -5.005  1.00 39.84           O  
-ATOM  24888  CB  VAL G 124      34.081 102.882  -2.582  1.00 29.70           C  
-ATOM  24889  CG1 VAL G 124      33.270 103.457  -1.434  1.00 22.06           C  
-ATOM  24890  CG2 VAL G 124      35.156 101.953  -2.058  1.00 28.09           C  
-ATOM  24891  N   ARG G 125      30.909 103.007  -3.714  1.00 33.10           N  
-ATOM  24892  CA  ARG G 125      29.859 103.866  -4.248  1.00 36.72           C  
-ATOM  24893  C   ARG G 125      29.518 104.997  -3.282  1.00 35.10           C  
-ATOM  24894  O   ARG G 125      29.723 104.876  -2.077  1.00 35.03           O  
-ATOM  24895  CB  ARG G 125      28.607 103.047  -4.559  1.00 30.72           C  
-ATOM  24896  CG  ARG G 125      27.892 103.487  -5.813  1.00 35.09           C  
-ATOM  24897  CD  ARG G 125      28.654 103.077  -7.058  1.00 33.74           C  
-ATOM  24898  NE  ARG G 125      27.905 103.405  -8.265  1.00 36.01           N  
-ATOM  24899  CZ  ARG G 125      26.990 102.610  -8.810  1.00 42.69           C  
-ATOM  24900  NH1 ARG G 125      26.351 102.985  -9.910  1.00 35.79           N  
-ATOM  24901  NH2 ARG G 125      26.715 101.438  -8.253  1.00 44.61           N  
-ATOM  24902  N   VAL G 126      29.002 106.099  -3.816  1.00 31.61           N  
-ATOM  24903  CA  VAL G 126      28.616 107.237  -2.986  1.00 26.31           C  
-ATOM  24904  C   VAL G 126      27.193 107.699  -3.287  1.00 24.05           C  
-ATOM  24905  O   VAL G 126      26.877 108.076  -4.414  1.00 21.60           O  
-ATOM  24906  CB  VAL G 126      29.573 108.429  -3.173  1.00 26.17           C  
-ATOM  24907  CG1 VAL G 126      29.082 109.632  -2.386  1.00 29.04           C  
-ATOM  24908  CG2 VAL G 126      30.982 108.051  -2.744  1.00 32.93           C  
-ATOM  24909  N   CYS G 127      26.337 107.671  -2.271  1.00 24.63           N  
-ATOM  24910  CA  CYS G 127      24.955 108.113  -2.422  1.00 21.17           C  
-ATOM  24911  C   CYS G 127      24.677 109.347  -1.568  1.00 22.56           C  
-ATOM  24912  O   CYS G 127      25.402 109.628  -0.614  1.00 24.17           O  
-ATOM  24913  CB  CYS G 127      23.991 106.982  -2.053  1.00 31.99           C  
-ATOM  24914  SG  CYS G 127      24.343 105.400  -2.865  1.00 25.58           S  
-ATOM  24915  N   ALA G 128      23.621 110.077  -1.913  1.00 31.98           N  
-ATOM  24916  CA  ALA G 128      23.291 111.320  -1.222  1.00 29.80           C  
-ATOM  24917  C   ALA G 128      22.358 111.091  -0.038  1.00 30.22           C  
-ATOM  24918  O   ALA G 128      22.089 112.012   0.734  1.00 39.89           O  
-ATOM  24919  CB  ALA G 128      22.670 112.311  -2.189  1.00 23.03           C  
-ATOM  24920  N   SER G 129      21.860 109.866   0.097  1.00 30.76           N  
-ATOM  24921  CA  SER G 129      20.983 109.521   1.210  1.00 30.65           C  
-ATOM  24922  C   SER G 129      20.808 108.017   1.333  1.00 36.99           C  
-ATOM  24923  O   SER G 129      21.249 107.260   0.472  1.00 42.61           O  
-ATOM  24924  CB  SER G 129      19.618 110.192   1.047  1.00 34.46           C  
-ATOM  24925  OG  SER G 129      18.949 109.699  -0.101  1.00 41.43           O  
-ATOM  24926  N   LEU G 130      20.165 107.593   2.413  1.00 27.55           N  
-ATOM  24927  CA  LEU G 130      19.892 106.183   2.635  1.00 29.65           C  
-ATOM  24928  C   LEU G 130      18.861 105.613   1.652  1.00 30.31           C  
-ATOM  24929  O   LEU G 130      19.049 104.499   1.155  1.00 37.87           O  
-ATOM  24930  CB  LEU G 130      19.430 105.957   4.075  1.00 29.52           C  
-ATOM  24931  CG  LEU G 130      19.424 104.495   4.519  1.00 27.46           C  
-ATOM  24932  CD1 LEU G 130      20.820 103.920   4.388  1.00 18.35           C  
-ATOM  24933  CD2 LEU G 130      18.926 104.370   5.943  1.00 25.37           C  
-ATOM  24934  N   PRO G 131      17.763 106.352   1.379  1.00 27.39           N  
-ATOM  24935  CA  PRO G 131      16.880 105.851   0.319  1.00 40.46           C  
-ATOM  24936  C   PRO G 131      17.588 105.771  -1.032  1.00 39.69           C  
-ATOM  24937  O   PRO G 131      17.253 104.908  -1.847  1.00 34.79           O  
-ATOM  24938  CB  PRO G 131      15.748 106.884   0.289  1.00 36.66           C  
-ATOM  24939  CG  PRO G 131      15.712 107.432   1.668  1.00 27.59           C  
-ATOM  24940  CD  PRO G 131      17.149 107.485   2.099  1.00 29.02           C  
-ATOM  24941  N   ALA G 132      18.552 106.660  -1.259  1.00 31.62           N  
-ATOM  24942  CA  ALA G 132      19.367 106.604  -2.466  1.00 34.16           C  
-ATOM  24943  C   ALA G 132      20.207 105.341  -2.473  1.00 41.15           C  
-ATOM  24944  O   ALA G 132      20.331 104.672  -3.497  1.00 45.89           O  
-ATOM  24945  CB  ALA G 132      20.258 107.824  -2.570  1.00 27.57           C  
-ATOM  24946  N   ALA G 133      20.787 105.032  -1.318  1.00 35.04           N  
-ATOM  24947  CA  ALA G 133      21.595 103.834  -1.144  1.00 28.33           C  
-ATOM  24948  C   ALA G 133      20.792 102.583  -1.460  1.00 37.36           C  
-ATOM  24949  O   ALA G 133      21.242 101.722  -2.218  1.00 38.28           O  
-ATOM  24950  CB  ALA G 133      22.139 103.761   0.272  1.00 22.54           C  
-ATOM  24951  N   LEU G 134      19.604 102.491  -0.870  1.00 41.12           N  
-ATOM  24952  CA  LEU G 134      18.737 101.334  -1.058  1.00 36.26           C  
-ATOM  24953  C   LEU G 134      18.233 101.216  -2.495  1.00 36.89           C  
-ATOM  24954  O   LEU G 134      18.185 100.119  -3.057  1.00 37.77           O  
-ATOM  24955  CB  LEU G 134      17.557 101.407  -0.089  1.00 36.63           C  
-ATOM  24956  CG  LEU G 134      17.917 101.437   1.399  1.00 30.12           C  
-ATOM  24957  CD1 LEU G 134      16.660 101.428   2.254  1.00 28.63           C  
-ATOM  24958  CD2 LEU G 134      18.823 100.270   1.753  1.00 26.43           C  
-ATOM  24959  N   SER G 135      17.850 102.347  -3.079  1.00 36.76           N  
-ATOM  24960  CA  SER G 135      17.407 102.376  -4.468  1.00 35.99           C  
-ATOM  24961  C   SER G 135      18.515 101.886  -5.391  1.00 42.39           C  
-ATOM  24962  O   SER G 135      18.262 101.122  -6.323  1.00 46.02           O  
-ATOM  24963  CB  SER G 135      16.967 103.785  -4.871  1.00 40.31           C  
-ATOM  24964  OG  SER G 135      15.842 104.209  -4.122  1.00 54.62           O  
-ATOM  24965  N   LEU G 136      19.740 102.332  -5.124  1.00 42.75           N  
-ATOM  24966  CA  LEU G 136      20.908 101.883  -5.872  1.00 37.09           C  
-ATOM  24967  C   LEU G 136      21.101 100.378  -5.718  1.00 36.80           C  
-ATOM  24968  O   LEU G 136      21.326  99.658  -6.693  1.00 45.11           O  
-ATOM  24969  CB  LEU G 136      22.156 102.631  -5.399  1.00 34.57           C  
-ATOM  24970  CG  LEU G 136      23.483 102.196  -6.015  1.00 30.52           C  
-ATOM  24971  CD1 LEU G 136      23.688 102.829  -7.381  1.00 28.28           C  
-ATOM  24972  CD2 LEU G 136      24.624 102.537  -5.082  1.00 34.98           C  
-ATOM  24973  N   LEU G 137      21.000  99.920  -4.476  1.00 36.03           N  
-ATOM  24974  CA  LEU G 137      21.145  98.511  -4.140  1.00 42.05           C  
-ATOM  24975  C   LEU G 137      20.143  97.639  -4.887  1.00 44.26           C  
-ATOM  24976  O   LEU G 137      20.473  96.532  -5.306  1.00 42.70           O  
-ATOM  24977  CB  LEU G 137      20.988  98.305  -2.629  1.00 38.79           C  
-ATOM  24978  CG  LEU G 137      22.214  97.855  -1.827  1.00 32.90           C  
-ATOM  24979  CD1 LEU G 137      23.480  97.858  -2.673  1.00 28.28           C  
-ATOM  24980  CD2 LEU G 137      22.378  98.734  -0.595  1.00 31.74           C  
-ATOM  24981  N   GLU G 138      18.922  98.133  -5.051  1.00 45.90           N  
-ATOM  24982  CA  GLU G 138      17.899  97.368  -5.753  1.00 48.11           C  
-ATOM  24983  C   GLU G 138      18.062  97.470  -7.267  1.00 50.00           C  
-ATOM  24984  O   GLU G 138      17.758  96.526  -7.998  1.00 59.89           O  
-ATOM  24985  CB  GLU G 138      16.500  97.838  -5.340  1.00 49.75           C  
-ATOM  24986  CG  GLU G 138      15.742  96.856  -4.448  1.00 65.96           C  
-ATOM  24987  CD  GLU G 138      15.332  95.586  -5.182  1.00 78.83           C  
-ATOM  24988  OE1 GLU G 138      15.170  95.639  -6.419  1.00 70.35           O  
-ATOM  24989  OE2 GLU G 138      15.177  94.531  -4.527  1.00 77.70           O  
-ATOM  24990  N   GLU G 139      18.547  98.614  -7.735  1.00 44.07           N  
-ATOM  24991  CA  GLU G 139      18.616  98.866  -9.167  1.00 44.54           C  
-ATOM  24992  C   GLU G 139      19.810  98.199  -9.844  1.00 35.68           C  
-ATOM  24993  O   GLU G 139      19.665  97.627 -10.920  1.00 44.35           O  
-ATOM  24994  CB  GLU G 139      18.635 100.372  -9.434  1.00 53.62           C  
-ATOM  24995  CG  GLU G 139      17.292 100.905  -9.919  1.00 70.12           C  
-ATOM  24996  CD  GLU G 139      16.965 102.281  -9.370  1.00 81.18           C  
-ATOM  24997  OE1 GLU G 139      17.847 103.166  -9.403  1.00 74.48           O  
-ATOM  24998  OE2 GLU G 139      15.822 102.476  -8.903  1.00 78.07           O  
-ATOM  24999  N   GLU G 140      20.983  98.260  -9.221  1.00 38.83           N  
-ATOM  25000  CA  GLU G 140      22.184  97.719  -9.852  1.00 40.76           C  
-ATOM  25001  C   GLU G 140      22.918  96.661  -9.030  1.00 46.29           C  
-ATOM  25002  O   GLU G 140      24.046  96.296  -9.361  1.00 52.53           O  
-ATOM  25003  CB  GLU G 140      23.161  98.851 -10.176  1.00 31.93           C  
-ATOM  25004  CG  GLU G 140      22.599 100.247 -10.014  1.00 30.19           C  
-ATOM  25005  CD  GLU G 140      23.574 101.303 -10.488  1.00 36.86           C  
-ATOM  25006  OE1 GLU G 140      23.175 102.479 -10.624  1.00 30.72           O  
-ATOM  25007  OE2 GLU G 140      24.747 100.951 -10.730  1.00 38.91           O  
-ATOM  25008  N   TYR G 141      22.298  96.165  -7.967  1.00 52.67           N  
-ATOM  25009  CA  TYR G 141      22.977  95.177  -7.138  1.00 52.99           C  
-ATOM  25010  C   TYR G 141      22.080  94.028  -6.691  1.00 63.66           C  
-ATOM  25011  O   TYR G 141      22.477  93.224  -5.849  1.00 63.83           O  
-ATOM  25012  CB  TYR G 141      23.600  95.850  -5.915  1.00 45.42           C  
-ATOM  25013  CG  TYR G 141      24.853  96.637  -6.231  1.00 43.83           C  
-ATOM  25014  CD1 TYR G 141      26.026  95.993  -6.609  1.00 39.23           C  
-ATOM  25015  CD2 TYR G 141      24.866  98.021  -6.144  1.00 44.91           C  
-ATOM  25016  CE1 TYR G 141      27.176  96.710  -6.896  1.00 36.01           C  
-ATOM  25017  CE2 TYR G 141      26.009  98.746  -6.427  1.00 42.32           C  
-ATOM  25018  CZ  TYR G 141      27.161  98.088  -6.802  1.00 36.63           C  
-ATOM  25019  OH  TYR G 141      28.294  98.819  -7.082  1.00 31.12           O  
-ATOM  25020  N   LYS G 142      20.877  93.945  -7.249  1.00 70.00           N  
-ATOM  25021  CA  LYS G 142      20.054  92.762  -7.039  1.00 66.83           C  
-ATOM  25022  C   LYS G 142      20.707  91.599  -7.756  1.00 69.22           C  
-ATOM  25023  O   LYS G 142      21.317  91.792  -8.806  1.00 76.62           O  
-ATOM  25024  CB  LYS G 142      18.625  92.979  -7.533  1.00 70.25           C  
-ATOM  25025  CG  LYS G 142      17.698  93.515  -6.461  1.00 75.15           C  
-ATOM  25026  CD  LYS G 142      17.849  92.720  -5.166  1.00 89.89           C  
-ATOM  25027  CE  LYS G 142      18.356  93.592  -4.019  1.00 84.04           C  
-ATOM  25028  NZ  LYS G 142      18.785  92.778  -2.842  1.00 57.97           N  
-ATOM  25029  N   ASP G 143      20.607  90.410  -7.161  1.00 64.75           N  
-ATOM  25030  CA  ASP G 143      21.254  89.197  -7.667  1.00 77.38           C  
-ATOM  25031  C   ASP G 143      22.780  89.306  -7.495  1.00 71.46           C  
-ATOM  25032  O   ASP G 143      23.533  88.380  -7.810  1.00 69.59           O  
-ATOM  25033  CB  ASP G 143      20.838  88.933  -9.131  1.00 82.95           C  
-ATOM  25034  CG  ASP G 143      22.010  88.925 -10.100  1.00103.71           C  
-ATOM  25035  OD1 ASP G 143      22.550  90.011 -10.416  1.00 95.72           O  
-ATOM  25036  OD2 ASP G 143      22.376  87.823 -10.562  1.00115.54           O  
-ATOM  25037  N   SER G 144      23.218  90.431  -6.935  1.00 59.79           N  
-ATOM  25038  CA  SER G 144      24.629  90.685  -6.676  1.00 51.52           C  
-ATOM  25039  C   SER G 144      24.926  90.741  -5.178  1.00 52.48           C  
-ATOM  25040  O   SER G 144      25.948  90.228  -4.723  1.00 45.98           O  
-ATOM  25041  CB  SER G 144      25.063  91.991  -7.345  1.00 54.53           C  
-ATOM  25042  OG  SER G 144      26.403  92.313  -7.021  1.00 48.92           O  
-ATOM  25043  N   VAL G 145      24.036  91.367  -4.412  1.00 60.08           N  
-ATOM  25044  CA  VAL G 145      24.226  91.470  -2.968  1.00 45.55           C  
-ATOM  25045  C   VAL G 145      23.243  90.588  -2.205  1.00 41.37           C  
-ATOM  25046  O   VAL G 145      22.125  90.342  -2.661  1.00 46.37           O  
-ATOM  25047  CB  VAL G 145      24.086  92.926  -2.472  1.00 42.88           C  
-ATOM  25048  CG1 VAL G 145      25.102  93.823  -3.164  1.00 49.81           C  
-ATOM  25049  CG2 VAL G 145      22.670  93.444  -2.689  1.00 46.70           C  
-ATOM  25050  N   ASP G 146      23.671  90.108  -1.042  1.00 38.38           N  
-ATOM  25051  CA  ASP G 146      22.812  89.293  -0.192  1.00 46.81           C  
-ATOM  25052  C   ASP G 146      22.211  90.135   0.929  1.00 52.48           C  
-ATOM  25053  O   ASP G 146      21.034  90.496   0.882  1.00 51.23           O  
-ATOM  25054  CB  ASP G 146      23.588  88.105   0.389  1.00 44.74           C  
-ATOM  25055  CG  ASP G 146      22.708  87.175   1.214  1.00 52.67           C  
-ATOM  25056  OD1 ASP G 146      21.470  87.201   1.038  1.00 41.79           O  
-ATOM  25057  OD2 ASP G 146      23.256  86.409   2.034  1.00 58.66           O  
-ATOM  25058  N   GLN G 147      23.022  90.452   1.934  1.00 50.49           N  
-ATOM  25059  CA  GLN G 147      22.542  91.227   3.071  1.00 40.55           C  
-ATOM  25060  C   GLN G 147      23.052  92.664   3.052  1.00 34.66           C  
-ATOM  25061  O   GLN G 147      24.148  92.949   2.558  1.00 33.95           O  
-ATOM  25062  CB  GLN G 147      22.938  90.552   4.386  1.00 41.62           C  
-ATOM  25063  CG  GLN G 147      22.349  89.164   4.577  1.00 45.06           C  
-ATOM  25064  CD  GLN G 147      22.179  88.800   6.040  1.00 49.69           C  
-ATOM  25065  OE1 GLN G 147      22.856  87.911   6.554  1.00 48.20           O  
-ATOM  25066  NE2 GLN G 147      21.267  89.487   6.718  1.00 50.44           N  
-ATOM  25067  N   ILE G 148      22.238  93.564   3.594  1.00 34.74           N  
-ATOM  25068  CA  ILE G 148      22.599  94.968   3.693  1.00 31.88           C  
-ATOM  25069  C   ILE G 148      22.753  95.366   5.156  1.00 32.63           C  
-ATOM  25070  O   ILE G 148      21.832  95.192   5.957  1.00 43.25           O  
-ATOM  25071  CB  ILE G 148      21.551  95.869   3.018  1.00 33.42           C  
-ATOM  25072  CG1 ILE G 148      21.314  95.418   1.576  1.00 25.93           C  
-ATOM  25073  CG2 ILE G 148      21.993  97.325   3.067  1.00 29.75           C  
-ATOM  25074  CD1 ILE G 148      20.207  96.171   0.881  1.00 18.49           C  
-ATOM  25075  N   PHE G 149      23.925  95.889   5.497  1.00 33.77           N  
-ATOM  25076  CA  PHE G 149      24.238  96.263   6.870  1.00 33.12           C  
-ATOM  25077  C   PHE G 149      24.463  97.763   7.021  1.00 27.23           C  
-ATOM  25078  O   PHE G 149      25.385  98.314   6.425  1.00 25.17           O  
-ATOM  25079  CB  PHE G 149      25.488  95.525   7.363  1.00 28.62           C  
-ATOM  25080  CG  PHE G 149      25.318  94.039   7.489  1.00 28.06           C  
-ATOM  25081  CD1 PHE G 149      24.752  93.488   8.626  1.00 29.28           C  
-ATOM  25082  CD2 PHE G 149      25.746  93.190   6.481  1.00 32.16           C  
-ATOM  25083  CE1 PHE G 149      24.603  92.116   8.751  1.00 42.03           C  
-ATOM  25084  CE2 PHE G 149      25.600  91.817   6.599  1.00 36.33           C  
-ATOM  25085  CZ  PHE G 149      25.028  91.280   7.735  1.00 34.72           C  
-ATOM  25086  N   VAL G 150      23.632  98.425   7.820  1.00 26.66           N  
-ATOM  25087  CA  VAL G 150      23.924  99.798   8.211  1.00 24.11           C  
-ATOM  25088  C   VAL G 150      24.961  99.759   9.331  1.00 28.20           C  
-ATOM  25089  O   VAL G 150      24.770  99.092  10.362  1.00 30.08           O  
-ATOM  25090  CB  VAL G 150      22.670 100.560   8.665  1.00 25.78           C  
-ATOM  25091  CG1 VAL G 150      23.048 101.940   9.186  1.00 27.26           C  
-ATOM  25092  CG2 VAL G 150      21.690 100.680   7.515  1.00 22.89           C  
-ATOM  25093  N   VAL G 151      26.056 100.481   9.114  1.00 29.35           N  
-ATOM  25094  CA  VAL G 151      27.263 100.317   9.915  1.00 22.99           C  
-ATOM  25095  C   VAL G 151      27.606 101.565  10.740  1.00 26.03           C  
-ATOM  25096  O   VAL G 151      28.228 101.466  11.803  1.00 31.44           O  
-ATOM  25097  CB  VAL G 151      28.441  99.918   8.989  1.00 22.36           C  
-ATOM  25098  CG1 VAL G 151      29.785 100.309   9.567  1.00 33.14           C  
-ATOM  25099  CG2 VAL G 151      28.387  98.426   8.698  1.00 20.76           C  
-ATOM  25100  N   GLY G 152      27.169 102.731  10.276  1.00 21.56           N  
-ATOM  25101  CA  GLY G 152      27.365 103.961  11.025  1.00 25.14           C  
-ATOM  25102  C   GLY G 152      27.226 105.217  10.183  1.00 31.28           C  
-ATOM  25103  O   GLY G 152      27.323 105.158   8.962  1.00 36.94           O  
-ATOM  25104  N   GLY G 153      26.997 106.358  10.829  1.00 24.92           N  
-ATOM  25105  CA  GLY G 153      26.872 106.429  12.271  1.00 18.41           C  
-ATOM  25106  C   GLY G 153      25.494 106.914  12.668  1.00 23.08           C  
-ATOM  25107  O   GLY G 153      24.497 106.435  12.137  1.00 28.54           O  
-ATOM  25108  N   ALA G 154      25.445 107.880  13.581  1.00 20.51           N  
-ATOM  25109  CA  ALA G 154      24.190 108.372  14.151  1.00 20.53           C  
-ATOM  25110  C   ALA G 154      23.157 108.778  13.102  1.00 24.46           C  
-ATOM  25111  O   ALA G 154      21.968 108.514  13.262  1.00 24.83           O  
-ATOM  25112  CB  ALA G 154      24.467 109.543  15.078  1.00 27.98           C  
-ATOM  25113  N   GLY G 155      23.615 109.421  12.034  1.00 29.16           N  
-ATOM  25114  CA  GLY G 155      22.733 109.842  10.962  1.00 29.07           C  
-ATOM  25115  C   GLY G 155      22.077 108.673  10.256  1.00 30.63           C  
-ATOM  25116  O   GLY G 155      20.858 108.646  10.077  1.00 37.06           O  
-ATOM  25117  N   LEU G 156      22.886 107.697   9.858  1.00 28.89           N  
-ATOM  25118  CA  LEU G 156      22.364 106.528   9.158  1.00 31.88           C  
-ATOM  25119  C   LEU G 156      21.499 105.656  10.057  1.00 28.39           C  
-ATOM  25120  O   LEU G 156      20.537 105.056   9.590  1.00 28.65           O  
-ATOM  25121  CB  LEU G 156      23.498 105.687   8.571  1.00 23.32           C  
-ATOM  25122  CG  LEU G 156      24.208 106.255   7.341  1.00 23.45           C  
-ATOM  25123  CD1 LEU G 156      24.691 105.119   6.460  1.00 24.22           C  
-ATOM  25124  CD2 LEU G 156      23.308 107.204   6.563  1.00 26.40           C  
-ATOM  25125  N   TYR G 157      21.848 105.576  11.337  1.00 21.78           N  
-ATOM  25126  CA  TYR G 157      21.045 104.825  12.295  1.00 22.10           C  
-ATOM  25127  C   TYR G 157      19.685 105.486  12.453  1.00 26.52           C  
-ATOM  25128  O   TYR G 157      18.650 104.824  12.376  1.00 26.74           O  
-ATOM  25129  CB  TYR G 157      21.753 104.728  13.649  1.00 23.10           C  
-ATOM  25130  CG  TYR G 157      23.049 103.950  13.604  1.00 22.41           C  
-ATOM  25131  CD1 TYR G 157      23.171 102.813  12.820  1.00 20.69           C  
-ATOM  25132  CD2 TYR G 157      24.151 104.356  14.342  1.00 28.88           C  
-ATOM  25133  CE1 TYR G 157      24.350 102.101  12.776  1.00 23.86           C  
-ATOM  25134  CE2 TYR G 157      25.338 103.655  14.301  1.00 21.86           C  
-ATOM  25135  CZ  TYR G 157      25.431 102.531  13.514  1.00 20.84           C  
-ATOM  25136  OH  TYR G 157      26.610 101.831  13.484  1.00 28.76           O  
-ATOM  25137  N   GLU G 158      19.706 106.798  12.672  1.00 29.32           N  
-ATOM  25138  CA  GLU G 158      18.489 107.592  12.803  1.00 32.04           C  
-ATOM  25139  C   GLU G 158      17.585 107.430  11.586  1.00 29.22           C  
-ATOM  25140  O   GLU G 158      16.388 107.182  11.724  1.00 32.72           O  
-ATOM  25141  CB  GLU G 158      18.835 109.073  13.010  1.00 34.93           C  
-ATOM  25142  CG  GLU G 158      17.631 110.009  13.049  1.00 60.73           C  
-ATOM  25143  CD  GLU G 158      16.945 110.054  14.409  1.00 71.48           C  
-ATOM  25144  OE1 GLU G 158      16.148 110.989  14.643  1.00 81.12           O  
-ATOM  25145  OE2 GLU G 158      17.199 109.161  15.246  1.00 63.44           O  
-ATOM  25146  N   ALA G 159      18.169 107.567  10.399  1.00 28.22           N  
-ATOM  25147  CA  ALA G 159      17.419 107.450   9.154  1.00 28.08           C  
-ATOM  25148  C   ALA G 159      16.838 106.052   8.975  1.00 26.82           C  
-ATOM  25149  O   ALA G 159      15.665 105.897   8.641  1.00 31.47           O  
-ATOM  25150  CB  ALA G 159      18.304 107.805   7.970  1.00 31.43           C  
-ATOM  25151  N   ALA G 160      17.672 105.040   9.200  1.00 27.28           N  
-ATOM  25152  CA  ALA G 160      17.275 103.645   9.037  1.00 29.78           C  
-ATOM  25153  C   ALA G 160      16.166 103.259  10.004  1.00 32.69           C  
-ATOM  25154  O   ALA G 160      15.311 102.435   9.682  1.00 38.37           O  
-ATOM  25155  CB  ALA G 160      18.473 102.730   9.222  1.00 24.83           C  
-ATOM  25156  N   LEU G 161      16.191 103.849  11.193  1.00 32.34           N  
-ATOM  25157  CA  LEU G 161      15.149 103.605  12.177  1.00 26.14           C  
-ATOM  25158  C   LEU G 161      13.884 104.358  11.796  1.00 26.21           C  
-ATOM  25159  O   LEU G 161      12.774 103.883  12.031  1.00 27.70           O  
-ATOM  25160  CB  LEU G 161      15.620 104.011  13.573  1.00 33.75           C  
-ATOM  25161  CG  LEU G 161      16.039 102.870  14.505  1.00 23.25           C  
-ATOM  25162  CD1 LEU G 161      16.243 101.577  13.737  1.00 14.15           C  
-ATOM  25163  CD2 LEU G 161      17.301 103.241  15.271  1.00 32.21           C  
-ATOM  25164  N   SER G 162      14.060 105.530  11.195  1.00 33.63           N  
-ATOM  25165  CA  SER G 162      12.931 106.335  10.745  1.00 35.77           C  
-ATOM  25166  C   SER G 162      12.155 105.614   9.648  1.00 37.54           C  
-ATOM  25167  O   SER G 162      10.936 105.479   9.728  1.00 43.05           O  
-ATOM  25168  CB  SER G 162      13.407 107.702  10.251  1.00 32.59           C  
-ATOM  25169  OG  SER G 162      13.885 108.492  11.328  1.00 61.74           O  
-ATOM  25170  N   LEU G 163      12.873 105.139   8.636  1.00 33.13           N  
-ATOM  25171  CA  LEU G 163      12.271 104.409   7.527  1.00 31.09           C  
-ATOM  25172  C   LEU G 163      11.594 103.126   7.991  1.00 34.80           C  
-ATOM  25173  O   LEU G 163      10.669 102.637   7.344  1.00 41.40           O  
-ATOM  25174  CB  LEU G 163      13.330 104.081   6.473  1.00 27.98           C  
-ATOM  25175  CG  LEU G 163      14.063 105.289   5.895  1.00 32.31           C  
-ATOM  25176  CD1 LEU G 163      15.146 104.857   4.916  1.00 33.99           C  
-ATOM  25177  CD2 LEU G 163      13.070 106.231   5.235  1.00 36.12           C  
-ATOM  25178  N   GLY G 164      12.058 102.581   9.111  1.00 38.23           N  
-ATOM  25179  CA  GLY G 164      11.516 101.339   9.626  1.00 43.54           C  
-ATOM  25180  C   GLY G 164      11.951 100.160   8.779  1.00 41.48           C  
-ATOM  25181  O   GLY G 164      11.228  99.173   8.649  1.00 53.55           O  
-ATOM  25182  N   VAL G 165      13.142 100.271   8.200  1.00 34.38           N  
-ATOM  25183  CA  VAL G 165      13.677  99.237   7.324  1.00 38.96           C  
-ATOM  25184  C   VAL G 165      14.532  98.241   8.102  1.00 39.71           C  
-ATOM  25185  O   VAL G 165      14.904  97.186   7.584  1.00 45.94           O  
-ATOM  25186  CB  VAL G 165      14.513  99.850   6.183  1.00 38.79           C  
-ATOM  25187  CG1 VAL G 165      13.606 100.529   5.169  1.00 43.42           C  
-ATOM  25188  CG2 VAL G 165      15.524 100.841   6.736  1.00 29.18           C  
-ATOM  25189  N   ALA G 166      14.836  98.580   9.351  1.00 33.06           N  
-ATOM  25190  CA  ALA G 166      15.675  97.737  10.193  1.00 33.78           C  
-ATOM  25191  C   ALA G 166      14.892  96.561  10.765  1.00 36.48           C  
-ATOM  25192  O   ALA G 166      13.926  96.744  11.504  1.00 40.99           O  
-ATOM  25193  CB  ALA G 166      16.286  98.557  11.314  1.00 36.08           C  
-ATOM  25194  N   SER G 167      15.319  95.353  10.420  1.00 31.49           N  
-ATOM  25195  CA  SER G 167      14.677  94.145  10.917  1.00 28.68           C  
-ATOM  25196  C   SER G 167      15.394  93.611  12.150  1.00 32.70           C  
-ATOM  25197  O   SER G 167      14.760  93.107  13.081  1.00 40.52           O  
-ATOM  25198  CB  SER G 167      14.641  93.074   9.827  1.00 30.65           C  
-ATOM  25199  OG  SER G 167      15.951  92.719   9.422  1.00 31.53           O  
-ATOM  25200  N   HIS G 168      16.719  93.727  12.147  1.00 30.58           N  
-ATOM  25201  CA  HIS G 168      17.540  93.221  13.240  1.00 30.30           C  
-ATOM  25202  C   HIS G 168      18.627  94.203  13.663  1.00 33.57           C  
-ATOM  25203  O   HIS G 168      19.213  94.893  12.828  1.00 35.40           O  
-ATOM  25204  CB  HIS G 168      18.176  91.888  12.848  1.00 24.76           C  
-ATOM  25205  CG  HIS G 168      17.187  90.778  12.682  1.00 41.19           C  
-ATOM  25206  ND1 HIS G 168      16.520  90.548  11.498  1.00 55.65           N  
-ATOM  25207  CD2 HIS G 168      16.741  89.844  13.554  1.00 46.85           C  
-ATOM  25208  CE1 HIS G 168      15.711  89.513  11.646  1.00 54.43           C  
-ATOM  25209  NE2 HIS G 168      15.826  89.068  12.884  1.00 37.83           N  
-ATOM  25210  N   LEU G 169      18.895  94.255  14.965  1.00 24.82           N  
-ATOM  25211  CA  LEU G 169      19.963  95.100  15.488  1.00 20.75           C  
-ATOM  25212  C   LEU G 169      21.067  94.270  16.137  1.00 27.46           C  
-ATOM  25213  O   LEU G 169      20.864  93.676  17.193  1.00 29.42           O  
-ATOM  25214  CB  LEU G 169      19.415  96.101  16.508  1.00 15.68           C  
-ATOM  25215  CG  LEU G 169      18.244  96.994  16.105  1.00 24.47           C  
-ATOM  25216  CD1 LEU G 169      17.985  98.033  17.188  1.00 23.32           C  
-ATOM  25217  CD2 LEU G 169      18.499  97.662  14.766  1.00 32.14           C  
-ATOM  25218  N   TYR G 170      22.236  94.226  15.507  1.00 28.77           N  
-ATOM  25219  CA  TYR G 170      23.392  93.575  16.114  1.00 22.07           C  
-ATOM  25220  C   TYR G 170      24.103  94.547  17.048  1.00 23.44           C  
-ATOM  25221  O   TYR G 170      24.984  95.294  16.623  1.00 23.26           O  
-ATOM  25222  CB  TYR G 170      24.363  93.065  15.048  1.00 20.95           C  
-ATOM  25223  CG  TYR G 170      23.829  91.924  14.212  1.00 26.35           C  
-ATOM  25224  CD1 TYR G 170      23.174  92.166  13.011  1.00 38.37           C  
-ATOM  25225  CD2 TYR G 170      23.989  90.604  14.618  1.00 30.59           C  
-ATOM  25226  CE1 TYR G 170      22.688  91.125  12.241  1.00 35.87           C  
-ATOM  25227  CE2 TYR G 170      23.505  89.558  13.854  1.00 24.31           C  
-ATOM  25228  CZ  TYR G 170      22.857  89.824  12.668  1.00 27.55           C  
-ATOM  25229  OH  TYR G 170      22.377  88.783  11.908  1.00 22.45           O  
-ATOM  25230  N   ILE G 171      23.721  94.539  18.321  1.00 20.36           N  
-ATOM  25231  CA  ILE G 171      24.268  95.501  19.275  1.00 19.68           C  
-ATOM  25232  C   ILE G 171      25.351  94.904  20.157  1.00 20.90           C  
-ATOM  25233  O   ILE G 171      25.161  93.847  20.753  1.00 22.45           O  
-ATOM  25234  CB  ILE G 171      23.173  96.079  20.192  1.00 25.05           C  
-ATOM  25235  CG1 ILE G 171      22.066  96.739  19.366  1.00 18.95           C  
-ATOM  25236  CG2 ILE G 171      23.777  97.069  21.182  1.00 22.49           C  
-ATOM  25237  CD1 ILE G 171      21.112  97.565  20.192  1.00 12.29           C  
-ATOM  25238  N   THR G 172      26.484  95.591  20.244  1.00 16.01           N  
-ATOM  25239  CA  THR G 172      27.529  95.198  21.176  1.00 16.18           C  
-ATOM  25240  C   THR G 172      27.497  96.116  22.389  1.00 17.61           C  
-ATOM  25241  O   THR G 172      28.055  97.213  22.362  1.00 22.82           O  
-ATOM  25242  CB  THR G 172      28.926  95.241  20.531  1.00 22.35           C  
-ATOM  25243  OG1 THR G 172      28.948  94.395  19.375  1.00 23.81           O  
-ATOM  25244  CG2 THR G 172      29.981  94.764  21.515  1.00 21.09           C  
-ATOM  25245  N   ARG G 173      26.826  95.665  23.445  1.00 19.37           N  
-ATOM  25246  CA  ARG G 173      26.716  96.439  24.677  1.00 20.39           C  
-ATOM  25247  C   ARG G 173      28.044  96.519  25.404  1.00 16.40           C  
-ATOM  25248  O   ARG G 173      28.499  95.533  25.991  1.00 18.88           O  
-ATOM  25249  CB  ARG G 173      25.667  95.838  25.609  1.00 15.26           C  
-ATOM  25250  CG  ARG G 173      24.320  95.620  24.962  1.00 16.49           C  
-ATOM  25251  CD  ARG G 173      23.716  94.327  25.455  1.00 19.89           C  
-ATOM  25252  NE  ARG G 173      22.813  94.514  26.582  1.00 14.39           N  
-ATOM  25253  CZ  ARG G 173      22.567  93.586  27.500  1.00 15.75           C  
-ATOM  25254  NH1 ARG G 173      23.174  92.409  27.443  1.00 12.89           N  
-ATOM  25255  NH2 ARG G 173      21.723  93.842  28.486  1.00 31.99           N  
-ATOM  25256  N   VAL G 174      28.659  97.695  25.336  1.00 15.07           N  
-ATOM  25257  CA  VAL G 174      29.826  98.021  26.139  1.00 15.79           C  
-ATOM  25258  C   VAL G 174      29.342  98.423  27.525  1.00 17.87           C  
-ATOM  25259  O   VAL G 174      28.520  99.325  27.653  1.00 19.52           O  
-ATOM  25260  CB  VAL G 174      30.644  99.161  25.511  1.00 16.20           C  
-ATOM  25261  CG1 VAL G 174      31.839  99.503  26.379  1.00 17.81           C  
-ATOM  25262  CG2 VAL G 174      31.081  98.785  24.099  1.00 14.51           C  
-ATOM  25263  N   ALA G 175      29.832  97.752  28.561  1.00 16.92           N  
-ATOM  25264  CA  ALA G 175      29.304  97.963  29.909  1.00 19.23           C  
-ATOM  25265  C   ALA G 175      29.836  99.237  30.566  1.00 17.66           C  
-ATOM  25266  O   ALA G 175      29.169  99.825  31.418  1.00 16.00           O  
-ATOM  25267  CB  ALA G 175      29.608  96.758  30.784  1.00 21.86           C  
-ATOM  25268  N   ARG G 176      31.035  99.657  30.176  1.00 16.07           N  
-ATOM  25269  CA  ARG G 176      31.640 100.864  30.732  1.00 17.00           C  
-ATOM  25270  C   ARG G 176      31.112 102.121  30.060  1.00 17.24           C  
-ATOM  25271  O   ARG G 176      30.733 102.103  28.891  1.00 20.20           O  
-ATOM  25272  CB  ARG G 176      33.159 100.827  30.591  1.00 24.86           C  
-ATOM  25273  CG  ARG G 176      33.859  99.897  31.552  1.00 25.72           C  
-ATOM  25274  CD  ARG G 176      35.365  99.925  31.337  1.00 25.35           C  
-ATOM  25275  NE  ARG G 176      35.926 101.265  31.489  1.00 24.31           N  
-ATOM  25276  CZ  ARG G 176      37.229 101.532  31.493  1.00 22.65           C  
-ATOM  25277  NH1 ARG G 176      37.650 102.781  31.634  1.00 43.68           N  
-ATOM  25278  NH2 ARG G 176      38.111 100.551  31.359  1.00 17.99           N  
-ATOM  25279  N   GLU G 177      31.098 103.217  30.805  1.00 19.42           N  
-ATOM  25280  CA  GLU G 177      30.730 104.501  30.238  1.00 16.53           C  
-ATOM  25281  C   GLU G 177      31.990 105.241  29.811  1.00 25.67           C  
-ATOM  25282  O   GLU G 177      32.996 105.238  30.521  1.00 35.73           O  
-ATOM  25283  CB  GLU G 177      29.924 105.327  31.238  1.00 23.22           C  
-ATOM  25284  CG  GLU G 177      29.107 106.423  30.588  1.00 22.91           C  
-ATOM  25285  CD  GLU G 177      28.256 105.901  29.449  1.00 32.47           C  
-ATOM  25286  OE1 GLU G 177      27.274 105.175  29.719  1.00 37.74           O  
-ATOM  25287  OE2 GLU G 177      28.580 106.208  28.282  1.00 33.83           O  
-ATOM  25288  N   PHE G 178      31.939 105.856  28.636  1.00 27.34           N  
-ATOM  25289  CA  PHE G 178      33.074 106.602  28.113  1.00 17.37           C  
-ATOM  25290  C   PHE G 178      32.632 107.982  27.649  1.00 20.08           C  
-ATOM  25291  O   PHE G 178      31.455 108.191  27.355  1.00 21.00           O  
-ATOM  25292  CB  PHE G 178      33.736 105.839  26.961  1.00 19.28           C  
-ATOM  25293  CG  PHE G 178      34.527 104.642  27.401  1.00 23.42           C  
-ATOM  25294  CD1 PHE G 178      33.920 103.405  27.535  1.00 23.50           C  
-ATOM  25295  CD2 PHE G 178      35.880 104.752  27.675  1.00 27.53           C  
-ATOM  25296  CE1 PHE G 178      34.646 102.302  27.935  1.00 24.04           C  
-ATOM  25297  CE2 PHE G 178      36.613 103.651  28.078  1.00 28.76           C  
-ATOM  25298  CZ  PHE G 178      35.993 102.424  28.210  1.00 30.76           C  
-ATOM  25299  N   PRO G 179      33.575 108.937  27.603  1.00 19.42           N  
-ATOM  25300  CA  PRO G 179      33.298 110.243  27.000  1.00 24.93           C  
-ATOM  25301  C   PRO G 179      32.820 110.096  25.556  1.00 25.22           C  
-ATOM  25302  O   PRO G 179      33.511 109.481  24.743  1.00 18.50           O  
-ATOM  25303  CB  PRO G 179      34.654 110.951  27.066  1.00 21.29           C  
-ATOM  25304  CG  PRO G 179      35.332 110.330  28.235  1.00 19.38           C  
-ATOM  25305  CD  PRO G 179      34.906 108.890  28.233  1.00 15.83           C  
-ATOM  25306  N   CYS G 180      31.648 110.648  25.252  1.00 22.18           N  
-ATOM  25307  CA  CYS G 180      31.065 110.524  23.919  1.00 26.29           C  
-ATOM  25308  C   CYS G 180      30.424 111.823  23.437  1.00 26.92           C  
-ATOM  25309  O   CYS G 180      29.909 112.606  24.236  1.00 29.21           O  
-ATOM  25310  CB  CYS G 180      30.025 109.402  23.902  1.00 28.17           C  
-ATOM  25311  SG  CYS G 180      30.707 107.759  24.185  1.00 30.62           S  
-ATOM  25312  N   ASP G 181      30.455 112.046  22.126  1.00 23.40           N  
-ATOM  25313  CA  ASP G 181      29.804 113.210  21.537  1.00 26.23           C  
-ATOM  25314  C   ASP G 181      28.828 112.797  20.436  1.00 26.29           C  
-ATOM  25315  O   ASP G 181      28.125 113.632  19.868  1.00 28.78           O  
-ATOM  25316  CB  ASP G 181      30.843 114.197  20.991  1.00 24.45           C  
-ATOM  25317  CG  ASP G 181      31.830 113.551  20.030  1.00 27.50           C  
-ATOM  25318  OD1 ASP G 181      31.483 112.536  19.394  1.00 35.45           O  
-ATOM  25319  OD2 ASP G 181      32.962 114.068  19.904  1.00 32.47           O  
-ATOM  25320  N   VAL G 182      28.800 111.502  20.135  1.00 22.71           N  
-ATOM  25321  CA  VAL G 182      27.879 110.954  19.142  1.00 22.50           C  
-ATOM  25322  C   VAL G 182      27.174 109.723  19.703  1.00 16.00           C  
-ATOM  25323  O   VAL G 182      27.823 108.769  20.129  1.00 15.66           O  
-ATOM  25324  CB  VAL G 182      28.603 110.579  17.834  1.00 27.38           C  
-ATOM  25325  CG1 VAL G 182      27.663 109.836  16.899  1.00 26.54           C  
-ATOM  25326  CG2 VAL G 182      29.162 111.822  17.158  1.00 24.89           C  
-ATOM  25327  N   PHE G 183      25.846 109.745  19.696  1.00 14.89           N  
-ATOM  25328  CA  PHE G 183      25.066 108.703  20.356  1.00 16.30           C  
-ATOM  25329  C   PHE G 183      24.150 107.944  19.403  1.00 20.04           C  
-ATOM  25330  O   PHE G 183      23.678 108.491  18.405  1.00 24.30           O  
-ATOM  25331  CB  PHE G 183      24.224 109.307  21.483  1.00 15.81           C  
-ATOM  25332  CG  PHE G 183      25.034 109.985  22.549  1.00 16.29           C  
-ATOM  25333  CD1 PHE G 183      25.438 111.301  22.402  1.00 19.60           C  
-ATOM  25334  CD2 PHE G 183      25.382 109.309  23.704  1.00 18.48           C  
-ATOM  25335  CE1 PHE G 183      26.184 111.925  23.385  1.00 26.37           C  
-ATOM  25336  CE2 PHE G 183      26.127 109.926  24.690  1.00 23.09           C  
-ATOM  25337  CZ  PHE G 183      26.528 111.236  24.531  1.00 23.30           C  
-ATOM  25338  N   PHE G 184      23.904 106.677  19.722  1.00 17.69           N  
-ATOM  25339  CA  PHE G 184      22.895 105.895  19.022  1.00 20.69           C  
-ATOM  25340  C   PHE G 184      21.529 106.437  19.427  1.00 29.19           C  
-ATOM  25341  O   PHE G 184      21.309 106.744  20.600  1.00 29.46           O  
-ATOM  25342  CB  PHE G 184      23.025 104.406  19.359  1.00 22.57           C  
-ATOM  25343  CG  PHE G 184      22.216 103.503  18.469  1.00 25.17           C  
-ATOM  25344  CD1 PHE G 184      22.725 103.065  17.257  1.00 26.03           C  
-ATOM  25345  CD2 PHE G 184      20.950 103.086  18.847  1.00 25.60           C  
-ATOM  25346  CE1 PHE G 184      21.985 102.234  16.435  1.00 21.56           C  
-ATOM  25347  CE2 PHE G 184      20.205 102.255  18.029  1.00 26.30           C  
-ATOM  25348  CZ  PHE G 184      20.724 101.829  16.822  1.00 21.95           C  
-ATOM  25349  N   PRO G 185      20.611 106.575  18.458  1.00 27.47           N  
-ATOM  25350  CA  PRO G 185      19.307 107.184  18.741  1.00 24.36           C  
-ATOM  25351  C   PRO G 185      18.472 106.384  19.738  1.00 32.31           C  
-ATOM  25352  O   PRO G 185      18.752 105.209  19.983  1.00 27.57           O  
-ATOM  25353  CB  PRO G 185      18.631 107.211  17.369  1.00 21.41           C  
-ATOM  25354  CG  PRO G 185      19.309 106.139  16.590  1.00 23.84           C  
-ATOM  25355  CD  PRO G 185      20.732 106.163  17.049  1.00 23.36           C  
-ATOM  25356  N   ALA G 186      17.461 107.029  20.313  1.00 31.56           N  
-ATOM  25357  CA  ALA G 186      16.549 106.355  21.224  1.00 23.95           C  
-ATOM  25358  C   ALA G 186      15.594 105.470  20.433  1.00 26.48           C  
-ATOM  25359  O   ALA G 186      15.029 105.899  19.427  1.00 32.06           O  
-ATOM  25360  CB  ALA G 186      15.779 107.365  22.060  1.00 22.90           C  
-ATOM  25361  N   PHE G 187      15.423 104.233  20.883  1.00 25.84           N  
-ATOM  25362  CA  PHE G 187      14.554 103.292  20.189  1.00 26.36           C  
-ATOM  25363  C   PHE G 187      13.731 102.480  21.180  1.00 27.47           C  
-ATOM  25364  O   PHE G 187      14.202 102.179  22.275  1.00 30.02           O  
-ATOM  25365  CB  PHE G 187      15.376 102.364  19.291  1.00 25.18           C  
-ATOM  25366  CG  PHE G 187      16.316 101.464  20.041  1.00 26.46           C  
-ATOM  25367  CD1 PHE G 187      17.587 101.895  20.377  1.00 27.67           C  
-ATOM  25368  CD2 PHE G 187      15.933 100.181  20.399  1.00 29.32           C  
-ATOM  25369  CE1 PHE G 187      18.455 101.068  21.063  1.00 25.68           C  
-ATOM  25370  CE2 PHE G 187      16.796  99.351  21.085  1.00 25.64           C  
-ATOM  25371  CZ  PHE G 187      18.059  99.795  21.417  1.00 22.31           C  
-ATOM  25372  N   PRO G 188      12.494 102.125  20.797  1.00 27.94           N  
-ATOM  25373  CA  PRO G 188      11.616 101.323  21.655  1.00 36.40           C  
-ATOM  25374  C   PRO G 188      12.249  99.991  22.041  1.00 34.85           C  
-ATOM  25375  O   PRO G 188      12.466  99.130  21.186  1.00 34.63           O  
-ATOM  25376  CB  PRO G 188      10.370 101.108  20.784  1.00 39.41           C  
-ATOM  25377  CG  PRO G 188      10.819 101.380  19.386  1.00 28.64           C  
-ATOM  25378  CD  PRO G 188      11.855 102.446  19.511  1.00 28.23           C  
-ATOM  25379  N   GLY G 189      12.553  99.836  23.324  1.00 34.11           N  
-ATOM  25380  CA  GLY G 189      13.165  98.618  23.814  1.00 36.01           C  
-ATOM  25381  C   GLY G 189      14.654  98.772  24.040  1.00 30.85           C  
-ATOM  25382  O   GLY G 189      15.402  97.803  23.939  1.00 34.44           O  
-ATOM  25383  N   ASP G 190      15.086  99.992  24.348  1.00 24.11           N  
-ATOM  25384  CA  ASP G 190      16.486 100.246  24.675  1.00 23.05           C  
-ATOM  25385  C   ASP G 190      16.761  99.962  26.152  1.00 24.56           C  
-ATOM  25386  O   ASP G 190      17.823 100.296  26.680  1.00 27.17           O  
-ATOM  25387  CB  ASP G 190      16.866 101.683  24.325  1.00 23.47           C  
-ATOM  25388  CG  ASP G 190      15.804 102.677  24.731  1.00 32.00           C  
-ATOM  25389  OD1 ASP G 190      14.926 102.311  25.540  1.00 42.87           O  
-ATOM  25390  OD2 ASP G 190      15.849 103.823  24.239  1.00 34.54           O  
-ATOM  25391  N   ASP G 191      15.796  99.324  26.807  1.00 25.51           N  
-ATOM  25392  CA  ASP G 191      15.934  98.915  28.199  1.00 22.65           C  
-ATOM  25393  C   ASP G 191      17.045  97.879  28.362  1.00 34.66           C  
-ATOM  25394  O   ASP G 191      17.488  97.603  29.476  1.00 42.34           O  
-ATOM  25395  CB  ASP G 191      14.609  98.357  28.725  1.00 18.19           C  
-ATOM  25396  N   ILE G 192      17.494  97.311  27.244  1.00 28.37           N  
-ATOM  25397  CA  ILE G 192      18.618  96.378  27.245  1.00 29.83           C  
-ATOM  25398  C   ILE G 192      19.954  97.102  27.374  1.00 28.48           C  
-ATOM  25399  O   ILE G 192      21.010  96.472  27.373  1.00 30.72           O  
-ATOM  25400  CB  ILE G 192      18.652  95.517  25.967  1.00 25.77           C  
-ATOM  25401  CG1 ILE G 192      17.963  96.242  24.813  1.00 24.93           C  
-ATOM  25402  CG2 ILE G 192      17.981  94.179  26.205  1.00 31.11           C  
-ATOM  25403  CD1 ILE G 192      18.785  97.340  24.188  1.00 26.01           C  
-ATOM  25404  N   LEU G 193      19.906  98.426  27.472  1.00 28.71           N  
-ATOM  25405  CA  LEU G 193      21.118  99.221  27.626  1.00 22.80           C  
-ATOM  25406  C   LEU G 193      21.255  99.755  29.046  1.00 22.86           C  
-ATOM  25407  O   LEU G 193      22.271  99.538  29.704  1.00 34.08           O  
-ATOM  25408  CB  LEU G 193      21.124 100.372  26.624  1.00 25.40           C  
-ATOM  25409  CG  LEU G 193      21.111  99.926  25.162  1.00 22.95           C  
-ATOM  25410  CD1 LEU G 193      20.728 101.076  24.256  1.00 23.71           C  
-ATOM  25411  CD2 LEU G 193      22.460  99.349  24.761  1.00 21.47           C  
-ATOM  25412  N   SER G 194      20.231 100.459  29.513  1.00 21.35           N  
-ATOM  25413  CA  SER G 194      20.225 100.981  30.872  1.00 21.62           C  
-ATOM  25414  C   SER G 194      18.796 101.108  31.379  1.00 27.95           C  
-ATOM  25415  O   SER G 194      17.847 100.731  30.689  1.00 27.57           O  
-ATOM  25416  CB  SER G 194      20.934 102.334  30.940  1.00 28.74           C  
-ATOM  25417  OG  SER G 194      20.212 103.330  30.233  1.00 29.71           O  
-ATOM  25418  N   ASN G 195      18.646 101.635  32.588  1.00 24.36           N  
-ATOM  25419  CA  ASN G 195      17.327 101.826  33.172  1.00 19.66           C  
-ATOM  25420  C   ASN G 195      16.712 103.142  32.711  1.00 25.90           C  
-ATOM  25421  O   ASN G 195      17.418 104.130  32.512  1.00 36.64           O  
-ATOM  25422  CB  ASN G 195      17.409 101.773  34.698  1.00 21.25           C  
-ATOM  25423  CG  ASN G 195      17.884 100.423  35.208  1.00 24.37           C  
-ATOM  25424  OD1 ASN G 195      18.191  99.524  34.426  1.00 24.66           O  
-ATOM  25425  ND2 ASN G 195      17.953 100.278  36.525  1.00 26.51           N  
-ATOM  25426  N   LYS G 196      15.396 103.150  32.532  1.00 26.52           N  
-ATOM  25427  CA  LYS G 196      14.696 104.350  32.088  1.00 32.47           C  
-ATOM  25428  C   LYS G 196      14.161 105.160  33.267  1.00 39.78           C  
-ATOM  25429  O   LYS G 196      14.169 106.393  33.243  1.00 43.68           O  
-ATOM  25430  CB  LYS G 196      13.551 103.980  31.144  1.00 39.90           C  
-ATOM  25431  CG  LYS G 196      13.996 103.600  29.740  1.00 29.96           C  
-ATOM  25432  CD  LYS G 196      14.740 104.748  29.077  1.00 29.56           C  
-ATOM  25433  CE  LYS G 196      14.529 104.741  27.573  1.00 35.58           C  
-ATOM  25434  NZ  LYS G 196      13.085 104.842  27.221  1.00 27.41           N  
-ATOM  25435  N   ALA G 225       5.948  99.482  17.052  1.00 49.45           N  
-ATOM  25436  CA  ALA G 225       6.768  98.275  16.999  1.00 66.43           C  
-ATOM  25437  C   ALA G 225       8.036  98.413  17.840  1.00 58.76           C  
-ATOM  25438  O   ALA G 225       8.795  99.371  17.684  1.00 42.40           O  
-ATOM  25439  CB  ALA G 225       7.127  97.946  15.558  1.00 66.18           C  
-ATOM  25440  N   THR G 226       8.263  97.447  18.726  1.00 57.40           N  
-ATOM  25441  CA  THR G 226       9.438  97.458  19.591  1.00 44.35           C  
-ATOM  25442  C   THR G 226      10.505  96.487  19.088  1.00 38.58           C  
-ATOM  25443  O   THR G 226      10.207  95.555  18.338  1.00 38.47           O  
-ATOM  25444  CB  THR G 226       9.069  97.100  21.049  1.00 41.78           C  
-ATOM  25445  OG1 THR G 226      10.208  97.287  21.898  1.00 46.67           O  
-ATOM  25446  CG2 THR G 226       8.599  95.657  21.148  1.00 41.21           C  
-ATOM  25447  N   TYR G 227      11.749  96.718  19.498  1.00 35.70           N  
-ATOM  25448  CA  TYR G 227      12.866  95.855  19.121  1.00 33.90           C  
-ATOM  25449  C   TYR G 227      13.253  94.938  20.278  1.00 39.30           C  
-ATOM  25450  O   TYR G 227      14.003  95.339  21.167  1.00 41.50           O  
-ATOM  25451  CB  TYR G 227      14.074  96.692  18.688  1.00 31.42           C  
-ATOM  25452  CG  TYR G 227      13.913  97.387  17.352  1.00 31.66           C  
-ATOM  25453  CD1 TYR G 227      14.312  96.769  16.174  1.00 30.72           C  
-ATOM  25454  CD2 TYR G 227      13.372  98.665  17.269  1.00 31.79           C  
-ATOM  25455  CE1 TYR G 227      14.171  97.398  14.951  1.00 32.53           C  
-ATOM  25456  CE2 TYR G 227      13.227  99.302  16.049  1.00 31.45           C  
-ATOM  25457  CZ  TYR G 227      13.629  98.663  14.893  1.00 36.10           C  
-ATOM  25458  OH  TYR G 227      13.490  99.287  13.671  1.00 34.36           O  
-ATOM  25459  N   ARG G 228      12.751  93.705  20.262  1.00 41.67           N  
-ATOM  25460  CA  ARG G 228      12.973  92.786  21.378  1.00 37.48           C  
-ATOM  25461  C   ARG G 228      14.176  91.872  21.164  1.00 34.01           C  
-ATOM  25462  O   ARG G 228      14.405  91.393  20.058  1.00 39.35           O  
-ATOM  25463  CB  ARG G 228      11.725  91.936  21.629  1.00 35.21           C  
-ATOM  25464  CG  ARG G 228      10.594  92.679  22.314  1.00 52.97           C  
-ATOM  25465  CD  ARG G 228       9.665  91.711  23.028  1.00 58.65           C  
-ATOM  25466  NE  ARG G 228       9.289  90.588  22.174  1.00 76.53           N  
-ATOM  25467  CZ  ARG G 228       8.317  90.631  21.268  1.00 80.38           C  
-ATOM  25468  NH1 ARG G 228       7.621  91.748  21.093  1.00 70.19           N  
-ATOM  25469  NH2 ARG G 228       8.042  89.559  20.536  1.00 53.27           N  
-ATOM  25470  N   PRO G 229      14.944  91.618  22.236  1.00 29.14           N  
-ATOM  25471  CA  PRO G 229      16.122  90.750  22.155  1.00 25.26           C  
-ATOM  25472  C   PRO G 229      15.758  89.292  21.912  1.00 33.43           C  
-ATOM  25473  O   PRO G 229      14.763  88.801  22.446  1.00 34.66           O  
-ATOM  25474  CB  PRO G 229      16.779  90.925  23.525  1.00 25.37           C  
-ATOM  25475  CG  PRO G 229      15.657  91.269  24.426  1.00 36.72           C  
-ATOM  25476  CD  PRO G 229      14.722  92.111  23.606  1.00 36.66           C  
-ATOM  25477  N   ILE G 230      16.568  88.614  21.108  1.00 32.32           N  
-ATOM  25478  CA  ILE G 230      16.340  87.212  20.791  1.00 31.77           C  
-ATOM  25479  C   ILE G 230      17.640  86.437  21.009  1.00 33.74           C  
-ATOM  25480  O   ILE G 230      17.701  85.219  20.836  1.00 36.31           O  
-ATOM  25481  CB  ILE G 230      15.837  87.040  19.337  1.00 30.59           C  
-ATOM  25482  CG1 ILE G 230      15.059  85.733  19.185  1.00 60.87           C  
-ATOM  25483  CG2 ILE G 230      16.993  87.134  18.344  1.00 20.37           C  
-ATOM  25484  CD1 ILE G 230      13.705  85.889  18.513  1.00 67.16           C  
-ATOM  25485  N   PHE G 231      18.671  87.168  21.423  1.00 29.12           N  
-ATOM  25486  CA  PHE G 231      20.024  86.644  21.558  1.00 25.07           C  
-ATOM  25487  C   PHE G 231      20.761  87.466  22.609  1.00 25.26           C  
-ATOM  25488  O   PHE G 231      20.820  88.687  22.505  1.00 31.23           O  
-ATOM  25489  CB  PHE G 231      20.746  86.699  20.204  1.00 28.54           C  
-ATOM  25490  CG  PHE G 231      22.177  86.209  20.229  1.00 30.53           C  
-ATOM  25491  CD1 PHE G 231      23.194  86.987  20.764  1.00 27.07           C  
-ATOM  25492  CD2 PHE G 231      22.510  84.991  19.663  1.00 33.03           C  
-ATOM  25493  CE1 PHE G 231      24.501  86.540  20.769  1.00 28.07           C  
-ATOM  25494  CE2 PHE G 231      23.818  84.543  19.658  1.00 25.99           C  
-ATOM  25495  CZ  PHE G 231      24.813  85.317  20.215  1.00 23.36           C  
-ATOM  25496  N   ILE G 232      21.306  86.803  23.625  1.00 27.20           N  
-ATOM  25497  CA  ILE G 232      22.161  87.462  24.611  1.00 20.37           C  
-ATOM  25498  C   ILE G 232      23.328  86.546  24.973  1.00 20.74           C  
-ATOM  25499  O   ILE G 232      23.121  85.470  25.534  1.00 28.29           O  
-ATOM  25500  CB  ILE G 232      21.396  87.836  25.901  1.00 18.26           C  
-ATOM  25501  CG1 ILE G 232      20.230  88.784  25.602  1.00 16.30           C  
-ATOM  25502  CG2 ILE G 232      22.343  88.472  26.907  1.00 20.20           C  
-ATOM  25503  CD1 ILE G 232      19.420  89.162  26.825  1.00 20.64           C  
-ATOM  25504  N   SER G 233      24.548  86.972  24.655  1.00 20.21           N  
-ATOM  25505  CA  SER G 233      25.739  86.142  24.852  1.00 24.25           C  
-ATOM  25506  C   SER G 233      26.340  86.284  26.248  1.00 18.82           C  
-ATOM  25507  O   SER G 233      25.879  87.094  27.052  1.00 19.64           O  
-ATOM  25508  CB  SER G 233      26.804  86.487  23.809  1.00 25.76           C  
-ATOM  25509  OG  SER G 233      27.368  87.766  24.052  1.00 13.05           O  
-ATOM  25510  N   LYS G 234      27.375  85.494  26.528  1.00 18.69           N  
-ATOM  25511  CA  LYS G 234      28.118  85.628  27.777  1.00 17.80           C  
-ATOM  25512  C   LYS G 234      28.977  86.886  27.716  1.00 20.06           C  
-ATOM  25513  O   LYS G 234      29.161  87.462  26.647  1.00 19.34           O  
-ATOM  25514  CB  LYS G 234      28.989  84.395  28.042  1.00 15.08           C  
-ATOM  25515  CG  LYS G 234      30.404  84.508  27.504  1.00 24.56           C  
-ATOM  25516  CD  LYS G 234      30.591  83.683  26.245  1.00 38.04           C  
-ATOM  25517  CE  LYS G 234      31.187  82.324  26.564  1.00 27.75           C  
-ATOM  25518  NZ  LYS G 234      32.554  82.466  27.133  1.00 26.86           N  
-ATOM  25519  N   THR G 235      29.503  87.316  28.856  1.00 21.87           N  
-ATOM  25520  CA  THR G 235      30.287  88.542  28.889  1.00 16.85           C  
-ATOM  25521  C   THR G 235      31.741  88.321  28.472  1.00 23.09           C  
-ATOM  25522  O   THR G 235      32.454  87.502  29.055  1.00 24.40           O  
-ATOM  25523  CB  THR G 235      30.263  89.183  30.282  1.00 14.38           C  
-ATOM  25524  OG1 THR G 235      28.904  89.408  30.679  1.00 18.83           O  
-ATOM  25525  CG2 THR G 235      31.007  90.504  30.261  1.00 11.72           C  
-ATOM  25526  N   PHE G 236      32.161  89.060  27.450  1.00 23.26           N  
-ATOM  25527  CA  PHE G 236      33.552  89.103  27.018  1.00 21.67           C  
-ATOM  25528  C   PHE G 236      34.214  90.352  27.581  1.00 23.39           C  
-ATOM  25529  O   PHE G 236      33.536  91.238  28.102  1.00 25.28           O  
-ATOM  25530  CB  PHE G 236      33.652  89.110  25.493  1.00 20.18           C  
-ATOM  25531  CG  PHE G 236      33.064  87.897  24.835  1.00 20.26           C  
-ATOM  25532  CD1 PHE G 236      31.693  87.744  24.725  1.00 21.56           C  
-ATOM  25533  CD2 PHE G 236      33.886  86.920  24.305  1.00 24.77           C  
-ATOM  25534  CE1 PHE G 236      31.155  86.632  24.116  1.00 24.86           C  
-ATOM  25535  CE2 PHE G 236      33.354  85.807  23.692  1.00 21.93           C  
-ATOM  25536  CZ  PHE G 236      31.987  85.662  23.597  1.00 26.89           C  
-ATOM  25537  N   SER G 237      35.534  90.434  27.467  1.00 23.25           N  
-ATOM  25538  CA  SER G 237      36.247  91.617  27.934  1.00 21.20           C  
-ATOM  25539  C   SER G 237      37.561  91.812  27.195  1.00 22.69           C  
-ATOM  25540  O   SER G 237      38.263  90.843  26.904  1.00 24.89           O  
-ATOM  25541  CB  SER G 237      36.519  91.527  29.433  1.00 18.84           C  
-ATOM  25542  OG  SER G 237      37.659  90.724  29.681  1.00 32.25           O  
-ATOM  25543  N   ASP G 238      37.884  93.070  26.898  1.00 20.90           N  
-ATOM  25544  CA  ASP G 238      39.186  93.434  26.341  1.00 21.12           C  
-ATOM  25545  C   ASP G 238      39.658  94.770  26.899  1.00 22.30           C  
-ATOM  25546  O   ASP G 238      38.880  95.722  26.985  1.00 32.12           O  
-ATOM  25547  CB  ASP G 238      39.135  93.497  24.817  1.00 19.24           C  
-ATOM  25548  CG  ASP G 238      39.078  92.131  24.187  1.00 25.27           C  
-ATOM  25549  OD1 ASP G 238      40.075  91.386  24.298  1.00 31.34           O  
-ATOM  25550  OD2 ASP G 238      38.038  91.802  23.579  1.00 26.01           O  
-ATOM  25551  N   ASN G 239      40.932  94.831  27.276  1.00 18.13           N  
-ATOM  25552  CA  ASN G 239      41.534  96.047  27.818  1.00 22.32           C  
-ATOM  25553  C   ASN G 239      40.733  96.675  28.957  1.00 20.96           C  
-ATOM  25554  O   ASN G 239      40.483  97.882  28.961  1.00 16.52           O  
-ATOM  25555  CB  ASN G 239      41.731  97.072  26.703  1.00 14.44           C  
-ATOM  25556  CG  ASN G 239      42.905  96.734  25.808  1.00 20.18           C  
-ATOM  25557  OD1 ASN G 239      42.738  96.474  24.618  1.00 32.14           O  
-ATOM  25558  ND2 ASN G 239      44.102  96.733  26.379  1.00 17.93           N  
-ATOM  25559  N   GLY G 240      40.331  95.850  29.920  1.00 14.26           N  
-ATOM  25560  CA  GLY G 240      39.616  96.337  31.086  1.00 17.75           C  
-ATOM  25561  C   GLY G 240      38.206  96.788  30.768  1.00 14.98           C  
-ATOM  25562  O   GLY G 240      37.554  97.440  31.585  1.00  9.84           O  
-ATOM  25563  N   VAL G 241      37.741  96.441  29.571  1.00 20.45           N  
-ATOM  25564  CA  VAL G 241      36.397  96.789  29.128  1.00 19.41           C  
-ATOM  25565  C   VAL G 241      35.549  95.539  28.970  1.00 24.52           C  
-ATOM  25566  O   VAL G 241      35.811  94.716  28.093  1.00 21.73           O  
-ATOM  25567  CB  VAL G 241      36.401  97.548  27.782  1.00 17.62           C  
-ATOM  25568  CG1 VAL G 241      34.986  97.966  27.407  1.00 22.09           C  
-ATOM  25569  CG2 VAL G 241      37.326  98.751  27.844  1.00 16.78           C  
-ATOM  25570  N   PRO G 242      34.534  95.393  29.832  1.00 22.63           N  
-ATOM  25571  CA  PRO G 242      33.546  94.316  29.760  1.00 18.60           C  
-ATOM  25572  C   PRO G 242      32.425  94.663  28.793  1.00 16.37           C  
-ATOM  25573  O   PRO G 242      31.965  95.804  28.775  1.00 16.49           O  
-ATOM  25574  CB  PRO G 242      33.020  94.231  31.192  1.00 16.70           C  
-ATOM  25575  CG  PRO G 242      33.116  95.633  31.683  1.00 15.81           C  
-ATOM  25576  CD  PRO G 242      34.340  96.233  31.027  1.00 16.92           C  
-ATOM  25577  N   TYR G 243      31.993  93.691  27.999  1.00 16.58           N  
-ATOM  25578  CA  TYR G 243      30.921  93.918  27.040  1.00 17.56           C  
-ATOM  25579  C   TYR G 243      30.284  92.602  26.620  1.00 13.79           C  
-ATOM  25580  O   TYR G 243      30.839  91.542  26.876  1.00 14.28           O  
-ATOM  25581  CB  TYR G 243      31.448  94.680  25.815  1.00 16.93           C  
-ATOM  25582  CG  TYR G 243      32.591  94.015  25.080  1.00 17.20           C  
-ATOM  25583  CD1 TYR G 243      33.902  94.196  25.492  1.00 20.92           C  
-ATOM  25584  CD2 TYR G 243      32.359  93.228  23.959  1.00 17.23           C  
-ATOM  25585  CE1 TYR G 243      34.952  93.599  24.818  1.00 24.23           C  
-ATOM  25586  CE2 TYR G 243      33.403  92.627  23.279  1.00 18.61           C  
-ATOM  25587  CZ  TYR G 243      34.696  92.817  23.714  1.00 18.24           C  
-ATOM  25588  OH  TYR G 243      35.739  92.225  23.044  1.00 20.27           O  
-ATOM  25589  N   ASP G 244      29.114  92.661  25.992  1.00 16.21           N  
-ATOM  25590  CA  ASP G 244      28.531  91.444  25.420  1.00 20.66           C  
-ATOM  25591  C   ASP G 244      27.776  91.744  24.130  1.00 21.54           C  
-ATOM  25592  O   ASP G 244      27.595  92.902  23.767  1.00 19.38           O  
-ATOM  25593  CB  ASP G 244      27.610  90.733  26.426  1.00 17.97           C  
-ATOM  25594  CG  ASP G 244      26.434  91.592  26.877  1.00 15.74           C  
-ATOM  25595  OD1 ASP G 244      26.245  92.705  26.348  1.00 17.22           O  
-ATOM  25596  OD2 ASP G 244      25.682  91.139  27.767  1.00 16.40           O  
-ATOM  25597  N   PHE G 245      27.340  90.695  23.441  1.00 19.07           N  
-ATOM  25598  CA  PHE G 245      26.647  90.859  22.168  1.00 16.22           C  
-ATOM  25599  C   PHE G 245      25.188  90.433  22.265  1.00 19.03           C  
-ATOM  25600  O   PHE G 245      24.880  89.354  22.770  1.00 18.25           O  
-ATOM  25601  CB  PHE G 245      27.336  90.051  21.069  1.00 15.70           C  
-ATOM  25602  CG  PHE G 245      28.825  90.224  21.025  1.00 18.03           C  
-ATOM  25603  CD1 PHE G 245      29.657  89.375  21.740  1.00 21.95           C  
-ATOM  25604  CD2 PHE G 245      29.395  91.222  20.256  1.00 19.44           C  
-ATOM  25605  CE1 PHE G 245      31.029  89.526  21.695  1.00 18.24           C  
-ATOM  25606  CE2 PHE G 245      30.765  91.378  20.207  1.00 25.36           C  
-ATOM  25607  CZ  PHE G 245      31.583  90.529  20.928  1.00 24.59           C  
-ATOM  25608  N   VAL G 246      24.292  91.286  21.780  1.00 18.68           N  
-ATOM  25609  CA  VAL G 246      22.884  90.931  21.683  1.00 21.61           C  
-ATOM  25610  C   VAL G 246      22.342  91.192  20.286  1.00 21.99           C  
-ATOM  25611  O   VAL G 246      22.846  92.050  19.554  1.00 29.13           O  
-ATOM  25612  CB  VAL G 246      22.014  91.700  22.697  1.00 16.90           C  
-ATOM  25613  CG1 VAL G 246      22.387  91.318  24.119  1.00 16.94           C  
-ATOM  25614  CG2 VAL G 246      22.126  93.198  22.474  1.00 18.40           C  
-ATOM  25615  N   VAL G 247      21.314  90.435  19.922  1.00 18.08           N  
-ATOM  25616  CA  VAL G 247      20.625  90.633  18.659  1.00 20.18           C  
-ATOM  25617  C   VAL G 247      19.167  90.979  18.923  1.00 22.30           C  
-ATOM  25618  O   VAL G 247      18.439  90.214  19.558  1.00 20.87           O  
-ATOM  25619  CB  VAL G 247      20.704  89.386  17.757  1.00 20.52           C  
-ATOM  25620  CG1 VAL G 247      20.018  89.656  16.428  1.00 27.46           C  
-ATOM  25621  CG2 VAL G 247      22.151  88.973  17.544  1.00 20.20           C  
-ATOM  25622  N   LEU G 248      18.751  92.144  18.443  1.00 21.77           N  
-ATOM  25623  CA  LEU G 248      17.369  92.572  18.574  1.00 23.02           C  
-ATOM  25624  C   LEU G 248      16.611  92.290  17.287  1.00 31.29           C  
-ATOM  25625  O   LEU G 248      17.198  92.241  16.205  1.00 26.57           O  
-ATOM  25626  CB  LEU G 248      17.286  94.059  18.916  1.00 23.75           C  
-ATOM  25627  CG  LEU G 248      18.155  94.565  20.066  1.00 20.28           C  
-ATOM  25628  CD1 LEU G 248      17.830  96.016  20.364  1.00 25.15           C  
-ATOM  25629  CD2 LEU G 248      17.971  93.713  21.304  1.00 25.08           C  
-ATOM  25630  N   GLU G 249      15.302  92.112  17.419  1.00 38.02           N  
-ATOM  25631  CA  GLU G 249      14.434  91.793  16.298  1.00 32.51           C  
-ATOM  25632  C   GLU G 249      13.195  92.680  16.343  1.00 34.58           C  
-ATOM  25633  O   GLU G 249      12.681  92.984  17.423  1.00 37.75           O  
-ATOM  25634  CB  GLU G 249      14.045  90.312  16.333  1.00 33.80           C  
-ATOM  25635  CG  GLU G 249      13.068  89.870  15.254  1.00 44.50           C  
-ATOM  25636  CD  GLU G 249      12.716  88.397  15.365  1.00 54.10           C  
-ATOM  25637  OE1 GLU G 249      13.175  87.609  14.510  1.00 50.32           O  
-ATOM  25638  OE2 GLU G 249      11.986  88.027  16.310  1.00 44.69           O  
-ATOM  25639  N   LYS G 250      12.734  93.111  15.174  1.00 29.43           N  
-ATOM  25640  CA  LYS G 250      11.505  93.890  15.081  1.00 32.05           C  
-ATOM  25641  C   LYS G 250      10.304  92.964  15.253  1.00 41.67           C  
-ATOM  25642  O   LYS G 250      10.226  91.917  14.607  1.00 47.15           O  
-ATOM  25643  CB  LYS G 250      11.437  94.630  13.745  1.00 34.69           C  
-ATOM  25644  CG  LYS G 250      10.467  95.798  13.729  1.00 41.76           C  
-ATOM  25645  CD  LYS G 250      10.689  96.675  12.509  1.00 34.08           C  
-ATOM  25646  CE  LYS G 250       9.871  97.953  12.590  1.00 41.01           C  
-ATOM  25647  NZ  LYS G 250      10.178  98.877  11.466  1.00 34.90           N  
-ATOM  25648  N   ARG G 251       9.370  93.337  16.123  1.00 40.73           N  
-ATOM  25649  CA  ARG G 251       8.301  92.413  16.493  1.00 60.23           C  
-ATOM  25650  C   ARG G 251       6.883  92.980  16.426  1.00 79.36           C  
-ATOM  25651  O   ARG G 251       5.936  92.235  16.159  1.00 79.17           O  
-ATOM  25652  CB  ARG G 251       8.555  91.869  17.902  1.00 63.12           C  
-ATOM  25653  CG  ARG G 251       9.605  90.772  17.960  1.00 61.59           C  
-ATOM  25654  CD  ARG G 251       9.336  89.709  16.904  1.00 69.75           C  
-ATOM  25655  NE  ARG G 251       7.961  89.218  16.950  1.00 86.65           N  
-ATOM  25656  CZ  ARG G 251       7.395  88.492  15.990  1.00 80.80           C  
-ATOM  25657  NH1 ARG G 251       6.137  88.088  16.114  1.00 63.34           N  
-ATOM  25658  NH2 ARG G 251       8.086  88.172  14.905  1.00 76.17           N  
-ATOM  25659  N   ARG G 252       6.740  94.279  16.676  1.00 71.99           N  
-ATOM  25660  CA  ARG G 252       5.424  94.918  16.730  1.00 70.91           C  
-ATOM  25661  C   ARG G 252       4.505  94.233  17.739  1.00 73.26           C  
-ATOM  25662  O   ARG G 252       4.335  94.706  18.864  1.00 67.71           O  
-ATOM  25663  CB  ARG G 252       4.763  94.927  15.346  1.00 67.37           C  
-ATOM  25664  CG  ARG G 252       3.242  94.907  15.393  1.00 69.41           C  
-ATOM  25665  CD  ARG G 252       2.637  94.574  14.037  1.00 75.39           C  
-ATOM  25666  NE  ARG G 252       1.346  93.903  14.174  1.00 86.67           N  
-ATOM  25667  CZ  ARG G 252       0.184  94.533  14.310  1.00 84.84           C  
-ATOM  25668  NH1 ARG G 252       0.142  95.858  14.324  1.00 80.67           N  
-ATOM  25669  NH2 ARG G 252      -0.939  93.837  14.433  1.00 69.05           N  
-ATOM  25670  N   SER G 285      12.545  53.831   8.105  1.00 86.97           N  
-ATOM  25671  CA  SER G 285      12.409  53.866   9.556  1.00 92.96           C  
-ATOM  25672  C   SER G 285      13.770  53.855  10.250  1.00 88.92           C  
-ATOM  25673  O   SER G 285      14.109  52.907  10.959  1.00 87.51           O  
-ATOM  25674  CB  SER G 285      11.558  52.688  10.036  1.00 84.54           C  
-ATOM  25675  OG  SER G 285      11.721  51.565   9.187  1.00 75.29           O  
-ATOM  25676  N   SER G 286      14.543  54.916  10.042  1.00 87.92           N  
-ATOM  25677  CA  SER G 286      15.859  55.037  10.661  1.00 95.38           C  
-ATOM  25678  C   SER G 286      15.730  55.193  12.174  1.00 95.93           C  
-ATOM  25679  O   SER G 286      15.845  54.222  12.925  1.00 83.52           O  
-ATOM  25680  CB  SER G 286      16.625  56.224  10.071  1.00 84.94           C  
-ATOM  25681  OG  SER G 286      16.759  56.105   8.665  1.00 71.19           O  
-ATOM  25682  N   ALA G 287      15.486  56.424  12.612  1.00 86.34           N  
-ATOM  25683  CA  ALA G 287      15.323  56.716  14.028  1.00 70.89           C  
-ATOM  25684  C   ALA G 287      13.876  57.082  14.334  1.00 74.99           C  
-ATOM  25685  O   ALA G 287      13.448  57.063  15.488  1.00 81.08           O  
-ATOM  25686  CB  ALA G 287      16.259  57.839  14.449  1.00 67.65           C  
-ATOM  25687  N   ALA G 288      13.127  57.400  13.284  1.00 73.89           N  
-ATOM  25688  CA  ALA G 288      11.764  57.899  13.419  1.00 81.18           C  
-ATOM  25689  C   ALA G 288      10.800  56.869  14.011  1.00 92.71           C  
-ATOM  25690  O   ALA G 288       9.817  57.234  14.656  1.00 84.04           O  
-ATOM  25691  CB  ALA G 288      11.253  58.373  12.067  1.00 66.58           C  
-ATOM  25692  N   ALA G 289      11.083  55.588  13.797  1.00 91.63           N  
-ATOM  25693  CA  ALA G 289      10.190  54.524  14.253  1.00 98.98           C  
-ATOM  25694  C   ALA G 289      10.367  54.222  15.739  1.00106.52           C  
-ATOM  25695  O   ALA G 289       9.751  53.298  16.273  1.00102.23           O  
-ATOM  25696  CB  ALA G 289      10.417  53.266  13.435  1.00 89.07           C  
-ATOM  25697  N   ILE G 290      11.209  55.004  16.404  1.00106.04           N  
-ATOM  25698  CA  ILE G 290      11.529  54.757  17.803  1.00 98.42           C  
-ATOM  25699  C   ILE G 290      10.992  55.889  18.682  1.00 97.74           C  
-ATOM  25700  O   ILE G 290      11.049  55.829  19.911  1.00 90.78           O  
-ATOM  25701  CB  ILE G 290      13.047  54.583  17.981  1.00 91.84           C  
-ATOM  25702  CG1 ILE G 290      13.589  53.715  16.842  1.00 99.01           C  
-ATOM  25703  CG2 ILE G 290      13.367  53.948  19.329  1.00 82.80           C  
-ATOM  25704  CD1 ILE G 290      14.971  54.083  16.377  1.00 98.57           C  
-ATOM  25705  N   ALA G 291      10.447  56.912  18.032  1.00102.67           N  
-ATOM  25706  CA  ALA G 291       9.726  57.982  18.716  1.00 96.72           C  
-ATOM  25707  C   ALA G 291       8.395  57.560  19.382  1.00 97.42           C  
-ATOM  25708  O   ALA G 291       7.924  58.263  20.274  1.00 93.01           O  
-ATOM  25709  CB  ALA G 291       9.471  59.128  17.742  1.00 90.54           C  
-ATOM  25710  N   PRO G 292       7.765  56.445  18.947  1.00 92.17           N  
-ATOM  25711  CA  PRO G 292       6.592  56.031  19.734  1.00 87.91           C  
-ATOM  25712  C   PRO G 292       6.907  55.551  21.155  1.00 90.18           C  
-ATOM  25713  O   PRO G 292       6.078  55.742  22.044  1.00 85.36           O  
-ATOM  25714  CB  PRO G 292       5.998  54.880  18.904  1.00 88.68           C  
-ATOM  25715  CG  PRO G 292       7.074  54.479  17.952  1.00 82.95           C  
-ATOM  25716  CD  PRO G 292       7.794  55.745  17.651  1.00 89.57           C  
-ATOM  25717  N   VAL G 293       8.062  54.928  21.370  1.00 98.64           N  
-ATOM  25718  CA  VAL G 293       8.456  54.545  22.724  1.00 93.55           C  
-ATOM  25719  C   VAL G 293       8.775  55.806  23.516  1.00 91.20           C  
-ATOM  25720  O   VAL G 293       8.556  55.871  24.727  1.00 81.97           O  
-ATOM  25721  CB  VAL G 293       9.674  53.603  22.737  1.00 83.39           C  
-ATOM  25722  CG1 VAL G 293       9.918  53.075  24.142  1.00 73.40           C  
-ATOM  25723  CG2 VAL G 293       9.457  52.455  21.781  1.00 71.46           C  
-ATOM  25724  N   LEU G 294       9.291  56.810  22.814  1.00106.40           N  
-ATOM  25725  CA  LEU G 294       9.516  58.121  23.405  1.00109.39           C  
-ATOM  25726  C   LEU G 294       8.191  58.780  23.767  1.00109.95           C  
-ATOM  25727  O   LEU G 294       8.130  59.588  24.687  1.00108.01           O  
-ATOM  25728  CB  LEU G 294      10.299  59.027  22.450  1.00113.61           C  
-ATOM  25729  CG  LEU G 294      11.802  58.792  22.291  1.00100.32           C  
-ATOM  25730  CD1 LEU G 294      12.377  59.731  21.242  1.00 96.66           C  
-ATOM  25731  CD2 LEU G 294      12.516  58.972  23.621  1.00 90.10           C  
-ATOM  25732  N   ALA G 295       7.133  58.415  23.046  1.00103.81           N  
-ATOM  25733  CA  ALA G 295       5.847  59.101  23.142  1.00100.85           C  
-ATOM  25734  C   ALA G 295       5.157  58.905  24.491  1.00106.06           C  
-ATOM  25735  O   ALA G 295       4.459  59.800  24.970  1.00106.61           O  
-ATOM  25736  CB  ALA G 295       4.928  58.646  22.016  1.00 85.58           C  
-ATOM  25737  N   TRP G 296       5.348  57.741  25.105  1.00 99.51           N  
-ATOM  25738  CA  TRP G 296       4.701  57.465  26.382  1.00102.46           C  
-ATOM  25739  C   TRP G 296       5.624  57.743  27.565  1.00105.28           C  
-ATOM  25740  O   TRP G 296       5.181  57.769  28.714  1.00104.71           O  
-ATOM  25741  CB  TRP G 296       4.197  56.022  26.433  1.00 95.43           C  
-ATOM  25742  CG  TRP G 296       5.263  54.967  26.452  1.00104.37           C  
-ATOM  25743  CD1 TRP G 296       5.820  54.341  25.373  1.00105.55           C  
-ATOM  25744  CD2 TRP G 296       5.877  54.391  27.611  1.00101.67           C  
-ATOM  25745  NE1 TRP G 296       6.752  53.419  25.790  1.00 95.78           N  
-ATOM  25746  CE2 TRP G 296       6.805  53.431  27.159  1.00 99.48           C  
-ATOM  25747  CE3 TRP G 296       5.737  54.599  28.988  1.00 86.88           C  
-ATOM  25748  CZ2 TRP G 296       7.586  52.680  28.034  1.00 86.17           C  
-ATOM  25749  CZ3 TRP G 296       6.515  53.854  29.853  1.00 86.57           C  
-ATOM  25750  CH2 TRP G 296       7.429  52.907  29.373  1.00 86.06           C  
-ATOM  25751  N   MET G 297       6.905  57.950  27.283  1.00102.86           N  
-ATOM  25752  CA  MET G 297       7.847  58.369  28.312  1.00 89.60           C  
-ATOM  25753  C   MET G 297       7.917  59.892  28.354  1.00 87.71           C  
-ATOM  25754  O   MET G 297       8.452  60.478  29.297  1.00 89.96           O  
-ATOM  25755  CB  MET G 297       9.234  57.778  28.055  1.00 81.04           C  
-ATOM  25756  CG  MET G 297       9.312  56.264  28.181  1.00 81.43           C  
-ATOM  25757  SD  MET G 297      11.011  55.675  28.024  1.00 75.98           S  
-ATOM  25758  CE  MET G 297      10.786  53.902  28.139  1.00 55.16           C  
-ATOM  25759  N   ASP G 298       7.362  60.520  27.321  1.00 94.31           N  
-ATOM  25760  CA  ASP G 298       7.401  61.970  27.165  1.00100.90           C  
-ATOM  25761  C   ASP G 298       6.260  62.636  27.925  1.00 95.65           C  
-ATOM  25762  O   ASP G 298       5.230  62.012  28.186  1.00 77.84           O  
-ATOM  25763  CB  ASP G 298       7.338  62.345  25.678  1.00100.42           C  
-ATOM  25764  CG  ASP G 298       7.537  63.828  25.432  1.00 88.27           C  
-ATOM  25765  OD1 ASP G 298       8.157  64.499  26.285  1.00 87.40           O  
-ATOM  25766  OD2 ASP G 298       7.075  64.322  24.381  1.00 69.16           O  
-ATOM  25767  N   GLU G 299       6.454  63.904  28.276  1.00103.27           N  
-ATOM  25768  CA  GLU G 299       5.438  64.686  28.973  1.00106.50           C  
-ATOM  25769  C   GLU G 299       5.045  65.922  28.166  1.00 93.56           C  
-ATOM  25770  O   GLU G 299       5.166  67.055  28.637  1.00 72.82           O  
-ATOM  25771  CB  GLU G 299       5.938  65.094  30.361  1.00 86.12           C  
-ATOM  25772  CG  GLU G 299       6.320  63.915  31.241  1.00 72.88           C  
-ATOM  25773  CD  GLU G 299       5.163  62.963  31.468  1.00 84.64           C  
-ATOM  25774  OE1 GLU G 299       4.070  63.435  31.844  1.00 80.53           O  
-ATOM  25775  OE2 GLU G 299       5.344  61.744  31.261  1.00 87.79           O  
-ATOM  25776  N   LEU G 310       5.862  76.160  32.732  1.00 22.87           N  
-ATOM  25777  CA  LEU G 310       4.833  77.195  32.708  1.00 50.15           C  
-ATOM  25778  C   LEU G 310       5.444  78.586  32.878  1.00 45.40           C  
-ATOM  25779  O   LEU G 310       5.262  79.461  32.031  1.00 48.65           O  
-ATOM  25780  CB  LEU G 310       3.788  76.938  33.799  1.00 57.81           C  
-ATOM  25781  CG  LEU G 310       2.312  77.195  33.468  1.00 59.29           C  
-ATOM  25782  CD1 LEU G 310       2.054  78.659  33.123  1.00 43.60           C  
-ATOM  25783  CD2 LEU G 310       1.826  76.277  32.347  1.00 39.16           C  
-ATOM  25784  N   ILE G 311       6.160  78.787  33.981  1.00 45.47           N  
-ATOM  25785  CA  ILE G 311       6.847  80.050  34.220  1.00 46.68           C  
-ATOM  25786  C   ILE G 311       8.263  80.003  33.656  1.00 47.14           C  
-ATOM  25787  O   ILE G 311       9.026  79.081  33.949  1.00 44.35           O  
-ATOM  25788  CB  ILE G 311       6.908  80.398  35.729  1.00 42.03           C  
-ATOM  25789  CG1 ILE G 311       5.582  80.998  36.203  1.00 52.36           C  
-ATOM  25790  CG2 ILE G 311       8.039  81.373  36.011  1.00 32.16           C  
-ATOM  25791  CD1 ILE G 311       4.581  79.978  36.715  1.00 56.16           C  
-ATOM  25792  N   ARG G 312       8.605  80.992  32.836  1.00 45.68           N  
-ATOM  25793  CA  ARG G 312       9.951  81.085  32.287  1.00 40.98           C  
-ATOM  25794  C   ARG G 312      10.433  82.531  32.224  1.00 49.20           C  
-ATOM  25795  O   ARG G 312       9.647  83.451  31.996  1.00 55.01           O  
-ATOM  25796  CB  ARG G 312      10.014  80.455  30.895  1.00 40.37           C  
-ATOM  25797  CG  ARG G 312      11.435  80.172  30.431  1.00 50.85           C  
-ATOM  25798  CD  ARG G 312      11.486  79.691  28.994  1.00 44.70           C  
-ATOM  25799  NE  ARG G 312      12.833  79.259  28.634  1.00 40.52           N  
-ATOM  25800  CZ  ARG G 312      13.237  79.021  27.392  1.00 48.82           C  
-ATOM  25801  NH1 ARG G 312      12.395  79.178  26.378  1.00 56.48           N  
-ATOM  25802  NH2 ARG G 312      14.485  78.632  27.162  1.00 28.03           N  
-ATOM  25803  N   ALA G 313      11.732  82.722  32.431  1.00 47.22           N  
-ATOM  25804  CA  ALA G 313      12.336  84.045  32.360  1.00 35.59           C  
-ATOM  25805  C   ALA G 313      12.607  84.435  30.912  1.00 40.14           C  
-ATOM  25806  O   ALA G 313      13.208  83.660  30.171  1.00 40.95           O  
-ATOM  25807  CB  ALA G 313      13.620  84.083  33.167  1.00 29.90           C  
-ATOM  25808  N   VAL G 314      12.179  85.646  30.542  1.00 38.49           N  
-ATOM  25809  CA  VAL G 314      12.296  86.213  29.185  1.00 36.10           C  
-ATOM  25810  C   VAL G 314      12.373  85.182  28.050  1.00 41.34           C  
-ATOM  25811  O   VAL G 314      13.434  84.966  27.461  1.00 37.17           O  
-ATOM  25812  CB  VAL G 314      13.523  87.165  29.078  1.00 24.94           C  
-ATOM  25813  CG1 VAL G 314      13.193  88.519  29.681  1.00 31.33           C  
-ATOM  25814  CG2 VAL G 314      14.761  86.576  29.744  1.00 30.85           C  
-ATOM  25815  N   PRO G 315      11.228  84.558  27.727  1.00 41.24           N  
-ATOM  25816  CA  PRO G 315      11.137  83.431  26.791  1.00 36.06           C  
-ATOM  25817  C   PRO G 315      11.477  83.788  25.345  1.00 35.28           C  
-ATOM  25818  O   PRO G 315      11.868  82.902  24.585  1.00 30.46           O  
-ATOM  25819  CB  PRO G 315       9.670  83.008  26.904  1.00 40.66           C  
-ATOM  25820  CG  PRO G 315       8.962  84.253  27.295  1.00 42.60           C  
-ATOM  25821  CD  PRO G 315       9.901  84.971  28.217  1.00 40.22           C  
-ATOM  25822  N   HIS G 316      11.327  85.056  24.974  1.00 33.50           N  
-ATOM  25823  CA  HIS G 316      11.600  85.486  23.605  1.00 35.75           C  
-ATOM  25824  C   HIS G 316      13.088  85.418  23.290  1.00 36.84           C  
-ATOM  25825  O   HIS G 316      13.482  85.358  22.126  1.00 37.91           O  
-ATOM  25826  CB  HIS G 316      11.074  86.903  23.370  1.00 38.55           C  
-ATOM  25827  CG  HIS G 316      11.375  87.852  24.486  1.00 36.64           C  
-ATOM  25828  ND1 HIS G 316      10.555  87.990  25.585  1.00 34.32           N  
-ATOM  25829  CD2 HIS G 316      12.406  88.711  24.675  1.00 36.15           C  
-ATOM  25830  CE1 HIS G 316      11.066  88.893  26.402  1.00 36.30           C  
-ATOM  25831  NE2 HIS G 316      12.189  89.345  25.873  1.00 37.70           N  
-ATOM  25832  N   VAL G 317      13.909  85.428  24.335  1.00 37.93           N  
-ATOM  25833  CA  VAL G 317      15.351  85.273  24.184  1.00 41.36           C  
-ATOM  25834  C   VAL G 317      15.700  83.805  23.936  1.00 41.03           C  
-ATOM  25835  O   VAL G 317      15.688  82.989  24.859  1.00 35.66           O  
-ATOM  25836  CB  VAL G 317      16.107  85.781  25.426  1.00 30.01           C  
-ATOM  25837  CG1 VAL G 317      17.608  85.681  25.212  1.00 30.89           C  
-ATOM  25838  CG2 VAL G 317      15.709  87.214  25.739  1.00 29.80           C  
-ATOM  25839  N   HIS G 318      16.015  83.474  22.688  1.00 36.31           N  
-ATOM  25840  CA  HIS G 318      16.221  82.080  22.308  1.00 39.28           C  
-ATOM  25841  C   HIS G 318      17.622  81.591  22.647  1.00 42.05           C  
-ATOM  25842  O   HIS G 318      17.775  80.568  23.316  1.00 44.51           O  
-ATOM  25843  CB  HIS G 318      15.920  81.889  20.822  1.00 43.61           C  
-ATOM  25844  CG  HIS G 318      14.457  81.919  20.506  1.00 61.31           C  
-ATOM  25845  ND1 HIS G 318      13.931  82.659  19.469  1.00 75.36           N  
-ATOM  25846  CD2 HIS G 318      13.406  81.300  21.096  1.00 57.21           C  
-ATOM  25847  CE1 HIS G 318      12.621  82.495  19.434  1.00 79.20           C  
-ATOM  25848  NE2 HIS G 318      12.277  81.675  20.410  1.00 78.02           N  
-ATOM  25849  N   PHE G 319      18.646  82.308  22.196  1.00 40.20           N  
-ATOM  25850  CA  PHE G 319      20.003  81.976  22.621  1.00 36.78           C  
-ATOM  25851  C   PHE G 319      20.287  82.591  23.984  1.00 36.25           C  
-ATOM  25852  O   PHE G 319      20.248  83.811  24.148  1.00 35.08           O  
-ATOM  25853  CB  PHE G 319      21.049  82.445  21.613  1.00 23.43           C  
-ATOM  25854  CG  PHE G 319      22.461  82.163  22.047  1.00 27.93           C  
-ATOM  25855  CD1 PHE G 319      22.985  80.884  21.956  1.00 24.41           C  
-ATOM  25856  CD2 PHE G 319      23.256  83.171  22.568  1.00 34.64           C  
-ATOM  25857  CE1 PHE G 319      24.278  80.616  22.365  1.00 20.76           C  
-ATOM  25858  CE2 PHE G 319      24.554  82.912  22.973  1.00 38.05           C  
-ATOM  25859  CZ  PHE G 319      25.063  81.632  22.872  1.00 34.94           C  
-ATOM  25860  N   ARG G 320      20.577  81.740  24.960  1.00 27.50           N  
-ATOM  25861  CA  ARG G 320      20.762  82.192  26.329  1.00 26.79           C  
-ATOM  25862  C   ARG G 320      22.185  81.940  26.813  1.00 28.76           C  
-ATOM  25863  O   ARG G 320      22.411  81.163  27.743  1.00 27.85           O  
-ATOM  25864  CB  ARG G 320      19.758  81.498  27.240  1.00 26.30           C  
-ATOM  25865  CG  ARG G 320      18.377  81.417  26.625  1.00 27.15           C  
-ATOM  25866  CD  ARG G 320      17.367  80.866  27.601  1.00 34.42           C  
-ATOM  25867  NE  ARG G 320      16.160  81.679  27.599  1.00 27.16           N  
-ATOM  25868  CZ  ARG G 320      15.487  82.015  28.692  1.00 34.06           C  
-ATOM  25869  NH1 ARG G 320      15.898  81.600  29.883  1.00 34.04           N  
-ATOM  25870  NH2 ARG G 320      14.401  82.765  28.591  1.00 36.24           N  
-ATOM  25871  N   GLY G 321      23.140  82.611  26.176  1.00 21.14           N  
-ATOM  25872  CA  GLY G 321      24.542  82.448  26.505  1.00 16.79           C  
-ATOM  25873  C   GLY G 321      24.912  83.073  27.833  1.00 17.03           C  
-ATOM  25874  O   GLY G 321      25.820  82.597  28.513  1.00 22.33           O  
-ATOM  25875  N   HIS G 322      24.208  84.138  28.204  1.00 17.45           N  
-ATOM  25876  CA  HIS G 322      24.499  84.854  29.441  1.00 18.02           C  
-ATOM  25877  C   HIS G 322      24.339  83.928  30.638  1.00 22.07           C  
-ATOM  25878  O   HIS G 322      23.316  83.260  30.785  1.00 20.70           O  
-ATOM  25879  CB  HIS G 322      23.593  86.076  29.587  1.00 14.65           C  
-ATOM  25880  CG  HIS G 322      24.114  87.101  30.545  1.00 16.99           C  
-ATOM  25881  ND1 HIS G 322      24.216  86.869  31.900  1.00 20.22           N  
-ATOM  25882  CD2 HIS G 322      24.562  88.362  30.345  1.00 22.67           C  
-ATOM  25883  CE1 HIS G 322      24.703  87.944  32.493  1.00 21.13           C  
-ATOM  25884  NE2 HIS G 322      24.922  88.865  31.573  1.00 24.30           N  
-ATOM  25885  N   GLU G 323      25.354  83.902  31.495  1.00 19.35           N  
-ATOM  25886  CA  GLU G 323      25.421  82.928  32.577  1.00 18.55           C  
-ATOM  25887  C   GLU G 323      24.428  83.217  33.704  1.00 21.10           C  
-ATOM  25888  O   GLU G 323      24.249  82.393  34.599  1.00 24.63           O  
-ATOM  25889  CB  GLU G 323      26.848  82.864  33.128  1.00 20.05           C  
-ATOM  25890  CG  GLU G 323      27.877  82.465  32.076  1.00 24.91           C  
-ATOM  25891  CD  GLU G 323      29.300  82.443  32.602  1.00 24.22           C  
-ATOM  25892  OE1 GLU G 323      29.561  83.053  33.662  1.00 31.10           O  
-ATOM  25893  OE2 GLU G 323      30.159  81.813  31.948  1.00 16.46           O  
-ATOM  25894  N   GLU G 324      23.778  84.379  33.649  1.00 19.59           N  
-ATOM  25895  CA  GLU G 324      22.749  84.749  34.624  1.00 19.54           C  
-ATOM  25896  C   GLU G 324      21.469  83.943  34.383  1.00 27.67           C  
-ATOM  25897  O   GLU G 324      20.621  83.781  35.277  1.00 29.18           O  
-ATOM  25898  CB  GLU G 324      22.470  86.252  34.551  1.00 15.25           C  
-ATOM  25899  CG  GLU G 324      21.537  86.781  35.625  1.00 18.77           C  
-ATOM  25900  CD  GLU G 324      21.836  88.225  35.993  1.00 26.57           C  
-ATOM  25901  OE1 GLU G 324      21.208  88.750  36.938  1.00 21.78           O  
-ATOM  25902  OE2 GLU G 324      22.710  88.833  35.339  1.00 29.34           O  
-ATOM  25903  N   PHE G 325      21.347  83.421  33.167  1.00 22.57           N  
-ATOM  25904  CA  PHE G 325      20.230  82.560  32.813  1.00 21.36           C  
-ATOM  25905  C   PHE G 325      20.242  81.279  33.640  1.00 21.99           C  
-ATOM  25906  O   PHE G 325      19.224  80.612  33.760  1.00 28.21           O  
-ATOM  25907  CB  PHE G 325      20.255  82.229  31.320  1.00 24.75           C  
-ATOM  25908  CG  PHE G 325      19.712  83.322  30.446  1.00 26.19           C  
-ATOM  25909  CD1 PHE G 325      18.363  83.635  30.466  1.00 28.66           C  
-ATOM  25910  CD2 PHE G 325      20.545  84.025  29.596  1.00 28.09           C  
-ATOM  25911  CE1 PHE G 325      17.857  84.637  29.658  1.00 30.09           C  
-ATOM  25912  CE2 PHE G 325      20.045  85.027  28.784  1.00 32.08           C  
-ATOM  25913  CZ  PHE G 325      18.699  85.334  28.816  1.00 26.78           C  
-ATOM  25914  N   GLN G 326      21.398  80.936  34.199  1.00 19.69           N  
-ATOM  25915  CA  GLN G 326      21.482  79.822  35.133  1.00 17.40           C  
-ATOM  25916  C   GLN G 326      20.623  80.131  36.345  1.00 20.27           C  
-ATOM  25917  O   GLN G 326      19.814  79.311  36.772  1.00 23.14           O  
-ATOM  25918  CB  GLN G 326      22.929  79.564  35.557  1.00 14.36           C  
-ATOM  25919  CG  GLN G 326      23.838  79.132  34.424  1.00 16.04           C  
-ATOM  25920  CD  GLN G 326      25.264  78.906  34.880  1.00 20.87           C  
-ATOM  25921  OE1 GLN G 326      25.612  77.825  35.358  1.00 20.33           O  
-ATOM  25922  NE2 GLN G 326      26.100  79.928  34.736  1.00 19.54           N  
-ATOM  25923  N   TYR G 327      20.802  81.333  36.881  1.00 18.81           N  
-ATOM  25924  CA  TYR G 327      20.057  81.783  38.047  1.00 21.10           C  
-ATOM  25925  C   TYR G 327      18.575  81.968  37.739  1.00 24.01           C  
-ATOM  25926  O   TYR G 327      17.709  81.510  38.496  1.00 26.49           O  
-ATOM  25927  CB  TYR G 327      20.651  83.089  38.576  1.00 18.74           C  
-ATOM  25928  CG  TYR G 327      19.881  83.703  39.720  1.00 28.29           C  
-ATOM  25929  CD1 TYR G 327      19.949  83.163  40.999  1.00 32.65           C  
-ATOM  25930  CD2 TYR G 327      19.089  84.826  39.524  1.00 21.75           C  
-ATOM  25931  CE1 TYR G 327      19.246  83.723  42.049  1.00 28.38           C  
-ATOM  25932  CE2 TYR G 327      18.385  85.394  40.570  1.00 20.96           C  
-ATOM  25933  CZ  TYR G 327      18.466  84.838  41.828  1.00 22.80           C  
-ATOM  25934  OH  TYR G 327      17.767  85.401  42.870  1.00 30.21           O  
-ATOM  25935  N   LEU G 328      18.284  82.640  36.630  1.00 22.81           N  
-ATOM  25936  CA  LEU G 328      16.893  82.864  36.245  1.00 26.05           C  
-ATOM  25937  C   LEU G 328      16.148  81.543  36.046  1.00 22.48           C  
-ATOM  25938  O   LEU G 328      15.052  81.340  36.592  1.00 25.08           O  
-ATOM  25939  CB  LEU G 328      16.821  83.709  34.973  1.00 30.64           C  
-ATOM  25940  CG  LEU G 328      17.435  85.109  35.073  1.00 22.93           C  
-ATOM  25941  CD1 LEU G 328      17.238  85.886  33.779  1.00 25.71           C  
-ATOM  25942  CD2 LEU G 328      16.857  85.872  36.258  1.00 21.98           C  
-ATOM  25943  N   ASP G 329      16.756  80.643  35.275  1.00 20.03           N  
-ATOM  25944  CA  ASP G 329      16.173  79.324  35.034  1.00 21.05           C  
-ATOM  25945  C   ASP G 329      16.113  78.506  36.316  1.00 24.43           C  
-ATOM  25946  O   ASP G 329      15.283  77.613  36.443  1.00 27.21           O  
-ATOM  25947  CB  ASP G 329      16.956  78.548  33.970  1.00 20.40           C  
-ATOM  25948  CG  ASP G 329      16.809  79.145  32.586  1.00 32.38           C  
-ATOM  25949  OD1 ASP G 329      15.872  79.947  32.383  1.00 40.12           O  
-ATOM  25950  OD2 ASP G 329      17.627  78.809  31.700  1.00 29.28           O  
-ATOM  25951  N   LEU G 330      17.004  78.797  37.258  1.00 20.96           N  
-ATOM  25952  CA  LEU G 330      16.957  78.131  38.552  1.00 21.03           C  
-ATOM  25953  C   LEU G 330      15.682  78.561  39.261  1.00 26.64           C  
-ATOM  25954  O   LEU G 330      14.949  77.731  39.796  1.00 34.61           O  
-ATOM  25955  CB  LEU G 330      18.196  78.462  39.391  1.00 20.54           C  
-ATOM  25956  CG  LEU G 330      18.573  77.565  40.578  1.00 11.46           C  
-ATOM  25957  CD1 LEU G 330      18.046  78.116  41.894  1.00 17.70           C  
-ATOM  25958  CD2 LEU G 330      18.085  76.144  40.357  1.00 10.21           C  
-ATOM  25959  N   ILE G 331      15.412  79.865  39.246  1.00 26.02           N  
-ATOM  25960  CA  ILE G 331      14.181  80.390  39.837  1.00 25.24           C  
-ATOM  25961  C   ILE G 331      12.934  79.788  39.196  1.00 27.03           C  
-ATOM  25962  O   ILE G 331      12.054  79.264  39.893  1.00 24.49           O  
-ATOM  25963  CB  ILE G 331      14.093  81.923  39.714  1.00 23.56           C  
-ATOM  25964  CG1 ILE G 331      15.264  82.582  40.438  1.00 23.02           C  
-ATOM  25965  CG2 ILE G 331      12.768  82.422  40.271  1.00 22.60           C  
-ATOM  25966  CD1 ILE G 331      15.142  84.077  40.516  1.00 24.01           C  
-ATOM  25967  N   ALA G 332      12.857  79.873  37.870  1.00 27.36           N  
-ATOM  25968  CA  ALA G 332      11.701  79.348  37.150  1.00 25.09           C  
-ATOM  25969  C   ALA G 332      11.510  77.850  37.414  1.00 32.68           C  
-ATOM  25970  O   ALA G 332      10.385  77.376  37.595  1.00 37.03           O  
-ATOM  25971  CB  ALA G 332      11.843  79.617  35.665  1.00 25.46           C  
-ATOM  25972  N   ASP G 333      12.619  77.116  37.457  1.00 32.65           N  
-ATOM  25973  CA  ASP G 333      12.578  75.681  37.708  1.00 30.75           C  
-ATOM  25974  C   ASP G 333      12.043  75.389  39.101  1.00 28.70           C  
-ATOM  25975  O   ASP G 333      11.185  74.532  39.266  1.00 34.75           O  
-ATOM  25976  CB  ASP G 333      13.966  75.057  37.542  1.00 30.66           C  
-ATOM  25977  CG  ASP G 333      13.920  73.540  37.456  1.00 44.13           C  
-ATOM  25978  OD1 ASP G 333      12.827  72.949  37.612  1.00 43.79           O  
-ATOM  25979  OD2 ASP G 333      14.988  72.936  37.235  1.00 46.63           O  
-ATOM  25980  N   ILE G 334      12.557  76.095  40.102  1.00 26.56           N  
-ATOM  25981  CA  ILE G 334      12.108  75.886  41.473  1.00 22.09           C  
-ATOM  25982  C   ILE G 334      10.621  76.201  41.602  1.00 30.18           C  
-ATOM  25983  O   ILE G 334       9.876  75.459  42.243  1.00 34.61           O  
-ATOM  25984  CB  ILE G 334      12.909  76.743  42.474  1.00 22.90           C  
-ATOM  25985  CG1 ILE G 334      14.343  76.231  42.572  1.00 17.46           C  
-ATOM  25986  CG2 ILE G 334      12.256  76.717  43.841  1.00 24.87           C  
-ATOM  25987  CD1 ILE G 334      15.157  76.939  43.616  1.00 17.55           C  
-ATOM  25988  N   ILE G 335      10.182  77.293  40.984  1.00 42.67           N  
-ATOM  25989  CA  ILE G 335       8.764  77.642  41.033  1.00 40.79           C  
-ATOM  25990  C   ILE G 335       7.892  76.578  40.352  1.00 31.55           C  
-ATOM  25991  O   ILE G 335       6.866  76.174  40.893  1.00 30.68           O  
-ATOM  25992  CB  ILE G 335       8.496  79.021  40.392  1.00 31.09           C  
-ATOM  25993  CG1 ILE G 335       9.122  80.133  41.241  1.00 34.37           C  
-ATOM  25994  CG2 ILE G 335       7.004  79.261  40.254  1.00 35.71           C  
-ATOM  25995  CD1 ILE G 335       8.806  81.529  40.743  1.00 47.70           C  
-ATOM  25996  N   ASN G 336       8.308  76.114  39.179  1.00 32.72           N  
-ATOM  25997  CA  ASN G 336       7.506  75.165  38.410  1.00 36.50           C  
-ATOM  25998  C   ASN G 336       7.454  73.757  39.004  1.00 35.08           C  
-ATOM  25999  O   ASN G 336       6.378  73.180  39.156  1.00 47.28           O  
-ATOM  26000  CB  ASN G 336       8.027  75.079  36.972  1.00 29.56           C  
-ATOM  26001  CG  ASN G 336       7.807  76.362  36.190  1.00 35.52           C  
-ATOM  26002  OD1 ASN G 336       6.902  77.141  36.490  1.00 42.02           O  
-ATOM  26003  ND2 ASN G 336       8.632  76.582  35.173  1.00 27.75           N  
-ATOM  26004  N   ASN G 337       8.618  73.209  39.338  1.00 33.44           N  
-ATOM  26005  CA  ASN G 337       8.722  71.804  39.716  1.00 34.75           C  
-ATOM  26006  C   ASN G 337       9.014  71.564  41.194  1.00 34.02           C  
-ATOM  26007  O   ASN G 337       8.965  70.425  41.663  1.00 35.03           O  
-ATOM  26008  CB  ASN G 337       9.803  71.126  38.873  1.00 27.60           C  
-ATOM  26009  CG  ASN G 337       9.607  71.354  37.390  1.00 39.29           C  
-ATOM  26010  OD1 ASN G 337       8.483  71.534  36.925  1.00 45.88           O  
-ATOM  26011  ND2 ASN G 337      10.702  71.356  36.638  1.00 48.02           N  
-ATOM  26012  N   GLY G 338       9.314  72.628  41.929  1.00 38.07           N  
-ATOM  26013  CA  GLY G 338       9.621  72.493  43.342  1.00 38.56           C  
-ATOM  26014  C   GLY G 338       8.419  72.049  44.153  1.00 36.74           C  
-ATOM  26015  O   GLY G 338       7.296  72.028  43.649  1.00 36.08           O  
-ATOM  26016  N   ARG G 339       8.655  71.691  45.411  1.00 32.34           N  
-ATOM  26017  CA  ARG G 339       7.574  71.264  46.294  1.00 30.42           C  
-ATOM  26018  C   ARG G 339       7.320  72.295  47.385  1.00 34.00           C  
-ATOM  26019  O   ARG G 339       8.263  72.883  47.916  1.00 35.92           O  
-ATOM  26020  CB  ARG G 339       7.898  69.909  46.922  1.00 31.06           C  
-ATOM  26021  CG  ARG G 339       8.181  68.812  45.919  1.00 34.11           C  
-ATOM  26022  CD  ARG G 339       7.012  68.612  44.973  1.00 36.66           C  
-ATOM  26023  NE  ARG G 339       7.071  67.300  44.340  1.00 50.61           N  
-ATOM  26024  CZ  ARG G 339       6.556  66.197  44.872  1.00 62.34           C  
-ATOM  26025  NH1 ARG G 339       5.935  66.255  46.044  1.00 49.86           N  
-ATOM  26026  NH2 ARG G 339       6.657  65.038  44.235  1.00 63.17           N  
-ATOM  26027  N   THR G 340       6.050  72.515  47.716  1.00 28.19           N  
-ATOM  26028  CA  THR G 340       5.713  73.437  48.793  1.00 27.50           C  
-ATOM  26029  C   THR G 340       5.803  72.746  50.148  1.00 31.13           C  
-ATOM  26030  O   THR G 340       5.126  71.753  50.400  1.00 39.13           O  
-ATOM  26031  CB  THR G 340       4.314  74.026  48.638  1.00 28.72           C  
-ATOM  26032  OG1 THR G 340       4.181  74.617  47.339  1.00 31.30           O  
-ATOM  26033  CG2 THR G 340       4.088  75.085  49.700  1.00 32.31           C  
-ATOM  26034  N   MET G 341       6.642  73.294  51.017  1.00 31.76           N  
-ATOM  26035  CA  MET G 341       6.959  72.691  52.299  1.00 29.71           C  
-ATOM  26036  C   MET G 341       6.896  73.719  53.419  1.00 35.44           C  
-ATOM  26037  O   MET G 341       7.034  74.927  53.180  1.00 44.91           O  
-ATOM  26038  CB  MET G 341       8.358  72.069  52.263  1.00 38.19           C  
-ATOM  26039  CG  MET G 341       8.638  71.184  51.060  1.00 37.01           C  
-ATOM  26040  SD  MET G 341       8.072  69.497  51.318  1.00 59.16           S  
-ATOM  26041  CE  MET G 341       8.991  69.076  52.797  1.00 45.29           C  
-ATOM  26042  N   ASP G 342       6.699  73.228  54.640  1.00 38.13           N  
-ATOM  26043  CA  ASP G 342       6.834  74.052  55.835  1.00 45.24           C  
-ATOM  26044  C   ASP G 342       8.306  74.357  56.085  1.00 46.30           C  
-ATOM  26045  O   ASP G 342       9.182  73.853  55.383  1.00 50.48           O  
-ATOM  26046  CB  ASP G 342       6.214  73.365  57.052  1.00 55.39           C  
-ATOM  26047  CG  ASP G 342       4.717  73.597  57.150  1.00 74.74           C  
-ATOM  26048  OD1 ASP G 342       4.240  74.631  56.631  1.00 68.32           O  
-ATOM  26049  OD2 ASP G 342       4.019  72.752  57.750  1.00 77.76           O  
-ATOM  26050  N   ASP G 343       8.581  75.170  57.096  1.00 44.40           N  
-ATOM  26051  CA  ASP G 343       9.918  75.719  57.259  1.00 38.96           C  
-ATOM  26052  C   ASP G 343      10.150  76.253  58.673  1.00 47.78           C  
-ATOM  26053  O   ASP G 343       9.204  76.638  59.360  1.00 51.97           O  
-ATOM  26054  CB  ASP G 343      10.135  76.811  56.204  1.00 42.04           C  
-ATOM  26055  CG  ASP G 343      11.257  77.754  56.553  1.00 47.21           C  
-ATOM  26056  OD1 ASP G 343      12.433  77.361  56.416  1.00 53.98           O  
-ATOM  26057  OD2 ASP G 343      10.958  78.894  56.959  1.00 40.62           O  
-ATOM  26058  N   ARG G 344      11.412  76.252  59.101  1.00 46.25           N  
-ATOM  26059  CA  ARG G 344      11.811  76.711  60.433  1.00 40.41           C  
-ATOM  26060  C   ARG G 344      11.259  78.089  60.799  1.00 44.84           C  
-ATOM  26061  O   ARG G 344      10.821  78.311  61.929  1.00 50.14           O  
-ATOM  26062  CB  ARG G 344      13.339  76.738  60.537  1.00 40.98           C  
-ATOM  26063  CG  ARG G 344      13.868  77.365  61.816  1.00 43.60           C  
-ATOM  26064  CD  ARG G 344      15.375  77.562  61.762  1.00 53.80           C  
-ATOM  26065  NE  ARG G 344      15.775  78.541  60.753  1.00 48.28           N  
-ATOM  26066  CZ  ARG G 344      15.944  79.838  60.994  1.00 58.91           C  
-ATOM  26067  NH1 ARG G 344      15.745  80.321  62.214  1.00 55.43           N  
-ATOM  26068  NH2 ARG G 344      16.313  80.654  60.016  1.00 56.13           N  
-ATOM  26069  N   THR G 345      11.280  79.006  59.838  1.00 44.10           N  
-ATOM  26070  CA  THR G 345      10.911  80.395  60.088  1.00 45.61           C  
-ATOM  26071  C   THR G 345       9.408  80.584  60.267  1.00 45.40           C  
-ATOM  26072  O   THR G 345       8.968  81.516  60.939  1.00 56.88           O  
-ATOM  26073  CB  THR G 345      11.378  81.309  58.942  1.00 63.24           C  
-ATOM  26074  OG1 THR G 345      10.547  81.098  57.793  1.00 64.34           O  
-ATOM  26075  CG2 THR G 345      12.830  81.014  58.577  1.00 61.93           C  
-ATOM  26076  N   GLY G 346       8.622  79.702  59.659  1.00 41.46           N  
-ATOM  26077  CA  GLY G 346       7.176  79.808  59.725  1.00 41.86           C  
-ATOM  26078  C   GLY G 346       6.586  80.191  58.383  1.00 49.50           C  
-ATOM  26079  O   GLY G 346       5.422  79.905  58.097  1.00 50.34           O  
-ATOM  26080  N   VAL G 347       7.395  80.850  57.559  1.00 48.90           N  
-ATOM  26081  CA  VAL G 347       6.987  81.187  56.203  1.00 43.07           C  
-ATOM  26082  C   VAL G 347       7.111  79.943  55.330  1.00 46.36           C  
-ATOM  26083  O   VAL G 347       8.006  79.125  55.535  1.00 41.76           O  
-ATOM  26084  CB  VAL G 347       7.837  82.327  55.615  1.00 44.90           C  
-ATOM  26085  CG1 VAL G 347       7.038  83.093  54.575  1.00 46.85           C  
-ATOM  26086  CG2 VAL G 347       8.310  83.264  56.720  1.00 39.48           C  
-ATOM  26087  N   GLY G 348       6.206  79.793  54.369  1.00 48.17           N  
-ATOM  26088  CA  GLY G 348       6.217  78.631  53.496  1.00 45.94           C  
-ATOM  26089  C   GLY G 348       7.376  78.680  52.522  1.00 36.49           C  
-ATOM  26090  O   GLY G 348       7.935  79.749  52.279  1.00 38.30           O  
-ATOM  26091  N   VAL G 349       7.742  77.531  51.960  1.00 32.30           N  
-ATOM  26092  CA  VAL G 349       8.872  77.481  51.035  1.00 27.14           C  
-ATOM  26093  C   VAL G 349       8.563  76.591  49.834  1.00 28.94           C  
-ATOM  26094  O   VAL G 349       7.786  75.655  49.941  1.00 29.62           O  
-ATOM  26095  CB  VAL G 349      10.159  76.986  51.759  1.00 29.72           C  
-ATOM  26096  CG1 VAL G 349      10.715  75.711  51.126  1.00 30.04           C  
-ATOM  26097  CG2 VAL G 349      11.208  78.084  51.789  1.00 28.82           C  
-ATOM  26098  N   ILE G 350       9.141  76.910  48.680  1.00 29.38           N  
-ATOM  26099  CA  ILE G 350       9.101  75.999  47.540  1.00 24.91           C  
-ATOM  26100  C   ILE G 350      10.523  75.543  47.241  1.00 31.18           C  
-ATOM  26101  O   ILE G 350      11.380  76.362  46.913  1.00 35.35           O  
-ATOM  26102  CB  ILE G 350       8.497  76.650  46.288  1.00 23.01           C  
-ATOM  26103  CG1 ILE G 350       7.244  77.450  46.644  1.00 34.09           C  
-ATOM  26104  CG2 ILE G 350       8.189  75.589  45.244  1.00 18.40           C  
-ATOM  26105  CD1 ILE G 350       6.661  78.217  45.474  1.00 28.94           C  
-ATOM  26106  N   SER G 351      10.782  74.243  47.356  1.00 27.62           N  
-ATOM  26107  CA  SER G 351      12.162  73.769  47.309  1.00 26.81           C  
-ATOM  26108  C   SER G 351      12.442  72.667  46.290  1.00 27.67           C  
-ATOM  26109  O   SER G 351      11.545  71.929  45.873  1.00 26.42           O  
-ATOM  26110  CB  SER G 351      12.587  73.282  48.698  1.00 27.27           C  
-ATOM  26111  OG  SER G 351      11.778  72.206  49.135  1.00 36.45           O  
-ATOM  26112  N   LYS G 352      13.710  72.590  45.896  1.00 23.68           N  
-ATOM  26113  CA  LYS G 352      14.255  71.471  45.140  1.00 21.10           C  
-ATOM  26114  C   LYS G 352      15.521  70.997  45.848  1.00 26.73           C  
-ATOM  26115  O   LYS G 352      16.020  71.675  46.748  1.00 27.70           O  
-ATOM  26116  CB  LYS G 352      14.564  71.866  43.695  1.00 20.90           C  
-ATOM  26117  CG  LYS G 352      13.352  72.312  42.898  1.00 28.88           C  
-ATOM  26118  CD  LYS G 352      13.590  72.156  41.400  1.00 27.60           C  
-ATOM  26119  CE  LYS G 352      13.873  70.704  41.041  1.00 31.97           C  
-ATOM  26120  NZ  LYS G 352      13.814  70.457  39.574  1.00 29.42           N  
-ATOM  26121  N   PHE G 353      16.045  69.844  45.447  1.00 21.36           N  
-ATOM  26122  CA  PHE G 353      17.233  69.298  46.095  1.00 20.29           C  
-ATOM  26123  C   PHE G 353      18.327  68.973  45.083  1.00 25.47           C  
-ATOM  26124  O   PHE G 353      18.077  68.315  44.072  1.00 31.32           O  
-ATOM  26125  CB  PHE G 353      16.870  68.051  46.899  1.00 25.99           C  
-ATOM  26126  CG  PHE G 353      17.911  67.649  47.905  1.00 24.02           C  
-ATOM  26127  CD1 PHE G 353      18.435  68.577  48.789  1.00 27.28           C  
-ATOM  26128  CD2 PHE G 353      18.347  66.337  47.983  1.00 19.04           C  
-ATOM  26129  CE1 PHE G 353      19.387  68.208  49.723  1.00 25.64           C  
-ATOM  26130  CE2 PHE G 353      19.295  65.960  48.915  1.00 25.22           C  
-ATOM  26131  CZ  PHE G 353      19.816  66.898  49.787  1.00 24.18           C  
-ATOM  26132  N   GLY G 354      19.541  69.435  45.363  1.00 25.38           N  
-ATOM  26133  CA  GLY G 354      20.657  69.225  44.460  1.00 23.04           C  
-ATOM  26134  C   GLY G 354      20.577  70.115  43.238  1.00 20.72           C  
-ATOM  26135  O   GLY G 354      19.960  69.757  42.236  1.00 30.39           O  
-ATOM  26136  N   CYS G 355      21.201  71.283  43.324  1.00 17.64           N  
-ATOM  26137  CA  CYS G 355      21.197  72.235  42.221  1.00 26.13           C  
-ATOM  26138  C   CYS G 355      22.616  72.706  41.917  1.00 27.88           C  
-ATOM  26139  O   CYS G 355      23.475  72.719  42.794  1.00 22.32           O  
-ATOM  26140  CB  CYS G 355      20.291  73.426  42.541  1.00 28.70           C  
-ATOM  26141  SG  CYS G 355      18.534  73.005  42.694  1.00 39.77           S  
-ATOM  26142  N   THR G 356      22.860  73.093  40.671  1.00 28.35           N  
-ATOM  26143  CA  THR G 356      24.212  73.413  40.239  1.00 17.67           C  
-ATOM  26144  C   THR G 356      24.263  74.656  39.362  1.00 18.61           C  
-ATOM  26145  O   THR G 356      23.431  74.836  38.473  1.00 20.56           O  
-ATOM  26146  CB  THR G 356      24.834  72.221  39.475  1.00 22.53           C  
-ATOM  26147  OG1 THR G 356      25.226  71.211  40.412  1.00 27.56           O  
-ATOM  26148  CG2 THR G 356      26.056  72.648  38.666  1.00 28.13           C  
-ATOM  26149  N   MET G 357      25.236  75.520  39.633  1.00 17.18           N  
-ATOM  26150  CA  MET G 357      25.569  76.602  38.714  1.00 16.40           C  
-ATOM  26151  C   MET G 357      27.079  76.703  38.582  1.00 16.65           C  
-ATOM  26152  O   MET G 357      27.804  76.121  39.376  1.00 20.38           O  
-ATOM  26153  CB  MET G 357      24.989  77.928  39.197  1.00 14.24           C  
-ATOM  26154  CG  MET G 357      23.492  78.043  39.028  1.00 13.37           C  
-ATOM  26155  SD  MET G 357      22.865  79.610  39.655  1.00 21.44           S  
-ATOM  26156  CE  MET G 357      23.385  79.518  41.367  1.00 17.05           C  
-ATOM  26157  N   ARG G 358      27.556  77.418  37.571  1.00 13.57           N  
-ATOM  26158  CA  ARG G 358      28.969  77.779  37.523  1.00 16.11           C  
-ATOM  26159  C   ARG G 358      29.193  79.024  36.671  1.00 19.74           C  
-ATOM  26160  O   ARG G 358      28.586  79.195  35.613  1.00 20.87           O  
-ATOM  26161  CB  ARG G 358      29.826  76.613  37.015  1.00 15.13           C  
-ATOM  26162  CG  ARG G 358      29.441  76.057  35.663  1.00 21.85           C  
-ATOM  26163  CD  ARG G 358      30.523  75.115  35.159  1.00 16.67           C  
-ATOM  26164  NE  ARG G 358      30.739  73.989  36.063  1.00 16.82           N  
-ATOM  26165  CZ  ARG G 358      31.905  73.370  36.228  1.00 18.98           C  
-ATOM  26166  NH1 ARG G 358      32.975  73.769  35.557  1.00 17.92           N  
-ATOM  26167  NH2 ARG G 358      32.003  72.352  37.069  1.00 23.05           N  
-ATOM  26168  N   TYR G 359      30.072  79.893  37.159  1.00 16.73           N  
-ATOM  26169  CA  TYR G 359      30.292  81.197  36.555  1.00 16.60           C  
-ATOM  26170  C   TYR G 359      31.758  81.416  36.215  1.00 18.90           C  
-ATOM  26171  O   TYR G 359      32.651  81.061  36.990  1.00 19.49           O  
-ATOM  26172  CB  TYR G 359      29.798  82.300  37.492  1.00 21.92           C  
-ATOM  26173  CG  TYR G 359      28.308  82.256  37.732  1.00 21.37           C  
-ATOM  26174  CD1 TYR G 359      27.435  82.938  36.898  1.00 24.74           C  
-ATOM  26175  CD2 TYR G 359      27.772  81.522  38.783  1.00 18.95           C  
-ATOM  26176  CE1 TYR G 359      26.071  82.898  37.107  1.00 21.17           C  
-ATOM  26177  CE2 TYR G 359      26.407  81.476  38.997  1.00 17.07           C  
-ATOM  26178  CZ  TYR G 359      25.562  82.167  38.155  1.00 16.33           C  
-ATOM  26179  OH  TYR G 359      24.202  82.131  38.356  1.00 22.49           O  
-ATOM  26180  N   SER G 360      31.993  82.002  35.047  1.00 16.71           N  
-ATOM  26181  CA  SER G 360      33.342  82.269  34.579  1.00 19.58           C  
-ATOM  26182  C   SER G 360      33.918  83.488  35.280  1.00 23.20           C  
-ATOM  26183  O   SER G 360      33.198  84.440  35.578  1.00 21.26           O  
-ATOM  26184  CB  SER G 360      33.348  82.474  33.067  1.00 21.61           C  
-ATOM  26185  OG  SER G 360      32.741  81.376  32.410  1.00 20.89           O  
-ATOM  26186  N   LEU G 361      35.221  83.455  35.536  1.00 21.22           N  
-ATOM  26187  CA  LEU G 361      35.877  84.529  36.268  1.00 23.11           C  
-ATOM  26188  C   LEU G 361      37.039  85.139  35.492  1.00 28.96           C  
-ATOM  26189  O   LEU G 361      37.695  86.061  35.977  1.00 31.87           O  
-ATOM  26190  CB  LEU G 361      36.381  84.016  37.619  1.00 26.20           C  
-ATOM  26191  CG  LEU G 361      35.348  83.363  38.538  1.00 21.68           C  
-ATOM  26192  CD1 LEU G 361      36.015  82.821  39.790  1.00 17.20           C  
-ATOM  26193  CD2 LEU G 361      34.258  84.350  38.899  1.00 16.51           C  
-ATOM  26194  N   ASP G 362      37.295  84.627  34.291  1.00 28.98           N  
-ATOM  26195  CA  ASP G 362      38.454  85.062  33.518  1.00 24.88           C  
-ATOM  26196  C   ASP G 362      38.155  86.275  32.635  1.00 28.52           C  
-ATOM  26197  O   ASP G 362      39.065  87.009  32.252  1.00 31.85           O  
-ATOM  26198  CB  ASP G 362      38.979  83.909  32.659  1.00 25.02           C  
-ATOM  26199  CG  ASP G 362      37.965  83.431  31.639  1.00 34.39           C  
-ATOM  26200  OD1 ASP G 362      37.007  82.733  32.034  1.00 38.19           O  
-ATOM  26201  OD2 ASP G 362      38.127  83.751  30.441  1.00 26.31           O  
-ATOM  26202  N   GLN G 363      36.883  86.487  32.314  1.00 32.65           N  
-ATOM  26203  CA  GLN G 363      36.500  87.617  31.472  1.00 29.10           C  
-ATOM  26204  C   GLN G 363      35.856  88.727  32.295  1.00 23.05           C  
-ATOM  26205  O   GLN G 363      36.280  89.880  32.239  1.00 19.65           O  
-ATOM  26206  CB  GLN G 363      35.549  87.162  30.365  1.00 39.31           C  
-ATOM  26207  CG  GLN G 363      36.141  86.120  29.424  1.00 46.30           C  
-ATOM  26208  CD  GLN G 363      37.241  86.681  28.546  1.00 35.73           C  
-ATOM  26209  OE1 GLN G 363      37.031  87.644  27.806  1.00 41.12           O  
-ATOM  26210  NE2 GLN G 363      38.423  86.080  28.623  1.00 36.75           N  
-ATOM  26211  N   ALA G 364      34.830  88.373  33.061  1.00 22.07           N  
-ATOM  26212  CA  ALA G 364      34.150  89.336  33.917  1.00 18.49           C  
-ATOM  26213  C   ALA G 364      33.748  88.697  35.243  1.00 20.45           C  
-ATOM  26214  O   ALA G 364      34.109  87.556  35.528  1.00 23.52           O  
-ATOM  26215  CB  ALA G 364      32.937  89.908  33.210  1.00 13.10           C  
-ATOM  26216  N   PHE G 365      32.998  89.437  36.050  1.00 15.79           N  
-ATOM  26217  CA  PHE G 365      32.649  88.991  37.391  1.00 14.12           C  
-ATOM  26218  C   PHE G 365      31.142  88.820  37.512  1.00 19.75           C  
-ATOM  26219  O   PHE G 365      30.386  89.738  37.190  1.00 21.52           O  
-ATOM  26220  CB  PHE G 365      33.164  89.988  38.430  1.00 17.70           C  
-ATOM  26221  CG  PHE G 365      33.001  89.534  39.853  1.00 18.87           C  
-ATOM  26222  CD1 PHE G 365      31.847  89.827  40.564  1.00 20.08           C  
-ATOM  26223  CD2 PHE G 365      34.014  88.839  40.490  1.00 17.78           C  
-ATOM  26224  CE1 PHE G 365      31.701  89.418  41.876  1.00 16.75           C  
-ATOM  26225  CE2 PHE G 365      33.875  88.431  41.800  1.00 19.06           C  
-ATOM  26226  CZ  PHE G 365      32.717  88.719  42.494  1.00 16.51           C  
-ATOM  26227  N   PRO G 366      30.702  87.645  37.988  1.00 21.27           N  
-ATOM  26228  CA  PRO G 366      29.279  87.306  38.078  1.00 15.58           C  
-ATOM  26229  C   PRO G 366      28.550  88.063  39.186  1.00 20.01           C  
-ATOM  26230  O   PRO G 366      28.028  87.449  40.117  1.00 27.41           O  
-ATOM  26231  CB  PRO G 366      29.298  85.806  38.367  1.00 13.25           C  
-ATOM  26232  CG  PRO G 366      30.569  85.592  39.096  1.00 15.57           C  
-ATOM  26233  CD  PRO G 366      31.558  86.567  38.513  1.00 16.15           C  
-ATOM  26234  N   LEU G 367      28.525  89.387  39.086  1.00 17.00           N  
-ATOM  26235  CA  LEU G 367      27.659  90.185  39.936  1.00 19.47           C  
-ATOM  26236  C   LEU G 367      26.330  90.344  39.202  1.00 21.81           C  
-ATOM  26237  O   LEU G 367      26.229  91.114  38.247  1.00 23.30           O  
-ATOM  26238  CB  LEU G 367      28.291  91.541  40.256  1.00 14.41           C  
-ATOM  26239  CG  LEU G 367      27.646  92.349  41.385  1.00 10.14           C  
-ATOM  26240  CD1 LEU G 367      27.673  91.568  42.688  1.00 16.86           C  
-ATOM  26241  CD2 LEU G 367      28.337  93.693  41.553  1.00  8.44           C  
-ATOM  26242  N   LEU G 368      25.324  89.594  39.646  1.00 14.89           N  
-ATOM  26243  CA  LEU G 368      24.049  89.483  38.940  1.00 18.05           C  
-ATOM  26244  C   LEU G 368      23.433  90.841  38.629  1.00 20.95           C  
-ATOM  26245  O   LEU G 368      23.460  91.751  39.454  1.00 22.00           O  
-ATOM  26246  CB  LEU G 368      23.067  88.632  39.749  1.00 24.62           C  
-ATOM  26247  CG  LEU G 368      23.372  87.131  39.820  1.00 26.72           C  
-ATOM  26248  CD1 LEU G 368      23.795  86.602  38.457  1.00 20.83           C  
-ATOM  26249  CD2 LEU G 368      24.431  86.813  40.867  1.00 31.37           C  
-ATOM  26250  N   THR G 369      22.877  90.964  37.427  1.00 18.66           N  
-ATOM  26251  CA  THR G 369      22.450  92.259  36.912  1.00 19.60           C  
-ATOM  26252  C   THR G 369      20.938  92.434  36.857  1.00 22.76           C  
-ATOM  26253  O   THR G 369      20.443  93.557  36.771  1.00 29.74           O  
-ATOM  26254  CB  THR G 369      23.007  92.497  35.502  1.00 20.86           C  
-ATOM  26255  OG1 THR G 369      22.475  91.513  34.608  1.00 22.43           O  
-ATOM  26256  CG2 THR G 369      24.526  92.407  35.508  1.00 20.04           C  
-ATOM  26257  N   THR G 370      20.201  91.330  36.903  1.00 21.54           N  
-ATOM  26258  CA  THR G 370      18.750  91.397  36.781  1.00 19.06           C  
-ATOM  26259  C   THR G 370      18.122  92.016  38.036  1.00 21.65           C  
-ATOM  26260  O   THR G 370      16.931  92.327  38.057  1.00 21.26           O  
-ATOM  26261  CB  THR G 370      18.148  90.005  36.508  1.00 17.44           C  
-ATOM  26262  OG1 THR G 370      16.793  90.142  36.065  1.00 34.41           O  
-ATOM  26263  CG2 THR G 370      18.190  89.149  37.749  1.00 20.70           C  
-ATOM  26264  N   LYS G 371      18.938  92.187  39.075  1.00 26.37           N  
-ATOM  26265  CA  LYS G 371      18.597  93.007  40.238  1.00 27.72           C  
-ATOM  26266  C   LYS G 371      19.893  93.483  40.897  1.00 30.93           C  
-ATOM  26267  O   LYS G 371      20.924  92.816  40.796  1.00 34.57           O  
-ATOM  26268  CB  LYS G 371      17.736  92.236  41.242  1.00 25.66           C  
-ATOM  26269  CG  LYS G 371      18.533  91.465  42.274  1.00 37.77           C  
-ATOM  26270  CD  LYS G 371      17.744  91.266  43.555  1.00 48.59           C  
-ATOM  26271  CE  LYS G 371      18.603  90.604  44.621  1.00 59.83           C  
-ATOM  26272  NZ  LYS G 371      17.859  90.401  45.894  1.00 65.90           N  
-ATOM  26273  N   ARG G 372      19.850  94.633  41.562  1.00 30.65           N  
-ATOM  26274  CA  ARG G 372      21.063  95.204  42.147  1.00 26.26           C  
-ATOM  26275  C   ARG G 372      21.522  94.437  43.384  1.00 26.01           C  
-ATOM  26276  O   ARG G 372      20.757  94.249  44.330  1.00 28.81           O  
-ATOM  26277  CB  ARG G 372      20.852  96.677  42.502  1.00 35.88           C  
-ATOM  26278  CG  ARG G 372      22.059  97.315  43.173  1.00 29.53           C  
-ATOM  26279  CD  ARG G 372      21.878  98.811  43.362  1.00 35.18           C  
-ATOM  26280  NE  ARG G 372      21.764  99.520  42.090  1.00 37.30           N  
-ATOM  26281  CZ  ARG G 372      22.802  99.918  41.363  1.00 28.72           C  
-ATOM  26282  NH1 ARG G 372      24.038  99.670  41.777  1.00 18.95           N  
-ATOM  26283  NH2 ARG G 372      22.604 100.560  40.218  1.00 22.28           N  
-ATOM  26284  N   VAL G 373      22.781  94.008  43.372  1.00 22.95           N  
-ATOM  26285  CA  VAL G 373      23.345  93.218  44.462  1.00 22.00           C  
-ATOM  26286  C   VAL G 373      24.209  94.078  45.390  1.00 26.05           C  
-ATOM  26287  O   VAL G 373      24.929  94.971  44.937  1.00 21.03           O  
-ATOM  26288  CB  VAL G 373      24.172  92.034  43.909  1.00 18.85           C  
-ATOM  26289  CG1 VAL G 373      24.839  91.252  45.032  1.00 11.65           C  
-ATOM  26290  CG2 VAL G 373      23.280  91.120  43.083  1.00 21.57           C  
-ATOM  26291  N   PHE G 374      24.119  93.796  46.689  1.00 28.67           N  
-ATOM  26292  CA  PHE G 374      24.788  94.567  47.737  1.00 20.28           C  
-ATOM  26293  C   PHE G 374      26.294  94.279  47.816  1.00 25.16           C  
-ATOM  26294  O   PHE G 374      26.773  93.600  48.735  1.00 30.18           O  
-ATOM  26295  CB  PHE G 374      24.126  94.272  49.082  1.00 21.56           C  
-ATOM  26296  CG  PHE G 374      24.464  95.257  50.157  1.00 20.88           C  
-ATOM  26297  CD1 PHE G 374      24.818  96.556  49.839  1.00 22.67           C  
-ATOM  26298  CD2 PHE G 374      24.440  94.879  51.489  1.00 16.39           C  
-ATOM  26299  CE1 PHE G 374      25.135  97.464  50.832  1.00 27.24           C  
-ATOM  26300  CE2 PHE G 374      24.755  95.775  52.481  1.00 16.26           C  
-ATOM  26301  CZ  PHE G 374      25.103  97.070  52.156  1.00 25.98           C  
-ATOM  26302  N   TRP G 375      27.041  94.824  46.863  1.00 21.60           N  
-ATOM  26303  CA  TRP G 375      28.461  94.516  46.729  1.00 21.41           C  
-ATOM  26304  C   TRP G 375      29.280  94.982  47.924  1.00 24.84           C  
-ATOM  26305  O   TRP G 375      30.218  94.300  48.341  1.00 31.45           O  
-ATOM  26306  CB  TRP G 375      29.033  95.132  45.455  1.00 17.94           C  
-ATOM  26307  CG  TRP G 375      30.480  94.805  45.283  1.00 27.68           C  
-ATOM  26308  CD1 TRP G 375      31.009  93.609  44.887  1.00 28.03           C  
-ATOM  26309  CD2 TRP G 375      31.589  95.677  45.515  1.00 22.54           C  
-ATOM  26310  NE1 TRP G 375      32.380  93.685  44.851  1.00 22.78           N  
-ATOM  26311  CE2 TRP G 375      32.761  94.945  45.235  1.00 28.22           C  
-ATOM  26312  CE3 TRP G 375      31.706  97.008  45.928  1.00 32.76           C  
-ATOM  26313  CZ2 TRP G 375      34.031  95.501  45.350  1.00 48.95           C  
-ATOM  26314  CZ3 TRP G 375      32.973  97.559  46.046  1.00 45.86           C  
-ATOM  26315  CH2 TRP G 375      34.117  96.807  45.758  1.00 53.13           C  
-ATOM  26316  N   LYS G 376      28.938  96.150  48.456  1.00 20.24           N  
-ATOM  26317  CA  LYS G 376      29.565  96.646  49.673  1.00 23.09           C  
-ATOM  26318  C   LYS G 376      29.395  95.603  50.769  1.00 28.70           C  
-ATOM  26319  O   LYS G 376      30.318  95.313  51.536  1.00 27.71           O  
-ATOM  26320  CB  LYS G 376      28.946  97.978  50.093  1.00 31.32           C  
-ATOM  26321  CG  LYS G 376      29.521  98.562  51.375  1.00 29.97           C  
-ATOM  26322  CD  LYS G 376      28.685  99.745  51.841  1.00 39.01           C  
-ATOM  26323  CE  LYS G 376      29.183 100.303  53.165  1.00 43.78           C  
-ATOM  26324  NZ  LYS G 376      30.454 101.068  53.027  1.00 45.01           N  
-ATOM  26325  N   GLY G 377      28.199  95.028  50.807  1.00 22.36           N  
-ATOM  26326  CA  GLY G 377      27.880  93.959  51.727  1.00 20.23           C  
-ATOM  26327  C   GLY G 377      28.752  92.735  51.527  1.00 22.21           C  
-ATOM  26328  O   GLY G 377      29.332  92.236  52.494  1.00 26.35           O  
-ATOM  26329  N   VAL G 378      28.866  92.244  50.293  1.00 19.95           N  
-ATOM  26330  CA  VAL G 378      29.649  91.018  50.089  1.00 24.46           C  
-ATOM  26331  C   VAL G 378      31.133  91.251  50.395  1.00 24.75           C  
-ATOM  26332  O   VAL G 378      31.801  90.376  50.962  1.00 30.38           O  
-ATOM  26333  CB  VAL G 378      29.477  90.429  48.647  1.00 18.40           C  
-ATOM  26334  CG1 VAL G 378      28.341  91.105  47.909  1.00 18.30           C  
-ATOM  26335  CG2 VAL G 378      30.767  90.497  47.840  1.00 22.05           C  
-ATOM  26336  N   LEU G 379      31.634  92.438  50.062  1.00 14.68           N  
-ATOM  26337  CA  LEU G 379      33.034  92.768  50.304  1.00 19.04           C  
-ATOM  26338  C   LEU G 379      33.319  92.850  51.795  1.00 22.74           C  
-ATOM  26339  O   LEU G 379      34.202  92.158  52.312  1.00 26.84           O  
-ATOM  26340  CB  LEU G 379      33.405  94.089  49.617  1.00 25.52           C  
-ATOM  26341  CG  LEU G 379      34.833  94.590  49.849  1.00 18.68           C  
-ATOM  26342  CD1 LEU G 379      35.864  93.581  49.366  1.00 18.45           C  
-ATOM  26343  CD2 LEU G 379      35.045  95.933  49.174  1.00 24.46           C  
-ATOM  26344  N   GLU G 380      32.558  93.698  52.479  1.00 19.64           N  
-ATOM  26345  CA  GLU G 380      32.741  93.903  53.909  1.00 24.79           C  
-ATOM  26346  C   GLU G 380      32.580  92.595  54.675  1.00 26.75           C  
-ATOM  26347  O   GLU G 380      33.377  92.294  55.563  1.00 25.35           O  
-ATOM  26348  CB  GLU G 380      31.756  94.952  54.436  1.00 23.52           C  
-ATOM  26349  CG  GLU G 380      32.393  95.966  55.366  1.00 29.89           C  
-ATOM  26350  CD  GLU G 380      33.505  96.751  54.692  1.00 36.21           C  
-ATOM  26351  OE1 GLU G 380      34.643  96.742  55.209  1.00 39.57           O  
-ATOM  26352  OE2 GLU G 380      33.240  97.375  53.644  1.00 25.85           O  
-ATOM  26353  N   GLU G 381      31.563  91.814  54.317  1.00 21.34           N  
-ATOM  26354  CA  GLU G 381      31.324  90.537  54.984  1.00 20.32           C  
-ATOM  26355  C   GLU G 381      32.449  89.546  54.709  1.00 22.02           C  
-ATOM  26356  O   GLU G 381      32.797  88.755  55.581  1.00 21.69           O  
-ATOM  26357  CB  GLU G 381      29.985  89.920  54.559  1.00 27.15           C  
-ATOM  26358  CG  GLU G 381      29.532  88.780  55.476  1.00 25.01           C  
-ATOM  26359  CD  GLU G 381      28.534  87.839  54.821  1.00 32.07           C  
-ATOM  26360  OE1 GLU G 381      27.610  87.365  55.519  1.00 33.02           O  
-ATOM  26361  OE2 GLU G 381      28.685  87.556  53.614  1.00 34.45           O  
-ATOM  26362  N   LEU G 382      33.012  89.577  53.503  1.00 24.43           N  
-ATOM  26363  CA  LEU G 382      34.099  88.657  53.175  1.00 18.78           C  
-ATOM  26364  C   LEU G 382      35.365  88.998  53.952  1.00 17.24           C  
-ATOM  26365  O   LEU G 382      36.012  88.112  54.511  1.00 18.58           O  
-ATOM  26366  CB  LEU G 382      34.386  88.656  51.668  1.00 17.43           C  
-ATOM  26367  CG  LEU G 382      35.444  87.642  51.213  1.00 21.31           C  
-ATOM  26368  CD1 LEU G 382      35.125  86.241  51.723  1.00 20.86           C  
-ATOM  26369  CD2 LEU G 382      35.573  87.639  49.698  1.00 15.47           C  
-ATOM  26370  N   LEU G 383      35.720  90.279  53.981  1.00 19.11           N  
-ATOM  26371  CA  LEU G 383      36.867  90.727  54.771  1.00 17.84           C  
-ATOM  26372  C   LEU G 383      36.660  90.352  56.236  1.00 20.14           C  
-ATOM  26373  O   LEU G 383      37.573  89.860  56.912  1.00 24.00           O  
-ATOM  26374  CB  LEU G 383      37.069  92.239  54.622  1.00 23.09           C  
-ATOM  26375  CG  LEU G 383      37.988  92.729  53.495  1.00 23.52           C  
-ATOM  26376  CD1 LEU G 383      37.939  91.801  52.294  1.00 25.06           C  
-ATOM  26377  CD2 LEU G 383      37.623  94.151  53.084  1.00 23.03           C  
-ATOM  26378  N   TRP G 384      35.433  90.577  56.696  1.00 17.17           N  
-ATOM  26379  CA  TRP G 384      34.987  90.209  58.035  1.00 20.01           C  
-ATOM  26380  C   TRP G 384      35.226  88.728  58.319  1.00 20.33           C  
-ATOM  26381  O   TRP G 384      35.666  88.362  59.409  1.00 16.19           O  
-ATOM  26382  CB  TRP G 384      33.502  90.554  58.191  1.00 30.64           C  
-ATOM  26383  CG  TRP G 384      32.943  90.377  59.570  1.00 24.62           C  
-ATOM  26384  CD1 TRP G 384      33.251  91.105  60.681  1.00 28.26           C  
-ATOM  26385  CD2 TRP G 384      31.946  89.433  59.972  1.00 21.17           C  
-ATOM  26386  NE1 TRP G 384      32.522  90.659  61.756  1.00 26.12           N  
-ATOM  26387  CE2 TRP G 384      31.711  89.633  61.346  1.00 25.32           C  
-ATOM  26388  CE3 TRP G 384      31.235  88.431  59.306  1.00 24.09           C  
-ATOM  26389  CZ2 TRP G 384      30.796  88.870  62.066  1.00 27.69           C  
-ATOM  26390  CZ3 TRP G 384      30.326  87.674  60.022  1.00 30.61           C  
-ATOM  26391  CH2 TRP G 384      30.114  87.898  61.387  1.00 32.39           C  
-ATOM  26392  N   PHE G 385      34.930  87.884  57.331  1.00 25.68           N  
-ATOM  26393  CA  PHE G 385      35.213  86.454  57.417  1.00 21.60           C  
-ATOM  26394  C   PHE G 385      36.700  86.207  57.578  1.00 18.90           C  
-ATOM  26395  O   PHE G 385      37.129  85.532  58.510  1.00 28.99           O  
-ATOM  26396  CB  PHE G 385      34.719  85.719  56.171  1.00 20.67           C  
-ATOM  26397  CG  PHE G 385      33.233  85.540  56.116  1.00 23.06           C  
-ATOM  26398  CD1 PHE G 385      32.483  85.481  57.278  1.00 24.15           C  
-ATOM  26399  CD2 PHE G 385      32.586  85.426  54.897  1.00 19.74           C  
-ATOM  26400  CE1 PHE G 385      31.115  85.315  57.225  1.00 23.46           C  
-ATOM  26401  CE2 PHE G 385      31.217  85.260  54.839  1.00 19.31           C  
-ATOM  26402  CZ  PHE G 385      30.481  85.203  56.003  1.00 25.17           C  
-ATOM  26403  N   ILE G 386      37.477  86.759  56.651  1.00 19.00           N  
-ATOM  26404  CA  ILE G 386      38.919  86.539  56.619  1.00 23.95           C  
-ATOM  26405  C   ILE G 386      39.589  86.915  57.937  1.00 25.02           C  
-ATOM  26406  O   ILE G 386      40.497  86.222  58.395  1.00 24.05           O  
-ATOM  26407  CB  ILE G 386      39.569  87.321  55.457  1.00 22.06           C  
-ATOM  26408  CG1 ILE G 386      39.058  86.780  54.119  1.00 15.05           C  
-ATOM  26409  CG2 ILE G 386      41.088  87.227  55.516  1.00 19.61           C  
-ATOM  26410  CD1 ILE G 386      39.742  87.371  52.927  1.00 13.38           C  
-ATOM  26411  N   ARG G 387      39.128  87.993  58.564  1.00 25.25           N  
-ATOM  26412  CA  ARG G 387      39.708  88.401  59.843  1.00 23.65           C  
-ATOM  26413  C   ARG G 387      39.384  87.421  60.973  1.00 24.40           C  
-ATOM  26414  O   ARG G 387      40.000  87.468  62.041  1.00 20.75           O  
-ATOM  26415  CB  ARG G 387      39.232  89.800  60.228  1.00 18.53           C  
-ATOM  26416  CG  ARG G 387      39.623  90.872  59.232  1.00 25.93           C  
-ATOM  26417  CD  ARG G 387      39.363  92.261  59.785  1.00 18.97           C  
-ATOM  26418  NE  ARG G 387      39.373  93.255  58.719  1.00 15.72           N  
-ATOM  26419  CZ  ARG G 387      38.283  93.674  58.086  1.00 20.93           C  
-ATOM  26420  NH1 ARG G 387      37.091  93.195  58.423  1.00 26.40           N  
-ATOM  26421  NH2 ARG G 387      38.382  94.577  57.122  1.00 20.99           N  
-ATOM  26422  N   GLY G 388      38.423  86.532  60.734  1.00 28.20           N  
-ATOM  26423  CA  GLY G 388      37.986  85.589  61.749  1.00 23.98           C  
-ATOM  26424  C   GLY G 388      37.086  86.279  62.754  1.00 31.07           C  
-ATOM  26425  O   GLY G 388      36.904  85.809  63.878  1.00 36.06           O  
-ATOM  26426  N   ASP G 389      36.516  87.404  62.335  1.00 22.28           N  
-ATOM  26427  CA  ASP G 389      35.699  88.234  63.209  1.00 22.74           C  
-ATOM  26428  C   ASP G 389      34.318  87.626  63.433  1.00 25.36           C  
-ATOM  26429  O   ASP G 389      33.695  87.116  62.502  1.00 25.30           O  
-ATOM  26430  CB  ASP G 389      35.571  89.636  62.616  1.00 29.85           C  
-ATOM  26431  CG  ASP G 389      35.194  90.684  63.648  1.00 31.73           C  
-ATOM  26432  OD1 ASP G 389      34.700  90.320  64.737  1.00 28.21           O  
-ATOM  26433  OD2 ASP G 389      35.393  91.884  63.359  1.00 21.93           O  
-ATOM  26434  N   THR G 390      33.843  87.688  64.673  1.00 30.28           N  
-ATOM  26435  CA  THR G 390      32.525  87.164  65.014  1.00 27.28           C  
-ATOM  26436  C   THR G 390      31.620  88.259  65.573  1.00 25.00           C  
-ATOM  26437  O   THR G 390      30.506  87.991  66.024  1.00 21.91           O  
-ATOM  26438  CB  THR G 390      32.624  86.016  66.033  1.00 21.73           C  
-ATOM  26439  OG1 THR G 390      33.287  86.480  67.215  1.00 21.91           O  
-ATOM  26440  CG2 THR G 390      33.410  84.855  65.444  1.00 26.30           C  
-ATOM  26441  N   ASN G 391      32.106  89.495  65.531  1.00 31.02           N  
-ATOM  26442  CA  ASN G 391      31.354  90.648  66.014  1.00 25.72           C  
-ATOM  26443  C   ASN G 391      30.552  91.298  64.887  1.00 34.43           C  
-ATOM  26444  O   ASN G 391      31.111  92.012  64.053  1.00 37.75           O  
-ATOM  26445  CB  ASN G 391      32.308  91.666  66.646  1.00 22.23           C  
-ATOM  26446  CG  ASN G 391      31.588  92.712  67.473  1.00 29.94           C  
-ATOM  26447  OD1 ASN G 391      30.414  93.002  67.248  1.00 46.11           O  
-ATOM  26448  ND2 ASN G 391      32.294  93.289  68.437  1.00 26.29           N  
-ATOM  26449  N   ALA G 392      29.244  91.056  64.873  1.00 28.15           N  
-ATOM  26450  CA  ALA G 392      28.385  91.545  63.798  1.00 26.50           C  
-ATOM  26451  C   ALA G 392      28.244  93.062  63.831  1.00 25.03           C  
-ATOM  26452  O   ALA G 392      27.864  93.681  62.839  1.00 32.81           O  
-ATOM  26453  CB  ALA G 392      27.014  90.883  63.875  1.00 31.25           C  
-ATOM  26454  N   ASN G 393      28.548  93.658  64.976  1.00 24.66           N  
-ATOM  26455  CA  ASN G 393      28.458  95.103  65.120  1.00 26.86           C  
-ATOM  26456  C   ASN G 393      29.499  95.805  64.260  1.00 35.63           C  
-ATOM  26457  O   ASN G 393      29.275  96.919  63.782  1.00 40.13           O  
-ATOM  26458  CB  ASN G 393      28.614  95.497  66.586  1.00 21.03           C  
-ATOM  26459  CG  ASN G 393      27.577  94.839  67.471  1.00 31.17           C  
-ATOM  26460  OD1 ASN G 393      26.385  94.838  67.157  1.00 35.71           O  
-ATOM  26461  ND2 ASN G 393      28.026  94.266  68.580  1.00 30.88           N  
-ATOM  26462  N   HIS G 394      30.632  95.140  64.058  1.00 36.89           N  
-ATOM  26463  CA  HIS G 394      31.676  95.645  63.173  1.00 29.40           C  
-ATOM  26464  C   HIS G 394      31.165  95.758  61.738  1.00 32.62           C  
-ATOM  26465  O   HIS G 394      31.648  96.580  60.963  1.00 34.01           O  
-ATOM  26466  CB  HIS G 394      32.910  94.743  63.227  1.00 23.65           C  
-ATOM  26467  CG  HIS G 394      33.575  94.714  64.566  1.00 21.24           C  
-ATOM  26468  ND1 HIS G 394      34.570  93.815  64.883  1.00 25.60           N  
-ATOM  26469  CD2 HIS G 394      33.392  95.477  65.668  1.00 24.75           C  
-ATOM  26470  CE1 HIS G 394      34.970  94.024  66.124  1.00 22.56           C  
-ATOM  26471  NE2 HIS G 394      34.272  95.028  66.623  1.00 26.32           N  
-ATOM  26472  N   LEU G 395      30.197  94.919  61.387  1.00 28.81           N  
-ATOM  26473  CA  LEU G 395      29.551  95.003  60.083  1.00 28.51           C  
-ATOM  26474  C   LEU G 395      28.428  96.026  60.116  1.00 32.42           C  
-ATOM  26475  O   LEU G 395      28.171  96.714  59.130  1.00 34.11           O  
-ATOM  26476  CB  LEU G 395      28.994  93.643  59.655  1.00 26.16           C  
-ATOM  26477  CG  LEU G 395      29.966  92.574  59.157  1.00 30.05           C  
-ATOM  26478  CD1 LEU G 395      29.202  91.316  58.769  1.00 29.12           C  
-ATOM  26479  CD2 LEU G 395      30.790  93.091  57.988  1.00 25.97           C  
-ATOM  26480  N   SER G 396      27.761  96.113  61.260  1.00 39.84           N  
-ATOM  26481  CA  SER G 396      26.568  96.933  61.393  1.00 38.29           C  
-ATOM  26482  C   SER G 396      26.888  98.423  61.359  1.00 37.07           C  
-ATOM  26483  O   SER G 396      26.146  99.202  60.762  1.00 37.71           O  
-ATOM  26484  CB  SER G 396      25.832  96.584  62.688  1.00 37.08           C  
-ATOM  26485  OG  SER G 396      24.440  96.832  62.574  1.00 45.89           O  
-ATOM  26486  N   GLU G 397      27.988  98.820  61.995  1.00 40.90           N  
-ATOM  26487  CA  GLU G 397      28.346 100.236  62.060  1.00 44.24           C  
-ATOM  26488  C   GLU G 397      29.112 100.676  60.803  1.00 42.08           C  
-ATOM  26489  O   GLU G 397      29.457 101.851  60.645  1.00 44.79           O  
-ATOM  26490  CB  GLU G 397      29.140 100.529  63.346  1.00 44.29           C  
-ATOM  26491  CG  GLU G 397      30.627 100.825  63.188  1.00 60.10           C  
-ATOM  26492  CD  GLU G 397      31.467  99.576  63.065  1.00 65.29           C  
-ATOM  26493  OE1 GLU G 397      31.845  99.002  64.111  1.00 61.99           O  
-ATOM  26494  OE2 GLU G 397      31.753  99.170  61.922  1.00 64.15           O  
-ATOM  26495  N   LYS G 398      29.341  99.734  59.892  1.00 37.69           N  
-ATOM  26496  CA  LYS G 398      29.894 100.060  58.581  1.00 31.01           C  
-ATOM  26497  C   LYS G 398      28.794 100.200  57.529  1.00 31.98           C  
-ATOM  26498  O   LYS G 398      29.073 100.510  56.372  1.00 34.55           O  
-ATOM  26499  CB  LYS G 398      30.899  99.003  58.133  1.00 28.92           C  
-ATOM  26500  CG  LYS G 398      32.248  99.088  58.830  1.00 41.99           C  
-ATOM  26501  CD  LYS G 398      33.261  98.158  58.187  1.00 36.62           C  
-ATOM  26502  CE  LYS G 398      34.574  98.153  58.954  1.00 36.31           C  
-ATOM  26503  NZ  LYS G 398      34.387  97.672  60.350  1.00 30.07           N  
-ATOM  26504  N   GLY G 399      27.547  99.968  57.928  1.00 30.78           N  
-ATOM  26505  CA  GLY G 399      26.421 100.124  57.024  1.00 25.75           C  
-ATOM  26506  C   GLY G 399      25.897  98.811  56.480  1.00 28.23           C  
-ATOM  26507  O   GLY G 399      25.055  98.796  55.582  1.00 26.23           O  
-ATOM  26508  N   VAL G 400      26.395  97.706  57.030  1.00 34.63           N  
-ATOM  26509  CA  VAL G 400      25.980  96.371  56.603  1.00 39.50           C  
-ATOM  26510  C   VAL G 400      25.238  95.650  57.732  1.00 41.99           C  
-ATOM  26511  O   VAL G 400      25.856  95.076  58.633  1.00 40.79           O  
-ATOM  26512  CB  VAL G 400      27.189  95.522  56.149  1.00 27.17           C  
-ATOM  26513  CG1 VAL G 400      26.730  94.189  55.597  1.00 26.10           C  
-ATOM  26514  CG2 VAL G 400      27.996  96.270  55.100  1.00 28.43           C  
-ATOM  26515  N   LYS G 401      23.910  95.680  57.676  1.00 36.51           N  
-ATOM  26516  CA  LYS G 401      23.085  95.157  58.763  1.00 47.10           C  
-ATOM  26517  C   LYS G 401      22.502  93.790  58.445  1.00 46.65           C  
-ATOM  26518  O   LYS G 401      21.422  93.442  58.920  1.00 44.98           O  
-ATOM  26519  CB  LYS G 401      21.950  96.133  59.079  1.00 42.27           C  
-ATOM  26520  CG  LYS G 401      22.404  97.496  59.557  1.00 40.84           C  
-ATOM  26521  CD  LYS G 401      21.468  98.581  59.056  1.00 48.26           C  
-ATOM  26522  CE  LYS G 401      21.513  98.682  57.535  1.00 69.66           C  
-ATOM  26523  NZ  LYS G 401      20.596  99.739  57.018  1.00 68.45           N  
-ATOM  26524  N   ILE G 402      23.225  93.014  57.649  1.00 42.79           N  
-ATOM  26525  CA  ILE G 402      22.713  91.742  57.160  1.00 50.65           C  
-ATOM  26526  C   ILE G 402      22.753  90.645  58.222  1.00 50.59           C  
-ATOM  26527  O   ILE G 402      22.265  89.537  57.999  1.00 49.26           O  
-ATOM  26528  CB  ILE G 402      23.499  91.276  55.930  1.00 42.81           C  
-ATOM  26529  CG1 ILE G 402      24.871  90.752  56.349  1.00 46.74           C  
-ATOM  26530  CG2 ILE G 402      23.652  92.423  54.949  1.00 47.37           C  
-ATOM  26531  CD1 ILE G 402      25.714  90.267  55.196  1.00 37.67           C  
-ATOM  26532  N   TRP G 403      23.329  90.955  59.378  1.00 47.59           N  
-ATOM  26533  CA  TRP G 403      23.432  89.980  60.459  1.00 49.37           C  
-ATOM  26534  C   TRP G 403      22.590  90.355  61.675  1.00 47.18           C  
-ATOM  26535  O   TRP G 403      22.317  89.509  62.526  1.00 44.66           O  
-ATOM  26536  CB  TRP G 403      24.893  89.808  60.880  1.00 48.45           C  
-ATOM  26537  CG  TRP G 403      25.620  88.751  60.112  1.00 43.54           C  
-ATOM  26538  CD1 TRP G 403      26.365  88.922  58.982  1.00 36.99           C  
-ATOM  26539  CD2 TRP G 403      25.675  87.354  60.422  1.00 50.19           C  
-ATOM  26540  NE1 TRP G 403      26.881  87.717  58.569  1.00 37.59           N  
-ATOM  26541  CE2 TRP G 403      26.472  86.738  59.438  1.00 51.09           C  
-ATOM  26542  CE3 TRP G 403      25.128  86.562  61.439  1.00 50.82           C  
-ATOM  26543  CZ2 TRP G 403      26.735  85.370  59.438  1.00 53.55           C  
-ATOM  26544  CZ3 TRP G 403      25.390  85.204  61.438  1.00 52.77           C  
-ATOM  26545  CH2 TRP G 403      26.187  84.622  60.444  1.00 54.98           C  
-ATOM  26546  N   ASP G 404      22.177  91.616  61.743  1.00 48.04           N  
-ATOM  26547  CA  ASP G 404      21.480  92.160  62.906  1.00 49.03           C  
-ATOM  26548  C   ASP G 404      20.318  91.296  63.396  1.00 42.94           C  
-ATOM  26549  O   ASP G 404      20.281  90.888  64.560  1.00 50.11           O  
-ATOM  26550  CB  ASP G 404      20.977  93.568  62.585  1.00 59.83           C  
-ATOM  26551  CG  ASP G 404      22.109  94.558  62.368  1.00 61.28           C  
-ATOM  26552  OD1 ASP G 404      23.263  94.123  62.158  1.00 58.71           O  
-ATOM  26553  OD2 ASP G 404      21.839  95.776  62.408  1.00 48.42           O  
-ATOM  26554  N   LYS G 405      19.387  90.996  62.497  1.00 38.60           N  
-ATOM  26555  CA  LYS G 405      18.195  90.233  62.853  1.00 42.73           C  
-ATOM  26556  C   LYS G 405      18.494  88.831  63.397  1.00 39.00           C  
-ATOM  26557  O   LYS G 405      17.600  88.167  63.915  1.00 36.46           O  
-ATOM  26558  CB  LYS G 405      17.263  90.124  61.643  1.00 44.95           C  
-ATOM  26559  CG  LYS G 405      16.504  91.400  61.320  1.00 53.95           C  
-ATOM  26560  CD  LYS G 405      15.556  91.190  60.153  1.00 57.10           C  
-ATOM  26561  CE  LYS G 405      14.758  92.449  59.873  1.00 63.95           C  
-ATOM  26562  NZ  LYS G 405      13.905  92.312  58.663  1.00 63.07           N  
-ATOM  26563  N   ASN G 406      19.743  88.385  63.288  1.00 48.45           N  
-ATOM  26564  CA  ASN G 406      20.122  87.061  63.780  1.00 41.65           C  
-ATOM  26565  C   ASN G 406      21.096  87.120  64.951  1.00 36.28           C  
-ATOM  26566  O   ASN G 406      21.633  86.099  65.371  1.00 39.45           O  
-ATOM  26567  CB  ASN G 406      20.724  86.223  62.649  1.00 39.65           C  
-ATOM  26568  CG  ASN G 406      19.682  85.766  61.649  1.00 44.87           C  
-ATOM  26569  OD1 ASN G 406      19.752  86.097  60.465  1.00 60.86           O  
-ATOM  26570  ND2 ASN G 406      18.705  85.004  62.122  1.00 39.91           N  
-ATOM  26571  N   VAL G 407      21.325  88.319  65.475  1.00 35.19           N  
-ATOM  26572  CA  VAL G 407      22.178  88.476  66.650  1.00 43.10           C  
-ATOM  26573  C   VAL G 407      21.525  89.383  67.687  1.00 49.64           C  
-ATOM  26574  O   VAL G 407      22.182  89.868  68.611  1.00 45.69           O  
-ATOM  26575  CB  VAL G 407      23.566  89.039  66.282  1.00 41.96           C  
-ATOM  26576  CG1 VAL G 407      24.384  87.997  65.537  1.00 41.10           C  
-ATOM  26577  CG2 VAL G 407      23.428  90.316  65.467  1.00 43.42           C  
-ATOM  26578  N   THR G 408      20.225  89.606  67.529  1.00 44.74           N  
-ATOM  26579  CA  THR G 408      19.455  90.342  68.520  1.00 43.92           C  
-ATOM  26580  C   THR G 408      19.387  89.548  69.817  1.00 54.82           C  
-ATOM  26581  O   THR G 408      19.598  88.337  69.814  1.00 56.24           O  
-ATOM  26582  CB  THR G 408      18.024  90.635  68.028  1.00 39.88           C  
-ATOM  26583  OG1 THR G 408      17.381  89.406  67.670  1.00 34.28           O  
-ATOM  26584  CG2 THR G 408      18.050  91.551  66.824  1.00 42.61           C  
-ATOM  26585  N   ARG G 409      19.103  90.232  70.921  1.00 48.60           N  
-ATOM  26586  CA  ARG G 409      18.927  89.574  72.212  1.00 42.02           C  
-ATOM  26587  C   ARG G 409      17.837  88.505  72.137  1.00 47.14           C  
-ATOM  26588  O   ARG G 409      17.997  87.392  72.648  1.00 50.33           O  
-ATOM  26589  CB  ARG G 409      18.594  90.615  73.288  1.00 36.62           C  
-ATOM  26590  CG  ARG G 409      18.094  90.053  74.605  1.00 45.31           C  
-ATOM  26591  CD  ARG G 409      19.230  89.679  75.546  1.00 43.02           C  
-ATOM  26592  NE  ARG G 409      19.798  88.368  75.246  1.00 48.74           N  
-ATOM  26593  CZ  ARG G 409      21.046  88.163  74.835  1.00 55.29           C  
-ATOM  26594  NH1 ARG G 409      21.877  89.186  74.675  1.00 51.43           N  
-ATOM  26595  NH2 ARG G 409      21.466  86.930  74.589  1.00 52.28           N  
-ATOM  26596  N   GLU G 410      16.739  88.857  71.479  1.00 44.05           N  
-ATOM  26597  CA  GLU G 410      15.600  87.965  71.317  1.00 46.99           C  
-ATOM  26598  C   GLU G 410      15.968  86.683  70.570  1.00 45.64           C  
-ATOM  26599  O   GLU G 410      15.590  85.584  70.987  1.00 42.88           O  
-ATOM  26600  CB  GLU G 410      14.468  88.701  70.589  1.00 52.21           C  
-ATOM  26601  CG  GLU G 410      13.112  88.025  70.669  1.00 69.77           C  
-ATOM  26602  CD  GLU G 410      12.019  88.857  70.024  1.00 87.10           C  
-ATOM  26603  OE1 GLU G 410      11.795  88.699  68.805  1.00 83.89           O  
-ATOM  26604  OE2 GLU G 410      11.389  89.673  70.731  1.00 89.04           O  
-ATOM  26605  N   PHE G 411      16.709  86.826  69.474  1.00 46.99           N  
-ATOM  26606  CA  PHE G 411      17.102  85.672  68.664  1.00 48.86           C  
-ATOM  26607  C   PHE G 411      18.152  84.826  69.374  1.00 41.02           C  
-ATOM  26608  O   PHE G 411      18.082  83.597  69.359  1.00 41.99           O  
-ATOM  26609  CB  PHE G 411      17.633  86.116  67.293  1.00 38.80           C  
-ATOM  26610  CG  PHE G 411      17.842  84.980  66.325  1.00 38.42           C  
-ATOM  26611  CD1 PHE G 411      16.803  84.541  65.519  1.00 36.45           C  
-ATOM  26612  CD2 PHE G 411      19.071  84.344  66.231  1.00 38.09           C  
-ATOM  26613  CE1 PHE G 411      16.985  83.490  64.632  1.00 42.79           C  
-ATOM  26614  CE2 PHE G 411      19.260  83.290  65.345  1.00 38.50           C  
-ATOM  26615  CZ  PHE G 411      18.215  82.866  64.546  1.00 44.57           C  
-ATOM  26616  N   LEU G 412      19.128  85.491  69.985  1.00 36.17           N  
-ATOM  26617  CA  LEU G 412      20.168  84.808  70.746  1.00 40.25           C  
-ATOM  26618  C   LEU G 412      19.563  84.005  71.891  1.00 48.46           C  
-ATOM  26619  O   LEU G 412      20.063  82.934  72.238  1.00 43.69           O  
-ATOM  26620  CB  LEU G 412      21.192  85.814  71.281  1.00 36.89           C  
-ATOM  26621  CG  LEU G 412      22.189  86.364  70.255  1.00 41.63           C  
-ATOM  26622  CD1 LEU G 412      23.131  87.385  70.884  1.00 39.69           C  
-ATOM  26623  CD2 LEU G 412      22.971  85.230  69.612  1.00 33.39           C  
-ATOM  26624  N   ASP G 413      18.485  84.526  72.470  1.00 56.13           N  
-ATOM  26625  CA  ASP G 413      17.777  83.824  73.532  1.00 44.08           C  
-ATOM  26626  C   ASP G 413      16.938  82.675  72.976  1.00 41.84           C  
-ATOM  26627  O   ASP G 413      16.854  81.606  73.584  1.00 38.27           O  
-ATOM  26628  CB  ASP G 413      16.897  84.796  74.320  1.00 44.71           C  
-ATOM  26629  CG  ASP G 413      17.701  85.666  75.268  1.00 51.85           C  
-ATOM  26630  OD1 ASP G 413      18.678  85.152  75.852  1.00 55.04           O  
-ATOM  26631  OD2 ASP G 413      17.359  86.856  75.434  1.00 47.41           O  
-ATOM  26632  N   SER G 414      16.318  82.897  71.820  1.00 48.34           N  
-ATOM  26633  CA  SER G 414      15.522  81.857  71.174  1.00 46.50           C  
-ATOM  26634  C   SER G 414      16.418  80.711  70.712  1.00 44.78           C  
-ATOM  26635  O   SER G 414      15.950  79.598  70.477  1.00 44.20           O  
-ATOM  26636  CB  SER G 414      14.738  82.428  69.991  1.00 49.53           C  
-ATOM  26637  OG  SER G 414      15.584  82.658  68.877  1.00 35.28           O  
-ATOM  26638  N   ARG G 415      17.711  80.998  70.589  1.00 52.54           N  
-ATOM  26639  CA  ARG G 415      18.713  79.999  70.226  1.00 53.05           C  
-ATOM  26640  C   ARG G 415      19.289  79.367  71.499  1.00 50.71           C  
-ATOM  26641  O   ARG G 415      20.292  78.651  71.459  1.00 43.25           O  
-ATOM  26642  CB  ARG G 415      19.820  80.644  69.379  1.00 43.20           C  
-ATOM  26643  CG  ARG G 415      20.789  79.682  68.693  1.00 40.81           C  
-ATOM  26644  CD  ARG G 415      20.313  79.267  67.308  1.00 39.53           C  
-ATOM  26645  NE  ARG G 415      21.301  78.434  66.622  1.00 46.86           N  
-ATOM  26646  CZ  ARG G 415      21.193  77.119  66.462  1.00 51.80           C  
-ATOM  26647  NH1 ARG G 415      22.142  76.447  65.824  1.00 54.82           N  
-ATOM  26648  NH2 ARG G 415      20.134  76.475  66.932  1.00 52.05           N  
-ATOM  26649  N   ASN G 416      18.635  79.639  72.627  1.00 50.26           N  
-ATOM  26650  CA  ASN G 416      19.067  79.148  73.933  1.00 48.63           C  
-ATOM  26651  C   ASN G 416      20.508  79.563  74.232  1.00 42.96           C  
-ATOM  26652  O   ASN G 416      21.350  78.735  74.576  1.00 38.70           O  
-ATOM  26653  CB  ASN G 416      18.911  77.626  74.011  1.00 46.71           C  
-ATOM  26654  CG  ASN G 416      18.944  77.108  75.435  1.00 54.77           C  
-ATOM  26655  OD1 ASN G 416      18.978  77.882  76.393  1.00 50.52           O  
-ATOM  26656  ND2 ASN G 416      18.924  75.788  75.582  1.00 57.87           N  
-ATOM  26657  N   LEU G 417      20.779  80.856  74.087  1.00 48.62           N  
-ATOM  26658  CA  LEU G 417      22.110  81.407  74.330  1.00 52.95           C  
-ATOM  26659  C   LEU G 417      22.050  82.775  75.004  1.00 51.86           C  
-ATOM  26660  O   LEU G 417      22.373  83.786  74.384  1.00 47.16           O  
-ATOM  26661  CB  LEU G 417      22.884  81.517  73.016  1.00 44.66           C  
-ATOM  26662  CG  LEU G 417      23.845  80.380  72.680  1.00 44.54           C  
-ATOM  26663  CD1 LEU G 417      24.356  80.528  71.259  1.00 35.78           C  
-ATOM  26664  CD2 LEU G 417      24.998  80.376  73.669  1.00 61.75           C  
-ATOM  26665  N   PRO G 418      21.637  82.811  76.282  1.00 55.78           N  
-ATOM  26666  CA  PRO G 418      21.514  84.087  76.996  1.00 56.15           C  
-ATOM  26667  C   PRO G 418      22.866  84.706  77.336  1.00 52.80           C  
-ATOM  26668  O   PRO G 418      22.942  85.906  77.597  1.00 54.60           O  
-ATOM  26669  CB  PRO G 418      20.756  83.703  78.277  1.00 56.66           C  
-ATOM  26670  CG  PRO G 418      20.172  82.346  78.003  1.00 52.34           C  
-ATOM  26671  CD  PRO G 418      21.158  81.687  77.101  1.00 51.43           C  
-ATOM  26672  N   HIS G 419      23.917  83.893  77.324  1.00 55.95           N  
-ATOM  26673  CA  HIS G 419      25.253  84.352  77.693  1.00 55.22           C  
-ATOM  26674  C   HIS G 419      25.898  85.194  76.596  1.00 47.57           C  
-ATOM  26675  O   HIS G 419      26.923  85.839  76.816  1.00 35.70           O  
-ATOM  26676  CB  HIS G 419      26.144  83.153  78.031  1.00 61.14           C  
-ATOM  26677  CG  HIS G 419      25.764  82.464  79.305  1.00 96.25           C  
-ATOM  26678  ND1 HIS G 419      26.526  82.545  80.451  1.00101.90           N  
-ATOM  26679  CD2 HIS G 419      24.697  81.690  79.617  1.00 96.46           C  
-ATOM  26680  CE1 HIS G 419      25.947  81.847  81.412  1.00 93.95           C  
-ATOM  26681  NE2 HIS G 419      24.836  81.319  80.933  1.00 97.11           N  
-ATOM  26682  N   ARG G 420      25.288  85.190  75.416  1.00 41.35           N  
-ATOM  26683  CA  ARG G 420      25.847  85.884  74.263  1.00 38.30           C  
-ATOM  26684  C   ARG G 420      25.546  87.377  74.280  1.00 42.76           C  
-ATOM  26685  O   ARG G 420      24.393  87.790  74.409  1.00 44.99           O  
-ATOM  26686  CB  ARG G 420      25.315  85.275  72.966  1.00 43.16           C  
-ATOM  26687  CG  ARG G 420      25.879  83.902  72.639  1.00 54.29           C  
-ATOM  26688  CD  ARG G 420      27.225  84.000  71.939  1.00 32.17           C  
-ATOM  26689  NE  ARG G 420      27.749  82.683  71.593  1.00 35.53           N  
-ATOM  26690  CZ  ARG G 420      28.614  82.005  72.340  1.00 43.60           C  
-ATOM  26691  NH1 ARG G 420      29.038  80.809  71.951  1.00 42.97           N  
-ATOM  26692  NH2 ARG G 420      29.060  82.525  73.475  1.00 40.88           N  
-ATOM  26693  N   GLU G 421      26.595  88.180  74.146  1.00 36.14           N  
-ATOM  26694  CA  GLU G 421      26.450  89.617  73.965  1.00 35.73           C  
-ATOM  26695  C   GLU G 421      25.776  89.883  72.620  1.00 38.09           C  
-ATOM  26696  O   GLU G 421      25.941  89.109  71.678  1.00 50.44           O  
-ATOM  26697  CB  GLU G 421      27.817  90.300  74.044  1.00 39.85           C  
-ATOM  26698  CG  GLU G 421      27.789  91.820  74.050  1.00 53.48           C  
-ATOM  26699  CD  GLU G 421      29.165  92.418  74.288  1.00 55.02           C  
-ATOM  26700  OE1 GLU G 421      29.951  91.818  75.056  1.00 35.77           O  
-ATOM  26701  OE2 GLU G 421      29.464  93.480  73.700  1.00 56.85           O  
-ATOM  26702  N   VAL G 422      25.004  90.962  72.531  1.00 36.93           N  
-ATOM  26703  CA  VAL G 422      24.293  91.279  71.295  1.00 41.06           C  
-ATOM  26704  C   VAL G 422      25.271  91.573  70.163  1.00 37.82           C  
-ATOM  26705  O   VAL G 422      26.075  92.500  70.251  1.00 41.12           O  
-ATOM  26706  CB  VAL G 422      23.348  92.483  71.467  1.00 43.05           C  
-ATOM  26707  CG1 VAL G 422      22.670  92.813  70.146  1.00 27.09           C  
-ATOM  26708  CG2 VAL G 422      22.310  92.198  72.546  1.00 45.97           C  
-ATOM  26709  N   GLY G 423      25.200  90.770  69.104  1.00 42.01           N  
-ATOM  26710  CA  GLY G 423      26.083  90.921  67.961  1.00 40.49           C  
-ATOM  26711  C   GLY G 423      27.042  89.754  67.798  1.00 44.39           C  
-ATOM  26712  O   GLY G 423      27.713  89.624  66.771  1.00 41.04           O  
-ATOM  26713  N   ASP G 424      27.102  88.904  68.817  1.00 39.36           N  
-ATOM  26714  CA  ASP G 424      28.014  87.767  68.829  1.00 23.24           C  
-ATOM  26715  C   ASP G 424      27.409  86.569  68.105  1.00 28.08           C  
-ATOM  26716  O   ASP G 424      26.490  85.927  68.611  1.00 45.90           O  
-ATOM  26717  CB  ASP G 424      28.368  87.397  70.270  1.00 26.39           C  
-ATOM  26718  CG  ASP G 424      29.617  86.546  70.369  1.00 34.68           C  
-ATOM  26719  OD1 ASP G 424      29.864  85.723  69.462  1.00 31.69           O  
-ATOM  26720  OD2 ASP G 424      30.357  86.704  71.363  1.00 35.72           O  
-ATOM  26721  N   ILE G 425      27.938  86.264  66.926  1.00 26.45           N  
-ATOM  26722  CA  ILE G 425      27.422  85.166  66.118  1.00 27.48           C  
-ATOM  26723  C   ILE G 425      27.938  83.819  66.607  1.00 27.58           C  
-ATOM  26724  O   ILE G 425      27.558  82.772  66.085  1.00 32.25           O  
-ATOM  26725  CB  ILE G 425      27.802  85.330  64.636  1.00 24.69           C  
-ATOM  26726  CG1 ILE G 425      29.280  84.997  64.426  1.00 21.94           C  
-ATOM  26727  CG2 ILE G 425      27.498  86.740  64.163  1.00 33.11           C  
-ATOM  26728  CD1 ILE G 425      29.669  84.860  62.974  1.00 25.18           C  
-ATOM  26729  N   GLY G 426      28.804  83.851  67.613  1.00 26.78           N  
-ATOM  26730  CA  GLY G 426      29.415  82.640  68.123  1.00 29.60           C  
-ATOM  26731  C   GLY G 426      30.536  82.162  67.221  1.00 30.04           C  
-ATOM  26732  O   GLY G 426      30.972  82.887  66.329  1.00 30.40           O  
-ATOM  26733  N   PRO G 427      31.011  80.930  67.448  1.00 32.33           N  
-ATOM  26734  CA  PRO G 427      32.114  80.351  66.675  1.00 28.20           C  
-ATOM  26735  C   PRO G 427      31.706  79.928  65.262  1.00 34.27           C  
-ATOM  26736  O   PRO G 427      31.711  78.735  64.962  1.00 34.62           O  
-ATOM  26737  CB  PRO G 427      32.512  79.131  67.510  1.00 27.38           C  
-ATOM  26738  CG  PRO G 427      31.261  78.735  68.204  1.00 32.08           C  
-ATOM  26739  CD  PRO G 427      30.538  80.019  68.506  1.00 31.97           C  
-ATOM  26740  N   GLY G 428      31.376  80.891  64.406  1.00 33.41           N  
-ATOM  26741  CA  GLY G 428      30.917  80.581  63.063  1.00 29.44           C  
-ATOM  26742  C   GLY G 428      31.784  81.133  61.947  1.00 31.31           C  
-ATOM  26743  O   GLY G 428      32.623  82.006  62.175  1.00 38.99           O  
-ATOM  26744  N   TYR G 429      31.562  80.608  60.741  1.00 32.71           N  
-ATOM  26745  CA  TYR G 429      32.258  81.009  59.512  1.00 26.18           C  
-ATOM  26746  C   TYR G 429      33.732  81.363  59.698  1.00 29.60           C  
-ATOM  26747  O   TYR G 429      34.586  80.480  59.718  1.00 36.93           O  
-ATOM  26748  CB  TYR G 429      31.530  82.184  58.858  1.00 23.43           C  
-ATOM  26749  CG  TYR G 429      30.167  81.818  58.318  1.00 23.96           C  
-ATOM  26750  CD1 TYR G 429      30.024  80.835  57.349  1.00 24.40           C  
-ATOM  26751  CD2 TYR G 429      29.024  82.459  58.774  1.00 31.18           C  
-ATOM  26752  CE1 TYR G 429      28.780  80.495  56.852  1.00 24.48           C  
-ATOM  26753  CE2 TYR G 429      27.775  82.130  58.281  1.00 31.92           C  
-ATOM  26754  CZ  TYR G 429      27.658  81.148  57.320  1.00 33.72           C  
-ATOM  26755  OH  TYR G 429      26.415  80.820  56.830  1.00 46.51           O  
-ATOM  26756  N   GLY G 430      34.022  82.654  59.830  1.00 24.92           N  
-ATOM  26757  CA  GLY G 430      35.390  83.125  59.971  1.00 22.65           C  
-ATOM  26758  C   GLY G 430      36.163  82.450  61.088  1.00 25.40           C  
-ATOM  26759  O   GLY G 430      37.347  82.124  60.938  1.00 29.23           O  
-ATOM  26760  N   PHE G 431      35.485  82.232  62.209  1.00 23.49           N  
-ATOM  26761  CA  PHE G 431      36.112  81.623  63.371  1.00 29.02           C  
-ATOM  26762  C   PHE G 431      36.567  80.201  63.094  1.00 26.31           C  
-ATOM  26763  O   PHE G 431      37.600  79.775  63.601  1.00 24.00           O  
-ATOM  26764  CB  PHE G 431      35.166  81.620  64.567  1.00 29.18           C  
-ATOM  26765  CG  PHE G 431      35.776  81.042  65.815  1.00 25.40           C  
-ATOM  26766  CD1 PHE G 431      36.555  81.826  66.648  1.00 25.53           C  
-ATOM  26767  CD2 PHE G 431      35.580  79.713  66.147  1.00 21.74           C  
-ATOM  26768  CE1 PHE G 431      37.118  81.296  67.792  1.00 28.54           C  
-ATOM  26769  CE2 PHE G 431      36.139  79.178  67.289  1.00 16.49           C  
-ATOM  26770  CZ  PHE G 431      36.909  79.969  68.113  1.00 20.40           C  
-ATOM  26771  N   GLN G 432      35.789  79.460  62.313  1.00 28.74           N  
-ATOM  26772  CA  GLN G 432      36.171  78.098  61.972  1.00 25.97           C  
-ATOM  26773  C   GLN G 432      37.252  78.139  60.899  1.00 27.54           C  
-ATOM  26774  O   GLN G 432      38.197  77.349  60.924  1.00 32.44           O  
-ATOM  26775  CB  GLN G 432      34.954  77.289  61.512  1.00 31.04           C  
-ATOM  26776  CG  GLN G 432      33.880  77.118  62.592  1.00 31.17           C  
-ATOM  26777  CD  GLN G 432      34.377  76.334  63.802  1.00 29.88           C  
-ATOM  26778  OE1 GLN G 432      35.151  75.386  63.669  1.00 28.81           O  
-ATOM  26779  NE2 GLN G 432      33.929  76.731  64.988  1.00 27.81           N  
-ATOM  26780  N   TRP G 433      37.109  79.083  59.972  1.00 26.35           N  
-ATOM  26781  CA  TRP G 433      38.094  79.315  58.917  1.00 31.95           C  
-ATOM  26782  C   TRP G 433      39.503  79.490  59.470  1.00 28.22           C  
-ATOM  26783  O   TRP G 433      40.439  78.820  59.036  1.00 26.53           O  
-ATOM  26784  CB  TRP G 433      37.733  80.560  58.097  1.00 24.63           C  
-ATOM  26785  CG  TRP G 433      36.605  80.397  57.131  1.00 22.96           C  
-ATOM  26786  CD1 TRP G 433      35.666  79.409  57.119  1.00 22.42           C  
-ATOM  26787  CD2 TRP G 433      36.301  81.255  56.024  1.00 31.92           C  
-ATOM  26788  NE1 TRP G 433      34.793  79.600  56.077  1.00 30.51           N  
-ATOM  26789  CE2 TRP G 433      35.161  80.726  55.390  1.00 29.89           C  
-ATOM  26790  CE3 TRP G 433      36.883  82.418  55.511  1.00 30.15           C  
-ATOM  26791  CZ2 TRP G 433      34.592  81.322  54.264  1.00 22.95           C  
-ATOM  26792  CZ3 TRP G 433      36.317  83.007  54.396  1.00 27.69           C  
-ATOM  26793  CH2 TRP G 433      35.183  82.458  53.785  1.00 24.37           C  
-ATOM  26794  N   ARG G 434      39.646  80.395  60.433  1.00 25.83           N  
-ATOM  26795  CA  ARG G 434      40.966  80.773  60.920  1.00 24.05           C  
-ATOM  26796  C   ARG G 434      41.363  80.015  62.186  1.00 27.29           C  
-ATOM  26797  O   ARG G 434      42.545  79.947  62.534  1.00 25.23           O  
-ATOM  26798  CB  ARG G 434      41.017  82.283  61.172  1.00 22.69           C  
-ATOM  26799  CG  ARG G 434      40.488  83.131  60.021  1.00 24.56           C  
-ATOM  26800  CD  ARG G 434      41.087  82.705  58.689  1.00 27.95           C  
-ATOM  26801  NE  ARG G 434      42.544  82.771  58.697  1.00 24.51           N  
-ATOM  26802  CZ  ARG G 434      43.243  83.829  58.304  1.00 22.97           C  
-ATOM  26803  NH1 ARG G 434      44.567  83.801  58.344  1.00 19.50           N  
-ATOM  26804  NH2 ARG G 434      42.619  84.915  57.867  1.00 29.25           N  
-ATOM  26805  N   HIS G 435      40.376  79.451  62.874  1.00 20.87           N  
-ATOM  26806  CA  HIS G 435      40.628  78.772  64.139  1.00 24.81           C  
-ATOM  26807  C   HIS G 435      39.728  77.562  64.344  1.00 24.80           C  
-ATOM  26808  O   HIS G 435      39.114  77.435  65.401  1.00 27.80           O  
-ATOM  26809  CB  HIS G 435      40.424  79.729  65.319  1.00 24.18           C  
-ATOM  26810  CG  HIS G 435      40.870  81.133  65.055  1.00 26.13           C  
-ATOM  26811  ND1 HIS G 435      42.187  81.527  65.152  1.00 28.24           N  
-ATOM  26812  CD2 HIS G 435      40.172  82.237  64.698  1.00 26.06           C  
-ATOM  26813  CE1 HIS G 435      42.281  82.813  64.864  1.00 30.30           C  
-ATOM  26814  NE2 HIS G 435      41.073  83.268  64.586  1.00 23.93           N  
-ATOM  26815  N   PHE G 436      39.646  76.675  63.357  1.00 22.39           N  
-ATOM  26816  CA  PHE G 436      38.784  75.497  63.477  1.00 28.72           C  
-ATOM  26817  C   PHE G 436      39.078  74.686  64.743  1.00 26.25           C  
-ATOM  26818  O   PHE G 436      40.216  74.285  64.990  1.00 27.02           O  
-ATOM  26819  CB  PHE G 436      38.926  74.591  62.249  1.00 28.78           C  
-ATOM  26820  CG  PHE G 436      37.918  73.474  62.205  1.00 26.11           C  
-ATOM  26821  CD1 PHE G 436      38.175  72.266  62.830  1.00 22.06           C  
-ATOM  26822  CD2 PHE G 436      36.707  73.638  61.549  1.00 32.06           C  
-ATOM  26823  CE1 PHE G 436      37.247  71.242  62.804  1.00 27.10           C  
-ATOM  26824  CE2 PHE G 436      35.775  72.615  61.517  1.00 30.67           C  
-ATOM  26825  CZ  PHE G 436      36.046  71.416  62.143  1.00 29.51           C  
-ATOM  26826  N   GLY G 437      38.041  74.453  65.541  1.00 25.17           N  
-ATOM  26827  CA  GLY G 437      38.146  73.590  66.704  1.00 29.50           C  
-ATOM  26828  C   GLY G 437      38.474  74.298  68.003  1.00 21.68           C  
-ATOM  26829  O   GLY G 437      38.277  73.742  69.083  1.00 20.33           O  
-ATOM  26830  N   ALA G 438      38.976  75.524  67.902  1.00 19.54           N  
-ATOM  26831  CA  ALA G 438      39.356  76.295  69.079  1.00 20.19           C  
-ATOM  26832  C   ALA G 438      38.159  76.542  70.000  1.00 29.76           C  
-ATOM  26833  O   ALA G 438      37.031  76.708  69.535  1.00 21.65           O  
-ATOM  26834  CB  ALA G 438      39.986  77.612  68.659  1.00 19.45           C  
-ATOM  26835  N   ALA G 439      38.412  76.555  71.306  1.00 34.55           N  
-ATOM  26836  CA  ALA G 439      37.359  76.787  72.290  1.00 30.26           C  
-ATOM  26837  C   ALA G 439      36.934  78.249  72.288  1.00 27.72           C  
-ATOM  26838  O   ALA G 439      37.733  79.138  72.580  1.00 31.27           O  
-ATOM  26839  CB  ALA G 439      37.821  76.370  73.680  1.00 44.90           C  
-ATOM  26840  N   TYR G 440      35.670  78.488  71.959  1.00 29.82           N  
-ATOM  26841  CA  TYR G 440      35.144  79.843  71.841  1.00 28.19           C  
-ATOM  26842  C   TYR G 440      34.742  80.415  73.197  1.00 29.47           C  
-ATOM  26843  O   TYR G 440      34.173  79.715  74.032  1.00 34.26           O  
-ATOM  26844  CB  TYR G 440      33.942  79.858  70.891  1.00 28.82           C  
-ATOM  26845  CG  TYR G 440      33.460  81.240  70.506  1.00 31.29           C  
-ATOM  26846  CD1 TYR G 440      34.052  81.936  69.458  1.00 31.59           C  
-ATOM  26847  CD2 TYR G 440      32.406  81.845  71.180  1.00 33.43           C  
-ATOM  26848  CE1 TYR G 440      33.613  83.197  69.099  1.00 27.25           C  
-ATOM  26849  CE2 TYR G 440      31.961  83.107  70.827  1.00 29.73           C  
-ATOM  26850  CZ  TYR G 440      32.567  83.777  69.787  1.00 28.76           C  
-ATOM  26851  OH  TYR G 440      32.127  85.031  69.435  1.00 27.91           O  
-ATOM  26852  N   LYS G 441      35.048  81.689  73.413  1.00 33.22           N  
-ATOM  26853  CA  LYS G 441      34.571  82.402  74.593  1.00 36.88           C  
-ATOM  26854  C   LYS G 441      33.565  83.474  74.182  1.00 35.18           C  
-ATOM  26855  O   LYS G 441      32.356  83.278  74.295  1.00 29.52           O  
-ATOM  26856  CB  LYS G 441      35.734  83.028  75.367  1.00 42.54           C  
-ATOM  26857  CG  LYS G 441      36.536  82.047  76.209  1.00 50.27           C  
-ATOM  26858  CD  LYS G 441      37.663  81.403  75.416  1.00 59.53           C  
-ATOM  26859  CE  LYS G 441      38.475  80.453  76.286  1.00 63.92           C  
-ATOM  26860  NZ  LYS G 441      39.042  81.140  77.481  1.00 66.54           N  
-ATOM  26861  N   ASP G 442      34.070  84.609  73.709  1.00 33.50           N  
-ATOM  26862  CA  ASP G 442      33.210  85.646  73.155  1.00 29.22           C  
-ATOM  26863  C   ASP G 442      33.854  86.279  71.927  1.00 31.14           C  
-ATOM  26864  O   ASP G 442      34.920  85.853  71.482  1.00 31.65           O  
-ATOM  26865  CB  ASP G 442      32.882  86.718  74.204  1.00 31.55           C  
-ATOM  26866  CG  ASP G 442      34.121  87.350  74.829  1.00 34.42           C  
-ATOM  26867  OD1 ASP G 442      35.162  87.480  74.151  1.00 29.45           O  
-ATOM  26868  OD2 ASP G 442      34.044  87.735  76.016  1.00 40.48           O  
-ATOM  26869  N   MET G 443      33.205  87.305  71.391  1.00 30.24           N  
-ATOM  26870  CA  MET G 443      33.684  87.970  70.187  1.00 25.99           C  
-ATOM  26871  C   MET G 443      34.811  88.955  70.477  1.00 32.41           C  
-ATOM  26872  O   MET G 443      35.354  89.567  69.558  1.00 35.08           O  
-ATOM  26873  CB  MET G 443      32.531  88.695  69.497  1.00 25.66           C  
-ATOM  26874  CG  MET G 443      31.863  89.743  70.363  1.00 24.43           C  
-ATOM  26875  SD  MET G 443      30.365  90.380  69.595  1.00 36.47           S  
-ATOM  26876  CE  MET G 443      29.725  91.411  70.910  1.00 39.81           C  
-ATOM  26877  N   HIS G 444      35.159  89.109  71.752  1.00 37.39           N  
-ATOM  26878  CA  HIS G 444      36.204  90.049  72.145  1.00 33.49           C  
-ATOM  26879  C   HIS G 444      37.524  89.342  72.428  1.00 28.77           C  
-ATOM  26880  O   HIS G 444      38.542  89.990  72.668  1.00 25.64           O  
-ATOM  26881  CB  HIS G 444      35.771  90.849  73.376  1.00 25.62           C  
-ATOM  26882  CG  HIS G 444      34.477  91.580  73.198  1.00 33.14           C  
-ATOM  26883  ND1 HIS G 444      34.256  92.459  72.159  1.00 36.64           N  
-ATOM  26884  CD2 HIS G 444      33.337  91.567  73.928  1.00 42.14           C  
-ATOM  26885  CE1 HIS G 444      33.034  92.953  72.256  1.00 45.42           C  
-ATOM  26886  NE2 HIS G 444      32.455  92.428  73.321  1.00 37.79           N  
-ATOM  26887  N   THR G 445      37.504  88.013  72.390  1.00 33.75           N  
-ATOM  26888  CA  THR G 445      38.673  87.219  72.753  1.00 36.91           C  
-ATOM  26889  C   THR G 445      39.673  87.105  71.604  1.00 42.59           C  
-ATOM  26890  O   THR G 445      39.288  87.013  70.437  1.00 38.77           O  
-ATOM  26891  CB  THR G 445      38.270  85.799  73.198  1.00 34.79           C  
-ATOM  26892  OG1 THR G 445      37.078  85.861  73.991  1.00 42.10           O  
-ATOM  26893  CG2 THR G 445      39.385  85.154  74.008  1.00 33.58           C  
-ATOM  26894  N   ASP G 446      40.960  87.114  71.943  1.00 41.89           N  
-ATOM  26895  CA  ASP G 446      42.016  86.905  70.959  1.00 36.89           C  
-ATOM  26896  C   ASP G 446      42.237  85.409  70.781  1.00 41.60           C  
-ATOM  26897  O   ASP G 446      42.348  84.672  71.761  1.00 45.14           O  
-ATOM  26898  CB  ASP G 446      43.312  87.597  71.394  1.00 41.50           C  
-ATOM  26899  CG  ASP G 446      44.264  87.847  70.233  1.00 44.66           C  
-ATOM  26900  OD1 ASP G 446      44.195  87.109  69.227  1.00 41.21           O  
-ATOM  26901  OD2 ASP G 446      45.085  88.786  70.328  1.00 40.03           O  
-ATOM  26902  N   TYR G 447      42.297  84.959  69.532  1.00 38.68           N  
-ATOM  26903  CA  TYR G 447      42.405  83.532  69.251  1.00 34.77           C  
-ATOM  26904  C   TYR G 447      43.614  83.177  68.400  1.00 31.50           C  
-ATOM  26905  O   TYR G 447      43.695  82.065  67.877  1.00 30.16           O  
-ATOM  26906  CB  TYR G 447      41.142  83.033  68.550  1.00 30.89           C  
-ATOM  26907  CG  TYR G 447      39.887  83.148  69.375  1.00 29.24           C  
-ATOM  26908  CD1 TYR G 447      39.632  82.261  70.409  1.00 26.55           C  
-ATOM  26909  CD2 TYR G 447      38.947  84.134  69.109  1.00 40.72           C  
-ATOM  26910  CE1 TYR G 447      38.480  82.358  71.163  1.00 38.87           C  
-ATOM  26911  CE2 TYR G 447      37.791  84.239  69.857  1.00 44.67           C  
-ATOM  26912  CZ  TYR G 447      37.562  83.347  70.882  1.00 37.76           C  
-ATOM  26913  OH  TYR G 447      36.413  83.448  71.631  1.00 36.86           O  
-ATOM  26914  N   THR G 448      44.546  84.113  68.252  1.00 41.63           N  
-ATOM  26915  CA  THR G 448      45.698  83.885  67.387  1.00 46.51           C  
-ATOM  26916  C   THR G 448      46.535  82.714  67.911  1.00 35.31           C  
-ATOM  26917  O   THR G 448      46.905  82.668  69.087  1.00 30.39           O  
-ATOM  26918  CB  THR G 448      46.568  85.168  67.238  1.00 33.49           C  
-ATOM  26919  OG1 THR G 448      47.664  84.910  66.349  1.00 35.18           O  
-ATOM  26920  CG2 THR G 448      47.098  85.652  68.585  1.00 36.23           C  
-ATOM  26921  N   GLY G 449      46.788  81.747  67.035  1.00 26.67           N  
-ATOM  26922  CA  GLY G 449      47.523  80.551  67.405  1.00 26.78           C  
-ATOM  26923  C   GLY G 449      46.623  79.362  67.691  1.00 31.77           C  
-ATOM  26924  O   GLY G 449      47.007  78.210  67.479  1.00 29.83           O  
-ATOM  26925  N   GLN G 450      45.417  79.642  68.173  1.00 37.42           N  
-ATOM  26926  CA  GLN G 450      44.462  78.593  68.514  1.00 34.55           C  
-ATOM  26927  C   GLN G 450      43.748  78.039  67.279  1.00 28.92           C  
-ATOM  26928  O   GLN G 450      43.400  78.785  66.361  1.00 27.92           O  
-ATOM  26929  CB  GLN G 450      43.427  79.119  69.508  1.00 25.36           C  
-ATOM  26930  CG  GLN G 450      44.009  79.690  70.788  1.00 23.17           C  
-ATOM  26931  CD  GLN G 450      42.934  80.207  71.730  1.00 36.86           C  
-ATOM  26932  OE1 GLN G 450      43.076  81.271  72.330  1.00 40.68           O  
-ATOM  26933  NE2 GLN G 450      41.849  79.451  71.862  1.00 34.66           N  
-ATOM  26934  N   GLY G 451      43.533  76.727  67.266  1.00 22.72           N  
-ATOM  26935  CA  GLY G 451      42.757  76.088  66.219  1.00 19.58           C  
-ATOM  26936  C   GLY G 451      43.487  75.933  64.901  1.00 23.35           C  
-ATOM  26937  O   GLY G 451      44.660  76.285  64.778  1.00 26.44           O  
-ATOM  26938  N   VAL G 452      42.779  75.402  63.908  1.00 23.21           N  
-ATOM  26939  CA  VAL G 452      43.347  75.177  62.584  1.00 22.67           C  
-ATOM  26940  C   VAL G 452      43.060  76.348  61.646  1.00 27.89           C  
-ATOM  26941  O   VAL G 452      41.908  76.753  61.483  1.00 28.61           O  
-ATOM  26942  CB  VAL G 452      42.799  73.884  61.954  1.00 18.42           C  
-ATOM  26943  CG1 VAL G 452      43.343  73.704  60.546  1.00 22.61           C  
-ATOM  26944  CG2 VAL G 452      43.142  72.684  62.826  1.00 16.64           C  
-ATOM  26945  N   ASP G 453      44.112  76.888  61.034  1.00 29.35           N  
-ATOM  26946  CA  ASP G 453      43.974  77.988  60.081  1.00 21.34           C  
-ATOM  26947  C   ASP G 453      43.804  77.449  58.662  1.00 23.68           C  
-ATOM  26948  O   ASP G 453      44.750  77.423  57.865  1.00 30.58           O  
-ATOM  26949  CB  ASP G 453      45.182  78.923  60.159  1.00 27.77           C  
-ATOM  26950  CG  ASP G 453      44.919  80.276  59.522  1.00 30.95           C  
-ATOM  26951  OD1 ASP G 453      44.101  80.355  58.578  1.00 32.37           O  
-ATOM  26952  OD2 ASP G 453      45.538  81.265  59.968  1.00 24.90           O  
-ATOM  26953  N   GLN G 454      42.581  77.031  58.358  1.00 19.88           N  
-ATOM  26954  CA  GLN G 454      42.262  76.417  57.078  1.00 21.23           C  
-ATOM  26955  C   GLN G 454      42.618  77.302  55.893  1.00 22.80           C  
-ATOM  26956  O   GLN G 454      43.068  76.803  54.868  1.00 25.10           O  
-ATOM  26957  CB  GLN G 454      40.778  76.059  57.014  1.00 22.10           C  
-ATOM  26958  CG  GLN G 454      40.371  74.919  57.927  1.00 25.52           C  
-ATOM  26959  CD  GLN G 454      38.950  74.464  57.679  1.00 23.01           C  
-ATOM  26960  OE1 GLN G 454      38.709  73.542  56.896  1.00 22.03           O  
-ATOM  26961  NE2 GLN G 454      37.997  75.109  58.345  1.00 18.50           N  
-ATOM  26962  N   LEU G 455      42.415  78.609  56.028  1.00 24.59           N  
-ATOM  26963  CA  LEU G 455      42.680  79.526  54.925  1.00 25.24           C  
-ATOM  26964  C   LEU G 455      44.171  79.571  54.604  1.00 29.83           C  
-ATOM  26965  O   LEU G 455      44.571  79.502  53.436  1.00 27.45           O  
-ATOM  26966  CB  LEU G 455      42.158  80.927  55.253  1.00 23.04           C  
-ATOM  26967  CG  LEU G 455      42.062  81.889  54.067  1.00 22.41           C  
-ATOM  26968  CD1 LEU G 455      41.245  81.272  52.943  1.00 15.39           C  
-ATOM  26969  CD2 LEU G 455      41.466  83.220  54.492  1.00 17.08           C  
-ATOM  26970  N   LYS G 456      44.991  79.672  55.646  1.00 26.69           N  
-ATOM  26971  CA  LYS G 456      46.437  79.690  55.470  1.00 28.82           C  
-ATOM  26972  C   LYS G 456      46.920  78.359  54.908  1.00 38.32           C  
-ATOM  26973  O   LYS G 456      47.755  78.329  54.002  1.00 35.49           O  
-ATOM  26974  CB  LYS G 456      47.150  80.001  56.789  1.00 28.75           C  
-ATOM  26975  CG  LYS G 456      48.600  80.428  56.608  1.00 41.06           C  
-ATOM  26976  CD  LYS G 456      49.179  81.028  57.883  1.00 38.27           C  
-ATOM  26977  CE  LYS G 456      49.434  79.977  58.952  1.00 50.40           C  
-ATOM  26978  NZ  LYS G 456      49.988  80.596  60.192  1.00 37.54           N  
-ATOM  26979  N   ASN G 457      46.385  77.263  55.445  1.00 36.30           N  
-ATOM  26980  CA  ASN G 457      46.701  75.931  54.928  1.00 39.41           C  
-ATOM  26981  C   ASN G 457      46.427  75.830  53.428  1.00 32.56           C  
-ATOM  26982  O   ASN G 457      47.281  75.391  52.654  1.00 31.96           O  
-ATOM  26983  CB  ASN G 457      45.905  74.855  55.675  1.00 28.28           C  
-ATOM  26984  CG  ASN G 457      46.414  74.625  57.086  1.00 35.19           C  
-ATOM  26985  OD1 ASN G 457      47.500  75.077  57.451  1.00 41.45           O  
-ATOM  26986  ND2 ASN G 457      45.635  73.904  57.883  1.00 35.46           N  
-ATOM  26987  N   VAL G 458      45.230  76.250  53.034  1.00 26.81           N  
-ATOM  26988  CA  VAL G 458      44.807  76.234  51.640  1.00 21.39           C  
-ATOM  26989  C   VAL G 458      45.714  77.084  50.761  1.00 23.42           C  
-ATOM  26990  O   VAL G 458      46.128  76.653  49.686  1.00 27.99           O  
-ATOM  26991  CB  VAL G 458      43.359  76.734  51.495  1.00 19.34           C  
-ATOM  26992  CG1 VAL G 458      43.067  77.123  50.058  1.00 20.46           C  
-ATOM  26993  CG2 VAL G 458      42.380  75.671  51.974  1.00 21.65           C  
-ATOM  26994  N   ILE G 459      46.025  78.291  51.216  1.00 24.59           N  
-ATOM  26995  CA  ILE G 459      46.853  79.188  50.419  1.00 27.29           C  
-ATOM  26996  C   ILE G 459      48.266  78.643  50.233  1.00 30.35           C  
-ATOM  26997  O   ILE G 459      48.764  78.589  49.107  1.00 24.97           O  
-ATOM  26998  CB  ILE G 459      46.915  80.590  51.039  1.00 22.88           C  
-ATOM  26999  CG1 ILE G 459      45.545  81.258  50.931  1.00 16.06           C  
-ATOM  27000  CG2 ILE G 459      47.959  81.435  50.336  1.00 14.71           C  
-ATOM  27001  CD1 ILE G 459      45.472  82.580  51.615  1.00 20.95           C  
-ATOM  27002  N   GLN G 460      48.904  78.229  51.324  1.00 37.25           N  
-ATOM  27003  CA  GLN G 460      50.253  77.671  51.234  1.00 35.62           C  
-ATOM  27004  C   GLN G 460      50.276  76.414  50.366  1.00 26.49           C  
-ATOM  27005  O   GLN G 460      51.183  76.224  49.552  1.00 25.03           O  
-ATOM  27006  CB  GLN G 460      50.806  77.377  52.631  1.00 36.09           C  
-ATOM  27007  CG  GLN G 460      51.263  78.623  53.368  1.00 42.71           C  
-ATOM  27008  CD  GLN G 460      51.685  78.334  54.797  1.00 78.46           C  
-ATOM  27009  OE1 GLN G 460      51.646  77.189  55.253  1.00 81.73           O  
-ATOM  27010  NE2 GLN G 460      52.089  79.377  55.514  1.00 70.78           N  
-ATOM  27011  N   MET G 461      49.262  75.573  50.532  1.00 24.28           N  
-ATOM  27012  CA  MET G 461      49.121  74.374  49.716  1.00 27.02           C  
-ATOM  27013  C   MET G 461      48.968  74.735  48.242  1.00 27.92           C  
-ATOM  27014  O   MET G 461      49.419  74.000  47.365  1.00 35.80           O  
-ATOM  27015  CB  MET G 461      47.922  73.541  50.182  1.00 35.43           C  
-ATOM  27016  CG  MET G 461      47.803  72.179  49.511  1.00 40.07           C  
-ATOM  27017  SD  MET G 461      49.178  71.088  49.916  1.00 44.29           S  
-ATOM  27018  CE  MET G 461      48.982  70.951  51.693  1.00 38.57           C  
-ATOM  27019  N   LEU G 462      48.332  75.870  47.973  1.00 29.98           N  
-ATOM  27020  CA  LEU G 462      48.151  76.341  46.604  1.00 24.71           C  
-ATOM  27021  C   LEU G 462      49.452  76.875  46.015  1.00 28.47           C  
-ATOM  27022  O   LEU G 462      49.720  76.711  44.826  1.00 32.34           O  
-ATOM  27023  CB  LEU G 462      47.072  77.425  46.552  1.00 21.51           C  
-ATOM  27024  CG  LEU G 462      45.618  76.959  46.463  1.00 18.04           C  
-ATOM  27025  CD1 LEU G 462      44.681  78.056  46.917  1.00 15.10           C  
-ATOM  27026  CD2 LEU G 462      45.293  76.548  45.047  1.00 17.95           C  
-ATOM  27027  N   ARG G 463      50.257  77.515  46.856  1.00 33.03           N  
-ATOM  27028  CA  ARG G 463      51.495  78.136  46.404  1.00 25.81           C  
-ATOM  27029  C   ARG G 463      52.637  77.131  46.273  1.00 30.94           C  
-ATOM  27030  O   ARG G 463      53.595  77.368  45.538  1.00 31.98           O  
-ATOM  27031  CB  ARG G 463      51.899  79.262  47.358  1.00 24.88           C  
-ATOM  27032  CG  ARG G 463      50.844  80.351  47.486  1.00 31.64           C  
-ATOM  27033  CD  ARG G 463      51.440  81.697  47.869  1.00 22.72           C  
-ATOM  27034  NE  ARG G 463      51.571  81.872  49.313  1.00 15.11           N  
-ATOM  27035  CZ  ARG G 463      51.369  83.028  49.937  1.00 17.26           C  
-ATOM  27036  NH1 ARG G 463      51.019  84.102  49.243  1.00 16.68           N  
-ATOM  27037  NH2 ARG G 463      51.512  83.113  51.252  1.00 21.16           N  
-ATOM  27038  N   THR G 464      52.530  76.004  46.972  1.00 31.16           N  
-ATOM  27039  CA  THR G 464      53.622  75.037  46.996  1.00 24.10           C  
-ATOM  27040  C   THR G 464      53.297  73.717  46.297  1.00 29.39           C  
-ATOM  27041  O   THR G 464      54.192  73.058  45.768  1.00 34.41           O  
-ATOM  27042  CB  THR G 464      54.047  74.733  48.440  1.00 24.69           C  
-ATOM  27043  OG1 THR G 464      53.031  73.961  49.091  1.00 38.79           O  
-ATOM  27044  CG2 THR G 464      54.270  76.027  49.206  1.00 25.17           C  
-ATOM  27045  N   ASN G 465      52.027  73.326  46.298  1.00 32.60           N  
-ATOM  27046  CA  ASN G 465      51.637  72.034  45.740  1.00 32.58           C  
-ATOM  27047  C   ASN G 465      50.242  72.071  45.121  1.00 34.17           C  
-ATOM  27048  O   ASN G 465      49.301  71.508  45.677  1.00 38.14           O  
-ATOM  27049  CB  ASN G 465      51.701  70.960  46.828  1.00 35.29           C  
-ATOM  27050  CG  ASN G 465      51.777  69.557  46.262  1.00 43.35           C  
-ATOM  27051  OD1 ASN G 465      51.390  69.313  45.120  1.00 36.78           O  
-ATOM  27052  ND2 ASN G 465      52.280  68.624  47.063  1.00 43.22           N  
-ATOM  27053  N   PRO G 466      50.111  72.716  43.951  1.00 33.76           N  
-ATOM  27054  CA  PRO G 466      48.806  73.018  43.346  1.00 31.31           C  
-ATOM  27055  C   PRO G 466      48.010  71.805  42.851  1.00 30.13           C  
-ATOM  27056  O   PRO G 466      46.881  71.983  42.395  1.00 39.92           O  
-ATOM  27057  CB  PRO G 466      49.177  73.923  42.165  1.00 37.02           C  
-ATOM  27058  CG  PRO G 466      50.565  73.522  41.808  1.00 44.87           C  
-ATOM  27059  CD  PRO G 466      51.229  73.188  43.114  1.00 38.80           C  
-ATOM  27060  N   THR G 467      48.570  70.604  42.940  1.00 30.82           N  
-ATOM  27061  CA  THR G 467      47.870  69.414  42.467  1.00 31.75           C  
-ATOM  27062  C   THR G 467      47.342  68.583  43.632  1.00 30.32           C  
-ATOM  27063  O   THR G 467      46.833  67.476  43.444  1.00 25.55           O  
-ATOM  27064  CB  THR G 467      48.776  68.536  41.584  1.00 36.27           C  
-ATOM  27065  OG1 THR G 467      50.024  68.305  42.251  1.00 33.73           O  
-ATOM  27066  CG2 THR G 467      49.039  69.223  40.256  1.00 32.45           C  
-ATOM  27067  N   ASP G 468      47.468  69.128  44.836  1.00 26.81           N  
-ATOM  27068  CA  ASP G 468      46.958  68.472  46.031  1.00 27.24           C  
-ATOM  27069  C   ASP G 468      45.436  68.443  45.983  1.00 29.60           C  
-ATOM  27070  O   ASP G 468      44.808  69.409  45.552  1.00 39.32           O  
-ATOM  27071  CB  ASP G 468      47.450  69.192  47.286  1.00 29.37           C  
-ATOM  27072  CG  ASP G 468      46.931  68.566  48.559  1.00 30.88           C  
-ATOM  27073  OD1 ASP G 468      47.562  67.609  49.054  1.00 34.35           O  
-ATOM  27074  OD2 ASP G 468      45.895  69.036  49.071  1.00 34.63           O  
-ATOM  27075  N   ARG G 469      44.841  67.335  46.411  1.00 32.59           N  
-ATOM  27076  CA  ARG G 469      43.388  67.196  46.354  1.00 29.29           C  
-ATOM  27077  C   ARG G 469      42.741  67.303  47.734  1.00 26.45           C  
-ATOM  27078  O   ARG G 469      41.671  66.744  47.965  1.00 27.11           O  
-ATOM  27079  CB  ARG G 469      42.997  65.866  45.702  1.00 23.94           C  
-ATOM  27080  CG  ARG G 469      43.620  65.615  44.332  1.00 29.67           C  
-ATOM  27081  CD  ARG G 469      42.918  64.457  43.633  1.00 29.55           C  
-ATOM  27082  NE  ARG G 469      43.832  63.545  42.947  1.00 35.75           N  
-ATOM  27083  CZ  ARG G 469      44.499  62.564  43.550  1.00 38.60           C  
-ATOM  27084  NH1 ARG G 469      44.368  62.379  44.854  1.00 31.07           N  
-ATOM  27085  NH2 ARG G 469      45.304  61.772  42.855  1.00 38.76           N  
-ATOM  27086  N   ARG G 470      43.390  68.019  48.648  1.00 25.84           N  
-ATOM  27087  CA  ARG G 470      42.851  68.207  49.993  1.00 23.93           C  
-ATOM  27088  C   ARG G 470      42.777  69.685  50.366  1.00 30.12           C  
-ATOM  27089  O   ARG G 470      42.831  70.042  51.545  1.00 22.79           O  
-ATOM  27090  CB  ARG G 470      43.692  67.457  51.030  1.00 25.63           C  
-ATOM  27091  CG  ARG G 470      43.641  65.940  50.928  1.00 23.60           C  
-ATOM  27092  CD  ARG G 470      44.681  65.408  49.955  1.00 32.85           C  
-ATOM  27093  NE  ARG G 470      44.972  63.997  50.186  1.00 32.70           N  
-ATOM  27094  CZ  ARG G 470      45.935  63.558  50.990  1.00 35.39           C  
-ATOM  27095  NH1 ARG G 470      46.703  64.423  51.642  1.00 22.86           N  
-ATOM  27096  NH2 ARG G 470      46.133  62.256  51.142  1.00 30.10           N  
-ATOM  27097  N   MET G 471      42.656  70.541  49.356  1.00 32.06           N  
-ATOM  27098  CA  MET G 471      42.553  71.979  49.580  1.00 34.50           C  
-ATOM  27099  C   MET G 471      41.118  72.382  49.892  1.00 26.89           C  
-ATOM  27100  O   MET G 471      40.389  72.852  49.016  1.00 23.35           O  
-ATOM  27101  CB  MET G 471      43.050  72.752  48.362  1.00 30.74           C  
-ATOM  27102  CG  MET G 471      44.371  72.269  47.810  1.00 28.16           C  
-ATOM  27103  SD  MET G 471      44.885  73.275  46.411  1.00 36.38           S  
-ATOM  27104  CE  MET G 471      46.246  72.307  45.782  1.00 37.21           C  
-ATOM  27105  N   LEU G 472      40.710  72.200  51.140  1.00 19.47           N  
-ATOM  27106  CA  LEU G 472      39.342  72.508  51.516  1.00 21.48           C  
-ATOM  27107  C   LEU G 472      39.263  73.400  52.745  1.00 25.32           C  
-ATOM  27108  O   LEU G 472      40.143  73.391  53.606  1.00 21.50           O  
-ATOM  27109  CB  LEU G 472      38.551  71.221  51.759  1.00 24.82           C  
-ATOM  27110  CG  LEU G 472      38.121  70.448  50.511  1.00 21.64           C  
-ATOM  27111  CD1 LEU G 472      39.199  69.471  50.056  1.00 30.31           C  
-ATOM  27112  CD2 LEU G 472      36.808  69.732  50.765  1.00 24.60           C  
-ATOM  27113  N   MET G 473      38.189  74.176  52.805  1.00 26.88           N  
-ATOM  27114  CA  MET G 473      37.897  75.014  53.950  1.00 23.38           C  
-ATOM  27115  C   MET G 473      36.462  74.739  54.373  1.00 22.57           C  
-ATOM  27116  O   MET G 473      35.528  74.973  53.607  1.00 29.33           O  
-ATOM  27117  CB  MET G 473      38.109  76.490  53.606  1.00 18.60           C  
-ATOM  27118  CG  MET G 473      38.189  77.410  54.810  1.00 25.32           C  
-ATOM  27119  SD  MET G 473      38.872  79.024  54.381  1.00 36.89           S  
-ATOM  27120  CE  MET G 473      37.746  79.534  53.084  1.00 24.89           C  
-ATOM  27121  N   THR G 474      36.288  74.213  55.580  1.00 17.85           N  
-ATOM  27122  CA  THR G 474      34.951  73.897  56.065  1.00 20.65           C  
-ATOM  27123  C   THR G 474      34.612  74.710  57.308  1.00 24.91           C  
-ATOM  27124  O   THR G 474      35.486  75.035  58.113  1.00 27.86           O  
-ATOM  27125  CB  THR G 474      34.794  72.393  56.377  1.00 18.73           C  
-ATOM  27126  OG1 THR G 474      33.451  72.127  56.803  1.00 18.88           O  
-ATOM  27127  CG2 THR G 474      35.765  71.957  57.465  1.00 17.65           C  
-ATOM  27128  N   ALA G 475      33.335  75.049  57.447  1.00 24.75           N  
-ATOM  27129  CA  ALA G 475      32.858  75.789  58.607  1.00 25.51           C  
-ATOM  27130  C   ALA G 475      31.858  74.948  59.385  1.00 22.59           C  
-ATOM  27131  O   ALA G 475      31.383  75.350  60.445  1.00 30.46           O  
-ATOM  27132  CB  ALA G 475      32.234  77.105  58.178  1.00 27.18           C  
-ATOM  27133  N   TRP G 476      31.541  73.777  58.846  1.00 22.79           N  
-ATOM  27134  CA  TRP G 476      30.585  72.881  59.478  1.00 23.40           C  
-ATOM  27135  C   TRP G 476      31.268  72.049  60.557  1.00 32.87           C  
-ATOM  27136  O   TRP G 476      31.844  70.998  60.276  1.00 37.25           O  
-ATOM  27137  CB  TRP G 476      29.931  71.975  58.434  1.00 21.71           C  
-ATOM  27138  CG  TRP G 476      28.746  71.221  58.951  1.00 20.94           C  
-ATOM  27139  CD1 TRP G 476      28.717  69.921  59.363  1.00 24.95           C  
-ATOM  27140  CD2 TRP G 476      27.415  71.723  59.114  1.00 20.21           C  
-ATOM  27141  NE1 TRP G 476      27.451  69.581  59.771  1.00 26.81           N  
-ATOM  27142  CE2 TRP G 476      26.632  70.671  59.628  1.00 25.51           C  
-ATOM  27143  CE3 TRP G 476      26.809  72.959  58.875  1.00 22.74           C  
-ATOM  27144  CZ2 TRP G 476      25.275  70.817  59.908  1.00 28.70           C  
-ATOM  27145  CZ3 TRP G 476      25.462  73.104  59.154  1.00 24.25           C  
-ATOM  27146  CH2 TRP G 476      24.709  72.039  59.665  1.00 28.98           C  
-ATOM  27147  N   ASN G 477      31.203  72.537  61.791  1.00 27.83           N  
-ATOM  27148  CA  ASN G 477      31.797  71.850  62.928  1.00 26.06           C  
-ATOM  27149  C   ASN G 477      30.721  71.455  63.934  1.00 30.69           C  
-ATOM  27150  O   ASN G 477      30.367  72.246  64.811  1.00 31.00           O  
-ATOM  27151  CB  ASN G 477      32.860  72.735  63.588  1.00 32.73           C  
-ATOM  27152  CG  ASN G 477      33.459  72.109  64.836  1.00 37.92           C  
-ATOM  27153  OD1 ASN G 477      33.419  70.893  65.021  1.00 35.77           O  
-ATOM  27154  ND2 ASN G 477      34.021  72.945  65.703  1.00 34.46           N  
-ATOM  27155  N   PRO G 478      30.198  70.224  63.805  1.00 29.74           N  
-ATOM  27156  CA  PRO G 478      29.111  69.660  64.618  1.00 24.03           C  
-ATOM  27157  C   PRO G 478      29.279  69.864  66.123  1.00 29.05           C  
-ATOM  27158  O   PRO G 478      28.285  69.880  66.849  1.00 38.66           O  
-ATOM  27159  CB  PRO G 478      29.162  68.173  64.267  1.00 21.04           C  
-ATOM  27160  CG  PRO G 478      29.650  68.154  62.870  1.00 25.21           C  
-ATOM  27161  CD  PRO G 478      30.650  69.274  62.772  1.00 27.88           C  
-ATOM  27162  N   ALA G 479      30.517  70.020  66.581  1.00 30.99           N  
-ATOM  27163  CA  ALA G 479      30.786  70.223  67.998  1.00 32.54           C  
-ATOM  27164  C   ALA G 479      30.320  71.598  68.471  1.00 37.44           C  
-ATOM  27165  O   ALA G 479      29.834  71.745  69.594  1.00 36.90           O  
-ATOM  27166  CB  ALA G 479      32.269  70.045  68.281  1.00 30.19           C  
-ATOM  27167  N   ALA G 480      30.463  72.598  67.607  1.00 31.82           N  
-ATOM  27168  CA  ALA G 480      30.204  73.980  67.992  1.00 37.38           C  
-ATOM  27169  C   ALA G 480      28.942  74.558  67.354  1.00 36.43           C  
-ATOM  27170  O   ALA G 480      28.722  75.768  67.398  1.00 31.31           O  
-ATOM  27171  CB  ALA G 480      31.406  74.845  67.641  1.00 31.73           C  
-ATOM  27172  N   LEU G 481      28.114  73.697  66.771  1.00 32.64           N  
-ATOM  27173  CA  LEU G 481      26.917  74.151  66.069  1.00 27.03           C  
-ATOM  27174  C   LEU G 481      25.902  74.807  66.998  1.00 33.34           C  
-ATOM  27175  O   LEU G 481      25.292  75.814  66.643  1.00 32.10           O  
-ATOM  27176  CB  LEU G 481      26.258  72.987  65.330  1.00 24.54           C  
-ATOM  27177  CG  LEU G 481      26.944  72.544  64.037  1.00 24.50           C  
-ATOM  27178  CD1 LEU G 481      26.103  71.501  63.318  1.00 22.88           C  
-ATOM  27179  CD2 LEU G 481      27.217  73.738  63.137  1.00 27.11           C  
-ATOM  27180  N   ASP G 482      25.723  74.240  68.186  1.00 40.48           N  
-ATOM  27181  CA  ASP G 482      24.753  74.774  69.137  1.00 41.32           C  
-ATOM  27182  C   ASP G 482      25.223  76.094  69.741  1.00 30.64           C  
-ATOM  27183  O   ASP G 482      24.435  76.828  70.334  1.00 29.19           O  
-ATOM  27184  CB  ASP G 482      24.470  73.757  70.245  1.00 37.00           C  
-ATOM  27185  CG  ASP G 482      23.736  72.529  69.736  1.00 43.82           C  
-ATOM  27186  OD1 ASP G 482      23.136  72.602  68.640  1.00 31.92           O  
-ATOM  27187  OD2 ASP G 482      23.754  71.493  70.436  1.00 40.00           O  
-ATOM  27188  N   GLU G 483      26.507  76.393  69.579  1.00 31.21           N  
-ATOM  27189  CA  GLU G 483      27.079  77.622  70.116  1.00 34.12           C  
-ATOM  27190  C   GLU G 483      27.011  78.762  69.106  1.00 34.12           C  
-ATOM  27191  O   GLU G 483      27.259  79.919  69.449  1.00 33.57           O  
-ATOM  27192  CB  GLU G 483      28.527  77.394  70.541  1.00 39.24           C  
-ATOM  27193  CG  GLU G 483      28.711  76.217  71.479  1.00 44.27           C  
-ATOM  27194  CD  GLU G 483      30.170  75.906  71.734  1.00 48.62           C  
-ATOM  27195  OE1 GLU G 483      30.965  76.859  71.886  1.00 41.57           O  
-ATOM  27196  OE2 GLU G 483      30.524  74.708  71.775  1.00 49.63           O  
-ATOM  27197  N   MET G 484      26.679  78.433  67.861  1.00 37.25           N  
-ATOM  27198  CA  MET G 484      26.562  79.440  66.812  1.00 32.10           C  
-ATOM  27199  C   MET G 484      25.173  80.066  66.808  1.00 28.32           C  
-ATOM  27200  O   MET G 484      24.195  79.435  67.207  1.00 31.70           O  
-ATOM  27201  CB  MET G 484      26.852  78.836  65.437  1.00 36.09           C  
-ATOM  27202  CG  MET G 484      28.203  78.160  65.302  1.00 36.21           C  
-ATOM  27203  SD  MET G 484      28.481  77.618  63.604  1.00 42.76           S  
-ATOM  27204  CE  MET G 484      29.808  76.439  63.826  1.00 33.54           C  
-ATOM  27205  N   ALA G 485      25.092  81.309  66.350  1.00 30.36           N  
-ATOM  27206  CA  ALA G 485      23.812  81.990  66.230  1.00 36.63           C  
-ATOM  27207  C   ALA G 485      22.998  81.358  65.111  1.00 34.84           C  
-ATOM  27208  O   ALA G 485      21.772  81.271  65.185  1.00 39.20           O  
-ATOM  27209  CB  ALA G 485      24.016  83.474  65.973  1.00 35.77           C  
-ATOM  27210  N   LEU G 486      23.697  80.911  64.075  1.00 28.24           N  
-ATOM  27211  CA  LEU G 486      23.057  80.259  62.944  1.00 33.18           C  
-ATOM  27212  C   LEU G 486      24.066  79.351  62.248  1.00 33.30           C  
-ATOM  27213  O   LEU G 486      25.129  79.811  61.827  1.00 29.00           O  
-ATOM  27214  CB  LEU G 486      22.494  81.300  61.970  1.00 34.27           C  
-ATOM  27215  CG  LEU G 486      21.212  80.955  61.203  1.00 42.53           C  
-ATOM  27216  CD1 LEU G 486      20.559  82.220  60.670  1.00 54.05           C  
-ATOM  27217  CD2 LEU G 486      21.481  79.980  60.065  1.00 48.07           C  
-ATOM  27218  N   PRO G 487      23.739  78.055  62.138  1.00 29.59           N  
-ATOM  27219  CA  PRO G 487      24.606  77.081  61.467  1.00 32.70           C  
-ATOM  27220  C   PRO G 487      24.956  77.537  60.055  1.00 30.09           C  
-ATOM  27221  O   PRO G 487      24.102  78.092  59.367  1.00 37.89           O  
-ATOM  27222  CB  PRO G 487      23.755  75.809  61.443  1.00 35.95           C  
-ATOM  27223  CG  PRO G 487      22.796  75.976  62.572  1.00 25.67           C  
-ATOM  27224  CD  PRO G 487      22.494  77.440  62.629  1.00 28.57           C  
-ATOM  27225  N   PRO G 488      26.208  77.315  59.633  1.00 25.34           N  
-ATOM  27226  CA  PRO G 488      26.688  77.822  58.344  1.00 32.93           C  
-ATOM  27227  C   PRO G 488      25.915  77.269  57.150  1.00 29.89           C  
-ATOM  27228  O   PRO G 488      25.720  76.059  57.038  1.00 31.29           O  
-ATOM  27229  CB  PRO G 488      28.150  77.359  58.307  1.00 26.54           C  
-ATOM  27230  CG  PRO G 488      28.214  76.217  59.260  1.00 26.62           C  
-ATOM  27231  CD  PRO G 488      27.249  76.562  60.349  1.00 24.59           C  
-ATOM  27232  N   CYS G 489      25.472  78.162  56.273  1.00 26.17           N  
-ATOM  27233  CA  CYS G 489      24.800  77.750  55.052  1.00 30.68           C  
-ATOM  27234  C   CYS G 489      25.856  77.431  53.994  1.00 31.55           C  
-ATOM  27235  O   CYS G 489      25.923  76.305  53.500  1.00 29.43           O  
-ATOM  27236  CB  CYS G 489      23.826  78.831  54.571  1.00 36.17           C  
-ATOM  27237  SG  CYS G 489      22.353  79.048  55.617  1.00 59.77           S  
-ATOM  27238  N   HIS G 490      26.689  78.411  53.658  1.00 30.28           N  
-ATOM  27239  CA  HIS G 490      27.865  78.141  52.838  1.00 26.81           C  
-ATOM  27240  C   HIS G 490      28.935  77.536  53.737  1.00 25.59           C  
-ATOM  27241  O   HIS G 490      29.703  78.255  54.373  1.00 33.21           O  
-ATOM  27242  CB  HIS G 490      28.369  79.410  52.137  1.00 33.76           C  
-ATOM  27243  CG  HIS G 490      28.466  80.611  53.027  1.00 35.38           C  
-ATOM  27244  ND1 HIS G 490      29.671  81.177  53.385  1.00 36.35           N  
-ATOM  27245  CD2 HIS G 490      27.507  81.367  53.614  1.00 40.38           C  
-ATOM  27246  CE1 HIS G 490      29.451  82.224  54.161  1.00 32.63           C  
-ATOM  27247  NE2 HIS G 490      28.146  82.359  54.317  1.00 38.68           N  
-ATOM  27248  N   LEU G 491      28.975  76.208  53.789  1.00 19.69           N  
-ATOM  27249  CA  LEU G 491      29.715  75.509  54.836  1.00 25.18           C  
-ATOM  27250  C   LEU G 491      31.061  74.930  54.404  1.00 24.63           C  
-ATOM  27251  O   LEU G 491      31.889  74.588  55.248  1.00 21.14           O  
-ATOM  27252  CB  LEU G 491      28.847  74.385  55.408  1.00 25.13           C  
-ATOM  27253  CG  LEU G 491      28.244  73.410  54.393  1.00 23.99           C  
-ATOM  27254  CD1 LEU G 491      29.150  72.219  54.125  1.00 22.06           C  
-ATOM  27255  CD2 LEU G 491      26.891  72.938  54.868  1.00 24.18           C  
-ATOM  27256  N   LEU G 492      31.275  74.809  53.099  1.00 24.70           N  
-ATOM  27257  CA  LEU G 492      32.472  74.148  52.593  1.00 17.88           C  
-ATOM  27258  C   LEU G 492      32.889  74.664  51.223  1.00 20.25           C  
-ATOM  27259  O   LEU G 492      32.048  74.892  50.357  1.00 17.57           O  
-ATOM  27260  CB  LEU G 492      32.241  72.639  52.526  1.00 17.72           C  
-ATOM  27261  CG  LEU G 492      33.316  71.781  51.866  1.00 21.22           C  
-ATOM  27262  CD1 LEU G 492      33.676  70.624  52.777  1.00 21.75           C  
-ATOM  27263  CD2 LEU G 492      32.844  71.269  50.509  1.00 18.84           C  
-ATOM  27264  N   CYS G 493      34.190  74.847  51.024  1.00 20.86           N  
-ATOM  27265  CA  CYS G 493      34.686  75.214  49.704  1.00 20.58           C  
-ATOM  27266  C   CYS G 493      35.995  74.506  49.378  1.00 24.16           C  
-ATOM  27267  O   CYS G 493      36.803  74.232  50.263  1.00 26.68           O  
-ATOM  27268  CB  CYS G 493      34.857  76.733  49.589  1.00 20.73           C  
-ATOM  27269  SG  CYS G 493      36.235  77.428  50.515  1.00 28.74           S  
-ATOM  27270  N   GLN G 494      36.186  74.205  48.097  1.00 27.70           N  
-ATOM  27271  CA  GLN G 494      37.371  73.489  47.634  1.00 29.23           C  
-ATOM  27272  C   GLN G 494      37.983  74.192  46.422  1.00 26.50           C  
-ATOM  27273  O   GLN G 494      37.266  74.764  45.599  1.00 19.62           O  
-ATOM  27274  CB  GLN G 494      37.016  72.038  47.293  1.00 18.59           C  
-ATOM  27275  CG  GLN G 494      38.193  71.181  46.870  1.00 23.04           C  
-ATOM  27276  CD  GLN G 494      37.763  69.822  46.363  1.00 19.89           C  
-ATOM  27277  OE1 GLN G 494      36.571  69.541  46.252  1.00 24.06           O  
-ATOM  27278  NE2 GLN G 494      38.732  68.969  46.049  1.00 14.51           N  
-ATOM  27279  N   PHE G 495      39.310  74.151  46.320  1.00 27.06           N  
-ATOM  27280  CA  PHE G 495      40.017  74.821  45.230  1.00 26.95           C  
-ATOM  27281  C   PHE G 495      40.695  73.839  44.276  1.00 25.79           C  
-ATOM  27282  O   PHE G 495      40.864  72.659  44.595  1.00 21.17           O  
-ATOM  27283  CB  PHE G 495      41.045  75.803  45.795  1.00 18.35           C  
-ATOM  27284  CG  PHE G 495      40.429  76.963  46.524  1.00 23.77           C  
-ATOM  27285  CD1 PHE G 495      39.947  78.059  45.826  1.00 20.93           C  
-ATOM  27286  CD2 PHE G 495      40.323  76.956  47.904  1.00 21.60           C  
-ATOM  27287  CE1 PHE G 495      39.377  79.128  46.492  1.00 17.86           C  
-ATOM  27288  CE2 PHE G 495      39.755  78.022  48.576  1.00 19.49           C  
-ATOM  27289  CZ  PHE G 495      39.281  79.109  47.868  1.00 19.50           C  
-ATOM  27290  N   TYR G 496      41.087  74.341  43.108  1.00 22.53           N  
-ATOM  27291  CA  TYR G 496      41.617  73.496  42.043  1.00 19.94           C  
-ATOM  27292  C   TYR G 496      42.491  74.290  41.076  1.00 21.22           C  
-ATOM  27293  O   TYR G 496      42.161  75.415  40.711  1.00 23.39           O  
-ATOM  27294  CB  TYR G 496      40.458  72.832  41.300  1.00 16.63           C  
-ATOM  27295  CG  TYR G 496      40.818  72.045  40.059  1.00 21.45           C  
-ATOM  27296  CD1 TYR G 496      40.842  72.654  38.809  1.00 22.91           C  
-ATOM  27297  CD2 TYR G 496      41.098  70.687  40.131  1.00 22.30           C  
-ATOM  27298  CE1 TYR G 496      41.157  71.941  37.672  1.00 21.52           C  
-ATOM  27299  CE2 TYR G 496      41.414  69.963  38.996  1.00 25.11           C  
-ATOM  27300  CZ  TYR G 496      41.441  70.597  37.770  1.00 27.74           C  
-ATOM  27301  OH  TYR G 496      41.752  69.887  36.634  1.00 39.29           O  
-ATOM  27302  N   VAL G 497      43.611  73.698  40.674  1.00 24.80           N  
-ATOM  27303  CA  VAL G 497      44.530  74.333  39.733  1.00 25.51           C  
-ATOM  27304  C   VAL G 497      44.874  73.380  38.590  1.00 34.26           C  
-ATOM  27305  O   VAL G 497      45.147  72.200  38.817  1.00 36.53           O  
-ATOM  27306  CB  VAL G 497      45.832  74.785  40.426  1.00 27.62           C  
-ATOM  27307  CG1 VAL G 497      46.758  75.467  39.431  1.00 36.52           C  
-ATOM  27308  CG2 VAL G 497      45.523  75.716  41.579  1.00 22.47           C  
-ATOM  27309  N   ASN G 498      44.865  73.893  37.363  1.00 29.86           N  
-ATOM  27310  CA  ASN G 498      45.099  73.055  36.193  1.00 34.03           C  
-ATOM  27311  C   ASN G 498      46.418  73.335  35.481  1.00 37.03           C  
-ATOM  27312  O   ASN G 498      47.369  73.840  36.077  1.00 31.79           O  
-ATOM  27313  CB  ASN G 498      43.946  73.208  35.196  1.00 32.73           C  
-ATOM  27314  CG  ASN G 498      43.782  74.637  34.700  1.00 26.21           C  
-ATOM  27315  OD1 ASN G 498      44.573  75.520  35.026  1.00 23.78           O  
-ATOM  27316  ND2 ASN G 498      42.749  74.865  33.898  1.00 30.76           N  
-ATOM  27317  N   ASP G 499      46.448  72.996  34.195  1.00 35.26           N  
-ATOM  27318  CA  ASP G 499      47.615  73.194  33.345  1.00 31.84           C  
-ATOM  27319  C   ASP G 499      48.147  74.619  33.389  1.00 41.85           C  
-ATOM  27320  O   ASP G 499      49.325  74.847  33.658  1.00 40.26           O  
-ATOM  27321  CB  ASP G 499      47.278  72.831  31.895  1.00 36.36           C  
-ATOM  27322  CG  ASP G 499      47.489  71.363  31.598  1.00 63.24           C  
-ATOM  27323  OD1 ASP G 499      48.168  70.693  32.405  1.00 74.44           O  
-ATOM  27324  OD2 ASP G 499      46.989  70.882  30.557  1.00 65.58           O  
-ATOM  27325  N   GLN G 500      47.260  75.574  33.137  1.00 38.41           N  
-ATOM  27326  CA  GLN G 500      47.661  76.946  32.866  1.00 33.25           C  
-ATOM  27327  C   GLN G 500      47.626  77.845  34.100  1.00 26.71           C  
-ATOM  27328  O   GLN G 500      47.371  79.046  33.988  1.00 26.47           O  
-ATOM  27329  CB  GLN G 500      46.762  77.528  31.775  1.00 39.46           C  
-ATOM  27330  CG  GLN G 500      46.257  76.497  30.767  1.00 34.76           C  
-ATOM  27331  CD  GLN G 500      47.268  76.182  29.679  1.00 43.59           C  
-ATOM  27332  OE1 GLN G 500      47.098  76.586  28.528  1.00 53.97           O  
-ATOM  27333  NE2 GLN G 500      48.322  75.454  30.034  1.00 42.50           N  
-ATOM  27334  N   LYS G 501      47.893  77.264  35.268  1.00 23.73           N  
-ATOM  27335  CA  LYS G 501      47.899  78.011  36.524  1.00 21.89           C  
-ATOM  27336  C   LYS G 501      46.598  78.778  36.727  1.00 24.13           C  
-ATOM  27337  O   LYS G 501      46.611  79.959  37.075  1.00 28.08           O  
-ATOM  27338  CB  LYS G 501      49.088  78.975  36.571  1.00 28.85           C  
-ATOM  27339  CG  LYS G 501      50.430  78.309  36.830  1.00 28.97           C  
-ATOM  27340  CD  LYS G 501      51.580  79.178  36.332  1.00 38.00           C  
-ATOM  27341  CE  LYS G 501      51.609  80.538  37.016  1.00 43.83           C  
-ATOM  27342  NZ  LYS G 501      51.990  80.440  38.453  1.00 39.81           N  
-ATOM  27343  N   GLU G 502      45.478  78.102  36.500  1.00 31.98           N  
-ATOM  27344  CA  GLU G 502      44.166  78.722  36.641  1.00 27.09           C  
-ATOM  27345  C   GLU G 502      43.418  78.137  37.835  1.00 25.65           C  
-ATOM  27346  O   GLU G 502      43.381  76.921  38.022  1.00 31.92           O  
-ATOM  27347  CB  GLU G 502      43.353  78.545  35.361  1.00 18.80           C  
-ATOM  27348  CG  GLU G 502      44.157  78.792  34.099  1.00 22.49           C  
-ATOM  27349  CD  GLU G 502      43.296  78.806  32.857  1.00 36.71           C  
-ATOM  27350  OE1 GLU G 502      42.952  79.912  32.389  1.00 57.26           O  
-ATOM  27351  OE2 GLU G 502      42.964  77.714  32.347  1.00 31.72           O  
-ATOM  27352  N   LEU G 503      42.824  79.007  38.644  1.00 25.19           N  
-ATOM  27353  CA  LEU G 503      42.168  78.575  39.872  1.00 21.61           C  
-ATOM  27354  C   LEU G 503      40.653  78.494  39.728  1.00 27.73           C  
-ATOM  27355  O   LEU G 503      40.006  79.452  39.305  1.00 35.77           O  
-ATOM  27356  CB  LEU G 503      42.523  79.517  41.020  1.00 20.82           C  
-ATOM  27357  CG  LEU G 503      41.864  79.199  42.361  1.00 16.32           C  
-ATOM  27358  CD1 LEU G 503      42.460  77.935  42.962  1.00 21.75           C  
-ATOM  27359  CD2 LEU G 503      41.998  80.375  43.313  1.00 13.54           C  
-ATOM  27360  N   SER G 504      40.098  77.340  40.084  1.00 21.72           N  
-ATOM  27361  CA  SER G 504      38.653  77.160  40.135  1.00 19.05           C  
-ATOM  27362  C   SER G 504      38.226  76.803  41.554  1.00 22.05           C  
-ATOM  27363  O   SER G 504      38.997  76.213  42.315  1.00 21.65           O  
-ATOM  27364  CB  SER G 504      38.201  76.082  39.148  1.00 29.67           C  
-ATOM  27365  OG  SER G 504      38.371  76.512  37.806  1.00 37.29           O  
-ATOM  27366  N   CYS G 505      36.997  77.164  41.906  1.00 23.83           N  
-ATOM  27367  CA  CYS G 505      36.515  76.996  43.270  1.00 19.29           C  
-ATOM  27368  C   CYS G 505      35.083  76.475  43.317  1.00 18.04           C  
-ATOM  27369  O   CYS G 505      34.216  76.946  42.584  1.00 16.20           O  
-ATOM  27370  CB  CYS G 505      36.615  78.323  44.025  1.00 20.42           C  
-ATOM  27371  SG  CYS G 505      35.772  78.343  45.619  1.00 27.49           S  
-ATOM  27372  N   ILE G 506      34.850  75.493  44.185  1.00 18.49           N  
-ATOM  27373  CA  ILE G 506      33.514  74.956  44.423  1.00 14.60           C  
-ATOM  27374  C   ILE G 506      33.052  75.318  45.826  1.00 18.01           C  
-ATOM  27375  O   ILE G 506      33.819  75.202  46.776  1.00 16.73           O  
-ATOM  27376  CB  ILE G 506      33.468  73.422  44.271  1.00 12.83           C  
-ATOM  27377  CG1 ILE G 506      33.790  73.005  42.840  1.00 17.65           C  
-ATOM  27378  CG2 ILE G 506      32.103  72.884  44.665  1.00 16.01           C  
-ATOM  27379  CD1 ILE G 506      33.869  71.507  42.658  1.00 21.96           C  
-ATOM  27380  N   MET G 507      31.806  75.759  45.962  1.00 16.70           N  
-ATOM  27381  CA  MET G 507      31.236  75.982  47.282  1.00 14.14           C  
-ATOM  27382  C   MET G 507      29.943  75.196  47.445  1.00 17.59           C  
-ATOM  27383  O   MET G 507      29.046  75.275  46.608  1.00 21.17           O  
-ATOM  27384  CB  MET G 507      30.986  77.469  47.528  1.00 18.69           C  
-ATOM  27385  CG  MET G 507      30.537  77.782  48.950  1.00 21.04           C  
-ATOM  27386  SD  MET G 507      28.747  77.782  49.159  1.00 23.57           S  
-ATOM  27387  CE  MET G 507      28.320  79.321  48.352  1.00 21.67           C  
-ATOM  27388  N   TYR G 508      29.857  74.428  48.526  1.00 18.14           N  
-ATOM  27389  CA  TYR G 508      28.646  73.680  48.832  1.00 17.72           C  
-ATOM  27390  C   TYR G 508      27.798  74.442  49.842  1.00 22.31           C  
-ATOM  27391  O   TYR G 508      28.289  74.876  50.884  1.00 26.78           O  
-ATOM  27392  CB  TYR G 508      28.979  72.285  49.366  1.00 18.10           C  
-ATOM  27393  CG  TYR G 508      27.754  71.424  49.581  1.00 17.55           C  
-ATOM  27394  CD1 TYR G 508      27.185  70.718  48.529  1.00 17.74           C  
-ATOM  27395  CD2 TYR G 508      27.160  71.326  50.831  1.00 22.43           C  
-ATOM  27396  CE1 TYR G 508      26.061  69.936  48.718  1.00 20.05           C  
-ATOM  27397  CE2 TYR G 508      26.037  70.546  51.030  1.00 22.97           C  
-ATOM  27398  CZ  TYR G 508      25.492  69.853  49.972  1.00 23.59           C  
-ATOM  27399  OH  TYR G 508      24.373  69.074  50.170  1.00 29.60           O  
-ATOM  27400  N   GLN G 509      26.520  74.599  49.524  1.00 21.88           N  
-ATOM  27401  CA  GLN G 509      25.611  75.349  50.376  1.00 26.36           C  
-ATOM  27402  C   GLN G 509      24.422  74.481  50.779  1.00 30.66           C  
-ATOM  27403  O   GLN G 509      23.634  74.063  49.930  1.00 25.89           O  
-ATOM  27404  CB  GLN G 509      25.143  76.611  49.656  1.00 19.42           C  
-ATOM  27405  CG  GLN G 509      24.531  77.657  50.559  1.00 25.85           C  
-ATOM  27406  CD  GLN G 509      24.151  78.911  49.800  1.00 35.84           C  
-ATOM  27407  OE1 GLN G 509      24.781  79.260  48.803  1.00 33.89           O  
-ATOM  27408  NE2 GLN G 509      23.109  79.590  50.261  1.00 46.60           N  
-ATOM  27409  N   ARG G 510      24.300  74.204  52.075  1.00 24.48           N  
-ATOM  27410  CA  ARG G 510      23.258  73.307  52.563  1.00 26.94           C  
-ATOM  27411  C   ARG G 510      21.866  73.892  52.368  1.00 22.80           C  
-ATOM  27412  O   ARG G 510      20.918  73.168  52.068  1.00 22.33           O  
-ATOM  27413  CB  ARG G 510      23.474  72.977  54.042  1.00 26.52           C  
-ATOM  27414  CG  ARG G 510      23.505  74.187  54.957  1.00 28.16           C  
-ATOM  27415  CD  ARG G 510      23.293  73.785  56.405  1.00 27.29           C  
-ATOM  27416  NE  ARG G 510      23.054  74.944  57.258  1.00 29.22           N  
-ATOM  27417  CZ  ARG G 510      21.870  75.529  57.401  1.00 28.56           C  
-ATOM  27418  NH1 ARG G 510      20.818  75.063  56.745  1.00 27.58           N  
-ATOM  27419  NH2 ARG G 510      21.738  76.581  58.197  1.00 31.99           N  
-ATOM  27420  N   SER G 511      21.751  75.204  52.541  1.00 23.60           N  
-ATOM  27421  CA  SER G 511      20.470  75.883  52.420  1.00 35.48           C  
-ATOM  27422  C   SER G 511      20.630  77.148  51.592  1.00 37.25           C  
-ATOM  27423  O   SER G 511      21.590  77.895  51.775  1.00 43.82           O  
-ATOM  27424  CB  SER G 511      19.904  76.216  53.800  1.00 32.29           C  
-ATOM  27425  OG  SER G 511      18.579  76.709  53.701  1.00 36.45           O  
-ATOM  27426  N   CYS G 512      19.691  77.391  50.684  1.00 31.03           N  
-ATOM  27427  CA  CYS G 512      19.839  78.487  49.737  1.00 26.92           C  
-ATOM  27428  C   CYS G 512      18.577  79.322  49.568  1.00 29.05           C  
-ATOM  27429  O   CYS G 512      17.636  78.908  48.891  1.00 29.72           O  
-ATOM  27430  CB  CYS G 512      20.265  77.942  48.373  1.00 30.78           C  
-ATOM  27431  SG  CYS G 512      21.740  76.901  48.401  1.00 36.65           S  
-ATOM  27432  N   ASP G 513      18.565  80.502  50.180  1.00 37.75           N  
-ATOM  27433  CA  ASP G 513      17.542  81.497  49.888  1.00 34.26           C  
-ATOM  27434  C   ASP G 513      17.820  82.046  48.493  1.00 27.62           C  
-ATOM  27435  O   ASP G 513      18.670  82.917  48.315  1.00 27.01           O  
-ATOM  27436  CB  ASP G 513      17.541  82.614  50.934  1.00 41.46           C  
-ATOM  27437  CG  ASP G 513      16.296  83.485  50.864  1.00 51.93           C  
-ATOM  27438  OD1 ASP G 513      15.657  83.533  49.790  1.00 50.15           O  
-ATOM  27439  OD2 ASP G 513      15.958  84.124  51.884  1.00 52.49           O  
-ATOM  27440  N   VAL G 514      17.101  81.522  47.507  1.00 22.30           N  
-ATOM  27441  CA  VAL G 514      17.391  81.804  46.105  1.00 21.84           C  
-ATOM  27442  C   VAL G 514      17.182  83.264  45.721  1.00 29.98           C  
-ATOM  27443  O   VAL G 514      18.038  83.869  45.076  1.00 37.22           O  
-ATOM  27444  CB  VAL G 514      16.541  80.919  45.183  1.00 18.82           C  
-ATOM  27445  CG1 VAL G 514      16.551  81.454  43.762  1.00 24.98           C  
-ATOM  27446  CG2 VAL G 514      17.062  79.502  45.219  1.00 24.70           C  
-ATOM  27447  N   GLY G 515      16.049  83.829  46.119  1.00 30.82           N  
-ATOM  27448  CA  GLY G 515      15.735  85.198  45.761  1.00 32.72           C  
-ATOM  27449  C   GLY G 515      16.656  86.214  46.408  1.00 34.66           C  
-ATOM  27450  O   GLY G 515      16.993  87.230  45.800  1.00 41.85           O  
-ATOM  27451  N   LEU G 516      17.083  85.928  47.633  1.00 31.02           N  
-ATOM  27452  CA  LEU G 516      17.778  86.921  48.445  1.00 41.01           C  
-ATOM  27453  C   LEU G 516      19.266  86.626  48.651  1.00 39.70           C  
-ATOM  27454  O   LEU G 516      20.106  87.511  48.487  1.00 42.03           O  
-ATOM  27455  CB  LEU G 516      17.082  87.044  49.801  1.00 40.81           C  
-ATOM  27456  CG  LEU G 516      17.372  88.280  50.648  1.00 50.95           C  
-ATOM  27457  CD1 LEU G 516      17.495  89.519  49.776  1.00 56.84           C  
-ATOM  27458  CD2 LEU G 516      16.260  88.454  51.667  1.00 65.15           C  
-ATOM  27459  N   GLY G 517      19.589  85.387  49.009  1.00 28.26           N  
-ATOM  27460  CA  GLY G 517      20.943  85.047  49.409  1.00 27.93           C  
-ATOM  27461  C   GLY G 517      21.886  84.605  48.302  1.00 30.99           C  
-ATOM  27462  O   GLY G 517      23.058  84.991  48.287  1.00 22.78           O  
-ATOM  27463  N   VAL G 518      21.379  83.792  47.379  1.00 25.87           N  
-ATOM  27464  CA  VAL G 518      22.203  83.158  46.349  1.00 20.87           C  
-ATOM  27465  C   VAL G 518      23.081  84.115  45.529  1.00 22.38           C  
-ATOM  27466  O   VAL G 518      24.269  83.841  45.358  1.00 23.91           O  
-ATOM  27467  CB  VAL G 518      21.325  82.325  45.385  1.00 17.98           C  
-ATOM  27468  CG1 VAL G 518      22.094  81.969  44.121  1.00 14.91           C  
-ATOM  27469  CG2 VAL G 518      20.845  81.077  46.085  1.00 22.84           C  
-ATOM  27470  N   PRO G 519      22.521  85.236  45.025  1.00 20.41           N  
-ATOM  27471  CA  PRO G 519      23.414  86.124  44.266  1.00 20.75           C  
-ATOM  27472  C   PRO G 519      24.575  86.639  45.114  1.00 19.34           C  
-ATOM  27473  O   PRO G 519      25.725  86.684  44.663  1.00 16.24           O  
-ATOM  27474  CB  PRO G 519      22.493  87.281  43.853  1.00 20.52           C  
-ATOM  27475  CG  PRO G 519      21.123  86.722  43.926  1.00 20.19           C  
-ATOM  27476  CD  PRO G 519      21.145  85.762  45.064  1.00 16.17           C  
-ATOM  27477  N   PHE G 520      24.242  87.017  46.344  1.00 15.28           N  
-ATOM  27478  CA  PHE G 520      25.201  87.476  47.334  1.00 12.77           C  
-ATOM  27479  C   PHE G 520      26.290  86.438  47.581  1.00 18.63           C  
-ATOM  27480  O   PHE G 520      27.469  86.778  47.674  1.00 27.30           O  
-ATOM  27481  CB  PHE G 520      24.471  87.800  48.634  1.00 19.20           C  
-ATOM  27482  CG  PHE G 520      25.292  88.573  49.624  1.00 26.60           C  
-ATOM  27483  CD1 PHE G 520      26.004  87.920  50.617  1.00 28.92           C  
-ATOM  27484  CD2 PHE G 520      25.329  89.956  49.578  1.00 25.09           C  
-ATOM  27485  CE1 PHE G 520      26.748  88.633  51.537  1.00 27.77           C  
-ATOM  27486  CE2 PHE G 520      26.068  90.672  50.495  1.00 31.43           C  
-ATOM  27487  CZ  PHE G 520      26.775  90.009  51.478  1.00 34.63           C  
-ATOM  27488  N   ASN G 521      25.894  85.173  47.688  1.00 18.23           N  
-ATOM  27489  CA  ASN G 521      26.855  84.094  47.882  1.00 20.10           C  
-ATOM  27490  C   ASN G 521      27.771  83.920  46.677  1.00 20.28           C  
-ATOM  27491  O   ASN G 521      28.994  83.817  46.827  1.00 22.01           O  
-ATOM  27492  CB  ASN G 521      26.132  82.783  48.172  1.00 22.05           C  
-ATOM  27493  CG  ASN G 521      25.400  82.807  49.490  1.00 24.73           C  
-ATOM  27494  OD1 ASN G 521      24.178  82.678  49.534  1.00 27.95           O  
-ATOM  27495  ND2 ASN G 521      26.142  82.984  50.576  1.00 27.60           N  
-ATOM  27496  N   ILE G 522      27.168  83.878  45.491  1.00 15.04           N  
-ATOM  27497  CA  ILE G 522      27.910  83.805  44.238  1.00 16.38           C  
-ATOM  27498  C   ILE G 522      28.991  84.877  44.181  1.00 17.35           C  
-ATOM  27499  O   ILE G 522      30.175  84.576  44.000  1.00 14.76           O  
-ATOM  27500  CB  ILE G 522      26.969  83.958  43.024  1.00 16.92           C  
-ATOM  27501  CG1 ILE G 522      25.977  82.794  42.969  1.00 20.58           C  
-ATOM  27502  CG2 ILE G 522      27.770  84.030  41.743  1.00 17.06           C  
-ATOM  27503  CD1 ILE G 522      24.956  82.925  41.866  1.00 19.72           C  
-ATOM  27504  N   ALA G 523      28.570  86.126  44.360  1.00 18.21           N  
-ATOM  27505  CA  ALA G 523      29.495  87.253  44.378  1.00 18.44           C  
-ATOM  27506  C   ALA G 523      30.574  87.069  45.442  1.00 16.62           C  
-ATOM  27507  O   ALA G 523      31.756  87.334  45.197  1.00 13.71           O  
-ATOM  27508  CB  ALA G 523      28.740  88.553  44.613  1.00 15.30           C  
-ATOM  27509  N   SER G 524      30.161  86.602  46.615  1.00 15.10           N  
-ATOM  27510  CA  SER G 524      31.070  86.440  47.739  1.00 16.55           C  
-ATOM  27511  C   SER G 524      32.208  85.472  47.436  1.00 18.43           C  
-ATOM  27512  O   SER G 524      33.383  85.827  47.552  1.00 22.82           O  
-ATOM  27513  CB  SER G 524      30.302  85.971  48.974  1.00 12.60           C  
-ATOM  27514  OG  SER G 524      31.130  86.032  50.117  1.00 17.55           O  
-ATOM  27515  N   TYR G 525      31.865  84.249  47.051  1.00 15.83           N  
-ATOM  27516  CA  TYR G 525      32.892  83.241  46.822  1.00 12.94           C  
-ATOM  27517  C   TYR G 525      33.641  83.471  45.515  1.00 15.66           C  
-ATOM  27518  O   TYR G 525      34.783  83.037  45.370  1.00 17.58           O  
-ATOM  27519  CB  TYR G 525      32.284  81.839  46.869  1.00 10.70           C  
-ATOM  27520  CG  TYR G 525      32.165  81.342  48.293  1.00 19.94           C  
-ATOM  27521  CD1 TYR G 525      31.076  81.691  49.080  1.00 23.63           C  
-ATOM  27522  CD2 TYR G 525      33.159  80.559  48.862  1.00 21.07           C  
-ATOM  27523  CE1 TYR G 525      30.970  81.261  50.386  1.00 19.89           C  
-ATOM  27524  CE2 TYR G 525      33.063  80.120  50.167  1.00 26.52           C  
-ATOM  27525  CZ  TYR G 525      31.966  80.474  50.926  1.00 24.69           C  
-ATOM  27526  OH  TYR G 525      31.864  80.039  52.227  1.00 33.80           O  
-ATOM  27527  N   SER G 526      33.018  84.169  44.571  1.00 17.40           N  
-ATOM  27528  CA  SER G 526      33.742  84.573  43.371  1.00 16.01           C  
-ATOM  27529  C   SER G 526      34.834  85.573  43.754  1.00 18.44           C  
-ATOM  27530  O   SER G 526      35.968  85.495  43.265  1.00 17.82           O  
-ATOM  27531  CB  SER G 526      32.797  85.179  42.335  1.00 17.20           C  
-ATOM  27532  OG  SER G 526      31.759  84.275  42.007  1.00 20.46           O  
-ATOM  27533  N   LEU G 527      34.484  86.501  44.644  1.00 20.41           N  
-ATOM  27534  CA  LEU G 527      35.442  87.472  45.171  1.00 16.04           C  
-ATOM  27535  C   LEU G 527      36.566  86.773  45.925  1.00 16.91           C  
-ATOM  27536  O   LEU G 527      37.745  87.096  45.738  1.00 20.17           O  
-ATOM  27537  CB  LEU G 527      34.748  88.480  46.092  1.00 15.14           C  
-ATOM  27538  CG  LEU G 527      35.631  89.622  46.608  1.00 16.39           C  
-ATOM  27539  CD1 LEU G 527      36.194  90.433  45.453  1.00 15.93           C  
-ATOM  27540  CD2 LEU G 527      34.863  90.521  47.565  1.00 22.30           C  
-ATOM  27541  N   LEU G 528      36.195  85.821  46.781  1.00 17.08           N  
-ATOM  27542  CA  LEU G 528      37.182  85.022  47.505  1.00 17.20           C  
-ATOM  27543  C   LEU G 528      38.141  84.371  46.523  1.00 19.99           C  
-ATOM  27544  O   LEU G 528      39.353  84.385  46.730  1.00 19.28           O  
-ATOM  27545  CB  LEU G 528      36.520  83.941  48.364  1.00 14.65           C  
-ATOM  27546  CG  LEU G 528      37.506  83.042  49.120  1.00  8.40           C  
-ATOM  27547  CD1 LEU G 528      38.215  83.845  50.192  1.00 13.68           C  
-ATOM  27548  CD2 LEU G 528      36.822  81.823  49.720  1.00 10.90           C  
-ATOM  27549  N   THR G 529      37.588  83.806  45.452  1.00 17.06           N  
-ATOM  27550  CA  THR G 529      38.400  83.167  44.423  1.00 16.28           C  
-ATOM  27551  C   THR G 529      39.365  84.162  43.789  1.00 16.71           C  
-ATOM  27552  O   THR G 529      40.532  83.842  43.585  1.00 21.22           O  
-ATOM  27553  CB  THR G 529      37.538  82.535  43.314  1.00 12.98           C  
-ATOM  27554  OG1 THR G 529      36.592  81.625  43.889  1.00 11.80           O  
-ATOM  27555  CG2 THR G 529      38.422  81.782  42.331  1.00 13.14           C  
-ATOM  27556  N   LEU G 530      38.877  85.361  43.478  1.00 18.77           N  
-ATOM  27557  CA  LEU G 530      39.746  86.415  42.958  1.00 17.49           C  
-ATOM  27558  C   LEU G 530      40.920  86.674  43.893  1.00 19.80           C  
-ATOM  27559  O   LEU G 530      42.081  86.627  43.477  1.00 20.04           O  
-ATOM  27560  CB  LEU G 530      38.977  87.720  42.751  1.00 14.73           C  
-ATOM  27561  CG  LEU G 530      37.997  87.838  41.589  1.00 12.89           C  
-ATOM  27562  CD1 LEU G 530      37.761  89.301  41.268  1.00 17.20           C  
-ATOM  27563  CD2 LEU G 530      38.523  87.110  40.378  1.00 16.39           C  
-ATOM  27564  N   MET G 531      40.610  86.941  45.158  1.00 17.07           N  
-ATOM  27565  CA  MET G 531      41.635  87.295  46.133  1.00 25.90           C  
-ATOM  27566  C   MET G 531      42.667  86.182  46.328  1.00 23.55           C  
-ATOM  27567  O   MET G 531      43.877  86.425  46.260  1.00 24.08           O  
-ATOM  27568  CB  MET G 531      40.974  87.656  47.461  1.00 18.37           C  
-ATOM  27569  CG  MET G 531      39.975  88.791  47.337  1.00 14.45           C  
-ATOM  27570  SD  MET G 531      38.898  88.929  48.769  1.00 32.19           S  
-ATOM  27571  CE  MET G 531      40.070  89.431  50.022  1.00 27.89           C  
-ATOM  27572  N   VAL G 532      42.183  84.967  46.567  1.00 17.83           N  
-ATOM  27573  CA  VAL G 532      43.055  83.806  46.688  1.00 18.93           C  
-ATOM  27574  C   VAL G 532      43.952  83.665  45.461  1.00 18.99           C  
-ATOM  27575  O   VAL G 532      45.162  83.466  45.585  1.00 19.54           O  
-ATOM  27576  CB  VAL G 532      42.245  82.510  46.877  1.00 18.38           C  
-ATOM  27577  CG1 VAL G 532      43.138  81.297  46.727  1.00 13.58           C  
-ATOM  27578  CG2 VAL G 532      41.568  82.510  48.235  1.00 23.70           C  
-ATOM  27579  N   ALA G 533      43.354  83.789  44.279  1.00 19.34           N  
-ATOM  27580  CA  ALA G 533      44.090  83.663  43.025  1.00 19.44           C  
-ATOM  27581  C   ALA G 533      45.209  84.695  42.940  1.00 25.69           C  
-ATOM  27582  O   ALA G 533      46.331  84.367  42.554  1.00 22.11           O  
-ATOM  27583  CB  ALA G 533      43.151  83.804  41.838  1.00 17.98           C  
-ATOM  27584  N   HIS G 534      44.902  85.940  43.297  1.00 27.35           N  
-ATOM  27585  CA  HIS G 534      45.910  86.993  43.273  1.00 26.92           C  
-ATOM  27586  C   HIS G 534      47.041  86.695  44.249  1.00 24.35           C  
-ATOM  27587  O   HIS G 534      48.214  86.832  43.906  1.00 29.81           O  
-ATOM  27588  CB  HIS G 534      45.306  88.357  43.603  1.00 21.98           C  
-ATOM  27589  CG  HIS G 534      46.334  89.405  43.895  1.00 24.23           C  
-ATOM  27590  ND1 HIS G 534      47.114  89.976  42.913  1.00 28.99           N  
-ATOM  27591  CD2 HIS G 534      46.737  89.959  45.064  1.00 21.68           C  
-ATOM  27592  CE1 HIS G 534      47.940  90.850  43.461  1.00 30.37           C  
-ATOM  27593  NE2 HIS G 534      47.730  90.859  44.765  1.00 23.37           N  
-ATOM  27594  N   VAL G 535      46.685  86.290  45.464  1.00 22.50           N  
-ATOM  27595  CA  VAL G 535      47.683  86.024  46.495  1.00 19.59           C  
-ATOM  27596  C   VAL G 535      48.566  84.821  46.134  1.00 21.37           C  
-ATOM  27597  O   VAL G 535      49.731  84.754  46.528  1.00 21.78           O  
-ATOM  27598  CB  VAL G 535      46.999  85.816  47.875  1.00 25.36           C  
-ATOM  27599  CG1 VAL G 535      47.893  85.051  48.840  1.00 31.20           C  
-ATOM  27600  CG2 VAL G 535      46.599  87.161  48.468  1.00 26.76           C  
-ATOM  27601  N   CYS G 536      48.028  83.894  45.347  1.00 27.30           N  
-ATOM  27602  CA  CYS G 536      48.775  82.695  44.970  1.00 18.58           C  
-ATOM  27603  C   CYS G 536      49.403  82.769  43.577  1.00 21.72           C  
-ATOM  27604  O   CYS G 536      49.863  81.756  43.051  1.00 29.14           O  
-ATOM  27605  CB  CYS G 536      47.865  81.471  45.040  1.00 15.77           C  
-ATOM  27606  SG  CYS G 536      47.159  81.176  46.669  1.00 40.65           S  
-ATOM  27607  N   ASN G 537      49.428  83.964  42.993  1.00 26.89           N  
-ATOM  27608  CA  ASN G 537      49.900  84.163  41.620  1.00 30.71           C  
-ATOM  27609  C   ASN G 537      49.214  83.235  40.624  1.00 28.13           C  
-ATOM  27610  O   ASN G 537      49.873  82.567  39.827  1.00 33.09           O  
-ATOM  27611  CB  ASN G 537      51.417  83.975  41.529  1.00 34.38           C  
-ATOM  27612  CG  ASN G 537      52.175  85.285  41.633  1.00 43.23           C  
-ATOM  27613  OD1 ASN G 537      52.247  86.052  40.671  1.00 44.91           O  
-ATOM  27614  ND2 ASN G 537      52.757  85.542  42.799  1.00 36.30           N  
-ATOM  27615  N   LEU G 538      47.888  83.198  40.675  1.00 26.01           N  
-ATOM  27616  CA  LEU G 538      47.112  82.353  39.776  1.00 29.57           C  
-ATOM  27617  C   LEU G 538      46.067  83.162  39.016  1.00 24.15           C  
-ATOM  27618  O   LEU G 538      45.783  84.308  39.358  1.00 23.71           O  
-ATOM  27619  CB  LEU G 538      46.433  81.226  40.555  1.00 27.93           C  
-ATOM  27620  CG  LEU G 538      47.366  80.229  41.241  1.00 20.68           C  
-ATOM  27621  CD1 LEU G 538      46.588  79.306  42.168  1.00 14.96           C  
-ATOM  27622  CD2 LEU G 538      48.132  79.432  40.201  1.00 21.32           C  
-ATOM  27623  N   LYS G 539      45.503  82.557  37.980  1.00 14.41           N  
-ATOM  27624  CA  LYS G 539      44.446  83.193  37.209  1.00 24.69           C  
-ATOM  27625  C   LYS G 539      43.080  82.665  37.638  1.00 30.89           C  
-ATOM  27626  O   LYS G 539      42.875  81.454  37.715  1.00 31.42           O  
-ATOM  27627  CB  LYS G 539      44.660  82.957  35.712  1.00 39.55           C  
-ATOM  27628  CG  LYS G 539      45.625  83.928  35.046  1.00 41.37           C  
-ATOM  27629  CD  LYS G 539      44.926  85.209  34.596  1.00 62.97           C  
-ATOM  27630  CE  LYS G 539      43.923  84.952  33.470  1.00 74.27           C  
-ATOM  27631  NZ  LYS G 539      42.558  84.586  33.960  1.00 49.04           N  
-ATOM  27632  N   PRO G 540      42.139  83.575  37.927  1.00 28.02           N  
-ATOM  27633  CA  PRO G 540      40.780  83.139  38.260  1.00 22.47           C  
-ATOM  27634  C   PRO G 540      40.068  82.555  37.046  1.00 26.60           C  
-ATOM  27635  O   PRO G 540      40.008  83.196  35.996  1.00 28.86           O  
-ATOM  27636  CB  PRO G 540      40.102  84.426  38.731  1.00 19.56           C  
-ATOM  27637  CG  PRO G 540      40.856  85.515  38.058  1.00 23.55           C  
-ATOM  27638  CD  PRO G 540      42.278  85.040  37.970  1.00 29.99           C  
-ATOM  27639  N   LYS G 541      39.536  81.346  37.191  1.00 23.84           N  
-ATOM  27640  CA  LYS G 541      38.913  80.656  36.072  1.00 23.10           C  
-ATOM  27641  C   LYS G 541      37.410  80.498  36.255  1.00 25.90           C  
-ATOM  27642  O   LYS G 541      36.628  80.883  35.384  1.00 30.76           O  
-ATOM  27643  CB  LYS G 541      39.547  79.279  35.873  1.00 26.24           C  
-ATOM  27644  CG  LYS G 541      39.032  78.530  34.650  1.00 32.26           C  
-ATOM  27645  CD  LYS G 541      39.718  79.002  33.375  1.00 35.10           C  
-ATOM  27646  CE  LYS G 541      39.015  78.471  32.137  1.00 41.60           C  
-ATOM  27647  NZ  LYS G 541      37.681  79.112  31.944  1.00 46.62           N  
-ATOM  27648  N   GLU G 542      37.004  79.938  37.390  1.00 25.05           N  
-ATOM  27649  CA  GLU G 542      35.619  79.519  37.545  1.00 27.06           C  
-ATOM  27650  C   GLU G 542      35.174  79.383  39.000  1.00 27.43           C  
-ATOM  27651  O   GLU G 542      35.910  78.858  39.837  1.00 21.06           O  
-ATOM  27652  CB  GLU G 542      35.423  78.188  36.822  1.00 18.50           C  
-ATOM  27653  CG  GLU G 542      34.029  77.944  36.309  1.00 21.33           C  
-ATOM  27654  CD  GLU G 542      33.941  76.659  35.517  1.00 36.38           C  
-ATOM  27655  OE1 GLU G 542      33.226  76.635  34.492  1.00 32.51           O  
-ATOM  27656  OE2 GLU G 542      34.594  75.671  35.920  1.00 38.12           O  
-ATOM  27657  N   PHE G 543      33.968  79.864  39.298  1.00 18.82           N  
-ATOM  27658  CA  PHE G 543      33.334  79.568  40.578  1.00 16.54           C  
-ATOM  27659  C   PHE G 543      32.183  78.599  40.370  1.00 17.65           C  
-ATOM  27660  O   PHE G 543      31.293  78.849  39.561  1.00 20.85           O  
-ATOM  27661  CB  PHE G 543      32.814  80.828  41.267  1.00 15.00           C  
-ATOM  27662  CG  PHE G 543      31.740  80.547  42.282  1.00 15.66           C  
-ATOM  27663  CD1 PHE G 543      32.033  79.851  43.444  1.00 14.61           C  
-ATOM  27664  CD2 PHE G 543      30.433  80.958  42.066  1.00 22.52           C  
-ATOM  27665  CE1 PHE G 543      31.046  79.578  44.374  1.00 16.44           C  
-ATOM  27666  CE2 PHE G 543      29.441  80.688  42.998  1.00 15.43           C  
-ATOM  27667  CZ  PHE G 543      29.749  79.998  44.150  1.00 15.22           C  
-ATOM  27668  N   ILE G 544      32.193  77.500  41.114  1.00 15.34           N  
-ATOM  27669  CA  ILE G 544      31.180  76.470  40.941  1.00 12.27           C  
-ATOM  27670  C   ILE G 544      30.277  76.365  42.166  1.00 17.43           C  
-ATOM  27671  O   ILE G 544      30.739  76.143  43.285  1.00 21.98           O  
-ATOM  27672  CB  ILE G 544      31.830  75.115  40.647  1.00 11.97           C  
-ATOM  27673  CG1 ILE G 544      32.835  75.267  39.504  1.00 14.33           C  
-ATOM  27674  CG2 ILE G 544      30.773  74.085  40.303  1.00 14.52           C  
-ATOM  27675  CD1 ILE G 544      33.701  74.060  39.276  1.00 18.38           C  
-ATOM  27676  N   HIS G 545      28.980  76.527  41.938  1.00 17.09           N  
-ATOM  27677  CA  HIS G 545      27.998  76.574  43.009  1.00 15.02           C  
-ATOM  27678  C   HIS G 545      27.214  75.269  43.144  1.00 16.76           C  
-ATOM  27679  O   HIS G 545      26.405  74.918  42.277  1.00 24.02           O  
-ATOM  27680  CB  HIS G 545      27.037  77.737  42.776  1.00 17.75           C  
-ATOM  27681  CG  HIS G 545      26.414  78.264  44.028  1.00 25.76           C  
-ATOM  27682  ND1 HIS G 545      26.554  77.636  45.248  1.00 25.19           N  
-ATOM  27683  CD2 HIS G 545      25.655  79.362  44.256  1.00 28.07           C  
-ATOM  27684  CE1 HIS G 545      25.904  78.321  46.170  1.00 28.29           C  
-ATOM  27685  NE2 HIS G 545      25.350  79.373  45.596  1.00 30.10           N  
-ATOM  27686  N   PHE G 546      27.473  74.555  44.237  1.00 15.91           N  
-ATOM  27687  CA  PHE G 546      26.744  73.337  44.582  1.00 17.90           C  
-ATOM  27688  C   PHE G 546      25.737  73.622  45.688  1.00 22.69           C  
-ATOM  27689  O   PHE G 546      26.102  74.077  46.771  1.00 28.28           O  
-ATOM  27690  CB  PHE G 546      27.705  72.229  45.021  1.00 18.20           C  
-ATOM  27691  CG  PHE G 546      28.397  71.541  43.881  1.00 24.94           C  
-ATOM  27692  CD1 PHE G 546      27.990  71.755  42.574  1.00 21.54           C  
-ATOM  27693  CD2 PHE G 546      29.445  70.669  44.117  1.00 21.13           C  
-ATOM  27694  CE1 PHE G 546      28.622  71.120  41.527  1.00 15.71           C  
-ATOM  27695  CE2 PHE G 546      30.081  70.031  43.070  1.00 18.81           C  
-ATOM  27696  CZ  PHE G 546      29.668  70.257  41.775  1.00 16.11           C  
-ATOM  27697  N   MET G 547      24.469  73.340  45.414  1.00 20.40           N  
-ATOM  27698  CA  MET G 547      23.385  73.761  46.291  1.00 17.00           C  
-ATOM  27699  C   MET G 547      22.575  72.577  46.813  1.00 19.82           C  
-ATOM  27700  O   MET G 547      22.076  71.763  46.039  1.00 20.18           O  
-ATOM  27701  CB  MET G 547      22.479  74.738  45.547  1.00 16.60           C  
-ATOM  27702  CG  MET G 547      23.241  75.598  44.546  1.00 27.75           C  
-ATOM  27703  SD  MET G 547      22.219  76.671  43.521  1.00 31.40           S  
-ATOM  27704  CE  MET G 547      21.738  77.904  44.721  1.00 31.53           C  
-ATOM  27705  N   GLY G 548      22.451  72.485  48.132  1.00 24.15           N  
-ATOM  27706  CA  GLY G 548      21.689  71.419  48.758  1.00 24.35           C  
-ATOM  27707  C   GLY G 548      20.200  71.694  48.729  1.00 23.24           C  
-ATOM  27708  O   GLY G 548      19.551  71.532  47.695  1.00 25.48           O  
-ATOM  27709  N   ASN G 549      19.652  72.102  49.869  1.00 20.74           N  
-ATOM  27710  CA  ASN G 549      18.260  72.523  49.925  1.00 19.81           C  
-ATOM  27711  C   ASN G 549      18.106  73.872  49.237  1.00 24.49           C  
-ATOM  27712  O   ASN G 549      18.426  74.910  49.814  1.00 35.13           O  
-ATOM  27713  CB  ASN G 549      17.771  72.601  51.373  1.00 22.00           C  
-ATOM  27714  CG  ASN G 549      16.263  72.758  51.474  1.00 31.17           C  
-ATOM  27715  OD1 ASN G 549      15.720  73.835  51.234  1.00 33.49           O  
-ATOM  27716  ND2 ASN G 549      15.579  71.680  51.840  1.00 30.76           N  
-ATOM  27717  N   THR G 550      17.628  73.850  47.998  1.00 23.10           N  
-ATOM  27718  CA  THR G 550      17.504  75.062  47.197  1.00 26.59           C  
-ATOM  27719  C   THR G 550      16.049  75.513  47.134  1.00 27.07           C  
-ATOM  27720  O   THR G 550      15.202  74.826  46.564  1.00 31.92           O  
-ATOM  27721  CB  THR G 550      18.041  74.843  45.775  1.00 27.15           C  
-ATOM  27722  OG1 THR G 550      19.268  74.107  45.838  1.00 26.02           O  
-ATOM  27723  CG2 THR G 550      18.291  76.168  45.090  1.00 30.75           C  
-ATOM  27724  N   HIS G 551      15.764  76.675  47.712  1.00 21.95           N  
-ATOM  27725  CA  HIS G 551      14.383  77.080  47.941  1.00 24.06           C  
-ATOM  27726  C   HIS G 551      14.133  78.563  47.708  1.00 24.41           C  
-ATOM  27727  O   HIS G 551      15.043  79.381  47.817  1.00 29.72           O  
-ATOM  27728  CB  HIS G 551      13.985  76.732  49.373  1.00 25.78           C  
-ATOM  27729  CG  HIS G 551      14.795  77.450  50.406  1.00 28.38           C  
-ATOM  27730  ND1 HIS G 551      15.991  76.961  50.886  1.00 28.33           N  
-ATOM  27731  CD2 HIS G 551      14.593  78.632  51.035  1.00 32.65           C  
-ATOM  27732  CE1 HIS G 551      16.485  77.805  51.774  1.00 34.38           C  
-ATOM  27733  NE2 HIS G 551      15.655  78.827  51.883  1.00 37.53           N  
-ATOM  27734  N   VAL G 552      12.887  78.902  47.391  1.00 26.64           N  
-ATOM  27735  CA  VAL G 552      12.450  80.293  47.409  1.00 39.70           C  
-ATOM  27736  C   VAL G 552      11.311  80.429  48.423  1.00 37.21           C  
-ATOM  27737  O   VAL G 552      10.517  79.502  48.613  1.00 31.65           O  
-ATOM  27738  CB  VAL G 552      12.004  80.790  46.005  1.00 33.68           C  
-ATOM  27739  CG1 VAL G 552      12.852  80.142  44.921  1.00 20.71           C  
-ATOM  27740  CG2 VAL G 552      10.524  80.523  45.755  1.00 27.60           C  
-ATOM  27741  N   TYR G 553      11.252  81.566  49.106  1.00 30.67           N  
-ATOM  27742  CA  TYR G 553      10.201  81.784  50.090  1.00 30.90           C  
-ATOM  27743  C   TYR G 553       8.938  82.268  49.397  1.00 36.14           C  
-ATOM  27744  O   TYR G 553       9.002  82.979  48.398  1.00 42.02           O  
-ATOM  27745  CB  TYR G 553      10.656  82.774  51.164  1.00 32.40           C  
-ATOM  27746  CG  TYR G 553      11.639  82.174  52.145  1.00 46.93           C  
-ATOM  27747  CD1 TYR G 553      11.202  81.364  53.186  1.00 45.20           C  
-ATOM  27748  CD2 TYR G 553      13.003  82.406  52.023  1.00 49.54           C  
-ATOM  27749  CE1 TYR G 553      12.095  80.804  54.081  1.00 46.98           C  
-ATOM  27750  CE2 TYR G 553      13.905  81.851  52.915  1.00 49.05           C  
-ATOM  27751  CZ  TYR G 553      13.444  81.051  53.941  1.00 48.09           C  
-ATOM  27752  OH  TYR G 553      14.333  80.496  54.833  1.00 45.41           O  
-ATOM  27753  N   THR G 554       7.789  81.863  49.926  1.00 45.07           N  
-ATOM  27754  CA  THR G 554       6.505  82.153  49.298  1.00 36.77           C  
-ATOM  27755  C   THR G 554       6.191  83.648  49.247  1.00 42.05           C  
-ATOM  27756  O   THR G 554       5.398  84.088  48.416  1.00 36.71           O  
-ATOM  27757  CB  THR G 554       5.360  81.429  50.024  1.00 41.41           C  
-ATOM  27758  OG1 THR G 554       5.542  81.550  51.440  1.00 44.91           O  
-ATOM  27759  CG2 THR G 554       5.340  79.954  49.646  1.00 31.53           C  
-ATOM  27760  N   ASN G 555       6.811  84.427  50.129  1.00 43.86           N  
-ATOM  27761  CA  ASN G 555       6.639  85.876  50.113  1.00 45.53           C  
-ATOM  27762  C   ASN G 555       7.629  86.551  49.165  1.00 39.06           C  
-ATOM  27763  O   ASN G 555       7.858  87.759  49.245  1.00 35.80           O  
-ATOM  27764  CB  ASN G 555       6.783  86.451  51.525  1.00 45.90           C  
-ATOM  27765  CG  ASN G 555       8.000  85.916  52.256  1.00 54.30           C  
-ATOM  27766  OD1 ASN G 555       8.403  84.772  52.056  1.00 56.45           O  
-ATOM  27767  ND2 ASN G 555       8.590  86.743  53.114  1.00 49.70           N  
-ATOM  27768  N   HIS G 556       8.206  85.759  48.266  1.00 43.46           N  
-ATOM  27769  CA  HIS G 556       9.163  86.258  47.285  1.00 38.39           C  
-ATOM  27770  C   HIS G 556       8.707  85.998  45.856  1.00 39.49           C  
-ATOM  27771  O   HIS G 556       9.218  86.604  44.921  1.00 43.76           O  
-ATOM  27772  CB  HIS G 556      10.534  85.613  47.491  1.00 37.11           C  
-ATOM  27773  CG  HIS G 556      11.235  86.059  48.735  1.00 44.35           C  
-ATOM  27774  ND1 HIS G 556      12.444  85.529  49.134  1.00 52.97           N  
-ATOM  27775  CD2 HIS G 556      10.903  86.983  49.665  1.00 51.64           C  
-ATOM  27776  CE1 HIS G 556      12.825  86.108  50.259  1.00 65.11           C  
-ATOM  27777  NE2 HIS G 556      11.908  86.995  50.603  1.00 63.52           N  
-ATOM  27778  N   VAL G 557       7.749  85.087  45.701  1.00 34.18           N  
-ATOM  27779  CA  VAL G 557       7.356  84.565  44.391  1.00 34.93           C  
-ATOM  27780  C   VAL G 557       6.895  85.641  43.410  1.00 44.33           C  
-ATOM  27781  O   VAL G 557       7.289  85.628  42.239  1.00 44.56           O  
-ATOM  27782  CB  VAL G 557       6.232  83.519  44.530  1.00 42.21           C  
-ATOM  27783  CG1 VAL G 557       5.817  83.001  43.165  1.00 32.44           C  
-ATOM  27784  CG2 VAL G 557       6.687  82.379  45.428  1.00 51.42           C  
-ATOM  27785  N  AGLU G 558       6.081  86.567  43.912  0.47 49.17           N  
-ATOM  27786  N  BGLU G 558       6.042  86.555  43.866  0.53 48.74           N  
-ATOM  27787  CA AGLU G 558       5.534  87.670  43.128  0.47 44.46           C  
-ATOM  27788  CA BGLU G 558       5.568  87.629  42.999  0.53 44.41           C  
-ATOM  27789  C  AGLU G 558       6.628  88.581  42.581  0.47 43.70           C  
-ATOM  27790  C  BGLU G 558       6.746  88.455  42.493  0.53 43.76           C  
-ATOM  27791  O  AGLU G 558       6.555  89.051  41.445  0.47 41.62           O  
-ATOM  27792  O  BGLU G 558       6.862  88.725  41.290  0.53 41.35           O  
-ATOM  27793  CB AGLU G 558       4.561  88.488  43.985  0.47 44.66           C  
-ATOM  27794  CB BGLU G 558       4.570  88.526  43.731  0.53 44.35           C  
-ATOM  27795  CG AGLU G 558       3.605  87.650  44.829  0.47 47.78           C  
-ATOM  27796  CG BGLU G 558       4.005  89.644  42.861  0.53 48.57           C  
-ATOM  27797  CD AGLU G 558       4.076  87.457  46.267  0.47 45.23           C  
-ATOM  27798  CD BGLU G 558       3.164  90.630  43.646  0.53 51.51           C  
-ATOM  27799  OE1AGLU G 558       4.987  86.633  46.503  0.47 37.30           O  
-ATOM  27800  OE1BGLU G 558       2.621  90.232  44.698  0.53 49.82           O  
-ATOM  27801  OE2AGLU G 558       3.524  88.127  47.165  0.47 43.38           O  
-ATOM  27802  OE2BGLU G 558       3.048  91.799  43.215  0.53 42.90           O  
-ATOM  27803  N   ALA G 559       7.629  88.830  43.414  1.00 40.02           N  
-ATOM  27804  CA  ALA G 559       8.763  89.674  43.074  1.00 46.89           C  
-ATOM  27805  C   ALA G 559       9.727  88.970  42.125  1.00 44.84           C  
-ATOM  27806  O   ALA G 559      10.287  89.594  41.229  1.00 45.86           O  
-ATOM  27807  CB  ALA G 559       9.486  90.108  44.340  1.00 47.47           C  
-ATOM  27808  N   LEU G 560       9.922  87.672  42.327  1.00 41.07           N  
-ATOM  27809  CA  LEU G 560      10.796  86.897  41.460  1.00 38.36           C  
-ATOM  27810  C   LEU G 560      10.189  86.799  40.071  1.00 33.63           C  
-ATOM  27811  O   LEU G 560      10.897  86.877  39.067  1.00 31.46           O  
-ATOM  27812  CB  LEU G 560      11.041  85.505  42.042  1.00 31.83           C  
-ATOM  27813  CG  LEU G 560      11.800  85.479  43.370  1.00 31.57           C  
-ATOM  27814  CD1 LEU G 560      12.031  84.052  43.850  1.00 39.31           C  
-ATOM  27815  CD2 LEU G 560      13.116  86.230  43.248  1.00 29.82           C  
-ATOM  27816  N   LYS G 561       8.871  86.631  40.024  1.00 31.43           N  
-ATOM  27817  CA  LYS G 561       8.149  86.619  38.760  1.00 34.73           C  
-ATOM  27818  C   LYS G 561       8.351  87.937  38.029  1.00 40.78           C  
-ATOM  27819  O   LYS G 561       8.474  87.964  36.802  1.00 31.87           O  
-ATOM  27820  CB  LYS G 561       6.659  86.356  38.987  1.00 45.33           C  
-ATOM  27821  CG  LYS G 561       6.334  84.912  39.322  1.00 40.20           C  
-ATOM  27822  CD  LYS G 561       4.832  84.669  39.362  1.00 41.22           C  
-ATOM  27823  CE  LYS G 561       4.516  83.198  39.585  1.00 46.66           C  
-ATOM  27824  NZ  LYS G 561       3.056  82.919  39.487  1.00 38.99           N  
-ATOM  27825  N   GLU G 562       8.374  89.027  38.793  1.00 49.15           N  
-ATOM  27826  CA  GLU G 562       8.715  90.331  38.243  1.00 40.88           C  
-ATOM  27827  C   GLU G 562      10.127  90.292  37.665  1.00 33.66           C  
-ATOM  27828  O   GLU G 562      10.359  90.701  36.530  1.00 28.78           O  
-ATOM  27829  CB  GLU G 562       8.608  91.420  39.316  1.00 40.61           C  
-ATOM  27830  CG  GLU G 562       7.187  91.736  39.768  1.00 60.15           C  
-ATOM  27831  CD  GLU G 562       6.557  92.872  38.980  1.00 68.32           C  
-ATOM  27832  OE1 GLU G 562       6.385  92.724  37.750  1.00 60.15           O  
-ATOM  27833  OE2 GLU G 562       6.237  93.914  39.593  1.00 67.87           O  
-ATOM  27834  N   GLN G 563      11.056  89.767  38.457  1.00 35.08           N  
-ATOM  27835  CA  GLN G 563      12.474  89.727  38.122  1.00 28.38           C  
-ATOM  27836  C   GLN G 563      12.744  88.922  36.854  1.00 28.61           C  
-ATOM  27837  O   GLN G 563      13.720  89.171  36.148  1.00 26.67           O  
-ATOM  27838  CB  GLN G 563      13.264  89.145  39.305  1.00 22.20           C  
-ATOM  27839  CG  GLN G 563      14.782  89.290  39.213  1.00 12.06           C  
-ATOM  27840  CD  GLN G 563      15.478  88.970  40.530  1.00 22.07           C  
-ATOM  27841  OE1 GLN G 563      14.862  89.002  41.596  1.00 39.83           O  
-ATOM  27842  NE2 GLN G 563      16.765  88.660  40.462  1.00 18.04           N  
-ATOM  27843  N   LEU G 564      11.874  87.963  36.560  1.00 27.94           N  
-ATOM  27844  CA  LEU G 564      12.085  87.082  35.420  1.00 26.50           C  
-ATOM  27845  C   LEU G 564      11.722  87.733  34.088  1.00 28.81           C  
-ATOM  27846  O   LEU G 564      12.042  87.199  33.028  1.00 29.66           O  
-ATOM  27847  CB  LEU G 564      11.287  85.790  35.594  1.00 35.51           C  
-ATOM  27848  CG  LEU G 564      11.709  84.876  36.747  1.00 36.06           C  
-ATOM  27849  CD1 LEU G 564      10.923  83.572  36.717  1.00 38.38           C  
-ATOM  27850  CD2 LEU G 564      13.205  84.608  36.711  1.00 35.02           C  
-ATOM  27851  N   ARG G 565      11.049  88.877  34.135  1.00 37.04           N  
-ATOM  27852  CA  ARG G 565      10.688  89.582  32.908  1.00 34.29           C  
-ATOM  27853  C   ARG G 565      11.840  90.459  32.438  1.00 24.95           C  
-ATOM  27854  O   ARG G 565      11.838  90.964  31.316  1.00 20.29           O  
-ATOM  27855  CB  ARG G 565       9.430  90.427  33.115  1.00 40.09           C  
-ATOM  27856  CG  ARG G 565       8.207  89.618  33.505  1.00 49.11           C  
-ATOM  27857  CD  ARG G 565       6.974  90.496  33.647  1.00 52.43           C  
-ATOM  27858  NE  ARG G 565       6.259  90.218  34.890  1.00 64.12           N  
-ATOM  27859  CZ  ARG G 565       5.364  89.246  35.042  1.00 60.55           C  
-ATOM  27860  NH1 ARG G 565       5.064  88.448  34.025  1.00 49.35           N  
-ATOM  27861  NH2 ARG G 565       4.768  89.071  36.214  1.00 49.82           N  
-ATOM  27862  N   ARG G 566      12.825  90.632  33.311  1.00 29.01           N  
-ATOM  27863  CA  ARG G 566      14.002  91.431  33.005  1.00 21.18           C  
-ATOM  27864  C   ARG G 566      15.077  90.579  32.340  1.00 25.64           C  
-ATOM  27865  O   ARG G 566      15.424  89.508  32.839  1.00 35.43           O  
-ATOM  27866  CB  ARG G 566      14.562  92.069  34.279  1.00 15.88           C  
-ATOM  27867  CG  ARG G 566      13.538  92.799  35.137  1.00 16.85           C  
-ATOM  27868  CD  ARG G 566      14.162  93.231  36.455  1.00 18.64           C  
-ATOM  27869  NE  ARG G 566      13.327  94.165  37.206  1.00 24.57           N  
-ATOM  27870  CZ  ARG G 566      13.689  94.720  38.359  1.00 32.10           C  
-ATOM  27871  NH1 ARG G 566      12.878  95.563  38.983  1.00 36.54           N  
-ATOM  27872  NH2 ARG G 566      14.869  94.431  38.890  1.00 31.97           N  
-ATOM  27873  N   GLU G 567      15.599  91.053  31.214  1.00 20.50           N  
-ATOM  27874  CA  GLU G 567      16.748  90.409  30.587  1.00 28.34           C  
-ATOM  27875  C   GLU G 567      18.034  90.988  31.169  1.00 23.08           C  
-ATOM  27876  O   GLU G 567      18.129  92.193  31.391  1.00 26.72           O  
-ATOM  27877  CB  GLU G 567      16.718  90.579  29.065  1.00 25.75           C  
-ATOM  27878  CG  GLU G 567      16.451  91.997  28.605  1.00 35.41           C  
-ATOM  27879  CD  GLU G 567      14.975  92.313  28.535  1.00 39.17           C  
-ATOM  27880  OE1 GLU G 567      14.202  91.429  28.112  1.00 36.59           O  
-ATOM  27881  OE2 GLU G 567      14.586  93.438  28.913  1.00 50.86           O  
-ATOM  27882  N   PRO G 568      19.029  90.123  31.421  1.00 19.85           N  
-ATOM  27883  CA  PRO G 568      20.269  90.518  32.099  1.00 18.38           C  
-ATOM  27884  C   PRO G 568      21.152  91.459  31.285  1.00 18.47           C  
-ATOM  27885  O   PRO G 568      21.033  91.538  30.062  1.00 20.14           O  
-ATOM  27886  CB  PRO G 568      20.980  89.181  32.322  1.00 17.16           C  
-ATOM  27887  CG  PRO G 568      20.473  88.310  31.233  1.00 19.30           C  
-ATOM  27888  CD  PRO G 568      19.037  88.696  31.056  1.00 20.86           C  
-ATOM  27889  N   ARG G 569      22.035  92.162  31.985  1.00 19.37           N  
-ATOM  27890  CA  ARG G 569      22.981  93.084  31.369  1.00 16.98           C  
-ATOM  27891  C   ARG G 569      24.382  92.478  31.441  1.00 17.66           C  
-ATOM  27892  O   ARG G 569      24.589  91.502  32.164  1.00 21.41           O  
-ATOM  27893  CB  ARG G 569      22.926  94.443  32.072  1.00 14.77           C  
-ATOM  27894  CG  ARG G 569      21.522  95.009  32.191  1.00 21.59           C  
-ATOM  27895  CD  ARG G 569      21.325  96.243  31.324  1.00 19.93           C  
-ATOM  27896  NE  ARG G 569      19.937  96.700  31.353  1.00 26.07           N  
-ATOM  27897  CZ  ARG G 569      19.414  97.447  32.322  1.00 23.02           C  
-ATOM  27898  NH1 ARG G 569      18.141  97.813  32.264  1.00 15.88           N  
-ATOM  27899  NH2 ARG G 569      20.160  97.825  33.351  1.00 17.89           N  
-ATOM  27900  N   PRO G 570      25.344  93.031  30.679  1.00 15.58           N  
-ATOM  27901  CA  PRO G 570      26.713  92.512  30.773  1.00 13.84           C  
-ATOM  27902  C   PRO G 570      27.272  92.551  32.193  1.00 14.89           C  
-ATOM  27903  O   PRO G 570      27.101  93.543  32.903  1.00 18.03           O  
-ATOM  27904  CB  PRO G 570      27.512  93.445  29.848  1.00 10.06           C  
-ATOM  27905  CG  PRO G 570      26.607  94.595  29.544  1.00 10.95           C  
-ATOM  27906  CD  PRO G 570      25.224  94.037  29.613  1.00 15.70           C  
-ATOM  27907  N   PHE G 571      27.916  91.461  32.598  1.00 13.06           N  
-ATOM  27908  CA  PHE G 571      28.568  91.392  33.897  1.00 10.73           C  
-ATOM  27909  C   PHE G 571      29.627  92.479  34.009  1.00 15.42           C  
-ATOM  27910  O   PHE G 571      30.242  92.855  33.013  1.00 18.97           O  
-ATOM  27911  CB  PHE G 571      29.202  90.016  34.113  1.00 14.47           C  
-ATOM  27912  CG  PHE G 571      28.237  88.968  34.586  1.00 16.85           C  
-ATOM  27913  CD1 PHE G 571      27.081  89.325  35.259  1.00 20.42           C  
-ATOM  27914  CD2 PHE G 571      28.490  87.623  34.363  1.00 18.77           C  
-ATOM  27915  CE1 PHE G 571      26.190  88.360  35.699  1.00 22.91           C  
-ATOM  27916  CE2 PHE G 571      27.606  86.654  34.801  1.00 19.70           C  
-ATOM  27917  CZ  PHE G 571      26.453  87.024  35.470  1.00 21.67           C  
-ATOM  27918  N   PRO G 572      29.833  93.003  35.224  1.00 16.73           N  
-ATOM  27919  CA  PRO G 572      30.896  93.988  35.428  1.00 18.30           C  
-ATOM  27920  C   PRO G 572      32.270  93.336  35.556  1.00 17.68           C  
-ATOM  27921  O   PRO G 572      32.387  92.112  35.536  1.00 15.75           O  
-ATOM  27922  CB  PRO G 572      30.493  94.662  36.740  1.00 18.33           C  
-ATOM  27923  CG  PRO G 572      29.791  93.583  37.491  1.00 14.21           C  
-ATOM  27924  CD  PRO G 572      29.051  92.777  36.453  1.00 18.03           C  
-ATOM  27925  N   ILE G 573      33.299  94.164  35.679  1.00 17.88           N  
-ATOM  27926  CA  ILE G 573      34.652  93.701  35.939  1.00 17.87           C  
-ATOM  27927  C   ILE G 573      35.069  94.127  37.337  1.00 19.40           C  
-ATOM  27928  O   ILE G 573      34.965  95.301  37.683  1.00 24.26           O  
-ATOM  27929  CB  ILE G 573      35.658  94.263  34.918  1.00 20.34           C  
-ATOM  27930  CG1 ILE G 573      35.582  93.491  33.601  1.00 20.75           C  
-ATOM  27931  CG2 ILE G 573      37.069  94.199  35.470  1.00 22.79           C  
-ATOM  27932  CD1 ILE G 573      36.602  93.938  32.579  1.00 11.72           C  
-ATOM  27933  N   VAL G 574      35.531  93.180  38.145  1.00 21.39           N  
-ATOM  27934  CA  VAL G 574      36.036  93.518  39.470  1.00 24.98           C  
-ATOM  27935  C   VAL G 574      37.559  93.575  39.444  1.00 23.23           C  
-ATOM  27936  O   VAL G 574      38.227  92.551  39.303  1.00 29.21           O  
-ATOM  27937  CB  VAL G 574      35.565  92.515  40.542  1.00 22.45           C  
-ATOM  27938  CG1 VAL G 574      36.330  92.726  41.840  1.00 22.78           C  
-ATOM  27939  CG2 VAL G 574      34.068  92.657  40.777  1.00 16.94           C  
-ATOM  27940  N   ASN G 575      38.098  94.783  39.565  1.00 21.84           N  
-ATOM  27941  CA  ASN G 575      39.539  94.986  39.561  1.00 19.37           C  
-ATOM  27942  C   ASN G 575      40.102  95.075  40.970  1.00 20.08           C  
-ATOM  27943  O   ASN G 575      39.516  95.714  41.848  1.00 21.08           O  
-ATOM  27944  CB  ASN G 575      39.905  96.252  38.781  1.00 19.52           C  
-ATOM  27945  CG  ASN G 575      39.728  96.089  37.285  1.00 20.45           C  
-ATOM  27946  OD1 ASN G 575      39.286  97.009  36.597  1.00 22.66           O  
-ATOM  27947  ND2 ASN G 575      40.071  94.913  36.772  1.00 15.49           N  
-ATOM  27948  N   ILE G 576      41.239  94.422  41.180  1.00 19.57           N  
-ATOM  27949  CA  ILE G 576      41.949  94.529  42.443  1.00 21.19           C  
-ATOM  27950  C   ILE G 576      42.995  95.629  42.344  1.00 22.99           C  
-ATOM  27951  O   ILE G 576      43.964  95.519  41.592  1.00 23.15           O  
-ATOM  27952  CB  ILE G 576      42.629  93.210  42.844  1.00 15.90           C  
-ATOM  27953  CG1 ILE G 576      41.586  92.106  43.014  1.00 19.22           C  
-ATOM  27954  CG2 ILE G 576      43.420  93.396  44.130  1.00 16.61           C  
-ATOM  27955  CD1 ILE G 576      42.162  90.790  43.489  1.00 19.95           C  
-ATOM  27956  N   LEU G 577      42.786  96.695  43.105  1.00 19.89           N  
-ATOM  27957  CA  LEU G 577      43.703  97.822  43.106  1.00 20.42           C  
-ATOM  27958  C   LEU G 577      44.890  97.542  44.019  1.00 27.76           C  
-ATOM  27959  O   LEU G 577      44.801  96.702  44.917  1.00 32.18           O  
-ATOM  27960  CB  LEU G 577      42.983  99.092  43.556  1.00 26.91           C  
-ATOM  27961  CG  LEU G 577      41.588  99.313  42.972  1.00 22.36           C  
-ATOM  27962  CD1 LEU G 577      40.881 100.462  43.678  1.00 22.44           C  
-ATOM  27963  CD2 LEU G 577      41.671  99.565  41.477  1.00 22.28           C  
-ATOM  27964  N   ASN G 578      45.996  98.243  43.778  1.00 29.00           N  
-ATOM  27965  CA  ASN G 578      47.171  98.190  44.648  1.00 26.41           C  
-ATOM  27966  C   ASN G 578      47.784  96.797  44.792  1.00 32.59           C  
-ATOM  27967  O   ASN G 578      48.245  96.420  45.874  1.00 26.69           O  
-ATOM  27968  CB  ASN G 578      46.811  98.728  46.029  1.00 18.78           C  
-ATOM  27969  CG  ASN G 578      45.968  99.981  45.957  1.00 15.75           C  
-ATOM  27970  OD1 ASN G 578      46.116 100.795  45.044  1.00 22.27           O  
-ATOM  27971  ND2 ASN G 578      45.073 100.142  46.921  1.00 15.85           N  
-ATOM  27972  N   LYS G 579      47.799  96.050  43.693  1.00 33.63           N  
-ATOM  27973  CA  LYS G 579      48.313  94.685  43.691  1.00 31.01           C  
-ATOM  27974  C   LYS G 579      49.703  94.570  44.306  1.00 33.83           C  
-ATOM  27975  O   LYS G 579      49.958  93.661  45.096  1.00 39.90           O  
-ATOM  27976  CB  LYS G 579      48.340  94.133  42.266  1.00 34.50           C  
-ATOM  27977  CG  LYS G 579      46.971  93.990  41.631  1.00 33.34           C  
-ATOM  27978  CD  LYS G 579      46.901  92.734  40.775  1.00 33.99           C  
-ATOM  27979  CE  LYS G 579      45.470  92.429  40.367  1.00 29.65           C  
-ATOM  27980  NZ  LYS G 579      45.356  91.073  39.768  1.00 40.14           N  
-ATOM  27981  N   GLU G 580      50.588  95.498  43.947  1.00 32.13           N  
-ATOM  27982  CA  GLU G 580      51.971  95.487  44.419  1.00 31.02           C  
-ATOM  27983  C   GLU G 580      52.055  95.490  45.940  1.00 30.79           C  
-ATOM  27984  O   GLU G 580      53.013  94.979  46.513  1.00 41.15           O  
-ATOM  27985  CB  GLU G 580      52.745  96.687  43.859  1.00 35.51           C  
-ATOM  27986  CG  GLU G 580      52.087  97.363  42.667  1.00 47.03           C  
-ATOM  27987  CD  GLU G 580      51.012  98.359  43.078  1.00 55.14           C  
-ATOM  27988  OE1 GLU G 580      51.103  98.914  44.197  1.00 43.30           O  
-ATOM  27989  OE2 GLU G 580      50.075  98.586  42.282  1.00 49.24           O  
-ATOM  27990  N   ARG G 581      51.046  96.059  46.591  1.00 30.91           N  
-ATOM  27991  CA  ARG G 581      51.042  96.136  48.046  1.00 23.75           C  
-ATOM  27992  C   ARG G 581      50.530  94.844  48.665  1.00 22.58           C  
-ATOM  27993  O   ARG G 581      50.921  94.477  49.773  1.00 26.07           O  
-ATOM  27994  CB  ARG G 581      50.188  97.312  48.528  1.00 22.60           C  
-ATOM  27995  CG  ARG G 581      50.507  97.759  49.941  1.00 20.71           C  
-ATOM  27996  CD  ARG G 581      49.367  98.544  50.564  1.00 25.55           C  
-ATOM  27997  NE  ARG G 581      48.231  97.689  50.896  1.00 30.19           N  
-ATOM  27998  CZ  ARG G 581      46.997  97.869  50.439  1.00 23.54           C  
-ATOM  27999  NH1 ARG G 581      46.027  97.039  50.799  1.00 21.23           N  
-ATOM  28000  NH2 ARG G 581      46.731  98.880  49.623  1.00 30.35           N  
-ATOM  28001  N   ILE G 582      49.658  94.155  47.940  1.00 25.52           N  
-ATOM  28002  CA  ILE G 582      48.955  93.004  48.488  1.00 25.29           C  
-ATOM  28003  C   ILE G 582      49.675  91.697  48.179  1.00 32.33           C  
-ATOM  28004  O   ILE G 582      49.715  91.256  47.030  1.00 31.54           O  
-ATOM  28005  CB  ILE G 582      47.515  92.937  47.952  1.00 20.86           C  
-ATOM  28006  CG1 ILE G 582      46.805  94.272  48.195  1.00 27.33           C  
-ATOM  28007  CG2 ILE G 582      46.759  91.793  48.602  1.00 19.58           C  
-ATOM  28008  CD1 ILE G 582      45.444  94.377  47.550  1.00 25.42           C  
-ATOM  28009  N   LYS G 583      50.248  91.085  49.212  1.00 31.96           N  
-ATOM  28010  CA  LYS G 583      51.015  89.855  49.047  1.00 22.68           C  
-ATOM  28011  C   LYS G 583      50.412  88.696  49.831  1.00 23.63           C  
-ATOM  28012  O   LYS G 583      50.653  87.531  49.515  1.00 27.07           O  
-ATOM  28013  CB  LYS G 583      52.464  90.078  49.477  1.00 26.81           C  
-ATOM  28014  CG  LYS G 583      53.263  90.944  48.522  1.00 30.86           C  
-ATOM  28015  CD  LYS G 583      54.445  91.591  49.223  1.00 35.94           C  
-ATOM  28016  CE  LYS G 583      55.517  91.982  48.222  1.00 67.88           C  
-ATOM  28017  NZ  LYS G 583      54.932  92.575  46.985  1.00 60.93           N  
-ATOM  28018  N   GLU G 584      49.633  89.018  50.857  1.00 29.13           N  
-ATOM  28019  CA  GLU G 584      48.978  87.994  51.662  1.00 37.06           C  
-ATOM  28020  C   GLU G 584      47.478  88.259  51.764  1.00 30.48           C  
-ATOM  28021  O   GLU G 584      47.026  89.388  51.569  1.00 26.67           O  
-ATOM  28022  CB  GLU G 584      49.607  87.925  53.057  1.00 36.86           C  
-ATOM  28023  CG  GLU G 584      51.119  87.702  53.060  1.00 33.91           C  
-ATOM  28024  CD  GLU G 584      51.522  86.262  52.767  1.00 34.03           C  
-ATOM  28025  OE1 GLU G 584      50.663  85.458  52.344  1.00 34.29           O  
-ATOM  28026  OE2 GLU G 584      52.710  85.931  52.967  1.00 36.30           O  
-ATOM  28027  N   ILE G 585      46.715  87.216  52.078  1.00 28.94           N  
-ATOM  28028  CA  ILE G 585      45.256  87.303  52.089  1.00 24.78           C  
-ATOM  28029  C   ILE G 585      44.741  88.346  53.082  1.00 21.92           C  
-ATOM  28030  O   ILE G 585      43.685  88.945  52.876  1.00 20.61           O  
-ATOM  28031  CB  ILE G 585      44.620  85.930  52.412  1.00 18.64           C  
-ATOM  28032  CG1 ILE G 585      43.096  85.985  52.264  1.00 21.47           C  
-ATOM  28033  CG2 ILE G 585      45.026  85.449  53.802  1.00 22.35           C  
-ATOM  28034  CD1 ILE G 585      42.632  86.342  50.866  1.00 21.95           C  
-ATOM  28035  N   ASP G 586      45.503  88.583  54.144  1.00 21.72           N  
-ATOM  28036  CA  ASP G 586      45.082  89.514  55.181  1.00 19.58           C  
-ATOM  28037  C   ASP G 586      45.401  90.958  54.811  1.00 27.43           C  
-ATOM  28038  O   ASP G 586      45.012  91.886  55.519  1.00 26.98           O  
-ATOM  28039  CB  ASP G 586      45.742  89.154  56.512  1.00 20.51           C  
-ATOM  28040  CG  ASP G 586      45.386  87.756  56.978  1.00 30.56           C  
-ATOM  28041  OD1 ASP G 586      44.326  87.594  57.622  1.00 28.84           O  
-ATOM  28042  OD2 ASP G 586      46.168  86.820  56.697  1.00 24.31           O  
-ATOM  28043  N   ASP G 587      46.101  91.145  53.696  1.00 30.90           N  
-ATOM  28044  CA  ASP G 587      46.531  92.478  53.285  1.00 28.59           C  
-ATOM  28045  C   ASP G 587      45.410  93.290  52.635  1.00 26.59           C  
-ATOM  28046  O   ASP G 587      45.476  94.519  52.591  1.00 25.08           O  
-ATOM  28047  CB  ASP G 587      47.725  92.378  52.330  1.00 30.58           C  
-ATOM  28048  CG  ASP G 587      48.997  91.928  53.031  1.00 38.37           C  
-ATOM  28049  OD1 ASP G 587      48.908  91.458  54.186  1.00 45.56           O  
-ATOM  28050  OD2 ASP G 587      50.087  92.043  52.431  1.00 33.64           O  
-ATOM  28051  N   PHE G 588      44.386  92.607  52.133  1.00 24.17           N  
-ATOM  28052  CA  PHE G 588      43.266  93.274  51.476  1.00 19.71           C  
-ATOM  28053  C   PHE G 588      42.505  94.205  52.415  1.00 21.51           C  
-ATOM  28054  O   PHE G 588      42.375  93.930  53.606  1.00 27.28           O  
-ATOM  28055  CB  PHE G 588      42.298  92.244  50.896  1.00 24.67           C  
-ATOM  28056  CG  PHE G 588      42.792  91.581  49.645  1.00 29.50           C  
-ATOM  28057  CD1 PHE G 588      42.588  92.171  48.409  1.00 20.12           C  
-ATOM  28058  CD2 PHE G 588      43.449  90.362  49.701  1.00 23.49           C  
-ATOM  28059  CE1 PHE G 588      43.034  91.562  47.251  1.00 16.00           C  
-ATOM  28060  CE2 PHE G 588      43.895  89.747  48.546  1.00 22.02           C  
-ATOM  28061  CZ  PHE G 588      43.689  90.350  47.320  1.00 15.12           C  
-ATOM  28062  N   THR G 589      42.010  95.311  51.870  1.00 21.22           N  
-ATOM  28063  CA  THR G 589      41.138  96.212  52.617  1.00 20.41           C  
-ATOM  28064  C   THR G 589      39.910  96.553  51.785  1.00 24.27           C  
-ATOM  28065  O   THR G 589      39.770  96.084  50.655  1.00 31.57           O  
-ATOM  28066  CB  THR G 589      41.853  97.511  53.016  1.00 26.95           C  
-ATOM  28067  OG1 THR G 589      42.230  98.228  51.835  1.00 28.70           O  
-ATOM  28068  CG2 THR G 589      43.093  97.209  53.846  1.00 32.94           C  
-ATOM  28069  N   ALA G 590      39.028  97.377  52.343  1.00 18.89           N  
-ATOM  28070  CA  ALA G 590      37.770  97.717  51.685  1.00 21.24           C  
-ATOM  28071  C   ALA G 590      37.976  98.567  50.431  1.00 33.81           C  
-ATOM  28072  O   ALA G 590      37.161  98.534  49.507  1.00 30.32           O  
-ATOM  28073  CB  ALA G 590      36.854  98.434  52.659  1.00 22.79           C  
-ATOM  28074  N   GLU G 591      39.069  99.321  50.397  1.00 35.13           N  
-ATOM  28075  CA  GLU G 591      39.327 100.244  49.297  1.00 28.17           C  
-ATOM  28076  C   GLU G 591      40.271  99.670  48.249  1.00 23.15           C  
-ATOM  28077  O   GLU G 591      40.808 100.405  47.421  1.00 28.46           O  
-ATOM  28078  CB  GLU G 591      39.897 101.559  49.830  1.00 31.01           C  
-ATOM  28079  CG  GLU G 591      38.887 102.422  50.564  1.00 35.22           C  
-ATOM  28080  CD  GLU G 591      38.574 101.903  51.951  1.00 44.32           C  
-ATOM  28081  OE1 GLU G 591      37.514 102.276  52.499  1.00 50.45           O  
-ATOM  28082  OE2 GLU G 591      39.391 101.126  52.492  1.00 45.80           O  
-ATOM  28083  N   ASP G 592      40.470  98.359  48.279  1.00 19.36           N  
-ATOM  28084  CA  ASP G 592      41.394  97.725  47.349  1.00 23.96           C  
-ATOM  28085  C   ASP G 592      40.665  97.087  46.174  1.00 25.49           C  
-ATOM  28086  O   ASP G 592      41.224  96.250  45.464  1.00 19.58           O  
-ATOM  28087  CB  ASP G 592      42.240  96.680  48.075  1.00 27.40           C  
-ATOM  28088  CG  ASP G 592      43.199  97.300  49.071  1.00 28.49           C  
-ATOM  28089  OD1 ASP G 592      43.878  98.287  48.714  1.00 25.32           O  
-ATOM  28090  OD2 ASP G 592      43.269  96.806  50.214  1.00 34.58           O  
-ATOM  28091  N   PHE G 593      39.418  97.494  45.963  1.00 37.00           N  
-ATOM  28092  CA  PHE G 593      38.606  96.905  44.905  1.00 31.22           C  
-ATOM  28093  C   PHE G 593      37.902  97.957  44.059  1.00 22.48           C  
-ATOM  28094  O   PHE G 593      37.749  99.107  44.471  1.00 22.32           O  
-ATOM  28095  CB  PHE G 593      37.584  95.940  45.505  1.00 27.07           C  
-ATOM  28096  CG  PHE G 593      38.205  94.749  46.169  1.00 19.68           C  
-ATOM  28097  CD1 PHE G 593      38.415  93.579  45.461  1.00 18.09           C  
-ATOM  28098  CD2 PHE G 593      38.596  94.804  47.496  1.00 18.99           C  
-ATOM  28099  CE1 PHE G 593      38.996  92.482  46.065  1.00 22.15           C  
-ATOM  28100  CE2 PHE G 593      39.179  93.710  48.106  1.00 25.27           C  
-ATOM  28101  CZ  PHE G 593      39.376  92.545  47.390  1.00 21.47           C  
-ATOM  28102  N   GLU G 594      37.479  97.546  42.868  1.00 24.62           N  
-ATOM  28103  CA  GLU G 594      36.855  98.460  41.922  1.00 22.98           C  
-ATOM  28104  C   GLU G 594      35.881  97.734  40.994  1.00 25.65           C  
-ATOM  28105  O   GLU G 594      36.299  96.994  40.106  1.00 24.14           O  
-ATOM  28106  CB  GLU G 594      37.931  99.171  41.101  1.00 25.77           C  
-ATOM  28107  CG  GLU G 594      37.402 100.259  40.188  1.00 32.80           C  
-ATOM  28108  CD  GLU G 594      38.437 100.727  39.185  1.00 42.65           C  
-ATOM  28109  OE1 GLU G 594      38.827  99.917  38.316  1.00 41.16           O  
-ATOM  28110  OE2 GLU G 594      38.865 101.898  39.268  1.00 43.16           O  
-ATOM  28111  N   VAL G 595      34.584  97.938  41.202  1.00 26.68           N  
-ATOM  28112  CA  VAL G 595      33.583  97.373  40.303  1.00 18.25           C  
-ATOM  28113  C   VAL G 595      33.401  98.300  39.113  1.00 18.28           C  
-ATOM  28114  O   VAL G 595      33.224  99.507  39.275  1.00 17.43           O  
-ATOM  28115  CB  VAL G 595      32.230  97.154  40.997  1.00 17.59           C  
-ATOM  28116  CG1 VAL G 595      31.223  96.573  40.016  1.00 18.09           C  
-ATOM  28117  CG2 VAL G 595      32.398  96.236  42.180  1.00 20.99           C  
-ATOM  28118  N   VAL G 596      33.438  97.727  37.917  1.00 19.76           N  
-ATOM  28119  CA  VAL G 596      33.523  98.512  36.695  1.00 20.91           C  
-ATOM  28120  C   VAL G 596      32.550  98.033  35.617  1.00 26.85           C  
-ATOM  28121  O   VAL G 596      32.638  96.901  35.142  1.00 22.70           O  
-ATOM  28122  CB  VAL G 596      34.959  98.479  36.135  1.00 17.55           C  
-ATOM  28123  CG1 VAL G 596      34.994  99.019  34.734  1.00 17.64           C  
-ATOM  28124  CG2 VAL G 596      35.897  99.264  37.037  1.00 21.01           C  
-ATOM  28125  N   GLY G 597      31.627  98.905  35.227  1.00 22.16           N  
-ATOM  28126  CA  GLY G 597      30.662  98.574  34.196  1.00 13.42           C  
-ATOM  28127  C   GLY G 597      29.450  97.852  34.748  1.00 16.39           C  
-ATOM  28128  O   GLY G 597      28.778  97.111  34.034  1.00 17.76           O  
-ATOM  28129  N   TYR G 598      29.168  98.061  36.028  1.00 17.42           N  
-ATOM  28130  CA  TYR G 598      27.978  97.482  36.633  1.00 18.22           C  
-ATOM  28131  C   TYR G 598      26.759  98.291  36.230  1.00 18.51           C  
-ATOM  28132  O   TYR G 598      26.586  99.423  36.677  1.00 16.30           O  
-ATOM  28133  CB  TYR G 598      28.095  97.440  38.157  1.00 21.95           C  
-ATOM  28134  CG  TYR G 598      27.100  96.514  38.822  1.00 14.99           C  
-ATOM  28135  CD1 TYR G 598      26.642  95.377  38.170  1.00 19.09           C  
-ATOM  28136  CD2 TYR G 598      26.615  96.778  40.096  1.00 14.41           C  
-ATOM  28137  CE1 TYR G 598      25.735  94.524  38.769  1.00 18.87           C  
-ATOM  28138  CE2 TYR G 598      25.705  95.931  40.704  1.00 17.50           C  
-ATOM  28139  CZ  TYR G 598      25.270  94.804  40.035  1.00 19.60           C  
-ATOM  28140  OH  TYR G 598      24.367  93.950  40.625  1.00 18.90           O  
-ATOM  28141  N   VAL G 599      25.920  97.713  35.376  1.00 21.69           N  
-ATOM  28142  CA  VAL G 599      24.683  98.368  34.962  1.00 16.46           C  
-ATOM  28143  C   VAL G 599      23.479  97.481  35.262  1.00 16.97           C  
-ATOM  28144  O   VAL G 599      22.883  96.920  34.346  1.00 22.85           O  
-ATOM  28145  CB  VAL G 599      24.691  98.706  33.455  1.00 15.41           C  
-ATOM  28146  CG1 VAL G 599      23.791  99.898  33.175  1.00 18.87           C  
-ATOM  28147  CG2 VAL G 599      26.105  98.987  32.973  1.00 17.11           C  
-ATOM  28148  N   PRO G 600      23.117  97.347  36.548  1.00 16.50           N  
-ATOM  28149  CA  PRO G 600      22.023  96.446  36.920  1.00 22.32           C  
-ATOM  28150  C   PRO G 600      20.651  97.097  36.801  1.00 31.19           C  
-ATOM  28151  O   PRO G 600      20.558  98.307  36.581  1.00 34.57           O  
-ATOM  28152  CB  PRO G 600      22.332  96.122  38.379  1.00 16.72           C  
-ATOM  28153  CG  PRO G 600      22.955  97.373  38.888  1.00 17.87           C  
-ATOM  28154  CD  PRO G 600      23.734  97.968  37.733  1.00 15.46           C  
-ATOM  28155  N   HIS G 601      19.598  96.298  36.943  1.00 23.26           N  
-ATOM  28156  CA  HIS G 601      18.250  96.840  37.024  1.00 27.38           C  
-ATOM  28157  C   HIS G 601      18.017  97.412  38.416  1.00 35.53           C  
-ATOM  28158  O   HIS G 601      18.928  97.438  39.244  1.00 50.83           O  
-ATOM  28159  CB  HIS G 601      17.209  95.769  36.709  1.00 25.04           C  
-ATOM  28160  CG  HIS G 601      17.200  95.337  35.277  1.00 22.77           C  
-ATOM  28161  ND1 HIS G 601      16.242  95.755  34.379  1.00 20.82           N  
-ATOM  28162  CD2 HIS G 601      18.033  94.522  34.586  1.00 19.36           C  
-ATOM  28163  CE1 HIS G 601      16.483  95.216  33.198  1.00 20.21           C  
-ATOM  28164  NE2 HIS G 601      17.565  94.464  33.296  1.00 17.06           N  
-ATOM  28165  N   GLY G 602      16.797  97.867  38.677  1.00 31.93           N  
-ATOM  28166  CA  GLY G 602      16.470  98.425  39.975  1.00 51.14           C  
-ATOM  28167  C   GLY G 602      16.465  97.372  41.068  1.00 59.12           C  
-ATOM  28168  O   GLY G 602      16.414  96.175  40.787  1.00 50.21           O  
-ATOM  28169  N   ARG G 603      16.526  97.814  42.321  1.00 67.64           N  
-ATOM  28170  CA  ARG G 603      16.412  96.895  43.447  1.00 61.47           C  
-ATOM  28171  C   ARG G 603      14.999  96.329  43.539  1.00 66.46           C  
-ATOM  28172  O   ARG G 603      14.035  96.956  43.094  1.00 63.79           O  
-ATOM  28173  CB  ARG G 603      16.779  97.586  44.763  1.00 55.11           C  
-ATOM  28174  CG  ARG G 603      18.272  97.766  44.995  1.00 61.08           C  
-ATOM  28175  CD  ARG G 603      18.542  98.222  46.424  1.00 58.28           C  
-ATOM  28176  NE  ARG G 603      19.965  98.423  46.695  1.00 65.52           N  
-ATOM  28177  CZ  ARG G 603      20.779  97.486  47.174  1.00 63.41           C  
-ATOM  28178  NH1 ARG G 603      20.318  96.268  47.435  1.00 41.20           N  
-ATOM  28179  NH2 ARG G 603      22.059  97.766  47.391  1.00 37.07           N  
-ATOM  28180  N   ILE G 604      14.884  95.138  44.114  1.00 65.49           N  
-ATOM  28181  CA  ILE G 604      13.583  94.531  44.360  1.00 68.07           C  
-ATOM  28182  C   ILE G 604      13.448  94.166  45.833  1.00 70.71           C  
-ATOM  28183  O   ILE G 604      14.142  93.277  46.330  1.00 65.38           O  
-ATOM  28184  CB  ILE G 604      13.362  93.278  43.496  1.00 68.16           C  
-ATOM  28185  CG1 ILE G 604      13.227  93.665  42.022  1.00 58.02           C  
-ATOM  28186  CG2 ILE G 604      12.121  92.537  43.954  1.00 63.91           C  
-ATOM  28187  CD1 ILE G 604      12.851  92.505  41.122  1.00 46.22           C  
-ATOM  28188  N   GLN G 605      12.554  94.865  46.524  1.00 72.55           N  
-ATOM  28189  CA  GLN G 605      12.375  94.688  47.960  1.00 72.37           C  
-ATOM  28190  C   GLN G 605      11.855  93.299  48.315  1.00 72.47           C  
-ATOM  28191  O   GLN G 605      10.780  92.893  47.875  1.00 73.52           O  
-ATOM  28192  CB  GLN G 605      11.426  95.754  48.512  1.00 62.04           C  
-ATOM  28193  CG  GLN G 605      12.129  96.878  49.255  1.00 75.89           C  
-ATOM  28194  CD  GLN G 605      12.762  96.411  50.554  1.00 92.35           C  
-ATOM  28195  OE1 GLN G 605      12.282  95.471  51.190  1.00 88.15           O  
-ATOM  28196  NE2 GLN G 605      13.849  97.065  50.953  1.00 85.56           N  
-ATOM  28197  N   MET G 606      12.634  92.578  49.114  1.00 59.16           N  
-ATOM  28198  CA  MET G 606      12.241  91.260  49.594  1.00 60.01           C  
-ATOM  28199  C   MET G 606      12.634  91.090  51.057  1.00 67.77           C  
-ATOM  28200  O   MET G 606      13.819  91.052  51.388  1.00 65.23           O  
-ATOM  28201  CB  MET G 606      12.875  90.158  48.742  1.00 68.82           C  
-ATOM  28202  CG  MET G 606      12.271  90.020  47.350  1.00 71.44           C  
-ATOM  28203  SD  MET G 606      13.078  88.760  46.341  1.00 73.88           S  
-ATOM  28204  CE  MET G 606      14.696  89.493  46.113  1.00 64.40           C  
-ATOM  28205  N   GLU G 607      11.631  90.993  51.925  1.00 77.20           N  
-ATOM  28206  CA  GLU G 607      11.855  90.829  53.358  1.00 67.35           C  
-ATOM  28207  C   GLU G 607      12.628  89.554  53.663  1.00 71.40           C  
-ATOM  28208  O   GLU G 607      12.431  88.525  53.015  1.00 71.42           O  
-ATOM  28209  CB  GLU G 607      10.526  90.810  54.114  1.00 70.91           C  
-ATOM  28210  CG  GLU G 607       9.768  92.125  54.098  1.00 86.23           C  
-ATOM  28211  CD  GLU G 607       8.459  92.049  54.864  1.00104.19           C  
-ATOM  28212  OE1 GLU G 607       7.792  93.096  55.009  1.00107.12           O  
-ATOM  28213  OE2 GLU G 607       8.095  90.942  55.321  1.00 79.56           O  
-ATOM  28214  N   MET G 608      13.506  89.627  54.657  1.00 72.26           N  
-ATOM  28215  CA  MET G 608      14.271  88.462  55.078  1.00 81.49           C  
-ATOM  28216  C   MET G 608      13.416  87.538  55.936  1.00 82.97           C  
-ATOM  28217  O   MET G 608      12.838  87.967  56.937  1.00 76.68           O  
-ATOM  28218  CB  MET G 608      15.521  88.887  55.855  1.00 85.31           C  
-ATOM  28219  CG  MET G 608      16.452  87.735  56.203  1.00 75.34           C  
-ATOM  28220  SD  MET G 608      17.453  88.048  57.671  1.00 74.42           S  
-ATOM  28221  CE  MET G 608      18.215  89.610  57.243  1.00 88.28           C  
-ATOM  28222  N   ALA G 609      13.332  86.272  55.536  1.00 81.57           N  
-ATOM  28223  CA  ALA G 609      12.671  85.268  56.357  1.00 78.23           C  
-ATOM  28224  C   ALA G 609      13.407  85.152  57.688  1.00 84.83           C  
-ATOM  28225  O   ALA G 609      14.430  84.472  57.794  1.00 87.23           O  
-ATOM  28226  CB  ALA G 609      12.626  83.932  55.642  1.00 71.40           C  
-ATOM  28227  N   VAL G 610      12.872  85.837  58.694  1.00 81.62           N  
-ATOM  28228  CA  VAL G 610      13.504  85.981  60.003  1.00 74.49           C  
-ATOM  28229  C   VAL G 610      13.767  84.667  60.735  1.00 67.10           C  
-ATOM  28230  O   VAL G 610      14.352  84.663  61.820  1.00 62.94           O  
-ATOM  28231  CB  VAL G 610      12.643  86.875  60.913  1.00 72.13           C  
-ATOM  28232  CG1 VAL G 610      12.943  88.343  60.648  1.00 69.27           C  
-ATOM  28233  CG2 VAL G 610      11.163  86.570  60.698  1.00 76.12           C  
-ATOM  28234  OXT VAL G 610      13.408  83.582  60.283  1.00 64.26           O  
-TER   28235      VAL G 610                                                      
-ATOM  28236  N   LYS H   3       7.860  46.892   3.364  1.00 78.56           N  
-ATOM  28237  CA  LYS H   3       7.331  45.789   4.163  1.00 85.42           C  
-ATOM  28238  C   LYS H   3       8.168  45.490   5.413  1.00 89.46           C  
-ATOM  28239  O   LYS H   3       8.566  44.342   5.627  1.00 71.81           O  
-ATOM  28240  CB  LYS H   3       7.244  44.523   3.306  1.00 86.98           C  
-ATOM  28241  CG  LYS H   3       6.692  44.744   1.905  1.00 74.04           C  
-ATOM  28242  CD  LYS H   3       7.623  44.169   0.846  1.00 64.33           C  
-ATOM  28243  CE  LYS H   3       8.854  45.041   0.658  1.00 54.98           C  
-ATOM  28244  NZ  LYS H   3       8.493  46.394   0.145  1.00 50.98           N  
-ATOM  28245  N   PRO H   4       8.438  46.510   6.249  1.00 93.08           N  
-ATOM  28246  CA  PRO H   4       9.276  46.228   7.420  1.00 77.70           C  
-ATOM  28247  C   PRO H   4       8.492  45.540   8.537  1.00 76.08           C  
-ATOM  28248  O   PRO H   4       7.282  45.731   8.653  1.00 78.71           O  
-ATOM  28249  CB  PRO H   4       9.749  47.624   7.862  1.00 72.66           C  
-ATOM  28250  CG  PRO H   4       9.307  48.577   6.761  1.00 68.87           C  
-ATOM  28251  CD  PRO H   4       8.095  47.938   6.174  1.00 77.05           C  
-ATOM  28252  N   VAL H   5       9.183  44.743   9.345  1.00 72.17           N  
-ATOM  28253  CA  VAL H   5       8.553  44.027  10.451  1.00 57.85           C  
-ATOM  28254  C   VAL H   5       9.270  44.348  11.762  1.00 64.47           C  
-ATOM  28255  O   VAL H   5      10.487  44.536  11.778  1.00 66.02           O  
-ATOM  28256  CB  VAL H   5       8.567  42.500  10.212  1.00 52.52           C  
-ATOM  28257  CG1 VAL H   5       7.758  41.778  11.275  1.00 49.87           C  
-ATOM  28258  CG2 VAL H   5       8.036  42.176   8.827  1.00 64.66           C  
-ATOM  28259  N   CYS H   6       8.517  44.425  12.856  1.00 59.85           N  
-ATOM  28260  CA  CYS H   6       9.105  44.646  14.174  1.00 53.80           C  
-ATOM  28261  C   CYS H   6       8.655  43.582  15.169  1.00 52.14           C  
-ATOM  28262  O   CYS H   6       7.478  43.225  15.211  1.00 50.63           O  
-ATOM  28263  CB  CYS H   6       8.744  46.036  14.701  1.00 52.90           C  
-ATOM  28264  SG  CYS H   6       9.551  47.394  13.827  1.00 77.11           S  
-ATOM  28265  N   LEU H   7       9.596  43.078  15.965  1.00 50.81           N  
-ATOM  28266  CA  LEU H   7       9.282  42.085  16.990  1.00 43.20           C  
-ATOM  28267  C   LEU H   7       9.153  42.736  18.365  1.00 43.96           C  
-ATOM  28268  O   LEU H   7      10.011  43.520  18.770  1.00 41.50           O  
-ATOM  28269  CB  LEU H   7      10.351  40.991  17.036  1.00 25.48           C  
-ATOM  28270  CG  LEU H   7      10.681  40.249  15.739  1.00 35.93           C  
-ATOM  28271  CD1 LEU H   7      11.505  38.998  16.025  1.00 28.18           C  
-ATOM  28272  CD2 LEU H   7       9.419  39.898  14.974  1.00 44.11           C  
-ATOM  28273  N   VAL H   8       8.078  42.410  19.077  1.00 38.84           N  
-ATOM  28274  CA  VAL H   8       7.865  42.935  20.422  1.00 37.62           C  
-ATOM  28275  C   VAL H   8       7.925  41.808  21.452  1.00 46.01           C  
-ATOM  28276  O   VAL H   8       7.100  40.892  21.432  1.00 44.22           O  
-ATOM  28277  CB  VAL H   8       6.518  43.669  20.539  1.00 33.59           C  
-ATOM  28278  CG1 VAL H   8       6.388  44.313  21.909  1.00 40.62           C  
-ATOM  28279  CG2 VAL H   8       6.395  44.719  19.449  1.00 39.55           C  
-ATOM  28280  N   VAL H   9       8.903  41.885  22.351  1.00 42.43           N  
-ATOM  28281  CA  VAL H   9       9.180  40.798  23.288  1.00 35.10           C  
-ATOM  28282  C   VAL H   9       9.457  41.261  24.714  1.00 34.16           C  
-ATOM  28283  O   VAL H   9       9.858  42.401  24.946  1.00 43.07           O  
-ATOM  28284  CB  VAL H   9      10.398  39.974  22.839  1.00 34.68           C  
-ATOM  28285  CG1 VAL H   9      10.005  38.952  21.800  1.00 40.29           C  
-ATOM  28286  CG2 VAL H   9      11.475  40.891  22.305  1.00 37.32           C  
-ATOM  28287  N   ALA H  10       9.247  40.352  25.660  1.00 32.73           N  
-ATOM  28288  CA  ALA H  10       9.676  40.536  27.041  1.00 30.39           C  
-ATOM  28289  C   ALA H  10      10.363  39.257  27.508  1.00 38.59           C  
-ATOM  28290  O   ALA H  10       9.706  38.238  27.724  1.00 41.41           O  
-ATOM  28291  CB  ALA H  10       8.498  40.881  27.936  1.00 32.02           C  
-ATOM  28292  N   MET H  11      11.684  39.308  27.656  1.00 30.57           N  
-ATOM  28293  CA  MET H  11      12.461  38.102  27.926  1.00 20.33           C  
-ATOM  28294  C   MET H  11      13.447  38.242  29.090  1.00 25.20           C  
-ATOM  28295  O   MET H  11      13.949  39.330  29.374  1.00 32.59           O  
-ATOM  28296  CB  MET H  11      13.220  37.687  26.665  1.00 17.80           C  
-ATOM  28297  CG  MET H  11      14.299  38.670  26.247  1.00 24.90           C  
-ATOM  28298  SD  MET H  11      15.177  38.168  24.755  1.00 38.01           S  
-ATOM  28299  CE  MET H  11      13.980  38.581  23.493  1.00 29.18           C  
-ATOM  28300  N   THR H  12      13.715  37.119  29.752  1.00 25.01           N  
-ATOM  28301  CA  THR H  12      14.705  37.035  30.824  1.00 21.06           C  
-ATOM  28302  C   THR H  12      16.116  37.068  30.218  1.00 26.00           C  
-ATOM  28303  O   THR H  12      16.250  37.045  28.994  1.00 23.89           O  
-ATOM  28304  CB  THR H  12      14.498  35.750  31.657  1.00 19.03           C  
-ATOM  28305  OG1 THR H  12      15.066  34.626  30.973  1.00 21.26           O  
-ATOM  28306  CG2 THR H  12      13.017  35.505  31.893  1.00 19.67           C  
-ATOM  28307  N   PRO H  13      17.175  37.145  31.055  1.00 31.24           N  
-ATOM  28308  CA  PRO H  13      18.506  37.146  30.430  1.00 26.95           C  
-ATOM  28309  C   PRO H  13      18.833  35.851  29.694  1.00 22.00           C  
-ATOM  28310  O   PRO H  13      19.640  35.873  28.767  1.00 20.98           O  
-ATOM  28311  CB  PRO H  13      19.453  37.339  31.618  1.00 25.84           C  
-ATOM  28312  CG  PRO H  13      18.635  38.017  32.641  1.00 28.94           C  
-ATOM  28313  CD  PRO H  13      17.262  37.433  32.498  1.00 25.35           C  
-ATOM  28314  N   LYS H  14      18.214  34.745  30.096  1.00 22.74           N  
-ATOM  28315  CA  LYS H  14      18.409  33.473  29.411  1.00 23.59           C  
-ATOM  28316  C   LYS H  14      17.418  33.319  28.258  1.00 30.22           C  
-ATOM  28317  O   LYS H  14      17.145  32.204  27.807  1.00 22.44           O  
-ATOM  28318  CB  LYS H  14      18.271  32.304  30.386  1.00 21.83           C  
-ATOM  28319  CG  LYS H  14      19.408  32.182  31.389  1.00 23.70           C  
-ATOM  28320  CD  LYS H  14      19.189  30.991  32.317  1.00 36.12           C  
-ATOM  28321  CE  LYS H  14      20.354  30.796  33.273  1.00 34.26           C  
-ATOM  28322  NZ  LYS H  14      20.154  29.613  34.155  1.00 25.55           N  
-ATOM  28323  N   ARG H  15      16.882  34.451  27.802  1.00 27.31           N  
-ATOM  28324  CA  ARG H  15      15.976  34.522  26.655  1.00 23.62           C  
-ATOM  28325  C   ARG H  15      14.661  33.775  26.867  1.00 27.22           C  
-ATOM  28326  O   ARG H  15      13.977  33.433  25.903  1.00 41.30           O  
-ATOM  28327  CB  ARG H  15      16.671  33.995  25.393  1.00 24.84           C  
-ATOM  28328  CG  ARG H  15      17.901  34.780  24.992  1.00 23.82           C  
-ATOM  28329  CD  ARG H  15      18.439  34.344  23.636  1.00 27.19           C  
-ATOM  28330  NE  ARG H  15      19.398  33.249  23.747  1.00 27.34           N  
-ATOM  28331  CZ  ARG H  15      19.104  31.970  23.541  1.00 29.42           C  
-ATOM  28332  NH1 ARG H  15      20.046  31.045  23.668  1.00 28.74           N  
-ATOM  28333  NH2 ARG H  15      17.872  31.614  23.207  1.00 30.10           N  
-ATOM  28334  N   GLY H  16      14.303  33.532  28.123  1.00 21.67           N  
-ATOM  28335  CA  GLY H  16      13.051  32.863  28.431  1.00 22.67           C  
-ATOM  28336  C   GLY H  16      11.872  33.801  28.272  1.00 21.21           C  
-ATOM  28337  O   GLY H  16      11.955  34.965  28.659  1.00 24.30           O  
-ATOM  28338  N   ILE H  17      10.772  33.309  27.706  1.00 27.12           N  
-ATOM  28339  CA  ILE H  17       9.609  34.164  27.472  1.00 23.38           C  
-ATOM  28340  C   ILE H  17       8.298  33.604  28.018  1.00 28.68           C  
-ATOM  28341  O   ILE H  17       7.320  34.340  28.149  1.00 35.23           O  
-ATOM  28342  CB  ILE H  17       9.413  34.445  25.972  1.00 25.39           C  
-ATOM  28343  CG1 ILE H  17       9.258  33.137  25.197  1.00 32.53           C  
-ATOM  28344  CG2 ILE H  17      10.573  35.262  25.429  1.00 34.73           C  
-ATOM  28345  CD1 ILE H  17       8.930  33.332  23.728  1.00 44.72           C  
-ATOM  28346  N   GLY H  18       8.264  32.313  28.331  1.00 31.15           N  
-ATOM  28347  CA  GLY H  18       7.032  31.713  28.811  1.00 34.21           C  
-ATOM  28348  C   GLY H  18       7.159  30.370  29.503  1.00 32.09           C  
-ATOM  28349  O   GLY H  18       8.210  29.728  29.466  1.00 28.90           O  
-ATOM  28350  N   ILE H  19       6.069  29.950  30.138  1.00 37.16           N  
-ATOM  28351  CA  ILE H  19       5.998  28.646  30.784  1.00 36.52           C  
-ATOM  28352  C   ILE H  19       4.537  28.254  31.028  1.00 33.79           C  
-ATOM  28353  O   ILE H  19       3.728  29.073  31.472  1.00 30.12           O  
-ATOM  28354  CB  ILE H  19       6.795  28.629  32.110  1.00 25.85           C  
-ATOM  28355  CG1 ILE H  19       6.750  27.241  32.753  1.00 24.66           C  
-ATOM  28356  CG2 ILE H  19       6.300  29.715  33.057  1.00 23.45           C  
-ATOM  28357  CD1 ILE H  19       7.661  27.096  33.950  1.00 20.07           C  
-ATOM  28358  N   ASN H  20       4.211  27.002  30.715  1.00 29.69           N  
-ATOM  28359  CA  ASN H  20       2.841  26.496  30.783  1.00 35.12           C  
-ATOM  28360  C   ASN H  20       1.866  27.387  30.021  1.00 38.32           C  
-ATOM  28361  O   ASN H  20       0.783  27.707  30.517  1.00 34.95           O  
-ATOM  28362  CB  ASN H  20       2.389  26.348  32.239  1.00 36.39           C  
-ATOM  28363  CG  ASN H  20       3.097  25.215  32.955  1.00 35.04           C  
-ATOM  28364  OD1 ASN H  20       3.563  24.263  32.327  1.00 35.68           O  
-ATOM  28365  ND2 ASN H  20       3.178  25.309  34.277  1.00 31.93           N  
-ATOM  28366  N   ASN H  21       2.269  27.779  28.814  1.00 39.63           N  
-ATOM  28367  CA  ASN H  21       1.481  28.661  27.958  1.00 36.20           C  
-ATOM  28368  C   ASN H  21       1.037  29.925  28.688  1.00 40.72           C  
-ATOM  28369  O   ASN H  21      -0.116  30.348  28.582  1.00 48.11           O  
-ATOM  28370  CB  ASN H  21       0.269  27.916  27.401  1.00 39.90           C  
-ATOM  28371  CG  ASN H  21       0.012  28.239  25.948  1.00 59.72           C  
-ATOM  28372  OD1 ASN H  21       0.747  27.797  25.065  1.00 62.65           O  
-ATOM  28373  ND2 ASN H  21      -1.039  29.010  25.687  1.00 68.71           N  
-ATOM  28374  N   GLY H  22       1.965  30.514  29.436  1.00 36.21           N  
-ATOM  28375  CA  GLY H  22       1.701  31.725  30.187  1.00 32.42           C  
-ATOM  28376  C   GLY H  22       2.980  32.507  30.398  1.00 26.96           C  
-ATOM  28377  O   GLY H  22       3.999  32.213  29.778  1.00 30.47           O  
-ATOM  28378  N   LEU H  23       2.934  33.501  31.277  1.00 22.38           N  
-ATOM  28379  CA  LEU H  23       4.093  34.351  31.516  1.00 24.17           C  
-ATOM  28380  C   LEU H  23       4.875  33.901  32.745  1.00 23.74           C  
-ATOM  28381  O   LEU H  23       4.285  33.568  33.773  1.00 28.23           O  
-ATOM  28382  CB  LEU H  23       3.657  35.808  31.666  1.00 30.21           C  
-ATOM  28383  CG  LEU H  23       3.024  36.398  30.406  1.00 19.70           C  
-ATOM  28384  CD1 LEU H  23       2.550  37.822  30.650  1.00 30.54           C  
-ATOM  28385  CD2 LEU H  23       4.012  36.343  29.254  1.00 19.27           C  
-ATOM  28386  N   PRO H  24       6.213  33.898  32.638  1.00 20.81           N  
-ATOM  28387  CA  PRO H  24       7.123  33.424  33.685  1.00 28.60           C  
-ATOM  28388  C   PRO H  24       7.094  34.312  34.920  1.00 25.90           C  
-ATOM  28389  O   PRO H  24       7.160  33.823  36.049  1.00 22.07           O  
-ATOM  28390  CB  PRO H  24       8.503  33.494  33.015  1.00 23.11           C  
-ATOM  28391  CG  PRO H  24       8.241  33.695  31.562  1.00 22.30           C  
-ATOM  28392  CD  PRO H  24       6.949  34.421  31.478  1.00 24.14           C  
-ATOM  28393  N   TRP H  25       6.992  35.614  34.685  1.00 20.44           N  
-ATOM  28394  CA  TRP H  25       7.091  36.617  35.736  1.00 20.54           C  
-ATOM  28395  C   TRP H  25       5.720  37.169  36.113  1.00 22.25           C  
-ATOM  28396  O   TRP H  25       4.780  37.090  35.322  1.00 23.19           O  
-ATOM  28397  CB  TRP H  25       8.016  37.748  35.277  1.00 23.69           C  
-ATOM  28398  CG  TRP H  25       8.171  37.789  33.786  1.00 32.72           C  
-ATOM  28399  CD1 TRP H  25       9.190  37.249  33.050  1.00 39.12           C  
-ATOM  28400  CD2 TRP H  25       7.271  38.380  32.847  1.00 28.78           C  
-ATOM  28401  NE1 TRP H  25       8.983  37.476  31.710  1.00 22.83           N  
-ATOM  28402  CE2 TRP H  25       7.808  38.170  31.559  1.00 34.33           C  
-ATOM  28403  CE3 TRP H  25       6.061  39.074  32.967  1.00 33.82           C  
-ATOM  28404  CZ2 TRP H  25       7.181  38.626  30.405  1.00 50.81           C  
-ATOM  28405  CZ3 TRP H  25       5.439  39.528  31.818  1.00 44.64           C  
-ATOM  28406  CH2 TRP H  25       5.999  39.302  30.555  1.00 58.88           C  
-ATOM  28407  N   PRO H  26       5.597  37.725  37.329  1.00 14.77           N  
-ATOM  28408  CA  PRO H  26       4.363  38.416  37.710  1.00 14.06           C  
-ATOM  28409  C   PRO H  26       4.097  39.632  36.824  1.00 30.95           C  
-ATOM  28410  O   PRO H  26       4.935  39.984  35.991  1.00 32.62           O  
-ATOM  28411  CB  PRO H  26       4.624  38.834  39.158  1.00 15.92           C  
-ATOM  28412  CG  PRO H  26       6.107  38.802  39.311  1.00 20.99           C  
-ATOM  28413  CD  PRO H  26       6.563  37.682  38.439  1.00 18.06           C  
-ATOM  28414  N   HIS H  27       2.945  40.267  37.013  1.00 30.12           N  
-ATOM  28415  CA  HIS H  27       2.480  41.306  36.101  1.00 26.76           C  
-ATOM  28416  C   HIS H  27       3.412  42.516  36.038  1.00 35.34           C  
-ATOM  28417  O   HIS H  27       3.725  43.124  37.062  1.00 35.32           O  
-ATOM  28418  CB  HIS H  27       1.077  41.761  36.502  1.00 27.95           C  
-ATOM  28419  CG  HIS H  27       0.328  42.444  35.400  1.00 29.99           C  
-ATOM  28420  ND1 HIS H  27       0.317  43.814  35.244  1.00 31.13           N  
-ATOM  28421  CD2 HIS H  27      -0.429  41.945  34.396  1.00 28.98           C  
-ATOM  28422  CE1 HIS H  27      -0.419  44.128  34.193  1.00 34.81           C  
-ATOM  28423  NE2 HIS H  27      -0.884  43.013  33.661  1.00 38.85           N  
-ATOM  28424  N   LEU H  28       3.845  42.857  34.825  1.00 36.49           N  
-ATOM  28425  CA  LEU H  28       4.693  44.027  34.597  1.00 30.35           C  
-ATOM  28426  C   LEU H  28       3.903  45.166  33.944  1.00 32.55           C  
-ATOM  28427  O   LEU H  28       3.823  45.274  32.714  1.00 41.38           O  
-ATOM  28428  CB  LEU H  28       5.900  43.652  33.739  1.00 29.61           C  
-ATOM  28429  CG  LEU H  28       6.742  42.484  34.257  1.00 30.59           C  
-ATOM  28430  CD1 LEU H  28       7.913  42.214  33.326  1.00 26.72           C  
-ATOM  28431  CD2 LEU H  28       7.228  42.757  35.669  1.00 24.55           C  
-ATOM  28432  N   THR H  29       3.335  46.015  34.795  1.00 31.55           N  
-ATOM  28433  CA  THR H  29       2.413  47.069  34.387  1.00 33.32           C  
-ATOM  28434  C   THR H  29       3.000  48.005  33.339  1.00 34.68           C  
-ATOM  28435  O   THR H  29       2.405  48.206  32.275  1.00 41.04           O  
-ATOM  28436  CB  THR H  29       1.973  47.910  35.594  1.00 31.64           C  
-ATOM  28437  OG1 THR H  29       1.513  47.044  36.638  1.00 29.87           O  
-ATOM  28438  CG2 THR H  29       0.864  48.868  35.197  1.00 35.37           C  
-ATOM  28439  N   THR H  30       4.160  48.579  33.645  1.00 26.57           N  
-ATOM  28440  CA  THR H  30       4.805  49.523  32.740  1.00 31.84           C  
-ATOM  28441  C   THR H  30       5.163  48.848  31.424  1.00 34.30           C  
-ATOM  28442  O   THR H  30       5.120  49.468  30.365  1.00 36.91           O  
-ATOM  28443  CB  THR H  30       6.072  50.133  33.370  1.00 30.67           C  
-ATOM  28444  OG1 THR H  30       5.742  50.727  34.632  1.00 37.51           O  
-ATOM  28445  CG2 THR H  30       6.670  51.194  32.460  1.00 40.10           C  
-ATOM  28446  N   ASP H  31       5.509  47.568  31.496  1.00 42.24           N  
-ATOM  28447  CA  ASP H  31       5.783  46.790  30.295  1.00 32.65           C  
-ATOM  28448  C   ASP H  31       4.530  46.668  29.442  1.00 34.12           C  
-ATOM  28449  O   ASP H  31       4.599  46.757  28.220  1.00 43.96           O  
-ATOM  28450  CB  ASP H  31       6.309  45.402  30.650  1.00 30.31           C  
-ATOM  28451  CG  ASP H  31       6.395  44.485  29.446  1.00 34.17           C  
-ATOM  28452  OD1 ASP H  31       6.970  44.893  28.416  1.00 28.71           O  
-ATOM  28453  OD2 ASP H  31       5.875  43.353  29.534  1.00 44.93           O  
-ATOM  28454  N   PHE H  32       3.382  46.468  30.083  1.00 40.25           N  
-ATOM  28455  CA  PHE H  32       2.133  46.372  29.333  1.00 43.12           C  
-ATOM  28456  C   PHE H  32       1.738  47.712  28.717  1.00 38.52           C  
-ATOM  28457  O   PHE H  32       1.266  47.757  27.577  1.00 37.52           O  
-ATOM  28458  CB  PHE H  32       1.007  45.841  30.219  1.00 42.33           C  
-ATOM  28459  CG  PHE H  32       0.867  44.347  30.176  1.00 45.33           C  
-ATOM  28460  CD1 PHE H  32       0.370  43.720  29.046  1.00 57.35           C  
-ATOM  28461  CD2 PHE H  32       1.241  43.568  31.257  1.00 48.25           C  
-ATOM  28462  CE1 PHE H  32       0.245  42.343  28.996  1.00 51.50           C  
-ATOM  28463  CE2 PHE H  32       1.116  42.189  31.214  1.00 53.49           C  
-ATOM  28464  CZ  PHE H  32       0.617  41.577  30.081  1.00 35.91           C  
-ATOM  28465  N   LYS H  33       1.923  48.795  29.467  1.00 40.03           N  
-ATOM  28466  CA  LYS H  33       1.672  50.133  28.936  1.00 48.82           C  
-ATOM  28467  C   LYS H  33       2.549  50.375  27.712  1.00 52.79           C  
-ATOM  28468  O   LYS H  33       2.095  50.889  26.692  1.00 61.43           O  
-ATOM  28469  CB  LYS H  33       1.937  51.202  30.002  1.00 40.78           C  
-ATOM  28470  CG  LYS H  33       0.930  51.229  31.146  1.00 52.00           C  
-ATOM  28471  CD  LYS H  33       1.342  52.248  32.204  1.00 53.30           C  
-ATOM  28472  CE  LYS H  33       0.410  52.214  33.407  1.00 64.13           C  
-ATOM  28473  NZ  LYS H  33       0.901  53.071  34.524  1.00 37.28           N  
-ATOM  28474  N   HIS H  34       3.812  49.984  27.840  1.00 51.85           N  
-ATOM  28475  CA  HIS H  34       4.799  50.064  26.770  1.00 55.86           C  
-ATOM  28476  C   HIS H  34       4.344  49.303  25.528  1.00 49.68           C  
-ATOM  28477  O   HIS H  34       4.383  49.838  24.419  1.00 52.57           O  
-ATOM  28478  CB  HIS H  34       6.147  49.521  27.262  1.00 50.79           C  
-ATOM  28479  CG  HIS H  34       7.107  49.178  26.164  1.00 47.87           C  
-ATOM  28480  ND1 HIS H  34       7.910  50.118  25.555  1.00 56.57           N  
-ATOM  28481  CD2 HIS H  34       7.406  47.993  25.580  1.00 45.54           C  
-ATOM  28482  CE1 HIS H  34       8.656  49.529  24.637  1.00 57.28           C  
-ATOM  28483  NE2 HIS H  34       8.369  48.239  24.632  1.00 57.33           N  
-ATOM  28484  N   PHE H  35       3.920  48.057  25.726  1.00 43.56           N  
-ATOM  28485  CA  PHE H  35       3.414  47.213  24.650  1.00 43.74           C  
-ATOM  28486  C   PHE H  35       2.253  47.892  23.933  1.00 48.84           C  
-ATOM  28487  O   PHE H  35       2.271  48.069  22.711  1.00 53.37           O  
-ATOM  28488  CB  PHE H  35       2.978  45.853  25.213  1.00 42.74           C  
-ATOM  28489  CG  PHE H  35       2.395  44.917  24.185  1.00 43.53           C  
-ATOM  28490  CD1 PHE H  35       1.025  44.853  23.981  1.00 47.54           C  
-ATOM  28491  CD2 PHE H  35       3.215  44.093  23.434  1.00 42.56           C  
-ATOM  28492  CE1 PHE H  35       0.486  43.990  23.036  1.00 45.51           C  
-ATOM  28493  CE2 PHE H  35       2.685  43.231  22.492  1.00 42.23           C  
-ATOM  28494  CZ  PHE H  35       1.319  43.178  22.292  1.00 41.29           C  
-ATOM  28495  N   SER H  36       1.250  48.276  24.715  1.00 50.17           N  
-ATOM  28496  CA  SER H  36       0.037  48.883  24.183  1.00 63.16           C  
-ATOM  28497  C   SER H  36       0.338  50.152  23.396  1.00 66.91           C  
-ATOM  28498  O   SER H  36      -0.222  50.366  22.325  1.00 73.38           O  
-ATOM  28499  CB  SER H  36      -0.946  49.191  25.316  1.00 64.57           C  
-ATOM  28500  OG  SER H  36      -2.270  48.816  24.963  1.00 58.93           O  
-ATOM  28501  N   ARG H  37       1.223  50.987  23.928  1.00 55.99           N  
-ATOM  28502  CA  ARG H  37       1.568  52.241  23.270  1.00 54.00           C  
-ATOM  28503  C   ARG H  37       2.353  52.017  21.984  1.00 46.76           C  
-ATOM  28504  O   ARG H  37       2.089  52.658  20.967  1.00 52.84           O  
-ATOM  28505  CB  ARG H  37       2.364  53.134  24.218  1.00 64.94           C  
-ATOM  28506  CG  ARG H  37       1.611  54.375  24.654  1.00 78.39           C  
-ATOM  28507  CD  ARG H  37       0.313  54.014  25.350  1.00 82.68           C  
-ATOM  28508  NE  ARG H  37       0.213  54.666  26.651  1.00 89.96           N  
-ATOM  28509  CZ  ARG H  37      -0.196  55.917  26.828  1.00 92.41           C  
-ATOM  28510  NH1 ARG H  37      -0.251  56.432  28.049  1.00 90.69           N  
-ATOM  28511  NH2 ARG H  37      -0.549  56.655  25.783  1.00 83.75           N  
-ATOM  28512  N   VAL H  38       3.317  51.105  22.035  1.00 53.55           N  
-ATOM  28513  CA  VAL H  38       4.140  50.801  20.870  1.00 55.04           C  
-ATOM  28514  C   VAL H  38       3.322  50.200  19.729  1.00 52.55           C  
-ATOM  28515  O   VAL H  38       3.462  50.607  18.578  1.00 54.84           O  
-ATOM  28516  CB  VAL H  38       5.289  49.829  21.225  1.00 48.11           C  
-ATOM  28517  CG1 VAL H  38       5.887  49.217  19.964  1.00 46.23           C  
-ATOM  28518  CG2 VAL H  38       6.359  50.541  22.034  1.00 38.92           C  
-ATOM  28519  N   THR H  39       2.455  49.246  20.047  1.00 49.02           N  
-ATOM  28520  CA  THR H  39       1.768  48.498  19.000  1.00 51.60           C  
-ATOM  28521  C   THR H  39       0.691  49.303  18.266  1.00 63.04           C  
-ATOM  28522  O   THR H  39       0.145  48.826  17.271  1.00 70.09           O  
-ATOM  28523  CB  THR H  39       1.124  47.213  19.553  1.00 53.61           C  
-ATOM  28524  OG1 THR H  39       0.689  47.426  20.901  1.00 63.05           O  
-ATOM  28525  CG2 THR H  39       2.124  46.064  19.527  1.00 43.45           C  
-ATOM  28526  N   LYS H  40       0.388  50.515  18.727  1.00 62.26           N  
-ATOM  28527  CA  LYS H  40      -0.601  51.332  18.024  1.00 61.68           C  
-ATOM  28528  C   LYS H  40      -0.173  52.788  17.826  1.00 67.12           C  
-ATOM  28529  O   LYS H  40       0.326  53.441  18.744  1.00 62.14           O  
-ATOM  28530  CB  LYS H  40      -1.945  51.288  18.755  1.00 62.85           C  
-ATOM  28531  CG  LYS H  40      -1.930  51.860  20.157  1.00 70.49           C  
-ATOM  28532  CD  LYS H  40      -3.288  52.432  20.526  1.00 78.15           C  
-ATOM  28533  CE  LYS H  40      -3.447  52.555  22.032  1.00 68.27           C  
-ATOM  28534  NZ  LYS H  40      -2.330  53.316  22.658  1.00 73.57           N  
-ATOM  28535  N   THR H  41      -0.369  53.277  16.604  1.00 90.13           N  
-ATOM  28536  CA  THR H  41      -0.149  54.682  16.267  1.00 96.80           C  
-ATOM  28537  C   THR H  41      -0.882  55.050  14.978  1.00 87.54           C  
-ATOM  28538  O   THR H  41      -0.562  54.543  13.900  1.00 76.72           O  
-ATOM  28539  CB  THR H  41       1.352  55.020  16.101  1.00 80.81           C  
-ATOM  28540  OG1 THR H  41       2.143  53.839  16.284  1.00 78.68           O  
-ATOM  28541  CG2 THR H  41       1.772  56.072  17.116  1.00 64.56           C  
-ATOM  28542  N   PHE H  74      -4.516  52.260  11.075  1.00 73.41           N  
-ATOM  28543  CA  PHE H  74      -4.255  51.414  12.235  1.00 83.59           C  
-ATOM  28544  C   PHE H  74      -3.035  50.520  12.021  1.00 87.60           C  
-ATOM  28545  O   PHE H  74      -2.557  50.366  10.898  1.00 87.14           O  
-ATOM  28546  CB  PHE H  74      -5.482  50.556  12.557  1.00 82.40           C  
-ATOM  28547  CG  PHE H  74      -6.075  49.863  11.360  1.00 89.59           C  
-ATOM  28548  CD1 PHE H  74      -5.466  48.743  10.814  1.00 85.30           C  
-ATOM  28549  CD2 PHE H  74      -7.248  50.325  10.788  1.00 96.70           C  
-ATOM  28550  CE1 PHE H  74      -6.011  48.105   9.715  1.00 93.23           C  
-ATOM  28551  CE2 PHE H  74      -7.799  49.689   9.690  1.00101.19           C  
-ATOM  28552  CZ  PHE H  74      -7.179  48.578   9.154  1.00104.27           C  
-ATOM  28553  N   ASN H  75      -2.540  49.930  13.105  1.00 79.69           N  
-ATOM  28554  CA  ASN H  75      -1.408  49.013  13.029  1.00 71.36           C  
-ATOM  28555  C   ASN H  75      -1.852  47.552  13.035  1.00 71.11           C  
-ATOM  28556  O   ASN H  75      -3.036  47.250  13.200  1.00 69.20           O  
-ATOM  28557  CB  ASN H  75      -0.433  49.268  14.181  1.00 66.21           C  
-ATOM  28558  CG  ASN H  75       0.535  50.400  13.887  1.00 74.32           C  
-ATOM  28559  OD1 ASN H  75       0.964  50.583  12.749  1.00 81.87           O  
-ATOM  28560  ND2 ASN H  75       0.889  51.160  14.915  1.00 67.22           N  
-ATOM  28561  N   ALA H  76      -0.896  46.648  12.852  1.00 65.54           N  
-ATOM  28562  CA  ALA H  76      -1.200  45.223  12.801  1.00 66.30           C  
-ATOM  28563  C   ALA H  76      -0.360  44.425  13.792  1.00 66.83           C  
-ATOM  28564  O   ALA H  76       0.805  44.741  14.035  1.00 64.19           O  
-ATOM  28565  CB  ALA H  76      -0.995  44.691  11.389  1.00 65.52           C  
-ATOM  28566  N   VAL H  77      -0.969  43.392  14.364  1.00 65.87           N  
-ATOM  28567  CA  VAL H  77      -0.279  42.467  15.253  1.00 56.91           C  
-ATOM  28568  C   VAL H  77      -0.440  41.032  14.747  1.00 54.33           C  
-ATOM  28569  O   VAL H  77      -1.516  40.637  14.293  1.00 56.92           O  
-ATOM  28570  CB  VAL H  77      -0.800  42.577  16.705  1.00 49.95           C  
-ATOM  28571  CG1 VAL H  77      -0.474  43.945  17.281  1.00 52.07           C  
-ATOM  28572  CG2 VAL H  77      -2.298  42.316  16.770  1.00 49.41           C  
-ATOM  28573  N   VAL H  78       0.640  40.260  14.806  1.00 41.12           N  
-ATOM  28574  CA  VAL H  78       0.616  38.881  14.334  1.00 45.71           C  
-ATOM  28575  C   VAL H  78       1.097  37.931  15.425  1.00 60.87           C  
-ATOM  28576  O   VAL H  78       2.255  37.981  15.838  1.00 65.55           O  
-ATOM  28577  CB  VAL H  78       1.486  38.692  13.077  1.00 41.53           C  
-ATOM  28578  CG1 VAL H  78       1.387  37.258  12.582  1.00 49.44           C  
-ATOM  28579  CG2 VAL H  78       1.068  39.665  11.989  1.00 42.66           C  
-ATOM  28580  N   MET H  79       0.201  37.062  15.883  1.00 63.06           N  
-ATOM  28581  CA  MET H  79       0.507  36.164  16.991  1.00 55.90           C  
-ATOM  28582  C   MET H  79       0.313  34.698  16.626  1.00 60.52           C  
-ATOM  28583  O   MET H  79      -0.438  34.364  15.708  1.00 67.57           O  
-ATOM  28584  CB  MET H  79      -0.354  36.518  18.204  1.00 63.00           C  
-ATOM  28585  CG  MET H  79      -1.835  36.664  17.889  1.00 72.66           C  
-ATOM  28586  SD  MET H  79      -2.673  37.812  19.000  1.00 66.29           S  
-ATOM  28587  CE  MET H  79      -2.306  37.058  20.579  1.00 55.91           C  
-ATOM  28588  N   GLY H  80       1.000  33.825  17.355  1.00 65.75           N  
-ATOM  28589  CA  GLY H  80       0.913  32.397  17.116  1.00 72.36           C  
-ATOM  28590  C   GLY H  80      -0.389  31.821  17.639  1.00 76.53           C  
-ATOM  28591  O   GLY H  80      -1.196  32.547  18.228  1.00 63.10           O  
-ATOM  28592  N   ARG H  81      -0.595  30.523  17.426  1.00 80.85           N  
-ATOM  28593  CA  ARG H  81      -1.832  29.871  17.839  1.00 83.39           C  
-ATOM  28594  C   ARG H  81      -1.986  29.897  19.351  1.00 80.26           C  
-ATOM  28595  O   ARG H  81      -2.967  30.422  19.873  1.00 80.14           O  
-ATOM  28596  CB  ARG H  81      -1.890  28.424  17.336  1.00 84.67           C  
-ATOM  28597  CG  ARG H  81      -3.180  27.697  17.745  1.00 83.47           C  
-ATOM  28598  CD  ARG H  81      -3.168  26.229  17.340  1.00 72.57           C  
-ATOM  28599  NE  ARG H  81      -2.243  25.454  18.160  1.00 80.07           N  
-ATOM  28600  CZ  ARG H  81      -2.557  24.907  19.332  1.00 82.41           C  
-ATOM  28601  NH1 ARG H  81      -3.780  25.043  19.837  1.00 82.23           N  
-ATOM  28602  NH2 ARG H  81      -1.643  24.220  20.004  1.00 74.31           N  
-ATOM  28603  N   LYS H  82      -1.007  29.335  20.047  1.00 73.38           N  
-ATOM  28604  CA  LYS H  82      -1.052  29.252  21.501  1.00 71.51           C  
-ATOM  28605  C   LYS H  82      -1.011  30.631  22.161  1.00 71.30           C  
-ATOM  28606  O   LYS H  82      -1.571  30.832  23.240  1.00 67.97           O  
-ATOM  28607  CB  LYS H  82       0.102  28.381  22.011  1.00 72.08           C  
-ATOM  28608  CG  LYS H  82      -0.161  26.883  21.913  1.00 80.57           C  
-ATOM  28609  CD  LYS H  82       0.971  26.153  21.205  1.00 77.39           C  
-ATOM  28610  CE  LYS H  82       2.173  25.957  22.112  1.00 75.83           C  
-ATOM  28611  NZ  LYS H  82       3.225  25.120  21.468  1.00 53.75           N  
-ATOM  28612  N   THR H  83      -0.356  31.578  21.496  1.00 71.05           N  
-ATOM  28613  CA  THR H  83      -0.206  32.936  22.016  1.00 68.43           C  
-ATOM  28614  C   THR H  83      -1.562  33.629  22.154  1.00 70.28           C  
-ATOM  28615  O   THR H  83      -1.782  34.413  23.079  1.00 67.35           O  
-ATOM  28616  CB  THR H  83       0.711  33.789  21.110  1.00 61.63           C  
-ATOM  28617  OG1 THR H  83       1.936  33.086  20.863  1.00 61.44           O  
-ATOM  28618  CG2 THR H  83       1.019  35.127  21.760  1.00 44.21           C  
-ATOM  28619  N   TRP H  84      -2.466  33.332  21.225  1.00 73.25           N  
-ATOM  28620  CA  TRP H  84      -3.817  33.880  21.253  1.00 75.28           C  
-ATOM  28621  C   TRP H  84      -4.605  33.297  22.421  1.00 76.21           C  
-ATOM  28622  O   TRP H  84      -5.441  33.974  23.027  1.00 70.19           O  
-ATOM  28623  CB  TRP H  84      -4.524  33.600  19.925  1.00 77.08           C  
-ATOM  28624  CG  TRP H  84      -6.002  33.833  19.945  1.00 75.08           C  
-ATOM  28625  CD1 TRP H  84      -6.966  32.929  20.284  1.00 79.42           C  
-ATOM  28626  CD2 TRP H  84      -6.692  35.041  19.599  1.00 61.96           C  
-ATOM  28627  NE1 TRP H  84      -8.209  33.499  20.179  1.00 75.58           N  
-ATOM  28628  CE2 TRP H  84      -8.069  34.795  19.759  1.00 61.29           C  
-ATOM  28629  CE3 TRP H  84      -6.279  36.308  19.177  1.00 71.58           C  
-ATOM  28630  CZ2 TRP H  84      -9.036  35.768  19.511  1.00 59.46           C  
-ATOM  28631  CZ3 TRP H  84      -7.241  37.270  18.926  1.00 65.56           C  
-ATOM  28632  CH2 TRP H  84      -8.602  36.996  19.096  1.00 51.73           C  
-ATOM  28633  N   GLU H  85      -4.329  32.036  22.737  1.00 71.64           N  
-ATOM  28634  CA  GLU H  85      -4.994  31.371  23.848  1.00 73.51           C  
-ATOM  28635  C   GLU H  85      -4.439  31.849  25.182  1.00 80.35           C  
-ATOM  28636  O   GLU H  85      -5.137  31.834  26.193  1.00 79.13           O  
-ATOM  28637  CB  GLU H  85      -4.850  29.855  23.724  1.00 74.85           C  
-ATOM  28638  CG  GLU H  85      -5.687  29.253  22.608  1.00 82.51           C  
-ATOM  28639  CD  GLU H  85      -5.266  27.840  22.262  1.00 85.90           C  
-ATOM  28640  OE1 GLU H  85      -4.129  27.455  22.612  1.00 81.86           O  
-ATOM  28641  OE2 GLU H  85      -6.071  27.115  21.638  1.00 78.15           O  
-ATOM  28642  N   SER H  86      -3.182  32.280  25.177  1.00 81.42           N  
-ATOM  28643  CA  SER H  86      -2.535  32.755  26.393  1.00 67.84           C  
-ATOM  28644  C   SER H  86      -3.245  33.990  26.943  1.00 62.67           C  
-ATOM  28645  O   SER H  86      -3.310  34.190  28.154  1.00 62.48           O  
-ATOM  28646  CB  SER H  86      -1.059  33.064  26.128  1.00 60.67           C  
-ATOM  28647  OG  SER H  86      -0.222  32.427  27.078  1.00 59.96           O  
-ATOM  28648  N   MET H  87      -3.787  34.807  26.046  1.00 59.34           N  
-ATOM  28649  CA  MET H  87      -4.479  36.031  26.438  1.00 63.95           C  
-ATOM  28650  C   MET H  87      -5.861  35.762  27.025  1.00 73.24           C  
-ATOM  28651  O   MET H  87      -6.613  34.939  26.498  1.00 71.54           O  
-ATOM  28652  CB  MET H  87      -4.623  36.973  25.240  1.00 72.48           C  
-ATOM  28653  CG  MET H  87      -3.318  37.517  24.690  1.00 69.20           C  
-ATOM  28654  SD  MET H  87      -3.622  38.728  23.388  1.00 63.89           S  
-ATOM  28655  CE  MET H  87      -4.687  39.883  24.246  1.00 65.29           C  
-ATOM  28656  N   PRO H  88      -6.191  36.450  28.130  1.00 74.74           N  
-ATOM  28657  CA  PRO H  88      -7.557  36.511  28.662  1.00 78.53           C  
-ATOM  28658  C   PRO H  88      -8.563  36.879  27.574  1.00 84.77           C  
-ATOM  28659  O   PRO H  88      -8.232  37.666  26.686  1.00 85.97           O  
-ATOM  28660  CB  PRO H  88      -7.478  37.614  29.720  1.00 66.42           C  
-ATOM  28661  CG  PRO H  88      -6.026  37.732  30.080  1.00 62.76           C  
-ATOM  28662  CD  PRO H  88      -5.200  36.960  29.092  1.00 67.32           C  
-ATOM  28663  N   ARG H  89      -9.771  36.328  27.651  1.00 85.23           N  
-ATOM  28664  CA  ARG H  89     -10.771  36.517  26.604  1.00 82.02           C  
-ATOM  28665  C   ARG H  89     -11.210  37.972  26.465  1.00 79.05           C  
-ATOM  28666  O   ARG H  89     -11.531  38.427  25.367  1.00 82.70           O  
-ATOM  28667  CB  ARG H  89     -11.994  35.638  26.872  1.00 80.62           C  
-ATOM  28668  CG  ARG H  89     -11.665  34.279  27.458  1.00 77.94           C  
-ATOM  28669  CD  ARG H  89     -12.326  34.105  28.816  1.00 97.55           C  
-ATOM  28670  NE  ARG H  89     -11.969  35.179  29.741  1.00102.40           N  
-ATOM  28671  CZ  ARG H  89     -11.267  35.004  30.856  1.00 87.88           C  
-ATOM  28672  NH1 ARG H  89     -10.850  33.791  31.194  1.00 84.44           N  
-ATOM  28673  NH2 ARG H  89     -10.988  36.040  31.636  1.00 68.80           N  
-ATOM  28674  N   LYS H  90     -11.224  38.698  27.578  1.00 72.25           N  
-ATOM  28675  CA  LYS H  90     -11.669  40.088  27.577  1.00 75.57           C  
-ATOM  28676  C   LYS H  90     -10.690  40.991  26.832  1.00 82.72           C  
-ATOM  28677  O   LYS H  90     -11.032  42.112  26.449  1.00 78.10           O  
-ATOM  28678  CB  LYS H  90     -11.860  40.593  29.008  1.00 82.07           C  
-ATOM  28679  CG  LYS H  90     -10.585  40.634  29.835  1.00 76.26           C  
-ATOM  28680  CD  LYS H  90     -10.855  41.208  31.216  1.00 78.78           C  
-ATOM  28681  CE  LYS H  90      -9.590  41.262  32.056  1.00 65.62           C  
-ATOM  28682  NZ  LYS H  90      -9.853  41.806  33.417  1.00 43.06           N  
-ATOM  28683  N   PHE H  91      -9.474  40.495  26.627  1.00 87.46           N  
-ATOM  28684  CA  PHE H  91      -8.440  41.246  25.925  1.00 90.61           C  
-ATOM  28685  C   PHE H  91      -8.168  40.713  24.521  1.00 88.02           C  
-ATOM  28686  O   PHE H  91      -7.531  41.395  23.716  1.00 77.54           O  
-ATOM  28687  CB  PHE H  91      -7.133  41.230  26.720  1.00 87.83           C  
-ATOM  28688  CG  PHE H  91      -7.091  42.220  27.848  1.00 97.58           C  
-ATOM  28689  CD1 PHE H  91      -7.116  43.581  27.593  1.00 94.56           C  
-ATOM  28690  CD2 PHE H  91      -6.997  41.790  29.161  1.00 90.75           C  
-ATOM  28691  CE1 PHE H  91      -7.068  44.497  28.628  1.00 88.84           C  
-ATOM  28692  CE2 PHE H  91      -6.947  42.699  30.202  1.00 78.12           C  
-ATOM  28693  CZ  PHE H  91      -6.982  44.054  29.935  1.00 80.34           C  
-ATOM  28694  N   ARG H  92      -8.648  39.503  24.236  1.00 87.01           N  
-ATOM  28695  CA  ARG H  92      -8.263  38.780  23.020  1.00 77.27           C  
-ATOM  28696  C   ARG H  92      -8.419  39.597  21.728  1.00 88.27           C  
-ATOM  28697  O   ARG H  92      -7.512  39.601  20.897  1.00 92.11           O  
-ATOM  28698  CB  ARG H  92      -9.042  37.462  22.912  1.00 69.19           C  
-ATOM  28699  CG  ARG H  92      -8.454  36.338  23.759  1.00 75.43           C  
-ATOM  28700  CD  ARG H  92      -8.624  34.982  23.091  1.00 71.61           C  
-ATOM  28701  NE  ARG H  92      -9.818  34.275  23.543  1.00 89.88           N  
-ATOM  28702  CZ  ARG H  92      -9.795  33.205  24.331  1.00 95.38           C  
-ATOM  28703  NH1 ARG H  92     -10.929  32.620  24.698  1.00 82.48           N  
-ATOM  28704  NH2 ARG H  92      -8.635  32.714  24.749  1.00 88.60           N  
-ATOM  28705  N   PRO H  93      -9.553  40.296  21.547  1.00 84.98           N  
-ATOM  28706  CA  PRO H  93      -9.489  41.216  20.407  1.00 70.10           C  
-ATOM  28707  C   PRO H  93      -8.675  42.459  20.756  1.00 73.89           C  
-ATOM  28708  O   PRO H  93      -9.231  43.413  21.301  1.00 75.22           O  
-ATOM  28709  CB  PRO H  93     -10.959  41.574  20.149  1.00 69.19           C  
-ATOM  28710  CG  PRO H  93     -11.759  40.548  20.904  1.00 91.56           C  
-ATOM  28711  CD  PRO H  93     -10.918  40.188  22.087  1.00 83.94           C  
-ATOM  28712  N   LEU H  94      -7.376  42.434  20.464  1.00 70.08           N  
-ATOM  28713  CA  LEU H  94      -6.499  43.571  20.737  1.00 70.92           C  
-ATOM  28714  C   LEU H  94      -7.016  44.822  20.040  1.00 62.26           C  
-ATOM  28715  O   LEU H  94      -6.797  45.014  18.844  1.00 64.14           O  
-ATOM  28716  CB  LEU H  94      -5.065  43.263  20.298  1.00 71.45           C  
-ATOM  28717  CG  LEU H  94      -4.273  42.338  21.226  1.00 68.82           C  
-ATOM  28718  CD1 LEU H  94      -3.025  41.808  20.536  1.00 54.90           C  
-ATOM  28719  CD2 LEU H  94      -3.908  43.064  22.514  1.00 61.64           C  
-ATOM  28720  N   VAL H  95      -7.702  45.667  20.804  1.00 63.02           N  
-ATOM  28721  CA  VAL H  95      -8.442  46.802  20.258  1.00 72.47           C  
-ATOM  28722  C   VAL H  95      -7.570  47.811  19.509  1.00 66.04           C  
-ATOM  28723  O   VAL H  95      -6.411  48.038  19.867  1.00 52.77           O  
-ATOM  28724  CB  VAL H  95      -9.213  47.547  21.374  1.00 71.73           C  
-ATOM  28725  CG1 VAL H  95     -10.307  46.656  21.952  1.00 49.34           C  
-ATOM  28726  CG2 VAL H  95      -8.261  48.011  22.466  1.00 60.60           C  
-ATOM  28727  N   ASP H  96      -8.154  48.393  18.461  1.00 76.12           N  
-ATOM  28728  CA  ASP H  96      -7.525  49.420  17.623  1.00 75.54           C  
-ATOM  28729  C   ASP H  96      -6.334  48.900  16.815  1.00 67.68           C  
-ATOM  28730  O   ASP H  96      -5.513  49.681  16.331  1.00 60.53           O  
-ATOM  28731  CB  ASP H  96      -7.093  50.615  18.479  1.00 64.61           C  
-ATOM  28732  CG  ASP H  96      -8.219  51.142  19.346  1.00 72.17           C  
-ATOM  28733  OD1 ASP H  96      -9.035  51.940  18.838  1.00 73.31           O  
-ATOM  28734  OD2 ASP H  96      -8.291  50.754  20.531  1.00 72.23           O  
-ATOM  28735  N   ARG H  97      -6.254  47.583  16.660  1.00 51.44           N  
-ATOM  28736  CA  ARG H  97      -5.195  46.965  15.871  1.00 50.79           C  
-ATOM  28737  C   ARG H  97      -5.718  45.734  15.147  1.00 58.42           C  
-ATOM  28738  O   ARG H  97      -6.495  44.961  15.706  1.00 52.44           O  
-ATOM  28739  CB  ARG H  97      -4.008  46.584  16.758  1.00 59.30           C  
-ATOM  28740  CG  ARG H  97      -3.151  47.756  17.209  1.00 58.85           C  
-ATOM  28741  CD  ARG H  97      -2.467  47.452  18.530  1.00 50.01           C  
-ATOM  28742  NE  ARG H  97      -3.408  47.491  19.645  1.00 66.47           N  
-ATOM  28743  CZ  ARG H  97      -3.202  46.902  20.818  1.00 72.24           C  
-ATOM  28744  NH1 ARG H  97      -2.088  46.217  21.031  1.00 64.15           N  
-ATOM  28745  NH2 ARG H  97      -4.115  46.992  21.776  1.00 76.94           N  
-ATOM  28746  N   LEU H  98      -5.290  45.555  13.902  1.00 62.38           N  
-ATOM  28747  CA  LEU H  98      -5.676  44.382  13.126  1.00 67.85           C  
-ATOM  28748  C   LEU H  98      -4.990  43.148  13.706  1.00 61.83           C  
-ATOM  28749  O   LEU H  98      -3.771  43.114  13.819  1.00 60.64           O  
-ATOM  28750  CB  LEU H  98      -5.309  44.572  11.649  1.00 69.78           C  
-ATOM  28751  CG  LEU H  98      -6.009  43.742  10.566  1.00 69.76           C  
-ATOM  28752  CD1 LEU H  98      -5.494  42.307  10.508  1.00 54.08           C  
-ATOM  28753  CD2 LEU H  98      -7.520  43.766  10.763  1.00 73.43           C  
-ATOM  28754  N   ASN H  99      -5.772  42.139  14.076  1.00 50.57           N  
-ATOM  28755  CA  ASN H  99      -5.204  40.922  14.650  1.00 51.15           C  
-ATOM  28756  C   ASN H  99      -5.046  39.806  13.622  1.00 52.38           C  
-ATOM  28757  O   ASN H  99      -5.932  39.577  12.798  1.00 67.67           O  
-ATOM  28758  CB  ASN H  99      -6.063  40.427  15.816  1.00 63.04           C  
-ATOM  28759  CG  ASN H  99      -6.000  41.349  17.023  1.00 68.58           C  
-ATOM  28760  OD1 ASN H  99      -5.840  42.562  16.884  1.00 55.71           O  
-ATOM  28761  ND2 ASN H  99      -6.119  40.773  18.216  1.00 59.53           N  
-ATOM  28762  N   ILE H 100      -3.910  39.118  13.675  1.00 54.89           N  
-ATOM  28763  CA  ILE H 100      -3.657  37.978  12.800  1.00 64.98           C  
-ATOM  28764  C   ILE H 100      -3.063  36.802  13.571  1.00 69.10           C  
-ATOM  28765  O   ILE H 100      -1.871  36.786  13.879  1.00 71.00           O  
-ATOM  28766  CB  ILE H 100      -2.701  38.339  11.640  1.00 57.63           C  
-ATOM  28767  CG1 ILE H 100      -3.282  39.467  10.788  1.00 58.31           C  
-ATOM  28768  CG2 ILE H 100      -2.427  37.118  10.771  1.00 53.62           C  
-ATOM  28769  CD1 ILE H 100      -2.426  39.833   9.597  1.00 64.55           C  
-ATOM  28770  N   VAL H 101      -3.904  35.822  13.886  1.00 61.26           N  
-ATOM  28771  CA  VAL H 101      -3.438  34.574  14.475  1.00 59.80           C  
-ATOM  28772  C   VAL H 101      -2.962  33.654  13.361  1.00 55.46           C  
-ATOM  28773  O   VAL H 101      -3.569  33.608  12.293  1.00 61.60           O  
-ATOM  28774  CB  VAL H 101      -4.548  33.874  15.288  1.00 60.02           C  
-ATOM  28775  CG1 VAL H 101      -4.020  32.609  15.950  1.00 63.93           C  
-ATOM  28776  CG2 VAL H 101      -5.115  34.818  16.326  1.00 63.54           C  
-ATOM  28777  N   VAL H 102      -1.869  32.934  13.589  1.00 56.92           N  
-ATOM  28778  CA  VAL H 102      -1.448  31.936  12.615  1.00 55.57           C  
-ATOM  28779  C   VAL H 102      -1.600  30.532  13.197  1.00 72.35           C  
-ATOM  28780  O   VAL H 102      -1.221  30.266  14.339  1.00 82.99           O  
-ATOM  28781  CB  VAL H 102       0.003  32.175  12.134  1.00 53.72           C  
-ATOM  28782  CG1 VAL H 102       0.123  33.560  11.515  1.00 55.19           C  
-ATOM  28783  CG2 VAL H 102       1.000  32.007  13.269  1.00 71.43           C  
-ATOM  28784  N   SER H 103      -2.188  29.643  12.404  1.00 76.19           N  
-ATOM  28785  CA  SER H 103      -2.438  28.272  12.832  1.00 92.58           C  
-ATOM  28786  C   SER H 103      -2.842  27.401  11.650  1.00 84.44           C  
-ATOM  28787  O   SER H 103      -2.643  27.769  10.494  1.00 77.77           O  
-ATOM  28788  CB  SER H 103      -3.527  28.233  13.909  1.00 85.81           C  
-ATOM  28789  OG  SER H 103      -3.811  26.903  14.304  1.00 88.31           O  
-ATOM  28790  N   SER H 104      -3.412  26.241  11.950  1.00 87.91           N  
-ATOM  28791  CA  SER H 104      -3.915  25.346  10.919  1.00 79.73           C  
-ATOM  28792  C   SER H 104      -5.126  24.576  11.429  1.00 85.15           C  
-ATOM  28793  O   SER H 104      -5.596  23.644  10.778  1.00 84.00           O  
-ATOM  28794  CB  SER H 104      -2.820  24.378  10.461  1.00 78.52           C  
-ATOM  28795  OG  SER H 104      -2.346  23.593  11.542  1.00 72.83           O  
-ATOM  28796  N   SER H 105      -5.631  24.973  12.594  1.00 85.65           N  
-ATOM  28797  CA  SER H 105      -6.723  24.245  13.230  1.00 90.06           C  
-ATOM  28798  C   SER H 105      -7.765  25.149  13.896  1.00 82.34           C  
-ATOM  28799  O   SER H 105      -8.639  24.663  14.615  1.00 77.32           O  
-ATOM  28800  CB  SER H 105      -6.160  23.268  14.267  1.00 88.38           C  
-ATOM  28801  OG  SER H 105      -5.213  22.388  13.684  1.00 69.49           O  
-ATOM  28802  N   LEU H 106      -7.688  26.454  13.654  1.00 66.26           N  
-ATOM  28803  CA  LEU H 106      -8.623  27.382  14.288  1.00 70.55           C  
-ATOM  28804  C   LEU H 106      -9.521  28.118  13.295  1.00 62.46           C  
-ATOM  28805  O   LEU H 106      -9.328  28.040  12.082  1.00 61.61           O  
-ATOM  28806  CB  LEU H 106      -7.864  28.398  15.144  1.00 83.13           C  
-ATOM  28807  CG  LEU H 106      -7.212  27.836  16.410  1.00 95.57           C  
-ATOM  28808  CD1 LEU H 106      -6.697  28.961  17.296  1.00 78.68           C  
-ATOM  28809  CD2 LEU H 106      -8.186  26.947  17.173  1.00 85.82           C  
-ATOM  28810  N   LYS H 107     -10.503  28.835  13.837  1.00 64.73           N  
-ATOM  28811  CA  LYS H 107     -11.509  29.535  13.043  1.00 58.90           C  
-ATOM  28812  C   LYS H 107     -10.890  30.613  12.159  1.00 55.38           C  
-ATOM  28813  O   LYS H 107     -11.507  31.645  11.896  1.00 50.08           O  
-ATOM  28814  CB  LYS H 107     -12.565  30.160  13.959  1.00 55.13           C  
-ATOM  28815  CG  LYS H 107     -13.963  30.207  13.365  1.00 63.78           C  
-ATOM  28816  CD  LYS H 107     -14.807  31.288  14.020  1.00 52.47           C  
-ATOM  28817  CE  LYS H 107     -15.021  32.457  13.071  1.00 55.71           C  
-ATOM  28818  NZ  LYS H 107     -13.743  32.929  12.464  1.00 38.79           N  
-ATOM  28819  N   VAL H 126      -6.749  35.214  10.151  1.00 25.56           N  
-ATOM  28820  CA  VAL H 126      -6.264  33.899  10.554  1.00 52.52           C  
-ATOM  28821  C   VAL H 126      -5.571  33.195   9.392  1.00 50.17           C  
-ATOM  28822  O   VAL H 126      -6.205  32.485   8.610  1.00 55.69           O  
-ATOM  28823  CB  VAL H 126      -7.406  33.009  11.081  1.00 54.26           C  
-ATOM  28824  CG1 VAL H 126      -6.854  31.693  11.626  1.00 37.56           C  
-ATOM  28825  CG2 VAL H 126      -8.193  33.746  12.151  1.00 49.41           C  
-ATOM  28826  N   CYS H 127      -4.263  33.398   9.290  1.00 47.81           N  
-ATOM  28827  CA  CYS H 127      -3.475  32.831   8.204  1.00 50.95           C  
-ATOM  28828  C   CYS H 127      -2.854  31.502   8.621  1.00 58.68           C  
-ATOM  28829  O   CYS H 127      -2.943  31.110   9.784  1.00 66.91           O  
-ATOM  28830  CB  CYS H 127      -2.399  33.823   7.770  1.00 59.56           C  
-ATOM  28831  SG  CYS H 127      -3.057  35.484   7.473  1.00 81.67           S  
-ATOM  28832  N   ALA H 128      -2.230  30.811   7.671  1.00 50.31           N  
-ATOM  28833  CA  ALA H 128      -1.708  29.472   7.924  1.00 55.97           C  
-ATOM  28834  C   ALA H 128      -0.189  29.464   8.063  1.00 64.58           C  
-ATOM  28835  O   ALA H 128       0.422  28.413   8.269  1.00 62.65           O  
-ATOM  28836  CB  ALA H 128      -2.141  28.523   6.817  1.00 61.34           C  
-ATOM  28837  N   SER H 129       0.411  30.643   7.944  1.00 66.99           N  
-ATOM  28838  CA  SER H 129       1.845  30.810   8.141  1.00 74.24           C  
-ATOM  28839  C   SER H 129       2.161  32.291   8.254  1.00 73.62           C  
-ATOM  28840  O   SER H 129       1.312  33.137   7.973  1.00 68.03           O  
-ATOM  28841  CB  SER H 129       2.643  30.186   6.992  1.00 76.08           C  
-ATOM  28842  OG  SER H 129       2.509  30.947   5.805  1.00 70.78           O  
-ATOM  28843  N   LEU H 130       3.382  32.603   8.672  1.00 66.28           N  
-ATOM  28844  CA  LEU H 130       3.828  33.990   8.733  1.00 68.54           C  
-ATOM  28845  C   LEU H 130       3.978  34.624   7.341  1.00 75.34           C  
-ATOM  28846  O   LEU H 130       3.559  35.767   7.148  1.00 66.15           O  
-ATOM  28847  CB  LEU H 130       5.143  34.098   9.508  1.00 71.82           C  
-ATOM  28848  CG  LEU H 130       5.693  35.515   9.667  1.00 58.90           C  
-ATOM  28849  CD1 LEU H 130       4.710  36.397  10.422  1.00 55.47           C  
-ATOM  28850  CD2 LEU H 130       7.032  35.474  10.372  1.00 57.12           C  
-ATOM  28851  N   PRO H 131       4.581  33.901   6.369  1.00 84.25           N  
-ATOM  28852  CA  PRO H 131       4.600  34.485   5.021  1.00 76.44           C  
-ATOM  28853  C   PRO H 131       3.204  34.763   4.475  1.00 74.39           C  
-ATOM  28854  O   PRO H 131       2.984  35.804   3.861  1.00 69.91           O  
-ATOM  28855  CB  PRO H 131       5.303  33.411   4.183  1.00 76.70           C  
-ATOM  28856  CG  PRO H 131       6.161  32.700   5.144  1.00 76.21           C  
-ATOM  28857  CD  PRO H 131       5.389  32.667   6.427  1.00 73.64           C  
-ATOM  28858  N   ALA H 132       2.279  33.834   4.697  1.00 75.81           N  
-ATOM  28859  CA  ALA H 132       0.894  34.022   4.287  1.00 76.97           C  
-ATOM  28860  C   ALA H 132       0.277  35.198   5.035  1.00 76.59           C  
-ATOM  28861  O   ALA H 132      -0.578  35.904   4.504  1.00 70.42           O  
-ATOM  28862  CB  ALA H 132       0.089  32.751   4.525  1.00 61.24           C  
-ATOM  28863  N   ALA H 133       0.722  35.403   6.271  1.00 76.30           N  
-ATOM  28864  CA  ALA H 133       0.233  36.507   7.085  1.00 74.40           C  
-ATOM  28865  C   ALA H 133       0.704  37.834   6.516  1.00 79.59           C  
-ATOM  28866  O   ALA H 133      -0.001  38.840   6.598  1.00 67.43           O  
-ATOM  28867  CB  ALA H 133       0.687  36.350   8.526  1.00 73.78           C  
-ATOM  28868  N   LEU H 134       1.902  37.829   5.940  1.00 79.51           N  
-ATOM  28869  CA  LEU H 134       2.434  39.018   5.289  1.00 77.05           C  
-ATOM  28870  C   LEU H 134       1.715  39.252   3.962  1.00 80.07           C  
-ATOM  28871  O   LEU H 134       1.444  40.394   3.581  1.00 72.83           O  
-ATOM  28872  CB  LEU H 134       3.943  38.882   5.071  1.00 75.80           C  
-ATOM  28873  CG  LEU H 134       4.780  38.647   6.331  1.00 49.22           C  
-ATOM  28874  CD1 LEU H 134       6.254  38.513   5.985  1.00 49.14           C  
-ATOM  28875  CD2 LEU H 134       4.562  39.765   7.330  1.00 48.62           C  
-ATOM  28876  N   SER H 135       1.403  38.159   3.271  1.00 77.37           N  
-ATOM  28877  CA  SER H 135       0.696  38.223   1.997  1.00 75.90           C  
-ATOM  28878  C   SER H 135      -0.701  38.804   2.178  1.00 76.41           C  
-ATOM  28879  O   SER H 135      -1.136  39.641   1.391  1.00 77.99           O  
-ATOM  28880  CB  SER H 135       0.611  36.836   1.358  1.00 76.74           C  
-ATOM  28881  OG  SER H 135       1.901  36.316   1.086  1.00 73.11           O  
-ATOM  28882  N   LEU H 136      -1.395  38.360   3.222  1.00 76.22           N  
-ATOM  28883  CA  LEU H 136      -2.722  38.873   3.555  1.00 87.23           C  
-ATOM  28884  C   LEU H 136      -2.668  40.356   3.906  1.00 80.95           C  
-ATOM  28885  O   LEU H 136      -3.667  41.069   3.802  1.00 72.31           O  
-ATOM  28886  CB  LEU H 136      -3.326  38.079   4.717  1.00 81.52           C  
-ATOM  28887  CG  LEU H 136      -4.349  36.992   4.379  1.00 86.24           C  
-ATOM  28888  CD1 LEU H 136      -5.670  37.607   3.937  1.00 79.62           C  
-ATOM  28889  CD2 LEU H 136      -3.809  36.053   3.312  1.00 87.09           C  
-ATOM  28890  N   LEU H 137      -1.493  40.811   4.329  1.00 83.97           N  
-ATOM  28891  CA  LEU H 137      -1.286  42.213   4.666  1.00 85.25           C  
-ATOM  28892  C   LEU H 137      -0.928  43.035   3.435  1.00 78.90           C  
-ATOM  28893  O   LEU H 137      -1.170  44.241   3.393  1.00 70.72           O  
-ATOM  28894  CB  LEU H 137      -0.185  42.352   5.720  1.00 96.88           C  
-ATOM  28895  CG  LEU H 137      -0.525  41.968   7.161  1.00 92.34           C  
-ATOM  28896  CD1 LEU H 137       0.741  41.932   8.001  1.00 84.31           C  
-ATOM  28897  CD2 LEU H 137      -1.540  42.934   7.759  1.00 82.78           C  
-ATOM  28898  N   GLU H 138      -0.346  42.382   2.435  1.00 84.50           N  
-ATOM  28899  CA  GLU H 138       0.065  43.080   1.222  1.00 84.09           C  
-ATOM  28900  C   GLU H 138      -1.079  43.196   0.220  1.00 88.37           C  
-ATOM  28901  O   GLU H 138      -1.293  44.259  -0.362  1.00 87.61           O  
-ATOM  28902  CB  GLU H 138       1.259  42.377   0.577  1.00 75.09           C  
-ATOM  28903  CG  GLU H 138       2.488  43.261   0.448  1.00 78.72           C  
-ATOM  28904  CD  GLU H 138       3.656  42.541  -0.195  1.00 79.59           C  
-ATOM  28905  OE1 GLU H 138       3.432  41.484  -0.822  1.00 69.76           O  
-ATOM  28906  OE2 GLU H 138       4.799  43.028  -0.071  1.00 64.58           O  
-ATOM  28907  N   GLU H 139      -1.803  42.098   0.017  1.00 83.34           N  
-ATOM  28908  CA  GLU H 139      -2.955  42.095  -0.881  1.00 87.82           C  
-ATOM  28909  C   GLU H 139      -3.991  43.112  -0.414  1.00 94.29           C  
-ATOM  28910  O   GLU H 139      -4.100  44.199  -0.980  1.00 86.13           O  
-ATOM  28911  CB  GLU H 139      -3.581  40.698  -0.969  1.00 81.56           C  
-ATOM  28912  CG  GLU H 139      -4.887  40.643  -1.763  1.00 96.04           C  
-ATOM  28913  CD  GLU H 139      -4.694  40.886  -3.249  1.00102.77           C  
-ATOM  28914  OE1 GLU H 139      -4.289  39.940  -3.957  1.00101.06           O  
-ATOM  28915  OE2 GLU H 139      -4.957  42.018  -3.710  1.00 91.87           O  
-ATOM  28916  N   GLU H 140      -4.749  42.760   0.619  1.00 89.04           N  
-ATOM  28917  CA  GLU H 140      -5.683  43.707   1.210  1.00 72.40           C  
-ATOM  28918  C   GLU H 140      -5.004  44.430   2.362  1.00 85.08           C  
-ATOM  28919  O   GLU H 140      -3.845  44.154   2.676  1.00 84.77           O  
-ATOM  28920  CB  GLU H 140      -6.958  43.007   1.685  1.00 58.67           C  
-ATOM  28921  CG  GLU H 140      -6.721  41.759   2.512  1.00 71.39           C  
-ATOM  28922  CD  GLU H 140      -7.233  40.505   1.830  1.00 77.89           C  
-ATOM  28923  OE1 GLU H 140      -6.487  39.930   1.010  1.00 88.07           O  
-ATOM  28924  OE2 GLU H 140      -8.380  40.097   2.111  1.00 54.94           O  
-ATOM  28925  N   TYR H 141      -5.734  45.365   2.967  1.00 88.75           N  
-ATOM  28926  CA  TYR H 141      -5.241  46.217   4.052  1.00 80.74           C  
-ATOM  28927  C   TYR H 141      -4.134  47.176   3.615  1.00 82.24           C  
-ATOM  28928  O   TYR H 141      -3.730  48.029   4.400  1.00 80.44           O  
-ATOM  28929  CB  TYR H 141      -4.724  45.384   5.231  1.00 70.29           C  
-ATOM  28930  CG  TYR H 141      -5.689  44.357   5.776  1.00 65.04           C  
-ATOM  28931  CD1 TYR H 141      -6.754  44.731   6.583  1.00 53.58           C  
-ATOM  28932  CD2 TYR H 141      -5.513  43.007   5.506  1.00 72.76           C  
-ATOM  28933  CE1 TYR H 141      -7.630  43.788   7.091  1.00 55.16           C  
-ATOM  28934  CE2 TYR H 141      -6.380  42.057   6.006  1.00 58.32           C  
-ATOM  28935  CZ  TYR H 141      -7.437  42.451   6.798  1.00 59.51           C  
-ATOM  28936  OH  TYR H 141      -8.301  41.502   7.296  1.00 50.76           O  
-ATOM  28937  N   LYS H 142      -3.661  47.043   2.374  1.00 85.43           N  
-ATOM  28938  CA  LYS H 142      -2.524  47.818   1.863  1.00 87.67           C  
-ATOM  28939  C   LYS H 142      -2.642  49.300   2.204  1.00 85.93           C  
-ATOM  28940  O   LYS H 142      -1.651  49.960   2.526  1.00 66.83           O  
-ATOM  28941  CB  LYS H 142      -2.393  47.648   0.348  1.00 85.96           C  
-ATOM  28942  CG  LYS H 142      -1.152  48.308  -0.239  1.00 90.45           C  
-ATOM  28943  CD  LYS H 142       0.092  47.462   0.003  1.00 92.63           C  
-ATOM  28944  CE  LYS H 142       1.364  48.272  -0.208  1.00 83.21           C  
-ATOM  28945  NZ  LYS H 142       1.380  48.971  -1.522  1.00 62.73           N  
-ATOM  28946  N   ASP H 143      -3.864  49.814   2.131  1.00 96.11           N  
-ATOM  28947  CA  ASP H 143      -4.172  51.128   2.670  1.00 98.16           C  
-ATOM  28948  C   ASP H 143      -4.748  50.951   4.069  1.00 93.19           C  
-ATOM  28949  O   ASP H 143      -5.682  50.166   4.249  1.00 84.03           O  
-ATOM  28950  CB  ASP H 143      -5.156  51.876   1.769  1.00 98.60           C  
-ATOM  28951  CG  ASP H 143      -4.688  51.946   0.329  1.00 95.67           C  
-ATOM  28952  OD1 ASP H 143      -4.004  51.001  -0.120  1.00 93.52           O  
-ATOM  28953  OD2 ASP H 143      -5.004  52.942  -0.356  1.00 84.65           O  
-ATOM  28954  N   SER H 144      -4.136  51.663   5.023  1.00 92.30           N  
-ATOM  28955  CA  SER H 144      -4.489  51.783   6.454  1.00 96.14           C  
-ATOM  28956  C   SER H 144      -3.419  51.176   7.362  1.00 88.38           C  
-ATOM  28957  O   SER H 144      -3.117  51.738   8.415  1.00 92.21           O  
-ATOM  28958  CB  SER H 144      -5.845  51.160   6.804  1.00 96.07           C  
-ATOM  28959  OG  SER H 144      -6.900  51.823   6.129  1.00109.89           O  
-ATOM  28960  N   VAL H 145      -2.848  50.038   6.975  1.00 89.00           N  
-ATOM  28961  CA  VAL H 145      -1.844  49.414   7.833  1.00 77.19           C  
-ATOM  28962  C   VAL H 145      -0.522  50.182   7.746  1.00 80.10           C  
-ATOM  28963  O   VAL H 145       0.109  50.273   6.692  1.00 94.03           O  
-ATOM  28964  CB  VAL H 145      -1.634  47.904   7.501  1.00 80.81           C  
-ATOM  28965  CG1 VAL H 145      -1.175  47.684   6.062  1.00 91.20           C  
-ATOM  28966  CG2 VAL H 145      -0.657  47.278   8.485  1.00 79.13           C  
-ATOM  28967  N   ASP H 146      -0.131  50.770   8.870  1.00 75.76           N  
-ATOM  28968  CA  ASP H 146       1.103  51.539   8.947  1.00 74.98           C  
-ATOM  28969  C   ASP H 146       2.298  50.598   9.001  1.00 74.18           C  
-ATOM  28970  O   ASP H 146       2.927  50.305   7.983  1.00 70.34           O  
-ATOM  28971  CB  ASP H 146       1.085  52.460  10.173  1.00 66.43           C  
-ATOM  28972  CG  ASP H 146       2.410  53.171  10.397  1.00 68.16           C  
-ATOM  28973  OD1 ASP H 146       3.113  53.460   9.405  1.00 63.88           O  
-ATOM  28974  OD2 ASP H 146       2.749  53.440  11.569  1.00 65.73           O  
-ATOM  28975  N   GLN H 147       2.600  50.127  10.204  1.00 75.60           N  
-ATOM  28976  CA  GLN H 147       3.660  49.156  10.417  1.00 65.14           C  
-ATOM  28977  C   GLN H 147       3.079  47.935  11.112  1.00 61.60           C  
-ATOM  28978  O   GLN H 147       2.077  48.036  11.820  1.00 50.60           O  
-ATOM  28979  CB  GLN H 147       4.790  49.762  11.248  1.00 59.63           C  
-ATOM  28980  CG  GLN H 147       4.300  50.494  12.486  1.00 61.73           C  
-ATOM  28981  CD  GLN H 147       5.429  50.903  13.409  1.00 56.98           C  
-ATOM  28982  OE1 GLN H 147       6.605  50.743  13.081  1.00 55.88           O  
-ATOM  28983  NE2 GLN H 147       5.077  51.429  14.574  1.00 56.90           N  
-ATOM  28984  N   ILE H 148       3.701  46.781  10.910  1.00 58.78           N  
-ATOM  28985  CA  ILE H 148       3.195  45.557  11.512  1.00 61.79           C  
-ATOM  28986  C   ILE H 148       4.011  45.173  12.740  1.00 63.81           C  
-ATOM  28987  O   ILE H 148       5.096  45.709  12.973  1.00 68.62           O  
-ATOM  28988  CB  ILE H 148       3.197  44.387  10.506  1.00 63.07           C  
-ATOM  28989  CG1 ILE H 148       4.517  43.617  10.564  1.00 66.46           C  
-ATOM  28990  CG2 ILE H 148       2.919  44.894   9.098  1.00 46.63           C  
-ATOM  28991  CD1 ILE H 148       4.423  42.234   9.976  1.00 70.69           C  
-ATOM  28992  N   PHE H 149       3.474  44.248  13.528  1.00 64.28           N  
-ATOM  28993  CA  PHE H 149       4.152  43.761  14.721  1.00 57.97           C  
-ATOM  28994  C   PHE H 149       3.956  42.258  14.903  1.00 56.66           C  
-ATOM  28995  O   PHE H 149       2.889  41.720  14.606  1.00 58.38           O  
-ATOM  28996  CB  PHE H 149       3.650  44.500  15.962  1.00 59.79           C  
-ATOM  28997  CG  PHE H 149       4.112  45.925  16.051  1.00 56.34           C  
-ATOM  28998  CD1 PHE H 149       5.417  46.219  16.405  1.00 57.03           C  
-ATOM  28999  CD2 PHE H 149       3.239  46.970  15.800  1.00 56.47           C  
-ATOM  29000  CE1 PHE H 149       5.847  47.528  16.498  1.00 55.35           C  
-ATOM  29001  CE2 PHE H 149       3.664  48.283  15.891  1.00 54.64           C  
-ATOM  29002  CZ  PHE H 149       4.970  48.561  16.241  1.00 48.66           C  
-ATOM  29003  N   VAL H 150       4.992  41.586  15.391  1.00 53.21           N  
-ATOM  29004  CA  VAL H 150       4.889  40.177  15.750  1.00 50.57           C  
-ATOM  29005  C   VAL H 150       5.101  40.015  17.253  1.00 47.56           C  
-ATOM  29006  O   VAL H 150       6.138  40.410  17.789  1.00 44.14           O  
-ATOM  29007  CB  VAL H 150       5.906  39.314  14.985  1.00 43.88           C  
-ATOM  29008  CG1 VAL H 150       5.780  37.857  15.399  1.00 39.57           C  
-ATOM  29009  CG2 VAL H 150       5.709  39.468  13.484  1.00 47.71           C  
-ATOM  29010  N   VAL H 151       4.114  39.434  17.928  1.00 48.85           N  
-ATOM  29011  CA  VAL H 151       4.118  39.365  19.386  1.00 34.15           C  
-ATOM  29012  C   VAL H 151       4.037  37.934  19.916  1.00 27.96           C  
-ATOM  29013  O   VAL H 151       4.325  36.972  19.202  1.00 24.56           O  
-ATOM  29014  CB  VAL H 151       2.949  40.174  19.971  1.00 36.00           C  
-ATOM  29015  CG1 VAL H 151       2.934  41.579  19.387  1.00 31.95           C  
-ATOM  29016  CG2 VAL H 151       1.633  39.473  19.691  1.00 41.86           C  
-ATOM  29017  N   GLY H 153       4.397  34.495  19.688  1.00 30.51           N  
-ATOM  29018  CA  GLY H 153       5.215  33.662  20.551  1.00 50.66           C  
-ATOM  29019  C   GLY H 153       6.388  33.051  19.809  1.00 55.45           C  
-ATOM  29020  O   GLY H 153       6.608  33.348  18.635  1.00 50.92           O  
-ATOM  29021  N   ALA H 154       7.144  32.197  20.493  1.00 48.94           N  
-ATOM  29022  CA  ALA H 154       8.305  31.552  19.888  1.00 44.78           C  
-ATOM  29023  C   ALA H 154       7.871  30.675  18.729  1.00 57.15           C  
-ATOM  29024  O   ALA H 154       6.735  30.203  18.686  1.00 65.12           O  
-ATOM  29025  CB  ALA H 154       9.062  30.736  20.913  1.00 51.18           C  
-ATOM  29026  N   GLY H 155       8.777  30.456  17.787  1.00 60.88           N  
-ATOM  29027  CA  GLY H 155       8.414  29.764  16.569  1.00 72.37           C  
-ATOM  29028  C   GLY H 155       7.972  30.777  15.534  1.00 63.16           C  
-ATOM  29029  O   GLY H 155       8.405  30.725  14.388  1.00 69.79           O  
-ATOM  29030  N   LEU H 156       7.099  31.694  15.937  1.00 50.30           N  
-ATOM  29031  CA  LEU H 156       6.736  32.820  15.090  1.00 54.98           C  
-ATOM  29032  C   LEU H 156       7.913  33.782  15.034  1.00 58.59           C  
-ATOM  29033  O   LEU H 156       8.237  34.326  13.981  1.00 63.05           O  
-ATOM  29034  CB  LEU H 156       5.482  33.519  15.619  1.00 47.57           C  
-ATOM  29035  CG  LEU H 156       4.711  34.370  14.609  1.00 56.23           C  
-ATOM  29036  CD1 LEU H 156       4.286  33.512  13.434  1.00 62.06           C  
-ATOM  29037  CD2 LEU H 156       3.506  34.995  15.280  1.00 50.87           C  
-ATOM  29038  N   TYR H 157       8.547  33.977  16.186  1.00 51.82           N  
-ATOM  29039  CA  TYR H 157       9.771  34.763  16.279  1.00 44.88           C  
-ATOM  29040  C   TYR H 157      10.864  34.162  15.409  1.00 51.64           C  
-ATOM  29041  O   TYR H 157      11.483  34.865  14.613  1.00 57.53           O  
-ATOM  29042  CB  TYR H 157      10.257  34.849  17.730  1.00 48.11           C  
-ATOM  29043  CG  TYR H 157       9.364  35.660  18.643  1.00 41.17           C  
-ATOM  29044  CD1 TYR H 157       8.830  36.872  18.229  1.00 37.43           C  
-ATOM  29045  CD2 TYR H 157       9.059  35.212  19.919  1.00 42.61           C  
-ATOM  29046  CE1 TYR H 157       8.021  37.614  19.060  1.00 31.15           C  
-ATOM  29047  CE2 TYR H 157       8.248  35.945  20.758  1.00 38.40           C  
-ATOM  29048  CZ  TYR H 157       7.728  37.143  20.322  1.00 34.59           C  
-ATOM  29049  OH  TYR H 157       6.921  37.883  21.155  1.00 36.93           O  
-ATOM  29050  N   GLU H 158      11.099  32.862  15.566  1.00 54.19           N  
-ATOM  29051  CA  GLU H 158      12.173  32.192  14.835  1.00 64.40           C  
-ATOM  29052  C   GLU H 158      11.849  32.122  13.348  1.00 63.31           C  
-ATOM  29053  O   GLU H 158      12.751  32.077  12.509  1.00 56.77           O  
-ATOM  29054  CB  GLU H 158      12.430  30.786  15.394  1.00 60.29           C  
-ATOM  29055  CG  GLU H 158      11.459  29.714  14.940  1.00 79.11           C  
-ATOM  29056  CD  GLU H 158      11.480  28.490  15.839  1.00 79.57           C  
-ATOM  29057  OE1 GLU H 158      12.218  28.505  16.846  1.00 73.19           O  
-ATOM  29058  OE2 GLU H 158      10.752  27.517  15.544  1.00 64.53           O  
-ATOM  29059  N   ALA H 159      10.559  32.113  13.029  1.00 59.14           N  
-ATOM  29060  CA  ALA H 159      10.125  32.181  11.643  1.00 58.45           C  
-ATOM  29061  C   ALA H 159      10.506  33.529  11.075  1.00 61.20           C  
-ATOM  29062  O   ALA H 159      11.112  33.619  10.013  1.00 68.99           O  
-ATOM  29063  CB  ALA H 159       8.629  31.963  11.531  1.00 57.83           C  
-ATOM  29064  N   ALA H 160      10.148  34.573  11.815  1.00 56.19           N  
-ATOM  29065  CA  ALA H 160      10.421  35.952  11.433  1.00 46.66           C  
-ATOM  29066  C   ALA H 160      11.913  36.225  11.300  1.00 51.75           C  
-ATOM  29067  O   ALA H 160      12.330  37.082  10.521  1.00 54.49           O  
-ATOM  29068  CB  ALA H 160       9.807  36.898  12.446  1.00 46.67           C  
-ATOM  29069  N   LEU H 161      12.714  35.495  12.067  1.00 52.89           N  
-ATOM  29070  CA  LEU H 161      14.158  35.684  12.057  1.00 50.17           C  
-ATOM  29071  C   LEU H 161      14.832  34.914  10.926  1.00 63.39           C  
-ATOM  29072  O   LEU H 161      15.659  35.468  10.199  1.00 66.92           O  
-ATOM  29073  CB  LEU H 161      14.752  35.270  13.403  1.00 47.05           C  
-ATOM  29074  CG  LEU H 161      14.637  36.321  14.509  1.00 42.86           C  
-ATOM  29075  CD1 LEU H 161      15.183  35.796  15.829  1.00 39.19           C  
-ATOM  29076  CD2 LEU H 161      15.356  37.597  14.097  1.00 37.78           C  
-ATOM  29077  N   SER H 162      14.481  33.639  10.781  1.00 59.86           N  
-ATOM  29078  CA  SER H 162      15.045  32.813   9.717  1.00 53.50           C  
-ATOM  29079  C   SER H 162      14.614  33.315   8.339  1.00 56.44           C  
-ATOM  29080  O   SER H 162      15.363  33.209   7.369  1.00 71.01           O  
-ATOM  29081  CB  SER H 162      14.643  31.348   9.906  1.00 52.76           C  
-ATOM  29082  OG  SER H 162      13.289  31.234  10.309  1.00 64.38           O  
-ATOM  29083  N   LEU H 163      13.408  33.870   8.261  1.00 52.70           N  
-ATOM  29084  CA  LEU H 163      12.917  34.470   7.024  1.00 48.41           C  
-ATOM  29085  C   LEU H 163      13.465  35.884   6.863  1.00 52.43           C  
-ATOM  29086  O   LEU H 163      13.199  36.551   5.862  1.00 48.72           O  
-ATOM  29087  CB  LEU H 163      11.385  34.488   6.993  1.00 45.51           C  
-ATOM  29088  CG  LEU H 163      10.683  33.127   6.983  1.00 55.54           C  
-ATOM  29089  CD1 LEU H 163       9.185  33.291   7.210  1.00 62.65           C  
-ATOM  29090  CD2 LEU H 163      10.954  32.384   5.685  1.00 77.83           C  
-ATOM  29091  N   GLY H 164      14.219  36.331   7.865  1.00 56.29           N  
-ATOM  29092  CA  GLY H 164      14.923  37.602   7.823  1.00 57.92           C  
-ATOM  29093  C   GLY H 164      14.090  38.803   7.419  1.00 56.63           C  
-ATOM  29094  O   GLY H 164      14.487  39.571   6.543  1.00 62.56           O  
-ATOM  29095  N   VAL H 165      12.939  38.973   8.059  1.00 51.00           N  
-ATOM  29096  CA  VAL H 165      12.029  40.056   7.704  1.00 57.67           C  
-ATOM  29097  C   VAL H 165      11.903  41.107   8.806  1.00 59.58           C  
-ATOM  29098  O   VAL H 165      11.326  42.173   8.589  1.00 62.79           O  
-ATOM  29099  CB  VAL H 165      10.628  39.516   7.369  1.00 56.14           C  
-ATOM  29100  CG1 VAL H 165      10.630  38.853   6.000  1.00 56.13           C  
-ATOM  29101  CG2 VAL H 165      10.165  38.542   8.442  1.00 53.83           C  
-ATOM  29102  N   ALA H 166      12.444  40.808   9.982  1.00 56.12           N  
-ATOM  29103  CA  ALA H 166      12.363  41.725  11.115  1.00 49.01           C  
-ATOM  29104  C   ALA H 166      13.538  42.699  11.123  1.00 54.11           C  
-ATOM  29105  O   ALA H 166      14.689  42.296  11.294  1.00 58.29           O  
-ATOM  29106  CB  ALA H 166      12.307  40.948  12.420  1.00 46.70           C  
-ATOM  29107  N   SER H 167      13.241  43.982  10.938  1.00 45.43           N  
-ATOM  29108  CA  SER H 167      14.276  45.010  10.883  1.00 48.79           C  
-ATOM  29109  C   SER H 167      14.628  45.531  12.271  1.00 53.31           C  
-ATOM  29110  O   SER H 167      15.779  45.899  12.535  1.00 57.36           O  
-ATOM  29111  CB  SER H 167      13.829  46.169   9.992  1.00 53.25           C  
-ATOM  29112  OG  SER H 167      12.641  46.762  10.486  1.00 54.67           O  
-ATOM  29113  N   HIS H 168      13.630  45.556  13.152  1.00 52.62           N  
-ATOM  29114  CA  HIS H 168      13.802  46.063  14.509  1.00 48.15           C  
-ATOM  29115  C   HIS H 168      13.335  45.067  15.570  1.00 46.56           C  
-ATOM  29116  O   HIS H 168      12.490  44.211  15.305  1.00 51.30           O  
-ATOM  29117  CB  HIS H 168      13.047  47.382  14.686  1.00 44.12           C  
-ATOM  29118  CG  HIS H 168      13.415  48.429  13.684  1.00 49.50           C  
-ATOM  29119  ND1 HIS H 168      14.653  49.035  13.661  1.00 58.08           N  
-ATOM  29120  CD2 HIS H 168      12.705  48.984  12.674  1.00 61.89           C  
-ATOM  29121  CE1 HIS H 168      14.692  49.915  12.677  1.00 61.04           C  
-ATOM  29122  NE2 HIS H 168      13.522  49.904  12.063  1.00 71.54           N  
-ATOM  29123  N   LEU H 169      13.889  45.193  16.773  1.00 36.13           N  
-ATOM  29124  CA  LEU H 169      13.483  44.368  17.907  1.00 36.63           C  
-ATOM  29125  C   LEU H 169      13.124  45.231  19.116  1.00 37.81           C  
-ATOM  29126  O   LEU H 169      13.984  45.916  19.664  1.00 36.43           O  
-ATOM  29127  CB  LEU H 169      14.593  43.386  18.295  1.00 28.46           C  
-ATOM  29128  CG  LEU H 169      15.084  42.373  17.262  1.00 27.18           C  
-ATOM  29129  CD1 LEU H 169      16.029  41.379  17.915  1.00 24.99           C  
-ATOM  29130  CD2 LEU H 169      13.921  41.651  16.624  1.00 31.84           C  
-ATOM  29131  N   TYR H 170      11.860  45.201  19.527  1.00 35.99           N  
-ATOM  29132  CA  TYR H 170      11.445  45.877  20.757  1.00 31.68           C  
-ATOM  29133  C   TYR H 170      11.508  44.910  21.933  1.00 29.51           C  
-ATOM  29134  O   TYR H 170      10.564  44.165  22.190  1.00 33.03           O  
-ATOM  29135  CB  TYR H 170      10.035  46.452  20.625  1.00 45.79           C  
-ATOM  29136  CG  TYR H 170       9.945  47.665  19.730  1.00 49.22           C  
-ATOM  29137  CD1 TYR H 170      10.109  48.945  20.243  1.00 42.24           C  
-ATOM  29138  CD2 TYR H 170       9.692  47.532  18.371  1.00 61.44           C  
-ATOM  29139  CE1 TYR H 170      10.028  50.056  19.427  1.00 56.58           C  
-ATOM  29140  CE2 TYR H 170       9.608  48.640  17.547  1.00 66.85           C  
-ATOM  29141  CZ  TYR H 170       9.776  49.901  18.081  1.00 62.94           C  
-ATOM  29142  OH  TYR H 170       9.694  51.013  17.272  1.00 55.69           O  
-ATOM  29143  N   ILE H 171      12.623  44.934  22.653  1.00 35.38           N  
-ATOM  29144  CA  ILE H 171      12.873  43.961  23.708  1.00 28.69           C  
-ATOM  29145  C   ILE H 171      12.745  44.544  25.111  1.00 32.70           C  
-ATOM  29146  O   ILE H 171      13.404  45.529  25.449  1.00 34.87           O  
-ATOM  29147  CB  ILE H 171      14.279  43.341  23.567  1.00 23.91           C  
-ATOM  29148  CG1 ILE H 171      14.449  42.701  22.187  1.00 21.42           C  
-ATOM  29149  CG2 ILE H 171      14.531  42.336  24.680  1.00 28.44           C  
-ATOM  29150  CD1 ILE H 171      15.753  41.970  22.011  1.00 21.76           C  
-ATOM  29151  N   THR H 172      11.894  43.923  25.923  1.00 37.80           N  
-ATOM  29152  CA  THR H 172      11.819  44.227  27.348  1.00 35.18           C  
-ATOM  29153  C   THR H 172      12.746  43.291  28.119  1.00 33.36           C  
-ATOM  29154  O   THR H 172      12.453  42.107  28.272  1.00 37.55           O  
-ATOM  29155  CB  THR H 172      10.389  44.083  27.902  1.00 26.59           C  
-ATOM  29156  OG1 THR H 172       9.485  44.875  27.125  1.00 32.17           O  
-ATOM  29157  CG2 THR H 172      10.333  44.534  29.354  1.00 23.00           C  
-ATOM  29158  N   ARG H 173      13.866  43.822  28.597  1.00 27.97           N  
-ATOM  29159  CA  ARG H 173      14.836  43.019  29.331  1.00 25.85           C  
-ATOM  29160  C   ARG H 173      14.434  42.810  30.774  1.00 20.03           C  
-ATOM  29161  O   ARG H 173      14.686  43.658  31.620  1.00 19.76           O  
-ATOM  29162  CB  ARG H 173      16.214  43.671  29.290  1.00 26.59           C  
-ATOM  29163  CG  ARG H 173      16.708  43.973  27.906  1.00 24.21           C  
-ATOM  29164  CD  ARG H 173      17.586  45.194  27.924  1.00 27.67           C  
-ATOM  29165  NE  ARG H 173      19.001  44.860  27.991  1.00 29.15           N  
-ATOM  29166  CZ  ARG H 173      19.953  45.740  28.272  1.00 37.05           C  
-ATOM  29167  NH1 ARG H 173      19.631  47.001  28.530  1.00 26.45           N  
-ATOM  29168  NH2 ARG H 173      21.223  45.361  28.310  1.00 42.40           N  
-ATOM  29169  N   VAL H 174      13.815  41.670  31.049  1.00 17.72           N  
-ATOM  29170  CA  VAL H 174      13.559  41.259  32.423  1.00 23.14           C  
-ATOM  29171  C   VAL H 174      14.882  40.854  33.070  1.00 24.50           C  
-ATOM  29172  O   VAL H 174      15.575  39.971  32.567  1.00 22.10           O  
-ATOM  29173  CB  VAL H 174      12.562  40.090  32.490  1.00 20.99           C  
-ATOM  29174  CG1 VAL H 174      12.342  39.656  33.922  1.00 18.27           C  
-ATOM  29175  CG2 VAL H 174      11.248  40.493  31.844  1.00 25.06           C  
-ATOM  29176  N   ALA H 175      15.243  41.506  34.172  1.00 17.44           N  
-ATOM  29177  CA  ALA H 175      16.549  41.277  34.790  1.00 16.44           C  
-ATOM  29178  C   ALA H 175      16.605  39.974  35.589  1.00 26.14           C  
-ATOM  29179  O   ALA H 175      17.660  39.342  35.671  1.00 29.38           O  
-ATOM  29180  CB  ALA H 175      16.924  42.448  35.677  1.00 15.35           C  
-ATOM  29181  N   ARG H 176      15.479  39.583  36.182  1.00 24.42           N  
-ATOM  29182  CA  ARG H 176      15.399  38.329  36.926  1.00 19.44           C  
-ATOM  29183  C   ARG H 176      15.229  37.140  35.999  1.00 21.18           C  
-ATOM  29184  O   ARG H 176      14.602  37.249  34.947  1.00 20.68           O  
-ATOM  29185  CB  ARG H 176      14.235  38.353  37.911  1.00 18.30           C  
-ATOM  29186  CG  ARG H 176      14.368  39.355  39.029  1.00 24.16           C  
-ATOM  29187  CD  ARG H 176      13.145  39.300  39.931  1.00 25.99           C  
-ATOM  29188  NE  ARG H 176      12.930  37.965  40.483  1.00 23.46           N  
-ATOM  29189  CZ  ARG H 176      11.935  37.646  41.305  1.00 27.58           C  
-ATOM  29190  NH1 ARG H 176      11.817  36.404  41.754  1.00 42.58           N  
-ATOM  29191  NH2 ARG H 176      11.058  38.567  41.678  1.00 23.93           N  
-ATOM  29192  N   GLU H 177      15.785  36.001  36.394  1.00 26.45           N  
-ATOM  29193  CA  GLU H 177      15.513  34.759  35.687  1.00 31.27           C  
-ATOM  29194  C   GLU H 177      14.327  34.052  36.323  1.00 24.65           C  
-ATOM  29195  O   GLU H 177      14.118  34.123  37.535  1.00 22.99           O  
-ATOM  29196  CB  GLU H 177      16.734  33.838  35.684  1.00 31.98           C  
-ATOM  29197  CG  GLU H 177      17.537  33.856  34.391  1.00 33.09           C  
-ATOM  29198  CD  GLU H 177      18.877  34.557  34.541  1.00 61.43           C  
-ATOM  29199  OE1 GLU H 177      18.903  35.700  35.047  1.00 68.91           O  
-ATOM  29200  OE2 GLU H 177      19.907  33.959  34.159  1.00 61.01           O  
-ATOM  29201  N   PHE H 178      13.549  33.377  35.489  1.00 24.96           N  
-ATOM  29202  CA  PHE H 178      12.410  32.608  35.958  1.00 21.54           C  
-ATOM  29203  C   PHE H 178      12.389  31.255  35.263  1.00 20.69           C  
-ATOM  29204  O   PHE H 178      12.966  31.102  34.185  1.00 17.50           O  
-ATOM  29205  CB  PHE H 178      11.102  33.363  35.700  1.00 22.82           C  
-ATOM  29206  CG  PHE H 178      10.932  34.595  36.545  1.00 25.13           C  
-ATOM  29207  CD1 PHE H 178      10.418  34.504  37.830  1.00 33.33           C  
-ATOM  29208  CD2 PHE H 178      11.274  35.846  36.054  1.00 22.53           C  
-ATOM  29209  CE1 PHE H 178      10.254  35.636  38.611  1.00 31.52           C  
-ATOM  29210  CE2 PHE H 178      11.112  36.981  36.829  1.00 22.49           C  
-ATOM  29211  CZ  PHE H 178      10.601  36.875  38.108  1.00 30.37           C  
-ATOM  29212  N   PRO H 179      11.748  30.261  35.893  1.00 23.15           N  
-ATOM  29213  CA  PRO H 179      11.507  28.977  35.231  1.00 26.99           C  
-ATOM  29214  C   PRO H 179      10.765  29.157  33.911  1.00 21.70           C  
-ATOM  29215  O   PRO H 179       9.728  29.822  33.869  1.00 21.51           O  
-ATOM  29216  CB  PRO H 179      10.653  28.217  36.248  1.00 19.07           C  
-ATOM  29217  CG  PRO H 179      11.065  28.781  37.561  1.00 17.72           C  
-ATOM  29218  CD  PRO H 179      11.350  30.234  37.312  1.00 18.09           C  
-ATOM  29219  N   CYS H 180      11.306  28.580  32.844  1.00 23.02           N  
-ATOM  29220  CA  CYS H 180      10.703  28.691  31.524  1.00 25.10           C  
-ATOM  29221  C   CYS H 180      10.850  27.396  30.740  1.00 32.59           C  
-ATOM  29222  O   CYS H 180      11.784  26.623  30.960  1.00 38.68           O  
-ATOM  29223  CB  CYS H 180      11.334  29.840  30.734  1.00 23.76           C  
-ATOM  29224  SG  CYS H 180      11.060  31.481  31.422  1.00 21.56           S  
-ATOM  29225  N   ASP H 181       9.919  27.165  29.822  1.00 32.43           N  
-ATOM  29226  CA  ASP H 181      10.022  26.041  28.904  1.00 35.78           C  
-ATOM  29227  C   ASP H 181       9.915  26.531  27.460  1.00 30.59           C  
-ATOM  29228  O   ASP H 181       9.887  25.733  26.525  1.00 40.59           O  
-ATOM  29229  CB  ASP H 181       8.948  24.988  29.209  1.00 37.42           C  
-ATOM  29230  CG  ASP H 181       7.550  25.580  29.323  1.00 38.54           C  
-ATOM  29231  OD1 ASP H 181       7.264  26.589  28.644  1.00 44.13           O  
-ATOM  29232  OD2 ASP H 181       6.732  25.030  30.091  1.00 31.01           O  
-ATOM  29233  N   VAL H 182       9.849  27.849  27.290  1.00 24.07           N  
-ATOM  29234  CA  VAL H 182       9.777  28.455  25.963  1.00 32.92           C  
-ATOM  29235  C   VAL H 182      10.708  29.661  25.867  1.00 30.34           C  
-ATOM  29236  O   VAL H 182      10.607  30.601  26.656  1.00 31.19           O  
-ATOM  29237  CB  VAL H 182       8.339  28.894  25.608  1.00 29.52           C  
-ATOM  29238  CG1 VAL H 182       8.332  29.683  24.313  1.00 32.74           C  
-ATOM  29239  CG2 VAL H 182       7.422  27.689  25.498  1.00 29.62           C  
-ATOM  29240  N   PHE H 183      11.605  29.636  24.888  1.00 28.77           N  
-ATOM  29241  CA  PHE H 183      12.655  30.644  24.799  1.00 29.18           C  
-ATOM  29242  C   PHE H 183      12.668  31.402  23.476  1.00 37.09           C  
-ATOM  29243  O   PHE H 183      12.245  30.884  22.442  1.00 35.36           O  
-ATOM  29244  CB  PHE H 183      14.021  29.992  25.020  1.00 28.45           C  
-ATOM  29245  CG  PHE H 183      14.199  29.408  26.391  1.00 26.13           C  
-ATOM  29246  CD1 PHE H 183      13.682  28.162  26.702  1.00 26.19           C  
-ATOM  29247  CD2 PHE H 183      14.892  30.102  27.366  1.00 24.30           C  
-ATOM  29248  CE1 PHE H 183      13.847  27.623  27.962  1.00 26.20           C  
-ATOM  29249  CE2 PHE H 183      15.061  29.569  28.627  1.00 24.56           C  
-ATOM  29250  CZ  PHE H 183      14.538  28.327  28.926  1.00 25.06           C  
-ATOM  29251  N   PHE H 184      13.170  32.633  23.526  1.00 36.35           N  
-ATOM  29252  CA  PHE H 184      13.412  33.426  22.326  1.00 34.19           C  
-ATOM  29253  C   PHE H 184      14.692  32.937  21.650  1.00 34.11           C  
-ATOM  29254  O   PHE H 184      15.696  32.695  22.320  1.00 32.01           O  
-ATOM  29255  CB  PHE H 184      13.515  34.915  22.674  1.00 31.79           C  
-ATOM  29256  CG  PHE H 184      13.494  35.826  21.475  1.00 38.70           C  
-ATOM  29257  CD1 PHE H 184      12.293  36.282  20.954  1.00 33.46           C  
-ATOM  29258  CD2 PHE H 184      14.675  36.231  20.874  1.00 34.29           C  
-ATOM  29259  CE1 PHE H 184      12.272  37.119  19.855  1.00 26.86           C  
-ATOM  29260  CE2 PHE H 184      14.658  37.070  19.775  1.00 29.69           C  
-ATOM  29261  CZ  PHE H 184      13.455  37.514  19.266  1.00 29.03           C  
-ATOM  29262  N   PRO H 185      14.656  32.783  20.319  1.00 32.50           N  
-ATOM  29263  CA  PRO H 185      15.779  32.244  19.544  1.00 33.12           C  
-ATOM  29264  C   PRO H 185      17.066  33.043  19.715  1.00 27.67           C  
-ATOM  29265  O   PRO H 185      17.019  34.265  19.845  1.00 28.17           O  
-ATOM  29266  CB  PRO H 185      15.281  32.334  18.099  1.00 36.74           C  
-ATOM  29267  CG  PRO H 185      13.802  32.363  18.210  1.00 34.89           C  
-ATOM  29268  CD  PRO H 185      13.504  33.109  19.463  1.00 32.33           C  
-ATOM  29269  N   ALA H 186      18.200  32.349  19.721  1.00 29.79           N  
-ATOM  29270  CA  ALA H 186      19.498  33.007  19.802  1.00 39.03           C  
-ATOM  29271  C   ALA H 186      19.740  33.828  18.541  1.00 44.36           C  
-ATOM  29272  O   ALA H 186      19.349  33.425  17.445  1.00 48.38           O  
-ATOM  29273  CB  ALA H 186      20.608  31.985  20.000  1.00 29.82           C  
-ATOM  29274  N   PHE H 187      20.382  34.980  18.699  1.00 46.33           N  
-ATOM  29275  CA  PHE H 187      20.594  35.892  17.581  1.00 47.49           C  
-ATOM  29276  C   PHE H 187      21.823  36.766  17.809  1.00 49.36           C  
-ATOM  29277  O   PHE H 187      22.212  36.998  18.954  1.00 52.78           O  
-ATOM  29278  CB  PHE H 187      19.356  36.767  17.368  1.00 44.22           C  
-ATOM  29279  CG  PHE H 187      19.034  37.657  18.536  1.00 39.96           C  
-ATOM  29280  CD1 PHE H 187      18.279  37.184  19.597  1.00 33.58           C  
-ATOM  29281  CD2 PHE H 187      19.483  38.967  18.572  1.00 42.07           C  
-ATOM  29282  CE1 PHE H 187      17.983  37.998  20.672  1.00 34.22           C  
-ATOM  29283  CE2 PHE H 187      19.189  39.787  19.646  1.00 36.50           C  
-ATOM  29284  CZ  PHE H 187      18.438  39.302  20.696  1.00 31.78           C  
-ATOM  29285  N   PRO H 188      22.445  37.248  16.718  1.00 42.67           N  
-ATOM  29286  CA  PRO H 188      23.572  38.179  16.823  1.00 43.20           C  
-ATOM  29287  C   PRO H 188      23.164  39.482  17.489  1.00 49.83           C  
-ATOM  29288  O   PRO H 188      22.286  40.184  16.982  1.00 48.86           O  
-ATOM  29289  CB  PRO H 188      23.967  38.423  15.365  1.00 46.38           C  
-ATOM  29290  CG  PRO H 188      23.492  37.241  14.651  1.00 51.48           C  
-ATOM  29291  CD  PRO H 188      22.208  36.854  15.321  1.00 52.55           C  
-ATOM  29292  N   GLY H 189      23.804  39.797  18.609  1.00 42.77           N  
-ATOM  29293  CA  GLY H 189      23.427  40.943  19.412  1.00 39.38           C  
-ATOM  29294  C   GLY H 189      22.989  40.457  20.777  1.00 46.90           C  
-ATOM  29295  O   GLY H 189      22.713  41.250  21.682  1.00 57.95           O  
-ATOM  29296  N   ASP H 190      22.951  39.134  20.925  1.00 45.74           N  
-ATOM  29297  CA  ASP H 190      22.560  38.479  22.170  1.00 36.22           C  
-ATOM  29298  C   ASP H 190      23.286  39.047  23.390  1.00 42.68           C  
-ATOM  29299  O   ASP H 190      22.798  38.942  24.517  1.00 44.71           O  
-ATOM  29300  CB  ASP H 190      22.814  36.972  22.066  1.00 43.20           C  
-ATOM  29301  CG  ASP H 190      21.554  36.155  22.285  1.00 63.21           C  
-ATOM  29302  OD1 ASP H 190      20.466  36.764  22.360  1.00 69.93           O  
-ATOM  29303  OD2 ASP H 190      21.645  34.912  22.378  1.00 66.51           O  
-ATOM  29304  N   ASP H 191      24.442  39.658  23.146  1.00 44.86           N  
-ATOM  29305  CA  ASP H 191      25.230  40.319  24.178  1.00 42.39           C  
-ATOM  29306  C   ASP H 191      24.436  41.308  25.024  1.00 44.61           C  
-ATOM  29307  O   ASP H 191      24.844  41.628  26.138  1.00 47.75           O  
-ATOM  29308  CB  ASP H 191      26.411  41.048  23.542  1.00 46.04           C  
-ATOM  29309  CG  ASP H 191      27.721  40.324  23.749  1.00 75.89           C  
-ATOM  29310  OD1 ASP H 191      27.697  39.103  24.024  1.00 83.85           O  
-ATOM  29311  OD2 ASP H 191      28.777  40.983  23.634  1.00 68.42           O  
-ATOM  29312  N   ILE H 192      23.312  41.799  24.501  1.00 41.15           N  
-ATOM  29313  CA  ILE H 192      22.518  42.801  25.221  1.00 38.43           C  
-ATOM  29314  C   ILE H 192      21.689  42.174  26.353  1.00 32.39           C  
-ATOM  29315  O   ILE H 192      21.134  42.880  27.197  1.00 34.76           O  
-ATOM  29316  CB  ILE H 192      21.598  43.575  24.244  1.00 35.98           C  
-ATOM  29317  CG1 ILE H 192      22.409  44.017  23.028  1.00 60.97           C  
-ATOM  29318  CG2 ILE H 192      20.978  44.798  24.908  1.00 31.80           C  
-ATOM  29319  CD1 ILE H 192      21.572  44.591  21.923  1.00 64.65           C  
-ATOM  29320  N   LEU H 193      21.625  40.847  26.386  1.00 27.31           N  
-ATOM  29321  CA  LEU H 193      20.869  40.162  27.432  1.00 24.27           C  
-ATOM  29322  C   LEU H 193      21.761  39.707  28.589  1.00 30.78           C  
-ATOM  29323  O   LEU H 193      21.441  39.940  29.755  1.00 32.30           O  
-ATOM  29324  CB  LEU H 193      20.118  38.976  26.839  1.00 19.88           C  
-ATOM  29325  CG  LEU H 193      19.134  39.384  25.744  1.00 21.83           C  
-ATOM  29326  CD1 LEU H 193      18.708  38.174  24.953  1.00 24.34           C  
-ATOM  29327  CD2 LEU H 193      17.920  40.105  26.317  1.00 13.52           C  
-ATOM  29328  N   SER H 194      22.874  39.057  28.264  1.00 32.73           N  
-ATOM  29329  CA  SER H 194      23.865  38.675  29.267  1.00 32.29           C  
-ATOM  29330  C   SER H 194      25.191  38.354  28.583  1.00 44.99           C  
-ATOM  29331  O   SER H 194      25.353  38.613  27.391  1.00 52.05           O  
-ATOM  29332  CB  SER H 194      23.377  37.488  30.101  1.00 30.06           C  
-ATOM  29333  OG  SER H 194      22.823  36.475  29.282  1.00 36.05           O  
-ATOM  29334  N   ASN H 195      26.138  37.796  29.334  1.00 42.68           N  
-ATOM  29335  CA  ASN H 195      27.500  37.612  28.833  1.00 38.33           C  
-ATOM  29336  C   ASN H 195      27.679  36.371  27.952  1.00 52.41           C  
-ATOM  29337  O   ASN H 195      28.768  35.791  27.900  1.00 50.08           O  
-ATOM  29338  CB  ASN H 195      28.479  37.559  30.010  1.00 34.73           C  
-ATOM  29339  CG  ASN H 195      28.457  38.832  30.841  1.00 35.75           C  
-ATOM  29340  OD1 ASN H 195      27.895  39.843  30.424  1.00 36.42           O  
-ATOM  29341  ND2 ASN H 195      29.078  38.791  32.014  1.00 39.22           N  
-ATOM  29342  N   LYS H 196      26.614  35.979  27.255  1.00 62.48           N  
-ATOM  29343  CA  LYS H 196      26.661  34.828  26.355  1.00 58.33           C  
-ATOM  29344  C   LYS H 196      27.685  35.059  25.250  1.00 46.61           C  
-ATOM  29345  O   LYS H 196      28.829  34.624  25.358  1.00 35.39           O  
-ATOM  29346  CB  LYS H 196      25.282  34.543  25.742  1.00 64.79           C  
-ATOM  29347  CG  LYS H 196      24.445  33.520  26.498  1.00 82.31           C  
-ATOM  29348  CD  LYS H 196      24.159  33.982  27.912  1.00 86.56           C  
-ATOM  29349  CE  LYS H 196      23.247  33.015  28.640  1.00 79.09           C  
-ATOM  29350  NZ  LYS H 196      22.921  33.510  30.005  1.00 55.70           N  
-ATOM  29351  N   GLU H 224      27.747  39.641   7.628  1.00 79.17           N  
-ATOM  29352  CA  GLU H 224      26.959  38.949   8.641  1.00 83.88           C  
-ATOM  29353  C   GLU H 224      25.973  39.904   9.307  1.00 92.17           C  
-ATOM  29354  O   GLU H 224      26.372  40.920   9.878  1.00 84.60           O  
-ATOM  29355  CB  GLU H 224      27.874  38.317   9.692  1.00 80.74           C  
-ATOM  29356  CG  GLU H 224      27.221  37.200  10.487  1.00 87.75           C  
-ATOM  29357  CD  GLU H 224      26.956  35.969   9.642  1.00 90.53           C  
-ATOM  29358  OE1 GLU H 224      25.837  35.849   9.097  1.00 74.83           O  
-ATOM  29359  OE2 GLU H 224      27.869  35.125   9.520  1.00 71.88           O  
-ATOM  29360  N   ALA H 225      24.687  39.572   9.233  1.00 86.90           N  
-ATOM  29361  CA  ALA H 225      23.644  40.419   9.805  1.00 74.22           C  
-ATOM  29362  C   ALA H 225      23.677  40.385  11.329  1.00 74.79           C  
-ATOM  29363  O   ALA H 225      23.744  39.315  11.935  1.00 75.16           O  
-ATOM  29364  CB  ALA H 225      22.277  39.992   9.297  1.00 55.21           C  
-ATOM  29365  N   THR H 226      23.628  41.563  11.943  1.00 65.59           N  
-ATOM  29366  CA  THR H 226      23.670  41.664  13.396  1.00 57.56           C  
-ATOM  29367  C   THR H 226      22.735  42.759  13.905  1.00 54.42           C  
-ATOM  29368  O   THR H 226      22.417  43.711  13.187  1.00 49.34           O  
-ATOM  29369  CB  THR H 226      25.104  41.939  13.901  1.00 50.62           C  
-ATOM  29370  OG1 THR H 226      25.167  41.723  15.316  1.00 54.57           O  
-ATOM  29371  CG2 THR H 226      25.527  43.368  13.582  1.00 51.10           C  
-ATOM  29372  N   TYR H 227      22.295  42.611  15.150  1.00 45.92           N  
-ATOM  29373  CA  TYR H 227      21.355  43.546  15.754  1.00 39.22           C  
-ATOM  29374  C   TYR H 227      22.036  44.497  16.729  1.00 46.94           C  
-ATOM  29375  O   TYR H 227      22.442  44.098  17.822  1.00 50.16           O  
-ATOM  29376  CB  TYR H 227      20.238  42.786  16.468  1.00 38.30           C  
-ATOM  29377  CG  TYR H 227      19.242  42.141  15.534  1.00 42.18           C  
-ATOM  29378  CD1 TYR H 227      18.145  42.852  15.065  1.00 43.49           C  
-ATOM  29379  CD2 TYR H 227      19.395  40.824  15.119  1.00 40.86           C  
-ATOM  29380  CE1 TYR H 227      17.230  42.272  14.212  1.00 42.17           C  
-ATOM  29381  CE2 TYR H 227      18.482  40.235  14.264  1.00 39.43           C  
-ATOM  29382  CZ  TYR H 227      17.402  40.966  13.813  1.00 40.05           C  
-ATOM  29383  OH  TYR H 227      16.483  40.396  12.962  1.00 50.67           O  
-ATOM  29384  N   ARG H 228      22.154  45.758  16.329  1.00 45.80           N  
-ATOM  29385  CA  ARG H 228      22.743  46.772  17.192  1.00 44.76           C  
-ATOM  29386  C   ARG H 228      21.654  47.541  17.934  1.00 45.26           C  
-ATOM  29387  O   ARG H 228      20.640  47.912  17.343  1.00 47.35           O  
-ATOM  29388  CB  ARG H 228      23.617  47.731  16.378  1.00 50.16           C  
-ATOM  29389  CG  ARG H 228      25.096  47.695  16.748  1.00 55.18           C  
-ATOM  29390  CD  ARG H 228      25.975  47.581  15.509  1.00 68.50           C  
-ATOM  29391  NE  ARG H 228      25.681  48.619  14.524  1.00 77.25           N  
-ATOM  29392  CZ  ARG H 228      26.352  49.762  14.417  1.00 71.70           C  
-ATOM  29393  NH1 ARG H 228      27.366  50.020  15.233  1.00 65.73           N  
-ATOM  29394  NH2 ARG H 228      26.010  50.648  13.490  1.00 49.83           N  
-ATOM  29395  N   PRO H 229      21.856  47.770  19.241  1.00 43.41           N  
-ATOM  29396  CA  PRO H 229      20.903  48.556  20.027  1.00 33.85           C  
-ATOM  29397  C   PRO H 229      20.998  50.041  19.694  1.00 44.61           C  
-ATOM  29398  O   PRO H 229      22.070  50.530  19.332  1.00 47.35           O  
-ATOM  29399  CB  PRO H 229      21.328  48.283  21.470  1.00 27.53           C  
-ATOM  29400  CG  PRO H 229      22.777  47.993  21.380  1.00 39.10           C  
-ATOM  29401  CD  PRO H 229      22.991  47.304  20.056  1.00 48.68           C  
-ATOM  29402  N   ILE H 230      19.880  50.746  19.823  1.00 38.20           N  
-ATOM  29403  CA  ILE H 230      19.792  52.140  19.415  1.00 36.95           C  
-ATOM  29404  C   ILE H 230      19.101  52.947  20.517  1.00 34.51           C  
-ATOM  29405  O   ILE H 230      19.228  54.176  20.613  1.00 35.31           O  
-ATOM  29406  CB  ILE H 230      19.021  52.258  18.078  1.00 29.79           C  
-ATOM  29407  CG1 ILE H 230      19.817  53.066  17.054  1.00 50.97           C  
-ATOM  29408  CG2 ILE H 230      17.621  52.810  18.291  1.00 35.56           C  
-ATOM  29409  CD1 ILE H 230      20.806  52.234  16.256  1.00 49.58           C  
-ATOM  29410  N   PHE H 231      18.396  52.207  21.365  1.00 32.09           N  
-ATOM  29411  CA  PHE H 231      17.536  52.752  22.397  1.00 33.58           C  
-ATOM  29412  C   PHE H 231      17.751  51.950  23.671  1.00 33.25           C  
-ATOM  29413  O   PHE H 231      17.563  50.740  23.672  1.00 36.25           O  
-ATOM  29414  CB  PHE H 231      16.072  52.687  21.944  1.00 35.84           C  
-ATOM  29415  CG  PHE H 231      15.083  53.182  22.963  1.00 37.46           C  
-ATOM  29416  CD1 PHE H 231      14.657  52.370  24.001  1.00 34.26           C  
-ATOM  29417  CD2 PHE H 231      14.551  54.451  22.859  1.00 51.28           C  
-ATOM  29418  CE1 PHE H 231      13.745  52.831  24.928  1.00 35.97           C  
-ATOM  29419  CE2 PHE H 231      13.639  54.917  23.780  1.00 55.18           C  
-ATOM  29420  CZ  PHE H 231      13.234  54.106  24.816  1.00 34.62           C  
-ATOM  29421  N   ILE H 232      18.164  52.607  24.747  1.00 33.04           N  
-ATOM  29422  CA  ILE H 232      18.252  51.937  26.043  1.00 28.97           C  
-ATOM  29423  C   ILE H 232      17.655  52.833  27.116  1.00 28.93           C  
-ATOM  29424  O   ILE H 232      18.127  53.949  27.333  1.00 26.72           O  
-ATOM  29425  CB  ILE H 232      19.699  51.573  26.425  1.00 31.89           C  
-ATOM  29426  CG1 ILE H 232      20.261  50.519  25.471  1.00 20.83           C  
-ATOM  29427  CG2 ILE H 232      19.753  51.047  27.856  1.00 31.24           C  
-ATOM  29428  CD1 ILE H 232      21.649  50.060  25.830  1.00 21.47           C  
-ATOM  29429  N   SER H 233      16.626  52.331  27.792  1.00 27.91           N  
-ATOM  29430  CA  SER H 233      15.822  53.154  28.688  1.00 28.65           C  
-ATOM  29431  C   SER H 233      16.237  53.076  30.151  1.00 25.28           C  
-ATOM  29432  O   SER H 233      17.105  52.292  30.534  1.00 27.19           O  
-ATOM  29433  CB  SER H 233      14.347  52.760  28.575  1.00 35.89           C  
-ATOM  29434  OG  SER H 233      14.099  51.518  29.215  1.00 25.23           O  
-ATOM  29435  N   LYS H 234      15.592  53.910  30.958  1.00 24.29           N  
-ATOM  29436  CA  LYS H 234      15.710  53.872  32.408  1.00 27.58           C  
-ATOM  29437  C   LYS H 234      15.229  52.512  32.914  1.00 31.94           C  
-ATOM  29438  O   LYS H 234      14.433  51.848  32.251  1.00 36.07           O  
-ATOM  29439  CB  LYS H 234      14.895  55.016  33.023  1.00 32.61           C  
-ATOM  29440  CG  LYS H 234      14.845  55.063  34.539  1.00 40.83           C  
-ATOM  29441  CD  LYS H 234      13.447  55.444  35.006  1.00 46.87           C  
-ATOM  29442  CE  LYS H 234      12.917  56.653  34.245  1.00 44.07           C  
-ATOM  29443  NZ  LYS H 234      11.447  56.823  34.411  1.00 42.44           N  
-ATOM  29444  N   THR H 235      15.721  52.085  34.073  1.00 33.16           N  
-ATOM  29445  CA  THR H 235      15.291  50.814  34.644  1.00 29.49           C  
-ATOM  29446  C   THR H 235      13.976  50.966  35.407  1.00 24.45           C  
-ATOM  29447  O   THR H 235      13.846  51.833  36.274  1.00 24.03           O  
-ATOM  29448  CB  THR H 235      16.361  50.228  35.581  1.00 24.01           C  
-ATOM  29449  OG1 THR H 235      17.589  50.060  34.860  1.00 21.53           O  
-ATOM  29450  CG2 THR H 235      15.908  48.882  36.118  1.00 28.76           C  
-ATOM  29451  N   PHE H 236      13.001  50.125  35.073  1.00 23.85           N  
-ATOM  29452  CA  PHE H 236      11.702  50.153  35.739  1.00 24.38           C  
-ATOM  29453  C   PHE H 236      11.534  48.933  36.634  1.00 25.87           C  
-ATOM  29454  O   PHE H 236      12.366  48.031  36.620  1.00 29.85           O  
-ATOM  29455  CB  PHE H 236      10.569  50.219  34.713  1.00 25.56           C  
-ATOM  29456  CG  PHE H 236      10.549  51.491  33.920  1.00 26.58           C  
-ATOM  29457  CD1 PHE H 236       9.846  52.594  34.376  1.00 36.61           C  
-ATOM  29458  CD2 PHE H 236      11.238  51.590  32.725  1.00 24.18           C  
-ATOM  29459  CE1 PHE H 236       9.828  53.769  33.654  1.00 37.33           C  
-ATOM  29460  CE2 PHE H 236      11.224  52.763  31.997  1.00 36.82           C  
-ATOM  29461  CZ  PHE H 236      10.517  53.855  32.463  1.00 44.37           C  
-ATOM  29462  N   SER H 237      10.460  48.907  37.417  1.00 35.32           N  
-ATOM  29463  CA  SER H 237      10.228  47.798  38.339  1.00 29.51           C  
-ATOM  29464  C   SER H 237       8.754  47.586  38.650  1.00 34.61           C  
-ATOM  29465  O   SER H 237       8.017  48.542  38.899  1.00 30.57           O  
-ATOM  29466  CB  SER H 237      10.979  48.026  39.649  1.00 30.92           C  
-ATOM  29467  OG  SER H 237      10.304  48.984  40.453  1.00 30.21           O  
-ATOM  29468  N   ASP H 238       8.336  46.325  38.648  1.00 33.07           N  
-ATOM  29469  CA  ASP H 238       6.994  45.961  39.085  1.00 31.81           C  
-ATOM  29470  C   ASP H 238       6.990  44.600  39.772  1.00 29.04           C  
-ATOM  29471  O   ASP H 238       7.570  43.637  39.266  1.00 27.66           O  
-ATOM  29472  CB  ASP H 238       6.017  45.961  37.909  1.00 32.21           C  
-ATOM  29473  CG  ASP H 238       5.560  47.356  37.532  1.00 37.01           C  
-ATOM  29474  OD1 ASP H 238       4.684  47.910  38.233  1.00 36.73           O  
-ATOM  29475  OD2 ASP H 238       6.074  47.901  36.533  1.00 35.77           O  
-ATOM  29476  N   ASN H 239       6.333  44.541  40.928  1.00 30.26           N  
-ATOM  29477  CA  ASN H 239       6.202  43.313  41.710  1.00 30.72           C  
-ATOM  29478  C   ASN H 239       7.544  42.677  42.058  1.00 27.10           C  
-ATOM  29479  O   ASN H 239       7.647  41.457  42.190  1.00 23.49           O  
-ATOM  29480  CB  ASN H 239       5.326  42.302  40.965  1.00 27.30           C  
-ATOM  29481  CG  ASN H 239       3.880  42.752  40.855  1.00 30.53           C  
-ATOM  29482  OD1 ASN H 239       3.274  43.182  41.837  1.00 31.49           O  
-ATOM  29483  ND2 ASN H 239       3.323  42.661  39.652  1.00 34.69           N  
-ATOM  29484  N   GLY H 240       8.568  43.510  42.211  1.00 22.51           N  
-ATOM  29485  CA  GLY H 240       9.887  43.029  42.577  1.00 31.50           C  
-ATOM  29486  C   GLY H 240      10.690  42.567  41.377  1.00 31.13           C  
-ATOM  29487  O   GLY H 240      11.709  41.887  41.519  1.00 26.78           O  
-ATOM  29488  N   VAL H 241      10.222  42.937  40.188  1.00 29.86           N  
-ATOM  29489  CA  VAL H 241      10.907  42.599  38.946  1.00 24.80           C  
-ATOM  29490  C   VAL H 241      11.406  43.854  38.245  1.00 25.33           C  
-ATOM  29491  O   VAL H 241      10.611  44.699  37.828  1.00 28.83           O  
-ATOM  29492  CB  VAL H 241       9.995  41.823  37.979  1.00 24.05           C  
-ATOM  29493  CG1 VAL H 241      10.802  41.298  36.801  1.00 19.85           C  
-ATOM  29494  CG2 VAL H 241       9.299  40.686  38.706  1.00 27.24           C  
-ATOM  29495  N   PRO H 242      12.734  43.986  38.130  1.00 17.23           N  
-ATOM  29496  CA  PRO H 242      13.365  45.080  37.389  1.00 22.34           C  
-ATOM  29497  C   PRO H 242      13.449  44.774  35.898  1.00 20.33           C  
-ATOM  29498  O   PRO H 242      13.778  43.647  35.540  1.00 21.24           O  
-ATOM  29499  CB  PRO H 242      14.759  45.155  38.011  1.00 18.43           C  
-ATOM  29500  CG  PRO H 242      15.042  43.746  38.422  1.00 16.10           C  
-ATOM  29501  CD  PRO H 242      13.721  43.165  38.853  1.00 16.72           C  
-ATOM  29502  N   TYR H 243      13.153  45.746  35.041  1.00 20.32           N  
-ATOM  29503  CA  TYR H 243      13.305  45.515  33.610  1.00 27.65           C  
-ATOM  29504  C   TYR H 243      13.673  46.760  32.804  1.00 29.50           C  
-ATOM  29505  O   TYR H 243      13.577  47.891  33.283  1.00 23.86           O  
-ATOM  29506  CB  TYR H 243      12.036  44.873  33.025  1.00 21.45           C  
-ATOM  29507  CG  TYR H 243      10.723  45.537  33.367  1.00 18.60           C  
-ATOM  29508  CD1 TYR H 243      10.075  45.256  34.561  1.00 25.19           C  
-ATOM  29509  CD2 TYR H 243      10.106  46.409  32.477  1.00 25.71           C  
-ATOM  29510  CE1 TYR H 243       8.863  45.845  34.874  1.00 28.90           C  
-ATOM  29511  CE2 TYR H 243       8.892  47.002  32.783  1.00 26.49           C  
-ATOM  29512  CZ  TYR H 243       8.277  46.714  33.982  1.00 24.54           C  
-ATOM  29513  OH  TYR H 243       7.072  47.297  34.293  1.00 23.24           O  
-ATOM  29514  N   ASP H 244      14.114  46.517  31.573  1.00 29.63           N  
-ATOM  29515  CA  ASP H 244      14.573  47.568  30.675  1.00 23.19           C  
-ATOM  29516  C   ASP H 244      13.784  47.556  29.377  1.00 33.27           C  
-ATOM  29517  O   ASP H 244      13.106  46.581  29.065  1.00 34.33           O  
-ATOM  29518  CB  ASP H 244      16.060  47.393  30.370  1.00 25.44           C  
-ATOM  29519  CG  ASP H 244      16.902  48.532  30.897  1.00 37.33           C  
-ATOM  29520  OD1 ASP H 244      16.434  49.246  31.809  1.00 40.78           O  
-ATOM  29521  OD2 ASP H 244      18.036  48.708  30.401  1.00 39.60           O  
-ATOM  29522  N   PHE H 245      13.878  48.643  28.622  1.00 37.19           N  
-ATOM  29523  CA  PHE H 245      13.315  48.689  27.279  1.00 27.88           C  
-ATOM  29524  C   PHE H 245      14.400  49.047  26.280  1.00 29.75           C  
-ATOM  29525  O   PHE H 245      14.962  50.140  26.330  1.00 31.82           O  
-ATOM  29526  CB  PHE H 245      12.166  49.697  27.190  1.00 21.08           C  
-ATOM  29527  CG  PHE H 245      11.021  49.392  28.104  1.00 34.16           C  
-ATOM  29528  CD1 PHE H 245      10.284  48.232  27.949  1.00 27.86           C  
-ATOM  29529  CD2 PHE H 245      10.669  50.275  29.111  1.00 43.48           C  
-ATOM  29530  CE1 PHE H 245       9.225  47.952  28.790  1.00 32.01           C  
-ATOM  29531  CE2 PHE H 245       9.610  50.003  29.955  1.00 37.42           C  
-ATOM  29532  CZ  PHE H 245       8.887  48.838  29.794  1.00 29.37           C  
-ATOM  29533  N   VAL H 246      14.699  48.123  25.374  1.00 26.69           N  
-ATOM  29534  CA  VAL H 246      15.675  48.397  24.330  1.00 27.36           C  
-ATOM  29535  C   VAL H 246      15.083  48.184  22.948  1.00 27.31           C  
-ATOM  29536  O   VAL H 246      14.178  47.373  22.769  1.00 29.45           O  
-ATOM  29537  CB  VAL H 246      16.935  47.525  24.472  1.00 20.93           C  
-ATOM  29538  CG1 VAL H 246      17.716  47.933  25.709  1.00 26.73           C  
-ATOM  29539  CG2 VAL H 246      16.565  46.052  24.512  1.00 18.41           C  
-ATOM  29540  N   VAL H 247      15.590  48.936  21.978  1.00 31.36           N  
-ATOM  29541  CA  VAL H 247      15.198  48.766  20.587  1.00 30.84           C  
-ATOM  29542  C   VAL H 247      16.438  48.480  19.746  1.00 32.22           C  
-ATOM  29543  O   VAL H 247      17.398  49.249  19.756  1.00 33.22           O  
-ATOM  29544  CB  VAL H 247      14.464  50.007  20.041  1.00 33.41           C  
-ATOM  29545  CG1 VAL H 247      13.864  49.706  18.677  1.00 42.38           C  
-ATOM  29546  CG2 VAL H 247      13.380  50.454  21.008  1.00 34.43           C  
-ATOM  29547  N   LEU H 248      16.415  47.360  19.034  1.00 30.84           N  
-ATOM  29548  CA  LEU H 248      17.544  46.940  18.213  1.00 30.51           C  
-ATOM  29549  C   LEU H 248      17.201  47.098  16.741  1.00 38.77           C  
-ATOM  29550  O   LEU H 248      16.029  47.107  16.376  1.00 41.30           O  
-ATOM  29551  CB  LEU H 248      17.918  45.485  18.504  1.00 35.37           C  
-ATOM  29552  CG  LEU H 248      18.769  45.111  19.719  1.00 30.17           C  
-ATOM  29553  CD1 LEU H 248      18.188  45.646  21.017  1.00 28.17           C  
-ATOM  29554  CD2 LEU H 248      18.899  43.599  19.786  1.00 35.37           C  
-ATOM  29555  N   GLU H 249      18.221  47.225  15.898  1.00 42.80           N  
-ATOM  29556  CA  GLU H 249      18.010  47.272  14.456  1.00 37.88           C  
-ATOM  29557  C   GLU H 249      19.050  46.422  13.737  1.00 45.72           C  
-ATOM  29558  O   GLU H 249      20.147  46.203  14.257  1.00 56.70           O  
-ATOM  29559  CB  GLU H 249      18.057  48.712  13.940  1.00 32.30           C  
-ATOM  29560  CG  GLU H 249      19.448  49.333  13.909  1.00 42.82           C  
-ATOM  29561  CD  GLU H 249      19.468  50.668  13.185  1.00 59.30           C  
-ATOM  29562  OE1 GLU H 249      18.376  51.167  12.833  1.00 58.24           O  
-ATOM  29563  OE2 GLU H 249      20.570  51.217  12.964  1.00 52.63           O  
-ATOM  29564  N   LYS H 250      18.702  45.935  12.549  1.00 37.34           N  
-ATOM  29565  CA  LYS H 250      19.661  45.193  11.734  1.00 39.63           C  
-ATOM  29566  C   LYS H 250      20.698  46.121  11.106  1.00 46.88           C  
-ATOM  29567  O   LYS H 250      20.367  47.207  10.630  1.00 47.92           O  
-ATOM  29568  CB  LYS H 250      18.950  44.399  10.639  1.00 45.98           C  
-ATOM  29569  CG  LYS H 250      18.463  43.033  11.081  1.00 49.11           C  
-ATOM  29570  CD  LYS H 250      18.109  42.159   9.889  1.00 50.73           C  
-ATOM  29571  CE  LYS H 250      17.004  42.779   9.050  1.00 57.55           C  
-ATOM  29572  NZ  LYS H 250      16.615  41.901   7.912  1.00 52.11           N  
-ATOM  29573  N   ARG H 251      21.953  45.684  11.107  1.00 49.93           N  
-ATOM  29574  CA  ARG H 251      23.034  46.462  10.512  1.00 62.06           C  
-ATOM  29575  C   ARG H 251      24.091  45.578   9.850  1.00 56.75           C  
-ATOM  29576  O   ARG H 251      23.925  44.365   9.734  1.00 46.64           O  
-ATOM  29577  CB  ARG H 251      23.691  47.357  11.567  1.00 56.31           C  
-ATOM  29578  CG  ARG H 251      23.139  48.774  11.607  1.00 61.31           C  
-ATOM  29579  CD  ARG H 251      23.260  49.455  10.244  1.00 78.22           C  
-ATOM  29580  NE  ARG H 251      24.624  49.395   9.720  1.00 90.02           N  
-ATOM  29581  CZ  ARG H 251      24.947  48.978   8.497  1.00 92.80           C  
-ATOM  29582  NH1 ARG H 251      26.220  48.960   8.119  1.00 81.00           N  
-ATOM  29583  NH2 ARG H 251      24.005  48.580   7.650  1.00 77.91           N  
-ATOM  29584  N   SER H 285      13.828  82.748  10.233  1.00 67.48           N  
-ATOM  29585  CA  SER H 285      14.127  84.174  10.134  1.00 70.76           C  
-ATOM  29586  C   SER H 285      15.115  84.609  11.207  1.00 56.27           C  
-ATOM  29587  O   SER H 285      16.185  85.129  10.900  1.00 46.35           O  
-ATOM  29588  CB  SER H 285      12.846  85.008  10.241  1.00 74.04           C  
-ATOM  29589  OG  SER H 285      11.962  84.750   9.163  1.00 75.70           O  
-ATOM  29590  N   SER H 286      14.746  84.399  12.466  1.00 61.78           N  
-ATOM  29591  CA  SER H 286      15.592  84.788  13.587  1.00 57.82           C  
-ATOM  29592  C   SER H 286      16.788  83.849  13.736  1.00 55.19           C  
-ATOM  29593  O   SER H 286      17.855  84.259  14.192  1.00 50.15           O  
-ATOM  29594  CB  SER H 286      14.778  84.816  14.878  1.00 41.63           C  
-ATOM  29595  OG  SER H 286      14.364  83.514  15.221  1.00 61.06           O  
-ATOM  29596  N   ALA H 287      16.604  82.588  13.358  1.00 57.60           N  
-ATOM  29597  CA  ALA H 287      17.693  81.617  13.408  1.00 54.86           C  
-ATOM  29598  C   ALA H 287      18.796  82.020  12.433  1.00 50.82           C  
-ATOM  29599  O   ALA H 287      19.987  81.843  12.708  1.00 46.26           O  
-ATOM  29600  CB  ALA H 287      17.183  80.216  13.092  1.00 49.03           C  
-ATOM  29601  N   ALA H 288      18.386  82.577  11.297  1.00 46.08           N  
-ATOM  29602  CA  ALA H 288      19.327  83.035  10.285  1.00 49.89           C  
-ATOM  29603  C   ALA H 288      20.090  84.252  10.789  1.00 43.74           C  
-ATOM  29604  O   ALA H 288      21.284  84.395  10.533  1.00 43.26           O  
-ATOM  29605  CB  ALA H 288      18.605  83.355   8.987  1.00 63.25           C  
-ATOM  29606  N   ALA H 289      19.394  85.126  11.508  1.00 34.52           N  
-ATOM  29607  CA  ALA H 289      20.023  86.303  12.097  1.00 32.31           C  
-ATOM  29608  C   ALA H 289      21.021  85.912  13.179  1.00 34.75           C  
-ATOM  29609  O   ALA H 289      22.072  86.534  13.321  1.00 38.26           O  
-ATOM  29610  CB  ALA H 289      18.970  87.236  12.669  1.00 31.61           C  
-ATOM  29611  N   ILE H 290      20.684  84.877  13.940  1.00 38.60           N  
-ATOM  29612  CA  ILE H 290      21.516  84.435  15.056  1.00 36.77           C  
-ATOM  29613  C   ILE H 290      22.758  83.697  14.556  1.00 41.28           C  
-ATOM  29614  O   ILE H 290      23.856  83.866  15.095  1.00 35.21           O  
-ATOM  29615  CB  ILE H 290      20.704  83.528  16.028  1.00 45.91           C  
-ATOM  29616  CG1 ILE H 290      19.648  84.360  16.760  1.00 45.88           C  
-ATOM  29617  CG2 ILE H 290      21.606  82.832  17.029  1.00 35.37           C  
-ATOM  29618  CD1 ILE H 290      18.726  83.542  17.657  1.00 49.90           C  
-ATOM  29619  N   ALA H 291      22.568  82.908  13.502  1.00 42.73           N  
-ATOM  29620  CA  ALA H 291      23.575  81.980  12.980  1.00 43.10           C  
-ATOM  29621  C   ALA H 291      25.013  82.517  12.836  1.00 39.37           C  
-ATOM  29622  O   ALA H 291      25.945  81.892  13.349  1.00 35.66           O  
-ATOM  29623  CB  ALA H 291      23.099  81.432  11.635  1.00 45.15           C  
-ATOM  29624  N   PRO H 292      25.207  83.663  12.151  1.00 34.09           N  
-ATOM  29625  CA  PRO H 292      26.599  84.055  11.890  1.00 33.29           C  
-ATOM  29626  C   PRO H 292      27.377  84.454  13.140  1.00 35.76           C  
-ATOM  29627  O   PRO H 292      28.595  84.611  13.065  1.00 39.25           O  
-ATOM  29628  CB  PRO H 292      26.453  85.254  10.951  1.00 32.70           C  
-ATOM  29629  CG  PRO H 292      25.141  85.834  11.299  1.00 31.19           C  
-ATOM  29630  CD  PRO H 292      24.260  84.659  11.614  1.00 34.31           C  
-ATOM  29631  N   VAL H 293      26.685  84.618  14.264  1.00 38.81           N  
-ATOM  29632  CA  VAL H 293      27.339  84.962  15.521  1.00 34.22           C  
-ATOM  29633  C   VAL H 293      27.730  83.689  16.263  1.00 37.58           C  
-ATOM  29634  O   VAL H 293      28.854  83.558  16.765  1.00 32.29           O  
-ATOM  29635  CB  VAL H 293      26.431  85.829  16.409  1.00 30.50           C  
-ATOM  29636  CG1 VAL H 293      27.203  86.337  17.610  1.00 33.88           C  
-ATOM  29637  CG2 VAL H 293      25.864  86.990  15.610  1.00 23.83           C  
-ATOM  29638  N   LEU H 294      26.785  82.754  16.321  1.00 41.11           N  
-ATOM  29639  CA  LEU H 294      27.046  81.410  16.810  1.00 34.64           C  
-ATOM  29640  C   LEU H 294      28.235  80.800  16.088  1.00 40.03           C  
-ATOM  29641  O   LEU H 294      29.040  80.093  16.691  1.00 48.82           O  
-ATOM  29642  CB  LEU H 294      25.818  80.521  16.624  1.00 31.84           C  
-ATOM  29643  CG  LEU H 294      24.632  80.776  17.551  1.00 33.87           C  
-ATOM  29644  CD1 LEU H 294      23.536  79.761  17.284  1.00 42.54           C  
-ATOM  29645  CD2 LEU H 294      25.080  80.714  18.996  1.00 34.15           C  
-ATOM  29646  N   ALA H 295      28.334  81.082  14.792  1.00 36.22           N  
-ATOM  29647  CA  ALA H 295      29.433  80.585  13.972  1.00 44.64           C  
-ATOM  29648  C   ALA H 295      30.792  80.955  14.566  1.00 47.97           C  
-ATOM  29649  O   ALA H 295      31.559  80.075  14.966  1.00 45.45           O  
-ATOM  29650  CB  ALA H 295      29.315  81.116  12.549  1.00 39.90           C  
-ATOM  29651  N   TRP H 296      31.079  82.253  14.639  1.00 48.99           N  
-ATOM  29652  CA  TRP H 296      32.385  82.711  15.103  1.00 43.48           C  
-ATOM  29653  C   TRP H 296      32.574  82.447  16.589  1.00 38.03           C  
-ATOM  29654  O   TRP H 296      33.702  82.282  17.050  1.00 43.75           O  
-ATOM  29655  CB  TRP H 296      32.595  84.203  14.802  1.00 39.43           C  
-ATOM  29656  CG  TRP H 296      31.851  85.176  15.684  1.00 33.10           C  
-ATOM  29657  CD1 TRP H 296      30.688  85.823  15.388  1.00 36.67           C  
-ATOM  29658  CD2 TRP H 296      32.242  85.636  16.987  1.00 35.14           C  
-ATOM  29659  NE1 TRP H 296      30.320  86.643  16.428  1.00 29.27           N  
-ATOM  29660  CE2 TRP H 296      31.258  86.545  17.423  1.00 30.89           C  
-ATOM  29661  CE3 TRP H 296      33.324  85.358  17.831  1.00 32.06           C  
-ATOM  29662  CZ2 TRP H 296      31.321  87.177  18.661  1.00 28.34           C  
-ATOM  29663  CZ3 TRP H 296      33.384  85.983  19.061  1.00 25.15           C  
-ATOM  29664  CH2 TRP H 296      32.388  86.883  19.464  1.00 32.53           C  
-ATOM  29665  N   MET H 297      31.480  82.406  17.342  1.00 35.82           N  
-ATOM  29666  CA  MET H 297      31.586  82.085  18.761  1.00 38.52           C  
-ATOM  29667  C   MET H 297      31.954  80.619  18.969  1.00 47.24           C  
-ATOM  29668  O   MET H 297      32.548  80.260  19.985  1.00 49.99           O  
-ATOM  29669  CB  MET H 297      30.285  82.416  19.486  1.00 35.11           C  
-ATOM  29670  CG  MET H 297      30.131  83.890  19.803  1.00 25.32           C  
-ATOM  29671  SD  MET H 297      28.565  84.275  20.594  1.00 36.45           S  
-ATOM  29672  CE  MET H 297      28.791  86.022  20.916  1.00 38.26           C  
-ATOM  29673  N   ASP H 298      31.611  79.774  18.001  1.00 61.10           N  
-ATOM  29674  CA  ASP H 298      31.929  78.354  18.097  1.00 64.33           C  
-ATOM  29675  C   ASP H 298      33.321  78.048  17.549  1.00 62.10           C  
-ATOM  29676  O   ASP H 298      34.055  77.255  18.137  1.00 62.69           O  
-ATOM  29677  CB  ASP H 298      30.888  77.510  17.359  1.00 55.08           C  
-ATOM  29678  CG  ASP H 298      30.909  76.057  17.793  1.00 67.16           C  
-ATOM  29679  OD1 ASP H 298      30.775  75.801  19.010  1.00 59.74           O  
-ATOM  29680  OD2 ASP H 298      31.070  75.172  16.925  1.00 84.90           O  
-ATOM  29681  N   GLU H 299      33.659  78.687  16.428  1.00 59.13           N  
-ATOM  29682  CA  GLU H 299      34.906  78.459  15.685  1.00 60.08           C  
-ATOM  29683  C   GLU H 299      36.114  78.086  16.537  1.00 66.88           C  
-ATOM  29684  O   GLU H 299      36.683  77.005  16.386  1.00 68.16           O  
-ATOM  29685  CB  GLU H 299      35.250  79.702  14.863  1.00 56.24           C  
-ATOM  29686  CG  GLU H 299      34.406  79.875  13.614  1.00 69.87           C  
-ATOM  29687  CD  GLU H 299      34.737  81.151  12.869  1.00 69.91           C  
-ATOM  29688  OE1 GLU H 299      35.705  81.836  13.267  1.00 51.00           O  
-ATOM  29689  OE2 GLU H 299      34.030  81.470  11.889  1.00 62.51           O  
-ATOM  29690  N   GLU H 300      36.506  78.991  17.424  1.00 74.93           N  
-ATOM  29691  CA  GLU H 300      37.599  78.727  18.350  1.00 86.98           C  
-ATOM  29692  C   GLU H 300      37.044  78.502  19.753  1.00 85.19           C  
-ATOM  29693  O   GLU H 300      36.462  79.412  20.346  1.00 80.61           O  
-ATOM  29694  CB  GLU H 300      38.604  79.882  18.342  1.00 92.51           C  
-ATOM  29695  CG  GLU H 300      39.500  79.951  19.568  1.00 98.05           C  
-ATOM  29696  CD  GLU H 300      39.218  81.175  20.423  1.00 94.79           C  
-ATOM  29697  OE1 GLU H 300      39.316  81.072  21.665  1.00 71.17           O  
-ATOM  29698  OE2 GLU H 300      38.902  82.240  19.850  1.00 95.18           O  
-ATOM  29699  N   ASP H 301      37.213  77.291  20.280  1.00 75.55           N  
-ATOM  29700  CA  ASP H 301      37.933  76.226  19.588  1.00 69.85           C  
-ATOM  29701  C   ASP H 301      36.969  75.259  18.903  1.00 60.65           C  
-ATOM  29702  O   ASP H 301      35.841  75.063  19.357  1.00 42.57           O  
-ATOM  29703  CB  ASP H 301      38.830  75.471  20.575  1.00 83.51           C  
-ATOM  29704  CG  ASP H 301      40.061  74.873  19.916  1.00 85.84           C  
-ATOM  29705  OD1 ASP H 301      41.033  75.622  19.677  1.00 69.08           O  
-ATOM  29706  OD2 ASP H 301      40.063  73.651  19.649  1.00 81.77           O  
-ATOM  29707  N   LYS H 308      41.503  65.202  19.906  1.00 58.37           N  
-ATOM  29708  CA  LYS H 308      41.486  65.269  18.449  1.00 72.44           C  
-ATOM  29709  C   LYS H 308      40.337  64.442  17.884  1.00 60.97           C  
-ATOM  29710  O   LYS H 308      39.529  64.938  17.099  1.00 50.13           O  
-ATOM  29711  CB  LYS H 308      42.824  64.792  17.877  1.00 68.73           C  
-ATOM  29712  CG  LYS H 308      43.363  65.661  16.751  1.00 62.97           C  
-ATOM  29713  CD  LYS H 308      43.639  67.080  17.231  1.00 64.68           C  
-ATOM  29714  CE  LYS H 308      42.654  68.079  16.637  1.00 61.73           C  
-ATOM  29715  NZ  LYS H 308      42.857  69.444  17.193  1.00 60.98           N  
-ATOM  29716  N   GLU H 309      40.278  63.176  18.284  1.00 50.44           N  
-ATOM  29717  CA  GLU H 309      39.141  62.322  17.963  1.00 58.39           C  
-ATOM  29718  C   GLU H 309      38.383  61.955  19.235  1.00 59.87           C  
-ATOM  29719  O   GLU H 309      38.899  61.245  20.100  1.00 52.45           O  
-ATOM  29720  CB  GLU H 309      39.588  61.060  17.223  1.00 65.07           C  
-ATOM  29721  CG  GLU H 309      39.373  61.123  15.718  1.00 75.64           C  
-ATOM  29722  CD  GLU H 309      39.771  59.837  15.018  1.00 85.28           C  
-ATOM  29723  OE1 GLU H 309      40.860  59.806  14.406  1.00 72.71           O  
-ATOM  29724  OE2 GLU H 309      38.994  58.859  15.076  1.00 83.93           O  
-ATOM  29725  N   LEU H 310      37.157  62.456  19.337  1.00 59.24           N  
-ATOM  29726  CA  LEU H 310      36.332  62.269  20.521  1.00 50.64           C  
-ATOM  29727  C   LEU H 310      35.958  60.809  20.720  1.00 42.20           C  
-ATOM  29728  O   LEU H 310      35.447  60.166  19.805  1.00 49.36           O  
-ATOM  29729  CB  LEU H 310      35.059  63.112  20.419  1.00 53.77           C  
-ATOM  29730  CG  LEU H 310      35.232  64.580  20.031  1.00 43.49           C  
-ATOM  29731  CD1 LEU H 310      34.142  64.999  19.056  1.00 48.67           C  
-ATOM  29732  CD2 LEU H 310      35.225  65.469  21.266  1.00 29.38           C  
-ATOM  29733  N   ILE H 311      36.217  60.287  21.915  1.00 46.66           N  
-ATOM  29734  CA  ILE H 311      35.719  58.966  22.276  1.00 50.55           C  
-ATOM  29735  C   ILE H 311      34.317  59.134  22.851  1.00 42.60           C  
-ATOM  29736  O   ILE H 311      33.985  60.186  23.401  1.00 34.21           O  
-ATOM  29737  CB  ILE H 311      36.637  58.238  23.292  1.00 41.19           C  
-ATOM  29738  CG1 ILE H 311      36.390  58.726  24.718  1.00 37.24           C  
-ATOM  29739  CG2 ILE H 311      38.098  58.409  22.920  1.00 46.61           C  
-ATOM  29740  CD1 ILE H 311      35.793  57.669  25.620  1.00 41.08           C  
-ATOM  29741  N   ARG H 312      33.490  58.106  22.713  1.00 35.95           N  
-ATOM  29742  CA  ARG H 312      32.110  58.193  23.167  1.00 36.77           C  
-ATOM  29743  C   ARG H 312      31.546  56.817  23.486  1.00 40.42           C  
-ATOM  29744  O   ARG H 312      31.750  55.863  22.737  1.00 52.03           O  
-ATOM  29745  CB  ARG H 312      31.250  58.892  22.112  1.00 46.84           C  
-ATOM  29746  CG  ARG H 312      29.777  59.000  22.467  1.00 51.39           C  
-ATOM  29747  CD  ARG H 312      29.082  60.032  21.594  1.00 51.23           C  
-ATOM  29748  NE  ARG H 312      27.628  59.994  21.730  1.00 53.09           N  
-ATOM  29749  CZ  ARG H 312      26.945  60.621  22.684  1.00 58.66           C  
-ATOM  29750  NH1 ARG H 312      25.622  60.530  22.721  1.00 47.82           N  
-ATOM  29751  NH2 ARG H 312      27.581  61.336  23.604  1.00 59.60           N  
-ATOM  29752  N   ALA H 313      30.841  56.720  24.609  1.00 36.55           N  
-ATOM  29753  CA  ALA H 313      30.240  55.461  25.028  1.00 37.58           C  
-ATOM  29754  C   ALA H 313      29.167  55.016  24.044  1.00 41.48           C  
-ATOM  29755  O   ALA H 313      28.237  55.771  23.762  1.00 40.86           O  
-ATOM  29756  CB  ALA H 313      29.655  55.592  26.419  1.00 33.16           C  
-ATOM  29757  N   VAL H 314      29.309  53.780  23.558  1.00 42.73           N  
-ATOM  29758  CA  VAL H 314      28.430  53.153  22.559  1.00 37.79           C  
-ATOM  29759  C   VAL H 314      27.629  54.139  21.703  1.00 39.81           C  
-ATOM  29760  O   VAL H 314      26.425  54.307  21.895  1.00 42.18           O  
-ATOM  29761  CB  VAL H 314      27.451  52.153  23.231  1.00 35.78           C  
-ATOM  29762  CG1 VAL H 314      28.158  50.839  23.508  1.00 32.38           C  
-ATOM  29763  CG2 VAL H 314      26.856  52.723  24.519  1.00 30.45           C  
-ATOM  29764  N   PRO H 315      28.306  54.787  20.742  1.00 39.68           N  
-ATOM  29765  CA  PRO H 315      27.744  55.870  19.922  1.00 46.39           C  
-ATOM  29766  C   PRO H 315      26.515  55.469  19.105  1.00 40.09           C  
-ATOM  29767  O   PRO H 315      25.725  56.337  18.731  1.00 39.80           O  
-ATOM  29768  CB  PRO H 315      28.906  56.241  18.993  1.00 47.25           C  
-ATOM  29769  CG  PRO H 315      29.758  55.024  18.949  1.00 46.64           C  
-ATOM  29770  CD  PRO H 315      29.673  54.438  20.322  1.00 40.84           C  
-ATOM  29771  N   HIS H 316      26.357  54.179  18.833  1.00 41.22           N  
-ATOM  29772  CA  HIS H 316      25.229  53.706  18.038  1.00 45.65           C  
-ATOM  29773  C   HIS H 316      23.908  53.800  18.800  1.00 42.07           C  
-ATOM  29774  O   HIS H 316      22.837  53.709  18.209  1.00 46.91           O  
-ATOM  29775  CB  HIS H 316      25.467  52.268  17.574  1.00 44.38           C  
-ATOM  29776  CG  HIS H 316      25.934  51.351  18.661  1.00 51.88           C  
-ATOM  29777  ND1 HIS H 316      27.268  51.100  18.900  1.00 51.12           N  
-ATOM  29778  CD2 HIS H 316      25.245  50.622  19.571  1.00 53.05           C  
-ATOM  29779  CE1 HIS H 316      27.381  50.257  19.911  1.00 57.23           C  
-ATOM  29780  NE2 HIS H 316      26.168  49.951  20.336  1.00 53.66           N  
-ATOM  29781  N   VAL H 317      23.985  53.985  20.112  1.00 38.27           N  
-ATOM  29782  CA  VAL H 317      22.783  54.168  20.915  1.00 41.67           C  
-ATOM  29783  C   VAL H 317      22.405  55.643  20.962  1.00 46.10           C  
-ATOM  29784  O   VAL H 317      22.982  56.416  21.726  1.00 46.63           O  
-ATOM  29785  CB  VAL H 317      22.964  53.639  22.351  1.00 45.08           C  
-ATOM  29786  CG1 VAL H 317      21.709  53.894  23.180  1.00 38.87           C  
-ATOM  29787  CG2 VAL H 317      23.302  52.156  22.333  1.00 29.58           C  
-ATOM  29788  N   HIS H 318      21.435  56.029  20.139  1.00 53.69           N  
-ATOM  29789  CA  HIS H 318      21.007  57.424  20.072  1.00 60.04           C  
-ATOM  29790  C   HIS H 318      20.122  57.817  21.249  1.00 51.27           C  
-ATOM  29791  O   HIS H 318      20.277  58.901  21.809  1.00 48.18           O  
-ATOM  29792  CB  HIS H 318      20.285  57.702  18.752  1.00 59.65           C  
-ATOM  29793  CG  HIS H 318      21.170  58.292  17.698  1.00 76.09           C  
-ATOM  29794  ND1 HIS H 318      21.627  59.591  17.755  1.00 76.52           N  
-ATOM  29795  CD2 HIS H 318      21.675  57.765  16.558  1.00 69.12           C  
-ATOM  29796  CE1 HIS H 318      22.378  59.838  16.697  1.00 70.95           C  
-ATOM  29797  NE2 HIS H 318      22.423  58.746  15.954  1.00 71.03           N  
-ATOM  29798  N   PHE H 319      19.191  56.946  21.626  1.00 53.05           N  
-ATOM  29799  CA  PHE H 319      18.297  57.265  22.739  1.00 51.43           C  
-ATOM  29800  C   PHE H 319      18.791  56.633  24.039  1.00 43.53           C  
-ATOM  29801  O   PHE H 319      18.580  55.447  24.292  1.00 44.01           O  
-ATOM  29802  CB  PHE H 319      16.866  56.824  22.425  1.00 51.09           C  
-ATOM  29803  CG  PHE H 319      16.370  57.303  21.088  1.00 68.90           C  
-ATOM  29804  CD1 PHE H 319      16.113  58.647  20.872  1.00 75.31           C  
-ATOM  29805  CD2 PHE H 319      16.167  56.410  20.046  1.00 66.14           C  
-ATOM  29806  CE1 PHE H 319      15.662  59.093  19.642  1.00 71.83           C  
-ATOM  29807  CE2 PHE H 319      15.716  56.851  18.815  1.00 69.59           C  
-ATOM  29808  CZ  PHE H 319      15.463  58.194  18.614  1.00 76.21           C  
-ATOM  29809  N   ARG H 320      19.440  57.452  24.860  1.00 30.38           N  
-ATOM  29810  CA  ARG H 320      20.180  56.976  26.022  1.00 28.33           C  
-ATOM  29811  C   ARG H 320      19.475  57.290  27.338  1.00 24.60           C  
-ATOM  29812  O   ARG H 320      19.844  58.233  28.038  1.00 23.82           O  
-ATOM  29813  CB  ARG H 320      21.578  57.593  26.022  1.00 33.25           C  
-ATOM  29814  CG  ARG H 320      22.381  57.274  24.770  1.00 33.21           C  
-ATOM  29815  CD  ARG H 320      23.432  58.333  24.489  1.00 31.77           C  
-ATOM  29816  NE  ARG H 320      24.740  57.738  24.230  1.00 35.45           N  
-ATOM  29817  CZ  ARG H 320      25.794  57.884  25.025  1.00 33.57           C  
-ATOM  29818  NH1 ARG H 320      26.946  57.307  24.717  1.00 30.33           N  
-ATOM  29819  NH2 ARG H 320      25.697  58.614  26.127  1.00 30.84           N  
-ATOM  29820  N   GLY H 321      18.474  56.485  27.680  1.00 24.18           N  
-ATOM  29821  CA  GLY H 321      17.685  56.710  28.878  1.00 19.54           C  
-ATOM  29822  C   GLY H 321      18.293  56.119  30.137  1.00 20.27           C  
-ATOM  29823  O   GLY H 321      17.981  56.560  31.242  1.00 26.09           O  
-ATOM  29824  N   HIS H 322      19.156  55.121  29.970  1.00 20.39           N  
-ATOM  29825  CA  HIS H 322      19.800  54.458  31.101  1.00 21.39           C  
-ATOM  29826  C   HIS H 322      20.632  55.452  31.899  1.00 22.08           C  
-ATOM  29827  O   HIS H 322      21.335  56.283  31.324  1.00 24.36           O  
-ATOM  29828  CB  HIS H 322      20.679  53.302  30.619  1.00 27.26           C  
-ATOM  29829  CG  HIS H 322      20.901  52.237  31.649  1.00 30.55           C  
-ATOM  29830  ND1 HIS H 322      21.507  52.487  32.862  1.00 21.83           N  
-ATOM  29831  CD2 HIS H 322      20.604  50.916  31.641  1.00 26.46           C  
-ATOM  29832  CE1 HIS H 322      21.569  51.366  33.558  1.00 18.50           C  
-ATOM  29833  NE2 HIS H 322      21.029  50.398  32.841  1.00 20.21           N  
-ATOM  29834  N   GLU H 323      20.555  55.363  33.223  1.00 24.36           N  
-ATOM  29835  CA  GLU H 323      21.211  56.337  34.088  1.00 21.91           C  
-ATOM  29836  C   GLU H 323      22.713  56.083  34.224  1.00 25.16           C  
-ATOM  29837  O   GLU H 323      23.434  56.917  34.769  1.00 29.08           O  
-ATOM  29838  CB  GLU H 323      20.549  56.347  35.471  1.00 26.97           C  
-ATOM  29839  CG  GLU H 323      19.102  56.836  35.459  1.00 24.30           C  
-ATOM  29840  CD  GLU H 323      18.467  56.868  36.842  1.00 28.47           C  
-ATOM  29841  OE1 GLU H 323      17.244  57.103  36.927  1.00 30.04           O  
-ATOM  29842  OE2 GLU H 323      19.186  56.660  37.842  1.00 24.71           O  
-ATOM  29843  N   GLU H 324      23.182  54.942  33.722  1.00 21.41           N  
-ATOM  29844  CA  GLU H 324      24.608  54.609  33.753  1.00 19.52           C  
-ATOM  29845  C   GLU H 324      25.377  55.405  32.694  1.00 27.50           C  
-ATOM  29846  O   GLU H 324      26.605  55.576  32.771  1.00 32.67           O  
-ATOM  29847  CB  GLU H 324      24.807  53.104  33.553  1.00 21.17           C  
-ATOM  29848  CG  GLU H 324      26.254  52.643  33.649  1.00 19.99           C  
-ATOM  29849  CD  GLU H 324      26.380  51.183  34.031  1.00 24.94           C  
-ATOM  29850  OE1 GLU H 324      27.521  50.690  34.158  1.00 20.73           O  
-ATOM  29851  OE2 GLU H 324      25.333  50.528  34.214  1.00 30.54           O  
-ATOM  29852  N   PHE H 325      24.635  55.907  31.713  1.00 22.24           N  
-ATOM  29853  CA  PHE H 325      25.202  56.777  30.695  1.00 19.99           C  
-ATOM  29854  C   PHE H 325      25.738  58.061  31.313  1.00 23.57           C  
-ATOM  29855  O   PHE H 325      26.537  58.758  30.700  1.00 32.89           O  
-ATOM  29856  CB  PHE H 325      24.165  57.100  29.619  1.00 25.41           C  
-ATOM  29857  CG  PHE H 325      23.952  55.994  28.631  1.00 22.06           C  
-ATOM  29858  CD1 PHE H 325      24.992  55.562  27.826  1.00 21.19           C  
-ATOM  29859  CD2 PHE H 325      22.713  55.394  28.497  1.00 23.55           C  
-ATOM  29860  CE1 PHE H 325      24.802  54.546  26.908  1.00 27.24           C  
-ATOM  29861  CE2 PHE H 325      22.514  54.379  27.581  1.00 29.69           C  
-ATOM  29862  CZ  PHE H 325      23.560  53.954  26.785  1.00 34.40           C  
-ATOM  29863  N   GLN H 326      25.288  58.377  32.523  1.00 19.88           N  
-ATOM  29864  CA  GLN H 326      25.875  59.476  33.274  1.00 22.70           C  
-ATOM  29865  C   GLN H 326      27.340  59.168  33.546  1.00 23.47           C  
-ATOM  29866  O   GLN H 326      28.225  59.985  33.279  1.00 26.90           O  
-ATOM  29867  CB  GLN H 326      25.129  59.707  34.589  1.00 22.08           C  
-ATOM  29868  CG  GLN H 326      23.669  60.080  34.423  1.00 19.25           C  
-ATOM  29869  CD  GLN H 326      23.051  60.557  35.720  1.00 21.17           C  
-ATOM  29870  OE1 GLN H 326      23.345  61.656  36.194  1.00 16.88           O  
-ATOM  29871  NE2 GLN H 326      22.195  59.728  36.308  1.00 26.26           N  
-ATOM  29872  N   TYR H 327      27.581  57.971  34.071  1.00 22.37           N  
-ATOM  29873  CA  TYR H 327      28.928  57.514  34.384  1.00 19.68           C  
-ATOM  29874  C   TYR H 327      29.776  57.378  33.127  1.00 21.09           C  
-ATOM  29875  O   TYR H 327      30.901  57.882  33.068  1.00 23.32           O  
-ATOM  29876  CB  TYR H 327      28.873  56.179  35.130  1.00 13.92           C  
-ATOM  29877  CG  TYR H 327      30.226  55.592  35.452  1.00 13.98           C  
-ATOM  29878  CD1 TYR H 327      31.007  56.118  36.473  1.00 18.88           C  
-ATOM  29879  CD2 TYR H 327      30.719  54.508  34.740  1.00 14.38           C  
-ATOM  29880  CE1 TYR H 327      32.244  55.583  36.773  1.00 17.30           C  
-ATOM  29881  CE2 TYR H 327      31.955  53.967  35.033  1.00 18.08           C  
-ATOM  29882  CZ  TYR H 327      32.712  54.508  36.051  1.00 18.33           C  
-ATOM  29883  OH  TYR H 327      33.942  53.969  36.346  1.00 24.11           O  
-ATOM  29884  N   LEU H 328      29.233  56.699  32.122  1.00 18.82           N  
-ATOM  29885  CA  LEU H 328      29.960  56.497  30.873  1.00 21.55           C  
-ATOM  29886  C   LEU H 328      30.341  57.824  30.210  1.00 28.83           C  
-ATOM  29887  O   LEU H 328      31.499  58.026  29.816  1.00 33.91           O  
-ATOM  29888  CB  LEU H 328      29.130  55.644  29.918  1.00 19.14           C  
-ATOM  29889  CG  LEU H 328      28.793  54.247  30.442  1.00 17.62           C  
-ATOM  29890  CD1 LEU H 328      27.989  53.459  29.420  1.00 20.34           C  
-ATOM  29891  CD2 LEU H 328      30.060  53.499  30.827  1.00 17.22           C  
-ATOM  29892  N   ASP H 329      29.372  58.729  30.101  1.00 24.55           N  
-ATOM  29893  CA  ASP H 329      29.625  60.045  29.524  1.00 21.96           C  
-ATOM  29894  C   ASP H 329      30.536  60.887  30.404  1.00 23.14           C  
-ATOM  29895  O   ASP H 329      31.165  61.822  29.923  1.00 31.93           O  
-ATOM  29896  CB  ASP H 329      28.318  60.796  29.278  1.00 29.94           C  
-ATOM  29897  CG  ASP H 329      27.481  60.165  28.189  1.00 40.02           C  
-ATOM  29898  OD1 ASP H 329      28.050  59.434  27.348  1.00 38.22           O  
-ATOM  29899  OD2 ASP H 329      26.254  60.403  28.175  1.00 30.66           O  
-ATOM  29900  N   LEU H 330      30.595  60.574  31.694  1.00 19.16           N  
-ATOM  29901  CA  LEU H 330      31.545  61.246  32.569  1.00 17.32           C  
-ATOM  29902  C   LEU H 330      32.952  60.795  32.215  1.00 20.23           C  
-ATOM  29903  O   LEU H 330      33.859  61.615  32.086  1.00 24.79           O  
-ATOM  29904  CB  LEU H 330      31.242  60.964  34.043  1.00 22.17           C  
-ATOM  29905  CG  LEU H 330      32.258  61.544  35.033  1.00 20.54           C  
-ATOM  29906  CD1 LEU H 330      32.434  63.042  34.825  1.00 13.21           C  
-ATOM  29907  CD2 LEU H 330      31.841  61.243  36.465  1.00 19.79           C  
-ATOM  29908  N   ILE H 331      33.122  59.486  32.052  1.00 22.04           N  
-ATOM  29909  CA  ILE H 331      34.402  58.928  31.620  1.00 25.99           C  
-ATOM  29910  C   ILE H 331      34.846  59.579  30.316  1.00 26.50           C  
-ATOM  29911  O   ILE H 331      35.959  60.113  30.214  1.00 19.86           O  
-ATOM  29912  CB  ILE H 331      34.330  57.398  31.409  1.00 23.68           C  
-ATOM  29913  CG1 ILE H 331      33.819  56.698  32.670  1.00 22.57           C  
-ATOM  29914  CG2 ILE H 331      35.687  56.860  30.967  1.00 22.00           C  
-ATOM  29915  CD1 ILE H 331      34.829  55.790  33.337  1.00 23.93           C  
-ATOM  29916  N   ALA H 332      33.955  59.541  29.327  1.00 26.45           N  
-ATOM  29917  CA  ALA H 332      34.236  60.120  28.019  1.00 23.61           C  
-ATOM  29918  C   ALA H 332      34.602  61.598  28.120  1.00 28.37           C  
-ATOM  29919  O   ALA H 332      35.604  62.032  27.554  1.00 34.77           O  
-ATOM  29920  CB  ALA H 332      33.045  59.934  27.095  1.00 27.90           C  
-ATOM  29921  N   ASP H 333      33.791  62.360  28.848  1.00 24.71           N  
-ATOM  29922  CA  ASP H 333      34.001  63.797  28.988  1.00 26.77           C  
-ATOM  29923  C   ASP H 333      35.340  64.103  29.644  1.00 34.45           C  
-ATOM  29924  O   ASP H 333      35.998  65.079  29.299  1.00 37.15           O  
-ATOM  29925  CB  ASP H 333      32.868  64.437  29.796  1.00 24.05           C  
-ATOM  29926  CG  ASP H 333      32.970  65.950  29.844  1.00 47.65           C  
-ATOM  29927  OD1 ASP H 333      33.291  66.560  28.799  1.00 44.94           O  
-ATOM  29928  OD2 ASP H 333      32.733  66.528  30.926  1.00 53.27           O  
-ATOM  29929  N   ILE H 334      35.743  63.265  30.592  1.00 28.26           N  
-ATOM  29930  CA  ILE H 334      37.017  63.461  31.268  1.00 21.52           C  
-ATOM  29931  C   ILE H 334      38.178  63.144  30.333  1.00 26.68           C  
-ATOM  29932  O   ILE H 334      39.149  63.897  30.265  1.00 28.12           O  
-ATOM  29933  CB  ILE H 334      37.121  62.596  32.535  1.00 22.30           C  
-ATOM  29934  CG1 ILE H 334      36.177  63.133  33.606  1.00 20.61           C  
-ATOM  29935  CG2 ILE H 334      38.541  62.584  33.065  1.00 19.21           C  
-ATOM  29936  CD1 ILE H 334      36.146  62.291  34.842  1.00 21.13           C  
-ATOM  29937  N   ILE H 335      38.076  62.035  29.607  1.00 32.26           N  
-ATOM  29938  CA  ILE H 335      39.151  61.637  28.701  1.00 31.51           C  
-ATOM  29939  C   ILE H 335      39.324  62.645  27.559  1.00 37.88           C  
-ATOM  29940  O   ILE H 335      40.446  62.938  27.144  1.00 44.43           O  
-ATOM  29941  CB  ILE H 335      38.904  60.224  28.127  1.00 28.51           C  
-ATOM  29942  CG1 ILE H 335      39.104  59.173  29.222  1.00 21.58           C  
-ATOM  29943  CG2 ILE H 335      39.834  59.938  26.960  1.00 24.02           C  
-ATOM  29944  CD1 ILE H 335      38.946  57.748  28.739  1.00 22.53           C  
-ATOM  29945  N   ASN H 336      38.215  63.198  27.076  1.00 34.63           N  
-ATOM  29946  CA  ASN H 336      38.253  64.136  25.956  1.00 30.55           C  
-ATOM  29947  C   ASN H 336      38.567  65.582  26.349  1.00 31.58           C  
-ATOM  29948  O   ASN H 336      39.277  66.282  25.628  1.00 32.59           O  
-ATOM  29949  CB  ASN H 336      36.923  64.103  25.201  1.00 24.10           C  
-ATOM  29950  CG  ASN H 336      36.686  62.783  24.494  1.00 34.18           C  
-ATOM  29951  OD1 ASN H 336      37.626  62.127  24.046  1.00 40.42           O  
-ATOM  29952  ND2 ASN H 336      35.425  62.386  24.388  1.00 29.50           N  
-ATOM  29953  N   ASN H 337      38.045  66.025  27.489  1.00 32.38           N  
-ATOM  29954  CA  ASN H 337      38.105  67.440  27.856  1.00 32.66           C  
-ATOM  29955  C   ASN H 337      38.833  67.736  29.167  1.00 30.16           C  
-ATOM  29956  O   ASN H 337      38.811  68.868  29.653  1.00 26.21           O  
-ATOM  29957  CB  ASN H 337      36.687  68.005  27.935  1.00 26.97           C  
-ATOM  29958  CG  ASN H 337      35.872  67.697  26.699  1.00 32.58           C  
-ATOM  29959  OD1 ASN H 337      36.390  67.698  25.583  1.00 29.49           O  
-ATOM  29960  ND2 ASN H 337      34.589  67.420  26.892  1.00 38.85           N  
-ATOM  29961  N   GLY H 338      39.479  66.726  29.737  1.00 30.29           N  
-ATOM  29962  CA  GLY H 338      40.192  66.910  30.988  1.00 26.93           C  
-ATOM  29963  C   GLY H 338      41.596  67.430  30.767  1.00 30.10           C  
-ATOM  29964  O   GLY H 338      42.058  67.514  29.630  1.00 43.47           O  
-ATOM  29965  N   ARG H 339      42.274  67.789  31.854  1.00 37.88           N  
-ATOM  29966  CA  ARG H 339      43.670  68.216  31.782  1.00 39.21           C  
-ATOM  29967  C   ARG H 339      44.576  67.141  32.372  1.00 36.22           C  
-ATOM  29968  O   ARG H 339      44.257  66.559  33.408  1.00 38.41           O  
-ATOM  29969  CB  ARG H 339      43.874  69.544  32.519  1.00 38.35           C  
-ATOM  29970  CG  ARG H 339      43.176  70.739  31.889  1.00 30.92           C  
-ATOM  29971  CD  ARG H 339      43.776  71.079  30.535  1.00 39.23           C  
-ATOM  29972  NE  ARG H 339      42.851  70.805  29.440  1.00 64.94           N  
-ATOM  29973  CZ  ARG H 339      43.226  70.453  28.214  1.00 81.43           C  
-ATOM  29974  NH1 ARG H 339      44.514  70.320  27.922  1.00 72.14           N  
-ATOM  29975  NH2 ARG H 339      42.311  70.224  27.280  1.00 79.52           N  
-ATOM  29976  N   THR H 340      45.699  66.874  31.714  1.00 24.15           N  
-ATOM  29977  CA  THR H 340      46.647  65.885  32.215  1.00 28.00           C  
-ATOM  29978  C   THR H 340      47.512  66.482  33.320  1.00 34.41           C  
-ATOM  29979  O   THR H 340      48.297  67.399  33.081  1.00 29.09           O  
-ATOM  29980  CB  THR H 340      47.545  65.344  31.096  1.00 39.76           C  
-ATOM  29981  OG1 THR H 340      46.735  64.687  30.112  1.00 38.07           O  
-ATOM  29982  CG2 THR H 340      48.561  64.358  31.658  1.00 30.82           C  
-ATOM  29983  N   MET H 341      47.363  65.952  34.530  1.00 38.28           N  
-ATOM  29984  CA  MET H 341      48.014  66.506  35.709  1.00 35.22           C  
-ATOM  29985  C   MET H 341      48.832  65.465  36.458  1.00 36.53           C  
-ATOM  29986  O   MET H 341      48.760  64.270  36.163  1.00 38.48           O  
-ATOM  29987  CB  MET H 341      46.970  67.100  36.657  1.00 36.19           C  
-ATOM  29988  CG  MET H 341      45.975  68.032  35.996  1.00 31.90           C  
-ATOM  29989  SD  MET H 341      46.747  69.567  35.467  1.00 45.71           S  
-ATOM  29990  CE  MET H 341      47.483  70.110  37.006  1.00 48.66           C  
-ATOM  29991  N   ASP H 342      49.602  65.933  37.436  1.00 45.32           N  
-ATOM  29992  CA  ASP H 342      50.300  65.051  38.366  1.00 51.93           C  
-ATOM  29993  C   ASP H 342      49.464  64.866  39.628  1.00 52.02           C  
-ATOM  29994  O   ASP H 342      48.368  65.419  39.738  1.00 51.92           O  
-ATOM  29995  CB  ASP H 342      51.677  65.612  38.722  1.00 46.22           C  
-ATOM  29996  CG  ASP H 342      52.597  65.705  37.523  1.00 54.22           C  
-ATOM  29997  OD1 ASP H 342      52.476  64.858  36.612  1.00 55.62           O  
-ATOM  29998  OD2 ASP H 342      53.444  66.623  37.495  1.00 52.17           O  
-ATOM  29999  N   ASP H 343      49.982  64.096  40.580  1.00 56.19           N  
-ATOM  30000  CA  ASP H 343      49.287  63.887  41.845  1.00 54.42           C  
-ATOM  30001  C   ASP H 343      50.193  63.287  42.916  1.00 51.44           C  
-ATOM  30002  O   ASP H 343      51.397  63.123  42.718  1.00 55.49           O  
-ATOM  30003  CB  ASP H 343      48.068  62.983  41.645  1.00 45.45           C  
-ATOM  30004  CG  ASP H 343      48.447  61.573  41.247  1.00 44.62           C  
-ATOM  30005  OD1 ASP H 343      49.350  61.413  40.399  1.00 51.52           O  
-ATOM  30006  OD2 ASP H 343      47.845  60.622  41.789  1.00 46.80           O  
-ATOM  30007  N   ARG H 344      49.586  62.966  44.053  1.00 47.40           N  
-ATOM  30008  CA  ARG H 344      50.281  62.371  45.186  1.00 51.92           C  
-ATOM  30009  C   ARG H 344      50.955  61.048  44.832  1.00 52.88           C  
-ATOM  30010  O   ARG H 344      52.096  60.794  45.223  1.00 55.05           O  
-ATOM  30011  CB  ARG H 344      49.296  62.159  46.341  1.00 53.17           C  
-ATOM  30012  CG  ARG H 344      49.581  60.939  47.209  1.00 59.26           C  
-ATOM  30013  CD  ARG H 344      50.381  61.303  48.450  1.00 73.80           C  
-ATOM  30014  NE  ARG H 344      51.661  61.922  48.120  1.00 86.62           N  
-ATOM  30015  CZ  ARG H 344      52.263  62.839  48.870  1.00 81.24           C  
-ATOM  30016  NH1 ARG H 344      51.702  63.254  50.000  1.00 84.79           N  
-ATOM  30017  NH2 ARG H 344      53.426  63.345  48.486  1.00 66.35           N  
-ATOM  30018  N   THR H 345      50.240  60.213  44.087  1.00 53.46           N  
-ATOM  30019  CA  THR H 345      50.688  58.855  43.803  1.00 52.66           C  
-ATOM  30020  C   THR H 345      51.873  58.814  42.837  1.00 53.80           C  
-ATOM  30021  O   THR H 345      52.710  57.911  42.904  1.00 50.20           O  
-ATOM  30022  CB  THR H 345      49.538  58.012  43.217  1.00 45.57           C  
-ATOM  30023  OG1 THR H 345      49.272  58.427  41.871  1.00 38.37           O  
-ATOM  30024  CG2 THR H 345      48.274  58.185  44.049  1.00 46.80           C  
-ATOM  30025  N   GLY H 346      51.941  59.795  41.942  1.00 55.34           N  
-ATOM  30026  CA  GLY H 346      52.984  59.835  40.932  1.00 50.05           C  
-ATOM  30027  C   GLY H 346      52.559  59.117  39.666  1.00 49.42           C  
-ATOM  30028  O   GLY H 346      53.304  59.065  38.688  1.00 44.01           O  
-ATOM  30029  N   VAL H 347      51.353  58.559  39.690  1.00 47.76           N  
-ATOM  30030  CA  VAL H 347      50.815  57.842  38.542  1.00 36.31           C  
-ATOM  30031  C   VAL H 347      50.443  58.820  37.432  1.00 41.49           C  
-ATOM  30032  O   VAL H 347      50.715  58.572  36.256  1.00 51.07           O  
-ATOM  30033  CB  VAL H 347      49.584  56.999  38.929  1.00 39.81           C  
-ATOM  30034  CG1 VAL H 347      48.944  56.387  37.694  1.00 50.13           C  
-ATOM  30035  CG2 VAL H 347      49.977  55.913  39.922  1.00 44.32           C  
-ATOM  30036  N   GLY H 348      49.835  59.939  37.815  1.00 29.27           N  
-ATOM  30037  CA  GLY H 348      49.413  60.942  36.855  1.00 37.22           C  
-ATOM  30038  C   GLY H 348      47.974  60.725  36.432  1.00 42.78           C  
-ATOM  30039  O   GLY H 348      47.564  59.592  36.168  1.00 45.48           O  
-ATOM  30040  N   VAL H 349      47.200  61.805  36.365  1.00 38.70           N  
-ATOM  30041  CA  VAL H 349      45.774  61.683  36.075  1.00 30.19           C  
-ATOM  30042  C   VAL H 349      45.328  62.561  34.917  1.00 33.23           C  
-ATOM  30043  O   VAL H 349      46.086  63.387  34.419  1.00 39.89           O  
-ATOM  30044  CB  VAL H 349      44.911  62.050  37.303  1.00 29.00           C  
-ATOM  30045  CG1 VAL H 349      45.362  61.281  38.530  1.00 34.97           C  
-ATOM  30046  CG2 VAL H 349      44.968  63.546  37.563  1.00 30.67           C  
-ATOM  30047  N   ILE H 350      44.089  62.356  34.487  1.00 28.23           N  
-ATOM  30048  CA  ILE H 350      43.401  63.286  33.603  1.00 24.08           C  
-ATOM  30049  C   ILE H 350      42.180  63.777  34.366  1.00 28.20           C  
-ATOM  30050  O   ILE H 350      41.263  63.004  34.631  1.00 32.33           O  
-ATOM  30051  CB  ILE H 350      42.981  62.633  32.273  1.00 24.84           C  
-ATOM  30052  CG1 ILE H 350      44.198  62.039  31.561  1.00 29.44           C  
-ATOM  30053  CG2 ILE H 350      42.273  63.642  31.385  1.00 26.13           C  
-ATOM  30054  CD1 ILE H 350      43.864  61.344  30.262  1.00 29.56           C  
-ATOM  30055  N   SER H 351      42.168  65.050  34.743  1.00 29.05           N  
-ATOM  30056  CA  SER H 351      41.172  65.512  35.701  1.00 24.68           C  
-ATOM  30057  C   SER H 351      40.290  66.646  35.196  1.00 23.89           C  
-ATOM  30058  O   SER H 351      40.650  67.377  34.270  1.00 26.64           O  
-ATOM  30059  CB  SER H 351      41.861  65.954  36.992  1.00 24.73           C  
-ATOM  30060  OG  SER H 351      42.634  67.120  36.777  1.00 30.88           O  
-ATOM  30061  N   LYS H 352      39.121  66.755  35.819  1.00 23.13           N  
-ATOM  30062  CA  LYS H 352      38.220  67.890  35.661  1.00 25.33           C  
-ATOM  30063  C   LYS H 352      37.779  68.325  37.052  1.00 28.22           C  
-ATOM  30064  O   LYS H 352      38.054  67.634  38.035  1.00 30.54           O  
-ATOM  30065  CB  LYS H 352      37.007  67.533  34.799  1.00 22.07           C  
-ATOM  30066  CG  LYS H 352      37.343  67.173  33.364  1.00 24.53           C  
-ATOM  30067  CD  LYS H 352      36.095  67.154  32.495  1.00 24.44           C  
-ATOM  30068  CE  LYS H 352      35.439  68.524  32.454  1.00 35.06           C  
-ATOM  30069  NZ  LYS H 352      34.270  68.561  31.529  1.00 41.62           N  
-ATOM  30070  N   PHE H 353      37.095  69.461  37.142  1.00 24.59           N  
-ATOM  30071  CA  PHE H 353      36.658  69.976  38.436  1.00 16.42           C  
-ATOM  30072  C   PHE H 353      35.180  70.357  38.420  1.00 19.66           C  
-ATOM  30073  O   PHE H 353      34.726  71.100  37.547  1.00 24.06           O  
-ATOM  30074  CB  PHE H 353      37.508  71.182  38.841  1.00 14.66           C  
-ATOM  30075  CG  PHE H 353      37.439  71.509  40.304  1.00 17.97           C  
-ATOM  30076  CD1 PHE H 353      37.713  70.540  41.254  1.00 19.33           C  
-ATOM  30077  CD2 PHE H 353      37.118  72.788  40.733  1.00 18.49           C  
-ATOM  30078  CE1 PHE H 353      37.659  70.833  42.603  1.00 19.27           C  
-ATOM  30079  CE2 PHE H 353      37.070  73.089  42.083  1.00 21.74           C  
-ATOM  30080  CZ  PHE H 353      37.337  72.108  43.019  1.00 19.35           C  
-ATOM  30081  N   GLY H 354      34.433  69.845  39.392  1.00 14.19           N  
-ATOM  30082  CA  GLY H 354      33.014  70.132  39.493  1.00 15.34           C  
-ATOM  30083  C   GLY H 354      32.180  69.285  38.554  1.00 17.61           C  
-ATOM  30084  O   GLY H 354      31.878  69.693  37.433  1.00 23.33           O  
-ATOM  30085  N   CYS H 355      31.807  68.097  39.016  1.00 16.08           N  
-ATOM  30086  CA  CYS H 355      31.013  67.181  38.211  1.00 16.79           C  
-ATOM  30087  C   CYS H 355      29.809  66.684  38.996  1.00 22.71           C  
-ATOM  30088  O   CYS H 355      29.827  66.651  40.227  1.00 24.81           O  
-ATOM  30089  CB  CYS H 355      31.871  66.012  37.733  1.00 14.86           C  
-ATOM  30090  SG  CYS H 355      33.166  66.511  36.572  1.00 21.69           S  
-ATOM  30091  N   THR H 356      28.763  66.297  38.276  1.00 23.01           N  
-ATOM  30092  CA  THR H 356      27.478  66.001  38.893  1.00 15.75           C  
-ATOM  30093  C   THR H 356      26.820  64.761  38.307  1.00 18.12           C  
-ATOM  30094  O   THR H 356      26.744  64.603  37.089  1.00 20.77           O  
-ATOM  30095  CB  THR H 356      26.517  67.200  38.743  1.00 17.53           C  
-ATOM  30096  OG1 THR H 356      26.847  68.194  39.719  1.00 39.35           O  
-ATOM  30097  CG2 THR H 356      25.065  66.775  38.934  1.00 22.18           C  
-ATOM  30098  N   MET H 357      26.350  63.879  39.182  1.00 19.74           N  
-ATOM  30099  CA  MET H 357      25.487  62.785  38.751  1.00 16.12           C  
-ATOM  30100  C   MET H 357      24.298  62.668  39.692  1.00 17.52           C  
-ATOM  30101  O   MET H 357      24.327  63.202  40.792  1.00 16.70           O  
-ATOM  30102  CB  MET H 357      26.254  61.465  38.703  1.00 13.15           C  
-ATOM  30103  CG  MET H 357      27.213  61.341  37.538  1.00 14.65           C  
-ATOM  30104  SD  MET H 357      28.013  59.726  37.493  1.00 27.21           S  
-ATOM  30105  CE  MET H 357      28.764  59.669  39.119  1.00 15.06           C  
-ATOM  30106  N   ARG H 358      23.243  61.992  39.254  1.00 14.20           N  
-ATOM  30107  CA  ARG H 358      22.149  61.668  40.160  1.00 15.71           C  
-ATOM  30108  C   ARG H 358      21.428  60.408  39.697  1.00 17.69           C  
-ATOM  30109  O   ARG H 358      21.124  60.244  38.515  1.00 15.51           O  
-ATOM  30110  CB  ARG H 358      21.172  62.844  40.298  1.00 15.72           C  
-ATOM  30111  CG  ARG H 358      20.541  63.331  39.012  1.00 27.58           C  
-ATOM  30112  CD  ARG H 358      19.441  64.344  39.306  1.00 25.79           C  
-ATOM  30113  NE  ARG H 358      19.955  65.528  39.990  1.00 34.75           N  
-ATOM  30114  CZ  ARG H 358      19.336  66.147  40.992  1.00 28.84           C  
-ATOM  30115  NH1 ARG H 358      18.174  65.693  41.442  1.00 23.35           N  
-ATOM  30116  NH2 ARG H 358      19.883  67.220  41.547  1.00 24.00           N  
-ATOM  30117  N   TYR H 359      21.174  59.513  40.648  1.00 18.71           N  
-ATOM  30118  CA  TYR H 359      20.603  58.209  40.343  1.00 16.26           C  
-ATOM  30119  C   TYR H 359      19.312  57.967  41.115  1.00 18.33           C  
-ATOM  30120  O   TYR H 359      19.257  58.140  42.334  1.00 17.43           O  
-ATOM  30121  CB  TYR H 359      21.620  57.103  40.643  1.00 21.94           C  
-ATOM  30122  CG  TYR H 359      22.855  57.165  39.770  1.00 19.10           C  
-ATOM  30123  CD1 TYR H 359      22.936  56.427  38.597  1.00 21.24           C  
-ATOM  30124  CD2 TYR H 359      23.936  57.968  40.111  1.00 14.34           C  
-ATOM  30125  CE1 TYR H 359      24.060  56.484  37.793  1.00 20.25           C  
-ATOM  30126  CE2 TYR H 359      25.062  58.031  39.313  1.00 12.07           C  
-ATOM  30127  CZ  TYR H 359      25.118  57.287  38.155  1.00 15.74           C  
-ATOM  30128  OH  TYR H 359      26.234  57.343  37.352  1.00 17.58           O  
-ATOM  30129  N   SER H 360      18.275  57.564  40.391  1.00 19.49           N  
-ATOM  30130  CA  SER H 360      16.972  57.314  40.987  1.00 20.93           C  
-ATOM  30131  C   SER H 360      16.980  56.040  41.832  1.00 23.35           C  
-ATOM  30132  O   SER H 360      17.644  55.063  41.485  1.00 23.86           O  
-ATOM  30133  CB  SER H 360      15.907  57.223  39.897  1.00 18.43           C  
-ATOM  30134  OG  SER H 360      14.621  57.056  40.466  1.00 42.48           O  
-ATOM  30135  N   LEU H 361      16.231  56.051  42.933  1.00 23.23           N  
-ATOM  30136  CA  LEU H 361      16.245  54.933  43.874  1.00 21.38           C  
-ATOM  30137  C   LEU H 361      14.888  54.256  44.075  1.00 24.91           C  
-ATOM  30138  O   LEU H 361      14.802  53.254  44.784  1.00 23.83           O  
-ATOM  30139  CB  LEU H 361      16.768  55.399  45.234  1.00 17.42           C  
-ATOM  30140  CG  LEU H 361      18.181  55.977  45.284  1.00 21.01           C  
-ATOM  30141  CD1 LEU H 361      18.580  56.273  46.721  1.00 14.27           C  
-ATOM  30142  CD2 LEU H 361      19.172  55.031  44.631  1.00 19.63           C  
-ATOM  30143  N   ASP H 362      13.834  54.792  43.468  1.00 27.76           N  
-ATOM  30144  CA  ASP H 362      12.491  54.270  43.717  1.00 19.47           C  
-ATOM  30145  C   ASP H 362      12.204  52.989  42.938  1.00 15.98           C  
-ATOM  30146  O   ASP H 362      11.549  52.083  43.447  1.00 15.18           O  
-ATOM  30147  CB  ASP H 362      11.433  55.324  43.386  1.00 17.61           C  
-ATOM  30148  CG  ASP H 362      11.480  55.765  41.940  1.00 17.63           C  
-ATOM  30149  OD1 ASP H 362      12.590  56.027  41.434  1.00 17.58           O  
-ATOM  30150  OD2 ASP H 362      10.406  55.843  41.307  1.00 17.31           O  
-ATOM  30151  N   GLN H 363      12.693  52.914  41.705  1.00 21.07           N  
-ATOM  30152  CA  GLN H 363      12.431  51.755  40.861  1.00 17.77           C  
-ATOM  30153  C   GLN H 363      13.509  50.690  41.037  1.00 17.04           C  
-ATOM  30154  O   GLN H 363      13.203  49.519  41.247  1.00 14.59           O  
-ATOM  30155  CB  GLN H 363      12.337  52.170  39.394  1.00 23.61           C  
-ATOM  30156  CG  GLN H 363      11.180  53.112  39.085  1.00 32.83           C  
-ATOM  30157  CD  GLN H 363       9.858  52.387  38.921  1.00 34.68           C  
-ATOM  30158  OE1 GLN H 363       9.706  51.540  38.040  1.00 26.98           O  
-ATOM  30159  NE2 GLN H 363       8.892  52.718  39.771  1.00 41.16           N  
-ATOM  30160  N   ALA H 364      14.771  51.099  40.961  1.00 18.18           N  
-ATOM  30161  CA  ALA H 364      15.873  50.144  41.030  1.00 18.19           C  
-ATOM  30162  C   ALA H 364      17.070  50.694  41.796  1.00 17.22           C  
-ATOM  30163  O   ALA H 364      17.034  51.815  42.303  1.00 18.88           O  
-ATOM  30164  CB  ALA H 364      16.292  49.732  39.630  1.00 17.84           C  
-ATOM  30165  N   PHE H 365      18.126  49.889  41.873  1.00 17.53           N  
-ATOM  30166  CA  PHE H 365      19.350  50.268  42.573  1.00 19.36           C  
-ATOM  30167  C   PHE H 365      20.498  50.420  41.578  1.00 17.17           C  
-ATOM  30168  O   PHE H 365      20.743  49.530  40.766  1.00 16.92           O  
-ATOM  30169  CB  PHE H 365      19.704  49.231  43.648  1.00 17.07           C  
-ATOM  30170  CG  PHE H 365      20.844  49.641  44.542  1.00 14.41           C  
-ATOM  30171  CD1 PHE H 365      22.153  49.335  44.204  1.00 18.45           C  
-ATOM  30172  CD2 PHE H 365      20.605  50.318  45.726  1.00 13.38           C  
-ATOM  30173  CE1 PHE H 365      23.203  49.708  45.025  1.00 16.58           C  
-ATOM  30174  CE2 PHE H 365      21.651  50.693  46.551  1.00 17.00           C  
-ATOM  30175  CZ  PHE H 365      22.951  50.387  46.199  1.00 15.18           C  
-ATOM  30176  N   PRO H 366      21.210  51.554  41.647  1.00 15.85           N  
-ATOM  30177  CA  PRO H 366      22.276  51.861  40.691  1.00 15.50           C  
-ATOM  30178  C   PRO H 366      23.554  51.067  40.939  1.00 21.14           C  
-ATOM  30179  O   PRO H 366      24.602  51.660  41.196  1.00 32.00           O  
-ATOM  30180  CB  PRO H 366      22.516  53.355  40.915  1.00 18.82           C  
-ATOM  30181  CG  PRO H 366      22.184  53.561  42.349  1.00 20.29           C  
-ATOM  30182  CD  PRO H 366      21.037  52.628  42.642  1.00 16.05           C  
-ATOM  30183  N   LEU H 367      23.468  49.743  40.864  1.00 20.47           N  
-ATOM  30184  CA  LEU H 367      24.664  48.911  40.903  1.00 22.71           C  
-ATOM  30185  C   LEU H 367      25.186  48.743  39.480  1.00 21.69           C  
-ATOM  30186  O   LEU H 367      24.626  47.978  38.695  1.00 23.65           O  
-ATOM  30187  CB  LEU H 367      24.373  47.554  41.544  1.00 16.52           C  
-ATOM  30188  CG  LEU H 367      25.600  46.721  41.922  1.00 15.77           C  
-ATOM  30189  CD1 LEU H 367      26.498  47.485  42.884  1.00 14.23           C  
-ATOM  30190  CD2 LEU H 367      25.181  45.393  42.528  1.00 18.19           C  
-ATOM  30191  N   LEU H 368      26.256  49.468  39.165  1.00 14.75           N  
-ATOM  30192  CA  LEU H 368      26.790  49.583  37.804  1.00 23.23           C  
-ATOM  30193  C   LEU H 368      26.916  48.241  37.077  1.00 27.56           C  
-ATOM  30194  O   LEU H 368      27.325  47.241  37.667  1.00 26.69           O  
-ATOM  30195  CB  LEU H 368      28.152  50.284  37.839  1.00 34.23           C  
-ATOM  30196  CG  LEU H 368      28.180  51.797  38.104  1.00 41.83           C  
-ATOM  30197  CD1 LEU H 368      27.332  52.544  37.087  1.00 26.88           C  
-ATOM  30198  CD2 LEU H 368      27.747  52.156  39.527  1.00 50.33           C  
-ATOM  30199  N   THR H 369      26.564  48.229  35.793  1.00 25.96           N  
-ATOM  30200  CA  THR H 369      26.449  46.978  35.048  1.00 22.61           C  
-ATOM  30201  C   THR H 369      27.517  46.778  33.973  1.00 22.05           C  
-ATOM  30202  O   THR H 369      27.748  45.650  33.537  1.00 26.81           O  
-ATOM  30203  CB  THR H 369      25.069  46.861  34.371  1.00 19.50           C  
-ATOM  30204  OG1 THR H 369      24.892  47.942  33.448  1.00 26.46           O  
-ATOM  30205  CG2 THR H 369      23.961  46.898  35.407  1.00 18.51           C  
-ATOM  30206  N   THR H 370      28.165  47.857  33.543  1.00 20.63           N  
-ATOM  30207  CA  THR H 370      29.191  47.756  32.505  1.00 24.54           C  
-ATOM  30208  C   THR H 370      30.441  47.060  33.035  1.00 22.72           C  
-ATOM  30209  O   THR H 370      31.340  46.702  32.274  1.00 22.70           O  
-ATOM  30210  CB  THR H 370      29.584  49.136  31.945  1.00 27.64           C  
-ATOM  30211  OG1 THR H 370      30.029  49.983  33.013  1.00 32.90           O  
-ATOM  30212  CG2 THR H 370      28.400  49.780  31.240  1.00 21.50           C  
-ATOM  30213  N   LYS H 371      30.491  46.880  34.349  1.00 24.26           N  
-ATOM  30214  CA  LYS H 371      31.526  46.079  34.983  1.00 22.82           C  
-ATOM  30215  C   LYS H 371      31.009  45.625  36.342  1.00 24.83           C  
-ATOM  30216  O   LYS H 371      30.215  46.322  36.976  1.00 28.81           O  
-ATOM  30217  CB  LYS H 371      32.833  46.869  35.113  1.00 23.84           C  
-ATOM  30218  CG  LYS H 371      33.036  47.563  36.450  1.00 27.04           C  
-ATOM  30219  CD  LYS H 371      34.280  48.441  36.452  1.00 30.86           C  
-ATOM  30220  CE  LYS H 371      34.825  48.623  37.865  1.00 36.26           C  
-ATOM  30221  NZ  LYS H 371      35.893  49.662  37.907  1.00 48.70           N  
-ATOM  30222  N   ARG H 372      31.439  44.448  36.780  1.00 29.90           N  
-ATOM  30223  CA  ARG H 372      30.966  43.910  38.048  1.00 26.83           C  
-ATOM  30224  C   ARG H 372      31.483  44.754  39.213  1.00 33.05           C  
-ATOM  30225  O   ARG H 372      32.681  45.028  39.316  1.00 27.41           O  
-ATOM  30226  CB  ARG H 372      31.390  42.447  38.209  1.00 23.19           C  
-ATOM  30227  CG  ARG H 372      30.927  41.817  39.510  1.00 25.92           C  
-ATOM  30228  CD  ARG H 372      31.045  40.303  39.481  1.00 31.28           C  
-ATOM  30229  NE  ARG H 372      30.033  39.685  38.628  1.00 30.01           N  
-ATOM  30230  CZ  ARG H 372      28.790  39.418  39.019  1.00 32.56           C  
-ATOM  30231  NH1 ARG H 372      28.400  39.721  40.251  1.00 26.16           N  
-ATOM  30232  NH2 ARG H 372      27.934  38.854  38.178  1.00 30.13           N  
-ATOM  30233  N   VAL H 373      30.565  45.178  40.077  1.00 27.19           N  
-ATOM  30234  CA  VAL H 373      30.908  46.003  41.229  1.00 21.69           C  
-ATOM  30235  C   VAL H 373      30.985  45.154  42.498  1.00 22.98           C  
-ATOM  30236  O   VAL H 373      30.150  44.279  42.718  1.00 22.90           O  
-ATOM  30237  CB  VAL H 373      29.885  47.144  41.414  1.00 24.21           C  
-ATOM  30238  CG1 VAL H 373      30.157  47.920  42.699  1.00 25.52           C  
-ATOM  30239  CG2 VAL H 373      29.912  48.071  40.209  1.00 27.39           C  
-ATOM  30240  N   PHE H 374      31.997  45.413  43.323  1.00 24.14           N  
-ATOM  30241  CA  PHE H 374      32.221  44.632  44.538  1.00 25.61           C  
-ATOM  30242  C   PHE H 374      31.181  44.938  45.620  1.00 24.03           C  
-ATOM  30243  O   PHE H 374      31.446  45.652  46.595  1.00 30.51           O  
-ATOM  30244  CB  PHE H 374      33.635  44.875  45.067  1.00 25.60           C  
-ATOM  30245  CG  PHE H 374      34.080  43.864  46.078  1.00 22.97           C  
-ATOM  30246  CD1 PHE H 374      33.704  42.539  45.957  1.00 25.30           C  
-ATOM  30247  CD2 PHE H 374      34.882  44.234  47.142  1.00 28.67           C  
-ATOM  30248  CE1 PHE H 374      34.111  41.601  46.886  1.00 31.30           C  
-ATOM  30249  CE2 PHE H 374      35.295  43.303  48.075  1.00 29.44           C  
-ATOM  30250  CZ  PHE H 374      34.908  41.983  47.947  1.00 26.63           C  
-ATOM  30251  N   TRP H 375      29.996  44.367  45.438  1.00 18.61           N  
-ATOM  30252  CA  TRP H 375      28.860  44.632  46.308  1.00 17.15           C  
-ATOM  30253  C   TRP H 375      29.107  44.258  47.763  1.00 20.92           C  
-ATOM  30254  O   TRP H 375      28.742  45.009  48.668  1.00 25.85           O  
-ATOM  30255  CB  TRP H 375      27.626  43.889  45.803  1.00 15.72           C  
-ATOM  30256  CG  TRP H 375      26.541  43.818  46.822  1.00 12.88           C  
-ATOM  30257  CD1 TRP H 375      26.172  42.729  47.552  1.00 10.88           C  
-ATOM  30258  CD2 TRP H 375      25.694  44.890  47.243  1.00 15.30           C  
-ATOM  30259  NE1 TRP H 375      25.139  43.052  48.397  1.00 14.00           N  
-ATOM  30260  CE2 TRP H 375      24.827  44.377  48.227  1.00 15.91           C  
-ATOM  30261  CE3 TRP H 375      25.582  46.235  46.882  1.00 13.13           C  
-ATOM  30262  CZ2 TRP H 375      23.858  45.157  48.852  1.00 15.64           C  
-ATOM  30263  CZ3 TRP H 375      24.620  47.011  47.503  1.00 18.06           C  
-ATOM  30264  CH2 TRP H 375      23.770  46.470  48.477  1.00 16.46           C  
-ATOM  30265  N   LYS H 376      29.705  43.091  47.986  1.00 17.06           N  
-ATOM  30266  CA  LYS H 376      30.018  42.644  49.338  1.00 19.06           C  
-ATOM  30267  C   LYS H 376      30.931  43.651  50.026  1.00 20.02           C  
-ATOM  30268  O   LYS H 376      30.752  43.971  51.197  1.00 17.20           O  
-ATOM  30269  CB  LYS H 376      30.675  41.261  49.319  1.00 25.05           C  
-ATOM  30270  CG  LYS H 376      30.659  40.565  50.671  1.00 37.16           C  
-ATOM  30271  CD  LYS H 376      32.023  40.013  51.059  1.00 35.07           C  
-ATOM  30272  CE  LYS H 376      32.463  38.881  50.142  1.00 47.79           C  
-ATOM  30273  NZ  LYS H 376      33.726  38.247  50.620  1.00 38.46           N  
-ATOM  30274  N   GLY H 377      31.904  44.157  49.278  1.00 22.12           N  
-ATOM  30275  CA  GLY H 377      32.802  45.176  49.784  1.00 21.15           C  
-ATOM  30276  C   GLY H 377      32.062  46.452  50.123  1.00 20.08           C  
-ATOM  30277  O   GLY H 377      32.328  47.075  51.152  1.00 20.92           O  
-ATOM  30278  N   VAL H 378      31.133  46.844  49.255  1.00 17.99           N  
-ATOM  30279  CA  VAL H 378      30.292  48.011  49.523  1.00 20.61           C  
-ATOM  30280  C   VAL H 378      29.559  47.862  50.856  1.00 23.08           C  
-ATOM  30281  O   VAL H 378      29.714  48.693  51.763  1.00 30.48           O  
-ATOM  30282  CB  VAL H 378      29.260  48.238  48.396  1.00 17.04           C  
-ATOM  30283  CG1 VAL H 378      28.236  49.283  48.808  1.00 14.07           C  
-ATOM  30284  CG2 VAL H 378      29.957  48.640  47.110  1.00 19.27           C  
-ATOM  30285  N   LEU H 379      28.780  46.790  50.960  1.00 18.37           N  
-ATOM  30286  CA  LEU H 379      27.984  46.488  52.141  1.00 20.04           C  
-ATOM  30287  C   LEU H 379      28.807  46.437  53.426  1.00 20.68           C  
-ATOM  30288  O   LEU H 379      28.485  47.102  54.411  1.00 19.86           O  
-ATOM  30289  CB  LEU H 379      27.247  45.158  51.925  1.00 18.42           C  
-ATOM  30290  CG  LEU H 379      26.375  44.663  53.082  1.00 25.09           C  
-ATOM  30291  CD1 LEU H 379      25.405  45.742  53.543  1.00 22.69           C  
-ATOM  30292  CD2 LEU H 379      25.627  43.409  52.666  1.00 24.55           C  
-ATOM  30293  N   GLU H 380      29.871  45.645  53.403  1.00 20.82           N  
-ATOM  30294  CA  GLU H 380      30.731  45.480  54.567  1.00 20.12           C  
-ATOM  30295  C   GLU H 380      31.404  46.783  54.972  1.00 22.69           C  
-ATOM  30296  O   GLU H 380      31.482  47.093  56.162  1.00 27.13           O  
-ATOM  30297  CB  GLU H 380      31.800  44.409  54.311  1.00 22.08           C  
-ATOM  30298  CG  GLU H 380      31.257  42.987  54.196  1.00 34.25           C  
-ATOM  30299  CD  GLU H 380      30.746  42.420  55.517  1.00 37.33           C  
-ATOM  30300  OE1 GLU H 380      30.862  43.103  56.559  1.00 34.00           O  
-ATOM  30301  OE2 GLU H 380      30.230  41.279  55.512  1.00 30.16           O  
-ATOM  30302  N   GLU H 381      31.890  47.546  53.996  1.00 18.53           N  
-ATOM  30303  CA  GLU H 381      32.522  48.822  54.319  1.00 19.07           C  
-ATOM  30304  C   GLU H 381      31.511  49.799  54.913  1.00 21.94           C  
-ATOM  30305  O   GLU H 381      31.852  50.593  55.792  1.00 20.76           O  
-ATOM  30306  CB  GLU H 381      33.186  49.447  53.090  1.00 20.14           C  
-ATOM  30307  CG  GLU H 381      34.138  50.589  53.433  1.00 19.42           C  
-ATOM  30308  CD  GLU H 381      34.327  51.560  52.284  1.00 34.28           C  
-ATOM  30309  OE1 GLU H 381      33.378  51.732  51.489  1.00 42.75           O  
-ATOM  30310  OE2 GLU H 381      35.420  52.157  52.179  1.00 35.14           O  
-ATOM  30311  N   LEU H 382      30.271  49.749  54.431  1.00 22.19           N  
-ATOM  30312  CA  LEU H 382      29.236  50.637  54.957  1.00 17.90           C  
-ATOM  30313  C   LEU H 382      28.851  50.269  56.388  1.00 17.72           C  
-ATOM  30314  O   LEU H 382      28.699  51.143  57.240  1.00 19.87           O  
-ATOM  30315  CB  LEU H 382      27.993  50.625  54.057  1.00 18.08           C  
-ATOM  30316  CG  LEU H 382      26.849  51.563  54.470  1.00 21.48           C  
-ATOM  30317  CD1 LEU H 382      27.379  52.944  54.823  1.00 16.60           C  
-ATOM  30318  CD2 LEU H 382      25.801  51.660  53.364  1.00 17.40           C  
-ATOM  30319  N   LEU H 383      28.690  48.977  56.650  1.00 19.00           N  
-ATOM  30320  CA  LEU H 383      28.386  48.515  58.002  1.00 16.08           C  
-ATOM  30321  C   LEU H 383      29.521  48.894  58.951  1.00 21.50           C  
-ATOM  30322  O   LEU H 383      29.287  49.347  60.072  1.00 23.32           O  
-ATOM  30323  CB  LEU H 383      28.151  47.004  58.010  1.00 15.12           C  
-ATOM  30324  CG  LEU H 383      26.885  46.536  57.290  1.00 11.09           C  
-ATOM  30325  CD1 LEU H 383      26.870  45.028  57.141  1.00 20.93           C  
-ATOM  30326  CD2 LEU H 383      25.650  47.005  58.030  1.00 17.20           C  
-ATOM  30327  N   TRP H 384      30.748  48.698  58.476  1.00 21.70           N  
-ATOM  30328  CA  TRP H 384      31.966  49.172  59.127  1.00 21.15           C  
-ATOM  30329  C   TRP H 384      31.839  50.642  59.542  1.00 22.69           C  
-ATOM  30330  O   TRP H 384      31.946  50.991  60.729  1.00 21.31           O  
-ATOM  30331  CB  TRP H 384      33.142  48.967  58.163  1.00 18.47           C  
-ATOM  30332  CG  TRP H 384      34.510  48.986  58.763  1.00 17.10           C  
-ATOM  30333  CD1 TRP H 384      34.989  48.171  59.744  1.00 16.81           C  
-ATOM  30334  CD2 TRP H 384      35.598  49.830  58.376  1.00 18.61           C  
-ATOM  30335  NE1 TRP H 384      36.300  48.475  60.014  1.00 16.68           N  
-ATOM  30336  CE2 TRP H 384      36.700  49.493  59.182  1.00 18.30           C  
-ATOM  30337  CE3 TRP H 384      35.746  50.852  57.431  1.00 18.53           C  
-ATOM  30338  CZ2 TRP H 384      37.931  50.135  59.078  1.00 22.47           C  
-ATOM  30339  CZ3 TRP H 384      36.967  51.488  57.326  1.00 17.43           C  
-ATOM  30340  CH2 TRP H 384      38.043  51.129  58.143  1.00 19.52           C  
-ATOM  30341  N   PHE H 385      31.605  51.490  58.543  1.00 20.31           N  
-ATOM  30342  CA  PHE H 385      31.375  52.914  58.750  1.00 21.56           C  
-ATOM  30343  C   PHE H 385      30.373  53.184  59.858  1.00 22.15           C  
-ATOM  30344  O   PHE H 385      30.657  53.939  60.784  1.00 23.68           O  
-ATOM  30345  CB  PHE H 385      30.875  53.567  57.460  1.00 20.49           C  
-ATOM  30346  CG  PHE H 385      31.926  53.725  56.410  1.00 28.90           C  
-ATOM  30347  CD1 PHE H 385      33.269  53.649  56.737  1.00 31.71           C  
-ATOM  30348  CD2 PHE H 385      31.571  53.959  55.092  1.00 27.38           C  
-ATOM  30349  CE1 PHE H 385      34.242  53.800  55.767  1.00 31.80           C  
-ATOM  30350  CE2 PHE H 385      32.539  54.111  54.114  1.00 29.39           C  
-ATOM  30351  CZ  PHE H 385      33.876  54.032  54.453  1.00 37.24           C  
-ATOM  30352  N   ILE H 386      29.203  52.561  59.752  1.00 17.84           N  
-ATOM  30353  CA  ILE H 386      28.124  52.806  60.700  1.00 16.14           C  
-ATOM  30354  C   ILE H 386      28.498  52.382  62.119  1.00 17.70           C  
-ATOM  30355  O   ILE H 386      28.135  53.052  63.085  1.00 20.86           O  
-ATOM  30356  CB  ILE H 386      26.831  52.090  60.260  1.00 16.63           C  
-ATOM  30357  CG1 ILE H 386      26.403  52.603  58.887  1.00 16.74           C  
-ATOM  30358  CG2 ILE H 386      25.715  52.324  61.267  1.00 14.86           C  
-ATOM  30359  CD1 ILE H 386      25.105  52.035  58.413  1.00 18.00           C  
-ATOM  30360  N   ARG H 387      29.230  51.280  62.249  1.00 28.71           N  
-ATOM  30361  CA  ARG H 387      29.730  50.885  63.562  1.00 23.55           C  
-ATOM  30362  C   ARG H 387      30.739  51.913  64.060  1.00 23.23           C  
-ATOM  30363  O   ARG H 387      30.910  52.102  65.264  1.00 21.94           O  
-ATOM  30364  CB  ARG H 387      30.376  49.500  63.520  1.00 24.87           C  
-ATOM  30365  CG  ARG H 387      29.433  48.374  63.140  1.00 28.15           C  
-ATOM  30366  CD  ARG H 387      30.093  47.016  63.332  1.00 25.40           C  
-ATOM  30367  NE  ARG H 387      29.493  45.998  62.475  1.00 30.09           N  
-ATOM  30368  CZ  ARG H 387      30.089  45.478  61.407  1.00 25.40           C  
-ATOM  30369  NH1 ARG H 387      31.309  45.873  61.068  1.00 25.09           N  
-ATOM  30370  NH2 ARG H 387      29.471  44.556  60.683  1.00 33.12           N  
-ATOM  30371  N   GLY H 388      31.400  52.587  63.124  1.00 23.20           N  
-ATOM  30372  CA  GLY H 388      32.416  53.557  63.485  1.00 19.50           C  
-ATOM  30373  C   GLY H 388      33.696  52.822  63.812  1.00 28.82           C  
-ATOM  30374  O   GLY H 388      34.479  53.237  64.666  1.00 21.99           O  
-ATOM  30375  N   ASP H 389      33.892  51.706  63.122  1.00 23.62           N  
-ATOM  30376  CA  ASP H 389      35.077  50.886  63.285  1.00 17.14           C  
-ATOM  30377  C   ASP H 389      36.230  51.497  62.498  1.00 23.00           C  
-ATOM  30378  O   ASP H 389      36.048  51.947  61.367  1.00 20.43           O  
-ATOM  30379  CB  ASP H 389      34.786  49.463  62.815  1.00 21.33           C  
-ATOM  30380  CG  ASP H 389      35.814  48.460  63.291  1.00 26.10           C  
-ATOM  30381  OD1 ASP H 389      36.872  48.871  63.816  1.00 20.15           O  
-ATOM  30382  OD2 ASP H 389      35.558  47.247  63.127  1.00 26.78           O  
-ATOM  30383  N   THR H 390      37.414  51.524  63.102  1.00 35.18           N  
-ATOM  30384  CA  THR H 390      38.592  52.077  62.442  1.00 20.86           C  
-ATOM  30385  C   THR H 390      39.657  51.003  62.256  1.00 19.74           C  
-ATOM  30386  O   THR H 390      40.819  51.301  61.987  1.00 24.48           O  
-ATOM  30387  CB  THR H 390      39.183  53.256  63.236  1.00 20.63           C  
-ATOM  30388  OG1 THR H 390      39.504  52.828  64.566  1.00 21.79           O  
-ATOM  30389  CG2 THR H 390      38.184  54.397  63.308  1.00 21.20           C  
-ATOM  30390  N   ASN H 391      39.243  49.750  62.402  1.00 18.49           N  
-ATOM  30391  CA  ASN H 391      40.131  48.610  62.219  1.00 21.70           C  
-ATOM  30392  C   ASN H 391      39.925  47.991  60.840  1.00 22.28           C  
-ATOM  30393  O   ASN H 391      38.899  47.364  60.585  1.00 27.54           O  
-ATOM  30394  CB  ASN H 391      39.889  47.570  63.318  1.00 21.55           C  
-ATOM  30395  CG  ASN H 391      40.965  46.500  63.367  1.00 21.67           C  
-ATOM  30396  OD1 ASN H 391      41.764  46.361  62.444  1.00 24.78           O  
-ATOM  30397  ND2 ASN H 391      40.989  45.737  64.452  1.00 24.19           N  
-ATOM  30398  N   ALA H 392      40.898  48.166  59.953  1.00 17.22           N  
-ATOM  30399  CA  ALA H 392      40.785  47.658  58.589  1.00 25.33           C  
-ATOM  30400  C   ALA H 392      40.896  46.136  58.532  1.00 28.10           C  
-ATOM  30401  O   ALA H 392      40.472  45.509  57.561  1.00 33.09           O  
-ATOM  30402  CB  ALA H 392      41.843  48.294  57.702  1.00 30.65           C  
-ATOM  30403  N   ASN H 393      41.468  45.547  59.575  1.00 24.20           N  
-ATOM  30404  CA  ASN H 393      41.629  44.102  59.636  1.00 25.28           C  
-ATOM  30405  C   ASN H 393      40.284  43.395  59.726  1.00 31.10           C  
-ATOM  30406  O   ASN H 393      40.147  42.246  59.307  1.00 38.18           O  
-ATOM  30407  CB  ASN H 393      42.513  43.715  60.821  1.00 30.00           C  
-ATOM  30408  CG  ASN H 393      43.895  44.328  60.738  1.00 25.04           C  
-ATOM  30409  OD1 ASN H 393      44.563  44.243  59.709  1.00 25.24           O  
-ATOM  30410  ND2 ASN H 393      44.325  44.963  61.820  1.00 32.87           N  
-ATOM  30411  N   HIS H 394      39.291  44.090  60.271  1.00 28.81           N  
-ATOM  30412  CA  HIS H 394      37.935  43.558  60.344  1.00 26.90           C  
-ATOM  30413  C   HIS H 394      37.319  43.467  58.952  1.00 28.20           C  
-ATOM  30414  O   HIS H 394      36.463  42.622  58.689  1.00 27.61           O  
-ATOM  30415  CB  HIS H 394      37.069  44.426  61.254  1.00 25.17           C  
-ATOM  30416  CG  HIS H 394      37.498  44.411  62.687  1.00 24.70           C  
-ATOM  30417  ND1 HIS H 394      36.949  45.244  63.638  1.00 21.52           N  
-ATOM  30418  CD2 HIS H 394      38.419  43.658  63.335  1.00 29.24           C  
-ATOM  30419  CE1 HIS H 394      37.514  45.007  64.808  1.00 21.41           C  
-ATOM  30420  NE2 HIS H 394      38.410  44.048  64.651  1.00 23.87           N  
-ATOM  30421  N   LEU H 395      37.767  44.351  58.069  1.00 29.20           N  
-ATOM  30422  CA  LEU H 395      37.348  44.338  56.675  1.00 27.46           C  
-ATOM  30423  C   LEU H 395      38.127  43.280  55.900  1.00 33.98           C  
-ATOM  30424  O   LEU H 395      37.576  42.577  55.052  1.00 28.83           O  
-ATOM  30425  CB  LEU H 395      37.552  45.717  56.045  1.00 21.21           C  
-ATOM  30426  CG  LEU H 395      36.315  46.442  55.517  1.00 22.91           C  
-ATOM  30427  CD1 LEU H 395      35.165  46.350  56.509  1.00 18.90           C  
-ATOM  30428  CD2 LEU H 395      36.653  47.895  55.218  1.00 20.51           C  
-ATOM  30429  N   SER H 396      39.416  43.173  56.209  1.00 38.19           N  
-ATOM  30430  CA  SER H 396      40.320  42.270  55.512  1.00 30.11           C  
-ATOM  30431  C   SER H 396      39.998  40.806  55.812  1.00 31.36           C  
-ATOM  30432  O   SER H 396      40.131  39.944  54.944  1.00 30.25           O  
-ATOM  30433  CB  SER H 396      41.768  42.586  55.895  1.00 29.06           C  
-ATOM  30434  OG  SER H 396      42.679  42.040  54.957  1.00 37.88           O  
-ATOM  30435  N  AGLU H 397      39.580  40.542  57.046  0.42 48.86           N  
-ATOM  30436  N  BGLU H 397      39.562  40.529  57.036  0.58 55.80           N  
-ATOM  30437  CA AGLU H 397      39.228  39.196  57.485  0.42 36.07           C  
-ATOM  30438  CA BGLU H 397      39.261  39.159  57.439  0.58 37.09           C  
-ATOM  30439  C  AGLU H 397      38.035  38.664  56.699  0.42 36.03           C  
-ATOM  30440  C  BGLU H 397      37.948  38.654  56.842  0.58 36.08           C  
-ATOM  30441  O  AGLU H 397      37.932  37.464  56.437  0.42 34.34           O  
-ATOM  30442  O  BGLU H 397      37.672  37.453  56.861  0.58 34.98           O  
-ATOM  30443  CB AGLU H 397      38.932  39.190  58.991  0.42 32.69           C  
-ATOM  30444  CB BGLU H 397      39.232  39.050  58.965  0.58 32.51           C  
-ATOM  30445  CG AGLU H 397      38.295  37.911  59.523  0.42 32.43           C  
-ATOM  30446  CG BGLU H 397      40.608  38.819  59.571  0.58 30.87           C  
-ATOM  30447  CD AGLU H 397      36.783  38.008  59.620  0.42 31.24           C  
-ATOM  30448  CD BGLU H 397      40.828  39.596  60.851  0.58 29.81           C  
-ATOM  30449  OE1AGLU H 397      36.108  36.962  59.507  0.42 25.13           O  
-ATOM  30450  OE1BGLU H 397      39.830  39.991  61.489  0.58 28.87           O  
-ATOM  30451  OE2AGLU H 397      36.271  39.130  59.816  0.42 30.99           O  
-ATOM  30452  OE2BGLU H 397      42.003  39.819  61.215  0.58 23.32           O  
-ATOM  30453  N   LYS H 398      37.143  39.569  56.308  1.00 34.88           N  
-ATOM  30454  CA  LYS H 398      35.928  39.191  55.594  1.00 28.17           C  
-ATOM  30455  C   LYS H 398      36.147  39.171  54.082  1.00 30.84           C  
-ATOM  30456  O   LYS H 398      35.196  39.053  53.310  1.00 26.99           O  
-ATOM  30457  CB  LYS H 398      34.780  40.141  55.933  1.00 30.10           C  
-ATOM  30458  CG  LYS H 398      34.391  40.167  57.400  1.00 31.32           C  
-ATOM  30459  CD  LYS H 398      33.056  40.870  57.592  1.00 20.86           C  
-ATOM  30460  CE  LYS H 398      33.051  41.713  58.854  1.00 18.95           C  
-ATOM  30461  NZ  LYS H 398      33.353  40.901  60.062  1.00 24.78           N  
-ATOM  30462  N   GLY H 399      37.403  39.292  53.664  1.00 37.52           N  
-ATOM  30463  CA  GLY H 399      37.739  39.228  52.253  1.00 33.91           C  
-ATOM  30464  C   GLY H 399      37.687  40.577  51.565  1.00 35.70           C  
-ATOM  30465  O   GLY H 399      37.945  40.680  50.366  1.00 40.88           O  
-ATOM  30466  N   VAL H 400      37.352  41.614  52.326  1.00 33.73           N  
-ATOM  30467  CA  VAL H 400      37.291  42.971  51.793  1.00 34.43           C  
-ATOM  30468  C   VAL H 400      38.580  43.723  52.097  1.00 31.56           C  
-ATOM  30469  O   VAL H 400      38.729  44.301  53.170  1.00 32.55           O  
-ATOM  30470  CB  VAL H 400      36.096  43.756  52.374  1.00 30.35           C  
-ATOM  30471  CG1 VAL H 400      36.018  45.143  51.756  1.00 27.56           C  
-ATOM  30472  CG2 VAL H 400      34.800  42.997  52.144  1.00 30.76           C  
-ATOM  30473  N   LYS H 401      39.512  43.720  51.150  1.00 30.65           N  
-ATOM  30474  CA  LYS H 401      40.812  44.342  51.383  1.00 38.94           C  
-ATOM  30475  C   LYS H 401      41.029  45.608  50.563  1.00 39.30           C  
-ATOM  30476  O   LYS H 401      42.094  45.812  49.987  1.00 57.36           O  
-ATOM  30477  CB  LYS H 401      41.930  43.333  51.106  1.00 46.55           C  
-ATOM  30478  CG  LYS H 401      41.627  42.321  50.016  1.00 49.55           C  
-ATOM  30479  CD  LYS H 401      42.512  41.091  50.181  1.00 63.38           C  
-ATOM  30480  CE  LYS H 401      42.680  40.321  48.876  1.00 72.79           C  
-ATOM  30481  NZ  LYS H 401      41.423  39.666  48.414  1.00 66.17           N  
-ATOM  30482  N   ILE H 402      40.017  46.467  50.533  1.00 35.94           N  
-ATOM  30483  CA  ILE H 402      40.102  47.723  49.799  1.00 31.97           C  
-ATOM  30484  C   ILE H 402      40.906  48.764  50.562  1.00 40.71           C  
-ATOM  30485  O   ILE H 402      41.243  49.813  50.019  1.00 50.14           O  
-ATOM  30486  CB  ILE H 402      38.709  48.306  49.505  1.00 33.74           C  
-ATOM  30487  CG1 ILE H 402      37.975  48.616  50.810  1.00 34.47           C  
-ATOM  30488  CG2 ILE H 402      37.899  47.350  48.652  1.00 42.73           C  
-ATOM  30489  CD1 ILE H 402      36.562  49.116  50.619  1.00 31.06           C  
-ATOM  30490  N   TRP H 403      41.214  48.474  51.820  1.00 42.25           N  
-ATOM  30491  CA  TRP H 403      41.886  49.439  52.681  1.00 40.95           C  
-ATOM  30492  C   TRP H 403      43.341  49.097  52.965  1.00 42.04           C  
-ATOM  30493  O   TRP H 403      44.108  49.957  53.390  1.00 42.60           O  
-ATOM  30494  CB  TRP H 403      41.135  49.565  54.006  1.00 34.33           C  
-ATOM  30495  CG  TRP H 403      40.103  50.628  54.006  1.00 38.59           C  
-ATOM  30496  CD1 TRP H 403      38.752  50.459  53.960  1.00 39.02           C  
-ATOM  30497  CD2 TRP H 403      40.333  52.040  54.055  1.00 47.79           C  
-ATOM  30498  NE1 TRP H 403      38.124  51.679  53.981  1.00 51.71           N  
-ATOM  30499  CE2 TRP H 403      39.072  52.666  54.039  1.00 60.71           C  
-ATOM  30500  CE3 TRP H 403      41.482  52.835  54.111  1.00 57.13           C  
-ATOM  30501  CZ2 TRP H 403      38.926  54.051  54.077  1.00 58.61           C  
-ATOM  30502  CZ3 TRP H 403      41.334  54.213  54.149  1.00 65.82           C  
-ATOM  30503  CH2 TRP H 403      40.065  54.805  54.132  1.00 62.94           C  
-ATOM  30504  N   ASP H 404      43.714  47.846  52.723  1.00 49.18           N  
-ATOM  30505  CA  ASP H 404      45.004  47.323  53.163  1.00 54.40           C  
-ATOM  30506  C   ASP H 404      46.208  48.135  52.681  1.00 43.99           C  
-ATOM  30507  O   ASP H 404      47.097  48.460  53.473  1.00 35.08           O  
-ATOM  30508  CB  ASP H 404      45.148  45.864  52.725  1.00 59.04           C  
-ATOM  30509  CG  ASP H 404      44.275  44.923  53.544  1.00 69.19           C  
-ATOM  30510  OD1 ASP H 404      43.681  45.374  54.549  1.00 55.72           O  
-ATOM  30511  OD2 ASP H 404      44.197  43.729  53.191  1.00 70.88           O  
-ATOM  30512  N   LYS H 405      46.228  48.477  51.396  1.00 43.11           N  
-ATOM  30513  CA  LYS H 405      47.349  49.215  50.817  1.00 38.94           C  
-ATOM  30514  C   LYS H 405      47.527  50.597  51.450  1.00 33.98           C  
-ATOM  30515  O   LYS H 405      48.563  51.232  51.271  1.00 32.77           O  
-ATOM  30516  CB  LYS H 405      47.174  49.347  49.300  1.00 32.71           C  
-ATOM  30517  CG  LYS H 405      47.239  48.024  48.556  1.00 40.60           C  
-ATOM  30518  CD  LYS H 405      47.218  48.234  47.054  1.00 33.69           C  
-ATOM  30519  CE  LYS H 405      47.261  46.910  46.318  1.00 23.84           C  
-ATOM  30520  NZ  LYS H 405      47.257  47.103  44.842  1.00 32.38           N  
-ATOM  30521  N   ASN H 406      46.522  51.054  52.195  1.00 36.27           N  
-ATOM  30522  CA  ASN H 406      46.582  52.356  52.856  1.00 32.27           C  
-ATOM  30523  C   ASN H 406      46.762  52.241  54.367  1.00 32.48           C  
-ATOM  30524  O   ASN H 406      46.739  53.243  55.078  1.00 27.38           O  
-ATOM  30525  CB  ASN H 406      45.322  53.168  52.545  1.00 31.62           C  
-ATOM  30526  CG  ASN H 406      45.260  53.609  51.096  1.00 41.64           C  
-ATOM  30527  OD1 ASN H 406      44.370  53.204  50.352  1.00 52.12           O  
-ATOM  30528  ND2 ASN H 406      46.210  54.444  50.688  1.00 39.82           N  
-ATOM  30529  N   VAL H 407      46.931  51.016  54.856  1.00 33.82           N  
-ATOM  30530  CA  VAL H 407      47.154  50.794  56.285  1.00 32.31           C  
-ATOM  30531  C   VAL H 407      48.333  49.859  56.542  1.00 35.43           C  
-ATOM  30532  O   VAL H 407      48.431  49.241  57.604  1.00 36.78           O  
-ATOM  30533  CB  VAL H 407      45.901  50.216  56.980  1.00 30.07           C  
-ATOM  30534  CG1 VAL H 407      44.769  51.229  56.965  1.00 26.65           C  
-ATOM  30535  CG2 VAL H 407      45.479  48.915  56.324  1.00 35.96           C  
-ATOM  30536  N   THR H 408      49.230  49.761  55.567  1.00 40.05           N  
-ATOM  30537  CA  THR H 408      50.474  49.028  55.753  1.00 30.13           C  
-ATOM  30538  C   THR H 408      51.457  49.857  56.569  1.00 43.21           C  
-ATOM  30539  O   THR H 408      51.310  51.078  56.685  1.00 47.24           O  
-ATOM  30540  CB  THR H 408      51.133  48.650  54.408  1.00 28.89           C  
-ATOM  30541  OG1 THR H 408      51.428  49.837  53.660  1.00 28.16           O  
-ATOM  30542  CG2 THR H 408      50.216  47.763  53.593  1.00 30.28           C  
-ATOM  30543  N   ARG H 409      52.454  49.183  57.134  1.00 46.43           N  
-ATOM  30544  CA  ARG H 409      53.509  49.840  57.898  1.00 45.10           C  
-ATOM  30545  C   ARG H 409      54.177  50.943  57.084  1.00 46.23           C  
-ATOM  30546  O   ARG H 409      54.390  52.051  57.579  1.00 44.01           O  
-ATOM  30547  CB  ARG H 409      54.550  48.812  58.351  1.00 39.42           C  
-ATOM  30548  CG  ARG H 409      55.771  49.399  59.035  1.00 43.34           C  
-ATOM  30549  CD  ARG H 409      55.595  49.466  60.542  1.00 39.88           C  
-ATOM  30550  NE  ARG H 409      54.852  50.647  60.972  1.00 45.57           N  
-ATOM  30551  CZ  ARG H 409      53.586  50.631  61.377  1.00 44.78           C  
-ATOM  30552  NH1 ARG H 409      52.911  49.490  61.409  1.00 44.08           N  
-ATOM  30553  NH2 ARG H 409      52.998  51.759  61.755  1.00 37.55           N  
-ATOM  30554  N   GLU H 410      54.492  50.630  55.831  1.00 41.38           N  
-ATOM  30555  CA  GLU H 410      55.181  51.560  54.950  1.00 41.31           C  
-ATOM  30556  C   GLU H 410      54.375  52.833  54.715  1.00 47.42           C  
-ATOM  30557  O   GLU H 410      54.906  53.940  54.824  1.00 48.55           O  
-ATOM  30558  CB  GLU H 410      55.496  50.878  53.618  1.00 44.92           C  
-ATOM  30559  CG  GLU H 410      56.437  51.663  52.725  1.00 62.23           C  
-ATOM  30560  CD  GLU H 410      56.870  50.870  51.509  1.00 61.11           C  
-ATOM  30561  OE1 GLU H 410      57.976  50.287  51.538  1.00 52.15           O  
-ATOM  30562  OE2 GLU H 410      56.103  50.830  50.523  1.00 49.57           O  
-ATOM  30563  N   PHE H 411      53.094  52.672  54.395  1.00 44.87           N  
-ATOM  30564  CA  PHE H 411      52.235  53.814  54.095  1.00 45.85           C  
-ATOM  30565  C   PHE H 411      51.950  54.635  55.346  1.00 47.51           C  
-ATOM  30566  O   PHE H 411      51.957  55.869  55.302  1.00 48.80           O  
-ATOM  30567  CB  PHE H 411      50.917  53.354  53.464  1.00 38.84           C  
-ATOM  30568  CG  PHE H 411      50.124  54.469  52.835  1.00 43.81           C  
-ATOM  30569  CD1 PHE H 411      49.203  55.193  53.575  1.00 43.15           C  
-ATOM  30570  CD2 PHE H 411      50.309  54.798  51.502  1.00 51.57           C  
-ATOM  30571  CE1 PHE H 411      48.478  56.224  52.995  1.00 44.47           C  
-ATOM  30572  CE2 PHE H 411      49.588  55.824  50.917  1.00 52.52           C  
-ATOM  30573  CZ  PHE H 411      48.672  56.537  51.663  1.00 43.84           C  
-ATOM  30574  N   LEU H 412      51.691  53.949  56.456  1.00 37.43           N  
-ATOM  30575  CA  LEU H 412      51.470  54.623  57.728  1.00 33.38           C  
-ATOM  30576  C   LEU H 412      52.688  55.446  58.107  1.00 38.42           C  
-ATOM  30577  O   LEU H 412      52.562  56.554  58.631  1.00 38.43           O  
-ATOM  30578  CB  LEU H 412      51.151  53.614  58.831  1.00 37.81           C  
-ATOM  30579  CG  LEU H 412      49.736  53.035  58.832  1.00 33.77           C  
-ATOM  30580  CD1 LEU H 412      49.609  51.952  59.886  1.00 34.42           C  
-ATOM  30581  CD2 LEU H 412      48.709  54.131  59.061  1.00 38.98           C  
-ATOM  30582  N   ASP H 413      53.867  54.895  57.836  1.00 37.43           N  
-ATOM  30583  CA  ASP H 413      55.111  55.604  58.092  1.00 35.42           C  
-ATOM  30584  C   ASP H 413      55.266  56.787  57.141  1.00 39.24           C  
-ATOM  30585  O   ASP H 413      55.807  57.825  57.518  1.00 36.53           O  
-ATOM  30586  CB  ASP H 413      56.305  54.655  57.971  1.00 42.65           C  
-ATOM  30587  CG  ASP H 413      56.356  53.644  59.098  1.00 41.38           C  
-ATOM  30588  OD1 ASP H 413      55.713  53.889  60.140  1.00 35.21           O  
-ATOM  30589  OD2 ASP H 413      57.039  52.610  58.943  1.00 46.05           O  
-ATOM  30590  N   SER H 414      54.788  56.626  55.911  1.00 44.94           N  
-ATOM  30591  CA  SER H 414      54.823  57.709  54.935  1.00 42.45           C  
-ATOM  30592  C   SER H 414      53.911  58.848  55.381  1.00 51.23           C  
-ATOM  30593  O   SER H 414      54.151  60.012  55.059  1.00 52.36           O  
-ATOM  30594  CB  SER H 414      54.418  57.209  53.544  1.00 36.41           C  
-ATOM  30595  OG  SER H 414      53.035  56.911  53.474  1.00 45.29           O  
-ATOM  30596  N   ARG H 415      52.867  58.503  56.130  1.00 46.08           N  
-ATOM  30597  CA  ARG H 415      51.951  59.498  56.676  1.00 41.79           C  
-ATOM  30598  C   ARG H 415      52.405  60.008  58.043  1.00 41.08           C  
-ATOM  30599  O   ARG H 415      51.611  60.582  58.790  1.00 45.97           O  
-ATOM  30600  CB  ARG H 415      50.540  58.916  56.776  1.00 35.67           C  
-ATOM  30601  CG  ARG H 415      49.744  58.991  55.484  1.00 41.94           C  
-ATOM  30602  CD  ARG H 415      49.292  60.417  55.190  1.00 45.80           C  
-ATOM  30603  NE  ARG H 415      48.131  60.804  55.988  1.00 43.46           N  
-ATOM  30604  CZ  ARG H 415      47.613  62.029  56.011  1.00 46.25           C  
-ATOM  30605  NH1 ARG H 415      46.555  62.290  56.765  1.00 39.35           N  
-ATOM  30606  NH2 ARG H 415      48.156  62.997  55.285  1.00 48.89           N  
-ATOM  30607  N   ASN H 416      53.683  59.800  58.355  1.00 38.94           N  
-ATOM  30608  CA  ASN H 416      54.260  60.198  59.639  1.00 43.91           C  
-ATOM  30609  C   ASN H 416      53.493  59.634  60.833  1.00 35.33           C  
-ATOM  30610  O   ASN H 416      53.245  60.339  61.809  1.00 33.22           O  
-ATOM  30611  CB  ASN H 416      54.331  61.725  59.745  1.00 41.14           C  
-ATOM  30612  CG  ASN H 416      55.378  62.325  58.830  1.00 38.02           C  
-ATOM  30613  OD1 ASN H 416      55.054  63.021  57.869  1.00 47.13           O  
-ATOM  30614  ND2 ASN H 416      56.644  62.064  59.129  1.00 37.22           N  
-ATOM  30615  N   LEU H 417      53.117  58.362  60.745  1.00 34.42           N  
-ATOM  30616  CA  LEU H 417      52.370  57.707  61.816  1.00 33.41           C  
-ATOM  30617  C   LEU H 417      52.983  56.366  62.211  1.00 36.97           C  
-ATOM  30618  O   LEU H 417      52.354  55.322  62.033  1.00 34.64           O  
-ATOM  30619  CB  LEU H 417      50.914  57.494  61.394  1.00 35.52           C  
-ATOM  30620  CG  LEU H 417      50.046  58.725  61.133  1.00 35.20           C  
-ATOM  30621  CD1 LEU H 417      48.794  58.337  60.360  1.00 20.91           C  
-ATOM  30622  CD2 LEU H 417      49.679  59.404  62.443  1.00 34.39           C  
-ATOM  30623  N   PRO H 418      54.209  56.386  62.760  1.00 35.05           N  
-ATOM  30624  CA  PRO H 418      54.861  55.124  63.123  1.00 35.03           C  
-ATOM  30625  C   PRO H 418      54.191  54.436  64.310  1.00 30.10           C  
-ATOM  30626  O   PRO H 418      54.379  53.239  64.506  1.00 29.99           O  
-ATOM  30627  CB  PRO H 418      56.284  55.561  63.477  1.00 28.87           C  
-ATOM  30628  CG  PRO H 418      56.129  56.954  63.955  1.00 23.26           C  
-ATOM  30629  CD  PRO H 418      55.040  57.552  63.108  1.00 30.50           C  
-ATOM  30630  N   HIS H 419      53.411  55.188  65.079  1.00 32.35           N  
-ATOM  30631  CA  HIS H 419      52.790  54.668  66.292  1.00 35.94           C  
-ATOM  30632  C   HIS H 419      51.442  54.003  66.023  1.00 41.60           C  
-ATOM  30633  O   HIS H 419      50.727  53.637  66.958  1.00 37.28           O  
-ATOM  30634  CB  HIS H 419      52.617  55.792  67.317  1.00 39.14           C  
-ATOM  30635  CG  HIS H 419      51.915  56.999  66.777  1.00 47.86           C  
-ATOM  30636  ND1 HIS H 419      52.586  58.058  66.207  1.00 40.17           N  
-ATOM  30637  CD2 HIS H 419      50.597  57.314  66.718  1.00 39.08           C  
-ATOM  30638  CE1 HIS H 419      51.716  58.974  65.820  1.00 38.18           C  
-ATOM  30639  NE2 HIS H 419      50.502  58.545  66.120  1.00 37.89           N  
-ATOM  30640  N   ARG H 420      51.101  53.846  64.747  1.00 42.04           N  
-ATOM  30641  CA  ARG H 420      49.849  53.201  64.364  1.00 41.93           C  
-ATOM  30642  C   ARG H 420      50.037  51.709  64.113  1.00 43.81           C  
-ATOM  30643  O   ARG H 420      51.005  51.298  63.470  1.00 40.59           O  
-ATOM  30644  CB  ARG H 420      49.266  53.861  63.114  1.00 29.52           C  
-ATOM  30645  CG  ARG H 420      48.612  55.208  63.360  1.00 34.10           C  
-ATOM  30646  CD  ARG H 420      47.140  55.060  63.713  1.00 28.65           C  
-ATOM  30647  NE  ARG H 420      46.473  56.357  63.797  1.00 37.10           N  
-ATOM  30648  CZ  ARG H 420      46.318  57.048  64.923  1.00 41.37           C  
-ATOM  30649  NH1 ARG H 420      45.700  58.222  64.903  1.00 37.35           N  
-ATOM  30650  NH2 ARG H 420      46.777  56.565  66.072  1.00 29.44           N  
-ATOM  30651  N   GLU H 421      49.113  50.901  64.626  1.00 40.71           N  
-ATOM  30652  CA  GLU H 421      49.078  49.480  64.300  1.00 30.74           C  
-ATOM  30653  C   GLU H 421      48.738  49.301  62.831  1.00 30.98           C  
-ATOM  30654  O   GLU H 421      48.063  50.144  62.241  1.00 35.30           O  
-ATOM  30655  CB  GLU H 421      48.050  48.737  65.152  1.00 24.77           C  
-ATOM  30656  CG  GLU H 421      48.610  48.076  66.394  1.00 33.01           C  
-ATOM  30657  CD  GLU H 421      47.679  47.013  66.945  1.00 40.84           C  
-ATOM  30658  OE1 GLU H 421      47.370  46.055  66.204  1.00 34.39           O  
-ATOM  30659  OE2 GLU H 421      47.249  47.139  68.112  1.00 43.84           O  
-ATOM  30660  N   VAL H 422      49.204  48.205  62.241  1.00 36.01           N  
-ATOM  30661  CA  VAL H 422      48.817  47.861  60.880  1.00 28.25           C  
-ATOM  30662  C   VAL H 422      47.318  47.591  60.829  1.00 27.38           C  
-ATOM  30663  O   VAL H 422      46.827  46.660  61.467  1.00 27.31           O  
-ATOM  30664  CB  VAL H 422      49.579  46.630  60.360  1.00 22.90           C  
-ATOM  30665  CG1 VAL H 422      49.014  46.186  59.020  1.00 29.05           C  
-ATOM  30666  CG2 VAL H 422      51.063  46.934  60.245  1.00 28.53           C  
-ATOM  30667  N   GLY H 423      46.595  48.419  60.082  1.00 27.81           N  
-ATOM  30668  CA  GLY H 423      45.157  48.274  59.956  1.00 30.78           C  
-ATOM  30669  C   GLY H 423      44.388  49.461  60.508  1.00 30.01           C  
-ATOM  30670  O   GLY H 423      43.230  49.678  60.158  1.00 30.20           O  
-ATOM  30671  N   ASP H 424      45.034  50.233  61.375  1.00 22.89           N  
-ATOM  30672  CA  ASP H 424      44.389  51.378  62.003  1.00 17.66           C  
-ATOM  30673  C   ASP H 424      44.336  52.570  61.050  1.00 27.57           C  
-ATOM  30674  O   ASP H 424      45.364  53.180  60.747  1.00 34.36           O  
-ATOM  30675  CB  ASP H 424      45.125  51.757  63.289  1.00 21.04           C  
-ATOM  30676  CG  ASP H 424      44.281  52.604  64.219  1.00 30.84           C  
-ATOM  30677  OD1 ASP H 424      43.362  53.299  63.736  1.00 31.14           O  
-ATOM  30678  OD2 ASP H 424      44.536  52.575  65.441  1.00 35.29           O  
-ATOM  30679  N   ILE H 425      43.133  52.907  60.589  1.00 25.08           N  
-ATOM  30680  CA  ILE H 425      42.959  54.014  59.652  1.00 30.82           C  
-ATOM  30681  C   ILE H 425      42.925  55.365  60.362  1.00 32.25           C  
-ATOM  30682  O   ILE H 425      42.764  56.407  59.724  1.00 35.54           O  
-ATOM  30683  CB  ILE H 425      41.665  53.865  58.827  1.00 24.75           C  
-ATOM  30684  CG1 ILE H 425      40.441  54.185  59.687  1.00 26.08           C  
-ATOM  30685  CG2 ILE H 425      41.564  52.469  58.239  1.00 25.93           C  
-ATOM  30686  CD1 ILE H 425      39.179  54.393  58.884  1.00 23.76           C  
-ATOM  30687  N   GLY H 426      43.079  55.344  61.682  1.00 25.43           N  
-ATOM  30688  CA  GLY H 426      43.017  56.560  62.469  1.00 26.71           C  
-ATOM  30689  C   GLY H 426      41.586  57.027  62.640  1.00 25.34           C  
-ATOM  30690  O   GLY H 426      40.653  56.288  62.338  1.00 25.63           O  
-ATOM  30691  N   PRO H 427      41.403  58.268  63.111  1.00 26.88           N  
-ATOM  30692  CA  PRO H 427      40.062  58.813  63.348  1.00 27.57           C  
-ATOM  30693  C   PRO H 427      39.357  59.240  62.061  1.00 31.31           C  
-ATOM  30694  O   PRO H 427      38.970  60.402  61.925  1.00 30.29           O  
-ATOM  30695  CB  PRO H 427      40.328  60.021  64.255  1.00 25.24           C  
-ATOM  30696  CG  PRO H 427      41.787  60.353  64.093  1.00 26.58           C  
-ATOM  30697  CD  PRO H 427      42.457  59.280  63.287  1.00 26.75           C  
-ATOM  30698  N   GLY H 428      39.186  58.298  61.136  1.00 23.04           N  
-ATOM  30699  CA  GLY H 428      38.567  58.586  59.856  1.00 16.52           C  
-ATOM  30700  C   GLY H 428      37.104  58.194  59.760  1.00 26.04           C  
-ATOM  30701  O   GLY H 428      36.530  57.671  60.716  1.00 33.73           O  
-ATOM  30702  N   TYR H 429      36.528  58.458  58.586  1.00 28.07           N  
-ATOM  30703  CA  TYR H 429      35.124  58.197  58.229  1.00 26.06           C  
-ATOM  30704  C   TYR H 429      34.163  57.882  59.380  1.00 26.86           C  
-ATOM  30705  O   TYR H 429      33.607  58.787  60.005  1.00 27.07           O  
-ATOM  30706  CB  TYR H 429      35.065  57.057  57.206  1.00 25.06           C  
-ATOM  30707  CG  TYR H 429      35.647  57.411  55.850  1.00 32.92           C  
-ATOM  30708  CD1 TYR H 429      35.066  58.392  55.058  1.00 40.88           C  
-ATOM  30709  CD2 TYR H 429      36.766  56.754  55.359  1.00 45.24           C  
-ATOM  30710  CE1 TYR H 429      35.591  58.717  53.817  1.00 45.35           C  
-ATOM  30711  CE2 TYR H 429      37.299  57.069  54.119  1.00 50.25           C  
-ATOM  30712  CZ  TYR H 429      36.706  58.050  53.352  1.00 50.23           C  
-ATOM  30713  OH  TYR H 429      37.237  58.362  52.120  1.00 42.14           O  
-ATOM  30714  N   GLY H 430      33.969  56.595  59.649  1.00 29.64           N  
-ATOM  30715  CA  GLY H 430      33.030  56.150  60.666  1.00 31.19           C  
-ATOM  30716  C   GLY H 430      33.222  56.762  62.042  1.00 30.28           C  
-ATOM  30717  O   GLY H 430      32.251  57.129  62.712  1.00 34.37           O  
-ATOM  30718  N   PHE H 431      34.476  56.866  62.468  1.00 23.17           N  
-ATOM  30719  CA  PHE H 431      34.783  57.443  63.768  1.00 28.25           C  
-ATOM  30720  C   PHE H 431      34.317  58.887  63.860  1.00 32.30           C  
-ATOM  30721  O   PHE H 431      33.932  59.347  64.934  1.00 30.77           O  
-ATOM  30722  CB  PHE H 431      36.278  57.376  64.071  1.00 24.37           C  
-ATOM  30723  CG  PHE H 431      36.655  58.057  65.356  1.00 22.80           C  
-ATOM  30724  CD1 PHE H 431      36.494  57.412  66.569  1.00 24.62           C  
-ATOM  30725  CD2 PHE H 431      37.139  59.353  65.355  1.00 22.30           C  
-ATOM  30726  CE1 PHE H 431      36.826  58.039  67.755  1.00 25.88           C  
-ATOM  30727  CE2 PHE H 431      37.475  59.986  66.538  1.00 23.60           C  
-ATOM  30728  CZ  PHE H 431      37.318  59.328  67.739  1.00 20.09           C  
-ATOM  30729  N   GLN H 432      34.373  59.606  62.744  1.00 28.86           N  
-ATOM  30730  CA  GLN H 432      33.876  60.972  62.721  1.00 26.71           C  
-ATOM  30731  C   GLN H 432      32.353  60.945  62.714  1.00 23.33           C  
-ATOM  30732  O   GLN H 432      31.714  61.692  63.450  1.00 27.64           O  
-ATOM  30733  CB  GLN H 432      34.438  61.734  61.515  1.00 30.25           C  
-ATOM  30734  CG  GLN H 432      35.939  62.000  61.617  1.00 28.31           C  
-ATOM  30735  CD  GLN H 432      36.300  62.830  62.844  1.00 32.64           C  
-ATOM  30736  OE1 GLN H 432      35.567  63.741  63.227  1.00 33.30           O  
-ATOM  30737  NE2 GLN H 432      37.434  62.516  63.463  1.00 34.65           N  
-ATOM  30738  N   TRP H 433      31.796  60.059  61.889  1.00 22.07           N  
-ATOM  30739  CA  TRP H 433      30.353  59.832  61.788  1.00 22.21           C  
-ATOM  30740  C   TRP H 433      29.682  59.690  63.147  1.00 23.27           C  
-ATOM  30741  O   TRP H 433      28.705  60.377  63.443  1.00 25.60           O  
-ATOM  30742  CB  TRP H 433      30.055  58.562  60.981  1.00 24.36           C  
-ATOM  30743  CG  TRP H 433      30.118  58.694  59.495  1.00 29.15           C  
-ATOM  30744  CD1 TRP H 433      30.726  59.682  58.779  1.00 31.53           C  
-ATOM  30745  CD2 TRP H 433      29.542  57.802  58.538  1.00 27.23           C  
-ATOM  30746  NE1 TRP H 433      30.570  59.459  57.434  1.00 30.84           N  
-ATOM  30747  CE2 TRP H 433      29.845  58.310  57.260  1.00 27.66           C  
-ATOM  30748  CE3 TRP H 433      28.801  56.622  58.638  1.00 24.89           C  
-ATOM  30749  CZ2 TRP H 433      29.430  57.678  56.091  1.00 28.42           C  
-ATOM  30750  CZ3 TRP H 433      28.391  55.999  57.481  1.00 30.49           C  
-ATOM  30751  CH2 TRP H 433      28.705  56.525  56.224  1.00 28.38           C  
-ATOM  30752  N   ARG H 434      30.216  58.792  63.969  1.00 23.48           N  
-ATOM  30753  CA  ARG H 434      29.572  58.439  65.226  1.00 23.77           C  
-ATOM  30754  C   ARG H 434      30.144  59.200  66.420  1.00 27.10           C  
-ATOM  30755  O   ARG H 434      29.460  59.383  67.428  1.00 27.65           O  
-ATOM  30756  CB  ARG H 434      29.684  56.929  65.463  1.00 23.82           C  
-ATOM  30757  CG  ARG H 434      29.234  56.068  64.286  1.00 20.64           C  
-ATOM  30758  CD  ARG H 434      27.866  56.488  63.767  1.00 18.43           C  
-ATOM  30759  NE  ARG H 434      26.848  56.442  64.812  1.00 29.00           N  
-ATOM  30760  CZ  ARG H 434      25.991  55.440  64.983  1.00 25.14           C  
-ATOM  30761  NH1 ARG H 434      25.099  55.491  65.962  1.00 18.86           N  
-ATOM  30762  NH2 ARG H 434      26.019  54.389  64.176  1.00 26.14           N  
-ATOM  30763  N   HIS H 435      31.397  59.633  66.310  1.00 28.22           N  
-ATOM  30764  CA  HIS H 435      32.050  60.332  67.410  1.00 31.27           C  
-ATOM  30765  C   HIS H 435      32.867  61.524  66.934  1.00 23.08           C  
-ATOM  30766  O   HIS H 435      34.055  61.601  67.219  1.00 26.97           O  
-ATOM  30767  CB  HIS H 435      32.967  59.383  68.185  1.00 31.30           C  
-ATOM  30768  CG  HIS H 435      32.396  58.014  68.384  1.00 33.71           C  
-ATOM  30769  ND1 HIS H 435      31.303  57.774  69.188  1.00 33.94           N  
-ATOM  30770  CD2 HIS H 435      32.763  56.813  67.878  1.00 28.54           C  
-ATOM  30771  CE1 HIS H 435      31.022  56.484  69.169  1.00 42.99           C  
-ATOM  30772  NE2 HIS H 435      31.892  55.877  68.383  1.00 32.81           N  
-ATOM  30773  N   PHE H 436      32.236  62.451  66.221  1.00 23.51           N  
-ATOM  30774  CA  PHE H 436      32.927  63.647  65.739  1.00 23.22           C  
-ATOM  30775  C   PHE H 436      33.587  64.445  66.867  1.00 21.59           C  
-ATOM  30776  O   PHE H 436      32.980  64.705  67.904  1.00 21.21           O  
-ATOM  30777  CB  PHE H 436      31.959  64.558  64.983  1.00 20.98           C  
-ATOM  30778  CG  PHE H 436      32.636  65.678  64.240  1.00 21.77           C  
-ATOM  30779  CD1 PHE H 436      32.917  66.881  64.869  1.00 19.39           C  
-ATOM  30780  CD2 PHE H 436      32.993  65.526  62.910  1.00 23.66           C  
-ATOM  30781  CE1 PHE H 436      33.547  67.907  64.186  1.00 25.93           C  
-ATOM  30782  CE2 PHE H 436      33.619  66.549  62.224  1.00 23.83           C  
-ATOM  30783  CZ  PHE H 436      33.895  67.740  62.861  1.00 23.22           C  
-ATOM  30784  N   GLY H 437      34.839  64.834  66.649  1.00 27.36           N  
-ATOM  30785  CA  GLY H 437      35.550  65.703  67.569  1.00 25.24           C  
-ATOM  30786  C   GLY H 437      36.149  65.012  68.778  1.00 24.66           C  
-ATOM  30787  O   GLY H 437      36.766  65.660  69.625  1.00 26.05           O  
-ATOM  30788  N   ALA H 438      35.972  63.698  68.864  1.00 25.34           N  
-ATOM  30789  CA  ALA H 438      36.485  62.933  69.992  1.00 19.31           C  
-ATOM  30790  C   ALA H 438      37.990  62.739  69.872  1.00 19.75           C  
-ATOM  30791  O   ALA H 438      38.536  62.730  68.769  1.00 20.08           O  
-ATOM  30792  CB  ALA H 438      35.778  61.589  70.089  1.00 18.74           C  
-ATOM  30793  N   ALA H 439      38.656  62.595  71.014  1.00 20.99           N  
-ATOM  30794  CA  ALA H 439      40.090  62.338  71.042  1.00 21.68           C  
-ATOM  30795  C   ALA H 439      40.367  60.877  70.707  1.00 29.40           C  
-ATOM  30796  O   ALA H 439      39.913  59.976  71.413  1.00 26.37           O  
-ATOM  30797  CB  ALA H 439      40.669  62.696  72.401  1.00 34.39           C  
-ATOM  30798  N   TYR H 440      41.110  60.647  69.629  1.00 31.97           N  
-ATOM  30799  CA  TYR H 440      41.370  59.291  69.155  1.00 24.87           C  
-ATOM  30800  C   TYR H 440      42.611  58.678  69.801  1.00 27.39           C  
-ATOM  30801  O   TYR H 440      43.640  59.339  69.947  1.00 26.62           O  
-ATOM  30802  CB  TYR H 440      41.518  59.280  67.631  1.00 23.60           C  
-ATOM  30803  CG  TYR H 440      41.575  57.891  67.034  1.00 26.07           C  
-ATOM  30804  CD1 TYR H 440      40.421  57.136  66.875  1.00 30.46           C  
-ATOM  30805  CD2 TYR H 440      42.780  57.335  66.628  1.00 29.68           C  
-ATOM  30806  CE1 TYR H 440      40.465  55.866  66.331  1.00 26.55           C  
-ATOM  30807  CE2 TYR H 440      42.835  56.065  66.082  1.00 27.44           C  
-ATOM  30808  CZ  TYR H 440      41.675  55.337  65.937  1.00 26.82           C  
-ATOM  30809  OH  TYR H 440      41.723  54.074  65.395  1.00 27.74           O  
-ATOM  30810  N   LYS H 441      42.502  57.410  70.184  1.00 28.96           N  
-ATOM  30811  CA  LYS H 441      43.622  56.674  70.760  1.00 22.70           C  
-ATOM  30812  C   LYS H 441      44.126  55.622  69.780  1.00 27.52           C  
-ATOM  30813  O   LYS H 441      45.151  55.812  69.123  1.00 33.27           O  
-ATOM  30814  CB  LYS H 441      43.219  56.019  72.084  1.00 31.39           C  
-ATOM  30815  CG  LYS H 441      43.424  56.898  73.317  1.00 51.57           C  
-ATOM  30816  CD  LYS H 441      42.468  58.082  73.346  1.00 51.34           C  
-ATOM  30817  CE  LYS H 441      42.767  59.009  74.516  1.00 48.13           C  
-ATOM  30818  NZ  LYS H 441      42.661  58.308  75.828  1.00 62.06           N  
-ATOM  30819  N   ASP H 442      43.403  54.510  69.687  1.00 30.78           N  
-ATOM  30820  CA  ASP H 442      43.701  53.486  68.690  1.00 34.85           C  
-ATOM  30821  C   ASP H 442      42.427  52.772  68.245  1.00 33.06           C  
-ATOM  30822  O   ASP H 442      41.325  53.134  68.657  1.00 30.65           O  
-ATOM  30823  CB  ASP H 442      44.721  52.474  69.225  1.00 28.72           C  
-ATOM  30824  CG  ASP H 442      44.283  51.823  70.525  1.00 31.51           C  
-ATOM  30825  OD1 ASP H 442      43.153  52.086  70.984  1.00 32.56           O  
-ATOM  30826  OD2 ASP H 442      45.074  51.036  71.086  1.00 40.40           O  
-ATOM  30827  N   MET H 443      42.586  51.750  67.411  1.00 31.60           N  
-ATOM  30828  CA  MET H 443      41.446  51.051  66.829  1.00 30.30           C  
-ATOM  30829  C   MET H 443      40.835  50.029  67.782  1.00 30.60           C  
-ATOM  30830  O   MET H 443      39.921  49.295  67.407  1.00 39.89           O  
-ATOM  30831  CB  MET H 443      41.861  50.356  65.533  1.00 29.94           C  
-ATOM  30832  CG  MET H 443      42.923  49.291  65.726  1.00 26.47           C  
-ATOM  30833  SD  MET H 443      43.457  48.554  64.174  1.00 37.01           S  
-ATOM  30834  CE  MET H 443      44.653  47.358  64.763  1.00 33.06           C  
-ATOM  30835  N   HIS H 444      41.341  49.978  69.009  1.00 25.63           N  
-ATOM  30836  CA  HIS H 444      40.841  49.023  69.989  1.00 32.69           C  
-ATOM  30837  C   HIS H 444      40.073  49.724  71.107  1.00 35.26           C  
-ATOM  30838  O   HIS H 444      39.393  49.079  71.905  1.00 34.97           O  
-ATOM  30839  CB  HIS H 444      41.993  48.204  70.577  1.00 34.85           C  
-ATOM  30840  CG  HIS H 444      42.753  47.411  69.560  1.00 35.45           C  
-ATOM  30841  ND1 HIS H 444      42.157  46.462  68.758  1.00 33.43           N  
-ATOM  30842  CD2 HIS H 444      44.064  47.421  69.219  1.00 31.28           C  
-ATOM  30843  CE1 HIS H 444      43.066  45.925  67.963  1.00 37.48           C  
-ATOM  30844  NE2 HIS H 444      44.232  46.491  68.223  1.00 30.16           N  
-ATOM  30845  N   THR H 445      40.180  51.047  71.153  1.00 32.33           N  
-ATOM  30846  CA  THR H 445      39.583  51.824  72.232  1.00 30.87           C  
-ATOM  30847  C   THR H 445      38.078  51.988  72.049  1.00 29.97           C  
-ATOM  30848  O   THR H 445      37.597  52.221  70.942  1.00 38.17           O  
-ATOM  30849  CB  THR H 445      40.233  53.218  72.341  1.00 32.67           C  
-ATOM  30850  OG1 THR H 445      41.659  53.081  72.364  1.00 33.27           O  
-ATOM  30851  CG2 THR H 445      39.776  53.928  73.608  1.00 40.10           C  
-ATOM  30852  N   ASP H 446      37.341  51.861  73.147  1.00 33.89           N  
-ATOM  30853  CA  ASP H 446      35.896  52.052  73.143  1.00 37.61           C  
-ATOM  30854  C   ASP H 446      35.551  53.538  73.247  1.00 39.98           C  
-ATOM  30855  O   ASP H 446      35.837  54.178  74.258  1.00 46.44           O  
-ATOM  30856  CB  ASP H 446      35.258  51.273  74.294  1.00 40.55           C  
-ATOM  30857  CG  ASP H 446      33.746  51.297  74.250  1.00 47.23           C  
-ATOM  30858  OD1 ASP H 446      33.181  51.413  73.142  1.00 56.68           O  
-ATOM  30859  OD2 ASP H 446      33.122  51.190  75.327  1.00 42.42           O  
-ATOM  30860  N   TYR H 447      34.938  54.085  72.201  1.00 39.49           N  
-ATOM  30861  CA  TYR H 447      34.654  55.517  72.152  1.00 32.72           C  
-ATOM  30862  C   TYR H 447      33.183  55.852  72.375  1.00 35.50           C  
-ATOM  30863  O   TYR H 447      32.753  56.966  72.074  1.00 33.42           O  
-ATOM  30864  CB  TYR H 447      35.092  56.102  70.807  1.00 27.25           C  
-ATOM  30865  CG  TYR H 447      36.563  55.953  70.510  1.00 25.57           C  
-ATOM  30866  CD1 TYR H 447      37.504  56.749  71.148  1.00 28.04           C  
-ATOM  30867  CD2 TYR H 447      37.012  55.027  69.579  1.00 28.65           C  
-ATOM  30868  CE1 TYR H 447      38.853  56.618  70.876  1.00 30.40           C  
-ATOM  30869  CE2 TYR H 447      38.358  54.890  69.300  1.00 35.09           C  
-ATOM  30870  CZ  TYR H 447      39.274  55.687  69.950  1.00 30.98           C  
-ATOM  30871  OH  TYR H 447      40.616  55.549  69.672  1.00 32.39           O  
-ATOM  30872  N   THR H 448      32.411  54.903  72.897  1.00 40.59           N  
-ATOM  30873  CA  THR H 448      30.973  55.115  73.043  1.00 45.58           C  
-ATOM  30874  C   THR H 448      30.669  56.235  74.041  1.00 38.26           C  
-ATOM  30875  O   THR H 448      31.270  56.313  75.114  1.00 39.03           O  
-ATOM  30876  CB  THR H 448      30.243  53.821  73.472  1.00 33.74           C  
-ATOM  30877  OG1 THR H 448      28.852  54.103  73.666  1.00 32.21           O  
-ATOM  30878  CG2 THR H 448      30.826  53.261  74.758  1.00 36.03           C  
-ATOM  30879  N   GLY H 449      29.748  57.116  73.662  1.00 32.55           N  
-ATOM  30880  CA  GLY H 449      29.388  58.253  74.488  1.00 33.16           C  
-ATOM  30881  C   GLY H 449      30.145  59.518  74.126  1.00 34.37           C  
-ATOM  30882  O   GLY H 449      29.648  60.629  74.314  1.00 32.83           O  
-ATOM  30883  N   GLN H 450      31.353  59.351  73.598  1.00 36.61           N  
-ATOM  30884  CA  GLN H 450      32.204  60.487  73.260  1.00 35.60           C  
-ATOM  30885  C   GLN H 450      31.861  61.086  71.895  1.00 41.78           C  
-ATOM  30886  O   GLN H 450      31.422  60.378  70.985  1.00 41.85           O  
-ATOM  30887  CB  GLN H 450      33.675  60.072  73.283  1.00 29.28           C  
-ATOM  30888  CG  GLN H 450      34.110  59.384  74.565  1.00 33.52           C  
-ATOM  30889  CD  GLN H 450      35.546  58.904  74.506  1.00 45.21           C  
-ATOM  30890  OE1 GLN H 450      36.446  59.647  74.112  1.00 41.84           O  
-ATOM  30891  NE2 GLN H 450      35.767  57.652  74.888  1.00 47.45           N  
-ATOM  30892  N   GLY H 451      32.063  62.394  71.763  1.00 36.31           N  
-ATOM  30893  CA  GLY H 451      31.863  63.083  70.501  1.00 24.50           C  
-ATOM  30894  C   GLY H 451      30.408  63.241  70.110  1.00 27.02           C  
-ATOM  30895  O   GLY H 451      29.507  62.904  70.877  1.00 27.95           O  
-ATOM  30896  N   VAL H 452      30.183  63.758  68.905  1.00 28.25           N  
-ATOM  30897  CA  VAL H 452      28.834  63.958  68.384  1.00 21.28           C  
-ATOM  30898  C   VAL H 452      28.411  62.775  67.521  1.00 23.46           C  
-ATOM  30899  O   VAL H 452      29.162  62.335  66.651  1.00 22.88           O  
-ATOM  30900  CB  VAL H 452      28.735  65.252  67.554  1.00 13.49           C  
-ATOM  30901  CG1 VAL H 452      27.338  65.413  66.972  1.00 14.95           C  
-ATOM  30902  CG2 VAL H 452      29.104  66.455  68.406  1.00 13.00           C  
-ATOM  30903  N   ASP H 453      27.211  62.258  67.765  1.00 21.81           N  
-ATOM  30904  CA  ASP H 453      26.680  61.169  66.953  1.00 20.54           C  
-ATOM  30905  C   ASP H 453      25.850  61.717  65.795  1.00 27.75           C  
-ATOM  30906  O   ASP H 453      24.618  61.740  65.845  1.00 31.06           O  
-ATOM  30907  CB  ASP H 453      25.847  60.213  67.804  1.00 27.62           C  
-ATOM  30908  CG  ASP H 453      25.654  58.864  67.140  1.00 32.15           C  
-ATOM  30909  OD1 ASP H 453      25.802  58.779  65.901  1.00 29.68           O  
-ATOM  30910  OD2 ASP H 453      25.349  57.888  67.856  1.00 29.47           O  
-ATOM  30911  N   GLN H 454      26.547  62.144  64.748  1.00 24.87           N  
-ATOM  30912  CA  GLN H 454      25.922  62.778  63.595  1.00 19.63           C  
-ATOM  30913  C   GLN H 454      24.858  61.904  62.952  1.00 25.33           C  
-ATOM  30914  O   GLN H 454      23.821  62.408  62.528  1.00 28.16           O  
-ATOM  30915  CB  GLN H 454      26.972  63.138  62.550  1.00 16.90           C  
-ATOM  30916  CG  GLN H 454      27.983  64.159  63.024  1.00 16.93           C  
-ATOM  30917  CD  GLN H 454      28.909  64.607  61.917  1.00 20.39           C  
-ATOM  30918  OE1 GLN H 454      28.619  65.563  61.199  1.00 24.10           O  
-ATOM  30919  NE2 GLN H 454      30.034  63.918  61.772  1.00 25.14           N  
-ATOM  30920  N   LEU H 455      25.113  60.602  62.873  1.00 24.63           N  
-ATOM  30921  CA  LEU H 455      24.161  59.685  62.256  1.00 25.96           C  
-ATOM  30922  C   LEU H 455      22.860  59.641  63.051  1.00 23.58           C  
-ATOM  30923  O   LEU H 455      21.764  59.770  62.492  1.00 18.30           O  
-ATOM  30924  CB  LEU H 455      24.776  58.287  62.137  1.00 18.83           C  
-ATOM  30925  CG  LEU H 455      24.024  57.253  61.297  1.00 18.19           C  
-ATOM  30926  CD1 LEU H 455      23.755  57.776  59.900  1.00 17.40           C  
-ATOM  30927  CD2 LEU H 455      24.811  55.959  61.227  1.00 19.85           C  
-ATOM  30928  N   LYS H 456      22.995  59.469  64.362  1.00 26.78           N  
-ATOM  30929  CA  LYS H 456      21.838  59.403  65.246  1.00 29.29           C  
-ATOM  30930  C   LYS H 456      21.062  60.709  65.229  1.00 25.56           C  
-ATOM  30931  O   LYS H 456      19.837  60.703  65.250  1.00 20.03           O  
-ATOM  30932  CB  LYS H 456      22.254  59.069  66.683  1.00 30.27           C  
-ATOM  30933  CG  LYS H 456      21.078  58.711  67.581  1.00 37.87           C  
-ATOM  30934  CD  LYS H 456      21.515  58.481  69.018  1.00 42.21           C  
-ATOM  30935  CE  LYS H 456      21.191  59.680  69.896  1.00 52.92           C  
-ATOM  30936  NZ  LYS H 456      21.903  60.910  69.449  1.00 61.37           N  
-ATOM  30937  N   ASN H 457      21.782  61.825  65.195  1.00 22.45           N  
-ATOM  30938  CA  ASN H 457      21.144  63.134  65.135  1.00 25.79           C  
-ATOM  30939  C   ASN H 457      20.375  63.329  63.828  1.00 32.15           C  
-ATOM  30940  O   ASN H 457      19.248  63.831  63.829  1.00 30.78           O  
-ATOM  30941  CB  ASN H 457      22.185  64.247  65.308  1.00 23.57           C  
-ATOM  30942  CG  ASN H 457      22.912  64.165  66.634  1.00 26.16           C  
-ATOM  30943  OD1 ASN H 457      22.519  63.413  67.525  1.00 25.08           O  
-ATOM  30944  ND2 ASN H 457      23.980  64.946  66.772  1.00 25.98           N  
-ATOM  30945  N   VAL H 458      20.990  62.927  62.720  1.00 27.87           N  
-ATOM  30946  CA  VAL H 458      20.364  63.023  61.408  1.00 23.18           C  
-ATOM  30947  C   VAL H 458      19.091  62.193  61.354  1.00 20.82           C  
-ATOM  30948  O   VAL H 458      18.051  62.668  60.904  1.00 25.48           O  
-ATOM  30949  CB  VAL H 458      21.322  62.566  60.289  1.00 17.63           C  
-ATOM  30950  CG1 VAL H 458      20.545  62.191  59.039  1.00 17.96           C  
-ATOM  30951  CG2 VAL H 458      22.333  63.658  59.980  1.00 15.79           C  
-ATOM  30952  N   ILE H 459      19.175  60.954  61.825  1.00 23.43           N  
-ATOM  30953  CA  ILE H 459      18.004  60.087  61.866  1.00 22.31           C  
-ATOM  30954  C   ILE H 459      16.911  60.671  62.759  1.00 23.74           C  
-ATOM  30955  O   ILE H 459      15.736  60.683  62.383  1.00 22.82           O  
-ATOM  30956  CB  ILE H 459      18.366  58.679  62.358  1.00 16.38           C  
-ATOM  30957  CG1 ILE H 459      19.269  57.991  61.339  1.00 15.02           C  
-ATOM  30958  CG2 ILE H 459      17.109  57.859  62.594  1.00 12.88           C  
-ATOM  30959  CD1 ILE H 459      19.609  56.573  61.701  1.00 25.16           C  
-ATOM  30960  N   GLN H 460      17.305  61.168  63.930  1.00 20.70           N  
-ATOM  30961  CA  GLN H 460      16.361  61.757  64.876  1.00 25.18           C  
-ATOM  30962  C   GLN H 460      15.609  62.931  64.268  1.00 26.23           C  
-ATOM  30963  O   GLN H 460      14.385  63.009  64.360  1.00 24.11           O  
-ATOM  30964  CB  GLN H 460      17.086  62.207  66.148  1.00 40.26           C  
-ATOM  30965  CG  GLN H 460      16.222  63.018  67.108  1.00 44.06           C  
-ATOM  30966  CD  GLN H 460      15.228  62.168  67.882  1.00 45.37           C  
-ATOM  30967  OE1 GLN H 460      15.092  60.965  67.641  1.00 34.95           O  
-ATOM  30968  NE2 GLN H 460      14.530  62.792  68.824  1.00 38.73           N  
-ATOM  30969  N   MET H 461      16.350  63.841  63.647  1.00 30.79           N  
-ATOM  30970  CA  MET H 461      15.750  65.003  63.004  1.00 27.02           C  
-ATOM  30971  C   MET H 461      14.891  64.580  61.816  1.00 22.06           C  
-ATOM  30972  O   MET H 461      13.902  65.229  61.502  1.00 25.33           O  
-ATOM  30973  CB  MET H 461      16.831  65.997  62.557  1.00 34.76           C  
-ATOM  30974  CG  MET H 461      16.284  67.309  62.000  1.00 45.05           C  
-ATOM  30975  SD  MET H 461      15.337  68.271  63.202  1.00 44.80           S  
-ATOM  30976  CE  MET H 461      16.638  68.796  64.320  1.00 33.25           C  
-ATOM  30977  N   LEU H 462      15.268  63.490  61.157  1.00 23.07           N  
-ATOM  30978  CA  LEU H 462      14.462  62.966  60.060  1.00 17.71           C  
-ATOM  30979  C   LEU H 462      13.122  62.447  60.559  1.00 22.10           C  
-ATOM  30980  O   LEU H 462      12.094  62.630  59.906  1.00 25.04           O  
-ATOM  30981  CB  LEU H 462      15.205  61.850  59.323  1.00 15.56           C  
-ATOM  30982  CG  LEU H 462      16.218  62.273  58.259  1.00 19.69           C  
-ATOM  30983  CD1 LEU H 462      16.997  61.074  57.758  1.00 21.61           C  
-ATOM  30984  CD2 LEU H 462      15.529  62.970  57.107  1.00 15.64           C  
-ATOM  30985  N   ARG H 463      13.137  61.800  61.721  1.00 21.98           N  
-ATOM  30986  CA  ARG H 463      11.935  61.169  62.254  1.00 22.14           C  
-ATOM  30987  C   ARG H 463      11.029  62.142  63.007  1.00 22.26           C  
-ATOM  30988  O   ARG H 463       9.821  61.925  63.098  1.00 19.87           O  
-ATOM  30989  CB  ARG H 463      12.316  59.998  63.166  1.00 17.55           C  
-ATOM  30990  CG  ARG H 463      13.017  58.867  62.430  1.00 18.26           C  
-ATOM  30991  CD  ARG H 463      12.865  57.526  63.132  1.00 18.69           C  
-ATOM  30992  NE  ARG H 463      13.846  57.327  64.195  1.00 20.87           N  
-ATOM  30993  CZ  ARG H 463      14.432  56.162  64.458  1.00 24.34           C  
-ATOM  30994  NH1 ARG H 463      14.143  55.090  63.731  1.00 11.25           N  
-ATOM  30995  NH2 ARG H 463      15.310  56.067  65.446  1.00 30.08           N  
-ATOM  30996  N   THR H 464      11.606  63.215  63.539  1.00 22.82           N  
-ATOM  30997  CA  THR H 464      10.831  64.165  64.329  1.00 17.45           C  
-ATOM  30998  C   THR H 464      10.438  65.411  63.542  1.00 18.89           C  
-ATOM  30999  O   THR H 464       9.347  65.949  63.728  1.00 25.83           O  
-ATOM  31000  CB  THR H 464      11.600  64.607  65.589  1.00 21.02           C  
-ATOM  31001  OG1 THR H 464      12.794  65.300  65.208  1.00 27.57           O  
-ATOM  31002  CG2 THR H 464      11.964  63.402  66.448  1.00 23.69           C  
-ATOM  31003  N   ASN H 465      11.325  65.865  62.663  1.00 24.38           N  
-ATOM  31004  CA  ASN H 465      11.142  67.141  61.978  1.00 27.35           C  
-ATOM  31005  C   ASN H 465      11.890  67.203  60.645  1.00 25.65           C  
-ATOM  31006  O   ASN H 465      12.966  67.794  60.557  1.00 29.00           O  
-ATOM  31007  CB  ASN H 465      11.603  68.276  62.892  1.00 23.19           C  
-ATOM  31008  CG  ASN H 465      11.305  69.641  62.323  1.00 30.00           C  
-ATOM  31009  OD1 ASN H 465      10.266  69.854  61.702  1.00 36.67           O  
-ATOM  31010  ND2 ASN H 465      12.224  70.577  62.524  1.00 39.54           N  
-ATOM  31011  N   PRO H 466      11.315  66.595  59.596  1.00 24.20           N  
-ATOM  31012  CA  PRO H 466      12.010  66.395  58.318  1.00 33.29           C  
-ATOM  31013  C   PRO H 466      12.180  67.654  57.466  1.00 30.38           C  
-ATOM  31014  O   PRO H 466      12.833  67.587  56.423  1.00 33.71           O  
-ATOM  31015  CB  PRO H 466      11.112  65.386  57.595  1.00 27.67           C  
-ATOM  31016  CG  PRO H 466       9.754  65.677  58.117  1.00 33.32           C  
-ATOM  31017  CD  PRO H 466       9.947  66.048  59.566  1.00 33.03           C  
-ATOM  31018  N   THR H 467      11.608  68.776  57.888  1.00 24.41           N  
-ATOM  31019  CA  THR H 467      11.716  70.006  57.108  1.00 34.77           C  
-ATOM  31020  C   THR H 467      12.971  70.794  57.473  1.00 36.57           C  
-ATOM  31021  O   THR H 467      13.302  71.788  56.825  1.00 31.91           O  
-ATOM  31022  CB  THR H 467      10.484  70.914  57.296  1.00 41.26           C  
-ATOM  31023  OG1 THR H 467      10.327  71.235  58.684  1.00 45.17           O  
-ATOM  31024  CG2 THR H 467       9.230  70.220  56.791  1.00 38.57           C  
-ATOM  31025  N   ASP H 468      13.663  70.343  58.515  1.00 32.22           N  
-ATOM  31026  CA  ASP H 468      14.900  70.979  58.954  1.00 30.67           C  
-ATOM  31027  C   ASP H 468      15.983  70.846  57.887  1.00 37.93           C  
-ATOM  31028  O   ASP H 468      16.126  69.795  57.263  1.00 45.73           O  
-ATOM  31029  CB  ASP H 468      15.372  70.369  60.274  1.00 31.06           C  
-ATOM  31030  CG  ASP H 468      16.775  70.797  60.647  1.00 34.07           C  
-ATOM  31031  OD1 ASP H 468      16.932  71.901  61.208  1.00 42.75           O  
-ATOM  31032  OD2 ASP H 468      17.721  70.024  60.389  1.00 32.60           O  
-ATOM  31033  N   ARG H 469      16.743  71.915  57.679  1.00 47.17           N  
-ATOM  31034  CA  ARG H 469      17.745  71.939  56.619  1.00 39.66           C  
-ATOM  31035  C   ARG H 469      19.166  71.813  57.154  1.00 32.16           C  
-ATOM  31036  O   ARG H 469      20.125  72.151  56.462  1.00 32.05           O  
-ATOM  31037  CB  ARG H 469      17.614  73.224  55.798  1.00 29.90           C  
-ATOM  31038  CG  ARG H 469      16.289  73.352  55.069  1.00 28.28           C  
-ATOM  31039  CD  ARG H 469      16.155  74.706  54.395  1.00 40.62           C  
-ATOM  31040  NE  ARG H 469      16.067  75.797  55.362  1.00 52.07           N  
-ATOM  31041  CZ  ARG H 469      15.157  76.766  55.315  1.00 47.48           C  
-ATOM  31042  NH1 ARG H 469      14.252  76.783  54.345  1.00 29.04           N  
-ATOM  31043  NH2 ARG H 469      15.150  77.718  56.239  1.00 46.79           N  
-ATOM  31044  N   ARG H 470      19.299  71.330  58.385  1.00 37.78           N  
-ATOM  31045  CA  ARG H 470      20.612  71.132  58.991  1.00 34.21           C  
-ATOM  31046  C   ARG H 470      20.920  69.650  59.171  1.00 28.42           C  
-ATOM  31047  O   ARG H 470      21.666  69.269  60.074  1.00 23.81           O  
-ATOM  31048  CB  ARG H 470      20.707  71.846  60.343  1.00 26.57           C  
-ATOM  31049  CG  ARG H 470      20.662  73.365  60.278  1.00 25.19           C  
-ATOM  31050  CD  ARG H 470      19.243  73.893  60.443  1.00 32.80           C  
-ATOM  31051  NE  ARG H 470      19.214  75.342  60.629  1.00 46.05           N  
-ATOM  31052  CZ  ARG H 470      19.031  75.949  61.800  1.00 51.20           C  
-ATOM  31053  NH1 ARG H 470      18.849  75.236  62.904  1.00 47.90           N  
-ATOM  31054  NH2 ARG H 470      19.024  77.274  61.865  1.00 43.32           N  
-ATOM  31055  N   MET H 471      20.343  68.819  58.308  1.00 25.59           N  
-ATOM  31056  CA  MET H 471      20.509  67.373  58.409  1.00 25.28           C  
-ATOM  31057  C   MET H 471      21.730  66.892  57.627  1.00 22.09           C  
-ATOM  31058  O   MET H 471      21.605  66.306  56.551  1.00 20.64           O  
-ATOM  31059  CB  MET H 471      19.240  66.665  57.925  1.00 26.94           C  
-ATOM  31060  CG  MET H 471      17.988  67.085  58.690  1.00 33.19           C  
-ATOM  31061  SD  MET H 471      16.499  66.178  58.233  1.00 19.76           S  
-ATOM  31062  CE  MET H 471      16.366  66.587  56.495  1.00 26.00           C  
-ATOM  31063  N   LEU H 472      22.912  67.145  58.182  1.00 31.19           N  
-ATOM  31064  CA  LEU H 472      24.166  66.804  57.517  1.00 23.11           C  
-ATOM  31065  C   LEU H 472      25.055  65.880  58.340  1.00 19.56           C  
-ATOM  31066  O   LEU H 472      24.962  65.823  59.565  1.00 27.92           O  
-ATOM  31067  CB  LEU H 472      24.958  68.070  57.179  1.00 26.00           C  
-ATOM  31068  CG  LEU H 472      24.424  68.999  56.091  1.00 29.52           C  
-ATOM  31069  CD1 LEU H 472      23.493  70.057  56.671  1.00 24.56           C  
-ATOM  31070  CD2 LEU H 472      25.585  69.635  55.348  1.00 31.33           C  
-ATOM  31071  N   MET H 473      25.930  65.169  57.642  1.00 22.39           N  
-ATOM  31072  CA  MET H 473      26.941  64.339  58.270  1.00 23.04           C  
-ATOM  31073  C   MET H 473      28.272  64.605  57.579  1.00 23.46           C  
-ATOM  31074  O   MET H 473      28.407  64.396  56.371  1.00 28.38           O  
-ATOM  31075  CB  MET H 473      26.554  62.860  58.190  1.00 23.04           C  
-ATOM  31076  CG  MET H 473      27.384  61.944  59.072  1.00 25.68           C  
-ATOM  31077  SD  MET H 473      26.655  60.299  59.231  1.00 44.83           S  
-ATOM  31078  CE  MET H 473      26.616  59.763  57.524  1.00 21.63           C  
-ATOM  31079  N   THR H 474      29.247  65.089  58.339  1.00 14.91           N  
-ATOM  31080  CA  THR H 474      30.542  65.434  57.768  1.00 17.95           C  
-ATOM  31081  C   THR H 474      31.647  64.537  58.312  1.00 25.06           C  
-ATOM  31082  O   THR H 474      31.612  64.124  59.472  1.00 28.77           O  
-ATOM  31083  CB  THR H 474      30.907  66.907  58.040  1.00 20.84           C  
-ATOM  31084  OG1 THR H 474      32.191  67.197  57.474  1.00 23.51           O  
-ATOM  31085  CG2 THR H 474      30.943  67.188  59.533  1.00 28.50           C  
-ATOM  31086  N   ALA H 475      32.621  64.229  57.462  1.00 29.28           N  
-ATOM  31087  CA  ALA H 475      33.764  63.419  57.863  1.00 24.68           C  
-ATOM  31088  C   ALA H 475      35.030  64.265  57.878  1.00 20.19           C  
-ATOM  31089  O   ALA H 475      36.085  63.813  58.319  1.00 21.52           O  
-ATOM  31090  CB  ALA H 475      33.927  62.228  56.930  1.00 23.31           C  
-ATOM  31091  N   TRP H 476      34.916  65.497  57.396  1.00 16.06           N  
-ATOM  31092  CA  TRP H 476      36.066  66.378  57.289  1.00 16.73           C  
-ATOM  31093  C   TRP H 476      36.327  67.120  58.594  1.00 20.34           C  
-ATOM  31094  O   TRP H 476      35.649  68.096  58.914  1.00 27.49           O  
-ATOM  31095  CB  TRP H 476      35.870  67.375  56.145  1.00 19.42           C  
-ATOM  31096  CG  TRP H 476      37.143  68.038  55.725  1.00 22.33           C  
-ATOM  31097  CD1 TRP H 476      37.575  69.282  56.078  1.00 25.29           C  
-ATOM  31098  CD2 TRP H 476      38.160  67.484  54.884  1.00 24.54           C  
-ATOM  31099  NE1 TRP H 476      38.795  69.540  55.502  1.00 27.85           N  
-ATOM  31100  CE2 TRP H 476      39.178  68.448  54.763  1.00 28.01           C  
-ATOM  31101  CE3 TRP H 476      38.310  66.263  54.217  1.00 21.69           C  
-ATOM  31102  CZ2 TRP H 476      40.326  68.236  54.004  1.00 29.30           C  
-ATOM  31103  CZ3 TRP H 476      39.449  66.052  53.464  1.00 23.56           C  
-ATOM  31104  CH2 TRP H 476      40.443  67.034  53.363  1.00 23.60           C  
-ATOM  31105  N   ASN H 477      37.316  66.645  59.342  1.00 18.28           N  
-ATOM  31106  CA  ASN H 477      37.738  67.305  60.570  1.00 23.40           C  
-ATOM  31107  C   ASN H 477      39.193  67.748  60.471  1.00 27.96           C  
-ATOM  31108  O   ASN H 477      40.105  66.937  60.639  1.00 33.05           O  
-ATOM  31109  CB  ASN H 477      37.548  66.379  61.773  1.00 26.81           C  
-ATOM  31110  CG  ASN H 477      37.807  67.075  63.102  1.00 33.35           C  
-ATOM  31111  OD1 ASN H 477      38.255  68.221  63.146  1.00 32.63           O  
-ATOM  31112  ND2 ASN H 477      37.531  66.375  64.198  1.00 43.00           N  
-ATOM  31113  N   PRO H 478      39.410  69.042  60.190  1.00 24.94           N  
-ATOM  31114  CA  PRO H 478      40.734  69.667  60.103  1.00 21.97           C  
-ATOM  31115  C   PRO H 478      41.637  69.349  61.295  1.00 25.09           C  
-ATOM  31116  O   PRO H 478      42.849  69.226  61.124  1.00 28.06           O  
-ATOM  31117  CB  PRO H 478      40.405  71.161  60.057  1.00 23.48           C  
-ATOM  31118  CG  PRO H 478      39.083  71.214  59.381  1.00 29.83           C  
-ATOM  31119  CD  PRO H 478      38.335  69.983  59.827  1.00 25.17           C  
-ATOM  31120  N   ALA H 479      41.047  69.205  62.478  1.00 26.47           N  
-ATOM  31121  CA  ALA H 479      41.808  68.973  63.703  1.00 28.80           C  
-ATOM  31122  C   ALA H 479      42.284  67.527  63.842  1.00 37.47           C  
-ATOM  31123  O   ALA H 479      42.974  67.186  64.804  1.00 40.38           O  
-ATOM  31124  CB  ALA H 479      40.974  69.361  64.914  1.00 24.08           C  
-ATOM  31125  N   ALA H 480      41.916  66.678  62.888  1.00 34.15           N  
-ATOM  31126  CA  ALA H 480      42.263  65.264  62.961  1.00 31.16           C  
-ATOM  31127  C   ALA H 480      42.673  64.700  61.605  1.00 34.32           C  
-ATOM  31128  O   ALA H 480      42.789  63.487  61.444  1.00 32.91           O  
-ATOM  31129  CB  ALA H 480      41.099  64.469  63.529  1.00 34.97           C  
-ATOM  31130  N   LEU H 481      42.892  65.579  60.633  1.00 36.60           N  
-ATOM  31131  CA  LEU H 481      43.287  65.147  59.298  1.00 27.03           C  
-ATOM  31132  C   LEU H 481      44.641  64.449  59.319  1.00 30.81           C  
-ATOM  31133  O   LEU H 481      44.808  63.388  58.721  1.00 36.36           O  
-ATOM  31134  CB  LEU H 481      43.324  66.333  58.332  1.00 26.90           C  
-ATOM  31135  CG  LEU H 481      41.992  66.909  57.841  1.00 28.05           C  
-ATOM  31136  CD1 LEU H 481      42.237  68.199  57.074  1.00 41.35           C  
-ATOM  31137  CD2 LEU H 481      41.240  65.911  56.975  1.00 19.37           C  
-ATOM  31138  N   ASP H 482      45.598  65.044  60.024  1.00 27.03           N  
-ATOM  31139  CA  ASP H 482      46.963  64.527  60.071  1.00 28.91           C  
-ATOM  31140  C   ASP H 482      47.060  63.163  60.752  1.00 29.78           C  
-ATOM  31141  O   ASP H 482      48.034  62.438  60.562  1.00 32.51           O  
-ATOM  31142  CB  ASP H 482      47.881  65.524  60.786  1.00 44.09           C  
-ATOM  31143  CG  ASP H 482      48.177  66.756  59.947  1.00 45.42           C  
-ATOM  31144  OD1 ASP H 482      47.466  66.978  58.944  1.00 43.24           O  
-ATOM  31145  OD2 ASP H 482      49.118  67.503  60.293  1.00 24.43           O  
-ATOM  31146  N   GLU H 483      46.048  62.814  61.537  1.00 34.39           N  
-ATOM  31147  CA  GLU H 483      46.081  61.577  62.311  1.00 30.69           C  
-ATOM  31148  C   GLU H 483      45.494  60.394  61.552  1.00 31.00           C  
-ATOM  31149  O   GLU H 483      45.583  59.252  62.003  1.00 28.41           O  
-ATOM  31150  CB  GLU H 483      45.330  61.764  63.625  1.00 26.76           C  
-ATOM  31151  CG  GLU H 483      45.869  62.897  64.466  1.00 33.85           C  
-ATOM  31152  CD  GLU H 483      44.859  63.396  65.474  1.00 39.38           C  
-ATOM  31153  OE1 GLU H 483      44.976  64.562  65.904  1.00 45.35           O  
-ATOM  31154  OE2 GLU H 483      43.946  62.623  65.832  1.00 40.60           O  
-ATOM  31155  N   MET H 484      44.896  60.667  60.399  1.00 34.37           N  
-ATOM  31156  CA  MET H 484      44.232  59.622  59.633  1.00 32.77           C  
-ATOM  31157  C   MET H 484      45.127  59.071  58.535  1.00 30.48           C  
-ATOM  31158  O   MET H 484      45.977  59.779  57.995  1.00 36.23           O  
-ATOM  31159  CB  MET H 484      42.933  60.150  59.029  1.00 33.82           C  
-ATOM  31160  CG  MET H 484      41.982  60.746  60.047  1.00 38.24           C  
-ATOM  31161  SD  MET H 484      40.569  61.546  59.266  1.00 35.46           S  
-ATOM  31162  CE  MET H 484      41.413  62.472  57.996  1.00 40.65           C  
-ATOM  31163  N   ALA H 485      44.925  57.798  58.213  1.00 27.67           N  
-ATOM  31164  CA  ALA H 485      45.672  57.141  57.152  1.00 29.42           C  
-ATOM  31165  C   ALA H 485      45.432  57.850  55.826  1.00 38.53           C  
-ATOM  31166  O   ALA H 485      46.361  58.091  55.056  1.00 45.40           O  
-ATOM  31167  CB  ALA H 485      45.280  55.679  57.057  1.00 30.29           C  
-ATOM  31168  N   LEU H 486      44.172  58.184  55.572  1.00 38.13           N  
-ATOM  31169  CA  LEU H 486      43.798  58.944  54.388  1.00 37.50           C  
-ATOM  31170  C   LEU H 486      42.715  59.961  54.718  1.00 36.77           C  
-ATOM  31171  O   LEU H 486      41.723  59.628  55.368  1.00 39.73           O  
-ATOM  31172  CB  LEU H 486      43.313  58.015  53.272  1.00 34.20           C  
-ATOM  31173  CG  LEU H 486      44.365  57.556  52.263  1.00 39.13           C  
-ATOM  31174  CD1 LEU H 486      43.723  56.771  51.127  1.00 56.50           C  
-ATOM  31175  CD2 LEU H 486      45.134  58.751  51.726  1.00 32.83           C  
-ATOM  31176  N   PRO H 487      42.909  61.214  54.281  1.00 28.88           N  
-ATOM  31177  CA  PRO H 487      41.855  62.227  54.355  1.00 29.68           C  
-ATOM  31178  C   PRO H 487      40.626  61.770  53.581  1.00 28.84           C  
-ATOM  31179  O   PRO H 487      40.774  61.271  52.468  1.00 29.58           O  
-ATOM  31180  CB  PRO H 487      42.497  63.452  53.702  1.00 27.07           C  
-ATOM  31181  CG  PRO H 487      43.956  63.250  53.881  1.00 28.07           C  
-ATOM  31182  CD  PRO H 487      44.175  61.772  53.779  1.00 31.48           C  
-ATOM  31183  N   PRO H 488      39.428  61.939  54.159  1.00 25.98           N  
-ATOM  31184  CA  PRO H 488      38.212  61.381  53.557  1.00 32.65           C  
-ATOM  31185  C   PRO H 488      37.904  61.943  52.172  1.00 32.44           C  
-ATOM  31186  O   PRO H 488      37.989  63.152  51.956  1.00 31.02           O  
-ATOM  31187  CB  PRO H 488      37.117  61.774  54.555  1.00 27.89           C  
-ATOM  31188  CG  PRO H 488      37.649  62.975  55.236  1.00 29.26           C  
-ATOM  31189  CD  PRO H 488      39.127  62.756  55.345  1.00 25.54           C  
-ATOM  31190  N   CYS H 489      37.563  61.059  51.241  1.00 32.04           N  
-ATOM  31191  CA  CYS H 489      37.148  61.484  49.913  1.00 31.50           C  
-ATOM  31192  C   CYS H 489      35.678  61.881  49.963  1.00 29.99           C  
-ATOM  31193  O   CYS H 489      35.341  63.055  49.810  1.00 26.93           O  
-ATOM  31194  CB  CYS H 489      37.392  60.378  48.884  1.00 31.92           C  
-ATOM  31195  SG  CYS H 489      39.141  60.068  48.536  1.00 58.25           S  
-ATOM  31196  N   HIS H 490      34.803  60.908  50.192  1.00 28.72           N  
-ATOM  31197  CA  HIS H 490      33.408  61.220  50.466  1.00 28.74           C  
-ATOM  31198  C   HIS H 490      33.316  61.789  51.879  1.00 30.81           C  
-ATOM  31199  O   HIS H 490      33.260  61.046  52.860  1.00 38.69           O  
-ATOM  31200  CB  HIS H 490      32.514  59.985  50.290  1.00 33.61           C  
-ATOM  31201  CG  HIS H 490      33.056  58.735  50.912  1.00 34.15           C  
-ATOM  31202  ND1 HIS H 490      32.531  58.188  52.063  1.00 36.22           N  
-ATOM  31203  CD2 HIS H 490      34.062  57.911  50.531  1.00 34.29           C  
-ATOM  31204  CE1 HIS H 490      33.193  57.087  52.369  1.00 33.81           C  
-ATOM  31205  NE2 HIS H 490      34.130  56.900  51.456  1.00 37.09           N  
-ATOM  31206  N   LEU H 491      33.313  63.115  51.973  1.00 22.08           N  
-ATOM  31207  CA  LEU H 491      33.485  63.787  53.255  1.00 23.35           C  
-ATOM  31208  C   LEU H 491      32.217  64.440  53.798  1.00 21.36           C  
-ATOM  31209  O   LEU H 491      32.211  64.927  54.928  1.00 20.16           O  
-ATOM  31210  CB  LEU H 491      34.593  64.839  53.141  1.00 28.18           C  
-ATOM  31211  CG  LEU H 491      34.511  65.854  51.995  1.00 20.64           C  
-ATOM  31212  CD1 LEU H 491      33.649  67.057  52.357  1.00 19.64           C  
-ATOM  31213  CD2 LEU H 491      35.904  66.298  51.588  1.00 20.19           C  
-ATOM  31214  N   LEU H 492      31.151  64.461  53.005  1.00 22.72           N  
-ATOM  31215  CA  LEU H 492      29.922  65.122  53.435  1.00 18.46           C  
-ATOM  31216  C   LEU H 492      28.670  64.533  52.791  1.00 22.18           C  
-ATOM  31217  O   LEU H 492      28.676  64.174  51.616  1.00 19.12           O  
-ATOM  31218  CB  LEU H 492      30.000  66.617  53.129  1.00 15.50           C  
-ATOM  31219  CG  LEU H 492      28.895  67.476  53.739  1.00 20.42           C  
-ATOM  31220  CD1 LEU H 492      29.507  68.634  54.502  1.00 20.82           C  
-ATOM  31221  CD2 LEU H 492      27.941  67.978  52.664  1.00 24.13           C  
-ATOM  31222  N   CYS H 493      27.595  64.432  53.566  1.00 22.89           N  
-ATOM  31223  CA  CYS H 493      26.312  64.019  53.007  1.00 21.83           C  
-ATOM  31224  C   CYS H 493      25.153  64.760  53.665  1.00 23.15           C  
-ATOM  31225  O   CYS H 493      25.193  65.054  54.856  1.00 26.26           O  
-ATOM  31226  CB  CYS H 493      26.120  62.506  53.144  1.00 29.26           C  
-ATOM  31227  SG  CYS H 493      25.861  61.920  54.827  1.00 26.65           S  
-ATOM  31228  N   GLN H 494      24.127  65.065  52.877  1.00 23.51           N  
-ATOM  31229  CA  GLN H 494      22.960  65.793  53.369  1.00 26.03           C  
-ATOM  31230  C   GLN H 494      21.682  65.110  52.898  1.00 25.36           C  
-ATOM  31231  O   GLN H 494      21.610  64.634  51.767  1.00 21.11           O  
-ATOM  31232  CB  GLN H 494      22.994  67.250  52.898  1.00 25.03           C  
-ATOM  31233  CG  GLN H 494      21.833  68.098  53.391  1.00 23.94           C  
-ATOM  31234  CD  GLN H 494      21.870  69.507  52.837  1.00 26.99           C  
-ATOM  31235  OE1 GLN H 494      22.686  69.824  51.973  1.00 23.49           O  
-ATOM  31236  NE2 GLN H 494      20.984  70.363  53.333  1.00 27.17           N  
-ATOM  31237  N   PHE H 495      20.678  65.057  53.767  1.00 25.29           N  
-ATOM  31238  CA  PHE H 495      19.432  64.371  53.441  1.00 22.25           C  
-ATOM  31239  C   PHE H 495      18.270  65.346  53.282  1.00 19.84           C  
-ATOM  31240  O   PHE H 495      18.300  66.458  53.812  1.00 16.77           O  
-ATOM  31241  CB  PHE H 495      19.111  63.325  54.508  1.00 23.07           C  
-ATOM  31242  CG  PHE H 495      20.131  62.227  54.597  1.00 24.06           C  
-ATOM  31243  CD1 PHE H 495      20.002  61.082  53.830  1.00 21.50           C  
-ATOM  31244  CD2 PHE H 495      21.226  62.345  55.437  1.00 24.35           C  
-ATOM  31245  CE1 PHE H 495      20.941  60.072  53.904  1.00 24.28           C  
-ATOM  31246  CE2 PHE H 495      22.170  61.339  55.515  1.00 19.12           C  
-ATOM  31247  CZ  PHE H 495      22.027  60.202  54.748  1.00 21.69           C  
-ATOM  31248  N   TYR H 496      17.248  64.918  52.547  1.00 20.92           N  
-ATOM  31249  CA  TYR H 496      16.135  65.792  52.193  1.00 21.39           C  
-ATOM  31250  C   TYR H 496      14.831  65.016  52.062  1.00 22.83           C  
-ATOM  31251  O   TYR H 496      14.783  63.967  51.422  1.00 27.46           O  
-ATOM  31252  CB  TYR H 496      16.456  66.525  50.889  1.00 23.06           C  
-ATOM  31253  CG  TYR H 496      15.327  67.327  50.277  1.00 27.21           C  
-ATOM  31254  CD1 TYR H 496      15.116  68.652  50.635  1.00 26.31           C  
-ATOM  31255  CD2 TYR H 496      14.496  66.770  49.311  1.00 27.17           C  
-ATOM  31256  CE1 TYR H 496      14.096  69.391  50.065  1.00 28.08           C  
-ATOM  31257  CE2 TYR H 496      13.476  67.499  48.738  1.00 19.42           C  
-ATOM  31258  CZ  TYR H 496      13.281  68.808  49.117  1.00 20.38           C  
-ATOM  31259  OH  TYR H 496      12.265  69.536  48.544  1.00 24.72           O  
-ATOM  31260  N   VAL H 497      13.772  65.531  52.674  1.00 20.20           N  
-ATOM  31261  CA  VAL H 497      12.465  64.895  52.574  1.00 23.13           C  
-ATOM  31262  C   VAL H 497      11.469  65.862  51.958  1.00 21.22           C  
-ATOM  31263  O   VAL H 497      11.462  67.048  52.287  1.00 25.11           O  
-ATOM  31264  CB  VAL H 497      11.937  64.429  53.950  1.00 19.82           C  
-ATOM  31265  CG1 VAL H 497      10.826  63.405  53.775  1.00 15.88           C  
-ATOM  31266  CG2 VAL H 497      13.056  63.845  54.777  1.00 21.12           C  
-ATOM  31267  N   ASN H 498      10.637  65.357  51.055  1.00 19.58           N  
-ATOM  31268  CA  ASN H 498       9.569  66.164  50.486  1.00 21.49           C  
-ATOM  31269  C   ASN H 498       8.247  65.878  51.191  1.00 32.60           C  
-ATOM  31270  O   ASN H 498       8.226  65.316  52.288  1.00 34.51           O  
-ATOM  31271  CB  ASN H 498       9.443  65.913  48.983  1.00 19.96           C  
-ATOM  31272  CG  ASN H 498       9.116  64.472  48.660  1.00 20.46           C  
-ATOM  31273  OD1 ASN H 498       9.269  63.588  49.501  1.00 19.46           O  
-ATOM  31274  ND2 ASN H 498       8.669  64.225  47.434  1.00 20.68           N  
-ATOM  31275  N   ASP H 499       7.145  66.262  50.560  1.00 31.97           N  
-ATOM  31276  CA  ASP H 499       5.829  66.082  51.159  1.00 34.32           C  
-ATOM  31277  C   ASP H 499       5.281  64.672  50.946  1.00 32.52           C  
-ATOM  31278  O   ASP H 499       4.240  64.315  51.495  1.00 33.08           O  
-ATOM  31279  CB  ASP H 499       4.855  67.117  50.596  1.00 43.63           C  
-ATOM  31280  CG  ASP H 499       4.946  67.242  49.087  1.00 45.19           C  
-ATOM  31281  OD1 ASP H 499       5.945  66.767  48.506  1.00 28.32           O  
-ATOM  31282  OD2 ASP H 499       4.022  67.826  48.483  1.00 57.83           O  
-ATOM  31283  N   GLN H 500       5.987  63.873  50.152  1.00 29.31           N  
-ATOM  31284  CA  GLN H 500       5.548  62.516  49.848  1.00 30.93           C  
-ATOM  31285  C   GLN H 500       6.286  61.482  50.694  1.00 26.55           C  
-ATOM  31286  O   GLN H 500       6.264  60.290  50.380  1.00 26.45           O  
-ATOM  31287  CB  GLN H 500       5.753  62.207  48.363  1.00 35.24           C  
-ATOM  31288  CG  GLN H 500       5.171  63.245  47.420  1.00 34.47           C  
-ATOM  31289  CD  GLN H 500       3.692  63.473  47.647  1.00 47.54           C  
-ATOM  31290  OE1 GLN H 500       3.295  64.427  48.318  1.00 49.31           O  
-ATOM  31291  NE2 GLN H 500       2.865  62.598  47.084  1.00 50.51           N  
-ATOM  31292  N   LYS H 501       6.930  61.947  51.764  1.00 19.31           N  
-ATOM  31293  CA  LYS H 501       7.768  61.101  52.615  1.00 20.53           C  
-ATOM  31294  C   LYS H 501       8.858  60.395  51.809  1.00 27.56           C  
-ATOM  31295  O   LYS H 501       9.194  59.242  52.088  1.00 29.40           O  
-ATOM  31296  CB  LYS H 501       6.922  60.062  53.359  1.00 19.02           C  
-ATOM  31297  CG  LYS H 501       5.851  60.645  54.266  1.00 19.61           C  
-ATOM  31298  CD  LYS H 501       6.202  60.448  55.733  1.00 20.20           C  
-ATOM  31299  CE  LYS H 501       5.075  60.924  56.629  1.00 25.43           C  
-ATOM  31300  NZ  LYS H 501       3.798  60.230  56.304  1.00 35.48           N  
-ATOM  31301  N   GLU H 502       9.403  61.088  50.811  1.00 26.52           N  
-ATOM  31302  CA  GLU H 502      10.465  60.532  49.976  1.00 23.33           C  
-ATOM  31303  C   GLU H 502      11.832  61.101  50.353  1.00 24.12           C  
-ATOM  31304  O   GLU H 502      12.016  62.317  50.416  1.00 22.09           O  
-ATOM  31305  CB  GLU H 502      10.184  60.795  48.496  1.00 19.68           C  
-ATOM  31306  CG  GLU H 502       8.983  60.054  47.944  1.00 25.64           C  
-ATOM  31307  CD  GLU H 502       8.704  60.409  46.496  1.00 46.60           C  
-ATOM  31308  OE1 GLU H 502       8.858  61.595  46.131  1.00 42.84           O  
-ATOM  31309  OE2 GLU H 502       8.336  59.501  45.721  1.00 55.36           O  
-ATOM  31310  N   LEU H 503      12.788  60.210  50.595  1.00 23.08           N  
-ATOM  31311  CA  LEU H 503      14.122  60.613  51.020  1.00 21.08           C  
-ATOM  31312  C   LEU H 503      15.093  60.731  49.849  1.00 25.52           C  
-ATOM  31313  O   LEU H 503      15.122  59.879  48.960  1.00 22.36           O  
-ATOM  31314  CB  LEU H 503      14.675  59.623  52.047  1.00 22.82           C  
-ATOM  31315  CG  LEU H 503      16.072  59.930  52.592  1.00 21.92           C  
-ATOM  31316  CD1 LEU H 503      16.062  61.207  53.421  1.00 18.11           C  
-ATOM  31317  CD2 LEU H 503      16.605  58.759  53.402  1.00 22.52           C  
-ATOM  31318  N   SER H 504      15.880  61.802  49.861  1.00 27.50           N  
-ATOM  31319  CA  SER H 504      16.941  62.013  48.886  1.00 19.89           C  
-ATOM  31320  C   SER H 504      18.241  62.310  49.623  1.00 23.50           C  
-ATOM  31321  O   SER H 504      18.220  62.845  50.736  1.00 22.40           O  
-ATOM  31322  CB  SER H 504      16.594  63.159  47.932  1.00 21.01           C  
-ATOM  31323  OG  SER H 504      15.373  62.921  47.252  1.00 31.34           O  
-ATOM  31324  N   CYS H 505      19.369  61.968  49.008  1.00 24.01           N  
-ATOM  31325  CA  CYS H 505      20.664  62.170  49.646  1.00 18.52           C  
-ATOM  31326  C   CYS H 505      21.713  62.731  48.693  1.00 20.12           C  
-ATOM  31327  O   CYS H 505      21.975  62.161  47.634  1.00 23.98           O  
-ATOM  31328  CB  CYS H 505      21.170  60.857  50.246  1.00 18.53           C  
-ATOM  31329  SG  CYS H 505      22.834  60.971  50.953  1.00 40.96           S  
-ATOM  31330  N   ILE H 506      22.302  63.858  49.084  1.00 23.83           N  
-ATOM  31331  CA  ILE H 506      23.455  64.430  48.397  1.00 22.72           C  
-ATOM  31332  C   ILE H 506      24.732  63.970  49.088  1.00 23.65           C  
-ATOM  31333  O   ILE H 506      24.781  63.886  50.312  1.00 23.48           O  
-ATOM  31334  CB  ILE H 506      23.412  65.982  48.385  1.00 21.44           C  
-ATOM  31335  CG1 ILE H 506      22.351  66.490  47.414  1.00 19.68           C  
-ATOM  31336  CG2 ILE H 506      24.761  66.570  47.994  1.00 18.72           C  
-ATOM  31337  CD1 ILE H 506      22.231  67.995  47.396  1.00 20.62           C  
-ATOM  31338  N   MET H 507      25.759  63.657  48.307  1.00 23.62           N  
-ATOM  31339  CA  MET H 507      27.066  63.360  48.871  1.00 21.39           C  
-ATOM  31340  C   MET H 507      28.153  64.113  48.113  1.00 21.47           C  
-ATOM  31341  O   MET H 507      28.287  63.975  46.896  1.00 23.54           O  
-ATOM  31342  CB  MET H 507      27.338  61.856  48.847  1.00 19.70           C  
-ATOM  31343  CG  MET H 507      28.633  61.451  49.534  1.00 21.30           C  
-ATOM  31344  SD  MET H 507      30.065  61.483  48.439  1.00 28.60           S  
-ATOM  31345  CE  MET H 507      29.822  59.976  47.503  1.00 20.78           C  
-ATOM  31346  N   TYR H 508      28.927  64.914  48.836  1.00 23.92           N  
-ATOM  31347  CA  TYR H 508      30.039  65.630  48.229  1.00 21.78           C  
-ATOM  31348  C   TYR H 508      31.330  64.835  48.362  1.00 20.04           C  
-ATOM  31349  O   TYR H 508      31.674  64.357  49.442  1.00 28.63           O  
-ATOM  31350  CB  TYR H 508      30.210  67.015  48.855  1.00 17.55           C  
-ATOM  31351  CG  TYR H 508      31.287  67.831  48.182  1.00 18.01           C  
-ATOM  31352  CD1 TYR H 508      31.030  68.514  47.001  1.00 20.99           C  
-ATOM  31353  CD2 TYR H 508      32.566  67.905  48.716  1.00 21.47           C  
-ATOM  31354  CE1 TYR H 508      32.013  69.255  46.374  1.00 21.74           C  
-ATOM  31355  CE2 TYR H 508      33.557  68.644  48.096  1.00 22.28           C  
-ATOM  31356  CZ  TYR H 508      33.274  69.316  46.926  1.00 20.71           C  
-ATOM  31357  OH  TYR H 508      34.253  70.053  46.302  1.00 28.84           O  
-ATOM  31358  N   GLN H 509      32.043  64.697  47.252  1.00 18.74           N  
-ATOM  31359  CA  GLN H 509      33.296  63.958  47.234  1.00 23.52           C  
-ATOM  31360  C   GLN H 509      34.416  64.827  46.663  1.00 28.66           C  
-ATOM  31361  O   GLN H 509      34.320  65.316  45.536  1.00 25.86           O  
-ATOM  31362  CB  GLN H 509      33.138  62.673  46.425  1.00 19.42           C  
-ATOM  31363  CG  GLN H 509      34.313  61.723  46.525  1.00 19.13           C  
-ATOM  31364  CD  GLN H 509      34.063  60.434  45.773  1.00 24.43           C  
-ATOM  31365  OE1 GLN H 509      32.932  60.137  45.389  1.00 20.58           O  
-ATOM  31366  NE2 GLN H 509      35.119  59.663  45.553  1.00 31.53           N  
-ATOM  31367  N   ARG H 510      35.472  65.021  47.449  1.00 22.32           N  
-ATOM  31368  CA  ARG H 510      36.563  65.912  47.067  1.00 21.09           C  
-ATOM  31369  C   ARG H 510      37.427  65.332  45.953  1.00 24.46           C  
-ATOM  31370  O   ARG H 510      37.972  66.069  45.129  1.00 23.72           O  
-ATOM  31371  CB  ARG H 510      37.446  66.226  48.276  1.00 19.83           C  
-ATOM  31372  CG  ARG H 510      38.133  65.011  48.875  1.00 24.05           C  
-ATOM  31373  CD  ARG H 510      39.249  65.405  49.822  1.00 24.87           C  
-ATOM  31374  NE  ARG H 510      39.924  64.239  50.385  1.00 26.48           N  
-ATOM  31375  CZ  ARG H 510      40.914  63.587  49.783  1.00 30.57           C  
-ATOM  31376  NH1 ARG H 510      41.470  62.538  50.371  1.00 35.13           N  
-ATOM  31377  NH2 ARG H 510      41.350  63.983  48.595  1.00 26.75           N  
-ATOM  31378  N   SER H 511      37.548  64.010  45.931  1.00 25.96           N  
-ATOM  31379  CA  SER H 511      38.484  63.344  45.037  1.00 26.04           C  
-ATOM  31380  C   SER H 511      37.891  62.040  44.522  1.00 29.31           C  
-ATOM  31381  O   SER H 511      37.522  61.166  45.306  1.00 35.34           O  
-ATOM  31382  CB  SER H 511      39.805  63.087  45.762  1.00 28.35           C  
-ATOM  31383  OG  SER H 511      40.763  62.518  44.897  1.00 31.33           O  
-ATOM  31384  N   CYS H 512      37.803  61.908  43.203  1.00 28.22           N  
-ATOM  31385  CA  CYS H 512      37.092  60.781  42.613  1.00 31.65           C  
-ATOM  31386  C   CYS H 512      37.929  59.964  41.635  1.00 34.70           C  
-ATOM  31387  O   CYS H 512      38.215  60.410  40.524  1.00 37.00           O  
-ATOM  31388  CB  CYS H 512      35.832  61.278  41.904  1.00 28.87           C  
-ATOM  31389  SG  CYS H 512      34.797  62.357  42.908  1.00 35.48           S  
-ATOM  31390  N   ASP H 513      38.310  58.763  42.053  1.00 35.85           N  
-ATOM  31391  CA  ASP H 513      38.885  57.788  41.139  1.00 28.22           C  
-ATOM  31392  C   ASP H 513      37.753  57.228  40.289  1.00 31.15           C  
-ATOM  31393  O   ASP H 513      37.091  56.267  40.681  1.00 38.92           O  
-ATOM  31394  CB  ASP H 513      39.602  56.673  41.903  1.00 36.67           C  
-ATOM  31395  CG  ASP H 513      40.464  55.801  41.004  1.00 40.13           C  
-ATOM  31396  OD1 ASP H 513      40.226  55.768  39.778  1.00 43.21           O  
-ATOM  31397  OD2 ASP H 513      41.385  55.143  41.531  1.00 44.87           O  
-ATOM  31398  N   VAL H 514      37.531  57.841  39.130  1.00 24.42           N  
-ATOM  31399  CA  VAL H 514      36.397  57.500  38.277  1.00 23.07           C  
-ATOM  31400  C   VAL H 514      36.419  56.041  37.842  1.00 27.92           C  
-ATOM  31401  O   VAL H 514      35.376  55.392  37.763  1.00 33.59           O  
-ATOM  31402  CB  VAL H 514      36.355  58.397  37.030  1.00 23.08           C  
-ATOM  31403  CG1 VAL H 514      35.126  58.089  36.186  1.00 23.49           C  
-ATOM  31404  CG2 VAL H 514      36.362  59.853  37.442  1.00 26.31           C  
-ATOM  31405  N   GLY H 515      37.613  55.525  37.575  1.00 35.99           N  
-ATOM  31406  CA  GLY H 515      37.756  54.150  37.140  1.00 30.64           C  
-ATOM  31407  C   GLY H 515      37.414  53.147  38.224  1.00 31.62           C  
-ATOM  31408  O   GLY H 515      36.672  52.194  37.991  1.00 41.29           O  
-ATOM  31409  N   LEU H 516      37.940  53.370  39.421  1.00 35.85           N  
-ATOM  31410  CA  LEU H 516      37.858  52.371  40.477  1.00 43.23           C  
-ATOM  31411  C   LEU H 516      36.815  52.706  41.541  1.00 44.37           C  
-ATOM  31412  O   LEU H 516      35.890  51.928  41.778  1.00 55.09           O  
-ATOM  31413  CB  LEU H 516      39.232  52.198  41.130  1.00 53.53           C  
-ATOM  31414  CG  LEU H 516      39.540  50.849  41.780  1.00 57.46           C  
-ATOM  31415  CD1 LEU H 516      39.321  49.712  40.797  1.00 52.49           C  
-ATOM  31416  CD2 LEU H 516      40.968  50.833  42.302  1.00 57.67           C  
-ATOM  31417  N   GLY H 517      36.963  53.868  42.169  1.00 37.52           N  
-ATOM  31418  CA  GLY H 517      36.193  54.203  43.354  1.00 42.98           C  
-ATOM  31419  C   GLY H 517      34.764  54.691  43.174  1.00 40.42           C  
-ATOM  31420  O   GLY H 517      33.917  54.430  44.027  1.00 39.81           O  
-ATOM  31421  N   VAL H 518      34.494  55.398  42.080  1.00 28.65           N  
-ATOM  31422  CA  VAL H 518      33.201  56.057  41.887  1.00 22.50           C  
-ATOM  31423  C   VAL H 518      31.984  55.119  41.905  1.00 24.51           C  
-ATOM  31424  O   VAL H 518      31.024  55.399  42.627  1.00 33.39           O  
-ATOM  31425  CB  VAL H 518      33.193  56.882  40.571  1.00 20.74           C  
-ATOM  31426  CG1 VAL H 518      31.770  57.128  40.089  1.00 20.29           C  
-ATOM  31427  CG2 VAL H 518      33.926  58.189  40.780  1.00 27.01           C  
-ATOM  31428  N   PRO H 519      32.006  54.012  41.129  1.00 21.11           N  
-ATOM  31429  CA  PRO H 519      30.833  53.130  41.193  1.00 25.58           C  
-ATOM  31430  C   PRO H 519      30.592  52.622  42.609  1.00 28.36           C  
-ATOM  31431  O   PRO H 519      29.453  52.579  43.096  1.00 26.90           O  
-ATOM  31432  CB  PRO H 519      31.209  51.974  40.253  1.00 24.98           C  
-ATOM  31433  CG  PRO H 519      32.218  52.549  39.338  1.00 19.63           C  
-ATOM  31434  CD  PRO H 519      33.009  53.496  40.180  1.00 22.65           C  
-ATOM  31435  N   PHE H 520      31.693  52.249  43.253  1.00 30.87           N  
-ATOM  31436  CA  PHE H 520      31.699  51.811  44.637  1.00 30.54           C  
-ATOM  31437  C   PHE H 520      31.014  52.836  45.537  1.00 29.02           C  
-ATOM  31438  O   PHE H 520      30.167  52.481  46.354  1.00 23.73           O  
-ATOM  31439  CB  PHE H 520      33.132  51.566  45.104  1.00 23.83           C  
-ATOM  31440  CG  PHE H 520      33.234  50.697  46.320  1.00 26.33           C  
-ATOM  31441  CD1 PHE H 520      33.150  51.242  47.590  1.00 24.70           C  
-ATOM  31442  CD2 PHE H 520      33.430  49.331  46.193  1.00 26.72           C  
-ATOM  31443  CE1 PHE H 520      33.250  50.438  48.706  1.00 28.65           C  
-ATOM  31444  CE2 PHE H 520      33.532  48.526  47.304  1.00 20.07           C  
-ATOM  31445  CZ  PHE H 520      33.445  49.079  48.562  1.00 25.89           C  
-ATOM  31446  N   ASN H 521      31.375  54.106  45.376  1.00 24.56           N  
-ATOM  31447  CA  ASN H 521      30.810  55.168  46.197  1.00 21.98           C  
-ATOM  31448  C   ASN H 521      29.319  55.357  45.944  1.00 22.45           C  
-ATOM  31449  O   ASN H 521      28.530  55.495  46.891  1.00 29.70           O  
-ATOM  31450  CB  ASN H 521      31.554  56.479  45.951  1.00 25.34           C  
-ATOM  31451  CG  ASN H 521      32.984  56.444  46.460  1.00 27.49           C  
-ATOM  31452  OD1 ASN H 521      33.926  56.720  45.719  1.00 28.75           O  
-ATOM  31453  ND2 ASN H 521      33.152  56.100  47.731  1.00 26.34           N  
-ATOM  31454  N   ILE H 522      28.946  55.363  44.666  1.00 18.61           N  
-ATOM  31455  CA  ILE H 522      27.544  55.419  44.265  1.00 16.29           C  
-ATOM  31456  C   ILE H 522      26.745  54.355  45.000  1.00 19.17           C  
-ATOM  31457  O   ILE H 522      25.770  54.666  45.697  1.00 21.03           O  
-ATOM  31458  CB  ILE H 522      27.377  55.225  42.742  1.00 15.47           C  
-ATOM  31459  CG1 ILE H 522      28.087  56.346  41.981  1.00 17.26           C  
-ATOM  31460  CG2 ILE H 522      25.907  55.177  42.373  1.00 12.40           C  
-ATOM  31461  CD1 ILE H 522      27.934  56.258  40.483  1.00 13.94           C  
-ATOM  31462  N   ALA H 523      27.183  53.106  44.858  1.00 20.68           N  
-ATOM  31463  CA  ALA H 523      26.525  51.982  45.519  1.00 21.95           C  
-ATOM  31464  C   ALA H 523      26.449  52.196  47.024  1.00 21.12           C  
-ATOM  31465  O   ALA H 523      25.405  51.967  47.645  1.00 21.95           O  
-ATOM  31466  CB  ALA H 523      27.251  50.682  45.211  1.00 23.81           C  
-ATOM  31467  N   SER H 524      27.559  52.647  47.599  1.00 19.13           N  
-ATOM  31468  CA  SER H 524      27.656  52.864  49.035  1.00 17.82           C  
-ATOM  31469  C   SER H 524      26.603  53.831  49.563  1.00 18.67           C  
-ATOM  31470  O   SER H 524      25.803  53.475  50.429  1.00 22.01           O  
-ATOM  31471  CB  SER H 524      29.054  53.371  49.394  1.00 18.33           C  
-ATOM  31472  OG  SER H 524      29.172  53.562  50.791  1.00 29.39           O  
-ATOM  31473  N   TYR H 525      26.601  55.056  49.051  1.00 22.37           N  
-ATOM  31474  CA  TYR H 525      25.686  56.058  49.590  1.00 21.42           C  
-ATOM  31475  C   TYR H 525      24.241  55.839  49.141  1.00 25.95           C  
-ATOM  31476  O   TYR H 525      23.309  56.255  49.836  1.00 34.39           O  
-ATOM  31477  CB  TYR H 525      26.163  57.467  49.237  1.00 15.99           C  
-ATOM  31478  CG  TYR H 525      27.242  57.930  50.192  1.00 18.02           C  
-ATOM  31479  CD1 TYR H 525      26.915  58.581  51.375  1.00 25.03           C  
-ATOM  31480  CD2 TYR H 525      28.580  57.683  49.930  1.00 15.50           C  
-ATOM  31481  CE1 TYR H 525      27.893  58.991  52.260  1.00 18.95           C  
-ATOM  31482  CE2 TYR H 525      29.564  58.087  50.806  1.00 16.13           C  
-ATOM  31483  CZ  TYR H 525      29.216  58.742  51.971  1.00 20.02           C  
-ATOM  31484  OH  TYR H 525      30.194  59.151  52.852  1.00 29.08           O  
-ATOM  31485  N   SER H 526      24.041  55.173  48.006  1.00 20.73           N  
-ATOM  31486  CA  SER H 526      22.686  54.773  47.631  1.00 21.19           C  
-ATOM  31487  C   SER H 526      22.145  53.784  48.665  1.00 25.71           C  
-ATOM  31488  O   SER H 526      21.008  53.909  49.139  1.00 29.36           O  
-ATOM  31489  CB  SER H 526      22.662  54.154  46.234  1.00 18.23           C  
-ATOM  31490  OG  SER H 526      23.116  55.074  45.258  1.00 15.94           O  
-ATOM  31491  N   LEU H 527      22.978  52.806  49.015  1.00 22.22           N  
-ATOM  31492  CA  LEU H 527      22.628  51.824  50.035  1.00 25.45           C  
-ATOM  31493  C   LEU H 527      22.342  52.497  51.374  1.00 24.79           C  
-ATOM  31494  O   LEU H 527      21.347  52.178  52.035  1.00 23.85           O  
-ATOM  31495  CB  LEU H 527      23.748  50.794  50.194  1.00 23.46           C  
-ATOM  31496  CG  LEU H 527      23.508  49.663  51.198  1.00 17.43           C  
-ATOM  31497  CD1 LEU H 527      22.221  48.923  50.879  1.00 16.00           C  
-ATOM  31498  CD2 LEU H 527      24.686  48.705  51.206  1.00 18.24           C  
-ATOM  31499  N   LEU H 528      23.215  53.422  51.771  1.00 19.40           N  
-ATOM  31500  CA  LEU H 528      23.002  54.183  53.001  1.00 19.87           C  
-ATOM  31501  C   LEU H 528      21.647  54.873  52.968  1.00 21.53           C  
-ATOM  31502  O   LEU H 528      20.912  54.867  53.962  1.00 26.36           O  
-ATOM  31503  CB  LEU H 528      24.102  55.227  53.218  1.00 21.63           C  
-ATOM  31504  CG  LEU H 528      23.895  56.159  54.421  1.00 12.71           C  
-ATOM  31505  CD1 LEU H 528      23.834  55.363  55.712  1.00 13.56           C  
-ATOM  31506  CD2 LEU H 528      24.985  57.216  54.503  1.00 16.72           C  
-ATOM  31507  N   THR H 529      21.319  55.464  51.821  1.00 16.92           N  
-ATOM  31508  CA  THR H 529      20.025  56.112  51.647  1.00 18.14           C  
-ATOM  31509  C   THR H 529      18.882  55.126  51.843  1.00 17.27           C  
-ATOM  31510  O   THR H 529      17.905  55.437  52.513  1.00 21.73           O  
-ATOM  31511  CB  THR H 529      19.893  56.764  50.261  1.00 18.44           C  
-ATOM  31512  OG1 THR H 529      20.964  57.695  50.069  1.00 18.31           O  
-ATOM  31513  CG2 THR H 529      18.567  57.502  50.152  1.00 22.16           C  
-ATOM  31514  N   LEU H 530      19.012  53.936  51.266  1.00 15.91           N  
-ATOM  31515  CA  LEU H 530      18.005  52.892  51.446  1.00 16.66           C  
-ATOM  31516  C   LEU H 530      17.799  52.543  52.923  1.00 18.53           C  
-ATOM  31517  O   LEU H 530      16.659  52.482  53.405  1.00 19.48           O  
-ATOM  31518  CB  LEU H 530      18.391  51.631  50.671  1.00 19.12           C  
-ATOM  31519  CG  LEU H 530      17.717  51.402  49.320  1.00 17.29           C  
-ATOM  31520  CD1 LEU H 530      17.960  52.576  48.392  1.00 18.49           C  
-ATOM  31521  CD2 LEU H 530      18.213  50.108  48.693  1.00 14.52           C  
-ATOM  31522  N   MET H 531      18.902  52.321  53.635  1.00 17.13           N  
-ATOM  31523  CA  MET H 531      18.845  51.953  55.048  1.00 15.98           C  
-ATOM  31524  C   MET H 531      18.200  53.040  55.913  1.00 22.01           C  
-ATOM  31525  O   MET H 531      17.268  52.767  56.691  1.00 25.22           O  
-ATOM  31526  CB  MET H 531      20.252  51.638  55.550  1.00 17.05           C  
-ATOM  31527  CG  MET H 531      20.939  50.535  54.762  1.00 16.79           C  
-ATOM  31528  SD  MET H 531      22.700  50.391  55.116  1.00 21.68           S  
-ATOM  31529  CE  MET H 531      22.661  49.944  56.845  1.00 13.55           C  
-ATOM  31530  N   VAL H 532      18.703  54.265  55.776  1.00 21.25           N  
-ATOM  31531  CA  VAL H 532      18.144  55.404  56.501  1.00 22.83           C  
-ATOM  31532  C   VAL H 532      16.647  55.564  56.211  1.00 22.30           C  
-ATOM  31533  O   VAL H 532      15.831  55.715  57.131  1.00 15.85           O  
-ATOM  31534  CB  VAL H 532      18.879  56.712  56.146  1.00 14.98           C  
-ATOM  31535  CG1 VAL H 532      18.160  57.891  56.743  1.00 16.33           C  
-ATOM  31536  CG2 VAL H 532      20.317  56.664  56.634  1.00 13.94           C  
-ATOM  31537  N   ALA H 533      16.297  55.514  54.928  1.00 18.13           N  
-ATOM  31538  CA  ALA H 533      14.905  55.601  54.505  1.00 16.54           C  
-ATOM  31539  C   ALA H 533      14.070  54.529  55.184  1.00 19.54           C  
-ATOM  31540  O   ALA H 533      12.939  54.792  55.594  1.00 27.02           O  
-ATOM  31541  CB  ALA H 533      14.789  55.479  52.993  1.00 19.70           C  
-ATOM  31542  N   HIS H 534      14.618  53.324  55.321  1.00 19.23           N  
-ATOM  31543  CA  HIS H 534      13.862  52.279  56.006  1.00 27.91           C  
-ATOM  31544  C   HIS H 534      13.676  52.572  57.493  1.00 27.03           C  
-ATOM  31545  O   HIS H 534      12.561  52.459  58.005  1.00 23.65           O  
-ATOM  31546  CB  HIS H 534      14.515  50.909  55.857  1.00 21.23           C  
-ATOM  31547  CG  HIS H 534      13.787  49.830  56.596  1.00 23.62           C  
-ATOM  31548  ND1 HIS H 534      14.270  49.261  57.756  1.00 29.35           N  
-ATOM  31549  CD2 HIS H 534      12.584  49.252  56.366  1.00 24.40           C  
-ATOM  31550  CE1 HIS H 534      13.408  48.361  58.194  1.00 27.85           C  
-ATOM  31551  NE2 HIS H 534      12.376  48.336  57.369  1.00 33.08           N  
-ATOM  31552  N   VAL H 535      14.750  52.941  58.192  1.00 26.91           N  
-ATOM  31553  CA  VAL H 535      14.616  53.170  59.634  1.00 25.49           C  
-ATOM  31554  C   VAL H 535      13.887  54.481  59.954  1.00 33.81           C  
-ATOM  31555  O   VAL H 535      13.617  54.774  61.121  1.00 28.10           O  
-ATOM  31556  CB  VAL H 535      15.981  53.169  60.360  1.00 20.61           C  
-ATOM  31557  CG1 VAL H 535      16.573  51.770  60.376  1.00 20.57           C  
-ATOM  31558  CG2 VAL H 535      16.947  54.165  59.729  1.00 22.03           C  
-ATOM  31559  N   CYS H 536      13.562  55.264  58.927  1.00 32.17           N  
-ATOM  31560  CA  CYS H 536      12.799  56.493  59.141  1.00 25.84           C  
-ATOM  31561  C   CYS H 536      11.380  56.412  58.582  1.00 24.90           C  
-ATOM  31562  O   CYS H 536      10.662  57.412  58.567  1.00 32.11           O  
-ATOM  31563  CB  CYS H 536      13.523  57.684  58.517  1.00 19.10           C  
-ATOM  31564  SG  CYS H 536      15.123  58.071  59.253  1.00 21.67           S  
-ATOM  31565  N   ASN H 537      10.985  55.224  58.131  1.00 26.62           N  
-ATOM  31566  CA  ASN H 537       9.695  55.023  57.470  1.00 29.01           C  
-ATOM  31567  C   ASN H 537       9.520  55.939  56.264  1.00 27.89           C  
-ATOM  31568  O   ASN H 537       8.413  56.380  55.956  1.00 30.67           O  
-ATOM  31569  CB  ASN H 537       8.543  55.227  58.457  1.00 28.55           C  
-ATOM  31570  CG  ASN H 537       8.401  54.077  59.428  1.00 46.63           C  
-ATOM  31571  OD1 ASN H 537       9.112  54.002  60.432  1.00 60.25           O  
-ATOM  31572  ND2 ASN H 537       7.479  53.169  59.134  1.00 41.39           N  
-ATOM  31573  N   LEU H 538      10.629  56.220  55.588  1.00 23.34           N  
-ATOM  31574  CA  LEU H 538      10.609  57.029  54.378  1.00 24.76           C  
-ATOM  31575  C   LEU H 538      10.864  56.154  53.160  1.00 24.16           C  
-ATOM  31576  O   LEU H 538      11.348  55.029  53.284  1.00 23.44           O  
-ATOM  31577  CB  LEU H 538      11.648  58.146  54.461  1.00 20.86           C  
-ATOM  31578  CG  LEU H 538      11.468  59.115  55.629  1.00 17.02           C  
-ATOM  31579  CD1 LEU H 538      12.646  60.065  55.717  1.00 19.26           C  
-ATOM  31580  CD2 LEU H 538      10.168  59.882  55.473  1.00 17.40           C  
-ATOM  31581  N   LYS H 539      10.526  56.671  51.985  1.00 21.67           N  
-ATOM  31582  CA  LYS H 539      10.731  55.941  50.741  1.00 21.92           C  
-ATOM  31583  C   LYS H 539      11.917  56.523  49.982  1.00 27.80           C  
-ATOM  31584  O   LYS H 539      11.935  57.716  49.681  1.00 34.34           O  
-ATOM  31585  CB  LYS H 539       9.468  55.988  49.879  1.00 20.86           C  
-ATOM  31586  CG  LYS H 539       8.256  55.308  50.507  1.00 22.95           C  
-ATOM  31587  CD  LYS H 539       6.973  55.662  49.768  1.00 24.96           C  
-ATOM  31588  CE  LYS H 539       6.293  56.882  50.380  1.00 31.43           C  
-ATOM  31589  NZ  LYS H 539       5.447  57.597  49.376  1.00 38.83           N  
-ATOM  31590  N   PRO H 540      12.922  55.685  49.682  1.00 18.51           N  
-ATOM  31591  CA  PRO H 540      14.094  56.163  48.945  1.00 18.20           C  
-ATOM  31592  C   PRO H 540      13.704  56.673  47.564  1.00 25.75           C  
-ATOM  31593  O   PRO H 540      12.892  56.046  46.885  1.00 31.91           O  
-ATOM  31594  CB  PRO H 540      14.987  54.922  48.855  1.00 20.69           C  
-ATOM  31595  CG  PRO H 540      14.063  53.771  49.032  1.00 23.70           C  
-ATOM  31596  CD  PRO H 540      13.014  54.249  49.989  1.00 24.54           C  
-ATOM  31597  N   LYS H 541      14.270  57.806  47.165  1.00 23.50           N  
-ATOM  31598  CA  LYS H 541      13.874  58.453  45.922  1.00 25.02           C  
-ATOM  31599  C   LYS H 541      15.057  58.754  45.011  1.00 25.56           C  
-ATOM  31600  O   LYS H 541      14.989  58.517  43.806  1.00 28.35           O  
-ATOM  31601  CB  LYS H 541      13.114  59.749  46.219  1.00 31.47           C  
-ATOM  31602  CG  LYS H 541      12.828  60.602  44.990  1.00 25.84           C  
-ATOM  31603  CD  LYS H 541      12.257  61.956  45.384  1.00 30.77           C  
-ATOM  31604  CE  LYS H 541      12.214  62.917  44.205  1.00 37.34           C  
-ATOM  31605  NZ  LYS H 541      11.310  62.431  43.128  1.00 44.17           N  
-ATOM  31606  N   GLU H 542      16.141  59.270  45.582  1.00 25.16           N  
-ATOM  31607  CA  GLU H 542      17.238  59.768  44.763  1.00 23.56           C  
-ATOM  31608  C   GLU H 542      18.559  59.895  45.515  1.00 22.56           C  
-ATOM  31609  O   GLU H 542      18.590  60.290  46.680  1.00 20.32           O  
-ATOM  31610  CB  GLU H 542      16.852  61.127  44.177  1.00 38.64           C  
-ATOM  31611  CG  GLU H 542      17.603  61.520  42.919  1.00 41.09           C  
-ATOM  31612  CD  GLU H 542      16.969  62.710  42.226  1.00 49.68           C  
-ATOM  31613  OE1 GLU H 542      17.133  62.843  40.993  1.00 44.28           O  
-ATOM  31614  OE2 GLU H 542      16.300  63.511  42.917  1.00 40.27           O  
-ATOM  31615  N   PHE H 543      19.650  59.555  44.835  1.00 24.78           N  
-ATOM  31616  CA  PHE H 543      20.985  59.850  45.337  1.00 18.79           C  
-ATOM  31617  C   PHE H 543      21.676  60.860  44.437  1.00 18.03           C  
-ATOM  31618  O   PHE H 543      21.886  60.606  43.251  1.00 15.05           O  
-ATOM  31619  CB  PHE H 543      21.842  58.592  45.434  1.00 16.24           C  
-ATOM  31620  CG  PHE H 543      23.313  58.880  45.541  1.00 14.74           C  
-ATOM  31621  CD1 PHE H 543      23.826  59.510  46.663  1.00 18.04           C  
-ATOM  31622  CD2 PHE H 543      24.180  58.534  44.519  1.00 14.41           C  
-ATOM  31623  CE1 PHE H 543      25.177  59.786  46.766  1.00 16.51           C  
-ATOM  31624  CE2 PHE H 543      25.533  58.806  44.617  1.00 14.01           C  
-ATOM  31625  CZ  PHE H 543      26.031  59.432  45.743  1.00 16.78           C  
-ATOM  31626  N   ILE H 544      22.039  62.002  45.007  1.00 18.02           N  
-ATOM  31627  CA  ILE H 544      22.715  63.041  44.248  1.00 17.10           C  
-ATOM  31628  C   ILE H 544      24.209  63.057  44.564  1.00 20.83           C  
-ATOM  31629  O   ILE H 544      24.623  63.215  45.713  1.00 17.75           O  
-ATOM  31630  CB  ILE H 544      22.099  64.419  44.526  1.00 22.13           C  
-ATOM  31631  CG1 ILE H 544      20.576  64.342  44.385  1.00 26.73           C  
-ATOM  31632  CG2 ILE H 544      22.684  65.465  43.590  1.00 15.89           C  
-ATOM  31633  CD1 ILE H 544      19.857  65.638  44.682  1.00 23.41           C  
-ATOM  31634  N   HIS H 545      25.009  62.886  43.519  1.00 16.52           N  
-ATOM  31635  CA  HIS H 545      26.452  62.752  43.636  1.00 16.22           C  
-ATOM  31636  C   HIS H 545      27.186  64.014  43.180  1.00 19.93           C  
-ATOM  31637  O   HIS H 545      27.204  64.345  41.984  1.00 22.38           O  
-ATOM  31638  CB  HIS H 545      26.922  61.548  42.819  1.00 17.48           C  
-ATOM  31639  CG  HIS H 545      28.290  61.066  43.177  1.00 19.86           C  
-ATOM  31640  ND1 HIS H 545      29.093  61.712  44.095  1.00 20.56           N  
-ATOM  31641  CD2 HIS H 545      29.000  59.998  42.747  1.00 15.64           C  
-ATOM  31642  CE1 HIS H 545      30.236  61.065  44.210  1.00 17.21           C  
-ATOM  31643  NE2 HIS H 545      30.207  60.018  43.403  1.00 20.55           N  
-ATOM  31644  N   PHE H 546      27.790  64.707  44.143  1.00 15.30           N  
-ATOM  31645  CA  PHE H 546      28.578  65.907  43.874  1.00 18.16           C  
-ATOM  31646  C   PHE H 546      30.072  65.607  43.939  1.00 18.41           C  
-ATOM  31647  O   PHE H 546      30.567  65.107  44.948  1.00 19.68           O  
-ATOM  31648  CB  PHE H 546      28.224  67.018  44.864  1.00 17.42           C  
-ATOM  31649  CG  PHE H 546      26.942  67.731  44.543  1.00 21.89           C  
-ATOM  31650  CD1 PHE H 546      26.229  67.421  43.394  1.00 21.86           C  
-ATOM  31651  CD2 PHE H 546      26.459  68.724  45.379  1.00 22.33           C  
-ATOM  31652  CE1 PHE H 546      25.054  68.081  43.093  1.00 17.06           C  
-ATOM  31653  CE2 PHE H 546      25.283  69.388  45.083  1.00 19.69           C  
-ATOM  31654  CZ  PHE H 546      24.580  69.065  43.937  1.00 19.53           C  
-ATOM  31655  N   MET H 547      30.790  65.922  42.865  1.00 18.82           N  
-ATOM  31656  CA  MET H 547      32.191  65.531  42.744  1.00 15.99           C  
-ATOM  31657  C   MET H 547      33.116  66.727  42.525  1.00 21.20           C  
-ATOM  31658  O   MET H 547      32.869  67.560  41.655  1.00 21.44           O  
-ATOM  31659  CB  MET H 547      32.346  64.532  41.598  1.00 16.26           C  
-ATOM  31660  CG  MET H 547      31.334  63.393  41.659  1.00 25.71           C  
-ATOM  31661  SD  MET H 547      31.137  62.469  40.124  1.00 25.97           S  
-ATOM  31662  CE  MET H 547      32.642  61.506  40.114  1.00 23.13           C  
-ATOM  31663  N   GLY H 548      34.179  66.809  43.320  1.00 24.91           N  
-ATOM  31664  CA  GLY H 548      35.151  67.883  43.196  1.00 20.53           C  
-ATOM  31665  C   GLY H 548      36.218  67.577  42.159  1.00 21.79           C  
-ATOM  31666  O   GLY H 548      35.993  67.741  40.960  1.00 18.33           O  
-ATOM  31667  N   ASN H 549      37.388  67.141  42.618  1.00 21.97           N  
-ATOM  31668  CA  ASN H 549      38.433  66.696  41.703  1.00 21.76           C  
-ATOM  31669  C   ASN H 549      38.045  65.357  41.088  1.00 24.40           C  
-ATOM  31670  O   ASN H 549      38.096  64.320  41.749  1.00 30.73           O  
-ATOM  31671  CB  ASN H 549      39.782  66.581  42.417  1.00 27.76           C  
-ATOM  31672  CG  ASN H 549      40.946  66.430  41.449  1.00 24.08           C  
-ATOM  31673  OD1 ASN H 549      41.182  65.350  40.906  1.00 25.27           O  
-ATOM  31674  ND2 ASN H 549      41.680  67.515  41.235  1.00 17.17           N  
-ATOM  31675  N   THR H 550      37.649  65.385  39.822  1.00 16.83           N  
-ATOM  31676  CA  THR H 550      37.166  64.187  39.152  1.00 21.83           C  
-ATOM  31677  C   THR H 550      38.190  63.701  38.130  1.00 31.02           C  
-ATOM  31678  O   THR H 550      38.280  64.236  37.025  1.00 36.74           O  
-ATOM  31679  CB  THR H 550      35.820  64.449  38.464  1.00 20.04           C  
-ATOM  31680  OG1 THR H 550      34.971  65.187  39.350  1.00 21.64           O  
-ATOM  31681  CG2 THR H 550      35.147  63.146  38.104  1.00 26.03           C  
-ATOM  31682  N   HIS H 551      38.955  62.679  38.503  1.00 22.93           N  
-ATOM  31683  CA  HIS H 551      40.119  62.279  37.721  1.00 22.68           C  
-ATOM  31684  C   HIS H 551      40.096  60.824  37.271  1.00 24.99           C  
-ATOM  31685  O   HIS H 551      39.546  59.958  37.948  1.00 32.51           O  
-ATOM  31686  CB  HIS H 551      41.391  62.528  38.530  1.00 35.85           C  
-ATOM  31687  CG  HIS H 551      41.369  61.898  39.886  1.00 36.04           C  
-ATOM  31688  ND1 HIS H 551      41.080  62.608  41.031  1.00 29.43           N  
-ATOM  31689  CD2 HIS H 551      41.583  60.619  40.281  1.00 35.94           C  
-ATOM  31690  CE1 HIS H 551      41.124  61.797  42.072  1.00 30.88           C  
-ATOM  31691  NE2 HIS H 551      41.427  60.585  41.645  1.00 28.88           N  
-ATOM  31692  N   VAL H 552      40.715  60.573  36.122  1.00 33.01           N  
-ATOM  31693  CA  VAL H 552      40.909  59.224  35.610  1.00 22.03           C  
-ATOM  31694  C   VAL H 552      42.402  58.931  35.528  1.00 28.03           C  
-ATOM  31695  O   VAL H 552      43.137  59.636  34.833  1.00 28.72           O  
-ATOM  31696  CB  VAL H 552      40.272  59.046  34.220  1.00 13.84           C  
-ATOM  31697  CG1 VAL H 552      40.792  57.788  33.557  1.00 22.82           C  
-ATOM  31698  CG2 VAL H 552      38.758  59.018  34.324  1.00 16.17           C  
-ATOM  31699  N   TYR H 553      42.854  57.905  36.245  1.00 35.70           N  
-ATOM  31700  CA  TYR H 553      44.275  57.562  36.254  1.00 35.78           C  
-ATOM  31701  C   TYR H 553      44.710  57.060  34.885  1.00 32.68           C  
-ATOM  31702  O   TYR H 553      43.990  56.307  34.227  1.00 32.81           O  
-ATOM  31703  CB  TYR H 553      44.583  56.526  37.341  1.00 27.57           C  
-ATOM  31704  CG  TYR H 553      44.622  57.128  38.730  1.00 36.54           C  
-ATOM  31705  CD1 TYR H 553      45.733  57.835  39.166  1.00 39.95           C  
-ATOM  31706  CD2 TYR H 553      43.544  57.004  39.597  1.00 33.88           C  
-ATOM  31707  CE1 TYR H 553      45.773  58.398  40.429  1.00 38.80           C  
-ATOM  31708  CE2 TYR H 553      43.575  57.563  40.864  1.00 30.37           C  
-ATOM  31709  CZ  TYR H 553      44.694  58.260  41.273  1.00 29.53           C  
-ATOM  31710  OH  TYR H 553      44.742  58.822  42.527  1.00 25.08           O  
-ATOM  31711  N   THR H 554      45.889  57.500  34.459  1.00 30.57           N  
-ATOM  31712  CA  THR H 554      46.389  57.214  33.119  1.00 35.53           C  
-ATOM  31713  C   THR H 554      46.496  55.719  32.817  1.00 34.49           C  
-ATOM  31714  O   THR H 554      46.306  55.300  31.676  1.00 31.40           O  
-ATOM  31715  CB  THR H 554      47.764  57.868  32.900  1.00 36.76           C  
-ATOM  31716  OG1 THR H 554      48.538  57.763  34.102  1.00 36.70           O  
-ATOM  31717  CG2 THR H 554      47.600  59.338  32.546  1.00 31.88           C  
-ATOM  31718  N   ASN H 555      46.789  54.917  33.835  1.00 34.45           N  
-ATOM  31719  CA  ASN H 555      46.897  53.474  33.649  1.00 27.38           C  
-ATOM  31720  C   ASN H 555      45.541  52.772  33.754  1.00 32.98           C  
-ATOM  31721  O   ASN H 555      45.474  51.558  33.949  1.00 38.45           O  
-ATOM  31722  CB  ASN H 555      47.884  52.878  34.658  1.00 29.46           C  
-ATOM  31723  CG  ASN H 555      47.453  53.089  36.099  1.00 33.84           C  
-ATOM  31724  OD1 ASN H 555      46.758  54.052  36.419  1.00 45.09           O  
-ATOM  31725  ND2 ASN H 555      47.874  52.189  36.978  1.00 33.75           N  
-ATOM  31726  N   HIS H 556      44.467  53.544  33.623  1.00 36.95           N  
-ATOM  31727  CA  HIS H 556      43.111  53.000  33.620  1.00 44.35           C  
-ATOM  31728  C   HIS H 556      42.439  53.239  32.275  1.00 38.77           C  
-ATOM  31729  O   HIS H 556      41.429  52.612  31.953  1.00 31.66           O  
-ATOM  31730  CB  HIS H 556      42.266  53.631  34.729  1.00 35.43           C  
-ATOM  31731  CG  HIS H 556      42.638  53.185  36.106  1.00 31.91           C  
-ATOM  31732  ND1 HIS H 556      41.933  53.572  37.225  1.00 42.28           N  
-ATOM  31733  CD2 HIS H 556      43.636  52.384  36.548  1.00 37.50           C  
-ATOM  31734  CE1 HIS H 556      42.481  53.030  38.298  1.00 50.40           C  
-ATOM  31735  NE2 HIS H 556      43.517  52.305  37.914  1.00 55.39           N  
-ATOM  31736  N   VAL H 557      43.017  54.155  31.504  1.00 29.31           N  
-ATOM  31737  CA  VAL H 557      42.391  54.693  30.302  1.00 29.62           C  
-ATOM  31738  C   VAL H 557      41.976  53.642  29.279  1.00 33.82           C  
-ATOM  31739  O   VAL H 557      40.864  53.689  28.749  1.00 33.15           O  
-ATOM  31740  CB  VAL H 557      43.332  55.699  29.612  1.00 35.45           C  
-ATOM  31741  CG1 VAL H 557      42.724  56.184  28.306  1.00 26.90           C  
-ATOM  31742  CG2 VAL H 557      43.631  56.865  30.541  1.00 31.65           C  
-ATOM  31743  N   GLU H 558      42.871  52.702  29.000  1.00 39.75           N  
-ATOM  31744  CA  GLU H 558      42.592  51.669  28.016  1.00 39.89           C  
-ATOM  31745  C   GLU H 558      41.437  50.784  28.482  1.00 41.50           C  
-ATOM  31746  O   GLU H 558      40.503  50.519  27.725  1.00 42.55           O  
-ATOM  31747  CB  GLU H 558      43.846  50.833  27.747  1.00 34.59           C  
-ATOM  31748  CG  GLU H 558      43.962  50.369  26.315  1.00 49.78           C  
-ATOM  31749  CD  GLU H 558      43.953  51.529  25.333  1.00 58.01           C  
-ATOM  31750  OE1 GLU H 558      44.757  52.468  25.515  1.00 44.90           O  
-ATOM  31751  OE2 GLU H 558      43.136  51.511  24.386  1.00 61.52           O  
-ATOM  31752  N   ALA H 559      41.503  50.349  29.737  1.00 39.48           N  
-ATOM  31753  CA  ALA H 559      40.463  49.513  30.321  1.00 37.86           C  
-ATOM  31754  C   ALA H 559      39.113  50.220  30.286  1.00 41.40           C  
-ATOM  31755  O   ALA H 559      38.089  49.607  29.993  1.00 36.53           O  
-ATOM  31756  CB  ALA H 559      40.827  49.134  31.747  1.00 33.53           C  
-ATOM  31757  N   LEU H 560      39.122  51.516  30.582  1.00 44.14           N  
-ATOM  31758  CA  LEU H 560      37.906  52.314  30.547  1.00 32.43           C  
-ATOM  31759  C   LEU H 560      37.380  52.445  29.129  1.00 34.53           C  
-ATOM  31760  O   LEU H 560      36.172  52.513  28.912  1.00 43.39           O  
-ATOM  31761  CB  LEU H 560      38.156  53.698  31.141  1.00 24.30           C  
-ATOM  31762  CG  LEU H 560      38.347  53.704  32.655  1.00 21.96           C  
-ATOM  31763  CD1 LEU H 560      38.520  55.112  33.174  1.00 19.59           C  
-ATOM  31764  CD2 LEU H 560      37.165  53.035  33.317  1.00 29.59           C  
-ATOM  31765  N   LYS H 561      38.293  52.492  28.167  1.00 35.63           N  
-ATOM  31766  CA  LYS H 561      37.906  52.572  26.768  1.00 36.82           C  
-ATOM  31767  C   LYS H 561      37.276  51.257  26.344  1.00 38.79           C  
-ATOM  31768  O   LYS H 561      36.410  51.221  25.469  1.00 37.25           O  
-ATOM  31769  CB  LYS H 561      39.110  52.917  25.892  1.00 39.13           C  
-ATOM  31770  CG  LYS H 561      39.474  54.393  25.934  1.00 35.65           C  
-ATOM  31771  CD  LYS H 561      40.869  54.670  25.393  1.00 46.63           C  
-ATOM  31772  CE  LYS H 561      40.986  54.323  23.917  1.00 62.67           C  
-ATOM  31773  NZ  LYS H 561      42.360  54.588  23.405  1.00 46.94           N  
-ATOM  31774  N   GLU H 562      37.713  50.176  26.979  1.00 36.60           N  
-ATOM  31775  CA  GLU H 562      37.091  48.881  26.768  1.00 37.56           C  
-ATOM  31776  C   GLU H 562      35.694  48.879  27.377  1.00 37.86           C  
-ATOM  31777  O   GLU H 562      34.749  48.371  26.779  1.00 34.08           O  
-ATOM  31778  CB  GLU H 562      37.944  47.761  27.373  1.00 40.15           C  
-ATOM  31779  CG  GLU H 562      39.077  47.263  26.480  1.00 56.99           C  
-ATOM  31780  CD  GLU H 562      38.623  46.234  25.455  1.00 66.92           C  
-ATOM  31781  OE1 GLU H 562      37.555  46.425  24.833  1.00 62.94           O  
-ATOM  31782  OE2 GLU H 562      39.339  45.225  25.273  1.00 71.09           O  
-ATOM  31783  N   GLN H 563      35.574  49.463  28.566  1.00 44.77           N  
-ATOM  31784  CA  GLN H 563      34.312  49.504  29.297  1.00 30.26           C  
-ATOM  31785  C   GLN H 563      33.271  50.344  28.567  1.00 28.67           C  
-ATOM  31786  O   GLN H 563      32.076  50.060  28.637  1.00 37.51           O  
-ATOM  31787  CB  GLN H 563      34.531  50.052  30.714  1.00 23.18           C  
-ATOM  31788  CG  GLN H 563      33.308  49.939  31.628  1.00 25.20           C  
-ATOM  31789  CD  GLN H 563      33.578  50.414  33.049  1.00 23.81           C  
-ATOM  31790  OE1 GLN H 563      34.711  50.742  33.405  1.00 22.95           O  
-ATOM  31791  NE2 GLN H 563      32.532  50.452  33.867  1.00 16.53           N  
-ATOM  31792  N   LEU H 564      33.727  51.371  27.860  1.00 25.61           N  
-ATOM  31793  CA  LEU H 564      32.818  52.304  27.204  1.00 24.27           C  
-ATOM  31794  C   LEU H 564      32.171  51.697  25.966  1.00 33.25           C  
-ATOM  31795  O   LEU H 564      31.222  52.260  25.420  1.00 45.63           O  
-ATOM  31796  CB  LEU H 564      33.546  53.597  26.825  1.00 36.03           C  
-ATOM  31797  CG  LEU H 564      33.837  54.638  27.913  1.00 27.38           C  
-ATOM  31798  CD1 LEU H 564      33.191  55.962  27.555  1.00 25.95           C  
-ATOM  31799  CD2 LEU H 564      33.375  54.182  29.287  1.00 32.30           C  
-ATOM  31800  N   ARG H 565      32.684  50.554  25.522  1.00 29.95           N  
-ATOM  31801  CA  ARG H 565      32.107  49.859  24.376  1.00 33.55           C  
-ATOM  31802  C   ARG H 565      31.007  48.901  24.823  1.00 32.96           C  
-ATOM  31803  O   ARG H 565      30.418  48.183  24.010  1.00 30.87           O  
-ATOM  31804  CB  ARG H 565      33.184  49.101  23.602  1.00 29.24           C  
-ATOM  31805  CG  ARG H 565      34.228  49.998  22.965  1.00 32.85           C  
-ATOM  31806  CD  ARG H 565      35.169  49.200  22.080  1.00 36.12           C  
-ATOM  31807  NE  ARG H 565      36.237  50.031  21.530  1.00 59.59           N  
-ATOM  31808  CZ  ARG H 565      37.457  50.120  22.051  1.00 62.76           C  
-ATOM  31809  NH1 ARG H 565      37.767  49.425  23.137  1.00 52.84           N  
-ATOM  31810  NH2 ARG H 565      38.368  50.901  21.484  1.00 54.78           N  
-ATOM  31811  N   ARG H 566      30.732  48.904  26.124  1.00 27.42           N  
-ATOM  31812  CA  ARG H 566      29.734  48.018  26.706  1.00 24.47           C  
-ATOM  31813  C   ARG H 566      28.410  48.734  26.950  1.00 25.17           C  
-ATOM  31814  O   ARG H 566      28.356  49.742  27.653  1.00 24.31           O  
-ATOM  31815  CB  ARG H 566      30.252  47.428  28.019  1.00 22.94           C  
-ATOM  31816  CG  ARG H 566      31.528  46.611  27.884  1.00 27.14           C  
-ATOM  31817  CD  ARG H 566      31.951  46.040  29.228  1.00 31.15           C  
-ATOM  31818  NE  ARG H 566      33.090  45.133  29.123  1.00 33.95           N  
-ATOM  31819  CZ  ARG H 566      33.593  44.448  30.146  1.00 37.42           C  
-ATOM  31820  NH1 ARG H 566      34.630  43.642  29.965  1.00 38.69           N  
-ATOM  31821  NH2 ARG H 566      33.058  44.570  31.353  1.00 37.13           N  
-ATOM  31822  N   GLU H 567      27.343  48.203  26.366  1.00 25.16           N  
-ATOM  31823  CA  GLU H 567      26.005  48.727  26.606  1.00 24.17           C  
-ATOM  31824  C   GLU H 567      25.484  48.261  27.961  1.00 21.85           C  
-ATOM  31825  O   GLU H 567      25.553  47.076  28.288  1.00 25.74           O  
-ATOM  31826  CB  GLU H 567      25.048  48.299  25.492  1.00 24.93           C  
-ATOM  31827  CG  GLU H 567      25.479  47.041  24.761  1.00 34.75           C  
-ATOM  31828  CD  GLU H 567      26.035  47.339  23.386  1.00 39.08           C  
-ATOM  31829  OE1 GLU H 567      26.802  46.506  22.858  1.00 48.19           O  
-ATOM  31830  OE2 GLU H 567      25.699  48.406  22.831  1.00 35.60           O  
-ATOM  31831  N   PRO H 568      24.957  49.202  28.754  1.00 17.49           N  
-ATOM  31832  CA  PRO H 568      24.483  48.932  30.113  1.00 19.66           C  
-ATOM  31833  C   PRO H 568      23.309  47.963  30.148  1.00 25.00           C  
-ATOM  31834  O   PRO H 568      22.496  47.940  29.224  1.00 30.22           O  
-ATOM  31835  CB  PRO H 568      24.048  50.313  30.615  1.00 19.60           C  
-ATOM  31836  CG  PRO H 568      24.730  51.287  29.716  1.00 22.40           C  
-ATOM  31837  CD  PRO H 568      24.791  50.616  28.389  1.00 17.44           C  
-ATOM  31838  N   ARG H 569      23.232  47.171  31.212  1.00 29.49           N  
-ATOM  31839  CA  ARG H 569      22.100  46.280  31.432  1.00 29.00           C  
-ATOM  31840  C   ARG H 569      21.178  46.867  32.504  1.00 24.75           C  
-ATOM  31841  O   ARG H 569      21.564  47.806  33.201  1.00 26.17           O  
-ATOM  31842  CB  ARG H 569      22.590  44.886  31.834  1.00 29.64           C  
-ATOM  31843  CG  ARG H 569      23.590  44.291  30.858  1.00 34.79           C  
-ATOM  31844  CD  ARG H 569      23.265  42.843  30.521  1.00 32.23           C  
-ATOM  31845  NE  ARG H 569      24.151  42.329  29.481  1.00 34.62           N  
-ATOM  31846  CZ  ARG H 569      25.345  41.796  29.715  1.00 30.60           C  
-ATOM  31847  NH1 ARG H 569      26.087  41.357  28.707  1.00 30.83           N  
-ATOM  31848  NH2 ARG H 569      25.798  41.703  30.957  1.00 33.06           N  
-ATOM  31849  N   PRO H 570      19.945  46.345  32.614  1.00 21.15           N  
-ATOM  31850  CA  PRO H 570      19.024  46.780  33.667  1.00 18.24           C  
-ATOM  31851  C   PRO H 570      19.657  46.800  35.054  1.00 19.47           C  
-ATOM  31852  O   PRO H 570      20.334  45.846  35.437  1.00 22.87           O  
-ATOM  31853  CB  PRO H 570      17.908  45.730  33.614  1.00 19.93           C  
-ATOM  31854  CG  PRO H 570      18.021  45.070  32.272  1.00 26.30           C  
-ATOM  31855  CD  PRO H 570      19.244  45.583  31.569  1.00 28.03           C  
-ATOM  31856  N   PHE H 571      19.449  47.891  35.784  1.00 21.64           N  
-ATOM  31857  CA  PHE H 571      19.818  47.947  37.189  1.00 16.97           C  
-ATOM  31858  C   PHE H 571      19.061  46.871  37.954  1.00 18.76           C  
-ATOM  31859  O   PHE H 571      17.899  46.594  37.657  1.00 15.78           O  
-ATOM  31860  CB  PHE H 571      19.509  49.324  37.783  1.00 22.77           C  
-ATOM  31861  CG  PHE H 571      20.530  50.375  37.457  1.00 19.75           C  
-ATOM  31862  CD1 PHE H 571      21.848  50.033  37.210  1.00 20.77           C  
-ATOM  31863  CD2 PHE H 571      20.168  51.711  37.405  1.00 21.85           C  
-ATOM  31864  CE1 PHE H 571      22.787  51.005  36.915  1.00 21.10           C  
-ATOM  31865  CE2 PHE H 571      21.100  52.686  37.111  1.00 22.49           C  
-ATOM  31866  CZ  PHE H 571      22.410  52.332  36.865  1.00 23.42           C  
-ATOM  31867  N   PRO H 572      19.721  46.250  38.938  1.00 23.57           N  
-ATOM  31868  CA  PRO H 572      19.026  45.317  39.827  1.00 21.92           C  
-ATOM  31869  C   PRO H 572      18.234  46.089  40.874  1.00 24.80           C  
-ATOM  31870  O   PRO H 572      18.328  47.317  40.914  1.00 26.14           O  
-ATOM  31871  CB  PRO H 572      20.168  44.535  40.471  1.00 17.00           C  
-ATOM  31872  CG  PRO H 572      21.282  45.525  40.524  1.00 18.84           C  
-ATOM  31873  CD  PRO H 572      21.150  46.369  39.275  1.00 18.23           C  
-ATOM  31874  N   ILE H 573      17.459  45.401  41.704  1.00 26.31           N  
-ATOM  31875  CA  ILE H 573      16.881  46.065  42.865  1.00 24.20           C  
-ATOM  31876  C   ILE H 573      17.486  45.443  44.117  1.00 19.44           C  
-ATOM  31877  O   ILE H 573      17.714  44.234  44.179  1.00 15.65           O  
-ATOM  31878  CB  ILE H 573      15.322  45.988  42.896  1.00 17.58           C  
-ATOM  31879  CG1 ILE H 573      14.823  44.772  43.671  1.00 24.62           C  
-ATOM  31880  CG2 ILE H 573      14.741  46.012  41.492  1.00 18.07           C  
-ATOM  31881  CD1 ILE H 573      13.316  44.723  43.808  1.00 41.13           C  
-ATOM  31882  N   VAL H 574      17.792  46.284  45.097  1.00 17.53           N  
-ATOM  31883  CA  VAL H 574      18.325  45.804  46.364  1.00 14.36           C  
-ATOM  31884  C   VAL H 574      17.212  45.755  47.399  1.00 13.17           C  
-ATOM  31885  O   VAL H 574      16.596  46.773  47.712  1.00 12.87           O  
-ATOM  31886  CB  VAL H 574      19.471  46.693  46.879  1.00 11.94           C  
-ATOM  31887  CG1 VAL H 574      19.790  46.371  48.325  1.00 16.47           C  
-ATOM  31888  CG2 VAL H 574      20.702  46.521  46.010  1.00 13.52           C  
-ATOM  31889  N   ASN H 575      16.945  44.564  47.921  1.00 13.34           N  
-ATOM  31890  CA  ASN H 575      15.915  44.412  48.938  1.00 17.53           C  
-ATOM  31891  C   ASN H 575      16.498  44.255  50.335  1.00 22.71           C  
-ATOM  31892  O   ASN H 575      17.472  43.525  50.544  1.00 22.30           O  
-ATOM  31893  CB  ASN H 575      15.016  43.220  48.614  1.00 15.93           C  
-ATOM  31894  CG  ASN H 575      14.158  43.463  47.400  1.00 16.64           C  
-ATOM  31895  OD1 ASN H 575      13.676  44.574  47.185  1.00 16.41           O  
-ATOM  31896  ND2 ASN H 575      13.966  42.429  46.590  1.00 18.60           N  
-ATOM  31897  N   ILE H 576      15.901  44.965  51.285  1.00 15.01           N  
-ATOM  31898  CA  ILE H 576      16.227  44.782  52.686  1.00 13.62           C  
-ATOM  31899  C   ILE H 576      15.398  43.627  53.224  1.00 17.39           C  
-ATOM  31900  O   ILE H 576      14.169  43.673  53.204  1.00 16.61           O  
-ATOM  31901  CB  ILE H 576      15.956  46.049  53.513  1.00 14.51           C  
-ATOM  31902  CG1 ILE H 576      16.844  47.196  53.036  1.00 12.07           C  
-ATOM  31903  CG2 ILE H 576      16.190  45.778  54.990  1.00 24.08           C  
-ATOM  31904  CD1 ILE H 576      16.665  48.460  53.834  1.00 17.38           C  
-ATOM  31905  N   LEU H 577      16.075  42.583  53.686  1.00 17.54           N  
-ATOM  31906  CA  LEU H 577      15.400  41.428  54.263  1.00 20.50           C  
-ATOM  31907  C   LEU H 577      15.176  41.652  55.756  1.00 28.57           C  
-ATOM  31908  O   LEU H 577      15.893  42.437  56.377  1.00 34.47           O  
-ATOM  31909  CB  LEU H 577      16.217  40.159  54.020  1.00 19.94           C  
-ATOM  31910  CG  LEU H 577      16.583  39.914  52.554  1.00 17.27           C  
-ATOM  31911  CD1 LEU H 577      17.766  38.966  52.434  1.00 25.54           C  
-ATOM  31912  CD2 LEU H 577      15.385  39.373  51.797  1.00 17.09           C  
-ATOM  31913  N   ASN H 578      14.180  40.972  56.320  1.00 25.67           N  
-ATOM  31914  CA  ASN H 578      13.863  41.088  57.746  1.00 33.91           C  
-ATOM  31915  C   ASN H 578      13.595  42.531  58.167  1.00 29.03           C  
-ATOM  31916  O   ASN H 578      14.137  43.008  59.168  1.00 25.43           O  
-ATOM  31917  CB  ASN H 578      14.996  40.507  58.594  1.00 30.44           C  
-ATOM  31918  CG  ASN H 578      15.596  39.256  57.985  1.00 31.98           C  
-ATOM  31919  OD1 ASN H 578      14.888  38.295  57.685  1.00 37.25           O  
-ATOM  31920  ND2 ASN H 578      16.908  39.269  57.788  1.00 28.45           N  
-ATOM  31921  N   LYS H 579      12.761  43.220  57.394  1.00 26.36           N  
-ATOM  31922  CA  LYS H 579      12.432  44.618  57.659  1.00 31.85           C  
-ATOM  31923  C   LYS H 579      11.733  44.783  59.002  1.00 28.95           C  
-ATOM  31924  O   LYS H 579      11.792  45.847  59.616  1.00 31.47           O  
-ATOM  31925  CB  LYS H 579      11.555  45.194  56.537  1.00 29.67           C  
-ATOM  31926  CG  LYS H 579      11.286  44.239  55.381  1.00 46.52           C  
-ATOM  31927  CD  LYS H 579      10.086  43.337  55.653  1.00 57.56           C  
-ATOM  31928  CE  LYS H 579       9.980  42.229  54.617  1.00 42.25           C  
-ATOM  31929  NZ  LYS H 579      11.162  41.319  54.647  1.00 35.32           N  
-ATOM  31930  N   GLU H 580      11.070  43.723  59.447  1.00 29.30           N  
-ATOM  31931  CA  GLU H 580      10.353  43.743  60.715  1.00 34.05           C  
-ATOM  31932  C   GLU H 580      11.314  43.864  61.891  1.00 27.81           C  
-ATOM  31933  O   GLU H 580      11.042  44.568  62.862  1.00 28.16           O  
-ATOM  31934  CB  GLU H 580       9.498  42.480  60.862  1.00 36.98           C  
-ATOM  31935  CG  GLU H 580       8.739  42.382  62.179  1.00 56.60           C  
-ATOM  31936  CD  GLU H 580       7.669  43.449  62.324  1.00 61.62           C  
-ATOM  31937  OE1 GLU H 580       7.323  43.791  63.475  1.00 56.53           O  
-ATOM  31938  OE2 GLU H 580       7.172  43.942  61.288  1.00 60.10           O  
-ATOM  31939  N   ARG H 581      12.446  43.180  61.787  1.00 26.19           N  
-ATOM  31940  CA  ARG H 581      13.398  43.102  62.886  1.00 25.38           C  
-ATOM  31941  C   ARG H 581      14.227  44.375  63.035  1.00 29.32           C  
-ATOM  31942  O   ARG H 581      14.692  44.699  64.129  1.00 32.23           O  
-ATOM  31943  CB  ARG H 581      14.325  41.901  62.688  1.00 24.99           C  
-ATOM  31944  CG  ARG H 581      15.267  41.660  63.849  1.00 28.67           C  
-ATOM  31945  CD  ARG H 581      16.190  40.481  63.597  1.00 29.50           C  
-ATOM  31946  NE  ARG H 581      16.929  40.609  62.344  1.00 31.76           N  
-ATOM  31947  CZ  ARG H 581      17.959  41.430  62.161  1.00 32.93           C  
-ATOM  31948  NH1 ARG H 581      18.373  42.216  63.148  1.00 30.43           N  
-ATOM  31949  NH2 ARG H 581      18.573  41.472  60.988  1.00 23.62           N  
-ATOM  31950  N   ILE H 582      14.406  45.096  61.933  1.00 32.38           N  
-ATOM  31951  CA  ILE H 582      15.299  46.250  61.915  1.00 23.77           C  
-ATOM  31952  C   ILE H 582      14.574  47.561  62.204  1.00 27.97           C  
-ATOM  31953  O   ILE H 582      13.780  48.038  61.393  1.00 27.52           O  
-ATOM  31954  CB  ILE H 582      16.017  46.359  60.563  1.00 21.79           C  
-ATOM  31955  CG1 ILE H 582      16.775  45.061  60.272  1.00 22.44           C  
-ATOM  31956  CG2 ILE H 582      16.953  47.554  60.553  1.00 21.19           C  
-ATOM  31957  CD1 ILE H 582      17.492  45.049  58.945  1.00 25.45           C  
-ATOM  31958  N   LYS H 583      14.862  48.144  63.365  1.00 27.86           N  
-ATOM  31959  CA  LYS H 583      14.208  49.379  63.785  1.00 29.78           C  
-ATOM  31960  C   LYS H 583      15.183  50.550  63.891  1.00 26.73           C  
-ATOM  31961  O   LYS H 583      14.778  51.710  63.807  1.00 23.41           O  
-ATOM  31962  CB  LYS H 583      13.502  49.173  65.126  1.00 31.69           C  
-ATOM  31963  CG  LYS H 583      12.477  48.051  65.119  1.00 29.02           C  
-ATOM  31964  CD  LYS H 583      11.756  47.973  66.455  1.00 52.64           C  
-ATOM  31965  CE  LYS H 583      10.696  46.880  66.458  1.00 69.44           C  
-ATOM  31966  NZ  LYS H 583       9.929  46.852  67.738  1.00 61.71           N  
-ATOM  31967  N   GLU H 584      16.463  50.246  64.084  1.00 28.38           N  
-ATOM  31968  CA  GLU H 584      17.488  51.281  64.158  1.00 21.48           C  
-ATOM  31969  C   GLU H 584      18.618  51.004  63.169  1.00 19.61           C  
-ATOM  31970  O   GLU H 584      18.787  49.878  62.703  1.00 23.82           O  
-ATOM  31971  CB  GLU H 584      18.037  51.393  65.585  1.00 23.28           C  
-ATOM  31972  CG  GLU H 584      16.975  51.656  66.650  1.00 26.48           C  
-ATOM  31973  CD  GLU H 584      16.328  53.022  66.515  1.00 26.99           C  
-ATOM  31974  OE1 GLU H 584      16.917  53.895  65.846  1.00 32.02           O  
-ATOM  31975  OE2 GLU H 584      15.230  53.224  67.077  1.00 33.25           O  
-ATOM  31976  N   ILE H 585      19.390  52.038  62.854  1.00 20.07           N  
-ATOM  31977  CA  ILE H 585      20.443  51.936  61.849  1.00 22.86           C  
-ATOM  31978  C   ILE H 585      21.525  50.925  62.246  1.00 21.72           C  
-ATOM  31979  O   ILE H 585      22.225  50.383  61.389  1.00 20.72           O  
-ATOM  31980  CB  ILE H 585      21.089  53.319  61.587  1.00 19.99           C  
-ATOM  31981  CG1 ILE H 585      22.020  53.271  60.372  1.00 19.48           C  
-ATOM  31982  CG2 ILE H 585      21.812  53.825  62.826  1.00 20.21           C  
-ATOM  31983  CD1 ILE H 585      21.314  52.940  59.078  1.00 14.99           C  
-ATOM  31984  N   ASP H 586      21.644  50.657  63.543  1.00 20.51           N  
-ATOM  31985  CA  ASP H 586      22.640  49.716  64.044  1.00 18.06           C  
-ATOM  31986  C   ASP H 586      22.183  48.270  63.879  1.00 20.99           C  
-ATOM  31987  O   ASP H 586      22.982  47.340  63.997  1.00 21.15           O  
-ATOM  31988  CB  ASP H 586      22.948  50.000  65.516  1.00 25.65           C  
-ATOM  31989  CG  ASP H 586      23.619  51.344  65.724  1.00 41.86           C  
-ATOM  31990  OD1 ASP H 586      24.584  51.649  64.990  1.00 34.00           O  
-ATOM  31991  OD2 ASP H 586      23.177  52.097  66.618  1.00 43.56           O  
-ATOM  31992  N   ASP H 587      20.897  48.087  63.597  1.00 18.03           N  
-ATOM  31993  CA  ASP H 587      20.306  46.753  63.566  1.00 14.88           C  
-ATOM  31994  C   ASP H 587      20.622  45.982  62.285  1.00 17.14           C  
-ATOM  31995  O   ASP H 587      20.381  44.777  62.208  1.00 23.97           O  
-ATOM  31996  CB  ASP H 587      18.790  46.848  63.752  1.00 17.28           C  
-ATOM  31997  CG  ASP H 587      18.399  47.257  65.161  1.00 24.31           C  
-ATOM  31998  OD1 ASP H 587      19.136  46.914  66.111  1.00 24.87           O  
-ATOM  31999  OD2 ASP H 587      17.352  47.918  65.320  1.00 31.41           O  
-ATOM  32000  N   PHE H 588      21.160  46.671  61.285  1.00 17.68           N  
-ATOM  32001  CA  PHE H 588      21.489  46.032  60.014  1.00 17.08           C  
-ATOM  32002  C   PHE H 588      22.690  45.101  60.142  1.00 18.67           C  
-ATOM  32003  O   PHE H 588      23.690  45.444  60.772  1.00 16.19           O  
-ATOM  32004  CB  PHE H 588      21.773  47.082  58.938  1.00 20.63           C  
-ATOM  32005  CG  PHE H 588      20.544  47.782  58.429  1.00 20.66           C  
-ATOM  32006  CD1 PHE H 588      19.829  47.267  57.362  1.00 20.14           C  
-ATOM  32007  CD2 PHE H 588      20.114  48.963  59.008  1.00 20.08           C  
-ATOM  32008  CE1 PHE H 588      18.702  47.911  56.889  1.00 15.35           C  
-ATOM  32009  CE2 PHE H 588      18.990  49.612  58.537  1.00 20.90           C  
-ATOM  32010  CZ  PHE H 588      18.282  49.084  57.477  1.00 15.67           C  
-ATOM  32011  N   THR H 589      22.583  43.920  59.542  1.00 19.43           N  
-ATOM  32012  CA  THR H 589      23.715  43.008  59.433  1.00 20.11           C  
-ATOM  32013  C   THR H 589      24.041  42.790  57.960  1.00 20.84           C  
-ATOM  32014  O   THR H 589      23.339  43.291  57.085  1.00 24.53           O  
-ATOM  32015  CB  THR H 589      23.436  41.655  60.106  1.00 27.93           C  
-ATOM  32016  OG1 THR H 589      22.474  40.924  59.336  1.00 30.32           O  
-ATOM  32017  CG2 THR H 589      22.905  41.861  61.517  1.00 27.37           C  
-ATOM  32018  N   ALA H 590      25.096  42.031  57.686  1.00 20.75           N  
-ATOM  32019  CA  ALA H 590      25.519  41.789  56.309  1.00 22.45           C  
-ATOM  32020  C   ALA H 590      24.655  40.732  55.633  1.00 18.08           C  
-ATOM  32021  O   ALA H 590      24.941  40.308  54.514  1.00 18.81           O  
-ATOM  32022  CB  ALA H 590      26.982  41.375  56.272  1.00 30.13           C  
-ATOM  32023  N   GLU H 591      23.594  40.314  56.315  1.00 19.78           N  
-ATOM  32024  CA  GLU H 591      22.735  39.248  55.818  1.00 21.20           C  
-ATOM  32025  C   GLU H 591      21.310  39.733  55.579  1.00 27.98           C  
-ATOM  32026  O   GLU H 591      20.426  38.940  55.251  1.00 30.33           O  
-ATOM  32027  CB  GLU H 591      22.722  38.076  56.802  1.00 22.96           C  
-ATOM  32028  CG  GLU H 591      24.093  37.692  57.336  1.00 32.71           C  
-ATOM  32029  CD  GLU H 591      24.999  37.103  56.273  1.00 32.22           C  
-ATOM  32030  OE1 GLU H 591      26.229  37.303  56.369  1.00 25.92           O  
-ATOM  32031  OE2 GLU H 591      24.485  36.433  55.350  1.00 35.36           O  
-ATOM  32032  N   ASP H 592      21.087  41.033  55.743  1.00 27.23           N  
-ATOM  32033  CA  ASP H 592      19.751  41.599  55.581  1.00 25.84           C  
-ATOM  32034  C   ASP H 592      19.555  42.253  54.217  1.00 23.24           C  
-ATOM  32035  O   ASP H 592      18.795  43.212  54.085  1.00 20.67           O  
-ATOM  32036  CB  ASP H 592      19.470  42.620  56.683  1.00 19.04           C  
-ATOM  32037  CG  ASP H 592      19.567  42.020  58.069  1.00 32.38           C  
-ATOM  32038  OD1 ASP H 592      18.656  41.254  58.450  1.00 37.37           O  
-ATOM  32039  OD2 ASP H 592      20.551  42.317  58.778  1.00 36.71           O  
-ATOM  32040  N   PHE H 593      20.237  41.731  53.204  1.00 20.27           N  
-ATOM  32041  CA  PHE H 593      20.143  42.291  51.862  1.00 19.57           C  
-ATOM  32042  C   PHE H 593      20.161  41.214  50.792  1.00 27.20           C  
-ATOM  32043  O   PHE H 593      20.925  40.251  50.880  1.00 30.66           O  
-ATOM  32044  CB  PHE H 593      21.289  43.271  51.603  1.00 16.11           C  
-ATOM  32045  CG  PHE H 593      21.285  44.465  52.507  1.00 15.52           C  
-ATOM  32046  CD1 PHE H 593      20.504  45.570  52.216  1.00 17.51           C  
-ATOM  32047  CD2 PHE H 593      22.071  44.487  53.645  1.00 15.38           C  
-ATOM  32048  CE1 PHE H 593      20.501  46.671  53.048  1.00 16.85           C  
-ATOM  32049  CE2 PHE H 593      22.073  45.584  54.482  1.00 17.55           C  
-ATOM  32050  CZ  PHE H 593      21.288  46.678  54.183  1.00 21.33           C  
-ATOM  32051  N   GLU H 594      19.315  41.379  49.781  1.00 24.50           N  
-ATOM  32052  CA  GLU H 594      19.428  40.566  48.579  1.00 19.24           C  
-ATOM  32053  C   GLU H 594      19.560  41.478  47.368  1.00 18.66           C  
-ATOM  32054  O   GLU H 594      18.874  42.496  47.259  1.00 17.98           O  
-ATOM  32055  CB  GLU H 594      18.235  39.614  48.424  1.00 17.09           C  
-ATOM  32056  CG  GLU H 594      16.878  40.274  48.226  1.00 29.88           C  
-ATOM  32057  CD  GLU H 594      15.771  39.260  47.973  1.00 34.90           C  
-ATOM  32058  OE1 GLU H 594      14.579  39.628  48.076  1.00 21.64           O  
-ATOM  32059  OE2 GLU H 594      16.097  38.092  47.670  1.00 29.72           O  
-ATOM  32060  N   VAL H 595      20.478  41.125  46.477  1.00 21.08           N  
-ATOM  32061  CA  VAL H 595      20.643  41.856  45.233  1.00 15.23           C  
-ATOM  32062  C   VAL H 595      19.945  41.083  44.127  1.00 16.68           C  
-ATOM  32063  O   VAL H 595      20.429  40.049  43.670  1.00 18.35           O  
-ATOM  32064  CB  VAL H 595      22.119  42.072  44.882  1.00 13.51           C  
-ATOM  32065  CG1 VAL H 595      22.245  42.674  43.496  1.00 22.35           C  
-ATOM  32066  CG2 VAL H 595      22.771  42.972  45.914  1.00 12.65           C  
-ATOM  32067  N   VAL H 596      18.795  41.597  43.712  1.00 19.75           N  
-ATOM  32068  CA  VAL H 596      17.906  40.887  42.808  1.00 18.12           C  
-ATOM  32069  C   VAL H 596      18.010  41.389  41.369  1.00 28.39           C  
-ATOM  32070  O   VAL H 596      17.770  42.567  41.089  1.00 35.30           O  
-ATOM  32071  CB  VAL H 596      16.445  41.004  43.289  1.00 14.69           C  
-ATOM  32072  CG1 VAL H 596      15.481  40.638  42.184  1.00 15.44           C  
-ATOM  32073  CG2 VAL H 596      16.224  40.138  44.521  1.00 14.71           C  
-ATOM  32074  N   GLY H 597      18.374  40.486  40.462  1.00 17.99           N  
-ATOM  32075  CA  GLY H 597      18.388  40.779  39.041  1.00 18.14           C  
-ATOM  32076  C   GLY H 597      19.642  41.473  38.546  1.00 22.25           C  
-ATOM  32077  O   GLY H 597      19.588  42.270  37.611  1.00 26.59           O  
-ATOM  32078  N   TYR H 598      20.778  41.169  39.164  1.00 24.48           N  
-ATOM  32079  CA  TYR H 598      22.038  41.785  38.763  1.00 25.03           C  
-ATOM  32080  C   TYR H 598      22.718  40.970  37.670  1.00 18.45           C  
-ATOM  32081  O   TYR H 598      23.206  39.871  37.921  1.00 24.92           O  
-ATOM  32082  CB  TYR H 598      22.966  41.940  39.971  1.00 26.43           C  
-ATOM  32083  CG  TYR H 598      24.172  42.814  39.720  1.00 19.25           C  
-ATOM  32084  CD1 TYR H 598      24.062  43.985  38.980  1.00 25.95           C  
-ATOM  32085  CD2 TYR H 598      25.417  42.480  40.237  1.00 18.01           C  
-ATOM  32086  CE1 TYR H 598      25.159  44.795  38.751  1.00 25.24           C  
-ATOM  32087  CE2 TYR H 598      26.522  43.283  40.013  1.00 28.62           C  
-ATOM  32088  CZ  TYR H 598      26.386  44.441  39.269  1.00 31.15           C  
-ATOM  32089  OH  TYR H 598      27.479  45.248  39.041  1.00 25.81           O  
-ATOM  32090  N   VAL H 599      22.737  41.513  36.455  1.00 21.50           N  
-ATOM  32091  CA  VAL H 599      23.362  40.846  35.314  1.00 18.69           C  
-ATOM  32092  C   VAL H 599      24.405  41.750  34.650  1.00 27.83           C  
-ATOM  32093  O   VAL H 599      24.130  42.372  33.624  1.00 33.72           O  
-ATOM  32094  CB  VAL H 599      22.315  40.429  34.259  1.00 16.56           C  
-ATOM  32095  CG1 VAL H 599      22.920  39.449  33.262  1.00 31.11           C  
-ATOM  32096  CG2 VAL H 599      21.095  39.820  34.928  1.00 23.52           C  
-ATOM  32097  N   PRO H 600      25.609  41.829  35.239  1.00 23.23           N  
-ATOM  32098  CA  PRO H 600      26.649  42.740  34.754  1.00 22.92           C  
-ATOM  32099  C   PRO H 600      27.598  42.114  33.736  1.00 29.06           C  
-ATOM  32100  O   PRO H 600      27.598  40.896  33.551  1.00 31.92           O  
-ATOM  32101  CB  PRO H 600      27.405  43.087  36.032  1.00 21.97           C  
-ATOM  32102  CG  PRO H 600      27.327  41.831  36.837  1.00 20.06           C  
-ATOM  32103  CD  PRO H 600      26.000  41.184  36.505  1.00 25.22           C  
-ATOM  32104  N   HIS H 601      28.399  42.948  33.080  1.00 26.05           N  
-ATOM  32105  CA  HIS H 601      29.467  42.450  32.226  1.00 26.49           C  
-ATOM  32106  C   HIS H 601      30.599  41.931  33.101  1.00 32.56           C  
-ATOM  32107  O   HIS H 601      30.530  42.011  34.329  1.00 32.35           O  
-ATOM  32108  CB  HIS H 601      29.975  43.539  31.281  1.00 29.65           C  
-ATOM  32109  CG  HIS H 601      28.979  43.957  30.244  1.00 29.40           C  
-ATOM  32110  ND1 HIS H 601      28.905  43.365  29.001  1.00 35.15           N  
-ATOM  32111  CD2 HIS H 601      28.018  44.911  30.264  1.00 24.80           C  
-ATOM  32112  CE1 HIS H 601      27.941  43.935  28.301  1.00 30.70           C  
-ATOM  32113  NE2 HIS H 601      27.387  44.876  29.044  1.00 23.98           N  
-ATOM  32114  N   GLY H 602      31.641  41.401  32.471  1.00 33.85           N  
-ATOM  32115  CA  GLY H 602      32.755  40.829  33.205  1.00 45.59           C  
-ATOM  32116  C   GLY H 602      33.519  41.858  34.015  1.00 42.60           C  
-ATOM  32117  O   GLY H 602      33.460  43.053  33.726  1.00 43.83           O  
-ATOM  32118  N   ARG H 603      34.236  41.393  35.035  1.00 43.41           N  
-ATOM  32119  CA  ARG H 603      35.061  42.274  35.854  1.00 36.34           C  
-ATOM  32120  C   ARG H 603      36.196  42.857  35.023  1.00 34.85           C  
-ATOM  32121  O   ARG H 603      36.816  42.149  34.231  1.00 31.16           O  
-ATOM  32122  CB  ARG H 603      35.632  41.523  37.060  1.00 49.01           C  
-ATOM  32123  CG  ARG H 603      34.632  40.636  37.784  1.00 58.88           C  
-ATOM  32124  CD  ARG H 603      35.214  40.103  39.082  1.00 49.06           C  
-ATOM  32125  NE  ARG H 603      35.015  41.034  40.191  1.00 81.33           N  
-ATOM  32126  CZ  ARG H 603      34.275  40.771  41.265  1.00 77.91           C  
-ATOM  32127  NH1 ARG H 603      34.143  41.679  42.225  1.00 42.07           N  
-ATOM  32128  NH2 ARG H 603      33.671  39.594  41.384  1.00 63.55           N  
-ATOM  32129  N   ILE H 604      36.460  44.147  35.200  1.00 42.86           N  
-ATOM  32130  CA  ILE H 604      37.581  44.791  34.524  1.00 44.50           C  
-ATOM  32131  C   ILE H 604      38.635  45.227  35.534  1.00 42.61           C  
-ATOM  32132  O   ILE H 604      38.402  46.132  36.335  1.00 47.36           O  
-ATOM  32133  CB  ILE H 604      37.138  46.013  33.703  1.00 44.29           C  
-ATOM  32134  CG1 ILE H 604      36.050  45.623  32.701  1.00 41.67           C  
-ATOM  32135  CG2 ILE H 604      38.334  46.622  32.986  1.00 41.06           C  
-ATOM  32136  CD1 ILE H 604      35.618  46.763  31.802  1.00 33.15           C  
-ATOM  32137  N   GLN H 605      39.796  44.583  35.480  1.00 45.21           N  
-ATOM  32138  CA  GLN H 605      40.847  44.797  36.469  1.00 56.41           C  
-ATOM  32139  C   GLN H 605      41.522  46.158  36.318  1.00 54.21           C  
-ATOM  32140  O   GLN H 605      41.958  46.532  35.228  1.00 43.27           O  
-ATOM  32141  CB  GLN H 605      41.891  43.679  36.374  1.00 57.77           C  
-ATOM  32142  CG  GLN H 605      42.644  43.412  37.671  1.00 68.27           C  
-ATOM  32143  CD  GLN H 605      44.031  44.027  37.691  1.00 65.60           C  
-ATOM  32144  OE1 GLN H 605      44.643  44.246  36.645  1.00 53.22           O  
-ATOM  32145  NE2 GLN H 605      44.537  44.306  38.888  1.00 55.98           N  
-ATOM  32146  N   MET H 606      41.595  46.894  37.424  1.00 54.15           N  
-ATOM  32147  CA  MET H 606      42.274  48.188  37.470  1.00 62.08           C  
-ATOM  32148  C   MET H 606      43.055  48.329  38.775  1.00 58.03           C  
-ATOM  32149  O   MET H 606      42.468  48.330  39.857  1.00 68.31           O  
-ATOM  32150  CB  MET H 606      41.272  49.338  37.332  1.00 56.95           C  
-ATOM  32151  CG  MET H 606      40.454  49.314  36.052  1.00 51.38           C  
-ATOM  32152  SD  MET H 606      39.183  50.591  36.011  1.00 47.59           S  
-ATOM  32153  CE  MET H 606      38.052  49.894  34.811  1.00 34.48           C  
-ATOM  32154  N   GLU H 607      44.375  48.449  38.670  1.00 53.53           N  
-ATOM  32155  CA  GLU H 607      45.232  48.516  39.852  1.00 63.47           C  
-ATOM  32156  C   GLU H 607      45.097  49.850  40.579  1.00 65.87           C  
-ATOM  32157  O   GLU H 607      45.092  50.916  39.960  1.00 54.35           O  
-ATOM  32158  CB  GLU H 607      46.698  48.266  39.478  1.00 67.48           C  
-ATOM  32159  CG  GLU H 607      47.252  49.191  38.406  1.00 82.20           C  
-ATOM  32160  CD  GLU H 607      46.901  48.734  37.002  1.00 96.43           C  
-ATOM  32161  OE1 GLU H 607      47.789  48.180  36.318  1.00 89.70           O  
-ATOM  32162  OE2 GLU H 607      45.738  48.927  36.585  1.00 82.84           O  
-ATOM  32163  N   MET H 608      44.995  49.775  41.902  1.00 74.72           N  
-ATOM  32164  CA  MET H 608      44.789  50.953  42.736  1.00 64.61           C  
-ATOM  32165  C   MET H 608      46.072  51.759  42.906  1.00 52.38           C  
-ATOM  32166  O   MET H 608      47.066  51.255  43.433  1.00 41.06           O  
-ATOM  32167  CB  MET H 608      44.251  50.544  44.111  1.00 65.17           C  
-ATOM  32168  CG  MET H 608      43.707  51.699  44.937  1.00 68.14           C  
-ATOM  32169  SD  MET H 608      44.149  51.599  46.685  1.00 47.91           S  
-ATOM  32170  CE  MET H 608      43.917  49.855  47.002  1.00 51.05           C  
-ATOM  32171  N   ALA H 609      46.042  53.012  42.460  1.00 55.39           N  
-ATOM  32172  CA  ALA H 609      47.159  53.926  42.671  1.00 50.28           C  
-ATOM  32173  C   ALA H 609      47.319  54.211  44.159  1.00 48.75           C  
-ATOM  32174  O   ALA H 609      46.564  54.996  44.736  1.00 52.66           O  
-ATOM  32175  CB  ALA H 609      46.949  55.217  41.897  1.00 43.09           C  
-ATOM  32176  N   VAL H 610      48.304  53.564  44.772  1.00 55.49           N  
-ATOM  32177  CA  VAL H 610      48.496  53.634  46.216  1.00 66.31           C  
-ATOM  32178  C   VAL H 610      48.924  55.026  46.671  1.00 60.67           C  
-ATOM  32179  O   VAL H 610      48.348  55.584  47.607  1.00 59.44           O  
-ATOM  32180  CB  VAL H 610      49.544  52.606  46.690  1.00 57.45           C  
-ATOM  32181  CG1 VAL H 610      49.676  52.640  48.205  1.00 53.93           C  
-ATOM  32182  CG2 VAL H 610      49.168  51.211  46.215  1.00 47.08           C  
-ATOM  32183  OXT VAL H 610      49.848  55.624  46.116  1.00 44.24           O  
-TER   32184      VAL H 610                                                      
-HETATM32185  N1  UMP A 701      -5.755  -7.316 -54.652  1.00 63.88           N  
-HETATM32186  C2  UMP A 701      -5.170  -7.310 -53.344  1.00 56.36           C  
-HETATM32187  N3  UMP A 701      -3.915  -7.669 -53.181  1.00 52.92           N  
-HETATM32188  C4  UMP A 701      -3.166  -8.045 -54.212  1.00 59.07           C  
-HETATM32189  C5  UMP A 701      -3.698  -8.069 -55.521  1.00 69.44           C  
-HETATM32190  C6  UMP A 701      -5.022  -7.695 -55.707  1.00 70.54           C  
-HETATM32191  O2  UMP A 701      -5.787  -6.974 -52.305  1.00 51.34           O  
-HETATM32192  O4  UMP A 701      -1.999  -8.373 -54.015  1.00 62.37           O  
-HETATM32193  C1' UMP A 701      -7.138  -6.938 -54.902  1.00 69.61           C  
-HETATM32194  C2' UMP A 701      -7.501  -5.527 -54.510  1.00 49.99           C  
-HETATM32195  C3' UMP A 701      -8.734  -5.253 -55.364  1.00 47.66           C  
-HETATM32196  C4' UMP A 701      -8.653  -6.248 -56.490  1.00 59.82           C  
-HETATM32197  O3' UMP A 701      -9.866  -5.703 -54.647  1.00 49.42           O  
-HETATM32198  O4' UMP A 701      -7.449  -7.008 -56.303  1.00 70.46           O  
-HETATM32199  C5' UMP A 701      -8.903  -5.670 -57.895  1.00 63.79           C  
-HETATM32200  O5' UMP A 701      -8.027  -4.675 -58.285  1.00 57.63           O  
-HETATM32201  P   UMP A 701      -8.498  -3.157 -58.657  1.00 51.27           P  
-HETATM32202  OP1 UMP A 701      -7.536  -2.916 -59.759  1.00 45.56           O  
-HETATM32203  OP2 UMP A 701      -8.252  -2.403 -57.345  1.00 30.93           O  
-HETATM32204  OP3 UMP A 701      -9.901  -3.092 -59.106  1.00 59.65           O  
-HETATM32205  CAG 1UG A 702      -3.013 -13.409 -54.048  1.00103.21           C  
-HETATM32206  CAE 1UG A 702      -2.450 -14.644 -53.888  1.00105.10           C  
-HETATM32207  CAJ 1UG A 702      -3.202 -15.738 -53.516  1.00105.69           C  
-HETATM32208  CAU 1UG A 702      -4.548 -15.634 -53.309  1.00 99.95           C  
-HETATM32209  CAI 1UG A 702      -5.198 -16.817 -52.943  1.00 93.06           C  
-HETATM32210  CAC 1UG A 702      -6.548 -16.793 -52.714  1.00 87.95           C  
-HETATM32211  CAD 1UG A 702      -7.159 -15.568 -52.874  1.00 89.29           C  
-HETATM32212  CAL 1UG A 702      -6.517 -14.372 -53.238  1.00 93.53           C  
-HETATM32213  CAX 1UG A 702      -5.152 -14.381 -53.473  1.00 95.98           C  
-HETATM32214  CAR 1UG A 702      -4.367 -13.254 -53.851  1.00 99.14           C  
-HETATM32215  SAP 1UG A 702      -4.856 -11.586 -54.122  1.00107.45           S  
-HETATM32216  CAS 1UG A 702      -4.783 -11.296 -55.954  1.00112.71           C  
-HETATM32217  CAY 1UG A 702      -5.878 -10.802 -56.585  1.00113.62           C  
-HETATM32218  CAZ 1UG A 702      -7.117 -10.440 -56.157  1.00103.32           C  
-HETATM32219  CAT 1UG A 702      -7.746 -10.427 -54.955  1.00 96.91           C  
-HETATM32220  OAB 1UG A 702      -7.216 -10.794 -53.909  1.00 92.86           O  
-HETATM32221  NAN 1UG A 702      -9.065  -9.983 -54.844  1.00 89.15           N  
-HETATM32222  CAQ 1UG A 702      -9.730  -9.554 -55.979  1.00 79.96           C  
-HETATM32223  NAA 1UG A 702     -10.981  -9.132 -55.876  1.00 72.22           N  
-HETATM32224  NAM 1UG A 702      -9.077  -9.581 -57.147  1.00 80.29           N  
-HETATM32225  CAW 1UG A 702      -7.804 -10.013 -57.234  1.00 95.54           C  
-HETATM32226  NAO 1UG A 702      -7.016 -10.106 -58.298  1.00103.08           N  
-HETATM32227  CAV 1UG A 702      -5.832 -10.586 -57.923  1.00115.52           C  
-HETATM32228  CAK 1UG A 702      -4.738 -10.841 -58.671  1.00115.78           C  
-HETATM32229  CAF 1UG A 702      -3.589 -11.346 -58.078  1.00110.88           C  
-HETATM32230  CAH 1UG A 702      -3.620 -11.571 -56.706  1.00113.52           C  
-HETATM32231  N1  FOL A 703       3.291 -23.276 -15.783  1.00 24.13           N  
-HETATM32232  C2  FOL A 703       3.838 -22.603 -16.821  1.00 24.52           C  
-HETATM32233  NA2 FOL A 703       3.152 -21.656 -17.486  1.00 32.49           N  
-HETATM32234  N3  FOL A 703       5.087 -22.815 -17.272  1.00 29.34           N  
-HETATM32235  C4  FOL A 703       5.905 -23.721 -16.724  1.00 41.00           C  
-HETATM32236  O4  FOL A 703       7.065 -23.958 -17.098  1.00 45.41           O  
-HETATM32237  C4A FOL A 703       5.393 -24.489 -15.601  1.00 38.42           C  
-HETATM32238  N5  FOL A 703       6.210 -25.406 -15.040  1.00 36.51           N  
-HETATM32239  C6  FOL A 703       5.744 -26.102 -14.025  1.00 49.61           C  
-HETATM32240  C7  FOL A 703       4.430 -25.833 -13.595  1.00 54.02           C  
-HETATM32241  N8  FOL A 703       3.549 -24.913 -14.126  1.00 33.67           N  
-HETATM32242  C8A FOL A 703       4.005 -24.208 -15.150  1.00 33.71           C  
-HETATM32243  C9  FOL A 703       6.633 -27.156 -13.353  1.00 52.20           C  
-HETATM32244  N10 FOL A 703       8.087 -27.031 -13.527  1.00 46.26           N  
-HETATM32245  C11 FOL A 703      10.489 -23.988 -11.988  1.00 36.66           C  
-HETATM32246  C12 FOL A 703       9.115 -23.836 -12.051  1.00 47.47           C  
-HETATM32247  C13 FOL A 703       8.309 -24.862 -12.566  1.00 45.30           C  
-HETATM32248  C14 FOL A 703       8.889 -26.040 -13.023  1.00 43.23           C  
-HETATM32249  C15 FOL A 703      10.276 -26.198 -12.965  1.00 31.90           C  
-HETATM32250  C16 FOL A 703      11.077 -25.173 -12.450  1.00 30.91           C  
-HETATM32251  C   FOL A 703      11.253 -22.818 -11.428  1.00 56.64           C  
-HETATM32252  O   FOL A 703      12.396 -22.939 -11.027  1.00 57.59           O  
-HETATM32253  N   FOL A 703      10.631 -21.636 -11.411  1.00 67.20           N  
-HETATM32254  CA  FOL A 703      11.155 -20.355 -10.946  1.00 69.21           C  
-HETATM32255  CB  FOL A 703      11.270 -19.393 -12.142  1.00 59.91           C  
-HETATM32256  CG  FOL A 703      12.632 -18.760 -12.347  1.00 61.39           C  
-HETATM32257  CD  FOL A 703      12.414 -17.270 -12.617  1.00 66.94           C  
-HETATM32258  OE1 FOL A 703      12.382 -16.816 -13.803  1.00 48.97           O  
-HETATM32259  OE2 FOL A 703      12.254 -16.507 -11.628  1.00 89.39           O  
-HETATM32260  CT  FOL A 703      10.238 -19.748  -9.908  1.00 58.53           C  
-HETATM32261  O1  FOL A 703      10.781 -19.181  -8.931  1.00 61.03           O  
-HETATM32262  O2  FOL A 703       8.979 -19.809 -10.041  1.00 44.26           O  
-HETATM32263  PA  NDP A 704       1.512 -35.151 -11.042  1.00 24.89           P  
-HETATM32264  O1A NDP A 704       0.078 -34.960 -11.211  1.00 27.94           O  
-HETATM32265  O2A NDP A 704       2.385 -33.996 -10.824  1.00 28.34           O  
-HETATM32266  O5B NDP A 704       1.778 -36.184  -9.871  1.00 34.42           O  
-HETATM32267  C5B NDP A 704       1.094 -37.450  -9.815  1.00 40.57           C  
-HETATM32268  C4B NDP A 704       1.188 -37.927  -8.353  1.00 37.06           C  
-HETATM32269  O4B NDP A 704       0.611 -36.907  -7.478  1.00 37.87           O  
-HETATM32270  C3B NDP A 704       0.334 -39.156  -8.145  1.00 35.56           C  
-HETATM32271  O3B NDP A 704       1.137 -40.283  -8.402  1.00 37.94           O  
-HETATM32272  C2B NDP A 704      -0.138 -38.988  -6.706  1.00 36.07           C  
-HETATM32273  O2B NDP A 704       0.965 -39.165  -5.789  1.00 37.92           O  
-HETATM32274  C1B NDP A 704      -0.387 -37.484  -6.650  1.00 34.57           C  
-HETATM32275  N9A NDP A 704      -1.738 -37.082  -7.081  1.00 35.29           N  
-HETATM32276  C8A NDP A 704      -2.021 -36.315  -8.155  1.00 36.30           C  
-HETATM32277  N7A NDP A 704      -3.348 -36.112  -8.301  1.00 40.61           N  
-HETATM32278  C5A NDP A 704      -3.937 -36.767  -7.293  1.00 30.90           C  
-HETATM32279  C6A NDP A 704      -5.323 -36.965  -6.856  1.00 40.46           C  
-HETATM32280  N6A NDP A 704      -6.331 -36.401  -7.559  1.00 52.85           N  
-HETATM32281  N1A NDP A 704      -5.533 -37.719  -5.746  1.00 56.35           N  
-HETATM32282  C2A NDP A 704      -4.530 -38.281  -5.045  1.00 42.74           C  
-HETATM32283  N3A NDP A 704      -3.246 -38.131  -5.400  1.00 38.20           N  
-HETATM32284  C4A NDP A 704      -2.887 -37.402  -6.491  1.00 39.34           C  
-HETATM32285  O3  NDP A 704       2.183 -36.037 -12.211  1.00 30.16           O  
-HETATM32286  PN  NDP A 704       1.854 -35.978 -13.807  1.00 33.04           P  
-HETATM32287  O1N NDP A 704       0.423 -35.816 -14.140  1.00 24.75           O  
-HETATM32288  O2N NDP A 704       2.708 -37.053 -14.429  1.00 34.72           O  
-HETATM32289  O5D NDP A 704       2.598 -34.633 -14.225  1.00 28.43           O  
-HETATM32290  C5D NDP A 704       4.028 -34.567 -14.199  1.00 32.17           C  
-HETATM32291  C4D NDP A 704       4.485 -34.315 -15.626  1.00 35.68           C  
-HETATM32292  O4D NDP A 704       3.844 -33.115 -16.041  1.00 39.61           O  
-HETATM32293  C3D NDP A 704       5.957 -34.019 -15.694  1.00 26.59           C  
-HETATM32294  O3D NDP A 704       6.395 -34.343 -16.996  1.00 26.38           O  
-HETATM32295  C2D NDP A 704       6.004 -32.541 -15.503  1.00 23.87           C  
-HETATM32296  O2D NDP A 704       7.228 -32.016 -15.940  1.00 27.43           O  
-HETATM32297  C1D NDP A 704       4.823 -32.097 -16.296  1.00 33.00           C  
-HETATM32298  N1N NDP A 704       4.230 -30.837 -15.903  1.00 26.18           N  
-HETATM32299  C2N NDP A 704       4.063 -29.909 -16.854  1.00 28.70           C  
-HETATM32300  C3N NDP A 704       3.501 -28.678 -16.578  1.00 34.96           C  
-HETATM32301  C7N NDP A 704       3.338 -27.670 -17.688  1.00 29.97           C  
-HETATM32302  O7N NDP A 704       2.684 -26.671 -17.486  1.00 31.39           O  
-HETATM32303  N7N NDP A 704       3.921 -27.914 -18.859  1.00 21.86           N  
-HETATM32304  C4N NDP A 704       3.046 -28.336 -15.176  1.00 39.82           C  
-HETATM32305  C5N NDP A 704       3.286 -29.425 -14.249  1.00 30.54           C  
-HETATM32306  C6N NDP A 704       3.856 -30.608 -14.653  1.00 26.80           C  
-HETATM32307  P2B NDP A 704       1.438 -40.546  -5.161  1.00 37.35           P  
-HETATM32308  O1X NDP A 704       2.692 -40.147  -4.460  1.00 34.09           O  
-HETATM32309  O2X NDP A 704       0.258 -40.941  -4.322  1.00 26.99           O  
-HETATM32310  O3X NDP A 704       1.762 -41.551  -6.255  1.00 36.57           O  
-HETATM32311  N1  UMP B 701      12.294  17.252 -47.190  1.00 62.14           N  
-HETATM32312  C2  UMP B 701      10.961  17.229 -46.663  1.00 54.17           C  
-HETATM32313  N3  UMP B 701       9.949  17.618 -47.411  1.00 58.50           N  
-HETATM32314  C4  UMP B 701      10.135  18.038 -48.660  1.00 58.49           C  
-HETATM32315  C5  UMP B 701      11.434  18.078 -49.222  1.00 71.01           C  
-HETATM32316  C6  UMP B 701      12.509  17.674 -48.443  1.00 70.09           C  
-HETATM32317  O2  UMP B 701      10.678  16.852 -45.500  1.00 42.77           O  
-HETATM32318  O4  UMP B 701       9.166  18.393 -49.326  1.00 55.20           O  
-HETATM32319  C1' UMP B 701      13.462  16.843 -46.427  1.00 61.21           C  
-HETATM32320  C2' UMP B 701      13.420  15.426 -45.902  1.00 47.19           C  
-HETATM32321  C3' UMP B 701      14.890  15.049 -45.850  1.00 39.07           C  
-HETATM32322  C4' UMP B 701      15.471  15.778 -47.023  1.00 40.11           C  
-HETATM32323  O3' UMP B 701      15.466  15.729 -44.758  1.00 38.64           O  
-HETATM32324  O4' UMP B 701      14.640  16.929 -47.258  1.00 64.92           O  
-HETATM32325  C5' UMP B 701      15.808  14.913 -48.249  1.00 34.41           C  
-HETATM32326  O5' UMP B 701      17.024  14.253 -48.212  1.00 34.87           O  
-HETATM32327  P   UMP B 701      17.151  12.685 -48.662  1.00 44.61           P  
-HETATM32328  OP1 UMP B 701      17.062  12.889 -50.125  1.00 50.91           O  
-HETATM32329  OP2 UMP B 701      15.918  12.073 -47.989  1.00 26.59           O  
-HETATM32330  OP3 UMP B 701      18.426  12.069 -48.242  1.00 42.98           O  
-HETATM32331  CAG 1UG B 702       9.652  24.189 -46.159  1.00 92.19           C  
-HETATM32332  CAE 1UG B 702       9.468  25.449 -45.637  1.00 94.91           C  
-HETATM32333  CAJ 1UG B 702      10.529  26.302 -45.426  1.00 92.04           C  
-HETATM32334  CAU 1UG B 702      11.802  25.910 -45.733  1.00 86.11           C  
-HETATM32335  CAI 1UG B 702      12.803  26.856 -45.476  1.00 75.25           C  
-HETATM32336  CAC 1UG B 702      14.106  26.539 -45.757  1.00 75.81           C  
-HETATM32337  CAD 1UG B 702      14.321  25.283 -46.279  1.00 88.23           C  
-HETATM32338  CAL 1UG B 702      13.335  24.323 -46.543  1.00 88.42           C  
-HETATM32339  CAX 1UG B 702      12.012  24.624 -46.267  1.00 88.68           C  
-HETATM32340  CAR 1UG B 702      10.916  23.746 -46.495  1.00 87.03           C  
-HETATM32341  SAP 1UG B 702      10.857  22.094 -47.124  1.00 88.39           S  
-HETATM32342  CAS 1UG B 702      11.961  21.769 -48.578  1.00101.44           C  
-HETATM32343  CAY 1UG B 702      13.151  21.120 -48.411  1.00104.35           C  
-HETATM32344  CAZ 1UG B 702      13.822  20.620 -47.332  1.00 95.77           C  
-HETATM32345  CAT 1UG B 702      13.575  20.548 -45.999  1.00 89.14           C  
-HETATM32346  OAB 1UG B 702      12.554  20.992 -45.475  1.00 90.55           O  
-HETATM32347  NAN 1UG B 702      14.496  19.950 -45.128  1.00 83.60           N  
-HETATM32348  CAQ 1UG B 702      15.671  19.427 -45.644  1.00 74.35           C  
-HETATM32349  NAA 1UG B 702      16.554  18.857 -44.839  1.00 64.66           N  
-HETATM32350  NAM 1UG B 702      15.879  19.516 -46.962  1.00 81.54           N  
-HETATM32351  CAW 1UG B 702      14.980  20.095 -47.782  1.00 95.14           C  
-HETATM32352  NAO 1UG B 702      15.032  20.263 -49.097  1.00104.96           N  
-HETATM32353  CAV 1UG B 702      13.928  20.886 -49.502  1.00111.17           C  
-HETATM32354  CAK 1UG B 702      13.571  21.253 -50.752  1.00110.38           C  
-HETATM32355  CAF 1UG B 702      12.363  21.903 -50.976  1.00110.41           C  
-HETATM32356  CAH 1UG B 702      11.554  22.153 -49.874  1.00106.33           C  
-HETATM32357  N1  FOL B 703     -20.886  32.292 -25.205  1.00 34.55           N  
-HETATM32358  C2  FOL B 703     -20.535  31.714 -26.380  1.00 33.05           C  
-HETATM32359  NA2 FOL B 703     -19.534  30.819 -26.461  1.00 38.28           N  
-HETATM32360  N3  FOL B 703     -21.140  31.975 -27.552  1.00 34.52           N  
-HETATM32361  C4  FOL B 703     -22.155  32.839 -27.654  1.00 50.13           C  
-HETATM32362  O4  FOL B 703     -22.757  33.127 -28.700  1.00 59.56           O  
-HETATM32363  C4A FOL B 703     -22.592  33.500 -26.438  1.00 46.52           C  
-HETATM32364  N5  FOL B 703     -23.613  34.369 -26.539  1.00 50.02           N  
-HETATM32365  C6  FOL B 703     -24.018  34.974 -25.446  1.00 60.21           C  
-HETATM32366  C7  FOL B 703     -23.362  34.672 -24.237  1.00 57.92           C  
-HETATM32367  N8  FOL B 703     -22.311  33.795 -24.077  1.00 46.98           N  
-HETATM32368  C8A FOL B 703     -21.890  33.176 -25.173  1.00 40.31           C  
-HETATM32369  C9  FOL B 703     -25.180  35.965 -25.565  1.00 71.53           C  
-HETATM32370  N10 FOL B 703     -25.990  35.847 -26.784  1.00 52.58           N  
-HETATM32371  C11 FOL B 703     -28.918  32.942 -27.389  1.00 64.77           C  
-HETATM32372  C12 FOL B 703     -28.009  32.813 -26.352  1.00 64.91           C  
-HETATM32373  C13 FOL B 703     -27.030  33.793 -26.153  1.00 57.49           C  
-HETATM32374  C14 FOL B 703     -26.953  34.898 -26.993  1.00 50.80           C  
-HETATM32375  C15 FOL B 703     -27.860  35.035 -28.044  1.00 52.81           C  
-HETATM32376  C16 FOL B 703     -28.844  34.052 -28.244  1.00 63.10           C  
-HETATM32377  C   FOL B 703     -29.942  31.857 -27.564  1.00 75.96           C  
-HETATM32378  O   FOL B 703     -30.907  32.054 -28.277  1.00 87.03           O  
-HETATM32379  N   FOL B 703     -29.775  30.686 -26.945  1.00 76.61           N  
-HETATM32380  CA  FOL B 703     -30.692  29.551 -27.027  1.00 92.58           C  
-HETATM32381  CB  FOL B 703     -30.526  28.812 -28.379  1.00 79.90           C  
-HETATM32382  CG  FOL B 703     -29.359  27.829 -28.516  1.00 78.12           C  
-HETATM32383  CD  FOL B 703     -29.269  27.405 -29.986  1.00 80.30           C  
-HETATM32384  OE1 FOL B 703     -29.537  28.230 -30.913  1.00 86.99           O  
-HETATM32385  OE2 FOL B 703     -28.933  26.221 -30.243  1.00 72.97           O  
-HETATM32386  CT  FOL B 703     -30.516  28.610 -25.853  1.00 93.62           C  
-HETATM32387  O1  FOL B 703     -31.563  28.175 -25.324  1.00 87.25           O  
-HETATM32388  O2  FOL B 703     -29.369  28.287 -25.429  1.00 83.48           O  
-HETATM32389  PA  NDP B 704     -23.714  44.240 -20.477  1.00 64.36           P  
-HETATM32390  O1A NDP B 704     -22.643  43.538 -19.780  1.00 64.03           O  
-HETATM32391  O2A NDP B 704     -24.744  43.470 -21.181  1.00 47.59           O  
-HETATM32392  O5B NDP B 704     -24.470  45.210 -19.474  1.00 91.83           O  
-HETATM32393  C5B NDP B 704     -24.008  46.523 -19.097  1.00 91.70           C  
-HETATM32394  C4B NDP B 704     -25.132  47.028 -18.172  1.00 89.91           C  
-HETATM32395  O4B NDP B 704     -25.326  46.017 -17.132  1.00 83.84           O  
-HETATM32396  C3B NDP B 704     -24.761  48.298 -17.439  1.00101.57           C  
-HETATM32397  O3B NDP B 704     -25.213  49.402 -18.186  1.00100.78           O  
-HETATM32398  C2B NDP B 704     -25.360  48.107 -16.041  1.00110.01           C  
-HETATM32399  O2B NDP B 704     -26.792  48.364 -15.977  1.00105.70           O  
-HETATM32400  C1B NDP B 704     -25.212  46.600 -15.840  1.00100.64           C  
-HETATM32401  N9A NDP B 704     -23.931  46.240 -15.197  1.00 94.54           N  
-HETATM32402  C8A NDP B 704     -22.912  45.568 -15.777  1.00 91.94           C  
-HETATM32403  N7A NDP B 704     -21.872  45.393 -14.935  1.00 92.65           N  
-HETATM32404  C5A NDP B 704     -22.227  45.968 -13.781  1.00 90.19           C  
-HETATM32405  C6A NDP B 704     -21.588  46.145 -12.471  1.00 97.15           C  
-HETATM32406  N6A NDP B 704     -20.346  45.653 -12.256  1.00 92.26           N  
-HETATM32407  N1A NDP B 704     -22.287  46.807 -11.515  1.00105.78           N  
-HETATM32408  C2A NDP B 704     -23.522  47.298 -11.725  1.00108.59           C  
-HETATM32409  N3A NDP B 704     -24.152  47.165 -12.900  1.00100.71           N  
-HETATM32410  C4A NDP B 704     -23.573  46.524 -13.949  1.00 89.27           C  
-HETATM32411  O3  NDP B 704     -23.224  45.410 -21.478  1.00 69.33           O  
-HETATM32412  PN  NDP B 704     -21.982  45.387 -22.536  1.00 67.92           P  
-HETATM32413  O1N NDP B 704     -20.634  45.457 -21.938  1.00 51.33           O  
-HETATM32414  O2N NDP B 704     -22.404  46.318 -23.643  1.00 75.23           O  
-HETATM32415  O5D NDP B 704     -22.138  43.941 -23.193  1.00 61.68           O  
-HETATM32416  C5D NDP B 704     -23.099  43.723 -24.235  1.00 58.21           C  
-HETATM32417  C4D NDP B 704     -22.340  43.552 -25.540  1.00 41.69           C  
-HETATM32418  O4D NDP B 704     -21.634  42.323 -25.455  1.00 40.67           O  
-HETATM32419  C3D NDP B 704     -23.289  43.376 -26.691  1.00 42.43           C  
-HETATM32420  O3D NDP B 704     -22.623  43.799 -27.864  1.00 38.19           O  
-HETATM32421  C2D NDP B 704     -23.493  41.898 -26.733  1.00 39.71           C  
-HETATM32422  O2D NDP B 704     -24.038  41.496 -27.964  1.00 38.62           O  
-HETATM32423  C1D NDP B 704     -22.112  41.407 -26.452  1.00 39.05           C  
-HETATM32424  N1N NDP B 704     -22.015  40.080 -25.880  1.00 42.05           N  
-HETATM32425  C2N NDP B 704     -21.185  39.204 -26.465  1.00 38.13           C  
-HETATM32426  C3N NDP B 704     -21.025  37.918 -25.983  1.00 40.69           C  
-HETATM32427  C7N NDP B 704     -20.078  36.972 -26.680  1.00 35.03           C  
-HETATM32428  O7N NDP B 704     -19.806  35.911 -26.164  1.00 36.90           O  
-HETATM32429  N7N NDP B 704     -19.565  37.334 -27.851  1.00 40.29           N  
-HETATM32430  C4N NDP B 704     -21.786  37.454 -24.760  1.00 40.42           C  
-HETATM32431  C5N NDP B 704     -22.644  38.495 -24.229  1.00 45.67           C  
-HETATM32432  C6N NDP B 704     -22.714  39.742 -24.806  1.00 44.99           C  
-HETATM32433  P2B NDP B 704     -27.407  49.694 -15.350  1.00106.04           P  
-HETATM32434  O1X NDP B 704     -28.869  49.400 -15.359  1.00 96.92           O  
-HETATM32435  O2X NDP B 704     -26.696  49.790 -14.034  1.00 88.68           O  
-HETATM32436  O3X NDP B 704     -27.096  50.882 -16.247  1.00 87.57           O  
-HETATM32437  N1  UMP C 701     -19.631   9.572-142.934  1.00 72.74           N  
-HETATM32438  C2  UMP C 701     -20.214   9.565-141.624  1.00 63.08           C  
-HETATM32439  N3  UMP C 701     -21.468   9.930-141.459  1.00 65.57           N  
-HETATM32440  C4  UMP C 701     -22.216  10.311-142.491  1.00 70.86           C  
-HETATM32441  C5  UMP C 701     -21.686  10.333-143.801  1.00 80.51           C  
-HETATM32442  C6  UMP C 701     -20.364   9.954-143.989  1.00 81.14           C  
-HETATM32443  O2  UMP C 701     -19.595   9.224-140.588  1.00 49.26           O  
-HETATM32444  O4  UMP C 701     -23.381  10.645-142.296  1.00 71.47           O  
-HETATM32445  C1' UMP C 701     -18.252   9.183-143.179  1.00 72.88           C  
-HETATM32446  C2' UMP C 701     -17.932   7.756-142.806  1.00 48.13           C  
-HETATM32447  C3' UMP C 701     -16.707   7.456-143.662  1.00 47.31           C  
-HETATM32448  C4' UMP C 701     -16.742   8.474-144.769  1.00 62.12           C  
-HETATM32449  O3' UMP C 701     -15.568   7.847-142.923  1.00 49.10           O  
-HETATM32450  O4' UMP C 701     -17.916   9.279-144.574  1.00 82.33           O  
-HETATM32451  C5' UMP C 701     -16.500   7.907-146.181  1.00 62.42           C  
-HETATM32452  O5' UMP C 701     -17.353   6.884-146.556  1.00 55.91           O  
-HETATM32453  P   UMP C 701     -16.850   5.386-146.969  1.00 48.99           P  
-HETATM32454  OP1 UMP C 701     -17.801   5.160-148.084  1.00 38.94           O  
-HETATM32455  OP2 UMP C 701     -17.091   4.589-145.680  1.00 32.57           O  
-HETATM32456  OP3 UMP C 701     -15.444   5.358-147.410  1.00 56.10           O  
-HETATM32457  CAG 1UG C 702     -21.611  16.166-141.466  1.00 96.80           C  
-HETATM32458  CAE 1UG C 702     -21.891  17.465-141.124  1.00 98.47           C  
-HETATM32459  CAJ 1UG C 702     -20.963  18.473-141.289  1.00104.32           C  
-HETATM32460  CAU 1UG C 702     -19.727  18.204-141.815  1.00106.10           C  
-HETATM32461  CAI 1UG C 702     -18.864  19.297-141.945  1.00105.94           C  
-HETATM32462  CAC 1UG C 702     -17.608  19.109-142.461  1.00109.11           C  
-HETATM32463  CAD 1UG C 702     -17.292  17.816-142.822  1.00111.72           C  
-HETATM32464  CAL 1UG C 702     -18.148  16.710-142.695  1.00116.53           C  
-HETATM32465  CAX 1UG C 702     -19.420  16.884-142.175  1.00107.57           C  
-HETATM32466  CAR 1UG C 702     -20.379  15.849-142.000  1.00100.44           C  
-HETATM32467  SAP 1UG C 702     -20.225  14.133-142.371  1.00105.59           S  
-HETATM32468  CAS 1UG C 702     -21.298  13.809-143.848  1.00121.85           C  
-HETATM32469  CAY 1UG C 702     -20.748  13.326-144.993  1.00132.17           C  
-HETATM32470  CAZ 1UG C 702     -19.479  12.993-145.358  1.00127.84           C  
-HETATM32471  CAT 1UG C 702     -18.269  13.005-144.741  1.00114.22           C  
-HETATM32472  OAB 1UG C 702     -18.105  13.373-143.580  1.00104.95           O  
-HETATM32473  NAN 1UG C 702     -17.118  12.585-145.414  1.00107.30           N  
-HETATM32474  CAQ 1UG C 702     -17.223  12.156-146.726  1.00116.34           C  
-HETATM32475  NAA 1UG C 702     -16.139  11.756-147.375  1.00116.51           N  
-HETATM32476  NAM 1UG C 702     -18.432  12.158-147.300  1.00126.34           N  
-HETATM32477  CAW 1UG C 702     -19.530  12.566-146.635  1.00133.12           C  
-HETATM32478  NAO 1UG C 702     -20.788  12.631-147.051  1.00133.84           N  
-HETATM32479  CAV 1UG C 702     -21.550  13.093-146.062  1.00131.15           C  
-HETATM32480  CAK 1UG C 702     -22.880  13.317-146.043  1.00123.83           C  
-HETATM32481  CAF 1UG C 702     -23.493  13.808-144.897  1.00121.00           C  
-HETATM32482  CAH 1UG C 702     -22.686  14.052-143.793  1.00117.32           C  
-HETATM32483  N1  FOL C 703     -28.620  25.437-104.008  1.00 26.04           N  
-HETATM32484  C2  FOL C 703     -29.148  24.761-105.055  1.00 30.59           C  
-HETATM32485  NA2 FOL C 703     -28.454  23.812-105.708  1.00 38.33           N  
-HETATM32486  N3  FOL C 703     -30.390  24.972-105.528  1.00 38.23           N  
-HETATM32487  C4  FOL C 703     -31.218  25.880-104.994  1.00 49.42           C  
-HETATM32488  O4  FOL C 703     -32.371  26.117-105.387  1.00 55.02           O  
-HETATM32489  C4A FOL C 703     -30.726  26.650-103.864  1.00 39.39           C  
-HETATM32490  N5  FOL C 703     -31.552  27.567-103.320  1.00 36.51           N  
-HETATM32491  C6  FOL C 703     -31.108  28.267-102.299  1.00 50.01           C  
-HETATM32492  C7  FOL C 703     -29.802  28.001-101.845  1.00 58.01           C  
-HETATM32493  N8  FOL C 703     -28.911  27.079-102.358  1.00 39.93           N  
-HETATM32494  C8A FOL C 703     -29.347  26.370-103.389  1.00 34.28           C  
-HETATM32495  C9  FOL C 703     -32.014  29.320-101.648  1.00 52.67           C  
-HETATM32496  N10 FOL C 703     -33.466  29.171-101.816  1.00 47.27           N  
-HETATM32497  C11 FOL C 703     -35.830  26.092-100.282  1.00 39.21           C  
-HETATM32498  C12 FOL C 703     -34.452  25.965-100.322  1.00 45.31           C  
-HETATM32499  C13 FOL C 703     -33.658  27.003-100.835  1.00 42.27           C  
-HETATM32500  C14 FOL C 703     -34.252  28.166-101.312  1.00 41.85           C  
-HETATM32501  C15 FOL C 703     -35.642  28.297-101.278  1.00 32.92           C  
-HETATM32502  C16 FOL C 703     -36.431  27.262-100.765  1.00 33.11           C  
-HETATM32503  C   FOL C 703     -36.590  24.919 -99.723  1.00 58.19           C  
-HETATM32504  O   FOL C 703     -37.723  25.047 -99.300  1.00 61.36           O  
-HETATM32505  N   FOL C 703     -35.984  23.728 -99.726  1.00 67.24           N  
-HETATM32506  CA  FOL C 703     -36.532  22.459 -99.259  1.00 73.10           C  
-HETATM32507  CB  FOL C 703     -36.659  21.495-100.453  1.00 66.19           C  
-HETATM32508  CG  FOL C 703     -38.022  20.858-100.646  1.00 67.78           C  
-HETATM32509  CD  FOL C 703     -37.799  19.362-100.870  1.00 68.69           C  
-HETATM32510  OE1 FOL C 703     -37.697  18.881-102.042  1.00 51.34           O  
-HETATM32511  OE2 FOL C 703     -37.706  18.621 -99.856  1.00 95.47           O  
-HETATM32512  CT  FOL C 703     -35.635  21.839 -98.213  1.00 61.42           C  
-HETATM32513  O1  FOL C 703     -36.196  21.298 -97.231  1.00 62.77           O  
-HETATM32514  O2  FOL C 703     -34.374  21.862 -98.343  1.00 48.47           O  
-HETATM32515  PA  NDP C 704     -26.814  37.229 -99.336  1.00 29.30           P  
-HETATM32516  O1A NDP C 704     -25.386  37.002 -99.520  1.00 33.24           O  
-HETATM32517  O2A NDP C 704     -27.717  36.095 -99.121  1.00 30.81           O  
-HETATM32518  O5B NDP C 704     -27.044  38.257 -98.153  1.00 36.66           O  
-HETATM32519  C5B NDP C 704     -26.409  39.549 -98.145  1.00 40.42           C  
-HETATM32520  C4B NDP C 704     -26.517  40.072 -96.700  1.00 32.81           C  
-HETATM32521  O4B NDP C 704     -25.972  39.065 -95.790  1.00 35.45           O  
-HETATM32522  C3B NDP C 704     -25.639  41.288 -96.514  1.00 31.26           C  
-HETATM32523  O3B NDP C 704     -26.400  42.426 -96.839  1.00 29.80           O  
-HETATM32524  C2B NDP C 704     -25.213  41.151 -95.057  1.00 32.96           C  
-HETATM32525  O2B NDP C 704     -26.343  41.326 -94.172  1.00 37.40           O  
-HETATM32526  C1B NDP C 704     -24.965  39.649 -94.975  1.00 32.61           C  
-HETATM32527  N9A NDP C 704     -23.619  39.237 -95.409  1.00 31.71           N  
-HETATM32528  C8A NDP C 704     -23.343  38.466 -96.482  1.00 39.15           C  
-HETATM32529  N7A NDP C 704     -22.017  38.255 -96.628  1.00 45.20           N  
-HETATM32530  C5A NDP C 704     -21.423  38.908 -95.621  1.00 34.28           C  
-HETATM32531  C6A NDP C 704     -20.035  39.099 -95.185  1.00 40.37           C  
-HETATM32532  N6A NDP C 704     -19.031  38.528 -95.888  1.00 48.26           N  
-HETATM32533  N1A NDP C 704     -19.822  39.854 -94.077  1.00 51.37           N  
-HETATM32534  C2A NDP C 704     -20.820  40.423 -93.378  1.00 43.00           C  
-HETATM32535  N3A NDP C 704     -22.105  40.280 -93.732  1.00 40.81           N  
-HETATM32536  C4A NDP C 704     -22.468  39.551 -94.821  1.00 34.93           C  
-HETATM32537  O3  NDP C 704     -27.470  38.141-100.491  1.00 29.65           O  
-HETATM32538  PN  NDP C 704     -27.139  38.080-102.085  1.00 36.66           P  
-HETATM32539  O1N NDP C 704     -25.707  37.910-102.409  1.00 21.26           O  
-HETATM32540  O2N NDP C 704     -27.988  39.162-102.704  1.00 34.29           O  
-HETATM32541  O5D NDP C 704     -27.888  36.738-102.511  1.00 33.85           O  
-HETATM32542  C5D NDP C 704     -29.319  36.664-102.489  1.00 35.44           C  
-HETATM32543  C4D NDP C 704     -29.785  36.434-103.919  1.00 36.02           C  
-HETATM32544  O4D NDP C 704     -29.168  35.231-104.363  1.00 34.85           O  
-HETATM32545  C3D NDP C 704     -31.261  36.157-103.984  1.00 28.72           C  
-HETATM32546  O3D NDP C 704     -31.696  36.487-105.286  1.00 26.38           O  
-HETATM32547  C2D NDP C 704     -31.321  34.680-103.791  1.00 25.26           C  
-HETATM32548  O2D NDP C 704     -32.562  34.162-104.191  1.00 27.26           O  
-HETATM32549  C1D NDP C 704     -30.163  34.229-104.613  1.00 29.76           C  
-HETATM32550  N1N NDP C 704     -29.581  32.961-104.234  1.00 26.18           N  
-HETATM32551  C2N NDP C 704     -29.393  32.050-105.198  1.00 25.89           C  
-HETATM32552  C3N NDP C 704     -28.838  30.812-104.930  1.00 33.00           C  
-HETATM32553  C7N NDP C 704     -28.648  29.824-106.052  1.00 26.13           C  
-HETATM32554  O7N NDP C 704     -27.943  28.855-105.875  1.00 26.37           O  
-HETATM32555  N7N NDP C 704     -29.264  30.050-107.209  1.00 21.42           N  
-HETATM32556  C4N NDP C 704     -28.415  30.445-103.523  1.00 36.11           C  
-HETATM32557  C5N NDP C 704     -28.675  31.518-102.583  1.00 31.91           C  
-HETATM32558  C6N NDP C 704     -29.236  32.709-102.981  1.00 31.36           C  
-HETATM32559  P2B NDP C 704     -26.721  42.662 -93.400  1.00 28.75           P  
-HETATM32560  O1X NDP C 704     -27.955  42.251 -92.673  1.00 35.72           O  
-HETATM32561  O2X NDP C 704     -25.487  42.930 -92.590  1.00 26.99           O  
-HETATM32562  O3X NDP C 704     -27.051  43.772 -94.385  1.00 30.70           O  
-HETATM32563  N1  UMP D 701     -37.729 -15.081-135.512  1.00 62.53           N  
-HETATM32564  C2  UMP D 701     -36.382 -15.030-135.023  1.00 53.98           C  
-HETATM32565  N3  UMP D 701     -35.383 -15.406-135.796  1.00 53.52           N  
-HETATM32566  C4  UMP D 701     -35.596 -15.838-137.037  1.00 58.04           C  
-HETATM32567  C5  UMP D 701     -36.909 -15.904-137.560  1.00 73.52           C  
-HETATM32568  C6  UMP D 701     -37.972 -15.516-136.755  1.00 67.28           C  
-HETATM32569  O2  UMP D 701     -36.071 -14.640-133.871  1.00 44.68           O  
-HETATM32570  O4  UMP D 701     -34.640 -16.180-137.729  1.00 49.79           O  
-HETATM32571  C1' UMP D 701     -38.881 -14.684-134.720  1.00 60.50           C  
-HETATM32572  C2' UMP D 701     -38.838 -13.257-134.223  1.00 44.60           C  
-HETATM32573  C3' UMP D 701     -40.305 -12.874-134.160  1.00 39.99           C  
-HETATM32574  C4' UMP D 701     -40.897 -13.633-135.308  1.00 46.48           C  
-HETATM32575  O3' UMP D 701     -40.866 -13.527-133.045  1.00 44.21           O  
-HETATM32576  O4' UMP D 701     -40.076 -14.796-135.522  1.00 66.53           O  
-HETATM32577  C5' UMP D 701     -41.247 -12.797-136.551  1.00 42.42           C  
-HETATM32578  O5' UMP D 701     -42.440 -12.098-136.492  1.00 43.06           O  
-HETATM32579  P   UMP D 701     -42.548 -10.541-136.980  1.00 43.86           P  
-HETATM32580  OP1 UMP D 701     -42.525 -10.790-138.437  1.00 51.32           O  
-HETATM32581  OP2 UMP D 701     -41.276  -9.934-136.373  1.00 25.14           O  
-HETATM32582  OP3 UMP D 701     -43.797  -9.887-136.538  1.00 46.08           O  
-HETATM32583  CAG 1UG D 702     -35.156 -22.106-134.603  1.00 79.81           C  
-HETATM32584  CAE 1UG D 702     -34.931 -23.344-134.046  1.00 84.80           C  
-HETATM32585  CAJ 1UG D 702     -35.968 -24.209-133.773  1.00 83.92           C  
-HETATM32586  CAU 1UG D 702     -37.259 -23.852-134.050  1.00 83.37           C  
-HETATM32587  CAI 1UG D 702     -38.231 -24.809-133.728  1.00 71.69           C  
-HETATM32588  CAC 1UG D 702     -39.549 -24.530-133.974  1.00 69.82           C  
-HETATM32589  CAD 1UG D 702     -39.809 -23.297-134.530  1.00 83.74           C  
-HETATM32590  CAL 1UG D 702     -38.851 -22.326-134.859  1.00 82.07           C  
-HETATM32591  CAX 1UG D 702     -37.512 -22.588-134.619  1.00 82.79           C  
-HETATM32592  CAR 1UG D 702     -36.439 -21.698-134.912  1.00 78.04           C  
-HETATM32593  SAP 1UG D 702     -36.413 -20.065-135.594  1.00 86.56           S  
-HETATM32594  CAS 1UG D 702     -37.626 -19.734-136.959  1.00 99.19           C  
-HETATM32595  CAY 1UG D 702     -38.786 -19.055-136.710  1.00101.67           C  
-HETATM32596  CAZ 1UG D 702     -39.358 -18.523-135.590  1.00 90.55           C  
-HETATM32597  CAT 1UG D 702     -39.005 -18.438-134.282  1.00 83.54           C  
-HETATM32598  OAB 1UG D 702     -37.956 -18.896-133.831  1.00 79.99           O  
-HETATM32599  NAN 1UG D 702     -39.843 -17.806-133.354  1.00 81.63           N  
-HETATM32600  CAQ 1UG D 702     -41.044 -17.264-133.784  1.00 74.13           C  
-HETATM32601  NAA 1UG D 702     -41.848 -16.663-132.922  1.00 66.65           N  
-HETATM32602  NAM 1UG D 702     -41.357 -17.367-135.080  1.00 77.85           N  
-HETATM32603  CAW 1UG D 702     -40.537 -17.980-135.956  1.00 90.25           C  
-HETATM32604  NAO 1UG D 702     -40.697 -18.165-137.259  1.00 99.27           N  
-HETATM32605  CAV 1UG D 702     -39.642 -18.819-137.740  1.00105.91           C  
-HETATM32606  CAK 1UG D 702     -39.396 -19.211-139.007  1.00106.32           C  
-HETATM32607  CAF 1UG D 702     -38.225 -19.890-139.317  1.00105.93           C  
-HETATM32608  CAH 1UG D 702     -37.335 -20.145-138.279  1.00101.87           C  
-HETATM32609  N1  FOL D 703      -4.487 -30.170-113.495  1.00 34.81           N  
-HETATM32610  C2  FOL D 703      -4.838 -29.572-114.659  1.00 36.66           C  
-HETATM32611  NA2 FOL D 703      -5.838 -28.675-114.720  1.00 43.43           N  
-HETATM32612  N3  FOL D 703      -4.233 -29.814-115.836  1.00 38.65           N  
-HETATM32613  C4  FOL D 703      -3.220 -30.679-115.952  1.00 50.08           C  
-HETATM32614  O4  FOL D 703      -2.618 -30.950-117.003  1.00 55.24           O  
-HETATM32615  C4A FOL D 703      -2.784 -31.361-114.747  1.00 47.07           C  
-HETATM32616  N5  FOL D 703      -1.765 -32.231-114.860  1.00 50.02           N  
-HETATM32617  C6  FOL D 703      -1.364 -32.853-113.774  1.00 59.83           C  
-HETATM32618  C7  FOL D 703      -2.020 -32.568-112.560  1.00 58.32           C  
-HETATM32619  N8  FOL D 703      -3.069 -31.692-112.388  1.00 45.93           N  
-HETATM32620  C8A FOL D 703      -3.486 -31.056-113.476  1.00 39.34           C  
-HETATM32621  C9  FOL D 703      -0.204 -33.845-113.904  1.00 61.92           C  
-HETATM32622  N10 FOL D 703       0.605 -33.714-115.121  1.00 52.58           N  
-HETATM32623  C11 FOL D 703       3.552 -30.829-115.715  1.00 60.34           C  
-HETATM32624  C12 FOL D 703       2.614 -30.671-114.710  1.00 59.01           C  
-HETATM32625  C13 FOL D 703       1.627 -31.644-114.512  1.00 52.24           C  
-HETATM32626  C14 FOL D 703       1.574 -32.770-115.325  1.00 49.66           C  
-HETATM32627  C15 FOL D 703       2.512 -32.934-116.345  1.00 57.87           C  
-HETATM32628  C16 FOL D 703       3.503 -31.958-116.544  1.00 62.80           C  
-HETATM32629  C   FOL D 703       4.578 -29.745-115.883  1.00 69.30           C  
-HETATM32630  O   FOL D 703       5.581 -29.960-116.537  1.00 84.38           O  
-HETATM32631  N   FOL D 703       4.367 -28.551-115.322  1.00 67.39           N  
-HETATM32632  CA  FOL D 703       5.277 -27.411-115.403  1.00 86.99           C  
-HETATM32633  CB  FOL D 703       5.103 -26.683-116.759  1.00 80.32           C  
-HETATM32634  CG  FOL D 703       3.950 -25.683-116.899  1.00 81.19           C  
-HETATM32635  CD  FOL D 703       3.896 -25.225-118.362  1.00 83.49           C  
-HETATM32636  OE1 FOL D 703       4.131 -26.043-119.303  1.00 86.99           O  
-HETATM32637  OE2 FOL D 703       3.623 -24.020-118.601  1.00 67.13           O  
-HETATM32638  CT  FOL D 703       5.104 -26.467-114.230  1.00 91.51           C  
-HETATM32639  O1  FOL D 703       6.152 -26.038-113.700  1.00 88.55           O  
-HETATM32640  O2  FOL D 703       3.959 -26.137-113.808  1.00 81.84           O  
-HETATM32641  PA  NDP D 704      -1.600 -42.079-108.791  1.00 65.81           P  
-HETATM32642  O1A NDP D 704      -2.650 -41.260-108.200  1.00 64.87           O  
-HETATM32643  O2A NDP D 704      -0.464 -41.434-109.461  1.00 62.10           O  
-HETATM32644  O5B NDP D 704      -0.985 -43.021-107.672  1.00 86.18           O  
-HETATM32645  C5B NDP D 704      -1.308 -44.416-107.510  1.00 89.72           C  
-HETATM32646  C4B NDP D 704      -0.230 -44.919-106.529  1.00 88.20           C  
-HETATM32647  O4B NDP D 704      -0.068 -43.907-105.484  1.00 85.59           O  
-HETATM32648  C3B NDP D 704      -0.642 -46.177-105.794  1.00 96.54           C  
-HETATM32649  O3B NDP D 704      -0.218 -47.295-106.535  1.00 97.00           O  
-HETATM32650  C2B NDP D 704      -0.025 -46.000-104.404  1.00102.36           C  
-HETATM32651  O2B NDP D 704       1.406 -46.263-104.368  1.00100.79           O  
-HETATM32652  C1B NDP D 704      -0.185 -44.495-104.194  1.00 99.03           C  
-HETATM32653  N9A NDP D 704      -1.475 -44.153-103.561  1.00 94.72           N  
-HETATM32654  C8A NDP D 704      -2.509 -43.516-104.153  1.00 88.35           C  
-HETATM32655  N7A NDP D 704      -3.556 -43.349-103.317  1.00 90.50           N  
-HETATM32656  C5A NDP D 704      -3.192 -43.896-102.151  1.00 92.82           C  
-HETATM32657  C6A NDP D 704      -3.830 -44.065-100.838  1.00 96.27           C  
-HETATM32658  N6A NDP D 704      -5.083 -43.599-100.634  1.00 85.77           N  
-HETATM32659  N1A NDP D 704      -3.117 -44.694 -99.871  1.00100.34           N  
-HETATM32660  C2A NDP D 704      -1.870 -45.159-100.071  1.00106.72           C  
-HETATM32661  N3A NDP D 704      -1.240 -45.033-101.247  1.00 99.63           N  
-HETATM32662  C4A NDP D 704      -1.832 -44.424-102.308  1.00 91.30           C  
-HETATM32663  O3  NDP D 704      -2.122 -43.263-109.762  1.00 72.51           O  
-HETATM32664  PN  NDP D 704      -3.351 -43.250-110.838  1.00 57.52           P  
-HETATM32665  O1N NDP D 704      -4.708 -43.340-110.262  1.00 49.62           O  
-HETATM32666  O2N NDP D 704      -2.904 -44.175-111.939  1.00 57.94           O  
-HETATM32667  O5D NDP D 704      -3.213 -41.803-111.498  1.00 50.06           O  
-HETATM32668  C5D NDP D 704      -2.229 -41.568-112.514  1.00 54.06           C  
-HETATM32669  C4D NDP D 704      -2.950 -41.423-113.844  1.00 45.41           C  
-HETATM32670  O4D NDP D 704      -3.679 -40.205-113.797  1.00 40.81           O  
-HETATM32671  C3D NDP D 704      -1.970 -41.241-114.968  1.00 37.54           C  
-HETATM32672  O3D NDP D 704      -2.605 -41.649-116.163  1.00 34.30           O  
-HETATM32673  C2D NDP D 704      -1.771 -39.763-114.990  1.00 37.85           C  
-HETATM32674  O2D NDP D 704      -1.174 -39.346-116.193  1.00 37.46           O  
-HETATM32675  C1D NDP D 704      -3.166 -39.282-114.769  1.00 38.59           C  
-HETATM32676  N1N NDP D 704      -3.292 -37.963-114.188  1.00 35.71           N  
-HETATM32677  C2N NDP D 704      -4.143 -37.102-114.765  1.00 35.67           C  
-HETATM32678  C3N NDP D 704      -4.326 -35.824-114.269  1.00 40.56           C  
-HETATM32679  C7N NDP D 704      -5.292 -34.885-114.947  1.00 39.71           C  
-HETATM32680  O7N NDP D 704      -5.571 -33.837-114.407  1.00 44.89           O  
-HETATM32681  N7N NDP D 704      -5.809 -35.236-116.120  1.00 37.99           N  
-HETATM32682  C4N NDP D 704      -3.570 -35.358-113.044  1.00 45.86           C  
-HETATM32683  C5N NDP D 704      -2.689 -36.384-112.525  1.00 45.70           C  
-HETATM32684  C6N NDP D 704      -2.596 -37.622-113.114  1.00 41.53           C  
-HETATM32685  P2B NDP D 704       2.021 -47.602-103.760  1.00101.22           P  
-HETATM32686  O1X NDP D 704       3.490 -47.392-103.911  1.00 83.31           O  
-HETATM32687  O2X NDP D 704       1.443 -47.627-102.376  1.00 92.52           O  
-HETATM32688  O3X NDP D 704       1.562 -48.798-104.579  1.00 77.85           O  
-HETATM32689  N1  UMP E 701       7.331 -79.941 -34.464  1.00 69.51           N  
-HETATM32690  C2  UMP E 701       6.714 -79.884 -35.758  1.00 56.18           C  
-HETATM32691  N3  UMP E 701       5.465 -80.268 -35.910  1.00 57.62           N  
-HETATM32692  C4  UMP E 701       4.750 -80.715 -34.881  1.00 63.25           C  
-HETATM32693  C5  UMP E 701       5.313 -80.792 -33.588  1.00 74.34           C  
-HETATM32694  C6  UMP E 701       6.631 -80.393 -33.414  1.00 78.64           C  
-HETATM32695  O2  UMP E 701       7.299 -79.480 -36.791  1.00 47.82           O  
-HETATM32696  O4  UMP E 701       3.588 -81.065 -35.063  1.00 63.29           O  
-HETATM32697  C1' UMP E 701       8.710 -79.540 -34.225  1.00 73.77           C  
-HETATM32698  C2' UMP E 701       9.048 -78.120 -34.612  1.00 51.29           C  
-HETATM32699  C3' UMP E 701      10.280 -77.825 -33.762  1.00 47.54           C  
-HETATM32700  C4' UMP E 701      10.229 -78.826 -32.641  1.00 59.07           C  
-HETATM32701  O3' UMP E 701      11.421 -78.240 -34.487  1.00 50.53           O  
-HETATM32702  O4' UMP E 701       9.046 -79.622 -32.828  1.00 75.91           O  
-HETATM32703  C5' UMP E 701      10.475 -78.247 -31.236  1.00 57.63           C  
-HETATM32704  O5' UMP E 701       9.617 -77.230 -30.863  1.00 58.70           O  
-HETATM32705  P   UMP E 701      10.123 -75.733 -30.449  1.00 51.94           P  
-HETATM32706  OP1 UMP E 701       9.906 -75.071 -31.756  1.00 34.56           O  
-HETATM32707  OP2 UMP E 701       9.155 -75.373 -29.313  1.00 39.72           O  
-HETATM32708  OP3 UMP E 701      11.537 -75.713 -30.036  1.00 57.19           O  
-HETATM32709  CAG 1UG E 702       5.361 -86.733 -36.011  1.00 90.17           C  
-HETATM32710  CAE 1UG E 702       5.444 -88.063 -36.356  1.00 93.41           C  
-HETATM32711  CAJ 1UG E 702       6.536 -88.838 -36.018  1.00 95.22           C  
-HETATM32712  CAU 1UG E 702       7.579 -88.298 -35.316  1.00100.41           C  
-HETATM32713  CAI 1UG E 702       8.639 -89.164 -35.018  1.00 98.31           C  
-HETATM32714  CAC 1UG E 702       9.716 -88.683 -34.318  1.00102.26           C  
-HETATM32715  CAD 1UG E 702       9.659 -87.353 -33.959  1.00109.63           C  
-HETATM32716  CAL 1UG E 702       8.607 -86.476 -34.248  1.00111.50           C  
-HETATM32717  CAX 1UG E 702       7.514 -86.944 -34.954  1.00102.67           C  
-HETATM32718  CAR 1UG E 702       6.391 -86.149 -35.300  1.00 92.82           C  
-HETATM32719  SAP 1UG E 702       6.108 -84.442 -34.957  1.00 96.33           S  
-HETATM32720  CAS 1UG E 702       6.147 -84.194 -33.122  1.00114.76           C  
-HETATM32721  CAY 1UG E 702       7.245 -83.653 -32.527  1.00115.56           C  
-HETATM32722  CAZ 1UG E 702       8.450 -83.210 -32.987  1.00107.14           C  
-HETATM32723  CAT 1UG E 702       9.036 -83.123 -34.210  1.00101.97           C  
-HETATM32724  OAB 1UG E 702       8.490 -83.486 -35.251  1.00 99.66           O  
-HETATM32725  NAN 1UG E 702      10.327 -82.603 -34.352  1.00 94.83           N  
-HETATM32726  CAQ 1UG E 702      11.007 -82.174 -33.224  1.00 84.64           C  
-HETATM32727  NAA 1UG E 702      12.229 -81.678 -33.341  1.00 75.40           N  
-HETATM32728  NAM 1UG E 702      10.397 -82.273 -32.037  1.00 87.37           N  
-HETATM32729  CAW 1UG E 702       9.153 -82.778 -31.922  1.00101.17           C  
-HETATM32730  NAO 1UG E 702       8.413 -82.946 -30.834  1.00107.94           N  
-HETATM32731  CAV 1UG E 702       7.242 -83.480 -31.180  1.00117.89           C  
-HETATM32732  CAK 1UG E 702       6.193 -83.817 -30.399  1.00116.58           C  
-HETATM32733  CAF 1UG E 702       5.046 -84.368 -30.958  1.00112.00           C  
-HETATM32734  CAH 1UG E 702       5.032 -84.552 -32.336  1.00112.62           C  
-HETATM32735  N1  FOL E 703      -1.676 -95.791 -73.355  1.00 24.74           N  
-HETATM32736  C2  FOL E 703      -2.214 -95.142 -72.295  1.00 29.50           C  
-HETATM32737  NA2 FOL E 703      -1.535 -94.196 -71.621  1.00 31.27           N  
-HETATM32738  N3  FOL E 703      -3.453 -95.379 -71.827  1.00 35.30           N  
-HETATM32739  C4  FOL E 703      -4.267 -96.287 -72.378  1.00 45.76           C  
-HETATM32740  O4  FOL E 703      -5.416 -96.546 -71.989  1.00 51.62           O  
-HETATM32741  C4A FOL E 703      -3.765 -97.029 -73.522  1.00 37.00           C  
-HETATM32742  N5  FOL E 703      -4.578 -97.948 -74.085  1.00 36.51           N  
-HETATM32743  C6  FOL E 703      -4.121 -98.621 -75.119  1.00 50.05           C  
-HETATM32744  C7  FOL E 703      -2.819 -98.328 -75.567  1.00 54.06           C  
-HETATM32745  N8  FOL E 703      -1.942 -97.404 -75.035  1.00 37.61           N  
-HETATM32746  C8A FOL E 703      -2.389 -96.722 -73.991  1.00 32.97           C  
-HETATM32747  C9  FOL E 703      -5.010 -99.674 -75.793  1.00 56.48           C  
-HETATM32748  N10 FOL E 703      -6.463 -99.553 -75.614  1.00 48.97           N  
-HETATM32749  C11 FOL E 703      -8.842 -96.477 -77.122  1.00 39.60           C  
-HETATM32750  C12 FOL E 703      -7.466 -96.341 -77.072  1.00 44.14           C  
-HETATM32751  C13 FOL E 703      -6.669 -97.379 -76.567  1.00 40.68           C  
-HETATM32752  C14 FOL E 703      -7.258 -98.552 -76.108  1.00 37.10           C  
-HETATM32753  C15 FOL E 703      -8.646 -98.694 -76.152  1.00 30.38           C  
-HETATM32754  C16 FOL E 703      -9.438 -97.658 -76.658  1.00 35.25           C  
-HETATM32755  C   FOL E 703      -9.609 -95.305 -77.669  1.00 53.66           C  
-HETATM32756  O   FOL E 703     -10.751 -95.435 -78.070  1.00 57.59           O  
-HETATM32757  N   FOL E 703      -9.003 -94.115 -77.680  1.00 66.00           N  
-HETATM32758  CA  FOL E 703      -9.561 -92.847 -78.140  1.00 73.37           C  
-HETATM32759  CB  FOL E 703      -9.713 -91.900 -76.936  1.00 67.87           C  
-HETATM32760  CG  FOL E 703     -11.074 -91.250 -76.773  1.00 67.91           C  
-HETATM32761  CD  FOL E 703     -10.841 -89.758 -76.532  1.00 71.82           C  
-HETATM32762  OE1 FOL E 703     -10.755 -89.287 -75.354  1.00 53.84           O  
-HETATM32763  OE2 FOL E 703     -10.722 -89.010 -77.538  1.00 90.06           O  
-HETATM32764  CT  FOL E 703      -8.662 -92.203 -79.171  1.00 58.24           C  
-HETATM32765  O1  FOL E 703      -9.221 -91.690 -80.168  1.00 65.55           O  
-HETATM32766  O2  FOL E 703      -7.403 -92.178 -79.016  1.00 39.11           O  
-HETATM32767  PA  NDP E 704       0.144-107.599 -78.090  1.00 23.76           P  
-HETATM32768  O1A NDP E 704       1.575-107.369 -77.947  1.00 27.13           O  
-HETATM32769  O2A NDP E 704      -0.766-106.468 -78.286  1.00 25.37           O  
-HETATM32770  O5B NDP E 704      -0.108-108.628 -79.267  1.00 34.80           O  
-HETATM32771  C5B NDP E 704       0.539-109.914 -79.294  1.00 37.87           C  
-HETATM32772  C4B NDP E 704       0.442-110.415 -80.748  1.00 33.65           C  
-HETATM32773  O4B NDP E 704       1.009-109.405 -81.642  1.00 37.96           O  
-HETATM32774  C3B NDP E 704       1.300-111.642 -80.945  1.00 31.75           C  
-HETATM32775  O3B NDP E 704       0.509-112.769 -80.653  1.00 40.22           O  
-HETATM32776  C2B NDP E 704       1.754-111.494 -82.393  1.00 34.21           C  
-HETATM32777  O2B NDP E 704       0.641-111.669 -83.300  1.00 37.36           O  
-HETATM32778  C1B NDP E 704       2.004-109.991 -82.469  1.00 33.00           C  
-HETATM32779  N9A NDP E 704       3.355-109.573 -82.051  1.00 33.17           N  
-HETATM32780  C8A NDP E 704       3.636-108.770 -81.003  1.00 34.45           C  
-HETATM32781  N7A NDP E 704       4.963-108.559 -80.865  1.00 40.91           N  
-HETATM32782  C5A NDP E 704       5.554-109.243 -81.852  1.00 37.51           C  
-HETATM32783  C6A NDP E 704       6.943-109.450 -82.285  1.00 42.02           C  
-HETATM32784  N6A NDP E 704       7.951-108.862 -81.603  1.00 43.10           N  
-HETATM32785  N1A NDP E 704       7.154-110.237 -83.370  1.00 48.61           N  
-HETATM32786  C2A NDP E 704       6.151-110.824 -84.051  1.00 44.64           C  
-HETATM32787  N3A NDP E 704       4.866-110.669 -83.700  1.00 42.43           N  
-HETATM32788  C4A NDP E 704       4.504-109.907 -82.632  1.00 41.57           C  
-HETATM32789  O3  NDP E 704      -0.484-108.518 -76.923  1.00 29.49           O  
-HETATM32790  PN  NDP E 704      -0.150-108.476 -75.328  1.00 32.26           P  
-HETATM32791  O1N NDP E 704       1.282-108.324 -74.996  1.00 21.26           O  
-HETATM32792  O2N NDP E 704      -1.007-109.554 -74.712  1.00 34.48           O  
-HETATM32793  O5D NDP E 704      -0.885-107.131 -74.890  1.00 27.21           O  
-HETATM32794  C5D NDP E 704      -2.314-107.043 -74.927  1.00 30.80           C  
-HETATM32795  C4D NDP E 704      -2.789-106.823 -73.498  1.00 30.77           C  
-HETATM32796  O4D NDP E 704      -2.192-105.612 -73.051  1.00 35.72           O  
-HETATM32797  C3D NDP E 704      -4.266-106.561 -73.443  1.00 25.38           C  
-HETATM32798  O3D NDP E 704      -4.693-106.871 -72.134  1.00 26.38           O  
-HETATM32799  C2D NDP E 704      -4.337-105.089 -73.665  1.00 21.43           C  
-HETATM32800  O2D NDP E 704      -5.592-104.580 -73.300  1.00 29.21           O  
-HETATM32801  C1D NDP E 704      -3.198-104.612 -72.830  1.00 26.51           C  
-HETATM32802  N1N NDP E 704      -2.614-103.346 -73.214  1.00 26.18           N  
-HETATM32803  C2N NDP E 704      -2.404-102.437 -72.252  1.00 23.21           C  
-HETATM32804  C3N NDP E 704      -1.844-101.203 -72.527  1.00 33.56           C  
-HETATM32805  C7N NDP E 704      -1.631-100.213 -71.409  1.00 28.73           C  
-HETATM32806  O7N NDP E 704      -0.971 -99.219 -71.621  1.00 26.77           O  
-HETATM32807  N7N NDP E 704      -2.177-100.465 -70.222  1.00 20.14           N  
-HETATM32808  C4N NDP E 704      -1.439-100.836 -73.939  1.00 37.84           C  
-HETATM32809  C5N NDP E 704      -1.720-101.907 -74.876  1.00 30.79           C  
-HETATM32810  C6N NDP E 704      -2.284-103.094 -74.471  1.00 29.56           C  
-HETATM32811  P2B NDP E 704       0.229-113.022 -84.027  1.00 39.81           P  
-HETATM32812  O1X NDP E 704      -0.991-112.603 -84.774  1.00 34.47           O  
-HETATM32813  O2X NDP E 704       1.457-113.354 -84.825  1.00 32.46           O  
-HETATM32814  O3X NDP E 704      -0.134-114.092 -83.010  1.00 33.22           O  
-HETATM32815  N1  UMP F 701     -10.792 -55.384 -41.893  1.00 65.82           N  
-HETATM32816  C2  UMP F 701      -9.452 -55.363 -42.400  1.00 54.32           C  
-HETATM32817  N3  UMP F 701      -8.457 -54.970 -41.631  1.00 55.86           N  
-HETATM32818  C4  UMP F 701      -8.668 -54.587 -40.374  1.00 58.60           C  
-HETATM32819  C5  UMP F 701      -9.975 -54.592 -39.831  1.00 70.85           C  
-HETATM32820  C6  UMP F 701     -11.033 -55.001 -40.633  1.00 68.97           C  
-HETATM32821  O2  UMP F 701      -9.149 -55.704 -43.569  1.00 40.11           O  
-HETATM32822  O4  UMP F 701      -7.717 -54.226 -39.685  1.00 50.42           O  
-HETATM32823  C1' UMP F 701     -11.931 -55.806 -42.693  1.00 62.27           C  
-HETATM32824  C2' UMP F 701     -11.888 -57.254 -43.125  1.00 41.84           C  
-HETATM32825  C3' UMP F 701     -13.358 -57.619 -43.225  1.00 35.41           C  
-HETATM32826  C4' UMP F 701     -13.977 -56.813 -42.125  1.00 43.60           C  
-HETATM32827  O3' UMP F 701     -13.875 -56.984 -44.372  1.00 41.48           O  
-HETATM32828  O4' UMP F 701     -13.155 -55.646 -41.942  1.00 68.43           O  
-HETATM32829  C5' UMP F 701     -14.355 -57.598 -40.856  1.00 42.91           C  
-HETATM32830  O5' UMP F 701     -15.533 -58.324 -40.916  1.00 43.52           O  
-HETATM32831  P   UMP F 701     -15.630 -59.878 -40.413  1.00 42.61           P  
-HETATM32832  OP1 UMP F 701     -14.422 -60.393 -41.100  1.00 26.01           O  
-HETATM32833  OP2 UMP F 701     -15.524 -59.736 -38.891  1.00 53.21           O  
-HETATM32834  OP3 UMP F 701     -16.874 -60.542 -40.848  1.00 43.94           O  
-HETATM32835  CAG 1UG F 702      -8.387 -49.159 -41.331  1.00 84.71           C  
-HETATM32836  CAE 1UG F 702      -7.935 -47.868 -41.254  1.00 86.38           C  
-HETATM32837  CAJ 1UG F 702      -8.627 -46.816 -41.819  1.00 87.08           C  
-HETATM32838  CAU 1UG F 702      -9.813 -47.023 -42.470  1.00 81.24           C  
-HETATM32839  CAI 1UG F 702     -10.437 -45.885 -42.997  1.00 82.90           C  
-HETATM32840  CAC 1UG F 702     -11.627 -46.021 -43.665  1.00 71.00           C  
-HETATM32841  CAD 1UG F 702     -12.120 -47.305 -43.762  1.00 78.63           C  
-HETATM32842  CAL 1UG F 702     -11.506 -48.454 -43.238  1.00 90.70           C  
-HETATM32843  CAX 1UG F 702     -10.302 -48.335 -42.559  1.00 87.19           C  
-HETATM32844  CAR 1UG F 702      -9.577 -49.417 -41.978  1.00 86.64           C  
-HETATM32845  SAP 1UG F 702      -9.966 -51.139 -41.961  1.00101.74           S  
-HETATM32846  CAS 1UG F 702     -11.071 -51.427 -40.504  1.00106.22           C  
-HETATM32847  CAY 1UG F 702     -12.302 -51.973 -40.688  1.00107.43           C  
-HETATM32848  CAZ 1UG F 702     -12.989 -52.402 -41.782  1.00 95.03           C  
-HETATM32849  CAT 1UG F 702     -12.724 -52.454 -43.111  1.00 86.41           C  
-HETATM32850  OAB 1UG F 702     -11.666 -52.068 -43.604  1.00 83.72           O  
-HETATM32851  NAN 1UG F 702     -13.665 -52.965 -44.005  1.00 83.69           N  
-HETATM32852  CAQ 1UG F 702     -14.878 -53.420 -43.521  1.00 77.82           C  
-HETATM32853  NAA 1UG F 702     -15.772 -53.904 -44.369  1.00 71.05           N  
-HETATM32854  NAM 1UG F 702     -15.106 -53.352 -42.204  1.00 85.21           N  
-HETATM32855  CAW 1UG F 702     -14.185 -52.855 -41.357  1.00 95.33           C  
-HETATM32856  NAO 1UG F 702     -14.240 -52.716 -40.041  1.00102.73           N  
-HETATM32857  CAV 1UG F 702     -13.099 -52.179 -39.612  1.00110.95           C  
-HETATM32858  CAK 1UG F 702     -12.721 -51.863 -38.354  1.00108.85           C  
-HETATM32859  CAF 1UG F 702     -11.470 -51.302 -38.113  1.00105.07           C  
-HETATM32860  CAH 1UG F 702     -10.641 -51.086 -39.206  1.00103.33           C  
-HETATM32861  N1  FOL F 703      22.361 -40.160 -63.919  1.00 36.87           N  
-HETATM32862  C2  FOL F 703      22.005 -40.739 -62.747  1.00 41.87           C  
-HETATM32863  NA2 FOL F 703      21.007 -41.638 -62.672  1.00 47.20           N  
-HETATM32864  N3  FOL F 703      22.603 -40.472 -61.572  1.00 40.10           N  
-HETATM32865  C4  FOL F 703      23.613 -39.603 -61.466  1.00 49.76           C  
-HETATM32866  O4  FOL F 703      24.207 -39.313 -60.416  1.00 63.88           O  
-HETATM32867  C4A FOL F 703      24.054 -38.941 -62.679  1.00 46.52           C  
-HETATM32868  N5  FOL F 703      25.070 -38.066 -62.577  1.00 50.02           N  
-HETATM32869  C6  FOL F 703      25.476 -37.461 -63.671  1.00 63.77           C  
-HETATM32870  C7  FOL F 703      24.827 -37.771 -64.883  1.00 63.73           C  
-HETATM32871  N8  FOL F 703      23.782 -38.653 -65.043  1.00 49.79           N  
-HETATM32872  C8A FOL F 703      23.360 -39.272 -63.947  1.00 37.61           C  
-HETATM32873  C9  FOL F 703      26.633 -36.463 -63.558  1.00 61.72           C  
-HETATM32874  N10 FOL F 703      27.469 -36.584 -62.357  1.00 54.55           N  
-HETATM32875  C11 FOL F 703      30.417 -39.463 -61.736  1.00 67.16           C  
-HETATM32876  C12 FOL F 703      29.472 -39.638 -62.731  1.00 66.76           C  
-HETATM32877  C13 FOL F 703      28.483 -38.669 -62.941  1.00 59.91           C  
-HETATM32878  C14 FOL F 703      28.438 -37.528 -62.148  1.00 57.96           C  
-HETATM32879  C15 FOL F 703      29.383 -37.347 -61.137  1.00 54.85           C  
-HETATM32880  C16 FOL F 703      30.375 -38.318 -60.927  1.00 62.74           C  
-HETATM32881  C   FOL F 703      31.444 -40.544 -61.556  1.00 72.74           C  
-HETATM32882  O   FOL F 703      32.444 -40.327 -60.896  1.00 80.78           O  
-HETATM32883  N   FOL F 703      31.238 -41.737 -62.116  1.00 69.97           N  
-HETATM32884  CA  FOL F 703      32.147 -42.877 -62.029  1.00 87.17           C  
-HETATM32885  CB  FOL F 703      31.966 -43.611 -60.677  1.00 78.83           C  
-HETATM32886  CG  FOL F 703      30.823 -44.624 -60.554  1.00 79.68           C  
-HETATM32887  CD  FOL F 703      30.752 -45.088 -59.094  1.00 82.06           C  
-HETATM32888  OE1 FOL F 703      30.988 -44.277 -58.146  1.00 86.99           O  
-HETATM32889  OE2 FOL F 703      30.464 -46.291 -58.864  1.00 66.17           O  
-HETATM32890  CT  FOL F 703      31.972 -43.807 -63.212  1.00 91.10           C  
-HETATM32891  O1  FOL F 703      33.018 -44.236 -63.746  1.00 90.34           O  
-HETATM32892  O2  FOL F 703      30.825 -44.124 -63.639  1.00 86.70           O  
-HETATM32893  PA  NDP F 704      25.191 -28.203 -68.616  1.00 61.64           P  
-HETATM32894  O1A NDP F 704      24.134 -28.935 -69.304  1.00 61.08           O  
-HETATM32895  O2A NDP F 704      26.256 -28.939 -67.926  1.00 52.24           O  
-HETATM32896  O5B NDP F 704      25.907 -27.222 -69.633  1.00 83.63           O  
-HETATM32897  C5B NDP F 704      25.426 -25.906 -69.965  1.00 85.43           C  
-HETATM32898  C4B NDP F 704      26.529 -25.373 -70.899  1.00 91.63           C  
-HETATM32899  O4B NDP F 704      26.744 -26.377 -71.942  1.00 87.27           O  
-HETATM32900  C3B NDP F 704      26.122 -24.113 -71.633  1.00100.22           C  
-HETATM32901  O3B NDP F 704      26.544 -23.003 -70.880  1.00 97.83           O  
-HETATM32902  C2B NDP F 704      26.745 -24.281 -73.021  1.00106.25           C  
-HETATM32903  O2B NDP F 704      28.169 -23.982 -73.049  1.00106.01           O  
-HETATM32904  C1B NDP F 704      26.619 -25.790 -73.231  1.00 97.96           C  
-HETATM32905  N9A NDP F 704      25.341 -26.171 -73.869  1.00 90.74           N  
-HETATM32906  C8A NDP F 704      24.321 -26.836 -73.280  1.00 88.49           C  
-HETATM32907  N7A NDP F 704      23.284 -27.035 -74.123  1.00 96.86           N  
-HETATM32908  C5A NDP F 704      23.642 -26.483 -75.288  1.00 97.66           C  
-HETATM32909  C6A NDP F 704      23.009 -26.337 -76.605  1.00 94.47           C  
-HETATM32910  N6A NDP F 704      21.772 -26.840 -76.815  1.00 83.34           N  
-HETATM32911  N1A NDP F 704      23.711 -25.692 -77.570  1.00103.10           N  
-HETATM32912  C2A NDP F 704      24.943 -25.191 -77.364  1.00105.06           C  
-HETATM32913  N3A NDP F 704      25.567 -25.295 -76.184  1.00 99.96           N  
-HETATM32914  C4A NDP F 704      24.985 -25.917 -75.124  1.00 92.86           C  
-HETATM32915  O3  NDP F 704      24.682 -27.035 -67.621  1.00 72.12           O  
-HETATM32916  PN  NDP F 704      23.454 -27.054 -66.546  1.00 65.47           P  
-HETATM32917  O1N NDP F 704      22.099 -26.994 -67.129  1.00 54.54           O  
-HETATM32918  O2N NDP F 704      23.887 -26.105 -65.459  1.00 57.06           O  
-HETATM32919  O5D NDP F 704      23.617 -28.493 -65.876  1.00 56.39           O  
-HETATM32920  C5D NDP F 704      24.601 -28.707 -64.856  1.00 53.49           C  
-HETATM32921  C4D NDP F 704      23.870 -28.894 -63.538  1.00 40.96           C  
-HETATM32922  O4D NDP F 704      23.153 -30.117 -63.629  1.00 38.75           O  
-HETATM32923  C3D NDP F 704      24.845 -29.090 -62.412  1.00 37.15           C  
-HETATM32924  O3D NDP F 704      24.238 -28.621 -61.224  1.00 33.61           O  
-HETATM32925  C2D NDP F 704      25.003 -30.573 -62.345  1.00 36.29           C  
-HETATM32926  O2D NDP F 704      25.522 -30.969 -61.099  1.00 30.05           O  
-HETATM32927  C1D NDP F 704      23.615 -31.041 -62.633  1.00 36.73           C  
-HETATM32928  N1N NDP F 704      23.505 -32.365 -63.210  1.00 37.11           N  
-HETATM32929  C2N NDP F 704      22.655 -33.231 -62.638  1.00 34.85           C  
-HETATM32930  C3N NDP F 704      22.487 -34.514 -63.128  1.00 37.05           C  
-HETATM32931  C7N NDP F 704      21.521 -35.456 -62.454  1.00 37.25           C  
-HETATM32932  O7N NDP F 704      21.283 -36.527 -62.965  1.00 44.95           O  
-HETATM32933  N7N NDP F 704      20.954 -35.083 -61.311  1.00 45.25           N  
-HETATM32934  C4N NDP F 704      23.260 -34.982 -64.341  1.00 43.05           C  
-HETATM32935  C5N NDP F 704      24.138 -33.951 -64.857  1.00 43.70           C  
-HETATM32936  C6N NDP F 704      24.215 -32.708 -64.274  1.00 41.35           C  
-HETATM32937  P2B NDP F 704      28.752 -22.624 -73.650  1.00108.99           P  
-HETATM32938  O1X NDP F 704      30.225 -22.822 -73.513  1.00 88.33           O  
-HETATM32939  O2X NDP F 704      28.156 -22.579 -75.024  1.00 92.43           O  
-HETATM32940  O3X NDP F 704      28.274 -21.447 -72.816  1.00 89.68           O  
-HETATM32941  N1  UMP G 701      20.932  81.836  53.865  1.00 68.42           N  
-HETATM32942  C2  UMP G 701      21.531  81.818  52.562  1.00 59.43           C  
-HETATM32943  N3  UMP G 701      22.784  82.184  52.410  1.00 57.18           N  
-HETATM32944  C4  UMP G 701      23.518  82.576  53.447  1.00 61.34           C  
-HETATM32945  C5  UMP G 701      22.973  82.611  54.750  1.00 69.96           C  
-HETATM32946  C6  UMP G 701      21.651  82.231  54.925  1.00 72.23           C  
-HETATM32947  O2  UMP G 701      20.928  81.466  51.519  1.00 49.53           O  
-HETATM32948  O4  UMP G 701      24.684  82.911  53.262  1.00 62.83           O  
-HETATM32949  C1' UMP G 701      19.550  81.448  54.102  1.00 69.35           C  
-HETATM32950  C2' UMP G 701      19.216  80.026  53.721  1.00 49.83           C  
-HETATM32951  C3' UMP G 701      18.004  79.717  54.593  1.00 45.05           C  
-HETATM32952  C4' UMP G 701      18.051  80.729  55.703  1.00 55.72           C  
-HETATM32953  O3' UMP G 701      16.846  80.110  53.883  1.00 54.04           O  
-HETATM32954  O4' UMP G 701      19.215  81.546  55.497  1.00 72.04           O  
-HETATM32955  C5' UMP G 701      17.836  80.154  57.115  1.00 60.73           C  
-HETATM32956  O5' UMP G 701      18.718  79.154  57.479  1.00 56.50           O  
-HETATM32957  P   UMP G 701      18.249  77.641  57.875  1.00 49.87           P  
-HETATM32958  OP1 UMP G 701      18.479  77.002  56.557  1.00 35.58           O  
-HETATM32959  OP2 UMP G 701      19.231  77.293  59.002  1.00 44.64           O  
-HETATM32960  OP3 UMP G 701      16.839  77.581  58.300  1.00 56.82           O  
-HETATM32961  CAG 1UG G 702      23.197  88.357  52.495  1.00 99.71           C  
-HETATM32962  CAE 1UG G 702      23.374  89.684  52.198  1.00103.81           C  
-HETATM32963  CAJ 1UG G 702      22.362  90.608  52.370  1.00109.09           C  
-HETATM32964  CAU 1UG G 702      21.139  90.226  52.858  1.00108.37           C  
-HETATM32965  CAI 1UG G 702      20.187  91.241  53.000  1.00107.53           C  
-HETATM32966  CAC 1UG G 702      18.941  90.928  53.480  1.00108.68           C  
-HETATM32967  CAD 1UG G 702      18.728  89.601  53.792  1.00112.93           C  
-HETATM32968  CAL 1UG G 702      19.674  88.573  53.654  1.00116.48           C  
-HETATM32969  CAX 1UG G 702      20.936  88.874  53.171  1.00106.97           C  
-HETATM32970  CAR 1UG G 702      21.982  87.928  52.987  1.00101.35           C  
-HETATM32971  SAP 1UG G 702      21.964  86.192  53.298  1.00104.82           S  
-HETATM32972  CAS 1UG G 702      22.075  85.980  55.133  1.00110.08           C  
-HETATM32973  CAY 1UG G 702      21.018  85.475  55.820  1.00111.90           C  
-HETATM32974  CAZ 1UG G 702      19.776  85.050  55.460  1.00102.92           C  
-HETATM32975  CAT 1UG G 702      19.102  84.956  54.285  1.00 95.15           C  
-HETATM32976  OAB 1UG G 702      19.576  85.290  53.201  1.00 95.62           O  
-HETATM32977  NAN 1UG G 702      17.796  84.460  54.250  1.00 85.76           N  
-HETATM32978  CAQ 1UG G 702      17.194  84.064  55.431  1.00 76.77           C  
-HETATM32979  NAA 1UG G 702      15.957  83.592  55.403  1.00 69.86           N  
-HETATM32980  NAM 1UG G 702      17.889  84.169  56.569  1.00 82.06           N  
-HETATM32981  CAW 1UG G 702      19.147  84.650  56.583  1.00 97.35           C  
-HETATM32982  NAO 1UG G 702      19.970  84.821  57.608  1.00105.59           N  
-HETATM32983  CAV 1UG G 702      21.120  85.325  57.163  1.00114.60           C  
-HETATM32984  CAK 1UG G 702      22.232  85.654  57.854  1.00114.18           C  
-HETATM32985  CAF 1UG G 702      23.343  86.172  57.195  1.00112.09           C  
-HETATM32986  CAH 1UG G 702      23.254  86.332  55.819  1.00111.14           C  
-HETATM32987  N1  FOL G 703      29.910  97.740  14.926  1.00 26.10           N  
-HETATM32988  C2  FOL G 703      30.445  97.091  15.985  1.00 26.67           C  
-HETATM32989  NA2 FOL G 703      29.764  96.139  16.649  1.00 36.40           N  
-HETATM32990  N3  FOL G 703      31.679  97.330  16.463  1.00 28.11           N  
-HETATM32991  C4  FOL G 703      32.492  98.244  15.921  1.00 38.07           C  
-HETATM32992  O4  FOL G 703      33.638  98.509  16.317  1.00 41.25           O  
-HETATM32993  C4A FOL G 703      31.991  98.986  14.778  1.00 37.00           C  
-HETATM32994  N5  FOL G 703      32.801  99.911  14.224  1.00 36.51           N  
-HETATM32995  C6  FOL G 703      32.350 100.587  13.190  1.00 44.03           C  
-HETATM32996  C7  FOL G 703      31.052 100.292  12.728  1.00 47.48           C  
-HETATM32997  N8  FOL G 703      30.177  99.362  13.252  1.00 34.40           N  
-HETATM32998  C8A FOL G 703      30.621  98.676  14.297  1.00 33.94           C  
-HETATM32999  C9  FOL G 703      33.253 101.642  12.541  1.00 47.30           C  
-HETATM33000  N10 FOL G 703      34.701 101.509  12.755  1.00 36.17           N  
-HETATM33001  C11 FOL G 703      37.099  98.483  11.168  1.00 41.72           C  
-HETATM33002  C12 FOL G 703      35.730  98.315  11.277  1.00 45.05           C  
-HETATM33003  C13 FOL G 703      34.929  99.336  11.808  1.00 45.34           C  
-HETATM33004  C14 FOL G 703      35.505 100.527  12.238  1.00 36.34           C  
-HETATM33005  C15 FOL G 703      36.887 100.703  12.135  1.00 27.79           C  
-HETATM33006  C16 FOL G 703      37.684  99.682  11.602  1.00 33.76           C  
-HETATM33007  C   FOL G 703      37.858  97.317  10.593  1.00 60.37           C  
-HETATM33008  O   FOL G 703      38.976  97.454  10.132  1.00 59.46           O  
-HETATM33009  N   FOL G 703      37.262  96.120  10.627  1.00 68.68           N  
-HETATM33010  CA  FOL G 703      37.787  94.840  10.161  1.00 66.65           C  
-HETATM33011  CB  FOL G 703      37.904  93.881  11.360  1.00 64.03           C  
-HETATM33012  CG  FOL G 703      39.259  93.225  11.557  1.00 68.69           C  
-HETATM33013  CD  FOL G 703      39.026  91.732  11.796  1.00 74.67           C  
-HETATM33014  OE1 FOL G 703      38.931  91.259  12.973  1.00 53.75           O  
-HETATM33015  OE2 FOL G 703      38.919  90.981  10.789  1.00 86.15           O  
-HETATM33016  CT  FOL G 703      36.876  94.221   9.123  1.00 54.87           C  
-HETATM33017  O1  FOL G 703      37.425  93.624   8.167  1.00 62.73           O  
-HETATM33018  O2  FOL G 703      35.617  94.297   9.234  1.00 37.99           O  
-HETATM33019  PA  NDP G 704      28.126 109.666  10.231  1.00 28.68           P  
-HETATM33020  O1A NDP G 704      26.691 109.505  10.423  1.00 26.71           O  
-HETATM33021  O2A NDP G 704      28.975 108.496   9.995  1.00 30.64           O  
-HETATM33022  O5B NDP G 704      28.396 110.700   9.062  1.00 37.06           O  
-HETATM33023  C5B NDP G 704      27.739 111.981   9.028  1.00 41.00           C  
-HETATM33024  C4B NDP G 704      27.786 112.448   7.562  1.00 30.08           C  
-HETATM33025  O4B NDP G 704      27.193 111.418   6.709  1.00 34.15           O  
-HETATM33026  C3B NDP G 704      26.911 113.663   7.374  1.00 27.22           C  
-HETATM33027  O3B NDP G 704      27.706 114.794   7.626  1.00 34.34           O  
-HETATM33028  C2B NDP G 704      26.435 113.495   5.938  1.00 32.51           C  
-HETATM33029  O2B NDP G 704      27.539 113.677   5.021  1.00 40.52           O  
-HETATM33030  C1B NDP G 704      26.189 111.991   5.885  1.00 30.68           C  
-HETATM33031  N9A NDP G 704      24.842 111.591   6.329  1.00 35.03           N  
-HETATM33032  C8A NDP G 704      24.564 110.851   7.424  1.00 38.38           C  
-HETATM33033  N7A NDP G 704      23.238 110.644   7.574  1.00 44.38           N  
-HETATM33034  C5A NDP G 704      22.645 111.267   6.547  1.00 38.34           C  
-HETATM33035  C6A NDP G 704      21.258 111.444   6.103  1.00 45.89           C  
-HETATM33036  N6A NDP G 704      20.252 110.893   6.819  1.00 51.42           N  
-HETATM33037  N1A NDP G 704      21.046 112.166   4.972  1.00 56.11           N  
-HETATM33038  C2A NDP G 704      22.046 112.715   4.258  1.00 44.10           C  
-HETATM33039  N3A NDP G 704      23.331 112.584   4.619  1.00 39.53           N  
-HETATM33040  C4A NDP G 704      23.692 111.887   5.729  1.00 40.54           C  
-HETATM33041  O3  NDP G 704      28.829 110.531  11.394  1.00 27.55           O  
-HETATM33042  PN  NDP G 704      28.470 110.490  12.982  1.00 36.27           P  
-HETATM33043  O1N NDP G 704      27.027 110.373  13.282  1.00 21.26           O  
-HETATM33044  O2N NDP G 704      29.345 111.545  13.614  1.00 34.80           O  
-HETATM33045  O5D NDP G 704      29.159 109.123  13.423  1.00 30.50           O  
-HETATM33046  C5D NDP G 704      30.585 108.987  13.392  1.00 33.46           C  
-HETATM33047  C4D NDP G 704      31.055 108.779  14.824  1.00 34.39           C  
-HETATM33048  O4D NDP G 704      30.451 107.575  15.285  1.00 33.57           O  
-HETATM33049  C3D NDP G 704      32.533 108.518  14.877  1.00 26.13           C  
-HETATM33050  O3D NDP G 704      32.977 108.860  16.172  1.00 26.38           O  
-HETATM33051  C2D NDP G 704      32.602 107.040  14.687  1.00 25.92           C  
-HETATM33052  O2D NDP G 704      33.853 106.533  15.070  1.00 32.27           O  
-HETATM33053  C1D NDP G 704      31.453 106.574  15.517  1.00 28.24           C  
-HETATM33054  N1N NDP G 704      30.874 105.304  15.133  1.00 26.18           N  
-HETATM33055  C2N NDP G 704      30.701 104.379  16.087  1.00 24.18           C  
-HETATM33056  C3N NDP G 704      30.151 103.140  15.809  1.00 31.52           C  
-HETATM33057  C7N NDP G 704      29.976 102.133  16.919  1.00 26.74           C  
-HETATM33058  O7N NDP G 704      29.296 101.149  16.725  1.00 25.51           O  
-HETATM33059  N7N NDP G 704      30.575 102.362  18.084  1.00 23.05           N  
-HETATM33060  C4N NDP G 704      29.717 102.788  14.402  1.00 39.04           C  
-HETATM33061  C5N NDP G 704      29.961 103.874  13.473  1.00 29.78           C  
-HETATM33062  C6N NDP G 704      30.518 105.063  13.881  1.00 28.19           C  
-HETATM33063  P2B NDP G 704      27.970 115.052   4.350  1.00 37.04           P  
-HETATM33064  O1X NDP G 704      29.256 114.681   3.691  1.00 34.02           O  
-HETATM33065  O2X NDP G 704      26.795 115.360   3.471  1.00 26.99           O  
-HETATM33066  O3X NDP G 704      28.226 116.112   5.408  1.00 37.35           O  
-HETATM33067  N1  UMP H 701      39.080  57.257  46.413  1.00 68.16           N  
-HETATM33068  C2  UMP H 701      37.737  57.270  45.914  1.00 60.08           C  
-HETATM33069  N3  UMP H 701      36.741  56.891  46.690  1.00 62.83           N  
-HETATM33070  C4  UMP H 701      36.955  56.493  47.942  1.00 59.80           C  
-HETATM33071  C5  UMP H 701      38.265  56.464  48.477  1.00 67.42           C  
-HETATM33072  C6  UMP H 701      39.323  56.857  47.669  1.00 70.94           C  
-HETATM33073  O2  UMP H 701      37.429  57.627  44.750  1.00 46.18           O  
-HETATM33074  O4  UMP H 701      36.003  56.146  48.635  1.00 58.24           O  
-HETATM33075  C1' UMP H 701      40.229  57.660  45.620  1.00 59.78           C  
-HETATM33076  C2' UMP H 701      40.175  59.088  45.129  1.00 43.41           C  
-HETATM33077  C3' UMP H 701      41.640  59.479  45.062  1.00 38.57           C  
-HETATM33078  C4' UMP H 701      42.245  58.719  46.202  1.00 43.89           C  
-HETATM33079  O3' UMP H 701      42.204  58.830  43.946  1.00 40.16           O  
-HETATM33080  O4' UMP H 701      41.428  57.554  46.418  1.00 67.64           O  
-HETATM33081  C5' UMP H 701      42.607  59.556  47.443  1.00 37.58           C  
-HETATM33082  O5' UMP H 701      43.781  60.287  47.366  1.00 42.26           O  
-HETATM33083  P   UMP H 701      43.874  61.843  47.867  1.00 43.71           P  
-HETATM33084  OP1 UMP H 701      42.672  62.351  47.165  1.00 24.72           O  
-HETATM33085  OP2 UMP H 701      43.756  61.705  49.389  1.00 54.63           O  
-HETATM33086  OP3 UMP H 701      45.120  62.509  47.440  1.00 34.59           O  
-HETATM33087  CAG 1UG H 702      36.522  50.741  45.042  1.00 91.61           C  
-HETATM33088  CAE 1UG H 702      36.370  49.637  44.237  1.00 94.28           C  
-HETATM33089  CAJ 1UG H 702      37.342  48.661  44.178  1.00 89.97           C  
-HETATM33090  CAU 1UG H 702      38.486  48.771  44.923  1.00 84.02           C  
-HETATM33091  CAI 1UG H 702      39.399  47.719  44.778  1.00 75.80           C  
-HETATM33092  CAC 1UG H 702      40.570  47.751  45.489  1.00 74.20           C  
-HETATM33093  CAD 1UG H 702      40.749  48.845  46.306  1.00 80.86           C  
-HETATM33094  CAL 1UG H 702      39.849  49.908  46.462  1.00 80.72           C  
-HETATM33095  CAX 1UG H 702      38.659  49.896  45.754  1.00 80.49           C  
-HETATM33096  CAR 1UG H 702      37.654  50.902  45.819  1.00 81.70           C  
-HETATM33097  SAP 1UG H 702      37.539  52.420  46.722  1.00 78.04           S  
-HETATM33098  CAS 1UG H 702      38.807  52.671  48.052  1.00 95.31           C  
-HETATM33099  CAY 1UG H 702      39.995  53.294  47.792  1.00100.67           C  
-HETATM33100  CAZ 1UG H 702      40.578  53.819  46.674  1.00 91.67           C  
-HETATM33101  CAT 1UG H 702      40.211  53.952  45.373  1.00 82.69           C  
-HETATM33102  OAB 1UG H 702      39.132  53.560  44.930  1.00 79.66           O  
-HETATM33103  NAN 1UG H 702      41.068  54.560  44.445  1.00 79.91           N  
-HETATM33104  CAQ 1UG H 702      42.303  55.027  44.868  1.00 73.34           C  
-HETATM33105  NAA 1UG H 702      43.126  55.606  44.008  1.00 65.25           N  
-HETATM33106  NAM 1UG H 702      42.629  54.880  46.157  1.00 78.61           N  
-HETATM33107  CAW 1UG H 702      41.789  54.293  47.033  1.00 91.07           C  
-HETATM33108  NAO 1UG H 702      41.960  54.072  48.328  1.00 98.81           N  
-HETATM33109  CAV 1UG H 702      40.879  53.464  48.812  1.00105.37           C  
-HETATM33110  CAK 1UG H 702      40.636  53.059  50.076  1.00105.05           C  
-HETATM33111  CAF 1UG H 702      39.438  52.436  50.395  1.00104.61           C  
-HETATM33112  CAH 1UG H 702      38.520  52.251  49.369  1.00100.19           C  
-HETATM33113  N1  FOL H 703       5.859  42.140  24.429  1.00 33.92           N  
-HETATM33114  C2  FOL H 703       6.215  42.703  25.609  1.00 33.92           C  
-HETATM33115  NA2 FOL H 703       7.211  43.602  25.696  1.00 40.05           N  
-HETATM33116  N3  FOL H 703       5.619  42.421  26.782  1.00 40.38           N  
-HETATM33117  C4  FOL H 703       4.610  41.548  26.878  1.00 55.31           C  
-HETATM33118  O4  FOL H 703       4.014  41.239  27.922  1.00 57.51           O  
-HETATM33119  C4A FOL H 703       4.168  40.903  25.655  1.00 50.43           C  
-HETATM33120  N5  FOL H 703       3.153  40.026  25.751  1.00 50.02           N  
-HETATM33121  C6  FOL H 703       2.746  39.435  24.651  1.00 62.04           C  
-HETATM33122  C7  FOL H 703       3.392  39.759  23.441  1.00 60.30           C  
-HETATM33123  N8  FOL H 703       4.436  40.644  23.286  1.00 45.60           N  
-HETATM33124  C8A FOL H 703       4.861  41.250  24.389  1.00 39.97           C  
-HETATM33125  C9  FOL H 703       1.590  38.436  24.761  1.00 64.61           C  
-HETATM33126  N10 FOL H 703       0.762  38.558  25.968  1.00 52.58           N  
-HETATM33127  C11 FOL H 703      -2.149  41.476  26.593  1.00 66.26           C  
-HETATM33128  C12 FOL H 703      -1.225  41.622  25.573  1.00 56.63           C  
-HETATM33129  C13 FOL H 703      -0.251  40.639  25.364  1.00 52.33           C  
-HETATM33130  C14 FOL H 703      -0.195  39.514  26.180  1.00 52.35           C  
-HETATM33131  C15 FOL H 703      -1.118  39.362  27.215  1.00 52.57           C  
-HETATM33132  C16 FOL H 703      -2.097  40.347  27.425  1.00 60.62           C  
-HETATM33133  C   FOL H 703      -3.167  42.567  26.776  1.00 74.60           C  
-HETATM33134  O   FOL H 703      -4.135  42.373  27.488  1.00 81.00           O  
-HETATM33135  N   FOL H 703      -2.995  43.739  26.162  1.00 71.67           N  
-HETATM33136  CA  FOL H 703      -3.909  44.875  26.252  1.00 90.88           C  
-HETATM33137  CB  FOL H 703      -3.746  45.612  27.606  1.00 84.29           C  
-HETATM33138  CG  FOL H 703      -2.532  46.529  27.792  1.00 82.21           C  
-HETATM33139  CD  FOL H 703      -2.493  46.983  29.256  1.00 81.33           C  
-HETATM33140  OE1 FOL H 703      -2.760  46.170  30.194  1.00 86.99           O  
-HETATM33141  OE2 FOL H 703      -2.198  48.182  29.502  1.00 67.34           O  
-HETATM33142  CT  FOL H 703      -3.743  45.813  25.073  1.00 93.65           C  
-HETATM33143  O1  FOL H 703      -4.792  46.186  24.503  1.00 88.28           O  
-HETATM33144  O2  FOL H 703      -2.600  46.192  24.684  1.00 81.85           O  
-HETATM33145  PA  NDP H 704       3.101  30.190  19.651  1.00 62.23           P  
-HETATM33146  O1A NDP H 704       4.163  30.980  19.042  1.00 63.93           O  
-HETATM33147  O2A NDP H 704       1.996  30.873  20.332  1.00 53.35           O  
-HETATM33148  O5B NDP H 704       2.453  29.247  18.552  1.00 89.00           O  
-HETATM33149  C5B NDP H 704       2.754  27.849  18.367  1.00 87.12           C  
-HETATM33150  C4B NDP H 704       1.637  27.379  17.410  1.00 89.65           C  
-HETATM33151  O4B NDP H 704       1.481  28.405  16.378  1.00 86.58           O  
-HETATM33152  C3B NDP H 704       1.991  26.113  16.659  1.00 99.20           C  
-HETATM33153  O3B NDP H 704       1.525  25.000  17.383  1.00 98.68           O  
-HETATM33154  C2B NDP H 704       1.399  26.329  15.262  1.00 99.65           C  
-HETATM33155  O2B NDP H 704      -0.037  26.097  15.187  1.00 93.84           O  
-HETATM33156  C1B NDP H 704       1.576  27.835  15.079  1.00 92.38           C  
-HETATM33157  N9A NDP H 704       2.863  28.172  14.437  1.00 92.51           N  
-HETATM33158  C8A NDP H 704       3.900  28.812  15.023  1.00 88.96           C  
-HETATM33159  N7A NDP H 704       4.942  28.973  14.180  1.00 90.23           N  
-HETATM33160  C5A NDP H 704       4.570  28.421  13.020  1.00 93.51           C  
-HETATM33161  C6A NDP H 704       5.201  28.246  11.705  1.00 98.29           C  
-HETATM33162  N6A NDP H 704       6.453  28.710  11.491  1.00 90.45           N  
-HETATM33163  N1A NDP H 704       4.483  27.613  10.743  1.00107.99           N  
-HETATM33164  C2A NDP H 704       3.237  27.149  10.951  1.00108.88           C  
-HETATM33165  N3A NDP H 704       2.613  27.282  12.129  1.00101.28           N  
-HETATM33166  C4A NDP H 704       3.212  27.895  13.184  1.00 93.80           C  
-HETATM33167  O3  NDP H 704       3.614  29.015  20.634  1.00 65.74           O  
-HETATM33168  PN  NDP H 704       4.831  29.070  21.719  1.00 63.64           P  
-HETATM33169  O1N NDP H 704       6.191  29.045  21.146  1.00 54.01           O  
-HETATM33170  O2N NDP H 704       4.418  28.118  22.810  1.00 62.09           O  
-HETATM33171  O5D NDP H 704       4.622  30.509  22.382  1.00 56.12           O  
-HETATM33172  C5D NDP H 704       3.653  30.694  23.424  1.00 55.81           C  
-HETATM33173  C4D NDP H 704       4.396  30.882  24.738  1.00 43.13           C  
-HETATM33174  O4D NDP H 704       5.107  32.110  24.654  1.00 40.08           O  
-HETATM33175  C3D NDP H 704       3.436  31.069  25.878  1.00 40.38           C  
-HETATM33176  O3D NDP H 704       4.087  30.652  27.062  1.00 35.20           O  
-HETATM33177  C2D NDP H 704       3.241  32.547  25.908  1.00 37.85           C  
-HETATM33178  O2D NDP H 704       2.674  32.964  27.125  1.00 40.28           O  
-HETATM33179  C1D NDP H 704       4.631  33.023  25.652  1.00 36.27           C  
-HETATM33180  N1N NDP H 704       4.743  34.350  25.088  1.00 37.94           N  
-HETATM33181  C2N NDP H 704       5.598  35.206  25.664  1.00 37.42           C  
-HETATM33182  C3N NDP H 704       5.769  36.493  25.187  1.00 40.83           C  
-HETATM33183  C7N NDP H 704       6.744  37.420  25.870  1.00 40.76           C  
-HETATM33184  O7N NDP H 704       6.996  38.493  25.366  1.00 45.48           O  
-HETATM33185  N7N NDP H 704       7.306  37.031  27.010  1.00 39.89           N  
-HETATM33186  C4N NDP H 704       4.993  36.976  23.980  1.00 42.44           C  
-HETATM33187  C5N NDP H 704       4.109  35.952  23.458  1.00 42.73           C  
-HETATM33188  C6N NDP H 704       4.030  34.704  24.030  1.00 42.13           C  
-HETATM33189  P2B NDP H 704      -0.663  24.765  14.572  1.00 95.95           P  
-HETATM33190  O1X NDP H 704      -2.126  25.051  14.589  1.00 79.11           O  
-HETATM33191  O2X NDP H 704       0.041  24.663  13.252  1.00 95.93           O  
-HETATM33192  O3X NDP H 704      -0.343  23.586  15.475  1.00 79.82           O  
-CONECT32185321863219032193                                                      
-CONECT32186321853218732191                                                      
-CONECT321873218632188                                                           
-CONECT32188321873218932192                                                      
-CONECT321893218832190                                                           
-CONECT321903218532189                                                           
-CONECT3219132186                                                                
-CONECT3219232188                                                                
-CONECT32193321853219432198                                                      
-CONECT321943219332195                                                           
-CONECT32195321943219632197                                                      
-CONECT32196321953219832199                                                      
-CONECT3219732195                                                                
-CONECT321983219332196                                                           
-CONECT321993219632200                                                           
-CONECT322003219932201                                                           
-CONECT3220132200322023220332204                                                 
-CONECT3220232201                                                                
-CONECT3220332201                                                                
-CONECT3220432201                                                                
-CONECT322053220632214                                                           
-CONECT322063220532207                                                           
-CONECT322073220632208                                                           
-CONECT32208322073220932213                                                      
-CONECT322093220832210                                                           
-CONECT322103220932211                                                           
-CONECT322113221032212                                                           
-CONECT322123221132213                                                           
-CONECT32213322083221232214                                                      
-CONECT32214322053221332215                                                      
-CONECT322153221432216                                                           
-CONECT32216322153221732230                                                      
-CONECT32217322163221832227                                                      
-CONECT32218322173221932225                                                      
-CONECT32219322183222032221                                                      
-CONECT3222032219                                                                
-CONECT322213221932222                                                           
-CONECT32222322213222332224                                                      
-CONECT3222332222                                                                
-CONECT322243222232225                                                           
-CONECT32225322183222432226                                                      
-CONECT322263222532227                                                           
-CONECT32227322173222632228                                                      
-CONECT322283222732229                                                           
-CONECT322293222832230                                                           
-CONECT322303221632229                                                           
-CONECT322313223232242                                                           
-CONECT32232322313223332234                                                      
-CONECT3223332232                                                                
-CONECT322343223232235                                                           
-CONECT32235322343223632237                                                      
-CONECT3223632235                                                                
-CONECT32237322353223832242                                                      
-CONECT322383223732239                                                           
-CONECT32239322383224032243                                                      
-CONECT322403223932241                                                           
-CONECT322413224032242                                                           
-CONECT32242322313223732241                                                      
-CONECT322433223932244                                                           
-CONECT322443224332248                                                           
-CONECT32245322463225032251                                                      
-CONECT322463224532247                                                           
-CONECT322473224632248                                                           
-CONECT32248322443224732249                                                      
-CONECT322493224832250                                                           
-CONECT322503224532249                                                           
-CONECT32251322453225232253                                                      
-CONECT3225232251                                                                
-CONECT322533225132254                                                           
-CONECT32254322533225532260                                                      
-CONECT322553225432256                                                           
-CONECT322563225532257                                                           
-CONECT32257322563225832259                                                      
-CONECT3225832257                                                                
-CONECT3225932257                                                                
-CONECT32260322543226132262                                                      
-CONECT3226132260                                                                
-CONECT3226232260                                                                
-CONECT3226332264322653226632285                                                 
-CONECT3226432263                                                                
-CONECT3226532263                                                                
-CONECT322663226332267                                                           
-CONECT322673226632268                                                           
-CONECT32268322673226932270                                                      
-CONECT322693226832274                                                           
-CONECT32270322683227132272                                                      
-CONECT3227132270                                                                
-CONECT32272322703227332274                                                      
-CONECT322733227232307                                                           
-CONECT32274322693227232275                                                      
-CONECT32275322743227632284                                                      
-CONECT322763227532277                                                           
-CONECT322773227632278                                                           
-CONECT32278322773227932284                                                      
-CONECT32279322783228032281                                                      
-CONECT3228032279                                                                
-CONECT322813227932282                                                           
-CONECT322823228132283                                                           
-CONECT322833228232284                                                           
-CONECT32284322753227832283                                                      
-CONECT322853226332286                                                           
-CONECT3228632285322873228832289                                                 
-CONECT3228732286                                                                
-CONECT3228832286                                                                
-CONECT322893228632290                                                           
-CONECT322903228932291                                                           
-CONECT32291322903229232293                                                      
-CONECT322923229132297                                                           
-CONECT32293322913229432295                                                      
-CONECT3229432293                                                                
-CONECT32295322933229632297                                                      
-CONECT3229632295                                                                
-CONECT32297322923229532298                                                      
-CONECT32298322973229932306                                                      
-CONECT322993229832300                                                           
-CONECT32300322993230132304                                                      
-CONECT32301323003230232303                                                      
-CONECT3230232301                                                                
-CONECT3230332301                                                                
-CONECT323043230032305                                                           
-CONECT323053230432306                                                           
-CONECT323063229832305                                                           
-CONECT3230732273323083230932310                                                 
-CONECT3230832307                                                                
-CONECT3230932307                                                                
-CONECT3231032307                                                                
-CONECT32311323123231632319                                                      
-CONECT32312323113231332317                                                      
-CONECT323133231232314                                                           
-CONECT32314323133231532318                                                      
-CONECT323153231432316                                                           
-CONECT323163231132315                                                           
-CONECT3231732312                                                                
-CONECT3231832314                                                                
-CONECT32319323113232032324                                                      
-CONECT323203231932321                                                           
-CONECT32321323203232232323                                                      
-CONECT32322323213232432325                                                      
-CONECT3232332321                                                                
-CONECT323243231932322                                                           
-CONECT323253232232326                                                           
-CONECT323263232532327                                                           
-CONECT3232732326323283232932330                                                 
-CONECT3232832327                                                                
-CONECT3232932327                                                                
-CONECT3233032327                                                                
-CONECT323313233232340                                                           
-CONECT323323233132333                                                           
-CONECT323333233232334                                                           
-CONECT32334323333233532339                                                      
-CONECT323353233432336                                                           
-CONECT323363233532337                                                           
-CONECT323373233632338                                                           
-CONECT323383233732339                                                           
-CONECT32339323343233832340                                                      
-CONECT32340323313233932341                                                      
-CONECT323413234032342                                                           
-CONECT32342323413234332356                                                      
-CONECT32343323423234432353                                                      
-CONECT32344323433234532351                                                      
-CONECT32345323443234632347                                                      
-CONECT3234632345                                                                
-CONECT323473234532348                                                           
-CONECT32348323473234932350                                                      
-CONECT3234932348                                                                
-CONECT323503234832351                                                           
-CONECT32351323443235032352                                                      
-CONECT323523235132353                                                           
-CONECT32353323433235232354                                                      
-CONECT323543235332355                                                           
-CONECT323553235432356                                                           
-CONECT323563234232355                                                           
-CONECT323573235832368                                                           
-CONECT32358323573235932360                                                      
-CONECT3235932358                                                                
-CONECT323603235832361                                                           
-CONECT32361323603236232363                                                      
-CONECT3236232361                                                                
-CONECT32363323613236432368                                                      
-CONECT323643236332365                                                           
-CONECT32365323643236632369                                                      
-CONECT323663236532367                                                           
-CONECT323673236632368                                                           
-CONECT32368323573236332367                                                      
-CONECT323693236532370                                                           
-CONECT323703236932374                                                           
-CONECT32371323723237632377                                                      
-CONECT323723237132373                                                           
-CONECT323733237232374                                                           
-CONECT32374323703237332375                                                      
-CONECT323753237432376                                                           
-CONECT323763237132375                                                           
-CONECT32377323713237832379                                                      
-CONECT3237832377                                                                
-CONECT323793237732380                                                           
-CONECT32380323793238132386                                                      
-CONECT323813238032382                                                           
-CONECT323823238132383                                                           
-CONECT32383323823238432385                                                      
-CONECT3238432383                                                                
-CONECT3238532383                                                                
-CONECT32386323803238732388                                                      
-CONECT3238732386                                                                
-CONECT3238832386                                                                
-CONECT3238932390323913239232411                                                 
-CONECT3239032389                                                                
-CONECT3239132389                                                                
-CONECT323923238932393                                                           
-CONECT323933239232394                                                           
-CONECT32394323933239532396                                                      
-CONECT323953239432400                                                           
-CONECT32396323943239732398                                                      
-CONECT3239732396                                                                
-CONECT32398323963239932400                                                      
-CONECT323993239832433                                                           
-CONECT32400323953239832401                                                      
-CONECT32401324003240232410                                                      
-CONECT324023240132403                                                           
-CONECT324033240232404                                                           
-CONECT32404324033240532410                                                      
-CONECT32405324043240632407                                                      
-CONECT3240632405                                                                
-CONECT324073240532408                                                           
-CONECT324083240732409                                                           
-CONECT324093240832410                                                           
-CONECT32410324013240432409                                                      
-CONECT324113238932412                                                           
-CONECT3241232411324133241432415                                                 
-CONECT3241332412                                                                
-CONECT3241432412                                                                
-CONECT324153241232416                                                           
-CONECT324163241532417                                                           
-CONECT32417324163241832419                                                      
-CONECT324183241732423                                                           
-CONECT32419324173242032421                                                      
-CONECT3242032419                                                                
-CONECT32421324193242232423                                                      
-CONECT3242232421                                                                
-CONECT32423324183242132424                                                      
-CONECT32424324233242532432                                                      
-CONECT324253242432426                                                           
-CONECT32426324253242732430                                                      
-CONECT32427324263242832429                                                      
-CONECT3242832427                                                                
-CONECT3242932427                                                                
-CONECT324303242632431                                                           
-CONECT324313243032432                                                           
-CONECT324323242432431                                                           
-CONECT3243332399324343243532436                                                 
-CONECT3243432433                                                                
-CONECT3243532433                                                                
-CONECT3243632433                                                                
-CONECT32437324383244232445                                                      
-CONECT32438324373243932443                                                      
-CONECT324393243832440                                                           
-CONECT32440324393244132444                                                      
-CONECT324413244032442                                                           
-CONECT324423243732441                                                           
-CONECT3244332438                                                                
-CONECT3244432440                                                                
-CONECT32445324373244632450                                                      
-CONECT324463244532447                                                           
-CONECT32447324463244832449                                                      
-CONECT32448324473245032451                                                      
-CONECT3244932447                                                                
-CONECT324503244532448                                                           
-CONECT324513244832452                                                           
-CONECT324523245132453                                                           
-CONECT3245332452324543245532456                                                 
-CONECT3245432453                                                                
-CONECT3245532453                                                                
-CONECT3245632453                                                                
-CONECT324573245832466                                                           
-CONECT324583245732459                                                           
-CONECT324593245832460                                                           
-CONECT32460324593246132465                                                      
-CONECT324613246032462                                                           
-CONECT324623246132463                                                           
-CONECT324633246232464                                                           
-CONECT324643246332465                                                           
-CONECT32465324603246432466                                                      
-CONECT32466324573246532467                                                      
-CONECT324673246632468                                                           
-CONECT32468324673246932482                                                      
-CONECT32469324683247032479                                                      
-CONECT32470324693247132477                                                      
-CONECT32471324703247232473                                                      
-CONECT3247232471                                                                
-CONECT324733247132474                                                           
-CONECT32474324733247532476                                                      
-CONECT3247532474                                                                
-CONECT324763247432477                                                           
-CONECT32477324703247632478                                                      
-CONECT324783247732479                                                           
-CONECT32479324693247832480                                                      
-CONECT324803247932481                                                           
-CONECT324813248032482                                                           
-CONECT324823246832481                                                           
-CONECT324833248432494                                                           
-CONECT32484324833248532486                                                      
-CONECT3248532484                                                                
-CONECT324863248432487                                                           
-CONECT32487324863248832489                                                      
-CONECT3248832487                                                                
-CONECT32489324873249032494                                                      
-CONECT324903248932491                                                           
-CONECT32491324903249232495                                                      
-CONECT324923249132493                                                           
-CONECT324933249232494                                                           
-CONECT32494324833248932493                                                      
-CONECT324953249132496                                                           
-CONECT324963249532500                                                           
-CONECT32497324983250232503                                                      
-CONECT324983249732499                                                           
-CONECT324993249832500                                                           
-CONECT32500324963249932501                                                      
-CONECT325013250032502                                                           
-CONECT325023249732501                                                           
-CONECT32503324973250432505                                                      
-CONECT3250432503                                                                
-CONECT325053250332506                                                           
-CONECT32506325053250732512                                                      
-CONECT325073250632508                                                           
-CONECT325083250732509                                                           
-CONECT32509325083251032511                                                      
-CONECT3251032509                                                                
-CONECT3251132509                                                                
-CONECT32512325063251332514                                                      
-CONECT3251332512                                                                
-CONECT3251432512                                                                
-CONECT3251532516325173251832537                                                 
-CONECT3251632515                                                                
-CONECT3251732515                                                                
-CONECT325183251532519                                                           
-CONECT325193251832520                                                           
-CONECT32520325193252132522                                                      
-CONECT325213252032526                                                           
-CONECT32522325203252332524                                                      
-CONECT3252332522                                                                
-CONECT32524325223252532526                                                      
-CONECT325253252432559                                                           
-CONECT32526325213252432527                                                      
-CONECT32527325263252832536                                                      
-CONECT325283252732529                                                           
-CONECT325293252832530                                                           
-CONECT32530325293253132536                                                      
-CONECT32531325303253232533                                                      
-CONECT3253232531                                                                
-CONECT325333253132534                                                           
-CONECT325343253332535                                                           
-CONECT325353253432536                                                           
-CONECT32536325273253032535                                                      
-CONECT325373251532538                                                           
-CONECT3253832537325393254032541                                                 
-CONECT3253932538                                                                
-CONECT3254032538                                                                
-CONECT325413253832542                                                           
-CONECT325423254132543                                                           
-CONECT32543325423254432545                                                      
-CONECT325443254332549                                                           
-CONECT32545325433254632547                                                      
-CONECT3254632545                                                                
-CONECT32547325453254832549                                                      
-CONECT3254832547                                                                
-CONECT32549325443254732550                                                      
-CONECT32550325493255132558                                                      
-CONECT325513255032552                                                           
-CONECT32552325513255332556                                                      
-CONECT32553325523255432555                                                      
-CONECT3255432553                                                                
-CONECT3255532553                                                                
-CONECT325563255232557                                                           
-CONECT325573255632558                                                           
-CONECT325583255032557                                                           
-CONECT3255932525325603256132562                                                 
-CONECT3256032559                                                                
-CONECT3256132559                                                                
-CONECT3256232559                                                                
-CONECT32563325643256832571                                                      
-CONECT32564325633256532569                                                      
-CONECT325653256432566                                                           
-CONECT32566325653256732570                                                      
-CONECT325673256632568                                                           
-CONECT325683256332567                                                           
-CONECT3256932564                                                                
-CONECT3257032566                                                                
-CONECT32571325633257232576                                                      
-CONECT325723257132573                                                           
-CONECT32573325723257432575                                                      
-CONECT32574325733257632577                                                      
-CONECT3257532573                                                                
-CONECT325763257132574                                                           
-CONECT325773257432578                                                           
-CONECT325783257732579                                                           
-CONECT3257932578325803258132582                                                 
-CONECT3258032579                                                                
-CONECT3258132579                                                                
-CONECT3258232579                                                                
-CONECT325833258432592                                                           
-CONECT325843258332585                                                           
-CONECT325853258432586                                                           
-CONECT32586325853258732591                                                      
-CONECT325873258632588                                                           
-CONECT325883258732589                                                           
-CONECT325893258832590                                                           
-CONECT325903258932591                                                           
-CONECT32591325863259032592                                                      
-CONECT32592325833259132593                                                      
-CONECT325933259232594                                                           
-CONECT32594325933259532608                                                      
-CONECT32595325943259632605                                                      
-CONECT32596325953259732603                                                      
-CONECT32597325963259832599                                                      
-CONECT3259832597                                                                
-CONECT325993259732600                                                           
-CONECT32600325993260132602                                                      
-CONECT3260132600                                                                
-CONECT326023260032603                                                           
-CONECT32603325963260232604                                                      
-CONECT326043260332605                                                           
-CONECT32605325953260432606                                                      
-CONECT326063260532607                                                           
-CONECT326073260632608                                                           
-CONECT326083259432607                                                           
-CONECT326093261032620                                                           
-CONECT32610326093261132612                                                      
-CONECT3261132610                                                                
-CONECT326123261032613                                                           
-CONECT32613326123261432615                                                      
-CONECT3261432613                                                                
-CONECT32615326133261632620                                                      
-CONECT326163261532617                                                           
-CONECT32617326163261832621                                                      
-CONECT326183261732619                                                           
-CONECT326193261832620                                                           
-CONECT32620326093261532619                                                      
-CONECT326213261732622                                                           
-CONECT326223262132626                                                           
-CONECT32623326243262832629                                                      
-CONECT326243262332625                                                           
-CONECT326253262432626                                                           
-CONECT32626326223262532627                                                      
-CONECT326273262632628                                                           
-CONECT326283262332627                                                           
-CONECT32629326233263032631                                                      
-CONECT3263032629                                                                
-CONECT326313262932632                                                           
-CONECT32632326313263332638                                                      
-CONECT326333263232634                                                           
-CONECT326343263332635                                                           
-CONECT32635326343263632637                                                      
-CONECT3263632635                                                                
-CONECT3263732635                                                                
-CONECT32638326323263932640                                                      
-CONECT3263932638                                                                
-CONECT3264032638                                                                
-CONECT3264132642326433264432663                                                 
-CONECT3264232641                                                                
-CONECT3264332641                                                                
-CONECT326443264132645                                                           
-CONECT326453264432646                                                           
-CONECT32646326453264732648                                                      
-CONECT326473264632652                                                           
-CONECT32648326463264932650                                                      
-CONECT3264932648                                                                
-CONECT32650326483265132652                                                      
-CONECT326513265032685                                                           
-CONECT32652326473265032653                                                      
-CONECT32653326523265432662                                                      
-CONECT326543265332655                                                           
-CONECT326553265432656                                                           
-CONECT32656326553265732662                                                      
-CONECT32657326563265832659                                                      
-CONECT3265832657                                                                
-CONECT326593265732660                                                           
-CONECT326603265932661                                                           
-CONECT326613266032662                                                           
-CONECT32662326533265632661                                                      
-CONECT326633264132664                                                           
-CONECT3266432663326653266632667                                                 
-CONECT3266532664                                                                
-CONECT3266632664                                                                
-CONECT326673266432668                                                           
-CONECT326683266732669                                                           
-CONECT32669326683267032671                                                      
-CONECT326703266932675                                                           
-CONECT32671326693267232673                                                      
-CONECT3267232671                                                                
-CONECT32673326713267432675                                                      
-CONECT3267432673                                                                
-CONECT32675326703267332676                                                      
-CONECT32676326753267732684                                                      
-CONECT326773267632678                                                           
-CONECT32678326773267932682                                                      
-CONECT32679326783268032681                                                      
-CONECT3268032679                                                                
-CONECT3268132679                                                                
-CONECT326823267832683                                                           
-CONECT326833268232684                                                           
-CONECT326843267632683                                                           
-CONECT3268532651326863268732688                                                 
-CONECT3268632685                                                                
-CONECT3268732685                                                                
-CONECT3268832685                                                                
-CONECT32689326903269432697                                                      
-CONECT32690326893269132695                                                      
-CONECT326913269032692                                                           
-CONECT32692326913269332696                                                      
-CONECT326933269232694                                                           
-CONECT326943268932693                                                           
-CONECT3269532690                                                                
-CONECT3269632692                                                                
-CONECT32697326893269832702                                                      
-CONECT326983269732699                                                           
-CONECT32699326983270032701                                                      
-CONECT32700326993270232703                                                      
-CONECT3270132699                                                                
-CONECT327023269732700                                                           
-CONECT327033270032704                                                           
-CONECT327043270332705                                                           
-CONECT3270532704327063270732708                                                 
-CONECT3270632705                                                                
-CONECT3270732705                                                                
-CONECT3270832705                                                                
-CONECT327093271032718                                                           
-CONECT327103270932711                                                           
-CONECT327113271032712                                                           
-CONECT32712327113271332717                                                      
-CONECT327133271232714                                                           
-CONECT327143271332715                                                           
-CONECT327153271432716                                                           
-CONECT327163271532717                                                           
-CONECT32717327123271632718                                                      
-CONECT32718327093271732719                                                      
-CONECT327193271832720                                                           
-CONECT32720327193272132734                                                      
-CONECT32721327203272232731                                                      
-CONECT32722327213272332729                                                      
-CONECT32723327223272432725                                                      
-CONECT3272432723                                                                
-CONECT327253272332726                                                           
-CONECT32726327253272732728                                                      
-CONECT3272732726                                                                
-CONECT327283272632729                                                           
-CONECT32729327223272832730                                                      
-CONECT327303272932731                                                           
-CONECT32731327213273032732                                                      
-CONECT327323273132733                                                           
-CONECT327333273232734                                                           
-CONECT327343272032733                                                           
-CONECT327353273632746                                                           
-CONECT32736327353273732738                                                      
-CONECT3273732736                                                                
-CONECT327383273632739                                                           
-CONECT32739327383274032741                                                      
-CONECT3274032739                                                                
-CONECT32741327393274232746                                                      
-CONECT327423274132743                                                           
-CONECT32743327423274432747                                                      
-CONECT327443274332745                                                           
-CONECT327453274432746                                                           
-CONECT32746327353274132745                                                      
-CONECT327473274332748                                                           
-CONECT327483274732752                                                           
-CONECT32749327503275432755                                                      
-CONECT327503274932751                                                           
-CONECT327513275032752                                                           
-CONECT32752327483275132753                                                      
-CONECT327533275232754                                                           
-CONECT327543274932753                                                           
-CONECT32755327493275632757                                                      
-CONECT3275632755                                                                
-CONECT327573275532758                                                           
-CONECT32758327573275932764                                                      
-CONECT327593275832760                                                           
-CONECT327603275932761                                                           
-CONECT32761327603276232763                                                      
-CONECT3276232761                                                                
-CONECT3276332761                                                                
-CONECT32764327583276532766                                                      
-CONECT3276532764                                                                
-CONECT3276632764                                                                
-CONECT3276732768327693277032789                                                 
-CONECT3276832767                                                                
-CONECT3276932767                                                                
-CONECT327703276732771                                                           
-CONECT327713277032772                                                           
-CONECT32772327713277332774                                                      
-CONECT327733277232778                                                           
-CONECT32774327723277532776                                                      
-CONECT3277532774                                                                
-CONECT32776327743277732778                                                      
-CONECT327773277632811                                                           
-CONECT32778327733277632779                                                      
-CONECT32779327783278032788                                                      
-CONECT327803277932781                                                           
-CONECT327813278032782                                                           
-CONECT32782327813278332788                                                      
-CONECT32783327823278432785                                                      
-CONECT3278432783                                                                
-CONECT327853278332786                                                           
-CONECT327863278532787                                                           
-CONECT327873278632788                                                           
-CONECT32788327793278232787                                                      
-CONECT327893276732790                                                           
-CONECT3279032789327913279232793                                                 
-CONECT3279132790                                                                
-CONECT3279232790                                                                
-CONECT327933279032794                                                           
-CONECT327943279332795                                                           
-CONECT32795327943279632797                                                      
-CONECT327963279532801                                                           
-CONECT32797327953279832799                                                      
-CONECT3279832797                                                                
-CONECT32799327973280032801                                                      
-CONECT3280032799                                                                
-CONECT32801327963279932802                                                      
-CONECT32802328013280332810                                                      
-CONECT328033280232804                                                           
-CONECT32804328033280532808                                                      
-CONECT32805328043280632807                                                      
-CONECT3280632805                                                                
-CONECT3280732805                                                                
-CONECT328083280432809                                                           
-CONECT328093280832810                                                           
-CONECT328103280232809                                                           
-CONECT3281132777328123281332814                                                 
-CONECT3281232811                                                                
-CONECT3281332811                                                                
-CONECT3281432811                                                                
-CONECT32815328163282032823                                                      
-CONECT32816328153281732821                                                      
-CONECT328173281632818                                                           
-CONECT32818328173281932822                                                      
-CONECT328193281832820                                                           
-CONECT328203281532819                                                           
-CONECT3282132816                                                                
-CONECT3282232818                                                                
-CONECT32823328153282432828                                                      
-CONECT328243282332825                                                           
-CONECT32825328243282632827                                                      
-CONECT32826328253282832829                                                      
-CONECT3282732825                                                                
-CONECT328283282332826                                                           
-CONECT328293282632830                                                           
-CONECT328303282932831                                                           
-CONECT3283132830328323283332834                                                 
-CONECT3283232831                                                                
-CONECT3283332831                                                                
-CONECT3283432831                                                                
-CONECT328353283632844                                                           
-CONECT328363283532837                                                           
-CONECT328373283632838                                                           
-CONECT32838328373283932843                                                      
-CONECT328393283832840                                                           
-CONECT328403283932841                                                           
-CONECT328413284032842                                                           
-CONECT328423284132843                                                           
-CONECT32843328383284232844                                                      
-CONECT32844328353284332845                                                      
-CONECT328453284432846                                                           
-CONECT32846328453284732860                                                      
-CONECT32847328463284832857                                                      
-CONECT32848328473284932855                                                      
-CONECT32849328483285032851                                                      
-CONECT3285032849                                                                
-CONECT328513284932852                                                           
-CONECT32852328513285332854                                                      
-CONECT3285332852                                                                
-CONECT328543285232855                                                           
-CONECT32855328483285432856                                                      
-CONECT328563285532857                                                           
-CONECT32857328473285632858                                                      
-CONECT328583285732859                                                           
-CONECT328593285832860                                                           
-CONECT328603284632859                                                           
-CONECT328613286232872                                                           
-CONECT32862328613286332864                                                      
-CONECT3286332862                                                                
-CONECT328643286232865                                                           
-CONECT32865328643286632867                                                      
-CONECT3286632865                                                                
-CONECT32867328653286832872                                                      
-CONECT328683286732869                                                           
-CONECT32869328683287032873                                                      
-CONECT328703286932871                                                           
-CONECT328713287032872                                                           
-CONECT32872328613286732871                                                      
-CONECT328733286932874                                                           
-CONECT328743287332878                                                           
-CONECT32875328763288032881                                                      
-CONECT328763287532877                                                           
-CONECT328773287632878                                                           
-CONECT32878328743287732879                                                      
-CONECT328793287832880                                                           
-CONECT328803287532879                                                           
-CONECT32881328753288232883                                                      
-CONECT3288232881                                                                
-CONECT328833288132884                                                           
-CONECT32884328833288532890                                                      
-CONECT328853288432886                                                           
-CONECT328863288532887                                                           
-CONECT32887328863288832889                                                      
-CONECT3288832887                                                                
-CONECT3288932887                                                                
-CONECT32890328843289132892                                                      
-CONECT3289132890                                                                
-CONECT3289232890                                                                
-CONECT3289332894328953289632915                                                 
-CONECT3289432893                                                                
-CONECT3289532893                                                                
-CONECT328963289332897                                                           
-CONECT328973289632898                                                           
-CONECT32898328973289932900                                                      
-CONECT328993289832904                                                           
-CONECT32900328983290132902                                                      
-CONECT3290132900                                                                
-CONECT32902329003290332904                                                      
-CONECT329033290232937                                                           
-CONECT32904328993290232905                                                      
-CONECT32905329043290632914                                                      
-CONECT329063290532907                                                           
-CONECT329073290632908                                                           
-CONECT32908329073290932914                                                      
-CONECT32909329083291032911                                                      
-CONECT3291032909                                                                
-CONECT329113290932912                                                           
-CONECT329123291132913                                                           
-CONECT329133291232914                                                           
-CONECT32914329053290832913                                                      
-CONECT329153289332916                                                           
-CONECT3291632915329173291832919                                                 
-CONECT3291732916                                                                
-CONECT3291832916                                                                
-CONECT329193291632920                                                           
-CONECT329203291932921                                                           
-CONECT32921329203292232923                                                      
-CONECT329223292132927                                                           
-CONECT32923329213292432925                                                      
-CONECT3292432923                                                                
-CONECT32925329233292632927                                                      
-CONECT3292632925                                                                
-CONECT32927329223292532928                                                      
-CONECT32928329273292932936                                                      
-CONECT329293292832930                                                           
-CONECT32930329293293132934                                                      
-CONECT32931329303293232933                                                      
-CONECT3293232931                                                                
-CONECT3293332931                                                                
-CONECT329343293032935                                                           
-CONECT329353293432936                                                           
-CONECT329363292832935                                                           
-CONECT3293732903329383293932940                                                 
-CONECT3293832937                                                                
-CONECT3293932937                                                                
-CONECT3294032937                                                                
-CONECT32941329423294632949                                                      
-CONECT32942329413294332947                                                      
-CONECT329433294232944                                                           
-CONECT32944329433294532948                                                      
-CONECT329453294432946                                                           
-CONECT329463294132945                                                           
-CONECT3294732942                                                                
-CONECT3294832944                                                                
-CONECT32949329413295032954                                                      
-CONECT329503294932951                                                           
-CONECT32951329503295232953                                                      
-CONECT32952329513295432955                                                      
-CONECT3295332951                                                                
-CONECT329543294932952                                                           
-CONECT329553295232956                                                           
-CONECT329563295532957                                                           
-CONECT3295732956329583295932960                                                 
-CONECT3295832957                                                                
-CONECT3295932957                                                                
-CONECT3296032957                                                                
-CONECT329613296232970                                                           
-CONECT329623296132963                                                           
-CONECT329633296232964                                                           
-CONECT32964329633296532969                                                      
-CONECT329653296432966                                                           
-CONECT329663296532967                                                           
-CONECT329673296632968                                                           
-CONECT329683296732969                                                           
-CONECT32969329643296832970                                                      
-CONECT32970329613296932971                                                      
-CONECT329713297032972                                                           
-CONECT32972329713297332986                                                      
-CONECT32973329723297432983                                                      
-CONECT32974329733297532981                                                      
-CONECT32975329743297632977                                                      
-CONECT3297632975                                                                
-CONECT329773297532978                                                           
-CONECT32978329773297932980                                                      
-CONECT3297932978                                                                
-CONECT329803297832981                                                           
-CONECT32981329743298032982                                                      
-CONECT329823298132983                                                           
-CONECT32983329733298232984                                                      
-CONECT329843298332985                                                           
-CONECT329853298432986                                                           
-CONECT329863297232985                                                           
-CONECT329873298832998                                                           
-CONECT32988329873298932990                                                      
-CONECT3298932988                                                                
-CONECT329903298832991                                                           
-CONECT32991329903299232993                                                      
-CONECT3299232991                                                                
-CONECT32993329913299432998                                                      
-CONECT329943299332995                                                           
-CONECT32995329943299632999                                                      
-CONECT329963299532997                                                           
-CONECT329973299632998                                                           
-CONECT32998329873299332997                                                      
-CONECT329993299533000                                                           
-CONECT330003299933004                                                           
-CONECT33001330023300633007                                                      
-CONECT330023300133003                                                           
-CONECT330033300233004                                                           
-CONECT33004330003300333005                                                      
-CONECT330053300433006                                                           
-CONECT330063300133005                                                           
-CONECT33007330013300833009                                                      
-CONECT3300833007                                                                
-CONECT330093300733010                                                           
-CONECT33010330093301133016                                                      
-CONECT330113301033012                                                           
-CONECT330123301133013                                                           
-CONECT33013330123301433015                                                      
-CONECT3301433013                                                                
-CONECT3301533013                                                                
-CONECT33016330103301733018                                                      
-CONECT3301733016                                                                
-CONECT3301833016                                                                
-CONECT3301933020330213302233041                                                 
-CONECT3302033019                                                                
-CONECT3302133019                                                                
-CONECT330223301933023                                                           
-CONECT330233302233024                                                           
-CONECT33024330233302533026                                                      
-CONECT330253302433030                                                           
-CONECT33026330243302733028                                                      
-CONECT3302733026                                                                
-CONECT33028330263302933030                                                      
-CONECT330293302833063                                                           
-CONECT33030330253302833031                                                      
-CONECT33031330303303233040                                                      
-CONECT330323303133033                                                           
-CONECT330333303233034                                                           
-CONECT33034330333303533040                                                      
-CONECT33035330343303633037                                                      
-CONECT3303633035                                                                
-CONECT330373303533038                                                           
-CONECT330383303733039                                                           
-CONECT330393303833040                                                           
-CONECT33040330313303433039                                                      
-CONECT330413301933042                                                           
-CONECT3304233041330433304433045                                                 
-CONECT3304333042                                                                
-CONECT3304433042                                                                
-CONECT330453304233046                                                           
-CONECT330463304533047                                                           
-CONECT33047330463304833049                                                      
-CONECT330483304733053                                                           
-CONECT33049330473305033051                                                      
-CONECT3305033049                                                                
-CONECT33051330493305233053                                                      
-CONECT3305233051                                                                
-CONECT33053330483305133054                                                      
-CONECT33054330533305533062                                                      
-CONECT330553305433056                                                           
-CONECT33056330553305733060                                                      
-CONECT33057330563305833059                                                      
-CONECT3305833057                                                                
-CONECT3305933057                                                                
-CONECT330603305633061                                                           
-CONECT330613306033062                                                           
-CONECT330623305433061                                                           
-CONECT3306333029330643306533066                                                 
-CONECT3306433063                                                                
-CONECT3306533063                                                                
-CONECT3306633063                                                                
-CONECT33067330683307233075                                                      
-CONECT33068330673306933073                                                      
-CONECT330693306833070                                                           
-CONECT33070330693307133074                                                      
-CONECT330713307033072                                                           
-CONECT330723306733071                                                           
-CONECT3307333068                                                                
-CONECT3307433070                                                                
-CONECT33075330673307633080                                                      
-CONECT330763307533077                                                           
-CONECT33077330763307833079                                                      
-CONECT33078330773308033081                                                      
-CONECT3307933077                                                                
-CONECT330803307533078                                                           
-CONECT330813307833082                                                           
-CONECT330823308133083                                                           
-CONECT3308333082330843308533086                                                 
-CONECT3308433083                                                                
-CONECT3308533083                                                                
-CONECT3308633083                                                                
-CONECT330873308833096                                                           
-CONECT330883308733089                                                           
-CONECT330893308833090                                                           
-CONECT33090330893309133095                                                      
-CONECT330913309033092                                                           
-CONECT330923309133093                                                           
-CONECT330933309233094                                                           
-CONECT330943309333095                                                           
-CONECT33095330903309433096                                                      
-CONECT33096330873309533097                                                      
-CONECT330973309633098                                                           
-CONECT33098330973309933112                                                      
-CONECT33099330983310033109                                                      
-CONECT33100330993310133107                                                      
-CONECT33101331003310233103                                                      
-CONECT3310233101                                                                
-CONECT331033310133104                                                           
-CONECT33104331033310533106                                                      
-CONECT3310533104                                                                
-CONECT331063310433107                                                           
-CONECT33107331003310633108                                                      
-CONECT331083310733109                                                           
-CONECT33109330993310833110                                                      
-CONECT331103310933111                                                           
-CONECT331113311033112                                                           
-CONECT331123309833111                                                           
-CONECT331133311433124                                                           
-CONECT33114331133311533116                                                      
-CONECT3311533114                                                                
-CONECT331163311433117                                                           
-CONECT33117331163311833119                                                      
-CONECT3311833117                                                                
-CONECT33119331173312033124                                                      
-CONECT331203311933121                                                           
-CONECT33121331203312233125                                                      
-CONECT331223312133123                                                           
-CONECT331233312233124                                                           
-CONECT33124331133311933123                                                      
-CONECT331253312133126                                                           
-CONECT331263312533130                                                           
-CONECT33127331283313233133                                                      
-CONECT331283312733129                                                           
-CONECT331293312833130                                                           
-CONECT33130331263312933131                                                      
-CONECT331313313033132                                                           
-CONECT331323312733131                                                           
-CONECT33133331273313433135                                                      
-CONECT3313433133                                                                
-CONECT331353313333136                                                           
-CONECT33136331353313733142                                                      
-CONECT331373313633138                                                           
-CONECT331383313733139                                                           
-CONECT33139331383314033141                                                      
-CONECT3314033139                                                                
-CONECT3314133139                                                                
-CONECT33142331363314333144                                                      
-CONECT3314333142                                                                
-CONECT3314433142                                                                
-CONECT3314533146331473314833167                                                 
-CONECT3314633145                                                                
-CONECT3314733145                                                                
-CONECT331483314533149                                                           
-CONECT331493314833150                                                           
-CONECT33150331493315133152                                                      
-CONECT331513315033156                                                           
-CONECT33152331503315333154                                                      
-CONECT3315333152                                                                
-CONECT33154331523315533156                                                      
-CONECT331553315433189                                                           
-CONECT33156331513315433157                                                      
-CONECT33157331563315833166                                                      
-CONECT331583315733159                                                           
-CONECT331593315833160                                                           
-CONECT33160331593316133166                                                      
-CONECT33161331603316233163                                                      
-CONECT3316233161                                                                
-CONECT331633316133164                                                           
-CONECT331643316333165                                                           
-CONECT331653316433166                                                           
-CONECT33166331573316033165                                                      
-CONECT331673314533168                                                           
-CONECT3316833167331693317033171                                                 
-CONECT3316933168                                                                
-CONECT3317033168                                                                
-CONECT331713316833172                                                           
-CONECT331723317133173                                                           
-CONECT33173331723317433175                                                      
-CONECT331743317333179                                                           
-CONECT33175331733317633177                                                      
-CONECT3317633175                                                                
-CONECT33177331753317833179                                                      
-CONECT3317833177                                                                
-CONECT33179331743317733180                                                      
-CONECT33180331793318133188                                                      
-CONECT331813318033182                                                           
-CONECT33182331813318333186                                                      
-CONECT33183331823318433185                                                      
-CONECT3318433183                                                                
-CONECT3318533183                                                                
-CONECT331863318233187                                                           
-CONECT331873318633188                                                           
-CONECT331883318033187                                                           
-CONECT3318933155331903319133192                                                 
-CONECT3319033189                                                                
-CONECT3319133189                                                                
-CONECT3319233189                                                                
-MASTER     1005    0   32  152  203    0  129    633072    8 1008  352          
-END                                                                             
diff --git a/plip/test/pdb/4pjt.pdb b/plip/test/pdb/4pjt.pdb
deleted file mode 100644
index cebc27c..0000000
--- a/plip/test/pdb/4pjt.pdb
+++ /dev/null
@@ -1,22489 +0,0 @@
-HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       12-MAY-14   4PJT              
-TITLE     STRUCTURE OF PARP1 CATALYTIC DOMAIN BOUND TO INHIBITOR BMN 673        
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 1;                            
-COMPND   3 CHAIN: A, B, C, D;                                                   
-COMPND   4 FRAGMENT: PARP1 HELICAL AND CATALYTIC DOMAINS (UNP RESIDUES 662-     
-COMPND   5 1011);                                                               
-COMPND   6 SYNONYM: PARP-1,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 1,ARTD1,
-COMPND   7 NAD(+) ADP-RIBOSYLTRANSFERASE 1,ADPRT 1,POLY[ADP-RIBOSE] SYNTHASE 1; 
-COMPND   8 EC: 2.4.2.30;                                                        
-COMPND   9 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: PARP1, ADPRT, PPOL;                                            
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
-KEYWDS    PARP1, INHIBITOR, COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX  
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    M.AOYAGI-SCHARBER,A.S.GARDBERG,T.L.ARAKAKI                            
-REVDAT   1   24-SEP-14 4PJT    0                                                
-JRNL        AUTH   M.AOYAGI-SCHARBER,A.S.GARDBERG,B.K.YIP,B.WANG,Y.SHEN,        
-JRNL        AUTH 2 P.A.FITZPATRICK                                              
-JRNL        TITL   STRUCTURAL BASIS FOR THE INHIBITION OF POLY(ADP-RIBOSE)      
-JRNL        TITL 2 POLYMERASES 1 AND 2 BY BMN 673, A POTENT INHIBITOR DERIVED   
-JRNL        TITL 3 FROM DIHYDROPYRIDOPHTHALAZINONE.                             
-JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  70  1143 2014              
-JRNL        REFN                   ESSN 2053-230X                               
-JRNL        PMID   25195882                                                     
-JRNL        DOI    10.1107/S2053230X14015088                                    
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : REFMAC 5.8.0071                                      
-REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.94                          
-REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
-REMARK   3   NUMBER OF REFLECTIONS             : 63499                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
-REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
-REMARK   3   R VALUE            (WORKING SET) : 0.188                           
-REMARK   3   FREE R VALUE                     : 0.228                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 3387                            
-REMARK   3                                                                      
-REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
-REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
-REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
-REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
-REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4577                         
-REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.44                        
-REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
-REMARK   3   BIN FREE R VALUE SET COUNT          : 232                          
-REMARK   3   BIN FREE R VALUE                    : 0.2710                       
-REMARK   3                                                                      
-REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
-REMARK   3   PROTEIN ATOMS            : 10173                                   
-REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
-REMARK   3   HETEROGEN ATOMS          : 205                                     
-REMARK   3   SOLVENT ATOMS            : 316                                     
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 43.40                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.82                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : -0.01000                                             
-REMARK   3    B22 (A**2) : -0.07000                                             
-REMARK   3    B33 (A**2) : 0.08000                                              
-REMARK   3    B12 (A**2) : 0.00000                                              
-REMARK   3    B13 (A**2) : 0.00000                                              
-REMARK   3    B23 (A**2) : 0.00000                                              
-REMARK   3                                                                      
-REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
-REMARK   3   ESU BASED ON R VALUE                            (A): 0.324         
-REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.224         
-REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
-REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.110        
-REMARK   3                                                                      
-REMARK   3 CORRELATION COEFFICIENTS.                                            
-REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
-REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
-REMARK   3                                                                      
-REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
-REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10591 ; 0.012 ; 0.019       
-REMARK   3   BOND LENGTHS OTHERS               (A):  9888 ; 0.007 ; 0.020       
-REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14409 ; 1.461 ; 1.996       
-REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22713 ; 1.255 ; 3.000       
-REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1333 ; 5.775 ; 5.000       
-REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   425 ;37.699 ;25.294       
-REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1709 ;14.247 ;15.000       
-REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;18.128 ;15.000       
-REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1669 ; 0.078 ; 0.200       
-REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11892 ; 0.008 ; 0.021       
-REMARK   3   GENERAL PLANES OTHERS             (A):  2239 ; 0.006 ; 0.020       
-REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
-REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
-REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
-REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
-REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5359 ; 2.308 ; 3.412       
-REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5358 ; 2.307 ; 3.411       
-REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6674 ; 3.560 ; 5.100       
-REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6675 ; 3.560 ; 5.100       
-REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5232 ; 2.860 ; 3.551       
-REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5232 ; 2.859 ; 3.551       
-REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7733 ; 4.479 ; 5.235       
-REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 11799 ; 6.073 ;26.654       
-REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 11720 ; 6.024 ;26.593       
-REMARK   3                                                                      
-REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
-REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
-REMARK   3                                                                      
-REMARK   3  NCS RESTRAINTS STATISTICS                                           
-REMARK   3   NCS TYPE: LOCAL                                                    
-REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
-REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
-REMARK   3    1     A   662   1010       B   662   1010   18558  0.11  0.05     
-REMARK   3    2     A   662   1010       C   662   1010   19168  0.12  0.05     
-REMARK   3    3     A   663   1009       D   663   1009   18422  0.09  0.05     
-REMARK   3    4     B   662   1010       C   662   1010   19157  0.09  0.05     
-REMARK   3    5     B   663   1009       D   663   1009   17719  0.10  0.05     
-REMARK   3    6     C   663   1009       D   663   1009   18110  0.11  0.05     
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 1                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   A   662        A  1101                          
-REMARK   3    ORIGIN FOR THE GROUP (A): -43.7499   3.3550 -10.5927              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.0248 T22:   0.0256                                     
-REMARK   3      T33:   0.0328 T12:   0.0012                                     
-REMARK   3      T13:  -0.0015 T23:  -0.0214                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.5187 L22:   0.4526                                     
-REMARK   3      L33:   0.2806 L12:  -0.1621                                     
-REMARK   3      L13:   0.1081 L23:   0.1240                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0029 S12:   0.0104 S13:  -0.0019                       
-REMARK   3      S21:  -0.0027 S22:   0.0208 S23:  -0.0045                       
-REMARK   3      S31:   0.0175 S32:   0.0075 S33:  -0.0237                       
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 2                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   B   662        B  1101                          
-REMARK   3    ORIGIN FOR THE GROUP (A): -83.8829  -3.6409   4.2278              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.0301 T22:   0.0513                                     
-REMARK   3      T33:   0.0286 T12:  -0.0310                                     
-REMARK   3      T13:  -0.0210 T23:   0.0283                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.6863 L22:   0.8257                                     
-REMARK   3      L33:   0.8405 L12:   0.1879                                     
-REMARK   3      L13:   0.0086 L23:  -0.0585                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0204 S12:   0.0022 S13:   0.0266                       
-REMARK   3      S21:   0.0213 S22:   0.0753 S23:  -0.0344                       
-REMARK   3      S31:   0.1358 S32:  -0.1665 S33:  -0.0957                       
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 3                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   C   662        C  1101                          
-REMARK   3    ORIGIN FOR THE GROUP (A): -74.9094  33.0828 -29.1980              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.0295 T22:   0.0238                                     
-REMARK   3      T33:   0.0226 T12:   0.0015                                     
-REMARK   3      T13:   0.0138 T23:   0.0126                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.5665 L22:   0.2765                                     
-REMARK   3      L33:   1.0166 L12:  -0.2135                                     
-REMARK   3      L13:  -0.3885 L23:   0.0196                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0391 S12:   0.0503 S13:   0.0568                       
-REMARK   3      S21:   0.0200 S22:   0.0260 S23:   0.0032                       
-REMARK   3      S31:  -0.0329 S32:  -0.0317 S33:  -0.0651                       
-REMARK   3                                                                      
-REMARK   3   TLS GROUP : 4                                                      
-REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
-REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
-REMARK   3    RESIDUE RANGE :   D   663        D  1101                          
-REMARK   3    ORIGIN FOR THE GROUP (A):-116.4501  19.2024 -23.7033              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.0635 T22:   0.0636                                     
-REMARK   3      T33:   0.0337 T12:  -0.0350                                     
-REMARK   3      T13:   0.0419 T23:  -0.0311                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.7583 L22:   0.2142                                     
-REMARK   3      L33:   0.6721 L12:  -0.5210                                     
-REMARK   3      L13:   0.2224 L23:  -0.0063                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0188 S12:   0.1591 S13:  -0.0579                       
-REMARK   3      S21:  -0.0311 S22:  -0.0650 S23:  -0.0066                       
-REMARK   3      S31:   0.1355 S32:  -0.0794 S33:   0.0463                       
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED : MASK                                                 
-REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
-REMARK   3   VDW PROBE RADIUS   : 1.20                                          
-REMARK   3   ION PROBE RADIUS   : 0.80                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
-REMARK   3  POSITIONS                                                           
-REMARK   4                                                                      
-REMARK   4 4PJT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-14.                  
-REMARK 100 THE DEPOSITION ID IS D_1000201517.                                   
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-10                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 7.20                               
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : ALS                                
-REMARK 200  BEAMLINE                       : 5.0.3                              
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97648                            
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
-REMARK 200  DATA SCALING SOFTWARE          : NULL                               
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66890                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 19.940                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
-REMARK 200  DATA REDUNDANCY                : 6.900                              
-REMARK 200  R MERGE                    (I) : 0.07900                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.2000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : 0.47900                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASER                                                
-REMARK 200 STARTING MODEL: 1UK0, 3L3M                                           
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 48.90                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 100MM TRIS, PH   
-REMARK 280  7.2                                                                 
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       51.84500            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.00000            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.07500            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.00000            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.84500            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.07500            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 300 REMARK: RUNS AS MONOMER ON SIZING EXCLUSION COLUMN                   
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 2                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 3                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 4                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     MET A   642                                                      
-REMARK 465     GLY A   643                                                      
-REMARK 465     SER A   644                                                      
-REMARK 465     SER A   645                                                      
-REMARK 465     HIS A   646                                                      
-REMARK 465     HIS A   647                                                      
-REMARK 465     HIS A   648                                                      
-REMARK 465     HIS A   649                                                      
-REMARK 465     HIS A   650                                                      
-REMARK 465     HIS A   651                                                      
-REMARK 465     SER A   652                                                      
-REMARK 465     GLY A   653                                                      
-REMARK 465     LEU A   654                                                      
-REMARK 465     VAL A   655                                                      
-REMARK 465     PRO A   656                                                      
-REMARK 465     ARG A   657                                                      
-REMARK 465     GLY A   658                                                      
-REMARK 465     SER A   659                                                      
-REMARK 465     HIS A   660                                                      
-REMARK 465     MET A   661                                                      
-REMARK 465     GLY A   723                                                      
-REMARK 465     SER A   724                                                      
-REMARK 465     SER A   725                                                      
-REMARK 465     GLY A   745                                                      
-REMARK 465     MET A   746                                                      
-REMARK 465     LYS A   747                                                      
-REMARK 465     GLY A   781                                                      
-REMARK 465     SER A   782                                                      
-REMARK 465     ASP A   783                                                      
-REMARK 465     ASP A   784                                                      
-REMARK 465     SER A   785                                                      
-REMARK 465     THR A  1011                                                      
-REMARK 465     MET B   642                                                      
-REMARK 465     GLY B   643                                                      
-REMARK 465     SER B   644                                                      
-REMARK 465     SER B   645                                                      
-REMARK 465     HIS B   646                                                      
-REMARK 465     HIS B   647                                                      
-REMARK 465     HIS B   648                                                      
-REMARK 465     HIS B   649                                                      
-REMARK 465     HIS B   650                                                      
-REMARK 465     HIS B   651                                                      
-REMARK 465     SER B   652                                                      
-REMARK 465     GLY B   653                                                      
-REMARK 465     LEU B   654                                                      
-REMARK 465     VAL B   655                                                      
-REMARK 465     PRO B   656                                                      
-REMARK 465     ARG B   657                                                      
-REMARK 465     GLY B   658                                                      
-REMARK 465     SER B   659                                                      
-REMARK 465     HIS B   660                                                      
-REMARK 465     MET B   661                                                      
-REMARK 465     GLN B   722                                                      
-REMARK 465     GLY B   723                                                      
-REMARK 465     SER B   724                                                      
-REMARK 465     SER B   725                                                      
-REMARK 465     PHE B   744                                                      
-REMARK 465     GLY B   745                                                      
-REMARK 465     MET B   746                                                      
-REMARK 465     LYS B   747                                                      
-REMARK 465     LYS B   748                                                      
-REMARK 465     PRO B   749                                                      
-REMARK 465     GLY B   781                                                      
-REMARK 465     SER B   782                                                      
-REMARK 465     ASP B   783                                                      
-REMARK 465     ASP B   784                                                      
-REMARK 465     SER B   785                                                      
-REMARK 465     HIS B   937                                                      
-REMARK 465     ILE B   938                                                      
-REMARK 465     THR B  1011                                                      
-REMARK 465     MET C   642                                                      
-REMARK 465     GLY C   643                                                      
-REMARK 465     SER C   644                                                      
-REMARK 465     SER C   645                                                      
-REMARK 465     HIS C   646                                                      
-REMARK 465     HIS C   647                                                      
-REMARK 465     HIS C   648                                                      
-REMARK 465     HIS C   649                                                      
-REMARK 465     HIS C   650                                                      
-REMARK 465     HIS C   651                                                      
-REMARK 465     SER C   652                                                      
-REMARK 465     GLY C   653                                                      
-REMARK 465     LEU C   654                                                      
-REMARK 465     VAL C   655                                                      
-REMARK 465     PRO C   656                                                      
-REMARK 465     ARG C   657                                                      
-REMARK 465     GLY C   658                                                      
-REMARK 465     SER C   659                                                      
-REMARK 465     HIS C   660                                                      
-REMARK 465     MET C   661                                                      
-REMARK 465     SER C   782                                                      
-REMARK 465     ASP C   783                                                      
-REMARK 465     ASP C   784                                                      
-REMARK 465     THR C  1011                                                      
-REMARK 465     MET D   642                                                      
-REMARK 465     GLY D   643                                                      
-REMARK 465     SER D   644                                                      
-REMARK 465     SER D   645                                                      
-REMARK 465     HIS D   646                                                      
-REMARK 465     HIS D   647                                                      
-REMARK 465     HIS D   648                                                      
-REMARK 465     HIS D   649                                                      
-REMARK 465     HIS D   650                                                      
-REMARK 465     HIS D   651                                                      
-REMARK 465     SER D   652                                                      
-REMARK 465     GLY D   653                                                      
-REMARK 465     LEU D   654                                                      
-REMARK 465     VAL D   655                                                      
-REMARK 465     PRO D   656                                                      
-REMARK 465     ARG D   657                                                      
-REMARK 465     GLY D   658                                                      
-REMARK 465     SER D   659                                                      
-REMARK 465     HIS D   660                                                      
-REMARK 465     MET D   661                                                      
-REMARK 465     LYS D   662                                                      
-REMARK 465     GLN D   722                                                      
-REMARK 465     GLY D   723                                                      
-REMARK 465     SER D   724                                                      
-REMARK 465     SER D   725                                                      
-REMARK 465     ASP D   726                                                      
-REMARK 465     SER D   727                                                      
-REMARK 465     GLN D   728                                                      
-REMARK 465     ILE D   729                                                      
-REMARK 465     PHE D   744                                                      
-REMARK 465     GLY D   745                                                      
-REMARK 465     MET D   746                                                      
-REMARK 465     LYS D   747                                                      
-REMARK 465     LYS D   748                                                      
-REMARK 465     GLY D   780                                                      
-REMARK 465     GLY D   781                                                      
-REMARK 465     SER D   782                                                      
-REMARK 465     ASP D   783                                                      
-REMARK 465     ASP D   784                                                      
-REMARK 465     SER D   785                                                      
-REMARK 465     SER D   786                                                      
-REMARK 465     LYS D   787                                                      
-REMARK 465     LYS D  1010                                                      
-REMARK 465     THR D  1011                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     LYS A 662    CG   CD   CE   NZ                                   
-REMARK 470     LYS A 664    CG   CD   CE   NZ                                   
-REMARK 470     LYS A 667    CG   CD   CE   NZ                                   
-REMARK 470     LYS A 700    CG   CD   CE   NZ                                   
-REMARK 470     LEU A 701    CG   CD1  CD2                                       
-REMARK 470     LYS A 703    CG   CD   CE   NZ                                   
-REMARK 470     ARG A 704    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     GLN A 705    CG   CD   OE1  NE2                                  
-REMARK 470     ASP A 726    CG   OD1  OD2                                       
-REMARK 470     GLN A 728    CG   CD   OE1  NE2                                  
-REMARK 470     LEU A 730    CG   CD1  CD2                                       
-REMARK 470     ARG A 735    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     LYS A 748    CG   CD   CE   NZ                                   
-REMARK 470     LEU A 751    CG   CD1  CD2                                       
-REMARK 470     ARG A 779    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     SER A 786    OG                                                  
-REMARK 470     LYS A 787    CG   CD   CE   NZ                                   
-REMARK 470     ARG A 806    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     LYS A 852    CG   CD   CE   NZ                                   
-REMARK 470     LYS A 940    CG   CD   CE   NZ                                   
-REMARK 470     LYS A 943    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 662    CG   CD   CE   NZ                                   
-REMARK 470     SER B 663    OG                                                  
-REMARK 470     LYS B 664    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 667    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 684    CG   CD   CE   NZ                                   
-REMARK 470     GLU B 690    CG   CD   OE1  OE2                                  
-REMARK 470     GLN B 694    CG   CD   OE1  NE2                                  
-REMARK 470     LYS B 695    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 700    CG   CD   CE   NZ                                   
-REMARK 470     ARG B 704    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     GLN B 705    CG   CD   OE1  NE2                                  
-REMARK 470     GLN B 718    CG   CD   OE1  NE2                                  
-REMARK 470     SER B 721    OG                                                  
-REMARK 470     ASP B 726    CG   OD1  OD2                                       
-REMARK 470     SER B 727    OG                                                  
-REMARK 470     LEU B 730    CG   CD1  CD2                                       
-REMARK 470     ARG B 735    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     ASP B 743    CG   OD1  OD2                                       
-REMARK 470     LEU B 751    CG   CD1  CD2                                       
-REMARK 470     ARG B 779    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     SER B 786    OG                                                  
-REMARK 470     LYS B 787    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 796    CG   CD   CE   NZ                                   
-REMARK 470     ARG B 806    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     GLN B 912    CG   CD   OE1  NE2                                  
-REMARK 470     LYS B 933    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 940    CG   CD   CE   NZ                                   
-REMARK 470     LYS B 953    CG   CD   CE   NZ                                   
-REMARK 470     SER B 959    OG                                                  
-REMARK 470     ASN B 980    CG   OD1  ND2                                       
-REMARK 470     ASP B 981    CG   OD1  OD2                                       
-REMARK 470     LYS B1006    CG   CD   CE   NZ                                   
-REMARK 470     LYS B1010    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 662    CG   CD   CE   NZ                                   
-REMARK 470     SER C 663    OG                                                  
-REMARK 470     LYS C 664    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 667    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 695    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 700    CG   CD   CE   NZ                                   
-REMARK 470     ARG C 704    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     GLN C 728    CG   CD   OE1  NE2                                  
-REMARK 470     ASP C 731    CG   OD1  OD2                                       
-REMARK 470     LYS C 747    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 748    CG   CD   CE   NZ                                   
-REMARK 470     ARG C 779    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     SER C 786    OG                                                  
-REMARK 470     LYS C 787    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 798    CG   CD   CE   NZ                                   
-REMARK 470     ARG C 806    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     GLU C 812    CG   CD   OE1  OE2                                  
-REMARK 470     LYS C 849    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 852    CG   CD   CE   NZ                                   
-REMARK 470     SER C 939    OG                                                  
-REMARK 470     LYS C 940    CG   CD   CE   NZ                                   
-REMARK 470     ASN C 980    CG   OD1  ND2                                       
-REMARK 470     LYS C1006    CG   CD   CE   NZ                                   
-REMARK 470     LYS C1010    CG   CD   CE   NZ                                   
-REMARK 470     LYS D 664    CG   CD   CE   NZ                                   
-REMARK 470     LYS D 667    CG   CD   CE   NZ                                   
-REMARK 470     LYS D 674    CG   CD   CE   NZ                                   
-REMARK 470     GLU D 680    CG   CD   OE1  OE2                                  
-REMARK 470     LYS D 683    CG   CD   CE   NZ                                   
-REMARK 470     GLU D 690    CG   CD   OE1  OE2                                  
-REMARK 470     ASP D 692    CG   OD1  OD2                                       
-REMARK 470     LEU D 693    CG   CD1  CD2                                       
-REMARK 470     GLN D 694    CG   CD   OE1  NE2                                  
-REMARK 470     LYS D 695    CG   CD   CE   NZ                                   
-REMARK 470     LEU D 698    CG   CD1  CD2                                       
-REMARK 470     LYS D 700    CG   CD   CE   NZ                                   
-REMARK 470     LEU D 701    CG   CD1  CD2                                       
-REMARK 470     LYS D 703    CG   CD   CE   NZ                                   
-REMARK 470     ARG D 704    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     GLN D 705    CG   CD   OE1  NE2                                  
-REMARK 470     LEU D 730    CG   CD1  CD2                                       
-REMARK 470     ARG D 735    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     PRO D 749    CG   CD                                             
-REMARK 470     SER D 757    OG                                                  
-REMARK 470     LYS D 761    CG   CD   CE   NZ                                   
-REMARK 470     TYR D 775    CG   CD1  CD2  CE1  CE2  CZ   OH                    
-REMARK 470     LEU D 778    CG   CD1  CD2                                       
-REMARK 470     ARG D 779    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     LYS D 798    CG   CD   CE   NZ                                   
-REMARK 470     ASP D 805    CG   OD1  OD2                                       
-REMARK 470     ARG D 806    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     ASP D 807    CG   OD1  OD2                                       
-REMARK 470     GLU D 809    CG   CD   OE1  OE2                                  
-REMARK 470     LYS D 816    CG   CD   CE   NZ                                   
-REMARK 470     GLU D 832    CG   CD   OE1  OE2                                  
-REMARK 470     GLU D 842    CG   CD   OE1  OE2                                  
-REMARK 470     LYS D 940    CG   CD   CE   NZ                                   
-REMARK 470     SER D 959    OG                                                  
-REMARK 470     SER D 963    OG                                                  
-REMARK 470     LYS D1006    CG   CD   CE   NZ                                   
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   NZ   LYS D   953     O    HOH D  1201              2.06            
-REMARK 500   O2   SO4 C  1101     O    HOH C  1266              2.18            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    ARG A 841   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
-REMARK 500    ARG A 841   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
-REMARK 500    ARG B 841   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
-REMARK 500    ARG B 841   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
-REMARK 500    ARG C 841   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
-REMARK 500    ARG C 841   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
-REMARK 500    ARG D 841   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
-REMARK 500    ARG D 841   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    HIS A 826       66.52   -102.27                                   
-REMARK 500    SER A 936      113.97   -161.38                                   
-REMARK 500    HIS B 826       62.86   -104.33                                   
-REMARK 500    HIS C 826       63.80   -104.43                                   
-REMARK 500    SER C 939      -74.73    -98.01                                   
-REMARK 500    HIS D 826       65.44   -102.69                                   
-REMARK 500    SER D 936      113.64   -162.28                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1101                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1102                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1103                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1104                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ A 1105                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1106                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1107                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1101                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1102                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1103                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1104                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ B 1105                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1106                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1101                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1102                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1103                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ C 1104                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AD9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1105                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AE1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1101                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AE2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1102                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AE3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1103                
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AE4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ D 1104                
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 4PJV   RELATED DB: PDB                                   
-DBREF  4PJT A  662  1011  UNP    P09874   PARP1_HUMAN    662   1011             
-DBREF  4PJT B  662  1011  UNP    P09874   PARP1_HUMAN    662   1011             
-DBREF  4PJT C  662  1011  UNP    P09874   PARP1_HUMAN    662   1011             
-DBREF  4PJT D  662  1011  UNP    P09874   PARP1_HUMAN    662   1011             
-SEQADV 4PJT MET A  642  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY A  643  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER A  644  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER A  645  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS A  646  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS A  647  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS A  648  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS A  649  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS A  650  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS A  651  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER A  652  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY A  653  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT LEU A  654  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT VAL A  655  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT PRO A  656  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT ARG A  657  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY A  658  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER A  659  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS A  660  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT MET A  661  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT MET B  642  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY B  643  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER B  644  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER B  645  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS B  646  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS B  647  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS B  648  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS B  649  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS B  650  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS B  651  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER B  652  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY B  653  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT LEU B  654  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT VAL B  655  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT PRO B  656  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT ARG B  657  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY B  658  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER B  659  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS B  660  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT MET B  661  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT MET C  642  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY C  643  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER C  644  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER C  645  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS C  646  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS C  647  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS C  648  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS C  649  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS C  650  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS C  651  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER C  652  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY C  653  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT LEU C  654  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT VAL C  655  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT PRO C  656  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT ARG C  657  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY C  658  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER C  659  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS C  660  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT MET C  661  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT MET D  642  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY D  643  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER D  644  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER D  645  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS D  646  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS D  647  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS D  648  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS D  649  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS D  650  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS D  651  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER D  652  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY D  653  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT LEU D  654  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT VAL D  655  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT PRO D  656  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT ARG D  657  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT GLY D  658  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT SER D  659  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT HIS D  660  UNP  P09874              EXPRESSION TAG                 
-SEQADV 4PJT MET D  661  UNP  P09874              EXPRESSION TAG                 
-SEQRES   1 A  370  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU          
-SEQRES   2 A  370  VAL PRO ARG GLY SER HIS MET LYS SER LYS LEU PRO LYS          
-SEQRES   3 A  370  PRO VAL GLN ASP LEU ILE LYS MET ILE PHE ASP VAL GLU          
-SEQRES   4 A  370  SER MET LYS LYS ALA MET VAL GLU TYR GLU ILE ASP LEU          
-SEQRES   5 A  370  GLN LYS MET PRO LEU GLY LYS LEU SER LYS ARG GLN ILE          
-SEQRES   6 A  370  GLN ALA ALA TYR SER ILE LEU SER GLU VAL GLN GLN ALA          
-SEQRES   7 A  370  VAL SER GLN GLY SER SER ASP SER GLN ILE LEU ASP LEU          
-SEQRES   8 A  370  SER ASN ARG PHE TYR THR LEU ILE PRO HIS ASP PHE GLY          
-SEQRES   9 A  370  MET LYS LYS PRO PRO LEU LEU ASN ASN ALA ASP SER VAL          
-SEQRES  10 A  370  GLN ALA LYS VAL GLU MET LEU ASP ASN LEU LEU ASP ILE          
-SEQRES  11 A  370  GLU VAL ALA TYR SER LEU LEU ARG GLY GLY SER ASP ASP          
-SEQRES  12 A  370  SER SER LYS ASP PRO ILE ASP VAL ASN TYR GLU LYS LEU          
-SEQRES  13 A  370  LYS THR ASP ILE LYS VAL VAL ASP ARG ASP SER GLU GLU          
-SEQRES  14 A  370  ALA GLU ILE ILE ARG LYS TYR VAL LYS ASN THR HIS ALA          
-SEQRES  15 A  370  THR THR HIS ASN ALA TYR ASP LEU GLU VAL ILE ASP ILE          
-SEQRES  16 A  370  PHE LYS ILE GLU ARG GLU GLY GLU CYS GLN ARG TYR LYS          
-SEQRES  17 A  370  PRO PHE LYS GLN LEU HIS ASN ARG ARG LEU LEU TRP HIS          
-SEQRES  18 A  370  GLY SER ARG THR THR ASN PHE ALA GLY ILE LEU SER GLN          
-SEQRES  19 A  370  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO VAL THR GLY          
-SEQRES  20 A  370  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET VAL          
-SEQRES  21 A  370  SER LYS SER ALA ASN TYR CYS HIS THR SER GLN GLY ASP          
-SEQRES  22 A  370  PRO ILE GLY LEU ILE LEU LEU GLY GLU VAL ALA LEU GLY          
-SEQRES  23 A  370  ASN MET TYR GLU LEU LYS HIS ALA SER HIS ILE SER LYS          
-SEQRES  24 A  370  LEU PRO LYS GLY LYS HIS SER VAL LYS GLY LEU GLY LYS          
-SEQRES  25 A  370  THR THR PRO ASP PRO SER ALA ASN ILE SER LEU ASP GLY          
-SEQRES  26 A  370  VAL ASP VAL PRO LEU GLY THR GLY ILE SER SER GLY VAL          
-SEQRES  27 A  370  ASN ASP THR SER LEU LEU TYR ASN GLU TYR ILE VAL TYR          
-SEQRES  28 A  370  ASP ILE ALA GLN VAL ASN LEU LYS TYR LEU LEU LYS LEU          
-SEQRES  29 A  370  LYS PHE ASN PHE LYS THR                                      
-SEQRES   1 B  370  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU          
-SEQRES   2 B  370  VAL PRO ARG GLY SER HIS MET LYS SER LYS LEU PRO LYS          
-SEQRES   3 B  370  PRO VAL GLN ASP LEU ILE LYS MET ILE PHE ASP VAL GLU          
-SEQRES   4 B  370  SER MET LYS LYS ALA MET VAL GLU TYR GLU ILE ASP LEU          
-SEQRES   5 B  370  GLN LYS MET PRO LEU GLY LYS LEU SER LYS ARG GLN ILE          
-SEQRES   6 B  370  GLN ALA ALA TYR SER ILE LEU SER GLU VAL GLN GLN ALA          
-SEQRES   7 B  370  VAL SER GLN GLY SER SER ASP SER GLN ILE LEU ASP LEU          
-SEQRES   8 B  370  SER ASN ARG PHE TYR THR LEU ILE PRO HIS ASP PHE GLY          
-SEQRES   9 B  370  MET LYS LYS PRO PRO LEU LEU ASN ASN ALA ASP SER VAL          
-SEQRES  10 B  370  GLN ALA LYS VAL GLU MET LEU ASP ASN LEU LEU ASP ILE          
-SEQRES  11 B  370  GLU VAL ALA TYR SER LEU LEU ARG GLY GLY SER ASP ASP          
-SEQRES  12 B  370  SER SER LYS ASP PRO ILE ASP VAL ASN TYR GLU LYS LEU          
-SEQRES  13 B  370  LYS THR ASP ILE LYS VAL VAL ASP ARG ASP SER GLU GLU          
-SEQRES  14 B  370  ALA GLU ILE ILE ARG LYS TYR VAL LYS ASN THR HIS ALA          
-SEQRES  15 B  370  THR THR HIS ASN ALA TYR ASP LEU GLU VAL ILE ASP ILE          
-SEQRES  16 B  370  PHE LYS ILE GLU ARG GLU GLY GLU CYS GLN ARG TYR LYS          
-SEQRES  17 B  370  PRO PHE LYS GLN LEU HIS ASN ARG ARG LEU LEU TRP HIS          
-SEQRES  18 B  370  GLY SER ARG THR THR ASN PHE ALA GLY ILE LEU SER GLN          
-SEQRES  19 B  370  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO VAL THR GLY          
-SEQRES  20 B  370  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET VAL          
-SEQRES  21 B  370  SER LYS SER ALA ASN TYR CYS HIS THR SER GLN GLY ASP          
-SEQRES  22 B  370  PRO ILE GLY LEU ILE LEU LEU GLY GLU VAL ALA LEU GLY          
-SEQRES  23 B  370  ASN MET TYR GLU LEU LYS HIS ALA SER HIS ILE SER LYS          
-SEQRES  24 B  370  LEU PRO LYS GLY LYS HIS SER VAL LYS GLY LEU GLY LYS          
-SEQRES  25 B  370  THR THR PRO ASP PRO SER ALA ASN ILE SER LEU ASP GLY          
-SEQRES  26 B  370  VAL ASP VAL PRO LEU GLY THR GLY ILE SER SER GLY VAL          
-SEQRES  27 B  370  ASN ASP THR SER LEU LEU TYR ASN GLU TYR ILE VAL TYR          
-SEQRES  28 B  370  ASP ILE ALA GLN VAL ASN LEU LYS TYR LEU LEU LYS LEU          
-SEQRES  29 B  370  LYS PHE ASN PHE LYS THR                                      
-SEQRES   1 C  370  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU          
-SEQRES   2 C  370  VAL PRO ARG GLY SER HIS MET LYS SER LYS LEU PRO LYS          
-SEQRES   3 C  370  PRO VAL GLN ASP LEU ILE LYS MET ILE PHE ASP VAL GLU          
-SEQRES   4 C  370  SER MET LYS LYS ALA MET VAL GLU TYR GLU ILE ASP LEU          
-SEQRES   5 C  370  GLN LYS MET PRO LEU GLY LYS LEU SER LYS ARG GLN ILE          
-SEQRES   6 C  370  GLN ALA ALA TYR SER ILE LEU SER GLU VAL GLN GLN ALA          
-SEQRES   7 C  370  VAL SER GLN GLY SER SER ASP SER GLN ILE LEU ASP LEU          
-SEQRES   8 C  370  SER ASN ARG PHE TYR THR LEU ILE PRO HIS ASP PHE GLY          
-SEQRES   9 C  370  MET LYS LYS PRO PRO LEU LEU ASN ASN ALA ASP SER VAL          
-SEQRES  10 C  370  GLN ALA LYS VAL GLU MET LEU ASP ASN LEU LEU ASP ILE          
-SEQRES  11 C  370  GLU VAL ALA TYR SER LEU LEU ARG GLY GLY SER ASP ASP          
-SEQRES  12 C  370  SER SER LYS ASP PRO ILE ASP VAL ASN TYR GLU LYS LEU          
-SEQRES  13 C  370  LYS THR ASP ILE LYS VAL VAL ASP ARG ASP SER GLU GLU          
-SEQRES  14 C  370  ALA GLU ILE ILE ARG LYS TYR VAL LYS ASN THR HIS ALA          
-SEQRES  15 C  370  THR THR HIS ASN ALA TYR ASP LEU GLU VAL ILE ASP ILE          
-SEQRES  16 C  370  PHE LYS ILE GLU ARG GLU GLY GLU CYS GLN ARG TYR LYS          
-SEQRES  17 C  370  PRO PHE LYS GLN LEU HIS ASN ARG ARG LEU LEU TRP HIS          
-SEQRES  18 C  370  GLY SER ARG THR THR ASN PHE ALA GLY ILE LEU SER GLN          
-SEQRES  19 C  370  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO VAL THR GLY          
-SEQRES  20 C  370  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET VAL          
-SEQRES  21 C  370  SER LYS SER ALA ASN TYR CYS HIS THR SER GLN GLY ASP          
-SEQRES  22 C  370  PRO ILE GLY LEU ILE LEU LEU GLY GLU VAL ALA LEU GLY          
-SEQRES  23 C  370  ASN MET TYR GLU LEU LYS HIS ALA SER HIS ILE SER LYS          
-SEQRES  24 C  370  LEU PRO LYS GLY LYS HIS SER VAL LYS GLY LEU GLY LYS          
-SEQRES  25 C  370  THR THR PRO ASP PRO SER ALA ASN ILE SER LEU ASP GLY          
-SEQRES  26 C  370  VAL ASP VAL PRO LEU GLY THR GLY ILE SER SER GLY VAL          
-SEQRES  27 C  370  ASN ASP THR SER LEU LEU TYR ASN GLU TYR ILE VAL TYR          
-SEQRES  28 C  370  ASP ILE ALA GLN VAL ASN LEU LYS TYR LEU LEU LYS LEU          
-SEQRES  29 C  370  LYS PHE ASN PHE LYS THR                                      
-SEQRES   1 D  370  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU          
-SEQRES   2 D  370  VAL PRO ARG GLY SER HIS MET LYS SER LYS LEU PRO LYS          
-SEQRES   3 D  370  PRO VAL GLN ASP LEU ILE LYS MET ILE PHE ASP VAL GLU          
-SEQRES   4 D  370  SER MET LYS LYS ALA MET VAL GLU TYR GLU ILE ASP LEU          
-SEQRES   5 D  370  GLN LYS MET PRO LEU GLY LYS LEU SER LYS ARG GLN ILE          
-SEQRES   6 D  370  GLN ALA ALA TYR SER ILE LEU SER GLU VAL GLN GLN ALA          
-SEQRES   7 D  370  VAL SER GLN GLY SER SER ASP SER GLN ILE LEU ASP LEU          
-SEQRES   8 D  370  SER ASN ARG PHE TYR THR LEU ILE PRO HIS ASP PHE GLY          
-SEQRES   9 D  370  MET LYS LYS PRO PRO LEU LEU ASN ASN ALA ASP SER VAL          
-SEQRES  10 D  370  GLN ALA LYS VAL GLU MET LEU ASP ASN LEU LEU ASP ILE          
-SEQRES  11 D  370  GLU VAL ALA TYR SER LEU LEU ARG GLY GLY SER ASP ASP          
-SEQRES  12 D  370  SER SER LYS ASP PRO ILE ASP VAL ASN TYR GLU LYS LEU          
-SEQRES  13 D  370  LYS THR ASP ILE LYS VAL VAL ASP ARG ASP SER GLU GLU          
-SEQRES  14 D  370  ALA GLU ILE ILE ARG LYS TYR VAL LYS ASN THR HIS ALA          
-SEQRES  15 D  370  THR THR HIS ASN ALA TYR ASP LEU GLU VAL ILE ASP ILE          
-SEQRES  16 D  370  PHE LYS ILE GLU ARG GLU GLY GLU CYS GLN ARG TYR LYS          
-SEQRES  17 D  370  PRO PHE LYS GLN LEU HIS ASN ARG ARG LEU LEU TRP HIS          
-SEQRES  18 D  370  GLY SER ARG THR THR ASN PHE ALA GLY ILE LEU SER GLN          
-SEQRES  19 D  370  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO VAL THR GLY          
-SEQRES  20 D  370  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET VAL          
-SEQRES  21 D  370  SER LYS SER ALA ASN TYR CYS HIS THR SER GLN GLY ASP          
-SEQRES  22 D  370  PRO ILE GLY LEU ILE LEU LEU GLY GLU VAL ALA LEU GLY          
-SEQRES  23 D  370  ASN MET TYR GLU LEU LYS HIS ALA SER HIS ILE SER LYS          
-SEQRES  24 D  370  LEU PRO LYS GLY LYS HIS SER VAL LYS GLY LEU GLY LYS          
-SEQRES  25 D  370  THR THR PRO ASP PRO SER ALA ASN ILE SER LEU ASP GLY          
-SEQRES  26 D  370  VAL ASP VAL PRO LEU GLY THR GLY ILE SER SER GLY VAL          
-SEQRES  27 D  370  ASN ASP THR SER LEU LEU TYR ASN GLU TYR ILE VAL TYR          
-SEQRES  28 D  370  ASP ILE ALA GLN VAL ASN LEU LYS TYR LEU LEU LYS LEU          
-SEQRES  29 D  370  LYS PHE ASN PHE LYS THR                                      
-HET    SO4  A1101       5                                                       
-HET    SO4  A1102       5                                                       
-HET    SO4  A1103       5                                                       
-HET    SO4  A1104       5                                                       
-HET    2YQ  A1105      28                                                       
-HET    GOL  A1106       6                                                       
-HET    GOL  A1107       6                                                       
-HET    SO4  B1101       5                                                       
-HET    SO4  B1102       5                                                       
-HET    SO4  B1103       5                                                       
-HET    SO4  B1104       5                                                       
-HET    2YQ  B1105      28                                                       
-HET    SO4  B1106       5                                                       
-HET    SO4  C1101       5                                                       
-HET    SO4  C1102       5                                                       
-HET    SO4  C1103       5                                                       
-HET    2YQ  C1104      28                                                       
-HET    GOL  C1105       6                                                       
-HET    SO4  D1101       5                                                       
-HET    SO4  D1102       5                                                       
-HET    SO4  D1103       5                                                       
-HET    2YQ  D1104      28                                                       
-HETNAM     SO4 SULFATE ION                                                      
-HETNAM     2YQ (8S,9R)-5-FLUORO-8-(4-FLUOROPHENYL)-9-(1-METHYL-1H-1,2,          
-HETNAM   2 2YQ  4-TRIAZOL-5-YL)-2,7,8,9-TETRAHYDRO-3H-PYRIDO[4,3,2-             
-HETNAM   3 2YQ  DE]PHTHALAZIN-3-ONE                                             
-HETNAM     GOL GLYCEROL                                                         
-HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
-FORMUL   5  SO4    15(O4 S 2-)                                                  
-FORMUL   9  2YQ    4(C19 H14 F2 N6 O)                                           
-FORMUL  10  GOL    3(C3 H8 O3)                                                  
-FORMUL  27  HOH   *316(H2 O)                                                    
-HELIX    1 AA1 PRO A  666  PHE A  677  1                                  12    
-HELIX    2 AA2 ASP A  678  TYR A  689  1                                  12    
-HELIX    3 AA3 PRO A  697  LEU A  701  5                                   5    
-HELIX    4 AA4 SER A  702  GLN A  722  1                                  21    
-HELIX    5 AA5 SER A  727  ILE A  740  1                                  14    
-HELIX    6 AA6 ASN A  754  GLY A  780  1                                  27    
-HELIX    7 AA7 ASP A  788  LEU A  797  1                                  10    
-HELIX    8 AA8 SER A  808  THR A  821  1                                  14    
-HELIX    9 AA9 GLY A  843  LYS A  849  1                                   7    
-HELIX   10 AB1 PRO A  850  LYS A  852  5                                   3    
-HELIX   11 AB2 ARG A  865  THR A  867  5                                   3    
-HELIX   12 AB3 ASN A  868  GLY A  876  1                                   9    
-HELIX   13 AB4 MET A  900  ASN A  906  1                                   7    
-HELIX   14 AB5 TYR A  907  HIS A  909  5                                   3    
-HELIX   15 AB6 PRO A  958  ASN A  961  5                                   4    
-HELIX   16 AB7 ASP A  993  ALA A  995  5                                   3    
-HELIX   17 AB8 PRO B  666  PHE B  677  1                                  12    
-HELIX   18 AB9 ASP B  678  TYR B  689  1                                  12    
-HELIX   19 AC1 PRO B  697  LEU B  701  5                                   5    
-HELIX   20 AC2 SER B  702  SER B  721  1                                  20    
-HELIX   21 AC3 SER B  727  ILE B  740  1                                  14    
-HELIX   22 AC4 ASN B  754  GLY B  780  1                                  27    
-HELIX   23 AC5 ASP B  788  LEU B  797  1                                  10    
-HELIX   24 AC6 SER B  808  THR B  821  1                                  14    
-HELIX   25 AC7 GLY B  843  GLN B  853  1                                  11    
-HELIX   26 AC8 ARG B  865  THR B  867  5                                   3    
-HELIX   27 AC9 ASN B  868  GLY B  876  1                                   9    
-HELIX   28 AD1 MET B  900  ASN B  906  1                                   7    
-HELIX   29 AD2 TYR B  907  HIS B  909  5                                   3    
-HELIX   30 AD3 PRO B  958  ASN B  961  5                                   4    
-HELIX   31 AD4 ASP B  993  ALA B  995  5                                   3    
-HELIX   32 AD5 PRO C  666  PHE C  677  1                                  12    
-HELIX   33 AD6 ASP C  678  TYR C  689  1                                  12    
-HELIX   34 AD7 PRO C  697  LEU C  701  5                                   5    
-HELIX   35 AD8 SER C  702  GLY C  723  1                                  22    
-HELIX   36 AD9 SER C  725  ILE C  740  1                                  16    
-HELIX   37 AE1 ASN C  754  GLY C  780  1                                  27    
-HELIX   38 AE2 ASP C  788  LEU C  797  1                                  10    
-HELIX   39 AE3 SER C  808  THR C  821  1                                  14    
-HELIX   40 AE4 GLY C  843  LYS C  849  1                                   7    
-HELIX   41 AE5 PRO C  850  LEU C  854  5                                   5    
-HELIX   42 AE6 ARG C  865  THR C  867  5                                   3    
-HELIX   43 AE7 ASN C  868  GLY C  876  1                                   9    
-HELIX   44 AE8 MET C  900  ASN C  906  1                                   7    
-HELIX   45 AE9 TYR C  907  HIS C  909  5                                   3    
-HELIX   46 AF1 PRO C  958  ASN C  961  5                                   4    
-HELIX   47 AF2 ASP C  993  ALA C  995  5                                   3    
-HELIX   48 AF3 PRO D  666  PHE D  677  1                                  12    
-HELIX   49 AF4 ASP D  678  TYR D  689  1                                  12    
-HELIX   50 AF5 PRO D  697  LEU D  701  5                                   5    
-HELIX   51 AF6 SER D  702  SER D  721  1                                  20    
-HELIX   52 AF7 ASP D  731  ILE D  740  1                                  10    
-HELIX   53 AF8 ASN D  754  ARG D  779  1                                  26    
-HELIX   54 AF9 PRO D  789  LEU D  797  1                                   9    
-HELIX   55 AG1 SER D  808  THR D  821  1                                  14    
-HELIX   56 AG2 GLY D  843  LYS D  849  1                                   7    
-HELIX   57 AG3 PRO D  850  LYS D  852  5                                   3    
-HELIX   58 AG4 ARG D  865  THR D  867  5                                   3    
-HELIX   59 AG5 ASN D  868  GLY D  876  1                                   9    
-HELIX   60 AG6 MET D  900  ASN D  906  1                                   7    
-HELIX   61 AG7 TYR D  907  HIS D  909  5                                   3    
-HELIX   62 AG8 PRO D  958  ASN D  961  5                                   4    
-HELIX   63 AG9 ASP D  993  ALA D  995  5                                   3    
-SHEET    1 AA1 5 THR A 799  VAL A 803  0                                        
-SHEET    2 AA1 5 TYR A 829  ARG A 841 -1  O  LYS A 838   N  LYS A 802           
-SHEET    3 AA1 5 VAL A 997  PHE A1009 -1  O  LYS A1004   N  ILE A 834           
-SHEET    4 AA1 5 ILE A 916  ALA A 925 -1  N  GLU A 923   O  ASN A 998           
-SHEET    5 AA1 5 ARG A 857  GLY A 863 -1  N  ARG A 858   O  VAL A 924           
-SHEET    1 AA2 4 ILE A 895  PHE A 897  0                                        
-SHEET    2 AA2 4 GLU A 988  VAL A 991 -1  O  VAL A 991   N  ILE A 895           
-SHEET    3 AA2 4 SER A 947  GLY A 950 -1  N  GLY A 950   O  GLU A 988           
-SHEET    4 AA2 4 MET A 929  LEU A 932  1  N  TYR A 930   O  SER A 947           
-SHEET    1 AA3 3 GLY A 974  SER A 976  0                                        
-SHEET    2 AA3 3 GLY A 952  PRO A 956 -1  N  THR A 955   O  ILE A 975           
-SHEET    3 AA3 3 LEU A 984  TYR A 986  1  O  LEU A 985   N  THR A 954           
-SHEET    1 AA4 3 VAL A 967  VAL A 969  0                                        
-SHEET    2 AA4 3 ILE A 962  LEU A 964 -1  N  LEU A 964   O  VAL A 967           
-SHEET    3 AA4 3 SER C 936  HIS C 937  1  O  HIS C 937   N  SER A 963           
-SHEET    1 AA5 5 THR B 799  VAL B 803  0                                        
-SHEET    2 AA5 5 TYR B 829  ARG B 841 -1  O  LYS B 838   N  LYS B 802           
-SHEET    3 AA5 5 VAL B 997  PHE B1009 -1  O  LYS B1004   N  ILE B 834           
-SHEET    4 AA5 5 ILE B 916  ALA B 925 -1  N  GLU B 923   O  ASN B 998           
-SHEET    5 AA5 5 ARG B 857  GLY B 863 -1  N  ARG B 858   O  VAL B 924           
-SHEET    1 AA6 4 ILE B 895  PHE B 897  0                                        
-SHEET    2 AA6 4 GLU B 988  VAL B 991 -1  O  TYR B 989   N  PHE B 897           
-SHEET    3 AA6 4 SER B 947  GLY B 950 -1  N  VAL B 948   O  ILE B 990           
-SHEET    4 AA6 4 MET B 929  LEU B 932  1  N  TYR B 930   O  SER B 947           
-SHEET    1 AA7 3 GLY B 974  SER B 976  0                                        
-SHEET    2 AA7 3 GLY B 952  PRO B 956 -1  N  THR B 955   O  ILE B 975           
-SHEET    3 AA7 3 LEU B 984  TYR B 986  1  O  LEU B 985   N  THR B 954           
-SHEET    1 AA8 2 ILE B 962  LEU B 964  0                                        
-SHEET    2 AA8 2 VAL B 967  VAL B 969 -1  O  VAL B 967   N  LEU B 964           
-SHEET    1 AA9 5 THR C 799  VAL C 803  0                                        
-SHEET    2 AA9 5 TYR C 829  ARG C 841 -1  O  LYS C 838   N  LYS C 802           
-SHEET    3 AA9 5 VAL C 997  PHE C1009 -1  O  LYS C1004   N  ILE C 834           
-SHEET    4 AA9 5 ILE C 916  ALA C 925 -1  N  GLU C 923   O  ASN C 998           
-SHEET    5 AA9 5 ARG C 857  GLY C 863 -1  N  ARG C 858   O  VAL C 924           
-SHEET    1 AB1 4 ILE C 895  PHE C 897  0                                        
-SHEET    2 AB1 4 GLU C 988  VAL C 991 -1  O  VAL C 991   N  ILE C 895           
-SHEET    3 AB1 4 SER C 947  GLY C 950 -1  N  VAL C 948   O  ILE C 990           
-SHEET    4 AB1 4 MET C 929  LEU C 932  1  N  TYR C 930   O  SER C 947           
-SHEET    1 AB2 3 GLY C 974  SER C 976  0                                        
-SHEET    2 AB2 3 GLY C 952  PRO C 956 -1  N  THR C 955   O  ILE C 975           
-SHEET    3 AB2 3 LEU C 984  TYR C 986  1  O  LEU C 985   N  THR C 954           
-SHEET    1 AB3 2 ILE C 962  LEU C 964  0                                        
-SHEET    2 AB3 2 VAL C 967  VAL C 969 -1  O  VAL C 969   N  ILE C 962           
-SHEET    1 AB4 5 THR D 799  VAL D 803  0                                        
-SHEET    2 AB4 5 ASP D 830  ARG D 841 -1  O  LYS D 838   N  LYS D 802           
-SHEET    3 AB4 5 VAL D 997  ASN D1008 -1  O  LYS D1004   N  ILE D 834           
-SHEET    4 AB4 5 ILE D 916  ALA D 925 -1  N  GLY D 917   O  LEU D1005           
-SHEET    5 AB4 5 ARG D 857  GLY D 863 -1  N  LEU D 860   O  GLY D 922           
-SHEET    1 AB5 4 ILE D 895  PHE D 897  0                                        
-SHEET    2 AB5 4 GLU D 988  VAL D 991 -1  O  VAL D 991   N  ILE D 895           
-SHEET    3 AB5 4 SER D 947  GLY D 950 -1  N  VAL D 948   O  ILE D 990           
-SHEET    4 AB5 4 MET D 929  LEU D 932  1  N  TYR D 930   O  SER D 947           
-SHEET    1 AB6 3 GLY D 974  SER D 976  0                                        
-SHEET    2 AB6 3 GLY D 952  PRO D 956 -1  N  THR D 955   O  ILE D 975           
-SHEET    3 AB6 3 LEU D 984  TYR D 986  1  O  LEU D 985   N  THR D 954           
-SHEET    1 AB7 2 ILE D 962  LEU D 964  0                                        
-SHEET    2 AB7 2 VAL D 967  VAL D 969 -1  O  VAL D 967   N  LEU D 964           
-SSBOND   1 CYS A  845    CYS B  845                          1555   1555  2.18  
-SSBOND   2 CYS C  845    CYS D  845                          1555   1555  2.15  
-SITE     1 AC1  4 LYS A 903  LEU A 984  LEU A 985  TYR A 986                    
-SITE     1 AC2  3 ARG A 858  MET A 929  LYS A 949                               
-SITE     1 AC3  8 ARG A 841  GLY A 843  CYS A 845  GLN A 846                    
-SITE     2 AC3  8 GLY B 843  GLU B 844  CYS B 845  GLN B 846                    
-SITE     1 AC4  5 SER A 808  GLU A 809  GLU A 810  HOH A1286                    
-SITE     2 AC4  5 HIS C 937                                                     
-SITE     1 AC5 16 GLN A 759  GLU A 763  HIS A 862  GLY A 863                    
-SITE     2 AC5 16 GLY A 888  TYR A 889  TYR A 896  PHE A 897                    
-SITE     3 AC5 16 ALA A 898  LYS A 903  SER A 904  TYR A 907                    
-SITE     4 AC5 16 GLU A 988  HOH A1220  HOH A1231  HOH A1272                    
-SITE     1 AC6  4 LYS A 933  HIS A 934  ALA A 935  SER A 936                    
-SITE     1 AC7  5 GLY A 944  HIS A 946  PRO D 850  LEU D 854                    
-SITE     2 AC7  5 HIS D 946                                                     
-SITE     1 AC8  4 LYS B 903  LEU B 984  LEU B 985  TYR B 986                    
-SITE     1 AC9  6 GLN A 846  LYS A 849  LYS B 838  ASP B 965                    
-SITE     2 AC9  6 LYS B1000  HOH B1241                                          
-SITE     1 AD1  3 ARG B 858  MET B 929  LYS B 949                               
-SITE     1 AD2  6 LYS B 943  GLY B 944  HIS B 946  SO4 B1106                    
-SITE     2 AD2  6 HOH B1234  HIS C 946                                          
-SITE     1 AD3 13 HIS B 862  GLY B 863  GLY B 888  TYR B 889                    
-SITE     2 AD3 13 TYR B 896  PHE B 897  ALA B 898  LYS B 903                    
-SITE     3 AD3 13 SER B 904  TYR B 907  GLU B 988  HOH B1221                    
-SITE     4 AD3 13 HOH B1224                                                     
-SITE     1 AD4  5 LYS B 945  HIS B 946  GLN B 996  SO4 B1104                    
-SITE     2 AD4  5 HOH B1213                                                     
-SITE     1 AD5  5 LYS C 903  LEU C 985  TYR C 986  GOL C1105                    
-SITE     2 AD5  5 HOH C1266                                                     
-SITE     1 AD6  4 LYS C 838  LYS C1000  GLN D 846  LYS D 849                    
-SITE     1 AD7  3 SER C 702  LYS C 703  ARG C 704                               
-SITE     1 AD8 15 GLN C 759  HIS C 862  GLY C 863  GLY C 888                    
-SITE     2 AD8 15 TYR C 889  TYR C 896  PHE C 897  ALA C 898                    
-SITE     3 AD8 15 LYS C 903  SER C 904  TYR C 907  GLU C 988                    
-SITE     4 AD8 15 GOL C1105  HOH C1224  HOH C1256                               
-SITE     1 AD9  8 GLY C 888  TYR C 889  MET C 890  TYR C 896                    
-SITE     2 AD9  8 GLU C 988  SO4 C1101  2YQ C1104  HOH C1215                    
-SITE     1 AE1  8 GLY C 843  CYS C 845  GLN C 846  GLU D 842                    
-SITE     2 AE1  8 GLY D 843  GLU D 844  CYS D 845  GLN D 846                    
-SITE     1 AE2  5 LYS D 903  LEU D 984  LEU D 985  TYR D 986                    
-SITE     2 AE2  5 HOH D1231                                                     
-SITE     1 AE3  3 ARG D 858  MET D 929  LYS D 949                               
-SITE     1 AE4 16 GLN D 759  GLU D 763  HIS D 862  GLY D 863                    
-SITE     2 AE4 16 GLY D 888  TYR D 889  TYR D 896  PHE D 897                    
-SITE     3 AE4 16 ALA D 898  LYS D 903  SER D 904  TYR D 907                    
-SITE     4 AE4 16 GLU D 988  HOH D1212  HOH D1237  HOH D1242                    
-CRYST1  103.690  108.150  142.000  90.00  90.00  90.00 P 21 21 21   16          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.009644  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.009246  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.007042        0.00000                         
-ATOM      1  N   LYS A 662     -64.699 -17.577 -24.714  1.00 54.01           N  
-ANISOU    1  N   LYS A 662     6455   6388   7679   -136   -643   -729       N  
-ATOM      2  CA  LYS A 662     -64.279 -16.248 -25.279  1.00 56.66           C  
-ANISOU    2  CA  LYS A 662     6819   6787   7923    -99   -636   -726       C  
-ATOM      3  C   LYS A 662     -64.604 -15.095 -24.311  1.00 56.98           C  
-ANISOU    3  C   LYS A 662     6853   6852   7945   -115   -586   -669       C  
-ATOM      4  O   LYS A 662     -65.661 -15.063 -23.690  1.00 54.31           O  
-ANISOU    4  O   LYS A 662     6476   6497   7661   -144   -575   -653       O  
-ATOM      5  CB  LYS A 662     -64.912 -15.969 -26.648  1.00 53.07           C  
-ANISOU    5  CB  LYS A 662     6355   6359   7452    -69   -692   -783       C  
-ATOM      6  N   SER A 663     -63.691 -14.132 -24.216  1.00 57.99           N  
-ANISOU    6  N   SER A 663     7017   7020   7996    -94   -556   -642       N  
-ATOM      7  CA  SER A 663     -63.817 -13.035 -23.269  1.00 58.01           C  
-ANISOU    7  CA  SER A 663     7020   7046   7977   -105   -508   -590       C  
-ATOM      8  C   SER A 663     -64.782 -11.948 -23.733  1.00 53.48           C  
-ANISOU    8  C   SER A 663     6427   6504   7390    -92   -521   -598       C  
-ATOM      9  O   SER A 663     -64.816 -11.613 -24.898  1.00 50.52           O  
-ANISOU    9  O   SER A 663     6061   6154   6979    -61   -559   -634       O  
-ATOM     10  CB  SER A 663     -62.435 -12.431 -23.102  1.00 58.30           C  
-ANISOU   10  CB  SER A 663     7101   7110   7941    -85   -478   -564       C  
-ATOM     11  OG  SER A 663     -62.527 -11.192 -22.428  1.00 63.20           O  
-ANISOU   11  OG  SER A 663     7724   7758   8530    -87   -440   -524       O  
-ATOM     12  N   LYS A 664     -65.540 -11.375 -22.805  1.00 53.08           N  
-ANISOU   12  N   LYS A 664     6350   6454   7363   -114   -490   -565       N  
-ATOM     13  CA  LYS A 664     -66.345 -10.191 -23.103  1.00 54.95           C  
-ANISOU   13  CA  LYS A 664     6571   6724   7582   -100   -497   -567       C  
-ATOM     14  C   LYS A 664     -65.551  -8.865 -23.041  1.00 49.91           C  
-ANISOU   14  C   LYS A 664     5971   6127   6867    -76   -470   -538       C  
-ATOM     15  O   LYS A 664     -66.069  -7.815 -23.416  1.00 50.53           O  
-ANISOU   15  O   LYS A 664     6045   6233   6922    -58   -480   -539       O  
-ATOM     16  CB  LYS A 664     -67.518 -10.134 -22.115  1.00 58.98           C  
-ANISOU   16  CB  LYS A 664     7034   7220   8154   -133   -473   -547       C  
-ATOM     17  N   LEU A 665     -64.310  -8.902 -22.561  1.00 45.67           N  
-ANISOU   17  N   LEU A 665     5468   5590   6292    -75   -438   -511       N  
-ATOM     18  CA  LEU A 665     -63.520  -7.675 -22.387  1.00 40.91           C  
-ANISOU   18  CA  LEU A 665     4899   5022   5625    -57   -410   -481       C  
-ATOM     19  C   LEU A 665     -63.119  -7.083 -23.725  1.00 37.36           C  
-ANISOU   19  C   LEU A 665     4475   4602   5117    -21   -440   -505       C  
-ATOM     20  O   LEU A 665     -62.798  -7.813 -24.643  1.00 36.00           O  
-ANISOU   20  O   LEU A 665     4315   4428   4938     -7   -472   -538       O  
-ATOM     21  CB  LEU A 665     -62.244  -7.960 -21.582  1.00 41.15           C  
-ANISOU   21  CB  LEU A 665     4956   5044   5634    -65   -372   -452       C  
-ATOM     22  CG  LEU A 665     -62.401  -8.462 -20.158  1.00 38.68           C  
-ANISOU   22  CG  LEU A 665     4628   4705   5363    -98   -336   -420       C  
-ATOM     23  CD1 LEU A 665     -61.077  -8.972 -19.635  1.00 40.90           C  
-ANISOU   23  CD1 LEU A 665     4941   4977   5624    -99   -314   -402       C  
-ATOM     24  CD2 LEU A 665     -62.929  -7.374 -19.268  1.00 38.74           C  
-ANISOU   24  CD2 LEU A 665     4623   4730   5367   -105   -303   -388       C  
-ATOM     25  N   PRO A 666     -63.066  -5.749 -23.816  1.00 37.15           N  
-ANISOU   25  N   PRO A 666     4462   4605   5048     -4   -428   -485       N  
-ATOM     26  CA  PRO A 666     -62.495  -5.102 -24.998  1.00 37.06           C  
-ANISOU   26  CA  PRO A 666     4483   4624   4973     30   -448   -495       C  
-ATOM     27  C   PRO A 666     -61.086  -5.599 -25.327  1.00 37.33           C  
-ANISOU   27  C   PRO A 666     4553   4664   4969     39   -438   -498       C  
-ATOM     28  O   PRO A 666     -60.319  -5.945 -24.414  1.00 38.45           O  
-ANISOU   28  O   PRO A 666     4701   4791   5118     22   -405   -476       O  
-ATOM     29  CB  PRO A 666     -62.441  -3.608 -24.602  1.00 37.14           C  
-ANISOU   29  CB  PRO A 666     4504   4656   4952     37   -421   -459       C  
-ATOM     30  CG  PRO A 666     -63.404  -3.452 -23.467  1.00 36.30           C  
-ANISOU   30  CG  PRO A 666     4361   4535   4897     13   -403   -444       C  
-ATOM     31  CD  PRO A 666     -63.396  -4.773 -22.752  1.00 37.39           C  
-ANISOU   31  CD  PRO A 666     4482   4642   5084    -16   -392   -448       C  
-ATOM     32  N   LYS A 667     -60.751  -5.625 -26.614  1.00 36.31           N  
-ANISOU   32  N   LYS A 667     4444   4555   4796     69   -468   -525       N  
-ATOM     33  CA  LYS A 667     -59.439  -6.130 -27.042  1.00 36.45           C  
-ANISOU   33  CA  LYS A 667     4492   4581   4777     81   -460   -533       C  
-ATOM     34  C   LYS A 667     -58.291  -5.415 -26.281  1.00 32.52           C  
-ANISOU   34  C   LYS A 667     4016   4092   4248     74   -410   -490       C  
-ATOM     35  O   LYS A 667     -57.420  -6.078 -25.743  1.00 29.80           O  
-ANISOU   35  O   LYS A 667     3677   3734   3911     64   -390   -486       O  
-ATOM     36  CB  LYS A 667     -59.249  -6.079 -28.584  1.00 36.61           C  
-ANISOU   36  CB  LYS A 667     4534   4631   4743    117   -494   -565       C  
-ATOM     37  N   PRO A 668     -58.311  -4.062 -26.222  1.00 30.91           N  
-ANISOU   37  N   PRO A 668     3821   3909   4013     81   -392   -460       N  
-ATOM     38  CA  PRO A 668     -57.230  -3.319 -25.537  1.00 30.49           C  
-ANISOU   38  CA  PRO A 668     3787   3864   3934     75   -348   -423       C  
-ATOM     39  C   PRO A 668     -56.995  -3.790 -24.119  1.00 28.94           C  
-ANISOU   39  C   PRO A 668     3577   3641   3778     48   -320   -405       C  
-ATOM     40  O   PRO A 668     -55.863  -3.897 -23.693  1.00 31.08           O  
-ANISOU   40  O   PRO A 668     3863   3913   4035     45   -294   -393       O  
-ATOM     41  CB  PRO A 668     -57.746  -1.874 -25.538  1.00 29.67           C  
-ANISOU   41  CB  PRO A 668     3684   3774   3813     82   -342   -397       C  
-ATOM     42  CG  PRO A 668     -58.638  -1.806 -26.724  1.00 29.90           C  
-ANISOU   42  CG  PRO A 668     3713   3817   3831    104   -385   -422       C  
-ATOM     43  CD  PRO A 668     -59.327  -3.144 -26.767  1.00 29.45           C  
-ANISOU   43  CD  PRO A 668     3631   3739   3820     95   -415   -459       C  
-ATOM     44  N   VAL A 669     -58.067  -4.104 -23.410  1.00 29.01           N  
-ANISOU   44  N   VAL A 669     3557   3629   3836     29   -324   -405       N  
-ATOM     45  CA  VAL A 669     -57.976  -4.590 -22.049  1.00 28.34           C  
-ANISOU   45  CA  VAL A 669     3460   3520   3788      3   -297   -385       C  
-ATOM     46  C   VAL A 669     -57.363  -5.990 -22.038  1.00 30.64           C  
-ANISOU   46  C   VAL A 669     3755   3790   4097     -3   -304   -403       C  
-ATOM     47  O   VAL A 669     -56.468  -6.294 -21.220  1.00 30.49           O  
-ANISOU   47  O   VAL A 669     3746   3760   4077    -12   -279   -386       O  
-ATOM     48  CB  VAL A 669     -59.352  -4.601 -21.374  1.00 27.70           C  
-ANISOU   48  CB  VAL A 669     3345   3424   3756    -16   -299   -381       C  
-ATOM     49  CG1 VAL A 669     -59.252  -5.122 -19.945  1.00 28.51           C  
-ANISOU   49  CG1 VAL A 669     3437   3504   3891    -42   -267   -357       C  
-ATOM     50  CG2 VAL A 669     -59.932  -3.193 -21.345  1.00 28.09           C  
-ANISOU   50  CG2 VAL A 669     3389   3493   3789     -7   -293   -365       C  
-ATOM     51  N   GLN A 670     -57.842  -6.846 -22.932  1.00 29.26           N  
-ANISOU   51  N   GLN A 670     3572   3606   3939      3   -341   -440       N  
-ATOM     52  CA  GLN A 670     -57.284  -8.197 -23.080  1.00 31.89           C  
-ANISOU   52  CA  GLN A 670     3909   3916   4291      2   -354   -463       C  
-ATOM     53  C   GLN A 670     -55.789  -8.167 -23.366  1.00 29.90           C  
-ANISOU   53  C   GLN A 670     3687   3681   3993     19   -340   -463       C  
-ATOM     54  O   GLN A 670     -55.028  -8.848 -22.709  1.00 29.15           O  
-ANISOU   54  O   GLN A 670     3598   3567   3911     11   -326   -457       O  
-ATOM     55  CB  GLN A 670     -57.990  -8.956 -24.201  1.00 33.64           C  
-ANISOU   55  CB  GLN A 670     4119   4131   4531     12   -402   -510       C  
-ATOM     56  CG  GLN A 670     -59.392  -9.388 -23.859  1.00 35.26           C  
-ANISOU   56  CG  GLN A 670     4288   4309   4798    -10   -419   -517       C  
-ATOM     57  CD  GLN A 670     -60.019 -10.143 -25.021  1.00 40.43           C  
-ANISOU   57  CD  GLN A 670     4931   4957   5472      3   -471   -568       C  
-ATOM     58  OE1 GLN A 670     -59.355 -10.913 -25.707  1.00 42.07           O  
-ANISOU   58  OE1 GLN A 670     5154   5162   5669     19   -491   -600       O  
-ATOM     59  NE2 GLN A 670     -61.311  -9.935 -25.233  1.00 44.71           N  
-ANISOU   59  NE2 GLN A 670     5444   5497   6045     -2   -494   -581       N  
-ATOM     60  N   ASP A 671     -55.384  -7.289 -24.277  1.00 32.88           N  
-ANISOU   60  N   ASP A 671     4083   4094   4317     43   -341   -467       N  
-ATOM     61  CA  ASP A 671     -53.973  -7.050 -24.562  1.00 34.88           C  
-ANISOU   61  CA  ASP A 671     4361   4368   4523     58   -321   -463       C  
-ATOM     62  C   ASP A 671     -53.158  -6.562 -23.346  1.00 30.23           C  
-ANISOU   62  C   ASP A 671     3777   3775   3933     44   -280   -425       C  
-ATOM     63  O   ASP A 671     -52.036  -7.010 -23.147  1.00 27.90           O  
-ANISOU   63  O   ASP A 671     3493   3478   3630     48   -268   -427       O  
-ATOM     64  CB  ASP A 671     -53.805  -6.104 -25.766  1.00 36.41           C  
-ANISOU   64  CB  ASP A 671     4572   4601   4660     84   -326   -467       C  
-ATOM     65  CG  ASP A 671     -54.231  -6.765 -27.111  1.00 44.36           C  
-ANISOU   65  CG  ASP A 671     5582   5619   5655    106   -369   -513       C  
-ATOM     66  OD1 ASP A 671     -54.518  -7.986 -27.119  1.00 44.60           O  
-ANISOU   66  OD1 ASP A 671     5599   5623   5724    102   -394   -544       O  
-ATOM     67  OD2 ASP A 671     -54.256  -6.068 -28.166  1.00 44.04           O  
-ANISOU   67  OD2 ASP A 671     5557   5611   5566    130   -378   -517       O  
-ATOM     68  N   LEU A 672     -53.752  -5.702 -22.520  1.00 28.68           N  
-ANISOU   68  N   LEU A 672     3572   3577   3748     30   -263   -394       N  
-ATOM     69  CA  LEU A 672     -53.116  -5.250 -21.284  1.00 27.91           C  
-ANISOU   69  CA  LEU A 672     3478   3475   3652     17   -228   -362       C  
-ATOM     70  C   LEU A 672     -52.921  -6.414 -20.305  1.00 27.81           C  
-ANISOU   70  C   LEU A 672     3458   3431   3677      1   -224   -360       C  
-ATOM     71  O   LEU A 672     -51.853  -6.547 -19.719  1.00 28.19           O  
-ANISOU   71  O   LEU A 672     3517   3477   3717      2   -206   -350       O  
-ATOM     72  CB  LEU A 672     -53.938  -4.145 -20.615  1.00 27.31           C  
-ANISOU   72  CB  LEU A 672     3390   3403   3582      7   -214   -335       C  
-ATOM     73  CG  LEU A 672     -53.470  -3.599 -19.278  1.00 27.70           C  
-ANISOU   73  CG  LEU A 672     3442   3450   3634     -4   -182   -305       C  
-ATOM     74  CD1 LEU A 672     -52.175  -2.824 -19.430  1.00 28.50           C  
-ANISOU   74  CD1 LEU A 672     3562   3570   3697      7   -163   -296       C  
-ATOM     75  CD2 LEU A 672     -54.517  -2.701 -18.644  1.00 30.56           C  
-ANISOU   75  CD2 LEU A 672     3788   3813   4009    -13   -173   -286       C  
-ATOM     76  N   ILE A 673     -53.948  -7.222 -20.116  1.00 27.61           N  
-ANISOU   76  N   ILE A 673     3415   3381   3694    -12   -241   -368       N  
-ATOM     77  CA  ILE A 673     -53.843  -8.369 -19.233  1.00 29.95           C  
-ANISOU   77  CA  ILE A 673     3706   3643   4029    -28   -238   -363       C  
-ATOM     78  C   ILE A 673     -52.739  -9.330 -19.685  1.00 30.97           C  
-ANISOU   78  C   ILE A 673     3851   3764   4153    -15   -251   -386       C  
-ATOM     79  O   ILE A 673     -51.983  -9.830 -18.854  1.00 27.34           O  
-ANISOU   79  O   ILE A 673     3400   3288   3702    -19   -237   -372       O  
-ATOM     80  CB  ILE A 673     -55.170  -9.151 -19.135  1.00 32.45           C  
-ANISOU   80  CB  ILE A 673     3998   3932   4398    -47   -257   -370       C  
-ATOM     81  CG1 ILE A 673     -56.283  -8.256 -18.613  1.00 34.28           C  
-ANISOU   81  CG1 ILE A 673     4211   4173   4641    -60   -242   -349       C  
-ATOM     82  CG2 ILE A 673     -55.039 -10.368 -18.232  1.00 32.93           C  
-ANISOU   82  CG2 ILE A 673     4056   3954   4501    -65   -252   -359       C  
-ATOM     83  CD1 ILE A 673     -55.889  -7.420 -17.415  1.00 36.07           C  
-ANISOU   83  CD1 ILE A 673     4446   4411   4849    -65   -205   -311       C  
-ATOM     84  N   LYS A 674     -52.655  -9.598 -20.984  1.00 33.28           N  
-ANISOU   84  N   LYS A 674     4147   4068   4431      3   -277   -422       N  
-ATOM     85  CA  LYS A 674     -51.567 -10.452 -21.521  1.00 36.92           C  
-ANISOU   85  CA  LYS A 674     4622   4525   4882     21   -288   -450       C  
-ATOM     86  C   LYS A 674     -50.215  -9.847 -21.253  1.00 33.46           C  
-ANISOU   86  C   LYS A 674     4200   4109   4405     32   -261   -435       C  
-ATOM     87  O   LYS A 674     -49.308 -10.490 -20.787  1.00 37.16           O  
-ANISOU   87  O   LYS A 674     4674   4563   4881     35   -256   -437       O  
-ATOM     88  CB  LYS A 674     -51.732 -10.673 -23.028  1.00 39.78           C  
-ANISOU   88  CB  LYS A 674     4986   4905   5225     43   -320   -494       C  
-ATOM     89  CG  LYS A 674     -52.904 -11.566 -23.381  1.00 44.53           C  
-ANISOU   89  CG  LYS A 674     5570   5478   5873     35   -356   -520       C  
-ATOM     90  CD  LYS A 674     -53.007 -11.750 -24.883  1.00 49.74           C  
-ANISOU   90  CD  LYS A 674     6234   6159   6507     61   -390   -567       C  
-ATOM     91  CE  LYS A 674     -54.336 -12.383 -25.244  1.00 55.99           C  
-ANISOU   91  CE  LYS A 674     7004   6927   7345     53   -428   -594       C  
-ATOM     92  NZ  LYS A 674     -54.666 -12.210 -26.688  1.00 63.99           N  
-ANISOU   92  NZ  LYS A 674     8021   7969   8324     81   -461   -635       N  
-ATOM     93  N   MET A 675     -50.107  -8.569 -21.524  1.00 32.77           N  
-ANISOU   93  N   MET A 675     4117   4055   4279     38   -243   -421       N  
-ATOM     94  CA  MET A 675     -48.878  -7.817 -21.277  1.00 33.16           C  
-ANISOU   94  CA  MET A 675     4178   4126   4295     45   -215   -405       C  
-ATOM     95  C   MET A 675     -48.405  -7.893 -19.813  1.00 32.67           C  
-ANISOU   95  C   MET A 675     4115   4044   4252     31   -194   -377       C  
-ATOM     96  O   MET A 675     -47.242  -8.145 -19.511  1.00 31.93           O  
-ANISOU   96  O   MET A 675     4028   3951   4152     39   -185   -380       O  
-ATOM     97  CB  MET A 675     -49.157  -6.409 -21.665  1.00 35.40           C  
-ANISOU   97  CB  MET A 675     4465   4439   4547     47   -202   -388       C  
-ATOM     98  CG  MET A 675     -47.946  -5.553 -21.844  1.00 44.35           C  
-ANISOU   98  CG  MET A 675     5609   5599   5643     57   -176   -377       C  
-ATOM     99  SD  MET A 675     -48.581  -3.930 -22.265  1.00 47.83           S  
-ANISOU   99  SD  MET A 675     6053   6064   6056     57   -166   -353       S  
-ATOM    100  CE  MET A 675     -47.054  -3.030 -22.158  1.00 47.52           C  
-ANISOU  100  CE  MET A 675     6021   6045   5987     61   -132   -337       C  
-ATOM    101  N   ILE A 676     -49.325  -7.724 -18.890  1.00 30.67           N  
-ANISOU  101  N   ILE A 676     3853   3776   4024     13   -189   -353       N  
-ATOM    102  CA  ILE A 676     -48.995  -7.638 -17.489  1.00 31.02           C  
-ANISOU  102  CA  ILE A 676     3900   3809   4079      2   -168   -325       C  
-ATOM    103  C   ILE A 676     -48.716  -9.006 -16.866  1.00 30.16           C  
-ANISOU  103  C   ILE A 676     3793   3666   4002     -2   -178   -327       C  
-ATOM    104  O   ILE A 676     -47.998  -9.099 -15.889  1.00 31.96           O  
-ANISOU  104  O   ILE A 676     4028   3887   4230     -2   -165   -310       O  
-ATOM    105  CB  ILE A 676     -50.262  -7.059 -16.825  1.00 31.74           C  
-ANISOU  105  CB  ILE A 676     3979   3896   4185    -16   -160   -301       C  
-ATOM    106  CG1 ILE A 676     -50.298  -5.547 -16.865  1.00 33.26           C  
-ANISOU  106  CG1 ILE A 676     4171   4116   4349    -12   -143   -287       C  
-ATOM    107  CG2 ILE A 676     -50.506  -7.550 -15.413  1.00 32.73           C  
-ANISOU  107  CG2 ILE A 676     4101   3998   4336    -31   -147   -275       C  
-ATOM    108  CD1 ILE A 676     -51.593  -5.073 -16.216  1.00 35.21           C  
-ANISOU  108  CD1 ILE A 676     4403   4359   4614    -27   -136   -269       C  
-ATOM    109  N   PHE A 677     -49.355 -10.047 -17.381  1.00 30.68           N  
-ANISOU  109  N   PHE A 677     3852   3708   4097     -6   -203   -347       N  
-ATOM    110  CA  PHE A 677     -49.134 -11.415 -16.901  1.00 31.66           C  
-ANISOU  110  CA  PHE A 677     3979   3794   4256    -10   -216   -350       C  
-ATOM    111  C   PHE A 677     -48.172 -12.225 -17.820  1.00 33.32           C  
-ANISOU  111  C   PHE A 677     4197   4001   4463     12   -237   -389       C  
-ATOM    112  O   PHE A 677     -48.157 -13.425 -17.763  1.00 37.53           O  
-ANISOU  112  O   PHE A 677     4731   4500   5030     12   -257   -401       O  
-ATOM    113  CB  PHE A 677     -50.479 -12.144 -16.724  1.00 30.80           C  
-ANISOU  113  CB  PHE A 677     3856   3654   4195    -31   -229   -345       C  
-ATOM    114  CG  PHE A 677     -51.233 -11.753 -15.456  1.00 30.32           C  
-ANISOU  114  CG  PHE A 677     3787   3585   4146    -53   -204   -303       C  
-ATOM    115  CD1 PHE A 677     -50.750 -12.104 -14.238  1.00 32.25           C  
-ANISOU  115  CD1 PHE A 677     4043   3814   4396    -58   -188   -274       C  
-ATOM    116  CD2 PHE A 677     -52.367 -10.991 -15.514  1.00 28.43           C  
-ANISOU  116  CD2 PHE A 677     3532   3361   3909    -65   -196   -295       C  
-ATOM    117  CE1 PHE A 677     -51.403 -11.725 -13.074  1.00 32.66           C  
-ANISOU  117  CE1 PHE A 677     4090   3865   4453    -75   -163   -236       C  
-ATOM    118  CE2 PHE A 677     -53.045 -10.636 -14.385  1.00 30.62           C  
-ANISOU  118  CE2 PHE A 677     3801   3636   4197    -83   -171   -260       C  
-ATOM    119  CZ  PHE A 677     -52.564 -11.003 -13.146  1.00 31.98           C  
-ANISOU  119  CZ  PHE A 677     3986   3795   4372    -88   -153   -229       C  
-ATOM    120  N   ASP A 678     -47.357 -11.537 -18.608  1.00 33.80           N  
-ANISOU  120  N   ASP A 678     4263   4098   4482     32   -231   -406       N  
-ATOM    121  CA  ASP A 678     -46.467 -12.136 -19.550  1.00 35.15           C  
-ANISOU  121  CA  ASP A 678     4439   4275   4642     55   -246   -444       C  
-ATOM    122  C   ASP A 678     -45.293 -12.797 -18.843  1.00 33.69           C  
-ANISOU  122  C   ASP A 678     4261   4074   4467     64   -244   -444       C  
-ATOM    123  O   ASP A 678     -44.328 -12.136 -18.434  1.00 32.98           O  
-ANISOU  123  O   ASP A 678     4174   4003   4352     71   -223   -432       O  
-ATOM    124  CB  ASP A 678     -45.963 -11.068 -20.537  1.00 38.53           C  
-ANISOU  124  CB  ASP A 678     4870   4751   5020     70   -233   -455       C  
-ATOM    125  CG  ASP A 678     -45.246 -11.665 -21.750  1.00 43.78           C  
-ANISOU  125  CG  ASP A 678     5538   5430   5667     96   -248   -500       C  
-ATOM    126  OD1 ASP A 678     -44.591 -12.724 -21.622  1.00 48.82           O  
-ANISOU  126  OD1 ASP A 678     6178   6047   6327    107   -262   -521       O  
-ATOM    127  OD2 ASP A 678     -45.338 -11.052 -22.834  1.00 53.83           O  
-ANISOU  127  OD2 ASP A 678     6813   6737   6904    108   -247   -514       O  
-ATOM    128  N   VAL A 679     -45.359 -14.119 -18.765  1.00 33.54           N  
-ANISOU  128  N   VAL A 679     4243   4015   4486     66   -269   -460       N  
-ATOM    129  CA  VAL A 679     -44.350 -14.932 -18.097  1.00 34.96           C  
-ANISOU  129  CA  VAL A 679     4430   4171   4682     76   -274   -461       C  
-ATOM    130  C   VAL A 679     -42.968 -14.819 -18.774  1.00 30.80           C  
-ANISOU  130  C   VAL A 679     3904   3673   4125    105   -271   -492       C  
-ATOM    131  O   VAL A 679     -41.943 -14.791 -18.121  1.00 28.28           O  
-ANISOU  131  O   VAL A 679     3589   3356   3801    114   -262   -485       O  
-ATOM    132  CB  VAL A 679     -44.820 -16.404 -18.063  1.00 39.29           C  
-ANISOU  132  CB  VAL A 679     4978   4668   5282     72   -306   -475       C  
-ATOM    133  CG1 VAL A 679     -43.738 -17.316 -17.539  1.00 40.70           C  
-ANISOU  133  CG1 VAL A 679     5166   4819   5479     89   -317   -481       C  
-ATOM    134  CG2 VAL A 679     -46.067 -16.516 -17.195  1.00 39.69           C  
-ANISOU  134  CG2 VAL A 679     5026   4689   5366     42   -302   -436       C  
-ATOM    135  N   GLU A 680     -42.957 -14.746 -20.083  1.00 28.69           N  
-ANISOU  135  N   GLU A 680     3633   3432   3837    119   -279   -529       N  
-ATOM    136  CA  GLU A 680     -41.713 -14.606 -20.811  1.00 29.70           C  
-ANISOU  136  CA  GLU A 680     3759   3591   3933    145   -271   -559       C  
-ATOM    137  C   GLU A 680     -41.013 -13.300 -20.443  1.00 27.58           C  
-ANISOU  137  C   GLU A 680     3490   3360   3631    142   -236   -532       C  
-ATOM    138  O   GLU A 680     -39.785 -13.264 -20.363  1.00 28.24           O  
-ANISOU  138  O   GLU A 680     3569   3457   3703    158   -225   -543       O  
-ATOM    139  CB  GLU A 680     -42.039 -14.635 -22.324  1.00 30.71           C  
-ANISOU  139  CB  GLU A 680     3885   3746   4037    161   -283   -599       C  
-ATOM    140  CG  GLU A 680     -40.860 -14.351 -23.228  1.00 32.74           C  
-ANISOU  140  CG  GLU A 680     4140   4045   4253    187   -269   -628       C  
-ATOM    141  CD  GLU A 680     -41.248 -14.310 -24.705  1.00 35.55           C  
-ANISOU  141  CD  GLU A 680     4498   4433   4577    204   -279   -664       C  
-ATOM    142  OE1 GLU A 680     -42.392 -14.706 -25.063  1.00 41.75           O  
-ANISOU  142  OE1 GLU A 680     5285   5200   5379    198   -305   -674       O  
-ATOM    143  OE2 GLU A 680     -40.414 -13.869 -25.513  1.00 34.18           O  
-ANISOU  143  OE2 GLU A 680     4323   4302   4361    223   -259   -681       O  
-ATOM    144  N   SER A 681     -41.775 -12.225 -20.273  1.00 25.88           N  
-ANISOU  144  N   SER A 681     3274   3159   3399    123   -218   -501       N  
-ATOM    145  CA  SER A 681     -41.190 -10.944 -19.844  1.00 26.58           C  
-ANISOU  145  CA  SER A 681     3361   3277   3462    118   -187   -475       C  
-ATOM    146  C   SER A 681     -40.609 -11.025 -18.463  1.00 25.60           C  
-ANISOU  146  C   SER A 681     3238   3133   3356    113   -181   -452       C  
-ATOM    147  O   SER A 681     -39.568 -10.453 -18.202  1.00 25.03           O  
-ANISOU  147  O   SER A 681     3160   3079   3269    120   -164   -450       O  
-ATOM    148  CB  SER A 681     -42.234  -9.836 -19.847  1.00 26.59           C  
-ANISOU  148  CB  SER A 681     3363   3291   3448     99   -174   -446       C  
-ATOM    149  OG  SER A 681     -42.559  -9.500 -21.141  1.00 29.84           O  
-ANISOU  149  OG  SER A 681     3776   3730   3834    108   -176   -464       O  
-ATOM    150  N   MET A 682     -41.293 -11.749 -17.581  1.00 28.20           N  
-ANISOU  150  N   MET A 682     3573   3425   3717    102   -196   -436       N  
-ATOM    151  CA  MET A 682     -40.773 -12.007 -16.252  1.00 28.46           C  
-ANISOU  151  CA  MET A 682     3610   3436   3765    101   -195   -414       C  
-ATOM    152  C   MET A 682     -39.399 -12.701 -16.362  1.00 28.29           C  
-ANISOU  152  C   MET A 682     3587   3413   3750    126   -205   -443       C  
-ATOM    153  O   MET A 682     -38.443 -12.290 -15.725  1.00 24.39           O  
-ANISOU  153  O   MET A 682     3090   2929   3247    133   -195   -437       O  
-ATOM    154  CB  MET A 682     -41.762 -12.854 -15.455  1.00 31.89           C  
-ANISOU  154  CB  MET A 682     4052   3829   4234     86   -210   -392       C  
-ATOM    155  CG  MET A 682     -43.134 -12.196 -15.159  1.00 32.78           C  
-ANISOU  155  CG  MET A 682     4164   3944   4347     61   -198   -363       C  
-ATOM    156  SD  MET A 682     -44.235 -13.407 -14.352  1.00 40.27           S  
-ANISOU  156  SD  MET A 682     5118   4842   5343     42   -213   -340       S  
-ATOM    157  CE  MET A 682     -45.855 -12.826 -14.876  1.00 38.80           C  
-ANISOU  157  CE  MET A 682     4918   4664   5160     20   -208   -333       C  
-ATOM    158  N   LYS A 683     -39.307 -13.755 -17.179  1.00 30.43           N  
-ANISOU  158  N   LYS A 683     3858   3670   4035    140   -228   -478       N  
-ATOM    159  CA  LYS A 683     -38.060 -14.551 -17.282  1.00 30.79           C  
-ANISOU  159  CA  LYS A 683     3899   3709   4090    166   -241   -509       C  
-ATOM    160  C   LYS A 683     -36.931 -13.786 -17.918  1.00 30.00           C  
-ANISOU  160  C   LYS A 683     3785   3653   3958    181   -220   -530       C  
-ATOM    161  O   LYS A 683     -35.803 -13.827 -17.405  1.00 26.81           O  
-ANISOU  161  O   LYS A 683     3375   3252   3558    195   -218   -536       O  
-ATOM    162  CB  LYS A 683     -38.305 -15.830 -18.057  1.00 34.12           C  
-ANISOU  162  CB  LYS A 683     4323   4105   4536    179   -271   -545       C  
-ATOM    163  CG  LYS A 683     -39.163 -16.823 -17.272  1.00 37.23           C  
-ANISOU  163  CG  LYS A 683     4728   4444   4972    166   -295   -525       C  
-ATOM    164  CD  LYS A 683     -39.740 -17.839 -18.230  1.00 42.77           C  
-ANISOU  164  CD  LYS A 683     5429   5123   5699    171   -323   -561       C  
-ATOM    165  CE  LYS A 683     -38.688 -18.854 -18.653  1.00 47.51           C  
-ANISOU  165  CE  LYS A 683     6027   5710   6314    203   -346   -606       C  
-ATOM    166  NZ  LYS A 683     -39.223 -19.672 -19.775  1.00 53.20           N  
-ANISOU  166  NZ  LYS A 683     6744   6417   7051    212   -374   -650       N  
-ATOM    167  N   LYS A 684     -37.254 -13.026 -18.964  1.00 30.03           N  
-ANISOU  167  N   LYS A 684     3785   3693   3933    177   -203   -538       N  
-ATOM    168  CA  LYS A 684     -36.270 -12.188 -19.618  1.00 33.06           C  
-ANISOU  168  CA  LYS A 684     4155   4120   4285    187   -176   -551       C  
-ATOM    169  C   LYS A 684     -35.680 -11.203 -18.633  1.00 31.01           C  
-ANISOU  169  C   LYS A 684     3890   3871   4023    177   -155   -522       C  
-ATOM    170  O   LYS A 684     -34.467 -11.030 -18.571  1.00 29.79           O  
-ANISOU  170  O   LYS A 684     3721   3731   3865    190   -144   -536       O  
-ATOM    171  CB  LYS A 684     -36.926 -11.385 -20.756  1.00 38.62           C  
-ANISOU  171  CB  LYS A 684     4861   4858   4955    181   -160   -550       C  
-ATOM    172  CG  LYS A 684     -35.982 -10.855 -21.809  1.00 43.98           C  
-ANISOU  172  CG  LYS A 684     5528   5582   5600    196   -135   -572       C  
-ATOM    173  CD  LYS A 684     -36.702  -9.913 -22.774  1.00 47.85           C  
-ANISOU  173  CD  LYS A 684     6025   6103   6053    187   -118   -559       C  
-ATOM    174  CE  LYS A 684     -35.775  -9.434 -23.899  1.00 54.85           C  
-ANISOU  174  CE  LYS A 684     6901   7036   6902    202    -90   -578       C  
-ATOM    175  NZ  LYS A 684     -36.393  -8.368 -24.754  1.00 57.19           N  
-ANISOU  175  NZ  LYS A 684     7206   7363   7159    194    -71   -557       N  
-ATOM    176  N   ALA A 685     -36.541 -10.567 -17.843  1.00 30.43           N  
-ANISOU  176  N   ALA A 685     3825   3786   3951    155   -150   -484       N  
-ATOM    177  CA  ALA A 685     -36.066  -9.637 -16.800  1.00 28.88           C  
-ANISOU  177  CA  ALA A 685     3625   3596   3753    146   -134   -458       C  
-ATOM    178  C   ALA A 685     -35.053 -10.353 -15.908  1.00 28.15           C  
-ANISOU  178  C   ALA A 685     3529   3485   3681    162   -150   -468       C  
-ATOM    179  O   ALA A 685     -34.028  -9.798 -15.587  1.00 25.73           O  
-ANISOU  179  O   ALA A 685     3209   3195   3373    168   -138   -472       O  
-ATOM    180  CB  ALA A 685     -37.246  -9.113 -15.977  1.00 28.26           C  
-ANISOU  180  CB  ALA A 685     3557   3503   3676    124   -132   -420       C  
-ATOM    181  N   MET A 686     -35.371 -11.576 -15.489  1.00 28.81           N  
-ANISOU  181  N   MET A 686     3624   3532   3788    169   -177   -471       N  
-ATOM    182  CA  MET A 686     -34.512 -12.312 -14.549  1.00 30.22           C  
-ANISOU  182  CA  MET A 686     3805   3689   3988    186   -196   -475       C  
-ATOM    183  C   MET A 686     -33.187 -12.702 -15.186  1.00 30.66           C  
-ANISOU  183  C   MET A 686     3842   3759   4047    212   -199   -517       C  
-ATOM    184  O   MET A 686     -32.140 -12.666 -14.531  1.00 28.83           O  
-ANISOU  184  O   MET A 686     3601   3529   3823    226   -204   -524       O  
-ATOM    185  CB  MET A 686     -35.249 -13.534 -13.973  1.00 32.30           C  
-ANISOU  185  CB  MET A 686     4088   3906   4278    186   -223   -462       C  
-ATOM    186  CG  MET A 686     -36.426 -13.145 -13.031  1.00 39.22           C  
-ANISOU  186  CG  MET A 686     4979   4769   5153    161   -217   -416       C  
-ATOM    187  SD  MET A 686     -37.446 -14.562 -12.557  1.00 49.50           S  
-ANISOU  187  SD  MET A 686     6302   6017   6489    154   -242   -398       S  
-ATOM    188  CE  MET A 686     -36.400 -15.235 -11.284  1.00 45.16           C  
-ANISOU  188  CE  MET A 686     5764   5443   5953    176   -262   -388       C  
-ATOM    189  N   VAL A 687     -33.235 -13.029 -16.472  1.00 29.89           N  
-ANISOU  189  N   VAL A 687     3738   3675   3942    220   -197   -547       N  
-ATOM    190  CA  VAL A 687     -32.023 -13.331 -17.195  1.00 30.21           C  
-ANISOU  190  CA  VAL A 687     3760   3737   3983    245   -195   -590       C  
-ATOM    191  C   VAL A 687     -31.145 -12.073 -17.279  1.00 30.86           C  
-ANISOU  191  C   VAL A 687     3820   3859   4045    240   -162   -587       C  
-ATOM    192  O   VAL A 687     -29.977 -12.133 -16.943  1.00 30.42           O  
-ANISOU  192  O   VAL A 687     3747   3810   4002    256   -163   -605       O  
-ATOM    193  CB  VAL A 687     -32.320 -13.879 -18.594  1.00 30.47           C  
-ANISOU  193  CB  VAL A 687     3792   3781   4005    255   -198   -623       C  
-ATOM    194  CG1 VAL A 687     -31.047 -13.890 -19.422  1.00 30.61           C  
-ANISOU  194  CG1 VAL A 687     3785   3833   4012    279   -183   -665       C  
-ATOM    195  CG2 VAL A 687     -32.896 -15.288 -18.485  1.00 31.82           C  
-ANISOU  195  CG2 VAL A 687     3978   3906   4206    265   -236   -636       C  
-ATOM    196  N   GLU A 688     -31.737 -10.934 -17.593  1.00 29.42           N  
-ANISOU  196  N   GLU A 688     3639   3700   3839    218   -136   -563       N  
-ATOM    197  CA  GLU A 688     -30.996  -9.676 -17.620  1.00 32.11           C  
-ANISOU  197  CA  GLU A 688     3960   4073   4167    209   -104   -555       C  
-ATOM    198  C   GLU A 688     -30.396  -9.287 -16.276  1.00 31.52           C  
-ANISOU  198  C   GLU A 688     3880   3987   4111    207   -110   -541       C  
-ATOM    199  O   GLU A 688     -29.351  -8.673 -16.241  1.00 30.37           O  
-ANISOU  199  O   GLU A 688     3709   3862   3968    210    -94   -552       O  
-ATOM    200  CB  GLU A 688     -31.853  -8.537 -18.161  1.00 34.14           C  
-ANISOU  200  CB  GLU A 688     4224   4349   4398    185    -79   -528       C  
-ATOM    201  CG  GLU A 688     -31.903  -8.569 -19.672  1.00 39.35           C  
-ANISOU  201  CG  GLU A 688     4881   5040   5032    192    -63   -548       C  
-ATOM    202  CD  GLU A 688     -32.910  -7.625 -20.283  1.00 44.63           C  
-ANISOU  202  CD  GLU A 688     5561   5723   5672    173    -46   -521       C  
-ATOM    203  OE1 GLU A 688     -33.729  -7.000 -19.565  1.00 46.97           O  
-ANISOU  203  OE1 GLU A 688     5869   6004   5973    153    -48   -488       O  
-ATOM    204  OE2 GLU A 688     -32.927  -7.583 -21.517  1.00 47.89           O  
-ANISOU  204  OE2 GLU A 688     5974   6163   6058    180    -32   -535       O  
-ATOM    205  N   TYR A 689     -31.043  -9.660 -15.174  1.00 32.44           N  
-ANISOU  205  N   TYR A 689     4016   4071   4239    203   -133   -519       N  
-ATOM    206  CA  TYR A 689     -30.470  -9.417 -13.848  1.00 31.99           C  
-ANISOU  206  CA  TYR A 689     3956   4003   4195    207   -144   -508       C  
-ATOM    207  C   TYR A 689     -29.402 -10.449 -13.483  1.00 30.62           C  
-ANISOU  207  C   TYR A 689     3775   3816   4044    236   -170   -537       C  
-ATOM    208  O   TYR A 689     -28.838 -10.368 -12.424  1.00 27.94           O  
-ANISOU  208  O   TYR A 689     3432   3467   3715    244   -184   -533       O  
-ATOM    209  CB  TYR A 689     -31.561  -9.431 -12.769  1.00 30.87           C  
-ANISOU  209  CB  TYR A 689     3841   3836   4053    194   -157   -471       C  
-ATOM    210  CG  TYR A 689     -32.528  -8.247 -12.780  1.00 31.11           C  
-ANISOU  210  CG  TYR A 689     3877   3878   4065    167   -134   -441       C  
-ATOM    211  CD1 TYR A 689     -32.075  -6.931 -12.678  1.00 30.19           C  
-ANISOU  211  CD1 TYR A 689     3744   3785   3941    157   -113   -437       C  
-ATOM    212  CD2 TYR A 689     -33.898  -8.459 -12.743  1.00 31.16           C  
-ANISOU  212  CD2 TYR A 689     3904   3869   4066    153   -137   -417       C  
-ATOM    213  CE1 TYR A 689     -32.964  -5.877 -12.585  1.00 30.05           C  
-ANISOU  213  CE1 TYR A 689     3733   3774   3910    136    -96   -410       C  
-ATOM    214  CE2 TYR A 689     -34.798  -7.403 -12.695  1.00 32.79           C  
-ANISOU  214  CE2 TYR A 689     4115   4086   4258    132   -119   -392       C  
-ATOM    215  CZ  TYR A 689     -34.328  -6.112 -12.604  1.00 33.17           C  
-ANISOU  215  CZ  TYR A 689     4148   4156   4298    124    -99   -388       C  
-ATOM    216  OH  TYR A 689     -35.256  -5.077 -12.524  1.00 39.20           O  
-ANISOU  216  OH  TYR A 689     4917   4926   5050    105    -85   -364       O  
-ATOM    217  N   GLU A 690     -29.191 -11.450 -14.336  1.00 34.11           N  
-ANISOU  217  N   GLU A 690     4214   4254   4493    253   -180   -567       N  
-ATOM    218  CA  GLU A 690     -28.235 -12.544 -14.095  1.00 35.29           C  
-ANISOU  218  CA  GLU A 690     4355   4386   4667    284   -208   -598       C  
-ATOM    219  C   GLU A 690     -28.636 -13.439 -12.914  1.00 34.38           C  
-ANISOU  219  C   GLU A 690     4268   4227   4568    292   -244   -577       C  
-ATOM    220  O   GLU A 690     -27.810 -14.061 -12.271  1.00 33.64           O  
-ANISOU  220  O   GLU A 690     4171   4117   4494    316   -269   -590       O  
-ATOM    221  CB  GLU A 690     -26.818 -12.024 -13.921  1.00 41.63           C  
-ANISOU  221  CB  GLU A 690     5125   5213   5478    297   -200   -621       C  
-ATOM    222  CG  GLU A 690     -26.253 -11.359 -15.157  1.00 46.18           C  
-ANISOU  222  CG  GLU A 690     5673   5833   6043    293   -163   -645       C  
-ATOM    223  CD  GLU A 690     -24.833 -10.912 -14.922  1.00 53.93           C  
-ANISOU  223  CD  GLU A 690     6616   6834   7039    304   -155   -669       C  
-ATOM    224  OE1 GLU A 690     -24.657  -9.948 -14.153  1.00 57.86           O  
-ANISOU  224  OE1 GLU A 690     7107   7337   7540    290   -149   -650       O  
-ATOM    225  OE2 GLU A 690     -23.895 -11.534 -15.465  1.00 63.05           O  
-ANISOU  225  OE2 GLU A 690     7748   8001   8208    329   -158   -710       O  
-ATOM    226  N   ILE A 691     -29.928 -13.542 -12.678  1.00 32.81           N  
-ANISOU  226  N   ILE A 691     4095   4007   4363    272   -245   -543       N  
-ATOM    227  CA  ILE A 691     -30.445 -14.448 -11.679  1.00 33.83           C  
-ANISOU  227  CA  ILE A 691     4252   4094   4508    277   -274   -518       C  
-ATOM    228  C   ILE A 691     -30.391 -15.889 -12.167  1.00 34.31           C  
-ANISOU  228  C   ILE A 691     4319   4122   4594    296   -302   -543       C  
-ATOM    229  O   ILE A 691     -30.572 -16.159 -13.346  1.00 32.70           O  
-ANISOU  229  O   ILE A 691     4108   3927   4391    297   -296   -570       O  
-ATOM    230  CB  ILE A 691     -31.863 -14.043 -11.317  1.00 34.81           C  
-ANISOU  230  CB  ILE A 691     4397   4209   4619    247   -262   -475       C  
-ATOM    231  CG1 ILE A 691     -31.697 -12.775 -10.513  1.00 36.76           C  
-ANISOU  231  CG1 ILE A 691     4639   4480   4846    236   -244   -454       C  
-ATOM    232  CG2 ILE A 691     -32.580 -15.133 -10.531  1.00 34.22           C  
-ANISOU  232  CG2 ILE A 691     4351   4088   4563    247   -287   -448       C  
-ATOM    233  CD1 ILE A 691     -32.922 -12.219  -9.927  1.00 40.45           C  
-ANISOU  233  CD1 ILE A 691     5124   4944   5299    211   -231   -413       C  
-ATOM    234  N   ASP A 692     -30.099 -16.802 -11.251  1.00 32.50           N  
-ANISOU  234  N   ASP A 692     4106   3857   4387    314   -334   -534       N  
-ATOM    235  CA  ASP A 692     -30.106 -18.182 -11.593  1.00 34.55           C  
-ANISOU  235  CA  ASP A 692     4374   4077   4675    332   -363   -554       C  
-ATOM    236  C   ASP A 692     -31.520 -18.710 -11.545  1.00 35.13           C  
-ANISOU  236  C   ASP A 692     4473   4117   4759    309   -367   -522       C  
-ATOM    237  O   ASP A 692     -32.020 -19.026 -10.448  1.00 33.74           O  
-ANISOU  237  O   ASP A 692     4321   3908   4589    302   -378   -480       O  
-ATOM    238  CB  ASP A 692     -29.224 -18.975 -10.646  1.00 34.43           C  
-ANISOU  238  CB  ASP A 692     4367   4033   4682    363   -398   -555       C  
-ATOM    239  CG  ASP A 692     -29.106 -20.432 -11.088  1.00 34.45           C  
-ANISOU  239  CG  ASP A 692     4377   3993   4721    385   -432   -582       C  
-ATOM    240  OD1 ASP A 692     -27.993 -20.921 -10.966  1.00 34.88           O  
-ANISOU  240  OD1 ASP A 692     4420   4041   4791    419   -455   -611       O  
-ATOM    241  OD2 ASP A 692     -30.102 -21.075 -11.558  1.00 31.82           O  
-ANISOU  241  OD2 ASP A 692     4058   3631   4402    371   -437   -575       O  
-ATOM    242  N   LEU A 693     -32.116 -18.887 -12.735  1.00 33.93           N  
-ANISOU  242  N   LEU A 693     4314   3968   4609    300   -361   -545       N  
-ATOM    243  CA  LEU A 693     -33.510 -19.331 -12.856  1.00 34.82           C  
-ANISOU  243  CA  LEU A 693     4444   4052   4735    275   -364   -521       C  
-ATOM    244  C   LEU A 693     -33.750 -20.751 -12.411  1.00 34.91           C  
-ANISOU  244  C   LEU A 693     4475   4001   4787    284   -400   -513       C  
-ATOM    245  O   LEU A 693     -34.875 -21.150 -12.100  1.00 37.22           O  
-ANISOU  245  O   LEU A 693     4783   4260   5097    261   -403   -481       O  
-ATOM    246  CB  LEU A 693     -34.010 -19.153 -14.297  1.00 37.76           C  
-ANISOU  246  CB  LEU A 693     4803   4446   5098    268   -353   -553       C  
-ATOM    247  CG  LEU A 693     -34.335 -17.728 -14.695  1.00 40.18           C  
-ANISOU  247  CG  LEU A 693     5098   4803   5365    247   -316   -543       C  
-ATOM    248  CD1 LEU A 693     -34.866 -17.632 -16.115  1.00 42.10           C  
-ANISOU  248  CD1 LEU A 693     5333   5068   5597    244   -309   -573       C  
-ATOM    249  CD2 LEU A 693     -35.383 -17.220 -13.740  1.00 45.12           C  
-ANISOU  249  CD2 LEU A 693     5739   5418   5986    218   -304   -490       C  
-ATOM    250  N   GLN A 694     -32.712 -21.543 -12.384  1.00 34.49           N  
-ANISOU  250  N   GLN A 694     4420   3931   4755    316   -427   -543       N  
-ATOM    251  CA  GLN A 694     -32.908 -22.833 -11.855  1.00 36.05           C  
-ANISOU  251  CA  GLN A 694     4638   4066   4993    325   -461   -529       C  
-ATOM    252  C   GLN A 694     -33.039 -22.790 -10.340  1.00 37.51           C  
-ANISOU  252  C   GLN A 694     4847   4230   5174    318   -463   -471       C  
-ATOM    253  O   GLN A 694     -33.902 -23.433  -9.753  1.00 40.44           O  
-ANISOU  253  O   GLN A 694     5242   4557   5568    301   -472   -431       O  
-ATOM    254  CB  GLN A 694     -31.768 -23.754 -12.246  1.00 35.57           C  
-ANISOU  254  CB  GLN A 694     4568   3989   4958    365   -493   -579       C  
-ATOM    255  CG  GLN A 694     -32.211 -25.144 -11.923  1.00 35.21           C  
-ANISOU  255  CG  GLN A 694     4545   3872   4961    369   -530   -566       C  
-ATOM    256  CD  GLN A 694     -31.242 -26.193 -12.273  1.00 37.83           C  
-ANISOU  256  CD  GLN A 694     4871   4175   5326    409   -568   -614       C  
-ATOM    257  OE1 GLN A 694     -30.025 -26.057 -12.092  1.00 39.76           O  
-ANISOU  257  OE1 GLN A 694     5104   4441   5562    441   -575   -638       O  
-ATOM    258  NE2 GLN A 694     -31.782 -27.310 -12.705  1.00 39.94           N  
-ANISOU  258  NE2 GLN A 694     5147   4390   5637    410   -595   -628       N  
-ATOM    259  N   LYS A 695     -32.124 -22.092  -9.716  1.00 39.46           N  
-ANISOU  259  N   LYS A 695     5089   4508   5395    333   -456   -468       N  
-ATOM    260  CA  LYS A 695     -32.000 -22.139  -8.270  1.00 42.39           C  
-ANISOU  260  CA  LYS A 695     5484   4861   5759    338   -465   -421       C  
-ATOM    261  C   LYS A 695     -32.968 -21.202  -7.627  1.00 42.20           C  
-ANISOU  261  C   LYS A 695     5470   4858   5705    305   -433   -373       C  
-ATOM    262  O   LYS A 695     -33.231 -21.316  -6.457  1.00 42.42           O  
-ANISOU  262  O   LYS A 695     5523   4869   5726    302   -436   -326       O  
-ATOM    263  CB  LYS A 695     -30.580 -21.774  -7.840  1.00 40.91           C  
-ANISOU  263  CB  LYS A 695     5285   4700   5559    371   -476   -444       C  
-ATOM    264  CG  LYS A 695     -29.536 -22.777  -8.274  1.00 42.63           C  
-ANISOU  264  CG  LYS A 695     5493   4895   5809    409   -512   -490       C  
-ATOM    265  CD  LYS A 695     -28.233 -22.412  -7.607  1.00 47.74           C  
-ANISOU  265  CD  LYS A 695     6129   5564   6444    441   -525   -504       C  
-ATOM    266  CE  LYS A 695     -27.055 -23.195  -8.157  1.00 51.01           C  
-ANISOU  266  CE  LYS A 695     6524   5968   6888    481   -556   -560       C  
-ATOM    267  NZ  LYS A 695     -25.802 -22.585  -7.625  1.00 52.16           N  
-ANISOU  267  NZ  LYS A 695     6650   6147   7021    507   -562   -579       N  
-ATOM    268  N   MET A 696     -33.466 -20.237  -8.379  1.00 47.70           N  
-ANISOU  268  N   MET A 696     6148   5594   6381    282   -402   -384       N  
-ATOM    269  CA  MET A 696     -34.477 -19.373  -7.831  1.00 50.00           C  
-ANISOU  269  CA  MET A 696     6448   5903   6648    252   -372   -342       C  
-ATOM    270  C   MET A 696     -35.569 -19.143  -8.826  1.00 50.92           C  
-ANISOU  270  C   MET A 696     6553   6025   6768    223   -353   -348       C  
-ATOM    271  O   MET A 696     -35.573 -18.108  -9.492  1.00 56.78           O  
-ANISOU  271  O   MET A 696     7276   6811   7486    215   -330   -366       O  
-ATOM    272  CB  MET A 696     -33.828 -18.058  -7.446  1.00 51.84           C  
-ANISOU  272  CB  MET A 696     6668   6186   6844    256   -353   -345       C  
-ATOM    273  CG  MET A 696     -34.818 -17.060  -6.913  1.00 57.34           C  
-ANISOU  273  CG  MET A 696     7370   6903   7513    228   -323   -307       C  
-ATOM    274  SD  MET A 696     -33.886 -15.906  -5.945  1.00 59.63           S  
-ANISOU  274  SD  MET A 696     7656   7232   7769    243   -316   -304       S  
-ATOM    275  CE  MET A 696     -34.862 -14.438  -6.085  1.00 58.13           C  
-ANISOU  275  CE  MET A 696     7456   7080   7551    210   -277   -289       C  
-ATOM    276  N   PRO A 697     -36.483 -20.117  -8.958  1.00 55.38           N  
-ANISOU  276  N   PRO A 697     7130   6547   7366    209   -365   -334       N  
-ATOM    277  CA  PRO A 697     -37.581 -19.966  -9.913  1.00 60.34           C  
-ANISOU  277  CA  PRO A 697     7746   7179   8001    183   -352   -343       C  
-ATOM    278  C   PRO A 697     -38.684 -19.051  -9.420  1.00 57.43           C  
-ANISOU  278  C   PRO A 697     7379   6829   7611    152   -321   -302       C  
-ATOM    279  O   PRO A 697     -38.807 -18.819  -8.238  1.00 60.47           O  
-ANISOU  279  O   PRO A 697     7779   7213   7983    147   -311   -260       O  
-ATOM    280  CB  PRO A 697     -38.140 -21.394 -10.047  1.00 60.18           C  
-ANISOU  280  CB  PRO A 697     7737   7098   8031    179   -379   -340       C  
-ATOM    281  CG  PRO A 697     -37.784 -22.072  -8.767  1.00 59.12           C  
-ANISOU  281  CG  PRO A 697     7628   6928   7909    189   -394   -301       C  
-ATOM    282  CD  PRO A 697     -36.458 -21.472  -8.362  1.00 58.62           C  
-ANISOU  282  CD  PRO A 697     7562   6898   7813    219   -395   -315       C  
-ATOM    283  N   LEU A 698     -39.501 -18.572 -10.339  1.00 63.13           N  
-ANISOU  283  N   LEU A 698     8086   7570   8331    133   -307   -316       N  
-ATOM    284  CA  LEU A 698     -40.606 -17.649 -10.034  1.00 68.34           C  
-ANISOU  284  CA  LEU A 698     8742   8250   8973    104   -278   -284       C  
-ATOM    285  C   LEU A 698     -41.463 -18.060  -8.827  1.00 71.55           C  
-ANISOU  285  C   LEU A 698     9166   8626   9393     85   -271   -230       C  
-ATOM    286  O   LEU A 698     -41.687 -17.264  -7.894  1.00 72.44           O  
-ANISOU  286  O   LEU A 698     9285   8761   9479     77   -248   -197       O  
-ATOM    287  CB  LEU A 698     -41.442 -17.511 -11.307  1.00 67.94           C  
-ANISOU  287  CB  LEU A 698     8675   8208   8930     90   -277   -311       C  
-ATOM    288  CG  LEU A 698     -40.754 -16.691 -12.419  1.00 68.93           C  
-ANISOU  288  CG  LEU A 698     8784   8379   9026    105   -271   -353       C  
-ATOM    289  CD1 LEU A 698     -41.529 -16.682 -13.723  1.00 66.15           C  
-ANISOU  289  CD1 LEU A 698     8420   8035   8679     96   -275   -381       C  
-ATOM    290  CD2 LEU A 698     -40.560 -15.274 -11.913  1.00 68.86           C  
-ANISOU  290  CD2 LEU A 698     8773   8413   8979    100   -242   -333       C  
-ATOM    291  N   GLY A 699     -41.887 -19.318  -8.815  1.00 76.99           N  
-ANISOU  291  N   GLY A 699     9863   9264  10125     79   -291   -222       N  
-ATOM    292  CA  GLY A 699     -42.706 -19.832  -7.720  1.00 81.24           C  
-ANISOU  292  CA  GLY A 699    10417   9769  10681     58   -282   -168       C  
-ATOM    293  C   GLY A 699     -42.002 -19.939  -6.372  1.00 83.99           C  
-ANISOU  293  C   GLY A 699    10791  10113  11010     75   -281   -131       C  
-ATOM    294  O   GLY A 699     -42.655 -20.045  -5.342  1.00 80.98           O  
-ANISOU  294  O   GLY A 699    10424   9720  10626     60   -264    -81       O  
-ATOM    295  N   LYS A 700     -40.670 -19.915  -6.372  1.00 86.70           N  
-ANISOU  295  N   LYS A 700    11138  10467  11337    108   -300   -157       N  
-ATOM    296  CA  LYS A 700     -39.900 -20.139  -5.165  1.00 88.59           C  
-ANISOU  296  CA  LYS A 700    11402  10699  11560    129   -308   -129       C  
-ATOM    297  C   LYS A 700     -39.582 -18.843  -4.431  1.00 88.51           C  
-ANISOU  297  C   LYS A 700    11392  10740  11498    135   -286   -118       C  
-ATOM    298  O   LYS A 700     -39.277 -18.874  -3.240  1.00101.43           O  
-ANISOU  298  O   LYS A 700    13051  12375  13113    148   -287    -85       O  
-ATOM    299  CB  LYS A 700     -38.593 -20.868  -5.504  1.00 83.69           C  
-ANISOU  299  CB  LYS A 700    10784  10060  10955    164   -345   -166       C  
-ATOM    300  N   LEU A 701     -39.624 -17.704  -5.117  1.00 87.94           N  
-ANISOU  300  N   LEU A 701    11297  10712  11405    129   -268   -146       N  
-ATOM    301  CA  LEU A 701     -39.329 -16.429  -4.455  1.00 85.37           C  
-ANISOU  301  CA  LEU A 701    10970  10432  11035    134   -249   -140       C  
-ATOM    302  C   LEU A 701     -40.100 -16.337  -3.143  1.00 80.66           C  
-ANISOU  302  C   LEU A 701    10394   9834  10421    123   -230    -86       C  
-ATOM    303  O   LEU A 701     -41.279 -16.686  -3.079  1.00 82.17           O  
-ANISOU  303  O   LEU A 701    10587  10006  10628     97   -215    -57       O  
-ATOM    304  CB  LEU A 701     -39.645 -15.249  -5.367  1.00 89.04           C  
-ANISOU  304  CB  LEU A 701    11409  10936  11487    120   -228   -166       C  
-ATOM    305  N   SER A 702     -39.410 -15.957  -2.077  1.00 76.96           N  
-ANISOU  305  N   SER A 702     9940   9382   9919    144   -234    -73       N  
-ATOM    306  CA  SER A 702     -40.054 -15.893  -0.776  1.00 78.43           C  
-ANISOU  306  CA  SER A 702    10149   9570  10080    139   -216    -22       C  
-ATOM    307  C   SER A 702     -39.881 -14.501  -0.194  1.00 75.91           C  
-ANISOU  307  C   SER A 702     9824   9301   9717    146   -199    -28       C  
-ATOM    308  O   SER A 702     -38.826 -13.881  -0.346  1.00 81.87           O  
-ANISOU  308  O   SER A 702    10570  10079  10460    167   -213    -63       O  
-ATOM    309  CB  SER A 702     -39.502 -16.955   0.176  1.00 79.27           C  
-ANISOU  309  CB  SER A 702    10288   9645  10188    161   -239      8       C  
-ATOM    310  OG  SER A 702     -38.621 -16.399   1.133  1.00 84.42           O  
-ANISOU  310  OG  SER A 702    10952  10324  10798    191   -249      7       O  
-ATOM    311  N   LYS A 703     -40.937 -14.016   0.449  1.00 66.76           N  
-ANISOU  311  N   LYS A 703     8670   8157   8538    128   -169      5       N  
-ATOM    312  CA  LYS A 703     -40.939 -12.706   1.057  1.00 65.24           C  
-ANISOU  312  CA  LYS A 703     8473   8010   8306    134   -152      1       C  
-ATOM    313  C   LYS A 703     -39.808 -12.598   2.098  1.00 65.66           C  
-ANISOU  313  C   LYS A 703     8547   8076   8327    170   -174     -1       C  
-ATOM    314  O   LYS A 703     -39.179 -11.556   2.200  1.00 61.66           O  
-ANISOU  314  O   LYS A 703     8029   7601   7800    184   -178    -30       O  
-ATOM    315  CB  LYS A 703     -42.294 -12.417   1.727  1.00 64.30           C  
-ANISOU  315  CB  LYS A 703     8359   7902   8171    113   -117     40       C  
-ATOM    316  N   ARG A 704     -39.553 -13.669   2.852  1.00 61.44           N  
-ANISOU  316  N   ARG A 704     8041   7513   7789    185   -190     31       N  
-ATOM    317  CA  ARG A 704     -38.585 -13.627   3.947  1.00 57.12           C  
-ANISOU  317  CA  ARG A 704     7517   6978   7207    222   -213     34       C  
-ATOM    318  C   ARG A 704     -37.157 -13.633   3.433  1.00 54.52           C  
-ANISOU  318  C   ARG A 704     7174   6647   6892    247   -249    -14       C  
-ATOM    319  O   ARG A 704     -36.287 -12.983   4.018  1.00 53.50           O  
-ANISOU  319  O   ARG A 704     7045   6544   6737    274   -265    -34       O  
-ATOM    320  CB  ARG A 704     -38.805 -14.785   4.936  1.00 57.54           C  
-ANISOU  320  CB  ARG A 704     7610   7003   7252    231   -218     88       C  
-ATOM    321  N   GLN A 705     -36.896 -14.355   2.344  1.00 51.78           N  
-ANISOU  321  N   GLN A 705     6814   6271   6589    241   -262    -34       N  
-ATOM    322  CA  GLN A 705     -35.554 -14.302   1.741  1.00 51.34           C  
-ANISOU  322  CA  GLN A 705     6739   6218   6549    264   -292    -84       C  
-ATOM    323  C   GLN A 705     -35.281 -12.885   1.203  1.00 48.55           C  
-ANISOU  323  C   GLN A 705     6353   5906   6187    257   -278   -124       C  
-ATOM    324  O   GLN A 705     -34.195 -12.352   1.375  1.00 42.88           O  
-ANISOU  324  O   GLN A 705     5624   5207   5461    279   -296   -156       O  
-ATOM    325  CB  GLN A 705     -35.360 -15.339   0.617  1.00 49.70           C  
-ANISOU  325  CB  GLN A 705     6522   5974   6388    260   -307   -103       C  
-ATOM    326  N   ILE A 706     -36.264 -12.309   0.521  1.00 45.98           N  
-ANISOU  326  N   ILE A 706     6012   5591   5867    225   -247   -123       N  
-ATOM    327  CA  ILE A 706     -36.078 -11.024  -0.112  1.00 51.62           C  
-ANISOU  327  CA  ILE A 706     6698   6339   6578    216   -233   -156       C  
-ATOM    328  C   ILE A 706     -35.827  -9.987   0.977  1.00 50.59           C  
-ANISOU  328  C   ILE A 706     6571   6239   6412    230   -231   -156       C  
-ATOM    329  O   ILE A 706     -34.959  -9.149   0.838  1.00 46.26           O  
-ANISOU  329  O   ILE A 706     6003   5711   5863    240   -239   -190       O  
-ATOM    330  CB  ILE A 706     -37.248 -10.675  -1.075  1.00 55.32           C  
-ANISOU  330  CB  ILE A 706     7151   6810   7059    182   -203   -152       C  
-ATOM    331  CG1 ILE A 706     -37.156 -11.559  -2.339  1.00 63.02           C  
-ANISOU  331  CG1 ILE A 706     8115   7759   8069    175   -212   -171       C  
-ATOM    332  CG2 ILE A 706     -37.215  -9.211  -1.483  1.00 54.25           C  
-ANISOU  332  CG2 ILE A 706     6991   6707   6913    173   -186   -176       C  
-ATOM    333  CD1 ILE A 706     -38.396 -11.601  -3.223  1.00 66.99           C  
-ANISOU  333  CD1 ILE A 706     8610   8256   8589    145   -192   -163       C  
-ATOM    334  N   GLN A 707     -36.578 -10.071   2.063  1.00 53.31           N  
-ANISOU  334  N   GLN A 707     6941   6586   6729    231   -221   -117       N  
-ATOM    335  CA  GLN A 707     -36.404  -9.174   3.198  1.00 50.54           C  
-ANISOU  335  CA  GLN A 707     6599   6265   6339    248   -221   -117       C  
-ATOM    336  C   GLN A 707     -35.001  -9.266   3.769  1.00 46.65           C  
-ANISOU  336  C   GLN A 707     6110   5776   5839    284   -259   -141       C  
-ATOM    337  O   GLN A 707     -34.370  -8.259   4.051  1.00 43.41           O  
-ANISOU  337  O   GLN A 707     5685   5392   5418    296   -267   -171       O  
-ATOM    338  CB  GLN A 707     -37.457  -9.495   4.242  1.00 58.59           C  
-ANISOU  338  CB  GLN A 707     7648   7285   7329    244   -203    -68       C  
-ATOM    339  CG  GLN A 707     -37.343  -8.734   5.550  1.00 67.12           C  
-ANISOU  339  CG  GLN A 707     8743   8397   8361    267   -204    -64       C  
-ATOM    340  CD  GLN A 707     -38.476  -9.061   6.513  1.00 70.23           C  
-ANISOU  340  CD  GLN A 707     9165   8796   8723    262   -179    -13       C  
-ATOM    341  OE1 GLN A 707     -39.591  -9.309   6.070  1.00 74.68           O  
-ANISOU  341  OE1 GLN A 707     9724   9349   9303    232   -149     12       O  
-ATOM    342  NE2 GLN A 707     -38.215  -9.009   7.816  1.00 74.40           N  
-ANISOU  342  NE2 GLN A 707     9720   9342   9205    292   -189      2       N  
-ATOM    343  N   ALA A 708     -34.484 -10.474   3.880  1.00 43.10           N  
-ANISOU  343  N   ALA A 708     5677   5298   5400    301   -284   -131       N  
-ATOM    344  CA  ALA A 708     -33.114 -10.661   4.389  1.00 40.38           C  
-ANISOU  344  CA  ALA A 708     5335   4955   5053    339   -324   -156       C  
-ATOM    345  C   ALA A 708     -32.075 -10.113   3.406  1.00 39.16           C  
-ANISOU  345  C   ALA A 708     5140   4810   4930    340   -334   -210       C  
-ATOM    346  O   ALA A 708     -31.030  -9.615   3.802  1.00 43.44           O  
-ANISOU  346  O   ALA A 708     5669   5367   5467    364   -358   -242       O  
-ATOM    347  CB  ALA A 708     -32.861 -12.141   4.666  1.00 40.84           C  
-ANISOU  347  CB  ALA A 708     5422   4977   5120    357   -349   -130       C  
-ATOM    348  N   ALA A 709     -32.366 -10.229   2.115  1.00 37.71           N  
-ANISOU  348  N   ALA A 709     4935   4615   4777    314   -316   -221       N  
-ATOM    349  CA  ALA A 709     -31.515  -9.695   1.068  1.00 34.04           C  
-ANISOU  349  CA  ALA A 709     4431   4161   4340    310   -317   -268       C  
-ATOM    350  C   ALA A 709     -31.454  -8.177   1.150  1.00 31.61           C  
-ANISOU  350  C   ALA A 709     4103   3887   4023    300   -302   -287       C  
-ATOM    351  O   ALA A 709     -30.388  -7.588   0.986  1.00 33.19           O  
-ANISOU  351  O   ALA A 709     4275   4100   4235    311   -314   -325       O  
-ATOM    352  CB  ALA A 709     -32.019 -10.144  -0.319  1.00 34.85           C  
-ANISOU  352  CB  ALA A 709     4521   4249   4471    285   -298   -271       C  
-ATOM    353  N   TYR A 710     -32.596  -7.536   1.378  1.00 31.81           N  
-ANISOU  353  N   TYR A 710     4137   3923   4028    280   -274   -263       N  
-ATOM    354  CA  TYR A 710     -32.624  -6.093   1.611  1.00 31.43           C  
-ANISOU  354  CA  TYR A 710     4072   3902   3969    273   -263   -280       C  
-ATOM    355  C   TYR A 710     -31.670  -5.708   2.752  1.00 32.82           C  
-ANISOU  355  C   TYR A 710     4250   4092   4128    305   -293   -299       C  
-ATOM    356  O   TYR A 710     -30.879  -4.777   2.634  1.00 34.55           O  
-ANISOU  356  O   TYR A 710     4442   4326   4361    308   -300   -335       O  
-ATOM    357  CB  TYR A 710     -34.038  -5.617   1.957  1.00 32.45           C  
-ANISOU  357  CB  TYR A 710     4216   4039   4074    254   -234   -248       C  
-ATOM    358  CG  TYR A 710     -34.956  -5.362   0.779  1.00 34.35           C  
-ANISOU  358  CG  TYR A 710     4442   4276   4332    220   -203   -241       C  
-ATOM    359  CD1 TYR A 710     -34.621  -4.461  -0.214  1.00 32.76           C  
-ANISOU  359  CD1 TYR A 710     4211   4084   4151    206   -193   -269       C  
-ATOM    360  CD2 TYR A 710     -36.198  -6.002   0.680  1.00 36.13           C  
-ANISOU  360  CD2 TYR A 710     4685   4489   4554    203   -185   -206       C  
-ATOM    361  CE1 TYR A 710     -35.489  -4.200  -1.266  1.00 35.08           C  
-ANISOU  361  CE1 TYR A 710     4496   4377   4457    178   -167   -262       C  
-ATOM    362  CE2 TYR A 710     -37.066  -5.757  -0.378  1.00 34.26           C  
-ANISOU  362  CE2 TYR A 710     4434   4250   4332    175   -161   -203       C  
-ATOM    363  CZ  TYR A 710     -36.710  -4.848  -1.347  1.00 35.24           C  
-ANISOU  363  CZ  TYR A 710     4532   4385   4472    164   -153   -230       C  
-ATOM    364  OH  TYR A 710     -37.579  -4.616  -2.402  1.00 37.62           O  
-ANISOU  364  OH  TYR A 710     4823   4686   4785    139   -132   -226       O  
-ATOM    365  N   SER A 711     -31.757  -6.407   3.871  1.00 35.39           N  
-ANISOU  365  N   SER A 711     4609   4413   4425    329   -311   -275       N  
-ATOM    366  CA  SER A 711     -30.898  -6.095   5.030  1.00 37.04           C  
-ANISOU  366  CA  SER A 711     4824   4636   4612    364   -344   -294       C  
-ATOM    367  C   SER A 711     -29.405  -6.226   4.702  1.00 37.52           C  
-ANISOU  367  C   SER A 711     4858   4693   4704    383   -377   -337       C  
-ATOM    368  O   SER A 711     -28.586  -5.380   5.078  1.00 40.51           O  
-ANISOU  368  O   SER A 711     5216   5090   5087    398   -396   -374       O  
-ATOM    369  CB  SER A 711     -31.214  -7.028   6.190  1.00 38.29           C  
-ANISOU  369  CB  SER A 711     5028   4789   4733    388   -359   -255       C  
-ATOM    370  OG  SER A 711     -32.542  -6.849   6.635  1.00 41.91           O  
-ANISOU  370  OG  SER A 711     5509   5255   5161    372   -328   -216       O  
-ATOM    371  N   ILE A 712     -29.045  -7.278   3.978  1.00 36.36           N  
-ANISOU  371  N   ILE A 712     4708   4523   4583    385   -384   -337       N  
-ATOM    372  CA  ILE A 712     -27.643  -7.463   3.582  1.00 37.33           C  
-ANISOU  372  CA  ILE A 712     4801   4643   4738    403   -412   -380       C  
-ATOM    373  C   ILE A 712     -27.174  -6.347   2.692  1.00 33.31           C  
-ANISOU  373  C   ILE A 712     4247   4151   4260    382   -394   -417       C  
-ATOM    374  O   ILE A 712     -26.072  -5.836   2.857  1.00 34.04           O  
-ANISOU  374  O   ILE A 712     4311   4254   4370    397   -416   -457       O  
-ATOM    375  CB  ILE A 712     -27.426  -8.818   2.877  1.00 40.08           C  
-ANISOU  375  CB  ILE A 712     5154   4964   5111    408   -420   -374       C  
-ATOM    376  CG1 ILE A 712     -27.574  -9.936   3.903  1.00 46.53           C  
-ANISOU  376  CG1 ILE A 712     6016   5761   5904    436   -448   -340       C  
-ATOM    377  CG2 ILE A 712     -26.045  -8.894   2.194  1.00 39.33           C  
-ANISOU  377  CG2 ILE A 712     5019   4870   5055    422   -440   -423       C  
-ATOM    378  CD1 ILE A 712     -27.648 -11.313   3.265  1.00 52.40           C  
-ANISOU  378  CD1 ILE A 712     6770   6470   6671    437   -454   -326       C  
-ATOM    379  N   LEU A 713     -28.021  -5.937   1.763  1.00 35.54           N  
-ANISOU  379  N   LEU A 713     4521   4434   4549    347   -355   -405       N  
-ATOM    380  CA  LEU A 713     -27.691  -4.770   0.926  1.00 35.67           C  
-ANISOU  380  CA  LEU A 713     4498   4465   4590    324   -334   -433       C  
-ATOM    381  C   LEU A 713     -27.503  -3.493   1.756  1.00 34.49           C  
-ANISOU  381  C   LEU A 713     4339   4335   4433    327   -341   -450       C  
-ATOM    382  O   LEU A 713     -26.647  -2.681   1.432  1.00 32.85           O  
-ANISOU  382  O   LEU A 713     4094   4135   4253    323   -343   -485       O  
-ATOM    383  CB  LEU A 713     -28.754  -4.532  -0.136  1.00 34.18           C  
-ANISOU  383  CB  LEU A 713     4308   4274   4404    288   -293   -412       C  
-ATOM    384  CG  LEU A 713     -28.786  -5.558  -1.257  1.00 34.47           C  
-ANISOU  384  CG  LEU A 713     4343   4297   4458    281   -285   -409       C  
-ATOM    385  CD1 LEU A 713     -29.868  -5.211  -2.267  1.00 34.31           C  
-ANISOU  385  CD1 LEU A 713     4322   4278   4437    248   -248   -391       C  
-ATOM    386  CD2 LEU A 713     -27.439  -5.621  -1.930  1.00 34.58           C  
-ANISOU  386  CD2 LEU A 713     4320   4315   4504    290   -294   -449       C  
-ATOM    387  N   SER A 714     -28.268  -3.350   2.833  1.00 36.86           N  
-ANISOU  387  N   SER A 714     4670   4640   4695    336   -346   -427       N  
-ATOM    388  CA  SER A 714     -28.086  -2.218   3.758  1.00 41.38           C  
-ANISOU  388  CA  SER A 714     5237   5229   5255    347   -358   -447       C  
-ATOM    389  C   SER A 714     -26.729  -2.286   4.456  1.00 40.71           C  
-ANISOU  389  C   SER A 714     5139   5150   5180    381   -403   -485       C  
-ATOM    390  O   SER A 714     -26.026  -1.280   4.553  1.00 39.09           O  
-ANISOU  390  O   SER A 714     4901   4953   4997    381   -414   -522       O  
-ATOM    391  CB  SER A 714     -29.227  -2.140   4.804  1.00 43.48           C  
-ANISOU  391  CB  SER A 714     5542   5504   5472    353   -352   -414       C  
-ATOM    392  OG  SER A 714     -30.444  -1.625   4.246  1.00 48.35           O  
-ANISOU  392  OG  SER A 714     6162   6123   6087    321   -312   -391       O  
-ATOM    393  N   GLU A 715     -26.340  -3.479   4.890  1.00 43.73           N  
-ANISOU  393  N   GLU A 715     5542   5522   5551    409   -430   -476       N  
-ATOM    394  CA  GLU A 715     -24.993  -3.664   5.481  1.00 47.06           C  
-ANISOU  394  CA  GLU A 715     5949   5947   5985    445   -477   -514       C  
-ATOM    395  C   GLU A 715     -23.877  -3.370   4.468  1.00 43.99           C  
-ANISOU  395  C   GLU A 715     5507   5556   5652    434   -477   -556       C  
-ATOM    396  O   GLU A 715     -22.859  -2.771   4.786  1.00 39.47           O  
-ANISOU  396  O   GLU A 715     4903   4992   5102    448   -503   -599       O  
-ATOM    397  CB  GLU A 715     -24.838  -5.069   6.054  1.00 47.62           C  
-ANISOU  397  CB  GLU A 715     6056   6004   6034    478   -507   -492       C  
-ATOM    398  CG  GLU A 715     -25.780  -5.370   7.217  1.00 54.49           C  
-ANISOU  398  CG  GLU A 715     6978   6879   6847    494   -510   -449       C  
-ATOM    399  CD  GLU A 715     -25.506  -6.747   7.837  1.00 63.64           C  
-ANISOU  399  CD  GLU A 715     8173   8022   7986    529   -543   -426       C  
-ATOM    400  OE1 GLU A 715     -26.467  -7.532   8.063  1.00 63.60           O  
-ANISOU  400  OE1 GLU A 715     8209   8004   7953    525   -526   -375       O  
-ATOM    401  OE2 GLU A 715     -24.306  -7.035   8.113  1.00 66.76           O  
-ANISOU  401  OE2 GLU A 715     8555   8415   8397    562   -586   -459       O  
-ATOM    402  N   VAL A 716     -24.088  -3.781   3.235  1.00 43.21           N  
-ANISOU  402  N   VAL A 716     5396   5446   5574    409   -446   -545       N  
-ATOM    403  CA  VAL A 716     -23.104  -3.502   2.190  1.00 44.56           C  
-ANISOU  403  CA  VAL A 716     5517   5620   5795    396   -437   -582       C  
-ATOM    404  C   VAL A 716     -22.906  -1.999   2.012  1.00 45.46           C  
-ANISOU  404  C   VAL A 716     5595   5746   5930    373   -420   -605       C  
-ATOM    405  O   VAL A 716     -21.767  -1.520   1.949  1.00 47.43           O  
-ANISOU  405  O   VAL A 716     5803   6002   6217    378   -435   -646       O  
-ATOM    406  CB  VAL A 716     -23.519  -4.120   0.846  1.00 41.53           C  
-ANISOU  406  CB  VAL A 716     5130   5226   5422    372   -402   -564       C  
-ATOM    407  CG1 VAL A 716     -22.673  -3.579  -0.288  1.00 42.45           C  
-ANISOU  407  CG1 VAL A 716     5196   5352   5583    353   -381   -597       C  
-ATOM    408  CG2 VAL A 716     -23.426  -5.628   0.896  1.00 41.74           C  
-ANISOU  408  CG2 VAL A 716     5182   5236   5443    397   -423   -552       C  
-ATOM    409  N   GLN A 717     -24.014  -1.268   1.929  1.00 46.44           N  
-ANISOU  409  N   GLN A 717     5735   5873   6035    347   -391   -579       N  
-ATOM    410  CA  GLN A 717     -23.981   0.163   1.707  1.00 47.50           C  
-ANISOU  410  CA  GLN A 717     5841   6014   6192    322   -373   -595       C  
-ATOM    411  C   GLN A 717     -23.225   0.820   2.844  1.00 44.61           C  
-ANISOU  411  C   GLN A 717     5462   5655   5832    346   -413   -632       C  
-ATOM    412  O   GLN A 717     -22.393   1.706   2.605  1.00 43.63           O  
-ANISOU  412  O   GLN A 717     5295   5533   5751    336   -415   -667       O  
-ATOM    413  CB  GLN A 717     -25.405   0.752   1.592  1.00 51.61           C  
-ANISOU  413  CB  GLN A 717     6388   6536   6687    297   -341   -560       C  
-ATOM    414  CG  GLN A 717     -25.437   2.212   1.143  1.00 54.28           C  
-ANISOU  414  CG  GLN A 717     6697   6876   7053    269   -319   -573       C  
-ATOM    415  CD  GLN A 717     -24.677   2.440  -0.156  1.00 62.70           C  
-ANISOU  415  CD  GLN A 717     7721   7939   8163    245   -295   -586       C  
-ATOM    416  OE1 GLN A 717     -25.114   2.014  -1.230  1.00 64.94           O  
-ANISOU  416  OE1 GLN A 717     8009   8221   8445    226   -264   -563       O  
-ATOM    417  NE2 GLN A 717     -23.528   3.129  -0.068  1.00 67.31           N  
-ANISOU  417  NE2 GLN A 717     8263   8524   8788    245   -309   -625       N  
-ATOM    418  N   GLN A 718     -23.500   0.385   4.068  1.00 41.67           N  
-ANISOU  418  N   GLN A 718     5126   5287   5418    379   -444   -624       N  
-ATOM    419  CA  GLN A 718     -22.788   0.919   5.217  1.00 46.75           C  
-ANISOU  419  CA  GLN A 718     5761   5940   6062    408   -488   -661       C  
-ATOM    420  C   GLN A 718     -21.275   0.618   5.150  1.00 47.96           C  
-ANISOU  420  C   GLN A 718     5874   6091   6256    428   -522   -706       C  
-ATOM    421  O   GLN A 718     -20.447   1.492   5.412  1.00 46.60           O  
-ANISOU  421  O   GLN A 718     5664   5923   6118    430   -542   -749       O  
-ATOM    422  CB  GLN A 718     -23.399   0.394   6.513  1.00 50.79           C  
-ANISOU  422  CB  GLN A 718     6325   6460   6513    442   -513   -640       C  
-ATOM    423  CG  GLN A 718     -22.919   1.163   7.743  1.00 61.77           C  
-ANISOU  423  CG  GLN A 718     7712   7864   7893    472   -555   -677       C  
-ATOM    424  CD  GLN A 718     -23.064   0.416   9.061  1.00 63.52           C  
-ANISOU  424  CD  GLN A 718     7982   8098   8057    517   -592   -664       C  
-ATOM    425  OE1 GLN A 718     -22.943  -0.816   9.136  1.00 68.71           O  
-ANISOU  425  OE1 GLN A 718     8663   8748   8696    537   -604   -641       O  
-ATOM    426  NE2 GLN A 718     -23.307   1.170  10.110  1.00 64.28           N  
-ANISOU  426  NE2 GLN A 718     8091   8210   8122    536   -611   -680       N  
-ATOM    427  N   ALA A 719     -20.924  -0.615   4.805  1.00 49.08           N  
-ANISOU  427  N   ALA A 719     6023   6227   6399    442   -529   -697       N  
-ATOM    428  CA  ALA A 719     -19.513  -1.000   4.686  1.00 51.91           C  
-ANISOU  428  CA  ALA A 719     6342   6584   6798    463   -560   -739       C  
-ATOM    429  C   ALA A 719     -18.790  -0.214   3.577  1.00 49.91           C  
-ANISOU  429  C   ALA A 719     6027   6331   6605    429   -531   -769       C  
-ATOM    430  O   ALA A 719     -17.696   0.235   3.767  1.00 49.97           O  
-ANISOU  430  O   ALA A 719     5991   6342   6653    438   -556   -814       O  
-ATOM    431  CB  ALA A 719     -19.397  -2.493   4.449  1.00 52.34           C  
-ANISOU  431  CB  ALA A 719     6417   6628   6841    484   -569   -721       C  
-ATOM    432  N   VAL A 720     -19.437  -0.006   2.449  1.00 51.28           N  
-ANISOU  432  N   VAL A 720     6197   6501   6784    390   -480   -742       N  
-ATOM    433  CA  VAL A 720     -18.891   0.871   1.406  1.00 54.70           C  
-ANISOU  433  CA  VAL A 720     6578   6936   7269    355   -446   -761       C  
-ATOM    434  C   VAL A 720     -18.682   2.323   1.873  1.00 55.69           C  
-ANISOU  434  C   VAL A 720     6677   7063   7420    341   -452   -786       C  
-ATOM    435  O   VAL A 720     -17.580   2.894   1.729  1.00 55.56           O  
-ANISOU  435  O   VAL A 720     6607   7047   7456    336   -461   -826       O  
-ATOM    436  CB  VAL A 720     -19.793   0.853   0.158  1.00 56.14           C  
-ANISOU  436  CB  VAL A 720     6772   7117   7443    319   -390   -722       C  
-ATOM    437  CG1 VAL A 720     -19.402   1.930  -0.846  1.00 57.96           C  
-ANISOU  437  CG1 VAL A 720     6955   7349   7718    280   -352   -733       C  
-ATOM    438  CG2 VAL A 720     -19.712  -0.522  -0.478  1.00 58.90           C  
-ANISOU  438  CG2 VAL A 720     7132   7464   7783    331   -386   -711       C  
-ATOM    439  N   SER A 721     -19.722   2.914   2.454  1.00 54.68           N  
-ANISOU  439  N   SER A 721     6583   6933   7258    336   -449   -764       N  
-ATOM    440  CA  SER A 721     -19.620   4.301   2.947  1.00 54.94           C  
-ANISOU  440  CA  SER A 721     6596   6965   7314    325   -458   -789       C  
-ATOM    441  C   SER A 721     -18.372   4.546   3.826  1.00 52.57           C  
-ANISOU  441  C   SER A 721     6261   6667   7046    353   -511   -845       C  
-ATOM    442  O   SER A 721     -17.799   5.622   3.761  1.00 51.53           O  
-ANISOU  442  O   SER A 721     6086   6529   6964    336   -513   -877       O  
-ATOM    443  CB  SER A 721     -20.906   4.724   3.661  1.00 54.67           C  
-ANISOU  443  CB  SER A 721     6608   6931   7231    327   -456   -762       C  
-ATOM    444  OG  SER A 721     -21.961   4.962   2.744  1.00 52.16           O  
-ANISOU  444  OG  SER A 721     6306   6609   6903    293   -407   -721       O  
-ATOM    445  N   GLN A 722     -17.935   3.556   4.611  1.00 56.61           N  
-ANISOU  445  N   GLN A 722     6790   7186   7534    397   -555   -857       N  
-ATOM    446  CA  GLN A 722     -16.570   3.595   5.213  1.00 57.96           C  
-ANISOU  446  CA  GLN A 722     6920   7360   7742    425   -605   -914       C  
-ATOM    447  C   GLN A 722     -15.539   2.646   4.596  1.00 62.77           C  
-ANISOU  447  C   GLN A 722     7496   7969   8383    436   -610   -931       C  
-ATOM    448  O   GLN A 722     -15.358   2.594   3.369  1.00 63.86           O  
-ANISOU  448  O   GLN A 722     7605   8104   8553    404   -566   -921       O  
-ATOM    449  CB  GLN A 722     -16.612   3.354   6.713  1.00 60.42           C  
-ANISOU  449  CB  GLN A 722     7267   7680   8009    474   -663   -929       C  
-ATOM    450  CG  GLN A 722     -17.138   2.018   7.203  1.00 62.61           C  
-ANISOU  450  CG  GLN A 722     7603   7962   8222    508   -678   -892       C  
-ATOM    451  CD  GLN A 722     -18.477   2.160   7.899  1.00 61.06           C  
-ANISOU  451  CD  GLN A 722     7466   7773   7961    512   -668   -853       C  
-ATOM    452  OE1 GLN A 722     -19.370   2.824   7.382  1.00 69.16           O  
-ANISOU  452  OE1 GLN A 722     8498   8795   8984    476   -625   -828       O  
-ATOM    453  NE2 GLN A 722     -18.628   1.542   9.070  1.00 57.40           N  
-ANISOU  453  NE2 GLN A 722     7047   7319   7443    557   -709   -846       N  
-ATOM    454  N   ASP A 726     -12.082  -3.977   2.462  1.00 86.95           N  
-ANISOU  454  N   ASP A 726    10513  11025  11500    566   -673   -977       N  
-ATOM    455  CA  ASP A 726     -12.189  -4.719   1.202  1.00 90.79           C  
-ANISOU  455  CA  ASP A 726    10992  11509  11994    551   -631   -963       C  
-ATOM    456  C   ASP A 726     -12.524  -6.192   1.403  1.00 94.24           C  
-ANISOU  456  C   ASP A 726    11479  11929  12398    587   -657   -940       C  
-ATOM    457  O   ASP A 726     -13.196  -6.803   0.576  1.00 88.42           O  
-ANISOU  457  O   ASP A 726    10765  11185  11646    572   -622   -910       O  
-ATOM    458  CB  ASP A 726     -10.877  -4.619   0.426  1.00 94.96           C  
-ANISOU  458  CB  ASP A 726    11445  12050  12587    549   -621  -1014       C  
-ATOM    459  N   SER A 727     -12.024  -6.756   2.495  1.00 94.26           N  
-ANISOU  459  N   SER A 727    11496  11925  12393    635   -719   -956       N  
-ATOM    460  CA  SER A 727     -12.280  -8.143   2.883  1.00 87.47           C  
-ANISOU  460  CA  SER A 727    10688  11045  11504    673   -753   -932       C  
-ATOM    461  C   SER A 727     -13.719  -8.379   3.379  1.00 82.49           C  
-ANISOU  461  C   SER A 727    10131  10401  10810    665   -742   -868       C  
-ATOM    462  O   SER A 727     -14.364  -9.344   2.968  1.00 77.41           O  
-ANISOU  462  O   SER A 727     9524   9739  10149    664   -729   -834       O  
-ATOM    463  CB  SER A 727     -11.269  -8.529   3.971  1.00 84.03           C  
-ANISOU  463  CB  SER A 727    10245  10607  11077    728   -825   -968       C  
-ATOM    464  OG  SER A 727     -11.522  -9.804   4.516  1.00 84.02           O  
-ANISOU  464  OG  SER A 727    10297  10583  11044    768   -863   -941       O  
-ATOM    465  N   GLN A 728     -14.207  -7.521   4.279  1.00 77.50           N  
-ANISOU  465  N   GLN A 728     9521   9778  10147    659   -749   -855       N  
-ATOM    466  CA  GLN A 728     -15.569  -7.653   4.813  1.00 74.07           C  
-ANISOU  466  CA  GLN A 728     9154   9336   9654    651   -737   -796       C  
-ATOM    467  C   GLN A 728     -16.621  -7.448   3.724  1.00 69.68           C  
-ANISOU  467  C   GLN A 728     8605   8778   9093    601   -672   -761       C  
-ATOM    468  O   GLN A 728     -17.671  -8.078   3.765  1.00 64.52           O  
-ANISOU  468  O   GLN A 728     8002   8110   8404    595   -658   -713       O  
-ATOM    469  CB  GLN A 728     -15.806  -6.669   5.955  1.00 70.72           C  
-ANISOU  469  CB  GLN A 728     8745   8927   9200    657   -756   -797       C  
-ATOM    470  N   ILE A 729     -16.321  -6.587   2.745  1.00 67.27           N  
-ANISOU  470  N   ILE A 729     8249   8486   8825    566   -633   -785       N  
-ATOM    471  CA  ILE A 729     -17.279  -6.278   1.678  1.00 65.61           C  
-ANISOU  471  CA  ILE A 729     8044   8276   8609    520   -573   -755       C  
-ATOM    472  C   ILE A 729     -17.411  -7.466   0.739  1.00 64.55           C  
-ANISOU  472  C   ILE A 729     7918   8128   8481    521   -559   -744       C  
-ATOM    473  O   ILE A 729     -18.503  -7.729   0.255  1.00 66.10           O  
-ANISOU  473  O   ILE A 729     8146   8316   8654    498   -527   -704       O  
-ATOM    474  CB  ILE A 729     -17.042  -4.897   0.956  1.00 68.13           C  
-ANISOU  474  CB  ILE A 729     8313   8613   8961    480   -534   -776       C  
-ATOM    475  CG1 ILE A 729     -16.923  -5.018  -0.561  1.00 67.70           C  
-ANISOU  475  CG1 ILE A 729     8228   8563   8933    452   -487   -780       C  
-ATOM    476  CG2 ILE A 729     -15.811  -4.173   1.485  1.00 70.26           C  
-ANISOU  476  CG2 ILE A 729     8534   8894   9268    494   -565   -827       C  
-ATOM    477  CD1 ILE A 729     -16.789  -3.661  -1.219  1.00 71.13           C  
-ANISOU  477  CD1 ILE A 729     8621   9012   9394    412   -446   -790       C  
-ATOM    478  N   LEU A 730     -16.321  -8.201   0.527  1.00 67.52           N  
-ANISOU  478  N   LEU A 730     8265   8500   8889    550   -585   -780       N  
-ATOM    479  CA  LEU A 730     -16.377  -9.467  -0.209  1.00 65.35           C  
-ANISOU  479  CA  LEU A 730     8001   8209   8621    561   -583   -775       C  
-ATOM    480  C   LEU A 730     -17.321 -10.449   0.469  1.00 61.92           C  
-ANISOU  480  C   LEU A 730     7633   7747   8147    578   -604   -727       C  
-ATOM    481  O   LEU A 730     -18.185 -10.993  -0.186  1.00 60.51           O  
-ANISOU  481  O   LEU A 730     7479   7555   7957    560   -577   -698       O  
-ATOM    482  CB  LEU A 730     -14.999 -10.106  -0.341  1.00 67.13           C  
-ANISOU  482  CB  LEU A 730     8186   8434   8887    598   -616   -825       C  
-ATOM    483  N   ASP A 731     -17.195 -10.633   1.784  1.00 59.96           N  
-ANISOU  483  N   ASP A 731     7414   7492   7877    610   -650   -718       N  
-ATOM    484  CA  ASP A 731     -18.079 -11.565   2.509  1.00 62.52           C  
-ANISOU  484  CA  ASP A 731     7803   7790   8162    625   -668   -668       C  
-ATOM    485  C   ASP A 731     -19.574 -11.167   2.425  1.00 64.67           C  
-ANISOU  485  C   ASP A 731     8112   8063   8398    586   -624   -616       C  
-ATOM    486  O   ASP A 731     -20.448 -12.036   2.302  1.00 56.90           O  
-ANISOU  486  O   ASP A 731     7167   7054   7399    580   -615   -576       O  
-ATOM    487  CB  ASP A 731     -17.639 -11.678   3.988  1.00 68.26           C  
-ANISOU  487  CB  ASP A 731     8554   8516   8865    669   -723   -667       C  
-ATOM    488  CG  ASP A 731     -18.806 -12.025   4.960  1.00 72.10           C  
-ANISOU  488  CG  ASP A 731     9110   8990   9297    672   -726   -605       C  
-ATOM    489  OD1 ASP A 731     -19.193 -13.203   5.140  1.00 71.43           O  
-ANISOU  489  OD1 ASP A 731     9066   8874   9199    687   -741   -570       O  
-ATOM    490  OD2 ASP A 731     -19.332 -11.080   5.582  1.00 80.70           O  
-ANISOU  490  OD2 ASP A 731    10211  10099  10354    658   -714   -591       O  
-ATOM    491  N   LEU A 732     -19.866  -9.861   2.505  1.00 60.26           N  
-ANISOU  491  N   LEU A 732     7538   7529   7830    559   -598   -619       N  
-ATOM    492  CA  LEU A 732     -21.250  -9.413   2.450  1.00 56.24           C  
-ANISOU  492  CA  LEU A 732     7059   7021   7289    524   -558   -575       C  
-ATOM    493  C   LEU A 732     -21.807  -9.647   1.061  1.00 50.63           C  
-ANISOU  493  C   LEU A 732     6338   6304   6595    490   -515   -566       C  
-ATOM    494  O   LEU A 732     -22.940 -10.106   0.915  1.00 48.12           O  
-ANISOU  494  O   LEU A 732     6055   5972   6258    473   -496   -525       O  
-ATOM    495  CB  LEU A 732     -21.386  -7.942   2.856  1.00 54.92           C  
-ANISOU  495  CB  LEU A 732     6876   6879   7111    506   -545   -584       C  
-ATOM    496  CG  LEU A 732     -21.107  -7.669   4.338  1.00 53.78           C  
-ANISOU  496  CG  LEU A 732     6751   6744   6938    539   -586   -587       C  
-ATOM    497  CD1 LEU A 732     -20.975  -6.168   4.570  1.00 55.38           C  
-ANISOU  497  CD1 LEU A 732     6927   6971   7146    523   -577   -612       C  
-ATOM    498  CD2 LEU A 732     -22.174  -8.265   5.238  1.00 52.63           C  
-ANISOU  498  CD2 LEU A 732     6668   6588   6741    549   -590   -533       C  
-ATOM    499  N   SER A 733     -21.004  -9.317   0.057  1.00 48.04           N  
-ANISOU  499  N   SER A 733     5961   5988   6304    481   -501   -606       N  
-ATOM    500  CA  SER A 733     -21.362  -9.569  -1.329  1.00 50.04           C  
-ANISOU  500  CA  SER A 733     6201   6239   6572    455   -463   -606       C  
-ATOM    501  C   SER A 733     -21.778 -11.037  -1.506  1.00 55.69           C  
-ANISOU  501  C   SER A 733     6950   6925   7285    470   -477   -586       C  
-ATOM    502  O   SER A 733     -22.815 -11.336  -2.099  1.00 54.98           O  
-ANISOU  502  O   SER A 733     6881   6824   7185    446   -451   -558       O  
-ATOM    503  CB  SER A 733     -20.191  -9.255  -2.246  1.00 47.44           C  
-ANISOU  503  CB  SER A 733     5815   5929   6283    454   -453   -655       C  
-ATOM    504  OG  SER A 733     -20.496  -8.208  -3.151  1.00 50.20           O  
-ANISOU  504  OG  SER A 733     6140   6298   6636    415   -405   -655       O  
-ATOM    505  N   ASN A 734     -20.965 -11.939  -0.974  1.00 58.02           N  
-ANISOU  505  N   ASN A 734     7248   7203   7592    509   -521   -602       N  
-ATOM    506  CA  ASN A 734     -21.217 -13.374  -1.088  1.00 56.52           C  
-ANISOU  506  CA  ASN A 734     7088   6979   7407    528   -541   -586       C  
-ATOM    507  C   ASN A 734     -22.428 -13.819  -0.308  1.00 52.33           C  
-ANISOU  507  C   ASN A 734     6614   6426   6844    521   -543   -528       C  
-ATOM    508  O   ASN A 734     -23.134 -14.710  -0.747  1.00 54.03           O  
-ANISOU  508  O   ASN A 734     6852   6613   7063    514   -537   -506       O  
-ATOM    509  CB  ASN A 734     -19.982 -14.180  -0.669  1.00 59.99           C  
-ANISOU  509  CB  ASN A 734     7516   7406   7870    575   -591   -619       C  
-ATOM    510  CG  ASN A 734     -18.809 -13.982  -1.627  1.00 62.02           C  
-ANISOU  510  CG  ASN A 734     7714   7684   8168    581   -585   -678       C  
-ATOM    511  OD1 ASN A 734     -18.991 -13.676  -2.805  1.00 61.66           O  
-ANISOU  511  OD1 ASN A 734     7643   7652   8132    554   -544   -690       O  
-ATOM    512  ND2 ASN A 734     -17.602 -14.148  -1.117  1.00 64.68           N  
-ANISOU  512  ND2 ASN A 734     8027   8023   8525    619   -625   -715       N  
-ATOM    513  N   ARG A 735     -22.674 -13.203   0.841  1.00 48.16           N  
-ANISOU  513  N   ARG A 735     6106   5908   6284    525   -552   -506       N  
-ATOM    514  CA  ARG A 735     -23.851 -13.551   1.613  1.00 44.81           C  
-ANISOU  514  CA  ARG A 735     5734   5466   5824    518   -548   -449       C  
-ATOM    515  C   ARG A 735     -25.094 -13.188   0.775  1.00 43.34           C  
-ANISOU  515  C   ARG A 735     5551   5284   5634    472   -498   -425       C  
-ATOM    516  O   ARG A 735     -26.085 -13.943   0.725  1.00 42.06           O  
-ANISOU  516  O   ARG A 735     5421   5096   5466    459   -489   -386       O  
-ATOM    517  CB  ARG A 735     -23.826 -12.861   2.996  1.00 47.31           C  
-ANISOU  517  CB  ARG A 735     6070   5802   6104    533   -565   -435       C  
-ATOM    518  N   PHE A 736     -25.032 -12.053   0.075  1.00 41.24           N  
-ANISOU  518  N   PHE A 736     5249   5047   5374    446   -467   -450       N  
-ATOM    519  CA  PHE A 736     -26.143 -11.633  -0.780  1.00 39.01           C  
-ANISOU  519  CA  PHE A 736     4966   4770   5087    406   -423   -431       C  
-ATOM    520  C   PHE A 736     -26.392 -12.642  -1.912  1.00 37.06           C  
-ANISOU  520  C   PHE A 736     4718   4500   4864    399   -416   -435       C  
-ATOM    521  O   PHE A 736     -27.505 -13.073  -2.133  1.00 34.10           O  
-ANISOU  521  O   PHE A 736     4367   4108   4483    379   -401   -403       O  
-ATOM    522  CB  PHE A 736     -25.900 -10.245  -1.374  1.00 37.14           C  
-ANISOU  522  CB  PHE A 736     4691   4566   4855    383   -395   -457       C  
-ATOM    523  CG  PHE A 736     -26.991  -9.797  -2.288  1.00 35.80           C  
-ANISOU  523  CG  PHE A 736     4520   4401   4680    345   -353   -440       C  
-ATOM    524  CD1 PHE A 736     -28.160  -9.263  -1.793  1.00 35.00           C  
-ANISOU  524  CD1 PHE A 736     4443   4304   4553    325   -334   -404       C  
-ATOM    525  CD2 PHE A 736     -26.859  -9.947  -3.654  1.00 36.66           C  
-ANISOU  525  CD2 PHE A 736     4606   4514   4810    332   -333   -461       C  
-ATOM    526  CE1 PHE A 736     -29.159  -8.833  -2.642  1.00 34.47           C  
-ANISOU  526  CE1 PHE A 736     4373   4241   4482    292   -299   -390       C  
-ATOM    527  CE2 PHE A 736     -27.873  -9.549  -4.507  1.00 37.51           C  
-ANISOU  527  CE2 PHE A 736     4715   4627   4911    300   -299   -445       C  
-ATOM    528  CZ  PHE A 736     -29.024  -8.987  -4.000  1.00 34.72           C  
-ANISOU  528  CZ  PHE A 736     4384   4275   4534    280   -283   -409       C  
-ATOM    529  N   TYR A 737     -25.327 -13.010  -2.606  1.00 37.65           N  
-ANISOU  529  N   TYR A 737     4762   4575   4967    416   -429   -477       N  
-ATOM    530  CA  TYR A 737     -25.404 -13.971  -3.713  1.00 39.90           C  
-ANISOU  530  CA  TYR A 737     5043   4842   5276    416   -426   -491       C  
-ATOM    531  C   TYR A 737     -25.842 -15.399  -3.289  1.00 41.84           C  
-ANISOU  531  C   TYR A 737     5327   5042   5528    432   -455   -464       C  
-ATOM    532  O   TYR A 737     -26.370 -16.153  -4.103  1.00 44.09           O  
-ANISOU  532  O   TYR A 737     5617   5306   5828    422   -449   -463       O  
-ATOM    533  CB  TYR A 737     -24.077 -14.010  -4.477  1.00 38.08           C  
-ANISOU  533  CB  TYR A 737     4768   4626   5073    435   -433   -546       C  
-ATOM    534  CG  TYR A 737     -23.777 -12.730  -5.253  1.00 38.23           C  
-ANISOU  534  CG  TYR A 737     4747   4685   5092    411   -396   -570       C  
-ATOM    535  CD1 TYR A 737     -24.689 -12.219  -6.146  1.00 39.66           C  
-ANISOU  535  CD1 TYR A 737     4928   4878   5262    377   -356   -556       C  
-ATOM    536  CD2 TYR A 737     -22.581 -12.038  -5.091  1.00 40.25           C  
-ANISOU  536  CD2 TYR A 737     4965   4966   5362    423   -401   -604       C  
-ATOM    537  CE1 TYR A 737     -24.414 -11.061  -6.855  1.00 40.60           C  
-ANISOU  537  CE1 TYR A 737     5014   5031   5381    356   -323   -572       C  
-ATOM    538  CE2 TYR A 737     -22.287 -10.871  -5.801  1.00 41.38           C  
-ANISOU  538  CE2 TYR A 737     5071   5142   5509    400   -365   -622       C  
-ATOM    539  CZ  TYR A 737     -23.217 -10.383  -6.683  1.00 41.08           C  
-ANISOU  539  CZ  TYR A 737     5037   5113   5456    366   -325   -604       C  
-ATOM    540  OH  TYR A 737     -22.963  -9.237  -7.430  1.00 40.71           O  
-ANISOU  540  OH  TYR A 737     4958   5098   5414    342   -288   -616       O  
-ATOM    541  N   THR A 738     -25.652 -15.730  -2.017  1.00 41.88           N  
-ANISOU  541  N   THR A 738     5359   5032   5521    455   -485   -442       N  
-ATOM    542  CA  THR A 738     -26.117 -16.986  -1.466  1.00 41.85           C  
-ANISOU  542  CA  THR A 738     5396   4984   5521    468   -510   -406       C  
-ATOM    543  C   THR A 738     -27.602 -16.934  -1.263  1.00 43.52           C  
-ANISOU  543  C   THR A 738     5638   5185   5713    434   -482   -355       C  
-ATOM    544  O   THR A 738     -28.304 -17.896  -1.547  1.00 47.78           O  
-ANISOU  544  O   THR A 738     6197   5689   6269    426   -484   -333       O  
-ATOM    545  CB  THR A 738     -25.419 -17.276  -0.123  1.00 43.85           C  
-ANISOU  545  CB  THR A 738     5671   5229   5762    506   -551   -395       C  
-ATOM    546  OG1 THR A 738     -24.027 -17.501  -0.360  1.00 42.53           O  
-ANISOU  546  OG1 THR A 738     5473   5066   5620    541   -582   -446       O  
-ATOM    547  CG2 THR A 738     -26.025 -18.505   0.563  1.00 44.83           C  
-ANISOU  547  CG2 THR A 738     5844   5306   5885    516   -573   -346       C  
-ATOM    548  N   LEU A 739     -28.097 -15.790  -0.801  1.00 45.51           N  
-ANISOU  548  N   LEU A 739     5890   5468   5933    415   -457   -338       N  
-ATOM    549  CA  LEU A 739     -29.531 -15.611  -0.615  1.00 44.78           C  
-ANISOU  549  CA  LEU A 739     5821   5372   5822    382   -427   -292       C  
-ATOM    550  C   LEU A 739     -30.274 -15.477  -1.937  1.00 41.82           C  
-ANISOU  550  C   LEU A 739     5426   4998   5463    349   -396   -302       C  
-ATOM    551  O   LEU A 739     -31.384 -15.977  -2.097  1.00 41.08           O  
-ANISOU  551  O   LEU A 739     5350   4882   5375    327   -383   -271       O  
-ATOM    552  CB  LEU A 739     -29.786 -14.357   0.191  1.00 50.92           C  
-ANISOU  552  CB  LEU A 739     6599   6185   6562    374   -409   -278       C  
-ATOM    553  CG  LEU A 739     -30.769 -14.454   1.329  1.00 58.65           C  
-ANISOU  553  CG  LEU A 739     7617   7158   7509    368   -401   -224       C  
-ATOM    554  CD1 LEU A 739     -30.447 -15.558   2.323  1.00 63.29           C  
-ANISOU  554  CD1 LEU A 739     8241   7715   8092    399   -436   -196       C  
-ATOM    555  CD2 LEU A 739     -30.794 -13.107   2.028  1.00 58.59           C  
-ANISOU  555  CD2 LEU A 739     7604   7191   7468    367   -388   -226       C  
-ATOM    556  N   ILE A 740     -29.671 -14.769  -2.881  1.00 39.36           N  
-ANISOU  556  N   ILE A 740     5079   4716   5162    345   -384   -345       N  
-ATOM    557  CA  ILE A 740     -30.277 -14.551  -4.195  1.00 38.53           C  
-ANISOU  557  CA  ILE A 740     4955   4618   5067    318   -356   -358       C  
-ATOM    558  C   ILE A 740     -29.311 -15.086  -5.225  1.00 35.82           C  
-ANISOU  558  C   ILE A 740     4587   4273   4751    335   -369   -406       C  
-ATOM    559  O   ILE A 740     -28.388 -14.389  -5.657  1.00 31.52           O  
-ANISOU  559  O   ILE A 740     4011   3759   4208    342   -362   -442       O  
-ATOM    560  CB  ILE A 740     -30.557 -13.085  -4.464  1.00 38.67           C  
-ANISOU  560  CB  ILE A 740     4953   4675   5064    294   -323   -362       C  
-ATOM    561  CG1 ILE A 740     -31.269 -12.473  -3.269  1.00 39.18           C  
-ANISOU  561  CG1 ILE A 740     5040   4746   5100    285   -314   -323       C  
-ATOM    562  CG2 ILE A 740     -31.383 -12.931  -5.752  1.00 41.65           C  
-ANISOU  562  CG2 ILE A 740     5320   5057   5448    267   -296   -367       C  
-ATOM    563  CD1 ILE A 740     -32.694 -12.936  -3.092  1.00 38.46           C  
-ANISOU  563  CD1 ILE A 740     4975   4634   5004    263   -301   -280       C  
-ATOM    564  N   PRO A 741     -29.515 -16.345  -5.599  1.00 36.17           N  
-ANISOU  564  N   PRO A 741     4644   4281   4819    343   -387   -407       N  
-ATOM    565  CA  PRO A 741     -28.539 -16.988  -6.475  1.00 35.14           C  
-ANISOU  565  CA  PRO A 741     4491   4146   4714    367   -404   -455       C  
-ATOM    566  C   PRO A 741     -28.502 -16.346  -7.836  1.00 31.76           C  
-ANISOU  566  C   PRO A 741     4032   3752   4285    351   -374   -489       C  
-ATOM    567  O   PRO A 741     -29.550 -16.111  -8.475  1.00 30.02           O  
-ANISOU  567  O   PRO A 741     3815   3534   4056    324   -351   -476       O  
-ATOM    568  CB  PRO A 741     -29.005 -18.449  -6.563  1.00 37.07           C  
-ANISOU  568  CB  PRO A 741     4759   4339   4986    374   -429   -445       C  
-ATOM    569  CG  PRO A 741     -30.177 -18.597  -5.652  1.00 38.15           C  
-ANISOU  569  CG  PRO A 741     4931   4452   5111    354   -425   -387       C  
-ATOM    570  CD  PRO A 741     -30.585 -17.257  -5.142  1.00 37.63           C  
-ANISOU  570  CD  PRO A 741     4864   4424   5011    333   -395   -364       C  
-ATOM    571  N   HIS A 742     -27.281 -16.068  -8.254  1.00 32.53           N  
-ANISOU  571  N   HIS A 742     4096   3873   4389    371   -375   -531       N  
-ATOM    572  CA  HIS A 742     -26.992 -15.506  -9.535  1.00 35.72           C  
-ANISOU  572  CA  HIS A 742     4470   4313   4791    362   -347   -565       C  
-ATOM    573  C   HIS A 742     -26.252 -16.522 -10.362  1.00 36.18           C  
-ANISOU  573  C   HIS A 742     4513   4362   4874    390   -364   -611       C  
-ATOM    574  O   HIS A 742     -25.715 -17.486  -9.841  1.00 36.22           O  
-ANISOU  574  O   HIS A 742     4525   4337   4900    418   -400   -620       O  
-ATOM    575  CB  HIS A 742     -26.163 -14.216  -9.363  1.00 35.82           C  
-ANISOU  575  CB  HIS A 742     4452   4366   4792    358   -327   -577       C  
-ATOM    576  CG  HIS A 742     -26.985 -13.036  -8.971  1.00 36.02           C  
-ANISOU  576  CG  HIS A 742     4487   4407   4793    327   -301   -541       C  
-ATOM    577  ND1 HIS A 742     -27.668 -12.973  -7.778  1.00 35.45           N  
-ANISOU  577  ND1 HIS A 742     4443   4317   4707    322   -312   -501       N  
-ATOM    578  CD2 HIS A 742     -27.262 -11.882  -9.623  1.00 36.02           C  
-ANISOU  578  CD2 HIS A 742     4471   4439   4777    302   -265   -539       C  
-ATOM    579  CE1 HIS A 742     -28.293 -11.814  -7.688  1.00 34.02           C  
-ANISOU  579  CE1 HIS A 742     4263   4157   4507    295   -285   -480       C  
-ATOM    580  NE2 HIS A 742     -28.069 -11.135  -8.796  1.00 34.74           N  
-ANISOU  580  NE2 HIS A 742     4327   4275   4597    282   -257   -502       N  
-ATOM    581  N   ASP A 743     -26.161 -16.245 -11.651  1.00 39.99           N  
-ANISOU  581  N   ASP A 743     4971   4873   5350    383   -338   -640       N  
-ATOM    582  CA  ASP A 743     -25.546 -17.127 -12.620  1.00 41.74           C  
-ANISOU  582  CA  ASP A 743     5176   5093   5590    409   -349   -688       C  
-ATOM    583  C   ASP A 743     -24.588 -16.261 -13.423  1.00 43.20           C  
-ANISOU  583  C   ASP A 743     5319   5329   5765    410   -316   -722       C  
-ATOM    584  O   ASP A 743     -24.929 -15.687 -14.453  1.00 45.49           O  
-ANISOU  584  O   ASP A 743     5600   5651   6035    393   -282   -728       O  
-ATOM    585  CB  ASP A 743     -26.573 -17.764 -13.547  1.00 46.24           C  
-ANISOU  585  CB  ASP A 743     5763   5648   6159    399   -347   -691       C  
-ATOM    586  CG  ASP A 743     -25.916 -18.666 -14.611  1.00 49.00           C  
-ANISOU  586  CG  ASP A 743     6093   5999   6525    429   -359   -747       C  
-ATOM    587  OD1 ASP A 743     -26.573 -19.069 -15.589  1.00 54.62           O  
-ANISOU  587  OD1 ASP A 743     6812   6710   7233    424   -355   -762       O  
-ATOM    588  OD2 ASP A 743     -24.715 -18.922 -14.484  1.00 48.13           O  
-ANISOU  588  OD2 ASP A 743     5960   5895   6430    458   -371   -780       O  
-ATOM    589  N   PHE A 744     -23.378 -16.147 -12.924  1.00 49.93           N  
-ANISOU  589  N   PHE A 744     6147   6191   6633    432   -326   -744       N  
-ATOM    590  CA  PHE A 744     -22.378 -15.330 -13.584  1.00 55.89           C  
-ANISOU  590  CA  PHE A 744     6857   6993   7385    432   -295   -775       C  
-ATOM    591  C   PHE A 744     -21.503 -16.153 -14.532  1.00 59.00           C  
-ANISOU  591  C   PHE A 744     7224   7398   7795    464   -298   -831       C  
-ATOM    592  O   PHE A 744     -21.842 -16.293 -15.704  1.00 61.50           O  
-ANISOU  592  O   PHE A 744     7538   7732   8097    460   -277   -848       O  
-ATOM    593  CB  PHE A 744     -21.530 -14.635 -12.539  1.00 53.14           C  
-ANISOU  593  CB  PHE A 744     6490   6653   7047    436   -302   -772       C  
-ATOM    594  CG  PHE A 744     -22.317 -13.705 -11.667  1.00 53.85           C  
-ANISOU  594  CG  PHE A 744     6603   6739   7118    407   -295   -723       C  
-ATOM    595  CD1 PHE A 744     -22.929 -12.585 -12.211  1.00 51.85           C  
-ANISOU  595  CD1 PHE A 744     6348   6513   6842    372   -253   -702       C  
-ATOM    596  CD2 PHE A 744     -22.451 -13.947 -10.310  1.00 51.08           C  
-ANISOU  596  CD2 PHE A 744     6277   6359   6771    416   -329   -698       C  
-ATOM    597  CE1 PHE A 744     -23.640 -11.723 -11.407  1.00 51.36           C  
-ANISOU  597  CE1 PHE A 744     6303   6446   6763    348   -248   -661       C  
-ATOM    598  CE2 PHE A 744     -23.148 -13.068  -9.500  1.00 49.76           C  
-ANISOU  598  CE2 PHE A 744     6129   6192   6584    392   -321   -658       C  
-ATOM    599  CZ  PHE A 744     -23.764 -11.972 -10.054  1.00 49.00           C  
-ANISOU  599  CZ  PHE A 744     6029   6121   6469    358   -281   -641       C  
-ATOM    600  N   LYS A 748     -17.279 -14.609 -13.103  1.00 62.36           N  
-ANISOU  600  N   LYS A 748     7513   7890   8290    508   -300   -912       N  
-ATOM    601  CA  LYS A 748     -16.728 -14.055 -11.847  1.00 67.61           C  
-ANISOU  601  CA  LYS A 748     8169   8549   8972    511   -324   -904       C  
-ATOM    602  C   LYS A 748     -17.712 -13.052 -11.186  1.00 67.02           C  
-ANISOU  602  C   LYS A 748     8124   8469   8870    474   -312   -850       C  
-ATOM    603  O   LYS A 748     -18.173 -12.116 -11.855  1.00 59.86           O  
-ANISOU  603  O   LYS A 748     7213   7588   7945    440   -267   -833       O  
-ATOM    604  CB  LYS A 748     -15.359 -13.386 -12.089  1.00 69.42           C  
-ANISOU  604  CB  LYS A 748     8334   8815   9227    516   -304   -944       C  
-ATOM    605  N   PRO A 749     -18.043 -13.244  -9.881  1.00 68.91           N  
-ANISOU  605  N   PRO A 749     8397   8677   9107    482   -352   -824       N  
-ATOM    606  CA  PRO A 749     -19.161 -12.476  -9.294  1.00 67.32           C  
-ANISOU  606  CA  PRO A 749     8232   8470   8878    451   -341   -773       C  
-ATOM    607  C   PRO A 749     -18.810 -11.021  -8.954  1.00 62.52           C  
-ANISOU  607  C   PRO A 749     7596   7888   8270    428   -319   -769       C  
-ATOM    608  O   PRO A 749     -17.930 -10.794  -8.131  1.00 61.08           O  
-ANISOU  608  O   PRO A 749     7392   7707   8107    445   -345   -787       O  
-ATOM    609  CB  PRO A 749     -19.535 -13.283  -8.033  1.00 69.71           C  
-ANISOU  609  CB  PRO A 749     8577   8733   9177    473   -391   -748       C  
-ATOM    610  CG  PRO A 749     -18.333 -14.109  -7.691  1.00 71.00           C  
-ANISOU  610  CG  PRO A 749     8720   8886   9371    516   -431   -788       C  
-ATOM    611  CD  PRO A 749     -17.408 -14.135  -8.889  1.00 70.24           C  
-ANISOU  611  CD  PRO A 749     8572   8818   9297    523   -407   -838       C  
-ATOM    612  N   PRO A 750     -19.500 -10.041  -9.587  1.00 59.88           N  
-ANISOU  612  N   PRO A 750     7262   7572   7917    390   -275   -746       N  
-ATOM    613  CA  PRO A 750     -19.201  -8.623  -9.344  1.00 58.86           C  
-ANISOU  613  CA  PRO A 750     7107   7464   7792    365   -253   -742       C  
-ATOM    614  C   PRO A 750     -19.298  -8.248  -7.879  1.00 55.72           C  
-ANISOU  614  C   PRO A 750     6727   7051   7393    371   -287   -726       C  
-ATOM    615  O   PRO A 750     -20.301  -8.558  -7.230  1.00 61.39           O  
-ANISOU  615  O   PRO A 750     7491   7747   8086    371   -303   -692       O  
-ATOM    616  CB  PRO A 750     -20.284  -7.858 -10.122  1.00 59.65           C  
-ANISOU  616  CB  PRO A 750     7224   7576   7866    327   -210   -708       C  
-ATOM    617  CG  PRO A 750     -21.075  -8.856 -10.881  1.00 57.73           C  
-ANISOU  617  CG  PRO A 750     7010   7322   7605    332   -207   -700       C  
-ATOM    618  CD  PRO A 750     -20.644 -10.238 -10.499  1.00 58.30           C  
-ANISOU  618  CD  PRO A 750     7090   7371   7691    370   -249   -722       C  
-ATOM    619  N   LEU A 751     -18.285  -7.543  -7.390  1.00 57.94           N  
-ANISOU  619  N   LEU A 751     6970   7344   7699    376   -295   -752       N  
-ATOM    620  CA  LEU A 751     -18.275  -7.061  -6.018  1.00 57.36           C  
-ANISOU  620  CA  LEU A 751     6909   7261   7623    383   -328   -744       C  
-ATOM    621  C   LEU A 751     -19.283  -5.947  -5.832  1.00 55.90           C  
-ANISOU  621  C   LEU A 751     6745   7080   7416    349   -304   -708       C  
-ATOM    622  O   LEU A 751     -19.373  -5.027  -6.651  1.00 51.60           O  
-ANISOU  622  O   LEU A 751     6179   6551   6877    317   -262   -704       O  
-ATOM    623  CB  LEU A 751     -16.875  -6.565  -5.591  1.00 59.70           C  
-ANISOU  623  CB  LEU A 751     7154   7570   7958    397   -346   -787       C  
-ATOM    624  N   LEU A 752     -20.067  -6.049  -4.762  1.00 56.41           N  
-ANISOU  624  N   LEU A 752     6852   7127   7453    356   -329   -679       N  
-ATOM    625  CA  LEU A 752     -21.024  -5.003  -4.433  1.00 56.19           C  
-ANISOU  625  CA  LEU A 752     6844   7102   7404    329   -310   -649       C  
-ATOM    626  C   LEU A 752     -20.320  -3.924  -3.639  1.00 60.10           C  
-ANISOU  626  C   LEU A 752     7312   7606   7918    329   -325   -670       C  
-ATOM    627  O   LEU A 752     -20.347  -3.957  -2.405  1.00 64.47           O  
-ANISOU  627  O   LEU A 752     7885   8152   8457    351   -361   -669       O  
-ATOM    628  CB  LEU A 752     -22.243  -5.599  -3.703  1.00 54.79           C  
-ANISOU  628  CB  LEU A 752     6723   6907   7188    335   -325   -608       C  
-ATOM    629  CG  LEU A 752     -23.015  -6.568  -4.598  1.00 55.32           C  
-ANISOU  629  CG  LEU A 752     6813   6962   7244    328   -308   -588       C  
-ATOM    630  CD1 LEU A 752     -24.119  -7.273  -3.830  1.00 55.11           C  
-ANISOU  630  CD1 LEU A 752     6838   6914   7187    334   -324   -549       C  
-ATOM    631  CD2 LEU A 752     -23.585  -5.827  -5.814  1.00 56.91           C  
-ANISOU  631  CD2 LEU A 752     7002   7177   7442    292   -261   -578       C  
-ATOM    632  N   ASN A 753     -19.702  -2.975  -4.358  1.00 56.09           N  
-ANISOU  632  N   ASN A 753     6759   7114   7441    306   -296   -690       N  
-ATOM    633  CA  ASN A 753     -18.719  -2.091  -3.755  1.00 55.66           C  
-ANISOU  633  CA  ASN A 753     6665   7065   7419    309   -313   -723       C  
-ATOM    634  C   ASN A 753     -18.919  -0.598  -4.034  1.00 53.99           C  
-ANISOU  634  C   ASN A 753     6432   6859   7222    272   -281   -716       C  
-ATOM    635  O   ASN A 753     -18.029   0.194  -3.771  1.00 51.98           O  
-ANISOU  635  O   ASN A 753     6137   6609   7005    268   -288   -746       O  
-ATOM    636  CB  ASN A 753     -17.321  -2.526  -4.174  1.00 57.41           C  
-ANISOU  636  CB  ASN A 753     6837   7296   7682    325   -320   -766       C  
-ATOM    637  CG  ASN A 753     -16.978  -2.138  -5.610  1.00 62.11           C  
-ANISOU  637  CG  ASN A 753     7393   7908   8300    296   -268   -772       C  
-ATOM    638  OD1 ASN A 753     -17.846  -1.854  -6.439  1.00 62.90           O  
-ANISOU  638  OD1 ASN A 753     7510   8010   8378    268   -228   -740       O  
-ATOM    639  ND2 ASN A 753     -15.693  -2.124  -5.898  1.00 63.48           N  
-ANISOU  639  ND2 ASN A 753     7512   8093   8516    303   -268   -812       N  
-ATOM    640  N   ASN A 754     -20.092  -0.225  -4.535  1.00 51.97           N  
-ANISOU  640  N   ASN A 754     6206   6602   6940    245   -248   -678       N  
-ATOM    641  CA  ASN A 754     -20.428   1.172  -4.755  1.00 52.32           C  
-ANISOU  641  CA  ASN A 754     6237   6646   6994    212   -221   -666       C  
-ATOM    642  C   ASN A 754     -21.930   1.362  -4.653  1.00 55.62           C  
-ANISOU  642  C   ASN A 754     6704   7057   7372    199   -209   -624       C  
-ATOM    643  O   ASN A 754     -22.700   0.391  -4.685  1.00 55.11           O  
-ANISOU  643  O   ASN A 754     6677   6989   7274    210   -213   -602       O  
-ATOM    644  CB  ASN A 754     -19.893   1.677  -6.090  1.00 56.46           C  
-ANISOU  644  CB  ASN A 754     6723   7183   7549    183   -176   -670       C  
-ATOM    645  CG  ASN A 754     -20.539   0.996  -7.280  1.00 60.36           C  
-ANISOU  645  CG  ASN A 754     7236   7683   8014    175   -142   -644       C  
-ATOM    646  OD1 ASN A 754     -21.611   1.395  -7.734  1.00 55.29           O  
-ANISOU  646  OD1 ASN A 754     6621   7039   7348    154   -118   -610       O  
-ATOM    647  ND2 ASN A 754     -19.891  -0.063  -7.777  1.00 61.52           N  
-ANISOU  647  ND2 ASN A 754     7370   7839   8167    194   -144   -664       N  
-ATOM    648  N   ALA A 755     -22.339   2.609  -4.478  1.00 56.28           N  
-ANISOU  648  N   ALA A 755     6784   7137   7461    177   -198   -615       N  
-ATOM    649  CA  ALA A 755     -23.733   2.938  -4.225  1.00 59.12           C  
-ANISOU  649  CA  ALA A 755     7185   7490   7786    168   -190   -581       C  
-ATOM    650  C   ALA A 755     -24.619   2.550  -5.400  1.00 58.78           C  
-ANISOU  650  C   ALA A 755     7162   7451   7722    150   -155   -548       C  
-ATOM    651  O   ALA A 755     -25.708   2.009  -5.222  1.00 61.51           O  
-ANISOU  651  O   ALA A 755     7546   7792   8033    155   -157   -522       O  
-ATOM    652  CB  ALA A 755     -23.873   4.421  -3.908  1.00 59.54           C  
-ANISOU  652  CB  ALA A 755     7225   7537   7859    149   -185   -583       C  
-ATOM    653  N   ASP A 756     -24.166   2.817  -6.614  1.00 63.62           N  
-ANISOU  653  N   ASP A 756     7747   8071   8354    130   -122   -549       N  
-ATOM    654  CA  ASP A 756     -24.984   2.464  -7.768  1.00 62.97           C  
-ANISOU  654  CA  ASP A 756     7684   7993   8248    117    -91   -521       C  
-ATOM    655  C   ASP A 756     -25.215   0.960  -7.918  1.00 58.81           C  
-ANISOU  655  C   ASP A 756     7180   7467   7698    138   -103   -520       C  
-ATOM    656  O   ASP A 756     -26.289   0.558  -8.298  1.00 62.20           O  
-ANISOU  656  O   ASP A 756     7640   7894   8100    133    -95   -495       O  
-ATOM    657  CB  ASP A 756     -24.447   2.999  -9.065  1.00 65.71           C  
-ANISOU  657  CB  ASP A 756     8001   8352   8614     94    -52   -520       C  
-ATOM    658  CG  ASP A 756     -25.556   3.137 -10.111  1.00 70.76           C  
-ANISOU  658  CG  ASP A 756     8665   8995   9225     76    -21   -486       C  
-ATOM    659  OD1 ASP A 756     -25.690   2.265 -11.023  1.00 66.95           O  
-ANISOU  659  OD1 ASP A 756     8191   8524   8724     81     -9   -483       O  
-ATOM    660  OD2 ASP A 756     -26.346   4.094  -9.952  1.00 68.55           O  
-ANISOU  660  OD2 ASP A 756     8399   8707   8941     60    -15   -464       O  
-ATOM    661  N   SER A 757     -24.201   0.144  -7.675  1.00 53.35           N  
-ANISOU  661  N   SER A 757     6472   6778   7021    161   -124   -549       N  
-ATOM    662  CA  SER A 757     -24.368  -1.312  -7.681  1.00 50.45           C  
-ANISOU  662  CA  SER A 757     6126   6406   6637    185   -142   -550       C  
-ATOM    663  C   SER A 757     -25.385  -1.794  -6.658  1.00 46.99           C  
-ANISOU  663  C   SER A 757     5732   5952   6170    196   -167   -527       C  
-ATOM    664  O   SER A 757     -26.119  -2.744  -6.907  1.00 46.57           O  
-ANISOU  664  O   SER A 757     5707   5891   6098    201   -169   -510       O  
-ATOM    665  CB  SER A 757     -23.058  -2.020  -7.398  1.00 51.05           C  
-ANISOU  665  CB  SER A 757     6176   6483   6736    212   -167   -587       C  
-ATOM    666  OG  SER A 757     -22.157  -1.681  -8.410  1.00 57.35           O  
-ANISOU  666  OG  SER A 757     6932   7298   7560    201   -139   -608       O  
-ATOM    667  N   VAL A 758     -25.346  -1.194  -5.483  1.00 42.13           N  
-ANISOU  667  N   VAL A 758     5121   5333   5555    202   -188   -528       N  
-ATOM    668  CA  VAL A 758     -26.230  -1.585  -4.422  1.00 41.54           C  
-ANISOU  668  CA  VAL A 758     5085   5247   5452    215   -209   -506       C  
-ATOM    669  C   VAL A 758     -27.650  -1.222  -4.828  1.00 42.08           C  
-ANISOU  669  C   VAL A 758     5177   5313   5497    191   -183   -471       C  
-ATOM    670  O   VAL A 758     -28.570  -2.040  -4.756  1.00 39.03           O  
-ANISOU  670  O   VAL A 758     4822   4918   5089    193   -185   -447       O  
-ATOM    671  CB  VAL A 758     -25.862  -0.880  -3.115  1.00 40.53           C  
-ANISOU  671  CB  VAL A 758     4954   5120   5324    228   -235   -520       C  
-ATOM    672  CG1 VAL A 758     -26.979  -1.049  -2.100  1.00 42.33           C  
-ANISOU  672  CG1 VAL A 758     5224   5342   5516    236   -246   -491       C  
-ATOM    673  CG2 VAL A 758     -24.574  -1.464  -2.597  1.00 42.11           C  
-ANISOU  673  CG2 VAL A 758     5136   5321   5543    258   -270   -553       C  
-ATOM    674  N   GLN A 759     -27.786   0.011  -5.297  1.00 41.06           N  
-ANISOU  674  N   GLN A 759     5031   5191   5378    167   -159   -470       N  
-ATOM    675  CA  GLN A 759     -29.042   0.551  -5.766  1.00 44.02           C  
-ANISOU  675  CA  GLN A 759     5424   5566   5737    145   -134   -440       C  
-ATOM    676  C   GLN A 759     -29.668  -0.363  -6.861  1.00 38.95           C  
-ANISOU  676  C   GLN A 759     4795   4922   5082    138   -118   -425       C  
-ATOM    677  O   GLN A 759     -30.855  -0.652  -6.831  1.00 40.08           O  
-ANISOU  677  O   GLN A 759     4964   5059   5205    133   -115   -400       O  
-ATOM    678  CB  GLN A 759     -28.790   1.968  -6.275  1.00 47.64           C  
-ANISOU  678  CB  GLN A 759     5856   6029   6215    122   -112   -445       C  
-ATOM    679  CG  GLN A 759     -29.836   3.046  -6.077  1.00 52.46           C  
-ANISOU  679  CG  GLN A 759     6480   6637   6818    106   -101   -424       C  
-ATOM    680  CD  GLN A 759     -29.181   4.447  -6.211  1.00 62.98           C  
-ANISOU  680  CD  GLN A 759     7782   7969   8181     90    -91   -437       C  
-ATOM    681  OE1 GLN A 759     -28.238   4.753  -5.461  1.00 69.03           O  
-ANISOU  681  OE1 GLN A 759     8527   8733   8968    100   -111   -464       O  
-ATOM    682  NE2 GLN A 759     -29.652   5.286  -7.158  1.00 61.24           N  
-ANISOU  682  NE2 GLN A 759     7556   7746   7965     66    -63   -419       N  
-ATOM    683  N   ALA A 760     -28.871  -0.798  -7.816  1.00 34.99           N  
-ANISOU  683  N   ALA A 760     4273   4427   4594    140   -110   -442       N  
-ATOM    684  CA  ALA A 760     -29.341  -1.672  -8.862  1.00 37.89           C  
-ANISOU  684  CA  ALA A 760     4651   4795   4950    138    -99   -435       C  
-ATOM    685  C   ALA A 760     -29.899  -2.980  -8.264  1.00 38.15           C  
-ANISOU  685  C   ALA A 760     4713   4811   4971    155   -123   -426       C  
-ATOM    686  O   ALA A 760     -30.872  -3.504  -8.793  1.00 38.23           O  
-ANISOU  686  O   ALA A 760     4742   4815   4968    148   -117   -409       O  
-ATOM    687  CB  ALA A 760     -28.226  -1.982  -9.857  1.00 39.18           C  
-ANISOU  687  CB  ALA A 760     4786   4972   5130    143    -88   -461       C  
-ATOM    688  N   LYS A 761     -29.251  -3.509  -7.213  1.00 35.10           N  
-ANISOU  688  N   LYS A 761     4330   4416   4591    177   -152   -437       N  
-ATOM    689  CA  LYS A 761     -29.709  -4.737  -6.559  1.00 34.30           C  
-ANISOU  689  CA  LYS A 761     4257   4295   4479    194   -176   -424       C  
-ATOM    690  C   LYS A 761     -30.976  -4.523  -5.774  1.00 32.49           C  
-ANISOU  690  C   LYS A 761     4057   4059   4228    185   -174   -391       C  
-ATOM    691  O   LYS A 761     -31.849  -5.393  -5.776  1.00 29.65           O  
-ANISOU  691  O   LYS A 761     3720   3684   3860    183   -177   -370       O  
-ATOM    692  CB  LYS A 761     -28.630  -5.414  -5.697  1.00 35.73           C  
-ANISOU  692  CB  LYS A 761     4435   4470   4671    224   -209   -444       C  
-ATOM    693  CG  LYS A 761     -27.447  -5.925  -6.495  1.00 36.76           C  
-ANISOU  693  CG  LYS A 761     4537   4605   4824    237   -212   -479       C  
-ATOM    694  CD  LYS A 761     -27.868  -6.983  -7.493  1.00 41.33           C  
-ANISOU  694  CD  LYS A 761     5126   5173   5403    237   -207   -478       C  
-ATOM    695  CE  LYS A 761     -26.739  -7.510  -8.354  1.00 43.34           C  
-ANISOU  695  CE  LYS A 761     5353   5437   5679    252   -208   -515       C  
-ATOM    696  NZ  LYS A 761     -27.266  -7.760  -9.723  1.00 47.04           N  
-ANISOU  696  NZ  LYS A 761     5821   5912   6142    239   -184   -516       N  
-ATOM    697  N   VAL A 762     -31.116  -3.357  -5.157  1.00 32.69           N  
-ANISOU  697  N   VAL A 762     4079   4095   4248    177   -168   -387       N  
-ATOM    698  CA  VAL A 762     -32.353  -3.026  -4.461  1.00 33.02           C  
-ANISOU  698  CA  VAL A 762     4144   4134   4268    168   -162   -358       C  
-ATOM    699  C   VAL A 762     -33.514  -2.962  -5.446  1.00 32.49           C  
-ANISOU  699  C   VAL A 762     4081   4065   4196    145   -138   -339       C  
-ATOM    700  O   VAL A 762     -34.600  -3.513  -5.217  1.00 33.01           O  
-ANISOU  700  O   VAL A 762     4170   4122   4252    140   -136   -314       O  
-ATOM    701  CB  VAL A 762     -32.257  -1.670  -3.733  1.00 36.38           C  
-ANISOU  701  CB  VAL A 762     4560   4572   4690    166   -160   -363       C  
-ATOM    702  CG1 VAL A 762     -33.609  -1.262  -3.155  1.00 36.62           C  
-ANISOU  702  CG1 VAL A 762     4612   4604   4699    157   -149   -336       C  
-ATOM    703  CG2 VAL A 762     -31.228  -1.737  -2.628  1.00 37.90           C  
-ANISOU  703  CG2 VAL A 762     4750   4766   4883    192   -189   -383       C  
-ATOM    704  N   GLU A 763     -33.276  -2.283  -6.552  1.00 36.78           N  
-ANISOU  704  N   GLU A 763     4605   4620   4751    131   -119   -350       N  
-ATOM    705  CA  GLU A 763     -34.301  -2.151  -7.595  1.00 41.51           C  
-ANISOU  705  CA  GLU A 763     5208   5220   5345    112    -99   -335       C  
-ATOM    706  C   GLU A 763     -34.610  -3.525  -8.169  1.00 36.17           C  
-ANISOU  706  C   GLU A 763     4542   4531   4668    116   -106   -333       C  
-ATOM    707  O   GLU A 763     -35.776  -3.841  -8.342  1.00 31.29           O  
-ANISOU  707  O   GLU A 763     3939   3905   4044    106   -102   -314       O  
-ATOM    708  CB  GLU A 763     -33.982  -1.069  -8.634  1.00 46.33           C  
-ANISOU  708  CB  GLU A 763     5797   5845   5961     97    -77   -343       C  
-ATOM    709  CG  GLU A 763     -34.251   0.307  -8.029  1.00 52.64           C  
-ANISOU  709  CG  GLU A 763     6592   6648   6760     88    -70   -336       C  
-ATOM    710  CD  GLU A 763     -33.870   1.454  -8.941  1.00 58.17           C  
-ANISOU  710  CD  GLU A 763     7272   7358   7472     72    -50   -340       C  
-ATOM    711  OE1 GLU A 763     -33.981   1.281 -10.173  1.00 60.27           O  
-ANISOU  711  OE1 GLU A 763     7536   7630   7734     65    -35   -337       O  
-ATOM    712  OE2 GLU A 763     -33.465   2.517  -8.409  1.00 57.94           O  
-ANISOU  712  OE2 GLU A 763     7231   7329   7454     69    -49   -345       O  
-ATOM    713  N   MET A 764     -33.586  -4.353  -8.360  1.00 32.05           N  
-ANISOU  713  N   MET A 764     4014   4006   4158    132   -120   -355       N  
-ATOM    714  CA  MET A 764     -33.804  -5.725  -8.719  1.00 33.90           C  
-ANISOU  714  CA  MET A 764     4260   4224   4398    140   -132   -356       C  
-ATOM    715  C   MET A 764     -34.729  -6.432  -7.736  1.00 30.33           C  
-ANISOU  715  C   MET A 764     3834   3749   3940    141   -145   -329       C  
-ATOM    716  O   MET A 764     -35.722  -7.003  -8.148  1.00 28.18           O  
-ANISOU  716  O   MET A 764     3573   3465   3668    131   -143   -316       O  
-ATOM    717  CB  MET A 764     -32.518  -6.509  -8.816  1.00 36.04           C  
-ANISOU  717  CB  MET A 764     4520   4491   4683    163   -150   -385       C  
-ATOM    718  CG  MET A 764     -32.784  -7.972  -9.155  1.00 37.47           C  
-ANISOU  718  CG  MET A 764     4715   4650   4873    173   -166   -387       C  
-ATOM    719  SD  MET A 764     -31.312  -8.944  -8.888  1.00 45.01           S  
-ANISOU  719  SD  MET A 764     5661   5595   5847    205   -194   -418       S  
-ATOM    720  CE  MET A 764     -31.494  -9.216  -7.103  1.00 46.12           C  
-ANISOU  720  CE  MET A 764     5827   5716   5981    216   -218   -390       C  
-ATOM    721  N   LEU A 765     -34.424  -6.359  -6.443  1.00 29.45           N  
-ANISOU  721  N   LEU A 765     3732   3636   3823    153   -158   -321       N  
-ATOM    722  CA  LEU A 765     -35.280  -6.991  -5.422  1.00 32.04           C  
-ANISOU  722  CA  LEU A 765     4087   3946   4142    155   -165   -290       C  
-ATOM    723  C   LEU A 765     -36.727  -6.456  -5.492  1.00 33.18           C  
-ANISOU  723  C   LEU A 765     4237   4094   4276    131   -144   -264       C  
-ATOM    724  O   LEU A 765     -37.683  -7.227  -5.359  1.00 32.09           O  
-ANISOU  724  O   LEU A 765     4114   3938   4140    123   -143   -242       O  
-ATOM    725  CB  LEU A 765     -34.698  -6.801  -4.012  1.00 32.50           C  
-ANISOU  725  CB  LEU A 765     4155   4008   4187    174   -181   -285       C  
-ATOM    726  CG  LEU A 765     -33.409  -7.535  -3.678  1.00 34.39           C  
-ANISOU  726  CG  LEU A 765     4393   4238   4435    201   -209   -305       C  
-ATOM    727  CD1 LEU A 765     -32.984  -7.268  -2.225  1.00 35.86           C  
-ANISOU  727  CD1 LEU A 765     4591   4430   4603    222   -226   -299       C  
-ATOM    728  CD2 LEU A 765     -33.603  -9.018  -3.905  1.00 36.94           C  
-ANISOU  728  CD2 LEU A 765     4732   4532   4771    208   -223   -296       C  
-ATOM    729  N   ASP A 766     -36.897  -5.151  -5.691  1.00 31.82           N  
-ANISOU  729  N   ASP A 766     4052   3942   4096    120   -127   -269       N  
-ATOM    730  CA  ASP A 766     -38.258  -4.588  -5.792  1.00 33.93           C  
-ANISOU  730  CA  ASP A 766     4323   4214   4356    100   -108   -248       C  
-ATOM    731  C   ASP A 766     -39.007  -5.228  -6.954  1.00 32.93           C  
-ANISOU  731  C   ASP A 766     4194   4076   4240     87   -103   -246       C  
-ATOM    732  O   ASP A 766     -40.183  -5.598  -6.828  1.00 31.44           O  
-ANISOU  732  O   ASP A 766     4015   3878   4054     75    -98   -225       O  
-ATOM    733  CB  ASP A 766     -38.224  -3.063  -6.031  1.00 37.05           C  
-ANISOU  733  CB  ASP A 766     4702   4629   4746     92    -93   -256       C  
-ATOM    734  CG  ASP A 766     -37.530  -2.274  -4.904  1.00 41.94           C  
-ANISOU  734  CG  ASP A 766     5320   5260   5357    105    -99   -264       C  
-ATOM    735  OD1 ASP A 766     -37.390  -2.769  -3.745  1.00 40.56           O  
-ANISOU  735  OD1 ASP A 766     5159   5080   5171    120   -112   -255       O  
-ATOM    736  OD2 ASP A 766     -37.118  -1.133  -5.199  1.00 40.49           O  
-ANISOU  736  OD2 ASP A 766     5119   5087   5178    100    -92   -278       O  
-ATOM    737  N   ASN A 767     -38.322  -5.328  -8.098  1.00 31.31           N  
-ANISOU  737  N   ASN A 767     3976   3875   4044     89   -105   -270       N  
-ATOM    738  CA  ASN A 767     -38.911  -5.846  -9.317  1.00 29.57           C  
-ANISOU  738  CA  ASN A 767     3754   3650   3831     80   -104   -276       C  
-ATOM    739  C   ASN A 767     -39.188  -7.343  -9.139  1.00 31.82           C  
-ANISOU  739  C   ASN A 767     4052   3907   4131     85   -121   -271       C  
-ATOM    740  O   ASN A 767     -40.245  -7.829  -9.537  1.00 29.10           O  
-ANISOU  740  O   ASN A 767     3712   3550   3796     72   -121   -262       O  
-ATOM    741  CB  ASN A 767     -38.001  -5.555 -10.507  1.00 30.29           C  
-ANISOU  741  CB  ASN A 767     3830   3758   3922     85   -100   -303       C  
-ATOM    742  CG  ASN A 767     -38.637  -5.856 -11.867  1.00 33.10           C  
-ANISOU  742  CG  ASN A 767     4184   4115   4278     78    -97   -311       C  
-ATOM    743  OD1 ASN A 767     -39.885  -5.893 -12.046  1.00 32.05           O  
-ANISOU  743  OD1 ASN A 767     4056   3975   4145     65    -96   -297       O  
-ATOM    744  ND2 ASN A 767     -37.765  -6.012 -12.865  1.00 34.68           N  
-ANISOU  744  ND2 ASN A 767     4373   4327   4476     88    -96   -337       N  
-ATOM    745  N   LEU A 768     -38.290  -8.046  -8.453  1.00 34.02           N  
-ANISOU  745  N   LEU A 768     4337   4173   4415    102   -137   -275       N  
-ATOM    746  CA  LEU A 768     -38.511  -9.459  -8.141  1.00 37.33           C  
-ANISOU  746  CA  LEU A 768     4772   4561   4851    107   -156   -266       C  
-ATOM    747  C   LEU A 768     -39.752  -9.670  -7.322  1.00 35.98           C  
-ANISOU  747  C   LEU A 768     4615   4375   4680     92   -149   -230       C  
-ATOM    748  O   LEU A 768     -40.529 -10.573  -7.591  1.00 36.69           O  
-ANISOU  748  O   LEU A 768     4711   4441   4789     82   -154   -221       O  
-ATOM    749  CB  LEU A 768     -37.315 -10.058  -7.377  1.00 39.10           C  
-ANISOU  749  CB  LEU A 768     5003   4775   5079    132   -176   -273       C  
-ATOM    750  CG  LEU A 768     -36.075 -10.355  -8.190  1.00 44.19           C  
-ANISOU  750  CG  LEU A 768     5632   5424   5733    150   -188   -312       C  
-ATOM    751  CD1 LEU A 768     -35.034 -11.095  -7.337  1.00 45.12           C  
-ANISOU  751  CD1 LEU A 768     5758   5527   5858    176   -213   -317       C  
-ATOM    752  CD2 LEU A 768     -36.430 -11.153  -9.435  1.00 47.86           C  
-ANISOU  752  CD2 LEU A 768     6094   5877   6214    146   -193   -330       C  
-ATOM    753  N   LEU A 769     -39.919  -8.836  -6.304  1.00 38.76           N  
-ANISOU  753  N   LEU A 769     4972   4743   5013     91   -137   -211       N  
-ATOM    754  CA  LEU A 769     -41.060  -8.936  -5.409  1.00 40.64           C  
-ANISOU  754  CA  LEU A 769     5222   4974   5246     78   -125   -175       C  
-ATOM    755  C   LEU A 769     -42.368  -8.840  -6.205  1.00 37.91           C  
-ANISOU  755  C   LEU A 769     4865   4625   4912     54   -112   -170       C  
-ATOM    756  O   LEU A 769     -43.241  -9.682  -6.074  1.00 36.33           O  
-ANISOU  756  O   LEU A 769     4671   4402   4730     42   -111   -150       O  
-ATOM    757  CB  LEU A 769     -40.986  -7.873  -4.304  1.00 46.16           C  
-ANISOU  757  CB  LEU A 769     5924   5696   5917     84   -113   -164       C  
-ATOM    758  CG  LEU A 769     -40.733  -8.323  -2.841  1.00 50.30           C  
-ANISOU  758  CG  LEU A 769     6472   6215   6426     99   -120   -140       C  
-ATOM    759  CD1 LEU A 769     -40.992  -7.093  -1.964  1.00 50.75           C  
-ANISOU  759  CD1 LEU A 769     6528   6301   6454    102   -104   -133       C  
-ATOM    760  CD2 LEU A 769     -41.552  -9.511  -2.343  1.00 51.80           C  
-ANISOU  760  CD2 LEU A 769     6679   6377   6625     91   -118   -104       C  
-ATOM    761  N   ASP A 770     -42.489  -7.846  -7.077  1.00 35.20           N  
-ANISOU  761  N   ASP A 770     4507   4305   4564     48   -102   -188       N  
-ATOM    762  CA  ASP A 770     -43.721  -7.679  -7.855  1.00 32.76           C  
-ANISOU  762  CA  ASP A 770     4188   3995   4265     29    -94   -186       C  
-ATOM    763  C   ASP A 770     -43.885  -8.779  -8.903  1.00 31.88           C  
-ANISOU  763  C   ASP A 770     4073   3861   4177     26   -110   -201       C  
-ATOM    764  O   ASP A 770     -45.022  -9.170  -9.250  1.00 29.56           O  
-ANISOU  764  O   ASP A 770     3774   3555   3902     10   -110   -194       O  
-ATOM    765  CB  ASP A 770     -43.779  -6.285  -8.500  1.00 34.80           C  
-ANISOU  765  CB  ASP A 770     4432   4282   4508     26    -82   -199       C  
-ATOM    766  CG  ASP A 770     -44.269  -5.178  -7.521  1.00 38.50           C  
-ANISOU  766  CG  ASP A 770     4900   4767   4960     23    -64   -181       C  
-ATOM    767  OD1 ASP A 770     -45.145  -5.443  -6.667  1.00 46.59           O  
-ANISOU  767  OD1 ASP A 770     5930   5786   5987     15    -56   -157       O  
-ATOM    768  OD2 ASP A 770     -43.826  -4.012  -7.656  1.00 40.03           O  
-ANISOU  768  OD2 ASP A 770     5088   4982   5142     27    -58   -191       O  
-ATOM    769  N   ILE A 771     -42.775  -9.261  -9.441  1.00 31.05           N  
-ANISOU  769  N   ILE A 771     3970   3753   4075     42   -125   -226       N  
-ATOM    770  CA  ILE A 771     -42.828 -10.433 -10.319  1.00 32.05           C  
-ANISOU  770  CA  ILE A 771     4096   3856   4226     43   -145   -245       C  
-ATOM    771  C   ILE A 771     -43.387 -11.648  -9.567  1.00 33.92           C  
-ANISOU  771  C   ILE A 771     4344   4054   4489     36   -154   -221       C  
-ATOM    772  O   ILE A 771     -44.249 -12.360 -10.081  1.00 37.06           O  
-ANISOU  772  O   ILE A 771     4738   4431   4913     23   -163   -223       O  
-ATOM    773  CB  ILE A 771     -41.458 -10.728 -10.965  1.00 33.61           C  
-ANISOU  773  CB  ILE A 771     4291   4059   4420     65   -158   -278       C  
-ATOM    774  CG1 ILE A 771     -41.190  -9.716 -12.075  1.00 34.07           C  
-ANISOU  774  CG1 ILE A 771     4335   4151   4458     67   -147   -300       C  
-ATOM    775  CG2 ILE A 771     -41.422 -12.122 -11.563  1.00 34.45           C  
-ANISOU  775  CG2 ILE A 771     4400   4135   4554     72   -182   -297       C  
-ATOM    776  CD1 ILE A 771     -39.728  -9.567 -12.465  1.00 35.98           C  
-ANISOU  776  CD1 ILE A 771     4570   4410   4690     87   -148   -327       C  
-ATOM    777  N   GLU A 772     -42.918 -11.887  -8.351  1.00 35.17           N  
-ANISOU  777  N   GLU A 772     4517   4204   4641     44   -154   -199       N  
-ATOM    778  CA  GLU A 772     -43.465 -12.957  -7.529  1.00 37.21           C  
-ANISOU  778  CA  GLU A 772     4790   4427   4922     36   -159   -168       C  
-ATOM    779  C   GLU A 772     -44.962 -12.777  -7.356  1.00 34.90           C  
-ANISOU  779  C   GLU A 772     4490   4132   4640      9   -140   -142       C  
-ATOM    780  O   GLU A 772     -45.707 -13.748  -7.425  1.00 35.09           O  
-ANISOU  780  O   GLU A 772     4513   4122   4696     -6   -146   -131       O  
-ATOM    781  CB  GLU A 772     -42.754 -12.974  -6.177  1.00 43.70           C  
-ANISOU  781  CB  GLU A 772     5630   5249   5724     52   -158   -144       C  
-ATOM    782  CG  GLU A 772     -43.408 -13.775  -5.058  1.00 51.88           C  
-ANISOU  782  CG  GLU A 772     6685   6257   6771     42   -153    -99       C  
-ATOM    783  CD  GLU A 772     -44.415 -12.972  -4.173  1.00 62.30           C  
-ANISOU  783  CD  GLU A 772     8004   7598   8069     26   -122    -65       C  
-ATOM    784  OE1 GLU A 772     -44.089 -11.875  -3.597  1.00 57.26           O  
-ANISOU  784  OE1 GLU A 772     7367   6995   7395     36   -110    -66       O  
-ATOM    785  OE2 GLU A 772     -45.560 -13.475  -4.023  1.00 64.17           O  
-ANISOU  785  OE2 GLU A 772     8239   7815   8328      3   -110    -39       O  
-ATOM    786  N   VAL A 773     -45.412 -11.545  -7.083  1.00 34.18           N  
-ANISOU  786  N   VAL A 773     4390   4073   4523      3   -118   -134       N  
-ATOM    787  CA  VAL A 773     -46.841 -11.283  -6.905  1.00 32.22           C  
-ANISOU  787  CA  VAL A 773     4132   3827   4284    -21    -98   -113       C  
-ATOM    788  C   VAL A 773     -47.592 -11.684  -8.160  1.00 33.42           C  
-ANISOU  788  C   VAL A 773     4266   3965   4466    -35   -110   -135       C  
-ATOM    789  O   VAL A 773     -48.622 -12.354  -8.100  1.00 38.07           O  
-ANISOU  789  O   VAL A 773     4849   4530   5087    -54   -108   -120       O  
-ATOM    790  CB  VAL A 773     -47.116  -9.811  -6.586  1.00 33.67           C  
-ANISOU  790  CB  VAL A 773     4308   4050   4438    -21    -77   -110       C  
-ATOM    791  CG1 VAL A 773     -48.608  -9.521  -6.672  1.00 35.22           C  
-ANISOU  791  CG1 VAL A 773     4486   4248   4647    -43    -60    -98       C  
-ATOM    792  CG2 VAL A 773     -46.572  -9.451  -5.207  1.00 32.28           C  
-ANISOU  792  CG2 VAL A 773     4148   3886   4232     -8    -65    -88       C  
-ATOM    793  N   ALA A 774     -47.069 -11.285  -9.303  1.00 32.59           N  
-ANISOU  793  N   ALA A 774     4154   3876   4353    -24   -123   -171       N  
-ATOM    794  CA  ALA A 774     -47.706 -11.579 -10.567  1.00 33.50           C  
-ANISOU  794  CA  ALA A 774     4255   3984   4489    -31   -137   -196       C  
-ATOM    795  C   ALA A 774     -47.751 -13.088 -10.806  1.00 38.83           C  
-ANISOU  795  C   ALA A 774     4934   4616   5204    -34   -160   -203       C  
-ATOM    796  O   ALA A 774     -48.779 -13.629 -11.198  1.00 37.51           O  
-ANISOU  796  O   ALA A 774     4755   4428   5069    -51   -168   -205       O  
-ATOM    797  CB  ALA A 774     -46.966 -10.883 -11.703  1.00 31.62           C  
-ANISOU  797  CB  ALA A 774     4014   3775   4227    -15   -144   -231       C  
-ATOM    798  N   TYR A 775     -46.631 -13.761 -10.547  1.00 40.61           N  
-ANISOU  798  N   TYR A 775     5174   4826   5429    -17   -173   -208       N  
-ATOM    799  CA  TYR A 775     -46.551 -15.188 -10.766  1.00 41.46           C  
-ANISOU  799  CA  TYR A 775     5287   4890   5575    -16   -198   -217       C  
-ATOM    800  C   TYR A 775     -47.502 -15.957  -9.844  1.00 41.63           C  
-ANISOU  800  C   TYR A 775     5312   4875   5632    -39   -191   -177       C  
-ATOM    801  O   TYR A 775     -48.134 -16.910 -10.279  1.00 42.04           O  
-ANISOU  801  O   TYR A 775     5357   4890   5727    -52   -208   -184       O  
-ATOM    802  CB  TYR A 775     -45.108 -15.703 -10.617  1.00 42.39           C  
-ANISOU  802  CB  TYR A 775     5420   5000   5686     11   -214   -231       C  
-ATOM    803  CG  TYR A 775     -44.927 -17.027 -11.282  1.00 41.56           C  
-ANISOU  803  CG  TYR A 775     5316   4854   5619     18   -245   -257       C  
-ATOM    804  CD1 TYR A 775     -44.872 -17.102 -12.650  1.00 44.40           C  
-ANISOU  804  CD1 TYR A 775     5664   5224   5983     26   -262   -304       C  
-ATOM    805  CD2 TYR A 775     -44.880 -18.212 -10.558  1.00 44.50           C  
-ANISOU  805  CD2 TYR A 775     5703   5180   6027     16   -259   -236       C  
-ATOM    806  CE1 TYR A 775     -44.755 -18.308 -13.298  1.00 45.05           C  
-ANISOU  806  CE1 TYR A 775     5746   5270   6102     34   -293   -334       C  
-ATOM    807  CE2 TYR A 775     -44.751 -19.447 -11.199  1.00 46.59           C  
-ANISOU  807  CE2 TYR A 775     5968   5402   6333     22   -291   -263       C  
-ATOM    808  CZ  TYR A 775     -44.682 -19.477 -12.577  1.00 46.66           C  
-ANISOU  808  CZ  TYR A 775     5962   5422   6344     32   -308   -315       C  
-ATOM    809  OH  TYR A 775     -44.539 -20.657 -13.273  1.00 51.36           O  
-ANISOU  809  OH  TYR A 775     6557   5980   6979     42   -342   -349       O  
-ATOM    810  N   SER A 776     -47.574 -15.561  -8.583  1.00 42.05           N  
-ANISOU  810  N   SER A 776     5375   4936   5665    -44   -167   -136       N  
-ATOM    811  CA  SER A 776     -48.489 -16.179  -7.632  1.00 43.41           C  
-ANISOU  811  CA  SER A 776     5550   5079   5863    -67   -153    -91       C  
-ATOM    812  C   SER A 776     -49.938 -16.035  -8.035  1.00 42.81           C  
-ANISOU  812  C   SER A 776     5450   5002   5814    -95   -142    -89       C  
-ATOM    813  O   SER A 776     -50.710 -16.975  -7.920  1.00 45.71           O  
-ANISOU  813  O   SER A 776     5811   5330   6227   -117   -145    -73       O  
-ATOM    814  CB  SER A 776     -48.338 -15.541  -6.254  1.00 47.66           C  
-ANISOU  814  CB  SER A 776     6103   5640   6363    -63   -125    -51       C  
-ATOM    815  OG  SER A 776     -47.092 -15.902  -5.700  1.00 57.93           O  
-ANISOU  815  OG  SER A 776     7429   6934   7647    -38   -139    -48       O  
-ATOM    816  N   LEU A 777     -50.327 -14.837  -8.446  1.00 43.28           N  
-ANISOU  816  N   LEU A 777     5494   5102   5848    -96   -129   -104       N  
-ATOM    817  CA  LEU A 777     -51.695 -14.596  -8.842  1.00 39.86           C  
-ANISOU  817  CA  LEU A 777     5034   4671   5439   -119   -121   -105       C  
-ATOM    818  C   LEU A 777     -52.037 -15.500 -10.000  1.00 41.14           C  
-ANISOU  818  C   LEU A 777     5183   4802   5646   -126   -153   -138       C  
-ATOM    819  O   LEU A 777     -53.079 -16.147  -9.989  1.00 37.89           O  
-ANISOU  819  O   LEU A 777     4755   4362   5281   -150   -153   -128       O  
-ATOM    820  CB  LEU A 777     -51.900 -13.153  -9.269  1.00 40.57           C  
-ANISOU  820  CB  LEU A 777     5112   4809   5494   -113   -110   -121       C  
-ATOM    821  CG  LEU A 777     -52.020 -12.112  -8.164  1.00 39.64           C  
-ANISOU  821  CG  LEU A 777     4998   4723   5340   -112    -77    -92       C  
-ATOM    822  CD1 LEU A 777     -52.168 -10.738  -8.812  1.00 40.39           C  
-ANISOU  822  CD1 LEU A 777     5081   4859   5408   -103    -73   -114       C  
-ATOM    823  CD2 LEU A 777     -53.197 -12.384  -7.231  1.00 38.09           C  
-ANISOU  823  CD2 LEU A 777     4790   4516   5167   -137    -51    -54       C  
-ATOM    824  N   LEU A 778     -51.120 -15.592 -10.951  1.00 40.73           N  
-ANISOU  824  N   LEU A 778     5138   4755   5581   -103   -179   -178       N  
-ATOM    825  CA  LEU A 778     -51.316 -16.375 -12.159  1.00 46.04           C  
-ANISOU  825  CA  LEU A 778     5801   5405   6289   -102   -212   -219       C  
-ATOM    826  C   LEU A 778     -51.453 -17.855 -11.868  1.00 46.96           C  
-ANISOU  826  C   LEU A 778     5920   5462   6459   -114   -229   -209       C  
-ATOM    827  O   LEU A 778     -52.300 -18.528 -12.448  1.00 45.25           O  
-ANISOU  827  O   LEU A 778     5686   5217   6290   -130   -248   -226       O  
-ATOM    828  CB  LEU A 778     -50.112 -16.156 -13.100  1.00 51.07           C  
-ANISOU  828  CB  LEU A 778     6448   6064   6892    -71   -231   -261       C  
-ATOM    829  CG  LEU A 778     -50.221 -16.531 -14.577  1.00 55.22           C  
-ANISOU  829  CG  LEU A 778     6963   6587   7430    -60   -264   -313       C  
-ATOM    830  CD1 LEU A 778     -51.475 -15.941 -15.198  1.00 56.31           C  
-ANISOU  830  CD1 LEU A 778     7079   6742   7575    -75   -264   -322       C  
-ATOM    831  CD2 LEU A 778     -48.980 -16.034 -15.306  1.00 58.66           C  
-ANISOU  831  CD2 LEU A 778     7409   7057   7820    -30   -268   -344       C  
-ATOM    832  N   ARG A 779     -50.610 -18.374 -10.979  1.00 47.99           N  
-ANISOU  832  N   ARG A 779     6074   5573   6585   -105   -226   -184       N  
-ATOM    833  CA  ARG A 779     -50.626 -19.812 -10.682  1.00 51.20           C  
-ANISOU  833  CA  ARG A 779     6489   5921   7045   -114   -244   -172       C  
-ATOM    834  C   ARG A 779     -51.781 -20.203  -9.727  1.00 51.98           C  
-ANISOU  834  C   ARG A 779     6579   5990   7180   -150   -220   -121       C  
-ATOM    835  O   ARG A 779     -52.279 -21.330  -9.787  1.00 53.81           O  
-ANISOU  835  O   ARG A 779     6805   6169   7472   -168   -236   -116       O  
-ATOM    836  CB  ARG A 779     -49.257 -20.268 -10.146  1.00 52.29           C  
-ANISOU  836  CB  ARG A 779     6656   6047   7166    -88   -254   -165       C  
-ATOM    837  N   GLY A 780     -52.253 -19.261  -8.905  1.00 51.94           N  
-ANISOU  837  N   GLY A 780     6572   6020   7144   -160   -182    -85       N  
-ATOM    838  CA  GLY A 780     -53.261 -19.564  -7.862  1.00 50.93           C  
-ANISOU  838  CA  GLY A 780     6437   5872   7043   -192   -152    -32       C  
-ATOM    839  C   GLY A 780     -54.716 -19.354  -8.246  1.00 48.87           C  
-ANISOU  839  C   GLY A 780     6138   5612   6817   -222   -141    -36       C  
-ATOM    840  O   GLY A 780     -55.040 -19.227  -9.424  1.00 47.51           O  
-ANISOU  840  O   GLY A 780     5945   5445   6661   -220   -166    -83       O  
-ATOM    841  N   SER A 786     -63.371 -23.070 -16.797  1.00 63.19           N  
-ANISOU  841  N   SER A 786     7631   7227   9151   -357   -425   -406       N  
-ATOM    842  CA  SER A 786     -64.654 -22.769 -17.410  1.00 69.31           C  
-ANISOU  842  CA  SER A 786     8359   8011   9964   -370   -444   -439       C  
-ATOM    843  C   SER A 786     -64.626 -21.412 -18.165  1.00 72.04           C  
-ANISOU  843  C   SER A 786     8709   8429  10233   -335   -451   -468       C  
-ATOM    844  O   SER A 786     -65.041 -21.336 -19.332  1.00 67.21           O  
-ANISOU  844  O   SER A 786     8081   7828   9629   -318   -498   -528       O  
-ATOM    845  CB  SER A 786     -65.764 -22.786 -16.341  1.00 66.51           C  
-ANISOU  845  CB  SER A 786     7967   7640   9665   -417   -399   -386       C  
-ATOM    846  N   LYS A 787     -64.118 -20.357 -17.507  1.00 70.34           N  
-ANISOU  846  N   LYS A 787     8519   8262   9946   -323   -407   -428       N  
-ATOM    847  CA  LYS A 787     -64.028 -19.009 -18.108  1.00 63.91           C  
-ANISOU  847  CA  LYS A 787     7712   7512   9058   -291   -409   -447       C  
-ATOM    848  C   LYS A 787     -62.761 -18.839 -18.983  1.00 58.80           C  
-ANISOU  848  C   LYS A 787     7107   6889   8344   -247   -435   -480       C  
-ATOM    849  O   LYS A 787     -61.771 -19.538 -18.779  1.00 56.78           O  
-ANISOU  849  O   LYS A 787     6880   6610   8084   -241   -436   -474       O  
-ATOM    850  CB  LYS A 787     -64.064 -17.939 -17.007  1.00 61.55           C  
-ANISOU  850  CB  LYS A 787     7419   7252   8716   -297   -351   -391       C  
-ATOM    851  N   ASP A 788     -62.789 -17.916 -19.950  1.00 56.10           N  
-ANISOU  851  N   ASP A 788     6769   6596   7952   -217   -455   -514       N  
-ATOM    852  CA  ASP A 788     -61.573 -17.537 -20.690  1.00 53.65           C  
-ANISOU  852  CA  ASP A 788     6498   6319   7568   -177   -468   -537       C  
-ATOM    853  C   ASP A 788     -60.490 -17.145 -19.660  1.00 51.25           C  
-ANISOU  853  C   ASP A 788     6227   6028   7218   -175   -421   -486       C  
-ATOM    854  O   ASP A 788     -60.772 -16.358 -18.755  1.00 47.59           O  
-ANISOU  854  O   ASP A 788     5759   5582   6739   -188   -380   -442       O  
-ATOM    855  CB  ASP A 788     -61.845 -16.341 -21.621  1.00 53.19           C  
-ANISOU  855  CB  ASP A 788     6440   6315   7455   -149   -482   -561       C  
-ATOM    856  CG  ASP A 788     -60.681 -16.050 -22.574  1.00 54.89           C  
-ANISOU  856  CG  ASP A 788     6692   6564   7599   -108   -498   -590       C  
-ATOM    857  OD1 ASP A 788     -60.900 -15.501 -23.689  1.00 58.81           O  
-ANISOU  857  OD1 ASP A 788     7190   7094   8061    -82   -527   -625       O  
-ATOM    858  OD2 ASP A 788     -59.533 -16.360 -22.219  1.00 53.97           O  
-ANISOU  858  OD2 ASP A 788     6604   6442   7460   -101   -481   -576       O  
-ATOM    859  N   PRO A 789     -59.264 -17.701 -19.783  1.00 47.40           N  
-ANISOU  859  N   PRO A 789     5770   5530   6708   -156   -428   -495       N  
-ATOM    860  CA  PRO A 789     -58.198 -17.371 -18.833  1.00 44.08           C  
-ANISOU  860  CA  PRO A 789     5380   5121   6247   -152   -388   -451       C  
-ATOM    861  C   PRO A 789     -57.891 -15.872 -18.696  1.00 41.33           C  
-ANISOU  861  C   PRO A 789     5044   4830   5829   -137   -359   -431       C  
-ATOM    862  O   PRO A 789     -57.592 -15.431 -17.618  1.00 38.56           O  
-ANISOU  862  O   PRO A 789     4704   4487   5462   -145   -320   -386       O  
-ATOM    863  CB  PRO A 789     -56.987 -18.122 -19.399  1.00 46.08           C  
-ANISOU  863  CB  PRO A 789     5660   5363   6487   -126   -413   -482       C  
-ATOM    864  CG  PRO A 789     -57.574 -19.293 -20.099  1.00 47.57           C  
-ANISOU  864  CG  PRO A 789     5829   5507   6738   -133   -457   -525       C  
-ATOM    865  CD  PRO A 789     -58.858 -18.790 -20.702  1.00 48.45           C  
-ANISOU  865  CD  PRO A 789     5909   5635   6864   -141   -473   -546       C  
-ATOM    866  N   ILE A 790     -57.980 -15.109 -19.785  1.00 41.32           N  
-ANISOU  866  N   ILE A 790     5044   4867   5790   -113   -377   -463       N  
-ATOM    867  CA  ILE A 790     -57.805 -13.666 -19.726  1.00 42.19           C  
-ANISOU  867  CA  ILE A 790     5163   5025   5841   -101   -352   -444       C  
-ATOM    868  C   ILE A 790     -58.771 -13.071 -18.706  1.00 42.23           C  
-ANISOU  868  C   ILE A 790     5146   5032   5866   -126   -321   -405       C  
-ATOM    869  O   ILE A 790     -58.365 -12.235 -17.898  1.00 41.44           O  
-ANISOU  869  O   ILE A 790     5059   4955   5733   -126   -286   -370       O  
-ATOM    870  CB  ILE A 790     -57.994 -13.007 -21.109  1.00 45.25           C  
-ANISOU  870  CB  ILE A 790     5552   5450   6193    -74   -381   -483       C  
-ATOM    871  CG1 ILE A 790     -56.848 -13.401 -22.045  1.00 46.35           C  
-ANISOU  871  CG1 ILE A 790     5717   5598   6295    -45   -401   -517       C  
-ATOM    872  CG2 ILE A 790     -58.015 -11.485 -21.005  1.00 46.00           C  
-ANISOU  872  CG2 ILE A 790     5653   5588   6237    -65   -356   -458       C  
-ATOM    873  CD1 ILE A 790     -57.242 -13.424 -23.512  1.00 51.82           C  
-ANISOU  873  CD1 ILE A 790     6407   6309   6975    -21   -444   -567       C  
-ATOM    874  N   ASP A 791     -60.026 -13.513 -18.732  1.00 39.66           N  
-ANISOU  874  N   ASP A 791     4787   4684   5597   -148   -335   -413       N  
-ATOM    875  CA  ASP A 791     -61.037 -13.030 -17.790  1.00 42.05           C  
-ANISOU  875  CA  ASP A 791     5064   4990   5925   -172   -305   -380       C  
-ATOM    876  C   ASP A 791     -60.734 -13.461 -16.356  1.00 41.59           C  
-ANISOU  876  C   ASP A 791     5012   4909   5881   -195   -265   -331       C  
-ATOM    877  O   ASP A 791     -61.000 -12.712 -15.405  1.00 39.90           O  
-ANISOU  877  O   ASP A 791     4794   4714   5653   -203   -227   -295       O  
-ATOM    878  CB  ASP A 791     -62.459 -13.516 -18.175  1.00 43.20           C  
-ANISOU  878  CB  ASP A 791     5166   5113   6136   -192   -329   -403       C  
-ATOM    879  CG  ASP A 791     -63.064 -12.770 -19.365  1.00 48.10           C  
-ANISOU  879  CG  ASP A 791     5774   5764   6739   -171   -363   -442       C  
-ATOM    880  OD1 ASP A 791     -64.281 -12.940 -19.600  1.00 54.48           O  
-ANISOU  880  OD1 ASP A 791     6543   6561   7597   -185   -382   -460       O  
-ATOM    881  OD2 ASP A 791     -62.352 -12.027 -20.077  1.00 54.46           O  
-ANISOU  881  OD2 ASP A 791     6607   6603   7482   -140   -373   -455       O  
-ATOM    882  N   VAL A 792     -60.213 -14.674 -16.192  1.00 41.57           N  
-ANISOU  882  N   VAL A 792     5021   4866   5907   -202   -274   -331       N  
-ATOM    883  CA  VAL A 792     -59.905 -15.167 -14.857  1.00 40.52           C  
-ANISOU  883  CA  VAL A 792     4898   4710   5787   -221   -239   -283       C  
-ATOM    884  C   VAL A 792     -58.802 -14.308 -14.245  1.00 37.83           C  
-ANISOU  884  C   VAL A 792     4592   4404   5380   -201   -211   -258       C  
-ATOM    885  O   VAL A 792     -58.899 -13.887 -13.101  1.00 37.64           O  
-ANISOU  885  O   VAL A 792     4569   4390   5343   -211   -173   -216       O  
-ATOM    886  CB  VAL A 792     -59.449 -16.644 -14.878  1.00 43.64           C  
-ANISOU  886  CB  VAL A 792     5303   5052   6225   -229   -260   -288       C  
-ATOM    887  CG1 VAL A 792     -58.953 -17.076 -13.500  1.00 42.22           C  
-ANISOU  887  CG1 VAL A 792     5143   4853   6047   -242   -225   -235       C  
-ATOM    888  CG2 VAL A 792     -60.582 -17.544 -15.339  1.00 46.95           C  
-ANISOU  888  CG2 VAL A 792     5687   5432   6721   -254   -286   -310       C  
-ATOM    889  N   ASN A 793     -57.757 -14.042 -15.020  1.00 35.53           N  
-ANISOU  889  N   ASN A 793     4323   4131   5044   -172   -230   -285       N  
-ATOM    890  CA  ASN A 793     -56.667 -13.223 -14.546  1.00 35.80           C  
-ANISOU  890  CA  ASN A 793     4386   4196   5021   -152   -207   -267       C  
-ATOM    891  C   ASN A 793     -57.036 -11.739 -14.350  1.00 33.81           C  
-ANISOU  891  C   ASN A 793     4127   3987   4731   -147   -184   -255       C  
-ATOM    892  O   ASN A 793     -56.551 -11.104 -13.429  1.00 32.89           O  
-ANISOU  892  O   ASN A 793     4025   3889   4584   -144   -155   -226       O  
-ATOM    893  CB  ASN A 793     -55.471 -13.427 -15.457  1.00 37.08           C  
-ANISOU  893  CB  ASN A 793     4572   4365   5154   -125   -232   -299       C  
-ATOM    894  CG  ASN A 793     -54.937 -14.854 -15.325  1.00 40.89           C  
-ANISOU  894  CG  ASN A 793     5063   4802   5671   -128   -249   -304       C  
-ATOM    895  OD1 ASN A 793     -54.496 -15.249 -14.262  1.00 38.64           O  
-ANISOU  895  OD1 ASN A 793     4792   4499   5391   -135   -230   -271       O  
-ATOM    896  ND2 ASN A 793     -55.070 -15.650 -16.372  1.00 40.61           N  
-ANISOU  896  ND2 ASN A 793     5021   4746   5662   -122   -286   -346       N  
-ATOM    897  N   TYR A 794     -57.889 -11.202 -15.210  1.00 33.09           N  
-ANISOU  897  N   TYR A 794     4016   3912   4644   -145   -201   -279       N  
-ATOM    898  CA  TYR A 794     -58.416  -9.848 -15.028  1.00 32.73           C  
-ANISOU  898  CA  TYR A 794     3960   3901   4573   -141   -183   -268       C  
-ATOM    899  C   TYR A 794     -59.001  -9.737 -13.640  1.00 31.87           C  
-ANISOU  899  C   TYR A 794     3839   3789   4480   -162   -145   -229       C  
-ATOM    900  O   TYR A 794     -58.692  -8.800 -12.918  1.00 31.57           O  
-ANISOU  900  O   TYR A 794     3811   3776   4407   -155   -119   -207       O  
-ATOM    901  CB  TYR A 794     -59.471  -9.536 -16.095  1.00 32.10           C  
-ANISOU  901  CB  TYR A 794     3856   3831   4510   -138   -210   -299       C  
-ATOM    902  CG  TYR A 794     -60.280  -8.284 -15.853  1.00 32.90           C  
-ANISOU  902  CG  TYR A 794     3940   3960   4599   -137   -195   -288       C  
-ATOM    903  CD1 TYR A 794     -59.726  -7.029 -16.025  1.00 32.91           C  
-ANISOU  903  CD1 TYR A 794     3961   3995   4550   -116   -187   -285       C  
-ATOM    904  CD2 TYR A 794     -61.602  -8.353 -15.459  1.00 32.62           C  
-ANISOU  904  CD2 TYR A 794     3868   3917   4607   -158   -188   -283       C  
-ATOM    905  CE1 TYR A 794     -60.465  -5.881 -15.822  1.00 32.28           C  
-ANISOU  905  CE1 TYR A 794     3865   3937   4462   -113   -176   -277       C  
-ATOM    906  CE2 TYR A 794     -62.347  -7.202 -15.235  1.00 32.71           C  
-ANISOU  906  CE2 TYR A 794     3862   3955   4610   -154   -175   -277       C  
-ATOM    907  CZ  TYR A 794     -61.778  -5.966 -15.418  1.00 31.91           C  
-ANISOU  907  CZ  TYR A 794     3782   3884   4458   -130   -170   -274       C  
-ATOM    908  OH  TYR A 794     -62.502  -4.806 -15.185  1.00 28.97           O  
-ANISOU  908  OH  TYR A 794     3393   3534   4078   -124   -159   -269       O  
-ATOM    909  N   GLU A 795     -59.863 -10.684 -13.280  1.00 33.07           N  
-ANISOU  909  N   GLU A 795     3968   3910   4686   -188   -143   -220       N  
-ATOM    910  CA  GLU A 795     -60.555 -10.653 -11.990  1.00 34.88           C  
-ANISOU  910  CA  GLU A 795     4181   4137   4933   -210   -105   -181       C  
-ATOM    911  C   GLU A 795     -59.580 -10.700 -10.825  1.00 35.18           C  
-ANISOU  911  C   GLU A 795     4251   4177   4940   -206    -75   -145       C  
-ATOM    912  O   GLU A 795     -59.837 -10.119  -9.772  1.00 35.05           O  
-ANISOU  912  O   GLU A 795     4231   4179   4907   -211    -40   -116       O  
-ATOM    913  CB  GLU A 795     -61.588 -11.775 -11.895  1.00 39.39           C  
-ANISOU  913  CB  GLU A 795     4722   4671   5574   -241   -108   -178       C  
-ATOM    914  CG  GLU A 795     -62.826 -11.528 -12.765  1.00 44.93           C  
-ANISOU  914  CG  GLU A 795     5383   5376   6311   -248   -130   -209       C  
-ATOM    915  CD  GLU A 795     -63.796 -12.719 -12.884  1.00 52.46           C  
-ANISOU  915  CD  GLU A 795     6302   6287   7341   -279   -142   -215       C  
-ATOM    916  OE1 GLU A 795     -63.559 -13.820 -12.316  1.00 53.40           O  
-ANISOU  916  OE1 GLU A 795     6430   6369   7493   -298   -133   -192       O  
-ATOM    917  OE2 GLU A 795     -64.833 -12.543 -13.559  1.00 58.37           O  
-ANISOU  917  OE2 GLU A 795     7015   7039   8123   -284   -163   -243       O  
-ATOM    918  N   LYS A 796     -58.457 -11.379 -11.013  1.00 34.61           N  
-ANISOU  918  N   LYS A 796     4206   4087   4857   -196    -91   -150       N  
-ATOM    919  CA  LYS A 796     -57.429 -11.476  -9.960  1.00 35.04           C  
-ANISOU  919  CA  LYS A 796     4291   4142   4880   -188    -70   -119       C  
-ATOM    920  C   LYS A 796     -56.768 -10.150  -9.614  1.00 33.27           C  
-ANISOU  920  C   LYS A 796     4084   3960   4599   -166    -54   -116       C  
-ATOM    921  O   LYS A 796     -56.254  -9.994  -8.513  1.00 35.44           O  
-ANISOU  921  O   LYS A 796     4376   4243   4848   -162    -31    -88       O  
-ATOM    922  CB  LYS A 796     -56.352 -12.460 -10.372  1.00 36.04           C  
-ANISOU  922  CB  LYS A 796     4441   4240   5010   -178    -96   -132       C  
-ATOM    923  CG  LYS A 796     -56.781 -13.925 -10.320  1.00 38.00           C  
-ANISOU  923  CG  LYS A 796     4683   4439   5318   -200   -108   -125       C  
-ATOM    924  CD  LYS A 796     -55.722 -14.786 -10.994  1.00 41.07           C  
-ANISOU  924  CD  LYS A 796     5092   4803   5710   -183   -141   -151       C  
-ATOM    925  CE  LYS A 796     -56.087 -16.263 -11.053  1.00 42.80           C  
-ANISOU  925  CE  LYS A 796     5305   4966   5993   -203   -159   -149       C  
-ATOM    926  NZ  LYS A 796     -55.123 -17.030 -11.901  1.00 44.60           N  
-ANISOU  926  NZ  LYS A 796     5549   5173   6226   -183   -197   -185       N  
-ATOM    927  N   LEU A 797     -56.757  -9.210 -10.562  1.00 31.88           N  
-ANISOU  927  N   LEU A 797     3902   3809   4402   -151    -69   -145       N  
-ATOM    928  CA  LEU A 797     -56.228  -7.857 -10.322  1.00 30.17           C  
-ANISOU  928  CA  LEU A 797     3696   3628   4137   -132    -56   -144       C  
-ATOM    929  C   LEU A 797     -57.121  -7.039  -9.377  1.00 30.76           C  
-ANISOU  929  C   LEU A 797     3755   3724   4209   -140    -25   -123       C  
-ATOM    930  O   LEU A 797     -56.652  -6.086  -8.790  1.00 30.98           O  
-ANISOU  930  O   LEU A 797     3794   3775   4201   -126     -9   -115       O  
-ATOM    931  CB  LEU A 797     -56.072  -7.078 -11.620  1.00 28.39           C  
-ANISOU  931  CB  LEU A 797     3470   3422   3895   -116    -78   -176       C  
-ATOM    932  CG  LEU A 797     -55.167  -7.694 -12.666  1.00 29.95           C  
-ANISOU  932  CG  LEU A 797     3683   3609   4087   -104   -107   -202       C  
-ATOM    933  CD1 LEU A 797     -55.249  -6.913 -13.962  1.00 31.86           C  
-ANISOU  933  CD1 LEU A 797     3922   3872   4311    -89   -126   -229       C  
-ATOM    934  CD2 LEU A 797     -53.734  -7.759 -12.176  1.00 30.02           C  
-ANISOU  934  CD2 LEU A 797     3719   3620   4067    -91    -99   -194       C  
-ATOM    935  N   LYS A 798     -58.399  -7.409  -9.249  1.00 32.64           N  
-ANISOU  935  N   LYS A 798     3965   3952   4487   -161    -17   -116       N  
-ATOM    936  CA  LYS A 798     -59.370  -6.713  -8.381  1.00 33.47           C  
-ANISOU  936  CA  LYS A 798     4047   4076   4592   -168     14    -99       C  
-ATOM    937  C   LYS A 798     -59.377  -5.228  -8.703  1.00 30.36           C  
-ANISOU  937  C   LYS A 798     3651   3715   4167   -148     11   -116       C  
-ATOM    938  O   LYS A 798     -59.337  -4.369  -7.830  1.00 28.82           O  
-ANISOU  938  O   LYS A 798     3461   3544   3947   -139     35   -103       O  
-ATOM    939  CB  LYS A 798     -59.054  -6.942  -6.900  1.00 37.50           C  
-ANISOU  939  CB  LYS A 798     4573   4589   5084   -172     48    -61       C  
-ATOM    940  CG  LYS A 798     -59.290  -8.367  -6.419  1.00 40.82           C  
-ANISOU  940  CG  LYS A 798     4993   4975   5540   -195     57    -35       C  
-ATOM    941  CD  LYS A 798     -59.186  -8.409  -4.906  1.00 48.65           C  
-ANISOU  941  CD  LYS A 798     5998   5978   6508   -197     96      5       C  
-ATOM    942  CE  LYS A 798     -59.028  -9.835  -4.379  1.00 56.28           C  
-ANISOU  942  CE  LYS A 798     6977   6907   7499   -214    102     37       C  
-ATOM    943  NZ  LYS A 798     -59.109  -9.903  -2.887  1.00 61.48           N  
-ANISOU  943  NZ  LYS A 798     7648   7578   8133   -217    143     81       N  
-ATOM    944  N   THR A 799     -59.419  -4.955  -9.987  1.00 28.13           N  
-ANISOU  944  N   THR A 799     3366   3434   3889   -139    -19   -145       N  
-ATOM    945  CA  THR A 799     -59.364  -3.604 -10.486  1.00 29.30           C  
-ANISOU  945  CA  THR A 799     3515   3607   4011   -120    -27   -160       C  
-ATOM    946  C   THR A 799     -60.312  -3.506 -11.659  1.00 29.12           C  
-ANISOU  946  C   THR A 799     3468   3582   4012   -120    -54   -185       C  
-ATOM    947  O   THR A 799     -60.241  -4.302 -12.603  1.00 32.37           O  
-ANISOU  947  O   THR A 799     3882   3978   4441   -123    -82   -203       O  
-ATOM    948  CB  THR A 799     -57.918  -3.266 -10.959  1.00 28.82           C  
-ANISOU  948  CB  THR A 799     3487   3551   3911   -101    -39   -168       C  
-ATOM    949  OG1 THR A 799     -57.027  -3.387  -9.849  1.00 30.97           O  
-ANISOU  949  OG1 THR A 799     3779   3824   4162    -99    -18   -147       O  
-ATOM    950  CG2 THR A 799     -57.842  -1.860 -11.502  1.00 27.92           C  
-ANISOU  950  CG2 THR A 799     3375   3459   3772    -83    -46   -179       C  
-ATOM    951  N   ASP A 800     -61.206  -2.551 -11.613  1.00 28.90           N  
-ANISOU  951  N   ASP A 800     3420   3572   3990   -116    -50   -189       N  
-ATOM    952  CA  ASP A 800     -62.063  -2.299 -12.755  1.00 28.31           C  
-ANISOU  952  CA  ASP A 800     3325   3499   3934   -110    -80   -215       C  
-ATOM    953  C   ASP A 800     -61.255  -1.521 -13.791  1.00 26.15           C  
-ANISOU  953  C   ASP A 800     3077   3237   3622    -87   -104   -228       C  
-ATOM    954  O   ASP A 800     -60.696  -0.501 -13.483  1.00 26.70           O  
-ANISOU  954  O   ASP A 800     3163   3321   3660    -73    -92   -219       O  
-ATOM    955  CB  ASP A 800     -63.297  -1.500 -12.347  1.00 29.05           C  
-ANISOU  955  CB  ASP A 800     3385   3608   4046   -111    -69   -215       C  
-ATOM    956  CG  ASP A 800     -64.279  -1.355 -13.497  1.00 31.49           C  
-ANISOU  956  CG  ASP A 800     3669   3916   4379   -105   -104   -243       C  
-ATOM    957  OD1 ASP A 800     -65.096  -2.269 -13.689  1.00 36.60           O  
-ANISOU  957  OD1 ASP A 800     4288   4548   5071   -123   -114   -253       O  
-ATOM    958  OD2 ASP A 800     -64.253  -0.345 -14.207  1.00 32.54           O  
-ANISOU  958  OD2 ASP A 800     3809   4062   4490    -83   -124   -255       O  
-ATOM    959  N   ILE A 801     -61.210  -2.024 -15.014  1.00 26.09           N  
-ANISOU  959  N   ILE A 801     3073   3222   3618    -82   -137   -250       N  
-ATOM    960  CA  ILE A 801     -60.506  -1.386 -16.094  1.00 25.09           C  
-ANISOU  960  CA  ILE A 801     2972   3107   3454    -60   -158   -261       C  
-ATOM    961  C   ILE A 801     -61.443  -1.116 -17.280  1.00 26.36           C  
-ANISOU  961  C   ILE A 801     3118   3274   3624    -48   -193   -285       C  
-ATOM    962  O   ILE A 801     -61.995  -2.044 -17.845  1.00 28.73           O  
-ANISOU  962  O   ILE A 801     3403   3562   3952    -55   -217   -305       O  
-ATOM    963  CB  ILE A 801     -59.333  -2.271 -16.581  1.00 24.03           C  
-ANISOU  963  CB  ILE A 801     2863   2964   3303    -58   -166   -268       C  
-ATOM    964  CG1 ILE A 801     -58.446  -2.684 -15.415  1.00 23.61           C  
-ANISOU  964  CG1 ILE A 801     2823   2902   3244    -68   -137   -246       C  
-ATOM    965  CG2 ILE A 801     -58.503  -1.517 -17.617  1.00 23.88           C  
-ANISOU  965  CG2 ILE A 801     2871   2963   3241    -35   -179   -275       C  
-ATOM    966  CD1 ILE A 801     -57.272  -3.581 -15.776  1.00 23.56           C  
-ANISOU  966  CD1 ILE A 801     2840   2886   3226    -65   -144   -253       C  
-ATOM    967  N   LYS A 802     -61.547   0.141 -17.687  1.00 27.54           N  
-ANISOU  967  N   LYS A 802     3274   3441   3750    -29   -200   -283       N  
-ATOM    968  CA  LYS A 802     -62.338   0.556 -18.829  1.00 29.22           C  
-ANISOU  968  CA  LYS A 802     3478   3661   3963    -12   -236   -303       C  
-ATOM    969  C   LYS A 802     -61.483   1.324 -19.821  1.00 29.35           C  
-ANISOU  969  C   LYS A 802     3529   3692   3931     11   -248   -301       C  
-ATOM    970  O   LYS A 802     -60.613   2.095 -19.440  1.00 27.44           O  
-ANISOU  970  O   LYS A 802     3308   3456   3661     15   -226   -280       O  
-ATOM    971  CB  LYS A 802     -63.467   1.491 -18.386  1.00 33.58           C  
-ANISOU  971  CB  LYS A 802     4003   4220   4536     -9   -233   -301       C  
-ATOM    972  CG  LYS A 802     -64.626   0.799 -17.663  1.00 39.28           C  
-ANISOU  972  CG  LYS A 802     4682   4932   5311    -30   -226   -308       C  
-ATOM    973  CD  LYS A 802     -65.659   1.851 -17.245  1.00 44.14           C  
-ANISOU  973  CD  LYS A 802     5270   5558   5943    -22   -221   -307       C  
-ATOM    974  CE  LYS A 802     -66.930   1.234 -16.649  1.00 49.26           C  
-ANISOU  974  CE  LYS A 802     5869   6200   6647    -41   -214   -317       C  
-ATOM    975  NZ  LYS A 802     -66.748   0.713 -15.257  1.00 48.78           N  
-ANISOU  975  NZ  LYS A 802     5801   6134   6599    -66   -168   -294       N  
-ATOM    976  N   VAL A 803     -61.761   1.133 -21.101  1.00 29.70           N  
-ANISOU  976  N   VAL A 803     3578   3742   3963     27   -285   -322       N  
-ATOM    977  CA  VAL A 803     -61.084   1.853 -22.149  1.00 29.37           C  
-ANISOU  977  CA  VAL A 803     3569   3717   3874     50   -297   -317       C  
-ATOM    978  C   VAL A 803     -61.672   3.254 -22.234  1.00 28.13           C  
-ANISOU  978  C   VAL A 803     3410   3568   3709     66   -302   -305       C  
-ATOM    979  O   VAL A 803     -62.872   3.403 -22.221  1.00 27.51           O  
-ANISOU  979  O   VAL A 803     3305   3488   3661     69   -321   -317       O  
-ATOM    980  CB  VAL A 803     -61.281   1.165 -23.504  1.00 29.72           C  
-ANISOU  980  CB  VAL A 803     3619   3767   3904     66   -336   -346       C  
-ATOM    981  CG1 VAL A 803     -60.612   1.967 -24.608  1.00 30.01           C  
-ANISOU  981  CG1 VAL A 803     3692   3826   3886     91   -346   -338       C  
-ATOM    982  CG2 VAL A 803     -60.711  -0.226 -23.444  1.00 31.12           C  
-ANISOU  982  CG2 VAL A 803     3798   3933   4093     52   -334   -362       C  
-ATOM    983  N   VAL A 804     -60.812   4.267 -22.287  1.00 27.78           N  
-ANISOU  983  N   VAL A 804     3394   3531   3631     75   -286   -281       N  
-ATOM    984  CA  VAL A 804     -61.244   5.618 -22.537  1.00 27.73           C  
-ANISOU  984  CA  VAL A 804     3393   3529   3616     93   -295   -267       C  
-ATOM    985  C   VAL A 804     -61.274   5.846 -24.037  1.00 29.40           C  
-ANISOU  985  C   VAL A 804     3627   3754   3791    118   -328   -272       C  
-ATOM    986  O   VAL A 804     -60.294   5.623 -24.737  1.00 29.54           O  
-ANISOU  986  O   VAL A 804     3673   3781   3770    123   -324   -267       O  
-ATOM    987  CB  VAL A 804     -60.319   6.631 -21.863  1.00 27.83           C  
-ANISOU  987  CB  VAL A 804     3423   3538   3614     90   -262   -239       C  
-ATOM    988  CG1 VAL A 804     -60.709   8.039 -22.264  1.00 27.91           C  
-ANISOU  988  CG1 VAL A 804     3442   3548   3615    110   -275   -224       C  
-ATOM    989  CG2 VAL A 804     -60.388   6.479 -20.340  1.00 28.07           C  
-ANISOU  989  CG2 VAL A 804     3431   3559   3676     69   -232   -236       C  
-ATOM    990  N   ASP A 805     -62.430   6.226 -24.548  1.00 32.06           N  
-ANISOU  990  N   ASP A 805     3950   4093   4138    135   -362   -284       N  
-ATOM    991  CA  ASP A 805     -62.622   6.399 -25.984  1.00 34.76           C  
-ANISOU  991  CA  ASP A 805     4313   4449   4445    163   -400   -290       C  
-ATOM    992  C   ASP A 805     -61.618   7.416 -26.516  1.00 32.28           C  
-ANISOU  992  C   ASP A 805     4040   4142   4081    176   -385   -256       C  
-ATOM    993  O   ASP A 805     -61.504   8.525 -25.977  1.00 32.66           O  
-ANISOU  993  O   ASP A 805     4093   4181   4135    176   -368   -231       O  
-ATOM    994  CB  ASP A 805     -64.073   6.874 -26.220  1.00 40.50           C  
-ANISOU  994  CB  ASP A 805     5016   5175   5198    180   -438   -305       C  
-ATOM    995  CG  ASP A 805     -64.457   6.935 -27.681  1.00 45.89           C  
-ANISOU  995  CG  ASP A 805     5716   5873   5845    212   -485   -317       C  
-ATOM    996  OD1 ASP A 805     -63.661   6.575 -28.573  1.00 51.51           O  
-ANISOU  996  OD1 ASP A 805     6461   6600   6511    222   -488   -316       O  
-ATOM    997  OD2 ASP A 805     -65.595   7.380 -27.934  1.00 57.11           O  
-ANISOU  997  OD2 ASP A 805     7119   7294   7286    230   -519   -329       O  
-ATOM    998  N   ARG A 806     -60.909   7.047 -27.572  1.00 32.60           N  
-ANISOU  998  N   ARG A 806     4110   4200   4075    188   -392   -257       N  
-ATOM    999  CA  ARG A 806     -59.879   7.902 -28.178  1.00 35.02           C  
-ANISOU  999  CA  ARG A 806     4456   4516   4333    198   -374   -223       C  
-ATOM   1000  C   ARG A 806     -60.374   9.274 -28.596  1.00 32.58           C  
-ANISOU 1000  C   ARG A 806     4161   4204   4012    220   -390   -197       C  
-ATOM   1001  O   ARG A 806     -59.601  10.237 -28.638  1.00 36.88           O  
-ANISOU 1001  O   ARG A 806     4731   4746   4537    220   -366   -161       O  
-ATOM   1002  CB  ARG A 806     -59.249   7.180 -29.398  1.00 39.09           C  
-ANISOU 1002  CB  ARG A 806     4998   5057   4798    213   -383   -234       C  
-ATOM   1003  N   ASP A 807     -61.658   9.368 -28.901  1.00 33.69           N  
-ANISOU 1003  N   ASP A 807     4286   4345   4170    238   -431   -215       N  
-ATOM   1004  CA  ASP A 807     -62.299  10.611 -29.376  1.00 35.30           C  
-ANISOU 1004  CA  ASP A 807     4502   4544   4365    263   -457   -194       C  
-ATOM   1005  C   ASP A 807     -62.933  11.431 -28.291  1.00 32.18           C  
-ANISOU 1005  C   ASP A 807     4081   4126   4020    256   -450   -188       C  
-ATOM   1006  O   ASP A 807     -63.506  12.456 -28.585  1.00 34.88           O  
-ANISOU 1006  O   ASP A 807     4431   4461   4363    278   -472   -174       O  
-ATOM   1007  CB  ASP A 807     -63.420  10.280 -30.384  1.00 38.19           C  
-ANISOU 1007  CB  ASP A 807     4864   4925   4723    293   -513   -222       C  
-ATOM   1008  CG  ASP A 807     -62.921   9.517 -31.597  1.00 42.74           C  
-ANISOU 1008  CG  ASP A 807     5469   5528   5244    308   -527   -233       C  
-ATOM   1009  OD1 ASP A 807     -61.757   9.750 -32.036  1.00 48.20           O  
-ANISOU 1009  OD1 ASP A 807     6196   6230   5887    308   -499   -204       O  
-ATOM   1010  OD2 ASP A 807     -63.683   8.671 -32.108  1.00 46.20           O  
-ANISOU 1010  OD2 ASP A 807     5891   5977   5687    321   -567   -273       O  
-ATOM   1011  N   SER A 808     -62.851  11.001 -27.036  1.00 33.38           N  
-ANISOU 1011  N   SER A 808     4203   4267   4213    228   -421   -200       N  
-ATOM   1012  CA  SER A 808     -63.433  11.760 -25.906  1.00 30.74           C  
-ANISOU 1012  CA  SER A 808     3842   3913   3924    222   -411   -198       C  
-ATOM   1013  C   SER A 808     -62.594  12.966 -25.566  1.00 31.36           C  
-ANISOU 1013  C   SER A 808     3945   3978   3994    220   -384   -161       C  
-ATOM   1014  O   SER A 808     -61.420  13.062 -25.928  1.00 29.64           O  
-ANISOU 1014  O   SER A 808     3757   3763   3741    214   -362   -138       O  
-ATOM   1015  CB  SER A 808     -63.557  10.856 -24.668  1.00 30.57           C  
-ANISOU 1015  CB  SER A 808     3784   3888   3943    193   -385   -220       C  
-ATOM   1016  OG  SER A 808     -62.281  10.434 -24.161  1.00 30.11           O  
-ANISOU 1016  OG  SER A 808     3740   3829   3871    170   -345   -207       O  
-ATOM   1017  N   GLU A 809     -63.178  13.879 -24.812  1.00 34.57           N  
-ANISOU 1017  N   GLU A 809     4334   4367   4434    224   -385   -159       N  
-ATOM   1018  CA  GLU A 809     -62.446  15.038 -24.318  1.00 35.07           C  
-ANISOU 1018  CA  GLU A 809     4414   4412   4500    221   -361   -130       C  
-ATOM   1019  C   GLU A 809     -61.486  14.601 -23.224  1.00 31.83           C  
-ANISOU 1019  C   GLU A 809     3997   3999   4099    191   -317   -131       C  
-ATOM   1020  O   GLU A 809     -60.398  15.162 -23.068  1.00 29.64           O  
-ANISOU 1020  O   GLU A 809     3741   3712   3810    182   -292   -107       O  
-ATOM   1021  CB  GLU A 809     -63.421  16.127 -23.803  1.00 40.64           C  
-ANISOU 1021  CB  GLU A 809     5100   5098   5242    238   -378   -133       C  
-ATOM   1022  CG  GLU A 809     -62.788  17.384 -23.174  1.00 47.58           C  
-ANISOU 1022  CG  GLU A 809     5992   5952   6134    235   -358   -109       C  
-ATOM   1023  CD  GLU A 809     -61.710  18.020 -24.025  1.00 51.40           C  
-ANISOU 1023  CD  GLU A 809     6520   6427   6582    237   -350    -69       C  
-ATOM   1024  OE1 GLU A 809     -61.645  17.708 -25.228  1.00 57.56           O  
-ANISOU 1024  OE1 GLU A 809     7324   7222   7324    248   -368    -57       O  
-ATOM   1025  OE2 GLU A 809     -60.961  18.870 -23.498  1.00 56.58           O  
-ANISOU 1025  OE2 GLU A 809     7186   7062   7250    227   -328    -50       O  
-ATOM   1026  N   GLU A 810     -61.897  13.600 -22.466  1.00 29.72           N  
-ANISOU 1026  N   GLU A 810     3698   3740   3855    176   -308   -159       N  
-ATOM   1027  CA  GLU A 810     -61.052  12.997 -21.444  1.00 30.27           C  
-ANISOU 1027  CA  GLU A 810     3761   3809   3930    150   -271   -161       C  
-ATOM   1028  C   GLU A 810     -59.715  12.569 -22.084  1.00 27.93           C  
-ANISOU 1028  C   GLU A 810     3496   3520   3596    141   -255   -145       C  
-ATOM   1029  O   GLU A 810     -58.628  12.927 -21.608  1.00 27.93           O  
-ANISOU 1029  O   GLU A 810     3508   3513   3590    129   -227   -130       O  
-ATOM   1030  CB  GLU A 810     -61.800  11.800 -20.847  1.00 32.92           C  
-ANISOU 1030  CB  GLU A 810     4063   4154   4291    138   -270   -190       C  
-ATOM   1031  CG  GLU A 810     -61.257  11.211 -19.558  1.00 35.11           C  
-ANISOU 1031  CG  GLU A 810     4327   4430   4582    114   -234   -194       C  
-ATOM   1032  CD  GLU A 810     -62.220  10.204 -18.938  1.00 36.16           C  
-ANISOU 1032  CD  GLU A 810     4425   4569   4745    103   -233   -218       C  
-ATOM   1033  OE1 GLU A 810     -63.082   9.628 -19.674  1.00 37.75           O  
-ANISOU 1033  OE1 GLU A 810     4612   4776   4955    108   -261   -234       O  
-ATOM   1034  OE2 GLU A 810     -62.123   9.989 -17.711  1.00 38.71           O  
-ANISOU 1034  OE2 GLU A 810     4732   4891   5084     88   -205   -220       O  
-ATOM   1035  N   ALA A 811     -59.793  11.820 -23.185  1.00 25.70           N  
-ANISOU 1035  N   ALA A 811     3224   3253   3287    148   -274   -152       N  
-ATOM   1036  CA  ALA A 811     -58.578  11.342 -23.848  1.00 26.08           C  
-ANISOU 1036  CA  ALA A 811     3300   3313   3298    142   -259   -141       C  
-ATOM   1037  C   ALA A 811     -57.728  12.510 -24.352  1.00 26.65           C  
-ANISOU 1037  C   ALA A 811     3403   3379   3345    149   -247   -106       C  
-ATOM   1038  O   ALA A 811     -56.497  12.471 -24.325  1.00 23.80           O  
-ANISOU 1038  O   ALA A 811     3056   3019   2968    136   -219    -92       O  
-ATOM   1039  CB  ALA A 811     -58.927  10.404 -24.998  1.00 26.22           C  
-ANISOU 1039  CB  ALA A 811     3324   3350   3290    155   -286   -158       C  
-ATOM   1040  N   GLU A 812     -58.400  13.546 -24.828  1.00 27.67           N  
-ANISOU 1040  N   GLU A 812     3540   3499   3474    168   -270    -91       N  
-ATOM   1041  CA  GLU A 812     -57.722  14.696 -25.384  1.00 28.19           C  
-ANISOU 1041  CA  GLU A 812     3636   3555   3520    175   -262    -53       C  
-ATOM   1042  C   GLU A 812     -56.901  15.391 -24.318  1.00 25.89           C  
-ANISOU 1042  C   GLU A 812     3340   3242   3255    156   -229    -40       C  
-ATOM   1043  O   GLU A 812     -55.757  15.797 -24.576  1.00 26.52           O  
-ANISOU 1043  O   GLU A 812     3440   3319   3318    146   -205    -15       O  
-ATOM   1044  CB  GLU A 812     -58.755  15.622 -26.059  1.00 30.07           C  
-ANISOU 1044  CB  GLU A 812     3883   3785   3757    203   -298    -41       C  
-ATOM   1045  CG  GLU A 812     -58.312  17.024 -26.425  1.00 33.32           C  
-ANISOU 1045  CG  GLU A 812     4322   4175   4161    210   -294      1       C  
-ATOM   1046  CD  GLU A 812     -57.213  17.062 -27.484  1.00 35.13           C  
-ANISOU 1046  CD  GLU A 812     4588   4417   4341    209   -275     34       C  
-ATOM   1047  OE1 GLU A 812     -56.928  16.050 -28.146  1.00 37.56           O  
-ANISOU 1047  OE1 GLU A 812     4904   4754   4613    210   -274     23       O  
-ATOM   1048  OE2 GLU A 812     -56.623  18.135 -27.655  1.00 40.36           O  
-ANISOU 1048  OE2 GLU A 812     5271   5060   5003    207   -261     72       O  
-ATOM   1049  N   ILE A 813     -57.509  15.576 -23.153  1.00 25.29           N  
-ANISOU 1049  N   ILE A 813     3236   3153   3219    151   -230    -59       N  
-ATOM   1050  CA  ILE A 813     -56.831  16.175 -22.014  1.00 25.22           C  
-ANISOU 1050  CA  ILE A 813     3219   3125   3237    136   -204    -55       C  
-ATOM   1051  C   ILE A 813     -55.570  15.345 -21.676  1.00 24.51           C  
-ANISOU 1051  C   ILE A 813     3131   3046   3135    113   -172    -58       C  
-ATOM   1052  O   ILE A 813     -54.472  15.887 -21.521  1.00 24.04           O  
-ANISOU 1052  O   ILE A 813     3083   2976   3076    102   -150    -41       O  
-ATOM   1053  CB  ILE A 813     -57.715  16.187 -20.765  1.00 26.35           C  
-ANISOU 1053  CB  ILE A 813     3331   3263   3419    136   -207    -82       C  
-ATOM   1054  CG1 ILE A 813     -58.986  17.026 -20.927  1.00 31.24           C  
-ANISOU 1054  CG1 ILE A 813     3942   3871   4058    159   -238    -85       C  
-ATOM   1055  CG2 ILE A 813     -56.973  16.706 -19.538  1.00 25.59           C  
-ANISOU 1055  CG2 ILE A 813     3227   3151   3346    122   -182    -84       C  
-ATOM   1056  CD1 ILE A 813     -58.715  18.471 -21.119  1.00 34.63           C  
-ANISOU 1056  CD1 ILE A 813     4389   4273   4496    169   -243    -60       C  
-ATOM   1057  N   ILE A 814     -55.730  14.029 -21.619  1.00 22.13           N  
-ANISOU 1057  N   ILE A 814     2819   2765   2826    108   -172    -81       N  
-ATOM   1058  CA  ILE A 814     -54.617  13.160 -21.288  1.00 22.14           C  
-ANISOU 1058  CA  ILE A 814     2821   2775   2818     90   -147    -87       C  
-ATOM   1059  C   ILE A 814     -53.493  13.187 -22.343  1.00 21.84           C  
-ANISOU 1059  C   ILE A 814     2809   2746   2745     88   -134    -66       C  
-ATOM   1060  O   ILE A 814     -52.316  13.248 -21.990  1.00 21.80           O  
-ANISOU 1060  O   ILE A 814     2806   2738   2740     74   -107    -59       O  
-ATOM   1061  CB  ILE A 814     -55.119  11.745 -21.030  1.00 21.77           C  
-ANISOU 1061  CB  ILE A 814     2756   2742   2773     85   -153   -115       C  
-ATOM   1062  CG1 ILE A 814     -55.891  11.748 -19.723  1.00 21.75           C  
-ANISOU 1062  CG1 ILE A 814     2727   2731   2806     80   -151   -131       C  
-ATOM   1063  CG2 ILE A 814     -53.939  10.777 -20.987  1.00 22.34           C  
-ANISOU 1063  CG2 ILE A 814     2834   2824   2830     71   -132   -120       C  
-ATOM   1064  CD1 ILE A 814     -56.615  10.469 -19.422  1.00 24.16           C  
-ANISOU 1064  CD1 ILE A 814     3012   3046   3122     75   -158   -154       C  
-ATOM   1065  N   ARG A 815     -53.852  13.223 -23.628  1.00 22.51           N  
-ANISOU 1065  N   ARG A 815     2912   2843   2799    104   -151    -55       N  
-ATOM   1066  CA  ARG A 815     -52.854  13.348 -24.704  1.00 23.29           C  
-ANISOU 1066  CA  ARG A 815     3036   2954   2859    105   -137    -32       C  
-ATOM   1067  C   ARG A 815     -52.138  14.676 -24.620  1.00 22.64           C  
-ANISOU 1067  C   ARG A 815     2965   2851   2785     98   -117      2       C  
-ATOM   1068  O   ARG A 815     -50.961  14.750 -24.905  1.00 22.09           O  
-ANISOU 1068  O   ARG A 815     2906   2787   2702     87    -90     18       O  
-ATOM   1069  CB  ARG A 815     -53.465  13.142 -26.098  1.00 24.70           C  
-ANISOU 1069  CB  ARG A 815     3235   3152   2998    128   -162    -28       C  
-ATOM   1070  CG  ARG A 815     -53.774  11.690 -26.424  1.00 27.52           C  
-ANISOU 1070  CG  ARG A 815     3584   3532   3340    133   -177    -62       C  
-ATOM   1071  CD  ARG A 815     -54.169  11.519 -27.891  1.00 32.13           C  
-ANISOU 1071  CD  ARG A 815     4191   4139   3878    158   -201    -59       C  
-ATOM   1072  NE  ARG A 815     -55.281  12.407 -28.223  1.00 32.85           N  
-ANISOU 1072  NE  ARG A 815     4289   4221   3974    177   -232    -47       N  
-ATOM   1073  CZ  ARG A 815     -56.563  12.055 -28.280  1.00 30.53           C  
-ANISOU 1073  CZ  ARG A 815     3979   3927   3693    191   -270    -72       C  
-ATOM   1074  NH1 ARG A 815     -57.460  12.977 -28.542  1.00 29.99           N  
-ANISOU 1074  NH1 ARG A 815     3916   3849   3631    210   -297    -59       N  
-ATOM   1075  NH2 ARG A 815     -56.942  10.810 -28.076  1.00 30.88           N  
-ANISOU 1075  NH2 ARG A 815     4003   3982   3750    187   -282   -110       N  
-ATOM   1076  N   LYS A 816     -52.845  15.714 -24.231  1.00 24.36           N  
-ANISOU 1076  N   LYS A 816     3181   3046   3031    105   -132     11       N  
-ATOM   1077  CA  LYS A 816     -52.236  17.029 -24.063  1.00 27.24           C  
-ANISOU 1077  CA  LYS A 816     3553   3383   3413     98   -117     41       C  
-ATOM   1078  C   LYS A 816     -51.201  16.991 -22.949  1.00 25.59           C  
-ANISOU 1078  C   LYS A 816     3328   3164   3232     75    -89     31       C  
-ATOM   1079  O   LYS A 816     -50.088  17.491 -23.092  1.00 25.68           O  
-ANISOU 1079  O   LYS A 816     3346   3167   3245     61    -64     52       O  
-ATOM   1080  CB  LYS A 816     -53.329  18.026 -23.676  1.00 32.01           C  
-ANISOU 1080  CB  LYS A 816     4153   3962   4048    112   -143     43       C  
-ATOM   1081  CG  LYS A 816     -53.685  19.085 -24.687  1.00 39.15           C  
-ANISOU 1081  CG  LYS A 816     5084   4853   4940    129   -160     79       C  
-ATOM   1082  CD  LYS A 816     -54.779  19.952 -24.077  1.00 44.17           C  
-ANISOU 1082  CD  LYS A 816     5707   5462   5614    143   -187     71       C  
-ATOM   1083  CE  LYS A 816     -55.241  21.032 -25.007  1.00 50.40           C  
-ANISOU 1083  CE  LYS A 816     6522   6232   6395    164   -209    106       C  
-ATOM   1084  NZ  LYS A 816     -56.148  20.434 -26.018  1.00 54.47           N  
-ANISOU 1084  NZ  LYS A 816     7048   6774   6874    188   -239    102       N  
-ATOM   1085  N   TYR A 817     -51.569  16.355 -21.844  1.00 24.20           N  
-ANISOU 1085  N   TYR A 817     3128   2990   3077     71    -93     -2       N  
-ATOM   1086  CA  TYR A 817     -50.668  16.252 -20.713  1.00 22.80           C  
-ANISOU 1086  CA  TYR A 817     2934   2805   2923     53    -71    -16       C  
-ATOM   1087  C   TYR A 817     -49.380  15.549 -21.156  1.00 23.18           C  
-ANISOU 1087  C   TYR A 817     2988   2870   2949     40    -46    -12       C  
-ATOM   1088  O   TYR A 817     -48.288  16.028 -20.876  1.00 23.92           O  
-ANISOU 1088  O   TYR A 817     3080   2953   3056     26    -25     -3       O  
-ATOM   1089  CB  TYR A 817     -51.349  15.477 -19.612  1.00 20.52           C  
-ANISOU 1089  CB  TYR A 817     2624   2523   2650     54    -79    -49       C  
-ATOM   1090  CG  TYR A 817     -50.763  15.595 -18.231  1.00 19.90           C  
-ANISOU 1090  CG  TYR A 817     2529   2434   2598     42    -65    -66       C  
-ATOM   1091  CD1 TYR A 817     -49.672  16.418 -17.933  1.00 19.14           C  
-ANISOU 1091  CD1 TYR A 817     2435   2321   2519     32    -49    -56       C  
-ATOM   1092  CD2 TYR A 817     -51.348  14.886 -17.188  1.00 18.93           C  
-ANISOU 1092  CD2 TYR A 817     2388   2318   2485     43    -68    -92       C  
-ATOM   1093  CE1 TYR A 817     -49.200  16.508 -16.631  1.00 19.43           C  
-ANISOU 1093  CE1 TYR A 817     2455   2349   2578     25    -42    -75       C  
-ATOM   1094  CE2 TYR A 817     -50.903  14.993 -15.913  1.00 18.58           C  
-ANISOU 1094  CE2 TYR A 817     2331   2268   2459     38    -58   -107       C  
-ATOM   1095  CZ  TYR A 817     -49.830  15.787 -15.631  1.00 18.79           C  
-ANISOU 1095  CZ  TYR A 817     2361   2279   2500     30    -47   -101       C  
-ATOM   1096  OH  TYR A 817     -49.449  15.820 -14.308  1.00 20.04           O  
-ANISOU 1096  OH  TYR A 817     2506   2434   2675     27    -41   -121       O  
-ATOM   1097  N   VAL A 818     -49.524  14.464 -21.912  1.00 22.90           N  
-ANISOU 1097  N   VAL A 818     2959   2861   2880     46    -50    -20       N  
-ATOM   1098  CA  VAL A 818     -48.347  13.736 -22.446  1.00 24.21           C  
-ANISOU 1098  CA  VAL A 818     3130   3047   3022     38    -28    -20       C  
-ATOM   1099  C   VAL A 818     -47.488  14.596 -23.383  1.00 26.10           C  
-ANISOU 1099  C   VAL A 818     3387   3285   3245     34     -7     16       C  
-ATOM   1100  O   VAL A 818     -46.287  14.703 -23.223  1.00 25.66           O  
-ANISOU 1100  O   VAL A 818     3325   3228   3197     18     20     21       O  
-ATOM   1101  CB  VAL A 818     -48.743  12.475 -23.203  1.00 23.37           C  
-ANISOU 1101  CB  VAL A 818     3030   2968   2883     49    -40    -37       C  
-ATOM   1102  CG1 VAL A 818     -47.539  11.860 -23.889  1.00 22.83           C  
-ANISOU 1102  CG1 VAL A 818     2968   2921   2787     45    -16    -36       C  
-ATOM   1103  CG2 VAL A 818     -49.395  11.469 -22.259  1.00 22.46           C  
-ANISOU 1103  CG2 VAL A 818     2894   2852   2786     48    -54    -69       C  
-ATOM   1104  N   LYS A 819     -48.139  15.281 -24.304  1.00 27.54           N  
-ANISOU 1104  N   LYS A 819     3589   3465   3409     47    -20     41       N  
-ATOM   1105  CA  LYS A 819     -47.444  16.084 -25.286  1.00 29.42           C  
-ANISOU 1105  CA  LYS A 819     3848   3703   3629     44      0     81       C  
-ATOM   1106  C   LYS A 819     -46.724  17.302 -24.689  1.00 29.22           C  
-ANISOU 1106  C   LYS A 819     3816   3644   3644     26     19    103       C  
-ATOM   1107  O   LYS A 819     -45.598  17.588 -25.031  1.00 29.69           O  
-ANISOU 1107  O   LYS A 819     3877   3705   3701     11     50    123       O  
-ATOM   1108  CB  LYS A 819     -48.443  16.553 -26.344  1.00 30.71           C  
-ANISOU 1108  CB  LYS A 819     4037   3870   3763     66    -24    104       C  
-ATOM   1109  CG  LYS A 819     -47.843  17.142 -27.598  1.00 33.40           C  
-ANISOU 1109  CG  LYS A 819     4405   4219   4067     69     -4    148       C  
-ATOM   1110  CD  LYS A 819     -48.882  18.052 -28.242  1.00 37.27           C  
-ANISOU 1110  CD  LYS A 819     4919   4695   4547     89    -32    177       C  
-ATOM   1111  CE  LYS A 819     -48.548  18.422 -29.672  1.00 42.38           C  
-ANISOU 1111  CE  LYS A 819     5600   5360   5142    100    -19    221       C  
-ATOM   1112  NZ  LYS A 819     -47.801  19.696 -29.743  1.00 44.55           N  
-ANISOU 1112  NZ  LYS A 819     5885   5605   5438     83      9    269       N  
-ATOM   1113  N   ASN A 820     -47.416  18.044 -23.846  1.00 27.95           N  
-ANISOU 1113  N   ASN A 820     3646   3453   3520     27      0     97       N  
-ATOM   1114  CA  ASN A 820     -46.884  19.278 -23.328  1.00 26.95           C  
-ANISOU 1114  CA  ASN A 820     3515   3291   3436     13     10    116       C  
-ATOM   1115  C   ASN A 820     -45.837  19.127 -22.273  1.00 25.22           C  
-ANISOU 1115  C   ASN A 820     3270   3063   3248     -7     29     93       C  
-ATOM   1116  O   ASN A 820     -45.082  20.061 -22.081  1.00 25.41           O  
-ANISOU 1116  O   ASN A 820     3289   3061   3304    -23     44    111       O  
-ATOM   1117  CB  ASN A 820     -48.006  20.103 -22.733  1.00 27.66           C  
-ANISOU 1117  CB  ASN A 820     3602   3352   3556     26    -20    111       C  
-ATOM   1118  CG  ASN A 820     -48.908  20.673 -23.779  1.00 29.13           C  
-ANISOU 1118  CG  ASN A 820     3813   3533   3721     45    -40    141       C  
-ATOM   1119  OD1 ASN A 820     -48.590  20.665 -24.963  1.00 31.69           O  
-ANISOU 1119  OD1 ASN A 820     4161   3872   4008     48    -29    172       O  
-ATOM   1120  ND2 ASN A 820     -50.023  21.244 -23.343  1.00 31.00           N  
-ANISOU 1120  ND2 ASN A 820     4047   3749   3981     61    -70    132       N  
-ATOM   1121  N   THR A 821     -45.806  18.005 -21.547  1.00 22.94           N  
-ANISOU 1121  N   THR A 821     2966   2795   2957     -7     27     56       N  
-ATOM   1122  CA  THR A 821     -44.899  17.904 -20.405  1.00 22.16           C  
-ANISOU 1122  CA  THR A 821     2843   2688   2889    -22     39     32       C  
-ATOM   1123  C   THR A 821     -43.729  16.935 -20.661  1.00 23.55           C  
-ANISOU 1123  C   THR A 821     3012   2890   3047    -32     63     23       C  
-ATOM   1124  O   THR A 821     -43.082  16.487 -19.744  1.00 22.69           O  
-ANISOU 1124  O   THR A 821     2883   2781   2955    -40     68     -3       O  
-ATOM   1125  CB  THR A 821     -45.644  17.547 -19.130  1.00 21.84           C  
-ANISOU 1125  CB  THR A 821     2788   2644   2867    -14     18     -3       C  
-ATOM   1126  OG1 THR A 821     -46.096  16.180 -19.165  1.00 21.74           O  
-ANISOU 1126  OG1 THR A 821     2775   2661   2826     -5     11    -24       O  
-ATOM   1127  CG2 THR A 821     -46.844  18.503 -18.911  1.00 21.40           C  
-ANISOU 1127  CG2 THR A 821     2736   2565   2829     -1     -6      2       C  
-ATOM   1128  N   HIS A 822     -43.455  16.637 -21.928  1.00 25.31           N  
-ANISOU 1128  N   HIS A 822     3250   3134   3233    -30     78     45       N  
-ATOM   1129  CA  HIS A 822     -42.258  15.899 -22.294  1.00 27.59           C  
-ANISOU 1129  CA  HIS A 822     3531   3446   3506    -40    105     39       C  
-ATOM   1130  C   HIS A 822     -41.085  16.868 -22.157  1.00 29.56           C  
-ANISOU 1130  C   HIS A 822     3767   3675   3789    -61    131     57       C  
-ATOM   1131  O   HIS A 822     -41.079  17.891 -22.789  1.00 30.06           O  
-ANISOU 1131  O   HIS A 822     3843   3722   3857    -67    141     94       O  
-ATOM   1132  CB  HIS A 822     -42.318  15.368 -23.731  1.00 28.02           C  
-ANISOU 1132  CB  HIS A 822     3606   3533   3508    -29    115     56       C  
-ATOM   1133  CG  HIS A 822     -41.230  14.389 -24.036  1.00 28.80           C  
-ANISOU 1133  CG  HIS A 822     3694   3661   3589    -33    138     40       C  
-ATOM   1134  ND1 HIS A 822     -41.487  13.103 -24.456  1.00 31.59           N  
-ANISOU 1134  ND1 HIS A 822     4053   4044   3907    -17    129     16       N  
-ATOM   1135  CD2 HIS A 822     -39.890  14.472 -23.893  1.00 28.58           C  
-ANISOU 1135  CD2 HIS A 822     3647   3633   3578    -49    168     39       C  
-ATOM   1136  CE1 HIS A 822     -40.356  12.434 -24.560  1.00 29.68           C  
-ANISOU 1136  CE1 HIS A 822     3797   3821   3660    -23    152      1       C  
-ATOM   1137  NE2 HIS A 822     -39.369  13.246 -24.233  1.00 29.16           N  
-ANISOU 1137  NE2 HIS A 822     3715   3739   3625    -42    177     15       N  
-ATOM   1138  N   ALA A 823     -40.127  16.576 -21.290  1.00 31.31           N  
-ANISOU 1138  N   ALA A 823     3964   3895   4039    -73    140     32       N  
-ATOM   1139  CA  ALA A 823     -39.049  17.514 -21.011  1.00 32.90           C  
-ANISOU 1139  CA  ALA A 823     4146   4071   4281    -95    161     43       C  
-ATOM   1140  C   ALA A 823     -38.074  17.631 -22.187  1.00 35.95           C  
-ANISOU 1140  C   ALA A 823     4534   4474   4652   -108    199     73       C  
-ATOM   1141  O   ALA A 823     -37.794  16.638 -22.859  1.00 35.82           O  
-ANISOU 1141  O   ALA A 823     4521   4494   4596   -100    212     66       O  
-ATOM   1142  CB  ALA A 823     -38.287  17.092 -19.762  1.00 31.00           C  
-ANISOU 1142  CB  ALA A 823     3877   3827   4073   -101    156      3       C  
-ATOM   1143  N   THR A 824     -37.548  18.846 -22.389  1.00 38.66           N  
-ANISOU 1143  N   THR A 824     4873   4789   5028   -127    217    104       N  
-ATOM   1144  CA  THR A 824     -36.578  19.124 -23.481  1.00 40.50           C  
-ANISOU 1144  CA  THR A 824     5104   5034   5250   -143    260    139       C  
-ATOM   1145  C   THR A 824     -35.307  18.305 -23.378  1.00 37.04           C  
-ANISOU 1145  C   THR A 824     4637   4622   4815   -152    286    113       C  
-ATOM   1146  O   THR A 824     -34.739  18.011 -24.400  1.00 39.32           O  
-ANISOU 1146  O   THR A 824     4929   4940   5072   -155    319    132       O  
-ATOM   1147  CB  THR A 824     -36.119  20.602 -23.578  1.00 40.32           C  
-ANISOU 1147  CB  THR A 824     5076   4970   5274   -168    278    178       C  
-ATOM   1148  OG1 THR A 824     -35.418  20.976 -22.382  1.00 43.34           O  
-ANISOU 1148  OG1 THR A 824     5425   5324   5720   -185    271    148       O  
-ATOM   1149  CG2 THR A 824     -37.308  21.525 -23.817  1.00 40.95           C  
-ANISOU 1149  CG2 THR A 824     5186   5020   5352   -158    254    209       C  
-ATOM   1150  N   THR A 825     -34.861  17.941 -22.169  1.00 34.24           N  
-ANISOU 1150  N   THR A 825     4255   4259   4496   -155    270     70       N  
-ATOM   1151  CA  THR A 825     -33.632  17.140 -21.995  1.00 35.18           C  
-ANISOU 1151  CA  THR A 825     4343   4401   4622   -161    289     41       C  
-ATOM   1152  C   THR A 825     -33.807  15.636 -22.067  1.00 33.37           C  
-ANISOU 1152  C   THR A 825     4119   4210   4349   -138    279      9       C  
-ATOM   1153  O   THR A 825     -32.838  14.904 -21.937  1.00 31.98           O  
-ANISOU 1153  O   THR A 825     3920   4053   4178   -139    292    -17       O  
-ATOM   1154  CB  THR A 825     -32.953  17.426 -20.644  1.00 37.50           C  
-ANISOU 1154  CB  THR A 825     4604   4669   4977   -172    275      8       C  
-ATOM   1155  OG1 THR A 825     -33.836  17.039 -19.580  1.00 38.91           O  
-ANISOU 1155  OG1 THR A 825     4791   4839   5154   -154    233    -23       O  
-ATOM   1156  CG2 THR A 825     -32.591  18.922 -20.538  1.00 39.44           C  
-ANISOU 1156  CG2 THR A 825     4838   4872   5276   -198    286     34       C  
-ATOM   1157  N   HIS A 826     -35.038  15.160 -22.227  1.00 34.20           N  
-ANISOU 1157  N   HIS A 826     4254   4324   4418   -118    254      8       N  
-ATOM   1158  CA  HIS A 826     -35.303  13.725 -22.360  1.00 33.58           C  
-ANISOU 1158  CA  HIS A 826     4182   4277   4300    -97    241    -21       C  
-ATOM   1159  C   HIS A 826     -35.548  13.426 -23.841  1.00 37.32           C  
-ANISOU 1159  C   HIS A 826     4679   4782   4719    -86    260      3       C  
-ATOM   1160  O   HIS A 826     -36.645  13.033 -24.245  1.00 42.24           O  
-ANISOU 1160  O   HIS A 826     5327   5414   5307    -68    238      4       O  
-ATOM   1161  CB  HIS A 826     -36.481  13.311 -21.491  1.00 30.74           C  
-ANISOU 1161  CB  HIS A 826     3833   3905   3939    -82    201    -41       C  
-ATOM   1162  CG  HIS A 826     -36.224  13.505 -20.028  1.00 31.85           C  
-ANISOU 1162  CG  HIS A 826     3955   4022   4126    -87    183    -67       C  
-ATOM   1163  ND1 HIS A 826     -37.211  13.851 -19.133  1.00 27.52           N  
-ANISOU 1163  ND1 HIS A 826     3413   3451   3591    -82    154    -73       N  
-ATOM   1164  CD2 HIS A 826     -35.071  13.442 -19.317  1.00 29.36           C  
-ANISOU 1164  CD2 HIS A 826     3610   3702   3843    -97    190    -89       C  
-ATOM   1165  CE1 HIS A 826     -36.672  13.991 -17.936  1.00 28.70           C  
-ANISOU 1165  CE1 HIS A 826     3542   3585   3776    -86    145    -97       C  
-ATOM   1166  NE2 HIS A 826     -35.381  13.737 -18.021  1.00 27.57           N  
-ANISOU 1166  NE2 HIS A 826     3377   3451   3646    -95    164   -108       N  
-ATOM   1167  N   ASN A 827     -34.501  13.591 -24.630  1.00 38.18           N  
-ANISOU 1167  N   ASN A 827     4777   4910   4821    -97    299     18       N  
-ATOM   1168  CA  ASN A 827     -34.593  13.503 -26.086  1.00 42.04           C  
-ANISOU 1168  CA  ASN A 827     5288   5430   5255    -88    323     46       C  
-ATOM   1169  C   ASN A 827     -34.368  12.149 -26.701  1.00 37.93           C  
-ANISOU 1169  C   ASN A 827     4769   4953   4691    -67    327     16       C  
-ATOM   1170  O   ASN A 827     -34.432  12.038 -27.913  1.00 39.97           O  
-ANISOU 1170  O   ASN A 827     5047   5242   4900    -56    346     35       O  
-ATOM   1171  CB  ASN A 827     -33.506  14.343 -26.726  1.00 47.97           C  
-ANISOU 1171  CB  ASN A 827     6025   6184   6017   -110    372     80       C  
-ATOM   1172  CG  ASN A 827     -33.573  15.782 -26.331  1.00 55.94           C  
-ANISOU 1172  CG  ASN A 827     7033   7150   7072   -133    374    115       C  
-ATOM   1173  OD1 ASN A 827     -32.783  16.240 -25.505  1.00 66.56           O  
-ANISOU 1173  OD1 ASN A 827     8346   8469   8473   -154    381    105       O  
-ATOM   1174  ND2 ASN A 827     -34.518  16.514 -26.902  1.00 61.90           N  
-ANISOU 1174  ND2 ASN A 827     7821   7892   7806   -128    366    154       N  
-ATOM   1175  N   ALA A 828     -34.030  11.164 -25.889  1.00 35.39           N  
-ANISOU 1175  N   ALA A 828     4427   4633   4387    -61    310    -29       N  
-ATOM   1176  CA  ALA A 828     -33.809   9.821 -26.366  1.00 34.84           C  
-ANISOU 1176  CA  ALA A 828     4357   4598   4283    -40    309    -62       C  
-ATOM   1177  C   ALA A 828     -35.042   9.179 -27.050  1.00 35.57           C  
-ANISOU 1177  C   ALA A 828     4483   4706   4327    -15    282    -66       C  
-ATOM   1178  O   ALA A 828     -34.878   8.210 -27.798  1.00 36.35           O  
-ANISOU 1178  O   ALA A 828     4586   4838   4387      3    285    -88       O  
-ATOM   1179  CB  ALA A 828     -33.333   8.940 -25.215  1.00 32.97           C  
-ANISOU 1179  CB  ALA A 828     4095   4351   4081    -38    289   -107       C  
-ATOM   1180  N   TYR A 829     -36.250   9.711 -26.812  1.00 32.97           N  
-ANISOU 1180  N   TYR A 829     4175   4354   3999    -15    254    -49       N  
-ATOM   1181  CA  TYR A 829     -37.465   9.130 -27.394  1.00 33.03           C  
-ANISOU 1181  CA  TYR A 829     4210   4373   3968      8    224    -55       C  
-ATOM   1182  C   TYR A 829     -38.607  10.148 -27.479  1.00 33.73           C  
-ANISOU 1182  C   TYR A 829     4321   4440   4055      7    207    -21       C  
-ATOM   1183  O   TYR A 829     -38.532  11.216 -26.879  1.00 35.10           O  
-ANISOU 1183  O   TYR A 829     4488   4585   4264    -11    212      2       O  
-ATOM   1184  CB  TYR A 829     -37.914   7.917 -26.565  1.00 32.21           C  
-ANISOU 1184  CB  TYR A 829     4098   4261   3879     18    189    -99       C  
-ATOM   1185  CG  TYR A 829     -38.165   8.233 -25.096  1.00 30.25           C  
-ANISOU 1185  CG  TYR A 829     3837   3977   3682      4    171   -104       C  
-ATOM   1186  CD1 TYR A 829     -39.348   8.833 -24.695  1.00 28.90           C  
-ANISOU 1186  CD1 TYR A 829     3678   3782   3521      3    147    -90       C  
-ATOM   1187  CD2 TYR A 829     -37.193   7.995 -24.126  1.00 29.47           C  
-ANISOU 1187  CD2 TYR A 829     3711   3867   3619     -6    178   -124       C  
-ATOM   1188  CE1 TYR A 829     -39.575   9.157 -23.372  1.00 28.75           C  
-ANISOU 1188  CE1 TYR A 829     3646   3733   3544     -7    132    -95       C  
-ATOM   1189  CE2 TYR A 829     -37.416   8.322 -22.807  1.00 29.18           C  
-ANISOU 1189  CE2 TYR A 829     3664   3800   3623    -16    161   -129       C  
-ATOM   1190  CZ  TYR A 829     -38.635   8.883 -22.436  1.00 28.49           C  
-ANISOU 1190  CZ  TYR A 829     3591   3693   3541    -16    139   -115       C  
-ATOM   1191  OH  TYR A 829     -38.893   9.288 -21.141  1.00 27.71           O  
-ANISOU 1191  OH  TYR A 829     3483   3567   3479    -23    124   -120       O  
-ATOM   1192  N   ASP A 830     -39.613   9.848 -28.298  1.00 34.50           N  
-ANISOU 1192  N   ASP A 830     4444   4553   4111     27    185    -20       N  
-ATOM   1193  CA  ASP A 830     -40.916  10.503 -28.246  1.00 34.77           C  
-ANISOU 1193  CA  ASP A 830     4497   4567   4147     33    155     -1       C  
-ATOM   1194  C   ASP A 830     -41.905   9.512 -27.753  1.00 31.69           C  
-ANISOU 1194  C   ASP A 830     4105   4172   3763     45    116    -38       C  
-ATOM   1195  O   ASP A 830     -41.692   8.328 -27.881  1.00 31.94           O  
-ANISOU 1195  O   ASP A 830     4131   4223   3782     55    110    -71       O  
-ATOM   1196  CB  ASP A 830     -41.474  10.798 -29.641  1.00 40.92           C  
-ANISOU 1196  CB  ASP A 830     5308   5370   4871     52    154     25       C  
-ATOM   1197  CG  ASP A 830     -40.733  11.821 -30.370  1.00 48.25           C  
-ANISOU 1197  CG  ASP A 830     6246   6305   5782     42    192     70       C  
-ATOM   1198  OD1 ASP A 830     -40.198  12.756 -29.730  1.00 54.92           O  
-ANISOU 1198  OD1 ASP A 830     7076   7120   6669     18    211     93       O  
-ATOM   1199  OD2 ASP A 830     -40.691  11.679 -31.604  1.00 54.56           O  
-ANISOU 1199  OD2 ASP A 830     7067   7138   6525     60    203     83       O  
-ATOM   1200  N   LEU A 831     -43.037  10.005 -27.305  1.00 30.82           N  
-ANISOU 1200  N   LEU A 831     4000   4038   3670     46     88    -30       N  
-ATOM   1201  CA  LEU A 831     -44.031   9.154 -26.789  1.00 31.11           C  
-ANISOU 1201  CA  LEU A 831     4033   4069   3719     55     53    -61       C  
-ATOM   1202  C   LEU A 831     -45.244   9.202 -27.673  1.00 31.43           C  
-ANISOU 1202  C   LEU A 831     4094   4119   3729     75     24    -56       C  
-ATOM   1203  O   LEU A 831     -45.640  10.256 -28.136  1.00 31.90           O  
-ANISOU 1203  O   LEU A 831     4169   4173   3778     78     23    -23       O  
-ATOM   1204  CB  LEU A 831     -44.436   9.573 -25.389  1.00 30.17           C  
-ANISOU 1204  CB  LEU A 831     3897   3916   3649     41     42    -64       C  
-ATOM   1205  CG  LEU A 831     -43.392   9.281 -24.314  1.00 31.92           C  
-ANISOU 1205  CG  LEU A 831     4097   4128   3903     25     60    -79       C  
-ATOM   1206  CD1 LEU A 831     -43.750   9.966 -23.011  1.00 33.13           C  
-ANISOU 1206  CD1 LEU A 831     4237   4251   4098     14     52    -76       C  
-ATOM   1207  CD2 LEU A 831     -43.204   7.765 -24.083  1.00 33.57           C  
-ANISOU 1207  CD2 LEU A 831     4296   4349   4110     31     50   -116       C  
-ATOM   1208  N   GLU A 832     -45.891   8.057 -27.792  1.00 30.08           N  
-ANISOU 1208  N   GLU A 832     3921   3958   3551     88     -3    -90       N  
-ATOM   1209  CA  GLU A 832     -47.135   7.962 -28.478  1.00 32.88           C  
-ANISOU 1209  CA  GLU A 832     4289   4318   3885    107    -37    -95       C  
-ATOM   1210  C   GLU A 832     -48.100   7.175 -27.607  1.00 30.07           C  
-ANISOU 1210  C   GLU A 832     3915   3944   3565    105    -67   -125       C  
-ATOM   1211  O   GLU A 832     -47.801   6.054 -27.179  1.00 26.14           O  
-ANISOU 1211  O   GLU A 832     3403   3447   3080    100    -68   -155       O  
-ATOM   1212  CB  GLU A 832     -46.870   7.259 -29.806  1.00 36.33           C  
-ANISOU 1212  CB  GLU A 832     4743   4792   4268    128    -38   -108       C  
-ATOM   1213  CG  GLU A 832     -48.083   6.762 -30.536  1.00 42.26           C  
-ANISOU 1213  CG  GLU A 832     5505   5554   4998    152    -81   -128       C  
-ATOM   1214  CD  GLU A 832     -47.738   6.114 -31.876  1.00 50.27           C  
-ANISOU 1214  CD  GLU A 832     6539   6608   5955    176    -82   -144       C  
-ATOM   1215  OE1 GLU A 832     -46.572   5.650 -32.096  1.00 51.02           O  
-ANISOU 1215  OE1 GLU A 832     6632   6722   6033    174    -52   -152       O  
-ATOM   1216  OE2 GLU A 832     -48.676   6.065 -32.705  1.00 61.00           O  
-ANISOU 1216  OE2 GLU A 832     7912   7979   7285    199   -115   -151       O  
-ATOM   1217  N   VAL A 833     -49.273   7.763 -27.352  1.00 29.90           N  
-ANISOU 1217  N   VAL A 833     3892   3907   3561    107    -91   -117       N  
-ATOM   1218  CA  VAL A 833     -50.283   7.099 -26.527  1.00 28.24           C  
-ANISOU 1218  CA  VAL A 833     3662   3680   3386    104   -116   -143       C  
-ATOM   1219  C   VAL A 833     -50.972   6.074 -27.382  1.00 27.37           C  
-ANISOU 1219  C   VAL A 833     3555   3587   3258    121   -147   -173       C  
-ATOM   1220  O   VAL A 833     -51.516   6.400 -28.417  1.00 28.83           O  
-ANISOU 1220  O   VAL A 833     3756   3786   3411    140   -167   -167       O  
-ATOM   1221  CB  VAL A 833     -51.303   8.112 -25.956  1.00 27.17           C  
-ANISOU 1221  CB  VAL A 833     3520   3524   3278    102   -129   -127       C  
-ATOM   1222  CG1 VAL A 833     -52.399   7.412 -25.166  1.00 26.91           C  
-ANISOU 1222  CG1 VAL A 833     3465   3479   3282     98   -152   -153       C  
-ATOM   1223  CG2 VAL A 833     -50.586   9.123 -25.068  1.00 27.43           C  
-ANISOU 1223  CG2 VAL A 833     3549   3539   3334     86   -101   -103       C  
-ATOM   1224  N   ILE A 834     -50.996   4.839 -26.933  1.00 28.87           N  
-ANISOU 1224  N   ILE A 834     3729   3772   3467    115   -155   -204       N  
-ATOM   1225  CA  ILE A 834     -51.676   3.779 -27.682  1.00 29.40           C  
-ANISOU 1225  CA  ILE A 834     3796   3849   3525    130   -188   -238       C  
-ATOM   1226  C   ILE A 834     -53.066   3.596 -27.130  1.00 31.55           C  
-ANISOU 1226  C   ILE A 834     4048   4102   3836    126   -217   -250       C  
-ATOM   1227  O   ILE A 834     -54.027   3.717 -27.862  1.00 37.37           O  
-ANISOU 1227  O   ILE A 834     4788   4846   4564    142   -248   -258       O  
-ATOM   1228  CB  ILE A 834     -50.896   2.453 -27.602  1.00 28.97           C  
-ANISOU 1228  CB  ILE A 834     3735   3797   3473    127   -182   -267       C  
-ATOM   1229  CG1 ILE A 834     -49.558   2.605 -28.288  1.00 30.44           C  
-ANISOU 1229  CG1 ILE A 834     3939   4008   3618    134   -154   -259       C  
-ATOM   1230  CG2 ILE A 834     -51.678   1.313 -28.262  1.00 28.73           C  
-ANISOU 1230  CG2 ILE A 834     3701   3771   3443    141   -221   -307       C  
-ATOM   1231  CD1 ILE A 834     -48.636   1.436 -27.991  1.00 34.28           C  
-ANISOU 1231  CD1 ILE A 834     4416   4494   4115    130   -144   -286       C  
-ATOM   1232  N   ASP A 835     -53.162   3.277 -25.834  1.00 31.78           N  
-ANISOU 1232  N   ASP A 835     4056   4109   3910    105   -206   -252       N  
-ATOM   1233  CA  ASP A 835     -54.437   3.118 -25.146  1.00 30.61           C  
-ANISOU 1233  CA  ASP A 835     3885   3943   3804     97   -225   -261       C  
-ATOM   1234  C   ASP A 835     -54.446   3.907 -23.844  1.00 28.69           C  
-ANISOU 1234  C   ASP A 835     3629   3682   3588     80   -201   -238       C  
-ATOM   1235  O   ASP A 835     -53.428   4.025 -23.156  1.00 25.24           O  
-ANISOU 1235  O   ASP A 835     3197   3242   3152     69   -173   -226       O  
-ATOM   1236  CB  ASP A 835     -54.695   1.658 -24.796  1.00 33.50           C  
-ANISOU 1236  CB  ASP A 835     4234   4297   4199     87   -237   -291       C  
-ATOM   1237  CG  ASP A 835     -54.900   0.778 -26.023  1.00 39.32           C  
-ANISOU 1237  CG  ASP A 835     4977   5047   4917    104   -268   -323       C  
-ATOM   1238  OD1 ASP A 835     -54.260  -0.314 -26.059  1.00 40.89           O  
-ANISOU 1238  OD1 ASP A 835     5176   5242   5118    102   -267   -343       O  
-ATOM   1239  OD2 ASP A 835     -55.684   1.165 -26.935  1.00 35.92           O  
-ANISOU 1239  OD2 ASP A 835     4551   4628   4469    123   -296   -329       O  
-ATOM   1240  N   ILE A 836     -55.635   4.382 -23.484  1.00 27.64           N  
-ANISOU 1240  N   ILE A 836     3480   3541   3479     80   -215   -236       N  
-ATOM   1241  CA  ILE A 836     -55.881   5.019 -22.208  1.00 25.48           C  
-ANISOU 1241  CA  ILE A 836     3192   3253   3236     67   -197   -222       C  
-ATOM   1242  C   ILE A 836     -56.938   4.208 -21.483  1.00 24.98           C  
-ANISOU 1242  C   ILE A 836     3100   3179   3213     56   -207   -240       C  
-ATOM   1243  O   ILE A 836     -58.023   4.015 -21.984  1.00 26.24           O  
-ANISOU 1243  O   ILE A 836     3246   3339   3384     63   -234   -254       O  
-ATOM   1244  CB  ILE A 836     -56.363   6.452 -22.389  1.00 24.89           C  
-ANISOU 1244  CB  ILE A 836     3122   3178   3157     79   -202   -203       C  
-ATOM   1245  CG1 ILE A 836     -55.345   7.251 -23.199  1.00 25.30           C  
-ANISOU 1245  CG1 ILE A 836     3203   3239   3170     88   -192   -181       C  
-ATOM   1246  CG2 ILE A 836     -56.538   7.115 -21.039  1.00 26.02           C  
-ANISOU 1246  CG2 ILE A 836     3250   3308   3329     68   -183   -193       C  
-ATOM   1247  CD1 ILE A 836     -55.839   8.621 -23.622  1.00 24.93           C  
-ANISOU 1247  CD1 ILE A 836     3166   3189   3116    103   -202   -161       C  
-ATOM   1248  N   PHE A 837     -56.624   3.790 -20.270  1.00 24.21           N  
-ANISOU 1248  N   PHE A 837     2992   3070   3136     39   -183   -236       N  
-ATOM   1249  CA  PHE A 837     -57.543   3.077 -19.444  1.00 23.33           C  
-ANISOU 1249  CA  PHE A 837     2854   2948   3063     25   -184   -245       C  
-ATOM   1250  C   PHE A 837     -57.893   3.887 -18.206  1.00 22.83           C  
-ANISOU 1250  C   PHE A 837     2777   2880   3016     19   -163   -231       C  
-ATOM   1251  O   PHE A 837     -57.029   4.448 -17.546  1.00 21.24           O  
-ANISOU 1251  O   PHE A 837     2587   2679   2803     17   -140   -216       O  
-ATOM   1252  CB  PHE A 837     -56.909   1.738 -19.031  1.00 24.42           C  
-ANISOU 1252  CB  PHE A 837     2993   3076   3209     11   -175   -253       C  
-ATOM   1253  CG  PHE A 837     -56.490   0.866 -20.197  1.00 24.48           C  
-ANISOU 1253  CG  PHE A 837     3013   3088   3201     19   -196   -272       C  
-ATOM   1254  CD1 PHE A 837     -57.402   0.011 -20.806  1.00 24.52           C  
-ANISOU 1254  CD1 PHE A 837     3003   3087   3226     19   -224   -296       C  
-ATOM   1255  CD2 PHE A 837     -55.188   0.887 -20.656  1.00 24.67           C  
-ANISOU 1255  CD2 PHE A 837     3061   3121   3192     27   -186   -269       C  
-ATOM   1256  CE1 PHE A 837     -57.016  -0.811 -21.845  1.00 25.62           C  
-ANISOU 1256  CE1 PHE A 837     3153   3230   3350     29   -246   -319       C  
-ATOM   1257  CE2 PHE A 837     -54.783   0.049 -21.693  1.00 26.21           C  
-ANISOU 1257  CE2 PHE A 837     3266   3321   3370     36   -204   -291       C  
-ATOM   1258  CZ  PHE A 837     -55.706  -0.795 -22.292  1.00 26.00           C  
-ANISOU 1258  CZ  PHE A 837     3227   3290   3361     39   -234   -316       C  
-ATOM   1259  N   LYS A 838     -59.158   3.828 -17.829  1.00 24.95           N  
-ANISOU 1259  N   LYS A 838     3018   3146   3315     15   -169   -238       N  
-ATOM   1260  CA  LYS A 838     -59.629   4.329 -16.553  1.00 27.01           C  
-ANISOU 1260  CA  LYS A 838     3262   3405   3596      8   -147   -229       C  
-ATOM   1261  C   LYS A 838     -59.647   3.196 -15.566  1.00 25.39           C  
-ANISOU 1261  C   LYS A 838     3044   3193   3411    -12   -128   -228       C  
-ATOM   1262  O   LYS A 838     -60.234   2.144 -15.842  1.00 27.73           O  
-ANISOU 1262  O   LYS A 838     3326   3481   3730    -22   -140   -239       O  
-ATOM   1263  CB  LYS A 838     -61.021   4.915 -16.702  1.00 31.27           C  
-ANISOU 1263  CB  LYS A 838     3775   3948   4159     16   -163   -238       C  
-ATOM   1264  CG  LYS A 838     -61.459   5.880 -15.596  1.00 33.75           C  
-ANISOU 1264  CG  LYS A 838     4075   4265   4485     19   -143   -231       C  
-ATOM   1265  CD  LYS A 838     -62.624   6.753 -16.080  1.00 39.62           C  
-ANISOU 1265  CD  LYS A 838     4799   5012   5243     36   -165   -241       C  
-ATOM   1266  CE  LYS A 838     -62.778   8.085 -15.333  1.00 44.08           C  
-ANISOU 1266  CE  LYS A 838     5360   5579   5810     48   -153   -235       C  
-ATOM   1267  NZ  LYS A 838     -62.468   8.043 -13.876  1.00 47.96           N  
-ANISOU 1267  NZ  LYS A 838     5845   6073   6304     37   -117   -229       N  
-ATOM   1268  N   ILE A 839     -59.000   3.368 -14.425  1.00 23.16           N  
-ANISOU 1268  N   ILE A 839     2768   2910   3121    -17   -100   -214       N  
-ATOM   1269  CA  ILE A 839     -58.869   2.248 -13.462  1.00 24.12           C  
-ANISOU 1269  CA  ILE A 839     2885   3025   3256    -34    -80   -207       C  
-ATOM   1270  C   ILE A 839     -59.432   2.564 -12.060  1.00 23.92           C  
-ANISOU 1270  C   ILE A 839     2842   3004   3241    -40    -53   -196       C  
-ATOM   1271  O   ILE A 839     -59.282   3.671 -11.571  1.00 24.85           O  
-ANISOU 1271  O   ILE A 839     2964   3132   3347    -29    -43   -193       O  
-ATOM   1272  CB  ILE A 839     -57.401   1.788 -13.330  1.00 23.31           C  
-ANISOU 1272  CB  ILE A 839     2810   2917   3130    -35    -73   -201       C  
-ATOM   1273  CG1 ILE A 839     -56.479   2.928 -12.974  1.00 22.72           C  
-ANISOU 1273  CG1 ILE A 839     2753   2851   3030    -24    -61   -193       C  
-ATOM   1274  CG2 ILE A 839     -56.937   1.157 -14.632  1.00 24.62           C  
-ANISOU 1274  CG2 ILE A 839     2988   3078   3287    -32    -97   -214       C  
-ATOM   1275  CD1 ILE A 839     -55.072   2.453 -12.643  1.00 23.69           C  
-ANISOU 1275  CD1 ILE A 839     2896   2970   3135    -25    -52   -188       C  
-ATOM   1276  N   GLU A 840     -60.052   1.579 -11.436  1.00 24.38           N  
-ANISOU 1276  N   GLU A 840     2883   3056   3324    -57    -40   -191       N  
-ATOM   1277  CA  GLU A 840     -60.552   1.707 -10.082  1.00 27.39           C  
-ANISOU 1277  CA  GLU A 840     3249   3445   3711    -63     -9   -179       C  
-ATOM   1278  C   GLU A 840     -60.127   0.456  -9.323  1.00 27.01           C  
-ANISOU 1278  C   GLU A 840     3209   3386   3666    -79      8   -162       C  
-ATOM   1279  O   GLU A 840     -60.676  -0.642  -9.536  1.00 27.39           O  
-ANISOU 1279  O   GLU A 840     3243   3420   3745    -97      5   -160       O  
-ATOM   1280  CB  GLU A 840     -62.090   1.813 -10.048  1.00 30.04           C  
-ANISOU 1280  CB  GLU A 840     3545   3786   4081    -68     -7   -186       C  
-ATOM   1281  CG  GLU A 840     -62.668   2.958 -10.861  1.00 34.67           C  
-ANISOU 1281  CG  GLU A 840     4121   4381   4670    -51    -30   -204       C  
-ATOM   1282  CD  GLU A 840     -64.208   2.899 -11.024  1.00 43.13           C  
-ANISOU 1282  CD  GLU A 840     5150   5455   5782    -56    -35   -216       C  
-ATOM   1283  OE1 GLU A 840     -64.869   1.901 -10.618  1.00 46.46           O  
-ANISOU 1283  OE1 GLU A 840     5548   5871   6233    -77    -22   -212       O  
-ATOM   1284  OE2 GLU A 840     -64.773   3.862 -11.575  1.00 47.39           O  
-ANISOU 1284  OE2 GLU A 840     5679   6001   6325    -39    -54   -230       O  
-ATOM   1285  N   ARG A 841     -59.145   0.604  -8.459  1.00 25.15           N  
-ANISOU 1285  N   ARG A 841     2997   3156   3403    -73     25   -149       N  
-ATOM   1286  CA  ARG A 841     -58.736  -0.501  -7.600  1.00 26.51           C  
-ANISOU 1286  CA  ARG A 841     3180   3319   3575    -85     42   -129       C  
-ATOM   1287  C   ARG A 841     -59.731  -0.722  -6.439  1.00 27.36           C  
-ANISOU 1287  C   ARG A 841     3266   3434   3694    -96     74   -112       C  
-ATOM   1288  O   ARG A 841     -60.114   0.192  -5.768  1.00 28.34           O  
-ANISOU 1288  O   ARG A 841     3381   3580   3807    -86     91   -112       O  
-ATOM   1289  CB  ARG A 841     -57.349  -0.234  -6.994  1.00 25.44           C  
-ANISOU 1289  CB  ARG A 841     3075   3188   3402    -72     47   -123       C  
-ATOM   1290  CG  ARG A 841     -56.191  -0.179  -7.977  1.00 24.99           C  
-ANISOU 1290  CG  ARG A 841     3039   3123   3332    -63     23   -136       C  
-ATOM   1291  CD  ARG A 841     -54.948  -0.842  -7.369  1.00 28.25           C  
-ANISOU 1291  CD  ARG A 841     3478   3530   3728    -60     26   -126       C  
-ATOM   1292  NE  ARG A 841     -54.704  -0.265  -6.098  1.00 29.68           N  
-ANISOU 1292  NE  ARG A 841     3665   3725   3886    -51     46   -116       N  
-ATOM   1293  CZ  ARG A 841     -54.767  -0.827  -4.907  1.00 27.13           C  
-ANISOU 1293  CZ  ARG A 841     3347   3404   3556    -53     66    -97       C  
-ATOM   1294  NH1 ARG A 841     -54.861  -2.122  -4.699  1.00 25.84           N  
-ANISOU 1294  NH1 ARG A 841     3188   3223   3406    -67     69    -79       N  
-ATOM   1295  NH2 ARG A 841     -54.600  -0.006  -3.895  1.00 28.48           N  
-ANISOU 1295  NH2 ARG A 841     3523   3595   3702    -40     80    -95       N  
-ATOM   1296  N   GLU A 842     -60.105  -1.964  -6.212  1.00 29.52           N  
-ANISOU 1296  N   GLU A 842     3532   3691   3993   -117     83    -96       N  
-ATOM   1297  CA  GLU A 842     -60.911  -2.362  -5.090  1.00 33.14           C  
-ANISOU 1297  CA  GLU A 842     3974   4156   4463   -131    118    -72       C  
-ATOM   1298  C   GLU A 842     -60.332  -1.852  -3.780  1.00 31.36           C  
-ANISOU 1298  C   GLU A 842     3769   3952   4194   -116    145    -56       C  
-ATOM   1299  O   GLU A 842     -59.148  -2.056  -3.476  1.00 29.40           O  
-ANISOU 1299  O   GLU A 842     3553   3700   3918   -106    139    -49       O  
-ATOM   1300  CB  GLU A 842     -60.931  -3.898  -5.094  1.00 41.12           C  
-ANISOU 1300  CB  GLU A 842     4986   5136   5501   -154    119    -53       C  
-ATOM   1301  CG  GLU A 842     -61.780  -4.659  -4.078  1.00 50.95           C  
-ANISOU 1301  CG  GLU A 842     6214   6378   6768   -176    155    -21       C  
-ATOM   1302  CD  GLU A 842     -62.209  -6.082  -4.613  1.00 65.28           C  
-ANISOU 1302  CD  GLU A 842     8015   8154   8635   -205    144    -14       C  
-ATOM   1303  OE1 GLU A 842     -62.525  -6.202  -5.829  1.00 72.74           O  
-ANISOU 1303  OE1 GLU A 842     8944   9084   9611   -209    112    -42       O  
-ATOM   1304  OE2 GLU A 842     -62.268  -7.102  -3.852  1.00 71.37           O  
-ANISOU 1304  OE2 GLU A 842     8792   8907   9419   -223    166     20       O  
-ATOM   1305  N   GLY A 843     -61.160  -1.139  -3.024  1.00 28.12           N  
-ANISOU 1305  N   GLY A 843     3339   3568   3779   -111    171    -55       N  
-ATOM   1306  CA  GLY A 843     -60.752  -0.694  -1.710  1.00 27.81           C  
-ANISOU 1306  CA  GLY A 843     3316   3552   3698    -96    198    -42       C  
-ATOM   1307  C   GLY A 843     -60.033   0.634  -1.697  1.00 27.03           C  
-ANISOU 1307  C   GLY A 843     3232   3470   3567    -68    184    -66       C  
-ATOM   1308  O   GLY A 843     -59.876   1.236  -0.632  1.00 28.58           O  
-ANISOU 1308  O   GLY A 843     3436   3691   3732    -51    203    -64       O  
-ATOM   1309  N   GLU A 844     -59.654   1.149  -2.854  1.00 25.85           N  
-ANISOU 1309  N   GLU A 844     3086   3310   3427    -62    151    -88       N  
-ATOM   1310  CA  GLU A 844     -58.860   2.369  -2.844  1.00 26.65           C  
-ANISOU 1310  CA  GLU A 844     3202   3422   3502    -39    138   -108       C  
-ATOM   1311  C   GLU A 844     -59.668   3.616  -2.527  1.00 26.09           C  
-ANISOU 1311  C   GLU A 844     3110   3372   3431    -24    147   -125       C  
-ATOM   1312  O   GLU A 844     -59.150   4.529  -1.891  1.00 27.51           O  
-ANISOU 1312  O   GLU A 844     3302   3566   3586     -4    149   -135       O  
-ATOM   1313  CB  GLU A 844     -58.093   2.541  -4.152  1.00 27.45           C  
-ANISOU 1313  CB  GLU A 844     3315   3504   3609    -37    104   -122       C  
-ATOM   1314  CG  GLU A 844     -56.748   3.190  -3.960  1.00 29.16           C  
-ANISOU 1314  CG  GLU A 844     3559   3724   3798    -20     93   -130       C  
-ATOM   1315  CD  GLU A 844     -55.939   3.266  -5.258  1.00 29.55           C  
-ANISOU 1315  CD  GLU A 844     3620   3757   3852    -20     65   -141       C  
-ATOM   1316  OE1 GLU A 844     -56.433   3.960  -6.182  1.00 28.05           O  
-ANISOU 1316  OE1 GLU A 844     3418   3564   3675    -18     51   -153       O  
-ATOM   1317  OE2 GLU A 844     -54.818   2.681  -5.321  1.00 28.40           O  
-ANISOU 1317  OE2 GLU A 844     3495   3602   3695    -20     57   -137       O  
-ATOM   1318  N   CYS A 845     -60.904   3.673  -2.988  1.00 25.80           N  
-ANISOU 1318  N   CYS A 845     3041   3337   3426    -32    149   -130       N  
-ATOM   1319  CA  CYS A 845     -61.773   4.808  -2.701  1.00 29.04           C  
-ANISOU 1319  CA  CYS A 845     3428   3767   3841    -17    157   -148       C  
-ATOM   1320  C   CYS A 845     -61.941   4.957  -1.189  1.00 27.03           C  
-ANISOU 1320  C   CYS A 845     3171   3539   3559     -8    193   -141       C  
-ATOM   1321  O   CYS A 845     -61.832   6.029  -0.644  1.00 24.83           O  
-ANISOU 1321  O   CYS A 845     2896   3278   3263     15    195   -158       O  
-ATOM   1322  CB  CYS A 845     -63.163   4.634  -3.368  1.00 29.73           C  
-ANISOU 1322  CB  CYS A 845     3475   3851   3969    -29    155   -155       C  
-ATOM   1323  SG  CYS A 845     -64.424   5.832  -2.901  1.00 35.40           S  
-ANISOU 1323  SG  CYS A 845     4156   4595   4700    -11    169   -177       S  
-ATOM   1324  N   GLN A 846     -62.242   3.847  -0.545  1.00 28.42           N  
-ANISOU 1324  N   GLN A 846     3345   3719   3735    -25    221   -115       N  
-ATOM   1325  CA  GLN A 846     -62.434   3.832   0.892  1.00 30.39           C  
-ANISOU 1325  CA  GLN A 846     3595   3996   3954    -17    259   -102       C  
-ATOM   1326  C   GLN A 846     -61.164   4.236   1.583  1.00 27.04           C  
-ANISOU 1326  C   GLN A 846     3209   3581   3485      5    252   -105       C  
-ATOM   1327  O   GLN A 846     -61.181   5.003   2.548  1.00 26.34           O  
-ANISOU 1327  O   GLN A 846     3122   3518   3367     28    267   -117       O  
-ATOM   1328  CB  GLN A 846     -62.942   2.442   1.355  1.00 32.63           C  
-ANISOU 1328  CB  GLN A 846     3871   4277   4248    -43    290    -66       C  
-ATOM   1329  CG  GLN A 846     -63.342   2.350   2.815  1.00 36.03           C  
-ANISOU 1329  CG  GLN A 846     4300   4741   4648    -37    336    -47       C  
-ATOM   1330  CD  GLN A 846     -64.553   3.222   3.183  1.00 41.56           C  
-ANISOU 1330  CD  GLN A 846     4961   5472   5357    -26    361    -67       C  
-ATOM   1331  OE1 GLN A 846     -65.490   3.422   2.382  1.00 39.79           O  
-ANISOU 1331  OE1 GLN A 846     4700   5240   5177    -36    353    -82       O  
-ATOM   1332  NE2 GLN A 846     -64.542   3.746   4.411  1.00 44.73           N  
-ANISOU 1332  NE2 GLN A 846     5369   5910   5715     -3    389    -68       N  
-ATOM   1333  N   ARG A 847     -60.049   3.717   1.109  1.00 26.85           N  
-ANISOU 1333  N   ARG A 847     3213   3533   3455      0    228    -98       N  
-ATOM   1334  CA  ARG A 847     -58.760   4.048   1.732  1.00 27.80           C  
-ANISOU 1334  CA  ARG A 847     3368   3658   3537     20    218   -103       C  
-ATOM   1335  C   ARG A 847     -58.422   5.522   1.517  1.00 25.87           C  
-ANISOU 1335  C   ARG A 847     3123   3419   3289     43    197   -138       C  
-ATOM   1336  O   ARG A 847     -57.901   6.181   2.400  1.00 25.42           O  
-ANISOU 1336  O   ARG A 847     3079   3379   3201     66    199   -151       O  
-ATOM   1337  CB  ARG A 847     -57.691   3.137   1.143  1.00 30.77           C  
-ANISOU 1337  CB  ARG A 847     3769   4007   3916      9    196    -90       C  
-ATOM   1338  CG  ARG A 847     -56.332   3.299   1.765  1.00 32.41           C  
-ANISOU 1338  CG  ARG A 847     4008   4217   4087     28    184    -94       C  
-ATOM   1339  CD  ARG A 847     -55.346   2.391   1.075  1.00 32.63           C  
-ANISOU 1339  CD  ARG A 847     4056   4218   4124     17    162    -85       C  
-ATOM   1340  NE  ARG A 847     -54.910   2.917  -0.220  1.00 34.46           N  
-ANISOU 1340  NE  ARG A 847     4284   4433   4378     14    133   -106       N  
-ATOM   1341  CZ  ARG A 847     -53.928   2.386  -0.958  1.00 35.15           C  
-ANISOU 1341  CZ  ARG A 847     4385   4499   4471      9    111   -106       C  
-ATOM   1342  NH1 ARG A 847     -53.285   1.315  -0.531  1.00 37.37           N  
-ANISOU 1342  NH1 ARG A 847     4685   4771   4741      7    112    -89       N  
-ATOM   1343  NH2 ARG A 847     -53.576   2.929  -2.103  1.00 35.08           N  
-ANISOU 1343  NH2 ARG A 847     4372   4478   4478      8     90   -124       N  
-ATOM   1344  N   TYR A 848     -58.750   6.059   0.344  1.00 24.64           N  
-ANISOU 1344  N   TYR A 848     2950   3246   3164     38    176   -153       N  
-ATOM   1345  CA  TYR A 848     -58.438   7.461   0.020  1.00 24.11           C  
-ANISOU 1345  CA  TYR A 848     2883   3177   3100     57    154   -182       C  
-ATOM   1346  C   TYR A 848     -59.347   8.476   0.748  1.00 25.44           C  
-ANISOU 1346  C   TYR A 848     3030   3370   3267     77    169   -203       C  
-ATOM   1347  O   TYR A 848     -59.024   9.653   0.826  1.00 25.40           O  
-ANISOU 1347  O   TYR A 848     3028   3365   3259     97    154   -228       O  
-ATOM   1348  CB  TYR A 848     -58.508   7.647  -1.492  1.00 23.14           C  
-ANISOU 1348  CB  TYR A 848     2754   3030   3009     47    127   -187       C  
-ATOM   1349  CG  TYR A 848     -58.088   8.986  -2.031  1.00 22.71           C  
-ANISOU 1349  CG  TYR A 848     2702   2965   2961     62    102   -210       C  
-ATOM   1350  CD1 TYR A 848     -56.760   9.388  -1.977  1.00 22.24           C  
-ANISOU 1350  CD1 TYR A 848     2667   2896   2887     70     87   -216       C  
-ATOM   1351  CD2 TYR A 848     -59.003   9.837  -2.635  1.00 22.46           C  
-ANISOU 1351  CD2 TYR A 848     2650   2931   2954     69     92   -223       C  
-ATOM   1352  CE1 TYR A 848     -56.351  10.593  -2.477  1.00 22.32           C  
-ANISOU 1352  CE1 TYR A 848     2680   2893   2907     80     67   -233       C  
-ATOM   1353  CE2 TYR A 848     -58.590  11.071  -3.156  1.00 23.13           C  
-ANISOU 1353  CE2 TYR A 848     2740   3001   3046     82     69   -240       C  
-ATOM   1354  CZ  TYR A 848     -57.267  11.447  -3.060  1.00 22.19           C  
-ANISOU 1354  CZ  TYR A 848     2645   2872   2915     87     58   -243       C  
-ATOM   1355  OH  TYR A 848     -56.796  12.625  -3.601  1.00 23.12           O  
-ANISOU 1355  OH  TYR A 848     2769   2972   3045     96     36   -255       O  
-ATOM   1356  N   LYS A 849     -60.470   8.017   1.257  1.00 28.72           N  
-ANISOU 1356  N   LYS A 849     3422   3804   3685     71    199   -193       N  
-ATOM   1357  CA  LYS A 849     -61.549   8.874   1.812  1.00 33.35           C  
-ANISOU 1357  CA  LYS A 849     3981   4416   4276     88    216   -213       C  
-ATOM   1358  C   LYS A 849     -61.090   9.975   2.760  1.00 33.06           C  
-ANISOU 1358  C   LYS A 849     3955   4397   4211    120    215   -240       C  
-ATOM   1359  O   LYS A 849     -61.490  11.117   2.593  1.00 35.01           O  
-ANISOU 1359  O   LYS A 849     4186   4644   4472    138    202   -268       O  
-ATOM   1360  CB  LYS A 849     -62.608   7.982   2.480  1.00 34.89           C  
-ANISOU 1360  CB  LYS A 849     4153   4633   4471     75    257   -192       C  
-ATOM   1361  CG  LYS A 849     -63.865   8.666   2.970  1.00 41.09           C  
-ANISOU 1361  CG  LYS A 849     4902   5446   5266     89    280   -211       C  
-ATOM   1362  CD  LYS A 849     -64.832   7.606   3.528  1.00 46.27           C  
-ANISOU 1362  CD  LYS A 849     5534   6121   5925     68    325   -183       C  
-ATOM   1363  CE  LYS A 849     -66.124   8.185   4.119  1.00 51.40           C  
-ANISOU 1363  CE  LYS A 849     6142   6803   6583     81    356   -201       C  
-ATOM   1364  NZ  LYS A 849     -66.752   9.191   3.226  1.00 54.15           N  
-ANISOU 1364  NZ  LYS A 849     6463   7141   6971     93    327   -235       N  
-ATOM   1365  N   PRO A 850     -60.236   9.652   3.737  1.00 33.54           N  
-ANISOU 1365  N   PRO A 850     4043   4471   4231    129    224   -233       N  
-ATOM   1366  CA  PRO A 850     -59.747  10.709   4.611  1.00 35.44           C  
-ANISOU 1366  CA  PRO A 850     4294   4728   4445    160    218   -264       C  
-ATOM   1367  C   PRO A 850     -59.015  11.841   3.880  1.00 37.55           C  
-ANISOU 1367  C   PRO A 850     4568   4967   4733    170    177   -291       C  
-ATOM   1368  O   PRO A 850     -58.989  12.976   4.368  1.00 41.53           O  
-ANISOU 1368  O   PRO A 850     5068   5478   5233    196    168   -324       O  
-ATOM   1369  CB  PRO A 850     -58.805   9.983   5.565  1.00 35.19           C  
-ANISOU 1369  CB  PRO A 850     4293   4709   4368    165    226   -248       C  
-ATOM   1370  CG  PRO A 850     -59.194   8.542   5.481  1.00 36.17           C  
-ANISOU 1370  CG  PRO A 850     4417   4832   4492    138    251   -205       C  
-ATOM   1371  CD  PRO A 850     -59.704   8.328   4.098  1.00 34.25           C  
-ANISOU 1371  CD  PRO A 850     4154   4561   4298    112    238   -198       C  
-ATOM   1372  N   PHE A 851     -58.460  11.552   2.708  1.00 35.56           N  
-ANISOU 1372  N   PHE A 851     4324   4682   4505    150    154   -278       N  
-ATOM   1373  CA  PHE A 851     -57.695  12.543   1.972  1.00 34.81           C  
-ANISOU 1373  CA  PHE A 851     4237   4559   4429    156    120   -297       C  
-ATOM   1374  C   PHE A 851     -58.511  13.220   0.862  1.00 32.11           C  
-ANISOU 1374  C   PHE A 851     3874   4199   4127    152    105   -303       C  
-ATOM   1375  O   PHE A 851     -58.066  14.189   0.273  1.00 31.36           O  
-ANISOU 1375  O   PHE A 851     3783   4081   4050    159     79   -317       O  
-ATOM   1376  CB  PHE A 851     -56.404  11.875   1.468  1.00 33.54           C  
-ANISOU 1376  CB  PHE A 851     4102   4379   4264    140    104   -279       C  
-ATOM   1377  CG  PHE A 851     -55.518  11.409   2.585  1.00 33.58           C  
-ANISOU 1377  CG  PHE A 851     4128   4400   4231    150    111   -278       C  
-ATOM   1378  CD1 PHE A 851     -54.788  12.320   3.335  1.00 36.10           C  
-ANISOU 1378  CD1 PHE A 851     4457   4724   4537    173     97   -308       C  
-ATOM   1379  CD2 PHE A 851     -55.430  10.067   2.917  1.00 34.02           C  
-ANISOU 1379  CD2 PHE A 851     4195   4465   4266    137    128   -250       C  
-ATOM   1380  CE1 PHE A 851     -53.966  11.901   4.381  1.00 34.15           C  
-ANISOU 1380  CE1 PHE A 851     4230   4492   4252    186     99   -309       C  
-ATOM   1381  CE2 PHE A 851     -54.639   9.641   3.970  1.00 33.16           C  
-ANISOU 1381  CE2 PHE A 851     4108   4371   4120    149    132   -247       C  
-ATOM   1382  CZ  PHE A 851     -53.905  10.558   4.703  1.00 33.44           C  
-ANISOU 1382  CZ  PHE A 851     4152   4413   4138    175    117   -278       C  
-ATOM   1383  N   LYS A 852     -59.694  12.697   0.594  1.00 32.13           N  
-ANISOU 1383  N   LYS A 852     3853   4211   4142    142    121   -292       N  
-ATOM   1384  CA  LYS A 852     -60.534  13.151  -0.517  1.00 37.27           C  
-ANISOU 1384  CA  LYS A 852     4484   4846   4831    139    105   -296       C  
-ATOM   1385  C   LYS A 852     -60.850  14.644  -0.528  1.00 36.70           C  
-ANISOU 1385  C   LYS A 852     4402   4767   4777    164     88   -326       C  
-ATOM   1386  O   LYS A 852     -61.091  15.209  -1.583  1.00 39.41           O  
-ANISOU 1386  O   LYS A 852     4740   5087   5148    163     64   -328       O  
-ATOM   1387  CB  LYS A 852     -61.862  12.342  -0.588  1.00 38.66           C  
-ANISOU 1387  CB  LYS A 852     4630   5038   5020    126    128   -284       C  
-ATOM   1388  N   GLN A 853     -60.827  15.257   0.642  1.00 36.81           N  
-ANISOU 1388  N   GLN A 853     4413   4800   4773    187     98   -350       N  
-ATOM   1389  CA  GLN A 853     -61.069  16.677   0.839  1.00 39.88           C  
-ANISOU 1389  CA  GLN A 853     4793   5183   5178    214     82   -384       C  
-ATOM   1390  C   GLN A 853     -59.902  17.458   1.411  1.00 36.26           C  
-ANISOU 1390  C   GLN A 853     4357   4714   4708    230     66   -405       C  
-ATOM   1391  O   GLN A 853     -60.081  18.605   1.817  1.00 35.91           O  
-ANISOU 1391  O   GLN A 853     4305   4666   4675    255     54   -437       O  
-ATOM   1392  CB  GLN A 853     -62.326  16.839   1.745  1.00 45.66           C  
-ANISOU 1392  CB  GLN A 853     5494   5949   5906    233    109   -404       C  
-ATOM   1393  CG  GLN A 853     -63.590  16.393   1.030  1.00 48.46           C  
-ANISOU 1393  CG  GLN A 853     5818   6307   6287    221    116   -392       C  
-ATOM   1394  CD  GLN A 853     -64.838  16.953   1.666  1.00 58.16           C  
-ANISOU 1394  CD  GLN A 853     7010   7562   7525    244    133   -420       C  
-ATOM   1395  OE1 GLN A 853     -65.568  17.754   1.070  1.00 61.55           O  
-ANISOU 1395  OE1 GLN A 853     7419   7978   7990    258    113   -438       O  
-ATOM   1396  NE2 GLN A 853     -65.106  16.515   2.894  1.00 63.06           N  
-ANISOU 1396  NE2 GLN A 853     7624   8222   8115    251    172   -423       N  
-ATOM   1397  N   LEU A 854     -58.700  16.875   1.448  1.00 36.69           N  
-ANISOU 1397  N   LEU A 854     4436   4761   4742    216     63   -389       N  
-ATOM   1398  CA  LEU A 854     -57.484  17.670   1.593  1.00 33.08           C  
-ANISOU 1398  CA  LEU A 854     3998   4283   4287    225     38   -407       C  
-ATOM   1399  C   LEU A 854     -57.466  18.575   0.381  1.00 30.89           C  
-ANISOU 1399  C   LEU A 854     3719   3966   4052    220     10   -406       C  
-ATOM   1400  O   LEU A 854     -57.908  18.214  -0.708  1.00 29.78           O  
-ANISOU 1400  O   LEU A 854     3574   3814   3927    204      8   -382       O  
-ATOM   1401  CB  LEU A 854     -56.247  16.764   1.602  1.00 36.83           C  
-ANISOU 1401  CB  LEU A 854     4497   4755   4741    207     39   -386       C  
-ATOM   1402  CG  LEU A 854     -54.986  17.138   2.368  1.00 36.15           C  
-ANISOU 1402  CG  LEU A 854     4428   4666   4640    219     25   -407       C  
-ATOM   1403  CD1 LEU A 854     -55.305  17.534   3.803  1.00 39.23           C  
-ANISOU 1403  CD1 LEU A 854     4814   5088   5004    250     35   -439       C  
-ATOM   1404  CD2 LEU A 854     -54.028  15.957   2.356  1.00 37.16           C  
-ANISOU 1404  CD2 LEU A 854     4576   4798   4745    201     30   -382       C  
-ATOM   1405  N   HIS A 855     -56.886  19.733   0.543  1.00 29.84           N  
-ANISOU 1405  N   HIS A 855     3590   3811   3936    235    -12   -431       N  
-ATOM   1406  CA  HIS A 855     -56.711  20.633  -0.570  1.00 28.52           C  
-ANISOU 1406  CA  HIS A 855     3425   3603   3808    230    -38   -426       C  
-ATOM   1407  C   HIS A 855     -55.478  20.220  -1.400  1.00 29.26           C  
-ANISOU 1407  C   HIS A 855     3540   3675   3903    204    -46   -398       C  
-ATOM   1408  O   HIS A 855     -54.726  19.285  -1.040  1.00 28.46           O  
-ANISOU 1408  O   HIS A 855     3450   3589   3775    192    -34   -389       O  
-ATOM   1409  CB  HIS A 855     -56.519  22.047  -0.036  1.00 28.88           C  
-ANISOU 1409  CB  HIS A 855     3468   3629   3878    254    -59   -463       C  
-ATOM   1410  CG  HIS A 855     -55.288  22.213   0.815  1.00 27.78           C  
-ANISOU 1410  CG  HIS A 855     3341   3488   3726    259    -66   -483       C  
-ATOM   1411  ND1 HIS A 855     -55.088  21.531   2.001  1.00 30.02           N  
-ANISOU 1411  ND1 HIS A 855     3628   3810   3969    269    -49   -497       N  
-ATOM   1412  CD2 HIS A 855     -54.185  22.969   0.640  1.00 27.79           C  
-ANISOU 1412  CD2 HIS A 855     3352   3455   3752    255    -89   -493       C  
-ATOM   1413  CE1 HIS A 855     -53.927  21.880   2.534  1.00 27.43           C  
-ANISOU 1413  CE1 HIS A 855     3310   3471   3639    273    -64   -517       C  
-ATOM   1414  NE2 HIS A 855     -53.363  22.754   1.729  1.00 27.85           N  
-ANISOU 1414  NE2 HIS A 855     3366   3481   3736    264    -88   -516       N  
-ATOM   1415  N   ASN A 856     -55.290  20.899  -2.528  1.00 28.80           N  
-ANISOU 1415  N   ASN A 856     3486   3581   3875    195    -65   -385       N  
-ATOM   1416  CA  ASN A 856     -54.131  20.687  -3.366  1.00 27.34           C  
-ANISOU 1416  CA  ASN A 856     3318   3375   3694    173    -70   -361       C  
-ATOM   1417  C   ASN A 856     -53.991  19.204  -3.804  1.00 26.95           C  
-ANISOU 1417  C   ASN A 856     3276   3347   3617    152    -53   -332       C  
-ATOM   1418  O   ASN A 856     -52.964  18.531  -3.602  1.00 26.44           O  
-ANISOU 1418  O   ASN A 856     3222   3288   3535    140    -47   -327       O  
-ATOM   1419  CB  ASN A 856     -52.892  21.194  -2.650  1.00 28.93           C  
-ANISOU 1419  CB  ASN A 856     3526   3564   3901    175    -79   -381       C  
-ATOM   1420  CG  ASN A 856     -51.675  21.223  -3.551  1.00 30.66           C  
-ANISOU 1420  CG  ASN A 856     3757   3758   4134    152    -85   -359       C  
-ATOM   1421  OD1 ASN A 856     -51.793  21.211  -4.775  1.00 32.89           O  
-ANISOU 1421  OD1 ASN A 856     4046   4025   4426    138    -86   -330       O  
-ATOM   1422  ND2 ASN A 856     -50.502  21.213  -2.951  1.00 31.76           N  
-ANISOU 1422  ND2 ASN A 856     3900   3894   4272    149    -88   -374       N  
-ATOM   1423  N   ARG A 857     -55.040  18.732  -4.465  1.00 25.82           N  
-ANISOU 1423  N   ARG A 857     3125   3212   3472    148    -48   -317       N  
-ATOM   1424  CA  ARG A 857     -55.082  17.430  -5.084  1.00 24.55           C  
-ANISOU 1424  CA  ARG A 857     2969   3065   3293    129    -37   -292       C  
-ATOM   1425  C   ARG A 857     -54.675  17.541  -6.537  1.00 23.51           C  
-ANISOU 1425  C   ARG A 857     2849   2910   3172    115    -50   -267       C  
-ATOM   1426  O   ARG A 857     -55.219  18.336  -7.265  1.00 22.24           O  
-ANISOU 1426  O   ARG A 857     2687   2734   3031    122    -64   -263       O  
-ATOM   1427  CB  ARG A 857     -56.459  16.830  -4.940  1.00 25.05           C  
-ANISOU 1427  CB  ARG A 857     3015   3151   3352    133    -26   -291       C  
-ATOM   1428  CG  ARG A 857     -56.625  16.287  -3.541  1.00 27.81           C  
-ANISOU 1428  CG  ARG A 857     3357   3529   3680    140     -4   -305       C  
-ATOM   1429  CD  ARG A 857     -58.020  16.066  -3.042  1.00 28.62           C  
-ANISOU 1429  CD  ARG A 857     3436   3655   3782    149     11   -313       C  
-ATOM   1430  NE  ARG A 857     -59.005  16.234  -4.064  1.00 35.65           N  
-ANISOU 1430  NE  ARG A 857     4313   4537   4697    148     -1   -307       N  
-ATOM   1431  CZ  ARG A 857     -59.913  17.190  -4.088  1.00 39.95           C  
-ANISOU 1431  CZ  ARG A 857     4839   5077   5263    167    -10   -324       C  
-ATOM   1432  NH1 ARG A 857     -60.019  18.077  -3.099  1.00 47.09           N  
-ANISOU 1432  NH1 ARG A 857     5736   5987   6169    189     -8   -352       N  
-ATOM   1433  NH2 ARG A 857     -60.729  17.249  -5.126  1.00 42.04           N  
-ANISOU 1433  NH2 ARG A 857     5093   5333   5548    165    -25   -316       N  
-ATOM   1434  N   ARG A 858     -53.737  16.691  -6.964  1.00 23.84           N  
-ANISOU 1434  N   ARG A 858     2904   2954   3198     98    -43   -251       N  
-ATOM   1435  CA  ARG A 858     -53.136  16.842  -8.276  1.00 24.93           C  
-ANISOU 1435  CA  ARG A 858     3056   3075   3342     86    -52   -230       C  
-ATOM   1436  C   ARG A 858     -53.054  15.502  -9.009  1.00 22.74           C  
-ANISOU 1436  C   ARG A 858     2785   2811   3044     71    -45   -212       C  
-ATOM   1437  O   ARG A 858     -52.733  14.464  -8.398  1.00 21.22           O  
-ANISOU 1437  O   ARG A 858     2592   2634   2834     65    -33   -216       O  
-ATOM   1438  CB  ARG A 858     -51.733  17.405  -8.117  1.00 27.80           C  
-ANISOU 1438  CB  ARG A 858     3429   3421   3713     80    -53   -232       C  
-ATOM   1439  CG  ARG A 858     -51.425  18.485  -9.113  1.00 34.78           C  
-ANISOU 1439  CG  ARG A 858     4320   4276   4619     77    -64   -217       C  
-ATOM   1440  CD  ARG A 858     -50.147  19.291  -8.822  1.00 38.08           C  
-ANISOU 1440  CD  ARG A 858     4741   4672   5057     71    -66   -223       C  
-ATOM   1441  NE  ARG A 858     -50.350  20.365  -7.841  1.00 45.99           N  
-ANISOU 1441  NE  ARG A 858     5733   5659   6081     86    -77   -249       N  
-ATOM   1442  CZ  ARG A 858     -49.458  21.316  -7.543  1.00 44.74           C  
-ANISOU 1442  CZ  ARG A 858     5573   5474   5951     84    -85   -260       C  
-ATOM   1443  NH1 ARG A 858     -48.282  21.366  -8.159  1.00 45.62           N  
-ANISOU 1443  NH1 ARG A 858     5691   5572   6072     65    -80   -244       N  
-ATOM   1444  NH2 ARG A 858     -49.747  22.217  -6.605  1.00 40.39           N  
-ANISOU 1444  NH2 ARG A 858     5013   4913   5421    102    -97   -290       N  
-ATOM   1445  N   LEU A 859     -53.305  15.554 -10.323  1.00 21.10           N  
-ANISOU 1445  N   LEU A 859     2584   2596   2837     67    -54   -195       N  
-ATOM   1446  CA  LEU A 859     -53.138  14.424 -11.191  1.00 20.34           C  
-ANISOU 1446  CA  LEU A 859     2495   2510   2722     56    -52   -181       C  
-ATOM   1447  C   LEU A 859     -51.690  14.383 -11.691  1.00 19.69           C  
-ANISOU 1447  C   LEU A 859     2428   2421   2632     45    -46   -171       C  
-ATOM   1448  O   LEU A 859     -51.265  15.198 -12.517  1.00 21.33           O  
-ANISOU 1448  O   LEU A 859     2645   2613   2845     43    -51   -157       O  
-ATOM   1449  CB  LEU A 859     -54.139  14.488 -12.338  1.00 22.21           C  
-ANISOU 1449  CB  LEU A 859     2732   2746   2960     61    -67   -171       C  
-ATOM   1450  CG  LEU A 859     -54.381  13.157 -13.072  1.00 21.51           C  
-ANISOU 1450  CG  LEU A 859     2645   2672   2855     53    -68   -166       C  
-ATOM   1451  CD1 LEU A 859     -55.240  12.234 -12.224  1.00 21.63           C  
-ANISOU 1451  CD1 LEU A 859     2642   2701   2874     51    -61   -179       C  
-ATOM   1452  CD2 LEU A 859     -55.024  13.388 -14.428  1.00 21.51           C  
-ANISOU 1452  CD2 LEU A 859     2651   2669   2852     60    -87   -156       C  
-ATOM   1453  N   LEU A 860     -50.966  13.366 -11.254  1.00 18.98           N  
-ANISOU 1453  N   LEU A 860     2339   2342   2529     36    -35   -175       N  
-ATOM   1454  CA  LEU A 860     -49.525  13.259 -11.478  1.00 18.73           C  
-ANISOU 1454  CA  LEU A 860     2316   2307   2493     27    -28   -172       C  
-ATOM   1455  C   LEU A 860     -49.125  11.894 -12.015  1.00 17.89           C  
-ANISOU 1455  C   LEU A 860     2216   2214   2368     19    -23   -168       C  
-ATOM   1456  O   LEU A 860     -49.855  10.903 -11.858  1.00 18.55           O  
-ANISOU 1456  O   LEU A 860     2295   2308   2443     19    -24   -171       O  
-ATOM   1457  CB  LEU A 860     -48.809  13.500 -10.172  1.00 19.39           C  
-ANISOU 1457  CB  LEU A 860     2395   2389   2584     29    -23   -189       C  
-ATOM   1458  CG  LEU A 860     -49.018  14.879  -9.539  1.00 19.68           C  
-ANISOU 1458  CG  LEU A 860     2425   2410   2643     38    -30   -199       C  
-ATOM   1459  CD1 LEU A 860     -48.441  14.889  -8.133  1.00 20.66           C  
-ANISOU 1459  CD1 LEU A 860     2544   2539   2768     44    -28   -221       C  
-ATOM   1460  CD2 LEU A 860     -48.381  15.982 -10.377  1.00 19.52           C  
-ANISOU 1460  CD2 LEU A 860     2410   2367   2641     33    -33   -186       C  
-ATOM   1461  N   TRP A 861     -47.976  11.855 -12.663  1.00 17.42           N  
-ANISOU 1461  N   TRP A 861     2164   2153   2304     12    -17   -162       N  
-ATOM   1462  CA  TRP A 861     -47.475  10.650 -13.310  1.00 17.79           C  
-ANISOU 1462  CA  TRP A 861     2216   2212   2333      7    -13   -161       C  
-ATOM   1463  C   TRP A 861     -46.724   9.732 -12.346  1.00 17.39           C  
-ANISOU 1463  C   TRP A 861     2162   2167   2280      5     -8   -174       C  
-ATOM   1464  O   TRP A 861     -46.035  10.204 -11.436  1.00 17.34           O  
-ANISOU 1464  O   TRP A 861     2150   2155   2283      6     -5   -183       O  
-ATOM   1465  CB  TRP A 861     -46.516  11.008 -14.451  1.00 18.33           C  
-ANISOU 1465  CB  TRP A 861     2291   2279   2394      1     -5   -148       C  
-ATOM   1466  CG  TRP A 861     -47.102  11.867 -15.518  1.00 18.53           C  
-ANISOU 1466  CG  TRP A 861     2325   2299   2416      4    -10   -130       C  
-ATOM   1467  CD1 TRP A 861     -46.897  13.213 -15.699  1.00 19.62           C  
-ANISOU 1467  CD1 TRP A 861     2465   2420   2568      3     -8   -116       C  
-ATOM   1468  CD2 TRP A 861     -47.980  11.450 -16.563  1.00 18.20           C  
-ANISOU 1468  CD2 TRP A 861     2291   2267   2356     10    -20   -123       C  
-ATOM   1469  NE1 TRP A 861     -47.596  13.648 -16.803  1.00 18.92           N  
-ANISOU 1469  NE1 TRP A 861     2388   2331   2469      8    -15    -97       N  
-ATOM   1470  CE2 TRP A 861     -48.261  12.580 -17.352  1.00 18.69           C  
-ANISOU 1470  CE2 TRP A 861     2363   2320   2418     14    -24   -102       C  
-ATOM   1471  CE3 TRP A 861     -48.539  10.227 -16.913  1.00 18.37           C  
-ANISOU 1471  CE3 TRP A 861     2313   2302   2363     14    -29   -132       C  
-ATOM   1472  CZ2 TRP A 861     -49.089  12.520 -18.476  1.00 18.89           C  
-ANISOU 1472  CZ2 TRP A 861     2399   2353   2424     24    -37    -92       C  
-ATOM   1473  CZ3 TRP A 861     -49.325  10.149 -18.025  1.00 18.80           C  
-ANISOU 1473  CZ3 TRP A 861     2376   2364   2402     22    -42   -126       C  
-ATOM   1474  CH2 TRP A 861     -49.628  11.309 -18.790  1.00 19.41           C  
-ANISOU 1474  CH2 TRP A 861     2464   2435   2476     28    -47   -106       C  
-ATOM   1475  N   HIS A 862     -46.836   8.421 -12.586  1.00 16.68           N  
-ANISOU 1475  N   HIS A 862     2074   2086   2178      4     -9   -177       N  
-ATOM   1476  CA  HIS A 862     -45.915   7.480 -11.990  1.00 17.10           C  
-ANISOU 1476  CA  HIS A 862     2128   2143   2228      3     -6   -187       C  
-ATOM   1477  C   HIS A 862     -45.589   6.389 -12.992  1.00 17.34           C  
-ANISOU 1477  C   HIS A 862     2163   2179   2247      2     -8   -189       C  
-ATOM   1478  O   HIS A 862     -46.478   5.634 -13.388  1.00 18.08           O  
-ANISOU 1478  O   HIS A 862     2259   2275   2337      2    -15   -188       O  
-ATOM   1479  CB  HIS A 862     -46.487   6.875 -10.722  1.00 16.73           C  
-ANISOU 1479  CB  HIS A 862     2078   2096   2182      7     -8   -192       C  
-ATOM   1480  CG  HIS A 862     -45.556   5.939 -10.059  1.00 18.48           C  
-ANISOU 1480  CG  HIS A 862     2302   2319   2400      9     -8   -200       C  
-ATOM   1481  ND1 HIS A 862     -44.659   6.355  -9.096  1.00 20.25           N  
-ANISOU 1481  ND1 HIS A 862     2526   2543   2627     14     -7   -209       N  
-ATOM   1482  CD2 HIS A 862     -45.343   4.615 -10.219  1.00 19.71           C  
-ANISOU 1482  CD2 HIS A 862     2463   2475   2550      8    -11   -201       C  
-ATOM   1483  CE1 HIS A 862     -43.959   5.314  -8.673  1.00 21.16           C  
-ANISOU 1483  CE1 HIS A 862     2644   2658   2736     18    -10   -214       C  
-ATOM   1484  NE2 HIS A 862     -44.357   4.249  -9.335  1.00 20.67           N  
-ANISOU 1484  NE2 HIS A 862     2586   2596   2671     14    -12   -209       N  
-ATOM   1485  N   GLY A 863     -44.317   6.276 -13.347  1.00 17.50           N  
-ANISOU 1485  N   GLY A 863     2183   2202   2264      1     -1   -194       N  
-ATOM   1486  CA  GLY A 863     -43.827   5.232 -14.222  1.00 17.79           C  
-ANISOU 1486  CA  GLY A 863     2223   2246   2289      3     -2   -201       C  
-ATOM   1487  C   GLY A 863     -43.152   4.103 -13.474  1.00 19.42           C  
-ANISOU 1487  C   GLY A 863     2428   2451   2499      6     -6   -214       C  
-ATOM   1488  O   GLY A 863     -42.591   4.313 -12.408  1.00 20.91           O  
-ANISOU 1488  O   GLY A 863     2613   2635   2696      8     -5   -218       O  
-ATOM   1489  N   SER A 864     -43.233   2.886 -14.021  1.00 20.46           N  
-ANISOU 1489  N   SER A 864     2564   2585   2625      9    -13   -222       N  
-ATOM   1490  CA  SER A 864     -42.640   1.691 -13.423  1.00 20.41           C  
-ANISOU 1490  CA  SER A 864     2559   2574   2624     15    -20   -234       C  
-ATOM   1491  C   SER A 864     -42.495   0.649 -14.521  1.00 21.77           C  
-ANISOU 1491  C   SER A 864     2735   2749   2789     19    -26   -246       C  
-ATOM   1492  O   SER A 864     -43.132   0.758 -15.572  1.00 24.09           O  
-ANISOU 1492  O   SER A 864     3031   3049   3072     19    -28   -245       O  
-ATOM   1493  CB  SER A 864     -43.542   1.145 -12.344  1.00 20.10           C  
-ANISOU 1493  CB  SER A 864     2523   2522   2592     13    -27   -226       C  
-ATOM   1494  OG  SER A 864     -42.890   0.189 -11.539  1.00 19.36           O  
-ANISOU 1494  OG  SER A 864     2433   2421   2502     19    -33   -232       O  
-ATOM   1495  N   ARG A 865     -41.647  -0.338 -14.312  1.00 22.40           N  
-ANISOU 1495  N   ARG A 865     2814   2825   2873     27    -32   -260       N  
-ATOM   1496  CA  ARG A 865     -41.458  -1.418 -15.282  1.00 25.45           C  
-ANISOU 1496  CA  ARG A 865     3202   3213   3255     34    -40   -278       C  
-ATOM   1497  C   ARG A 865     -42.770  -2.193 -15.446  1.00 24.39           C  
-ANISOU 1497  C   ARG A 865     3075   3067   3127     31    -55   -276       C  
-ATOM   1498  O   ARG A 865     -43.517  -2.383 -14.491  1.00 24.12           O  
-ANISOU 1498  O   ARG A 865     3042   3018   3106     24    -60   -263       O  
-ATOM   1499  CB  ARG A 865     -40.369  -2.395 -14.835  1.00 27.67           C  
-ANISOU 1499  CB  ARG A 865     3480   3487   3545     45    -47   -294       C  
-ATOM   1500  CG  ARG A 865     -38.955  -1.880 -14.886  1.00 30.53           C  
-ANISOU 1500  CG  ARG A 865     3832   3862   3905     50    -35   -304       C  
-ATOM   1501  CD  ARG A 865     -38.019  -2.818 -14.108  1.00 34.57           C  
-ANISOU 1501  CD  ARG A 865     4341   4363   4430     63    -47   -319       C  
-ATOM   1502  NE  ARG A 865     -36.740  -2.186 -13.838  1.00 37.45           N  
-ANISOU 1502  NE  ARG A 865     4690   4738   4799     66    -37   -328       N  
-ATOM   1503  CZ  ARG A 865     -35.695  -2.229 -14.643  1.00 37.23           C  
-ANISOU 1503  CZ  ARG A 865     4650   4726   4770     73    -27   -347       C  
-ATOM   1504  NH1 ARG A 865     -34.602  -1.567 -14.323  1.00 40.07           N  
-ANISOU 1504  NH1 ARG A 865     4992   5094   5140     73    -18   -354       N  
-ATOM   1505  NH2 ARG A 865     -35.744  -2.892 -15.779  1.00 41.93           N  
-ANISOU 1505  NH2 ARG A 865     5246   5329   5354     80    -27   -360       N  
-ATOM   1506  N   THR A 866     -43.009  -2.638 -16.665  1.00 23.04           N  
-ANISOU 1506  N   THR A 866     2905   2903   2947     36    -63   -290       N  
-ATOM   1507  CA  THR A 866     -44.211  -3.380 -17.026  1.00 22.99           C  
-ANISOU 1507  CA  THR A 866     2901   2885   2950     33    -81   -294       C  
-ATOM   1508  C   THR A 866     -44.448  -4.585 -16.156  1.00 22.14           C  
-ANISOU 1508  C   THR A 866     2794   2750   2867     30    -94   -295       C  
-ATOM   1509  O   THR A 866     -45.595  -4.866 -15.764  1.00 24.10           O  
-ANISOU 1509  O   THR A 866     3040   2984   3132     19   -101   -285       O  
-ATOM   1510  CB  THR A 866     -44.147  -3.776 -18.503  1.00 23.14           C  
-ANISOU 1510  CB  THR A 866     2923   2917   2952     44    -90   -316       C  
-ATOM   1511  OG1 THR A 866     -43.961  -2.593 -19.251  1.00 27.12           O  
-ANISOU 1511  OG1 THR A 866     3428   3445   3430     46    -75   -308       O  
-ATOM   1512  CG2 THR A 866     -45.437  -4.422 -18.978  1.00 24.58           C  
-ANISOU 1512  CG2 THR A 866     3106   3089   3146     41   -112   -325       C  
-ATOM   1513  N   THR A 867     -43.371  -5.272 -15.808  1.00 21.68           N  
-ANISOU 1513  N   THR A 867     2737   2685   2813     39    -96   -306       N  
-ATOM   1514  CA  THR A 867     -43.446  -6.465 -14.975  1.00 21.52           C  
-ANISOU 1514  CA  THR A 867     2721   2637   2817     38   -109   -304       C  
-ATOM   1515  C   THR A 867     -43.840  -6.198 -13.533  1.00 22.15           C  
-ANISOU 1515  C   THR A 867     2804   2707   2906     28   -101   -276       C  
-ATOM   1516  O   THR A 867     -44.068  -7.130 -12.765  1.00 27.21           O  
-ANISOU 1516  O   THR A 867     3451   3324   3565     25   -109   -267       O  
-ATOM   1517  CB  THR A 867     -42.108  -7.221 -15.017  1.00 21.53           C  
-ANISOU 1517  CB  THR A 867     2724   2635   2821     54   -116   -324       C  
-ATOM   1518  OG1 THR A 867     -41.031  -6.328 -14.715  1.00 20.53           O  
-ANISOU 1518  OG1 THR A 867     2593   2527   2680     60   -101   -323       O  
-ATOM   1519  CG2 THR A 867     -41.873  -7.859 -16.423  1.00 19.55           C  
-ANISOU 1519  CG2 THR A 867     2471   2390   2565     66   -128   -357       C  
-ATOM   1520  N   ASN A 868     -43.931  -4.935 -13.149  1.00 22.67           N  
-ANISOU 1520  N   ASN A 868     2867   2789   2957     23    -85   -262       N  
-ATOM   1521  CA  ASN A 868     -44.440  -4.574 -11.854  1.00 22.73           C  
-ANISOU 1521  CA  ASN A 868     2876   2792   2968     16    -76   -238       C  
-ATOM   1522  C   ASN A 868     -45.959  -4.368 -11.805  1.00 22.24           C  
-ANISOU 1522  C   ASN A 868     2809   2727   2915      2    -72   -224       C  
-ATOM   1523  O   ASN A 868     -46.517  -4.264 -10.728  1.00 20.31           O  
-ANISOU 1523  O   ASN A 868     2565   2477   2673     -4    -64   -204       O  
-ATOM   1524  CB  ASN A 868     -43.797  -3.305 -11.355  1.00 23.66           C  
-ANISOU 1524  CB  ASN A 868     2992   2927   3070     20    -62   -234       C  
-ATOM   1525  CG  ASN A 868     -42.318  -3.439 -11.075  1.00 25.41           C  
-ANISOU 1525  CG  ASN A 868     3215   3152   3289     33    -65   -246       C  
-ATOM   1526  OD1 ASN A 868     -41.581  -2.470 -11.255  1.00 28.97           O  
-ANISOU 1526  OD1 ASN A 868     3658   3617   3730     36    -56   -253       O  
-ATOM   1527  ND2 ASN A 868     -41.870  -4.580 -10.621  1.00 25.48           N  
-ANISOU 1527  ND2 ASN A 868     3230   3144   3306     41    -77   -250       N  
-ATOM   1528  N   PHE A 869     -46.625  -4.265 -12.951  1.00 23.67           N  
-ANISOU 1528  N   PHE A 869     2984   2912   3097     -2    -79   -234       N  
-ATOM   1529  CA  PHE A 869     -48.003  -3.722 -12.958  1.00 23.74           C  
-ANISOU 1529  CA  PHE A 869     2983   2923   3112    -13    -75   -223       C  
-ATOM   1530  C   PHE A 869     -49.086  -4.639 -12.408  1.00 25.87           C  
-ANISOU 1530  C   PHE A 869     3248   3173   3409    -26    -79   -212       C  
-ATOM   1531  O   PHE A 869     -50.143  -4.156 -11.949  1.00 25.62           O  
-ANISOU 1531  O   PHE A 869     3206   3144   3383    -35    -69   -199       O  
-ATOM   1532  CB  PHE A 869     -48.372  -3.168 -14.302  1.00 23.64           C  
-ANISOU 1532  CB  PHE A 869     2967   2924   3090    -10    -83   -236       C  
-ATOM   1533  CG  PHE A 869     -48.025  -1.730 -14.426  1.00 24.15           C  
-ANISOU 1533  CG  PHE A 869     3032   3009   3134     -5    -70   -230       C  
-ATOM   1534  CD1 PHE A 869     -46.759  -1.337 -14.740  1.00 23.16           C  
-ANISOU 1534  CD1 PHE A 869     2914   2895   2993      4    -64   -236       C  
-ATOM   1535  CD2 PHE A 869     -48.958  -0.760 -14.135  1.00 25.59           C  
-ANISOU 1535  CD2 PHE A 869     3208   3197   3318    -10    -64   -218       C  
-ATOM   1536  CE1 PHE A 869     -46.427   0.000 -14.813  1.00 23.77           C  
-ANISOU 1536  CE1 PHE A 869     2990   2985   3056      5    -51   -228       C  
-ATOM   1537  CE2 PHE A 869     -48.617   0.586 -14.189  1.00 25.48           C  
-ANISOU 1537  CE2 PHE A 869     3196   3196   3291     -6    -54   -211       C  
-ATOM   1538  CZ  PHE A 869     -47.350   0.959 -14.525  1.00 23.39           C  
-ANISOU 1538  CZ  PHE A 869     2938   2939   3011      1    -48   -216       C  
-ATOM   1539  N   ALA A 870     -48.843  -5.931 -12.412  1.00 24.62           N  
-ANISOU 1539  N   ALA A 870     3094   2992   3267    -27    -91   -217       N  
-ATOM   1540  CA  ALA A 870     -49.796  -6.819 -11.764  1.00 25.69           C  
-ANISOU 1540  CA  ALA A 870     3225   3105   3432    -42    -91   -202       C  
-ATOM   1541  C   ALA A 870     -49.789  -6.565 -10.295  1.00 23.50           C  
-ANISOU 1541  C   ALA A 870     2952   2829   3147    -45    -70   -174       C  
-ATOM   1542  O   ALA A 870     -50.821  -6.563  -9.651  1.00 25.96           O  
-ANISOU 1542  O   ALA A 870     3255   3137   3472    -59    -57   -155       O  
-ATOM   1543  CB  ALA A 870     -49.474  -8.280 -12.062  1.00 27.28           C  
-ANISOU 1543  CB  ALA A 870     3432   3278   3657    -42   -110   -213       C  
-ATOM   1544  N   GLY A 871     -48.605  -6.363  -9.752  1.00 22.67           N  
-ANISOU 1544  N   GLY A 871     2862   2731   3022    -32    -67   -172       N  
-ATOM   1545  CA  GLY A 871     -48.441  -6.078  -8.356  1.00 21.53           C  
-ANISOU 1545  CA  GLY A 871     2725   2592   2864    -29    -50   -149       C  
-ATOM   1546  C   GLY A 871     -49.068  -4.726  -8.044  1.00 22.28           C  
-ANISOU 1546  C   GLY A 871     2810   2710   2944    -31    -33   -144       C  
-ATOM   1547  O   GLY A 871     -49.786  -4.596  -7.052  1.00 24.58           O  
-ANISOU 1547  O   GLY A 871     3099   3005   3234    -37    -17   -123       O  
-ATOM   1548  N   ILE A 872     -48.781  -3.715  -8.854  1.00 20.31           N  
-ANISOU 1548  N   ILE A 872     2556   2479   2684    -25    -36   -161       N  
-ATOM   1549  CA  ILE A 872     -49.327  -2.378  -8.615  1.00 20.74           C  
-ANISOU 1549  CA  ILE A 872     2600   2551   2727    -25    -24   -158       C  
-ATOM   1550  C   ILE A 872     -50.856  -2.372  -8.699  1.00 21.51           C  
-ANISOU 1550  C   ILE A 872     2682   2648   2842    -38    -18   -151       C  
-ATOM   1551  O   ILE A 872     -51.492  -1.786  -7.882  1.00 21.68           O  
-ANISOU 1551  O   ILE A 872     2697   2680   2860    -39     -2   -140       O  
-ATOM   1552  CB  ILE A 872     -48.766  -1.367  -9.608  1.00 21.04           C  
-ANISOU 1552  CB  ILE A 872     2638   2604   2755    -17    -29   -175       C  
-ATOM   1553  CG1 ILE A 872     -47.272  -1.132  -9.311  1.00 20.96           C  
-ANISOU 1553  CG1 ILE A 872     2637   2598   2729     -5    -30   -183       C  
-ATOM   1554  CG2 ILE A 872     -49.526  -0.049  -9.566  1.00 20.40           C  
-ANISOU 1554  CG2 ILE A 872     2546   2536   2669    -18    -21   -173       C  
-ATOM   1555  CD1 ILE A 872     -46.553  -0.449 -10.446  1.00 19.94           C  
-ANISOU 1555  CD1 ILE A 872     2507   2478   2593     -1    -34   -198       C  
-ATOM   1556  N   LEU A 873     -51.440  -3.025  -9.690  1.00 22.92           N  
-ANISOU 1556  N   LEU A 873     2853   2816   3041    -46    -31   -159       N  
-ATOM   1557  CA  LEU A 873     -52.849  -3.040  -9.774  1.00 23.64           C  
-ANISOU 1557  CA  LEU A 873     2925   2905   3153    -59    -28   -155       C  
-ATOM   1558  C   LEU A 873     -53.465  -3.806  -8.636  1.00 24.55           C  
-ANISOU 1558  C   LEU A 873     3036   3009   3284    -72    -12   -132       C  
-ATOM   1559  O   LEU A 873     -54.465  -3.369  -8.067  1.00 22.61           O  
-ANISOU 1559  O   LEU A 873     2775   2773   3044    -78      5   -122       O  
-ATOM   1560  CB  LEU A 873     -53.326  -3.562 -11.140  1.00 25.15           C  
-ANISOU 1560  CB  LEU A 873     3107   3086   3362    -63    -51   -174       C  
-ATOM   1561  CG  LEU A 873     -52.959  -2.627 -12.284  1.00 26.08           C  
-ANISOU 1561  CG  LEU A 873     3229   3220   3461    -50    -63   -192       C  
-ATOM   1562  CD1 LEU A 873     -53.493  -3.214 -13.574  1.00 28.00           C  
-ANISOU 1562  CD1 LEU A 873     3464   3456   3718    -51    -87   -211       C  
-ATOM   1563  CD2 LEU A 873     -53.498  -1.209 -12.108  1.00 25.49           C  
-ANISOU 1563  CD2 LEU A 873     3145   3163   3376    -46    -53   -187       C  
-ATOM   1564  N   SER A 874     -52.903  -4.950  -8.274  1.00 25.30           N  
-ANISOU 1564  N   SER A 874     3144   3084   3385    -75    -15   -123       N  
-ATOM   1565  CA  SER A 874     -53.536  -5.713  -7.217  1.00 26.48           C  
-ANISOU 1565  CA  SER A 874     3291   3221   3550    -88      3    -96       C  
-ATOM   1566  C   SER A 874     -53.250  -5.116  -5.842  1.00 26.56           C  
-ANISOU 1566  C   SER A 874     3312   3250   3530    -79     26    -76       C  
-ATOM   1567  O   SER A 874     -54.109  -5.204  -4.966  1.00 26.08           O  
-ANISOU 1567  O   SER A 874     3243   3194   3474    -89     49    -54       O  
-ATOM   1568  CB  SER A 874     -53.166  -7.201  -7.267  1.00 29.30           C  
-ANISOU 1568  CB  SER A 874     3658   3545   3929    -95    -10    -89       C  
-ATOM   1569  OG  SER A 874     -51.875  -7.401  -6.773  1.00 31.00           O  
-ANISOU 1569  OG  SER A 874     3899   3759   4121    -80    -14    -85       O  
-ATOM   1570  N   GLN A 875     -52.096  -4.483  -5.637  1.00 26.19           N  
-ANISOU 1570  N   GLN A 875     3282   3217   3453    -60     21    -85       N  
-ATOM   1571  CA  GLN A 875     -51.766  -3.984  -4.275  1.00 29.46           C  
-ANISOU 1571  CA  GLN A 875     3708   3649   3837    -48     39    -70       C  
-ATOM   1572  C   GLN A 875     -51.580  -2.478  -4.168  1.00 27.59           C  
-ANISOU 1572  C   GLN A 875     3467   3438   3578    -34     43    -86       C  
-ATOM   1573  O   GLN A 875     -51.395  -1.966  -3.087  1.00 27.77           O  
-ANISOU 1573  O   GLN A 875     3497   3477   3577    -23     56    -79       O  
-ATOM   1574  CB  GLN A 875     -50.490  -4.636  -3.769  1.00 33.89           C  
-ANISOU 1574  CB  GLN A 875     4294   4200   4383    -35     29    -65       C  
-ATOM   1575  CG  GLN A 875     -50.476  -6.140  -3.795  1.00 38.13           C  
-ANISOU 1575  CG  GLN A 875     4840   4706   4942    -45     22    -48       C  
-ATOM   1576  CD  GLN A 875     -49.316  -6.736  -3.023  1.00 46.67           C  
-ANISOU 1576  CD  GLN A 875     5947   5779   6006    -29     13    -38       C  
-ATOM   1577  OE1 GLN A 875     -48.389  -6.037  -2.586  1.00 52.43           O  
-ANISOU 1577  OE1 GLN A 875     6686   6527   6707     -9      9    -49       O  
-ATOM   1578  NE2 GLN A 875     -49.327  -8.051  -2.922  1.00 49.21           N  
-ANISOU 1578  NE2 GLN A 875     6278   6071   6348    -37      7    -20       N  
-ATOM   1579  N   GLY A 876     -51.613  -1.768  -5.285  1.00 25.34           N  
-ANISOU 1579  N   GLY A 876     3172   3156   3301    -34     31   -107       N  
-ATOM   1580  CA  GLY A 876     -51.442  -0.303  -5.262  1.00 24.15           C  
-ANISOU 1580  CA  GLY A 876     3017   3025   3135    -22     33   -121       C  
-ATOM   1581  C   GLY A 876     -49.970   0.067  -5.160  1.00 22.83           C  
-ANISOU 1581  C   GLY A 876     2864   2860   2949     -7     22   -133       C  
-ATOM   1582  O   GLY A 876     -49.119  -0.805  -5.001  1.00 21.56           O  
-ANISOU 1582  O   GLY A 876     2717   2689   2785     -4     14   -130       O  
-ATOM   1583  N   LEU A 877     -49.681   1.352  -5.297  1.00 21.34           N  
-ANISOU 1583  N   LEU A 877     2672   2683   2754      1     20   -147       N  
-ATOM   1584  CA  LEU A 877     -48.337   1.846  -5.127  1.00 20.56           C  
-ANISOU 1584  CA  LEU A 877     2582   2587   2642     14     12   -160       C  
-ATOM   1585  C   LEU A 877     -47.974   1.709  -3.646  1.00 22.09           C  
-ANISOU 1585  C   LEU A 877     2787   2789   2817     26     18   -154       C  
-ATOM   1586  O   LEU A 877     -48.798   1.975  -2.773  1.00 21.67           O  
-ANISOU 1586  O   LEU A 877     2732   2747   2755     28     32   -146       O  
-ATOM   1587  CB  LEU A 877     -48.231   3.282  -5.577  1.00 19.18           C  
-ANISOU 1587  CB  LEU A 877     2399   2418   2469     18     10   -174       C  
-ATOM   1588  CG  LEU A 877     -48.406   3.492  -7.058  1.00 18.74           C  
-ANISOU 1588  CG  LEU A 877     2338   2357   2427      9      3   -178       C  
-ATOM   1589  CD1 LEU A 877     -48.349   4.949  -7.412  1.00 18.29           C  
-ANISOU 1589  CD1 LEU A 877     2274   2303   2372     13      2   -186       C  
-ATOM   1590  CD2 LEU A 877     -47.378   2.713  -7.841  1.00 20.13           C  
-ANISOU 1590  CD2 LEU A 877     2521   2526   2603      8     -6   -183       C  
-ATOM   1591  N   ARG A 878     -46.762   1.253  -3.395  1.00 22.46           N  
-ANISOU 1591  N   ARG A 878     2846   2831   2856     35      6   -159       N  
-ATOM   1592  CA  ARG A 878     -46.287   0.998  -2.046  1.00 25.95           C  
-ANISOU 1592  CA  ARG A 878     3302   3280   3276     50      6   -154       C  
-ATOM   1593  C   ARG A 878     -44.976   1.715  -1.804  1.00 24.36           C  
-ANISOU 1593  C   ARG A 878     3103   3084   3069     65     -8   -176       C  
-ATOM   1594  O   ARG A 878     -44.365   2.218  -2.714  1.00 21.51           O  
-ANISOU 1594  O   ARG A 878     2732   2719   2722     61    -16   -192       O  
-ATOM   1595  CB  ARG A 878     -46.106  -0.503  -1.825  1.00 29.65           C  
-ANISOU 1595  CB  ARG A 878     3785   3736   3745     48      3   -135       C  
-ATOM   1596  CG  ARG A 878     -47.421  -1.251  -1.596  1.00 34.03           C  
-ANISOU 1596  CG  ARG A 878     4340   4286   4305     34     20   -109       C  
-ATOM   1597  CD  ARG A 878     -47.384  -2.600  -2.302  1.00 39.84           C  
-ANISOU 1597  CD  ARG A 878     5079   4997   5062     22     12    -99       C  
-ATOM   1598  NE  ARG A 878     -47.308  -2.395  -3.760  1.00 45.10           N  
-ANISOU 1598  NE  ARG A 878     5732   5656   5749     13      1   -119       N  
-ATOM   1599  CZ  ARG A 878     -46.739  -3.223  -4.647  1.00 47.74           C  
-ANISOU 1599  CZ  ARG A 878     6068   5972   6098     11    -15   -127       C  
-ATOM   1600  NH1 ARG A 878     -46.163  -4.369  -4.273  1.00 49.71           N  
-ANISOU 1600  NH1 ARG A 878     6333   6206   6351     16    -24   -119       N  
-ATOM   1601  NH2 ARG A 878     -46.736  -2.877  -5.924  1.00 46.21           N  
-ANISOU 1601  NH2 ARG A 878     5864   5779   5916      6    -21   -145       N  
-ATOM   1602  N   ILE A 879     -44.583   1.764  -0.544  1.00 25.25           N  
-ANISOU 1602  N   ILE A 879     3227   3209   3160     83    -12   -178       N  
-ATOM   1603  CA  ILE A 879     -43.354   2.417  -0.113  1.00 25.38           C  
-ANISOU 1603  CA  ILE A 879     3243   3229   3170    100    -29   -202       C  
-ATOM   1604  C   ILE A 879     -42.297   1.328   0.206  1.00 24.30           C  
-ANISOU 1604  C   ILE A 879     3120   3085   3027    111    -45   -200       C  
-ATOM   1605  O   ILE A 879     -42.614   0.266   0.723  1.00 22.46           O  
-ANISOU 1605  O   ILE A 879     2903   2848   2781    114    -43   -177       O  
-ATOM   1606  CB  ILE A 879     -43.678   3.276   1.132  1.00 27.12           C  
-ANISOU 1606  CB  ILE A 879     3467   3470   3368    117    -25   -210       C  
-ATOM   1607  CG1 ILE A 879     -44.586   4.455   0.754  1.00 27.66           C  
-ANISOU 1607  CG1 ILE A 879     3519   3542   3447    108    -13   -217       C  
-ATOM   1608  CG2 ILE A 879     -42.419   3.746   1.812  1.00 27.48           C  
-ANISOU 1608  CG2 ILE A 879     3515   3521   3406    137    -47   -236       C  
-ATOM   1609  CD1 ILE A 879     -45.141   5.181   1.956  1.00 28.59           C  
-ANISOU 1609  CD1 ILE A 879     3640   3681   3542    125     -6   -225       C  
-ATOM   1610  N   ALA A 880     -41.045   1.604  -0.090  1.00 24.43           N  
-ANISOU 1610  N   ALA A 880     3129   3098   3055    118    -63   -224       N  
-ATOM   1611  CA  ALA A 880     -39.951   0.691   0.235  1.00 24.74           C  
-ANISOU 1611  CA  ALA A 880     3178   3132   3091    133    -83   -228       C  
-ATOM   1612  C   ALA A 880     -39.953   0.240   1.703  1.00 25.98           C  
-ANISOU 1612  C   ALA A 880     3357   3298   3216    156    -90   -217       C  
-ATOM   1613  O   ALA A 880     -40.216   1.034   2.587  1.00 26.49           O  
-ANISOU 1613  O   ALA A 880     3425   3380   3261    167    -88   -223       O  
-ATOM   1614  CB  ALA A 880     -38.629   1.355  -0.100  1.00 24.68           C  
-ANISOU 1614  CB  ALA A 880     3153   3124   3102    139    -99   -260       C  
-ATOM   1615  N   PRO A 881     -39.597  -1.020   1.970  1.00 28.30           N  
-ANISOU 1615  N   PRO A 881     3668   3581   3503    165   -101   -201       N  
-ATOM   1616  CA  PRO A 881     -39.608  -1.486   3.355  1.00 30.54           C  
-ANISOU 1616  CA  PRO A 881     3978   3874   3753    187   -108   -185       C  
-ATOM   1617  C   PRO A 881     -38.477  -0.906   4.212  1.00 31.92           C  
-ANISOU 1617  C   PRO A 881     4154   4063   3912    216   -135   -214       C  
-ATOM   1618  O   PRO A 881     -37.458  -0.449   3.689  1.00 30.73           O  
-ANISOU 1618  O   PRO A 881     3983   3908   3785    218   -152   -246       O  
-ATOM   1619  CB  PRO A 881     -39.471  -3.011   3.233  1.00 30.65           C  
-ANISOU 1619  CB  PRO A 881     4009   3866   3772    187   -115   -160       C  
-ATOM   1620  CG  PRO A 881     -38.920  -3.274   1.898  1.00 31.18           C  
-ANISOU 1620  CG  PRO A 881     4057   3915   3875    174   -122   -178       C  
-ATOM   1621  CD  PRO A 881     -39.207  -2.080   1.018  1.00 30.55           C  
-ANISOU 1621  CD  PRO A 881     3951   3844   3812    156   -108   -197       C  
-ATOM   1622  N   PRO A 882     -38.642  -0.933   5.528  1.00 34.07           N  
-ANISOU 1622  N   PRO A 882     4448   4352   4145    239   -139   -205       N  
-ATOM   1623  CA  PRO A 882     -37.594  -0.481   6.494  1.00 35.45           C  
-ANISOU 1623  CA  PRO A 882     4627   4542   4300    271   -170   -233       C  
-ATOM   1624  C   PRO A 882     -36.209  -1.085   6.242  1.00 34.52           C  
-ANISOU 1624  C   PRO A 882     4505   4409   4201    285   -203   -252       C  
-ATOM   1625  O   PRO A 882     -35.195  -0.405   6.380  1.00 33.18           O  
-ANISOU 1625  O   PRO A 882     4319   4246   4042    299   -227   -291       O  
-ATOM   1626  CB  PRO A 882     -38.128  -0.948   7.853  1.00 37.56           C  
-ANISOU 1626  CB  PRO A 882     4928   4826   4515    294   -166   -205       C  
-ATOM   1627  CG  PRO A 882     -39.610  -1.131   7.658  1.00 40.29           C  
-ANISOU 1627  CG  PRO A 882     5279   5174   4857    269   -126   -169       C  
-ATOM   1628  CD  PRO A 882     -39.860  -1.425   6.187  1.00 37.28           C  
-ANISOU 1628  CD  PRO A 882     4876   4767   4522    235   -113   -165       C  
-ATOM   1629  N   GLU A 883     -36.169  -2.354   5.854  1.00 35.70           N  
-ANISOU 1629  N   GLU A 883     4667   4538   4359    280   -203   -227       N  
-ATOM   1630  CA  GLU A 883     -34.910  -3.061   5.635  1.00 39.82           C  
-ANISOU 1630  CA  GLU A 883     5185   5045   4900    296   -235   -243       C  
-ATOM   1631  C   GLU A 883     -34.116  -2.576   4.423  1.00 38.87           C  
-ANISOU 1631  C   GLU A 883     5028   4916   4823    281   -238   -279       C  
-ATOM   1632  O   GLU A 883     -32.891  -2.830   4.313  1.00 40.32           O  
-ANISOU 1632  O   GLU A 883     5199   5095   5025    297   -266   -305       O  
-ATOM   1633  CB  GLU A 883     -35.180  -4.561   5.453  1.00 43.51           C  
-ANISOU 1633  CB  GLU A 883     5674   5488   5369    294   -233   -207       C  
-ATOM   1634  CG  GLU A 883     -35.865  -5.234   6.636  1.00 47.04           C  
-ANISOU 1634  CG  GLU A 883     6161   5940   5774    308   -229   -164       C  
-ATOM   1635  CD  GLU A 883     -37.386  -5.174   6.624  1.00 49.64           C  
-ANISOU 1635  CD  GLU A 883     6497   6272   6092    282   -188   -128       C  
-ATOM   1636  OE1 GLU A 883     -37.970  -5.478   7.692  1.00 57.10           O  
-ANISOU 1636  OE1 GLU A 883     7470   7227   6997    293   -179    -95       O  
-ATOM   1637  OE2 GLU A 883     -38.003  -4.822   5.589  1.00 46.27           O  
-ANISOU 1637  OE2 GLU A 883     6047   5839   5693    252   -166   -133       O  
-ATOM   1638  N   ALA A 884     -34.807  -1.942   3.482  1.00 36.20           N  
-ANISOU 1638  N   ALA A 884     4672   4578   4505    251   -210   -278       N  
-ATOM   1639  CA  ALA A 884     -34.147  -1.482   2.284  1.00 34.80           C  
-ANISOU 1639  CA  ALA A 884     4462   4395   4365    235   -208   -306       C  
-ATOM   1640  C   ALA A 884     -33.220  -0.322   2.608  1.00 33.77           C  
-ANISOU 1640  C   ALA A 884     4309   4277   4246    246   -224   -344       C  
-ATOM   1641  O   ALA A 884     -33.577   0.529   3.426  1.00 33.55           O  
-ANISOU 1641  O   ALA A 884     4286   4263   4199    253   -225   -350       O  
-ATOM   1642  CB  ALA A 884     -35.171  -1.063   1.243  1.00 35.39           C  
-ANISOU 1642  CB  ALA A 884     4527   4466   4453    203   -176   -292       C  
-ATOM   1643  N   PRO A 885     -32.055  -0.251   1.923  1.00 32.63           N  
-ANISOU 1643  N   PRO A 885     4137   4126   4133    245   -236   -374       N  
-ATOM   1644  CA  PRO A 885     -31.229   0.935   2.034  1.00 35.48           C  
-ANISOU 1644  CA  PRO A 885     4469   4495   4515    247   -247   -410       C  
-ATOM   1645  C   PRO A 885     -31.962   2.173   1.531  1.00 36.97           C  
-ANISOU 1645  C   PRO A 885     4646   4687   4714    221   -220   -408       C  
-ATOM   1646  O   PRO A 885     -32.730   2.071   0.573  1.00 41.35           O  
-ANISOU 1646  O   PRO A 885     5202   5236   5274    197   -193   -387       O  
-ATOM   1647  CB  PRO A 885     -30.006   0.636   1.144  1.00 34.79           C  
-ANISOU 1647  CB  PRO A 885     4352   4400   4465    244   -254   -434       C  
-ATOM   1648  CG  PRO A 885     -30.174  -0.739   0.625  1.00 34.26           C  
-ANISOU 1648  CG  PRO A 885     4301   4323   4394    246   -250   -413       C  
-ATOM   1649  CD  PRO A 885     -31.535  -1.221   0.945  1.00 33.15           C  
-ANISOU 1649  CD  PRO A 885     4194   4179   4222    241   -236   -374       C  
-ATOM   1650  N   VAL A 886     -31.745   3.297   2.196  1.00 36.93           N  
-ANISOU 1650  N   VAL A 886     4630   4690   4713    228   -231   -432       N  
-ATOM   1651  CA  VAL A 886     -32.374   4.570   1.840  1.00 40.45           C  
-ANISOU 1651  CA  VAL A 886     5063   5134   5171    207   -211   -434       C  
-ATOM   1652  C   VAL A 886     -31.602   5.239   0.711  1.00 40.84           C  
-ANISOU 1652  C   VAL A 886     5078   5173   5266    184   -202   -451       C  
-ATOM   1653  O   VAL A 886     -32.129   6.131   0.025  1.00 43.81           O  
-ANISOU 1653  O   VAL A 886     5445   5544   5658    161   -180   -443       O  
-ATOM   1654  CB  VAL A 886     -32.425   5.527   3.045  1.00 40.91           C  
-ANISOU 1654  CB  VAL A 886     5125   5203   5217    225   -230   -457       C  
-ATOM   1655  CG1 VAL A 886     -31.024   5.961   3.433  1.00 41.67           C  
-ANISOU 1655  CG1 VAL A 886     5195   5297   5340    239   -262   -499       C  
-ATOM   1656  CG2 VAL A 886     -33.287   6.753   2.723  1.00 44.77           C  
-ANISOU 1656  CG2 VAL A 886     5606   5688   5718    206   -210   -454       C  
-ATOM   1657  N   THR A 887     -30.378   4.781   0.494  1.00 43.26           N  
-ANISOU 1657  N   THR A 887     5366   5478   5594    191   -216   -471       N  
-ATOM   1658  CA  THR A 887     -29.505   5.320  -0.546  1.00 45.36           C  
-ANISOU 1658  CA  THR A 887     5595   5736   5903    171   -205   -487       C  
-ATOM   1659  C   THR A 887     -30.232   5.338  -1.901  1.00 37.89           C  
-ANISOU 1659  C   THR A 887     4650   4786   4960    142   -168   -458       C  
-ATOM   1660  O   THR A 887     -30.876   4.382  -2.304  1.00 36.36           O  
-ANISOU 1660  O   THR A 887     4477   4594   4745    141   -157   -434       O  
-ATOM   1661  CB  THR A 887     -28.117   4.595  -0.590  1.00 46.53           C  
-ANISOU 1661  CB  THR A 887     5722   5886   6071    185   -225   -512       C  
-ATOM   1662  OG1 THR A 887     -27.287   5.142   0.456  1.00 52.25           O  
-ANISOU 1662  OG1 THR A 887     6432   6613   6809    205   -258   -548       O  
-ATOM   1663  CG2 THR A 887     -27.426   4.811  -1.917  1.00 46.32           C  
-ANISOU 1663  CG2 THR A 887     5662   5855   6081    161   -201   -518       C  
-ATOM   1664  N   GLY A 888     -30.121   6.461  -2.583  1.00 32.78           N  
-ANISOU 1664  N   GLY A 888     3981   4133   4342    119   -150   -461       N  
-ATOM   1665  CA  GLY A 888     -30.825   6.670  -3.835  1.00 28.24           C  
-ANISOU 1665  CA  GLY A 888     3408   3554   3767     94   -118   -433       C  
-ATOM   1666  C   GLY A 888     -32.134   7.407  -3.663  1.00 25.45           C  
-ANISOU 1666  C   GLY A 888     3073   3197   3400     87   -109   -414       C  
-ATOM   1667  O   GLY A 888     -32.575   8.034  -4.594  1.00 25.68           O  
-ANISOU 1667  O   GLY A 888     3098   3220   3438     66    -86   -398       O  
-ATOM   1668  N   TYR A 889     -32.764   7.314  -2.494  1.00 25.50           N  
-ANISOU 1668  N   TYR A 889     3100   3208   3381    105   -125   -415       N  
-ATOM   1669  CA  TYR A 889     -33.997   8.046  -2.227  1.00 27.56           C  
-ANISOU 1669  CA  TYR A 889     3375   3467   3629    101   -117   -401       C  
-ATOM   1670  C   TYR A 889     -33.753   9.472  -1.797  1.00 25.77           C  
-ANISOU 1670  C   TYR A 889     3132   3232   3429     99   -126   -423       C  
-ATOM   1671  O   TYR A 889     -33.562   9.764  -0.631  1.00 27.47           O  
-ANISOU 1671  O   TYR A 889     3349   3451   3638    118   -149   -447       O  
-ATOM   1672  CB  TYR A 889     -34.843   7.350  -1.165  1.00 28.71           C  
-ANISOU 1672  CB  TYR A 889     3548   3624   3735    121   -126   -392       C  
-ATOM   1673  CG  TYR A 889     -35.565   6.144  -1.672  1.00 29.76           C  
-ANISOU 1673  CG  TYR A 889     3700   3760   3847    117   -112   -363       C  
-ATOM   1674  CD1 TYR A 889     -35.033   4.864  -1.531  1.00 33.86           C  
-ANISOU 1674  CD1 TYR A 889     4228   4282   4355    128   -122   -361       C  
-ATOM   1675  CD2 TYR A 889     -36.782   6.280  -2.294  1.00 33.94           C  
-ANISOU 1675  CD2 TYR A 889     4238   4288   4369    102    -91   -338       C  
-ATOM   1676  CE1 TYR A 889     -35.715   3.751  -2.006  1.00 35.64           C  
-ANISOU 1676  CE1 TYR A 889     4471   4506   4567    124   -112   -335       C  
-ATOM   1677  CE2 TYR A 889     -37.487   5.177  -2.755  1.00 32.60           C  
-ANISOU 1677  CE2 TYR A 889     4083   4119   4184     97    -81   -314       C  
-ATOM   1678  CZ  TYR A 889     -36.940   3.925  -2.626  1.00 33.60           C  
-ANISOU 1678  CZ  TYR A 889     4218   4246   4304    107    -91   -313       C  
-ATOM   1679  OH  TYR A 889     -37.657   2.853  -3.091  1.00 39.08           O  
-ANISOU 1679  OH  TYR A 889     4926   4937   4988    101    -83   -291       O  
-ATOM   1680  N   MET A 890     -33.809  10.367  -2.760  1.00 25.88           N  
-ANISOU 1680  N   MET A 890     3131   3232   3470     76   -108   -415       N  
-ATOM   1681  CA  MET A 890     -33.501  11.756  -2.559  1.00 24.85           C  
-ANISOU 1681  CA  MET A 890     2981   3085   3374     69   -115   -434       C  
-ATOM   1682  C   MET A 890     -34.331  12.382  -1.451  1.00 23.94           C  
-ANISOU 1682  C   MET A 890     2880   2972   3245     86   -130   -446       C  
-ATOM   1683  O   MET A 890     -33.834  13.241  -0.709  1.00 28.78           O  
-ANISOU 1683  O   MET A 890     3479   3576   3880     94   -151   -477       O  
-ATOM   1684  CB  MET A 890     -33.715  12.490  -3.866  1.00 25.28           C  
-ANISOU 1684  CB  MET A 890     3028   3126   3454     41    -89   -411       C  
-ATOM   1685  CG  MET A 890     -33.328  13.944  -3.801  1.00 29.87           C  
-ANISOU 1685  CG  MET A 890     3588   3683   4079     30    -95   -427       C  
-ATOM   1686  SD  MET A 890     -33.219  14.692  -5.426  1.00 34.79           S  
-ANISOU 1686  SD  MET A 890     4199   4288   4733     -4    -63   -395       S  
-ATOM   1687  CE  MET A 890     -32.632  16.332  -4.922  1.00 37.45           C  
-ANISOU 1687  CE  MET A 890     4508   4592   5128    -13    -78   -421       C  
-ATOM   1688  N   PHE A 891     -35.599  12.011  -1.342  1.00 22.08           N  
-ANISOU 1688  N   PHE A 891     2669   2747   2976     91   -120   -424       N  
-ATOM   1689  CA  PHE A 891     -36.461  12.583  -0.303  1.00 21.87           C  
-ANISOU 1689  CA  PHE A 891     2653   2725   2932    109   -130   -435       C  
-ATOM   1690  C   PHE A 891     -37.006  11.551   0.654  1.00 21.14           C  
-ANISOU 1690  C   PHE A 891     2585   2657   2792    131   -134   -430       C  
-ATOM   1691  O   PHE A 891     -38.096  11.692   1.207  1.00 21.24           O  
-ANISOU 1691  O   PHE A 891     2611   2679   2780    141   -129   -424       O  
-ATOM   1692  CB  PHE A 891     -37.562  13.403  -0.939  1.00 22.81           C  
-ANISOU 1692  CB  PHE A 891     2774   2832   3059     95   -113   -417       C  
-ATOM   1693  CG  PHE A 891     -37.048  14.546  -1.759  1.00 23.26           C  
-ANISOU 1693  CG  PHE A 891     2810   2863   3164     75   -110   -420       C  
-ATOM   1694  CD1 PHE A 891     -36.466  15.633  -1.156  1.00 23.68           C  
-ANISOU 1694  CD1 PHE A 891     2847   2901   3250     79   -130   -453       C  
-ATOM   1695  CD2 PHE A 891     -37.105  14.515  -3.128  1.00 24.85           C  
-ANISOU 1695  CD2 PHE A 891     3009   3055   3377     51    -88   -391       C  
-ATOM   1696  CE1 PHE A 891     -35.968  16.705  -1.892  1.00 23.29           C  
-ANISOU 1696  CE1 PHE A 891     2778   2822   3250     58   -126   -453       C  
-ATOM   1697  CE2 PHE A 891     -36.605  15.585  -3.883  1.00 26.54           C  
-ANISOU 1697  CE2 PHE A 891     3205   3244   3635     31    -83   -389       C  
-ATOM   1698  CZ  PHE A 891     -36.038  16.682  -3.251  1.00 25.02           C  
-ANISOU 1698  CZ  PHE A 891     2996   3032   3479     33   -101   -418       C  
-ATOM   1699  N   GLY A 892     -36.244  10.493   0.850  1.00 20.90           N  
-ANISOU 1699  N   GLY A 892     2558   2635   2749    139   -143   -431       N  
-ATOM   1700  CA  GLY A 892     -36.695   9.408   1.692  1.00 22.81           C  
-ANISOU 1700  CA  GLY A 892     2825   2896   2946    159   -145   -419       C  
-ATOM   1701  C   GLY A 892     -37.625   8.415   1.025  1.00 22.58           C  
-ANISOU 1701  C   GLY A 892     2812   2870   2899    147   -122   -380       C  
-ATOM   1702  O   GLY A 892     -38.001   8.539  -0.158  1.00 23.01           O  
-ANISOU 1702  O   GLY A 892     2858   2913   2970    124   -103   -363       O  
-ATOM   1703  N   LYS A 893     -37.978   7.426   1.804  1.00 22.95           N  
-ANISOU 1703  N   LYS A 893     2879   2930   2910    162   -123   -367       N  
-ATOM   1704  CA  LYS A 893     -38.828   6.359   1.359  1.00 24.48           C  
-ANISOU 1704  CA  LYS A 893     3089   3126   3089    152   -104   -333       C  
-ATOM   1705  C   LYS A 893     -40.226   6.858   1.266  1.00 24.66           C  
-ANISOU 1705  C   LYS A 893     3113   3152   3104    143    -84   -318       C  
-ATOM   1706  O   LYS A 893     -40.806   7.166   2.252  1.00 26.77           O  
-ANISOU 1706  O   LYS A 893     3389   3434   3350    158    -83   -321       O  
-ATOM   1707  CB  LYS A 893     -38.707   5.182   2.291  1.00 24.12           C  
-ANISOU 1707  CB  LYS A 893     3064   3089   3010    171   -113   -321       C  
-ATOM   1708  CG  LYS A 893     -37.334   4.499   2.199  1.00 25.87           C  
-ANISOU 1708  CG  LYS A 893     3283   3304   3242    180   -135   -334       C  
-ATOM   1709  CD  LYS A 893     -37.211   3.400   3.257  1.00 28.66           C  
-ANISOU 1709  CD  LYS A 893     3662   3667   3561    204   -148   -322       C  
-ATOM   1710  CE  LYS A 893     -35.791   2.819   3.334  1.00 30.47           C  
-ANISOU 1710  CE  LYS A 893     3887   3889   3800    219   -176   -340       C  
-ATOM   1711  NZ  LYS A 893     -35.841   1.580   4.158  1.00 35.94           N  
-ANISOU 1711  NZ  LYS A 893     4609   4585   4460    239   -185   -318       N  
-ATOM   1712  N   GLY A 894     -40.741   6.981   0.046  1.00 23.17           N  
-ANISOU 1712  N   GLY A 894     2915   2952   2935    121    -68   -304       N  
-ATOM   1713  CA  GLY A 894     -42.090   7.422  -0.167  1.00 21.13           C  
-ANISOU 1713  CA  GLY A 894     2657   2697   2676    113    -51   -290       C  
-ATOM   1714  C   GLY A 894     -42.527   6.969  -1.550  1.00 21.22           C  
-ANISOU 1714  C   GLY A 894     2663   2696   2701     91    -39   -270       C  
-ATOM   1715  O   GLY A 894     -41.812   6.191  -2.202  1.00 20.73           O  
-ANISOU 1715  O   GLY A 894     2602   2628   2646     84    -42   -266       O  
-ATOM   1716  N   ILE A 895     -43.660   7.496  -2.017  1.00 18.81           N  
-ANISOU 1716  N   ILE A 895     2353   2390   2402     81    -27   -261       N  
-ATOM   1717  CA  ILE A 895     -44.099   7.262  -3.361  1.00 19.52           C  
-ANISOU 1717  CA  ILE A 895     2439   2471   2506     64    -19   -246       C  
-ATOM   1718  C   ILE A 895     -43.857   8.547  -4.130  1.00 19.57           C  
-ANISOU 1718  C   ILE A 895     2434   2467   2535     57    -21   -254       C  
-ATOM   1719  O   ILE A 895     -44.333   9.597  -3.729  1.00 19.60           O  
-ANISOU 1719  O   ILE A 895     2433   2470   2545     62    -22   -263       O  
-ATOM   1720  CB  ILE A 895     -45.592   6.878  -3.432  1.00 19.53           C  
-ANISOU 1720  CB  ILE A 895     2441   2477   2500     58     -6   -228       C  
-ATOM   1721  CG1 ILE A 895     -45.888   5.715  -2.501  1.00 19.19           C  
-ANISOU 1721  CG1 ILE A 895     2410   2443   2437     64     -1   -215       C  
-ATOM   1722  CG2 ILE A 895     -45.972   6.503  -4.842  1.00 19.82           C  
-ANISOU 1722  CG2 ILE A 895     2475   2506   2549     42     -3   -216       C  
-ATOM   1723  CD1 ILE A 895     -47.369   5.530  -2.263  1.00 20.09           C  
-ANISOU 1723  CD1 ILE A 895     2522   2566   2547     60     15   -201       C  
-ATOM   1724  N   TYR A 896     -43.151   8.421  -5.249  1.00 18.56           N  
-ANISOU 1724  N   TYR A 896     2302   2331   2419     45    -20   -251       N  
-ATOM   1725  CA  TYR A 896     -42.668   9.515  -6.029  1.00 18.63           C  
-ANISOU 1725  CA  TYR A 896     2302   2328   2449     37    -20   -255       C  
-ATOM   1726  C   TYR A 896     -43.498   9.679  -7.302  1.00 18.50           C  
-ANISOU 1726  C   TYR A 896     2286   2308   2436     26    -12   -236       C  
-ATOM   1727  O   TYR A 896     -43.822   8.691  -7.966  1.00 19.55           O  
-ANISOU 1727  O   TYR A 896     2425   2446   2558     21     -9   -225       O  
-ATOM   1728  CB  TYR A 896     -41.195   9.243  -6.424  1.00 20.08           C  
-ANISOU 1728  CB  TYR A 896     2479   2509   2642     33    -22   -263       C  
-ATOM   1729  CG  TYR A 896     -40.199   9.423  -5.328  1.00 19.22           C  
-ANISOU 1729  CG  TYR A 896     2364   2401   2539     44    -35   -286       C  
-ATOM   1730  CD1 TYR A 896     -40.194   8.593  -4.241  1.00 19.54           C  
-ANISOU 1730  CD1 TYR A 896     2413   2451   2559     59    -44   -292       C  
-ATOM   1731  CD2 TYR A 896     -39.248  10.433  -5.384  1.00 20.11           C  
-ANISOU 1731  CD2 TYR A 896     2461   2502   2678     40    -39   -301       C  
-ATOM   1732  CE1 TYR A 896     -39.306   8.765  -3.211  1.00 19.82           C  
-ANISOU 1732  CE1 TYR A 896     2445   2489   2596     73    -59   -315       C  
-ATOM   1733  CE2 TYR A 896     -38.316  10.600  -4.346  1.00 19.88           C  
-ANISOU 1733  CE2 TYR A 896     2424   2474   2656     52    -55   -327       C  
-ATOM   1734  CZ  TYR A 896     -38.351   9.755  -3.285  1.00 19.65           C  
-ANISOU 1734  CZ  TYR A 896     2406   2457   2602     70    -66   -335       C  
-ATOM   1735  OH  TYR A 896     -37.500   9.889  -2.233  1.00 19.41           O  
-ANISOU 1735  OH  TYR A 896     2370   2430   2573     86    -86   -361       O  
-ATOM   1736  N   PHE A 897     -43.761  10.930  -7.668  1.00 18.07           N  
-ANISOU 1736  N   PHE A 897     2226   2242   2397     23    -12   -234       N  
-ATOM   1737  CA  PHE A 897     -44.532  11.315  -8.831  1.00 17.62           C  
-ANISOU 1737  CA  PHE A 897     2172   2180   2343     16     -8   -217       C  
-ATOM   1738  C   PHE A 897     -43.921  12.531  -9.502  1.00 17.48           C  
-ANISOU 1738  C   PHE A 897     2149   2146   2345      8     -6   -212       C  
-ATOM   1739  O   PHE A 897     -43.247  13.320  -8.863  1.00 18.22           O  
-ANISOU 1739  O   PHE A 897     2235   2229   2458      9    -10   -225       O  
-ATOM   1740  CB  PHE A 897     -45.951  11.732  -8.437  1.00 17.71           C  
-ANISOU 1740  CB  PHE A 897     2183   2192   2354     23    -11   -215       C  
-ATOM   1741  CG  PHE A 897     -46.736  10.646  -7.761  1.00 18.39           C  
-ANISOU 1741  CG  PHE A 897     2271   2293   2422     28     -9   -216       C  
-ATOM   1742  CD1 PHE A 897     -46.668  10.477  -6.413  1.00 17.94           C  
-ANISOU 1742  CD1 PHE A 897     2214   2244   2358     38     -9   -228       C  
-ATOM   1743  CD2 PHE A 897     -47.582   9.796  -8.508  1.00 19.05           C  
-ANISOU 1743  CD2 PHE A 897     2357   2382   2498     23     -7   -203       C  
-ATOM   1744  CE1 PHE A 897     -47.419   9.504  -5.787  1.00 17.53           C  
-ANISOU 1744  CE1 PHE A 897     2164   2205   2290     41     -3   -223       C  
-ATOM   1745  CE2 PHE A 897     -48.337   8.821  -7.894  1.00 17.88           C  
-ANISOU 1745  CE2 PHE A 897     2208   2244   2341     24     -3   -201       C  
-ATOM   1746  CZ  PHE A 897     -48.217   8.656  -6.533  1.00 18.87           C  
-ANISOU 1746  CZ  PHE A 897     2335   2377   2458     33      0   -209       C  
-ATOM   1747  N   ALA A 898     -44.168  12.670 -10.791  1.00 16.59           N  
-ANISOU 1747  N   ALA A 898     2043   2031   2230      1     -1   -192       N  
-ATOM   1748  CA  ALA A 898     -43.670  13.796 -11.579  1.00 17.01           C  
-ANISOU 1748  CA  ALA A 898     2093   2067   2300     -8      4   -179       C  
-ATOM   1749  C   ALA A 898     -44.854  14.538 -12.219  1.00 17.01           C  
-ANISOU 1749  C   ALA A 898     2101   2059   2302     -5     -2   -162       C  
-ATOM   1750  O   ALA A 898     -45.939  13.936 -12.405  1.00 15.37           O  
-ANISOU 1750  O   ALA A 898     1899   1863   2078      2     -7   -160       O  
-ATOM   1751  CB  ALA A 898     -42.798  13.284 -12.684  1.00 17.56           C  
-ANISOU 1751  CB  ALA A 898     2166   2146   2360    -18     17   -167       C  
-ATOM   1752  N   ASP A 899     -44.655  15.819 -12.530  1.00 17.61           N  
-ANISOU 1752  N   ASP A 899     2176   2113   2400     -9     -2   -152       N  
-ATOM   1753  CA  ASP A 899     -45.610  16.564 -13.356  1.00 18.47           C  
-ANISOU 1753  CA  ASP A 899     2296   2212   2512     -5     -8   -131       C  
-ATOM   1754  C   ASP A 899     -45.137  16.640 -14.794  1.00 19.18           C  
-ANISOU 1754  C   ASP A 899     2397   2302   2589    -14      4   -102       C  
-ATOM   1755  O   ASP A 899     -45.864  17.164 -15.649  1.00 19.47           O  
-ANISOU 1755  O   ASP A 899     2446   2332   2621    -10     -2    -80       O  
-ATOM   1756  CB  ASP A 899     -45.981  17.924 -12.796  1.00 19.23           C  
-ANISOU 1756  CB  ASP A 899     2387   2281   2639      1    -20   -135       C  
-ATOM   1757  CG  ASP A 899     -44.779  18.849 -12.565  1.00 21.23           C  
-ANISOU 1757  CG  ASP A 899     2632   2509   2924    -11    -15   -137       C  
-ATOM   1758  OD1 ASP A 899     -43.702  18.660 -13.163  1.00 23.86           O  
-ANISOU 1758  OD1 ASP A 899     2964   2844   3257    -26      1   -125       O  
-ATOM   1759  OD2 ASP A 899     -44.929  19.768 -11.721  1.00 22.03           O  
-ANISOU 1759  OD2 ASP A 899     2725   2590   3054     -5    -27   -154       O  
-ATOM   1760  N   MET A 900     -43.951  16.093 -15.082  1.00 19.94           N  
-ANISOU 1760  N   MET A 900     2489   2408   2678    -26     20   -102       N  
-ATOM   1761  CA  MET A 900     -43.459  15.960 -16.453  1.00 20.91           C  
-ANISOU 1761  CA  MET A 900     2623   2541   2782    -33     36    -77       C  
-ATOM   1762  C   MET A 900     -43.513  14.482 -16.858  1.00 20.60           C  
-ANISOU 1762  C   MET A 900     2587   2531   2708    -28     38    -86       C  
-ATOM   1763  O   MET A 900     -42.818  13.662 -16.272  1.00 19.62           O  
-ANISOU 1763  O   MET A 900     2453   2418   2585    -30     43   -106       O  
-ATOM   1764  CB  MET A 900     -42.009  16.474 -16.582  1.00 24.10           C  
-ANISOU 1764  CB  MET A 900     3016   2935   3207    -50     57    -70       C  
-ATOM   1765  CG  MET A 900     -41.812  17.924 -16.140  1.00 27.65           C  
-ANISOU 1765  CG  MET A 900     3458   3349   3699    -58     53    -64       C  
-ATOM   1766  SD  MET A 900     -42.451  19.088 -17.304  1.00 32.46           S  
-ANISOU 1766  SD  MET A 900     4087   3937   4309    -59     54    -21       S  
-ATOM   1767  CE  MET A 900     -41.183  19.091 -18.591  1.00 28.61           C  
-ANISOU 1767  CE  MET A 900     3602   3459   3809    -78     90     12       C  
-ATOM   1768  N   VAL A 901     -44.268  14.162 -17.910  1.00 19.33           N  
-ANISOU 1768  N   VAL A 901     2442   2384   2519    -20     34    -72       N  
-ATOM   1769  CA  VAL A 901     -44.456  12.774 -18.319  1.00 18.82           C  
-ANISOU 1769  CA  VAL A 901     2382   2344   2426    -13     31    -84       C  
-ATOM   1770  C   VAL A 901     -43.146  12.031 -18.528  1.00 20.04           C  
-ANISOU 1770  C   VAL A 901     2530   2513   2572    -20     50    -93       C  
-ATOM   1771  O   VAL A 901     -43.024  10.872 -18.149  1.00 21.32           O  
-ANISOU 1771  O   VAL A 901     2687   2687   2727    -16     45   -114       O  
-ATOM   1772  CB  VAL A 901     -45.358  12.651 -19.574  1.00 18.57           C  
-ANISOU 1772  CB  VAL A 901     2368   2325   2365     -2     22    -69       C  
-ATOM   1773  CG1 VAL A 901     -44.707  13.229 -20.822  1.00 18.55           C  
-ANISOU 1773  CG1 VAL A 901     2378   2327   2343     -5     39    -41       C  
-ATOM   1774  CG2 VAL A 901     -45.751  11.227 -19.825  1.00 19.32           C  
-ANISOU 1774  CG2 VAL A 901     2464   2440   2438      5     12    -88       C  
-ATOM   1775  N   SER A 902     -42.161  12.683 -19.126  1.00 21.12           N  
-ANISOU 1775  N   SER A 902     2666   2649   2712    -30     71    -76       N  
-ATOM   1776  CA  SER A 902     -40.909  12.012 -19.466  1.00 20.70           C  
-ANISOU 1776  CA  SER A 902     2604   2613   2650    -35     91    -84       C  
-ATOM   1777  C   SER A 902     -40.073  11.663 -18.242  1.00 21.13           C  
-ANISOU 1777  C   SER A 902     2636   2660   2730    -40     90   -111       C  
-ATOM   1778  O   SER A 902     -39.431  10.626 -18.204  1.00 21.60           O  
-ANISOU 1778  O   SER A 902     2689   2735   2782    -37     94   -130       O  
-ATOM   1779  CB  SER A 902     -40.102  12.872 -20.442  1.00 21.56           C  
-ANISOU 1779  CB  SER A 902     2714   2722   2756    -46    118    -56       C  
-ATOM   1780  OG  SER A 902     -39.774  14.140 -19.894  1.00 21.80           O  
-ANISOU 1780  OG  SER A 902     2735   2724   2824    -60    123    -43       O  
-ATOM   1781  N   LYS A 903     -40.135  12.491 -17.195  1.00 21.99           N  
-ANISOU 1781  N   LYS A 903     2737   2747   2872    -45     82   -115       N  
-ATOM   1782  CA  LYS A 903     -39.436  12.182 -15.952  1.00 20.55           C  
-ANISOU 1782  CA  LYS A 903     2537   2559   2711    -46     76   -142       C  
-ATOM   1783  C   LYS A 903     -39.925  10.870 -15.396  1.00 20.44           C  
-ANISOU 1783  C   LYS A 903     2528   2558   2681    -33     61   -162       C  
-ATOM   1784  O   LYS A 903     -39.129  10.042 -14.948  1.00 20.01           O  
-ANISOU 1784  O   LYS A 903     2463   2511   2627    -30     61   -181       O  
-ATOM   1785  CB  LYS A 903     -39.624  13.299 -14.927  1.00 21.35           C  
-ANISOU 1785  CB  LYS A 903     2632   2636   2846    -49     65   -145       C  
-ATOM   1786  CG  LYS A 903     -38.843  13.066 -13.651  1.00 22.27           C  
-ANISOU 1786  CG  LYS A 903     2730   2748   2981    -47     57   -174       C  
-ATOM   1787  CD  LYS A 903     -38.630  14.360 -12.866  1.00 22.27           C  
-ANISOU 1787  CD  LYS A 903     2720   2724   3020    -52     50   -181       C  
-ATOM   1788  CE  LYS A 903     -37.765  14.113 -11.639  1.00 22.45           C  
-ANISOU 1788  CE  LYS A 903     2725   2745   3059    -48     39   -213       C  
-ATOM   1789  NZ  LYS A 903     -37.717  15.327 -10.750  1.00 24.20           N  
-ANISOU 1789  NZ  LYS A 903     2937   2942   3316    -48     26   -226       N  
-ATOM   1790  N   SER A 904     -41.246  10.646 -15.445  1.00 21.86           N  
-ANISOU 1790  N   SER A 904     2720   2738   2845    -25     47   -156       N  
-ATOM   1791  CA  SER A 904     -41.822   9.375 -14.997  1.00 22.41           C  
-ANISOU 1791  CA  SER A 904     2794   2818   2902    -16     35   -171       C  
-ATOM   1792  C   SER A 904     -41.599   8.260 -16.004  1.00 21.51           C  
-ANISOU 1792  C   SER A 904     2686   2721   2765    -12     38   -174       C  
-ATOM   1793  O   SER A 904     -41.340   7.131 -15.613  1.00 21.73           O  
-ANISOU 1793  O   SER A 904     2712   2755   2790     -7     32   -191       O  
-ATOM   1794  CB  SER A 904     -43.308   9.512 -14.657  1.00 22.14           C  
-ANISOU 1794  CB  SER A 904     2767   2778   2866    -10     20   -166       C  
-ATOM   1795  OG  SER A 904     -43.469  10.149 -13.392  1.00 21.24           O  
-ANISOU 1795  OG  SER A 904     2646   2652   2771     -9     15   -174       O  
-ATOM   1796  N   ALA A 905     -41.758   8.558 -17.285  1.00 21.85           N  
-ANISOU 1796  N   ALA A 905     2739   2774   2791    -13     46   -159       N  
-ATOM   1797  CA  ALA A 905     -41.626   7.549 -18.340  1.00 21.67           C  
-ANISOU 1797  CA  ALA A 905     2723   2770   2742     -6     48   -165       C  
-ATOM   1798  C   ALA A 905     -40.242   6.922 -18.348  1.00 21.82           C  
-ANISOU 1798  C   ALA A 905     2729   2798   2762     -6     61   -181       C  
-ATOM   1799  O   ALA A 905     -40.097   5.774 -18.698  1.00 20.08           O  
-ANISOU 1799  O   ALA A 905     2511   2589   2528      2     56   -197       O  
-ATOM   1800  CB  ALA A 905     -41.919   8.158 -19.695  1.00 22.45           C  
-ANISOU 1800  CB  ALA A 905     2834   2878   2817     -4     56   -144       C  
-ATOM   1801  N   ASN A 906     -39.227   7.679 -17.926  1.00 23.20           N  
-ANISOU 1801  N   ASN A 906     2891   2967   2958    -16     76   -178       N  
-ATOM   1802  CA  ASN A 906     -37.875   7.119 -17.800  1.00 22.99           C  
-ANISOU 1802  CA  ASN A 906     2848   2948   2938    -16     86   -197       C  
-ATOM   1803  C   ASN A 906     -37.823   5.907 -16.866  1.00 23.17           C  
-ANISOU 1803  C   ASN A 906     2867   2968   2966     -6     67   -222       C  
-ATOM   1804  O   ASN A 906     -37.025   5.009 -17.088  1.00 23.91           O  
-ANISOU 1804  O   ASN A 906     2955   3073   3057      1     70   -240       O  
-ATOM   1805  CB  ASN A 906     -36.870   8.164 -17.337  1.00 23.11           C  
-ANISOU 1805  CB  ASN A 906     2845   2954   2983    -28    101   -194       C  
-ATOM   1806  CG  ASN A 906     -36.574   9.210 -18.392  1.00 23.44           C  
-ANISOU 1806  CG  ASN A 906     2886   2999   3021    -40    126   -167       C  
-ATOM   1807  OD1 ASN A 906     -36.823   9.015 -19.576  1.00 23.28           O  
-ANISOU 1807  OD1 ASN A 906     2879   2996   2970    -36    137   -155       O  
-ATOM   1808  ND2 ASN A 906     -36.050  10.342 -17.957  1.00 24.70           N  
-ANISOU 1808  ND2 ASN A 906     3032   3141   3212    -54    135   -159       N  
-ATOM   1809  N   TYR A 907     -38.697   5.857 -15.871  1.00 20.65           N  
-ANISOU 1809  N   TYR A 907     2555   2635   2655     -4     49   -222       N  
-ATOM   1810  CA  TYR A 907     -38.736   4.741 -14.952  1.00 20.06           C  
-ANISOU 1810  CA  TYR A 907     2481   2556   2585      5     32   -239       C  
-ATOM   1811  C   TYR A 907     -39.528   3.531 -15.457  1.00 20.80           C  
-ANISOU 1811  C   TYR A 907     2587   2653   2662     13     21   -243       C  
-ATOM   1812  O   TYR A 907     -39.629   2.513 -14.780  1.00 20.39           O  
-ANISOU 1812  O   TYR A 907     2537   2594   2614     19      7   -253       O  
-ATOM   1813  CB  TYR A 907     -39.252   5.211 -13.622  1.00 19.44           C  
-ANISOU 1813  CB  TYR A 907     2404   2464   2520      4     22   -236       C  
-ATOM   1814  CG  TYR A 907     -38.287   6.157 -12.976  1.00 19.09           C  
-ANISOU 1814  CG  TYR A 907     2345   2414   2496      0     27   -241       C  
-ATOM   1815  CD1 TYR A 907     -37.126   5.683 -12.378  1.00 19.74           C  
-ANISOU 1815  CD1 TYR A 907     2415   2497   2588      6     23   -261       C  
-ATOM   1816  CD2 TYR A 907     -38.504   7.530 -12.963  1.00 19.15           C  
-ANISOU 1816  CD2 TYR A 907     2348   2412   2514     -9     33   -229       C  
-ATOM   1817  CE1 TYR A 907     -36.222   6.546 -11.792  1.00 19.39           C  
-ANISOU 1817  CE1 TYR A 907     2353   2447   2566      3     24   -270       C  
-ATOM   1818  CE2 TYR A 907     -37.614   8.408 -12.347  1.00 18.74           C  
-ANISOU 1818  CE2 TYR A 907     2282   2353   2487    -13     35   -238       C  
-ATOM   1819  CZ  TYR A 907     -36.468   7.907 -11.773  1.00 19.49           C  
-ANISOU 1819  CZ  TYR A 907     2363   2450   2593     -8     31   -259       C  
-ATOM   1820  OH  TYR A 907     -35.578   8.742 -11.148  1.00 19.65           O  
-ANISOU 1820  OH  TYR A 907     2365   2461   2640    -12     29   -271       O  
-ATOM   1821  N   CYS A 908     -40.034   3.607 -16.680  1.00 21.75           N  
-ANISOU 1821  N   CYS A 908     2716   2785   2765     13     25   -236       N  
-ATOM   1822  CA  CYS A 908     -40.581   2.425 -17.325  1.00 22.82           C  
-ANISOU 1822  CA  CYS A 908     2859   2924   2887     21     12   -247       C  
-ATOM   1823  C   CYS A 908     -39.465   1.451 -17.745  1.00 24.74           C  
-ANISOU 1823  C   CYS A 908     3097   3177   3126     31     15   -269       C  
-ATOM   1824  O   CYS A 908     -39.712   0.260 -17.895  1.00 24.93           O  
-ANISOU 1824  O   CYS A 908     3126   3198   3149     39      0   -285       O  
-ATOM   1825  CB  CYS A 908     -41.434   2.802 -18.521  1.00 23.12           C  
-ANISOU 1825  CB  CYS A 908     2908   2973   2905     22     12   -236       C  
-ATOM   1826  SG  CYS A 908     -42.905   3.783 -18.145  1.00 23.44           S  
-ANISOU 1826  SG  CYS A 908     2954   3001   2951     15      4   -214       S  
-ATOM   1827  N   HIS A 909     -38.259   1.983 -17.962  1.00 26.54           N  
-ANISOU 1827  N   HIS A 909     3312   3415   3355     29     34   -271       N  
-ATOM   1828  CA  HIS A 909     -37.095   1.244 -18.421  1.00 27.46           C  
-ANISOU 1828  CA  HIS A 909     3419   3546   3469     39     41   -294       C  
-ATOM   1829  C   HIS A 909     -37.425   0.490 -19.699  1.00 28.91           C  
-ANISOU 1829  C   HIS A 909     3613   3746   3627     50     39   -305       C  
-ATOM   1830  O   HIS A 909     -37.118  -0.689 -19.843  1.00 26.93           O  
-ANISOU 1830  O   HIS A 909     3360   3495   3376     63     27   -330       O  
-ATOM   1831  CB  HIS A 909     -36.543   0.313 -17.340  1.00 28.61           C  
-ANISOU 1831  CB  HIS A 909     3558   3677   3636     47     25   -313       C  
-ATOM   1832  CG  HIS A 909     -35.977   1.037 -16.160  1.00 32.42           C  
-ANISOU 1832  CG  HIS A 909     4029   4149   4139     40     27   -308       C  
-ATOM   1833  ND1 HIS A 909     -34.774   1.711 -16.208  1.00 35.07           N  
-ANISOU 1833  ND1 HIS A 909     4345   4494   4487     36     44   -313       N  
-ATOM   1834  CD2 HIS A 909     -36.455   1.218 -14.905  1.00 32.37           C  
-ANISOU 1834  CD2 HIS A 909     4028   4126   4146     37     13   -300       C  
-ATOM   1835  CE1 HIS A 909     -34.550   2.299 -15.047  1.00 33.27           C  
-ANISOU 1835  CE1 HIS A 909     4110   4253   4278     32     38   -311       C  
-ATOM   1836  NE2 HIS A 909     -35.539   1.991 -14.230  1.00 32.77           N  
-ANISOU 1836  NE2 HIS A 909     4063   4176   4214     34     19   -304       N  
-ATOM   1837  N   THR A 910     -38.054   1.187 -20.641  1.00 29.68           N  
-ANISOU 1837  N   THR A 910     3721   3856   3702     47     47   -288       N  
-ATOM   1838  CA  THR A 910     -38.306   0.600 -21.915  1.00 31.65           C  
-ANISOU 1838  CA  THR A 910     3980   4125   3921     60     45   -300       C  
-ATOM   1839  C   THR A 910     -37.013   0.671 -22.749  1.00 32.38           C  
-ANISOU 1839  C   THR A 910     4062   4245   3997     67     73   -309       C  
-ATOM   1840  O   THR A 910     -36.057   1.294 -22.357  1.00 33.81           O  
-ANISOU 1840  O   THR A 910     4227   4427   4193     57     94   -302       O  
-ATOM   1841  CB  THR A 910     -39.452   1.291 -22.643  1.00 31.90           C  
-ANISOU 1841  CB  THR A 910     4029   4162   3931     58     41   -279       C  
-ATOM   1842  OG1 THR A 910     -39.219   2.703 -22.658  1.00 29.97           O  
-ANISOU 1842  OG1 THR A 910     3783   3920   3686     46     64   -248       O  
-ATOM   1843  CG2 THR A 910     -40.748   0.968 -21.984  1.00 31.38           C  
-ANISOU 1843  CG2 THR A 910     3969   4073   3881     55     13   -277       C  
-ATOM   1844  N   SER A 911     -37.002  -0.008 -23.885  1.00 36.15           N  
-ANISOU 1844  N   SER A 911     4546   4744   4444     83     72   -328       N  
-ATOM   1845  CA  SER A 911     -35.823  -0.055 -24.771  1.00 36.94           C  
-ANISOU 1845  CA  SER A 911     4635   4876   4523     92    101   -340       C  
-ATOM   1846  C   SER A 911     -36.302  -0.346 -26.174  1.00 39.24           C  
-ANISOU 1846  C   SER A 911     4945   5196   4770    110    100   -347       C  
-ATOM   1847  O   SER A 911     -37.491  -0.565 -26.406  1.00 36.75           O  
-ANISOU 1847  O   SER A 911     4647   4873   4444    115     74   -347       O  
-ATOM   1848  CB  SER A 911     -34.852  -1.144 -24.311  1.00 38.15           C  
-ANISOU 1848  CB  SER A 911     4770   5026   4698    104     95   -376       C  
-ATOM   1849  OG  SER A 911     -35.519  -2.407 -24.238  1.00 42.20           O  
-ANISOU 1849  OG  SER A 911     5294   5525   5216    118     60   -403       O  
-ATOM   1850  N   GLN A 912     -35.390  -0.317 -27.132  1.00 44.90           N  
-ANISOU 1850  N   GLN A 912     5656   5948   5458    120    129   -355       N  
-ATOM   1851  CA  GLN A 912     -35.751  -0.553 -28.531  1.00 44.45           C  
-ANISOU 1851  CA  GLN A 912     5617   5924   5349    140    131   -363       C  
-ATOM   1852  C   GLN A 912     -36.305  -1.951 -28.713  1.00 40.32           C  
-ANISOU 1852  C   GLN A 912     5100   5395   4824    162     92   -407       C  
-ATOM   1853  O   GLN A 912     -37.217  -2.151 -29.474  1.00 41.92           O  
-ANISOU 1853  O   GLN A 912     5323   5607   4998    175     73   -412       O  
-ATOM   1854  CB  GLN A 912     -34.560  -0.272 -29.442  1.00 51.68           C  
-ANISOU 1854  CB  GLN A 912     6522   6880   6233    147    175   -363       C  
-ATOM   1855  CG  GLN A 912     -34.527   1.208 -29.793  1.00 57.92           C  
-ANISOU 1855  CG  GLN A 912     7320   7681   7008    129    209   -312       C  
-ATOM   1856  CD  GLN A 912     -33.162   1.813 -30.039  1.00 64.37           C  
-ANISOU 1856  CD  GLN A 912     8113   8520   7825    119    260   -299       C  
-ATOM   1857  OE1 GLN A 912     -32.565   2.399 -29.120  1.00 76.70           O  
-ANISOU 1857  OE1 GLN A 912     9653  10060   9431     96    273   -285       O  
-ATOM   1858  NE2 GLN A 912     -32.672   1.729 -31.278  1.00 66.04           N  
-ANISOU 1858  NE2 GLN A 912     8329   8777   7987    135    291   -302       N  
-ATOM   1859  N   GLY A 913     -35.778  -2.893 -27.958  1.00 39.90           N  
-ANISOU 1859  N   GLY A 913     5032   5324   4807    165     79   -436       N  
-ATOM   1860  CA  GLY A 913     -36.246  -4.266 -27.968  1.00 43.54           C  
-ANISOU 1860  CA  GLY A 913     5496   5769   5277    183     40   -477       C  
-ATOM   1861  C   GLY A 913     -37.554  -4.506 -27.263  1.00 48.75           C  
-ANISOU 1861  C   GLY A 913     6167   6391   5964    172      3   -468       C  
-ATOM   1862  O   GLY A 913     -38.244  -5.470 -27.596  1.00 47.11           O  
-ANISOU 1862  O   GLY A 913     5968   6174   5757    186    -29   -497       O  
-ATOM   1863  N   ASP A 914     -37.890  -3.649 -26.281  1.00 52.35           N  
-ANISOU 1863  N   ASP A 914     6622   6826   6445    148      8   -432       N  
-ATOM   1864  CA  ASP A 914     -39.233  -3.616 -25.675  1.00 49.44           C  
-ANISOU 1864  CA  ASP A 914     6262   6426   6095    136    -19   -417       C  
-ATOM   1865  C   ASP A 914     -39.729  -2.165 -25.468  1.00 42.37           C  
-ANISOU 1865  C   ASP A 914     5373   5531   5194    118     -4   -374       C  
-ATOM   1866  O   ASP A 914     -39.607  -1.612 -24.370  1.00 36.97           O  
-ANISOU 1866  O   ASP A 914     4680   4827   4538    101      4   -353       O  
-ATOM   1867  CB  ASP A 914     -39.264  -4.390 -24.355  1.00 55.80           C  
-ANISOU 1867  CB  ASP A 914     7059   7194   6947    128    -38   -424       C  
-ATOM   1868  CG  ASP A 914     -40.708  -4.725 -23.918  1.00 67.92           C  
-ANISOU 1868  CG  ASP A 914     8602   8700   8503    119    -69   -418       C  
-ATOM   1869  OD1 ASP A 914     -40.872  -5.523 -22.975  1.00 70.61           O  
-ANISOU 1869  OD1 ASP A 914     8940   9011   8879    114    -86   -424       O  
-ATOM   1870  OD2 ASP A 914     -41.690  -4.227 -24.552  1.00 65.85           O  
-ANISOU 1870  OD2 ASP A 914     8350   8447   8222    118    -76   -408       O  
-ATOM   1871  N   PRO A 915     -40.282  -1.554 -26.528  1.00 34.40           N  
-ANISOU 1871  N   PRO A 915     4378   4544   4147    124      0   -362       N  
-ATOM   1872  CA  PRO A 915     -40.585  -0.140 -26.543  1.00 33.16           C  
-ANISOU 1872  CA  PRO A 915     4227   4389   3981    111     17   -321       C  
-ATOM   1873  C   PRO A 915     -42.007   0.264 -26.091  1.00 32.04           C  
-ANISOU 1873  C   PRO A 915     4093   4225   3855    102     -8   -304       C  
-ATOM   1874  O   PRO A 915     -42.395   1.421 -26.248  1.00 33.18           O  
-ANISOU 1874  O   PRO A 915     4245   4372   3990     95      1   -272       O  
-ATOM   1875  CB  PRO A 915     -40.400   0.199 -28.023  1.00 32.12           C  
-ANISOU 1875  CB  PRO A 915     4111   4297   3797    127     32   -317       C  
-ATOM   1876  CG  PRO A 915     -40.941  -1.027 -28.718  1.00 31.61           C  
-ANISOU 1876  CG  PRO A 915     4054   4241   3717    150      0   -357       C  
-ATOM   1877  CD  PRO A 915     -40.642  -2.184 -27.818  1.00 32.61           C  
-ANISOU 1877  CD  PRO A 915     4164   4342   3885    148    -16   -387       C  
-ATOM   1878  N   ILE A 916     -42.769  -0.667 -25.562  1.00 32.74           N  
-ANISOU 1878  N   ILE A 916     4179   4292   3970    102    -38   -323       N  
-ATOM   1879  CA  ILE A 916     -44.091  -0.375 -25.066  1.00 34.64           C  
-ANISOU 1879  CA  ILE A 916     4420   4511   4229     93    -59   -310       C  
-ATOM   1880  C   ILE A 916     -44.019  -0.371 -23.552  1.00 32.60           C  
-ANISOU 1880  C   ILE A 916     4149   4224   4012     75    -55   -301       C  
-ATOM   1881  O   ILE A 916     -43.570  -1.328 -22.951  1.00 34.13           O  
-ANISOU 1881  O   ILE A 916     4335   4406   4227     75    -60   -319       O  
-ATOM   1882  CB  ILE A 916     -45.102  -1.410 -25.552  1.00 40.49           C  
-ANISOU 1882  CB  ILE A 916     5164   5247   4973    104    -94   -338       C  
-ATOM   1883  CG1 ILE A 916     -45.229  -1.330 -27.080  1.00 44.76           C  
-ANISOU 1883  CG1 ILE A 916     5720   5820   5466    125   -101   -349       C  
-ATOM   1884  CG2 ILE A 916     -46.464  -1.136 -24.981  1.00 40.10           C  
-ANISOU 1884  CG2 ILE A 916     5111   5177   4949     93   -114   -326       C  
-ATOM   1885  CD1 ILE A 916     -46.228  -2.301 -27.685  1.00 50.13           C  
-ANISOU 1885  CD1 ILE A 916     6402   6497   6147    139   -140   -382       C  
-ATOM   1886  N   GLY A 917     -44.449   0.730 -22.954  1.00 29.68           N  
-ANISOU 1886  N   GLY A 917     3778   3846   3653     63    -47   -273       N  
-ATOM   1887  CA  GLY A 917     -44.467   0.882 -21.520  1.00 28.89           C  
-ANISOU 1887  CA  GLY A 917     3668   3723   3585     48    -44   -263       C  
-ATOM   1888  C   GLY A 917     -45.838   1.227 -20.967  1.00 28.00           C  
-ANISOU 1888  C   GLY A 917     3554   3595   3491     41    -58   -251       C  
-ATOM   1889  O   GLY A 917     -46.756   1.612 -21.705  1.00 29.17           O  
-ANISOU 1889  O   GLY A 917     3708   3750   3627     46    -70   -246       O  
-ATOM   1890  N   LEU A 918     -45.932   1.126 -19.647  1.00 25.51           N  
-ANISOU 1890  N   LEU A 918     3229   3261   3203     31    -56   -246       N  
-ATOM   1891  CA  LEU A 918     -47.088   1.470 -18.918  1.00 25.75           C  
-ANISOU 1891  CA  LEU A 918     3254   3279   3252     23    -64   -235       C  
-ATOM   1892  C   LEU A 918     -46.768   2.577 -17.914  1.00 26.37           C  
-ANISOU 1892  C   LEU A 918     3329   3352   3339     16    -47   -217       C  
-ATOM   1893  O   LEU A 918     -45.739   2.531 -17.182  1.00 24.23           O  
-ANISOU 1893  O   LEU A 918     3055   3078   3073     13    -35   -218       O  
-ATOM   1894  CB  LEU A 918     -47.622   0.246 -18.184  1.00 26.75           C  
-ANISOU 1894  CB  LEU A 918     3374   3387   3401     18    -76   -246       C  
-ATOM   1895  CG  LEU A 918     -48.154  -0.903 -19.032  1.00 26.29           C  
-ANISOU 1895  CG  LEU A 918     3316   3327   3345     23    -98   -267       C  
-ATOM   1896  CD1 LEU A 918     -48.556  -2.092 -18.169  1.00 24.96           C  
-ANISOU 1896  CD1 LEU A 918     3140   3136   3207     14   -107   -272       C  
-ATOM   1897  CD2 LEU A 918     -49.316  -0.447 -19.872  1.00 27.56           C  
-ANISOU 1897  CD2 LEU A 918     3476   3495   3500     27   -113   -267       C  
-ATOM   1898  N   ILE A 919     -47.676   3.564 -17.859  1.00 24.09           N  
-ANISOU 1898  N   ILE A 919     3039   3062   3054     14    -49   -203       N  
-ATOM   1899  CA  ILE A 919     -47.536   4.672 -16.953  1.00 22.74           C  
-ANISOU 1899  CA  ILE A 919     2864   2884   2893     10    -37   -190       C  
-ATOM   1900  C   ILE A 919     -48.878   5.016 -16.303  1.00 22.16           C  
-ANISOU 1900  C   ILE A 919     2783   2803   2836      8    -45   -185       C  
-ATOM   1901  O   ILE A 919     -49.947   4.921 -16.931  1.00 21.47           O  
-ANISOU 1901  O   ILE A 919     2693   2717   2748     11    -59   -187       O  
-ATOM   1902  CB  ILE A 919     -46.934   5.870 -17.708  1.00 24.10           C  
-ANISOU 1902  CB  ILE A 919     3042   3061   3052     11    -27   -176       C  
-ATOM   1903  CG1 ILE A 919     -46.484   6.941 -16.756  1.00 24.64           C  
-ANISOU 1903  CG1 ILE A 919     3106   3120   3136      6    -15   -168       C  
-ATOM   1904  CG2 ILE A 919     -47.936   6.473 -18.650  1.00 25.21           C  
-ANISOU 1904  CG2 ILE A 919     3190   3207   3183     18    -38   -166       C  
-ATOM   1905  CD1 ILE A 919     -45.521   7.903 -17.406  1.00 26.38           C  
-ANISOU 1905  CD1 ILE A 919     3331   3343   3350      4     -1   -155       C  
-ATOM   1906  N   LEU A 920     -48.829   5.417 -15.045  1.00 20.25           N  
-ANISOU 1906  N   LEU A 920     2533   2553   2606      4    -36   -182       N  
-ATOM   1907  CA  LEU A 920     -50.028   5.748 -14.290  1.00 19.74           C  
-ANISOU 1907  CA  LEU A 920     2458   2484   2556      4    -39   -180       C  
-ATOM   1908  C   LEU A 920     -50.279   7.246 -14.182  1.00 19.22           C  
-ANISOU 1908  C   LEU A 920     2392   2416   2495      8    -37   -172       C  
-ATOM   1909  O   LEU A 920     -49.346   8.029 -14.113  1.00 19.34           O  
-ANISOU 1909  O   LEU A 920     2411   2428   2508      8    -29   -167       O  
-ATOM   1910  CB  LEU A 920     -49.914   5.213 -12.877  1.00 19.52           C  
-ANISOU 1910  CB  LEU A 920     2425   2453   2537      0    -30   -182       C  
-ATOM   1911  CG  LEU A 920     -49.853   3.720 -12.749  1.00 20.76           C  
-ANISOU 1911  CG  LEU A 920     2584   2607   2697     -5    -33   -187       C  
-ATOM   1912  CD1 LEU A 920     -49.317   3.320 -11.379  1.00 22.11           C  
-ANISOU 1912  CD1 LEU A 920     2756   2775   2869     -6    -23   -185       C  
-ATOM   1913  CD2 LEU A 920     -51.220   3.118 -12.945  1.00 21.17           C  
-ANISOU 1913  CD2 LEU A 920     2626   2657   2762    -10    -42   -187       C  
-ATOM   1914  N   LEU A 921     -51.556   7.629 -14.162  1.00 19.52           N  
-ANISOU 1914  N   LEU A 921     2420   2453   2543     12    -46   -171       N  
-ATOM   1915  CA  LEU A 921     -51.942   8.931 -13.638  1.00 17.79           C  
-ANISOU 1915  CA  LEU A 921     2197   2229   2336     18    -44   -167       C  
-ATOM   1916  C   LEU A 921     -52.663   8.700 -12.340  1.00 17.46           C  
-ANISOU 1916  C   LEU A 921     2140   2189   2305     17    -37   -174       C  
-ATOM   1917  O   LEU A 921     -53.616   7.959 -12.273  1.00 18.92           O  
-ANISOU 1917  O   LEU A 921     2314   2377   2497     15    -40   -177       O  
-ATOM   1918  CB  LEU A 921     -52.822   9.675 -14.583  1.00 17.83           C  
-ANISOU 1918  CB  LEU A 921     2201   2231   2342     26    -59   -162       C  
-ATOM   1919  CG  LEU A 921     -52.111  10.308 -15.762  1.00 18.51           C  
-ANISOU 1919  CG  LEU A 921     2304   2315   2414     29    -62   -148       C  
-ATOM   1920  CD1 LEU A 921     -53.135  10.692 -16.807  1.00 19.23           C  
-ANISOU 1920  CD1 LEU A 921     2398   2407   2502     39    -82   -143       C  
-ATOM   1921  CD2 LEU A 921     -51.306  11.524 -15.356  1.00 18.98           C  
-ANISOU 1921  CD2 LEU A 921     2368   2362   2482     28    -53   -140       C  
-ATOM   1922  N   GLY A 922     -52.154   9.308 -11.277  1.00 17.80           N  
-ANISOU 1922  N   GLY A 922     2183   2230   2351     20    -27   -178       N  
-ATOM   1923  CA  GLY A 922     -52.735   9.195  -9.949  1.00 17.60           C  
-ANISOU 1923  CA  GLY A 922     2146   2211   2331     23    -18   -184       C  
-ATOM   1924  C   GLY A 922     -53.230  10.531  -9.458  1.00 17.40           C  
-ANISOU 1924  C   GLY A 922     2112   2182   2316     35    -19   -191       C  
-ATOM   1925  O   GLY A 922     -52.587  11.571  -9.685  1.00 18.09           O  
-ANISOU 1925  O   GLY A 922     2207   2260   2408     39    -24   -192       O  
-ATOM   1926  N   GLU A 923     -54.349  10.514  -8.772  1.00 17.41           N  
-ANISOU 1926  N   GLU A 923     2098   2192   2324     39    -14   -197       N  
-ATOM   1927  CA  GLU A 923     -54.775  11.679  -8.015  1.00 19.52           C  
-ANISOU 1927  CA  GLU A 923     2356   2460   2600     53    -12   -209       C  
-ATOM   1928  C   GLU A 923     -54.002  11.592  -6.691  1.00 19.23           C  
-ANISOU 1928  C   GLU A 923     2325   2431   2551     57      0   -217       C  
-ATOM   1929  O   GLU A 923     -54.127  10.605  -5.960  1.00 19.05           O  
-ANISOU 1929  O   GLU A 923     2300   2421   2516     53     14   -214       O  
-ATOM   1930  CB  GLU A 923     -56.277  11.666  -7.742  1.00 21.12           C  
-ANISOU 1930  CB  GLU A 923     2537   2673   2815     59     -9   -214       C  
-ATOM   1931  CG  GLU A 923     -56.760  12.896  -6.989  1.00 23.47           C  
-ANISOU 1931  CG  GLU A 923     2823   2972   3123     77     -9   -231       C  
-ATOM   1932  CD  GLU A 923     -58.221  12.805  -6.536  1.00 26.40           C  
-ANISOU 1932  CD  GLU A 923     3168   3359   3505     83      0   -239       C  
-ATOM   1933  OE1 GLU A 923     -59.027  12.209  -7.268  1.00 27.30           O  
-ANISOU 1933  OE1 GLU A 923     3270   3474   3630     76     -5   -233       O  
-ATOM   1934  OE2 GLU A 923     -58.578  13.411  -5.506  1.00 28.54           O  
-ANISOU 1934  OE2 GLU A 923     3428   3640   3776     98     10   -255       O  
-ATOM   1935  N   VAL A 924     -53.181  12.600  -6.420  1.00 18.80           N  
-ANISOU 1935  N   VAL A 924     2277   2367   2500     65     -6   -227       N  
-ATOM   1936  CA  VAL A 924     -52.372  12.615  -5.243  1.00 19.98           C  
-ANISOU 1936  CA  VAL A 924     2431   2523   2637     71      0   -238       C  
-ATOM   1937  C   VAL A 924     -52.808  13.770  -4.338  1.00 19.95           C  
-ANISOU 1937  C   VAL A 924     2419   2522   2641     90     -1   -260       C  
-ATOM   1938  O   VAL A 924     -52.861  14.927  -4.755  1.00 19.73           O  
-ANISOU 1938  O   VAL A 924     2387   2476   2633     96    -14   -267       O  
-ATOM   1939  CB  VAL A 924     -50.891  12.793  -5.609  1.00 20.51           C  
-ANISOU 1939  CB  VAL A 924     2511   2576   2706     65     -7   -238       C  
-ATOM   1940  CG1 VAL A 924     -50.014  12.690  -4.349  1.00 21.31           C  
-ANISOU 1940  CG1 VAL A 924     2617   2686   2794     74     -5   -253       C  
-ATOM   1941  CG2 VAL A 924     -50.459  11.732  -6.617  1.00 19.48           C  
-ANISOU 1941  CG2 VAL A 924     2389   2444   2568     50     -6   -220       C  
-ATOM   1942  N   ALA A 925     -53.109  13.454  -3.093  1.00 21.06           N  
-ANISOU 1942  N   ALA A 925     2555   2683   2763    100     12   -270       N  
-ATOM   1943  CA  ALA A 925     -53.568  14.473  -2.160  1.00 22.12           C  
-ANISOU 1943  CA  ALA A 925     2680   2824   2900    122     11   -295       C  
-ATOM   1944  C   ALA A 925     -52.348  15.093  -1.470  1.00 21.34           C  
-ANISOU 1944  C   ALA A 925     2591   2719   2799    132      0   -315       C  
-ATOM   1945  O   ALA A 925     -51.869  14.572  -0.472  1.00 21.27           O  
-ANISOU 1945  O   ALA A 925     2590   2727   2764    139      7   -321       O  
-ATOM   1946  CB  ALA A 925     -54.507  13.862  -1.145  1.00 21.94           C  
-ANISOU 1946  CB  ALA A 925     2648   2831   2857    130     33   -296       C  
-ATOM   1947  N   LEU A 926     -51.866  16.195  -2.013  1.00 20.79           N  
-ANISOU 1947  N   LEU A 926     2521   2622   2755    132    -18   -324       N  
-ATOM   1948  CA  LEU A 926     -50.585  16.762  -1.585  1.00 21.93           C  
-ANISOU 1948  CA  LEU A 926     2672   2755   2907    136    -32   -342       C  
-ATOM   1949  C   LEU A 926     -50.731  17.685  -0.390  1.00 22.70           C  
-ANISOU 1949  C   LEU A 926     2763   2858   3004    162    -39   -378       C  
-ATOM   1950  O   LEU A 926     -49.796  17.811   0.393  1.00 24.17           O  
-ANISOU 1950  O   LEU A 926     2954   3046   3183    170    -48   -398       O  
-ATOM   1951  CB  LEU A 926     -49.950  17.550  -2.710  1.00 21.13           C  
-ANISOU 1951  CB  LEU A 926     2571   2619   2838    123    -46   -334       C  
-ATOM   1952  CG  LEU A 926     -49.655  16.759  -3.956  1.00 20.82           C  
-ANISOU 1952  CG  LEU A 926     2540   2575   2796    101    -40   -302       C  
-ATOM   1953  CD1 LEU A 926     -49.360  17.694  -5.095  1.00 21.98           C  
-ANISOU 1953  CD1 LEU A 926     2688   2691   2973     91    -50   -290       C  
-ATOM   1954  CD2 LEU A 926     -48.484  15.829  -3.727  1.00 20.81           C  
-ANISOU 1954  CD2 LEU A 926     2547   2582   2779     92    -36   -300       C  
-ATOM   1955  N   GLY A 927     -51.887  18.322  -0.254  1.00 21.74           N  
-ANISOU 1955  N   GLY A 927     2630   2739   2891    176    -38   -388       N  
-ATOM   1956  CA  GLY A 927     -52.113  19.242   0.853  1.00 22.53           C  
-ANISOU 1956  CA  GLY A 927     2723   2846   2992    203    -45   -427       C  
-ATOM   1957  C   GLY A 927     -51.047  20.328   0.872  1.00 22.15           C  
-ANISOU 1957  C   GLY A 927     2676   2766   2974    206    -71   -450       C  
-ATOM   1958  O   GLY A 927     -50.668  20.829  -0.166  1.00 22.63           O  
-ANISOU 1958  O   GLY A 927     2738   2793   3068    190    -82   -435       O  
-ATOM   1959  N   ASN A 928     -50.584  20.663   2.054  1.00 22.34           N  
-ANISOU 1959  N   ASN A 928     2701   2801   2986    227    -80   -485       N  
-ATOM   1960  CA  ASN A 928     -49.459  21.575   2.248  1.00 24.86           C  
-ANISOU 1960  CA  ASN A 928     3020   3092   3335    230   -106   -512       C  
-ATOM   1961  C   ASN A 928     -48.123  20.896   2.001  1.00 23.29           C  
-ANISOU 1961  C   ASN A 928     2830   2888   3132    211   -109   -498       C  
-ATOM   1962  O   ASN A 928     -47.714  19.962   2.743  1.00 21.96           O  
-ANISOU 1962  O   ASN A 928     2670   2749   2926    217   -102   -500       O  
-ATOM   1963  CB  ASN A 928     -49.467  22.088   3.677  1.00 26.30           C  
-ANISOU 1963  CB  ASN A 928     3199   3293   3501    264   -117   -561       C  
-ATOM   1964  CG  ASN A 928     -50.693  22.857   3.997  1.00 27.32           C  
-ANISOU 1964  CG  ASN A 928     3316   3427   3636    287   -116   -582       C  
-ATOM   1965  OD1 ASN A 928     -51.157  23.661   3.174  1.00 31.66           O  
-ANISOU 1965  OD1 ASN A 928     3858   3945   4226    281   -125   -577       O  
-ATOM   1966  ND2 ASN A 928     -51.216  22.679   5.215  1.00 28.34           N  
-ANISOU 1966  ND2 ASN A 928     3446   3597   3726    316   -107   -609       N  
-ATOM   1967  N   MET A 929     -47.459  21.378   0.966  1.00 23.02           N  
-ANISOU 1967  N   MET A 929     2792   2816   3137    189   -118   -484       N  
-ATOM   1968  CA  MET A 929     -46.228  20.762   0.488  1.00 24.78           C  
-ANISOU 1968  CA  MET A 929     3020   3033   3364    167   -118   -467       C  
-ATOM   1969  C   MET A 929     -45.026  21.330   1.217  1.00 25.33           C  
-ANISOU 1969  C   MET A 929     3083   3090   3452    174   -141   -504       C  
-ATOM   1970  O   MET A 929     -44.908  22.535   1.386  1.00 23.77           O  
-ANISOU 1970  O   MET A 929     2876   2864   3292    181   -160   -530       O  
-ATOM   1971  CB  MET A 929     -46.089  21.017  -0.992  1.00 25.61           C  
-ANISOU 1971  CB  MET A 929     3123   3107   3499    140   -113   -433       C  
-ATOM   1972  CG  MET A 929     -47.190  20.366  -1.809  1.00 25.54           C  
-ANISOU 1972  CG  MET A 929     3121   3112   3472    132    -94   -398       C  
-ATOM   1973  SD  MET A 929     -47.129  20.756  -3.547  1.00 27.81           S  
-ANISOU 1973  SD  MET A 929     3411   3366   3788    107    -91   -360       S  
-ATOM   1974  CE  MET A 929     -47.180  22.533  -3.548  1.00 28.93           C  
-ANISOU 1974  CE  MET A 929     3545   3466   3982    114   -112   -378       C  
-ATOM   1975  N   TYR A 930     -44.156  20.436   1.648  1.00 24.40           N  
-ANISOU 1975  N   TYR A 930     2969   2990   3310    173   -141   -506       N  
-ATOM   1976  CA  TYR A 930     -42.848  20.793   2.160  1.00 25.05           C  
-ANISOU 1976  CA  TYR A 930     3044   3061   3414    176   -163   -537       C  
-ATOM   1977  C   TYR A 930     -41.967  20.945   0.930  1.00 24.55           C  
-ANISOU 1977  C   TYR A 930     2971   2965   3390    143   -160   -513       C  
-ATOM   1978  O   TYR A 930     -41.608  19.966   0.306  1.00 24.54           O  
-ANISOU 1978  O   TYR A 930     2975   2974   3374    127   -144   -484       O  
-ATOM   1979  CB  TYR A 930     -42.369  19.677   3.107  1.00 23.57           C  
-ANISOU 1979  CB  TYR A 930     2867   2910   3179    192   -165   -546       C  
-ATOM   1980  CG  TYR A 930     -41.111  19.922   3.889  1.00 24.55           C  
-ANISOU 1980  CG  TYR A 930     2983   3030   3315    203   -193   -586       C  
-ATOM   1981  CD1 TYR A 930     -40.686  21.202   4.235  1.00 25.35           C  
-ANISOU 1981  CD1 TYR A 930     3069   3104   3460    210   -220   -627       C  
-ATOM   1982  CD2 TYR A 930     -40.377  18.844   4.379  1.00 24.54           C  
-ANISOU 1982  CD2 TYR A 930     2990   3053   3281    210   -197   -586       C  
-ATOM   1983  CE1 TYR A 930     -39.527  21.392   4.971  1.00 25.08           C  
-ANISOU 1983  CE1 TYR A 930     3024   3067   3438    221   -249   -666       C  
-ATOM   1984  CE2 TYR A 930     -39.221  19.024   5.117  1.00 25.94           C  
-ANISOU 1984  CE2 TYR A 930     3159   3229   3468    223   -226   -624       C  
-ATOM   1985  CZ  TYR A 930     -38.810  20.297   5.419  1.00 26.98           C  
-ANISOU 1985  CZ  TYR A 930     3273   3334   3644    229   -253   -666       C  
-ATOM   1986  OH  TYR A 930     -37.681  20.448   6.194  1.00 28.08           O  
-ANISOU 1986  OH  TYR A 930     3401   3473   3793    244   -285   -708       O  
-ATOM   1987  N   GLU A 931     -41.630  22.182   0.589  1.00 25.56           N  
-ANISOU 1987  N   GLU A 931     3086   3054   3572    134   -174   -525       N  
-ATOM   1988  CA  GLU A 931     -40.915  22.460  -0.635  1.00 27.41           C  
-ANISOU 1988  CA  GLU A 931     3312   3257   3846    103   -165   -498       C  
-ATOM   1989  C   GLU A 931     -39.418  22.411  -0.405  1.00 26.62           C  
-ANISOU 1989  C   GLU A 931     3196   3149   3771     93   -178   -518       C  
-ATOM   1990  O   GLU A 931     -38.900  23.110   0.427  1.00 26.02           O  
-ANISOU 1990  O   GLU A 931     3107   3059   3720    105   -203   -560       O  
-ATOM   1991  CB  GLU A 931     -41.297  23.815  -1.174  1.00 29.59           C  
-ANISOU 1991  CB  GLU A 931     3582   3492   4171     95   -172   -494       C  
-ATOM   1992  CG  GLU A 931     -42.801  23.946  -1.306  1.00 34.97           C  
-ANISOU 1992  CG  GLU A 931     4275   4181   4831    109   -165   -481       C  
-ATOM   1993  CD  GLU A 931     -43.237  25.104  -2.197  1.00 38.72           C  
-ANISOU 1993  CD  GLU A 931     4748   4613   5350     98   -168   -463       C  
-ATOM   1994  OE1 GLU A 931     -42.403  25.966  -2.531  1.00 44.32           O  
-ANISOU 1994  OE1 GLU A 931     5446   5282   6110     82   -178   -465       O  
-ATOM   1995  OE2 GLU A 931     -44.404  25.108  -2.606  1.00 42.96           O  
-ANISOU 1995  OE2 GLU A 931     5294   5155   5872    105   -160   -444       O  
-ATOM   1996  N   LEU A 932     -38.722  21.572  -1.143  1.00 25.22           N  
-ANISOU 1996  N   LEU A 932     3017   2979   3586     73   -161   -492       N  
-ATOM   1997  CA  LEU A 932     -37.289  21.374  -0.903  1.00 24.85           C  
-ANISOU 1997  CA  LEU A 932     2952   2929   3560     66   -171   -512       C  
-ATOM   1998  C   LEU A 932     -36.559  21.535  -2.206  1.00 25.87           C  
-ANISOU 1998  C   LEU A 932     3068   3035   3725     32   -152   -481       C  
-ATOM   1999  O   LEU A 932     -37.043  21.096  -3.278  1.00 27.03           O  
-ANISOU 1999  O   LEU A 932     3228   3189   3855     18   -126   -438       O  
-ATOM   2000  CB  LEU A 932     -37.048  19.984  -0.312  1.00 23.28           C  
-ANISOU 2000  CB  LEU A 932     2764   2771   3311     82   -171   -517       C  
-ATOM   2001  CG  LEU A 932     -37.652  19.762   1.068  1.00 23.17           C  
-ANISOU 2001  CG  LEU A 932     2764   2784   3257    117   -188   -546       C  
-ATOM   2002  CD1 LEU A 932     -37.499  18.328   1.518  1.00 23.48           C  
-ANISOU 2002  CD1 LEU A 932     2817   2859   3244    130   -184   -539       C  
-ATOM   2003  CD2 LEU A 932     -37.021  20.703   2.088  1.00 24.21           C  
-ANISOU 2003  CD2 LEU A 932     2880   2901   3417    134   -223   -599       C  
-ATOM   2004  N   LYS A 933     -35.358  22.068  -2.115  1.00 27.25           N  
-ANISOU 2004  N   LYS A 933     3218   3188   3948     20   -163   -503       N  
-ATOM   2005  CA  LYS A 933     -34.487  22.210  -3.279  1.00 28.83           C  
-ANISOU 2005  CA  LYS A 933     3401   3369   4184    -14   -141   -475       C  
-ATOM   2006  C   LYS A 933     -33.405  21.173  -3.325  1.00 27.54           C  
-ANISOU 2006  C   LYS A 933     3226   3229   4011    -18   -136   -481       C  
-ATOM   2007  O   LYS A 933     -32.767  21.022  -4.354  1.00 30.98           O  
-ANISOU 2007  O   LYS A 933     3649   3659   4462    -43   -111   -455       O  
-ATOM   2008  CB  LYS A 933     -33.851  23.576  -3.286  1.00 31.83           C  
-ANISOU 2008  CB  LYS A 933     3756   3703   4636    -30   -154   -492       C  
-ATOM   2009  CG  LYS A 933     -34.833  24.704  -3.447  1.00 35.68           C  
-ANISOU 2009  CG  LYS A 933     4254   4158   5144    -30   -159   -482       C  
-ATOM   2010  CD  LYS A 933     -34.151  26.046  -3.258  1.00 40.76           C  
-ANISOU 2010  CD  LYS A 933     4871   4752   5863    -44   -177   -506       C  
-ATOM   2011  CE  LYS A 933     -35.158  27.007  -2.686  1.00 47.56           C  
-ANISOU 2011  CE  LYS A 933     5744   5591   6737    -24   -201   -525       C  
-ATOM   2012  NZ  LYS A 933     -34.746  28.424  -2.861  1.00 51.66           N  
-ANISOU 2012  NZ  LYS A 933     6242   6051   7335    -43   -214   -533       N  
-ATOM   2013  N   HIS A 934     -33.154  20.465  -2.224  1.00 26.00           N  
-ANISOU 2013  N   HIS A 934     3031   3059   3787      8   -158   -515       N  
-ATOM   2014  CA  HIS A 934     -32.050  19.501  -2.166  1.00 25.98           C  
-ANISOU 2014  CA  HIS A 934     3015   3076   3779      8   -159   -526       C  
-ATOM   2015  C   HIS A 934     -32.432  18.294  -1.350  1.00 23.98           C  
-ANISOU 2015  C   HIS A 934     2785   2861   3465     38   -170   -534       C  
-ATOM   2016  O   HIS A 934     -33.394  18.319  -0.647  1.00 24.81           O  
-ANISOU 2016  O   HIS A 934     2912   2977   3539     59   -179   -539       O  
-ATOM   2017  CB  HIS A 934     -30.796  20.167  -1.558  1.00 28.20           C  
-ANISOU 2017  CB  HIS A 934     3261   3338   4115      6   -185   -570       C  
-ATOM   2018  CG  HIS A 934     -30.469  21.499  -2.165  1.00 29.21           C  
-ANISOU 2018  CG  HIS A 934     3366   3422   4311    -23   -178   -565       C  
-ATOM   2019  ND1 HIS A 934     -29.862  21.618  -3.396  1.00 29.51           N  
-ANISOU 2019  ND1 HIS A 934     3386   3446   4380    -57   -146   -532       N  
-ATOM   2020  CD2 HIS A 934     -30.689  22.765  -1.732  1.00 30.32           C  
-ANISOU 2020  CD2 HIS A 934     3498   3528   4493    -24   -198   -587       C  
-ATOM   2021  CE1 HIS A 934     -29.718  22.897  -3.694  1.00 30.69           C  
-ANISOU 2021  CE1 HIS A 934     3518   3553   4588    -79   -145   -530       C  
-ATOM   2022  NE2 HIS A 934     -30.210  23.615  -2.699  1.00 31.11           N  
-ANISOU 2022  NE2 HIS A 934     3576   3591   4652    -59   -179   -564       N  
-ATOM   2023  N   ALA A 935     -31.664  17.230  -1.476  1.00 24.57           N  
-ANISOU 2023  N   ALA A 935     2855   2955   3526     40   -166   -534       N  
-ATOM   2024  CA  ALA A 935     -31.959  15.947  -0.844  1.00 24.81           C  
-ANISOU 2024  CA  ALA A 935     2909   3018   3501     66   -174   -534       C  
-ATOM   2025  C   ALA A 935     -32.237  16.112   0.650  1.00 26.27           C  
-ANISOU 2025  C   ALA A 935     3105   3214   3663     98   -207   -569       C  
-ATOM   2026  O   ALA A 935     -31.562  16.865   1.342  1.00 28.14           O  
-ANISOU 2026  O   ALA A 935     3322   3438   3931    106   -234   -608       O  
-ATOM   2027  CB  ALA A 935     -30.804  14.976  -1.067  1.00 23.87           C  
-ANISOU 2027  CB  ALA A 935     2774   2910   3383     65   -175   -540       C  
-ATOM   2028  N   SER A 936     -33.207  15.357   1.138  1.00 25.59           N  
-ANISOU 2028  N   SER A 936     3050   3152   3522    118   -203   -554       N  
-ATOM   2029  CA  SER A 936     -33.526  15.303   2.539  1.00 25.05           C  
-ANISOU 2029  CA  SER A 936     2996   3101   3419    152   -228   -581       C  
-ATOM   2030  C   SER A 936     -34.334  14.028   2.766  1.00 24.75           C  
-ANISOU 2030  C   SER A 936     2991   3092   3322    165   -215   -551       C  
-ATOM   2031  O   SER A 936     -35.456  13.897   2.270  1.00 24.64           O  
-ANISOU 2031  O   SER A 936     2991   3080   3290    155   -190   -519       O  
-ATOM   2032  CB  SER A 936     -34.342  16.507   2.905  1.00 24.68           C  
-ANISOU 2032  CB  SER A 936     2952   3043   3383    156   -233   -594       C  
-ATOM   2033  OG  SER A 936     -34.450  16.583   4.307  1.00 26.69           O  
-ANISOU 2033  OG  SER A 936     3217   3317   3608    191   -260   -629       O  
-ATOM   2034  N   HIS A 937     -33.755  13.104   3.509  1.00 24.07           N  
-ANISOU 2034  N   HIS A 937     2913   3024   3208    187   -233   -562       N  
-ATOM   2035  CA  HIS A 937     -34.343  11.812   3.766  1.00 24.66           C  
-ANISOU 2035  CA  HIS A 937     3016   3121   3231    199   -222   -533       C  
-ATOM   2036  C   HIS A 937     -35.418  11.919   4.850  1.00 23.66           C  
-ANISOU 2036  C   HIS A 937     2915   3015   3059    223   -223   -533       C  
-ATOM   2037  O   HIS A 937     -35.157  11.741   6.023  1.00 24.22           O  
-ANISOU 2037  O   HIS A 937     2998   3105   3101    253   -247   -555       O  
-ATOM   2038  CB  HIS A 937     -33.277  10.781   4.168  1.00 26.01           C  
-ANISOU 2038  CB  HIS A 937     3189   3302   3390    216   -243   -542       C  
-ATOM   2039  CG  HIS A 937     -32.289  10.449   3.095  1.00 29.64           C  
-ANISOU 2039  CG  HIS A 937     3627   3748   3889    194   -238   -539       C  
-ATOM   2040  ND1 HIS A 937     -32.227  11.092   1.872  1.00 35.63           N  
-ANISOU 2040  ND1 HIS A 937     4363   4487   4689    162   -215   -529       N  
-ATOM   2041  CD2 HIS A 937     -31.258   9.580   3.100  1.00 33.74           C  
-ANISOU 2041  CD2 HIS A 937     4139   4271   4411    203   -252   -547       C  
-ATOM   2042  CE1 HIS A 937     -31.239  10.590   1.150  1.00 33.23           C  
-ANISOU 2042  CE1 HIS A 937     4040   4178   4407    151   -212   -530       C  
-ATOM   2043  NE2 HIS A 937     -30.636   9.670   1.875  1.00 34.69           N  
-ANISOU 2043  NE2 HIS A 937     4233   4376   4573    176   -235   -543       N  
-ATOM   2044  N   ILE A 938     -36.639  12.187   4.434  1.00 23.07           N  
-ANISOU 2044  N   ILE A 938     2848   2940   2978    211   -197   -509       N  
-ATOM   2045  CA  ILE A 938     -37.722  12.451   5.346  1.00 24.25           C  
-ANISOU 2045  CA  ILE A 938     3014   3109   3092    231   -193   -511       C  
-ATOM   2046  C   ILE A 938     -38.071  11.169   6.067  1.00 23.52           C  
-ANISOU 2046  C   ILE A 938     2949   3042   2944    249   -187   -488       C  
-ATOM   2047  O   ILE A 938     -38.243  10.153   5.419  1.00 24.40           O  
-ANISOU 2047  O   ILE A 938     3068   3151   3050    233   -170   -454       O  
-ATOM   2048  CB  ILE A 938     -38.953  12.897   4.576  1.00 25.13           C  
-ANISOU 2048  CB  ILE A 938     3123   3211   3212    211   -165   -487       C  
-ATOM   2049  CG1 ILE A 938     -38.658  14.145   3.747  1.00 25.56           C  
-ANISOU 2049  CG1 ILE A 938     3154   3235   3322    191   -168   -501       C  
-ATOM   2050  CG2 ILE A 938     -40.102  13.137   5.519  1.00 26.17           C  
-ANISOU 2050  CG2 ILE A 938     3270   3366   3308    232   -157   -490       C  
-ATOM   2051  CD1 ILE A 938     -38.151  15.330   4.550  1.00 27.64           C  
-ANISOU 2051  CD1 ILE A 938     3404   3491   3607    208   -197   -549       C  
-ATOM   2052  N   SER A 939     -38.068  11.203   7.400  1.00 23.51           N  
-ANISOU 2052  N   SER A 939     2963   3065   2905    282   -204   -509       N  
-ATOM   2053  CA ASER A 939     -38.606  10.113   8.224  0.50 23.91           C  
-ANISOU 2053  CA ASER A 939     3044   3144   2899    301   -194   -483       C  
-ATOM   2054  CA BSER A 939     -38.612  10.143   8.247  0.50 23.21           C  
-ANISOU 2054  CA BSER A 939     2955   3055   2809    301   -194   -484       C  
-ATOM   2055  C   SER A 939     -39.942  10.527   8.803  1.00 23.95           C  
-ANISOU 2055  C   SER A 939     3059   3169   2873    311   -172   -477       C  
-ATOM   2056  O   SER A 939     -40.772   9.690   9.011  1.00 26.13           O  
-ANISOU 2056  O   SER A 939     3353   3460   3114    310   -147   -441       O  
-ATOM   2057  CB ASER A 939     -37.633   9.677   9.334  0.50 24.75           C  
-ANISOU 2057  CB ASER A 939     3164   3266   2974    335   -227   -504       C  
-ATOM   2058  CB BSER A 939     -37.728   9.951   9.458  0.50 23.35           C  
-ANISOU 2058  CB BSER A 939     2985   3091   2796    338   -228   -511       C  
-ATOM   2059  OG ASER A 939     -36.463   9.098   8.770  0.50 24.80           O  
-ANISOU 2059  OG ASER A 939     3161   3255   3007    326   -245   -505       O  
-ATOM   2060  OG BSER A 939     -38.133   8.849  10.252  0.50 21.81           O  
-ANISOU 2060  OG BSER A 939     2823   2921   2545    357   -219   -481       O  
-ATOM   2061  N   LYS A 940     -40.126  11.816   9.098  1.00 25.20           N  
-ANISOU 2061  N   LYS A 940     3203   3327   3045    320   -182   -514       N  
-ATOM   2062  CA  LYS A 940     -41.432  12.336   9.465  1.00 26.10           C  
-ANISOU 2062  CA  LYS A 940     3320   3457   3140    327   -160   -512       C  
-ATOM   2063  C   LYS A 940     -41.517  13.737   8.930  1.00 26.63           C  
-ANISOU 2063  C   LYS A 940     3363   3501   3257    317   -168   -542       C  
-ATOM   2064  O   LYS A 940     -40.586  14.524   9.107  1.00 28.57           O  
-ANISOU 2064  O   LYS A 940     3594   3731   3529    326   -199   -582       O  
-ATOM   2065  CB  LYS A 940     -41.706  12.364  10.989  1.00 27.25           C  
-ANISOU 2065  CB  LYS A 940     3486   3642   3226    368   -166   -531       C  
-ATOM   2066  N   LEU A 941     -42.631  14.051   8.285  1.00 24.65           N  
-ANISOU 2066  N   LEU A 941     3104   3243   3020    300   -142   -523       N  
-ATOM   2067  CA  LEU A 941     -42.873  15.380   7.777  1.00 25.21           C  
-ANISOU 2067  CA  LEU A 941     3154   3290   3136    292   -148   -547       C  
-ATOM   2068  C   LEU A 941     -43.029  16.382   8.916  1.00 26.21           C  
-ANISOU 2068  C   LEU A 941     3279   3430   3249    327   -167   -595       C  
-ATOM   2069  O   LEU A 941     -43.449  16.015   9.984  1.00 26.94           O  
-ANISOU 2069  O   LEU A 941     3387   3559   3289    354   -161   -600       O  
-ATOM   2070  CB  LEU A 941     -44.140  15.394   6.926  1.00 24.60           C  
-ANISOU 2070  CB  LEU A 941     3071   3206   3069    272   -117   -515       C  
-ATOM   2071  CG  LEU A 941     -44.010  14.725   5.563  1.00 26.58           C  
-ANISOU 2071  CG  LEU A 941     3318   3435   3345    237   -104   -475       C  
-ATOM   2072  CD1 LEU A 941     -45.380  14.632   4.878  1.00 26.03           C  
-ANISOU 2072  CD1 LEU A 941     3245   3366   3278    222    -76   -446       C  
-ATOM   2073  CD2 LEU A 941     -43.045  15.504   4.689  1.00 26.18           C  
-ANISOU 2073  CD2 LEU A 941     3251   3349   3347    219   -122   -488       C  
-ATOM   2074  N   PRO A 942     -42.719  17.659   8.666  1.00 26.84           N  
-ANISOU 2074  N   PRO A 942     3339   3481   3377    325   -188   -630       N  
-ATOM   2075  CA  PRO A 942     -43.086  18.659   9.644  1.00 28.30           C  
-ANISOU 2075  CA  PRO A 942     3521   3678   3554    357   -204   -677       C  
-ATOM   2076  C   PRO A 942     -44.582  18.604   9.873  1.00 30.07           C  
-ANISOU 2076  C   PRO A 942     3751   3928   3748    367   -173   -662       C  
-ATOM   2077  O   PRO A 942     -45.349  18.408   8.913  1.00 31.24           O  
-ANISOU 2077  O   PRO A 942     3893   4064   3912    341   -147   -625       O  
-ATOM   2078  CB  PRO A 942     -42.689  19.992   8.978  1.00 28.06           C  
-ANISOU 2078  CB  PRO A 942     3467   3601   3595    343   -227   -705       C  
-ATOM   2079  CG  PRO A 942     -41.637  19.624   7.992  1.00 28.60           C  
-ANISOU 2079  CG  PRO A 942     3527   3640   3701    310   -231   -682       C  
-ATOM   2080  CD  PRO A 942     -41.927  18.214   7.551  1.00 27.14           C  
-ANISOU 2080  CD  PRO A 942     3358   3475   3480    295   -201   -630       C  
-ATOM   2081  N   LYS A 943     -45.002  18.787  11.123  1.00 29.88           N  
-ANISOU 2081  N   LYS A 943     3735   3940   3677    405   -175   -692       N  
-ATOM   2082  CA  LYS A 943     -46.413  18.742  11.474  1.00 31.03           C  
-ANISOU 2082  CA  LYS A 943     3884   4116   3790    417   -142   -682       C  
-ATOM   2083  C   LYS A 943     -47.102  19.808  10.628  1.00 29.63           C  
-ANISOU 2083  C   LYS A 943     3683   3906   3668    404   -141   -690       C  
-ATOM   2084  O   LYS A 943     -46.585  20.924  10.439  1.00 28.63           O  
-ANISOU 2084  O   LYS A 943     3544   3745   3590    406   -172   -727       O  
-ATOM   2085  CB  LYS A 943     -46.592  18.965  12.994  1.00 33.14           C  
-ANISOU 2085  CB  LYS A 943     4162   4428   4000    465   -149   -722       C  
-ATOM   2086  N   GLY A 944     -48.226  19.442  10.028  1.00 27.61           N  
-ANISOU 2086  N   GLY A 944     3423   3655   3411    387   -108   -653       N  
-ATOM   2087  CA  GLY A 944     -48.930  20.349   9.144  1.00 26.54           C  
-ANISOU 2087  CA  GLY A 944     3268   3488   3327    375   -107   -655       C  
-ATOM   2088  C   GLY A 944     -48.627  20.227   7.666  1.00 26.58           C  
-ANISOU 2088  C   GLY A 944     3268   3453   3380    335   -107   -618       C  
-ATOM   2089  O   GLY A 944     -49.365  20.767   6.836  1.00 30.04           O  
-ANISOU 2089  O   GLY A 944     3693   3869   3853    323   -102   -608       O  
-ATOM   2090  N   LYS A 945     -47.569  19.517   7.315  1.00 25.88           N  
-ANISOU 2090  N   LYS A 945     3188   3354   3292    315   -114   -599       N  
-ATOM   2091  CA  LYS A 945     -47.222  19.239   5.906  1.00 26.04           C  
-ANISOU 2091  CA  LYS A 945     3205   3341   3349    278   -110   -561       C  
-ATOM   2092  C   LYS A 945     -47.698  17.833   5.540  1.00 24.79           C  
-ANISOU 2092  C   LYS A 945     3057   3204   3159    261    -80   -514       C  
-ATOM   2093  O   LYS A 945     -47.613  16.932   6.367  1.00 24.74           O  
-ANISOU 2093  O   LYS A 945     3064   3229   3107    273    -71   -508       O  
-ATOM   2094  CB  LYS A 945     -45.718  19.294   5.714  1.00 27.03           C  
-ANISOU 2094  CB  LYS A 945     3329   3443   3497    267   -134   -571       C  
-ATOM   2095  CG  LYS A 945     -45.128  20.652   6.068  1.00 27.21           C  
-ANISOU 2095  CG  LYS A 945     3340   3440   3559    281   -167   -619       C  
-ATOM   2096  CD  LYS A 945     -45.481  21.661   5.017  1.00 27.54           C  
-ANISOU 2096  CD  LYS A 945     3368   3440   3655    263   -169   -612       C  
-ATOM   2097  CE  LYS A 945     -44.686  22.930   5.210  1.00 26.97           C  
-ANISOU 2097  CE  LYS A 945     3282   3332   3633    268   -202   -654       C  
-ATOM   2098  NZ  LYS A 945     -45.051  23.916   4.186  1.00 28.14           N  
-ANISOU 2098  NZ  LYS A 945     3420   3437   3835    251   -205   -642       N  
-ATOM   2099  N   HIS A 946     -48.177  17.650   4.313  1.00 24.28           N  
-ANISOU 2099  N   HIS A 946     2986   3121   3118    235    -68   -481       N  
-ATOM   2100  CA  HIS A 946     -48.688  16.340   3.908  1.00 23.64           C  
-ANISOU 2100  CA  HIS A 946     2913   3057   3014    219    -42   -440       C  
-ATOM   2101  C   HIS A 946     -47.908  15.695   2.791  1.00 23.52           C  
-ANISOU 2101  C   HIS A 946     2901   3020   3016    190    -45   -412       C  
-ATOM   2102  O   HIS A 946     -48.140  14.532   2.469  1.00 22.23           O  
-ANISOU 2102  O   HIS A 946     2745   2866   2835    177    -28   -381       O  
-ATOM   2103  CB  HIS A 946     -50.132  16.474   3.489  1.00 24.76           C  
-ANISOU 2103  CB  HIS A 946     3043   3203   3162    215    -24   -427       C  
-ATOM   2104  CG  HIS A 946     -50.959  17.228   4.463  1.00 26.45           C  
-ANISOU 2104  CG  HIS A 946     3248   3437   3364    244    -20   -457       C  
-ATOM   2105  ND1 HIS A 946     -51.191  18.578   4.322  1.00 28.78           N  
-ANISOU 2105  ND1 HIS A 946     3530   3710   3693    255    -38   -486       N  
-ATOM   2106  CD2 HIS A 946     -51.551  16.856   5.617  1.00 26.31           C  
-ANISOU 2106  CD2 HIS A 946     3234   3458   3305    265     -2   -465       C  
-ATOM   2107  CE1 HIS A 946     -51.914  19.004   5.341  1.00 27.85           C  
-ANISOU 2107  CE1 HIS A 946     3407   3620   3557    284    -31   -514       C  
-ATOM   2108  NE2 HIS A 946     -52.143  17.977   6.139  1.00 28.06           N  
-ANISOU 2108  NE2 HIS A 946     3442   3684   3534    290     -8   -501       N  
-ATOM   2109  N   SER A 947     -46.958  16.429   2.214  1.00 21.64           N  
-ANISOU 2109  N   SER A 947     2657   2752   2813    181    -64   -423       N  
-ATOM   2110  CA  SER A 947     -46.166  15.901   1.130  1.00 21.32           C  
-ANISOU 2110  CA  SER A 947     2619   2693   2788    156    -64   -399       C  
-ATOM   2111  C   SER A 947     -44.890  16.697   0.947  1.00 21.65           C  
-ANISOU 2111  C   SER A 947     2654   2710   2864    151    -85   -419       C  
-ATOM   2112  O   SER A 947     -44.728  17.771   1.538  1.00 23.58           O  
-ANISOU 2112  O   SER A 947     2889   2943   3125    166   -102   -452       O  
-ATOM   2113  CB  SER A 947     -46.965  15.985  -0.148  1.00 21.54           C  
-ANISOU 2113  CB  SER A 947     2642   2707   2834    137    -53   -372       C  
-ATOM   2114  OG  SER A 947     -47.295  17.316  -0.458  1.00 20.01           O  
-ANISOU 2114  OG  SER A 947     2439   2491   2674    140    -63   -385       O  
-ATOM   2115  N   VAL A 948     -43.973  16.159   0.167  1.00 19.94           N  
-ANISOU 2115  N   VAL A 948     2437   2483   2658    132    -84   -403       N  
-ATOM   2116  CA  VAL A 948     -42.815  16.899  -0.260  1.00 20.04           C  
-ANISOU 2116  CA  VAL A 948     2438   2469   2709    121    -98   -415       C  
-ATOM   2117  C   VAL A 948     -42.955  17.265  -1.727  1.00 20.21           C  
-ANISOU 2117  C   VAL A 948     2455   2466   2758     96    -87   -387       C  
-ATOM   2118  O   VAL A 948     -43.379  16.427  -2.549  1.00 19.66           O  
-ANISOU 2118  O   VAL A 948     2393   2405   2672     85    -71   -357       O  
-ATOM   2119  CB  VAL A 948     -41.519  16.109  -0.054  1.00 19.53           C  
-ANISOU 2119  CB  VAL A 948     2373   2410   2638    119   -105   -421       C  
-ATOM   2120  CG1 VAL A 948     -40.358  16.767  -0.792  1.00 20.40           C  
-ANISOU 2120  CG1 VAL A 948     2466   2492   2792    100   -112   -426       C  
-ATOM   2121  CG2 VAL A 948     -41.173  16.039   1.422  1.00 20.51           C  
-ANISOU 2121  CG2 VAL A 948     2501   2553   2739    146   -123   -455       C  
-ATOM   2122  N   LYS A 949     -42.586  18.497  -2.061  1.00 20.04           N  
-ANISOU 2122  N   LYS A 949     2422   2414   2777     89    -97   -396       N  
-ATOM   2123  CA  LYS A 949     -42.367  18.881  -3.463  1.00 20.56           C  
-ANISOU 2123  CA  LYS A 949     2486   2456   2871     65    -87   -368       C  
-ATOM   2124  C   LYS A 949     -40.903  19.224  -3.663  1.00 21.07           C  
-ANISOU 2124  C   LYS A 949     2537   2502   2969     50    -93   -377       C  
-ATOM   2125  O   LYS A 949     -40.394  20.159  -3.036  1.00 22.19           O  
-ANISOU 2125  O   LYS A 949     2665   2623   3142     55   -111   -406       O  
-ATOM   2126  CB  LYS A 949     -43.175  20.105  -3.813  1.00 20.40           C  
-ANISOU 2126  CB  LYS A 949     2463   2409   2877     66    -92   -364       C  
-ATOM   2127  CG  LYS A 949     -42.964  20.553  -5.235  1.00 20.76           C  
-ANISOU 2127  CG  LYS A 949     2510   2431   2949     43    -83   -331       C  
-ATOM   2128  CD  LYS A 949     -43.810  21.739  -5.570  1.00 21.73           C  
-ANISOU 2128  CD  LYS A 949     2633   2526   3097     47    -91   -325       C  
-ATOM   2129  CE  LYS A 949     -43.585  22.142  -6.999  1.00 23.56           C  
-ANISOU 2129  CE  LYS A 949     2869   2734   3348     25    -80   -286       C  
-ATOM   2130  NZ  LYS A 949     -44.254  23.410  -7.303  1.00 25.49           N  
-ANISOU 2130  NZ  LYS A 949     3115   2945   3624     30    -91   -279       N  
-ATOM   2131  N   GLY A 950     -40.220  18.454  -4.503  1.00 20.83           N  
-ANISOU 2131  N   GLY A 950     2505   2477   2932     33    -78   -355       N  
-ATOM   2132  CA  GLY A 950     -38.862  18.787  -4.915  1.00 22.46           C  
-ANISOU 2132  CA  GLY A 950     2695   2666   3174     15    -77   -358       C  
-ATOM   2133  C   GLY A 950     -38.978  19.842  -5.992  1.00 22.94           C  
-ANISOU 2133  C   GLY A 950     2752   2695   3268     -4    -67   -333       C  
-ATOM   2134  O   GLY A 950     -39.621  19.588  -6.992  1.00 24.50           O  
-ANISOU 2134  O   GLY A 950     2964   2898   3449    -11    -51   -299       O  
-ATOM   2135  N   LEU A 951     -38.369  21.004  -5.788  1.00 23.18           N  
-ANISOU 2135  N   LEU A 951     2766   2693   3347    -12    -79   -348       N  
-ATOM   2136  CA  LEU A 951     -38.544  22.150  -6.686  1.00 24.21           C  
-ANISOU 2136  CA  LEU A 951     2896   2788   3515    -29    -72   -323       C  
-ATOM   2137  C   LEU A 951     -37.630  22.077  -7.904  1.00 25.56           C  
-ANISOU 2137  C   LEU A 951     3060   2952   3701    -57    -47   -291       C  
-ATOM   2138  O   LEU A 951     -36.429  22.165  -7.768  1.00 26.06           O  
-ANISOU 2138  O   LEU A 951     3101   3007   3794    -70    -46   -305       O  
-ATOM   2139  CB  LEU A 951     -38.271  23.434  -5.949  1.00 24.54           C  
-ANISOU 2139  CB  LEU A 951     2922   2794   3608    -26    -95   -353       C  
-ATOM   2140  CG  LEU A 951     -39.213  23.676  -4.786  1.00 26.42           C  
-ANISOU 2140  CG  LEU A 951     3167   3039   3832      4   -119   -387       C  
-ATOM   2141  CD1 LEU A 951     -38.869  24.989  -4.084  1.00 27.86           C  
-ANISOU 2141  CD1 LEU A 951     3333   3183   4069      8   -145   -423       C  
-ATOM   2142  CD2 LEU A 951     -40.658  23.715  -5.254  1.00 26.70           C  
-ANISOU 2142  CD2 LEU A 951     3223   3080   3842     14   -112   -362       C  
-ATOM   2143  N   GLY A 952     -38.210  21.895  -9.094  1.00 26.64           N  
-ANISOU 2143  N   GLY A 952     3213   3093   3815    -65    -27   -249       N  
-ATOM   2144  CA  GLY A 952     -37.433  21.915 -10.343  1.00 27.25           C  
-ANISOU 2144  CA  GLY A 952     3286   3166   3902    -90      0   -214       C  
-ATOM   2145  C   GLY A 952     -37.155  23.318 -10.873  1.00 27.16           C  
-ANISOU 2145  C   GLY A 952     3268   3109   3941   -110      5   -192       C  
-ATOM   2146  O   GLY A 952     -37.802  24.272 -10.472  1.00 24.03           O  
-ANISOU 2146  O   GLY A 952     2876   2685   3570   -102    -15   -199       O  
-ATOM   2147  N   LYS A 953     -36.193  23.423 -11.777  1.00 28.73           N  
-ANISOU 2147  N   LYS A 953     3457   3303   4158   -135     31   -166       N  
-ATOM   2148  CA  LYS A 953     -35.942  24.673 -12.514  1.00 31.15           C  
-ANISOU 2148  CA  LYS A 953     3760   3567   4508   -158     43   -133       C  
-ATOM   2149  C   LYS A 953     -37.044  24.963 -13.538  1.00 32.68           C  
-ANISOU 2149  C   LYS A 953     3985   3756   4674   -153     50    -87       C  
-ATOM   2150  O   LYS A 953     -37.276  26.115 -13.907  1.00 33.33           O  
-ANISOU 2150  O   LYS A 953     4073   3798   4791   -162     48    -61       O  
-ATOM   2151  CB  LYS A 953     -34.589  24.609 -13.236  1.00 31.54           C  
-ANISOU 2151  CB  LYS A 953     3787   3617   4578   -187     76   -114       C  
-ATOM   2152  CG  LYS A 953     -33.436  24.517 -12.273  1.00 35.74           C  
-ANISOU 2152  CG  LYS A 953     4284   4146   5150   -193     66   -160       C  
-ATOM   2153  CD  LYS A 953     -32.060  24.486 -12.902  1.00 42.14           C  
-ANISOU 2153  CD  LYS A 953     5066   4957   5989   -222     98   -147       C  
-ATOM   2154  CE  LYS A 953     -31.035  24.221 -11.766  1.00 46.22           C  
-ANISOU 2154  CE  LYS A 953     5546   5476   6539   -220     78   -203       C  
-ATOM   2155  NZ  LYS A 953     -29.690  24.662 -12.210  1.00 52.31           N  
-ANISOU 2155  NZ  LYS A 953     6281   6230   7365   -253    104   -195       N  
-ATOM   2156  N   THR A 954     -37.682  23.906 -14.031  1.00 30.15           N  
-ANISOU 2156  N   THR A 954     3685   3477   4293   -139     58    -76       N  
-ATOM   2157  CA  THR A 954     -38.742  24.023 -15.013  1.00 30.03           C  
-ANISOU 2157  CA  THR A 954     3699   3464   4246   -131     61    -37       C  
-ATOM   2158  C   THR A 954     -40.005  23.419 -14.421  1.00 31.71           C  
-ANISOU 2158  C   THR A 954     3925   3698   4424   -102     36    -60       C  
-ATOM   2159  O   THR A 954     -39.956  22.353 -13.768  1.00 31.78           O  
-ANISOU 2159  O   THR A 954     3928   3738   4407    -92     32    -90       O  
-ATOM   2160  CB  THR A 954     -38.364  23.265 -16.286  1.00 30.75           C  
-ANISOU 2160  CB  THR A 954     3801   3587   4296   -140     93     -3       C  
-ATOM   2161  OG1 THR A 954     -37.154  23.813 -16.824  1.00 27.57           O  
-ANISOU 2161  OG1 THR A 954     3382   3167   3925   -168    121     20       O  
-ATOM   2162  CG2 THR A 954     -39.469  23.327 -17.340  1.00 31.65           C  
-ANISOU 2162  CG2 THR A 954     3947   3708   4371   -128     92     35       C  
-ATOM   2163  N   THR A 955     -41.114  24.110 -14.619  1.00 32.08           N  
-ANISOU 2163  N   THR A 955     3989   3727   4473    -90     20    -45       N  
-ATOM   2164  CA  THR A 955     -42.384  23.713 -14.089  1.00 35.86           C  
-ANISOU 2164  CA  THR A 955     4477   4221   4926    -64     -1    -66       C  
-ATOM   2165  C   THR A 955     -43.447  23.890 -15.177  1.00 42.43           C  
-ANISOU 2165  C   THR A 955     5334   5055   5734    -55     -4    -29       C  
-ATOM   2166  O   THR A 955     -43.300  24.752 -16.020  1.00 41.64           O  
-ANISOU 2166  O   THR A 955     5245   4928   5650    -64      2      7       O  
-ATOM   2167  CB  THR A 955     -42.768  24.529 -12.847  1.00 35.91           C  
-ANISOU 2167  CB  THR A 955     4472   4202   4971    -52    -28   -101       C  
-ATOM   2168  OG1 THR A 955     -43.962  23.985 -12.284  1.00 39.24           O  
-ANISOU 2168  OG1 THR A 955     4899   4647   5363    -27    -43   -122       O  
-ATOM   2169  CG2 THR A 955     -43.026  26.017 -13.157  1.00 37.25           C  
-ANISOU 2169  CG2 THR A 955     4647   4322   5185    -54    -39    -81       C  
-ATOM   2170  N   PRO A 956     -44.515  23.058 -15.171  1.00 47.15           N  
-ANISOU 2170  N   PRO A 956     5941   5682   6293    -35    -14    -38       N  
-ATOM   2171  CA  PRO A 956     -45.595  23.300 -16.133  1.00 46.24           C  
-ANISOU 2171  CA  PRO A 956     5846   5564   6157    -23    -23     -9       C  
-ATOM   2172  C   PRO A 956     -46.248  24.643 -15.874  1.00 41.76           C  
-ANISOU 2172  C   PRO A 956     5281   4956   5629    -13    -45     -7       C  
-ATOM   2173  O   PRO A 956     -46.409  25.035 -14.723  1.00 45.70           O  
-ANISOU 2173  O   PRO A 956     5765   5442   6157     -5    -60    -41       O  
-ATOM   2174  CB  PRO A 956     -46.570  22.155 -15.853  1.00 47.74           C  
-ANISOU 2174  CB  PRO A 956     6036   5791   6311     -6    -33    -31       C  
-ATOM   2175  CG  PRO A 956     -45.724  21.055 -15.302  1.00 49.40           C  
-ANISOU 2175  CG  PRO A 956     6234   6029   6507    -15    -18    -54       C  
-ATOM   2176  CD  PRO A 956     -44.745  21.809 -14.417  1.00 47.74           C  
-ANISOU 2176  CD  PRO A 956     6008   5793   6340    -26    -16    -71       C  
-ATOM   2177  N   ASP A 957     -46.549  25.365 -16.940  1.00 41.08           N  
-ANISOU 2177  N   ASP A 957     5215   4851   5545    -12    -47     34       N  
-ATOM   2178  CA  ASP A 957     -47.106  26.714 -16.842  1.00 39.64           C  
-ANISOU 2178  CA  ASP A 957     5036   4622   5402     -2    -69     43       C  
-ATOM   2179  C   ASP A 957     -48.399  26.718 -16.049  1.00 39.84           C  
-ANISOU 2179  C   ASP A 957     5055   4653   5431     25    -97      8       C  
-ATOM   2180  O   ASP A 957     -49.393  26.148 -16.487  1.00 36.95           O  
-ANISOU 2180  O   ASP A 957     4697   4312   5031     42   -106     11       O  
-ATOM   2181  CB  ASP A 957     -47.372  27.232 -18.240  1.00 41.88           C  
-ANISOU 2181  CB  ASP A 957     5348   4893   5673     -1    -68     96       C  
-ATOM   2182  CG  ASP A 957     -47.808  28.693 -18.260  1.00 45.43           C  
-ANISOU 2182  CG  ASP A 957     5805   5288   6168      7    -90    112       C  
-ATOM   2183  OD1 ASP A 957     -48.210  29.227 -17.213  1.00 42.35           O  
-ANISOU 2183  OD1 ASP A 957     5399   4876   5815     19   -112     76       O  
-ATOM   2184  OD2 ASP A 957     -47.770  29.291 -19.360  1.00 48.33           O  
-ANISOU 2184  OD2 ASP A 957     6196   5635   6533      4    -87    163       O  
-ATOM   2185  N   PRO A 958     -48.406  27.369 -14.877  1.00 45.75           N  
-ANISOU 2185  N   PRO A 958     5785   5378   6219     31   -111    -28       N  
-ATOM   2186  CA  PRO A 958     -49.590  27.365 -13.998  1.00 46.25           C  
-ANISOU 2186  CA  PRO A 958     5837   5450   6285     58   -133    -66       C  
-ATOM   2187  C   PRO A 958     -50.862  27.910 -14.637  1.00 48.55           C  
-ANISOU 2187  C   PRO A 958     6142   5729   6578     81   -156    -50       C  
-ATOM   2188  O   PRO A 958     -51.952  27.508 -14.254  1.00 54.03           O  
-ANISOU 2188  O   PRO A 958     6827   6446   7257    102   -169    -74       O  
-ATOM   2189  CB  PRO A 958     -49.171  28.268 -12.837  1.00 46.81           C  
-ANISOU 2189  CB  PRO A 958     5892   5489   6405     60   -145   -101       C  
-ATOM   2190  CG  PRO A 958     -47.692  28.274 -12.853  1.00 46.72           C  
-ANISOU 2190  CG  PRO A 958     5876   5467   6409     32   -125    -93       C  
-ATOM   2191  CD  PRO A 958     -47.266  28.080 -14.270  1.00 45.50           C  
-ANISOU 2191  CD  PRO A 958     5741   5314   6234     13   -106    -39       C  
-ATOM   2192  N   SER A 959     -50.731  28.799 -15.611  1.00 48.78           N  
-ANISOU 2192  N   SER A 959     6190   5722   6623     77   -162     -8       N  
-ATOM   2193  CA  SER A 959     -51.914  29.389 -16.217  1.00 51.27           C  
-ANISOU 2193  CA  SER A 959     6518   6022   6941    102   -188      8       C  
-ATOM   2194  C   SER A 959     -52.631  28.391 -17.118  1.00 48.81           C  
-ANISOU 2194  C   SER A 959     6218   5752   6576    111   -187     25       C  
-ATOM   2195  O   SER A 959     -53.809  28.585 -17.464  1.00 48.46           O  
-ANISOU 2195  O   SER A 959     6178   5707   6527    136   -212     25       O  
-ATOM   2196  CB  SER A 959     -51.573  30.693 -16.961  1.00 51.38           C  
-ANISOU 2196  CB  SER A 959     6552   5981   6990     97   -196     51       C  
-ATOM   2197  OG  SER A 959     -50.906  30.449 -18.178  1.00 55.02           O  
-ANISOU 2197  OG  SER A 959     7036   6448   7422     78   -175    103       O  
-ATOM   2198  N   ALA A 960     -51.922  27.338 -17.533  1.00 45.16           N  
-ANISOU 2198  N   ALA A 960     5760   5324   6075     92   -161     36       N  
-ATOM   2199  CA  ALA A 960     -52.534  26.304 -18.368  1.00 39.71           C  
-ANISOU 2199  CA  ALA A 960     5079   4674   5334    100   -162     46       C  
-ATOM   2200  C   ALA A 960     -53.137  25.145 -17.556  1.00 37.17           C  
-ANISOU 2200  C   ALA A 960     4735   4392   4995    107   -162      3       C  
-ATOM   2201  O   ALA A 960     -53.646  24.207 -18.141  1.00 37.49           O  
-ANISOU 2201  O   ALA A 960     4780   4465   5000    112   -163      5       O  
-ATOM   2202  CB  ALA A 960     -51.553  25.804 -19.411  1.00 38.98           C  
-ANISOU 2202  CB  ALA A 960     5006   4597   5208     80   -137     82       C  
-ATOM   2203  N   ASN A 961     -53.096  25.184 -16.227  1.00 35.06           N  
-ANISOU 2203  N   ASN A 961     4446   4124   4753    107   -159    -36       N  
-ATOM   2204  CA  ASN A 961     -53.816  24.126 -15.476  1.00 35.50           C  
-ANISOU 2204  CA  ASN A 961     4481   4216   4790    115   -158    -71       C  
-ATOM   2205  C   ASN A 961     -55.298  23.903 -15.853  1.00 37.81           C  
-ANISOU 2205  C   ASN A 961     4769   4523   5073    137   -180    -77       C  
-ATOM   2206  O   ASN A 961     -56.031  24.843 -16.026  1.00 43.81           O  
-ANISOU 2206  O   ASN A 961     5530   5260   5856    156   -203    -74       O  
-ATOM   2207  CB  ASN A 961     -53.823  24.417 -14.003  1.00 36.58           C  
-ANISOU 2207  CB  ASN A 961     4596   4348   4953    119   -157   -111       C  
-ATOM   2208  CG  ASN A 961     -52.507  24.135 -13.314  1.00 39.37           C  
-ANISOU 2208  CG  ASN A 961     4946   4704   5309     99   -136   -121       C  
-ATOM   2209  OD1 ASN A 961     -52.467  24.283 -12.124  1.00 47.80           O  
-ANISOU 2209  OD1 ASN A 961     5997   5772   6391    105   -136   -154       O  
-ATOM   2210  ND2 ASN A 961     -51.431  23.800 -14.029  1.00 39.62           N  
-ANISOU 2210  ND2 ASN A 961     4990   4737   5326     78   -120    -95       N  
-ATOM   2211  N   ILE A 962     -55.735  22.656 -15.916  1.00 37.47           N  
-ANISOU 2211  N   ILE A 962     4718   4517   5002    136   -174    -87       N  
-ATOM   2212  CA  ILE A 962     -57.115  22.296 -16.218  1.00 40.50           C  
-ANISOU 2212  CA  ILE A 962     5091   4917   5380    154   -194    -98       C  
-ATOM   2213  C   ILE A 962     -57.636  21.401 -15.115  1.00 42.19           C  
-ANISOU 2213  C   ILE A 962     5277   5159   5594    153   -182   -133       C  
-ATOM   2214  O   ILE A 962     -56.915  20.539 -14.647  1.00 45.71           O  
-ANISOU 2214  O   ILE A 962     5722   5622   6025    135   -160   -138       O  
-ATOM   2215  CB  ILE A 962     -57.238  21.443 -17.501  1.00 44.02           C  
-ANISOU 2215  CB  ILE A 962     5552   5384   5790    152   -199    -77       C  
-ATOM   2216  CG1 ILE A 962     -56.484  22.114 -18.638  1.00 49.82           C  
-ANISOU 2216  CG1 ILE A 962     6318   6098   6512    149   -200    -36       C  
-ATOM   2217  CG2 ILE A 962     -58.690  21.176 -17.879  1.00 45.18           C  
-ANISOU 2217  CG2 ILE A 962     5686   5544   5937    173   -225    -89       C  
-ATOM   2218  CD1 ILE A 962     -56.969  23.473 -19.117  1.00 56.17           C  
-ANISOU 2218  CD1 ILE A 962     7135   6869   7338    168   -226    -16       C  
-ATOM   2219  N   SER A 963     -58.895  21.551 -14.731  1.00 40.67           N  
-ANISOU 2219  N   SER A 963     5062   4971   5418    172   -197   -154       N  
-ATOM   2220  CA  SER A 963     -59.479  20.664 -13.733  1.00 40.24           C  
-ANISOU 2220  CA  SER A 963     4981   4946   5363    170   -182   -183       C  
-ATOM   2221  C   SER A 963     -60.085  19.537 -14.477  1.00 38.47           C  
-ANISOU 2221  C   SER A 963     4752   4745   5120    166   -187   -179       C  
-ATOM   2222  O   SER A 963     -60.798  19.769 -15.459  1.00 37.97           O  
-ANISOU 2222  O   SER A 963     4693   4678   5058    179   -212   -170       O  
-ATOM   2223  CB  SER A 963     -60.616  21.307 -12.961  1.00 39.09           C  
-ANISOU 2223  CB  SER A 963     4809   4799   5245    192   -192   -211       C  
-ATOM   2224  OG  SER A 963     -60.113  22.249 -12.068  1.00 43.38           O  
-ANISOU 2224  OG  SER A 963     5352   5324   5806    198   -188   -224       O  
-ATOM   2225  N   LEU A 964     -59.863  18.338 -13.967  1.00 36.61           N  
-ANISOU 2225  N   LEU A 964     4508   4532   4869    149   -165   -188       N  
-ATOM   2226  CA  LEU A 964     -60.496  17.125 -14.501  1.00 36.04           C  
-ANISOU 2226  CA  LEU A 964     4426   4482   4786    142   -169   -190       C  
-ATOM   2227  C   LEU A 964     -61.176  16.423 -13.356  1.00 38.77           C  
-ANISOU 2227  C   LEU A 964     4742   4848   5143    138   -151   -213       C  
-ATOM   2228  O   LEU A 964     -60.520  15.965 -12.410  1.00 38.01           O  
-ANISOU 2228  O   LEU A 964     4645   4759   5038    125   -126   -216       O  
-ATOM   2229  CB  LEU A 964     -59.462  16.230 -15.151  1.00 35.06           C  
-ANISOU 2229  CB  LEU A 964     4325   4364   4634    124   -160   -173       C  
-ATOM   2230  CG  LEU A 964     -59.850  14.909 -15.811  1.00 35.66           C  
-ANISOU 2230  CG  LEU A 964     4396   4458   4696    116   -165   -175       C  
-ATOM   2231  CD1 LEU A 964     -60.623  15.210 -17.083  1.00 38.10           C  
-ANISOU 2231  CD1 LEU A 964     4709   4764   5002    133   -198   -170       C  
-ATOM   2232  CD2 LEU A 964     -58.629  14.081 -16.159  1.00 33.96           C  
-ANISOU 2232  CD2 LEU A 964     4201   4248   4454     99   -151   -164       C  
-ATOM   2233  N   ASP A 965     -62.509  16.448 -13.396  1.00 42.04           N  
-ANISOU 2233  N   ASP A 965     5128   5268   5576    150   -164   -228       N  
-ATOM   2234  CA  ASP A 965     -63.359  15.885 -12.385  1.00 43.38           C  
-ANISOU 2234  CA  ASP A 965     5264   5457   5760    148   -147   -248       C  
-ATOM   2235  C   ASP A 965     -62.902  16.285 -10.969  1.00 41.45           C  
-ANISOU 2235  C   ASP A 965     5017   5218   5516    148   -120   -258       C  
-ATOM   2236  O   ASP A 965     -62.761  15.454 -10.074  1.00 45.22           O  
-ANISOU 2236  O   ASP A 965     5486   5712   5984    135    -93   -262       O  
-ATOM   2237  CB  ASP A 965     -63.439  14.395 -12.668  1.00 51.02           C  
-ANISOU 2237  CB  ASP A 965     6227   6440   6719    127   -139   -244       C  
-ATOM   2238  CG  ASP A 965     -64.116  14.072 -14.067  1.00 60.63           C  
-ANISOU 2238  CG  ASP A 965     7441   7655   7939    132   -172   -243       C  
-ATOM   2239  OD1 ASP A 965     -63.938  12.924 -14.583  1.00 61.68           O  
-ANISOU 2239  OD1 ASP A 965     7578   7794   8062    116   -172   -239       O  
-ATOM   2240  OD2 ASP A 965     -64.809  14.962 -14.659  1.00 59.87           O  
-ANISOU 2240  OD2 ASP A 965     7341   7551   7856    154   -199   -247       O  
-ATOM   2241  N   GLY A 966     -62.630  17.583 -10.812  1.00 38.86           N  
-ANISOU 2241  N   GLY A 966     4699   4871   5197    165   -130   -262       N  
-ATOM   2242  CA  GLY A 966     -62.300  18.197  -9.536  1.00 35.98           C  
-ANISOU 2242  CA  GLY A 966     4329   4507   4834    173   -113   -279       C  
-ATOM   2243  C   GLY A 966     -60.821  18.252  -9.212  1.00 35.82           C  
-ANISOU 2243  C   GLY A 966     4336   4477   4796    161   -102   -269       C  
-ATOM   2244  O   GLY A 966     -60.419  18.837  -8.201  1.00 37.58           O  
-ANISOU 2244  O   GLY A 966     4559   4699   5021    169    -93   -285       O  
-ATOM   2245  N   VAL A 967     -59.992  17.635 -10.035  1.00 32.07           N  
-ANISOU 2245  N   VAL A 967     3883   3997   4304    143   -103   -246       N  
-ATOM   2246  CA  VAL A 967     -58.539  17.550  -9.728  1.00 29.05           C  
-ANISOU 2246  CA  VAL A 967     3522   3609   3906    130    -91   -238       C  
-ATOM   2247  C   VAL A 967     -57.764  18.394 -10.708  1.00 27.47           C  
-ANISOU 2247  C   VAL A 967     3345   3381   3710    129   -107   -220       C  
-ATOM   2248  O   VAL A 967     -57.996  18.343 -11.905  1.00 30.11           O  
-ANISOU 2248  O   VAL A 967     3689   3709   4042    129   -122   -202       O  
-ATOM   2249  CB  VAL A 967     -58.057  16.088  -9.846  1.00 27.75           C  
-ANISOU 2249  CB  VAL A 967     3364   3461   3718    109    -75   -227       C  
-ATOM   2250  CG1 VAL A 967     -56.577  15.972  -9.548  1.00 25.67           C  
-ANISOU 2250  CG1 VAL A 967     3121   3193   3441     98    -65   -221       C  
-ATOM   2251  CG2 VAL A 967     -58.883  15.181  -8.927  1.00 27.99           C  
-ANISOU 2251  CG2 VAL A 967     3372   3516   3745    107    -57   -239       C  
-ATOM   2252  N   ASP A 968     -56.780  19.101 -10.235  1.00 31.44           N  
-ANISOU 2252  N   ASP A 968     3859   3868   4220    128   -104   -223       N  
-ATOM   2253  CA  ASP A 968     -55.918  19.826 -11.138  1.00 32.92           C  
-ANISOU 2253  CA  ASP A 968     4066   4028   4412    123   -114   -201       C  
-ATOM   2254  C   ASP A 968     -54.976  18.939 -11.939  1.00 28.79           C  
-ANISOU 2254  C   ASP A 968     3560   3512   3865    102   -103   -179       C  
-ATOM   2255  O   ASP A 968     -54.257  18.088 -11.403  1.00 27.14           O  
-ANISOU 2255  O   ASP A 968     3352   3319   3642     90    -87   -184       O  
-ATOM   2256  CB  ASP A 968     -55.070  20.843 -10.388  1.00 40.89           C  
-ANISOU 2256  CB  ASP A 968     5078   5015   5442    125   -113   -213       C  
-ATOM   2257  CG  ASP A 968     -55.873  22.093  -9.997  1.00 51.24           C  
-ANISOU 2257  CG  ASP A 968     6379   6307   6783    148   -131   -230       C  
-ATOM   2258  OD1 ASP A 968     -57.002  22.276 -10.532  1.00 54.30           O  
-ANISOU 2258  OD1 ASP A 968     6760   6694   7177    161   -146   -227       O  
-ATOM   2259  OD2 ASP A 968     -55.366  22.877  -9.150  1.00 66.63           O  
-ANISOU 2259  OD2 ASP A 968     8325   8240   8751    153   -133   -250       O  
-ATOM   2260  N   VAL A 969     -54.898  19.281 -13.208  1.00 26.15           N  
-ANISOU 2260  N   VAL A 969     3243   3166   3529    101   -114   -154       N  
-ATOM   2261  CA  VAL A 969     -53.982  18.677 -14.129  1.00 25.75           C  
-ANISOU 2261  CA  VAL A 969     3209   3120   3455     86   -106   -132       C  
-ATOM   2262  C   VAL A 969     -53.005  19.729 -14.607  1.00 25.54           C  
-ANISOU 2262  C   VAL A 969     3199   3066   3440     80   -104   -111       C  
-ATOM   2263  O   VAL A 969     -53.379  20.622 -15.367  1.00 25.22           O  
-ANISOU 2263  O   VAL A 969     3168   3005   3408     89   -119    -92       O  
-ATOM   2264  CB  VAL A 969     -54.770  18.118 -15.297  1.00 25.68           C  
-ANISOU 2264  CB  VAL A 969     3206   3124   3427     91   -118   -119       C  
-ATOM   2265  CG1 VAL A 969     -53.885  17.286 -16.165  1.00 26.09           C  
-ANISOU 2265  CG1 VAL A 969     3274   3188   3450     77   -107   -103       C  
-ATOM   2266  CG2 VAL A 969     -55.953  17.297 -14.768  1.00 26.58           C  
-ANISOU 2266  CG2 VAL A 969     3299   3258   3542     98   -123   -141       C  
-ATOM   2267  N   PRO A 970     -51.738  19.644 -14.166  1.00 26.44           N  
-ANISOU 2267  N   PRO A 970     3313   3176   3556     64    -87   -113       N  
-ATOM   2268  CA  PRO A 970     -50.753  20.638 -14.602  1.00 26.62           C  
-ANISOU 2268  CA  PRO A 970     3347   3172   3597     55    -83    -92       C  
-ATOM   2269  C   PRO A 970     -50.188  20.361 -15.989  1.00 27.61           C  
-ANISOU 2269  C   PRO A 970     3491   3302   3698     44    -74    -59       C  
-ATOM   2270  O   PRO A 970     -49.002  20.000 -16.140  1.00 28.66           O  
-ANISOU 2270  O   PRO A 970     3626   3441   3824     27    -55    -53       O  
-ATOM   2271  CB  PRO A 970     -49.671  20.515 -13.543  1.00 26.55           C  
-ANISOU 2271  CB  PRO A 970     3327   3162   3599     43    -70   -113       C  
-ATOM   2272  CG  PRO A 970     -49.694  19.050 -13.191  1.00 27.37           C  
-ANISOU 2272  CG  PRO A 970     3425   3300   3673     41    -60   -128       C  
-ATOM   2273  CD  PRO A 970     -51.119  18.600 -13.337  1.00 26.17           C  
-ANISOU 2273  CD  PRO A 970     3271   3164   3510     55    -72   -132       C  
-ATOM   2274  N   LEU A 971     -51.018  20.520 -17.011  1.00 27.65           N  
-ANISOU 2274  N   LEU A 971     3510   3308   3689     56    -88    -39       N  
-ATOM   2275  CA  LEU A 971     -50.632  20.088 -18.359  1.00 28.78           C  
-ANISOU 2275  CA  LEU A 971     3672   3465   3798     51    -80    -10       C  
-ATOM   2276  C   LEU A 971     -50.016  21.202 -19.190  1.00 30.61           C  
-ANISOU 2276  C   LEU A 971     3922   3671   4039     45    -74     28       C  
-ATOM   2277  O   LEU A 971     -49.814  21.045 -20.396  1.00 30.19           O  
-ANISOU 2277  O   LEU A 971     3888   3628   3954     44    -68     57       O  
-ATOM   2278  CB  LEU A 971     -51.800  19.422 -19.087  1.00 29.49           C  
-ANISOU 2278  CB  LEU A 971     3768   3577   3861     67    -98    -10       C  
-ATOM   2279  CG  LEU A 971     -53.155  20.092 -19.059  1.00 29.82           C  
-ANISOU 2279  CG  LEU A 971     3806   3605   3918     88   -127    -14       C  
-ATOM   2280  CD1 LEU A 971     -53.080  21.452 -19.715  1.00 30.53           C  
-ANISOU 2280  CD1 LEU A 971     3915   3664   4022     95   -136     18       C  
-ATOM   2281  CD2 LEU A 971     -54.156  19.220 -19.764  1.00 30.13           C  
-ANISOU 2281  CD2 LEU A 971     3847   3671   3931    102   -144    -20       C  
-ATOM   2282  N   GLY A 972     -49.668  22.310 -18.554  1.00 32.21           N  
-ANISOU 2282  N   GLY A 972     4118   3839   4282     40    -75     29       N  
-ATOM   2283  CA  GLY A 972     -48.957  23.377 -19.252  1.00 34.46           C  
-ANISOU 2283  CA  GLY A 972     4418   4093   4581     29    -66     67       C  
-ATOM   2284  C   GLY A 972     -47.598  22.943 -19.772  1.00 36.65           C  
-ANISOU 2284  C   GLY A 972     4699   4384   4843      6    -33     85       C  
-ATOM   2285  O   GLY A 972     -46.941  22.060 -19.189  1.00 37.76           O  
-ANISOU 2285  O   GLY A 972     4823   4545   4978     -4    -19     59       O  
-ATOM   2286  N   THR A 973     -47.152  23.564 -20.865  1.00 36.00           N  
-ANISOU 2286  N   THR A 973     4636   4288   4753     -1    -21    129       N  
-ATOM   2287  CA  THR A 973     -45.781  23.376 -21.316  1.00 37.56           C  
-ANISOU 2287  CA  THR A 973     4833   4494   4944    -25     14    148       C  
-ATOM   2288  C   THR A 973     -44.808  23.979 -20.300  1.00 35.18           C  
-ANISOU 2288  C   THR A 973     4507   4163   4696    -45     24    132       C  
-ATOM   2289  O   THR A 973     -45.120  24.909 -19.557  1.00 34.45           O  
-ANISOU 2289  O   THR A 973     4407   4034   4648    -42      6    122       O  
-ATOM   2290  CB  THR A 973     -45.522  24.035 -22.691  1.00 42.74           C  
-ANISOU 2290  CB  THR A 973     5516   5142   5582    -29     29    205       C  
-ATOM   2291  OG1 THR A 973     -46.025  25.373 -22.659  1.00 45.34           O  
-ANISOU 2291  OG1 THR A 973     5855   5424   5948    -24     10    227       O  
-ATOM   2292  CG2 THR A 973     -46.246  23.289 -23.830  1.00 42.69           C  
-ANISOU 2292  CG2 THR A 973     5534   5173   5513     -8     22    219       C  
-ATOM   2293  N   GLY A 974     -43.622  23.396 -20.248  1.00 37.73           N  
-ANISOU 2293  N   GLY A 974     4817   4504   5016    -64     52    125       N  
-ATOM   2294  CA  GLY A 974     -42.603  23.788 -19.282  1.00 39.92           C  
-ANISOU 2294  CA  GLY A 974     5067   4758   5341    -83     60    104       C  
-ATOM   2295  C   GLY A 974     -42.075  25.196 -19.440  1.00 43.72           C  
-ANISOU 2295  C   GLY A 974     5548   5192   5873   -101     67    133       C  
-ATOM   2296  O   GLY A 974     -41.606  25.562 -20.519  1.00 52.95           O  
-ANISOU 2296  O   GLY A 974     6730   6355   7033   -114     91    179       O  
-ATOM   2297  N   ILE A 975     -42.117  25.958 -18.350  1.00 41.81           N  
-ANISOU 2297  N   ILE A 975     5290   4914   5683   -101     47    106       N  
-ATOM   2298  CA  ILE A 975     -41.511  27.263 -18.267  1.00 41.88           C  
-ANISOU 2298  CA  ILE A 975     5290   4870   5751   -120     49    124       C  
-ATOM   2299  C   ILE A 975     -40.613  27.313 -17.036  1.00 41.33           C  
-ANISOU 2299  C   ILE A 975     5187   4790   5727   -132     46     78       C  
-ATOM   2300  O   ILE A 975     -40.591  26.394 -16.216  1.00 34.82           O  
-ANISOU 2300  O   ILE A 975     4349   3996   4883   -122     39     35       O  
-ATOM   2301  CB  ILE A 975     -42.563  28.386 -18.145  1.00 43.91           C  
-ANISOU 2301  CB  ILE A 975     5562   5086   6037   -103     18    132       C  
-ATOM   2302  CG1 ILE A 975     -43.285  28.301 -16.796  1.00 44.51           C  
-ANISOU 2302  CG1 ILE A 975     5622   5162   6126    -81    -14     75       C  
-ATOM   2303  CG2 ILE A 975     -43.546  28.304 -19.299  1.00 46.07           C  
-ANISOU 2303  CG2 ILE A 975     5868   5373   6264    -86     14    173       C  
-ATOM   2304  CD1 ILE A 975     -44.199  29.467 -16.508  1.00 44.72           C  
-ANISOU 2304  CD1 ILE A 975     5656   5144   6190    -64    -46     74       C  
-ATOM   2305  N   SER A 976     -39.880  28.416 -16.917  1.00 41.54           N  
-ANISOU 2305  N   SER A 976     5200   4768   5813   -153     50     88       N  
-ATOM   2306  CA  SER A 976     -38.940  28.603 -15.837  1.00 41.25           C  
-ANISOU 2306  CA  SER A 976     5131   4717   5827   -166     45     46       C  
-ATOM   2307  C   SER A 976     -39.717  28.817 -14.563  1.00 40.74           C  
-ANISOU 2307  C   SER A 976     5060   4642   5777   -141      6     -5       C  
-ATOM   2308  O   SER A 976     -40.700  29.552 -14.557  1.00 40.54           O  
-ANISOU 2308  O   SER A 976     5050   4591   5763   -125    -17      1       O  
-ATOM   2309  CB  SER A 976     -38.067  29.830 -16.106  1.00 44.58           C  
-ANISOU 2309  CB  SER A 976     5539   5083   6316   -196     56     72       C  
-ATOM   2310  OG  SER A 976     -37.087  29.936 -15.105  1.00 42.80           O  
-ANISOU 2310  OG  SER A 976     5278   4845   6139   -209     50     27       O  
-ATOM   2311  N   SER A 977     -39.296  28.140 -13.497  1.00 38.60           N  
-ANISOU 2311  N   SER A 977     4769   4395   5504   -135     -3    -56       N  
-ATOM   2312  CA  SER A 977     -39.948  28.268 -12.211  1.00 38.31           C  
-ANISOU 2312  CA  SER A 977     4725   4355   5475   -109    -36   -106       C  
-ATOM   2313  C   SER A 977     -39.390  29.451 -11.450  1.00 39.51           C  
-ANISOU 2313  C   SER A 977     4856   4457   5699   -117    -56   -133       C  
-ATOM   2314  O   SER A 977     -39.992  29.888 -10.479  1.00 37.86           O  
-ANISOU 2314  O   SER A 977     4644   4236   5506    -95    -86   -172       O  
-ATOM   2315  CB  SER A 977     -39.724  27.016 -11.367  1.00 36.57           C  
-ANISOU 2315  CB  SER A 977     4494   4183   5217    -97    -38   -147       C  
-ATOM   2316  OG  SER A 977     -38.330  26.817 -11.173  1.00 33.92           O  
-ANISOU 2316  OG  SER A 977     4135   3849   4906   -118    -25   -160       O  
-ATOM   2317  N   GLY A 978     -38.236  29.958 -11.882  1.00 41.40           N  
-ANISOU 2317  N   GLY A 978     5079   4668   5983   -149    -39   -114       N  
-ATOM   2318  CA  GLY A 978     -37.579  31.048 -11.181  1.00 44.86           C  
-ANISOU 2318  CA  GLY A 978     5492   5054   6497   -160    -58   -142       C  
-ATOM   2319  C   GLY A 978     -36.749  30.575 -10.010  1.00 45.37           C  
-ANISOU 2319  C   GLY A 978     5528   5137   6573   -156    -71   -202       C  
-ATOM   2320  O   GLY A 978     -36.203  31.378  -9.284  1.00 51.19           O  
-ANISOU 2320  O   GLY A 978     6242   5837   7370   -162    -93   -236       O  
-ATOM   2321  N   VAL A 979     -36.646  29.267  -9.829  1.00 46.51           N  
-ANISOU 2321  N   VAL A 979     5674   5338   6660   -146    -61   -214       N  
-ATOM   2322  CA  VAL A 979     -35.823  28.704  -8.786  1.00 44.70           C  
-ANISOU 2322  CA  VAL A 979     5421   5130   6434   -141    -73   -266       C  
-ATOM   2323  C   VAL A 979     -34.510  28.321  -9.448  1.00 47.31           C  
-ANISOU 2323  C   VAL A 979     5730   5467   6779   -172    -42   -247       C  
-ATOM   2324  O   VAL A 979     -34.507  27.406 -10.263  1.00 49.46           O  
-ANISOU 2324  O   VAL A 979     6014   5775   7002   -176    -14   -215       O  
-ATOM   2325  CB  VAL A 979     -36.502  27.461  -8.172  1.00 44.94           C  
-ANISOU 2325  CB  VAL A 979     5466   5215   6393   -110    -80   -289       C  
-ATOM   2326  CG1 VAL A 979     -35.568  26.723  -7.219  1.00 45.64           C  
-ANISOU 2326  CG1 VAL A 979     5533   5330   6477   -105    -90   -334       C  
-ATOM   2327  CG2 VAL A 979     -37.794  27.844  -7.444  1.00 42.39           C  
-ANISOU 2327  CG2 VAL A 979     5160   4890   6058    -79   -107   -311       C  
-ATOM   2328  N   ASN A 980     -33.404  28.980  -9.093  1.00 49.74           N  
-ANISOU 2328  N   ASN A 980     6004   5741   7153   -192    -49   -269       N  
-ATOM   2329  CA  ASN A 980     -32.068  28.653  -9.675  1.00 49.66           C  
-ANISOU 2329  CA  ASN A 980     5967   5738   7164   -223    -18   -255       C  
-ATOM   2330  C   ASN A 980     -31.227  27.736  -8.797  1.00 47.99           C  
-ANISOU 2330  C   ASN A 980     5730   5560   6942   -213    -30   -305       C  
-ATOM   2331  O   ASN A 980     -30.524  26.867  -9.330  1.00 47.53           O  
-ANISOU 2331  O   ASN A 980     5663   5535   6863   -223     -3   -292       O  
-ATOM   2332  CB  ASN A 980     -31.211  29.881 -10.092  1.00 53.49           C  
-ANISOU 2332  CB  ASN A 980     6425   6165   7735   -260     -8   -237       C  
-ATOM   2333  CG  ASN A 980     -29.865  29.467 -10.797  1.00 60.90           C  
-ANISOU 2333  CG  ASN A 980     7332   7117   8690   -293     32   -218       C  
-ATOM   2334  OD1 ASN A 980     -29.832  28.533 -11.632  1.00 65.87           O  
-ANISOU 2334  OD1 ASN A 980     7975   7790   9265   -295     66   -186       O  
-ATOM   2335  ND2 ASN A 980     -28.758  30.135 -10.434  1.00 53.82           N  
-ANISOU 2335  ND2 ASN A 980     6393   6185   7873   -318     26   -242       N  
-ATOM   2336  N   ASP A 981     -31.334  27.894  -7.479  1.00 43.88           N  
-ANISOU 2336  N   ASP A 981     5202   5036   6433   -188    -72   -362       N  
-ATOM   2337  CA  ASP A 981     -30.518  27.129  -6.531  1.00 40.46           C  
-ANISOU 2337  CA  ASP A 981     4747   4631   5993   -175    -91   -414       C  
-ATOM   2338  C   ASP A 981     -31.146  25.781  -6.129  1.00 36.01           C  
-ANISOU 2338  C   ASP A 981     4210   4124   5347   -143    -94   -422       C  
-ATOM   2339  O   ASP A 981     -31.481  25.550  -4.965  1.00 32.82           O  
-ANISOU 2339  O   ASP A 981     3812   3736   4922   -112   -127   -466       O  
-ATOM   2340  CB  ASP A 981     -30.257  27.988  -5.287  1.00 41.28           C  
-ANISOU 2340  CB  ASP A 981     4831   4705   6150   -163   -136   -473       C  
-ATOM   2341  CG  ASP A 981     -31.563  28.386  -4.541  1.00 44.30           C  
-ANISOU 2341  CG  ASP A 981     5242   5083   6508   -130   -165   -492       C  
-ATOM   2342  OD1 ASP A 981     -32.624  28.571  -5.178  1.00 41.20           O  
-ANISOU 2342  OD1 ASP A 981     4878   4687   6090   -128   -151   -453       O  
-ATOM   2343  OD2 ASP A 981     -31.527  28.487  -3.295  1.00 47.75           O  
-ANISOU 2343  OD2 ASP A 981     5671   5524   6947   -103   -204   -550       O  
-ATOM   2344  N   THR A 982     -31.249  24.869  -7.086  1.00 35.38           N  
-ANISOU 2344  N   THR A 982     4144   4076   5221   -149    -61   -382       N  
-ATOM   2345  CA  THR A 982     -31.860  23.565  -6.849  1.00 33.71           C  
-ANISOU 2345  CA  THR A 982     3958   3913   4937   -123    -61   -384       C  
-ATOM   2346  C   THR A 982     -31.081  22.439  -7.475  1.00 33.04           C  
-ANISOU 2346  C   THR A 982     3865   3861   4827   -132    -35   -371       C  
-ATOM   2347  O   THR A 982     -30.425  22.608  -8.504  1.00 35.46           O  
-ANISOU 2347  O   THR A 982     4157   4160   5156   -159     -4   -342       O  
-ATOM   2348  CB  THR A 982     -33.311  23.516  -7.372  1.00 35.41           C  
-ANISOU 2348  CB  THR A 982     4211   4136   5108   -113    -52   -348       C  
-ATOM   2349  OG1 THR A 982     -33.819  22.182  -7.283  1.00 36.98           O  
-ANISOU 2349  OG1 THR A 982     4430   4379   5241    -93    -48   -346       O  
-ATOM   2350  CG2 THR A 982     -33.373  23.950  -8.826  1.00 36.78           C  
-ANISOU 2350  CG2 THR A 982     4391   4293   5292   -140    -18   -293       C  
-ATOM   2351  N   SER A 983     -31.191  21.264  -6.864  1.00 31.64           N  
-ANISOU 2351  N   SER A 983     3697   3721   4602   -107    -47   -392       N  
-ATOM   2352  CA  SER A 983     -30.594  20.067  -7.391  1.00 32.63           C  
-ANISOU 2352  CA  SER A 983     3819   3879   4699   -109    -27   -383       C  
-ATOM   2353  C   SER A 983     -31.378  19.461  -8.569  1.00 30.73           C  
-ANISOU 2353  C   SER A 983     3607   3658   4411   -113      3   -336       C  
-ATOM   2354  O   SER A 983     -30.909  18.509  -9.157  1.00 32.05           O  
-ANISOU 2354  O   SER A 983     3772   3851   4555   -115     22   -327       O  
-ATOM   2355  CB  SER A 983     -30.494  19.001  -6.273  1.00 33.04           C  
-ANISOU 2355  CB  SER A 983     3876   3961   4716    -79    -54   -420       C  
-ATOM   2356  OG  SER A 983     -29.852  19.521  -5.129  1.00 34.72           O  
-ANISOU 2356  OG  SER A 983     4067   4160   4965    -69    -87   -467       O  
-ATOM   2357  N   LEU A 984     -32.558  19.987  -8.896  1.00 27.94           N  
-ANISOU 2357  N   LEU A 984     3279   3294   4044   -112      5   -310       N  
-ATOM   2358  CA  LEU A 984     -33.471  19.287  -9.774  1.00 27.23           C  
-ANISOU 2358  CA  LEU A 984     3218   3226   3902   -107     23   -275       C  
-ATOM   2359  C   LEU A 984     -33.787  20.091 -11.016  1.00 26.65           C  
-ANISOU 2359  C   LEU A 984     3153   3134   3839   -127     48   -230       C  
-ATOM   2360  O   LEU A 984     -34.107  21.282 -10.937  1.00 27.84           O  
-ANISOU 2360  O   LEU A 984     3305   3251   4024   -134     40   -223       O  
-ATOM   2361  CB  LEU A 984     -34.786  18.984  -9.021  1.00 27.76           C  
-ANISOU 2361  CB  LEU A 984     3311   3303   3933    -81      1   -285       C  
-ATOM   2362  CG  LEU A 984     -34.793  17.975  -7.870  1.00 27.27           C  
-ANISOU 2362  CG  LEU A 984     3252   3267   3843    -57    -19   -318       C  
-ATOM   2363  CD1 LEU A 984     -36.117  18.008  -7.143  1.00 28.38           C  
-ANISOU 2363  CD1 LEU A 984     3414   3411   3957    -36    -36   -323       C  
-ATOM   2364  CD2 LEU A 984     -34.524  16.573  -8.355  1.00 28.62           C  
-ANISOU 2364  CD2 LEU A 984     3429   3469   3977    -54     -6   -310       C  
-ATOM   2365  N   LEU A 985     -33.773  19.433 -12.154  1.00 25.40           N  
-ANISOU 2365  N   LEU A 985     3005   2997   3647   -133     75   -200       N  
-ATOM   2366  CA  LEU A 985     -34.258  20.056 -13.389  1.00 28.17           C  
-ANISOU 2366  CA  LEU A 985     3373   3337   3993   -147     97   -153       C  
-ATOM   2367  C   LEU A 985     -35.788  20.218 -13.371  1.00 26.10           C  
-ANISOU 2367  C   LEU A 985     3141   3072   3703   -129     80   -141       C  
-ATOM   2368  O   LEU A 985     -36.319  21.222 -13.837  1.00 27.12           O  
-ANISOU 2368  O   LEU A 985     3281   3175   3847   -135     81   -114       O  
-ATOM   2369  CB  LEU A 985     -33.830  19.227 -14.625  1.00 29.44           C  
-ANISOU 2369  CB  LEU A 985     3538   3529   4119   -154    130   -128       C  
-ATOM   2370  CG  LEU A 985     -32.309  19.130 -14.919  1.00 32.40           C  
-ANISOU 2370  CG  LEU A 985     3879   3909   4521   -173    155   -133       C  
-ATOM   2371  CD1 LEU A 985     -32.006  18.210 -16.111  1.00 30.92           C  
-ANISOU 2371  CD1 LEU A 985     3699   3759   4291   -174    187   -113       C  
-ATOM   2372  CD2 LEU A 985     -31.710  20.516 -15.172  1.00 33.83           C  
-ANISOU 2372  CD2 LEU A 985     4043   4053   4760   -201    170   -113       C  
-ATOM   2373  N   TYR A 986     -36.489  19.226 -12.841  1.00 24.65           N  
-ANISOU 2373  N   TYR A 986     2970   2914   3481   -108     65   -160       N  
-ATOM   2374  CA  TYR A 986     -37.940  19.213 -12.854  1.00 23.46           C  
-ANISOU 2374  CA  TYR A 986     2844   2767   3303    -91     51   -150       C  
-ATOM   2375  C   TYR A 986     -38.485  18.905 -11.466  1.00 22.29           C  
-ANISOU 2375  C   TYR A 986     2695   2624   3150    -71     25   -187       C  
-ATOM   2376  O   TYR A 986     -37.808  18.263 -10.643  1.00 23.07           O  
-ANISOU 2376  O   TYR A 986     2782   2736   3249    -66     18   -216       O  
-ATOM   2377  CB  TYR A 986     -38.434  18.196 -13.912  1.00 23.53           C  
-ANISOU 2377  CB  TYR A 986     2872   2806   3262    -86     65   -128       C  
-ATOM   2378  CG  TYR A 986     -37.705  18.353 -15.231  1.00 26.02           C  
-ANISOU 2378  CG  TYR A 986     3187   3124   3575   -104     94    -95       C  
-ATOM   2379  CD1 TYR A 986     -37.950  19.439 -16.062  1.00 27.35           C  
-ANISOU 2379  CD1 TYR A 986     3366   3271   3756   -114    104    -59       C  
-ATOM   2380  CD2 TYR A 986     -36.695  17.461 -15.608  1.00 29.41           C  
-ANISOU 2380  CD2 TYR A 986     3605   3578   3991   -110    114   -102       C  
-ATOM   2381  CE1 TYR A 986     -37.239  19.600 -17.254  1.00 28.51           C  
-ANISOU 2381  CE1 TYR A 986     3514   3422   3898   -131    135    -26       C  
-ATOM   2382  CE2 TYR A 986     -35.977  17.607 -16.790  1.00 28.49           C  
-ANISOU 2382  CE2 TYR A 986     3486   3469   3870   -125    145    -73       C  
-ATOM   2383  CZ  TYR A 986     -36.248  18.692 -17.603  1.00 29.88           C  
-ANISOU 2383  CZ  TYR A 986     3673   3624   4055   -136    157    -34       C  
-ATOM   2384  OH  TYR A 986     -35.529  18.840 -18.781  1.00 31.23           O  
-ANISOU 2384  OH  TYR A 986     3843   3804   4218   -151    192     -2       O  
-ATOM   2385  N   ASN A 987     -39.731  19.303 -11.225  1.00 20.19           N  
-ANISOU 2385  N   ASN A 987     2442   2351   2877    -57     10   -184       N  
-ATOM   2386  CA  ASN A 987     -40.398  18.989  -9.988  1.00 20.12           C  
-ANISOU 2386  CA  ASN A 987     2435   2352   2857    -37     -9   -214       C  
-ATOM   2387  C   ASN A 987     -40.514  17.487  -9.750  1.00 20.08           C  
-ANISOU 2387  C   ASN A 987     2436   2382   2811    -28     -7   -222       C  
-ATOM   2388  O   ASN A 987     -40.475  16.678 -10.681  1.00 19.19           O  
-ANISOU 2388  O   ASN A 987     2331   2285   2674    -33      7   -203       O  
-ATOM   2389  CB  ASN A 987     -41.810  19.552  -9.950  1.00 20.91           C  
-ANISOU 2389  CB  ASN A 987     2548   2444   2953    -24    -21   -208       C  
-ATOM   2390  CG  ASN A 987     -41.847  21.054 -10.088  1.00 21.40           C  
-ANISOU 2390  CG  ASN A 987     2606   2467   3057    -29    -28   -201       C  
-ATOM   2391  OD1 ASN A 987     -40.997  21.736  -9.582  1.00 22.91           O  
-ANISOU 2391  OD1 ASN A 987     2782   2637   3285    -36    -34   -219       O  
-ATOM   2392  ND2 ASN A 987     -42.820  21.557 -10.800  1.00 22.07           N  
-ANISOU 2392  ND2 ASN A 987     2704   2541   3140    -25    -30   -177       N  
-ATOM   2393  N   GLU A 988     -40.636  17.131  -8.483  1.00 19.63           N  
-ANISOU 2393  N   GLU A 988     2376   2336   2748    -12    -21   -251       N  
-ATOM   2394  CA  GLU A 988     -41.167  15.838  -8.114  1.00 20.19           C  
-ANISOU 2394  CA  GLU A 988     2457   2434   2781     -1    -21   -254       C  
-ATOM   2395  C   GLU A 988     -41.943  15.981  -6.817  1.00 19.02           C  
-ANISOU 2395  C   GLU A 988     2311   2292   2625     19    -35   -276       C  
-ATOM   2396  O   GLU A 988     -41.809  16.968  -6.116  1.00 18.30           O  
-ANISOU 2396  O   GLU A 988     2212   2185   2557     25    -48   -296       O  
-ATOM   2397  CB  GLU A 988     -40.104  14.743  -8.010  1.00 20.39           C  
-ANISOU 2397  CB  GLU A 988     2478   2476   2794     -3    -17   -263       C  
-ATOM   2398  CG  GLU A 988     -38.880  15.091  -7.202  1.00 20.65           C  
-ANISOU 2398  CG  GLU A 988     2493   2500   2851     -2    -27   -290       C  
-ATOM   2399  CD  GLU A 988     -37.776  14.073  -7.411  1.00 20.31           C  
-ANISOU 2399  CD  GLU A 988     2443   2471   2801     -5    -22   -295       C  
-ATOM   2400  OE1 GLU A 988     -37.541  13.232  -6.522  1.00 19.57           O  
-ANISOU 2400  OE1 GLU A 988     2352   2392   2691      9    -33   -313       O  
-ATOM   2401  OE2 GLU A 988     -37.154  14.078  -8.495  1.00 21.17           O  
-ANISOU 2401  OE2 GLU A 988     2545   2578   2920    -21     -5   -280       O  
-ATOM   2402  N   TYR A 989     -42.804  15.002  -6.573  1.00 18.53           N  
-ANISOU 2402  N   TYR A 989     2259   2251   2532     28    -33   -271       N  
-ATOM   2403  CA  TYR A 989     -43.744  15.065  -5.500  1.00 18.11           C  
-ANISOU 2403  CA  TYR A 989     2208   2207   2466     45    -39   -285       C  
-ATOM   2404  C   TYR A 989     -43.714  13.742  -4.790  1.00 17.34           C  
-ANISOU 2404  C   TYR A 989     2118   2133   2337     53    -37   -289       C  
-ATOM   2405  O   TYR A 989     -43.777  12.697  -5.419  1.00 18.51           O  
-ANISOU 2405  O   TYR A 989     2272   2291   2471     45    -28   -272       O  
-ATOM   2406  CB  TYR A 989     -45.147  15.334  -6.048  1.00 17.57           C  
-ANISOU 2406  CB  TYR A 989     2144   2137   2394     46    -35   -269       C  
-ATOM   2407  CG  TYR A 989     -45.272  16.591  -6.845  1.00 17.12           C  
-ANISOU 2407  CG  TYR A 989     2084   2055   2365     40    -39   -260       C  
-ATOM   2408  CD1 TYR A 989     -45.040  16.584  -8.188  1.00 17.25           C  
-ANISOU 2408  CD1 TYR A 989     2106   2064   2386     25    -32   -234       C  
-ATOM   2409  CD2 TYR A 989     -45.700  17.767  -6.262  1.00 18.00           C  
-ANISOU 2409  CD2 TYR A 989     2189   2151   2498     51    -51   -276       C  
-ATOM   2410  CE1 TYR A 989     -45.202  17.705  -8.945  1.00 17.98           C  
-ANISOU 2410  CE1 TYR A 989     2199   2132   2502     20    -34   -220       C  
-ATOM   2411  CE2 TYR A 989     -45.849  18.910  -7.000  1.00 18.80           C  
-ANISOU 2411  CE2 TYR A 989     2290   2225   2629     46    -56   -265       C  
-ATOM   2412  CZ  TYR A 989     -45.589  18.873  -8.350  1.00 18.31           C  
-ANISOU 2412  CZ  TYR A 989     2235   2154   2569     30    -47   -234       C  
-ATOM   2413  OH  TYR A 989     -45.724  19.968  -9.122  1.00 18.01           O  
-ANISOU 2413  OH  TYR A 989     2199   2088   2557     25    -51   -218       O  
-ATOM   2414  N   ILE A 990     -43.650  13.785  -3.483  1.00 17.44           N  
-ANISOU 2414  N   ILE A 990     2131   2156   2341     69    -45   -311       N  
-ATOM   2415  CA  ILE A 990     -43.546  12.584  -2.680  1.00 17.18           C  
-ANISOU 2415  CA  ILE A 990     2107   2144   2277     79    -44   -312       C  
-ATOM   2416  C   ILE A 990     -44.578  12.596  -1.560  1.00 18.13           C  
-ANISOU 2416  C   ILE A 990     2232   2282   2375     97    -41   -319       C  
-ATOM   2417  O   ILE A 990     -44.741  13.593  -0.848  1.00 16.76           O  
-ANISOU 2417  O   ILE A 990     2053   2107   2208    111    -50   -341       O  
-ATOM   2418  CB  ILE A 990     -42.134  12.417  -2.095  1.00 18.02           C  
-ANISOU 2418  CB  ILE A 990     2210   2250   2386     85    -57   -332       C  
-ATOM   2419  CG1 ILE A 990     -41.071  12.467  -3.183  1.00 17.72           C  
-ANISOU 2419  CG1 ILE A 990     2163   2198   2373     67    -56   -327       C  
-ATOM   2420  CG2 ILE A 990     -42.001  11.084  -1.373  1.00 18.33           C  
-ANISOU 2420  CG2 ILE A 990     2262   2309   2393     96    -58   -328       C  
-ATOM   2421  CD1 ILE A 990     -40.580  13.856  -3.510  1.00 17.95           C  
-ANISOU 2421  CD1 ILE A 990     2177   2204   2439     59    -62   -339       C  
-ATOM   2422  N   VAL A 991     -45.311  11.485  -1.437  1.00 18.87           N  
-ANISOU 2422  N   VAL A 991     2335   2392   2444     96    -29   -300       N  
-ATOM   2423  CA  VAL A 991     -46.142  11.245  -0.269  1.00 20.41           C  
-ANISOU 2423  CA  VAL A 991     2535   2608   2613    113    -21   -303       C  
-ATOM   2424  C   VAL A 991     -45.627  10.046   0.541  1.00 20.96           C  
-ANISOU 2424  C   VAL A 991     2619   2693   2653    121    -21   -296       C  
-ATOM   2425  O   VAL A 991     -44.993   9.156  -0.007  1.00 20.53           O  
-ANISOU 2425  O   VAL A 991     2570   2632   2601    110    -23   -284       O  
-ATOM   2426  CB  VAL A 991     -47.627  11.083  -0.629  1.00 20.46           C  
-ANISOU 2426  CB  VAL A 991     2536   2620   2617    106     -5   -285       C  
-ATOM   2427  CG1 VAL A 991     -48.161  12.370  -1.238  1.00 21.08           C  
-ANISOU 2427  CG1 VAL A 991     2603   2685   2723    105     -9   -294       C  
-ATOM   2428  CG2 VAL A 991     -47.861   9.899  -1.553  1.00 20.29           C  
-ANISOU 2428  CG2 VAL A 991     2518   2594   2595     88      4   -258       C  
-ATOM   2429  N   TYR A 992     -45.935  10.041   1.838  1.00 21.86           N  
-ANISOU 2429  N   TYR A 992     2740   2827   2739    141    -19   -305       N  
-ATOM   2430  CA  TYR A 992     -45.379   9.085   2.798  1.00 22.24           C  
-ANISOU 2430  CA  TYR A 992     2805   2890   2755    155    -22   -301       C  
-ATOM   2431  C   TYR A 992     -46.424   8.185   3.420  1.00 22.51           C  
-ANISOU 2431  C   TYR A 992     2850   2944   2760    157      1   -275       C  
-ATOM   2432  O   TYR A 992     -46.144   7.481   4.339  1.00 22.61           O  
-ANISOU 2432  O   TYR A 992     2879   2971   2742    171      1   -268       O  
-ATOM   2433  CB  TYR A 992     -44.583   9.845   3.889  1.00 21.55           C  
-ANISOU 2433  CB  TYR A 992     2720   2812   2655    181    -42   -336       C  
-ATOM   2434  CG  TYR A 992     -43.473  10.627   3.219  1.00 19.59           C  
-ANISOU 2434  CG  TYR A 992     2458   2541   2445    173    -63   -358       C  
-ATOM   2435  CD1 TYR A 992     -43.716  11.900   2.732  1.00 19.10           C  
-ANISOU 2435  CD1 TYR A 992     2380   2464   2414    167    -67   -374       C  
-ATOM   2436  CD2 TYR A 992     -42.228  10.047   2.958  1.00 18.06           C  
-ANISOU 2436  CD2 TYR A 992     2265   2337   2258    170    -78   -360       C  
-ATOM   2437  CE1 TYR A 992     -42.732  12.618   2.055  1.00 18.30           C  
-ANISOU 2437  CE1 TYR A 992     2266   2339   2351    157    -82   -390       C  
-ATOM   2438  CE2 TYR A 992     -41.237  10.753   2.298  1.00 17.43           C  
-ANISOU 2438  CE2 TYR A 992     2170   2238   2216    160    -92   -379       C  
-ATOM   2439  CZ  TYR A 992     -41.501  12.033   1.836  1.00 18.31           C  
-ANISOU 2439  CZ  TYR A 992     2266   2334   2358    152    -93   -391       C  
-ATOM   2440  OH  TYR A 992     -40.525  12.753   1.167  1.00 19.09           O  
-ANISOU 2440  OH  TYR A 992     2348   2410   2497    139   -104   -405       O  
-ATOM   2441  N   ASP A 993     -47.620   8.190   2.853  1.00 23.82           N  
-ANISOU 2441  N   ASP A 993     3005   3108   2936    143     20   -260       N  
-ATOM   2442  CA  ASP A 993     -48.710   7.350   3.291  1.00 23.87           C  
-ANISOU 2442  CA  ASP A 993     3015   3131   2924    139     45   -233       C  
-ATOM   2443  C   ASP A 993     -49.388   6.854   2.027  1.00 22.16           C  
-ANISOU 2443  C   ASP A 993     2787   2897   2736    113     53   -213       C  
-ATOM   2444  O   ASP A 993     -49.845   7.647   1.231  1.00 21.28           O  
-ANISOU 2444  O   ASP A 993     2661   2777   2650    105     51   -222       O  
-ATOM   2445  CB  ASP A 993     -49.680   8.191   4.149  1.00 25.47           C  
-ANISOU 2445  CB  ASP A 993     3210   3357   3112    156     60   -247       C  
-ATOM   2446  CG  ASP A 993     -50.879   7.381   4.703  1.00 27.80           C  
-ANISOU 2446  CG  ASP A 993     3504   3672   3387    152     92   -218       C  
-ATOM   2447  OD1 ASP A 993     -51.234   6.293   4.184  1.00 26.84           O  
-ANISOU 2447  OD1 ASP A 993     3383   3540   3275    130    103   -188       O  
-ATOM   2448  OD2 ASP A 993     -51.472   7.869   5.681  1.00 32.04           O  
-ANISOU 2448  OD2 ASP A 993     4039   4236   3900    170    107   -229       O  
-ATOM   2449  N   ILE A 994     -49.462   5.547   1.861  1.00 22.25           N  
-ANISOU 2449  N   ILE A 994     2808   2903   2745    100     61   -186       N  
-ATOM   2450  CA  ILE A 994     -50.011   4.946   0.635  1.00 22.49           C  
-ANISOU 2450  CA  ILE A 994     2827   2915   2802     76     64   -170       C  
-ATOM   2451  C   ILE A 994     -51.465   5.330   0.372  1.00 22.37           C  
-ANISOU 2451  C   ILE A 994     2792   2907   2802     67     81   -167       C  
-ATOM   2452  O   ILE A 994     -51.952   5.219  -0.757  1.00 23.50           O  
-ANISOU 2452  O   ILE A 994     2923   3036   2971     51     77   -163       O  
-ATOM   2453  CB  ILE A 994     -49.878   3.393   0.649  1.00 22.95           C  
-ANISOU 2453  CB  ILE A 994     2899   2964   2857     65     68   -144       C  
-ATOM   2454  CG1 ILE A 994     -50.680   2.787   1.793  1.00 24.20           C  
-ANISOU 2454  CG1 ILE A 994     3062   3138   2993     68     93   -121       C  
-ATOM   2455  CG2 ILE A 994     -48.412   2.990   0.778  1.00 21.98           C  
-ANISOU 2455  CG2 ILE A 994     2793   2832   2725     75     48   -150       C  
-ATOM   2456  CD1 ILE A 994     -50.592   1.272   1.887  1.00 25.67           C  
-ANISOU 2456  CD1 ILE A 994     3263   3311   3180     57     97    -90       C  
-ATOM   2457  N   ALA A 995     -52.164   5.756   1.411  1.00 22.05           N  
-ANISOU 2457  N   ALA A 995     2747   2888   2743     80     98   -170       N  
-ATOM   2458  CA  ALA A 995     -53.558   6.130   1.290  1.00 22.10           C  
-ANISOU 2458  CA  ALA A 995     2730   2903   2763     75    116   -169       C  
-ATOM   2459  C   ALA A 995     -53.776   7.485   0.638  1.00 22.00           C  
-ANISOU 2459  C   ALA A 995     2702   2885   2771     81    102   -194       C  
-ATOM   2460  O   ALA A 995     -54.907   7.825   0.322  1.00 21.35           O  
-ANISOU 2460  O   ALA A 995     2599   2806   2706     78    110   -196       O  
-ATOM   2461  CB  ALA A 995     -54.226   6.089   2.672  1.00 22.81           C  
-ANISOU 2461  CB  ALA A 995     2820   3024   2824     88    143   -163       C  
-ATOM   2462  N   GLN A 996     -52.716   8.279   0.498  1.00 21.93           N  
-ANISOU 2462  N   GLN A 996     2703   2868   2763     92     80   -214       N  
-ATOM   2463  CA  GLN A 996     -52.813   9.587  -0.149  1.00 21.97           C  
-ANISOU 2463  CA  GLN A 996     2697   2861   2791     96     66   -235       C  
-ATOM   2464  C   GLN A 996     -52.816   9.520  -1.701  1.00 22.27           C  
-ANISOU 2464  C   GLN A 996     2730   2876   2856     78     53   -226       C  
-ATOM   2465  O   GLN A 996     -52.838  10.552  -2.362  1.00 21.09           O  
-ANISOU 2465  O   GLN A 996     2574   2714   2725     81     40   -237       O  
-ATOM   2466  CB  GLN A 996     -51.649  10.472   0.280  1.00 23.16           C  
-ANISOU 2466  CB  GLN A 996     2856   3007   2935    112     48   -258       C  
-ATOM   2467  CG  GLN A 996     -51.889  11.196   1.582  1.00 24.20           C  
-ANISOU 2467  CG  GLN A 996     2986   3159   3048    136     53   -281       C  
-ATOM   2468  CD  GLN A 996     -50.676  11.921   2.092  1.00 22.79           C  
-ANISOU 2468  CD  GLN A 996     2817   2975   2865    152     32   -307       C  
-ATOM   2469  OE1 GLN A 996     -49.892  11.361   2.821  1.00 22.65           O  
-ANISOU 2469  OE1 GLN A 996     2815   2968   2824    160     30   -307       O  
-ATOM   2470  NE2 GLN A 996     -50.486  13.154   1.635  1.00 22.64           N  
-ANISOU 2470  NE2 GLN A 996     2790   2939   2875    155     16   -327       N  
-ATOM   2471  N   VAL A 997     -52.901   8.324  -2.272  1.00 22.78           N  
-ANISOU 2471  N   VAL A 997     2798   2936   2923     61     56   -206       N  
-ATOM   2472  CA  VAL A 997     -52.919   8.142  -3.726  1.00 22.66           C  
-ANISOU 2472  CA  VAL A 997     2780   2903   2927     47     44   -199       C  
-ATOM   2473  C   VAL A 997     -54.186   7.417  -4.177  1.00 22.83           C  
-ANISOU 2473  C   VAL A 997     2786   2925   2961     35     52   -187       C  
-ATOM   2474  O   VAL A 997     -54.534   6.376  -3.617  1.00 22.40           O  
-ANISOU 2474  O   VAL A 997     2731   2878   2901     27     66   -173       O  
-ATOM   2475  CB  VAL A 997     -51.754   7.258  -4.162  1.00 22.81           C  
-ANISOU 2475  CB  VAL A 997     2815   2911   2940     38     36   -191       C  
-ATOM   2476  CG1 VAL A 997     -51.787   7.066  -5.652  1.00 23.22           C  
-ANISOU 2476  CG1 VAL A 997     2865   2950   3007     27     24   -187       C  
-ATOM   2477  CG2 VAL A 997     -50.446   7.896  -3.744  1.00 24.26           C  
-ANISOU 2477  CG2 VAL A 997     3010   3093   3116     49     27   -205       C  
-ATOM   2478  N   ASN A 998     -54.863   7.962  -5.199  1.00 22.46           N  
-ANISOU 2478  N   ASN A 998     2728   2872   2934     32     41   -191       N  
-ATOM   2479  CA  ASN A 998     -55.997   7.285  -5.832  1.00 22.49           C  
-ANISOU 2479  CA  ASN A 998     2716   2875   2956     21     42   -184       C  
-ATOM   2480  C   ASN A 998     -55.673   7.186  -7.321  1.00 21.96           C  
-ANISOU 2480  C   ASN A 998     2655   2792   2896     14     20   -183       C  
-ATOM   2481  O   ASN A 998     -55.666   8.187  -8.039  1.00 23.34           O  
-ANISOU 2481  O   ASN A 998     2830   2961   3076     22      6   -189       O  
-ATOM   2482  CB  ASN A 998     -57.292   8.027  -5.523  1.00 23.81           C  
-ANISOU 2482  CB  ASN A 998     2859   3052   3136     29     48   -193       C  
-ATOM   2483  CG  ASN A 998     -58.566   7.275  -5.944  1.00 26.87           C  
-ANISOU 2483  CG  ASN A 998     3223   3441   3545     16     52   -187       C  
-ATOM   2484  OD1 ASN A 998     -58.569   6.067  -6.118  1.00 32.89           O  
-ANISOU 2484  OD1 ASN A 998     3987   4199   4313      0     55   -175       O  
-ATOM   2485  ND2 ASN A 998     -59.659   7.981  -6.041  1.00 27.13           N  
-ANISOU 2485  ND2 ASN A 998     3232   3480   3595     24     50   -198       N  
-ATOM   2486  N   LEU A 999     -55.357   5.968  -7.767  1.00 20.85           N  
-ANISOU 2486  N   LEU A 999     2522   2646   2756      2     17   -175       N  
-ATOM   2487  CA  LEU A 999     -54.993   5.733  -9.135  1.00 21.96           C  
-ANISOU 2487  CA  LEU A 999     2670   2776   2899     -2     -1   -176       C  
-ATOM   2488  C   LEU A 999     -56.196   5.956 -10.035  1.00 22.21           C  
-ANISOU 2488  C   LEU A 999     2685   2807   2947     -2    -15   -181       C  
-ATOM   2489  O   LEU A 999     -57.280   5.502  -9.717  1.00 23.21           O  
-ANISOU 2489  O   LEU A 999     2792   2937   3091     -8     -9   -181       O  
-ATOM   2490  CB  LEU A 999     -54.433   4.331  -9.305  1.00 21.59           C  
-ANISOU 2490  CB  LEU A 999     2633   2723   2849    -13     -2   -171       C  
-ATOM   2491  CG  LEU A 999     -53.128   4.082  -8.559  1.00 21.33           C  
-ANISOU 2491  CG  LEU A 999     2618   2689   2799    -10      5   -168       C  
-ATOM   2492  CD1 LEU A 999     -52.649   2.675  -8.858  1.00 21.35           C  
-ANISOU 2492  CD1 LEU A 999     2628   2681   2803    -19      0   -164       C  
-ATOM   2493  CD2 LEU A 999     -52.041   5.080  -8.922  1.00 21.30           C  
-ANISOU 2493  CD2 LEU A 999     2625   2685   2784     -1     -1   -174       C  
-ATOM   2494  N   LYS A1000     -56.012   6.726 -11.112  1.00 23.88           N  
-ANISOU 2494  N   LYS A1000     2904   3015   3156      6    -32   -184       N  
-ATOM   2495  CA  LYS A1000     -57.132   7.086 -12.018  1.00 25.61           C  
-ANISOU 2495  CA  LYS A1000     3109   3233   3388     11    -50   -189       C  
-ATOM   2496  C   LYS A1000     -57.005   6.517 -13.422  1.00 22.66           C  
-ANISOU 2496  C   LYS A1000     2745   2857   3009     10    -71   -191       C  
-ATOM   2497  O   LYS A1000     -57.971   6.004 -13.966  1.00 21.04           O  
-ANISOU 2497  O   LYS A1000     2524   2651   2817      8    -85   -198       O  
-ATOM   2498  CB  LYS A1000     -57.271   8.603 -12.183  1.00 27.24           C  
-ANISOU 2498  CB  LYS A1000     3317   3439   3595     26    -57   -190       C  
-ATOM   2499  CG  LYS A1000     -57.390   9.398 -10.910  1.00 31.73           C  
-ANISOU 2499  CG  LYS A1000     3877   4010   4168     33    -41   -194       C  
-ATOM   2500  CD  LYS A1000     -58.363   8.835  -9.889  1.00 35.13           C  
-ANISOU 2500  CD  LYS A1000     4284   4452   4611     28    -25   -199       C  
-ATOM   2501  CE  LYS A1000     -59.797   9.124 -10.243  1.00 40.54           C  
-ANISOU 2501  CE  LYS A1000     4943   5141   5319     34    -35   -207       C  
-ATOM   2502  NZ  LYS A1000     -60.664   8.817  -9.047  1.00 46.05           N  
-ANISOU 2502  NZ  LYS A1000     5616   5852   6028     31    -12   -211       N  
-ATOM   2503  N   TYR A1001     -55.829   6.669 -14.027  1.00 21.02           N  
-ANISOU 2503  N   TYR A1001     2559   2647   2779     12    -73   -186       N  
-ATOM   2504  CA  TYR A1001     -55.611   6.179 -15.398  1.00 20.61           C  
-ANISOU 2504  CA  TYR A1001     2518   2596   2715     14    -91   -189       C  
-ATOM   2505  C   TYR A1001     -54.346   5.341 -15.529  1.00 20.15           C  
-ANISOU 2505  C   TYR A1001     2476   2537   2641      8    -83   -190       C  
-ATOM   2506  O   TYR A1001     -53.386   5.513 -14.768  1.00 18.40           O  
-ANISOU 2506  O   TYR A1001     2262   2315   2415      5    -67   -184       O  
-ATOM   2507  CB  TYR A1001     -55.571   7.323 -16.409  1.00 19.90           C  
-ANISOU 2507  CB  TYR A1001     2441   2508   2612     28   -104   -183       C  
-ATOM   2508  CG  TYR A1001     -56.803   8.207 -16.397  1.00 21.14           C  
-ANISOU 2508  CG  TYR A1001     2584   2664   2786     38   -116   -184       C  
-ATOM   2509  CD1 TYR A1001     -57.956   7.857 -17.077  1.00 20.98           C  
-ANISOU 2509  CD1 TYR A1001     2549   2646   2775     43   -139   -195       C  
-ATOM   2510  CD2 TYR A1001     -56.818   9.374 -15.659  1.00 20.79           C  
-ANISOU 2510  CD2 TYR A1001     2536   2613   2749     43   -107   -178       C  
-ATOM   2511  CE1 TYR A1001     -59.084   8.687 -17.078  1.00 21.59           C  
-ANISOU 2511  CE1 TYR A1001     2611   2722   2870     55   -153   -198       C  
-ATOM   2512  CE2 TYR A1001     -57.921  10.208 -15.672  1.00 23.15           C  
-ANISOU 2512  CE2 TYR A1001     2821   2910   3064     55   -120   -182       C  
-ATOM   2513  CZ  TYR A1001     -59.053   9.864 -16.381  1.00 22.19           C  
-ANISOU 2513  CZ  TYR A1001     2685   2793   2952     61   -143   -191       C  
-ATOM   2514  OH  TYR A1001     -60.147  10.696 -16.316  1.00 23.40           O  
-ANISOU 2514  OH  TYR A1001     2821   2944   3124     75   -156   -197       O  
-ATOM   2515  N   LEU A1002     -54.366   4.461 -16.523  1.00 20.13           N  
-ANISOU 2515  N   LEU A1002     2478   2537   2633      9    -99   -199       N  
-ATOM   2516  CA  LEU A1002     -53.229   3.695 -16.904  1.00 20.83           C  
-ANISOU 2516  CA  LEU A1002     2581   2627   2706      7    -96   -203       C  
-ATOM   2517  C   LEU A1002     -53.067   3.876 -18.394  1.00 21.75           C  
-ANISOU 2517  C   LEU A1002     2710   2753   2799     19   -111   -207       C  
-ATOM   2518  O   LEU A1002     -53.988   3.652 -19.142  1.00 22.67           O  
-ANISOU 2518  O   LEU A1002     2822   2872   2918     25   -132   -217       O  
-ATOM   2519  CB  LEU A1002     -53.456   2.241 -16.548  1.00 21.57           C  
-ANISOU 2519  CB  LEU A1002     2666   2711   2817     -2    -99   -214       C  
-ATOM   2520  CG  LEU A1002     -52.365   1.239 -16.918  1.00 24.42           C  
-ANISOU 2520  CG  LEU A1002     3040   3071   3168     -2   -100   -223       C  
-ATOM   2521  CD1 LEU A1002     -51.097   1.549 -16.181  1.00 26.42           C  
-ANISOU 2521  CD1 LEU A1002     3303   3326   3411     -3    -80   -214       C  
-ATOM   2522  CD2 LEU A1002     -52.787  -0.152 -16.525  1.00 25.07           C  
-ANISOU 2522  CD2 LEU A1002     3114   3139   3275    -12   -107   -232       C  
-ATOM   2523  N   LEU A1003     -51.907   4.330 -18.829  1.00 22.86           N  
-ANISOU 2523  N   LEU A1003     2867   2901   2916     23   -100   -200       N  
-ATOM   2524  CA  LEU A1003     -51.656   4.533 -20.246  1.00 23.41           C  
-ANISOU 2524  CA  LEU A1003     2952   2984   2957     35   -109   -200       C  
-ATOM   2525  C   LEU A1003     -50.676   3.494 -20.741  1.00 24.06           C  
-ANISOU 2525  C   LEU A1003     3042   3074   3024     37   -106   -214       C  
-ATOM   2526  O   LEU A1003     -49.650   3.208 -20.104  1.00 25.92           O  
-ANISOU 2526  O   LEU A1003     3278   3307   3264     30    -89   -214       O  
-ATOM   2527  CB  LEU A1003     -51.048   5.914 -20.491  1.00 23.94           C  
-ANISOU 2527  CB  LEU A1003     3031   3055   3009     39    -95   -178       C  
-ATOM   2528  CG  LEU A1003     -51.985   7.108 -20.528  1.00 23.73           C  
-ANISOU 2528  CG  LEU A1003     3003   3023   2990     45   -104   -164       C  
-ATOM   2529  CD1 LEU A1003     -52.641   7.320 -19.176  1.00 24.07           C  
-ANISOU 2529  CD1 LEU A1003     3027   3052   3065     37   -101   -166       C  
-ATOM   2530  CD2 LEU A1003     -51.192   8.341 -20.942  1.00 23.83           C  
-ANISOU 2530  CD2 LEU A1003     3032   3036   2988     47    -90   -140       C  
-ATOM   2531  N   LYS A1004     -50.980   2.949 -21.900  1.00 25.15           N  
-ANISOU 2531  N   LYS A1004     3187   3224   3146     48   -125   -229       N  
-ATOM   2532  CA  LYS A1004     -50.046   2.163 -22.671  1.00 24.89           C  
-ANISOU 2532  CA  LYS A1004     3165   3204   3090     56   -124   -244       C  
-ATOM   2533  C   LYS A1004     -49.364   3.098 -23.650  1.00 23.59           C  
-ANISOU 2533  C   LYS A1004     3017   3060   2887     66   -111   -228       C  
-ATOM   2534  O   LYS A1004     -50.031   3.692 -24.489  1.00 23.49           O  
-ANISOU 2534  O   LYS A1004     3014   3056   2855     78   -124   -221       O  
-ATOM   2535  CB  LYS A1004     -50.797   1.067 -23.392  1.00 27.38           C  
-ANISOU 2535  CB  LYS A1004     3476   3520   3405     65   -153   -272       C  
-ATOM   2536  CG  LYS A1004     -49.922   0.070 -24.131  1.00 32.14           C  
-ANISOU 2536  CG  LYS A1004     4088   4135   3989     75   -156   -296       C  
-ATOM   2537  CD  LYS A1004     -50.793  -1.106 -24.563  1.00 37.19           C  
-ANISOU 2537  CD  LYS A1004     4720   4766   4643     80   -189   -328       C  
-ATOM   2538  CE  LYS A1004     -50.266  -1.799 -25.799  1.00 39.69           C  
-ANISOU 2538  CE  LYS A1004     5049   5104   4928    100   -201   -356       C  
-ATOM   2539  NZ  LYS A1004     -51.142  -2.944 -26.160  1.00 43.05           N  
-ANISOU 2539  NZ  LYS A1004     5465   5517   5374    105   -238   -390       N  
-ATOM   2540  N   LEU A1005     -48.049   3.250 -23.509  1.00 24.60           N  
-ANISOU 2540  N   LEU A1005     3148   3193   3006     62    -84   -222       N  
-ATOM   2541  CA  LEU A1005     -47.241   4.167 -24.325  1.00 27.78           C  
-ANISOU 2541  CA  LEU A1005     3565   3613   3377     68    -64   -202       C  
-ATOM   2542  C   LEU A1005     -46.195   3.461 -25.187  1.00 28.09           C  
-ANISOU 2542  C   LEU A1005     3611   3676   3387     77    -53   -217       C  
-ATOM   2543  O   LEU A1005     -45.566   2.510 -24.752  1.00 26.23           O  
-ANISOU 2543  O   LEU A1005     3365   3436   3164     75    -50   -238       O  
-ATOM   2544  CB  LEU A1005     -46.471   5.114 -23.431  1.00 31.57           C  
-ANISOU 2544  CB  LEU A1005     4039   4082   3875     53    -38   -180       C  
-ATOM   2545  CG  LEU A1005     -47.215   6.060 -22.491  1.00 33.72           C  
-ANISOU 2545  CG  LEU A1005     4305   4333   4176     44    -42   -163       C  
-ATOM   2546  CD1 LEU A1005     -46.197   6.883 -21.724  1.00 37.32           C  
-ANISOU 2546  CD1 LEU A1005     4754   4779   4647     31    -17   -149       C  
-ATOM   2547  CD2 LEU A1005     -48.109   6.974 -23.278  1.00 33.24           C  
-ANISOU 2547  CD2 LEU A1005     4256   4275   4100     53    -54   -145       C  
-ATOM   2548  N   LYS A1006     -46.063   3.899 -26.429  1.00 28.51           N  
-ANISOU 2548  N   LYS A1006     3681   3753   3399     91    -48   -207       N  
-ATOM   2549  CA  LYS A1006     -45.021   3.431 -27.313  1.00 29.01           C  
-ANISOU 2549  CA  LYS A1006     3750   3843   3429    102    -31   -219       C  
-ATOM   2550  C   LYS A1006     -43.951   4.478 -27.199  1.00 27.48           C  
-ANISOU 2550  C   LYS A1006     3556   3653   3233     90      7   -188       C  
-ATOM   2551  O   LYS A1006     -44.239   5.659 -27.363  1.00 24.95           O  
-ANISOU 2551  O   LYS A1006     3245   3328   2907     86     14   -155       O  
-ATOM   2552  CB  LYS A1006     -45.521   3.348 -28.765  1.00 33.26           C  
-ANISOU 2552  CB  LYS A1006     4310   4410   3919    125    -46   -224       C  
-ATOM   2553  CG  LYS A1006     -44.464   3.274 -29.871  1.00 37.00           C  
-ANISOU 2553  CG  LYS A1006     4794   4919   4344    139    -20   -224       C  
-ATOM   2554  CD  LYS A1006     -43.990   1.853 -30.117  1.00 40.69           C  
-ANISOU 2554  CD  LYS A1006     5254   5399   4806    152    -28   -270       C  
-ATOM   2555  CE  LYS A1006     -43.059   1.768 -31.330  1.00 43.97           C  
-ANISOU 2555  CE  LYS A1006     5682   5857   5168    170     -3   -275       C  
-ATOM   2556  NZ  LYS A1006     -43.777   2.116 -32.588  1.00 47.64           N  
-ANISOU 2556  NZ  LYS A1006     6172   6348   5580    193    -18   -267       N  
-ATOM   2557  N   PHE A1007     -42.742   4.028 -26.905  1.00 26.51           N  
-ANISOU 2557  N   PHE A1007     3420   3535   3117     85     30   -201       N  
-ATOM   2558  CA  PHE A1007     -41.570   4.853 -26.895  1.00 28.86           C  
-ANISOU 2558  CA  PHE A1007     3712   3840   3415     73     67   -178       C  
-ATOM   2559  C   PHE A1007     -40.910   4.719 -28.274  1.00 30.19           C  
-ANISOU 2559  C   PHE A1007     3891   4046   3533     88     89   -178       C  
-ATOM   2560  O   PHE A1007     -40.478   3.639 -28.637  1.00 32.59           O  
-ANISOU 2560  O   PHE A1007     4191   4368   3824    102     86   -211       O  
-ATOM   2561  CB  PHE A1007     -40.574   4.361 -25.841  1.00 27.24           C  
-ANISOU 2561  CB  PHE A1007     3483   3622   3245     62     78   -196       C  
-ATOM   2562  CG  PHE A1007     -40.986   4.606 -24.424  1.00 25.56           C  
-ANISOU 2562  CG  PHE A1007     3260   3375   3076     47     65   -193       C  
-ATOM   2563  CD1 PHE A1007     -42.112   3.986 -23.894  1.00 25.67           C  
-ANISOU 2563  CD1 PHE A1007     3276   3373   3104     50     34   -207       C  
-ATOM   2564  CD2 PHE A1007     -40.240   5.443 -23.597  1.00 25.77           C  
-ANISOU 2564  CD2 PHE A1007     3272   3388   3131     31     84   -179       C  
-ATOM   2565  CE1 PHE A1007     -42.485   4.219 -22.568  1.00 25.66           C  
-ANISOU 2565  CE1 PHE A1007     3265   3346   3139     38     25   -203       C  
-ATOM   2566  CE2 PHE A1007     -40.628   5.706 -22.276  1.00 23.83           C  
-ANISOU 2566  CE2 PHE A1007     3018   3114   2920     20     71   -178       C  
-ATOM   2567  CZ  PHE A1007     -41.751   5.086 -21.767  1.00 24.06           C  
-ANISOU 2567  CZ  PHE A1007     3051   3131   2958     25     43   -189       C  
-ATOM   2568  N   ASN A1008     -40.830   5.807 -29.029  1.00 30.73           N  
-ANISOU 2568  N   ASN A1008     3974   4126   3575     87    110   -141       N  
-ATOM   2569  CA  ASN A1008     -40.133   5.807 -30.331  1.00 32.68           C  
-ANISOU 2569  CA  ASN A1008     4232   4413   3770    100    137   -134       C  
-ATOM   2570  C   ASN A1008     -38.748   6.389 -30.184  1.00 32.91           C  
-ANISOU 2570  C   ASN A1008     4244   4447   3812     82    184   -116       C  
-ATOM   2571  O   ASN A1008     -38.581   7.615 -30.138  1.00 32.71           O  
-ANISOU 2571  O   ASN A1008     4222   4410   3797     66    205    -74       O  
-ATOM   2572  CB  ASN A1008     -40.929   6.623 -31.338  1.00 33.30           C  
-ANISOU 2572  CB  ASN A1008     4341   4504   3807    112    132   -101       C  
-ATOM   2573  CG  ASN A1008     -42.252   5.980 -31.657  1.00 38.18           C  
-ANISOU 2573  CG  ASN A1008     4974   5123   4409    133     84   -124       C  
-ATOM   2574  OD1 ASN A1008     -42.325   4.763 -31.932  1.00 45.80           O  
-ANISOU 2574  OD1 ASN A1008     5936   6103   5361    150     66   -167       O  
-ATOM   2575  ND2 ASN A1008     -43.315   6.758 -31.608  1.00 41.57           N  
-ANISOU 2575  ND2 ASN A1008     5417   5535   4844    133     62   -100       N  
-ATOM   2576  N   PHE A1009     -37.768   5.505 -30.028  1.00 34.30           N  
-ANISOU 2576  N   PHE A1009     4400   4637   3996     85    197   -149       N  
-ATOM   2577  CA  PHE A1009     -36.392   5.915 -29.768  1.00 38.34           C  
-ANISOU 2577  CA  PHE A1009     4887   5152   4529     68    239   -140       C  
-ATOM   2578  C   PHE A1009     -35.709   6.559 -30.981  1.00 40.77           C  
-ANISOU 2578  C   PHE A1009     5203   5495   4793     69    284   -109       C  
-ATOM   2579  O   PHE A1009     -35.978   6.201 -32.112  1.00 41.70           O  
-ANISOU 2579  O   PHE A1009     5341   5647   4855     92    285   -112       O  
-ATOM   2580  CB  PHE A1009     -35.582   4.729 -29.275  1.00 37.61           C  
-ANISOU 2580  CB  PHE A1009     4769   5064   4456     74    237   -187       C  
-ATOM   2581  CG  PHE A1009     -35.964   4.287 -27.916  1.00 38.17           C  
-ANISOU 2581  CG  PHE A1009     4829   5098   4576     66    203   -207       C  
-ATOM   2582  CD1 PHE A1009     -36.919   3.296 -27.739  1.00 38.86           C  
-ANISOU 2582  CD1 PHE A1009     4927   5176   4661     81    162   -234       C  
-ATOM   2583  CD2 PHE A1009     -35.399   4.899 -26.792  1.00 38.17           C  
-ANISOU 2583  CD2 PHE A1009     4807   5071   4623     44    212   -197       C  
-ATOM   2584  CE1 PHE A1009     -37.310   2.909 -26.468  1.00 37.47           C  
-ANISOU 2584  CE1 PHE A1009     4743   4967   4528     74    135   -247       C  
-ATOM   2585  CE2 PHE A1009     -35.776   4.504 -25.522  1.00 39.55           C  
-ANISOU 2585  CE2 PHE A1009     4975   5215   4837     40    181   -214       C  
-ATOM   2586  CZ  PHE A1009     -36.737   3.509 -25.362  1.00 39.26           C  
-ANISOU 2586  CZ  PHE A1009     4951   5170   4795     54    145   -236       C  
-ATOM   2587  N   LYS A1010     -34.860   7.552 -30.717  1.00 49.07           N  
-ANISOU 2587  N   LYS A1010     6237   6536   5871     44    321    -78       N  
-ATOM   2588  CA  LYS A1010     -34.039   8.217 -31.731  1.00 55.57           C  
-ANISOU 2588  CA  LYS A1010     7062   7390   6664     39    373    -44       C  
-ATOM   2589  C   LYS A1010     -32.594   7.695 -31.729  1.00 59.37           C  
-ANISOU 2589  C   LYS A1010     7507   7894   7156     35    409    -69       C  
-ATOM   2590  O   LYS A1010     -32.297   6.570 -31.268  1.00 61.97           O  
-ANISOU 2590  O   LYS A1010     7819   8227   7500     47    391   -119       O  
-ATOM   2591  CB  LYS A1010     -34.047   9.726 -31.462  1.00 57.22           C  
-ANISOU 2591  CB  LYS A1010     7272   7566   6901     10    390     10       C  
-ATOM   2592  CG  LYS A1010     -35.418  10.346 -31.676  1.00 58.89           C  
-ANISOU 2592  CG  LYS A1010     7520   7761   7096     18    359     40       C  
-ATOM   2593  CD  LYS A1010     -35.559  11.656 -30.922  1.00 61.82           C  
-ANISOU 2593  CD  LYS A1010     7887   8085   7518    -10    359     77       C  
-ATOM   2594  CE  LYS A1010     -37.025  12.038 -30.742  1.00 63.30           C  
-ANISOU 2594  CE  LYS A1010     8101   8247   7702      0    315     88       C  
-ATOM   2595  NZ  LYS A1010     -37.176  13.368 -30.087  1.00 60.07           N  
-ANISOU 2595  NZ  LYS A1010     7689   7792   7341    -23    315    124       N  
-TER    2596      LYS A1010                                                      
-ATOM   2597  N   LYS B 662     -59.894 -23.541  11.761  1.00 81.72           N  
-ANISOU 2597  N   LYS B 662    10650   8942  11457    906  -1213     32       N  
-ATOM   2598  CA  LYS B 662     -59.621 -22.449  12.731  1.00 81.84           C  
-ANISOU 2598  CA  LYS B 662    10593   9051  11452    886  -1270     58       C  
-ATOM   2599  C   LYS B 662     -59.730 -21.133  11.973  1.00 82.75           C  
-ANISOU 2599  C   LYS B 662    10624   9263  11554    839  -1181      3       C  
-ATOM   2600  O   LYS B 662     -58.809 -20.762  11.255  1.00 83.65           O  
-ANISOU 2600  O   LYS B 662    10637   9394  11754    890  -1135    -51       O  
-ATOM   2601  CB  LYS B 662     -58.221 -22.604  13.352  1.00 78.66           C  
-ANISOU 2601  CB  LYS B 662    10105   8631  11152    987  -1355     68       C  
-ATOM   2602  N   SER B 663     -60.870 -20.454  12.108  1.00 80.97           N  
-ANISOU 2602  N   SER B 663    10442   9098  11225    742  -1154     19       N  
-ATOM   2603  CA  SER B 663     -61.052 -19.122  11.528  1.00 74.79           C  
-ANISOU 2603  CA  SER B 663     9587   8408  10423    693  -1079    -23       C  
-ATOM   2604  C   SER B 663     -60.290 -18.088  12.336  1.00 68.11           C  
-ANISOU 2604  C   SER B 663     8646   7630   9604    705  -1132    -19       C  
-ATOM   2605  O   SER B 663     -60.250 -18.169  13.556  1.00 64.02           O  
-ANISOU 2605  O   SER B 663     8153   7116   9057    704  -1224     29       O  
-ATOM   2606  CB  SER B 663     -62.541 -18.745  11.502  1.00 74.74           C  
-ANISOU 2606  CB  SER B 663     9656   8443  10300    591  -1041     -2       C  
-ATOM   2607  N   LYS B 664     -59.707 -17.101  11.659  1.00 67.34           N  
-ANISOU 2607  N   LYS B 664     8444   7587   9555    710  -1073    -70       N  
-ATOM   2608  CA  LYS B 664     -59.151 -15.928  12.343  1.00 70.32           C  
-ANISOU 2608  CA  LYS B 664     8735   8037   9946    699  -1111    -73       C  
-ATOM   2609  C   LYS B 664     -60.214 -14.869  12.738  1.00 65.61           C  
-ANISOU 2609  C   LYS B 664     8171   7510   9247    607  -1094    -59       C  
-ATOM   2610  O   LYS B 664     -59.904 -13.920  13.461  1.00 64.36           O  
-ANISOU 2610  O   LYS B 664     7964   7407   9083    588  -1133    -58       O  
-ATOM   2611  CB  LYS B 664     -58.084 -15.261  11.464  1.00 73.76           C  
-ANISOU 2611  CB  LYS B 664     9045   8503  10479    735  -1052   -131       C  
-ATOM   2612  N   LEU B 665     -61.450 -15.021  12.265  1.00 58.58           N  
-ANISOU 2612  N   LEU B 665     7362   6618   8279    550  -1036    -50       N  
-ATOM   2613  CA  LEU B 665     -62.475 -14.000  12.491  1.00 54.59           C  
-ANISOU 2613  CA  LEU B 665     6878   6177   7686    470  -1006    -42       C  
-ATOM   2614  C   LEU B 665     -62.923 -13.965  13.940  1.00 54.57           C  
-ANISOU 2614  C   LEU B 665     6931   6193   7612    441  -1089      8       C  
-ATOM   2615  O   LEU B 665     -63.027 -15.007  14.574  1.00 54.20           O  
-ANISOU 2615  O   LEU B 665     6952   6097   7544    457  -1151     49       O  
-ATOM   2616  CB  LEU B 665     -63.710 -14.263  11.629  1.00 51.04           C  
-ANISOU 2616  CB  LEU B 665     6498   5723   7174    419   -930    -40       C  
-ATOM   2617  CG  LEU B 665     -63.535 -14.229  10.114  1.00 47.99           C  
-ANISOU 2617  CG  LEU B 665     6075   5328   6831    430   -837    -88       C  
-ATOM   2618  CD1 LEU B 665     -64.764 -14.802   9.441  1.00 46.23           C  
-ANISOU 2618  CD1 LEU B 665     5938   5088   6539    380   -788    -78       C  
-ATOM   2619  CD2 LEU B 665     -63.265 -12.822   9.631  1.00 48.03           C  
-ANISOU 2619  CD2 LEU B 665     5994   5400   6856    410   -782   -122       C  
-ATOM   2620  N   PRO B 666     -63.256 -12.769  14.450  1.00 51.16           N  
-ANISOU 2620  N   PRO B 666     6477   5827   7133    394  -1085      3       N  
-ATOM   2621  CA  PRO B 666     -63.851 -12.675  15.785  1.00 49.06           C  
-ANISOU 2621  CA  PRO B 666     6274   5585   6781    356  -1149     46       C  
-ATOM   2622  C   PRO B 666     -65.112 -13.526  15.908  1.00 49.64           C  
-ANISOU 2622  C   PRO B 666     6456   5636   6770    314  -1137     90       C  
-ATOM   2623  O   PRO B 666     -65.850 -13.695  14.922  1.00 47.81           O  
-ANISOU 2623  O   PRO B 666     6244   5397   6525    289  -1062     80       O  
-ATOM   2624  CB  PRO B 666     -64.205 -11.184  15.918  1.00 50.92           C  
-ANISOU 2624  CB  PRO B 666     6471   5893   6983    308  -1110     20       C  
-ATOM   2625  CG  PRO B 666     -63.352 -10.474  14.903  1.00 51.42           C  
-ANISOU 2625  CG  PRO B 666     6434   5967   7137    333  -1058    -32       C  
-ATOM   2626  CD  PRO B 666     -63.142 -11.455  13.787  1.00 50.10           C  
-ANISOU 2626  CD  PRO B 666     6267   5747   7023    371  -1017    -41       C  
-ATOM   2627  N   LYS B 667     -65.379 -14.023  17.115  1.00 47.73           N  
-ANISOU 2627  N   LYS B 667     6283   5387   6466    301  -1211    139       N  
-ATOM   2628  CA  LYS B 667     -66.548 -14.877  17.358  1.00 49.22           C  
-ANISOU 2628  CA  LYS B 667     6575   5553   6572    256  -1206    188       C  
-ATOM   2629  C   LYS B 667     -67.861 -14.204  16.882  1.00 42.60           C  
-ANISOU 2629  C   LYS B 667     5752   4768   5668    186  -1119    179       C  
-ATOM   2630  O   LYS B 667     -68.609 -14.811  16.116  1.00 39.00           O  
-ANISOU 2630  O   LYS B 667     5335   4288   5197    161  -1070    187       O  
-ATOM   2631  CB  LYS B 667     -66.639 -15.324  18.837  1.00 49.89           C  
-ANISOU 2631  CB  LYS B 667     6731   5636   6590    243  -1297    245       C  
-ATOM   2632  N   PRO B 668     -68.112 -12.946  17.293  1.00 38.99           N  
-ANISOU 2632  N   PRO B 668     5258   4380   5175    157  -1099    161       N  
-ATOM   2633  CA  PRO B 668     -69.326 -12.232  16.826  1.00 37.95           C  
-ANISOU 2633  CA  PRO B 668     5130   4300   4989    100  -1017    153       C  
-ATOM   2634  C   PRO B 668     -69.522 -12.276  15.311  1.00 37.21           C  
-ANISOU 2634  C   PRO B 668     5005   4193   4941    102   -940    125       C  
-ATOM   2635  O   PRO B 668     -70.642 -12.427  14.846  1.00 37.73           O  
-ANISOU 2635  O   PRO B 668     5105   4273   4959     56   -889    139       O  
-ATOM   2636  CB  PRO B 668     -69.095 -10.792  17.292  1.00 37.27           C  
-ANISOU 2636  CB  PRO B 668     4988   4274   4899     94  -1010    121       C  
-ATOM   2637  CG  PRO B 668     -68.161 -10.931  18.453  1.00 37.33           C  
-ANISOU 2637  CG  PRO B 668     5000   4272   4911    122  -1104    131       C  
-ATOM   2638  CD  PRO B 668     -67.243 -12.058  18.075  1.00 37.74           C  
-ANISOU 2638  CD  PRO B 668     5049   4256   5036    177  -1149    140       C  
-ATOM   2639  N   VAL B 669     -68.437 -12.157  14.556  1.00 37.43           N  
-ANISOU 2639  N   VAL B 669     4967   4196   5057    153   -932     85       N  
-ATOM   2640  CA  VAL B 669     -68.509 -12.158  13.099  1.00 37.81           C  
-ANISOU 2640  CA  VAL B 669     4986   4234   5147    156   -858     55       C  
-ATOM   2641  C   VAL B 669     -68.829 -13.566  12.600  1.00 38.83           C  
-ANISOU 2641  C   VAL B 669     5182   4301   5271    156   -858     74       C  
-ATOM   2642  O   VAL B 669     -69.699 -13.761  11.752  1.00 39.95           O  
-ANISOU 2642  O   VAL B 669     5351   4447   5383    118   -802     73       O  
-ATOM   2643  CB  VAL B 669     -67.201 -11.651  12.475  1.00 35.15           C  
-ANISOU 2643  CB  VAL B 669     4560   3890   4905    209   -845      7       C  
-ATOM   2644  CG1 VAL B 669     -67.270 -11.698  10.965  1.00 35.56           C  
-ANISOU 2644  CG1 VAL B 669     4590   3934   4989    210   -766    -24       C  
-ATOM   2645  CG2 VAL B 669     -66.901 -10.238  12.932  1.00 35.75           C  
-ANISOU 2645  CG2 VAL B 669     4573   4022   4987    200   -845    -13       C  
-ATOM   2646  N   GLN B 670     -68.154 -14.540  13.167  1.00 41.24           N  
-ANISOU 2646  N   GLN B 670     5518   4548   5604    197   -925     92       N  
-ATOM   2647  CA  GLN B 670     -68.447 -15.937  12.866  1.00 43.71           C  
-ANISOU 2647  CA  GLN B 670     5906   4790   5911    198   -934    114       C  
-ATOM   2648  C   GLN B 670     -69.919 -16.252  13.112  1.00 40.29           C  
-ANISOU 2648  C   GLN B 670     5552   4374   5382    120   -920    156       C  
-ATOM   2649  O   GLN B 670     -70.551 -16.880  12.280  1.00 38.91           O  
-ANISOU 2649  O   GLN B 670     5418   4172   5194     91   -880    154       O  
-ATOM   2650  CB  GLN B 670     -67.558 -16.875  13.700  1.00 47.08           C  
-ANISOU 2650  CB  GLN B 670     6361   5152   6376    254  -1022    139       C  
-ATOM   2651  CG  GLN B 670     -66.096 -16.902  13.259  1.00 49.80           C  
-ANISOU 2651  CG  GLN B 670     6629   5464   6829    338  -1034     98       C  
-ATOM   2652  CD  GLN B 670     -65.266 -17.853  14.115  1.00 52.48           C  
-ANISOU 2652  CD  GLN B 670     6994   5739   7208    398  -1128    130       C  
-ATOM   2653  OE1 GLN B 670     -65.751 -18.893  14.540  1.00 53.25           O  
-ANISOU 2653  OE1 GLN B 670     7184   5782   7268    385  -1165    176       O  
-ATOM   2654  NE2 GLN B 670     -64.032 -17.478  14.396  1.00 52.63           N  
-ANISOU 2654  NE2 GLN B 670     6932   5765   7301    460  -1169    111       N  
-ATOM   2655  N   ASP B 671     -70.454 -15.814  14.249  1.00 39.33           N  
-ANISOU 2655  N   ASP B 671     5451   4299   5194     84   -950    191       N  
-ATOM   2656  CA  ASP B 671     -71.864 -16.021  14.587  1.00 40.60           C  
-ANISOU 2656  CA  ASP B 671     5675   4488   5263      8   -932    233       C  
-ATOM   2657  C   ASP B 671     -72.797 -15.347  13.586  1.00 40.12           C  
-ANISOU 2657  C   ASP B 671     5584   4480   5181    -37   -848    211       C  
-ATOM   2658  O   ASP B 671     -73.825 -15.914  13.234  1.00 41.73           O  
-ANISOU 2658  O   ASP B 671     5835   4681   5339    -91   -823    234       O  
-ATOM   2659  CB  ASP B 671     -72.169 -15.550  16.029  1.00 45.09           C  
-ANISOU 2659  CB  ASP B 671     6263   5105   5764    -16   -973    268       C  
-ATOM   2660  CG  ASP B 671     -71.592 -16.504  17.105  1.00 51.66           C  
-ANISOU 2660  CG  ASP B 671     7157   5883   6590      8  -1062    311       C  
-ATOM   2661  OD1 ASP B 671     -71.044 -17.576  16.730  1.00 51.94           O  
-ANISOU 2661  OD1 ASP B 671     7222   5837   6676     45  -1092    317       O  
-ATOM   2662  OD2 ASP B 671     -71.660 -16.170  18.326  1.00 53.59           O  
-ANISOU 2662  OD2 ASP B 671     7421   6164   6778     -6  -1105    339       O  
-ATOM   2663  N   LEU B 672     -72.430 -14.151  13.117  1.00 38.75           N  
-ANISOU 2663  N   LEU B 672     5330   4352   5041    -16   -810    170       N  
-ATOM   2664  CA  LEU B 672     -73.203 -13.453  12.088  1.00 35.04           C  
-ANISOU 2664  CA  LEU B 672     4826   3930   4559    -51   -735    151       C  
-ATOM   2665  C   LEU B 672     -73.218 -14.247  10.805  1.00 35.61           C  
-ANISOU 2665  C   LEU B 672     4915   3957   4657    -52   -703    134       C  
-ATOM   2666  O   LEU B 672     -74.271 -14.415  10.193  1.00 33.29           O  
-ANISOU 2666  O   LEU B 672     4646   3684   4321   -105   -665    145       O  
-ATOM   2667  CB  LEU B 672     -72.618 -12.052  11.840  1.00 34.60           C  
-ANISOU 2667  CB  LEU B 672     4685   3919   4543    -22   -705    111       C  
-ATOM   2668  CG  LEU B 672     -73.258 -11.211  10.758  1.00 33.48           C  
-ANISOU 2668  CG  LEU B 672     4502   3823   4397    -48   -632     94       C  
-ATOM   2669  CD1 LEU B 672     -74.673 -10.801  11.142  1.00 34.21           C  
-ANISOU 2669  CD1 LEU B 672     4612   3973   4413   -105   -609    127       C  
-ATOM   2670  CD2 LEU B 672     -72.423  -9.965  10.461  1.00 35.82           C  
-ANISOU 2670  CD2 LEU B 672     4720   4143   4749    -13   -608     55       C  
-ATOM   2671  N   ILE B 673     -72.052 -14.745  10.380  1.00 36.33           N  
-ANISOU 2671  N   ILE B 673     4995   3989   4820      7   -718    103       N  
-ATOM   2672  CA  ILE B 673     -71.983 -15.550   9.154  1.00 39.14           C  
-ANISOU 2672  CA  ILE B 673     5373   4296   5201     10   -684     78       C  
-ATOM   2673  C   ILE B 673     -72.865 -16.802   9.248  1.00 40.48           C  
-ANISOU 2673  C   ILE B 673     5638   4422   5322    -38   -703    114       C  
-ATOM   2674  O   ILE B 673     -73.541 -17.158   8.285  1.00 40.71           O  
-ANISOU 2674  O   ILE B 673     5693   4446   5327    -79   -663    105       O  
-ATOM   2675  CB  ILE B 673     -70.538 -15.977   8.824  1.00 42.63           C  
-ANISOU 2675  CB  ILE B 673     5788   4676   5732     89   -698     40       C  
-ATOM   2676  CG1 ILE B 673     -69.629 -14.761   8.647  1.00 44.06           C  
-ANISOU 2676  CG1 ILE B 673     5871   4901   5967    129   -676      4       C  
-ATOM   2677  CG2 ILE B 673     -70.482 -16.843   7.571  1.00 42.31           C  
-ANISOU 2677  CG2 ILE B 673     5780   4582   5712     93   -658      8       C  
-ATOM   2678  CD1 ILE B 673     -70.229 -13.677   7.775  1.00 45.43           C  
-ANISOU 2678  CD1 ILE B 673     6003   5141   6116     90   -606    -13       C  
-ATOM   2679  N   LYS B 674     -72.840 -17.479  10.390  1.00 41.47           N  
-ANISOU 2679  N   LYS B 674     5815   4511   5429    -36   -766    155       N  
-ATOM   2680  CA  LYS B 674     -73.697 -18.663  10.587  1.00 44.76           C  
-ANISOU 2680  CA  LYS B 674     6326   4883   5797    -90   -786    195       C  
-ATOM   2681  C   LYS B 674     -75.174 -18.300  10.508  1.00 42.44           C  
-ANISOU 2681  C   LYS B 674     6043   4659   5424   -177   -750    222       C  
-ATOM   2682  O   LYS B 674     -75.955 -18.962   9.840  1.00 43.34           O  
-ANISOU 2682  O   LYS B 674     6202   4756   5510   -231   -729    228       O  
-ATOM   2683  CB  LYS B 674     -73.410 -19.321  11.942  1.00 47.69           C  
-ANISOU 2683  CB  LYS B 674     6750   5212   6157    -75   -862    243       C  
-ATOM   2684  CG  LYS B 674     -72.063 -20.029  12.005  1.00 54.43           C  
-ANISOU 2684  CG  LYS B 674     7610   5980   7091     10   -909    227       C  
-ATOM   2685  CD  LYS B 674     -71.847 -20.653  13.378  1.00 59.10           C  
-ANISOU 2685  CD  LYS B 674     8258   6534   7663     21   -991    284       C  
-ATOM   2686  CE  LYS B 674     -70.402 -21.080  13.554  1.00 66.49           C  
-ANISOU 2686  CE  LYS B 674     9174   7401   8686    118  -1045    269       C  
-ATOM   2687  NZ  LYS B 674     -70.045 -21.320  14.985  1.00 69.81           N  
-ANISOU 2687  NZ  LYS B 674     9628   7810   9088    136  -1132    324       N  
-ATOM   2688  N   MET B 675     -75.529 -17.239  11.210  1.00 39.84           N  
-ANISOU 2688  N   MET B 675     5668   4408   5061   -190   -744    238       N  
-ATOM   2689  CA  MET B 675     -76.861 -16.721  11.212  1.00 41.85           C  
-ANISOU 2689  CA  MET B 675     5914   4738   5248   -261   -707    262       C  
-ATOM   2690  C   MET B 675     -77.374 -16.432   9.792  1.00 42.94           C  
-ANISOU 2690  C   MET B 675     6021   4903   5391   -287   -648    233       C  
-ATOM   2691  O   MET B 675     -78.489 -16.818   9.421  1.00 45.70           O  
-ANISOU 2691  O   MET B 675     6399   5272   5693   -356   -630    255       O  
-ATOM   2692  CB  MET B 675     -76.827 -15.446  12.027  1.00 47.19           C  
-ANISOU 2692  CB  MET B 675     6533   5486   5910   -245   -702    262       C  
-ATOM   2693  CG  MET B 675     -78.152 -14.915  12.483  1.00 49.85           C  
-ANISOU 2693  CG  MET B 675     6863   5901   6175   -307   -673    295       C  
-ATOM   2694  SD  MET B 675     -77.789 -13.431  13.454  1.00 48.29           S  
-ANISOU 2694  SD  MET B 675     6606   5767   5975   -270   -671    281       S  
-ATOM   2695  CE  MET B 675     -79.470 -12.855  13.616  1.00 50.76           C  
-ANISOU 2695  CE  MET B 675     6904   6169   6214   -339   -618    311       C  
-ATOM   2696  N   ILE B 676     -76.557 -15.791   8.969  1.00 43.16           N  
-ANISOU 2696  N   ILE B 676     5993   4933   5474   -237   -620    185       N  
-ATOM   2697  CA  ILE B 676     -77.056 -15.337   7.658  1.00 41.46           C  
-ANISOU 2697  CA  ILE B 676     5745   4755   5253   -263   -564    162       C  
-ATOM   2698  C   ILE B 676     -77.006 -16.419   6.596  1.00 39.34           C  
-ANISOU 2698  C   ILE B 676     5528   4425   4993   -278   -555    141       C  
-ATOM   2699  O   ILE B 676     -77.775 -16.361   5.639  1.00 38.04           O  
-ANISOU 2699  O   ILE B 676     5364   4293   4799   -326   -521    136       O  
-ATOM   2700  CB  ILE B 676     -76.434 -14.004   7.170  1.00 39.88           C  
-ANISOU 2700  CB  ILE B 676     5462   4599   5094   -218   -527    127       C  
-ATOM   2701  CG1 ILE B 676     -74.976 -14.123   6.801  1.00 42.03           C  
-ANISOU 2701  CG1 ILE B 676     5713   4817   5439   -148   -530     83       C  
-ATOM   2702  CG2 ILE B 676     -76.611 -12.919   8.227  1.00 41.87           C  
-ANISOU 2702  CG2 ILE B 676     5671   4908   5331   -212   -533    146       C  
-ATOM   2703  CD1 ILE B 676     -74.431 -12.744   6.447  1.00 46.67           C  
-ANISOU 2703  CD1 ILE B 676     6219   5452   6064   -116   -494     55       C  
-ATOM   2704  N   PHE B 677     -76.133 -17.414   6.763  1.00 40.18           N  
-ANISOU 2704  N   PHE B 677     5681   4446   5140   -237   -588    127       N  
-ATOM   2705  CA  PHE B 677     -76.119 -18.555   5.845  1.00 42.24           C  
-ANISOU 2705  CA  PHE B 677     6005   4637   5408   -252   -581    103       C  
-ATOM   2706  C   PHE B 677     -76.853 -19.798   6.378  1.00 43.89           C  
-ANISOU 2706  C   PHE B 677     6306   4794   5576   -308   -621    144       C  
-ATOM   2707  O   PHE B 677     -76.649 -20.901   5.880  1.00 43.27           O  
-ANISOU 2707  O   PHE B 677     6295   4634   5514   -309   -628    125       O  
-ATOM   2708  CB  PHE B 677     -74.689 -18.893   5.447  1.00 43.78           C  
-ANISOU 2708  CB  PHE B 677     6192   4762   5680   -168   -580     54       C  
-ATOM   2709  CG  PHE B 677     -74.109 -17.966   4.414  1.00 42.58           C  
-ANISOU 2709  CG  PHE B 677     5967   4650   5561   -135   -524      5       C  
-ATOM   2710  CD1 PHE B 677     -74.559 -17.995   3.096  1.00 43.06           C  
-ANISOU 2710  CD1 PHE B 677     6039   4727   5596   -173   -474    -23       C  
-ATOM   2711  CD2 PHE B 677     -73.101 -17.088   4.746  1.00 41.81           C  
-ANISOU 2711  CD2 PHE B 677     5794   4575   5518    -70   -522    -11       C  
-ATOM   2712  CE1 PHE B 677     -74.021 -17.147   2.139  1.00 42.57           C  
-ANISOU 2712  CE1 PHE B 677     5915   4702   5559   -146   -421    -64       C  
-ATOM   2713  CE2 PHE B 677     -72.542 -16.247   3.787  1.00 40.56           C  
-ANISOU 2713  CE2 PHE B 677     5570   4450   5390    -45   -468    -53       C  
-ATOM   2714  CZ  PHE B 677     -72.991 -16.287   2.483  1.00 40.54           C  
-ANISOU 2714  CZ  PHE B 677     5582   4462   5359    -81   -415    -78       C  
-ATOM   2715  N   ASP B 678     -77.752 -19.602   7.335  1.00 44.22           N  
-ANISOU 2715  N   ASP B 678     6353   4884   5564   -358   -640    198       N  
-ATOM   2716  CA  ASP B 678     -78.480 -20.693   7.973  1.00 47.98           C  
-ANISOU 2716  CA  ASP B 678     6913   5318   5999   -419   -676    246       C  
-ATOM   2717  C   ASP B 678     -79.536 -21.283   7.032  1.00 46.58           C  
-ANISOU 2717  C   ASP B 678     6776   5141   5779   -504   -654    245       C  
-ATOM   2718  O   ASP B 678     -80.606 -20.709   6.829  1.00 44.91           O  
-ANISOU 2718  O   ASP B 678     6530   5015   5520   -567   -628    265       O  
-ATOM   2719  CB  ASP B 678     -79.128 -20.186   9.268  1.00 49.78           C  
-ANISOU 2719  CB  ASP B 678     7126   5611   6177   -449   -694    301       C  
-ATOM   2720  CG  ASP B 678     -79.657 -21.297  10.144  1.00 52.77           C  
-ANISOU 2720  CG  ASP B 678     7592   5942   6516   -502   -736    357       C  
-ATOM   2721  OD1 ASP B 678     -80.138 -22.323   9.626  1.00 56.11           O  
-ANISOU 2721  OD1 ASP B 678     8081   6310   6926   -556   -740    362       O  
-ATOM   2722  OD2 ASP B 678     -79.619 -21.130  11.374  1.00 57.86           O  
-ANISOU 2722  OD2 ASP B 678     8242   6603   7137   -496   -766    396       O  
-ATOM   2723  N   VAL B 679     -79.233 -22.464   6.512  1.00 47.92           N  
-ANISOU 2723  N   VAL B 679     7023   5214   5970   -507   -667    224       N  
-ATOM   2724  CA  VAL B 679     -80.097 -23.168   5.562  1.00 50.12           C  
-ANISOU 2724  CA  VAL B 679     7353   5477   6213   -588   -652    214       C  
-ATOM   2725  C   VAL B 679     -81.456 -23.563   6.183  1.00 50.06           C  
-ANISOU 2725  C   VAL B 679     7380   5501   6138   -693   -670    278       C  
-ATOM   2726  O   VAL B 679     -82.496 -23.480   5.534  1.00 44.05           O  
-ANISOU 2726  O   VAL B 679     6609   4795   5333   -773   -649    283       O  
-ATOM   2727  CB  VAL B 679     -79.353 -24.413   5.039  1.00 52.27           C  
-ANISOU 2727  CB  VAL B 679     7711   5622   6528   -559   -666    175       C  
-ATOM   2728  CG1 VAL B 679     -80.262 -25.284   4.203  1.00 53.91           C  
-ANISOU 2728  CG1 VAL B 679     7990   5800   6694   -653   -659    166       C  
-ATOM   2729  CG2 VAL B 679     -78.135 -23.980   4.230  1.00 50.44           C  
-ANISOU 2729  CG2 VAL B 679     7433   5373   6357   -465   -633    107       C  
-ATOM   2730  N   GLU B 680     -81.451 -23.952   7.454  1.00 51.05           N  
-ANISOU 2730  N   GLU B 680     7541   5600   6254   -694   -709    329       N  
-ATOM   2731  CA  GLU B 680     -82.718 -24.281   8.123  1.00 51.54           C  
-ANISOU 2731  CA  GLU B 680     7630   5699   6252   -795   -720    393       C  
-ATOM   2732  C   GLU B 680     -83.614 -23.045   8.266  1.00 51.51           C  
-ANISOU 2732  C   GLU B 680     7532   5833   6207   -827   -685    413       C  
-ATOM   2733  O   GLU B 680     -84.834 -23.146   8.130  1.00 52.99           O  
-ANISOU 2733  O   GLU B 680     7715   6075   6345   -920   -672    443       O  
-ATOM   2734  CB  GLU B 680     -82.559 -25.085   9.432  1.00 53.93           C  
-ANISOU 2734  CB  GLU B 680     8007   5938   6546   -799   -769    448       C  
-ATOM   2735  CG  GLU B 680     -83.574 -26.246   9.471  1.00 59.20           C  
-ANISOU 2735  CG  GLU B 680     8760   6562   7170   -911   -784    489       C  
-ATOM   2736  CD  GLU B 680     -83.394 -27.281   8.346  1.00 58.00           C  
-ANISOU 2736  CD  GLU B 680     8683   6309   7046   -929   -789    445       C  
-ATOM   2737  OE1 GLU B 680     -84.393 -27.897   7.893  1.00 68.29           O  
-ANISOU 2737  OE1 GLU B 680    10027   7609   8312  -1033   -785    457       O  
-ATOM   2738  OE2 GLU B 680     -82.242 -27.498   7.918  1.00 55.53           O  
-ANISOU 2738  OE2 GLU B 680     8387   5917   6793   -840   -795    395       O  
-ATOM   2739  N   SER B 681     -83.024 -21.867   8.484  1.00 47.96           N  
-ANISOU 2739  N   SER B 681     7004   5439   5781   -751   -667    395       N  
-ATOM   2740  CA  SER B 681     -83.814 -20.614   8.485  1.00 46.53           C  
-ANISOU 2740  CA  SER B 681     6730   5379   5568   -770   -629    406       C  
-ATOM   2741  C   SER B 681     -84.428 -20.325   7.131  1.00 43.13           C  
-ANISOU 2741  C   SER B 681     6263   4994   5130   -809   -596    380       C  
-ATOM   2742  O   SER B 681     -85.560 -19.859   7.047  1.00 42.30           O  
-ANISOU 2742  O   SER B 681     6112   4977   4985   -869   -575    408       O  
-ATOM   2743  CB  SER B 681     -82.970 -19.420   8.900  1.00 44.03           C  
-ANISOU 2743  CB  SER B 681     6345   5099   5284   -680   -618    384       C  
-ATOM   2744  OG  SER B 681     -82.671 -19.500  10.260  1.00 45.87           O  
-ANISOU 2744  OG  SER B 681     6602   5320   5507   -660   -648    417       O  
-ATOM   2745  N   MET B 682     -83.674 -20.614   6.078  1.00 43.76           N  
-ANISOU 2745  N   MET B 682     6364   5017   5247   -774   -591    327       N  
-ATOM   2746  CA  MET B 682     -84.192 -20.477   4.713  1.00 46.84           C  
-ANISOU 2746  CA  MET B 682     6735   5440   5622   -816   -565    301       C  
-ATOM   2747  C   MET B 682     -85.427 -21.352   4.520  1.00 47.71           C  
-ANISOU 2747  C   MET B 682     6891   5556   5680   -929   -580    333       C  
-ATOM   2748  O   MET B 682     -86.466 -20.888   4.070  1.00 47.71           O  
-ANISOU 2748  O   MET B 682     6842   5643   5645   -988   -564    351       O  
-ATOM   2749  CB  MET B 682     -83.101 -20.826   3.678  1.00 47.22           C  
-ANISOU 2749  CB  MET B 682     6815   5413   5713   -762   -556    235       C  
-ATOM   2750  CG  MET B 682     -81.890 -19.878   3.670  1.00 47.78           C  
-ANISOU 2750  CG  MET B 682     6827   5490   5839   -657   -536    200       C  
-ATOM   2751  SD  MET B 682     -80.595 -20.447   2.550  1.00 46.13           S  
-ANISOU 2751  SD  MET B 682     6657   5189   5682   -595   -520    125       S  
-ATOM   2752  CE  MET B 682     -79.130 -19.815   3.320  1.00 44.48           C  
-ANISOU 2752  CE  MET B 682     6399   4958   5545   -479   -524    108       C  
-ATOM   2753  N   LYS B 683     -85.328 -22.616   4.912  1.00 49.40           N  
-ANISOU 2753  N   LYS B 683     7199   5678   5894   -960   -612    343       N  
-ATOM   2754  CA  LYS B 683     -86.476 -23.530   4.805  1.00 49.83           C  
-ANISOU 2754  CA  LYS B 683     7303   5727   5901  -1076   -629    376       C  
-ATOM   2755  C   LYS B 683     -87.676 -23.122   5.674  1.00 48.11           C  
-ANISOU 2755  C   LYS B 683     7035   5607   5638  -1142   -624    442       C  
-ATOM   2756  O   LYS B 683     -88.822 -23.202   5.229  1.00 49.07           O  
-ANISOU 2756  O   LYS B 683     7135   5788   5720  -1233   -620    463       O  
-ATOM   2757  CB  LYS B 683     -86.031 -24.954   5.119  1.00 53.27           C  
-ANISOU 2757  CB  LYS B 683     7856   6031   6351  -1090   -665    375       C  
-ATOM   2758  CG  LYS B 683     -85.087 -25.567   4.087  1.00 58.44           C  
-ANISOU 2758  CG  LYS B 683     8571   6586   7046  -1045   -665    306       C  
-ATOM   2759  CD  LYS B 683     -84.619 -26.921   4.606  1.00 64.60           C  
-ANISOU 2759  CD  LYS B 683     9465   7230   7849  -1044   -702    313       C  
-ATOM   2760  CE  LYS B 683     -83.440 -27.499   3.837  1.00 69.97           C  
-ANISOU 2760  CE  LYS B 683    10202   7800   8584   -969   -700    243       C  
-ATOM   2761  NZ  LYS B 683     -82.999 -28.761   4.493  1.00 73.57           N  
-ANISOU 2761  NZ  LYS B 683    10764   8121   9067   -960   -740    259       N  
-ATOM   2762  N   LYS B 684     -87.424 -22.701   6.910  1.00 46.52           N  
-ANISOU 2762  N   LYS B 684     6813   5423   5438  -1099   -626    474       N  
-ATOM   2763  CA  LYS B 684     -88.520 -22.248   7.811  1.00 49.30           C  
-ANISOU 2763  CA  LYS B 684     7114   5872   5746  -1153   -612    533       C  
-ATOM   2764  C   LYS B 684     -89.296 -21.112   7.163  1.00 52.39           C  
-ANISOU 2764  C   LYS B 684     7398   6382   6125  -1163   -575    530       C  
-ATOM   2765  O   LYS B 684     -90.533 -21.090   7.155  1.00 51.02           O  
-ANISOU 2765  O   LYS B 684     7188   6284   5914  -1246   -565    568       O  
-ATOM   2766  CB  LYS B 684     -88.001 -21.836   9.218  1.00 46.76           C  
-ANISOU 2766  CB  LYS B 684     6787   5554   5425  -1093   -615    559       C  
-ATOM   2767  N   ALA B 685     -88.549 -20.174   6.599  1.00 54.84           N  
-ANISOU 2767  N   ALA B 685     7659   6707   6471  -1078   -557    486       N  
-ATOM   2768  CA  ALA B 685     -89.164 -19.049   5.910  1.00 56.21           C  
-ANISOU 2768  CA  ALA B 685     7735   6982   6638  -1076   -526    483       C  
-ATOM   2769  C   ALA B 685     -90.087 -19.518   4.794  1.00 54.43           C  
-ANISOU 2769  C   ALA B 685     7512   6783   6386  -1165   -532    486       C  
-ATOM   2770  O   ALA B 685     -91.235 -19.072   4.693  1.00 52.56           O  
-ANISOU 2770  O   ALA B 685     7207   6643   6122  -1218   -520    520       O  
-ATOM   2771  CB  ALA B 685     -88.093 -18.156   5.349  1.00 55.61           C  
-ANISOU 2771  CB  ALA B 685     7626   6897   6608   -978   -509    434       C  
-ATOM   2772  N   MET B 686     -89.606 -20.472   4.002  1.00 53.02           N  
-ANISOU 2772  N   MET B 686     7413   6519   6214  -1184   -554    449       N  
-ATOM   2773  CA  MET B 686     -90.419 -21.047   2.921  1.00 54.13           C  
-ANISOU 2773  CA  MET B 686     7571   6673   6323  -1276   -567    445       C  
-ATOM   2774  C   MET B 686     -91.672 -21.782   3.445  1.00 56.60           C  
-ANISOU 2774  C   MET B 686     7896   7014   6595  -1392   -585    500       C  
-ATOM   2775  O   MET B 686     -92.756 -21.731   2.849  1.00 57.30           O  
-ANISOU 2775  O   MET B 686     7942   7177   6652  -1473   -589    520       O  
-ATOM   2776  CB  MET B 686     -89.556 -21.984   2.049  1.00 54.11           C  
-ANISOU 2776  CB  MET B 686     7665   6559   6336  -1269   -583    387       C  
-ATOM   2777  CG  MET B 686     -88.475 -21.240   1.281  1.00 53.05           C  
-ANISOU 2777  CG  MET B 686     7507   6414   6235  -1171   -558    332       C  
-ATOM   2778  SD  MET B 686     -87.292 -22.192   0.306  1.00 52.38           S  
-ANISOU 2778  SD  MET B 686     7524   6202   6176  -1139   -562    255       S  
-ATOM   2779  CE  MET B 686     -88.368 -22.758  -0.995  1.00 54.72           C  
-ANISOU 2779  CE  MET B 686     7851   6527   6413  -1259   -576    244       C  
-ATOM   2780  N   VAL B 687     -91.524 -22.491   4.554  1.00 56.54           N  
-ANISOU 2780  N   VAL B 687     7947   6949   6586  -1404   -597    528       N  
-ATOM   2781  CA  VAL B 687     -92.670 -23.157   5.148  1.00 59.87           C  
-ANISOU 2781  CA  VAL B 687     8379   7398   6969  -1515   -608    584       C  
-ATOM   2782  C   VAL B 687     -93.683 -22.097   5.569  1.00 58.42           C  
-ANISOU 2782  C   VAL B 687     8076   7354   6766  -1528   -578    628       C  
-ATOM   2783  O   VAL B 687     -94.862 -22.255   5.301  1.00 58.58           O  
-ANISOU 2783  O   VAL B 687     8056   7444   6757  -1623   -580    660       O  
-ATOM   2784  CB  VAL B 687     -92.265 -24.069   6.336  1.00 63.60           C  
-ANISOU 2784  CB  VAL B 687     8941   7781   7441  -1521   -627    612       C  
-ATOM   2785  CG1 VAL B 687     -93.487 -24.499   7.142  1.00 64.01           C  
-ANISOU 2785  CG1 VAL B 687     8986   7885   7450  -1630   -626    681       C  
-ATOM   2786  CG2 VAL B 687     -91.502 -25.292   5.826  1.00 63.27           C  
-ANISOU 2786  CG2 VAL B 687     9022   7598   7419  -1527   -660    575       C  
-ATOM   2787  N   GLU B 688     -93.226 -21.030   6.219  1.00 56.18           N  
-ANISOU 2787  N   GLU B 688     7735   7111   6502  -1434   -549    627       N  
-ATOM   2788  CA  GLU B 688     -94.135 -19.970   6.670  1.00 63.50           C  
-ANISOU 2788  CA  GLU B 688     8550   8163   7415  -1433   -514    663       C  
-ATOM   2789  C   GLU B 688     -94.872 -19.306   5.512  1.00 60.99           C  
-ANISOU 2789  C   GLU B 688     8146   7932   7096  -1453   -507    659       C  
-ATOM   2790  O   GLU B 688     -95.974 -18.828   5.684  1.00 59.15           O  
-ANISOU 2790  O   GLU B 688     7827   7801   6847  -1493   -488    698       O  
-ATOM   2791  CB  GLU B 688     -93.407 -18.909   7.518  1.00 67.75           C  
-ANISOU 2791  CB  GLU B 688     9051   8716   7974  -1322   -485    653       C  
-ATOM   2792  CG  GLU B 688     -93.263 -19.223   9.005  1.00 77.62           C  
-ANISOU 2792  CG  GLU B 688    10342   9945   9205  -1321   -482    684       C  
-ATOM   2793  CD  GLU B 688     -92.830 -17.987   9.817  1.00 90.54           C  
-ANISOU 2793  CD  GLU B 688    11923  11625  10853  -1225   -449    675       C  
-ATOM   2794  OE1 GLU B 688     -91.640 -17.899  10.202  1.00 90.55           O  
-ANISOU 2794  OE1 GLU B 688    11969  11558  10878  -1149   -463    646       O  
-ATOM   2795  OE2 GLU B 688     -93.675 -17.079  10.070  1.00 98.49           O  
-ANISOU 2795  OE2 GLU B 688    12838  12734  11848  -1225   -410    695       O  
-ATOM   2796  N   TYR B 689     -94.274 -19.295   4.326  1.00 64.29           N  
-ANISOU 2796  N   TYR B 689     8587   8310   7530  -1427   -523    613       N  
-ATOM   2797  CA  TYR B 689     -94.985 -18.818   3.121  1.00 63.88           C  
-ANISOU 2797  CA  TYR B 689     8469   8335   7469  -1459   -527    612       C  
-ATOM   2798  C   TYR B 689     -95.913 -19.845   2.483  1.00 65.28           C  
-ANISOU 2798  C   TYR B 689     8675   8518   7610  -1587   -561    628       C  
-ATOM   2799  O   TYR B 689     -96.537 -19.572   1.446  1.00 66.75           O  
-ANISOU 2799  O   TYR B 689     8813   8767   7781  -1625   -575    629       O  
-ATOM   2800  CB  TYR B 689     -93.986 -18.372   2.064  1.00 62.74           C  
-ANISOU 2800  CB  TYR B 689     8340   8150   7346  -1385   -527    557       C  
-ATOM   2801  CG  TYR B 689     -93.282 -17.108   2.409  1.00 58.94           C  
-ANISOU 2801  CG  TYR B 689     7804   7690   6902  -1270   -493    544       C  
-ATOM   2802  CD1 TYR B 689     -93.989 -15.950   2.737  1.00 56.91           C  
-ANISOU 2802  CD1 TYR B 689     7440   7534   6648  -1243   -466    578       C  
-ATOM   2803  CD2 TYR B 689     -91.900 -17.061   2.394  1.00 59.12           C  
-ANISOU 2803  CD2 TYR B 689     7879   7628   6957  -1187   -488    497       C  
-ATOM   2804  CE1 TYR B 689     -93.326 -14.787   3.054  1.00 57.31           C  
-ANISOU 2804  CE1 TYR B 689     7448   7594   6734  -1141   -436    563       C  
-ATOM   2805  CE2 TYR B 689     -91.234 -15.912   2.709  1.00 59.02           C  
-ANISOU 2805  CE2 TYR B 689     7816   7631   6978  -1089   -459    484       C  
-ATOM   2806  CZ  TYR B 689     -91.944 -14.774   3.037  1.00 56.60           C  
-ANISOU 2806  CZ  TYR B 689     7413   7419   6674  -1068   -434    516       C  
-ATOM   2807  OH  TYR B 689     -91.228 -13.659   3.365  1.00 52.65           O  
-ANISOU 2807  OH  TYR B 689     6874   6922   6208   -973   -407    499       O  
-ATOM   2808  N   GLU B 690     -95.959 -21.036   3.068  1.00 63.53           N  
-ANISOU 2808  N   GLU B 690     8538   8226   7374  -1653   -579    639       N  
-ATOM   2809  CA  GLU B 690     -96.809 -22.103   2.569  1.00 66.54           C  
-ANISOU 2809  CA  GLU B 690     8958   8602   7723  -1784   -614    653       C  
-ATOM   2810  C   GLU B 690     -96.324 -22.642   1.220  1.00 65.03           C  
-ANISOU 2810  C   GLU B 690     8839   8344   7526  -1801   -643    596       C  
-ATOM   2811  O   GLU B 690     -97.088 -23.219   0.443  1.00 63.77           O  
-ANISOU 2811  O   GLU B 690     8691   8204   7336  -1905   -674    598       O  
-ATOM   2812  CB  GLU B 690     -98.272 -21.635   2.484  1.00 62.43           C  
-ANISOU 2812  CB  GLU B 690     8321   8218   7180  -1859   -610    706       C  
-ATOM   2813  N   ILE B 691     -95.030 -22.498   0.972  1.00 65.40           N  
-ANISOU 2813  N   ILE B 691     8938   8311   7601  -1702   -634    543       N  
-ATOM   2814  CA  ILE B 691     -94.421 -23.061  -0.219  1.00 67.09           C  
-ANISOU 2814  CA  ILE B 691     9232   8450   7810  -1708   -652    482       C  
-ATOM   2815  C   ILE B 691     -94.283 -24.564  -0.072  1.00 70.71           C  
-ANISOU 2815  C   ILE B 691     9816   8790   8261  -1779   -680    468       C  
-ATOM   2816  O   ILE B 691     -93.970 -25.067   0.997  1.00 70.84           O  
-ANISOU 2816  O   ILE B 691     9879   8742   8294  -1766   -680    488       O  
-ATOM   2817  CB  ILE B 691     -93.065 -22.393  -0.483  1.00 63.72           C  
-ANISOU 2817  CB  ILE B 691     8811   7978   7420  -1577   -625    431       C  
-ATOM   2818  CG1 ILE B 691     -93.406 -20.984  -0.954  1.00 62.90           C  
-ANISOU 2818  CG1 ILE B 691     8591   7993   7315  -1534   -605    445       C  
-ATOM   2819  CG2 ILE B 691     -92.231 -23.144  -1.521  1.00 63.09           C  
-ANISOU 2819  CG2 ILE B 691     8831   7799   7340  -1571   -635    361       C  
-ATOM   2820  CD1 ILE B 691     -92.272 -20.107  -1.350  1.00 62.85           C  
-ANISOU 2820  CD1 ILE B 691     8568   7970   7341  -1418   -576    404       C  
-ATOM   2821  N   ASP B 692     -94.502 -25.277  -1.160  1.00 68.80           N  
-ANISOU 2821  N   ASP B 692     9634   8515   7991  -1854   -707    432       N  
-ATOM   2822  CA  ASP B 692     -94.342 -26.699  -1.139  1.00 71.20           C  
-ANISOU 2822  CA  ASP B 692    10066   8697   8291  -1920   -733    410       C  
-ATOM   2823  C   ASP B 692     -92.877 -27.089  -1.328  1.00 69.51           C  
-ANISOU 2823  C   ASP B 692     9945   8351   8114  -1821   -721    344       C  
-ATOM   2824  O   ASP B 692     -92.394 -27.156  -2.462  1.00 61.38           O  
-ANISOU 2824  O   ASP B 692     8952   7291   7077  -1803   -718    281       O  
-ATOM   2825  CB  ASP B 692     -95.180 -27.338  -2.234  1.00 74.09           C  
-ANISOU 2825  CB  ASP B 692    10465   9076   8610  -2047   -767    392       C  
-ATOM   2826  CG  ASP B 692     -95.220 -28.839  -2.094  1.00 76.39           C  
-ANISOU 2826  CG  ASP B 692    10887   9242   8896  -2134   -797    379       C  
-ATOM   2827  OD1 ASP B 692     -96.321 -29.361  -2.283  1.00 82.39           O  
-ANISOU 2827  OD1 ASP B 692    11648  10037   9620  -2268   -828    407       O  
-ATOM   2828  OD2 ASP B 692     -94.184 -29.481  -1.741  1.00 72.92           O  
-ANISOU 2828  OD2 ASP B 692    10546   8669   8491  -2071   -790    347       O  
-ATOM   2829  N   LEU B 693     -92.201 -27.404  -0.223  1.00 68.43           N  
-ANISOU 2829  N   LEU B 693     9848   8137   8014  -1762   -716    360       N  
-ATOM   2830  CA  LEU B 693     -90.780 -27.772  -0.261  1.00 71.93           C  
-ANISOU 2830  CA  LEU B 693    10369   8457   8503  -1658   -707    304       C  
-ATOM   2831  C   LEU B 693     -90.502 -29.145  -0.888  1.00 78.96           C  
-ANISOU 2831  C   LEU B 693    11396   9213   9393  -1707   -729    253       C  
-ATOM   2832  O   LEU B 693     -89.375 -29.427  -1.309  1.00 75.25           O  
-ANISOU 2832  O   LEU B 693    10985   8649   8957  -1624   -716    191       O  
-ATOM   2833  CB  LEU B 693     -90.185 -27.758   1.135  1.00 71.20           C  
-ANISOU 2833  CB  LEU B 693    10281   8323   8449  -1586   -705    342       C  
-ATOM   2834  CG  LEU B 693     -89.942 -26.396   1.768  1.00 70.59           C  
-ANISOU 2834  CG  LEU B 693    10091   8341   8388  -1496   -677    368       C  
-ATOM   2835  CD1 LEU B 693     -89.284 -26.576   3.120  1.00 70.46           C  
-ANISOU 2835  CD1 LEU B 693    10101   8267   8402  -1433   -684    399       C  
-ATOM   2836  CD2 LEU B 693     -89.054 -25.550   0.876  1.00 69.41           C  
-ANISOU 2836  CD2 LEU B 693     9899   8209   8263  -1399   -649    309       C  
-ATOM   2837  N   GLN B 694     -91.524 -29.998  -0.945  1.00 85.46           N  
-ANISOU 2837  N   GLN B 694    12267  10025  10179  -1841   -760    278       N  
-ATOM   2838  CA  GLN B 694     -91.409 -31.275  -1.647  1.00 87.81           C  
-ANISOU 2838  CA  GLN B 694    12696  10199  10469  -1904   -782    226       C  
-ATOM   2839  C   GLN B 694     -91.305 -31.017  -3.146  1.00 84.17           C  
-ANISOU 2839  C   GLN B 694    12236   9766   9980  -1908   -770    153       C  
-ATOM   2840  O   GLN B 694     -90.425 -31.564  -3.796  1.00 85.88           O  
-ANISOU 2840  O   GLN B 694    12539   9877  10213  -1861   -760     79       O  
-ATOM   2841  CB  GLN B 694     -92.586 -32.212  -1.336  1.00 88.21           C  
-ANISOU 2841  CB  GLN B 694    12795  10236  10485  -2059   -819    273       C  
-ATOM   2842  N   LYS B 695     -92.157 -30.146  -3.685  1.00 80.93           N  
-ANISOU 2842  N   LYS B 695    11725   9498   9526  -1956   -770    173       N  
-ATOM   2843  CA  LYS B 695     -92.126 -29.851  -5.124  1.00 84.85           C  
-ANISOU 2843  CA  LYS B 695    12221  10033   9984  -1967   -764    112       C  
-ATOM   2844  C   LYS B 695     -91.082 -28.774  -5.511  1.00 89.05           C  
-ANISOU 2844  C   LYS B 695    12695  10598  10542  -1828   -719     76       C  
-ATOM   2845  O   LYS B 695     -90.577 -28.769  -6.637  1.00 86.61           O  
-ANISOU 2845  O   LYS B 695    12423  10269  10214  -1807   -702      7       O  
-ATOM   2846  CB  LYS B 695     -93.520 -29.465  -5.625  1.00 84.94           C  
-ANISOU 2846  CB  LYS B 695    12157  10179   9936  -2086   -793    152       C  
-ATOM   2847  N   MET B 696     -90.763 -27.857  -4.595  1.00 88.80           N  
-ANISOU 2847  N   MET B 696    12573  10617  10549  -1738   -697    121       N  
-ATOM   2848  CA  MET B 696     -89.753 -26.813  -4.860  1.00 83.10           C  
-ANISOU 2848  CA  MET B 696    11793   9923   9857  -1609   -655     91       C  
-ATOM   2849  C   MET B 696     -88.795 -26.632  -3.699  1.00 80.26           C  
-ANISOU 2849  C   MET B 696    11422   9509   9564  -1498   -637    106       C  
-ATOM   2850  O   MET B 696     -88.948 -25.700  -2.906  1.00 69.82           O  
-ANISOU 2850  O   MET B 696    10006   8266   8257  -1457   -628    158       O  
-ATOM   2851  CB  MET B 696     -90.389 -25.460  -5.175  1.00 82.10           C  
-ANISOU 2851  CB  MET B 696    11540   9949   9705  -1608   -645    130       C  
-ATOM   2852  CG  MET B 696     -89.376 -24.437  -5.690  1.00 79.22           C  
-ANISOU 2852  CG  MET B 696    11128   9607   9363  -1493   -602     93       C  
-ATOM   2853  SD  MET B 696     -90.135 -22.932  -6.275  1.00 85.47           S  
-ANISOU 2853  SD  MET B 696    11791  10562  10121  -1498   -595    135       S  
-ATOM   2854  CE  MET B 696     -90.572 -22.105  -4.736  1.00 88.64           C  
-ANISOU 2854  CE  MET B 696    12087  11031  10561  -1460   -592    217       C  
-ATOM   2855  N   PRO B 697     -87.787 -27.507  -3.605  1.00 81.06           N  
-ANISOU 2855  N   PRO B 697    11618   9476   9704  -1445   -633     58       N  
-ATOM   2856  CA  PRO B 697     -86.818 -27.351  -2.531  1.00 81.59           C  
-ANISOU 2856  CA  PRO B 697    11673   9492   9835  -1337   -624     73       C  
-ATOM   2857  C   PRO B 697     -85.952 -26.116  -2.717  1.00 78.27           C  
-ANISOU 2857  C   PRO B 697    11164   9129   9445  -1224   -584     52       C  
-ATOM   2858  O   PRO B 697     -85.903 -25.540  -3.795  1.00 75.20           O  
-ANISOU 2858  O   PRO B 697    10745   8794   9034  -1220   -558     16       O  
-ATOM   2859  CB  PRO B 697     -85.956 -28.609  -2.650  1.00 81.27           C  
-ANISOU 2859  CB  PRO B 697    11755   9293   9829  -1308   -630     18       C  
-ATOM   2860  CG  PRO B 697     -86.118 -29.054  -4.058  1.00 82.70           C  
-ANISOU 2860  CG  PRO B 697    11996   9455   9971  -1363   -620    -49       C  
-ATOM   2861  CD  PRO B 697     -87.523 -28.698  -4.430  1.00 83.69           C  
-ANISOU 2861  CD  PRO B 697    12075   9697  10028  -1484   -640     -9       C  
-ATOM   2862  N   LEU B 698     -85.262 -25.744  -1.657  1.00 72.88           N  
-ANISOU 2862  N   LEU B 698    10447   8432   8813  -1137   -581     77       N  
-ATOM   2863  CA  LEU B 698     -84.290 -24.670  -1.692  1.00 71.75           C  
-ANISOU 2863  CA  LEU B 698    10228   8324   8710  -1027   -547     56       C  
-ATOM   2864  C   LEU B 698     -83.378 -24.712  -2.937  1.00 73.32           C  
-ANISOU 2864  C   LEU B 698    10452   8483   8923   -977   -510    -25       C  
-ATOM   2865  O   LEU B 698     -83.154 -23.692  -3.589  1.00 69.35           O  
-ANISOU 2865  O   LEU B 698     9881   8054   8416   -943   -476    -41       O  
-ATOM   2866  CB  LEU B 698     -83.436 -24.774  -0.440  1.00 69.64           C  
-ANISOU 2866  CB  LEU B 698     9963   7998   8501   -944   -560     76       C  
-ATOM   2867  CG  LEU B 698     -82.795 -23.504   0.080  1.00 69.20           C  
-ANISOU 2867  CG  LEU B 698     9807   8005   8480   -853   -539     87       C  
-ATOM   2868  CD1 LEU B 698     -83.708 -22.290   0.160  1.00 68.52           C  
-ANISOU 2868  CD1 LEU B 698     9626   8052   8358   -886   -527    130       C  
-ATOM   2869  CD2 LEU B 698     -82.215 -23.818   1.445  1.00 65.51           C  
-ANISOU 2869  CD2 LEU B 698     9357   7480   8053   -799   -569    118       C  
-ATOM   2870  N   GLY B 699     -82.856 -25.893  -3.258  1.00 71.78           N  
-ANISOU 2870  N   GLY B 699    10358   8170   8746   -972   -514    -74       N  
-ATOM   2871  CA  GLY B 699     -81.971 -26.059  -4.416  1.00 69.88           C  
-ANISOU 2871  CA  GLY B 699    10151   7883   8518   -924   -472   -158       C  
-ATOM   2872  C   GLY B 699     -82.608 -25.827  -5.785  1.00 68.72           C  
-ANISOU 2872  C   GLY B 699    10009   7800   8300   -997   -452   -189       C  
-ATOM   2873  O   GLY B 699     -81.902 -25.604  -6.761  1.00 64.89           O  
-ANISOU 2873  O   GLY B 699     9527   7312   7816   -954   -408   -251       O  
-ATOM   2874  N   LYS B 700     -83.936 -25.848  -5.857  1.00 70.48           N  
-ANISOU 2874  N   LYS B 700    10229   8089   8461  -1109   -485   -145       N  
-ATOM   2875  CA  LYS B 700     -84.642 -25.701  -7.135  1.00 73.59           C  
-ANISOU 2875  CA  LYS B 700    10633   8547   8782  -1190   -480   -169       C  
-ATOM   2876  C   LYS B 700     -85.053 -24.260  -7.425  1.00 74.13           C  
-ANISOU 2876  C   LYS B 700    10586   8756   8824  -1184   -465   -130       C  
-ATOM   2877  O   LYS B 700     -85.397 -23.950  -8.560  1.00 80.75           O  
-ANISOU 2877  O   LYS B 700    11423   9652   9607  -1228   -455   -151       O  
-ATOM   2878  CB  LYS B 700     -85.877 -26.612  -7.201  1.00 75.17           C  
-ANISOU 2878  CB  LYS B 700    10896   8738   8928  -1324   -528   -147       C  
-ATOM   2879  N   LEU B 701     -85.051 -23.393  -6.411  1.00 72.14           N  
-ANISOU 2879  N   LEU B 701    10245   8557   8609  -1134   -467    -72       N  
-ATOM   2880  CA  LEU B 701     -85.315 -21.967  -6.613  1.00 69.95           C  
-ANISOU 2880  CA  LEU B 701     9859   8398   8319  -1112   -449    -36       C  
-ATOM   2881  C   LEU B 701     -84.386 -21.397  -7.676  1.00 65.51           C  
-ANISOU 2881  C   LEU B 701     9288   7843   7760  -1051   -400    -92       C  
-ATOM   2882  O   LEU B 701     -83.173 -21.564  -7.598  1.00 64.34           O  
-ANISOU 2882  O   LEU B 701     9160   7623   7664   -968   -368   -138       O  
-ATOM   2883  CB  LEU B 701     -85.071 -21.163  -5.331  1.00 73.06           C  
-ANISOU 2883  CB  LEU B 701    10172   8819   8767  -1042   -447     13       C  
-ATOM   2884  CG  LEU B 701     -86.075 -21.303  -4.190  1.00 76.82           C  
-ANISOU 2884  CG  LEU B 701    10625   9326   9235  -1095   -485     82       C  
-ATOM   2885  CD1 LEU B 701     -85.666 -20.411  -3.031  1.00 75.13           C  
-ANISOU 2885  CD1 LEU B 701    10337   9139   9070  -1015   -475    118       C  
-ATOM   2886  CD2 LEU B 701     -87.472 -20.936  -4.654  1.00 77.82           C  
-ANISOU 2886  CD2 LEU B 701    10708   9558   9303  -1188   -505    126       C  
-ATOM   2887  N   SER B 702     -84.953 -20.689  -8.636  1.00 60.00           N  
-ANISOU 2887  N   SER B 702     8554   7235   7007  -1092   -394    -82       N  
-ATOM   2888  CA  SER B 702     -84.174 -20.124  -9.727  1.00 60.15           C  
-ANISOU 2888  CA  SER B 702     8568   7270   7015  -1048   -345   -128       C  
-ATOM   2889  C   SER B 702     -84.521 -18.645  -9.946  1.00 57.33           C  
-ANISOU 2889  C   SER B 702     8111   7028   6646  -1032   -335    -77       C  
-ATOM   2890  O   SER B 702     -85.675 -18.224  -9.819  1.00 54.80           O  
-ANISOU 2890  O   SER B 702     7741   6787   6292  -1090   -371    -17       O  
-ATOM   2891  CB  SER B 702     -84.415 -20.932 -11.011  1.00 64.16           C  
-ANISOU 2891  CB  SER B 702     9168   7759   7452  -1122   -346   -183       C  
-ATOM   2892  OG  SER B 702     -85.292 -20.251 -11.892  1.00 64.64           O  
-ANISOU 2892  OG  SER B 702     9195   7925   7441  -1186   -360   -152       O  
-ATOM   2893  N   LYS B 703     -83.505 -17.866 -10.287  1.00 60.14           N  
-ANISOU 2893  N   LYS B 703     8433   7387   7032   -954   -285   -101       N  
-ATOM   2894  CA  LYS B 703     -83.655 -16.444 -10.576  1.00 62.63           C  
-ANISOU 2894  CA  LYS B 703     8662   7795   7341   -931   -268    -58       C  
-ATOM   2895  C   LYS B 703     -84.669 -16.196 -11.702  1.00 64.00           C  
-ANISOU 2895  C   LYS B 703     8839   8050   7428  -1014   -289    -35       C  
-ATOM   2896  O   LYS B 703     -85.477 -15.264 -11.632  1.00 61.22           O  
-ANISOU 2896  O   LYS B 703     8414   7784   7062  -1029   -309     30       O  
-ATOM   2897  CB  LYS B 703     -82.281 -15.890 -10.977  1.00 66.35           C  
-ANISOU 2897  CB  LYS B 703     9119   8241   7852   -847   -205   -102       C  
-ATOM   2898  CG  LYS B 703     -82.085 -14.400 -10.795  1.00 73.62           C  
-ANISOU 2898  CG  LYS B 703     9944   9225   8804   -795   -183    -58       C  
-ATOM   2899  CD  LYS B 703     -80.598 -14.084 -10.530  1.00 76.71           C  
-ANISOU 2899  CD  LYS B 703    10314   9564   9268   -701   -132    -99       C  
-ATOM   2900  CE  LYS B 703     -79.636 -14.809 -11.471  1.00 82.84           C  
-ANISOU 2900  CE  LYS B 703    11156  10284  10034   -687    -84   -178       C  
-ATOM   2901  NZ  LYS B 703     -78.497 -13.960 -11.951  1.00 86.58           N  
-ANISOU 2901  NZ  LYS B 703    11589  10767  10542   -625    -20   -202       N  
-ATOM   2902  N   ARG B 704     -84.655 -17.059 -12.716  1.00 69.02           N  
-ANISOU 2902  N   ARG B 704     9562   8658   8005  -1068   -286    -88       N  
-ATOM   2903  CA  ARG B 704     -85.532 -16.878 -13.874  1.00 74.47           C  
-ANISOU 2903  CA  ARG B 704    10265   9426   8605  -1150   -310    -72       C  
-ATOM   2904  C   ARG B 704     -87.001 -17.237 -13.557  1.00 69.43           C  
-ANISOU 2904  C   ARG B 704     9614   8837   7931  -1243   -380    -18       C  
-ATOM   2905  O   ARG B 704     -87.916 -16.585 -14.068  1.00 68.03           O  
-ANISOU 2905  O   ARG B 704     9390   8755   7705  -1289   -411     35       O  
-ATOM   2906  CB  ARG B 704     -85.010 -17.668 -15.086  1.00 71.19           C  
-ANISOU 2906  CB  ARG B 704     9952   8967   8130  -1180   -281   -152       C  
-ATOM   2907  N   GLN B 705     -87.222 -18.252 -12.720  1.00 63.77           N  
-ANISOU 2907  N   GLN B 705     8935   8056   7239  -1269   -407    -26       N  
-ATOM   2908  CA  GLN B 705     -88.582 -18.595 -12.281  1.00 61.01           C  
-ANISOU 2908  CA  GLN B 705     8564   7752   6865  -1357   -468     28       C  
-ATOM   2909  C   GLN B 705     -89.174 -17.463 -11.444  1.00 58.63           C  
-ANISOU 2909  C   GLN B 705     8144   7533   6600  -1324   -479    110       C  
-ATOM   2910  O   GLN B 705     -90.315 -17.076 -11.625  1.00 60.87           O  
-ANISOU 2910  O   GLN B 705     8372   7907   6848  -1382   -518    166       O  
-ATOM   2911  CB  GLN B 705     -88.626 -19.907 -11.481  1.00 57.50           C  
-ANISOU 2911  CB  GLN B 705     8189   7215   6444  -1391   -489      6       C  
-ATOM   2912  N   ILE B 706     -88.378 -16.902 -10.546  1.00 56.05           N  
-ANISOU 2912  N   ILE B 706     7774   7176   6345  -1228   -443    114       N  
-ATOM   2913  CA  ILE B 706     -88.880 -15.840  -9.680  1.00 53.30           C  
-ANISOU 2913  CA  ILE B 706     7321   6896   6034  -1191   -447    183       C  
-ATOM   2914  C   ILE B 706     -89.214 -14.600 -10.484  1.00 50.58           C  
-ANISOU 2914  C   ILE B 706     6909   6644   5665  -1179   -442    221       C  
-ATOM   2915  O   ILE B 706     -90.268 -13.989 -10.297  1.00 50.01           O  
-ANISOU 2915  O   ILE B 706     6761   6655   5583  -1204   -470    285       O  
-ATOM   2916  CB  ILE B 706     -87.882 -15.523  -8.554  1.00 51.43           C  
-ANISOU 2916  CB  ILE B 706     7063   6603   5876  -1093   -413    173       C  
-ATOM   2917  CG1 ILE B 706     -87.893 -16.691  -7.573  1.00 51.62           C  
-ANISOU 2917  CG1 ILE B 706     7141   6552   5921  -1115   -433    162       C  
-ATOM   2918  CG2 ILE B 706     -88.260 -14.234  -7.830  1.00 48.46           C  
-ANISOU 2918  CG2 ILE B 706     6582   6297   5535  -1045   -407    233       C  
-ATOM   2919  CD1 ILE B 706     -86.694 -16.728  -6.652  1.00 50.34           C  
-ANISOU 2919  CD1 ILE B 706     6989   6312   5828  -1025   -406    135       C  
-ATOM   2920  N   GLN B 707     -88.336 -14.257 -11.411  1.00 51.98           N  
-ANISOU 2920  N   GLN B 707     7115   6806   5829  -1143   -406    182       N  
-ATOM   2921  CA  GLN B 707     -88.588 -13.143 -12.311  1.00 54.70           C  
-ANISOU 2921  CA  GLN B 707     7411   7231   6142  -1137   -402    218       C  
-ATOM   2922  C   GLN B 707     -89.907 -13.345 -13.071  1.00 51.83           C  
-ANISOU 2922  C   GLN B 707     7043   6947   5702  -1236   -459    256       C  
-ATOM   2923  O   GLN B 707     -90.683 -12.406 -13.220  1.00 46.92           O  
-ANISOU 2923  O   GLN B 707     6344   6411   5072  -1237   -481    321       O  
-ATOM   2924  CB  GLN B 707     -87.414 -13.003 -13.268  1.00 58.53           C  
-ANISOU 2924  CB  GLN B 707     7947   7680   6613  -1100   -351    162       C  
-ATOM   2925  CG  GLN B 707     -87.576 -11.940 -14.335  1.00 63.63           C  
-ANISOU 2925  CG  GLN B 707     8561   8400   7214  -1100   -344    197       C  
-ATOM   2926  CD  GLN B 707     -86.523 -12.078 -15.414  1.00 65.15           C  
-ANISOU 2926  CD  GLN B 707     8822   8559   7373  -1089   -294    135       C  
-ATOM   2927  OE1 GLN B 707     -86.499 -13.077 -16.140  1.00 66.42           O  
-ANISOU 2927  OE1 GLN B 707     9069   8694   7474  -1146   -300     83       O  
-ATOM   2928  NE2 GLN B 707     -85.689 -11.075 -15.566  1.00 64.66           N  
-ANISOU 2928  NE2 GLN B 707     8726   8499   7344  -1020   -244    140       N  
-ATOM   2929  N   ALA B 708     -90.163 -14.573 -13.525  1.00 50.78           N  
-ANISOU 2929  N   ALA B 708     6993   6784   5518  -1318   -486    215       N  
-ATOM   2930  CA  ALA B 708     -91.403 -14.877 -14.257  1.00 52.41           C  
-ANISOU 2930  CA  ALA B 708     7201   7065   5649  -1423   -548    246       C  
-ATOM   2931  C   ALA B 708     -92.606 -14.781 -13.333  1.00 50.98           C  
-ANISOU 2931  C   ALA B 708     6937   6940   5492  -1456   -592    315       C  
-ATOM   2932  O   ALA B 708     -93.687 -14.376 -13.748  1.00 51.97           O  
-ANISOU 2932  O   ALA B 708     7004   7160   5582  -1507   -638    372       O  
-ATOM   2933  CB  ALA B 708     -91.332 -16.265 -14.913  1.00 53.16           C  
-ANISOU 2933  CB  ALA B 708     7412   7101   5684  -1506   -564    178       C  
-ATOM   2934  N   ALA B 709     -92.416 -15.171 -12.076  1.00 48.35           N  
-ANISOU 2934  N   ALA B 709     6599   6553   5221  -1427   -577    311       N  
-ATOM   2935  CA  ALA B 709     -93.466 -15.050 -11.066  1.00 48.80           C  
-ANISOU 2935  CA  ALA B 709     6575   6662   5306  -1451   -605    374       C  
-ATOM   2936  C   ALA B 709     -93.831 -13.578 -10.794  1.00 47.45           C  
-ANISOU 2936  C   ALA B 709     6287   6573   5170  -1383   -595    439       C  
-ATOM   2937  O   ALA B 709     -95.010 -13.231 -10.675  1.00 48.83           O  
-ANISOU 2937  O   ALA B 709     6381   6835   5336  -1421   -630    501       O  
-ATOM   2938  CB  ALA B 709     -93.044 -15.748  -9.791  1.00 48.56           C  
-ANISOU 2938  CB  ALA B 709     6574   6549   5328  -1428   -586    353       C  
-ATOM   2939  N   TYR B 710     -92.828 -12.709 -10.746  1.00 46.96           N  
-ANISOU 2939  N   TYR B 710     6213   6482   5146  -1285   -546    425       N  
-ATOM   2940  CA  TYR B 710     -93.075 -11.268 -10.629  1.00 48.48           C  
-ANISOU 2940  CA  TYR B 710     6308   6741   5370  -1219   -534    481       C  
-ATOM   2941  C   TYR B 710     -93.954 -10.786 -11.759  1.00 47.63           C  
-ANISOU 2941  C   TYR B 710     6164   6725   5207  -1266   -575    528       C  
-ATOM   2942  O   TYR B 710     -94.921 -10.060 -11.530  1.00 48.66           O  
-ANISOU 2942  O   TYR B 710     6201   6936   5352  -1261   -598    595       O  
-ATOM   2943  CB  TYR B 710     -91.770 -10.459 -10.647  1.00 47.65           C  
-ANISOU 2943  CB  TYR B 710     6213   6586   5308  -1120   -477    452       C  
-ATOM   2944  CG  TYR B 710     -91.048 -10.323  -9.331  1.00 45.91           C  
-ANISOU 2944  CG  TYR B 710     5979   6304   5159  -1047   -439    434       C  
-ATOM   2945  CD1 TYR B 710     -91.652  -9.734  -8.231  1.00 43.81           C  
-ANISOU 2945  CD1 TYR B 710     5635   6073   4937  -1016   -439    479       C  
-ATOM   2946  CD2 TYR B 710     -89.728 -10.731  -9.215  1.00 47.76           C  
-ANISOU 2946  CD2 TYR B 710     6279   6449   5418  -1004   -403    370       C  
-ATOM   2947  CE1 TYR B 710     -90.980  -9.591  -7.048  1.00 44.01           C  
-ANISOU 2947  CE1 TYR B 710     5655   6046   5019   -953   -408    460       C  
-ATOM   2948  CE2 TYR B 710     -89.046 -10.609  -8.025  1.00 44.39           C  
-ANISOU 2948  CE2 TYR B 710     5841   5970   5055   -939   -376    355       C  
-ATOM   2949  CZ  TYR B 710     -89.676 -10.039  -6.955  1.00 44.80           C  
-ANISOU 2949  CZ  TYR B 710     5822   6058   5140   -917   -381    400       C  
-ATOM   2950  OH  TYR B 710     -88.999  -9.890  -5.788  1.00 44.81           O  
-ANISOU 2950  OH  TYR B 710     5817   6011   5197   -856   -357    384       O  
-ATOM   2951  N   SER B 711     -93.597 -11.172 -12.982  1.00 49.59           N  
-ANISOU 2951  N   SER B 711     6487   6963   5392  -1307   -584    493       N  
-ATOM   2952  CA  SER B 711     -94.346 -10.753 -14.155  1.00 53.42           C  
-ANISOU 2952  CA  SER B 711     6949   7534   5812  -1356   -628    536       C  
-ATOM   2953  C   SER B 711     -95.781 -11.192 -14.057  1.00 49.99           C  
-ANISOU 2953  C   SER B 711     6466   7175   5352  -1443   -695    583       C  
-ATOM   2954  O   SER B 711     -96.660 -10.406 -14.327  1.00 49.95           O  
-ANISOU 2954  O   SER B 711     6376   7260   5342  -1445   -729    652       O  
-ATOM   2955  CB  SER B 711     -93.736 -11.305 -15.452  1.00 55.50           C  
-ANISOU 2955  CB  SER B 711     7318   7771   5999  -1400   -627    480       C  
-ATOM   2956  OG  SER B 711     -92.455 -10.753 -15.655  1.00 57.87           O  
-ANISOU 2956  OG  SER B 711     7649   8016   6322  -1319   -563    445       O  
-ATOM   2957  N   ILE B 712     -96.010 -12.439 -13.667  1.00 48.06           N  
-ANISOU 2957  N   ILE B 712     6271   6893   5095  -1516   -712    548       N  
-ATOM   2958  CA  ILE B 712     -97.368 -12.944 -13.532  1.00 49.68           C  
-ANISOU 2958  CA  ILE B 712     6429   7168   5278  -1610   -774    591       C  
-ATOM   2959  C   ILE B 712     -98.147 -12.137 -12.524  1.00 49.12           C  
-ANISOU 2959  C   ILE B 712     6232   7161   5271  -1565   -771    662       C  
-ATOM   2960  O   ILE B 712     -99.284 -11.786 -12.756  1.00 51.77           O  
-ANISOU 2960  O   ILE B 712     6482   7594   5593  -1604   -818    724       O  
-ATOM   2961  CB  ILE B 712     -97.394 -14.443 -13.182  1.00 51.45           C  
-ANISOU 2961  CB  ILE B 712     6737   7326   5485  -1695   -787    541       C  
-ATOM   2962  CG1 ILE B 712     -96.943 -15.251 -14.403  1.00 54.03           C  
-ANISOU 2962  CG1 ILE B 712     7183   7611   5734  -1760   -803    476       C  
-ATOM   2963  CG2 ILE B 712     -98.779 -14.897 -12.726  1.00 52.71           C  
-ANISOU 2963  CG2 ILE B 712     6832   7555   5641  -1786   -840    591       C  
-ATOM   2964  CD1 ILE B 712     -96.689 -16.705 -14.095  1.00 57.94           C  
-ANISOU 2964  CD1 ILE B 712     7782   8012   6220  -1825   -804    413       C  
-ATOM   2965  N   LEU B 713     -97.536 -11.819 -11.398  1.00 48.75           N  
-ANISOU 2965  N   LEU B 713     6169   7061   5293  -1481   -716    651       N  
-ATOM   2966  CA  LEU B 713     -98.201 -10.949 -10.410  1.00 48.59           C  
-ANISOU 2966  CA  LEU B 713     6032   7098   5334  -1427   -703    711       C  
-ATOM   2967  C   LEU B 713     -98.537  -9.568 -10.970  1.00 46.66           C  
-ANISOU 2967  C   LEU B 713     5702   6928   5099  -1367   -709    768       C  
-ATOM   2968  O   LEU B 713     -99.561  -8.976 -10.622  1.00 43.96           O  
-ANISOU 2968  O   LEU B 713     5252   6667   4783  -1359   -726    831       O  
-ATOM   2969  CB  LEU B 713     -97.335 -10.823  -9.140  1.00 49.41           C  
-ANISOU 2969  CB  LEU B 713     6149   7124   5502  -1345   -641    681       C  
-ATOM   2970  CG  LEU B 713     -97.222 -12.100  -8.299  1.00 49.44           C  
-ANISOU 2970  CG  LEU B 713     6216   7064   5507  -1398   -638    645       C  
-ATOM   2971  CD1 LEU B 713     -96.336 -11.854  -7.083  1.00 51.53           C  
-ANISOU 2971  CD1 LEU B 713     6490   7259   5830  -1310   -583    621       C  
-ATOM   2972  CD2 LEU B 713     -98.595 -12.591  -7.885  1.00 47.11           C  
-ANISOU 2972  CD2 LEU B 713     5859   6840   5199  -1485   -676    692       C  
-ATOM   2973  N   SER B 714     -97.674  -9.061 -11.845  1.00 48.30           N  
-ANISOU 2973  N   SER B 714     5958   7106   5288  -1325   -694    747       N  
-ATOM   2974  CA  SER B 714     -97.932  -7.791 -12.526  1.00 52.99           C  
-ANISOU 2974  CA  SER B 714     6488   7762   5884  -1274   -704    804       C  
-ATOM   2975  C   SER B 714     -99.088  -7.931 -13.472  1.00 49.68           C  
-ANISOU 2975  C   SER B 714     6031   7439   5405  -1357   -780    855       C  
-ATOM   2976  O   SER B 714     -99.908  -7.042 -13.549  1.00 47.99           O  
-ANISOU 2976  O   SER B 714     5718   7303   5211  -1329   -804    926       O  
-ATOM   2977  CB  SER B 714     -96.712  -7.280 -13.323  1.00 54.15           C  
-ANISOU 2977  CB  SER B 714     6704   7855   6016  -1222   -669    772       C  
-ATOM   2978  OG  SER B 714     -95.792  -6.696 -12.433  1.00 58.24           O  
-ANISOU 2978  OG  SER B 714     7217   8306   6604  -1127   -604    748       O  
-ATOM   2979  N   GLU B 715     -99.138  -9.043 -14.204  1.00 53.24           N  
-ANISOU 2979  N   GLU B 715     6562   7883   5782  -1458   -818    818       N  
-ATOM   2980  CA  GLU B 715    -100.257  -9.313 -15.125  1.00 54.05           C  
-ANISOU 2980  CA  GLU B 715     6637   8079   5819  -1554   -899    861       C  
-ATOM   2981  C   GLU B 715    -101.543  -9.422 -14.338  1.00 52.58           C  
-ANISOU 2981  C   GLU B 715     6341   7968   5671  -1589   -932    915       C  
-ATOM   2982  O   GLU B 715    -102.556  -8.924 -14.759  1.00 50.91           O  
-ANISOU 2982  O   GLU B 715     6038   7855   5449  -1608   -986    984       O  
-ATOM   2983  CB  GLU B 715    -100.025 -10.568 -15.963  1.00 56.45           C  
-ANISOU 2983  CB  GLU B 715     7060   8352   6038  -1661   -930    799       C  
-ATOM   2984  CG  GLU B 715     -98.878 -10.426 -16.967  1.00 63.18           C  
-ANISOU 2984  CG  GLU B 715     8016   9150   6840  -1636   -901    750       C  
-ATOM   2985  CD  GLU B 715     -98.618 -11.669 -17.827  1.00 74.62           C  
-ANISOU 2985  CD  GLU B 715     9590  10563   8201  -1738   -924    679       C  
-ATOM   2986  OE1 GLU B 715     -99.433 -12.619 -17.806  1.00 81.03           O  
-ANISOU 2986  OE1 GLU B 715    10408  11397   8980  -1842   -977    675       O  
-ATOM   2987  OE2 GLU B 715     -97.591 -11.692 -18.544  1.00 80.35           O  
-ANISOU 2987  OE2 GLU B 715    10408  11235   8887  -1717   -887    626       O  
-ATOM   2988  N   VAL B 716    -101.496 -10.043 -13.165  1.00 53.36           N  
-ANISOU 2988  N   VAL B 716     6442   8022   5813  -1594   -898    887       N  
-ATOM   2989  CA  VAL B 716    -102.680 -10.114 -12.311  1.00 56.66           C  
-ANISOU 2989  CA  VAL B 716     6749   8509   6268  -1623   -915    938       C  
-ATOM   2990  C   VAL B 716    -103.196  -8.713 -11.964  1.00 56.49           C  
-ANISOU 2990  C   VAL B 716     6598   8557   6309  -1525   -901   1009       C  
-ATOM   2991  O   VAL B 716    -104.378  -8.435 -12.101  1.00 60.30           O  
-ANISOU 2991  O   VAL B 716     6974   9142   6797  -1553   -948   1074       O  
-ATOM   2992  CB  VAL B 716    -102.393 -10.897 -11.015  1.00 57.60           C  
-ANISOU 2992  CB  VAL B 716     6901   8559   6425  -1630   -868    898       C  
-ATOM   2993  CG1 VAL B 716    -103.515 -10.706 -10.015  1.00 59.91           C  
-ANISOU 2993  CG1 VAL B 716     7070   8928   6766  -1636   -866    954       C  
-ATOM   2994  CG2 VAL B 716    -102.199 -12.381 -11.323  1.00 61.18           C  
-ANISOU 2994  CG2 VAL B 716     7468   8955   6821  -1743   -895    841       C  
-ATOM   2995  N   GLN B 717    -102.297  -7.844 -11.529  1.00 57.76           N  
-ANISOU 2995  N   GLN B 717     6768   8659   6519  -1410   -838    994       N  
-ATOM   2996  CA  GLN B 717    -102.650  -6.489 -11.139  1.00 62.05           C  
-ANISOU 2996  CA  GLN B 717     7202   9246   7126  -1307   -816   1051       C  
-ATOM   2997  C   GLN B 717    -103.220  -5.723 -12.334  1.00 64.75           C  
-ANISOU 2997  C   GLN B 717     7493   9667   7441  -1304   -874   1115       C  
-ATOM   2998  O   GLN B 717    -104.222  -5.038 -12.195  1.00 68.41           O  
-ANISOU 2998  O   GLN B 717     7838  10214   7942  -1276   -896   1183       O  
-ATOM   2999  CB  GLN B 717    -101.428  -5.746 -10.570  1.00 65.42           C  
-ANISOU 2999  CB  GLN B 717     7670   9583   7603  -1194   -740   1014       C  
-ATOM   3000  CG  GLN B 717    -101.723  -4.323 -10.106  1.00 67.81           C  
-ANISOU 3000  CG  GLN B 717     7872   9916   7977  -1084   -711   1064       C  
-ATOM   3001  CD  GLN B 717    -100.620  -3.334 -10.408  1.00 75.45           C  
-ANISOU 3001  CD  GLN B 717     8883  10817   8966   -991   -671   1050       C  
-ATOM   3002  OE1 GLN B 717     -99.698  -3.160  -9.612  1.00 80.93           O  
-ANISOU 3002  OE1 GLN B 717     9616  11433   9699   -933   -611   1003       O  
-ATOM   3003  NE2 GLN B 717    -100.734  -2.641 -11.545  1.00 79.25           N  
-ANISOU 3003  NE2 GLN B 717     9355  11334   9424   -979   -707   1095       N  
-ATOM   3004  N   GLN B 718    -102.591  -5.864 -13.501  1.00 62.93           N  
-ANISOU 3004  N   GLN B 718     7353   9411   7145  -1332   -898   1093       N  
-ATOM   3005  CA  GLN B 718    -103.096  -5.257 -14.753  1.00 63.48           C  
-ANISOU 3005  CA  GLN B 718     7393   9556   7171  -1344   -963   1155       C  
-ATOM   3006  C   GLN B 718    -104.487  -5.799 -15.126  1.00 63.10           C  
-ANISOU 3006  C   GLN B 718     7271   9617   7088  -1445  -1048   1204       C  
-ATOM   3007  O   GLN B 718    -105.380  -5.019 -15.437  1.00 64.63           O  
-ANISOU 3007  O   GLN B 718     7359   9898   7299  -1420  -1093   1283       O  
-ATOM   3008  CB  GLN B 718    -102.120  -5.453 -15.926  1.00 57.26           C  
-ANISOU 3008  CB  GLN B 718     6730   8720   6306  -1370   -967   1114       C  
-ATOM   3009  N   ALA B 719    -104.690  -7.114 -15.021  1.00 59.77           N  
-ANISOU 3009  N   ALA B 719     6898   9188   6624  -1555  -1070   1160       N  
-ATOM   3010  CA  ALA B 719    -106.004  -7.711 -15.304  1.00 61.52           C  
-ANISOU 3010  CA  ALA B 719     7049   9512   6815  -1664  -1151   1203       C  
-ATOM   3011  C   ALA B 719    -107.062  -7.195 -14.340  1.00 60.63           C  
-ANISOU 3011  C   ALA B 719     6780   9474   6784  -1624  -1144   1265       C  
-ATOM   3012  O   ALA B 719    -108.159  -6.894 -14.747  1.00 61.55           O  
-ANISOU 3012  O   ALA B 719     6790   9697   6899  -1650  -1209   1336       O  
-ATOM   3013  CB  ALA B 719    -105.940  -9.231 -15.255  1.00 59.49           C  
-ANISOU 3013  CB  ALA B 719     6882   9214   6505  -1789  -1166   1137       C  
-ATOM   3014  N   VAL B 720    -106.733  -7.094 -13.061  1.00 62.37           N  
-ANISOU 3014  N   VAL B 720     6985   9640   7072  -1560  -1065   1240       N  
-ATOM   3015  CA  VAL B 720    -107.664  -6.523 -12.101  1.00 65.23           C  
-ANISOU 3015  CA  VAL B 720     7202  10069   7512  -1510  -1044   1293       C  
-ATOM   3016  C   VAL B 720    -107.974  -5.075 -12.497  1.00 67.32           C  
-ANISOU 3016  C   VAL B 720     7373  10387   7819  -1403  -1055   1363       C  
-ATOM   3017  O   VAL B 720    -109.131  -4.692 -12.611  1.00 69.08           O  
-ANISOU 3017  O   VAL B 720     7467  10715   8067  -1406  -1100   1435       O  
-ATOM   3018  CB  VAL B 720    -107.122  -6.637 -10.652  1.00 69.08           C  
-ANISOU 3018  CB  VAL B 720     7708  10482   8056  -1456   -952   1247       C  
-ATOM   3019  CG1 VAL B 720    -107.965  -5.813  -9.689  1.00 68.07           C  
-ANISOU 3019  CG1 VAL B 720     7434  10419   8009  -1381   -916   1298       C  
-ATOM   3020  CG2 VAL B 720    -107.079  -8.106 -10.193  1.00 69.83           C  
-ANISOU 3020  CG2 VAL B 720     7876  10540   8116  -1570   -951   1196       C  
-ATOM   3021  N   SER B 721    -106.930  -4.283 -12.724  1.00 70.76           N  
-ANISOU 3021  N   SER B 721     7875  10748   8265  -1309  -1015   1345       N  
-ATOM   3022  CA  SER B 721    -107.060  -2.885 -13.148  1.00 72.22           C  
-ANISOU 3022  CA  SER B 721     7994  10960   8488  -1204  -1022   1409       C  
-ATOM   3023  C   SER B 721    -107.757  -2.704 -14.497  1.00 71.65           C  
-ANISOU 3023  C   SER B 721     7888  10976   8361  -1252  -1120   1476       C  
-ATOM   3024  O   SER B 721    -108.667  -1.883 -14.619  1.00 66.69           O  
-ANISOU 3024  O   SER B 721     7136  10428   7775  -1203  -1155   1555       O  
-ATOM   3025  CB  SER B 721    -105.680  -2.237 -13.218  1.00 71.27           C  
-ANISOU 3025  CB  SER B 721     7972  10731   8377  -1117   -961   1367       C  
-ATOM   3026  N   ASP B 726    -111.626 -12.126 -15.673  1.00 70.26           N  
-ANISOU 3026  N   ASP B 726     7895  11010   7791  -2328  -1495   1306       N  
-ATOM   3027  CA  ASP B 726    -112.373 -12.879 -14.653  1.00 71.52           C  
-ANISOU 3027  CA  ASP B 726     7991  11193   7992  -2404  -1480   1312       C  
-ATOM   3028  C   ASP B 726    -112.043 -14.385 -14.643  1.00 72.88           C  
-ANISOU 3028  C   ASP B 726     8303  11280   8107  -2538  -1487   1236       C  
-ATOM   3029  O   ASP B 726    -111.532 -14.940 -13.660  1.00 69.43           O  
-ANISOU 3029  O   ASP B 726     7927  10754   7701  -2531  -1416   1191       O  
-ATOM   3030  CB  ASP B 726    -113.874 -12.658 -14.824  1.00 73.45           C  
-ANISOU 3030  CB  ASP B 726     8060  11593   8256  -2463  -1556   1398       C  
-ATOM   3031  N   SER B 727    -112.398 -15.047 -15.743  1.00 77.88           N  
-ANISOU 3031  N   SER B 727     8987  11947   8658  -2665  -1578   1225       N  
-ATOM   3032  CA  SER B 727    -111.837 -16.364 -16.104  1.00 74.42           C  
-ANISOU 3032  CA  SER B 727     8719  11408   8149  -2779  -1591   1139       C  
-ATOM   3033  C   SER B 727    -110.317 -16.254 -16.296  1.00 69.86           C  
-ANISOU 3033  C   SER B 727     8296  10697   7551  -2684  -1524   1065       C  
-ATOM   3034  O   SER B 727    -109.583 -17.151 -15.904  1.00 65.10           O  
-ANISOU 3034  O   SER B 727     7819   9977   6941  -2711  -1479    992       O  
-ATOM   3035  CB  SER B 727    -112.482 -16.908 -17.395  1.00 72.94           C  
-ANISOU 3035  CB  SER B 727     8556  11289   7868  -2922  -1706   1141       C  
-ATOM   3036  N   GLN B 728    -109.871 -15.152 -16.908  1.00 68.18           N  
-ANISOU 3036  N   GLN B 728     8070  10505   7331  -2576  -1519   1086       N  
-ATOM   3037  CA  GLN B 728    -108.458 -14.902 -17.188  1.00 67.35           C  
-ANISOU 3037  CA  GLN B 728     8094  10289   7208  -2483  -1456   1023       C  
-ATOM   3038  C   GLN B 728    -107.634 -14.733 -15.901  1.00 69.81           C  
-ANISOU 3038  C   GLN B 728     8420  10504   7601  -2374  -1350    995       C  
-ATOM   3039  O   GLN B 728    -106.528 -15.265 -15.778  1.00 64.70           O  
-ANISOU 3039  O   GLN B 728     7904   9736   6942  -2354  -1298    918       O  
-ATOM   3040  CB  GLN B 728    -108.293 -13.693 -18.134  1.00 64.54           C  
-ANISOU 3040  CB  GLN B 728     7706   9989   6827  -2401  -1479   1066       C  
-ATOM   3041  CG  GLN B 728    -108.667 -14.050 -19.560  1.00 63.56           C  
-ANISOU 3041  CG  GLN B 728     7633   9923   6595  -2511  -1576   1065       C  
-ATOM   3042  CD  GLN B 728    -108.576 -12.855 -20.476  1.00 62.09           C  
-ANISOU 3042  CD  GLN B 728     7413   9798   6380  -2434  -1603   1119       C  
-ATOM   3043  OE1 GLN B 728    -109.299 -11.880 -20.306  1.00 62.48           O  
-ANISOU 3043  OE1 GLN B 728     7320   9939   6482  -2373  -1627   1207       O  
-ATOM   3044  NE2 GLN B 728    -107.701 -12.931 -21.471  1.00 61.22           N  
-ANISOU 3044  NE2 GLN B 728     7437   9637   6187  -2438  -1600   1067       N  
-ATOM   3045  N   ILE B 729    -108.198 -14.015 -14.941  1.00 70.22           N  
-ANISOU 3045  N   ILE B 729     8335  10612   7735  -2305  -1321   1056       N  
-ATOM   3046  CA  ILE B 729    -107.517 -13.773 -13.670  1.00 66.55           C  
-ANISOU 3046  CA  ILE B 729     7872  10069   7344  -2203  -1225   1036       C  
-ATOM   3047  C   ILE B 729    -107.438 -15.065 -12.824  1.00 63.88           C  
-ANISOU 3047  C   ILE B 729     7604   9656   7011  -2286  -1201    989       C  
-ATOM   3048  O   ILE B 729    -106.452 -15.299 -12.126  1.00 57.22           O  
-ANISOU 3048  O   ILE B 729     6844   8704   6194  -2228  -1134    938       O  
-ATOM   3049  CB  ILE B 729    -108.041 -12.517 -12.905  1.00 66.96           C  
-ANISOU 3049  CB  ILE B 729     7768  10196   7480  -2091  -1191   1108       C  
-ATOM   3050  CG1 ILE B 729    -108.434 -12.850 -11.473  1.00 68.68           C  
-ANISOU 3050  CG1 ILE B 729     7928  10409   7759  -2095  -1140   1116       C  
-ATOM   3051  CG2 ILE B 729    -109.231 -11.869 -13.590  1.00 71.21           C  
-ANISOU 3051  CG2 ILE B 729     8171  10873   8013  -2113  -1266   1191       C  
-ATOM   3052  CD1 ILE B 729    -108.822 -11.608 -10.721  1.00 70.36           C  
-ANISOU 3052  CD1 ILE B 729     8003  10682   8050  -1976  -1095   1174       C  
-ATOM   3053  N   LEU B 730    -108.439 -15.929 -12.938  1.00 64.04           N  
-ANISOU 3053  N   LEU B 730     7599   9731   7004  -2424  -1262   1006       N  
-ATOM   3054  CA  LEU B 730    -108.323 -17.285 -12.384  1.00 65.71           C  
-ANISOU 3054  CA  LEU B 730     7904   9860   7204  -2523  -1251    958       C  
-ATOM   3055  C   LEU B 730    -107.120 -18.020 -12.992  1.00 65.42           C  
-ANISOU 3055  C   LEU B 730     8052   9692   7115  -2534  -1241    867       C  
-ATOM   3056  O   LEU B 730    -106.328 -18.628 -12.276  1.00 60.20           O  
-ANISOU 3056  O   LEU B 730     7483   8916   6475  -2512  -1187    817       O  
-ATOM   3057  CB  LEU B 730    -109.600 -18.094 -12.630  1.00 64.93           C  
-ANISOU 3057  CB  LEU B 730     7753   9842   7074  -2686  -1328    989       C  
-ATOM   3058  N   ASP B 731    -106.993 -17.976 -14.318  1.00 68.67           N  
-ANISOU 3058  N   ASP B 731     8516  10121   7456  -2566  -1293    846       N  
-ATOM   3059  CA  ASP B 731    -105.880 -18.650 -15.000  1.00 69.54           C  
-ANISOU 3059  CA  ASP B 731     8798  10114   7511  -2576  -1280    756       C  
-ATOM   3060  C   ASP B 731    -104.523 -18.061 -14.591  1.00 68.04           C  
-ANISOU 3060  C   ASP B 731     8658   9831   7363  -2425  -1192    719       C  
-ATOM   3061  O   ASP B 731    -103.559 -18.802 -14.463  1.00 65.25           O  
-ANISOU 3061  O   ASP B 731     8432   9356   7005  -2418  -1154    646       O  
-ATOM   3062  CB  ASP B 731    -106.025 -18.629 -16.529  1.00 69.51           C  
-ANISOU 3062  CB  ASP B 731     8838  10159   7415  -2639  -1349    743       C  
-ATOM   3063  CG  ASP B 731    -104.784 -19.214 -17.250  1.00 69.46           C  
-ANISOU 3063  CG  ASP B 731     9009  10032   7352  -2632  -1321    644       C  
-ATOM   3064  OD1 ASP B 731    -104.519 -20.429 -17.074  1.00 70.04           O  
-ANISOU 3064  OD1 ASP B 731     9193  10009   7410  -2707  -1315    580       O  
-ATOM   3065  OD2 ASP B 731    -104.080 -18.470 -17.990  1.00 66.24           O  
-ANISOU 3065  OD2 ASP B 731     8629   9625   6916  -2553  -1301    631       O  
-ATOM   3066  N   LEU B 732    -104.462 -16.745 -14.379  1.00 63.50           N  
-ANISOU 3066  N   LEU B 732     7982   9312   6833  -2307  -1163    770       N  
-ATOM   3067  CA  LEU B 732    -103.224 -16.100 -13.967  1.00 62.31           C  
-ANISOU 3067  CA  LEU B 732     7867   9082   6727  -2168  -1083    740       C  
-ATOM   3068  C   LEU B 732    -102.854 -16.549 -12.567  1.00 62.57           C  
-ANISOU 3068  C   LEU B 732     7913   9035   6824  -2135  -1025    722       C  
-ATOM   3069  O   LEU B 732    -101.704 -16.880 -12.324  1.00 61.94           O  
-ANISOU 3069  O   LEU B 732     7934   8844   6756  -2083   -976    660       O  
-ATOM   3070  CB  LEU B 732    -103.314 -14.567 -14.054  1.00 60.69           C  
-ANISOU 3070  CB  LEU B 732     7550   8953   6557  -2056  -1069    802       C  
-ATOM   3071  CG  LEU B 732    -103.376 -14.028 -15.481  1.00 61.79           C  
-ANISOU 3071  CG  LEU B 732     7698   9151   6630  -2067  -1118    817       C  
-ATOM   3072  CD1 LEU B 732    -103.759 -12.555 -15.485  1.00 62.30           C  
-ANISOU 3072  CD1 LEU B 732     7635   9301   6736  -1970  -1117    896       C  
-ATOM   3073  CD2 LEU B 732    -102.079 -14.257 -16.248  1.00 60.19           C  
-ANISOU 3073  CD2 LEU B 732     7636   8855   6380  -2041  -1084    740       C  
-ATOM   3074  N   SER B 733    -103.832 -16.582 -11.666  1.00 60.04           N  
-ANISOU 3074  N   SER B 733     7494   8775   6542  -2168  -1033    776       N  
-ATOM   3075  CA  SER B 733    -103.618 -17.126 -10.326  1.00 61.02           C  
-ANISOU 3075  CA  SER B 733     7636   8832   6715  -2158   -985    765       C  
-ATOM   3076  C   SER B 733    -102.970 -18.514 -10.387  1.00 62.05           C  
-ANISOU 3076  C   SER B 733     7921   8841   6815  -2228   -986    692       C  
-ATOM   3077  O   SER B 733    -101.995 -18.791  -9.691  1.00 61.54           O  
-ANISOU 3077  O   SER B 733     7928   8671   6781  -2166   -934    651       O  
-ATOM   3078  CB  SER B 733    -104.949 -17.228  -9.564  1.00 61.96           C  
-ANISOU 3078  CB  SER B 733     7638   9044   6859  -2225  -1003    831       C  
-ATOM   3079  OG  SER B 733    -104.937 -16.471  -8.378  1.00 62.16           O  
-ANISOU 3079  OG  SER B 733     7581   9086   6951  -2128   -943    864       O  
-ATOM   3080  N   ASN B 734    -103.549 -19.381 -11.212  1.00 62.21           N  
-ANISOU 3080  N   ASN B 734     7988   8875   6775  -2358  -1049    678       N  
-ATOM   3081  CA  ASN B 734    -103.091 -20.752 -11.339  1.00 61.16           C  
-ANISOU 3081  CA  ASN B 734     8000   8627   6610  -2438  -1057    610       C  
-ATOM   3082  C   ASN B 734    -101.739 -20.831 -11.985  1.00 58.37           C  
-ANISOU 3082  C   ASN B 734     7770   8171   6238  -2369  -1025    532       C  
-ATOM   3083  O   ASN B 734    -100.941 -21.673 -11.614  1.00 60.68           O  
-ANISOU 3083  O   ASN B 734     8172   8341   6542  -2362   -996    476       O  
-ATOM   3084  CB  ASN B 734    -104.088 -21.590 -12.150  1.00 65.40           C  
-ANISOU 3084  CB  ASN B 734     8555   9210   7083  -2601  -1137    612       C  
-ATOM   3085  CG  ASN B 734    -105.411 -21.778 -11.432  1.00 66.20           C  
-ANISOU 3085  CG  ASN B 734     8546   9399   7207  -2690  -1167    683       C  
-ATOM   3086  OD1 ASN B 734    -105.479 -21.746 -10.199  1.00 67.05           O  
-ANISOU 3086  OD1 ASN B 734     8610   9494   7371  -2655  -1122    713       O  
-ATOM   3087  ND2 ASN B 734    -106.473 -21.972 -12.199  1.00 71.06           N  
-ANISOU 3087  ND2 ASN B 734     9114  10110   7776  -2808  -1242    711       N  
-ATOM   3088  N   ARG B 735    -101.460 -19.943 -12.930  1.00 58.32           N  
-ANISOU 3088  N   ARG B 735     7742   8213   6203  -2313  -1028    531       N  
-ATOM   3089  CA  ARG B 735    -100.145 -19.909 -13.550  1.00 61.49           C  
-ANISOU 3089  CA  ARG B 735     8248   8527   6588  -2241   -988    459       C  
-ATOM   3090  C   ARG B 735     -99.103 -19.580 -12.466  1.00 65.90           C  
-ANISOU 3090  C   ARG B 735     8811   9005   7224  -2113   -913    445       C  
-ATOM   3091  O   ARG B 735     -98.018 -20.158 -12.435  1.00 62.80           O  
-ANISOU 3091  O   ARG B 735     8525   8497   6839  -2076   -875    377       O  
-ATOM   3092  CB  ARG B 735    -100.102 -18.879 -14.694  1.00 63.30           C  
-ANISOU 3092  CB  ARG B 735     8441   8836   6774  -2203  -1002    475       C  
-ATOM   3093  N   PHE B 736     -99.444 -18.661 -11.565  1.00 67.01           N  
-ANISOU 3093  N   PHE B 736     8833   9206   7421  -2045   -891    509       N  
-ATOM   3094  CA  PHE B 736     -98.541 -18.292 -10.489  1.00 64.99           C  
-ANISOU 3094  CA  PHE B 736     8575   8885   7235  -1931   -827    500       C  
-ATOM   3095  C   PHE B 736     -98.248 -19.490  -9.595  1.00 65.46           C  
-ANISOU 3095  C   PHE B 736     8716   8840   7314  -1965   -816    468       C  
-ATOM   3096  O   PHE B 736     -97.093 -19.777  -9.304  1.00 61.62           O  
-ANISOU 3096  O   PHE B 736     8308   8249   6854  -1898   -776    416       O  
-ATOM   3097  CB  PHE B 736     -99.104 -17.139  -9.644  1.00 63.63           C  
-ANISOU 3097  CB  PHE B 736     8262   8800   7114  -1865   -809    572       C  
-ATOM   3098  CG  PHE B 736     -98.223 -16.761  -8.492  1.00 62.80           C  
-ANISOU 3098  CG  PHE B 736     8155   8631   7074  -1755   -747    562       C  
-ATOM   3099  CD1 PHE B 736     -97.151 -15.887  -8.685  1.00 60.78           C  
-ANISOU 3099  CD1 PHE B 736     7906   8345   6844  -1642   -704    537       C  
-ATOM   3100  CD2 PHE B 736     -98.448 -17.271  -7.235  1.00 60.78           C  
-ANISOU 3100  CD2 PHE B 736     7894   8348   6850  -1770   -734    577       C  
-ATOM   3101  CE1 PHE B 736     -96.334 -15.531  -7.640  1.00 58.29           C  
-ANISOU 3101  CE1 PHE B 736     7587   7973   6586  -1547   -654    526       C  
-ATOM   3102  CE2 PHE B 736     -97.626 -16.920  -6.185  1.00 60.26           C  
-ANISOU 3102  CE2 PHE B 736     7831   8227   6837  -1673   -683    567       C  
-ATOM   3103  CZ  PHE B 736     -96.571 -16.045  -6.391  1.00 56.99           C  
-ANISOU 3103  CZ  PHE B 736     7420   7785   6450  -1561   -646    541       C  
-ATOM   3104  N   TYR B 737     -99.303 -20.167  -9.152  1.00 62.91           N  
-ANISOU 3104  N   TYR B 737     8371   8550   6982  -2070   -852    504       N  
-ATOM   3105  CA  TYR B 737     -99.167 -21.310  -8.248  1.00 61.63           C  
-ANISOU 3105  CA  TYR B 737     8284   8293   6839  -2114   -846    487       C  
-ATOM   3106  C   TYR B 737     -98.466 -22.501  -8.890  1.00 63.12           C  
-ANISOU 3106  C   TYR B 737     8626   8362   6996  -2160   -857    409       C  
-ATOM   3107  O   TYR B 737     -97.899 -23.333  -8.197  1.00 64.93           O  
-ANISOU 3107  O   TYR B 737     8938   8481   7251  -2153   -839    382       O  
-ATOM   3108  CB  TYR B 737    -100.526 -21.720  -7.701  1.00 58.65           C  
-ANISOU 3108  CB  TYR B 737     7843   7987   6456  -2226   -881    548       C  
-ATOM   3109  CG  TYR B 737    -101.095 -20.716  -6.725  1.00 59.06           C  
-ANISOU 3109  CG  TYR B 737     7756   8133   6551  -2169   -853    618       C  
-ATOM   3110  CD1 TYR B 737    -100.379 -20.354  -5.574  1.00 59.41           C  
-ANISOU 3110  CD1 TYR B 737     7797   8130   6647  -2066   -798    620       C  
-ATOM   3111  CD2 TYR B 737    -102.341 -20.125  -6.933  1.00 58.21           C  
-ANISOU 3111  CD2 TYR B 737     7520   8162   6434  -2216   -882    681       C  
-ATOM   3112  CE1 TYR B 737    -100.893 -19.447  -4.656  1.00 58.07           C  
-ANISOU 3112  CE1 TYR B 737     7508   8042   6513  -2014   -768    677       C  
-ATOM   3113  CE2 TYR B 737    -102.866 -19.213  -6.020  1.00 59.59           C  
-ANISOU 3113  CE2 TYR B 737     7569   8420   6652  -2158   -850    741       C  
-ATOM   3114  CZ  TYR B 737    -102.134 -18.882  -4.885  1.00 58.73           C  
-ANISOU 3114  CZ  TYR B 737     7468   8257   6589  -2059   -790    735       C  
-ATOM   3115  OH  TYR B 737    -102.635 -17.993  -3.977  1.00 59.94           O  
-ANISOU 3115  OH  TYR B 737     7505   8488   6781  -2002   -755    787       O  
-ATOM   3116  N   THR B 738     -98.466 -22.553 -10.212  1.00 63.82           N  
-ANISOU 3116  N   THR B 738     8754   8467   7028  -2199   -884    372       N  
-ATOM   3117  CA  THR B 738     -97.704 -23.554 -10.938  1.00 69.25           C  
-ANISOU 3117  CA  THR B 738     9588   9041   7684  -2227   -885    288       C  
-ATOM   3118  C   THR B 738     -96.223 -23.215 -10.924  1.00 66.99           C  
-ANISOU 3118  C   THR B 738     9350   8671   7433  -2092   -823    234       C  
-ATOM   3119  O   THR B 738     -95.398 -24.103 -10.799  1.00 65.91           O  
-ANISOU 3119  O   THR B 738     9322   8410   7310  -2077   -803    174       O  
-ATOM   3120  CB  THR B 738     -98.195 -23.661 -12.401  1.00 73.35           C  
-ANISOU 3120  CB  THR B 738    10134   9615   8121  -2316   -932    264       C  
-ATOM   3121  OG1 THR B 738     -99.542 -24.145 -12.402  1.00 76.73           O  
-ANISOU 3121  OG1 THR B 738    10525  10111   8518  -2454   -995    308       O  
-ATOM   3122  CG2 THR B 738     -97.321 -24.607 -13.230  1.00 72.19           C  
-ANISOU 3122  CG2 THR B 738    10143   9350   7936  -2333   -922    165       C  
-ATOM   3123  N   LEU B 739     -95.892 -21.937 -11.086  1.00 67.79           N  
-ANISOU 3123  N   LEU B 739     9368   8840   7550  -1995   -794    256       N  
-ATOM   3124  CA  LEU B 739     -94.502 -21.494 -11.052  1.00 72.50           C  
-ANISOU 3124  CA  LEU B 739     9993   9369   8184  -1868   -734    211       C  
-ATOM   3125  C   LEU B 739     -93.954 -21.592  -9.636  1.00 69.28           C  
-ANISOU 3125  C   LEU B 739     9578   8895   7852  -1794   -702    223       C  
-ATOM   3126  O   LEU B 739     -92.808 -21.936  -9.441  1.00 67.94           O  
-ANISOU 3126  O   LEU B 739     9475   8623   7715  -1724   -667    171       O  
-ATOM   3127  CB  LEU B 739     -94.368 -20.047 -11.525  1.00 72.57           C  
-ANISOU 3127  CB  LEU B 739     9910   9469   8193  -1791   -714    241       C  
-ATOM   3128  CG  LEU B 739     -93.257 -19.701 -12.494  1.00 74.48           C  
-ANISOU 3128  CG  LEU B 739    10203   9678   8418  -1726   -674    182       C  
-ATOM   3129  CD1 LEU B 739     -93.254 -20.565 -13.740  1.00 78.47           C  
-ANISOU 3129  CD1 LEU B 739    10815  10154   8846  -1809   -695    120       C  
-ATOM   3130  CD2 LEU B 739     -93.415 -18.238 -12.875  1.00 74.80           C  
-ANISOU 3130  CD2 LEU B 739    10142   9821   8456  -1670   -665    232       C  
-ATOM   3131  N   ILE B 740     -94.773 -21.236  -8.662  1.00 66.14           N  
-ANISOU 3131  N   ILE B 740     9091   8560   7479  -1808   -714    293       N  
-ATOM   3132  CA  ILE B 740     -94.363 -21.260  -7.277  1.00 65.49           C  
-ANISOU 3132  CA  ILE B 740     8997   8429   7457  -1745   -687    312       C  
-ATOM   3133  C   ILE B 740     -95.348 -22.177  -6.522  1.00 64.58           C  
-ANISOU 3133  C   ILE B 740     8893   8311   7334  -1850   -721    351       C  
-ATOM   3134  O   ILE B 740     -96.384 -21.729  -6.030  1.00 55.40           O  
-ANISOU 3134  O   ILE B 740     7635   7245   6170  -1887   -733    416       O  
-ATOM   3135  CB  ILE B 740     -94.351 -19.851  -6.665  1.00 63.44           C  
-ANISOU 3135  CB  ILE B 740     8619   8248   7236  -1652   -657    360       C  
-ATOM   3136  CG1 ILE B 740     -93.638 -18.850  -7.585  1.00 63.10           C  
-ANISOU 3136  CG1 ILE B 740     8553   8230   7192  -1572   -630    334       C  
-ATOM   3137  CG2 ILE B 740     -93.684 -19.893  -5.307  1.00 66.78           C  
-ANISOU 3137  CG2 ILE B 740     9048   8608   7716  -1578   -627    364       C  
-ATOM   3138  CD1 ILE B 740     -92.138 -19.032  -7.686  1.00 62.55           C  
-ANISOU 3138  CD1 ILE B 740     8558   8055   7152  -1486   -591    267       C  
-ATOM   3139  N   PRO B 741     -95.031 -23.476  -6.460  1.00 67.44           N  
-ANISOU 3139  N   PRO B 741     9372   8560   7690  -1900   -734    310       N  
-ATOM   3140  CA  PRO B 741     -95.950 -24.442  -5.860  1.00 71.24           C  
-ANISOU 3140  CA  PRO B 741     9879   9029   8159  -2014   -768    345       C  
-ATOM   3141  C   PRO B 741     -96.159 -24.194  -4.379  1.00 70.89           C  
-ANISOU 3141  C   PRO B 741     9777   9003   8155  -1983   -749    405       C  
-ATOM   3142  O   PRO B 741     -95.196 -23.986  -3.646  1.00 73.95           O  
-ANISOU 3142  O   PRO B 741    10181   9331   8587  -1881   -717    394       O  
-ATOM   3143  CB  PRO B 741     -95.287 -25.804  -6.098  1.00 71.27           C  
-ANISOU 3143  CB  PRO B 741    10034   8885   8160  -2046   -777    281       C  
-ATOM   3144  CG  PRO B 741     -94.054 -25.553  -6.886  1.00 73.20           C  
-ANISOU 3144  CG  PRO B 741    10327   9073   8413  -1949   -746    209       C  
-ATOM   3145  CD  PRO B 741     -93.787 -24.088  -6.955  1.00 70.41           C  
-ANISOU 3145  CD  PRO B 741     9863   8813   8075  -1850   -715    231       C  
-ATOM   3146  N   HIS B 742     -97.425 -24.191  -3.975  1.00 70.55           N  
-ANISOU 3146  N   HIS B 742     9662   9048   8095  -2073   -770    468       N  
-ATOM   3147  CA  HIS B 742     -97.816 -23.986  -2.594  1.00 73.03           C  
-ANISOU 3147  CA  HIS B 742     9918   9395   8436  -2063   -750    529       C  
-ATOM   3148  C   HIS B 742     -98.511 -25.231  -2.042  1.00 77.71           C  
-ANISOU 3148  C   HIS B 742    10570   9944   9012  -2188   -777    556       C  
-ATOM   3149  O   HIS B 742     -98.852 -26.135  -2.789  1.00 75.70           O  
-ANISOU 3149  O   HIS B 742    10383   9652   8726  -2291   -815    532       O  
-ATOM   3150  CB  HIS B 742     -98.780 -22.811  -2.516  1.00 72.74           C  
-ANISOU 3150  CB  HIS B 742     9730   9511   8397  -2056   -741    586       C  
-ATOM   3151  CG  HIS B 742     -98.118 -21.475  -2.574  1.00 72.37           C  
-ANISOU 3151  CG  HIS B 742     9616   9502   8379  -1921   -705    577       C  
-ATOM   3152  ND1 HIS B 742     -97.427 -21.030  -3.684  1.00 75.25           N  
-ANISOU 3152  ND1 HIS B 742    10000   9854   8738  -1866   -705    530       N  
-ATOM   3153  CD2 HIS B 742     -98.064 -20.474  -1.666  1.00 69.77           C  
-ANISOU 3153  CD2 HIS B 742     9202   9224   8083  -1835   -666    609       C  
-ATOM   3154  CE1 HIS B 742     -96.976 -19.809  -3.451  1.00 76.63           C  
-ANISOU 3154  CE1 HIS B 742    10103  10068   8945  -1754   -669    537       C  
-ATOM   3155  NE2 HIS B 742     -97.353 -19.450  -2.236  1.00 73.64           N  
-ANISOU 3155  NE2 HIS B 742     9663   9727   8592  -1733   -646    583       N  
-ATOM   3156  N   ASP B 743     -98.748 -25.240  -0.734  1.00 80.48           N  
-ANISOU 3156  N   ASP B 743    10893  10305   9381  -2184   -756    607       N  
-ATOM   3157  CA  ASP B 743     -99.502 -26.320  -0.069  1.00 82.38           C  
-ANISOU 3157  CA  ASP B 743    11177  10519   9606  -2307   -775    648       C  
-ATOM   3158  C   ASP B 743    -100.983 -25.994  -0.054  1.00 82.93           C  
-ANISOU 3158  C   ASP B 743    11126  10731   9653  -2406   -784    708       C  
-ATOM   3159  O   ASP B 743    -101.341 -24.935   0.435  1.00 84.16           O  
-ANISOU 3159  O   ASP B 743    11162  10992   9822  -2349   -752    746       O  
-ATOM   3160  CB  ASP B 743     -99.051 -26.499   1.380  1.00 75.71           C  
-ANISOU 3160  CB  ASP B 743    10363   9619   8784  -2259   -746    679       C  
-ATOM   3161  N   PRO B 750    -106.749 -19.865  -3.012  1.00 74.24           N  
-ANISOU 3161  N   PRO B 750     9116  10539   8554  -2399   -832    945       N  
-ATOM   3162  CA  PRO B 750    -106.567 -18.461  -2.592  1.00 73.00           C  
-ANISOU 3162  CA  PRO B 750     8862  10437   8438  -2256   -782    963       C  
-ATOM   3163  C   PRO B 750    -106.378 -17.586  -3.839  1.00 74.28           C  
-ANISOU 3163  C   PRO B 750     8991  10636   8594  -2195   -813    953       C  
-ATOM   3164  O   PRO B 750    -105.280 -17.511  -4.415  1.00 74.19           O  
-ANISOU 3164  O   PRO B 750     9076  10540   8573  -2135   -814    901       O  
-ATOM   3165  CB  PRO B 750    -105.350 -18.488  -1.633  1.00 71.07           C  
-ANISOU 3165  CB  PRO B 750     8711  10079   8214  -2162   -725    925       C  
-ATOM   3166  CG  PRO B 750    -104.904 -19.911  -1.560  1.00 73.07           C  
-ANISOU 3166  CG  PRO B 750     9107  10217   8438  -2251   -747    891       C  
-ATOM   3167  CD  PRO B 750    -105.684 -20.756  -2.530  1.00 73.17           C  
-ANISOU 3167  CD  PRO B 750     9134  10256   8412  -2394   -813    895       C  
-ATOM   3168  N   LEU B 751    -107.493 -17.016  -4.300  1.00 71.10           N  
-ANISOU 3168  N   LEU B 751     8456  10363   8195  -2223   -844   1006       N  
-ATOM   3169  CA  LEU B 751    -107.543 -16.346  -5.592  1.00 70.76           C  
-ANISOU 3169  CA  LEU B 751     8381  10369   8136  -2197   -891   1009       C  
-ATOM   3170  C   LEU B 751    -106.798 -15.024  -5.507  1.00 69.80           C  
-ANISOU 3170  C   LEU B 751     8232  10238   8053  -2036   -844   1004       C  
-ATOM   3171  O   LEU B 751    -107.013 -14.245  -4.577  1.00 66.86           O  
-ANISOU 3171  O   LEU B 751     7773   9904   7728  -1957   -791   1033       O  
-ATOM   3172  CB  LEU B 751    -108.991 -16.111  -6.048  1.00 70.53           C  
-ANISOU 3172  CB  LEU B 751     8209  10485   8104  -2271   -943   1075       C  
-ATOM   3173  N   LEU B 752    -105.909 -14.789  -6.468  1.00 64.15           N  
-ANISOU 3173  N   LEU B 752     7594   9466   7313  -1992   -861    964       N  
-ATOM   3174  CA  LEU B 752    -105.136 -13.556  -6.511  1.00 63.99           C  
-ANISOU 3174  CA  LEU B 752     7558   9429   7326  -1848   -820    957       C  
-ATOM   3175  C   LEU B 752    -105.868 -12.505  -7.349  1.00 64.58           C  
-ANISOU 3175  C   LEU B 752     7518   9613   7405  -1818   -856   1011       C  
-ATOM   3176  O   LEU B 752    -105.602 -12.327  -8.530  1.00 66.16           O  
-ANISOU 3176  O   LEU B 752     7756   9815   7569  -1822   -898   1003       O  
-ATOM   3177  CB  LEU B 752    -103.740 -13.829  -7.064  1.00 62.92           C  
-ANISOU 3177  CB  LEU B 752     7564   9176   7166  -1813   -812    887       C  
-ATOM   3178  CG  LEU B 752    -102.940 -14.862  -6.257  1.00 63.04           C  
-ANISOU 3178  CG  LEU B 752     7694   9076   7183  -1831   -780    835       C  
-ATOM   3179  CD1 LEU B 752    -101.641 -15.193  -6.966  1.00 64.73           C  
-ANISOU 3179  CD1 LEU B 752     8039   9183   7374  -1803   -777    765       C  
-ATOM   3180  CD2 LEU B 752    -102.681 -14.394  -4.834  1.00 59.08           C  
-ANISOU 3180  CD2 LEU B 752     7156   8555   6735  -1747   -715    844       C  
-ATOM   3181  N   ASN B 753    -106.810 -11.819  -6.721  1.00 69.26           N  
-ANISOU 3181  N   ASN B 753     7974  10299   8044  -1787   -840   1070       N  
-ATOM   3182  CA  ASN B 753    -107.737 -10.913  -7.415  1.00 74.33           C  
-ANISOU 3182  CA  ASN B 753     8487  11056   8697  -1767   -881   1134       C  
-ATOM   3183  C   ASN B 753    -107.861  -9.548  -6.743  1.00 73.63           C  
-ANISOU 3183  C   ASN B 753     8293  11004   8679  -1632   -825   1168       C  
-ATOM   3184  O   ASN B 753    -108.775  -8.784  -7.028  1.00 78.86           O  
-ANISOU 3184  O   ASN B 753     8829  11766   9368  -1606   -849   1229       O  
-ATOM   3185  CB  ASN B 753    -109.125 -11.592  -7.561  1.00 75.22           C  
-ANISOU 3185  CB  ASN B 753     8514  11274   8793  -1896   -939   1181       C  
-ATOM   3186  CG  ASN B 753    -109.756 -11.999  -6.244  1.00 76.01           C  
-ANISOU 3186  CG  ASN B 753     8552  11401   8927  -1929   -892   1197       C  
-ATOM   3187  OD1 ASN B 753    -109.299 -11.610  -5.175  1.00 79.31           O  
-ANISOU 3187  OD1 ASN B 753     8973  11776   9385  -1844   -816   1182       O  
-ATOM   3188  ND2 ASN B 753    -110.801 -12.840  -6.313  1.00 76.35           N  
-ANISOU 3188  ND2 ASN B 753     8545  11514   8949  -2062   -937   1227       N  
-ATOM   3189  N   ASN B 754    -106.939  -9.245  -5.846  1.00 72.42           N  
-ANISOU 3189  N   ASN B 754     8192  10766   8556  -1545   -753   1128       N  
-ATOM   3190  CA  ASN B 754    -106.981  -7.991  -5.118  1.00 73.48           C  
-ANISOU 3190  CA  ASN B 754     8242  10922   8757  -1418   -694   1150       C  
-ATOM   3191  C   ASN B 754    -105.565  -7.577  -4.744  1.00 66.87           C  
-ANISOU 3191  C   ASN B 754     7503   9970   7934  -1323   -640   1093       C  
-ATOM   3192  O   ASN B 754    -104.646  -8.387  -4.744  1.00 66.13           O  
-ANISOU 3192  O   ASN B 754     7532   9786   7809  -1356   -637   1039       O  
-ATOM   3193  CB  ASN B 754    -107.884  -8.113  -3.874  1.00 72.15           C  
-ANISOU 3193  CB  ASN B 754     7980  10814   8622  -1433   -651   1176       C  
-ATOM   3194  CG  ASN B 754    -107.340  -9.093  -2.853  1.00 71.13           C  
-ANISOU 3194  CG  ASN B 754     7944  10608   8475  -1477   -610   1129       C  
-ATOM   3195  OD1 ASN B 754    -106.527  -8.734  -1.995  1.00 73.08           O  
-ANISOU 3195  OD1 ASN B 754     8237  10786   8745  -1396   -549   1094       O  
-ATOM   3196  ND2 ASN B 754    -107.769 -10.338  -2.949  1.00 71.54           N  
-ANISOU 3196  ND2 ASN B 754     8029  10669   8485  -1608   -647   1130       N  
-ATOM   3197  N   ALA B 755    -105.419  -6.316  -4.383  1.00 66.31           N  
-ANISOU 3197  N   ALA B 755     7375   9903   7917  -1203   -596   1106       N  
-ATOM   3198  CA  ALA B 755    -104.127  -5.734  -4.099  1.00 63.20           C  
-ANISOU 3198  CA  ALA B 755     7059   9410   7544  -1108   -549   1059       C  
-ATOM   3199  C   ALA B 755    -103.429  -6.394  -2.895  1.00 65.86           C  
-ANISOU 3199  C   ALA B 755     7472   9671   7880  -1113   -499   1006       C  
-ATOM   3200  O   ALA B 755    -102.233  -6.685  -2.957  1.00 59.37           O  
-ANISOU 3200  O   ALA B 755     6759   8754   7046  -1098   -490    954       O  
-ATOM   3201  CB  ALA B 755    -104.285  -4.236  -3.880  1.00 61.60           C  
-ANISOU 3201  CB  ALA B 755     6769   9232   7402   -987   -513   1088       C  
-ATOM   3202  N   ASP B 756    -104.170  -6.636  -1.817  1.00 69.87           N  
-ANISOU 3202  N   ASP B 756     7922  10223   8402  -1134   -468   1022       N  
-ATOM   3203  CA  ASP B 756    -103.593  -7.245  -0.609  1.00 74.65           C  
-ANISOU 3203  CA  ASP B 756     8597  10763   9001  -1140   -423    981       C  
-ATOM   3204  C   ASP B 756    -102.986  -8.631  -0.854  1.00 68.56           C  
-ANISOU 3204  C   ASP B 756     7948   9921   8181  -1232   -457    945       C  
-ATOM   3205  O   ASP B 756    -101.850  -8.916  -0.428  1.00 70.96           O  
-ANISOU 3205  O   ASP B 756     8351  10129   8483  -1203   -436    895       O  
-ATOM   3206  CB  ASP B 756    -104.635  -7.236   0.548  1.00 83.38           C  
-ANISOU 3206  CB  ASP B 756     9612  11945  10124  -1154   -382   1012       C  
-ATOM   3207  CG  ASP B 756    -104.617  -5.903   1.294  1.00 89.41           C  
-ANISOU 3207  CG  ASP B 756    10310  12722  10941  -1031   -319   1013       C  
-ATOM   3208  OD1 ASP B 756    -103.622  -5.695   2.012  1.00 92.04           O  
-ANISOU 3208  OD1 ASP B 756    10715  12976  11280   -973   -280    967       O  
-ATOM   3209  OD2 ASP B 756    -105.531  -5.051   1.140  1.00 94.31           O  
-ANISOU 3209  OD2 ASP B 756    10812  13426  11597   -989   -311   1056       O  
-ATOM   3210  N   SER B 757    -103.716  -9.466  -1.584  1.00 66.80           N  
-ANISOU 3210  N   SER B 757     7718   9742   7922  -1340   -511    968       N  
-ATOM   3211  CA  SER B 757    -103.239 -10.803  -1.934  1.00 63.11           C  
-ANISOU 3211  CA  SER B 757     7367   9205   7408  -1433   -547    933       C  
-ATOM   3212  C   SER B 757    -101.991 -10.766  -2.846  1.00 56.77           C  
-ANISOU 3212  C   SER B 757     6666   8314   6591  -1394   -562    883       C  
-ATOM   3213  O   SER B 757    -101.012 -11.512  -2.645  1.00 52.95           O  
-ANISOU 3213  O   SER B 757     6294   7731   6094  -1402   -555    833       O  
-ATOM   3214  CB  SER B 757    -104.430 -11.550  -2.561  1.00 69.79           C  
-ANISOU 3214  CB  SER B 757     8168  10129   8219  -1558   -604    971       C  
-ATOM   3215  OG  SER B 757    -104.794 -10.968  -3.815  1.00 72.73           O  
-ANISOU 3215  OG  SER B 757     8490  10561   8584  -1553   -650    996       O  
-ATOM   3216  N   VAL B 758    -101.974  -9.820  -3.780  1.00 55.33           N  
-ANISOU 3216  N   VAL B 758     6441   8165   6416  -1343   -577    898       N  
-ATOM   3217  CA  VAL B 758    -100.845  -9.672  -4.693  1.00 52.95           C  
-ANISOU 3217  CA  VAL B 758     6225   7792   6100  -1306   -584    856       C  
-ATOM   3218  C   VAL B 758     -99.609  -9.213  -3.936  1.00 52.46           C  
-ANISOU 3218  C   VAL B 758     6213   7644   6077  -1207   -529    813       C  
-ATOM   3219  O   VAL B 758     -98.526  -9.794  -4.087  1.00 54.36           O  
-ANISOU 3219  O   VAL B 758     6556   7794   6304  -1206   -524    759       O  
-ATOM   3220  CB  VAL B 758    -101.172  -8.688  -5.824  1.00 54.05           C  
-ANISOU 3220  CB  VAL B 758     6305   7995   6238  -1274   -612    892       C  
-ATOM   3221  CG1 VAL B 758     -99.944  -8.366  -6.650  1.00 50.13           C  
-ANISOU 3221  CG1 VAL B 758     5890   7426   5730  -1224   -605    851       C  
-ATOM   3222  CG2 VAL B 758    -102.255  -9.277  -6.736  1.00 56.30           C  
-ANISOU 3222  CG2 VAL B 758     6557   8359   6475  -1382   -681    929       C  
-ATOM   3223  N   GLN B 759     -99.790  -8.173  -3.129  1.00 53.51           N  
-ANISOU 3223  N   GLN B 759     6269   7805   6257  -1125   -487    834       N  
-ATOM   3224  CA  GLN B 759     -98.732  -7.596  -2.286  1.00 57.91           C  
-ANISOU 3224  CA  GLN B 759     6859   8292   6854  -1031   -435    797       C  
-ATOM   3225  C   GLN B 759     -98.038  -8.646  -1.436  1.00 58.67           C  
-ANISOU 3225  C   GLN B 759     7044   8309   6938  -1059   -423    754       C  
-ATOM   3226  O   GLN B 759     -96.803  -8.704  -1.384  1.00 58.67           O  
-ANISOU 3226  O   GLN B 759     7120   8223   6948  -1015   -409    706       O  
-ATOM   3227  CB  GLN B 759     -99.358  -6.593  -1.292  1.00 60.05           C  
-ANISOU 3227  CB  GLN B 759     7032   8617   7169   -965   -393    828       C  
-ATOM   3228  CG  GLN B 759     -99.494  -5.187  -1.819  1.00 61.56           C  
-ANISOU 3228  CG  GLN B 759     7152   8842   7396   -882   -383    855       C  
-ATOM   3229  CD  GLN B 759    -100.443  -4.330  -0.980  1.00 64.33           C  
-ANISOU 3229  CD  GLN B 759     7394   9262   7786   -832   -348    892       C  
-ATOM   3230  OE1 GLN B 759    -101.438  -3.683  -1.445  1.00 66.89           O  
-ANISOU 3230  OE1 GLN B 759     7621   9667   8128   -820   -362    944       O  
-ATOM   3231  NE2 GLN B 759    -100.102  -4.289   0.282  1.00 61.62           N  
-ANISOU 3231  NE2 GLN B 759     7067   8885   7460   -798   -301    863       N  
-ATOM   3232  N   ALA B 760     -98.843  -9.474  -0.771  1.00 54.09           N  
-ANISOU 3232  N   ALA B 760     6453   7760   6339  -1132   -430    774       N  
-ATOM   3233  CA  ALA B 760     -98.294 -10.538   0.047  1.00 52.25           C  
-ANISOU 3233  CA  ALA B 760     6308   7454   6092  -1167   -425    743       C  
-ATOM   3234  C   ALA B 760     -97.410 -11.481  -0.766  1.00 51.78           C  
-ANISOU 3234  C   ALA B 760     6359   7309   6007  -1203   -456    699       C  
-ATOM   3235  O   ALA B 760     -96.360 -11.938  -0.271  1.00 51.10           O  
-ANISOU 3235  O   ALA B 760     6354   7132   5928  -1176   -445    657       O  
-ATOM   3236  CB  ALA B 760     -99.408 -11.316   0.728  1.00 52.94           C  
-ANISOU 3236  CB  ALA B 760     6365   7593   6156  -1256   -431    780       C  
-ATOM   3237  N   LYS B 761     -97.820 -11.785  -1.997  1.00 49.10           N  
-ANISOU 3237  N   LYS B 761     6023   6998   5637  -1264   -497    706       N  
-ATOM   3238  CA  LYS B 761     -97.002 -12.636  -2.855  1.00 49.38           C  
-ANISOU 3238  CA  LYS B 761     6164   6955   5645  -1296   -521    657       C  
-ATOM   3239  C   LYS B 761     -95.728 -11.978  -3.351  1.00 44.75           C  
-ANISOU 3239  C   LYS B 761     5613   6310   5079  -1206   -498    615       C  
-ATOM   3240  O   LYS B 761     -94.690 -12.649  -3.484  1.00 44.47           O  
-ANISOU 3240  O   LYS B 761     5670   6184   5042  -1198   -495    564       O  
-ATOM   3241  CB  LYS B 761     -97.826 -13.214  -4.022  1.00 55.61           C  
-ANISOU 3241  CB  LYS B 761     6955   7791   6385  -1397   -573    672       C  
-ATOM   3242  CG  LYS B 761     -98.939 -14.134  -3.547  1.00 58.82           C  
-ANISOU 3242  CG  LYS B 761     7345   8236   6769  -1504   -599    705       C  
-ATOM   3243  CD  LYS B 761     -98.369 -15.281  -2.722  1.00 62.61           C  
-ANISOU 3243  CD  LYS B 761     7923   8618   7247  -1533   -591    673       C  
-ATOM   3244  CE  LYS B 761     -99.443 -16.204  -2.188  1.00 65.30           C  
-ANISOU 3244  CE  LYS B 761     8253   8991   7566  -1645   -612    709       C  
-ATOM   3245  NZ  LYS B 761     -99.047 -16.624  -0.818  1.00 66.75           N  
-ANISOU 3245  NZ  LYS B 761     8478   9116   7769  -1626   -581    707       N  
-ATOM   3246  N   VAL B 762     -95.783 -10.679  -3.609  1.00 43.64           N  
-ANISOU 3246  N   VAL B 762     5399   6218   4963  -1136   -480    637       N  
-ATOM   3247  CA  VAL B 762     -94.585  -9.955  -4.048  1.00 46.36           C  
-ANISOU 3247  CA  VAL B 762     5771   6513   5332  -1053   -454    602       C  
-ATOM   3248  C   VAL B 762     -93.551  -9.973  -2.936  1.00 47.33           C  
-ANISOU 3248  C   VAL B 762     5930   6558   5494   -989   -419    565       C  
-ATOM   3249  O   VAL B 762     -92.364 -10.229  -3.167  1.00 48.12           O  
-ANISOU 3249  O   VAL B 762     6098   6581   5604   -958   -408    516       O  
-ATOM   3250  CB  VAL B 762     -94.909  -8.498  -4.425  1.00 47.22           C  
-ANISOU 3250  CB  VAL B 762     5793   6686   5465   -991   -441    640       C  
-ATOM   3251  CG1 VAL B 762     -93.634  -7.717  -4.695  1.00 46.69           C  
-ANISOU 3251  CG1 VAL B 762     5752   6561   5428   -907   -408    605       C  
-ATOM   3252  CG2 VAL B 762     -95.808  -8.448  -5.664  1.00 45.70           C  
-ANISOU 3252  CG2 VAL B 762     5568   6566   5228  -1050   -484    678       C  
-ATOM   3253  N   GLU B 763     -94.024  -9.683  -1.734  1.00 48.25           N  
-ANISOU 3253  N   GLU B 763     5999   6701   5633   -970   -402    590       N  
-ATOM   3254  CA  GLU B 763     -93.198  -9.711  -0.547  1.00 51.31           C  
-ANISOU 3254  CA  GLU B 763     6417   7027   6050   -918   -376    562       C  
-ATOM   3255  C   GLU B 763     -92.523 -11.057  -0.406  1.00 50.33           C  
-ANISOU 3255  C   GLU B 763     6393   6820   5910   -957   -394    525       C  
-ATOM   3256  O   GLU B 763     -91.300 -11.168  -0.123  1.00 44.57           O  
-ANISOU 3256  O   GLU B 763     5716   6012   5206   -905   -383    483       O  
-ATOM   3257  CB  GLU B 763     -94.140  -9.505   0.638  1.00 57.09           C  
-ANISOU 3257  CB  GLU B 763     7090   7816   6786   -925   -361    601       C  
-ATOM   3258  CG  GLU B 763     -93.581  -9.909   2.001  1.00 67.31           C  
-ANISOU 3258  CG  GLU B 763     8428   9057   8089   -905   -346    582       C  
-ATOM   3259  CD  GLU B 763     -94.620 -10.114   3.110  1.00 75.54           C  
-ANISOU 3259  CD  GLU B 763     9432  10155   9115   -944   -334    620       C  
-ATOM   3260  OE1 GLU B 763     -95.687 -10.766   2.914  1.00 79.98           O  
-ANISOU 3260  OE1 GLU B 763     9974  10767   9646  -1028   -352    655       O  
-ATOM   3261  OE2 GLU B 763     -94.335  -9.639   4.220  1.00 76.26           O  
-ANISOU 3261  OE2 GLU B 763     9515  10238   9221   -893   -305    614       O  
-ATOM   3262  N   MET B 764     -93.331 -12.090  -0.572  1.00 44.05           N  
-ANISOU 3262  N   MET B 764     5621   6040   5077  -1050   -424    543       N  
-ATOM   3263  CA  MET B 764     -92.766 -13.397  -0.534  1.00 44.61           C  
-ANISOU 3263  CA  MET B 764     5791   6026   5133  -1091   -444    510       C  
-ATOM   3264  C   MET B 764     -91.666 -13.560  -1.569  1.00 43.03           C  
-ANISOU 3264  C   MET B 764     5652   5760   4937  -1062   -444    457       C  
-ATOM   3265  O   MET B 764     -90.572 -14.079  -1.263  1.00 43.67           O  
-ANISOU 3265  O   MET B 764     5801   5753   5040  -1026   -438    415       O  
-ATOM   3266  CB  MET B 764     -93.837 -14.426  -0.767  1.00 48.72           C  
-ANISOU 3266  CB  MET B 764     6329   6572   5610  -1204   -478    535       C  
-ATOM   3267  CG  MET B 764     -93.267 -15.823  -0.834  1.00 52.96           C  
-ANISOU 3267  CG  MET B 764     6979   7010   6133  -1249   -500    499       C  
-ATOM   3268  SD  MET B 764     -94.502 -16.949  -1.491  1.00 74.44           S  
-ANISOU 3268  SD  MET B 764     9724   9760   8799  -1393   -545    521       S  
-ATOM   3269  CE  MET B 764     -94.281 -16.646  -3.227  1.00 66.79           C  
-ANISOU 3269  CE  MET B 764     8765   8807   7806  -1395   -558    487       C  
-ATOM   3270  N   LEU B 765     -91.953 -13.174  -2.800  1.00 40.53           N  
-ANISOU 3270  N   LEU B 765     5314   5487   4599  -1079   -451    459       N  
-ATOM   3271  CA  LEU B 765     -90.958 -13.334  -3.853  1.00 42.30           C  
-ANISOU 3271  CA  LEU B 765     5598   5657   4819  -1058   -445    408       C  
-ATOM   3272  C   LEU B 765     -89.677 -12.545  -3.568  1.00 39.75           C  
-ANISOU 3272  C   LEU B 765     5268   5289   4547   -954   -407    377       C  
-ATOM   3273  O   LEU B 765     -88.581 -13.051  -3.830  1.00 40.97           O  
-ANISOU 3273  O   LEU B 765     5486   5365   4714   -927   -397    325       O  
-ATOM   3274  CB  LEU B 765     -91.497 -12.913  -5.215  1.00 45.03           C  
-ANISOU 3274  CB  LEU B 765     5918   6066   5125  -1093   -458    421       C  
-ATOM   3275  CG  LEU B 765     -92.557 -13.806  -5.858  1.00 46.30           C  
-ANISOU 3275  CG  LEU B 765     6102   6262   5229  -1204   -503    436       C  
-ATOM   3276  CD1 LEU B 765     -92.897 -13.261  -7.236  1.00 47.95           C  
-ANISOU 3276  CD1 LEU B 765     6289   6533   5397  -1226   -517    447       C  
-ATOM   3277  CD2 LEU B 765     -92.064 -15.234  -5.979  1.00 46.97           C  
-ANISOU 3277  CD2 LEU B 765     6297   6255   5294  -1253   -516    385       C  
-ATOM   3278  N   ASP B 766     -89.804 -11.349  -2.998  1.00 38.54           N  
-ANISOU 3278  N   ASP B 766     5037   5181   4425   -896   -386    406       N  
-ATOM   3279  CA  ASP B 766     -88.616 -10.568  -2.587  1.00 41.14           C  
-ANISOU 3279  CA  ASP B 766     5357   5468   4805   -804   -353    378       C  
-ATOM   3280  C   ASP B 766     -87.712 -11.374  -1.641  1.00 41.87           C  
-ANISOU 3280  C   ASP B 766     5508   5476   4924   -780   -354    343       C  
-ATOM   3281  O   ASP B 766     -86.482 -11.458  -1.844  1.00 39.71           O  
-ANISOU 3281  O   ASP B 766     5270   5139   4681   -732   -340    297       O  
-ATOM   3282  CB  ASP B 766     -89.006  -9.266  -1.890  1.00 39.37           C  
-ANISOU 3282  CB  ASP B 766     5049   5298   4611   -753   -333    413       C  
-ATOM   3283  CG  ASP B 766     -89.791  -8.351  -2.781  1.00 40.10           C  
-ANISOU 3283  CG  ASP B 766     5079   5467   4689   -760   -332    452       C  
-ATOM   3284  OD1 ASP B 766     -89.719  -8.520  -4.046  1.00 41.56           O  
-ANISOU 3284  OD1 ASP B 766     5289   5657   4844   -789   -341    444       O  
-ATOM   3285  OD2 ASP B 766     -90.474  -7.471  -2.211  1.00 39.75           O  
-ANISOU 3285  OD2 ASP B 766     4965   5476   4662   -734   -322    489       O  
-ATOM   3286  N   ASN B 767     -88.334 -12.027  -0.665  1.00 40.66           N  
-ANISOU 3286  N   ASN B 767     5366   5324   4758   -818   -374    366       N  
-ATOM   3287  CA  ASN B 767     -87.580 -12.801   0.301  1.00 42.75           C  
-ANISOU 3287  CA  ASN B 767     5688   5513   5043   -799   -382    344       C  
-ATOM   3288  C   ASN B 767     -87.018 -14.058  -0.373  1.00 41.15           C  
-ANISOU 3288  C   ASN B 767     5573   5232   4830   -828   -399    305       C  
-ATOM   3289  O   ASN B 767     -85.876 -14.445  -0.143  1.00 38.26           O  
-ANISOU 3289  O   ASN B 767     5250   4788   4497   -779   -397    266       O  
-ATOM   3290  CB  ASN B 767     -88.482 -13.057   1.500  1.00 47.55           C  
-ANISOU 3290  CB  ASN B 767     6282   6152   5633   -835   -394    388       C  
-ATOM   3291  CG  ASN B 767     -87.757 -13.668   2.698  1.00 58.96           C  
-ANISOU 3291  CG  ASN B 767     7779   7528   7095   -809   -405    377       C  
-ATOM   3292  OD1 ASN B 767     -86.509 -13.602   2.868  1.00 58.74           O  
-ANISOU 3292  OD1 ASN B 767     7776   7437   7106   -743   -402    339       O  
-ATOM   3293  ND2 ASN B 767     -88.552 -14.282   3.560  1.00 63.16           N  
-ANISOU 3293  ND2 ASN B 767     8326   8073   7598   -864   -420    413       N  
-ATOM   3294  N   LEU B 768     -87.787 -14.651  -1.267  1.00 42.42           N  
-ANISOU 3294  N   LEU B 768     5758   5413   4948   -905   -416    310       N  
-ATOM   3295  CA  LEU B 768     -87.304 -15.820  -2.011  1.00 45.37           C  
-ANISOU 3295  CA  LEU B 768     6220   5711   5307   -936   -428    266       C  
-ATOM   3296  C   LEU B 768     -86.085 -15.482  -2.859  1.00 44.02           C  
-ANISOU 3296  C   LEU B 768     6063   5501   5163   -870   -399    212       C  
-ATOM   3297  O   LEU B 768     -85.120 -16.244  -2.905  1.00 40.51           O  
-ANISOU 3297  O   LEU B 768     5681   4970   4742   -842   -395    166       O  
-ATOM   3298  CB  LEU B 768     -88.399 -16.402  -2.900  1.00 47.98           C  
-ANISOU 3298  CB  LEU B 768     6571   6078   5580  -1036   -452    279       C  
-ATOM   3299  CG  LEU B 768     -89.528 -17.204  -2.246  1.00 50.35           C  
-ANISOU 3299  CG  LEU B 768     6885   6395   5851  -1124   -485    321       C  
-ATOM   3300  CD1 LEU B 768     -90.422 -17.825  -3.308  1.00 50.94           C  
-ANISOU 3300  CD1 LEU B 768     6986   6497   5870  -1225   -512    322       C  
-ATOM   3301  CD2 LEU B 768     -88.983 -18.296  -1.347  1.00 51.41           C  
-ANISOU 3301  CD2 LEU B 768     7098   6430   6004  -1122   -498    307       C  
-ATOM   3302  N   LEU B 769     -86.118 -14.315  -3.479  1.00 44.22           N  
-ANISOU 3302  N   LEU B 769     6024   5589   5187   -843   -375    221       N  
-ATOM   3303  CA  LEU B 769     -85.005 -13.838  -4.285  1.00 46.74           C  
-ANISOU 3303  CA  LEU B 769     6345   5884   5530   -785   -340    177       C  
-ATOM   3304  C   LEU B 769     -83.704 -13.797  -3.531  1.00 42.64           C  
-ANISOU 3304  C   LEU B 769     5830   5297   5074   -703   -323    144       C  
-ATOM   3305  O   LEU B 769     -82.703 -14.367  -3.970  1.00 44.68           O  
-ANISOU 3305  O   LEU B 769     6136   5488   5352   -674   -308     92       O  
-ATOM   3306  CB  LEU B 769     -85.301 -12.426  -4.758  1.00 51.84           C  
-ANISOU 3306  CB  LEU B 769     6913   6609   6173   -763   -320    207       C  
-ATOM   3307  CG  LEU B 769     -84.650 -11.856  -6.026  1.00 58.37           C  
-ANISOU 3307  CG  LEU B 769     7740   7444   6994   -741   -286    179       C  
-ATOM   3308  CD1 LEU B 769     -83.516 -10.877  -5.714  1.00 58.94           C  
-ANISOU 3308  CD1 LEU B 769     7769   7498   7127   -654   -249    163       C  
-ATOM   3309  CD2 LEU B 769     -84.166 -12.963  -6.957  1.00 61.54           C  
-ANISOU 3309  CD2 LEU B 769     8225   7791   7366   -771   -282    124       C  
-ATOM   3310  N   ASP B 770     -83.721 -13.140  -2.377  1.00 40.81           N  
-ANISOU 3310  N   ASP B 770     5549   5083   4874   -665   -327    173       N  
-ATOM   3311  CA  ASP B 770     -82.516 -13.052  -1.558  1.00 39.40           C  
-ANISOU 3311  CA  ASP B 770     5368   4847   4754   -590   -320    147       C  
-ATOM   3312  C   ASP B 770     -82.111 -14.403  -0.957  1.00 37.99           C  
-ANISOU 3312  C   ASP B 770     5263   4585   4585   -594   -348    128       C  
-ATOM   3313  O   ASP B 770     -80.909 -14.699  -0.792  1.00 38.37           O  
-ANISOU 3313  O   ASP B 770     5331   4567   4681   -535   -343     89       O  
-ATOM   3314  CB  ASP B 770     -82.707 -12.017  -0.467  1.00 40.20           C  
-ANISOU 3314  CB  ASP B 770     5406   4992   4877   -556   -319    181       C  
-ATOM   3315  CG  ASP B 770     -82.451 -10.583  -0.957  1.00 43.40           C  
-ANISOU 3315  CG  ASP B 770     5744   5444   5304   -515   -285    182       C  
-ATOM   3316  OD1 ASP B 770     -81.542 -10.394  -1.811  1.00 45.80           O  
-ANISOU 3316  OD1 ASP B 770     6050   5724   5630   -485   -259    146       O  
-ATOM   3317  OD2 ASP B 770     -83.143  -9.650  -0.482  1.00 42.96           O  
-ANISOU 3317  OD2 ASP B 770     5633   5446   5245   -512   -281    219       O  
-ATOM   3318  N   ILE B 771     -83.089 -15.242  -0.652  1.00 37.31           N  
-ANISOU 3318  N   ILE B 771     5217   4500   4459   -663   -378    157       N  
-ATOM   3319  CA  ILE B 771     -82.766 -16.620  -0.259  1.00 41.87           C  
-ANISOU 3319  CA  ILE B 771     5878   4989   5043   -676   -406    141       C  
-ATOM   3320  C   ILE B 771     -82.026 -17.370  -1.397  1.00 43.96           C  
-ANISOU 3320  C   ILE B 771     6201   5186   5314   -668   -391     81       C  
-ATOM   3321  O   ILE B 771     -81.026 -18.051  -1.140  1.00 42.09           O  
-ANISOU 3321  O   ILE B 771     6007   4865   5120   -619   -395     47       O  
-ATOM   3322  CB  ILE B 771     -84.019 -17.373   0.221  1.00 43.01           C  
-ANISOU 3322  CB  ILE B 771     6055   5147   5139   -763   -439    186       C  
-ATOM   3323  CG1 ILE B 771     -84.410 -16.864   1.609  1.00 41.38           C  
-ANISOU 3323  CG1 ILE B 771     5806   4981   4935   -753   -449    234       C  
-ATOM   3324  CG2 ILE B 771     -83.765 -18.866   0.301  1.00 47.59           C  
-ANISOU 3324  CG2 ILE B 771     6733   5628   5719   -790   -465    167       C  
-ATOM   3325  CD1 ILE B 771     -85.839 -17.121   1.993  1.00 42.20           C  
-ANISOU 3325  CD1 ILE B 771     5904   5141   4989   -840   -465    287       C  
-ATOM   3326  N   GLU B 772     -82.495 -17.235  -2.640  1.00 44.66           N  
-ANISOU 3326  N   GLU B 772     6292   5314   5361   -712   -373     67       N  
-ATOM   3327  CA  GLU B 772     -81.806 -17.847  -3.793  1.00 46.92           C  
-ANISOU 3327  CA  GLU B 772     6635   5546   5647   -706   -350      5       C  
-ATOM   3328  C   GLU B 772     -80.375 -17.348  -3.898  1.00 45.29           C  
-ANISOU 3328  C   GLU B 772     6399   5308   5501   -610   -313    -37       C  
-ATOM   3329  O   GLU B 772     -79.446 -18.140  -4.094  1.00 48.77           O  
-ANISOU 3329  O   GLU B 772     6890   5667   5975   -571   -302    -88       O  
-ATOM   3330  CB  GLU B 772     -82.564 -17.588  -5.093  1.00 48.83           C  
-ANISOU 3330  CB  GLU B 772     6876   5851   5825   -770   -338      3       C  
-ATOM   3331  CG  GLU B 772     -82.027 -18.269  -6.371  1.00 51.57           C  
-ANISOU 3331  CG  GLU B 772     7293   6150   6151   -780   -312    -64       C  
-ATOM   3332  CD  GLU B 772     -80.727 -17.665  -6.930  1.00 53.17           C  
-ANISOU 3332  CD  GLU B 772     7469   6339   6394   -697   -258   -111       C  
-ATOM   3333  OE1 GLU B 772     -80.537 -16.436  -6.882  1.00 51.27           O  
-ANISOU 3333  OE1 GLU B 772     7150   6161   6172   -660   -237    -88       O  
-ATOM   3334  OE2 GLU B 772     -79.881 -18.430  -7.436  1.00 55.53           O  
-ANISOU 3334  OE2 GLU B 772     7825   6564   6708   -670   -233   -174       O  
-ATOM   3335  N   VAL B 773     -80.178 -16.054  -3.688  1.00 44.14           N  
-ANISOU 3335  N   VAL B 773     6170   5223   5376   -569   -293    -16       N  
-ATOM   3336  CA  VAL B 773     -78.825 -15.499  -3.696  1.00 41.12           C  
-ANISOU 3336  CA  VAL B 773     5749   4818   5057   -483   -260    -52       C  
-ATOM   3337  C   VAL B 773     -77.962 -16.135  -2.621  1.00 39.92           C  
-ANISOU 3337  C   VAL B 773     5614   4588   4964   -426   -284    -64       C  
-ATOM   3338  O   VAL B 773     -76.821 -16.554  -2.882  1.00 44.27           O  
-ANISOU 3338  O   VAL B 773     6180   5077   5562   -370   -264   -114       O  
-ATOM   3339  CB  VAL B 773     -78.825 -13.989  -3.480  1.00 43.45           C  
-ANISOU 3339  CB  VAL B 773     5956   5186   5368   -456   -242    -22       C  
-ATOM   3340  CG1 VAL B 773     -77.408 -13.478  -3.280  1.00 43.39           C  
-ANISOU 3340  CG1 VAL B 773     5906   5149   5432   -373   -215    -55       C  
-ATOM   3341  CG2 VAL B 773     -79.492 -13.282  -4.651  1.00 45.17           C  
-ANISOU 3341  CG2 VAL B 773     6153   5475   5534   -499   -216     -9       C  
-ATOM   3342  N   ALA B 774     -78.503 -16.233  -1.413  1.00 38.74           N  
-ANISOU 3342  N   ALA B 774     5464   4444   4813   -440   -326    -19       N  
-ATOM   3343  CA  ALA B 774     -77.773 -16.850  -0.301  1.00 41.00           C  
-ANISOU 3343  CA  ALA B 774     5771   4659   5146   -391   -359    -20       C  
-ATOM   3344  C   ALA B 774     -77.441 -18.293  -0.603  1.00 41.87           C  
-ANISOU 3344  C   ALA B 774     5969   4675   5264   -394   -372    -53       C  
-ATOM   3345  O   ALA B 774     -76.309 -18.740  -0.390  1.00 44.56           O  
-ANISOU 3345  O   ALA B 774     6321   4946   5665   -325   -374    -86       O  
-ATOM   3346  CB  ALA B 774     -78.580 -16.759   0.988  1.00 39.35           C  
-ANISOU 3346  CB  ALA B 774     5558   4479   4915   -420   -400     39       C  
-ATOM   3347  N   TYR B 775     -78.424 -19.027  -1.113  1.00 45.40           N  
-ANISOU 3347  N   TYR B 775     6478   5117   5655   -473   -381    -46       N  
-ATOM   3348  CA  TYR B 775     -78.220 -20.439  -1.399  1.00 50.21           C  
-ANISOU 3348  CA  TYR B 775     7181   5628   6268   -484   -394    -79       C  
-ATOM   3349  C   TYR B 775     -77.189 -20.660  -2.508  1.00 50.41           C  
-ANISOU 3349  C   TYR B 775     7222   5609   6324   -434   -347   -152       C  
-ATOM   3350  O   TYR B 775     -76.370 -21.562  -2.391  1.00 53.83           O  
-ANISOU 3350  O   TYR B 775     7702   5946   6803   -385   -352   -187       O  
-ATOM   3351  CB  TYR B 775     -79.538 -21.142  -1.750  1.00 52.46           C  
-ANISOU 3351  CB  TYR B 775     7530   5922   6483   -591   -414    -58       C  
-ATOM   3352  CG  TYR B 775     -79.401 -22.632  -1.567  1.00 58.48           C  
-ANISOU 3352  CG  TYR B 775     8395   6569   7255   -605   -442    -75       C  
-ATOM   3353  CD1 TYR B 775     -79.341 -23.180  -0.292  1.00 59.61           C  
-ANISOU 3353  CD1 TYR B 775     8566   6661   7423   -592   -487    -34       C  
-ATOM   3354  CD2 TYR B 775     -79.263 -23.490  -2.654  1.00 60.66           C  
-ANISOU 3354  CD2 TYR B 775     8745   6783   7518   -626   -424   -133       C  
-ATOM   3355  CE1 TYR B 775     -79.188 -24.542  -0.098  1.00 60.43           C  
-ANISOU 3355  CE1 TYR B 775     8768   6651   7540   -601   -516    -44       C  
-ATOM   3356  CE2 TYR B 775     -79.101 -24.858  -2.467  1.00 60.03           C  
-ANISOU 3356  CE2 TYR B 775     8766   6587   7454   -634   -449   -151       C  
-ATOM   3357  CZ  TYR B 775     -79.066 -25.376  -1.184  1.00 61.94           C  
-ANISOU 3357  CZ  TYR B 775     9034   6777   7725   -620   -496   -103       C  
-ATOM   3358  OH  TYR B 775     -78.913 -26.725  -0.947  1.00 61.15           O  
-ANISOU 3358  OH  TYR B 775     9036   6553   7643   -626   -525   -113       O  
-ATOM   3359  N   SER B 776     -77.240 -19.848  -3.568  1.00 48.01           N  
-ANISOU 3359  N   SER B 776     6877   5371   5994   -445   -301   -174       N  
-ATOM   3360  CA  SER B 776     -76.255 -19.911  -4.649  1.00 51.20           C  
-ANISOU 3360  CA  SER B 776     7286   5746   6421   -399   -246   -243       C  
-ATOM   3361  C   SER B 776     -74.847 -19.645  -4.172  1.00 50.74           C  
-ANISOU 3361  C   SER B 776     7176   5653   6450   -294   -230   -267       C  
-ATOM   3362  O   SER B 776     -73.912 -20.338  -4.561  1.00 54.87           O  
-ANISOU 3362  O   SER B 776     7730   6103   7017   -242   -206   -324       O  
-ATOM   3363  CB  SER B 776     -76.553 -18.884  -5.724  1.00 55.15           C  
-ANISOU 3363  CB  SER B 776     7742   6337   6876   -428   -202   -248       C  
-ATOM   3364  OG  SER B 776     -77.706 -19.254  -6.423  1.00 66.27           O  
-ANISOU 3364  OG  SER B 776     9203   7773   8204   -521   -214   -239       O  
-ATOM   3365  N   LEU B 777     -74.680 -18.623  -3.353  1.00 48.53           N  
-ANISOU 3365  N   LEU B 777     6815   5425   6198   -264   -243   -228       N  
-ATOM   3366  CA  LEU B 777     -73.360 -18.311  -2.831  1.00 50.34           C  
-ANISOU 3366  CA  LEU B 777     6987   5628   6511   -172   -236   -247       C  
-ATOM   3367  C   LEU B 777     -72.808 -19.496  -2.060  1.00 50.90           C  
-ANISOU 3367  C   LEU B 777     7109   5599   6631   -127   -277   -255       C  
-ATOM   3368  O   LEU B 777     -71.656 -19.869  -2.229  1.00 48.82           O  
-ANISOU 3368  O   LEU B 777     6836   5279   6434    -53   -258   -301       O  
-ATOM   3369  CB  LEU B 777     -73.407 -17.095  -1.912  1.00 49.95           C  
-ANISOU 3369  CB  LEU B 777     6855   5646   6476   -159   -255   -200       C  
-ATOM   3370  CG  LEU B 777     -73.520 -15.732  -2.601  1.00 50.47           C  
-ANISOU 3370  CG  LEU B 777     6852   5800   6525   -172   -209   -196       C  
-ATOM   3371  CD1 LEU B 777     -73.623 -14.669  -1.528  1.00 47.75           C  
-ANISOU 3371  CD1 LEU B 777     6440   5505   6197   -160   -235   -151       C  
-ATOM   3372  CD2 LEU B 777     -72.343 -15.452  -3.537  1.00 47.32           C  
-ANISOU 3372  CD2 LEU B 777     6417   5392   6170   -121   -147   -253       C  
-ATOM   3373  N   LEU B 778     -73.666 -20.086  -1.235  1.00 53.80           N  
-ANISOU 3373  N   LEU B 778     7530   5946   6967   -173   -333   -208       N  
-ATOM   3374  CA  LEU B 778     -73.295 -21.176  -0.358  1.00 58.22           C  
-ANISOU 3374  CA  LEU B 778     8144   6411   7564   -138   -384   -199       C  
-ATOM   3375  C   LEU B 778     -72.923 -22.418  -1.171  1.00 62.90           C  
-ANISOU 3375  C   LEU B 778     8819   6907   8174   -124   -364   -256       C  
-ATOM   3376  O   LEU B 778     -71.937 -23.090  -0.866  1.00 69.78           O  
-ANISOU 3376  O   LEU B 778     9704   7695   9114    -47   -376   -280       O  
-ATOM   3377  CB  LEU B 778     -74.458 -21.477   0.595  1.00 57.33           C  
-ANISOU 3377  CB  LEU B 778     8075   6309   7399   -209   -439   -132       C  
-ATOM   3378  CG  LEU B 778     -74.200 -22.273   1.873  1.00 59.63           C  
-ANISOU 3378  CG  LEU B 778     8409   6529   7721   -181   -504    -95       C  
-ATOM   3379  CD1 LEU B 778     -73.050 -21.689   2.698  1.00 61.37           C  
-ANISOU 3379  CD1 LEU B 778     8557   6753   8010    -89   -523    -91       C  
-ATOM   3380  CD2 LEU B 778     -75.474 -22.302   2.694  1.00 59.09           C  
-ANISOU 3380  CD2 LEU B 778     8368   6498   7585   -264   -542    -27       C  
-ATOM   3381  N   ARG B 779     -73.680 -22.698  -2.223  1.00 62.82           N  
-ANISOU 3381  N   ARG B 779     8860   6907   8100   -195   -334   -280       N  
-ATOM   3382  CA  ARG B 779     -73.389 -23.862  -3.078  1.00 70.83           C  
-ANISOU 3382  CA  ARG B 779     9962   7829   9122   -189   -310   -343       C  
-ATOM   3383  C   ARG B 779     -72.141 -23.674  -3.980  1.00 74.79           C  
-ANISOU 3383  C   ARG B 779    10425   8316   9676   -107   -242   -417       C  
-ATOM   3384  O   ARG B 779     -71.572 -24.667  -4.428  1.00 79.82           O  
-ANISOU 3384  O   ARG B 779    11123   8859  10345    -69   -223   -473       O  
-ATOM   3385  CB  ARG B 779     -74.616 -24.240  -3.941  1.00 66.22           C  
-ANISOU 3385  CB  ARG B 779     9450   7263   8447   -299   -303   -348       C  
-ATOM   3386  N   GLY B 780     -71.689 -22.431  -4.203  1.00 71.17           N  
-ANISOU 3386  N   GLY B 780     9866   7943   9230    -79   -204   -418       N  
-ATOM   3387  CA  GLY B 780     -70.680 -22.129  -5.252  1.00 69.99           C  
-ANISOU 3387  CA  GLY B 780     9678   7802   9113    -25   -127   -487       C  
-ATOM   3388  C   GLY B 780     -69.215 -21.991  -4.844  1.00 67.02           C  
-ANISOU 3388  C   GLY B 780     9228   7394   8841     88   -112   -512       C  
-ATOM   3389  O   GLY B 780     -68.840 -22.308  -3.717  1.00 66.40           O  
-ANISOU 3389  O   GLY B 780     9138   7270   8820    136   -170   -481       O  
-ATOM   3390  N   SER B 786     -59.983 -26.330   1.920  1.00 66.36           N  
-ANISOU 3390  N   SER B 786     8844   6737   9631    972   -492   -481       N  
-ATOM   3391  CA  SER B 786     -58.785 -26.020   2.706  1.00 69.62           C  
-ANISOU 3391  CA  SER B 786     9142   7166  10145   1064   -545   -463       C  
-ATOM   3392  C   SER B 786     -58.969 -24.984   3.858  1.00 73.62           C  
-ANISOU 3392  C   SER B 786     9588   7764  10618   1020   -622   -392       C  
-ATOM   3393  O   SER B 786     -58.407 -25.167   4.942  1.00 76.36           O  
-ANISOU 3393  O   SER B 786     9905   8090  11017   1075   -714   -345       O  
-ATOM   3394  CB  SER B 786     -57.630 -25.591   1.787  1.00 69.44           C  
-ANISOU 3394  CB  SER B 786     9000   7178  10206   1136   -455   -538       C  
-ATOM   3395  N   LYS B 787     -59.724 -23.902   3.624  1.00 71.95           N  
-ANISOU 3395  N   LYS B 787     9361   7653  10323    924   -586   -385       N  
-ATOM   3396  CA  LYS B 787     -60.030 -22.887   4.669  1.00 70.51           C  
-ANISOU 3396  CA  LYS B 787     9136   7556  10098    873   -650   -325       C  
-ATOM   3397  C   LYS B 787     -61.222 -23.310   5.558  1.00 63.36           C  
-ANISOU 3397  C   LYS B 787     8345   6628   9102    802   -722   -255       C  
-ATOM   3398  O   LYS B 787     -62.045 -24.110   5.133  1.00 61.74           O  
-ANISOU 3398  O   LYS B 787     8247   6365   8846    761   -703   -257       O  
-ATOM   3399  CB  LYS B 787     -60.322 -21.519   4.006  1.00 68.59           C  
-ANISOU 3399  CB  LYS B 787     8826   7425   9809    806   -576   -349       C  
-ATOM   3400  N   ASP B 788     -61.304 -22.787   6.785  1.00 62.17           N  
-ANISOU 3400  N   ASP B 788     8171   6520   8929    785   -803   -195       N  
-ATOM   3401  CA  ASP B 788     -62.515 -22.941   7.620  1.00 63.96           C  
-ANISOU 3401  CA  ASP B 788     8494   6751   9056    703   -857   -129       C  
-ATOM   3402  C   ASP B 788     -63.717 -22.489   6.785  1.00 65.43           C  
-ANISOU 3402  C   ASP B 788     8720   6988   9151    604   -781   -145       C  
-ATOM   3403  O   ASP B 788     -63.664 -21.415   6.177  1.00 64.86           O  
-ANISOU 3403  O   ASP B 788     8573   6998   9073    581   -720   -178       O  
-ATOM   3404  CB  ASP B 788     -62.418 -22.084   8.900  1.00 62.20           C  
-ANISOU 3404  CB  ASP B 788     8222   6599   8813    689   -931    -77       C  
-ATOM   3405  CG  ASP B 788     -63.554 -22.362   9.905  1.00 62.73           C  
-ANISOU 3405  CG  ASP B 788     8388   6664   8781    615   -991     -5       C  
-ATOM   3406  OD1 ASP B 788     -64.620 -22.856   9.494  1.00 60.62           O  
-ANISOU 3406  OD1 ASP B 788     8210   6373   8448    550   -959      3       O  
-ATOM   3407  OD2 ASP B 788     -63.397 -22.069  11.121  1.00 68.67           O  
-ANISOU 3407  OD2 ASP B 788     9129   7443   9518    617  -1070     44       O  
-ATOM   3408  N   PRO B 789     -64.791 -23.296   6.737  1.00 63.83           N  
-ANISOU 3408  N   PRO B 789     8632   6739   8880    543   -786   -120       N  
-ATOM   3409  CA  PRO B 789     -65.962 -22.908   5.942  1.00 61.44           C  
-ANISOU 3409  CA  PRO B 789     8364   6488   8492    447   -721   -132       C  
-ATOM   3410  C   PRO B 789     -66.572 -21.542   6.300  1.00 61.90           C  
-ANISOU 3410  C   PRO B 789     8366   6663   8489    384   -714   -106       C  
-ATOM   3411  O   PRO B 789     -67.044 -20.842   5.408  1.00 54.19           O  
-ANISOU 3411  O   PRO B 789     7364   5747   7477    337   -646   -135       O  
-ATOM   3412  CB  PRO B 789     -66.957 -24.031   6.216  1.00 62.16           C  
-ANISOU 3412  CB  PRO B 789     8584   6509   8526    392   -755    -93       C  
-ATOM   3413  CG  PRO B 789     -66.093 -25.216   6.484  1.00 63.77           C  
-ANISOU 3413  CG  PRO B 789     8827   6596   8807    478   -799    -95       C  
-ATOM   3414  CD  PRO B 789     -64.897 -24.684   7.223  1.00 63.94           C  
-ANISOU 3414  CD  PRO B 789     8749   6641   8903    563   -844    -87       C  
-ATOM   3415  N   ILE B 790     -66.559 -21.168   7.577  1.00 62.05           N  
-ANISOU 3415  N   ILE B 790     8369   6711   8495    382   -783    -55       N  
-ATOM   3416  CA  ILE B 790     -67.031 -19.846   7.981  1.00 63.34           C  
-ANISOU 3416  CA  ILE B 790     8478   6979   8609    333   -775    -37       C  
-ATOM   3417  C   ILE B 790     -66.257 -18.767   7.209  1.00 60.16           C  
-ANISOU 3417  C   ILE B 790     7967   6633   8257    364   -716    -90       C  
-ATOM   3418  O   ILE B 790     -66.860 -17.819   6.712  1.00 58.94           O  
-ANISOU 3418  O   ILE B 790     7785   6550   8060    311   -664    -99       O  
-ATOM   3419  CB  ILE B 790     -66.902 -19.637   9.501  1.00 69.16           C  
-ANISOU 3419  CB  ILE B 790     9213   7733   9332    340   -860     18       C  
-ATOM   3420  CG1 ILE B 790     -67.896 -20.532  10.246  1.00 76.63           C  
-ANISOU 3420  CG1 ILE B 790    10268   8640  10206    287   -907     78       C  
-ATOM   3421  CG2 ILE B 790     -67.195 -18.192   9.882  1.00 71.97           C  
-ANISOU 3421  CG2 ILE B 790     9504   8191   9650    301   -847     23       C  
-ATOM   3422  CD1 ILE B 790     -67.427 -20.940  11.631  1.00 82.07           C  
-ANISOU 3422  CD1 ILE B 790    10981   9299  10902    321  -1003    129       C  
-ATOM   3423  N   ASP B 791     -64.935 -18.924   7.105  1.00 56.08           N  
-ANISOU 3423  N   ASP B 791     7390   6083   7834    448   -724   -122       N  
-ATOM   3424  CA  ASP B 791     -64.091 -17.976   6.375  1.00 54.77           C  
-ANISOU 3424  CA  ASP B 791     7119   5967   7726    478   -666   -172       C  
-ATOM   3425  C   ASP B 791     -64.375 -17.987   4.872  1.00 52.86           C  
-ANISOU 3425  C   ASP B 791     6886   5728   7470    455   -569   -220       C  
-ATOM   3426  O   ASP B 791     -64.322 -16.938   4.221  1.00 54.52           O  
-ANISOU 3426  O   ASP B 791     7034   6006   7677    433   -510   -244       O  
-ATOM   3427  CB  ASP B 791     -62.597 -18.258   6.591  1.00 55.02           C  
-ANISOU 3427  CB  ASP B 791     7078   5961   7867    576   -696   -195       C  
-ATOM   3428  CG  ASP B 791     -62.092 -17.820   7.961  1.00 56.52           C  
-ANISOU 3428  CG  ASP B 791     7224   6176   8076    597   -786   -156       C  
-ATOM   3429  OD1 ASP B 791     -60.855 -17.786   8.126  1.00 62.52           O  
-ANISOU 3429  OD1 ASP B 791     7902   6927   8927    670   -810   -175       O  
-ATOM   3430  OD2 ASP B 791     -62.891 -17.512   8.876  1.00 55.97           O  
-ANISOU 3430  OD2 ASP B 791     7196   6137   7932    543   -832   -109       O  
-ATOM   3431  N   VAL B 792     -64.678 -19.156   4.316  1.00 50.54           N  
-ANISOU 3431  N   VAL B 792     6675   5363   7166    458   -554   -234       N  
-ATOM   3432  CA  VAL B 792     -64.986 -19.244   2.895  1.00 48.18           C  
-ANISOU 3432  CA  VAL B 792     6396   5065   6843    431   -467   -282       C  
-ATOM   3433  C   VAL B 792     -66.254 -18.451   2.608  1.00 48.37           C  
-ANISOU 3433  C   VAL B 792     6441   5166   6773    335   -439   -259       C  
-ATOM   3434  O   VAL B 792     -66.309 -17.683   1.654  1.00 49.14           O  
-ANISOU 3434  O   VAL B 792     6499   5317   6855    311   -371   -288       O  
-ATOM   3435  CB  VAL B 792     -65.188 -20.695   2.422  1.00 49.97           C  
-ANISOU 3435  CB  VAL B 792     6723   5195   7068    441   -462   -303       C  
-ATOM   3436  CG1 VAL B 792     -65.694 -20.743   0.976  1.00 48.80           C  
-ANISOU 3436  CG1 VAL B 792     6611   5059   6873    395   -376   -350       C  
-ATOM   3437  CG2 VAL B 792     -63.887 -21.474   2.554  1.00 52.08           C  
-ANISOU 3437  CG2 VAL B 792     6966   5384   7439    548   -479   -332       C  
-ATOM   3438  N   ASN B 793     -67.276 -18.653   3.425  1.00 47.31           N  
-ANISOU 3438  N   ASN B 793     6367   5034   6574    280   -492   -205       N  
-ATOM   3439  CA  ASN B 793     -68.534 -17.986   3.221  1.00 46.36           C  
-ANISOU 3439  CA  ASN B 793     6264   4984   6368    194   -470   -178       C  
-ATOM   3440  C   ASN B 793     -68.463 -16.477   3.533  1.00 43.45           C  
-ANISOU 3440  C   ASN B 793     5808   4705   5998    184   -460   -166       C  
-ATOM   3441  O   ASN B 793     -69.087 -15.685   2.845  1.00 42.77           O  
-ANISOU 3441  O   ASN B 793     5703   4679   5869    137   -412   -169       O  
-ATOM   3442  CB  ASN B 793     -69.618 -18.677   4.032  1.00 47.55           C  
-ANISOU 3442  CB  ASN B 793     6500   5113   6455    139   -525   -124       C  
-ATOM   3443  CG  ASN B 793     -69.933 -20.076   3.526  1.00 48.18           C  
-ANISOU 3443  CG  ASN B 793     6677   5108   6523    125   -525   -137       C  
-ATOM   3444  OD1 ASN B 793     -70.115 -20.302   2.328  1.00 48.48           O  
-ANISOU 3444  OD1 ASN B 793     6737   5138   6546    105   -470   -179       O  
-ATOM   3445  ND2 ASN B 793     -70.063 -21.013   4.455  1.00 48.06           N  
-ANISOU 3445  ND2 ASN B 793     6727   5028   6506    129   -590    -99       N  
-ATOM   3446  N   TYR B 794     -67.676 -16.085   4.531  1.00 41.85           N  
-ANISOU 3446  N   TYR B 794     5552   4506   5843    231   -507   -154       N  
-ATOM   3447  CA  TYR B 794     -67.398 -14.675   4.786  1.00 40.74           C  
-ANISOU 3447  CA  TYR B 794     5326   4438   5715    229   -495   -154       C  
-ATOM   3448  C   TYR B 794     -66.897 -14.002   3.516  1.00 42.54           C  
-ANISOU 3448  C   TYR B 794     5495   4696   5974    237   -415   -200       C  
-ATOM   3449  O   TYR B 794     -67.413 -12.966   3.129  1.00 41.18           O  
-ANISOU 3449  O   TYR B 794     5294   4585   5767    195   -377   -194       O  
-ATOM   3450  CB  TYR B 794     -66.369 -14.516   5.891  1.00 40.07           C  
-ANISOU 3450  CB  TYR B 794     5191   4343   5691    285   -558   -147       C  
-ATOM   3451  CG  TYR B 794     -65.825 -13.112   6.078  1.00 36.98           C  
-ANISOU 3451  CG  TYR B 794     4707   4013   5329    290   -546   -158       C  
-ATOM   3452  CD1 TYR B 794     -66.589 -12.127   6.652  1.00 37.60           C  
-ANISOU 3452  CD1 TYR B 794     4781   4150   5354    241   -554   -131       C  
-ATOM   3453  CD2 TYR B 794     -64.528 -12.786   5.690  1.00 37.57           C  
-ANISOU 3453  CD2 TYR B 794     4698   4087   5491    344   -525   -198       C  
-ATOM   3454  CE1 TYR B 794     -66.086 -10.834   6.849  1.00 37.75           C  
-ANISOU 3454  CE1 TYR B 794     4723   4218   5403    243   -544   -144       C  
-ATOM   3455  CE2 TYR B 794     -64.016 -11.503   5.860  1.00 35.66           C  
-ANISOU 3455  CE2 TYR B 794     4372   3897   5278    340   -516   -209       C  
-ATOM   3456  CZ  TYR B 794     -64.797 -10.523   6.452  1.00 37.03           C  
-ANISOU 3456  CZ  TYR B 794     4551   4122   5396    289   -527   -181       C  
-ATOM   3457  OH  TYR B 794     -64.312  -9.238   6.659  1.00 33.39           O  
-ANISOU 3457  OH  TYR B 794     4016   3705   4964    283   -519   -193       O  
-ATOM   3458  N   GLU B 795     -65.915 -14.615   2.865  1.00 44.96           N  
-ANISOU 3458  N   GLU B 795     5784   4956   6344    292   -389   -244       N  
-ATOM   3459  CA  GLU B 795     -65.293 -14.053   1.652  1.00 48.11           C  
-ANISOU 3459  CA  GLU B 795     6124   5380   6775    304   -307   -291       C  
-ATOM   3460  C   GLU B 795     -66.274 -13.935   0.517  1.00 45.66           C  
-ANISOU 3460  C   GLU B 795     5861   5098   6391    242   -246   -296       C  
-ATOM   3461  O   GLU B 795     -66.197 -12.986  -0.266  1.00 45.97           O  
-ANISOU 3461  O   GLU B 795     5853   5189   6423    221   -187   -309       O  
-ATOM   3462  CB  GLU B 795     -64.070 -14.870   1.208  1.00 50.00           C  
-ANISOU 3462  CB  GLU B 795     6340   5562   7096    380   -287   -339       C  
-ATOM   3463  CG  GLU B 795     -62.863 -14.657   2.124  1.00 56.36           C  
-ANISOU 3463  CG  GLU B 795     7062   6361   7991    447   -336   -340       C  
-ATOM   3464  CD  GLU B 795     -61.663 -15.560   1.823  1.00 62.46           C  
-ANISOU 3464  CD  GLU B 795     7806   7072   8854    532   -325   -383       C  
-ATOM   3465  OE1 GLU B 795     -61.748 -16.478   0.966  1.00 62.43           O  
-ANISOU 3465  OE1 GLU B 795     7857   7018   8843    546   -281   -416       O  
-ATOM   3466  OE2 GLU B 795     -60.611 -15.350   2.469  1.00 64.72           O  
-ANISOU 3466  OE2 GLU B 795     8012   7359   9220    588   -363   -385       O  
-ATOM   3467  N   LYS B 796     -67.235 -14.856   0.470  1.00 44.76           N  
-ANISOU 3467  N   LYS B 796     5838   4951   6216    205   -265   -280       N  
-ATOM   3468  CA  LYS B 796     -68.265 -14.844  -0.544  1.00 45.42           C  
-ANISOU 3468  CA  LYS B 796     5972   5062   6223    139   -220   -281       C  
-ATOM   3469  C   LYS B 796     -69.206 -13.590  -0.441  1.00 45.53           C  
-ANISOU 3469  C   LYS B 796     5958   5159   6181     79   -216   -239       C  
-ATOM   3470  O   LYS B 796     -69.781 -13.170  -1.444  1.00 41.61           O  
-ANISOU 3470  O   LYS B 796     5470   4705   5637     34   -168   -242       O  
-ATOM   3471  CB  LYS B 796     -69.056 -16.184  -0.511  1.00 48.98           C  
-ANISOU 3471  CB  LYS B 796     6527   5455   6629    109   -251   -272       C  
-ATOM   3472  N   LEU B 797     -69.331 -12.988   0.754  1.00 41.28           N  
-ANISOU 3472  N   LEU B 797     5389   4645   5650     81   -265   -201       N  
-ATOM   3473  CA  LEU B 797     -70.085 -11.754   0.939  1.00 39.57           C  
-ANISOU 3473  CA  LEU B 797     5140   4499   5394     39   -258   -167       C  
-ATOM   3474  C   LEU B 797     -69.414 -10.525   0.313  1.00 38.83           C  
-ANISOU 3474  C   LEU B 797     4969   4447   5337     52   -205   -187       C  
-ATOM   3475  O   LEU B 797     -70.081  -9.540   0.092  1.00 37.12           O  
-ANISOU 3475  O   LEU B 797     4735   4284   5086     16   -185   -164       O  
-ATOM   3476  CB  LEU B 797     -70.335 -11.464   2.423  1.00 39.81           C  
-ANISOU 3476  CB  LEU B 797     5164   4540   5422     41   -321   -129       C  
-ATOM   3477  CG  LEU B 797     -71.078 -12.555   3.193  1.00 42.05           C  
-ANISOU 3477  CG  LEU B 797     5523   4790   5664     19   -375    -98       C  
-ATOM   3478  CD1 LEU B 797     -71.091 -12.230   4.673  1.00 41.03           C  
-ANISOU 3478  CD1 LEU B 797     5383   4672   5535     28   -433    -66       C  
-ATOM   3479  CD2 LEU B 797     -72.494 -12.745   2.676  1.00 41.96           C  
-ANISOU 3479  CD2 LEU B 797     5562   4808   5574    -52   -358    -72       C  
-ATOM   3480  N   LYS B 798     -68.115 -10.588   0.060  1.00 38.95           N  
-ANISOU 3480  N   LYS B 798     4939   4438   5424    105   -184   -227       N  
-ATOM   3481  CA  LYS B 798     -67.344  -9.484  -0.513  1.00 41.82           C  
-ANISOU 3481  CA  LYS B 798     5226   4836   5829    116   -132   -247       C  
-ATOM   3482  C   LYS B 798     -67.560  -8.196   0.289  1.00 38.50           C  
-ANISOU 3482  C   LYS B 798     4759   4458   5412    100   -155   -216       C  
-ATOM   3483  O   LYS B 798     -67.825  -7.127  -0.261  1.00 36.75           O  
-ANISOU 3483  O   LYS B 798     4510   4279   5174     71   -113   -206       O  
-ATOM   3484  CB  LYS B 798     -67.703  -9.293  -1.972  1.00 45.36           C  
-ANISOU 3484  CB  LYS B 798     5690   5309   6234     81    -60   -259       C  
-ATOM   3485  CG  LYS B 798     -67.264 -10.426  -2.892  1.00 50.82           C  
-ANISOU 3485  CG  LYS B 798     6420   5960   6930    101    -22   -305       C  
-ATOM   3486  CD  LYS B 798     -67.481 -10.009  -4.352  1.00 58.31           C  
-ANISOU 3486  CD  LYS B 798     7376   6945   7834     63     54   -318       C  
-ATOM   3487  CE  LYS B 798     -67.464 -11.197  -5.314  1.00 64.71           C  
-ANISOU 3487  CE  LYS B 798     8253   7718   8616     63     89   -361       C  
-ATOM   3488  NZ  LYS B 798     -67.506 -10.777  -6.749  1.00 65.29           N  
-ANISOU 3488  NZ  LYS B 798     8332   7830   8644     30    167   -379       N  
-ATOM   3489  N   THR B 799     -67.480  -8.332   1.604  1.00 37.03           N  
-ANISOU 3489  N   THR B 799     4571   4257   5240    118   -222   -200       N  
-ATOM   3490  CA  THR B 799     -67.803  -7.258   2.517  1.00 37.23           C  
-ANISOU 3490  CA  THR B 799     4571   4317   5258    102   -250   -174       C  
-ATOM   3491  C   THR B 799     -66.835  -7.349   3.674  1.00 39.20           C  
-ANISOU 3491  C   THR B 799     4785   4544   5564    144   -309   -184       C  
-ATOM   3492  O   THR B 799     -66.734  -8.390   4.321  1.00 41.22           O  
-ANISOU 3492  O   THR B 799     5078   4763   5821    168   -361   -179       O  
-ATOM   3493  CB  THR B 799     -69.256  -7.380   3.045  1.00 34.53           C  
-ANISOU 3493  CB  THR B 799     4290   3995   4836     59   -278   -132       C  
-ATOM   3494  OG1 THR B 799     -70.166  -7.315   1.958  1.00 37.55           O  
-ANISOU 3494  OG1 THR B 799     4700   4403   5167     18   -230   -120       O  
-ATOM   3495  CG2 THR B 799     -69.603  -6.260   4.012  1.00 34.96           C  
-ANISOU 3495  CG2 THR B 799     4319   4084   4881     47   -300   -111       C  
-ATOM   3496  N   ASP B 800     -66.154  -6.253   3.973  1.00 38.68           N  
-ANISOU 3496  N   ASP B 800     4653   4500   5545    151   -307   -195       N  
-ATOM   3497  CA  ASP B 800     -65.330  -6.200   5.162  1.00 38.23           C  
-ANISOU 3497  CA  ASP B 800     4562   4431   5534    182   -373   -201       C  
-ATOM   3498  C   ASP B 800     -66.226  -5.972   6.383  1.00 36.00           C  
-ANISOU 3498  C   ASP B 800     4323   4163   5191    157   -427   -168       C  
-ATOM   3499  O   ASP B 800     -66.997  -5.046   6.409  1.00 34.75           O  
-ANISOU 3499  O   ASP B 800     4170   4038   4995    122   -405   -154       O  
-ATOM   3500  CB  ASP B 800     -64.293  -5.095   5.069  1.00 39.97           C  
-ANISOU 3500  CB  ASP B 800     4695   4669   5823    190   -354   -226       C  
-ATOM   3501  CG  ASP B 800     -63.297  -5.156   6.216  1.00 41.56           C  
-ANISOU 3501  CG  ASP B 800     4854   4858   6077    223   -428   -236       C  
-ATOM   3502  OD1 ASP B 800     -62.310  -5.893   6.102  1.00 45.99           O  
-ANISOU 3502  OD1 ASP B 800     5381   5394   6700    269   -443   -256       O  
-ATOM   3503  OD2 ASP B 800     -63.510  -4.491   7.247  1.00 42.76           O  
-ANISOU 3503  OD2 ASP B 800     5009   5027   6210    205   -474   -225       O  
-ATOM   3504  N   ILE B 801     -66.135  -6.856   7.372  1.00 36.03           N  
-ANISOU 3504  N   ILE B 801     4362   4141   5186    178   -496   -155       N  
-ATOM   3505  CA  ILE B 801     -66.931  -6.759   8.585  1.00 35.00           C  
-ANISOU 3505  CA  ILE B 801     4279   4026   4994    154   -547   -124       C  
-ATOM   3506  C   ILE B 801     -66.036  -6.709   9.813  1.00 35.55           C  
-ANISOU 3506  C   ILE B 801     4324   4087   5095    181   -623   -128       C  
-ATOM   3507  O   ILE B 801     -65.260  -7.634  10.041  1.00 39.41           O  
-ANISOU 3507  O   ILE B 801     4812   4540   5624    222   -668   -131       O  
-ATOM   3508  CB  ILE B 801     -67.890  -7.960   8.725  1.00 34.13           C  
-ANISOU 3508  CB  ILE B 801     4252   3894   4820    139   -564    -91       C  
-ATOM   3509  CG1 ILE B 801     -68.709  -8.148   7.454  1.00 34.27           C  
-ANISOU 3509  CG1 ILE B 801     4293   3919   4808    110   -497    -89       C  
-ATOM   3510  CG2 ILE B 801     -68.799  -7.749   9.924  1.00 34.94           C  
-ANISOU 3510  CG2 ILE B 801     4400   4023   4853    107   -602    -58       C  
-ATOM   3511  CD1 ILE B 801     -69.666  -9.328   7.485  1.00 34.62           C  
-ANISOU 3511  CD1 ILE B 801     4419   3942   4793     85   -511    -59       C  
-ATOM   3512  N   LYS B 802     -66.149  -5.642  10.594  1.00 34.05           N  
-ANISOU 3512  N   LYS B 802     4119   3929   4888    160   -640   -130       N  
-ATOM   3513  CA  LYS B 802     -65.375  -5.463  11.810  1.00 38.68           C  
-ANISOU 3513  CA  LYS B 802     4687   4516   5493    176   -716   -136       C  
-ATOM   3514  C   LYS B 802     -66.304  -5.229  12.979  1.00 37.82           C  
-ANISOU 3514  C   LYS B 802     4639   4431   5300    144   -750   -111       C  
-ATOM   3515  O   LYS B 802     -67.326  -4.568  12.841  1.00 37.17           O  
-ANISOU 3515  O   LYS B 802     4578   4377   5168    109   -703   -104       O  
-ATOM   3516  CB  LYS B 802     -64.458  -4.239  11.715  1.00 43.32           C  
-ANISOU 3516  CB  LYS B 802     5194   5122   6145    176   -706   -172       C  
-ATOM   3517  CG  LYS B 802     -63.217  -4.441  10.857  1.00 49.80           C  
-ANISOU 3517  CG  LYS B 802     5937   5923   7060    213   -688   -199       C  
-ATOM   3518  CD  LYS B 802     -62.403  -3.143  10.823  1.00 56.61           C  
-ANISOU 3518  CD  LYS B 802     6721   6808   7981    199   -676   -231       C  
-ATOM   3519  CE  LYS B 802     -61.055  -3.299  10.103  1.00 59.21           C  
-ANISOU 3519  CE  LYS B 802     6962   7126   8411    234   -661   -259       C  
-ATOM   3520  NZ  LYS B 802     -61.179  -3.373   8.615  1.00 57.06           N  
-ANISOU 3520  NZ  LYS B 802     6675   6850   8156    234   -566   -268       N  
-ATOM   3521  N   VAL B 803     -65.924  -5.750  14.138  1.00 36.35           N  
-ANISOU 3521  N   VAL B 803     4478   4236   5099    158   -832    -97       N  
-ATOM   3522  CA  VAL B 803     -66.677  -5.552  15.343  1.00 36.27           C  
-ANISOU 3522  CA  VAL B 803     4527   4251   5005    128   -867    -77       C  
-ATOM   3523  C   VAL B 803     -66.360  -4.172  15.886  1.00 36.26           C  
-ANISOU 3523  C   VAL B 803     4488   4280   5010    111   -872   -110       C  
-ATOM   3524  O   VAL B 803     -65.210  -3.792  15.948  1.00 35.58           O  
-ANISOU 3524  O   VAL B 803     4341   4188   4990    130   -904   -137       O  
-ATOM   3525  CB  VAL B 803     -66.314  -6.601  16.408  1.00 37.43           C  
-ANISOU 3525  CB  VAL B 803     4718   4375   5127    146   -958    -47       C  
-ATOM   3526  CG1 VAL B 803     -67.079  -6.325  17.696  1.00 37.58           C  
-ANISOU 3526  CG1 VAL B 803     4801   4427   5051    110   -990    -28       C  
-ATOM   3527  CG2 VAL B 803     -66.611  -7.996  15.898  1.00 35.93           C  
-ANISOU 3527  CG2 VAL B 803     4573   4144   4935    162   -956    -15       C  
-ATOM   3528  N   VAL B 804     -67.388  -3.405  16.229  1.00 37.06           N  
-ANISOU 3528  N   VAL B 804     4623   4413   5047     75   -836   -109       N  
-ATOM   3529  CA  VAL B 804     -67.195  -2.122  16.900  1.00 39.58           C  
-ANISOU 3529  CA  VAL B 804     4923   4754   5360     57   -843   -142       C  
-ATOM   3530  C   VAL B 804     -67.127  -2.378  18.422  1.00 43.17           C  
-ANISOU 3530  C   VAL B 804     5430   5222   5750     48   -924   -133       C  
-ATOM   3531  O   VAL B 804     -68.032  -2.977  19.001  1.00 45.26           O  
-ANISOU 3531  O   VAL B 804     5763   5498   5934     33   -929   -100       O  
-ATOM   3532  CB  VAL B 804     -68.332  -1.138  16.560  1.00 38.15           C  
-ANISOU 3532  CB  VAL B 804     4754   4597   5143     29   -763   -148       C  
-ATOM   3533  CG1 VAL B 804     -68.214   0.134  17.395  1.00 36.42           C  
-ANISOU 3533  CG1 VAL B 804     4533   4395   4911     11   -772   -185       C  
-ATOM   3534  CG2 VAL B 804     -68.332  -0.806  15.063  1.00 36.65           C  
-ANISOU 3534  CG2 VAL B 804     4514   4397   5014     35   -690   -154       C  
-ATOM   3535  N   ASP B 805     -66.061  -1.910  19.055  1.00 47.49           N  
-ANISOU 3535  N   ASP B 805     5943   5769   6330     54   -986   -162       N  
-ATOM   3536  CA  ASP B 805     -65.842  -2.094  20.492  1.00 47.88           C  
-ANISOU 3536  CA  ASP B 805     6039   5833   6319     44  -1072   -156       C  
-ATOM   3537  C   ASP B 805     -67.014  -1.505  21.273  1.00 46.41           C  
-ANISOU 3537  C   ASP B 805     5921   5680   6032      6  -1041   -158       C  
-ATOM   3538  O   ASP B 805     -67.383  -0.348  21.066  1.00 49.97           O  
-ANISOU 3538  O   ASP B 805     6358   6143   6487    -11   -983   -193       O  
-ATOM   3539  CB  ASP B 805     -64.529  -1.397  20.888  1.00 53.10           C  
-ANISOU 3539  CB  ASP B 805     6641   6496   7040     47  -1134   -196       C  
-ATOM   3540  CG  ASP B 805     -64.160  -1.568  22.380  1.00 62.24           C  
-ANISOU 3540  CG  ASP B 805     7843   7671   8134     36  -1237   -192       C  
-ATOM   3541  OD1 ASP B 805     -63.270  -2.382  22.686  1.00 67.31           O  
-ANISOU 3541  OD1 ASP B 805     8467   8300   8807     63  -1320   -171       O  
-ATOM   3542  OD2 ASP B 805     -64.735  -0.883  23.255  1.00 65.85           O  
-ANISOU 3542  OD2 ASP B 805     8353   8154   8512      0  -1236   -210       O  
-ATOM   3543  N   ARG B 806     -67.588  -2.304  22.169  1.00 47.67           N  
-ANISOU 3543  N   ARG B 806     6156   5852   6103     -5  -1077   -121       N  
-ATOM   3544  CA  ARG B 806     -68.745  -1.911  22.995  1.00 50.49           C  
-ANISOU 3544  CA  ARG B 806     6583   6246   6356    -40  -1045   -119       C  
-ATOM   3545  C   ARG B 806     -68.532  -0.641  23.807  1.00 53.85           C  
-ANISOU 3545  C   ARG B 806     7012   6694   6756    -61  -1055   -172       C  
-ATOM   3546  O   ARG B 806     -69.483   0.066  24.091  1.00 50.54           O  
-ANISOU 3546  O   ARG B 806     6625   6299   6280    -82   -995   -189       O  
-ATOM   3547  CB  ARG B 806     -69.093  -3.041  23.974  1.00 53.38           C  
-ANISOU 3547  CB  ARG B 806     7029   6621   6633    -50  -1101    -68       C  
-ATOM   3548  N   ASP B 807     -67.278  -0.353  24.162  1.00 58.82           N  
-ANISOU 3548  N   ASP B 807     7605   7314   7431    -54  -1130   -201       N  
-ATOM   3549  CA  ASP B 807     -66.930   0.824  24.958  1.00 61.55           C  
-ANISOU 3549  CA  ASP B 807     7955   7674   7756    -80  -1152   -256       C  
-ATOM   3550  C   ASP B 807     -66.564   2.049  24.136  1.00 60.44           C  
-ANISOU 3550  C   ASP B 807     7746   7516   7703    -81  -1100   -307       C  
-ATOM   3551  O   ASP B 807     -66.266   3.081  24.722  1.00 65.66           O  
-ANISOU 3551  O   ASP B 807     8410   8182   8354   -105  -1114   -358       O  
-ATOM   3552  CB  ASP B 807     -65.743   0.520  25.869  1.00 67.84           C  
-ANISOU 3552  CB  ASP B 807     8751   8475   8552    -81  -1273   -260       C  
-ATOM   3553  CG  ASP B 807     -66.009  -0.625  26.821  1.00 71.29           C  
-ANISOU 3553  CG  ASP B 807     9264   8927   8896    -83  -1338   -207       C  
-ATOM   3554  OD1 ASP B 807     -67.161  -0.799  27.272  1.00 76.55           O  
-ANISOU 3554  OD1 ASP B 807    10004   9616   9466   -103  -1293   -187       O  
-ATOM   3555  OD2 ASP B 807     -65.051  -1.360  27.121  1.00 76.42           O  
-ANISOU 3555  OD2 ASP B 807     9897   9566   9571    -63  -1434   -182       O  
-ATOM   3556  N   SER B 808     -66.546   1.950  22.807  1.00 55.01           N  
-ANISOU 3556  N   SER B 808     6999   6805   7096    -59  -1042   -295       N  
-ATOM   3557  CA  SER B 808     -66.142   3.083  21.967  1.00 53.02           C  
-ANISOU 3557  CA  SER B 808     6682   6534   6929    -63   -992   -336       C  
-ATOM   3558  C   SER B 808     -67.206   4.151  21.983  1.00 54.09           C  
-ANISOU 3558  C   SER B 808     6851   6675   7026    -80   -911   -361       C  
-ATOM   3559  O   SER B 808     -68.353   3.895  22.375  1.00 51.54           O  
-ANISOU 3559  O   SER B 808     6588   6374   6620    -84   -877   -340       O  
-ATOM   3560  CB  SER B 808     -65.901   2.638  20.520  1.00 54.88           C  
-ANISOU 3560  CB  SER B 808     6854   6748   7251    -36   -947   -312       C  
-ATOM   3561  OG  SER B 808     -67.088   2.127  19.924  1.00 51.45           O  
-ANISOU 3561  OG  SER B 808     6452   6318   6779    -28   -879   -274       O  
-ATOM   3562  N   GLU B 809     -66.828   5.352  21.552  1.00 56.99           N  
-ANISOU 3562  N   GLU B 809     7177   7022   7456    -91   -879   -403       N  
-ATOM   3563  CA  GLU B 809     -67.793   6.448  21.434  1.00 58.59           C  
-ANISOU 3563  CA  GLU B 809     7405   7219   7638   -100   -797   -427       C  
-ATOM   3564  C   GLU B 809     -68.728   6.176  20.250  1.00 50.42           C  
-ANISOU 3564  C   GLU B 809     6354   6183   6619    -79   -714   -385       C  
-ATOM   3565  O   GLU B 809     -69.908   6.506  20.281  1.00 45.48           O  
-ANISOU 3565  O   GLU B 809     5764   5570   5947    -76   -652   -378       O  
-ATOM   3566  CB  GLU B 809     -67.082   7.800  21.303  1.00 63.40           C  
-ANISOU 3566  CB  GLU B 809     7979   7796   8313   -121   -791   -482       C  
-ATOM   3567  CG  GLU B 809     -68.022   9.005  21.327  1.00 69.48           C  
-ANISOU 3567  CG  GLU B 809     8784   8553   9065   -126   -714   -511       C  
-ATOM   3568  CD  GLU B 809     -67.306  10.346  21.074  1.00 74.53           C  
-ANISOU 3568  CD  GLU B 809     9390   9147   9778   -149   -704   -562       C  
-ATOM   3569  OE1 GLU B 809     -66.108  10.476  21.443  1.00 74.11           O  
-ANISOU 3569  OE1 GLU B 809     9309   9086   9762   -174   -774   -592       O  
-ATOM   3570  OE2 GLU B 809     -67.933  11.299  20.547  1.00 74.75           O  
-ANISOU 3570  OE2 GLU B 809     9423   9148   9830   -144   -628   -572       O  
-ATOM   3571  N   GLU B 810     -68.182   5.536  19.229  1.00 48.20           N  
-ANISOU 3571  N   GLU B 810     6020   5890   6403    -64   -714   -357       N  
-ATOM   3572  CA  GLU B 810     -68.955   5.086  18.074  1.00 46.45           C  
-ANISOU 3572  CA  GLU B 810     5785   5670   6192    -47   -648   -314       C  
-ATOM   3573  C   GLU B 810     -70.163   4.245  18.563  1.00 42.96           C  
-ANISOU 3573  C   GLU B 810     5405   5260   5658    -45   -638   -277       C  
-ATOM   3574  O   GLU B 810     -71.307   4.534  18.231  1.00 36.64           O  
-ANISOU 3574  O   GLU B 810     4618   4473   4829    -44   -573   -262       O  
-ATOM   3575  CB  GLU B 810     -68.012   4.272  17.179  1.00 47.73           C  
-ANISOU 3575  CB  GLU B 810     5893   5818   6423    -31   -669   -296       C  
-ATOM   3576  CG  GLU B 810     -68.467   4.003  15.761  1.00 50.17           C  
-ANISOU 3576  CG  GLU B 810     6176   6121   6763    -19   -601   -265       C  
-ATOM   3577  CD  GLU B 810     -67.348   3.405  14.903  1.00 53.49           C  
-ANISOU 3577  CD  GLU B 810     6538   6524   7259     -4   -616   -261       C  
-ATOM   3578  OE1 GLU B 810     -66.356   2.877  15.450  1.00 50.38           O  
-ANISOU 3578  OE1 GLU B 810     6128   6126   6888      5   -685   -272       O  
-ATOM   3579  OE2 GLU B 810     -67.443   3.470  13.658  1.00 62.98           O  
-ANISOU 3579  OE2 GLU B 810     7710   7719   8500      1   -557   -249       O  
-ATOM   3580  N   ALA B 811     -69.887   3.225  19.378  1.00 41.06           N  
-ANISOU 3580  N   ALA B 811     5197   5031   5372    -46   -706   -261       N  
-ATOM   3581  CA  ALA B 811     -70.924   2.352  19.878  1.00 39.64           C  
-ANISOU 3581  CA  ALA B 811     5076   4880   5107    -51   -702   -222       C  
-ATOM   3582  C   ALA B 811     -71.940   3.132  20.724  1.00 40.17           C  
-ANISOU 3582  C   ALA B 811     5188   4974   5098    -67   -664   -240       C  
-ATOM   3583  O   ALA B 811     -73.126   2.846  20.679  1.00 41.21           O  
-ANISOU 3583  O   ALA B 811     5347   5133   5179    -71   -615   -211       O  
-ATOM   3584  CB  ALA B 811     -70.317   1.191  20.663  1.00 41.33           C  
-ANISOU 3584  CB  ALA B 811     5320   5094   5289    -51   -789   -200       C  
-ATOM   3585  N   GLU B 812     -71.462   4.113  21.487  1.00 44.81           N  
-ANISOU 3585  N   GLU B 812     5785   5557   5683    -77   -684   -292       N  
-ATOM   3586  CA  GLU B 812     -72.302   4.925  22.392  1.00 46.83           C  
-ANISOU 3586  CA  GLU B 812     6089   5834   5868    -89   -648   -322       C  
-ATOM   3587  C   GLU B 812     -73.325   5.705  21.612  1.00 41.99           C  
-ANISOU 3587  C   GLU B 812     5457   5221   5277    -76   -553   -321       C  
-ATOM   3588  O   GLU B 812     -74.520   5.741  21.959  1.00 40.01           O  
-ANISOU 3588  O   GLU B 812     5237   5001   4963    -76   -502   -310       O  
-ATOM   3589  CB  GLU B 812     -71.434   5.938  23.232  1.00 52.49           C  
-ANISOU 3589  CB  GLU B 812     6817   6535   6590   -104   -691   -387       C  
-ATOM   3590  CG  GLU B 812     -70.889   5.360  24.543  1.00 57.96           C  
-ANISOU 3590  CG  GLU B 812     7562   7250   7212   -124   -780   -393       C  
-ATOM   3591  CD  GLU B 812     -69.780   6.202  25.177  1.00 65.43           C  
-ANISOU 3591  CD  GLU B 812     8504   8177   8179   -143   -841   -454       C  
-ATOM   3592  OE1 GLU B 812     -69.563   7.363  24.739  1.00 65.69           O  
-ANISOU 3592  OE1 GLU B 812     8506   8180   8274   -145   -804   -498       O  
-ATOM   3593  OE2 GLU B 812     -69.124   5.693  26.124  1.00 68.04           O  
-ANISOU 3593  OE2 GLU B 812     8865   8523   8464   -159   -930   -455       O  
-ATOM   3594  N   ILE B 813     -72.840   6.347  20.555  1.00 40.46           N  
-ANISOU 3594  N   ILE B 813     5206   4992   5174    -64   -529   -331       N  
-ATOM   3595  CA  ILE B 813     -73.699   7.105  19.641  1.00 37.89           C  
-ANISOU 3595  CA  ILE B 813     4856   4660   4882    -48   -445   -323       C  
-ATOM   3596  C   ILE B 813     -74.774   6.171  19.102  1.00 36.62           C  
-ANISOU 3596  C   ILE B 813     4695   4533   4687    -42   -410   -264       C  
-ATOM   3597  O   ILE B 813     -75.975   6.524  19.083  1.00 34.90           O  
-ANISOU 3597  O   ILE B 813     4485   4339   4438    -34   -349   -253       O  
-ATOM   3598  CB  ILE B 813     -72.871   7.744  18.493  1.00 38.40           C  
-ANISOU 3598  CB  ILE B 813     4861   4682   5049    -43   -434   -332       C  
-ATOM   3599  CG1 ILE B 813     -71.811   8.707  19.162  1.00 40.68           C  
-ANISOU 3599  CG1 ILE B 813     5151   4937   5368    -59   -473   -394       C  
-ATOM   3600  CG2 ILE B 813     -73.796   8.417  17.447  1.00 39.08           C  
-ANISOU 3600  CG2 ILE B 813     4923   4762   5166    -25   -352   -310       C  
-ATOM   3601  CD1 ILE B 813     -71.032   9.686  18.284  1.00 41.73           C  
-ANISOU 3601  CD1 ILE B 813     5234   5023   5596    -62   -455   -415       C  
-ATOM   3602  N   ILE B 814     -74.356   4.992  18.650  1.00 35.44           N  
-ANISOU 3602  N   ILE B 814     4534   4385   4547    -46   -448   -228       N  
-ATOM   3603  CA  ILE B 814     -75.286   4.061  18.004  1.00 34.99           C  
-ANISOU 3603  CA  ILE B 814     4476   4353   4465    -47   -419   -174       C  
-ATOM   3604  C   ILE B 814     -76.326   3.570  18.997  1.00 35.71           C  
-ANISOU 3604  C   ILE B 814     4617   4487   4462    -61   -412   -155       C  
-ATOM   3605  O   ILE B 814     -77.504   3.486  18.655  1.00 35.95           O  
-ANISOU 3605  O   ILE B 814     4644   4549   4468    -63   -358   -125       O  
-ATOM   3606  CB  ILE B 814     -74.529   2.903  17.319  1.00 35.57           C  
-ANISOU 3606  CB  ILE B 814     4534   4409   4573    -47   -462   -146       C  
-ATOM   3607  CG1 ILE B 814     -73.833   3.446  16.068  1.00 35.33           C  
-ANISOU 3607  CG1 ILE B 814     4446   4347   4632    -34   -440   -156       C  
-ATOM   3608  CG2 ILE B 814     -75.484   1.775  16.938  1.00 35.69           C  
-ANISOU 3608  CG2 ILE B 814     4566   4449   4545    -58   -446    -93       C  
-ATOM   3609  CD1 ILE B 814     -72.879   2.486  15.387  1.00 36.75           C  
-ANISOU 3609  CD1 ILE B 814     4603   4504   4857    -28   -477   -144       C  
-ATOM   3610  N   ARG B 815     -75.908   3.271  20.225  1.00 37.02           N  
-ANISOU 3610  N   ARG B 815     4830   4661   4575    -74   -464   -172       N  
-ATOM   3611  CA  ARG B 815     -76.852   2.853  21.275  1.00 39.51           C  
-ANISOU 3611  CA  ARG B 815     5199   5020   4792    -93   -454   -156       C  
-ATOM   3612  C   ARG B 815     -77.804   3.972  21.638  1.00 37.16           C  
-ANISOU 3612  C   ARG B 815     4904   4746   4468    -85   -383   -185       C  
-ATOM   3613  O   ARG B 815     -78.970   3.714  21.901  1.00 35.81           O  
-ANISOU 3613  O   ARG B 815     4749   4619   4240    -94   -337   -160       O  
-ATOM   3614  CB  ARG B 815     -76.140   2.331  22.538  1.00 42.50           C  
-ANISOU 3614  CB  ARG B 815     5634   5402   5113   -110   -531   -166       C  
-ATOM   3615  CG  ARG B 815     -75.550   0.931  22.398  1.00 43.77           C  
-ANISOU 3615  CG  ARG B 815     5806   5548   5277   -117   -598   -122       C  
-ATOM   3616  CD  ARG B 815     -75.093   0.385  23.764  1.00 45.75           C  
-ANISOU 3616  CD  ARG B 815     6120   5809   5452   -135   -672   -120       C  
-ATOM   3617  NE  ARG B 815     -74.148   1.299  24.386  1.00 45.26           N  
-ANISOU 3617  NE  ARG B 815     6058   5735   5405   -131   -713   -177       N  
-ATOM   3618  CZ  ARG B 815     -72.825   1.200  24.319  1.00 46.18           C  
-ANISOU 3618  CZ  ARG B 815     6150   5819   5578   -120   -787   -191       C  
-ATOM   3619  NH1 ARG B 815     -72.092   2.144  24.889  1.00 50.17           N  
-ANISOU 3619  NH1 ARG B 815     6652   6317   6093   -124   -818   -246       N  
-ATOM   3620  NH2 ARG B 815     -72.222   0.188  23.701  1.00 44.50           N  
-ANISOU 3620  NH2 ARG B 815     5914   5581   5415   -106   -830   -154       N  
-ATOM   3621  N   LYS B 816     -77.334   5.214  21.607  1.00 37.24           N  
-ANISOU 3621  N   LYS B 816     4899   4727   4525    -69   -370   -237       N  
-ATOM   3622  CA  LYS B 816     -78.241   6.362  21.846  1.00 41.52           C  
-ANISOU 3622  CA  LYS B 816     5441   5280   5055    -52   -296   -268       C  
-ATOM   3623  C   LYS B 816     -79.297   6.434  20.748  1.00 38.46           C  
-ANISOU 3623  C   LYS B 816     5005   4907   4700    -34   -228   -226       C  
-ATOM   3624  O   LYS B 816     -80.480   6.661  21.014  1.00 39.93           O  
-ANISOU 3624  O   LYS B 816     5193   5132   4847    -26   -169   -218       O  
-ATOM   3625  CB  LYS B 816     -77.495   7.726  21.904  1.00 47.91           C  
-ANISOU 3625  CB  LYS B 816     6243   6041   5919    -39   -295   -331       C  
-ATOM   3626  CG  LYS B 816     -78.080   8.778  22.880  1.00 55.41           C  
-ANISOU 3626  CG  LYS B 816     7232   6998   6824    -30   -249   -386       C  
-ATOM   3627  CD  LYS B 816     -77.359  10.137  22.763  1.00 58.72           C  
-ANISOU 3627  CD  LYS B 816     7643   7357   7309    -19   -246   -447       C  
-ATOM   3628  CE  LYS B 816     -77.490  11.133  23.962  1.00 62.96           C  
-ANISOU 3628  CE  LYS B 816     8238   7887   7799    -20   -226   -521       C  
-ATOM   3629  NZ  LYS B 816     -78.858  11.597  24.378  1.00 64.17           N  
-ANISOU 3629  NZ  LYS B 816     8409   8069   7905      7   -140   -532       N  
-ATOM   3630  N   TYR B 817     -78.865   6.252  19.504  1.00 34.22           N  
-ANISOU 3630  N   TYR B 817     4423   4343   4235    -28   -238   -200       N  
-ATOM   3631  CA  TYR B 817     -79.788   6.344  18.382  1.00 31.30           C  
-ANISOU 3631  CA  TYR B 817     4008   3988   3897    -13   -183   -159       C  
-ATOM   3632  C   TYR B 817     -80.877   5.297  18.593  1.00 31.03           C  
-ANISOU 3632  C   TYR B 817     3984   4010   3795    -33   -168   -111       C  
-ATOM   3633  O   TYR B 817     -82.082   5.577  18.414  1.00 28.08           O  
-ANISOU 3633  O   TYR B 817     3588   3674   3408    -22   -110    -91       O  
-ATOM   3634  CB  TYR B 817     -79.027   6.117  17.078  1.00 28.86           C  
-ANISOU 3634  CB  TYR B 817     3660   3645   3661    -12   -204   -139       C  
-ATOM   3635  CG  TYR B 817     -79.680   6.562  15.787  1.00 28.32           C  
-ANISOU 3635  CG  TYR B 817     3543   3577   3639      5   -154   -107       C  
-ATOM   3636  CD1 TYR B 817     -80.959   7.145  15.731  1.00 27.50           C  
-ANISOU 3636  CD1 TYR B 817     3423   3503   3522     24    -94    -91       C  
-ATOM   3637  CD2 TYR B 817     -79.011   6.342  14.587  1.00 27.26           C  
-ANISOU 3637  CD2 TYR B 817     3378   3416   3561      3   -167    -88       C  
-ATOM   3638  CE1 TYR B 817     -81.521   7.522  14.510  1.00 27.33           C  
-ANISOU 3638  CE1 TYR B 817     3355   3483   3544     40    -58    -55       C  
-ATOM   3639  CE2 TYR B 817     -79.554   6.716  13.384  1.00 26.09           C  
-ANISOU 3639  CE2 TYR B 817     3193   3271   3449     14   -128    -56       C  
-ATOM   3640  CZ  TYR B 817     -80.801   7.295  13.338  1.00 27.32           C  
-ANISOU 3640  CZ  TYR B 817     3333   3455   3592     32    -77    -37       C  
-ATOM   3641  OH  TYR B 817     -81.285   7.609  12.083  1.00 26.84           O  
-ANISOU 3641  OH  TYR B 817     3233   3398   3566     42    -48      2       O  
-ATOM   3642  N   VAL B 818     -80.467   4.082  18.960  1.00 31.84           N  
-ANISOU 3642  N   VAL B 818     4120   4120   3859    -61   -223    -91       N  
-ATOM   3643  CA  VAL B 818     -81.443   2.996  19.181  1.00 32.92           C  
-ANISOU 3643  CA  VAL B 818     4273   4306   3931    -89   -213    -42       C  
-ATOM   3644  C   VAL B 818     -82.414   3.351  20.324  1.00 34.70           C  
-ANISOU 3644  C   VAL B 818     4523   4578   4082    -94   -169    -54       C  
-ATOM   3645  O   VAL B 818     -83.626   3.195  20.199  1.00 37.65           O  
-ANISOU 3645  O   VAL B 818     4876   5000   4429   -101   -118    -22       O  
-ATOM   3646  CB  VAL B 818     -80.748   1.651  19.514  1.00 32.45           C  
-ANISOU 3646  CB  VAL B 818     4255   4233   3840   -118   -284    -19       C  
-ATOM   3647  CG1 VAL B 818     -81.778   0.624  19.968  1.00 31.76           C  
-ANISOU 3647  CG1 VAL B 818     4197   4194   3678   -154   -273     28       C  
-ATOM   3648  CG2 VAL B 818     -79.976   1.127  18.304  1.00 31.93           C  
-ANISOU 3648  CG2 VAL B 818     4162   4127   3844   -113   -316     -3       C  
-ATOM   3649  N   LYS B 819     -81.870   3.834  21.432  1.00 39.33           N  
-ANISOU 3649  N   LYS B 819     5153   5155   4635    -91   -187   -102       N  
-ATOM   3650  CA  LYS B 819     -82.656   4.112  22.637  1.00 43.66           C  
-ANISOU 3650  CA  LYS B 819     5738   5749   5101    -98   -147   -121       C  
-ATOM   3651  C   LYS B 819     -83.626   5.270  22.452  1.00 42.46           C  
-ANISOU 3651  C   LYS B 819     5547   5615   4972    -63    -61   -143       C  
-ATOM   3652  O   LYS B 819     -84.793   5.170  22.796  1.00 40.66           O  
-ANISOU 3652  O   LYS B 819     5311   5441   4696    -67     -4   -124       O  
-ATOM   3653  CB  LYS B 819     -81.721   4.442  23.782  1.00 49.14           C  
-ANISOU 3653  CB  LYS B 819     6491   6424   5757   -103   -192   -174       C  
-ATOM   3654  CG  LYS B 819     -82.370   4.542  25.151  1.00 57.46           C  
-ANISOU 3654  CG  LYS B 819     7599   7525   6709   -119   -161   -195       C  
-ATOM   3655  CD  LYS B 819     -81.560   5.507  26.020  1.00 61.13           C  
-ANISOU 3655  CD  LYS B 819     8105   7961   7159   -110   -183   -270       C  
-ATOM   3656  CE  LYS B 819     -82.033   5.547  27.478  1.00 62.64           C  
-ANISOU 3656  CE  LYS B 819     8366   8200   7235   -131   -162   -298       C  
-ATOM   3657  NZ  LYS B 819     -82.216   6.924  28.040  1.00 61.77           N  
-ANISOU 3657  NZ  LYS B 819     8272   8082   7118   -105   -107   -375       N  
-ATOM   3658  N   ASN B 820     -83.144   6.361  21.874  1.00 40.73           N  
-ANISOU 3658  N   ASN B 820     5299   5347   4829    -28    -52   -178       N  
-ATOM   3659  CA  ASN B 820     -83.979   7.538  21.715  1.00 40.44           C  
-ANISOU 3659  CA  ASN B 820     5229   5314   4821     13     25   -201       C  
-ATOM   3660  C   ASN B 820     -85.052   7.471  20.645  1.00 38.87           C  
-ANISOU 3660  C   ASN B 820     4964   5145   4660     30     73   -147       C  
-ATOM   3661  O   ASN B 820     -86.021   8.195  20.738  1.00 42.05           O  
-ANISOU 3661  O   ASN B 820     5340   5571   5067     62    140   -154       O  
-ATOM   3662  CB  ASN B 820     -83.124   8.745  21.416  1.00 39.68           C  
-ANISOU 3662  CB  ASN B 820     5129   5150   4797     43     18   -252       C  
-ATOM   3663  CG  ASN B 820     -82.361   9.217  22.612  1.00 41.00           C  
-ANISOU 3663  CG  ASN B 820     5359   5295   4926     34     -9   -320       C  
-ATOM   3664  OD1 ASN B 820     -82.577   8.749  23.712  1.00 46.86           O  
-ANISOU 3664  OD1 ASN B 820     6150   6076   5581     11    -14   -331       O  
-ATOM   3665  ND2 ASN B 820     -81.449  10.133  22.400  1.00 41.52           N  
-ANISOU 3665  ND2 ASN B 820     5425   5297   5053     46    -28   -365       N  
-ATOM   3666  N   THR B 821     -84.883   6.671  19.609  1.00 35.18           N  
-ANISOU 3666  N   THR B 821     4468   4674   4224     11     39    -95       N  
-ATOM   3667  CA  THR B 821     -85.823   6.743  18.479  1.00 34.91           C  
-ANISOU 3667  CA  THR B 821     4369   4665   4232     26     77    -46       C  
-ATOM   3668  C   THR B 821     -86.763   5.552  18.407  1.00 34.39           C  
-ANISOU 3668  C   THR B 821     4289   4663   4115    -12     82     12       C  
-ATOM   3669  O   THR B 821     -87.350   5.257  17.364  1.00 34.11           O  
-ANISOU 3669  O   THR B 821     4205   4648   4108    -16     89     60       O  
-ATOM   3670  CB  THR B 821     -85.073   6.940  17.128  1.00 34.59           C  
-ANISOU 3670  CB  THR B 821     4298   4573   4271     36     47    -32       C  
-ATOM   3671  OG1 THR B 821     -84.348   5.749  16.768  1.00 31.87           O  
-ANISOU 3671  OG1 THR B 821     3972   4220   3918     -3    -13     -7       O  
-ATOM   3672  CG2 THR B 821     -84.111   8.109  17.238  1.00 33.15           C  
-ANISOU 3672  CG2 THR B 821     4129   4325   4139     65     42    -87       C  
-ATOM   3673  N   HIS B 822     -86.889   4.831  19.510  1.00 38.72           N  
-ANISOU 3673  N   HIS B 822     4884   5244   4585    -46     73      9       N  
-ATOM   3674  CA  HIS B 822     -87.895   3.787  19.598  1.00 40.82           C  
-ANISOU 3674  CA  HIS B 822     5139   5573   4797    -87     87     62       C  
-ATOM   3675  C   HIS B 822     -89.250   4.480  19.730  1.00 41.66           C  
-ANISOU 3675  C   HIS B 822     5192   5736   4900    -61    169     67       C  
-ATOM   3676  O   HIS B 822     -89.440   5.242  20.641  1.00 42.59           O  
-ANISOU 3676  O   HIS B 822     5326   5863   4993    -34    212     23       O  
-ATOM   3677  CB  HIS B 822     -87.646   2.892  20.804  1.00 41.68           C  
-ANISOU 3677  CB  HIS B 822     5319   5699   4820   -131     59     61       C  
-ATOM   3678  CG  HIS B 822     -88.462   1.647  20.770  1.00 42.95           C  
-ANISOU 3678  CG  HIS B 822     5477   5909   4932   -185     59    122       C  
-ATOM   3679  ND1 HIS B 822     -87.900   0.390  20.781  1.00 44.71           N  
-ANISOU 3679  ND1 HIS B 822     5747   6111   5128   -231     -5    152       N  
-ATOM   3680  CD2 HIS B 822     -89.797   1.467  20.648  1.00 41.43           C  
-ANISOU 3680  CD2 HIS B 822     5237   5783   4720   -202    114    160       C  
-ATOM   3681  CE1 HIS B 822     -88.860  -0.512  20.695  1.00 43.48           C  
-ANISOU 3681  CE1 HIS B 822     5580   6004   4936   -279     11    206       C  
-ATOM   3682  NE2 HIS B 822     -90.016   0.118  20.594  1.00 40.20           N  
-ANISOU 3682  NE2 HIS B 822     5104   5646   4525   -264     82    211       N  
-ATOM   3683  N   ALA B 823     -90.173   4.234  18.812  1.00 43.68           N  
-ANISOU 3683  N   ALA B 823     5383   6031   5182    -66    189    119       N  
-ATOM   3684  CA  ALA B 823     -91.451   4.944  18.812  1.00 44.86           C  
-ANISOU 3684  CA  ALA B 823     5467   6235   5344    -33    263    128       C  
-ATOM   3685  C   ALA B 823     -92.370   4.467  19.955  1.00 51.82           C  
-ANISOU 3685  C   ALA B 823     6356   7189   6143    -63    311    134       C  
-ATOM   3686  O   ALA B 823     -92.373   3.299  20.306  1.00 49.69           O  
-ANISOU 3686  O   ALA B 823     6122   6943   5815   -125    282    164       O  
-ATOM   3687  CB  ALA B 823     -92.157   4.751  17.485  1.00 42.61           C  
-ANISOU 3687  CB  ALA B 823     5107   5975   5106    -36    261    186       C  
-ATOM   3688  N   THR B 824     -93.163   5.390  20.485  1.00 54.81           N  
-ANISOU 3688  N   THR B 824     6701   7602   6523    -18    386    108       N  
-ATOM   3689  CA  THR B 824     -94.142   5.120  21.542  1.00 58.69           C  
-ANISOU 3689  CA  THR B 824     7188   8171   6941    -39    449    110       C  
-ATOM   3690  C   THR B 824     -95.146   4.025  21.187  1.00 57.93           C  
-ANISOU 3690  C   THR B 824     7042   8148   6820    -98    454    182       C  
-ATOM   3691  O   THR B 824     -95.534   3.244  22.043  1.00 57.71           O  
-ANISOU 3691  O   THR B 824     7042   8170   6714   -151    471    197       O  
-ATOM   3692  CB  THR B 824     -94.916   6.433  21.825  1.00 59.43           C  
-ANISOU 3692  CB  THR B 824     7230   8284   7067     36    536     71       C  
-ATOM   3693  OG1 THR B 824     -94.103   7.267  22.647  1.00 59.92           O  
-ANISOU 3693  OG1 THR B 824     7361   8290   7115     71    543     -6       O  
-ATOM   3694  CG2 THR B 824     -96.301   6.240  22.497  1.00 66.38           C  
-ANISOU 3694  CG2 THR B 824     8060   9263   7899     26    620     89       C  
-ATOM   3695  N   THR B 825     -95.591   4.006  19.938  1.00 55.06           N  
-ANISOU 3695  N   THR B 825     6605   7794   6522    -91    440    228       N  
-ATOM   3696  CA  THR B 825     -96.617   3.061  19.516  1.00 53.06           C  
-ANISOU 3696  CA  THR B 825     6294   7613   6252   -148    444    295       C  
-ATOM   3697  C   THR B 825     -96.082   1.679  19.169  1.00 52.19           C  
-ANISOU 3697  C   THR B 825     6237   7482   6111   -228    368    334       C  
-ATOM   3698  O   THR B 825     -96.850   0.806  18.812  1.00 48.32           O  
-ANISOU 3698  O   THR B 825     5710   7043   5605   -287    363    388       O  
-ATOM   3699  CB  THR B 825     -97.389   3.563  18.284  1.00 52.56           C  
-ANISOU 3699  CB  THR B 825     6128   7575   6267   -114    453    333       C  
-ATOM   3700  OG1 THR B 825     -96.490   3.712  17.179  1.00 51.17           O  
-ANISOU 3700  OG1 THR B 825     5969   7328   6147    -98    388    335       O  
-ATOM   3701  CG2 THR B 825     -98.088   4.893  18.585  1.00 52.80           C  
-ANISOU 3701  CG2 THR B 825     6095   7629   6337    -29    532    303       C  
-ATOM   3702  N   HIS B 826     -94.772   1.485  19.225  1.00 54.42           N  
-ANISOU 3702  N   HIS B 826     6600   7687   6390   -230    308    306       N  
-ATOM   3703  CA  HIS B 826     -94.196   0.174  18.933  1.00 53.58           C  
-ANISOU 3703  CA  HIS B 826     6549   7552   6259   -297    237    338       C  
-ATOM   3704  C   HIS B 826     -93.794  -0.462  20.259  1.00 54.39           C  
-ANISOU 3704  C   HIS B 826     6737   7650   6277   -336    229    325       C  
-ATOM   3705  O   HIS B 826     -92.615  -0.705  20.530  1.00 47.28           O  
-ANISOU 3705  O   HIS B 826     5911   6687   5368   -335    174    300       O  
-ATOM   3706  CB  HIS B 826     -93.007   0.324  17.981  1.00 50.17           C  
-ANISOU 3706  CB  HIS B 826     6140   7037   5886   -271    174    321       C  
-ATOM   3707  CG  HIS B 826     -93.385   0.875  16.644  1.00 52.43           C  
-ANISOU 3707  CG  HIS B 826     6350   7326   6243   -241    178    341       C  
-ATOM   3708  ND1 HIS B 826     -92.554   1.691  15.904  1.00 51.61           N  
-ANISOU 3708  ND1 HIS B 826     6244   7162   6204   -189    158    314       N  
-ATOM   3709  CD2 HIS B 826     -94.529   0.754  15.929  1.00 54.00           C  
-ANISOU 3709  CD2 HIS B 826     6472   7586   6458   -258    199    388       C  
-ATOM   3710  CE1 HIS B 826     -93.162   2.027  14.779  1.00 55.84           C  
-ANISOU 3710  CE1 HIS B 826     6710   7719   6787   -174    165    346       C  
-ATOM   3711  NE2 HIS B 826     -94.360   1.463  14.765  1.00 54.75           N  
-ANISOU 3711  NE2 HIS B 826     6525   7655   6622   -215    186    391       N  
-ATOM   3712  N   ASN B 827     -94.804  -0.694  21.091  1.00 55.93           N  
-ANISOU 3712  N   ASN B 827     6917   7920   6413   -368    286    343       N  
-ATOM   3713  CA  ASN B 827     -94.593  -1.038  22.505  1.00 57.71           C  
-ANISOU 3713  CA  ASN B 827     7222   8157   6550   -397    297    327       C  
-ATOM   3714  C   ASN B 827     -94.560  -2.546  22.757  1.00 53.48           C  
-ANISOU 3714  C   ASN B 827     6743   7622   5953   -484    252    380       C  
-ATOM   3715  O   ASN B 827     -94.369  -2.978  23.870  1.00 54.07           O  
-ANISOU 3715  O   ASN B 827     6890   7704   5950   -517    251    379       O  
-ATOM   3716  CB  ASN B 827     -95.621  -0.313  23.412  1.00 61.00           C  
-ANISOU 3716  CB  ASN B 827     7599   8651   6927   -377    395    307       C  
-ATOM   3717  CG  ASN B 827     -97.061  -0.496  22.955  1.00 66.07           C  
-ANISOU 3717  CG  ASN B 827     8142   9378   7585   -401    452    356       C  
-ATOM   3718  OD1 ASN B 827     -97.362  -1.226  21.997  1.00 67.84           O  
-ANISOU 3718  OD1 ASN B 827     8329   9607   7839   -443    415    408       O  
-ATOM   3719  ND2 ASN B 827     -97.963   0.174  23.647  1.00 66.82           N  
-ANISOU 3719  ND2 ASN B 827     8191   9541   7657   -374    542    337       N  
-ATOM   3720  N   ALA B 828     -94.722  -3.338  21.705  1.00 54.17           N  
-ANISOU 3720  N   ALA B 828     6806   7698   6078   -523    212    427       N  
-ATOM   3721  CA  ALA B 828     -94.641  -4.797  21.783  1.00 52.33           C  
-ANISOU 3721  CA  ALA B 828     6633   7450   5801   -605    162    477       C  
-ATOM   3722  C   ALA B 828     -93.263  -5.322  22.212  1.00 49.99           C  
-ANISOU 3722  C   ALA B 828     6440   7070   5482   -605     87    461       C  
-ATOM   3723  O   ALA B 828     -93.166  -6.467  22.633  1.00 48.98           O  
-ANISOU 3723  O   ALA B 828     6378   6928   5304   -668     52    500       O  
-ATOM   3724  CB  ALA B 828     -95.034  -5.405  20.436  1.00 53.69           C  
-ANISOU 3724  CB  ALA B 828     6757   7619   6025   -640    133    519       C  
-ATOM   3725  N   TYR B 829     -92.204  -4.507  22.112  1.00 46.01           N  
-ANISOU 3725  N   TYR B 829     5951   6511   5020   -536     60    408       N  
-ATOM   3726  CA  TYR B 829     -90.852  -4.956  22.475  1.00 46.54           C  
-ANISOU 3726  CA  TYR B 829     6103   6502   5076   -531    -16    392       C  
-ATOM   3727  C   TYR B 829     -89.937  -3.787  22.891  1.00 45.81           C  
-ANISOU 3727  C   TYR B 829     6023   6380   5004   -460    -20    324       C  
-ATOM   3728  O   TYR B 829     -90.236  -2.653  22.601  1.00 46.03           O  
-ANISOU 3728  O   TYR B 829     5992   6426   5073   -412     28    290       O  
-ATOM   3729  CB  TYR B 829     -90.242  -5.763  21.312  1.00 44.46           C  
-ANISOU 3729  CB  TYR B 829     5847   6175   4872   -542    -82    414       C  
-ATOM   3730  CG  TYR B 829     -90.167  -4.986  20.007  1.00 45.73           C  
-ANISOU 3730  CG  TYR B 829     5933   6321   5119   -494    -73    392       C  
-ATOM   3731  CD1 TYR B 829     -89.136  -4.075  19.777  1.00 45.55           C  
-ANISOU 3731  CD1 TYR B 829     5907   6250   5149   -428    -91    340       C  
-ATOM   3732  CD2 TYR B 829     -91.130  -5.145  19.006  1.00 45.45           C  
-ANISOU 3732  CD2 TYR B 829     5833   6323   5113   -518    -48    425       C  
-ATOM   3733  CE1 TYR B 829     -89.066  -3.342  18.596  1.00 46.29           C  
-ANISOU 3733  CE1 TYR B 829     5938   6330   5319   -387    -81    324       C  
-ATOM   3734  CE2 TYR B 829     -91.074  -4.401  17.826  1.00 46.82           C  
-ANISOU 3734  CE2 TYR B 829     5943   6487   5360   -475    -41    409       C  
-ATOM   3735  CZ  TYR B 829     -90.029  -3.496  17.629  1.00 45.20           C  
-ANISOU 3735  CZ  TYR B 829     5740   6230   5203   -409    -56    360       C  
-ATOM   3736  OH  TYR B 829     -89.911  -2.760  16.469  1.00 42.11           O  
-ANISOU 3736  OH  TYR B 829     5294   5825   4882   -369    -51    348       O  
-ATOM   3737  N   ASP B 830     -88.845  -4.087  23.590  1.00 47.22           N  
-ANISOU 3737  N   ASP B 830     6277   6509   5153   -458    -81    308       N  
-ATOM   3738  CA  ASP B 830     -87.719  -3.152  23.721  1.00 52.26           C  
-ANISOU 3738  CA  ASP B 830     6927   7102   5829   -399   -109    247       C  
-ATOM   3739  C   ASP B 830     -86.530  -3.795  22.993  1.00 47.93           C  
-ANISOU 3739  C   ASP B 830     6399   6475   5336   -391   -193    254       C  
-ATOM   3740  O   ASP B 830     -86.538  -4.994  22.676  1.00 48.35           O  
-ANISOU 3740  O   ASP B 830     6478   6510   5383   -431   -230    302       O  
-ATOM   3741  CB  ASP B 830     -87.386  -2.672  25.167  1.00 58.24           C  
-ANISOU 3741  CB  ASP B 830     7744   7873   6511   -393   -106    208       C  
-ATOM   3742  CG  ASP B 830     -87.343  -3.787  26.172  1.00 68.26           C  
-ANISOU 3742  CG  ASP B 830     9095   9153   7687   -449   -143    250       C  
-ATOM   3743  OD1 ASP B 830     -86.263  -4.414  26.292  1.00 77.26           O  
-ANISOU 3743  OD1 ASP B 830    10288  10236   8830   -452   -227    258       O  
-ATOM   3744  OD2 ASP B 830     -88.369  -4.004  26.879  1.00 75.33           O  
-ANISOU 3744  OD2 ASP B 830    10003  10114   8506   -490    -86    274       O  
-ATOM   3745  N   LEU B 831     -85.549  -2.977  22.653  1.00 41.92           N  
-ANISOU 3745  N   LEU B 831     5621   5670   4637   -339   -217    205       N  
-ATOM   3746  CA  LEU B 831     -84.441  -3.443  21.858  1.00 40.66           C  
-ANISOU 3746  CA  LEU B 831     5465   5442   4541   -324   -283    205       C  
-ATOM   3747  C   LEU B 831     -83.184  -3.368  22.661  1.00 41.86           C  
-ANISOU 3747  C   LEU B 831     5668   5555   4684   -306   -347    174       C  
-ATOM   3748  O   LEU B 831     -82.962  -2.430  23.422  1.00 40.48           O  
-ANISOU 3748  O   LEU B 831     5501   5392   4488   -285   -336    129       O  
-ATOM   3749  CB  LEU B 831     -84.251  -2.600  20.607  1.00 39.04           C  
-ANISOU 3749  CB  LEU B 831     5190   5216   4427   -283   -261    179       C  
-ATOM   3750  CG  LEU B 831     -85.293  -2.743  19.505  1.00 38.89           C  
-ANISOU 3750  CG  LEU B 831     5115   5226   4435   -297   -216    214       C  
-ATOM   3751  CD1 LEU B 831     -85.181  -1.642  18.460  1.00 37.51           C  
-ANISOU 3751  CD1 LEU B 831     4874   5039   4337   -252   -187    187       C  
-ATOM   3752  CD2 LEU B 831     -85.178  -4.121  18.884  1.00 38.34           C  
-ANISOU 3752  CD2 LEU B 831     5070   5130   4368   -336   -259    258       C  
-ATOM   3753  N   GLU B 832     -82.347  -4.360  22.459  1.00 41.38           N  
-ANISOU 3753  N   GLU B 832     5639   5444   4641   -313   -417    196       N  
-ATOM   3754  CA  GLU B 832     -81.078  -4.412  23.110  1.00 45.04           C  
-ANISOU 3754  CA  GLU B 832     6141   5868   5106   -293   -491    173       C  
-ATOM   3755  C   GLU B 832     -80.050  -4.718  22.031  1.00 43.39           C  
-ANISOU 3755  C   GLU B 832     5901   5596   4989   -263   -535    167       C  
-ATOM   3756  O   GLU B 832     -80.162  -5.712  21.286  1.00 42.54           O  
-ANISOU 3756  O   GLU B 832     5795   5463   4903   -278   -547    204       O  
-ATOM   3757  CB  GLU B 832     -81.120  -5.513  24.165  1.00 49.69           C  
-ANISOU 3757  CB  GLU B 832     6810   6461   5611   -333   -537    218       C  
-ATOM   3758  CG  GLU B 832     -79.778  -5.952  24.705  1.00 56.72           C  
-ANISOU 3758  CG  GLU B 832     7743   7303   6507   -316   -632    214       C  
-ATOM   3759  CD  GLU B 832     -79.885  -6.991  25.832  1.00 62.58           C  
-ANISOU 3759  CD  GLU B 832     8572   8051   7156   -356   -679    265       C  
-ATOM   3760  OE1 GLU B 832     -80.960  -7.636  26.025  1.00 62.22           O  
-ANISOU 3760  OE1 GLU B 832     8555   8036   7050   -404   -641    313       O  
-ATOM   3761  OE2 GLU B 832     -78.861  -7.152  26.521  1.00 62.66           O  
-ANISOU 3761  OE2 GLU B 832     8618   8033   7155   -341   -757    260       O  
-ATOM   3762  N   VAL B 833     -79.036  -3.883  21.964  1.00 40.61           N  
-ANISOU 3762  N   VAL B 833     5521   5218   4690   -225   -558    118       N  
-ATOM   3763  CA  VAL B 833     -77.987  -4.070  20.988  1.00 40.24           C  
-ANISOU 3763  CA  VAL B 833     5439   5117   4732   -194   -593    107       C  
-ATOM   3764  C   VAL B 833     -77.050  -5.161  21.473  1.00 40.05           C  
-ANISOU 3764  C   VAL B 833     5461   5053   4703   -192   -679    129       C  
-ATOM   3765  O   VAL B 833     -76.511  -5.071  22.563  1.00 44.69           O  
-ANISOU 3765  O   VAL B 833     6085   5643   5252   -191   -730    119       O  
-ATOM   3766  CB  VAL B 833     -77.228  -2.750  20.763  1.00 39.39           C  
-ANISOU 3766  CB  VAL B 833     5283   4999   4687   -159   -585     48       C  
-ATOM   3767  CG1 VAL B 833     -76.068  -2.955  19.802  1.00 38.76           C  
-ANISOU 3767  CG1 VAL B 833     5162   4867   4698   -130   -620     36       C  
-ATOM   3768  CG2 VAL B 833     -78.188  -1.680  20.243  1.00 39.19           C  
-ANISOU 3768  CG2 VAL B 833     5215   5005   4671   -155   -501     32       C  
-ATOM   3769  N   ILE B 834     -76.854  -6.198  20.673  1.00 40.98           N  
-ANISOU 3769  N   ILE B 834     5581   5132   4859   -191   -698    158       N  
-ATOM   3770  CA  ILE B 834     -75.950  -7.275  21.051  1.00 41.04           C  
-ANISOU 3770  CA  ILE B 834     5628   5091   4873   -180   -780    182       C  
-ATOM   3771  C   ILE B 834     -74.581  -6.986  20.478  1.00 41.38           C  
-ANISOU 3771  C   ILE B 834     5621   5092   5010   -131   -816    144       C  
-ATOM   3772  O   ILE B 834     -73.612  -6.933  21.219  1.00 42.63           O  
-ANISOU 3772  O   ILE B 834     5787   5237   5175   -111   -882    131       O  
-ATOM   3773  CB  ILE B 834     -76.460  -8.635  20.565  1.00 42.89           C  
-ANISOU 3773  CB  ILE B 834     5901   5297   5097   -204   -783    233       C  
-ATOM   3774  CG1 ILE B 834     -77.764  -8.978  21.261  1.00 45.82           C  
-ANISOU 3774  CG1 ILE B 834     6323   5714   5373   -260   -752    275       C  
-ATOM   3775  CG2 ILE B 834     -75.456  -9.748  20.851  1.00 42.98           C  
-ANISOU 3775  CG2 ILE B 834     5953   5247   5131   -182   -867    256       C  
-ATOM   3776  CD1 ILE B 834     -78.461 -10.145  20.605  1.00 48.54           C  
-ANISOU 3776  CD1 ILE B 834     6695   6036   5713   -295   -739    321       C  
-ATOM   3777  N   ASP B 835     -74.503  -6.851  19.152  1.00 40.28           N  
-ANISOU 3777  N   ASP B 835     5428   4935   4941   -115   -774    128       N  
-ATOM   3778  CA  ASP B 835     -73.258  -6.566  18.459  1.00 39.60           C  
-ANISOU 3778  CA  ASP B 835     5286   4813   4948    -71   -793     92       C  
-ATOM   3779  C   ASP B 835     -73.463  -5.429  17.482  1.00 38.43           C  
-ANISOU 3779  C   ASP B 835     5074   4683   4843    -66   -722     57       C  
-ATOM   3780  O   ASP B 835     -74.524  -5.303  16.860  1.00 40.11           O  
-ANISOU 3780  O   ASP B 835     5283   4920   5036    -89   -661     71       O  
-ATOM   3781  CB  ASP B 835     -72.749  -7.782  17.678  1.00 42.86           C  
-ANISOU 3781  CB  ASP B 835     5704   5171   5410    -51   -817    110       C  
-ATOM   3782  CG  ASP B 835     -72.326  -8.944  18.570  1.00 48.85           C  
-ANISOU 3782  CG  ASP B 835     6523   5895   6142    -45   -897    146       C  
-ATOM   3783  OD1 ASP B 835     -72.736 -10.088  18.260  1.00 54.28           O  
-ANISOU 3783  OD1 ASP B 835     7256   6551   6817    -58   -900    182       O  
-ATOM   3784  OD2 ASP B 835     -71.568  -8.725  19.551  1.00 53.57           O  
-ANISOU 3784  OD2 ASP B 835     7125   6495   6734    -29   -959    139       O  
-ATOM   3785  N   ILE B 836     -72.410  -4.637  17.315  1.00 36.26           N  
-ANISOU 3785  N   ILE B 836     4747   4396   4634    -37   -734     16       N  
-ATOM   3786  CA  ILE B 836     -72.369  -3.584  16.311  1.00 34.05           C  
-ANISOU 3786  CA  ILE B 836     4407   4123   4409    -30   -674    -15       C  
-ATOM   3787  C   ILE B 836     -71.217  -3.884  15.381  1.00 33.45           C  
-ANISOU 3787  C   ILE B 836     4283   4007   4418      1   -685    -32       C  
-ATOM   3788  O   ILE B 836     -70.089  -4.036  15.823  1.00 32.79           O  
-ANISOU 3788  O   ILE B 836     4183   3902   4373     25   -743    -48       O  
-ATOM   3789  CB  ILE B 836     -72.175  -2.206  16.941  1.00 33.41           C  
-ANISOU 3789  CB  ILE B 836     4305   4063   4329    -31   -668    -53       C  
-ATOM   3790  CG1 ILE B 836     -73.288  -1.921  17.943  1.00 31.90           C  
-ANISOU 3790  CG1 ILE B 836     4162   3911   4048    -57   -652    -42       C  
-ATOM   3791  CG2 ILE B 836     -72.181  -1.131  15.858  1.00 32.27           C  
-ANISOU 3791  CG2 ILE B 836     4103   3918   4242    -24   -604    -77       C  
-ATOM   3792  CD1 ILE B 836     -73.046  -0.681  18.778  1.00 33.39           C  
-ANISOU 3792  CD1 ILE B 836     4346   4114   4228    -58   -656    -85       C  
-ATOM   3793  N   PHE B 837     -71.524  -4.012  14.093  1.00 32.37           N  
-ANISOU 3793  N   PHE B 837     4125   3865   4310      1   -631    -27       N  
-ATOM   3794  CA  PHE B 837     -70.526  -4.286  13.097  1.00 31.77           C  
-ANISOU 3794  CA  PHE B 837     4005   3756   4311     29   -626    -45       C  
-ATOM   3795  C   PHE B 837     -70.389  -3.088  12.152  1.00 32.26           C  
-ANISOU 3795  C   PHE B 837     4009   3829   4418     28   -564    -71       C  
-ATOM   3796  O   PHE B 837     -71.384  -2.466  11.736  1.00 31.43           O  
-ANISOU 3796  O   PHE B 837     3907   3751   4284      6   -511    -61       O  
-ATOM   3797  CB  PHE B 837     -70.915  -5.504  12.279  1.00 31.84           C  
-ANISOU 3797  CB  PHE B 837     4044   3742   4311     26   -611    -21       C  
-ATOM   3798  CG  PHE B 837     -71.101  -6.767  13.084  1.00 34.28           C  
-ANISOU 3798  CG  PHE B 837     4418   4030   4578     23   -668     10       C  
-ATOM   3799  CD1 PHE B 837     -70.007  -7.600  13.384  1.00 34.61           C  
-ANISOU 3799  CD1 PHE B 837     4461   4028   4662     61   -728      6       C  
-ATOM   3800  CD2 PHE B 837     -72.362  -7.155  13.498  1.00 33.42           C  
-ANISOU 3800  CD2 PHE B 837     4366   3943   4391    -16   -660     47       C  
-ATOM   3801  CE1 PHE B 837     -70.179  -8.766  14.107  1.00 35.38           C  
-ANISOU 3801  CE1 PHE B 837     4623   4098   4722     59   -782     41       C  
-ATOM   3802  CE2 PHE B 837     -72.544  -8.338  14.201  1.00 35.90           C  
-ANISOU 3802  CE2 PHE B 837     4743   4233   4664    -24   -709     81       C  
-ATOM   3803  CZ  PHE B 837     -71.451  -9.137  14.526  1.00 35.17           C  
-ANISOU 3803  CZ  PHE B 837     4660   4091   4613     14   -772     80       C  
-ATOM   3804  N   LYS B 838     -69.155  -2.777  11.797  1.00 32.81           N  
-ANISOU 3804  N   LYS B 838     4024   3879   4562     52   -572   -102       N  
-ATOM   3805  CA  LYS B 838     -68.856  -1.790  10.781  1.00 34.58           C  
-ANISOU 3805  CA  LYS B 838     4194   4108   4838     50   -514   -123       C  
-ATOM   3806  C   LYS B 838     -68.685  -2.549   9.504  1.00 33.31           C  
-ANISOU 3806  C   LYS B 838     4023   3930   4702     60   -477   -119       C  
-ATOM   3807  O   LYS B 838     -67.883  -3.468   9.448  1.00 39.39           O  
-ANISOU 3807  O   LYS B 838     4786   4673   5506     87   -507   -127       O  
-ATOM   3808  CB  LYS B 838     -67.581  -1.036  11.133  1.00 38.97           C  
-ANISOU 3808  CB  LYS B 838     4693   4655   5460     63   -540   -159       C  
-ATOM   3809  CG  LYS B 838     -67.190   0.030  10.132  1.00 44.91           C  
-ANISOU 3809  CG  LYS B 838     5388   5407   6267     55   -480   -179       C  
-ATOM   3810  CD  LYS B 838     -66.159   0.985  10.722  1.00 52.52           C  
-ANISOU 3810  CD  LYS B 838     6304   6366   7285     53   -509   -213       C  
-ATOM   3811  CE  LYS B 838     -65.908   2.240   9.867  1.00 58.62           C  
-ANISOU 3811  CE  LYS B 838     7029   7137   8105     35   -447   -228       C  
-ATOM   3812  NZ  LYS B 838     -65.938   2.039   8.384  1.00 60.59           N  
-ANISOU 3812  NZ  LYS B 838     7259   7386   8377     37   -380   -216       N  
-ATOM   3813  N   ILE B 839     -69.403  -2.151   8.463  1.00 31.32           N  
-ANISOU 3813  N   ILE B 839     3770   3694   4436     41   -414   -108       N  
-ATOM   3814  CA  ILE B 839     -69.366  -2.880   7.201  1.00 30.29           C  
-ANISOU 3814  CA  ILE B 839     3641   3552   4316     44   -376   -106       C  
-ATOM   3815  C   ILE B 839     -68.967  -2.041   6.002  1.00 30.87           C  
-ANISOU 3815  C   ILE B 839     3667   3633   4431     39   -313   -120       C  
-ATOM   3816  O   ILE B 839     -69.348  -0.857   5.879  1.00 30.56           O  
-ANISOU 3816  O   ILE B 839     3610   3613   4388     22   -283   -114       O  
-ATOM   3817  CB  ILE B 839     -70.712  -3.547   6.905  1.00 30.22           C  
-ANISOU 3817  CB  ILE B 839     3690   3558   4235     17   -362    -72       C  
-ATOM   3818  CG1 ILE B 839     -71.858  -2.548   6.926  1.00 30.54           C  
-ANISOU 3818  CG1 ILE B 839     3733   3637   4233    -11   -331    -49       C  
-ATOM   3819  CG2 ILE B 839     -70.978  -4.653   7.932  1.00 30.47           C  
-ANISOU 3819  CG2 ILE B 839     3774   3574   4229     19   -421    -55       C  
-ATOM   3820  CD1 ILE B 839     -73.152  -3.159   6.443  1.00 32.76           C  
-ANISOU 3820  CD1 ILE B 839     4056   3939   4451    -41   -314    -15       C  
-ATOM   3821  N   GLU B 840     -68.180  -2.642   5.117  1.00 29.79           N  
-ANISOU 3821  N   GLU B 840     3510   3477   4333     57   -291   -139       N  
-ATOM   3822  CA  GLU B 840     -67.755  -1.979   3.874  1.00 32.32           C  
-ANISOU 3822  CA  GLU B 840     3789   3805   4687     49   -225   -151       C  
-ATOM   3823  C   GLU B 840     -67.931  -2.991   2.773  1.00 31.76           C  
-ANISOU 3823  C   GLU B 840     3747   3726   4594     49   -191   -151       C  
-ATOM   3824  O   GLU B 840     -67.154  -3.942   2.645  1.00 31.58           O  
-ANISOU 3824  O   GLU B 840     3720   3675   4603     79   -201   -175       O  
-ATOM   3825  CB  GLU B 840     -66.286  -1.527   3.917  1.00 36.70           C  
-ANISOU 3825  CB  GLU B 840     4273   4347   5326     71   -224   -185       C  
-ATOM   3826  CG  GLU B 840     -65.960  -0.574   5.058  1.00 41.26           C  
-ANISOU 3826  CG  GLU B 840     4821   4927   5927     68   -266   -192       C  
-ATOM   3827  CD  GLU B 840     -64.449  -0.347   5.278  1.00 50.28           C  
-ANISOU 3827  CD  GLU B 840     5891   6058   7156     88   -283   -227       C  
-ATOM   3828  OE1 GLU B 840     -63.586  -0.997   4.601  1.00 50.95           O  
-ANISOU 3828  OE1 GLU B 840     5941   6131   7287    113   -262   -246       O  
-ATOM   3829  OE2 GLU B 840     -64.132   0.484   6.179  1.00 54.02           O  
-ANISOU 3829  OE2 GLU B 840     6341   6534   7650     79   -319   -237       O  
-ATOM   3830  N   ARG B 841     -68.971  -2.799   1.980  1.00 31.34           N  
-ANISOU 3830  N   ARG B 841     3725   3696   4486     17   -154   -126       N  
-ATOM   3831  CA  ARG B 841     -69.157  -3.626   0.803  1.00 31.23           C  
-ANISOU 3831  CA  ARG B 841     3742   3679   4445      8   -117   -130       C  
-ATOM   3832  C   ARG B 841     -68.136  -3.229  -0.274  1.00 29.82           C  
-ANISOU 3832  C   ARG B 841     3517   3500   4314     16    -57   -158       C  
-ATOM   3833  O   ARG B 841     -67.972  -2.069  -0.579  1.00 29.10           O  
-ANISOU 3833  O   ARG B 841     3388   3428   4241      3    -25   -151       O  
-ATOM   3834  CB  ARG B 841     -70.578  -3.481   0.268  1.00 29.84           C  
-ANISOU 3834  CB  ARG B 841     3608   3536   4194    -33   -101    -93       C  
-ATOM   3835  CG  ARG B 841     -71.692  -3.945   1.197  1.00 31.05           C  
-ANISOU 3835  CG  ARG B 841     3805   3696   4296    -48   -149    -63       C  
-ATOM   3836  CD  ARG B 841     -72.820  -4.607   0.397  1.00 32.07           C  
-ANISOU 3836  CD  ARG B 841     3984   3844   4357    -86   -137    -40       C  
-ATOM   3837  NE  ARG B 841     -73.211  -3.716  -0.618  1.00 35.49           N  
-ANISOU 3837  NE  ARG B 841     4400   4312   4773   -108    -92    -23       N  
-ATOM   3838  CZ  ARG B 841     -73.085  -3.848  -1.930  1.00 33.35           C  
-ANISOU 3838  CZ  ARG B 841     4138   4048   4486   -123    -49    -31       C  
-ATOM   3839  NH1 ARG B 841     -72.735  -4.960  -2.534  1.00 30.53           N  
-ANISOU 3839  NH1 ARG B 841     3815   3667   4120   -124    -40    -59       N  
-ATOM   3840  NH2 ARG B 841     -73.417  -2.786  -2.640  1.00 36.21           N  
-ANISOU 3840  NH2 ARG B 841     4478   4443   4837   -140    -15     -6       N  
-ATOM   3841  N   GLU B 842     -67.518  -4.209  -0.877  1.00 31.00           N  
-ANISOU 3841  N   GLU B 842     3673   3626   4478     36    -38   -188       N  
-ATOM   3842  CA  GLU B 842     -66.632  -3.976  -2.006  1.00 35.65           C  
-ANISOU 3842  CA  GLU B 842     4225   4219   5101     41     29   -216       C  
-ATOM   3843  C   GLU B 842     -67.326  -3.224  -3.155  1.00 32.28           C  
-ANISOU 3843  C   GLU B 842     3814   3830   4622     -3     86   -191       C  
-ATOM   3844  O   GLU B 842     -68.450  -3.553  -3.567  1.00 29.24           O  
-ANISOU 3844  O   GLU B 842     3486   3459   4164    -33     83   -166       O  
-ATOM   3845  CB  GLU B 842     -66.050  -5.298  -2.503  1.00 39.72           C  
-ANISOU 3845  CB  GLU B 842     4759   4702   5629     71     44   -254       C  
-ATOM   3846  CG  GLU B 842     -64.956  -5.778  -1.586  1.00 46.03           C  
-ANISOU 3846  CG  GLU B 842     5516   5467   6506    125      2   -282       C  
-ATOM   3847  CD  GLU B 842     -64.498  -7.193  -1.896  1.00 53.07           C  
-ANISOU 3847  CD  GLU B 842     6436   6316   7414    164      6   -316       C  
-ATOM   3848  OE1 GLU B 842     -64.714  -7.662  -3.040  1.00 54.97           O  
-ANISOU 3848  OE1 GLU B 842     6714   6555   7617    151     61   -334       O  
-ATOM   3849  OE2 GLU B 842     -63.910  -7.810  -0.982  1.00 51.68           O  
-ANISOU 3849  OE2 GLU B 842     6246   6105   7287    209    -49   -326       O  
-ATOM   3850  N   GLY B 843     -66.681  -2.144  -3.569  1.00 31.35           N  
-ANISOU 3850  N   GLY B 843     3642   3727   4542    -11    129   -192       N  
-ATOM   3851  CA  GLY B 843     -67.176  -1.356  -4.657  1.00 29.90           C  
-ANISOU 3851  CA  GLY B 843     3470   3575   4316    -50    182   -165       C  
-ATOM   3852  C   GLY B 843     -68.160  -0.285  -4.240  1.00 28.50           C  
-ANISOU 3852  C   GLY B 843     3300   3417   4113    -74    159   -117       C  
-ATOM   3853  O   GLY B 843     -68.519   0.560  -5.057  1.00 30.47           O  
-ANISOU 3853  O   GLY B 843     3551   3689   4336   -103    198    -87       O  
-ATOM   3854  N   GLU B 844     -68.669  -0.321  -3.016  1.00 26.10           N  
-ANISOU 3854  N   GLU B 844     3004   3105   3809    -63     98   -106       N  
-ATOM   3855  CA  GLU B 844     -69.776   0.593  -2.702  1.00 26.39           C  
-ANISOU 3855  CA  GLU B 844     3053   3162   3813    -83     83    -62       C  
-ATOM   3856  C   GLU B 844     -69.288   2.024  -2.527  1.00 26.37           C  
-ANISOU 3856  C   GLU B 844     3004   3154   3860    -85    101    -55       C  
-ATOM   3857  O   GLU B 844     -70.029   2.967  -2.876  1.00 26.94           O  
-ANISOU 3857  O   GLU B 844     3084   3242   3910   -105    118    -16       O  
-ATOM   3858  CB  GLU B 844     -70.541   0.175  -1.462  1.00 27.02           C  
-ANISOU 3858  CB  GLU B 844     3157   3238   3870    -73     21    -52       C  
-ATOM   3859  CG  GLU B 844     -72.018   0.580  -1.495  1.00 28.07           C  
-ANISOU 3859  CG  GLU B 844     3320   3402   3944    -96     13     -5       C  
-ATOM   3860  CD  GLU B 844     -72.788   0.111  -0.280  1.00 30.73           C  
-ANISOU 3860  CD  GLU B 844     3680   3741   4255    -91    -40      4       C  
-ATOM   3861  OE1 GLU B 844     -72.399   0.541   0.831  1.00 32.39           O  
-ANISOU 3861  OE1 GLU B 844     3870   3936   4500    -72    -67    -10       O  
-ATOM   3862  OE2 GLU B 844     -73.735  -0.718  -0.423  1.00 28.85           O  
-ANISOU 3862  OE2 GLU B 844     3481   3520   3959   -109    -55     24       O  
-ATOM   3863  N   CYS B 845     -68.083   2.199  -1.969  1.00 25.15           N  
-ANISOU 3863  N   CYS B 845     2802   2977   3777    -67     95    -91       N  
-ATOM   3864  CA  CYS B 845     -67.521   3.536  -1.786  1.00 28.73           C  
-ANISOU 3864  CA  CYS B 845     3211   3421   4283    -76    111    -90       C  
-ATOM   3865  C   CYS B 845     -67.404   4.202  -3.161  1.00 27.52           C  
-ANISOU 3865  C   CYS B 845     3053   3281   4124   -104    180    -68       C  
-ATOM   3866  O   CYS B 845     -67.816   5.332  -3.356  1.00 24.70           O  
-ANISOU 3866  O   CYS B 845     2697   2923   3766   -123    197    -35       O  
-ATOM   3867  CB  CYS B 845     -66.136   3.522  -1.086  1.00 29.27           C  
-ANISOU 3867  CB  CYS B 845     3223   3468   4431    -58     92   -134       C  
-ATOM   3868  SG  CYS B 845     -65.318   5.172  -1.028  1.00 35.58           S  
-ANISOU 3868  SG  CYS B 845     3965   4253   5302    -83    119   -136       S  
-ATOM   3869  N   GLN B 846     -66.839   3.477  -4.103  1.00 29.55           N  
-ANISOU 3869  N   GLN B 846     3305   3546   4375   -106    221    -86       N  
-ATOM   3870  CA  GLN B 846     -66.677   3.978  -5.458  1.00 32.54           C  
-ANISOU 3870  CA  GLN B 846     3685   3942   4738   -135    291    -67       C  
-ATOM   3871  C   GLN B 846     -68.054   4.277  -6.094  1.00 29.95           C  
-ANISOU 3871  C   GLN B 846     3412   3638   4331   -159    294    -13       C  
-ATOM   3872  O   GLN B 846     -68.224   5.294  -6.738  1.00 28.21           O  
-ANISOU 3872  O   GLN B 846     3191   3423   4104   -183    327     24       O  
-ATOM   3873  CB  GLN B 846     -65.837   2.997  -6.296  1.00 35.86           C  
-ANISOU 3873  CB  GLN B 846     4096   4369   5159   -128    336   -105       C  
-ATOM   3874  CG  GLN B 846     -65.440   3.485  -7.695  1.00 39.79           C  
-ANISOU 3874  CG  GLN B 846     4589   4887   5642   -161    417    -93       C  
-ATOM   3875  CD  GLN B 846     -64.499   4.695  -7.675  1.00 44.16           C  
-ANISOU 3875  CD  GLN B 846     5081   5430   6266   -179    451    -90       C  
-ATOM   3876  OE1 GLN B 846     -63.646   4.847  -6.777  1.00 44.30           O  
-ANISOU 3876  OE1 GLN B 846     5042   5428   6362   -161    427   -121       O  
-ATOM   3877  NE2 GLN B 846     -64.664   5.576  -8.657  1.00 44.66           N  
-ANISOU 3877  NE2 GLN B 846     5157   5508   6303   -218    504    -50       N  
-ATOM   3878  N   ARG B 847     -69.022   3.392  -5.893  1.00 28.01           N  
-ANISOU 3878  N   ARG B 847     3211   3404   4029   -152    256     -6       N  
-ATOM   3879  CA  ARG B 847     -70.359   3.594  -6.430  1.00 28.38           C  
-ANISOU 3879  CA  ARG B 847     3302   3479   4004   -173    250     46       C  
-ATOM   3880  C   ARG B 847     -71.044   4.800  -5.796  1.00 27.40           C  
-ANISOU 3880  C   ARG B 847     3167   3349   3894   -171    227     85       C  
-ATOM   3881  O   ARG B 847     -71.718   5.586  -6.481  1.00 27.75           O  
-ANISOU 3881  O   ARG B 847     3225   3410   3909   -189    245    135       O  
-ATOM   3882  CB  ARG B 847     -71.201   2.320  -6.249  1.00 31.67           C  
-ANISOU 3882  CB  ARG B 847     3762   3909   4362   -171    210     41       C  
-ATOM   3883  CG  ARG B 847     -72.601   2.368  -6.864  1.00 32.01           C  
-ANISOU 3883  CG  ARG B 847     3845   3989   4329   -198    200     92       C  
-ATOM   3884  CD  ARG B 847     -73.344   1.080  -6.561  1.00 31.77           C  
-ANISOU 3884  CD  ARG B 847     3853   3967   4250   -201    159     83       C  
-ATOM   3885  NE  ARG B 847     -73.835   1.062  -5.184  1.00 32.86           N  
-ANISOU 3885  NE  ARG B 847     3983   4096   4407   -181    108     86       N  
-ATOM   3886  CZ  ARG B 847     -74.686   0.167  -4.695  1.00 32.79           C  
-ANISOU 3886  CZ  ARG B 847     4003   4096   4358   -188     67     92       C  
-ATOM   3887  NH1 ARG B 847     -75.119  -0.794  -5.452  1.00 33.92           N  
-ANISOU 3887  NH1 ARG B 847     4187   4254   4446   -215     66     91       N  
-ATOM   3888  NH2 ARG B 847     -75.114   0.247  -3.436  1.00 36.22           N  
-ANISOU 3888  NH2 ARG B 847     4429   4526   4807   -172     28     97       N  
-ATOM   3889  N   TYR B 848     -70.831   4.989  -4.505  1.00 25.16           N  
-ANISOU 3889  N   TYR B 848     2861   3041   3657   -147    190     63       N  
-ATOM   3890  CA  TYR B 848     -71.446   6.098  -3.802  1.00 25.67           C  
-ANISOU 3890  CA  TYR B 848     2920   3096   3738   -140    172     90       C  
-ATOM   3891  C   TYR B 848     -70.813   7.475  -4.080  1.00 27.03           C  
-ANISOU 3891  C   TYR B 848     3065   3242   3963   -151    207    101       C  
-ATOM   3892  O   TYR B 848     -71.436   8.502  -3.828  1.00 25.19           O  
-ANISOU 3892  O   TYR B 848     2836   2998   3738   -148    203    132       O  
-ATOM   3893  CB  TYR B 848     -71.379   5.801  -2.311  1.00 25.40           C  
-ANISOU 3893  CB  TYR B 848     2878   3045   3728   -116    121     57       C  
-ATOM   3894  CG  TYR B 848     -72.063   6.777  -1.399  1.00 24.87           C  
-ANISOU 3894  CG  TYR B 848     2811   2967   3671   -104    100     73       C  
-ATOM   3895  CD1 TYR B 848     -73.445   6.900  -1.401  1.00 23.93           C  
-ANISOU 3895  CD1 TYR B 848     2717   2873   3504   -101     90    115       C  
-ATOM   3896  CD2 TYR B 848     -71.333   7.553  -0.506  1.00 24.46           C  
-ANISOU 3896  CD2 TYR B 848     2734   2881   3679    -96     89     43       C  
-ATOM   3897  CE1 TYR B 848     -74.085   7.756  -0.540  1.00 23.70           C  
-ANISOU 3897  CE1 TYR B 848     2686   2833   3485    -84     76    124       C  
-ATOM   3898  CE2 TYR B 848     -71.971   8.444   0.350  1.00 23.78           C  
-ANISOU 3898  CE2 TYR B 848     2655   2782   3600    -84     74     51       C  
-ATOM   3899  CZ  TYR B 848     -73.351   8.541   0.319  1.00 25.03           C  
-ANISOU 3899  CZ  TYR B 848     2838   2964   3710    -75     70     91       C  
-ATOM   3900  OH  TYR B 848     -74.032   9.427   1.125  1.00 25.94           O  
-ANISOU 3900  OH  TYR B 848     2958   3065   3832    -57     63     97       O  
-ATOM   3901  N   LYS B 849     -69.589   7.473  -4.603  1.00 30.69           N  
-ANISOU 3901  N   LYS B 849     3500   3696   4466   -164    245     75       N  
-ATOM   3902  CA  LYS B 849     -68.749   8.664  -4.743  1.00 33.51           C  
-ANISOU 3902  CA  LYS B 849     3824   4024   4884   -181    278     77       C  
-ATOM   3903  C   LYS B 849     -69.465   9.876  -5.337  1.00 31.91           C  
-ANISOU 3903  C   LYS B 849     3643   3815   4668   -197    301    136       C  
-ATOM   3904  O   LYS B 849     -69.406  10.949  -4.756  1.00 32.60           O  
-ANISOU 3904  O   LYS B 849     3719   3866   4801   -196    294    141       O  
-ATOM   3905  CB  LYS B 849     -67.516   8.321  -5.581  1.00 38.99           C  
-ANISOU 3905  CB  LYS B 849     4487   4724   5602   -199    328     51       C  
-ATOM   3906  CG  LYS B 849     -66.474   9.422  -5.747  1.00 44.64           C  
-ANISOU 3906  CG  LYS B 849     5160   5413   6387   -225    367     48       C  
-ATOM   3907  CD  LYS B 849     -65.284   8.889  -6.565  1.00 50.66           C  
-ANISOU 3907  CD  LYS B 849     5887   6193   7170   -240    421     19       C  
-ATOM   3908  CE  LYS B 849     -64.175   9.926  -6.871  1.00 56.22           C  
-ANISOU 3908  CE  LYS B 849     6540   6877   7942   -275    470     18       C  
-ATOM   3909  NZ  LYS B 849     -63.668   9.916  -8.280  1.00 55.14           N  
-ANISOU 3909  NZ  LYS B 849     6400   6765   7784   -307    550     33       N  
-ATOM   3910  N   PRO B 850     -70.149   9.712  -6.478  1.00 31.36           N  
-ANISOU 3910  N   PRO B 850     3604   3775   4534   -212    324    181       N  
-ATOM   3911  CA  PRO B 850     -70.872  10.862  -7.017  1.00 33.76           C  
-ANISOU 3911  CA  PRO B 850     3929   4072   4827   -222    338    245       C  
-ATOM   3912  C   PRO B 850     -71.892  11.486  -6.056  1.00 35.82           C  
-ANISOU 3912  C   PRO B 850     4198   4314   5097   -192    296    264       C  
-ATOM   3913  O   PRO B 850     -72.115  12.697  -6.114  1.00 35.13           O  
-ANISOU 3913  O   PRO B 850     4115   4194   5038   -192    307    300       O  
-ATOM   3914  CB  PRO B 850     -71.604  10.297  -8.243  1.00 33.18           C  
-ANISOU 3914  CB  PRO B 850     3891   4045   4669   -238    351    287       C  
-ATOM   3915  CG  PRO B 850     -70.894   9.040  -8.574  1.00 32.89           C  
-ANISOU 3915  CG  PRO B 850     3851   4032   4612   -246    367    238       C  
-ATOM   3916  CD  PRO B 850     -70.381   8.504  -7.274  1.00 31.84           C  
-ANISOU 3916  CD  PRO B 850     3690   3878   4529   -219    332    178       C  
-ATOM   3917  N   PHE B 851     -72.483  10.677  -5.174  1.00 34.90           N  
-ANISOU 3917  N   PHE B 851     4087   4216   4959   -167    252    240       N  
-ATOM   3918  CA  PHE B 851     -73.530  11.177  -4.299  1.00 35.27           C  
-ANISOU 3918  CA  PHE B 851     4141   4255   5007   -138    219    256       C  
-ATOM   3919  C   PHE B 851     -73.014  11.690  -3.010  1.00 35.95           C  
-ANISOU 3919  C   PHE B 851     4209   4298   5151   -122    202    211       C  
-ATOM   3920  O   PHE B 851     -73.724  12.442  -2.360  1.00 36.55           O  
-ANISOU 3920  O   PHE B 851     4293   4355   5240    -99    189    223       O  
-ATOM   3921  CB  PHE B 851     -74.572  10.125  -4.032  1.00 35.41           C  
-ANISOU 3921  CB  PHE B 851     4174   4317   4964   -125    184    261       C  
-ATOM   3922  CG  PHE B 851     -75.381   9.822  -5.224  1.00 38.27           C  
-ANISOU 3922  CG  PHE B 851     4556   4722   5263   -141    192    314       C  
-ATOM   3923  CD1 PHE B 851     -76.340  10.747  -5.683  1.00 38.70           C  
-ANISOU 3923  CD1 PHE B 851     4616   4781   5306   -133    194    378       C  
-ATOM   3924  CD2 PHE B 851     -75.101   8.713  -5.973  1.00 38.88           C  
-ANISOU 3924  CD2 PHE B 851     4647   4830   5295   -165    199    302       C  
-ATOM   3925  CE1 PHE B 851     -77.042  10.512  -6.842  1.00 38.65           C  
-ANISOU 3925  CE1 PHE B 851     4627   4818   5239   -151    196    431       C  
-ATOM   3926  CE2 PHE B 851     -75.808   8.468  -7.122  1.00 41.22           C  
-ANISOU 3926  CE2 PHE B 851     4966   5167   5527   -187    204    349       C  
-ATOM   3927  CZ  PHE B 851     -76.778   9.362  -7.561  1.00 41.13           C  
-ANISOU 3927  CZ  PHE B 851     4959   5167   5501   -182    200    415       C  
-ATOM   3928  N   LYS B 852     -71.752  11.404  -2.707  1.00 39.81           N  
-ANISOU 3928  N   LYS B 852     4674   4770   5680   -134    205    160       N  
-ATOM   3929  CA  LYS B 852     -71.072  12.023  -1.597  1.00 43.85           C  
-ANISOU 3929  CA  LYS B 852     5169   5240   6254   -129    188    116       C  
-ATOM   3930  C   LYS B 852     -71.058  13.544  -1.729  1.00 43.57           C  
-ANISOU 3930  C   LYS B 852     5136   5156   6263   -137    213    140       C  
-ATOM   3931  O   LYS B 852     -70.975  14.226  -0.730  1.00 47.80           O  
-ANISOU 3931  O   LYS B 852     5672   5655   6836   -128    194    112       O  
-ATOM   3932  CB  LYS B 852     -69.650  11.449  -1.497  1.00 49.68           C  
-ANISOU 3932  CB  LYS B 852     5871   5975   7030   -145    188     67       C  
-ATOM   3933  CG  LYS B 852     -68.899  11.689  -0.200  1.00 53.12           C  
-ANISOU 3933  CG  LYS B 852     6284   6381   7517   -141    152     12       C  
-ATOM   3934  CD  LYS B 852     -69.475  10.903   0.952  1.00 53.92           C  
-ANISOU 3934  CD  LYS B 852     6404   6500   7584   -113     99    -11       C  
-ATOM   3935  CE  LYS B 852     -68.876  11.361   2.280  1.00 59.02           C  
-ANISOU 3935  CE  LYS B 852     7038   7116   8272   -111     60    -59       C  
-ATOM   3936  NZ  LYS B 852     -69.647  10.828   3.455  1.00 54.19           N  
-ANISOU 3936  NZ  LYS B 852     6455   6519   7615    -86     14    -74       N  
-ATOM   3937  N   GLN B 853     -71.197  14.074  -2.950  1.00 45.62           N  
-ANISOU 3937  N   GLN B 853     5405   5415   6516   -155    253    193       N  
-ATOM   3938  CA  GLN B 853     -71.132  15.528  -3.196  1.00 47.75           C  
-ANISOU 3938  CA  GLN B 853     5681   5630   6830   -166    279    223       C  
-ATOM   3939  C   GLN B 853     -72.466  16.202  -2.857  1.00 45.54           C  
-ANISOU 3939  C   GLN B 853     5430   5336   6537   -129    264    260       C  
-ATOM   3940  O   GLN B 853     -72.558  17.406  -2.605  1.00 48.17           O  
-ANISOU 3940  O   GLN B 853     5775   5612   6915   -122    273    270       O  
-ATOM   3941  CB  GLN B 853     -70.772  15.815  -4.699  1.00 52.14           C  
-ANISOU 3941  CB  GLN B 853     6241   6192   7377   -202    328    274       C  
-ATOM   3942  CG  GLN B 853     -69.856  17.019  -4.883  1.00 58.62           C  
-ANISOU 3942  CG  GLN B 853     7053   6953   8266   -236    362    278       C  
-ATOM   3943  CD  GLN B 853     -68.528  16.852  -4.174  1.00 62.59           C  
-ANISOU 3943  CD  GLN B 853     7514   7441   8827   -259    357    208       C  
-ATOM   3944  OE1 GLN B 853     -68.140  15.742  -3.824  1.00 56.45           O  
-ANISOU 3944  OE1 GLN B 853     6712   6701   8034   -251    338    164       O  
-ATOM   3945  NE2 GLN B 853     -67.814  17.962  -3.972  1.00 67.50           N  
-ANISOU 3945  NE2 GLN B 853     8126   8003   9516   -288    373    200       N  
-ATOM   3946  N   LEU B 854     -73.512  15.397  -2.830  1.00 44.02           N  
-ANISOU 3946  N   LEU B 854     5247   5194   6285   -103    242    277       N  
-ATOM   3947  CA  LEU B 854     -74.849  15.866  -2.541  1.00 40.61           C  
-ANISOU 3947  CA  LEU B 854     4830   4763   5837    -64    229    313       C  
-ATOM   3948  C   LEU B 854     -74.977  16.267  -1.083  1.00 40.35           C  
-ANISOU 3948  C   LEU B 854     4799   4697   5836    -36    208    262       C  
-ATOM   3949  O   LEU B 854     -74.296  15.746  -0.180  1.00 40.71           O  
-ANISOU 3949  O   LEU B 854     4835   4742   5890    -43    188    201       O  
-ATOM   3950  CB  LEU B 854     -75.827  14.754  -2.805  1.00 40.80           C  
-ANISOU 3950  CB  LEU B 854     4856   4857   5789    -53    208    336       C  
-ATOM   3951  CG  LEU B 854     -77.177  15.052  -3.402  1.00 41.01           C  
-ANISOU 3951  CG  LEU B 854     4890   4910   5782    -30    205    406       C  
-ATOM   3952  CD1 LEU B 854     -77.061  15.922  -4.639  1.00 43.89           C  
-ANISOU 3952  CD1 LEU B 854     5267   5253   6157    -45    233    468       C  
-ATOM   3953  CD2 LEU B 854     -77.835  13.727  -3.731  1.00 40.21           C  
-ANISOU 3953  CD2 LEU B 854     4787   4882   5608    -38    182    417       C  
-ATOM   3954  N   HIS B 855     -75.801  17.261  -0.843  1.00 40.24           N  
-ANISOU 3954  N   HIS B 855     4798   4650   5841     -2    214    288       N  
-ATOM   3955  CA  HIS B 855     -75.998  17.747   0.506  1.00 41.52           C  
-ANISOU 3955  CA  HIS B 855     4967   4778   6029     26    202    238       C  
-ATOM   3956  C   HIS B 855     -77.019  16.839   1.207  1.00 39.51           C  
-ANISOU 3956  C   HIS B 855     4709   4584   5719     56    178    230       C  
-ATOM   3957  O   HIS B 855     -77.584  15.951   0.581  1.00 43.02           O  
-ANISOU 3957  O   HIS B 855     5144   5088   6112     52    170    266       O  
-ATOM   3958  CB  HIS B 855     -76.460  19.204   0.467  1.00 44.36           C  
-ANISOU 3958  CB  HIS B 855     5347   5072   6438     54    225    266       C  
-ATOM   3959  CG  HIS B 855     -77.746  19.406  -0.263  1.00 49.41           C  
-ANISOU 3959  CG  HIS B 855     5985   5736   7053     91    232    341       C  
-ATOM   3960  ND1 HIS B 855     -77.882  19.174  -1.619  1.00 52.62           N  
-ANISOU 3960  ND1 HIS B 855     6387   6174   7432     72    239    409       N  
-ATOM   3961  CD2 HIS B 855     -78.963  19.805   0.178  1.00 50.02           C  
-ANISOU 3961  CD2 HIS B 855     6062   5815   7129    145    232    358       C  
-ATOM   3962  CE1 HIS B 855     -79.131  19.414  -1.978  1.00 52.09           C  
-ANISOU 3962  CE1 HIS B 855     6316   6129   7347    112    235    468       C  
-ATOM   3963  NE2 HIS B 855     -79.803  19.805  -0.910  1.00 51.34           N  
-ANISOU 3963  NE2 HIS B 855     6220   6016   7272    159    233    439       N  
-ATOM   3964  N   ASN B 856     -77.238  17.071   2.498  1.00 37.44           N  
-ANISOU 3964  N   ASN B 856     4456   4305   5465     80    168    181       N  
-ATOM   3965  CA  ASN B 856     -78.290  16.406   3.260  1.00 36.10           C  
-ANISOU 3965  CA  ASN B 856     4284   4187   5246    109    153    174       C  
-ATOM   3966  C   ASN B 856     -78.109  14.869   3.234  1.00 35.56           C  
-ANISOU 3966  C   ASN B 856     4207   4183   5122     82    125    166       C  
-ATOM   3967  O   ASN B 856     -78.977  14.103   2.794  1.00 37.55           O  
-ANISOU 3967  O   ASN B 856     4449   4492   5326     85    119    206       O  
-ATOM   3968  CB  ASN B 856     -79.644  16.837   2.723  1.00 35.97           C  
-ANISOU 3968  CB  ASN B 856     4258   4189   5220    148    170    238       C  
-ATOM   3969  CG  ASN B 856     -80.774  16.354   3.564  1.00 36.96           C  
-ANISOU 3969  CG  ASN B 856     4374   4365   5304    179    163    231       C  
-ATOM   3970  OD1 ASN B 856     -80.599  16.007   4.730  1.00 39.46           O  
-ANISOU 3970  OD1 ASN B 856     4702   4686   5605    178    152    174       O  
-ATOM   3971  ND2 ASN B 856     -81.963  16.302   2.975  1.00 38.01           N  
-ANISOU 3971  ND2 ASN B 856     4485   4540   5416    204    169    292       N  
-ATOM   3972  N   ARG B 857     -76.952  14.458   3.718  1.00 33.22           N  
-ANISOU 3972  N   ARG B 857     3913   3872   4837     54    106    115       N  
-ATOM   3973  CA  ARG B 857     -76.607  13.074   3.890  1.00 31.63           C  
-ANISOU 3973  CA  ARG B 857     3708   3714   4595     34     77     97       C  
-ATOM   3974  C   ARG B 857     -76.925  12.638   5.298  1.00 30.59           C  
-ANISOU 3974  C   ARG B 857     3591   3600   4433     47     51     56       C  
-ATOM   3975  O   ARG B 857     -76.507  13.270   6.257  1.00 30.00           O  
-ANISOU 3975  O   ARG B 857     3528   3489   4382     52     45     10       O  
-ATOM   3976  CB  ARG B 857     -75.137  12.871   3.561  1.00 33.18           C  
-ANISOU 3976  CB  ARG B 857     3893   3887   4826      1     71     69       C  
-ATOM   3977  CG  ARG B 857     -74.949  12.855   2.071  1.00 34.88           C  
-ANISOU 3977  CG  ARG B 857     4097   4109   5046    -17     98    114       C  
-ATOM   3978  CD  ARG B 857     -73.581  13.156   1.524  1.00 36.05           C  
-ANISOU 3978  CD  ARG B 857     4229   4225   5244    -47    114     97       C  
-ATOM   3979  NE  ARG B 857     -72.486  13.124   2.448  1.00 37.45           N  
-ANISOU 3979  NE  ARG B 857     4395   4377   5459    -58     90     37       N  
-ATOM   3980  CZ  ARG B 857     -71.780  14.177   2.835  1.00 43.50           C  
-ANISOU 3980  CZ  ARG B 857     5155   5091   6282    -70     96      9       C  
-ATOM   3981  NH1 ARG B 857     -72.061  15.423   2.403  1.00 40.08           N  
-ANISOU 3981  NH1 ARG B 857     4733   4616   5881    -69    128     37       N  
-ATOM   3982  NH2 ARG B 857     -70.771  13.965   3.692  1.00 47.44           N  
-ANISOU 3982  NH2 ARG B 857     5639   5578   6808    -83     64    -46       N  
-ATOM   3983  N   ARG B 858     -77.685  11.555   5.419  1.00 28.71           N  
-ANISOU 3983  N   ARG B 858     3355   3417   4137     47     36     74       N  
-ATOM   3984  CA  ARG B 858     -78.238  11.155   6.701  1.00 29.15           C  
-ANISOU 3984  CA  ARG B 858     3426   3496   4153     59     19     48       C  
-ATOM   3985  C   ARG B 858     -77.995   9.659   7.007  1.00 28.32           C  
-ANISOU 3985  C   ARG B 858     3332   3428   4002     36    -18     40       C  
-ATOM   3986  O   ARG B 858     -78.133   8.807   6.101  1.00 28.12           O  
-ANISOU 3986  O   ARG B 858     3299   3429   3956     19    -21     73       O  
-ATOM   3987  CB  ARG B 858     -79.744  11.421   6.701  1.00 33.12           C  
-ANISOU 3987  CB  ARG B 858     3922   4034   4629     86     43     87       C  
-ATOM   3988  CG  ARG B 858     -80.231  12.045   7.978  1.00 38.37           C  
-ANISOU 3988  CG  ARG B 858     4601   4690   5287    113     54     51       C  
-ATOM   3989  CD  ARG B 858     -81.654  12.606   7.920  1.00 39.42           C  
-ANISOU 3989  CD  ARG B 858     4716   4848   5413    150     89     87       C  
-ATOM   3990  NE  ARG B 858     -81.727  13.934   7.297  1.00 41.57           N  
-ANISOU 3990  NE  ARG B 858     4979   5071   5744    179    119    104       N  
-ATOM   3991  CZ  ARG B 858     -82.797  14.726   7.310  1.00 40.16           C  
-ANISOU 3991  CZ  ARG B 858     4785   4894   5579    223    151    128       C  
-ATOM   3992  NH1 ARG B 858     -83.923  14.343   7.914  1.00 40.20           N  
-ANISOU 3992  NH1 ARG B 858     4776   4955   5543    243    162    135       N  
-ATOM   3993  NH2 ARG B 858     -82.749  15.905   6.698  1.00 38.56           N  
-ANISOU 3993  NH2 ARG B 858     4579   4637   5433    249    173    147       N  
-ATOM   3994  N   LEU B 859     -77.677   9.368   8.271  1.00 27.26           N  
-ANISOU 3994  N   LEU B 859     3218   3291   3850     35    -46     -3       N  
-ATOM   3995  CA  LEU B 859     -77.535   8.020   8.779  1.00 28.52           C  
-ANISOU 3995  CA  LEU B 859     3394   3478   3964     18    -84     -8       C  
-ATOM   3996  C   LEU B 859     -78.893   7.487   9.246  1.00 27.07           C  
-ANISOU 3996  C   LEU B 859     3222   3345   3718     20    -78     19       C  
-ATOM   3997  O   LEU B 859     -79.456   7.948  10.239  1.00 26.04           O  
-ANISOU 3997  O   LEU B 859     3104   3224   3566     34    -68      2       O  
-ATOM   3998  CB  LEU B 859     -76.506   7.974   9.907  1.00 30.78           C  
-ANISOU 3998  CB  LEU B 859     3698   3740   4258     13   -123    -61       C  
-ATOM   3999  CG  LEU B 859     -75.961   6.560  10.194  1.00 32.70           C  
-ANISOU 3999  CG  LEU B 859     3954   3995   4473     -3   -170    -64       C  
-ATOM   4000  CD1 LEU B 859     -74.984   6.104   9.111  1.00 33.95           C  
-ANISOU 4000  CD1 LEU B 859     4089   4136   4675    -11   -175    -60       C  
-ATOM   4001  CD2 LEU B 859     -75.284   6.521  11.560  1.00 32.24           C  
-ANISOU 4001  CD2 LEU B 859     3920   3926   4405     -4   -214   -108       C  
-ATOM   4002  N   LEU B 860     -79.420   6.516   8.505  1.00 26.03           N  
-ANISOU 4002  N   LEU B 860     3086   3248   3557      3    -81     59       N  
-ATOM   4003  CA  LEU B 860     -80.822   6.070   8.657  1.00 25.53           C  
-ANISOU 4003  CA  LEU B 860     3022   3238   3442     -1    -69     95       C  
-ATOM   4004  C   LEU B 860     -80.907   4.570   8.739  1.00 24.54           C  
-ANISOU 4004  C   LEU B 860     2918   3137   3269    -33   -101    109       C  
-ATOM   4005  O   LEU B 860     -80.014   3.865   8.295  1.00 25.75           O  
-ANISOU 4005  O   LEU B 860     3083   3268   3435    -47   -126    100       O  
-ATOM   4006  CB  LEU B 860     -81.660   6.547   7.451  1.00 25.77           C  
-ANISOU 4006  CB  LEU B 860     3019   3289   3485      5    -37    143       C  
-ATOM   4007  CG  LEU B 860     -81.787   8.066   7.257  1.00 24.96           C  
-ANISOU 4007  CG  LEU B 860     2895   3158   3429     41     -3    142       C  
-ATOM   4008  CD1 LEU B 860     -82.417   8.378   5.913  1.00 24.16           C  
-ANISOU 4008  CD1 LEU B 860     2765   3075   3339     44     16    196       C  
-ATOM   4009  CD2 LEU B 860     -82.594   8.694   8.387  1.00 24.08           C  
-ANISOU 4009  CD2 LEU B 860     2784   3060   3305     69     19    127       C  
-ATOM   4010  N   TRP B 861     -82.013   4.093   9.285  1.00 25.23           N  
-ANISOU 4010  N   TRP B 861     3011   3270   3305    -45    -96    131       N  
-ATOM   4011  CA  TRP B 861     -82.215   2.673   9.514  1.00 25.24           C  
-ANISOU 4011  CA  TRP B 861     3041   3293   3258    -80   -126    147       C  
-ATOM   4012  C   TRP B 861     -82.824   1.971   8.317  1.00 25.54           C  
-ANISOU 4012  C   TRP B 861     3066   3356   3283   -108   -125    189       C  
-ATOM   4013  O   TRP B 861     -83.646   2.542   7.590  1.00 24.59           O  
-ANISOU 4013  O   TRP B 861     2910   3264   3168   -102    -97    220       O  
-ATOM   4014  CB  TRP B 861     -83.182   2.466  10.696  1.00 25.50           C  
-ANISOU 4014  CB  TRP B 861     3086   3367   3237    -89   -118    155       C  
-ATOM   4015  CG  TRP B 861     -82.724   3.055  11.990  1.00 25.07           C  
-ANISOU 4015  CG  TRP B 861     3053   3295   3177    -68   -121    112       C  
-ATOM   4016  CD1 TRP B 861     -83.192   4.194  12.580  1.00 25.77           C  
-ANISOU 4016  CD1 TRP B 861     3128   3393   3270    -39    -84     93       C  
-ATOM   4017  CD2 TRP B 861     -81.707   2.541  12.855  1.00 25.16           C  
-ANISOU 4017  CD2 TRP B 861     3107   3277   3177    -75   -165     81       C  
-ATOM   4018  NE1 TRP B 861     -82.508   4.437  13.751  1.00 24.88           N  
-ANISOU 4018  NE1 TRP B 861     3050   3258   3144    -32   -101     48       N  
-ATOM   4019  CE2 TRP B 861     -81.606   3.426  13.953  1.00 26.37           C  
-ANISOU 4019  CE2 TRP B 861     3272   3426   3321    -55   -154     43       C  
-ATOM   4020  CE3 TRP B 861     -80.884   1.416  12.819  1.00 24.36           C  
-ANISOU 4020  CE3 TRP B 861     3035   3151   3071    -94   -214     82       C  
-ATOM   4021  CZ2 TRP B 861     -80.712   3.208  15.001  1.00 26.47           C  
-ANISOU 4021  CZ2 TRP B 861     3324   3416   3316    -59   -197      9       C  
-ATOM   4022  CZ3 TRP B 861     -79.996   1.211  13.835  1.00 25.07           C  
-ANISOU 4022  CZ3 TRP B 861     3158   3216   3150    -91   -255     51       C  
-ATOM   4023  CH2 TRP B 861     -79.913   2.097  14.922  1.00 25.92           C  
-ANISOU 4023  CH2 TRP B 861     3277   3326   3244    -76   -249     17       C  
-ATOM   4024  N   HIS B 862     -82.448   0.714   8.134  1.00 24.26           N  
-ANISOU 4024  N   HIS B 862     2936   3183   3101   -137   -157    192       N  
-ATOM   4025  CA  HIS B 862     -83.176  -0.167   7.252  1.00 23.98           C  
-ANISOU 4025  CA  HIS B 862     2901   3175   3035   -175   -161    229       C  
-ATOM   4026  C   HIS B 862     -83.201  -1.569   7.856  1.00 24.05           C  
-ANISOU 4026  C   HIS B 862     2956   3179   3002   -210   -195    232       C  
-ATOM   4027  O   HIS B 862     -82.165  -2.196   8.007  1.00 21.34           O  
-ANISOU 4027  O   HIS B 862     2647   2790   2672   -207   -224    208       O  
-ATOM   4028  CB  HIS B 862     -82.559  -0.218   5.864  1.00 23.23           C  
-ANISOU 4028  CB  HIS B 862     2801   3056   2969   -177   -159    227       C  
-ATOM   4029  CG  HIS B 862     -83.317  -1.075   4.910  1.00 24.99           C  
-ANISOU 4029  CG  HIS B 862     3030   3308   3156   -219   -165    261       C  
-ATOM   4030  ND1 HIS B 862     -84.336  -0.598   4.127  1.00 26.89           N  
-ANISOU 4030  ND1 HIS B 862     3236   3596   3386   -230   -146    299       N  
-ATOM   4031  CD2 HIS B 862     -83.231  -2.394   4.631  1.00 28.11           C  
-ANISOU 4031  CD2 HIS B 862     3465   3692   3524   -257   -190    261       C  
-ATOM   4032  CE1 HIS B 862     -84.831  -1.572   3.390  1.00 26.17           C  
-ANISOU 4032  CE1 HIS B 862     3161   3525   3260   -276   -162    320       C  
-ATOM   4033  NE2 HIS B 862     -84.174  -2.673   3.673  1.00 27.50           N  
-ANISOU 4033  NE2 HIS B 862     3377   3654   3417   -294   -187    296       N  
-ATOM   4034  N   GLY B 863     -84.404  -2.053   8.146  1.00 24.76           N  
-ANISOU 4034  N   GLY B 863     3045   3316   3045   -245   -191    267       N  
-ATOM   4035  CA  GLY B 863     -84.600  -3.384   8.664  1.00 26.52           C  
-ANISOU 4035  CA  GLY B 863     3315   3537   3225   -287   -220    280       C  
-ATOM   4036  C   GLY B 863     -85.082  -4.336   7.603  1.00 27.60           C  
-ANISOU 4036  C   GLY B 863     3462   3682   3343   -334   -231    306       C  
-ATOM   4037  O   GLY B 863     -85.748  -3.936   6.635  1.00 28.63           O  
-ANISOU 4037  O   GLY B 863     3554   3848   3476   -344   -213    327       O  
-ATOM   4038  N   SER B 864     -84.763  -5.605   7.794  1.00 27.55           N  
-ANISOU 4038  N   SER B 864     3511   3641   3316   -365   -264    305       N  
-ATOM   4039  CA  SER B 864     -85.136  -6.647   6.832  1.00 28.76           C  
-ANISOU 4039  CA  SER B 864     3688   3790   3449   -415   -279    322       C  
-ATOM   4040  C   SER B 864     -85.026  -8.007   7.534  1.00 29.99           C  
-ANISOU 4040  C   SER B 864     3909   3909   3575   -451   -314    328       C  
-ATOM   4041  O   SER B 864     -84.364  -8.110   8.563  1.00 27.38           O  
-ANISOU 4041  O   SER B 864     3607   3548   3249   -426   -331    315       O  
-ATOM   4042  CB  SER B 864     -84.190  -6.615   5.642  1.00 27.73           C  
-ANISOU 4042  CB  SER B 864     3563   3618   3356   -394   -279    293       C  
-ATOM   4043  OG  SER B 864     -84.704  -7.329   4.558  1.00 30.70           O  
-ANISOU 4043  OG  SER B 864     3953   4002   3708   -441   -285    307       O  
-ATOM   4044  N   ARG B 865     -85.667  -9.029   6.972  1.00 30.86           N  
-ANISOU 4044  N   ARG B 865     4048   4022   3655   -511   -328    350       N  
-ATOM   4045  CA  ARG B 865     -85.573 -10.370   7.501  1.00 32.19           C  
-ANISOU 4045  CA  ARG B 865     4286   4146   3799   -549   -362    359       C  
-ATOM   4046  C   ARG B 865     -84.153 -10.858   7.415  1.00 30.79           C  
-ANISOU 4046  C   ARG B 865     4155   3885   3660   -507   -387    321       C  
-ATOM   4047  O   ARG B 865     -83.424 -10.551   6.468  1.00 30.09           O  
-ANISOU 4047  O   ARG B 865     4052   3773   3609   -474   -377    289       O  
-ATOM   4048  CB  ARG B 865     -86.476 -11.320   6.731  1.00 36.12           C  
-ANISOU 4048  CB  ARG B 865     4806   4655   4264   -625   -371    384       C  
-ATOM   4049  CG  ARG B 865     -87.965 -11.128   6.992  1.00 40.35           C  
-ANISOU 4049  CG  ARG B 865     5299   5274   4759   -679   -353    430       C  
-ATOM   4050  CD  ARG B 865     -88.788 -11.865   5.964  1.00 45.89           C  
-ANISOU 4050  CD  ARG B 865     6008   5993   5435   -752   -364    448       C  
-ATOM   4051  NE  ARG B 865     -90.200 -11.468   6.038  1.00 51.17           N  
-ANISOU 4051  NE  ARG B 865     6612   6755   6076   -797   -346    491       N  
-ATOM   4052  CZ  ARG B 865     -91.122 -12.071   6.794  1.00 56.43           C  
-ANISOU 4052  CZ  ARG B 865     7284   7454   6704   -859   -348    529       C  
-ATOM   4053  NH1 ARG B 865     -92.372 -11.622   6.785  1.00 64.81           N  
-ANISOU 4053  NH1 ARG B 865     8272   8605   7748   -892   -326    566       N  
-ATOM   4054  NH2 ARG B 865     -90.812 -13.107   7.561  1.00 54.88           N  
-ANISOU 4054  NH2 ARG B 865     7162   7202   6489   -888   -370    534       N  
-ATOM   4055  N   THR B 866     -83.772 -11.621   8.424  1.00 31.44           N  
-ANISOU 4055  N   THR B 866     4290   3924   3732   -508   -419    327       N  
-ATOM   4056  CA  THR B 866     -82.433 -12.161   8.555  1.00 32.24           C  
-ANISOU 4056  CA  THR B 866     4432   3945   3871   -463   -450    297       C  
-ATOM   4057  C   THR B 866     -82.011 -12.934   7.318  1.00 31.40           C  
-ANISOU 4057  C   THR B 866     4356   3787   3788   -469   -454    273       C  
-ATOM   4058  O   THR B 866     -80.859 -12.836   6.889  1.00 31.56           O  
-ANISOU 4058  O   THR B 866     4371   3762   3858   -415   -455    234       O  
-ATOM   4059  CB  THR B 866     -82.344 -13.002   9.847  1.00 33.00           C  
-ANISOU 4059  CB  THR B 866     4589   4008   3940   -476   -491    322       C  
-ATOM   4060  OG1 THR B 866     -82.721 -12.166  10.959  1.00 37.33           O  
-ANISOU 4060  OG1 THR B 866     5109   4612   4462   -469   -480    338       O  
-ATOM   4061  CG2 THR B 866     -80.944 -13.479  10.098  1.00 33.38           C  
-ANISOU 4061  CG2 THR B 866     4671   3977   4033   -420   -529    296       C  
-ATOM   4062  N   THR B 867     -82.950 -13.650   6.718  1.00 31.52           N  
-ANISOU 4062  N   THR B 867     4397   3812   3766   -536   -452    293       N  
-ATOM   4063  CA  THR B 867     -82.678 -14.468   5.535  1.00 32.07           C  
-ANISOU 4063  CA  THR B 867     4506   3832   3846   -552   -454    267       C  
-ATOM   4064  C   THR B 867     -82.413 -13.647   4.261  1.00 34.83           C  
-ANISOU 4064  C   THR B 867     4807   4209   4218   -528   -419    236       C  
-ATOM   4065  O   THR B 867     -82.054 -14.201   3.226  1.00 36.91           O  
-ANISOU 4065  O   THR B 867     5101   4433   4488   -534   -413    206       O  
-ATOM   4066  CB  THR B 867     -83.844 -15.443   5.267  1.00 32.71           C  
-ANISOU 4066  CB  THR B 867     4631   3920   3877   -642   -466    298       C  
-ATOM   4067  OG1 THR B 867     -85.100 -14.747   5.281  1.00 32.86           O  
-ANISOU 4067  OG1 THR B 867     4593   4033   3858   -687   -446    334       O  
-ATOM   4068  CG2 THR B 867     -83.861 -16.523   6.331  1.00 34.45           C  
-ANISOU 4068  CG2 THR B 867     4921   4087   4082   -666   -503    324       C  
-ATOM   4069  N   ASN B 868     -82.591 -12.334   4.338  1.00 33.40           N  
-ANISOU 4069  N   ASN B 868     4556   4091   4045   -502   -392    243       N  
-ATOM   4070  CA  ASN B 868     -82.227 -11.474   3.240  1.00 30.99           C  
-ANISOU 4070  CA  ASN B 868     4206   3806   3762   -475   -360    218       C  
-ATOM   4071  C   ASN B 868     -80.802 -10.971   3.316  1.00 28.19           C  
-ANISOU 4071  C   ASN B 868     3833   3411   3467   -401   -351    178       C  
-ATOM   4072  O   ASN B 868     -80.307 -10.454   2.345  1.00 26.91           O  
-ANISOU 4072  O   ASN B 868     3646   3251   3327   -379   -323    153       O  
-ATOM   4073  CB  ASN B 868     -83.138 -10.263   3.198  1.00 32.38           C  
-ANISOU 4073  CB  ASN B 868     4315   4065   3923   -482   -335    248       C  
-ATOM   4074  CG  ASN B 868     -84.574 -10.590   2.894  1.00 32.99           C  
-ANISOU 4074  CG  ASN B 868     4389   4197   3947   -554   -339    288       C  
-ATOM   4075  OD1 ASN B 868     -85.470  -9.923   3.395  1.00 36.51           O  
-ANISOU 4075  OD1 ASN B 868     4789   4706   4378   -564   -329    322       O  
-ATOM   4076  ND2 ASN B 868     -84.815 -11.570   2.053  1.00 35.23           N  
-ANISOU 4076  ND2 ASN B 868     4719   4460   4206   -605   -352    283       N  
-ATOM   4077  N   PHE B 869     -80.115 -11.129   4.439  1.00 29.20           N  
-ANISOU 4077  N   PHE B 869     3973   3503   3620   -364   -376    172       N  
-ATOM   4078  CA  PHE B 869     -78.861 -10.389   4.646  1.00 30.68           C  
-ANISOU 4078  CA  PHE B 869     4123   3668   3864   -297   -370    139       C  
-ATOM   4079  C   PHE B 869     -77.643 -10.851   3.867  1.00 32.15           C  
-ANISOU 4079  C   PHE B 869     4321   3797   4098   -259   -363     95       C  
-ATOM   4080  O   PHE B 869     -76.713 -10.060   3.632  1.00 33.60           O  
-ANISOU 4080  O   PHE B 869     4457   3978   4330   -214   -343     67       O  
-ATOM   4081  CB  PHE B 869     -78.537 -10.241   6.132  1.00 29.11           C  
-ANISOU 4081  CB  PHE B 869     3926   3463   3674   -271   -403    148       C  
-ATOM   4082  CG  PHE B 869     -79.142  -9.024   6.714  1.00 29.80           C  
-ANISOU 4082  CG  PHE B 869     3965   3611   3745   -271   -385    166       C  
-ATOM   4083  CD1 PHE B 869     -80.461  -9.028   7.148  1.00 31.05           C  
-ANISOU 4083  CD1 PHE B 869     4128   3819   3848   -317   -381    206       C  
-ATOM   4084  CD2 PHE B 869     -78.435  -7.849   6.755  1.00 29.56           C  
-ANISOU 4084  CD2 PHE B 869     3884   3590   3757   -227   -368    142       C  
-ATOM   4085  CE1 PHE B 869     -81.056  -7.891   7.640  1.00 29.89           C  
-ANISOU 4085  CE1 PHE B 869     3937   3729   3691   -312   -358    218       C  
-ATOM   4086  CE2 PHE B 869     -79.014  -6.711   7.275  1.00 30.57           C  
-ANISOU 4086  CE2 PHE B 869     3975   3768   3874   -225   -349    154       C  
-ATOM   4087  CZ  PHE B 869     -80.329  -6.728   7.704  1.00 30.36           C  
-ANISOU 4087  CZ  PHE B 869     3953   3789   3793   -263   -342    191       C  
-ATOM   4088  N   ALA B 870     -77.613 -12.109   3.470  1.00 32.74           N  
-ANISOU 4088  N   ALA B 870     4454   3822   4163   -278   -377     86       N  
-ATOM   4089  CA  ALA B 870     -76.534 -12.547   2.582  1.00 35.84           C  
-ANISOU 4089  CA  ALA B 870     4856   4162   4598   -242   -359     38       C  
-ATOM   4090  C   ALA B 870     -76.665 -11.825   1.251  1.00 33.08           C  
-ANISOU 4090  C   ALA B 870     4475   3855   4241   -255   -308     23       C  
-ATOM   4091  O   ALA B 870     -75.683 -11.399   0.669  1.00 37.28           O  
-ANISOU 4091  O   ALA B 870     4973   4374   4815   -214   -277    -12       O  
-ATOM   4092  CB  ALA B 870     -76.567 -14.044   2.360  1.00 36.77           C  
-ANISOU 4092  CB  ALA B 870     5052   4214   4705   -261   -380     29       C  
-ATOM   4093  N   GLY B 871     -77.884 -11.721   0.766  1.00 31.29           N  
-ANISOU 4093  N   GLY B 871     4256   3676   3956   -314   -300     52       N  
-ATOM   4094  CA  GLY B 871     -78.134 -11.023  -0.463  1.00 31.43           C  
-ANISOU 4094  CA  GLY B 871     4247   3738   3956   -331   -259     47       C  
-ATOM   4095  C   GLY B 871     -77.804  -9.560  -0.304  1.00 31.14           C  
-ANISOU 4095  C   GLY B 871     4139   3742   3951   -295   -235     54       C  
-ATOM   4096  O   GLY B 871     -77.154  -8.977  -1.162  1.00 33.24           O  
-ANISOU 4096  O   GLY B 871     4378   4013   4240   -275   -197     32       O  
-ATOM   4097  N   ILE B 872     -78.264  -8.959   0.796  1.00 29.33           N  
-ANISOU 4097  N   ILE B 872     3881   3540   3722   -291   -254     85       N  
-ATOM   4098  CA  ILE B 872     -78.005  -7.553   1.024  1.00 27.84           C  
-ANISOU 4098  CA  ILE B 872     3631   3384   3565   -258   -234     90       C  
-ATOM   4099  C   ILE B 872     -76.499  -7.262   1.133  1.00 29.36           C  
-ANISOU 4099  C   ILE B 872     3798   3534   3823   -203   -224     48       C  
-ATOM   4100  O   ILE B 872     -76.000  -6.304   0.549  1.00 27.74           O  
-ANISOU 4100  O   ILE B 872     3551   3342   3646   -184   -189     37       O  
-ATOM   4101  CB  ILE B 872     -78.742  -7.030   2.248  1.00 25.19           C  
-ANISOU 4101  CB  ILE B 872     3276   3080   3214   -261   -254    122       C  
-ATOM   4102  CG1 ILE B 872     -80.234  -7.016   2.007  1.00 24.03           C  
-ANISOU 4102  CG1 ILE B 872     3131   2989   3012   -313   -252    165       C  
-ATOM   4103  CG2 ILE B 872     -78.247  -5.641   2.631  1.00 25.87           C  
-ANISOU 4103  CG2 ILE B 872     3307   3179   3342   -221   -235    115       C  
-ATOM   4104  CD1 ILE B 872     -81.040  -6.876   3.268  1.00 25.39           C  
-ANISOU 4104  CD1 ILE B 872     3295   3189   3161   -322   -270    195       C  
-ATOM   4105  N   LEU B 873     -75.770  -8.056   1.876  1.00 29.97           N  
-ANISOU 4105  N   LEU B 873     3898   3562   3927   -176   -256     28       N  
-ATOM   4106  CA  LEU B 873     -74.334  -7.803   1.965  1.00 31.23           C  
-ANISOU 4106  CA  LEU B 873     4024   3687   4155   -123   -250    -10       C  
-ATOM   4107  C   LEU B 873     -73.620  -8.041   0.646  1.00 31.88           C  
-ANISOU 4107  C   LEU B 873     4104   3751   4259   -114   -207    -45       C  
-ATOM   4108  O   LEU B 873     -72.775  -7.242   0.249  1.00 33.52           O  
-ANISOU 4108  O   LEU B 873     4262   3963   4510    -88   -174    -66       O  
-ATOM   4109  CB  LEU B 873     -73.701  -8.612   3.087  1.00 31.41           C  
-ANISOU 4109  CB  LEU B 873     4068   3662   4204    -93   -301    -19       C  
-ATOM   4110  CG  LEU B 873     -74.230  -8.189   4.462  1.00 33.22           C  
-ANISOU 4110  CG  LEU B 873     4296   3915   4412    -99   -338     11       C  
-ATOM   4111  CD1 LEU B 873     -73.531  -9.041   5.495  1.00 34.34           C  
-ANISOU 4111  CD1 LEU B 873     4464   4008   4576    -70   -393      6       C  
-ATOM   4112  CD2 LEU B 873     -73.987  -6.700   4.741  1.00 34.67           C  
-ANISOU 4112  CD2 LEU B 873     4419   4134   4622    -83   -320      7       C  
-ATOM   4113  N   SER B 874     -73.956  -9.098  -0.072  1.00 30.01           N  
-ANISOU 4113  N   SER B 874     3920   3494   3988   -138   -202    -53       N  
-ATOM   4114  CA  SER B 874     -73.247  -9.325  -1.321  1.00 31.99           C  
-ANISOU 4114  CA  SER B 874     4172   3728   4254   -128   -155    -92       C  
-ATOM   4115  C   SER B 874     -73.678  -8.375  -2.432  1.00 30.20           C  
-ANISOU 4115  C   SER B 874     3924   3556   3996   -158   -107    -80       C  
-ATOM   4116  O   SER B 874     -72.869  -8.028  -3.274  1.00 29.02           O  
-ANISOU 4116  O   SER B 874     3750   3405   3872   -141    -60   -108       O  
-ATOM   4117  CB  SER B 874     -73.335 -10.759  -1.787  1.00 32.73           C  
-ANISOU 4117  CB  SER B 874     4337   3775   4325   -141   -161   -114       C  
-ATOM   4118  OG  SER B 874     -74.581 -10.986  -2.311  1.00 36.48           O  
-ANISOU 4118  OG  SER B 874     4853   4281   4728   -203   -163    -89       O  
-ATOM   4119  N   GLN B 875     -74.934  -7.942  -2.437  1.00 30.10           N  
-ANISOU 4119  N   GLN B 875     3916   3591   3929   -202   -118    -35       N  
-ATOM   4120  CA  GLN B 875     -75.417  -7.123  -3.557  1.00 32.88           C  
-ANISOU 4120  CA  GLN B 875     4254   3993   4247   -232    -79    -17       C  
-ATOM   4121  C   GLN B 875     -75.914  -5.743  -3.204  1.00 30.58           C  
-ANISOU 4121  C   GLN B 875     3912   3747   3961   -231    -77     23       C  
-ATOM   4122  O   GLN B 875     -76.238  -4.988  -4.089  1.00 30.49           O  
-ANISOU 4122  O   GLN B 875     3885   3772   3927   -249    -48     43       O  
-ATOM   4123  CB  GLN B 875     -76.528  -7.866  -4.255  1.00 36.18           C  
-ANISOU 4123  CB  GLN B 875     4724   4431   4591   -289    -89      0       C  
-ATOM   4124  CG  GLN B 875     -76.056  -9.258  -4.564  1.00 39.63           C  
-ANISOU 4124  CG  GLN B 875     5221   4813   5025   -290    -92    -45       C  
-ATOM   4125  CD  GLN B 875     -76.354  -9.593  -5.979  1.00 48.10           C  
-ANISOU 4125  CD  GLN B 875     6333   5901   6040   -332    -62    -59       C  
-ATOM   4126  OE1 GLN B 875     -77.430 -10.110  -6.285  1.00 49.92           O  
-ANISOU 4126  OE1 GLN B 875     6605   6154   6210   -388    -86    -38       O  
-ATOM   4127  NE2 GLN B 875     -75.447  -9.204  -6.891  1.00 55.51           N  
-ANISOU 4127  NE2 GLN B 875     7257   6840   6996   -311     -8    -91       N  
-ATOM   4128  N   GLY B 876     -75.982  -5.429  -1.918  1.00 27.63           N  
-ANISOU 4128  N   GLY B 876     3516   3369   3613   -210   -108     35       N  
-ATOM   4129  CA  GLY B 876     -76.431  -4.133  -1.463  1.00 26.43           C  
-ANISOU 4129  CA  GLY B 876     3320   3251   3470   -204   -105     67       C  
-ATOM   4130  C   GLY B 876     -77.937  -4.108  -1.418  1.00 25.13           C  
-ANISOU 4130  C   GLY B 876     3166   3133   3248   -242   -121    113       C  
-ATOM   4131  O   GLY B 876     -78.599  -4.985  -1.921  1.00 25.38           O  
-ANISOU 4131  O   GLY B 876     3235   3176   3232   -280   -132    122       O  
-ATOM   4132  N   LEU B 877     -78.472  -3.024  -0.894  1.00 26.27           N  
-ANISOU 4132  N   LEU B 877     3273   3307   3401   -232   -120    142       N  
-ATOM   4133  CA  LEU B 877     -79.894  -2.758  -0.984  1.00 25.89           C  
-ANISOU 4133  CA  LEU B 877     3217   3312   3308   -261   -127    189       C  
-ATOM   4134  C   LEU B 877     -80.266  -2.488  -2.422  1.00 26.13           C  
-ANISOU 4134  C   LEU B 877     3247   3373   3309   -286   -105    211       C  
-ATOM   4135  O   LEU B 877     -79.558  -1.795  -3.153  1.00 24.64           O  
-ANISOU 4135  O   LEU B 877     3043   3174   3143   -271    -73    203       O  
-ATOM   4136  CB  LEU B 877     -80.281  -1.575  -0.108  1.00 25.91           C  
-ANISOU 4136  CB  LEU B 877     3178   3333   3334   -233   -123    209       C  
-ATOM   4137  CG  LEU B 877     -80.096  -1.805   1.365  1.00 25.16           C  
-ANISOU 4137  CG  LEU B 877     3089   3218   3252   -215   -147    192       C  
-ATOM   4138  CD1 LEU B 877     -80.441  -0.564   2.159  1.00 24.77           C  
-ANISOU 4138  CD1 LEU B 877     3003   3185   3224   -187   -136    203       C  
-ATOM   4139  CD2 LEU B 877     -80.952  -2.984   1.828  1.00 25.84           C  
-ANISOU 4139  CD2 LEU B 877     3209   3321   3290   -251   -177    208       C  
-ATOM   4140  N   ARG B 878     -81.366  -3.095  -2.835  1.00 29.52           N  
-ANISOU 4140  N   ARG B 878     3694   3840   3682   -331   -124    240       N  
-ATOM   4141  CA  ARG B 878     -81.830  -3.024  -4.189  1.00 31.00           C  
-ANISOU 4141  CA  ARG B 878     3888   4062   3828   -365   -114    263       C  
-ATOM   4142  C   ARG B 878     -83.258  -2.540  -4.203  1.00 31.08           C  
-ANISOU 4142  C   ARG B 878     3867   4135   3808   -386   -132    320       C  
-ATOM   4143  O   ARG B 878     -83.929  -2.484  -3.198  1.00 30.31           O  
-ANISOU 4143  O   ARG B 878     3747   4054   3716   -380   -148    337       O  
-ATOM   4144  CB  ARG B 878     -81.714  -4.374  -4.879  1.00 34.36           C  
-ANISOU 4144  CB  ARG B 878     4372   4472   4212   -407   -124    236       C  
-ATOM   4145  CG  ARG B 878     -80.292  -4.711  -5.323  1.00 39.20           C  
-ANISOU 4145  CG  ARG B 878     5010   5031   4852   -383    -95    181       C  
-ATOM   4146  CD  ARG B 878     -80.008  -6.179  -5.110  1.00 41.35           C  
-ANISOU 4146  CD  ARG B 878     5338   5259   5113   -399   -114    142       C  
-ATOM   4147  NE  ARG B 878     -80.060  -6.440  -3.670  1.00 46.80           N  
-ANISOU 4147  NE  ARG B 878     6021   5927   5833   -379   -143    143       N  
-ATOM   4148  CZ  ARG B 878     -80.452  -7.576  -3.098  1.00 47.37           C  
-ANISOU 4148  CZ  ARG B 878     6135   5980   5885   -404   -177    140       C  
-ATOM   4149  NH1 ARG B 878     -80.834  -8.626  -3.821  1.00 44.84           N  
-ANISOU 4149  NH1 ARG B 878     5868   5652   5519   -452   -187    131       N  
-ATOM   4150  NH2 ARG B 878     -80.475  -7.647  -1.774  1.00 49.34           N  
-ANISOU 4150  NH2 ARG B 878     6376   6215   6157   -385   -201    147       N  
-ATOM   4151  N   ILE B 879     -83.703  -2.186  -5.389  1.00 32.19           N  
-ANISOU 4151  N   ILE B 879     4003   4313   3915   -409   -127    351       N  
-ATOM   4152  CA  ILE B 879     -85.035  -1.717  -5.612  1.00 33.84           C  
-ANISOU 4152  CA  ILE B 879     4176   4586   4097   -428   -147    410       C  
-ATOM   4153  C   ILE B 879     -85.787  -2.892  -6.226  1.00 34.85           C  
-ANISOU 4153  C   ILE B 879     4338   4745   4159   -496   -179    417       C  
-ATOM   4154  O   ILE B 879     -85.215  -3.674  -6.966  1.00 31.71           O  
-ANISOU 4154  O   ILE B 879     3993   4324   3733   -524   -176    383       O  
-ATOM   4155  CB  ILE B 879     -84.966  -0.507  -6.565  1.00 35.64           C  
-ANISOU 4155  CB  ILE B 879     4379   4831   4330   -409   -126    444       C  
-ATOM   4156  CG1 ILE B 879     -84.341   0.689  -5.823  1.00 35.86           C  
-ANISOU 4156  CG1 ILE B 879     4373   4824   4428   -346    -97    439       C  
-ATOM   4157  CG2 ILE B 879     -86.328  -0.149  -7.126  1.00 35.50           C  
-ANISOU 4157  CG2 ILE B 879     4329   4884   4276   -433   -153    510       C  
-ATOM   4158  CD1 ILE B 879     -84.020   1.838  -6.743  1.00 37.45           C  
-ANISOU 4158  CD1 ILE B 879     4562   5025   4643   -328    -72    467       C  
-ATOM   4159  N   ALA B 880     -87.072  -2.991  -5.949  1.00 35.10           N  
-ANISOU 4159  N   ALA B 880     4338   4831   4167   -524   -209    460       N  
-ATOM   4160  CA  ALA B 880     -87.896  -3.984  -6.624  1.00 37.60           C  
-ANISOU 4160  CA  ALA B 880     4681   5186   4420   -598   -245    473       C  
-ATOM   4161  C   ALA B 880     -87.658  -3.962  -8.156  1.00 39.45           C  
-ANISOU 4161  C   ALA B 880     4948   5433   4609   -627   -244    474       C  
-ATOM   4162  O   ALA B 880     -87.575  -2.898  -8.783  1.00 39.56           O  
-ANISOU 4162  O   ALA B 880     4936   5467   4630   -599   -229    504       O  
-ATOM   4163  CB  ALA B 880     -89.344  -3.718  -6.316  1.00 37.32           C  
-ANISOU 4163  CB  ALA B 880     4584   5222   4372   -618   -272    531       C  
-ATOM   4164  N   PRO B 881     -87.524  -5.134  -8.764  1.00 39.37           N  
-ANISOU 4164  N   PRO B 881     5002   5409   4550   -683   -258    440       N  
-ATOM   4165  CA  PRO B 881     -87.250  -5.168 -10.201  1.00 42.90           C  
-ANISOU 4165  CA  PRO B 881     5488   5866   4944   -713   -252    434       C  
-ATOM   4166  C   PRO B 881     -88.399  -4.616 -11.069  1.00 45.86           C  
-ANISOU 4166  C   PRO B 881     5830   6325   5271   -749   -287    500       C  
-ATOM   4167  O   PRO B 881     -89.516  -4.459 -10.585  1.00 45.99           O  
-ANISOU 4167  O   PRO B 881     5792   6391   5291   -761   -320    548       O  
-ATOM   4168  CB  PRO B 881     -87.020  -6.645 -10.490  1.00 44.10           C  
-ANISOU 4168  CB  PRO B 881     5719   5984   5055   -768   -264    380       C  
-ATOM   4169  CG  PRO B 881     -87.615  -7.387  -9.352  1.00 44.42           C  
-ANISOU 4169  CG  PRO B 881     5751   6015   5111   -786   -292    381       C  
-ATOM   4170  CD  PRO B 881     -87.705  -6.462  -8.173  1.00 41.39           C  
-ANISOU 4170  CD  PRO B 881     5299   5638   4792   -725   -280    410       C  
-ATOM   4171  N   PRO B 882     -88.106  -4.266 -12.331  1.00 47.78           N  
-ANISOU 4171  N   PRO B 882     6100   6584   5470   -763   -278    507       N  
-ATOM   4172  CA  PRO B 882     -89.098  -3.727 -13.285  1.00 49.24           C  
-ANISOU 4172  CA  PRO B 882     6259   6847   5602   -797   -316    574       C  
-ATOM   4173  C   PRO B 882     -90.324  -4.637 -13.412  1.00 47.97           C  
-ANISOU 4173  C   PRO B 882     6097   6741   5387   -875   -377    592       C  
-ATOM   4174  O   PRO B 882     -91.442  -4.152 -13.495  1.00 44.93           O  
-ANISOU 4174  O   PRO B 882     5651   6425   4994   -887   -418    659       O  
-ATOM   4175  CB  PRO B 882     -88.328  -3.696 -14.609  1.00 50.30           C  
-ANISOU 4175  CB  PRO B 882     6457   6974   5682   -816   -292    552       C  
-ATOM   4176  CG  PRO B 882     -86.885  -3.622 -14.229  1.00 48.93           C  
-ANISOU 4176  CG  PRO B 882     6307   6722   5561   -762   -227    492       C  
-ATOM   4177  CD  PRO B 882     -86.730  -4.238 -12.867  1.00 48.92           C  
-ANISOU 4177  CD  PRO B 882     6295   6674   5619   -739   -226    455       C  
-ATOM   4178  N   GLU B 883     -90.100  -5.948 -13.353  1.00 50.66           N  
-ANISOU 4178  N   GLU B 883     6503   7045   5700   -925   -382    534       N  
-ATOM   4179  CA  GLU B 883     -91.160  -6.948 -13.483  1.00 51.75           C  
-ANISOU 4179  CA  GLU B 883     6653   7223   5785  -1011   -439    542       C  
-ATOM   4180  C   GLU B 883     -92.127  -6.967 -12.294  1.00 53.15           C  
-ANISOU 4180  C   GLU B 883     6758   7430   6007  -1010   -464    580       C  
-ATOM   4181  O   GLU B 883     -93.250  -7.457 -12.417  1.00 55.52           O  
-ANISOU 4181  O   GLU B 883     7037   7788   6271  -1079   -515    611       O  
-ATOM   4182  CB  GLU B 883     -90.565  -8.339 -13.627  1.00 56.09           C  
-ANISOU 4182  CB  GLU B 883     7299   7709   6304  -1058   -431    465       C  
-ATOM   4183  CG  GLU B 883     -89.636  -8.512 -14.824  1.00 60.39           C  
-ANISOU 4183  CG  GLU B 883     7922   8225   6798  -1067   -401    417       C  
-ATOM   4184  CD  GLU B 883     -88.200  -8.034 -14.569  1.00 66.16           C  
-ANISOU 4184  CD  GLU B 883     8664   8887   7586   -983   -331    375       C  
-ATOM   4185  OE1 GLU B 883     -87.504  -7.659 -15.549  1.00 74.29           O  
-ANISOU 4185  OE1 GLU B 883     9726   9915   8584   -974   -297    359       O  
-ATOM   4186  OE2 GLU B 883     -87.755  -7.998 -13.398  1.00 61.56           O  
-ANISOU 4186  OE2 GLU B 883     8055   8257   7079   -928   -309    360       O  
-ATOM   4187  N   ALA B 884     -91.714  -6.437 -11.145  1.00 46.40           N  
-ANISOU 4187  N   ALA B 884     5864   6540   5227   -936   -427    577       N  
-ATOM   4188  CA  ALA B 884     -92.580  -6.414  -9.968  1.00 46.56           C  
-ANISOU 4188  CA  ALA B 884     5818   6589   5285   -931   -441    610       C  
-ATOM   4189  C   ALA B 884     -93.688  -5.381 -10.075  1.00 45.23           C  
-ANISOU 4189  C   ALA B 884     5554   6506   5126   -915   -465    687       C  
-ATOM   4190  O   ALA B 884     -93.488  -4.327 -10.642  1.00 48.54           O  
-ANISOU 4190  O   ALA B 884     5949   6938   5555   -869   -453    715       O  
-ATOM   4191  CB  ALA B 884     -91.765  -6.128  -8.723  1.00 48.26           C  
-ANISOU 4191  CB  ALA B 884     6027   6740   5570   -857   -395    580       C  
-ATOM   4192  N   PRO B 885     -94.853  -5.661  -9.490  1.00 45.82           N  
-ANISOU 4192  N   PRO B 885     5569   6636   5202   -951   -494    723       N  
-ATOM   4193  CA  PRO B 885     -95.911  -4.651  -9.412  1.00 48.98           C  
-ANISOU 4193  CA  PRO B 885     5866   7117   5628   -922   -511    796       C  
-ATOM   4194  C   PRO B 885     -95.571  -3.545  -8.409  1.00 50.93           C  
-ANISOU 4194  C   PRO B 885     6064   7338   5951   -820   -461    802       C  
-ATOM   4195  O   PRO B 885     -94.793  -3.780  -7.502  1.00 53.51           O  
-ANISOU 4195  O   PRO B 885     6425   7599   6309   -790   -423    754       O  
-ATOM   4196  CB  PRO B 885     -97.123  -5.420  -8.900  1.00 47.31           C  
-ANISOU 4196  CB  PRO B 885     5609   6964   5402   -991   -546    821       C  
-ATOM   4197  CG  PRO B 885     -96.714  -6.830  -8.717  1.00 47.66           C  
-ANISOU 4197  CG  PRO B 885     5741   6955   5414  -1060   -551    764       C  
-ATOM   4198  CD  PRO B 885     -95.251  -6.966  -8.932  1.00 48.18           C  
-ANISOU 4198  CD  PRO B 885     5899   6927   5482  -1024   -514    700       C  
-ATOM   4199  N   VAL B 886     -96.203  -2.384  -8.546  1.00 48.98           N  
-ANISOU 4199  N   VAL B 886     5736   7142   5734   -770   -464    861       N  
-ATOM   4200  CA  VAL B 886     -96.055  -1.268  -7.600  1.00 51.35           C  
-ANISOU 4200  CA  VAL B 886     5984   7421   6106   -675   -419    869       C  
-ATOM   4201  C   VAL B 886     -96.898  -1.396  -6.309  1.00 52.28           C  
-ANISOU 4201  C   VAL B 886     6036   7572   6257   -668   -406    878       C  
-ATOM   4202  O   VAL B 886     -96.682  -0.681  -5.317  1.00 48.84           O  
-ANISOU 4202  O   VAL B 886     5573   7110   5876   -596   -362    867       O  
-ATOM   4203  CB  VAL B 886     -96.424   0.065  -8.309  1.00 53.48           C  
-ANISOU 4203  CB  VAL B 886     6197   7726   6399   -620   -427    931       C  
-ATOM   4204  CG1 VAL B 886     -97.916   0.134  -8.593  1.00 53.38           C  
-ANISOU 4204  CG1 VAL B 886     6095   7813   6374   -648   -476   1000       C  
-ATOM   4205  CG2 VAL B 886     -95.992   1.268  -7.483  1.00 52.30           C  
-ANISOU 4205  CG2 VAL B 886     6017   7530   6323   -520   -375    926       C  
-ATOM   4206  N   THR B 887     -97.901  -2.264  -6.363  1.00 54.21           N  
-ANISOU 4206  N   THR B 887     6253   7880   6465   -745   -445    901       N  
-ATOM   4207  CA  THR B 887     -98.911  -2.362  -5.318  1.00 56.50           C  
-ANISOU 4207  CA  THR B 887     6466   8223   6779   -749   -435    923       C  
-ATOM   4208  C   THR B 887     -98.279  -2.516  -3.924  1.00 53.67           C  
-ANISOU 4208  C   THR B 887     6138   7804   6450   -714   -382    874       C  
-ATOM   4209  O   THR B 887     -97.370  -3.320  -3.700  1.00 51.62           O  
-ANISOU 4209  O   THR B 887     5966   7476   6171   -740   -375    821       O  
-ATOM   4210  CB  THR B 887     -99.988  -3.453  -5.660  1.00 60.76           C  
-ANISOU 4210  CB  THR B 887     6983   8835   7269   -858   -488    951       C  
-ATOM   4211  OG1 THR B 887    -100.955  -2.912  -6.599  1.00 66.66           O  
-ANISOU 4211  OG1 THR B 887     7652   9667   8008   -866   -534   1017       O  
-ATOM   4212  CG2 THR B 887    -100.727  -3.855  -4.430  1.00 59.39           C  
-ANISOU 4212  CG2 THR B 887     6757   8695   7113   -876   -466    956       C  
-ATOM   4213  N   GLY B 888     -98.768  -1.709  -2.990  1.00 51.38           N  
-ANISOU 4213  N   GLY B 888     5775   7538   6207   -652   -345    891       N  
-ATOM   4214  CA  GLY B 888     -98.216  -1.664  -1.645  1.00 49.82           C  
-ANISOU 4214  CA  GLY B 888     5602   7290   6036   -611   -295    847       C  
-ATOM   4215  C   GLY B 888     -97.142  -0.604  -1.442  1.00 48.98           C  
-ANISOU 4215  C   GLY B 888     5524   7112   5973   -519   -257    815       C  
-ATOM   4216  O   GLY B 888     -96.925  -0.171  -0.327  1.00 47.80           O  
-ANISOU 4216  O   GLY B 888     5369   6939   5855   -469   -215    791       O  
-ATOM   4217  N   TYR B 889     -96.456  -0.198  -2.511  1.00 48.36           N  
-ANISOU 4217  N   TYR B 889     5480   7000   5895   -503   -272    815       N  
-ATOM   4218  CA  TYR B 889     -95.435   0.845  -2.404  1.00 45.73           C  
-ANISOU 4218  CA  TYR B 889     5171   6599   5606   -424   -237    789       C  
-ATOM   4219  C   TYR B 889     -96.053   2.226  -2.320  1.00 44.02           C  
-ANISOU 4219  C   TYR B 889     4876   6409   5440   -348   -217    829       C  
-ATOM   4220  O   TYR B 889     -96.354   2.825  -3.327  1.00 47.22           O  
-ANISOU 4220  O   TYR B 889     5254   6839   5850   -334   -239    874       O  
-ATOM   4221  CB  TYR B 889     -94.462   0.777  -3.580  1.00 44.24           C  
-ANISOU 4221  CB  TYR B 889     5046   6365   5397   -438   -254    775       C  
-ATOM   4222  CG  TYR B 889     -93.446  -0.325  -3.462  1.00 45.01           C  
-ANISOU 4222  CG  TYR B 889     5231   6405   5467   -480   -255    716       C  
-ATOM   4223  CD1 TYR B 889     -93.624  -1.545  -4.107  1.00 46.37           C  
-ANISOU 4223  CD1 TYR B 889     5442   6593   5583   -562   -292    712       C  
-ATOM   4224  CD2 TYR B 889     -92.297  -0.153  -2.689  1.00 45.94           C  
-ANISOU 4224  CD2 TYR B 889     5389   6448   5617   -438   -222    663       C  
-ATOM   4225  CE1 TYR B 889     -92.689  -2.562  -3.977  1.00 47.58           C  
-ANISOU 4225  CE1 TYR B 889     5676   6685   5717   -593   -291    658       C  
-ATOM   4226  CE2 TYR B 889     -91.335  -1.155  -2.581  1.00 45.28           C  
-ANISOU 4226  CE2 TYR B 889     5381   6310   5515   -468   -225    612       C  
-ATOM   4227  CZ  TYR B 889     -91.538  -2.363  -3.209  1.00 47.08           C  
-ANISOU 4227  CZ  TYR B 889     5648   6549   5691   -543   -258    609       C  
-ATOM   4228  OH  TYR B 889     -90.589  -3.360  -3.071  1.00 44.82           O  
-ANISOU 4228  OH  TYR B 889     5435   6201   5392   -565   -260    557       O  
-ATOM   4229  N   MET B 890     -96.114   2.758  -1.112  1.00 42.68           N  
-ANISOU 4229  N   MET B 890     4682   6227   5309   -294   -174    808       N  
-ATOM   4230  CA  MET B 890     -96.658   4.067  -0.853  1.00 43.50           C  
-ANISOU 4230  CA  MET B 890     4717   6344   5468   -213   -146    836       C  
-ATOM   4231  C   MET B 890     -96.017   5.194  -1.651  1.00 44.43           C  
-ANISOU 4231  C   MET B 890     4850   6411   5622   -157   -143    848       C  
-ATOM   4232  O   MET B 890     -96.723   6.106  -2.105  1.00 45.97           O  
-ANISOU 4232  O   MET B 890     4984   6636   5849   -110   -147    901       O  
-ATOM   4233  CB  MET B 890     -96.517   4.384   0.634  1.00 47.64           C  
-ANISOU 4233  CB  MET B 890     5239   6842   6019   -167    -93    792       C  
-ATOM   4234  CG  MET B 890     -97.213   5.664   1.044  1.00 50.67           C  
-ANISOU 4234  CG  MET B 890     5551   7242   6460    -83    -57    814       C  
-ATOM   4235  SD  MET B 890     -97.417   5.808   2.820  1.00 56.50           S  
-ANISOU 4235  SD  MET B 890     6277   7979   7211    -47      5    765       S  
-ATOM   4236  CE  MET B 890     -98.325   7.342   2.875  1.00 58.15           C  
-ANISOU 4236  CE  MET B 890     6396   8208   7490     55     42    800       C  
-ATOM   4237  N   PHE B 891     -94.692   5.152  -1.829  1.00 40.00           N  
-ANISOU 4237  N   PHE B 891     4366   5774   5058   -159   -136    804       N  
-ATOM   4238  CA  PHE B 891     -94.002   6.175  -2.617  1.00 37.53           C  
-ANISOU 4238  CA  PHE B 891     4073   5411   4776   -117   -130    816       C  
-ATOM   4239  C   PHE B 891     -93.245   5.598  -3.822  1.00 35.84           C  
-ANISOU 4239  C   PHE B 891     3920   5181   4519   -172   -159    815       C  
-ATOM   4240  O   PHE B 891     -92.250   6.135  -4.268  1.00 35.96           O  
-ANISOU 4240  O   PHE B 891     3976   5137   4550   -152   -144    800       O  
-ATOM   4241  CB  PHE B 891     -93.075   6.969  -1.714  1.00 35.88           C  
-ANISOU 4241  CB  PHE B 891     3893   5123   4618    -58    -84    764       C  
-ATOM   4242  CG  PHE B 891     -93.784   7.664  -0.598  1.00 38.86           C  
-ANISOU 4242  CG  PHE B 891     4218   5512   5036      1    -50    761       C  
-ATOM   4243  CD1 PHE B 891     -94.621   8.752  -0.855  1.00 39.12           C  
-ANISOU 4243  CD1 PHE B 891     4188   5564   5112     61    -42    812       C  
-ATOM   4244  CD2 PHE B 891     -93.646   7.226   0.710  1.00 40.20           C  
-ANISOU 4244  CD2 PHE B 891     4401   5673   5199     -2    -25    709       C  
-ATOM   4245  CE1 PHE B 891     -95.285   9.387   0.178  1.00 40.50           C  
-ANISOU 4245  CE1 PHE B 891     4314   5747   5325    121     -4    803       C  
-ATOM   4246  CE2 PHE B 891     -94.328   7.846   1.747  1.00 42.08           C  
-ANISOU 4246  CE2 PHE B 891     4594   5925   5467     51     13    701       C  
-ATOM   4247  CZ  PHE B 891     -95.129   8.940   1.484  1.00 42.00           C  
-ANISOU 4247  CZ  PHE B 891     4521   5932   5504    114     27    745       C  
-ATOM   4248  N   GLY B 892     -93.764   4.526  -4.385  1.00 36.36           N  
-ANISOU 4248  N   GLY B 892     3988   5300   4526   -242   -198    832       N  
-ATOM   4249  CA  GLY B 892     -93.134   3.892  -5.527  1.00 33.95           C  
-ANISOU 4249  CA  GLY B 892     3743   4985   4172   -298   -223    826       C  
-ATOM   4250  C   GLY B 892     -92.049   2.907  -5.151  1.00 32.87           C  
-ANISOU 4250  C   GLY B 892     3679   4794   4016   -332   -210    755       C  
-ATOM   4251  O   GLY B 892     -91.669   2.772  -3.987  1.00 33.96           O  
-ANISOU 4251  O   GLY B 892     3825   4897   4180   -310   -185    712       O  
-ATOM   4252  N   LYS B 893     -91.524   2.255  -6.176  1.00 34.33           N  
-ANISOU 4252  N   LYS B 893     3918   4972   4155   -382   -228    744       N  
-ATOM   4253  CA  LYS B 893     -90.437   1.323  -6.052  1.00 36.89           C  
-ANISOU 4253  CA  LYS B 893     4312   5242   4463   -410   -217    680       C  
-ATOM   4254  C   LYS B 893     -89.161   2.072  -5.739  1.00 36.34           C  
-ANISOU 4254  C   LYS B 893     4265   5100   4444   -355   -175    642       C  
-ATOM   4255  O   LYS B 893     -88.696   2.837  -6.556  1.00 37.65           O  
-ANISOU 4255  O   LYS B 893     4438   5250   4619   -337   -162    658       O  
-ATOM   4256  CB  LYS B 893     -90.212   0.582  -7.360  1.00 39.58           C  
-ANISOU 4256  CB  LYS B 893     4705   5593   4742   -471   -240    678       C  
-ATOM   4257  CG  LYS B 893     -91.307  -0.384  -7.751  1.00 44.54           C  
-ANISOU 4257  CG  LYS B 893     5327   6285   5311   -543   -287    703       C  
-ATOM   4258  CD  LYS B 893     -90.962  -0.966  -9.121  1.00 49.59           C  
-ANISOU 4258  CD  LYS B 893     6027   6929   5886   -599   -304    694       C  
-ATOM   4259  CE  LYS B 893     -92.060  -1.825  -9.702  1.00 48.75           C  
-ANISOU 4259  CE  LYS B 893     5918   6889   5716   -679   -358    722       C  
-ATOM   4260  NZ  LYS B 893     -91.518  -2.702 -10.786  1.00 51.12           N  
-ANISOU 4260  NZ  LYS B 893     6299   7173   5950   -739   -368    686       N  
-ATOM   4261  N   GLY B 894     -88.631   1.888  -4.533  1.00 33.37           N  
-ANISOU 4261  N   GLY B 894     3897   4681   4100   -331   -156    596       N  
-ATOM   4262  CA  GLY B 894     -87.423   2.569  -4.127  1.00 32.08           C  
-ANISOU 4262  CA  GLY B 894     3750   4452   3989   -284   -122    557       C  
-ATOM   4263  C   GLY B 894     -86.865   1.834  -2.937  1.00 30.66           C  
-ANISOU 4263  C   GLY B 894     3595   4235   3819   -283   -119    503       C  
-ATOM   4264  O   GLY B 894     -87.347   0.750  -2.592  1.00 29.17           O  
-ANISOU 4264  O   GLY B 894     3420   4068   3595   -323   -142    498       O  
-ATOM   4265  N   ILE B 895     -85.845   2.411  -2.316  1.00 26.84           N  
-ANISOU 4265  N   ILE B 895     3118   3696   3383   -241    -95    465       N  
-ATOM   4266  CA  ILE B 895     -85.318   1.860  -1.096  1.00 25.07           C  
-ANISOU 4266  CA  ILE B 895     2914   3440   3172   -233    -97    418       C  
-ATOM   4267  C   ILE B 895     -85.808   2.762  -0.004  1.00 23.12           C  
-ANISOU 4267  C   ILE B 895     2631   3199   2956   -191    -83    424       C  
-ATOM   4268  O   ILE B 895     -85.582   3.956  -0.044  1.00 22.93           O  
-ANISOU 4268  O   ILE B 895     2585   3154   2973   -150    -60    429       O  
-ATOM   4269  CB  ILE B 895     -83.774   1.820  -1.084  1.00 25.82           C  
-ANISOU 4269  CB  ILE B 895     3040   3470   3300   -218    -84    367       C  
-ATOM   4270  CG1 ILE B 895     -83.246   1.120  -2.315  1.00 25.19           C  
-ANISOU 4270  CG1 ILE B 895     2993   3383   3194   -252    -85    359       C  
-ATOM   4271  CG2 ILE B 895     -83.257   1.099   0.155  1.00 25.14           C  
-ANISOU 4271  CG2 ILE B 895     2977   3354   3220   -214    -98    324       C  
-ATOM   4272  CD1 ILE B 895     -81.758   1.344  -2.552  1.00 25.43           C  
-ANISOU 4272  CD1 ILE B 895     3037   3359   3265   -231    -62    317       C  
-ATOM   4273  N   TYR B 896     -86.402   2.142   1.017  1.00 23.49           N  
-ANISOU 4273  N   TYR B 896     2676   3268   2980   -203    -94    419       N  
-ATOM   4274  CA  TYR B 896     -87.073   2.807   2.103  1.00 23.64           C  
-ANISOU 4274  CA  TYR B 896     2662   3305   3013   -170    -77    424       C  
-ATOM   4275  C   TYR B 896     -86.243   2.758   3.395  1.00 22.45           C  
-ANISOU 4275  C   TYR B 896     2541   3111   2878   -150    -73    373       C  
-ATOM   4276  O   TYR B 896     -85.701   1.724   3.750  1.00 24.07           O  
-ANISOU 4276  O   TYR B 896     2785   3296   3062   -177    -94    348       O  
-ATOM   4277  CB  TYR B 896     -88.442   2.128   2.325  1.00 24.03           C  
-ANISOU 4277  CB  TYR B 896     2687   3423   3020   -205    -89    461       C  
-ATOM   4278  CG  TYR B 896     -89.505   2.440   1.289  1.00 25.25           C  
-ANISOU 4278  CG  TYR B 896     2795   3634   3165   -216    -95    518       C  
-ATOM   4279  CD1 TYR B 896     -89.381   2.013  -0.022  1.00 26.32           C  
-ANISOU 4279  CD1 TYR B 896     2947   3777   3278   -252   -117    537       C  
-ATOM   4280  CD2 TYR B 896     -90.641   3.162   1.623  1.00 26.40           C  
-ANISOU 4280  CD2 TYR B 896     2879   3828   3322   -187    -79    553       C  
-ATOM   4281  CE1 TYR B 896     -90.323   2.309  -0.969  1.00 26.58           C  
-ANISOU 4281  CE1 TYR B 896     2938   3863   3297   -264   -130    592       C  
-ATOM   4282  CE2 TYR B 896     -91.607   3.461   0.657  1.00 28.16           C  
-ANISOU 4282  CE2 TYR B 896     3054   4106   3541   -193    -91    611       C  
-ATOM   4283  CZ  TYR B 896     -91.438   3.036  -0.626  1.00 26.29           C  
-ANISOU 4283  CZ  TYR B 896     2836   3875   3277   -233   -121    631       C  
-ATOM   4284  OH  TYR B 896     -92.372   3.306  -1.585  1.00 26.00           O  
-ANISOU 4284  OH  TYR B 896     2754   3895   3230   -243   -141    690       O  
-ATOM   4285  N   PHE B 897     -86.203   3.870   4.118  1.00 22.81           N  
-ANISOU 4285  N   PHE B 897     2567   3140   2958   -103    -48    358       N  
-ATOM   4286  CA  PHE B 897     -85.467   4.029   5.388  1.00 21.84           C  
-ANISOU 4286  CA  PHE B 897     2470   2981   2849    -83    -45    308       C  
-ATOM   4287  C   PHE B 897     -86.289   4.811   6.392  1.00 23.03           C  
-ANISOU 4287  C   PHE B 897     2596   3155   3001    -50    -18    307       C  
-ATOM   4288  O   PHE B 897     -87.142   5.610   6.011  1.00 21.73           O  
-ANISOU 4288  O   PHE B 897     2388   3015   2853    -24      6    339       O  
-ATOM   4289  CB  PHE B 897     -84.175   4.836   5.194  1.00 22.64           C  
-ANISOU 4289  CB  PHE B 897     2583   3019   3002    -55    -39    273       C  
-ATOM   4290  CG  PHE B 897     -83.203   4.232   4.231  1.00 21.85           C  
-ANISOU 4290  CG  PHE B 897     2503   2891   2908    -79    -56    266       C  
-ATOM   4291  CD1 PHE B 897     -83.299   4.501   2.865  1.00 21.63           C  
-ANISOU 4291  CD1 PHE B 897     2460   2870   2887    -86    -46    298       C  
-ATOM   4292  CD2 PHE B 897     -82.190   3.443   4.683  1.00 21.93           C  
-ANISOU 4292  CD2 PHE B 897     2546   2869   2917    -91    -79    228       C  
-ATOM   4293  CE1 PHE B 897     -82.430   3.916   1.971  1.00 21.12           C  
-ANISOU 4293  CE1 PHE B 897     2417   2784   2824   -108    -54    287       C  
-ATOM   4294  CE2 PHE B 897     -81.273   2.889   3.796  1.00 22.75           C  
-ANISOU 4294  CE2 PHE B 897     2664   2947   3032   -106    -88    217       C  
-ATOM   4295  CZ  PHE B 897     -81.422   3.103   2.430  1.00 22.32           C  
-ANISOU 4295  CZ  PHE B 897     2598   2904   2980   -117    -72    245       C  
-ATOM   4296  N   ALA B 898     -86.012   4.583   7.678  1.00 24.41           N  
-ANISOU 4296  N   ALA B 898     2798   3319   3158    -48    -20    270       N  
-ATOM   4297  CA  ALA B 898     -86.646   5.299   8.764  1.00 24.09           C  
-ANISOU 4297  CA  ALA B 898     2744   3295   3113    -17     11    257       C  
-ATOM   4298  C   ALA B 898     -85.609   6.070   9.590  1.00 24.99           C  
-ANISOU 4298  C   ALA B 898     2888   3352   3254     12     14    199       C  
-ATOM   4299  O   ALA B 898     -84.442   5.690   9.623  1.00 23.72           O  
-ANISOU 4299  O   ALA B 898     2760   3150   3102     -2    -16    171       O  
-ATOM   4300  CB  ALA B 898     -87.326   4.299   9.657  1.00 25.97           C  
-ANISOU 4300  CB  ALA B 898     2996   3582   3291    -51      6    264       C  
-ATOM   4301  N   ASP B 899     -86.053   7.121  10.283  1.00 26.18           N  
-ANISOU 4301  N   ASP B 899     3027   3503   3419     52     51    180       N  
-ATOM   4302  CA  ASP B 899     -85.233   7.748  11.310  1.00 27.67           C  
-ANISOU 4302  CA  ASP B 899     3250   3646   3619     71     53    121       C  
-ATOM   4303  C   ASP B 899     -85.648   7.311  12.716  1.00 28.20           C  
-ANISOU 4303  C   ASP B 899     3344   3746   3625     61     59     98       C  
-ATOM   4304  O   ASP B 899     -84.997   7.680  13.705  1.00 27.51           O  
-ANISOU 4304  O   ASP B 899     3293   3628   3529     69     53     46       O  
-ATOM   4305  CB  ASP B 899     -85.209   9.279  11.202  1.00 27.87           C  
-ANISOU 4305  CB  ASP B 899     3259   3628   3700    121     88    101       C  
-ATOM   4306  CG  ASP B 899     -86.609   9.908  11.235  1.00 29.44           C  
-ANISOU 4306  CG  ASP B 899     3417   3868   3903    159    137    128       C  
-ATOM   4307  OD1 ASP B 899     -87.576   9.308  11.748  1.00 29.73           O  
-ANISOU 4307  OD1 ASP B 899     3438   3965   3891    148    150    145       O  
-ATOM   4308  OD2 ASP B 899     -86.726  11.035  10.759  1.00 31.76           O  
-ANISOU 4308  OD2 ASP B 899     3690   4128   4250    200    162    132       O  
-ATOM   4309  N   MET B 900     -86.671   6.462  12.802  1.00 31.34           N  
-ANISOU 4309  N   MET B 900     3727   4207   3975     36     65    136       N  
-ATOM   4310  CA  MET B 900     -87.065   5.811  14.087  1.00 31.86           C  
-ANISOU 4310  CA  MET B 900     3822   4310   3971     13     69    124       C  
-ATOM   4311  C   MET B 900     -86.698   4.341  14.037  1.00 30.07           C  
-ANISOU 4311  C   MET B 900     3628   4091   3704    -41     20    146       C  
-ATOM   4312  O   MET B 900     -87.216   3.597  13.201  1.00 31.67           O  
-ANISOU 4312  O   MET B 900     3809   4323   3903    -70     10    192       O  
-ATOM   4313  CB  MET B 900     -88.569   5.946  14.321  1.00 36.15           C  
-ANISOU 4313  CB  MET B 900     4322   4924   4492     22    121    153       C  
-ATOM   4314  CG  MET B 900     -89.116   7.372  14.333  1.00 37.35           C  
-ANISOU 4314  CG  MET B 900     4434   5069   4687     84    176    137       C  
-ATOM   4315  SD  MET B 900     -88.670   8.252  15.843  1.00 43.83           S  
-ANISOU 4315  SD  MET B 900     5306   5858   5489    116    204     58       S  
-ATOM   4316  CE  MET B 900     -89.850   7.592  17.015  1.00 47.08           C  
-ANISOU 4316  CE  MET B 900     5716   6354   5816     93    246     67       C  
-ATOM   4317  N   VAL B 901     -85.803   3.906  14.927  1.00 32.80           N  
-ANISOU 4317  N   VAL B 901     4030   4411   4023    -56    -15    113       N  
-ATOM   4318  CA  VAL B 901     -85.300   2.526  14.893  1.00 32.71           C  
-ANISOU 4318  CA  VAL B 901     4055   4391   3981   -100    -68    132       C  
-ATOM   4319  C   VAL B 901     -86.421   1.476  14.840  1.00 32.31           C  
-ANISOU 4319  C   VAL B 901     3999   4397   3881   -145    -60    183       C  
-ATOM   4320  O   VAL B 901     -86.320   0.495  14.136  1.00 32.14           O  
-ANISOU 4320  O   VAL B 901     3985   4369   3858   -178    -91    213       O  
-ATOM   4321  CB  VAL B 901     -84.317   2.234  16.057  1.00 33.39           C  
-ANISOU 4321  CB  VAL B 901     4202   4448   4037   -107   -108     95       C  
-ATOM   4322  CG1 VAL B 901     -85.002   2.266  17.416  1.00 34.59           C  
-ANISOU 4322  CG1 VAL B 901     4381   4643   4118   -116    -83     86       C  
-ATOM   4323  CG2 VAL B 901     -83.639   0.880  15.862  1.00 33.14           C  
-ANISOU 4323  CG2 VAL B 901     4206   4394   3993   -141   -167    115       C  
-ATOM   4324  N   SER B 902     -87.499   1.702  15.580  1.00 34.47           N  
-ANISOU 4324  N   SER B 902     4258   4727   4114   -147    -16    192       N  
-ATOM   4325  CA  SER B 902     -88.567   0.702  15.695  1.00 34.27           C  
-ANISOU 4325  CA  SER B 902     4226   4759   4037   -197     -7    240       C  
-ATOM   4326  C   SER B 902     -89.370   0.571  14.415  1.00 33.19           C  
-ANISOU 4326  C   SER B 902     4030   4652   3930   -209      3    284       C  
-ATOM   4327  O   SER B 902     -89.788  -0.548  14.062  1.00 34.18           O  
-ANISOU 4327  O   SER B 902     4161   4798   4028   -263    -18    324       O  
-ATOM   4328  CB  SER B 902     -89.484   1.014  16.877  1.00 35.47           C  
-ANISOU 4328  CB  SER B 902     4373   4967   4136   -197     45    234       C  
-ATOM   4329  OG  SER B 902     -90.090   2.296  16.744  1.00 38.34           O  
-ANISOU 4329  OG  SER B 902     4680   5351   4536   -144    102    218       O  
-ATOM   4330  N   LYS B 903     -89.551   1.674  13.687  1.00 31.16           N  
-ANISOU 4330  N   LYS B 903     3720   4393   3727   -162     30    279       N  
-ATOM   4331  CA  LYS B 903     -90.229   1.601  12.374  1.00 30.37           C  
-ANISOU 4331  CA  LYS B 903     3565   4319   3655   -173     30    324       C  
-ATOM   4332  C   LYS B 903     -89.513   0.638  11.442  1.00 29.51           C  
-ANISOU 4332  C   LYS B 903     3488   4174   3551   -210    -22    336       C  
-ATOM   4333  O   LYS B 903     -90.149  -0.186  10.776  1.00 30.32           O  
-ANISOU 4333  O   LYS B 903     3576   4308   3635   -257    -36    376       O  
-ATOM   4334  CB  LYS B 903     -90.340   2.960  11.716  1.00 29.86           C  
-ANISOU 4334  CB  LYS B 903     3450   4245   3650   -113     59    319       C  
-ATOM   4335  CG  LYS B 903     -91.109   2.919  10.400  1.00 28.90           C  
-ANISOU 4335  CG  LYS B 903     3271   4158   3550   -123     55    370       C  
-ATOM   4336  CD  LYS B 903     -91.627   4.294  10.016  1.00 31.17           C  
-ANISOU 4336  CD  LYS B 903     3500   4455   3890    -60     93    378       C  
-ATOM   4337  CE  LYS B 903     -92.496   4.241   8.755  1.00 32.57           C  
-ANISOU 4337  CE  LYS B 903     3617   4677   4082    -72     83    436       C  
-ATOM   4338  NZ  LYS B 903     -92.865   5.601   8.253  1.00 33.13           N  
-ANISOU 4338  NZ  LYS B 903     3635   4743   4209     -5    111    450       N  
-ATOM   4339  N   SER B 904     -88.191   0.693  11.452  1.00 29.13           N  
-ANISOU 4339  N   SER B 904     3483   4060   3525   -193    -51    299       N  
-ATOM   4340  CA  SER B 904     -87.398  -0.227  10.651  1.00 29.33           C  
-ANISOU 4340  CA  SER B 904     3541   4045   3558   -221    -95    302       C  
-ATOM   4341  C   SER B 904     -87.316  -1.601  11.293  1.00 28.67           C  
-ANISOU 4341  C   SER B 904     3513   3957   3424   -270   -128    311       C  
-ATOM   4342  O   SER B 904     -87.350  -2.618  10.585  1.00 27.58           O  
-ANISOU 4342  O   SER B 904     3392   3811   3276   -311   -155    333       O  
-ATOM   4343  CB  SER B 904     -85.983   0.330  10.385  1.00 28.78           C  
-ANISOU 4343  CB  SER B 904     3490   3908   3538   -183   -111    261       C  
-ATOM   4344  OG  SER B 904     -86.039   1.312   9.380  1.00 29.13           O  
-ANISOU 4344  OG  SER B 904     3491   3950   3629   -153    -89    266       O  
-ATOM   4345  N   ALA B 905     -87.133  -1.651  12.608  1.00 29.68           N  
-ANISOU 4345  N   ALA B 905     3674   4083   3520   -267   -129    293       N  
-ATOM   4346  CA  ALA B 905     -87.019  -2.943  13.317  1.00 30.72           C  
-ANISOU 4346  CA  ALA B 905     3865   4206   3601   -313   -163    307       C  
-ATOM   4347  C   ALA B 905     -88.260  -3.840  13.111  1.00 32.19           C  
-ANISOU 4347  C   ALA B 905     4041   4443   3745   -375   -154    357       C  
-ATOM   4348  O   ALA B 905     -88.150  -5.059  13.115  1.00 31.08           O  
-ANISOU 4348  O   ALA B 905     3948   4282   3579   -421   -189    377       O  
-ATOM   4349  CB  ALA B 905     -86.779  -2.717  14.792  1.00 30.07           C  
-ANISOU 4349  CB  ALA B 905     3818   4125   3481   -302   -161    284       C  
-ATOM   4350  N   ASN B 906     -89.428  -3.237  12.905  1.00 32.49           N  
-ANISOU 4350  N   ASN B 906     4017   4546   3783   -375   -110    379       N  
-ATOM   4351  CA  ASN B 906     -90.619  -4.019  12.622  1.00 34.59           C  
-ANISOU 4351  CA  ASN B 906     4260   4867   4015   -437   -103    427       C  
-ATOM   4352  C   ASN B 906     -90.474  -4.873  11.387  1.00 35.82           C  
-ANISOU 4352  C   ASN B 906     4428   4997   4184   -475   -141    445       C  
-ATOM   4353  O   ASN B 906     -91.081  -5.947  11.306  1.00 38.83           O  
-ANISOU 4353  O   ASN B 906     4827   5396   4531   -542   -157    479       O  
-ATOM   4354  CB  ASN B 906     -91.842  -3.125  12.468  1.00 35.72           C  
-ANISOU 4354  CB  ASN B 906     4319   5085   4168   -421    -51    447       C  
-ATOM   4355  CG  ASN B 906     -92.309  -2.547  13.783  1.00 35.11           C  
-ANISOU 4355  CG  ASN B 906     4232   5048   4062   -400     -4    435       C  
-ATOM   4356  OD1 ASN B 906     -91.957  -3.037  14.860  1.00 36.29           O  
-ANISOU 4356  OD1 ASN B 906     4440   5183   4166   -419    -11    424       O  
-ATOM   4357  ND2 ASN B 906     -93.076  -1.467  13.703  1.00 33.54           N  
-ANISOU 4357  ND2 ASN B 906     3960   4895   3887   -358     46    436       N  
-ATOM   4358  N   TYR B 907     -89.670  -4.416  10.427  1.00 32.71           N  
-ANISOU 4358  N   TYR B 907     4029   4561   3838   -437   -155    422       N  
-ATOM   4359  CA  TYR B 907     -89.465  -5.163   9.183  1.00 30.10           C  
-ANISOU 4359  CA  TYR B 907     3713   4205   3517   -470   -186    432       C  
-ATOM   4360  C   TYR B 907     -88.451  -6.279   9.324  1.00 30.53           C  
-ANISOU 4360  C   TYR B 907     3847   4188   3564   -488   -228    413       C  
-ATOM   4361  O   TYR B 907     -88.172  -6.984   8.372  1.00 32.79           O  
-ANISOU 4361  O   TYR B 907     4158   4444   3857   -513   -253    413       O  
-ATOM   4362  CB  TYR B 907     -89.087  -4.216   8.039  1.00 31.15           C  
-ANISOU 4362  CB  TYR B 907     3809   4329   3699   -426   -177    418       C  
-ATOM   4363  CG  TYR B 907     -90.238  -3.348   7.643  1.00 31.47           C  
-ANISOU 4363  CG  TYR B 907     3772   4438   3746   -417   -145    449       C  
-ATOM   4364  CD1 TYR B 907     -91.297  -3.867   6.899  1.00 32.01           C  
-ANISOU 4364  CD1 TYR B 907     3811   4560   3793   -472   -154    491       C  
-ATOM   4365  CD2 TYR B 907     -90.318  -2.021   8.078  1.00 31.58           C  
-ANISOU 4365  CD2 TYR B 907     3743   4466   3789   -356   -109    438       C  
-ATOM   4366  CE1 TYR B 907     -92.385  -3.077   6.571  1.00 33.22           C  
-ANISOU 4366  CE1 TYR B 907     3885   4781   3955   -460   -129    525       C  
-ATOM   4367  CE2 TYR B 907     -91.404  -1.222   7.752  1.00 31.64           C  
-ANISOU 4367  CE2 TYR B 907     3678   4535   3809   -340    -80    469       C  
-ATOM   4368  CZ  TYR B 907     -92.427  -1.747   7.007  1.00 33.43           C  
-ANISOU 4368  CZ  TYR B 907     3868   4817   4016   -389    -91    514       C  
-ATOM   4369  OH  TYR B 907     -93.492  -0.967   6.661  1.00 34.77           O  
-ANISOU 4369  OH  TYR B 907     3958   5049   4202   -370    -68    548       O  
-ATOM   4370  N   CYS B 908     -87.896  -6.468  10.515  1.00 34.04           N  
-ANISOU 4370  N   CYS B 908     4334   4605   3995   -475   -239    398       N  
-ATOM   4371  CA  CYS B 908     -87.075  -7.655  10.771  1.00 33.90           C  
-ANISOU 4371  CA  CYS B 908     4392   4522   3967   -494   -284    391       C  
-ATOM   4372  C   CYS B 908     -87.939  -8.918  10.860  1.00 35.58           C  
-ANISOU 4372  C   CYS B 908     4639   4748   4133   -572   -298    432       C  
-ATOM   4373  O   CYS B 908     -87.455 -10.015  10.577  1.00 33.41           O  
-ANISOU 4373  O   CYS B 908     4423   4416   3857   -597   -335    432       O  
-ATOM   4374  CB  CYS B 908     -86.273  -7.474  12.039  1.00 34.33           C  
-ANISOU 4374  CB  CYS B 908     4480   4548   4015   -459   -298    370       C  
-ATOM   4375  SG  CYS B 908     -85.055  -6.143  11.977  1.00 36.08           S  
-ANISOU 4375  SG  CYS B 908     4672   4740   4297   -377   -292    317       S  
-ATOM   4376  N   HIS B 909     -89.214  -8.735  11.231  1.00 36.61           N  
-ANISOU 4376  N   HIS B 909     4729   4953   4227   -609   -267    467       N  
-ATOM   4377  CA  HIS B 909     -90.178  -9.824  11.418  1.00 41.21           C  
-ANISOU 4377  CA  HIS B 909     5334   5560   4763   -692   -274    510       C  
-ATOM   4378  C   HIS B 909     -89.663 -10.832  12.421  1.00 38.71           C  
-ANISOU 4378  C   HIS B 909     5103   5191   4414   -715   -307    518       C  
-ATOM   4379  O   HIS B 909     -89.670 -12.021  12.179  1.00 36.33           O  
-ANISOU 4379  O   HIS B 909     4857   4848   4099   -768   -339    536       O  
-ATOM   4380  CB  HIS B 909     -90.601 -10.465  10.081  1.00 42.69           C  
-ANISOU 4380  CB  HIS B 909     5516   5745   4957   -742   -292    524       C  
-ATOM   4381  CG  HIS B 909     -91.439  -9.547   9.241  1.00 47.23           C  
-ANISOU 4381  CG  HIS B 909     6004   6392   5549   -735   -262    534       C  
-ATOM   4382  ND1 HIS B 909     -91.006  -9.017   8.035  1.00 49.37           N  
-ANISOU 4382  ND1 HIS B 909     6251   6649   5859   -701   -266    513       N  
-ATOM   4383  CD2 HIS B 909     -92.657  -9.005   9.473  1.00 48.20           C  
-ANISOU 4383  CD2 HIS B 909     6054   6603   5658   -752   -227    566       C  
-ATOM   4384  CE1 HIS B 909     -91.941  -8.215   7.551  1.00 49.90           C  
-ANISOU 4384  CE1 HIS B 909     6238   6789   5931   -698   -241    535       C  
-ATOM   4385  NE2 HIS B 909     -92.948  -8.183   8.408  1.00 51.50           N  
-ANISOU 4385  NE2 HIS B 909     6406   7055   6107   -726   -217    566       N  
-ATOM   4386  N   THR B 910     -89.169 -10.325  13.540  1.00 38.59           N  
-ANISOU 4386  N   THR B 910     5102   5173   4388   -673   -301    503       N  
-ATOM   4387  CA  THR B 910     -88.742 -11.194  14.608  1.00 38.55           C  
-ANISOU 4387  CA  THR B 910     5176   5126   4344   -694   -333    517       C  
-ATOM   4388  C   THR B 910     -89.960 -11.621  15.390  1.00 39.24           C  
-ANISOU 4388  C   THR B 910     5266   5275   4369   -765   -307    565       C  
-ATOM   4389  O   THR B 910     -91.035 -11.082  15.204  1.00 43.90           O  
-ANISOU 4389  O   THR B 910     5786   5943   4950   -784   -260    579       O  
-ATOM   4390  CB  THR B 910     -87.719 -10.515  15.521  1.00 34.65           C  
-ANISOU 4390  CB  THR B 910     4700   4609   3857   -627   -344    483       C  
-ATOM   4391  OG1 THR B 910     -88.205  -9.253  15.953  1.00 32.24           O  
-ANISOU 4391  OG1 THR B 910     4335   4371   3545   -597   -293    468       O  
-ATOM   4392  CG2 THR B 910     -86.430 -10.364  14.790  1.00 37.39           C  
-ANISOU 4392  CG2 THR B 910     5052   4887   4267   -569   -377    442       C  
-ATOM   4393  N   SER B 911     -89.786 -12.585  16.275  1.00 41.89           N  
-ANISOU 4393  N   SER B 911     5680   5577   4661   -803   -336    592       N  
-ATOM   4394  CA  SER B 911     -90.897 -13.093  17.107  1.00 45.44           C  
-ANISOU 4394  CA  SER B 911     6141   6082   5042   -879   -309    642       C  
-ATOM   4395  C   SER B 911     -90.337 -13.646  18.409  1.00 44.26           C  
-ANISOU 4395  C   SER B 911     6078   5895   4842   -886   -339    659       C  
-ATOM   4396  O   SER B 911     -89.113 -13.683  18.595  1.00 47.96           O  
-ANISOU 4396  O   SER B 911     6594   6295   5333   -831   -386    633       O  
-ATOM   4397  CB  SER B 911     -91.674 -14.160  16.347  1.00 42.92           C  
-ANISOU 4397  CB  SER B 911     5831   5758   4719   -965   -320    681       C  
-ATOM   4398  OG  SER B 911     -90.790 -15.201  15.957  1.00 44.59           O  
-ANISOU 4398  OG  SER B 911     6124   5867   4952   -970   -380    678       O  
-ATOM   4399  N   GLN B 912     -91.219 -14.030  19.328  1.00 49.27           N  
-ANISOU 4399  N   GLN B 912     6732   6580   5407   -951   -311    704       N  
-ATOM   4400  CA  GLN B 912     -90.782 -14.555  20.639  1.00 46.91           C  
-ANISOU 4400  CA  GLN B 912     6522   6256   5048   -965   -338    728       C  
-ATOM   4401  C   GLN B 912     -89.942 -15.811  20.426  1.00 45.07           C  
-ANISOU 4401  C   GLN B 912     6380   5913   4830   -979   -414    748       C  
-ATOM   4402  O   GLN B 912     -88.939 -16.020  21.112  1.00 46.62           O  
-ANISOU 4402  O   GLN B 912     6642   6053   5017   -941   -463    745       O  
-ATOM   4403  CB  GLN B 912     -91.966 -14.797  21.589  1.00 47.57           C  
-ANISOU 4403  CB  GLN B 912     6608   6416   5048  -1043   -287    778       C  
-ATOM   4404  N   GLY B 913     -90.318 -16.615  19.435  1.00 46.49           N  
-ANISOU 4404  N   GLY B 913     6562   6061   5040  -1028   -426    765       N  
-ATOM   4405  CA  GLY B 913     -89.585 -17.821  19.082  1.00 48.39           C  
-ANISOU 4405  CA  GLY B 913     6889   6192   5306  -1039   -492    778       C  
-ATOM   4406  C   GLY B 913     -88.270 -17.601  18.384  1.00 53.12           C  
-ANISOU 4406  C   GLY B 913     7488   6716   5977   -950   -534    725       C  
-ATOM   4407  O   GLY B 913     -87.399 -18.479  18.456  1.00 54.03           O  
-ANISOU 4407  O   GLY B 913     7680   6737   6110   -934   -593    732       O  
-ATOM   4408  N   ASP B 914     -88.132 -16.467  17.676  1.00 55.62           N  
-ANISOU 4408  N   ASP B 914     7720   7074   6340   -892   -504    675       N  
-ATOM   4409  CA  ASP B 914     -86.854 -16.036  17.076  1.00 59.50           C  
-ANISOU 4409  CA  ASP B 914     8199   7509   6899   -804   -533    621       C  
-ATOM   4410  C   ASP B 914     -86.640 -14.514  17.258  1.00 55.46           C  
-ANISOU 4410  C   ASP B 914     7611   7058   6402   -738   -497    578       C  
-ATOM   4411  O   ASP B 914     -86.940 -13.707  16.357  1.00 53.13           O  
-ANISOU 4411  O   ASP B 914     7241   6801   6143   -718   -460    550       O  
-ATOM   4412  CB  ASP B 914     -86.780 -16.424  15.589  1.00 67.08           C  
-ANISOU 4412  CB  ASP B 914     9145   8428   7915   -808   -537    599       C  
-ATOM   4413  CG  ASP B 914     -85.338 -16.377  15.038  1.00 75.05           C  
-ANISOU 4413  CG  ASP B 914    10164   9358   8992   -726   -574    551       C  
-ATOM   4414  OD1 ASP B 914     -85.089 -16.962  13.954  1.00 84.95           O  
-ANISOU 4414  OD1 ASP B 914    11432  10559  10285   -729   -586    534       O  
-ATOM   4415  OD2 ASP B 914     -84.447 -15.782  15.705  1.00 74.49           O  
-ANISOU 4415  OD2 ASP B 914    10088   9280   8934   -662   -591    530       O  
-ATOM   4416  N   PRO B 915     -86.124 -14.120  18.428  1.00 47.75           N  
-ANISOU 4416  N   PRO B 915     6658   6088   5396   -705   -511    574       N  
-ATOM   4417  CA  PRO B 915     -86.116 -12.731  18.853  1.00 48.03           C  
-ANISOU 4417  CA  PRO B 915     6635   6186   5429   -659   -473    539       C  
-ATOM   4418  C   PRO B 915     -84.831 -11.935  18.511  1.00 45.45           C  
-ANISOU 4418  C   PRO B 915     6280   5820   5168   -574   -497    482       C  
-ATOM   4419  O   PRO B 915     -84.647 -10.832  18.997  1.00 43.27           O  
-ANISOU 4419  O   PRO B 915     5971   5580   4889   -535   -476    450       O  
-ATOM   4420  CB  PRO B 915     -86.278 -12.873  20.370  1.00 48.17           C  
-ANISOU 4420  CB  PRO B 915     6707   6229   5367   -683   -479    567       C  
-ATOM   4421  CG  PRO B 915     -85.473 -14.099  20.694  1.00 46.96           C  
-ANISOU 4421  CG  PRO B 915     6643   5990   5209   -691   -553    596       C  
-ATOM   4422  CD  PRO B 915     -85.598 -15.005  19.482  1.00 49.02           C  
-ANISOU 4422  CD  PRO B 915     6910   6199   5518   -718   -566    607       C  
-ATOM   4423  N   ILE B 916     -83.948 -12.522  17.713  1.00 44.95           N  
-ANISOU 4423  N   ILE B 916     6234   5682   5162   -549   -539    469       N  
-ATOM   4424  CA  ILE B 916     -82.735 -11.874  17.289  1.00 42.75           C  
-ANISOU 4424  CA  ILE B 916     5925   5368   4951   -476   -559    418       C  
-ATOM   4425  C   ILE B 916     -82.901 -11.421  15.828  1.00 41.32           C  
-ANISOU 4425  C   ILE B 916     5680   5193   4826   -464   -521    392       C  
-ATOM   4426  O   ILE B 916     -83.175 -12.240  14.935  1.00 39.16           O  
-ANISOU 4426  O   ILE B 916     5421   4893   4566   -494   -524    406       O  
-ATOM   4427  CB  ILE B 916     -81.525 -12.821  17.393  1.00 44.53           C  
-ANISOU 4427  CB  ILE B 916     6206   5504   5207   -447   -629    419       C  
-ATOM   4428  CG1 ILE B 916     -81.444 -13.436  18.813  1.00 46.90           C  
-ANISOU 4428  CG1 ILE B 916     6581   5796   5445   -468   -674    458       C  
-ATOM   4429  CG2 ILE B 916     -80.270 -12.092  16.924  1.00 45.06           C  
-ANISOU 4429  CG2 ILE B 916     6228   5544   5350   -373   -644    365       C  
-ATOM   4430  CD1 ILE B 916     -81.172 -12.463  19.935  1.00 46.61           C  
-ANISOU 4430  CD1 ILE B 916     6534   5804   5373   -443   -677    441       C  
-ATOM   4431  N   GLY B 917     -82.727 -10.114  15.610  1.00 37.40           N  
-ANISOU 4431  N   GLY B 917     5119   4731   4359   -421   -489    355       N  
-ATOM   4432  CA  GLY B 917     -82.801  -9.533  14.286  1.00 37.61           C  
-ANISOU 4432  CA  GLY B 917     5087   4766   4437   -404   -455    332       C  
-ATOM   4433  C   GLY B 917     -81.561  -8.758  13.859  1.00 35.53           C  
-ANISOU 4433  C   GLY B 917     4790   4469   4240   -339   -463    284       C  
-ATOM   4434  O   GLY B 917     -80.683  -8.445  14.680  1.00 33.34           O  
-ANISOU 4434  O   GLY B 917     4523   4173   3972   -304   -493    263       O  
-ATOM   4435  N   LEU B 918     -81.513  -8.457  12.559  1.00 33.75           N  
-ANISOU 4435  N   LEU B 918     4524   4241   4059   -329   -438    268       N  
-ATOM   4436  CA  LEU B 918     -80.467  -7.653  11.965  1.00 32.13           C  
-ANISOU 4436  CA  LEU B 918     4278   4011   3917   -276   -433    225       C  
-ATOM   4437  C   LEU B 918     -81.044  -6.376  11.353  1.00 31.82           C  
-ANISOU 4437  C   LEU B 918     4176   4021   3892   -267   -380    218       C  
-ATOM   4438  O   LEU B 918     -82.080  -6.401  10.674  1.00 32.59           O  
-ANISOU 4438  O   LEU B 918     4256   4157   3971   -299   -350    243       O  
-ATOM   4439  CB  LEU B 918     -79.753  -8.446  10.896  1.00 32.59           C  
-ANISOU 4439  CB  LEU B 918     4350   4015   4017   -268   -447    212       C  
-ATOM   4440  CG  LEU B 918     -78.966  -9.686  11.343  1.00 31.25           C  
-ANISOU 4440  CG  LEU B 918     4239   3781   3853   -261   -502    214       C  
-ATOM   4441  CD1 LEU B 918     -78.398 -10.425  10.130  1.00 32.15           C  
-ANISOU 4441  CD1 LEU B 918     4363   3844   4009   -252   -502    196       C  
-ATOM   4442  CD2 LEU B 918     -77.865  -9.290  12.300  1.00 30.36           C  
-ANISOU 4442  CD2 LEU B 918     4122   3647   3766   -214   -538    193       C  
-ATOM   4443  N   ILE B 919     -80.359  -5.262  11.610  1.00 29.42           N  
-ANISOU 4443  N   ILE B 919     3840   3714   3624   -224   -372    185       N  
-ATOM   4444  CA  ILE B 919     -80.770  -3.969  11.106  1.00 27.58           C  
-ANISOU 4444  CA  ILE B 919     3552   3516   3412   -208   -324    177       C  
-ATOM   4445  C   ILE B 919     -79.544  -3.166  10.608  1.00 28.79           C  
-ANISOU 4445  C   ILE B 919     3675   3633   3633   -166   -323    137       C  
-ATOM   4446  O   ILE B 919     -78.449  -3.225  11.195  1.00 32.28           O  
-ANISOU 4446  O   ILE B 919     4128   4039   4099   -143   -358    110       O  
-ATOM   4447  CB  ILE B 919     -81.548  -3.217  12.195  1.00 27.66           C  
-ANISOU 4447  CB  ILE B 919     3555   3570   3384   -208   -303    181       C  
-ATOM   4448  CG1 ILE B 919     -82.245  -2.010  11.628  1.00 28.87           C  
-ANISOU 4448  CG1 ILE B 919     3653   3759   3556   -193   -252    183       C  
-ATOM   4449  CG2 ILE B 919     -80.618  -2.755  13.302  1.00 28.47           C  
-ANISOU 4449  CG2 ILE B 919     3674   3650   3494   -180   -329    146       C  
-ATOM   4450  CD1 ILE B 919     -83.329  -1.509  12.543  1.00 30.05           C  
-ANISOU 4450  CD1 ILE B 919     3795   3961   3662   -198   -221    194       C  
-ATOM   4451  N   LEU B 920     -79.725  -2.435   9.515  1.00 27.11           N  
-ANISOU 4451  N   LEU B 920     3421   3430   3449   -158   -285    137       N  
-ATOM   4452  CA  LEU B 920     -78.652  -1.640   8.918  1.00 25.73           C  
-ANISOU 4452  CA  LEU B 920     3214   3224   3337   -126   -275    106       C  
-ATOM   4453  C   LEU B 920     -78.716  -0.166   9.300  1.00 25.28           C  
-ANISOU 4453  C   LEU B 920     3126   3179   3302   -103   -249     90       C  
-ATOM   4454  O   LEU B 920     -79.800   0.389   9.499  1.00 25.81           O  
-ANISOU 4454  O   LEU B 920     3181   3284   3342   -107   -221    110       O  
-ATOM   4455  CB  LEU B 920     -78.734  -1.714   7.420  1.00 25.40           C  
-ANISOU 4455  CB  LEU B 920     3155   3183   3313   -135   -249    117       C  
-ATOM   4456  CG  LEU B 920     -78.500  -3.087   6.830  1.00 26.98           C  
-ANISOU 4456  CG  LEU B 920     3388   3361   3501   -155   -269    121       C  
-ATOM   4457  CD1 LEU B 920     -79.004  -3.144   5.414  1.00 27.86           C  
-ANISOU 4457  CD1 LEU B 920     3490   3491   3606   -177   -240    139       C  
-ATOM   4458  CD2 LEU B 920     -77.038  -3.425   6.871  1.00 28.40           C  
-ANISOU 4458  CD2 LEU B 920     3572   3490   3730   -127   -292     84       C  
-ATOM   4459  N   LEU B 921     -77.552   0.452   9.429  1.00 24.41           N  
-ANISOU 4459  N   LEU B 921     3000   3034   3242    -78   -258     54       N  
-ATOM   4460  CA  LEU B 921     -77.476   1.911   9.360  1.00 26.29           C  
-ANISOU 4460  CA  LEU B 921     3205   3269   3515    -59   -226     38       C  
-ATOM   4461  C   LEU B 921     -76.809   2.241   8.053  1.00 24.58           C  
-ANISOU 4461  C   LEU B 921     2959   3031   3351    -54   -204     35       C  
-ATOM   4462  O   LEU B 921     -75.702   1.796   7.796  1.00 23.66           O  
-ANISOU 4462  O   LEU B 921     2838   2885   3267    -50   -223     14       O  
-ATOM   4463  CB  LEU B 921     -76.684   2.495  10.511  1.00 27.10           C  
-ANISOU 4463  CB  LEU B 921     3314   3350   3635    -44   -251     -3       C  
-ATOM   4464  CG  LEU B 921     -77.444   2.573  11.833  1.00 27.69           C  
-ANISOU 4464  CG  LEU B 921     3417   3450   3653    -47   -258     -4       C  
-ATOM   4465  CD1 LEU B 921     -76.451   2.825  12.954  1.00 26.86           C  
-ANISOU 4465  CD1 LEU B 921     3328   3321   3556    -39   -300    -46       C  
-ATOM   4466  CD2 LEU B 921     -78.489   3.685  11.814  1.00 28.67           C  
-ANISOU 4466  CD2 LEU B 921     3524   3598   3771    -37   -207      3       C  
-ATOM   4467  N   GLY B 922     -77.520   2.984   7.221  1.00 23.55           N  
-ANISOU 4467  N   GLY B 922     2806   2917   3224    -54   -163     60       N  
-ATOM   4468  CA  GLY B 922     -76.994   3.426   5.948  1.00 22.98           C  
-ANISOU 4468  CA  GLY B 922     2710   2830   3194    -53   -136     63       C  
-ATOM   4469  C   GLY B 922     -76.804   4.945   5.898  1.00 23.09           C  
-ANISOU 4469  C   GLY B 922     2697   2824   3251    -36   -107     55       C  
-ATOM   4470  O   GLY B 922     -77.596   5.709   6.457  1.00 23.22           O  
-ANISOU 4470  O   GLY B 922     2713   2852   3258    -23    -94     62       O  
-ATOM   4471  N   GLU B 923     -75.724   5.387   5.265  1.00 22.00           N  
-ANISOU 4471  N   GLU B 923     2540   2655   3166    -35    -95     37       N  
-ATOM   4472  CA  GLU B 923     -75.584   6.814   4.932  1.00 22.60           C  
-ANISOU 4472  CA  GLU B 923     2594   2707   3285    -26    -62     39       C  
-ATOM   4473  C   GLU B 923     -76.373   6.973   3.638  1.00 21.85           C  
-ANISOU 4473  C   GLU B 923     2493   2635   3174    -33    -29     89       C  
-ATOM   4474  O   GLU B 923     -76.068   6.316   2.645  1.00 22.05           O  
-ANISOU 4474  O   GLU B 923     2519   2669   3191    -49    -22    100       O  
-ATOM   4475  CB  GLU B 923     -74.128   7.199   4.731  1.00 23.93           C  
-ANISOU 4475  CB  GLU B 923     2741   2837   3515    -31    -61      5       C  
-ATOM   4476  CG  GLU B 923     -73.944   8.690   4.476  1.00 25.94           C  
-ANISOU 4476  CG  GLU B 923     2980   3059   3817    -28    -29      6       C  
-ATOM   4477  CD  GLU B 923     -72.519   9.069   4.084  1.00 25.88           C  
-ANISOU 4477  CD  GLU B 923     2945   3018   3872    -42    -21    -21       C  
-ATOM   4478  OE1 GLU B 923     -71.586   8.431   4.629  1.00 26.08           O  
-ANISOU 4478  OE1 GLU B 923     2959   3037   3913    -45    -54    -57       O  
-ATOM   4479  OE2 GLU B 923     -72.351  10.000   3.234  1.00 26.08           O  
-ANISOU 4479  OE2 GLU B 923     2957   3022   3930    -51     17     -2       O  
-ATOM   4480  N   VAL B 924     -77.416   7.786   3.671  1.00 21.28           N  
-ANISOU 4480  N   VAL B 924     2417   2575   3092    -19    -11    118       N  
-ATOM   4481  CA  VAL B 924     -78.268   7.994   2.502  1.00 22.26           C  
-ANISOU 4481  CA  VAL B 924     2533   2725   3198    -23     13    172       C  
-ATOM   4482  C   VAL B 924     -78.112   9.433   2.006  1.00 22.87           C  
-ANISOU 4482  C   VAL B 924     2597   2768   3324     -9     44    188       C  
-ATOM   4483  O   VAL B 924     -78.266  10.391   2.769  1.00 25.63           O  
-ANISOU 4483  O   VAL B 924     2945   3091   3702     15     52    173       O  
-ATOM   4484  CB  VAL B 924     -79.740   7.731   2.858  1.00 22.88           C  
-ANISOU 4484  CB  VAL B 924     2611   2851   3230    -16      7    204       C  
-ATOM   4485  CG1 VAL B 924     -80.622   7.836   1.641  1.00 23.28           C  
-ANISOU 4485  CG1 VAL B 924     2650   2936   3259    -23     20    262       C  
-ATOM   4486  CG2 VAL B 924     -79.900   6.367   3.508  1.00 23.69           C  
-ANISOU 4486  CG2 VAL B 924     2734   2981   3288    -34    -25    189       C  
-ATOM   4487  N   ALA B 925     -77.798   9.596   0.738  1.00 24.03           N  
-ANISOU 4487  N   ALA B 925     2740   2913   3478    -25     64    216       N  
-ATOM   4488  CA  ALA B 925     -77.610  10.938   0.174  1.00 25.37           C  
-ANISOU 4488  CA  ALA B 925     2901   3045   3693    -17     94    239       C  
-ATOM   4489  C   ALA B 925     -78.966  11.460  -0.312  1.00 25.82           C  
-ANISOU 4489  C   ALA B 925     2954   3128   3729      2    102    300       C  
-ATOM   4490  O   ALA B 925     -79.398  11.173  -1.423  1.00 25.56           O  
-ANISOU 4490  O   ALA B 925     2921   3128   3663    -13    105    347       O  
-ATOM   4491  CB  ALA B 925     -76.619  10.896  -0.970  1.00 25.14           C  
-ANISOU 4491  CB  ALA B 925     2871   3004   3677    -46    116    245       C  
-ATOM   4492  N   LEU B 926     -79.639  12.221   0.543  1.00 26.72           N  
-ANISOU 4492  N   LEU B 926     3063   3228   3862     37    105    298       N  
-ATOM   4493  CA  LEU B 926     -81.022  12.589   0.274  1.00 28.08           C  
-ANISOU 4493  CA  LEU B 926     3221   3432   4017     64    108    353       C  
-ATOM   4494  C   LEU B 926     -81.147  13.816  -0.616  1.00 29.60           C  
-ANISOU 4494  C   LEU B 926     3410   3590   4246     80    131    402       C  
-ATOM   4495  O   LEU B 926     -82.163  13.993  -1.286  1.00 32.78           O  
-ANISOU 4495  O   LEU B 926     3799   4026   4631     94    128    463       O  
-ATOM   4496  CB  LEU B 926     -81.759  12.839   1.597  1.00 26.82           C  
-ANISOU 4496  CB  LEU B 926     3055   3275   3861    100    107    327       C  
-ATOM   4497  CG  LEU B 926     -81.831  11.641   2.522  1.00 26.56           C  
-ANISOU 4497  CG  LEU B 926     3029   3281   3784     84     84    290       C  
-ATOM   4498  CD1 LEU B 926     -82.267  12.086   3.890  1.00 27.56           C  
-ANISOU 4498  CD1 LEU B 926     3156   3398   3917    117     92    254       C  
-ATOM   4499  CD2 LEU B 926     -82.783  10.610   1.987  1.00 27.18           C  
-ANISOU 4499  CD2 LEU B 926     3094   3428   3805     65     68    332       C  
-ATOM   4500  N   GLY B 927     -80.164  14.708  -0.532  1.00 30.35           N  
-ANISOU 4500  N   GLY B 927     3518   3619   4396     79    150    378       N  
-ATOM   4501  CA  GLY B 927     -80.229  15.947  -1.247  1.00 32.10           C  
-ANISOU 4501  CA  GLY B 927     3743   3794   4657     94    172    424       C  
-ATOM   4502  C   GLY B 927     -81.520  16.693  -0.924  1.00 32.35           C  
-ANISOU 4502  C   GLY B 927     3763   3827   4703    149    175    459       C  
-ATOM   4503  O   GLY B 927     -81.907  16.800   0.224  1.00 33.68           O  
-ANISOU 4503  O   GLY B 927     3927   3989   4880    179    175    419       O  
-ATOM   4504  N   ASN B 928     -82.109  17.295  -1.936  1.00 33.03           N  
-ANISOU 4504  N   ASN B 928     3844   3912   4793    163    180    532       N  
-ATOM   4505  CA  ASN B 928     -83.378  18.019  -1.841  1.00 35.87           C  
-ANISOU 4505  CA  ASN B 928     4184   4274   5170    221    181    578       C  
-ATOM   4506  C   ASN B 928     -84.533  17.025  -1.861  1.00 32.46           C  
-ANISOU 4506  C   ASN B 928     3719   3934   4680    226    157    604       C  
-ATOM   4507  O   ASN B 928     -84.787  16.325  -2.844  1.00 31.72           O  
-ANISOU 4507  O   ASN B 928     3618   3897   4536    194    136    649       O  
-ATOM   4508  CB  ASN B 928     -83.469  18.990  -3.030  1.00 39.82           C  
-ANISOU 4508  CB  ASN B 928     4693   4739   5695    230    189    655       C  
-ATOM   4509  CG  ASN B 928     -84.507  20.059  -2.872  1.00 46.77           C  
-ANISOU 4509  CG  ASN B 928     5559   5590   6620    300    195    698       C  
-ATOM   4510  OD1 ASN B 928     -85.315  20.093  -1.919  1.00 45.58           O  
-ANISOU 4510  OD1 ASN B 928     5385   5454   6481    347    198    673       O  
-ATOM   4511  ND2 ASN B 928     -84.544  20.933  -3.886  1.00 48.83           N  
-ANISOU 4511  ND2 ASN B 928     5834   5814   6906    308    198    769       N  
-ATOM   4512  N   MET B 929     -85.210  16.968  -0.735  1.00 34.08           N  
-ANISOU 4512  N   MET B 929     3905   4154   4890    262    161    571       N  
-ATOM   4513  CA  MET B 929     -86.252  15.993  -0.489  1.00 34.03           C  
-ANISOU 4513  CA  MET B 929     3864   4233   4832    261    142    583       C  
-ATOM   4514  C   MET B 929     -87.600  16.507  -0.984  1.00 33.90           C  
-ANISOU 4514  C   MET B 929     3805   4251   4825    307    137    657       C  
-ATOM   4515  O   MET B 929     -87.951  17.646  -0.752  1.00 32.70           O  
-ANISOU 4515  O   MET B 929     3645   4052   4728    366    158    670       O  
-ATOM   4516  CB  MET B 929     -86.348  15.728   1.013  1.00 34.98           C  
-ANISOU 4516  CB  MET B 929     3983   4356   4951    277    154    513       C  
-ATOM   4517  CG  MET B 929     -85.095  15.100   1.602  1.00 33.42           C  
-ANISOU 4517  CG  MET B 929     3823   4135   4740    233    148    443       C  
-ATOM   4518  SD  MET B 929     -85.122  14.886   3.395  1.00 33.05           S  
-ANISOU 4518  SD  MET B 929     3786   4085   4685    249    158    363       S  
-ATOM   4519  CE  MET B 929     -85.460  16.544   3.946  1.00 36.85           C  
-ANISOU 4519  CE  MET B 929     4269   4497   5235    318    197    351       C  
-ATOM   4520  N   TYR B 930     -88.306  15.651  -1.702  1.00 34.49           N  
-ANISOU 4520  N   TYR B 930     3852   4406   4846    280    107    705       N  
-ATOM   4521  CA  TYR B 930     -89.640  15.893  -2.110  1.00 36.39           C  
-ANISOU 4521  CA  TYR B 930     4041   4699   5087    316     92    774       C  
-ATOM   4522  C   TYR B 930     -90.475  15.442  -0.924  1.00 37.99           C  
-ANISOU 4522  C   TYR B 930     4205   4948   5282    337    103    740       C  
-ATOM   4523  O   TYR B 930     -90.616  14.252  -0.672  1.00 35.43           O  
-ANISOU 4523  O   TYR B 930     3876   4683   4903    290     87    721       O  
-ATOM   4524  CB  TYR B 930     -89.928  15.070  -3.368  1.00 38.84           C  
-ANISOU 4524  CB  TYR B 930     4344   5078   5336    262     51    833       C  
-ATOM   4525  CG  TYR B 930     -91.248  15.315  -4.081  1.00 43.32           C  
-ANISOU 4525  CG  TYR B 930     4855   5705   5898    290     22    919       C  
-ATOM   4526  CD1 TYR B 930     -91.919  16.521  -4.002  1.00 50.79           C  
-ANISOU 4526  CD1 TYR B 930     5768   6622   6906    367     34    961       C  
-ATOM   4527  CD2 TYR B 930     -91.769  14.345  -4.914  1.00 49.24           C  
-ANISOU 4527  CD2 TYR B 930     5590   6538   6583    236    -20    960       C  
-ATOM   4528  CE1 TYR B 930     -93.103  16.740  -4.703  1.00 56.78           C  
-ANISOU 4528  CE1 TYR B 930     6471   7439   7665    394      2   1045       C  
-ATOM   4529  CE2 TYR B 930     -92.949  14.546  -5.614  1.00 54.43           C  
-ANISOU 4529  CE2 TYR B 930     6192   7255   7232    255    -55   1042       C  
-ATOM   4530  CZ  TYR B 930     -93.614  15.745  -5.507  1.00 55.87           C  
-ANISOU 4530  CZ  TYR B 930     6335   7413   7481    336    -45   1087       C  
-ATOM   4531  OH  TYR B 930     -94.801  15.920  -6.181  1.00 59.87           O  
-ANISOU 4531  OH  TYR B 930     6779   7985   7984    359    -85   1171       O  
-ATOM   4532  N   GLU B 931     -91.038  16.397  -0.205  1.00 39.84           N  
-ANISOU 4532  N   GLU B 931     4414   5153   5569    408    133    734       N  
-ATOM   4533  CA  GLU B 931     -91.762  16.098   1.023  1.00 42.30           C  
-ANISOU 4533  CA  GLU B 931     4694   5504   5875    432    156    694       C  
-ATOM   4534  C   GLU B 931     -93.231  15.808   0.729  1.00 43.25           C  
-ANISOU 4534  C   GLU B 931     4737   5715   5982    451    141    757       C  
-ATOM   4535  O   GLU B 931     -93.907  16.622   0.148  1.00 50.85           O  
-ANISOU 4535  O   GLU B 931     5660   6675   6984    503    137    818       O  
-ATOM   4536  CB  GLU B 931     -91.629  17.263   1.982  1.00 41.67           C  
-ANISOU 4536  CB  GLU B 931     4628   5348   5857    500    202    647       C  
-ATOM   4537  CG  GLU B 931     -90.182  17.647   2.195  1.00 44.06           C  
-ANISOU 4537  CG  GLU B 931     5002   5560   6178    477    212    590       C  
-ATOM   4538  CD  GLU B 931     -89.953  18.504   3.423  1.00 48.94           C  
-ANISOU 4538  CD  GLU B 931     5645   6110   6839    524    254    519       C  
-ATOM   4539  OE1 GLU B 931     -90.934  19.031   3.983  1.00 55.43           O  
-ANISOU 4539  OE1 GLU B 931     6432   6943   7688    588    284    520       O  
-ATOM   4540  OE2 GLU B 931     -88.783  18.634   3.830  1.00 53.03           O  
-ANISOU 4540  OE2 GLU B 931     6218   6568   7365    496    258    461       O  
-ATOM   4541  N   LEU B 932     -93.713  14.641   1.118  1.00 41.58           N  
-ANISOU 4541  N   LEU B 932     4501   5583   5715    406    129    747       N  
-ATOM   4542  CA  LEU B 932     -95.067  14.213   0.792  1.00 43.10           C  
-ANISOU 4542  CA  LEU B 932     4615   5870   5889    407    109    807       C  
-ATOM   4543  C   LEU B 932     -95.772  13.739   2.058  1.00 45.04           C  
-ANISOU 4543  C   LEU B 932     4825   6168   6121    413    142    768       C  
-ATOM   4544  O   LEU B 932     -95.140  13.148   2.951  1.00 41.76           O  
-ANISOU 4544  O   LEU B 932     4457   5738   5674    379    157    702       O  
-ATOM   4545  CB  LEU B 932     -95.047  13.075  -0.234  1.00 41.93           C  
-ANISOU 4545  CB  LEU B 932     4472   5781   5676    324     55    845       C  
-ATOM   4546  CG  LEU B 932     -94.466  13.464  -1.598  1.00 45.08           C  
-ANISOU 4546  CG  LEU B 932     4905   6147   6078    311     23    891       C  
-ATOM   4547  CD1 LEU B 932     -94.340  12.260  -2.512  1.00 42.44           C  
-ANISOU 4547  CD1 LEU B 932     4589   5865   5670    224    -24    912       C  
-ATOM   4548  CD2 LEU B 932     -95.323  14.541  -2.259  1.00 47.00           C  
-ANISOU 4548  CD2 LEU B 932     5094   6395   6368    377     14    968       C  
-ATOM   4549  N   LYS B 933     -97.075  14.011   2.125  1.00 45.87           N  
-ANISOU 4549  N   LYS B 933     4846   6336   6248    458    151    811       N  
-ATOM   4550  CA  LYS B 933     -97.901  13.634   3.273  1.00 47.52           C  
-ANISOU 4550  CA  LYS B 933     5006   6604   6444    467    190    783       C  
-ATOM   4551  C   LYS B 933     -98.766  12.417   2.947  1.00 49.53           C  
-ANISOU 4551  C   LYS B 933     5206   6968   6645    399    154    826       C  
-ATOM   4552  O   LYS B 933     -99.243  11.750   3.860  1.00 53.59           O  
-ANISOU 4552  O   LYS B 933     5698   7535   7128    374    179    800       O  
-ATOM   4553  CB  LYS B 933     -98.752  14.829   3.731  1.00 46.58           C  
-ANISOU 4553  CB  LYS B 933     4825   6477   6395    571    238    792       C  
-ATOM   4554  N   HIS B 934     -98.921  12.075   1.666  1.00 50.16           N  
-ANISOU 4554  N   HIS B 934     5272   7080   6707    359     95    890       N  
-ATOM   4555  CA  HIS B 934     -99.766  10.949   1.269  1.00 52.51           C  
-ANISOU 4555  CA  HIS B 934     5518   7479   6954    288     55    932       C  
-ATOM   4556  C   HIS B 934     -99.147  10.172   0.121  1.00 50.69           C  
-ANISOU 4556  C   HIS B 934     5341   7246   6671    208     -7    953       C  
-ATOM   4557  O   HIS B 934     -98.252  10.652  -0.531  1.00 51.29           O  
-ANISOU 4557  O   HIS B 934     5475   7255   6758    218    -18    952       O  
-ATOM   4558  CB  HIS B 934    -101.169  11.441   0.871  1.00 54.66           C  
-ANISOU 4558  CB  HIS B 934     5676   7828   7266    336     45   1005       C  
-ATOM   4559  CG  HIS B 934    -101.773  12.376   1.866  1.00 60.57           C  
-ANISOU 4559  CG  HIS B 934     6368   8570   8076    431    111    987       C  
-ATOM   4560  ND1 HIS B 934    -102.309  11.945   3.066  1.00 62.25           N  
-ANISOU 4560  ND1 HIS B 934     6547   8830   8274    425    162    947       N  
-ATOM   4561  CD2 HIS B 934    -101.882  13.725   1.865  1.00 61.49           C  
-ANISOU 4561  CD2 HIS B 934     6464   8632   8267    534    140    997       C  
-ATOM   4562  CE1 HIS B 934    -102.728  12.991   3.754  1.00 64.96           C  
-ANISOU 4562  CE1 HIS B 934     6850   9153   8680    523    221    930       C  
-ATOM   4563  NE2 HIS B 934    -102.484  14.081   3.047  1.00 64.40           N  
-ANISOU 4563  NE2 HIS B 934     6786   9017   8665    592    208    959       N  
-ATOM   4564  N   ALA B 935     -99.657   8.970  -0.108  1.00 50.69           N  
-ANISOU 4564  N   ALA B 935     5321   7321   6615    126    -42    971       N  
-ATOM   4565  CA  ALA B 935     -99.153   8.076  -1.127  1.00 55.04           C  
-ANISOU 4565  CA  ALA B 935     5927   7877   7109     43    -97    983       C  
-ATOM   4566  C   ALA B 935     -99.043   8.719  -2.503  1.00 60.44           C  
-ANISOU 4566  C   ALA B 935     6612   8549   7803     59   -138   1040       C  
-ATOM   4567  O   ALA B 935     -99.886   9.521  -2.910  1.00 66.22           O  
-ANISOU 4567  O   ALA B 935     7272   9315   8574    112   -149   1100       O  
-ATOM   4568  CB  ALA B 935    -100.051   6.852  -1.225  1.00 56.96           C  
-ANISOU 4568  CB  ALA B 935     6129   8214   7301    -40   -132   1007       C  
-ATOM   4569  N   SER B 936     -98.004   8.360  -3.243  1.00 69.17           N  
-ANISOU 4569  N   SER B 936     7801   9608   8872     13   -160   1022       N  
-ATOM   4570  CA  SER B 936     -97.957   8.767  -4.652  1.00 72.28           C  
-ANISOU 4570  CA  SER B 936     8203  10006   9255      9   -203   1081       C  
-ATOM   4571  C   SER B 936     -97.312   7.724  -5.539  1.00 74.25           C  
-ANISOU 4571  C   SER B 936     8523  10257   9431    -82   -241   1069       C  
-ATOM   4572  O   SER B 936     -97.892   7.375  -6.561  1.00 81.05           O  
-ANISOU 4572  O   SER B 936     9366  11180  10250   -127   -294   1121       O  
-ATOM   4573  CB  SER B 936     -97.273  10.117  -4.832  1.00 72.35           C  
-ANISOU 4573  CB  SER B 936     8238   9932   9320     85   -176   1087       C  
-ATOM   4574  OG  SER B 936     -97.544  10.634  -6.141  1.00 73.39           O  
-ANISOU 4574  OG  SER B 936     8358  10082   9445     90   -220   1163       O  
-ATOM   4575  N   SER B 939     -93.165   8.072 -10.494  1.00 88.69           N  
-ANISOU 4575  N   SER B 939    10667  11926  11107   -205   -277   1084       N  
-ATOM   4576  CA  SER B 939     -92.390   7.494 -11.598  1.00 85.64           C  
-ANISOU 4576  CA  SER B 939    10354  11536  10651   -269   -284   1070       C  
-ATOM   4577  C   SER B 939     -91.093   8.250 -11.899  1.00 80.19           C  
-ANISOU 4577  C   SER B 939     9717  10767   9986   -245   -236   1052       C  
-ATOM   4578  O   SER B 939     -90.114   7.642 -12.303  1.00 85.45           O  
-ANISOU 4578  O   SER B 939    10445  11408  10615   -288   -216   1004       O  
-ATOM   4579  CB  SER B 939     -93.255   7.387 -12.848  1.00 84.68           C  
-ANISOU 4579  CB  SER B 939    10222  11489  10462   -311   -344   1144       C  
-ATOM   4580  OG  SER B 939     -94.350   6.534 -12.582  1.00 87.28           O  
-ANISOU 4580  OG  SER B 939    10505  11893  10765   -348   -388   1152       O  
-ATOM   4581  N   LYS B 940     -91.086   9.565 -11.706  1.00 71.43           N  
-ANISOU 4581  N   LYS B 940     8582   9617   8942   -177   -217   1089       N  
-ATOM   4582  CA  LYS B 940     -89.883  10.355 -11.842  1.00 61.15           C  
-ANISOU 4582  CA  LYS B 940     7323   8235   7674   -155   -169   1072       C  
-ATOM   4583  C   LYS B 940     -89.954  11.478 -10.835  1.00 56.58           C  
-ANISOU 4583  C   LYS B 940     6707   7602   7189    -76   -141   1072       C  
-ATOM   4584  O   LYS B 940     -90.982  12.133 -10.718  1.00 57.08           O  
-ANISOU 4584  O   LYS B 940     6717   7688   7283    -29   -163   1130       O  
-ATOM   4585  CB  LYS B 940     -89.812  10.938 -13.260  1.00 59.41           C  
-ANISOU 4585  CB  LYS B 940     7134   8026   7413   -173   -185   1143       C  
-ATOM   4586  N   LEU B 941     -88.856  11.727 -10.133  1.00 49.39           N  
-ANISOU 4586  N   LEU B 941     5824   6617   6325    -60    -93   1009       N  
-ATOM   4587  CA  LEU B 941     -88.814  12.835  -9.207  1.00 45.16           C  
-ANISOU 4587  CA  LEU B 941     5264   6020   5875     10    -63   1002       C  
-ATOM   4588  C   LEU B 941     -88.882  14.177  -9.963  1.00 43.80           C  
-ANISOU 4588  C   LEU B 941     5095   5811   5735     47    -61   1076       C  
-ATOM   4589  O   LEU B 941     -88.436  14.268 -11.072  1.00 41.81           O  
-ANISOU 4589  O   LEU B 941     4882   5560   5445     11    -65   1111       O  
-ATOM   4590  CB  LEU B 941     -87.529  12.777  -8.369  1.00 44.84           C  
-ANISOU 4590  CB  LEU B 941     5256   5909   5872      9    -19    916       C  
-ATOM   4591  CG  LEU B 941     -87.454  11.665  -7.320  1.00 45.43           C  
-ANISOU 4591  CG  LEU B 941     5325   6002   5933     -9    -19    843       C  
-ATOM   4592  CD1 LEU B 941     -86.080  11.607  -6.694  1.00 45.82           C  
-ANISOU 4592  CD1 LEU B 941     5409   5986   6014    -15     17    767       C  
-ATOM   4593  CD2 LEU B 941     -88.502  11.905  -6.258  1.00 45.42           C  
-ANISOU 4593  CD2 LEU B 941     5273   6021   5966     40    -24    846       C  
-ATOM   4594  N   PRO B 942     -89.421  15.226  -9.341  1.00 42.27           N  
-ANISOU 4594  N   PRO B 942     4866   5582   5613    119    -52   1099       N  
-ATOM   4595  CA  PRO B 942     -89.268  16.560  -9.902  1.00 44.65           C  
-ANISOU 4595  CA  PRO B 942     5182   5823   5958    157    -42   1160       C  
-ATOM   4596  C   PRO B 942     -87.777  16.910 -10.080  1.00 45.40           C  
-ANISOU 4596  C   PRO B 942     5338   5841   6069    128      1   1121       C  
-ATOM   4597  O   PRO B 942     -86.972  16.513  -9.233  1.00 46.07           O  
-ANISOU 4597  O   PRO B 942     5436   5895   6172    115     31   1036       O  
-ATOM   4598  CB  PRO B 942     -89.921  17.466  -8.845  1.00 45.42           C  
-ANISOU 4598  CB  PRO B 942     5236   5881   6139    242    -27   1157       C  
-ATOM   4599  CG  PRO B 942     -90.870  16.585  -8.084  1.00 45.46           C  
-ANISOU 4599  CG  PRO B 942     5186   5961   6125    247    -45   1131       C  
-ATOM   4600  CD  PRO B 942     -90.264  15.208  -8.129  1.00 45.56           C  
-ANISOU 4600  CD  PRO B 942     5228   6014   6069    168    -50   1074       C  
-ATOM   4601  N   LYS B 943     -87.427  17.638 -11.150  1.00 42.14           N  
-ANISOU 4601  N   LYS B 943     4961   5400   5651    116      4   1184       N  
-ATOM   4602  CA  LYS B 943     -86.066  18.122 -11.365  1.00 42.26           C  
-ANISOU 4602  CA  LYS B 943     5027   5341   5689     89     49   1157       C  
-ATOM   4603  C   LYS B 943     -85.630  18.872 -10.130  1.00 39.99           C  
-ANISOU 4603  C   LYS B 943     4734   4969   5492    135     84   1100       C  
-ATOM   4604  O   LYS B 943     -86.375  19.690  -9.604  1.00 40.91           O  
-ANISOU 4604  O   LYS B 943     4824   5054   5665    201     79   1124       O  
-ATOM   4605  CB  LYS B 943     -85.963  19.101 -12.565  1.00 45.41           C  
-ANISOU 4605  CB  LYS B 943     5460   5710   6083     84     47   1250       C  
-ATOM   4606  CG  LYS B 943     -85.905  18.454 -13.934  1.00 48.51           C  
-ANISOU 4606  CG  LYS B 943     5883   6171   6377     19     27   1296       C  
-ATOM   4607  CD  LYS B 943     -84.504  17.948 -14.244  1.00 52.03           C  
-ANISOU 4607  CD  LYS B 943     6374   6601   6794    -48     73   1236       C  
-ATOM   4608  CE  LYS B 943     -84.308  17.286 -15.588  1.00 55.92           C  
-ANISOU 4608  CE  LYS B 943     6906   7157   7184   -116     66   1267       C  
-ATOM   4609  NZ  LYS B 943     -85.540  16.629 -16.067  1.00 55.71           N  
-ANISOU 4609  NZ  LYS B 943     6859   7220   7087   -121      4   1313       N  
-ATOM   4610  N   GLY B 944     -84.428  18.591  -9.661  1.00 38.16           N  
-ANISOU 4610  N   GLY B 944     4524   4699   5274    101    119   1022       N  
-ATOM   4611  CA  GLY B 944     -83.927  19.234  -8.471  1.00 36.47           C  
-ANISOU 4611  CA  GLY B 944     4310   4409   5139    135    148    960       C  
-ATOM   4612  C   GLY B 944     -84.199  18.489  -7.172  1.00 33.50           C  
-ANISOU 4612  C   GLY B 944     3904   4058   4766    153    143    883       C  
-ATOM   4613  O   GLY B 944     -83.681  18.904  -6.139  1.00 32.93           O  
-ANISOU 4613  O   GLY B 944     3836   3927   4748    172    165    821       O  
-ATOM   4614  N   LYS B 945     -85.018  17.437  -7.226  1.00 32.09           N  
-ANISOU 4614  N   LYS B 945     3699   3965   4528    143    111    890       N  
-ATOM   4615  CA  LYS B 945     -85.265  16.571  -6.076  1.00 31.57           C  
-ANISOU 4615  CA  LYS B 945     3611   3933   4453    149    105    823       C  
-ATOM   4616  C   LYS B 945     -84.556  15.245  -6.173  1.00 28.64           C  
-ANISOU 4616  C   LYS B 945     3255   3599   4026     87    100    773       C  
-ATOM   4617  O   LYS B 945     -84.464  14.695  -7.238  1.00 27.73           O  
-ANISOU 4617  O   LYS B 945     3156   3524   3858     45     88    804       O  
-ATOM   4618  CB  LYS B 945     -86.745  16.286  -5.939  1.00 32.13           C  
-ANISOU 4618  CB  LYS B 945     3634   4071   4501    180     76    863       C  
-ATOM   4619  CG  LYS B 945     -87.579  17.547  -5.804  1.00 33.56           C  
-ANISOU 4619  CG  LYS B 945     3790   4220   4742    253     80    914       C  
-ATOM   4620  CD  LYS B 945     -87.382  18.185  -4.447  1.00 32.85           C  
-ANISOU 4620  CD  LYS B 945     3700   4066   4717    300    113    849       C  
-ATOM   4621  CE  LYS B 945     -88.412  19.275  -4.224  1.00 34.22           C  
-ANISOU 4621  CE  LYS B 945     3840   4216   4946    381    119    894       C  
-ATOM   4622  NZ  LYS B 945     -88.202  19.900  -2.888  1.00 34.37           N  
-ANISOU 4622  NZ  LYS B 945     3867   4170   5023    425    156    822       N  
-ATOM   4623  N   HIS B 946     -83.996  14.763  -5.067  1.00 29.03           N  
-ANISOU 4623  N   HIS B 946     3307   3632   4090     84    110    695       N  
-ATOM   4624  CA  HIS B 946     -83.210  13.526  -5.103  1.00 29.94           C  
-ANISOU 4624  CA  HIS B 946     3441   3771   4164     33    105    645       C  
-ATOM   4625  C   HIS B 946     -83.757  12.392  -4.290  1.00 30.49           C  
-ANISOU 4625  C   HIS B 946     3497   3891   4199     27     83    610       C  
-ATOM   4626  O   HIS B 946     -83.237  11.275  -4.346  1.00 32.94           O  
-ANISOU 4626  O   HIS B 946     3823   4221   4472    -12     74    574       O  
-ATOM   4627  CB  HIS B 946     -81.814  13.846  -4.652  1.00 30.05           C  
-ANISOU 4627  CB  HIS B 946     3474   3719   4224     24    133    585       C  
-ATOM   4628  CG  HIS B 946     -81.298  15.055  -5.332  1.00 33.91           C  
-ANISOU 4628  CG  HIS B 946     3978   4152   4756     27    158    619       C  
-ATOM   4629  ND1 HIS B 946     -81.303  16.295  -4.739  1.00 36.88           N  
-ANISOU 4629  ND1 HIS B 946     4353   4463   5198     66    174    618       N  
-ATOM   4630  CD2 HIS B 946     -80.885  15.242  -6.598  1.00 34.79           C  
-ANISOU 4630  CD2 HIS B 946     4108   4264   4848     -6    171    663       C  
-ATOM   4631  CE1 HIS B 946     -80.846  17.189  -5.592  1.00 38.44           C  
-ANISOU 4631  CE1 HIS B 946     4568   4617   5420     56    195    660       C  
-ATOM   4632  NE2 HIS B 946     -80.585  16.574  -6.728  1.00 40.58           N  
-ANISOU 4632  NE2 HIS B 946     4851   4931   5639     12    194    689       N  
-ATOM   4633  N   SER B 947     -84.763  12.695  -3.500  1.00 29.23           N  
-ANISOU 4633  N   SER B 947     3307   3746   4053     68     77    619       N  
-ATOM   4634  CA  SER B 947     -85.354  11.705  -2.648  1.00 30.65           C  
-ANISOU 4634  CA  SER B 947     3472   3973   4200     61     59    591       C  
-ATOM   4635  C   SER B 947     -86.763  12.135  -2.253  1.00 30.45           C  
-ANISOU 4635  C   SER B 947     3403   3985   4183    104     55    630       C  
-ATOM   4636  O   SER B 947     -87.165  13.273  -2.473  1.00 33.48           O  
-ANISOU 4636  O   SER B 947     3769   4344   4607    149     67    669       O  
-ATOM   4637  CB  SER B 947     -84.495  11.534  -1.392  1.00 29.76           C  
-ANISOU 4637  CB  SER B 947     3378   3819   4112     65     71    513       C  
-ATOM   4638  OG  SER B 947     -84.440  12.738  -0.661  1.00 27.15           O  
-ANISOU 4638  OG  SER B 947     3042   3435   3839    113     95    497       O  
-ATOM   4639  N   VAL B 948     -87.504  11.203  -1.693  1.00 32.19           N  
-ANISOU 4639  N   VAL B 948     3603   4262   4364     90     39    621       N  
-ATOM   4640  CA  VAL B 948     -88.782  11.512  -1.089  1.00 32.48           C  
-ANISOU 4640  CA  VAL B 948     3592   4339   4412    130     43    645       C  
-ATOM   4641  C   VAL B 948     -88.638  11.378   0.416  1.00 31.38           C  
-ANISOU 4641  C   VAL B 948     3457   4183   4282    147     63    581       C  
-ATOM   4642  O   VAL B 948     -87.981  10.456   0.920  1.00 29.75           O  
-ANISOU 4642  O   VAL B 948     3283   3974   4046    109     55    533       O  
-ATOM   4643  CB  VAL B 948     -89.899  10.575  -1.597  1.00 35.03           C  
-ANISOU 4643  CB  VAL B 948     3879   4751   4679     96     10    692       C  
-ATOM   4644  CG1 VAL B 948     -91.144  10.682  -0.717  1.00 34.40           C  
-ANISOU 4644  CG1 VAL B 948     3742   4719   4608    131     19    703       C  
-ATOM   4645  CG2 VAL B 948     -90.263  10.906  -3.036  1.00 34.64           C  
-ANISOU 4645  CG2 VAL B 948     3818   4725   4619     88    -14    765       C  
-ATOM   4646  N   LYS B 949     -89.241  12.322   1.125  1.00 31.22           N  
-ANISOU 4646  N   LYS B 949     3410   4149   4302    206     90    579       N  
-ATOM   4647  CA  LYS B 949     -89.457  12.197   2.566  1.00 32.35           C  
-ANISOU 4647  CA  LYS B 949     3552   4297   4444    224    112    527       C  
-ATOM   4648  C   LYS B 949     -90.961  12.148   2.825  1.00 33.83           C  
-ANISOU 4648  C   LYS B 949     3677   4557   4622    250    120    565       C  
-ATOM   4649  O   LYS B 949     -91.670  13.095   2.520  1.00 30.52           O  
-ANISOU 4649  O   LYS B 949     3217   4136   4243    304    134    604       O  
-ATOM   4650  CB  LYS B 949     -88.888  13.367   3.309  1.00 32.40           C  
-ANISOU 4650  CB  LYS B 949     3580   4225   4504    273    146    481       C  
-ATOM   4651  CG  LYS B 949     -89.127  13.277   4.798  1.00 34.14           C  
-ANISOU 4651  CG  LYS B 949     3804   4453   4713    291    170    424       C  
-ATOM   4652  CD  LYS B 949     -88.534  14.462   5.522  1.00 36.91           C  
-ANISOU 4652  CD  LYS B 949     4186   4723   5116    335    201    372       C  
-ATOM   4653  CE  LYS B 949     -88.778  14.347   7.007  1.00 40.33           C  
-ANISOU 4653  CE  LYS B 949     4629   5168   5527    348    226    313       C  
-ATOM   4654  NZ  LYS B 949     -88.374  15.593   7.706  1.00 43.90           N  
-ANISOU 4654  NZ  LYS B 949     5110   5543   6027    395    259    261       N  
-ATOM   4655  N   GLY B 950     -91.426  11.017   3.342  1.00 34.29           N  
-ANISOU 4655  N   GLY B 950     3725   4677   4628    210    110    556       N  
-ATOM   4656  CA  GLY B 950     -92.783  10.904   3.819  1.00 36.93           C  
-ANISOU 4656  CA  GLY B 950     3997   5082   4953    228    125    581       C  
-ATOM   4657  C   GLY B 950     -92.843  11.532   5.192  1.00 38.43           C  
-ANISOU 4657  C   GLY B 950     4192   5247   5164    277    173    527       C  
-ATOM   4658  O   GLY B 950     -92.090  11.132   6.076  1.00 38.14           O  
-ANISOU 4658  O   GLY B 950     4205   5183   5103    254    178    468       O  
-ATOM   4659  N   LEU B 951     -93.712  12.526   5.365  1.00 38.33           N  
-ANISOU 4659  N   LEU B 951     4128   5240   5195    346    207    545       N  
-ATOM   4660  CA  LEU B 951     -93.715  13.345   6.585  1.00 40.43           C  
-ANISOU 4660  CA  LEU B 951     4405   5468   5488    403    260    488       C  
-ATOM   4661  C   LEU B 951     -94.529  12.726   7.701  1.00 42.59           C  
-ANISOU 4661  C   LEU B 951     4652   5811   5719    394    290    466       C  
-ATOM   4662  O   LEU B 951     -95.736  12.579   7.561  1.00 45.89           O  
-ANISOU 4662  O   LEU B 951     4997   6303   6137    407    300    512       O  
-ATOM   4663  CB  LEU B 951     -94.286  14.720   6.285  1.00 41.46           C  
-ANISOU 4663  CB  LEU B 951     4496   5566   5690    488    289    514       C  
-ATOM   4664  CG  LEU B 951     -93.475  15.527   5.269  1.00 43.40           C  
-ANISOU 4664  CG  LEU B 951     4775   5732   5983    502    267    536       C  
-ATOM   4665  CD1 LEU B 951     -94.126  16.880   5.013  1.00 42.00           C  
-ANISOU 4665  CD1 LEU B 951     4560   5518   5879    591    295    568       C  
-ATOM   4666  CD2 LEU B 951     -92.048  15.716   5.765  1.00 43.69           C  
-ANISOU 4666  CD2 LEU B 951     4893   5685   6022    480    270    465       C  
-ATOM   4667  N   GLY B 952     -93.871  12.327   8.786  1.00 41.62           N  
-ANISOU 4667  N   GLY B 952     4586   5668   5558    367    301    401       N  
-ATOM   4668  CA  GLY B 952     -94.584  11.759   9.950  1.00 42.36           C  
-ANISOU 4668  CA  GLY B 952     4665   5826   5603    355    335    378       C  
-ATOM   4669  C   GLY B 952     -95.146  12.804  10.896  1.00 40.30           C  
-ANISOU 4669  C   GLY B 952     4386   5556   5372    430    402    340       C  
-ATOM   4670  O   GLY B 952     -94.729  13.956  10.847  1.00 42.04           O  
-ANISOU 4670  O   GLY B 952     4626   5700   5646    487    420    314       O  
-ATOM   4671  N   LYS B 953     -96.079  12.392  11.757  1.00 39.14           N  
-ANISOU 4671  N   LYS B 953     4204   5483   5187    427    443    334       N  
-ATOM   4672  CA  LYS B 953     -96.576  13.245  12.869  1.00 41.55           C  
-ANISOU 4672  CA  LYS B 953     4500   5784   5503    492    517    283       C  
-ATOM   4673  C   LYS B 953     -95.527  13.415  13.976  1.00 40.36           C  
-ANISOU 4673  C   LYS B 953     4446   5572   5319    482    529    198       C  
-ATOM   4674  O   LYS B 953     -95.521  14.401  14.696  1.00 36.19           O  
-ANISOU 4674  O   LYS B 953     3937   5001   4813    540    579    143       O  
-ATOM   4675  CB  LYS B 953     -97.893  12.709  13.461  1.00 42.28           C  
-ANISOU 4675  CB  LYS B 953     4523   5983   5560    486    563    304       C  
-ATOM   4676  N   THR B 954     -94.636  12.438  14.097  1.00 39.51           N  
-ANISOU 4676  N   THR B 954     4398   5458   5158    407    478    188       N  
-ATOM   4677  CA  THR B 954     -93.559  12.475  15.082  1.00 40.93           C  
-ANISOU 4677  CA  THR B 954     4666   5584   5301    388    472    114       C  
-ATOM   4678  C   THR B 954     -92.222  12.428  14.320  1.00 41.29           C  
-ANISOU 4678  C   THR B 954     4760   5556   5374    360    407    113       C  
-ATOM   4679  O   THR B 954     -92.067  11.671  13.356  1.00 40.33           O  
-ANISOU 4679  O   THR B 954     4621   5450   5251    319    360    164       O  
-ATOM   4680  CB  THR B 954     -93.696  11.279  16.038  1.00 41.25           C  
-ANISOU 4680  CB  THR B 954     4734   5688   5251    324    470    105       C  
-ATOM   4681  OG1 THR B 954     -94.963  11.360  16.704  1.00 42.41           O  
-ANISOU 4681  OG1 THR B 954     4831   5908   5375    349    539    108       O  
-ATOM   4682  CG2 THR B 954     -92.567  11.211  17.053  1.00 42.58           C  
-ANISOU 4682  CG2 THR B 954     4995   5807   5375    300    452     36       C  
-ATOM   4683  N   THR B 955     -91.277  13.231  14.775  1.00 41.89           N  
-ANISOU 4683  N   THR B 955     4893   5553   5471    380    409     51       N  
-ATOM   4684  CA  THR B 955     -89.955  13.312  14.195  1.00 42.19           C  
-ANISOU 4684  CA  THR B 955     4973   5519   5537    356    356     40       C  
-ATOM   4685  C   THR B 955     -88.920  13.345  15.312  1.00 41.53           C  
-ANISOU 4685  C   THR B 955     4965   5394   5420    334    342    -35       C  
-ATOM   4686  O   THR B 955     -89.224  13.838  16.384  1.00 44.68           O  
-ANISOU 4686  O   THR B 955     5387   5794   5796    359    384    -86       O  
-ATOM   4687  CB  THR B 955     -89.833  14.576  13.309  1.00 42.24           C  
-ANISOU 4687  CB  THR B 955     4961   5458   5631    410    368     52       C  
-ATOM   4688  OG1 THR B 955     -88.594  14.537  12.605  1.00 43.86           O  
-ANISOU 4688  OG1 THR B 955     5197   5605   5862    377    318     52       O  
-ATOM   4689  CG2 THR B 955     -89.911  15.869  14.122  1.00 41.31           C  
-ANISOU 4689  CG2 THR B 955     4867   5284   5544    470    419    -10       C  
-ATOM   4690  N   PRO B 956     -87.695  12.835  15.076  1.00 43.50           N  
-ANISOU 4690  N   PRO B 956     5253   5609   5667    288    283    -44       N  
-ATOM   4691  CA  PRO B 956     -86.638  13.046  16.073  1.00 46.50           C  
-ANISOU 4691  CA  PRO B 956     5699   5943   6026    272    263   -115       C  
-ATOM   4692  C   PRO B 956     -86.363  14.518  16.289  1.00 44.35           C  
-ANISOU 4692  C   PRO B 956     5446   5597   5809    318    294   -167       C  
-ATOM   4693  O   PRO B 956     -86.354  15.288  15.340  1.00 47.20           O  
-ANISOU 4693  O   PRO B 956     5779   5913   6240    347    304   -143       O  
-ATOM   4694  CB  PRO B 956     -85.413  12.355  15.449  1.00 47.94           C  
-ANISOU 4694  CB  PRO B 956     5896   6098   6219    224    196   -103       C  
-ATOM   4695  CG  PRO B 956     -86.014  11.328  14.556  1.00 49.67           C  
-ANISOU 4695  CG  PRO B 956     6075   6374   6425    202    183    -31       C  
-ATOM   4696  CD  PRO B 956     -87.182  12.051  13.943  1.00 48.84           C  
-ANISOU 4696  CD  PRO B 956     5914   6287   6356    249    232      6       C  
-ATOM   4697  N   ASP B 957     -86.172  14.893  17.541  1.00 45.24           N  
-ANISOU 4697  N   ASP B 957     5609   5696   5885    321    310   -237       N  
-ATOM   4698  CA  ASP B 957     -85.958  16.272  17.923  1.00 44.36           C  
-ANISOU 4698  CA  ASP B 957     5527   5511   5817    361    343   -298       C  
-ATOM   4699  C   ASP B 957     -84.749  16.836  17.186  1.00 42.82           C  
-ANISOU 4699  C   ASP B 957     5344   5233   5691    347    302   -305       C  
-ATOM   4700  O   ASP B 957     -83.625  16.456  17.465  1.00 37.73           O  
-ANISOU 4700  O   ASP B 957     4734   4571   5032    300    249   -332       O  
-ATOM   4701  CB  ASP B 957     -85.739  16.340  19.436  1.00 45.53           C  
-ANISOU 4701  CB  ASP B 957     5740   5664   5896    348    351   -376       C  
-ATOM   4702  CG  ASP B 957     -85.673  17.757  19.969  1.00 47.78           C  
-ANISOU 4702  CG  ASP B 957     6062   5876   6215    390    394   -449       C  
-ATOM   4703  OD1 ASP B 957     -85.487  18.716  19.173  1.00 50.58           O  
-ANISOU 4703  OD1 ASP B 957     6403   6160   6657    422    404   -443       O  
-ATOM   4704  OD2 ASP B 957     -85.768  17.895  21.210  1.00 46.13           O  
-ANISOU 4704  OD2 ASP B 957     5905   5679   5944    388    416   -515       O  
-ATOM   4705  N   PRO B 958     -84.980  17.793  16.272  1.00 47.38           N  
-ANISOU 4705  N   PRO B 958     5894   5761   6348    389    329   -280       N  
-ATOM   4706  CA  PRO B 958     -83.883  18.416  15.509  1.00 46.52           C  
-ANISOU 4706  CA  PRO B 958     5795   5572   6309    373    299   -281       C  
-ATOM   4707  C   PRO B 958     -82.766  19.027  16.343  1.00 43.31           C  
-ANISOU 4707  C   PRO B 958     5450   5099   5909    347    277   -363       C  
-ATOM   4708  O   PRO B 958     -81.633  19.079  15.882  1.00 42.71           O  
-ANISOU 4708  O   PRO B 958     5379   4980   5869    309    235   -366       O  
-ATOM   4709  CB  PRO B 958     -84.584  19.526  14.718  1.00 48.36           C  
-ANISOU 4709  CB  PRO B 958     6000   5759   6616    433    345   -249       C  
-ATOM   4710  CG  PRO B 958     -86.019  19.154  14.694  1.00 46.93           C  
-ANISOU 4710  CG  PRO B 958     5772   5653   6408    474    384   -205       C  
-ATOM   4711  CD  PRO B 958     -86.288  18.405  15.957  1.00 46.70           C  
-ANISOU 4711  CD  PRO B 958     5765   5687   6292    455    391   -248       C  
-ATOM   4712  N   SER B 959     -83.070  19.486  17.553  1.00 41.12           N  
-ANISOU 4712  N   SER B 959     5215   4814   5595    365    307   -432       N  
-ATOM   4713  CA  SER B 959     -82.063  20.115  18.400  1.00 41.92           C  
-ANISOU 4713  CA  SER B 959     5379   4852   5696    338    284   -515       C  
-ATOM   4714  C   SER B 959     -81.050  19.099  18.931  1.00 41.65           C  
-ANISOU 4714  C   SER B 959     5366   4854   5605    272    213   -533       C  
-ATOM   4715  O   SER B 959     -79.949  19.470  19.346  1.00 45.39           O  
-ANISOU 4715  O   SER B 959     5876   5278   6090    235    173   -587       O  
-ATOM   4716  CB  SER B 959     -82.745  20.845  19.582  1.00 42.70           C  
-ANISOU 4716  CB  SER B 959     5525   4939   5760    376    340   -588       C  
-ATOM   4717  N   ALA B 960     -81.419  17.822  18.922  1.00 40.05           N  
-ANISOU 4717  N   ALA B 960     5139   4735   5344    256    195   -487       N  
-ATOM   4718  CA  ALA B 960     -80.502  16.753  19.318  1.00 40.73           C  
-ANISOU 4718  CA  ALA B 960     5240   4854   5382    199    124   -490       C  
-ATOM   4719  C   ALA B 960     -79.759  16.070  18.129  1.00 37.90           C  
-ANISOU 4719  C   ALA B 960     4837   4495   5069    172     78   -432       C  
-ATOM   4720  O   ALA B 960     -78.957  15.166  18.338  1.00 38.17           O  
-ANISOU 4720  O   ALA B 960     4876   4551   5075    132     19   -430       O  
-ATOM   4721  CB  ALA B 960     -81.240  15.709  20.135  1.00 38.21           C  
-ANISOU 4721  CB  ALA B 960     4934   4619   4967    192    128   -479       C  
-ATOM   4722  N   ASN B 961     -79.999  16.512  16.902  1.00 37.93           N  
-ANISOU 4722  N   ASN B 961     4798   4473   5141    195    105   -385       N  
-ATOM   4723  CA  ASN B 961     -79.250  15.998  15.756  1.00 39.06           C  
-ANISOU 4723  CA  ASN B 961     4905   4611   5327    168     70   -338       C  
-ATOM   4724  C   ASN B 961     -77.768  16.278  15.920  1.00 37.52           C  
-ANISOU 4724  C   ASN B 961     4725   4365   5167    129     22   -382       C  
-ATOM   4725  O   ASN B 961     -77.401  17.311  16.461  1.00 36.43           O  
-ANISOU 4725  O   ASN B 961     4618   4170   5054    129     28   -438       O  
-ATOM   4726  CB  ASN B 961     -79.751  16.629  14.458  1.00 40.39           C  
-ANISOU 4726  CB  ASN B 961     5034   4754   5559    199    110   -284       C  
-ATOM   4727  CG  ASN B 961     -79.033  16.070  13.250  1.00 42.90           C  
-ANISOU 4727  CG  ASN B 961     5317   5073   5909    170     81   -236       C  
-ATOM   4728  OD1 ASN B 961     -79.262  14.928  12.845  1.00 43.38           O  
-ANISOU 4728  OD1 ASN B 961     5357   5191   5936    157     64   -193       O  
-ATOM   4729  ND2 ASN B 961     -78.089  16.826  12.737  1.00 42.29           N  
-ANISOU 4729  ND2 ASN B 961     5239   4932   5898    154     75   -248       N  
-ATOM   4730  N   ILE B 962     -76.925  15.326  15.521  1.00 37.31           N  
-ANISOU 4730  N   ILE B 962     4677   4359   5141     95    -28   -360       N  
-ATOM   4731  CA  ILE B 962     -75.487  15.569  15.526  1.00 36.61           C  
-ANISOU 4731  CA  ILE B 962     4585   4227   5097     58    -73   -395       C  
-ATOM   4732  C   ILE B 962     -74.946  15.310  14.143  1.00 35.67           C  
-ANISOU 4732  C   ILE B 962     4418   4100   5035     47    -74   -346       C  
-ATOM   4733  O   ILE B 962     -75.522  14.538  13.389  1.00 34.21           O  
-ANISOU 4733  O   ILE B 962     4209   3956   4833     58    -61   -290       O  
-ATOM   4734  CB  ILE B 962     -74.726  14.722  16.546  1.00 39.19           C  
-ANISOU 4734  CB  ILE B 962     4933   4583   5376     27   -139   -429       C  
-ATOM   4735  CG1 ILE B 962     -74.792  13.229  16.215  1.00 38.05           C  
-ANISOU 4735  CG1 ILE B 962     4767   4497   5194     22   -167   -379       C  
-ATOM   4736  CG2 ILE B 962     -75.234  15.025  17.955  1.00 40.22           C  
-ANISOU 4736  CG2 ILE B 962     5120   4723   5439     33   -137   -482       C  
-ATOM   4737  CD1 ILE B 962     -73.820  12.403  17.024  1.00 40.93           C  
-ANISOU 4737  CD1 ILE B 962     5144   4878   5528     -7   -241   -404       C  
-ATOM   4738  N   SER B 963     -73.855  15.984  13.820  1.00 36.22           N  
-ANISOU 4738  N   SER B 963     4476   4116   5170     21    -87   -369       N  
-ATOM   4739  CA  SER B 963     -73.194  15.824  12.546  1.00 37.49           C  
-ANISOU 4739  CA  SER B 963     4591   4267   5385      5    -84   -329       C  
-ATOM   4740  C   SER B 963     -71.850  15.140  12.752  1.00 37.81           C  
-ANISOU 4740  C   SER B 963     4609   4316   5440    -32   -142   -353       C  
-ATOM   4741  O   SER B 963     -71.001  15.603  13.506  1.00 38.93           O  
-ANISOU 4741  O   SER B 963     4760   4430   5602    -57   -176   -406       O  
-ATOM   4742  CB  SER B 963     -73.056  17.167  11.832  1.00 35.10           C  
-ANISOU 4742  CB  SER B 963     4285   3898   5155      4    -43   -324       C  
-ATOM   4743  OG  SER B 963     -72.176  17.059  10.735  1.00 36.94           O  
-ANISOU 4743  OG  SER B 963     4476   4120   5438    -23    -42   -296       O  
-ATOM   4744  N   LEU B 964     -71.697  14.009  12.076  1.00 38.98           N  
-ANISOU 4744  N   LEU B 964     4727   4505   5577    -32   -153   -313       N  
-ATOM   4745  CA  LEU B 964     -70.513  13.163  12.190  1.00 39.58           C  
-ANISOU 4745  CA  LEU B 964     4776   4597   5667    -55   -206   -327       C  
-ATOM   4746  C   LEU B 964     -69.912  12.962  10.808  1.00 36.19           C  
-ANISOU 4746  C   LEU B 964     4297   4162   5290    -66   -183   -293       C  
-ATOM   4747  O   LEU B 964     -70.511  12.303   9.956  1.00 34.53           O  
-ANISOU 4747  O   LEU B 964     4081   3981   5059    -51   -156   -246       O  
-ATOM   4748  CB  LEU B 964     -70.874  11.802  12.760  1.00 37.79           C  
-ANISOU 4748  CB  LEU B 964     4565   4422   5372    -43   -243   -315       C  
-ATOM   4749  CG  LEU B 964     -71.073  11.669  14.272  1.00 40.55           C  
-ANISOU 4749  CG  LEU B 964     4960   4786   5661    -44   -285   -353       C  
-ATOM   4750  CD1 LEU B 964     -71.108  10.168  14.578  1.00 39.08           C  
-ANISOU 4750  CD1 LEU B 964     4780   4645   5423    -40   -327   -330       C  
-ATOM   4751  CD2 LEU B 964     -69.971  12.340  15.079  1.00 40.37           C  
-ANISOU 4751  CD2 LEU B 964     4938   4732   5670    -71   -330   -412       C  
-ATOM   4752  N   ASP B 965     -68.726  13.507  10.601  1.00 35.75           N  
-ANISOU 4752  N   ASP B 965     4209   4075   5302    -94   -192   -318       N  
-ATOM   4753  CA  ASP B 965     -68.025  13.344   9.330  1.00 37.18           C  
-ANISOU 4753  CA  ASP B 965     4341   4253   5533   -108   -165   -290       C  
-ATOM   4754  C   ASP B 965     -68.897  13.827   8.153  1.00 35.86           C  
-ANISOU 4754  C   ASP B 965     4182   4078   5366    -97    -99   -238       C  
-ATOM   4755  O   ASP B 965     -68.976  13.172   7.101  1.00 34.44           O  
-ANISOU 4755  O   ASP B 965     3983   3924   5180    -93    -74   -199       O  
-ATOM   4756  CB  ASP B 965     -67.602  11.841   9.122  1.00 38.03           C  
-ANISOU 4756  CB  ASP B 965     4422   4405   5622    -99   -195   -278       C  
-ATOM   4757  CG  ASP B 965     -66.538  11.661   7.996  1.00 43.90           C  
-ANISOU 4757  CG  ASP B 965     5108   5147   6427   -116   -172   -269       C  
-ATOM   4758  OD1 ASP B 965     -66.196  10.501   7.694  1.00 50.18           O  
-ANISOU 4758  OD1 ASP B 965     5881   5970   7213   -104   -186   -260       O  
-ATOM   4759  OD2 ASP B 965     -66.023  12.650   7.410  1.00 44.75           O  
-ANISOU 4759  OD2 ASP B 965     5190   5221   6590   -142   -138   -270       O  
-ATOM   4760  N   GLY B 966     -69.611  14.919   8.369  1.00 33.36           N  
-ANISOU 4760  N   GLY B 966     3898   3728   5052    -89    -73   -238       N  
-ATOM   4761  CA  GLY B 966     -70.469  15.482   7.346  1.00 33.75           C  
-ANISOU 4761  CA  GLY B 966     3955   3765   5103    -75    -18   -186       C  
-ATOM   4762  C   GLY B 966     -71.833  14.788   7.219  1.00 32.09           C  
-ANISOU 4762  C   GLY B 966     3764   3602   4826    -39     -7   -146       C  
-ATOM   4763  O   GLY B 966     -72.577  15.126   6.336  1.00 32.71           O  
-ANISOU 4763  O   GLY B 966     3846   3681   4903    -25     31    -98       O  
-ATOM   4764  N   VAL B 967     -72.168  13.831   8.092  1.00 31.36           N  
-ANISOU 4764  N   VAL B 967     3686   3550   4679    -26    -43   -163       N  
-ATOM   4765  CA  VAL B 967     -73.456  13.122   8.048  1.00 29.58           C  
-ANISOU 4765  CA  VAL B 967     3476   3373   4390      0    -34   -126       C  
-ATOM   4766  C   VAL B 967     -74.298  13.402   9.283  1.00 29.99           C  
-ANISOU 4766  C   VAL B 967     3561   3430   4402     22    -40   -152       C  
-ATOM   4767  O   VAL B 967     -73.827  13.302  10.398  1.00 30.58           O  
-ANISOU 4767  O   VAL B 967     3653   3500   4465     13    -76   -200       O  
-ATOM   4768  CB  VAL B 967     -73.234  11.595   7.945  1.00 27.77           C  
-ANISOU 4768  CB  VAL B 967     3238   3191   4123     -8    -66   -117       C  
-ATOM   4769  CG1 VAL B 967     -74.549  10.832   7.791  1.00 28.21           C  
-ANISOU 4769  CG1 VAL B 967     3308   3296   4115      8    -57    -76       C  
-ATOM   4770  CG2 VAL B 967     -72.280  11.276   6.795  1.00 27.51           C  
-ANISOU 4770  CG2 VAL B 967     3171   3152   4128    -28    -56   -104       C  
-ATOM   4771  N   ASP B 968     -75.562  13.742   9.081  1.00 29.94           N  
-ANISOU 4771  N   ASP B 968     3564   3438   4375     50     -5   -118       N  
-ATOM   4772  CA  ASP B 968     -76.480  13.891  10.202  1.00 30.27           C  
-ANISOU 4772  CA  ASP B 968     3633   3495   4374     74     -1   -139       C  
-ATOM   4773  C   ASP B 968     -76.942  12.553  10.778  1.00 29.59           C  
-ANISOU 4773  C   ASP B 968     3555   3471   4217     70    -28   -132       C  
-ATOM   4774  O   ASP B 968     -77.263  11.616  10.049  1.00 27.60           O  
-ANISOU 4774  O   ASP B 968     3287   3258   3942     64    -31    -89       O  
-ATOM   4775  CB  ASP B 968     -77.668  14.703   9.771  1.00 30.72           C  
-ANISOU 4775  CB  ASP B 968     3686   3547   4440    111     47   -104       C  
-ATOM   4776  CG  ASP B 968     -77.311  16.142   9.453  1.00 35.13           C  
-ANISOU 4776  CG  ASP B 968     4250   4033   5067    119     74   -115       C  
-ATOM   4777  OD1 ASP B 968     -76.348  16.707  10.030  1.00 37.95           O  
-ANISOU 4777  OD1 ASP B 968     4623   4341   5455     99     59   -169       O  
-ATOM   4778  OD2 ASP B 968     -78.011  16.748   8.628  1.00 42.40           O  
-ANISOU 4778  OD2 ASP B 968     5158   4941   6010    144    109    -68       O  
-ATOM   4779  N   VAL B 969     -76.934  12.466  12.101  1.00 30.24           N  
-ANISOU 4779  N   VAL B 969     3668   3560   4262     70    -49   -177       N  
-ATOM   4780  CA  VAL B 969     -77.512  11.347  12.816  1.00 30.66           C  
-ANISOU 4780  CA  VAL B 969     3739   3669   4242     66    -69   -169       C  
-ATOM   4781  C   VAL B 969     -78.664  11.922  13.643  1.00 32.23           C  
-ANISOU 4781  C   VAL B 969     3958   3885   4405     93    -31   -182       C  
-ATOM   4782  O   VAL B 969     -78.420  12.636  14.625  1.00 31.40           O  
-ANISOU 4782  O   VAL B 969     3882   3752   4295     97    -32   -236       O  
-ATOM   4783  CB  VAL B 969     -76.499  10.698  13.752  1.00 30.05           C  
-ANISOU 4783  CB  VAL B 969     3684   3591   4143     41   -127   -209       C  
-ATOM   4784  CG1 VAL B 969     -77.096   9.443  14.353  1.00 31.00           C  
-ANISOU 4784  CG1 VAL B 969     3825   3765   4187     33   -148   -189       C  
-ATOM   4785  CG2 VAL B 969     -75.209  10.388  13.008  1.00 30.63           C  
-ANISOU 4785  CG2 VAL B 969     3730   3639   4268     21   -159   -208       C  
-ATOM   4786  N   PRO B 970     -79.917  11.667  13.228  1.00 31.32           N  
-ANISOU 4786  N   PRO B 970     3823   3812   4264    111      3   -134       N  
-ATOM   4787  CA  PRO B 970     -81.059  12.249  13.891  1.00 30.76           C  
-ANISOU 4787  CA  PRO B 970     3760   3760   4168    142     48   -143       C  
-ATOM   4788  C   PRO B 970     -81.449  11.423  15.090  1.00 34.33           C  
-ANISOU 4788  C   PRO B 970     4241   4261   4540    128     35   -159       C  
-ATOM   4789  O   PRO B 970     -82.526  10.804  15.113  1.00 34.92           O  
-ANISOU 4789  O   PRO B 970     4303   4395   4572    130     56   -122       O  
-ATOM   4790  CB  PRO B 970     -82.148  12.199  12.821  1.00 31.08           C  
-ANISOU 4790  CB  PRO B 970     3756   3832   4220    162     82    -77       C  
-ATOM   4791  CG  PRO B 970     -81.826  10.971  12.048  1.00 31.30           C  
-ANISOU 4791  CG  PRO B 970     3772   3889   4233    126     45    -37       C  
-ATOM   4792  CD  PRO B 970     -80.311  10.842  12.075  1.00 31.70           C  
-ANISOU 4792  CD  PRO B 970     3840   3894   4310    101      3    -72       C  
-ATOM   4793  N   LEU B 971     -80.610  11.451  16.110  1.00 36.14           N  
-ANISOU 4793  N   LEU B 971     4512   4470   4748    110      2   -213       N  
-ATOM   4794  CA  LEU B 971     -80.811  10.591  17.264  1.00 41.35           C  
-ANISOU 4794  CA  LEU B 971     5209   5175   5326     90    -19   -226       C  
-ATOM   4795  C   LEU B 971     -81.630  11.233  18.412  1.00 39.78           C  
-ANISOU 4795  C   LEU B 971     5040   4994   5079    110     26   -265       C  
-ATOM   4796  O   LEU B 971     -81.696  10.690  19.503  1.00 41.25           O  
-ANISOU 4796  O   LEU B 971     5268   5214   5192     91     11   -284       O  
-ATOM   4797  CB  LEU B 971     -79.466  10.023  17.772  1.00 41.63           C  
-ANISOU 4797  CB  LEU B 971     5274   5191   5351     56    -91   -254       C  
-ATOM   4798  CG  LEU B 971     -78.301  10.976  17.958  1.00 42.34           C  
-ANISOU 4798  CG  LEU B 971     5375   5220   5493     53   -115   -310       C  
-ATOM   4799  CD1 LEU B 971     -78.651  12.025  18.987  1.00 42.28           C  
-ANISOU 4799  CD1 LEU B 971     5405   5197   5461     68    -84   -368       C  
-ATOM   4800  CD2 LEU B 971     -77.081  10.168  18.371  1.00 45.73           C  
-ANISOU 4800  CD2 LEU B 971     5819   5645   5910     21   -193   -323       C  
-ATOM   4801  N   GLY B 972     -82.283  12.349  18.152  1.00 40.16           N  
-ANISOU 4801  N   GLY B 972     5070   5022   5168    151     84   -275       N  
-ATOM   4802  CA  GLY B 972     -83.184  12.940  19.141  1.00 42.89           C  
-ANISOU 4802  CA  GLY B 972     5438   5387   5472    179    140   -311       C  
-ATOM   4803  C   GLY B 972     -84.391  12.076  19.456  1.00 44.10           C  
-ANISOU 4803  C   GLY B 972     5577   5623   5558    176    170   -271       C  
-ATOM   4804  O   GLY B 972     -84.828  11.300  18.605  1.00 44.04           O  
-ANISOU 4804  O   GLY B 972     5526   5650   5557    165    163   -207       O  
-ATOM   4805  N   THR B 973     -84.926  12.196  20.672  1.00 44.27           N  
-ANISOU 4805  N   THR B 973     5633   5676   5512    180    204   -311       N  
-ATOM   4806  CA  THR B 973     -86.199  11.534  21.009  1.00 46.57           C  
-ANISOU 4806  CA  THR B 973     5904   6048   5743    179    249   -275       C  
-ATOM   4807  C   THR B 973     -87.333  12.096  20.160  1.00 48.88           C  
-ANISOU 4807  C   THR B 973     6125   6355   6091    228    311   -237       C  
-ATOM   4808  O   THR B 973     -87.300  13.252  19.774  1.00 49.48           O  
-ANISOU 4808  O   THR B 973     6189   6378   6235    275    338   -260       O  
-ATOM   4809  CB  THR B 973     -86.579  11.634  22.514  1.00 47.39           C  
-ANISOU 4809  CB  THR B 973     6061   6186   5759    175    285   -328       C  
-ATOM   4810  OG1 THR B 973     -86.564  12.992  22.916  1.00 50.10           O  
-ANISOU 4810  OG1 THR B 973     6424   6481   6131    220    329   -396       O  
-ATOM   4811  CG2 THR B 973     -85.598  10.859  23.396  1.00 49.54           C  
-ANISOU 4811  CG2 THR B 973     6403   6460   5961    121    216   -349       C  
-ATOM   4812  N   GLY B 974     -88.336  11.269  19.892  1.00 50.47           N  
-ANISOU 4812  N   GLY B 974     6283   6630   6265    216    330   -178       N  
-ATOM   4813  CA  GLY B 974     -89.478  11.666  19.078  1.00 52.56           C  
-ANISOU 4813  CA  GLY B 974     6471   6922   6577    258    380   -133       C  
-ATOM   4814  C   GLY B 974     -90.354  12.745  19.688  1.00 52.51           C  
-ANISOU 4814  C   GLY B 974     6450   6921   6581    320    461   -172       C  
-ATOM   4815  O   GLY B 974     -90.825  12.618  20.813  1.00 53.94           O  
-ANISOU 4815  O   GLY B 974     6656   7145   6694    316    503   -205       O  
-ATOM   4816  N   ILE B 975     -90.550  13.818  18.926  1.00 52.21           N  
-ANISOU 4816  N   ILE B 975     6374   6836   6627    379    486   -167       N  
-ATOM   4817  CA  ILE B 975     -91.438  14.911  19.297  1.00 50.79           C  
-ANISOU 4817  CA  ILE B 975     6171   6652   6476    451    566   -198       C  
-ATOM   4818  C   ILE B 975     -92.398  15.174  18.148  1.00 51.10           C  
-ANISOU 4818  C   ILE B 975     6119   6713   6584    496    586   -127       C  
-ATOM   4819  O   ILE B 975     -92.229  14.642  17.046  1.00 49.18           O  
-ANISOU 4819  O   ILE B 975     5843   6477   6365    468    536    -63       O  
-ATOM   4820  CB  ILE B 975     -90.667  16.221  19.603  1.00 47.92           C  
-ANISOU 4820  CB  ILE B 975     5862   6188   6158    490    576   -272       C  
-ATOM   4821  CG1 ILE B 975     -90.026  16.787  18.333  1.00 46.23           C  
-ANISOU 4821  CG1 ILE B 975     5632   5899   6036    504    536   -240       C  
-ATOM   4822  CG2 ILE B 975     -89.633  15.995  20.692  1.00 45.09           C  
-ANISOU 4822  CG2 ILE B 975     5592   5806   5733    441    543   -341       C  
-ATOM   4823  CD1 ILE B 975     -89.442  18.172  18.506  1.00 46.96           C  
-ANISOU 4823  CD1 ILE B 975     5768   5888   6186    545    554   -303       C  
-ATOM   4824  N   SER B 976     -93.368  16.043  18.401  1.00 51.77           N  
-ANISOU 4824  N   SER B 976     6165   6806   6700    567    660   -141       N  
-ATOM   4825  CA  SER B 976     -94.347  16.402  17.406  1.00 53.37           C  
-ANISOU 4825  CA  SER B 976     6277   7030   6970    620    680    -75       C  
-ATOM   4826  C   SER B 976     -93.687  17.201  16.298  1.00 49.75           C  
-ANISOU 4826  C   SER B 976     5823   6482   6598    646    643    -54       C  
-ATOM   4827  O   SER B 976     -92.915  18.104  16.566  1.00 48.83           O  
-ANISOU 4827  O   SER B 976     5765   6275   6512    669    646   -112       O  
-ATOM   4828  CB  SER B 976     -95.460  17.238  18.036  1.00 54.60           C  
-ANISOU 4828  CB  SER B 976     6392   7205   7146    700    772   -104       C  
-ATOM   4829  OG  SER B 976     -96.469  17.474  17.071  1.00 56.13           O  
-ANISOU 4829  OG  SER B 976     6488   7433   7405    750    785    -31       O  
-ATOM   4830  N   SER B 977     -93.987  16.847  15.056  1.00 49.47           N  
-ANISOU 4830  N   SER B 977     5727   6473   6595    638    605     28       N  
-ATOM   4831  CA  SER B 977     -93.423  17.542  13.900  1.00 49.69           C  
-ANISOU 4831  CA  SER B 977     5758   6425   6698    658    570     61       C  
-ATOM   4832  C   SER B 977     -94.255  18.757  13.552  1.00 53.41           C  
-ANISOU 4832  C   SER B 977     6180   6865   7249    752    617     79       C  
-ATOM   4833  O   SER B 977     -93.822  19.601  12.780  1.00 58.80           O  
-ANISOU 4833  O   SER B 977     6875   7469   7999    782    601     96       O  
-ATOM   4834  CB  SER B 977     -93.392  16.618  12.683  1.00 46.94           C  
-ANISOU 4834  CB  SER B 977     5371   6120   6342    605    509    142       C  
-ATOM   4835  OG  SER B 977     -94.696  16.151  12.367  1.00 44.25           O  
-ANISOU 4835  OG  SER B 977     4946   5874   5994    617    523    203       O  
-ATOM   4836  N   GLY B 978     -95.473  18.815  14.075  1.00 56.46           N  
-ANISOU 4836  N   GLY B 978     6508   7316   7629    799    675     81       N  
-ATOM   4837  CA  GLY B 978     -96.401  19.880  13.724  1.00 59.15           C  
-ANISOU 4837  CA  GLY B 978     6788   7637   8050    897    721    107       C  
-ATOM   4838  C   GLY B 978     -97.138  19.625  12.423  1.00 59.88           C  
-ANISOU 4838  C   GLY B 978     6791   7783   8179    906    684    212       C  
-ATOM   4839  O   GLY B 978     -97.881  20.477  11.967  1.00 61.72           O  
-ANISOU 4839  O   GLY B 978     6968   8000   8484    988    708    248       O  
-ATOM   4840  N   VAL B 979     -96.938  18.468  11.806  1.00 59.30           N  
-ANISOU 4840  N   VAL B 979     6706   7769   8057    824    624    262       N  
-ATOM   4841  CA  VAL B 979     -97.617  18.179  10.544  1.00 62.91           C  
-ANISOU 4841  CA  VAL B 979     7084   8279   8539    823    583    360       C  
-ATOM   4842  C   VAL B 979     -98.996  17.569  10.774  1.00 67.35           C  
-ANISOU 4842  C   VAL B 979     7549   8962   9080    828    610    397       C  
-ATOM   4843  O   VAL B 979     -99.116  16.486  11.361  1.00 68.77           O  
-ANISOU 4843  O   VAL B 979     7730   9213   9185    761    611    383       O  
-ATOM   4844  CB  VAL B 979     -96.713  17.316   9.629  1.00 60.83           C  
-ANISOU 4844  CB  VAL B 979     6859   8014   8240    734    505    395       C  
-ATOM   4845  CG1 VAL B 979     -97.502  16.754   8.460  1.00 58.13           C  
-ANISOU 4845  CG1 VAL B 979     6439   7749   7898    714    461    490       C  
-ATOM   4846  CG2 VAL B 979     -95.534  18.151   9.133  1.00 61.33           C  
-ANISOU 4846  CG2 VAL B 979     6993   7962   8348    743    483    377       C  
-ATOM   4847  N   ASN B 980    -100.040  18.259  10.297  1.00 69.77           N  
-ANISOU 4847  N   ASN B 980     7768   9290   9452    907    630    448       N  
-ATOM   4848  CA  ASN B 980    -101.395  17.845  10.574  1.00 73.64           C  
-ANISOU 4848  CA  ASN B 980     8153   9893   9934    924    665    480       C  
-ATOM   4849  C   ASN B 980    -101.899  16.737   9.661  1.00 72.66           C  
-ANISOU 4849  C   ASN B 980     7965   9867   9777    851    601    564       C  
-ATOM   4850  O   ASN B 980    -102.223  15.623  10.124  1.00 76.53           O  
-ANISOU 4850  O   ASN B 980     8438  10442  10199    779    603    561       O  
-ATOM   4851  CB  ASN B 980    -102.328  19.070  10.466  1.00 74.90           C  
-ANISOU 4851  CB  ASN B 980     8236  10035  10185   1047    713    501       C  
-ATOM   4852  N   ASP B 981    -101.941  17.024   8.372  1.00 66.98           N  
-ANISOU 4852  N   ASP B 981     7218   9133   9100    863    543    637       N  
-ATOM   4853  CA  ASP B 981    -102.741  16.223   7.470  1.00 69.96           C  
-ANISOU 4853  CA  ASP B 981     7512   9611   9461    817    490    722       C  
-ATOM   4854  C   ASP B 981    -101.810  15.224   6.842  1.00 69.88           C  
-ANISOU 4854  C   ASP B 981     7572   9593   9386    710    420    731       C  
-ATOM   4855  O   ASP B 981    -101.389  15.434   5.720  1.00 74.36           O  
-ANISOU 4855  O   ASP B 981     8159  10124   9971    703    364    777       O  
-ATOM   4856  CB  ASP B 981    -103.446  17.085   6.401  1.00 70.65           C  
-ANISOU 4856  CB  ASP B 981     7519   9697   9625    894    463    803       C  
-ATOM   4857  N   THR B 982    -101.451  14.157   7.559  1.00 67.14           N  
-ANISOU 4857  N   THR B 982     7270   9276   8965    629    424    688       N  
-ATOM   4858  CA  THR B 982    -100.553  13.145   6.986  1.00 64.60           C  
-ANISOU 4858  CA  THR B 982     7017   8944   8584    531    360    693       C  
-ATOM   4859  C   THR B 982    -101.054  11.728   7.218  1.00 59.13           C  
-ANISOU 4859  C   THR B 982     6300   8346   7822    439    343    707       C  
-ATOM   4860  O   THR B 982    -101.655  11.436   8.230  1.00 53.51           O  
-ANISOU 4860  O   THR B 982     5558   7687   7087    436    393    683       O  
-ATOM   4861  CB  THR B 982     -99.094  13.262   7.514  1.00 61.65           C  
-ANISOU 4861  CB  THR B 982     6761   8470   8192    515    365    618       C  
-ATOM   4862  OG1 THR B 982     -98.317  12.160   7.028  1.00 59.14           O  
-ANISOU 4862  OG1 THR B 982     6499   8153   7818    422    308    622       O  
-ATOM   4863  CG2 THR B 982     -99.054  13.227   9.040  1.00 61.63           C  
-ANISOU 4863  CG2 THR B 982     6788   8468   8162    524    427    542       C  
-ATOM   4864  N   SER B 983    -100.732  10.849   6.280  1.00 59.59           N  
-ANISOU 4864  N   SER B 983     6380   8420   7843    361    276    744       N  
-ATOM   4865  CA  SER B 983    -101.012   9.422   6.404  1.00 59.35           C  
-ANISOU 4865  CA  SER B 983     6348   8461   7743    262    251    754       C  
-ATOM   4866  C   SER B 983    -100.031   8.682   7.339  1.00 56.67           C  
-ANISOU 4866  C   SER B 983     6107   8080   7348    209    261    687       C  
-ATOM   4867  O   SER B 983    -100.225   7.508   7.588  1.00 51.76           O  
-ANISOU 4867  O   SER B 983     5492   7505   6668    130    245    692       O  
-ATOM   4868  CB  SER B 983    -100.942   8.767   5.012  1.00 58.29           C  
-ANISOU 4868  CB  SER B 983     6214   8347   7588    198    173    811       C  
-ATOM   4869  OG  SER B 983    -101.736   9.481   4.067  1.00 67.59           O  
-ANISOU 4869  OG  SER B 983     7309   9558   8815    246    152    878       O  
-ATOM   4870  N   LEU B 984     -98.978   9.343   7.831  1.00 51.72           N  
-ANISOU 4870  N   LEU B 984     5554   7362   6736    249    281    628       N  
-ATOM   4871  CA  LEU B 984     -97.866   8.629   8.464  1.00 48.90           C  
-ANISOU 4871  CA  LEU B 984     5294   6958   6329    197    270    573       C  
-ATOM   4872  C   LEU B 984     -97.654   9.045   9.907  1.00 46.55           C  
-ANISOU 4872  C   LEU B 984     5030   6636   6022    231    329    506       C  
-ATOM   4873  O   LEU B 984     -97.648  10.241  10.211  1.00 44.95           O  
-ANISOU 4873  O   LEU B 984     4819   6392   5867    310    370    479       O  
-ATOM   4874  CB  LEU B 984     -96.569   8.891   7.687  1.00 46.96           C  
-ANISOU 4874  CB  LEU B 984     5117   6624   6102    196    230    559       C  
-ATOM   4875  CG  LEU B 984     -96.409   8.326   6.269  1.00 45.91           C  
-ANISOU 4875  CG  LEU B 984     4983   6499   5961    147    168    610       C  
-ATOM   4876  CD1 LEU B 984     -95.159   8.892   5.626  1.00 44.10           C  
-ANISOU 4876  CD1 LEU B 984     4814   6181   5761    164    148    591       C  
-ATOM   4877  CD2 LEU B 984     -96.339   6.800   6.272  1.00 44.04           C  
-ANISOU 4877  CD2 LEU B 984     4775   6300   5657     53    132    614       C  
-ATOM   4878  N   LEU B 985     -97.479   8.059  10.792  1.00 45.61           N  
-ANISOU 4878  N   LEU B 985     4954   6538   5837    171    331    480       N  
-ATOM   4879  CA  LEU B 985     -97.107   8.351  12.182  1.00 48.08           C  
-ANISOU 4879  CA  LEU B 985     5318   6826   6125    192    378    413       C  
-ATOM   4880  C   LEU B 985     -95.655   8.847  12.265  1.00 45.31           C  
-ANISOU 4880  C   LEU B 985     5052   6372   5790    210    356    358       C  
-ATOM   4881  O   LEU B 985     -95.349   9.762  13.011  1.00 45.88           O  
-ANISOU 4881  O   LEU B 985     5152   6401   5880    262    395    305       O  
-ATOM   4882  CB  LEU B 985     -97.291   7.118  13.073  1.00 50.33           C  
-ANISOU 4882  CB  LEU B 985     5630   7161   6330    118    380    407       C  
-ATOM   4883  CG  LEU B 985     -98.728   6.585  13.268  1.00 52.91           C  
-ANISOU 4883  CG  LEU B 985     5874   7595   6633     90    413    453       C  
-ATOM   4884  CD1 LEU B 985     -98.727   5.316  14.121  1.00 53.22           C  
-ANISOU 4884  CD1 LEU B 985     5959   7670   6591      6    409    450       C  
-ATOM   4885  CD2 LEU B 985     -99.632   7.633  13.901  1.00 54.27           C  
-ANISOU 4885  CD2 LEU B 985     5980   7802   6837    168    493    437       C  
-ATOM   4886  N   TYR B 986     -94.776   8.253  11.462  1.00 42.45           N  
-ANISOU 4886  N   TYR B 986     4732   5974   5424    165    295    372       N  
-ATOM   4887  CA  TYR B 986     -93.355   8.582  11.492  1.00 40.08           C  
-ANISOU 4887  CA  TYR B 986     4506   5585   5140    171    270    324       C  
-ATOM   4888  C   TYR B 986     -92.807   8.821  10.074  1.00 34.99           C  
-ANISOU 4888  C   TYR B 986     3856   4898   4540    173    229    356       C  
-ATOM   4889  O   TYR B 986     -93.388   8.374   9.078  1.00 33.04           O  
-ANISOU 4889  O   TYR B 986     3567   4695   4293    149    205    414       O  
-ATOM   4890  CB  TYR B 986     -92.587   7.461  12.203  1.00 39.43           C  
-ANISOU 4890  CB  TYR B 986     4493   5495   4995    108    239    296       C  
-ATOM   4891  CG  TYR B 986     -93.270   7.044  13.480  1.00 43.23           C  
-ANISOU 4891  CG  TYR B 986     4977   6031   5418     93    276    281       C  
-ATOM   4892  CD1 TYR B 986     -93.215   7.843  14.608  1.00 43.52           C  
-ANISOU 4892  CD1 TYR B 986     5036   6051   5449    135    322    226       C  
-ATOM   4893  CD2 TYR B 986     -94.035   5.881  13.540  1.00 43.89           C  
-ANISOU 4893  CD2 TYR B 986     5040   6185   5451     32    268    323       C  
-ATOM   4894  CE1 TYR B 986     -93.867   7.485  15.774  1.00 44.29           C  
-ANISOU 4894  CE1 TYR B 986     5137   6204   5486    119    363    212       C  
-ATOM   4895  CE2 TYR B 986     -94.698   5.528  14.700  1.00 43.89           C  
-ANISOU 4895  CE2 TYR B 986     5040   6239   5396     14    308    313       C  
-ATOM   4896  CZ  TYR B 986     -94.613   6.328  15.818  1.00 44.89           C  
-ANISOU 4896  CZ  TYR B 986     5191   6353   5513     59    358    258       C  
-ATOM   4897  OH  TYR B 986     -95.289   5.974  16.982  1.00 43.33           O  
-ANISOU 4897  OH  TYR B 986     4997   6214   5251     38    404    248       O  
-ATOM   4898  N   ASN B 987     -91.706   9.553  10.003  1.00 32.22           N  
-ANISOU 4898  N   ASN B 987     3550   4467   4226    199    223    318       N  
-ATOM   4899  CA  ASN B 987     -91.052   9.830   8.734  1.00 33.20           C  
-ANISOU 4899  CA  ASN B 987     3678   4547   4389    198    191    342       C  
-ATOM   4900  C   ASN B 987     -90.610   8.546   8.044  1.00 33.01           C  
-ANISOU 4900  C   ASN B 987     3676   4539   4327    129    141    365       C  
-ATOM   4901  O   ASN B 987     -90.441   7.496   8.681  1.00 31.44           O  
-ANISOU 4901  O   ASN B 987     3507   4360   4077     83    125    348       O  
-ATOM   4902  CB  ASN B 987     -89.795  10.677   8.922  1.00 32.71           C  
-ANISOU 4902  CB  ASN B 987     3667   4396   4367    222    192    291       C  
-ATOM   4903  CG  ASN B 987     -90.083  12.023   9.544  1.00 32.89           C  
-ANISOU 4903  CG  ASN B 987     3682   4383   4433    290    240    261       C  
-ATOM   4904  OD1 ASN B 987     -91.093  12.633   9.254  1.00 34.76           O  
-ANISOU 4904  OD1 ASN B 987     3866   4644   4698    335    268    295       O  
-ATOM   4905  ND2 ASN B 987     -89.198  12.486  10.401  1.00 33.92           N  
-ANISOU 4905  ND2 ASN B 987     3864   4455   4569    298    247    195       N  
-ATOM   4906  N   GLU B 988     -90.502   8.624   6.729  1.00 30.62           N  
-ANISOU 4906  N   GLU B 988     3358   4230   4046    122    118    406       N  
-ATOM   4907  CA  GLU B 988     -89.733   7.667   5.999  1.00 30.57           C  
-ANISOU 4907  CA  GLU B 988     3387   4213   4016     67     76    410       C  
-ATOM   4908  C   GLU B 988     -89.056   8.376   4.837  1.00 30.31           C  
-ANISOU 4908  C   GLU B 988     3359   4133   4026     82     68    425       C  
-ATOM   4909  O   GLU B 988     -89.452   9.475   4.447  1.00 31.70           O  
-ANISOU 4909  O   GLU B 988     3504   4298   4244    129     88    450       O  
-ATOM   4910  CB  GLU B 988     -90.556   6.471   5.542  1.00 31.41           C  
-ANISOU 4910  CB  GLU B 988     3473   4388   4073     12     51    453       C  
-ATOM   4911  CG  GLU B 988     -91.852   6.770   4.829  1.00 33.58           C  
-ANISOU 4911  CG  GLU B 988     3679   4726   4355     23     54    515       C  
-ATOM   4912  CD  GLU B 988     -92.699   5.517   4.686  1.00 35.98           C  
-ANISOU 4912  CD  GLU B 988     3964   5101   4605    -41     30    548       C  
-ATOM   4913  OE1 GLU B 988     -92.818   4.996   3.557  1.00 39.39           O  
-ANISOU 4913  OE1 GLU B 988     4393   5554   5020    -81     -4    584       O  
-ATOM   4914  OE2 GLU B 988     -93.252   5.049   5.710  1.00 39.49           O  
-ANISOU 4914  OE2 GLU B 988     4400   5582   5022    -55     47    538       O  
-ATOM   4915  N   TYR B 989     -88.005   7.751   4.334  1.00 28.02           N  
-ANISOU 4915  N   TYR B 989     3110   3812   3726     45     42    409       N  
-ATOM   4916  CA  TYR B 989     -87.164   8.355   3.348  1.00 27.01           C  
-ANISOU 4916  CA  TYR B 989     2994   3635   3633     52     40    414       C  
-ATOM   4917  C   TYR B 989     -86.950   7.345   2.258  1.00 26.26           C  
-ANISOU 4917  C   TYR B 989     2914   3562   3503      0     11    437       C  
-ATOM   4918  O   TYR B 989     -86.671   6.169   2.533  1.00 24.85           O  
-ANISOU 4918  O   TYR B 989     2762   3393   3287    -40    -10    416       O  
-ATOM   4919  CB  TYR B 989     -85.832   8.723   3.968  1.00 28.17           C  
-ANISOU 4919  CB  TYR B 989     3180   3713   3810     62     46    354       C  
-ATOM   4920  CG  TYR B 989     -85.913   9.659   5.132  1.00 26.49           C  
-ANISOU 4920  CG  TYR B 989     2966   3472   3626    106     73    318       C  
-ATOM   4921  CD1 TYR B 989     -86.110   9.179   6.412  1.00 28.02           C  
-ANISOU 4921  CD1 TYR B 989     3173   3684   3788    103     74    283       C  
-ATOM   4922  CD2 TYR B 989     -85.784  11.019   4.960  1.00 27.86           C  
-ANISOU 4922  CD2 TYR B 989     3132   3598   3854    150     98    319       C  
-ATOM   4923  CE1 TYR B 989     -86.179  10.023   7.495  1.00 26.94           C  
-ANISOU 4923  CE1 TYR B 989     3043   3525   3669    141    101    244       C  
-ATOM   4924  CE2 TYR B 989     -85.847  11.874   6.035  1.00 27.02           C  
-ANISOU 4924  CE2 TYR B 989     3033   3462   3774    189    125    278       C  
-ATOM   4925  CZ  TYR B 989     -86.030  11.359   7.300  1.00 27.25           C  
-ANISOU 4925  CZ  TYR B 989     3075   3513   3764    184    126    238       C  
-ATOM   4926  OH  TYR B 989     -86.099  12.176   8.389  1.00 27.54           O  
-ANISOU 4926  OH  TYR B 989     3124   3522   3816    220    154    193       O  
-ATOM   4927  N   ILE B 990     -87.109   7.781   1.013  1.00 24.91           N  
-ANISOU 4927  N   ILE B 990     2728   3396   3340      0      9    482       N  
-ATOM   4928  CA  ILE B 990     -86.997   6.889  -0.126  1.00 24.67           C  
-ANISOU 4928  CA  ILE B 990     2714   3390   3269    -50    -16    505       C  
-ATOM   4929  C   ILE B 990     -86.043   7.470  -1.153  1.00 25.97           C  
-ANISOU 4929  C   ILE B 990     2898   3511   3457    -49     -7    509       C  
-ATOM   4930  O   ILE B 990     -86.154   8.658  -1.550  1.00 25.17           O  
-ANISOU 4930  O   ILE B 990     2779   3390   3393    -14      9    539       O  
-ATOM   4931  CB  ILE B 990     -88.373   6.640  -0.795  1.00 26.99           C  
-ANISOU 4931  CB  ILE B 990     2968   3757   3528    -67    -36    567       C  
-ATOM   4932  CG1 ILE B 990     -89.377   6.108   0.227  1.00 28.00           C  
-ANISOU 4932  CG1 ILE B 990     3068   3934   3635    -72    -39    567       C  
-ATOM   4933  CG2 ILE B 990     -88.274   5.619  -1.896  1.00 27.05           C  
-ANISOU 4933  CG2 ILE B 990     3002   3791   3485   -127    -65    582       C  
-ATOM   4934  CD1 ILE B 990     -90.113   7.202   0.983  1.00 28.05           C  
-ANISOU 4934  CD1 ILE B 990     3028   3948   3682    -11    -10    578       C  
-ATOM   4935  N   VAL B 991     -85.107   6.627  -1.612  1.00 25.41           N  
-ANISOU 4935  N   VAL B 991     2865   3423   3365    -87    -15    480       N  
-ATOM   4936  CA  VAL B 991     -84.286   6.966  -2.786  1.00 24.50           C  
-ANISOU 4936  CA  VAL B 991     2768   3282   3257    -98     -4    489       C  
-ATOM   4937  C   VAL B 991     -84.543   5.988  -3.924  1.00 25.71           C  
-ANISOU 4937  C   VAL B 991     2941   3477   3350   -149    -23    511       C  
-ATOM   4938  O   VAL B 991     -84.978   4.864  -3.686  1.00 26.68           O  
-ANISOU 4938  O   VAL B 991     3073   3632   3432   -180    -47    501       O  
-ATOM   4939  CB  VAL B 991     -82.791   7.011  -2.439  1.00 24.93           C  
-ANISOU 4939  CB  VAL B 991     2848   3275   3349    -94     14    430       C  
-ATOM   4940  CG1 VAL B 991     -82.511   8.119  -1.442  1.00 24.68           C  
-ANISOU 4940  CG1 VAL B 991     2801   3199   3376    -50     32    409       C  
-ATOM   4941  CG2 VAL B 991     -82.272   5.679  -1.908  1.00 25.06           C  
-ANISOU 4941  CG2 VAL B 991     2890   3290   3343   -120     -3    382       C  
-ATOM   4942  N   TYR B 992     -84.292   6.435  -5.153  1.00 26.99           N  
-ANISOU 4942  N   TYR B 992     3113   3640   3504   -160    -14    542       N  
-ATOM   4943  CA  TYR B 992     -84.688   5.731  -6.379  1.00 27.80           C  
-ANISOU 4943  CA  TYR B 992     3234   3788   3541   -208    -33    572       C  
-ATOM   4944  C   TYR B 992     -83.501   5.281  -7.196  1.00 28.38           C  
-ANISOU 4944  C   TYR B 992     3350   3834   3597   -236    -12    539       C  
-ATOM   4945  O   TYR B 992     -83.663   4.873  -8.313  1.00 29.67           O  
-ANISOU 4945  O   TYR B 992     3538   4029   3708   -275    -20    560       O  
-ATOM   4946  CB  TYR B 992     -85.664   6.610  -7.209  1.00 26.87           C  
-ANISOU 4946  CB  TYR B 992     3089   3709   3411   -199    -45    650       C  
-ATOM   4947  CG  TYR B 992     -86.873   6.916  -6.373  1.00 27.55           C  
-ANISOU 4947  CG  TYR B 992     3126   3827   3516   -168    -63    678       C  
-ATOM   4948  CD1 TYR B 992     -86.913   8.025  -5.548  1.00 28.62           C  
-ANISOU 4948  CD1 TYR B 992     3233   3928   3715   -109    -41    679       C  
-ATOM   4949  CD2 TYR B 992     -87.948   6.038  -6.328  1.00 27.89           C  
-ANISOU 4949  CD2 TYR B 992     3150   3933   3512   -200    -97    697       C  
-ATOM   4950  CE1 TYR B 992     -88.009   8.289  -4.720  1.00 29.23           C  
-ANISOU 4950  CE1 TYR B 992     3262   4034   3809    -76    -48    698       C  
-ATOM   4951  CE2 TYR B 992     -89.040   6.299  -5.530  1.00 28.19           C  
-ANISOU 4951  CE2 TYR B 992     3136   4005   3569   -172   -107    721       C  
-ATOM   4952  CZ  TYR B 992     -89.071   7.415  -4.720  1.00 27.52           C  
-ANISOU 4952  CZ  TYR B 992     3021   3887   3547   -107    -80    720       C  
-ATOM   4953  OH  TYR B 992     -90.154   7.661  -3.869  1.00 27.80           O  
-ANISOU 4953  OH  TYR B 992     3004   3958   3602    -75    -80    738       O  
-ATOM   4954  N   ASP B 993     -82.302   5.375  -6.630  1.00 30.23           N  
-ANISOU 4954  N   ASP B 993     3594   4014   3880   -218     14    485       N  
-ATOM   4955  CA  ASP B 993     -81.073   4.960  -7.294  1.00 29.16           C  
-ANISOU 4955  CA  ASP B 993     3488   3851   3739   -239     41    447       C  
-ATOM   4956  C   ASP B 993     -80.247   4.258  -6.233  1.00 28.11           C  
-ANISOU 4956  C   ASP B 993     3360   3680   3639   -226     41    380       C  
-ATOM   4957  O   ASP B 993     -79.960   4.831  -5.205  1.00 27.07           O  
-ANISOU 4957  O   ASP B 993     3206   3517   3560   -193     43    363       O  
-ATOM   4958  CB  ASP B 993     -80.359   6.193  -7.827  1.00 31.51           C  
-ANISOU 4958  CB  ASP B 993     3779   4118   4076   -224     79    464       C  
-ATOM   4959  CG  ASP B 993     -79.038   5.880  -8.541  1.00 33.65           C  
-ANISOU 4959  CG  ASP B 993     4073   4365   4348   -244    117    426       C  
-ATOM   4960  OD1 ASP B 993     -78.420   4.798  -8.364  1.00 32.02           O  
-ANISOU 4960  OD1 ASP B 993     3883   4149   4133   -255    118    371       O  
-ATOM   4961  OD2 ASP B 993     -78.600   6.761  -9.311  1.00 37.72           O  
-ANISOU 4961  OD2 ASP B 993     4590   4869   4874   -249    149    452       O  
-ATOM   4962  N   ILE B 994     -79.874   3.018  -6.483  1.00 27.78           N  
-ANISOU 4962  N   ILE B 994     3350   3639   3566   -252     35    344       N  
-ATOM   4963  CA  ILE B 994     -79.159   2.209  -5.493  1.00 27.82           C  
-ANISOU 4963  CA  ILE B 994     3362   3609   3599   -239     26    287       C  
-ATOM   4964  C   ILE B 994     -77.796   2.766  -5.097  1.00 26.71           C  
-ANISOU 4964  C   ILE B 994     3203   3419   3525   -210     54    247       C  
-ATOM   4965  O   ILE B 994     -77.267   2.431  -4.025  1.00 28.25           O  
-ANISOU 4965  O   ILE B 994     3393   3585   3756   -189     38    209       O  
-ATOM   4966  CB  ILE B 994     -78.970   0.757  -5.978  1.00 28.56           C  
-ANISOU 4966  CB  ILE B 994     3499   3704   3649   -271     18    256       C  
-ATOM   4967  CG1 ILE B 994     -78.095   0.717  -7.234  1.00 31.11           C  
-ANISOU 4967  CG1 ILE B 994     3841   4020   3961   -285     59    238       C  
-ATOM   4968  CG2 ILE B 994     -80.308   0.131  -6.237  1.00 26.98           C  
-ANISOU 4968  CG2 ILE B 994     3316   3551   3384   -308    -15    290       C  
-ATOM   4969  CD1 ILE B 994     -77.853  -0.680  -7.784  1.00 33.38           C  
-ANISOU 4969  CD1 ILE B 994     4175   4301   4206   -312     58    200       C  
-ATOM   4970  N   ALA B 995     -77.231   3.612  -5.939  1.00 25.86           N  
-ANISOU 4970  N   ALA B 995     3087   3304   3436   -212     91    259       N  
-ATOM   4971  CA  ALA B 995     -75.939   4.232  -5.666  1.00 24.91           C  
-ANISOU 4971  CA  ALA B 995     2942   3140   3382   -192    120    226       C  
-ATOM   4972  C   ALA B 995     -76.021   5.345  -4.627  1.00 25.58           C  
-ANISOU 4972  C   ALA B 995     2998   3202   3520   -163    111    232       C  
-ATOM   4973  O   ALA B 995     -74.988   5.802  -4.170  1.00 25.12           O  
-ANISOU 4973  O   ALA B 995     2918   3106   3519   -149    124    200       O  
-ATOM   4974  CB  ALA B 995     -75.333   4.761  -6.953  1.00 25.60           C  
-ANISOU 4974  CB  ALA B 995     3032   3229   3467   -211    167    240       C  
-ATOM   4975  N   GLN B 996     -77.232   5.781  -4.252  1.00 26.38           N  
-ANISOU 4975  N   GLN B 996     3095   3324   3603   -153     90    272       N  
-ATOM   4976  CA  GLN B 996     -77.403   6.803  -3.225  1.00 26.67           C  
-ANISOU 4976  CA  GLN B 996     3110   3337   3686   -123     84    273       C  
-ATOM   4977  C   GLN B 996     -77.270   6.305  -1.777  1.00 27.29           C  
-ANISOU 4977  C   GLN B 996     3188   3403   3779   -105     54    229       C  
-ATOM   4978  O   GLN B 996     -77.477   7.083  -0.835  1.00 24.95           O  
-ANISOU 4978  O   GLN B 996     2878   3089   3511    -81     49    224       O  
-ATOM   4979  CB  GLN B 996     -78.762   7.514  -3.370  1.00 27.36           C  
-ANISOU 4979  CB  GLN B 996     3190   3452   3753   -112     78    331       C  
-ATOM   4980  CG  GLN B 996     -78.781   8.641  -4.368  1.00 28.36           C  
-ANISOU 4980  CG  GLN B 996     3313   3570   3894   -112    106    377       C  
-ATOM   4981  CD  GLN B 996     -80.178   9.176  -4.605  1.00 27.94           C  
-ANISOU 4981  CD  GLN B 996     3249   3549   3818    -98     93    440       C  
-ATOM   4982  OE1 GLN B 996     -80.841   8.749  -5.534  1.00 28.21           O  
-ANISOU 4982  OE1 GLN B 996     3291   3628   3799   -120     83    481       O  
-ATOM   4983  NE2 GLN B 996     -80.586  10.172  -3.836  1.00 28.23           N  
-ANISOU 4983  NE2 GLN B 996     3267   3562   3897    -60     96    448       N  
-ATOM   4984  N   VAL B 997     -76.905   5.043  -1.601  1.00 25.54           N  
-ANISOU 4984  N   VAL B 997     2981   3185   3536   -117     35    198       N  
-ATOM   4985  CA  VAL B 997     -76.808   4.461  -0.289  1.00 25.09           C  
-ANISOU 4985  CA  VAL B 997     2930   3119   3484   -104      2    165       C  
-ATOM   4986  C   VAL B 997     -75.411   3.928  -0.067  1.00 25.72           C  
-ANISOU 4986  C   VAL B 997     3007   3164   3600   -100     -2    115       C  
-ATOM   4987  O   VAL B 997     -74.897   3.159  -0.897  1.00 26.63           O  
-ANISOU 4987  O   VAL B 997     3132   3278   3706   -113      9    104       O  
-ATOM   4988  CB  VAL B 997     -77.756   3.257  -0.165  1.00 25.23           C  
-ANISOU 4988  CB  VAL B 997     2973   3171   3442   -122    -25    179       C  
-ATOM   4989  CG1 VAL B 997     -77.616   2.625   1.214  1.00 26.48           C  
-ANISOU 4989  CG1 VAL B 997     3144   3318   3601   -111    -60    149       C  
-ATOM   4990  CG2 VAL B 997     -79.189   3.698  -0.384  1.00 26.00           C  
-ANISOU 4990  CG2 VAL B 997     3063   3311   3504   -127    -24    230       C  
-ATOM   4991  N   ASN B 998     -74.836   4.231   1.102  1.00 23.75           N  
-ANISOU 4991  N   ASN B 998     2746   2888   3389    -80    -23     82       N  
-ATOM   4992  CA  ASN B 998     -73.594   3.615   1.517  1.00 23.84           C  
-ANISOU 4992  CA  ASN B 998     2750   2872   3435    -72    -41     37       C  
-ATOM   4993  C   ASN B 998     -73.822   3.008   2.891  1.00 25.16           C  
-ANISOU 4993  C   ASN B 998     2936   3039   3585    -61    -89     22       C  
-ATOM   4994  O   ASN B 998     -73.974   3.724   3.911  1.00 25.14           O  
-ANISOU 4994  O   ASN B 998     2930   3031   3592    -51   -104     14       O  
-ATOM   4995  CB  ASN B 998     -72.496   4.671   1.503  1.00 26.10           C  
-ANISOU 4995  CB  ASN B 998     3000   3128   3788    -66    -21     14       C  
-ATOM   4996  CG  ASN B 998     -71.099   4.119   1.709  1.00 25.11           C  
-ANISOU 4996  CG  ASN B 998     2851   2979   3709    -58    -35    -29       C  
-ATOM   4997  OD1 ASN B 998     -70.197   4.859   2.099  1.00 27.48           O  
-ANISOU 4997  OD1 ASN B 998     3119   3257   4065    -55    -36    -54       O  
-ATOM   4998  ND2 ASN B 998     -70.887   2.881   1.380  1.00 25.23           N  
-ANISOU 4998  ND2 ASN B 998     2881   2999   3707    -55    -43    -39       N  
-ATOM   4999  N   LEU B 999     -73.882   1.682   2.917  1.00 25.84           N  
-ANISOU 4999  N   LEU B 999     3049   3129   3641    -66   -113     19       N  
-ATOM   5000  CA  LEU B 999     -74.085   0.958   4.162  1.00 27.28           C  
-ANISOU 5000  CA  LEU B 999     3256   3309   3800    -60   -160     11       C  
-ATOM   5001  C   LEU B 999     -72.881   1.119   5.106  1.00 26.02           C  
-ANISOU 5001  C   LEU B 999     3078   3118   3689    -39   -192    -28       C  
-ATOM   5002  O   LEU B 999     -71.745   1.049   4.678  1.00 27.39           O  
-ANISOU 5002  O   LEU B 999     3225   3270   3912    -28   -186    -53       O  
-ATOM   5003  CB  LEU B 999     -74.317  -0.516   3.868  1.00 27.14           C  
-ANISOU 5003  CB  LEU B 999     3274   3291   3745    -72   -178     18       C  
-ATOM   5004  CG  LEU B 999     -75.569  -0.785   3.048  1.00 25.81           C  
-ANISOU 5004  CG  LEU B 999     3126   3157   3522   -101   -158     56       C  
-ATOM   5005  CD1 LEU B 999     -75.707  -2.287   2.861  1.00 27.51           C  
-ANISOU 5005  CD1 LEU B 999     3384   3363   3705   -117   -180     56       C  
-ATOM   5006  CD2 LEU B 999     -76.810  -0.215   3.693  1.00 25.79           C  
-ANISOU 5006  CD2 LEU B 999     3125   3191   3485   -110   -160     87       C  
-ATOM   5007  N   LYS B1000     -73.148   1.442   6.358  1.00 26.50           N  
-ANISOU 5007  N   LYS B1000     3150   3184   3736    -34   -222    -33       N  
-ATOM   5008  CA  LYS B1000     -72.090   1.727   7.326  1.00 27.65           C  
-ANISOU 5008  CA  LYS B1000     3279   3305   3921    -18   -258    -68       C  
-ATOM   5009  C   LYS B1000     -72.036   0.713   8.448  1.00 27.98           C  
-ANISOU 5009  C   LYS B1000     3355   3345   3932    -13   -316    -72       C  
-ATOM   5010  O   LYS B1000     -70.954   0.280   8.830  1.00 27.80           O  
-ANISOU 5010  O   LYS B1000     3320   3298   3944      2   -355    -95       O  
-ATOM   5011  CB  LYS B1000     -72.269   3.115   7.968  1.00 28.94           C  
-ANISOU 5011  CB  LYS B1000     3432   3470   4096    -19   -249    -80       C  
-ATOM   5012  CG  LYS B1000     -72.392   4.294   7.004  1.00 29.76           C  
-ANISOU 5012  CG  LYS B1000     3508   3570   4231    -23   -194    -71       C  
-ATOM   5013  CD  LYS B1000     -71.382   4.299   5.895  1.00 30.68           C  
-ANISOU 5013  CD  LYS B1000     3589   3669   4400    -26   -170    -80       C  
-ATOM   5014  CE  LYS B1000     -70.021   4.744   6.350  1.00 34.62           C  
-ANISOU 5014  CE  LYS B1000     4052   4141   4963    -22   -191   -120       C  
-ATOM   5015  NZ  LYS B1000     -69.168   5.005   5.156  1.00 36.26           N  
-ANISOU 5015  NZ  LYS B1000     4218   4336   5222    -30   -150   -124       N  
-ATOM   5016  N   TYR B1001     -73.181   0.427   9.063  1.00 27.71           N  
-ANISOU 5016  N   TYR B1001     3360   3335   3833    -25   -324    -47       N  
-ATOM   5017  CA  TYR B1001     -73.203  -0.466  10.240  1.00 28.77           C  
-ANISOU 5017  CA  TYR B1001     3534   3468   3929    -25   -378    -44       C  
-ATOM   5018  C   TYR B1001     -74.288  -1.522  10.094  1.00 28.54           C  
-ANISOU 5018  C   TYR B1001     3547   3456   3839    -46   -376     -6       C  
-ATOM   5019  O   TYR B1001     -75.294  -1.311   9.392  1.00 26.26           O  
-ANISOU 5019  O   TYR B1001     3256   3194   3527    -63   -334     18       O  
-ATOM   5020  CB  TYR B1001     -73.416   0.293  11.552  1.00 28.17           C  
-ANISOU 5020  CB  TYR B1001     3472   3406   3827    -26   -397    -57       C  
-ATOM   5021  CG  TYR B1001     -72.386   1.338  11.822  1.00 31.94           C  
-ANISOU 5021  CG  TYR B1001     3914   3864   4359    -14   -406    -97       C  
-ATOM   5022  CD1 TYR B1001     -71.134   1.005  12.373  1.00 32.54           C  
-ANISOU 5022  CD1 TYR B1001     3978   3916   4469     -2   -463   -122       C  
-ATOM   5023  CD2 TYR B1001     -72.651   2.684  11.529  1.00 34.20           C  
-ANISOU 5023  CD2 TYR B1001     4176   4153   4667    -16   -361   -109       C  
-ATOM   5024  CE1 TYR B1001     -70.195   1.974  12.612  1.00 33.87           C  
-ANISOU 5024  CE1 TYR B1001     4109   4069   4689      2   -474   -159       C  
-ATOM   5025  CE2 TYR B1001     -71.719   3.672  11.771  1.00 32.93           C  
-ANISOU 5025  CE2 TYR B1001     3986   3969   4558    -12   -369   -146       C  
-ATOM   5026  CZ  TYR B1001     -70.499   3.304  12.306  1.00 35.68           C  
-ANISOU 5026  CZ  TYR B1001     4320   4299   4937     -7   -425   -172       C  
-ATOM   5027  OH  TYR B1001     -69.559   4.255  12.521  1.00 40.23           O  
-ANISOU 5027  OH  TYR B1001     4863   4856   5567    -10   -436   -209       O  
-ATOM   5028  N   LEU B1002     -74.027  -2.666  10.731  1.00 27.35           N  
-ANISOU 5028  N   LEU B1002     3434   3288   3668    -46   -425      0       N  
-ATOM   5029  CA  LEU B1002     -74.979  -3.731  10.838  1.00 27.49           C  
-ANISOU 5029  CA  LEU B1002     3500   3318   3628    -72   -433     36       C  
-ATOM   5030  C   LEU B1002     -75.106  -4.054  12.298  1.00 26.97           C  
-ANISOU 5030  C   LEU B1002     3474   3257   3517    -77   -479     45       C  
-ATOM   5031  O   LEU B1002     -74.129  -4.291  12.953  1.00 26.19           O  
-ANISOU 5031  O   LEU B1002     3381   3132   3438    -57   -528     29       O  
-ATOM   5032  CB  LEU B1002     -74.496  -4.924  10.067  1.00 30.03           C  
-ANISOU 5032  CB  LEU B1002     3837   3602   3971    -67   -446     38       C  
-ATOM   5033  CG  LEU B1002     -75.362  -6.192  10.075  1.00 32.40           C  
-ANISOU 5033  CG  LEU B1002     4194   3899   4217    -99   -459     73       C  
-ATOM   5034  CD1 LEU B1002     -76.702  -5.922   9.464  1.00 35.95           C  
-ANISOU 5034  CD1 LEU B1002     4641   4394   4625   -137   -413     99       C  
-ATOM   5035  CD2 LEU B1002     -74.701  -7.271   9.265  1.00 34.32           C  
-ANISOU 5035  CD2 LEU B1002     4453   4093   4492    -88   -469     63       C  
-ATOM   5036  N   LEU B1003     -76.322  -3.997  12.834  1.00 28.71           N  
-ANISOU 5036  N   LEU B1003     3720   3517   3673   -106   -462     71       N  
-ATOM   5037  CA  LEU B1003     -76.543  -4.273  14.244  1.00 29.39           C  
-ANISOU 5037  CA  LEU B1003     3849   3615   3703   -117   -498     82       C  
-ATOM   5038  C   LEU B1003     -77.267  -5.594  14.400  1.00 30.04           C  
-ANISOU 5038  C   LEU B1003     3985   3698   3733   -151   -514    125       C  
-ATOM   5039  O   LEU B1003     -78.241  -5.880  13.683  1.00 28.91           O  
-ANISOU 5039  O   LEU B1003     3840   3576   3570   -180   -477    150       O  
-ATOM   5040  CB  LEU B1003     -77.364  -3.180  14.891  1.00 29.92           C  
-ANISOU 5040  CB  LEU B1003     3907   3729   3732   -125   -461     76       C  
-ATOM   5041  CG  LEU B1003     -76.680  -1.889  15.318  1.00 31.01           C  
-ANISOU 5041  CG  LEU B1003     4016   3863   3903    -99   -460     32       C  
-ATOM   5042  CD1 LEU B1003     -76.141  -1.140  14.120  1.00 30.11           C  
-ANISOU 5042  CD1 LEU B1003     3846   3729   3863    -78   -430     10       C  
-ATOM   5043  CD2 LEU B1003     -77.676  -1.026  16.082  1.00 31.71           C  
-ANISOU 5043  CD2 LEU B1003     4111   3996   3941   -108   -422     28       C  
-ATOM   5044  N   LYS B1004     -76.787  -6.390  15.341  1.00 31.16           N  
-ANISOU 5044  N   LYS B1004     4173   3815   3850   -151   -571    136       N  
-ATOM   5045  CA  LYS B1004     -77.525  -7.560  15.802  1.00 33.86           C  
-ANISOU 5045  CA  LYS B1004     4577   4158   4132   -189   -589    182       C  
-ATOM   5046  C   LYS B1004     -78.303  -7.117  17.022  1.00 32.77           C  
-ANISOU 5046  C   LYS B1004     4460   4070   3919   -214   -580    195       C  
-ATOM   5047  O   LYS B1004     -77.716  -6.694  17.999  1.00 30.55           O  
-ANISOU 5047  O   LYS B1004     4191   3791   3626   -197   -612    177       O  
-ATOM   5048  CB  LYS B1004     -76.549  -8.672  16.143  1.00 38.04           C  
-ANISOU 5048  CB  LYS B1004     5149   4628   4678   -172   -659    191       C  
-ATOM   5049  CG  LYS B1004     -77.164 -10.001  16.521  1.00 40.46           C  
-ANISOU 5049  CG  LYS B1004     5525   4916   4930   -212   -683    241       C  
-ATOM   5050  CD  LYS B1004     -76.067 -11.057  16.557  1.00 44.50           C  
-ANISOU 5050  CD  LYS B1004     6072   5355   5483   -180   -749    245       C  
-ATOM   5051  CE  LYS B1004     -76.386 -12.189  17.519  1.00 51.80           C  
-ANISOU 5051  CE  LYS B1004     7078   6257   6346   -211   -797    297       C  
-ATOM   5052  NZ  LYS B1004     -75.288 -13.203  17.510  1.00 53.48           N  
-ANISOU 5052  NZ  LYS B1004     7322   6391   6608   -171   -863    303       N  
-ATOM   5053  N   LEU B1005     -79.625  -7.189  16.928  1.00 35.19           N  
-ANISOU 5053  N   LEU B1005     4771   4422   4179   -255   -533    224       N  
-ATOM   5054  CA  LEU B1005     -80.528  -6.747  17.974  1.00 36.55           C  
-ANISOU 5054  CA  LEU B1005     4958   4651   4280   -280   -507    235       C  
-ATOM   5055  C   LEU B1005     -81.344  -7.890  18.583  1.00 37.52           C  
-ANISOU 5055  C   LEU B1005     5139   4787   4330   -334   -517    288       C  
-ATOM   5056  O   LEU B1005     -81.822  -8.777  17.873  1.00 35.97           O  
-ANISOU 5056  O   LEU B1005     4953   4577   4137   -366   -513    319       O  
-ATOM   5057  CB  LEU B1005     -81.526  -5.756  17.393  1.00 39.96           C  
-ANISOU 5057  CB  LEU B1005     5330   5134   4717   -282   -434    228       C  
-ATOM   5058  CG  LEU B1005     -81.040  -4.441  16.797  1.00 39.91           C  
-ANISOU 5058  CG  LEU B1005     5266   5125   4775   -237   -407    182       C  
-ATOM   5059  CD1 LEU B1005     -82.237  -3.659  16.326  1.00 41.63           C  
-ANISOU 5059  CD1 LEU B1005     5435   5395   4987   -243   -339    190       C  
-ATOM   5060  CD2 LEU B1005     -80.292  -3.645  17.827  1.00 42.45           C  
-ANISOU 5060  CD2 LEU B1005     5597   5440   5091   -209   -428    143       C  
-ATOM   5061  N   LYS B1006     -81.488  -7.865  19.906  1.00 40.40           N  
-ANISOU 5061  N   LYS B1006     5547   5177   4627   -349   -530    298       N  
-ATOM   5062  CA  LYS B1006     -82.366  -8.757  20.611  1.00 39.07           C  
-ANISOU 5062  CA  LYS B1006     5432   5032   4380   -406   -527    349       C  
-ATOM   5063  C   LYS B1006     -83.616  -7.949  20.829  1.00 38.48           C  
-ANISOU 5063  C   LYS B1006     5319   5036   4265   -427   -450    348       C  
-ATOM   5064  O   LYS B1006     -83.553  -6.846  21.362  1.00 36.72           O  
-ANISOU 5064  O   LYS B1006     5076   4845   4033   -399   -425    310       O  
-ATOM   5065  CB  LYS B1006     -81.791  -9.154  21.995  1.00 42.65           C  
-ANISOU 5065  CB  LYS B1006     5958   5473   4774   -411   -584    363       C  
-ATOM   5066  N   PHE B1007     -84.747  -8.519  20.416  1.00 37.96           N  
-ANISOU 5066  N   PHE B1007     5244   5001   4177   -477   -414    389       N  
-ATOM   5067  CA  PHE B1007     -86.064  -7.974  20.676  1.00 39.37           C  
-ANISOU 5067  CA  PHE B1007     5385   5260   4313   -505   -341    400       C  
-ATOM   5068  C   PHE B1007     -86.597  -8.633  21.960  1.00 43.76           C  
-ANISOU 5068  C   PHE B1007     6005   5848   4775   -558   -340    439       C  
-ATOM   5069  O   PHE B1007     -86.751  -9.847  21.992  1.00 41.79           O  
-ANISOU 5069  O   PHE B1007     5805   5575   4500   -608   -371    487       O  
-ATOM   5070  CB  PHE B1007     -87.003  -8.326  19.515  1.00 39.62           C  
-ANISOU 5070  CB  PHE B1007     5369   5312   4372   -538   -309    428       C  
-ATOM   5071  CG  PHE B1007     -86.716  -7.594  18.231  1.00 37.70           C  
-ANISOU 5071  CG  PHE B1007     5060   5054   4209   -493   -298    396       C  
-ATOM   5072  CD1 PHE B1007     -85.540  -7.813  17.525  1.00 36.54           C  
-ANISOU 5072  CD1 PHE B1007     4926   4836   4122   -460   -346    373       C  
-ATOM   5073  CD2 PHE B1007     -87.667  -6.725  17.694  1.00 37.99           C  
-ANISOU 5073  CD2 PHE B1007     5021   5150   4263   -486   -237    393       C  
-ATOM   5074  CE1 PHE B1007     -85.293  -7.140  16.336  1.00 37.52           C  
-ANISOU 5074  CE1 PHE B1007     4993   4950   4313   -424   -331    347       C  
-ATOM   5075  CE2 PHE B1007     -87.423  -6.045  16.508  1.00 37.12           C  
-ANISOU 5075  CE2 PHE B1007     4857   5026   4222   -447   -228    370       C  
-ATOM   5076  CZ  PHE B1007     -86.233  -6.255  15.828  1.00 35.06           C  
-ANISOU 5076  CZ  PHE B1007     4614   4695   4012   -419   -274    347       C  
-ATOM   5077  N   ASN B1008     -86.837  -7.849  23.018  1.00 45.86           N  
-ANISOU 5077  N   ASN B1008     6276   6164   4987   -548   -305    418       N  
-ATOM   5078  CA  ASN B1008     -87.407  -8.366  24.265  1.00 46.81           C  
-ANISOU 5078  CA  ASN B1008     6454   6324   5006   -601   -293    453       C  
-ATOM   5079  C   ASN B1008     -88.882  -8.055  24.293  1.00 47.09           C  
-ANISOU 5079  C   ASN B1008     6437   6446   5010   -636   -204    470       C  
-ATOM   5080  O   ASN B1008     -89.283  -6.933  24.609  1.00 44.48           O  
-ANISOU 5080  O   ASN B1008     6063   6166   4672   -604   -144    431       O  
-ATOM   5081  CB  ASN B1008     -86.712  -7.750  25.485  1.00 49.67           C  
-ANISOU 5081  CB  ASN B1008     6863   6690   5317   -573   -312    417       C  
-ATOM   5082  CG  ASN B1008     -85.265  -8.210  25.624  1.00 49.47           C  
-ANISOU 5082  CG  ASN B1008     6894   6587   5315   -546   -409    411       C  
-ATOM   5083  OD1 ASN B1008     -84.970  -9.396  25.509  1.00 49.56           O  
-ANISOU 5083  OD1 ASN B1008     6953   6552   5325   -573   -464    458       O  
-ATOM   5084  ND2 ASN B1008     -84.364  -7.268  25.808  1.00 48.75           N  
-ANISOU 5084  ND2 ASN B1008     6790   6479   5253   -491   -431    354       N  
-ATOM   5085  N   PHE B1009     -89.683  -9.044  23.921  1.00 49.11           N  
-ANISOU 5085  N   PHE B1009     6692   6714   5252   -700   -196    526       N  
-ATOM   5086  CA  PHE B1009     -91.131  -8.854  23.813  1.00 52.89           C  
-ANISOU 5086  CA  PHE B1009     7106   7277   5711   -739   -115    549       C  
-ATOM   5087  C   PHE B1009     -91.763  -8.683  25.205  1.00 58.80           C  
-ANISOU 5087  C   PHE B1009     7884   8096   6362   -769    -61    557       C  
-ATOM   5088  O   PHE B1009     -91.372  -9.350  26.158  1.00 56.56           O  
-ANISOU 5088  O   PHE B1009     7688   7793   6008   -802    -96    581       O  
-ATOM   5089  CB  PHE B1009     -91.732  -9.992  23.002  1.00 51.67           C  
-ANISOU 5089  CB  PHE B1009     6946   7114   5572   -807   -130    605       C  
-ATOM   5090  CG  PHE B1009     -91.365  -9.926  21.539  1.00 54.36           C  
-ANISOU 5090  CG  PHE B1009     7241   7408   6004   -776   -159    588       C  
-ATOM   5091  CD1 PHE B1009     -90.249 -10.586  21.054  1.00 55.49           C  
-ANISOU 5091  CD1 PHE B1009     7437   7459   6185   -761   -235    583       C  
-ATOM   5092  CD2 PHE B1009     -92.118  -9.160  20.650  1.00 55.42           C  
-ANISOU 5092  CD2 PHE B1009     7278   7593   6187   -757   -110    576       C  
-ATOM   5093  CE1 PHE B1009     -89.902 -10.513  19.702  1.00 57.48           C  
-ANISOU 5093  CE1 PHE B1009     7651   7673   6516   -733   -255    565       C  
-ATOM   5094  CE2 PHE B1009     -91.776  -9.080  19.299  1.00 58.00           C  
-ANISOU 5094  CE2 PHE B1009     7568   7880   6589   -732   -137    562       C  
-ATOM   5095  CZ  PHE B1009     -90.659  -9.757  18.821  1.00 57.35           C  
-ANISOU 5095  CZ  PHE B1009     7544   7709   6539   -721   -207    554       C  
-ATOM   5096  N   LYS B1010     -92.700  -7.746  25.317  1.00 62.00           N  
-ANISOU 5096  N   LYS B1010     8215   8579   6763   -753     24    536       N  
-ATOM   5097  CA  LYS B1010     -93.217  -7.301  26.617  1.00 63.75           C  
-ANISOU 5097  CA  LYS B1010     8456   8869   6897   -762     88    524       C  
-ATOM   5098  C   LYS B1010     -94.647  -7.809  26.803  1.00 64.29           C  
-ANISOU 5098  C   LYS B1010     8486   9022   6921   -836    159    577       C  
-ATOM   5099  O   LYS B1010     -95.151  -8.524  25.940  1.00 58.31           O  
-ANISOU 5099  O   LYS B1010     7692   8264   6201   -881    147    622       O  
-ATOM   5100  CB  LYS B1010     -93.139  -5.771  26.722  1.00 61.39           C  
-ANISOU 5100  CB  LYS B1010     8107   8592   6628   -680    139    451       C  
-TER    5101      LYS B1010                                                      
-ATOM   5102  N   LYS C 662     -99.899  44.477 -47.591  1.00 70.03           N  
-ANISOU 5102  N   LYS C 662     7775  11209   7625   1641    308   1168       N  
-ATOM   5103  CA  LYS C 662     -99.204  45.194 -46.461  1.00 72.25           C  
-ANISOU 5103  CA  LYS C 662     8178  11279   7995   1639    372   1190       C  
-ATOM   5104  C   LYS C 662     -99.310  44.419 -45.145  1.00 71.43           C  
-ANISOU 5104  C   LYS C 662     8068  11112   7962   1514    346   1122       C  
-ATOM   5105  O   LYS C 662    -100.357  43.840 -44.844  1.00 74.87           O  
-ANISOU 5105  O   LYS C 662     8404  11675   8367   1487    308   1097       O  
-ATOM   5106  CB  LYS C 662     -99.753  46.614 -46.264  1.00 75.55           C  
-ANISOU 5106  CB  LYS C 662     8632  11691   8382   1801    451   1292       C  
-ATOM   5107  N   SER C 663     -98.226  44.397 -44.371  1.00 66.58           N  
-ANISOU 5107  N   SER C 663     7555  10306   7437   1437    366   1092       N  
-ATOM   5108  CA  SER C 663     -98.185  43.594 -43.140  1.00 64.21           C  
-ANISOU 5108  CA  SER C 663     7257   9936   7204   1316    341   1025       C  
-ATOM   5109  C   SER C 663     -98.924  44.283 -42.007  1.00 61.97           C  
-ANISOU 5109  C   SER C 663     6983   9630   6932   1372    385   1064       C  
-ATOM   5110  O   SER C 663     -98.885  45.511 -41.882  1.00 58.79           O  
-ANISOU 5110  O   SER C 663     6646   9167   6526   1483    452   1134       O  
-ATOM   5111  CB  SER C 663     -96.745  43.309 -42.701  1.00 66.67           C  
-ANISOU 5111  CB  SER C 663     7669  10063   7602   1219    345    979       C  
-ATOM   5112  N   LYS C 664     -99.578  43.485 -41.171  1.00 58.00           N  
-ANISOU 5112  N   LYS C 664     6421   9172   6445   1295    352   1018       N  
-ATOM   5113  CA  LYS C 664    -100.159  43.996 -39.945  1.00 61.65           C  
-ANISOU 5113  CA  LYS C 664     6900   9596   6929   1329    391   1043       C  
-ATOM   5114  C   LYS C 664     -99.140  44.082 -38.792  1.00 59.28           C  
-ANISOU 5114  C   LYS C 664     6711   9094   6720   1261    417   1014       C  
-ATOM   5115  O   LYS C 664     -99.511  44.505 -37.703  1.00 59.73           O  
-ANISOU 5115  O   LYS C 664     6792   9103   6798   1284    451   1029       O  
-ATOM   5116  CB  LYS C 664    -101.369  43.136 -39.530  1.00 68.78           C  
-ANISOU 5116  CB  LYS C 664     7685  10643   7805   1279    348   1011       C  
-ATOM   5117  N   LEU C 665     -97.887  43.662 -39.016  1.00 53.79           N  
-ANISOU 5117  N   LEU C 665     6077   8289   6072   1180    401    970       N  
-ATOM   5118  CA  LEU C 665     -96.841  43.720 -37.986  1.00 47.92           C  
-ANISOU 5118  CA  LEU C 665     5433   7365   5409   1115    422    938       C  
-ATOM   5119  C   LEU C 665     -96.329  45.134 -37.772  1.00 47.89           C  
-ANISOU 5119  C   LEU C 665     5530   7241   5423   1205    496    994       C  
-ATOM   5120  O   LEU C 665     -96.189  45.899 -38.720  1.00 49.82           O  
-ANISOU 5120  O   LEU C 665     5796   7499   5634   1290    527   1045       O  
-ATOM   5121  CB  LEU C 665     -95.637  42.862 -38.375  1.00 45.87           C  
-ANISOU 5121  CB  LEU C 665     5203   7037   5188   1009    382    877       C  
-ATOM   5122  CG  LEU C 665     -95.862  41.361 -38.564  1.00 44.35           C  
-ANISOU 5122  CG  LEU C 665     4935   6925   4991    900    312    810       C  
-ATOM   5123  CD1 LEU C 665     -94.654  40.725 -39.234  1.00 43.70           C  
-ANISOU 5123  CD1 LEU C 665     4887   6783   4932    829    283    765       C  
-ATOM   5124  CD2 LEU C 665     -96.164  40.683 -37.250  1.00 44.52           C  
-ANISOU 5124  CD2 LEU C 665     4949   6913   5053    823    300    769       C  
-ATOM   5125  N   PRO C 666     -96.009  45.477 -36.527  1.00 46.70           N  
-ANISOU 5125  N   PRO C 666     5450   6969   5327   1183    528    982       N  
-ATOM   5126  CA  PRO C 666     -95.372  46.757 -36.246  1.00 47.56           C  
-ANISOU 5126  CA  PRO C 666     5666   6942   5462   1246    600   1020       C  
-ATOM   5127  C   PRO C 666     -94.077  46.951 -37.045  1.00 51.01           C  
-ANISOU 5127  C   PRO C 666     6165   7293   5923   1221    609   1013       C  
-ATOM   5128  O   PRO C 666     -93.384  45.977 -37.362  1.00 53.48           O  
-ANISOU 5128  O   PRO C 666     6459   7604   6256   1126    556    959       O  
-ATOM   5129  CB  PRO C 666     -95.048  46.669 -34.749  1.00 46.09           C  
-ANISOU 5129  CB  PRO C 666     5531   6645   5335   1182    609    977       C  
-ATOM   5130  CG  PRO C 666     -95.946  45.606 -34.208  1.00 44.93           C  
-ANISOU 5130  CG  PRO C 666     5295   6599   5176   1129    558    945       C  
-ATOM   5131  CD  PRO C 666     -96.166  44.642 -35.322  1.00 44.62           C  
-ANISOU 5131  CD  PRO C 666     5169   6683   5101   1092    499    927       C  
-ATOM   5132  N   LYS C 667     -93.759  48.197 -37.369  1.00 53.09           N  
-ANISOU 5132  N   LYS C 667     6504   7484   6184   1307    678   1068       N  
-ATOM   5133  CA  LYS C 667     -92.574  48.496 -38.171  1.00 55.34           C  
-ANISOU 5133  CA  LYS C 667     6848   7690   6488   1291    696   1070       C  
-ATOM   5134  C   LYS C 667     -91.305  47.855 -37.566  1.00 53.55           C  
-ANISOU 5134  C   LYS C 667     6663   7351   6332   1160    668    994       C  
-ATOM   5135  O   LYS C 667     -90.564  47.193 -38.279  1.00 52.98           O  
-ANISOU 5135  O   LYS C 667     6575   7289   6266   1102    630    964       O  
-ATOM   5136  CB  LYS C 667     -92.385  50.017 -38.331  1.00 52.16           C  
-ANISOU 5136  CB  LYS C 667     6538   7195   6084   1393    790   1138       C  
-ATOM   5137  N   PRO C 668     -91.067  48.053 -36.257  1.00 48.75           N  
-ANISOU 5137  N   PRO C 668     6106   6645   5772   1120    686    963       N  
-ATOM   5138  CA  PRO C 668     -89.884  47.489 -35.622  1.00 45.58           C  
-ANISOU 5138  CA  PRO C 668     5741   6147   5431   1006    661    893       C  
-ATOM   5139  C   PRO C 668     -89.730  46.000 -35.863  1.00 39.82           C  
-ANISOU 5139  C   PRO C 668     4941   5489   4702    916    580    839       C  
-ATOM   5140  O   PRO C 668     -88.627  45.523 -36.073  1.00 38.91           O  
-ANISOU 5140  O   PRO C 668     4844   5323   4616    844    557    798       O  
-ATOM   5141  CB  PRO C 668     -90.120  47.769 -34.142  1.00 50.31           C  
-ANISOU 5141  CB  PRO C 668     6376   6680   6060    993    681    872       C  
-ATOM   5142  CG  PRO C 668     -91.013  48.998 -34.122  1.00 49.58           C  
-ANISOU 5142  CG  PRO C 668     6312   6590   5936   1114    750    942       C  
-ATOM   5143  CD  PRO C 668     -91.915  48.798 -35.298  1.00 50.66           C  
-ANISOU 5143  CD  PRO C 668     6371   6869   6009   1185    731    991       C  
-ATOM   5144  N   VAL C 669     -90.833  45.285 -35.866  1.00 38.09           N  
-ANISOU 5144  N   VAL C 669     4639   5387   4446    923    540    838       N  
-ATOM   5145  CA  VAL C 669     -90.811  43.852 -36.079  1.00 37.25           C  
-ANISOU 5145  CA  VAL C 669     4468   5348   4337    837    469    786       C  
-ATOM   5146  C   VAL C 669     -90.459  43.563 -37.527  1.00 39.98           C  
-ANISOU 5146  C   VAL C 669     4786   5751   4652    842    446    792       C  
-ATOM   5147  O   VAL C 669     -89.652  42.678 -37.831  1.00 41.69           O  
-ANISOU 5147  O   VAL C 669     5000   5953   4888    765    406    745       O  
-ATOM   5148  CB  VAL C 669     -92.164  43.203 -35.685  1.00 35.53           C  
-ANISOU 5148  CB  VAL C 669     4167   5244   4087    838    438    783       C  
-ATOM   5149  CG1 VAL C 669     -92.160  41.713 -35.942  1.00 33.71           C  
-ANISOU 5149  CG1 VAL C 669     3877   5076   3856    744    371    726       C  
-ATOM   5150  CG2 VAL C 669     -92.469  43.461 -34.218  1.00 34.42           C  
-ANISOU 5150  CG2 VAL C 669     4057   5044   3977    832    461    776       C  
-ATOM   5151  N   GLN C 670     -91.089  44.299 -38.427  1.00 42.66           N  
-ANISOU 5151  N   GLN C 670     5105   6162   4940    940    473    854       N  
-ATOM   5152  CA  GLN C 670     -90.819  44.168 -39.845  1.00 42.15           C  
-ANISOU 5152  CA  GLN C 670     5016   6160   4838    962    458    869       C  
-ATOM   5153  C   GLN C 670     -89.348  44.390 -40.118  1.00 39.64           C  
-ANISOU 5153  C   GLN C 670     4772   5726   4562    924    477    854       C  
-ATOM   5154  O   GLN C 670     -88.728  43.613 -40.835  1.00 40.04           O  
-ANISOU 5154  O   GLN C 670     4804   5798   4610    873    438    821       O  
-ATOM   5155  CB  GLN C 670     -91.684  45.154 -40.659  1.00 46.79           C  
-ANISOU 5155  CB  GLN C 670     5585   6831   5362   1092    498    949       C  
-ATOM   5156  CG  GLN C 670     -93.163  44.757 -40.754  1.00 47.43           C  
-ANISOU 5156  CG  GLN C 670     5566   7072   5384   1130    466    961       C  
-ATOM   5157  CD  GLN C 670     -94.057  45.696 -41.566  1.00 51.20           C  
-ANISOU 5157  CD  GLN C 670     6015   7649   5788   1269    503   1043       C  
-ATOM   5158  OE1 GLN C 670     -95.286  45.724 -41.373  1.00 52.10           O  
-ANISOU 5158  OE1 GLN C 670     6062   7875   5858   1321    497   1066       O  
-ATOM   5159  NE2 GLN C 670     -93.465  46.459 -42.467  1.00 52.97           N  
-ANISOU 5159  NE2 GLN C 670     6290   7840   5998   1334    544   1089       N  
-ATOM   5160  N   ASP C 671     -88.790  45.439 -39.537  1.00 38.68           N  
-ANISOU 5160  N   ASP C 671     4733   5485   4480    947    538    876       N  
-ATOM   5161  CA  ASP C 671     -87.359  45.715 -39.666  1.00 39.21           C  
-ANISOU 5161  CA  ASP C 671     4869   5437   4591    903    561    859       C  
-ATOM   5162  C   ASP C 671     -86.469  44.585 -39.111  1.00 38.54           C  
-ANISOU 5162  C   ASP C 671     4780   5311   4551    785    508    780       C  
-ATOM   5163  O   ASP C 671     -85.443  44.268 -39.719  1.00 34.57           O  
-ANISOU 5163  O   ASP C 671     4291   4782   4062    744    497    760       O  
-ATOM   5164  CB  ASP C 671     -87.005  47.051 -39.005  1.00 44.70           C  
-ANISOU 5164  CB  ASP C 671     5653   6008   5321    939    639    888       C  
-ATOM   5165  CG  ASP C 671     -87.520  48.275 -39.809  1.00 53.02           C  
-ANISOU 5165  CG  ASP C 671     6734   7077   6334   1061    706    973       C  
-ATOM   5166  OD1 ASP C 671     -88.082  48.087 -40.918  1.00 53.98           O  
-ANISOU 5166  OD1 ASP C 671     6801   7311   6397   1119    689   1010       O  
-ATOM   5167  OD2 ASP C 671     -87.391  49.422 -39.312  1.00 59.22           O  
-ANISOU 5167  OD2 ASP C 671     7596   7763   7142   1102    778   1003       O  
-ATOM   5168  N   LEU C 672     -86.880  43.964 -37.995  1.00 35.39           N  
-ANISOU 5168  N   LEU C 672     4363   4913   4172    737    479    741       N  
-ATOM   5169  CA  LEU C 672     -86.161  42.833 -37.450  1.00 33.81           C  
-ANISOU 5169  CA  LEU C 672     4157   4683   4006    637    430    673       C  
-ATOM   5170  C   LEU C 672     -86.164  41.666 -38.430  1.00 34.56           C  
-ANISOU 5170  C   LEU C 672     4194   4865   4072    603    374    648       C  
-ATOM   5171  O   LEU C 672     -85.134  41.030 -38.653  1.00 32.86           O  
-ANISOU 5171  O   LEU C 672     3992   4616   3878    544    350    609       O  
-ATOM   5172  CB  LEU C 672     -86.768  42.412 -36.107  1.00 33.51           C  
-ANISOU 5172  CB  LEU C 672     4107   4638   3985    605    414    645       C  
-ATOM   5173  CG  LEU C 672     -86.190  41.178 -35.415  1.00 32.33           C  
-ANISOU 5173  CG  LEU C 672     3952   4465   3867    511    367    580       C  
-ATOM   5174  CD1 LEU C 672     -84.767  41.442 -34.953  1.00 33.08           C  
-ANISOU 5174  CD1 LEU C 672     4110   4450   4008    468    382    551       C  
-ATOM   5175  CD2 LEU C 672     -87.052  40.776 -34.239  1.00 32.66           C  
-ANISOU 5175  CD2 LEU C 672     3973   4522   3913    494    356    565       C  
-ATOM   5176  N   ILE C 673     -87.323  41.370 -39.006  1.00 36.86           N  
-ANISOU 5176  N   ILE C 673     4420   5273   4313    639    352    667       N  
-ATOM   5177  CA  ILE C 673     -87.433  40.267 -39.962  1.00 37.40           C  
-ANISOU 5177  CA  ILE C 673     4431   5432   4348    605    299    638       C  
-ATOM   5178  C   ILE C 673     -86.526  40.477 -41.162  1.00 36.92           C  
-ANISOU 5178  C   ILE C 673     4390   5364   4275    622    306    650       C  
-ATOM   5179  O   ILE C 673     -85.879  39.548 -41.643  1.00 36.57           O  
-ANISOU 5179  O   ILE C 673     4336   5325   4232    566    269    607       O  
-ATOM   5180  CB  ILE C 673     -88.896  40.067 -40.443  1.00 39.70           C  
-ANISOU 5180  CB  ILE C 673     4641   5863   4579    647    278    658       C  
-ATOM   5181  CG1 ILE C 673     -89.817  39.760 -39.267  1.00 40.69           C  
-ANISOU 5181  CG1 ILE C 673     4739   6004   4716    623    270    644       C  
-ATOM   5182  CG2 ILE C 673     -88.988  38.937 -41.463  1.00 38.79           C  
-ANISOU 5182  CG2 ILE C 673     4468   5842   4427    605    224    620       C  
-ATOM   5183  CD1 ILE C 673     -89.259  38.732 -38.312  1.00 43.20           C  
-ANISOU 5183  CD1 ILE C 673     5077   6254   5083    523    242    581       C  
-ATOM   5184  N   LYS C 674     -86.490  41.693 -41.675  1.00 40.08           N  
-ANISOU 5184  N   LYS C 674     4819   5750   4660    704    358    711       N  
-ATOM   5185  CA  LYS C 674     -85.616  41.998 -42.826  1.00 40.60           C  
-ANISOU 5185  CA  LYS C 674     4908   5805   4713    726    374    730       C  
-ATOM   5186  C   LYS C 674     -84.148  41.805 -42.469  1.00 38.72           C  
-ANISOU 5186  C   LYS C 674     4724   5455   4531    655    379    691       C  
-ATOM   5187  O   LYS C 674     -83.360  41.209 -43.217  1.00 39.13           O  
-ANISOU 5187  O   LYS C 674     4773   5517   4580    623    356    667       O  
-ATOM   5188  CB  LYS C 674     -85.823  43.439 -43.287  1.00 42.08           C  
-ANISOU 5188  CB  LYS C 674     5130   5979   4879    828    442    808       C  
-ATOM   5189  CG  LYS C 674     -87.146  43.682 -43.986  1.00 48.49           C  
-ANISOU 5189  CG  LYS C 674     5883   6922   5620    918    440    857       C  
-ATOM   5190  CD  LYS C 674     -87.257  45.145 -44.420  1.00 52.85           C  
-ANISOU 5190  CD  LYS C 674     6483   7447   6153   1028    516    941       C  
-ATOM   5191  CE  LYS C 674     -88.680  45.500 -44.786  1.00 56.99           C  
-ANISOU 5191  CE  LYS C 674     6951   8096   6608   1128    521    994       C  
-ATOM   5192  NZ  LYS C 674     -88.895  46.975 -44.816  1.00 61.11           N  
-ANISOU 5192  NZ  LYS C 674     7531   8567   7119   1238    605   1076       N  
-ATOM   5193  N   MET C 675     -83.803  42.344 -41.319  1.00 35.66           N  
-ANISOU 5193  N   MET C 675     4386   4969   4194    635    409    685       N  
-ATOM   5194  CA  MET C 675     -82.476  42.248 -40.782  1.00 37.32           C  
-ANISOU 5194  CA  MET C 675     4643   5079   4457    569    415    646       C  
-ATOM   5195  C   MET C 675     -82.002  40.781 -40.681  1.00 35.98           C  
-ANISOU 5195  C   MET C 675     4445   4931   4296    489    352    581       C  
-ATOM   5196  O   MET C 675     -80.890  40.435 -41.135  1.00 33.52           O  
-ANISOU 5196  O   MET C 675     4147   4592   3997    454    344    559       O  
-ATOM   5197  CB  MET C 675     -82.505  42.899 -39.417  1.00 38.34           C  
-ANISOU 5197  CB  MET C 675     4815   5125   4628    559    447    642       C  
-ATOM   5198  CG  MET C 675     -81.176  43.220 -38.830  1.00 42.44           C  
-ANISOU 5198  CG  MET C 675     5389   5538   5198    505    469    612       C  
-ATOM   5199  SD  MET C 675     -81.527  43.961 -37.223  1.00 45.31           S  
-ANISOU 5199  SD  MET C 675     5795   5825   5597    503    502    605       S  
-ATOM   5200  CE  MET C 675     -79.868  43.990 -36.601  1.00 40.42           C  
-ANISOU 5200  CE  MET C 675     5219   5107   5030    422    509    552       C  
-ATOM   5201  N   ILE C 676     -82.860  39.911 -40.146  1.00 34.06           N  
-ANISOU 5201  N   ILE C 676     4161   4736   4043    463    311    554       N  
-ATOM   5202  CA  ILE C 676     -82.423  38.533 -39.877  1.00 33.51           C  
-ANISOU 5202  CA  ILE C 676     4076   4668   3986    388    260    492       C  
-ATOM   5203  C   ILE C 676     -82.476  37.622 -41.086  1.00 32.36           C  
-ANISOU 5203  C   ILE C 676     3891   4602   3801    378    222    476       C  
-ATOM   5204  O   ILE C 676     -81.727  36.640 -41.158  1.00 30.71           O  
-ANISOU 5204  O   ILE C 676     3687   4377   3604    325    192    430       O  
-ATOM   5205  CB  ILE C 676     -83.072  37.907 -38.640  1.00 34.69           C  
-ANISOU 5205  CB  ILE C 676     4214   4813   4153    349    239    463       C  
-ATOM   5206  CG1 ILE C 676     -84.534  37.612 -38.816  1.00 37.10           C  
-ANISOU 5206  CG1 ILE C 676     4463   5215   4420    370    221    475       C  
-ATOM   5207  CG2 ILE C 676     -82.875  38.807 -37.425  1.00 36.12           C  
-ANISOU 5207  CG2 ILE C 676     4440   4912   4372    356    277    473       C  
-ATOM   5208  CD1 ILE C 676     -85.102  37.101 -37.510  1.00 37.59           C  
-ANISOU 5208  CD1 ILE C 676     4519   5262   4503    331    209    450       C  
-ATOM   5209  N   PHE C 677     -83.299  37.970 -42.077  1.00 32.46           N  
-ANISOU 5209  N   PHE C 677     3868   4702   3765    436    225    512       N  
-ATOM   5210  CA  PHE C 677     -83.352  37.200 -43.333  1.00 31.12           C  
-ANISOU 5210  CA  PHE C 677     3659   4615   3549    432    190    496       C  
-ATOM   5211  C   PHE C 677     -82.590  37.857 -44.506  1.00 32.32           C  
-ANISOU 5211  C   PHE C 677     3830   4768   3681    480    216    531       C  
-ATOM   5212  O   PHE C 677     -82.780  37.494 -45.650  1.00 32.42           O  
-ANISOU 5212  O   PHE C 677     3811   4862   3646    500    196    531       O  
-ATOM   5213  CB  PHE C 677     -84.791  36.921 -43.715  1.00 30.49           C  
-ANISOU 5213  CB  PHE C 677     3513   4654   3417    455    165    502       C  
-ATOM   5214  CG  PHE C 677     -85.422  35.795 -42.938  1.00 29.65           C  
-ANISOU 5214  CG  PHE C 677     3378   4567   3321    386    126    450       C  
-ATOM   5215  CD1 PHE C 677     -85.008  34.480 -43.127  1.00 29.86           C  
-ANISOU 5215  CD1 PHE C 677     3401   4593   3351    314     87    389       C  
-ATOM   5216  CD2 PHE C 677     -86.446  36.047 -42.057  1.00 28.45           C  
-ANISOU 5216  CD2 PHE C 677     3203   4433   3173    395    133    465       C  
-ATOM   5217  CE1 PHE C 677     -85.592  33.433 -42.422  1.00 30.50           C  
-ANISOU 5217  CE1 PHE C 677     3462   4685   3443    248     58    344       C  
-ATOM   5218  CE2 PHE C 677     -87.044  35.011 -41.355  1.00 29.92           C  
-ANISOU 5218  CE2 PHE C 677     3363   4637   3369    328    103    420       C  
-ATOM   5219  CZ  PHE C 677     -86.629  33.696 -41.547  1.00 29.52           C  
-ANISOU 5219  CZ  PHE C 677     3311   4581   3323    253     66    359       C  
-ATOM   5220  N   ASP C 678     -81.652  38.744 -44.195  1.00 34.68           N  
-ANISOU 5220  N   ASP C 678     4184   4974   4020    491    262    555       N  
-ATOM   5221  CA  ASP C 678     -80.882  39.466 -45.202  1.00 34.22           C  
-ANISOU 5221  CA  ASP C 678     4149   4902   3949    533    298    593       C  
-ATOM   5222  C   ASP C 678     -79.861  38.577 -45.902  1.00 32.27           C  
-ANISOU 5222  C   ASP C 678     3902   4660   3699    492    270    554       C  
-ATOM   5223  O   ASP C 678     -78.795  38.247 -45.352  1.00 32.52           O  
-ANISOU 5223  O   ASP C 678     3963   4620   3775    437    268    519       O  
-ATOM   5224  CB  ASP C 678     -80.196  40.663 -44.547  1.00 38.79           C  
-ANISOU 5224  CB  ASP C 678     4788   5374   4575    543    359    622       C  
-ATOM   5225  CG  ASP C 678     -79.663  41.640 -45.570  1.00 43.92           C  
-ANISOU 5225  CG  ASP C 678     5465   6011   5210    598    411    677       C  
-ATOM   5226  OD1 ASP C 678     -79.145  41.229 -46.625  1.00 44.57           O  
-ANISOU 5226  OD1 ASP C 678     5534   6134   5266    601    398    674       O  
-ATOM   5227  OD2 ASP C 678     -79.734  42.841 -45.309  1.00 52.79           O  
-ANISOU 5227  OD2 ASP C 678     6629   7080   6349    639    470    723       O  
-ATOM   5228  N   VAL C 679     -80.172  38.213 -47.140  1.00 31.77           N  
-ANISOU 5228  N   VAL C 679     3804   4688   3579    522    250    560       N  
-ATOM   5229  CA  VAL C 679     -79.343  37.287 -47.958  1.00 31.66           C  
-ANISOU 5229  CA  VAL C 679     3786   4695   3550    492    220    522       C  
-ATOM   5230  C   VAL C 679     -77.979  37.879 -48.279  1.00 31.93           C  
-ANISOU 5230  C   VAL C 679     3862   4659   3609    497    262    543       C  
-ATOM   5231  O   VAL C 679     -76.947  37.190 -48.275  1.00 31.83           O  
-ANISOU 5231  O   VAL C 679     3862   4614   3617    451    247    503       O  
-ATOM   5232  CB  VAL C 679     -80.080  36.937 -49.257  1.00 32.11           C  
-ANISOU 5232  CB  VAL C 679     3795   4872   3532    533    194    529       C  
-ATOM   5233  CG1 VAL C 679     -79.202  36.160 -50.219  1.00 32.66           C  
-ANISOU 5233  CG1 VAL C 679     3867   4962   3580    515    174    497       C  
-ATOM   5234  CG2 VAL C 679     -81.332  36.152 -48.922  1.00 32.06           C  
-ANISOU 5234  CG2 VAL C 679     3741   4938   3503    508    148    493       C  
-ATOM   5235  N   GLU C 680     -77.952  39.173 -48.505  1.00 31.12           N  
-ANISOU 5235  N   GLU C 680     3784   4532   3508    553    318    605       N  
-ATOM   5236  CA  GLU C 680     -76.682  39.843 -48.745  1.00 33.22           C  
-ANISOU 5236  CA  GLU C 680     4091   4727   3803    552    366    627       C  
-ATOM   5237  C   GLU C 680     -75.749  39.771 -47.514  1.00 28.44           C  
-ANISOU 5237  C   GLU C 680     3517   4023   3267    480    372    588       C  
-ATOM   5238  O   GLU C 680     -74.552  39.615 -47.658  1.00 27.67           O  
-ANISOU 5238  O   GLU C 680     3433   3889   3190    448    380    570       O  
-ATOM   5239  CB  GLU C 680     -76.949  41.314 -49.120  1.00 32.72           C  
-ANISOU 5239  CB  GLU C 680     4055   4645   3731    625    435    704       C  
-ATOM   5240  CG  GLU C 680     -75.662  42.098 -49.360  1.00 37.37           C  
-ANISOU 5240  CG  GLU C 680     4690   5156   4353    617    495    729       C  
-ATOM   5241  CD  GLU C 680     -75.858  43.505 -49.930  1.00 42.43           C  
-ANISOU 5241  CD  GLU C 680     5366   5776   4981    693    571    810       C  
-ATOM   5242  OE1 GLU C 680     -76.803  43.730 -50.708  1.00 44.17           O  
-ANISOU 5242  OE1 GLU C 680     5567   6074   5143    771    574    855       O  
-ATOM   5243  OE2 GLU C 680     -75.042  44.387 -49.603  1.00 44.51           O  
-ANISOU 5243  OE2 GLU C 680     5678   5944   5290    674    632    828       O  
-ATOM   5244  N   SER C 681     -76.307  39.942 -46.319  1.00 28.61           N  
-ANISOU 5244  N   SER C 681     3545   4006   3318    461    369    576       N  
-ATOM   5245  CA  SER C 681     -75.534  39.769 -45.097  1.00 29.65           C  
-ANISOU 5245  CA  SER C 681     3700   4060   3506    396    366    534       C  
-ATOM   5246  C   SER C 681     -74.986  38.352 -44.969  1.00 27.43           C  
-ANISOU 5246  C   SER C 681     3399   3796   3226    342    311    473       C  
-ATOM   5247  O   SER C 681     -73.854  38.174 -44.519  1.00 29.37           O  
-ANISOU 5247  O   SER C 681     3661   3993   3505    300    314    445       O  
-ATOM   5248  CB  SER C 681     -76.345  40.076 -43.853  1.00 31.31           C  
-ANISOU 5248  CB  SER C 681     3918   4239   3740    389    368    530       C  
-ATOM   5249  OG  SER C 681     -76.591  41.465 -43.775  1.00 33.36           O  
-ANISOU 5249  OG  SER C 681     4210   4456   4009    433    429    582       O  
-ATOM   5250  N   MET C 682     -75.777  37.360 -45.377  1.00 25.57           N  
-ANISOU 5250  N   MET C 682     3131   3633   2953    345    264    452       N  
-ATOM   5251  CA  MET C 682     -75.308  35.966 -45.408  1.00 25.12           C  
-ANISOU 5251  CA  MET C 682     3063   3591   2892    301    217    396       C  
-ATOM   5252  C   MET C 682     -74.072  35.809 -46.304  1.00 24.27           C  
-ANISOU 5252  C   MET C 682     2963   3483   2777    302    226    393       C  
-ATOM   5253  O   MET C 682     -73.049  35.272 -45.888  1.00 22.35           O  
-ANISOU 5253  O   MET C 682     2732   3203   2558    265    218    359       O  
-ATOM   5254  CB  MET C 682     -76.423  35.023 -45.861  1.00 24.04           C  
-ANISOU 5254  CB  MET C 682     2890   3533   2710    302    173    375       C  
-ATOM   5255  CG  MET C 682     -77.615  34.967 -44.915  1.00 25.49           C  
-ANISOU 5255  CG  MET C 682     3060   3724   2903    291    160    370       C  
-ATOM   5256  SD  MET C 682     -78.932  33.975 -45.658  1.00 28.91           S  
-ANISOU 5256  SD  MET C 682     3442   4265   3278    290    114    346       S  
-ATOM   5257  CE  MET C 682     -80.394  34.713 -44.905  1.00 29.72           C  
-ANISOU 5257  CE  MET C 682     3520   4394   3379    315    125    380       C  
-ATOM   5258  N   LYS C 683     -74.162  36.318 -47.525  1.00 25.11           N  
-ANISOU 5258  N   LYS C 683     3061   3635   2845    351    247    433       N  
-ATOM   5259  CA  LYS C 683     -73.031  36.267 -48.454  1.00 26.75           C  
-ANISOU 5259  CA  LYS C 683     3275   3847   3042    359    261    437       C  
-ATOM   5260  C   LYS C 683     -71.814  37.046 -47.962  1.00 25.34           C  
-ANISOU 5260  C   LYS C 683     3123   3593   2912    338    305    449       C  
-ATOM   5261  O   LYS C 683     -70.674  36.594 -48.093  1.00 24.59           O  
-ANISOU 5261  O   LYS C 683     3030   3485   2826    314    303    425       O  
-ATOM   5262  CB  LYS C 683     -73.452  36.772 -49.814  1.00 28.39           C  
-ANISOU 5262  CB  LYS C 683     3470   4120   3197    423    280    484       C  
-ATOM   5263  CG  LYS C 683     -74.389  35.839 -50.545  1.00 30.61           C  
-ANISOU 5263  CG  LYS C 683     3716   4492   3420    437    231    461       C  
-ATOM   5264  CD  LYS C 683     -74.850  36.549 -51.831  1.00 37.00           C  
-ANISOU 5264  CD  LYS C 683     4513   5373   4173    511    255    516       C  
-ATOM   5265  CE  LYS C 683     -76.047  35.884 -52.488  1.00 40.92           C  
-ANISOU 5265  CE  LYS C 683     4966   5975   4606    532    209    499       C  
-ATOM   5266  NZ  LYS C 683     -76.495  36.691 -53.653  1.00 46.16           N  
-ANISOU 5266  NZ  LYS C 683     5615   6712   5212    614    235    559       N  
-ATOM   5267  N   LYS C 684     -72.046  38.229 -47.429  1.00 25.49           N  
-ANISOU 5267  N   LYS C 684     3162   3564   2959    347    349    484       N  
-ATOM   5268  CA  LYS C 684     -70.937  39.029 -46.903  1.00 28.35           C  
-ANISOU 5268  CA  LYS C 684     3550   3853   3369    317    393    489       C  
-ATOM   5269  C   LYS C 684     -70.190  38.267 -45.816  1.00 26.54           C  
-ANISOU 5269  C   LYS C 684     3318   3591   3174    256    362    431       C  
-ATOM   5270  O   LYS C 684     -68.958  38.250 -45.770  1.00 25.17           O  
-ANISOU 5270  O   LYS C 684     3147   3397   3021    226    374    415       O  
-ATOM   5271  CB  LYS C 684     -71.437  40.388 -46.425  1.00 31.24           C  
-ANISOU 5271  CB  LYS C 684     3945   4166   3758    335    446    531       C  
-ATOM   5272  CG  LYS C 684     -71.520  41.378 -47.562  1.00 35.63           C  
-ANISOU 5272  CG  LYS C 684     4516   4732   4290    393    501    596       C  
-ATOM   5273  CD  LYS C 684     -71.882  42.754 -47.011  1.00 42.65           C  
-ANISOU 5273  CD  LYS C 684     5445   5552   5208    409    563    637       C  
-ATOM   5274  CE  LYS C 684     -71.995  43.790 -48.125  1.00 47.66           C  
-ANISOU 5274  CE  LYS C 684     6104   6189   5818    474    628    709       C  
-ATOM   5275  NZ  LYS C 684     -72.152  45.182 -47.605  1.00 50.75           N  
-ANISOU 5275  NZ  LYS C 684     6547   6495   6242    486    701    748       N  
-ATOM   5276  N   ALA C 685     -70.946  37.636 -44.925  1.00 26.75           N  
-ANISOU 5276  N   ALA C 685     3339   3619   3205    240    323    401       N  
-ATOM   5277  CA  ALA C 685     -70.343  36.829 -43.855  1.00 26.45           C  
-ANISOU 5277  CA  ALA C 685     3301   3556   3194    191    292    348       C  
-ATOM   5278  C   ALA C 685     -69.461  35.759 -44.445  1.00 26.01           C  
-ANISOU 5278  C   ALA C 685     3232   3532   3119    183    265    320       C  
-ATOM   5279  O   ALA C 685     -68.315  35.594 -44.015  1.00 26.83           O  
-ANISOU 5279  O   ALA C 685     3336   3614   3244    155    267    296       O  
-ATOM   5280  CB  ALA C 685     -71.414  36.202 -43.019  1.00 28.16           C  
-ANISOU 5280  CB  ALA C 685     3513   3778   3408    183    256    327       C  
-ATOM   5281  N   MET C 686     -69.944  35.099 -45.500  1.00 25.43           N  
-ANISOU 5281  N   MET C 686     3146   3514   3003    211    243    322       N  
-ATOM   5282  CA  MET C 686     -69.135  34.075 -46.167  1.00 26.01           C  
-ANISOU 5282  CA  MET C 686     3212   3616   3053    210    221    295       C  
-ATOM   5283  C   MET C 686     -67.884  34.651 -46.819  1.00 25.13           C  
-ANISOU 5283  C   MET C 686     3099   3502   2946    217    258    315       C  
-ATOM   5284  O   MET C 686     -66.790  34.022 -46.825  1.00 23.55           O  
-ANISOU 5284  O   MET C 686     2895   3305   2748    204    250    289       O  
-ATOM   5285  CB  MET C 686     -69.979  33.297 -47.194  1.00 27.04           C  
-ANISOU 5285  CB  MET C 686     3332   3810   3133    236    192    290       C  
-ATOM   5286  CG  MET C 686     -71.072  32.465 -46.537  1.00 28.79           C  
-ANISOU 5286  CG  MET C 686     3551   4038   3350    216    153    258       C  
-ATOM   5287  SD  MET C 686     -72.256  31.652 -47.669  1.00 31.74           S  
-ANISOU 5287  SD  MET C 686     3904   4491   3663    234    119    245       S  
-ATOM   5288  CE  MET C 686     -71.144  30.419 -48.310  1.00 29.13           C  
-ANISOU 5288  CE  MET C 686     3587   4168   3312    227    101    202       C  
-ATOM   5289  N   VAL C 687     -68.016  35.836 -47.404  1.00 26.36           N  
-ANISOU 5289  N   VAL C 687     3259   3654   3102    241    302    364       N  
-ATOM   5290  CA  VAL C 687     -66.849  36.493 -47.983  1.00 26.81           C  
-ANISOU 5290  CA  VAL C 687     3316   3703   3168    242    346    387       C  
-ATOM   5291  C   VAL C 687     -65.849  36.781 -46.875  1.00 26.19           C  
-ANISOU 5291  C   VAL C 687     3239   3574   3137    191    359    362       C  
-ATOM   5292  O   VAL C 687     -64.686  36.493 -47.031  1.00 24.80           O  
-ANISOU 5292  O   VAL C 687     3050   3408   2965    176    363    346       O  
-ATOM   5293  CB  VAL C 687     -67.224  37.772 -48.745  1.00 27.70           C  
-ANISOU 5293  CB  VAL C 687     3441   3811   3273    278    400    449       C  
-ATOM   5294  CG1 VAL C 687     -65.994  38.617 -49.054  1.00 26.91           C  
-ANISOU 5294  CG1 VAL C 687     3346   3682   3196    263    456    471       C  
-ATOM   5295  CG2 VAL C 687     -67.947  37.409 -50.039  1.00 29.74           C  
-ANISOU 5295  CG2 VAL C 687     3690   4139   3472    334    386    471       C  
-ATOM   5296  N   GLU C 688     -66.310  37.312 -45.753  1.00 28.13           N  
-ANISOU 5296  N   GLU C 688     3498   3774   3416    167    364    357       N  
-ATOM   5297  CA  GLU C 688     -65.417  37.608 -44.637  1.00 33.41           C  
-ANISOU 5297  CA  GLU C 688     4166   4401   4126    117    374    328       C  
-ATOM   5298  C   GLU C 688     -64.697  36.363 -44.095  1.00 32.86           C  
-ANISOU 5298  C   GLU C 688     4077   4355   4052     98    328    278       C  
-ATOM   5299  O   GLU C 688     -63.585  36.475 -43.589  1.00 29.41           O  
-ANISOU 5299  O   GLU C 688     3627   3912   3636     66    337    256       O  
-ATOM   5300  CB  GLU C 688     -66.141  38.352 -43.506  1.00 36.94           C  
-ANISOU 5300  CB  GLU C 688     4634   4798   4605     99    386    327       C  
-ATOM   5301  CG  GLU C 688     -66.298  39.832 -43.788  1.00 44.26           C  
-ANISOU 5301  CG  GLU C 688     5585   5681   5549    104    450    372       C  
-ATOM   5302  CD  GLU C 688     -67.285  40.545 -42.873  1.00 49.12           C  
-ANISOU 5302  CD  GLU C 688     6228   6250   6185    104    463    379       C  
-ATOM   5303  OE1 GLU C 688     -67.811  39.969 -41.900  1.00 51.63           O  
-ANISOU 5303  OE1 GLU C 688     6543   6568   6506     93    423    348       O  
-ATOM   5304  OE2 GLU C 688     -67.558  41.713 -43.189  1.00 53.13           O  
-ANISOU 5304  OE2 GLU C 688     6763   6720   6702    120    519    421       O  
-ATOM   5305  N   TYR C 689     -65.316  35.192 -44.224  1.00 31.04           N  
-ANISOU 5305  N   TYR C 689     3847   4154   3793    119    283    260       N  
-ATOM   5306  CA  TYR C 689     -64.646  33.945 -43.842  1.00 31.35           C  
-ANISOU 5306  CA  TYR C 689     3876   4211   3822    113    246    219       C  
-ATOM   5307  C   TYR C 689     -63.733  33.413 -44.911  1.00 33.49           C  
-ANISOU 5307  C   TYR C 689     4134   4524   4066    134    248    218       C  
-ATOM   5308  O   TYR C 689     -63.107  32.370 -44.711  1.00 33.81           O  
-ANISOU 5308  O   TYR C 689     4170   4581   4094    138    222    188       O  
-ATOM   5309  CB  TYR C 689     -65.660  32.868 -43.495  1.00 29.45           C  
-ANISOU 5309  CB  TYR C 689     3649   3975   3565    121    203    197       C  
-ATOM   5310  CG  TYR C 689     -66.374  33.098 -42.193  1.00 28.16           C  
-ANISOU 5310  CG  TYR C 689     3497   3776   3428     99    195    187       C  
-ATOM   5311  CD1 TYR C 689     -65.669  33.263 -40.990  1.00 29.07           C  
-ANISOU 5311  CD1 TYR C 689     3609   3866   3570     71    196    165       C  
-ATOM   5312  CD2 TYR C 689     -67.735  33.105 -42.158  1.00 26.82           C  
-ANISOU 5312  CD2 TYR C 689     3335   3604   3251    107    185    198       C  
-ATOM   5313  CE1 TYR C 689     -66.335  33.456 -39.802  1.00 28.93           C  
-ANISOU 5313  CE1 TYR C 689     3602   3817   3572     55    188    156       C  
-ATOM   5314  CE2 TYR C 689     -68.403  33.303 -41.006  1.00 28.37           C  
-ANISOU 5314  CE2 TYR C 689     3541   3771   3469     91    179    192       C  
-ATOM   5315  CZ  TYR C 689     -67.713  33.470 -39.827  1.00 28.86           C  
-ANISOU 5315  CZ  TYR C 689     3605   3803   3557     65    181    171       C  
-ATOM   5316  OH  TYR C 689     -68.449  33.672 -38.684  1.00 29.87           O  
-ANISOU 5316  OH  TYR C 689     3744   3904   3702     53    177    165       O  
-ATOM   5317  N   GLU C 690     -63.661  34.117 -46.045  1.00 34.04           N  
-ANISOU 5317  N   GLU C 690     4200   4609   4124    153    281    255       N  
-ATOM   5318  CA  GLU C 690     -62.797  33.749 -47.160  1.00 33.80           C  
-ANISOU 5318  CA  GLU C 690     4156   4620   4065    177    290    261       C  
-ATOM   5319  C   GLU C 690     -63.251  32.477 -47.825  1.00 34.85           C  
-ANISOU 5319  C   GLU C 690     4298   4789   4155    209    251    242       C  
-ATOM   5320  O   GLU C 690     -62.460  31.761 -48.440  1.00 34.43           O  
-ANISOU 5320  O   GLU C 690     4238   4768   4076    228    246    230       O  
-ATOM   5321  CB  GLU C 690     -61.340  33.656 -46.732  1.00 39.36           C  
-ANISOU 5321  CB  GLU C 690     4838   5331   4785    154    299    241       C  
-ATOM   5322  CG  GLU C 690     -60.758  35.010 -46.352  1.00 44.59           C  
-ANISOU 5322  CG  GLU C 690     5490   5965   5488    115    346    259       C  
-ATOM   5323  CD  GLU C 690     -59.256  34.968 -46.069  1.00 52.44           C  
-ANISOU 5323  CD  GLU C 690     6449   6982   6492     90    357    238       C  
-ATOM   5324  OE1 GLU C 690     -58.653  33.865 -45.913  1.00 54.69           O  
-ANISOU 5324  OE1 GLU C 690     6719   7302   6757    106    325    209       O  
-ATOM   5325  OE2 GLU C 690     -58.671  36.069 -46.009  1.00 58.40           O  
-ANISOU 5325  OE2 GLU C 690     7192   7720   7276     54    402    252       O  
-ATOM   5326  N   ILE C 691     -64.540  32.189 -47.692  1.00 34.54           N  
-ANISOU 5326  N   ILE C 691     4273   4746   4105    213    226    238       N  
-ATOM   5327  CA  ILE C 691     -65.132  31.067 -48.372  1.00 35.11           C  
-ANISOU 5327  CA  ILE C 691     4354   4852   4135    235    193    216       C  
-ATOM   5328  C   ILE C 691     -65.216  31.350 -49.869  1.00 38.49           C  
-ANISOU 5328  C   ILE C 691     4775   5327   4523    273    209    245       C  
-ATOM   5329  O   ILE C 691     -65.499  32.461 -50.269  1.00 43.19           O  
-ANISOU 5329  O   ILE C 691     5364   5924   5120    286    241    288       O  
-ATOM   5330  CB  ILE C 691     -66.489  30.758 -47.765  1.00 34.80           C  
-ANISOU 5330  CB  ILE C 691     4325   4800   4098    221    165    202       C  
-ATOM   5331  CG1 ILE C 691     -66.191  30.152 -46.395  1.00 34.85           C  
-ANISOU 5331  CG1 ILE C 691     4342   4766   4135    191    147    169       C  
-ATOM   5332  CG2 ILE C 691     -67.304  29.805 -48.633  1.00 33.51           C  
-ANISOU 5332  CG2 ILE C 691     4166   4677   3888    237    135    181       C  
-ATOM   5333  CD1 ILE C 691     -67.343  29.699 -45.575  1.00 38.42           C  
-ANISOU 5333  CD1 ILE C 691     4805   5197   4594    171    121    150       C  
-ATOM   5334  N   ASP C 692     -64.953  30.343 -50.683  1.00 39.28           N  
-ANISOU 5334  N   ASP C 692     4879   5463   4582    294    191    221       N  
-ATOM   5335  CA  ASP C 692     -65.042  30.472 -52.121  1.00 37.38           C  
-ANISOU 5335  CA  ASP C 692     4632   5275   4294    334    201    242       C  
-ATOM   5336  C   ASP C 692     -66.489  30.331 -52.573  1.00 36.11           C  
-ANISOU 5336  C   ASP C 692     4472   5148   4100    345    177    240       C  
-ATOM   5337  O   ASP C 692     -66.998  29.221 -52.690  1.00 33.08           O  
-ANISOU 5337  O   ASP C 692     4098   4780   3690    337    140    196       O  
-ATOM   5338  CB  ASP C 692     -64.187  29.394 -52.780  1.00 42.22           C  
-ANISOU 5338  CB  ASP C 692     5253   5915   4874    353    190    211       C  
-ATOM   5339  CG  ASP C 692     -64.008  29.569 -54.316  1.00 45.17           C  
-ANISOU 5339  CG  ASP C 692     5618   6347   5196    399    208    235       C  
-ATOM   5340  OD1 ASP C 692     -64.957  29.477 -55.146  1.00 50.02           O  
-ANISOU 5340  OD1 ASP C 692     6232   7005   5766    421    193    237       O  
-ATOM   5341  OD2 ASP C 692     -62.840  29.704 -54.690  1.00 49.87           O  
-ANISOU 5341  OD2 ASP C 692     6206   6951   5790    414    234    248       O  
-ATOM   5342  N   LEU C 693     -67.152  31.468 -52.797  1.00 36.65           N  
-ANISOU 5342  N   LEU C 693     4529   5226   4169    361    200    287       N  
-ATOM   5343  CA  LEU C 693     -68.569  31.496 -53.174  1.00 37.41           C  
-ANISOU 5343  CA  LEU C 693     4617   5365   4232    376    179    292       C  
-ATOM   5344  C   LEU C 693     -68.823  30.986 -54.580  1.00 36.55           C  
-ANISOU 5344  C   LEU C 693     4499   5332   4055    413    164    284       C  
-ATOM   5345  O   LEU C 693     -69.939  30.629 -54.930  1.00 35.38           O  
-ANISOU 5345  O   LEU C 693     4339   5234   3870    418    135    268       O  
-ATOM   5346  CB  LEU C 693     -69.138  32.901 -53.028  1.00 37.77           C  
-ANISOU 5346  CB  LEU C 693     4656   5402   4294    395    214    350       C  
-ATOM   5347  CG  LEU C 693     -69.403  33.426 -51.621  1.00 39.65           C  
-ANISOU 5347  CG  LEU C 693     4901   5574   4589    360    222    353       C  
-ATOM   5348  CD1 LEU C 693     -70.041  34.805 -51.688  1.00 39.57           C  
-ANISOU 5348  CD1 LEU C 693     4891   5560   4584    391    261    413       C  
-ATOM   5349  CD2 LEU C 693     -70.344  32.485 -50.882  1.00 40.18           C  
-ANISOU 5349  CD2 LEU C 693     4966   5644   4658    328    174    307       C  
-ATOM   5350  N   GLN C 694     -67.784  30.956 -55.391  1.00 42.21           N  
-ANISOU 5350  N   GLN C 694     5220   6065   4754    439    185    294       N  
-ATOM   5351  CA  GLN C 694     -67.863  30.341 -56.706  1.00 46.60           C  
-ANISOU 5351  CA  GLN C 694     5771   6692   5242    474    170    279       C  
-ATOM   5352  C   GLN C 694     -68.018  28.835 -56.584  1.00 44.29           C  
-ANISOU 5352  C   GLN C 694     5493   6402   4932    444    124    205       C  
-ATOM   5353  O   GLN C 694     -68.892  28.261 -57.212  1.00 46.25           O  
-ANISOU 5353  O   GLN C 694     5736   6706   5131    449     94    175       O  
-ATOM   5354  CB  GLN C 694     -66.619  30.678 -57.543  1.00 52.91           C  
-ANISOU 5354  CB  GLN C 694     6572   7503   6027    509    209    309       C  
-ATOM   5355  CG  GLN C 694     -66.795  30.497 -59.052  1.00 56.45           C  
-ANISOU 5355  CG  GLN C 694     7014   8035   6400    562    206    316       C  
-ATOM   5356  CD  GLN C 694     -66.554  29.114 -59.592  1.00 54.68           C  
-ANISOU 5356  CD  GLN C 694     6802   7841   6133    561    172    252       C  
-ATOM   5357  OE1 GLN C 694     -65.419  28.672 -59.656  1.00 57.08           O  
-ANISOU 5357  OE1 GLN C 694     7119   8125   6445    563    184    239       O  
-ATOM   5358  NE2 GLN C 694     -67.605  28.468 -60.072  1.00 58.20           N  
-ANISOU 5358  NE2 GLN C 694     7244   8341   6530    561    132    213       N  
-ATOM   5359  N   LYS C 695     -67.207  28.196 -55.734  1.00 44.34           N  
-ANISOU 5359  N   LYS C 695     5520   6349   4978    414    121    174       N  
-ATOM   5360  CA  LYS C 695     -67.294  26.718 -55.554  1.00 42.79           C  
-ANISOU 5360  CA  LYS C 695     5350   6141   4769    388     86    105       C  
-ATOM   5361  C   LYS C 695     -68.373  26.293 -54.536  1.00 42.68           C  
-ANISOU 5361  C   LYS C 695     5341   6097   4780    340     57     75       C  
-ATOM   5362  O   LYS C 695     -68.942  25.216 -54.643  1.00 40.29           O  
-ANISOU 5362  O   LYS C 695     5054   5801   4453    316     28     21       O  
-ATOM   5363  CB  LYS C 695     -65.914  26.115 -55.223  1.00 43.41           C  
-ANISOU 5363  CB  LYS C 695     5450   6178   4866    391     98     89       C  
-ATOM   5364  N   MET C 696     -68.673  27.150 -53.563  1.00 41.29           N  
-ANISOU 5364  N   MET C 696     5152   5886   4651    323     68    107       N  
-ATOM   5365  CA  MET C 696     -69.718  26.858 -52.593  1.00 40.45           C  
-ANISOU 5365  CA  MET C 696     5046   5755   4567    281     45     85       C  
-ATOM   5366  C   MET C 696     -70.652  28.041 -52.336  1.00 39.00           C  
-ANISOU 5366  C   MET C 696     4835   5588   4397    287     54    131       C  
-ATOM   5367  O   MET C 696     -70.500  28.742 -51.354  1.00 38.62           O  
-ANISOU 5367  O   MET C 696     4787   5491   4395    276     72    157       O  
-ATOM   5368  CB  MET C 696     -69.124  26.423 -51.265  1.00 40.86           C  
-ANISOU 5368  CB  MET C 696     5122   5731   4670    250     46     67       C  
-ATOM   5369  CG  MET C 696     -70.175  25.848 -50.315  1.00 41.95           C  
-ANISOU 5369  CG  MET C 696     5269   5844   4827    206     23     37       C  
-ATOM   5370  SD  MET C 696     -69.451  25.122 -48.849  1.00 50.16           S  
-ANISOU 5370  SD  MET C 696     6343   6801   5914    179     24     14       S  
-ATOM   5371  CE  MET C 696     -69.031  26.567 -47.879  1.00 53.91           C  
-ANISOU 5371  CE  MET C 696     6798   7247   6440    183     50     65       C  
-ATOM   5372  N   PRO C 697     -71.638  28.247 -53.207  1.00 36.85           N  
-ANISOU 5372  N   PRO C 697     4537   5386   4076    307     43    138       N  
-ATOM   5373  CA  PRO C 697     -72.585  29.342 -52.966  1.00 36.53           C  
-ANISOU 5373  CA  PRO C 697     4470   5366   4042    322     53    184       C  
-ATOM   5374  C   PRO C 697     -73.483  29.094 -51.749  1.00 33.73           C  
-ANISOU 5374  C   PRO C 697     4114   4981   3722    277     35    164       C  
-ATOM   5375  O   PRO C 697     -73.580  27.974 -51.296  1.00 34.14           O  
-ANISOU 5375  O   PRO C 697     4180   5010   3781    233     10    111       O  
-ATOM   5376  CB  PRO C 697     -73.433  29.363 -54.236  1.00 35.43           C  
-ANISOU 5376  CB  PRO C 697     4301   5326   3833    356     38    188       C  
-ATOM   5377  CG  PRO C 697     -73.299  28.009 -54.810  1.00 38.36           C  
-ANISOU 5377  CG  PRO C 697     4684   5722   4169    332      6    122       C  
-ATOM   5378  CD  PRO C 697     -71.904  27.551 -54.476  1.00 38.41           C  
-ANISOU 5378  CD  PRO C 697     4728   5656   4208    322     21    108       C  
-ATOM   5379  N   LEU C 698     -74.168  30.137 -51.301  1.00 33.81           N  
-ANISOU 5379  N   LEU C 698     4106   4993   3748    292     51    208       N  
-ATOM   5380  CA  LEU C 698     -75.180  30.057 -50.260  1.00 33.98           C  
-ANISOU 5380  CA  LEU C 698     4117   5000   3793    259     37    198       C  
-ATOM   5381  C   LEU C 698     -76.093  28.855 -50.441  1.00 34.11           C  
-ANISOU 5381  C   LEU C 698     4118   5062   3778    221     -5    141       C  
-ATOM   5382  O   LEU C 698     -76.374  28.124 -49.490  1.00 34.61           O  
-ANISOU 5382  O   LEU C 698     4194   5085   3870    171    -19    105       O  
-ATOM   5383  CB  LEU C 698     -76.008  31.339 -50.245  1.00 33.93           C  
-ANISOU 5383  CB  LEU C 698     4087   5023   3782    300     59    256       C  
-ATOM   5384  CG  LEU C 698     -76.706  31.740 -48.960  1.00 36.96           C  
-ANISOU 5384  CG  LEU C 698     4469   5369   4206    281     64    267       C  
-ATOM   5385  CD1 LEU C 698     -75.860  31.663 -47.704  1.00 36.18           C  
-ANISOU 5385  CD1 LEU C 698     4405   5173   4169    244     76    254       C  
-ATOM   5386  CD2 LEU C 698     -77.283  33.143 -49.120  1.00 39.54           C  
-ANISOU 5386  CD2 LEU C 698     4781   5718   4524    338     97    333       C  
-ATOM   5387  N   GLY C 699     -76.577  28.650 -51.651  1.00 35.83           N  
-ANISOU 5387  N   GLY C 699     4311   5368   3936    241    -22    131       N  
-ATOM   5388  CA  GLY C 699     -77.537  27.556 -51.919  1.00 39.84           C  
-ANISOU 5388  CA  GLY C 699     4798   5931   4408    198    -61     71       C  
-ATOM   5389  C   GLY C 699     -76.958  26.153 -51.776  1.00 40.39           C  
-ANISOU 5389  C   GLY C 699     4908   5950   4487    146    -77      4       C  
-ATOM   5390  O   GLY C 699     -77.710  25.193 -51.658  1.00 46.06           O  
-ANISOU 5390  O   GLY C 699     5621   6684   5193     93   -102    -49       O  
-ATOM   5391  N   LYS C 700     -75.637  26.025 -51.797  1.00 37.99           N  
-ANISOU 5391  N   LYS C 700     4644   5587   4202    161    -59      8       N  
-ATOM   5392  CA  LYS C 700     -74.985  24.717 -51.801  1.00 39.11           C  
-ANISOU 5392  CA  LYS C 700     4830   5686   4346    128    -68    -50       C  
-ATOM   5393  C   LYS C 700     -74.568  24.251 -50.407  1.00 39.24           C  
-ANISOU 5393  C   LYS C 700     4883   5605   4420     93    -59    -62       C  
-ATOM   5394  O   LYS C 700     -74.227  23.099 -50.220  1.00 38.60           O  
-ANISOU 5394  O   LYS C 700     4841   5481   4342     64    -65   -109       O  
-ATOM   5395  CB  LYS C 700     -73.755  24.754 -52.726  1.00 40.67           C  
-ANISOU 5395  CB  LYS C 700     5046   5886   4521    173    -54    -41       C  
-ATOM   5396  N   LEU C 701     -74.543  25.165 -49.438  1.00 43.51           N  
-ANISOU 5396  N   LEU C 701     5415   6111   5005    101    -43    -17       N  
-ATOM   5397  CA  LEU C 701     -74.286  24.809 -48.033  1.00 41.83           C  
-ANISOU 5397  CA  LEU C 701     5232   5818   4844     71    -36    -25       C  
-ATOM   5398  C   LEU C 701     -75.165  23.669 -47.577  1.00 38.59           C  
-ANISOU 5398  C   LEU C 701     4835   5396   4434     14    -54    -75       C  
-ATOM   5399  O   LEU C 701     -76.380  23.754 -47.710  1.00 36.62           O  
-ANISOU 5399  O   LEU C 701     4550   5196   4167     -8    -68    -81       O  
-ATOM   5400  CB  LEU C 701     -74.569  26.016 -47.122  1.00 43.04           C  
-ANISOU 5400  CB  LEU C 701     5365   5955   5035     81    -20     24       C  
-ATOM   5401  CG  LEU C 701     -73.537  27.147 -47.138  1.00 46.02           C  
-ANISOU 5401  CG  LEU C 701     5742   6313   5431    123      8     72       C  
-ATOM   5402  CD1 LEU C 701     -73.944  28.237 -46.151  1.00 48.43           C  
-ANISOU 5402  CD1 LEU C 701     6034   6593   5772    125     25    111       C  
-ATOM   5403  CD2 LEU C 701     -72.162  26.612 -46.788  1.00 46.12           C  
-ANISOU 5403  CD2 LEU C 701     5788   6272   5463    123     16     56       C  
-ATOM   5404  N   SER C 702     -74.570  22.622 -47.007  1.00 37.96           N  
-ANISOU 5404  N   SER C 702     4802   5248   4371     -7    -50   -108       N  
-ATOM   5405  CA  SER C 702     -75.350  21.452 -46.581  1.00 38.43           C  
-ANISOU 5405  CA  SER C 702     4885   5284   4432    -65    -59   -157       C  
-ATOM   5406  C   SER C 702     -75.041  21.043 -45.139  1.00 37.03           C  
-ANISOU 5406  C   SER C 702     4746   5023   4300    -81    -44   -154       C  
-ATOM   5407  O   SER C 702     -73.917  21.103 -44.691  1.00 34.28           O  
-ANISOU 5407  O   SER C 702     4424   4630   3971    -49    -31   -138       O  
-ATOM   5408  CB  SER C 702     -75.094  20.285 -47.539  1.00 39.57           C  
-ANISOU 5408  CB  SER C 702     5063   5432   4539    -79    -66   -212       C  
-ATOM   5409  OG  SER C 702     -74.254  19.299 -46.978  1.00 41.53           O  
-ANISOU 5409  OG  SER C 702     5375   5599   4805    -81    -50   -234       O  
-ATOM   5410  N   LYS C 703     -76.062  20.593 -44.432  1.00 39.89           N  
-ANISOU 5410  N   LYS C 703     5109   5372   4676   -130    -47   -171       N  
-ATOM   5411  CA  LYS C 703     -75.925  20.141 -43.050  1.00 38.42           C  
-ANISOU 5411  CA  LYS C 703     4959   5111   4528   -146    -31   -168       C  
-ATOM   5412  C   LYS C 703     -74.944  18.991 -42.917  1.00 35.52           C  
-ANISOU 5412  C   LYS C 703     4658   4676   4160   -139    -17   -196       C  
-ATOM   5413  O   LYS C 703     -74.175  18.938 -41.963  1.00 32.43           O  
-ANISOU 5413  O   LYS C 703     4296   4232   3794   -114     -2   -177       O  
-ATOM   5414  CB  LYS C 703     -77.278  19.712 -42.506  1.00 45.07           C  
-ANISOU 5414  CB  LYS C 703     5790   5955   5378   -206    -33   -187       C  
-ATOM   5415  CG  LYS C 703     -78.237  20.857 -42.235  1.00 50.83           C  
-ANISOU 5415  CG  LYS C 703     6458   6741   6114   -205    -41   -151       C  
-ATOM   5416  CD  LYS C 703     -79.507  20.402 -41.543  1.00 58.20           C  
-ANISOU 5416  CD  LYS C 703     7378   7676   7058   -264    -39   -167       C  
-ATOM   5417  CE  LYS C 703     -80.442  19.629 -42.463  1.00 64.21           C  
-ANISOU 5417  CE  LYS C 703     8120   8489   7785   -320    -54   -218       C  
-ATOM   5418  NZ  LYS C 703     -80.874  20.454 -43.632  1.00 69.45           N  
-ANISOU 5418  NZ  LYS C 703     8721   9256   8410   -296    -77   -209       N  
-ATOM   5419  N   ARG C 704     -74.952  18.083 -43.891  1.00 34.05           N  
-ANISOU 5419  N   ARG C 704     4498   4497   3944   -156    -20   -241       N  
-ATOM   5420  CA  ARG C 704     -74.112  16.893 -43.820  1.00 32.66           C  
-ANISOU 5420  CA  ARG C 704     4394   4253   3764   -147     -2   -270       C  
-ATOM   5421  C   ARG C 704     -72.643  17.230 -44.135  1.00 32.32           C  
-ANISOU 5421  C   ARG C 704     4359   4208   3712    -77      3   -245       C  
-ATOM   5422  O   ARG C 704     -71.734  16.647 -43.543  1.00 32.09           O  
-ANISOU 5422  O   ARG C 704     4377   4122   3693    -47     22   -243       O  
-ATOM   5423  CB  ARG C 704     -74.683  15.743 -44.678  1.00 31.68           C  
-ANISOU 5423  CB  ARG C 704     4302   4126   3609   -196     -3   -333       C  
-ATOM   5424  N   GLN C 705     -72.397  18.178 -45.037  1.00 31.16           N  
-ANISOU 5424  N   GLN C 705     4165   4127   3548    -48    -10   -225       N  
-ATOM   5425  CA  GLN C 705     -71.048  18.634 -45.286  1.00 31.88           C  
-ANISOU 5425  CA  GLN C 705     4254   4224   3636     12     -2   -198       C  
-ATOM   5426  C   GLN C 705     -70.474  19.335 -44.046  1.00 28.35           C  
-ANISOU 5426  C   GLN C 705     3794   3749   3226     34      7   -156       C  
-ATOM   5427  O   GLN C 705     -69.323  19.119 -43.670  1.00 27.30           O  
-ANISOU 5427  O   GLN C 705     3684   3591   3098     73     19   -148       O  
-ATOM   5428  CB  GLN C 705     -70.969  19.556 -46.522  1.00 36.33           C  
-ANISOU 5428  CB  GLN C 705     4769   4862   4172     36    -13   -181       C  
-ATOM   5429  CG  GLN C 705     -71.229  18.850 -47.870  1.00 46.16           C  
-ANISOU 5429  CG  GLN C 705     6027   6143   5370     28    -22   -225       C  
-ATOM   5430  CD  GLN C 705     -70.329  17.614 -48.154  1.00 49.19           C  
-ANISOU 5430  CD  GLN C 705     6475   6481   5734     48     -9   -262       C  
-ATOM   5431  OE1 GLN C 705     -70.682  16.452 -47.852  1.00 50.37           O  
-ANISOU 5431  OE1 GLN C 705     6677   6578   5883     14     -2   -304       O  
-ATOM   5432  NE2 GLN C 705     -69.158  17.877 -48.709  1.00 52.75           N  
-ANISOU 5432  NE2 GLN C 705     6924   6949   6170    103      0   -243       N  
-ATOM   5433  N   ILE C 706     -71.269  20.168 -43.413  1.00 25.70           N  
-ANISOU 5433  N   ILE C 706     3424   3426   2915     12      1   -133       N  
-ATOM   5434  CA  ILE C 706     -70.803  20.915 -42.239  1.00 24.64           C  
-ANISOU 5434  CA  ILE C 706     3276   3270   2814     28      9    -98       C  
-ATOM   5435  C   ILE C 706     -70.492  19.957 -41.106  1.00 25.39           C  
-ANISOU 5435  C   ILE C 706     3420   3303   2923     28     20   -109       C  
-ATOM   5436  O   ILE C 706     -69.470  20.085 -40.463  1.00 25.52           O  
-ANISOU 5436  O   ILE C 706     3443   3305   2950     62     28    -94       O  
-ATOM   5437  CB  ILE C 706     -71.813  22.013 -41.838  1.00 24.06           C  
-ANISOU 5437  CB  ILE C 706     3159   3221   2760      7      4    -71       C  
-ATOM   5438  CG1 ILE C 706     -71.769  23.148 -42.888  1.00 23.91           C  
-ANISOU 5438  CG1 ILE C 706     3097   3261   2728     29      1    -46       C  
-ATOM   5439  CG2 ILE C 706     -71.490  22.594 -40.464  1.00 24.29           C  
-ANISOU 5439  CG2 ILE C 706     3187   3219   2824     15     13    -46       C  
-ATOM   5440  CD1 ILE C 706     -72.964  24.077 -42.869  1.00 24.31           C  
-ANISOU 5440  CD1 ILE C 706     3108   3346   2784     14     -3    -23       C  
-ATOM   5441  N   GLN C 707     -71.362  18.969 -40.901  1.00 26.66           N  
-ANISOU 5441  N   GLN C 707     3615   3432   3082    -10     23   -138       N  
-ATOM   5442  CA  GLN C 707     -71.133  17.954 -39.916  1.00 28.58           C  
-ANISOU 5442  CA  GLN C 707     3913   3611   3335     -8     40   -147       C  
-ATOM   5443  C   GLN C 707     -69.823  17.232 -40.163  1.00 26.00           C  
-ANISOU 5443  C   GLN C 707     3627   3262   2988     42     52   -155       C  
-ATOM   5444  O   GLN C 707     -69.061  16.981 -39.221  1.00 26.76           O  
-ANISOU 5444  O   GLN C 707     3747   3328   3092     78     65   -140       O  
-ATOM   5445  CB  GLN C 707     -72.292  16.984 -39.903  1.00 32.28           C  
-ANISOU 5445  CB  GLN C 707     4413   4049   3801    -65     46   -181       C  
-ATOM   5446  CG  GLN C 707     -72.134  15.774 -38.991  1.00 37.04           C  
-ANISOU 5446  CG  GLN C 707     5087   4575   4411    -65     72   -191       C  
-ATOM   5447  CD  GLN C 707     -73.161  14.681 -39.291  1.00 44.92           C  
-ANISOU 5447  CD  GLN C 707     6124   5538   5403   -129     84   -234       C  
-ATOM   5448  OE1 GLN C 707     -73.182  14.116 -40.386  1.00 49.46           O  
-ANISOU 5448  OE1 GLN C 707     6719   6121   5955   -144     83   -272       O  
-ATOM   5449  NE2 GLN C 707     -73.988  14.369 -38.329  1.00 48.18           N  
-ANISOU 5449  NE2 GLN C 707     6552   5916   5838   -168     99   -231       N  
-ATOM   5450  N   ALA C 708     -69.543  16.916 -41.416  1.00 24.35           N  
-ANISOU 5450  N   ALA C 708     3426   3075   2752     51     49   -177       N  
-ATOM   5451  CA  ALA C 708     -68.305  16.229 -41.772  1.00 24.85           C  
-ANISOU 5451  CA  ALA C 708     3527   3122   2792    105     63   -185       C  
-ATOM   5452  C   ALA C 708     -67.097  17.140 -41.523  1.00 24.21           C  
-ANISOU 5452  C   ALA C 708     3405   3079   2717    157     61   -149       C  
-ATOM   5453  O   ALA C 708     -66.017  16.684 -41.144  1.00 24.68           O  
-ANISOU 5453  O   ALA C 708     3487   3123   2766    207     74   -142       O  
-ATOM   5454  CB  ALA C 708     -68.327  15.758 -43.238  1.00 24.34           C  
-ANISOU 5454  CB  ALA C 708     3476   3079   2693    102     60   -219       C  
-ATOM   5455  N   ALA C 709     -67.280  18.417 -41.779  1.00 23.37           N  
-ANISOU 5455  N   ALA C 709     3236   3021   2622    144     46   -126       N  
-ATOM   5456  CA  ALA C 709     -66.232  19.400 -41.520  1.00 23.20           C  
-ANISOU 5456  CA  ALA C 709     3172   3033   2610    178     47    -95       C  
-ATOM   5457  C   ALA C 709     -65.908  19.479 -40.010  1.00 22.78           C  
-ANISOU 5457  C   ALA C 709     3121   2954   2578    188     51    -80       C  
-ATOM   5458  O   ALA C 709     -64.744  19.587 -39.626  1.00 21.64           O  
-ANISOU 5458  O   ALA C 709     2967   2826   2431    229     56    -68       O  
-ATOM   5459  CB  ALA C 709     -66.647  20.772 -42.066  1.00 22.33           C  
-ANISOU 5459  CB  ALA C 709     3004   2969   2510    158     38    -74       C  
-ATOM   5460  N   TYR C 710     -66.936  19.449 -39.168  1.00 22.29           N  
-ANISOU 5460  N   TYR C 710     3069   2862   2537    152     49    -80       N  
-ATOM   5461  CA  TYR C 710     -66.717  19.399 -37.719  1.00 21.63           C  
-ANISOU 5461  CA  TYR C 710     2995   2755   2469    164     54    -67       C  
-ATOM   5462  C   TYR C 710     -65.855  18.217 -37.345  1.00 23.22           C  
-ANISOU 5462  C   TYR C 710     3246   2928   2650    212     68    -74       C  
-ATOM   5463  O   TYR C 710     -64.867  18.351 -36.596  1.00 23.83           O  
-ANISOU 5463  O   TYR C 710     3312   3021   2723    253     71    -60       O  
-ATOM   5464  CB  TYR C 710     -68.029  19.297 -36.973  1.00 21.86           C  
-ANISOU 5464  CB  TYR C 710     3037   2751   2517    120     54    -68       C  
-ATOM   5465  CG  TYR C 710     -68.762  20.597 -36.727  1.00 20.88           C  
-ANISOU 5465  CG  TYR C 710     2864   2653   2418     88     43    -50       C  
-ATOM   5466  CD1 TYR C 710     -68.156  21.652 -36.034  1.00 20.47           C  
-ANISOU 5466  CD1 TYR C 710     2776   2621   2381    103     41    -30       C  
-ATOM   5467  CD2 TYR C 710     -70.078  20.747 -37.122  1.00 20.72           C  
-ANISOU 5467  CD2 TYR C 710     2833   2636   2403     45     38    -55       C  
-ATOM   5468  CE1 TYR C 710     -68.854  22.810 -35.776  1.00 20.44           C  
-ANISOU 5468  CE1 TYR C 710     2737   2631   2398     77     37    -14       C  
-ATOM   5469  CE2 TYR C 710     -70.775  21.926 -36.905  1.00 20.64           C  
-ANISOU 5469  CE2 TYR C 710     2780   2649   2411     25     32    -35       C  
-ATOM   5470  CZ  TYR C 710     -70.166  22.947 -36.241  1.00 21.13           C  
-ANISOU 5470  CZ  TYR C 710     2818   2722   2490     43     34    -14       C  
-ATOM   5471  OH  TYR C 710     -70.896  24.080 -35.978  1.00 23.62           O  
-ANISOU 5471  OH  TYR C 710     3100   3051   2823     26     33      5       O  
-ATOM   5472  N   SER C 711     -66.192  17.052 -37.876  1.00 24.07           N  
-ANISOU 5472  N   SER C 711     3410   2997   2741    209     80    -97       N  
-ATOM   5473  CA  SER C 711     -65.418  15.850 -37.593  1.00 26.29           C  
-ANISOU 5473  CA  SER C 711     3750   3242   2999    261    101   -102       C  
-ATOM   5474  C   SER C 711     -63.979  15.966 -37.980  1.00 25.42           C  
-ANISOU 5474  C   SER C 711     3619   3175   2865    324    102    -94       C  
-ATOM   5475  O   SER C 711     -63.115  15.578 -37.211  1.00 30.00           O  
-ANISOU 5475  O   SER C 711     4212   3754   3431    378    113    -80       O  
-ATOM   5476  CB  SER C 711     -65.989  14.620 -38.306  1.00 27.28           C  
-ANISOU 5476  CB  SER C 711     3943   3314   3109    243    119   -135       C  
-ATOM   5477  OG  SER C 711     -67.267  14.362 -37.814  1.00 30.93           O  
-ANISOU 5477  OG  SER C 711     4426   3736   3592    184    123   -144       O  
-ATOM   5478  N   ILE C 712     -63.721  16.478 -39.160  1.00 24.32           N  
-ANISOU 5478  N   ILE C 712     3446   3078   2718    319     93    -99       N  
-ATOM   5479  CA  ILE C 712     -62.352  16.635 -39.606  1.00 25.47           C  
-ANISOU 5479  CA  ILE C 712     3566   3272   2841    376     96    -90       C  
-ATOM   5480  C   ILE C 712     -61.592  17.556 -38.666  1.00 24.54           C  
-ANISOU 5480  C   ILE C 712     3391   3198   2735    392     87    -66       C  
-ATOM   5481  O   ILE C 712     -60.464  17.280 -38.330  1.00 22.83           O  
-ANISOU 5481  O   ILE C 712     3169   3009   2499    448     94    -57       O  
-ATOM   5482  CB  ILE C 712     -62.293  17.183 -41.056  1.00 26.37           C  
-ANISOU 5482  CB  ILE C 712     3648   3428   2946    362     89    -97       C  
-ATOM   5483  CG1 ILE C 712     -62.752  16.126 -42.052  1.00 28.13           C  
-ANISOU 5483  CG1 ILE C 712     3928   3616   3143    360     98   -128       C  
-ATOM   5484  CG2 ILE C 712     -60.904  17.655 -41.419  1.00 26.17           C  
-ANISOU 5484  CG2 ILE C 712     3577   3462   2903    410     92    -81       C  
-ATOM   5485  CD1 ILE C 712     -61.940  14.845 -42.142  1.00 29.63           C  
-ANISOU 5485  CD1 ILE C 712     4180   3777   3300    421    121   -140       C  
-ATOM   5486  N   LEU C 713     -62.218  18.659 -38.257  1.00 24.52           N  
-ANISOU 5486  N   LEU C 713     3345   3206   2764    342     73    -56       N  
-ATOM   5487  CA  LEU C 713     -61.589  19.550 -37.296  1.00 24.08           C  
-ANISOU 5487  CA  LEU C 713     3241   3188   2722    347     66    -40       C  
-ATOM   5488  C   LEU C 713     -61.254  18.827 -35.983  1.00 25.33           C  
-ANISOU 5488  C   LEU C 713     3427   3330   2869    386     71    -36       C  
-ATOM   5489  O   LEU C 713     -60.231  19.117 -35.351  1.00 23.86           O  
-ANISOU 5489  O   LEU C 713     3205   3190   2672    420     68    -29       O  
-ATOM   5490  CB  LEU C 713     -62.452  20.798 -37.059  1.00 22.93           C  
-ANISOU 5490  CB  LEU C 713     3058   3044   2611    288     56    -33       C  
-ATOM   5491  CG  LEU C 713     -62.557  21.794 -38.203  1.00 22.39           C  
-ANISOU 5491  CG  LEU C 713     2950   3005   2552    260     55    -27       C  
-ATOM   5492  CD1 LEU C 713     -63.454  22.989 -37.840  1.00 24.04           C  
-ANISOU 5492  CD1 LEU C 713     3131   3208   2794    211     50    -16       C  
-ATOM   5493  CD2 LEU C 713     -61.194  22.259 -38.597  1.00 22.86           C  
-ANISOU 5493  CD2 LEU C 713     2967   3118   2600    287     60    -21       C  
-ATOM   5494  N   SER C 714     -62.122  17.898 -35.577  1.00 26.21           N  
-ANISOU 5494  N   SER C 714     3599   3378   2980    381     81    -41       N  
-ATOM   5495  CA  SER C 714     -61.882  17.099 -34.375  1.00 26.95           C  
-ANISOU 5495  CA  SER C 714     3731   3449   3060    424     92    -33       C  
-ATOM   5496  C   SER C 714     -60.702  16.160 -34.583  1.00 28.66           C  
-ANISOU 5496  C   SER C 714     3974   3680   3237    503    107    -30       C  
-ATOM   5497  O   SER C 714     -59.877  16.010 -33.678  1.00 30.73           O  
-ANISOU 5497  O   SER C 714     4225   3973   3478    558    109    -16       O  
-ATOM   5498  CB  SER C 714     -63.104  16.258 -33.982  1.00 26.36           C  
-ANISOU 5498  CB  SER C 714     3723   3297   2995    396    107    -37       C  
-ATOM   5499  OG  SER C 714     -64.038  17.069 -33.343  1.00 25.89           O  
-ANISOU 5499  OG  SER C 714     3638   3234   2967    343     94    -32       O  
-ATOM   5500  N   GLU C 715     -60.620  15.542 -35.751  1.00 26.94           N  
-ANISOU 5500  N   GLU C 715     3788   3445   3004    513    119    -43       N  
-ATOM   5501  CA  GLU C 715     -59.492  14.696 -36.070  1.00 30.21           C  
-ANISOU 5501  CA  GLU C 715     4227   3874   3379    593    136    -40       C  
-ATOM   5502  C   GLU C 715     -58.196  15.492 -36.100  1.00 29.04           C  
-ANISOU 5502  C   GLU C 715     3999   3818   3215    628    123    -29       C  
-ATOM   5503  O   GLU C 715     -57.180  15.022 -35.649  1.00 28.51           O  
-ANISOU 5503  O   GLU C 715     3930   3786   3115    702    132    -17       O  
-ATOM   5504  CB  GLU C 715     -59.682  13.967 -37.399  1.00 32.80           C  
-ANISOU 5504  CB  GLU C 715     4604   4168   3693    593    151    -61       C  
-ATOM   5505  CG  GLU C 715     -60.809  12.943 -37.369  1.00 38.69           C  
-ANISOU 5505  CG  GLU C 715     5436   4820   4445    563    171    -79       C  
-ATOM   5506  CD  GLU C 715     -60.872  12.119 -38.663  1.00 43.06           C  
-ANISOU 5506  CD  GLU C 715     6043   5341   4978    567    188   -107       C  
-ATOM   5507  OE1 GLU C 715     -61.978  11.986 -39.257  1.00 49.07           O  
-ANISOU 5507  OE1 GLU C 715     6827   6063   5754    499    186   -134       O  
-ATOM   5508  OE2 GLU C 715     -59.790  11.652 -39.102  1.00 45.08           O  
-ANISOU 5508  OE2 GLU C 715     6310   5618   5199    639    202   -103       O  
-ATOM   5509  N   VAL C 716     -58.239  16.693 -36.637  1.00 29.09           N  
-ANISOU 5509  N   VAL C 716     3939   3867   3245    576    104    -32       N  
-ATOM   5510  CA  VAL C 716     -57.078  17.558 -36.617  1.00 32.62           C  
-ANISOU 5510  CA  VAL C 716     4308   4401   3686    593     94    -24       C  
-ATOM   5511  C   VAL C 716     -56.586  17.763 -35.184  1.00 32.86           C  
-ANISOU 5511  C   VAL C 716     4309   4468   3710    616     86    -15       C  
-ATOM   5512  O   VAL C 716     -55.392  17.639 -34.910  1.00 33.66           O  
-ANISOU 5512  O   VAL C 716     4375   4636   3780    674     87     -9       O  
-ATOM   5513  CB  VAL C 716     -57.380  18.943 -37.256  1.00 33.17           C  
-ANISOU 5513  CB  VAL C 716     4318   4496   3789    521     82    -26       C  
-ATOM   5514  CG1 VAL C 716     -56.283  19.938 -36.952  1.00 35.55           C  
-ANISOU 5514  CG1 VAL C 716     4538   4879   4091    521     75    -21       C  
-ATOM   5515  CG2 VAL C 716     -57.562  18.790 -38.750  1.00 35.08           C  
-ANISOU 5515  CG2 VAL C 716     4576   4729   4025    514     90    -33       C  
-ATOM   5516  N   GLN C 717     -57.502  18.130 -34.292  1.00 35.51           N  
-ANISOU 5516  N   GLN C 717     4652   4767   4072    572     77    -15       N  
-ATOM   5517  CA  GLN C 717     -57.162  18.429 -32.882  1.00 35.71           C  
-ANISOU 5517  CA  GLN C 717     4649   4828   4091    587     66    -10       C  
-ATOM   5518  C   GLN C 717     -56.566  17.189 -32.256  1.00 35.63           C  
-ANISOU 5518  C   GLN C 717     4681   4820   4036    677     80      3       C  
-ATOM   5519  O   GLN C 717     -55.545  17.266 -31.594  1.00 39.18           O  
-ANISOU 5519  O   GLN C 717     5088   5343   4456    726     74      8       O  
-ATOM   5520  CB  GLN C 717     -58.400  18.899 -32.125  1.00 40.58           C  
-ANISOU 5520  CB  GLN C 717     5281   5395   4743    527     59    -11       C  
-ATOM   5521  CG  GLN C 717     -58.184  19.240 -30.651  1.00 50.34           C  
-ANISOU 5521  CG  GLN C 717     6491   6664   5971    539     47     -8       C  
-ATOM   5522  CD  GLN C 717     -59.417  18.926 -29.760  1.00 57.40           C  
-ANISOU 5522  CD  GLN C 717     7438   7489   6880    518     52     -2       C  
-ATOM   5523  OE1 GLN C 717     -60.200  17.975 -30.011  1.00 54.62           O  
-ANISOU 5523  OE1 GLN C 717     7156   7066   6531    522     70      4       O  
-ATOM   5524  NE2 GLN C 717     -59.608  19.751 -28.722  1.00 61.85           N  
-ANISOU 5524  NE2 GLN C 717     7969   8075   7455    492     39     -5       N  
-ATOM   5525  N   GLN C 718     -57.143  16.032 -32.530  1.00 36.67           N  
-ANISOU 5525  N   GLN C 718     4897   4875   4160    701    103      7       N  
-ATOM   5526  CA  GLN C 718     -56.560  14.766 -32.061  1.00 39.60           C  
-ANISOU 5526  CA  GLN C 718     5323   5236   4486    796    126     23       C  
-ATOM   5527  C   GLN C 718     -55.166  14.477 -32.597  1.00 42.00           C  
-ANISOU 5527  C   GLN C 718     5598   5613   4749    873    132     29       C  
-ATOM   5528  O   GLN C 718     -54.288  14.048 -31.848  1.00 39.16           O  
-ANISOU 5528  O   GLN C 718     5228   5304   4346    955    137     45       O  
-ATOM   5529  CB  GLN C 718     -57.455  13.578 -32.373  1.00 42.28           C  
-ANISOU 5529  CB  GLN C 718     5767   5469   4829    798    157     23       C  
-ATOM   5530  CG  GLN C 718     -58.706  13.557 -31.545  1.00 47.58           C  
-ANISOU 5530  CG  GLN C 718     6475   6073   5529    746    160     25       C  
-ATOM   5531  CD  GLN C 718     -59.659  12.508 -32.076  1.00 54.04           C  
-ANISOU 5531  CD  GLN C 718     7387   6788   6357    725    190     15       C  
-ATOM   5532  OE1 GLN C 718     -60.845  12.793 -32.280  1.00 54.63           O  
-ANISOU 5532  OE1 GLN C 718     7471   6818   6469    642    184      1       O  
-ATOM   5533  NE2 GLN C 718     -59.141  11.291 -32.336  1.00 51.26           N  
-ANISOU 5533  NE2 GLN C 718     7105   6400   5970    798    224     21       N  
-ATOM   5534  N   ALA C 719     -54.981  14.659 -33.899  1.00 41.72           N  
-ANISOU 5534  N   ALA C 719     5548   5584   4719    853    133     17       N  
-ATOM   5535  CA  ALA C 719     -53.684  14.430 -34.509  1.00 43.07           C  
-ANISOU 5535  CA  ALA C 719     5686   5826   4850    923    140     22       C  
-ATOM   5536  C   ALA C 719     -52.634  15.357 -33.945  1.00 41.37           C  
-ANISOU 5536  C   ALA C 719     5368   5728   4624    931    118     25       C  
-ATOM   5537  O   ALA C 719     -51.517  14.952 -33.677  1.00 45.95           O  
-ANISOU 5537  O   ALA C 719     5921   6380   5158   1015    123     37       O  
-ATOM   5538  CB  ALA C 719     -53.760  14.612 -36.009  1.00 44.82           C  
-ANISOU 5538  CB  ALA C 719     5907   6039   5085    889    144      8       C  
-ATOM   5539  N   VAL C 720     -52.979  16.604 -33.765  1.00 44.35           N  
-ANISOU 5539  N   VAL C 720     5685   6126   5040    846     94     13       N  
-ATOM   5540  CA  VAL C 720     -52.040  17.493 -33.160  1.00 47.76           C  
-ANISOU 5540  CA  VAL C 720     6022   6662   5463    842     75      8       C  
-ATOM   5541  C   VAL C 720     -51.668  16.931 -31.768  1.00 52.68           C  
-ANISOU 5541  C   VAL C 720     6650   7319   6047    912     71     20       C  
-ATOM   5542  O   VAL C 720     -50.488  16.705 -31.494  1.00 53.32           O  
-ANISOU 5542  O   VAL C 720     6684   7494   6082    984     70     26       O  
-ATOM   5543  CB  VAL C 720     -52.604  18.909 -33.047  1.00 46.57           C  
-ANISOU 5543  CB  VAL C 720     5821   6509   5362    736     56     -8       C  
-ATOM   5544  CG1 VAL C 720     -51.722  19.757 -32.140  1.00 48.55           C  
-ANISOU 5544  CG1 VAL C 720     5983   6861   5602    727     37    -20       C  
-ATOM   5545  CG2 VAL C 720     -52.706  19.533 -34.427  1.00 48.48           C  
-ANISOU 5545  CG2 VAL C 720     6045   6742   5632    683     62    -14       C  
-ATOM   5546  N   SER C 721     -52.670  16.685 -30.912  1.00 50.78           N  
-ANISOU 5546  N   SER C 721     6465   7007   5821    896     71     24       N  
-ATOM   5547  CA  SER C 721     -52.432  16.159 -29.553  1.00 47.54           C  
-ANISOU 5547  CA  SER C 721     6067   6624   5373    964     71     39       C  
-ATOM   5548  C   SER C 721     -51.683  14.820 -29.526  1.00 50.08           C  
-ANISOU 5548  C   SER C 721     6435   6959   5636   1087     97     64       C  
-ATOM   5549  O   SER C 721     -50.818  14.620 -28.699  1.00 48.37           O  
-ANISOU 5549  O   SER C 721     6182   6827   5370   1163     91     76       O  
-ATOM   5550  CB  SER C 721     -53.755  16.013 -28.807  1.00 47.99           C  
-ANISOU 5550  CB  SER C 721     6189   6587   5458    925     75     43       C  
-ATOM   5551  OG  SER C 721     -54.316  17.309 -28.576  1.00 53.14           O  
-ANISOU 5551  OG  SER C 721     6791   7244   6155    827     50     22       O  
-ATOM   5552  N   GLN C 722     -52.009  13.926 -30.454  1.00 51.53           N  
-ANISOU 5552  N   GLN C 722     6697   7061   5820   1110    126     72       N  
-ATOM   5553  CA  GLN C 722     -51.454  12.582 -30.510  1.00 54.05           C  
-ANISOU 5553  CA  GLN C 722     7081   7366   6087   1226    160     96       C  
-ATOM   5554  C   GLN C 722     -50.006  12.646 -30.956  1.00 58.14           C  
-ANISOU 5554  C   GLN C 722     7527   8002   6561   1296    156    100       C  
-ATOM   5555  O   GLN C 722     -49.265  11.696 -30.754  1.00 55.23           O  
-ANISOU 5555  O   GLN C 722     7187   7661   6137   1411    179    125       O  
-ATOM   5556  CB  GLN C 722     -52.267  11.737 -31.492  1.00 53.59           C  
-ANISOU 5556  CB  GLN C 722     7126   7184   6050   1211    192     92       C  
-ATOM   5557  CG  GLN C 722     -51.763  10.311 -31.757  1.00 58.03           C  
-ANISOU 5557  CG  GLN C 722     7774   7711   6563   1326    236    114       C  
-ATOM   5558  CD  GLN C 722     -52.062   9.306 -30.640  1.00 62.10           C  
-ANISOU 5558  CD  GLN C 722     8375   8168   7053   1397    267    143       C  
-ATOM   5559  OE1 GLN C 722     -52.839   9.557 -29.708  1.00 61.24           O  
-ANISOU 5559  OE1 GLN C 722     8276   8026   6966   1352    259    146       O  
-ATOM   5560  NE2 GLN C 722     -51.434   8.146 -30.745  1.00 62.46           N  
-ANISOU 5560  NE2 GLN C 722     8488   8197   7048   1512    308    166       N  
-ATOM   5561  N   GLY C 723     -49.621  13.764 -31.576  1.00 63.96           N  
-ANISOU 5561  N   GLY C 723     8172   8808   7323   1227    130     78       N  
-ATOM   5562  CA  GLY C 723     -48.269  13.963 -32.108  1.00 65.57           C  
-ANISOU 5562  CA  GLY C 723     8294   9130   7490   1275    127     79       C  
-ATOM   5563  C   GLY C 723     -48.072  13.195 -33.394  1.00 67.18           C  
-ANISOU 5563  C   GLY C 723     8551   9293   7680   1319    157     85       C  
-ATOM   5564  O   GLY C 723     -47.096  12.470 -33.560  1.00 63.79           O  
-ANISOU 5564  O   GLY C 723     8121   8920   7197   1425    176    103       O  
-ATOM   5565  N   SER C 724     -49.026  13.341 -34.306  1.00 74.30           N  
-ANISOU 5565  N   SER C 724     9501  10099   8629   1241    162     69       N  
-ATOM   5566  CA  SER C 724     -48.970  12.648 -35.590  1.00 68.92           C  
-ANISOU 5566  CA  SER C 724     8876   9373   7938   1271    189     68       C  
-ATOM   5567  C   SER C 724     -48.016  13.377 -36.523  1.00 64.05           C  
-ANISOU 5567  C   SER C 724     8167   8854   7314   1262    182     61       C  
-ATOM   5568  O   SER C 724     -47.629  14.535 -36.281  1.00 56.55           O  
-ANISOU 5568  O   SER C 724     7116   7986   6382   1205    156     53       O  
-ATOM   5569  CB  SER C 724     -50.365  12.585 -36.217  1.00 66.39           C  
-ANISOU 5569  CB  SER C 724     8631   8928   7665   1186    194     49       C  
-ATOM   5570  OG  SER C 724     -51.245  11.840 -35.400  1.00 65.96           O  
-ANISOU 5570  OG  SER C 724     8664   8780   7617   1193    208     55       O  
-ATOM   5571  N   SER C 725     -47.650  12.686 -37.592  1.00 62.45           N  
-ANISOU 5571  N   SER C 725     8004   8639   7086   1316    208     64       N  
-ATOM   5572  CA  SER C 725     -46.778  13.243 -38.610  1.00 65.82           C  
-ANISOU 5572  CA  SER C 725     8355   9151   7503   1315    208     62       C  
-ATOM   5573  C   SER C 725     -47.284  14.612 -39.072  1.00 66.76           C  
-ANISOU 5573  C   SER C 725     8413   9274   7679   1188    185     44       C  
-ATOM   5574  O   SER C 725     -48.485  14.889 -39.022  1.00 66.97           O  
-ANISOU 5574  O   SER C 725     8482   9212   7750   1110    175     32       O  
-ATOM   5575  CB  SER C 725     -46.710  12.284 -39.800  1.00 67.95           C  
-ANISOU 5575  CB  SER C 725     8700   9371   7746   1373    241     61       C  
-ATOM   5576  OG  SER C 725     -48.013  11.887 -40.220  1.00 65.14           O  
-ANISOU 5576  OG  SER C 725     8443   8885   7421   1319    248     43       O  
-ATOM   5577  N   ASP C 726     -46.366  15.464 -39.515  1.00 64.13           N  
-ANISOU 5577  N   ASP C 726     7980   9043   7343   1171    179     45       N  
-ATOM   5578  CA  ASP C 726     -46.748  16.700 -40.199  1.00 65.19           C  
-ANISOU 5578  CA  ASP C 726     8067   9176   7526   1064    169     33       C  
-ATOM   5579  C   ASP C 726     -47.472  16.383 -41.489  1.00 57.06           C  
-ANISOU 5579  C   ASP C 726     7107   8068   6507   1047    185     28       C  
-ATOM   5580  O   ASP C 726     -48.315  17.133 -41.930  1.00 58.52           O  
-ANISOU 5580  O   ASP C 726     7294   8206   6734    962    177     19       O  
-ATOM   5581  CB  ASP C 726     -45.528  17.573 -40.450  1.00 68.49           C  
-ANISOU 5581  CB  ASP C 726     8369   9720   7935   1054    170     36       C  
-ATOM   5582  CG  ASP C 726     -44.972  18.135 -39.158  1.00 72.88           C  
-ANISOU 5582  CG  ASP C 726     8846  10357   8489   1040    148     31       C  
-ATOM   5583  OD1 ASP C 726     -45.275  17.559 -38.090  1.00 78.36           O  
-ANISOU 5583  OD1 ASP C 726     9579  11026   9170   1076    137     32       O  
-ATOM   5584  OD2 ASP C 726     -44.241  19.141 -39.201  1.00 79.18           O  
-ANISOU 5584  OD2 ASP C 726     9544  11243   9297    991    144     24       O  
-ATOM   5585  N   SER C 727     -47.155  15.238 -42.053  1.00 57.14           N  
-ANISOU 5585  N   SER C 727     7176   8061   6473   1135    208     32       N  
-ATOM   5586  CA  SER C 727     -47.826  14.719 -43.220  1.00 57.17           C  
-ANISOU 5586  CA  SER C 727     7257   7988   6476   1131    223     21       C  
-ATOM   5587  C   SER C 727     -49.296  14.368 -42.947  1.00 52.88           C  
-ANISOU 5587  C   SER C 727     6802   7325   5964   1078    216      4       C  
-ATOM   5588  O   SER C 727     -50.152  14.589 -43.799  1.00 55.67           O  
-ANISOU 5588  O   SER C 727     7184   7628   6340   1020    213    -10       O  
-ATOM   5589  CB  SER C 727     -47.064  13.470 -43.710  1.00 58.87           C  
-ANISOU 5589  CB  SER C 727     7523   8213   6632   1247    254     27       C  
-ATOM   5590  OG  SER C 727     -47.833  12.744 -44.651  1.00 59.24           O  
-ANISOU 5590  OG  SER C 727     7665   8168   6674   1246    270      8       O  
-ATOM   5591  N   GLN C 728     -49.595  13.773 -41.799  1.00 49.91           N  
-ANISOU 5591  N   GLN C 728     6469   6907   5587   1102    214      7       N  
-ATOM   5592  CA  GLN C 728     -50.988  13.394 -41.529  1.00 48.30           C  
-ANISOU 5592  CA  GLN C 728     6347   6591   5412   1050    211     -8       C  
-ATOM   5593  C   GLN C 728     -51.847  14.617 -41.271  1.00 45.90           C  
-ANISOU 5593  C   GLN C 728     5996   6280   5162    941    183    -14       C  
-ATOM   5594  O   GLN C 728     -52.978  14.705 -41.768  1.00 42.64           O  
-ANISOU 5594  O   GLN C 728     5623   5802   4777    877    178    -30       O  
-ATOM   5595  CB  GLN C 728     -51.137  12.413 -40.365  1.00 46.12           C  
-ANISOU 5595  CB  GLN C 728     6137   6265   5121   1104    223      0       C  
-ATOM   5596  N   ILE C 729     -51.316  15.578 -40.538  1.00 43.04           N  
-ANISOU 5596  N   ILE C 729     5550   5990   4814    920    165     -3       N  
-ATOM   5597  CA  ILE C 729     -52.137  16.705 -40.231  1.00 45.07           C  
-ANISOU 5597  CA  ILE C 729     5772   6231   5121    824    144     -8       C  
-ATOM   5598  C   ILE C 729     -52.252  17.639 -41.437  1.00 43.79           C  
-ANISOU 5598  C   ILE C 729     5569   6089   4978    768    143    -10       C  
-ATOM   5599  O   ILE C 729     -53.254  18.315 -41.595  1.00 39.49           O  
-ANISOU 5599  O   ILE C 729     5029   5505   4472    695    133    -16       O  
-ATOM   5600  CB  ILE C 729     -51.725  17.469 -38.958  1.00 47.88           C  
-ANISOU 5600  CB  ILE C 729     6061   6643   5490    807    126     -2       C  
-ATOM   5601  CG1 ILE C 729     -50.896  18.659 -39.317  1.00 49.74           C  
-ANISOU 5601  CG1 ILE C 729     6199   6964   5734    773    121      0       C  
-ATOM   5602  CG2 ILE C 729     -51.002  16.633 -37.894  1.00 50.51           C  
-ANISOU 5602  CG2 ILE C 729     6403   7007   5783    892    129      8       C  
-ATOM   5603  CD1 ILE C 729     -50.659  19.522 -38.120  1.00 56.12           C  
-ANISOU 5603  CD1 ILE C 729     6944   7818   6560    735    103     -4       C  
-ATOM   5604  N   LEU C 730     -51.242  17.667 -42.299  1.00 46.60           N  
-ANISOU 5604  N   LEU C 730     5889   6510   5308    808    157     -4       N  
-ATOM   5605  CA  LEU C 730     -51.392  18.354 -43.568  1.00 44.57           C  
-ANISOU 5605  CA  LEU C 730     5611   6264   5062    768    163     -3       C  
-ATOM   5606  C   LEU C 730     -52.568  17.780 -44.352  1.00 39.96           C  
-ANISOU 5606  C   LEU C 730     5105   5599   4478    750    164    -18       C  
-ATOM   5607  O   LEU C 730     -53.346  18.527 -44.912  1.00 38.95           O  
-ANISOU 5607  O   LEU C 730     4969   5453   4376    688    158    -19       O  
-ATOM   5608  CB  LEU C 730     -50.133  18.239 -44.400  1.00 46.45           C  
-ANISOU 5608  CB  LEU C 730     5808   6578   5262    825    182      7       C  
-ATOM   5609  CG  LEU C 730     -50.336  18.751 -45.833  1.00 50.33           C  
-ANISOU 5609  CG  LEU C 730     6292   7075   5757    797    194     10       C  
-ATOM   5610  CD1 LEU C 730     -50.514  20.270 -45.859  1.00 51.25           C  
-ANISOU 5610  CD1 LEU C 730     6342   7215   5917    714    190     22       C  
-ATOM   5611  CD2 LEU C 730     -49.184  18.294 -46.724  1.00 52.98           C  
-ANISOU 5611  CD2 LEU C 730     6610   7475   6046    870    217     18       C  
-ATOM   5612  N   ASP C 731     -52.647  16.457 -44.456  1.00 39.05           N  
-ANISOU 5612  N   ASP C 731     5066   5439   4331    807    176    -31       N  
-ATOM   5613  CA  ASP C 731     -53.740  15.834 -45.219  1.00 37.41           C  
-ANISOU 5613  CA  ASP C 731     4935   5158   4121    785    178    -54       C  
-ATOM   5614  C   ASP C 731     -55.100  16.182 -44.628  1.00 35.22           C  
-ANISOU 5614  C   ASP C 731     4676   4821   3885    708    159    -62       C  
-ATOM   5615  O   ASP C 731     -56.052  16.361 -45.360  1.00 35.66           O  
-ANISOU 5615  O   ASP C 731     4750   4850   3951    660    152    -76       O  
-ATOM   5616  CB  ASP C 731     -53.606  14.298 -45.259  1.00 37.58           C  
-ANISOU 5616  CB  ASP C 731     5046   5130   4105    855    199    -70       C  
-ATOM   5617  N   LEU C 732     -55.193  16.235 -43.290  1.00 36.33           N  
-ANISOU 5617  N   LEU C 732     4812   4947   4046    701    151    -54       N  
-ATOM   5618  CA  LEU C 732     -56.455  16.548 -42.635  1.00 34.36           C  
-ANISOU 5618  CA  LEU C 732     4578   4643   3834    633    135    -60       C  
-ATOM   5619  C   LEU C 732     -56.822  18.003 -42.895  1.00 32.22           C  
-ANISOU 5619  C   LEU C 732     4240   4405   3597    567    120    -50       C  
-ATOM   5620  O   LEU C 732     -57.958  18.299 -43.233  1.00 31.66           O  
-ANISOU 5620  O   LEU C 732     4182   4301   3544    513    111    -58       O  
-ATOM   5621  CB  LEU C 732     -56.375  16.263 -41.142  1.00 34.23           C  
-ANISOU 5621  CB  LEU C 732     4571   4609   3824    650    133    -52       C  
-ATOM   5622  CG  LEU C 732     -56.290  14.784 -40.779  1.00 34.79           C  
-ANISOU 5622  CG  LEU C 732     4726   4627   3866    712    153    -59       C  
-ATOM   5623  CD1 LEU C 732     -55.935  14.648 -39.315  1.00 34.62           C  
-ANISOU 5623  CD1 LEU C 732     4698   4612   3843    745    153    -41       C  
-ATOM   5624  CD2 LEU C 732     -57.590  14.030 -41.099  1.00 34.60           C  
-ANISOU 5624  CD2 LEU C 732     4782   4514   3852    671    160    -83       C  
-ATOM   5625  N   SER C 733     -55.838  18.892 -42.808  1.00 30.77           N  
-ANISOU 5625  N   SER C 733     3985   4289   3417    573    121    -32       N  
-ATOM   5626  CA  SER C 733     -56.016  20.287 -43.161  1.00 31.34           C  
-ANISOU 5626  CA  SER C 733     3999   4390   3518    516    117    -20       C  
-ATOM   5627  C   SER C 733     -56.607  20.435 -44.558  1.00 32.39           C  
-ANISOU 5627  C   SER C 733     4146   4516   3644    499    121    -22       C  
-ATOM   5628  O   SER C 733     -57.598  21.166 -44.782  1.00 32.52           O  
-ANISOU 5628  O   SER C 733     4157   4514   3685    446    114    -18       O  
-ATOM   5629  CB  SER C 733     -54.687  21.016 -43.104  1.00 32.79           C  
-ANISOU 5629  CB  SER C 733     4109   4649   3699    530    126     -6       C  
-ATOM   5630  OG  SER C 733     -54.822  22.259 -42.496  1.00 33.41           O  
-ANISOU 5630  OG  SER C 733     4140   4739   3816    472    121      2       O  
-ATOM   5631  N   ASN C 734     -56.028  19.715 -45.508  1.00 34.80           N  
-ANISOU 5631  N   ASN C 734     4470   4840   3911    548    134    -28       N  
-ATOM   5632  CA  ASN C 734     -56.496  19.748 -46.892  1.00 35.68           C  
-ANISOU 5632  CA  ASN C 734     4596   4956   4006    542    138    -33       C  
-ATOM   5633  C   ASN C 734     -57.852  19.125 -47.048  1.00 36.77           C  
-ANISOU 5633  C   ASN C 734     4793   5034   4143    512    125    -58       C  
-ATOM   5634  O   ASN C 734     -58.650  19.593 -47.881  1.00 38.18           O  
-ANISOU 5634  O   ASN C 734     4967   5218   4322    480    120    -59       O  
-ATOM   5635  CB  ASN C 734     -55.501  19.057 -47.830  1.00 36.81           C  
-ANISOU 5635  CB  ASN C 734     4749   5134   4103    607    156    -37       C  
-ATOM   5636  CG  ASN C 734     -54.186  19.831 -47.944  1.00 39.73           C  
-ANISOU 5636  CG  ASN C 734     5046   5578   4471    628    171    -10       C  
-ATOM   5637  OD1 ASN C 734     -54.144  21.043 -47.729  1.00 39.07           O  
-ANISOU 5637  OD1 ASN C 734     4907   5519   4420    582    172     10       O  
-ATOM   5638  ND2 ASN C 734     -53.105  19.124 -48.234  1.00 40.54           N  
-ANISOU 5638  ND2 ASN C 734     5149   5717   4536    695    187    -11       N  
-ATOM   5639  N   ARG C 735     -58.140  18.077 -46.278  1.00 36.07           N  
-ANISOU 5639  N   ARG C 735     4760   4893   4052    524    123    -78       N  
-ATOM   5640  CA  ARG C 735     -59.461  17.472 -46.357  1.00 38.92           C  
-ANISOU 5640  CA  ARG C 735     5175   5197   4416    485    114   -105       C  
-ATOM   5641  C   ARG C 735     -60.512  18.523 -45.938  1.00 34.60           C  
-ANISOU 5641  C   ARG C 735     4593   4646   3907    419     96    -93       C  
-ATOM   5642  O   ARG C 735     -61.590  18.638 -46.533  1.00 34.41           O  
-ANISOU 5642  O   ARG C 735     4576   4615   3882    380     86   -105       O  
-ATOM   5643  CB  ARG C 735     -59.543  16.194 -45.528  1.00 46.99           C  
-ANISOU 5643  CB  ARG C 735     6266   6156   5432    507    122   -124       C  
-ATOM   5644  CG  ARG C 735     -60.563  15.171 -46.027  1.00 58.45           C  
-ANISOU 5644  CG  ARG C 735     7789   7551   6869    481    124   -164       C  
-ATOM   5645  CD  ARG C 735     -60.551  13.875 -45.197  1.00 62.27           C  
-ANISOU 5645  CD  ARG C 735     8350   7962   7347    506    143   -179       C  
-ATOM   5646  NE  ARG C 735     -59.359  13.080 -45.453  1.00 64.85           N  
-ANISOU 5646  NE  ARG C 735     8710   8293   7637    588    167   -178       N  
-ATOM   5647  CZ  ARG C 735     -59.192  12.287 -46.512  1.00 71.39           C  
-ANISOU 5647  CZ  ARG C 735     9587   9109   8429    614    183   -207       C  
-ATOM   5648  NH1 ARG C 735     -60.147  12.166 -47.432  1.00 73.62           N  
-ANISOU 5648  NH1 ARG C 735     9890   9379   8705    562    174   -242       N  
-ATOM   5649  NH2 ARG C 735     -58.055  11.612 -46.666  1.00 71.83           N  
-ANISOU 5649  NH2 ARG C 735     9671   9172   8450    697    207   -201       N  
-ATOM   5650  N   PHE C 736     -60.189  19.304 -44.925  1.00 30.84           N  
-ANISOU 5650  N   PHE C 736     4076   4180   3462    409     94    -69       N  
-ATOM   5651  CA  PHE C 736     -61.111  20.339 -44.459  1.00 30.17           C  
-ANISOU 5651  CA  PHE C 736     3962   4090   3413    354     82    -56       C  
-ATOM   5652  C   PHE C 736     -61.381  21.390 -45.541  1.00 28.43           C  
-ANISOU 5652  C   PHE C 736     3702   3909   3193    334     83    -39       C  
-ATOM   5653  O   PHE C 736     -62.531  21.708 -45.834  1.00 29.65           O  
-ANISOU 5653  O   PHE C 736     3857   4056   3354    299     74    -41       O  
-ATOM   5654  CB  PHE C 736     -60.577  21.026 -43.209  1.00 28.79           C  
-ANISOU 5654  CB  PHE C 736     3751   3922   3267    349     82    -37       C  
-ATOM   5655  CG  PHE C 736     -61.450  22.131 -42.739  1.00 27.16           C  
-ANISOU 5655  CG  PHE C 736     3517   3707   3096    298     74    -23       C  
-ATOM   5656  CD1 PHE C 736     -62.540  21.849 -41.950  1.00 26.12           C  
-ANISOU 5656  CD1 PHE C 736     3413   3532   2981    268     64    -32       C  
-ATOM   5657  CD2 PHE C 736     -61.229  23.460 -43.136  1.00 27.31           C  
-ANISOU 5657  CD2 PHE C 736     3486   3760   3131    279     83      0       C  
-ATOM   5658  CE1 PHE C 736     -63.391  22.854 -41.551  1.00 24.79           C  
-ANISOU 5658  CE1 PHE C 736     3221   3357   2842    227     59    -18       C  
-ATOM   5659  CE2 PHE C 736     -62.094  24.478 -42.745  1.00 25.83           C  
-ANISOU 5659  CE2 PHE C 736     3282   3559   2974    238     81     14       C  
-ATOM   5660  CZ  PHE C 736     -63.166  24.171 -41.943  1.00 25.23           C  
-ANISOU 5660  CZ  PHE C 736     3231   3443   2912    214     68      5       C  
-ATOM   5661  N   TYR C 737     -60.323  21.892 -46.146  1.00 27.65           N  
-ANISOU 5661  N   TYR C 737     3567   3855   3083    361     97    -22       N  
-ATOM   5662  CA  TYR C 737     -60.448  22.881 -47.218  1.00 31.13           C  
-ANISOU 5662  CA  TYR C 737     3975   4334   3520    352    106      0       C  
-ATOM   5663  C   TYR C 737     -61.129  22.368 -48.475  1.00 34.04           C  
-ANISOU 5663  C   TYR C 737     4369   4713   3852    360    101    -16       C  
-ATOM   5664  O   TYR C 737     -61.676  23.143 -49.245  1.00 38.15           O  
-ANISOU 5664  O   TYR C 737     4869   5259   4368    347    103      1       O  
-ATOM   5665  CB  TYR C 737     -59.086  23.471 -47.554  1.00 29.39           C  
-ANISOU 5665  CB  TYR C 737     3711   4160   3296    377    128     22       C  
-ATOM   5666  CG  TYR C 737     -58.566  24.348 -46.441  1.00 29.05           C  
-ANISOU 5666  CG  TYR C 737     3628   4118   3291    353    134     37       C  
-ATOM   5667  CD1 TYR C 737     -59.285  25.466 -45.997  1.00 29.71           C  
-ANISOU 5667  CD1 TYR C 737     3694   4184   3410    307    135     54       C  
-ATOM   5668  CD2 TYR C 737     -57.374  24.085 -45.832  1.00 29.76           C  
-ANISOU 5668  CD2 TYR C 737     3698   4231   3378    377    139     33       C  
-ATOM   5669  CE1 TYR C 737     -58.821  26.288 -44.971  1.00 28.50           C  
-ANISOU 5669  CE1 TYR C 737     3509   4030   3291    280    142     61       C  
-ATOM   5670  CE2 TYR C 737     -56.907  24.913 -44.817  1.00 28.99           C  
-ANISOU 5670  CE2 TYR C 737     3560   4143   3312    349    142     41       C  
-ATOM   5671  CZ  TYR C 737     -57.626  26.021 -44.410  1.00 28.42           C  
-ANISOU 5671  CZ  TYR C 737     3475   4047   3276    297    144     53       C  
-ATOM   5672  OH  TYR C 737     -57.129  26.852 -43.430  1.00 30.50           O  
-ANISOU 5672  OH  TYR C 737     3701   4317   3568    266    149     54       O  
-ATOM   5673  N   THR C 738     -61.133  21.055 -48.667  1.00 36.69           N  
-ANISOU 5673  N   THR C 738     4754   5028   4159    381     95    -50       N  
-ATOM   5674  CA  THR C 738     -61.888  20.437 -49.737  1.00 37.93           C  
-ANISOU 5674  CA  THR C 738     4941   5189   4280    379     87    -78       C  
-ATOM   5675  C   THR C 738     -63.363  20.414 -49.420  1.00 38.74           C  
-ANISOU 5675  C   THR C 738     5056   5268   4397    327     67    -93       C  
-ATOM   5676  O   THR C 738     -64.171  20.612 -50.317  1.00 43.54           O  
-ANISOU 5676  O   THR C 738     5656   5905   4983    313     58   -100       O  
-ATOM   5677  CB  THR C 738     -61.378  19.000 -49.975  1.00 42.98           C  
-ANISOU 5677  CB  THR C 738     5637   5806   4887    415     93   -114       C  
-ATOM   5678  OG1 THR C 738     -60.025  19.068 -50.454  1.00 41.81           O  
-ANISOU 5678  OG1 THR C 738     5472   5696   4719    469    112    -97       O  
-ATOM   5679  CG2 THR C 738     -62.222  18.257 -50.984  1.00 44.64           C  
-ANISOU 5679  CG2 THR C 738     5887   6016   5060    403     84   -154       C  
-ATOM   5680  N   LEU C 739     -63.734  20.153 -48.161  1.00 36.68           N  
-ANISOU 5680  N   LEU C 739     4810   4958   4168    301     62    -99       N  
-ATOM   5681  CA  LEU C 739     -65.149  20.185 -47.777  1.00 33.69           C  
-ANISOU 5681  CA  LEU C 739     4437   4560   3805    250     45   -110       C  
-ATOM   5682  C   LEU C 739     -65.653  21.599 -47.787  1.00 32.61           C  
-ANISOU 5682  C   LEU C 739     4246   4455   3688    232     42    -73       C  
-ATOM   5683  O   LEU C 739     -66.788  21.827 -48.133  1.00 35.73           O  
-ANISOU 5683  O   LEU C 739     4631   4868   4078    205     30    -78       O  
-ATOM   5684  CB  LEU C 739     -65.389  19.690 -46.361  1.00 35.02           C  
-ANISOU 5684  CB  LEU C 739     4631   4670   4004    230     44   -118       C  
-ATOM   5685  CG  LEU C 739     -65.644  18.243 -45.944  1.00 37.82           C  
-ANISOU 5685  CG  LEU C 739     5052   4967   4350    223     48   -156       C  
-ATOM   5686  CD1 LEU C 739     -65.938  17.385 -47.155  1.00 37.83           C  
-ANISOU 5686  CD1 LEU C 739     5088   4976   4312    221     47   -196       C  
-ATOM   5687  CD2 LEU C 739     -64.442  17.691 -45.195  1.00 41.40           C  
-ANISOU 5687  CD2 LEU C 739     5531   5393   4806    271     64   -149       C  
-ATOM   5688  N   ILE C 740     -64.837  22.524 -47.305  1.00 29.13           N  
-ANISOU 5688  N   ILE C 740     3774   4021   3273    246     56    -39       N  
-ATOM   5689  CA  ILE C 740     -65.253  23.898 -47.208  1.00 29.69           C  
-ANISOU 5689  CA  ILE C 740     3804   4110   3368    230     61     -2       C  
-ATOM   5690  C   ILE C 740     -64.250  24.742 -48.010  1.00 31.33           C  
-ANISOU 5690  C   ILE C 740     3981   4357   3567    259     82     28       C  
-ATOM   5691  O   ILE C 740     -63.220  25.161 -47.494  1.00 30.09           O  
-ANISOU 5691  O   ILE C 740     3807   4196   3430    266     98     43       O  
-ATOM   5692  CB  ILE C 740     -65.300  24.356 -45.757  1.00 31.02           C  
-ANISOU 5692  CB  ILE C 740     3966   4242   3580    207     62      9       C  
-ATOM   5693  CG1 ILE C 740     -66.026  23.333 -44.870  1.00 30.12           C  
-ANISOU 5693  CG1 ILE C 740     3888   4085   3472    185     46    -21       C  
-ATOM   5694  CG2 ILE C 740     -65.969  25.711 -45.685  1.00 32.56           C  
-ANISOU 5694  CG2 ILE C 740     4128   4446   3795    189     69     42       C  
-ATOM   5695  CD1 ILE C 740     -67.517  23.268 -45.090  1.00 30.06           C  
-ANISOU 5695  CD1 ILE C 740     3882   4080   3459    152     32    -30       C  
-ATOM   5696  N   PRO C 741     -64.530  24.935 -49.299  1.00 31.74           N  
-ANISOU 5696  N   PRO C 741     4025   4450   3585    275     85     36       N  
-ATOM   5697  CA  PRO C 741     -63.571  25.567 -50.161  1.00 33.34           C  
-ANISOU 5697  CA  PRO C 741     4203   4689   3774    306    110     64       C  
-ATOM   5698  C   PRO C 741     -63.357  27.011 -49.769  1.00 33.63           C  
-ANISOU 5698  C   PRO C 741     4208   4723   3848    293    134    107       C  
-ATOM   5699  O   PRO C 741     -64.327  27.746 -49.551  1.00 34.90           O  
-ANISOU 5699  O   PRO C 741     4361   4875   4024    274    134    126       O  
-ATOM   5700  CB  PRO C 741     -64.184  25.453 -51.561  1.00 34.75           C  
-ANISOU 5700  CB  PRO C 741     4384   4915   3905    325    104     62       C  
-ATOM   5701  CG  PRO C 741     -65.458  24.692 -51.415  1.00 36.12           C  
-ANISOU 5701  CG  PRO C 741     4579   5079   4066    299     74     26       C  
-ATOM   5702  CD  PRO C 741     -65.762  24.499 -49.987  1.00 33.35           C  
-ANISOU 5702  CD  PRO C 741     4239   4674   3758    265     65     15       C  
-ATOM   5703  N   HIS C 742     -62.095  27.393 -49.685  1.00 32.85           N  
-ANISOU 5703  N   HIS C 742     4089   4630   3761    302    158    122       N  
-ATOM   5704  CA  HIS C 742     -61.703  28.744 -49.346  1.00 35.12           C  
-ANISOU 5704  CA  HIS C 742     4348   4910   4084    284    188    157       C  
-ATOM   5705  C   HIS C 742     -60.965  29.374 -50.517  1.00 34.77           C  
-ANISOU 5705  C   HIS C 742     4284   4905   4021    308    222    190       C  
-ATOM   5706  O   HIS C 742     -60.551  28.706 -51.444  1.00 35.86           O  
-ANISOU 5706  O   HIS C 742     4426   5078   4120    342    220    182       O  
-ATOM   5707  CB  HIS C 742     -60.783  28.741 -48.140  1.00 33.45           C  
-ANISOU 5707  CB  HIS C 742     4125   4680   3906    263    190    144       C  
-ATOM   5708  CG  HIS C 742     -61.488  28.556 -46.839  1.00 35.60           C  
-ANISOU 5708  CG  HIS C 742     4411   4909   4205    235    167    125       C  
-ATOM   5709  ND1 HIS C 742     -62.188  27.406 -46.522  1.00 35.48           N  
-ANISOU 5709  ND1 HIS C 742     4428   4877   4175    240    136     95       N  
-ATOM   5710  CD2 HIS C 742     -61.568  29.360 -45.755  1.00 35.11           C  
-ANISOU 5710  CD2 HIS C 742     4339   4819   4183    202    174    131       C  
-ATOM   5711  CE1 HIS C 742     -62.665  27.517 -45.298  1.00 33.33           C  
-ANISOU 5711  CE1 HIS C 742     4162   4570   3933    213    125     88       C  
-ATOM   5712  NE2 HIS C 742     -62.323  28.703 -44.823  1.00 33.59           N  
-ANISOU 5712  NE2 HIS C 742     4169   4596   3997    191    146    108       N  
-ATOM   5713  N   ASP C 743     -60.822  30.678 -50.449  1.00 40.42           N  
-ANISOU 5713  N   ASP C 743     4981   5610   4765    290    257    227       N  
-ATOM   5714  CA  ASP C 743     -60.274  31.483 -51.505  1.00 46.51           C  
-ANISOU 5714  CA  ASP C 743     5736   6410   5525    308    299    266       C  
-ATOM   5715  C   ASP C 743     -59.124  32.235 -50.894  1.00 51.26           C  
-ANISOU 5715  C   ASP C 743     6312   6999   6167    275    332    275       C  
-ATOM   5716  O   ASP C 743     -59.236  33.325 -50.313  1.00 48.59           O  
-ANISOU 5716  O   ASP C 743     5969   6624   5867    239    358    293       O  
-ATOM   5717  CB  ASP C 743     -61.365  32.381 -52.059  1.00 54.88           C  
-ANISOU 5717  CB  ASP C 743     6806   7465   6579    318    316    305       C  
-ATOM   5718  CG  ASP C 743     -61.187  32.677 -53.519  1.00 65.56           C  
-ANISOU 5718  CG  ASP C 743     8155   8864   7891    360    344    341       C  
-ATOM   5719  OD1 ASP C 743     -60.022  32.899 -53.965  1.00 62.53           O  
-ANISOU 5719  OD1 ASP C 743     7754   8498   7507    366    376    355       O  
-ATOM   5720  OD2 ASP C 743     -62.244  32.663 -54.209  1.00 72.32           O  
-ANISOU 5720  OD2 ASP C 743     9022   9744   8713    390    332    354       O  
-ATOM   5721  N   PHE C 744     -57.995  31.562 -50.950  1.00 64.78           N  
-ANISOU 5721  N   PHE C 744     8005   8742   7866    286    329    255       N  
-ATOM   5722  CA  PHE C 744     -56.722  32.205 -50.749  1.00 72.06           C  
-ANISOU 5722  CA  PHE C 744     8890   9677   8811    261    364    264       C  
-ATOM   5723  C   PHE C 744     -56.612  33.368 -51.758  1.00 71.32           C  
-ANISOU 5723  C   PHE C 744     8790   9589   8720    261    419    315       C  
-ATOM   5724  O   PHE C 744     -57.090  33.261 -52.904  1.00 73.15           O  
-ANISOU 5724  O   PHE C 744     9038   9843   8914    304    425    339       O  
-ATOM   5725  CB  PHE C 744     -55.617  31.170 -50.988  1.00 76.94           C  
-ANISOU 5725  CB  PHE C 744     9489  10346   9400    292    353    242       C  
-ATOM   5726  CG  PHE C 744     -55.544  30.659 -52.411  1.00 82.79           C  
-ANISOU 5726  CG  PHE C 744    10239  11127  10090    346    360    256       C  
-ATOM   5727  CD1 PHE C 744     -54.664  31.238 -53.328  1.00 85.58           C  
-ANISOU 5727  CD1 PHE C 744    10565  11519  10433    357    405    288       C  
-ATOM   5728  CD2 PHE C 744     -56.343  29.601 -52.836  1.00 88.40           C  
-ANISOU 5728  CD2 PHE C 744    10986  11839  10761    384    323    234       C  
-ATOM   5729  CE1 PHE C 744     -54.585  30.776 -54.630  1.00 88.75           C  
-ANISOU 5729  CE1 PHE C 744    10975  11961  10783    410    412    301       C  
-ATOM   5730  CE2 PHE C 744     -56.266  29.133 -54.140  1.00 93.36           C  
-ANISOU 5730  CE2 PHE C 744    11626  12508  11340    432    329    241       C  
-ATOM   5731  CZ  PHE C 744     -55.383  29.718 -55.036  1.00 94.66           C  
-ANISOU 5731  CZ  PHE C 744    11761  12713  11491    448    372    276       C  
-ATOM   5732  N   GLY C 745     -56.018  34.478 -51.334  1.00 64.20           N  
-ANISOU 5732  N   GLY C 745     7868   8667   7860    214    461    330       N  
-ATOM   5733  CA  GLY C 745     -55.527  35.459 -52.297  1.00 63.18           C  
-ANISOU 5733  CA  GLY C 745     7728   8547   7731    213    523    377       C  
-ATOM   5734  C   GLY C 745     -54.037  35.233 -52.503  1.00 61.50           C  
-ANISOU 5734  C   GLY C 745     7469   8385   7513    205    542    368       C  
-ATOM   5735  O   GLY C 745     -53.621  34.313 -53.201  1.00 60.60           O  
-ANISOU 5735  O   GLY C 745     7346   8323   7356    253    526    362       O  
-ATOM   5736  N   MET C 746     -53.244  36.045 -51.826  1.00 62.35           N  
-ANISOU 5736  N   MET C 746     7546   8481   7663    143    574    363       N  
-ATOM   5737  CA  MET C 746     -51.781  36.035 -51.926  1.00 64.90           C  
-ANISOU 5737  CA  MET C 746     7814   8858   7987    123    599    355       C  
-ATOM   5738  C   MET C 746     -51.128  34.875 -51.154  1.00 65.87           C  
-ANISOU 5738  C   MET C 746     7905   9029   8094    136    547    305       C  
-ATOM   5739  O   MET C 746     -50.218  34.223 -51.668  1.00 67.59           O  
-ANISOU 5739  O   MET C 746     8090   9312   8280    170    547    302       O  
-ATOM   5740  CB  MET C 746     -51.248  37.360 -51.370  1.00 62.07           C  
-ANISOU 5740  CB  MET C 746     7433   8468   7681     41    652    359       C  
-ATOM   5741  CG  MET C 746     -50.070  37.885 -52.127  1.00 63.33           C  
-ANISOU 5741  CG  MET C 746     7552   8670   7842     21    712    383       C  
-ATOM   5742  SD  MET C 746     -49.669  39.588 -51.724  1.00 66.34           S  
-ANISOU 5742  SD  MET C 746     7925   8994   8287    -81    790    396       S  
-ATOM   5743  CE  MET C 746     -51.249  40.390 -51.982  1.00 62.27           C  
-ANISOU 5743  CE  MET C 746     7494   8381   7785    -61    811    440       C  
-ATOM   5744  N   LYS C 747     -51.588  34.667 -49.914  1.00 67.15           N  
-ANISOU 5744  N   LYS C 747     8077   9161   8278    112    507    270       N  
-ATOM   5745  CA  LYS C 747     -51.200  33.536 -49.044  1.00 69.67           C  
-ANISOU 5745  CA  LYS C 747     8378   9514   8579    133    455    225       C  
-ATOM   5746  C   LYS C 747     -52.014  32.294 -49.379  1.00 66.70           C  
-ANISOU 5746  C   LYS C 747     8048   9131   8164    200    411    219       C  
-ATOM   5747  O   LYS C 747     -53.202  32.409 -49.638  1.00 63.65           O  
-ANISOU 5747  O   LYS C 747     7708   8698   7779    208    403    232       O  
-ATOM   5748  CB  LYS C 747     -51.466  33.888 -47.565  1.00 67.06           C  
-ANISOU 5748  CB  LYS C 747     8045   9147   8286     80    435    193       C  
-ATOM   5749  N   LYS C 748     -51.388  31.117 -49.375  1.00 68.57           N  
-ANISOU 5749  N   LYS C 748     8273   9416   8365    248    385    197       N  
-ATOM   5750  CA  LYS C 748     -52.147  29.849 -49.382  1.00 66.74           C  
-ANISOU 5750  CA  LYS C 748     8090   9166   8101    301    341    179       C  
-ATOM   5751  C   LYS C 748     -52.922  29.758 -48.057  1.00 62.20           C  
-ANISOU 5751  C   LYS C 748     7538   8541   7553    273    307    154       C  
-ATOM   5752  O   LYS C 748     -52.556  30.406 -47.074  1.00 55.20           O  
-ANISOU 5752  O   LYS C 748     6621   7653   6699    226    312    143       O  
-ATOM   5753  CB  LYS C 748     -51.229  28.638 -49.548  1.00 66.89           C  
-ANISOU 5753  CB  LYS C 748     8098   9240   8077    361    327    161       C  
-ATOM   5754  N   PRO C 749     -54.014  28.972 -48.023  1.00 63.99           N  
-ANISOU 5754  N   PRO C 749     7818   8730   7766    297    276    143       N  
-ATOM   5755  CA  PRO C 749     -54.779  28.923 -46.765  1.00 61.16           C  
-ANISOU 5755  CA  PRO C 749     7480   8325   7434    269    248    123       C  
-ATOM   5756  C   PRO C 749     -53.944  28.367 -45.596  1.00 50.94           C  
-ANISOU 5756  C   PRO C 749     6161   7054   6138    275    230     95       C  
-ATOM   5757  O   PRO C 749     -53.086  27.521 -45.817  1.00 55.90           O  
-ANISOU 5757  O   PRO C 749     6779   7728   6734    322    226     87       O  
-ATOM   5758  CB  PRO C 749     -55.953  27.999 -47.076  1.00 62.83           C  
-ANISOU 5758  CB  PRO C 749     7748   8502   7624    298    221    114       C  
-ATOM   5759  CG  PRO C 749     -55.941  27.764 -48.557  1.00 63.71           C  
-ANISOU 5759  CG  PRO C 749     7868   8638   7699    334    234    129       C  
-ATOM   5760  CD  PRO C 749     -54.563  28.082 -49.062  1.00 64.72           C  
-ANISOU 5760  CD  PRO C 749     7952   8823   7818    346    264    143       C  
-ATOM   5761  N   PRO C 750     -54.172  28.872 -44.376  1.00 45.60           N  
-ANISOU 5761  N   PRO C 750     5477   6354   5494    233    220     82       N  
-ATOM   5762  CA  PRO C 750     -53.445  28.446 -43.168  1.00 46.12           C  
-ANISOU 5762  CA  PRO C 750     5517   6449   5555    239    201     56       C  
-ATOM   5763  C   PRO C 750     -53.447  26.943 -42.891  1.00 44.27           C  
-ANISOU 5763  C   PRO C 750     5316   6218   5285    302    173     41       C  
-ATOM   5764  O   PRO C 750     -54.498  26.302 -43.012  1.00 44.11           O  
-ANISOU 5764  O   PRO C 750     5353   6147   5260    317    158     40       O  
-ATOM   5765  CB  PRO C 750     -54.230  29.105 -42.024  1.00 47.78           C  
-ANISOU 5765  CB  PRO C 750     5739   6613   5802    189    190     46       C  
-ATOM   5766  CG  PRO C 750     -55.239  30.015 -42.629  1.00 45.53           C  
-ANISOU 5766  CG  PRO C 750     5479   6277   5544    156    209     69       C  
-ATOM   5767  CD  PRO C 750     -55.210  29.894 -44.106  1.00 44.28           C  
-ANISOU 5767  CD  PRO C 750     5328   6133   5364    184    228     93       C  
-ATOM   5768  N   LEU C 751     -52.309  26.406 -42.471  1.00 39.93           N  
-ANISOU 5768  N   LEU C 751     4733   5728   4711    338    169     30       N  
-ATOM   5769  CA  LEU C 751     -52.248  25.037 -41.992  1.00 42.49           C  
-ANISOU 5769  CA  LEU C 751     5093   6052   5001    402    148     18       C  
-ATOM   5770  C   LEU C 751     -53.020  24.946 -40.672  1.00 40.11           C  
-ANISOU 5770  C   LEU C 751     4817   5705   4717    382    126      5       C  
-ATOM   5771  O   LEU C 751     -52.806  25.765 -39.779  1.00 37.63           O  
-ANISOU 5771  O   LEU C 751     4464   5407   4425    340    122     -4       O  
-ATOM   5772  CB  LEU C 751     -50.792  24.608 -41.763  1.00 45.31           C  
-ANISOU 5772  CB  LEU C 751     5398   6494   5325    450    151     14       C  
-ATOM   5773  CG  LEU C 751     -50.569  23.110 -41.512  1.00 47.66           C  
-ANISOU 5773  CG  LEU C 751     5737   6794   5578    536    141      9       C  
-ATOM   5774  CD1 LEU C 751     -51.108  22.278 -42.671  1.00 48.15           C  
-ANISOU 5774  CD1 LEU C 751     5864   6810   5620    573    149     15       C  
-ATOM   5775  CD2 LEU C 751     -49.082  22.850 -41.322  1.00 50.23           C  
-ANISOU 5775  CD2 LEU C 751     6000   7217   5867    587    146      9       C  
-ATOM   5776  N   LEU C 752     -53.897  23.947 -40.565  1.00 35.23           N  
-ANISOU 5776  N   LEU C 752     4266   5031   4088    411    113      2       N  
-ATOM   5777  CA  LEU C 752     -54.672  23.736 -39.355  1.00 36.00           C  
-ANISOU 5777  CA  LEU C 752     4394   5083   4199    399     95     -8       C  
-ATOM   5778  C   LEU C 752     -53.941  22.803 -38.368  1.00 40.25           C  
-ANISOU 5778  C   LEU C 752     4934   5653   4705    458     86    -15       C  
-ATOM   5779  O   LEU C 752     -54.179  21.604 -38.339  1.00 42.24           O  
-ANISOU 5779  O   LEU C 752     5242   5873   4932    509     85    -15       O  
-ATOM   5780  CB  LEU C 752     -56.049  23.190 -39.698  1.00 33.61           C  
-ANISOU 5780  CB  LEU C 752     4161   4706   3904    391     90     -7       C  
-ATOM   5781  CG  LEU C 752     -56.839  24.108 -40.640  1.00 32.33           C  
-ANISOU 5781  CG  LEU C 752     3996   4523   3767    341     98      3       C  
-ATOM   5782  CD1 LEU C 752     -58.109  23.442 -41.053  1.00 31.23           C  
-ANISOU 5782  CD1 LEU C 752     3915   4326   3624    338     91     -1       C  
-ATOM   5783  CD2 LEU C 752     -57.111  25.468 -40.003  1.00 31.75           C  
-ANISOU 5783  CD2 LEU C 752     3887   4445   3732    282    100      8       C  
-ATOM   5784  N   ASN C 753     -53.015  23.374 -37.606  1.00 39.41           N  
-ANISOU 5784  N   ASN C 753     4765   5613   4598    452     81    -22       N  
-ATOM   5785  CA  ASN C 753     -52.088  22.602 -36.804  1.00 43.76           C  
-ANISOU 5785  CA  ASN C 753     5300   6220   5109    517     74    -26       C  
-ATOM   5786  C   ASN C 753     -51.985  23.121 -35.365  1.00 42.22           C  
-ANISOU 5786  C   ASN C 753     5070   6051   4920    493     56    -40       C  
-ATOM   5787  O   ASN C 753     -51.069  22.772 -34.651  1.00 44.31           O  
-ANISOU 5787  O   ASN C 753     5299   6386   5150    540     48    -45       O  
-ATOM   5788  CB  ASN C 753     -50.697  22.565 -37.466  1.00 46.10           C  
-ANISOU 5788  CB  ASN C 753     5537   6605   5374    555     85    -22       C  
-ATOM   5789  CG  ASN C 753     -49.960  23.891 -37.403  1.00 49.16           C  
-ANISOU 5789  CG  ASN C 753     5837   7061   5783    492     89    -32       C  
-ATOM   5790  OD1 ASN C 753     -50.551  24.950 -37.214  1.00 43.46           O  
-ANISOU 5790  OD1 ASN C 753     5106   6304   5103    415     89    -39       O  
-ATOM   5791  ND2 ASN C 753     -48.638  23.826 -37.575  1.00 51.69           N  
-ANISOU 5791  ND2 ASN C 753     6092   7478   6072    526     95    -34       N  
-ATOM   5792  N   ASN C 754     -52.919  23.967 -34.968  1.00 38.31           N  
-ANISOU 5792  N   ASN C 754     4585   5506   4466    424     51    -46       N  
-ATOM   5793  CA  ASN C 754     -52.893  24.558 -33.647  1.00 40.22           C  
-ANISOU 5793  CA  ASN C 754     4797   5769   4715    395     36    -63       C  
-ATOM   5794  C   ASN C 754     -54.326  24.882 -33.215  1.00 39.46           C  
-ANISOU 5794  C   ASN C 754     4751   5585   4654    350     32    -62       C  
-ATOM   5795  O   ASN C 754     -55.242  24.942 -34.032  1.00 39.57           O  
-ANISOU 5795  O   ASN C 754     4806   5536   4692    327     42    -50       O  
-ATOM   5796  CB  ASN C 754     -52.013  25.815 -33.621  1.00 39.80           C  
-ANISOU 5796  CB  ASN C 754     4662   5785   4677    337     40    -82       C  
-ATOM   5797  CG  ASN C 754     -52.565  26.920 -34.475  1.00 39.56           C  
-ANISOU 5797  CG  ASN C 754     4632   5706   4693    264     60    -77       C  
-ATOM   5798  OD1 ASN C 754     -53.391  27.724 -34.028  1.00 39.25           O  
-ANISOU 5798  OD1 ASN C 754     4609   5616   4689    208     61    -83       O  
-ATOM   5799  ND2 ASN C 754     -52.127  26.968 -35.725  1.00 41.83           N  
-ANISOU 5799  ND2 ASN C 754     4906   6009   4980    268     79    -63       N  
-ATOM   5800  N   ALA C 755     -54.492  25.087 -31.927  1.00 35.71           N  
-ANISOU 5800  N   ALA C 755     4271   5118   4179    341     18    -75       N  
-ATOM   5801  CA  ALA C 755     -55.790  25.250 -31.343  1.00 33.33           C  
-ANISOU 5801  CA  ALA C 755     4018   4743   3904    311     15    -72       C  
-ATOM   5802  C   ALA C 755     -56.502  26.517 -31.857  1.00 34.36           C  
-ANISOU 5802  C   ALA C 755     4143   4831   4082    234     27    -73       C  
-ATOM   5803  O   ALA C 755     -57.689  26.481 -32.143  1.00 31.38           O  
-ANISOU 5803  O   ALA C 755     3811   4385   3726    218     31    -60       O  
-ATOM   5804  CB  ALA C 755     -55.654  25.271 -29.818  1.00 31.83           C  
-ANISOU 5804  CB  ALA C 755     3816   4582   3697    322     -1    -87       C  
-ATOM   5805  N   ASP C 756     -55.782  27.626 -31.954  1.00 35.37           N  
-ANISOU 5805  N   ASP C 756     4215   5001   4225    189     34    -88       N  
-ATOM   5806  CA  ASP C 756     -56.361  28.903 -32.406  1.00 35.52           C  
-ANISOU 5806  CA  ASP C 756     4231   4977   4287    120     53    -87       C  
-ATOM   5807  C   ASP C 756     -56.932  28.818 -33.837  1.00 33.23           C  
-ANISOU 5807  C   ASP C 756     3970   4645   4010    122     69    -59       C  
-ATOM   5808  O   ASP C 756     -58.070  29.264 -34.082  1.00 32.67           O  
-ANISOU 5808  O   ASP C 756     3933   4515   3964     96     78    -46       O  
-ATOM   5809  CB  ASP C 756     -55.302  30.050 -32.289  1.00 39.31           C  
-ANISOU 5809  CB  ASP C 756     4646   5511   4778     68     65   -111       C  
-ATOM   5810  CG  ASP C 756     -55.190  30.629 -30.866  1.00 45.93           C  
-ANISOU 5810  CG  ASP C 756     5465   6369   5619     37     53   -144       C  
-ATOM   5811  OD1 ASP C 756     -54.433  31.611 -30.727  1.00 51.88           O  
-ANISOU 5811  OD1 ASP C 756     6169   7160   6385    -17     65   -170       O  
-ATOM   5812  OD2 ASP C 756     -55.838  30.147 -29.895  1.00 49.28           O  
-ANISOU 5812  OD2 ASP C 756     5921   6772   6032     61     34   -146       O  
-ATOM   5813  N   SER C 757     -56.186  28.203 -34.754  1.00 30.34           N  
-ANISOU 5813  N   SER C 757     3591   4315   3620    158     74    -51       N  
-ATOM   5814  CA  SER C 757     -56.678  28.034 -36.131  1.00 30.98           C  
-ANISOU 5814  CA  SER C 757     3699   4367   3705    166     87    -28       C  
-ATOM   5815  C   SER C 757     -57.886  27.088 -36.200  1.00 28.94           C  
-ANISOU 5815  C   SER C 757     3504   4051   3440    191     75    -19       C  
-ATOM   5816  O   SER C 757     -58.822  27.352 -36.932  1.00 28.18           O  
-ANISOU 5816  O   SER C 757     3433   3916   3360    173     83     -5       O  
-ATOM   5817  CB  SER C 757     -55.604  27.504 -37.032  1.00 32.54           C  
-ANISOU 5817  CB  SER C 757     3872   4617   3874    204     94    -24       C  
-ATOM   5818  OG  SER C 757     -54.467  28.341 -36.982  1.00 36.73           O  
-ANISOU 5818  OG  SER C 757     4339   5207   4410    176    107    -34       O  
-ATOM   5819  N   VAL C 758     -57.900  26.062 -35.360  1.00 27.59           N  
-ANISOU 5819  N   VAL C 758     3358   3878   3248    230     59    -27       N  
-ATOM   5820  CA  VAL C 758     -59.009  25.110 -35.325  1.00 28.60           C  
-ANISOU 5820  CA  VAL C 758     3546   3949   3370    247     52    -22       C  
-ATOM   5821  C   VAL C 758     -60.258  25.796 -34.810  1.00 27.58           C  
-ANISOU 5821  C   VAL C 758     3432   3773   3273    201     50    -19       C  
-ATOM   5822  O   VAL C 758     -61.332  25.724 -35.433  1.00 27.69           O  
-ANISOU 5822  O   VAL C 758     3475   3748   3297    186     53     -9       O  
-ATOM   5823  CB  VAL C 758     -58.677  23.873 -34.478  1.00 27.82           C  
-ANISOU 5823  CB  VAL C 758     3475   3854   3241    301     43    -27       C  
-ATOM   5824  CG1 VAL C 758     -59.898  23.011 -34.276  1.00 28.44           C  
-ANISOU 5824  CG1 VAL C 758     3617   3866   3321    305     42    -24       C  
-ATOM   5825  CG2 VAL C 758     -57.591  23.055 -35.183  1.00 29.52           C  
-ANISOU 5825  CG2 VAL C 758     3686   4110   3421    358     49    -26       C  
-ATOM   5826  N   GLN C 759     -60.098  26.497 -33.700  1.00 27.15           N  
-ANISOU 5826  N   GLN C 759     3355   3729   3231    180     46    -28       N  
-ATOM   5827  CA  GLN C 759     -61.186  27.238 -33.063  1.00 27.54           C  
-ANISOU 5827  CA  GLN C 759     3417   3738   3308    141     47    -26       C  
-ATOM   5828  C   GLN C 759     -61.839  28.249 -34.019  1.00 23.99           C  
-ANISOU 5828  C   GLN C 759     2964   3267   2886    104     64    -11       C  
-ATOM   5829  O   GLN C 759     -63.043  28.314 -34.108  1.00 23.58           O  
-ANISOU 5829  O   GLN C 759     2937   3176   2846     92     64      0       O  
-ATOM   5830  CB  GLN C 759     -60.634  27.986 -31.841  1.00 31.66           C  
-ANISOU 5830  CB  GLN C 759     3909   4286   3837    123     43    -44       C  
-ATOM   5831  CG  GLN C 759     -61.662  28.488 -30.849  1.00 34.16           C  
-ANISOU 5831  CG  GLN C 759     4244   4563   4172     97     42    -46       C  
-ATOM   5832  CD  GLN C 759     -60.989  29.251 -29.713  1.00 37.73           C  
-ANISOU 5832  CD  GLN C 759     4664   5047   4624     78     38    -71       C  
-ATOM   5833  OE1 GLN C 759     -59.840  28.919 -29.337  1.00 40.48           O  
-ANISOU 5833  OE1 GLN C 759     4981   5453   4947     99     28    -87       O  
-ATOM   5834  NE2 GLN C 759     -61.666  30.292 -29.170  1.00 34.86           N  
-ANISOU 5834  NE2 GLN C 759     4305   4652   4286     38     48    -76       N  
-ATOM   5835  N   ALA C 760     -61.030  28.991 -34.756  1.00 23.85           N  
-ANISOU 5835  N   ALA C 760     2911   3276   2873     90     79     -9       N  
-ATOM   5836  CA  ALA C 760     -61.555  29.938 -35.753  1.00 25.22           C  
-ANISOU 5836  CA  ALA C 760     3084   3431   3068     64    100     12       C  
-ATOM   5837  C   ALA C 760     -62.404  29.234 -36.829  1.00 25.36           C  
-ANISOU 5837  C   ALA C 760     3130   3433   3071     86     96     28       C  
-ATOM   5838  O   ALA C 760     -63.447  29.747 -37.211  1.00 25.55           O  
-ANISOU 5838  O   ALA C 760     3167   3433   3108     72    104     45       O  
-ATOM   5839  CB  ALA C 760     -60.432  30.693 -36.429  1.00 25.05           C  
-ANISOU 5839  CB  ALA C 760     3024   3443   3051     50    122     13       C  
-ATOM   5840  N   LYS C 761     -61.984  28.046 -37.252  1.00 24.87           N  
-ANISOU 5840  N   LYS C 761     3079   3389   2981    121     84     21       N  
-ATOM   5841  CA  LYS C 761     -62.804  27.261 -38.176  1.00 25.13           C  
-ANISOU 5841  CA  LYS C 761     3142   3408   2998    136     78     27       C  
-ATOM   5842  C   LYS C 761     -64.092  26.711 -37.582  1.00 23.02           C  
-ANISOU 5842  C   LYS C 761     2910   3103   2735    127     65     23       C  
-ATOM   5843  O   LYS C 761     -65.114  26.677 -38.269  1.00 21.60           O  
-ANISOU 5843  O   LYS C 761     2743   2913   2553    118     64     30       O  
-ATOM   5844  CB  LYS C 761     -61.989  26.161 -38.842  1.00 25.84           C  
-ANISOU 5844  CB  LYS C 761     3241   3521   3055    176     75     17       C  
-ATOM   5845  CG  LYS C 761     -60.855  26.731 -39.684  1.00 28.62           C  
-ANISOU 5845  CG  LYS C 761     3556   3917   3402    184     91     26       C  
-ATOM   5846  CD  LYS C 761     -61.381  27.694 -40.726  1.00 30.36           C  
-ANISOU 5846  CD  LYS C 761     3767   4137   3633    163    107     48       C  
-ATOM   5847  CE  LYS C 761     -60.287  28.167 -41.631  1.00 35.86           C  
-ANISOU 5847  CE  LYS C 761     4430   4874   4321    172    128     59       C  
-ATOM   5848  NZ  LYS C 761     -60.490  29.601 -41.896  1.00 41.59           N  
-ANISOU 5848  NZ  LYS C 761     5137   5593   5074    139    154     82       N  
-ATOM   5849  N   VAL C 762     -64.060  26.283 -36.324  1.00 24.34           N  
-ANISOU 5849  N   VAL C 762     3089   3254   2904    131     56     12       N  
-ATOM   5850  CA  VAL C 762     -65.279  25.775 -35.656  1.00 23.85           C  
-ANISOU 5850  CA  VAL C 762     3060   3156   2848    120     49     10       C  
-ATOM   5851  C   VAL C 762     -66.322  26.890 -35.538  1.00 26.36           C  
-ANISOU 5851  C   VAL C 762     3365   3460   3190     87     54     24       C  
-ATOM   5852  O   VAL C 762     -67.503  26.718 -35.871  1.00 30.27           O  
-ANISOU 5852  O   VAL C 762     3873   3943   3686     74     52     30       O  
-ATOM   5853  CB  VAL C 762     -64.973  25.228 -34.258  1.00 23.62           C  
-ANISOU 5853  CB  VAL C 762     3045   3115   2815    134     42      0       C  
-ATOM   5854  CG1 VAL C 762     -66.269  24.871 -33.538  1.00 24.13           C  
-ANISOU 5854  CG1 VAL C 762     3139   3142   2889    118     40      2       C  
-ATOM   5855  CG2 VAL C 762     -64.085  24.014 -34.315  1.00 23.57           C  
-ANISOU 5855  CG2 VAL C 762     3058   3117   2779    177     40    -10       C  
-ATOM   5856  N   GLU C 763     -65.878  28.043 -35.084  1.00 28.66           N  
-ANISOU 5856  N   GLU C 763     3631   3759   3500     74     64     29       N  
-ATOM   5857  CA  GLU C 763     -66.731  29.217 -35.005  1.00 31.01           C  
-ANISOU 5857  CA  GLU C 763     3921   4041   3820     50     77     45       C  
-ATOM   5858  C   GLU C 763     -67.300  29.591 -36.361  1.00 26.25           C  
-ANISOU 5858  C   GLU C 763     3312   3448   3213     51     86     66       C  
-ATOM   5859  O   GLU C 763     -68.502  29.888 -36.489  1.00 25.89           O  
-ANISOU 5859  O   GLU C 763     3271   3394   3171     45     89     80       O  
-ATOM   5860  CB  GLU C 763     -65.875  30.405 -34.508  1.00 38.99           C  
-ANISOU 5860  CB  GLU C 763     4908   5056   4849     34     93     42       C  
-ATOM   5861  CG  GLU C 763     -66.439  31.795 -34.847  1.00 53.47           C  
-ANISOU 5861  CG  GLU C 763     6737   6873   6706     15    119     63       C  
-ATOM   5862  CD  GLU C 763     -65.662  32.964 -34.193  1.00 64.04           C  
-ANISOU 5862  CD  GLU C 763     8062   8205   8067    -11    139     53       C  
-ATOM   5863  OE1 GLU C 763     -64.518  33.316 -34.602  1.00 68.38           O  
-ANISOU 5863  OE1 GLU C 763     8589   8774   8618    -21    151     46       O  
-ATOM   5864  OE2 GLU C 763     -66.229  33.553 -33.241  1.00 73.77           O  
-ANISOU 5864  OE2 GLU C 763     9306   9410   9314    -25    145     49       O  
-ATOM   5865  N   MET C 764     -66.460  29.568 -37.386  1.00 22.80           N  
-ANISOU 5865  N   MET C 764     2864   3036   2765     63     92     68       N  
-ATOM   5866  CA  MET C 764     -66.993  29.752 -38.727  1.00 23.95           C  
-ANISOU 5866  CA  MET C 764     3005   3198   2897     72     99     87       C  
-ATOM   5867  C   MET C 764     -68.084  28.732 -39.059  1.00 23.06           C  
-ANISOU 5867  C   MET C 764     2910   3087   2764     75     79     79       C  
-ATOM   5868  O   MET C 764     -69.175  29.102 -39.542  1.00 22.63           O  
-ANISOU 5868  O   MET C 764     2851   3042   2705     72     80     95       O  
-ATOM   5869  CB  MET C 764     -65.920  29.615 -39.758  1.00 27.10           C  
-ANISOU 5869  CB  MET C 764     3392   3626   3279     89    106     88       C  
-ATOM   5870  CG  MET C 764     -66.460  29.713 -41.167  1.00 30.02           C  
-ANISOU 5870  CG  MET C 764     3760   4020   3628    103    111    106       C  
-ATOM   5871  SD  MET C 764     -65.235  29.193 -42.348  1.00 40.99           S  
-ANISOU 5871  SD  MET C 764     5140   5444   4989    129    116    102       S  
-ATOM   5872  CE  MET C 764     -65.439  27.428 -42.224  1.00 37.79           C  
-ANISOU 5872  CE  MET C 764     4766   5034   4558    141     85     66       C  
-ATOM   5873  N   LEU C 765     -67.821  27.464 -38.801  1.00 21.80           N  
-ANISOU 5873  N   LEU C 765     2772   2921   2591     81     63     55       N  
-ATOM   5874  CA  LEU C 765     -68.841  26.437 -39.098  1.00 22.33           C  
-ANISOU 5874  CA  LEU C 765     2860   2984   2641     73     48     40       C  
-ATOM   5875  C   LEU C 765     -70.134  26.672 -38.324  1.00 22.74           C  
-ANISOU 5875  C   LEU C 765     2912   3020   2707     50     45     47       C  
-ATOM   5876  O   LEU C 765     -71.204  26.468 -38.880  1.00 22.07           O  
-ANISOU 5876  O   LEU C 765     2823   2951   2611     38     38     46       O  
-ATOM   5877  CB  LEU C 765     -68.314  25.046 -38.809  1.00 21.89           C  
-ANISOU 5877  CB  LEU C 765     2836   2910   2570     84     40     14       C  
-ATOM   5878  CG  LEU C 765     -67.226  24.489 -39.724  1.00 23.33           C  
-ANISOU 5878  CG  LEU C 765     3024   3110   2728    112     42      4       C  
-ATOM   5879  CD1 LEU C 765     -66.881  23.042 -39.327  1.00 23.19           C  
-ANISOU 5879  CD1 LEU C 765     3050   3066   2696    128     39    -20       C  
-ATOM   5880  CD2 LEU C 765     -67.675  24.539 -41.167  1.00 24.03           C  
-ANISOU 5880  CD2 LEU C 765     3105   3230   2795    112     40      5       C  
-ATOM   5881  N   ASP C 766     -70.039  27.097 -37.058  1.00 23.04           N  
-ANISOU 5881  N   ASP C 766     2952   3035   2769     45     50     51       N  
-ATOM   5882  CA  ASP C 766     -71.245  27.384 -36.273  1.00 25.57           C  
-ANISOU 5882  CA  ASP C 766     3272   3342   3103     27     50     59       C  
-ATOM   5883  C   ASP C 766     -72.095  28.454 -36.968  1.00 27.40           C  
-ANISOU 5883  C   ASP C 766     3478   3598   3335     27     59     85       C  
-ATOM   5884  O   ASP C 766     -73.317  28.306 -37.112  1.00 28.17           O  
-ANISOU 5884  O   ASP C 766     3568   3709   3425     16     54     89       O  
-ATOM   5885  CB  ASP C 766     -70.912  27.886 -34.863  1.00 26.22           C  
-ANISOU 5885  CB  ASP C 766     3358   3399   3206     25     57     61       C  
-ATOM   5886  CG  ASP C 766     -70.190  26.846 -34.015  1.00 31.11           C  
-ANISOU 5886  CG  ASP C 766     4000   4000   3819     34     49     40       C  
-ATOM   5887  OD1 ASP C 766     -70.201  25.621 -34.349  1.00 34.05           O  
-ANISOU 5887  OD1 ASP C 766     4396   4366   4174     38     42     26       O  
-ATOM   5888  OD2 ASP C 766     -69.513  27.271 -33.056  1.00 31.08           O  
-ANISOU 5888  OD2 ASP C 766     3994   3991   3825     40     52     38       O  
-ATOM   5889  N   ASN C 767     -71.434  29.506 -37.444  1.00 25.16           N  
-ANISOU 5889  N   ASN C 767     3180   3321   3057     40     76    103       N  
-ATOM   5890  CA  ASN C 767     -72.141  30.574 -38.141  1.00 24.87           C  
-ANISOU 5890  CA  ASN C 767     3125   3305   3018     51     91    134       C  
-ATOM   5891  C   ASN C 767     -72.693  30.085 -39.493  1.00 23.70           C  
-ANISOU 5891  C   ASN C 767     2966   3202   2839     61     79    136       C  
-ATOM   5892  O   ASN C 767     -73.823  30.410 -39.881  1.00 21.51           O  
-ANISOU 5892  O   ASN C 767     2672   2954   2548     67     79    153       O  
-ATOM   5893  CB  ASN C 767     -71.210  31.779 -38.261  1.00 26.29           C  
-ANISOU 5893  CB  ASN C 767     3302   3473   3216     60    119    152       C  
-ATOM   5894  CG  ASN C 767     -71.901  33.053 -38.788  1.00 31.56           C  
-ANISOU 5894  CG  ASN C 767     3960   4147   3885     78    146    191       C  
-ATOM   5895  OD1 ASN C 767     -73.151  33.257 -38.688  1.00 31.75           O  
-ANISOU 5895  OD1 ASN C 767     3979   4182   3902     86    145    207       O  
-ATOM   5896  ND2 ASN C 767     -71.073  33.961 -39.298  1.00 33.07           N  
-ANISOU 5896  ND2 ASN C 767     4151   4330   4085     85    174    209       N  
-ATOM   5897  N   LEU C 768     -71.918  29.262 -40.193  1.00 23.89           N  
-ANISOU 5897  N   LEU C 768     2996   3236   2845     64     69    116       N  
-ATOM   5898  CA  LEU C 768     -72.395  28.691 -41.469  1.00 26.86           C  
-ANISOU 5898  CA  LEU C 768     3363   3656   3185     71     56    109       C  
-ATOM   5899  C   LEU C 768     -73.648  27.861 -41.260  1.00 27.96           C  
-ANISOU 5899  C   LEU C 768     3503   3808   3313     46     36     89       C  
-ATOM   5900  O   LEU C 768     -74.586  27.916 -42.049  1.00 29.94           O  
-ANISOU 5900  O   LEU C 768     3731   4107   3539     48     28     93       O  
-ATOM   5901  CB  LEU C 768     -71.320  27.824 -42.119  1.00 27.40           C  
-ANISOU 5901  CB  LEU C 768     3447   3727   3236     79     49     85       C  
-ATOM   5902  CG  LEU C 768     -70.165  28.534 -42.800  1.00 28.21           C  
-ANISOU 5902  CG  LEU C 768     3541   3841   3337    104     68    105       C  
-ATOM   5903  CD1 LEU C 768     -69.259  27.541 -43.508  1.00 30.76           C  
-ANISOU 5903  CD1 LEU C 768     3876   4174   3636    116     60     80       C  
-ATOM   5904  CD2 LEU C 768     -70.642  29.571 -43.772  1.00 29.33           C  
-ANISOU 5904  CD2 LEU C 768     3661   4019   3465    125     84    141       C  
-ATOM   5905  N   LEU C 769     -73.672  27.104 -40.181  1.00 29.91           N  
-ANISOU 5905  N   LEU C 769     3771   4015   3576     23     29     67       N  
-ATOM   5906  CA  LEU C 769     -74.802  26.250 -39.870  1.00 32.70           C  
-ANISOU 5906  CA  LEU C 769     4128   4372   3924     -9     16     46       C  
-ATOM   5907  C   LEU C 769     -76.099  27.049 -39.769  1.00 31.83           C  
-ANISOU 5907  C   LEU C 769     3984   4296   3813    -11     18     70       C  
-ATOM   5908  O   LEU C 769     -77.104  26.709 -40.370  1.00 32.20           O  
-ANISOU 5908  O   LEU C 769     4009   4389   3837    -27      5     60       O  
-ATOM   5909  CB  LEU C 769     -74.532  25.580 -38.535  1.00 36.03           C  
-ANISOU 5909  CB  LEU C 769     4582   4739   4369    -25     19     31       C  
-ATOM   5910  CG  LEU C 769     -75.205  24.278 -38.117  1.00 41.75           C  
-ANISOU 5910  CG  LEU C 769     5331   5443   5090    -61     13      1       C  
-ATOM   5911  CD1 LEU C 769     -76.369  24.517 -37.136  1.00 46.02           C  
-ANISOU 5911  CD1 LEU C 769     5858   5981   5647    -83     16     13       C  
-ATOM   5912  CD2 LEU C 769     -75.672  23.495 -39.327  1.00 42.38           C  
-ANISOU 5912  CD2 LEU C 769     5408   5556   5140    -81      0    -27       C  
-ATOM   5913  N   ASP C 770     -76.074  28.112 -38.977  1.00 32.10           N  
-ANISOU 5913  N   ASP C 770     4013   4311   3872      4     35    100       N  
-ATOM   5914  CA  ASP C 770     -77.259  28.939 -38.782  1.00 29.78           C  
-ANISOU 5914  CA  ASP C 770     3690   4045   3578     12     42    127       C  
-ATOM   5915  C   ASP C 770     -77.608  29.739 -40.016  1.00 29.16           C  
-ANISOU 5915  C   ASP C 770     3583   4024   3473     44     46    154       C  
-ATOM   5916  O   ASP C 770     -78.803  29.995 -40.296  1.00 28.90           O  
-ANISOU 5916  O   ASP C 770     3517   4043   3420     51     43    168       O  
-ATOM   5917  CB  ASP C 770     -77.052  29.871 -37.592  1.00 34.92           C  
-ANISOU 5917  CB  ASP C 770     4353   4653   4261     23     62    148       C  
-ATOM   5918  CG  ASP C 770     -77.365  29.192 -36.228  1.00 38.82           C  
-ANISOU 5918  CG  ASP C 770     4865   5112   4774     -5     58    130       C  
-ATOM   5919  OD1 ASP C 770     -78.290  28.341 -36.170  1.00 40.60           O  
-ANISOU 5919  OD1 ASP C 770     5082   5357   4989    -32     46    115       O  
-ATOM   5920  OD2 ASP C 770     -76.683  29.521 -35.237  1.00 38.48           O  
-ANISOU 5920  OD2 ASP C 770     4843   5025   4753     -1     68    131       O  
-ATOM   5921  N   ILE C 771     -76.594  30.090 -40.811  1.00 27.24           N  
-ANISOU 5921  N   ILE C 771     3348   3779   3224     67     55    163       N  
-ATOM   5922  CA  ILE C 771     -76.877  30.660 -42.123  1.00 27.87           C  
-ANISOU 5922  CA  ILE C 771     3402   3917   3270    101     59    188       C  
-ATOM   5923  C   ILE C 771     -77.648  29.664 -43.032  1.00 27.29           C  
-ANISOU 5923  C   ILE C 771     3306   3909   3155     85     29    159       C  
-ATOM   5924  O   ILE C 771     -78.639  30.039 -43.671  1.00 28.15           O  
-ANISOU 5924  O   ILE C 771     3378   4085   3232    105     25    177       O  
-ATOM   5925  CB  ILE C 771     -75.600  31.190 -42.796  1.00 27.54           C  
-ANISOU 5925  CB  ILE C 771     3374   3859   3230    126     78    203       C  
-ATOM   5926  CG1 ILE C 771     -75.188  32.492 -42.123  1.00 27.40           C  
-ANISOU 5926  CG1 ILE C 771     3370   3796   3246    142    113    238       C  
-ATOM   5927  CG2 ILE C 771     -75.836  31.445 -44.271  1.00 27.60           C  
-ANISOU 5927  CG2 ILE C 771     3360   3933   3195    161     78    222       C  
-ATOM   5928  CD1 ILE C 771     -73.746  32.860 -42.324  1.00 27.77           C  
-ANISOU 5928  CD1 ILE C 771     3433   3809   3309    146    134    241       C  
-ATOM   5929  N   GLU C 772     -77.211  28.416 -43.078  1.00 29.20           N  
-ANISOU 5929  N   GLU C 772     3568   4133   3394     52     11    114       N  
-ATOM   5930  CA  GLU C 772     -77.933  27.377 -43.851  1.00 30.64           C  
-ANISOU 5930  CA  GLU C 772     3735   4368   3539     24    -16     75       C  
-ATOM   5931  C   GLU C 772     -79.394  27.295 -43.364  1.00 30.70           C  
-ANISOU 5931  C   GLU C 772     3710   4412   3542     -2    -25     72       C  
-ATOM   5932  O   GLU C 772     -80.320  27.202 -44.181  1.00 30.74           O  
-ANISOU 5932  O   GLU C 772     3675   4497   3508     -4    -41     65       O  
-ATOM   5933  CB  GLU C 772     -77.239  26.025 -43.728  1.00 32.09           C  
-ANISOU 5933  CB  GLU C 772     3958   4506   3727    -10    -26     26       C  
-ATOM   5934  CG  GLU C 772     -77.787  24.854 -44.575  1.00 34.66           C  
-ANISOU 5934  CG  GLU C 772     4281   4873   4015    -45    -48    -24       C  
-ATOM   5935  CD  GLU C 772     -79.149  24.296 -44.120  1.00 35.82           C  
-ANISOU 5935  CD  GLU C 772     4407   5043   4159    -97    -60    -48       C  
-ATOM   5936  OE1 GLU C 772     -79.404  24.186 -42.896  1.00 35.34           O  
-ANISOU 5936  OE1 GLU C 772     4360   4935   4135   -119    -51    -44       O  
-ATOM   5937  OE2 GLU C 772     -79.959  23.945 -45.007  1.00 39.67           O  
-ANISOU 5937  OE2 GLU C 772     4863   5602   4608   -117    -79    -75       O  
-ATOM   5938  N   VAL C 773     -79.609  27.354 -42.052  1.00 27.89           N  
-ANISOU 5938  N   VAL C 773     3367   4008   3223    -20    -15     78       N  
-ATOM   5939  CA  VAL C 773     -80.973  27.297 -41.525  1.00 27.84           C  
-ANISOU 5939  CA  VAL C 773     3328   4037   3215    -44    -21     78       C  
-ATOM   5940  C   VAL C 773     -81.810  28.459 -42.030  1.00 29.17           C  
-ANISOU 5940  C   VAL C 773     3447   4278   3357      2    -15    122       C  
-ATOM   5941  O   VAL C 773     -82.951  28.284 -42.472  1.00 31.26           O  
-ANISOU 5941  O   VAL C 773     3665   4623   3590     -9    -30    114       O  
-ATOM   5942  CB  VAL C 773     -80.989  27.302 -39.990  1.00 28.11           C  
-ANISOU 5942  CB  VAL C 773     3386   4004   3291    -60     -6     85       C  
-ATOM   5943  CG1 VAL C 773     -82.411  27.478 -39.466  1.00 25.71           C  
-ANISOU 5943  CG1 VAL C 773     3042   3744   2984    -74     -6     95       C  
-ATOM   5944  CG2 VAL C 773     -80.359  26.013 -39.449  1.00 27.27           C  
-ANISOU 5944  CG2 VAL C 773     3327   3834   3203   -103    -10     43       C  
-ATOM   5945  N   ALA C 774     -81.241  29.652 -41.971  1.00 30.13           N  
-ANISOU 5945  N   ALA C 774     3580   4374   3492     54      9    167       N  
-ATOM   5946  CA  ALA C 774     -81.921  30.834 -42.411  1.00 29.06           C  
-ANISOU 5946  CA  ALA C 774     3411   4296   3335    108     24    215       C  
-ATOM   5947  C   ALA C 774     -82.245  30.727 -43.899  1.00 32.36           C  
-ANISOU 5947  C   ALA C 774     3793   4804   3697    130      7    214       C  
-ATOM   5948  O   ALA C 774     -83.358  31.040 -44.328  1.00 30.98           O  
-ANISOU 5948  O   ALA C 774     3568   4716   3485    154      0    231       O  
-ATOM   5949  CB  ALA C 774     -81.062  32.065 -42.140  1.00 29.47           C  
-ANISOU 5949  CB  ALA C 774     3496   4288   3414    153     60    259       C  
-ATOM   5950  N   TYR C 775     -81.258  30.305 -44.682  1.00 33.86           N  
-ANISOU 5950  N   TYR C 775     4006   4981   3878    128      0    195       N  
-ATOM   5951  CA  TYR C 775     -81.430  30.215 -46.109  1.00 35.27           C  
-ANISOU 5951  CA  TYR C 775     4156   5245   4002    153    -14    192       C  
-ATOM   5952  C   TYR C 775     -82.489  29.184 -46.487  1.00 35.50           C  
-ANISOU 5952  C   TYR C 775     4143   5352   3993    108    -51    144       C  
-ATOM   5953  O   TYR C 775     -83.292  29.441 -47.389  1.00 34.09           O  
-ANISOU 5953  O   TYR C 775     3915   5276   3762    136    -63    154       O  
-ATOM   5954  CB  TYR C 775     -80.115  29.895 -46.820  1.00 33.51           C  
-ANISOU 5954  CB  TYR C 775     3968   4988   3777    157    -12    178       C  
-ATOM   5955  CG  TYR C 775     -80.212  30.205 -48.257  1.00 34.71           C  
-ANISOU 5955  CG  TYR C 775     4093   5223   3871    204    -17    194       C  
-ATOM   5956  CD1 TYR C 775     -80.271  31.510 -48.667  1.00 36.11           C  
-ANISOU 5956  CD1 TYR C 775     4260   5425   4036    272     13    258       C  
-ATOM   5957  CD2 TYR C 775     -80.311  29.190 -49.224  1.00 37.60           C  
-ANISOU 5957  CD2 TYR C 775     4446   5648   4193    181    -48    145       C  
-ATOM   5958  CE1 TYR C 775     -80.416  31.845 -50.001  1.00 38.12           C  
-ANISOU 5958  CE1 TYR C 775     4489   5763   4232    324     12    280       C  
-ATOM   5959  CE2 TYR C 775     -80.448  29.514 -50.576  1.00 40.92           C  
-ANISOU 5959  CE2 TYR C 775     4838   6156   4553    229    -53    161       C  
-ATOM   5960  CZ  TYR C 775     -80.481  30.856 -50.947  1.00 39.49           C  
-ANISOU 5960  CZ  TYR C 775     4646   6001   4359    304    -22    232       C  
-ATOM   5961  OH  TYR C 775     -80.566  31.216 -52.257  1.00 44.55           O  
-ANISOU 5961  OH  TYR C 775     5262   6727   4938    360    -22    255       O  
-ATOM   5962  N   SER C 776     -82.473  28.029 -45.828  1.00 34.17           N  
-ANISOU 5962  N   SER C 776     3996   5139   3849     38    -65     91       N  
-ATOM   5963  CA  SER C 776     -83.508  26.996 -46.055  1.00 37.08           C  
-ANISOU 5963  CA  SER C 776     4329   5571   4189    -21    -94     39       C  
-ATOM   5964  C   SER C 776     -84.915  27.476 -45.741  1.00 35.65           C  
-ANISOU 5964  C   SER C 776     4086   5467   3991    -16    -97     60       C  
-ATOM   5965  O   SER C 776     -85.847  27.215 -46.480  1.00 38.24           O  
-ANISOU 5965  O   SER C 776     4358   5900   4270    -28   -121     38       O  
-ATOM   5966  CB  SER C 776     -83.247  25.788 -45.190  1.00 39.03           C  
-ANISOU 5966  CB  SER C 776     4619   5736   4473    -93    -96    -11       C  
-ATOM   5967  OG  SER C 776     -82.118  25.131 -45.674  1.00 43.20           O  
-ANISOU 5967  OG  SER C 776     5196   6216   5003    -99    -98    -40       O  
-ATOM   5968  N   LEU C 777     -85.070  28.179 -44.633  1.00 35.82           N  
-ANISOU 5968  N   LEU C 777     4116   5442   4052      2    -74    100       N  
-ATOM   5969  CA  LEU C 777     -86.380  28.694 -44.271  1.00 37.07           C  
-ANISOU 5969  CA  LEU C 777     4216   5672   4195     15    -73    125       C  
-ATOM   5970  C   LEU C 777     -86.889  29.613 -45.353  1.00 37.63           C  
-ANISOU 5970  C   LEU C 777     4237   5851   4210     88    -75    166       C  
-ATOM   5971  O   LEU C 777     -88.050  29.540 -45.748  1.00 41.81           O  
-ANISOU 5971  O   LEU C 777     4699   6493   4695     87    -93    160       O  
-ATOM   5972  CB  LEU C 777     -86.332  29.423 -42.943  1.00 34.92           C  
-ANISOU 5972  CB  LEU C 777     3970   5326   3972     35    -43    165       C  
-ATOM   5973  CG  LEU C 777     -86.262  28.555 -41.679  1.00 35.70           C  
-ANISOU 5973  CG  LEU C 777     4102   5344   4117    -32    -40    132       C  
-ATOM   5974  CD1 LEU C 777     -86.147  29.471 -40.461  1.00 33.41           C  
-ANISOU 5974  CD1 LEU C 777     3837   4989   3868      2    -10    176       C  
-ATOM   5975  CD2 LEU C 777     -87.475  27.640 -41.541  1.00 35.96           C  
-ANISOU 5975  CD2 LEU C 777     4087   5441   4134    -97    -59     93       C  
-ATOM   5976  N   LEU C 778     -86.007  30.486 -45.800  1.00 39.42           N  
-ANISOU 5976  N   LEU C 778     4496   6044   4438    153    -53    208       N  
-ATOM   5977  CA  LEU C 778     -86.341  31.500 -46.766  1.00 42.22           C  
-ANISOU 5977  CA  LEU C 778     4816   6483   4743    236    -44    260       C  
-ATOM   5978  C   LEU C 778     -86.727  30.857 -48.109  1.00 44.51           C  
-ANISOU 5978  C   LEU C 778     5058   6888   4964    229    -80    224       C  
-ATOM   5979  O   LEU C 778     -87.686  31.280 -48.752  1.00 44.65           O  
-ANISOU 5979  O   LEU C 778     5012   7026   4924    274    -89    247       O  
-ATOM   5980  CB  LEU C 778     -85.153  32.436 -46.923  1.00 43.31           C  
-ANISOU 5980  CB  LEU C 778     5011   6542   4905    292     -7    307       C  
-ATOM   5981  CG  LEU C 778     -85.370  33.818 -47.528  1.00 48.62           C  
-ANISOU 5981  CG  LEU C 778     5671   7257   5545    391     25    381       C  
-ATOM   5982  CD1 LEU C 778     -86.487  34.618 -46.863  1.00 47.77           C  
-ANISOU 5982  CD1 LEU C 778     5533   7184   5433    433     44    425       C  
-ATOM   5983  CD2 LEU C 778     -84.050  34.579 -47.431  1.00 50.45           C  
-ANISOU 5983  CD2 LEU C 778     5970   7382   5818    419     66    415       C  
-ATOM   5984  N   ARG C 779     -85.997  29.826 -48.505  1.00 43.49           N  
-ANISOU 5984  N   ARG C 779     4958   6726   4839    174   -100    167       N  
-ATOM   5985  CA  ARG C 779     -86.271  29.120 -49.747  1.00 47.45           C  
-ANISOU 5985  CA  ARG C 779     5424   7329   5277    158   -134    122       C  
-ATOM   5986  C   ARG C 779     -87.518  28.198 -49.674  1.00 50.81           C  
-ANISOU 5986  C   ARG C 779     5789   7842   5676     87   -169     63       C  
-ATOM   5987  O   ARG C 779     -88.148  27.958 -50.701  1.00 51.72           O  
-ANISOU 5987  O   ARG C 779     5848   8081   5725     89   -197     38       O  
-ATOM   5988  CB  ARG C 779     -85.020  28.330 -50.215  1.00 45.35           C  
-ANISOU 5988  CB  ARG C 779     5216   6993   5023    128   -139     80       C  
-ATOM   5989  N   GLY C 780     -87.866  27.679 -48.493  1.00 53.42           N  
-ANISOU 5989  N   GLY C 780     6128   8113   6055     21   -165     40       N  
-ATOM   5990  CA  GLY C 780     -89.145  26.955 -48.272  1.00 56.35           C  
-ANISOU 5990  CA  GLY C 780     6438   8566   6407    -49   -189     -6       C  
-ATOM   5991  C   GLY C 780     -90.404  27.808 -48.485  1.00 62.07           C  
-ANISOU 5991  C   GLY C 780     7074   9428   7082      5   -195     36       C  
-ATOM   5992  O   GLY C 780     -90.388  29.014 -48.239  1.00 68.02           O  
-ANISOU 5992  O   GLY C 780     7829  10175   7841     92   -168    111       O  
-ATOM   5993  N   GLY C 781     -91.502  27.183 -48.926  1.00 70.39           N  
-ANISOU 5993  N   GLY C 781     8051  10607   8086    -45   -227    -13       N  
-ATOM   5994  CA  GLY C 781     -92.653  27.900 -49.530  1.00 71.98           C  
-ANISOU 5994  CA  GLY C 781     8156  10977   8218     16   -241     20       C  
-ATOM   5995  C   GLY C 781     -93.911  28.038 -48.686  1.00 71.85           C  
-ANISOU 5995  C   GLY C 781     8072  11024   8204     -3   -238     31       C  
-ATOM   5996  O   GLY C 781     -93.862  28.031 -47.452  1.00 75.82           O  
-ANISOU 5996  O   GLY C 781     8611  11427   8771    -30   -213     45       O  
-ATOM   5997  N   SER C 785     -98.886  33.443 -52.387  1.00 62.28           N  
-ANISOU 5997  N   SER C 785     6393  10737   6535    628   -248    369       N  
-ATOM   5998  CA  SER C 785     -99.689  33.541 -51.176  1.00 68.32           C  
-ANISOU 5998  CA  SER C 785     7127  11494   7337    604   -232    381       C  
-ATOM   5999  C   SER C 785    -100.236  34.961 -50.989  1.00 69.73           C  
-ANISOU 5999  C   SER C 785     7289  11722   7485    759   -189    490       C  
-ATOM   6000  O   SER C 785     -99.667  35.934 -51.494  1.00 74.42           O  
-ANISOU 6000  O   SER C 785     7936  12279   8062    874   -154    563       O  
-ATOM   6001  CB  SER C 785     -98.869  33.131 -49.943  1.00 69.30           C  
-ANISOU 6001  CB  SER C 785     7353  11403   7575    515   -207    358       C  
-ATOM   6002  OG  SER C 785     -99.468  33.591 -48.728  1.00 68.70           O  
-ANISOU 6002  OG  SER C 785     7270  11296   7538    531   -176    398       O  
-ATOM   6003  N   SER C 786    -101.328  35.062 -50.233  1.00 69.37           N  
-ANISOU 6003  N   SER C 786     7172  11751   7433    758   -185    502       N  
-ATOM   6004  CA  SER C 786    -102.013  36.348 -49.955  1.00 67.79           C  
-ANISOU 6004  CA  SER C 786     6948  11609   7200    905   -142    603       C  
-ATOM   6005  C   SER C 786    -101.119  37.343 -49.205  1.00 64.67           C  
-ANISOU 6005  C   SER C 786     6682  11013   6879    973    -76    675       C  
-ATOM   6006  O   SER C 786    -101.244  38.553 -49.395  1.00 60.07           O  
-ANISOU 6006  O   SER C 786     6116  10444   6262   1117    -31    766       O  
-ATOM   6007  CB  SER C 786    -103.275  36.096 -49.129  1.00 63.58           C  
-ANISOU 6007  CB  SER C 786     6320  11177   6660    868   -151    590       C  
-ATOM   6008  N   LYS C 787    -100.215  36.823 -48.364  1.00 64.84           N  
-ANISOU 6008  N   LYS C 787     6793  10847   6996    871    -67    633       N  
-ATOM   6009  CA  LYS C 787     -99.567  37.648 -47.344  1.00 58.89           C  
-ANISOU 6009  CA  LYS C 787     6145   9912   6318    911     -8    686       C  
-ATOM   6010  C   LYS C 787     -98.335  38.368 -47.872  1.00 53.12           C  
-ANISOU 6010  C   LYS C 787     5516   9061   5605    975     27    729       C  
-ATOM   6011  O   LYS C 787     -97.627  37.902 -48.780  1.00 51.62           O  
-ANISOU 6011  O   LYS C 787     5343   8869   5402    944      2    696       O  
-ATOM   6012  CB  LYS C 787     -99.253  36.832 -46.066  1.00 58.97           C  
-ANISOU 6012  CB  LYS C 787     6198   9788   6419    781    -12    627       C  
-ATOM   6013  N   ASP C 788     -98.133  39.555 -47.324  1.00 50.38           N  
-ANISOU 6013  N   ASP C 788     5237   8620   5285   1069     89    806       N  
-ATOM   6014  CA  ASP C 788     -96.872  40.275 -47.463  1.00 55.88           C  
-ANISOU 6014  CA  ASP C 788     6048   9162   6024   1109    135    843       C  
-ATOM   6015  C   ASP C 788     -95.711  39.305 -47.142  1.00 55.69           C  
-ANISOU 6015  C   ASP C 788     6084   9001   6074    975    110    766       C  
-ATOM   6016  O   ASP C 788     -95.811  38.521 -46.198  1.00 54.77           O  
-ANISOU 6016  O   ASP C 788     5964   8839   6007    875     89    711       O  
-ATOM   6017  CB  ASP C 788     -96.892  41.441 -46.477  1.00 58.43           C  
-ANISOU 6017  CB  ASP C 788     6437   9377   6386   1184    203    911       C  
-ATOM   6018  CG  ASP C 788     -95.694  42.383 -46.622  1.00 61.32           C  
-ANISOU 6018  CG  ASP C 788     6919   9589   6791   1235    261    958       C  
-ATOM   6019  OD1 ASP C 788     -95.799  43.567 -46.230  1.00 64.24           O  
-ANISOU 6019  OD1 ASP C 788     7340   9900   7167   1332    326   1029       O  
-ATOM   6020  OD2 ASP C 788     -94.637  41.926 -47.081  1.00 61.67           O  
-ANISOU 6020  OD2 ASP C 788     7004   9565   6861   1175    246    921       O  
-ATOM   6021  N   PRO C 789     -94.632  39.312 -47.952  1.00 58.31           N  
-ANISOU 6021  N   PRO C 789     6469   9276   6409    975    113    763       N  
-ATOM   6022  CA  PRO C 789     -93.503  38.397 -47.688  1.00 56.13           C  
-ANISOU 6022  CA  PRO C 789     6250   8879   6200    859     91    694       C  
-ATOM   6023  C   PRO C 789     -92.885  38.514 -46.290  1.00 53.63           C  
-ANISOU 6023  C   PRO C 789     6011   8394   5974    808    121    685       C  
-ATOM   6024  O   PRO C 789     -92.446  37.509 -45.735  1.00 49.86           O  
-ANISOU 6024  O   PRO C 789     5549   7852   5544    700     92    619       O  
-ATOM   6025  CB  PRO C 789     -92.480  38.780 -48.766  1.00 56.43           C  
-ANISOU 6025  CB  PRO C 789     6337   8883   6221    904    107    718       C  
-ATOM   6026  CG  PRO C 789     -93.312  39.263 -49.899  1.00 57.03           C  
-ANISOU 6026  CG  PRO C 789     6344   9123   6201   1008    104    765       C  
-ATOM   6027  CD  PRO C 789     -94.489  39.969 -49.269  1.00 59.21           C  
-ANISOU 6027  CD  PRO C 789     6579   9462   6456   1078    127    816       C  
-ATOM   6028  N   ILE C 790     -92.845  39.722 -45.742  1.00 52.89           N  
-ANISOU 6028  N   ILE C 790     5967   8229   5901    887    179    751       N  
-ATOM   6029  CA  ILE C 790     -92.363  39.910 -44.386  1.00 55.09           C  
-ANISOU 6029  CA  ILE C 790     6313   8361   6257    846    207    743       C  
-ATOM   6030  C   ILE C 790     -93.180  39.031 -43.427  1.00 54.71           C  
-ANISOU 6030  C   ILE C 790     6214   8349   6225    770    173    695       C  
-ATOM   6031  O   ILE C 790     -92.609  38.368 -42.567  1.00 50.74           O  
-ANISOU 6031  O   ILE C 790     5749   7748   5782    680    163    646       O  
-ATOM   6032  CB  ILE C 790     -92.430  41.392 -43.968  1.00 56.33           C  
-ANISOU 6032  CB  ILE C 790     6524   8456   6423    949    277    821       C  
-ATOM   6033  CG1 ILE C 790     -91.388  42.212 -44.736  1.00 58.69           C  
-ANISOU 6033  CG1 ILE C 790     6893   8680   6726   1002    319    862       C  
-ATOM   6034  CG2 ILE C 790     -92.151  41.549 -42.487  1.00 57.26           C  
-ANISOU 6034  CG2 ILE C 790     6698   8444   6612    905    301    806       C  
-ATOM   6035  CD1 ILE C 790     -91.785  43.664 -44.946  1.00 63.21           C  
-ANISOU 6035  CD1 ILE C 790     7495   9253   7268   1134    387    952       C  
-ATOM   6036  N   ASP C 791     -94.503  39.012 -43.600  1.00 54.53           N  
-ANISOU 6036  N   ASP C 791     6104   8470   6146    806    159    710       N  
-ATOM   6037  CA  ASP C 791     -95.387  38.178 -42.777  1.00 52.29           C  
-ANISOU 6037  CA  ASP C 791     5761   8237   5871    734    130    668       C  
-ATOM   6038  C   ASP C 791     -95.138  36.681 -43.003  1.00 47.45           C  
-ANISOU 6038  C   ASP C 791     5122   7637   5268    608     74    582       C  
-ATOM   6039  O   ASP C 791     -95.248  35.880 -42.073  1.00 43.28           O  
-ANISOU 6039  O   ASP C 791     4596   7067   4783    519     61    536       O  
-ATOM   6040  CB  ASP C 791     -96.876  38.491 -43.031  1.00 56.86           C  
-ANISOU 6040  CB  ASP C 791     6240   8986   6378    802    126    703       C  
-ATOM   6041  CG  ASP C 791     -97.339  39.816 -42.407  1.00 62.92           C  
-ANISOU 6041  CG  ASP C 791     7031   9731   7143    916    184    782       C  
-ATOM   6042  OD1 ASP C 791     -98.571  40.045 -42.378  1.00 65.65           O  
-ANISOU 6042  OD1 ASP C 791     7297  10209   7438    970    184    811       O  
-ATOM   6043  OD2 ASP C 791     -96.507  40.642 -41.983  1.00 64.32           O  
-ANISOU 6043  OD2 ASP C 791     7305   9768   7365    953    232    815       O  
-ATOM   6044  N   VAL C 792     -94.824  36.292 -44.232  1.00 44.98           N  
-ANISOU 6044  N   VAL C 792     4790   7384   4916    602     45    560       N  
-ATOM   6045  CA  VAL C 792     -94.585  34.872 -44.523  1.00 46.46           C  
-ANISOU 6045  CA  VAL C 792     4960   7583   5110    485     -4    476       C  
-ATOM   6046  C   VAL C 792     -93.345  34.410 -43.769  1.00 46.43           C  
-ANISOU 6046  C   VAL C 792     5050   7407   5185    415      5    442       C  
-ATOM   6047  O   VAL C 792     -93.338  33.351 -43.166  1.00 44.65           O  
-ANISOU 6047  O   VAL C 792     4826   7146   4992    316    -15    384       O  
-ATOM   6048  CB  VAL C 792     -94.407  34.612 -46.028  1.00 50.56           C  
-ANISOU 6048  CB  VAL C 792     5448   8196   5568    501    -34    460       C  
-ATOM   6049  CG1 VAL C 792     -93.957  33.177 -46.305  1.00 49.27           C  
-ANISOU 6049  CG1 VAL C 792     5288   8014   5417    382    -77    370       C  
-ATOM   6050  CG2 VAL C 792     -95.709  34.914 -46.770  1.00 55.50           C  
-ANISOU 6050  CG2 VAL C 792     5967   9014   6105    564    -51    484       C  
-ATOM   6051  N   ASN C 793     -92.293  35.213 -43.831  1.00 45.19           N  
-ANISOU 6051  N   ASN C 793     4969   7148   5055    466     38    480       N  
-ATOM   6052  CA  ASN C 793     -91.035  34.849 -43.197  1.00 46.14           C  
-ANISOU 6052  CA  ASN C 793     5171   7116   5242    408     47    450       C  
-ATOM   6053  C   ASN C 793     -91.123  34.952 -41.657  1.00 41.60           C  
-ANISOU 6053  C   ASN C 793     4629   6452   4725    382     69    452       C  
-ATOM   6054  O   ASN C 793     -90.542  34.138 -40.973  1.00 37.09           O  
-ANISOU 6054  O   ASN C 793     4096   5798   4200    305     59    407       O  
-ATOM   6055  CB  ASN C 793     -89.901  35.709 -43.760  1.00 44.52           C  
-ANISOU 6055  CB  ASN C 793     5029   6839   5046    467     77    489       C  
-ATOM   6056  CG  ASN C 793     -89.558  35.371 -45.201  1.00 46.08           C  
-ANISOU 6056  CG  ASN C 793     5208   7105   5196    476     52    475       C  
-ATOM   6057  OD1 ASN C 793     -89.442  34.192 -45.581  1.00 49.47           O  
-ANISOU 6057  OD1 ASN C 793     5619   7561   5617    403     12    412       O  
-ATOM   6058  ND2 ASN C 793     -89.392  36.402 -46.019  1.00 45.61           N  
-ANISOU 6058  ND2 ASN C 793     5157   7070   5103    569     81    534       N  
-ATOM   6059  N   TYR C 794     -91.886  35.917 -41.145  1.00 39.75           N  
-ANISOU 6059  N   TYR C 794     4380   6242   4482    450    100    505       N  
-ATOM   6060  CA  TYR C 794     -92.190  35.994 -39.717  1.00 40.26           C  
-ANISOU 6060  CA  TYR C 794     4463   6244   4588    429    119    507       C  
-ATOM   6061  C   TYR C 794     -92.755  34.688 -39.219  1.00 40.90           C  
-ANISOU 6061  C   TYR C 794     4502   6359   4677    333     85    449       C  
-ATOM   6062  O   TYR C 794     -92.246  34.121 -38.259  1.00 41.41           O  
-ANISOU 6062  O   TYR C 794     4612   6328   4792    271     86    418       O  
-ATOM   6063  CB  TYR C 794     -93.173  37.099 -39.426  1.00 41.04           C  
-ANISOU 6063  CB  TYR C 794     4535   6398   4662    521    153    569       C  
-ATOM   6064  CG  TYR C 794     -93.738  37.095 -38.012  1.00 41.23           C  
-ANISOU 6064  CG  TYR C 794     4561   6388   4716    502    170    569       C  
-ATOM   6065  CD1 TYR C 794     -92.982  37.515 -36.958  1.00 39.95           C  
-ANISOU 6065  CD1 TYR C 794     4478   6092   4609    497    200    572       C  
-ATOM   6066  CD2 TYR C 794     -95.049  36.724 -37.764  1.00 40.67           C  
-ANISOU 6066  CD2 TYR C 794     4410   6429   4616    493    156    567       C  
-ATOM   6067  CE1 TYR C 794     -93.505  37.553 -35.692  1.00 40.44           C  
-ANISOU 6067  CE1 TYR C 794     4543   6129   4695    488    216    574       C  
-ATOM   6068  CE2 TYR C 794     -95.582  36.745 -36.497  1.00 40.23           C  
-ANISOU 6068  CE2 TYR C 794     4354   6346   4584    481    174    571       C  
-ATOM   6069  CZ  TYR C 794     -94.803  37.159 -35.457  1.00 41.49           C  
-ANISOU 6069  CZ  TYR C 794     4598   6368   4798    480    205    575       C  
-ATOM   6070  OH  TYR C 794     -95.310  37.185 -34.167  1.00 40.89           O  
-ANISOU 6070  OH  TYR C 794     4527   6266   4745    472    224    579       O  
-ATOM   6071  N   GLU C 795     -93.745  34.172 -39.919  1.00 41.03           N  
-ANISOU 6071  N   GLU C 795     4436   6511   4644    318     55    433       N  
-ATOM   6072  CA  GLU C 795     -94.395  32.915 -39.543  1.00 42.44           C  
-ANISOU 6072  CA  GLU C 795     4569   6731   4827    219     26    376       C  
-ATOM   6073  C   GLU C 795     -93.431  31.756 -39.550  1.00 41.41           C  
-ANISOU 6073  C   GLU C 795     4489   6513   4731    127      6    313       C  
-ATOM   6074  O   GLU C 795     -93.572  30.822 -38.756  1.00 39.42           O  
-ANISOU 6074  O   GLU C 795     4244   6222   4511     45      1    273       O  
-ATOM   6075  CB  GLU C 795     -95.622  32.622 -40.451  1.00 46.42           C  
-ANISOU 6075  CB  GLU C 795     4965   7410   5261    218     -3    365       C  
-ATOM   6076  CG  GLU C 795     -96.805  33.554 -40.156  1.00 50.27           C  
-ANISOU 6076  CG  GLU C 795     5390   7996   5714    299     18    423       C  
-ATOM   6077  CD  GLU C 795     -97.969  33.475 -41.146  1.00 57.54           C  
-ANISOU 6077  CD  GLU C 795     6198   9108   6556    320    -10    422       C  
-ATOM   6078  OE1 GLU C 795     -97.925  32.703 -42.131  1.00 64.64           O  
-ANISOU 6078  OE1 GLU C 795     7062  10075   7423    269    -49    372       O  
-ATOM   6079  OE2 GLU C 795     -98.971  34.190 -40.925  1.00 60.61           O  
-ANISOU 6079  OE2 GLU C 795     6529   9590   6912    390      6    470       O  
-ATOM   6080  N   LYS C 796     -92.455  31.786 -40.456  1.00 41.81           N  
-ANISOU 6080  N   LYS C 796     4576   6534   4776    141     -3    306       N  
-ATOM   6081  CA  LYS C 796     -91.454  30.706 -40.527  1.00 40.37           C  
-ANISOU 6081  CA  LYS C 796     4446   6268   4624     64    -20    249       C  
-ATOM   6082  C   LYS C 796     -90.562  30.596 -39.294  1.00 35.97           C  
-ANISOU 6082  C   LYS C 796     3968   5568   4132     40      2    246       C  
-ATOM   6083  O   LYS C 796     -90.020  29.528 -39.023  1.00 34.48           O  
-ANISOU 6083  O   LYS C 796     3815   5316   3970    -31     -9    198       O  
-ATOM   6084  CB  LYS C 796     -90.563  30.886 -41.742  1.00 44.62           C  
-ANISOU 6084  CB  LYS C 796     5006   6806   5139     97    -30    249       C  
-ATOM   6085  CG  LYS C 796     -91.243  30.566 -43.062  1.00 48.81           C  
-ANISOU 6085  CG  LYS C 796     5466   7475   5603     97    -62    229       C  
-ATOM   6086  CD  LYS C 796     -90.365  31.019 -44.213  1.00 50.88           C  
-ANISOU 6086  CD  LYS C 796     5754   7739   5840    152    -63    246       C  
-ATOM   6087  CE  LYS C 796     -91.012  30.775 -45.577  1.00 52.39           C  
-ANISOU 6087  CE  LYS C 796     5874   8075   5956    163    -95    228       C  
-ATOM   6088  NZ  LYS C 796     -90.189  31.395 -46.667  1.00 51.93           N  
-ANISOU 6088  NZ  LYS C 796     5840   8020   5869    233    -88    258       N  
-ATOM   6089  N   LEU C 797     -90.412  31.693 -38.559  1.00 33.57           N  
-ANISOU 6089  N   LEU C 797     3693   5213   3850    101     34    296       N  
-ATOM   6090  CA  LEU C 797     -89.655  31.690 -37.304  1.00 33.28           C  
-ANISOU 6090  CA  LEU C 797     3722   5053   3868     84     55    294       C  
-ATOM   6091  C   LEU C 797     -90.365  30.946 -36.192  1.00 32.61           C  
-ANISOU 6091  C   LEU C 797     3625   4962   3803     26     56    273       C  
-ATOM   6092  O   LEU C 797     -89.722  30.527 -35.255  1.00 32.68           O  
-ANISOU 6092  O   LEU C 797     3687   4878   3852     -6     64    256       O  
-ATOM   6093  CB  LEU C 797     -89.356  33.111 -36.824  1.00 31.50           C  
-ANISOU 6093  CB  LEU C 797     3531   4779   3658    162     92    348       C  
-ATOM   6094  CG  LEU C 797     -88.570  33.984 -37.792  1.00 32.80           C  
-ANISOU 6094  CG  LEU C 797     3720   4933   3811    221    104    377       C  
-ATOM   6095  CD1 LEU C 797     -88.516  35.412 -37.277  1.00 33.76           C  
-ANISOU 6095  CD1 LEU C 797     3873   5010   3945    294    148    430       C  
-ATOM   6096  CD2 LEU C 797     -87.169  33.454 -38.025  1.00 33.43           C  
-ANISOU 6096  CD2 LEU C 797     3853   4933   3917    183     93    343       C  
-ATOM   6097  N   LYS C 798     -91.680  30.770 -36.305  1.00 34.60           N  
-ANISOU 6097  N   LYS C 798     3804   5317   4024     15     48    274       N  
-ATOM   6098  CA  LYS C 798     -92.455  30.001 -35.342  1.00 34.68           C  
-ANISOU 6098  CA  LYS C 798     3794   5332   4049    -46     51    253       C  
-ATOM   6099  C   LYS C 798     -92.226  30.621 -33.946  1.00 34.65           C  
-ANISOU 6099  C   LYS C 798     3839   5244   4084    -15     84    284       C  
-ATOM   6100  O   LYS C 798     -92.032  29.933 -32.929  1.00 33.84           O  
-ANISOU 6100  O   LYS C 798     3771   5073   4014    -64     92    264       O  
-ATOM   6101  CB  LYS C 798     -92.064  28.500 -35.429  1.00 35.47           C  
-ANISOU 6101  CB  LYS C 798     3918   5393   4165   -143     32    191       C  
-ATOM   6102  N   THR C 799     -92.274  31.942 -33.907  1.00 33.52           N  
-ANISOU 6102  N   THR C 799     3698   5106   3932     71    106    335       N  
-ATOM   6103  CA  THR C 799     -91.970  32.693 -32.706  1.00 34.36           C  
-ANISOU 6103  CA  THR C 799     3855   5131   4069    108    138    362       C  
-ATOM   6104  C   THR C 799     -92.903  33.887 -32.661  1.00 36.53           C  
-ANISOU 6104  C   THR C 799     4093   5470   4318    190    163    415       C  
-ATOM   6105  O   THR C 799     -92.970  34.673 -33.610  1.00 37.05           O  
-ANISOU 6105  O   THR C 799     4141   5581   4353    252    166    445       O  
-ATOM   6106  CB  THR C 799     -90.501  33.193 -32.735  1.00 33.36           C  
-ANISOU 6106  CB  THR C 799     3804   4900   3970    130    146    362       C  
-ATOM   6107  OG1 THR C 799     -89.612  32.068 -32.804  1.00 37.44           O  
-ANISOU 6107  OG1 THR C 799     4354   5363   4508     63    124    315       O  
-ATOM   6108  CG2 THR C 799     -90.157  33.984 -31.499  1.00 34.81           C  
-ANISOU 6108  CG2 THR C 799     4040   5003   4184    163    178    382       C  
-ATOM   6109  N   ASP C 800     -93.602  34.053 -31.550  1.00 37.83           N  
-ANISOU 6109  N   ASP C 800     4249   5633   4490    198    184    431       N  
-ATOM   6110  CA  ASP C 800     -94.411  35.249 -31.363  1.00 39.16           C  
-ANISOU 6110  CA  ASP C 800     4394   5848   4635    286    215    484       C  
-ATOM   6111  C   ASP C 800     -93.492  36.405 -30.961  1.00 36.86           C  
-ANISOU 6111  C   ASP C 800     4184   5453   4368    346    248    509       C  
-ATOM   6112  O   ASP C 800     -92.726  36.273 -30.020  1.00 36.23           O  
-ANISOU 6112  O   ASP C 800     4164   5274   4326    317    256    488       O  
-ATOM   6113  CB  ASP C 800     -95.486  35.031 -30.302  1.00 40.77           C  
-ANISOU 6113  CB  ASP C 800     4562   6091   4838    275    229    492       C  
-ATOM   6114  CG  ASP C 800     -96.436  36.212 -30.206  1.00 41.90           C  
-ANISOU 6114  CG  ASP C 800     4673   6300   4949    373    261    549       C  
-ATOM   6115  OD1 ASP C 800     -97.407  36.233 -30.975  1.00 47.09           O  
-ANISOU 6115  OD1 ASP C 800     5249   7082   5561    396    250    566       O  
-ATOM   6116  OD2 ASP C 800     -96.194  37.132 -29.396  1.00 39.84           O  
-ANISOU 6116  OD2 ASP C 800     4467   5966   4703    428    297    575       O  
-ATOM   6117  N   ILE C 801     -93.554  37.516 -31.696  1.00 34.70           N  
-ANISOU 6117  N   ILE C 801     3912   5202   4070    428    269    552       N  
-ATOM   6118  CA  ILE C 801     -92.713  38.679 -31.422  1.00 34.62           C  
-ANISOU 6118  CA  ILE C 801     3980   5092   4082    482    307    575       C  
-ATOM   6119  C   ILE C 801     -93.584  39.917 -31.212  1.00 37.50           C  
-ANISOU 6119  C   ILE C 801     4340   5487   4422    581    351    632       C  
-ATOM   6120  O   ILE C 801     -94.323  40.303 -32.117  1.00 35.15           O  
-ANISOU 6120  O   ILE C 801     3993   5284   4080    641    355    670       O  
-ATOM   6121  CB  ILE C 801     -91.714  38.952 -32.572  1.00 34.80           C  
-ANISOU 6121  CB  ILE C 801     4032   5086   4104    491    302    575       C  
-ATOM   6122  CG1 ILE C 801     -90.922  37.683 -32.915  1.00 35.34           C  
-ANISOU 6122  CG1 ILE C 801     4099   5137   4190    402    257    520       C  
-ATOM   6123  CG2 ILE C 801     -90.767  40.077 -32.182  1.00 33.72           C  
-ANISOU 6123  CG2 ILE C 801     3979   4835   3997    528    344    590       C  
-ATOM   6124  CD1 ILE C 801     -89.931  37.847 -34.050  1.00 36.76           C  
-ANISOU 6124  CD1 ILE C 801     4303   5296   4368    407    251    518       C  
-ATOM   6125  N   LYS C 802     -93.465  40.541 -30.032  1.00 37.08           N  
-ANISOU 6125  N   LYS C 802     4340   5354   4393    602    387    638       N  
-ATOM   6126  CA  LYS C 802     -94.178  41.749 -29.703  1.00 38.34           C  
-ANISOU 6126  CA  LYS C 802     4512   5522   4533    698    436    690       C  
-ATOM   6127  C   LYS C 802     -93.201  42.839 -29.296  1.00 38.43           C  
-ANISOU 6127  C   LYS C 802     4622   5404   4575    728    480    695       C  
-ATOM   6128  O   LYS C 802     -92.199  42.580 -28.652  1.00 37.39           O  
-ANISOU 6128  O   LYS C 802     4543   5180   4484    668    473    652       O  
-ATOM   6129  CB  LYS C 802     -95.125  41.513 -28.532  1.00 42.18           C  
-ANISOU 6129  CB  LYS C 802     4972   6040   5016    697    444    691       C  
-ATOM   6130  CG  LYS C 802     -96.378  40.728 -28.867  1.00 46.35           C  
-ANISOU 6130  CG  LYS C 802     5395   6710   5506    685    416    698       C  
-ATOM   6131  CD  LYS C 802     -97.217  40.539 -27.604  1.00 50.20           C  
-ANISOU 6131  CD  LYS C 802     5862   7216   5995    681    430    700       C  
-ATOM   6132  CE  LYS C 802     -98.579  39.887 -27.875  1.00 54.52           C  
-ANISOU 6132  CE  LYS C 802     6299   7913   6502    673    411    711       C  
-ATOM   6133  NZ  LYS C 802     -98.495  38.416 -28.135  1.00 55.79           N  
-ANISOU 6133  NZ  LYS C 802     6415   8108   6675    560    361    659       N  
-ATOM   6134  N   VAL C 803     -93.523  44.074 -29.650  1.00 38.21           N  
-ANISOU 6134  N   VAL C 803     4620   5373   4526    824    530    747       N  
-ATOM   6135  CA  VAL C 803     -92.736  45.209 -29.265  1.00 37.98           C  
-ANISOU 6135  CA  VAL C 803     4686   5220   4524    855    581    754       C  
-ATOM   6136  C   VAL C 803     -93.073  45.554 -27.833  1.00 40.37           C  
-ANISOU 6136  C   VAL C 803     5024   5476   4840    866    609    746       C  
-ATOM   6137  O   VAL C 803     -94.233  45.614 -27.474  1.00 42.83           O  
-ANISOU 6137  O   VAL C 803     5293   5860   5122    916    620    774       O  
-ATOM   6138  CB  VAL C 803     -93.051  46.423 -30.155  1.00 39.49           C  
-ANISOU 6138  CB  VAL C 803     4898   5421   4684    961    633    818       C  
-ATOM   6139  CG1 VAL C 803     -92.279  47.651 -29.690  1.00 40.30           C  
-ANISOU 6139  CG1 VAL C 803     5109   5386   4818    989    697    823       C  
-ATOM   6140  CG2 VAL C 803     -92.719  46.097 -31.606  1.00 38.53           C  
-ANISOU 6140  CG2 VAL C 803     4743   5353   4544    956    606    829       C  
-ATOM   6141  N   VAL C 804     -92.055  45.781 -27.019  1.00 40.13           N  
-ANISOU 6141  N   VAL C 804     5067   5331   4851    821    621    705       N  
-ATOM   6142  CA  VAL C 804     -92.258  46.281 -25.682  1.00 39.01           C  
-ANISOU 6142  CA  VAL C 804     4971   5133   4719    838    654    695       C  
-ATOM   6143  C   VAL C 804     -92.281  47.813 -25.727  1.00 42.09           C  
-ANISOU 6143  C   VAL C 804     5435   5453   5104    924    727    733       C  
-ATOM   6144  O   VAL C 804     -91.355  48.452 -26.232  1.00 40.34           O  
-ANISOU 6144  O   VAL C 804     5272   5152   4902    919    752    729       O  
-ATOM   6145  CB  VAL C 804     -91.156  45.791 -24.746  1.00 37.48           C  
-ANISOU 6145  CB  VAL C 804     4818   4856   4565    749    631    629       C  
-ATOM   6146  CG1 VAL C 804     -91.282  46.452 -23.391  1.00 37.21           C  
-ANISOU 6146  CG1 VAL C 804     4841   4760   4538    772    670    617       C  
-ATOM   6147  CG2 VAL C 804     -91.203  44.266 -24.611  1.00 38.42           C  
-ANISOU 6147  CG2 VAL C 804     4873   5038   4687    673    568    597       C  
-ATOM   6148  N   ASP C 805     -93.354  48.397 -25.206  1.00 46.36           N  
-ANISOU 6148  N   ASP C 805     5974   6022   5617   1005    766    770       N  
-ATOM   6149  CA  ASP C 805     -93.540  49.843 -25.231  1.00 48.72           C  
-ANISOU 6149  CA  ASP C 805     6346   6258   5906   1100    843    812       C  
-ATOM   6150  C   ASP C 805     -92.370  50.524 -24.527  1.00 44.18           C  
-ANISOU 6150  C   ASP C 805     5876   5535   5374   1057    876    765       C  
-ATOM   6151  O   ASP C 805     -92.039  50.183 -23.389  1.00 41.51           O  
-ANISOU 6151  O   ASP C 805     5556   5159   5057   1000    860    713       O  
-ATOM   6152  CB  ASP C 805     -94.867  50.179 -24.531  1.00 55.82           C  
-ANISOU 6152  CB  ASP C 805     7225   7214   6770   1184    873    850       C  
-ATOM   6153  CG  ASP C 805     -95.255  51.633 -24.681  1.00 63.99           C  
-ANISOU 6153  CG  ASP C 805     8329   8200   7784   1301    957    904       C  
-ATOM   6154  OD1 ASP C 805     -95.244  52.373 -23.667  1.00 67.30           O  
-ANISOU 6154  OD1 ASP C 805     8823   8536   8214   1327   1005    892       O  
-ATOM   6155  OD2 ASP C 805     -95.592  52.030 -25.821  1.00 67.01           O  
-ANISOU 6155  OD2 ASP C 805     8693   8630   8138   1372    975    961       O  
-ATOM   6156  N   ARG C 806     -91.759  51.493 -25.200  1.00 45.76           N  
-ANISOU 6156  N   ARG C 806     6144   5657   5586   1084    925    783       N  
-ATOM   6157  CA  ARG C 806     -90.601  52.234 -24.679  1.00 46.89           C  
-ANISOU 6157  CA  ARG C 806     6387   5660   5770   1038    963    736       C  
-ATOM   6158  C   ARG C 806     -90.838  52.886 -23.314  1.00 50.93           C  
-ANISOU 6158  C   ARG C 806     6962   6103   6285   1058   1005    713       C  
-ATOM   6159  O   ARG C 806     -89.898  53.071 -22.551  1.00 54.00           O  
-ANISOU 6159  O   ARG C 806     7409   6402   6707    990   1010    650       O  
-ATOM   6160  CB  ARG C 806     -90.145  53.285 -25.701  1.00 49.68           C  
-ANISOU 6160  CB  ARG C 806     6803   5945   6129   1081   1024    774       C  
-ATOM   6161  N   ASP C 807     -92.090  53.223 -23.011  1.00 56.41           N  
-ANISOU 6161  N   ASP C 807     7642   6847   6942   1153   1036    760       N  
-ATOM   6162  CA  ASP C 807     -92.459  53.871 -21.751  1.00 60.34           C  
-ANISOU 6162  CA  ASP C 807     8200   7289   7436   1188   1081    745       C  
-ATOM   6163  C   ASP C 807     -92.873  52.918 -20.642  1.00 57.84           C  
-ANISOU 6163  C   ASP C 807     7829   7035   7113   1149   1030    710       C  
-ATOM   6164  O   ASP C 807     -93.185  53.379 -19.554  1.00 59.48           O  
-ANISOU 6164  O   ASP C 807     8081   7204   7314   1177   1063    695       O  
-ATOM   6165  CB  ASP C 807     -93.633  54.837 -21.968  1.00 65.68           C  
-ANISOU 6165  CB  ASP C 807     8897   7985   8072   1327   1150    820       C  
-ATOM   6166  CG  ASP C 807     -93.326  55.934 -22.971  1.00 70.23           C  
-ANISOU 6166  CG  ASP C 807     9545   8490   8651   1386   1218    864       C  
-ATOM   6167  OD1 ASP C 807     -92.162  56.386 -23.042  1.00 71.64           O  
-ANISOU 6167  OD1 ASP C 807     9799   8553   8869   1322   1240    823       O  
-ATOM   6168  OD2 ASP C 807     -94.266  56.352 -23.679  1.00 74.53           O  
-ANISOU 6168  OD2 ASP C 807    10068   9096   9153   1498   1252    942       O  
-ATOM   6169  N   SER C 808     -92.903  51.615 -20.899  1.00 53.43           N  
-ANISOU 6169  N   SER C 808     7178   6569   6554   1088    955    699       N  
-ATOM   6170  CA  SER C 808     -93.327  50.661 -19.881  1.00 48.96           C  
-ANISOU 6170  CA  SER C 808     6561   6061   5982   1052    912    672       C  
-ATOM   6171  C   SER C 808     -92.270  50.541 -18.808  1.00 50.63           C  
-ANISOU 6171  C   SER C 808     6827   6186   6223    971    898    597       C  
-ATOM   6172  O   SER C 808     -91.106  50.930 -19.017  1.00 52.65           O  
-ANISOU 6172  O   SER C 808     7140   6356   6509    921    905    559       O  
-ATOM   6173  CB  SER C 808     -93.576  49.287 -20.513  1.00 50.41           C  
-ANISOU 6173  CB  SER C 808     6640   6356   6160   1001    840    678       C  
-ATOM   6174  OG  SER C 808     -92.389  48.744 -21.089  1.00 50.06           O  
-ANISOU 6174  OG  SER C 808     6596   6278   6145    915    799    639       O  
-ATOM   6175  N   GLU C 809     -92.657  49.967 -17.673  1.00 49.89           N  
-ANISOU 6175  N   GLU C 809     6712   6124   6119    956    879    575       N  
-ATOM   6176  CA  GLU C 809     -91.701  49.694 -16.616  1.00 52.76           C  
-ANISOU 6176  CA  GLU C 809     7115   6428   6504    881    858    504       C  
-ATOM   6177  C   GLU C 809     -90.777  48.542 -17.054  1.00 46.11           C  
-ANISOU 6177  C   GLU C 809     6228   5608   5685    786    790    470       C  
-ATOM   6178  O   GLU C 809     -89.608  48.509 -16.702  1.00 43.26           O  
-ANISOU 6178  O   GLU C 809     5905   5185   5346    721    774    413       O  
-ATOM   6179  CB  GLU C 809     -92.392  49.349 -15.276  1.00 57.57           C  
-ANISOU 6179  CB  GLU C 809     7713   7070   7090    897    856    494       C  
-ATOM   6180  CG  GLU C 809     -91.390  49.143 -14.125  1.00 62.60           C  
-ANISOU 6180  CG  GLU C 809     8394   7649   7740    830    837    420       C  
-ATOM   6181  CD  GLU C 809     -91.803  48.233 -12.971  1.00 69.81           C  
-ANISOU 6181  CD  GLU C 809     9272   8616   8635    815    809    406       C  
-ATOM   6182  OE1 GLU C 809     -92.525  47.228 -13.179  1.00 80.07           O  
-ANISOU 6182  OE1 GLU C 809    10494  10004   9925    811    778    440       O  
-ATOM   6183  OE2 GLU C 809     -91.295  48.467 -11.853  1.00 65.09           O  
-ANISOU 6183  OE2 GLU C 809     8726   7971   8035    798    816    356       O  
-ATOM   6184  N   GLU C 810     -91.334  47.604 -17.809  1.00 43.21           N  
-ANISOU 6184  N   GLU C 810     5779   5331   5308    779    751    504       N  
-ATOM   6185  CA  GLU C 810     -90.593  46.502 -18.400  1.00 41.51           C  
-ANISOU 6185  CA  GLU C 810     5520   5141   5111    700    692    480       C  
-ATOM   6186  C   GLU C 810     -89.369  47.058 -19.169  1.00 38.76           C  
-ANISOU 6186  C   GLU C 810     5218   4720   4789    669    698    458       C  
-ATOM   6187  O   GLU C 810     -88.239  46.662 -18.919  1.00 33.07           O  
-ANISOU 6187  O   GLU C 810     4513   3961   4090    599    669    407       O  
-ATOM   6188  CB  GLU C 810     -91.550  45.734 -19.316  1.00 45.39           C  
-ANISOU 6188  CB  GLU C 810     5924   5738   5583    715    666    527       C  
-ATOM   6189  CG  GLU C 810     -91.123  44.346 -19.766  1.00 51.35           C  
-ANISOU 6189  CG  GLU C 810     6624   6537   6349    637    604    505       C  
-ATOM   6190  CD  GLU C 810     -92.253  43.594 -20.490  1.00 53.64           C  
-ANISOU 6190  CD  GLU C 810     6827   6937   6616    649    582    545       C  
-ATOM   6191  OE1 GLU C 810     -93.225  44.226 -20.946  1.00 55.35           O  
-ANISOU 6191  OE1 GLU C 810     7020   7203   6807    721    611    594       O  
-ATOM   6192  OE2 GLU C 810     -92.195  42.353 -20.570  1.00 58.74           O  
-ANISOU 6192  OE2 GLU C 810     7428   7625   7267    587    537    527       O  
-ATOM   6193  N   ALA C 811     -89.609  48.016 -20.062  1.00 37.36           N  
-ANISOU 6193  N   ALA C 811     5063   4524   4608    726    741    499       N  
-ATOM   6194  CA  ALA C 811     -88.547  48.593 -20.868  1.00 37.40           C  
-ANISOU 6194  CA  ALA C 811     5111   4461   4637    700    756    486       C  
-ATOM   6195  C   ALA C 811     -87.535  49.325 -20.005  1.00 38.46           C  
-ANISOU 6195  C   ALA C 811     5326   4491   4795    663    783    429       C  
-ATOM   6196  O   ALA C 811     -86.328  49.248 -20.252  1.00 39.24           O  
-ANISOU 6196  O   ALA C 811     5443   4548   4920    596    767    388       O  
-ATOM   6197  CB  ALA C 811     -89.118  49.522 -21.909  1.00 40.41           C  
-ANISOU 6197  CB  ALA C 811     5507   4844   5005    781    806    549       C  
-ATOM   6198  N   GLU C 812     -88.013  49.978 -18.951  1.00 37.81           N  
-ANISOU 6198  N   GLU C 812     5289   4375   4702    701    822    421       N  
-ATOM   6199  CA  GLU C 812     -87.130  50.731 -18.051  1.00 36.88           C  
-ANISOU 6199  CA  GLU C 812     5250   4161   4601    665    850    360       C  
-ATOM   6200  C   GLU C 812     -86.169  49.824 -17.295  1.00 33.81           C  
-ANISOU 6200  C   GLU C 812     4842   3782   4224    577    792    293       C  
-ATOM   6201  O   GLU C 812     -84.980  50.127 -17.190  1.00 34.71           O  
-ANISOU 6201  O   GLU C 812     4992   3836   4359    515    792    239       O  
-ATOM   6202  CB  GLU C 812     -87.917  51.618 -17.074  1.00 35.44           C  
-ANISOU 6202  CB  GLU C 812     5124   3944   4400    731    906    365       C  
-ATOM   6203  N   ILE C 813     -86.688  48.711 -16.803  1.00 31.27           N  
-ANISOU 6203  N   ILE C 813     4461   3537   3885    573    745    298       N  
-ATOM   6204  CA  ILE C 813     -85.882  47.678 -16.184  1.00 31.77           C  
-ANISOU 6204  CA  ILE C 813     4497   3622   3952    502    688    247       C  
-ATOM   6205  C   ILE C 813     -84.791  47.213 -17.174  1.00 30.50           C  
-ANISOU 6205  C   ILE C 813     4313   3459   3815    440    654    231       C  
-ATOM   6206  O   ILE C 813     -83.624  47.114 -16.818  1.00 30.15           O  
-ANISOU 6206  O   ILE C 813     4285   3386   3783    380    634    175       O  
-ATOM   6207  CB  ILE C 813     -86.738  46.438 -15.801  1.00 32.59           C  
-ANISOU 6207  CB  ILE C 813     4535   3812   4035    511    648    271       C  
-ATOM   6208  CG1 ILE C 813     -87.834  46.767 -14.780  1.00 35.89           C  
-ANISOU 6208  CG1 ILE C 813     4966   4245   4427    570    680    289       C  
-ATOM   6209  CG2 ILE C 813     -85.903  45.291 -15.230  1.00 31.62           C  
-ANISOU 6209  CG2 ILE C 813     4388   3712   3915    445    593    227       C  
-ATOM   6210  CD1 ILE C 813     -87.294  47.223 -13.468  1.00 38.59           C  
-ANISOU 6210  CD1 ILE C 813     5364   4536   4762    556    693    232       C  
-ATOM   6211  N   ILE C 814     -85.192  46.917 -18.401  1.00 30.05           N  
-ANISOU 6211  N   ILE C 814     4217   3442   3760    459    646    280       N  
-ATOM   6212  CA  ILE C 814     -84.270  46.369 -19.387  1.00 31.85           C  
-ANISOU 6212  CA  ILE C 814     4417   3679   4006    408    612    271       C  
-ATOM   6213  C   ILE C 814     -83.194  47.396 -19.743  1.00 31.51           C  
-ANISOU 6213  C   ILE C 814     4430   3556   3987    381    646    243       C  
-ATOM   6214  O   ILE C 814     -82.029  47.033 -19.839  1.00 31.99           O  
-ANISOU 6214  O   ILE C 814     4484   3606   4063    318    617    201       O  
-ATOM   6215  CB  ILE C 814     -85.018  45.847 -20.620  1.00 32.08           C  
-ANISOU 6215  CB  ILE C 814     4391   3773   4026    437    597    328       C  
-ATOM   6216  CG1 ILE C 814     -85.762  44.551 -20.235  1.00 35.40           C  
-ANISOU 6216  CG1 ILE C 814     4750   4272   4428    430    553    336       C  
-ATOM   6217  CG2 ILE C 814     -84.054  45.588 -21.749  1.00 32.62           C  
-ANISOU 6217  CG2 ILE C 814     4445   3837   4110    395    577    321       C  
-ATOM   6218  CD1 ILE C 814     -86.723  44.024 -21.288  1.00 35.98           C  
-ANISOU 6218  CD1 ILE C 814     4762   4422   4485    458    539    387       C  
-ATOM   6219  N   ARG C 815     -83.572  48.669 -19.878  1.00 31.14           N  
-ANISOU 6219  N   ARG C 815     4437   3452   3942    427    710    265       N  
-ATOM   6220  CA  ARG C 815     -82.595  49.735 -20.144  1.00 33.38           C  
-ANISOU 6220  CA  ARG C 815     4784   3648   4251    397    754    238       C  
-ATOM   6221  C   ARG C 815     -81.650  49.926 -18.965  1.00 32.64           C  
-ANISOU 6221  C   ARG C 815     4725   3511   4167    335    749    159       C  
-ATOM   6222  O   ARG C 815     -80.471  50.176 -19.175  1.00 30.13           O  
-ANISOU 6222  O   ARG C 815     4423   3153   3870    272    749    116       O  
-ATOM   6223  CB  ARG C 815     -83.251  51.073 -20.508  1.00 36.37           C  
-ANISOU 6223  CB  ARG C 815     5224   3967   4629    467    833    281       C  
-ATOM   6224  CG  ARG C 815     -83.836  51.138 -21.917  1.00 38.70           C  
-ANISOU 6224  CG  ARG C 815     5494   4295   4916    524    847    356       C  
-ATOM   6225  CD  ARG C 815     -84.257  52.575 -22.293  1.00 40.74           C  
-ANISOU 6225  CD  ARG C 815     5827   4479   5174    593    935    397       C  
-ATOM   6226  NE  ARG C 815     -85.188  53.103 -21.309  1.00 42.23           N  
-ANISOU 6226  NE  ARG C 815     6051   4652   5343    653    970    404       N  
-ATOM   6227  CZ  ARG C 815     -86.520  53.098 -21.408  1.00 43.59           C  
-ANISOU 6227  CZ  ARG C 815     6196   4882   5483    744    982    466       C  
-ATOM   6228  NH1 ARG C 815     -87.241  53.550 -20.397  1.00 43.54           N  
-ANISOU 6228  NH1 ARG C 815     6225   4860   5460    791   1013    464       N  
-ATOM   6229  NH2 ARG C 815     -87.138  52.654 -22.496  1.00 45.25           N  
-ANISOU 6229  NH2 ARG C 815     6346   5173   5674    788    963    527       N  
-ATOM   6230  N   LYS C 816     -82.144  49.745 -17.741  1.00 32.21           N  
-ANISOU 6230  N   LYS C 816     4675   3471   4092    350    740    138       N  
-ATOM   6231  CA  LYS C 816     -81.261  49.805 -16.577  1.00 33.68           C  
-ANISOU 6231  CA  LYS C 816     4886   3633   4279    293    726     60       C  
-ATOM   6232  C   LYS C 816     -80.259  48.649 -16.634  1.00 32.96           C  
-ANISOU 6232  C   LYS C 816     4737   3594   4190    228    658     26       C  
-ATOM   6233  O   LYS C 816     -79.075  48.847 -16.370  1.00 35.37           O  
-ANISOU 6233  O   LYS C 816     5055   3876   4507    164    650    -34       O  
-ATOM   6234  CB  LYS C 816     -82.030  49.713 -15.259  1.00 36.91           C  
-ANISOU 6234  CB  LYS C 816     5306   4059   4659    329    726     49       C  
-ATOM   6235  CG  LYS C 816     -81.457  50.492 -14.094  1.00 41.96           C  
-ANISOU 6235  CG  LYS C 816     6005   4643   5294    298    750    -24       C  
-ATOM   6236  CD  LYS C 816     -82.206  50.206 -12.779  1.00 47.40           C  
-ANISOU 6236  CD  LYS C 816     6695   5365   5949    336    742    -33       C  
-ATOM   6237  CE  LYS C 816     -81.765  51.199 -11.714  1.00 55.09           C  
-ANISOU 6237  CE  LYS C 816     7740   6275   6916    316    777   -104       C  
-ATOM   6238  NZ  LYS C 816     -82.426  51.137 -10.374  1.00 57.26           N  
-ANISOU 6238  NZ  LYS C 816     8030   6571   7155    355    779   -120       N  
-ATOM   6239  N   TYR C 817     -80.729  47.446 -16.961  1.00 29.51           N  
-ANISOU 6239  N   TYR C 817     4239   3232   3743    244    611     63       N  
-ATOM   6240  CA  TYR C 817     -79.847  46.287 -17.015  1.00 27.15           C  
-ANISOU 6240  CA  TYR C 817     3890   2981   3443    193    551     37       C  
-ATOM   6241  C   TYR C 817     -78.715  46.574 -18.019  1.00 26.48           C  
-ANISOU 6241  C   TYR C 817     3806   2870   3384    145    553     21       C  
-ATOM   6242  O   TYR C 817     -77.551  46.342 -17.730  1.00 26.03           O  
-ANISOU 6242  O   TYR C 817     3740   2819   3332     89    527    -31       O  
-ATOM   6243  CB  TYR C 817     -80.647  45.057 -17.421  1.00 24.91           C  
-ANISOU 6243  CB  TYR C 817     3550   2767   3147    219    513     85       C  
-ATOM   6244  CG  TYR C 817     -80.058  43.695 -17.139  1.00 23.01           C  
-ANISOU 6244  CG  TYR C 817     3267   2579   2898    184    455     64       C  
-ATOM   6245  CD1 TYR C 817     -78.809  43.518 -16.545  1.00 22.85           C  
-ANISOU 6245  CD1 TYR C 817     3251   2557   2876    137    431      6       C  
-ATOM   6246  CD2 TYR C 817     -80.763  42.556 -17.520  1.00 22.05           C  
-ANISOU 6246  CD2 TYR C 817     3099   2512   2766    200    426    104       C  
-ATOM   6247  CE1 TYR C 817     -78.295  42.228 -16.324  1.00 21.89           C  
-ANISOU 6247  CE1 TYR C 817     3091   2484   2741    117    381     -6       C  
-ATOM   6248  CE2 TYR C 817     -80.273  41.281 -17.280  1.00 21.95           C  
-ANISOU 6248  CE2 TYR C 817     3056   2538   2745    173    380     88       C  
-ATOM   6249  CZ  TYR C 817     -79.065  41.117 -16.678  1.00 21.85           C  
-ANISOU 6249  CZ  TYR C 817     3051   2522   2729    138    358     37       C  
-ATOM   6250  OH  TYR C 817     -78.634  39.836 -16.539  1.00 22.88           O  
-ANISOU 6250  OH  TYR C 817     3154   2691   2848    123    317     31       O  
-ATOM   6251  N   VAL C 818     -79.063  47.116 -19.173  1.00 27.32           N  
-ANISOU 6251  N   VAL C 818     3922   2954   3505    170    586     68       N  
-ATOM   6252  CA  VAL C 818     -78.064  47.443 -20.174  1.00 29.13           C  
-ANISOU 6252  CA  VAL C 818     4153   3157   3758    130    596     61       C  
-ATOM   6253  C   VAL C 818     -77.074  48.504 -19.673  1.00 30.25           C  
-ANISOU 6253  C   VAL C 818     4347   3230   3918     78    633      1       C  
-ATOM   6254  O   VAL C 818     -75.860  48.362 -19.819  1.00 30.35           O  
-ANISOU 6254  O   VAL C 818     4344   3246   3943     15    614    -42       O  
-ATOM   6255  CB  VAL C 818     -78.710  47.968 -21.470  1.00 30.49           C  
-ANISOU 6255  CB  VAL C 818     4334   3314   3938    178    635    127       C  
-ATOM   6256  CG1 VAL C 818     -77.633  48.518 -22.414  1.00 29.51           C  
-ANISOU 6256  CG1 VAL C 818     4224   3149   3839    136    659    118       C  
-ATOM   6257  CG2 VAL C 818     -79.508  46.873 -22.158  1.00 29.53           C  
-ANISOU 6257  CG2 VAL C 818     4152   3270   3799    213    594    178       C  
-ATOM   6258  N   LYS C 819     -77.599  49.554 -19.064  1.00 31.73           N  
-ANISOU 6258  N   LYS C 819     4594   3357   4104    103    685     -5       N  
-ATOM   6259  CA  LYS C 819     -76.778  50.652 -18.629  1.00 34.80           C  
-ANISOU 6259  CA  LYS C 819     5039   3671   4510     52    729    -64       C  
-ATOM   6260  C   LYS C 819     -75.850  50.283 -17.490  1.00 33.38           C  
-ANISOU 6260  C   LYS C 819     4844   3519   4321    -11    688   -145       C  
-ATOM   6261  O   LYS C 819     -74.673  50.625 -17.500  1.00 36.68           O  
-ANISOU 6261  O   LYS C 819     5266   3917   4754    -83    691   -201       O  
-ATOM   6262  CB  LYS C 819     -77.646  51.827 -18.198  1.00 40.52           C  
-ANISOU 6262  CB  LYS C 819     5839   4323   5234    101    799    -51       C  
-ATOM   6263  CG  LYS C 819     -76.820  53.122 -18.147  1.00 45.53           C  
-ANISOU 6263  CG  LYS C 819     6545   4860   5894     46    862   -101       C  
-ATOM   6264  CD  LYS C 819     -77.032  53.958 -16.906  1.00 52.99           C  
-ANISOU 6264  CD  LYS C 819     7556   5748   6829     45    900   -153       C  
-ATOM   6265  CE  LYS C 819     -76.509  55.389 -17.134  1.00 57.55           C  
-ANISOU 6265  CE  LYS C 819     8219   6210   7437      5    984   -182       C  
-ATOM   6266  NZ  LYS C 819     -75.604  55.907 -16.065  1.00 61.47           N  
-ANISOU 6266  NZ  LYS C 819     8750   6671   7936    -79    991   -285       N  
-ATOM   6267  N   ASN C 820     -76.381  49.614 -16.492  1.00 31.66           N  
-ANISOU 6267  N   ASN C 820     4607   3349   4074     16    652   -153       N  
-ATOM   6268  CA  ASN C 820     -75.594  49.295 -15.331  1.00 31.39           C  
-ANISOU 6268  CA  ASN C 820     4560   3346   4021    -30    615   -227       C  
-ATOM   6269  C   ASN C 820     -74.578  48.198 -15.501  1.00 30.27           C  
-ANISOU 6269  C   ASN C 820     4352   3276   3873    -73    552   -248       C  
-ATOM   6270  O   ASN C 820     -73.625  48.167 -14.750  1.00 32.77           O  
-ANISOU 6270  O   ASN C 820     4658   3614   4178   -123    529   -316       O  
-ATOM   6271  CB  ASN C 820     -76.502  48.885 -14.198  1.00 33.89           C  
-ANISOU 6271  CB  ASN C 820     4878   3694   4304     19    599   -223       C  
-ATOM   6272  CG  ASN C 820     -77.251  50.044 -13.603  1.00 36.15           C  
-ANISOU 6272  CG  ASN C 820     5236   3913   4587     52    660   -229       C  
-ATOM   6273  OD1 ASN C 820     -76.976  51.194 -13.897  1.00 37.84           O  
-ANISOU 6273  OD1 ASN C 820     5504   4049   4823     30    715   -247       O  
-ATOM   6274  ND2 ASN C 820     -78.194  49.737 -12.737  1.00 38.30           N  
-ANISOU 6274  ND2 ASN C 820     5510   4212   4830    106    654   -213       N  
-ATOM   6275  N   THR C 821     -74.761  47.277 -16.443  1.00 28.18           N  
-ANISOU 6275  N   THR C 821     4041   3052   3612    -52    522   -194       N  
-ATOM   6276  CA  THR C 821     -73.868  46.115 -16.510  1.00 28.97           C  
-ANISOU 6276  CA  THR C 821     4082   3223   3702    -80    462   -212       C  
-ATOM   6277  C   THR C 821     -72.900  46.170 -17.693  1.00 29.88           C  
-ANISOU 6277  C   THR C 821     4175   3335   3842   -123    462   -211       C  
-ATOM   6278  O   THR C 821     -72.310  45.164 -18.074  1.00 29.50           O  
-ANISOU 6278  O   THR C 821     4079   3344   3788   -133    418   -208       O  
-ATOM   6279  CB  THR C 821     -74.647  44.771 -16.478  1.00 25.92           C  
-ANISOU 6279  CB  THR C 821     3657   2897   3295    -31    419   -164       C  
-ATOM   6280  OG1 THR C 821     -75.345  44.604 -17.707  1.00 25.93           O  
-ANISOU 6280  OG1 THR C 821     3648   2892   3312     -1    430    -99       O  
-ATOM   6281  CG2 THR C 821     -75.619  44.767 -15.334  1.00 25.13           C  
-ANISOU 6281  CG2 THR C 821     3579   2800   3171     10    425   -161       C  
-ATOM   6282  N   HIS C 822     -72.699  47.361 -18.243  1.00 32.20           N  
-ANISOU 6282  N   HIS C 822     4509   3561   4164   -147    517   -216       N  
-ATOM   6283  CA  HIS C 822     -71.639  47.556 -19.223  1.00 32.07           C  
-ANISOU 6283  CA  HIS C 822     4476   3538   4171   -197    525   -225       C  
-ATOM   6284  C   HIS C 822     -70.299  47.550 -18.511  1.00 31.43           C  
-ANISOU 6284  C   HIS C 822     4371   3488   4083   -268    501   -305       C  
-ATOM   6285  O   HIS C 822     -70.090  48.347 -17.648  1.00 34.00           O  
-ANISOU 6285  O   HIS C 822     4730   3782   4407   -301    524   -360       O  
-ATOM   6286  CB  HIS C 822     -71.828  48.861 -19.969  1.00 32.99           C  
-ANISOU 6286  CB  HIS C 822     4649   3568   4319   -202    598   -204       C  
-ATOM   6287  CG  HIS C 822     -70.985  48.951 -21.193  1.00 34.59           C  
-ANISOU 6287  CG  HIS C 822     4832   3767   4545   -238    610   -191       C  
-ATOM   6288  ND1 HIS C 822     -71.509  49.168 -22.439  1.00 32.89           N  
-ANISOU 6288  ND1 HIS C 822     4629   3526   4344   -198    642   -122       N  
-ATOM   6289  CD2 HIS C 822     -69.647  48.799 -21.363  1.00 35.12           C  
-ANISOU 6289  CD2 HIS C 822     4863   3863   4620   -306    592   -236       C  
-ATOM   6290  CE1 HIS C 822     -70.531  49.159 -23.327  1.00 33.34           C  
-ANISOU 6290  CE1 HIS C 822     4662   3589   4417   -240    645   -125       C  
-ATOM   6291  NE2 HIS C 822     -69.394  48.938 -22.700  1.00 33.17           N  
-ANISOU 6291  NE2 HIS C 822     4610   3600   4393   -307    616   -193       N  
-ATOM   6292  N   ALA C 823     -69.403  46.622 -18.839  1.00 32.79           N  
-ANISOU 6292  N   ALA C 823     4484   3729   4247   -289    453   -314       N  
-ATOM   6293  CA  ALA C 823     -68.141  46.490 -18.109  1.00 33.31           C  
-ANISOU 6293  CA  ALA C 823     4514   3845   4296   -348    423   -389       C  
-ATOM   6294  C   ALA C 823     -67.163  47.621 -18.415  1.00 36.24           C  
-ANISOU 6294  C   ALA C 823     4900   4176   4696   -428    466   -438       C  
-ATOM   6295  O   ALA C 823     -67.129  48.116 -19.532  1.00 34.97           O  
-ANISOU 6295  O   ALA C 823     4754   3966   4566   -438    506   -403       O  
-ATOM   6296  CB  ALA C 823     -67.484  45.167 -18.441  1.00 34.42           C  
-ANISOU 6296  CB  ALA C 823     4588   4071   4417   -337    364   -378       C  
-ATOM   6297  N   THR C 824     -66.374  48.023 -17.411  1.00 42.32           N  
-ANISOU 6297  N   THR C 824     5662   4966   5451   -485    459   -520       N  
-ATOM   6298  CA  THR C 824     -65.387  49.130 -17.567  1.00 46.94           C  
-ANISOU 6298  CA  THR C 824     6259   5514   6062   -577    502   -580       C  
-ATOM   6299  C   THR C 824     -64.338  48.833 -18.628  1.00 46.62           C  
-ANISOU 6299  C   THR C 824     6164   5511   6037   -616    495   -572       C  
-ATOM   6300  O   THR C 824     -63.904  49.748 -19.310  1.00 51.07           O  
-ANISOU 6300  O   THR C 824     6751   6016   6636   -672    549   -580       O  
-ATOM   6301  CB  THR C 824     -64.580  49.480 -16.297  1.00 47.13           C  
-ANISOU 6301  CB  THR C 824     6268   5577   6061   -642    486   -681       C  
-ATOM   6302  OG1 THR C 824     -63.806  48.343 -15.895  1.00 45.08           O  
-ANISOU 6302  OG1 THR C 824     5929   5438   5762   -636    413   -703       O  
-ATOM   6303  CG2 THR C 824     -65.499  49.936 -15.177  1.00 46.46           C  
-ANISOU 6303  CG2 THR C 824     6241   5451   5959   -613    500   -701       C  
-ATOM   6304  N   THR C 825     -63.943  47.574 -18.777  1.00 43.54           N  
-ANISOU 6304  N   THR C 825     5708   5214   5622   -585    433   -554       N  
-ATOM   6305  CA  THR C 825     -62.916  47.220 -19.755  1.00 42.83           C  
-ANISOU 6305  CA  THR C 825     5563   5169   5541   -616    423   -547       C  
-ATOM   6306  C   THR C 825     -63.417  47.067 -21.179  1.00 42.05           C  
-ANISOU 6306  C   THR C 825     5479   5029   5469   -575    447   -465       C  
-ATOM   6307  O   THR C 825     -62.629  46.773 -22.075  1.00 43.68           O  
-ANISOU 6307  O   THR C 825     5644   5269   5683   -594    443   -453       O  
-ATOM   6308  CB  THR C 825     -62.202  45.903 -19.396  1.00 42.45           C  
-ANISOU 6308  CB  THR C 825     5439   5239   5451   -593    350   -561       C  
-ATOM   6309  OG1 THR C 825     -63.143  44.825 -19.398  1.00 37.92           O  
-ANISOU 6309  OG1 THR C 825     4870   4681   4858   -505    315   -500       O  
-ATOM   6310  CG2 THR C 825     -61.534  46.020 -18.018  1.00 43.65           C  
-ANISOU 6310  CG2 THR C 825     5563   5453   5567   -633    321   -646       C  
-ATOM   6311  N   HIS C 826     -64.713  47.197 -21.398  1.00 41.39           N  
-ANISOU 6311  N   HIS C 826     5447   4884   5394   -515    469   -408       N  
-ATOM   6312  CA  HIS C 826     -65.265  47.086 -22.755  1.00 40.28           C  
-ANISOU 6312  CA  HIS C 826     5319   4712   5272   -472    492   -330       C  
-ATOM   6313  C   HIS C 826     -65.600  48.485 -23.232  1.00 41.32           C  
-ANISOU 6313  C   HIS C 826     5518   4742   5440   -493    572   -315       C  
-ATOM   6314  O   HIS C 826     -66.755  48.840 -23.467  1.00 37.19           O  
-ANISOU 6314  O   HIS C 826     5044   4163   4923   -438    603   -264       O  
-ATOM   6315  CB  HIS C 826     -66.497  46.163 -22.752  1.00 37.34           C  
-ANISOU 6315  CB  HIS C 826     4951   4357   4880   -386    459   -272       C  
-ATOM   6316  CG  HIS C 826     -66.182  44.749 -22.364  1.00 34.79           C  
-ANISOU 6316  CG  HIS C 826     4572   4123   4523   -362    389   -279       C  
-ATOM   6317  ND1 HIS C 826     -67.060  43.949 -21.661  1.00 32.38           N  
-ANISOU 6317  ND1 HIS C 826     4269   3841   4192   -308    354   -262       N  
-ATOM   6318  CD2 HIS C 826     -65.061  44.008 -22.549  1.00 32.43           C  
-ANISOU 6318  CD2 HIS C 826     4216   3895   4210   -383    351   -301       C  
-ATOM   6319  CE1 HIS C 826     -66.494  42.775 -21.431  1.00 31.37           C  
-ANISOU 6319  CE1 HIS C 826     4094   3787   4037   -296    301   -273       C  
-ATOM   6320  NE2 HIS C 826     -65.286  42.786 -21.963  1.00 32.62           N  
-ANISOU 6320  NE2 HIS C 826     4215   3977   4201   -337    298   -296       N  
-ATOM   6321  N   ASN C 827     -64.547  49.278 -23.351  1.00 45.97           N  
-ANISOU 6321  N   ASN C 827     6106   5310   6051   -574    607   -362       N  
-ATOM   6322  CA  ASN C 827     -64.674  50.727 -23.554  1.00 50.55           C  
-ANISOU 6322  CA  ASN C 827     6757   5783   6666   -612    692   -367       C  
-ATOM   6323  C   ASN C 827     -64.655  51.154 -25.033  1.00 46.89           C  
-ANISOU 6323  C   ASN C 827     6313   5273   6231   -603    746   -303       C  
-ATOM   6324  O   ASN C 827     -64.792  52.325 -25.334  1.00 49.76           O  
-ANISOU 6324  O   ASN C 827     6742   5542   6623   -624    823   -294       O  
-ATOM   6325  CB  ASN C 827     -63.605  51.479 -22.735  1.00 54.67           C  
-ANISOU 6325  CB  ASN C 827     7278   6298   7198   -716    711   -463       C  
-ATOM   6326  CG  ASN C 827     -62.191  50.968 -22.988  1.00 56.59           C  
-ANISOU 6326  CG  ASN C 827     7439   6628   7436   -779    676   -502       C  
-ATOM   6327  OD1 ASN C 827     -61.942  50.093 -23.828  1.00 59.55           O  
-ANISOU 6327  OD1 ASN C 827     7763   7062   7803   -746    643   -458       O  
-ATOM   6328  ND2 ASN C 827     -61.259  51.504 -22.232  1.00 58.62           N  
-ANISOU 6328  ND2 ASN C 827     7680   6899   7694   -871    682   -590       N  
-ATOM   6329  N   ALA C 828     -64.550  50.193 -25.944  1.00 44.14           N  
-ANISOU 6329  N   ALA C 828     5914   4988   5871   -563    707   -255       N  
-ATOM   6330  CA  ALA C 828     -64.622  50.458 -27.371  1.00 44.52           C  
-ANISOU 6330  CA  ALA C 828     5975   5004   5936   -540    751   -188       C  
-ATOM   6331  C   ALA C 828     -65.969  51.041 -27.864  1.00 48.42           C  
-ANISOU 6331  C   ALA C 828     6538   5425   6435   -464    800   -115       C  
-ATOM   6332  O   ALA C 828     -66.022  51.592 -28.968  1.00 49.22           O  
-ANISOU 6332  O   ALA C 828     6667   5483   6552   -448    854    -63       O  
-ATOM   6333  CB  ALA C 828     -64.294  49.185 -28.138  1.00 45.73           C  
-ANISOU 6333  CB  ALA C 828     6059   5249   6068   -507    691   -158       C  
-ATOM   6334  N   TYR C 829     -67.049  50.899 -27.082  1.00 44.99           N  
-ANISOU 6334  N   TYR C 829     6127   4983   5983   -411    781   -109       N  
-ATOM   6335  CA  TYR C 829     -68.361  51.355 -27.525  1.00 41.94           C  
-ANISOU 6335  CA  TYR C 829     5794   4545   5594   -330    822    -38       C  
-ATOM   6336  C   TYR C 829     -69.291  51.621 -26.346  1.00 41.29           C  
-ANISOU 6336  C   TYR C 829     5752   4435   5502   -300    822    -56       C  
-ATOM   6337  O   TYR C 829     -69.003  51.233 -25.225  1.00 40.33           O  
-ANISOU 6337  O   TYR C 829     5609   4347   5369   -333    779   -116       O  
-ATOM   6338  CB  TYR C 829     -68.993  50.321 -28.466  1.00 39.39           C  
-ANISOU 6338  CB  TYR C 829     5428   4290   5247   -255    777     29       C  
-ATOM   6339  CG  TYR C 829     -69.142  48.925 -27.843  1.00 40.09           C  
-ANISOU 6339  CG  TYR C 829     5456   4468   5307   -240    689      8       C  
-ATOM   6340  CD1 TYR C 829     -70.201  48.637 -26.980  1.00 37.90           C  
-ANISOU 6340  CD1 TYR C 829     5189   4199   5011   -195    665     11       C  
-ATOM   6341  CD2 TYR C 829     -68.207  47.918 -28.080  1.00 38.32           C  
-ANISOU 6341  CD2 TYR C 829     5169   4318   5074   -270    634    -15       C  
-ATOM   6342  CE1 TYR C 829     -70.327  47.389 -26.382  1.00 37.34           C  
-ANISOU 6342  CE1 TYR C 829     5070   4202   4916   -183    593     -6       C  
-ATOM   6343  CE2 TYR C 829     -68.322  46.677 -27.481  1.00 36.83           C  
-ANISOU 6343  CE2 TYR C 829     4935   4201   4860   -254    563    -32       C  
-ATOM   6344  CZ  TYR C 829     -69.400  46.411 -26.642  1.00 38.05           C  
-ANISOU 6344  CZ  TYR C 829     5103   4357   4997   -211    543    -26       C  
-ATOM   6345  OH  TYR C 829     -69.575  45.180 -26.051  1.00 34.73           O  
-ANISOU 6345  OH  TYR C 829     4644   4000   4551   -193    479    -38       O  
-ATOM   6346  N   ASP C 830     -70.368  52.345 -26.618  1.00 41.43           N  
-ANISOU 6346  N   ASP C 830     5829   4392   5521   -235    876     -1       N  
-ATOM   6347  CA  ASP C 830     -71.510  52.431 -25.731  1.00 44.72           C  
-ANISOU 6347  CA  ASP C 830     6275   4796   5919   -180    873      6       C  
-ATOM   6348  C   ASP C 830     -72.653  51.806 -26.410  1.00 37.15           C  
-ANISOU 6348  C   ASP C 830     5293   3886   4937    -88    850     82       C  
-ATOM   6349  O   ASP C 830     -72.663  51.729 -27.605  1.00 38.48           O  
-ANISOU 6349  O   ASP C 830     5448   4066   5105    -61    862    135       O  
-ATOM   6350  CB  ASP C 830     -71.973  53.877 -25.567  1.00 51.80           C  
-ANISOU 6350  CB  ASP C 830     7266   5583   6834   -164    965     16       C  
-ATOM   6351  CG  ASP C 830     -70.929  54.758 -24.975  1.00 60.45           C  
-ANISOU 6351  CG  ASP C 830     8402   6609   7957   -261   1008    -61       C  
-ATOM   6352  OD1 ASP C 830     -70.007  54.241 -24.301  1.00 70.26           O  
-ANISOU 6352  OD1 ASP C 830     9597   7901   9198   -334    957   -133       O  
-ATOM   6353  OD2 ASP C 830     -71.042  55.979 -25.193  1.00 66.17           O  
-ANISOU 6353  OD2 ASP C 830     9207   7230   8703   -261   1096    -48       O  
-ATOM   6354  N   LEU C 831     -73.668  51.470 -25.642  1.00 36.05           N  
-ANISOU 6354  N   LEU C 831     5152   3770   4775    -38    825     90       N  
-ATOM   6355  CA  LEU C 831     -74.812  50.808 -26.196  1.00 34.78           C  
-ANISOU 6355  CA  LEU C 831     4960   3667   4588     43    799    156       C  
-ATOM   6356  C   LEU C 831     -76.019  51.646 -26.053  1.00 32.88           C  
-ANISOU 6356  C   LEU C 831     4772   3382   4338    118    853    201       C  
-ATOM   6357  O   LEU C 831     -76.217  52.299 -25.043  1.00 31.57           O  
-ANISOU 6357  O   LEU C 831     4656   3164   4177    114    882    170       O  
-ATOM   6358  CB  LEU C 831     -75.082  49.489 -25.476  1.00 34.86           C  
-ANISOU 6358  CB  LEU C 831     4910   3760   4575     44    718    134       C  
-ATOM   6359  CG  LEU C 831     -74.069  48.380 -25.749  1.00 34.40           C  
-ANISOU 6359  CG  LEU C 831     4790   3764   4516     -7    656    105       C  
-ATOM   6360  CD1 LEU C 831     -74.244  47.211 -24.800  1.00 34.59           C  
-ANISOU 6360  CD1 LEU C 831     4771   3852   4519    -11    589     76       C  
-ATOM   6361  CD2 LEU C 831     -74.170  47.934 -27.193  1.00 34.80           C  
-ANISOU 6361  CD2 LEU C 831     4809   3853   4561     22    648    159       C  
-ATOM   6362  N   GLU C 832     -76.851  51.584 -27.066  1.00 33.47           N  
-ANISOU 6362  N   GLU C 832     4835   3485   4396    191    863    275       N  
-ATOM   6363  CA  GLU C 832     -78.116  52.272 -27.041  1.00 39.17           C  
-ANISOU 6363  CA  GLU C 832     5596   4185   5100    279    910    329       C  
-ATOM   6364  C   GLU C 832     -79.194  51.299 -27.480  1.00 36.57           C  
-ANISOU 6364  C   GLU C 832     5200   3957   4736    343    859    379       C  
-ATOM   6365  O   GLU C 832     -79.085  50.676 -28.548  1.00 37.07           O  
-ANISOU 6365  O   GLU C 832     5217   4079   4790    349    830    408       O  
-ATOM   6366  CB  GLU C 832     -78.018  53.467 -28.005  1.00 45.52           C  
-ANISOU 6366  CB  GLU C 832     6463   4916   5917    311    995    377       C  
-ATOM   6367  CG  GLU C 832     -79.325  54.112 -28.390  1.00 52.61           C  
-ANISOU 6367  CG  GLU C 832     7393   5808   6789    423   1046    454       C  
-ATOM   6368  CD  GLU C 832     -79.144  55.344 -29.287  1.00 58.69           C  
-ANISOU 6368  CD  GLU C 832     8235   6493   7570    457   1139    503       C  
-ATOM   6369  OE1 GLU C 832     -78.041  55.585 -29.854  1.00 55.19           O  
-ANISOU 6369  OE1 GLU C 832     7807   6008   7154    395   1161    487       O  
-ATOM   6370  OE2 GLU C 832     -80.144  56.079 -29.411  1.00 64.69           O  
-ANISOU 6370  OE2 GLU C 832     9039   7230   8310    551   1195    562       O  
-ATOM   6371  N   VAL C 833     -80.233  51.175 -26.670  1.00 35.28           N  
-ANISOU 6371  N   VAL C 833     5033   3819   4553    387    850    386       N  
-ATOM   6372  CA  VAL C 833     -81.318  50.267 -26.977  1.00 33.05           C  
-ANISOU 6372  CA  VAL C 833     4684   3634   4237    440    804    428       C  
-ATOM   6373  C   VAL C 833     -82.226  50.907 -27.996  1.00 34.51           C  
-ANISOU 6373  C   VAL C 833     4878   3833   4399    532    850    507       C  
-ATOM   6374  O   VAL C 833     -82.701  52.000 -27.788  1.00 38.06           O  
-ANISOU 6374  O   VAL C 833     5389   4225   4847    587    917    534       O  
-ATOM   6375  CB  VAL C 833     -82.097  49.911 -25.708  1.00 32.78           C  
-ANISOU 6375  CB  VAL C 833     4640   3625   4190    453    782    408       C  
-ATOM   6376  CG1 VAL C 833     -83.281  49.007 -26.045  1.00 32.30           C  
-ANISOU 6376  CG1 VAL C 833     4508   3668   4095    502    740    452       C  
-ATOM   6377  CG2 VAL C 833     -81.181  49.219 -24.700  1.00 33.51           C  
-ANISOU 6377  CG2 VAL C 833     4721   3713   4298    369    735    333       C  
-ATOM   6378  N   ILE C 834     -82.412  50.263 -29.131  1.00 35.69           N  
-ANISOU 6378  N   ILE C 834     4972   4058   4529    551    818    543       N  
-ATOM   6379  CA  ILE C 834     -83.257  50.802 -30.175  1.00 35.82           C  
-ANISOU 6379  CA  ILE C 834     4988   4105   4516    643    856    619       C  
-ATOM   6380  C   ILE C 834     -84.644  50.249 -30.006  1.00 37.80           C  
-ANISOU 6380  C   ILE C 834     5181   4452   4727    703    825    650       C  
-ATOM   6381  O   ILE C 834     -85.592  51.011 -29.845  1.00 41.33           O  
-ANISOU 6381  O   ILE C 834     5653   4897   5154    785    872    695       O  
-ATOM   6382  CB  ILE C 834     -82.731  50.459 -31.584  1.00 38.33           C  
-ANISOU 6382  CB  ILE C 834     5274   4461   4826    636    840    643       C  
-ATOM   6383  CG1 ILE C 834     -81.406  51.153 -31.820  1.00 39.56           C  
-ANISOU 6383  CG1 ILE C 834     5489   4521   5020    583    884    621       C  
-ATOM   6384  CG2 ILE C 834     -83.707  50.925 -32.669  1.00 38.84           C  
-ANISOU 6384  CG2 ILE C 834     5329   4579   4850    741    873    725       C  
-ATOM   6385  CD1 ILE C 834     -80.715  50.637 -33.054  1.00 42.78           C  
-ANISOU 6385  CD1 ILE C 834     5861   4969   5424    561    859    631       C  
-ATOM   6386  N   ASP C 835     -84.765  48.925 -30.030  1.00 37.21           N  
-ANISOU 6386  N   ASP C 835     5031   4464   4643    661    749    626       N  
-ATOM   6387  CA  ASP C 835     -86.051  48.235 -29.810  1.00 37.61           C  
-ANISOU 6387  CA  ASP C 835     5017   4613   4660    699    714    646       C  
-ATOM   6388  C   ASP C 835     -85.908  47.087 -28.826  1.00 36.28           C  
-ANISOU 6388  C   ASP C 835     4814   4467   4505    625    654    589       C  
-ATOM   6389  O   ASP C 835     -84.851  46.429 -28.766  1.00 32.22           O  
-ANISOU 6389  O   ASP C 835     4297   3931   4014    549    618    541       O  
-ATOM   6390  CB  ASP C 835     -86.561  47.631 -31.125  1.00 41.77           C  
-ANISOU 6390  CB  ASP C 835     5475   5245   5151    729    682    684       C  
-ATOM   6391  CG  ASP C 835     -86.909  48.692 -32.164  1.00 46.52           C  
-ANISOU 6391  CG  ASP C 835     6101   5848   5727    820    739    753       C  
-ATOM   6392  OD1 ASP C 835     -86.495  48.506 -33.334  1.00 51.27           O  
-ANISOU 6392  OD1 ASP C 835     6683   6479   6317    819    729    769       O  
-ATOM   6393  OD2 ASP C 835     -87.628  49.667 -31.811  1.00 46.10           O  
-ANISOU 6393  OD2 ASP C 835     6084   5771   5660    897    796    793       O  
-ATOM   6394  N   ILE C 836     -86.980  46.838 -28.087  1.00 33.81           N  
-ANISOU 6394  N   ILE C 836     4473   4201   4173    654    646    598       N  
-ATOM   6395  CA  ILE C 836     -87.063  45.729 -27.175  1.00 31.65           C  
-ANISOU 6395  CA  ILE C 836     4164   3958   3905    597    596    555       C  
-ATOM   6396  C   ILE C 836     -88.227  44.883 -27.608  1.00 32.94           C  
-ANISOU 6396  C   ILE C 836     4247   4235   4034    618    561    582       C  
-ATOM   6397  O   ILE C 836     -89.358  45.383 -27.700  1.00 36.85           O  
-ANISOU 6397  O   ILE C 836     4723   4779   4500    691    588    629       O  
-ATOM   6398  CB  ILE C 836     -87.282  46.193 -25.739  1.00 32.73           C  
-ANISOU 6398  CB  ILE C 836     4343   4044   4050    604    622    536       C  
-ATOM   6399  CG1 ILE C 836     -86.154  47.126 -25.305  1.00 32.19           C  
-ANISOU 6399  CG1 ILE C 836     4355   3863   4013    580    660    503       C  
-ATOM   6400  CG2 ILE C 836     -87.320  44.993 -24.806  1.00 31.94           C  
-ANISOU 6400  CG2 ILE C 836     4207   3975   3954    547    571    495       C  
-ATOM   6401  CD1 ILE C 836     -86.396  47.810 -23.974  1.00 31.92           C  
-ANISOU 6401  CD1 ILE C 836     4373   3774   3983    597    696    485       C  
-ATOM   6402  N   PHE C 837     -87.955  43.616 -27.901  1.00 30.40           N  
-ANISOU 6402  N   PHE C 837     3878   3959   3715    555    504    553       N  
-ATOM   6403  CA  PHE C 837     -88.982  42.689 -28.308  1.00 30.68           C  
-ANISOU 6403  CA  PHE C 837     3835   4102   3721    555    468    567       C  
-ATOM   6404  C   PHE C 837     -89.184  41.601 -27.250  1.00 29.87           C  
-ANISOU 6404  C   PHE C 837     3710   4011   3627    497    435    529       C  
-ATOM   6405  O   PHE C 837     -88.226  41.093 -26.681  1.00 28.48           O  
-ANISOU 6405  O   PHE C 837     3563   3779   3478    439    416    486       O  
-ATOM   6406  CB  PHE C 837     -88.603  42.017 -29.618  1.00 31.86           C  
-ANISOU 6406  CB  PHE C 837     3948   4297   3861    528    433    562       C  
-ATOM   6407  CG  PHE C 837     -88.346  42.963 -30.763  1.00 33.08           C  
-ANISOU 6407  CG  PHE C 837     4122   4446   4003    583    464    601       C  
-ATOM   6408  CD1 PHE C 837     -89.389  43.415 -31.538  1.00 34.22           C  
-ANISOU 6408  CD1 PHE C 837     4227   4670   4105    658    480    654       C  
-ATOM   6409  CD2 PHE C 837     -87.066  43.391 -31.062  1.00 33.29           C  
-ANISOU 6409  CD2 PHE C 837     4202   4390   4057    561    479    586       C  
-ATOM   6410  CE1 PHE C 837     -89.172  44.291 -32.580  1.00 35.07           C  
-ANISOU 6410  CE1 PHE C 837     4356   4772   4197    717    513    696       C  
-ATOM   6411  CE2 PHE C 837     -86.837  44.267 -32.111  1.00 34.36           C  
-ANISOU 6411  CE2 PHE C 837     4359   4516   4181    611    513    626       C  
-ATOM   6412  CZ  PHE C 837     -87.898  44.729 -32.864  1.00 34.05           C  
-ANISOU 6412  CZ  PHE C 837     4287   4552   4098    693    532    683       C  
-ATOM   6413  N   LYS C 838     -90.443  41.250 -27.004  1.00 31.90           N  
-ANISOU 6413  N   LYS C 838     3913   4347   3859    517    430    550       N  
-ATOM   6414  CA  LYS C 838     -90.790  40.124 -26.168  1.00 34.11           C  
-ANISOU 6414  CA  LYS C 838     4164   4652   4144    462    402    522       C  
-ATOM   6415  C   LYS C 838     -90.990  38.969 -27.099  1.00 31.67           C  
-ANISOU 6415  C   LYS C 838     3795   4416   3823    414    358    509       C  
-ATOM   6416  O   LYS C 838     -91.769  39.066 -28.036  1.00 29.84           O  
-ANISOU 6416  O   LYS C 838     3510   4267   3560    446    355    538       O  
-ATOM   6417  CB  LYS C 838     -92.084  40.375 -25.385  1.00 40.56           C  
-ANISOU 6417  CB  LYS C 838     4952   5518   4940    506    425    550       C  
-ATOM   6418  CG  LYS C 838     -92.584  39.152 -24.575  1.00 47.35           C  
-ANISOU 6418  CG  LYS C 838     5775   6413   5803    447    400    527       C  
-ATOM   6419  CD  LYS C 838     -92.613  39.306 -23.057  1.00 59.95           C  
-ANISOU 6419  CD  LYS C 838     7410   7958   7410    451    422    517       C  
-ATOM   6420  CE  LYS C 838     -93.388  38.176 -22.319  1.00 65.48           C  
-ANISOU 6420  CE  LYS C 838     8066   8708   8106    407    408    509       C  
-ATOM   6421  NZ  LYS C 838     -93.363  36.796 -22.920  1.00 65.63           N  
-ANISOU 6421  NZ  LYS C 838     8041   8767   8128    330    368    485       N  
-ATOM   6422  N   ILE C 839     -90.315  37.853 -26.827  1.00 29.17           N  
-ANISOU 6422  N   ILE C 839     3486   4071   3527    340    326    466       N  
-ATOM   6423  CA  ILE C 839     -90.390  36.691 -27.729  1.00 28.67           C  
-ANISOU 6423  CA  ILE C 839     3376   4063   3454    287    286    446       C  
-ATOM   6424  C   ILE C 839     -90.863  35.399 -27.051  1.00 28.83           C  
-ANISOU 6424  C   ILE C 839     3370   4105   3478    224    267    421       C  
-ATOM   6425  O   ILE C 839     -90.506  35.122 -25.904  1.00 29.60           O  
-ANISOU 6425  O   ILE C 839     3505   4145   3597    203    273    404       O  
-ATOM   6426  CB  ILE C 839     -89.029  36.453 -28.424  1.00 28.08           C  
-ANISOU 6426  CB  ILE C 839     3337   3936   3397    257    267    419       C  
-ATOM   6427  CG1 ILE C 839     -87.899  36.306 -27.426  1.00 27.70           C  
-ANISOU 6427  CG1 ILE C 839     3350   3795   3381    227    268    388       C  
-ATOM   6428  CG2 ILE C 839     -88.719  37.602 -29.357  1.00 28.34           C  
-ANISOU 6428  CG2 ILE C 839     3384   3964   3421    314    287    449       C  
-ATOM   6429  CD1 ILE C 839     -86.604  35.864 -28.064  1.00 27.59           C  
-ANISOU 6429  CD1 ILE C 839     3360   3742   3381    192    246    358       C  
-ATOM   6430  N   GLU C 840     -91.677  34.625 -27.757  1.00 29.86           N  
-ANISOU 6430  N   GLU C 840     3437   4321   3588    194    246    417       N  
-ATOM   6431  CA  GLU C 840     -92.150  33.324 -27.288  1.00 29.49           C  
-ANISOU 6431  CA  GLU C 840     3365   4295   3546    124    231    391       C  
-ATOM   6432  C   GLU C 840     -91.977  32.346 -28.412  1.00 28.96           C  
-ANISOU 6432  C   GLU C 840     3272   4262   3471     68    198    360       C  
-ATOM   6433  O   GLU C 840     -92.701  32.390 -29.404  1.00 29.47           O  
-ANISOU 6433  O   GLU C 840     3276   4417   3505     76    186    368       O  
-ATOM   6434  CB  GLU C 840     -93.619  33.359 -26.889  1.00 32.11           C  
-ANISOU 6434  CB  GLU C 840     3633   4710   3855    135    245    415       C  
-ATOM   6435  CG  GLU C 840     -93.957  34.405 -25.828  1.00 35.36           C  
-ANISOU 6435  CG  GLU C 840     4067   5099   4268    200    282    449       C  
-ATOM   6436  CD  GLU C 840     -95.468  34.654 -25.642  1.00 39.37           C  
-ANISOU 6436  CD  GLU C 840     4503   5709   4746    231    299    482       C  
-ATOM   6437  OE1 GLU C 840     -96.318  34.042 -26.343  1.00 42.00           O  
-ANISOU 6437  OE1 GLU C 840     4762   6140   5056    199    281    478       O  
-ATOM   6438  OE2 GLU C 840     -95.799  35.495 -24.776  1.00 43.47           O  
-ANISOU 6438  OE2 GLU C 840     5041   6212   5264    289    332    510       O  
-ATOM   6439  N   ARG C 841     -90.952  31.508 -28.310  1.00 28.84           N  
-ANISOU 6439  N   ARG C 841     3303   4176   3478     19    183    325       N  
-ATOM   6440  CA  ARG C 841     -90.752  30.457 -29.301  1.00 29.25           C  
-ANISOU 6440  CA  ARG C 841     3340   4251   3524    -37    155    290       C  
-ATOM   6441  C   ARG C 841     -91.778  29.346 -29.097  1.00 29.28           C  
-ANISOU 6441  C   ARG C 841     3300   4304   3521   -104    151    270       C  
-ATOM   6442  O   ARG C 841     -91.980  28.876 -27.995  1.00 30.84           O  
-ANISOU 6442  O   ARG C 841     3516   4466   3735   -130    168    268       O  
-ATOM   6443  CB  ARG C 841     -89.338  29.859 -29.205  1.00 27.75           C  
-ANISOU 6443  CB  ARG C 841     3217   3970   3359    -64    145    259       C  
-ATOM   6444  CG  ARG C 841     -88.182  30.803 -29.520  1.00 27.49           C  
-ANISOU 6444  CG  ARG C 841     3224   3887   3333    -15    147    270       C  
-ATOM   6445  CD  ARG C 841     -87.079  30.056 -30.256  1.00 28.60           C  
-ANISOU 6445  CD  ARG C 841     3394   3994   3480    -46    125    237       C  
-ATOM   6446  NE  ARG C 841     -86.747  28.924 -29.496  1.00 30.49           N  
-ANISOU 6446  NE  ARG C 841     3665   4183   3735    -93    123    209       N  
-ATOM   6447  CZ  ARG C 841     -86.878  27.651 -29.826  1.00 30.21           C  
-ANISOU 6447  CZ  ARG C 841     3629   4153   3697   -150    111    178       C  
-ATOM   6448  NH1 ARG C 841     -87.229  27.211 -31.016  1.00 29.70           N  
-ANISOU 6448  NH1 ARG C 841     3530   4142   3612   -176     93    160       N  
-ATOM   6449  NH2 ARG C 841     -86.571  26.791 -28.892  1.00 34.60           N  
-ANISOU 6449  NH2 ARG C 841     4225   4651   4269   -179    120    164       N  
-ATOM   6450  N   GLU C 842     -92.375  28.898 -30.171  1.00 32.24           N  
-ANISOU 6450  N   GLU C 842     3619   4760   3869   -135    130    254       N  
-ATOM   6451  CA  GLU C 842     -93.309  27.793 -30.103  1.00 35.46           C  
-ANISOU 6451  CA  GLU C 842     3985   5217   4272   -212    127    226       C  
-ATOM   6452  C   GLU C 842     -92.681  26.557 -29.504  1.00 32.75           C  
-ANISOU 6452  C   GLU C 842     3702   4784   3959   -279    133    191       C  
-ATOM   6453  O   GLU C 842     -91.563  26.147 -29.877  1.00 32.46           O  
-ANISOU 6453  O   GLU C 842     3719   4681   3934   -288    121    168       O  
-ATOM   6454  CB  GLU C 842     -93.906  27.524 -31.482  1.00 39.38           C  
-ANISOU 6454  CB  GLU C 842     4413   5817   4731   -237    100    205       C  
-ATOM   6455  CG  GLU C 842     -94.972  28.561 -31.801  1.00 46.59           C  
-ANISOU 6455  CG  GLU C 842     5250   6845   5608   -176    102    245       C  
-ATOM   6456  CD  GLU C 842     -95.452  28.520 -33.235  1.00 52.77           C  
-ANISOU 6456  CD  GLU C 842     5964   7741   6346   -180     73    230       C  
-ATOM   6457  OE1 GLU C 842     -95.328  27.449 -33.882  1.00 51.22           O  
-ANISOU 6457  OE1 GLU C 842     5764   7554   6145   -256     51    179       O  
-ATOM   6458  OE2 GLU C 842     -95.940  29.582 -33.686  1.00 56.88           O  
-ANISOU 6458  OE2 GLU C 842     6439   8340   6832   -101     74    272       O  
-ATOM   6459  N   GLY C 843     -93.369  26.012 -28.508  1.00 29.10           N  
-ANISOU 6459  N   GLY C 843     3233   4315   3508   -319    155    192       N  
-ATOM   6460  CA  GLY C 843     -92.933  24.795 -27.860  1.00 29.16           C  
-ANISOU 6460  CA  GLY C 843     3298   4240   3542   -380    169    165       C  
-ATOM   6461  C   GLY C 843     -91.971  24.992 -26.708  1.00 27.98           C  
-ANISOU 6461  C   GLY C 843     3225   3990   3418   -340    186    183       C  
-ATOM   6462  O   GLY C 843     -91.681  24.038 -25.983  1.00 30.13           O  
-ANISOU 6462  O   GLY C 843     3545   4195   3707   -378    204    170       O  
-ATOM   6463  N   GLU C 844     -91.407  26.189 -26.560  1.00 26.30           N  
-ANISOU 6463  N   GLU C 844     3026   3763   3204   -263    183    210       N  
-ATOM   6464  CA  GLU C 844     -90.330  26.357 -25.588  1.00 24.70           C  
-ANISOU 6464  CA  GLU C 844     2894   3470   3021   -229    194    217       C  
-ATOM   6465  C   GLU C 844     -90.843  26.370 -24.164  1.00 25.90           C  
-ANISOU 6465  C   GLU C 844     3056   3604   3180   -222    224    239       C  
-ATOM   6466  O   GLU C 844     -90.169  25.853 -23.274  1.00 24.92           O  
-ANISOU 6466  O   GLU C 844     2989   3410   3069   -225    236    234       O  
-ATOM   6467  CB  GLU C 844     -89.539  27.626 -25.841  1.00 25.00           C  
-ANISOU 6467  CB  GLU C 844     2947   3494   3057   -160    185    233       C  
-ATOM   6468  CG  GLU C 844     -88.082  27.501 -25.425  1.00 24.92           C  
-ANISOU 6468  CG  GLU C 844     3006   3400   3064   -145    181    220       C  
-ATOM   6469  CD  GLU C 844     -87.287  28.764 -25.742  1.00 27.30           C  
-ANISOU 6469  CD  GLU C 844     3319   3688   3365    -88    176    232       C  
-ATOM   6470  OE1 GLU C 844     -87.639  29.816 -25.148  1.00 26.76           O  
-ANISOU 6470  OE1 GLU C 844     3245   3626   3295    -45    192    257       O  
-ATOM   6471  OE2 GLU C 844     -86.295  28.697 -26.529  1.00 25.00           O  
-ANISOU 6471  OE2 GLU C 844     3047   3376   3076    -88    158    215       O  
-ATOM   6472  N   CYS C 845     -92.052  26.907 -23.941  1.00 27.37           N  
-ANISOU 6472  N   CYS C 845     3186   3860   3354   -210    237    264       N  
-ATOM   6473  CA  CYS C 845     -92.675  26.874 -22.597  1.00 29.42           C  
-ANISOU 6473  CA  CYS C 845     3449   4112   3617   -204    268    286       C  
-ATOM   6474  C   CYS C 845     -92.835  25.450 -22.119  1.00 28.63           C  
-ANISOU 6474  C   CYS C 845     3371   3978   3529   -275    285    268       C  
-ATOM   6475  O   CYS C 845     -92.457  25.106 -21.022  1.00 26.83           O  
-ANISOU 6475  O   CYS C 845     3194   3690   3311   -269    306    275       O  
-ATOM   6476  CB  CYS C 845     -94.041  27.604 -22.563  1.00 30.47           C  
-ANISOU 6476  CB  CYS C 845     3508   4338   3731   -181    281    315       C  
-ATOM   6477  SG  CYS C 845     -94.920  27.471 -20.992  1.00 35.68           S  
-ANISOU 6477  SG  CYS C 845     4165   5000   4392   -179    323    343       S  
-ATOM   6478  N   GLN C 846     -93.397  24.627 -22.981  1.00 31.94           N  
-ANISOU 6478  N   GLN C 846     3753   4438   3945   -344    277    244       N  
-ATOM   6479  CA  GLN C 846     -93.631  23.215 -22.676  1.00 33.54           C  
-ANISOU 6479  CA  GLN C 846     3978   4606   4160   -423    299    223       C  
-ATOM   6480  C   GLN C 846     -92.292  22.505 -22.467  1.00 31.86           C  
-ANISOU 6480  C   GLN C 846     3853   4289   3962   -422    298    206       C  
-ATOM   6481  O   GLN C 846     -92.143  21.761 -21.512  1.00 35.47           O  
-ANISOU 6481  O   GLN C 846     4360   4686   4430   -437    328    212       O  
-ATOM   6482  CB  GLN C 846     -94.451  22.541 -23.784  1.00 34.17           C  
-ANISOU 6482  CB  GLN C 846     3998   4753   4231   -501    288    191       C  
-ATOM   6483  CG  GLN C 846     -94.904  21.127 -23.445  1.00 38.58           C  
-ANISOU 6483  CG  GLN C 846     4575   5280   4804   -594    319    168       C  
-ATOM   6484  CD  GLN C 846     -95.914  21.051 -22.271  1.00 42.30           C  
-ANISOU 6484  CD  GLN C 846     5021   5771   5279   -608    360    198       C  
-ATOM   6485  OE1 GLN C 846     -96.751  21.943 -22.083  1.00 44.82           O  
-ANISOU 6485  OE1 GLN C 846     5275   6173   5584   -574    359    226       O  
-ATOM   6486  NE2 GLN C 846     -95.822  19.991 -21.486  1.00 39.63           N  
-ANISOU 6486  NE2 GLN C 846     4740   5358   4959   -654    398    196       N  
-ATOM   6487  N   ARG C 847     -91.310  22.772 -23.311  1.00 28.23           N  
-ANISOU 6487  N   ARG C 847     3414   3811   3501   -397    268    189       N  
-ATOM   6488  CA  ARG C 847     -89.964  22.201 -23.118  1.00 29.16           C  
-ANISOU 6488  CA  ARG C 847     3611   3840   3628   -383    266    176       C  
-ATOM   6489  C   ARG C 847     -89.296  22.673 -21.784  1.00 27.31           C  
-ANISOU 6489  C   ARG C 847     3424   3556   3397   -320    280    203       C  
-ATOM   6490  O   ARG C 847     -88.652  21.889 -21.100  1.00 27.61           O  
-ANISOU 6490  O   ARG C 847     3523   3528   3441   -320    297    201       O  
-ATOM   6491  CB  ARG C 847     -89.070  22.536 -24.310  1.00 29.22           C  
-ANISOU 6491  CB  ARG C 847     3621   3849   3630   -363    231    155       C  
-ATOM   6492  CG  ARG C 847     -87.702  21.887 -24.305  1.00 30.00           C  
-ANISOU 6492  CG  ARG C 847     3792   3870   3735   -352    227    138       C  
-ATOM   6493  CD  ARG C 847     -86.893  22.375 -25.526  1.00 31.19           C  
-ANISOU 6493  CD  ARG C 847     3935   4036   3879   -329    193    122       C  
-ATOM   6494  NE  ARG C 847     -86.369  23.735 -25.345  1.00 30.39           N  
-ANISOU 6494  NE  ARG C 847     3824   3947   3776   -262    181    144       N  
-ATOM   6495  CZ  ARG C 847     -85.506  24.327 -26.176  1.00 34.53           C  
-ANISOU 6495  CZ  ARG C 847     4348   4474   4296   -232    158    137       C  
-ATOM   6496  NH1 ARG C 847     -85.053  23.679 -27.234  1.00 33.73           N  
-ANISOU 6496  NH1 ARG C 847     4256   4369   4190   -256    143    111       N  
-ATOM   6497  NH2 ARG C 847     -85.039  25.558 -25.929  1.00 34.91           N  
-ANISOU 6497  NH2 ARG C 847     4393   4525   4346   -178    154    156       N  
-ATOM   6498  N   TYR C 848     -89.484  23.935 -21.423  1.00 24.41           N  
-ANISOU 6498  N   TYR C 848     3029   3223   3024   -266    276    226       N  
-ATOM   6499  CA  TYR C 848     -88.875  24.484 -20.234  1.00 23.76           C  
-ANISOU 6499  CA  TYR C 848     2985   3102   2940   -209    286    244       C  
-ATOM   6500  C   TYR C 848     -89.555  24.057 -18.942  1.00 25.47           C  
-ANISOU 6500  C   TYR C 848     3214   3309   3155   -215    322    266       C  
-ATOM   6501  O   TYR C 848     -88.956  24.148 -17.881  1.00 23.00           O  
-ANISOU 6501  O   TYR C 848     2945   2957   2838   -175    332    276       O  
-ATOM   6502  CB  TYR C 848     -88.910  26.009 -20.335  1.00 23.04           C  
-ANISOU 6502  CB  TYR C 848     2865   3047   2842   -153    274    258       C  
-ATOM   6503  CG  TYR C 848     -88.248  26.767 -19.246  1.00 22.30           C  
-ANISOU 6503  CG  TYR C 848     2808   2920   2745    -96    280    268       C  
-ATOM   6504  CD1 TYR C 848     -86.876  26.755 -19.119  1.00 22.26           C  
-ANISOU 6504  CD1 TYR C 848     2849   2866   2741    -75    265    251       C  
-ATOM   6505  CD2 TYR C 848     -88.980  27.558 -18.369  1.00 24.46           C  
-ANISOU 6505  CD2 TYR C 848     3066   3217   3011    -62    301    292       C  
-ATOM   6506  CE1 TYR C 848     -86.236  27.489 -18.152  1.00 22.48           C  
-ANISOU 6506  CE1 TYR C 848     2906   2872   2763    -28    268    253       C  
-ATOM   6507  CE2 TYR C 848     -88.348  28.304 -17.365  1.00 24.13           C  
-ANISOU 6507  CE2 TYR C 848     3060   3145   2963    -12    306    294       C  
-ATOM   6508  CZ  TYR C 848     -86.965  28.273 -17.283  1.00 24.08           C  
-ANISOU 6508  CZ  TYR C 848     3097   3093   2958      2    288    272       C  
-ATOM   6509  OH  TYR C 848     -86.283  28.933 -16.282  1.00 24.26           O  
-ANISOU 6509  OH  TYR C 848     3153   3093   2972     45    291    267       O  
-ATOM   6510  N   LYS C 849     -90.809  23.590 -19.044  1.00 29.07           N  
-ANISOU 6510  N   LYS C 849     3626   3806   3612   -266    341    272       N  
-ATOM   6511  CA  LYS C 849     -91.685  23.316 -17.872  1.00 32.46           C  
-ANISOU 6511  CA  LYS C 849     4053   4242   4040   -273    380    298       C  
-ATOM   6512  C   LYS C 849     -91.011  22.535 -16.738  1.00 33.35           C  
-ANISOU 6512  C   LYS C 849     4239   4280   4153   -261    406    306       C  
-ATOM   6513  O   LYS C 849     -91.065  22.989 -15.594  1.00 32.02           O  
-ANISOU 6513  O   LYS C 849     4084   4107   3974   -215    423    330       O  
-ATOM   6514  CB  LYS C 849     -92.999  22.605 -18.256  1.00 35.38           C  
-ANISOU 6514  CB  LYS C 849     4368   4660   4413   -350    399    296       C  
-ATOM   6515  N   PRO C 850     -90.344  21.403 -17.054  1.00 31.80           N  
-ANISOU 6515  N   PRO C 850     4092   4027   3965   -295    409    287       N  
-ATOM   6516  CA  PRO C 850     -89.684  20.679 -15.949  1.00 32.90           C  
-ANISOU 6516  CA  PRO C 850     4304   4099   4099   -270    436    301       C  
-ATOM   6517  C   PRO C 850     -88.655  21.528 -15.196  1.00 31.01           C  
-ANISOU 6517  C   PRO C 850     4093   3847   3843   -187    418    309       C  
-ATOM   6518  O   PRO C 850     -88.468  21.340 -14.006  1.00 30.44           O  
-ANISOU 6518  O   PRO C 850     4057   3750   3757   -151    442    330       O  
-ATOM   6519  CB  PRO C 850     -88.974  19.511 -16.646  1.00 33.71           C  
-ANISOU 6519  CB  PRO C 850     4455   4144   4210   -306    436    277       C  
-ATOM   6520  CG  PRO C 850     -89.631  19.389 -17.982  1.00 31.99           C  
-ANISOU 6520  CG  PRO C 850     4185   3965   4003   -373    420    249       C  
-ATOM   6521  CD  PRO C 850     -90.092  20.768 -18.356  1.00 30.95           C  
-ANISOU 6521  CD  PRO C 850     3983   3912   3867   -345    389    254       C  
-ATOM   6522  N   PHE C 851     -88.040  22.506 -15.864  1.00 32.31           N  
-ANISOU 6522  N   PHE C 851     4237   4033   4007   -157    379    292       N  
-ATOM   6523  CA  PHE C 851     -86.983  23.298 -15.212  1.00 29.83           C  
-ANISOU 6523  CA  PHE C 851     3949   3707   3679    -89    362    291       C  
-ATOM   6524  C   PHE C 851     -87.484  24.488 -14.511  1.00 29.79           C  
-ANISOU 6524  C   PHE C 851     3917   3737   3664    -50    365    305       C  
-ATOM   6525  O   PHE C 851     -86.750  25.075 -13.737  1.00 30.48           O  
-ANISOU 6525  O   PHE C 851     4030   3815   3737      0    359    303       O  
-ATOM   6526  CB  PHE C 851     -85.925  23.653 -16.200  1.00 30.40           C  
-ANISOU 6526  CB  PHE C 851     4023   3773   3755    -79    324    264       C  
-ATOM   6527  CG  PHE C 851     -85.153  22.469 -16.634  1.00 31.21           C  
-ANISOU 6527  CG  PHE C 851     4167   3832   3859    -98    323    250       C  
-ATOM   6528  CD1 PHE C 851     -84.225  21.906 -15.779  1.00 35.46           C  
-ANISOU 6528  CD1 PHE C 851     4759   4332   4382    -60    332    255       C  
-ATOM   6529  CD2 PHE C 851     -85.375  21.896 -17.851  1.00 32.77           C  
-ANISOU 6529  CD2 PHE C 851     4351   4029   4071   -149    315    233       C  
-ATOM   6530  CE1 PHE C 851     -83.500  20.788 -16.154  1.00 36.16           C  
-ANISOU 6530  CE1 PHE C 851     4893   4378   4470    -67    336    245       C  
-ATOM   6531  CE2 PHE C 851     -84.664  20.782 -18.243  1.00 34.42           C  
-ANISOU 6531  CE2 PHE C 851     4605   4192   4280   -163    318    219       C  
-ATOM   6532  CZ  PHE C 851     -83.728  20.228 -17.396  1.00 35.52           C  
-ANISOU 6532  CZ  PHE C 851     4803   4289   4405   -120    330    227       C  
-ATOM   6533  N   LYS C 852     -88.741  24.853 -14.751  1.00 31.01           N  
-ANISOU 6533  N   LYS C 852     4021   3937   3824    -72    377    319       N  
-ATOM   6534  CA  LYS C 852     -89.333  25.952 -14.016  1.00 36.64           C  
-ANISOU 6534  CA  LYS C 852     4712   4684   4526    -30    388    337       C  
-ATOM   6535  C   LYS C 852     -89.349  25.619 -12.525  1.00 39.67           C  
-ANISOU 6535  C   LYS C 852     5133   5047   4892     -2    418    356       C  
-ATOM   6536  O   LYS C 852     -89.448  26.518 -11.727  1.00 45.17           O  
-ANISOU 6536  O   LYS C 852     5831   5757   5574     45    424    364       O  
-ATOM   6537  CB  LYS C 852     -90.706  26.412 -14.594  1.00 38.61           C  
-ANISOU 6537  CB  LYS C 852     4894   4995   4780    -51    397    352       C  
-ATOM   6538  N   GLN C 853     -89.218  24.336 -12.151  1.00 42.74           N  
-ANISOU 6538  N   GLN C 853     5559   5401   5281    -27    439    363       N  
-ATOM   6539  CA  GLN C 853     -89.202  23.942 -10.720  1.00 44.35           C  
-ANISOU 6539  CA  GLN C 853     5802   5585   5464      6    471    386       C  
-ATOM   6540  C   GLN C 853     -87.921  24.236 -10.021  1.00 41.03           C  
-ANISOU 6540  C   GLN C 853     5427   5141   5020     65    453    374       C  
-ATOM   6541  O   GLN C 853     -87.811  24.225  -8.807  1.00 38.21           O  
-ANISOU 6541  O   GLN C 853     5099   4782   4638    108    472    389       O  
-ATOM   6542  CB  GLN C 853     -89.315  22.431 -10.551  1.00 49.31           C  
-ANISOU 6542  CB  GLN C 853     6466   6172   6097    -34    504    400       C  
-ATOM   6543  CG  GLN C 853     -90.658  21.902 -10.942  1.00 54.79           C  
-ANISOU 6543  CG  GLN C 853     7120   6888   6809   -103    533    413       C  
-ATOM   6544  CD  GLN C 853     -91.706  22.720 -10.239  1.00 57.45           C  
-ANISOU 6544  CD  GLN C 853     7414   7278   7135    -81    552    437       C  
-ATOM   6545  OE1 GLN C 853     -92.349  23.577 -10.843  1.00 52.09           O  
-ANISOU 6545  OE1 GLN C 853     6676   6652   6463    -87    536    433       O  
-ATOM   6546  NE2 GLN C 853     -91.790  22.546  -8.918  1.00 59.74           N  
-ANISOU 6546  NE2 GLN C 853     7738   7557   7405    -44    586    464       N  
-ATOM   6547  N   LEU C 854     -86.907  24.359 -10.823  1.00 38.12           N  
-ANISOU 6547  N   LEU C 854     5066   4758   4659     65    418    345       N  
-ATOM   6548  CA  LEU C 854     -85.612  24.585 -10.286  1.00 35.70           C  
-ANISOU 6548  CA  LEU C 854     4795   4438   4330    115    397    328       C  
-ATOM   6549  C   LEU C 854     -85.556  26.004  -9.696  1.00 34.78           C  
-ANISOU 6549  C   LEU C 854     4664   4352   4200    157    386    317       C  
-ATOM   6550  O   LEU C 854     -86.221  26.944 -10.152  1.00 30.72           O  
-ANISOU 6550  O   LEU C 854     4113   3861   3700    148    383    315       O  
-ATOM   6551  CB  LEU C 854     -84.646  24.440 -11.422  1.00 35.12           C  
-ANISOU 6551  CB  LEU C 854     4723   4350   4271     99    364    301       C  
-ATOM   6552  CG  LEU C 854     -83.435  23.592 -11.247  1.00 37.24           C  
-ANISOU 6552  CG  LEU C 854     5036   4590   4523    122    356    294       C  
-ATOM   6553  CD1 LEU C 854     -83.791  22.227 -10.664  1.00 38.15           C  
-ANISOU 6553  CD1 LEU C 854     5193   4673   4631    116    397    323       C  
-ATOM   6554  CD2 LEU C 854     -82.769  23.459 -12.595  1.00 33.90           C  
-ANISOU 6554  CD2 LEU C 854     4604   4157   4120     95    328    269       C  
-ATOM   6555  N   HIS C 855     -84.834  26.138  -8.619  1.00 33.24           N  
-ANISOU 6555  N   HIS C 855     4500   4157   3974    205    384    311       N  
-ATOM   6556  CA AHIS C 855     -84.595  27.429  -7.992  0.50 33.04           C  
-ANISOU 6556  CA AHIS C 855     4470   4153   3930    243    373    290       C  
-ATOM   6557  CA BHIS C 855     -84.650  27.463  -8.039  0.50 36.64           C  
-ANISOU 6557  CA BHIS C 855     4924   4610   4388    241    373    290       C  
-ATOM   6558  C   HIS C 855     -83.530  28.172  -8.807  1.00 36.03           C  
-ANISOU 6558  C   HIS C 855     4840   4529   4320    238    334    250       C  
-ATOM   6559  O   HIS C 855     -82.956  27.608  -9.759  1.00 35.47           O  
-ANISOU 6559  O   HIS C 855     4767   4444   4266    212    316    242       O  
-ATOM   6560  CB AHIS C 855     -84.134  27.220  -6.538  0.50 32.22           C  
-ANISOU 6560  CB AHIS C 855     4402   4058   3783    295    383    293       C  
-ATOM   6561  CB BHIS C 855     -84.431  27.376  -6.538  0.50 40.58           C  
-ANISOU 6561  CB BHIS C 855     5454   5119   4844    292    388    296       C  
-ATOM   6562  CG AHIS C 855     -82.873  26.415  -6.407  0.50 29.34           C  
-ANISOU 6562  CG AHIS C 855     4066   3684   3397    314    365    282       C  
-ATOM   6563  CG BHIS C 855     -85.580  26.720  -5.827  0.50 44.27           C  
-ANISOU 6563  CG BHIS C 855     5926   5589   5304    293    431    340       C  
-ATOM   6564  ND1AHIS C 855     -82.786  25.094  -6.789  0.50 28.82           N  
-ANISOU 6564  ND1AHIS C 855     4020   3591   3339    297    377    304       N  
-ATOM   6565  ND1BHIS C 855     -86.865  26.735  -6.340  0.50 44.17           N  
-ANISOU 6565  ND1BHIS C 855     5880   5583   5319    256    454    363       N  
-ATOM   6566  CD2AHIS C 855     -81.648  26.748  -5.944  0.50 27.91           C  
-ANISOU 6566  CD2AHIS C 855     3896   3521   3185    350    337    250       C  
-ATOM   6567  CD2BHIS C 855     -85.647  26.040  -4.657  0.50 43.91           C  
-ANISOU 6567  CD2BHIS C 855     5913   5544   5225    327    459    365       C  
-ATOM   6568  CE1AHIS C 855     -81.568  24.648  -6.569  0.50 27.42           C  
-ANISOU 6568  CE1AHIS C 855     3868   3416   3136    330    359    292       C  
-ATOM   6569  CE1BHIS C 855     -87.667  26.081  -5.521  0.50 45.74           C  
-ANISOU 6569  CE1BHIS C 855     6088   5785   5504    261    494    400       C  
-ATOM   6570  NE2AHIS C 855     -80.857  25.635  -6.059  0.50 26.69           N  
-ANISOU 6570  NE2AHIS C 855     3765   3356   3019    361    333    258       N  
-ATOM   6571  NE2BHIS C 855     -86.955  25.658  -4.488  0.50 45.62           N  
-ANISOU 6571  NE2BHIS C 855     6117   5764   5454    306    499    403       N  
-ATOM   6572  N   ASN C 856     -83.255  29.412  -8.434  1.00 36.07           N  
-ANISOU 6572  N   ASN C 856     4843   4547   4316    260    325    224       N  
-ATOM   6573  CA  ASN C 856     -82.154  30.177  -9.014  1.00 32.34           C  
-ANISOU 6573  CA  ASN C 856     4367   4071   3851    254    294    184       C  
-ATOM   6574  C   ASN C 856     -82.293  30.330 -10.545  1.00 32.07           C  
-ANISOU 6574  C   ASN C 856     4306   4025   3854    215    284    185       C  
-ATOM   6575  O   ASN C 856     -81.420  29.941 -11.335  1.00 29.68           O  
-ANISOU 6575  O   ASN C 856     4002   3715   3562    197    261    170       O  
-ATOM   6576  CB  ASN C 856     -80.840  29.529  -8.606  1.00 33.00           C  
-ANISOU 6576  CB  ASN C 856     4470   4160   3908    272    272    164       C  
-ATOM   6577  CG  ASN C 856     -79.661  30.379  -8.936  1.00 36.07           C  
-ANISOU 6577  CG  ASN C 856     4851   4556   4297    267    243    117       C  
-ATOM   6578  OD1 ASN C 856     -79.789  31.566  -9.151  1.00 39.94           O  
-ANISOU 6578  OD1 ASN C 856     5333   5042   4801    257    244     97       O  
-ATOM   6579  ND2 ASN C 856     -78.495  29.760  -9.035  1.00 40.38           N  
-ANISOU 6579  ND2 ASN C 856     5401   5113   4828    273    220    102       N  
-ATOM   6580  N   ARG C 857     -83.436  30.870 -10.934  1.00 28.21           N  
-ANISOU 6580  N   ARG C 857     3795   3540   3383    207    302    205       N  
-ATOM   6581  CA  ARG C 857     -83.724  31.175 -12.290  1.00 27.31           C  
-ANISOU 6581  CA  ARG C 857     3652   3425   3297    179    295    210       C  
-ATOM   6582  C   ARG C 857     -83.355  32.612 -12.549  1.00 28.30           C  
-ANISOU 6582  C   ARG C 857     3779   3544   3430    191    292    187       C  
-ATOM   6583  O   ARG C 857     -83.747  33.506 -11.809  1.00 27.42           O  
-ANISOU 6583  O   ARG C 857     3679   3433   3308    218    311    185       O  
-ATOM   6584  CB  ARG C 857     -85.187  30.920 -12.552  1.00 29.72           C  
-ANISOU 6584  CB  ARG C 857     3930   3751   3612    167    318    246       C  
-ATOM   6585  CG  ARG C 857     -85.419  29.448 -12.749  1.00 31.55           C  
-ANISOU 6585  CG  ARG C 857     4160   3981   3847    135    320    262       C  
-ATOM   6586  CD  ARG C 857     -86.812  28.925 -12.544  1.00 35.35           C  
-ANISOU 6586  CD  ARG C 857     4618   4485   4330    119    349    295       C  
-ATOM   6587  NE  ARG C 857     -87.872  29.898 -12.511  1.00 37.47           N  
-ANISOU 6587  NE  ARG C 857     4855   4785   4597    137    366    312       N  
-ATOM   6588  CZ  ARG C 857     -88.618  30.186 -11.454  1.00 45.29           C  
-ANISOU 6588  CZ  ARG C 857     5847   5791   5572    165    394    331       C  
-ATOM   6589  NH1 ARG C 857     -88.406  29.597 -10.272  1.00 45.86           N  
-ANISOU 6589  NH1 ARG C 857     5951   5849   5624    180    408    336       N  
-ATOM   6590  NH2 ARG C 857     -89.596  31.088 -11.596  1.00 49.83           N  
-ANISOU 6590  NH2 ARG C 857     6388   6398   6145    185    410    348       N  
-ATOM   6591  N   ARG C 858     -82.550  32.835 -13.586  1.00 27.90           N  
-ANISOU 6591  N   ARG C 858     3721   3482   3396    172    272    169       N  
-ATOM   6592  CA  ARG C 858     -81.944  34.143 -13.808  1.00 26.67           C  
-ANISOU 6592  CA  ARG C 858     3574   3310   3247    177    272    143       C  
-ATOM   6593  C   ARG C 858     -82.128  34.620 -15.226  1.00 24.61           C  
-ANISOU 6593  C   ARG C 858     3294   3046   3012    163    272    154       C  
-ATOM   6594  O   ARG C 858     -81.979  33.826 -16.169  1.00 22.40           O  
-ANISOU 6594  O   ARG C 858     2995   2774   2742    139    255    162       O  
-ATOM   6595  CB  ARG C 858     -80.479  34.144 -13.532  1.00 28.00           C  
-ANISOU 6595  CB  ARG C 858     3759   3472   3408    170    249    102       C  
-ATOM   6596  CG  ARG C 858     -80.083  34.922 -12.334  1.00 31.94           C  
-ANISOU 6596  CG  ARG C 858     4282   3968   3886    189    256     70       C  
-ATOM   6597  CD  ARG C 858     -78.591  35.004 -12.040  1.00 33.52           C  
-ANISOU 6597  CD  ARG C 858     4488   4174   4073    178    231     23       C  
-ATOM   6598  NE  ARG C 858     -78.530  34.275 -10.786  1.00 35.58           N  
-ANISOU 6598  NE  ARG C 858     4761   4459   4298    204    226     21       N  
-ATOM   6599  CZ  ARG C 858     -77.483  34.192  -9.983  1.00 39.48           C  
-ANISOU 6599  CZ  ARG C 858     5262   4977   4762    212    207    -15       C  
-ATOM   6600  NH1 ARG C 858     -76.354  34.826 -10.275  1.00 40.72           N  
-ANISOU 6600  NH1 ARG C 858     5411   5138   4923    189    190    -60       N  
-ATOM   6601  NH2 ARG C 858     -77.582  33.454  -8.888  1.00 38.82           N  
-ANISOU 6601  NH2 ARG C 858     5189   4918   4642    245    206     -7       N  
-ATOM   6602  N   LEU C 859     -82.372  35.930 -15.351  1.00 21.42           N  
-ANISOU 6602  N   LEU C 859     2897   2627   2615    179    293    153       N  
-ATOM   6603  CA  LEU C 859     -82.449  36.608 -16.634  1.00 20.02           C  
-ANISOU 6603  CA  LEU C 859     2707   2443   2457    176    300    165       C  
-ATOM   6604  C   LEU C 859     -81.070  37.104 -17.066  1.00 19.47           C  
-ANISOU 6604  C   LEU C 859     2652   2346   2398    155    288    130       C  
-ATOM   6605  O   LEU C 859     -80.495  38.011 -16.473  1.00 19.56           O  
-ANISOU 6605  O   LEU C 859     2691   2331   2409    157    300    101       O  
-ATOM   6606  CB  LEU C 859     -83.453  37.754 -16.575  1.00 19.95           C  
-ANISOU 6606  CB  LEU C 859     2704   2429   2447    212    336    189       C  
-ATOM   6607  CG  LEU C 859     -83.927  38.230 -17.938  1.00 19.79           C  
-ANISOU 6607  CG  LEU C 859     2663   2418   2440    221    346    219       C  
-ATOM   6608  CD1 LEU C 859     -84.920  37.269 -18.532  1.00 20.29           C  
-ANISOU 6608  CD1 LEU C 859     2680   2533   2498    216    334    252       C  
-ATOM   6609  CD2 LEU C 859     -84.575  39.617 -17.808  1.00 21.58           C  
-ANISOU 6609  CD2 LEU C 859     2910   2625   2664    266    388    236       C  
-ATOM   6610  N   LEU C 860     -80.545  36.474 -18.109  1.00 19.40           N  
-ANISOU 6610  N   LEU C 860     2624   2347   2400    132    266    132       N  
-ATOM   6611  CA  LEU C 860     -79.133  36.596 -18.489  1.00 20.39           C  
-ANISOU 6611  CA  LEU C 860     2756   2458   2533    107    250     99       C  
-ATOM   6612  C   LEU C 860     -78.997  36.877 -19.983  1.00 19.77           C  
-ANISOU 6612  C   LEU C 860     2662   2377   2471     98    252    114       C  
-ATOM   6613  O   LEU C 860     -79.889  36.557 -20.760  1.00 18.93           O  
-ANISOU 6613  O   LEU C 860     2534   2292   2366    106    253    148       O  
-ATOM   6614  CB  LEU C 860     -78.368  35.326 -18.155  1.00 19.96           C  
-ANISOU 6614  CB  LEU C 860     2695   2422   2465     94    219     82       C  
-ATOM   6615  CG  LEU C 860     -78.289  34.970 -16.674  1.00 22.81           C  
-ANISOU 6615  CG  LEU C 860     3074   2791   2804    107    215     66       C  
-ATOM   6616  CD1 LEU C 860     -77.694  33.568 -16.498  1.00 23.72           C  
-ANISOU 6616  CD1 LEU C 860     3185   2924   2904    104    190     62       C  
-ATOM   6617  CD2 LEU C 860     -77.463  35.995 -15.890  1.00 22.61           C  
-ANISOU 6617  CD2 LEU C 860     3067   2753   2772    105    220     24       C  
-ATOM   6618  N   TRP C 861     -77.863  37.476 -20.353  1.00 19.27           N  
-ANISOU 6618  N   TRP C 861     2608   2295   2420     79    252     89       N  
-ATOM   6619  CA  TRP C 861     -77.610  37.875 -21.722  1.00 18.40           C  
-ANISOU 6619  CA  TRP C 861     2488   2180   2325     73    259    103       C  
-ATOM   6620  C   TRP C 861     -77.007  36.758 -22.545  1.00 18.54           C  
-ANISOU 6620  C   TRP C 861     2481   2223   2340     55    227    101       C  
-ATOM   6621  O   TRP C 861     -76.253  35.902 -22.047  1.00 17.82           O  
-ANISOU 6621  O   TRP C 861     2388   2144   2239     42    202     77       O  
-ATOM   6622  CB  TRP C 861     -76.619  39.026 -21.748  1.00 19.43           C  
-ANISOU 6622  CB  TRP C 861     2639   2274   2469     55    279     75       C  
-ATOM   6623  CG  TRP C 861     -77.047  40.244 -21.012  1.00 19.16           C  
-ANISOU 6623  CG  TRP C 861     2639   2202   2439     69    317     70       C  
-ATOM   6624  CD1 TRP C 861     -76.574  40.681 -19.813  1.00 19.31           C  
-ANISOU 6624  CD1 TRP C 861     2681   2204   2452     56    322     28       C  
-ATOM   6625  CD2 TRP C 861     -78.002  41.204 -21.434  1.00 19.28           C  
-ANISOU 6625  CD2 TRP C 861     2671   2194   2460    101    357    105       C  
-ATOM   6626  NE1 TRP C 861     -77.222  41.819 -19.433  1.00 19.00           N  
-ANISOU 6626  NE1 TRP C 861     2676   2126   2418     76    363     34       N  
-ATOM   6627  CE2 TRP C 861     -78.086  42.183 -20.429  1.00 20.55           C  
-ANISOU 6627  CE2 TRP C 861     2871   2316   2622    107    387     83       C  
-ATOM   6628  CE3 TRP C 861     -78.774  41.350 -22.559  1.00 20.30           C  
-ANISOU 6628  CE3 TRP C 861     2787   2335   2592    129    370    153       C  
-ATOM   6629  CZ2 TRP C 861     -78.929  43.310 -20.536  1.00 20.84           C  
-ANISOU 6629  CZ2 TRP C 861     2939   2317   2664    144    436    111       C  
-ATOM   6630  CZ3 TRP C 861     -79.628  42.453 -22.653  1.00 20.80           C  
-ANISOU 6630  CZ3 TRP C 861     2875   2372   2656    169    416    184       C  
-ATOM   6631  CH2 TRP C 861     -79.688  43.408 -21.660  1.00 21.18           C  
-ANISOU 6631  CH2 TRP C 861     2966   2374   2707    178    450    164       C  
-ATOM   6632  N   HIS C 862     -77.350  36.750 -23.824  1.00 19.22           N  
-ANISOU 6632  N   HIS C 862     2551   2320   2431     59    230    128       N  
-ATOM   6633  CA  HIS C 862     -76.620  35.932 -24.797  1.00 18.98           C  
-ANISOU 6633  CA  HIS C 862     2503   2309   2399     43    206    123       C  
-ATOM   6634  C   HIS C 862     -76.536  36.680 -26.104  1.00 18.35           C  
-ANISOU 6634  C   HIS C 862     2417   2227   2329     48    223    144       C  
-ATOM   6635  O   HIS C 862     -77.556  36.976 -26.729  1.00 17.45           O  
-ANISOU 6635  O   HIS C 862     2294   2127   2211     70    236    177       O  
-ATOM   6636  CB  HIS C 862     -77.287  34.587 -25.042  1.00 18.84           C  
-ANISOU 6636  CB  HIS C 862     2468   2321   2369     42    183    135       C  
-ATOM   6637  CG  HIS C 862     -76.533  33.710 -25.998  1.00 20.10           C  
-ANISOU 6637  CG  HIS C 862     2616   2496   2524     28    160    127       C  
-ATOM   6638  ND1 HIS C 862     -75.564  32.813 -25.588  1.00 21.39           N  
-ANISOU 6638  ND1 HIS C 862     2787   2658   2680     18    140    101       N  
-ATOM   6639  CD2 HIS C 862     -76.612  33.581 -27.338  1.00 20.96           C  
-ANISOU 6639  CD2 HIS C 862     2708   2623   2631     27    156    140       C  
-ATOM   6640  CE1 HIS C 862     -75.091  32.163 -26.635  1.00 21.19           C  
-ANISOU 6640  CE1 HIS C 862     2753   2647   2652     12    126    100       C  
-ATOM   6641  NE2 HIS C 862     -75.682  32.638 -27.713  1.00 21.79           N  
-ANISOU 6641  NE2 HIS C 862     2814   2735   2731     15    135    121       N  
-ATOM   6642  N   GLY C 863     -75.314  36.983 -26.507  1.00 19.00           N  
-ANISOU 6642  N   GLY C 863     2502   2297   2419     30    224    124       N  
-ATOM   6643  CA  GLY C 863     -75.069  37.683 -27.780  1.00 20.67           C  
-ANISOU 6643  CA  GLY C 863     2710   2504   2639     34    244    145       C  
-ATOM   6644  C   GLY C 863     -74.590  36.735 -28.859  1.00 20.80           C  
-ANISOU 6644  C   GLY C 863     2705   2553   2647     28    218    146       C  
-ATOM   6645  O   GLY C 863     -73.980  35.706 -28.561  1.00 20.62           O  
-ANISOU 6645  O   GLY C 863     2674   2544   2616     13    190    122       O  
-ATOM   6646  N   SER C 864     -74.903  37.072 -30.097  1.00 21.30           N  
-ANISOU 6646  N   SER C 864     2758   2629   2706     44    231    176       N  
-ATOM   6647  CA  SER C 864     -74.548  36.258 -31.237  1.00 22.90           C  
-ANISOU 6647  CA  SER C 864     2941   2864   2896     42    210    179       C  
-ATOM   6648  C   SER C 864     -74.596  37.149 -32.488  1.00 22.94           C  
-ANISOU 6648  C   SER C 864     2944   2872   2900     62    238    212       C  
-ATOM   6649  O   SER C 864     -75.207  38.193 -32.468  1.00 22.43           O  
-ANISOU 6649  O   SER C 864     2892   2789   2841     84    271    238       O  
-ATOM   6650  CB  SER C 864     -75.533  35.105 -31.372  1.00 22.78           C  
-ANISOU 6650  CB  SER C 864     2909   2884   2861     47    182    183       C  
-ATOM   6651  OG  SER C 864     -75.022  34.106 -32.238  1.00 24.46           O  
-ANISOU 6651  OG  SER C 864     3110   3122   3061     38    158    172       O  
-ATOM   6652  N   ARG C 865     -73.946  36.719 -33.556  1.00 23.97           N  
-ANISOU 6652  N   ARG C 865     3062   3026   3022     60    228    212       N  
-ATOM   6653  CA  ARG C 865     -73.978  37.427 -34.822  1.00 27.02           C  
-ANISOU 6653  CA  ARG C 865     3445   3422   3401     83    253    246       C  
-ATOM   6654  C   ARG C 865     -75.394  37.467 -35.350  1.00 26.02           C  
-ANISOU 6654  C   ARG C 865     3304   3331   3251    120    254    280       C  
-ATOM   6655  O   ARG C 865     -76.155  36.508 -35.203  1.00 24.98           O  
-ANISOU 6655  O   ARG C 865     3154   3235   3104    116    222    271       O  
-ATOM   6656  CB  ARG C 865     -73.077  36.760 -35.868  1.00 28.86           C  
-ANISOU 6656  CB  ARG C 865     3662   3682   3621     77    237    237       C  
-ATOM   6657  CG  ARG C 865     -71.595  36.881 -35.604  1.00 32.14           C  
-ANISOU 6657  CG  ARG C 865     4082   4074   4054     47    243    210       C  
-ATOM   6658  CD  ARG C 865     -70.820  35.899 -36.486  1.00 35.58           C  
-ANISOU 6658  CD  ARG C 865     4501   4547   4473     45    219    198       C  
-ATOM   6659  NE  ARG C 865     -69.442  35.744 -36.001  1.00 39.16           N  
-ANISOU 6659  NE  ARG C 865     4950   4990   4938     18    216    166       N  
-ATOM   6660  CZ  ARG C 865     -68.424  36.498 -36.389  1.00 42.41           C  
-ANISOU 6660  CZ  ARG C 865     5358   5393   5362      5    244    168       C  
-ATOM   6661  NH1 ARG C 865     -67.222  36.286 -35.884  1.00 47.10           N  
-ANISOU 6661  NH1 ARG C 865     5940   5992   5963    -21    237    136       N  
-ATOM   6662  NH2 ARG C 865     -68.596  37.472 -37.276  1.00 46.01           N  
-ANISOU 6662  NH2 ARG C 865     5821   5838   5822     17    282    204       N  
-ATOM   6663  N   THR C 866     -75.723  38.583 -35.976  1.00 26.83           N  
-ANISOU 6663  N   THR C 866     3415   3428   3350    154    292    320       N  
-ATOM   6664  CA  THR C 866     -77.046  38.815 -36.541  1.00 27.42           C  
-ANISOU 6664  CA  THR C 866     3474   3547   3398    200    298    360       C  
-ATOM   6665  C   THR C 866     -77.486  37.732 -37.498  1.00 26.35           C  
-ANISOU 6665  C   THR C 866     3300   3482   3228    203    259    356       C  
-ATOM   6666  O   THR C 866     -78.661  37.304 -37.466  1.00 25.86           O  
-ANISOU 6666  O   THR C 866     3212   3469   3145    216    240    363       O  
-ATOM   6667  CB  THR C 866     -77.084  40.200 -37.202  1.00 28.02           C  
-ANISOU 6667  CB  THR C 866     3572   3602   3474    243    352    407       C  
-ATOM   6668  OG1 THR C 866     -76.702  41.170 -36.210  1.00 26.96           O  
-ANISOU 6668  OG1 THR C 866     3477   3393   3373    231    390    402       O  
-ATOM   6669  CG2 THR C 866     -78.484  40.551 -37.668  1.00 27.43           C  
-ANISOU 6669  CG2 THR C 866     3478   3577   3366    302    362    453       C  
-ATOM   6670  N   THR C 867     -76.542  37.221 -38.283  1.00 26.21           N  
-ANISOU 6670  N   THR C 867     3279   3474   3205    188    246    341       N  
-ATOM   6671  CA  THR C 867     -76.825  36.142 -39.243  1.00 25.21           C  
-ANISOU 6671  CA  THR C 867     3122   3411   3045    187    209    330       C  
-ATOM   6672  C   THR C 867     -77.186  34.805 -38.595  1.00 25.27           C  
-ANISOU 6672  C   THR C 867     3118   3431   3051    149    168    289       C  
-ATOM   6673  O   THR C 867     -77.552  33.853 -39.300  1.00 24.66           O  
-ANISOU 6673  O   THR C 867     3020   3403   2946    141    139    273       O  
-ATOM   6674  CB  THR C 867     -75.646  35.940 -40.230  1.00 25.19           C  
-ANISOU 6674  CB  THR C 867     3123   3412   3036    184    210    324       C  
-ATOM   6675  OG1 THR C 867     -74.410  35.833 -39.528  1.00 23.23           O  
-ANISOU 6675  OG1 THR C 867     2895   3111   2819    150    212    295       O  
-ATOM   6676  CG2 THR C 867     -75.563  37.141 -41.189  1.00 26.34           C  
-ANISOU 6676  CG2 THR C 867     3274   3562   3171    229    252    373       C  
-ATOM   6677  N   ASN C 868     -77.065  34.711 -37.267  1.00 23.91           N  
-ANISOU 6677  N   ASN C 868     2964   3213   2907    125    167    270       N  
-ATOM   6678  CA  ASN C 868     -77.465  33.516 -36.571  1.00 24.22           C  
-ANISOU 6678  CA  ASN C 868     2999   3258   2946     93    137    238       C  
-ATOM   6679  C   ASN C 868     -78.897  33.553 -36.076  1.00 24.90           C  
-ANISOU 6679  C   ASN C 868     3066   3371   3024     98    136    251       C  
-ATOM   6680  O   ASN C 868     -79.420  32.527 -35.701  1.00 25.63           O  
-ANISOU 6680  O   ASN C 868     3149   3477   3111     70    113    228       O  
-ATOM   6681  CB  ASN C 868     -76.576  33.257 -35.358  1.00 23.52           C  
-ANISOU 6681  CB  ASN C 868     2937   3114   2884     67    136    210       C  
-ATOM   6682  CG  ASN C 868     -75.131  32.920 -35.695  1.00 22.89           C  
-ANISOU 6682  CG  ASN C 868     2870   3017   2809     57    130    190       C  
-ATOM   6683  OD1 ASN C 868     -74.248  33.303 -34.963  1.00 26.06           O  
-ANISOU 6683  OD1 ASN C 868     3287   3383   3232     48    141    179       O  
-ATOM   6684  ND2 ASN C 868     -74.893  32.231 -36.743  1.00 23.16           N  
-ANISOU 6684  ND2 ASN C 868     2895   3081   2823     57    115    182       N  
-ATOM   6685  N   PHE C 869     -79.541  34.710 -36.079  1.00 27.02           N  
-ANISOU 6685  N   PHE C 869     3329   3648   3291    136    163    288       N  
-ATOM   6686  CA  PHE C 869     -80.801  34.858 -35.344  1.00 28.93           C  
-ANISOU 6686  CA  PHE C 869     3555   3909   3529    145    167    302       C  
-ATOM   6687  C   PHE C 869     -82.049  34.195 -35.916  1.00 31.01           C  
-ANISOU 6687  C   PHE C 869     3771   4252   3758    143    145    304       C  
-ATOM   6688  O   PHE C 869     -82.975  33.869 -35.180  1.00 30.79           O  
-ANISOU 6688  O   PHE C 869     3727   4242   3730    131    140    301       O  
-ATOM   6689  CB  PHE C 869     -81.067  36.305 -35.015  1.00 28.62           C  
-ANISOU 6689  CB  PHE C 869     3531   3845   3497    189    208    340       C  
-ATOM   6690  CG  PHE C 869     -80.470  36.701 -33.701  1.00 28.85           C  
-ANISOU 6690  CG  PHE C 869     3598   3802   3560    174    224    325       C  
-ATOM   6691  CD1 PHE C 869     -79.157  37.073 -33.626  1.00 29.58           C  
-ANISOU 6691  CD1 PHE C 869     3723   3842   3675    159    236    310       C  
-ATOM   6692  CD2 PHE C 869     -81.208  36.612 -32.538  1.00 27.54           C  
-ANISOU 6692  CD2 PHE C 869     3433   3630   3400    170    226    321       C  
-ATOM   6693  CE1 PHE C 869     -78.589  37.436 -32.422  1.00 29.71           C  
-ANISOU 6693  CE1 PHE C 869     3769   3801   3717    141    249    289       C  
-ATOM   6694  CE2 PHE C 869     -80.644  36.932 -31.336  1.00 28.15           C  
-ANISOU 6694  CE2 PHE C 869     3545   3648   3503    156    238    302       C  
-ATOM   6695  CZ  PHE C 869     -79.323  37.354 -31.277  1.00 29.16           C  
-ANISOU 6695  CZ  PHE C 869     3703   3725   3651    141    248    285       C  
-ATOM   6696  N   ALA C 870     -82.062  33.937 -37.211  1.00 32.45           N  
-ANISOU 6696  N   ALA C 870     3931   4488   3912    151    131    305       N  
-ATOM   6697  CA  ALA C 870     -83.141  33.159 -37.773  1.00 30.63           C  
-ANISOU 6697  CA  ALA C 870     3653   4338   3648    137    104    294       C  
-ATOM   6698  C   ALA C 870     -83.059  31.761 -37.250  1.00 28.87           C  
-ANISOU 6698  C   ALA C 870     3436   4096   3435     73     78    246       C  
-ATOM   6699  O   ALA C 870     -84.062  31.160 -36.918  1.00 31.61           O  
-ANISOU 6699  O   ALA C 870     3755   4481   3775     46     67    234       O  
-ATOM   6700  CB  ALA C 870     -83.072  33.142 -39.293  1.00 34.07           C  
-ANISOU 6700  CB  ALA C 870     4064   4836   4044    159     93    300       C  
-ATOM   6701  N   GLY C 871     -81.856  31.214 -37.207  1.00 27.27           N  
-ANISOU 6701  N   GLY C 871     3272   3839   3252     50     72    219       N  
-ATOM   6702  CA  GLY C 871     -81.646  29.891 -36.659  1.00 24.29           C  
-ANISOU 6702  CA  GLY C 871     2914   3431   2886     -2     55    177       C  
-ATOM   6703  C   GLY C 871     -81.979  29.852 -35.184  1.00 23.63           C  
-ANISOU 6703  C   GLY C 871     2845   3307   2828    -16     66    178       C  
-ATOM   6704  O   GLY C 871     -82.687  28.949 -34.738  1.00 24.43           O  
-ANISOU 6704  O   GLY C 871     2938   3417   2928    -55     58    159       O  
-ATOM   6705  N   ILE C 872     -81.498  30.846 -34.425  1.00 22.42           N  
-ANISOU 6705  N   ILE C 872     2713   3109   2696     13     88    200       N  
-ATOM   6706  CA  ILE C 872     -81.793  30.904 -32.996  1.00 21.74           C  
-ANISOU 6706  CA  ILE C 872     2642   2987   2630      6     99    202       C  
-ATOM   6707  C   ILE C 872     -83.289  31.038 -32.710  1.00 23.35           C  
-ANISOU 6707  C   ILE C 872     2809   3240   2823      8    105    220       C  
-ATOM   6708  O   ILE C 872     -83.836  30.329 -31.869  1.00 22.39           O  
-ANISOU 6708  O   ILE C 872     2687   3113   2708    -22    103    208       O  
-ATOM   6709  CB  ILE C 872     -81.067  32.037 -32.324  1.00 21.26           C  
-ANISOU 6709  CB  ILE C 872     2609   2878   2591     35    122    218       C  
-ATOM   6710  CG1 ILE C 872     -79.568  31.734 -32.319  1.00 19.97           C  
-ANISOU 6710  CG1 ILE C 872     2477   2669   2440     24    116    194       C  
-ATOM   6711  CG2 ILE C 872     -81.573  32.266 -30.896  1.00 20.80           C  
-ANISOU 6711  CG2 ILE C 872     2562   2794   2546     37    136    223       C  
-ATOM   6712  CD1 ILE C 872     -78.748  32.951 -32.011  1.00 20.14           C  
-ANISOU 6712  CD1 ILE C 872     2520   2654   2480     47    138    205       C  
-ATOM   6713  N   LEU C 873     -83.983  31.894 -33.436  1.00 26.16           N  
-ANISOU 6713  N   LEU C 873     3130   3650   3158     45    112    250       N  
-ATOM   6714  CA  LEU C 873     -85.425  31.996 -33.220  1.00 27.42           C  
-ANISOU 6714  CA  LEU C 873     3246   3871   3301     51    116    268       C  
-ATOM   6715  C   LEU C 873     -86.181  30.747 -33.639  1.00 26.31           C  
-ANISOU 6715  C   LEU C 873     3068   3786   3142     -1     92    239       C  
-ATOM   6716  O   LEU C 873     -87.044  30.268 -32.925  1.00 26.14           O  
-ANISOU 6716  O   LEU C 873     3029   3782   3123    -29     94    234       O  
-ATOM   6717  CB  LEU C 873     -86.003  33.241 -33.883  1.00 26.91           C  
-ANISOU 6717  CB  LEU C 873     3154   3856   3214    114    134    312       C  
-ATOM   6718  CG  LEU C 873     -85.474  34.519 -33.266  1.00 27.32           C  
-ANISOU 6718  CG  LEU C 873     3247   3846   3287    160    168    340       C  
-ATOM   6719  CD1 LEU C 873     -86.120  35.704 -33.968  1.00 28.89           C  
-ANISOU 6719  CD1 LEU C 873     3424   4091   3460    229    192    388       C  
-ATOM   6720  CD2 LEU C 873     -85.743  34.603 -31.773  1.00 27.52           C  
-ANISOU 6720  CD2 LEU C 873     3293   3829   3335    153    183    338       C  
-ATOM   6721  N   SER C 874     -85.840  30.178 -34.768  1.00 26.92           N  
-ANISOU 6721  N   SER C 874     3138   3889   3202    -19     70    217       N  
-ATOM   6722  CA  SER C 874     -86.517  28.987 -35.219  1.00 25.70           C  
-ANISOU 6722  CA  SER C 874     2951   3783   3028    -76     48    182       C  
-ATOM   6723  C   SER C 874     -86.176  27.739 -34.383  1.00 26.47           C  
-ANISOU 6723  C   SER C 874     3090   3817   3152   -136     47    145       C  
-ATOM   6724  O   SER C 874     -87.017  26.890 -34.174  1.00 27.43           O  
-ANISOU 6724  O   SER C 874     3190   3964   3269   -187     44    123       O  
-ATOM   6725  CB  SER C 874     -86.098  28.803 -36.675  1.00 26.53           C  
-ANISOU 6725  CB  SER C 874     3046   3927   3105    -72     28    166       C  
-ATOM   6726  OG  SER C 874     -85.684  27.521 -37.039  1.00 31.21           O  
-ANISOU 6726  OG  SER C 874     3660   4502   3698   -128     11    118       O  
-ATOM   6727  N   GLN C 875     -84.934  27.601 -33.936  1.00 26.59           N  
-ANISOU 6727  N   GLN C 875     3163   3749   3191   -130     53    137       N  
-ATOM   6728  CA  GLN C 875     -84.513  26.366 -33.286  1.00 27.62           C  
-ANISOU 6728  CA  GLN C 875     3336   3820   3340   -177     53    105       C  
-ATOM   6729  C   GLN C 875     -84.070  26.534 -31.830  1.00 25.74           C  
-ANISOU 6729  C   GLN C 875     3137   3513   3128   -163     72    119       C  
-ATOM   6730  O   GLN C 875     -83.776  25.549 -31.182  1.00 24.69           O  
-ANISOU 6730  O   GLN C 875     3042   3333   3007   -192     77     99       O  
-ATOM   6731  CB  GLN C 875     -83.353  25.714 -34.052  1.00 30.26           C  
-ANISOU 6731  CB  GLN C 875     3706   4121   3670   -183     41     77       C  
-ATOM   6732  CG  GLN C 875     -83.602  25.438 -35.517  1.00 37.16           C  
-ANISOU 6732  CG  GLN C 875     4550   5056   4513   -197     21     57       C  
-ATOM   6733  CD  GLN C 875     -82.591  24.470 -36.143  1.00 44.53           C  
-ANISOU 6733  CD  GLN C 875     5525   5951   5442   -214     12     21       C  
-ATOM   6734  OE1 GLN C 875     -81.533  24.200 -35.580  1.00 47.39           O  
-ANISOU 6734  OE1 GLN C 875     5937   6247   5824   -202     20     19       O  
-ATOM   6735  NE2 GLN C 875     -82.881  24.023 -37.354  1.00 48.70           N  
-ANISOU 6735  NE2 GLN C 875     6032   6532   5941   -235     -5     -5       N  
-ATOM   6736  N   GLY C 876     -83.965  27.767 -31.349  1.00 24.99           N  
-ANISOU 6736  N   GLY C 876     3040   3415   3042   -116     84    150       N  
-ATOM   6737  CA  GLY C 876     -83.532  28.026 -29.991  1.00 24.85           C  
-ANISOU 6737  CA  GLY C 876     3056   3341   3045   -101    100    159       C  
-ATOM   6738  C   GLY C 876     -82.034  27.969 -29.888  1.00 24.87           C  
-ANISOU 6738  C   GLY C 876     3103   3289   3058    -87     96    146       C  
-ATOM   6739  O   GLY C 876     -81.346  27.606 -30.847  1.00 24.65           O  
-ANISOU 6739  O   GLY C 876     3081   3262   3023    -92     83    130       O  
-ATOM   6740  N   LEU C 877     -81.518  28.344 -28.729  1.00 23.74           N  
-ANISOU 6740  N   LEU C 877     2987   3105   2929    -69    108    151       N  
-ATOM   6741  CA  LEU C 877     -80.091  28.212 -28.468  1.00 23.29           C  
-ANISOU 6741  CA  LEU C 877     2966   3005   2879    -58    103    135       C  
-ATOM   6742  C   LEU C 877     -79.738  26.755 -28.377  1.00 22.50           C  
-ANISOU 6742  C   LEU C 877     2894   2882   2775    -82     96    113       C  
-ATOM   6743  O   LEU C 877     -80.491  25.952 -27.828  1.00 23.44           O  
-ANISOU 6743  O   LEU C 877     3020   2994   2894   -106    104    111       O  
-ATOM   6744  CB  LEU C 877     -79.708  28.920 -27.176  1.00 21.98           C  
-ANISOU 6744  CB  LEU C 877     2818   2810   2723    -35    116    141       C  
-ATOM   6745  CG  LEU C 877     -79.853  30.425 -27.236  1.00 22.50           C  
-ANISOU 6745  CG  LEU C 877     2870   2884   2795     -8    129    160       C  
-ATOM   6746  CD1 LEU C 877     -79.506  31.026 -25.889  1.00 23.13           C  
-ANISOU 6746  CD1 LEU C 877     2972   2934   2882      7    141    157       C  
-ATOM   6747  CD2 LEU C 877     -78.981  31.015 -28.313  1.00 22.18           C  
-ANISOU 6747  CD2 LEU C 877     2826   2846   2756      1    125    158       C  
-ATOM   6748  N   ARG C 878     -78.616  26.408 -28.964  1.00 24.04           N  
-ANISOU 6748  N   ARG C 878     3105   3063   2966    -76     86     97       N  
-ATOM   6749  CA  ARG C 878     -78.202  25.022 -29.071  1.00 26.56           C  
-ANISOU 6749  CA  ARG C 878     3457   3357   3278    -92     82     76       C  
-ATOM   6750  C   ARG C 878     -76.792  24.888 -28.591  1.00 24.76           C  
-ANISOU 6750  C   ARG C 878     3259   3102   3049    -63     80     69       C  
-ATOM   6751  O   ARG C 878     -76.104  25.865 -28.402  1.00 24.89           O  
-ANISOU 6751  O   ARG C 878     3264   3124   3070    -39     78     74       O  
-ATOM   6752  CB  ARG C 878     -78.321  24.518 -30.524  1.00 28.23           C  
-ANISOU 6752  CB  ARG C 878     3657   3591   3477   -112     71     60       C  
-ATOM   6753  CG  ARG C 878     -79.731  24.152 -30.953  1.00 31.86           C  
-ANISOU 6753  CG  ARG C 878     4092   4084   3932   -152     71     57       C  
-ATOM   6754  CD  ARG C 878     -79.965  24.572 -32.411  1.00 35.20           C  
-ANISOU 6754  CD  ARG C 878     4478   4559   4339   -154     56     53       C  
-ATOM   6755  NE  ARG C 878     -79.883  26.041 -32.508  1.00 37.87           N  
-ANISOU 6755  NE  ARG C 878     4788   4922   4681   -116     57     82       N  
-ATOM   6756  CZ  ARG C 878     -79.469  26.740 -33.558  1.00 36.16           C  
-ANISOU 6756  CZ  ARG C 878     4553   4733   4454    -93     51     90       C  
-ATOM   6757  NH1 ARG C 878     -79.087  26.153 -34.682  1.00 38.25           N  
-ANISOU 6757  NH1 ARG C 878     4819   5013   4701   -100     38     70       N  
-ATOM   6758  NH2 ARG C 878     -79.420  28.053 -33.455  1.00 37.38           N  
-ANISOU 6758  NH2 ARG C 878     4692   4896   4615    -60     61    118       N  
-ATOM   6759  N   ILE C 879     -76.373  23.645 -28.405  1.00 26.46           N  
-ANISOU 6759  N   ILE C 879     3512   3287   3256    -64     84     56       N  
-ATOM   6760  CA  ILE C 879     -75.067  23.313 -27.924  1.00 26.42           C  
-ANISOU 6760  CA  ILE C 879     3534   3263   3243    -30     83     50       C  
-ATOM   6761  C   ILE C 879     -74.291  22.795 -29.148  1.00 29.55           C  
-ANISOU 6761  C   ILE C 879     3937   3664   3628    -25     74     34       C  
-ATOM   6762  O   ILE C 879     -74.822  22.082 -29.979  1.00 25.61           O  
-ANISOU 6762  O   ILE C 879     3447   3161   3125    -51     75     22       O  
-ATOM   6763  CB  ILE C 879     -75.181  22.256 -26.833  1.00 28.33           C  
-ANISOU 6763  CB  ILE C 879     3818   3468   3478    -24     99     53       C  
-ATOM   6764  CG1 ILE C 879     -75.821  22.868 -25.570  1.00 27.84           C  
-ANISOU 6764  CG1 ILE C 879     3747   3407   3423    -21    108     70       C  
-ATOM   6765  CG2 ILE C 879     -73.833  21.608 -26.475  1.00 29.79           C  
-ANISOU 6765  CG2 ILE C 879     4036   3638   3645     19    100     48       C  
-ATOM   6766  CD1 ILE C 879     -76.202  21.814 -24.537  1.00 27.54           C  
-ANISOU 6766  CD1 ILE C 879     3751   3333   3378    -20    131     79       C  
-ATOM   6767  N   ALA C 880     -73.000  23.085 -29.184  1.00 29.16           N  
-ANISOU 6767  N   ALA C 880     3885   3624   3572      8     67     30       N  
-ATOM   6768  CA  ALA C 880     -72.140  22.509 -30.178  1.00 28.63           C  
-ANISOU 6768  CA  ALA C 880     3828   3559   3490     22     62     17       C  
-ATOM   6769  C   ALA C 880     -72.362  20.990 -30.321  1.00 24.56           C  
-ANISOU 6769  C   ALA C 880     3363   3007   2963     16     73      5       C  
-ATOM   6770  O   ALA C 880     -72.460  20.256 -29.348  1.00 25.96           O  
-ANISOU 6770  O   ALA C 880     3575   3151   3136     25     88     10       O  
-ATOM   6771  CB  ALA C 880     -70.688  22.808 -29.838  1.00 29.04           C  
-ANISOU 6771  CB  ALA C 880     3874   3627   3534     62     56     16       C  
-ATOM   6772  N   PRO C 881     -72.405  20.505 -31.550  1.00 23.41           N  
-ANISOU 6772  N   PRO C 881     3223   2864   2809      2     70    -11       N  
-ATOM   6773  CA  PRO C 881     -72.655  19.068 -31.761  1.00 23.70           C  
-ANISOU 6773  CA  PRO C 881     3312   2858   2834    -10     86    -29       C  
-ATOM   6774  C   PRO C 881     -71.518  18.173 -31.294  1.00 24.87           C  
-ANISOU 6774  C   PRO C 881     3509   2975   2966     40    100    -28       C  
-ATOM   6775  O   PRO C 881     -70.398  18.641 -31.100  1.00 25.30           O  
-ANISOU 6775  O   PRO C 881     3547   3055   3012     85     91    -20       O  
-ATOM   6776  CB  PRO C 881     -72.845  18.957 -33.278  1.00 23.90           C  
-ANISOU 6776  CB  PRO C 881     3326   2905   2850    -33     76    -50       C  
-ATOM   6777  CG  PRO C 881     -72.235  20.176 -33.877  1.00 23.56           C  
-ANISOU 6777  CG  PRO C 881     3233   2912   2807    -12     58    -39       C  
-ATOM   6778  CD  PRO C 881     -72.198  21.246 -32.814  1.00 23.05           C  
-ANISOU 6778  CD  PRO C 881     3140   2860   2760     -1     56    -15       C  
-ATOM   6779  N   PRO C 882     -71.807  16.903 -31.035  1.00 26.36           N  
-ANISOU 6779  N   PRO C 882     3759   3110   3149     34    124    -36       N  
-ATOM   6780  CA  PRO C 882     -70.802  15.892 -30.623  1.00 28.37           C  
-ANISOU 6780  CA  PRO C 882     4070   3328   3382     90    145    -32       C  
-ATOM   6781  C   PRO C 882     -69.536  15.877 -31.524  1.00 31.32           C  
-ANISOU 6781  C   PRO C 882     4438   3728   3734    136    134    -41       C  
-ATOM   6782  O   PRO C 882     -68.427  15.721 -31.031  1.00 28.53           O  
-ANISOU 6782  O   PRO C 882     4094   3385   3363    198    138    -28       O  
-ATOM   6783  CB  PRO C 882     -71.550  14.562 -30.788  1.00 29.65           C  
-ANISOU 6783  CB  PRO C 882     4300   3423   3543     56    176    -49       C  
-ATOM   6784  CG  PRO C 882     -72.997  14.920 -30.710  1.00 29.97           C  
-ANISOU 6784  CG  PRO C 882     4312   3467   3607    -17    173    -53       C  
-ATOM   6785  CD  PRO C 882     -73.162  16.348 -31.165  1.00 28.24           C  
-ANISOU 6785  CD  PRO C 882     4013   3319   3397    -29    138    -49       C  
-ATOM   6786  N   GLU C 883     -69.733  16.088 -32.829  1.00 31.88           N  
-ANISOU 6786  N   GLU C 883     4487   3820   3804    106    121    -61       N  
-ATOM   6787  CA  GLU C 883     -68.660  16.071 -33.809  1.00 33.87           C  
-ANISOU 6787  CA  GLU C 883     4732   4100   4036    144    114    -70       C  
-ATOM   6788  C   GLU C 883     -67.694  17.249 -33.664  1.00 33.44           C  
-ANISOU 6788  C   GLU C 883     4617   4106   3982    177     93    -52       C  
-ATOM   6789  O   GLU C 883     -66.573  17.187 -34.151  1.00 33.87           O  
-ANISOU 6789  O   GLU C 883     4665   4186   4017    221     92    -53       O  
-ATOM   6790  CB  GLU C 883     -69.230  16.083 -35.242  1.00 37.06           C  
-ANISOU 6790  CB  GLU C 883     5125   4517   4437    101    104    -96       C  
-ATOM   6791  CG  GLU C 883     -70.129  14.898 -35.588  1.00 40.41           C  
-ANISOU 6791  CG  GLU C 883     5608   4888   4858     58    123   -125       C  
-ATOM   6792  CD  GLU C 883     -71.596  15.094 -35.213  1.00 42.62           C  
-ANISOU 6792  CD  GLU C 883     5871   5161   5161    -11    122   -129       C  
-ATOM   6793  OE1 GLU C 883     -72.328  14.088 -35.238  1.00 46.04           O  
-ANISOU 6793  OE1 GLU C 883     6353   5546   5595    -52    143   -152       O  
-ATOM   6794  OE2 GLU C 883     -72.037  16.229 -34.937  1.00 42.16           O  
-ANISOU 6794  OE2 GLU C 883     5754   5147   5119    -26    103   -110       O  
-ATOM   6795  N   ALA C 884     -68.140  18.336 -33.053  1.00 29.45           N  
-ANISOU 6795  N   ALA C 884     4066   3624   3498    153     80    -38       N  
-ATOM   6796  CA  ALA C 884     -67.290  19.511 -32.887  1.00 28.29           C  
-ANISOU 6796  CA  ALA C 884     3864   3530   3356    173     65    -27       C  
-ATOM   6797  C   ALA C 884     -66.207  19.270 -31.849  1.00 26.97           C  
-ANISOU 6797  C   ALA C 884     3703   3373   3172    227     69    -18       C  
-ATOM   6798  O   ALA C 884     -66.440  18.611 -30.856  1.00 25.21           O  
-ANISOU 6798  O   ALA C 884     3516   3118   2943    242     81    -11       O  
-ATOM   6799  CB  ALA C 884     -68.121  20.707 -32.470  1.00 28.31           C  
-ANISOU 6799  CB  ALA C 884     3825   3546   3384    133     56    -17       C  
-ATOM   6800  N   PRO C 885     -65.008  19.787 -32.089  1.00 26.99           N  
-ANISOU 6800  N   PRO C 885     3667   3425   3163    257     60    -17       N  
-ATOM   6801  CA  PRO C 885     -64.004  19.803 -31.018  1.00 27.34           C  
-ANISOU 6801  CA  PRO C 885     3699   3499   3190    304     58    -10       C  
-ATOM   6802  C   PRO C 885     -64.386  20.682 -29.817  1.00 27.89           C  
-ANISOU 6802  C   PRO C 885     3742   3579   3275    282     50     -5       C  
-ATOM   6803  O   PRO C 885     -65.157  21.639 -29.946  1.00 33.23           O  
-ANISOU 6803  O   PRO C 885     4395   4253   3980    233     44     -6       O  
-ATOM   6804  CB  PRO C 885     -62.778  20.419 -31.690  1.00 25.34           C  
-ANISOU 6804  CB  PRO C 885     3395   3307   2927    322     50    -15       C  
-ATOM   6805  CG  PRO C 885     -63.165  20.760 -33.065  1.00 26.06           C  
-ANISOU 6805  CG  PRO C 885     3476   3394   3031    287     49    -20       C  
-ATOM   6806  CD  PRO C 885     -64.609  20.560 -33.269  1.00 25.12           C  
-ANISOU 6806  CD  PRO C 885     3389   3226   2931    243     52    -22       C  
-ATOM   6807  N   VAL C 886     -63.767  20.430 -28.689  1.00 30.66           N  
-ANISOU 6807  N   VAL C 886     4095   3949   3605    325     50      0       N  
-ATOM   6808  CA  VAL C 886     -63.982  21.223 -27.455  1.00 32.21           C  
-ANISOU 6808  CA  VAL C 886     4267   4162   3809    312     41      1       C  
-ATOM   6809  C   VAL C 886     -63.163  22.533 -27.395  1.00 33.02           C  
-ANISOU 6809  C   VAL C 886     4303   4326   3917    295     25    -14       C  
-ATOM   6810  O   VAL C 886     -63.398  23.405 -26.528  1.00 32.21           O  
-ANISOU 6810  O   VAL C 886     4177   4235   3825    271     18    -20       O  
-ATOM   6811  CB  VAL C 886     -63.663  20.346 -26.243  1.00 34.83           C  
-ANISOU 6811  CB  VAL C 886     4631   4495   4109    369     49     12       C  
-ATOM   6812  CG1 VAL C 886     -62.164  20.098 -26.156  1.00 40.00           C  
-ANISOU 6812  CG1 VAL C 886     5260   5212   4725    431     42      9       C  
-ATOM   6813  CG2 VAL C 886     -64.151  20.962 -24.948  1.00 39.23           C  
-ANISOU 6813  CG2 VAL C 886     5177   5057   4670    356     43     13       C  
-ATOM   6814  N   THR C 887     -62.157  22.630 -28.255  1.00 32.34           N  
-ANISOU 6814  N   THR C 887     4187   4279   3822    308     22    -20       N  
-ATOM   6815  CA  THR C 887     -61.166  23.718 -28.202  1.00 33.39           C  
-ANISOU 6815  CA  THR C 887     4256   4476   3956    293     11    -36       C  
-ATOM   6816  C   THR C 887     -61.734  25.121 -28.025  1.00 30.05           C  
-ANISOU 6816  C   THR C 887     3806   4044   3568    230     10    -45       C  
-ATOM   6817  O   THR C 887     -62.611  25.552 -28.782  1.00 28.84           O  
-ANISOU 6817  O   THR C 887     3663   3851   3443    193     18    -37       O  
-ATOM   6818  CB  THR C 887     -60.350  23.750 -29.540  1.00 37.92           C  
-ANISOU 6818  CB  THR C 887     4804   5077   4526    297     14    -38       C  
-ATOM   6819  OG1 THR C 887     -60.028  22.428 -29.952  1.00 41.72           O  
-ANISOU 6819  OG1 THR C 887     5322   5551   4978    354     21    -29       O  
-ATOM   6820  CG2 THR C 887     -59.081  24.587 -29.442  1.00 39.76           C  
-ANISOU 6820  CG2 THR C 887     4970   5385   4751    291      7    -54       C  
-ATOM   6821  N   GLY C 888     -61.222  25.833 -27.033  1.00 28.84           N  
-ANISOU 6821  N   GLY C 888     3619   3930   3410    222      1    -62       N  
-ATOM   6822  CA  GLY C 888     -61.714  27.143 -26.757  1.00 27.43           C  
-ANISOU 6822  CA  GLY C 888     3422   3737   3262    166      5    -73       C  
-ATOM   6823  C   GLY C 888     -62.871  27.171 -25.772  1.00 27.26           C  
-ANISOU 6823  C   GLY C 888     3435   3675   3249    160      6    -67       C  
-ATOM   6824  O   GLY C 888     -63.092  28.206 -25.168  1.00 29.00           O  
-ANISOU 6824  O   GLY C 888     3641   3894   3484    126      8    -82       O  
-ATOM   6825  N   TYR C 889     -63.600  26.071 -25.596  1.00 25.21           N  
-ANISOU 6825  N   TYR C 889     3221   3380   2979    189      9    -48       N  
-ATOM   6826  CA  TYR C 889     -64.626  26.019 -24.560  1.00 26.46           C  
-ANISOU 6826  CA  TYR C 889     3408   3505   3140    187     12    -40       C  
-ATOM   6827  C   TYR C 889     -64.005  25.852 -23.175  1.00 27.35           C  
-ANISOU 6827  C   TYR C 889     3513   3659   3219    222      2    -52       C  
-ATOM   6828  O   TYR C 889     -63.728  24.746 -22.728  1.00 31.84           O  
-ANISOU 6828  O   TYR C 889     4106   4236   3757    274      2    -40       O  
-ATOM   6829  CB  TYR C 889     -65.611  24.892 -24.813  1.00 24.74           C  
-ANISOU 6829  CB  TYR C 889     3241   3237   2924    199     23    -17       C  
-ATOM   6830  CG  TYR C 889     -66.608  25.182 -25.891  1.00 24.48           C  
-ANISOU 6830  CG  TYR C 889     3214   3167   2922    159     31     -7       C  
-ATOM   6831  CD1 TYR C 889     -66.423  24.731 -27.192  1.00 23.52           C  
-ANISOU 6831  CD1 TYR C 889     3095   3040   2801    158     32     -5       C  
-ATOM   6832  CD2 TYR C 889     -67.781  25.895 -25.596  1.00 23.15           C  
-ANISOU 6832  CD2 TYR C 889     3047   2972   2776    125     38      0       C  
-ATOM   6833  CE1 TYR C 889     -67.374  24.995 -28.170  1.00 24.27           C  
-ANISOU 6833  CE1 TYR C 889     3192   3111   2917    124     38      3       C  
-ATOM   6834  CE2 TYR C 889     -68.737  26.137 -26.563  1.00 25.26           C  
-ANISOU 6834  CE2 TYR C 889     3315   3216   3065     95     44     10       C  
-ATOM   6835  CZ  TYR C 889     -68.526  25.714 -27.844  1.00 24.58           C  
-ANISOU 6835  CZ  TYR C 889     3229   3132   2978     94     43     11       C  
-ATOM   6836  OH  TYR C 889     -69.503  25.968 -28.778  1.00 28.35           O  
-ANISOU 6836  OH  TYR C 889     3703   3597   3471     67     48     21       O  
-ATOM   6837  N   MET C 890     -63.967  26.936 -22.450  1.00 26.46           N  
-ANISOU 6837  N   MET C 890     3375   3566   3114    194     -3    -73       N  
-ATOM   6838  CA  MET C 890     -63.490  26.959 -21.091  1.00 28.34           C  
-ANISOU 6838  CA  MET C 890     3601   3848   3318    220    -14    -89       C  
-ATOM   6839  C   MET C 890     -64.183  25.996 -20.101  1.00 25.91           C  
-ANISOU 6839  C   MET C 890     3339   3519   2988    265     -9    -66       C  
-ATOM   6840  O   MET C 890     -63.511  25.406 -19.243  1.00 25.85           O  
-ANISOU 6840  O   MET C 890     3329   3556   2936    317    -17    -67       O  
-ATOM   6841  CB  MET C 890     -63.593  28.380 -20.572  1.00 30.76           C  
-ANISOU 6841  CB  MET C 890     3882   4162   3642    171    -15   -119       C  
-ATOM   6842  CG  MET C 890     -62.929  28.553 -19.228  1.00 39.31           C  
-ANISOU 6842  CG  MET C 890     4942   5306   4686    191    -31   -147       C  
-ATOM   6843  SD  MET C 890     -62.642  30.295 -18.859  1.00 47.62           S  
-ANISOU 6843  SD  MET C 890     5958   6377   5758    122    -31   -197       S  
-ATOM   6844  CE  MET C 890     -61.830  30.131 -17.333  1.00 48.39           C  
-ANISOU 6844  CE  MET C 890     6028   6560   5796    158    -55   -230       C  
-ATOM   6845  N   PHE C 891     -65.491  25.831 -20.224  1.00 21.97           N  
-ANISOU 6845  N   PHE C 891     2879   2956   2514    246      8    -43       N  
-ATOM   6846  CA  PHE C 891     -66.235  24.938 -19.330  1.00 22.37           C  
-ANISOU 6846  CA  PHE C 891     2974   2979   2547    280     20    -19       C  
-ATOM   6847  C   PHE C 891     -66.998  23.858 -20.099  1.00 21.80           C  
-ANISOU 6847  C   PHE C 891     2947   2848   2490    281     38     10       C  
-ATOM   6848  O   PHE C 891     -68.064  23.387 -19.697  1.00 21.76           O  
-ANISOU 6848  O   PHE C 891     2978   2800   2491    277     56     30       O  
-ATOM   6849  CB  PHE C 891     -67.189  25.770 -18.461  1.00 22.73           C  
-ANISOU 6849  CB  PHE C 891     3023   3008   2606    253     25    -22       C  
-ATOM   6850  CG  PHE C 891     -66.479  26.785 -17.604  1.00 23.07           C  
-ANISOU 6850  CG  PHE C 891     3029   3106   2632    249      9    -57       C  
-ATOM   6851  CD1 PHE C 891     -65.689  26.371 -16.551  1.00 24.55           C  
-ANISOU 6851  CD1 PHE C 891     3210   3348   2771    299     -3    -66       C  
-ATOM   6852  CD2 PHE C 891     -66.541  28.144 -17.901  1.00 22.64           C  
-ANISOU 6852  CD2 PHE C 891     2947   3048   2607    196      8    -83       C  
-ATOM   6853  CE1 PHE C 891     -65.014  27.296 -15.785  1.00 24.15           C  
-ANISOU 6853  CE1 PHE C 891     3121   3355   2700    289    -19   -105       C  
-ATOM   6854  CE2 PHE C 891     -65.887  29.078 -17.129  1.00 22.16           C  
-ANISOU 6854  CE2 PHE C 891     2857   3033   2531    184     -3   -122       C  
-ATOM   6855  CZ  PHE C 891     -65.133  28.652 -16.058  1.00 23.85           C  
-ANISOU 6855  CZ  PHE C 891     3059   3307   2695    227    -19   -136       C  
-ATOM   6856  N   GLY C 892     -66.443  23.448 -21.225  1.00 23.20           N  
-ANISOU 6856  N   GLY C 892     3119   3025   2669    284     36      9       N  
-ATOM   6857  CA  GLY C 892     -67.094  22.451 -22.067  1.00 21.83           C  
-ANISOU 6857  CA  GLY C 892     2988   2798   2508    278     53     27       C  
-ATOM   6858  C   GLY C 892     -68.149  23.011 -23.016  1.00 22.54           C  
-ANISOU 6858  C   GLY C 892     3070   2855   2638    218     56     27       C  
-ATOM   6859  O   GLY C 892     -68.517  24.190 -22.981  1.00 22.07           O  
-ANISOU 6859  O   GLY C 892     2980   2805   2599    184     50     19       O  
-ATOM   6860  N   LYS C 893     -68.662  22.117 -23.838  1.00 24.14           N  
-ANISOU 6860  N   LYS C 893     3305   3020   2848    208     68     36       N  
-ATOM   6861  CA  LYS C 893     -69.719  22.407 -24.770  1.00 23.95           C  
-ANISOU 6861  CA  LYS C 893     3276   2972   2854    158     71     37       C  
-ATOM   6862  C   LYS C 893     -71.002  22.646 -24.002  1.00 22.21           C  
-ANISOU 6862  C   LYS C 893     3063   2730   2647    132     82     49       C  
-ATOM   6863  O   LYS C 893     -71.508  21.756 -23.365  1.00 26.39           O  
-ANISOU 6863  O   LYS C 893     3630   3230   3169    140     99     61       O  
-ATOM   6864  CB  LYS C 893     -69.934  21.236 -25.701  1.00 23.41           C  
-ANISOU 6864  CB  LYS C 893     3244   2871   2782    153     82     37       C  
-ATOM   6865  CG  LYS C 893     -68.804  20.968 -26.686  1.00 25.68           C  
-ANISOU 6865  CG  LYS C 893     3525   3177   3055    177     74     26       C  
-ATOM   6866  CD  LYS C 893     -69.118  19.678 -27.456  1.00 25.48           C  
-ANISOU 6866  CD  LYS C 893     3548   3109   3024    174     90     23       C  
-ATOM   6867  CE  LYS C 893     -67.990  19.246 -28.317  1.00 26.40           C  
-ANISOU 6867  CE  LYS C 893     3668   3241   3121    208     86     13       C  
-ATOM   6868  NZ  LYS C 893     -68.462  18.268 -29.345  1.00 27.81           N  
-ANISOU 6868  NZ  LYS C 893     3887   3380   3299    190     99      2       N  
-ATOM   6869  N   GLY C 894     -71.545  23.845 -24.087  1.00 21.38           N  
-ANISOU 6869  N   GLY C 894     2923   2638   2562    103     76     47       N  
-ATOM   6870  CA  GLY C 894     -72.793  24.187 -23.390  1.00 20.61           C  
-ANISOU 6870  CA  GLY C 894     2827   2528   2477     82     88     60       C  
-ATOM   6871  C   GLY C 894     -73.306  25.489 -23.958  1.00 20.14           C  
-ANISOU 6871  C   GLY C 894     2731   2483   2439     55     84     59       C  
-ATOM   6872  O   GLY C 894     -72.772  25.972 -24.948  1.00 20.86           O  
-ANISOU 6872  O   GLY C 894     2801   2589   2536     49     75     51       O  
-ATOM   6873  N   ILE C 895     -74.361  26.046 -23.369  1.00 19.75           N  
-ANISOU 6873  N   ILE C 895     2675   2430   2399     42     94     71       N  
-ATOM   6874  CA  ILE C 895     -74.834  27.364 -23.766  1.00 18.65           C  
-ANISOU 6874  CA  ILE C 895     2506   2302   2277     28     95     75       C  
-ATOM   6875  C   ILE C 895     -74.317  28.331 -22.705  1.00 18.32           C  
-ANISOU 6875  C   ILE C 895     2461   2266   2232     43     97     65       C  
-ATOM   6876  O   ILE C 895     -74.563  28.129 -21.518  1.00 17.27           O  
-ANISOU 6876  O   ILE C 895     2343   2129   2089     57    102     67       O  
-ATOM   6877  CB  ILE C 895     -76.341  27.420 -23.839  1.00 20.13           C  
-ANISOU 6877  CB  ILE C 895     2686   2489   2474      9    108     94       C  
-ATOM   6878  CG1 ILE C 895     -76.886  26.305 -24.724  1.00 22.09           C  
-ANISOU 6878  CG1 ILE C 895     2938   2734   2721    -15    106     96       C  
-ATOM   6879  CG2 ILE C 895     -76.798  28.754 -24.418  1.00 19.50           C  
-ANISOU 6879  CG2 ILE C 895     2577   2423   2407      4    112    102       C  
-ATOM   6880  CD1 ILE C 895     -78.371  26.083 -24.570  1.00 22.77           C  
-ANISOU 6880  CD1 ILE C 895     3014   2825   2811    -38    119    111       C  
-ATOM   6881  N   TYR C 896     -73.639  29.370 -23.164  1.00 17.23           N  
-ANISOU 6881  N   TYR C 896     2304   2138   2104     39     94     53       N  
-ATOM   6882  CA  TYR C 896     -72.948  30.334 -22.336  1.00 17.43           C  
-ANISOU 6882  CA  TYR C 896     2326   2170   2128     43     95     33       C  
-ATOM   6883  C   TYR C 896     -73.738  31.655 -22.276  1.00 17.32           C  
-ANISOU 6883  C   TYR C 896     2307   2142   2132     33    114     40       C  
-ATOM   6884  O   TYR C 896     -74.259  32.131 -23.298  1.00 16.64           O  
-ANISOU 6884  O   TYR C 896     2211   2051   2060     24    123     57       O  
-ATOM   6885  CB  TYR C 896     -71.548  30.601 -22.911  1.00 17.73           C  
-ANISOU 6885  CB  TYR C 896     2347   2226   2164     39     84     11       C  
-ATOM   6886  CG  TYR C 896     -70.543  29.483 -22.663  1.00 17.45           C  
-ANISOU 6886  CG  TYR C 896     2315   2212   2104     61     67      0       C  
-ATOM   6887  CD1 TYR C 896     -70.690  28.271 -23.272  1.00 17.46           C  
-ANISOU 6887  CD1 TYR C 896     2330   2206   2099     71     63     14       C  
-ATOM   6888  CD2 TYR C 896     -69.432  29.671 -21.851  1.00 17.88           C  
-ANISOU 6888  CD2 TYR C 896     2359   2297   2140     73     56    -26       C  
-ATOM   6889  CE1 TYR C 896     -69.792  27.241 -23.027  1.00 18.25           C  
-ANISOU 6889  CE1 TYR C 896     2439   2321   2173    101     53      8       C  
-ATOM   6890  CE2 TYR C 896     -68.497  28.648 -21.644  1.00 18.86           C  
-ANISOU 6890  CE2 TYR C 896     2483   2448   2236    104     42    -32       C  
-ATOM   6891  CZ  TYR C 896     -68.699  27.439 -22.242  1.00 18.14           C  
-ANISOU 6891  CZ  TYR C 896     2413   2342   2139    121     42    -12       C  
-ATOM   6892  OH  TYR C 896     -67.799  26.417 -22.075  1.00 21.03           O  
-ANISOU 6892  OH  TYR C 896     2786   2730   2475    160     34    -14       O  
-ATOM   6893  N   PHE C 897     -73.821  32.226 -21.070  1.00 17.18           N  
-ANISOU 6893  N   PHE C 897     2299   2120   2107     40    121     28       N  
-ATOM   6894  CA  PHE C 897     -74.518  33.478 -20.799  1.00 17.30           C  
-ANISOU 6894  CA  PHE C 897     2320   2118   2136     37    144     32       C  
-ATOM   6895  C   PHE C 897     -73.672  34.349 -19.898  1.00 18.11           C  
-ANISOU 6895  C   PHE C 897     2428   2219   2233     32    147     -4       C  
-ATOM   6896  O   PHE C 897     -72.890  33.848 -19.128  1.00 18.22           O  
-ANISOU 6896  O   PHE C 897     2441   2255   2226     38    129    -28       O  
-ATOM   6897  CB  PHE C 897     -75.849  33.234 -20.070  1.00 17.44           C  
-ANISOU 6897  CB  PHE C 897     2348   2132   2148     53    155     55       C  
-ATOM   6898  CG  PHE C 897     -76.818  32.402 -20.816  1.00 17.09           C  
-ANISOU 6898  CG  PHE C 897     2294   2094   2107     50    155     86       C  
-ATOM   6899  CD1 PHE C 897     -76.776  31.009 -20.727  1.00 17.25           C  
-ANISOU 6899  CD1 PHE C 897     2319   2120   2115     49    142     89       C  
-ATOM   6900  CD2 PHE C 897     -77.810  32.982 -21.556  1.00 17.40           C  
-ANISOU 6900  CD2 PHE C 897     2320   2134   2159     50    170    110       C  
-ATOM   6901  CE1 PHE C 897     -77.666  30.235 -21.427  1.00 16.05           C  
-ANISOU 6901  CE1 PHE C 897     2158   1972   1966     37    143    110       C  
-ATOM   6902  CE2 PHE C 897     -78.739  32.193 -22.232  1.00 17.40           C  
-ANISOU 6902  CE2 PHE C 897     2304   2150   2157     43    167    133       C  
-ATOM   6903  CZ  PHE C 897     -78.651  30.819 -22.169  1.00 16.07           C  
-ANISOU 6903  CZ  PHE C 897     2140   1985   1980     31    153    130       C  
-ATOM   6904  N   ALA C 898     -73.911  35.660 -19.961  1.00 19.91           N  
-ANISOU 6904  N   ALA C 898     2665   2423   2478     22    171     -9       N  
-ATOM   6905  CA  ALA C 898     -73.283  36.639 -19.091  1.00 20.46           C  
-ANISOU 6905  CA  ALA C 898     2745   2484   2544      9    181    -49       C  
-ATOM   6906  C   ALA C 898     -74.333  37.384 -18.251  1.00 21.99           C  
-ANISOU 6906  C   ALA C 898     2965   2653   2737     25    206    -42       C  
-ATOM   6907  O   ALA C 898     -75.482  37.503 -18.659  1.00 21.39           O  
-ANISOU 6907  O   ALA C 898     2893   2563   2670     43    224     -4       O  
-ATOM   6908  CB  ALA C 898     -72.559  37.648 -19.943  1.00 21.70           C  
-ANISOU 6908  CB  ALA C 898     2899   2622   2724    -21    197    -63       C  
-ATOM   6909  N   ASP C 899     -73.895  37.947 -17.119  1.00 22.51           N  
-ANISOU 6909  N   ASP C 899     3045   2719   2790     19    209    -82       N  
-ATOM   6910  CA  ASP C 899     -74.688  38.935 -16.416  1.00 22.58           C  
-ANISOU 6910  CA  ASP C 899     3084   2697   2800     31    240    -85       C  
-ATOM   6911  C   ASP C 899     -74.230  40.380 -16.696  1.00 23.80           C  
-ANISOU 6911  C   ASP C 899     3258   2809   2975      2    272   -114       C  
-ATOM   6912  O   ASP C 899     -74.858  41.314 -16.202  1.00 22.45           O  
-ANISOU 6912  O   ASP C 899     3120   2602   2807     12    305   -117       O  
-ATOM   6913  CB  ASP C 899     -74.757  38.654 -14.900  1.00 22.71           C  
-ANISOU 6913  CB  ASP C 899     3110   2736   2783     48    230   -109       C  
-ATOM   6914  CG  ASP C 899     -73.413  38.568 -14.231  1.00 21.65           C  
-ANISOU 6914  CG  ASP C 899     2964   2634   2627     27    205   -164       C  
-ATOM   6915  OD1 ASP C 899     -72.408  39.098 -14.738  1.00 22.94           O  
-ANISOU 6915  OD1 ASP C 899     3116   2796   2803    -11    203   -196       O  
-ATOM   6916  OD2 ASP C 899     -73.351  37.918 -13.177  1.00 22.60           O  
-ANISOU 6916  OD2 ASP C 899     3083   2791   2714     49    186   -174       O  
-ATOM   6917  N   MET C 900     -73.167  40.542 -17.482  1.00 24.19           N  
-ANISOU 6917  N   MET C 900     3292   2860   3039    -34    267   -132       N  
-ATOM   6918  CA  MET C 900     -72.693  41.867 -17.916  1.00 24.86           C  
-ANISOU 6918  CA  MET C 900     3398   2898   3149    -68    303   -155       C  
-ATOM   6919  C   MET C 900     -73.002  42.025 -19.409  1.00 24.13           C  
-ANISOU 6919  C   MET C 900     3302   2784   3082    -62    322   -106       C  
-ATOM   6920  O   MET C 900     -72.510  41.247 -20.231  1.00 23.46           O  
-ANISOU 6920  O   MET C 900     3185   2730   2999    -68    297    -93       O  
-ATOM   6921  CB  MET C 900     -71.206  42.031 -17.705  1.00 26.13           C  
-ANISOU 6921  CB  MET C 900     3540   3082   3307   -119    288   -213       C  
-ATOM   6922  CG  MET C 900     -70.703  41.851 -16.292  1.00 28.14           C  
-ANISOU 6922  CG  MET C 900     3789   3374   3529   -127    264   -267       C  
-ATOM   6923  SD  MET C 900     -71.120  43.265 -15.235  1.00 32.46           S  
-ANISOU 6923  SD  MET C 900     4388   3868   4076   -140    306   -309       S  
-ATOM   6924  CE  MET C 900     -69.881  44.446 -15.712  1.00 31.75           C  
-ANISOU 6924  CE  MET C 900     4303   3747   4013   -218    334   -365       C  
-ATOM   6925  N   VAL C 901     -73.854  42.992 -19.750  1.00 23.33           N  
-ANISOU 6925  N   VAL C 901     3234   2633   2996    -43    367    -78       N  
-ATOM   6926  CA  VAL C 901     -74.343  43.144 -21.117  1.00 24.71           C  
-ANISOU 6926  CA  VAL C 901     3406   2794   3187    -22    387    -25       C  
-ATOM   6927  C   VAL C 901     -73.204  43.198 -22.145  1.00 24.07           C  
-ANISOU 6927  C   VAL C 901     3307   2715   3122    -60    386    -34       C  
-ATOM   6928  O   VAL C 901     -73.296  42.584 -23.207  1.00 23.80           O  
-ANISOU 6928  O   VAL C 901     3248   2707   3089    -46    371      2       O  
-ATOM   6929  CB  VAL C 901     -75.287  44.358 -21.289  1.00 25.77           C  
-ANISOU 6929  CB  VAL C 901     3584   2873   3332      9    444      6       C  
-ATOM   6930  CG1 VAL C 901     -74.557  45.681 -21.076  1.00 27.04           C  
-ANISOU 6930  CG1 VAL C 901     3790   2971   3514    -28    490    -33       C  
-ATOM   6931  CG2 VAL C 901     -75.931  44.350 -22.664  1.00 25.35           C  
-ANISOU 6931  CG2 VAL C 901     3521   2826   3286     44    457     67       C  
-ATOM   6932  N   SER C 902     -72.123  43.873 -21.815  1.00 25.33           N  
-ANISOU 6932  N   SER C 902     3478   2855   3294   -109    399    -84       N  
-ATOM   6933  CA  SER C 902     -71.018  44.045 -22.766  1.00 25.58           C  
-ANISOU 6933  CA  SER C 902     3491   2886   3341   -149    405    -93       C  
-ATOM   6934  C   SER C 902     -70.278  42.734 -23.048  1.00 24.95           C  
-ANISOU 6934  C   SER C 902     3358   2874   3245   -155    351    -99       C  
-ATOM   6935  O   SER C 902     -69.836  42.511 -24.163  1.00 26.10           O  
-ANISOU 6935  O   SER C 902     3484   3032   3399   -160    350    -78       O  
-ATOM   6936  CB  SER C 902     -70.079  45.129 -22.276  1.00 28.16           C  
-ANISOU 6936  CB  SER C 902     3840   3176   3684   -208    437   -149       C  
-ATOM   6937  OG  SER C 902     -69.503  44.815 -21.016  1.00 31.43           O  
-ANISOU 6937  OG  SER C 902     4238   3626   4077   -234    404   -209       O  
-ATOM   6938  N   LYS C 903     -70.164  41.847 -22.049  1.00 24.62           N  
-ANISOU 6938  N   LYS C 903     3298   2877   3179   -148    309   -124       N  
-ATOM   6939  CA  LYS C 903     -69.511  40.570 -22.252  1.00 22.53           C  
-ANISOU 6939  CA  LYS C 903     2992   2673   2897   -144    263   -127       C  
-ATOM   6940  C   LYS C 903     -70.224  39.800 -23.362  1.00 21.63           C  
-ANISOU 6940  C   LYS C 903     2869   2568   2784   -108    254    -71       C  
-ATOM   6941  O   LYS C 903     -69.577  39.204 -24.211  1.00 20.36           O  
-ANISOU 6941  O   LYS C 903     2681   2433   2620   -113    238    -65       O  
-ATOM   6942  CB  LYS C 903     -69.453  39.740 -20.976  1.00 23.02           C  
-ANISOU 6942  CB  LYS C 903     3043   2775   2927   -129    226   -152       C  
-ATOM   6943  CG  LYS C 903     -68.715  38.398 -21.139  1.00 22.42           C  
-ANISOU 6943  CG  LYS C 903     2930   2758   2829   -117    183   -153       C  
-ATOM   6944  CD  LYS C 903     -68.247  37.829 -19.811  1.00 22.54           C  
-ANISOU 6944  CD  LYS C 903     2935   2818   2811   -108    153   -189       C  
-ATOM   6945  CE  LYS C 903     -67.418  36.557 -19.973  1.00 22.50           C  
-ANISOU 6945  CE  LYS C 903     2897   2870   2781    -89    117   -188       C  
-ATOM   6946  NZ  LYS C 903     -67.104  35.891 -18.674  1.00 23.11           N  
-ANISOU 6946  NZ  LYS C 903     2968   2994   2820    -64     90   -212       N  
-ATOM   6947  N   SER C 904     -71.555  39.828 -23.329  1.00 21.71           N  
-ANISOU 6947  N   SER C 904     2898   2558   2792    -74    265    -35       N  
-ATOM   6948  CA  SER C 904     -72.362  39.177 -24.350  1.00 21.20           C  
-ANISOU 6948  CA  SER C 904     2822   2507   2726    -44    258     13       C  
-ATOM   6949  C   SER C 904     -72.424  39.977 -25.635  1.00 22.39           C  
-ANISOU 6949  C   SER C 904     2978   2634   2894    -43    291     43       C  
-ATOM   6950  O   SER C 904     -72.305  39.406 -26.702  1.00 24.07           O  
-ANISOU 6950  O   SER C 904     3171   2871   3103    -36    278     64       O  
-ATOM   6951  CB  SER C 904     -73.771  38.897 -23.836  1.00 21.02           C  
-ANISOU 6951  CB  SER C 904     2809   2484   2693    -10    258     40       C  
-ATOM   6952  OG  SER C 904     -73.783  37.764 -22.969  1.00 19.94           O  
-ANISOU 6952  OG  SER C 904     2663   2377   2537     -5    224     26       O  
-ATOM   6953  N   ALA C 905     -72.548  41.302 -25.534  1.00 22.97           N  
-ANISOU 6953  N   ALA C 905     3084   2660   2985    -48    336     43       N  
-ATOM   6954  CA  ALA C 905     -72.561  42.159 -26.700  1.00 24.62           C  
-ANISOU 6954  CA  ALA C 905     3305   2840   3208    -42    375     75       C  
-ATOM   6955  C   ALA C 905     -71.295  42.032 -27.567  1.00 24.78           C  
-ANISOU 6955  C   ALA C 905     3303   2874   3236    -75    371     63       C  
-ATOM   6956  O   ALA C 905     -71.370  42.199 -28.784  1.00 24.82           O  
-ANISOU 6956  O   ALA C 905     3305   2880   3244    -60    388     99       O  
-ATOM   6957  CB  ALA C 905     -72.756  43.621 -26.296  1.00 24.76           C  
-ANISOU 6957  CB  ALA C 905     3370   2793   3244    -46    431     72       C  
-ATOM   6958  N   ASN C 906     -70.155  41.712 -26.959  1.00 23.99           N  
-ANISOU 6958  N   ASN C 906     3185   2793   3136   -116    349     14       N  
-ATOM   6959  CA  ASN C 906     -68.949  41.476 -27.732  1.00 23.94           C  
-ANISOU 6959  CA  ASN C 906     3151   2811   3133   -144    342      2       C  
-ATOM   6960  C   ASN C 906     -69.114  40.374 -28.746  1.00 24.31           C  
-ANISOU 6960  C   ASN C 906     3172   2902   3165   -113    312     34       C  
-ATOM   6961  O   ASN C 906     -68.491  40.404 -29.810  1.00 25.66           O  
-ANISOU 6961  O   ASN C 906     3328   3083   3339   -120    321     47       O  
-ATOM   6962  CB  ASN C 906     -67.762  41.176 -26.844  1.00 23.46           C  
-ANISOU 6962  CB  ASN C 906     3067   2782   3067   -184    316    -55       C  
-ATOM   6963  CG  ASN C 906     -67.273  42.390 -26.100  1.00 24.95           C  
-ANISOU 6963  CG  ASN C 906     3276   2932   3273   -231    350    -97       C  
-ATOM   6964  OD1 ASN C 906     -67.577  43.544 -26.466  1.00 26.17           O  
-ANISOU 6964  OD1 ASN C 906     3467   3027   3450   -241    403    -82       O  
-ATOM   6965  ND2 ASN C 906     -66.534  42.153 -25.035  1.00 24.65           N  
-ANISOU 6965  ND2 ASN C 906     3218   2927   3222   -259    324   -151       N  
-ATOM   6966  N   TYR C 907     -69.961  39.401 -28.441  1.00 25.17           N  
-ANISOU 6966  N   TYR C 907     3275   3034   3255    -82    279     46       N  
-ATOM   6967  CA  TYR C 907     -70.170  38.253 -29.345  1.00 23.82           C  
-ANISOU 6967  CA  TYR C 907     3082   2902   3066    -58    250     69       C  
-ATOM   6968  C   TYR C 907     -71.151  38.562 -30.469  1.00 23.95           C  
-ANISOU 6968  C   TYR C 907     3104   2914   3081    -28    269    117       C  
-ATOM   6969  O   TYR C 907     -71.435  37.702 -31.296  1.00 22.52           O  
-ANISOU 6969  O   TYR C 907     2907   2767   2884    -10    247    134       O  
-ATOM   6970  CB  TYR C 907     -70.605  37.021 -28.549  1.00 23.33           C  
-ANISOU 6970  CB  TYR C 907     3015   2865   2985    -44    210     58       C  
-ATOM   6971  CG  TYR C 907     -69.478  36.478 -27.691  1.00 22.50           C  
-ANISOU 6971  CG  TYR C 907     2897   2781   2871    -62    186     17       C  
-ATOM   6972  CD1 TYR C 907     -68.429  35.768 -28.273  1.00 22.57           C  
-ANISOU 6972  CD1 TYR C 907     2883   2824   2870    -65    168      6       C  
-ATOM   6973  CD2 TYR C 907     -69.448  36.700 -26.337  1.00 22.95           C  
-ANISOU 6973  CD2 TYR C 907     2964   2832   2926    -70    183    -11       C  
-ATOM   6974  CE1 TYR C 907     -67.375  35.307 -27.528  1.00 22.73           C  
-ANISOU 6974  CE1 TYR C 907     2886   2873   2877    -74    147    -28       C  
-ATOM   6975  CE2 TYR C 907     -68.404  36.237 -25.578  1.00 23.63           C  
-ANISOU 6975  CE2 TYR C 907     3033   2947   2996    -80    160    -47       C  
-ATOM   6976  CZ  TYR C 907     -67.376  35.540 -26.184  1.00 23.88           C  
-ANISOU 6976  CZ  TYR C 907     3040   3017   3018    -80    142    -55       C  
-ATOM   6977  OH  TYR C 907     -66.334  35.091 -25.451  1.00 25.23           O  
-ANISOU 6977  OH  TYR C 907     3189   3227   3169    -83    121    -88       O  
-ATOM   6978  N   CYS C 908     -71.659  39.785 -30.521  1.00 24.99           N  
-ANISOU 6978  N   CYS C 908     3262   3008   3227    -20    312    138       N  
-ATOM   6979  CA  CYS C 908     -72.436  40.211 -31.673  1.00 27.14           C  
-ANISOU 6979  CA  CYS C 908     3537   3282   3493     16    335    187       C  
-ATOM   6980  C   CYS C 908     -71.534  40.439 -32.886  1.00 28.93           C  
-ANISOU 6980  C   CYS C 908     3755   3514   3723      8    352    198       C  
-ATOM   6981  O   CYS C 908     -71.994  40.329 -34.017  1.00 33.47           O  
-ANISOU 6981  O   CYS C 908     4322   4114   4282     40    355    235       O  
-ATOM   6982  CB  CYS C 908     -73.218  41.485 -31.357  1.00 27.85           C  
-ANISOU 6982  CB  CYS C 908     3662   3327   3595     37    383    211       C  
-ATOM   6983  SG  CYS C 908     -74.485  41.307 -30.087  1.00 31.58           S  
-ANISOU 6983  SG  CYS C 908     4143   3799   4059     58    371    209       S  
-ATOM   6984  N   HIS C 909     -70.263  40.746 -32.631  1.00 31.36           N  
-ANISOU 6984  N   HIS C 909     4062   3805   4047    -34    361    166       N  
-ATOM   6985  CA  HIS C 909     -69.257  41.037 -33.660  1.00 33.71           C  
-ANISOU 6985  CA  HIS C 909     4351   4107   4351    -49    382    173       C  
-ATOM   6986  C   HIS C 909     -69.740  42.178 -34.556  1.00 33.70           C  
-ANISOU 6986  C   HIS C 909     4377   4070   4356    -23    438    222       C  
-ATOM   6987  O   HIS C 909     -69.682  42.088 -35.752  1.00 31.36           O  
-ANISOU 6987  O   HIS C 909     4072   3798   4048      0    446    254       O  
-ATOM   6988  CB  HIS C 909     -68.863  39.775 -34.451  1.00 31.96           C  
-ANISOU 6988  CB  HIS C 909     4094   3942   4106    -38    341    172       C  
-ATOM   6989  CG  HIS C 909     -68.133  38.768 -33.623  1.00 35.70           C  
-ANISOU 6989  CG  HIS C 909     4547   4444   4574    -61    297    127       C  
-ATOM   6990  ND1 HIS C 909     -66.840  38.961 -33.198  1.00 37.77           N  
-ANISOU 6990  ND1 HIS C 909     4796   4710   4847   -100    301     91       N  
-ATOM   6991  CD2 HIS C 909     -68.528  37.573 -33.100  1.00 35.56           C  
-ANISOU 6991  CD2 HIS C 909     4520   4453   4538    -47    253    113       C  
-ATOM   6992  CE1 HIS C 909     -66.452  37.920 -32.477  1.00 39.12           C  
-ANISOU 6992  CE1 HIS C 909     4948   4913   5003   -102    258     59       C  
-ATOM   6993  NE2 HIS C 909     -67.462  37.068 -32.395  1.00 37.27           N  
-ANISOU 6993  NE2 HIS C 909     4721   4688   4752    -70    232     73       N  
-ATOM   6994  N   THR C 910     -70.236  43.247 -33.938  1.00 34.36           N  
-ANISOU 6994  N   THR C 910     4499   4099   4456    -21    479    228       N  
-ATOM   6995  CA  THR C 910     -70.625  44.412 -34.672  1.00 32.70           C  
-ANISOU 6995  CA  THR C 910     4324   3847   4253      7    541    275       C  
-ATOM   6996  C   THR C 910     -69.392  45.221 -34.968  1.00 35.73           C  
-ANISOU 6996  C   THR C 910     4722   4190   4662    -41    587    263       C  
-ATOM   6997  O   THR C 910     -68.327  44.947 -34.435  1.00 34.85           O  
-ANISOU 6997  O   THR C 910     4591   4087   4565    -98    569    212       O  
-ATOM   6998  CB  THR C 910     -71.647  45.272 -33.916  1.00 31.30           C  
-ANISOU 6998  CB  THR C 910     4190   3621   4083     33    574    290       C  
-ATOM   6999  OG1 THR C 910     -71.170  45.546 -32.603  1.00 32.30           O  
-ANISOU 6999  OG1 THR C 910     4331   3710   4230    -17    575    235       O  
-ATOM   7000  CG2 THR C 910     -72.962  44.571 -33.867  1.00 29.97           C  
-ANISOU 7000  CG2 THR C 910     4002   3500   3886     86    538    314       C  
-ATOM   7001  N   SER C 911     -69.542  46.207 -35.848  1.00 40.52           N  
-ANISOU 7001  N   SER C 911     5362   4759   5275    -16    649    311       N  
-ATOM   7002  CA  SER C 911     -68.417  47.039 -36.276  1.00 44.50           C  
-ANISOU 7002  CA  SER C 911     5883   5219   5805    -63    704    306       C  
-ATOM   7003  C   SER C 911     -68.957  48.396 -36.733  1.00 46.57           C  
-ANISOU 7003  C   SER C 911     6209   5409   6079    -29    787    359       C  
-ATOM   7004  O   SER C 911     -70.161  48.625 -36.740  1.00 42.27           O  
-ANISOU 7004  O   SER C 911     5686   4857   5516     36    797    399       O  
-ATOM   7005  CB  SER C 911     -67.671  46.356 -37.407  1.00 41.90           C  
-ANISOU 7005  CB  SER C 911     5512   4946   5460    -62    685    319       C  
-ATOM   7006  OG  SER C 911     -68.571  46.084 -38.476  1.00 46.25           O  
-ANISOU 7006  OG  SER C 911     6060   5534   5979     12    680    378       O  
-ATOM   7007  N   GLN C 912     -68.057  49.312 -37.069  1.00 52.72           N  
-ANISOU 7007  N   GLN C 912     7015   6131   6884    -73    852    359       N  
-ATOM   7008  CA  GLN C 912     -68.462  50.666 -37.475  1.00 52.60           C  
-ANISOU 7008  CA  GLN C 912     7071   6032   6883    -43    943    409       C  
-ATOM   7009  C   GLN C 912     -69.296  50.616 -38.753  1.00 50.08           C  
-ANISOU 7009  C   GLN C 912     6754   5747   6527     51    956    491       C  
-ATOM   7010  O   GLN C 912     -70.253  51.352 -38.891  1.00 49.98           O  
-ANISOU 7010  O   GLN C 912     6788   5696   6505    116   1002    542       O  
-ATOM   7011  CB  GLN C 912     -67.254  51.564 -37.623  1.00 53.99           C  
-ANISOU 7011  CB  GLN C 912     7275   6143   7097   -119   1011    390       C  
-ATOM   7012  CG  GLN C 912     -66.799  52.182 -36.307  1.00 60.46           C  
-ANISOU 7012  CG  GLN C 912     8122   6897   7951   -199   1031    320       C  
-ATOM   7013  CD  GLN C 912     -65.386  52.723 -36.371  1.00 67.31           C  
-ANISOU 7013  CD  GLN C 912     8990   7731   8855   -298   1075    279       C  
-ATOM   7014  OE1 GLN C 912     -64.467  52.257 -35.664  1.00 70.85           O  
-ANISOU 7014  OE1 GLN C 912     9389   8217   9312   -374   1031    207       O  
-ATOM   7015  NE2 GLN C 912     -65.203  53.716 -37.232  1.00 67.13           N  
-ANISOU 7015  NE2 GLN C 912     9018   7640   8848   -295   1164    327       N  
-ATOM   7016  N   GLY C 913     -68.972  49.680 -39.626  1.00 52.17           N  
-ANISOU 7016  N   GLY C 913     6963   6091   6767     63    910    501       N  
-ATOM   7017  CA  GLY C 913     -69.726  49.455 -40.846  1.00 52.15           C  
-ANISOU 7017  CA  GLY C 913     6950   6141   6722    150    908    569       C  
-ATOM   7018  C   GLY C 913     -71.072  48.794 -40.678  1.00 58.34           C  
-ANISOU 7018  C   GLY C 913     7712   6986   7470    216    854    584       C  
-ATOM   7019  O   GLY C 913     -71.937  48.978 -41.542  1.00 57.56           O  
-ANISOU 7019  O   GLY C 913     7618   6917   7335    297    870    647       O  
-ATOM   7020  N   ASP C 914     -71.220  47.972 -39.623  1.00 58.72           N  
-ANISOU 7020  N   ASP C 914     7730   7059   7523    182    789    529       N  
-ATOM   7021  CA  ASP C 914     -72.515  47.368 -39.252  1.00 56.08           C  
-ANISOU 7021  CA  ASP C 914     7375   6775   7160    232    741    536       C  
-ATOM   7022  C   ASP C 914     -72.696  47.435 -37.716  1.00 53.67           C  
-ANISOU 7022  C   ASP C 914     7084   6429   6879    194    728    487       C  
-ATOM   7023  O   ASP C 914     -72.402  46.461 -37.000  1.00 49.49           O  
-ANISOU 7023  O   ASP C 914     6519   5932   6353    151    666    434       O  
-ATOM   7024  CB  ASP C 914     -72.582  45.926 -39.771  1.00 63.08           C  
-ANISOU 7024  CB  ASP C 914     8198   7757   8014    236    664    521       C  
-ATOM   7025  CG  ASP C 914     -73.958  45.300 -39.648  1.00 69.83           C  
-ANISOU 7025  CG  ASP C 914     9026   8673   8835    287    620    535       C  
-ATOM   7026  OD1 ASP C 914     -74.881  45.783 -40.325  1.00 72.49           O  
-ANISOU 7026  OD1 ASP C 914     9369   9032   9142    357    646    591       O  
-ATOM   7027  OD2 ASP C 914     -74.096  44.298 -38.895  1.00 76.31           O  
-ANISOU 7027  OD2 ASP C 914     9816   9523   9655    256    560    490       O  
-ATOM   7028  N   PRO C 915     -73.114  48.610 -37.202  1.00 47.06           N  
-ANISOU 7028  N   PRO C 915     6305   5518   6059    211    790    504       N  
-ATOM   7029  CA  PRO C 915     -73.111  48.891 -35.767  1.00 46.45           C  
-ANISOU 7029  CA  PRO C 915     6252   5389   6007    170    790    454       C  
-ATOM   7030  C   PRO C 915     -74.409  48.527 -35.026  1.00 41.67           C  
-ANISOU 7030  C   PRO C 915     5637   4815   5381    216    758    459       C  
-ATOM   7031  O   PRO C 915     -74.586  48.892 -33.865  1.00 40.05           O  
-ANISOU 7031  O   PRO C 915     5460   4566   5192    197    767    428       O  
-ATOM   7032  CB  PRO C 915     -72.898  50.405 -35.740  1.00 45.68           C  
-ANISOU 7032  CB  PRO C 915     6230   5188   5936    168    884    474       C  
-ATOM   7033  CG  PRO C 915     -73.670  50.879 -36.931  1.00 45.56           C  
-ANISOU 7033  CG  PRO C 915     6232   5185   5893    257    927    557       C  
-ATOM   7034  CD  PRO C 915     -73.594  49.776 -37.963  1.00 45.94           C  
-ANISOU 7034  CD  PRO C 915     6214   5331   5910    274    868    572       C  
-ATOM   7035  N   ILE C 916     -75.299  47.820 -35.695  1.00 38.81           N  
-ANISOU 7035  N   ILE C 916     5234   4532   4982    272    721    496       N  
-ATOM   7036  CA  ILE C 916     -76.527  47.382 -35.109  1.00 39.57           C  
-ANISOU 7036  CA  ILE C 916     5309   4669   5055    312    688    503       C  
-ATOM   7037  C   ILE C 916     -76.409  45.885 -34.835  1.00 37.90           C  
-ANISOU 7037  C   ILE C 916     5038   4527   4833    273    606    460       C  
-ATOM   7038  O   ILE C 916     -76.163  45.080 -35.755  1.00 39.32           O  
-ANISOU 7038  O   ILE C 916     5178   4765   4995    272    571    464       O  
-ATOM   7039  CB  ILE C 916     -77.719  47.648 -36.049  1.00 41.88           C  
-ANISOU 7039  CB  ILE C 916     5594   5011   5308    404    706    574       C  
-ATOM   7040  CG1 ILE C 916     -77.747  49.132 -36.496  1.00 45.70           C  
-ANISOU 7040  CG1 ILE C 916     6143   5422   5798    452    797    626       C  
-ATOM   7041  CG2 ILE C 916     -79.004  47.148 -35.393  1.00 41.23           C  
-ANISOU 7041  CG2 ILE C 916     5481   4983   5203    439    671    577       C  
-ATOM   7042  CD1 ILE C 916     -77.984  50.146 -35.395  1.00 48.63           C  
-ANISOU 7042  CD1 ILE C 916     6578   5705   6194    455    850    618       C  
-ATOM   7043  N   GLY C 917     -76.604  45.521 -33.575  1.00 33.29           N  
-ANISOU 7043  N   GLY C 917     4453   3937   4260    246    579    419       N  
-ATOM   7044  CA  GLY C 917     -76.585  44.112 -33.154  1.00 32.85           C  
-ANISOU 7044  CA  GLY C 917     4349   3938   4195    214    508    381       C  
-ATOM   7045  C   GLY C 917     -77.842  43.645 -32.438  1.00 30.44           C  
-ANISOU 7045  C   GLY C 917     4026   3669   3872    242    483    386       C  
-ATOM   7046  O   GLY C 917     -78.720  44.455 -32.067  1.00 28.75           O  
-ANISOU 7046  O   GLY C 917     3836   3435   3654    285    519    414       O  
-ATOM   7047  N   LEU C 918     -77.931  42.329 -32.308  1.00 27.99           N  
-ANISOU 7047  N   LEU C 918     3674   3411   3550    218    425    362       N  
-ATOM   7048  CA  LEU C 918     -79.018  41.666 -31.630  1.00 27.34           C  
-ANISOU 7048  CA  LEU C 918     3568   3368   3452    230    397    361       C  
-ATOM   7049  C   LEU C 918     -78.481  40.874 -30.440  1.00 26.87           C  
-ANISOU 7049  C   LEU C 918     3508   3294   3406    180    364    309       C  
-ATOM   7050  O   LEU C 918     -77.472  40.153 -30.540  1.00 26.26           O  
-ANISOU 7050  O   LEU C 918     3422   3219   3335    141    336    277       O  
-ATOM   7051  CB  LEU C 918     -79.758  40.733 -32.574  1.00 27.85           C  
-ANISOU 7051  CB  LEU C 918     3584   3513   3486    247    362    380       C  
-ATOM   7052  CG  LEU C 918     -80.488  41.355 -33.758  1.00 29.79           C  
-ANISOU 7052  CG  LEU C 918     3817   3797   3705    306    387    434       C  
-ATOM   7053  CD1 LEU C 918     -81.074  40.287 -34.655  1.00 30.59           C  
-ANISOU 7053  CD1 LEU C 918     3865   3985   3774    308    343    438       C  
-ATOM   7054  CD2 LEU C 918     -81.566  42.305 -33.272  1.00 32.44           C  
-ANISOU 7054  CD2 LEU C 918     4166   4125   4033    361    425    470       C  
-ATOM   7055  N   ILE C 919     -79.179  41.019 -29.327  1.00 25.92           N  
-ANISOU 7055  N   ILE C 919     3398   3163   3286    190    370    305       N  
-ATOM   7056  CA  ILE C 919     -78.827  40.347 -28.101  1.00 27.20           C  
-ANISOU 7056  CA  ILE C 919     3564   3316   3456    154    344    263       C  
-ATOM   7057  C   ILE C 919     -80.100  39.798 -27.394  1.00 25.22           C  
-ANISOU 7057  C   ILE C 919     3294   3099   3189    173    331    274       C  
-ATOM   7058  O   ILE C 919     -81.157  40.417 -27.396  1.00 27.43           O  
-ANISOU 7058  O   ILE C 919     3574   3390   3459    215    356    308       O  
-ATOM   7059  CB  ILE C 919     -78.036  41.303 -27.206  1.00 27.35           C  
-ANISOU 7059  CB  ILE C 919     3626   3272   3496    136    373    234       C  
-ATOM   7060  CG1 ILE C 919     -77.383  40.538 -26.081  1.00 30.86           C  
-ANISOU 7060  CG1 ILE C 919     4068   3716   3942     99    340    186       C  
-ATOM   7061  CG2 ILE C 919     -78.932  42.358 -26.638  1.00 28.30           C  
-ANISOU 7061  CG2 ILE C 919     3776   3362   3616    175    415    255       C  
-ATOM   7062  CD1 ILE C 919     -76.286  41.338 -25.445  1.00 34.95           C  
-ANISOU 7062  CD1 ILE C 919     4616   4186   4476     67    359    146       C  
-ATOM   7063  N   LEU C 920     -79.978  38.620 -26.842  1.00 22.81           N  
-ANISOU 7063  N   LEU C 920     2973   2814   2880    144    294    249       N  
-ATOM   7064  CA  LEU C 920     -81.069  37.974 -26.146  1.00 21.53           C  
-ANISOU 7064  CA  LEU C 920     2793   2682   2704    151    283    256       C  
-ATOM   7065  C   LEU C 920     -81.016  38.173 -24.644  1.00 21.09           C  
-ANISOU 7065  C   LEU C 920     2765   2596   2654    148    292    235       C  
-ATOM   7066  O   LEU C 920     -79.945  38.226 -24.049  1.00 19.08           O  
-ANISOU 7066  O   LEU C 920     2533   2308   2409    125    286    200       O  
-ATOM   7067  CB  LEU C 920     -81.013  36.486 -26.403  1.00 20.73           C  
-ANISOU 7067  CB  LEU C 920     2666   2616   2595    120    243    242       C  
-ATOM   7068  CG  LEU C 920     -81.216  36.071 -27.837  1.00 21.24           C  
-ANISOU 7068  CG  LEU C 920     2699   2722   2648    119    229    257       C  
-ATOM   7069  CD1 LEU C 920     -80.771  34.664 -28.055  1.00 21.13           C  
-ANISOU 7069  CD1 LEU C 920     2675   2721   2631     82    195    232       C  
-ATOM   7070  CD2 LEU C 920     -82.684  36.195 -28.187  1.00 23.80           C  
-ANISOU 7070  CD2 LEU C 920     2990   3098   2954    146    237    291       C  
-ATOM   7071  N   LEU C 921     -82.196  38.255 -24.027  1.00 22.16           N  
-ANISOU 7071  N   LEU C 921     2893   2749   2779    174    304    256       N  
-ATOM   7072  CA  LEU C 921     -82.326  37.974 -22.578  1.00 21.32           C  
-ANISOU 7072  CA  LEU C 921     2802   2631   2669    169    303    237       C  
-ATOM   7073  C   LEU C 921     -83.047  36.663 -22.431  1.00 21.71           C  
-ANISOU 7073  C   LEU C 921     2820   2724   2707    154    279    244       C  
-ATOM   7074  O   LEU C 921     -84.152  36.481 -22.949  1.00 22.16           O  
-ANISOU 7074  O   LEU C 921     2843   2825   2754    167    282    274       O  
-ATOM   7075  CB  LEU C 921     -83.088  39.064 -21.861  1.00 20.12           C  
-ANISOU 7075  CB  LEU C 921     2671   2463   2513    209    341    253       C  
-ATOM   7076  CG  LEU C 921     -82.285  40.327 -21.606  1.00 20.31           C  
-ANISOU 7076  CG  LEU C 921     2741   2427   2550    214    370    233       C  
-ATOM   7077  CD1 LEU C 921     -83.231  41.444 -21.238  1.00 20.75           C  
-ANISOU 7077  CD1 LEU C 921     2819   2467   2600    265    415    259       C  
-ATOM   7078  CD2 LEU C 921     -81.251  40.130 -20.507  1.00 20.52           C  
-ANISOU 7078  CD2 LEU C 921     2792   2425   2580    182    356    183       C  
-ATOM   7079  N   GLY C 922     -82.403  35.726 -21.756  1.00 22.22           N  
-ANISOU 7079  N   GLY C 922     2894   2778   2771    126    258    217       N  
-ATOM   7080  CA  GLY C 922     -82.985  34.401 -21.511  1.00 21.17           C  
-ANISOU 7080  CA  GLY C 922     2742   2673   2629    107    242    221       C  
-ATOM   7081  C   GLY C 922     -83.211  34.175 -20.034  1.00 21.66           C  
-ANISOU 7081  C   GLY C 922     2822   2724   2682    114    250    215       C  
-ATOM   7082  O   GLY C 922     -82.410  34.592 -19.193  1.00 20.23           O  
-ANISOU 7082  O   GLY C 922     2672   2515   2501    121    253    192       O  
-ATOM   7083  N   GLU C 923     -84.305  33.499 -19.716  1.00 20.84           N  
-ANISOU 7083  N   GLU C 923     2699   2650   2571    110    256    235       N  
-ATOM   7084  CA  GLU C 923     -84.504  32.990 -18.376  1.00 21.00           C  
-ANISOU 7084  CA  GLU C 923     2735   2663   2581    113    264    233       C  
-ATOM   7085  C   GLU C 923     -83.773  31.663 -18.365  1.00 20.09           C  
-ANISOU 7085  C   GLU C 923     2632   2535   2465     83    243    216       C  
-ATOM   7086  O   GLU C 923     -84.101  30.757 -19.141  1.00 19.87           O  
-ANISOU 7086  O   GLU C 923     2586   2523   2441     53    234    222       O  
-ATOM   7087  CB  GLU C 923     -85.999  32.776 -18.050  1.00 20.27           C  
-ANISOU 7087  CB  GLU C 923     2614   2607   2480    118    284    264       C  
-ATOM   7088  CG  GLU C 923     -86.227  32.332 -16.607  1.00 21.58           C  
-ANISOU 7088  CG  GLU C 923     2801   2765   2634    126    298    266       C  
-ATOM   7089  CD  GLU C 923     -87.674  31.954 -16.307  1.00 22.14           C  
-ANISOU 7089  CD  GLU C 923     2839   2876   2698    123    320    296       C  
-ATOM   7090  OE1 GLU C 923     -88.571  32.566 -16.877  1.00 22.35           O  
-ANISOU 7090  OE1 GLU C 923     2830   2940   2723    137    330    317       O  
-ATOM   7091  OE2 GLU C 923     -87.913  31.008 -15.523  1.00 24.28           O  
-ANISOU 7091  OE2 GLU C 923     3118   3145   2962    108    328    301       O  
-ATOM   7092  N   VAL C 924     -82.758  31.553 -17.519  1.00 19.57           N  
-ANISOU 7092  N   VAL C 924     2600   2445   2392     92    236    194       N  
-ATOM   7093  CA  VAL C 924     -81.952  30.347 -17.439  1.00 17.83           C  
-ANISOU 7093  CA  VAL C 924     2397   2213   2167     77    220    181       C  
-ATOM   7094  C   VAL C 924     -82.179  29.698 -16.087  1.00 18.67           C  
-ANISOU 7094  C   VAL C 924     2524   2314   2254     90    233    188       C  
-ATOM   7095  O   VAL C 924     -82.005  30.324 -15.040  1.00 18.13           O  
-ANISOU 7095  O   VAL C 924     2472   2244   2173    118    241    181       O  
-ATOM   7096  CB  VAL C 924     -80.465  30.708 -17.601  1.00 18.05           C  
-ANISOU 7096  CB  VAL C 924     2438   2227   2194     82    200    150       C  
-ATOM   7097  CG1 VAL C 924     -79.597  29.454 -17.616  1.00 18.19           C  
-ANISOU 7097  CG1 VAL C 924     2473   2237   2202     76    185    140       C  
-ATOM   7098  CG2 VAL C 924     -80.256  31.504 -18.875  1.00 19.06           C  
-ANISOU 7098  CG2 VAL C 924     2547   2356   2339     72    194    147       C  
-ATOM   7099  N   ALA C 925     -82.519  28.422 -16.080  1.00 19.53           N  
-ANISOU 7099  N   ALA C 925     2640   2419   2362     71    239    201       N  
-ATOM   7100  CA  ALA C 925     -82.759  27.711 -14.833  1.00 19.88           C  
-ANISOU 7100  CA  ALA C 925     2710   2456   2388     85    258    214       C  
-ATOM   7101  C   ALA C 925     -81.460  27.130 -14.350  1.00 20.45           C  
-ANISOU 7101  C   ALA C 925     2816   2513   2443    107    245    198       C  
-ATOM   7102  O   ALA C 925     -81.061  26.024 -14.733  1.00 21.14           O  
-ANISOU 7102  O   ALA C 925     2920   2582   2529     95    242    199       O  
-ATOM   7103  CB  ALA C 925     -83.785  26.601 -15.061  1.00 21.18           C  
-ANISOU 7103  CB  ALA C 925     2868   2619   2560     50    277    237       C  
-ATOM   7104  N   LEU C 926     -80.767  27.864 -13.500  1.00 22.10           N  
-ANISOU 7104  N   LEU C 926     3035   2730   2633    141    237    181       N  
-ATOM   7105  CA  LEU C 926     -79.423  27.512 -13.110  1.00 21.36           C  
-ANISOU 7105  CA  LEU C 926     2962   2637   2518    165    219    160       C  
-ATOM   7106  C   LEU C 926     -79.373  26.521 -11.981  1.00 24.61           C  
-ANISOU 7106  C   LEU C 926     3406   3046   2900    196    235    178       C  
-ATOM   7107  O   LEU C 926     -78.386  25.771 -11.846  1.00 21.97           O  
-ANISOU 7107  O   LEU C 926     3092   2711   2546    218    225    172       O  
-ATOM   7108  CB  LEU C 926     -78.654  28.759 -12.663  1.00 21.01           C  
-ANISOU 7108  CB  LEU C 926     2911   2611   2463    183    203    127       C  
-ATOM   7109  CG  LEU C 926     -78.522  29.817 -13.726  1.00 19.97           C  
-ANISOU 7109  CG  LEU C 926     2754   2476   2358    158    193    110       C  
-ATOM   7110  CD1 LEU C 926     -78.077  31.119 -13.102  1.00 21.49           C  
-ANISOU 7110  CD1 LEU C 926     2947   2676   2542    169    191     79       C  
-ATOM   7111  CD2 LEU C 926     -77.540  29.380 -14.787  1.00 20.58           C  
-ANISOU 7111  CD2 LEU C 926     2824   2551   2444    142    171     97       C  
-ATOM   7112  N   GLY C 927     -80.378  26.560 -11.094  1.00 27.11           N  
-ANISOU 7112  N   GLY C 927     3728   3364   3208    205    261    200       N  
-ATOM   7113  CA  GLY C 927     -80.395  25.687  -9.922  1.00 26.20           C  
-ANISOU 7113  CA  GLY C 927     3647   3247   3061    240    282    222       C  
-ATOM   7114  C   GLY C 927     -79.153  25.858  -9.083  1.00 25.88           C  
-ANISOU 7114  C   GLY C 927     3621   3232   2981    288    263    200       C  
-ATOM   7115  O   GLY C 927     -78.689  26.951  -8.887  1.00 29.50           O  
-ANISOU 7115  O   GLY C 927     4062   3715   3433    295    243    167       O  
-ATOM   7116  N   ASN C 928     -78.636  24.762  -8.584  1.00 27.53           N  
-ANISOU 7116  N   ASN C 928     3862   3437   3162    322    271    216       N  
-ATOM   7117  CA  ASN C 928     -77.375  24.702  -7.877  1.00 31.59           C  
-ANISOU 7117  CA  ASN C 928     4385   3986   3632    374    251    198       C  
-ATOM   7118  C   ASN C 928     -76.182  24.778  -8.853  1.00 26.81           C  
-ANISOU 7118  C   ASN C 928     3761   3390   3034    364    217    167       C  
-ATOM   7119  O   ASN C 928     -75.932  23.871  -9.649  1.00 25.11           O  
-ANISOU 7119  O   ASN C 928     3560   3149   2832    356    220    180       O  
-ATOM   7120  CB  ASN C 928     -77.342  23.389  -7.070  1.00 36.97           C  
-ANISOU 7120  CB  ASN C 928     5111   4656   4278    420    280    237       C  
-ATOM   7121  CG  ASN C 928     -76.318  23.376  -5.966  1.00 44.97           C  
-ANISOU 7121  CG  ASN C 928     6134   5721   5233    489    266    227       C  
-ATOM   7122  OD1 ASN C 928     -75.504  24.293  -5.792  1.00 44.95           O  
-ANISOU 7122  OD1 ASN C 928     6102   5766   5212    499    231    184       O  
-ATOM   7123  ND2 ASN C 928     -76.337  22.269  -5.212  1.00 47.81           N  
-ANISOU 7123  ND2 ASN C 928     6537   6071   5557    539    297    267       N  
-ATOM   7124  N   MET C 929     -75.448  25.870  -8.733  1.00 24.64           N  
-ANISOU 7124  N   MET C 929     3458   3153   2750    365    187    126       N  
-ATOM   7125  CA  MET C 929     -74.369  26.184  -9.617  1.00 25.17           C  
-ANISOU 7125  CA  MET C 929     3500   3237   2827    350    157     93       C  
-ATOM   7126  C   MET C 929     -73.076  25.557  -9.142  1.00 24.23           C  
-ANISOU 7126  C   MET C 929     3385   3161   2661    402    139     85       C  
-ATOM   7127  O   MET C 929     -72.717  25.652  -7.974  1.00 23.55           O  
-ANISOU 7127  O   MET C 929     3302   3118   2529    445    135     76       O  
-ATOM   7128  CB  MET C 929     -74.193  27.707  -9.694  1.00 25.30           C  
-ANISOU 7128  CB  MET C 929     3484   3271   2857    320    139     50       C  
-ATOM   7129  CG  MET C 929     -75.381  28.399 -10.281  1.00 25.33           C  
-ANISOU 7129  CG  MET C 929     3483   3238   2904    278    156     61       C  
-ATOM   7130  SD  MET C 929     -75.281  30.212 -10.299  1.00 27.61           S  
-ANISOU 7130  SD  MET C 929     3750   3534   3208    250    149     16       S  
-ATOM   7131  CE  MET C 929     -75.001  30.535  -8.560  1.00 29.84           C  
-ANISOU 7131  CE  MET C 929     4045   3857   3437    292    147     -8       C  
-ATOM   7132  N   TYR C 930     -72.383  24.913 -10.061  1.00 24.61           N  
-ANISOU 7132  N   TYR C 930     3431   3202   2717    401    130     87       N  
-ATOM   7133  CA  TYR C 930     -71.010  24.434  -9.838  1.00 25.44           C  
-ANISOU 7133  CA  TYR C 930     3529   3358   2779    451    110     75       C  
-ATOM   7134  C   TYR C 930     -70.096  25.616 -10.106  1.00 25.71           C  
-ANISOU 7134  C   TYR C 930     3513   3441   2815    425     75     22       C  
-ATOM   7135  O   TYR C 930     -69.953  26.049 -11.249  1.00 24.56           O  
-ANISOU 7135  O   TYR C 930     3346   3278   2709    378     66      7       O  
-ATOM   7136  CB  TYR C 930     -70.745  23.277 -10.791  1.00 25.25           C  
-ANISOU 7136  CB  TYR C 930     3527   3300   2766    459    120    100       C  
-ATOM   7137  CG  TYR C 930     -69.465  22.481 -10.606  1.00 26.36           C  
-ANISOU 7137  CG  TYR C 930     3671   3484   2859    525    109    103       C  
-ATOM   7138  CD1 TYR C 930     -68.820  22.405  -9.389  1.00 27.95           C  
-ANISOU 7138  CD1 TYR C 930     3869   3750   3001    589    101    100       C  
-ATOM   7139  CD2 TYR C 930     -68.931  21.774 -11.673  1.00 26.06           C  
-ANISOU 7139  CD2 TYR C 930     3641   3428   2833    528    109    110       C  
-ATOM   7140  CE1 TYR C 930     -67.654  21.664  -9.235  1.00 29.45           C  
-ANISOU 7140  CE1 TYR C 930     4059   3990   3142    658     92    107       C  
-ATOM   7141  CE2 TYR C 930     -67.787  21.047 -11.531  1.00 27.09           C  
-ANISOU 7141  CE2 TYR C 930     3774   3600   2918    594    103    116       C  
-ATOM   7142  CZ  TYR C 930     -67.167  20.967 -10.307  1.00 29.36           C  
-ANISOU 7142  CZ  TYR C 930     4057   3955   3145    662     95    117       C  
-ATOM   7143  OH  TYR C 930     -66.019  20.230 -10.199  1.00 32.13           O  
-ANISOU 7143  OH  TYR C 930     4406   4355   3446    737     89    126       O  
-ATOM   7144  N   GLU C 931     -69.549  26.201  -9.056  1.00 28.13           N  
-ANISOU 7144  N   GLU C 931     3800   3808   3080    448     58     -8       N  
-ATOM   7145  CA  GLU C 931     -68.807  27.468  -9.186  1.00 30.47           C  
-ANISOU 7145  CA  GLU C 931     4051   4147   3381    410     31    -66       C  
-ATOM   7146  C   GLU C 931     -67.339  27.197  -9.450  1.00 31.34           C  
-ANISOU 7146  C   GLU C 931     4126   4322   3462    432      4    -89       C  
-ATOM   7147  O   GLU C 931     -66.711  26.501  -8.693  1.00 33.97           O  
-ANISOU 7147  O   GLU C 931     4459   4711   3739    495     -5    -82       O  
-ATOM   7148  CB  GLU C 931     -68.951  28.296  -7.932  1.00 33.24           C  
-ANISOU 7148  CB  GLU C 931     4396   4533   3700    416     27    -97       C  
-ATOM   7149  CG  GLU C 931     -70.402  28.523  -7.560  1.00 35.44           C  
-ANISOU 7149  CG  GLU C 931     4709   4755   4002    405     57    -70       C  
-ATOM   7150  CD  GLU C 931     -70.617  29.661  -6.584  1.00 37.75           C  
-ANISOU 7150  CD  GLU C 931     4997   5070   4277    395     55   -110       C  
-ATOM   7151  OE1 GLU C 931     -69.658  30.114  -5.937  1.00 42.54           O  
-ANISOU 7151  OE1 GLU C 931     5578   5743   4843    404     30   -158       O  
-ATOM   7152  OE2 GLU C 931     -71.765  30.082  -6.433  1.00 42.38           O  
-ANISOU 7152  OE2 GLU C 931     5605   5611   4887    379     79    -94       O  
-ATOM   7153  N   LEU C 932     -66.805  27.716 -10.551  1.00 29.56           N  
-ANISOU 7153  N   LEU C 932     3868   4093   3270    384     -8   -113       N  
-ATOM   7154  CA  LEU C 932     -65.441  27.380 -10.965  1.00 29.26           C  
-ANISOU 7154  CA  LEU C 932     3793   4116   3207    404    -31   -129       C  
-ATOM   7155  C   LEU C 932     -64.688  28.642 -11.303  1.00 29.65           C  
-ANISOU 7155  C   LEU C 932     3792   4202   3272    344    -50   -187       C  
-ATOM   7156  O   LEU C 932     -65.271  29.636 -11.740  1.00 29.25           O  
-ANISOU 7156  O   LEU C 932     3743   4102   3267    283    -39   -202       O  
-ATOM   7157  CB  LEU C 932     -65.471  26.471 -12.194  1.00 26.82           C  
-ANISOU 7157  CB  LEU C 932     3503   3762   2926    409    -20    -92       C  
-ATOM   7158  CG  LEU C 932     -66.109  25.104 -11.987  1.00 26.27           C  
-ANISOU 7158  CG  LEU C 932     3488   3649   2843    462      5    -37       C  
-ATOM   7159  CD1 LEU C 932     -66.207  24.342 -13.293  1.00 25.50           C  
-ANISOU 7159  CD1 LEU C 932     3410   3499   2778    453     17    -11       C  
-ATOM   7160  CD2 LEU C 932     -65.312  24.287 -10.965  1.00 27.47           C  
-ANISOU 7160  CD2 LEU C 932     3644   3869   2926    547     -2    -27       C  
-ATOM   7161  N   LYS C 933     -63.402  28.621 -11.024  1.00 32.89           N  
-ANISOU 7161  N   LYS C 933     4155   4701   3639    365    -76   -219       N  
-ATOM   7162  CA  LYS C 933     -62.546  29.794 -11.250  1.00 33.81           C  
-ANISOU 7162  CA  LYS C 933     4218   4864   3765    303    -93   -281       C  
-ATOM   7163  C   LYS C 933     -61.643  29.617 -12.431  1.00 32.20           C  
-ANISOU 7163  C   LYS C 933     3979   4679   3577    288   -100   -282       C  
-ATOM   7164  O   LYS C 933     -61.071  30.583 -12.892  1.00 36.10           O  
-ANISOU 7164  O   LYS C 933     4433   5189   4093    226   -105   -324       O  
-ATOM   7165  CB  LYS C 933     -61.672  30.060 -10.007  1.00 36.29           C  
-ANISOU 7165  CB  LYS C 933     4490   5284   4013    325   -120   -329       C  
-ATOM   7166  CG  LYS C 933     -62.439  30.460  -8.760  1.00 38.11           C  
-ANISOU 7166  CG  LYS C 933     4749   5508   4222    333   -115   -342       C  
-ATOM   7167  CD  LYS C 933     -61.544  30.459  -7.540  1.00 44.57           C  
-ANISOU 7167  CD  LYS C 933     5527   6445   4963    372   -145   -383       C  
-ATOM   7168  CE  LYS C 933     -62.202  29.720  -6.362  1.00 52.09           C  
-ANISOU 7168  CE  LYS C 933     6521   7405   5867    451   -138   -347       C  
-ATOM   7169  NZ  LYS C 933     -61.645  30.208  -5.075  1.00 56.09           N  
-ANISOU 7169  NZ  LYS C 933     6993   8013   6306    465   -164   -403       N  
-ATOM   7170  N   HIS C 934     -61.471  28.383 -12.888  1.00 29.68           N  
-ANISOU 7170  N   HIS C 934     3675   4358   3244    347    -98   -237       N  
-ATOM   7171  CA AHIS C 934     -60.573  28.091 -13.986  0.50 28.43           C  
-ANISOU 7171  CA AHIS C 934     3485   4224   3094    345   -103   -235       C  
-ATOM   7172  CA BHIS C 934     -60.581  28.112 -13.997  0.50 29.90           C  
-ANISOU 7172  CA BHIS C 934     3670   4409   3280    343   -103   -235       C  
-ATOM   7173  C   HIS C 934     -61.170  27.021 -14.890  1.00 28.07           C  
-ANISOU 7173  C   HIS C 934     3489   4105   3072    375    -83   -178       C  
-ATOM   7174  O   HIS C 934     -62.128  26.345 -14.511  1.00 25.22           O  
-ANISOU 7174  O   HIS C 934     3182   3689   2710    406    -66   -141       O  
-ATOM   7175  CB AHIS C 934     -59.215  27.610 -13.462  0.50 29.00           C  
-ANISOU 7175  CB AHIS C 934     3506   4415   3100    402   -129   -252       C  
-ATOM   7176  CB BHIS C 934     -59.129  27.843 -13.529  0.50 32.53           C  
-ANISOU 7176  CB BHIS C 934     3943   4865   3551    387   -131   -262       C  
-ATOM   7177  CG AHIS C 934     -58.645  28.479 -12.386  0.50 28.96           C  
-ANISOU 7177  CG AHIS C 934     3451   4496   3057    381   -152   -311       C  
-ATOM   7178  CG BHIS C 934     -58.877  26.493 -12.931  0.50 34.59           C  
-ANISOU 7178  CG BHIS C 934     4224   5166   3752    491   -134   -223       C  
-ATOM   7179  ND1AHIS C 934     -58.049  29.697 -12.644  0.50 29.14           N  
-ANISOU 7179  ND1AHIS C 934     3421   4551   3101    299   -162   -370       N  
-ATOM   7180  ND1BHIS C 934     -58.582  25.381 -13.690  0.50 35.98           N  
-ANISOU 7180  ND1BHIS C 934     4420   5329   3923    545   -123   -180       N  
-ATOM   7181  CD2AHIS C 934     -58.619  28.323 -11.045  0.50 28.38           C  
-ANISOU 7181  CD2AHIS C 934     3376   4480   2926    428   -166   -322       C  
-ATOM   7182  CD2BHIS C 934     -58.780  26.100 -11.641  0.50 37.06           C  
-ANISOU 7182  CD2BHIS C 934     4541   5537   4004    555   -143   -220       C  
-ATOM   7183  CE1AHIS C 934     -57.667  30.242 -11.505  0.50 27.85           C  
-ANISOU 7183  CE1AHIS C 934     3224   4463   2894    292   -182   -420       C  
-ATOM   7184  CE1BHIS C 934     -58.351  24.357 -12.893  0.50 36.97           C  
-ANISOU 7184  CE1BHIS C 934     4565   5495   3988    639   -123   -151       C  
-ATOM   7185  NE2AHIS C 934     -58.001  29.428 -10.523  0.50 27.71           N  
-ANISOU 7185  NE2AHIS C 934     3236   4466   2827    372   -187   -391       N  
-ATOM   7186  NE2BHIS C 934     -58.471  24.763 -11.643  0.50 36.68           N  
-ANISOU 7186  NE2BHIS C 934     4518   5504   3916    648   -135   -172       N  
-ATOM   7187  N   ALA C 935     -60.592  26.887 -16.073  1.00 26.09           N  
-ANISOU 7187  N   ALA C 935     3218   3855   2840    362    -83   -175       N  
-ATOM   7188  CA  ALA C 935     -61.091  26.002 -17.110  1.00 28.48           C  
-ANISOU 7188  CA  ALA C 935     3564   4089   3168    378    -64   -132       C  
-ATOM   7189  C   ALA C 935     -61.231  24.541 -16.642  1.00 31.66           C  
-ANISOU 7189  C   ALA C 935     4015   4483   3532    462    -54    -90       C  
-ATOM   7190  O   ALA C 935     -60.426  24.045 -15.863  1.00 28.74           O  
-ANISOU 7190  O   ALA C 935     3630   4185   3106    526    -65    -91       O  
-ATOM   7191  CB  ALA C 935     -60.170  26.042 -18.291  1.00 28.37           C  
-ANISOU 7191  CB  ALA C 935     3513   4102   3163    366    -68   -140       C  
-ATOM   7192  N   SER C 936     -62.319  23.911 -17.019  1.00 32.46           N  
-ANISOU 7192  N   SER C 936     4175   4497   3660    459    -30    -55       N  
-ATOM   7193  CA  SER C 936     -62.557  22.600 -16.478  1.00 36.26           C  
-ANISOU 7193  CA  SER C 936     4711   4957   4109    530    -12    -16       C  
-ATOM   7194  C   SER C 936     -63.207  21.692 -17.492  1.00 35.27           C  
-ANISOU 7194  C   SER C 936     4639   4748   4013    526     13     15       C  
-ATOM   7195  O   SER C 936     -64.063  22.104 -18.276  1.00 32.54           O  
-ANISOU 7195  O   SER C 936     4302   4346   3717    462     20     13       O  
-ATOM   7196  CB  SER C 936     -63.355  22.710 -15.166  1.00 41.57           C  
-ANISOU 7196  CB  SER C 936     5408   5618   4767    540     -5     -8       C  
-ATOM   7197  OG  SER C 936     -63.491  21.438 -14.560  1.00 53.79           O  
-ANISOU 7197  OG  SER C 936     7010   7150   6279    614     17     32       O  
-ATOM   7198  N   HIS C 937     -62.723  20.464 -17.550  1.00 35.51           N  
-ANISOU 7198  N   HIS C 937     4705   4778   4011    595     28     41       N  
-ATOM   7199  CA  HIS C 937     -63.457  19.423 -18.255  1.00 37.65           C  
-ANISOU 7199  CA  HIS C 937     5042   4960   4303    595     59     69       C  
-ATOM   7200  C   HIS C 937     -64.750  19.049 -17.543  1.00 40.80           C  
-ANISOU 7200  C   HIS C 937     5496   5292   4714    583     85     94       C  
-ATOM   7201  O   HIS C 937     -64.713  18.494 -16.451  1.00 41.63           O  
-ANISOU 7201  O   HIS C 937     5630   5406   4782    641     99    116       O  
-ATOM   7202  CB  HIS C 937     -62.572  18.203 -18.397  1.00 38.89           C  
-ANISOU 7202  CB  HIS C 937     5232   5129   4418    679     74     91       C  
-ATOM   7203  CG  HIS C 937     -63.307  17.018 -18.888  1.00 39.65           C  
-ANISOU 7203  CG  HIS C 937     5409   5130   4528    685    112    119       C  
-ATOM   7204  ND1 HIS C 937     -63.765  16.942 -20.174  1.00 42.71           N  
-ANISOU 7204  ND1 HIS C 937     5809   5462   4957    629    118    109       N  
-ATOM   7205  CD2 HIS C 937     -63.752  15.910 -18.260  1.00 42.13           C  
-ANISOU 7205  CD2 HIS C 937     5795   5388   4822    731    150    154       C  
-ATOM   7206  CE1 HIS C 937     -64.427  15.814 -20.338  1.00 45.12           C  
-ANISOU 7206  CE1 HIS C 937     6191   5686   5268    637    156    131       C  
-ATOM   7207  NE2 HIS C 937     -64.428  15.164 -19.193  1.00 44.76           N  
-ANISOU 7207  NE2 HIS C 937     6186   5634   5188    698    178    160       N  
-ATOM   7208  N   ILE C 938     -65.878  19.445 -18.138  1.00 50.39           N  
-ANISOU 7208  N   ILE C 938     6717   6448   5979    508     91     89       N  
-ATOM   7209  CA  ILE C 938     -67.190  18.951 -17.759  1.00 54.88           C  
-ANISOU 7209  CA  ILE C 938     7337   6948   6567    486    121    113       C  
-ATOM   7210  C   ILE C 938     -67.793  17.932 -18.749  1.00 60.02           C  
-ANISOU 7210  C   ILE C 938     8041   7522   7242    463    149    126       C  
-ATOM   7211  O   ILE C 938     -68.121  18.276 -19.905  1.00 58.51           O  
-ANISOU 7211  O   ILE C 938     7831   7314   7085    407    140    109       O  
-ATOM   7212  CB  ILE C 938     -68.257  20.088 -17.603  1.00 57.13           C  
-ANISOU 7212  CB  ILE C 938     7593   7225   6890    416    113    101       C  
-ATOM   7213  CG1 ILE C 938     -67.781  21.226 -16.676  1.00 51.80           C  
-ANISOU 7213  CG1 ILE C 938     6869   6616   6196    424     87     80       C  
-ATOM   7214  CG2 ILE C 938     -69.558  19.478 -17.050  1.00 58.61           C  
-ANISOU 7214  CG2 ILE C 938     7829   7351   7088    402    146    129       C  
-ATOM   7215  CD1 ILE C 938     -67.300  20.734 -15.326  1.00 49.86           C  
-ANISOU 7215  CD1 ILE C 938     6640   6406   5897    496     92     94       C  
-ATOM   7216  N   SER C 939     -67.931  16.693 -18.287  1.00 60.62           N  
-ANISOU 7216  N   SER C 939     8183   7553   7296    507    185    155       N  
-ATOM   7217  CA  SER C 939     -68.804  15.671 -18.948  1.00 66.91           C  
-ANISOU 7217  CA  SER C 939     9042   8262   8117    472    222    165       C  
-ATOM   7218  C   SER C 939     -70.171  15.583 -18.251  1.00 68.64           C  
-ANISOU 7218  C   SER C 939     9286   8436   8357    430    248    182       C  
-ATOM   7219  O   SER C 939     -71.176  16.069 -18.780  1.00 67.88           O  
-ANISOU 7219  O   SER C 939     9168   8323   8300    355    243    169       O  
-ATOM   7220  CB  SER C 939     -68.174  14.259 -18.952  1.00 61.55           C  
-ANISOU 7220  CB  SER C 939     8435   7545   7406    542    257    187       C  
-ATOM   7221  N   LYS C 940     -70.177  14.956 -17.068  1.00 62.00           N  
-ANISOU 7221  N   LYS C 940     8490   7583   7486    485    277    214       N  
-ATOM   7222  CA  LYS C 940     -71.326  14.948 -16.167  1.00 59.12           C  
-ANISOU 7222  CA  LYS C 940     8143   7189   7132    458    303    234       C  
-ATOM   7223  C   LYS C 940     -71.110  16.049 -15.130  1.00 54.79           C  
-ANISOU 7223  C   LYS C 940     7542   6712   6563    482    273    231       C  
-ATOM   7224  O   LYS C 940     -70.054  16.092 -14.493  1.00 60.81           O  
-ANISOU 7224  O   LYS C 940     8296   7529   7282    555    259    235       O  
-ATOM   7225  CB  LYS C 940     -71.461  13.577 -15.438  1.00 57.62           C  
-ANISOU 7225  CB  LYS C 940     8039   6936   6917    507    360    275       C  
-ATOM   7226  N   LEU C 941     -72.092  16.936 -14.946  1.00 43.30           N  
-ANISOU 7226  N   LEU C 941     6052   5264   5137    424    264    223       N  
-ATOM   7227  CA  LEU C 941     -72.080  17.808 -13.774  1.00 38.37           C  
-ANISOU 7227  CA  LEU C 941     5396   4692   4491    449    249    223       C  
-ATOM   7228  C   LEU C 941     -72.105  16.951 -12.521  1.00 35.93           C  
-ANISOU 7228  C   LEU C 941     5140   4370   4141    513    285    261       C  
-ATOM   7229  O   LEU C 941     -72.653  15.863 -12.538  1.00 34.91           O  
-ANISOU 7229  O   LEU C 941     5070   4175   4018    511    330    290       O  
-ATOM   7230  CB  LEU C 941     -73.307  18.711 -13.770  1.00 35.78           C  
-ANISOU 7230  CB  LEU C 941     5037   4359   4200    381    246    215       C  
-ATOM   7231  CG  LEU C 941     -73.275  19.888 -14.750  1.00 34.13           C  
-ANISOU 7231  CG  LEU C 941     4768   4176   4023    329    209    180       C  
-ATOM   7232  CD1 LEU C 941     -74.609  20.587 -14.761  1.00 32.01           C  
-ANISOU 7232  CD1 LEU C 941     4478   3896   3788    272    216    181       C  
-ATOM   7233  CD2 LEU C 941     -72.191  20.867 -14.346  1.00 34.77           C  
-ANISOU 7233  CD2 LEU C 941     4806   4324   4079    361    173    154       C  
-ATOM   7234  N   PRO C 942     -71.520  17.433 -11.419  1.00 34.64           N  
-ANISOU 7234  N   PRO C 942     4956   4271   3934    571    268    262       N  
-ATOM   7235  CA  PRO C 942     -71.669  16.702 -10.187  1.00 34.42           C  
-ANISOU 7235  CA  PRO C 942     4977   4236   3866    634    304    302       C  
-ATOM   7236  C   PRO C 942     -73.134  16.567  -9.829  1.00 37.94           C  
-ANISOU 7236  C   PRO C 942     5448   4625   4340    584    342    325       C  
-ATOM   7237  O   PRO C 942     -73.950  17.428 -10.208  1.00 36.26           O  
-ANISOU 7237  O   PRO C 942     5196   4412   4169    513    328    304       O  
-ATOM   7238  CB  PRO C 942     -71.019  17.606  -9.146  1.00 34.26           C  
-ANISOU 7238  CB  PRO C 942     4912   4306   3800    681    270    285       C  
-ATOM   7239  CG  PRO C 942     -70.047  18.434  -9.901  1.00 34.15           C  
-ANISOU 7239  CG  PRO C 942     4837   4347   3792    664    220    239       C  
-ATOM   7240  CD  PRO C 942     -70.611  18.580 -11.284  1.00 35.43           C  
-ANISOU 7240  CD  PRO C 942     4992   4455   4017    583    219    224       C  
-ATOM   7241  N   LYS C 943     -73.437  15.536  -9.037  1.00 39.53           N  
-ANISOU 7241  N   LYS C 943     5714   4788   4518    628    393    370       N  
-ATOM   7242  CA  LYS C 943     -74.807  15.219  -8.673  1.00 37.98           C  
-ANISOU 7242  CA  LYS C 943     5547   4536   4347    582    438    398       C  
-ATOM   7243  C   LYS C 943     -75.367  16.348  -7.869  1.00 33.69           C  
-ANISOU 7243  C   LYS C 943     4957   4043   3800    570    419    388       C  
-ATOM   7244  O   LYS C 943     -74.721  16.856  -6.973  1.00 34.42           O  
-ANISOU 7244  O   LYS C 943     5030   4200   3846    631    397    383       O  
-ATOM   7245  CB  LYS C 943     -74.896  13.918  -7.860  1.00 41.68           C  
-ANISOU 7245  CB  LYS C 943     6099   4954   4784    641    502    452       C  
-ATOM   7246  CG  LYS C 943     -74.630  12.674  -8.671  1.00 43.65           C  
-ANISOU 7246  CG  LYS C 943     6411   5128   5045    641    538    465       C  
-ATOM   7247  CD  LYS C 943     -75.823  12.264  -9.496  1.00 47.78           C  
-ANISOU 7247  CD  LYS C 943     6952   5573   5628    538    570    459       C  
-ATOM   7248  CE  LYS C 943     -75.415  11.091 -10.393  1.00 53.96           C  
-ANISOU 7248  CE  LYS C 943     7799   6282   6420    537    600    461       C  
-ATOM   7249  NZ  LYS C 943     -76.503  10.654 -11.319  1.00 56.61           N  
-ANISOU 7249  NZ  LYS C 943     8149   6546   6812    429    628    445       N  
-ATOM   7250  N   GLY C 944     -76.562  16.780  -8.217  1.00 32.56           N  
-ANISOU 7250  N   GLY C 944     4792   3877   3704    492    427    382       N  
-ATOM   7251  CA  GLY C 944     -77.151  17.918  -7.535  1.00 34.43           C  
-ANISOU 7251  CA  GLY C 944     4984   4158   3938    480    411    372       C  
-ATOM   7252  C   GLY C 944     -76.786  19.296  -8.089  1.00 33.32           C  
-ANISOU 7252  C   GLY C 944     4777   4069   3814    453    355    323       C  
-ATOM   7253  O   GLY C 944     -77.271  20.290  -7.559  1.00 34.74           O  
-ANISOU 7253  O   GLY C 944     4925   4280   3993    443    344    312       O  
-ATOM   7254  N   LYS C 945     -75.899  19.356  -9.088  1.00 30.48           N  
-ANISOU 7254  N   LYS C 945     4401   3716   3465    445    323    295       N  
-ATOM   7255  CA  LYS C 945     -75.586  20.618  -9.775  1.00 29.63           C  
-ANISOU 7255  CA  LYS C 945     4235   3645   3379    410    277    251       C  
-ATOM   7256  C   LYS C 945     -76.299  20.690 -11.108  1.00 26.96           C  
-ANISOU 7256  C   LYS C 945     3880   3270   3094    336    277    243       C  
-ATOM   7257  O   LYS C 945     -76.390  19.706 -11.810  1.00 25.55           O  
-ANISOU 7257  O   LYS C 945     3730   3047   2929    318    296    254       O  
-ATOM   7258  CB  LYS C 945     -74.096  20.744 -10.011  1.00 28.80           C  
-ANISOU 7258  CB  LYS C 945     4113   3582   3246    449    242    225       C  
-ATOM   7259  CG  LYS C 945     -73.285  20.689  -8.744  1.00 28.97           C  
-ANISOU 7259  CG  LYS C 945     4142   3657   3207    526    236    228       C  
-ATOM   7260  CD  LYS C 945     -73.454  21.948  -7.931  1.00 30.66           C  
-ANISOU 7260  CD  LYS C 945     4319   3919   3409    522    216    202       C  
-ATOM   7261  CE  LYS C 945     -72.456  22.002  -6.794  1.00 32.65           C  
-ANISOU 7261  CE  LYS C 945     4568   4243   3596    596    199    192       C  
-ATOM   7262  NZ  LYS C 945     -72.635  23.242  -5.999  1.00 34.62           N  
-ANISOU 7262  NZ  LYS C 945     4786   4537   3832    587    181    159       N  
-ATOM   7263  N   HIS C 946     -76.802  21.868 -11.464  1.00 25.64           N  
-ANISOU 7263  N   HIS C 946     3667   3121   2952    295    258    222       N  
-ATOM   7264  CA  HIS C 946     -77.506  22.000 -12.730  1.00 23.87           C  
-ANISOU 7264  CA  HIS C 946     3422   2874   2773    231    257    215       C  
-ATOM   7265  C   HIS C 946     -76.856  22.902 -13.750  1.00 22.14           C  
-ANISOU 7265  C   HIS C 946     3163   2677   2571    212    220    182       C  
-ATOM   7266  O   HIS C 946     -77.340  23.031 -14.875  1.00 21.67           O  
-ANISOU 7266  O   HIS C 946     3085   2606   2543    166    216    176       O  
-ATOM   7267  CB  HIS C 946     -78.887  22.469 -12.403  1.00 24.78           C  
-ANISOU 7267  CB  HIS C 946     3521   2988   2906    200    276    230       C  
-ATOM   7268  CG  HIS C 946     -79.497  21.679 -11.302  1.00 27.69           C  
-ANISOU 7268  CG  HIS C 946     3927   3339   3256    220    316    264       C  
-ATOM   7269  ND1 HIS C 946     -79.529  22.127 -10.001  1.00 29.72           N  
-ANISOU 7269  ND1 HIS C 946     4188   3622   3483    263    322    272       N  
-ATOM   7270  CD2 HIS C 946     -79.998  20.426 -11.284  1.00 27.90           C  
-ANISOU 7270  CD2 HIS C 946     3993   3322   3287    205    353    291       C  
-ATOM   7271  CE1 HIS C 946     -80.051  21.192  -9.226  1.00 29.12           C  
-ANISOU 7271  CE1 HIS C 946     4150   3521   3392    278    363    308       C  
-ATOM   7272  NE2 HIS C 946     -80.343  20.152  -9.984  1.00 30.91           N  
-ANISOU 7272  NE2 HIS C 946     4400   3703   3642    241    384    320       N  
-ATOM   7273  N   SER C 947     -75.814  23.604 -13.327  1.00 20.94           N  
-ANISOU 7273  N   SER C 947     2996   2564   2397    246    194    159       N  
-ATOM   7274  CA  SER C 947     -75.155  24.553 -14.175  1.00 20.33           C  
-ANISOU 7274  CA  SER C 947     2882   2507   2335    226    165    127       C  
-ATOM   7275  C   SER C 947     -73.765  24.830 -13.673  1.00 20.03           C  
-ANISOU 7275  C   SER C 947     2835   2512   2265    266    141    102       C  
-ATOM   7276  O   SER C 947     -73.415  24.494 -12.558  1.00 21.00           O  
-ANISOU 7276  O   SER C 947     2973   2655   2349    311    144    107       O  
-ATOM   7277  CB  SER C 947     -75.953  25.863 -14.212  1.00 20.45           C  
-ANISOU 7277  CB  SER C 947     2869   2529   2373    196    164    119       C  
-ATOM   7278  OG  SER C 947     -76.020  26.455 -12.951  1.00 20.41           O  
-ANISOU 7278  OG  SER C 947     2865   2544   2344    223    168    113       O  
-ATOM   7279  N   VAL C 948     -72.979  25.479 -14.502  1.00 20.62           N  
-ANISOU 7279  N   VAL C 948     2879   2605   2352    248    118     74       N  
-ATOM   7280  CA  VAL C 948     -71.702  26.014 -14.083  1.00 20.96           C  
-ANISOU 7280  CA  VAL C 948     2899   2698   2368    271     93     42       C  
-ATOM   7281  C   VAL C 948     -71.766  27.539 -14.036  1.00 20.64           C  
-ANISOU 7281  C   VAL C 948     2828   2669   2344    237     85     11       C  
-ATOM   7282  O   VAL C 948     -72.383  28.179 -14.897  1.00 20.86           O  
-ANISOU 7282  O   VAL C 948     2847   2670   2410    197     91     13       O  
-ATOM   7283  CB  VAL C 948     -70.568  25.589 -15.043  1.00 21.41           C  
-ANISOU 7283  CB  VAL C 948     2943   2771   2423    276     76     31       C  
-ATOM   7284  CG1 VAL C 948     -69.309  26.396 -14.789  1.00 21.37           C  
-ANISOU 7284  CG1 VAL C 948     2898   2824   2396    282     50     -8       C  
-ATOM   7285  CG2 VAL C 948     -70.261  24.113 -14.875  1.00 22.10           C  
-ANISOU 7285  CG2 VAL C 948     3066   2850   2482    324     87     58       C  
-ATOM   7286  N   LYS C 949     -71.154  28.111 -13.003  1.00 21.75           N  
-ANISOU 7286  N   LYS C 949     2958   2852   2453    256     73    -17       N  
-ATOM   7287  CA  LYS C 949     -70.910  29.530 -12.937  1.00 21.24           C  
-ANISOU 7287  CA  LYS C 949     2869   2801   2401    223     65    -57       C  
-ATOM   7288  C   LYS C 949     -69.419  29.737 -12.911  1.00 22.18           C  
-ANISOU 7288  C   LYS C 949     2956   2976   2496    227     39    -96       C  
-ATOM   7289  O   LYS C 949     -68.755  29.327 -11.968  1.00 21.99           O  
-ANISOU 7289  O   LYS C 949     2928   3002   2425    267     26   -108       O  
-ATOM   7290  CB  LYS C 949     -71.503  30.153 -11.708  1.00 22.81           C  
-ANISOU 7290  CB  LYS C 949     3080   3004   2582    233     75    -66       C  
-ATOM   7291  CG  LYS C 949     -71.224  31.666 -11.600  1.00 23.98           C  
-ANISOU 7291  CG  LYS C 949     3211   3158   2741    196     73   -113       C  
-ATOM   7292  CD  LYS C 949     -71.836  32.258 -10.357  1.00 24.91           C  
-ANISOU 7292  CD  LYS C 949     3347   3279   2839    210     85   -125       C  
-ATOM   7293  CE  LYS C 949     -71.540  33.747 -10.283  1.00 27.61           C  
-ANISOU 7293  CE  LYS C 949     3681   3617   3193    170     88   -176       C  
-ATOM   7294  NZ  LYS C 949     -71.965  34.312  -8.970  1.00 29.03           N  
-ANISOU 7294  NZ  LYS C 949     3879   3807   3344    187     97   -197       N  
-ATOM   7295  N   GLY C 950     -68.891  30.393 -13.952  1.00 21.06           N  
-ANISOU 7295  N   GLY C 950     2788   2829   2383    186     34   -116       N  
-ATOM   7296  CA  GLY C 950     -67.518  30.834 -13.942  1.00 22.55           C  
-ANISOU 7296  CA  GLY C 950     2940   3074   2554    175     12   -160       C  
-ATOM   7297  C   GLY C 950     -67.452  32.113 -13.148  1.00 24.14           C  
-ANISOU 7297  C   GLY C 950     3132   3288   2752    145     13   -206       C  
-ATOM   7298  O   GLY C 950     -68.142  33.073 -13.464  1.00 26.18           O  
-ANISOU 7298  O   GLY C 950     3403   3498   3047    108     33   -209       O  
-ATOM   7299  N   LEU C 951     -66.628  32.137 -12.115  1.00 24.90           N  
-ANISOU 7299  N   LEU C 951     3208   3452   2802    164     -7   -242       N  
-ATOM   7300  CA  LEU C 951     -66.611  33.267 -11.159  1.00 25.89           C  
-ANISOU 7300  CA  LEU C 951     3331   3593   2915    139     -6   -292       C  
-ATOM   7301  C   LEU C 951     -65.730  34.424 -11.607  1.00 26.31           C  
-ANISOU 7301  C   LEU C 951     3351   3659   2987     74     -8   -348       C  
-ATOM   7302  O   LEU C 951     -64.516  34.258 -11.729  1.00 25.56           O  
-ANISOU 7302  O   LEU C 951     3212   3630   2870     69    -31   -376       O  
-ATOM   7303  CB  LEU C 951     -66.091  32.785  -9.811  1.00 26.16           C  
-ANISOU 7303  CB  LEU C 951     3353   3703   2881    188    -28   -312       C  
-ATOM   7304  CG  LEU C 951     -66.958  31.726  -9.168  1.00 27.43           C  
-ANISOU 7304  CG  LEU C 951     3552   3850   3019    252    -18   -258       C  
-ATOM   7305  CD1 LEU C 951     -66.374  31.289  -7.827  1.00 29.77           C  
-ANISOU 7305  CD1 LEU C 951     3838   4229   3243    308    -38   -276       C  
-ATOM   7306  CD2 LEU C 951     -68.350  32.253  -8.963  1.00 26.06           C  
-ANISOU 7306  CD2 LEU C 951     3419   3607   2876    237     11   -240       C  
-ATOM   7307  N   GLY C 952     -66.344  35.571 -11.902  1.00 25.44           N  
-ANISOU 7307  N   GLY C 952     3262   3486   2918     26     19   -360       N  
-ATOM   7308  CA  GLY C 952     -65.572  36.761 -12.286  1.00 28.57           C  
-ANISOU 7308  CA  GLY C 952     3637   3882   3337    -42     26   -414       C  
-ATOM   7309  C   GLY C 952     -65.017  37.547 -11.110  1.00 31.15           C  
-ANISOU 7309  C   GLY C 952     3953   4254   3630    -68     18   -485       C  
-ATOM   7310  O   GLY C 952     -65.485  37.384  -9.993  1.00 29.68           O  
-ANISOU 7310  O   GLY C 952     3785   4085   3409    -32     12   -490       O  
-ATOM   7311  N   LYS C 953     -64.040  38.416 -11.377  1.00 35.18           N  
-ANISOU 7311  N   LYS C 953     4432   4784   4151   -133     19   -542       N  
-ATOM   7312  CA  LYS C 953     -63.557  39.394 -10.392  1.00 38.97           C  
-ANISOU 7312  CA  LYS C 953     4904   5295   4607   -178     18   -621       C  
-ATOM   7313  C   LYS C 953     -64.578  40.507 -10.136  1.00 36.33           C  
-ANISOU 7313  C   LYS C 953     4631   4870   4304   -204     60   -631       C  
-ATOM   7314  O   LYS C 953     -64.597  41.092  -9.067  1.00 40.22           O  
-ANISOU 7314  O   LYS C 953     5135   5377   4768   -217     60   -684       O  
-ATOM   7315  CB  LYS C 953     -62.252  40.039 -10.849  1.00 45.09           C  
-ANISOU 7315  CB  LYS C 953     5630   6111   5392   -252     14   -681       C  
-ATOM   7316  CG  LYS C 953     -61.115  39.047 -10.974  1.00 52.16           C  
-ANISOU 7316  CG  LYS C 953     6458   7113   6248   -226    -27   -681       C  
-ATOM   7317  CD  LYS C 953     -59.807  39.712 -11.386  1.00 59.08           C  
-ANISOU 7317  CD  LYS C 953     7277   8041   7131   -303    -30   -743       C  
-ATOM   7318  CE  LYS C 953     -58.706  38.700 -11.647  1.00 63.39           C  
-ANISOU 7318  CE  LYS C 953     7753   8694   7639   -269    -67   -734       C  
-ATOM   7319  NZ  LYS C 953     -57.939  38.352 -10.418  1.00 67.71           N  
-ANISOU 7319  NZ  LYS C 953     8249   9367   8110   -242   -110   -784       N  
-ATOM   7320  N   THR C 954     -65.414  40.784 -11.122  1.00 32.21           N  
-ANISOU 7320  N   THR C 954     4145   4258   3834   -207     94   -580       N  
-ATOM   7321  CA  THR C 954     -66.427  41.793 -11.023  1.00 31.97           C  
-ANISOU 7321  CA  THR C 954     4174   4140   3834   -219    138   -578       C  
-ATOM   7322  C   THR C 954     -67.779  41.125 -11.213  1.00 34.12           C  
-ANISOU 7322  C   THR C 954     4478   4372   4116   -154    147   -499       C  
-ATOM   7323  O   THR C 954     -67.953  40.267 -12.090  1.00 37.80           O  
-ANISOU 7323  O   THR C 954     4929   4837   4596   -127    138   -443       O  
-ATOM   7324  CB  THR C 954     -66.200  42.874 -12.087  1.00 31.76           C  
-ANISOU 7324  CB  THR C 954     4161   4045   3861   -283    179   -587       C  
-ATOM   7325  OG1 THR C 954     -64.912  43.488 -11.881  1.00 30.92           O  
-ANISOU 7325  OG1 THR C 954     4021   3979   3747   -355    173   -666       O  
-ATOM   7326  CG2 THR C 954     -67.300  43.952 -12.061  1.00 31.49           C  
-ANISOU 7326  CG2 THR C 954     4195   3913   3858   -286    232   -577       C  
-ATOM   7327  N   THR C 955     -68.731  41.493 -10.367  1.00 32.79           N  
-ANISOU 7327  N   THR C 955     4350   4173   3936   -128    166   -498       N  
-ATOM   7328  CA  THR C 955     -70.072  40.954 -10.407  1.00 32.45           C  
-ANISOU 7328  CA  THR C 955     4334   4098   3899    -70    178   -429       C  
-ATOM   7329  C   THR C 955     -71.069  42.119 -10.284  1.00 33.16           C  
-ANISOU 7329  C   THR C 955     4477   4110   4011    -73    226   -427       C  
-ATOM   7330  O   THR C 955     -70.745  43.089  -9.663  1.00 32.56           O  
-ANISOU 7330  O   THR C 955     4422   4021   3929   -106    242   -487       O  
-ATOM   7331  CB  THR C 955     -70.277  39.928  -9.280  1.00 32.09           C  
-ANISOU 7331  CB  THR C 955     4280   4111   3801    -16    148   -419       C  
-ATOM   7332  OG1 THR C 955     -71.541  39.295  -9.431  1.00 32.87           O  
-ANISOU 7332  OG1 THR C 955     4398   4181   3909     32    161   -350       O  
-ATOM   7333  CG2 THR C 955     -70.223  40.565  -7.878  1.00 32.87           C  
-ANISOU 7333  CG2 THR C 955     4398   4232   3861    -15    150   -477       C  
-ATOM   7334  N   PRO C 956     -72.287  42.002 -10.855  1.00 33.78           N  
-ANISOU 7334  N   PRO C 956     4577   4144   4115    -37    250   -361       N  
-ATOM   7335  CA  PRO C 956     -73.304  42.980 -10.560  1.00 32.55           C  
-ANISOU 7335  CA  PRO C 956     4470   3929   3970    -22    295   -354       C  
-ATOM   7336  C   PRO C 956     -73.620  43.013  -9.082  1.00 32.03           C  
-ANISOU 7336  C   PRO C 956     4423   3886   3861      5    291   -384       C  
-ATOM   7337  O   PRO C 956     -73.682  41.969  -8.449  1.00 31.60           O  
-ANISOU 7337  O   PRO C 956     4347   3887   3772     39    260   -369       O  
-ATOM   7338  CB  PRO C 956     -74.518  42.473 -11.343  1.00 34.63           C  
-ANISOU 7338  CB  PRO C 956     4733   4172   4253     22    307   -273       C  
-ATOM   7339  CG  PRO C 956     -73.915  41.686 -12.461  1.00 33.71           C  
-ANISOU 7339  CG  PRO C 956     4577   4077   4154      5    281   -250       C  
-ATOM   7340  CD  PRO C 956     -72.798  40.967 -11.776  1.00 33.83           C  
-ANISOU 7340  CD  PRO C 956     4562   4157   4136     -8    238   -292       C  
-ATOM   7341  N   ASP C 957     -73.787  44.213  -8.541  1.00 31.94           N  
-ANISOU 7341  N   ASP C 957     4455   3831   3849     -9    326   -426       N  
-ATOM   7342  CA  ASP C 957     -74.047  44.402  -7.131  1.00 33.67           C  
-ANISOU 7342  CA  ASP C 957     4697   4070   4025     14    327   -462       C  
-ATOM   7343  C   ASP C 957     -75.273  43.611  -6.704  1.00 33.68           C  
-ANISOU 7343  C   ASP C 957     4701   4088   4008     84    327   -398       C  
-ATOM   7344  O   ASP C 957     -76.380  43.951  -7.077  1.00 34.86           O  
-ANISOU 7344  O   ASP C 957     4875   4191   4179    114    363   -349       O  
-ATOM   7345  CB  ASP C 957     -74.247  45.873  -6.873  1.00 35.78           C  
-ANISOU 7345  CB  ASP C 957     5022   4267   4305     -9    377   -506       C  
-ATOM   7346  CG  ASP C 957     -74.381  46.213  -5.401  1.00 38.36           C  
-ANISOU 7346  CG  ASP C 957     5377   4614   4584      8    379   -559       C  
-ATOM   7347  OD1 ASP C 957     -74.575  45.311  -4.557  1.00 40.42           O  
-ANISOU 7347  OD1 ASP C 957     5616   4940   4802     50    347   -546       O  
-ATOM   7348  OD2 ASP C 957     -74.256  47.413  -5.098  1.00 40.37           O  
-ANISOU 7348  OD2 ASP C 957     5680   4816   4844    -24    416   -615       O  
-ATOM   7349  N   PRO C 958     -75.080  42.563  -5.893  1.00 36.79           N  
-ANISOU 7349  N   PRO C 958     5068   4551   4359    111    290   -396       N  
-ATOM   7350  CA  PRO C 958     -76.211  41.735  -5.421  1.00 40.11           C  
-ANISOU 7350  CA  PRO C 958     5490   4989   4762    173    293   -335       C  
-ATOM   7351  C   PRO C 958     -77.331  42.497  -4.713  1.00 42.11           C  
-ANISOU 7351  C   PRO C 958     5787   5208   5004    209    335   -328       C  
-ATOM   7352  O   PRO C 958     -78.483  42.061  -4.763  1.00 45.51           O  
-ANISOU 7352  O   PRO C 958     6218   5635   5439    252    352   -265       O  
-ATOM   7353  CB  PRO C 958     -75.570  40.778  -4.431  1.00 40.44           C  
-ANISOU 7353  CB  PRO C 958     5508   5106   4750    192    254   -354       C  
-ATOM   7354  CG  PRO C 958     -74.116  40.786  -4.755  1.00 40.27           C  
-ANISOU 7354  CG  PRO C 958     5456   5117   4726    145    221   -406       C  
-ATOM   7355  CD  PRO C 958     -73.803  42.139  -5.301  1.00 37.60           C  
-ANISOU 7355  CD  PRO C 958     5139   4722   4424     90    247   -452       C  
-ATOM   7356  N   SER C 959     -77.023  43.616  -4.065  1.00 39.89           N  
-ANISOU 7356  N   SER C 959     5541   4904   4709    191    354   -393       N  
-ATOM   7357  CA  SER C 959     -78.054  44.347  -3.341  1.00 40.54           C  
-ANISOU 7357  CA  SER C 959     5670   4955   4778    231    395   -390       C  
-ATOM   7358  C   SER C 959     -79.002  45.080  -4.308  1.00 41.00           C  
-ANISOU 7358  C   SER C 959     5753   4941   4882    243    443   -342       C  
-ATOM   7359  O   SER C 959     -80.112  45.461  -3.907  1.00 44.48           O  
-ANISOU 7359  O   SER C 959     6224   5362   5315    292    480   -313       O  
-ATOM   7360  CB  SER C 959     -77.424  45.289  -2.330  1.00 43.55           C  
-ANISOU 7360  CB  SER C 959     6087   5334   5127    207    402   -479       C  
-ATOM   7361  OG  SER C 959     -76.859  46.412  -2.969  1.00 49.38           O  
-ANISOU 7361  OG  SER C 959     6852   6010   5902    151    426   -526       O  
-ATOM   7362  N   ALA C 960     -78.598  45.239  -5.577  1.00 34.89           N  
-ANISOU 7362  N   ALA C 960     4967   4137   4153    206    444   -329       N  
-ATOM   7363  CA  ALA C 960     -79.472  45.808  -6.598  1.00 33.87           C  
-ANISOU 7363  CA  ALA C 960     4855   3952   4064    225    486   -276       C  
-ATOM   7364  C   ALA C 960     -80.203  44.771  -7.467  1.00 31.16           C  
-ANISOU 7364  C   ALA C 960     4465   3639   3737    251    471   -195       C  
-ATOM   7365  O   ALA C 960     -80.960  45.137  -8.343  1.00 30.46           O  
-ANISOU 7365  O   ALA C 960     4381   3520   3674    272    500   -146       O  
-ATOM   7366  CB  ALA C 960     -78.682  46.752  -7.489  1.00 36.22           C  
-ANISOU 7366  CB  ALA C 960     5173   4192   4398    172    506   -308       C  
-ATOM   7367  N   ASN C 961     -80.015  43.494  -7.206  1.00 30.18           N  
-ANISOU 7367  N   ASN C 961     4299   3574   3594    253    428   -180       N  
-ATOM   7368  CA  ASN C 961     -80.789  42.467  -7.871  1.00 32.70           C  
-ANISOU 7368  CA  ASN C 961     4580   3921   3925    274    417   -110       C  
-ATOM   7369  C   ASN C 961     -82.255  42.661  -7.624  1.00 30.33           C  
-ANISOU 7369  C   ASN C 961     4288   3617   3618    327    453    -61       C  
-ATOM   7370  O   ASN C 961     -82.646  43.055  -6.517  1.00 31.01           O  
-ANISOU 7370  O   ASN C 961     4403   3704   3675    358    473    -77       O  
-ATOM   7371  CB  ASN C 961     -80.391  41.080  -7.381  1.00 37.65           C  
-ANISOU 7371  CB  ASN C 961     5174   4604   4526    272    375   -106       C  
-ATOM   7372  CG  ASN C 961     -81.151  40.005  -8.093  1.00 46.72           C  
-ANISOU 7372  CG  ASN C 961     6288   5774   5689    283    368    -41       C  
-ATOM   7373  OD1 ASN C 961     -80.877  39.720  -9.265  1.00 55.89           O  
-ANISOU 7373  OD1 ASN C 961     7426   6929   6879    257    355    -25       O  
-ATOM   7374  ND2 ASN C 961     -82.145  39.422  -7.423  1.00 51.49           N  
-ANISOU 7374  ND2 ASN C 961     6887   6403   6274    319    378     -4       N  
-ATOM   7375  N   ILE C 962     -83.082  42.429  -8.643  1.00 27.29           N  
-ANISOU 7375  N   ILE C 962     3877   3234   3256    340    463     -2       N  
-ATOM   7376  CA  ILE C 962     -84.517  42.452  -8.427  1.00 27.78           C  
-ANISOU 7376  CA  ILE C 962     3935   3313   3310    391    494     50       C  
-ATOM   7377  C   ILE C 962     -85.123  41.122  -8.860  1.00 27.78           C  
-ANISOU 7377  C   ILE C 962     3881   3362   3312    389    471    101       C  
-ATOM   7378  O   ILE C 962     -84.561  40.453  -9.696  1.00 27.75           O  
-ANISOU 7378  O   ILE C 962     3851   3365   3326    353    442    104       O  
-ATOM   7379  CB  ILE C 962     -85.209  43.604  -9.148  1.00 28.77           C  
-ANISOU 7379  CB  ILE C 962     4079   3401   3453    421    538     75       C  
-ATOM   7380  CG1 ILE C 962     -85.125  43.456 -10.656  1.00 29.64           C  
-ANISOU 7380  CG1 ILE C 962     4159   3509   3594    401    528    106       C  
-ATOM   7381  CG2 ILE C 962     -84.655  44.939  -8.650  1.00 28.99           C  
-ANISOU 7381  CG2 ILE C 962     4170   3367   3477    421    569     22       C  
-ATOM   7382  CD1 ILE C 962     -86.045  44.399 -11.375  1.00 31.71           C  
-ANISOU 7382  CD1 ILE C 962     4430   3752   3865    447    573    148       C  
-ATOM   7383  N   SER C 963     -86.263  40.762  -8.280  1.00 25.87           N  
-ANISOU 7383  N   SER C 963     3625   3152   3051    425    489    139       N  
-ATOM   7384  CA  SER C 963     -86.981  39.561  -8.658  1.00 25.73           C  
-ANISOU 7384  CA  SER C 963     3558   3179   3037    417    477    186       C  
-ATOM   7385  C   SER C 963     -88.279  39.920  -9.408  1.00 27.34           C  
-ANISOU 7385  C   SER C 963     3732   3404   3251    446    505    238       C  
-ATOM   7386  O   SER C 963     -89.085  40.739  -8.944  1.00 26.39           O  
-ANISOU 7386  O   SER C 963     3627   3284   3117    494    542    253       O  
-ATOM   7387  CB  SER C 963     -87.279  38.707  -7.438  1.00 24.82           C  
-ANISOU 7387  CB  SER C 963     3442   3095   2892    429    476    193       C  
-ATOM   7388  OG  SER C 963     -88.298  37.760  -7.744  1.00 24.17           O  
-ANISOU 7388  OG  SER C 963     3315   3052   2814    426    481    244       O  
-ATOM   7389  N   LEU C 964     -88.435  39.328 -10.588  1.00 27.11           N  
-ANISOU 7389  N   LEU C 964     3661   3395   3243    419    487    263       N  
-ATOM   7390  CA  LEU C 964     -89.496  39.665 -11.510  1.00 29.59           C  
-ANISOU 7390  CA  LEU C 964     3940   3739   3564    442    506    308       C  
-ATOM   7391  C   LEU C 964     -90.178  38.378 -11.957  1.00 29.81           C  
-ANISOU 7391  C   LEU C 964     3909   3823   3594    412    488    340       C  
-ATOM   7392  O   LEU C 964     -89.570  37.513 -12.598  1.00 30.92           O  
-ANISOU 7392  O   LEU C 964     4035   3963   3750    364    456    329       O  
-ATOM   7393  CB  LEU C 964     -88.818  40.450 -12.637  1.00 31.34           C  
-ANISOU 7393  CB  LEU C 964     4176   3925   3808    435    503    296       C  
-ATOM   7394  CG  LEU C 964     -89.436  41.535 -13.494  1.00 36.31           C  
-ANISOU 7394  CG  LEU C 964     4804   4552   4441    479    534    327       C  
-ATOM   7395  CD1 LEU C 964     -89.862  42.711 -12.605  1.00 35.62           C  
-ANISOU 7395  CD1 LEU C 964     4763   4434   4336    537    581    326       C  
-ATOM   7396  CD2 LEU C 964     -88.455  42.046 -14.563  1.00 37.47           C  
-ANISOU 7396  CD2 LEU C 964     4970   4656   4611    457    526    310       C  
-ATOM   7397  N   ASP C 965     -91.415  38.194 -11.523  1.00 30.83           N  
-ANISOU 7397  N   ASP C 965     4007   3999   3707    437    511    375       N  
-ATOM   7398  CA  ASP C 965     -92.141  36.970 -11.840  1.00 33.66           C  
-ANISOU 7398  CA  ASP C 965     4310   4412   4068    401    500    401       C  
-ATOM   7399  C   ASP C 965     -91.297  35.707 -11.451  1.00 30.31           C  
-ANISOU 7399  C   ASP C 965     3901   3966   3650    348    473    377       C  
-ATOM   7400  O   ASP C 965     -91.273  34.717 -12.157  1.00 29.34           O  
-ANISOU 7400  O   ASP C 965     3750   3858   3540    301    453    380       O  
-ATOM   7401  CB  ASP C 965     -92.486  36.949 -13.344  1.00 37.14           C  
-ANISOU 7401  CB  ASP C 965     4703   4887   4522    386    487    419       C  
-ATOM   7402  CG  ASP C 965     -93.657  35.986 -13.702  1.00 43.07           C  
-ANISOU 7402  CG  ASP C 965     5384   5713   5268    357    487    450       C  
-ATOM   7403  OD1 ASP C 965     -94.087  35.981 -14.885  1.00 56.08           O  
-ANISOU 7403  OD1 ASP C 965     6985   7405   6920    348    476    465       O  
-ATOM   7404  OD2 ASP C 965     -94.160  35.227 -12.853  1.00 44.63           O  
-ANISOU 7404  OD2 ASP C 965     5570   5929   5458    341    499    459       O  
-ATOM   7405  N   GLY C 966     -90.637  35.750 -10.301  1.00 28.85           N  
-ANISOU 7405  N   GLY C 966     3763   3748   3451    361    475    353       N  
-ATOM   7406  CA  GLY C 966     -89.882  34.604  -9.797  1.00 29.09           C  
-ANISOU 7406  CA  GLY C 966     3812   3763   3480    328    456    336       C  
-ATOM   7407  C   GLY C 966     -88.498  34.449 -10.430  1.00 27.65           C  
-ANISOU 7407  C   GLY C 966     3650   3544   3312    298    420    300       C  
-ATOM   7408  O   GLY C 966     -87.792  33.549 -10.100  1.00 31.18           O  
-ANISOU 7408  O   GLY C 966     4113   3979   3755    278    403    287       O  
-ATOM   7409  N   VAL C 967     -88.073  35.389 -11.258  1.00 27.23           N  
-ANISOU 7409  N   VAL C 967     3601   3473   3273    302    412    285       N  
-ATOM   7410  CA  VAL C 967     -86.744  35.361 -11.851  1.00 25.78           C  
-ANISOU 7410  CA  VAL C 967     3434   3258   3103    276    382    251       C  
-ATOM   7411  C   VAL C 967     -85.867  36.546 -11.387  1.00 25.90           C  
-ANISOU 7411  C   VAL C 967     3490   3238   3114    295    385    212       C  
-ATOM   7412  O   VAL C 967     -86.298  37.691 -11.358  1.00 25.69           O  
-ANISOU 7412  O   VAL C 967     3475   3199   3086    325    411    215       O  
-ATOM   7413  CB  VAL C 967     -86.887  35.450 -13.372  1.00 24.85           C  
-ANISOU 7413  CB  VAL C 967     3285   3149   3008    255    372    264       C  
-ATOM   7414  CG1 VAL C 967     -85.555  35.364 -14.067  1.00 24.99           C  
-ANISOU 7414  CG1 VAL C 967     3315   3139   3040    228    343    232       C  
-ATOM   7415  CG2 VAL C 967     -87.878  34.414 -13.862  1.00 24.96           C  
-ANISOU 7415  CG2 VAL C 967     3254   3204   3025    232    371    296       C  
-ATOM   7416  N   ASP C 968     -84.636  36.271 -11.021  1.00 26.68           N  
-ANISOU 7416  N   ASP C 968     3611   3321   3207    278    361    174       N  
-ATOM   7417  CA  ASP C 968     -83.723  37.334 -10.682  1.00 27.37           C  
-ANISOU 7417  CA  ASP C 968     3730   3378   3290    283    362    130       C  
-ATOM   7418  C   ASP C 968     -83.179  38.062 -11.924  1.00 28.06           C  
-ANISOU 7418  C   ASP C 968     3816   3441   3406    261    358    119       C  
-ATOM   7419  O   ASP C 968     -82.811  37.439 -12.912  1.00 26.24           O  
-ANISOU 7419  O   ASP C 968     3562   3215   3191    234    337    127       O  
-ATOM   7420  CB  ASP C 968     -82.568  36.753  -9.887  1.00 30.99           C  
-ANISOU 7420  CB  ASP C 968     4203   3843   3728    272    335     92       C  
-ATOM   7421  CG  ASP C 968     -82.983  36.273  -8.498  1.00 36.34           C  
-ANISOU 7421  CG  ASP C 968     4895   4543   4371    302    344     98       C  
-ATOM   7422  OD1 ASP C 968     -83.944  36.799  -7.905  1.00 40.07           O  
-ANISOU 7422  OD1 ASP C 968     5375   5017   4832    332    374    114       O  
-ATOM   7423  OD2 ASP C 968     -82.320  35.357  -7.979  1.00 44.26           O  
-ANISOU 7423  OD2 ASP C 968     5899   5563   5353    300    323     89       O  
-ATOM   7424  N   VAL C 969     -83.124  39.389 -11.843  1.00 28.09           N  
-ANISOU 7424  N   VAL C 969     3848   3411   3414    275    384    101       N  
-ATOM   7425  CA  VAL C 969     -82.467  40.212 -12.822  1.00 27.90           C  
-ANISOU 7425  CA  VAL C 969     3833   3353   3414    256    388     86       C  
-ATOM   7426  C   VAL C 969     -81.311  40.892 -12.114  1.00 29.25           C  
-ANISOU 7426  C   VAL C 969     4038   3496   3578    236    386     25       C  
-ATOM   7427  O   VAL C 969     -81.521  41.817 -11.315  1.00 29.67           O  
-ANISOU 7427  O   VAL C 969     4128   3525   3621    255    415      4       O  
-ATOM   7428  CB  VAL C 969     -83.408  41.270 -13.376  1.00 27.57           C  
-ANISOU 7428  CB  VAL C 969     3801   3291   3383    290    430    118       C  
-ATOM   7429  CG1 VAL C 969     -82.744  41.985 -14.545  1.00 27.21           C  
-ANISOU 7429  CG1 VAL C 969     3765   3211   3364    270    437    112       C  
-ATOM   7430  CG2 VAL C 969     -84.714  40.617 -13.825  1.00 27.68           C  
-ANISOU 7430  CG2 VAL C 969     3774   3350   3394    314    432    175       C  
-ATOM   7431  N   PRO C 970     -80.083  40.441 -12.385  1.00 28.67           N  
-ANISOU 7431  N   PRO C 970     3953   3430   3509    197    354     -7       N  
-ATOM   7432  CA  PRO C 970     -78.919  41.031 -11.726  1.00 30.15           C  
-ANISOU 7432  CA  PRO C 970     4163   3605   3687    170    348    -71       C  
-ATOM   7433  C   PRO C 970     -78.463  42.332 -12.399  1.00 30.49           C  
-ANISOU 7433  C   PRO C 970     4231   3596   3757    146    377    -94       C  
-ATOM   7434  O   PRO C 970     -77.377  42.385 -12.969  1.00 32.69           O  
-ANISOU 7434  O   PRO C 970     4499   3871   4050    105    361   -122       O  
-ATOM   7435  CB  PRO C 970     -77.851  39.934 -11.879  1.00 28.99           C  
-ANISOU 7435  CB  PRO C 970     3985   3497   3534    144    303    -87       C  
-ATOM   7436  CG  PRO C 970     -78.178  39.336 -13.201  1.00 29.01           C  
-ANISOU 7436  CG  PRO C 970     3961   3502   3561    140    296    -41       C  
-ATOM   7437  CD  PRO C 970     -79.683  39.419 -13.361  1.00 28.29           C  
-ANISOU 7437  CD  PRO C 970     3869   3405   3474    175    323     11       C  
-ATOM   7438  N   LEU C 971     -79.249  43.378 -12.254  1.00 29.08           N  
-ANISOU 7438  N   LEU C 971     4089   3376   3584    172    421    -84       N  
-ATOM   7439  CA  LEU C 971     -78.998  44.614 -12.941  1.00 31.10           C  
-ANISOU 7439  CA  LEU C 971     4377   3573   3866    157    460    -94       C  
-ATOM   7440  C   LEU C 971     -78.195  45.650 -12.140  1.00 31.11           C  
-ANISOU 7440  C   LEU C 971     4423   3534   3863    124    480   -166       C  
-ATOM   7441  O   LEU C 971     -78.055  46.795 -12.552  1.00 31.92           O  
-ANISOU 7441  O   LEU C 971     4566   3575   3987    111    523   -178       O  
-ATOM   7442  CB  LEU C 971     -80.314  45.226 -13.465  1.00 31.28           C  
-ANISOU 7442  CB  LEU C 971     4417   3569   3897    210    504    -36       C  
-ATOM   7443  CG  LEU C 971     -81.489  45.342 -12.541  1.00 32.57           C  
-ANISOU 7443  CG  LEU C 971     4597   3742   4037    264    526    -15       C  
-ATOM   7444  CD1 LEU C 971     -81.138  46.219 -11.364  1.00 34.38           C  
-ANISOU 7444  CD1 LEU C 971     4878   3933   4251    259    549    -74       C  
-ATOM   7445  CD2 LEU C 971     -82.665  45.902 -13.310  1.00 34.76           C  
-ANISOU 7445  CD2 LEU C 971     4880   4005   4324    318    567     47       C  
-ATOM   7446  N   GLY C 972     -77.609  45.242 -11.038  1.00 31.84           N  
-ANISOU 7446  N   GLY C 972     4509   3663   3927    108    449   -215       N  
-ATOM   7447  CA  GLY C 972     -76.679  46.121 -10.324  1.00 32.65           C  
-ANISOU 7447  CA  GLY C 972     4642   3740   4021     64    460   -294       C  
-ATOM   7448  C   GLY C 972     -75.433  46.496 -11.129  1.00 33.32           C  
-ANISOU 7448  C   GLY C 972     4718   3808   4134     -3    457   -331       C  
-ATOM   7449  O   GLY C 972     -74.991  45.737 -11.979  1.00 32.28           O  
-ANISOU 7449  O   GLY C 972     4543   3707   4014    -16    427   -306       O  
-ATOM   7450  N   THR C 973     -74.854  47.659 -10.849  1.00 35.84           N  
-ANISOU 7450  N   THR C 973     5079   4078   4462    -47    490   -392       N  
-ATOM   7451  CA  THR C 973     -73.556  48.016 -11.430  1.00 35.80           C  
-ANISOU 7451  CA  THR C 973     5060   4063   4478   -121    487   -438       C  
-ATOM   7452  C   THR C 973     -72.476  47.058 -10.955  1.00 35.38           C  
-ANISOU 7452  C   THR C 973     4947   4098   4396   -152    424   -480       C  
-ATOM   7453  O   THR C 973     -72.548  46.542  -9.859  1.00 32.71           O  
-ANISOU 7453  O   THR C 973     4598   3812   4018   -129    394   -502       O  
-ATOM   7454  CB  THR C 973     -73.125  49.474 -11.112  1.00 39.70           C  
-ANISOU 7454  CB  THR C 973     5614   4484   4986   -173    540   -505       C  
-ATOM   7455  OG1 THR C 973     -73.156  49.695  -9.704  1.00 44.90           O  
-ANISOU 7455  OG1 THR C 973     6295   5159   5607   -172    534   -565       O  
-ATOM   7456  CG2 THR C 973     -74.044  50.486 -11.779  1.00 40.90           C  
-ANISOU 7456  CG2 THR C 973     5830   4541   5170   -141    611   -458       C  
-ATOM   7457  N   GLY C 974     -71.449  46.884 -11.771  1.00 37.26           N  
-ANISOU 7457  N   GLY C 974     5149   4354   4653   -200    408   -492       N  
-ATOM   7458  CA  GLY C 974     -70.330  46.005 -11.455  1.00 39.63           C  
-ANISOU 7458  CA  GLY C 974     5389   4743   4927   -226    351   -529       C  
-ATOM   7459  C   GLY C 974     -69.464  46.446 -10.287  1.00 41.11           C  
-ANISOU 7459  C   GLY C 974     5573   4966   5081   -272    337   -622       C  
-ATOM   7460  O   GLY C 974     -68.961  47.563 -10.262  1.00 44.38           O  
-ANISOU 7460  O   GLY C 974     6015   5337   5513   -334    371   -680       O  
-ATOM   7461  N   ILE C 975     -69.316  45.555  -9.312  1.00 39.79           N  
-ANISOU 7461  N   ILE C 975     5373   4881   4864   -240    290   -635       N  
-ATOM   7462  CA  ILE C 975     -68.470  45.770  -8.155  1.00 40.56           C  
-ANISOU 7462  CA  ILE C 975     5455   5038   4917   -273    266   -721       C  
-ATOM   7463  C   ILE C 975     -67.576  44.566  -8.005  1.00 40.34           C  
-ANISOU 7463  C   ILE C 975     5356   5118   4852   -260    205   -724       C  
-ATOM   7464  O   ILE C 975     -67.754  43.547  -8.682  1.00 38.37           O  
-ANISOU 7464  O   ILE C 975     5082   4886   4610   -219    186   -657       O  
-ATOM   7465  CB  ILE C 975     -69.276  45.938  -6.845  1.00 43.08           C  
-ANISOU 7465  CB  ILE C 975     5813   5358   5197   -230    272   -738       C  
-ATOM   7466  CG1 ILE C 975     -69.982  44.644  -6.456  1.00 42.70           C  
-ANISOU 7466  CG1 ILE C 975     5748   5360   5118   -146    240   -672       C  
-ATOM   7467  CG2 ILE C 975     -70.290  47.084  -6.968  1.00 46.05           C  
-ANISOU 7467  CG2 ILE C 975     6264   5626   5606   -226    336   -727       C  
-ATOM   7468  CD1 ILE C 975     -70.627  44.671  -5.071  1.00 43.74           C  
-ANISOU 7468  CD1 ILE C 975     5907   5511   5201   -101    240   -689       C  
-ATOM   7469  N   SER C 976     -66.664  44.660  -7.058  1.00 38.22           N  
-ANISOU 7469  N   SER C 976     5059   4926   4538   -289    176   -801       N  
-ATOM   7470  CA  SER C 976     -65.724  43.601  -6.802  1.00 39.05           C  
-ANISOU 7470  CA  SER C 976     5096   5144   4599   -271    120   -809       C  
-ATOM   7471  C   SER C 976     -66.447  42.434  -6.178  1.00 36.37           C  
-ANISOU 7471  C   SER C 976     4758   4841   4219   -178     96   -751       C  
-ATOM   7472  O   SER C 976     -67.246  42.623  -5.282  1.00 36.41           O  
-ANISOU 7472  O   SER C 976     4802   4830   4203   -145    107   -752       O  
-ATOM   7473  CB  SER C 976     -64.630  44.087  -5.856  1.00 40.08           C  
-ANISOU 7473  CB  SER C 976     5192   5354   4682   -322     96   -912       C  
-ATOM   7474  OG  SER C 976     -63.664  43.072  -5.706  1.00 45.68           O  
-ANISOU 7474  OG  SER C 976     5830   6180   5346   -299     43   -915       O  
-ATOM   7475  N   SER C 977     -66.157  41.227  -6.650  1.00 33.25           N  
-ANISOU 7475  N   SER C 977     4324   4493   3816   -138     65   -699       N  
-ATOM   7476  CA  SER C 977     -66.777  40.039  -6.108  1.00 33.19           C  
-ANISOU 7476  CA  SER C 977     4321   4517   3773    -54     47   -641       C  
-ATOM   7477  C   SER C 977     -66.019  39.540  -4.904  1.00 34.12           C  
-ANISOU 7477  C   SER C 977     4404   4745   3815    -23      7   -683       C  
-ATOM   7478  O   SER C 977     -66.516  38.677  -4.174  1.00 33.32           O  
-ANISOU 7478  O   SER C 977     4313   4673   3673     49     -4   -644       O  
-ATOM   7479  CB  SER C 977     -66.822  38.925  -7.168  1.00 31.79           C  
-ANISOU 7479  CB  SER C 977     4126   4334   3619    -22     38   -567       C  
-ATOM   7480  OG  SER C 977     -65.520  38.626  -7.613  1.00 31.72           O  
-ANISOU 7480  OG  SER C 977     4062   4391   3599    -46      9   -594       O  
-ATOM   7481  N   GLY C 978     -64.787  40.014  -4.747  1.00 35.26           N  
-ANISOU 7481  N   GLY C 978     4503   4957   3938    -75    -15   -759       N  
-ATOM   7482  CA  GLY C 978     -63.914  39.505  -3.715  1.00 38.83           C  
-ANISOU 7482  CA  GLY C 978     4908   5533   4312    -45    -59   -800       C  
-ATOM   7483  C   GLY C 978     -63.224  38.206  -4.080  1.00 41.67           C  
-ANISOU 7483  C   GLY C 978     5220   5967   4646      9    -92   -756       C  
-ATOM   7484  O   GLY C 978     -62.498  37.652  -3.272  1.00 42.73           O  
-ANISOU 7484  O   GLY C 978     5313   6212   4710     50   -128   -778       O  
-ATOM   7485  N   VAL C 979     -63.443  37.704  -5.294  1.00 43.62           N  
-ANISOU 7485  N   VAL C 979     5472   6156   4944     13    -79   -692       N  
-ATOM   7486  CA  VAL C 979     -62.754  36.513  -5.781  1.00 46.12           C  
-ANISOU 7486  CA  VAL C 979     5749   6532   5241     60   -105   -651       C  
-ATOM   7487  C   VAL C 979     -61.527  37.020  -6.549  1.00 46.57           C  
-ANISOU 7487  C   VAL C 979     5749   6630   5316     -9   -116   -701       C  
-ATOM   7488  O   VAL C 979     -61.669  37.682  -7.562  1.00 43.38           O  
-ANISOU 7488  O   VAL C 979     5357   6150   4976    -70    -90   -699       O  
-ATOM   7489  CB  VAL C 979     -63.656  35.709  -6.741  1.00 46.80           C  
-ANISOU 7489  CB  VAL C 979     5874   6533   5376     95    -82   -561       C  
-ATOM   7490  CG1 VAL C 979     -62.873  34.605  -7.440  1.00 47.45           C  
-ANISOU 7490  CG1 VAL C 979     5920   6662   5446    132   -102   -525       C  
-ATOM   7491  CG2 VAL C 979     -64.839  35.140  -5.985  1.00 45.96           C  
-ANISOU 7491  CG2 VAL C 979     5818   6392   5251    159    -68   -511       C  
-ATOM   7492  N   ASN C 980     -60.338  36.740  -6.056  1.00 53.32           N  
-ANISOU 7492  N   ASN C 980     6540   7609   6112      2   -153   -744       N  
-ATOM   7493  CA  ASN C 980     -59.107  37.247  -6.686  1.00 58.20           C  
-ANISOU 7493  CA  ASN C 980     7093   8281   6740    -68   -165   -797       C  
-ATOM   7494  C   ASN C 980     -58.444  36.205  -7.583  1.00 58.07           C  
-ANISOU 7494  C   ASN C 980     7037   8304   6722    -26   -180   -747       C  
-ATOM   7495  O   ASN C 980     -57.889  36.551  -8.635  1.00 60.23           O  
-ANISOU 7495  O   ASN C 980     7283   8564   7037    -82   -170   -756       O  
-ATOM   7496  CB  ASN C 980     -58.117  37.726  -5.597  1.00 59.63           C  
-ANISOU 7496  CB  ASN C 980     7214   8588   6853    -95   -198   -890       C  
-ATOM   7497  N   ASP C 981     -58.503  34.934  -7.173  1.00 55.73           N  
-ANISOU 7497  N   ASP C 981     6743   8055   6375     75   -198   -694       N  
-ATOM   7498  CA  ASP C 981     -57.780  33.855  -7.867  1.00 54.72           C  
-ANISOU 7498  CA  ASP C 981     6581   7977   6232    129   -213   -650       C  
-ATOM   7499  C   ASP C 981     -58.578  33.193  -9.019  1.00 49.21           C  
-ANISOU 7499  C   ASP C 981     5936   7168   5593    152   -185   -569       C  
-ATOM   7500  O   ASP C 981     -58.950  32.026  -8.931  1.00 45.61           O  
-ANISOU 7500  O   ASP C 981     5511   6703   5116    235   -184   -506       O  
-ATOM   7501  CB  ASP C 981     -57.375  32.792  -6.840  1.00 59.58           C  
-ANISOU 7501  CB  ASP C 981     7177   8701   6760    233   -242   -633       C  
-ATOM   7502  CG  ASP C 981     -58.594  32.136  -6.140  1.00 68.87           C  
-ANISOU 7502  CG  ASP C 981     8428   9814   7924    305   -226   -575       C  
-ATOM   7503  OD1 ASP C 981     -59.609  32.831  -5.864  1.00 65.77           O  
-ANISOU 7503  OD1 ASP C 981     8084   9338   7566    266   -204   -582       O  
-ATOM   7504  OD2 ASP C 981     -58.515  30.919  -5.838  1.00 78.45           O  
-ANISOU 7504  OD2 ASP C 981     9651  11065   9091    403   -232   -521       O  
-ATOM   7505  N   THR C 982     -58.857  33.950 -10.071  1.00 40.62           N  
-ANISOU 7505  N   THR C 982     4862   5995   4577     77   -159   -571       N  
-ATOM   7506  CA  THR C 982     -59.727  33.481 -11.117  1.00 38.36           C  
-ANISOU 7506  CA  THR C 982     4626   5605   4344     90   -133   -503       C  
-ATOM   7507  C   THR C 982     -59.199  33.867 -12.478  1.00 38.25           C  
-ANISOU 7507  C   THR C 982     4587   5569   4379     34   -122   -505       C  
-ATOM   7508  O   THR C 982     -58.565  34.893 -12.652  1.00 37.66           O  
-ANISOU 7508  O   THR C 982     4476   5514   4320    -40   -118   -560       O  
-ATOM   7509  CB  THR C 982     -61.178  34.025 -10.961  1.00 39.74           C  
-ANISOU 7509  CB  THR C 982     4868   5671   4561     70   -103   -484       C  
-ATOM   7510  OG1 THR C 982     -61.940  33.700 -12.126  1.00 37.04           O  
-ANISOU 7510  OG1 THR C 982     4562   5238   4272     70    -79   -425       O  
-ATOM   7511  CG2 THR C 982     -61.187  35.540 -10.806  1.00 40.76           C  
-ANISOU 7511  CG2 THR C 982     4995   5773   4718    -15    -88   -546       C  
-ATOM   7512  N   SER C 983     -59.504  33.035 -13.459  1.00 38.85           N  
-ANISOU 7512  N   SER C 983     4685   5599   4479     69   -112   -445       N  
-ATOM   7513  CA  SER C 983     -59.156  33.312 -14.833  1.00 37.37           C  
-ANISOU 7513  CA  SER C 983     4481   5381   4336     25    -97   -437       C  
-ATOM   7514  C   SER C 983     -60.088  34.340 -15.490  1.00 35.75           C  
-ANISOU 7514  C   SER C 983     4316   5069   4196    -38    -63   -431       C  
-ATOM   7515  O   SER C 983     -59.847  34.714 -16.625  1.00 37.44           O  
-ANISOU 7515  O   SER C 983     4521   5255   4450    -78    -46   -425       O  
-ATOM   7516  CB  SER C 983     -59.219  32.009 -15.634  1.00 39.75           C  
-ANISOU 7516  CB  SER C 983     4798   5670   4635     89    -98   -375       C  
-ATOM   7517  OG  SER C 983     -58.461  30.986 -15.007  1.00 45.85           O  
-ANISOU 7517  OG  SER C 983     5544   6532   5344    163   -124   -370       O  
-ATOM   7518  N   LEU C 984     -61.138  34.799 -14.812  1.00 32.40           N  
-ANISOU 7518  N   LEU C 984     3938   4589   3783    -44    -49   -431       N  
-ATOM   7519  CA  LEU C 984     -62.186  35.557 -15.480  1.00 29.95           C  
-ANISOU 7519  CA  LEU C 984     3674   4177   3530    -81    -14   -409       C  
-ATOM   7520  C   LEU C 984     -62.348  36.944 -14.890  1.00 29.35           C  
-ANISOU 7520  C   LEU C 984     3610   4074   3469   -140      6   -460       C  
-ATOM   7521  O   LEU C 984     -62.423  37.109 -13.664  1.00 28.82           O  
-ANISOU 7521  O   LEU C 984     3547   4036   3367   -131     -6   -494       O  
-ATOM   7522  CB  LEU C 984     -63.522  34.800 -15.344  1.00 30.45           C  
-ANISOU 7522  CB  LEU C 984     3789   4184   3596    -27     -6   -352       C  
-ATOM   7523  CG  LEU C 984     -63.712  33.446 -16.073  1.00 29.26           C  
-ANISOU 7523  CG  LEU C 984     3646   4028   3442     25    -14   -295       C  
-ATOM   7524  CD1 LEU C 984     -64.996  32.788 -15.642  1.00 28.20           C  
-ANISOU 7524  CD1 LEU C 984     3560   3848   3306     67     -5   -251       C  
-ATOM   7525  CD2 LEU C 984     -63.723  33.642 -17.585  1.00 29.50           C  
-ANISOU 7525  CD2 LEU C 984     3675   4017   3518     -4      3   -272       C  
-ATOM   7526  N   LEU C 985     -62.460  37.941 -15.750  1.00 29.84           N  
-ANISOU 7526  N   LEU C 985     3684   4074   3580   -198     38   -465       N  
-ATOM   7527  CA  LEU C 985     -62.819  39.282 -15.312  1.00 30.63           C  
-ANISOU 7527  CA  LEU C 985     3813   4122   3701   -251     69   -504       C  
-ATOM   7528  C   LEU C 985     -64.278  39.348 -14.866  1.00 29.95           C  
-ANISOU 7528  C   LEU C 985     3787   3970   3624   -214     87   -470       C  
-ATOM   7529  O   LEU C 985     -64.611  40.003 -13.884  1.00 29.78           O  
-ANISOU 7529  O   LEU C 985     3788   3935   3590   -225     96   -505       O  
-ATOM   7530  CB  LEU C 985     -62.566  40.308 -16.429  1.00 34.09           C  
-ANISOU 7530  CB  LEU C 985     4257   4505   4192   -315    108   -510       C  
-ATOM   7531  CG  LEU C 985     -61.100  40.553 -16.865  1.00 36.98           C  
-ANISOU 7531  CG  LEU C 985     4563   4931   4556   -371    101   -553       C  
-ATOM   7532  CD1 LEU C 985     -61.014  41.551 -18.020  1.00 38.40           C  
-ANISOU 7532  CD1 LEU C 985     4758   5041   4790   -430    149   -546       C  
-ATOM   7533  CD2 LEU C 985     -60.246  41.047 -15.711  1.00 37.39           C  
-ANISOU 7533  CD2 LEU C 985     4581   5051   4574   -415     85   -636       C  
-ATOM   7534  N   TYR C 986     -65.156  38.666 -15.581  1.00 28.86           N  
-ANISOU 7534  N   TYR C 986     3670   3792   3503   -172     92   -403       N  
-ATOM   7535  CA  TYR C 986     -66.605  38.718 -15.298  1.00 27.88           C  
-ANISOU 7535  CA  TYR C 986     3595   3609   3389   -139    111   -364       C  
-ATOM   7536  C   TYR C 986     -67.197  37.298 -15.232  1.00 26.53           C  
-ANISOU 7536  C   TYR C 986     3427   3457   3198    -75     90   -312       C  
-ATOM   7537  O   TYR C 986     -66.633  36.349 -15.799  1.00 24.29           O  
-ANISOU 7537  O   TYR C 986     3117   3207   2904    -57     68   -293       O  
-ATOM   7538  CB  TYR C 986     -67.300  39.568 -16.369  1.00 27.32           C  
-ANISOU 7538  CB  TYR C 986     3554   3459   3367   -161    153   -334       C  
-ATOM   7539  CG  TYR C 986     -66.546  40.866 -16.620  1.00 29.67           C  
-ANISOU 7539  CG  TYR C 986     3851   3733   3689   -227    181   -382       C  
-ATOM   7540  CD1 TYR C 986     -66.597  41.911 -15.691  1.00 31.28           C  
-ANISOU 7540  CD1 TYR C 986     4082   3914   3890   -258    202   -432       C  
-ATOM   7541  CD2 TYR C 986     -65.765  41.040 -17.748  1.00 29.66           C  
-ANISOU 7541  CD2 TYR C 986     3826   3732   3712   -261    189   -379       C  
-ATOM   7542  CE1 TYR C 986     -65.913  43.094 -15.882  1.00 32.59           C  
-ANISOU 7542  CE1 TYR C 986     4252   4050   4078   -326    232   -480       C  
-ATOM   7543  CE2 TYR C 986     -65.070  42.221 -17.946  1.00 31.46           C  
-ANISOU 7543  CE2 TYR C 986     4055   3935   3962   -328    220   -423       C  
-ATOM   7544  CZ  TYR C 986     -65.143  43.244 -17.013  1.00 33.03           C  
-ANISOU 7544  CZ  TYR C 986     4283   4105   4160   -363    243   -475       C  
-ATOM   7545  OH  TYR C 986     -64.418  44.409 -17.195  1.00 34.97           O  
-ANISOU 7545  OH  TYR C 986     4535   4322   4431   -438    278   -524       O  
-ATOM   7546  N   ASN C 987     -68.346  37.181 -14.570  1.00 24.73           N  
-ANISOU 7546  N   ASN C 987     3233   3202   2964    -43     99   -288       N  
-ATOM   7547  CA  ASN C 987     -69.049  35.916 -14.475  1.00 23.80           C  
-ANISOU 7547  CA  ASN C 987     3123   3089   2830      8     88   -238       C  
-ATOM   7548  C   ASN C 987     -69.439  35.405 -15.846  1.00 23.19           C  
-ANISOU 7548  C   ASN C 987     3045   2983   2784     10     94   -191       C  
-ATOM   7549  O   ASN C 987     -69.562  36.160 -16.814  1.00 19.86           O  
-ANISOU 7549  O   ASN C 987     2625   2526   2397    -20    114   -185       O  
-ATOM   7550  CB  ASN C 987     -70.326  36.044 -13.662  1.00 23.87           C  
-ANISOU 7550  CB  ASN C 987     3166   3068   2834     34    106   -218       C  
-ATOM   7551  CG  ASN C 987     -70.072  36.478 -12.235  1.00 23.90           C  
-ANISOU 7551  CG  ASN C 987     3177   3103   2802     40    100   -263       C  
-ATOM   7552  OD1 ASN C 987     -69.099  36.105 -11.662  1.00 25.71           O  
-ANISOU 7552  OD1 ASN C 987     3383   3392   2996     47     74   -294       O  
-ATOM   7553  ND2 ASN C 987     -70.970  37.276 -11.678  1.00 23.83           N  
-ANISOU 7553  ND2 ASN C 987     3199   3057   2799     41    126   -266       N  
-ATOM   7554  N   GLU C 988     -69.602  34.095 -15.909  1.00 21.79           N  
-ANISOU 7554  N   GLU C 988     2867   2823   2590     46     79   -158       N  
-ATOM   7555  CA  GLU C 988     -70.373  33.505 -16.957  1.00 21.02           C  
-ANISOU 7555  CA  GLU C 988     2777   2692   2515     52     87   -112       C  
-ATOM   7556  C   GLU C 988     -71.098  32.298 -16.423  1.00 18.97           C  
-ANISOU 7556  C   GLU C 988     2537   2435   2237     90     84    -80       C  
-ATOM   7557  O   GLU C 988     -70.757  31.758 -15.390  1.00 20.01           O  
-ANISOU 7557  O   GLU C 988     2673   2597   2334    118     72    -89       O  
-ATOM   7558  CB  GLU C 988     -69.509  33.171 -18.178  1.00 22.89           C  
-ANISOU 7558  CB  GLU C 988     2992   2942   2763     39     76   -111       C  
-ATOM   7559  CG  GLU C 988     -68.263  32.380 -17.919  1.00 23.75           C  
-ANISOU 7559  CG  GLU C 988     3079   3104   2841     58     51   -130       C  
-ATOM   7560  CD  GLU C 988     -67.347  32.350 -19.141  1.00 25.66           C  
-ANISOU 7560  CD  GLU C 988     3294   3359   3095     41     45   -134       C  
-ATOM   7561  OE1 GLU C 988     -67.250  31.280 -19.780  1.00 26.61           O  
-ANISOU 7561  OE1 GLU C 988     3417   3484   3209     64     37   -110       O  
-ATOM   7562  OE2 GLU C 988     -66.765  33.401 -19.485  1.00 26.40           O  
-ANISOU 7562  OE2 GLU C 988     3369   3456   3206      2     52   -161       O  
-ATOM   7563  N   TYR C 989     -72.125  31.904 -17.130  1.00 18.64           N  
-ANISOU 7563  N   TYR C 989     2506   2361   2215     88     96    -42       N  
-ATOM   7564  CA  TYR C 989     -73.026  30.874 -16.693  1.00 19.09           C  
-ANISOU 7564  CA  TYR C 989     2583   2410   2262    112    102    -10       C  
-ATOM   7565  C   TYR C 989     -73.227  29.911 -17.846  1.00 19.12           C  
-ANISOU 7565  C   TYR C 989     2586   2400   2278    106    100     15       C  
-ATOM   7566  O   TYR C 989     -73.465  30.339 -18.982  1.00 18.58           O  
-ANISOU 7566  O   TYR C 989     2505   2320   2235     82    103     21       O  
-ATOM   7567  CB  TYR C 989     -74.369  31.482 -16.325  1.00 20.13           C  
-ANISOU 7567  CB  TYR C 989     2725   2518   2406    109    125      8       C  
-ATOM   7568  CG  TYR C 989     -74.312  32.538 -15.241  1.00 21.18           C  
-ANISOU 7568  CG  TYR C 989     2865   2656   2528    114    132    -19       C  
-ATOM   7569  CD1 TYR C 989     -74.031  33.854 -15.558  1.00 21.20           C  
-ANISOU 7569  CD1 TYR C 989     2861   2646   2548     90    140    -43       C  
-ATOM   7570  CD2 TYR C 989     -74.550  32.216 -13.927  1.00 20.79           C  
-ANISOU 7570  CD2 TYR C 989     2831   2621   2449    142    134    -19       C  
-ATOM   7571  CE1 TYR C 989     -73.982  34.823 -14.588  1.00 22.59           C  
-ANISOU 7571  CE1 TYR C 989     3049   2820   2713     90    150    -73       C  
-ATOM   7572  CE2 TYR C 989     -74.475  33.171 -12.950  1.00 21.90           C  
-ANISOU 7572  CE2 TYR C 989     2979   2768   2574    146    140    -48       C  
-ATOM   7573  CZ  TYR C 989     -74.217  34.481 -13.290  1.00 23.47           C  
-ANISOU 7573  CZ  TYR C 989     3174   2951   2794    118    149    -77       C  
-ATOM   7574  OH  TYR C 989     -74.115  35.457 -12.336  1.00 22.86           O  
-ANISOU 7574  OH  TYR C 989     3109   2874   2701    117    157   -113       O  
-ATOM   7575  N   ILE C 990     -73.136  28.624 -17.555  1.00 18.83           N  
-ANISOU 7575  N   ILE C 990     2566   2366   2222    129     97     29       N  
-ATOM   7576  CA  ILE C 990     -73.255  27.597 -18.589  1.00 19.06           C  
-ANISOU 7576  CA  ILE C 990     2603   2380   2260    122     97     46       C  
-ATOM   7577  C   ILE C 990     -74.289  26.528 -18.185  1.00 19.55           C  
-ANISOU 7577  C   ILE C 990     2694   2417   2318    127    115     74       C  
-ATOM   7578  O   ILE C 990     -74.240  26.001 -17.052  1.00 18.50           O  
-ANISOU 7578  O   ILE C 990     2583   2287   2160    157    122     82       O  
-ATOM   7579  CB  ILE C 990     -71.894  26.938 -18.864  1.00 19.23           C  
-ANISOU 7579  CB  ILE C 990     2624   2422   2262    144     80     32       C  
-ATOM   7580  CG1 ILE C 990     -70.832  27.975 -19.226  1.00 19.98           C  
-ANISOU 7580  CG1 ILE C 990     2685   2546   2361    132     65      3       C  
-ATOM   7581  CG2 ILE C 990     -71.991  25.992 -20.024  1.00 20.01           C  
-ANISOU 7581  CG2 ILE C 990     2732   2500   2369    135     82     45       C  
-ATOM   7582  CD1 ILE C 990     -70.101  28.555 -18.042  1.00 20.18           C  
-ANISOU 7582  CD1 ILE C 990     2699   2606   2361    148     56    -24       C  
-ATOM   7583  N   VAL C 991     -75.205  26.219 -19.103  1.00 19.12           N  
-ANISOU 7583  N   VAL C 991     2637   2343   2284     97    123     89       N  
-ATOM   7584  CA  VAL C 991     -76.077  25.062 -18.963  1.00 19.07           C  
-ANISOU 7584  CA  VAL C 991     2656   2313   2277     89    142    111       C  
-ATOM   7585  C   VAL C 991     -75.809  24.047 -20.070  1.00 20.45           C  
-ANISOU 7585  C   VAL C 991     2843   2470   2456     75    140    108       C  
-ATOM   7586  O   VAL C 991     -75.319  24.425 -21.134  1.00 20.17           O  
-ANISOU 7586  O   VAL C 991     2788   2446   2429     65    124     95       O  
-ATOM   7587  CB  VAL C 991     -77.557  25.450 -18.927  1.00 19.17           C  
-ANISOU 7587  CB  VAL C 991     2654   2322   2306     61    158    128       C  
-ATOM   7588  CG1 VAL C 991     -77.842  26.297 -17.690  1.00 19.79           C  
-ANISOU 7588  CG1 VAL C 991     2730   2413   2377     83    166    132       C  
-ATOM   7589  CG2 VAL C 991     -77.988  26.143 -20.168  1.00 18.06           C  
-ANISOU 7589  CG2 VAL C 991     2481   2195   2188     33    150    125       C  
-ATOM   7590  N   TYR C 992     -76.094  22.777 -19.791  1.00 19.87           N  
-ANISOU 7590  N   TYR C 992     2808   2367   2374     77    159    121       N  
-ATOM   7591  CA  TYR C 992     -75.696  21.656 -20.623  1.00 22.04           C  
-ANISOU 7591  CA  TYR C 992     3111   2618   2647     72    162    116       C  
-ATOM   7592  C   TYR C 992     -76.886  20.918 -21.187  1.00 23.50           C  
-ANISOU 7592  C   TYR C 992     3306   2776   2848     22    181    121       C  
-ATOM   7593  O   TYR C 992     -76.728  19.864 -21.726  1.00 25.41           O  
-ANISOU 7593  O   TYR C 992     3580   2986   3087     13    192    115       O  
-ATOM   7594  CB  TYR C 992     -74.764  20.685 -19.827  1.00 22.31           C  
-ANISOU 7594  CB  TYR C 992     3191   2636   2652    124    173    124       C  
-ATOM   7595  CG  TYR C 992     -73.539  21.437 -19.373  1.00 20.73           C  
-ANISOU 7595  CG  TYR C 992     2968   2477   2431    168    150    112       C  
-ATOM   7596  CD1 TYR C 992     -73.532  22.103 -18.170  1.00 21.28           C  
-ANISOU 7596  CD1 TYR C 992     3027   2572   2488    191    147    115       C  
-ATOM   7597  CD2 TYR C 992     -72.428  21.565 -20.210  1.00 19.78           C  
-ANISOU 7597  CD2 TYR C 992     2831   2378   2306    181    129     94       C  
-ATOM   7598  CE1 TYR C 992     -72.431  22.846 -17.766  1.00 22.36           C  
-ANISOU 7598  CE1 TYR C 992     3138   2753   2605    222    124     97       C  
-ATOM   7599  CE2 TYR C 992     -71.309  22.289 -19.821  1.00 20.08           C  
-ANISOU 7599  CE2 TYR C 992     2840   2462   2326    212    107     79       C  
-ATOM   7600  CZ  TYR C 992     -71.308  22.930 -18.600  1.00 21.04           C  
-ANISOU 7600  CZ  TYR C 992     2951   2609   2434    230    104     78       C  
-ATOM   7601  OH  TYR C 992     -70.241  23.685 -18.187  1.00 21.74           O  
-ANISOU 7601  OH  TYR C 992     3008   2747   2504    251     83     56       O  
-ATOM   7602  N   ASP C 993     -78.065  21.511 -21.088  1.00 24.24           N  
-ANISOU 7602  N   ASP C 993     3370   2884   2957    -10    186    129       N  
-ATOM   7603  CA  ASP C 993     -79.288  20.949 -21.617  1.00 24.55           C  
-ANISOU 7603  CA  ASP C 993     3404   2913   3010    -65    202    130       C  
-ATOM   7604  C   ASP C 993     -80.078  22.127 -22.199  1.00 24.33           C  
-ANISOU 7604  C   ASP C 993     3318   2931   2995    -87    186    130       C  
-ATOM   7605  O   ASP C 993     -80.360  23.058 -21.495  1.00 24.62           O  
-ANISOU 7605  O   ASP C 993     3333   2987   3032    -69    187    142       O  
-ATOM   7606  CB  ASP C 993     -80.064  20.267 -20.485  1.00 25.58           C  
-ANISOU 7606  CB  ASP C 993     3563   3018   3138    -72    237    151       C  
-ATOM   7607  CG  ASP C 993     -81.365  19.603 -20.956  1.00 27.48           C  
-ANISOU 7607  CG  ASP C 993     3797   3251   3394   -139    257    149       C  
-ATOM   7608  OD1 ASP C 993     -81.950  19.967 -21.997  1.00 27.54           O  
-ANISOU 7608  OD1 ASP C 993     3761   3291   3411   -177    241    135       O  
-ATOM   7609  OD2 ASP C 993     -81.846  18.718 -20.224  1.00 31.11           O  
-ANISOU 7609  OD2 ASP C 993     4293   3676   3853   -153    292    163       O  
-ATOM   7610  N   ILE C 994     -80.400  22.077 -23.484  1.00 24.42           N  
-ANISOU 7610  N   ILE C 994     3305   2960   3013   -121    174    116       N  
-ATOM   7611  CA  ILE C 994     -81.069  23.159 -24.164  1.00 23.76           C  
-ANISOU 7611  CA  ILE C 994     3168   2925   2937   -132    161    119       C  
-ATOM   7612  C   ILE C 994     -82.448  23.507 -23.598  1.00 23.51           C  
-ANISOU 7612  C   ILE C 994     3106   2918   2909   -150    177    137       C  
-ATOM   7613  O   ILE C 994     -82.945  24.624 -23.802  1.00 22.71           O  
-ANISOU 7613  O   ILE C 994     2963   2856   2810   -138    170    149       O  
-ATOM   7614  CB  ILE C 994     -81.240  22.868 -25.667  1.00 26.25           C  
-ANISOU 7614  CB  ILE C 994     3462   3261   3250   -164    146    100       C  
-ATOM   7615  CG1 ILE C 994     -82.144  21.642 -25.889  1.00 27.82           C  
-ANISOU 7615  CG1 ILE C 994     3671   3449   3450   -220    162     87       C  
-ATOM   7616  CG2 ILE C 994     -79.876  22.651 -26.292  1.00 27.35           C  
-ANISOU 7616  CG2 ILE C 994     3626   3381   3383   -141    131     83       C  
-ATOM   7617  CD1 ILE C 994     -82.354  21.294 -27.354  1.00 29.08           C  
-ANISOU 7617  CD1 ILE C 994     3810   3635   3603   -256    146     62       C  
-ATOM   7618  N   ALA C 995     -83.062  22.565 -22.890  1.00 23.16           N  
-ANISOU 7618  N   ALA C 995     3083   2851   2866   -175    201    143       N  
-ATOM   7619  CA  ALA C 995     -84.359  22.782 -22.276  1.00 23.95           C  
-ANISOU 7619  CA  ALA C 995     3155   2977   2969   -193    220    162       C  
-ATOM   7620  C   ALA C 995     -84.288  23.658 -21.023  1.00 24.34           C  
-ANISOU 7620  C   ALA C 995     3207   3027   3015   -146    229    184       C  
-ATOM   7621  O   ALA C 995     -85.329  24.071 -20.523  1.00 25.89           O  
-ANISOU 7621  O   ALA C 995     3374   3251   3210   -150    244    202       O  
-ATOM   7622  CB  ALA C 995     -85.011  21.430 -21.932  1.00 25.26           C  
-ANISOU 7622  CB  ALA C 995     3345   3114   3138   -243    250    161       C  
-ATOM   7623  N   GLN C 996     -83.086  23.937 -20.504  1.00 23.86           N  
-ANISOU 7623  N   GLN C 996     3178   2940   2947   -101    220    180       N  
-ATOM   7624  CA  GLN C 996     -82.923  24.828 -19.347  1.00 23.34           C  
-ANISOU 7624  CA  GLN C 996     3116   2878   2873    -58    225    193       C  
-ATOM   7625  C   GLN C 996     -83.006  26.332 -19.666  1.00 22.25           C  
-ANISOU 7625  C   GLN C 996     2944   2772   2740    -36    213    193       C  
-ATOM   7626  O   GLN C 996     -82.809  27.160 -18.785  1.00 21.18           O  
-ANISOU 7626  O   GLN C 996     2813   2635   2598     -3    217    197       O  
-ATOM   7627  CB  GLN C 996     -81.605  24.563 -18.617  1.00 24.52           C  
-ANISOU 7627  CB  GLN C 996     3309   2998   3010    -19    220    184       C  
-ATOM   7628  CG  GLN C 996     -81.668  23.436 -17.630  1.00 25.85           C  
-ANISOU 7628  CG  GLN C 996     3519   3137   3166    -14    245    198       C  
-ATOM   7629  CD  GLN C 996     -80.318  23.057 -17.068  1.00 24.97           C  
-ANISOU 7629  CD  GLN C 996     3446   3006   3034     30    238    190       C  
-ATOM   7630  OE1 GLN C 996     -79.639  22.201 -17.619  1.00 26.51           O  
-ANISOU 7630  OE1 GLN C 996     3666   3179   3226     29    234    182       O  
-ATOM   7631  NE2 GLN C 996     -79.936  23.672 -15.973  1.00 24.81           N  
-ANISOU 7631  NE2 GLN C 996     3431   3000   2996     72    236    193       N  
-ATOM   7632  N   VAL C 997     -83.344  26.678 -20.905  1.00 22.01           N  
-ANISOU 7632  N   VAL C 997     2878   2767   2717    -55    201    190       N  
-ATOM   7633  CA  VAL C 997     -83.381  28.066 -21.331  1.00 21.35           C  
-ANISOU 7633  CA  VAL C 997     2769   2707   2637    -31    195    195       C  
-ATOM   7634  C   VAL C 997     -84.762  28.419 -21.882  1.00 22.57           C  
-ANISOU 7634  C   VAL C 997     2876   2908   2791    -43    203    215       C  
-ATOM   7635  O   VAL C 997     -85.281  27.695 -22.717  1.00 22.86           O  
-ANISOU 7635  O   VAL C 997     2890   2968   2827    -79    197    211       O  
-ATOM   7636  CB  VAL C 997     -82.386  28.309 -22.473  1.00 20.90           C  
-ANISOU 7636  CB  VAL C 997     2711   2646   2584    -30    173    179       C  
-ATOM   7637  CG1 VAL C 997     -82.473  29.761 -22.915  1.00 22.75           C  
-ANISOU 7637  CG1 VAL C 997     2924   2897   2822     -5    176    188       C  
-ATOM   7638  CG2 VAL C 997     -80.963  27.999 -22.028  1.00 20.25           C  
-ANISOU 7638  CG2 VAL C 997     2665   2529   2498    -16    163    159       C  
-ATOM   7639  N   ASN C 998     -85.328  29.537 -21.428  1.00 22.84           N  
-ANISOU 7639  N   ASN C 998     2895   2959   2822    -10    217    233       N  
-ATOM   7640  CA  ASN C 998     -86.562  30.070 -21.984  1.00 23.24           C  
-ANISOU 7640  CA  ASN C 998     2898   3064   2868     -6    226    256       C  
-ATOM   7641  C   ASN C 998     -86.292  31.508 -22.408  1.00 21.91           C  
-ANISOU 7641  C   ASN C 998     2728   2898   2700     39    229    265       C  
-ATOM   7642  O   ASN C 998     -86.083  32.414 -21.570  1.00 21.27           O  
-ANISOU 7642  O   ASN C 998     2670   2791   2619     74    245    270       O  
-ATOM   7643  CB  ASN C 998     -87.683  29.949 -20.941  1.00 24.44           C  
-ANISOU 7643  CB  ASN C 998     3037   3237   3014     -3    250    276       C  
-ATOM   7644  CG  ASN C 998     -89.078  30.249 -21.503  1.00 25.74           C  
-ANISOU 7644  CG  ASN C 998     3141   3473   3168     -4    258    299       C  
-ATOM   7645  OD1 ASN C 998     -89.318  30.165 -22.699  1.00 28.70           O  
-ANISOU 7645  OD1 ASN C 998     3480   3887   3538    -19    243    296       O  
-ATOM   7646  ND2 ASN C 998     -90.004  30.569 -20.636  1.00 27.01           N  
-ANISOU 7646  ND2 ASN C 998     3285   3656   3320     16    282    321       N  
-ATOM   7647  N   LEU C 999     -86.187  31.702 -23.706  1.00 21.29           N  
-ANISOU 7647  N   LEU C 999     2627   2843   2619     36    216    266       N  
-ATOM   7648  CA  LEU C 999     -85.884  33.029 -24.259  1.00 22.83           C  
-ANISOU 7648  CA  LEU C 999     2824   3034   2814     77    224    279       C  
-ATOM   7649  C   LEU C 999     -87.047  33.979 -23.987  1.00 24.37           C  
-ANISOU 7649  C   LEU C 999     2997   3265   2999    120    250    312       C  
-ATOM   7650  O   LEU C 999     -88.198  33.594 -24.155  1.00 23.41           O  
-ANISOU 7650  O   LEU C 999     2830   3201   2864    113    251    328       O  
-ATOM   7651  CB  LEU C 999     -85.621  32.923 -25.767  1.00 23.12           C  
-ANISOU 7651  CB  LEU C 999     2840   3098   2846     69    206    277       C  
-ATOM   7652  CG  LEU C 999     -84.386  32.095 -26.120  1.00 23.49           C  
-ANISOU 7652  CG  LEU C 999     2913   3111   2903     36    183    245       C  
-ATOM   7653  CD1 LEU C 999     -84.188  32.117 -27.613  1.00 23.84           C  
-ANISOU 7653  CD1 LEU C 999     2936   3185   2939     34    169    246       C  
-ATOM   7654  CD2 LEU C 999     -83.126  32.624 -25.421  1.00 23.34           C  
-ANISOU 7654  CD2 LEU C 999     2938   3032   2897     49    188    230       C  
-ATOM   7655  N   LYS C1000     -86.738  35.185 -23.498  1.00 26.32           N  
-ANISOU 7655  N   LYS C1000     3275   3475   3250    161    273    320       N  
-ATOM   7656  CA  LYS C1000     -87.762  36.150 -23.118  1.00 26.73           C  
-ANISOU 7656  CA  LYS C1000     3316   3549   3290    211    305    352       C  
-ATOM   7657  C   LYS C1000     -87.768  37.416 -23.958  1.00 26.14           C  
-ANISOU 7657  C   LYS C1000     3246   3475   3212    260    325    377       C  
-ATOM   7658  O   LYS C1000     -88.815  37.872 -24.369  1.00 25.39           O  
-ANISOU 7658  O   LYS C1000     3117   3433   3098    300    341    412       O  
-ATOM   7659  CB  LYS C1000     -87.603  36.583 -21.654  1.00 27.81           C  
-ANISOU 7659  CB  LYS C1000     3494   3640   3432    228    326    343       C  
-ATOM   7660  CG  LYS C1000     -87.539  35.486 -20.625  1.00 28.96           C  
-ANISOU 7660  CG  LYS C1000     3646   3778   3579    192    313    324       C  
-ATOM   7661  CD  LYS C1000     -88.601  34.420 -20.775  1.00 31.27           C  
-ANISOU 7661  CD  LYS C1000     3891   4129   3863    164    306    338       C  
-ATOM   7662  CE  LYS C1000     -89.959  34.856 -20.310  1.00 33.59           C  
-ANISOU 7662  CE  LYS C1000     4153   4470   4140    198    332    370       C  
-ATOM   7663  NZ  LYS C1000     -90.854  33.665 -20.198  1.00 36.51           N  
-ANISOU 7663  NZ  LYS C1000     4478   4889   4503    156    327    375       N  
-ATOM   7664  N   TYR C1001     -86.606  38.024 -24.139  1.00 27.67           N  
-ANISOU 7664  N   TYR C1001     3483   3608   3421    260    331    361       N  
-ATOM   7665  CA  TYR C1001     -86.493  39.274 -24.884  1.00 27.89           C  
-ANISOU 7665  CA  TYR C1001     3528   3620   3448    305    359    385       C  
-ATOM   7666  C   TYR C1001     -85.406  39.229 -25.929  1.00 26.93           C  
-ANISOU 7666  C   TYR C1001     3416   3479   3338    283    345    372       C  
-ATOM   7667  O   TYR C1001     -84.417  38.490 -25.816  1.00 28.35           O  
-ANISOU 7667  O   TYR C1001     3606   3634   3531    235    318    336       O  
-ATOM   7668  CB  TYR C1001     -86.242  40.476 -23.959  1.00 29.62           C  
-ANISOU 7668  CB  TYR C1001     3802   3774   3677    337    399    382       C  
-ATOM   7669  CG  TYR C1001     -87.269  40.652 -22.876  1.00 30.95           C  
-ANISOU 7669  CG  TYR C1001     3969   3958   3833    368    419    396       C  
-ATOM   7670  CD1 TYR C1001     -88.480  41.288 -23.135  1.00 32.02           C  
-ANISOU 7670  CD1 TYR C1001     4082   4138   3947    429    448    442       C  
-ATOM   7671  CD2 TYR C1001     -87.039  40.172 -21.589  1.00 32.07           C  
-ANISOU 7671  CD2 TYR C1001     4128   4076   3980    341    411    365       C  
-ATOM   7672  CE1 TYR C1001     -89.432  41.442 -22.135  1.00 32.30           C  
-ANISOU 7672  CE1 TYR C1001     4113   4192   3969    461    468    456       C  
-ATOM   7673  CE2 TYR C1001     -87.986  40.304 -20.596  1.00 33.60           C  
-ANISOU 7673  CE2 TYR C1001     4320   4288   4160    371    430    379       C  
-ATOM   7674  CZ  TYR C1001     -89.181  40.950 -20.872  1.00 33.79           C  
-ANISOU 7674  CZ  TYR C1001     4321   4354   4165    429    460    424       C  
-ATOM   7675  OH  TYR C1001     -90.126  41.068 -19.866  1.00 35.85           O  
-ANISOU 7675  OH  TYR C1001     4575   4635   4410    461    481    439       O  
-ATOM   7676  N   LEU C1002     -85.603  40.038 -26.953  1.00 28.16           N  
-ANISOU 7676  N   LEU C1002     3567   3647   3483    323    366    405       N  
-ATOM   7677  CA  LEU C1002     -84.604  40.265 -27.983  1.00 27.52           C  
-ANISOU 7677  CA  LEU C1002     3501   3544   3412    313    364    400       C  
-ATOM   7678  C   LEU C1002     -84.424  41.750 -28.104  1.00 26.85           C  
-ANISOU 7678  C   LEU C1002     3460   3407   3333    359    416    425       C  
-ATOM   7679  O   LEU C1002     -85.394  42.451 -28.292  1.00 27.22           O  
-ANISOU 7679  O   LEU C1002     3502   3479   3362    419    446    467       O  
-ATOM   7680  CB  LEU C1002     -85.093  39.662 -29.288  1.00 28.53           C  
-ANISOU 7680  CB  LEU C1002     3577   3748   3515    318    340    420       C  
-ATOM   7681  CG  LEU C1002     -84.198  39.796 -30.520  1.00 29.10           C  
-ANISOU 7681  CG  LEU C1002     3655   3813   3589    314    337    422       C  
-ATOM   7682  CD1 LEU C1002     -82.908  39.095 -30.301  1.00 32.61           C  
-ANISOU 7682  CD1 LEU C1002     4119   4216   4057    255    311    376       C  
-ATOM   7683  CD2 LEU C1002     -84.859  39.142 -31.711  1.00 30.30           C  
-ANISOU 7683  CD2 LEU C1002     3751   4052   3708    322    310    438       C  
-ATOM   7684  N   LEU C1003     -83.206  42.236 -27.939  1.00 25.33           N  
-ANISOU 7684  N   LEU C1003     3314   3145   3166    332    430    398       N  
-ATOM   7685  CA  LEU C1003     -82.936  43.643 -28.052  1.00 26.80           C  
-ANISOU 7685  CA  LEU C1003     3552   3269   3363    365    485    416       C  
-ATOM   7686  C   LEU C1003     -82.183  43.933 -29.335  1.00 27.73           C  
-ANISOU 7686  C   LEU C1003     3674   3377   3484    363    495    430       C  
-ATOM   7687  O   LEU C1003     -81.230  43.227 -29.704  1.00 27.18           O  
-ANISOU 7687  O   LEU C1003     3591   3312   3426    314    463    401       O  
-ATOM   7688  CB  LEU C1003     -82.101  44.139 -26.887  1.00 27.70           C  
-ANISOU 7688  CB  LEU C1003     3717   3306   3503    331    503    372       C  
-ATOM   7689  CG  LEU C1003     -82.813  44.409 -25.573  1.00 30.64           C  
-ANISOU 7689  CG  LEU C1003     4107   3664   3871    350    517    365       C  
-ATOM   7690  CD1 LEU C1003     -83.410  43.142 -24.999  1.00 32.28           C  
-ANISOU 7690  CD1 LEU C1003     4267   3933   4064    334    470    355       C  
-ATOM   7691  CD2 LEU C1003     -81.828  45.019 -24.600  1.00 32.68           C  
-ANISOU 7691  CD2 LEU C1003     4420   3846   4152    313    537    316       C  
-ATOM   7692  N   LYS C1004     -82.619  44.973 -30.015  1.00 29.42           N  
-ANISOU 7692  N   LYS C1004     3909   3581   3689    423    544    479       N  
-ATOM   7693  CA  LYS C1004     -81.856  45.568 -31.112  1.00 31.53           C  
-ANISOU 7693  CA  LYS C1004     4198   3820   3962    428    572    497       C  
-ATOM   7694  C   LYS C1004     -81.048  46.697 -30.520  1.00 30.36           C  
-ANISOU 7694  C   LYS C1004     4120   3569   3846    410    625    479       C  
-ATOM   7695  O   LYS C1004     -81.614  47.640 -29.967  1.00 29.57           O  
-ANISOU 7695  O   LYS C1004     4063   3427   3747    452    674    497       O  
-ATOM   7696  CB  LYS C1004     -82.799  46.072 -32.169  1.00 34.73           C  
-ANISOU 7696  CB  LYS C1004     4589   4272   4334    509    599    564       C  
-ATOM   7697  CG  LYS C1004     -82.140  46.602 -33.433  1.00 41.19           C  
-ANISOU 7697  CG  LYS C1004     5425   5074   5151    525    629    593       C  
-ATOM   7698  CD  LYS C1004     -83.224  46.825 -34.493  1.00 45.77           C  
-ANISOU 7698  CD  LYS C1004     5975   5732   5685    612    641    659       C  
-ATOM   7699  CE  LYS C1004     -82.848  47.906 -35.473  1.00 49.47           C  
-ANISOU 7699  CE  LYS C1004     6488   6159   6150    660    703    708       C  
-ATOM   7700  NZ  LYS C1004     -83.900  48.065 -36.503  1.00 52.36           N  
-ANISOU 7700  NZ  LYS C1004     6819   6614   6463    752    711    773       N  
-ATOM   7701  N   LEU C1005     -79.729  46.569 -30.584  1.00 30.86           N  
-ANISOU 7701  N   LEU C1005     4195   3595   3935    346    617    438       N  
-ATOM   7702  CA  LEU C1005     -78.815  47.531 -29.991  1.00 33.01           C  
-ANISOU 7702  CA  LEU C1005     4527   3774   4240    308    662    406       C  
-ATOM   7703  C   LEU C1005     -77.976  48.263 -31.058  1.00 34.38           C  
-ANISOU 7703  C   LEU C1005     4729   3906   4428    301    707    426       C  
-ATOM   7704  O   LEU C1005     -77.479  47.632 -31.986  1.00 36.60           O  
-ANISOU 7704  O   LEU C1005     4974   4230   4704    286    679    431       O  
-ATOM   7705  CB  LEU C1005     -77.843  46.808 -29.060  1.00 34.80           C  
-ANISOU 7705  CB  LEU C1005     4740   3997   4485    230    618    336       C  
-ATOM   7706  CG  LEU C1005     -78.371  46.060 -27.838  1.00 33.81           C  
-ANISOU 7706  CG  LEU C1005     4594   3901   4349    223    576    306       C  
-ATOM   7707  CD1 LEU C1005     -77.212  45.443 -27.109  1.00 34.08           C  
-ANISOU 7707  CD1 LEU C1005     4618   3933   4398    152    538    242       C  
-ATOM   7708  CD2 LEU C1005     -79.106  47.012 -26.937  1.00 35.90           C  
-ANISOU 7708  CD2 LEU C1005     4906   4119   4614    257    621    312       C  
-ATOM   7709  N   LYS C1006     -77.775  49.570 -30.866  1.00 34.06           N  
-ANISOU 7709  N   LYS C1006     4756   3777   4407    307    780    433       N  
-ATOM   7710  CA  LYS C1006     -76.831  50.330 -31.637  1.00 34.97           C  
-ANISOU 7710  CA  LYS C1006     4908   3836   4544    284    830    441       C  
-ATOM   7711  C   LYS C1006     -75.599  50.389 -30.804  1.00 33.10           C  
-ANISOU 7711  C   LYS C1006     4684   3551   4340    190    825    366       C  
-ATOM   7712  O   LYS C1006     -75.658  50.762 -29.636  1.00 31.95           O  
-ANISOU 7712  O   LYS C1006     4571   3364   4207    168    836    326       O  
-ATOM   7713  CB  LYS C1006     -77.291  51.780 -31.930  1.00 37.48           C  
-ANISOU 7713  CB  LYS C1006     5302   4074   4865    342    924    491       C  
-ATOM   7714  N   PHE C1007     -74.490  50.001 -31.415  1.00 33.04           N  
-ANISOU 7714  N   PHE C1007     4649   3559   4345    137    807    347       N  
-ATOM   7715  CA  PHE C1007     -73.177  50.152 -30.824  1.00 35.41           C  
-ANISOU 7715  CA  PHE C1007     4956   3824   4675     46    808    279       C  
-ATOM   7716  C   PHE C1007     -72.601  51.483 -31.325  1.00 37.96           C  
-ANISOU 7716  C   PHE C1007     5342   4056   5025     26    896    292       C  
-ATOM   7717  O   PHE C1007     -72.401  51.645 -32.513  1.00 34.85           O  
-ANISOU 7717  O   PHE C1007     4946   3665   4629     46    923    338       O  
-ATOM   7718  CB  PHE C1007     -72.265  49.004 -31.300  1.00 33.78           C  
-ANISOU 7718  CB  PHE C1007     4683   3689   4464      5    746    256       C  
-ATOM   7719  CG  PHE C1007     -72.608  47.641 -30.714  1.00 30.73           C  
-ANISOU 7719  CG  PHE C1007     4241   3380   4054      9    664    233       C  
-ATOM   7720  CD1 PHE C1007     -73.792  47.003 -31.029  1.00 30.52           C  
-ANISOU 7720  CD1 PHE C1007     4191   3406   4000     74    635    275       C  
-ATOM   7721  CD2 PHE C1007     -71.713  46.988 -29.900  1.00 30.54           C  
-ANISOU 7721  CD2 PHE C1007     4187   3379   4035    -51    619    169       C  
-ATOM   7722  CE1 PHE C1007     -74.086  45.734 -30.534  1.00 29.03           C  
-ANISOU 7722  CE1 PHE C1007     3956   3281   3792     72    566    255       C  
-ATOM   7723  CE2 PHE C1007     -72.011  45.730 -29.378  1.00 29.53           C  
-ANISOU 7723  CE2 PHE C1007     4017   3317   3887    -42    551    153       C  
-ATOM   7724  CZ  PHE C1007     -73.194  45.102 -29.714  1.00 27.96           C  
-ANISOU 7724  CZ  PHE C1007     3801   3159   3664     16    527    196       C  
-ATOM   7725  N   ASN C1008     -72.344  52.413 -30.414  1.00 41.68           N  
-ANISOU 7725  N   ASN C1008     5869   4446   5521    -15    943    251       N  
-ATOM   7726  CA  ASN C1008     -71.687  53.668 -30.754  1.00 43.10           C  
-ANISOU 7726  CA  ASN C1008     6114   4530   5733    -52   1031    250       C  
-ATOM   7727  C   ASN C1008     -70.214  53.564 -30.416  1.00 41.43           C  
-ANISOU 7727  C   ASN C1008     5878   4318   5547   -163   1017    175       C  
-ATOM   7728  O   ASN C1008     -69.812  53.761 -29.270  1.00 39.85           O  
-ANISOU 7728  O   ASN C1008     5687   4094   5358   -224   1010    104       O  
-ATOM   7729  CB  ASN C1008     -72.333  54.824 -30.002  1.00 44.96           C  
-ANISOU 7729  CB  ASN C1008     6434   4669   5977    -30   1100    249       C  
-ATOM   7730  CG  ASN C1008     -73.767  55.045 -30.434  1.00 50.23           C  
-ANISOU 7730  CG  ASN C1008     7127   5341   6616     88   1124    331       C  
-ATOM   7731  OD1 ASN C1008     -74.071  55.089 -31.629  1.00 53.99           O  
-ANISOU 7731  OD1 ASN C1008     7599   5836   7079    147   1145    402       O  
-ATOM   7732  ND2 ASN C1008     -74.664  55.157 -29.469  1.00 55.98           N  
-ANISOU 7732  ND2 ASN C1008     7877   6061   7332    127   1119    323       N  
-ATOM   7733  N   PHE C1009     -69.405  53.271 -31.428  1.00 44.36           N  
-ANISOU 7733  N   PHE C1009     6212   4719   5922   -188   1013    190       N  
-ATOM   7734  CA  PHE C1009     -67.954  53.113 -31.243  1.00 47.47           C  
-ANISOU 7734  CA  PHE C1009     6569   5128   6337   -290    999    124       C  
-ATOM   7735  C   PHE C1009     -67.221  54.440 -30.943  1.00 49.75           C  
-ANISOU 7735  C   PHE C1009     6922   5315   6666   -370   1084     84       C  
-ATOM   7736  O   PHE C1009     -67.603  55.478 -31.459  1.00 54.23           O  
-ANISOU 7736  O   PHE C1009     7562   5794   7248   -342   1169    130       O  
-ATOM   7737  CB  PHE C1009     -67.377  52.409 -32.457  1.00 47.24           C  
-ANISOU 7737  CB  PHE C1009     6485   5166   6300   -285    974    157       C  
-ATOM   7738  CG  PHE C1009     -67.811  50.984 -32.565  1.00 46.22           C  
-ANISOU 7738  CG  PHE C1009     6288   5139   6135   -235    883    170       C  
-ATOM   7739  CD1 PHE C1009     -68.924  50.640 -33.324  1.00 48.11           C  
-ANISOU 7739  CD1 PHE C1009     6527   5407   6347   -143    873    241       C  
-ATOM   7740  CD2 PHE C1009     -67.126  49.982 -31.884  1.00 47.11           C  
-ANISOU 7740  CD2 PHE C1009     6339   5322   6240   -280    810    110       C  
-ATOM   7741  CE1 PHE C1009     -69.334  49.314 -33.418  1.00 46.85           C  
-ANISOU 7741  CE1 PHE C1009     6308   5338   6157   -106    793    246       C  
-ATOM   7742  CE2 PHE C1009     -67.529  48.651 -31.982  1.00 45.93           C  
-ANISOU 7742  CE2 PHE C1009     6136   5258   6059   -236    733    122       C  
-ATOM   7743  CZ  PHE C1009     -68.638  48.324 -32.744  1.00 44.79           C  
-ANISOU 7743  CZ  PHE C1009     5993   5133   5891   -154    726    188       C  
-ATOM   7744  N   LYS C1010     -66.225  54.400 -30.060  1.00 52.08           N  
-ANISOU 7744  N   LYS C1010     7191   5621   6975   -466   1062     -3       N  
-ATOM   7745  CA  LYS C1010     -65.492  55.613 -29.641  1.00 57.96           C  
-ANISOU 7745  CA  LYS C1010     7992   6274   7757   -559   1138    -58       C  
-ATOM   7746  C   LYS C1010     -64.306  55.954 -30.550  1.00 60.54           C  
-ANISOU 7746  C   LYS C1010     8302   6590   8109   -630   1182    -59       C  
-ATOM   7747  O   LYS C1010     -63.980  55.201 -31.466  1.00 61.78           O  
-ANISOU 7747  O   LYS C1010     8401   6820   8254   -607   1148    -21       O  
-ATOM   7748  CB  LYS C1010     -65.035  55.520 -28.166  1.00 58.50           C  
-ANISOU 7748  CB  LYS C1010     8042   6363   7824   -632   1098   -159       C  
-TER    7749      LYS C1010                                                      
-ATOM   7750  N   SER D 663     -95.841   5.962 -42.016  1.00 94.09           N  
-ANISOU 7750  N   SER D 663    11528  13740  10483   1484    363  -1340       N  
-ATOM   7751  CA  SER D 663     -96.047   6.750 -40.758  1.00 88.61           C  
-ANISOU 7751  CA  SER D 663    10895  12870   9902   1342    399  -1182       C  
-ATOM   7752  C   SER D 663     -95.213   6.202 -39.607  1.00 87.83           C  
-ANISOU 7752  C   SER D 663    10872  12597   9902   1318    398  -1170       C  
-ATOM   7753  O   SER D 663     -95.241   4.999 -39.341  1.00 84.56           O  
-ANISOU 7753  O   SER D 663    10519  12058   9552   1345    353  -1310       O  
-ATOM   7754  CB  SER D 663     -97.527   6.785 -40.311  1.00 88.60           C  
-ANISOU 7754  CB  SER D 663    10954  12718   9993   1233    378  -1214       C  
-ATOM   7755  OG  SER D 663     -97.653   7.361 -39.007  1.00 85.05           O  
-ANISOU 7755  OG  SER D 663    10569  12093   9655   1110    405  -1087       O  
-ATOM   7756  N   LYS D 664     -94.521   7.090 -38.896  1.00 87.29           N  
-ANISOU 7756  N   LYS D 664    10798  12511   9856   1264    445  -1002       N  
-ATOM   7757  CA  LYS D 664     -93.828   6.714 -37.659  1.00 85.99           C  
-ANISOU 7757  CA  LYS D 664    10705  12177   9788   1228    447   -973       C  
-ATOM   7758  C   LYS D 664     -94.762   6.658 -36.432  1.00 78.21           C  
-ANISOU 7758  C   LYS D 664     9815  10961   8941   1103    437   -959       C  
-ATOM   7759  O   LYS D 664     -94.351   6.171 -35.391  1.00 76.75           O  
-ANISOU 7759  O   LYS D 664     9695  10628   8839   1078    432   -953       O  
-ATOM   7760  CB  LYS D 664     -92.668   7.675 -37.364  1.00 86.64           C  
-ANISOU 7760  CB  LYS D 664    10736  12341   9843   1223    496   -810       C  
-ATOM   7761  N   LEU D 665     -96.009   7.131 -36.553  1.00 72.92           N  
-ANISOU 7761  N   LEU D 665     9148  10269   8288   1031    434   -952       N  
-ATOM   7762  CA  LEU D 665     -96.910   7.223 -35.394  1.00 67.18           C  
-ANISOU 7762  CA  LEU D 665     8498   9348   7680    912    430   -921       C  
-ATOM   7763  C   LEU D 665     -97.410   5.857 -34.916  1.00 62.85           C  
-ANISOU 7763  C   LEU D 665     8030   8625   7224    905    385  -1053       C  
-ATOM   7764  O   LEU D 665     -97.680   4.983 -35.728  1.00 67.65           O  
-ANISOU 7764  O   LEU D 665     8630   9262   7810    969    347  -1194       O  
-ATOM   7765  CB  LEU D 665     -98.144   8.065 -35.716  1.00 65.81           C  
-ANISOU 7765  CB  LEU D 665     8301   9208   7496    846    437   -885       C  
-ATOM   7766  CG  LEU D 665     -97.930   9.516 -36.120  1.00 64.73           C  
-ANISOU 7766  CG  LEU D 665     8087   9214   7294    833    479   -740       C  
-ATOM   7767  CD1 LEU D 665     -99.220  10.095 -36.669  1.00 64.67           C  
-ANISOU 7767  CD1 LEU D 665     8054   9253   7264    793    476   -739       C  
-ATOM   7768  CD2 LEU D 665     -97.429  10.336 -34.949  1.00 64.79           C  
-ANISOU 7768  CD2 LEU D 665     8113   9131   7372    759    509   -603       C  
-ATOM   7769  N   PRO D 666     -97.561   5.680 -33.597  1.00 57.59           N  
-ANISOU 7769  N   PRO D 666     7436   7781   6666    827    388  -1006       N  
-ATOM   7770  CA  PRO D 666     -98.151   4.458 -33.055  1.00 57.05           C  
-ANISOU 7770  CA  PRO D 666     7441   7533   6703    803    351  -1103       C  
-ATOM   7771  C   PRO D 666     -99.549   4.204 -33.626  1.00 59.14           C  
-ANISOU 7771  C   PRO D 666     7703   7779   6987    766    320  -1197       C  
-ATOM   7772  O   PRO D 666    -100.258   5.157 -33.981  1.00 58.17           O  
-ANISOU 7772  O   PRO D 666     7543   7740   6818    723    336  -1148       O  
-ATOM   7773  CB  PRO D 666     -98.250   4.748 -31.562  1.00 58.27           C  
-ANISOU 7773  CB  PRO D 666     7650   7545   6945    711    373   -992       C  
-ATOM   7774  CG  PRO D 666     -97.269   5.836 -31.297  1.00 56.36           C  
-ANISOU 7774  CG  PRO D 666     7369   7398   6646    717    414   -865       C  
-ATOM   7775  CD  PRO D 666     -97.205   6.650 -32.548  1.00 55.99           C  
-ANISOU 7775  CD  PRO D 666     7241   7540   6492    758    427   -856       C  
-ATOM   7776  N   LYS D 667     -99.929   2.934 -33.731  1.00 61.73           N  
-ANISOU 7776  N   LYS D 667     8068   7998   7388    785    273  -1331       N  
-ATOM   7777  CA  LYS D 667    -101.217   2.561 -34.321  1.00 63.30           C  
-ANISOU 7777  CA  LYS D 667     8260   8177   7614    756    236  -1441       C  
-ATOM   7778  C   LYS D 667    -102.376   3.302 -33.629  1.00 62.13           C  
-ANISOU 7778  C   LYS D 667     8129   7966   7510    632    257  -1351       C  
-ATOM   7779  O   LYS D 667    -103.204   3.913 -34.312  1.00 59.85           O  
-ANISOU 7779  O   LYS D 667     7798   7777   7167    612    256  -1365       O  
-ATOM   7780  CB  LYS D 667    -101.432   1.035 -34.284  1.00 61.25           C  
-ANISOU 7780  CB  LYS D 667     8043   7762   7465    778    180  -1589       C  
-ATOM   7781  N   PRO D 668    -102.416   3.287 -32.278  1.00 60.74           N  
-ANISOU 7781  N   PRO D 668     8012   7642   7426    555    276  -1254       N  
-ATOM   7782  CA  PRO D 668    -103.494   3.981 -31.543  1.00 59.77           C  
-ANISOU 7782  CA  PRO D 668     7902   7465   7341    444    295  -1170       C  
-ATOM   7783  C   PRO D 668    -103.673   5.439 -31.935  1.00 55.28           C  
-ANISOU 7783  C   PRO D 668     7281   7048   6676    428    328  -1084       C  
-ATOM   7784  O   PRO D 668    -104.798   5.904 -32.089  1.00 53.92           O  
-ANISOU 7784  O   PRO D 668     7093   6892   6502    370    326  -1083       O  
-ATOM   7785  CB  PRO D 668    -103.046   3.885 -30.086  1.00 58.46           C  
-ANISOU 7785  CB  PRO D 668     7791   7172   7251    401    318  -1064       C  
-ATOM   7786  CG  PRO D 668    -102.185   2.663 -30.049  1.00 60.70           C  
-ANISOU 7786  CG  PRO D 668     8105   7377   7582    471    295  -1132       C  
-ATOM   7787  CD  PRO D 668    -101.451   2.665 -31.354  1.00 60.62           C  
-ANISOU 7787  CD  PRO D 668     8044   7516   7471    576    282  -1215       C  
-ATOM   7788  N   VAL D 669    -102.566   6.124 -32.174  1.00 55.55           N  
-ANISOU 7788  N   VAL D 669     7280   7193   6632    484    355  -1016       N  
-ATOM   7789  CA  VAL D 669    -102.597   7.518 -32.600  1.00 57.87           C  
-ANISOU 7789  CA  VAL D 669     7516   7627   6845    476    387   -923       C  
-ATOM   7790  C   VAL D 669    -103.139   7.632 -34.024  1.00 58.22           C  
-ANISOU 7790  C   VAL D 669     7500   7817   6803    523    371  -1000       C  
-ATOM   7791  O   VAL D 669    -103.998   8.480 -34.321  1.00 59.53           O  
-ANISOU 7791  O   VAL D 669     7635   8045   6940    483    381   -962       O  
-ATOM   7792  CB  VAL D 669    -101.200   8.163 -32.503  1.00 58.75           C  
-ANISOU 7792  CB  VAL D 669     7599   7817   6908    522    419   -827       C  
-ATOM   7793  CG1 VAL D 669    -101.242   9.611 -32.951  1.00 60.84           C  
-ANISOU 7793  CG1 VAL D 669     7797   8211   7107    509    450   -722       C  
-ATOM   7794  CG2 VAL D 669    -100.684   8.080 -31.074  1.00 58.41           C  
-ANISOU 7794  CG2 VAL D 669     7608   7641   6942    480    432   -757       C  
-ATOM   7795  N   GLN D 670    -102.647   6.767 -34.898  1.00 60.11           N  
-ANISOU 7795  N   GLN D 670     7721   8119   7001    615    345  -1114       N  
-ATOM   7796  CA  GLN D 670    -103.135   6.718 -36.266  1.00 63.14           C  
-ANISOU 7796  CA  GLN D 670     8043   8652   7296    676    324  -1210       C  
-ATOM   7797  C   GLN D 670    -104.640   6.503 -36.292  1.00 61.21           C  
-ANISOU 7797  C   GLN D 670     7813   8344   7100    607    295  -1281       C  
-ATOM   7798  O   GLN D 670    -105.349   7.195 -37.011  1.00 60.92           O  
-ANISOU 7798  O   GLN D 670     7724   8429   6995    606    300  -1273       O  
-ATOM   7799  CB  GLN D 670    -102.417   5.612 -37.061  1.00 69.96           C  
-ANISOU 7799  CB  GLN D 670     8890   9568   8122    789    289  -1351       C  
-ATOM   7800  CG  GLN D 670    -100.962   5.925 -37.418  1.00 70.08           C  
-ANISOU 7800  CG  GLN D 670     8863   9716   8050    880    317  -1290       C  
-ATOM   7801  CD  GLN D 670    -100.309   4.804 -38.212  1.00 68.20           C  
-ANISOU 7801  CD  GLN D 670     8606   9536   7771   1000    278  -1444       C  
-ATOM   7802  OE1 GLN D 670    -100.967   4.151 -39.012  1.00 69.33           O  
-ANISOU 7802  OE1 GLN D 670     8730   9715   7898   1041    233  -1594       O  
-ATOM   7803  NE2 GLN D 670     -99.019   4.590 -38.004  1.00 65.59           N  
-ANISOU 7803  NE2 GLN D 670     8277   9220   7423   1061    291  -1413       N  
-ATOM   7804  N   ASP D 671    -105.122   5.551 -35.502  1.00 61.65           N  
-ANISOU 7804  N   ASP D 671     7934   8213   7276    551    268  -1342       N  
-ATOM   7805  CA  ASP D 671    -106.564   5.292 -35.399  1.00 63.64           C  
-ANISOU 7805  CA  ASP D 671     8200   8389   7593    473    242  -1403       C  
-ATOM   7806  C   ASP D 671    -107.352   6.512 -34.893  1.00 61.00           C  
-ANISOU 7806  C   ASP D 671     7859   8069   7250    386    276  -1275       C  
-ATOM   7807  O   ASP D 671    -108.451   6.776 -35.371  1.00 59.20           O  
-ANISOU 7807  O   ASP D 671     7601   7890   7001    357    264  -1313       O  
-ATOM   7808  CB  ASP D 671    -106.832   4.051 -34.529  1.00 66.59           C  
-ANISOU 7808  CB  ASP D 671     8641   8548   8112    423    211  -1465       C  
-ATOM   7809  CG  ASP D 671    -106.433   2.722 -35.234  1.00 73.96           C  
-ANISOU 7809  CG  ASP D 671     9574   9457   9073    507    159  -1635       C  
-ATOM   7810  OD1 ASP D 671    -106.056   2.763 -36.434  1.00 73.57           O  
-ANISOU 7810  OD1 ASP D 671     9466   9572   8917    606    143  -1719       O  
-ATOM   7811  OD2 ASP D 671    -106.495   1.645 -34.584  1.00 71.31           O  
-ANISOU 7811  OD2 ASP D 671     9289   8938   8866    479    132  -1683       O  
-ATOM   7812  N   LEU D 672    -106.782   7.255 -33.943  1.00 59.33           N  
-ANISOU 7812  N   LEU D 672     7671   7818   7054    351    317  -1133       N  
-ATOM   7813  CA  LEU D 672    -107.406   8.482 -33.435  1.00 55.28           C  
-ANISOU 7813  CA  LEU D 672     7148   7319   6535    279    347  -1015       C  
-ATOM   7814  C   LEU D 672    -107.516   9.524 -34.545  1.00 55.52           C  
-ANISOU 7814  C   LEU D 672     7105   7537   6455    322    361   -981       C  
-ATOM   7815  O   LEU D 672    -108.564  10.142 -34.712  1.00 54.46           O  
-ANISOU 7815  O   LEU D 672     6948   7437   6306    280    362   -964       O  
-ATOM   7816  CB  LEU D 672    -106.601   9.048 -32.256  1.00 53.27           C  
-ANISOU 7816  CB  LEU D 672     6925   6997   6318    249    380   -885       C  
-ATOM   7817  CG  LEU D 672    -107.065  10.375 -31.654  1.00 52.38           C  
-ANISOU 7817  CG  LEU D 672     6800   6895   6206    185    408   -766       C  
-ATOM   7818  CD1 LEU D 672    -108.405  10.209 -30.965  1.00 50.95           C  
-ANISOU 7818  CD1 LEU D 672     6650   6618   6091     99    395   -783       C  
-ATOM   7819  CD2 LEU D 672    -106.036  10.925 -30.678  1.00 51.82           C  
-ANISOU 7819  CD2 LEU D 672     6745   6785   6161    178    434   -659       C  
-ATOM   7820  N   ILE D 673    -106.438   9.714 -35.304  1.00 56.97           N  
-ANISOU 7820  N   ILE D 673     7245   7845   6557    410    374   -965       N  
-ATOM   7821  CA  ILE D 673    -106.461  10.670 -36.410  1.00 58.16           C  
-ANISOU 7821  CA  ILE D 673     7315   8186   6597    460    392   -917       C  
-ATOM   7822  C   ILE D 673    -107.531  10.322 -37.450  1.00 58.78           C  
-ANISOU 7822  C   ILE D 673     7356   8356   6623    486    360  -1035       C  
-ATOM   7823  O   ILE D 673    -108.235  11.207 -37.935  1.00 57.17           O  
-ANISOU 7823  O   ILE D 673     7105   8250   6366    477    372   -984       O  
-ATOM   7824  CB  ILE D 673    -105.097  10.759 -37.113  1.00 59.34           C  
-ANISOU 7824  CB  ILE D 673     7415   8467   6663    559    410   -888       C  
-ATOM   7825  CG1 ILE D 673    -104.011  11.194 -36.128  1.00 59.09           C  
-ANISOU 7825  CG1 ILE D 673     7411   8360   6682    534    441   -769       C  
-ATOM   7826  CG2 ILE D 673    -105.147  11.747 -38.277  1.00 61.12           C  
-ANISOU 7826  CG2 ILE D 673     7549   8901   6774    614    432   -821       C  
-ATOM   7827  CD1 ILE D 673    -104.409  12.355 -35.250  1.00 59.12           C  
-ANISOU 7827  CD1 ILE D 673     7424   8297   6741    445    466   -640       C  
-ATOM   7828  N   LYS D 674    -107.640   9.046 -37.806  1.00 59.70           N  
-ANISOU 7828  N   LYS D 674     7488   8440   6754    522    317  -1193       N  
-ATOM   7829  CA  LYS D 674    -108.654   8.617 -38.781  1.00 60.87           C  
-ANISOU 7829  CA  LYS D 674     7597   8672   6860    548    279  -1329       C  
-ATOM   7830  C   LYS D 674    -110.047   8.868 -38.228  1.00 59.35           C  
-ANISOU 7830  C   LYS D 674     7428   8389   6733    444    271  -1321       C  
-ATOM   7831  O   LYS D 674    -110.900   9.389 -38.908  1.00 55.21           O  
-ANISOU 7831  O   LYS D 674     6854   7978   6147    449    268  -1331       O  
-ATOM   7832  CB  LYS D 674    -108.469   7.155 -39.185  1.00 57.92           C  
-ANISOU 7832  CB  LYS D 674     7235   8258   6514    604    226  -1514       C  
-ATOM   7833  N   MET D 675    -110.250   8.504 -36.970  1.00 61.03           N  
-ANISOU 7833  N   MET D 675     7713   8407   7068    355    271  -1296       N  
-ATOM   7834  CA  MET D 675    -111.501   8.732 -36.274  1.00 60.72           C  
-ANISOU 7834  CA  MET D 675     7698   8276   7097    253    269  -1273       C  
-ATOM   7835  C   MET D 675    -111.927  10.211 -36.310  1.00 58.99           C  
-ANISOU 7835  C   MET D 675     7442   8153   6818    230    305  -1144       C  
-ATOM   7836  O   MET D 675    -113.091  10.534 -36.615  1.00 59.72           O  
-ANISOU 7836  O   MET D 675     7507   8290   6893    199    294  -1167       O  
-ATOM   7837  CB  MET D 675    -111.304   8.274 -34.840  1.00 63.17           C  
-ANISOU 7837  CB  MET D 675     8084   8389   7529    179    277  -1226       C  
-ATOM   7838  CG  MET D 675    -112.554   8.082 -34.033  1.00 65.54           C  
-ANISOU 7838  CG  MET D 675     8413   8571   7918     76    266  -1229       C  
-ATOM   7839  SD  MET D 675    -112.004   7.546 -32.413  1.00 64.86           S  
-ANISOU 7839  SD  MET D 675     8405   8288   7951     17    282  -1153       S  
-ATOM   7840  CE  MET D 675    -113.587   7.644 -31.573  1.00 68.60           C  
-ANISOU 7840  CE  MET D 675     8890   8678   8498    -99    280  -1130       C  
-ATOM   7841  N   ILE D 676    -110.995  11.117 -36.021  1.00 55.62           N  
-ANISOU 7841  N   ILE D 676     7011   7757   6366    247    344  -1010       N  
-ATOM   7842  CA  ILE D 676    -111.383  12.529 -35.866  1.00 60.06           C  
-ANISOU 7842  CA  ILE D 676     7545   8371   6903    215    374   -880       C  
-ATOM   7843  C   ILE D 676    -111.491  13.266 -37.187  1.00 57.77           C  
-ANISOU 7843  C   ILE D 676     7173   8279   6497    287    383   -858       C  
-ATOM   7844  O   ILE D 676    -112.211  14.256 -37.269  1.00 53.84           O  
-ANISOU 7844  O   ILE D 676     6646   7830   5980    262    396   -785       O  
-ATOM   7845  CB  ILE D 676    -110.552  13.312 -34.812  1.00 58.04           C  
-ANISOU 7845  CB  ILE D 676     7317   8039   6697    183    408   -742       C  
-ATOM   7846  CG1 ILE D 676    -109.122  13.546 -35.235  1.00 57.75           C  
-ANISOU 7846  CG1 ILE D 676     7252   8079   6612    255    430   -685       C  
-ATOM   7847  CG2 ILE D 676    -110.590  12.591 -33.471  1.00 57.84           C  
-ANISOU 7847  CG2 ILE D 676     7367   7834   6777    115    400   -760       C  
-ATOM   7848  CD1 ILE D 676    -108.374  14.217 -34.100  1.00 61.07           C  
-ANISOU 7848  CD1 ILE D 676     7699   8408   7096    215    455   -568       C  
-ATOM   7849  N   PHE D 677    -110.804  12.776 -38.218  1.00 63.95           N  
-ANISOU 7849  N   PHE D 677     7916   9184   7200    380    375   -920       N  
-ATOM   7850  CA  PHE D 677    -110.924  13.356 -39.569  1.00 65.26           C  
-ANISOU 7850  CA  PHE D 677     7992   9564   7239    462    383   -905       C  
-ATOM   7851  C   PHE D 677    -111.821  12.537 -40.508  1.00 68.23           C  
-ANISOU 7851  C   PHE D 677     8336  10027   7560    502    339  -1073       C  
-ATOM   7852  O   PHE D 677    -111.776  12.711 -41.722  1.00 69.32           O  
-ANISOU 7852  O   PHE D 677     8397  10362   7580    592    338  -1095       O  
-ATOM   7853  CB  PHE D 677    -109.546  13.550 -40.189  1.00 65.26           C  
-ANISOU 7853  CB  PHE D 677     7946   9687   7164    553    408   -844       C  
-ATOM   7854  CG  PHE D 677    -108.813  14.741 -39.668  1.00 61.21           C  
-ANISOU 7854  CG  PHE D 677     7425   9157   6677    527    454   -658       C  
-ATOM   7855  CD1 PHE D 677    -109.230  16.017 -39.994  1.00 61.16           C  
-ANISOU 7855  CD1 PHE D 677     7364   9234   6639    521    480   -530       C  
-ATOM   7856  CD2 PHE D 677    -107.688  14.588 -38.881  1.00 59.90           C  
-ANISOU 7856  CD2 PHE D 677     7298   8890   6569    514    468   -612       C  
-ATOM   7857  CE1 PHE D 677    -108.549  17.130 -39.529  1.00 60.10           C  
-ANISOU 7857  CE1 PHE D 677     7216   9072   6546    495    517   -362       C  
-ATOM   7858  CE2 PHE D 677    -106.993  15.692 -38.420  1.00 57.09           C  
-ANISOU 7858  CE2 PHE D 677     6926   8520   6246    490    505   -450       C  
-ATOM   7859  CZ  PHE D 677    -107.423  16.967 -38.742  1.00 58.14           C  
-ANISOU 7859  CZ  PHE D 677     7004   8724   6360    478    528   -326       C  
-ATOM   7860  N   ASP D 678    -112.687  11.703 -39.934  1.00 70.52           N  
-ANISOU 7860  N   ASP D 678     8678  10176   7939    432    303  -1184       N  
-ATOM   7861  CA  ASP D 678    -113.585  10.850 -40.705  1.00 71.55           C  
-ANISOU 7861  CA  ASP D 678     8781  10361   8045    456    254  -1358       C  
-ATOM   7862  C   ASP D 678    -114.701  11.662 -41.385  1.00 72.35           C  
-ANISOU 7862  C   ASP D 678     8819  10603   8068    460    255  -1339       C  
-ATOM   7863  O   ASP D 678    -115.675  12.071 -40.752  1.00 72.56           O  
-ANISOU 7863  O   ASP D 678     8869  10550   8151    374    258  -1300       O  
-ATOM   7864  CB  ASP D 678    -114.179   9.776 -39.791  1.00 73.95           C  
-ANISOU 7864  CB  ASP D 678     9155  10456   8487    366    218  -1460       C  
-ATOM   7865  CG  ASP D 678    -114.860   8.657 -40.558  1.00 77.46           C  
-ANISOU 7865  CG  ASP D 678     9571  10926   8932    394    158  -1664       C  
-ATOM   7866  OD1 ASP D 678    -115.485   8.924 -41.600  1.00 78.68           O  
-ANISOU 7866  OD1 ASP D 678     9655  11251   8989    446    142  -1723       O  
-ATOM   7867  OD2 ASP D 678    -114.763   7.500 -40.115  1.00 79.25           O  
-ANISOU 7867  OD2 ASP D 678     9845  11001   9265    366    124  -1767       O  
-ATOM   7868  N   VAL D 679    -114.554  11.843 -42.695  1.00 74.33           N  
-ANISOU 7868  N   VAL D 679     8987  11072   8184    567    252  -1371       N  
-ATOM   7869  CA  VAL D 679    -115.493  12.618 -43.516  1.00 72.43           C  
-ANISOU 7869  CA  VAL D 679     8672  11001   7846    596    255  -1348       C  
-ATOM   7870  C   VAL D 679    -116.896  11.984 -43.543  1.00 69.19           C  
-ANISOU 7870  C   VAL D 679     8264  10551   7475    545    206  -1499       C  
-ATOM   7871  O   VAL D 679    -117.904  12.686 -43.506  1.00 63.02           O  
-ANISOU 7871  O   VAL D 679     7464   9800   6682    505    213  -1451       O  
-ATOM   7872  CB  VAL D 679    -114.932  12.763 -44.953  1.00 74.71           C  
-ANISOU 7872  CB  VAL D 679     8864  11550   7972    737    259  -1363       C  
-ATOM   7873  CG1 VAL D 679    -115.952  13.395 -45.888  1.00 75.88           C  
-ANISOU 7873  CG1 VAL D 679     8929  11890   8011    780    255  -1361       C  
-ATOM   7874  CG2 VAL D 679    -113.655  13.587 -44.919  1.00 74.31           C  
-ANISOU 7874  CG2 VAL D 679     8799  11549   7886    777    314  -1181       C  
-ATOM   7875  N   GLU D 680    -116.955  10.657 -43.587  1.00 68.83           N  
-ANISOU 7875  N   GLU D 680     8240  10430   7484    544    154  -1682       N  
-ATOM   7876  CA  GLU D 680    -118.239   9.959 -43.547  1.00 68.13           C  
-ANISOU 7876  CA  GLU D 680     8150  10279   7456    485    104  -1830       C  
-ATOM   7877  C   GLU D 680    -118.965  10.227 -42.212  1.00 67.78           C  
-ANISOU 7877  C   GLU D 680     8175  10038   7540    346    121  -1744       C  
-ATOM   7878  O   GLU D 680    -120.185  10.399 -42.211  1.00 62.03           O  
-ANISOU 7878  O   GLU D 680     7426   9322   6820    296    105  -1775       O  
-ATOM   7879  CB  GLU D 680    -118.079   8.443 -43.797  1.00 66.35           C  
-ANISOU 7879  CB  GLU D 680     7935   9985   7292    507     42  -2042       C  
-ATOM   7880  N   SER D 681    -118.226  10.292 -41.094  1.00 63.59           N  
-ANISOU 7880  N   SER D 681     7719   9344   7099    291    152  -1637       N  
-ATOM   7881  CA  SER D 681    -118.825  10.665 -39.801  1.00 62.86           C  
-ANISOU 7881  CA  SER D 681     7684   9090   7109    173    173  -1540       C  
-ATOM   7882  C   SER D 681    -119.375  12.078 -39.814  1.00 59.60           C  
-ANISOU 7882  C   SER D 681     7240   8772   6634    164    208  -1404       C  
-ATOM   7883  O   SER D 681    -120.433  12.332 -39.251  1.00 55.88           O  
-ANISOU 7883  O   SER D 681     6779   8245   6208     87    206  -1388       O  
-ATOM   7884  CB  SER D 681    -117.842  10.535 -38.653  1.00 61.10           C  
-ANISOU 7884  CB  SER D 681     7537   8703   6976    133    200  -1449       C  
-ATOM   7885  OG  SER D 681    -117.580   9.168 -38.400  1.00 62.58           O  
-ANISOU 7885  OG  SER D 681     7762   8761   7253    118    165  -1569       O  
-ATOM   7886  N   MET D 682    -118.664  12.986 -40.474  1.00 58.02           N  
-ANISOU 7886  N   MET D 682     6998   8716   6332    245    240  -1304       N  
-ATOM   7887  CA  MET D 682    -119.147  14.359 -40.646  1.00 59.71           C  
-ANISOU 7887  CA  MET D 682     7172   9028   6486    250    271  -1172       C  
-ATOM   7888  C   MET D 682    -120.490  14.389 -41.392  1.00 60.47           C  
-ANISOU 7888  C   MET D 682     7210   9244   6522    260    243  -1258       C  
-ATOM   7889  O   MET D 682    -121.450  15.001 -40.930  1.00 60.07           O  
-ANISOU 7889  O   MET D 682     7163   9165   6497    201    248  -1208       O  
-ATOM   7890  CB  MET D 682    -118.109  15.207 -41.382  1.00 60.11           C  
-ANISOU 7890  CB  MET D 682     7175   9223   6442    344    307  -1053       C  
-ATOM   7891  CG  MET D 682    -116.792  15.388 -40.632  1.00 62.56           C  
-ANISOU 7891  CG  MET D 682     7533   9428   6810    332    339   -949       C  
-ATOM   7892  SD  MET D 682    -115.580  16.249 -41.646  1.00 64.75           S  
-ANISOU 7892  SD  MET D 682     7736   9892   6974    444    379   -818       S  
-ATOM   7893  CE  MET D 682    -114.038  15.602 -41.031  1.00 61.58           C  
-ANISOU 7893  CE  MET D 682     7389   9379   6631    448    389   -813       C  
-ATOM   7894  N   LYS D 683    -120.568  13.685 -42.515  1.00 62.09           N  
-ANISOU 7894  N   LYS D 683     7360   9583   6648    335    208  -1397       N  
-ATOM   7895  CA  LYS D 683    -121.804  13.637 -43.292  1.00 63.46           C  
-ANISOU 7895  CA  LYS D 683     7470   9885   6758    353    176  -1497       C  
-ATOM   7896  C   LYS D 683    -122.938  12.930 -42.564  1.00 62.80           C  
-ANISOU 7896  C   LYS D 683     7421   9657   6784    245    141  -1601       C  
-ATOM   7897  O   LYS D 683    -124.066  13.397 -42.610  1.00 63.92           O  
-ANISOU 7897  O   LYS D 683     7532   9846   6906    214    135  -1597       O  
-ATOM   7898  CB  LYS D 683    -121.562  12.962 -44.636  1.00 66.56           C  
-ANISOU 7898  CB  LYS D 683     7791  10459   7041    465    141  -1642       C  
-ATOM   7899  N   LYS D 684    -122.642  11.815 -41.898  1.00 66.53           N  
-ANISOU 7899  N   LYS D 684     7953   9955   7372    188    117  -1687       N  
-ATOM   7900  CA  LYS D 684    -123.651  11.092 -41.130  1.00 69.85           C  
-ANISOU 7900  CA  LYS D 684     8403  10223   7913     78     87  -1768       C  
-ATOM   7901  C   LYS D 684    -124.251  12.015 -40.095  1.00 71.25           C  
-ANISOU 7901  C   LYS D 684     8612  10327   8132     -5    124  -1623       C  
-ATOM   7902  O   LYS D 684    -125.456  12.043 -39.923  1.00 73.86           O  
-ANISOU 7902  O   LYS D 684     8922  10655   8484    -64    108  -1657       O  
-ATOM   7903  CB  LYS D 684    -123.058   9.888 -40.383  1.00 74.41           C  
-ANISOU 7903  CB  LYS D 684     9047  10601   8624     27     69  -1831       C  
-ATOM   7904  CG  LYS D 684    -124.075   8.851 -39.935  1.00 81.98           C  
-ANISOU 7904  CG  LYS D 684    10014  11427   9707    -68     24  -1952       C  
-ATOM   7905  CD  LYS D 684    -123.452   7.864 -38.956  1.00 90.21           C  
-ANISOU 7905  CD  LYS D 684    11131  12251  10895   -128     20  -1957       C  
-ATOM   7906  CE  LYS D 684    -124.457   6.808 -38.500  1.00 97.32           C  
-ANISOU 7906  CE  LYS D 684    12033  13010  11935   -228    -22  -2062       C  
-ATOM   7907  NZ  LYS D 684    -123.940   5.951 -37.389  1.00 98.52           N  
-ANISOU 7907  NZ  LYS D 684    12257  12940  12237   -296    -18  -2028       N  
-ATOM   7908  N   ALA D 685    -123.399  12.756 -39.389  1.00 70.39           N  
-ANISOU 7908  N   ALA D 685     8550  10159   8038     -9    170  -1467       N  
-ATOM   7909  CA  ALA D 685    -123.856  13.698 -38.383  1.00 69.06           C  
-ANISOU 7909  CA  ALA D 685     8409   9924   7907    -76    202  -1333       C  
-ATOM   7910  C   ALA D 685    -124.859  14.652 -39.014  1.00 68.11           C  
-ANISOU 7910  C   ALA D 685     8225   9955   7698    -50    204  -1306       C  
-ATOM   7911  O   ALA D 685    -125.912  14.896 -38.439  1.00 64.74           O  
-ANISOU 7911  O   ALA D 685     7798   9492   7307   -116    200  -1295       O  
-ATOM   7912  CB  ALA D 685    -122.683  14.469 -37.784  1.00 67.92           C  
-ANISOU 7912  CB  ALA D 685     8305   9729   7773    -59    245  -1181       C  
-ATOM   7913  N   MET D 686    -124.524  15.183 -40.192  1.00 67.73           N  
-ANISOU 7913  N   MET D 686     8117  10085   7532     52    210  -1289       N  
-ATOM   7914  CA  MET D 686    -125.398  16.142 -40.884  1.00 68.27           C  
-ANISOU 7914  CA  MET D 686     8119  10314   7507     92    214  -1249       C  
-ATOM   7915  C   MET D 686    -126.722  15.498 -41.324  1.00 69.67           C  
-ANISOU 7915  C   MET D 686     8252  10551   7669     69    170  -1401       C  
-ATOM   7916  O   MET D 686    -127.793  16.107 -41.221  1.00 65.92           O  
-ANISOU 7916  O   MET D 686     7750  10118   7177     43    170  -1374       O  
-ATOM   7917  CB  MET D 686    -124.673  16.784 -42.072  1.00 67.14           C  
-ANISOU 7917  CB  MET D 686     7915  10358   7238    213    234  -1186       C  
-ATOM   7918  CG  MET D 686    -123.532  17.703 -41.649  1.00 66.02           C  
-ANISOU 7918  CG  MET D 686     7801  10169   7114    229    281  -1009       C  
-ATOM   7919  SD  MET D 686    -122.525  18.366 -42.984  1.00 67.20           S  
-ANISOU 7919  SD  MET D 686     7874  10529   7129    365    310   -915       S  
-ATOM   7920  CE  MET D 686    -123.699  19.582 -43.630  1.00 69.62           C  
-ANISOU 7920  CE  MET D 686     8105  10995   7352    403    319   -832       C  
-ATOM   7921  N   VAL D 687    -126.654  14.245 -41.760  1.00 67.58           N  
-ANISOU 7921  N   VAL D 687     7979  10278   7420     75    128  -1565       N  
-ATOM   7922  CA  VAL D 687    -127.863  13.524 -42.094  1.00 67.85           C  
-ANISOU 7922  CA  VAL D 687     7971  10345   7466     41     80  -1722       C  
-ATOM   7923  C   VAL D 687    -128.708  13.360 -40.837  1.00 69.74           C  
-ANISOU 7923  C   VAL D 687     8255  10415   7827    -87     80  -1703       C  
-ATOM   7924  O   VAL D 687    -129.901  13.632 -40.869  1.00 64.55           O  
-ANISOU 7924  O   VAL D 687     7559   9813   7155   -120     68  -1725       O  
-ATOM   7925  CB  VAL D 687    -127.565  12.167 -42.756  1.00 71.61           C  
-ANISOU 7925  CB  VAL D 687     8428  10823   7958     71     28  -1913       C  
-ATOM   7926  CG1 VAL D 687    -128.818  11.310 -42.821  1.00 72.29           C  
-ANISOU 7926  CG1 VAL D 687     8480  10883   8104      6    -26  -2078       C  
-ATOM   7927  CG2 VAL D 687    -126.990  12.388 -44.148  1.00 70.12           C  
-ANISOU 7927  CG2 VAL D 687     8170  10855   7617    212     24  -1949       C  
-ATOM   7928  N   GLU D 688    -128.097  12.961 -39.722  1.00 70.99           N  
-ANISOU 7928  N   GLU D 688     8491  10383   8100   -155     96  -1652       N  
-ATOM   7929  CA  GLU D 688    -128.845  12.797 -38.465  1.00 71.69           C  
-ANISOU 7929  CA  GLU D 688     8617  10322   8299   -272    101  -1619       C  
-ATOM   7930  C   GLU D 688    -129.466  14.094 -37.965  1.00 68.64           C  
-ANISOU 7930  C   GLU D 688     8225   9979   7877   -288    134  -1486       C  
-ATOM   7931  O   GLU D 688    -130.510  14.060 -37.323  1.00 67.71           O  
-ANISOU 7931  O   GLU D 688     8101   9818   7806   -364    128  -1491       O  
-ATOM   7932  CB  GLU D 688    -127.988  12.150 -37.377  1.00 76.10           C  
-ANISOU 7932  CB  GLU D 688     9255  10686   8975   -328    115  -1578       C  
-ATOM   7933  CG  GLU D 688    -127.933  10.629 -37.523  1.00 81.69           C  
-ANISOU 7933  CG  GLU D 688     9967  11297   9773   -359     70  -1729       C  
-ATOM   7934  CD  GLU D 688    -127.083   9.920 -36.461  1.00 86.19           C  
-ANISOU 7934  CD  GLU D 688    10614  11673  10462   -410     84  -1685       C  
-ATOM   7935  OE1 GLU D 688    -125.959   9.463 -36.788  1.00 88.25           O  
-ANISOU 7935  OE1 GLU D 688    10898  11909  10722   -352     80  -1714       O  
-ATOM   7936  OE2 GLU D 688    -127.545   9.802 -35.291  1.00 84.38           O  
-ANISOU 7936  OE2 GLU D 688    10416  11322  10324   -502     99  -1619       O  
-ATOM   7937  N   TYR D 689    -128.864  15.236 -38.289  1.00 68.65           N  
-ANISOU 7937  N   TYR D 689     8221  10067   7797   -213    166  -1371       N  
-ATOM   7938  CA  TYR D 689    -129.472  16.528 -37.961  1.00 69.69           C  
-ANISOU 7938  CA  TYR D 689     8339  10247   7894   -213    190  -1254       C  
-ATOM   7939  C   TYR D 689    -130.560  16.920 -38.945  1.00 70.81           C  
-ANISOU 7939  C   TYR D 689     8401  10563   7940   -170    171  -1304       C  
-ATOM   7940  O   TYR D 689    -131.167  17.954 -38.779  1.00 66.63           O  
-ANISOU 7940  O   TYR D 689     7853  10084   7379   -163    186  -1220       O  
-ATOM   7941  CB  TYR D 689    -128.435  17.646 -37.916  1.00 69.17           C  
-ANISOU 7941  CB  TYR D 689     8291  10193   7797   -153    230  -1104       C  
-ATOM   7942  CG  TYR D 689    -127.517  17.609 -36.721  1.00 67.83           C  
-ANISOU 7942  CG  TYR D 689     8195   9856   7720   -199    253  -1027       C  
-ATOM   7943  CD1 TYR D 689    -128.017  17.603 -35.412  1.00 66.81           C  
-ANISOU 7943  CD1 TYR D 689     8105   9604   7675   -285    257   -999       C  
-ATOM   7944  CD2 TYR D 689    -126.143  17.634 -36.899  1.00 67.17           C  
-ANISOU 7944  CD2 TYR D 689     8135   9753   7632   -151    271   -978       C  
-ATOM   7945  CE1 TYR D 689    -127.162  17.586 -34.324  1.00 63.42           C  
-ANISOU 7945  CE1 TYR D 689     7738   9039   7320   -317    277   -930       C  
-ATOM   7946  CE2 TYR D 689    -125.285  17.624 -35.829  1.00 63.91           C  
-ANISOU 7946  CE2 TYR D 689     7785   9198   7299   -188    290   -911       C  
-ATOM   7947  CZ  TYR D 689    -125.795  17.594 -34.551  1.00 63.85           C  
-ANISOU 7947  CZ  TYR D 689     7815   9073   7370   -269    293   -889       C  
-ATOM   7948  OH  TYR D 689    -124.917  17.590 -33.515  1.00 62.97           O  
-ANISOU 7948  OH  TYR D 689     7760   8839   7327   -295    311   -825       O  
-ATOM   7949  N   GLU D 690    -130.790  16.097 -39.969  1.00 76.77           N  
-ANISOU 7949  N   GLU D 690     9108  11414   8649   -136    135  -1447       N  
-ATOM   7950  CA  GLU D 690    -131.828  16.327 -40.974  1.00 74.66           C  
-ANISOU 7950  CA  GLU D 690     8756  11327   8282    -89    111  -1517       C  
-ATOM   7951  C   GLU D 690    -131.479  17.512 -41.853  1.00 71.88           C  
-ANISOU 7951  C   GLU D 690     8361  11145   7807     23    137  -1409       C  
-ATOM   7952  O   GLU D 690    -132.358  18.147 -42.431  1.00 72.89           O  
-ANISOU 7952  O   GLU D 690     8427  11417   7853     63    132  -1401       O  
-ATOM   7953  CB  GLU D 690    -133.208  16.518 -40.318  1.00 74.04           C  
-ANISOU 7953  CB  GLU D 690     8665  11225   8243   -170    102  -1524       C  
-ATOM   7954  N   ILE D 691    -130.186  17.786 -41.964  1.00 69.55           N  
-ANISOU 7954  N   ILE D 691     8093  10833   7499     75    166  -1321       N  
-ATOM   7955  CA  ILE D 691    -129.686  18.840 -42.815  1.00 71.48           C  
-ANISOU 7955  CA  ILE D 691     8292  11230   7638    181    195  -1203       C  
-ATOM   7956  C   ILE D 691    -129.806  18.397 -44.280  1.00 72.07           C  
-ANISOU 7956  C   ILE D 691     8282  11517   7584    280    168  -1315       C  
-ATOM   7957  O   ILE D 691    -129.584  17.236 -44.609  1.00 68.98           O  
-ANISOU 7957  O   ILE D 691     7887  11121   7199    281    134  -1467       O  
-ATOM   7958  CB  ILE D 691    -128.202  19.153 -42.458  1.00 70.96           C  
-ANISOU 7958  CB  ILE D 691     8276  11077   7608    199    232  -1082       C  
-ATOM   7959  CG1 ILE D 691    -128.017  19.522 -40.968  1.00 71.71           C  
-ANISOU 7959  CG1 ILE D 691     8451  10965   7830    106    253   -989       C  
-ATOM   7960  CG2 ILE D 691    -127.593  20.070 -43.523  1.00 71.59           C  
-ANISOU 7960  CG2 ILE D 691     8293  11331   7575    316    260   -966       C  
-ATOM   7961  CD1 ILE D 691    -128.482  20.888 -40.617  1.00 72.73           C  
-ANISOU 7961  CD1 ILE D 691     8571  11103   7961    109    276   -850       C  
-ATOM   7962  N   ASP D 692    -130.190  19.320 -45.155  1.00 74.20           N  
-ANISOU 7962  N   ASP D 692     8479  11977   7738    367    180  -1243       N  
-ATOM   7963  CA  ASP D 692    -130.286  19.016 -46.582  1.00 73.98           C  
-ANISOU 7963  CA  ASP D 692     8359  12182   7568    477    158  -1336       C  
-ATOM   7964  C   ASP D 692    -128.909  19.123 -47.224  1.00 73.12           C  
-ANISOU 7964  C   ASP D 692     8236  12153   7395    570    185  -1264       C  
-ATOM   7965  O   ASP D 692    -128.458  20.227 -47.548  1.00 66.30           O  
-ANISOU 7965  O   ASP D 692     7344  11372   6475    634    228  -1086       O  
-ATOM   7966  CB  ASP D 692    -131.272  19.942 -47.293  1.00 77.37           C  
-ANISOU 7966  CB  ASP D 692     8707  12801   7887    542    162  -1281       C  
-ATOM   7967  N   LEU D 693    -128.251  17.972 -47.389  1.00 75.77           N  
-ANISOU 7967  N   LEU D 693     8587  12456   7746    575    158  -1401       N  
-ATOM   7968  CA  LEU D 693    -126.891  17.907 -47.933  1.00 81.85           C  
-ANISOU 7968  CA  LEU D 693     9345  13294   8460    660    180  -1353       C  
-ATOM   7969  C   LEU D 693    -126.853  18.275 -49.432  1.00 86.90           C  
-ANISOU 7969  C   LEU D 693     9870  14235   8914    809    183  -1343       C  
-ATOM   7970  O   LEU D 693    -125.797  18.623 -49.962  1.00 85.34           O  
-ANISOU 7970  O   LEU D 693     9642  14137   8647    894    217  -1240       O  
-ATOM   7971  CB  LEU D 693    -126.259  16.515 -47.694  1.00 79.84           C  
-ANISOU 7971  CB  LEU D 693     9137  12923   8276    630    145  -1518       C  
-ATOM   7972  N   GLN D 694    -127.996  18.207 -50.114  1.00 89.13           N  
-ANISOU 7972  N   GLN D 694    10081  14673   9113    845    150  -1444       N  
-ATOM   7973  CA  GLN D 694    -128.066  18.651 -51.502  1.00 92.77           C  
-ANISOU 7973  CA  GLN D 694    10425  15436   9388    992    155  -1420       C  
-ATOM   7974  C   GLN D 694    -127.941  20.169 -51.550  1.00 89.89           C  
-ANISOU 7974  C   GLN D 694    10037  15130   8986   1028    218  -1157       C  
-ATOM   7975  O   GLN D 694    -127.181  20.691 -52.352  1.00 89.62           O  
-ANISOU 7975  O   GLN D 694     9940  15266   8845   1136    253  -1036       O  
-ATOM   7976  CB  GLN D 694    -129.350  18.174 -52.196  1.00 92.63           C  
-ANISOU 7976  CB  GLN D 694    10332  15573   9290   1022     99  -1606       C  
-ATOM   7977  N   LYS D 695    -128.671  20.873 -50.685  1.00 87.62           N  
-ANISOU 7977  N   LYS D 695     9798  14702   8793    939    231  -1067       N  
-ATOM   7978  CA  LYS D 695    -128.645  22.346 -50.680  1.00 86.17           C  
-ANISOU 7978  CA  LYS D 695     9593  14551   8596    969    283   -824       C  
-ATOM   7979  C   LYS D 695    -127.468  22.923 -49.878  1.00 85.83           C  
-ANISOU 7979  C   LYS D 695     9619  14327   8664    924    329   -648       C  
-ATOM   7980  O   LYS D 695    -126.984  24.015 -50.173  1.00 79.52           O  
-ANISOU 7980  O   LYS D 695     8783  13589   7840    979    375   -442       O  
-ATOM   7981  CB  LYS D 695    -129.976  22.906 -50.160  1.00 86.33           C  
-ANISOU 7981  CB  LYS D 695     9625  14516   8662    909    272   -812       C  
-ATOM   7982  N   MET D 696    -126.999  22.191 -48.868  1.00 86.06           N  
-ANISOU 7982  N   MET D 696     9743  14134   8820    824    317   -725       N  
-ATOM   7983  CA  MET D 696    -125.849  22.635 -48.068  1.00 86.67           C  
-ANISOU 7983  CA  MET D 696     9886  14040   9005    779    356   -580       C  
-ATOM   7984  C   MET D 696    -124.848  21.510 -47.817  1.00 81.01           C  
-ANISOU 7984  C   MET D 696     9218  13235   8326    757    343   -689       C  
-ATOM   7985  O   MET D 696    -124.835  20.926 -46.741  1.00 73.33           O  
-ANISOU 7985  O   MET D 696     8333  12051   7477    654    327   -761       O  
-ATOM   7986  CB  MET D 696    -126.300  23.225 -46.725  1.00 87.45           C  
-ANISOU 7986  CB  MET D 696    10064  13911   9251    665    362   -512       C  
-ATOM   7987  CG  MET D 696    -125.162  23.905 -45.967  1.00 90.37           C  
-ANISOU 7987  CG  MET D 696    10485  14127   9726    631    400   -348       C  
-ATOM   7988  SD  MET D 696    -125.756  24.805 -44.509  1.00 95.08           S  
-ANISOU 7988  SD  MET D 696    11153  14497  10476    523    404   -263       S  
-ATOM   7989  CE  MET D 696    -125.823  26.481 -45.145  1.00 97.59           C  
-ANISOU 7989  CE  MET D 696    11394  14924  10761    603    440    -35       C  
-ATOM   7990  N   PRO D 697    -123.989  21.216 -48.803  1.00 80.73           N  
-ANISOU 7990  N   PRO D 697     9124  13367   8184    860    352   -694       N  
-ATOM   7991  CA  PRO D 697    -122.968  20.179 -48.591  1.00 78.41           C  
-ANISOU 7991  CA  PRO D 697     8875  12994   7925    850    340   -793       C  
-ATOM   7992  C   PRO D 697    -121.897  20.580 -47.584  1.00 72.58           C  
-ANISOU 7992  C   PRO D 697     8210  12059   7309    785    377   -655       C  
-ATOM   7993  O   PRO D 697    -121.799  21.762 -47.242  1.00 71.42           O  
-ANISOU 7993  O   PRO D 697     8064  11869   7205    767    414   -467       O  
-ATOM   7994  CB  PRO D 697    -122.330  20.030 -49.969  1.00 79.09           C  
-ANISOU 7994  CB  PRO D 697     8861  13344   7847    994    347   -799       C  
-ATOM   7995  CG  PRO D 697    -122.584  21.333 -50.652  1.00 79.09           C  
-ANISOU 7995  CG  PRO D 697     8778  13515   7757   1066    387   -606       C  
-ATOM   7996  CD  PRO D 697    -123.916  21.797 -50.155  1.00 79.46           C  
-ANISOU 7996  CD  PRO D 697     8847  13486   7858    996    372   -609       C  
-ATOM   7997  N   LEU D 698    -121.122  19.588 -47.126  1.00 71.45           N  
-ANISOU 7997  N   LEU D 698     8125  11797   7224    754    362   -754       N  
-ATOM   7998  CA  LEU D 698    -119.972  19.789 -46.224  1.00 70.62           C  
-ANISOU 7998  CA  LEU D 698     8087  11523   7224    703    392   -647       C  
-ATOM   7999  C   LEU D 698    -119.107  20.974 -46.659  1.00 73.04           C  
-ANISOU 7999  C   LEU D 698     8337  11926   7489    765    445   -427       C  
-ATOM   8000  O   LEU D 698    -118.783  21.838 -45.844  1.00 71.34           O  
-ANISOU 8000  O   LEU D 698     8159  11573   7376    705    474   -280       O  
-ATOM   8001  CB  LEU D 698    -119.115  18.513 -46.103  1.00 69.23           C  
-ANISOU 8001  CB  LEU D 698     7950  11285   7068    707    370   -784       C  
-ATOM   8002  N   GLY D 699    -118.802  21.057 -47.953  1.00 74.58           N  
-ANISOU 8002  N   GLY D 699     8434  12366   7537    885    457   -403       N  
-ATOM   8003  CA  GLY D 699    -117.973  22.138 -48.471  1.00 75.51           C  
-ANISOU 8003  CA  GLY D 699     8483  12596   7610    950    510   -183       C  
-ATOM   8004  C   GLY D 699    -118.579  23.536 -48.407  1.00 80.30           C  
-ANISOU 8004  C   GLY D 699     9060  13203   8248    935    538      2       C  
-ATOM   8005  O   GLY D 699    -117.853  24.524 -48.502  1.00 81.34           O  
-ANISOU 8005  O   GLY D 699     9153  13349   8402    955    582    206       O  
-ATOM   8006  N   LYS D 700    -119.898  23.636 -48.245  1.00 85.64           N  
-ANISOU 8006  N   LYS D 700     9748  13858   8931    901    512    -64       N  
-ATOM   8007  CA  LYS D 700    -120.594  24.925 -48.297  1.00 89.80           C  
-ANISOU 8007  CA  LYS D 700    10239  14405   9475    902    533     95       C  
-ATOM   8008  C   LYS D 700    -120.849  25.547 -46.923  1.00 92.76           C  
-ANISOU 8008  C   LYS D 700    10701  14522  10023    785    532    154       C  
-ATOM   8009  O   LYS D 700    -121.201  26.725 -46.847  1.00 92.42           O  
-ANISOU 8009  O   LYS D 700    10632  14462  10022    784    551    306       O  
-ATOM   8010  CB  LYS D 700    -121.919  24.786 -49.059  1.00 94.09           C  
-ANISOU 8010  CB  LYS D 700    10728  15117   9905    953    505      0       C  
-ATOM   8011  N   LEU D 701    -120.701  24.773 -45.847  1.00 92.42           N  
-ANISOU 8011  N   LEU D 701    10753  14282  10080    692    508     33       N  
-ATOM   8012  CA  LEU D 701    -120.820  25.321 -44.484  1.00 88.04           C  
-ANISOU 8012  CA  LEU D 701    10277  13492   9683    588    508     83       C  
-ATOM   8013  C   LEU D 701    -119.898  26.540 -44.279  1.00 86.65           C  
-ANISOU 8013  C   LEU D 701    10081  13259   9585    591    546    297       C  
-ATOM   8014  O   LEU D 701    -118.709  26.473 -44.583  1.00 84.36           O  
-ANISOU 8014  O   LEU D 701     9768  13003   9282    625    571    363       O  
-ATOM   8015  CB  LEU D 701    -120.531  24.221 -43.459  1.00 85.51           C  
-ANISOU 8015  CB  LEU D 701    10050  12997   9442    505    484    -61       C  
-ATOM   8016  N   SER D 702    -120.453  27.658 -43.797  1.00 83.73           N  
-ANISOU 8016  N   SER D 702     9712  12805   9298    560    549    403       N  
-ATOM   8017  CA  SER D 702    -119.675  28.895 -43.642  1.00 83.71           C  
-ANISOU 8017  CA  SER D 702     9680  12739   9387    562    580    606       C  
-ATOM   8018  C   SER D 702    -119.811  29.500 -42.242  1.00 84.74           C  
-ANISOU 8018  C   SER D 702     9879  12634   9683    470    564    623       C  
-ATOM   8019  O   SER D 702    -120.891  29.479 -41.651  1.00 89.05           O  
-ANISOU 8019  O   SER D 702    10465  13115  10254    428    536    538       O  
-ATOM   8020  CB  SER D 702    -120.103  29.922 -44.698  1.00 83.47           C  
-ANISOU 8020  CB  SER D 702     9552  12870   9294    645    602    761       C  
-ATOM   8021  OG  SER D 702    -120.927  30.941 -44.162  1.00 80.27           O  
-ANISOU 8021  OG  SER D 702     9155  12362   8981    613    591    827       O  
-ATOM   8022  N   LYS D 703    -118.717  30.074 -41.743  1.00 81.40           N  
-ANISOU 8022  N   LYS D 703     9462  12097   9369    444    580    734       N  
-ATOM   8023  CA  LYS D 703    -118.699  30.726 -40.431  1.00 75.04           C  
-ANISOU 8023  CA  LYS D 703     8710  11077   8723    367    563    752       C  
-ATOM   8024  C   LYS D 703    -119.743  31.840 -40.337  1.00 75.28           C  
-ANISOU 8024  C   LYS D 703     8718  11082   8805    371    550    819       C  
-ATOM   8025  O   LYS D 703    -120.390  32.003 -39.300  1.00 81.57           O  
-ANISOU 8025  O   LYS D 703     9567  11745   9679    315    521    748       O  
-ATOM   8026  CB  LYS D 703    -117.302  31.263 -40.078  1.00 72.73           C  
-ANISOU 8026  CB  LYS D 703     8408  10688   8539    349    581    871       C  
-ATOM   8027  N   ARG D 704    -119.931  32.594 -41.420  1.00 72.50           N  
-ANISOU 8027  N   ARG D 704     8281  10863   8403    444    572    956       N  
-ATOM   8028  CA  ARG D 704    -120.841  33.745 -41.389  1.00 66.68           C  
-ANISOU 8028  CA  ARG D 704     7514  10098   7724    458    561   1040       C  
-ATOM   8029  C   ARG D 704    -122.316  33.323 -41.397  1.00 63.68           C  
-ANISOU 8029  C   ARG D 704     7155   9781   7259    461    535    906       C  
-ATOM   8030  O   ARG D 704    -123.163  33.975 -40.753  1.00 62.46           O  
-ANISOU 8030  O   ARG D 704     7020   9535   7178    437    510    898       O  
-ATOM   8031  CB  ARG D 704    -120.547  34.689 -42.557  1.00 65.40           C  
-ANISOU 8031  CB  ARG D 704     7249  10060   7539    538    596   1248       C  
-ATOM   8032  N   GLN D 705    -122.633  32.250 -42.122  1.00 61.66           N  
-ANISOU 8032  N   GLN D 705     6891   9684   6852    493    537    798       N  
-ATOM   8033  CA  GLN D 705    -124.009  31.723 -42.120  1.00 62.90           C  
-ANISOU 8033  CA  GLN D 705     7064   9902   6931    487    510    655       C  
-ATOM   8034  C   GLN D 705    -124.351  31.188 -40.726  1.00 60.84           C  
-ANISOU 8034  C   GLN D 705     6896   9466   6754    391    479    513       C  
-ATOM   8035  O   GLN D 705    -125.442  31.454 -40.181  1.00 56.75           O  
-ANISOU 8035  O   GLN D 705     6397   8905   6261    365    455    461       O  
-ATOM   8036  CB  GLN D 705    -124.185  30.618 -43.185  1.00 60.02           C  
-ANISOU 8036  CB  GLN D 705     6668   9739   6400    540    513    552       C  
-ATOM   8037  N   ILE D 706    -123.409  30.461 -40.139  1.00 60.94           N  
-ANISOU 8037  N   ILE D 706     6962   9386   6808    343    481    458       N  
-ATOM   8038  CA  ILE D 706    -123.634  29.870 -38.824  1.00 64.42           C  
-ANISOU 8038  CA  ILE D 706     7484   9672   7319    258    456    334       C  
-ATOM   8039  C   ILE D 706    -123.823  30.965 -37.762  1.00 60.94           C  
-ANISOU 8039  C   ILE D 706     7065   9078   7011    221    441    394       C  
-ATOM   8040  O   ILE D 706    -124.741  30.887 -36.948  1.00 59.11           O  
-ANISOU 8040  O   ILE D 706     6868   8787   6804    179    417    309       O  
-ATOM   8041  CB  ILE D 706    -122.517  28.870 -38.455  1.00 64.38           C  
-ANISOU 8041  CB  ILE D 706     7528   9605   7328    223    462    273       C  
-ATOM   8042  CG1 ILE D 706    -122.644  27.616 -39.344  1.00 67.91           C  
-ANISOU 8042  CG1 ILE D 706     7963  10191   7649    253    462    161       C  
-ATOM   8043  CG2 ILE D 706    -122.597  28.479 -36.987  1.00 63.07           C  
-ANISOU 8043  CG2 ILE D 706     7441   9270   7254    139    442    186       C  
-ATOM   8044  CD1 ILE D 706    -121.407  26.739 -39.389  1.00 68.50           C  
-ANISOU 8044  CD1 ILE D 706     8062  10248   7716    252    473    128       C  
-ATOM   8045  N   GLN D 707    -122.991  31.997 -37.814  1.00 58.77           N  
-ANISOU 8045  N   GLN D 707     6760   8749   6821    242    455    539       N  
-ATOM   8046  CA  GLN D 707    -123.126  33.129 -36.921  1.00 60.31           C  
-ANISOU 8046  CA  GLN D 707     6963   8801   7152    220    436    596       C  
-ATOM   8047  C   GLN D 707    -124.516  33.763 -37.038  1.00 63.18           C  
-ANISOU 8047  C   GLN D 707     7301   9207   7496    245    417    593       C  
-ATOM   8048  O   GLN D 707    -125.141  34.103 -36.021  1.00 62.94           O  
-ANISOU 8048  O   GLN D 707     7303   9076   7536    211    388    536       O  
-ATOM   8049  CB  GLN D 707    -122.028  34.128 -37.217  1.00 60.99           C  
-ANISOU 8049  CB  GLN D 707     7002   8840   7331    245    454    763       C  
-ATOM   8050  CG  GLN D 707    -122.078  35.424 -36.433  1.00 66.42           C  
-ANISOU 8050  CG  GLN D 707     7683   9375   8177    231    430    833       C  
-ATOM   8051  CD  GLN D 707    -120.920  36.334 -36.855  1.00 70.78           C  
-ANISOU 8051  CD  GLN D 707     8179   9885   8829    252    450   1007       C  
-ATOM   8052  OE1 GLN D 707    -119.916  35.860 -37.385  1.00 73.26           O  
-ANISOU 8052  OE1 GLN D 707     8478  10255   9104    259    480   1053       O  
-ATOM   8053  NE2 GLN D 707    -121.049  37.626 -36.620  1.00 71.59           N  
-ANISOU 8053  NE2 GLN D 707     8248   9887   9067    261    431   1104       N  
-ATOM   8054  N   ALA D 708    -125.014  33.906 -38.266  1.00 63.93           N  
-ANISOU 8054  N   ALA D 708     7335   9464   7491    311    433    649       N  
-ATOM   8055  CA  ALA D 708    -126.349  34.492 -38.476  1.00 63.55           C  
-ANISOU 8055  CA  ALA D 708     7258   9475   7414    344    416    649       C  
-ATOM   8056  C   ALA D 708    -127.464  33.571 -37.952  1.00 59.47           C  
-ANISOU 8056  C   ALA D 708     6784   8982   6830    302    392    473       C  
-ATOM   8057  O   ALA D 708    -128.497  34.033 -37.425  1.00 63.20           O  
-ANISOU 8057  O   ALA D 708     7260   9426   7328    295    368    438       O  
-ATOM   8058  CB  ALA D 708    -126.559  34.800 -39.949  1.00 66.52           C  
-ANISOU 8058  CB  ALA D 708     7552  10036   7685    432    441    753       C  
-ATOM   8059  N   ALA D 709    -127.242  32.268 -38.080  1.00 55.54           N  
-ANISOU 8059  N   ALA D 709     6314   8533   6255    273    398    363       N  
-ATOM   8060  CA  ALA D 709    -128.155  31.269 -37.533  1.00 54.88           C  
-ANISOU 8060  CA  ALA D 709     6271   8454   6127    219    377    201       C  
-ATOM   8061  C   ALA D 709    -128.220  31.336 -35.987  1.00 55.05           C  
-ANISOU 8061  C   ALA D 709     6354   8306   6255    148    356    148       C  
-ATOM   8062  O   ALA D 709    -129.312  31.236 -35.407  1.00 51.07           O  
-ANISOU 8062  O   ALA D 709     5861   7799   5744    120    335     69       O  
-ATOM   8063  CB  ALA D 709    -127.745  29.877 -37.997  1.00 54.55           C  
-ANISOU 8063  CB  ALA D 709     6244   8478   6004    205    385    103       C  
-ATOM   8064  N   TYR D 710    -127.067  31.531 -35.337  1.00 50.37           N  
-ANISOU 8064  N   TYR D 710     5794   7587   5757    123    362    193       N  
-ATOM   8065  CA  TYR D 710    -127.032  31.756 -33.889  1.00 50.91           C  
-ANISOU 8065  CA  TYR D 710     5910   7506   5927     71    341    155       C  
-ATOM   8066  C   TYR D 710    -127.935  32.933 -33.494  1.00 52.85           C  
-ANISOU 8066  C   TYR D 710     6131   7725   6224     94    317    186       C  
-ATOM   8067  O   TYR D 710    -128.754  32.823 -32.581  1.00 57.24           O  
-ANISOU 8067  O   TYR D 710     6710   8250   6790     62    295    102       O  
-ATOM   8068  CB  TYR D 710    -125.601  32.031 -33.375  1.00 47.65           C  
-ANISOU 8068  CB  TYR D 710     5519   6972   5613     56    349    216       C  
-ATOM   8069  CG  TYR D 710    -124.739  30.810 -33.107  1.00 46.16           C  
-ANISOU 8069  CG  TYR D 710     5377   6756   5404     14    362    152       C  
-ATOM   8070  CD1 TYR D 710    -125.147  29.819 -32.237  1.00 47.12           C  
-ANISOU 8070  CD1 TYR D 710     5549   6844   5511    -42    351     35       C  
-ATOM   8071  CD2 TYR D 710    -123.515  30.673 -33.698  1.00 48.94           C  
-ANISOU 8071  CD2 TYR D 710     5720   7117   5758     34    385    217       C  
-ATOM   8072  CE1 TYR D 710    -124.353  28.718 -31.980  1.00 48.54           C  
-ANISOU 8072  CE1 TYR D 710     5771   6990   5682    -76    362    -16       C  
-ATOM   8073  CE2 TYR D 710    -122.713  29.568 -33.455  1.00 49.92           C  
-ANISOU 8073  CE2 TYR D 710     5886   7215   5865      2    396    158       C  
-ATOM   8074  CZ  TYR D 710    -123.133  28.593 -32.596  1.00 49.44           C  
-ANISOU 8074  CZ  TYR D 710     5877   7111   5795    -52    383     41       C  
-ATOM   8075  OH  TYR D 710    -122.327  27.483 -32.387  1.00 50.85           O  
-ANISOU 8075  OH  TYR D 710     6097   7259   5964    -78    393    -11       O  
-ATOM   8076  N   SER D 711    -127.788  34.051 -34.183  1.00 53.31           N  
-ANISOU 8076  N   SER D 711     6140   7799   6318    152    322    309       N  
-ATOM   8077  CA  SER D 711    -128.602  35.223 -33.878  1.00 56.25           C  
-ANISOU 8077  CA  SER D 711     6485   8138   6749    184    296    343       C  
-ATOM   8078  C   SER D 711    -130.116  34.958 -34.000  1.00 57.78           C  
-ANISOU 8078  C   SER D 711     6666   8439   6848    192    283    260       C  
-ATOM   8079  O   SER D 711    -130.916  35.374 -33.152  1.00 57.21           O  
-ANISOU 8079  O   SER D 711     6602   8324   6813    185    254    209       O  
-ATOM   8080  CB  SER D 711    -128.217  36.374 -34.796  1.00 58.00           C  
-ANISOU 8080  CB  SER D 711     6647   8371   7019    249    307    504       C  
-ATOM   8081  OG  SER D 711    -126.857  36.737 -34.588  1.00 58.69           O  
-ANISOU 8081  OG  SER D 711     6739   8348   7213    236    315    585       O  
-ATOM   8082  N   ILE D 712    -130.513  34.281 -35.066  1.00 58.14           N  
-ANISOU 8082  N   ILE D 712     6685   8634   6771    212    301    244       N  
-ATOM   8083  CA  ILE D 712    -131.935  33.968 -35.257  1.00 61.58           C  
-ANISOU 8083  CA  ILE D 712     7101   9183   7114    218    288    161       C  
-ATOM   8084  C   ILE D 712    -132.442  33.084 -34.123  1.00 59.19           C  
-ANISOU 8084  C   ILE D 712     6847   8833   6810    142    272     23       C  
-ATOM   8085  O   ILE D 712    -133.548  33.296 -33.623  1.00 59.34           O  
-ANISOU 8085  O   ILE D 712     6856   8871   6817    138    251    -30       O  
-ATOM   8086  CB  ILE D 712    -132.185  33.283 -36.615  1.00 64.25           C  
-ANISOU 8086  CB  ILE D 712     7399   9696   7319    253    307    150       C  
-ATOM   8087  CG1 ILE D 712    -131.979  34.298 -37.732  1.00 67.29           C  
-ANISOU 8087  CG1 ILE D 712     7720  10158   7690    342    322    299       C  
-ATOM   8088  CG2 ILE D 712    -133.592  32.670 -36.686  1.00 65.75           C  
-ANISOU 8088  CG2 ILE D 712     7573   9995   7415    239    290     31       C  
-ATOM   8089  CD1 ILE D 712    -131.946  33.677 -39.105  1.00 72.11           C  
-ANISOU 8089  CD1 ILE D 712     8283  10950   8166    389    344    302       C  
-ATOM   8090  N   LEU D 713    -131.643  32.106 -33.717  1.00 55.36           N  
-ANISOU 8090  N   LEU D 713     6409   8291   6335     86    283    -27       N  
-ATOM   8091  CA  LEU D 713    -132.015  31.283 -32.588  1.00 56.66           C  
-ANISOU 8091  CA  LEU D 713     6616   8402   6510     14    272   -135       C  
-ATOM   8092  C   LEU D 713    -132.177  32.096 -31.321  1.00 59.98           C  
-ANISOU 8092  C   LEU D 713     7052   8719   7018      7    249   -132       C  
-ATOM   8093  O   LEU D 713    -133.053  31.786 -30.502  1.00 57.50           O  
-ANISOU 8093  O   LEU D 713     6745   8413   6690    -28    235   -210       O  
-ATOM   8094  CB  LEU D 713    -131.004  30.167 -32.360  1.00 56.07           C  
-ANISOU 8094  CB  LEU D 713     6589   8271   6444    -37    287   -172       C  
-ATOM   8095  CG  LEU D 713    -131.032  29.055 -33.401  1.00 56.33           C  
-ANISOU 8095  CG  LEU D 713     6610   8405   6386    -40    300   -225       C  
-ATOM   8096  CD1 LEU D 713    -130.000  27.983 -33.066  1.00 56.49           C  
-ANISOU 8096  CD1 LEU D 713     6681   8353   6431    -87    312   -263       C  
-ATOM   8097  CD2 LEU D 713    -132.422  28.435 -33.488  1.00 55.88           C  
-ANISOU 8097  CD2 LEU D 713     6531   8439   6262    -67    286   -323       C  
-ATOM   8098  N   SER D 714    -131.356  33.137 -31.165  1.00 59.43           N  
-ANISOU 8098  N   SER D 714     6980   8559   7040     41    245    -45       N  
-ATOM   8099  CA  SER D 714    -131.496  34.041 -30.023  1.00 61.12           C  
-ANISOU 8099  CA  SER D 714     7200   8678   7346     47    215    -51       C  
-ATOM   8100  C   SER D 714    -132.818  34.780 -30.077  1.00 61.88           C  
-ANISOU 8100  C   SER D 714     7255   8837   7418     89    193    -62       C  
-ATOM   8101  O   SER D 714    -133.504  34.915 -29.047  1.00 63.73           O  
-ANISOU 8101  O   SER D 714     7495   9054   7666     78    169   -131       O  
-ATOM   8102  CB  SER D 714    -130.324  35.039 -29.927  1.00 63.55           C  
-ANISOU 8102  CB  SER D 714     7505   8867   7773     75    209     42       C  
-ATOM   8103  OG  SER D 714    -129.145  34.427 -29.422  1.00 62.04           O  
-ANISOU 8103  OG  SER D 714     7356   8598   7619     32    221     31       O  
-ATOM   8104  N   GLU D 715    -133.176  35.262 -31.263  1.00 62.15           N  
-ANISOU 8104  N   GLU D 715     7246   8955   7413    144    200      7       N  
-ATOM   8105  CA  GLU D 715    -134.457  35.955 -31.428  1.00 61.76           C  
-ANISOU 8105  CA  GLU D 715     7154   8978   7333    191    180      1       C  
-ATOM   8106  C   GLU D 715    -135.622  35.006 -31.148  1.00 59.93           C  
-ANISOU 8106  C   GLU D 715     6922   8848   7000    150    178   -114       C  
-ATOM   8107  O   GLU D 715    -136.617  35.388 -30.524  1.00 58.04           O  
-ANISOU 8107  O   GLU D 715     6666   8630   6756    162    154   -163       O  
-ATOM   8108  CB  GLU D 715    -134.569  36.567 -32.819  1.00 65.45           C  
-ANISOU 8108  CB  GLU D 715     7571   9530   7767    261    193    106       C  
-ATOM   8109  CG  GLU D 715    -133.561  37.680 -33.080  1.00 69.63           C  
-ANISOU 8109  CG  GLU D 715     8086   9958   8414    305    193    240       C  
-ATOM   8110  CD  GLU D 715    -133.675  38.317 -34.466  1.00 78.65           C  
-ANISOU 8110  CD  GLU D 715     9168  11193   9521    380    210    367       C  
-ATOM   8111  OE1 GLU D 715    -134.636  38.009 -35.205  1.00 81.99           O  
-ANISOU 8111  OE1 GLU D 715     9558  11767   9826    408    217    343       O  
-ATOM   8112  OE2 GLU D 715    -132.788  39.129 -34.829  1.00 79.98           O  
-ANISOU 8112  OE2 GLU D 715     9317  11289   9783    412    218    496       O  
-ATOM   8113  N   VAL D 716    -135.496  33.759 -31.581  1.00 58.23           N  
-ANISOU 8113  N   VAL D 716     6722   8693   6710    102    201   -161       N  
-ATOM   8114  CA  VAL D 716    -136.532  32.752 -31.300  1.00 58.30           C  
-ANISOU 8114  CA  VAL D 716     6728   8784   6641     50    198   -269       C  
-ATOM   8115  C   VAL D 716    -136.750  32.563 -29.801  1.00 56.92           C  
-ANISOU 8115  C   VAL D 716     6581   8537   6509      1    185   -332       C  
-ATOM   8116  O   VAL D 716    -137.893  32.591 -29.323  1.00 51.38           O  
-ANISOU 8116  O   VAL D 716     5854   7896   5773     -5    170   -386       O  
-ATOM   8117  CB  VAL D 716    -136.190  31.386 -31.916  1.00 60.22           C  
-ANISOU 8117  CB  VAL D 716     6985   9072   6825      1    220   -316       C  
-ATOM   8118  CG1 VAL D 716    -137.109  30.294 -31.380  1.00 59.03           C  
-ANISOU 8118  CG1 VAL D 716     6835   8964   6629    -71    215   -425       C  
-ATOM   8119  CG2 VAL D 716    -136.274  31.451 -33.431  1.00 63.08           C  
-ANISOU 8119  CG2 VAL D 716     7303   9553   7110     56    230   -279       C  
-ATOM   8120  N   GLN D 717    -135.652  32.396 -29.069  1.00 53.39           N  
-ANISOU 8120  N   GLN D 717     6179   7973   6132    -28    190   -321       N  
-ATOM   8121  CA  GLN D 717    -135.713  32.189 -27.638  1.00 57.10           C  
-ANISOU 8121  CA  GLN D 717     6673   8385   6638    -67    179   -373       C  
-ATOM   8122  C   GLN D 717    -136.388  33.375 -26.959  1.00 53.76           C  
-ANISOU 8122  C   GLN D 717     6221   7957   6247    -15    147   -377       C  
-ATOM   8123  O   GLN D 717    -137.227  33.191 -26.083  1.00 52.56           O  
-ANISOU 8123  O   GLN D 717     6057   7846   6069    -32    135   -439       O  
-ATOM   8124  CB  GLN D 717    -134.311  31.979 -27.055  1.00 59.97           C  
-ANISOU 8124  CB  GLN D 717     7085   8628   7074    -91    187   -351       C  
-ATOM   8125  CG  GLN D 717    -134.325  31.501 -25.612  1.00 62.49           C  
-ANISOU 8125  CG  GLN D 717     7427   8907   7410   -135    182   -407       C  
-ATOM   8126  CD  GLN D 717    -135.165  30.235 -25.420  1.00 69.87           C  
-ANISOU 8126  CD  GLN D 717     8359   9916   8273   -201    197   -468       C  
-ATOM   8127  OE1 GLN D 717    -134.791  29.140 -25.872  1.00 77.87           O  
-ANISOU 8127  OE1 GLN D 717     9395  10927   9266   -249    219   -478       O  
-ATOM   8128  NE2 GLN D 717    -136.295  30.375 -24.728  1.00 67.82           N  
-ANISOU 8128  NE2 GLN D 717     8068   9721   7981   -202    183   -510       N  
-ATOM   8129  N   GLN D 718    -136.021  34.583 -27.374  1.00 55.17           N  
-ANISOU 8129  N   GLN D 718     6385   8088   6489     52    131   -309       N  
-ATOM   8130  CA  GLN D 718    -136.633  35.787 -26.850  1.00 61.29           C  
-ANISOU 8130  CA  GLN D 718     7129   8848   7309    113     95   -315       C  
-ATOM   8131  C   GLN D 718    -138.139  35.844 -27.149  1.00 64.27           C  
-ANISOU 8131  C   GLN D 718     7462   9358   7599    136     87   -352       C  
-ATOM   8132  O   GLN D 718    -138.936  36.173 -26.271  1.00 66.42           O  
-ANISOU 8132  O   GLN D 718     7715   9656   7866    152     62   -410       O  
-ATOM   8133  CB  GLN D 718    -135.918  37.006 -27.440  1.00 66.88           C  
-ANISOU 8133  CB  GLN D 718     7826   9472   8114    176     82   -219       C  
-ATOM   8134  CG  GLN D 718    -136.430  38.340 -26.923  1.00 75.75           C  
-ANISOU 8134  CG  GLN D 718     8917  10553   9311    246     37   -224       C  
-ATOM   8135  CD  GLN D 718    -135.881  39.532 -27.694  1.00 81.09           C  
-ANISOU 8135  CD  GLN D 718     9571  11151  10089    308     26   -113       C  
-ATOM   8136  OE1 GLN D 718    -135.501  39.428 -28.864  1.00 84.82           O  
-ANISOU 8136  OE1 GLN D 718    10035  11653  10539    314     56    -23       O  
-ATOM   8137  NE2 GLN D 718    -135.817  40.673 -27.018  1.00 82.23           N  
-ANISOU 8137  NE2 GLN D 718     9701  11194  10350    357    -19   -120       N  
-ATOM   8138  N   ALA D 719    -138.526  35.530 -28.386  1.00 63.51           N  
-ANISOU 8138  N   ALA D 719     7344   9356   7431    142    106   -323       N  
-ATOM   8139  CA  ALA D 719    -139.940  35.517 -28.766  1.00 60.93           C  
-ANISOU 8139  CA  ALA D 719     6969   9166   7015    162    100   -361       C  
-ATOM   8140  C   ALA D 719    -140.724  34.475 -27.981  1.00 59.30           C  
-ANISOU 8140  C   ALA D 719     6761   9025   6744     92    104   -456       C  
-ATOM   8141  O   ALA D 719    -141.820  34.733 -27.537  1.00 65.78           O  
-ANISOU 8141  O   ALA D 719     7546   9919   7529    109     86   -501       O  
-ATOM   8142  CB  ALA D 719    -140.085  35.283 -30.253  1.00 61.00           C  
-ANISOU 8142  CB  ALA D 719     6952   9271   6954    182    119   -318       C  
-ATOM   8143  N   VAL D 720    -140.156  33.301 -27.771  1.00 62.29           N  
-ANISOU 8143  N   VAL D 720     7176   9375   7116     14    127   -483       N  
-ATOM   8144  CA  VAL D 720    -140.798  32.289 -26.910  1.00 64.98           C  
-ANISOU 8144  CA  VAL D 720     7514   9760   7417    -59    133   -557       C  
-ATOM   8145  C   VAL D 720    -141.052  32.834 -25.471  1.00 69.41           C  
-ANISOU 8145  C   VAL D 720     8070  10292   8009    -43    112   -584       C  
-ATOM   8146  O   VAL D 720    -142.158  32.685 -24.941  1.00 70.97           O  
-ANISOU 8146  O   VAL D 720     8229  10582   8156    -53    105   -632       O  
-ATOM   8147  CB  VAL D 720    -140.003  30.957 -26.939  1.00 63.35           C  
-ANISOU 8147  CB  VAL D 720     7349   9504   7215   -141    161   -569       C  
-ATOM   8148  CG1 VAL D 720    -140.483  29.973 -25.880  1.00 64.32           C  
-ANISOU 8148  CG1 VAL D 720     7473   9644   7324   -217    169   -622       C  
-ATOM   8149  CG2 VAL D 720    -140.094  30.319 -28.328  1.00 66.36           C  
-ANISOU 8149  CG2 VAL D 720     7718   9953   7544   -152    174   -574       C  
-ATOM   8150  N   SER D 721    -140.066  33.496 -24.856  1.00 68.32           N  
-ANISOU 8150  N   SER D 721     7964  10040   7954    -12    100   -557       N  
-ATOM   8151  CA  SER D 721    -140.284  34.145 -23.535  1.00 66.22           C  
-ANISOU 8151  CA  SER D 721     7685   9757   7718     22     72   -595       C  
-ATOM   8152  C   SER D 721    -141.374  35.236 -23.555  1.00 61.41           C  
-ANISOU 8152  C   SER D 721     7024   9218   7092    100     39   -614       C  
-ATOM   8153  O   SER D 721    -141.170  36.347 -24.058  1.00 54.91           O  
-ANISOU 8153  O   SER D 721     6193   8345   6325    172     16   -575       O  
-ATOM   8154  CB  SER D 721    -138.978  34.756 -22.982  1.00 70.10           C  
-ANISOU 8154  CB  SER D 721     8213  10110   8311     48     57   -571       C  
-ATOM   8155  OG  SER D 721    -137.959  33.796 -22.697  1.00 63.18           O  
-ANISOU 8155  OG  SER D 721     7384   9171   7451    -17     84   -561       O  
-ATOM   8156  N   LEU D 730    -142.652  31.308 -35.300  1.00 77.77           N  
-ANISOU 8156  N   LEU D 730     8904  12054   8592    130    163   -533       N  
-ATOM   8157  CA  LEU D 730    -143.201  30.848 -36.585  1.00 81.27           C  
-ANISOU 8157  CA  LEU D 730     9287  12663   8928    160    160   -578       C  
-ATOM   8158  C   LEU D 730    -142.414  31.395 -37.819  1.00 78.68           C  
-ANISOU 8158  C   LEU D 730     8940  12391   8563    252    175   -481       C  
-ATOM   8159  O   LEU D 730    -141.702  30.645 -38.522  1.00 77.19           O  
-ANISOU 8159  O   LEU D 730     8755  12229   8343    246    186   -503       O  
-ATOM   8160  CB  LEU D 730    -144.712  31.182 -36.652  1.00 81.87           C  
-ANISOU 8160  CB  LEU D 730     9300  12869   8938    184    140   -622       C  
-ATOM   8161  N   ASP D 731    -142.509  32.695 -38.080  1.00 77.68           N  
-ANISOU 8161  N   ASP D 731     8789  12283   8443    340    176   -369       N  
-ATOM   8162  CA  ASP D 731    -141.677  33.319 -39.115  1.00 83.97           C  
-ANISOU 8162  CA  ASP D 731     9566  13116   9223    426    195   -246       C  
-ATOM   8163  C   ASP D 731    -140.171  33.202 -38.797  1.00 83.29           C  
-ANISOU 8163  C   ASP D 731     9540  12881   9224    395    216   -186       C  
-ATOM   8164  O   ASP D 731    -139.341  33.031 -39.701  1.00 83.79           O  
-ANISOU 8164  O   ASP D 731     9590  12992   9252    432    235   -134       O  
-ATOM   8165  CB  ASP D 731    -142.076  34.779 -39.334  1.00 87.19           C  
-ANISOU 8165  CB  ASP D 731     9936  13546   9646    521    191   -124       C  
-ATOM   8166  CG  ASP D 731    -141.214  35.452 -40.352  1.00 93.75           C  
-ANISOU 8166  CG  ASP D 731    10740  14410  10470    606    215     25       C  
-ATOM   8167  OD1 ASP D 731    -140.232  36.092 -39.950  1.00 98.97           O  
-ANISOU 8167  OD1 ASP D 731    11438  14925  11242    607    225    127       O  
-ATOM   8168  OD2 ASP D 731    -141.490  35.299 -41.563  1.00 98.66           O  
-ANISOU 8168  OD2 ASP D 731    11300  15213  10976    670    223     38       O  
-ATOM   8169  N   LEU D 732    -139.814  33.282 -37.519  1.00 79.43           N  
-ANISOU 8169  N   LEU D 732     9112  12224   8843    333    211   -196       N  
-ATOM   8170  CA  LEU D 732    -138.408  33.152 -37.120  1.00 77.41           C  
-ANISOU 8170  CA  LEU D 732     8914  11826   8673    301    227   -149       C  
-ATOM   8171  C   LEU D 732    -137.922  31.725 -37.342  1.00 71.29           C  
-ANISOU 8171  C   LEU D 732     8162  11068   7857    240    237   -241       C  
-ATOM   8172  O   LEU D 732    -136.811  31.532 -37.840  1.00 73.12           O  
-ANISOU 8172  O   LEU D 732     8407  11281   8095    254    256   -192       O  
-ATOM   8173  CB  LEU D 732    -138.214  33.563 -35.665  1.00 75.84           C  
-ANISOU 8173  CB  LEU D 732     8766  11459   8590    255    215   -152       C  
-ATOM   8174  CG  LEU D 732    -138.404  35.058 -35.391  1.00 77.19           C  
-ANISOU 8174  CG  LEU D 732     8920  11575   8833    320    200    -56       C  
-ATOM   8175  CD1 LEU D 732    -138.511  35.297 -33.897  1.00 75.10           C  
-ANISOU 8175  CD1 LEU D 732     8696  11181   8659    277    179   -105       C  
-ATOM   8176  CD2 LEU D 732    -137.289  35.900 -36.009  1.00 77.06           C  
-ANISOU 8176  CD2 LEU D 732     8896  11505   8879    377    216     90       C  
-ATOM   8177  N   SER D 733    -138.760  30.747 -36.988  1.00 70.15           N  
-ANISOU 8177  N   SER D 733     8018  10958   7676    175    222   -372       N  
-ATOM   8178  CA  SER D 733    -138.492  29.327 -37.277  1.00 72.43           C  
-ANISOU 8178  CA  SER D 733     8320  11268   7931    118    224   -476       C  
-ATOM   8179  C   SER D 733    -138.128  29.145 -38.744  1.00 77.25           C  
-ANISOU 8179  C   SER D 733     8884  12016   8450    188    233   -461       C  
-ATOM   8180  O   SER D 733    -137.105  28.546 -39.072  1.00 77.40           O  
-ANISOU 8180  O   SER D 733     8926  12009   8473    182    245   -465       O  
-ATOM   8181  CB  SER D 733    -139.711  28.447 -36.950  1.00 71.69           C  
-ANISOU 8181  CB  SER D 733     8206  11227   7805     52    203   -608       C  
-ATOM   8182  OG  SER D 733    -139.424  27.473 -35.975  1.00 64.61           O  
-ANISOU 8182  OG  SER D 733     7362  10210   6975    -45    203   -674       O  
-ATOM   8183  N   ASN D 734    -138.956  29.710 -39.616  1.00 79.99           N  
-ANISOU 8183  N   ASN D 734     9162  12518   8711    262    226   -440       N  
-ATOM   8184  CA  ASN D 734    -138.737  29.615 -41.047  1.00 83.17           C  
-ANISOU 8184  CA  ASN D 734     9506  13086   9008    344    233   -424       C  
-ATOM   8185  C   ASN D 734    -137.484  30.354 -41.500  1.00 84.19           C  
-ANISOU 8185  C   ASN D 734     9640  13188   9159    409    263   -271       C  
-ATOM   8186  O   ASN D 734    -136.806  29.898 -42.424  1.00 92.66           O  
-ANISOU 8186  O   ASN D 734    10689  14351  10168    450    275   -270       O  
-ATOM   8187  CB  ASN D 734    -139.967  30.119 -41.815  1.00 85.34           C  
-ANISOU 8187  CB  ASN D 734     9701  13541   9182    414    220   -428       C  
-ATOM   8188  CG  ASN D 734    -141.193  29.249 -41.588  1.00 83.52           C  
-ANISOU 8188  CG  ASN D 734     9449  13369   8915    352    190   -590       C  
-ATOM   8189  OD1 ASN D 734    -141.080  28.054 -41.310  1.00 82.94           O  
-ANISOU 8189  OD1 ASN D 734     9402  13249   8862    272    179   -711       O  
-ATOM   8190  ND2 ASN D 734    -142.371  29.842 -41.710  1.00 81.98           N  
-ANISOU 8190  ND2 ASN D 734     9203  13274   8672    388    176   -590       N  
-ATOM   8191  N   ARG D 735    -137.173  31.491 -40.876  1.00 80.50           N  
-ANISOU 8191  N   ARG D 735     9197  12604   8784    421    273   -145       N  
-ATOM   8192  CA  ARG D 735    -135.933  32.217 -41.225  1.00 80.55           C  
-ANISOU 8192  CA  ARG D 735     9205  12565   8836    471    300     10       C  
-ATOM   8193  C   ARG D 735    -134.713  31.324 -40.930  1.00 71.63           C  
-ANISOU 8193  C   ARG D 735     8130  11340   7747    415    312    -28       C  
-ATOM   8194  O   ARG D 735    -133.752  31.236 -41.714  1.00 69.55           O  
-ANISOU 8194  O   ARG D 735     7847  11130   7450    459    335     36       O  
-ATOM   8195  CB  ARG D 735    -135.844  33.563 -40.475  1.00 80.13           C  
-ANISOU 8195  CB  ARG D 735     9168  12375   8902    483    300    134       C  
-ATOM   8196  N   PHE D 736    -134.786  30.611 -39.815  1.00 65.95           N  
-ANISOU 8196  N   PHE D 736     7474  10492   7091    320    298   -133       N  
-ATOM   8197  CA  PHE D 736    -133.710  29.708 -39.441  1.00 65.73           C  
-ANISOU 8197  CA  PHE D 736     7501  10368   7106    265    307   -176       C  
-ATOM   8198  C   PHE D 736    -133.529  28.587 -40.464  1.00 64.15           C  
-ANISOU 8198  C   PHE D 736     7273  10297   6804    283    307   -266       C  
-ATOM   8199  O   PHE D 736    -132.414  28.322 -40.918  1.00 62.02           O  
-ANISOU 8199  O   PHE D 736     7009  10032   6526    307    325   -231       O  
-ATOM   8200  CB  PHE D 736    -133.959  29.107 -38.056  1.00 65.33           C  
-ANISOU 8200  CB  PHE D 736     7515  10172   7135    164    291   -270       C  
-ATOM   8201  CG  PHE D 736    -132.905  28.133 -37.639  1.00 64.45           C  
-ANISOU 8201  CG  PHE D 736     7460   9961   7067    109    300   -315       C  
-ATOM   8202  CD1 PHE D 736    -131.709  28.583 -37.093  1.00 62.60           C  
-ANISOU 8202  CD1 PHE D 736     7267   9601   6919    104    316   -226       C  
-ATOM   8203  CD2 PHE D 736    -133.091  26.770 -37.831  1.00 64.71           C  
-ANISOU 8203  CD2 PHE D 736     7500  10026   7060     66    289   -447       C  
-ATOM   8204  CE1 PHE D 736    -130.731  27.688 -36.718  1.00 63.06           C  
-ANISOU 8204  CE1 PHE D 736     7374   9573   7012     59    323   -266       C  
-ATOM   8205  CE2 PHE D 736    -132.112  25.872 -37.466  1.00 64.36           C  
-ANISOU 8205  CE2 PHE D 736     7508   9887   7061     22    295   -486       C  
-ATOM   8206  CZ  PHE D 736    -130.933  26.331 -36.909  1.00 62.77           C  
-ANISOU 8206  CZ  PHE D 736     7348   9567   6933     20    314   -393       C  
-ATOM   8207  N   TYR D 737    -134.631  27.934 -40.810  1.00 67.58           N  
-ANISOU 8207  N   TYR D 737     7674  10838   7164    274    284   -389       N  
-ATOM   8208  CA  TYR D 737    -134.601  26.833 -41.765  1.00 72.21           C  
-ANISOU 8208  CA  TYR D 737     8228  11550   7659    292    273   -504       C  
-ATOM   8209  C   TYR D 737    -134.192  27.260 -43.179  1.00 78.02           C  
-ANISOU 8209  C   TYR D 737     8891  12469   8284    409    289   -427       C  
-ATOM   8210  O   TYR D 737    -133.707  26.447 -43.962  1.00 79.26           O  
-ANISOU 8210  O   TYR D 737     9026  12717   8373    440    286   -497       O  
-ATOM   8211  CB  TYR D 737    -135.955  26.120 -41.785  1.00 70.76           C  
-ANISOU 8211  CB  TYR D 737     8015  11437   7432    253    239   -654       C  
-ATOM   8212  CG  TYR D 737    -136.216  25.330 -40.518  1.00 66.78           C  
-ANISOU 8212  CG  TYR D 737     7574  10770   7028    134    225   -745       C  
-ATOM   8213  CD1 TYR D 737    -135.334  24.341 -40.111  1.00 63.66           C  
-ANISOU 8213  CD1 TYR D 737     7234  10261   6693     77    226   -800       C  
-ATOM   8214  CD2 TYR D 737    -137.340  25.561 -39.737  1.00 66.08           C  
-ANISOU 8214  CD2 TYR D 737     7485  10652   6970     83    212   -769       C  
-ATOM   8215  CE1 TYR D 737    -135.556  23.617 -38.958  1.00 62.53           C  
-ANISOU 8215  CE1 TYR D 737     7144   9975   6642    -27    217   -866       C  
-ATOM   8216  CE2 TYR D 737    -137.576  24.827 -38.582  1.00 64.80           C  
-ANISOU 8216  CE2 TYR D 737     7372  10357   6893    -22    203   -838       C  
-ATOM   8217  CZ  TYR D 737    -136.676  23.855 -38.194  1.00 64.65           C  
-ANISOU 8217  CZ  TYR D 737     7407  10222   6936    -77    206   -881       C  
-ATOM   8218  OH  TYR D 737    -136.871  23.111 -37.052  1.00 62.12           O  
-ANISOU 8218  OH  TYR D 737     7130   9772   6701   -178    201   -933       O  
-ATOM   8219  N   THR D 738    -134.366  28.539 -43.492  1.00 80.01           N  
-ANISOU 8219  N   THR D 738     9104  12775   8521    477    306   -280       N  
-ATOM   8220  CA  THR D 738    -133.876  29.090 -44.742  1.00 82.10           C  
-ANISOU 8220  CA  THR D 738     9298  13204   8693    590    329   -166       C  
-ATOM   8221  C   THR D 738    -132.357  29.224 -44.716  1.00 76.93           C  
-ANISOU 8221  C   THR D 738     8670  12469   8090    598    360    -60       C  
-ATOM   8222  O   THR D 738    -131.695  28.937 -45.706  1.00 79.14           O  
-ANISOU 8222  O   THR D 738     8904  12884   8282    667    375    -40       O  
-ATOM   8223  CB  THR D 738    -134.528  30.458 -45.023  1.00 86.79           C  
-ANISOU 8223  CB  THR D 738     9840  13862   9273    658    339    -23       C  
-ATOM   8224  OG1 THR D 738    -135.934  30.277 -45.221  1.00 82.87           O  
-ANISOU 8224  OG1 THR D 738     9305  13476   8704    665    311   -127       O  
-ATOM   8225  CG2 THR D 738    -133.918  31.119 -46.260  1.00 89.00           C  
-ANISOU 8225  CG2 THR D 738    10042  14303   9469    776    370    132       C  
-ATOM   8226  N   LEU D 739    -131.804  29.668 -43.590  1.00 76.14           N  
-ANISOU 8226  N   LEU D 739     8638  12161   8129    533    368      6       N  
-ATOM   8227  CA  LEU D 739    -130.345  29.792 -43.453  1.00 72.94           C  
-ANISOU 8227  CA  LEU D 739     8260  11666   7786    530    395    102       C  
-ATOM   8228  C   LEU D 739    -129.672  28.431 -43.372  1.00 67.84           C  
-ANISOU 8228  C   LEU D 739     7655  10995   7126    489    389    -30       C  
-ATOM   8229  O   LEU D 739    -128.579  28.229 -43.878  1.00 67.00           O  
-ANISOU 8229  O   LEU D 739     7536  10926   6995    525    409     16       O  
-ATOM   8230  CB  LEU D 739    -129.996  30.565 -42.188  1.00 74.62           C  
-ANISOU 8230  CB  LEU D 739     8535  11662   8156    468    398    181       C  
-ATOM   8231  CG  LEU D 739    -128.930  31.637 -42.288  1.00 75.46           C  
-ANISOU 8231  CG  LEU D 739     8624  11711   8336    504    427    372       C  
-ATOM   8232  CD1 LEU D 739    -129.192  32.661 -43.371  1.00 75.23           C  
-ANISOU 8232  CD1 LEU D 739     8506  11828   8249    604    445    523       C  
-ATOM   8233  CD2 LEU D 739    -128.845  32.321 -40.933  1.00 76.52           C  
-ANISOU 8233  CD2 LEU D 739     8817  11630   8627    438    415    403       C  
-ATOM   8234  N   ILE D 740    -130.310  27.505 -42.672  1.00 67.39           N  
-ANISOU 8234  N   ILE D 740     7646  10866   7094    410    360   -189       N  
-ATOM   8235  CA  ILE D 740    -129.754  26.173 -42.497  1.00 66.10           C  
-ANISOU 8235  CA  ILE D 740     7524  10654   6937    364    349   -320       C  
-ATOM   8236  C   ILE D 740    -130.782  25.222 -43.052  1.00 67.13           C  
-ANISOU 8236  C   ILE D 740     7620  10903   6982    364    316   -489       C  
-ATOM   8237  O   ILE D 740    -131.686  24.786 -42.329  1.00 66.66           O  
-ANISOU 8237  O   ILE D 740     7590  10772   6968    288    291   -587       O  
-ATOM   8238  CB  ILE D 740    -129.441  25.868 -41.020  1.00 63.10           C  
-ANISOU 8238  CB  ILE D 740     7235  10050   6691    259    344   -347       C  
-ATOM   8239  CG1 ILE D 740    -128.649  27.023 -40.381  1.00 57.99           C  
-ANISOU 8239  CG1 ILE D 740     6613   9284   6138    258    369   -185       C  
-ATOM   8240  CG2 ILE D 740    -128.669  24.551 -40.907  1.00 63.27           C  
-ANISOU 8240  CG2 ILE D 740     7298  10017   6725    224    338   -456       C  
-ATOM   8241  CD1 ILE D 740    -127.216  27.139 -40.864  1.00 55.32           C  
-ANISOU 8241  CD1 ILE D 740     6266   8956   5798    303    397    -93       C  
-ATOM   8242  N   PRO D 741    -130.657  24.910 -44.352  1.00 70.84           N  
-ANISOU 8242  N   PRO D 741     8021  11567   7329    452    313   -522       N  
-ATOM   8243  CA  PRO D 741    -131.673  24.103 -45.011  1.00 71.70           C  
-ANISOU 8243  CA  PRO D 741     8080  11812   7350    466    277   -688       C  
-ATOM   8244  C   PRO D 741    -131.750  22.695 -44.455  1.00 71.48           C  
-ANISOU 8244  C   PRO D 741     8102  11672   7383    378    244   -868       C  
-ATOM   8245  O   PRO D 741    -130.724  22.025 -44.266  1.00 64.51           O  
-ANISOU 8245  O   PRO D 741     7262  10706   6543    361    248   -896       O  
-ATOM   8246  CB  PRO D 741    -131.248  24.072 -46.487  1.00 74.77           C  
-ANISOU 8246  CB  PRO D 741     8383  12432   7594    591    283   -679       C  
-ATOM   8247  CG  PRO D 741    -130.024  24.897 -46.610  1.00 72.83           C  
-ANISOU 8247  CG  PRO D 741     8140  12172   7361    640    328   -492       C  
-ATOM   8248  CD  PRO D 741    -129.550  25.286 -45.247  1.00 71.74           C  
-ANISOU 8248  CD  PRO D 741     8092  11787   7378    545    344   -411       C  
-ATOM   8249  N   HIS D 742    -132.976  22.291 -44.152  1.00 72.80           N  
-ANISOU 8249  N   HIS D 742     8263  11833   7566    320    212   -980       N  
-ATOM   8250  CA  HIS D 742    -133.261  20.986 -43.609  1.00 76.54           C  
-ANISOU 8250  CA  HIS D 742     8773  12197   8111    228    179  -1145       C  
-ATOM   8251  C   HIS D 742    -134.142  20.252 -44.592  1.00 77.64           C  
-ANISOU 8251  C   HIS D 742     8835  12501   8163    260    135  -1312       C  
-ATOM   8252  O   HIS D 742    -134.610  20.826 -45.556  1.00 80.89           O  
-ANISOU 8252  O   HIS D 742     9170  13107   8457    349    134  -1293       O  
-ATOM   8253  CB  HIS D 742    -134.004  21.119 -42.275  1.00 75.27           C  
-ANISOU 8253  CB  HIS D 742     8664  11877   8058    119    178  -1130       C  
-ATOM   8254  CG  HIS D 742    -133.121  21.455 -41.107  1.00 75.87           C  
-ANISOU 8254  CG  HIS D 742     8823  11762   8242     67    208  -1019       C  
-ATOM   8255  ND1 HIS D 742    -132.441  22.649 -41.000  1.00 74.94           N  
-ANISOU 8255  ND1 HIS D 742     8717  11631   8126    115    243   -853       N  
-ATOM   8256  CD2 HIS D 742    -132.835  20.761 -39.980  1.00 75.18           C  
-ANISOU 8256  CD2 HIS D 742     8806  11493   8267    -27    206  -1050       C  
-ATOM   8257  CE1 HIS D 742    -131.767  22.674 -39.862  1.00 74.89           C  
-ANISOU 8257  CE1 HIS D 742     8784  11446   8225     53    258   -799       C  
-ATOM   8258  NE2 HIS D 742    -131.991  21.541 -39.224  1.00 74.23           N  
-ANISOU 8258  NE2 HIS D 742     8738  11264   8203    -31    239   -913       N  
-ATOM   8259  N   ASP D 743    -134.389  18.982 -44.314  1.00 81.81           N  
-ANISOU 8259  N   ASP D 743     9381  12946   8758    186     98  -1476       N  
-ATOM   8260  CA  ASP D 743    -135.362  18.218 -45.091  1.00 81.60           C  
-ANISOU 8260  CA  ASP D 743     9280  13047   8676    196     47  -1657       C  
-ATOM   8261  C   ASP D 743    -136.164  17.234 -44.241  1.00 75.48           C  
-ANISOU 8261  C   ASP D 743     8531  12124   8024     67     13  -1781       C  
-ATOM   8262  O   ASP D 743    -135.645  16.187 -43.865  1.00 69.43           O  
-ANISOU 8262  O   ASP D 743     7808  11220   7352     10     -4  -1865       O  
-ATOM   8263  CB  ASP D 743    -134.624  17.478 -46.206  1.00 87.16           C  
-ANISOU 8263  CB  ASP D 743     9943  13868   9305    283     24  -1769       C  
-ATOM   8264  CG  ASP D 743    -135.576  16.776 -47.191  1.00 91.61           C  
-ANISOU 8264  CG  ASP D 743    10413  14600   9794    318    -35  -1967       C  
-ATOM   8265  OD1 ASP D 743    -136.658  17.331 -47.469  1.00 94.86           O  
-ANISOU 8265  OD1 ASP D 743    10767  15134  10141    334    -41  -1963       O  
-ATOM   8266  OD2 ASP D 743    -135.254  15.669 -47.682  1.00 92.61           O  
-ANISOU 8266  OD2 ASP D 743    10522  14737   9929    332    -77  -2134       O  
-ATOM   8267  N   PRO D 749    -141.793  20.214 -40.643  1.00 71.13           N  
-ANISOU 8267  N   PRO D 749     7932  11522   7573   -199     43  -1541       N  
-ATOM   8268  CA  PRO D 749    -140.631  21.037 -40.328  1.00 77.23           C  
-ANISOU 8268  CA  PRO D 749     8770  12217   8358   -152     83  -1391       C  
-ATOM   8269  C   PRO D 749    -140.804  21.514 -38.878  1.00 75.11           C  
-ANISOU 8269  C   PRO D 749     8556  11806   8177   -222    105  -1299       C  
-ATOM   8270  O   PRO D 749    -141.626  22.390 -38.616  1.00 70.15           O  
-ANISOU 8270  O   PRO D 749     7901  11233   7519   -205    109  -1246       O  
-ATOM   8271  CB  PRO D 749    -140.531  22.223 -41.302  1.00 75.78           C  
-ANISOU 8271  CB  PRO D 749     8543  12194   8058    -24     97  -1299       C  
-ATOM   8272  N   PRO D 750    -140.052  20.923 -37.928  1.00 73.07           N  
-ANISOU 8272  N   PRO D 750     8368  11373   8021   -295    118  -1284       N  
-ATOM   8273  CA  PRO D 750    -140.321  21.154 -36.477  1.00 71.68           C  
-ANISOU 8273  CA  PRO D 750     8234  11074   7926   -369    134  -1221       C  
-ATOM   8274  C   PRO D 750    -140.311  22.621 -36.017  1.00 66.83           C  
-ANISOU 8274  C   PRO D 750     7633  10466   7293   -313    156  -1089       C  
-ATOM   8275  O   PRO D 750    -139.341  23.348 -36.233  1.00 63.78           O  
-ANISOU 8275  O   PRO D 750     7276  10057   6899   -248    175   -998       O  
-ATOM   8276  CB  PRO D 750    -139.197  20.388 -35.757  1.00 70.55           C  
-ANISOU 8276  CB  PRO D 750     8165  10760   7879   -424    147  -1209       C  
-ATOM   8277  CG  PRO D 750    -138.406  19.665 -36.801  1.00 72.47           C  
-ANISOU 8277  CG  PRO D 750     8407  11028   8100   -388    135  -1279       C  
-ATOM   8278  CD  PRO D 750    -138.913  20.016 -38.172  1.00 72.28           C  
-ANISOU 8278  CD  PRO D 750     8309  11194   7962   -303    116  -1326       C  
-ATOM   8279  N   LEU D 751    -141.382  23.034 -35.360  1.00 63.81           N  
-ANISOU 8279  N   LEU D 751     7225  10109   6911   -341    152  -1082       N  
-ATOM   8280  CA  LEU D 751    -141.528  24.413 -34.922  1.00 66.34           C  
-ANISOU 8280  CA  LEU D 751     7550  10438   7219   -284    164   -977       C  
-ATOM   8281  C   LEU D 751    -140.593  24.699 -33.754  1.00 64.74           C  
-ANISOU 8281  C   LEU D 751     7420  10079   7101   -308    185   -897       C  
-ATOM   8282  O   LEU D 751    -140.547  23.936 -32.793  1.00 60.58           O  
-ANISOU 8282  O   LEU D 751     6923   9458   6637   -390    188   -923       O  
-ATOM   8283  CB  LEU D 751    -142.975  24.673 -34.510  1.00 67.18           C  
-ANISOU 8283  CB  LEU D 751     7603  10624   7299   -307    151  -1007       C  
-ATOM   8284  CG  LEU D 751    -143.358  26.140 -34.311  1.00 68.15           C  
-ANISOU 8284  CG  LEU D 751     7711  10790   7393   -230    153   -920       C  
-ATOM   8285  CD1 LEU D 751    -143.096  26.972 -35.562  1.00 65.98           C  
-ANISOU 8285  CD1 LEU D 751     7408  10612   7048   -120    154   -867       C  
-ATOM   8286  CD2 LEU D 751    -144.826  26.214 -33.906  1.00 72.04           C  
-ANISOU 8286  CD2 LEU D 751     8147  11370   7855   -256    138   -966       C  
-ATOM   8287  N   LEU D 752    -139.845  25.801 -33.846  1.00 66.35           N  
-ANISOU 8287  N   LEU D 752     7645  10256   7308   -234    197   -797       N  
-ATOM   8288  CA  LEU D 752    -138.908  26.192 -32.791  1.00 66.60           C  
-ANISOU 8288  CA  LEU D 752     7738  10145   7420   -246    212   -725       C  
-ATOM   8289  C   LEU D 752    -139.627  27.086 -31.775  1.00 63.66           C  
-ANISOU 8289  C   LEU D 752     7358   9762   7068   -240    205   -693       C  
-ATOM   8290  O   LEU D 752    -139.533  28.319 -31.826  1.00 62.97           O  
-ANISOU 8290  O   LEU D 752     7263   9678   6985   -169    202   -622       O  
-ATOM   8291  CB  LEU D 752    -137.661  26.863 -33.404  1.00 66.85           C  
-ANISOU 8291  CB  LEU D 752     7794  10146   7462   -176    225   -638       C  
-ATOM   8292  CG  LEU D 752    -136.916  25.947 -34.385  1.00 68.66           C  
-ANISOU 8292  CG  LEU D 752     8026  10398   7662   -174    231   -676       C  
-ATOM   8293  CD1 LEU D 752    -135.795  26.694 -35.103  1.00 68.94           C  
-ANISOU 8293  CD1 LEU D 752     8067  10435   7692    -96    248   -577       C  
-ATOM   8294  CD2 LEU D 752    -136.384  24.696 -33.693  1.00 66.23           C  
-ANISOU 8294  CD2 LEU D 752     7769   9982   7414   -258    235   -735       C  
-ATOM   8295  N   ASN D 753    -140.325  26.435 -30.846  1.00 60.78           N  
-ANISOU 8295  N   ASN D 753     6990   9384   6721   -314    202   -746       N  
-ATOM   8296  CA  ASN D 753    -141.261  27.106 -29.951  1.00 62.39           C  
-ANISOU 8296  CA  ASN D 753     7168   9617   6921   -309    192   -739       C  
-ATOM   8297  C   ASN D 753    -141.073  26.785 -28.471  1.00 59.19           C  
-ANISOU 8297  C   ASN D 753     6794   9122   6573   -366    200   -734       C  
-ATOM   8298  O   ASN D 753    -141.938  27.101 -27.651  1.00 58.28           O  
-ANISOU 8298  O   ASN D 753     6649   9047   6446   -372    193   -743       O  
-ATOM   8299  CB  ASN D 753    -142.706  26.804 -30.367  1.00 63.22           C  
-ANISOU 8299  CB  ASN D 753     7204   9857   6960   -327    179   -806       C  
-ATOM   8300  CG  ASN D 753    -143.137  25.375 -30.047  1.00 65.94           C  
-ANISOU 8300  CG  ASN D 753     7539  10196   7321   -431    181   -879       C  
-ATOM   8301  OD1 ASN D 753    -142.313  24.487 -29.796  1.00 67.70           O  
-ANISOU 8301  OD1 ASN D 753     7806  10321   7598   -485    192   -886       O  
-ATOM   8302  ND2 ASN D 753    -144.444  25.161 -30.032  1.00 63.57           N  
-ANISOU 8302  ND2 ASN D 753     7175   9998   6980   -461    169   -930       N  
-ATOM   8303  N   ASN D 754    -139.940  26.189 -28.129  1.00 58.21           N  
-ANISOU 8303  N   ASN D 754     6726   8888   6504   -400    214   -718       N  
-ATOM   8304  CA  ASN D 754    -139.615  25.926 -26.737  1.00 61.40           C  
-ANISOU 8304  CA  ASN D 754     7160   9212   6958   -442    223   -702       C  
-ATOM   8305  C   ASN D 754    -138.095  25.940 -26.549  1.00 57.62           C  
-ANISOU 8305  C   ASN D 754     6744   8613   6537   -430    235   -658       C  
-ATOM   8306  O   ASN D 754    -137.335  25.856 -27.512  1.00 63.87           O  
-ANISOU 8306  O   ASN D 754     7555   9383   7329   -407    239   -647       O  
-ATOM   8307  CB  ASN D 754    -140.249  24.605 -26.256  1.00 61.81           C  
-ANISOU 8307  CB  ASN D 754     7196   9275   7016   -538    232   -748       C  
-ATOM   8308  CG  ASN D 754    -139.682  23.400 -26.968  1.00 63.16           C  
-ANISOU 8308  CG  ASN D 754     7390   9396   7212   -588    239   -781       C  
-ATOM   8309  OD1 ASN D 754    -138.639  22.873 -26.580  1.00 63.37           O  
-ANISOU 8309  OD1 ASN D 754     7468   9320   7290   -610    252   -760       O  
-ATOM   8310  ND2 ASN D 754    -140.339  22.984 -28.041  1.00 63.75           N  
-ANISOU 8310  ND2 ASN D 754     7425   9549   7249   -597    227   -841       N  
-ATOM   8311  N   ALA D 755    -137.674  26.068 -25.297  1.00 53.84           N  
-ANISOU 8311  N   ALA D 755     6291   8068   6098   -439    239   -634       N  
-ATOM   8312  CA  ALA D 755    -136.275  26.202 -24.952  1.00 50.38           C  
-ANISOU 8312  CA  ALA D 755     5905   7521   5715   -423    246   -593       C  
-ATOM   8313  C   ALA D 755    -135.459  24.959 -25.343  1.00 52.92           C  
-ANISOU 8313  C   ALA D 755     6266   7782   6059   -474    264   -603       C  
-ATOM   8314  O   ALA D 755    -134.366  25.083 -25.885  1.00 52.08           O  
-ANISOU 8314  O   ALA D 755     6191   7621   5974   -446    269   -576       O  
-ATOM   8315  CB  ALA D 755    -136.139  26.498 -23.461  1.00 47.58           C  
-ANISOU 8315  CB  ALA D 755     5559   7131   5389   -423    244   -580       C  
-ATOM   8316  N   ASP D 756    -135.989  23.764 -25.088  1.00 54.78           N  
-ANISOU 8316  N   ASP D 756     6494   8026   6293   -548    273   -640       N  
-ATOM   8317  CA  ASP D 756    -135.281  22.526 -25.429  1.00 58.22           C  
-ANISOU 8317  CA  ASP D 756     6964   8394   6761   -596    284   -658       C  
-ATOM   8318  C   ASP D 756    -135.029  22.400 -26.933  1.00 59.54           C  
-ANISOU 8318  C   ASP D 756     7127   8592   6902   -568    278   -689       C  
-ATOM   8319  O   ASP D 756    -133.957  21.993 -27.333  1.00 56.01           O  
-ANISOU 8319  O   ASP D 756     6718   8086   6478   -559    285   -684       O  
-ATOM   8320  CB  ASP D 756    -136.045  21.310 -24.908  1.00 60.76           C  
-ANISOU 8320  CB  ASP D 756     7267   8717   7101   -682    290   -690       C  
-ATOM   8321  CG  ASP D 756    -135.223  19.992 -24.898  1.00 63.89           C  
-ANISOU 8321  CG  ASP D 756     7705   9014   7556   -734    301   -700       C  
-ATOM   8322  OD1 ASP D 756    -135.167  19.302 -25.945  1.00 66.91           O  
-ANISOU 8322  OD1 ASP D 756     8086   9395   7943   -748    293   -754       O  
-ATOM   8323  OD2 ASP D 756    -134.693  19.597 -23.834  1.00 62.39           O  
-ANISOU 8323  OD2 ASP D 756     7545   8754   7409   -759    317   -658       O  
-ATOM   8324  N   SER D 757    -136.020  22.730 -27.755  1.00 60.97           N  
-ANISOU 8324  N   SER D 757     7259   8879   7029   -548    264   -723       N  
-ATOM   8325  CA  SER D 757    -135.876  22.705 -29.217  1.00 64.75           C  
-ANISOU 8325  CA  SER D 757     7720   9418   7464   -508    257   -752       C  
-ATOM   8326  C   SER D 757    -134.810  23.707 -29.707  1.00 64.05           C  
-ANISOU 8326  C   SER D 757     7652   9314   7371   -428    263   -683       C  
-ATOM   8327  O   SER D 757    -134.046  23.412 -30.606  1.00 68.17           O  
-ANISOU 8327  O   SER D 757     8184   9838   7880   -402    268   -687       O  
-ATOM   8328  CB  SER D 757    -137.237  22.981 -29.897  1.00 62.73           C  
-ANISOU 8328  CB  SER D 757     7398   9293   7143   -495    240   -796       C  
-ATOM   8329  N   VAL D 758    -134.764  24.890 -29.109  1.00 61.09           N  
-ANISOU 8329  N   VAL D 758     7278   8922   7011   -388    263   -620       N  
-ATOM   8330  CA  VAL D 758    -133.777  25.912 -29.490  1.00 60.81           C  
-ANISOU 8330  CA  VAL D 758     7255   8858   6991   -319    267   -544       C  
-ATOM   8331  C   VAL D 758    -132.377  25.435 -29.133  1.00 56.58           C  
-ANISOU 8331  C   VAL D 758     6773   8216   6510   -335    282   -521       C  
-ATOM   8332  O   VAL D 758    -131.463  25.478 -29.943  1.00 56.95           O  
-ANISOU 8332  O   VAL D 758     6828   8259   6552   -300    291   -490       O  
-ATOM   8333  CB  VAL D 758    -134.069  27.242 -28.777  1.00 60.10           C  
-ANISOU 8333  CB  VAL D 758     7153   8754   6929   -280    256   -495       C  
-ATOM   8334  CG1 VAL D 758    -132.909  28.212 -28.922  1.00 61.72           C  
-ANISOU 8334  CG1 VAL D 758     7374   8893   7184   -225    259   -413       C  
-ATOM   8335  CG2 VAL D 758    -135.333  27.843 -29.348  1.00 59.75           C  
-ANISOU 8335  CG2 VAL D 758     7053   8823   6827   -245    242   -507       C  
-ATOM   8336  N   GLN D 759    -132.254  24.964 -27.909  1.00 56.26           N  
-ANISOU 8336  N   GLN D 759     6764   8100   6513   -386    285   -533       N  
-ATOM   8337  CA  GLN D 759    -131.009  24.439 -27.395  1.00 56.45           C  
-ANISOU 8337  CA  GLN D 759     6837   8024   6586   -404    298   -515       C  
-ATOM   8338  C   GLN D 759    -130.458  23.325 -28.296  1.00 54.50           C  
-ANISOU 8338  C   GLN D 759     6607   7776   6326   -419    306   -551       C  
-ATOM   8339  O   GLN D 759    -129.278  23.290 -28.584  1.00 54.38           O  
-ANISOU 8339  O   GLN D 759     6618   7716   6329   -395    316   -521       O  
-ATOM   8340  CB  GLN D 759    -131.235  23.946 -25.975  1.00 56.96           C  
-ANISOU 8340  CB  GLN D 759     6921   8038   6684   -457    300   -528       C  
-ATOM   8341  CG  GLN D 759    -130.036  23.807 -25.083  1.00 59.08           C  
-ANISOU 8341  CG  GLN D 759     7233   8209   7005   -461    309   -496       C  
-ATOM   8342  CD  GLN D 759    -130.499  23.334 -23.683  1.00 66.20           C  
-ANISOU 8342  CD  GLN D 759     8138   9092   7921   -506    312   -505       C  
-ATOM   8343  OE1 GLN D 759    -131.611  23.683 -23.238  1.00 62.31           O  
-ANISOU 8343  OE1 GLN D 759     7610   8662   7404   -512    304   -518       O  
-ATOM   8344  NE2 GLN D 759    -129.665  22.539 -22.994  1.00 62.31           N  
-ANISOU 8344  NE2 GLN D 759     7684   8527   7464   -534    326   -492       N  
-ATOM   8345  N   ALA D 760    -131.308  22.398 -28.721  1.00 52.62           N  
-ANISOU 8345  N   ALA D 760     6348   7585   6059   -459    300   -622       N  
-ATOM   8346  CA  ALA D 760    -130.874  21.324 -29.625  1.00 51.07           C  
-ANISOU 8346  CA  ALA D 760     6160   7392   5853   -467    299   -677       C  
-ATOM   8347  C   ALA D 760    -130.320  21.892 -30.956  1.00 47.17           C  
-ANISOU 8347  C   ALA D 760     5644   6972   5306   -390    300   -656       C  
-ATOM   8348  O   ALA D 760    -129.374  21.376 -31.506  1.00 47.12           O  
-ANISOU 8348  O   ALA D 760     5656   6949   5298   -371    306   -666       O  
-ATOM   8349  CB  ALA D 760    -132.028  20.371 -29.894  1.00 51.94           C  
-ANISOU 8349  CB  ALA D 760     6238   7547   5949   -520    284   -766       C  
-ATOM   8350  N   LYS D 761    -130.926  22.954 -31.461  1.00 45.65           N  
-ANISOU 8350  N   LYS D 761     5409   6867   5068   -342    296   -622       N  
-ATOM   8351  CA  LYS D 761    -130.426  23.631 -32.661  1.00 49.29           C  
-ANISOU 8351  CA  LYS D 761     5841   7408   5478   -263    301   -574       C  
-ATOM   8352  C   LYS D 761    -129.100  24.385 -32.450  1.00 48.70           C  
-ANISOU 8352  C   LYS D 761     5792   7264   5447   -227    318   -475       C  
-ATOM   8353  O   LYS D 761    -128.243  24.387 -33.350  1.00 46.12           O  
-ANISOU 8353  O   LYS D 761     5455   6975   5093   -179    329   -445       O  
-ATOM   8354  CB  LYS D 761    -131.514  24.551 -33.235  1.00 50.35           C  
-ANISOU 8354  CB  LYS D 761     5918   7656   5557   -221    292   -556       C  
-ATOM   8355  N   VAL D 762    -128.932  25.006 -31.277  1.00 43.92           N  
-ANISOU 8355  N   VAL D 762     5213   6567   4909   -246    319   -430       N  
-ATOM   8356  CA  VAL D 762    -127.671  25.656 -30.915  1.00 41.91           C  
-ANISOU 8356  CA  VAL D 762     4981   6230   4712   -223    330   -348       C  
-ATOM   8357  C   VAL D 762    -126.563  24.614 -30.862  1.00 41.31           C  
-ANISOU 8357  C   VAL D 762     4946   6097   4652   -244    342   -372       C  
-ATOM   8358  O   VAL D 762    -125.483  24.798 -31.425  1.00 40.88           O  
-ANISOU 8358  O   VAL D 762     4891   6042   4599   -206    355   -321       O  
-ATOM   8359  CB  VAL D 762    -127.746  26.357 -29.538  1.00 39.56           C  
-ANISOU 8359  CB  VAL D 762     4703   5845   4485   -243    320   -324       C  
-ATOM   8360  CG1 VAL D 762    -126.368  26.860 -29.108  1.00 37.68           C  
-ANISOU 8360  CG1 VAL D 762     4488   5515   4315   -227    327   -259       C  
-ATOM   8361  CG2 VAL D 762    -128.723  27.502 -29.595  1.00 38.61           C  
-ANISOU 8361  CG2 VAL D 762     4540   5772   4357   -210    305   -297       C  
-ATOM   8362  N   GLU D 763    -126.848  23.506 -30.210  1.00 43.13           N  
-ANISOU 8362  N   GLU D 763     5208   6284   4896   -303    338   -445       N  
-ATOM   8363  CA  GLU D 763    -125.892  22.406 -30.154  1.00 48.55           C  
-ANISOU 8363  CA  GLU D 763     5934   6912   5601   -322    346   -475       C  
-ATOM   8364  C   GLU D 763    -125.582  21.882 -31.549  1.00 49.72           C  
-ANISOU 8364  C   GLU D 763     6061   7141   5690   -282    348   -509       C  
-ATOM   8365  O   GLU D 763    -124.426  21.620 -31.862  1.00 50.49           O  
-ANISOU 8365  O   GLU D 763     6173   7218   5791   -255    359   -491       O  
-ATOM   8366  CB  GLU D 763    -126.280  21.325 -29.125  1.00 50.38           C  
-ANISOU 8366  CB  GLU D 763     6200   7072   5871   -393    343   -533       C  
-ATOM   8367  CG  GLU D 763    -126.016  21.858 -27.726  1.00 55.23           C  
-ANISOU 8367  CG  GLU D 763     6838   7607   6539   -411    347   -483       C  
-ATOM   8368  CD  GLU D 763    -126.554  20.965 -26.656  1.00 60.43           C  
-ANISOU 8368  CD  GLU D 763     7517   8217   7226   -475    346   -518       C  
-ATOM   8369  OE1 GLU D 763    -127.181  21.573 -25.768  1.00 62.78           O  
-ANISOU 8369  OE1 GLU D 763     7803   8520   7532   -486    342   -498       O  
-ATOM   8370  OE2 GLU D 763    -126.358  19.710 -26.708  1.00 59.82           O  
-ANISOU 8370  OE2 GLU D 763     7463   8099   7166   -510    349   -560       O  
-ATOM   8371  N   MET D 764    -126.593  21.768 -32.405  1.00 49.26           N  
-ANISOU 8371  N   MET D 764     5959   7186   5571   -270    336   -561       N  
-ATOM   8372  CA  MET D 764    -126.323  21.419 -33.787  1.00 51.65           C  
-ANISOU 8372  CA  MET D 764     6228   7592   5803   -216    334   -594       C  
-ATOM   8373  C   MET D 764    -125.348  22.412 -34.416  1.00 47.22           C  
-ANISOU 8373  C   MET D 764     5645   7076   5219   -144    354   -488       C  
-ATOM   8374  O   MET D 764    -124.371  22.006 -35.045  1.00 43.06           O  
-ANISOU 8374  O   MET D 764     5118   6575   4668   -106    363   -488       O  
-ATOM   8375  CB  MET D 764    -127.590  21.359 -34.621  1.00 56.21           C  
-ANISOU 8375  CB  MET D 764     6753   8294   6312   -204    316   -659       C  
-ATOM   8376  CG  MET D 764    -127.287  21.088 -36.100  1.00 60.96           C  
-ANISOU 8376  CG  MET D 764     7308   9028   6826   -131    313   -694       C  
-ATOM   8377  SD  MET D 764    -128.714  21.428 -37.102  1.00 68.55           S  
-ANISOU 8377  SD  MET D 764     8193  10158   7693    -96    294   -739       S  
-ATOM   8378  CE  MET D 764    -128.553  23.208 -37.223  1.00 71.12           C  
-ANISOU 8378  CE  MET D 764     8491  10528   8004    -33    319   -571       C  
-ATOM   8379  N   LEU D 765    -125.633  23.703 -34.278  1.00 43.79           N  
-ANISOU 8379  N   LEU D 765     5187   6656   4795   -122    359   -397       N  
-ATOM   8380  CA  LEU D 765    -124.751  24.713 -34.851  1.00 44.88           C  
-ANISOU 8380  CA  LEU D 765     5297   6827   4930    -59    378   -279       C  
-ATOM   8381  C   LEU D 765    -123.321  24.623 -34.305  1.00 45.09           C  
-ANISOU 8381  C   LEU D 765     5362   6752   5018    -68    392   -233       C  
-ATOM   8382  O   LEU D 765    -122.362  24.771 -35.049  1.00 49.88           O  
-ANISOU 8382  O   LEU D 765     5945   7406   5601    -19    409   -176       O  
-ATOM   8383  CB  LEU D 765    -125.297  26.107 -34.626  1.00 44.97           C  
-ANISOU 8383  CB  LEU D 765     5279   6836   4969    -42    376   -191       C  
-ATOM   8384  CG  LEU D 765    -126.553  26.490 -35.405  1.00 50.47           C  
-ANISOU 8384  CG  LEU D 765     5923   7659   5594     -9    366   -202       C  
-ATOM   8385  CD1 LEU D 765    -126.912  27.940 -35.117  1.00 53.47           C  
-ANISOU 8385  CD1 LEU D 765     6279   8015   6022     15    364   -102       C  
-ATOM   8386  CD2 LEU D 765    -126.358  26.283 -36.896  1.00 52.52           C  
-ANISOU 8386  CD2 LEU D 765     6129   8072   5754     61    377   -193       C  
-ATOM   8387  N   ASP D 766    -123.174  24.348 -33.014  1.00 44.21           N  
-ANISOU 8387  N   ASP D 766     5303   6513   4980   -127    386   -258       N  
-ATOM   8388  CA  ASP D 766    -121.844  24.171 -32.440  1.00 43.83           C  
-ANISOU 8388  CA  ASP D 766     5291   6373   4988   -135    398   -226       C  
-ATOM   8389  C   ASP D 766    -121.110  23.054 -33.168  1.00 40.95           C  
-ANISOU 8389  C   ASP D 766     4935   6048   4577   -115    405   -277       C  
-ATOM   8390  O   ASP D 766    -119.926  23.185 -33.483  1.00 39.22           O  
-ANISOU 8390  O   ASP D 766     4710   5831   4362    -81    421   -221       O  
-ATOM   8391  CB  ASP D 766    -121.919  23.829 -30.944  1.00 44.62           C  
-ANISOU 8391  CB  ASP D 766     5445   6352   5158   -198    389   -262       C  
-ATOM   8392  CG  ASP D 766    -122.574  24.921 -30.122  1.00 47.10           C  
-ANISOU 8392  CG  ASP D 766     5748   6628   5518   -210    377   -225       C  
-ATOM   8393  OD1 ASP D 766    -122.645  26.096 -30.575  1.00 44.55           O  
-ANISOU 8393  OD1 ASP D 766     5386   6339   5204   -171    376   -151       O  
-ATOM   8394  OD2 ASP D 766    -123.003  24.591 -28.989  1.00 53.34           O  
-ANISOU 8394  OD2 ASP D 766     6569   7357   6340   -256    367   -268       O  
-ATOM   8395  N   ASN D 767    -121.807  21.934 -33.373  1.00 42.34           N  
-ANISOU 8395  N   ASN D 767     5123   6248   4718   -138    391   -387       N  
-ATOM   8396  CA  ASN D 767    -121.210  20.749 -33.973  1.00 44.78           C  
-ANISOU 8396  CA  ASN D 767     5441   6578   4994   -120    389   -461       C  
-ATOM   8397  C   ASN D 767    -120.878  21.046 -35.429  1.00 46.20           C  
-ANISOU 8397  C   ASN D 767     5562   6907   5086    -38    398   -436       C  
-ATOM   8398  O   ASN D 767    -119.809  20.703 -35.903  1.00 46.40           O  
-ANISOU 8398  O   ASN D 767     5584   6958   5089      3    409   -428       O  
-ATOM   8399  CB  ASN D 767    -122.133  19.525 -33.794  1.00 44.50           C  
-ANISOU 8399  CB  ASN D 767     5426   6518   4964   -170    366   -589       C  
-ATOM   8400  CG  ASN D 767    -121.508  18.201 -34.276  1.00 48.84           C  
-ANISOU 8400  CG  ASN D 767     5992   7061   5503   -156    356   -682       C  
-ATOM   8401  OD1 ASN D 767    -122.211  17.261 -34.722  1.00 52.42           O  
-ANISOU 8401  OD1 ASN D 767     6435   7540   5941   -169    332   -795       O  
-ATOM   8402  ND2 ASN D 767    -120.192  18.113 -34.171  1.00 46.18           N  
-ANISOU 8402  ND2 ASN D 767     5677   6686   5181   -128    371   -640       N  
-ATOM   8403  N   LEU D 768    -121.762  21.774 -36.100  1.00 50.78           N  
-ANISOU 8403  N   LEU D 768     6090   7593   5613    -10    396   -410       N  
-ATOM   8404  CA  LEU D 768    -121.502  22.207 -37.478  1.00 53.74           C  
-ANISOU 8404  CA  LEU D 768     6396   8129   5895     76    407   -363       C  
-ATOM   8405  C   LEU D 768    -120.240  23.052 -37.567  1.00 52.50           C  
-ANISOU 8405  C   LEU D 768     6223   7965   5759    114    437   -225       C  
-ATOM   8406  O   LEU D 768    -119.431  22.857 -38.468  1.00 53.04           O  
-ANISOU 8406  O   LEU D 768     6256   8131   5765    177    450   -205       O  
-ATOM   8407  CB  LEU D 768    -122.699  22.998 -38.047  1.00 55.22           C  
-ANISOU 8407  CB  LEU D 768     6529   8423   6030    101    402   -338       C  
-ATOM   8408  CG  LEU D 768    -123.940  22.184 -38.438  1.00 57.09           C  
-ANISOU 8408  CG  LEU D 768     6751   8729   6212     88    373   -476       C  
-ATOM   8409  CD1 LEU D 768    -124.971  23.083 -39.105  1.00 56.82           C  
-ANISOU 8409  CD1 LEU D 768     6655   8822   6115    129    372   -434       C  
-ATOM   8410  CD2 LEU D 768    -123.573  21.023 -39.347  1.00 58.51           C  
-ANISOU 8410  CD2 LEU D 768     6913   8995   6322    129    360   -589       C  
-ATOM   8411  N   LEU D 769    -120.084  23.990 -36.643  1.00 50.61           N  
-ANISOU 8411  N   LEU D 769     6004   7617   5610     78    444   -134       N  
-ATOM   8412  CA  LEU D 769    -118.900  24.849 -36.629  1.00 54.01           C  
-ANISOU 8412  CA  LEU D 769     6416   8022   6084    103    467     -1       C  
-ATOM   8413  C   LEU D 769    -117.588  24.034 -36.563  1.00 55.01           C  
-ANISOU 8413  C   LEU D 769     6568   8119   6214    109    478    -23       C  
-ATOM   8414  O   LEU D 769    -116.668  24.239 -37.354  1.00 56.84           O  
-ANISOU 8414  O   LEU D 769     6756   8434   6407    166    499     50       O  
-ATOM   8415  CB  LEU D 769    -118.975  25.860 -35.478  1.00 58.62           C  
-ANISOU 8415  CB  LEU D 769     7022   8471   6781     56    462     67       C  
-ATOM   8416  CG  LEU D 769    -119.094  27.364 -35.798  1.00 60.37           C  
-ANISOU 8416  CG  LEU D 769     7187   8714   7037     86    470    206       C  
-ATOM   8417  CD1 LEU D 769    -118.759  28.103 -34.509  1.00 56.52           C  
-ANISOU 8417  CD1 LEU D 769     6730   8067   6679     39    459    244       C  
-ATOM   8418  CD2 LEU D 769    -118.253  27.902 -36.951  1.00 61.79           C  
-ANISOU 8418  CD2 LEU D 769     7297   9000   7179    154    499    331       C  
-ATOM   8419  N   ASP D 770    -117.506  23.104 -35.624  1.00 54.43           N  
-ANISOU 8419  N   ASP D 770     6562   7934   6185     56    464   -117       N  
-ATOM   8420  CA  ASP D 770    -116.296  22.320 -35.462  1.00 58.56           C  
-ANISOU 8420  CA  ASP D 770     7113   8417   6718     62    471   -141       C  
-ATOM   8421  C   ASP D 770    -116.111  21.345 -36.639  1.00 55.49           C  
-ANISOU 8421  C   ASP D 770     6700   8156   6230    122    469   -220       C  
-ATOM   8422  O   ASP D 770    -114.971  21.000 -37.000  1.00 49.19           O  
-ANISOU 8422  O   ASP D 770     5893   7389   5409    164    482   -206       O  
-ATOM   8423  CB  ASP D 770    -116.297  21.585 -34.112  1.00 62.57           C  
-ANISOU 8423  CB  ASP D 770     7698   8773   7302     -7    457   -211       C  
-ATOM   8424  CG  ASP D 770    -115.807  22.474 -32.926  1.00 65.85           C  
-ANISOU 8424  CG  ASP D 770     8134   9072   7814    -44    462   -128       C  
-ATOM   8425  OD1 ASP D 770    -114.915  23.337 -33.099  1.00 68.64           O  
-ANISOU 8425  OD1 ASP D 770     8455   9434   8192    -18    478    -26       O  
-ATOM   8426  OD2 ASP D 770    -116.307  22.287 -31.796  1.00 64.89           O  
-ANISOU 8426  OD2 ASP D 770     8056   8852   7745    -99    448   -168       O  
-ATOM   8427  N   ILE D 771    -117.214  20.896 -37.227  1.00 51.30           N  
-ANISOU 8427  N   ILE D 771     6152   7701   5638    130    450   -310       N  
-ATOM   8428  CA  ILE D 771    -117.131  20.098 -38.460  1.00 54.01           C  
-ANISOU 8428  CA  ILE D 771     6455   8187   5879    200    442   -394       C  
-ATOM   8429  C   ILE D 771    -116.507  20.915 -39.611  1.00 53.65           C  
-ANISOU 8429  C   ILE D 771     6329   8307   5750    288    469   -281       C  
-ATOM   8430  O   ILE D 771    -115.608  20.429 -40.291  1.00 49.44           O  
-ANISOU 8430  O   ILE D 771     5769   7859   5156    351    477   -296       O  
-ATOM   8431  CB  ILE D 771    -118.499  19.502 -38.857  1.00 52.57           C  
-ANISOU 8431  CB  ILE D 771     6262   8058   5654    189    411   -521       C  
-ATOM   8432  CG1 ILE D 771    -118.814  18.318 -37.940  1.00 52.54           C  
-ANISOU 8432  CG1 ILE D 771     6329   7907   5728    115    384   -645       C  
-ATOM   8433  CG2 ILE D 771    -118.481  19.017 -40.306  1.00 54.05           C  
-ANISOU 8433  CG2 ILE D 771     6384   8434   5720    280    401   -593       C  
-ATOM   8434  CD1 ILE D 771    -120.276  17.939 -37.893  1.00 54.24           C  
-ANISOU 8434  CD1 ILE D 771     6542   8122   5945     70    356   -742       C  
-ATOM   8435  N   GLU D 772    -116.946  22.159 -39.777  1.00 53.78           N  
-ANISOU 8435  N   GLU D 772     6303   8365   5767    295    485   -160       N  
-ATOM   8436  CA  GLU D 772    -116.330  23.056 -40.746  1.00 60.46           C  
-ANISOU 8436  CA  GLU D 772     7069   9351   6554    371    516    -19       C  
-ATOM   8437  C   GLU D 772    -114.817  23.183 -40.485  1.00 64.06           C  
-ANISOU 8437  C   GLU D 772     7528   9760   7053    378    541     67       C  
-ATOM   8438  O   GLU D 772    -114.017  23.140 -41.422  1.00 65.81           O  
-ANISOU 8438  O   GLU D 772     7690  10120   7195    453    562    115       O  
-ATOM   8439  CB  GLU D 772    -117.020  24.426 -40.730  1.00 63.40           C  
-ANISOU 8439  CB  GLU D 772     7404   9727   6957    364    527    110       C  
-ATOM   8440  CG  GLU D 772    -116.587  25.456 -41.794  1.00 69.88           C  
-ANISOU 8440  CG  GLU D 772     8130  10699   7722    442    561    279       C  
-ATOM   8441  CD  GLU D 772    -115.181  26.038 -41.604  1.00 70.73           C  
-ANISOU 8441  CD  GLU D 772     8220  10760   7895    445    591    420       C  
-ATOM   8442  OE1 GLU D 772    -114.784  26.328 -40.447  1.00 76.26           O  
-ANISOU 8442  OE1 GLU D 772     8975  11278   8722    373    586    441       O  
-ATOM   8443  OE2 GLU D 772    -114.485  26.246 -42.626  1.00 75.39           O  
-ANISOU 8443  OE2 GLU D 772     8733  11504   8407    521    620    514       O  
-ATOM   8444  N   VAL D 773    -114.423  23.327 -39.222  1.00 61.55           N  
-ANISOU 8444  N   VAL D 773     7274   9258   6854    304    539     85       N  
-ATOM   8445  CA  VAL D 773    -113.000  23.433 -38.887  1.00 63.27           C  
-ANISOU 8445  CA  VAL D 773     7496   9425   7121    306    559    157       C  
-ATOM   8446  C   VAL D 773    -112.259  22.188 -39.346  1.00 62.71           C  
-ANISOU 8446  C   VAL D 773     7432   9416   6977    352    556     58       C  
-ATOM   8447  O   VAL D 773    -111.178  22.273 -39.932  1.00 65.61           O  
-ANISOU 8447  O   VAL D 773     7753   9872   7305    407    580    127       O  
-ATOM   8448  CB  VAL D 773    -112.770  23.647 -37.365  1.00 62.80           C  
-ANISOU 8448  CB  VAL D 773     7505   9160   7194    221    549    162       C  
-ATOM   8449  CG1 VAL D 773    -111.294  23.508 -37.011  1.00 61.03           C  
-ANISOU 8449  CG1 VAL D 773     7289   8890   7011    224    564    206       C  
-ATOM   8450  CG2 VAL D 773    -113.305  25.011 -36.939  1.00 61.47           C  
-ANISOU 8450  CG2 VAL D 773     7318   8933   7106    188    549    268       C  
-ATOM   8451  N   ALA D 774    -112.837  21.032 -39.047  1.00 59.17           N  
-ANISOU 8451  N   ALA D 774     7041   8918   6522    327    526   -102       N  
-ATOM   8452  CA  ALA D 774    -112.213  19.767 -39.387  1.00 61.46           C  
-ANISOU 8452  CA  ALA D 774     7347   9241   6764    368    515   -217       C  
-ATOM   8453  C   ALA D 774    -112.099  19.632 -40.908  1.00 66.05           C  
-ANISOU 8453  C   ALA D 774     7844  10046   7207    473    521   -228       C  
-ATOM   8454  O   ALA D 774    -111.043  19.262 -41.416  1.00 73.29           O  
-ANISOU 8454  O   ALA D 774     8732  11043   8071    536    533   -225       O  
-ATOM   8455  CB  ALA D 774    -113.010  18.610 -38.804  1.00 57.32           C  
-ANISOU 8455  CB  ALA D 774     6893   8611   6276    317    477   -380       C  
-ATOM   8456  N   TYR D 775    -113.177  19.966 -41.617  1.00 66.55           N  
-ANISOU 8456  N   TYR D 775     7862  10219   7205    496    513   -239       N  
-ATOM   8457  CA  TYR D 775    -113.200  19.869 -43.073  1.00 68.89           C  
-ANISOU 8457  CA  TYR D 775     8069  10748   7357    603    517   -254       C  
-ATOM   8458  C   TYR D 775    -112.194  20.817 -43.720  1.00 67.44           C  
-ANISOU 8458  C   TYR D 775     7806  10693   7126    667    562    -72       C  
-ATOM   8459  O   TYR D 775    -111.510  20.418 -44.644  1.00 65.56           O  
-ANISOU 8459  O   TYR D 775     7509  10617   6783    758    571    -88       O  
-ATOM   8460  CB  TYR D 775    -114.602  20.114 -43.642  1.00 68.06           C  
-ANISOU 8460  CB  TYR D 775     7928  10738   7194    614    500   -294       C  
-ATOM   8461  N   SER D 776    -112.092  22.049 -43.217  1.00 65.14           N  
-ANISOU 8461  N   SER D 776     7508  10325   6917    621    589     97       N  
-ATOM   8462  CA  SER D 776    -111.103  23.018 -43.706  1.00 67.34           C  
-ANISOU 8462  CA  SER D 776     7709  10694   7183    665    633    290       C  
-ATOM   8463  C   SER D 776    -109.681  22.558 -43.520  1.00 70.84           C  
-ANISOU 8463  C   SER D 776     8159  11119   7638    681    647    299       C  
-ATOM   8464  O   SER D 776    -108.860  22.695 -44.420  1.00 78.80           O  
-ANISOU 8464  O   SER D 776     9086  12295   8560    762    676    380       O  
-ATOM   8465  CB  SER D 776    -111.239  24.354 -42.993  1.00 67.20           C  
-ANISOU 8465  CB  SER D 776     7694  10548   7290    597    650    449       C  
-ATOM   8466  OG  SER D 776    -112.435  24.977 -43.389  1.00 71.25           O  
-ANISOU 8466  OG  SER D 776     8177  11119   7777    605    645    479       O  
-ATOM   8467  N   LEU D 777    -109.372  22.043 -42.342  1.00 70.88           N  
-ANISOU 8467  N   LEU D 777     8256  10929   7747    606    630    225       N  
-ATOM   8468  CA  LEU D 777    -108.028  21.555 -42.088  1.00 72.77           C  
-ANISOU 8468  CA  LEU D 777     8507  11143   8001    620    640    224       C  
-ATOM   8469  C   LEU D 777    -107.686  20.463 -43.091  1.00 73.53           C  
-ANISOU 8469  C   LEU D 777     8569  11406   7961    719    631    108       C  
-ATOM   8470  O   LEU D 777    -106.595  20.453 -43.659  1.00 71.57           O  
-ANISOU 8470  O   LEU D 777     8262  11277   7653    786    656    170       O  
-ATOM   8471  CB  LEU D 777    -107.898  21.010 -40.665  1.00 73.16           C  
-ANISOU 8471  CB  LEU D 777     8663  10964   8170    532    617    140       C  
-ATOM   8472  CG  LEU D 777    -107.791  22.041 -39.539  1.00 73.03           C  
-ANISOU 8472  CG  LEU D 777     8674  10781   8293    446    626    253       C  
-ATOM   8473  CD1 LEU D 777    -107.737  21.306 -38.208  1.00 70.26           C  
-ANISOU 8473  CD1 LEU D 777     8425  10240   8032    375    600    148       C  
-ATOM   8474  CD2 LEU D 777    -106.567  22.937 -39.707  1.00 72.80           C  
-ANISOU 8474  CD2 LEU D 777     8578  10789   8292    463    661    421       C  
-ATOM   8475  N   LEU D 778    -108.634  19.553 -43.293  1.00 74.81           N  
-ANISOU 8475  N   LEU D 778     8765  11579   8081    728    593    -65       N  
-ATOM   8476  CA  LEU D 778    -108.438  18.392 -44.163  1.00 76.06           C  
-ANISOU 8476  CA  LEU D 778     8899  11874   8125    820    570   -216       C  
-ATOM   8477  C   LEU D 778    -108.239  18.838 -45.616  1.00 77.99           C  
-ANISOU 8477  C   LEU D 778     9021  12396   8215    937    595   -141       C  
-ATOM   8478  O   LEU D 778    -107.379  18.289 -46.308  1.00 80.07           O  
-ANISOU 8478  O   LEU D 778     9237  12801   8386   1028    599   -178       O  
-ATOM   8479  CB  LEU D 778    -109.594  17.392 -44.020  1.00 74.51           C  
-ANISOU 8479  CB  LEU D 778     8759  11611   7939    792    519   -417       C  
-ATOM   8480  N   ARG D 779    -109.002  19.853 -46.031  1.00 77.54           N  
-ANISOU 8480  N   ARG D 779     8911  12417   8133    936    613    -28       N  
-ATOM   8481  CA  ARG D 779    -108.889  20.523 -47.322  1.00 79.76           C  
-ANISOU 8481  CA  ARG D 779     9068  12958   8279   1040    646     92       C  
-ATOM   8482  C   ARG D 779    -108.212  21.880 -47.151  1.00 78.49           C  
-ANISOU 8482  C   ARG D 779     8860  12781   8180   1013    698    346       C  
-ATOM   8483  O   ARG D 779    -107.019  21.950 -46.880  1.00 69.52           O  
-ANISOU 8483  O   ARG D 779     7717  11614   7081   1011    722    422       O  
-ATOM   8484  CB  ARG D 779    -110.287  20.716 -47.941  1.00 77.04           C  
-ANISOU 8484  CB  ARG D 779     8691  12716   7865   1063    627     46       C  
-ATOM   8485  N   ASP D 788     -97.041  10.113 -45.573  1.00 68.67           N  
-ANISOU 8485  N   ASP D 788     7920  11349   6822   1566    502   -911       N  
-ATOM   8486  CA  ASP D 788     -98.289   9.437 -45.236  1.00 76.80           C  
-ANISOU 8486  CA  ASP D 788     9033  12213   7936   1508    450  -1066       C  
-ATOM   8487  C   ASP D 788     -99.371  10.472 -44.855  1.00 79.50           C  
-ANISOU 8487  C   ASP D 788     9391  12479   8337   1390    472   -947       C  
-ATOM   8488  O   ASP D 788     -99.123  11.335 -44.000  1.00 76.03           O  
-ANISOU 8488  O   ASP D 788     8979  11930   7980   1295    511   -782       O  
-ATOM   8489  CB  ASP D 788     -98.078   8.443 -44.074  1.00 77.53           C  
-ANISOU 8489  CB  ASP D 788     9243  12041   8172   1452    416  -1166       C  
-ATOM   8490  CG  ASP D 788     -99.273   7.487 -43.876  1.00 79.88           C  
-ANISOU 8490  CG  ASP D 788     9615  12185   8553   1414    354  -1353       C  
-ATOM   8491  OD1 ASP D 788    -100.401   7.832 -44.298  1.00 77.11           O  
-ANISOU 8491  OD1 ASP D 788     9242  11877   8180   1385    344  -1371       O  
-ATOM   8492  OD2 ASP D 788     -99.102   6.401 -43.268  1.00 82.95           O  
-ANISOU 8492  OD2 ASP D 788    10080  12400   9037   1407    314  -1475       O  
-ATOM   8493  N   PRO D 789    -100.575  10.384 -45.473  1.00 82.49           N  
-ANISOU 8493  N   PRO D 789     9752  12916   8676   1397    443  -1037       N  
-ATOM   8494  CA  PRO D 789    -101.643  11.344 -45.144  1.00 83.91           C  
-ANISOU 8494  CA  PRO D 789     9945  13031   8907   1293    462   -931       C  
-ATOM   8495  C   PRO D 789    -102.033  11.417 -43.653  1.00 81.41           C  
-ANISOU 8495  C   PRO D 789     9743  12425   8765   1147    460   -896       C  
-ATOM   8496  O   PRO D 789    -102.343  12.501 -43.164  1.00 79.28           O  
-ANISOU 8496  O   PRO D 789     9476  12103   8544   1064    494   -743       O  
-ATOM   8497  CB  PRO D 789    -102.826  10.853 -45.984  1.00 82.24           C  
-ANISOU 8497  CB  PRO D 789     9707  12907   8632   1335    416  -1091       C  
-ATOM   8498  CG  PRO D 789    -102.193  10.198 -47.149  1.00 83.81           C  
-ANISOU 8498  CG  PRO D 789     9825  13333   8688   1490    397  -1204       C  
-ATOM   8499  CD  PRO D 789    -100.950   9.539 -46.623  1.00 82.64           C  
-ANISOU 8499  CD  PRO D 789     9717  13100   8583   1515    396  -1229       C  
-ATOM   8500  N   ILE D 790    -102.000  10.291 -42.946  1.00 83.41           N  
-ANISOU 8500  N   ILE D 790    10083  12499   9110   1122    420  -1033       N  
-ATOM   8501  CA  ILE D 790    -102.247  10.289 -41.510  1.00 83.79           C  
-ANISOU 8501  CA  ILE D 790    10233  12293   9312    998    421   -993       C  
-ATOM   8502  C   ILE D 790    -101.285  11.255 -40.805  1.00 86.30           C  
-ANISOU 8502  C   ILE D 790    10547  12579   9664    957    472   -803       C  
-ATOM   8503  O   ILE D 790    -101.717  12.052 -39.962  1.00 91.81           O  
-ANISOU 8503  O   ILE D 790    11278  13163  10444    856    491   -697       O  
-ATOM   8504  CB  ILE D 790    -102.125   8.875 -40.917  1.00 84.55           C  
-ANISOU 8504  CB  ILE D 790    10411  12218   9496    996    376  -1151       C  
-ATOM   8505  CG1 ILE D 790    -103.273   7.991 -41.417  1.00 84.96           C  
-ANISOU 8505  CG1 ILE D 790    10472  12252   9557   1005    320  -1335       C  
-ATOM   8506  CG2 ILE D 790    -102.185   8.925 -39.396  1.00 85.37           C  
-ANISOU 8506  CG2 ILE D 790    10609  12085   9745    879    385  -1082       C  
-ATOM   8507  CD1 ILE D 790    -102.923   6.518 -41.491  1.00 87.32           C  
-ANISOU 8507  CD1 ILE D 790    10805  12477   9894   1065    267  -1520       C  
-ATOM   8508  N   ASP D 791    -100.000  11.208 -41.167  1.00 81.36           N  
-ANISOU 8508  N   ASP D 791     9875  12064   8975   1037    492   -766       N  
-ATOM   8509  CA  ASP D 791     -99.003  12.127 -40.594  1.00 76.70           C  
-ANISOU 8509  CA  ASP D 791     9266  11461   8415   1004    538   -589       C  
-ATOM   8510  C   ASP D 791     -99.255  13.590 -40.968  1.00 74.21           C  
-ANISOU 8510  C   ASP D 791     8876  11248   8071    973    580   -415       C  
-ATOM   8511  O   ASP D 791     -99.006  14.500 -40.171  1.00 69.38           O  
-ANISOU 8511  O   ASP D 791     8274  10545   7542    895    606   -278       O  
-ATOM   8512  CB  ASP D 791     -97.577  11.744 -41.026  1.00 79.92           C  
-ANISOU 8512  CB  ASP D 791     9625  11989   8750   1105    550   -588       C  
-ATOM   8513  CG  ASP D 791     -97.016  10.545 -40.255  1.00 81.72           C  
-ANISOU 8513  CG  ASP D 791     9936  12067   9045   1114    520   -705       C  
-ATOM   8514  OD1 ASP D 791     -95.773  10.371 -40.257  1.00 93.18           O  
-ANISOU 8514  OD1 ASP D 791    11363  13575  10467   1173    535   -677       O  
-ATOM   8515  OD2 ASP D 791     -97.794   9.772 -39.664  1.00 80.33           O  
-ANISOU 8515  OD2 ASP D 791     9846  11723   8953   1066    482   -818       O  
-ATOM   8516  N   VAL D 792     -99.723  13.827 -42.191  1.00 73.78           N  
-ANISOU 8516  N   VAL D 792     8742  11388   7902   1041    583   -419       N  
-ATOM   8517  CA  VAL D 792     -99.988  15.196 -42.638  1.00 72.03           C  
-ANISOU 8517  CA  VAL D 792     8443  11272   7652   1022    623   -245       C  
-ATOM   8518  C   VAL D 792    -101.112  15.799 -41.790  1.00 68.64           C  
-ANISOU 8518  C   VAL D 792     8076  10669   7335    903    616   -211       C  
-ATOM   8519  O   VAL D 792    -101.005  16.927 -41.315  1.00 65.79           O  
-ANISOU 8519  O   VAL D 792     7700  10256   7042    838    645    -54       O  
-ATOM   8520  CB  VAL D 792    -100.381  15.258 -44.136  1.00 71.56           C  
-ANISOU 8520  CB  VAL D 792     8284  11468   7437   1127    626   -263       C  
-ATOM   8521  CG1 VAL D 792    -100.846  16.663 -44.518  1.00 71.21           C  
-ANISOU 8521  CG1 VAL D 792     8168  11507   7380   1099    664    -78       C  
-ATOM   8522  CG2 VAL D 792     -99.217  14.819 -45.008  1.00 70.97           C  
-ANISOU 8522  CG2 VAL D 792     8130  11596   7240   1254    638   -276       C  
-ATOM   8523  N   ASN D 793    -102.180  15.036 -41.604  1.00 62.29           N  
-ANISOU 8523  N   ASN D 793     7337   9777   6554    877    575   -361       N  
-ATOM   8524  CA  ASN D 793    -103.318  15.500 -40.818  1.00 63.64           C  
-ANISOU 8524  CA  ASN D 793     7564   9796   6820    771    566   -344       C  
-ATOM   8525  C   ASN D 793    -103.029  15.592 -39.311  1.00 59.95           C  
-ANISOU 8525  C   ASN D 793     7180   9105   6492    674    567   -307       C  
-ATOM   8526  O   ASN D 793    -103.480  16.522 -38.667  1.00 62.05           O  
-ANISOU 8526  O   ASN D 793     7458   9286   6831    596    578   -212       O  
-ATOM   8527  CB  ASN D 793    -104.523  14.633 -41.125  1.00 59.68           C  
-ANISOU 8527  CB  ASN D 793     7095   9282   6299    775    522   -513       C  
-ATOM   8528  CG  ASN D 793    -104.996  14.839 -42.552  1.00 60.53           C  
-ANISOU 8528  CG  ASN D 793     7109   9619   6270    862    522   -529       C  
-ATOM   8529  OD1 ASN D 793    -105.367  15.951 -42.943  1.00 65.16           O  
-ANISOU 8529  OD1 ASN D 793     7638  10295   6825    856    550   -399       O  
-ATOM   8530  ND2 ASN D 793    -104.877  13.816 -43.365  1.00 60.98           N  
-ANISOU 8530  ND2 ASN D 793     7144   9785   6242    954    492   -680       N  
-ATOM   8531  N   TYR D 794    -102.223  14.676 -38.781  1.00 57.85           N  
-ANISOU 8531  N   TYR D 794     6963   8759   6256    687    554   -377       N  
-ATOM   8532  CA  TYR D 794    -101.714  14.787 -37.416  1.00 59.33           C  
-ANISOU 8532  CA  TYR D 794     7214   8771   6556    614    560   -329       C  
-ATOM   8533  C   TYR D 794    -101.072  16.147 -37.186  1.00 59.34           C  
-ANISOU 8533  C   TYR D 794     7163   8796   6588    585    597   -152       C  
-ATOM   8534  O   TYR D 794    -101.415  16.839 -36.241  1.00 58.60           O  
-ANISOU 8534  O   TYR D 794     7100   8578   6586    502    599    -90       O  
-ATOM   8535  CB  TYR D 794    -100.690  13.686 -37.126  1.00 58.95           C  
-ANISOU 8535  CB  TYR D 794     7202   8683   6512    661    548   -409       C  
-ATOM   8536  CG  TYR D 794     -99.926  13.844 -35.832  1.00 57.31           C  
-ANISOU 8536  CG  TYR D 794     7041   8334   6398    607    558   -346       C  
-ATOM   8537  CD1 TYR D 794    -100.533  13.598 -34.617  1.00 57.76           C  
-ANISOU 8537  CD1 TYR D 794     7180   8210   6555    525    542   -375       C  
-ATOM   8538  CD2 TYR D 794     -98.592  14.218 -35.822  1.00 57.06           C  
-ANISOU 8538  CD2 TYR D 794     6966   8361   6352    641    584   -259       C  
-ATOM   8539  CE1 TYR D 794     -99.841  13.736 -33.427  1.00 53.52           C  
-ANISOU 8539  CE1 TYR D 794     6680   7562   6094    484    549   -323       C  
-ATOM   8540  CE2 TYR D 794     -97.887  14.350 -34.639  1.00 55.20           C  
-ANISOU 8540  CE2 TYR D 794     6768   8006   6199    596    590   -212       C  
-ATOM   8541  CZ  TYR D 794     -98.522  14.115 -33.436  1.00 52.66           C  
-ANISOU 8541  CZ  TYR D 794     6528   7511   5970    520    571   -246       C  
-ATOM   8542  OH  TYR D 794     -97.835  14.245 -32.244  1.00 46.24           O  
-ANISOU 8542  OH  TYR D 794     5745   6594   5228    483    575   -204       O  
-ATOM   8543  N   GLU D 795    -100.166  16.535 -38.076  1.00 61.69           N  
-ANISOU 8543  N   GLU D 795     7375   9257   6809    656    625    -72       N  
-ATOM   8544  CA  GLU D 795     -99.451  17.808 -37.953  1.00 61.09           C  
-ANISOU 8544  CA  GLU D 795     7236   9206   6771    630    660    104       C  
-ATOM   8545  C   GLU D 795    -100.397  19.009 -37.988  1.00 57.20           C  
-ANISOU 8545  C   GLU D 795     6715   8699   6319    572    669    203       C  
-ATOM   8546  O   GLU D 795    -100.135  20.027 -37.355  1.00 51.13           O  
-ANISOU 8546  O   GLU D 795     5932   7852   5643    512    682    319       O  
-ATOM   8547  CB  GLU D 795     -98.356  17.929 -39.036  1.00 65.10           C  
-ANISOU 8547  CB  GLU D 795     7643   9915   7177    723    690    177       C  
-ATOM   8548  CG  GLU D 795     -97.153  17.018 -38.756  1.00 69.13           C  
-ANISOU 8548  CG  GLU D 795     8173  10420   7673    770    687    115       C  
-ATOM   8549  CD  GLU D 795     -96.091  16.959 -39.861  1.00 72.63           C  
-ANISOU 8549  CD  GLU D 795     8517  11080   8000    875    713    164       C  
-ATOM   8550  OE1 GLU D 795     -96.284  17.523 -40.967  1.00 72.49           O  
-ANISOU 8550  OE1 GLU D 795     8407  11241   7894    925    736    242       O  
-ATOM   8551  OE2 GLU D 795     -95.044  16.324 -39.607  1.00 71.25           O  
-ANISOU 8551  OE2 GLU D 795     8352  10904   7816    914    712    126       O  
-ATOM   8552  N   LYS D 796    -101.497  18.883 -38.722  1.00 57.91           N  
-ANISOU 8552  N   LYS D 796     6797   8862   6345    594    658    151       N  
-ATOM   8553  CA  LYS D 796    -102.479  19.967 -38.812  1.00 57.47           C  
-ANISOU 8553  CA  LYS D 796     6716   8799   6321    549    664    237       C  
-ATOM   8554  C   LYS D 796    -103.180  20.272 -37.489  1.00 56.45           C  
-ANISOU 8554  C   LYS D 796     6666   8466   6318    446    644    220       C  
-ATOM   8555  O   LYS D 796    -103.687  21.388 -37.301  1.00 54.62           O  
-ANISOU 8555  O   LYS D 796     6410   8198   6144    401    650    317       O  
-ATOM   8556  CB  LYS D 796    -103.528  19.642 -39.867  1.00 60.57           C  
-ANISOU 8556  CB  LYS D 796     7083   9322   6608    600    653    166       C  
-ATOM   8557  CG  LYS D 796    -103.042  19.748 -41.304  1.00 61.51           C  
-ANISOU 8557  CG  LYS D 796     7096   9682   6592    707    678    221       C  
-ATOM   8558  CD  LYS D 796    -104.087  19.172 -42.245  1.00 65.74           C  
-ANISOU 8558  CD  LYS D 796     7616  10342   7019    764    656    104       C  
-ATOM   8559  CE  LYS D 796    -103.650  19.195 -43.708  1.00 70.31           C  
-ANISOU 8559  CE  LYS D 796     8083  11188   7443    886    678    144       C  
-ATOM   8560  NZ  LYS D 796    -104.611  18.438 -44.563  1.00 70.49           N  
-ANISOU 8560  NZ  LYS D 796     8095  11330   7357    949    647    -10       N  
-ATOM   8561  N   LEU D 797    -103.235  19.278 -36.593  1.00 53.62           N  
-ANISOU 8561  N   LEU D 797     6395   7980   5999    416    618     97       N  
-ATOM   8562  CA  LEU D 797    -103.822  19.465 -35.265  1.00 53.24           C  
-ANISOU 8562  CA  LEU D 797     6418   7751   6059    327    600     78       C  
-ATOM   8563  C   LEU D 797    -102.957  20.337 -34.377  1.00 54.31           C  
-ANISOU 8563  C   LEU D 797     6544   7803   6290    285    611    182       C  
-ATOM   8564  O   LEU D 797    -103.461  20.881 -33.403  1.00 52.93           O  
-ANISOU 8564  O   LEU D 797     6401   7509   6201    218    598    195       O  
-ATOM   8565  CB  LEU D 797    -104.051  18.134 -34.560  1.00 52.03           C  
-ANISOU 8565  CB  LEU D 797     6353   7494   5922    312    573    -64       C  
-ATOM   8566  CG  LEU D 797    -104.968  17.159 -35.277  1.00 54.24           C  
-ANISOU 8566  CG  LEU D 797     6650   7824   6134    342    551   -191       C  
-ATOM   8567  CD1 LEU D 797    -104.953  15.818 -34.574  1.00 57.06           C  
-ANISOU 8567  CD1 LEU D 797     7087   8066   6528    329    526   -314       C  
-ATOM   8568  CD2 LEU D 797    -106.385  17.699 -35.387  1.00 54.67           C  
-ANISOU 8568  CD2 LEU D 797     6700   7877   6194    300    542   -191       C  
-ATOM   8569  N   LYS D 798    -101.666  20.470 -34.700  1.00 53.14           N  
-ANISOU 8569  N   LYS D 798     6345   7721   6125    325    633    250       N  
-ATOM   8570  CA  LYS D 798    -100.736  21.315 -33.918  1.00 51.93           C  
-ANISOU 8570  CA  LYS D 798     6168   7496   6067    286    641    347       C  
-ATOM   8571  C   LYS D 798    -100.772  20.882 -32.437  1.00 49.28           C  
-ANISOU 8571  C   LYS D 798     5917   6996   5810    232    616    270       C  
-ATOM   8572  O   LYS D 798    -100.828  21.691 -31.520  1.00 50.92           O  
-ANISOU 8572  O   LYS D 798     6129   7105   6114    175    606    312       O  
-ATOM   8573  CB  LYS D 798    -101.051  22.830 -34.077  1.00 50.31           C  
-ANISOU 8573  CB  LYS D 798     5897   7289   5927    250    651    482       C  
-ATOM   8574  N   THR D 799    -100.738  19.580 -32.232  1.00 47.21           N  
-ANISOU 8574  N   THR D 799     5718   6712   5507    255    605    157       N  
-ATOM   8575  CA  THR D 799    -100.872  18.984 -30.930  1.00 46.98           C  
-ANISOU 8575  CA  THR D 799     5768   6545   5535    214    584     85       C  
-ATOM   8576  C   THR D 799     -99.968  17.756 -30.852  1.00 48.17           C  
-ANISOU 8576  C   THR D 799     5952   6699   5650    263    583     17       C  
-ATOM   8577  O   THR D 799    -100.056  16.864 -31.691  1.00 50.75           O  
-ANISOU 8577  O   THR D 799     6285   7094   5904    317    581    -51       O  
-ATOM   8578  CB  THR D 799    -102.342  18.534 -30.675  1.00 48.00           C  
-ANISOU 8578  CB  THR D 799     5956   6615   5667    178    563      3       C  
-ATOM   8579  OG1 THR D 799    -103.216  19.665 -30.758  1.00 48.95           O  
-ANISOU 8579  OG1 THR D 799     6046   6736   5816    139    563     61       O  
-ATOM   8580  CG2 THR D 799    -102.504  17.904 -29.301  1.00 48.11           C  
-ANISOU 8580  CG2 THR D 799     6045   6496   5737    137    546    -56       C  
-ATOM   8581  N   ASP D 800     -99.100  17.713 -29.847  1.00 48.54           N  
-ANISOU 8581  N   ASP D 800     6018   6676   5750    251    581     31       N  
-ATOM   8582  CA  ASP D 800     -98.298  16.536 -29.610  1.00 48.25           C  
-ANISOU 8582  CA  ASP D 800     6019   6624   5688    296    578    -33       C  
-ATOM   8583  C   ASP D 800     -99.176  15.482 -28.937  1.00 49.28           C  
-ANISOU 8583  C   ASP D 800     6237   6650   5839    273    557   -130       C  
-ATOM   8584  O   ASP D 800     -99.780  15.750 -27.922  1.00 47.31           O  
-ANISOU 8584  O   ASP D 800     6020   6307   5647    215    547   -126       O  
-ATOM   8585  CB  ASP D 800     -97.092  16.875 -28.739  1.00 49.48           C  
-ANISOU 8585  CB  ASP D 800     6161   6748   5892    291    583     18       C  
-ATOM   8586  CG  ASP D 800     -96.173  15.680 -28.503  1.00 52.71           C  
-ANISOU 8586  CG  ASP D 800     6605   7148   6274    347    581    -40       C  
-ATOM   8587  OD1 ASP D 800     -96.398  14.935 -27.510  1.00 56.62           O  
-ANISOU 8587  OD1 ASP D 800     7171   7541   6803    331    566    -95       O  
-ATOM   8588  OD2 ASP D 800     -95.214  15.504 -29.277  1.00 48.42           O  
-ANISOU 8588  OD2 ASP D 800     6017   6705   5677    409    595    -25       O  
-ATOM   8589  N   ILE D 801     -99.251  14.292 -29.526  1.00 51.74           N  
-ANISOU 8589  N   ILE D 801     6577   6980   6104    322    548   -218       N  
-ATOM   8590  CA  ILE D 801    -100.036  13.197 -28.981  1.00 50.00           C  
-ANISOU 8590  CA  ILE D 801     6431   6654   5913    301    527   -306       C  
-ATOM   8591  C   ILE D 801     -99.149  11.971 -28.745  1.00 49.69           C  
-ANISOU 8591  C   ILE D 801     6429   6576   5874    356    519   -363       C  
-ATOM   8592  O   ILE D 801     -98.562  11.453 -29.673  1.00 49.58           O  
-ANISOU 8592  O   ILE D 801     6393   6641   5804    427    518   -405       O  
-ATOM   8593  CB  ILE D 801    -101.185  12.804 -29.931  1.00 50.07           C  
-ANISOU 8593  CB  ILE D 801     6440   6697   5887    304    513   -379       C  
-ATOM   8594  CG1 ILE D 801    -102.000  14.039 -30.322  1.00 49.52           C  
-ANISOU 8594  CG1 ILE D 801     6324   6684   5806    264    521   -318       C  
-ATOM   8595  CG2 ILE D 801    -102.079  11.752 -29.274  1.00 49.76           C  
-ANISOU 8595  CG2 ILE D 801     6472   6534   5902    266    490   -459       C  
-ATOM   8596  CD1 ILE D 801    -103.148  13.764 -31.282  1.00 50.96           C  
-ANISOU 8596  CD1 ILE D 801     6499   6919   5946    269    508   -387       C  
-ATOM   8597  N   LYS D 802     -99.095  11.504 -27.502  1.00 50.57           N  
-ANISOU 8597  N   LYS D 802     6595   6572   6046    327    514   -363       N  
-ATOM   8598  CA  LYS D 802     -98.346  10.310 -27.120  1.00 51.48           C  
-ANISOU 8598  CA  LYS D 802     6754   6632   6175    375    506   -408       C  
-ATOM   8599  C   LYS D 802     -99.269   9.307 -26.454  1.00 52.14           C  
-ANISOU 8599  C   LYS D 802     6904   6587   6319    339    487   -460       C  
-ATOM   8600  O   LYS D 802    -100.172   9.677 -25.704  1.00 50.34           O  
-ANISOU 8600  O   LYS D 802     6694   6302   6132    270    488   -430       O  
-ATOM   8601  CB  LYS D 802     -97.240  10.660 -26.123  1.00 51.83           C  
-ANISOU 8601  CB  LYS D 802     6793   6662   6239    381    518   -341       C  
-ATOM   8602  CG  LYS D 802     -96.040  11.366 -26.732  1.00 52.61           C  
-ANISOU 8602  CG  LYS D 802     6824   6877   6288    428    535   -292       C  
-ATOM   8603  CD  LYS D 802     -95.025  11.680 -25.641  1.00 54.90           C  
-ANISOU 8603  CD  LYS D 802     7109   7144   6607    427    542   -236       C  
-ATOM   8604  CE  LYS D 802     -93.703  12.237 -26.188  1.00 56.63           C  
-ANISOU 8604  CE  LYS D 802     7257   7474   6786    475    558   -188       C  
-ATOM   8605  NZ  LYS D 802     -93.790  13.662 -26.633  1.00 55.51           N  
-ANISOU 8605  NZ  LYS D 802     7043   7403   6647    435    571   -111       N  
-ATOM   8606  N   VAL D 803     -99.013   8.027 -26.693  1.00 51.42           N  
-ANISOU 8606  N   VAL D 803     6848   6449   6241    388    471   -535       N  
-ATOM   8607  CA  VAL D 803     -99.760   6.968 -26.052  1.00 49.87           C  
-ANISOU 8607  CA  VAL D 803     6711   6118   6119    357    454   -575       C  
-ATOM   8608  C   VAL D 803     -99.243   6.805 -24.640  1.00 48.76           C  
-ANISOU 8608  C   VAL D 803     6603   5900   6022    345    465   -506       C  
-ATOM   8609  O   VAL D 803     -98.044   6.768 -24.429  1.00 51.48           O  
-ANISOU 8609  O   VAL D 803     6941   6274   6346    399    473   -482       O  
-ATOM   8610  CB  VAL D 803     -99.586   5.639 -26.802  1.00 53.45           C  
-ANISOU 8610  CB  VAL D 803     7186   6537   6586    419    426   -683       C  
-ATOM   8611  CG1 VAL D 803    -100.315   4.513 -26.076  1.00 56.75           C  
-ANISOU 8611  CG1 VAL D 803     7662   6796   7104    381    408   -711       C  
-ATOM   8612  CG2 VAL D 803    -100.106   5.784 -28.214  1.00 54.44           C  
-ANISOU 8612  CG2 VAL D 803     7270   6757   6656    440    412   -762       C  
-ATOM   8613  N   VAL D 804    -100.148   6.712 -23.676  1.00 47.58           N  
-ANISOU 8613  N   VAL D 804     6484   5666   5929    279    466   -473       N  
-ATOM   8614  CA  VAL D 804     -99.772   6.391 -22.309  1.00 49.55           C  
-ANISOU 8614  CA  VAL D 804     6764   5846   6218    274    475   -409       C  
-ATOM   8615  C   VAL D 804     -99.768   4.858 -22.144  1.00 54.82           C  
-ANISOU 8615  C   VAL D 804     7481   6397   6952    301    460   -448       C  
-ATOM   8616  O   VAL D 804    -100.764   4.197 -22.443  1.00 51.47           O  
-ANISOU 8616  O   VAL D 804     7076   5901   6580    266    444   -495       O  
-ATOM   8617  CB  VAL D 804    -100.725   7.045 -21.297  1.00 47.22           C  
-ANISOU 8617  CB  VAL D 804     6468   5531   5944    198    485   -347       C  
-ATOM   8618  CG1 VAL D 804    -100.421   6.561 -19.886  1.00 45.16           C  
-ANISOU 8618  CG1 VAL D 804     6234   5209   5717    202    495   -283       C  
-ATOM   8619  CG2 VAL D 804    -100.624   8.563 -21.375  1.00 46.11           C  
-ANISOU 8619  CG2 VAL D 804     6277   5489   5753    179    495   -311       C  
-ATOM   8620  N   ASP D 805     -98.635   4.315 -21.690  1.00 56.65           N  
-ANISOU 8620  N   ASP D 805     7728   6608   7186    364    464   -428       N  
-ATOM   8621  CA  ASP D 805     -98.461   2.875 -21.562  1.00 64.85           C  
-ANISOU 8621  CA  ASP D 805     8811   7533   8295    402    448   -460       C  
-ATOM   8622  C   ASP D 805     -99.530   2.317 -20.621  1.00 67.46           C  
-ANISOU 8622  C   ASP D 805     9174   7748   8710    335    449   -412       C  
-ATOM   8623  O   ASP D 805     -99.711   2.830 -19.516  1.00 67.41           O  
-ANISOU 8623  O   ASP D 805     9163   7754   8697    299    470   -323       O  
-ATOM   8624  CB  ASP D 805     -97.048   2.537 -21.049  1.00 66.98           C  
-ANISOU 8624  CB  ASP D 805     9089   7812   8548    481    456   -427       C  
-ATOM   8625  N   ARG D 806    -100.242   1.283 -21.080  1.00 68.00           N  
-ANISOU 8625  N   ARG D 806     9267   7711   8859    319    425   -475       N  
-ATOM   8626  CA  ARG D 806    -101.329   0.645 -20.316  1.00 68.05           C  
-ANISOU 8626  CA  ARG D 806     9296   7599   8960    250    425   -429       C  
-ATOM   8627  C   ARG D 806    -100.916   0.172 -18.915  1.00 61.83           C  
-ANISOU 8627  C   ARG D 806     8531   6750   8211    262    446   -315       C  
-ATOM   8628  O   ARG D 806    -101.756   0.129 -18.024  1.00 60.84           O  
-ANISOU 8628  O   ARG D 806     8406   6584   8125    200    460   -236       O  
-ATOM   8629  CB  ARG D 806    -101.909  -0.540 -21.113  1.00 68.99           C  
-ANISOU 8629  CB  ARG D 806     9435   7601   9178    245    388   -527       C  
-ATOM   8630  N   ASP D 807     -99.632  -0.153 -18.744  1.00 60.66           N  
-ANISOU 8630  N   ASP D 807     8394   6611   8043    346    448   -305       N  
-ATOM   8631  CA  ASP D 807     -99.074  -0.659 -17.494  1.00 62.69           C  
-ANISOU 8631  CA  ASP D 807     8670   6823   8328    377    466   -201       C  
-ATOM   8632  C   ASP D 807     -98.504   0.428 -16.587  1.00 67.25           C  
-ANISOU 8632  C   ASP D 807     9218   7524   8809    387    495   -121       C  
-ATOM   8633  O   ASP D 807     -98.052   0.117 -15.490  1.00 72.93           O  
-ANISOU 8633  O   ASP D 807     9944   8231   9534    417    511    -32       O  
-ATOM   8634  CB  ASP D 807     -97.940  -1.694 -17.771  1.00 64.76           C  
-ANISOU 8634  CB  ASP D 807     8959   7023   8625    473    450   -238       C  
-ATOM   8635  N   SER D 808     -98.508   1.689 -17.018  1.00 67.08           N  
-ANISOU 8635  N   SER D 808     9161   7621   8706    366    499   -151       N  
-ATOM   8636  CA  SER D 808     -97.943   2.772 -16.210  1.00 62.28           C  
-ANISOU 8636  CA  SER D 808     8519   7125   8019    376    518    -92       C  
-ATOM   8637  C   SER D 808     -98.839   3.080 -15.031  1.00 60.98           C  
-ANISOU 8637  C   SER D 808     8345   6963   7862    319    534     -9       C  
-ATOM   8638  O   SER D 808    -100.016   2.689 -15.004  1.00 59.42           O  
-ANISOU 8638  O   SER D 808     8160   6698   7720    258    533      1       O  
-ATOM   8639  CB  SER D 808     -97.770   4.040 -17.047  1.00 61.27           C  
-ANISOU 8639  CB  SER D 808     8351   7108   7822    364    514   -144       C  
-ATOM   8640  OG  SER D 808     -99.016   4.541 -17.502  1.00 56.25           O  
-ANISOU 8640  OG  SER D 808     7706   6473   7195    289    510   -169       O  
-ATOM   8641  N   GLU D 809     -98.274   3.775 -14.051  1.00 61.29           N  
-ANISOU 8641  N   GLU D 809     8355   7087   7844    343    547     47       N  
-ATOM   8642  CA  GLU D 809     -99.046   4.234 -12.897  1.00 64.45           C  
-ANISOU 8642  CA  GLU D 809     8734   7524   8230    302    560    118       C  
-ATOM   8643  C   GLU D 809    -100.009   5.334 -13.334  1.00 61.50           C  
-ANISOU 8643  C   GLU D 809     8333   7199   7834    232    554     78       C  
-ATOM   8644  O   GLU D 809    -101.130   5.435 -12.841  1.00 61.38           O  
-ANISOU 8644  O   GLU D 809     8311   7179   7833    177    560    113       O  
-ATOM   8645  CB  GLU D 809     -98.110   4.751 -11.794  1.00 62.47           C  
-ANISOU 8645  CB  GLU D 809     8452   7368   7917    356    568    166       C  
-ATOM   8646  N   GLU D 810     -99.555   6.137 -14.281  1.00 58.47           N  
-ANISOU 8646  N   GLU D 810     7932   6867   7418    237    543     12       N  
-ATOM   8647  CA  GLU D 810    -100.369   7.177 -14.899  1.00 58.71           C  
-ANISOU 8647  CA  GLU D 810     7937   6940   7432    179    535    -27       C  
-ATOM   8648  C   GLU D 810    -101.689   6.583 -15.432  1.00 54.24           C  
-ANISOU 8648  C   GLU D 810     7394   6300   6915    120    532    -48       C  
-ATOM   8649  O   GLU D 810    -102.783   7.023 -15.069  1.00 46.12           O  
-ANISOU 8649  O   GLU D 810     6351   5284   5888     64    534    -30       O  
-ATOM   8650  CB  GLU D 810     -99.550   7.794 -16.027  1.00 62.37           C  
-ANISOU 8650  CB  GLU D 810     8380   7453   7865    206    527    -84       C  
-ATOM   8651  CG  GLU D 810    -100.014   9.125 -16.565  1.00 64.01           C  
-ANISOU 8651  CG  GLU D 810     8547   7726   8048    164    520   -107       C  
-ATOM   8652  CD  GLU D 810     -98.972   9.756 -17.484  1.00 64.57           C  
-ANISOU 8652  CD  GLU D 810     8587   7859   8089    199    517   -135       C  
-ATOM   8653  OE1 GLU D 810     -98.107   9.023 -18.036  1.00 73.19           O  
-ANISOU 8653  OE1 GLU D 810     9694   8941   9175    252    518   -156       O  
-ATOM   8654  OE2 GLU D 810     -99.012  10.986 -17.661  1.00 60.40           O  
-ANISOU 8654  OE2 GLU D 810     8014   7389   7545    176    513   -132       O  
-ATOM   8655  N   ALA D 811    -101.584   5.532 -16.230  1.00 51.35           N  
-ANISOU 8655  N   ALA D 811     7062   5856   6594    136    524    -89       N  
-ATOM   8656  CA  ALA D 811    -102.773   4.872 -16.772  1.00 53.65           C  
-ANISOU 8656  CA  ALA D 811     7371   6069   6943     82    514   -121       C  
-ATOM   8657  C   ALA D 811    -103.676   4.301 -15.666  1.00 52.50           C  
-ANISOU 8657  C   ALA D 811     7234   5866   6848     37    527    -43       C  
-ATOM   8658  O   ALA D 811    -104.900   4.343 -15.771  1.00 54.48           O  
-ANISOU 8658  O   ALA D 811     7476   6097   7125    -29    525    -47       O  
-ATOM   8659  CB  ALA D 811    -102.372   3.764 -17.747  1.00 54.93           C  
-ANISOU 8659  CB  ALA D 811     7564   6154   7154    119    497   -190       C  
-ATOM   8660  N   GLU D 812    -103.063   3.770 -14.618  1.00 52.33           N  
-ANISOU 8660  N   GLU D 812     7222   5824   6836     76    541     34       N  
-ATOM   8661  CA  GLU D 812    -103.796   3.155 -13.517  1.00 58.59           C  
-ANISOU 8661  CA  GLU D 812     8016   6572   7674     45    558    129       C  
-ATOM   8662  C   GLU D 812    -104.640   4.178 -12.766  1.00 53.26           C  
-ANISOU 8662  C   GLU D 812     7300   5992   6944      0    570    169       C  
-ATOM   8663  O   GLU D 812    -105.815   3.928 -12.458  1.00 49.51           O  
-ANISOU 8663  O   GLU D 812     6816   5490   6505    -60    577    207       O  
-ATOM   8664  CB  GLU D 812    -102.803   2.422 -12.606  1.00 65.59           C  
-ANISOU 8664  CB  GLU D 812     8916   7435   8569    113    571    206       C  
-ATOM   8665  CG  GLU D 812    -103.283   1.975 -11.237  1.00 74.95           C  
-ANISOU 8665  CG  GLU D 812    10089   8618   9772    103    596    332       C  
-ATOM   8666  CD  GLU D 812    -104.308   0.852 -11.266  1.00 80.92           C  
-ANISOU 8666  CD  GLU D 812    10861   9246  10639     45    598    376       C  
-ATOM   8667  OE1 GLU D 812    -104.666   0.354 -12.365  1.00 90.79           O  
-ANISOU 8667  OE1 GLU D 812    12135  10400  11962     13    576    294       O  
-ATOM   8668  OE2 GLU D 812    -104.766   0.477 -10.161  1.00 85.61           O  
-ANISOU 8668  OE2 GLU D 812    11436   9842  11249     33    623    494       O  
-ATOM   8669  N   ILE D 813    -104.036   5.334 -12.517  1.00 49.28           N  
-ANISOU 8669  N   ILE D 813     6768   5598   6359     31    569    155       N  
-ATOM   8670  CA  ILE D 813    -104.731   6.463 -11.907  1.00 46.68           C  
-ANISOU 8670  CA  ILE D 813     6396   5365   5976      0    571    169       C  
-ATOM   8671  C   ILE D 813    -105.931   6.839 -12.776  1.00 43.56           C  
-ANISOU 8671  C   ILE D 813     5996   4957   5598    -70    561    116       C  
-ATOM   8672  O   ILE D 813    -107.048   7.000 -12.278  1.00 42.37           O  
-ANISOU 8672  O   ILE D 813     5824   4827   5448   -118    568    148       O  
-ATOM   8673  CB  ILE D 813    -103.811   7.699 -11.790  1.00 48.37           C  
-ANISOU 8673  CB  ILE D 813     6579   5678   6121     42    561    135       C  
-ATOM   8674  CG1 ILE D 813    -102.582   7.464 -10.924  1.00 50.42           C  
-ANISOU 8674  CG1 ILE D 813     6835   5971   6353    116    568    177       C  
-ATOM   8675  CG2 ILE D 813    -104.550   8.898 -11.244  1.00 47.61           C  
-ANISOU 8675  CG2 ILE D 813     6438   5672   5982     14    556    132       C  
-ATOM   8676  CD1 ILE D 813    -102.912   7.172  -9.493  1.00 55.70           C  
-ANISOU 8676  CD1 ILE D 813     7483   6680   7001    130    585    265       C  
-ATOM   8677  N   ILE D 814    -105.707   6.942 -14.083  1.00 40.80           N  
-ANISOU 8677  N   ILE D 814     5661   4583   5259    -72    546     35       N  
-ATOM   8678  CA  ILE D 814    -106.759   7.359 -14.990  1.00 39.76           C  
-ANISOU 8678  CA  ILE D 814     5519   4454   5133   -128    534    -21       C  
-ATOM   8679  C   ILE D 814    -107.898   6.340 -15.041  1.00 41.29           C  
-ANISOU 8679  C   ILE D 814     5727   4564   5396   -185    536     -8       C  
-ATOM   8680  O   ILE D 814    -109.064   6.725 -15.038  1.00 41.53           O  
-ANISOU 8680  O   ILE D 814     5736   4619   5425   -242    535    -10       O  
-ATOM   8681  CB  ILE D 814    -106.191   7.689 -16.381  1.00 40.97           C  
-ANISOU 8681  CB  ILE D 814     5676   4619   5270   -106    519   -103       C  
-ATOM   8682  CG1 ILE D 814    -105.378   8.999 -16.282  1.00 43.12           C  
-ANISOU 8682  CG1 ILE D 814     5917   4986   5482    -72    518   -103       C  
-ATOM   8683  CG2 ILE D 814    -107.305   7.840 -17.405  1.00 41.89           C  
-ANISOU 8683  CG2 ILE D 814     5785   4732   5397   -157    506   -162       C  
-ATOM   8684  CD1 ILE D 814    -104.577   9.358 -17.513  1.00 42.73           C  
-ANISOU 8684  CD1 ILE D 814     5861   4964   5410    -39    509   -158       C  
-ATOM   8685  N   ARG D 815    -107.566   5.058 -15.054  1.00 42.76           N  
-ANISOU 8685  N   ARG D 815     5946   4650   5650   -171    536      6       N  
-ATOM   8686  CA  ARG D 815    -108.593   4.016 -15.045  1.00 46.57           C  
-ANISOU 8686  CA  ARG D 815     6437   5035   6221   -228    535     24       C  
-ATOM   8687  C   ARG D 815    -109.368   4.013 -13.735  1.00 42.60           C  
-ANISOU 8687  C   ARG D 815     5909   4558   5720   -265    559    133       C  
-ATOM   8688  O   ARG D 815    -110.576   3.762 -13.745  1.00 43.18           O  
-ANISOU 8688  O   ARG D 815     5966   4604   5836   -333    560    145       O  
-ATOM   8689  CB  ARG D 815    -108.005   2.619 -15.327  1.00 48.53           C  
-ANISOU 8689  CB  ARG D 815     6724   5155   6559   -200    525     15       C  
-ATOM   8690  CG  ARG D 815    -107.646   2.369 -16.787  1.00 49.39           C  
-ANISOU 8690  CG  ARG D 815     6852   5229   6684   -177    496   -110       C  
-ATOM   8691  CD  ARG D 815    -107.283   0.908 -17.022  1.00 53.77           C  
-ANISOU 8691  CD  ARG D 815     7442   5643   7347   -154    479   -128       C  
-ATOM   8692  NE  ARG D 815    -106.220   0.510 -16.105  1.00 54.02           N  
-ANISOU 8692  NE  ARG D 815     7491   5655   7378    -93    497    -45       N  
-ATOM   8693  CZ  ARG D 815    -104.926   0.422 -16.407  1.00 56.55           C  
-ANISOU 8693  CZ  ARG D 815     7830   5989   7667    -11    491    -79       C  
-ATOM   8694  NH1 ARG D 815    -104.065   0.070 -15.451  1.00 55.93           N  
-ANISOU 8694  NH1 ARG D 815     7764   5901   7586     41    509      8       N  
-ATOM   8695  NH2 ARG D 815    -104.475   0.673 -17.638  1.00 55.53           N  
-ANISOU 8695  NH2 ARG D 815     7703   5894   7502     23    469   -193       N  
-ATOM   8696  N   LYS D 816    -108.699   4.318 -12.625  1.00 40.88           N  
-ANISOU 8696  N   LYS D 816     5680   4404   5449   -217    578    208       N  
-ATOM   8697  CA  LYS D 816    -109.410   4.414 -11.336  1.00 41.56           C  
-ANISOU 8697  CA  LYS D 816     5730   4546   5515   -239    601    312       C  
-ATOM   8698  C   LYS D 816    -110.394   5.572 -11.384  1.00 42.61           C  
-ANISOU 8698  C   LYS D 816     5825   4777   5589   -281    597    278       C  
-ATOM   8699  O   LYS D 816    -111.523   5.459 -10.919  1.00 45.98           O  
-ANISOU 8699  O   LYS D 816     6223   5219   6028   -333    608    328       O  
-ATOM   8700  CB  LYS D 816    -108.471   4.501 -10.130  1.00 43.33           C  
-ANISOU 8700  CB  LYS D 816     5943   4836   5684   -168    619    392       C  
-ATOM   8701  N   TYR D 817    -109.977   6.696 -11.960  1.00 41.29           N  
-ANISOU 8701  N   TYR D 817     5653   4675   5362   -258    580    198       N  
-ATOM   8702  CA  TYR D 817    -110.831   7.877 -12.007  1.00 38.94           C  
-ANISOU 8702  CA  TYR D 817     5318   4466   5012   -289    572    165       C  
-ATOM   8703  C   TYR D 817    -112.080   7.523 -12.778  1.00 38.08           C  
-ANISOU 8703  C   TYR D 817     5208   4309   4951   -362    566    133       C  
-ATOM   8704  O   TYR D 817    -113.180   7.855 -12.364  1.00 34.88           O  
-ANISOU 8704  O   TYR D 817     4769   3954   4530   -404    572    157       O  
-ATOM   8705  CB  TYR D 817    -110.071   9.024 -12.692  1.00 39.16           C  
-ANISOU 8705  CB  TYR D 817     5343   4544   4992   -253    553     87       C  
-ATOM   8706  CG  TYR D 817    -110.596  10.422 -12.527  1.00 36.36           C  
-ANISOU 8706  CG  TYR D 817     4946   4285   4582   -261    542     59       C  
-ATOM   8707  CD1 TYR D 817    -111.722  10.722 -11.756  1.00 34.20           C  
-ANISOU 8707  CD1 TYR D 817     4637   4069   4286   -292    548     92       C  
-ATOM   8708  CD2 TYR D 817    -109.933  11.486 -13.174  1.00 34.23           C  
-ANISOU 8708  CD2 TYR D 817     4669   4050   4287   -234    524      1       C  
-ATOM   8709  CE1 TYR D 817    -112.158  12.044 -11.627  1.00 33.63           C  
-ANISOU 8709  CE1 TYR D 817     4527   4083   4168   -290    532     56       C  
-ATOM   8710  CE2 TYR D 817    -110.359  12.790 -13.050  1.00 31.37           C  
-ANISOU 8710  CE2 TYR D 817     4267   3761   3890   -238    510    -26       C  
-ATOM   8711  CZ  TYR D 817    -111.444  13.083 -12.288  1.00 31.05           C  
-ANISOU 8711  CZ  TYR D 817     4197   3772   3829   -262    511     -5       C  
-ATOM   8712  OH  TYR D 817    -111.808  14.398 -12.210  1.00 27.13           O  
-ANISOU 8712  OH  TYR D 817     3661   3341   3304   -258    492    -42       O  
-ATOM   8713  N   VAL D 818    -111.905   6.839 -13.905  1.00 40.48           N  
-ANISOU 8713  N   VAL D 818     5545   4522   5312   -373    552     73       N  
-ATOM   8714  CA  VAL D 818    -113.040   6.429 -14.723  1.00 41.64           C  
-ANISOU 8714  CA  VAL D 818     5688   4621   5510   -439    541     28       C  
-ATOM   8715  C   VAL D 818    -113.964   5.487 -13.937  1.00 44.23           C  
-ANISOU 8715  C   VAL D 818     6002   4897   5905   -494    557    111       C  
-ATOM   8716  O   VAL D 818    -115.175   5.673 -13.926  1.00 45.52           O  
-ANISOU 8716  O   VAL D 818     6134   5089   6073   -553    558    114       O  
-ATOM   8717  CB  VAL D 818    -112.604   5.724 -16.027  1.00 42.27           C  
-ANISOU 8717  CB  VAL D 818     5802   4615   5642   -429    519    -61       C  
-ATOM   8718  CG1 VAL D 818    -113.816   5.107 -16.741  1.00 43.67           C  
-ANISOU 8718  CG1 VAL D 818     5969   4734   5887   -499    503   -109       C  
-ATOM   8719  CG2 VAL D 818    -111.897   6.697 -16.969  1.00 41.35           C  
-ANISOU 8719  CG2 VAL D 818     5687   4567   5458   -383    505   -138       C  
-ATOM   8720  N   LYS D 819    -113.389   4.493 -13.276  1.00 44.91           N  
-ANISOU 8720  N   LYS D 819     6108   4912   6045   -474    571    186       N  
-ATOM   8721  CA  LYS D 819    -114.172   3.484 -12.568  1.00 47.86           C  
-ANISOU 8721  CA  LYS D 819     6464   5221   6499   -526    589    282       C  
-ATOM   8722  C   LYS D 819    -114.919   4.037 -11.365  1.00 49.72           C  
-ANISOU 8722  C   LYS D 819     6649   5570   6674   -542    615    379       C  
-ATOM   8723  O   LYS D 819    -116.088   3.750 -11.167  1.00 49.08           O  
-ANISOU 8723  O   LYS D 819     6533   5485   6630   -609    624    420       O  
-ATOM   8724  CB  LYS D 819    -113.246   2.367 -12.105  1.00 53.45           C  
-ANISOU 8724  CB  LYS D 819     7203   5831   7275   -486    598    351       C  
-ATOM   8725  CG  LYS D 819    -113.929   1.107 -11.602  1.00 58.34           C  
-ANISOU 8725  CG  LYS D 819     7810   6343   8015   -541    612    451       C  
-ATOM   8726  CD  LYS D 819    -112.994   0.370 -10.656  1.00 59.68           C  
-ANISOU 8726  CD  LYS D 819     7995   6474   8209   -484    635    566       C  
-ATOM   8727  CE  LYS D 819    -113.392  -1.085 -10.439  1.00 62.83           C  
-ANISOU 8727  CE  LYS D 819     8393   6717   8763   -530    641    654       C  
-ATOM   8728  NZ  LYS D 819    -114.246  -1.244  -9.243  1.00 62.44           N  
-ANISOU 8728  NZ  LYS D 819     8287   6720   8716   -570    679    813       N  
-ATOM   8729  N   ASN D 820    -114.237   4.822 -10.544  1.00 48.77           N  
-ANISOU 8729  N   ASN D 820     6517   5557   6458   -478    627    411       N  
-ATOM   8730  CA  ASN D 820    -114.843   5.314  -9.321  1.00 48.88           C  
-ANISOU 8730  CA  ASN D 820     6476   5692   6403   -477    649    498       C  
-ATOM   8731  C   ASN D 820    -115.861   6.418  -9.475  1.00 48.21           C  
-ANISOU 8731  C   ASN D 820     6351   5710   6255   -508    640    445       C  
-ATOM   8732  O   ASN D 820    -116.684   6.593  -8.573  1.00 46.85           O  
-ANISOU 8732  O   ASN D 820     6128   5627   6046   -523    658    517       O  
-ATOM   8733  CB  ASN D 820    -113.771   5.825  -8.384  1.00 52.41           C  
-ANISOU 8733  CB  ASN D 820     6916   6230   6766   -390    658    533       C  
-ATOM   8734  CG  ASN D 820    -112.976   4.719  -7.773  1.00 50.63           C  
-ANISOU 8734  CG  ASN D 820     6711   5941   6587   -353    678    629       C  
-ATOM   8735  OD1 ASN D 820    -113.322   3.548  -7.893  1.00 58.84           O  
-ANISOU 8735  OD1 ASN D 820     7762   6866   7727   -396    688    689       O  
-ATOM   8736  ND2 ASN D 820    -111.892   5.076  -7.136  1.00 51.99           N  
-ANISOU 8736  ND2 ASN D 820     6882   6180   6691   -273    681    643       N  
-ATOM   8737  N   THR D 821    -115.797   7.198 -10.560  1.00 45.48           N  
-ANISOU 8737  N   THR D 821     6024   5364   5890   -510    612    327       N  
-ATOM   8738  CA  THR D 821    -116.652   8.378 -10.649  1.00 41.98           C  
-ANISOU 8738  CA  THR D 821     5543   5025   5382   -525    601    279       C  
-ATOM   8739  C   THR D 821    -117.749   8.215 -11.682  1.00 45.14           C  
-ANISOU 8739  C   THR D 821     5940   5383   5829   -598    589    222       C  
-ATOM   8740  O   THR D 821    -118.358   9.194 -12.135  1.00 42.85           O  
-ANISOU 8740  O   THR D 821     5629   5159   5492   -608    573    159       O  
-ATOM   8741  CB  THR D 821    -115.832   9.659 -10.915  1.00 41.80           C  
-ANISOU 8741  CB  THR D 821     5526   5064   5290   -466    580    202       C  
-ATOM   8742  OG1 THR D 821    -115.315   9.657 -12.257  1.00 36.87           O  
-ANISOU 8742  OG1 THR D 821     4942   4368   4699   -467    561    119       O  
-ATOM   8743  CG2 THR D 821    -114.700   9.774  -9.905  1.00 42.07           C  
-ANISOU 8743  CG2 THR D 821     5559   5141   5284   -394    589    248       C  
-ATOM   8744  N   HIS D 822    -118.035   6.974 -12.053  1.00 49.02           N  
-ANISOU 8744  N   HIS D 822     6447   5761   6416   -648    592    242       N  
-ATOM   8745  CA  HIS D 822    -119.214   6.712 -12.852  1.00 51.53           C  
-ANISOU 8745  CA  HIS D 822     6749   6047   6783   -722    580    195       C  
-ATOM   8746  C   HIS D 822    -120.407   6.870 -11.940  1.00 50.98           C  
-ANISOU 8746  C   HIS D 822     6620   6062   6690   -764    600    273       C  
-ATOM   8747  O   HIS D 822    -120.484   6.191 -10.936  1.00 57.43           O  
-ANISOU 8747  O   HIS D 822     7416   6873   7532   -773    626    386       O  
-ATOM   8748  CB  HIS D 822    -119.191   5.314 -13.442  1.00 52.40           C  
-ANISOU 8748  CB  HIS D 822     6886   6007   7017   -764    572    188       C  
-ATOM   8749  CG  HIS D 822    -120.221   5.124 -14.500  1.00 53.90           C  
-ANISOU 8749  CG  HIS D 822     7061   6163   7256   -830    548    103       C  
-ATOM   8750  ND1 HIS D 822    -119.904   4.769 -15.790  1.00 54.24           N  
-ANISOU 8750  ND1 HIS D 822     7136   6130   7343   -827    517    -10       N  
-ATOM   8751  CD2 HIS D 822    -121.559   5.313 -14.479  1.00 54.26           C  
-ANISOU 8751  CD2 HIS D 822     7057   6258   7301   -894    549    107       C  
-ATOM   8752  CE1 HIS D 822    -121.008   4.706 -16.509  1.00 51.96           C  
-ANISOU 8752  CE1 HIS D 822     6818   5842   7084   -887    499    -74       C  
-ATOM   8753  NE2 HIS D 822    -122.025   5.040 -15.738  1.00 53.99           N  
-ANISOU 8753  NE2 HIS D 822     7026   6172   7315   -931    518     -3       N  
-ATOM   8754  N   ALA D 823    -121.334   7.768 -12.270  1.00 48.94           N  
-ANISOU 8754  N   ALA D 823     6328   5889   6378   -786    588    219       N  
-ATOM   8755  CA  ALA D 823    -122.444   8.050 -11.364  1.00 50.79           C  
-ANISOU 8755  CA  ALA D 823     6499   6228   6572   -814    607    288       C  
-ATOM   8756  C   ALA D 823    -123.456   6.901 -11.349  1.00 52.39           C  
-ANISOU 8756  C   ALA D 823     6671   6364   6871   -902    619    347       C  
-ATOM   8757  O   ALA D 823    -123.705   6.277 -12.366  1.00 50.66           O  
-ANISOU 8757  O   ALA D 823     6470   6042   6735   -952    600    284       O  
-ATOM   8758  CB  ALA D 823    -123.140   9.339 -11.753  1.00 47.91           C  
-ANISOU 8758  CB  ALA D 823     6107   5970   6128   -806    588    210       C  
-ATOM   8759  N   THR D 824    -124.050   6.681 -10.188  1.00 53.79           N  
-ANISOU 8759  N   THR D 824     6794   6612   7032   -919    650    465       N  
-ATOM   8760  CA  THR D 824    -125.038   5.637  -9.952  1.00 57.62           C  
-ANISOU 8760  CA  THR D 824     7235   7049   7609  -1005    668    551       C  
-ATOM   8761  C   THR D 824    -126.265   5.787 -10.885  1.00 57.45           C  
-ANISOU 8761  C   THR D 824     7185   7029   7616  -1078    646    467       C  
-ATOM   8762  O   THR D 824    -126.821   4.787 -11.354  1.00 61.58           O  
-ANISOU 8762  O   THR D 824     7697   7444   8258  -1158    640    472       O  
-ATOM   8763  CB  THR D 824    -125.396   5.633  -8.419  1.00 58.13           C  
-ANISOU 8763  CB  THR D 824     7234   7237   7616   -989    709    704       C  
-ATOM   8764  OG1 THR D 824    -125.578   4.303  -7.941  1.00 63.61           O  
-ANISOU 8764  OG1 THR D 824     7906   7840   8422  -1043    736    837       O  
-ATOM   8765  CG2 THR D 824    -126.629   6.494  -8.119  1.00 58.50           C  
-ANISOU 8765  CG2 THR D 824     7210   7442   7575  -1005    713    698       C  
-ATOM   8766  N   THR D 825    -126.669   7.023 -11.181  1.00 53.67           N  
-ANISOU 8766  N   THR D 825     6692   6668   7034  -1050    630    385       N  
-ATOM   8767  CA  THR D 825    -127.852   7.266 -12.015  1.00 53.25           C  
-ANISOU 8767  CA  THR D 825     6605   6639   6989  -1110    610    308       C  
-ATOM   8768  C   THR D 825    -127.601   7.243 -13.521  1.00 53.84           C  
-ANISOU 8768  C   THR D 825     6727   6625   7105  -1117    572    168       C  
-ATOM   8769  O   THR D 825    -128.521   7.456 -14.298  1.00 50.19           O  
-ANISOU 8769  O   THR D 825     6238   6188   6645  -1158    552     94       O  
-ATOM   8770  CB  THR D 825    -128.492   8.638 -11.702  1.00 53.56           C  
-ANISOU 8770  CB  THR D 825     6602   6847   6899  -1072    608    280       C  
-ATOM   8771  OG1 THR D 825    -127.566   9.696 -12.017  1.00 48.55           O  
-ANISOU 8771  OG1 THR D 825     6014   6242   6190   -988    589    202       O  
-ATOM   8772  CG2 THR D 825    -128.930   8.715 -10.229  1.00 53.50           C  
-ANISOU 8772  CG2 THR D 825     6532   6962   6835  -1060    643    407       C  
-ATOM   8773  N   HIS D 826    -126.356   7.074 -13.938  1.00 58.19           N  
-ANISOU 8773  N   HIS D 826     7343   7093   7674  -1068    561    130       N  
-ATOM   8774  CA  HIS D 826    -126.042   7.006 -15.360  1.00 59.72           C  
-ANISOU 8774  CA  HIS D 826     7576   7217   7898  -1064    527      1       C  
-ATOM   8775  C   HIS D 826    -125.821   5.542 -15.688  1.00 59.94           C  
-ANISOU 8775  C   HIS D 826     7623   7086   8064  -1111    518      3       C  
-ATOM   8776  O   HIS D 826    -124.727   5.114 -16.066  1.00 62.22           O  
-ANISOU 8776  O   HIS D 826     7966   7287   8388  -1071    508    -29       O  
-ATOM   8777  CB  HIS D 826    -124.826   7.864 -15.692  1.00 57.65           C  
-ANISOU 8777  CB  HIS D 826     7364   6979   7561   -975    518    -49       C  
-ATOM   8778  CG  HIS D 826    -125.049   9.322 -15.448  1.00 58.27           C  
-ANISOU 8778  CG  HIS D 826     7421   7195   7524   -931    518    -60       C  
-ATOM   8779  ND1 HIS D 826    -124.051  10.170 -15.017  1.00 57.66           N  
-ANISOU 8779  ND1 HIS D 826     7367   7162   7380   -855    522    -49       N  
-ATOM   8780  CD2 HIS D 826    -126.168  10.080 -15.544  1.00 59.77           C  
-ANISOU 8780  CD2 HIS D 826     7563   7484   7662   -950    512    -84       C  
-ATOM   8781  CE1 HIS D 826    -124.541  11.390 -14.877  1.00 55.19           C  
-ANISOU 8781  CE1 HIS D 826     7023   6959   6988   -830    516    -69       C  
-ATOM   8782  NE2 HIS D 826    -125.824  11.365 -15.192  1.00 57.49           N  
-ANISOU 8782  NE2 HIS D 826     7273   7289   7283   -884    511    -89       N  
-ATOM   8783  N   ASN D 827    -126.900   4.786 -15.558  1.00 60.65           N  
-ANISOU 8783  N   ASN D 827     7666   7140   8240  -1197    520     36       N  
-ATOM   8784  CA  ASN D 827    -126.836   3.323 -15.586  1.00 64.53           C  
-ANISOU 8784  CA  ASN D 827     8161   7470   8887  -1253    515     66       C  
-ATOM   8785  C   ASN D 827    -127.080   2.730 -16.971  1.00 62.90           C  
-ANISOU 8785  C   ASN D 827     7962   7168   8768  -1288    468    -79       C  
-ATOM   8786  O   ASN D 827    -127.014   1.521 -17.141  1.00 66.34           O  
-ANISOU 8786  O   ASN D 827     8403   7456   9349  -1332    453    -81       O  
-ATOM   8787  CB  ASN D 827    -127.777   2.728 -14.519  1.00 68.07           C  
-ANISOU 8787  CB  ASN D 827     8544   7920   9399  -1329    547    209       C  
-ATOM   8788  CG  ASN D 827    -129.196   3.295 -14.588  1.00 70.90           C  
-ANISOU 8788  CG  ASN D 827     8832   8395   9711  -1384    546    193       C  
-ATOM   8789  OD1 ASN D 827    -129.564   4.021 -15.517  1.00 71.35           O  
-ANISOU 8789  OD1 ASN D 827     8889   8515   9706  -1374    519     70       O  
-ATOM   8790  ND2 ASN D 827    -129.995   2.954 -13.598  1.00 73.24           N  
-ANISOU 8790  ND2 ASN D 827     9064   8728  10036  -1440    579    326       N  
-ATOM   8791  N   ALA D 828    -127.298   3.582 -17.971  1.00 62.71           N  
-ANISOU 8791  N   ALA D 828     7939   7229   8659  -1261    443   -202       N  
-ATOM   8792  CA  ALA D 828    -127.471   3.139 -19.358  1.00 64.64           C  
-ANISOU 8792  CA  ALA D 828     8185   7414   8959  -1276    395   -355       C  
-ATOM   8793  C   ALA D 828    -126.247   2.440 -19.975  1.00 67.13           C  
-ANISOU 8793  C   ALA D 828     8560   7612   9333  -1224    371   -423       C  
-ATOM   8794  O   ALA D 828    -126.384   1.754 -20.985  1.00 74.11           O  
-ANISOU 8794  O   ALA D 828     9441   8422  10296  -1241    329   -545       O  
-ATOM   8795  CB  ALA D 828    -127.898   4.318 -20.230  1.00 62.58           C  
-ANISOU 8795  CB  ALA D 828     7910   7296   8573  -1242    379   -454       C  
-ATOM   8796  N   TYR D 829    -125.060   2.615 -19.391  1.00 66.00           N  
-ANISOU 8796  N   TYR D 829     8468   7459   9150  -1157    396   -355       N  
-ATOM   8797  CA  TYR D 829    -123.829   2.042 -19.952  1.00 63.26           C  
-ANISOU 8797  CA  TYR D 829     8176   7017   8842  -1097    375   -417       C  
-ATOM   8798  C   TYR D 829    -122.749   1.861 -18.886  1.00 59.71           C  
-ANISOU 8798  C   TYR D 829     7768   6527   8394  -1053    409   -296       C  
-ATOM   8799  O   TYR D 829    -122.835   2.442 -17.821  1.00 58.48           O  
-ANISOU 8799  O   TYR D 829     7599   6447   8173  -1050    447   -180       O  
-ATOM   8800  CB  TYR D 829    -123.315   2.929 -21.112  1.00 65.18           C  
-ANISOU 8800  CB  TYR D 829     8439   7356   8971  -1022    354   -539       C  
-ATOM   8801  CG  TYR D 829    -123.048   4.382 -20.713  1.00 64.99           C  
-ANISOU 8801  CG  TYR D 829     8418   7477   8797   -971    383   -485       C  
-ATOM   8802  CD1 TYR D 829    -121.868   4.739 -20.094  1.00 64.39           C  
-ANISOU 8802  CD1 TYR D 829     8383   7410   8673   -906    407   -417       C  
-ATOM   8803  CD2 TYR D 829    -123.991   5.393 -20.953  1.00 64.39           C  
-ANISOU 8803  CD2 TYR D 829     8301   7527   8637   -986    384   -505       C  
-ATOM   8804  CE1 TYR D 829    -121.622   6.053 -19.722  1.00 64.29           C  
-ANISOU 8804  CE1 TYR D 829     8368   7518   8543   -862    428   -377       C  
-ATOM   8805  CE2 TYR D 829    -123.750   6.704 -20.576  1.00 63.31           C  
-ANISOU 8805  CE2 TYR D 829     8166   7506   8383   -939    405   -460       C  
-ATOM   8806  CZ  TYR D 829    -122.550   7.028 -19.961  1.00 62.09           C  
-ANISOU 8806  CZ  TYR D 829     8050   7349   8192   -878    425   -398       C  
-ATOM   8807  OH  TYR D 829    -122.255   8.313 -19.569  1.00 55.94           O  
-ANISOU 8807  OH  TYR D 829     7269   6672   7313   -831    441   -362       O  
-ATOM   8808  N   ASP D 830    -121.747   1.042 -19.178  1.00 59.52           N  
-ANISOU 8808  N   ASP D 830     7788   6389   8439  -1013    393   -329       N  
-ATOM   8809  CA  ASP D 830    -120.478   1.054 -18.432  1.00 60.33           C  
-ANISOU 8809  CA  ASP D 830     7936   6476   8512   -944    419   -244       C  
-ATOM   8810  C   ASP D 830    -119.391   1.482 -19.422  1.00 54.52           C  
-ANISOU 8810  C   ASP D 830     7240   5774   7702   -856    398   -355       C  
-ATOM   8811  O   ASP D 830    -119.584   1.489 -20.642  1.00 52.54           O  
-ANISOU 8811  O   ASP D 830     6982   5533   7447   -850    362   -489       O  
-ATOM   8812  CB  ASP D 830    -120.135  -0.252 -17.645  1.00 68.27           C  
-ANISOU 8812  CB  ASP D 830     8956   7328   9657   -963    429   -146       C  
-ATOM   8813  CG  ASP D 830    -120.355  -1.515 -18.440  1.00 74.99           C  
-ANISOU 8813  CG  ASP D 830     9808   8017  10669  -1002    385   -237       C  
-ATOM   8814  OD1 ASP D 830    -119.419  -1.899 -19.172  1.00 79.51           O  
-ANISOU 8814  OD1 ASP D 830    10421   8529  11262   -939    357   -333       O  
-ATOM   8815  OD2 ASP D 830    -121.434  -2.146 -18.296  1.00 81.29           O  
-ANISOU 8815  OD2 ASP D 830    10561   8745  11579  -1092    378   -212       O  
-ATOM   8816  N   LEU D 831    -118.275   1.936 -18.891  1.00 51.70           N  
-ANISOU 8816  N   LEU D 831     6914   5455   7273   -787    421   -297       N  
-ATOM   8817  CA  LEU D 831    -117.227   2.489 -19.725  1.00 53.09           C  
-ANISOU 8817  CA  LEU D 831     7119   5684   7368   -705    408   -380       C  
-ATOM   8818  C   LEU D 831    -116.019   1.595 -19.656  1.00 50.89           C  
-ANISOU 8818  C   LEU D 831     6884   5303   7148   -650    403   -377       C  
-ATOM   8819  O   LEU D 831    -115.656   1.111 -18.586  1.00 48.87           O  
-ANISOU 8819  O   LEU D 831     6643   4990   6936   -649    427   -267       O  
-ATOM   8820  CB  LEU D 831    -116.802   3.905 -19.276  1.00 52.63           C  
-ANISOU 8820  CB  LEU D 831     7058   5766   7174   -661    435   -329       C  
-ATOM   8821  CG  LEU D 831    -117.526   5.197 -19.618  1.00 50.15           C  
-ANISOU 8821  CG  LEU D 831     6709   5582   6763   -672    436   -356       C  
-ATOM   8822  CD1 LEU D 831    -117.917   5.284 -21.082  1.00 47.92           C  
-ANISOU 8822  CD1 LEU D 831     6414   5327   6468   -671    404   -484       C  
-ATOM   8823  CD2 LEU D 831    -118.698   5.292 -18.700  1.00 52.97           C  
-ANISOU 8823  CD2 LEU D 831     7030   5962   7133   -740    454   -278       C  
-ATOM   8824  N   GLU D 832    -115.355   1.466 -20.789  1.00 48.84           N  
-ANISOU 8824  N   GLU D 832     6643   5041   6875   -594    374   -494       N  
-ATOM   8825  CA  GLU D 832    -114.110   0.743 -20.864  1.00 52.42           C  
-ANISOU 8825  CA  GLU D 832     7135   5416   7364   -526    366   -508       C  
-ATOM   8826  C   GLU D 832    -113.094   1.626 -21.579  1.00 51.29           C  
-ANISOU 8826  C   GLU D 832     7001   5387   7099   -443    366   -564       C  
-ATOM   8827  O   GLU D 832    -113.351   2.137 -22.684  1.00 50.49           O  
-ANISOU 8827  O   GLU D 832     6879   5366   6939   -430    346   -662       O  
-ATOM   8828  CB  GLU D 832    -114.307  -0.583 -21.607  1.00 52.46           C  
-ANISOU 8828  CB  GLU D 832     7147   5283   7503   -539    322   -611       C  
-ATOM   8829  N   VAL D 833    -111.947   1.819 -20.943  1.00 51.62           N  
-ANISOU 8829  N   VAL D 833     7068   5443   7101   -385    389   -494       N  
-ATOM   8830  CA  VAL D 833    -110.906   2.651 -21.521  1.00 50.78           C  
-ANISOU 8830  CA  VAL D 833     6965   5441   6888   -309    392   -528       C  
-ATOM   8831  C   VAL D 833    -110.196   1.831 -22.582  1.00 50.99           C  
-ANISOU 8831  C   VAL D 833     7007   5422   6944   -248    359   -640       C  
-ATOM   8832  O   VAL D 833    -109.681   0.778 -22.291  1.00 53.71           O  
-ANISOU 8832  O   VAL D 833     7380   5655   7371   -225    350   -636       O  
-ATOM   8833  CB  VAL D 833    -109.921   3.145 -20.441  1.00 48.18           C  
-ANISOU 8833  CB  VAL D 833     6649   5146   6510   -270    424   -421       C  
-ATOM   8834  CG1 VAL D 833    -108.778   3.939 -21.059  1.00 45.69           C  
-ANISOU 8834  CG1 VAL D 833     6331   4930   6100   -196    426   -453       C  
-ATOM   8835  CG2 VAL D 833    -110.664   4.001 -19.408  1.00 46.87           C  
-ANISOU 8835  CG2 VAL D 833     6460   5040   6308   -322    451   -326       C  
-ATOM   8836  N   ILE D 834    -110.150   2.333 -23.804  1.00 52.12           N  
-ANISOU 8836  N   ILE D 834     7127   5660   7016   -215    341   -737       N  
-ATOM   8837  CA  ILE D 834    -109.447   1.642 -24.869  1.00 55.91           C  
-ANISOU 8837  CA  ILE D 834     7613   6127   7503   -143    309   -853       C  
-ATOM   8838  C   ILE D 834    -108.022   2.163 -24.958  1.00 56.93           C  
-ANISOU 8838  C   ILE D 834     7749   6338   7544    -57    327   -827       C  
-ATOM   8839  O   ILE D 834    -107.083   1.388 -24.851  1.00 59.88           O  
-ANISOU 8839  O   ILE D 834     8148   6648   7953     -1    319   -839       O  
-ATOM   8840  CB  ILE D 834    -110.164   1.814 -26.222  1.00 57.49           C  
-ANISOU 8840  CB  ILE D 834     7775   6403   7666   -142    278   -980       C  
-ATOM   8841  CG1 ILE D 834    -111.524   1.147 -26.171  1.00 58.33           C  
-ANISOU 8841  CG1 ILE D 834     7870   6417   7874   -225    253  -1021       C  
-ATOM   8842  CG2 ILE D 834    -109.356   1.191 -27.352  1.00 60.74           C  
-ANISOU 8842  CG2 ILE D 834     8182   6832   8063    -51    243  -1107       C  
-ATOM   8843  CD1 ILE D 834    -112.383   1.531 -27.344  1.00 61.24           C  
-ANISOU 8843  CD1 ILE D 834     8193   6883   8191   -233    227  -1129       C  
-ATOM   8844  N   ASP D 835    -107.874   3.471 -25.177  1.00 56.63           N  
-ANISOU 8844  N   ASP D 835     7682   6437   7398    -48    349   -790       N  
-ATOM   8845  CA  ASP D 835    -106.557   4.130 -25.270  1.00 52.98           C  
-ANISOU 8845  CA  ASP D 835     7214   6065   6853     23    368   -754       C  
-ATOM   8846  C   ASP D 835    -106.526   5.413 -24.442  1.00 51.72           C  
-ANISOU 8846  C   ASP D 835     7040   5971   6642     -8    402   -642       C  
-ATOM   8847  O   ASP D 835    -107.554   6.089 -24.287  1.00 48.98           O  
-ANISOU 8847  O   ASP D 835     6674   5652   6285    -68    408   -618       O  
-ATOM   8848  CB  ASP D 835    -106.238   4.531 -26.705  1.00 53.90           C  
-ANISOU 8848  CB  ASP D 835     7291   6304   6884     84    355   -837       C  
-ATOM   8849  CG  ASP D 835    -106.048   3.344 -27.637  1.00 57.87           C  
-ANISOU 8849  CG  ASP D 835     7799   6770   7419    139    317   -968       C  
-ATOM   8850  OD1 ASP D 835    -106.632   3.391 -28.745  1.00 54.98           O  
-ANISOU 8850  OD1 ASP D 835     7399   6474   7018    150    293  -1062       O  
-ATOM   8851  OD2 ASP D 835    -105.311   2.390 -27.269  1.00 58.97           O  
-ANISOU 8851  OD2 ASP D 835     7973   6816   7617    178    307   -980       O  
-ATOM   8852  N   ILE D 836    -105.346   5.707 -23.898  1.00 49.69           N  
-ANISOU 8852  N   ILE D 836     6789   5735   6356     37    421   -582       N  
-ATOM   8853  CA  ILE D 836    -105.103   6.905 -23.148  1.00 47.21           C  
-ANISOU 8853  CA  ILE D 836     6456   5483   5998     21    446   -492       C  
-ATOM   8854  C   ILE D 836    -103.989   7.634 -23.848  1.00 46.57           C  
-ANISOU 8854  C   ILE D 836     6344   5505   5846     83    453   -492       C  
-ATOM   8855  O   ILE D 836    -102.906   7.107 -24.010  1.00 45.59           O  
-ANISOU 8855  O   ILE D 836     6229   5378   5715    145    452   -508       O  
-ATOM   8856  CB  ILE D 836    -104.691   6.614 -21.692  1.00 47.74           C  
-ANISOU 8856  CB  ILE D 836     6550   5487   6103     16    461   -411       C  
-ATOM   8857  CG1 ILE D 836    -105.774   5.795 -20.986  1.00 48.29           C  
-ANISOU 8857  CG1 ILE D 836     6644   5456   6248    -44    458   -394       C  
-ATOM   8858  CG2 ILE D 836    -104.502   7.930 -20.935  1.00 47.93           C  
-ANISOU 8858  CG2 ILE D 836     6545   5583   6082      2    479   -338       C  
-ATOM   8859  CD1 ILE D 836    -105.355   5.280 -19.625  1.00 50.85           C  
-ANISOU 8859  CD1 ILE D 836     6992   5719   6609    -37    474   -311       C  
-ATOM   8860  N   PHE D 837    -104.271   8.864 -24.247  1.00 48.29           N  
-ANISOU 8860  N   PHE D 837     6520   5814   6015     65    461   -469       N  
-ATOM   8861  CA  PHE D 837    -103.298   9.712 -24.901  1.00 47.52           C  
-ANISOU 8861  CA  PHE D 837     6380   5819   5856    113    471   -448       C  
-ATOM   8862  C   PHE D 837    -102.940  10.929 -24.037  1.00 48.12           C  
-ANISOU 8862  C   PHE D 837     6433   5923   5929     91    487   -362       C  
-ATOM   8863  O   PHE D 837    -103.813  11.532 -23.395  1.00 43.73           O  
-ANISOU 8863  O   PHE D 837     5874   5350   5392     35    487   -332       O  
-ATOM   8864  CB  PHE D 837    -103.862  10.218 -26.215  1.00 50.11           C  
-ANISOU 8864  CB  PHE D 837     6668   6238   6135    117    466   -486       C  
-ATOM   8865  CG  PHE D 837    -104.279   9.126 -27.172  1.00 53.57           C  
-ANISOU 8865  CG  PHE D 837     7116   6666   6570    144    443   -590       C  
-ATOM   8866  CD1 PHE D 837    -103.351   8.540 -28.017  1.00 55.34           C  
-ANISOU 8866  CD1 PHE D 837     7331   6938   6758    223    436   -644       C  
-ATOM   8867  CD2 PHE D 837    -105.599   8.708 -27.238  1.00 52.86           C  
-ANISOU 8867  CD2 PHE D 837     7041   6528   6515     92    426   -640       C  
-ATOM   8868  CE1 PHE D 837    -103.729   7.545 -28.898  1.00 58.29           C  
-ANISOU 8868  CE1 PHE D 837     7709   7305   7133    254    408   -757       C  
-ATOM   8869  CE2 PHE D 837    -105.992   7.718 -28.123  1.00 56.80           C  
-ANISOU 8869  CE2 PHE D 837     7543   7015   7022    115    399   -749       C  
-ATOM   8870  CZ  PHE D 837    -105.049   7.131 -28.955  1.00 58.12           C  
-ANISOU 8870  CZ  PHE D 837     7702   7226   7155    199    387   -813       C  
-ATOM   8871  N   LYS D 838    -101.653  11.263 -24.015  1.00 45.49           N  
-ANISOU 8871  N   LYS D 838     6077   5633   5573    137    496   -328       N  
-ATOM   8872  CA  LYS D 838    -101.156  12.471 -23.379  1.00 46.41           C  
-ANISOU 8872  CA  LYS D 838     6158   5782   5692    123    505   -259       C  
-ATOM   8873  C   LYS D 838    -101.041  13.517 -24.448  1.00 42.47           C  
-ANISOU 8873  C   LYS D 838     5600   5376   5159    130    511   -236       C  
-ATOM   8874  O   LYS D 838    -100.444  13.264 -25.476  1.00 38.97           O  
-ANISOU 8874  O   LYS D 838     5136   4997   4675    179    516   -254       O  
-ATOM   8875  CB  LYS D 838     -99.795  12.229 -22.736  1.00 49.78           C  
-ANISOU 8875  CB  LYS D 838     6588   6205   6122    167    511   -234       C  
-ATOM   8876  CG  LYS D 838     -99.369  13.280 -21.727  1.00 53.56           C  
-ANISOU 8876  CG  LYS D 838     7035   6693   6621    148    513   -177       C  
-ATOM   8877  CD  LYS D 838     -98.299  12.766 -20.766  1.00 56.58           C  
-ANISOU 8877  CD  LYS D 838     7432   7053   7010    186    514   -164       C  
-ATOM   8878  CE  LYS D 838     -98.290  13.510 -19.424  1.00 58.54           C  
-ANISOU 8878  CE  LYS D 838     7665   7293   7285    161    508   -130       C  
-ATOM   8879  NZ  LYS D 838     -98.772  14.923 -19.483  1.00 57.88           N  
-ANISOU 8879  NZ  LYS D 838     7534   7239   7220    117    500   -111       N  
-ATOM   8880  N   ILE D 839    -101.679  14.664 -24.240  1.00 40.28           N  
-ANISOU 8880  N   ILE D 839     5294   5111   4899     84    510   -197       N  
-ATOM   8881  CA  ILE D 839    -101.751  15.683 -25.281  1.00 40.79           C  
-ANISOU 8881  CA  ILE D 839     5300   5258   4939     86    516   -163       C  
-ATOM   8882  C   ILE D 839    -101.169  17.040 -24.852  1.00 44.26           C  
-ANISOU 8882  C   ILE D 839     5688   5713   5416     70    519    -89       C  
-ATOM   8883  O   ILE D 839    -101.339  17.457 -23.716  1.00 44.78           O  
-ANISOU 8883  O   ILE D 839     5762   5724   5527     37    508    -79       O  
-ATOM   8884  CB  ILE D 839    -103.188  15.873 -25.797  1.00 39.78           C  
-ANISOU 8884  CB  ILE D 839     5174   5139   4802     51    510   -187       C  
-ATOM   8885  CG1 ILE D 839    -104.158  16.192 -24.671  1.00 41.00           C  
-ANISOU 8885  CG1 ILE D 839     5353   5225   5001     -7    499   -184       C  
-ATOM   8886  CG2 ILE D 839    -103.654  14.631 -26.525  1.00 39.35           C  
-ANISOU 8886  CG2 ILE D 839     5152   5086   4713     72    504   -266       C  
-ATOM   8887  CD1 ILE D 839    -105.517  16.602 -25.188  1.00 39.81           C  
-ANISOU 8887  CD1 ILE D 839     5191   5095   4840    -41    493   -198       C  
-ATOM   8888  N   GLU D 840    -100.469  17.700 -25.777  1.00 44.25           N  
-ANISOU 8888  N   GLU D 840     5626   5789   5397     96    531    -39       N  
-ATOM   8889  CA  GLU D 840     -99.928  19.038 -25.557  1.00 43.34           C  
-ANISOU 8889  CA  GLU D 840     5450   5685   5333     77    531     37       C  
-ATOM   8890  C   GLU D 840    -100.279  19.851 -26.775  1.00 40.58           C  
-ANISOU 8890  C   GLU D 840     5043   5410   4966     79    542     92       C  
-ATOM   8891  O   GLU D 840     -99.681  19.678 -27.844  1.00 39.20           O  
-ANISOU 8891  O   GLU D 840     4831   5325   4738    125    561    118       O  
-ATOM   8892  CB  GLU D 840     -98.408  19.025 -25.386  1.00 45.41           C  
-ANISOU 8892  CB  GLU D 840     5681   5970   5603    111    539     68       C  
-ATOM   8893  CG  GLU D 840     -97.908  18.123 -24.266  1.00 49.07           C  
-ANISOU 8893  CG  GLU D 840     6198   6376   6072    124    531     20       C  
-ATOM   8894  CD  GLU D 840     -96.390  17.870 -24.307  1.00 54.32           C  
-ANISOU 8894  CD  GLU D 840     6835   7082   6724    171    541     40       C  
-ATOM   8895  OE1 GLU D 840     -95.663  18.377 -25.208  1.00 56.55           O  
-ANISOU 8895  OE1 GLU D 840     7052   7442   6992    192    556     94       O  
-ATOM   8896  OE2 GLU D 840     -95.902  17.146 -23.408  1.00 59.29           O  
-ANISOU 8896  OE2 GLU D 840     7502   7671   7354    189    535      7       O  
-ATOM   8897  N   ARG D 841    -101.265  20.728 -26.632  1.00 36.85           N  
-ANISOU 8897  N   ARG D 841     4559   4910   4532     37    532    111       N  
-ATOM   8898  CA  ARG D 841    -101.576  21.664 -27.690  1.00 37.64           C  
-ANISOU 8898  CA  ARG D 841     4598   5077   4628     39    542    182       C  
-ATOM   8899  C   ARG D 841    -100.506  22.766 -27.780  1.00 38.09           C  
-ANISOU 8899  C   ARG D 841     4577   5148   4746     38    549    281       C  
-ATOM   8900  O   ARG D 841    -100.124  23.360 -26.784  1.00 40.29           O  
-ANISOU 8900  O   ARG D 841     4847   5353   5107      7    531    290       O  
-ATOM   8901  CB  ARG D 841    -102.926  22.327 -27.466  1.00 37.30           C  
-ANISOU 8901  CB  ARG D 841     4562   4994   4616     -3    526    176       C  
-ATOM   8902  CG  ARG D 841    -104.120  21.378 -27.501  1.00 39.11           C  
-ANISOU 8902  CG  ARG D 841     4851   5216   4790     -9    520     90       C  
-ATOM   8903  CD  ARG D 841    -105.307  22.070 -28.163  1.00 38.67           C  
-ANISOU 8903  CD  ARG D 841     4771   5196   4725    -23    517    111       C  
-ATOM   8904  NE  ARG D 841    -105.493  23.303 -27.481  1.00 38.96           N  
-ANISOU 8904  NE  ARG D 841     4781   5176   4846    -58    502    159       N  
-ATOM   8905  CZ  ARG D 841    -105.389  24.530 -27.978  1.00 37.04           C  
-ANISOU 8905  CZ  ARG D 841     4473   4954   4648    -58    505    248       C  
-ATOM   8906  NH1 ARG D 841    -105.253  24.798 -29.272  1.00 34.57           N  
-ANISOU 8906  NH1 ARG D 841     4107   4735   4291    -25    527    316       N  
-ATOM   8907  NH2 ARG D 841    -105.548  25.510 -27.119  1.00 34.84           N  
-ANISOU 8907  NH2 ARG D 841     4179   4597   4461    -91    482    265       N  
-ATOM   8908  N   GLU D 842    -100.048  23.045 -28.987  1.00 38.42           N  
-ANISOU 8908  N   GLU D 842     4557   5291   4750     72    573    355       N  
-ATOM   8909  CA  GLU D 842     -99.122  24.134 -29.220  1.00 40.72           C  
-ANISOU 8909  CA  GLU D 842     4763   5602   5107     66    583    468       C  
-ATOM   8910  C   GLU D 842     -99.654  25.437 -28.656  1.00 39.48           C  
-ANISOU 8910  C   GLU D 842     4579   5358   5065     11    561    512       C  
-ATOM   8911  O   GLU D 842    -100.800  25.847 -28.930  1.00 40.64           O  
-ANISOU 8911  O   GLU D 842     4731   5498   5212     -3    555    516       O  
-ATOM   8912  CB  GLU D 842     -98.847  24.303 -30.737  1.00 43.43           C  
-ANISOU 8912  CB  GLU D 842     5034   6086   5381    113    617    557       C  
-ATOM   8913  N   GLY D 843     -98.819  26.096 -27.869  1.00 36.79           N  
-ANISOU 8913  N   GLY D 843     4204   4950   4824    -16    545    540       N  
-ATOM   8914  CA  GLY D 843     -99.164  27.417 -27.349  1.00 36.56           C  
-ANISOU 8914  CA  GLY D 843     4136   4832   4923    -63    518    578       C  
-ATOM   8915  C   GLY D 843     -99.947  27.385 -26.039  1.00 34.79           C  
-ANISOU 8915  C   GLY D 843     3975   4509   4736    -92    480    473       C  
-ATOM   8916  O   GLY D 843    -100.101  28.413 -25.399  1.00 33.71           O  
-ANISOU 8916  O   GLY D 843     3807   4292   4710   -125    448    480       O  
-ATOM   8917  N   GLU D 844    -100.428  26.221 -25.627  1.00 31.96           N  
-ANISOU 8917  N   GLU D 844     3697   4156   4291    -79    481    378       N  
-ATOM   8918  CA  GLU D 844    -101.326  26.199 -24.478  1.00 33.00           C  
-ANISOU 8918  CA  GLU D 844     3879   4214   4444   -103    449    293       C  
-ATOM   8919  C   GLU D 844    -100.575  26.384 -23.166  1.00 31.98           C  
-ANISOU 8919  C   GLU D 844     3747   4023   4382   -113    421    250       C  
-ATOM   8920  O   GLU D 844    -101.103  27.006 -22.251  1.00 29.11           O  
-ANISOU 8920  O   GLU D 844     3382   3599   4080   -135    387    208       O  
-ATOM   8921  CB  GLU D 844    -102.160  24.927 -24.443  1.00 33.10           C  
-ANISOU 8921  CB  GLU D 844     3972   4249   4355    -91    460    217       C  
-ATOM   8922  CG  GLU D 844    -103.524  25.144 -23.828  1.00 37.15           C  
-ANISOU 8922  CG  GLU D 844     4517   4719   4878   -118    438    166       C  
-ATOM   8923  CD  GLU D 844    -104.399  23.883 -23.859  1.00 37.54           C  
-ANISOU 8923  CD  GLU D 844     4637   4788   4838   -114    449     99       C  
-ATOM   8924  OE1 GLU D 844    -103.975  22.915 -23.224  1.00 33.12           O  
-ANISOU 8924  OE1 GLU D 844     4120   4213   4251   -104    451     55       O  
-ATOM   8925  OE2 GLU D 844    -105.497  23.902 -24.521  1.00 38.90           O  
-ANISOU 8925  OE2 GLU D 844     4816   4988   4976   -121    453     96       O  
-ATOM   8926  N   CYS D 845     -99.343  25.874 -23.091  1.00 32.21           N  
-ANISOU 8926  N   CYS D 845     3767   4077   4396    -92    433    257       N  
-ATOM   8927  CA  CYS D 845     -98.510  26.041 -21.895  1.00 32.55           C  
-ANISOU 8927  CA  CYS D 845     3796   4077   4496    -96    407    217       C  
-ATOM   8928  C   CYS D 845     -98.258  27.522 -21.641  1.00 32.04           C  
-ANISOU 8928  C   CYS D 845     3652   3955   4566   -127    374    252       C  
-ATOM   8929  O   CYS D 845     -98.435  28.021 -20.538  1.00 30.74           O  
-ANISOU 8929  O   CYS D 845     3482   3734   4465   -140    334    190       O  
-ATOM   8930  CB  CYS D 845     -97.159  25.294 -22.007  1.00 32.50           C  
-ANISOU 8930  CB  CYS D 845     3783   4117   4449    -64    427    230       C  
-ATOM   8931  SG  CYS D 845     -96.008  25.651 -20.621  1.00 35.24           S  
-ANISOU 8931  SG  CYS D 845     4093   4424   4872    -65    392    187       S  
-ATOM   8932  N   GLN D 846     -97.882  28.224 -22.689  1.00 33.10           N  
-ANISOU 8932  N   GLN D 846     3721   4107   4746   -136    390    352       N  
-ATOM   8933  CA  GLN D 846     -97.644  29.665 -22.606  1.00 36.16           C  
-ANISOU 8933  CA  GLN D 846     4026   4429   5283   -170    360    402       C  
-ATOM   8934  C   GLN D 846     -98.934  30.420 -22.259  1.00 33.32           C  
-ANISOU 8934  C   GLN D 846     3678   4005   4978   -190    327    367       C  
-ATOM   8935  O   GLN D 846     -98.931  31.291 -21.393  1.00 31.64           O  
-ANISOU 8935  O   GLN D 846     3431   3713   4877   -209    280    324       O  
-ATOM   8936  CB  GLN D 846     -97.031  30.176 -23.918  1.00 37.85           C  
-ANISOU 8936  CB  GLN D 846     4166   4688   5528   -173    393    540       C  
-ATOM   8937  CG  GLN D 846     -96.573  31.629 -23.876  1.00 42.30           C  
-ANISOU 8937  CG  GLN D 846     4631   5174   6266   -212    364    610       C  
-ATOM   8938  CD  GLN D 846     -95.436  31.880 -22.876  1.00 44.31           C  
-ANISOU 8938  CD  GLN D 846     4845   5380   6612   -227    329    563       C  
-ATOM   8939  OE1 GLN D 846     -94.539  31.033 -22.684  1.00 45.95           O  
-ANISOU 8939  OE1 GLN D 846     5066   5644   6748   -204    346    538       O  
-ATOM   8940  NE2 GLN D 846     -95.432  33.073 -22.281  1.00 44.49           N  
-ANISOU 8940  NE2 GLN D 846     4809   5299   6799   -262    278    550       N  
-ATOM   8941  N   ARG D 847    -100.036  30.038 -22.881  1.00 31.39           N  
-ANISOU 8941  N   ARG D 847     3479   3797   4650   -181    349    374       N  
-ATOM   8942  CA  ARG D 847    -101.317  30.657 -22.547  1.00 35.55           C  
-ANISOU 8942  CA  ARG D 847     4021   4275   5213   -194    320    336       C  
-ATOM   8943  C   ARG D 847    -101.743  30.366 -21.084  1.00 36.25           C  
-ANISOU 8943  C   ARG D 847     4155   4326   5291   -192    283    209       C  
-ATOM   8944  O   ARG D 847    -102.260  31.236 -20.391  1.00 36.66           O  
-ANISOU 8944  O   ARG D 847     4185   4316   5426   -202    239    164       O  
-ATOM   8945  CB  ARG D 847    -102.391  30.176 -23.518  1.00 36.01           C  
-ANISOU 8945  CB  ARG D 847     4118   4395   5169   -183    353    362       C  
-ATOM   8946  CG  ARG D 847    -103.732  30.868 -23.383  1.00 35.34           C  
-ANISOU 8946  CG  ARG D 847     4039   4272   5116   -193    328    340       C  
-ATOM   8947  CD  ARG D 847    -104.701  30.295 -24.391  1.00 35.84           C  
-ANISOU 8947  CD  ARG D 847     4136   4411   5069   -179    362    363       C  
-ATOM   8948  NE  ARG D 847    -105.222  28.988 -23.966  1.00 36.42           N  
-ANISOU 8948  NE  ARG D 847     4290   4520   5028   -172    372    272       N  
-ATOM   8949  CZ  ARG D 847    -106.195  28.325 -24.591  1.00 35.45           C  
-ANISOU 8949  CZ  ARG D 847     4205   4454   4809   -164    393    256       C  
-ATOM   8950  NH1 ARG D 847    -106.782  28.847 -25.643  1.00 37.65           N  
-ANISOU 8950  NH1 ARG D 847     4453   4773   5080   -157    405    320       N  
-ATOM   8951  NH2 ARG D 847    -106.600  27.141 -24.145  1.00 37.95           N  
-ANISOU 8951  NH2 ARG D 847     4588   4788   5043   -163    399    177       N  
-ATOM   8952  N   TYR D 848    -101.466  29.157 -20.601  1.00 35.75           N  
-ANISOU 8952  N   TYR D 848     4149   4305   5129   -173    300    154       N  
-ATOM   8953  CA  TYR D 848    -101.856  28.760 -19.236  1.00 34.40           C  
-ANISOU 8953  CA  TYR D 848     4019   4121   4932   -164    272     49       C  
-ATOM   8954  C   TYR D 848    -100.970  29.346 -18.127  1.00 34.68           C  
-ANISOU 8954  C   TYR D 848     4007   4117   5053   -160    229     -1       C  
-ATOM   8955  O   TYR D 848    -101.368  29.392 -16.971  1.00 34.72           O  
-ANISOU 8955  O   TYR D 848     4023   4113   5056   -149    196    -87       O  
-ATOM   8956  CB  TYR D 848    -101.860  27.242 -19.157  1.00 31.62           C  
-ANISOU 8956  CB  TYR D 848     3739   3822   4452   -144    307     24       C  
-ATOM   8957  CG  TYR D 848    -102.392  26.662 -17.871  1.00 31.43           C  
-ANISOU 8957  CG  TYR D 848     3760   3801   4382   -132    291    -60       C  
-ATOM   8958  CD1 TYR D 848    -103.748  26.746 -17.547  1.00 29.52           C  
-ANISOU 8958  CD1 TYR D 848     3542   3557   4116   -141    280    -97       C  
-ATOM   8959  CD2 TYR D 848    -101.559  25.959 -17.007  1.00 29.75           C  
-ANISOU 8959  CD2 TYR D 848     3561   3605   4137   -108    290    -95       C  
-ATOM   8960  CE1 TYR D 848    -104.255  26.159 -16.380  1.00 30.18           C  
-ANISOU 8960  CE1 TYR D 848     3660   3660   4148   -128    270   -161       C  
-ATOM   8961  CE2 TYR D 848    -102.062  25.373 -15.842  1.00 29.86           C  
-ANISOU 8961  CE2 TYR D 848     3611   3636   4100    -92    280   -156       C  
-ATOM   8962  CZ  TYR D 848    -103.407  25.481 -15.533  1.00 28.98           C  
-ANISOU 8962  CZ  TYR D 848     3519   3526   3966   -103    271   -186       C  
-ATOM   8963  OH  TYR D 848    -103.923  24.926 -14.395  1.00 31.17           O  
-ANISOU 8963  OH  TYR D 848     3822   3833   4189    -86    265   -233       O  
-ATOM   8964  N   LYS D 849     -99.798  29.835 -18.505  1.00 36.47           N  
-ANISOU 8964  N   LYS D 849     4173   4327   5355   -169    228     52       N  
-ATOM   8965  CA  LYS D 849     -98.758  30.284 -17.569  1.00 36.71           C  
-ANISOU 8965  CA  LYS D 849     4152   4329   5467   -165    189      5       C  
-ATOM   8966  C   LYS D 849     -99.243  31.187 -16.434  1.00 34.34           C  
-ANISOU 8966  C   LYS D 849     3820   3974   5251   -165    125    -90       C  
-ATOM   8967  O   LYS D 849     -98.897  30.961 -15.291  1.00 35.80           O  
-ANISOU 8967  O   LYS D 849     4005   4176   5421   -141     97   -177       O  
-ATOM   8968  CB  LYS D 849     -97.632  30.975 -18.363  1.00 40.93           C  
-ANISOU 8968  CB  LYS D 849     4607   4842   6101   -188    195     96       C  
-ATOM   8969  CG  LYS D 849     -96.405  31.356 -17.558  1.00 43.58           C  
-ANISOU 8969  CG  LYS D 849     4882   5155   6522   -188    159     55       C  
-ATOM   8970  CD  LYS D 849     -95.358  31.911 -18.490  1.00 48.04           C  
-ANISOU 8970  CD  LYS D 849     5369   5710   7176   -214    175    165       C  
-ATOM   8971  CE  LYS D 849     -94.096  32.223 -17.728  1.00 51.58           C  
-ANISOU 8971  CE  LYS D 849     5751   6141   7707   -217    140    123       C  
-ATOM   8972  NZ  LYS D 849     -94.326  33.269 -16.697  1.00 53.79           N  
-ANISOU 8972  NZ  LYS D 849     5982   6336   8118   -230     66     27       N  
-ATOM   8973  N   PRO D 850    -100.057  32.215 -16.733  1.00 32.84           N  
-ANISOU 8973  N   PRO D 850     3602   3727   5148   -184    100    -78       N  
-ATOM   8974  CA  PRO D 850    -100.545  33.075 -15.632  1.00 33.44           C  
-ANISOU 8974  CA  PRO D 850     3647   3754   5304   -175     33   -184       C  
-ATOM   8975  C   PRO D 850    -101.374  32.315 -14.573  1.00 34.67           C  
-ANISOU 8975  C   PRO D 850     3863   3973   5340   -139     27   -283       C  
-ATOM   8976  O   PRO D 850    -101.443  32.736 -13.426  1.00 34.55           O  
-ANISOU 8976  O   PRO D 850     3818   3953   5356   -115    -26   -388       O  
-ATOM   8977  CB  PRO D 850    -101.394  34.129 -16.342  1.00 32.06           C  
-ANISOU 8977  CB  PRO D 850     3444   3513   5224   -197     19   -137       C  
-ATOM   8978  CG  PRO D 850    -100.946  34.095 -17.768  1.00 32.55           C  
-ANISOU 8978  CG  PRO D 850     3493   3579   5295   -222     70      5       C  
-ATOM   8979  CD  PRO D 850    -100.487  32.700 -18.050  1.00 31.98           C  
-ANISOU 8979  CD  PRO D 850     3479   3598   5074   -209    127     30       C  
-ATOM   8980  N   PHE D 851    -101.951  31.180 -14.957  1.00 32.97           N  
-ANISOU 8980  N   PHE D 851     3723   3819   4987   -135     81   -249       N  
-ATOM   8981  CA  PHE D 851    -102.785  30.413 -14.064  1.00 32.51           C  
-ANISOU 8981  CA  PHE D 851     3716   3818   4817   -108     83   -317       C  
-ATOM   8982  C   PHE D 851    -102.062  29.234 -13.431  1.00 33.53           C  
-ANISOU 8982  C   PHE D 851     3880   4008   4852    -82    106   -334       C  
-ATOM   8983  O   PHE D 851    -102.568  28.612 -12.509  1.00 30.14           O  
-ANISOU 8983  O   PHE D 851     3482   3631   4339    -55    105   -386       O  
-ATOM   8984  CB  PHE D 851    -104.065  30.019 -14.830  1.00 31.92           C  
-ANISOU 8984  CB  PHE D 851     3696   3761   4673   -123    118   -275       C  
-ATOM   8985  CG  PHE D 851    -104.881  31.220 -15.260  1.00 31.75           C  
-ANISOU 8985  CG  PHE D 851     3638   3687   4740   -138     89   -269       C  
-ATOM   8986  CD1 PHE D 851    -105.613  31.942 -14.334  1.00 31.88           C  
-ANISOU 8986  CD1 PHE D 851     3628   3691   4792   -119     38   -357       C  
-ATOM   8987  CD2 PHE D 851    -104.873  31.657 -16.588  1.00 32.95           C  
-ANISOU 8987  CD2 PHE D 851     3774   3805   4939   -164    112   -173       C  
-ATOM   8988  CE1 PHE D 851    -106.338  33.061 -14.723  1.00 33.16           C  
-ANISOU 8988  CE1 PHE D 851     3756   3799   5044   -127      7   -353       C  
-ATOM   8989  CE2 PHE D 851    -105.586  32.768 -16.991  1.00 31.54           C  
-ANISOU 8989  CE2 PHE D 851     3560   3576   4848   -173     86   -157       C  
-ATOM   8990  CZ  PHE D 851    -106.330  33.468 -16.054  1.00 33.50           C  
-ANISOU 8990  CZ  PHE D 851     3789   3801   5140   -155     32   -249       C  
-ATOM   8991  N   LYS D 852    -100.866  28.951 -13.923  1.00 36.32           N  
-ANISOU 8991  N   LYS D 852     4223   4358   5220    -87    127   -284       N  
-ATOM   8992  CA  LYS D 852    -100.070  27.778 -13.526  1.00 38.01           C  
-ANISOU 8992  CA  LYS D 852     4470   4625   5346    -60    155   -284       C  
-ATOM   8993  C   LYS D 852     -99.800  27.660 -12.026  1.00 37.90           C  
-ANISOU 8993  C   LYS D 852     4440   4653   5308    -19    121   -372       C  
-ATOM   8994  O   LYS D 852     -99.684  26.545 -11.516  1.00 35.75           O  
-ANISOU 8994  O   LYS D 852     4213   4435   4937     10    146   -373       O  
-ATOM   8995  CB  LYS D 852     -98.731  27.824 -14.295  1.00 40.53           C  
-ANISOU 8995  CB  LYS D 852     4757   4932   5710    -70    172   -222       C  
-ATOM   8996  CG  LYS D 852     -97.746  26.693 -14.089  1.00 42.82           C  
-ANISOU 8996  CG  LYS D 852     5075   5272   5923    -39    201   -212       C  
-ATOM   8997  CD  LYS D 852     -98.254  25.388 -14.664  1.00 47.40           C  
-ANISOU 8997  CD  LYS D 852     5737   5881   6391    -32    254   -172       C  
-ATOM   8998  CE  LYS D 852     -97.352  24.233 -14.221  1.00 47.18           C  
-ANISOU 8998  CE  LYS D 852     5740   5896   6291      8    275   -175       C  
-ATOM   8999  NZ  LYS D 852     -97.977  22.939 -14.555  1.00 50.45           N  
-ANISOU 8999  NZ  LYS D 852     6234   6324   6611     16    315   -154       N  
-ATOM   9000  N   GLN D 853     -99.773  28.794 -11.332  1.00 37.93           N  
-ANISOU 9000  N   GLN D 853     4377   4634   5401    -12     61   -445       N  
-ATOM   9001  CA  GLN D 853     -99.616  28.861  -9.882  1.00 41.26           C  
-ANISOU 9001  CA  GLN D 853     4768   5109   5800     36     18   -545       C  
-ATOM   9002  C   GLN D 853    -100.803  29.442  -9.109  1.00 40.53           C  
-ANISOU 9002  C   GLN D 853     4660   5033   5705     55    -22   -625       C  
-ATOM   9003  O   GLN D 853    -100.664  29.741  -7.934  1.00 40.15           O  
-ANISOU 9003  O   GLN D 853     4569   5035   5653    101    -69   -720       O  
-ATOM   9004  CB  GLN D 853     -98.332  29.633  -9.586  1.00 46.74           C  
-ANISOU 9004  CB  GLN D 853     5381   5777   6599     41    -27   -587       C  
-ATOM   9005  CG  GLN D 853     -97.101  28.841 -10.017  1.00 48.68           C  
-ANISOU 9005  CG  GLN D 853     5641   6043   6813     41     13   -522       C  
-ATOM   9006  CD  GLN D 853     -95.916  29.116  -9.154  1.00 51.91           C  
-ANISOU 9006  CD  GLN D 853     5983   6481   7261     71    -28   -590       C  
-ATOM   9007  OE1 GLN D 853     -95.266  30.135  -9.287  1.00 55.29           O  
-ANISOU 9007  OE1 GLN D 853     6335   6853   7820     48    -70   -614       O  
-ATOM   9008  NE2 GLN D 853     -95.648  28.208  -8.224  1.00 58.26           N  
-ANISOU 9008  NE2 GLN D 853     6809   7373   7955    125    -19   -623       N  
-ATOM   9009  N   LEU D 854    -101.978  29.593  -9.741  1.00 40.13           N  
-ANISOU 9009  N   LEU D 854     4643   4956   5650     28     -7   -592       N  
-ATOM   9010  CA  LEU D 854    -103.237  29.742  -8.984  1.00 38.96           C  
-ANISOU 9010  CA  LEU D 854     4498   4853   5452     53    -28   -655       C  
-ATOM   9011  C   LEU D 854    -103.355  28.475  -8.173  1.00 37.63           C  
-ANISOU 9011  C   LEU D 854     4371   4783   5142     89      6   -651       C  
-ATOM   9012  O   LEU D 854    -102.940  27.394  -8.597  1.00 38.88           O  
-ANISOU 9012  O   LEU D 854     4582   4949   5240     78     58   -577       O  
-ATOM   9013  CB  LEU D 854    -104.443  29.874  -9.929  1.00 38.96           C  
-ANISOU 9013  CB  LEU D 854     4534   4816   5451     16     -4   -602       C  
-ATOM   9014  CG  LEU D 854    -105.691  30.675  -9.562  1.00 40.54           C  
-ANISOU 9014  CG  LEU D 854     4712   5021   5669     28    -42   -665       C  
-ATOM   9015  CD1 LEU D 854    -105.325  32.053  -9.048  1.00 45.07           C  
-ANISOU 9015  CD1 LEU D 854     5204   5547   6373     49   -119   -758       C  
-ATOM   9016  CD2 LEU D 854    -106.613  30.790 -10.784  1.00 39.74           C  
-ANISOU 9016  CD2 LEU D 854     4645   4874   5578    -15    -12   -592       C  
-ATOM   9017  N   HIS D 855    -104.005  28.578  -7.041  1.00 37.29           N  
-ANISOU 9017  N   HIS D 855     4305   4816   5046    134    -23   -724       N  
-ATOM   9018  CA  HIS D 855    -104.289  27.406  -6.226  1.00 35.66           C  
-ANISOU 9018  CA  HIS D 855     4132   4712   4705    169     12   -705       C  
-ATOM   9019  C   HIS D 855    -105.542  26.666  -6.745  1.00 32.41           C  
-ANISOU 9019  C   HIS D 855     3783   4304   4225    135     62   -635       C  
-ATOM   9020  O   HIS D 855    -106.212  27.127  -7.679  1.00 30.10           O  
-ANISOU 9020  O   HIS D 855     3507   3949   3982     92     65   -614       O  
-ATOM   9021  CB  HIS D 855    -104.499  27.835  -4.784  1.00 36.90           C  
-ANISOU 9021  CB  HIS D 855     4227   4971   4823    239    -39   -809       C  
-ATOM   9022  CG  HIS D 855    -105.691  28.719  -4.592  1.00 36.34           C  
-ANISOU 9022  CG  HIS D 855     4125   4908   4772    246    -76   -874       C  
-ATOM   9023  ND1 HIS D 855    -105.794  29.974  -5.155  1.00 34.64           N  
-ANISOU 9023  ND1 HIS D 855     3876   4600   4685    223   -123   -921       N  
-ATOM   9024  CD2 HIS D 855    -106.833  28.525  -3.890  1.00 36.83           C  
-ANISOU 9024  CD2 HIS D 855     4183   5066   4744    278    -74   -894       C  
-ATOM   9025  CE1 HIS D 855    -106.955  30.510  -4.819  1.00 35.48           C  
-ANISOU 9025  CE1 HIS D 855     3962   4740   4779    242   -150   -976       C  
-ATOM   9026  NE2 HIS D 855    -107.591  29.663  -4.029  1.00 36.66           N  
-ANISOU 9026  NE2 HIS D 855     4126   5010   4792    277   -122   -964       N  
-ATOM   9027  N   ASN D 856    -105.803  25.494  -6.171  1.00 31.04           N  
-ANISOU 9027  N   ASN D 856     3645   4205   3945    154    101   -592       N  
-ATOM   9028  CA  ASN D 856    -106.979  24.716  -6.489  1.00 32.27           C  
-ANISOU 9028  CA  ASN D 856     3851   4372   4039    123    145   -530       C  
-ATOM   9029  C   ASN D 856    -107.079  24.367  -7.992  1.00 32.21           C  
-ANISOU 9029  C   ASN D 856     3900   4268   4069     58    183   -461       C  
-ATOM   9030  O   ASN D 856    -108.041  24.696  -8.704  1.00 31.41           O  
-ANISOU 9030  O   ASN D 856     3811   4135   3986     21    187   -452       O  
-ATOM   9031  CB  ASN D 856    -108.221  25.455  -5.985  1.00 34.97           C  
-ANISOU 9031  CB  ASN D 856     4156   4766   4366    137    115   -587       C  
-ATOM   9032  CG  ASN D 856    -109.464  24.614  -6.076  1.00 38.45           C  
-ANISOU 9032  CG  ASN D 856     4635   5241   4733    110    158   -527       C  
-ATOM   9033  OD1 ASN D 856    -109.392  23.397  -6.144  1.00 38.60           O  
-ANISOU 9033  OD1 ASN D 856     4700   5264   4703     94    207   -450       O  
-ATOM   9034  ND2 ASN D 856    -110.607  25.261  -6.102  1.00 43.00           N  
-ANISOU 9034  ND2 ASN D 856     5189   5837   5310    104    139   -561       N  
-ATOM   9035  N   ARG D 857    -106.031  23.718  -8.464  1.00 33.44           N  
-ANISOU 9035  N   ARG D 857     4086   4385   4233     52    209   -416       N  
-ATOM   9036  CA  ARG D 857    -105.958  23.228  -9.821  1.00 33.12           C  
-ANISOU 9036  CA  ARG D 857     4096   4276   4214      5    245   -355       C  
-ATOM   9037  C   ARG D 857    -106.424  21.791  -9.828  1.00 32.61           C  
-ANISOU 9037  C   ARG D 857     4089   4223   4078     -6    292   -298       C  
-ATOM   9038  O   ARG D 857    -105.970  20.992  -9.017  1.00 32.85           O  
-ANISOU 9038  O   ARG D 857     4129   4291   4063     27    306   -280       O  
-ATOM   9039  CB  ARG D 857    -104.538  23.350 -10.314  1.00 35.63           C  
-ANISOU 9039  CB  ARG D 857     4404   4553   4579     11    244   -344       C  
-ATOM   9040  CG  ARG D 857    -104.273  24.773 -10.735  1.00 38.59           C  
-ANISOU 9040  CG  ARG D 857     4726   4887   5050     -1    203   -377       C  
-ATOM   9041  CD  ARG D 857    -102.828  25.187 -10.855  1.00 38.12           C  
-ANISOU 9041  CD  ARG D 857     4629   4805   5052     11    187   -381       C  
-ATOM   9042  NE  ARG D 857    -101.865  24.111 -10.711  1.00 39.20           N  
-ANISOU 9042  NE  ARG D 857     4794   4964   5137     34    217   -350       N  
-ATOM   9043  CZ  ARG D 857    -100.986  24.001  -9.728  1.00 43.45           C  
-ANISOU 9043  CZ  ARG D 857     5303   5544   5660     77    199   -383       C  
-ATOM   9044  NH1 ARG D 857    -100.922  24.907  -8.753  1.00 45.37           N  
-ANISOU 9044  NH1 ARG D 857     5485   5818   5936    104    148   -460       N  
-ATOM   9045  NH2 ARG D 857    -100.153  22.970  -9.738  1.00 50.57           N  
-ANISOU 9045  NH2 ARG D 857     6236   6461   6515     98    230   -345       N  
-ATOM   9046  N   ARG D 858    -107.319  21.470 -10.745  1.00 31.71           N  
-ANISOU 9046  N   ARG D 858     4010   4075   3962    -50    315   -269       N  
-ATOM   9047  CA  ARG D 858    -107.998  20.200 -10.705  1.00 34.34           C  
-ANISOU 9047  CA  ARG D 858     4389   4412   4245    -69    352   -224       C  
-ATOM   9048  C   ARG D 858    -108.065  19.548 -12.061  1.00 30.93           C  
-ANISOU 9048  C   ARG D 858     4004   3918   3828   -107    379   -194       C  
-ATOM   9049  O   ARG D 858    -108.283  20.224 -13.071  1.00 30.22           O  
-ANISOU 9049  O   ARG D 858     3908   3804   3771   -130    371   -206       O  
-ATOM   9050  CB  ARG D 858    -109.439  20.392 -10.175  1.00 34.86           C  
-ANISOU 9050  CB  ARG D 858     4439   4527   4280    -83    347   -235       C  
-ATOM   9051  CG  ARG D 858    -109.819  19.348  -9.159  1.00 41.24           C  
-ANISOU 9051  CG  ARG D 858     5256   5385   5029    -71    371   -194       C  
-ATOM   9052  CD  ARG D 858    -111.112  19.635  -8.395  1.00 43.97           C  
-ANISOU 9052  CD  ARG D 858     5568   5807   5333    -72    364   -204       C  
-ATOM   9053  NE  ARG D 858    -110.919  20.525  -7.247  1.00 45.47           N  
-ANISOU 9053  NE  ARG D 858     5698   6082   5499    -14    328   -256       N  
-ATOM   9054  CZ  ARG D 858    -111.838  20.789  -6.322  1.00 49.86           C  
-ANISOU 9054  CZ  ARG D 858     6211   6732   6002      8    318   -271       C  
-ATOM   9055  NH1 ARG D 858    -113.047  20.224  -6.372  1.00 50.56           N  
-ANISOU 9055  NH1 ARG D 858     6308   6842   6059    -28    345   -227       N  
-ATOM   9056  NH2 ARG D 858    -111.553  21.644  -5.342  1.00 51.22           N  
-ANISOU 9056  NH2 ARG D 858     6324   6984   6155     70    279   -337       N  
-ATOM   9057  N   LEU D 859    -107.864  18.228 -12.065  1.00 30.31           N  
-ANISOU 9057  N   LEU D 859     3970   3819   3729   -108    409   -156       N  
-ATOM   9058  CA  LEU D 859    -107.968  17.411 -13.261  1.00 30.21           C  
-ANISOU 9058  CA  LEU D 859     4002   3751   3727   -137    432   -140       C  
-ATOM   9059  C   LEU D 859    -109.411  16.931 -13.426  1.00 32.37           C  
-ANISOU 9059  C   LEU D 859     4290   4020   3989   -182    443   -133       C  
-ATOM   9060  O   LEU D 859    -109.914  16.118 -12.640  1.00 32.12           O  
-ANISOU 9060  O   LEU D 859     4270   3996   3940   -189    457   -103       O  
-ATOM   9061  CB  LEU D 859    -107.000  16.231 -13.175  1.00 31.55           C  
-ANISOU 9061  CB  LEU D 859     4207   3887   3892   -111    452   -111       C  
-ATOM   9062  CG  LEU D 859    -106.714  15.575 -14.540  1.00 32.71           C  
-ANISOU 9062  CG  LEU D 859     4389   3982   4055   -123    465   -116       C  
-ATOM   9063  CD1 LEU D 859    -105.789  16.442 -15.401  1.00 31.83           C  
-ANISOU 9063  CD1 LEU D 859     4255   3881   3959   -105    455   -132       C  
-ATOM   9064  CD2 LEU D 859    -106.114  14.190 -14.337  1.00 33.78           C  
-ANISOU 9064  CD2 LEU D 859     4567   4076   4191   -100    484    -90       C  
-ATOM   9065  N   LEU D 860    -110.073  17.459 -14.450  1.00 31.52           N  
-ANISOU 9065  N   LEU D 860     4177   3905   3893   -212    437   -156       N  
-ATOM   9066  CA  LEU D 860    -111.517  17.329 -14.601  1.00 29.76           C  
-ANISOU 9066  CA  LEU D 860     3953   3694   3659   -254    440   -161       C  
-ATOM   9067  C   LEU D 860    -111.878  16.900 -16.025  1.00 30.72           C  
-ANISOU 9067  C   LEU D 860     4098   3783   3792   -284    448   -176       C  
-ATOM   9068  O   LEU D 860    -111.093  17.086 -16.960  1.00 29.13           O  
-ANISOU 9068  O   LEU D 860     3901   3567   3599   -266    447   -186       O  
-ATOM   9069  CB  LEU D 860    -112.188  18.667 -14.315  1.00 30.15           C  
-ANISOU 9069  CB  LEU D 860     3957   3793   3705   -254    416   -186       C  
-ATOM   9070  CG  LEU D 860    -112.036  19.212 -12.902  1.00 32.19           C  
-ANISOU 9070  CG  LEU D 860     4181   4102   3948   -219    399   -192       C  
-ATOM   9071  CD1 LEU D 860    -112.571  20.643 -12.830  1.00 31.22           C  
-ANISOU 9071  CD1 LEU D 860     4012   4013   3837   -211    367   -233       C  
-ATOM   9072  CD2 LEU D 860    -112.763  18.326 -11.882  1.00 33.69           C  
-ANISOU 9072  CD2 LEU D 860     4374   4328   4100   -227    417   -160       C  
-ATOM   9073  N   TRP D 861    -113.062  16.316 -16.160  1.00 28.61           N  
-ANISOU 9073  N   TRP D 861     3838   3512   3520   -325    455   -179       N  
-ATOM   9074  CA  TRP D 861    -113.509  15.763 -17.405  1.00 29.24           C  
-ANISOU 9074  CA  TRP D 861     3936   3567   3608   -352    459   -206       C  
-ATOM   9075  C   TRP D 861    -114.175  16.797 -18.293  1.00 28.61           C  
-ANISOU 9075  C   TRP D 861     3827   3530   3515   -360    445   -232       C  
-ATOM   9076  O   TRP D 861    -114.853  17.705 -17.803  1.00 26.02           O  
-ANISOU 9076  O   TRP D 861     3468   3242   3176   -365    434   -231       O  
-ATOM   9077  CB  TRP D 861    -114.536  14.638 -17.148  1.00 30.35           C  
-ANISOU 9077  CB  TRP D 861     4090   3681   3761   -398    469   -200       C  
-ATOM   9078  CG  TRP D 861    -114.033  13.496 -16.335  1.00 30.12           C  
-ANISOU 9078  CG  TRP D 861     4088   3601   3755   -394    484   -160       C  
-ATOM   9079  CD1 TRP D 861    -114.329  13.224 -15.022  1.00 29.85           C  
-ANISOU 9079  CD1 TRP D 861     4043   3582   3716   -400    496   -108       C  
-ATOM   9080  CD2 TRP D 861    -113.163  12.455 -16.774  1.00 30.53           C  
-ANISOU 9080  CD2 TRP D 861     4178   3585   3838   -378    490   -165       C  
-ATOM   9081  NE1 TRP D 861    -113.671  12.087 -14.608  1.00 31.26           N  
-ANISOU 9081  NE1 TRP D 861     4251   3702   3924   -388    510    -69       N  
-ATOM   9082  CE2 TRP D 861    -112.951  11.591 -15.666  1.00 32.06           C  
-ANISOU 9082  CE2 TRP D 861     4386   3745   4052   -375    505   -108       C  
-ATOM   9083  CE3 TRP D 861    -112.546  12.155 -17.991  1.00 31.45           C  
-ANISOU 9083  CE3 TRP D 861     4314   3673   3964   -358    484   -211       C  
-ATOM   9084  CZ2 TRP D 861    -112.148  10.457 -15.749  1.00 34.13           C  
-ANISOU 9084  CZ2 TRP D 861     4683   3931   4352   -356    512    -97       C  
-ATOM   9085  CZ3 TRP D 861    -111.739  11.014 -18.074  1.00 31.66           C  
-ANISOU 9085  CZ3 TRP D 861     4376   3631   4023   -337    489   -211       C  
-ATOM   9086  CH2 TRP D 861    -111.546  10.191 -16.963  1.00 33.91           C  
-ANISOU 9086  CH2 TRP D 861     4677   3869   4336   -337    502   -154       C  
-ATOM   9087  N   HIS D 862    -114.027  16.609 -19.605  1.00 27.78           N  
-ANISOU 9087  N   HIS D 862     3729   3421   3406   -356    446   -258       N  
-ATOM   9088  CA  HIS D 862    -114.870  17.319 -20.561  1.00 29.82           C  
-ANISOU 9088  CA  HIS D 862     3960   3725   3646   -367    437   -279       C  
-ATOM   9089  C   HIS D 862    -115.163  16.441 -21.777  1.00 29.86           C  
-ANISOU 9089  C   HIS D 862     3977   3728   3641   -376    439   -321       C  
-ATOM   9090  O   HIS D 862    -114.259  16.008 -22.460  1.00 27.21           O  
-ANISOU 9090  O   HIS D 862     3655   3382   3303   -347    443   -332       O  
-ATOM   9091  CB  HIS D 862    -114.222  18.610 -21.038  1.00 29.29           C  
-ANISOU 9091  CB  HIS D 862     3863   3690   3578   -332    429   -259       C  
-ATOM   9092  CG  HIS D 862    -115.084  19.387 -21.968  1.00 30.10           C  
-ANISOU 9092  CG  HIS D 862     3933   3842   3662   -336    421   -267       C  
-ATOM   9093  ND1 HIS D 862    -115.958  20.355 -21.537  1.00 31.54           N  
-ANISOU 9093  ND1 HIS D 862     4086   4050   3847   -346    408   -262       N  
-ATOM   9094  CD2 HIS D 862    -115.238  19.311 -23.307  1.00 34.01           C  
-ANISOU 9094  CD2 HIS D 862     4416   4374   4130   -326    424   -281       C  
-ATOM   9095  CE1 HIS D 862    -116.610  20.854 -22.571  1.00 33.51           C  
-ANISOU 9095  CE1 HIS D 862     4311   4345   4077   -344    404   -267       C  
-ATOM   9096  NE2 HIS D 862    -116.184  20.246 -23.660  1.00 35.17           N  
-ANISOU 9096  NE2 HIS D 862     4529   4568   4265   -330    415   -276       N  
-ATOM   9097  N   GLY D 863    -116.437  16.138 -21.982  1.00 34.48           N  
-ANISOU 9097  N   GLY D 863     4554   4328   4221   -416    434   -350       N  
-ATOM   9098  CA  GLY D 863    -116.871  15.276 -23.062  1.00 37.34           C  
-ANISOU 9098  CA  GLY D 863     4920   4689   4578   -428    429   -407       C  
-ATOM   9099  C   GLY D 863    -117.466  16.094 -24.168  1.00 38.28           C  
-ANISOU 9099  C   GLY D 863     5002   4887   4655   -415    420   -428       C  
-ATOM   9100  O   GLY D 863    -118.020  17.169 -23.921  1.00 42.63           O  
-ANISOU 9100  O   GLY D 863     5526   5480   5192   -418    417   -401       O  
-ATOM   9101  N   SER D 864    -117.401  15.554 -25.378  1.00 39.30           N  
-ANISOU 9101  N   SER D 864     5127   5042   4763   -397    413   -481       N  
-ATOM   9102  CA  SER D 864    -117.920  16.221 -26.570  1.00 40.90           C  
-ANISOU 9102  CA  SER D 864     5289   5337   4915   -374    406   -501       C  
-ATOM   9103  C   SER D 864    -118.062  15.185 -27.682  1.00 40.61           C  
-ANISOU 9103  C   SER D 864     5249   5320   4860   -363    394   -585       C  
-ATOM   9104  O   SER D 864    -117.476  14.126 -27.601  1.00 36.54           O  
-ANISOU 9104  O   SER D 864     4765   4743   4377   -361    391   -620       O  
-ATOM   9105  CB  SER D 864    -116.948  17.321 -27.004  1.00 41.89           C  
-ANISOU 9105  CB  SER D 864     5393   5509   5015   -320    416   -441       C  
-ATOM   9106  OG  SER D 864    -117.552  18.212 -27.905  1.00 44.39           O  
-ANISOU 9106  OG  SER D 864     5664   5914   5287   -300    412   -431       O  
-ATOM   9107  N   ARG D 865    -118.841  15.502 -28.709  1.00 41.94           N  
-ANISOU 9107  N   ARG D 865     5378   5578   4980   -351    383   -623       N  
-ATOM   9108  CA  ARG D 865    -119.009  14.606 -29.855  1.00 45.83           C  
-ANISOU 9108  CA  ARG D 865     5855   6111   5446   -329    365   -719       C  
-ATOM   9109  C   ARG D 865    -117.687  14.454 -30.570  1.00 46.56           C  
-ANISOU 9109  C   ARG D 865     5949   6233   5507   -260    370   -720       C  
-ATOM   9110  O   ARG D 865    -116.900  15.398 -30.653  1.00 47.79           O  
-ANISOU 9110  O   ARG D 865     6092   6429   5635   -221    389   -641       O  
-ATOM   9111  CB  ARG D 865    -120.039  15.126 -30.845  1.00 45.16           C  
-ANISOU 9111  CB  ARG D 865     5718   6141   5299   -317    353   -753       C  
-ATOM   9112  CG  ARG D 865    -121.470  15.051 -30.342  1.00 47.56           C  
-ANISOU 9112  CG  ARG D 865     6012   6430   5627   -384    342   -777       C  
-ATOM   9113  CD  ARG D 865    -122.366  15.896 -31.226  1.00 50.25           C  
-ANISOU 9113  CD  ARG D 865     6298   6897   5899   -360    335   -784       C  
-ATOM   9114  NE  ARG D 865    -123.672  16.110 -30.614  1.00 52.84           N  
-ANISOU 9114  NE  ARG D 865     6612   7219   6243   -419    329   -785       N  
-ATOM   9115  CZ  ARG D 865    -124.739  15.335 -30.802  1.00 56.39           C  
-ANISOU 9115  CZ  ARG D 865     7044   7675   6707   -464    308   -869       C  
-ATOM   9116  NH1 ARG D 865    -125.886  15.635 -30.199  1.00 55.73           N  
-ANISOU 9116  NH1 ARG D 865     6943   7598   6635   -515    306   -856       N  
-ATOM   9117  NH2 ARG D 865    -124.670  14.263 -31.579  1.00 57.91           N  
-ANISOU 9117  NH2 ARG D 865     7230   7868   6906   -457    286   -970       N  
-ATOM   9118  N   THR D 866    -117.455  13.247 -31.070  1.00 47.63           N  
-ANISOU 9118  N   THR D 866     6096   6346   5655   -245    352   -813       N  
-ATOM   9119  CA  THR D 866    -116.220  12.899 -31.761  1.00 47.31           C  
-ANISOU 9119  CA  THR D 866     6055   6337   5582   -174    353   -833       C  
-ATOM   9120  C   THR D 866    -115.902  13.846 -32.915  1.00 46.86           C  
-ANISOU 9120  C   THR D 866     5942   6432   5429   -102    364   -800       C  
-ATOM   9121  O   THR D 866    -114.746  14.211 -33.112  1.00 46.44           O  
-ANISOU 9121  O   THR D 866     5883   6412   5349    -51    382   -743       O  
-ATOM   9122  CB  THR D 866    -116.306  11.445 -32.238  1.00 48.85           C  
-ANISOU 9122  CB  THR D 866     6262   6492   5807   -166    322   -963       C  
-ATOM   9123  OG1 THR D 866    -116.578  10.626 -31.109  1.00 44.33           O  
-ANISOU 9123  OG1 THR D 866     5738   5771   5335   -236    317   -967       O  
-ATOM   9124  CG2 THR D 866    -115.001  10.980 -32.870  1.00 51.00           C  
-ANISOU 9124  CG2 THR D 866     6536   6794   6049    -87    320   -994       C  
-ATOM   9125  N   THR D 867    -116.942  14.256 -33.644  1.00 46.06           N  
-ANISOU 9125  N   THR D 867     5796   6427   5277   -100    354   -828       N  
-ATOM   9126  CA  THR D 867    -116.791  15.144 -34.788  1.00 48.51           C  
-ANISOU 9126  CA  THR D 867     6044   6896   5492    -30    364   -788       C  
-ATOM   9127  C   THR D 867    -116.358  16.560 -34.388  1.00 47.62           C  
-ANISOU 9127  C   THR D 867     5919   6793   5381    -27    396   -640       C  
-ATOM   9128  O   THR D 867    -116.100  17.389 -35.258  1.00 48.62           O  
-ANISOU 9128  O   THR D 867     5992   7040   5441     30    410   -578       O  
-ATOM   9129  CB  THR D 867    -118.089  15.190 -35.646  1.00 48.36           C  
-ANISOU 9129  CB  THR D 867     5976   6981   5417    -25    343   -858       C  
-ATOM   9130  OG1 THR D 867    -119.233  15.420 -34.795  1.00 47.26           O  
-ANISOU 9130  OG1 THR D 867     5854   6771   5331   -104    338   -849       O  
-ATOM   9131  CG2 THR D 867    -118.269  13.859 -36.396  1.00 50.13           C  
-ANISOU 9131  CG2 THR D 867     6192   7230   5627      0    307  -1016       C  
-ATOM   9132  N   ASN D 868    -116.292  16.848 -33.092  1.00 46.69           N  
-ANISOU 9132  N   ASN D 868     5845   6554   5340    -86    404   -584       N  
-ATOM   9133  CA  ASN D 868    -115.751  18.136 -32.619  1.00 44.67           C  
-ANISOU 9133  CA  ASN D 868     5579   6289   5106    -84    426   -459       C  
-ATOM   9134  C   ASN D 868    -114.263  18.132 -32.338  1.00 41.33           C  
-ANISOU 9134  C   ASN D 868     5170   5829   4705    -57    443   -406       C  
-ATOM   9135  O   ASN D 868    -113.695  19.179 -32.141  1.00 39.21           O  
-ANISOU 9135  O   ASN D 868     4880   5563   4455    -48    459   -307       O  
-ATOM   9136  CB  ASN D 868    -116.473  18.592 -31.353  1.00 41.85           C  
-ANISOU 9136  CB  ASN D 868     5249   5838   4815   -151    423   -431       C  
-ATOM   9137  CG  ASN D 868    -117.912  19.010 -31.615  1.00 41.67           C  
-ANISOU 9137  CG  ASN D 868     5199   5868   4768   -172    411   -451       C  
-ATOM   9138  OD1 ASN D 868    -118.250  19.516 -32.680  1.00 41.34           O  
-ANISOU 9138  OD1 ASN D 868     5107   5937   4664   -130    412   -439       O  
-ATOM   9139  ND2 ASN D 868    -118.768  18.802 -30.642  1.00 39.77           N  
-ANISOU 9139  ND2 ASN D 868     4985   5557   4571   -233    401   -477       N  
-ATOM   9140  N   PHE D 869    -113.642  16.961 -32.272  1.00 42.77           N  
-ANISOU 9140  N   PHE D 869     5387   5970   4894    -46    437   -474       N  
-ATOM   9141  CA  PHE D 869    -112.309  16.879 -31.679  1.00 43.57           C  
-ANISOU 9141  CA  PHE D 869     5513   6013   5031    -34    450   -429       C  
-ATOM   9142  C   PHE D 869    -111.171  17.418 -32.498  1.00 47.51           C  
-ANISOU 9142  C   PHE D 869     5965   6605   5483     32    470   -363       C  
-ATOM   9143  O   PHE D 869    -110.134  17.813 -31.942  1.00 45.79           O  
-ANISOU 9143  O   PHE D 869     5752   6347   5301     35    484   -294       O  
-ATOM   9144  CB  PHE D 869    -112.012  15.475 -31.194  1.00 44.42           C  
-ANISOU 9144  CB  PHE D 869     5674   6030   5173    -45    438   -512       C  
-ATOM   9145  CG  PHE D 869    -112.419  15.272 -29.770  1.00 42.89           C  
-ANISOU 9145  CG  PHE D 869     5529   5711   5055   -113    435   -502       C  
-ATOM   9146  CD1 PHE D 869    -113.730  14.958 -29.462  1.00 42.63           C  
-ANISOU 9146  CD1 PHE D 869     5508   5645   5044   -167    420   -548       C  
-ATOM   9147  CD2 PHE D 869    -111.522  15.486 -28.746  1.00 40.45           C  
-ANISOU 9147  CD2 PHE D 869     5245   5333   4789   -120    447   -442       C  
-ATOM   9148  CE1 PHE D 869    -114.129  14.804 -28.149  1.00 42.86           C  
-ANISOU 9148  CE1 PHE D 869     5572   5577   5134   -225    421   -528       C  
-ATOM   9149  CE2 PHE D 869    -111.910  15.334 -27.429  1.00 42.09           C  
-ANISOU 9149  CE2 PHE D 869     5490   5448   5055   -174    445   -430       C  
-ATOM   9150  CZ  PHE D 869    -113.218  14.988 -27.131  1.00 41.99           C  
-ANISOU 9150  CZ  PHE D 869     5487   5407   5059   -225    433   -469       C  
-ATOM   9151  N   ALA D 870    -111.349  17.486 -33.811  1.00 50.29           N  
-ANISOU 9151  N   ALA D 870     6264   7091   5753     88    471   -378       N  
-ATOM   9152  CA  ALA D 870    -110.345  18.151 -34.632  1.00 50.66           C  
-ANISOU 9152  CA  ALA D 870     6251   7248   5750    151    494   -291       C  
-ATOM   9153  C   ALA D 870    -110.335  19.636 -34.287  1.00 48.07           C  
-ANISOU 9153  C   ALA D 870     5892   6907   5465    126    512   -157       C  
-ATOM   9154  O   ALA D 870    -109.286  20.238 -34.175  1.00 45.30           O  
-ANISOU 9154  O   ALA D 870     5516   6556   5138    140    530    -66       O  
-ATOM   9155  CB  ALA D 870    -110.623  17.952 -36.121  1.00 51.42           C  
-ANISOU 9155  CB  ALA D 870     6288   7512   5738    224    493   -331       C  
-ATOM   9156  N   GLY D 871    -111.523  20.212 -34.126  1.00 47.73           N  
-ANISOU 9156  N   GLY D 871     5845   6852   5437     89    502   -151       N  
-ATOM   9157  CA  GLY D 871    -111.648  21.602 -33.720  1.00 48.54           C  
-ANISOU 9157  CA  GLY D 871     5922   6925   5598     64    511    -39       C  
-ATOM   9158  C   GLY D 871    -111.076  21.826 -32.316  1.00 44.55           C  
-ANISOU 9158  C   GLY D 871     5460   6278   5191     14    507    -16       C  
-ATOM   9159  O   GLY D 871    -110.313  22.750 -32.091  1.00 44.19           O  
-ANISOU 9159  O   GLY D 871     5385   6211   5196     15    517     79       O  
-ATOM   9160  N   ILE D 872    -111.435  20.964 -31.380  1.00 42.58           N  
-ANISOU 9160  N   ILE D 872     5273   5936   4968    -28    491   -102       N  
-ATOM   9161  CA  ILE D 872    -110.932  21.092 -30.004  1.00 41.94           C  
-ANISOU 9161  CA  ILE D 872     5230   5739   4967    -67    486    -88       C  
-ATOM   9162  C   ILE D 872    -109.421  20.950 -29.927  1.00 41.95           C  
-ANISOU 9162  C   ILE D 872     5227   5731   4981    -39    499    -52       C  
-ATOM   9163  O   ILE D 872    -108.762  21.729 -29.255  1.00 37.41           O  
-ANISOU 9163  O   ILE D 872     4640   5107   4469    -52    500     10       O  
-ATOM   9164  CB  ILE D 872    -111.573  20.055 -29.076  1.00 41.13           C  
-ANISOU 9164  CB  ILE D 872     5191   5556   4881   -110    471   -177       C  
-ATOM   9165  CG1 ILE D 872    -113.052  20.391 -28.893  1.00 41.73           C  
-ANISOU 9165  CG1 ILE D 872     5265   5632   4959   -147    458   -200       C  
-ATOM   9166  CG2 ILE D 872    -110.867  20.008 -27.723  1.00 39.29           C  
-ANISOU 9166  CG2 ILE D 872     4993   5226   4712   -133    469   -164       C  
-ATOM   9167  CD1 ILE D 872    -113.842  19.254 -28.308  1.00 42.78           C  
-ANISOU 9167  CD1 ILE D 872     5446   5713   5096   -187    446   -285       C  
-ATOM   9168  N   LEU D 873    -108.851  19.967 -30.613  1.00 43.35           N  
-ANISOU 9168  N   LEU D 873     5410   5958   5102      3    507    -95       N  
-ATOM   9169  CA  LEU D 873    -107.396  19.836 -30.578  1.00 44.42           C  
-ANISOU 9169  CA  LEU D 873     5537   6098   5244     35    520    -59       C  
-ATOM   9170  C   LEU D 873    -106.710  21.002 -31.264  1.00 44.31           C  
-ANISOU 9170  C   LEU D 873     5448   6158   5230     63    539     55       C  
-ATOM   9171  O   LEU D 873    -105.738  21.529 -30.743  1.00 43.74           O  
-ANISOU 9171  O   LEU D 873     5359   6048   5213     57    545    117       O  
-ATOM   9172  CB  LEU D 873    -106.941  18.505 -31.157  1.00 45.89           C  
-ANISOU 9172  CB  LEU D 873     5743   6322   5371     81    520   -139       C  
-ATOM   9173  CG  LEU D 873    -107.397  17.305 -30.310  1.00 43.18           C  
-ANISOU 9173  CG  LEU D 873     5475   5876   5056     49    502   -237       C  
-ATOM   9174  CD1 LEU D 873    -106.871  16.029 -30.955  1.00 46.14           C  
-ANISOU 9174  CD1 LEU D 873     5864   6281   5385    101    497   -318       C  
-ATOM   9175  CD2 LEU D 873    -106.911  17.408 -28.878  1.00 41.27           C  
-ANISOU 9175  CD2 LEU D 873     5270   5525   4887     11    501   -209       C  
-ATOM   9176  N   SER D 874    -107.221  21.447 -32.404  1.00 45.04           N  
-ANISOU 9176  N   SER D 874     5489   6359   5268     93    548     90       N  
-ATOM   9177  CA  SER D 874    -106.526  22.532 -33.084  1.00 45.88           C  
-ANISOU 9177  CA  SER D 874     5515   6538   5378    121    570    219       C  
-ATOM   9178  C   SER D 874    -106.782  23.886 -32.416  1.00 46.64           C  
-ANISOU 9178  C   SER D 874     5591   6554   5577     73    563    304       C  
-ATOM   9179  O   SER D 874    -105.893  24.736 -32.416  1.00 39.90           O  
-ANISOU 9179  O   SER D 874     4686   5694   4779     74    574    406       O  
-ATOM   9180  CB  SER D 874    -106.848  22.573 -34.569  1.00 47.34           C  
-ANISOU 9180  CB  SER D 874     5641   6884   5463    181    585    245       C  
-ATOM   9181  OG  SER D 874    -108.114  23.153 -34.766  1.00 50.07           O  
-ANISOU 9181  OG  SER D 874     5976   7240   5808    163    576    253       O  
-ATOM   9182  N   GLN D 875    -107.961  24.086 -31.807  1.00 43.97           N  
-ANISOU 9182  N   GLN D 875     5287   6148   5269     31    542    258       N  
-ATOM   9183  CA  GLN D 875    -108.278  25.399 -31.226  1.00 45.63           C  
-ANISOU 9183  CA  GLN D 875     5474   6287   5577     -5    529    327       C  
-ATOM   9184  C   GLN D 875    -108.505  25.448 -29.719  1.00 41.59           C  
-ANISOU 9184  C   GLN D 875     5014   5645   5144    -56    503    268       C  
-ATOM   9185  O   GLN D 875    -108.648  26.532 -29.168  1.00 39.75           O  
-ANISOU 9185  O   GLN D 875     4758   5348   4998    -80    486    311       O  
-ATOM   9186  CB  GLN D 875    -109.493  25.990 -31.922  1.00 50.16           C  
-ANISOU 9186  CB  GLN D 875     6018   6917   6123      3    527    352       C  
-ATOM   9187  CG  GLN D 875    -109.349  26.005 -33.430  1.00 56.01           C  
-ANISOU 9187  CG  GLN D 875     6698   7808   6775     62    554    415       C  
-ATOM   9188  CD  GLN D 875    -110.002  27.224 -34.037  1.00 66.48           C  
-ANISOU 9188  CD  GLN D 875     7962   9175   8122     74    558    518       C  
-ATOM   9189  OE1 GLN D 875    -111.006  27.141 -34.754  1.00 71.68           O  
-ANISOU 9189  OE1 GLN D 875     8608   9919   8707     97    558    499       O  
-ATOM   9190  NE2 GLN D 875    -109.438  28.385 -33.728  1.00 72.53           N  
-ANISOU 9190  NE2 GLN D 875     8687   9875   8998     56    558    628       N  
-ATOM   9191  N   GLY D 876    -108.531  24.296 -29.066  1.00 36.03           N  
-ANISOU 9191  N   GLY D 876     4373   4905   4410    -68    496    172       N  
-ATOM   9192  CA  GLY D 876    -108.736  24.249 -27.640  1.00 37.28           C  
-ANISOU 9192  CA  GLY D 876     4576   4962   4627   -108    475    121       C  
-ATOM   9193  C   GLY D 876    -110.207  24.387 -27.331  1.00 37.39           C  
-ANISOU 9193  C   GLY D 876     4608   4962   4635   -135    458     77       C  
-ATOM   9194  O   GLY D 876    -111.030  24.632 -28.211  1.00 36.43           O  
-ANISOU 9194  O   GLY D 876     4464   4902   4474   -125    462     90       O  
-ATOM   9195  N   LEU D 877    -110.542  24.200 -26.067  1.00 36.84           N  
-ANISOU 9195  N   LEU D 877     4577   4822   4598   -166    440     25       N  
-ATOM   9196  CA  LEU D 877    -111.907  24.408 -25.613  1.00 34.31           C  
-ANISOU 9196  CA  LEU D 877     4268   4491   4277   -192    424    -14       C  
-ATOM   9197  C   LEU D 877    -112.214  25.885 -25.650  1.00 34.72           C  
-ANISOU 9197  C   LEU D 877     4271   4532   4390   -189    407     39       C  
-ATOM   9198  O   LEU D 877    -111.376  26.715 -25.307  1.00 34.56           O  
-ANISOU 9198  O   LEU D 877     4220   4468   4443   -184    398     84       O  
-ATOM   9199  CB  LEU D 877    -112.082  23.875 -24.203  1.00 32.02           C  
-ANISOU 9199  CB  LEU D 877     4021   4142   4003   -218    411    -71       C  
-ATOM   9200  CG  LEU D 877    -111.962  22.373 -24.091  1.00 31.20           C  
-ANISOU 9200  CG  LEU D 877     3967   4035   3853   -224    425   -120       C  
-ATOM   9201  CD1 LEU D 877    -112.106  21.951 -22.638  1.00 31.46           C  
-ANISOU 9201  CD1 LEU D 877     4032   4017   3904   -246    415   -154       C  
-ATOM   9202  CD2 LEU D 877    -113.014  21.678 -24.958  1.00 32.94           C  
-ANISOU 9202  CD2 LEU D 877     4198   4302   4015   -233    431   -159       C  
-ATOM   9203  N   ARG D 878    -113.403  26.206 -26.123  1.00 35.06           N  
-ANISOU 9203  N   ARG D 878     4302   4614   4407   -191    403     35       N  
-ATOM   9204  CA  ARG D 878    -113.790  27.590 -26.330  1.00 37.67           C  
-ANISOU 9204  CA  ARG D 878     4583   4937   4794   -182    388     91       C  
-ATOM   9205  C   ARG D 878    -115.114  27.833 -25.650  1.00 33.58           C  
-ANISOU 9205  C   ARG D 878     4075   4407   4275   -199    365     37       C  
-ATOM   9206  O   ARG D 878    -115.762  26.926 -25.219  1.00 31.82           O  
-ANISOU 9206  O   ARG D 878     3891   4197   4001   -220    366    -30       O  
-ATOM   9207  CB  ARG D 878    -113.896  27.895 -27.826  1.00 40.24           C  
-ANISOU 9207  CB  ARG D 878     4866   5346   5079   -151    408    162       C  
-ATOM   9208  CG  ARG D 878    -112.565  28.104 -28.522  1.00 47.88           C  
-ANISOU 9208  CG  ARG D 878     5797   6331   6065   -127    429    246       C  
-ATOM   9209  CD  ARG D 878    -112.583  27.481 -29.920  1.00 54.30           C  
-ANISOU 9209  CD  ARG D 878     6593   7263   6776    -92    458    267       C  
-ATOM   9210  NE  ARG D 878    -112.720  26.022 -29.812  1.00 59.51           N  
-ANISOU 9210  NE  ARG D 878     7309   7944   7359    -99    463    166       N  
-ATOM   9211  CZ  ARG D 878    -113.302  25.203 -30.701  1.00 64.72           C  
-ANISOU 9211  CZ  ARG D 878     7973   8692   7924    -79    472    119       C  
-ATOM   9212  NH1 ARG D 878    -113.833  25.649 -31.833  1.00 67.28           N  
-ANISOU 9212  NH1 ARG D 878     8249   9116   8198    -45    480    163       N  
-ATOM   9213  NH2 ARG D 878    -113.355  23.901 -30.444  1.00 68.01           N  
-ANISOU 9213  NH2 ARG D 878     8441   9097   8301    -92    470     24       N  
-ATOM   9214  N   ILE D 879    -115.477  29.099 -25.559  1.00 34.85           N  
-ANISOU 9214  N   ILE D 879     4196   4542   4502   -189    343     72       N  
-ATOM   9215  CA  ILE D 879    -116.698  29.556 -24.931  1.00 34.42           C  
-ANISOU 9215  CA  ILE D 879     4141   4482   4456   -195    317     25       C  
-ATOM   9216  C   ILE D 879    -117.676  29.981 -26.049  1.00 38.60           C  
-ANISOU 9216  C   ILE D 879     4640   5078   4947   -177    323     63       C  
-ATOM   9217  O   ILE D 879    -117.264  30.508 -27.085  1.00 38.02           O  
-ANISOU 9217  O   ILE D 879     4530   5030   4888   -152    337    147       O  
-ATOM   9218  CB  ILE D 879    -116.380  30.759 -24.002  1.00 34.11           C  
-ANISOU 9218  CB  ILE D 879     4072   4358   4529   -188    279     27       C  
-ATOM   9219  CG1 ILE D 879    -115.558  30.292 -22.781  1.00 33.04           C  
-ANISOU 9219  CG1 ILE D 879     3963   4175   4415   -201    269    -26       C  
-ATOM   9220  CG2 ILE D 879    -117.646  31.478 -23.573  1.00 34.03           C  
-ANISOU 9220  CG2 ILE D 879     4047   4351   4533   -179    249    -10       C  
-ATOM   9221  CD1 ILE D 879    -115.003  31.440 -21.949  1.00 32.64           C  
-ANISOU 9221  CD1 ILE D 879     3875   4044   4481   -189    229    -32       C  
-ATOM   9222  N   ALA D 880    -118.963  29.718 -25.847  1.00 38.92           N  
-ANISOU 9222  N   ALA D 880     4693   5159   4935   -186    315      5       N  
-ATOM   9223  CA  ALA D 880    -119.997  30.064 -26.822  1.00 41.26           C  
-ANISOU 9223  CA  ALA D 880     4961   5530   5187   -167    319     28       C  
-ATOM   9224  C   ALA D 880    -119.928  31.526 -27.262  1.00 42.44           C  
-ANISOU 9224  C   ALA D 880     5056   5654   5413   -132    305    114       C  
-ATOM   9225  O   ALA D 880    -119.632  32.387 -26.437  1.00 40.65           O  
-ANISOU 9225  O   ALA D 880     4818   5343   5285   -129    276    117       O  
-ATOM   9226  CB  ALA D 880    -121.362  29.764 -26.226  1.00 39.51           C  
-ANISOU 9226  CB  ALA D 880     4754   5338   4920   -185    304    -50       C  
-ATOM   9227  N   PRO D 881    -120.219  31.803 -28.554  1.00 43.57           N  
-ANISOU 9227  N   PRO D 881     5164   5874   5517   -101    322    183       N  
-ATOM   9228  CA  PRO D 881    -120.127  33.180 -29.020  1.00 46.96           C  
-ANISOU 9228  CA  PRO D 881     5537   6276   6028    -66    312    284       C  
-ATOM   9229  C   PRO D 881    -121.229  34.073 -28.467  1.00 45.82           C  
-ANISOU 9229  C   PRO D 881     5379   6101   5930    -54    276    257       C  
-ATOM   9230  O   PRO D 881    -122.287  33.588 -28.084  1.00 47.88           O  
-ANISOU 9230  O   PRO D 881     5663   6406   6124    -65    268    172       O  
-ATOM   9231  CB  PRO D 881    -120.210  33.067 -30.562  1.00 47.68           C  
-ANISOU 9231  CB  PRO D 881     5592   6485   6039    -30    345    365       C  
-ATOM   9232  CG  PRO D 881    -120.817  31.742 -30.851  1.00 48.16           C  
-ANISOU 9232  CG  PRO D 881     5688   6641   5971    -43    360    274       C  
-ATOM   9233  CD  PRO D 881    -120.589  30.866 -29.634  1.00 47.33           C  
-ANISOU 9233  CD  PRO D 881     5643   6467   5875    -92    350    172       C  
-ATOM   9234  N   PRO D 882    -120.986  35.382 -28.437  1.00 49.38           N  
-ANISOU 9234  N   PRO D 882     5787   6476   6500    -30    254    329       N  
-ATOM   9235  CA  PRO D 882    -122.015  36.383 -28.055  1.00 50.07           C  
-ANISOU 9235  CA  PRO D 882     5851   6531   6642     -5    216    312       C  
-ATOM   9236  C   PRO D 882    -123.402  36.196 -28.733  1.00 48.41           C  
-ANISOU 9236  C   PRO D 882     5632   6437   6323     18    225    298       C  
-ATOM   9237  O   PRO D 882    -124.432  36.369 -28.093  1.00 45.68           O  
-ANISOU 9237  O   PRO D 882     5293   6096   5966     23    198    223       O  
-ATOM   9238  CB  PRO D 882    -121.396  37.717 -28.502  1.00 51.09           C  
-ANISOU 9238  CB  PRO D 882     5923   6579   6911     23    204    435       C  
-ATOM   9239  CG  PRO D 882    -119.931  37.463 -28.632  1.00 50.95           C  
-ANISOU 9239  CG  PRO D 882     5903   6521   6935      0    225    491       C  
-ATOM   9240  CD  PRO D 882    -119.738  36.001 -28.921  1.00 49.55           C  
-ANISOU 9240  CD  PRO D 882     5771   6443   6615    -22    264    444       C  
-ATOM   9241  N   GLU D 883    -123.408  35.823 -30.012  1.00 50.33           N  
-ANISOU 9241  N   GLU D 883     5857   6784   6482     36    262    366       N  
-ATOM   9242  CA  GLU D 883    -124.646  35.652 -30.790  1.00 52.50           C  
-ANISOU 9242  CA  GLU D 883     6115   7184   6650     63    270    357       C  
-ATOM   9243  C   GLU D 883    -125.488  34.447 -30.354  1.00 53.39           C  
-ANISOU 9243  C   GLU D 883     6271   7363   6653     27    271    225       C  
-ATOM   9244  O   GLU D 883    -126.702  34.396 -30.619  1.00 55.94           O  
-ANISOU 9244  O   GLU D 883     6581   7769   6906     42    265    189       O  
-ATOM   9245  CB  GLU D 883    -124.328  35.474 -32.269  1.00 57.20           C  
-ANISOU 9245  CB  GLU D 883     6673   7889   7172     98    308    455       C  
-ATOM   9246  CG  GLU D 883    -123.578  36.631 -32.908  1.00 62.24           C  
-ANISOU 9246  CG  GLU D 883     7255   8487   7907    136    316    613       C  
-ATOM   9247  CD  GLU D 883    -122.057  36.558 -32.772  1.00 66.58           C  
-ANISOU 9247  CD  GLU D 883     7807   8962   8529    113    330    667       C  
-ATOM   9248  OE1 GLU D 883    -121.418  37.600 -33.041  1.00 68.85           O  
-ANISOU 9248  OE1 GLU D 883     8046   9184   8930    132    329    794       O  
-ATOM   9249  OE2 GLU D 883    -121.502  35.483 -32.422  1.00 63.43           O  
-ANISOU 9249  OE2 GLU D 883     7454   8568   8079     76    342    590       O  
-ATOM   9250  N   ALA D 884    -124.860  33.478 -29.686  1.00 52.55           N  
-ANISOU 9250  N   ALA D 884     6212   7220   6536    -20    279    159       N  
-ATOM   9251  CA  ALA D 884    -125.577  32.294 -29.233  1.00 51.90           C  
-ANISOU 9251  CA  ALA D 884     6167   7185   6368    -60    281     48       C  
-ATOM   9252  C   ALA D 884    -126.507  32.639 -28.081  1.00 51.07           C  
-ANISOU 9252  C   ALA D 884     6068   7049   6287    -71    250    -22       C  
-ATOM   9253  O   ALA D 884    -126.168  33.455 -27.226  1.00 50.44           O  
-ANISOU 9253  O   ALA D 884     5985   6878   6300    -62    224    -17       O  
-ATOM   9254  CB  ALA D 884    -124.605  31.215 -28.799  1.00 52.55           C  
-ANISOU 9254  CB  ALA D 884     6295   7227   6444   -102    297     10       C  
-ATOM   9255  N   PRO D 885    -127.692  32.017 -28.057  1.00 51.55           N  
-ANISOU 9255  N   PRO D 885     6131   7192   6265    -88    250    -92       N  
-ATOM   9256  CA  PRO D 885    -128.545  32.176 -26.885  1.00 50.39           C  
-ANISOU 9256  CA  PRO D 885     5987   7031   6127   -101    224   -161       C  
-ATOM   9257  C   PRO D 885    -127.869  31.636 -25.644  1.00 45.52           C  
-ANISOU 9257  C   PRO D 885     5409   6340   5545   -139    221   -207       C  
-ATOM   9258  O   PRO D 885    -127.144  30.659 -25.724  1.00 45.52           O  
-ANISOU 9258  O   PRO D 885     5441   6327   5526   -173    244   -212       O  
-ATOM   9259  CB  PRO D 885    -129.809  31.349 -27.213  1.00 51.65           C  
-ANISOU 9259  CB  PRO D 885     6139   7301   6185   -124    232   -221       C  
-ATOM   9260  CG  PRO D 885    -129.630  30.801 -28.575  1.00 55.06           C  
-ANISOU 9260  CG  PRO D 885     6563   7803   6556   -119    257   -194       C  
-ATOM   9261  CD  PRO D 885    -128.232  31.062 -29.040  1.00 54.46           C  
-ANISOU 9261  CD  PRO D 885     6494   7668   6528    -99    271   -117       C  
-ATOM   9262  N   VAL D 886    -128.125  32.282 -24.518  1.00 45.74           N  
-ANISOU 9262  N   VAL D 886     5430   6329   5621   -127    192   -242       N  
-ATOM   9263  CA  VAL D 886    -127.614  31.850 -23.235  1.00 46.70           C  
-ANISOU 9263  CA  VAL D 886     5578   6401   5764   -152    186   -289       C  
-ATOM   9264  C   VAL D 886    -128.464  30.695 -22.672  1.00 48.11           C  
-ANISOU 9264  C   VAL D 886     5771   6649   5860   -197    200   -349       C  
-ATOM   9265  O   VAL D 886    -128.040  29.996 -21.761  1.00 41.05           O  
-ANISOU 9265  O   VAL D 886     4902   5732   4964   -226    207   -376       O  
-ATOM   9266  CB  VAL D 886    -127.600  33.022 -22.237  1.00 48.24           C  
-ANISOU 9266  CB  VAL D 886     5749   6542   6037   -111    143   -314       C  
-ATOM   9267  CG1 VAL D 886    -129.021  33.456 -21.875  1.00 47.91           C  
-ANISOU 9267  CG1 VAL D 886     5676   6571   5958    -86    120   -362       C  
-ATOM   9268  CG2 VAL D 886    -126.835  32.626 -20.975  1.00 50.95           C  
-ANISOU 9268  CG2 VAL D 886     6115   6840   6404   -127    136   -356       C  
-ATOM   9269  N   THR D 887    -129.676  30.513 -23.218  1.00 49.92           N  
-ANISOU 9269  N   THR D 887     5978   6965   6023   -203    204   -366       N  
-ATOM   9270  CA  THR D 887    -130.632  29.484 -22.765  1.00 46.12           C  
-ANISOU 9270  CA  THR D 887     5498   6554   5473   -250    216   -417       C  
-ATOM   9271  C   THR D 887    -129.974  28.123 -22.734  1.00 40.83           C  
-ANISOU 9271  C   THR D 887     4868   5855   4789   -306    245   -420       C  
-ATOM   9272  O   THR D 887    -129.265  27.723 -23.653  1.00 42.24           O  
-ANISOU 9272  O   THR D 887     5066   6012   4971   -312    261   -395       O  
-ATOM   9273  CB  THR D 887    -131.865  29.385 -23.687  1.00 51.60           C  
-ANISOU 9273  CB  THR D 887     6160   7343   6102   -252    219   -430       C  
-ATOM   9274  OG1 THR D 887    -132.873  28.525 -23.118  1.00 50.67           O  
-ANISOU 9274  OG1 THR D 887     6031   7291   5931   -300    226   -478       O  
-ATOM   9275  CG2 THR D 887    -131.494  28.827 -25.063  1.00 53.33           C  
-ANISOU 9275  CG2 THR D 887     6389   7579   6297   -262    240   -406       C  
-ATOM   9276  N   GLY D 888    -130.194  27.428 -21.644  1.00 37.16           N  
-ANISOU 9276  N   GLY D 888     4411   5396   4311   -341    250   -448       N  
-ATOM   9277  CA  GLY D 888    -129.564  26.143 -21.434  1.00 35.86           C  
-ANISOU 9277  CA  GLY D 888     4284   5193   4147   -391    275   -446       C  
-ATOM   9278  C   GLY D 888    -128.251  26.223 -20.681  1.00 34.34           C  
-ANISOU 9278  C   GLY D 888     4122   4921   4004   -377    276   -425       C  
-ATOM   9279  O   GLY D 888    -127.861  25.232 -20.102  1.00 36.18           O  
-ANISOU 9279  O   GLY D 888     4380   5130   4236   -412    293   -424       O  
-ATOM   9280  N   TYR D 889    -127.575  27.383 -20.693  1.00 34.72           N  
-ANISOU 9280  N   TYR D 889     4163   4928   4100   -326    255   -408       N  
-ATOM   9281  CA  TYR D 889    -126.365  27.599 -19.865  1.00 36.31           C  
-ANISOU 9281  CA  TYR D 889     4383   5061   4353   -308    248   -398       C  
-ATOM   9282  C   TYR D 889    -126.693  27.986 -18.419  1.00 36.15           C  
-ANISOU 9282  C   TYR D 889     4340   5064   4332   -287    226   -434       C  
-ATOM   9283  O   TYR D 889    -126.948  29.142 -18.090  1.00 37.09           O  
-ANISOU 9283  O   TYR D 889     4426   5187   4479   -240    193   -456       O  
-ATOM   9284  CB  TYR D 889    -125.473  28.682 -20.447  1.00 37.88           C  
-ANISOU 9284  CB  TYR D 889     4575   5200   4619   -266    232   -365       C  
-ATOM   9285  CG  TYR D 889    -124.698  28.210 -21.638  1.00 37.50           C  
-ANISOU 9285  CG  TYR D 889     4548   5127   4571   -279    257   -322       C  
-ATOM   9286  CD1 TYR D 889    -125.162  28.404 -22.937  1.00 38.49           C  
-ANISOU 9286  CD1 TYR D 889     4658   5295   4672   -270    264   -297       C  
-ATOM   9287  CD2 TYR D 889    -123.511  27.505 -21.455  1.00 39.71           C  
-ANISOU 9287  CD2 TYR D 889     4863   5357   4869   -294    273   -308       C  
-ATOM   9288  CE1 TYR D 889    -124.431  27.940 -24.032  1.00 38.51           C  
-ANISOU 9288  CE1 TYR D 889     4674   5295   4663   -272    287   -262       C  
-ATOM   9289  CE2 TYR D 889    -122.777  27.038 -22.531  1.00 36.65           C  
-ANISOU 9289  CE2 TYR D 889     4492   4959   4475   -298    295   -275       C  
-ATOM   9290  CZ  TYR D 889    -123.234  27.257 -23.824  1.00 37.93           C  
-ANISOU 9290  CZ  TYR D 889     4633   5169   4608   -286    302   -253       C  
-ATOM   9291  OH  TYR D 889    -122.482  26.764 -24.878  1.00 40.48           O  
-ANISOU 9291  OH  TYR D 889     4967   5500   4915   -281    323   -224       O  
-ATOM   9292  N   MET D 890    -126.706  26.982 -17.579  1.00 33.07           N  
-ANISOU 9292  N   MET D 890     3963   4694   3908   -318    245   -440       N  
-ATOM   9293  CA  MET D 890    -127.108  27.124 -16.200  1.00 35.16           C  
-ANISOU 9293  CA  MET D 890     4200   5011   4149   -298    231   -469       C  
-ATOM   9294  C   MET D 890    -126.285  28.161 -15.454  1.00 31.24           C  
-ANISOU 9294  C   MET D 890     3690   4479   3703   -239    196   -495       C  
-ATOM   9295  O   MET D 890    -126.811  28.847 -14.591  1.00 29.85           O  
-ANISOU 9295  O   MET D 890     3473   4354   3514   -197    167   -539       O  
-ATOM   9296  CB  MET D 890    -126.969  25.749 -15.535  1.00 38.49           C  
-ANISOU 9296  CB  MET D 890     4642   5446   4536   -343    265   -446       C  
-ATOM   9297  CG  MET D 890    -127.439  25.718 -14.120  1.00 43.35           C  
-ANISOU 9297  CG  MET D 890     5221   6140   5108   -323    259   -460       C  
-ATOM   9298  SD  MET D 890    -127.664  24.038 -13.503  1.00 45.66           S  
-ANISOU 9298  SD  MET D 890     5526   6463   5362   -386    305   -408       S  
-ATOM   9299  CE  MET D 890    -128.271  24.444 -11.865  1.00 44.57           C  
-ANISOU 9299  CE  MET D 890     5325   6449   5162   -336    291   -425       C  
-ATOM   9300  N   PHE D 891    -124.994  28.258 -15.770  1.00 28.95           N  
-ANISOU 9300  N   PHE D 891     3426   4105   3470   -234    196   -474       N  
-ATOM   9301  CA  PHE D 891    -124.119  29.211 -15.096  1.00 29.78           C  
-ANISOU 9301  CA  PHE D 891     3513   4165   3636   -184    159   -503       C  
-ATOM   9302  C   PHE D 891    -123.491  30.211 -16.054  1.00 29.66           C  
-ANISOU 9302  C   PHE D 891     3495   4068   3708   -166    140   -482       C  
-ATOM   9303  O   PHE D 891    -122.399  30.716 -15.813  1.00 27.22           O  
-ANISOU 9303  O   PHE D 891     3181   3693   3467   -145    120   -485       O  
-ATOM   9304  CB  PHE D 891    -123.074  28.457 -14.293  1.00 29.78           C  
-ANISOU 9304  CB  PHE D 891     3535   4149   3631   -190    173   -496       C  
-ATOM   9305  CG  PHE D 891    -123.682  27.570 -13.247  1.00 32.25           C  
-ANISOU 9305  CG  PHE D 891     3841   4548   3865   -200    192   -502       C  
-ATOM   9306  CD1 PHE D 891    -124.291  28.137 -12.132  1.00 32.27           C  
-ANISOU 9306  CD1 PHE D 891     3794   4629   3836   -153    163   -554       C  
-ATOM   9307  CD2 PHE D 891    -123.688  26.185 -13.381  1.00 31.14           C  
-ANISOU 9307  CD2 PHE D 891     3735   4413   3684   -253    237   -454       C  
-ATOM   9308  CE1 PHE D 891    -124.871  27.339 -11.156  1.00 33.27           C  
-ANISOU 9308  CE1 PHE D 891     3904   4852   3884   -159    183   -546       C  
-ATOM   9309  CE2 PHE D 891    -124.255  25.379 -12.398  1.00 33.40           C  
-ANISOU 9309  CE2 PHE D 891     4007   4776   3907   -264    256   -442       C  
-ATOM   9310  CZ  PHE D 891    -124.849  25.963 -11.283  1.00 32.75           C  
-ANISOU 9310  CZ  PHE D 891     3872   4785   3786   -217    232   -482       C  
-ATOM   9311  N   GLY D 892    -124.180  30.476 -17.163  1.00 28.84           N  
-ANISOU 9311  N   GLY D 892     3387   3972   3599   -175    147   -455       N  
-ATOM   9312  CA  GLY D 892    -123.654  31.374 -18.167  1.00 29.30           C  
-ANISOU 9312  CA  GLY D 892     3436   3963   3734   -158    135   -413       C  
-ATOM   9313  C   GLY D 892    -122.713  30.699 -19.137  1.00 30.31           C  
-ANISOU 9313  C   GLY D 892     3597   4056   3864   -189    172   -351       C  
-ATOM   9314  O   GLY D 892    -122.394  29.505 -19.038  1.00 29.99           O  
-ANISOU 9314  O   GLY D 892     3592   4029   3774   -223    203   -347       O  
-ATOM   9315  N   LYS D 893    -122.307  31.483 -20.127  1.00 33.33           N  
-ANISOU 9315  N   LYS D 893     3963   4395   4306   -173    167   -298       N  
-ATOM   9316  CA  LYS D 893    -121.407  31.033 -21.161  1.00 35.18           C  
-ANISOU 9316  CA  LYS D 893     4215   4610   4542   -190    199   -233       C  
-ATOM   9317  C   LYS D 893    -120.025  30.864 -20.563  1.00 33.87           C  
-ANISOU 9317  C   LYS D 893     4063   4382   4425   -193    198   -231       C  
-ATOM   9318  O   LYS D 893    -119.422  31.811 -20.145  1.00 35.53           O  
-ANISOU 9318  O   LYS D 893     4245   4531   4723   -170    167   -231       O  
-ATOM   9319  CB  LYS D 893    -121.406  32.019 -22.334  1.00 37.78           C  
-ANISOU 9319  CB  LYS D 893     4510   4925   4919   -165    196   -163       C  
-ATOM   9320  CG  LYS D 893    -122.716  32.044 -23.105  1.00 38.74           C  
-ANISOU 9320  CG  LYS D 893     4620   5124   4977   -158    203   -159       C  
-ATOM   9321  CD  LYS D 893    -122.713  33.143 -24.167  1.00 42.63           C  
-ANISOU 9321  CD  LYS D 893     5071   5605   5523   -123    197    -79       C  
-ATOM   9322  CE  LYS D 893    -124.074  33.313 -24.835  1.00 45.19           C  
-ANISOU 9322  CE  LYS D 893     5375   6012   5785   -107    198    -79       C  
-ATOM   9323  NZ  LYS D 893    -123.932  34.117 -26.070  1.00 50.71           N  
-ANISOU 9323  NZ  LYS D 893     6035   6718   6514    -73    205     20       N  
-ATOM   9324  N   GLY D 894    -119.548  29.632 -20.524  1.00 32.24           N  
-ANISOU 9324  N   GLY D 894     3895   4190   4163   -220    229   -233       N  
-ATOM   9325  CA  GLY D 894    -118.234  29.331 -20.018  1.00 30.23           C  
-ANISOU 9325  CA  GLY D 894     3656   3888   3942   -222    232   -229       C  
-ATOM   9326  C   GLY D 894    -117.840  27.953 -20.516  1.00 29.10           C  
-ANISOU 9326  C   GLY D 894     3555   3766   3734   -248    273   -213       C  
-ATOM   9327  O   GLY D 894    -118.530  27.386 -21.362  1.00 27.85           O  
-ANISOU 9327  O   GLY D 894     3409   3653   3519   -263    293   -207       O  
-ATOM   9328  N   ILE D 895    -116.743  27.410 -19.990  1.00 27.70           N  
-ANISOU 9328  N   ILE D 895     3399   3558   3568   -250    280   -214       N  
-ATOM   9329  CA  ILE D 895    -116.349  26.054 -20.290  1.00 28.94           C  
-ANISOU 9329  CA  ILE D 895     3598   3725   3672   -270    314   -210       C  
-ATOM   9330  C   ILE D 895    -116.695  25.239 -19.092  1.00 27.87           C  
-ANISOU 9330  C   ILE D 895     3487   3600   3503   -284    315   -250       C  
-ATOM   9331  O   ILE D 895    -116.262  25.559 -17.987  1.00 29.17           O  
-ANISOU 9331  O   ILE D 895     3640   3749   3692   -267    297   -269       O  
-ATOM   9332  CB  ILE D 895    -114.853  25.928 -20.574  1.00 30.49           C  
-ANISOU 9332  CB  ILE D 895     3800   3886   3900   -257    324   -175       C  
-ATOM   9333  CG1 ILE D 895    -114.442  26.910 -21.663  1.00 33.15           C  
-ANISOU 9333  CG1 ILE D 895     4098   4217   4281   -240    322   -118       C  
-ATOM   9334  CG2 ILE D 895    -114.512  24.515 -21.051  1.00 29.67           C  
-ANISOU 9334  CG2 ILE D 895     3739   3794   3741   -270    356   -176       C  
-ATOM   9335  CD1 ILE D 895    -112.933  27.072 -21.774  1.00 34.37           C  
-ANISOU 9335  CD1 ILE D 895     4241   4337   4483   -227    327    -78       C  
-ATOM   9336  N   TYR D 896    -117.442  24.160 -19.329  1.00 26.93           N  
-ANISOU 9336  N   TYR D 896     3394   3509   3329   -314    337   -261       N  
-ATOM   9337  CA  TYR D 896    -118.021  23.328 -18.295  1.00 26.75           C  
-ANISOU 9337  CA  TYR D 896     3387   3503   3273   -334    343   -283       C  
-ATOM   9338  C   TYR D 896    -117.259  21.997 -18.173  1.00 27.64           C  
-ANISOU 9338  C   TYR D 896     3542   3585   3376   -348    368   -270       C  
-ATOM   9339  O   TYR D 896    -116.918  21.360 -19.196  1.00 29.50           O  
-ANISOU 9339  O   TYR D 896     3799   3802   3606   -356    384   -264       O  
-ATOM   9340  CB  TYR D 896    -119.495  23.031 -18.649  1.00 27.92           C  
-ANISOU 9340  CB  TYR D 896     3528   3698   3382   -365    348   -300       C  
-ATOM   9341  CG  TYR D 896    -120.444  24.184 -18.431  1.00 27.21           C  
-ANISOU 9341  CG  TYR D 896     3397   3649   3292   -349    323   -317       C  
-ATOM   9342  CD1 TYR D 896    -120.338  25.346 -19.183  1.00 27.66           C  
-ANISOU 9342  CD1 TYR D 896     3429   3699   3382   -322    305   -307       C  
-ATOM   9343  CD2 TYR D 896    -121.440  24.119 -17.471  1.00 26.08           C  
-ANISOU 9343  CD2 TYR D 896     3236   3555   3120   -358    317   -339       C  
-ATOM   9344  CE1 TYR D 896    -121.205  26.404 -18.986  1.00 27.80           C  
-ANISOU 9344  CE1 TYR D 896     3409   3745   3408   -303    279   -325       C  
-ATOM   9345  CE2 TYR D 896    -122.307  25.179 -17.274  1.00 27.95           C  
-ANISOU 9345  CE2 TYR D 896     3433   3832   3354   -336    291   -363       C  
-ATOM   9346  CZ  TYR D 896    -122.187  26.314 -18.040  1.00 27.98           C  
-ANISOU 9346  CZ  TYR D 896     3417   3817   3396   -308    271   -359       C  
-ATOM   9347  OH  TYR D 896    -123.007  27.384 -17.830  1.00 32.27           O  
-ANISOU 9347  OH  TYR D 896     3921   4392   3948   -280    242   -384       O  
-ATOM   9348  N   PHE D 897    -117.041  21.559 -16.932  1.00 26.36           N  
-ANISOU 9348  N   PHE D 897     3386   3422   3208   -344    370   -269       N  
-ATOM   9349  CA  PHE D 897    -116.319  20.324 -16.604  1.00 25.64           C  
-ANISOU 9349  CA  PHE D 897     3332   3298   3113   -350    392   -250       C  
-ATOM   9350  C   PHE D 897    -117.021  19.590 -15.482  1.00 26.75           C  
-ANISOU 9350  C   PHE D 897     3472   3465   3228   -368    402   -238       C  
-ATOM   9351  O   PHE D 897    -117.694  20.205 -14.660  1.00 24.09           O  
-ANISOU 9351  O   PHE D 897     3101   3180   2872   -359    389   -247       O  
-ATOM   9352  CB  PHE D 897    -114.909  20.606 -16.109  1.00 26.31           C  
-ANISOU 9352  CB  PHE D 897     3417   3358   3220   -311    386   -240       C  
-ATOM   9353  CG  PHE D 897    -114.031  21.332 -17.100  1.00 27.74           C  
-ANISOU 9353  CG  PHE D 897     3590   3515   3433   -292    378   -235       C  
-ATOM   9354  CD1 PHE D 897    -114.043  22.711 -17.170  1.00 28.11           C  
-ANISOU 9354  CD1 PHE D 897     3597   3570   3513   -274    353   -243       C  
-ATOM   9355  CD2 PHE D 897    -113.169  20.622 -17.923  1.00 28.23           C  
-ANISOU 9355  CD2 PHE D 897     3680   3548   3497   -289    396   -220       C  
-ATOM   9356  CE1 PHE D 897    -113.243  23.375 -18.085  1.00 30.75           C  
-ANISOU 9356  CE1 PHE D 897     3915   3882   3884   -260    349   -221       C  
-ATOM   9357  CE2 PHE D 897    -112.363  21.261 -18.827  1.00 29.40           C  
-ANISOU 9357  CE2 PHE D 897     3812   3690   3668   -269    394   -205       C  
-ATOM   9358  CZ  PHE D 897    -112.394  22.648 -18.909  1.00 32.34           C  
-ANISOU 9358  CZ  PHE D 897     4142   4070   4077   -258    372   -198       C  
-ATOM   9359  N   ALA D 898    -116.820  18.272 -15.430  1.00 27.84           N  
-ANISOU 9359  N   ALA D 898     3643   3566   3369   -390    426   -214       N  
-ATOM   9360  CA  ALA D 898    -117.373  17.431 -14.367  1.00 28.87           C  
-ANISOU 9360  CA  ALA D 898     3770   3714   3484   -409    441   -180       C  
-ATOM   9361  C   ALA D 898    -116.257  16.726 -13.611  1.00 28.87           C  
-ANISOU 9361  C   ALA D 898     3793   3686   3491   -382    455   -144       C  
-ATOM   9362  O   ALA D 898    -115.166  16.534 -14.157  1.00 29.96           O  
-ANISOU 9362  O   ALA D 898     3959   3773   3651   -362    455   -149       O  
-ATOM   9363  CB  ALA D 898    -118.275  16.380 -14.985  1.00 29.81           C  
-ANISOU 9363  CB  ALA D 898     3905   3804   3617   -466    457   -176       C  
-ATOM   9364  N   ASP D 899    -116.518  16.377 -12.362  1.00 27.45           N  
-ANISOU 9364  N   ASP D 899     3594   3548   3287   -375    465   -103       N  
-ATOM   9365  CA  ASP D 899    -115.645  15.474 -11.629  1.00 31.43           C  
-ANISOU 9365  CA  ASP D 899     4118   4028   3795   -352    483    -53       C  
-ATOM   9366  C   ASP D 899    -116.165  14.026 -11.639  1.00 32.66           C  
-ANISOU 9366  C   ASP D 899     4296   4132   3980   -400    510      1       C  
-ATOM   9367  O   ASP D 899    -115.496  13.125 -11.105  1.00 34.95           O  
-ANISOU 9367  O   ASP D 899     4606   4389   4286   -384    528     53       O  
-ATOM   9368  CB  ASP D 899    -115.335  15.945 -10.176  1.00 31.47           C  
-ANISOU 9368  CB  ASP D 899     4085   4119   3755   -299    478    -33       C  
-ATOM   9369  CG  ASP D 899    -116.562  16.172  -9.324  1.00 33.10           C  
-ANISOU 9369  CG  ASP D 899     4242   4418   3916   -307    480    -16       C  
-ATOM   9370  OD1 ASP D 899    -117.650  15.587  -9.599  1.00 35.88           O  
-ANISOU 9370  OD1 ASP D 899     4593   4763   4278   -362    497     11       O  
-ATOM   9371  OD2 ASP D 899    -116.431  16.930  -8.335  1.00 31.22           O  
-ANISOU 9371  OD2 ASP D 899     3961   4269   3632   -255    464    -32       O  
-ATOM   9372  N   MET D 900    -117.326  13.814 -12.254  1.00 33.45           N  
-ANISOU 9372  N   MET D 900     4390   4223   4096   -456    512    -12       N  
-ATOM   9373  CA  MET D 900    -117.855  12.467 -12.483  1.00 34.66           C  
-ANISOU 9373  CA  MET D 900     4560   4308   4301   -511    530     24       C  
-ATOM   9374  C   MET D 900    -117.741  12.143 -13.963  1.00 34.30           C  
-ANISOU 9374  C   MET D 900     4549   4184   4298   -535    518    -39       C  
-ATOM   9375  O   MET D 900    -118.374  12.800 -14.795  1.00 32.68           O  
-ANISOU 9375  O   MET D 900     4331   4007   4079   -552    503    -95       O  
-ATOM   9376  CB  MET D 900    -119.326  12.385 -12.047  1.00 37.65           C  
-ANISOU 9376  CB  MET D 900     4895   4742   4668   -561    539     54       C  
-ATOM   9377  CG  MET D 900    -119.589  12.744 -10.582  1.00 43.64           C  
-ANISOU 9377  CG  MET D 900     5606   5606   5368   -531    551    114       C  
-ATOM   9378  SD  MET D 900    -119.062  11.460  -9.475  1.00 49.60           S  
-ANISOU 9378  SD  MET D 900     6366   6336   6146   -521    584    230       S  
-ATOM   9379  CE  MET D 900    -119.625  12.041  -7.891  1.00 59.12           C  
-ANISOU 9379  CE  MET D 900     7497   7705   7259   -481    595    290       C  
-ATOM   9380  N   VAL D 901    -116.993  11.095 -14.298  1.00 35.08           N  
-ANISOU 9380  N   VAL D 901     4689   4193   4449   -533    524    -32       N  
-ATOM   9381  CA  VAL D 901    -116.751  10.746 -15.697  1.00 34.87           C  
-ANISOU 9381  CA  VAL D 901     4690   4103   4455   -541    509   -103       C  
-ATOM   9382  C   VAL D 901    -118.029  10.621 -16.523  1.00 36.43           C  
-ANISOU 9382  C   VAL D 901     4870   4302   4671   -599    498   -150       C  
-ATOM   9383  O   VAL D 901    -118.084  11.067 -17.661  1.00 40.27           O  
-ANISOU 9383  O   VAL D 901     5356   4804   5140   -592    482   -220       O  
-ATOM   9384  CB  VAL D 901    -115.889   9.478 -15.837  1.00 37.32           C  
-ANISOU 9384  CB  VAL D 901     5043   4312   4826   -529    514    -92       C  
-ATOM   9385  CG1 VAL D 901    -116.605   8.227 -15.342  1.00 38.87           C  
-ANISOU 9385  CG1 VAL D 901     5238   4438   5095   -583    526    -40       C  
-ATOM   9386  CG2 VAL D 901    -115.447   9.274 -17.274  1.00 37.84           C  
-ANISOU 9386  CG2 VAL D 901     5133   4338   4909   -515    495   -177       C  
-ATOM   9387  N   SER D 902    -119.069  10.039 -15.951  1.00 37.53           N  
-ANISOU 9387  N   SER D 902     4986   4435   4840   -654    508   -109       N  
-ATOM   9388  CA  SER D 902    -120.303   9.788 -16.692  1.00 37.84           C  
-ANISOU 9388  CA  SER D 902     5002   4471   4905   -715    497   -155       C  
-ATOM   9389  C   SER D 902    -121.064  11.061 -17.023  1.00 34.18           C  
-ANISOU 9389  C   SER D 902     4503   4110   4372   -712    486   -193       C  
-ATOM   9390  O   SER D 902    -121.667  11.164 -18.081  1.00 36.94           O  
-ANISOU 9390  O   SER D 902     4843   4471   4722   -733    469   -261       O  
-ATOM   9391  CB  SER D 902    -121.192   8.791 -15.927  1.00 39.85           C  
-ANISOU 9391  CB  SER D 902     5234   4688   5221   -779    512    -88       C  
-ATOM   9392  OG  SER D 902    -121.556   9.273 -14.651  1.00 40.36           O  
-ANISOU 9392  OG  SER D 902     5263   4834   5237   -774    534     -5       O  
-ATOM   9393  N   LYS D 903    -121.016  12.046 -16.142  1.00 34.52           N  
-ANISOU 9393  N   LYS D 903     4526   4233   4357   -680    493   -155       N  
-ATOM   9394  CA  LYS D 903    -121.657  13.343 -16.416  1.00 33.16           C  
-ANISOU 9394  CA  LYS D 903     4320   4151   4126   -667    479   -191       C  
-ATOM   9395  C   LYS D 903    -121.083  13.956 -17.689  1.00 32.67           C  
-ANISOU 9395  C   LYS D 903     4277   4086   4051   -633    461   -256       C  
-ATOM   9396  O   LYS D 903    -121.832  14.467 -18.520  1.00 34.42           O  
-ANISOU 9396  O   LYS D 903     4476   4349   4251   -644    448   -301       O  
-ATOM   9397  CB  LYS D 903    -121.491  14.303 -15.239  1.00 31.67           C  
-ANISOU 9397  CB  LYS D 903     4108   4038   3886   -625    482   -152       C  
-ATOM   9398  CG  LYS D 903    -122.205  15.629 -15.445  1.00 31.50           C  
-ANISOU 9398  CG  LYS D 903     4050   4101   3818   -609    464   -191       C  
-ATOM   9399  CD  LYS D 903    -122.475  16.344 -14.116  1.00 31.05           C  
-ANISOU 9399  CD  LYS D 903     3954   4127   3715   -579    464   -160       C  
-ATOM   9400  CE  LYS D 903    -123.298  17.605 -14.322  1.00 31.10           C  
-ANISOU 9400  CE  LYS D 903     3922   4210   3684   -563    442   -203       C  
-ATOM   9401  NZ  LYS D 903    -123.381  18.433 -13.084  1.00 34.72           N  
-ANISOU 9401  NZ  LYS D 903     4341   4751   4099   -516    433   -195       N  
-ATOM   9402  N   SER D 904    -119.765  13.862 -17.857  1.00 30.56           N  
-ANISOU 9402  N   SER D 904     4043   3775   3793   -591    462   -254       N  
-ATOM   9403  CA  SER D 904    -119.111  14.334 -19.065  1.00 32.53           C  
-ANISOU 9403  CA  SER D 904     4304   4026   4029   -556    450   -302       C  
-ATOM   9404  C   SER D 904    -119.262  13.378 -20.246  1.00 32.99           C  
-ANISOU 9404  C   SER D 904     4377   4043   4114   -576    443   -358       C  
-ATOM   9405  O   SER D 904    -119.501  13.820 -21.356  1.00 33.26           O  
-ANISOU 9405  O   SER D 904     4397   4119   4122   -564    430   -406       O  
-ATOM   9406  CB  SER D 904    -117.625  14.630 -18.817  1.00 33.24           C  
-ANISOU 9406  CB  SER D 904     4416   4096   4117   -501    454   -279       C  
-ATOM   9407  OG  SER D 904    -117.483  15.856 -18.122  1.00 31.07           O  
-ANISOU 9407  OG  SER D 904     4116   3873   3815   -473    449   -256       O  
-ATOM   9408  N   ALA D 905    -119.161  12.079 -19.993  1.00 34.37           N  
-ANISOU 9408  N   ALA D 905     4576   4140   4345   -602    448   -353       N  
-ATOM   9409  CA  ALA D 905    -119.331  11.076 -21.047  1.00 37.02           C  
-ANISOU 9409  CA  ALA D 905     4921   4425   4720   -621    433   -422       C  
-ATOM   9410  C   ALA D 905    -120.702  11.150 -21.729  1.00 37.11           C  
-ANISOU 9410  C   ALA D 905     4896   4480   4724   -666    418   -475       C  
-ATOM   9411  O   ALA D 905    -120.809  10.851 -22.902  1.00 38.31           O  
-ANISOU 9411  O   ALA D 905     5042   4637   4875   -659    399   -553       O  
-ATOM   9412  CB  ALA D 905    -119.112   9.680 -20.485  1.00 38.84           C  
-ANISOU 9412  CB  ALA D 905     5178   4549   5030   -648    439   -400       C  
-ATOM   9413  N   ASN D 906    -121.735  11.562 -21.002  1.00 37.74           N  
-ANISOU 9413  N   ASN D 906     4945   4602   4792   -705    426   -437       N  
-ATOM   9414  CA  ASN D 906    -123.042  11.764 -21.616  1.00 38.49           C  
-ANISOU 9414  CA  ASN D 906     5000   4754   4872   -743    412   -485       C  
-ATOM   9415  C   ASN D 906    -123.001  12.738 -22.786  1.00 40.47           C  
-ANISOU 9415  C   ASN D 906     5234   5085   5056   -697    398   -538       C  
-ATOM   9416  O   ASN D 906    -123.778  12.593 -23.730  1.00 43.16           O  
-ANISOU 9416  O   ASN D 906     5549   5462   5388   -714    380   -605       O  
-ATOM   9417  CB  ASN D 906    -124.078  12.247 -20.596  1.00 36.76           C  
-ANISOU 9417  CB  ASN D 906     4744   4587   4635   -780    423   -430       C  
-ATOM   9418  CG  ASN D 906    -124.499  11.154 -19.623  1.00 37.53           C  
-ANISOU 9418  CG  ASN D 906     4837   4622   4799   -839    438   -376       C  
-ATOM   9419  OD1 ASN D 906    -124.286   9.964 -19.868  1.00 37.96           O  
-ANISOU 9419  OD1 ASN D 906     4910   4582   4930   -868    433   -393       O  
-ATOM   9420  ND2 ASN D 906    -125.071  11.557 -18.501  1.00 36.03           N  
-ANISOU 9420  ND2 ASN D 906     4618   4486   4585   -854    454   -308       N  
-ATOM   9421  N   TYR D 907    -122.099  13.718 -22.731  1.00 40.04           N  
-ANISOU 9421  N   TYR D 907     5191   5062   4960   -639    405   -504       N  
-ATOM   9422  CA  TYR D 907    -121.974  14.721 -23.801  1.00 38.20           C  
-ANISOU 9422  CA  TYR D 907     4938   4905   4670   -592    396   -530       C  
-ATOM   9423  C   TYR D 907    -121.169  14.217 -24.989  1.00 39.53           C  
-ANISOU 9423  C   TYR D 907     5120   5068   4832   -553    387   -582       C  
-ATOM   9424  O   TYR D 907    -121.016  14.932 -25.976  1.00 40.26           O  
-ANISOU 9424  O   TYR D 907     5190   5232   4873   -509    382   -596       O  
-ATOM   9425  CB  TYR D 907    -121.390  16.024 -23.252  1.00 35.88           C  
-ANISOU 9425  CB  TYR D 907     4641   4642   4350   -550    404   -468       C  
-ATOM   9426  CG  TYR D 907    -122.360  16.711 -22.307  1.00 35.92           C  
-ANISOU 9426  CG  TYR D 907     4619   4683   4344   -574    404   -439       C  
-ATOM   9427  CD1 TYR D 907    -123.477  17.377 -22.801  1.00 33.75           C  
-ANISOU 9427  CD1 TYR D 907     4306   4481   4035   -581    393   -461       C  
-ATOM   9428  CD2 TYR D 907    -122.200  16.640 -20.928  1.00 34.80           C  
-ANISOU 9428  CD2 TYR D 907     4487   4514   4222   -585    414   -392       C  
-ATOM   9429  CE1 TYR D 907    -124.376  17.984 -21.960  1.00 32.97           C  
-ANISOU 9429  CE1 TYR D 907     4179   4423   3924   -596    391   -440       C  
-ATOM   9430  CE2 TYR D 907    -123.108  17.244 -20.071  1.00 33.64           C  
-ANISOU 9430  CE2 TYR D 907     4309   4418   4057   -598    412   -372       C  
-ATOM   9431  CZ  TYR D 907    -124.184  17.918 -20.599  1.00 34.11           C  
-ANISOU 9431  CZ  TYR D 907     4332   4545   4085   -603    400   -398       C  
-ATOM   9432  OH  TYR D 907    -125.099  18.504 -19.768  1.00 36.53           O  
-ANISOU 9432  OH  TYR D 907     4604   4907   4370   -611    397   -384       O  
-ATOM   9433  N   CYS D 908    -120.705  12.969 -24.943  1.00 40.88           N  
-ANISOU 9433  N   CYS D 908     5321   5158   5055   -566    385   -611       N  
-ATOM   9434  CA  CYS D 908    -120.148  12.346 -26.147  1.00 43.09           C  
-ANISOU 9434  CA  CYS D 908     5606   5441   5327   -528    370   -685       C  
-ATOM   9435  C   CYS D 908    -121.230  12.001 -27.174  1.00 42.96           C  
-ANISOU 9435  C   CYS D 908     5552   5474   5297   -547    345   -775       C  
-ATOM   9436  O   CYS D 908    -120.938  11.934 -28.369  1.00 43.96           O  
-ANISOU 9436  O   CYS D 908     5662   5658   5382   -498    331   -840       O  
-ATOM   9437  CB  CYS D 908    -119.361  11.094 -25.787  1.00 44.28           C  
-ANISOU 9437  CB  CYS D 908     5797   5483   5544   -531    369   -698       C  
-ATOM   9438  SG  CYS D 908    -117.903  11.404 -24.750  1.00 42.54           S  
-ANISOU 9438  SG  CYS D 908     5617   5218   5330   -493    394   -605       S  
-ATOM   9439  N   HIS D 909    -122.462  11.784 -26.691  1.00 47.18           N  
-ANISOU 9439  N   HIS D 909     6067   5995   5862   -614    340   -780       N  
-ATOM   9440  CA  HIS D 909    -123.625  11.395 -27.513  1.00 49.76           C  
-ANISOU 9440  CA  HIS D 909     6353   6365   6189   -644    315   -869       C  
-ATOM   9441  C   HIS D 909    -123.317  10.142 -28.335  1.00 50.21           C  
-ANISOU 9441  C   HIS D 909     6417   6371   6291   -636    286   -975       C  
-ATOM   9442  O   HIS D 909    -123.525  10.096 -29.530  1.00 49.61           O  
-ANISOU 9442  O   HIS D 909     6308   6369   6171   -601    262  -1065       O  
-ATOM   9443  CB  HIS D 909    -124.106  12.558 -28.400  1.00 49.79           C  
-ANISOU 9443  CB  HIS D 909     6314   6506   6098   -603    311   -880       C  
-ATOM   9444  CG  HIS D 909    -124.715  13.687 -27.616  1.00 54.38           C  
-ANISOU 9444  CG  HIS D 909     6880   7129   6651   -620    328   -799       C  
-ATOM   9445  ND1 HIS D 909    -124.146  14.947 -27.529  1.00 51.08           N  
-ANISOU 9445  ND1 HIS D 909     6464   6760   6183   -568    344   -728       N  
-ATOM   9446  CD2 HIS D 909    -125.828  13.728 -26.848  1.00 54.77           C  
-ANISOU 9446  CD2 HIS D 909     6911   7178   6721   -680    330   -780       C  
-ATOM   9447  CE1 HIS D 909    -124.898  15.716 -26.765  1.00 50.42           C  
-ANISOU 9447  CE1 HIS D 909     6364   6701   6092   -592    351   -680       C  
-ATOM   9448  NE2 HIS D 909    -125.920  14.999 -26.333  1.00 52.10           N  
-ANISOU 9448  NE2 HIS D 909     6564   6891   6340   -657    344   -708       N  
-ATOM   9449  N   THR D 910    -122.766   9.143 -27.672  1.00 49.59           N  
-ANISOU 9449  N   THR D 910     6377   6168   6299   -659    288   -963       N  
-ATOM   9450  CA  THR D 910    -122.530   7.867 -28.315  1.00 50.43           C  
-ANISOU 9450  CA  THR D 910     6489   6201   6472   -656    256  -1068       C  
-ATOM   9451  C   THR D 910    -123.848   7.077 -28.341  1.00 53.21           C  
-ANISOU 9451  C   THR D 910     6805   6509   6902   -737    229  -1132       C  
-ATOM   9452  O   THR D 910    -124.819   7.485 -27.736  1.00 50.00           O  
-ANISOU 9452  O   THR D 910     6376   6126   6496   -795    243  -1079       O  
-ATOM   9453  CB  THR D 910    -121.428   7.080 -27.586  1.00 47.09           C  
-ANISOU 9453  CB  THR D 910     6120   5652   6122   -647    267  -1025       C  
-ATOM   9454  OG1 THR D 910    -121.711   7.034 -26.183  1.00 44.38           O  
-ANISOU 9454  OG1 THR D 910     5792   5238   5832   -708    294   -915       O  
-ATOM   9455  CG2 THR D 910    -120.088   7.725 -27.827  1.00 47.34           C  
-ANISOU 9455  CG2 THR D 910     6176   5735   6078   -561    284   -991       C  
-ATOM   9456  N   SER D 911    -123.858   5.941 -29.027  1.00 57.45           N  
-ANISOU 9456  N   SER D 911     7335   6981   7511   -740    190  -1250       N  
-ATOM   9457  CA  SER D 911    -125.043   5.079 -29.114  1.00 60.10           C  
-ANISOU 9457  CA  SER D 911     7632   7260   7944   -821    157  -1324       C  
-ATOM   9458  C   SER D 911    -124.600   3.648 -29.373  1.00 63.61           C  
-ANISOU 9458  C   SER D 911     8092   7562   8514   -825    120  -1417       C  
-ATOM   9459  O   SER D 911    -123.420   3.398 -29.589  1.00 66.47           O  
-ANISOU 9459  O   SER D 911     8493   7894   8868   -756    118  -1433       O  
-ATOM   9460  CB  SER D 911    -125.973   5.571 -30.238  1.00 59.18           C  
-ANISOU 9460  CB  SER D 911     7454   7285   7749   -807    130  -1427       C  
-ATOM   9461  OG  SER D 911    -125.268   5.634 -31.466  1.00 58.30           O  
-ANISOU 9461  OG  SER D 911     7335   7254   7561   -712    106  -1528       O  
-ATOM   9462  N   GLN D 912    -125.547   2.716 -29.396  1.00 70.30           N  
-ANISOU 9462  N   GLN D 912     8905   8324   9482   -903     86  -1485       N  
-ATOM   9463  CA  GLN D 912    -125.226   1.315 -29.673  1.00 74.73           C  
-ANISOU 9463  CA  GLN D 912     9474   8734  10186   -912     41  -1586       C  
-ATOM   9464  C   GLN D 912    -124.611   1.134 -31.061  1.00 72.95           C  
-ANISOU 9464  C   GLN D 912     9238   8575   9903   -813     -4  -1752       C  
-ATOM   9465  O   GLN D 912    -123.680   0.351 -31.236  1.00 70.41           O  
-ANISOU 9465  O   GLN D 912     8949   8163   9642   -766    -25  -1805       O  
-ATOM   9466  CB  GLN D 912    -126.469   0.447 -29.524  1.00 81.19           C  
-ANISOU 9466  CB  GLN D 912    10242   9456  11150  -1020      8  -1633       C  
-ATOM   9467  CG  GLN D 912    -126.885   0.243 -28.084  1.00 86.09           C  
-ANISOU 9467  CG  GLN D 912    10874   9975  11863  -1115     49  -1466       C  
-ATOM   9468  CD  GLN D 912    -128.115   1.063 -27.719  1.00 89.66           C  
-ANISOU 9468  CD  GLN D 912    11277  10537  12252  -1178     74  -1400       C  
-ATOM   9469  OE1 GLN D 912    -127.990   2.222 -27.318  1.00 85.51           O  
-ANISOU 9469  OE1 GLN D 912    10766  10130  11594  -1145    118  -1303       O  
-ATOM   9470  NE2 GLN D 912    -129.307   0.466 -27.858  1.00 87.82           N  
-ANISOU 9470  NE2 GLN D 912    10982  10265  12122  -1267     43  -1458       N  
-ATOM   9471  N   GLY D 913    -125.108   1.898 -32.028  1.00 72.13           N  
-ANISOU 9471  N   GLY D 913     9087   8645   9675   -773    -17  -1827       N  
-ATOM   9472  CA  GLY D 913    -124.568   1.907 -33.381  1.00 72.08           C  
-ANISOU 9472  CA  GLY D 913     9058   8749   9579   -667    -53  -1972       C  
-ATOM   9473  C   GLY D 913    -123.215   2.577 -33.549  1.00 75.57           C  
-ANISOU 9473  C   GLY D 913     9541   9270   9902   -563    -19  -1909       C  
-ATOM   9474  O   GLY D 913    -122.486   2.231 -34.485  1.00 69.76           O  
-ANISOU 9474  O   GLY D 913     8797   8581   9127   -473    -50  -2022       O  
-ATOM   9475  N   ASP D 914    -122.890   3.540 -32.669  1.00 76.42           N  
-ANISOU 9475  N   ASP D 914     9684   9401   9951   -573     41  -1736       N  
-ATOM   9476  CA  ASP D 914    -121.544   4.138 -32.588  1.00 76.48           C  
-ANISOU 9476  CA  ASP D 914     9733   9453   9873   -491     77  -1654       C  
-ATOM   9477  C   ASP D 914    -121.108   4.317 -31.107  1.00 74.25           C  
-ANISOU 9477  C   ASP D 914     9507   9062   9642   -539    125  -1487       C  
-ATOM   9478  O   ASP D 914    -121.228   5.411 -30.527  1.00 71.66           O  
-ANISOU 9478  O   ASP D 914     9184   8798   9246   -552    166  -1366       O  
-ATOM   9479  CB  ASP D 914    -121.483   5.470 -33.346  1.00 76.18           C  
-ANISOU 9479  CB  ASP D 914     9660   9615   9668   -423     98  -1626       C  
-ATOM   9480  CG  ASP D 914    -120.042   5.904 -33.647  1.00 77.60           C  
-ANISOU 9480  CG  ASP D 914     9864   9856   9765   -326    121  -1583       C  
-ATOM   9481  OD1 ASP D 914    -119.857   6.808 -34.489  1.00 78.58           O  
-ANISOU 9481  OD1 ASP D 914     9951  10144   9761   -257    131  -1576       O  
-ATOM   9482  OD2 ASP D 914    -119.085   5.324 -33.064  1.00 79.13           O  
-ANISOU 9482  OD2 ASP D 914    10107   9937  10021   -316    129  -1552       O  
-ATOM   9483  N   PRO D 915    -120.584   3.238 -30.499  1.00 70.13           N  
-ANISOU 9483  N   PRO D 915     9026   8379   9242   -558    117  -1484       N  
-ATOM   9484  CA  PRO D 915    -120.343   3.183 -29.067  1.00 64.11           C  
-ANISOU 9484  CA  PRO D 915     8308   7508   8544   -610    156  -1336       C  
-ATOM   9485  C   PRO D 915    -118.929   3.609 -28.621  1.00 62.72           C  
-ANISOU 9485  C   PRO D 915     8179   7340   8312   -542    191  -1246       C  
-ATOM   9486  O   PRO D 915    -118.570   3.407 -27.460  1.00 61.49           O  
-ANISOU 9486  O   PRO D 915     8060   7092   8212   -570    219  -1136       O  
-ATOM   9487  CB  PRO D 915    -120.567   1.701 -28.777  1.00 66.69           C  
-ANISOU 9487  CB  PRO D 915     8643   7654   9040   -663    123  -1388       C  
-ATOM   9488  CG  PRO D 915    -119.984   1.021 -29.986  1.00 65.11           C  
-ANISOU 9488  CG  PRO D 915     8437   7456   8846   -586     73  -1551       C  
-ATOM   9489  CD  PRO D 915    -120.225   1.957 -31.148  1.00 67.59           C  
-ANISOU 9489  CD  PRO D 915     8705   7966   9009   -528     65  -1626       C  
-ATOM   9490  N   ILE D 916    -118.132   4.176 -29.526  1.00 64.17           N  
-ANISOU 9490  N   ILE D 916     8356   7639   8387   -452    190  -1287       N  
-ATOM   9491  CA  ILE D 916    -116.794   4.658 -29.191  1.00 64.06           C  
-ANISOU 9491  CA  ILE D 916     8376   7647   8317   -388    222  -1204       C  
-ATOM   9492  C   ILE D 916    -116.823   6.172 -29.115  1.00 61.03           C  
-ANISOU 9492  C   ILE D 916     7974   7396   7819   -376    257  -1112       C  
-ATOM   9493  O   ILE D 916    -117.185   6.844 -30.084  1.00 61.53           O  
-ANISOU 9493  O   ILE D 916     7995   7588   7796   -346    250  -1157       O  
-ATOM   9494  CB  ILE D 916    -115.735   4.229 -30.230  1.00 66.33           C  
-ANISOU 9494  CB  ILE D 916     8663   7972   8567   -289    199  -1302       C  
-ATOM   9495  CG1 ILE D 916    -115.635   2.709 -30.281  1.00 70.93           C  
-ANISOU 9495  CG1 ILE D 916     9266   8409   9277   -293    157  -1401       C  
-ATOM   9496  CG2 ILE D 916    -114.363   4.748 -29.857  1.00 63.32           C  
-ANISOU 9496  CG2 ILE D 916     8311   7618   8129   -229    233  -1210       C  
-ATOM   9497  CD1 ILE D 916    -114.637   2.184 -31.298  1.00 78.23           C  
-ANISOU 9497  CD1 ILE D 916    10186   9370  10169   -189    128  -1516       C  
-ATOM   9498  N   GLY D 917    -116.421   6.693 -27.960  1.00 56.19           N  
-ANISOU 9498  N   GLY D 917     7390   6752   7210   -395    294   -986       N  
-ATOM   9499  CA  GLY D 917    -116.355   8.127 -27.728  1.00 55.46           C  
-ANISOU 9499  CA  GLY D 917     7282   6760   7031   -384    324   -896       C  
-ATOM   9500  C   GLY D 917    -114.980   8.628 -27.290  1.00 52.84           C  
-ANISOU 9500  C   GLY D 917     6974   6436   6666   -331    350   -818       C  
-ATOM   9501  O   GLY D 917    -114.090   7.845 -26.919  1.00 48.47           O  
-ANISOU 9501  O   GLY D 917     6455   5802   6158   -308    350   -815       O  
-ATOM   9502  N   LEU D 918    -114.834   9.954 -27.350  1.00 49.25           N  
-ANISOU 9502  N   LEU D 918     6496   6077   6139   -312    369   -755       N  
-ATOM   9503  CA  LEU D 918    -113.650  10.652 -26.907  1.00 45.76           C  
-ANISOU 9503  CA  LEU D 918     6065   5653   5670   -271    392   -675       C  
-ATOM   9504  C   LEU D 918    -113.989  11.612 -25.754  1.00 44.70           C  
-ANISOU 9504  C   LEU D 918     5929   5515   5541   -311    411   -583       C  
-ATOM   9505  O   LEU D 918    -114.979  12.356 -25.798  1.00 41.51           O  
-ANISOU 9505  O   LEU D 918     5497   5160   5116   -342    410   -572       O  
-ATOM   9506  CB  LEU D 918    -113.036  11.435 -28.056  1.00 44.25           C  
-ANISOU 9506  CB  LEU D 918     5836   5578   5398   -206    396   -680       C  
-ATOM   9507  CG  LEU D 918    -112.480  10.631 -29.227  1.00 45.78           C  
-ANISOU 9507  CG  LEU D 918     6022   5808   5565   -144    378   -769       C  
-ATOM   9508  CD1 LEU D 918    -111.998  11.555 -30.331  1.00 43.33           C  
-ANISOU 9508  CD1 LEU D 918     5662   5639   5163    -79    387   -751       C  
-ATOM   9509  CD2 LEU D 918    -111.359   9.723 -28.765  1.00 45.73           C  
-ANISOU 9509  CD2 LEU D 918     6057   5718   5602   -114    379   -775       C  
-ATOM   9510  N   ILE D 919    -113.131  11.588 -24.735  1.00 42.44           N  
-ANISOU 9510  N   ILE D 919     5669   5177   5279   -303    426   -522       N  
-ATOM   9511  CA  ILE D 919    -113.284  12.440 -23.578  1.00 41.34           C  
-ANISOU 9511  CA  ILE D 919     5525   5040   5143   -327    439   -446       C  
-ATOM   9512  C   ILE D 919    -111.931  13.040 -23.155  1.00 38.38           C  
-ANISOU 9512  C   ILE D 919     5152   4675   4754   -281    451   -393       C  
-ATOM   9513  O   ILE D 919    -110.886  12.365 -23.193  1.00 39.19           O  
-ANISOU 9513  O   ILE D 919     5279   4745   4868   -245    454   -399       O  
-ATOM   9514  CB  ILE D 919    -113.953  11.643 -22.441  1.00 40.27           C  
-ANISOU 9514  CB  ILE D 919     5411   4829   5061   -380    442   -426       C  
-ATOM   9515  CG1 ILE D 919    -114.418  12.559 -21.340  1.00 38.53           C  
-ANISOU 9515  CG1 ILE D 919     5174   4637   4829   -403    451   -365       C  
-ATOM   9516  CG2 ILE D 919    -113.000  10.617 -21.869  1.00 39.56           C  
-ANISOU 9516  CG2 ILE D 919     5359   4658   5013   -359    448   -409       C  
-ATOM   9517  CD1 ILE D 919    -115.427  11.887 -20.455  1.00 41.85           C  
-ANISOU 9517  CD1 ILE D 919     5597   5017   5286   -459    455   -344       C  
-ATOM   9518  N   LEU D 920    -111.961  14.291 -22.717  1.00 33.86           N  
-ANISOU 9518  N   LEU D 920     4554   4145   4167   -283    455   -346       N  
-ATOM   9519  CA  LEU D 920    -110.749  14.970 -22.248  1.00 33.94           C  
-ANISOU 9519  CA  LEU D 920     4557   4163   4176   -247    461   -299       C  
-ATOM   9520  C   LEU D 920    -110.577  14.959 -20.750  1.00 31.66           C  
-ANISOU 9520  C   LEU D 920     4280   3838   3911   -257    465   -262       C  
-ATOM   9521  O   LEU D 920    -111.549  15.014 -19.993  1.00 31.70           O  
-ANISOU 9521  O   LEU D 920     4283   3839   3924   -293    463   -254       O  
-ATOM   9522  CB  LEU D 920    -110.790  16.420 -22.674  1.00 34.45           C  
-ANISOU 9522  CB  LEU D 920     4576   4290   4223   -238    458   -272       C  
-ATOM   9523  CG  LEU D 920    -110.784  16.635 -24.176  1.00 37.71           C  
-ANISOU 9523  CG  LEU D 920     4964   4764   4600   -214    458   -288       C  
-ATOM   9524  CD1 LEU D 920    -111.247  18.038 -24.505  1.00 36.12           C  
-ANISOU 9524  CD1 LEU D 920     4717   4616   4393   -217    454   -252       C  
-ATOM   9525  CD2 LEU D 920    -109.395  16.395 -24.717  1.00 40.16           C  
-ANISOU 9525  CD2 LEU D 920     5272   5090   4898   -163    467   -278       C  
-ATOM   9526  N   LEU D 921    -109.329  14.922 -20.304  1.00 31.54           N  
-ANISOU 9526  N   LEU D 921     4272   3810   3902   -220    470   -237       N  
-ATOM   9527  CA  LEU D 921    -108.992  15.358 -18.952  1.00 32.21           C  
-ANISOU 9527  CA  LEU D 921     4349   3892   3996   -215    469   -202       C  
-ATOM   9528  C   LEU D 921    -108.224  16.654 -19.065  1.00 30.78           C  
-ANISOU 9528  C   LEU D 921     4129   3749   3817   -190    460   -185       C  
-ATOM   9529  O   LEU D 921    -107.200  16.718 -19.728  1.00 29.93           O  
-ANISOU 9529  O   LEU D 921     4015   3652   3707   -159    464   -180       O  
-ATOM   9530  CB  LEU D 921    -108.155  14.326 -18.206  1.00 35.05           C  
-ANISOU 9530  CB  LEU D 921     4741   4210   4366   -190    479   -185       C  
-ATOM   9531  CG  LEU D 921    -108.939  13.125 -17.668  1.00 36.50           C  
-ANISOU 9531  CG  LEU D 921     4957   4344   4569   -219    486   -178       C  
-ATOM   9532  CD1 LEU D 921    -107.957  12.036 -17.298  1.00 38.68           C  
-ANISOU 9532  CD1 LEU D 921     5266   4570   4862   -185    496   -161       C  
-ATOM   9533  CD2 LEU D 921    -109.791  13.504 -16.466  1.00 35.08           C  
-ANISOU 9533  CD2 LEU D 921     4757   4188   4382   -245    487   -147       C  
-ATOM   9534  N   GLY D 922    -108.733  17.688 -18.414  1.00 31.01           N  
-ANISOU 9534  N   GLY D 922     4127   3800   3854   -204    447   -178       N  
-ATOM   9535  CA  GLY D 922    -108.090  19.000 -18.396  1.00 30.15           C  
-ANISOU 9535  CA  GLY D 922     3974   3712   3770   -186    432   -165       C  
-ATOM   9536  C   GLY D 922    -107.621  19.394 -17.005  1.00 28.00           C  
-ANISOU 9536  C   GLY D 922     3686   3442   3513   -169    418   -165       C  
-ATOM   9537  O   GLY D 922    -108.289  19.104 -16.018  1.00 28.87           O  
-ANISOU 9537  O   GLY D 922     3803   3559   3607   -177    415   -172       O  
-ATOM   9538  N   GLU D 923    -106.479  20.070 -16.939  1.00 28.31           N  
-ANISOU 9538  N   GLU D 923     3693   3482   3580   -144    407   -156       N  
-ATOM   9539  CA  GLU D 923    -106.063  20.732 -15.705  1.00 28.72           C  
-ANISOU 9539  CA  GLU D 923     3713   3545   3654   -124    383   -170       C  
-ATOM   9540  C   GLU D 923    -106.740  22.080 -15.742  1.00 27.55           C  
-ANISOU 9540  C   GLU D 923     3521   3402   3546   -140    356   -187       C  
-ATOM   9541  O   GLU D 923    -106.568  22.835 -16.696  1.00 27.09           O  
-ANISOU 9541  O   GLU D 923     3437   3332   3525   -148    352   -167       O  
-ATOM   9542  CB  GLU D 923    -104.550  20.902 -15.636  1.00 28.96           C  
-ANISOU 9542  CB  GLU D 923     3723   3573   3709    -94    379   -160       C  
-ATOM   9543  CG  GLU D 923    -104.099  21.528 -14.335  1.00 32.23           C  
-ANISOU 9543  CG  GLU D 923     4098   4005   4144    -70    350   -190       C  
-ATOM   9544  CD  GLU D 923    -102.629  21.923 -14.323  1.00 33.23           C  
-ANISOU 9544  CD  GLU D 923     4189   4130   4308    -45    339   -185       C  
-ATOM   9545  OE1 GLU D 923    -101.830  21.193 -14.920  1.00 35.56           O  
-ANISOU 9545  OE1 GLU D 923     4506   4421   4584    -33    364   -157       O  
-ATOM   9546  OE2 GLU D 923    -102.269  22.909 -13.645  1.00 32.01           O  
-ANISOU 9546  OE2 GLU D 923     3981   3980   4201    -35    304   -218       O  
-ATOM   9547  N   VAL D 924    -107.596  22.325 -14.761  1.00 27.14           N  
-ANISOU 9547  N   VAL D 924     3459   3371   3481   -140    339   -217       N  
-ATOM   9548  CA  VAL D 924    -108.398  23.524 -14.730  1.00 27.09           C  
-ANISOU 9548  CA  VAL D 924     3414   3370   3510   -150    310   -241       C  
-ATOM   9549  C   VAL D 924    -107.999  24.325 -13.488  1.00 26.17           C  
-ANISOU 9549  C   VAL D 924     3251   3268   3423   -118    271   -288       C  
-ATOM   9550  O   VAL D 924    -108.017  23.813 -12.384  1.00 23.73           O  
-ANISOU 9550  O   VAL D 924     2946   2999   3070    -95    269   -308       O  
-ATOM   9551  CB  VAL D 924    -109.909  23.193 -14.654  1.00 26.80           C  
-ANISOU 9551  CB  VAL D 924     3397   3359   3429   -173    318   -251       C  
-ATOM   9552  CG1 VAL D 924    -110.739  24.481 -14.711  1.00 26.74           C  
-ANISOU 9552  CG1 VAL D 924     3347   3356   3457   -176    286   -277       C  
-ATOM   9553  CG2 VAL D 924    -110.320  22.250 -15.777  1.00 27.04           C  
-ANISOU 9553  CG2 VAL D 924     3470   3378   3427   -202    352   -220       C  
-ATOM   9554  N   ALA D 925    -107.656  25.588 -13.688  1.00 25.08           N  
-ANISOU 9554  N   ALA D 925     3064   3101   3364   -114    237   -304       N  
-ATOM   9555  CA  ALA D 925    -107.184  26.394 -12.593  1.00 27.12           C  
-ANISOU 9555  CA  ALA D 925     3272   3368   3665    -82    192   -364       C  
-ATOM   9556  C   ALA D 925    -108.399  27.092 -11.991  1.00 28.27           C  
-ANISOU 9556  C   ALA D 925     3392   3539   3811    -73    160   -417       C  
-ATOM   9557  O   ALA D 925    -108.815  28.149 -12.466  1.00 32.75           O  
-ANISOU 9557  O   ALA D 925     3929   4069   4447    -83    133   -428       O  
-ATOM   9558  CB  ALA D 925    -106.159  27.399 -13.097  1.00 28.67           C  
-ANISOU 9558  CB  ALA D 925     3420   3507   3966    -86    167   -356       C  
-ATOM   9559  N   LEU D 926    -108.968  26.499 -10.961  1.00 28.18           N  
-ANISOU 9559  N   LEU D 926     3389   3595   3721    -51    163   -446       N  
-ATOM   9560  CA  LEU D 926    -110.256  26.948 -10.436  1.00 28.25           C  
-ANISOU 9560  CA  LEU D 926     3378   3649   3705    -41    142   -489       C  
-ATOM   9561  C   LEU D 926    -110.103  28.078  -9.438  1.00 28.28           C  
-ANISOU 9561  C   LEU D 926     3315   3674   3755      6     80   -580       C  
-ATOM   9562  O   LEU D 926    -111.009  28.874  -9.271  1.00 27.17           O  
-ANISOU 9562  O   LEU D 926     3145   3545   3633     18     48   -627       O  
-ATOM   9563  CB  LEU D 926    -110.977  25.796  -9.753  1.00 26.91           C  
-ANISOU 9563  CB  LEU D 926     3238   3557   3430    -37    175   -469       C  
-ATOM   9564  CG  LEU D 926    -111.262  24.621 -10.654  1.00 27.69           C  
-ANISOU 9564  CG  LEU D 926     3399   3631   3491    -84    229   -394       C  
-ATOM   9565  CD1 LEU D 926    -111.655  23.424  -9.806  1.00 29.92           C  
-ANISOU 9565  CD1 LEU D 926     3702   3975   3690    -78    260   -366       C  
-ATOM   9566  CD2 LEU D 926    -112.372  24.961 -11.612  1.00 28.48           C  
-ANISOU 9566  CD2 LEU D 926     3507   3711   3602   -120    234   -385       C  
-ATOM   9567  N   GLY D 927    -108.971  28.119  -8.743  1.00 30.57           N  
-ANISOU 9567  N   GLY D 927     3579   3974   4062     39     60   -613       N  
-ATOM   9568  CA  GLY D 927    -108.747  29.133  -7.703  1.00 31.30           C  
-ANISOU 9568  CA  GLY D 927     3601   4094   4198     91     -6   -718       C  
-ATOM   9569  C   GLY D 927    -109.875  29.112  -6.676  1.00 30.05           C  
-ANISOU 9569  C   GLY D 927     3422   4041   3956    133    -21   -773       C  
-ATOM   9570  O   GLY D 927    -110.306  28.059  -6.272  1.00 28.66           O  
-ANISOU 9570  O   GLY D 927     3275   3941   3674    136     21   -729       O  
-ATOM   9571  N   ASN D 928    -110.308  30.291  -6.242  1.00 30.24           N  
-ANISOU 9571  N   ASN D 928     3387   4069   4034    167    -83   -868       N  
-ATOM   9572  CA  ASN D 928    -111.446  30.458  -5.359  1.00 31.41           C  
-ANISOU 9572  CA  ASN D 928     3505   4322   4109    213   -103   -929       C  
-ATOM   9573  C   ASN D 928    -112.770  30.326  -6.137  1.00 31.95           C  
-ANISOU 9573  C   ASN D 928     3609   4380   4151    171    -72   -874       C  
-ATOM   9574  O   ASN D 928    -113.093  31.143  -7.030  1.00 30.72           O  
-ANISOU 9574  O   ASN D 928     3453   4136   4084    144    -89   -874       O  
-ATOM   9575  CB  ASN D 928    -111.396  31.821  -4.701  1.00 32.91           C  
-ANISOU 9575  CB  ASN D 928     3616   4510   4379    270   -188  -1063       C  
-ATOM   9576  CG  ASN D 928    -110.183  32.007  -3.816  1.00 34.27           C  
-ANISOU 9576  CG  ASN D 928     3739   4710   4573    318   -229  -1139       C  
-ATOM   9577  OD1 ASN D 928    -109.792  31.098  -3.086  1.00 34.96           O  
-ANISOU 9577  OD1 ASN D 928     3832   4895   4557    347   -202  -1120       O  
-ATOM   9578  ND2 ASN D 928    -109.602  33.193  -3.860  1.00 33.18           N  
-ANISOU 9578  ND2 ASN D 928     3547   4486   4574    330   -298  -1226       N  
-ATOM   9579  N   MET D 929    -113.511  29.288  -5.779  1.00 29.68           N  
-ANISOU 9579  N   MET D 929     3348   4186   3744    168    -25   -824       N  
-ATOM   9580  CA  MET D 929    -114.713  28.911  -6.473  1.00 30.50           C  
-ANISOU 9580  CA  MET D 929     3487   4292   3811    123     13   -766       C  
-ATOM   9581  C   MET D 929    -115.910  29.655  -5.906  1.00 30.45           C  
-ANISOU 9581  C   MET D 929     3431   4363   3776    164    -24   -838       C  
-ATOM   9582  O   MET D 929    -116.075  29.727  -4.706  1.00 32.07           O  
-ANISOU 9582  O   MET D 929     3587   4681   3918    227    -48   -899       O  
-ATOM   9583  CB  MET D 929    -114.921  27.413  -6.339  1.00 32.09           C  
-ANISOU 9583  CB  MET D 929     3733   4548   3912     95     78   -675       C  
-ATOM   9584  CG  MET D 929    -113.828  26.591  -7.007  1.00 33.57           C  
-ANISOU 9584  CG  MET D 929     3974   4655   4124     56    117   -603       C  
-ATOM   9585  SD  MET D 929    -113.977  24.805  -6.768  1.00 34.34           S  
-ANISOU 9585  SD  MET D 929     4122   4799   4126     29    187   -501       S  
-ATOM   9586  CE  MET D 929    -114.017  24.707  -4.979  1.00 38.78           C  
-ANISOU 9586  CE  MET D 929     4623   5514   4597    108    170   -537       C  
-ATOM   9587  N   TYR D 930    -116.717  30.229  -6.798  1.00 28.71           N  
-ANISOU 9587  N   TYR D 930     3218   4087   3601    135    -30   -832       N  
-ATOM   9588  CA  TYR D 930    -118.012  30.770  -6.465  1.00 28.17           C  
-ANISOU 9588  CA  TYR D 930     3113   4092   3498    165    -54   -883       C  
-ATOM   9589  C   TYR D 930    -118.966  29.568  -6.449  1.00 29.30           C  
-ANISOU 9589  C   TYR D 930     3285   4320   3525    130      8   -804       C  
-ATOM   9590  O   TYR D 930    -119.297  29.016  -7.499  1.00 28.36           O  
-ANISOU 9590  O   TYR D 930     3217   4148   3412     64     51   -727       O  
-ATOM   9591  CB  TYR D 930    -118.408  31.786  -7.520  1.00 26.82           C  
-ANISOU 9591  CB  TYR D 930     2943   3821   3427    146    -80   -893       C  
-ATOM   9592  CG  TYR D 930    -119.652  32.612  -7.277  1.00 27.44           C  
-ANISOU 9592  CG  TYR D 930     2978   3953   3495    186   -118   -960       C  
-ATOM   9593  CD1 TYR D 930    -120.131  32.872  -5.997  1.00 28.72           C  
-ANISOU 9593  CD1 TYR D 930     3081   4239   3591    259   -154  -1051       C  
-ATOM   9594  CD2 TYR D 930    -120.332  33.177  -8.352  1.00 27.40           C  
-ANISOU 9594  CD2 TYR D 930     2985   3880   3545    159   -120   -934       C  
-ATOM   9595  CE1 TYR D 930    -121.256  33.660  -5.797  1.00 28.56           C  
-ANISOU 9595  CE1 TYR D 930     3018   4270   3562    303   -192  -1119       C  
-ATOM   9596  CE2 TYR D 930    -121.445  33.977  -8.175  1.00 28.43           C  
-ANISOU 9596  CE2 TYR D 930     3076   4055   3673    200   -157   -996       C  
-ATOM   9597  CZ  TYR D 930    -121.909  34.216  -6.896  1.00 31.56           C  
-ANISOU 9597  CZ  TYR D 930     3416   4570   4006    272   -194  -1091       C  
-ATOM   9598  OH  TYR D 930    -123.030  35.022  -6.742  1.00 32.70           O  
-ANISOU 9598  OH  TYR D 930     3517   4761   4145    319   -233  -1158       O  
-ATOM   9599  N   GLU D 931    -119.375  29.153  -5.260  1.00 30.30           N  
-ANISOU 9599  N   GLU D 931     3376   4585   3553    174     12   -822       N  
-ATOM   9600  CA  GLU D 931    -120.161  27.946  -5.113  1.00 33.05           C  
-ANISOU 9600  CA  GLU D 931     3743   5014   3802    138     71   -735       C  
-ATOM   9601  C   GLU D 931    -121.632  28.248  -5.234  1.00 31.96           C  
-ANISOU 9601  C   GLU D 931     3578   4941   3624    135     69   -748       C  
-ATOM   9602  O   GLU D 931    -122.153  29.047  -4.502  1.00 32.86           O  
-ANISOU 9602  O   GLU D 931     3632   5142   3712    201     26   -830       O  
-ATOM   9603  CB  GLU D 931    -119.857  27.305  -3.769  1.00 35.64           C  
-ANISOU 9603  CB  GLU D 931     4036   5468   4038    188     83   -727       C  
-ATOM   9604  CG  GLU D 931    -118.377  27.064  -3.594  1.00 39.06           C  
-ANISOU 9604  CG  GLU D 931     4489   5846   4507    200     80   -722       C  
-ATOM   9605  CD  GLU D 931    -118.054  26.068  -2.511  1.00 43.75           C  
-ANISOU 9605  CD  GLU D 931     5066   6551   5005    232    112   -670       C  
-ATOM   9606  OE1 GLU D 931    -118.928  25.747  -1.694  1.00 50.76           O  
-ANISOU 9606  OE1 GLU D 931     5911   7579   5797    261    127   -651       O  
-ATOM   9607  OE2 GLU D 931    -116.888  25.605  -2.471  1.00 52.84           O  
-ANISOU 9607  OE2 GLU D 931     6244   7655   6176    231    124   -642       O  
-ATOM   9608  N   LEU D 932    -122.309  27.606  -6.165  1.00 32.18           N  
-ANISOU 9608  N   LEU D 932     3648   4931   3648     62    113   -673       N  
-ATOM   9609  CA  LEU D 932    -123.716  27.920  -6.421  1.00 34.83           C  
-ANISOU 9609  CA  LEU D 932     3959   5323   3952     54    110   -685       C  
-ATOM   9610  C   LEU D 932    -124.527  26.638  -6.421  1.00 35.56           C  
-ANISOU 9610  C   LEU D 932     4064   5478   3971     -4    170   -593       C  
-ATOM   9611  O   LEU D 932    -124.059  25.577  -6.883  1.00 32.63           O  
-ANISOU 9611  O   LEU D 932     3744   5041   3613    -64    214   -515       O  
-ATOM   9612  CB  LEU D 932    -123.888  28.628  -7.769  1.00 33.69           C  
-ANISOU 9612  CB  LEU D 932     3844   5065   3893     22     95   -696       C  
-ATOM   9613  CG  LEU D 932    -123.215  29.996  -7.835  1.00 35.02           C  
-ANISOU 9613  CG  LEU D 932     3991   5160   4155     75     33   -778       C  
-ATOM   9614  CD1 LEU D 932    -123.271  30.557  -9.235  1.00 35.93           C  
-ANISOU 9614  CD1 LEU D 932     4136   5160   4355     38     29   -757       C  
-ATOM   9615  CD2 LEU D 932    -123.861  30.948  -6.861  1.00 36.12           C  
-ANISOU 9615  CD2 LEU D 932     4060   5395   4269    156    -21   -878       C  
-ATOM   9616  N   LYS D 933    -125.752  26.757  -5.951  1.00 35.30           N  
-ANISOU 9616  N   LYS D 933     3979   5563   3868     13    169   -605       N  
-ATOM   9617  CA  LYS D 933    -126.658  25.624  -5.916  1.00 39.12           C  
-ANISOU 9617  CA  LYS D 933     4461   6113   4292    -45    223   -517       C  
-ATOM   9618  C   LYS D 933    -127.713  25.682  -7.004  1.00 37.84           C  
-ANISOU 9618  C   LYS D 933     4310   5920   4147   -102    231   -509       C  
-ATOM   9619  O   LYS D 933    -128.353  24.673  -7.268  1.00 37.34           O  
-ANISOU 9619  O   LYS D 933     4255   5871   4061   -169    275   -437       O  
-ATOM   9620  CB  LYS D 933    -127.365  25.566  -4.563  1.00 38.86           C  
-ANISOU 9620  CB  LYS D 933     4350   6262   4154     10    224   -519       C  
-ATOM   9621  CG  LYS D 933    -126.443  25.325  -3.381  1.00 40.26           C  
-ANISOU 9621  CG  LYS D 933     4503   6503   4289     70    223   -513       C  
-ATOM   9622  CD  LYS D 933    -127.194  25.509  -2.048  1.00 44.29           C  
-ANISOU 9622  CD  LYS D 933     4922   7222   4686    147    215   -532       C  
-ATOM   9623  CE  LYS D 933    -126.394  26.208  -0.947  1.00 46.70           C  
-ANISOU 9623  CE  LYS D 933     5178   7608   4956    256    168   -620       C  
-ATOM   9624  NZ  LYS D 933    -127.137  26.721   0.272  1.00 48.19           N  
-ANISOU 9624  NZ  LYS D 933     5266   8010   5032    355    142   -679       N  
-ATOM   9625  N   HIS D 934    -127.918  26.853  -7.604  1.00 35.52           N  
-ANISOU 9625  N   HIS D 934     4012   5587   3896    -73    188   -582       N  
-ATOM   9626  CA  HIS D 934    -128.961  27.010  -8.610  1.00 36.45           C  
-ANISOU 9626  CA  HIS D 934     4133   5694   4022   -113    193   -579       C  
-ATOM   9627  C   HIS D 934    -128.467  27.874  -9.739  1.00 34.08           C  
-ANISOU 9627  C   HIS D 934     3869   5270   3810   -110    164   -613       C  
-ATOM   9628  O   HIS D 934    -127.476  28.565  -9.604  1.00 34.27           O  
-ANISOU 9628  O   HIS D 934     3901   5230   3891    -68    132   -651       O  
-ATOM   9629  CB  HIS D 934    -130.230  27.632  -7.984  1.00 36.62           C  
-ANISOU 9629  CB  HIS D 934     4082   5855   3975    -65    171   -627       C  
-ATOM   9630  CG  HIS D 934    -130.644  26.968  -6.718  1.00 39.67           C  
-ANISOU 9630  CG  HIS D 934     4417   6388   4269    -49    194   -594       C  
-ATOM   9631  ND1 HIS D 934    -131.255  25.729  -6.710  1.00 40.81           N  
-ANISOU 9631  ND1 HIS D 934     4558   6575   4372   -122    249   -502       N  
-ATOM   9632  CD2 HIS D 934    -130.488  27.328  -5.416  1.00 39.37           C  
-ANISOU 9632  CD2 HIS D 934     4323   6464   4173     33    172   -635       C  
-ATOM   9633  CE1 HIS D 934    -131.468  25.362  -5.456  1.00 41.49           C  
-ANISOU 9633  CE1 HIS D 934     4588   6798   4377    -87    263   -473       C  
-ATOM   9634  NE2 HIS D 934    -131.003  26.305  -4.654  1.00 40.60           N  
-ANISOU 9634  NE2 HIS D 934     4442   6739   4245     10    218   -555       N  
-ATOM   9635  N   ALA D 935    -129.192  27.842 -10.840  1.00 31.63           N  
-ANISOU 9635  N   ALA D 935     3573   4936   3510   -153    176   -595       N  
-ATOM   9636  CA  ALA D 935    -128.829  28.565 -12.043  1.00 32.24           C  
-ANISOU 9636  CA  ALA D 935     3679   4910   3662   -154    157   -605       C  
-ATOM   9637  C   ALA D 935    -128.527  30.042 -11.771  1.00 33.45           C  
-ANISOU 9637  C   ALA D 935     3803   5036   3871    -76     99   -674       C  
-ATOM   9638  O   ALA D 935    -129.226  30.706 -11.014  1.00 33.11           O  
-ANISOU 9638  O   ALA D 935     3707   5074   3797    -20     67   -733       O  
-ATOM   9639  CB  ALA D 935    -129.947  28.436 -13.084  1.00 29.52           C  
-ANISOU 9639  CB  ALA D 935     3331   4588   3296   -193    172   -588       C  
-ATOM   9640  N   SER D 936    -127.492  30.555 -12.433  1.00 33.14           N  
-ANISOU 9640  N   SER D 936     3793   4880   3919    -71     85   -667       N  
-ATOM   9641  CA  SER D 936    -127.109  31.942 -12.327  1.00 34.03           C  
-ANISOU 9641  CA  SER D 936     3879   4937   4115     -8     29   -723       C  
-ATOM   9642  C   SER D 936    -126.204  32.285 -13.514  1.00 33.48           C  
-ANISOU 9642  C   SER D 936     3843   4741   4138    -30     31   -675       C  
-ATOM   9643  O   SER D 936    -125.104  31.736 -13.655  1.00 33.15           O  
-ANISOU 9643  O   SER D 936     3836   4641   4121    -59     53   -638       O  
-ATOM   9644  CB  SER D 936    -126.357  32.171 -11.034  1.00 34.80           C  
-ANISOU 9644  CB  SER D 936     3952   5050   4221     42     -2   -781       C  
-ATOM   9645  OG  SER D 936    -126.192  33.566 -10.838  1.00 35.70           O  
-ANISOU 9645  OG  SER D 936     4028   5116   4421    107    -66   -855       O  
-ATOM   9646  N   HIS D 937    -126.701  33.150 -14.386  1.00 33.62           N  
-ANISOU 9646  N   HIS D 937     3847   4725   4202    -15     13   -668       N  
-ATOM   9647  CA  HIS D 937    -126.010  33.493 -15.623  1.00 33.42           C  
-ANISOU 9647  CA  HIS D 937     3843   4601   4253    -33     21   -605       C  
-ATOM   9648  C   HIS D 937    -124.906  34.495 -15.360  1.00 32.23           C  
-ANISOU 9648  C   HIS D 937     3676   4348   4223      3    -22   -624       C  
-ATOM   9649  O   HIS D 937    -125.114  35.694 -15.411  1.00 30.74           O  
-ANISOU 9649  O   HIS D 937     3451   4114   4115     48    -68   -651       O  
-ATOM   9650  CB  HIS D 937    -126.992  34.012 -16.664  1.00 37.04           C  
-ANISOU 9650  CB  HIS D 937     4289   5076   4710    -27     20   -578       C  
-ATOM   9651  CG  HIS D 937    -127.952  32.960 -17.123  1.00 42.75           C  
-ANISOU 9651  CG  HIS D 937     5027   5890   5325    -72     63   -555       C  
-ATOM   9652  ND1 HIS D 937    -129.099  33.245 -17.838  1.00 47.62           N  
-ANISOU 9652  ND1 HIS D 937     5624   6561   5909    -65     64   -548       N  
-ATOM   9653  CD2 HIS D 937    -127.951  31.616 -16.931  1.00 42.60           C  
-ANISOU 9653  CD2 HIS D 937     5038   5916   5233   -125    105   -542       C  
-ATOM   9654  CE1 HIS D 937    -129.748  32.121 -18.086  1.00 47.54           C  
-ANISOU 9654  CE1 HIS D 937     5628   6625   5810   -115    102   -537       C  
-ATOM   9655  NE2 HIS D 937    -129.067  31.119 -17.553  1.00 46.86           N  
-ANISOU 9655  NE2 HIS D 937     5573   6527   5704   -154    127   -531       N  
-ATOM   9656  N   ILE D 938    -123.725  33.972 -15.094  1.00 31.10           N  
-ANISOU 9656  N   ILE D 938     3556   4163   4097    -18     -8   -609       N  
-ATOM   9657  CA  ILE D 938    -122.579  34.783 -14.716  1.00 33.61           C  
-ANISOU 9657  CA  ILE D 938     3854   4389   4528      9    -48   -633       C  
-ATOM   9658  C   ILE D 938    -122.138  35.579 -15.924  1.00 33.11           C  
-ANISOU 9658  C   ILE D 938     3784   4226   4569      3    -53   -563       C  
-ATOM   9659  O   ILE D 938    -121.947  34.988 -16.970  1.00 35.26           O  
-ANISOU 9659  O   ILE D 938     4088   4498   4813    -37     -6   -480       O  
-ATOM   9660  CB  ILE D 938    -121.396  33.904 -14.279  1.00 32.90           C  
-ANISOU 9660  CB  ILE D 938     3792   4287   4420    -16    -24   -621       C  
-ATOM   9661  CG1 ILE D 938    -121.802  32.999 -13.123  1.00 31.85           C  
-ANISOU 9661  CG1 ILE D 938     3664   4260   4178    -11    -11   -666       C  
-ATOM   9662  CG2 ILE D 938    -120.211  34.778 -13.909  1.00 34.68           C  
-ANISOU 9662  CG2 ILE D 938     3988   4420   4767     10    -69   -651       C  
-ATOM   9663  CD1 ILE D 938    -122.338  33.744 -11.919  1.00 33.01           C  
-ANISOU 9663  CD1 ILE D 938     3758   4462   4321     53    -65   -768       C  
-ATOM   9664  N   SER D 939    -122.087  36.903 -15.795  1.00 35.61           N  
-ANISOU 9664  N   SER D 939     4056   4470   5005     46   -109   -595       N  
-ATOM   9665  CA  SER D 939    -121.443  37.761 -16.796  1.00 39.27           C  
-ANISOU 9665  CA  SER D 939     4502   4822   5596     41   -118   -517       C  
-ATOM   9666  C   SER D 939    -120.084  38.194 -16.295  1.00 36.93           C  
-ANISOU 9666  C   SER D 939     4185   4432   5415     43   -149   -537       C  
-ATOM   9667  O   SER D 939    -119.171  38.311 -17.073  1.00 38.90           O  
-ANISOU 9667  O   SER D 939     4434   4612   5733     16   -131   -451       O  
-ATOM   9668  CB  SER D 939    -122.282  38.968 -17.176  1.00 41.81           C  
-ANISOU 9668  CB  SER D 939     4784   5107   5996     82   -157   -517       C  
-ATOM   9669  OG  SER D 939    -123.485  38.534 -17.790  1.00 53.01           O  
-ANISOU 9669  OG  SER D 939     6220   6619   7304     77   -124   -489       O  
-ATOM   9670  N   LYS D 940    -119.953  38.412 -14.990  1.00 36.30           N  
-ANISOU 9670  N   LYS D 940     4082   4361   5350     78   -197   -651       N  
-ATOM   9671  CA  LYS D 940    -118.677  38.699 -14.375  1.00 35.18           C  
-ANISOU 9671  CA  LYS D 940     3917   4148   5303     82   -229   -689       C  
-ATOM   9672  C   LYS D 940    -118.686  38.057 -12.995  1.00 33.92           C  
-ANISOU 9672  C   LYS D 940     3759   4082   5046    107   -241   -795       C  
-ATOM   9673  O   LYS D 940    -119.630  38.231 -12.219  1.00 35.35           O  
-ANISOU 9673  O   LYS D 940     3920   4337   5173    152   -270   -882       O  
-ATOM   9674  CB  LYS D 940    -118.418  40.225 -14.262  1.00 35.36           C  
-ANISOU 9674  CB  LYS D 940     3876   4044   5514    118   -305   -732       C  
-ATOM   9675  N   LEU D 941    -117.627  37.344 -12.682  1.00 32.73           N  
-ANISOU 9675  N   LEU D 941     3627   3937   4873     85   -219   -783       N  
-ATOM   9676  CA  LEU D 941    -117.466  36.734 -11.371  1.00 34.85           C  
-ANISOU 9676  CA  LEU D 941     3892   4296   5054    113   -228   -869       C  
-ATOM   9677  C   LEU D 941    -117.327  37.791 -10.272  1.00 35.89           C  
-ANISOU 9677  C   LEU D 941     3957   4410   5271    179   -313  -1006       C  
-ATOM   9678  O   LEU D 941    -116.818  38.856 -10.519  1.00 35.70           O  
-ANISOU 9678  O   LEU D 941     3894   4269   5402    187   -362  -1024       O  
-ATOM   9679  CB  LEU D 941    -116.235  35.828 -11.366  1.00 33.17           C  
-ANISOU 9679  CB  LEU D 941     3710   4079   4815     78   -188   -821       C  
-ATOM   9680  CG  LEU D 941    -116.396  34.539 -12.167  1.00 34.23           C  
-ANISOU 9680  CG  LEU D 941     3910   4256   4840     24   -108   -716       C  
-ATOM   9681  CD1 LEU D 941    -115.053  33.790 -12.277  1.00 35.05           C  
-ANISOU 9681  CD1 LEU D 941     4039   4335   4942     -4    -76   -668       C  
-ATOM   9682  CD2 LEU D 941    -117.429  33.642 -11.512  1.00 34.14           C  
-ANISOU 9682  CD2 LEU D 941     3919   4369   4685     33    -82   -739       C  
-ATOM   9683  N   PRO D 942    -117.779  37.482  -9.054  1.00 37.93           N  
-ANISOU 9683  N   PRO D 942     4196   4789   5428    230   -331  -1101       N  
-ATOM   9684  CA  PRO D 942    -117.349  38.326  -7.926  1.00 38.48           C  
-ANISOU 9684  CA  PRO D 942     4198   4855   5569    298   -413  -1243       C  
-ATOM   9685  C   PRO D 942    -115.816  38.470  -7.875  1.00 38.36           C  
-ANISOU 9685  C   PRO D 942     4168   4749   5657    280   -431  -1245       C  
-ATOM   9686  O   PRO D 942    -115.080  37.498  -8.138  1.00 35.49           O  
-ANISOU 9686  O   PRO D 942     3848   4399   5237    234   -372  -1161       O  
-ATOM   9687  CB  PRO D 942    -117.849  37.564  -6.684  1.00 37.84           C  
-ANISOU 9687  CB  PRO D 942     4105   4950   5321    347   -405  -1310       C  
-ATOM   9688  CG  PRO D 942    -118.931  36.667  -7.188  1.00 39.24           C  
-ANISOU 9688  CG  PRO D 942     4334   5207   5369    310   -334  -1216       C  
-ATOM   9689  CD  PRO D 942    -118.589  36.330  -8.616  1.00 38.01           C  
-ANISOU 9689  CD  PRO D 942     4236   4946   5260    228   -279  -1082       C  
-ATOM   9690  N   LYS D 943    -115.341  39.670  -7.566  1.00 37.93           N  
-ANISOU 9690  N   LYS D 943     4050   4600   5761    314   -512  -1340       N  
-ATOM   9691  CA  LYS D 943    -113.905  39.922  -7.514  1.00 37.44           C  
-ANISOU 9691  CA  LYS D 943     3963   4448   5816    295   -536  -1349       C  
-ATOM   9692  C   LYS D 943    -113.310  38.958  -6.530  1.00 35.15           C  
-ANISOU 9692  C   LYS D 943     3677   4281   5397    317   -518  -1388       C  
-ATOM   9693  O   LYS D 943    -113.891  38.709  -5.470  1.00 35.73           O  
-ANISOU 9693  O   LYS D 943     3731   4490   5356    380   -535  -1480       O  
-ATOM   9694  CB  LYS D 943    -113.641  41.365  -7.084  1.00 43.39           C  
-ANISOU 9694  CB  LYS D 943     4634   5095   6757    340   -640  -1478       C  
-ATOM   9695  CG  LYS D 943    -114.094  42.368  -8.161  1.00 46.73           C  
-ANISOU 9695  CG  LYS D 943     5049   5372   7334    314   -657  -1414       C  
-ATOM   9696  CD  LYS D 943    -113.682  43.790  -7.869  1.00 52.59           C  
-ANISOU 9696  CD  LYS D 943     5710   5973   8299    346   -760  -1523       C  
-ATOM   9697  CE  LYS D 943    -114.280  44.721  -8.942  1.00 52.59           C  
-ANISOU 9697  CE  LYS D 943     5705   5836   8440    326   -770  -1442       C  
-ATOM   9698  NZ  LYS D 943    -113.828  46.134  -8.774  1.00 56.60           N  
-ANISOU 9698  NZ  LYS D 943     6131   6175   9199    348   -870  -1529       N  
-ATOM   9699  N   GLY D 944    -112.175  38.381  -6.878  1.00 33.15           N  
-ANISOU 9699  N   GLY D 944     3449   3993   5155    269   -479  -1312       N  
-ATOM   9700  CA  GLY D 944    -111.564  37.381  -6.032  1.00 34.04           C  
-ANISOU 9700  CA  GLY D 944     3571   4219   5144    289   -454  -1330       C  
-ATOM   9701  C   GLY D 944    -111.939  35.931  -6.303  1.00 34.55           C  
-ANISOU 9701  C   GLY D 944     3713   4378   5038    256   -361  -1215       C  
-ATOM   9702  O   GLY D 944    -111.294  35.024  -5.781  1.00 35.10           O  
-ANISOU 9702  O   GLY D 944     3798   4520   5019    262   -331  -1200       O  
-ATOM   9703  N   LYS D 945    -112.981  35.699  -7.096  1.00 34.28           N  
-ANISOU 9703  N   LYS D 945     3723   4342   4959    223   -318  -1138       N  
-ATOM   9704  CA  LYS D 945    -113.377  34.331  -7.504  1.00 33.93           C  
-ANISOU 9704  CA  LYS D 945     3750   4366   4776    182   -233  -1027       C  
-ATOM   9705  C   LYS D 945    -112.833  34.081  -8.880  1.00 31.05           C  
-ANISOU 9705  C   LYS D 945     3432   3900   4466    112   -186   -907       C  
-ATOM   9706  O   LYS D 945    -112.870  34.976  -9.726  1.00 30.41           O  
-ANISOU 9706  O   LYS D 945     3336   3719   4500     92   -206   -884       O  
-ATOM   9707  CB  LYS D 945    -114.904  34.222  -7.537  1.00 36.07           C  
-ANISOU 9707  CB  LYS D 945     4033   4709   4963    190   -218  -1025       C  
-ATOM   9708  CG  LYS D 945    -115.544  34.506  -6.178  1.00 38.31           C  
-ANISOU 9708  CG  LYS D 945     4263   5114   5180    268   -265  -1144       C  
-ATOM   9709  CD  LYS D 945    -115.293  33.363  -5.238  1.00 36.94           C  
-ANISOU 9709  CD  LYS D 945     4097   5068   4870    288   -229  -1132       C  
-ATOM   9710  CE  LYS D 945    -116.142  33.512  -3.993  1.00 38.37           C  
-ANISOU 9710  CE  LYS D 945     4223   5401   4955    366   -261  -1226       C  
-ATOM   9711  NZ  LYS D 945    -115.884  32.378  -3.065  1.00 40.46           N  
-ANISOU 9711  NZ  LYS D 945     4489   5798   5084    389   -222  -1196       N  
-ATOM   9712  N   HIS D 946    -112.409  32.856  -9.150  1.00 30.34           N  
-ANISOU 9712  N   HIS D 946     3396   3841   4292     79   -122   -826       N  
-ATOM   9713  CA  HIS D 946    -111.882  32.530 -10.483  1.00 31.01           C  
-ANISOU 9713  CA  HIS D 946     3522   3849   4413     20    -76   -716       C  
-ATOM   9714  C   HIS D 946    -112.701  31.515 -11.285  1.00 28.96           C  
-ANISOU 9714  C   HIS D 946     3325   3624   4055    -19    -11   -632       C  
-ATOM   9715  O   HIS D 946    -112.426  31.267 -12.471  1.00 27.35           O  
-ANISOU 9715  O   HIS D 946     3151   3371   3870    -60     26   -549       O  
-ATOM   9716  CB  HIS D 946    -110.457  32.037 -10.340  1.00 31.36           C  
-ANISOU 9716  CB  HIS D 946     3570   3876   4468     15    -63   -696       C  
-ATOM   9717  CG  HIS D 946    -109.633  32.897  -9.452  1.00 35.74           C  
-ANISOU 9717  CG  HIS D 946     4060   4410   5110     54   -128   -790       C  
-ATOM   9718  ND1 HIS D 946    -109.490  32.641  -8.105  1.00 35.32           N  
-ANISOU 9718  ND1 HIS D 946     3981   4447   4992    107   -153   -876       N  
-ATOM   9719  CD2 HIS D 946    -108.972  34.055  -9.693  1.00 36.92           C  
-ANISOU 9719  CD2 HIS D 946     4155   4461   5412     51   -178   -816       C  
-ATOM   9720  CE1 HIS D 946    -108.762  33.594  -7.555  1.00 37.36           C  
-ANISOU 9720  CE1 HIS D 946     4174   4668   5355    137   -219   -965       C  
-ATOM   9721  NE2 HIS D 946    -108.432  34.459  -8.502  1.00 38.95           N  
-ANISOU 9721  NE2 HIS D 946     4356   4745   5696    100   -236   -929       N  
-ATOM   9722  N   SER D 947    -113.689  30.925 -10.654  1.00 27.89           N  
-ANISOU 9722  N   SER D 947     3202   3578   3815     -6      3   -654       N  
-ATOM   9723  CA  SER D 947    -114.506  29.911 -11.319  1.00 26.30           C  
-ANISOU 9723  CA  SER D 947     3054   3411   3528    -47     60   -585       C  
-ATOM   9724  C   SER D 947    -115.837  29.745 -10.587  1.00 28.98           C  
-ANISOU 9724  C   SER D 947     3383   3845   3785    -28     56   -623       C  
-ATOM   9725  O   SER D 947    -116.015  30.247  -9.453  1.00 29.74           O  
-ANISOU 9725  O   SER D 947     3433   3999   3870     24     15   -701       O  
-ATOM   9726  CB  SER D 947    -113.767  28.596 -11.286  1.00 25.49           C  
-ANISOU 9726  CB  SER D 947     2996   3322   3365    -66    107   -533       C  
-ATOM   9727  OG  SER D 947    -113.533  28.170  -9.963  1.00 26.59           O  
-ANISOU 9727  OG  SER D 947     3122   3534   3449    -29     99   -572       O  
-ATOM   9728  N   VAL D 948    -116.758  29.018 -11.205  1.00 27.63           N  
-ANISOU 9728  N   VAL D 948     3247   3700   3552    -67     98   -571       N  
-ATOM   9729  CA  VAL D 948    -117.968  28.609 -10.526  1.00 27.95           C  
-ANISOU 9729  CA  VAL D 948     3277   3839   3504    -59    107   -588       C  
-ATOM   9730  C   VAL D 948    -117.909  27.109 -10.289  1.00 27.64           C  
-ANISOU 9730  C   VAL D 948     3278   3839   3386    -90    160   -529       C  
-ATOM   9731  O   VAL D 948    -117.462  26.345 -11.160  1.00 28.85           O  
-ANISOU 9731  O   VAL D 948     3478   3936   3548   -133    196   -470       O  
-ATOM   9732  CB  VAL D 948    -119.224  28.955 -11.355  1.00 28.46           C  
-ANISOU 9732  CB  VAL D 948     3341   3909   3565    -81    110   -578       C  
-ATOM   9733  CG1 VAL D 948    -120.441  28.216 -10.826  1.00 28.63           C  
-ANISOU 9733  CG1 VAL D 948     3358   4032   3488    -91    134   -572       C  
-ATOM   9734  CG2 VAL D 948    -119.477  30.446 -11.329  1.00 28.10           C  
-ANISOU 9734  CG2 VAL D 948     3247   3837   3592    -39     53   -641       C  
-ATOM   9735  N   LYS D 949    -118.354  26.700  -9.109  1.00 26.60           N  
-ANISOU 9735  N   LYS D 949     3121   3805   3180    -63    163   -544       N  
-ATOM   9736  CA  LYS D 949    -118.625  25.318  -8.836  1.00 27.10           C  
-ANISOU 9736  CA  LYS D 949     3213   3912   3174    -94    212   -478       C  
-ATOM   9737  C   LYS D 949    -120.134  25.184  -8.589  1.00 29.84           C  
-ANISOU 9737  C   LYS D 949     3534   4346   3459   -105    222   -474       C  
-ATOM   9738  O   LYS D 949    -120.653  25.728  -7.617  1.00 28.05           O  
-ANISOU 9738  O   LYS D 949     3254   4215   3190    -55    196   -522       O  
-ATOM   9739  CB  LYS D 949    -117.896  24.849  -7.616  1.00 27.09           C  
-ANISOU 9739  CB  LYS D 949     3194   3968   3129    -52    215   -475       C  
-ATOM   9740  CG  LYS D 949    -118.199  23.400  -7.289  1.00 29.60           C  
-ANISOU 9740  CG  LYS D 949     3536   4325   3385    -83    268   -391       C  
-ATOM   9741  CD  LYS D 949    -117.433  22.944  -6.076  1.00 32.14           C  
-ANISOU 9741  CD  LYS D 949     3839   4712   3662    -34    273   -376       C  
-ATOM   9742  CE  LYS D 949    -117.743  21.494  -5.775  1.00 36.57           C  
-ANISOU 9742  CE  LYS D 949     4421   5299   4174    -67    327   -277       C  
-ATOM   9743  NZ  LYS D 949    -117.150  21.098  -4.472  1.00 41.32           N  
-ANISOU 9743  NZ  LYS D 949     4992   5992   4717     -7    332   -252       N  
-ATOM   9744  N   GLY D 950    -120.819  24.448  -9.468  1.00 30.20           N  
-ANISOU 9744  N   GLY D 950     3613   4364   3497   -169    258   -423       N  
-ATOM   9745  CA  GLY D 950    -122.196  24.030  -9.214  1.00 30.85           C  
-ANISOU 9745  CA  GLY D 950     3671   4530   3519   -192    276   -403       C  
-ATOM   9746  C   GLY D 950    -122.169  22.861  -8.242  1.00 31.32           C  
-ANISOU 9746  C   GLY D 950     3727   4650   3524   -198    312   -340       C  
-ATOM   9747  O   GLY D 950    -121.549  21.844  -8.519  1.00 30.78           O  
-ANISOU 9747  O   GLY D 950     3703   4519   3475   -234    344   -284       O  
-ATOM   9748  N   LEU D 951    -122.822  23.014  -7.097  1.00 32.37           N  
-ANISOU 9748  N   LEU D 951     3802   4910   3588   -158    306   -348       N  
-ATOM   9749  CA  LEU D 951    -122.726  22.038  -6.010  1.00 33.78           C  
-ANISOU 9749  CA  LEU D 951     3961   5165   3707   -149    339   -279       C  
-ATOM   9750  C   LEU D 951    -123.671  20.878  -6.205  1.00 34.99           C  
-ANISOU 9750  C   LEU D 951     4120   5330   3845   -220    386   -192       C  
-ATOM   9751  O   LEU D 951    -124.882  21.057  -6.133  1.00 34.24           O  
-ANISOU 9751  O   LEU D 951     3985   5312   3714   -234    387   -194       O  
-ATOM   9752  CB  LEU D 951    -123.043  22.719  -4.683  1.00 36.46           C  
-ANISOU 9752  CB  LEU D 951     4224   5657   3970    -66    312   -323       C  
-ATOM   9753  CG  LEU D 951    -122.079  23.840  -4.303  1.00 37.51           C  
-ANISOU 9753  CG  LEU D 951     4341   5786   4126     11    258   -421       C  
-ATOM   9754  CD1 LEU D 951    -122.467  24.476  -2.976  1.00 37.62           C  
-ANISOU 9754  CD1 LEU D 951     4271   5965   4058    101    227   -480       C  
-ATOM   9755  CD2 LEU D 951    -120.666  23.278  -4.219  1.00 37.16           C  
-ANISOU 9755  CD2 LEU D 951     4335   5672   4111     15    271   -389       C  
-ATOM   9756  N   GLY D 952    -123.126  19.683  -6.420  1.00 35.71           N  
-ANISOU 9756  N   GLY D 952     4256   5345   3968   -266    423   -115       N  
-ATOM   9757  CA  GLY D 952    -123.957  18.475  -6.484  1.00 39.65           C  
-ANISOU 9757  CA  GLY D 952     4753   5843   4468   -336    466    -26       C  
-ATOM   9758  C   GLY D 952    -124.325  17.877  -5.124  1.00 40.99           C  
-ANISOU 9758  C   GLY D 952     4865   6138   4570   -314    494     59       C  
-ATOM   9759  O   GLY D 952    -123.713  18.196  -4.106  1.00 40.23           O  
-ANISOU 9759  O   GLY D 952     4739   6124   4421   -238    485     55       O  
-ATOM   9760  N   LYS D 953    -125.333  17.009  -5.112  1.00 44.72           N  
-ANISOU 9760  N   LYS D 953     5316   6632   5045   -378    529    139       N  
-ATOM   9761  CA  LYS D 953    -125.685  16.218  -3.903  1.00 47.91           C  
-ANISOU 9761  CA  LYS D 953     5662   7144   5396   -370    567    254       C  
-ATOM   9762  C   LYS D 953    -124.654  15.145  -3.599  1.00 44.05           C  
-ANISOU 9762  C   LYS D 953     5210   6580   4945   -373    596    343       C  
-ATOM   9763  O   LYS D 953    -124.482  14.736  -2.443  1.00 42.19           O  
-ANISOU 9763  O   LYS D 953     4931   6445   4655   -330    620    429       O  
-ATOM   9764  CB  LYS D 953    -127.048  15.548  -4.084  1.00 54.53           C  
-ANISOU 9764  CB  LYS D 953     6465   8008   6248   -451    596    322       C  
-ATOM   9765  CG  LYS D 953    -128.184  16.538  -4.205  1.00 63.32           C  
-ANISOU 9765  CG  LYS D 953     7528   9224   7308   -441    572    249       C  
-ATOM   9766  CD  LYS D 953    -129.541  15.860  -4.335  1.00 69.40           C  
-ANISOU 9766  CD  LYS D 953     8251  10030   8088   -522    601    320       C  
-ATOM   9767  CE  LYS D 953    -130.642  16.877  -4.576  1.00 79.32           C  
-ANISOU 9767  CE  LYS D 953     9462  11384   9293   -509    574    237       C  
-ATOM   9768  NZ  LYS D 953    -131.212  17.419  -3.306  1.00 83.37           N  
-ANISOU 9768  NZ  LYS D 953     9883  12104   9691   -435    575    254       N  
-ATOM   9769  N   THR D 954    -123.977  14.698  -4.654  1.00 41.23           N  
-ANISOU 9769  N   THR D 954     4931   6055   4679   -418    593    321       N  
-ATOM   9770  CA  THR D 954    -122.958  13.692  -4.537  1.00 43.96           C  
-ANISOU 9770  CA  THR D 954     5321   6310   5073   -420    616    392       C  
-ATOM   9771  C   THR D 954    -121.645  14.266  -5.043  1.00 44.75           C  
-ANISOU 9771  C   THR D 954     5477   6333   5192   -375    585    305       C  
-ATOM   9772  O   THR D 954    -121.608  14.955  -6.077  1.00 47.01           O  
-ANISOU 9772  O   THR D 954     5797   6557   5510   -389    557    210       O  
-ATOM   9773  CB  THR D 954    -123.343  12.462  -5.378  1.00 44.91           C  
-ANISOU 9773  CB  THR D 954     5477   6291   5294   -518    640    448       C  
-ATOM   9774  OG1 THR D 954    -124.598  11.952  -4.926  1.00 44.90           O  
-ANISOU 9774  OG1 THR D 954     5415   6359   5286   -568    667    532       O  
-ATOM   9775  CG2 THR D 954    -122.300  11.375  -5.269  1.00 45.68           C  
-ANISOU 9775  CG2 THR D 954     5620   6284   5451   -517    661    520       C  
-ATOM   9776  N   THR D 955    -120.582  13.999  -4.294  1.00 47.47           N  
-ANISOU 9776  N   THR D 955     5827   6694   5517   -317    593    343       N  
-ATOM   9777  CA  THR D 955    -119.266  14.493  -4.611  1.00 48.70           C  
-ANISOU 9777  CA  THR D 955     6025   6790   5687   -270    567    272       C  
-ATOM   9778  C   THR D 955    -118.261  13.361  -4.433  1.00 53.57           C  
-ANISOU 9778  C   THR D 955     6681   7330   6341   -264    593    352       C  
-ATOM   9779  O   THR D 955    -118.485  12.474  -3.621  1.00 51.55           O  
-ANISOU 9779  O   THR D 955     6400   7115   6071   -264    627    463       O  
-ATOM   9780  CB  THR D 955    -118.872  15.678  -3.723  1.00 49.77           C  
-ANISOU 9780  CB  THR D 955     6113   7054   5745   -179    534    206       C  
-ATOM   9781  OG1 THR D 955    -117.626  16.197  -4.187  1.00 53.38           O  
-ANISOU 9781  OG1 THR D 955     6609   7438   6235   -147    506    133       O  
-ATOM   9782  CG2 THR D 955    -118.695  15.275  -2.243  1.00 50.03           C  
-ANISOU 9782  CG2 THR D 955     6089   7221   5698   -115    556    287       C  
-ATOM   9783  N   PRO D 956    -117.170  13.356  -5.230  1.00 59.95           N  
-ANISOU 9783  N   PRO D 956     7550   8027   7201   -258    579    302       N  
-ATOM   9784  CA  PRO D 956    -116.143  12.343  -4.973  1.00 59.72           C  
-ANISOU 9784  CA  PRO D 956     7555   7937   7200   -238    600    371       C  
-ATOM   9785  C   PRO D 956    -115.568  12.505  -3.562  1.00 58.23           C  
-ANISOU 9785  C   PRO D 956     7318   7877   6930   -152    605    414       C  
-ATOM   9786  O   PRO D 956    -115.345  13.625  -3.118  1.00 55.72           O  
-ANISOU 9786  O   PRO D 956     6964   7656   6553    -95    574    338       O  
-ATOM   9787  CB  PRO D 956    -115.089  12.633  -6.060  1.00 59.46           C  
-ANISOU 9787  CB  PRO D 956     7580   7796   7216   -234    577    288       C  
-ATOM   9788  CG  PRO D 956    -115.865  13.268  -7.185  1.00 61.94           C  
-ANISOU 9788  CG  PRO D 956     7904   8073   7558   -286    557    210       C  
-ATOM   9789  CD  PRO D 956    -116.852  14.142  -6.445  1.00 61.40           C  
-ANISOU 9789  CD  PRO D 956     7771   8134   7422   -273    547    195       C  
-ATOM   9790  N   ASP D 957    -115.328  11.387  -2.886  1.00 56.88           N  
-ANISOU 9790  N   ASP D 957     7144   7705   6762   -141    640    533       N  
-ATOM   9791  CA  ASP D 957    -114.822  11.386  -1.522  1.00 58.50           C  
-ANISOU 9791  CA  ASP D 957     7299   8046   6883    -55    650    590       C  
-ATOM   9792  C   ASP D 957    -113.486  12.127  -1.410  1.00 58.29           C  
-ANISOU 9792  C   ASP D 957     7281   8039   6827     20    617    501       C  
-ATOM   9793  O   ASP D 957    -112.492  11.662  -1.939  1.00 51.53           O  
-ANISOU 9793  O   ASP D 957     6480   7075   6024     21    618    499       O  
-ATOM   9794  CB  ASP D 957    -114.635   9.943  -1.070  1.00 63.35           C  
-ANISOU 9794  CB  ASP D 957     7922   8617   7530    -62    695    742       C  
-ATOM   9795  CG  ASP D 957    -114.269   9.824   0.398  1.00 68.32           C  
-ANISOU 9795  CG  ASP D 957     8489   9408   8062     29    713    828       C  
-ATOM   9796  OD1 ASP D 957    -113.882  10.831   1.029  1.00 66.80           O  
-ANISOU 9796  OD1 ASP D 957     8253   9351   7779    106    685    750       O  
-ATOM   9797  OD2 ASP D 957    -114.376   8.694   0.918  1.00 75.27           O  
-ANISOU 9797  OD2 ASP D 957     9358  10279   8961     24    755    976       O  
-ATOM   9798  N   PRO D 958    -113.462  13.271  -0.704  1.00 63.67           N  
-ANISOU 9798  N   PRO D 958     7904   8861   7428     84    585    424       N  
-ATOM   9799  CA  PRO D 958    -112.239  14.079  -0.585  1.00 65.27           C  
-ANISOU 9799  CA  PRO D 958     8104   9082   7614    151    547    328       C  
-ATOM   9800  C   PRO D 958    -111.044  13.332   0.019  1.00 64.66           C  
-ANISOU 9800  C   PRO D 958     8034   9016   7518    211    564    392       C  
-ATOM   9801  O   PRO D 958    -109.917  13.676  -0.273  1.00 61.36           O  
-ANISOU 9801  O   PRO D 958     7639   8555   7121    240    540    326       O  
-ATOM   9802  CB  PRO D 958    -112.657  15.227   0.336  1.00 63.06           C  
-ANISOU 9802  CB  PRO D 958     7742   8971   7247    215    513    252       C  
-ATOM   9803  CG  PRO D 958    -114.136  15.294   0.242  1.00 63.16           C  
-ANISOU 9803  CG  PRO D 958     7731   9018   7247    164    525    275       C  
-ATOM   9804  CD  PRO D 958    -114.612  13.905  -0.029  1.00 66.50           C  
-ANISOU 9804  CD  PRO D 958     8190   9363   7713     97    579    413       C  
-ATOM   9805  N   SER D 959    -111.290  12.320   0.842  1.00 71.64           N  
-ANISOU 9805  N   SER D 959     8897   9959   8366    230    606    526       N  
-ATOM   9806  CA  SER D 959    -110.195  11.563   1.467  1.00 75.20           C  
-ANISOU 9806  CA  SER D 959     9350  10427   8794    294    624    601       C  
-ATOM   9807  C   SER D 959    -109.445  10.713   0.444  1.00 77.75           C  
-ANISOU 9807  C   SER D 959     9760  10560   9219    250    637    623       C  
-ATOM   9808  O   SER D 959    -108.300  10.314   0.685  1.00 75.54           O  
-ANISOU 9808  O   SER D 959     9495  10271   8935    304    640    645       O  
-ATOM   9809  CB  SER D 959    -110.709  10.659   2.604  1.00 71.97           C  
-ANISOU 9809  CB  SER D 959     8890  10130   8324    326    670    761       C  
-ATOM   9810  N   ALA D 960    -110.098  10.413  -0.684  1.00 78.71           N  
-ANISOU 9810  N   ALA D 960     9935  10542   9430    157    644    615       N  
-ATOM   9811  CA  ALA D 960    -109.465   9.646  -1.755  1.00 79.47           C  
-ANISOU 9811  CA  ALA D 960    10109  10463   9622    118    650    617       C  
-ATOM   9812  C   ALA D 960    -108.847  10.528  -2.843  1.00 74.79           C  
-ANISOU 9812  C   ALA D 960     9552   9803   9063    104    612    480       C  
-ATOM   9813  O   ALA D 960    -108.300   9.999  -3.799  1.00 80.29           O  
-ANISOU 9813  O   ALA D 960    10307  10371   9828     79    613    467       O  
-ATOM   9814  CB  ALA D 960    -110.457   8.667  -2.367  1.00 82.14           C  
-ANISOU 9814  CB  ALA D 960    10479  10685  10043     31    677    687       C  
-ATOM   9815  N   ASN D 961    -108.924  11.854  -2.713  1.00 68.55           N  
-ANISOU 9815  N   ASN D 961     8721   9097   8227    124    577    382       N  
-ATOM   9816  CA  ASN D 961    -108.258  12.747  -3.660  1.00 70.36           C  
-ANISOU 9816  CA  ASN D 961     8972   9269   8492    116    542    269       C  
-ATOM   9817  C   ASN D 961    -106.768  12.457  -3.641  1.00 67.49           C  
-ANISOU 9817  C   ASN D 961     8629   8880   8135    169    539    267       C  
-ATOM   9818  O   ASN D 961    -106.206  12.194  -2.584  1.00 66.01           O  
-ANISOU 9818  O   ASN D 961     8411   8777   7893    237    546    310       O  
-ATOM   9819  CB  ASN D 961    -108.496  14.236  -3.345  1.00 73.10           C  
-ANISOU 9819  CB  ASN D 961     9263   9712   8801    139    501    170       C  
-ATOM   9820  CG  ASN D 961    -109.923  14.714  -3.726  1.00 78.66           C  
-ANISOU 9820  CG  ASN D 961     9955  10420   9512     80    497    147       C  
-ATOM   9821  OD1 ASN D 961    -110.889  13.943  -3.765  1.00 81.41           O  
-ANISOU 9821  OD1 ASN D 961    10313  10751   9866     35    527    219       O  
-ATOM   9822  ND2 ASN D 961    -110.039  15.994  -4.053  1.00 81.81           N  
-ANISOU 9822  ND2 ASN D 961    10330  10835   9919     80    458     48       N  
-ATOM   9823  N   ILE D 962    -106.146  12.471  -4.814  1.00 58.99           N  
-ANISOU 9823  N   ILE D 962     7599   7696   7119    143    531    220       N  
-ATOM   9824  CA  ILE D 962    -104.706  12.304  -4.925  1.00 59.01           C  
-ANISOU 9824  CA  ILE D 962     7616   7676   7128    191    525    207       C  
-ATOM   9825  C   ILE D 962    -104.114  13.430  -5.779  1.00 63.16           C  
-ANISOU 9825  C   ILE D 962     8135   8180   7682    181    492    107       C  
-ATOM   9826  O   ILE D 962    -104.812  14.016  -6.593  1.00 68.91           O  
-ANISOU 9826  O   ILE D 962     8869   8871   8442    127    481     65       O  
-ATOM   9827  CB  ILE D 962    -104.334  10.944  -5.554  1.00 57.99           C  
-ANISOU 9827  CB  ILE D 962     7552   7433   7050    178    554    267       C  
-ATOM   9828  CG1 ILE D 962    -104.895  10.821  -6.998  1.00 54.94           C  
-ANISOU 9828  CG1 ILE D 962     7211   6934   6729    105    553    230       C  
-ATOM   9829  CG2 ILE D 962    -104.763   9.802  -4.643  1.00 59.28           C  
-ANISOU 9829  CG2 ILE D 962     7715   7609   7199    193    587    382       C  
-ATOM   9830  CD1 ILE D 962    -103.789  10.815  -7.998  1.00 56.13           C  
-ANISOU 9830  CD1 ILE D 962     7392   7024   6911    119    544    182       C  
-ATOM   9831  N   SER D 963    -102.836  13.748  -5.582  1.00 62.90           N  
-ANISOU 9831  N   SER D 963     8085   8174   7641    233    475     76       N  
-ATOM   9832  CA  SER D 963    -102.171  14.780  -6.378  1.00 61.54           C  
-ANISOU 9832  CA  SER D 963     7899   7978   7507    222    446     -2       C  
-ATOM   9833  C   SER D 963    -101.321  14.083  -7.424  1.00 61.43           C  
-ANISOU 9833  C   SER D 963     7934   7877   7529    217    462     13       C  
-ATOM   9834  O   SER D 963    -100.467  13.270  -7.087  1.00 66.78           O  
-ANISOU 9834  O   SER D 963     8627   8556   8191    263    476     50       O  
-ATOM   9835  CB  SER D 963    -101.373  15.757  -5.497  1.00 58.27           C  
-ANISOU 9835  CB  SER D 963     7418   7655   7068    277    410    -60       C  
-ATOM   9836  N   LEU D 964    -101.584  14.391  -8.695  1.00 67.94           N  
-ANISOU 9836  N   LEU D 964     8780   8636   8399    166    460    -16       N  
-ATOM   9837  CA  LEU D 964    -100.885  13.794  -9.845  1.00 74.54           C  
-ANISOU 9837  CA  LEU D 964     9657   9401   9264    163    473    -12       C  
-ATOM   9838  C   LEU D 964    -100.118  14.925 -10.511  1.00 83.56           C  
-ANISOU 9838  C   LEU D 964    10762  10556  10431    161    451    -61       C  
-ATOM   9839  O   LEU D 964    -100.716  15.854 -11.084  1.00 83.12           O  
-ANISOU 9839  O   LEU D 964    10687  10495  10401    119    437    -91       O  
-ATOM   9840  CB  LEU D 964    -101.850  13.161 -10.849  1.00 74.21           C  
-ANISOU 9840  CB  LEU D 964     9662   9286   9248    110    490     -3       C  
-ATOM   9841  CG  LEU D 964    -101.267  12.554 -12.118  1.00 73.89           C  
-ANISOU 9841  CG  LEU D 964     9658   9183   9232    112    499    -14       C  
-ATOM   9842  CD1 LEU D 964    -100.374  11.383 -11.762  1.00 79.63           C  
-ANISOU 9842  CD1 LEU D 964    10415   9885   9955    164    514     20       C  
-ATOM   9843  CD2 LEU D 964    -102.398  12.110 -13.016  1.00 70.36           C  
-ANISOU 9843  CD2 LEU D 964     9244   8680   8809     59    507    -23       C  
-ATOM   9844  N   ASP D 965     -98.794  14.857 -10.390  1.00 87.45           N  
-ANISOU 9844  N   ASP D 965    11240  11068  10918    207    447    -63       N  
-ATOM   9845  CA  ASP D 965     -97.889  15.857 -10.910  1.00 85.29           C  
-ANISOU 9845  CA  ASP D 965    10922  10811  10675    209    428    -97       C  
-ATOM   9846  C   ASP D 965     -98.368  17.270 -10.547  1.00 74.00           C  
-ANISOU 9846  C   ASP D 965     9435   9410   9272    183    395   -139       C  
-ATOM   9847  O   ASP D 965     -98.416  18.174 -11.386  1.00 69.23           O  
-ANISOU 9847  O   ASP D 965     8806   8785   8713    148    382   -156       O  
-ATOM   9848  CB  ASP D 965     -97.685  15.607 -12.398  1.00 93.68           C  
-ANISOU 9848  CB  ASP D 965    12011  11826  11758    188    444    -90       C  
-ATOM   9849  CG  ASP D 965     -97.039  14.215 -12.690  1.00 98.70           C  
-ANISOU 9849  CG  ASP D 965    12696  12434  12371    228    468    -65       C  
-ATOM   9850  OD1 ASP D 965     -96.233  13.774 -11.846  1.00 99.58           O  
-ANISOU 9850  OD1 ASP D 965    12803  12572  12459    279    469    -51       O  
-ATOM   9851  OD2 ASP D 965     -97.337  13.553 -13.730  1.00 95.25           O  
-ANISOU 9851  OD2 ASP D 965    12299  11952  11939    215    484    -63       O  
-ATOM   9852  N   GLY D 966     -98.727  17.423  -9.269  1.00 65.01           N  
-ANISOU 9852  N   GLY D 966     8273   8324   8104    206    379   -154       N  
-ATOM   9853  CA  GLY D 966     -99.103  18.708  -8.688  1.00 61.04           C  
-ANISOU 9853  CA  GLY D 966     7710   7859   7625    199    340   -210       C  
-ATOM   9854  C   GLY D 966    -100.576  19.057  -8.761  1.00 58.44           C  
-ANISOU 9854  C   GLY D 966     7388   7520   7297    158    337   -217       C  
-ATOM   9855  O   GLY D 966    -101.010  20.049  -8.190  1.00 54.94           O  
-ANISOU 9855  O   GLY D 966     6897   7110   6867    159    303   -268       O  
-ATOM   9856  N   VAL D 967    -101.355  18.257  -9.476  1.00 52.20           N  
-ANISOU 9856  N   VAL D 967     6654   6683   6495    123    370   -174       N  
-ATOM   9857  CA  VAL D 967    -102.747  18.587  -9.706  1.00 44.54           C  
-ANISOU 9857  CA  VAL D 967     5691   5704   5530     79    369   -181       C  
-ATOM   9858  C   VAL D 967    -103.644  17.638  -8.927  1.00 44.03           C  
-ANISOU 9858  C   VAL D 967     5652   5666   5412     83    391   -143       C  
-ATOM   9859  O   VAL D 967    -103.426  16.432  -8.948  1.00 40.84           O  
-ANISOU 9859  O   VAL D 967     5291   5238   4989     92    421    -93       O  
-ATOM   9860  CB  VAL D 967    -103.100  18.472 -11.197  1.00 40.35           C  
-ANISOU 9860  CB  VAL D 967     5195   5106   5029     31    386   -165       C  
-ATOM   9861  CG1 VAL D 967    -104.565  18.819 -11.428  1.00 37.72           C  
-ANISOU 9861  CG1 VAL D 967     4865   4770   4697    -11    383   -173       C  
-ATOM   9862  CG2 VAL D 967    -102.194  19.382 -12.027  1.00 40.80           C  
-ANISOU 9862  CG2 VAL D 967     5219   5144   5138     28    370   -181       C  
-ATOM   9863  N   ASP D 968    -104.701  18.161  -8.322  1.00 40.82           N  
-ANISOU 9863  N   ASP D 968     5217   5305   4986     75    377   -163       N  
-ATOM   9864  CA  ASP D 968    -105.629  17.293  -7.639  1.00 43.39           C  
-ANISOU 9864  CA  ASP D 968     5559   5663   5264     72    402   -115       C  
-ATOM   9865  C   ASP D 968    -106.527  16.478  -8.600  1.00 43.30           C  
-ANISOU 9865  C   ASP D 968     5600   5581   5271     13    432    -75       C  
-ATOM   9866  O   ASP D 968    -107.087  17.009  -9.552  1.00 38.09           O  
-ANISOU 9866  O   ASP D 968     4946   4884   4642    -30    424   -103       O  
-ATOM   9867  CB  ASP D 968    -106.462  18.107  -6.680  1.00 45.99           C  
-ANISOU 9867  CB  ASP D 968     5834   6081   5560     88    377   -151       C  
-ATOM   9868  CG  ASP D 968    -105.627  18.702  -5.553  1.00 52.93           C  
-ANISOU 9868  CG  ASP D 968     6655   7044   6411    158    345   -196       C  
-ATOM   9869  OD1 ASP D 968    -104.565  18.104  -5.186  1.00 56.89           O  
-ANISOU 9869  OD1 ASP D 968     7163   7557   6895    198    356   -170       O  
-ATOM   9870  OD2 ASP D 968    -106.037  19.765  -5.037  1.00 55.64           O  
-ANISOU 9870  OD2 ASP D 968     6944   7445   6750    175    307   -263       O  
-ATOM   9871  N   VAL D 969    -106.659  15.188  -8.307  1.00 39.55           N  
-ANISOU 9871  N   VAL D 969     5159   5087   4781     13    463    -10       N  
-ATOM   9872  CA  VAL D 969    -107.490  14.289  -9.071  1.00 39.99           C  
-ANISOU 9872  CA  VAL D 969     5259   5073   4863    -42    487     23       C  
-ATOM   9873  C   VAL D 969    -108.535  13.728  -8.127  1.00 38.96           C  
-ANISOU 9873  C   VAL D 969     5114   4985   4703    -53    506     81       C  
-ATOM   9874  O   VAL D 969    -108.216  12.924  -7.239  1.00 40.16           O  
-ANISOU 9874  O   VAL D 969     5266   5160   4833    -20    525    146       O  
-ATOM   9875  CB  VAL D 969    -106.671  13.131  -9.639  1.00 40.88           C  
-ANISOU 9875  CB  VAL D 969     5423   5105   5005    -34    507     53       C  
-ATOM   9876  CG1 VAL D 969    -107.522  12.299 -10.585  1.00 40.76           C  
-ANISOU 9876  CG1 VAL D 969     5448   5009   5031    -91    522     62       C  
-ATOM   9877  CG2 VAL D 969    -105.429  13.665 -10.337  1.00 40.07           C  
-ANISOU 9877  CG2 VAL D 969     5321   4986   4916     -6    492      8       C  
-ATOM   9878  N   PRO D 970    -109.774  14.182  -8.273  1.00 37.82           N  
-ANISOU 9878  N   PRO D 970     4952   4864   4554    -95    501     65       N  
-ATOM   9879  CA  PRO D 970    -110.825  13.773  -7.326  1.00 39.02           C  
-ANISOU 9879  CA  PRO D 970     5076   5077   4671   -106    518    123       C  
-ATOM   9880  C   PRO D 970    -111.420  12.426  -7.722  1.00 39.42           C  
-ANISOU 9880  C   PRO D 970     5165   5046   4766   -158    549    190       C  
-ATOM   9881  O   PRO D 970    -112.561  12.350  -8.132  1.00 36.67           O  
-ANISOU 9881  O   PRO D 970     4813   4684   4434   -215    554    189       O  
-ATOM   9882  CB  PRO D 970    -111.855  14.887  -7.454  1.00 36.84           C  
-ANISOU 9882  CB  PRO D 970     4764   4856   4379   -128    496     67       C  
-ATOM   9883  CG  PRO D 970    -111.732  15.301  -8.902  1.00 37.15           C  
-ANISOU 9883  CG  PRO D 970     4835   4812   4469   -164    482      8       C  
-ATOM   9884  CD  PRO D 970    -110.279  15.121  -9.283  1.00 36.15           C  
-ANISOU 9884  CD  PRO D 970     4737   4634   4366   -132    480     -1       C  
-ATOM   9885  N   LEU D 971    -110.631  11.371  -7.592  1.00 43.66           N  
-ANISOU 9885  N   LEU D 971     5734   5526   5329   -139    568    244       N  
-ATOM   9886  CA  LEU D 971    -111.038  10.075  -8.091  1.00 46.69           C  
-ANISOU 9886  CA  LEU D 971     6157   5806   5778   -187    590    295       C  
-ATOM   9887  C   LEU D 971    -111.766   9.217  -7.042  1.00 50.96           C  
-ANISOU 9887  C   LEU D 971     6673   6374   6317   -199    620    407       C  
-ATOM   9888  O   LEU D 971    -111.960   8.028  -7.255  1.00 50.98           O  
-ANISOU 9888  O   LEU D 971     6702   6280   6387   -233    638    466       O  
-ATOM   9889  CB  LEU D 971    -109.844   9.341  -8.716  1.00 49.12           C  
-ANISOU 9889  CB  LEU D 971     6516   6016   6131   -162    590    286       C  
-ATOM   9890  CG  LEU D 971    -108.517   9.283  -7.979  1.00 50.72           C  
-ANISOU 9890  CG  LEU D 971     6717   6254   6301    -84    593    312       C  
-ATOM   9891  CD1 LEU D 971    -108.695   8.564  -6.659  1.00 52.68           C  
-ANISOU 9891  CD1 LEU D 971     6941   6548   6527    -59    619    423       C  
-ATOM   9892  CD2 LEU D 971    -107.473   8.589  -8.839  1.00 47.59           C  
-ANISOU 9892  CD2 LEU D 971     6372   5757   5954    -66    590    289       C  
-ATOM   9893  N   GLY D 972    -112.141   9.805  -5.906  1.00 51.38           N  
-ANISOU 9893  N   GLY D 972     6668   6559   6294   -168    623    439       N  
-ATOM   9894  CA  GLY D 972    -112.907   9.086  -4.887  1.00 52.86           C  
-ANISOU 9894  CA  GLY D 972     6818   6800   6467   -177    655    557       C  
-ATOM   9895  C   GLY D 972    -114.278   8.674  -5.397  1.00 55.16           C  
-ANISOU 9895  C   GLY D 972     7105   7042   6811   -265    666    578       C  
-ATOM   9896  O   GLY D 972    -114.834   9.308  -6.319  1.00 57.38           O  
-ANISOU 9896  O   GLY D 972     7395   7301   7105   -308    644    487       O  
-ATOM   9897  N   THR D 973    -114.803   7.572  -4.861  1.00 51.48           N  
-ANISOU 9897  N   THR D 973     6624   6552   6385   -294    698    700       N  
-ATOM   9898  CA  THR D 973    -116.171   7.172  -5.175  1.00 53.41           C  
-ANISOU 9898  CA  THR D 973     6849   6766   6680   -381    709    731       C  
-ATOM   9899  C   THR D 973    -117.133   8.195  -4.551  1.00 50.19           C  
-ANISOU 9899  C   THR D 973     6373   6520   6177   -375    707    719       C  
-ATOM   9900  O   THR D 973    -116.822   8.877  -3.571  1.00 45.23           O  
-ANISOU 9900  O   THR D 973     5702   6032   5451   -302    706    726       O  
-ATOM   9901  CB  THR D 973    -116.526   5.770  -4.631  1.00 53.67           C  
-ANISOU 9901  CB  THR D 973     6868   6737   6786   -415    746    882       C  
-ATOM   9902  OG1 THR D 973    -116.140   5.704  -3.260  1.00 52.64           O  
-ANISOU 9902  OG1 THR D 973     6693   6729   6580   -344    772    992       O  
-ATOM   9903  CG2 THR D 973    -115.811   4.660  -5.391  1.00 54.13           C  
-ANISOU 9903  CG2 THR D 973     6994   6611   6964   -434    743    884       C  
-ATOM   9904  N   GLY D 974    -118.292   8.315  -5.172  1.00 51.70           N  
-ANISOU 9904  N   GLY D 974     6552   6695   6398   -448    702    687       N  
-ATOM   9905  CA  GLY D 974    -119.275   9.297  -4.764  1.00 52.76           C  
-ANISOU 9905  CA  GLY D 974     6625   6972   6449   -445    695    659       C  
-ATOM   9906  C   GLY D 974    -119.871   9.087  -3.384  1.00 55.94           C  
-ANISOU 9906  C   GLY D 974     6950   7518   6786   -422    727    782       C  
-ATOM   9907  O   GLY D 974    -120.396   8.010  -3.101  1.00 57.26           O  
-ANISOU 9907  O   GLY D 974     7099   7650   7009   -471    761    904       O  
-ATOM   9908  N   ILE D 975    -119.811  10.144  -2.567  1.00 51.78           N  
-ANISOU 9908  N   ILE D 975     6375   7156   6145   -346    714    745       N  
-ATOM   9909  CA  ILE D 975    -120.469  10.199  -1.285  1.00 50.69           C  
-ANISOU 9909  CA  ILE D 975     6149   7195   5915   -309    738    836       C  
-ATOM   9910  C   ILE D 975    -121.292  11.466  -1.206  1.00 47.00           C  
-ANISOU 9910  C   ILE D 975     5633   6857   5367   -290    710    738       C  
-ATOM   9911  O   ILE D 975    -121.272  12.308  -2.106  1.00 47.25           O  
-ANISOU 9911  O   ILE D 975     5700   6834   5418   -302    672    608       O  
-ATOM   9912  CB  ILE D 975    -119.473  10.217  -0.119  1.00 52.81           C  
-ANISOU 9912  CB  ILE D 975     6391   7572   6104   -206    746    886       C  
-ATOM   9913  CG1 ILE D 975    -118.700  11.538  -0.104  1.00 55.90           C  
-ANISOU 9913  CG1 ILE D 975     6788   8023   6429   -128    698    736       C  
-ATOM   9914  CG2 ILE D 975    -118.537   9.021  -0.220  1.00 53.25           C  
-ANISOU 9914  CG2 ILE D 975     6499   7494   6238   -213    770    976       C  
-ATOM   9915  CD1 ILE D 975    -117.836  11.724   1.120  1.00 56.06           C  
-ANISOU 9915  CD1 ILE D 975     6765   8183   6355    -18    698    761       C  
-ATOM   9916  N   SER D 976    -122.063  11.555  -0.142  1.00 48.06           N  
-ANISOU 9916  N   SER D 976     5682   7166   5414   -260    730    810       N  
-ATOM   9917  CA  SER D 976    -122.975  12.644   0.047  1.00 51.77           C  
-ANISOU 9917  CA  SER D 976     6093   7772   5804   -238    706    730       C  
-ATOM   9918  C   SER D 976    -122.168  13.879   0.359  1.00 50.24           C  
-ANISOU 9918  C   SER D 976     5896   7652   5540   -138    659    599       C  
-ATOM   9919  O   SER D 976    -121.228  13.810   1.139  1.00 50.16           O  
-ANISOU 9919  O   SER D 976     5875   7699   5485    -63    660    621       O  
-ATOM   9920  CB  SER D 976    -123.921  12.342   1.208  1.00 54.57           C  
-ANISOU 9920  CB  SER D 976     6347   8313   6073   -218    742    852       C  
-ATOM   9921  OG  SER D 976    -124.857  13.399   1.328  1.00 58.64           O  
-ANISOU 9921  OG  SER D 976     6807   8961   6513   -195    716    764       O  
-ATOM   9922  N   SER D 977    -122.517  14.991  -0.276  1.00 46.09           N  
-ANISOU 9922  N   SER D 977     5378   7118   5016   -140    616    463       N  
-ATOM   9923  CA  SER D 977    -121.817  16.230  -0.048  1.00 45.20           C  
-ANISOU 9923  CA  SER D 977     5257   7057   4860    -54    565    331       C  
-ATOM   9924  C   SER D 977    -122.378  16.945   1.143  1.00 48.16           C  
-ANISOU 9924  C   SER D 977     5535   7650   5114     32    550    306       C  
-ATOM   9925  O   SER D 977    -121.777  17.899   1.631  1.00 47.21           O  
-ANISOU 9925  O   SER D 977     5389   7602   4947    120    506    202       O  
-ATOM   9926  CB  SER D 977    -121.957  17.128  -1.266  1.00 47.38           C  
-ANISOU 9926  CB  SER D 977     5580   7223   5200    -91    525    205       C  
-ATOM   9927  OG  SER D 977    -123.322  17.384  -1.549  1.00 43.81           O  
-ANISOU 9927  OG  SER D 977     5094   6816   4735   -133    526    196       O  
-ATOM   9928  N   GLY D 978    -123.559  16.524   1.591  1.00 51.23           N  
-ANISOU 9928  N   GLY D 978     5864   8149   5454      9    584    394       N  
-ATOM   9929  CA  GLY D 978    -124.256  17.220   2.660  1.00 53.04           C  
-ANISOU 9929  CA  GLY D 978     5991   8603   5558     92    570    367       C  
-ATOM   9930  C   GLY D 978    -125.025  18.456   2.191  1.00 54.37           C  
-ANISOU 9930  C   GLY D 978     6144   8795   5720    100    521    225       C  
-ATOM   9931  O   GLY D 978    -125.589  19.171   3.017  1.00 53.14           O  
-ANISOU 9931  O   GLY D 978     5904   8823   5463    179    499    174       O  
-ATOM   9932  N   VAL D 979    -125.051  18.696   0.877  1.00 50.30           N  
-ANISOU 9932  N   VAL D 979     5703   8100   5307     26    504    163       N  
-ATOM   9933  CA  VAL D 979    -125.797  19.784   0.310  1.00 51.02           C  
-ANISOU 9933  CA  VAL D 979     5785   8194   5406     26    462     46       C  
-ATOM   9934  C   VAL D 979    -127.092  19.172  -0.193  1.00 51.89           C  
-ANISOU 9934  C   VAL D 979     5885   8300   5531    -65    499    122       C  
-ATOM   9935  O   VAL D 979    -127.081  18.384  -1.148  1.00 51.12           O  
-ANISOU 9935  O   VAL D 979     5852   8049   5524   -161    524    175       O  
-ATOM   9936  CB  VAL D 979    -125.045  20.420  -0.864  1.00 54.08           C  
-ANISOU 9936  CB  VAL D 979     6254   8397   5896      1    423    -56       C  
-ATOM   9937  CG1 VAL D 979    -125.917  21.433  -1.585  1.00 55.67           C  
-ANISOU 9937  CG1 VAL D 979     6449   8586   6117     -9    387   -154       C  
-ATOM   9938  CG2 VAL D 979    -123.766  21.074  -0.372  1.00 54.23           C  
-ANISOU 9938  CG2 VAL D 979     6275   8418   5911     86    383   -137       C  
-ATOM   9939  N   ASN D 980    -128.214  19.495   0.451  1.00 52.12           N  
-ANISOU 9939  N   ASN D 980     5829   8503   5473    -34    500    126       N  
-ATOM   9940  CA  ASN D 980    -129.509  18.930  -0.002  1.00 50.19           C  
-ANISOU 9940  CA  ASN D 980     5563   8265   5242   -123    534    199       C  
-ATOM   9941  C   ASN D 980    -130.258  19.892  -0.940  1.00 48.66           C  
-ANISOU 9941  C   ASN D 980     5381   8032   5074   -141    495     82       C  
-ATOM   9942  O   ASN D 980    -130.978  19.433  -1.819  1.00 51.81           O  
-ANISOU 9942  O   ASN D 980     5802   8354   5529   -234    513    114       O  
-ATOM   9943  CB  ASN D 980    -130.429  18.414   1.132  1.00 48.87           C  
-ANISOU 9943  CB  ASN D 980     5292   8304   4973   -105    575    314       C  
-ATOM   9944  CG  ASN D 980    -131.701  17.675   0.581  1.00 48.08           C  
-ANISOU 9944  CG  ASN D 980     5171   8186   4910   -217    614    402       C  
-ATOM   9945  OD1 ASN D 980    -131.629  16.903  -0.400  1.00 48.01           O  
-ANISOU 9945  OD1 ASN D 980     5230   7998   5014   -321    632    442       O  
-ATOM   9946  ND2 ASN D 980    -132.860  17.958   1.172  1.00 42.15           N  
-ANISOU 9946  ND2 ASN D 980     4324   7622   4067   -192    621    420       N  
-ATOM   9947  N   ASP D 981    -130.132  21.199  -0.704  1.00 45.91           N  
-ANISOU 9947  N   ASP D 981     5012   7746   4688    -50    439    -50       N  
-ATOM   9948  CA  ASP D 981    -130.909  22.205  -1.409  1.00 45.26           C  
-ANISOU 9948  CA  ASP D 981     4925   7654   4619    -47    399   -156       C  
-ATOM   9949  C   ASP D 981    -130.222  22.672  -2.680  1.00 43.45           C  
-ANISOU 9949  C   ASP D 981     4785   7224   4498    -81    369   -230       C  
-ATOM   9950  O   ASP D 981    -129.873  23.844  -2.825  1.00 39.94           O  
-ANISOU 9950  O   ASP D 981     4346   6757   4072    -18    315   -345       O  
-ATOM   9951  CB  ASP D 981    -131.213  23.403  -0.484  1.00 47.70           C  
-ANISOU 9951  CB  ASP D 981     5154   8132   4836     75    350   -263       C  
-ATOM   9952  CG  ASP D 981    -129.936  24.124   0.006  1.00 50.40           C  
-ANISOU 9952  CG  ASP D 981     5509   8453   5187    166    303   -356       C  
-ATOM   9953  OD1 ASP D 981    -128.889  23.459   0.228  1.00 48.79           O  
-ANISOU 9953  OD1 ASP D 981     5342   8192   5005    157    325   -299       O  
-ATOM   9954  OD2 ASP D 981    -129.987  25.362   0.147  1.00 54.97           O  
-ANISOU 9954  OD2 ASP D 981     6060   9067   5760    246    242   -489       O  
-ATOM   9955  N   THR D 982    -130.131  21.771  -3.648  1.00 44.66           N  
-ANISOU 9955  N   THR D 982     5001   7238   4727   -181    403   -163       N  
-ATOM   9956  CA  THR D 982    -129.456  22.075  -4.898  1.00 47.74           C  
-ANISOU 9956  CA  THR D 982     5473   7452   5213   -214    382   -217       C  
-ATOM   9957  C   THR D 982    -130.203  21.550  -6.110  1.00 47.07           C  
-ANISOU 9957  C   THR D 982     5420   7285   5181   -310    402   -191       C  
-ATOM   9958  O   THR D 982    -130.900  20.541  -6.040  1.00 52.60           O  
-ANISOU 9958  O   THR D 982     6100   8012   5873   -376    442   -107       O  
-ATOM   9959  CB  THR D 982    -128.023  21.504  -4.908  1.00 49.08           C  
-ANISOU 9959  CB  THR D 982     5703   7512   5433   -218    394   -184       C  
-ATOM   9960  OG1 THR D 982    -127.464  21.654  -6.210  1.00 49.83           O  
-ANISOU 9960  OG1 THR D 982     5871   7446   5616   -259    381   -220       O  
-ATOM   9961  CG2 THR D 982    -128.032  20.031  -4.564  1.00 51.72           C  
-ANISOU 9961  CG2 THR D 982     6041   7843   5766   -276    449    -57       C  
-ATOM   9962  N   SER D 983    -130.021  22.236  -7.235  1.00 44.92           N  
-ANISOU 9962  N   SER D 983     5191   6911   4964   -317    373   -261       N  
-ATOM   9963  CA  SER D 983    -130.578  21.804  -8.503  1.00 45.49           C  
-ANISOU 9963  CA  SER D 983     5295   6903   5084   -398    386   -252       C  
-ATOM   9964  C   SER D 983    -129.806  20.647  -9.143  1.00 44.45           C  
-ANISOU 9964  C   SER D 983     5229   6639   5021   -465    415   -197       C  
-ATOM   9965  O   SER D 983    -130.240  20.132 -10.158  1.00 47.11           O  
-ANISOU 9965  O   SER D 983     5589   6914   5397   -532    426   -192       O  
-ATOM   9966  CB  SER D 983    -130.616  22.986  -9.478  1.00 44.93           C  
-ANISOU 9966  CB  SER D 983     5244   6785   5044   -369    345   -338       C  
-ATOM   9967  OG  SER D 983    -131.265  24.123  -8.896  1.00 46.71           O  
-ANISOU 9967  OG  SER D 983     5411   7119   5219   -298    310   -400       O  
-ATOM   9968  N   LEU D 984    -128.686  20.228  -8.564  1.00 41.60           N  
-ANISOU 9968  N   LEU D 984     4895   6240   4672   -443    426   -162       N  
-ATOM   9969  CA  LEU D 984    -127.752  19.358  -9.277  1.00 40.56           C  
-ANISOU 9969  CA  LEU D 984     4831   5969   4610   -488    443   -132       C  
-ATOM   9970  C   LEU D 984    -127.500  18.060  -8.538  1.00 39.12           C  
-ANISOU 9970  C   LEU D 984     4648   5781   4433   -518    483    -35       C  
-ATOM   9971  O   LEU D 984    -127.271  18.055  -7.312  1.00 37.63           O  
-ANISOU 9971  O   LEU D 984     4424   5680   4193   -470    491      5       O  
-ATOM   9972  CB  LEU D 984    -126.403  20.075  -9.455  1.00 38.36           C  
-ANISOU 9972  CB  LEU D 984     4593   5623   4357   -431    417   -182       C  
-ATOM   9973  CG  LEU D 984    -126.317  21.282 -10.389  1.00 40.98           C  
-ANISOU 9973  CG  LEU D 984     4938   5917   4714   -405    379   -262       C  
-ATOM   9974  CD1 LEU D 984    -124.965  21.957 -10.236  1.00 42.10           C  
-ANISOU 9974  CD1 LEU D 984     5103   6008   4884   -347    355   -295       C  
-ATOM   9975  CD2 LEU D 984    -126.530  20.898 -11.850  1.00 39.15           C  
-ANISOU 9975  CD2 LEU D 984     4746   5601   4528   -464    387   -268       C  
-ATOM   9976  N   LEU D 985    -127.514  16.960  -9.274  1.00 40.11           N  
-ANISOU 9976  N   LEU D 985     4811   5805   4624   -593    505      3       N  
-ATOM   9977  CA  LEU D 985    -127.135  15.665  -8.703  1.00 45.65           C  
-ANISOU 9977  CA  LEU D 985     5521   6467   5357   -624    540    101       C  
-ATOM   9978  C   LEU D 985    -125.627  15.586  -8.456  1.00 42.23           C  
-ANISOU 9978  C   LEU D 985     5137   5971   4939   -574    538    106       C  
-ATOM   9979  O   LEU D 985    -125.174  15.065  -7.427  1.00 45.05           O  
-ANISOU 9979  O   LEU D 985     5480   6361   5277   -548    560    181       O  
-ATOM   9980  CB  LEU D 985    -127.579  14.518  -9.625  1.00 49.64           C  
-ANISOU 9980  CB  LEU D 985     6050   6865   5945   -718    556    125       C  
-ATOM   9981  CG  LEU D 985    -129.092  14.294  -9.814  1.00 53.75           C  
-ANISOU 9981  CG  LEU D 985     6516   7440   6464   -784    563    136       C  
-ATOM   9982  CD1 LEU D 985    -129.369  13.179 -10.814  1.00 54.54           C  
-ANISOU 9982  CD1 LEU D 985     6642   7418   6662   -873    569    137       C  
-ATOM   9983  CD2 LEU D 985    -129.780  13.969  -8.486  1.00 55.79           C  
-ANISOU 9983  CD2 LEU D 985     6702   7820   6676   -786    593    238       C  
-ATOM   9984  N   TYR D 986    -124.853  16.129  -9.383  1.00 39.23           N  
-ANISOU 9984  N   TYR D 986     4806   5510   4588   -556    513     31       N  
-ATOM   9985  CA  TYR D 986    -123.401  16.077  -9.297  1.00 37.81           C  
-ANISOU 9985  CA  TYR D 986     4672   5267   4429   -512    509     28       C  
-ATOM   9986  C   TYR D 986    -122.799  17.453  -9.529  1.00 35.41           C  
-ANISOU 9986  C   TYR D 986     4371   4976   4106   -451    472    -56       C  
-ATOM   9987  O   TYR D 986    -123.423  18.355 -10.122  1.00 35.30           O  
-ANISOU 9987  O   TYR D 986     4342   4984   4086   -451    449   -116       O  
-ATOM   9988  CB  TYR D 986    -122.863  15.077 -10.321  1.00 39.40           C  
-ANISOU 9988  CB  TYR D 986     4934   5330   4707   -560    520     36       C  
-ATOM   9989  CG  TYR D 986    -123.647  13.798 -10.273  1.00 39.38           C  
-ANISOU 9989  CG  TYR D 986     4922   5295   4745   -632    548    104       C  
-ATOM   9990  CD1 TYR D 986    -123.473  12.895  -9.229  1.00 40.07           C  
-ANISOU 9990  CD1 TYR D 986     4994   5391   4838   -633    578    205       C  
-ATOM   9991  CD2 TYR D 986    -124.608  13.512 -11.257  1.00 39.57           C  
-ANISOU 9991  CD2 TYR D 986     4943   5284   4807   -699    544     71       C  
-ATOM   9992  CE1 TYR D 986    -124.227  11.741  -9.168  1.00 40.89           C  
-ANISOU 9992  CE1 TYR D 986     5082   5458   4996   -705    603    278       C  
-ATOM   9993  CE2 TYR D 986    -125.360  12.356 -11.212  1.00 40.99           C  
-ANISOU 9993  CE2 TYR D 986     5107   5428   5041   -771    565    130       C  
-ATOM   9994  CZ  TYR D 986    -125.178  11.486 -10.150  1.00 41.96           C  
-ANISOU 9994  CZ  TYR D 986     5214   5549   5179   -777    595    237       C  
-ATOM   9995  OH  TYR D 986    -125.934  10.339 -10.103  1.00 46.85           O  
-ANISOU 9995  OH  TYR D 986     5811   6121   5868   -854    615    305       O  
-ATOM   9996  N   ASN D 987    -121.565  17.611  -9.061  1.00 33.01           N  
-ANISOU 9996  N   ASN D 987     4083   4656   3802   -398    466    -57       N  
-ATOM   9997  CA  ASN D 987    -120.848  18.866  -9.262  1.00 32.13           C  
-ANISOU 9997  CA  ASN D 987     3973   4541   3694   -344    429   -132       C  
-ATOM   9998  C   ASN D 987    -120.680  19.203 -10.744  1.00 30.80           C  
-ANISOU 9998  C   ASN D 987     3842   4282   3577   -372    417   -175       C  
-ATOM   9999  O   ASN D 987    -120.682  18.325 -11.601  1.00 27.82           O  
-ANISOU 9999  O   ASN D 987     3503   3833   3234   -421    436   -154       O  
-ATOM  10000  CB  ASN D 987    -119.467  18.792  -8.626  1.00 31.45           C  
-ANISOU10000  CB  ASN D 987     3899   4440   3609   -293    427   -122       C  
-ATOM  10001  CG  ASN D 987    -119.526  18.552  -7.132  1.00 31.49           C  
-ANISOU10001  CG  ASN D 987     3860   4554   3552   -249    436    -81       C  
-ATOM  10002  OD1 ASN D 987    -120.388  19.083  -6.456  1.00 31.45           O  
-ANISOU10002  OD1 ASN D 987     3800   4657   3494   -226    426    -97       O  
-ATOM  10003  ND2 ASN D 987    -118.587  17.807  -6.614  1.00 30.35           N  
-ANISOU10003  ND2 ASN D 987     3732   4392   3406   -228    455    -31       N  
-ATOM  10004  N   GLU D 988    -120.513  20.478 -11.013  1.00 29.93           N  
-ANISOU10004  N   GLU D 988     3716   4180   3475   -336    383   -234       N  
-ATOM  10005  CA  GLU D 988    -119.883  20.900 -12.241  1.00 30.34           C  
-ANISOU10005  CA  GLU D 988     3799   4152   3576   -341    372   -260       C  
-ATOM  10006  C   GLU D 988    -119.061  22.152 -11.978  1.00 28.91           C  
-ANISOU10006  C   GLU D 988     3598   3970   3419   -284    336   -303       C  
-ATOM  10007  O   GLU D 988    -119.221  22.815 -10.943  1.00 27.52           O  
-ANISOU10007  O   GLU D 988     3378   3858   3219   -241    313   -333       O  
-ATOM  10008  CB  GLU D 988    -120.889  21.112 -13.372  1.00 30.58           C  
-ANISOU10008  CB  GLU D 988     3829   4178   3612   -379    370   -278       C  
-ATOM  10009  CG  GLU D 988    -122.075  21.969 -13.033  1.00 31.59           C  
-ANISOU10009  CG  GLU D 988     3909   4385   3710   -367    350   -308       C  
-ATOM  10010  CD  GLU D 988    -123.145  21.862 -14.110  1.00 32.98           C  
-ANISOU10010  CD  GLU D 988     4084   4564   3882   -411    356   -316       C  
-ATOM  10011  OE1 GLU D 988    -123.313  22.829 -14.879  1.00 33.34           O  
-ANISOU10011  OE1 GLU D 988     4120   4605   3943   -394    334   -346       O  
-ATOM  10012  OE2 GLU D 988    -123.803  20.798 -14.185  1.00 34.98           O  
-ANISOU10012  OE2 GLU D 988     4343   4824   4122   -462    381   -291       O  
-ATOM  10013  N   TYR D 989    -118.140  22.425 -12.897  1.00 27.16           N  
-ANISOU10013  N   TYR D 989     3400   3675   3244   -283    332   -306       N  
-ATOM  10014  CA  TYR D 989    -117.152  23.448 -12.715  1.00 27.17           C  
-ANISOU10014  CA  TYR D 989     3382   3653   3287   -239    301   -335       C  
-ATOM  10015  C   TYR D 989    -117.115  24.239 -13.984  1.00 27.06           C  
-ANISOU10015  C   TYR D 989     3369   3593   3322   -248    289   -340       C  
-ATOM  10016  O   TYR D 989    -117.028  23.677 -15.061  1.00 27.75           O  
-ANISOU10016  O   TYR D 989     3487   3646   3411   -278    313   -312       O  
-ATOM  10017  CB  TYR D 989    -115.781  22.832 -12.439  1.00 27.35           C  
-ANISOU10017  CB  TYR D 989     3430   3640   3321   -225    313   -313       C  
-ATOM  10018  CG  TYR D 989    -115.720  21.937 -11.231  1.00 26.68           C  
-ANISOU10018  CG  TYR D 989     3346   3602   3187   -212    330   -291       C  
-ATOM  10019  CD1 TYR D 989    -116.034  20.609 -11.328  1.00 28.61           C  
-ANISOU10019  CD1 TYR D 989     3625   3837   3409   -248    368   -240       C  
-ATOM  10020  CD2 TYR D 989    -115.316  22.418 -10.001  1.00 29.34           C  
-ANISOU10020  CD2 TYR D 989     3645   3996   3507   -159    307   -319       C  
-ATOM  10021  CE1 TYR D 989    -115.992  19.772 -10.226  1.00 28.76           C  
-ANISOU10021  CE1 TYR D 989     3640   3898   3388   -236    387   -201       C  
-ATOM  10022  CE2 TYR D 989    -115.268  21.596  -8.886  1.00 29.93           C  
-ANISOU10022  CE2 TYR D 989     3713   4131   3527   -139    325   -288       C  
-ATOM  10023  CZ  TYR D 989    -115.603  20.267  -9.028  1.00 30.13           C  
-ANISOU10023  CZ  TYR D 989     3774   4141   3532   -180    368   -219       C  
-ATOM  10024  OH  TYR D 989    -115.553  19.436  -7.972  1.00 33.13           O  
-ANISOU10024  OH  TYR D 989     4146   4577   3867   -161    390   -170       O  
-ATOM  10025  N   ILE D 990    -117.139  25.554 -13.847  1.00 25.69           N  
-ANISOU10025  N   ILE D 990     3155   3417   3188   -217    251   -376       N  
-ATOM  10026  CA  ILE D 990    -117.142  26.431 -14.991  1.00 25.97           C  
-ANISOU10026  CA  ILE D 990     3180   3410   3277   -220    239   -367       C  
-ATOM  10027  C   ILE D 990    -116.055  27.519 -14.870  1.00 26.16           C  
-ANISOU10027  C   ILE D 990     3174   3381   3384   -188    205   -380       C  
-ATOM  10028  O   ILE D 990    -115.900  28.160 -13.813  1.00 26.35           O  
-ANISOU10028  O   ILE D 990     3164   3417   3431   -152    169   -431       O  
-ATOM  10029  CB  ILE D 990    -118.523  27.118 -15.159  1.00 25.29           C  
-ANISOU10029  CB  ILE D 990     3067   3363   3179   -219    222   -390       C  
-ATOM  10030  CG1 ILE D 990    -119.627  26.084 -15.227  1.00 25.18           C  
-ANISOU10030  CG1 ILE D 990     3073   3404   3091   -255    252   -380       C  
-ATOM  10031  CG2 ILE D 990    -118.562  27.939 -16.429  1.00 25.44           C  
-ANISOU10031  CG2 ILE D 990     3076   3343   3248   -220    215   -364       C  
-ATOM  10032  CD1 ILE D 990    -120.182  25.664 -13.881  1.00 25.56           C  
-ANISOU10032  CD1 ILE D 990     3105   3521   3086   -246    252   -403       C  
-ATOM  10033  N   VAL D 991    -115.303  27.702 -15.945  1.00 25.86           N  
-ANISOU10033  N   VAL D 991     3144   3292   3392   -198    216   -335       N  
-ATOM  10034  CA  VAL D 991    -114.377  28.830 -16.041  1.00 27.80           C  
-ANISOU10034  CA  VAL D 991     3351   3478   3733   -178    185   -333       C  
-ATOM  10035  C   VAL D 991    -114.790  29.726 -17.197  1.00 27.94           C  
-ANISOU10035  C   VAL D 991     3346   3468   3800   -182    179   -293       C  
-ATOM  10036  O   VAL D 991    -115.410  29.262 -18.137  1.00 27.67           O  
-ANISOU10036  O   VAL D 991     3334   3464   3717   -202    209   -257       O  
-ATOM  10037  CB  VAL D 991    -112.885  28.401 -16.155  1.00 26.53           C  
-ANISOU10037  CB  VAL D 991     3201   3283   3595   -179    200   -302       C  
-ATOM  10038  CG1 VAL D 991    -112.444  27.691 -14.887  1.00 26.72           C  
-ANISOU10038  CG1 VAL D 991     3238   3336   3578   -163    199   -342       C  
-ATOM  10039  CG2 VAL D 991    -112.636  27.549 -17.381  1.00 24.86           C  
-ANISOU10039  CG2 VAL D 991     3026   3074   3345   -203    245   -240       C  
-ATOM  10040  N   TYR D 992    -114.431  31.004 -17.092  1.00 28.70           N  
-ANISOU10040  N   TYR D 992     3394   3510   4000   -162    138   -300       N  
-ATOM  10041  CA  TYR D 992    -114.914  32.044 -18.000  1.00 31.07           C  
-ANISOU10041  CA  TYR D 992     3662   3779   4363   -158    125   -260       C  
-ATOM  10042  C   TYR D 992    -113.803  32.664 -18.811  1.00 29.89           C  
-ANISOU10042  C   TYR D 992     3483   3564   4308   -163    127   -185       C  
-ATOM  10043  O   TYR D 992    -114.012  33.646 -19.481  1.00 30.66           O  
-ANISOU10043  O   TYR D 992     3544   3624   4480   -157    113   -139       O  
-ATOM  10044  CB  TYR D 992    -115.689  33.116 -17.204  1.00 31.08           C  
-ANISOU10044  CB  TYR D 992     3624   3765   4419   -128     71   -329       C  
-ATOM  10045  CG  TYR D 992    -116.836  32.461 -16.509  1.00 29.54           C  
-ANISOU10045  CG  TYR D 992     3452   3653   4118   -123     76   -388       C  
-ATOM  10046  CD1 TYR D 992    -116.666  31.906 -15.264  1.00 30.07           C  
-ANISOU10046  CD1 TYR D 992     3527   3760   4139   -111     69   -450       C  
-ATOM  10047  CD2 TYR D 992    -118.080  32.297 -17.161  1.00 28.33           C  
-ANISOU10047  CD2 TYR D 992     3310   3550   3904   -133     95   -369       C  
-ATOM  10048  CE1 TYR D 992    -117.724  31.258 -14.633  1.00 30.94           C  
-ANISOU10048  CE1 TYR D 992     3650   3956   4150   -109     80   -487       C  
-ATOM  10049  CE2 TYR D 992    -119.137  31.642 -16.557  1.00 28.02           C  
-ANISOU10049  CE2 TYR D 992     3285   3590   3769   -136    104   -414       C  
-ATOM  10050  CZ  TYR D 992    -118.965  31.119 -15.285  1.00 29.50           C  
-ANISOU10050  CZ  TYR D 992     3477   3816   3916   -125     97   -468       C  
-ATOM  10051  OH  TYR D 992    -119.988  30.460 -14.650  1.00 24.45           O  
-ANISOU10051  OH  TYR D 992     2844   3262   3185   -129    109   -497       O  
-ATOM  10052  N   ASP D 993    -112.637  32.034 -18.801  1.00 31.62           N  
-ANISOU10052  N   ASP D 993     3717   3778   4520   -173    148   -164       N  
-ATOM  10053  CA  ASP D 993    -111.490  32.493 -19.582  1.00 31.40           C  
-ANISOU10053  CA  ASP D 993     3656   3703   4571   -180    156    -85       C  
-ATOM  10054  C   ASP D 993    -110.865  31.233 -20.129  1.00 30.55           C  
-ANISOU10054  C   ASP D 993     3591   3645   4373   -192    207    -48       C  
-ATOM  10055  O   ASP D 993    -110.467  30.359 -19.371  1.00 30.94           O  
-ANISOU10055  O   ASP D 993     3673   3712   4371   -192    214    -95       O  
-ATOM  10056  CB  ASP D 993    -110.539  33.253 -18.661  1.00 31.78           C  
-ANISOU10056  CB  ASP D 993     3661   3682   4733   -172    111   -125       C  
-ATOM  10057  CG  ASP D 993    -109.286  33.781 -19.367  1.00 32.67           C  
-ANISOU10057  CG  ASP D 993     3729   3741   4943   -184    116    -39       C  
-ATOM  10058  OD1 ASP D 993    -108.884  33.308 -20.459  1.00 35.16           O  
-ANISOU10058  OD1 ASP D 993     4053   4091   5216   -194    163     50       O  
-ATOM  10059  OD2 ASP D 993    -108.674  34.666 -18.770  1.00 34.64           O  
-ANISOU10059  OD2 ASP D 993     3929   3919   5315   -181     71    -68       O  
-ATOM  10060  N   ILE D 994    -110.738  31.141 -21.448  1.00 31.69           N  
-ANISOU10060  N   ILE D 994     3729   3816   4497   -196    241     36       N  
-ATOM  10061  CA  ILE D 994    -110.186  29.926 -22.095  1.00 31.25           C  
-ANISOU10061  CA  ILE D 994     3709   3815   4351   -199    287     63       C  
-ATOM  10062  C   ILE D 994    -108.747  29.575 -21.673  1.00 30.01           C  
-ANISOU10062  C   ILE D 994     3549   3635   4217   -197    291     65       C  
-ATOM  10063  O   ILE D 994    -108.307  28.427 -21.820  1.00 31.12           O  
-ANISOU10063  O   ILE D 994     3729   3814   4281   -194    320     57       O  
-ATOM  10064  CB  ILE D 994    -110.250  30.023 -23.632  1.00 33.72           C  
-ANISOU10064  CB  ILE D 994     4000   4176   4635   -191    319    152       C  
-ATOM  10065  CG1 ILE D 994    -109.360  31.179 -24.139  1.00 38.78           C  
-ANISOU10065  CG1 ILE D 994     4572   4777   5387   -187    312    246       C  
-ATOM  10066  CG2 ILE D 994    -111.677  30.229 -24.091  1.00 33.29           C  
-ANISOU10066  CG2 ILE D 994     3950   4158   4541   -189    317    146       C  
-ATOM  10067  CD1 ILE D 994    -109.369  31.357 -25.650  1.00 40.75           C  
-ANISOU10067  CD1 ILE D 994     4786   5091   5606   -172    346    352       C  
-ATOM  10068  N   ALA D 995    -108.019  30.560 -21.158  1.00 29.73           N  
-ANISOU10068  N   ALA D 995     3465   3538   4294   -197    258     71       N  
-ATOM  10069  CA  ALA D 995    -106.638  30.367 -20.718  1.00 30.63           C  
-ANISOU10069  CA  ALA D 995     3565   3632   4441   -195    257     71       C  
-ATOM  10070  C   ALA D 995    -106.519  29.645 -19.396  1.00 29.29           C  
-ANISOU10070  C   ALA D 995     3433   3467   4228   -187    243    -21       C  
-ATOM  10071  O   ALA D 995    -105.421  29.235 -19.021  1.00 25.79           O  
-ANISOU10071  O   ALA D 995     2989   3024   3787   -180    247    -27       O  
-ATOM  10072  CB  ALA D 995    -105.913  31.711 -20.645  1.00 32.93           C  
-ANISOU10072  CB  ALA D 995     3780   3850   4880   -202    222    107       C  
-ATOM  10073  N   GLN D 996    -107.646  29.463 -18.692  1.00 28.19           N  
-ANISOU10073  N   GLN D 996     3323   3341   4045   -184    228    -87       N  
-ATOM  10074  CA  GLN D 996    -107.622  28.719 -17.412  1.00 28.42           C  
-ANISOU10074  CA  GLN D 996     3384   3392   4021   -171    220   -162       C  
-ATOM  10075  C   GLN D 996    -107.626  27.190 -17.559  1.00 27.65           C  
-ANISOU10075  C   GLN D 996     3351   3341   3815   -173    264   -155       C  
-ATOM  10076  O   GLN D 996    -107.716  26.479 -16.571  1.00 25.90           O  
-ANISOU10076  O   GLN D 996     3156   3141   3544   -162    263   -200       O  
-ATOM  10077  CB  GLN D 996    -108.801  29.135 -16.545  1.00 28.88           C  
-ANISOU10077  CB  GLN D 996     3439   3460   4075   -163    188   -229       C  
-ATOM  10078  CG  GLN D 996    -108.534  30.383 -15.731  1.00 31.33           C  
-ANISOU10078  CG  GLN D 996     3689   3726   4490   -146    130   -283       C  
-ATOM  10079  CD  GLN D 996    -109.795  30.867 -15.029  1.00 29.74           C  
-ANISOU10079  CD  GLN D 996     3478   3543   4278   -130     97   -350       C  
-ATOM  10080  OE1 GLN D 996    -110.520  31.691 -15.570  1.00 27.48           O  
-ANISOU10080  OE1 GLN D 996     3171   3229   4040   -134     82   -337       O  
-ATOM  10081  NE2 GLN D 996    -110.044  30.360 -13.809  1.00 27.01           N  
-ANISOU10081  NE2 GLN D 996     3143   3252   3867   -106     87   -419       N  
-ATOM  10082  N   VAL D 997    -107.511  26.697 -18.785  1.00 28.53           N  
-ANISOU10082  N   VAL D 997     3480   3469   3892   -181    299   -100       N  
-ATOM  10083  CA  VAL D 997    -107.562  25.265 -19.063  1.00 28.19           C  
-ANISOU10083  CA  VAL D 997     3494   3459   3760   -182    335   -101       C  
-ATOM  10084  C   VAL D 997    -106.279  24.817 -19.760  1.00 29.03           C  
-ANISOU10084  C   VAL D 997     3598   3571   3860   -167    359    -59       C  
-ATOM  10085  O   VAL D 997    -105.889  25.396 -20.753  1.00 32.25           O  
-ANISOU10085  O   VAL D 997     3970   3988   4297   -166    367     -5       O  
-ATOM  10086  CB  VAL D 997    -108.722  24.923 -20.010  1.00 26.38           C  
-ANISOU10086  CB  VAL D 997     3286   3258   3479   -197    354    -92       C  
-ATOM  10087  CG1 VAL D 997    -108.739  23.440 -20.299  1.00 27.54           C  
-ANISOU10087  CG1 VAL D 997     3486   3425   3551   -198    384   -105       C  
-ATOM  10088  CG2 VAL D 997    -110.041  25.359 -19.403  1.00 27.78           C  
-ANISOU10088  CG2 VAL D 997     3460   3438   3655   -210    333   -130       C  
-ATOM  10089  N   ASN D 998    -105.670  23.762 -19.253  1.00 30.02           N  
-ANISOU10089  N   ASN D 998     3759   3701   3945   -153    372    -79       N  
-ATOM  10090  CA  ASN D 998    -104.565  23.124 -19.916  1.00 30.39           C  
-ANISOU10090  CA  ASN D 998     3812   3764   3970   -133    396    -50       C  
-ATOM  10091  C   ASN D 998    -104.930  21.634 -20.123  1.00 29.45           C  
-ANISOU10091  C   ASN D 998     3757   3657   3777   -128    420    -74       C  
-ATOM  10092  O   ASN D 998    -104.991  20.839 -19.152  1.00 26.39           O  
-ANISOU10092  O   ASN D 998     3406   3254   3369   -124    420   -104       O  
-ATOM  10093  CB  ASN D 998    -103.293  23.325 -19.082  1.00 31.65           C  
-ANISOU10093  CB  ASN D 998     3948   3909   4168   -115    383    -53       C  
-ATOM  10094  CG  ASN D 998    -102.015  22.911 -19.805  1.00 33.57           C  
-ANISOU10094  CG  ASN D 998     4181   4176   4400    -91    405    -15       C  
-ATOM  10095  OD1 ASN D 998    -100.991  22.653 -19.181  1.00 33.24           O  
-ANISOU10095  OD1 ASN D 998     4133   4132   4364    -70    402    -23       O  
-ATOM  10096  ND2 ASN D 998    -102.061  22.873 -21.131  1.00 36.34           N  
-ANISOU10096  ND2 ASN D 998     4521   4559   4726    -88    427     27       N  
-ATOM  10097  N   LEU D 999    -105.247  21.282 -21.373  1.00 27.90           N  
-ANISOU10097  N   LEU D 999     3567   3490   3543   -127    439    -61       N  
-ATOM  10098  CA  LEU D 999    -105.631  19.911 -21.696  1.00 30.51           C  
-ANISOU10098  CA  LEU D 999     3951   3824   3819   -122    455    -96       C  
-ATOM  10099  C   LEU D 999    -104.457  18.969 -21.459  1.00 29.90           C  
-ANISOU10099  C   LEU D 999     3898   3737   3727    -90    466   -101       C  
-ATOM  10100  O   LEU D 999    -103.339  19.271 -21.852  1.00 30.11           O  
-ANISOU10100  O   LEU D 999     3893   3786   3760    -63    472    -71       O  
-ATOM  10101  CB  LEU D 999    -106.113  19.839 -23.139  1.00 33.04           C  
-ANISOU10101  CB  LEU D 999     4260   4191   4101   -118    467    -91       C  
-ATOM  10102  CG  LEU D 999    -107.384  20.654 -23.405  1.00 33.54           C  
-ANISOU10102  CG  LEU D 999     4304   4269   4171   -146    457    -88       C  
-ATOM  10103  CD1 LEU D 999    -107.793  20.466 -24.863  1.00 35.64           C  
-ANISOU10103  CD1 LEU D 999     4556   4599   4388   -132    469    -87       C  
-ATOM  10104  CD2 LEU D 999    -108.526  20.260 -22.486  1.00 31.56           C  
-ANISOU10104  CD2 LEU D 999     4087   3984   3919   -180    446   -131       C  
-ATOM  10105  N   LYS D1000    -104.705  17.856 -20.777  1.00 33.30           N  
-ANISOU10105  N   LYS D1000     4378   4132   4143    -91    469   -132       N  
-ATOM  10106  CA  LYS D1000    -103.648  16.881 -20.429  1.00 36.16           C  
-ANISOU10106  CA  LYS D1000     4767   4476   4495    -55    477   -136       C  
-ATOM  10107  C   LYS D1000    -103.793  15.518 -21.109  1.00 36.55           C  
-ANISOU10107  C   LYS D1000     4861   4508   4518    -41    488   -171       C  
-ATOM  10108  O   LYS D1000    -102.826  14.984 -21.614  1.00 34.32           O  
-ANISOU10108  O   LYS D1000     4582   4238   4219      1    495   -176       O  
-ATOM  10109  CB  LYS D1000    -103.602  16.614 -18.923  1.00 38.19           C  
-ANISOU10109  CB  LYS D1000     5044   4702   4767    -57    471   -136       C  
-ATOM  10110  CG  LYS D1000    -103.479  17.835 -18.045  1.00 42.10           C  
-ANISOU10110  CG  LYS D1000     5494   5211   5290    -64    453   -124       C  
-ATOM  10111  CD  LYS D1000    -102.436  18.842 -18.497  1.00 44.95           C  
-ANISOU10111  CD  LYS D1000     5804   5597   5680    -49    446   -102       C  
-ATOM  10112  CE  LYS D1000    -101.026  18.423 -18.177  1.00 47.63           C  
-ANISOU10112  CE  LYS D1000     6140   5944   6015     -8    451    -93       C  
-ATOM  10113  NZ  LYS D1000    -100.108  19.594 -18.372  1.00 51.99           N  
-ANISOU10113  NZ  LYS D1000     6626   6517   6611     -4    439    -69       N  
-ATOM  10114  N   TYR D1001    -104.989  14.942 -21.057  1.00 36.55           N  
-ANISOU10114  N   TYR D1001     4891   4478   4519    -74    485   -198       N  
-ATOM  10115  CA  TYR D1001    -105.218  13.626 -21.618  1.00 35.81           C  
-ANISOU10115  CA  TYR D1001     4835   4352   4419    -65    488   -241       C  
-ATOM  10116  C   TYR D1001    -106.452  13.586 -22.494  1.00 36.25           C  
-ANISOU10116  C   TYR D1001     4887   4422   4463    -97    481   -279       C  
-ATOM  10117  O   TYR D1001    -107.398  14.363 -22.327  1.00 32.66           O  
-ANISOU10117  O   TYR D1001     4414   3986   4011   -135    477   -268       O  
-ATOM  10118  CB  TYR D1001    -105.345  12.561 -20.520  1.00 36.63           C  
-ANISOU10118  CB  TYR D1001     4984   4383   4552    -74    490   -238       C  
-ATOM  10119  CG  TYR D1001    -104.172  12.502 -19.566  1.00 34.71           C  
-ANISOU10119  CG  TYR D1001     4744   4132   4313    -37    495   -202       C  
-ATOM  10120  CD1 TYR D1001    -103.013  11.807 -19.910  1.00 37.18           C  
-ANISOU10120  CD1 TYR D1001     5070   4437   4619     16    499   -212       C  
-ATOM  10121  CD2 TYR D1001    -104.223  13.123 -18.346  1.00 31.98           C  
-ANISOU10121  CD2 TYR D1001     4382   3795   3972    -49    494   -165       C  
-ATOM  10122  CE1 TYR D1001    -101.941  11.736 -19.053  1.00 34.91           C  
-ANISOU10122  CE1 TYR D1001     4783   4149   4332     53    504   -180       C  
-ATOM  10123  CE2 TYR D1001    -103.160  13.066 -17.475  1.00 34.19           C  
-ANISOU10123  CE2 TYR D1001     4659   4080   4250    -11    496   -139       C  
-ATOM  10124  CZ  TYR D1001    -102.016  12.382 -17.832  1.00 36.93           C  
-ANISOU10124  CZ  TYR D1001     5021   4417   4592     38    502   -143       C  
-ATOM  10125  OH  TYR D1001    -100.963  12.367 -16.939  1.00 36.59           O  
-ANISOU10125  OH  TYR D1001     4972   4388   4544     79    503   -117       O  
-ATOM  10126  N   LEU D1002    -106.420  12.650 -23.439  1.00 41.01           N  
-ANISOU10126  N   LEU D1002     5506   5022   5055    -74    478   -333       N  
-ATOM  10127  CA  LEU D1002    -107.551  12.345 -24.280  1.00 42.19           C  
-ANISOU10127  CA  LEU D1002     5652   5182   5196    -98    467   -387       C  
-ATOM  10128  C   LEU D1002    -107.775  10.849 -24.170  1.00 43.88           C  
-ANISOU10128  C   LEU D1002     5910   5314   5450   -102    457   -441       C  
-ATOM  10129  O   LEU D1002    -106.864  10.084 -24.404  1.00 46.61           O  
-ANISOU10129  O   LEU D1002     6273   5637   5799    -55    455   -466       O  
-ATOM  10130  CB  LEU D1002    -107.242  12.750 -25.706  1.00 42.48           C  
-ANISOU10130  CB  LEU D1002     5650   5312   5178    -55    467   -410       C  
-ATOM  10131  CG  LEU D1002    -108.312  12.470 -26.765  1.00 43.66           C  
-ANISOU10131  CG  LEU D1002     5786   5500   5304    -65    453   -477       C  
-ATOM  10132  CD1 LEU D1002    -109.571  13.231 -26.469  1.00 46.51           C  
-ANISOU10132  CD1 LEU D1002     6133   5869   5672   -122    451   -456       C  
-ATOM  10133  CD2 LEU D1002    -107.812  12.940 -28.113  1.00 47.30           C  
-ANISOU10133  CD2 LEU D1002     6199   6076   5696     -7    457   -484       C  
-ATOM  10134  N   LEU D1003    -108.976  10.434 -23.796  1.00 43.48           N  
-ANISOU10134  N   LEU D1003     5871   5213   5435   -159    450   -457       N  
-ATOM  10135  CA  LEU D1003    -109.289   9.023 -23.685  1.00 45.37           C  
-ANISOU10135  CA  LEU D1003     6146   5359   5734   -173    438   -502       C  
-ATOM  10136  C   LEU D1003    -110.237   8.597 -24.796  1.00 47.40           C  
-ANISOU10136  C   LEU D1003     6389   5628   5993   -189    416   -591       C  
-ATOM  10137  O   LEU D1003    -111.217   9.281 -25.106  1.00 43.48           O  
-ANISOU10137  O   LEU D1003     5863   5186   5470   -224    414   -597       O  
-ATOM  10138  CB  LEU D1003    -109.950   8.714 -22.352  1.00 46.17           C  
-ANISOU10138  CB  LEU D1003     6266   5389   5888   -229    447   -446       C  
-ATOM  10139  CG  LEU D1003    -109.066   8.580 -21.123  1.00 48.25           C  
-ANISOU10139  CG  LEU D1003     6550   5616   6166   -208    463   -372       C  
-ATOM  10140  CD1 LEU D1003    -108.368   9.891 -20.804  1.00 49.54           C  
-ANISOU10140  CD1 LEU D1003     6688   5860   6274   -182    474   -326       C  
-ATOM  10141  CD2 LEU D1003    -109.914   8.127 -19.952  1.00 47.04           C  
-ANISOU10141  CD2 LEU D1003     6406   5405   6060   -262    472   -318       C  
-ATOM  10142  N   LYS D1004    -109.926   7.451 -25.394  1.00 50.39           N  
-ANISOU10142  N   LYS D1004     6785   5957   6404   -159    396   -668       N  
-ATOM  10143  CA  LYS D1004    -110.856   6.756 -26.286  1.00 52.42           C  
-ANISOU10143  CA  LYS D1004     7031   6200   6687   -177    367   -770       C  
-ATOM  10144  C   LYS D1004    -111.601   5.736 -25.446  1.00 49.81           C  
-ANISOU10144  C   LYS D1004     6727   5737   6462   -242    359   -764       C  
-ATOM  10145  O   LYS D1004    -110.980   4.865 -24.838  1.00 47.41           O  
-ANISOU10145  O   LYS D1004     6458   5334   6221   -229    359   -744       O  
-ATOM  10146  CB  LYS D1004    -110.080   6.074 -27.392  1.00 56.36           C  
-ANISOU10146  CB  LYS D1004     7527   6720   7169   -101    344   -867       C  
-ATOM  10147  CG  LYS D1004    -110.929   5.421 -28.456  1.00 63.05           C  
-ANISOU10147  CG  LYS D1004     8352   7573   8031   -104    307   -995       C  
-ATOM  10148  CD  LYS D1004    -110.023   5.027 -29.611  1.00 71.97           C  
-ANISOU10148  CD  LYS D1004     9466   8768   9111     -9    286  -1089       C  
-ATOM  10149  CE  LYS D1004    -110.559   3.841 -30.385  1.00 77.75           C  
-ANISOU10149  CE  LYS D1004    10191   9449   9901      1    237  -1239       C  
-ATOM  10150  NZ  LYS D1004    -109.645   3.507 -31.516  1.00 83.50           N  
-ANISOU10150  NZ  LYS D1004    10898  10262  10568    107    216  -1337       N  
-ATOM  10151  N   LEU D1005    -112.915   5.906 -25.355  1.00 51.19           N  
-ANISOU10151  N   LEU D1005     6882   5914   6655   -311    354   -768       N  
-ATOM  10152  CA  LEU D1005    -113.761   5.079 -24.501  1.00 56.10           C  
-ANISOU10152  CA  LEU D1005     7516   6422   7377   -384    351   -742       C  
-ATOM  10153  C   LEU D1005    -114.766   4.255 -25.306  1.00 52.99           C  
-ANISOU10153  C   LEU D1005     7103   5985   7045   -422    315   -851       C  
-ATOM  10154  O   LEU D1005    -115.389   4.776 -26.230  1.00 52.29           O  
-ANISOU10154  O   LEU D1005     6978   5989   6899   -422    300   -918       O  
-ATOM  10155  CB  LEU D1005    -114.557   5.972 -23.532  1.00 58.32           C  
-ANISOU10155  CB  LEU D1005     7781   6745   7633   -441    378   -645       C  
-ATOM  10156  CG  LEU D1005    -113.835   6.840 -22.504  1.00 59.08           C  
-ANISOU10156  CG  LEU D1005     7887   6881   7680   -419    410   -539       C  
-ATOM  10157  CD1 LEU D1005    -114.867   7.598 -21.692  1.00 59.74           C  
-ANISOU10157  CD1 LEU D1005     7946   7009   7746   -475    425   -475       C  
-ATOM  10158  CD2 LEU D1005    -112.991   5.973 -21.585  1.00 61.21           C  
-ANISOU10158  CD2 LEU D1005     8193   7056   8007   -401    421   -482       C  
-ATOM  10159  N   LYS D1006    -114.959   3.001 -24.902  1.00 51.62           N  
-ANISOU10159  N   LYS D1006     6948   5671   6994   -457    299   -862       N  
-ATOM  10160  CA  LYS D1006    -116.039   2.179 -25.415  1.00 52.68           C  
-ANISOU10160  CA  LYS D1006     7059   5741   7216   -512    263   -953       C  
-ATOM  10161  C   LYS D1006    -117.142   2.293 -24.391  1.00 53.40           C  
-ANISOU10161  C   LYS D1006     7135   5803   7353   -606    284   -856       C  
-ATOM  10162  O   LYS D1006    -116.911   2.061 -23.218  1.00 53.50           O  
-ANISOU10162  O   LYS D1006     7169   5751   7408   -627    312   -741       O  
-ATOM  10163  CB  LYS D1006    -115.645   0.695 -25.580  1.00 53.99           C  
-ANISOU10163  CB  LYS D1006     7248   5753   7513   -500    228  -1022       C  
-ATOM  10164  N   PHE D1007    -118.332   2.658 -24.857  1.00 54.47           N  
-ANISOU10164  N   PHE D1007     7228   5999   7470   -656    272   -903       N  
-ATOM  10165  CA  PHE D1007    -119.545   2.650 -24.069  1.00 54.29           C  
-ANISOU10165  CA  PHE D1007     7177   5955   7495   -748    285   -834       C  
-ATOM  10166  C   PHE D1007    -120.232   1.285 -24.281  1.00 58.49           C  
-ANISOU10166  C   PHE D1007     7694   6348   8182   -811    248   -901       C  
-ATOM  10167  O   PHE D1007    -120.617   0.964 -25.395  1.00 60.64           O  
-ANISOU10167  O   PHE D1007     7941   6628   8471   -807    205  -1040       O  
-ATOM  10168  CB  PHE D1007    -120.492   3.747 -24.565  1.00 53.62           C  
-ANISOU10168  CB  PHE D1007     7049   6012   7312   -765    286   -862       C  
-ATOM  10169  CG  PHE D1007    -120.044   5.145 -24.256  1.00 51.28           C  
-ANISOU10169  CG  PHE D1007     6758   5839   6887   -719    319   -787       C  
-ATOM  10170  CD1 PHE D1007    -118.876   5.670 -24.818  1.00 51.65           C  
-ANISOU10170  CD1 PHE D1007     6826   5943   6856   -634    322   -808       C  
-ATOM  10171  CD2 PHE D1007    -120.804   5.956 -23.409  1.00 50.46           C  
-ANISOU10171  CD2 PHE D1007     6632   5795   6744   -761    346   -698       C  
-ATOM  10172  CE1 PHE D1007    -118.470   6.972 -24.525  1.00 50.72           C  
-ANISOU10172  CE1 PHE D1007     6707   5925   6639   -598    349   -738       C  
-ATOM  10173  CE2 PHE D1007    -120.398   7.263 -23.116  1.00 49.56           C  
-ANISOU10173  CE2 PHE D1007     6520   5784   6527   -718    369   -640       C  
-ATOM  10174  CZ  PHE D1007    -119.239   7.771 -23.674  1.00 46.38           C  
-ANISOU10174  CZ  PHE D1007     6138   5423   6063   -640    370   -659       C  
-ATOM  10175  N   ASN D1008    -120.386   0.492 -23.225  1.00 60.29           N  
-ANISOU10175  N   ASN D1008     7931   6453   8524   -866    264   -801       N  
-ATOM  10176  CA  ASN D1008    -121.110  -0.787 -23.296  1.00 60.86           C  
-ANISOU10176  CA  ASN D1008     7980   6377   8767   -939    231   -842       C  
-ATOM  10177  C   ASN D1008    -122.516  -0.615 -22.752  1.00 60.31           C  
-ANISOU10177  C   ASN D1008     7859   6332   8725  -1039    245   -777       C  
-ATOM  10178  O   ASN D1008    -122.720  -0.624 -21.539  1.00 57.52           O  
-ANISOU10178  O   ASN D1008     7501   5959   8395  -1081    286   -625       O  
-ATOM  10179  CB  ASN D1008    -120.364  -1.857 -22.504  1.00 62.06           C  
-ANISOU10179  CB  ASN D1008     8170   6367   9044   -935    239   -761       C  
-ATOM  10180  CG  ASN D1008    -119.012  -2.172 -23.106  1.00 62.64           C  
-ANISOU10180  CG  ASN D1008     8290   6407   9104   -836    218   -840       C  
-ATOM  10181  OD1 ASN D1008    -118.893  -2.400 -24.316  1.00 63.39           O  
-ANISOU10181  OD1 ASN D1008     8378   6509   9198   -797    171  -1002       O  
-ATOM  10182  ND2 ASN D1008    -117.985  -2.191 -22.273  1.00 64.69           N  
-ANISOU10182  ND2 ASN D1008     8592   6641   9346   -788    251   -731       N  
-ATOM  10183  N   PHE D1009    -123.473  -0.428 -23.655  1.00 59.32           N  
-ANISOU10183  N   PHE D1009     7688   6265   8587  -1072    213   -892       N  
-ATOM  10184  CA  PHE D1009    -124.862  -0.142 -23.276  1.00 59.02           C  
-ANISOU10184  CA  PHE D1009     7591   6276   8556  -1162    225   -846       C  
-ATOM  10185  C   PHE D1009    -125.629  -1.343 -22.695  1.00 61.98           C  
-ANISOU10185  C   PHE D1009     7932   6498   9118  -1265    216   -795       C  
-ATOM  10186  O   PHE D1009    -125.336  -2.488 -23.035  1.00 60.49           O  
-ANISOU10186  O   PHE D1009     7754   6154   9075  -1274    179   -860       O  
-ATOM  10187  CB  PHE D1009    -125.607   0.418 -24.483  1.00 57.30           C  
-ANISOU10187  CB  PHE D1009     7333   6176   8264  -1157    190   -990       C  
-ATOM  10188  CG  PHE D1009    -125.163   1.792 -24.868  1.00 55.89           C  
-ANISOU10188  CG  PHE D1009     7170   6167   7899  -1075    210   -996       C  
-ATOM  10189  CD1 PHE D1009    -124.173   1.978 -25.815  1.00 55.52           C  
-ANISOU10189  CD1 PHE D1009     7152   6159   7785   -981    190  -1090       C  
-ATOM  10190  CD2 PHE D1009    -125.720   2.911 -24.250  1.00 56.40           C  
-ANISOU10190  CD2 PHE D1009     7215   6354   7862  -1090    247   -901       C  
-ATOM  10191  CE1 PHE D1009    -123.751   3.257 -26.157  1.00 57.72           C  
-ANISOU10191  CE1 PHE D1009     7438   6588   7905   -910    210  -1079       C  
-ATOM  10192  CE2 PHE D1009    -125.301   4.195 -24.587  1.00 55.19           C  
-ANISOU10192  CE2 PHE D1009     7073   6340   7555  -1016    263   -901       C  
-ATOM  10193  CZ  PHE D1009    -124.311   4.369 -25.540  1.00 55.91           C  
-ANISOU10193  CZ  PHE D1009     7192   6462   7589   -930    246   -983       C  
-TER   10194      PHE D1009                                                      
-HETATM10195  S   SO4 A1101     -34.370  15.705 -12.542  1.00 37.32           S  
-ANISOU10195  S   SO4 A1101     4548   4601   5031    -94     79   -213       S  
-HETATM10196  O1  SO4 A1101     -33.126  16.535 -12.469  1.00 37.55           O  
-ANISOU10196  O1  SO4 A1101     4546   4611   5109   -112     88   -221       O  
-HETATM10197  O2  SO4 A1101     -34.504  14.830 -13.833  1.00 41.30           O  
-ANISOU10197  O2  SO4 A1101     5065   5131   5495    -94    102   -190       O  
-HETATM10198  O3  SO4 A1101     -34.353  14.759 -11.373  1.00 37.89           O  
-ANISOU10198  O3  SO4 A1101     4619   4686   5090    -74     55   -247       O  
-HETATM10199  O4  SO4 A1101     -35.532  16.589 -12.369  1.00 29.06           O  
-ANISOU10199  O4  SO4 A1101     3520   3535   3988    -90     67   -200       O  
-HETATM10200  S   SO4 A1102     -47.579  24.690  -7.071  0.50 32.00           S  
-ANISOU10200  S   SO4 A1102     3948   3758   4451     79   -120   -289       S  
-HETATM10201  O1  SO4 A1102     -47.621  25.235  -8.437  0.50 31.70           O  
-ANISOU10201  O1  SO4 A1102     3922   3693   4431     65   -118   -248       O  
-HETATM10202  O2  SO4 A1102     -46.895  23.376  -7.048  0.50 30.34           O  
-ANISOU10202  O2  SO4 A1102     3741   3582   4207     66   -102   -283       O  
-HETATM10203  O3  SO4 A1102     -48.932  24.534  -6.502  0.50 33.78           O  
-ANISOU10203  O3  SO4 A1102     4170   4006   4658    104   -125   -307       O  
-HETATM10204  O4  SO4 A1102     -46.986  25.703  -6.180  0.50 34.79           O  
-ANISOU10204  O4  SO4 A1102     4290   4084   4844     85   -137   -323       O  
-HETATM10205  S   SO4 A1103     -63.994   0.620  -2.925  1.00 43.38           S  
-ANISOU10205  S   SO4 A1103     5185   5545   5754   -106    200    -86       S  
-HETATM10206  O1  SO4 A1103     -63.179   1.066  -4.107  1.00 50.09           O  
-ANISOU10206  O1  SO4 A1103     6055   6380   6598    -94    156   -108       O  
-HETATM10207  O2  SO4 A1103     -65.325   1.154  -3.292  1.00 37.55           O  
-ANISOU10207  O2  SO4 A1103     4402   4817   5050   -107    200   -105       O  
-HETATM10208  O3  SO4 A1103     -63.243   1.195  -1.763  1.00 39.64           O  
-ANISOU10208  O3  SO4 A1103     4738   5094   5231    -86    220    -78       O  
-HETATM10209  O4  SO4 A1103     -64.126  -0.910  -2.872  1.00 44.06           O  
-ANISOU10209  O4  SO4 A1103     5269   5607   5866   -136    210    -60       O  
-HETATM10210  S   SO4 A1104     -66.232  13.306 -23.086  0.50 29.03           S  
-ANISOU10210  S   SO4 A1104     3521   3664   3847    225   -413   -233       S  
-HETATM10211  O1  SO4 A1104     -67.274  12.328 -22.711  0.50 32.22           O  
-ANISOU10211  O1  SO4 A1104     3879   4076   4288    216   -420   -267       O  
-HETATM10212  O2  SO4 A1104     -66.089  13.373 -24.560  0.50 28.52           O  
-ANISOU10212  O2  SO4 A1104     3490   3607   3741    247   -447   -223       O  
-HETATM10213  O3  SO4 A1104     -64.998  12.874 -22.397  0.50 28.67           O  
-ANISOU10213  O3  SO4 A1104     3489   3617   3787    197   -368   -219       O  
-HETATM10214  O4  SO4 A1104     -66.722  14.607 -22.606  0.50 28.99           O  
-ANISOU10214  O4  SO4 A1104     3507   3643   3863    242   -417   -227       O  
-HETATM10215  N1  2YQ A1105     -40.422   6.025 -10.001  1.00 19.14           N  
-ANISOU10215  N1  2YQ A1105     2369   2404   2500     14     -4   -239       N  
-HETATM10216  N3  2YQ A1105     -37.918   8.786  -8.269  1.00 18.48           N  
-ANISOU10216  N3  2YQ A1105     2248   2304   2471     15    -12   -278       N  
-HETATM10217  C4  2YQ A1105     -41.676   7.708 -11.076  1.00 19.31           C  
-ANISOU10217  C4  2YQ A1105     2392   2420   2525      2      6   -217       C  
-HETATM10218  C5  2YQ A1105     -38.493   6.442  -8.560  1.00 19.96           C  
-ANISOU10218  C5  2YQ A1105     2455   2504   2622     25    -15   -269       C  
-HETATM10219  C6  2YQ A1105     -38.006   7.503  -7.559  1.00 20.24           C  
-ANISOU10219  C6  2YQ A1105     2481   2534   2673     28    -22   -283       C  
-HETATM10220  C7  2YQ A1105     -38.923   9.161  -9.081  1.00 19.04           C  
-ANISOU10220  C7  2YQ A1105     2327   2373   2536      7     -2   -257       C  
-HETATM10221  C8  2YQ A1105     -39.129  10.515  -9.324  1.00 19.30           C  
-ANISOU10221  C8  2YQ A1105     2355   2393   2586     -2      2   -251       C  
-HETATM10222  C10 2YQ A1105     -41.029  10.025 -10.727  1.00 19.28           C  
-ANISOU10222  C10 2YQ A1105     2374   2398   2554     -5     11   -218       C  
-HETATM10223  C13 2YQ A1105     -34.287   6.636  -7.460  1.00 22.57           C  
-ANISOU10223  C13 2YQ A1105     2734   2836   3006     39    -36   -335       C  
-HETATM10224  C15 2YQ A1105     -35.378   5.776  -5.506  1.00 23.41           C  
-ANISOU10224  C15 2YQ A1105     2873   2945   3078     66    -63   -333       C  
-HETATM10225  C17 2YQ A1105     -38.769   5.199  -7.865  1.00 19.99           C  
-ANISOU10225  C17 2YQ A1105     2473   2512   2612     36    -25   -269       C  
-HETATM10226  F2  2YQ A1105     -33.098   5.382  -5.827  1.00 24.44           F  
-ANISOU10226  F2  2YQ A1105     2970   3078   3239     72    -72   -367       F  
-HETATM10227  C14 2YQ A1105     -34.229   5.945  -6.262  1.00 23.24           C  
-ANISOU10227  C14 2YQ A1105     2829   2923   3079     59    -57   -346       C  
-HETATM10228  C12 2YQ A1105     -35.519   7.161  -7.866  1.00 22.40           C  
-ANISOU10228  C12 2YQ A1105     2726   2811   2974     29    -25   -313       C  
-HETATM10229  C16 2YQ A1105     -36.592   6.314  -5.912  1.00 21.61           C  
-ANISOU10229  C16 2YQ A1105     2653   2714   2843     54    -49   -313       C  
-HETATM10230  C11 2YQ A1105     -36.676   6.995  -7.103  1.00 20.98           C  
-ANISOU10230  C11 2YQ A1105     2565   2632   2776     37    -32   -304       C  
-HETATM10231  N6  2YQ A1105     -39.695   4.942  -6.923  1.00 21.24           N  
-ANISOU10231  N6  2YQ A1105     2642   2670   2758     42    -30   -262       N  
-HETATM10232  C18 2YQ A1105     -39.523   3.660  -6.508  1.00 22.11           C  
-ANISOU10232  C18 2YQ A1105     2762   2780   2858     51    -39   -262       C  
-HETATM10233  N5  2YQ A1105     -38.495   3.098  -7.160  1.00 20.23           N  
-ANISOU10233  N5  2YQ A1105     2518   2542   2628     53    -41   -272       N  
-HETATM10234  N4  2YQ A1105     -38.021   4.092  -7.984  1.00 21.45           N  
-ANISOU10234  N4  2YQ A1105     2657   2698   2794     43    -31   -278       N  
-HETATM10235  C19 2YQ A1105     -36.860   3.733  -8.837  1.00 20.29           C  
-ANISOU10235  C19 2YQ A1105     2497   2554   2656     42    -27   -290       C  
-HETATM10236  C3  2YQ A1105     -39.614   6.907  -9.414  1.00 19.90           C  
-ANISOU10236  C3  2YQ A1105     2455   2496   2610     15     -5   -250       C  
-HETATM10237  C2  2YQ A1105     -39.791   8.250  -9.655  1.00 19.45           C  
-ANISOU10237  C2  2YQ A1105     2392   2432   2566      7      1   -244       C  
-HETATM10238  C9  2YQ A1105     -40.157  10.931 -10.120  1.00 19.62           C  
-ANISOU10238  C9  2YQ A1105     2405   2431   2621     -7      9   -230       C  
-HETATM10239  F1  2YQ A1105     -40.319  12.229 -10.275  1.00 20.94           F  
-ANISOU10239  F1  2YQ A1105     2568   2582   2807    -13     10   -224       F  
-HETATM10240  C1  2YQ A1105     -40.850   8.665 -10.476  1.00 19.59           C  
-ANISOU10240  C1  2YQ A1105     2418   2449   2579      1      7   -226       C  
-HETATM10241  O   2YQ A1105     -42.601   8.009 -11.835  1.00 18.52           O  
-ANISOU10241  O   2YQ A1105     2298   2320   2420     -1      8   -204       O  
-HETATM10242  N2  2YQ A1105     -41.467   6.427 -10.846  1.00 18.62           N  
-ANISOU10242  N2  2YQ A1105     2308   2337   2428      8      1   -224       N  
-HETATM10243  C1  GOL A1106     -33.462  23.360   1.707  1.00 53.63           C  
-HETATM10244  O1  GOL A1106     -34.313  23.727   0.621  1.00 42.76           O  
-HETATM10245  C2  GOL A1106     -32.898  21.999   1.335  1.00 56.18           C  
-HETATM10246  O2  GOL A1106     -33.686  21.620   0.231  1.00 51.03           O  
-HETATM10247  C3  GOL A1106     -33.010  20.917   2.421  1.00 62.55           C  
-HETATM10248  O3  GOL A1106     -32.720  19.628   1.858  1.00 56.32           O  
-HETATM10249  C1  GOL A1107     -52.358  19.076  11.923  1.00 60.91           C  
-HETATM10250  O1  GOL A1107     -51.186  18.755  12.686  1.00 54.88           O  
-HETATM10251  C2  GOL A1107     -52.387  18.260  10.628  1.00 62.05           C  
-HETATM10252  O2  GOL A1107     -52.088  19.173   9.582  1.00 60.59           O  
-HETATM10253  C3  GOL A1107     -53.756  17.593  10.383  1.00 65.19           C  
-HETATM10254  O3  GOL A1107     -53.995  17.284   8.992  1.00 59.26           O  
-HETATM10255  S   SO4 B1101     -96.011   4.644  10.082  1.00 55.52           S  
-ANISOU10255  S   SO4 B1101     6348   7783   6963    -49    190    502       S  
-HETATM10256  O1  SO4 B1101     -95.819   4.156   8.706  1.00 56.77           O  
-ANISOU10256  O1  SO4 B1101     6506   7935   7129    -86    135    541       O  
-HETATM10257  O2  SO4 B1101     -97.421   5.093  10.210  1.00 60.88           O  
-ANISOU10257  O2  SO4 B1101     6933   8541   7658    -22    234    536       O  
-HETATM10258  O3  SO4 B1101     -95.718   3.468  10.985  1.00 54.03           O  
-ANISOU10258  O3  SO4 B1101     6221   7599   6709   -114    180    484       O  
-HETATM10259  O4  SO4 B1101     -95.188   5.887  10.280  1.00 47.74           O  
-ANISOU10259  O4  SO4 B1101     5390   6724   6024     25    211    456       O  
-HETATM10260  S   SO4 B1102     -66.128   5.793   7.040  1.00 52.15           S  
-ANISOU10260  S   SO4 B1102     6135   6303   7377    -30   -244   -222       S  
-HETATM10261  O1  SO4 B1102     -66.422   5.175   5.737  1.00 57.49           O  
-ANISOU10261  O1  SO4 B1102     6814   6991   8041    -25   -194   -196       O  
-HETATM10262  O2  SO4 B1102     -65.353   7.062   6.964  1.00 53.35           O  
-ANISOU10262  O2  SO4 B1102     6245   6434   7592    -54   -228   -244       O  
-HETATM10263  O3  SO4 B1102     -65.329   4.817   7.806  1.00 57.10           O  
-ANISOU10263  O3  SO4 B1102     6748   6931   8018    -10   -309   -244       O  
-HETATM10264  O4  SO4 B1102     -67.429   6.081   7.668  1.00 52.68           O  
-ANISOU10264  O4  SO4 B1102     6259   6379   7379    -30   -249   -205       O  
-HETATM10265  S   SO4 B1103     -85.495  17.746   7.865  0.50 31.79           S  
-ANISOU10265  S   SO4 B1103     3689   3781   4610    392    261    156       S  
-HETATM10266  O1  SO4 B1103     -84.293  18.352   7.287  0.50 31.21           O  
-ANISOU10266  O1  SO4 B1103     3643   3631   4584    368    249    148       O  
-HETATM10267  O2  SO4 B1103     -85.722  16.433   7.244  0.50 33.84           O  
-ANISOU10267  O2  SO4 B1103     3922   4120   4818    351    230    201       O  
-HETATM10268  O3  SO4 B1103     -86.706  18.535   7.644  0.50 34.54           O  
-ANISOU10268  O3  SO4 B1103     4003   4132   4990    458    295    196       O  
-HETATM10269  O4  SO4 B1103     -85.310  17.628   9.317  0.50 34.53           O  
-ANISOU10269  O4  SO4 B1103     4067   4126   4926    390    269     79       O  
-HETATM10270  S   SO4 B1104     -81.509  16.695 -10.577  0.50 28.99           S  
-ANISOU10270  S   SO4 B1104     3429   3560   4026    -55    178    900       S  
-HETATM10271  O1  SO4 B1104     -80.730  17.171 -11.740  0.50 29.40           O  
-ANISOU10271  O1  SO4 B1104     3516   3592   4061    -97    209    941       O  
-HETATM10272  O2  SO4 B1104     -82.919  16.748 -10.985  0.50 25.60           O  
-ANISOU10272  O2  SO4 B1104     2984   3182   3562    -29    136    973       O  
-HETATM10273  O3  SO4 B1104     -81.021  15.334 -10.214  0.50 26.82           O  
-ANISOU10273  O3  SO4 B1104     3151   3325   3715    -87    178    824       O  
-HETATM10274  O4  SO4 B1104     -81.176  17.544  -9.408  0.50 27.40           O  
-ANISOU10274  O4  SO4 B1104     3216   3282   3913    -15    196    859       O  
-HETATM10275  N1  2YQ B1105     -88.298  -2.030   4.917  1.00 23.86           N  
-ANISOU10275  N1  2YQ B1105     2804   3386   2876   -343   -156    411       N  
-HETATM10276  N3  2YQ B1105     -91.425   0.554   4.037  1.00 26.14           N  
-ANISOU10276  N3  2YQ B1105     2891   3843   3196   -288    -95    522       N  
-HETATM10277  C4  2YQ B1105     -87.340  -0.490   6.484  1.00 24.46           C  
-ANISOU10277  C4  2YQ B1105     2874   3419   3002   -252   -122    359       C  
-HETATM10278  C5  2YQ B1105     -90.367  -1.635   3.664  1.00 27.45           C  
-ANISOU10278  C5  2YQ B1105     3167   3953   3311   -378   -150    491       C  
-HETATM10279  C6  2YQ B1105     -91.097  -0.423   2.983  1.00 27.86           C  
-ANISOU10279  C6  2YQ B1105     3148   4049   3388   -343   -132    527       C  
-HETATM10280  C7  2YQ B1105     -90.478   0.914   4.943  1.00 24.53           C  
-ANISOU10280  C7  2YQ B1105     2722   3585   3012   -250    -79    476       C  
-HETATM10281  C8  2YQ B1105     -90.564   2.148   5.569  1.00 23.82           C  
-ANISOU10281  C8  2YQ B1105     2602   3491   2958   -187    -43    464       C  
-HETATM10282  C10 2YQ B1105     -88.479   1.657   6.756  1.00 23.63           C  
-ANISOU10282  C10 2YQ B1105     2678   3363   2936   -180    -60    379       C  
-HETATM10283  C13 2YQ B1105     -94.586  -1.845   2.411  1.00 37.91           C  
-ANISOU10283  C13 2YQ B1105     4305   5523   4578   -485   -170    649       C  
-HETATM10284  C15 2YQ B1105     -93.423  -1.765   0.287  1.00 35.05           C  
-ANISOU10284  C15 2YQ B1105     3999   5104   4216   -489   -209    639       C  
-HETATM10285  C17 2YQ B1105     -89.892  -2.561   2.607  1.00 28.27           C  
-ANISOU10285  C17 2YQ B1105     3317   4031   3395   -423   -180    486       C  
-HETATM10286  F2  2YQ B1105     -95.611  -2.611   0.415  1.00 45.41           F  
-ANISOU10286  F2  2YQ B1105     5228   6544   5483   -580   -235    709       F  
-HETATM10287  C14 2YQ B1105     -94.552  -2.079   1.035  1.00 40.66           C  
-ANISOU10287  C14 2YQ B1105     4662   5875   4912   -517   -205    666       C  
-HETATM10288  C12 2YQ B1105     -93.470  -1.287   3.055  1.00 35.74           C  
-ANISOU10288  C12 2YQ B1105     4068   5179   4332   -425   -146    603       C  
-HETATM10289  C16 2YQ B1105     -92.327  -1.218   0.944  1.00 34.54           C  
-ANISOU10289  C16 2YQ B1105     3965   4974   4186   -430   -181    596       C  
-HETATM10290  C11 2YQ B1105     -92.326  -0.971   2.323  1.00 31.73           C  
-ANISOU10290  C11 2YQ B1105     3602   4610   3845   -398   -153    577       C  
-HETATM10291  N6  2YQ B1105     -88.939  -2.309   1.672  1.00 31.69           N  
-ANISOU10291  N6  2YQ B1105     3772   4421   3847   -405   -182    465       N  
-HETATM10292  C18 2YQ B1105     -88.827  -3.375   0.829  1.00 30.35           C  
-ANISOU10292  C18 2YQ B1105     3645   4241   3645   -458   -208    462       C  
-HETATM10293  N5  2YQ B1105     -89.724  -4.297   1.205  1.00 27.76           N  
-ANISOU10293  N5  2YQ B1105     3321   3947   3279   -515   -227    483       N  
-HETATM10294  N4  2YQ B1105     -90.368  -3.770   2.328  1.00 28.04           N  
-ANISOU10294  N4  2YQ B1105     3314   4018   3324   -492   -208    499       N  
-HETATM10295  C19 2YQ B1105     -91.382  -4.678   2.985  1.00 28.68           C  
-ANISOU10295  C19 2YQ B1105     3391   4140   3365   -552   -220    525       C  
-HETATM10296  C3  2YQ B1105     -89.318  -1.213   4.621  1.00 25.02           C  
-ANISOU10296  C3  2YQ B1105     2888   3588   3029   -330   -135    446       C  
-HETATM10297  C2  2YQ B1105     -89.398   0.041   5.247  1.00 25.25           C  
-ANISOU10297  C2  2YQ B1105     2882   3622   3091   -271   -102    438       C  
-HETATM10298  C9  2YQ B1105     -89.563   2.492   6.463  1.00 24.49           C  
-ANISOU10298  C9  2YQ B1105     2726   3520   3059   -156    -33    413       C  
-HETATM10299  F1  2YQ B1105     -89.589   3.675   7.051  1.00 27.60           F  
-ANISOU10299  F1  2YQ B1105     3098   3902   3486   -100      1    395       F  
-HETATM10300  C1  2YQ B1105     -88.382   0.409   6.155  1.00 23.68           C  
-ANISOU10300  C1  2YQ B1105     2714   3370   2912   -234    -94    392       C  
-HETATM10301  O   2YQ B1105     -86.405  -0.223   7.321  1.00 25.33           O  
-ANISOU10301  O   2YQ B1105     3011   3485   3129   -223   -123    320       O  
-HETATM10302  N2  2YQ B1105     -87.298  -1.684   5.848  1.00 22.75           N  
-ANISOU10302  N2  2YQ B1105     2689   3197   2759   -302   -151    370       N  
-HETATM10303  S   SO4 B1106     -81.718  11.489  -8.680  0.50 54.85           S  
-HETATM10304  O1  SO4 B1106     -80.608  11.122  -9.598  0.50 49.89           O  
-HETATM10305  O2  SO4 B1106     -82.510  12.609  -9.231  0.50 46.35           O  
-HETATM10306  O3  SO4 B1106     -82.659  10.351  -8.464  0.50 54.35           O  
-HETATM10307  O4  SO4 B1106     -81.080  11.865  -7.393  0.50 49.47           O  
-HETATM10308  S   SO4 C1101     -63.783  37.785 -19.360  1.00 54.01           S  
-ANISOU10308  S   SO4 C1101     6792   6982   6747   -193     97   -327       S  
-HETATM10309  O1  SO4 C1101     -63.813  36.517 -20.149  1.00 53.91           O  
-ANISOU10309  O1  SO4 C1101     6770   6987   6726   -146     78   -281       O  
-HETATM10310  O2  SO4 C1101     -64.071  38.947 -20.348  1.00 40.09           O  
-ANISOU10310  O2  SO4 C1101     5051   5149   5032   -237    142   -317       O  
-HETATM10311  O3  SO4 C1101     -62.432  37.786 -18.699  1.00 43.29           O  
-ANISOU10311  O3  SO4 C1101     5385   5706   5359   -215     73   -384       O  
-HETATM10312  O4  SO4 C1101     -64.772  37.658 -18.281  1.00 36.26           O  
-ANISOU10312  O4  SO4 C1101     4579   4716   4484   -162     94   -322       O  
-HETATM10313  S   SO4 C1102     -93.949  35.578 -19.518  1.00 59.18           S  
-ANISOU10313  S   SO4 C1102     7260   7900   7324    284    399    467       S  
-HETATM10314  O1  SO4 C1102     -93.949  34.664 -20.681  1.00 67.11           O  
-ANISOU10314  O1  SO4 C1102     8223   8946   8332    228    367    454       O  
-HETATM10315  O2  SO4 C1102     -94.685  36.821 -19.834  1.00 64.24           O  
-ANISOU10315  O2  SO4 C1102     7881   8581   7944    361    426    504       O  
-HETATM10316  O3  SO4 C1102     -94.670  34.945 -18.394  1.00 61.69           O  
-ANISOU10316  O3  SO4 C1102     7564   8238   7638    267    416    473       O  
-HETATM10317  O4  SO4 C1102     -92.532  35.840 -19.139  1.00 55.28           O  
-ANISOU10317  O4  SO4 C1102     6841   7312   6851    281    393    437       O  
-HETATM10318  S   SO4 C1103     -78.259  18.570 -46.229  0.50 33.09           S  
-ANISOU10318  S   SO4 C1103     4234   4602   3736   -258    -80   -301       S  
-HETATM10319  O1  SO4 C1103     -77.289  18.468 -47.322  0.50 33.42           O  
-ANISOU10319  O1  SO4 C1103     4295   4657   3745   -215    -83   -311       O  
-HETATM10320  O2  SO4 C1103     -79.558  18.257 -46.832  0.50 31.70           O  
-ANISOU10320  O2  SO4 C1103     4016   4500   3527   -315   -100   -343       O  
-HETATM10321  O3  SO4 C1103     -77.805  17.570 -45.251  0.50 31.33           O  
-ANISOU10321  O3  SO4 C1103     4081   4276   3546   -281    -57   -319       O  
-HETATM10322  O4  SO4 C1103     -78.367  19.938 -45.622  0.50 30.03           O  
-ANISOU10322  O4  SO4 C1103     3802   4237   3372   -217    -79   -236       O  
-HETATM10323  N1  2YQ C1104     -71.491  33.627 -26.897  1.00 19.07           N  
-ANISOU10323  N1  2YQ C1104     2474   2376   2398    -10    130     44       N  
-HETATM10324  N3  2YQ C1104     -68.491  32.366 -24.299  1.00 17.77           N  
-ANISOU10324  N3  2YQ C1104     2294   2275   2185     -1     81    -42       N  
-HETATM10325  C4  2YQ C1104     -72.469  35.026 -25.267  1.00 19.46           C  
-ANISOU10325  C4  2YQ C1104     2547   2388   2458    -10    159     40       C  
-HETATM10326  C5  2YQ C1104     -69.458  32.292 -26.545  1.00 19.03           C  
-ANISOU10326  C5  2YQ C1104     2454   2411   2366     -6     96      4       C  
-HETATM10327  C6  2YQ C1104     -68.753  31.489 -25.429  1.00 19.63           C  
-ANISOU10327  C6  2YQ C1104     2531   2508   2419     10     76    -19       C  
-HETATM10328  C7  2YQ C1104     -69.447  33.244 -23.883  1.00 18.90           C  
-ANISOU10328  C7  2YQ C1104     2451   2388   2343    -11    100    -35       C  
-HETATM10329  C8  2YQ C1104     -69.417  33.744 -22.588  1.00 18.46           C  
-ANISOU10329  C8  2YQ C1104     2403   2332   2280    -14    102    -58       C  
-HETATM10330  C10 2YQ C1104     -71.403  35.049 -23.052  1.00 18.93           C  
-ANISOU10330  C10 2YQ C1104     2489   2331   2373    -18    144    -17       C  
-HETATM10331  C13 2YQ C1104     -65.261  31.071 -26.837  1.00 23.72           C  
-ANISOU10331  C13 2YQ C1104     2982   3118   2912     14     57    -58       C  
-HETATM10332  C15 2YQ C1104     -66.428  28.954 -27.004  1.00 22.67           C  
-ANISOU10332  C15 2YQ C1104     2898   2958   2756     62     43    -26       C  
-HETATM10333  C17 2YQ C1104     -69.947  31.353 -27.558  1.00 20.03           C  
-ANISOU10333  C17 2YQ C1104     2585   2541   2487      5     88     24       C  
-HETATM10334  F2  2YQ C1104     -64.247  29.168 -27.751  1.00 28.58           F  
-ANISOU10334  F2  2YQ C1104     3595   3772   3490     67     37    -50       F  
-HETATM10335  C14 2YQ C1104     -65.315  29.729 -27.220  1.00 24.89           C  
-ANISOU10335  C14 2YQ C1104     3146   3271   3041     48     44    -44       C  
-HETATM10336  C12 2YQ C1104     -66.388  31.646 -26.276  1.00 22.21           C  
-ANISOU10336  C12 2YQ C1104     2812   2890   2736      1     67    -50       C  
-HETATM10337  C16 2YQ C1104     -67.528  29.551 -26.393  1.00 21.90           C  
-ANISOU10337  C16 2YQ C1104     2814   2832   2675     45     52    -19       C  
-HETATM10338  C11 2YQ C1104     -67.522  30.884 -26.037  1.00 20.34           C  
-ANISOU10338  C11 2YQ C1104     2603   2630   2495     20     64    -29       C  
-HETATM10339  N6  2YQ C1104     -70.848  30.382 -27.356  1.00 22.43           N  
-ANISOU10339  N6  2YQ C1104     2904   2837   2782     15     81     35       N  
-HETATM10340  C18 2YQ C1104     -70.996  29.664 -28.527  1.00 21.53           C  
-ANISOU10340  C18 2YQ C1104     2790   2730   2662     17     75     44       C  
-HETATM10341  N5  2YQ C1104     -70.180  30.150 -29.451  1.00 18.24           N  
-ANISOU10341  N5  2YQ C1104     2356   2326   2248     14     78     42       N  
-HETATM10342  N4  2YQ C1104     -69.513  31.191 -28.828  1.00 20.31           N  
-ANISOU10342  N4  2YQ C1104     2609   2588   2521      5     87     30       N  
-HETATM10343  C19 2YQ C1104     -68.486  31.935 -29.645  1.00 20.05           C  
-ANISOU10343  C19 2YQ C1104     2555   2568   2496     -5     98     26       C  
-HETATM10344  C3  2YQ C1104     -70.510  33.210 -26.061  1.00 19.00           C  
-ANISOU10344  C3  2YQ C1104     2463   2380   2377    -12    115     15       C  
-HETATM10345  C2  2YQ C1104     -70.474  33.675 -24.765  1.00 18.87           C  
-ANISOU10345  C2  2YQ C1104     2455   2357   2358    -15    118     -5       C  
-HETATM10346  C9  2YQ C1104     -70.405  34.642 -22.185  1.00 19.78           C  
-ANISOU10346  C9  2YQ C1104     2588   2466   2461    -19    124    -50       C  
-HETATM10347  F1  2YQ C1104     -70.401  35.124 -20.915  1.00 20.71           F  
-ANISOU10347  F1  2YQ C1104     2716   2583   2569    -20    127    -75       F  
-HETATM10348  C1  2YQ C1104     -71.458  34.565 -24.361  1.00 19.02           C  
-ANISOU10348  C1  2YQ C1104     2489   2349   2390    -16    140      6       C  
-HETATM10349  O   2YQ C1104     -73.377  35.873 -24.924  1.00 19.59           O  
-ANISOU10349  O   2YQ C1104     2577   2382   2483     -3    182     54       O  
-HETATM10350  N2  2YQ C1104     -72.486  34.547 -26.520  1.00 17.45           N  
-ANISOU10350  N2  2YQ C1104     2280   2148   2203     -8    152     58       N  
-HETATM10351  C1  GOL C1105     -64.636  32.391 -22.449  1.00 36.90           C  
-HETATM10352  O1  GOL C1105     -64.756  33.445 -21.434  1.00 31.84           O  
-HETATM10353  C2  GOL C1105     -65.668  31.286 -22.190  1.00 32.91           C  
-HETATM10354  O2  GOL C1105     -66.929  31.861 -22.353  1.00 28.13           O  
-HETATM10355  C3  GOL C1105     -65.809  30.142 -23.168  1.00 35.07           C  
-HETATM10356  O3  GOL C1105     -64.758  29.245 -23.151  1.00 31.56           O  
-HETATM10357  S   SO4 D1101     -95.974  26.230 -25.978  1.00 44.87           S  
-ANISOU10357  S   SO4 D1101     5146   6397   5507   -328    224    253       S  
-HETATM10358  O1  SO4 D1101     -95.459  27.094 -27.054  1.00 50.00           O  
-ANISOU10358  O1  SO4 D1101     5788   7070   6139   -271    197    259       O  
-HETATM10359  O2  SO4 D1101     -96.697  25.170 -26.746  1.00 51.73           O  
-ANISOU10359  O2  SO4 D1101     5961   7329   6364   -420    214    214       O  
-HETATM10360  O3  SO4 D1101     -96.897  26.998 -25.123  1.00 46.43           O  
-ANISOU10360  O3  SO4 D1101     5304   6643   5694   -281    250    295       O  
-HETATM10361  O4  SO4 D1101     -94.900  25.599 -25.202  1.00 43.48           O  
-ANISOU10361  O4  SO4 D1101     5060   6098   5361   -343    236    241       O  
-HETATM10362  S   SO4 D1102    -126.742  16.777 -13.106  1.00 66.04           S  
-ANISOU10362  S   SO4 D1102     8229   8809   8053   -670    470   -142       S  
-HETATM10363  O1  SO4 D1102    -126.878  18.086 -13.831  1.00 58.88           O  
-ANISOU10363  O1  SO4 D1102     7318   7933   7122   -631    440   -212       O  
-HETATM10364  O2  SO4 D1102    -126.502  15.653 -14.105  1.00 51.19           O  
-ANISOU10364  O2  SO4 D1102     6390   6819   6239   -725    478   -146       O  
-HETATM10365  O3  SO4 D1102    -127.991  16.615 -12.317  1.00 61.22           O  
-ANISOU10365  O3  SO4 D1102     7557   8295   7407   -698    483   -103       O  
-HETATM10366  O4  SO4 D1102    -125.652  16.884 -12.090  1.00 50.54           O  
-ANISOU10366  O4  SO4 D1102     6278   6848   6076   -615    475   -107       O  
-HETATM10367  S   SO4 D1103    -113.863  21.268  -2.874  0.50 37.58           S  
-ANISOU10367  S   SO4 D1103     4490   5558   4231    141    293   -305       S  
-HETATM10368  O1  SO4 D1103    -112.447  21.654  -2.817  0.50 40.29           O  
-ANISOU10368  O1  SO4 D1103     4833   5863   4612    178    265   -354       O  
-HETATM10369  O2  SO4 D1103    -114.345  21.304  -4.286  0.50 37.63           O  
-ANISOU10369  O2  SO4 D1103     4549   5440   4308     61    303   -296       O  
-HETATM10370  O3  SO4 D1103    -114.028  19.896  -2.367  0.50 42.18           O  
-ANISOU10370  O3  SO4 D1103     5087   6182   4758    133    347   -189       O  
-HETATM10371  O4  SO4 D1103    -114.605  22.205  -2.022  0.50 39.62           O  
-ANISOU10371  O4  SO4 D1103     4675   5941   4438    196    254   -381       O  
-HETATM10372  N1  2YQ D1104    -120.146  19.642 -22.258  1.00 25.68           N  
-ANISOU10372  N1  2YQ D1104     3309   3414   3033   -445    398   -352       N  
-HETATM10373  N3  2YQ D1104    -122.729  21.210 -19.390  1.00 27.63           N  
-ANISOU10373  N3  2YQ D1104     3483   3756   3258   -472    372   -345       N  
-HETATM10374  C4  2YQ D1104    -118.968  18.368 -20.577  1.00 24.07           C  
-ANISOU10374  C4  2YQ D1104     3157   3117   2872   -457    414   -323       C  
-HETATM10375  C5  2YQ D1104    -122.081  21.079 -21.723  1.00 27.82           C  
-ANISOU10375  C5  2YQ D1104     3521   3770   3279   -456    376   -357       C  
-HETATM10376  C6  2YQ D1104    -122.581  22.004 -20.585  1.00 27.90           C  
-ANISOU10376  C6  2YQ D1104     3506   3802   3293   -445    362   -348       C  
-HETATM10377  C7  2YQ D1104    -121.735  20.344 -19.022  1.00 27.28           C  
-ANISOU10377  C7  2YQ D1104     3474   3657   3235   -476    386   -328       C  
-HETATM10378  C8  2YQ D1104    -121.621  19.992 -17.666  1.00 26.57           C  
-ANISOU10378  C8  2YQ D1104     3385   3564   3145   -480    393   -307       C  
-HETATM10379  C10 2YQ D1104    -119.735  18.566 -18.211  1.00 24.44           C  
-ANISOU10379  C10 2YQ D1104     3183   3187   2915   -475    415   -288       C  
-HETATM10380  C13 2YQ D1104    -126.182  22.193 -21.606  1.00 30.71           C  
-ANISOU10380  C13 2YQ D1104     3783   4325   3562   -498    347   -415       C  
-HETATM10381  C15 2YQ D1104    -125.104  24.267 -22.184  1.00 30.13           C  
-ANISOU10381  C15 2YQ D1104     3692   4234   3521   -408    326   -372       C  
-HETATM10382  C17 2YQ D1104    -121.729  21.889 -22.932  1.00 29.98           C  
-ANISOU10382  C17 2YQ D1104     3777   4068   3545   -417    371   -345       C  
-HETATM10383  F2  2YQ D1104    -127.363  23.913 -22.658  1.00 31.12           F  
-ANISOU10383  F2  2YQ D1104     3774   4473   3577   -448    322   -422       F  
-HETATM10384  C14 2YQ D1104    -126.221  23.458 -22.168  1.00 30.44           C  
-ANISOU10384  C14 2YQ D1104     3724   4318   3523   -451    332   -405       C  
-HETATM10385  C12 2YQ D1104    -124.993  21.726 -21.075  1.00 31.13           C  
-ANISOU10385  C12 2YQ D1104     3871   4310   3646   -495    358   -393       C  
-HETATM10386  C16 2YQ D1104    -123.913  23.776 -21.648  1.00 29.16           C  
-ANISOU10386  C16 2YQ D1104     3604   4047   3429   -410    336   -356       C  
-HETATM10387  C11 2YQ D1104    -123.858  22.522 -21.087  1.00 28.49           C  
-ANISOU10387  C11 2YQ D1104     3546   3940   3338   -450    352   -368       C  
-HETATM10388  N6  2YQ D1104    -120.734  22.827 -23.118  1.00 31.78           N  
-ANISOU10388  N6  2YQ D1104     3998   4278   3800   -376    367   -305       N  
-HETATM10389  C18 2YQ D1104    -120.810  23.314 -24.378  1.00 34.21           C  
-ANISOU10389  C18 2YQ D1104     4281   4630   4088   -351    368   -290       C  
-HETATM10390  N5  2YQ D1104    -121.860  22.718 -25.004  1.00 32.92           N  
-ANISOU10390  N5  2YQ D1104     4110   4518   3879   -372    369   -331       N  
-HETATM10391  N4  2YQ D1104    -122.414  21.849 -24.060  1.00 32.35           N  
-ANISOU10391  N4  2YQ D1104     4059   4423   3811   -417    370   -365       N  
-HETATM10392  C19 2YQ D1104    -123.580  21.017 -24.504  1.00 33.97           C  
-ANISOU10392  C19 2YQ D1104     4256   4669   3984   -455    369   -416       C  
-HETATM10393  C3  2YQ D1104    -120.990  20.167 -21.320  1.00 26.50           C  
-ANISOU10393  C3  2YQ D1104     3394   3541   3136   -459    390   -346       C  
-HETATM10394  C2  2YQ D1104    -120.844  19.821 -19.965  1.00 25.84           C  
-ANISOU10394  C2  2YQ D1104     3321   3433   3066   -470    395   -329       C  
-HETATM10395  C9  2YQ D1104    -120.620  19.118 -17.262  1.00 25.67           C  
-ANISOU10395  C9  2YQ D1104     3305   3397   3051   -479    408   -283       C  
-HETATM10396  F1  2YQ D1104    -120.545  18.836 -15.934  1.00 28.31           F  
-ANISOU10396  F1  2YQ D1104     3633   3744   3377   -474    415   -255       F  
-HETATM10397  C1  2YQ D1104    -119.832  18.914 -19.574  1.00 24.78           C  
-ANISOU10397  C1  2YQ D1104     3222   3241   2953   -470    408   -314       C  
-HETATM10398  O   2YQ D1104    -118.045  17.549 -20.297  1.00 24.03           O  
-ANISOU10398  O   2YQ D1104     3184   3061   2886   -451    425   -313       O  
-HETATM10399  N2  2YQ D1104    -119.120  18.715 -21.880  1.00 23.83           N  
-ANISOU10399  N2  2YQ D1104     3113   3120   2823   -444    409   -344       N  
-HETATM10400  O   HOH A1201     -38.125  -0.441 -31.066  1.00 37.54           O  
-HETATM10401  O   HOH A1202     -51.481  25.262   1.204  0.50 28.02           O  
-HETATM10402  O   HOH A1203     -27.878  26.141 -10.981  1.00 31.58           O  
-HETATM10403  O   HOH A1204     -60.983  21.091   1.825  1.00 45.05           O  
-HETATM10404  O   HOH A1205     -39.100  16.514   8.146  1.00 24.61           O  
-HETATM10405  O   HOH A1206     -61.042   4.782   5.203  1.00 35.35           O  
-HETATM10406  O   HOH A1207     -31.823  16.848   5.084  1.00 52.45           O  
-HETATM10407  O   HOH A1208     -45.980  14.893  10.715  1.00 34.21           O  
-HETATM10408  O   HOH A1209     -30.639 -19.228 -15.276  1.00 39.13           O  
-HETATM10409  O   HOH A1210     -32.146  -0.107   6.155  1.00 37.86           O  
-HETATM10410  O   HOH A1211     -38.742   2.491 -30.911  1.00 50.75           O  
-HETATM10411  O   HOH A1212     -35.251   8.198   5.816  1.00 42.75           O  
-HETATM10412  O   HOH A1213     -30.599   2.244   5.363  1.00 55.72           O  
-HETATM10413  O   HOH A1214     -27.655   8.593  -0.595  1.00 56.90           O  
-HETATM10414  O   HOH A1215     -36.326  23.793   5.401  1.00 50.22           O  
-HETATM10415  O   HOH A1216     -67.717  20.672   1.890  1.00 46.59           O  
-HETATM10416  O   HOH A1217     -38.512   6.102   6.845  0.50 13.85           O  
-HETATM10417  O   HOH A1218     -31.551  21.720 -18.925  1.00 42.35           O  
-HETATM10418  O   HOH A1219     -57.784   4.540 -25.509  1.00 24.12           O  
-HETATM10419  O   HOH A1220     -36.131  11.082  -7.300  1.00 19.46           O  
-HETATM10420  O   HOH A1221     -50.853   3.881  -2.985  1.00 20.60           O  
-HETATM10421  O   HOH A1222     -52.033   3.069  -5.316  1.00 20.41           O  
-HETATM10422  O   HOH A1223     -45.108   0.225  -5.767  1.00 33.53           O  
-HETATM10423  O   HOH A1224     -43.560   0.305 -18.259  1.00 18.03           O  
-HETATM10424  O   HOH A1225     -35.348   4.896 -20.021  1.00 37.56           O  
-HETATM10425  O   HOH A1226     -56.405  -0.623  -1.621  1.00 32.66           O  
-HETATM10426  O   HOH A1227     -56.808  -3.812  -6.451  1.00 29.82           O  
-HETATM10427  O   HOH A1228     -46.234   0.442   1.564  1.00 31.13           O  
-HETATM10428  O   HOH A1229     -48.647   4.011   4.315  1.00 30.92           O  
-HETATM10429  O   HOH A1230     -43.604   9.544   7.656  1.00 35.23           O  
-HETATM10430  O   HOH A1231     -42.128   5.746  -5.886  1.00 16.02           O  
-HETATM10431  O   HOH A1232     -34.572   9.823  -5.725  1.00 26.87           O  
-HETATM10432  O   HOH A1233     -60.001  -6.860 -11.928  1.00 28.68           O  
-HETATM10433  O   HOH A1234     -65.988  -2.383 -16.519  1.00 37.66           O  
-HETATM10434  O   HOH A1235     -61.013   4.302 -28.454  1.00 40.15           O  
-HETATM10435  O   HOH A1236     -35.775  11.345 -11.271  1.00 32.14           O  
-HETATM10436  O   HOH A1237     -55.341   8.433 -27.729  1.00 44.92           O  
-HETATM10437  O   HOH A1238     -37.921   4.362 -20.388  1.00 25.39           O  
-HETATM10438  O   HOH A1239     -43.565   1.410  -7.698  1.00 31.54           O  
-HETATM10439  O   HOH A1240     -51.611   3.861   5.598  1.00 39.36           O  
-HETATM10440  O   HOH A1241     -47.464  12.190   3.167  1.00 17.54           O  
-HETATM10441  O   HOH A1242     -41.971  16.686 -12.880  1.00 20.51           O  
-HETATM10442  O   HOH A1243     -50.174  23.516 -16.038  1.00 23.60           O  
-HETATM10443  O   HOH A1244     -53.631  -2.544 -24.644  1.00 29.30           O  
-HETATM10444  O   HOH A1245     -48.326  23.949  -0.207  1.00 33.52           O  
-HETATM10445  O   HOH A1246     -57.864   3.347  -8.214  1.00 25.73           O  
-HETATM10446  O   HOH A1247     -46.251  -7.431 -11.092  1.00 26.12           O  
-HETATM10447  O   HOH A1248     -46.912  -6.983 -14.500  1.00 25.74           O  
-HETATM10448  O   HOH A1249     -41.429  20.083 -13.557  1.00 21.02           O  
-HETATM10449  O   HOH A1250     -36.470  10.527 -15.109  1.00 20.41           O  
-HETATM10450  O   HOH A1251     -47.529  16.093   9.074  1.00 45.53           O  
-HETATM10451  O   HOH A1252     -37.366  -0.925  -1.943  1.00 29.92           O  
-HETATM10452  O   HOH A1253     -44.622  11.857   7.776  1.00 23.14           O  
-HETATM10453  O   HOH A1254     -42.475  24.405   2.509  1.00 26.62           O  
-HETATM10454  O   HOH A1255     -51.039   0.538  -2.105  1.00 25.22           O  
-HETATM10455  O   HOH A1256     -40.233  24.430  -9.213  1.00 29.22           O  
-HETATM10456  O   HOH A1257     -32.621  -2.849 -11.183  1.00 46.06           O  
-HETATM10457  O   HOH A1258     -40.986  -1.897 -18.615  1.00 31.80           O  
-HETATM10458  O   HOH A1259     -37.275   7.412   4.717  1.00 35.10           O  
-HETATM10459  O   HOH A1260     -40.387   4.075  -1.433  1.00 25.68           O  
-HETATM10460  O   HOH A1261     -35.188  12.673  -9.004  1.00 27.00           O  
-HETATM10461  O   HOH A1262     -50.586  -7.664 -25.172  1.00 42.41           O  
-HETATM10462  O   HOH A1263     -24.929 -16.670  -6.939  1.00 47.42           O  
-HETATM10463  O   HOH A1264     -49.840  12.966 -26.658  1.00 34.15           O  
-HETATM10464  O   HOH A1265     -38.765  21.058 -20.525  1.00 38.68           O  
-HETATM10465  O   HOH A1266     -57.693   2.724 -27.146  1.00 33.56           O  
-HETATM10466  O   HOH A1267     -33.042  -0.108 -12.160  1.00 44.72           O  
-HETATM10467  O   HOH A1268     -64.282  -0.313 -21.577  1.00 32.68           O  
-HETATM10468  O   HOH A1269     -50.689  10.165   6.845  1.00 41.19           O  
-HETATM10469  O   HOH A1270     -55.779   5.318  -1.547  1.00 38.78           O  
-HETATM10470  O   HOH A1271     -36.362   0.816  -3.509  1.00 39.01           O  
-HETATM10471  O   HOH A1272     -40.270   3.152 -10.191  1.00 21.59           O  
-HETATM10472  O   HOH A1273     -35.222  22.483 -16.252  1.00 30.04           O  
-HETATM10473  O   HOH A1274     -31.833   2.057  -2.388  1.00 33.23           O  
-HETATM10474  O   HOH A1275     -40.254   2.044   4.962  1.00 31.02           O  
-HETATM10475  O   HOH A1276     -60.729  10.254  -6.372  1.00 38.49           O  
-HETATM10476  O   HOH A1277     -59.920   1.682 -28.082  1.00 44.75           O  
-HETATM10477  O   HOH A1278     -55.843  -3.164  -0.947  1.00 41.08           O  
-HETATM10478  O   HOH A1279     -57.145   5.225   4.849  1.00 35.13           O  
-HETATM10479  O   HOH A1280     -32.894   2.169  -5.062  1.00 46.10           O  
-HETATM10480  O   HOH A1281     -35.247   3.304   6.519  0.50 21.59           O  
-HETATM10481  O   HOH A1282     -24.042  -8.574  -9.295  1.00 52.80           O  
-HETATM10482  O   HOH A1283     -20.974  -4.520  -8.484  1.00 52.99           O  
-HETATM10483  O   HOH A1284     -64.650   6.903 -22.860  0.50 10.70           O  
-HETATM10484  O   HOH A1285     -56.217   6.149 -26.789  1.00 38.42           O  
-HETATM10485  O   HOH A1286     -64.861  10.242 -21.589  1.00 49.69           O  
-HETATM10486  O   HOH A1287     -32.404   6.656 -28.412  1.00 49.69           O  
-HETATM10487  O   HOH A1288     -62.703   1.797 -14.228  1.00 31.83           O  
-HETATM10488  O   HOH A1289     -60.431   5.642  -9.493  1.00 41.78           O  
-HETATM10489  O   HOH A1290     -60.601   6.087 -11.919  1.00 41.26           O  
-HETATM10490  O   HOH A1291     -61.069  11.605 -13.829  1.00 38.52           O  
-HETATM10491  O   HOH A1292     -34.665   3.132 -11.954  1.00 42.98           O  
-HETATM10492  O   HOH A1293     -34.368  21.396 -18.392  0.50 16.85           O  
-HETATM10493  O   HOH A1294     -49.276  25.456 -22.095  0.50 21.02           O  
-HETATM10494  O   HOH A1295     -63.009  -4.454 -28.513  1.00 36.29           O  
-HETATM10495  O   HOH A1296     -39.922  30.526 -19.150  1.00 36.82           O  
-HETATM10496  O   HOH A1297     -58.856  23.707  -8.687  0.50 38.99           O  
-HETATM10497  O   HOH A1298     -49.208  24.086 -12.282  1.00 47.02           O  
-HETATM10498  O   HOH A1299     -60.059  -0.119   1.673  0.50 14.00           O  
-HETATM10499  O   HOH A1300     -38.669   1.863 -12.282  0.50 18.16           O  
-HETATM10500  O   HOH A1301     -44.085  17.175 -27.117  1.00 46.60           O  
-HETATM10501  O   HOH A1302     -62.495   8.342  -1.726  1.00 34.69           O  
-HETATM10502  O   HOH A1303     -34.874   5.710 -22.043  1.00 42.57           O  
-HETATM10503  O   HOH A1304     -48.207   5.873   6.560  1.00 59.81           O  
-HETATM10504  O   HOH A1305     -29.875  10.576  -1.905  1.00 52.51           O  
-HETATM10505  O   HOH A1306     -56.612  23.571  -4.001  1.00 46.83           O  
-HETATM10506  O   HOH A1307     -53.229  21.737  -7.599  1.00 42.08           O  
-HETATM10507  O   HOH A1308     -57.400  20.610  -5.449  1.00 37.64           O  
-HETATM10508  O   HOH B1201     -74.156  16.913   8.753  1.00 43.19           O  
-HETATM10509  O   HOH B1202     -75.111  16.083   5.297  1.00 27.68           O  
-HETATM10510  O   HOH B1203     -77.615  19.553  14.002  1.00 30.17           O  
-HETATM10511  O   HOH B1204     -72.168   5.309  -9.096  1.00 31.47           O  
-HETATM10512  O   HOH B1205     -76.470  -0.826  -0.354  1.00 22.57           O  
-HETATM10513  O   HOH B1206     -78.073   0.472  -2.258  1.00 21.18           O  
-HETATM10514  O   HOH B1207     -70.333  -6.732  -1.377  1.00 22.13           O  
-HETATM10515  O   HOH B1208     -66.896  -0.072   0.368  1.00 40.98           O  
-HETATM10516  O   HOH B1209     -70.703  -0.771   2.443  1.00 21.49           O  
-HETATM10517  O   HOH B1210     -94.982   1.504   1.555  1.00 40.20           O  
-HETATM10518  O   HOH B1211     -66.094 -10.802   2.791  1.00 40.28           O  
-HETATM10519  O   HOH B1212     -65.425  -2.953   8.006  1.00 35.27           O  
-HETATM10520  O   HOH B1213     -83.359   9.058  -5.778  1.00 21.91           O  
-HETATM10521  O   HOH B1214     -77.195  -2.445  -4.270  1.00 31.53           O  
-HETATM10522  O   HOH B1215     -90.111  10.038  12.298  1.00 27.46           O  
-HETATM10523  O   HOH B1216     -80.548   2.086  -9.208  1.00 33.15           O  
-HETATM10524  O   HOH B1217     -92.936  -0.429  11.083  1.00 29.12           O  
-HETATM10525  O   HOH B1218     -88.887   7.118  10.996  1.00 28.98           O  
-HETATM10526  O   HOH B1219     -83.708  -9.551  10.790  1.00 23.22           O  
-HETATM10527  O   HOH B1220     -86.937  19.279   1.214  0.50 28.09           O  
-HETATM10528  O   HOH B1221     -86.926  -0.881   0.792  1.00 27.15           O  
-HETATM10529  O   HOH B1222     -69.735   7.255   3.421  1.00 26.97           O  
-HETATM10530  O   HOH B1223     -61.305  -6.587   8.868  1.00 47.11           O  
-HETATM10531  O   HOH B1224     -93.531   2.351   3.560  1.00 26.95           O  
-HETATM10532  O   HOH B1225     -82.500  -5.165  -1.072  1.00 25.86           O  
-HETATM10533  O   HOH B1226     -85.851 -12.331  10.521  1.00 41.41           O  
-HETATM10534  O   HOH B1227     -81.058 -16.396   8.171  1.00 60.84           O  
-HETATM10535  O   HOH B1228     -67.921   0.112  -7.638  1.00 36.83           O  
-HETATM10536  O   HOH B1229     -72.947 -12.049  15.939  1.00 36.57           O  
-HETATM10537  O   HOH B1230     -71.168  13.936  -8.285  1.00 32.74           O  
-HETATM10538  O   HOH B1231     -73.676   3.260  -3.290  1.00 33.06           O  
-HETATM10539  O   HOH B1232     -88.225  -1.506  -4.205  1.00 37.61           O  
-HETATM10540  O   HOH B1233     -79.283 -14.267   4.877  1.00 41.82           O  
-HETATM10541  O   HOH B1234     -78.901  16.506 -10.324  1.00 45.52           O  
-HETATM10542  O   HOH B1235     -63.411  -8.850  11.809  1.00 39.92           O  
-HETATM10543  O   HOH B1236     -69.992  -4.526  18.988  1.00 37.72           O  
-HETATM10544  O   HOH B1237     -66.437  20.117  -4.516  1.00 51.33           O  
-HETATM10545  O   HOH B1238     -81.932  -2.614  -7.674  1.00 33.16           O  
-HETATM10546  O   HOH B1239     -89.570  -7.316  14.039  1.00 40.45           O  
-HETATM10547  O   HOH B1240     -77.324   3.507 -10.278  1.00 45.04           O  
-HETATM10548  O   HOH B1241     -68.399   5.393   9.879  1.00 46.91           O  
-HETATM10549  O   HOH B1242     -69.797  -5.966  -3.604  1.00 34.16           O  
-HETATM10550  O   HOH B1243     -95.277   2.844   5.247  1.00 52.59           O  
-HETATM10551  O   HOH B1244     -60.811   4.456  -7.152  1.00 28.00           O  
-HETATM10552  O   HOH B1245     -87.388 -14.108   8.968  1.00 55.78           O  
-HETATM10553  O   HOH B1246     -92.079  -7.259  14.202  1.00 43.07           O  
-HETATM10554  O   HOH B1247     -63.097   9.278 -10.893  1.00 52.04           O  
-HETATM10555  O   HOH B1248     -68.759  10.334   5.798  1.00 48.52           O  
-HETATM10556  O   HOH B1249     -67.791   7.277  -1.589  1.00 36.50           O  
-HETATM10557  O   HOH B1250     -72.864  18.980  -0.446  1.00 52.23           O  
-HETATM10558  O   HOH B1251     -68.994   1.952   4.613  0.50 14.81           O  
-HETATM10559  O   HOH B1252     -85.625  -4.882   2.732  1.00 36.79           O  
-HETATM10560  O   HOH B1253     -90.719  19.311  -1.051  1.00 38.85           O  
-HETATM10561  O   HOH B1254     -96.970  10.121  15.407  1.00 41.15           O  
-HETATM10562  O   HOH B1255     -95.849  -2.587   5.603  1.00 48.97           O  
-HETATM10563  O   HOH C1201     -71.879  13.885 -42.643  1.00 44.82           O  
-HETATM10564  O   HOH C1202     -86.539  35.710  -8.048  1.00 37.51           O  
-HETATM10565  O   HOH C1203     -85.503  32.233  -9.225  1.00 29.92           O  
-HETATM10566  O   HOH C1204     -72.221  32.304 -55.047  1.00 39.04           O  
-HETATM10567  O   HOH C1205     -82.986  40.294  -4.783  1.00 32.93           O  
-HETATM10568  O   HOH C1206     -80.429  41.069  -2.747  0.50 28.45           O  
-HETATM10569  O   HOH C1207     -85.201  30.847  -6.614  1.00 40.08           O  
-HETATM10570  O   HOH C1208     -73.717  32.543 -53.103  1.00 35.75           O  
-HETATM10571  O   HOH C1209     -75.138  34.141  -7.016  1.00 33.43           O  
-HETATM10572  O   HOH C1210     -73.749  22.675  -2.792  1.00 45.64           O  
-HETATM10573  O   HOH C1211     -79.118  50.376  -9.348  1.00 41.35           O  
-HETATM10574  O   HOH C1212     -63.347  22.655 -21.114  1.00 42.21           O  
-HETATM10575  O   HOH C1213     -82.232  26.587 -25.567  1.00 19.51           O  
-HETATM10576  O   HOH C1214     -69.899  24.860  -6.329  1.00 27.56           O  
-HETATM10577  O   HOH C1215     -65.990  35.727 -22.898  1.00 35.32           O  
-HETATM10578  O   HOH C1216     -91.119  33.230 -23.454  1.00 43.18           O  
-HETATM10579  O   HOH C1217     -88.640  24.571 -28.692  1.00 46.44           O  
-HETATM10580  O   HOH C1218     -74.540  17.293 -17.574  1.00 39.33           O  
-HETATM10581  O   HOH C1219     -89.290  31.815 -26.049  1.00 20.52           O  
-HETATM10582  O   HOH C1220     -83.545  28.642 -26.617  1.00 21.64           O  
-HETATM10583  O   HOH C1221     -83.028  24.947 -28.696  1.00 23.41           O  
-HETATM10584  O   HOH C1222     -69.747  39.659 -14.021  1.00 22.56           O  
-HETATM10585  O   HOH C1223     -94.106  37.526 -27.379  1.00 36.81           O  
-HETATM10586  O   HOH C1224     -71.810  33.595 -29.708  1.00 25.23           O  
-HETATM10587  O   HOH C1225     -71.720  24.944 -27.500  1.00 26.60           O  
-HETATM10588  O   HOH C1226     -78.142  21.410 -29.072  1.00 26.51           O  
-HETATM10589  O   HOH C1227     -66.715  39.355 -24.180  1.00 21.28           O  
-HETATM10590  O   HOH C1228     -79.733  19.388 -24.730  1.00 27.20           O  
-HETATM10591  O   HOH C1229     -77.147  21.963 -17.185  1.00 16.01           O  
-HETATM10592  O   HOH C1230     -68.464  26.173 -30.869  1.00 23.68           O  
-HETATM10593  O   HOH C1231     -92.450  26.511 -18.655  1.00 39.84           O  
-HETATM10594  O   HOH C1232     -52.042  24.579 -30.102  1.00 39.04           O  
-HETATM10595  O   HOH C1233     -86.633  25.294 -22.964  1.00 27.74           O  
-HETATM10596  O   HOH C1234     -59.994  25.556 -50.337  1.00 36.99           O  
-HETATM10597  O   HOH C1235     -65.581  15.680 -30.982  1.00 33.40           O  
-HETATM10598  O   HOH C1236     -90.531  31.423 -18.116  1.00 38.06           O  
-HETATM10599  O   HOH C1237     -76.826  19.256 -16.974  0.50 24.25           O  
-HETATM10600  O   HOH C1238     -92.759  29.141 -18.353  1.00 50.03           O  
-HETATM10601  O   HOH C1239     -64.227  24.569 -30.591  1.00 33.64           O  
-HETATM10602  O   HOH C1240     -64.983  19.978 -21.188  1.00 49.82           O  
-HETATM10603  O   HOH C1241     -65.859  26.999 -30.753  1.00 32.96           O  
-HETATM10604  O   HOH C1242     -71.457  22.894 -47.087  1.00 38.92           O  
-HETATM10605  O   HOH C1243     -73.524  40.529 -36.205  1.00 26.34           O  
-HETATM10606  O   HOH C1244     -78.770  37.375 -42.630  1.00 33.21           O  
-HETATM10607  O   HOH C1245     -80.231  35.722 -38.962  1.00 26.72           O  
-HETATM10608  O   HOH C1246     -79.748  32.338 -38.855  1.00 27.20           O  
-HETATM10609  O   HOH C1247     -56.748  12.402 -35.748  1.00 38.07           O  
-HETATM10610  O   HOH C1248     -93.342  33.224 -36.231  1.00 42.51           O  
-HETATM10611  O   HOH C1249     -89.524  28.697 -32.645  1.00 30.45           O  
-HETATM10612  O   HOH C1250     -96.276  42.274 -32.886  1.00 45.61           O  
-HETATM10613  O   HOH C1251     -88.990  48.782 -27.549  1.00 31.56           O  
-HETATM10614  O   HOH C1252     -79.788  51.761 -21.347  1.00 42.89           O  
-HETATM10615  O   HOH C1253     -67.001  46.683 -14.831  1.00 34.46           O  
-HETATM10616  O   HOH C1254     -63.250  42.385 -13.321  1.00 33.02           O  
-HETATM10617  O   HOH C1255     -73.304  51.857 -22.985  1.00 48.37           O  
-HETATM10618  O   HOH C1256     -73.222  29.413 -26.053  1.00 18.81           O  
-HETATM10619  O   HOH C1257     -75.881  40.717 -33.481  1.00 22.43           O  
-HETATM10620  O   HOH C1258     -67.691  19.447 -23.463  1.00 35.24           O  
-HETATM10621  O   HOH C1259     -70.967  38.506 -17.056  1.00 19.79           O  
-HETATM10622  O   HOH C1260     -76.307  27.732  -6.587  1.00 33.94           O  
-HETATM10623  O   HOH C1261     -62.704  40.822  -7.064  1.00 43.12           O  
-HETATM10624  O   HOH C1262     -77.519  42.991  -9.297  1.00 28.58           O  
-HETATM10625  O   HOH C1263     -61.409  33.506  -3.967  1.00 53.63           O  
-HETATM10626  O   HOH C1264     -73.951  27.635 -27.940  1.00 35.75           O  
-HETATM10627  O   HOH C1265     -96.525  44.286 -31.126  1.00 44.75           O  
-HETATM10628  O   HOH C1266     -64.615  38.114 -22.288  1.00 38.23           O  
-HETATM10629  O   HOH C1267     -66.382  34.988 -31.158  1.00 41.98           O  
-HETATM10630  O   HOH C1268     -70.594  35.256 -31.484  1.00 26.57           O  
-HETATM10631  O   HOH C1269     -59.675  24.881 -24.787  1.00 57.58           O  
-HETATM10632  O   HOH C1270     -61.519  15.964 -30.007  1.00 41.74           O  
-HETATM10633  O   HOH C1271     -74.237  30.003 -34.574  1.00 33.89           O  
-HETATM10634  O   HOH C1272     -97.974  39.949 -33.573  1.00 47.54           O  
-HETATM10635  O   HOH C1273     -83.892  52.511 -16.953  1.00 46.40           O  
-HETATM10636  O   HOH C1274     -69.595  43.424 -30.951  1.00 28.07           O  
-HETATM10637  O   HOH C1275     -62.214  26.172  -9.778  1.00 41.21           O  
-HETATM10638  O   HOH C1276     -78.515  19.447 -27.253  1.00 40.03           O  
-HETATM10639  O   HOH C1277     -59.466  26.094 -22.190  1.00 56.32           O  
-HETATM10640  O   HOH C1278     -99.659  21.939 -23.086  1.00 42.42           O  
-HETATM10641  O   HOH C1279     -67.164  43.887 -30.860  1.00 46.23           O  
-HETATM10642  O   HOH C1280     -58.173  29.052 -39.183  1.00 37.51           O  
-HETATM10643  O   HOH C1281     -78.905  22.561 -38.446  1.00 44.01           O  
-HETATM10644  O   HOH C1282     -81.523  22.251 -39.218  1.00 36.46           O  
-HETATM10645  O   HOH C1283     -77.884  23.924 -40.950  1.00 41.01           O  
-HETATM10646  O   HOH C1284     -90.207  26.508 -32.187  1.00 37.79           O  
-HETATM10647  O   HOH C1285     -57.693  26.571 -26.324  0.50 37.38           O  
-HETATM10648  O   HOH C1286     -77.890  18.358 -14.609  1.00 48.73           O  
-HETATM10649  O   HOH C1287     -49.688  10.636 -28.112  1.00 36.83           O  
-HETATM10650  O   HOH C1288     -78.441  39.220 -40.704  1.00 38.39           O  
-HETATM10651  O   HOH C1289     -78.694  34.791 -41.729  1.00 47.17           O  
-HETATM10652  O   HOH C1290     -79.173  23.479 -35.872  1.00 43.94           O  
-HETATM10653  O   HOH C1291     -77.480  20.045 -38.289  1.00 41.43           O  
-HETATM10654  O   HOH C1292     -76.393  40.794 -40.539  1.00 39.39           O  
-HETATM10655  O   HOH C1293     -78.727  42.530 -41.474  1.00 39.16           O  
-HETATM10656  O   HOH C1294     -83.087  22.146 -31.221  1.00 44.32           O  
-HETATM10657  O   HOH C1295     -74.513  31.665 -30.325  1.00 38.94           O  
-HETATM10658  O   HOH C1296     -77.389  28.442 -30.649  1.00 22.83           O  
-HETATM10659  O   HOH C1297     -65.016  38.459 -26.913  1.00 56.99           O  
-HETATM10660  O   HOH C1298     -65.084  31.624 -31.378  1.00 51.00           O  
-HETATM10661  O   HOH C1299     -72.389  40.288 -42.363  1.00 42.02           O  
-HETATM10662  O   HOH C1300     -74.267  25.568 -32.352  1.00 48.77           O  
-HETATM10663  O   HOH D1201    -133.263  17.367  -3.107  1.00 35.99           O  
-HETATM10664  O   HOH D1202     -99.491  31.381 -12.230  1.00 37.37           O  
-HETATM10665  O   HOH D1203    -125.265  34.699  -8.220  1.00 43.91           O  
-HETATM10666  O   HOH D1204    -129.058  35.683 -19.019  1.00 44.93           O  
-HETATM10667  O   HOH D1205    -121.218  37.008 -10.264  1.00 29.98           O  
-HETATM10668  O   HOH D1206     -99.813  29.365  -5.212  0.50 28.00           O  
-HETATM10669  O   HOH D1207    -118.734  30.981  -2.862  1.00 31.00           O  
-HETATM10670  O   HOH D1208    -132.949  14.644  -4.297  1.00 51.91           O  
-HETATM10671  O   HOH D1209    -124.317  34.360  -3.563  1.00 44.89           O  
-HETATM10672  O   HOH D1210    -108.382  24.076 -24.222  1.00 33.99           O  
-HETATM10673  O   HOH D1211    -109.451  26.367 -23.237  1.00 26.23           O  
-HETATM10674  O   HOH D1212    -124.549  22.054 -17.175  1.00 28.26           O  
-HETATM10675  O   HOH D1213    -124.570  14.473 -17.914  1.00 33.18           O  
-HETATM10676  O   HOH D1214    -113.045  32.040 -14.906  1.00 19.99           O  
-HETATM10677  O   HOH D1215    -102.321  20.939 -23.907  1.00 37.09           O  
-HETATM10678  O   HOH D1216    -119.399  16.073 -11.638  1.00 27.11           O  
-HETATM10679  O   HOH D1217     -95.341  27.870 -17.059  1.00 37.05           O  
-HETATM10680  O   HOH D1218     -98.072  27.080 -17.955  1.00 32.27           O  
-HETATM10681  O   HOH D1219     -92.901  30.710 -20.691  1.00 33.43           O  
-HETATM10682  O   HOH D1220    -122.662  34.095 -19.732  1.00 42.84           O  
-HETATM10683  O   HOH D1221    -115.140  12.464 -36.064  1.00 57.60           O  
-HETATM10684  O   HOH D1222    -113.955  18.928 -35.557  1.00 41.57           O  
-HETATM10685  O   HOH D1223    -128.965  11.005 -13.738  1.00 38.00           O  
-HETATM10686  O   HOH D1224    -104.506  27.649 -21.480  1.00 37.72           O  
-HETATM10687  O   HOH D1225    -103.802  23.049  -6.692  1.00 47.46           O  
-HETATM10688  O   HOH D1226    -116.999  11.322 -28.244  1.00 41.74           O  
-HETATM10689  O   HOH D1227    -109.085  27.595 -26.728  1.00 34.80           O  
-HETATM10690  O   HOH D1228    -113.801  31.288 -26.731  1.00 32.69           O  
-HETATM10691  O   HOH D1229    -122.448  27.966 -28.710  1.00 37.31           O  
-HETATM10692  O   HOH D1230    -126.046  24.142 -18.231  1.00 39.52           O  
-HETATM10693  O   HOH D1231    -126.064  20.392 -15.477  1.00 36.43           O  
-HETATM10694  O   HOH D1232    -119.977  15.295  -8.343  1.00 32.26           O  
-HETATM10695  O   HOH D1233    -122.596   9.481 -24.586  1.00 38.37           O  
-HETATM10696  O   HOH D1234    -107.865  21.007  -6.650  1.00 51.12           O  
-HETATM10697  O   HOH D1235    -119.726  11.419 -31.072  1.00 41.20           O  
-HETATM10698  O   HOH D1236     -91.966  31.078 -24.021  1.00 34.88           O  
-HETATM10699  O   HOH D1237    -120.212  19.376 -25.068  1.00 37.34           O  
-HETATM10700  O   HOH D1238    -119.511  27.538 -31.486  1.00 47.72           O  
-HETATM10701  O   HOH D1239    -130.148  28.352 -17.675  0.50 25.72           O  
-HETATM10702  O   HOH D1240    -120.079  12.737 -33.511  1.00 43.79           O  
-HETATM10703  O   HOH D1241    -113.176  28.178  -3.159  1.00 42.67           O  
-HETATM10704  O   HOH D1242    -118.442  23.743 -22.016  1.00 27.33           O  
-HETATM10705  O   HOH D1243    -118.646  20.765 -26.347  1.00 41.02           O  
-HETATM10706  O   HOH D1244     -99.916  17.853 -34.440  1.00 41.17           O  
-HETATM10707  O   HOH D1245    -102.986  33.899 -21.316  1.00 39.03           O  
-HETATM10708  O   HOH D1246    -116.629  21.900 -26.426  1.00 40.84           O  
-HETATM10709  O   HOH D1247    -125.161   9.753 -24.250  1.00 52.71           O  
-HETATM10710  O   HOH D1248    -103.784  24.186  -4.118  1.00 48.78           O  
-HETATM10711  O   HOH D1249    -115.152  23.993 -27.218  1.00 34.18           O  
-HETATM10712  O   HOH D1250    -119.803  26.926 -28.289  1.00 39.51           O  
-HETATM10713  O   HOH D1251    -117.644  26.203 -27.991  1.00 54.07           O  
-HETATM10714  O   HOH D1252    -111.708  33.492 -23.110  1.00 30.87           O  
-HETATM10715  O   HOH D1253    -112.714  33.431 -25.369  1.00 40.48           O  
-CONECT 1323 3868                                                                
-CONECT 3868 1323                                                                
-CONECT 6477 8931                                                                
-CONECT 8931 6477                                                                
-CONECT1019510196101971019810199                                                 
-CONECT1019610195                                                                
-CONECT1019710195                                                                
-CONECT1019810195                                                                
-CONECT1019910195                                                                
-CONECT1020010201102021020310204                                                 
-CONECT1020110200                                                                
-CONECT1020210200                                                                
-CONECT1020310200                                                                
-CONECT1020410200                                                                
-CONECT1020510206102071020810209                                                 
-CONECT1020610205                                                                
-CONECT1020710205                                                                
-CONECT1020810205                                                                
-CONECT1020910205                                                                
-CONECT1021010211102121021310214                                                 
-CONECT1021110210                                                                
-CONECT1021210210                                                                
-CONECT1021310210                                                                
-CONECT1021410210                                                                
-CONECT102151023610242                                                           
-CONECT102161021910220                                                           
-CONECT10217102401024110242                                                      
-CONECT10218102191022510236                                                      
-CONECT10219102161021810230                                                      
-CONECT10220102161022110237                                                      
-CONECT102211022010238                                                           
-CONECT102221023810240                                                           
-CONECT102231022710228                                                           
-CONECT102241022710229                                                           
-CONECT10225102181023110234                                                      
-CONECT1022610227                                                                
-CONECT10227102231022410226                                                      
-CONECT102281022310230                                                           
-CONECT102291022410230                                                           
-CONECT10230102191022810229                                                      
-CONECT102311022510232                                                           
-CONECT102321023110233                                                           
-CONECT102331023210234                                                           
-CONECT10234102251023310235                                                      
-CONECT1023510234                                                                
-CONECT10236102151021810237                                                      
-CONECT10237102201023610240                                                      
-CONECT10238102211022210239                                                      
-CONECT1023910238                                                                
-CONECT10240102171022210237                                                      
-CONECT1024110217                                                                
-CONECT102421021510217                                                           
-CONECT102431024410245                                                           
-CONECT1024410243                                                                
-CONECT10245102431024610247                                                      
-CONECT1024610245                                                                
-CONECT102471024510248                                                           
-CONECT1024810247                                                                
-CONECT102491025010251                                                           
-CONECT1025010249                                                                
-CONECT10251102491025210253                                                      
-CONECT1025210251                                                                
-CONECT102531025110254                                                           
-CONECT1025410253                                                                
-CONECT1025510256102571025810259                                                 
-CONECT1025610255                                                                
-CONECT1025710255                                                                
-CONECT1025810255                                                                
-CONECT1025910255                                                                
-CONECT1026010261102621026310264                                                 
-CONECT1026110260                                                                
-CONECT1026210260                                                                
-CONECT1026310260                                                                
-CONECT1026410260                                                                
-CONECT1026510266102671026810269                                                 
-CONECT1026610265                                                                
-CONECT1026710265                                                                
-CONECT1026810265                                                                
-CONECT1026910265                                                                
-CONECT1027010271102721027310274                                                 
-CONECT1027110270                                                                
-CONECT1027210270                                                                
-CONECT1027310270                                                                
-CONECT1027410270                                                                
-CONECT102751029610302                                                           
-CONECT102761027910280                                                           
-CONECT10277103001030110302                                                      
-CONECT10278102791028510296                                                      
-CONECT10279102761027810290                                                      
-CONECT10280102761028110297                                                      
-CONECT102811028010298                                                           
-CONECT102821029810300                                                           
-CONECT102831028710288                                                           
-CONECT102841028710289                                                           
-CONECT10285102781029110294                                                      
-CONECT1028610287                                                                
-CONECT10287102831028410286                                                      
-CONECT102881028310290                                                           
-CONECT102891028410290                                                           
-CONECT10290102791028810289                                                      
-CONECT102911028510292                                                           
-CONECT102921029110293                                                           
-CONECT102931029210294                                                           
-CONECT10294102851029310295                                                      
-CONECT1029510294                                                                
-CONECT10296102751027810297                                                      
-CONECT10297102801029610300                                                      
-CONECT10298102811028210299                                                      
-CONECT1029910298                                                                
-CONECT10300102771028210297                                                      
-CONECT1030110277                                                                
-CONECT103021027510277                                                           
-CONECT1030310304103051030610307                                                 
-CONECT1030410303                                                                
-CONECT1030510303                                                                
-CONECT1030610303                                                                
-CONECT1030710303                                                                
-CONECT1030810309103101031110312                                                 
-CONECT1030910308                                                                
-CONECT1031010308                                                                
-CONECT1031110308                                                                
-CONECT1031210308                                                                
-CONECT1031310314103151031610317                                                 
-CONECT1031410313                                                                
-CONECT1031510313                                                                
-CONECT1031610313                                                                
-CONECT1031710313                                                                
-CONECT1031810319103201032110322                                                 
-CONECT1031910318                                                                
-CONECT1032010318                                                                
-CONECT1032110318                                                                
-CONECT1032210318                                                                
-CONECT103231034410350                                                           
-CONECT103241032710328                                                           
-CONECT10325103481034910350                                                      
-CONECT10326103271033310344                                                      
-CONECT10327103241032610338                                                      
-CONECT10328103241032910345                                                      
-CONECT103291032810346                                                           
-CONECT103301034610348                                                           
-CONECT103311033510336                                                           
-CONECT103321033510337                                                           
-CONECT10333103261033910342                                                      
-CONECT1033410335                                                                
-CONECT10335103311033210334                                                      
-CONECT103361033110338                                                           
-CONECT103371033210338                                                           
-CONECT10338103271033610337                                                      
-CONECT103391033310340                                                           
-CONECT103401033910341                                                           
-CONECT103411034010342                                                           
-CONECT10342103331034110343                                                      
-CONECT1034310342                                                                
-CONECT10344103231032610345                                                      
-CONECT10345103281034410348                                                      
-CONECT10346103291033010347                                                      
-CONECT1034710346                                                                
-CONECT10348103251033010345                                                      
-CONECT1034910325                                                                
-CONECT103501032310325                                                           
-CONECT103511035210353                                                           
-CONECT1035210351                                                                
-CONECT10353103511035410355                                                      
-CONECT1035410353                                                                
-CONECT103551035310356                                                           
-CONECT1035610355                                                                
-CONECT1035710358103591036010361                                                 
-CONECT1035810357                                                                
-CONECT1035910357                                                                
-CONECT1036010357                                                                
-CONECT1036110357                                                                
-CONECT1036210363103641036510366                                                 
-CONECT1036310362                                                                
-CONECT1036410362                                                                
-CONECT1036510362                                                                
-CONECT1036610362                                                                
-CONECT1036710368103691037010371                                                 
-CONECT1036810367                                                                
-CONECT1036910367                                                                
-CONECT1037010367                                                                
-CONECT1037110367                                                                
-CONECT103721039310399                                                           
-CONECT103731037610377                                                           
-CONECT10374103971039810399                                                      
-CONECT10375103761038210393                                                      
-CONECT10376103731037510387                                                      
-CONECT10377103731037810394                                                      
-CONECT103781037710395                                                           
-CONECT103791039510397                                                           
-CONECT103801038410385                                                           
-CONECT103811038410386                                                           
-CONECT10382103751038810391                                                      
-CONECT1038310384                                                                
-CONECT10384103801038110383                                                      
-CONECT103851038010387                                                           
-CONECT103861038110387                                                           
-CONECT10387103761038510386                                                      
-CONECT103881038210389                                                           
-CONECT103891038810390                                                           
-CONECT103901038910391                                                           
-CONECT10391103821039010392                                                      
-CONECT1039210391                                                                
-CONECT10393103721037510394                                                      
-CONECT10394103771039310397                                                      
-CONECT10395103781037910396                                                      
-CONECT1039610395                                                                
-CONECT10397103741037910394                                                      
-CONECT1039810374                                                                
-CONECT103991037210374                                                           
-MASTER      753    0   22   63   57    0   44    610694    4  209  116          
-END                                                                             
diff --git a/plip/test/pdb/4qnb.pdb b/plip/test/pdb/4qnb.pdb
deleted file mode 100644
index 54c5363..0000000
--- a/plip/test/pdb/4qnb.pdb
+++ /dev/null
@@ -1,4070 +0,0 @@
-HEADER    VIRAL PROTEIN/INHIBITOR                 17-JUN-14   4QNB              
-TITLE     DISULFIDE STABILIZED HIV-1 CA HEXAMER IN COMPLEX WITH PHENYL-L-       
-TITLE    2 PHENYLALANINAMIDE INHIBITOR                                          
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CAPSID PROTEIN P24;                                        
-COMPND   3 CHAIN: A;                                                            
-COMPND   4 ENGINEERED: YES;                                                     
-COMPND   5 MUTATION: YES                                                        
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (NEW YORK-5 
-SOURCE   3 ISOLATE);                                                            
-SOURCE   4 ORGANISM_COMMON: HIV-1;                                              
-SOURCE   5 ORGANISM_TAXID: 11698;                                               
-SOURCE   6 GENE: GAG-POL;                                                       
-SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
-SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
-SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
-KEYWDS    CAPSID PROTEIN, DISULFIDE CROSSLINK, VIRAL PROTEIN, VIRAL PROTEIN-    
-KEYWDS   2 INHIBITOR COMPLEX                                                    
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    O.PORNILLOS                                                           
-REVDAT   1   31-DEC-14 4QNB    0                                                
-JRNL        AUTH   A.BHATTACHARYA,S.L.ALAM,T.FRICKE,K.ZADROZNY,J.SEDZICKI,      
-JRNL        AUTH 2 A.B.TAYLOR,B.DEMELER,O.PORNILLOS,B.K.GANSER-PORNILLOS,       
-JRNL        AUTH 3 F.DIAZ-GRIFFERO,D.N.IVANOV,M.YEAGER                          
-JRNL        TITL   STRUCTURAL BASIS OF HIV-1 CAPSID RECOGNITION BY PF74 AND     
-JRNL        TITL 2 CPSF6.                                                       
-JRNL        REF    PROC.NATL.ACAD.SCI.USA                     2014              
-JRNL        REFN                   ESSN 1091-6490                               
-JRNL        PMID   25518861                                                     
-JRNL        DOI    10.1073/PNAS.1419945112                                      
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : ML                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.64                          
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
-REMARK   3   NUMBER OF REFLECTIONS             : 18417                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
-REMARK   3   R VALUE            (WORKING SET) : 0.220                           
-REMARK   3   FREE R VALUE                     : 0.271                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 897                             
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 26.6444 -  3.6252    1.00     2983   154  0.2212 0.2564        
-REMARK   3     2  3.6252 -  2.8785    1.00     2922   152  0.2313 0.2818        
-REMARK   3     3  2.8785 -  2.5150    1.00     2933   130  0.2210 0.2823        
-REMARK   3     4  2.5150 -  2.2851    1.00     2885   160  0.2140 0.2942        
-REMARK   3     5  2.2851 -  2.1214    1.00     2922   140  0.2019 0.2633        
-REMARK   3     6  2.1214 -  1.9964    1.00     2875   161  0.2074 0.2649        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.11                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
-REMARK   3   K_SOL              : NULL                                          
-REMARK   3   B_SOL              : NULL                                          
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.530           
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : 28.00                          
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.008           1734                                  
-REMARK   3   ANGLE     :  0.997           2356                                  
-REMARK   3   CHIRALITY :  0.040            262                                  
-REMARK   3   PLANARITY :  0.005            306                                  
-REMARK   3   DIHEDRAL  : 14.198            647                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
-REMARK   3   TLS GROUP : 1                                                      
-REMARK   3    SELECTION: all                                                    
-REMARK   3    ORIGIN FOR THE GROUP (A):  24.8716  10.3507  -0.7647              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1573 T22:   0.1716                                     
-REMARK   3      T33:   0.1686 T12:  -0.0086                                     
-REMARK   3      T13:   0.0037 T23:  -0.0232                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.7925 L22:   1.0844                                     
-REMARK   3      L33:   1.4389 L12:  -0.3571                                     
-REMARK   3      L13:   0.5725 L23:  -0.6160                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0229 S12:   0.1284 S13:   0.0101                       
-REMARK   3      S21:  -0.0656 S22:  -0.0921 S23:  -0.0280                       
-REMARK   3      S31:  -0.0118 S32:   0.1688 S33:   0.0598                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 4QNB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-14.                  
-REMARK 100 THE RCSB ID CODE IS RCSB086270.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 11-JAN-11                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 8                                  
-REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : APS                                
-REMARK 200  BEAMLINE                       : 22-BM                              
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
-REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18424                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.996                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY                : 11.100                             
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : 0.08700                            
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 43.9000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: MOLREP                                                
-REMARK 200 STARTING MODEL: 3H47                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 54.08                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8,000, 2% TACSIMATE, 100 MM      
-REMARK 280  TRIS, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K               
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -Y,X-Y,Z                                                
-REMARK 290       3555   -X+Y,-X,Z                                               
-REMARK 290       4555   -X,-Y,Z                                                 
-REMARK 290       5555   Y,-X+Y,Z                                                
-REMARK 290       6555   X-Y,X,Z                                                 
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 14990 ANGSTROM**2                         
-REMARK 350 SURFACE AREA OF THE COMPLEX: 61050 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
-REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
-REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
-REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
-REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
-REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
-REMARK 350   BIOMT1   5  0.500000  0.866025  0.000000        0.00000            
-REMARK 350   BIOMT2   5 -0.866025  0.500000  0.000000        0.00000            
-REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
-REMARK 350   BIOMT1   6  0.500000 -0.866025  0.000000        0.00000            
-REMARK 350   BIOMT2   6  0.866025  0.500000  0.000000        0.00000            
-REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     LYS A   182                                                      
-REMARK 465     ASN A   183                                                      
-REMARK 465     ALA A   184                                                      
-REMARK 465     ALA A   185                                                      
-REMARK 465     GLY A   220                                                      
-REMARK 465     VAL A   221                                                      
-REMARK 465     GLY A   222                                                      
-REMARK 465     GLY A   223                                                      
-REMARK 465     PRO A   224                                                      
-REMARK 465     GLY A   225                                                      
-REMARK 465     HIS A   226                                                      
-REMARK 465     LYS A   227                                                      
-REMARK 465     ALA A   228                                                      
-REMARK 465     ARG A   229                                                      
-REMARK 465     VAL A   230                                                      
-REMARK 465     LEU A   231                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     GLN A   4    CG   CD   OE1  NE2                                  
-REMARK 470     LEU A   6    CG   CD1  CD2                                       
-REMARK 470     GLN A   7    CG   CD   OE1  NE2                                  
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   NH1  ARG A   100     O    HOH A   450              2.16            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASN A   5     -157.95    -97.04                                   
-REMARK 500    ALA A  31     -132.83     55.82                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1B0 A 301                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 3H47   RELATED DB: PDB                                   
-DBREF  4QNB A    1   231  UNP    P12497   POL_HV1N5      133    363             
-SEQADV 4QNB CYS A   14  UNP  P12497    ALA   146 ENGINEERED MUTATION            
-SEQADV 4QNB CYS A   45  UNP  P12497    GLU   177 ENGINEERED MUTATION            
-SEQADV 4QNB ALA A  184  UNP  P12497    TRP   316 ENGINEERED MUTATION            
-SEQADV 4QNB ALA A  185  UNP  P12497    MET   317 ENGINEERED MUTATION            
-SEQRES   1 A  231  PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN          
-SEQRES   2 A  231  CYS ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL          
-SEQRES   3 A  231  VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET          
-SEQRES   4 A  231  PHE SER ALA LEU SER CYS GLY ALA THR PRO GLN ASP LEU          
-SEQRES   5 A  231  ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA          
-SEQRES   6 A  231  MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA          
-SEQRES   7 A  231  GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE          
-SEQRES   8 A  231  ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE          
-SEQRES   9 A  231  ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP          
-SEQRES  10 A  231  MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR          
-SEQRES  11 A  231  LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG          
-SEQRES  12 A  231  MET TYR SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY          
-SEQRES  13 A  231  PRO LYS GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR          
-SEQRES  14 A  231  LYS THR LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS          
-SEQRES  15 A  231  ASN ALA ALA THR GLU THR LEU LEU VAL GLN ASN ALA ASN          
-SEQRES  16 A  231  PRO ASP CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY          
-SEQRES  17 A  231  ALA THR LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL          
-SEQRES  18 A  231  GLY GLY PRO GLY HIS LYS ALA ARG VAL LEU                      
-HET    1B0  A 301      59                                                       
-HETNAM     1B0 N-METHYL-NALPHA-[(2-METHYL-1H-INDOL-3-YL)ACETYL]-N-              
-HETNAM   2 1B0  PHENYL-L-PHENYLALANINAMIDE                                      
-FORMUL   2  1B0    C27 H27 N3 O2                                                
-FORMUL   3  HOH   *100(H2 O)                                                    
-HELIX    1   1 SER A   16  ALA A   31  1                                  16    
-HELIX    2   2 GLU A   35  SER A   44  1                                  10    
-HELIX    3   3 THR A   48  THR A   58  1                                  11    
-HELIX    4   4 HIS A   62  HIS A   84  1                                  23    
-HELIX    5   5 ARG A  100  ALA A  105  1                                   6    
-HELIX    6   6 THR A  110  HIS A  120  1                                  11    
-HELIX    7   7 PRO A  125  SER A  146  1                                  22    
-HELIX    8   8 SER A  149  ILE A  153  5                                   5    
-HELIX    9   9 PRO A  160  GLN A  176  1                                  17    
-HELIX   10  10 GLU A  187  ASN A  193  1                                   7    
-HELIX   11  11 ASN A  195  ALA A  204  1                                  10    
-HELIX   12  12 THR A  210  CYS A  218  1                                   9    
-SHEET    1   A 2 ILE A   2  GLN A   4  0                                        
-SHEET    2   A 2 MET A  10  HIS A  12 -1  O  VAL A  11   N  VAL A   3           
-SSBOND   1 CYS A   14    CYS A   45                          1555   6555  2.06  
-CISPEP   1 GLN A    7    GLY A    8          0        -3.47                     
-CISPEP   2 ASN A  121    PRO A  122          0        -1.06                     
-SITE     1 AC1 11 ASN A  53  LEU A  56  ASN A  57  GLN A  63                    
-SITE     2 AC1 11 MET A  66  LYS A  70  THR A 107  TYR A 130                    
-SITE     3 AC1 11 ARG A 173  SER A 178  GLU A 180                               
-CRYST1   91.383   91.383   56.587  90.00  90.00 120.00 P 6           6          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.010943  0.006318  0.000000        0.00000                         
-SCALE2      0.000000  0.012636  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.017672        0.00000                         
-ATOM      1  N   PRO A   1       9.981  12.464 -12.296  1.00 29.41           N  
-ANISOU    1  N   PRO A   1     3777   3613   3786     32   -584   -351       N  
-ATOM      2  CA  PRO A   1      11.174  11.956 -12.979  1.00 28.03           C  
-ANISOU    2  CA  PRO A   1     3679   3445   3525     51   -568   -381       C  
-ATOM      3  C   PRO A   1      10.958  11.828 -14.477  1.00 28.46           C  
-ANISOU    3  C   PRO A   1     3802   3502   3509     76   -641   -398       C  
-ATOM      4  O   PRO A   1       9.854  12.075 -14.963  1.00 29.85           O  
-ANISOU    4  O   PRO A   1     3963   3669   3711     70   -714   -386       O  
-ATOM      5  CB  PRO A   1      11.397  10.578 -12.327  1.00 30.38           C  
-ANISOU    5  CB  PRO A   1     3973   3718   3851     29   -569   -414       C  
-ATOM      6  CG  PRO A   1      10.239  10.377 -11.355  1.00 31.90           C  
-ANISOU    6  CG  PRO A   1     4082   3894   4146    -11   -590   -392       C  
-ATOM      7  CD  PRO A   1       9.716  11.732 -11.045  1.00 28.75           C  
-ANISOU    7  CD  PRO A   1     3632   3516   3775      1   -561   -351       C  
-ATOM      8  N   ILE A   2      12.012  11.461 -15.192  1.00 26.97           N  
-ANISOU    8  N   ILE A   2     3688   3332   3229    111   -619   -422       N  
-ATOM      9  CA  ILE A   2      11.908  11.127 -16.612  1.00 28.30           C  
-ANISOU    9  CA  ILE A   2     3939   3503   3311    147   -688   -448       C  
-ATOM     10  C   ILE A   2      11.986   9.616 -16.754  1.00 30.65           C  
-ANISOU   10  C   ILE A   2     4290   3763   3591    154   -738   -508       C  
-ATOM     11  O   ILE A   2      12.921   8.993 -16.253  1.00 31.92           O  
-ANISOU   11  O   ILE A   2     4463   3927   3738    169   -681   -528       O  
-ATOM     12  CB  ILE A   2      13.031  11.797 -17.451  1.00 32.25           C  
-ANISOU   12  CB  ILE A   2     4494   4058   3700    196   -627   -427       C  
-ATOM     13  CG1 ILE A   2      13.160  13.269 -17.085  1.00 32.10           C  
-ANISOU   13  CG1 ILE A   2     4424   4062   3708    178   -571   -363       C  
-ATOM     14  CG2 ILE A   2      12.779  11.634 -18.973  1.00 28.39           C  
-ANISOU   14  CG2 ILE A   2     4097   3579   3112    242   -698   -448       C  
-ATOM     15  CD1 ILE A   2      12.125  14.136 -17.728  1.00 35.70           C  
-ANISOU   15  CD1 ILE A   2     4881   4510   4173    176   -635   -336       C  
-ATOM     16  N   VAL A   3      10.984   9.037 -17.405  1.00 35.39           N  
-ANISOU   16  N   VAL A   3     4924   4323   4198    142   -854   -534       N  
-ATOM     17  CA  VAL A   3      10.951   7.608 -17.725  1.00 42.60           C  
-ANISOU   17  CA  VAL A   3     5915   5183   5088    148   -933   -595       C  
-ATOM     18  C   VAL A   3      10.570   7.429 -19.192  1.00 43.61           C  
-ANISOU   18  C   VAL A   3     6146   5298   5125    185  -1035   -628       C  
-ATOM     19  O   VAL A   3      10.121   8.369 -19.831  1.00 41.54           O  
-ANISOU   19  O   VAL A   3     5875   5066   4841    191  -1054   -596       O  
-ATOM     20  CB  VAL A   3       9.942   6.844 -16.856  1.00 45.25           C  
-ANISOU   20  CB  VAL A   3     6186   5460   5546     71  -1002   -591       C  
-ATOM     21  CG1 VAL A   3      10.278   7.007 -15.389  1.00 47.43           C  
-ANISOU   21  CG1 VAL A   3     6367   5751   5902     40   -901   -558       C  
-ATOM     22  CG2 VAL A   3       8.544   7.346 -17.135  1.00 46.40           C  
-ANISOU   22  CG2 VAL A   3     6274   5600   5754     26  -1090   -554       C  
-ATOM     23  N   GLN A   4      10.741   6.224 -19.724  1.00 48.04           N  
-ANISOU   23  N   GLN A   4     6815   5810   5629    215  -1108   -693       N  
-ATOM     24  CA  GLN A   4      10.354   5.948 -21.108  1.00 51.42           C  
-ANISOU   24  CA  GLN A   4     7360   6216   5961    254  -1221   -734       C  
-ATOM     25  C   GLN A   4       8.932   5.398 -21.174  1.00 52.82           C  
-ANISOU   25  C   GLN A   4     7526   6319   6226    176  -1381   -740       C  
-ATOM     26  O   GLN A   4       8.527   4.629 -20.310  1.00 52.70           O  
-ANISOU   26  O   GLN A   4     7462   6248   6311    110  -1418   -739       O  
-ATOM     27  CB  GLN A   4      11.332   4.963 -21.757  1.00 52.77           C  
-ANISOU   27  CB  GLN A   4     7674   6370   6004    346  -1221   -808       C  
-ATOM     28  N   ASN A   5       8.167   5.807 -22.182  1.00 56.10           N  
-ANISOU   28  N   ASN A   5     7977   6735   6604    177  -1479   -735       N  
-ATOM     29  CA  ASN A   5       6.830   5.245 -22.375  1.00 58.00           C  
-ANISOU   29  CA  ASN A   5     8208   6906   6921    101  -1649   -736       C  
-ATOM     30  C   ASN A   5       6.870   4.125 -23.415  1.00 61.76           C  
-ANISOU   30  C   ASN A   5     8860   7308   7297    137  -1786   -819       C  
-ATOM     31  O   ASN A   5       7.924   3.539 -23.655  1.00 62.75           O  
-ANISOU   31  O   ASN A   5     9098   7425   7319    217  -1737   -879       O  
-ATOM     32  CB  ASN A   5       5.812   6.333 -22.759  1.00 56.00           C  
-ANISOU   32  CB  ASN A   5     7877   6693   6707     72  -1694   -674       C  
-ATOM     33  CG  ASN A   5       6.123   7.020 -24.088  1.00 56.66           C  
-ANISOU   33  CG  ASN A   5     8062   6818   6647    152  -1702   -688       C  
-ATOM     34  OD1 ASN A   5       6.816   6.481 -24.952  1.00 58.92           O  
-ANISOU   34  OD1 ASN A   5     8498   7092   6798    225  -1722   -752       O  
-ATOM     35  ND2 ASN A   5       5.585   8.221 -24.257  1.00 54.48           N  
-ANISOU   35  ND2 ASN A   5     7711   6593   6397    146  -1688   -626       N  
-ATOM     36  N   LEU A   6       5.730   3.826 -24.026  1.00 65.26           N  
-ANISOU   36  N   LEU A   6     9312   7703   7780     85  -1925   -804       N  
-ATOM     37  CA  LEU A   6       5.644   2.687 -24.938  1.00 67.95           C  
-ANISOU   37  CA  LEU A   6     9787   7965   8066    112  -2006   -847       C  
-ATOM     38  C   LEU A   6       5.923   3.078 -26.385  1.00 69.77           C  
-ANISOU   38  C   LEU A   6    10142   8225   8144    208  -2017   -877       C  
-ATOM     39  O   LEU A   6       5.887   2.234 -27.278  1.00 71.49           O  
-ANISOU   39  O   LEU A   6    10484   8381   8298    247  -2086   -916       O  
-ATOM     40  CB  LEU A   6       4.267   2.026 -24.837  1.00 69.61           C  
-ANISOU   40  CB  LEU A   6     9941   8100   8406      1  -2145   -805       C  
-ATOM     41  N   GLN A   7       6.195   4.359 -26.611  1.00 70.28           N  
-ANISOU   41  N   GLN A   7    10174   8381   8147    247  -1952   -852       N  
-ATOM     42  CA  GLN A   7       6.509   4.856 -27.951  1.00 73.21           C  
-ANISOU   42  CA  GLN A   7    10654   8795   8367    339  -1946   -867       C  
-ATOM     43  C   GLN A   7       7.783   4.260 -28.584  1.00 74.73           C  
-ANISOU   43  C   GLN A   7    10989   8998   8407    462  -1866   -927       C  
-ATOM     44  O   GLN A   7       7.825   4.099 -29.807  1.00 76.59           O  
-ANISOU   44  O   GLN A   7    11340   9229   8532    531  -1901   -951       O  
-ATOM     45  CB  GLN A   7       6.620   6.385 -27.932  1.00 73.47           C  
-ANISOU   45  CB  GLN A   7    10618   8928   8370    354  -1883   -815       C  
-ATOM     46  N   GLY A   8       8.823   3.948 -27.801  1.00 73.18           N  
-ANISOU   46  N   GLY A   8    10784   8821   8200    498  -1755   -948       N  
-ATOM     47  CA  GLY A   8       8.899   4.188 -26.368  1.00 69.82           C  
-ANISOU   47  CA  GLY A   8    10230   8406   7891    427  -1702   -924       C  
-ATOM     48  C   GLY A   8       9.812   5.353 -26.041  1.00 65.65           C  
-ANISOU   48  C   GLY A   8     9644   7989   7313    471  -1551   -886       C  
-ATOM     49  O   GLY A   8      11.031   5.260 -26.172  1.00 64.83           O  
-ANISOU   49  O   GLY A   8     9590   7936   7106    562  -1436   -904       O  
-ATOM     50  N   GLN A   9       9.216   6.450 -25.591  1.00 62.76           N  
-ANISOU   50  N   GLN A   9     9140   7661   7046    402  -1520   -807       N  
-ATOM     51  CA  GLN A   9       9.912   7.728 -25.526  1.00 60.64           C  
-ANISOU   51  CA  GLN A   9     8804   7489   6747    433  -1372   -740       C  
-ATOM     52  C   GLN A   9      10.146   8.216 -24.097  1.00 54.33           C  
-ANISOU   52  C   GLN A   9     7854   6710   6080    373  -1256   -686       C  
-ATOM     53  O   GLN A   9       9.438   7.814 -23.174  1.00 52.17           O  
-ANISOU   53  O   GLN A   9     7500   6385   5937    296  -1299   -682       O  
-ATOM     54  CB  GLN A   9       9.122   8.771 -26.313  1.00 63.12           C  
-ANISOU   54  CB  GLN A   9     9108   7831   7044    423  -1430   -692       C  
-ATOM     55  CG  GLN A   9       9.708  10.165 -26.293  1.00 64.74           C  
-ANISOU   55  CG  GLN A   9     9251   8121   7226    442  -1300   -615       C  
-ATOM     56  CD  GLN A   9       9.177  11.013 -27.428  1.00 67.13           C  
-ANISOU   56  CD  GLN A   9     9599   8451   7455    465  -1362   -581       C  
-ATOM     57  OE1 GLN A   9       8.207  10.643 -28.095  1.00 66.58           O  
-ANISOU   57  OE1 GLN A   9     9584   8337   7377    454  -1509   -610       O  
-ATOM     58  NE2 GLN A   9       9.817  12.154 -27.663  1.00 68.33           N  
-ANISOU   58  NE2 GLN A   9     9732   8675   7556    494  -1258   -514       N  
-ATOM     59  N   MET A  10      11.148   9.076 -23.924  1.00 50.43           N  
-ANISOU   59  N   MET A  10     7322   6292   5546    407  -1114   -640       N  
-ATOM     60  CA  MET A  10      11.466   9.639 -22.614  1.00 46.75           C  
-ANISOU   60  CA  MET A  10     6729   5845   5189    357  -1007   -590       C  
-ATOM     61  C   MET A  10      10.507  10.771 -22.292  1.00 42.07           C  
-ANISOU   61  C   MET A  10     6040   5253   4690    298  -1026   -527       C  
-ATOM     62  O   MET A  10      10.463  11.786 -22.996  1.00 37.62           O  
-ANISOU   62  O   MET A  10     5490   4729   4076    320  -1019   -485       O  
-ATOM     63  CB  MET A  10      12.913  10.141 -22.557  1.00 49.16           C  
-ANISOU   63  CB  MET A  10     7032   6227   5421    407   -862   -557       C  
-ATOM     64  CG  MET A  10      13.965   9.057 -22.807  1.00 51.80           C  
-ANISOU   64  CG  MET A  10     7448   6574   5659    483   -824   -612       C  
-ATOM     65  SD  MET A  10      13.582   7.468 -22.029  1.00 66.35           S  
-ANISOU   65  SD  MET A  10     9311   8319   7580    455   -900   -691       S  
-ATOM     66  CE  MET A  10      13.787   7.841 -20.295  1.00 41.24           C  
-ANISOU   66  CE  MET A  10     5979   5141   4548    375   -806   -641       C  
-ATOM     67  N   VAL A  11       9.734  10.586 -21.226  1.00 38.38           N  
-ANISOU   67  N   VAL A  11     5478   4746   4358    231  -1049   -519       N  
-ATOM     68  CA  VAL A  11       8.739  11.577 -20.845  1.00 36.19           C  
-ANISOU   68  CA  VAL A  11     5105   4471   4174    189  -1068   -463       C  
-ATOM     69  C   VAL A  11       8.775  11.860 -19.352  1.00 32.09           C  
-ANISOU   69  C   VAL A  11     4476   3952   3767    148   -985   -433       C  
-ATOM     70  O   VAL A  11       9.238  11.037 -18.549  1.00 29.62           O  
-ANISOU   70  O   VAL A  11     4148   3621   3485    131   -946   -459       O  
-ATOM     71  CB  VAL A  11       7.319  11.133 -21.216  1.00 37.51           C  
-ANISOU   71  CB  VAL A  11     5259   4596   4396    152  -1214   -471       C  
-ATOM     72  CG1 VAL A  11       7.154  11.063 -22.738  1.00 40.97           C  
-ANISOU   72  CG1 VAL A  11     5812   5035   4720    194  -1310   -495       C  
-ATOM     73  CG2 VAL A  11       7.007   9.801 -20.557  1.00 37.18           C  
-ANISOU   73  CG2 VAL A  11     5200   4501   4425    103  -1265   -508       C  
-ATOM     74  N   HIS A  12       8.269  13.030 -18.992  1.00 30.84           N  
-ANISOU   74  N   HIS A  12     4246   3808   3663    139   -961   -379       N  
-ATOM     75  CA  HIS A  12       8.197  13.421 -17.599  1.00 29.93           C  
-ANISOU   75  CA  HIS A  12     4035   3693   3644    112   -888   -351       C  
-ATOM     76  C   HIS A  12       7.007  12.763 -16.930  1.00 29.83           C  
-ANISOU   76  C   HIS A  12     3940   3655   3739     68   -949   -349       C  
-ATOM     77  O   HIS A  12       5.930  12.666 -17.516  1.00 30.72           O  
-ANISOU   77  O   HIS A  12     4036   3759   3877     56  -1050   -339       O  
-ATOM     78  CB  HIS A  12       8.097  14.934 -17.468  1.00 30.91           C  
-ANISOU   78  CB  HIS A  12     4130   3835   3780    130   -845   -299       C  
-ATOM     79  CG  HIS A  12       7.959  15.398 -16.055  1.00 32.66           C  
-ANISOU   79  CG  HIS A  12     4269   4052   4090    116   -777   -276       C  
-ATOM     80  ND1 HIS A  12       6.733  15.617 -15.461  1.00 34.49           N  
-ANISOU   80  ND1 HIS A  12     4415   4279   4412    110   -807   -252       N  
-ATOM     81  CD2 HIS A  12       8.890  15.661 -15.108  1.00 31.23           C  
-ANISOU   81  CD2 HIS A  12     4079   3872   3914    112   -683   -272       C  
-ATOM     82  CE1 HIS A  12       6.918  16.014 -14.214  1.00 33.45           C  
-ANISOU   82  CE1 HIS A  12     4235   4146   4329    111   -728   -239       C  
-ATOM     83  NE2 HIS A  12       8.217  16.042 -13.973  1.00 31.50           N  
-ANISOU   83  NE2 HIS A  12     4037   3898   4033    108   -659   -253       N  
-ATOM     84  N   GLN A  13       7.222  12.308 -15.703  1.00 28.33           N  
-ANISOU   84  N   GLN A  13     3696   3458   3612     41   -889   -351       N  
-ATOM     85  CA  GLN A  13       6.183  11.703 -14.898  1.00 33.06           C  
-ANISOU   85  CA  GLN A  13     4202   4044   4315     -4   -926   -333       C  
-ATOM     86  C   GLN A  13       6.203  12.340 -13.512  1.00 32.25           C  
-ANISOU   86  C   GLN A  13     4016   3962   4275     -1   -826   -299       C  
-ATOM     87  O   GLN A  13       7.268  12.691 -13.014  1.00 28.73           O  
-ANISOU   87  O   GLN A  13     3601   3521   3795     17   -737   -310       O  
-ATOM     88  CB  GLN A  13       6.399  10.201 -14.810  1.00 38.31           C  
-ANISOU   88  CB  GLN A  13     4900   4671   4985    -42   -969   -373       C  
-ATOM     89  CG  GLN A  13       5.441   9.478 -13.899  1.00 42.95           C  
-ANISOU   89  CG  GLN A  13     5391   5246   5684   -102  -1003   -343       C  
-ATOM     90  CD  GLN A  13       5.698   7.990 -13.908  1.00 46.10           C  
-ANISOU   90  CD  GLN A  13     5842   5591   6083   -142  -1060   -382       C  
-ATOM     91  OE1 GLN A  13       6.234   7.437 -12.950  1.00 45.99           O  
-ANISOU   91  OE1 GLN A  13     5814   5566   6093   -157   -999   -387       O  
-ATOM     92  NE2 GLN A  13       5.333   7.334 -15.005  1.00 48.51           N  
-ANISOU   92  NE2 GLN A  13     6219   5857   6357   -156  -1185   -412       N  
-ATOM     93  N   CYS A  14       5.031  12.523 -12.905  1.00 32.41           N  
-ANISOU   93  N   CYS A  14     3934   3997   4383    -14   -843   -256       N  
-ATOM     94  CA  CYS A  14       4.976  13.145 -11.584  1.00 30.46           C  
-ANISOU   94  CA  CYS A  14     3616   3772   4183      5   -748   -226       C  
-ATOM     95  C   CYS A  14       5.667  12.248 -10.561  1.00 26.84           C  
-ANISOU   95  C   CYS A  14     3155   3303   3740    -27   -689   -245       C  
-ATOM     96  O   CYS A  14       5.604  11.029 -10.671  1.00 24.91           O  
-ANISOU   96  O   CYS A  14     2917   3037   3513    -73   -740   -260       O  
-ATOM     97  CB  CYS A  14       3.526  13.416 -11.174  1.00 30.43           C  
-ANISOU   97  CB  CYS A  14     3495   3800   4266      9   -774   -170       C  
-ATOM     98  SG  CYS A  14       2.774  14.772 -12.145  1.00 44.80           S  
-ANISOU   98  SG  CYS A  14     5315   5638   6071     68   -823   -142       S  
-ATOM     99  N   ILE A  15       6.329  12.858  -9.584  1.00 23.92           N  
-ANISOU   99  N   ILE A  15     2785   2942   3362     -1   -592   -243       N  
-ATOM    100  CA  ILE A  15       6.918  12.111  -8.480  1.00 26.89           C  
-ANISOU  100  CA  ILE A  15     3151   3312   3755    -26   -534   -253       C  
-ATOM    101  C   ILE A  15       5.792  11.485  -7.668  1.00 28.07           C  
-ANISOU  101  C   ILE A  15     3196   3479   3988    -55   -545   -211       C  
-ATOM    102  O   ILE A  15       4.784  12.133  -7.433  1.00 26.57           O  
-ANISOU  102  O   ILE A  15     2932   3322   3841    -30   -543   -169       O  
-ATOM    103  CB  ILE A  15       7.789  13.015  -7.591  1.00 30.22           C  
-ANISOU  103  CB  ILE A  15     3595   3738   4148      8   -439   -256       C  
-ATOM    104  CG1 ILE A  15       8.394  12.205  -6.437  1.00 30.09           C  
-ANISOU  104  CG1 ILE A  15     3568   3717   4146    -17   -385   -265       C  
-ATOM    105  CG2 ILE A  15       6.969  14.213  -7.095  1.00 32.76           C  
-ANISOU  105  CG2 ILE A  15     3869   4080   4498     56   -412   -222       C  
-ATOM    106  CD1 ILE A  15       9.768  12.694  -5.996  1.00 33.30           C  
-ANISOU  106  CD1 ILE A  15     4036   4116   4501     -3   -320   -286       C  
-ATOM    107  N   SER A  16       5.929  10.223  -7.263  1.00 25.59           N  
-ANISOU  107  N   SER A  16     2875   3147   3702   -107   -559   -216       N  
-ATOM    108  CA  SER A  16       4.778   9.564  -6.637  1.00 25.56           C  
-ANISOU  108  CA  SER A  16     2765   3164   3784   -148   -583   -160       C  
-ATOM    109  C   SER A  16       4.773   9.746  -5.127  1.00 23.83           C  
-ANISOU  109  C   SER A  16     2485   2978   3589   -131   -483   -127       C  
-ATOM    110  O   SER A  16       5.828   9.900  -4.503  1.00 23.78           O  
-ANISOU  110  O   SER A  16     2535   2961   3540   -111   -412   -158       O  
-ATOM    111  CB  SER A  16       4.753   8.071  -6.957  1.00 28.17           C  
-ANISOU  111  CB  SER A  16     3116   3448   4139   -221   -667   -169       C  
-ATOM    112  OG  SER A  16       5.610   7.389  -6.070  1.00 30.37           O  
-ANISOU  112  OG  SER A  16     3424   3707   4409   -236   -611   -185       O  
-ATOM    113  N   PRO A  17       3.578   9.719  -4.535  1.00 25.55           N  
-ANISOU  113  N   PRO A  17     2587   3245   3876   -137   -477    -58       N  
-ATOM    114  CA  PRO A  17       3.434   9.801  -3.079  1.00 26.10           C  
-ANISOU  114  CA  PRO A  17     2594   3357   3965   -115   -380    -18       C  
-ATOM    115  C   PRO A  17       4.227   8.693  -2.418  1.00 26.97           C  
-ANISOU  115  C   PRO A  17     2741   3435   4073   -167   -362    -32       C  
-ATOM    116  O   PRO A  17       4.806   8.910  -1.350  1.00 26.04           O  
-ANISOU  116  O   PRO A  17     2638   3328   3926   -137   -276    -38       O  
-ATOM    117  CB  PRO A  17       1.924   9.637  -2.864  1.00 26.92           C  
-ANISOU  117  CB  PRO A  17     2556   3524   4151   -130   -402     70       C  
-ATOM    118  CG  PRO A  17       1.328  10.233  -4.117  1.00 29.83           C  
-ANISOU  118  CG  PRO A  17     2919   3891   4523   -114   -481     66       C  
-ATOM    119  CD  PRO A  17       2.277   9.792  -5.230  1.00 29.40           C  
-ANISOU  119  CD  PRO A  17     2991   3760   4419   -152   -555     -9       C  
-ATOM    120  N   ARG A  18       4.300   7.541  -3.086  1.00 27.42           N  
-ANISOU  120  N   ARG A  18     2824   3442   4150   -240   -451    -43       N  
-ATOM    121  CA  ARG A  18       5.060   6.408  -2.577  1.00 29.33           C  
-ANISOU  121  CA  ARG A  18     3112   3641   4391   -286   -449    -59       C  
-ATOM    122  C   ARG A  18       6.513   6.814  -2.373  1.00 26.38           C  
-ANISOU  122  C   ARG A  18     2839   3246   3938   -239   -384   -126       C  
-ATOM    123  O   ARG A  18       7.098   6.573  -1.321  1.00 27.51           O  
-ANISOU  123  O   ARG A  18     2990   3393   4071   -235   -319   -123       O  
-ATOM    124  CB  ARG A  18       4.982   5.212  -3.534  1.00 34.67           C  
-ANISOU  124  CB  ARG A  18     3833   4251   5089   -356   -571    -76       C  
-ATOM    125  CG  ARG A  18       3.586   4.650  -3.778  1.00 41.44           C  
-ANISOU  125  CG  ARG A  18     4593   5118   6034   -426   -661     -4       C  
-ATOM    126  CD  ARG A  18       2.882   4.321  -2.474  1.00 48.58           C  
-ANISOU  126  CD  ARG A  18     5378   6075   7006   -459   -605     89       C  
-ATOM    127  NE  ARG A  18       3.681   3.449  -1.614  1.00 53.53           N  
-ANISOU  127  NE  ARG A  18     6050   6666   7624   -485   -569     82       N  
-ATOM    128  CZ  ARG A  18       3.209   2.371  -0.989  1.00 57.95           C  
-ANISOU  128  CZ  ARG A  18     6555   7213   8249   -565   -599    152       C  
-ATOM    129  NH1 ARG A  18       1.938   2.016  -1.135  1.00 59.96           N  
-ANISOU  129  NH1 ARG A  18     6700   7494   8590   -634   -668    239       N  
-ATOM    130  NH2 ARG A  18       4.010   1.641  -0.222  1.00 58.33           N  
-ANISOU  130  NH2 ARG A  18     6655   7225   8282   -580   -565    141       N  
-ATOM    131  N   THR A  19       7.094   7.448  -3.386  1.00 23.69           N  
-ANISOU  131  N   THR A  19     2572   2888   3541   -204   -404   -179       N  
-ATOM    132  CA  THR A  19       8.484   7.880  -3.302  1.00 21.32           C  
-ANISOU  132  CA  THR A  19     2355   2574   3170   -166   -349   -231       C  
-ATOM    133  C   THR A  19       8.666   8.991  -2.263  1.00 24.94           C  
-ANISOU  133  C   THR A  19     2794   3070   3612   -118   -257   -217       C  
-ATOM    134  O   THR A  19       9.622   8.971  -1.480  1.00 22.46           O  
-ANISOU  134  O   THR A  19     2515   2749   3268   -110   -203   -233       O  
-ATOM    135  CB  THR A  19       8.988   8.359  -4.675  1.00 21.08           C  
-ANISOU  135  CB  THR A  19     2398   2528   3082   -141   -389   -275       C  
-ATOM    136  OG1 THR A  19       8.882   7.277  -5.609  1.00 20.85           O  
-ANISOU  136  OG1 THR A  19     2408   2460   3055   -174   -478   -298       O  
-ATOM    137  CG2 THR A  19      10.434   8.804  -4.598  1.00 21.56           C  
-ANISOU  137  CG2 THR A  19     2530   2587   3076   -109   -332   -311       C  
-ATOM    138  N   LEU A  20       7.751   9.955  -2.276  1.00 25.66           N  
-ANISOU  138  N   LEU A  20     2836   3195   3720    -83   -247   -188       N  
-ATOM    139  CA  LEU A  20       7.822  11.103  -1.378  1.00 25.87           C  
-ANISOU  139  CA  LEU A  20     2860   3245   3724    -24   -172   -182       C  
-ATOM    140  C   LEU A  20       7.796  10.618   0.059  1.00 25.73           C  
-ANISOU  140  C   LEU A  20     2806   3249   3721    -27   -110   -155       C  
-ATOM    141  O   LEU A  20       8.622  11.022   0.877  1.00 25.22           O  
-ANISOU  141  O   LEU A  20     2789   3178   3615     -2    -56   -175       O  
-ATOM    142  CB  LEU A  20       6.661  12.065  -1.648  1.00 28.25           C  
-ANISOU  142  CB  LEU A  20     3108   3580   4046     24   -179   -151       C  
-ATOM    143  CG  LEU A  20       6.761  12.872  -2.955  1.00 30.22           C  
-ANISOU  143  CG  LEU A  20     3407   3808   4268     43   -230   -176       C  
-ATOM    144  CD1 LEU A  20       5.414  13.453  -3.362  1.00 31.30           C  
-ANISOU  144  CD1 LEU A  20     3473   3978   4442     78   -260   -137       C  
-ATOM    145  CD2 LEU A  20       7.775  13.973  -2.805  1.00 30.44           C  
-ANISOU  145  CD2 LEU A  20     3519   3810   4235     81   -192   -209       C  
-ATOM    146  N   ASN A  21       6.861   9.717   0.352  1.00 24.36           N  
-ANISOU  146  N   ASN A  21     2549   3101   3606    -64   -124   -104       N  
-ATOM    147  CA  ASN A  21       6.729   9.219   1.711  1.00 26.38           C  
-ANISOU  147  CA  ASN A  21     2763   3386   3875    -69    -63    -64       C  
-ATOM    148  C   ASN A  21       7.933   8.383   2.136  1.00 24.36           C  
-ANISOU  148  C   ASN A  21     2573   3089   3594   -106    -56    -95       C  
-ATOM    149  O   ASN A  21       8.408   8.518   3.267  1.00 21.40           O  
-ANISOU  149  O   ASN A  21     2215   2726   3189    -82      9    -93       O  
-ATOM    150  CB  ASN A  21       5.449   8.411   1.857  1.00 32.16           C  
-ANISOU  150  CB  ASN A  21     3380   4157   4681   -112    -86     14       C  
-ATOM    151  CG  ASN A  21       5.184   8.028   3.287  1.00 37.66           C  
-ANISOU  151  CG  ASN A  21     4023   4900   5387   -107    -11     71       C  
-ATOM    152  OD1 ASN A  21       5.066   8.895   4.161  1.00 39.69           O  
-ANISOU  152  OD1 ASN A  21     4272   5202   5606    -30     70     78       O  
-ATOM    153  ND2 ASN A  21       5.099   6.729   3.547  1.00 36.99           N  
-ANISOU  153  ND2 ASN A  21     3908   4801   5347   -186    -40    111       N  
-ATOM    154  N   ALA A  22       8.447   7.545   1.227  1.00 24.69           N  
-ANISOU  154  N   ALA A  22     2658   3081   3642   -155   -124   -126       N  
-ATOM    155  CA  ALA A  22       9.633   6.728   1.521  1.00 27.10           C  
-ANISOU  155  CA  ALA A  22     3028   3346   3921   -179   -122   -157       C  
-ATOM    156  C   ALA A  22      10.801   7.579   1.985  1.00 27.20           C  
-ANISOU  156  C   ALA A  22     3103   3359   3871   -134    -66   -196       C  
-ATOM    157  O   ALA A  22      11.449   7.263   2.987  1.00 29.64           O  
-ANISOU  157  O   ALA A  22     3430   3667   4163   -134    -25   -193       O  
-ATOM    158  CB  ALA A  22      10.050   5.905   0.301  1.00 26.86           C  
-ANISOU  158  CB  ALA A  22     3052   3265   3891   -212   -203   -196       C  
-ATOM    159  N   TRP A  23      11.076   8.660   1.259  1.00 21.59           N  
-ANISOU  159  N   TRP A  23     2428   2649   3126    -99    -70   -226       N  
-ATOM    160  CA  TRP A  23      12.231   9.489   1.579  1.00 22.13           C  
-ANISOU  160  CA  TRP A  23     2557   2711   3140    -71    -34   -256       C  
-ATOM    161  C   TRP A  23      12.049  10.188   2.918  1.00 22.82           C  
-ANISOU  161  C   TRP A  23     2637   2820   3214    -35     26   -239       C  
-ATOM    162  O   TRP A  23      12.992  10.264   3.736  1.00 22.34           O  
-ANISOU  162  O   TRP A  23     2618   2751   3121    -32     55   -251       O  
-ATOM    163  CB  TRP A  23      12.475  10.518   0.470  1.00 20.32           C  
-ANISOU  163  CB  TRP A  23     2365   2474   2882    -50    -58   -279       C  
-ATOM    164  CG  TRP A  23      13.499  11.573   0.821  1.00 23.44           C  
-ANISOU  164  CG  TRP A  23     2815   2862   3231    -29    -30   -295       C  
-ATOM    165  CD1 TRP A  23      13.308  12.925   0.815  1.00 21.49           C  
-ANISOU  165  CD1 TRP A  23     2591   2610   2966      5    -24   -294       C  
-ATOM    166  CD2 TRP A  23      14.858  11.365   1.221  1.00 23.08           C  
-ANISOU  166  CD2 TRP A  23     2808   2806   3154    -45    -15   -308       C  
-ATOM    167  NE1 TRP A  23      14.456  13.563   1.180  1.00 22.96           N  
-ANISOU  167  NE1 TRP A  23     2831   2778   3114      2    -13   -305       N  
-ATOM    168  CE2 TRP A  23      15.427  12.634   1.430  1.00 23.33           C  
-ANISOU  168  CE2 TRP A  23     2882   2829   3155    -30     -6   -311       C  
-ATOM    169  CE3 TRP A  23      15.651  10.227   1.420  1.00 22.78           C  
-ANISOU  169  CE3 TRP A  23     2774   2766   3116    -69    -13   -315       C  
-ATOM    170  CZ2 TRP A  23      16.750  12.803   1.836  1.00 23.20           C  
-ANISOU  170  CZ2 TRP A  23     2901   2805   3109    -48      1   -314       C  
-ATOM    171  CZ3 TRP A  23      16.962  10.395   1.809  1.00 24.34           C  
-ANISOU  171  CZ3 TRP A  23     3004   2963   3282    -75      1   -320       C  
-ATOM    172  CH2 TRP A  23      17.502  11.675   2.013  1.00 24.07           C  
-ANISOU  172  CH2 TRP A  23     3001   2924   3220    -69      7   -317       C  
-ATOM    173  N   VAL A  24      10.850  10.718   3.128  1.00 24.29           N  
-ANISOU  173  N   VAL A  24     2773   3036   3421     -2     43   -210       N  
-ATOM    174  CA  VAL A  24      10.543  11.426   4.360  1.00 28.38           C  
-ANISOU  174  CA  VAL A  24     3289   3578   3914     53    103   -196       C  
-ATOM    175  C   VAL A  24      10.736  10.508   5.567  1.00 25.45           C  
-ANISOU  175  C   VAL A  24     2905   3224   3543     35    142   -172       C  
-ATOM    176  O   VAL A  24      11.319  10.915   6.571  1.00 24.12           O  
-ANISOU  176  O   VAL A  24     2784   3052   3328     64    179   -185       O  
-ATOM    177  CB  VAL A  24       9.110  11.988   4.335  1.00 33.78           C  
-ANISOU  177  CB  VAL A  24     3907   4306   4624    103    119   -160       C  
-ATOM    178  CG1 VAL A  24       8.573  12.214   5.755  1.00 35.81           C  
-ANISOU  178  CG1 VAL A  24     4140   4608   4860    162    192   -129       C  
-ATOM    179  CG2 VAL A  24       9.077  13.277   3.515  1.00 34.11           C  
-ANISOU  179  CG2 VAL A  24     3991   4325   4644    146     93   -188       C  
-ATOM    180  N   LYS A  25      10.267   9.268   5.458  1.00 25.97           N  
-ANISOU  180  N   LYS A  25     2910   3298   3658    -17    124   -136       N  
-ATOM    181  CA  LYS A  25      10.352   8.324   6.571  1.00 29.37           C  
-ANISOU  181  CA  LYS A  25     3323   3743   4093    -40    157   -101       C  
-ATOM    182  C   LYS A  25      11.779   7.824   6.824  1.00 30.34           C  
-ANISOU  182  C   LYS A  25     3518   3824   4185    -66    146   -137       C  
-ATOM    183  O   LYS A  25      12.183   7.668   7.974  1.00 32.68           O  
-ANISOU  183  O   LYS A  25     3834   4130   4452    -55    186   -127       O  
-ATOM    184  CB  LYS A  25       9.408   7.142   6.323  1.00 30.95           C  
-ANISOU  184  CB  LYS A  25     3440   3956   4363    -98    127    -43       C  
-ATOM    185  CG  LYS A  25       7.965   7.558   6.152  1.00 35.58           C  
-ANISOU  185  CG  LYS A  25     3934   4597   4988    -77    137      9       C  
-ATOM    186  CD  LYS A  25       7.341   7.875   7.499  1.00 41.32           C  
-ANISOU  186  CD  LYS A  25     4613   5394   5694    -22    225     63       C  
-ATOM    187  CE  LYS A  25       6.213   8.876   7.387  1.00 44.55           C  
-ANISOU  187  CE  LYS A  25     4957   5861   6107     49    256     91       C  
-ATOM    188  NZ  LYS A  25       5.705   9.214   8.743  1.00 46.95           N  
-ANISOU  188  NZ  LYS A  25     5228   6238   6372    122    351    137       N  
-ATOM    189  N   VAL A  26      12.533   7.570   5.755  1.00 27.42           N  
-ANISOU  189  N   VAL A  26     3185   3414   3819    -94     94   -177       N  
-ATOM    190  CA  VAL A  26      13.957   7.222   5.853  1.00 28.02           C  
-ANISOU  190  CA  VAL A  26     3323   3460   3864   -107     85   -210       C  
-ATOM    191  C   VAL A  26      14.752   8.248   6.680  1.00 27.88           C  
-ANISOU  191  C   VAL A  26     3354   3448   3791    -71    120   -229       C  
-ATOM    192  O   VAL A  26      15.492   7.913   7.621  1.00 26.52           O  
-ANISOU  192  O   VAL A  26     3208   3272   3595    -75    137   -226       O  
-ATOM    193  CB  VAL A  26      14.592   7.124   4.438  1.00 45.26           C  
-ANISOU  193  CB  VAL A  26     5537   5617   6045   -119     35   -248       C  
-ATOM    194  CG1 VAL A  26      16.083   7.418   4.485  1.00 45.73           C  
-ANISOU  194  CG1 VAL A  26     5650   5667   6060   -110     40   -278       C  
-ATOM    195  CG2 VAL A  26      14.304   5.772   3.810  1.00 46.06           C  
-ANISOU  195  CG2 VAL A  26     5626   5691   6185   -156    -14   -244       C  
-ATOM    196  N   VAL A  27      14.573   9.516   6.347  1.00 26.26           N  
-ANISOU  196  N   VAL A  27     3168   3246   3566    -38    122   -246       N  
-ATOM    197  CA  VAL A  27      15.244  10.579   7.105  1.00 27.18           C  
-ANISOU  197  CA  VAL A  27     3343   3353   3631     -8    139   -264       C  
-ATOM    198  C   VAL A  27      14.743  10.637   8.546  1.00 27.18           C  
-ANISOU  198  C   VAL A  27     3345   3377   3607     28    187   -244       C  
-ATOM    199  O   VAL A  27      15.538  10.787   9.476  1.00 28.94           O  
-ANISOU  199  O   VAL A  27     3619   3590   3790     34    195   -254       O  
-ATOM    200  CB  VAL A  27      15.048  11.938   6.415  1.00 28.76           C  
-ANISOU  200  CB  VAL A  27     3570   3540   3817     20    122   -283       C  
-ATOM    201  CG1 VAL A  27      15.630  13.068   7.274  1.00 30.02           C  
-ANISOU  201  CG1 VAL A  27     3804   3677   3927     50    126   -301       C  
-ATOM    202  CG2 VAL A  27      15.695  11.896   5.033  1.00 29.23           C  
-ANISOU  202  CG2 VAL A  27     3635   3585   3888    -15     80   -297       C  
-ATOM    203  N   GLU A  28      13.431  10.509   8.732  1.00 29.40           N  
-ANISOU  203  N   GLU A  28     3567   3694   3910     55    219   -211       N  
-ATOM    204  CA  GLU A  28      12.833  10.537  10.068  1.00 32.56           C  
-ANISOU  204  CA  GLU A  28     3958   4132   4280    102    278   -181       C  
-ATOM    205  C   GLU A  28      13.401   9.415  10.961  1.00 35.41           C  
-ANISOU  205  C   GLU A  28     4322   4497   4635     66    291   -159       C  
-ATOM    206  O   GLU A  28      13.726   9.633  12.134  1.00 34.49           O  
-ANISOU  206  O   GLU A  28     4252   4389   4463     99    321   -159       O  
-ATOM    207  CB  GLU A  28      11.304  10.422   9.978  1.00 32.41           C  
-ANISOU  207  CB  GLU A  28     3850   4167   4298    129    311   -131       C  
-ATOM    208  CG  GLU A  28      10.601  11.718   9.573  1.00 35.62           C  
-ANISOU  208  CG  GLU A  28     4262   4582   4691    199    317   -147       C  
-ATOM    209  CD  GLU A  28       9.076  11.625   9.615  1.00 41.07           C  
-ANISOU  209  CD  GLU A  28     4848   5340   5415    237    357    -87       C  
-ATOM    210  OE1 GLU A  28       8.537  10.522   9.867  1.00 40.68           O  
-ANISOU  210  OE1 GLU A  28     4717   5331   5408    194    374    -27       O  
-ATOM    211  OE2 GLU A  28       8.413  12.664   9.394  1.00 43.74           O  
-ANISOU  211  OE2 GLU A  28     5185   5693   5741    310    369    -95       O  
-ATOM    212  N   GLU A  29      13.526   8.222  10.395  1.00 32.37           N  
-ANISOU  212  N   GLU A  29     3896   4099   4302      2    261   -141       N  
-ATOM    213  CA  GLU A  29      13.998   7.073  11.154  1.00 35.81           C  
-ANISOU  213  CA  GLU A  29     4334   4532   4740    -33    266   -114       C  
-ATOM    214  C   GLU A  29      15.524   7.027  11.279  1.00 35.76           C  
-ANISOU  214  C   GLU A  29     4397   4488   4702    -47    236   -154       C  
-ATOM    215  O   GLU A  29      16.041   6.673  12.328  1.00 38.27           O  
-ANISOU  215  O   GLU A  29     4744   4809   4989    -45    252   -142       O  
-ATOM    216  CB  GLU A  29      13.469   5.781  10.520  0.60 35.92           C  
-ANISOU  216  CB  GLU A  29     4288   4538   4825    -92    235    -76       C  
-ATOM    217  CG  GLU A  29      11.955   5.653  10.626  0.60 37.55           C  
-ANISOU  217  CG  GLU A  29     4407   4792   5069    -91    263    -13       C  
-ATOM    218  CD  GLU A  29      11.373   4.551   9.752  0.60 39.63           C  
-ANISOU  218  CD  GLU A  29     4615   5033   5410   -161    208     19       C  
-ATOM    219  OE1 GLU A  29      12.148   3.809   9.120  0.60 39.43           O  
-ANISOU  219  OE1 GLU A  29     4631   4951   5401   -201    151    -13       O  
-ATOM    220  OE2 GLU A  29      10.128   4.434   9.697  0.60 41.28           O  
-ANISOU  220  OE2 GLU A  29     4741   5282   5662   -173    217     79       O  
-ATOM    221  N   LYS A  30      16.248   7.424  10.240  1.00 33.85           N  
-ANISOU  221  N   LYS A  30     4179   4218   4466    -60    194   -196       N  
-ATOM    222  CA  LYS A  30      17.679   7.119  10.172  1.00 32.95           C  
-ANISOU  222  CA  LYS A  30     4104   4078   4337    -81    164   -218       C  
-ATOM    223  C   LYS A  30      18.628   8.314  10.248  1.00 32.87           C  
-ANISOU  223  C   LYS A  30     4148   4059   4285    -68    149   -249       C  
-ATOM    224  O   LYS A  30      19.842   8.130  10.328  1.00 32.91           O  
-ANISOU  224  O   LYS A  30     4174   4054   4277    -86    125   -256       O  
-ATOM    225  CB  LYS A  30      17.975   6.351   8.881  1.00 32.38           C  
-ANISOU  225  CB  LYS A  30     4013   3987   4305   -109    125   -230       C  
-ATOM    226  CG  LYS A  30      17.311   4.977   8.797  1.00 33.03           C  
-ANISOU  226  CG  LYS A  30     4060   4057   4432   -136    115   -202       C  
-ATOM    227  CD  LYS A  30      17.804   4.028   9.868  1.00 34.27           C  
-ANISOU  227  CD  LYS A  30     4231   4208   4584   -147    123   -176       C  
-ATOM    228  CE  LYS A  30      17.386   2.571   9.564  1.00 35.80           C  
-ANISOU  228  CE  LYS A  30     4406   4370   4828   -183     92   -151       C  
-ATOM    229  NZ  LYS A  30      18.335   1.857   8.621  1.00 34.75           N  
-ANISOU  229  NZ  LYS A  30     4304   4197   4701   -182     44   -187       N  
-ATOM    230  N   ALA A  31      18.089   9.530  10.198  1.00 34.55           N  
-ANISOU  230  N   ALA A  31     4380   4271   4477    -38    156   -262       N  
-ATOM    231  CA  ALA A  31      18.927  10.730  10.228  1.00 35.76           C  
-ANISOU  231  CA  ALA A  31     4592   4401   4595    -34    128   -287       C  
-ATOM    232  C   ALA A  31      19.952  10.682   9.104  1.00 35.49           C  
-ANISOU  232  C   ALA A  31     4547   4358   4580    -74     90   -293       C  
-ATOM    233  O   ALA A  31      19.608  10.368   7.968  1.00 38.77           O  
-ANISOU  233  O   ALA A  31     4925   4780   5025    -81     86   -294       O  
-ATOM    234  CB  ALA A  31      19.619  10.873  11.576  1.00 36.77           C  
-ANISOU  234  CB  ALA A  31     4774   4521   4675    -28    124   -288       C  
-ATOM    235  N   PHE A  32      21.213  10.971   9.417  1.00 33.02           N  
-ANISOU  235  N   PHE A  32     4264   4036   4246    -97     60   -293       N  
-ATOM    236  CA  PHE A  32      22.265  10.893   8.398  1.00 31.32           C  
-ANISOU  236  CA  PHE A  32     4025   3830   4045   -129     34   -286       C  
-ATOM    237  C   PHE A  32      23.218   9.723   8.624  1.00 29.75           C  
-ANISOU  237  C   PHE A  32     3800   3651   3854   -142     32   -272       C  
-ATOM    238  O   PHE A  32      24.414   9.804   8.336  1.00 31.83           O  
-ANISOU  238  O   PHE A  32     4051   3929   4114   -163     10   -256       O  
-ATOM    239  CB  PHE A  32      23.015  12.219   8.331  1.00 33.86           C  
-ANISOU  239  CB  PHE A  32     4386   4134   4347   -153     -6   -281       C  
-ATOM    240  CG  PHE A  32      22.128  13.345   7.953  1.00 36.51           C  
-ANISOU  240  CG  PHE A  32     4753   4443   4677   -134    -11   -295       C  
-ATOM    241  CD1 PHE A  32      21.725  13.500   6.637  1.00 37.83           C  
-ANISOU  241  CD1 PHE A  32     4892   4619   4864   -133     -8   -293       C  
-ATOM    242  CD2 PHE A  32      21.618  14.201   8.918  1.00 37.32           C  
-ANISOU  242  CD2 PHE A  32     4920   4511   4749   -106    -17   -313       C  
-ATOM    243  CE1 PHE A  32      20.867  14.525   6.283  1.00 39.91           C  
-ANISOU  243  CE1 PHE A  32     5183   4856   5123   -110    -15   -303       C  
-ATOM    244  CE2 PHE A  32      20.755  15.226   8.568  1.00 36.82           C  
-ANISOU  244  CE2 PHE A  32     4889   4420   4679    -74    -21   -327       C  
-ATOM    245  CZ  PHE A  32      20.380  15.385   7.250  1.00 38.28           C  
-ANISOU  245  CZ  PHE A  32     5039   4615   4892    -79    -21   -320       C  
-ATOM    246  N   SER A  33      22.667   8.623   9.125  1.00 30.36           N  
-ANISOU  246  N   SER A  33     3865   3729   3943   -128     56   -270       N  
-ATOM    247  CA  SER A  33      23.362   7.349   9.081  1.00 31.52           C  
-ANISOU  247  CA  SER A  33     3987   3885   4103   -130     53   -260       C  
-ATOM    248  C   SER A  33      23.728   7.085   7.614  1.00 29.16           C  
-ANISOU  248  C   SER A  33     3661   3599   3819   -125     45   -267       C  
-ATOM    249  O   SER A  33      22.982   7.469   6.703  1.00 29.83           O  
-ANISOU  249  O   SER A  33     3741   3681   3912   -121     48   -280       O  
-ATOM    250  CB  SER A  33      22.483   6.234   9.657  1.00 35.63           C  
-ANISOU  250  CB  SER A  33     4501   4394   4641   -122     73   -252       C  
-ATOM    251  OG  SER A  33      23.253   5.070   9.901  1.00 40.67           O  
-ANISOU  251  OG  SER A  33     5135   5031   5288   -121     63   -241       O  
-ATOM    252  N   PRO A  34      24.887   6.463   7.371  1.00 27.32           N  
-ANISOU  252  N   PRO A  34     3411   3386   3583   -118     37   -257       N  
-ATOM    253  CA  PRO A  34      25.342   6.377   5.973  1.00 23.25           C  
-ANISOU  253  CA  PRO A  34     2874   2894   3064   -100     36   -262       C  
-ATOM    254  C   PRO A  34      24.379   5.652   5.018  1.00 21.45           C  
-ANISOU  254  C   PRO A  34     2653   2646   2850    -78     37   -289       C  
-ATOM    255  O   PRO A  34      24.336   6.023   3.843  1.00 22.22           O  
-ANISOU  255  O   PRO A  34     2747   2760   2937    -67     36   -297       O  
-ATOM    256  CB  PRO A  34      26.684   5.620   6.081  1.00 26.85           C  
-ANISOU  256  CB  PRO A  34     3308   3381   3513    -79     34   -244       C  
-ATOM    257  CG  PRO A  34      26.768   5.118   7.513  1.00 27.32           C  
-ANISOU  257  CG  PRO A  34     3382   3419   3578    -89     27   -234       C  
-ATOM    258  CD  PRO A  34      25.924   6.036   8.332  1.00 25.60           C  
-ANISOU  258  CD  PRO A  34     3191   3179   3356   -120     27   -237       C  
-ATOM    259  N   GLU A  35      23.597   4.683   5.494  1.00 23.56           N  
-ANISOU  259  N   GLU A  35     2932   2878   3140    -78     33   -296       N  
-ATOM    260  CA  GLU A  35      22.751   3.905   4.576  1.00 26.83           C  
-ANISOU  260  CA  GLU A  35     3357   3266   3573    -66     16   -318       C  
-ATOM    261  C   GLU A  35      21.574   4.744   4.056  1.00 27.70           C  
-ANISOU  261  C   GLU A  35     3460   3372   3693    -84     13   -324       C  
-ATOM    262  O   GLU A  35      20.813   4.299   3.203  1.00 27.83           O  
-ANISOU  262  O   GLU A  35     3482   3368   3724    -81    -11   -340       O  
-ATOM    263  CB  GLU A  35      22.252   2.605   5.232  1.00 25.65           C  
-ANISOU  263  CB  GLU A  35     3219   3073   3453    -74      0   -313       C  
-ATOM    264  CG  GLU A  35      21.178   2.767   6.298  1.00 28.98           C  
-ANISOU  264  CG  GLU A  35     3628   3485   3900   -109     13   -287       C  
-ATOM    265  CD  GLU A  35      21.755   2.968   7.691  1.00 29.05           C  
-ANISOU  265  CD  GLU A  35     3637   3508   3891   -114     36   -263       C  
-ATOM    266  OE1 GLU A  35      22.933   3.416   7.820  1.00 26.79           O  
-ANISOU  266  OE1 GLU A  35     3356   3246   3577   -101     40   -265       O  
-ATOM    267  OE2 GLU A  35      21.021   2.672   8.657  1.00 30.94           O  
-ANISOU  267  OE2 GLU A  35     3872   3739   4143   -132     49   -236       O  
-ATOM    268  N   VAL A  36      21.467   5.976   4.543  1.00 26.88           N  
-ANISOU  268  N   VAL A  36     3349   3285   3580    -98     31   -312       N  
-ATOM    269  CA  VAL A  36      20.476   6.916   4.055  1.00 28.03           C  
-ANISOU  269  CA  VAL A  36     3489   3430   3730   -102     30   -316       C  
-ATOM    270  C   VAL A  36      20.810   7.408   2.643  1.00 26.90           C  
-ANISOU  270  C   VAL A  36     3351   3302   3566    -90     17   -328       C  
-ATOM    271  O   VAL A  36      19.910   7.683   1.843  1.00 29.12           O  
-ANISOU  271  O   VAL A  36     3630   3577   3856    -88      2   -336       O  
-ATOM    272  CB  VAL A  36      20.350   8.120   5.029  1.00 32.58           C  
-ANISOU  272  CB  VAL A  36     4074   4010   4294   -108     48   -304       C  
-ATOM    273  CG1 VAL A  36      19.752   9.310   4.343  1.00 32.88           C  
-ANISOU  273  CG1 VAL A  36     4117   4049   4327   -102     42   -309       C  
-ATOM    274  CG2 VAL A  36      19.529   7.718   6.251  1.00 30.38           C  
-ANISOU  274  CG2 VAL A  36     3789   3725   4030   -108     68   -291       C  
-ATOM    275  N   ILE A  37      22.100   7.509   2.344  1.00 23.65           N  
-ANISOU  275  N   ILE A  37     2941   2917   3127    -82     22   -321       N  
-ATOM    276  CA  ILE A  37      22.575   8.062   1.078  1.00 21.13           C  
-ANISOU  276  CA  ILE A  37     2622   2627   2780    -69     20   -318       C  
-ATOM    277  C   ILE A  37      22.207   7.209  -0.139  1.00 22.14           C  
-ANISOU  277  C   ILE A  37     2765   2751   2896    -37      4   -344       C  
-ATOM    278  O   ILE A  37      21.664   7.727  -1.120  1.00 22.90           O  
-ANISOU  278  O   ILE A  37     2870   2850   2980    -32     -9   -350       O  
-ATOM    279  CB  ILE A  37      24.117   8.266   1.062  1.00 37.70           C  
-ANISOU  279  CB  ILE A  37     4703   4769   4851    -67     35   -289       C  
-ATOM    280  CG1 ILE A  37      24.561   9.314   2.088  1.00 38.27           C  
-ANISOU  280  CG1 ILE A  37     4771   4840   4930   -108     32   -261       C  
-ATOM    281  CG2 ILE A  37      24.588   8.661  -0.338  1.00 35.11           C  
-ANISOU  281  CG2 ILE A  37     4369   4484   4487    -47     41   -276       C  
-ATOM    282  CD1 ILE A  37      23.581  10.448   2.301  1.00 41.12           C  
-ANISOU  282  CD1 ILE A  37     5157   5167   5300   -129     20   -265       C  
-ATOM    283  N   PRO A  38      22.518   5.903  -0.099  1.00 22.97           N  
-ANISOU  283  N   PRO A  38     2881   2843   3001    -11     -3   -362       N  
-ATOM    284  CA  PRO A  38      22.070   4.997  -1.171  1.00 22.45           C  
-ANISOU  284  CA  PRO A  38     2850   2756   2923     22    -34   -396       C  
-ATOM    285  C   PRO A  38      20.548   4.916  -1.284  1.00 22.09           C  
-ANISOU  285  C   PRO A  38     2811   2667   2916     -8    -72   -408       C  
-ATOM    286  O   PRO A  38      20.024   4.647  -2.360  1.00 19.84           O  
-ANISOU  286  O   PRO A  38     2554   2367   2618      7   -109   -432       O  
-ATOM    287  CB  PRO A  38      22.652   3.631  -0.752  1.00 21.03           C  
-ANISOU  287  CB  PRO A  38     2690   2554   2746     51    -41   -410       C  
-ATOM    288  CG  PRO A  38      22.898   3.768   0.727  1.00 21.35           C  
-ANISOU  288  CG  PRO A  38     2701   2594   2818     16    -19   -381       C  
-ATOM    289  CD  PRO A  38      23.333   5.200   0.905  1.00 22.15           C  
-ANISOU  289  CD  PRO A  38     2770   2740   2905     -6     10   -352       C  
-ATOM    290  N   MET A  39      19.836   5.106  -0.181  1.00 21.93           N  
-ANISOU  290  N   MET A  39     2763   2630   2940    -48    -66   -389       N  
-ATOM    291  CA  MET A  39      18.385   5.152  -0.281  1.00 23.66           C  
-ANISOU  291  CA  MET A  39     2967   2825   3198    -75    -95   -385       C  
-ATOM    292  C   MET A  39      17.987   6.416  -1.062  1.00 20.14           C  
-ANISOU  292  C   MET A  39     2514   2403   2736    -70    -94   -383       C  
-ATOM    293  O   MET A  39      17.124   6.349  -1.950  1.00 20.03           O  
-ANISOU  293  O   MET A  39     2505   2376   2729    -71   -135   -393       O  
-ATOM    294  CB  MET A  39      17.719   5.117   1.105  1.00 26.53           C  
-ANISOU  294  CB  MET A  39     3295   3181   3605   -107    -75   -355       C  
-ATOM    295  CG  MET A  39      16.194   4.995   1.065  1.00 29.55           C  
-ANISOU  295  CG  MET A  39     3643   3550   4035   -134   -102   -337       C  
-ATOM    296  SD  MET A  39      15.628   3.421   0.337  1.00 32.46           S  
-ANISOU  296  SD  MET A  39     4033   3863   4436   -158   -180   -348       S  
-ATOM    297  CE  MET A  39      15.767   2.295   1.716  1.00 29.51           C  
-ANISOU  297  CE  MET A  39     3651   3463   4097   -187   -169   -317       C  
-ATOM    298  N   PHE A  40      18.621   7.552  -0.751  1.00 21.36           N  
-ANISOU  298  N   PHE A  40     2663   2586   2868    -67    -58   -367       N  
-ATOM    299  CA  PHE A  40      18.332   8.798  -1.476  1.00 20.49           C  
-ANISOU  299  CA  PHE A  40     2555   2491   2741    -63    -62   -360       C  
-ATOM    300  C   PHE A  40      18.569   8.612  -2.963  1.00 20.40           C  
-ANISOU  300  C   PHE A  40     2570   2491   2690    -39    -86   -376       C  
-ATOM    301  O   PHE A  40      17.715   8.944  -3.790  1.00 21.27           O  
-ANISOU  301  O   PHE A  40     2686   2595   2801    -36   -117   -380       O  
-ATOM    302  CB  PHE A  40      19.183   9.976  -0.971  1.00 22.07           C  
-ANISOU  302  CB  PHE A  40     2757   2707   2920    -70    -32   -338       C  
-ATOM    303  CG  PHE A  40      18.954  11.258  -1.740  1.00 25.29           C  
-ANISOU  303  CG  PHE A  40     3177   3121   3312    -68    -43   -325       C  
-ATOM    304  CD1 PHE A  40      17.797  11.997  -1.541  1.00 24.94           C  
-ANISOU  304  CD1 PHE A  40     3129   3058   3291    -65    -53   -323       C  
-ATOM    305  CD2 PHE A  40      19.883  11.711  -2.671  1.00 26.82           C  
-ANISOU  305  CD2 PHE A  40     3383   3342   3464    -66    -41   -308       C  
-ATOM    306  CE1 PHE A  40      17.569  13.167  -2.253  1.00 26.44           C  
-ANISOU  306  CE1 PHE A  40     3336   3245   3466    -59    -69   -310       C  
-ATOM    307  CE2 PHE A  40      19.664  12.891  -3.382  1.00 26.55           C  
-ANISOU  307  CE2 PHE A  40     3364   3309   3415    -69    -54   -288       C  
-ATOM    308  CZ  PHE A  40      18.510  13.619  -3.160  1.00 27.30           C  
-ANISOU  308  CZ  PHE A  40     3464   3373   3536    -66    -72   -292       C  
-ATOM    309  N   SER A  41      19.728   8.061  -3.295  1.00 22.18           N  
-ANISOU  309  N   SER A  41     2812   2737   2878    -16    -71   -382       N  
-ATOM    310  CA  SER A  41      20.090   7.843  -4.694  1.00 24.62           C  
-ANISOU  310  CA  SER A  41     3153   3068   3132     23    -84   -397       C  
-ATOM    311  C   SER A  41      19.094   6.962  -5.435  1.00 24.43           C  
-ANISOU  311  C   SER A  41     3163   3005   3113     35   -142   -434       C  
-ATOM    312  O   SER A  41      18.748   7.250  -6.579  1.00 23.16           O  
-ANISOU  312  O   SER A  41     3030   2853   2918     53   -169   -443       O  
-ATOM    313  CB  SER A  41      21.485   7.228  -4.797  1.00 21.32           C  
-ANISOU  313  CB  SER A  41     2742   2685   2672     62    -52   -396       C  
-ATOM    314  OG  SER A  41      21.877   7.201  -6.154  1.00 25.77           O  
-ANISOU  314  OG  SER A  41     3337   3285   3170    111    -52   -403       O  
-ATOM    315  N   ALA A  42      18.630   5.889  -4.795  1.00 24.68           N  
-ANISOU  315  N   ALA A  42     3197   2993   3189     19   -168   -450       N  
-ATOM    316  CA  ALA A  42      17.689   4.984  -5.445  1.00 23.64           C  
-ANISOU  316  CA  ALA A  42     3100   2813   3069     17   -240   -480       C  
-ATOM    317  C   ALA A  42      16.292   5.610  -5.542  1.00 21.61           C  
-ANISOU  317  C   ALA A  42     2808   2545   2857    -23   -275   -462       C  
-ATOM    318  O   ALA A  42      15.635   5.514  -6.562  1.00 21.27           O  
-ANISOU  318  O   ALA A  42     2792   2487   2801    -19   -333   -479       O  
-ATOM    319  CB  ALA A  42      17.631   3.640  -4.705  1.00 24.28           C  
-ANISOU  319  CB  ALA A  42     3194   2844   3189      3   -265   -491       C  
-ATOM    320  N   LEU A  43      15.835   6.266  -4.490  1.00 23.95           N  
-ANISOU  320  N   LEU A  43     3046   2853   3202    -55   -241   -428       N  
-ATOM    321  CA  LEU A  43      14.525   6.923  -4.561  1.00 23.43           C  
-ANISOU  321  CA  LEU A  43     2938   2788   3176    -78   -266   -405       C  
-ATOM    322  C   LEU A  43      14.477   8.051  -5.600  1.00 25.55           C  
-ANISOU  322  C   LEU A  43     3222   3081   3404    -54   -272   -405       C  
-ATOM    323  O   LEU A  43      13.404   8.382  -6.112  1.00 26.27           O  
-ANISOU  323  O   LEU A  43     3295   3168   3516    -61   -315   -396       O  
-ATOM    324  CB  LEU A  43      14.135   7.459  -3.186  1.00 21.36           C  
-ANISOU  324  CB  LEU A  43     2617   2539   2958    -96   -217   -370       C  
-ATOM    325  CG  LEU A  43      13.888   6.326  -2.187  1.00 22.05           C  
-ANISOU  325  CG  LEU A  43     2681   2605   3091   -127   -218   -357       C  
-ATOM    326  CD1 LEU A  43      13.651   6.895  -0.780  1.00 22.55           C  
-ANISOU  326  CD1 LEU A  43     2698   2693   3179   -131   -158   -322       C  
-ATOM    327  CD2 LEU A  43      12.691   5.502  -2.651  1.00 23.23           C  
-ANISOU  327  CD2 LEU A  43     2810   2727   3290   -162   -292   -346       C  
-ATOM    328  N   SER A  44      15.636   8.623  -5.921  1.00 24.34           N  
-ANISOU  328  N   SER A  44     3099   2955   3194    -27   -232   -407       N  
-ATOM    329  CA  SER A  44      15.703   9.735  -6.882  1.00 25.49           C  
-ANISOU  329  CA  SER A  44     3263   3126   3298     -9   -234   -396       C  
-ATOM    330  C   SER A  44      16.151   9.290  -8.289  1.00 25.57           C  
-ANISOU  330  C   SER A  44     3329   3147   3237     26   -262   -420       C  
-ATOM    331  O   SER A  44      16.633  10.089  -9.090  1.00 24.51           O  
-ANISOU  331  O   SER A  44     3217   3046   3051     47   -248   -404       O  
-ATOM    332  CB  SER A  44      16.631  10.837  -6.347  1.00 24.96           C  
-ANISOU  332  CB  SER A  44     3187   3084   3214    -11   -176   -367       C  
-ATOM    333  OG  SER A  44      17.982  10.397  -6.254  1.00 25.90           O  
-ANISOU  333  OG  SER A  44     3318   3226   3295      0   -139   -368       O  
-ATOM    334  N   CYS A  45      15.973   8.009  -8.590  1.00 25.73           N  
-ANISOU  334  N   CYS A  45     3382   3138   3255     35   -306   -457       N  
-ATOM    335  CA  CYS A  45      16.221   7.483  -9.924  1.00 28.87           C  
-ANISOU  335  CA  CYS A  45     3850   3539   3580     80   -345   -490       C  
-ATOM    336  C   CYS A  45      15.409   8.246 -11.006  1.00 25.48           C  
-ANISOU  336  C   CYS A  45     3437   3116   3127     84   -393   -483       C  
-ATOM    337  O   CYS A  45      14.181   8.359 -10.916  1.00 29.48           O  
-ANISOU  337  O   CYS A  45     3914   3596   3691     49   -447   -475       O  
-ATOM    338  CB  CYS A  45      15.888   5.977  -9.940  1.00 31.31           C  
-ANISOU  338  CB  CYS A  45     4200   3790   3904     81   -409   -534       C  
-ATOM    339  SG  CYS A  45      16.136   5.113 -11.498  1.00 40.12           S  
-ANISOU  339  SG  CYS A  45     5432   4891   4923    149   -473   -591       S  
-ATOM    340  N   GLY A  46      16.096   8.798 -12.001  1.00 20.64           N  
-ANISOU  340  N   GLY A  46     2864   2548   2431    127   -370   -476       N  
-ATOM    341  CA  GLY A  46      15.441   9.546 -13.075  1.00 24.61           C  
-ANISOU  341  CA  GLY A  46     3390   3061   2901    136   -414   -464       C  
-ATOM    342  C   GLY A  46      14.996  10.966 -12.729  1.00 24.82           C  
-ANISOU  342  C   GLY A  46     3363   3098   2968    105   -394   -414       C  
-ATOM    343  O   GLY A  46      14.312  11.630 -13.524  1.00 24.14           O  
-ANISOU  343  O   GLY A  46     3291   3014   2867    110   -437   -400       O  
-ATOM    344  N   ALA A  47      15.391  11.441 -11.547  1.00 25.62           N  
-ANISOU  344  N   ALA A  47     3414   3203   3119     78   -335   -388       N  
-ATOM    345  CA  ALA A  47      14.960  12.744 -11.038  1.00 24.58           C  
-ANISOU  345  CA  ALA A  47     3244   3067   3029     55   -321   -348       C  
-ATOM    346  C   ALA A  47      15.420  13.942 -11.872  1.00 22.73           C  
-ANISOU  346  C   ALA A  47     3037   2860   2738     67   -308   -308       C  
-ATOM    347  O   ALA A  47      16.595  14.062 -12.221  1.00 21.00           O  
-ANISOU  347  O   ALA A  47     2836   2679   2462     77   -265   -288       O  
-ATOM    348  CB  ALA A  47      15.452  12.931  -9.575  1.00 18.42           C  
-ANISOU  348  CB  ALA A  47     2423   2280   2296     30   -264   -336       C  
-ATOM    349  N   THR A  48      14.492  14.856 -12.149  1.00 21.02           N  
-ANISOU  349  N   THR A  48     2816   2627   2542     66   -345   -288       N  
-ATOM    350  CA  THR A  48      14.869  16.198 -12.578  1.00 19.89           C  
-ANISOU  350  CA  THR A  48     2694   2494   2369     66   -332   -238       C  
-ATOM    351  C   THR A  48      15.417  16.970 -11.387  1.00 18.83           C  
-ANISOU  351  C   THR A  48     2537   2342   2275     38   -287   -212       C  
-ATOM    352  O   THR A  48      15.182  16.596 -10.232  1.00 16.86           O  
-ANISOU  352  O   THR A  48     2255   2071   2080     28   -271   -235       O  
-ATOM    353  CB  THR A  48      13.693  16.997 -13.120  1.00 21.35           C  
-ANISOU  353  CB  THR A  48     2885   2658   2570     79   -389   -223       C  
-ATOM    354  OG1 THR A  48      12.778  17.211 -12.049  1.00 20.51           O  
-ANISOU  354  OG1 THR A  48     2731   2517   2543     75   -395   -231       O  
-ATOM    355  CG2 THR A  48      12.999  16.275 -14.253  1.00 22.69           C  
-ANISOU  355  CG2 THR A  48     3079   2837   2706    101   -452   -250       C  
-ATOM    356  N   PRO A  49      16.117  18.075 -11.660  1.00 19.72           N  
-ANISOU  356  N   PRO A  49     2674   2460   2360     23   -273   -161       N  
-ATOM    357  CA  PRO A  49      16.513  18.979 -10.575  1.00 18.39           C  
-ANISOU  357  CA  PRO A  49     2502   2257   2230     -6   -254   -137       C  
-ATOM    358  C   PRO A  49      15.310  19.430  -9.721  1.00 20.53           C  
-ANISOU  358  C   PRO A  49     2763   2476   2563     12   -277   -159       C  
-ATOM    359  O   PRO A  49      15.450  19.578  -8.508  1.00 17.92           O  
-ANISOU  359  O   PRO A  49     2423   2119   2268      2   -256   -169       O  
-ATOM    360  CB  PRO A  49      17.130  20.154 -11.319  1.00 21.89           C  
-ANISOU  360  CB  PRO A  49     2980   2704   2634    -27   -262    -71       C  
-ATOM    361  CG  PRO A  49      17.730  19.490 -12.568  1.00 22.76           C  
-ANISOU  361  CG  PRO A  49     3095   2883   2669    -12   -245    -57       C  
-ATOM    362  CD  PRO A  49      16.699  18.460 -12.955  1.00 20.51           C  
-ANISOU  362  CD  PRO A  49     2808   2599   2384     30   -274   -119       C  
-ATOM    363  N   GLN A  50      14.151  19.649 -10.340  1.00 20.00           N  
-ANISOU  363  N   GLN A  50     2697   2399   2504     43   -320   -164       N  
-ATOM    364  CA  GLN A  50      12.949  19.983  -9.575  1.00 20.20           C  
-ANISOU  364  CA  GLN A  50     2698   2391   2586     75   -335   -180       C  
-ATOM    365  C   GLN A  50      12.592  18.888  -8.566  1.00 20.72           C  
-ANISOU  365  C   GLN A  50     2710   2468   2694     75   -309   -216       C  
-ATOM    366  O   GLN A  50      12.276  19.177  -7.399  1.00 20.84           O  
-ANISOU  366  O   GLN A  50     2710   2463   2746     90   -286   -223       O  
-ATOM    367  CB  GLN A  50      11.769  20.212 -10.515  1.00 21.08           C  
-ANISOU  367  CB  GLN A  50     2804   2505   2701    109   -390   -173       C  
-ATOM    368  CG  GLN A  50      10.480  20.663  -9.807  1.00 24.03           C  
-ANISOU  368  CG  GLN A  50     3142   2857   3132    154   -402   -177       C  
-ATOM    369  CD  GLN A  50       9.294  20.679 -10.742  1.00 25.80           C  
-ANISOU  369  CD  GLN A  50     3341   3095   3367    185   -461   -167       C  
-ATOM    370  OE1 GLN A  50       8.955  19.664 -11.342  1.00 30.18           O  
-ANISOU  370  OE1 GLN A  50     3868   3680   3921    169   -491   -182       O  
-ATOM    371  NE2 GLN A  50       8.671  21.835 -10.888  1.00 27.73           N  
-ANISOU  371  NE2 GLN A  50     3604   3312   3620    229   -488   -143       N  
-ATOM    372  N   ASP A  51      12.623  17.635  -9.024  1.00 21.47           N  
-ANISOU  372  N   ASP A  51     2784   2594   2781     61   -315   -238       N  
-ATOM    373  CA  ASP A  51      12.328  16.482  -8.162  1.00 20.14           C  
-ANISOU  373  CA  ASP A  51     2567   2431   2652     51   -298   -265       C  
-ATOM    374  C   ASP A  51      13.323  16.385  -7.009  1.00 18.55           C  
-ANISOU  374  C   ASP A  51     2370   2225   2454     33   -243   -270       C  
-ATOM    375  O   ASP A  51      12.946  16.080  -5.878  1.00 19.54           O  
-ANISOU  375  O   ASP A  51     2462   2344   2617     35   -219   -279       O  
-ATOM    376  CB  ASP A  51      12.347  15.166  -8.957  1.00 20.97           C  
-ANISOU  376  CB  ASP A  51     2673   2555   2741     39   -328   -290       C  
-ATOM    377  CG  ASP A  51      11.229  15.078  -9.977  1.00 27.49           C  
-ANISOU  377  CG  ASP A  51     3493   3382   3572     51   -398   -289       C  
-ATOM    378  OD1 ASP A  51      10.166  15.698  -9.751  1.00 29.14           O  
-ANISOU  378  OD1 ASP A  51     3663   3584   3824     68   -417   -270       O  
-ATOM    379  OD2 ASP A  51      11.415  14.382 -11.005  1.00 25.53           O  
-ANISOU  379  OD2 ASP A  51     3279   3140   3280     50   -436   -308       O  
-ATOM    380  N   LEU A  52      14.594  16.627  -7.308  1.00 16.68           N  
-ANISOU  380  N   LEU A  52     2170   1997   2172     13   -224   -258       N  
-ATOM    381  CA  LEU A  52      15.633  16.602  -6.278  1.00 19.27           C  
-ANISOU  381  CA  LEU A  52     2500   2322   2501    -10   -183   -255       C  
-ATOM    382  C   LEU A  52      15.397  17.679  -5.220  1.00 19.97           C  
-ANISOU  382  C   LEU A  52     2603   2371   2614     -3   -176   -247       C  
-ATOM    383  O   LEU A  52      15.489  17.405  -4.008  1.00 20.43           O  
-ANISOU  383  O   LEU A  52     2649   2420   2692     -5   -150   -261       O  
-ATOM    384  CB  LEU A  52      17.024  16.748  -6.922  1.00 17.61           C  
-ANISOU  384  CB  LEU A  52     2313   2138   2240    -32   -168   -229       C  
-ATOM    385  CG  LEU A  52      17.443  15.538  -7.765  1.00 19.96           C  
-ANISOU  385  CG  LEU A  52     2605   2477   2501    -21   -163   -245       C  
-ATOM    386  CD1 LEU A  52      18.563  15.859  -8.795  1.00 24.60           C  
-ANISOU  386  CD1 LEU A  52     3212   3110   3025    -24   -147   -207       C  
-ATOM    387  CD2 LEU A  52      17.888  14.394  -6.864  1.00 19.68           C  
-ANISOU  387  CD2 LEU A  52     2545   2446   2485    -27   -135   -272       C  
-ATOM    388  N   ASN A  53      15.059  18.892  -5.650  1.00 19.36           N  
-ANISOU  388  N   ASN A  53     2560   2267   2530     12   -203   -226       N  
-ATOM    389  CA  ASN A  53      14.722  19.934  -4.683  1.00 20.36           C  
-ANISOU  389  CA  ASN A  53     2717   2346   2673     34   -206   -225       C  
-ATOM    390  C   ASN A  53      13.480  19.595  -3.877  1.00 19.38           C  
-ANISOU  390  C   ASN A  53     2553   2225   2585     83   -190   -250       C  
-ATOM    391  O   ASN A  53      13.395  19.887  -2.675  1.00 21.11           O  
-ANISOU  391  O   ASN A  53     2786   2423   2812    106   -168   -262       O  
-ATOM    392  CB  ASN A  53      14.556  21.283  -5.391  1.00 22.94           C  
-ANISOU  392  CB  ASN A  53     3097   2635   2986     46   -246   -197       C  
-ATOM    393  CG  ASN A  53      15.888  21.851  -5.825  1.00 22.26           C  
-ANISOU  393  CG  ASN A  53     3051   2539   2868    -11   -258   -156       C  
-ATOM    394  OD1 ASN A  53      16.909  21.580  -5.187  1.00 23.81           O  
-ANISOU  394  OD1 ASN A  53     3245   2740   3060    -51   -238   -153       O  
-ATOM    395  ND2 ASN A  53      15.903  22.585  -6.936  1.00 19.14           N  
-ANISOU  395  ND2 ASN A  53     2684   2136   2450    -17   -290   -118       N  
-ATOM    396  N   THR A  54      12.519  18.951  -4.525  1.00 19.00           N  
-ANISOU  396  N   THR A  54     2454   2207   2557     99   -203   -252       N  
-ATOM    397  CA  THR A  54      11.313  18.537  -3.821  1.00 20.49           C  
-ANISOU  397  CA  THR A  54     2585   2415   2787    138   -188   -259       C  
-ATOM    398  C   THR A  54      11.653  17.616  -2.663  1.00 20.61           C  
-ANISOU  398  C   THR A  54     2574   2445   2814    119   -143   -272       C  
-ATOM    399  O   THR A  54      11.173  17.809  -1.531  1.00 20.11           O  
-ANISOU  399  O   THR A  54     2497   2382   2762    157   -110   -273       O  
-ATOM    400  CB  THR A  54      10.314  17.816  -4.759  1.00 19.94           C  
-ANISOU  400  CB  THR A  54     2456   2377   2744    137   -223   -251       C  
-ATOM    401  OG1 THR A  54       9.774  18.762  -5.684  1.00 21.90           O  
-ANISOU  401  OG1 THR A  54     2724   2614   2984    168   -265   -235       O  
-ATOM    402  CG2 THR A  54       9.172  17.225  -3.947  1.00 21.27           C  
-ANISOU  402  CG2 THR A  54     2544   2575   2961    160   -204   -242       C  
-ATOM    403  N   MET A  55      12.467  16.599  -2.949  1.00 21.22           N  
-ANISOU  403  N   MET A  55     2646   2536   2882     70   -142   -281       N  
-ATOM    404  CA  MET A  55      12.802  15.615  -1.929  1.00 20.78           C  
-ANISOU  404  CA  MET A  55     2565   2491   2837     50   -107   -290       C  
-ATOM    405  C   MET A  55      13.560  16.268  -0.795  1.00 19.56           C  
-ANISOU  405  C   MET A  55     2455   2314   2662     56    -76   -295       C  
-ATOM    406  O   MET A  55      13.299  15.985   0.374  1.00 20.45           O  
-ANISOU  406  O   MET A  55     2553   2434   2785     72    -43   -298       O  
-ATOM    407  CB  MET A  55      13.618  14.467  -2.530  1.00 20.37           C  
-ANISOU  407  CB  MET A  55     2513   2451   2774      8   -117   -301       C  
-ATOM    408  CG  MET A  55      12.830  13.613  -3.532  1.00 22.45           C  
-ANISOU  408  CG  MET A  55     2747   2727   3058      1   -159   -304       C  
-ATOM    409  SD  MET A  55      13.899  12.420  -4.399  1.00 32.84           S  
-ANISOU  409  SD  MET A  55     4092   4046   4338    -25   -176   -327       S  
-ATOM    410  CE  MET A  55      14.339  11.330  -3.041  1.00 27.17           C  
-ANISOU  410  CE  MET A  55     3354   3325   3645    -45   -139   -334       C  
-ATOM    411  N   LEU A  56      14.486  17.165  -1.138  1.00 17.26           N  
-ANISOU  411  N   LEU A  56     2222   1998   2340     41    -93   -291       N  
-ATOM    412  CA  LEU A  56      15.280  17.836  -0.122  1.00 18.54           C  
-ANISOU  412  CA  LEU A  56     2434   2127   2481     36    -84   -293       C  
-ATOM    413  C   LEU A  56      14.394  18.751   0.730  1.00 20.92           C  
-ANISOU  413  C   LEU A  56     2766   2401   2783     98    -78   -303       C  
-ATOM    414  O   LEU A  56      14.574  18.850   1.960  1.00 24.21           O  
-ANISOU  414  O   LEU A  56     3209   2803   3185    115    -57   -316       O  
-ATOM    415  CB  LEU A  56      16.430  18.630  -0.768  1.00 19.04           C  
-ANISOU  415  CB  LEU A  56     2545   2169   2519     -6   -115   -273       C  
-ATOM    416  CG  LEU A  56      17.542  17.817  -1.460  1.00 23.05           C  
-ANISOU  416  CG  LEU A  56     3027   2715   3014    -55   -109   -258       C  
-ATOM    417  CD1 LEU A  56      18.589  18.749  -2.068  1.00 21.90           C  
-ANISOU  417  CD1 LEU A  56     2917   2559   2846    -95   -135   -219       C  
-ATOM    418  CD2 LEU A  56      18.218  16.833  -0.508  1.00 22.26           C  
-ANISOU  418  CD2 LEU A  56     2906   2634   2919    -73    -81   -269       C  
-ATOM    419  N   ASN A  57      13.432  19.404   0.076  1.00 18.24           N  
-ANISOU  419  N   ASN A  57     2423   2055   2453    140    -96   -296       N  
-ATOM    420  CA  ASN A  57      12.530  20.321   0.749  1.00 18.55           C  
-ANISOU  420  CA  ASN A  57     2491   2071   2488    219    -89   -304       C  
-ATOM    421  C   ASN A  57      11.515  19.636   1.673  1.00 19.81           C  
-ANISOU  421  C   ASN A  57     2587   2278   2664    270    -37   -305       C  
-ATOM    422  O   ASN A  57      10.964  20.288   2.572  1.00 20.25           O  
-ANISOU  422  O   ASN A  57     2671   2323   2701    346    -14   -315       O  
-ATOM    423  CB  ASN A  57      11.775  21.183  -0.278  1.00 18.71           C  
-ANISOU  423  CB  ASN A  57     2519   2074   2514    256   -126   -291       C  
-ATOM    424  CG  ASN A  57      12.591  22.381  -0.765  1.00 20.04           C  
-ANISOU  424  CG  ASN A  57     2780   2176   2657    233   -176   -283       C  
-ATOM    425  OD1 ASN A  57      13.472  22.878  -0.058  1.00 21.58           O  
-ANISOU  425  OD1 ASN A  57     3044   2324   2829    212   -187   -292       O  
-ATOM    426  ND2 ASN A  57      12.289  22.857  -1.985  1.00 20.98           N  
-ANISOU  426  ND2 ASN A  57     2902   2290   2782    232   -214   -261       N  
-ATOM    427  N   THR A  58      11.243  18.346   1.462  1.00 20.06           N  
-ANISOU  427  N   THR A  58     2535   2361   2728    233    -21   -292       N  
-ATOM    428  CA  THR A  58      10.217  17.708   2.275  1.00 24.09           C  
-ANISOU  428  CA  THR A  58     2972   2922   3261    272     26   -276       C  
-ATOM    429  C   THR A  58      10.800  17.282   3.609  1.00 26.38           C  
-ANISOU  429  C   THR A  58     3284   3214   3526    268     68   -286       C  
-ATOM    430  O   THR A  58      10.060  16.875   4.506  1.00 28.83           O  
-ANISOU  430  O   THR A  58     3546   3567   3841    307    117   -268       O  
-ATOM    431  CB  THR A  58       9.543  16.483   1.586  1.00 27.95           C  
-ANISOU  431  CB  THR A  58     3362   3456   3800    229     15   -249       C  
-ATOM    432  OG1 THR A  58      10.525  15.531   1.171  1.00 23.34           O  
-ANISOU  432  OG1 THR A  58     2789   2863   3218    152     -5   -261       O  
-ATOM    433  CG2 THR A  58       8.706  16.924   0.386  1.00 31.26           C  
-ANISOU  433  CG2 THR A  58     3752   3882   4244    246    -29   -235       C  
-ATOM    434  N   VAL A  59      12.118  17.398   3.744  1.00 24.05           N  
-ANISOU  434  N   VAL A  59     3057   2879   3202    222     50   -307       N  
-ATOM    435  CA  VAL A  59      12.770  17.191   5.035  1.00 27.23           C  
-ANISOU  435  CA  VAL A  59     3499   3276   3573    222     77   -319       C  
-ATOM    436  C   VAL A  59      12.463  18.353   5.978  1.00 24.30           C  
-ANISOU  436  C   VAL A  59     3202   2876   3157    304     90   -338       C  
-ATOM    437  O   VAL A  59      12.793  19.511   5.697  1.00 26.10           O  
-ANISOU  437  O   VAL A  59     3510   3046   3363    320     48   -356       O  
-ATOM    438  CB  VAL A  59      14.307  17.050   4.916  1.00 27.53           C  
-ANISOU  438  CB  VAL A  59     3583   3282   3596    149     46   -330       C  
-ATOM    439  CG1 VAL A  59      14.911  16.801   6.295  1.00 28.82           C  
-ANISOU  439  CG1 VAL A  59     3783   3440   3727    150     67   -340       C  
-ATOM    440  CG2 VAL A  59      14.686  15.931   3.948  1.00 27.48           C  
-ANISOU  440  CG2 VAL A  59     3518   3302   3622     85     35   -318       C  
-ATOM    441  N   GLY A  60      11.836  18.030   7.100  1.00 24.85           N  
-ANISOU  441  N   GLY A  60     3250   2983   3208    361    145   -331       N  
-ATOM    442  CA  GLY A  60      11.426  19.023   8.070  1.00 27.28           C  
-ANISOU  442  CA  GLY A  60     3632   3273   3461    462    167   -352       C  
-ATOM    443  C   GLY A  60      12.535  19.449   9.021  1.00 30.67           C  
-ANISOU  443  C   GLY A  60     4175   3645   3831    453    143   -387       C  
-ATOM    444  O   GLY A  60      12.722  20.637   9.258  1.00 31.52           O  
-ANISOU  444  O   GLY A  60     4391   3687   3897    500    106   -419       O  
-ATOM    445  N   GLY A  61      13.274  18.497   9.576  1.00 30.34           N  
-ANISOU  445  N   GLY A  61     4117   3622   3787    393    154   -380       N  
-ATOM    446  CA  GLY A  61      14.274  18.866  10.577  1.00 32.78           C  
-ANISOU  446  CA  GLY A  61     4531   3883   4039    387    126   -409       C  
-ATOM    447  C   GLY A  61      15.651  19.078   9.971  1.00 27.51           C  
-ANISOU  447  C   GLY A  61     3903   3161   3389    288     52   -415       C  
-ATOM    448  O   GLY A  61      15.760  19.453   8.804  1.00 25.93           O  
-ANISOU  448  O   GLY A  61     3686   2941   3224    251     17   -406       O  
-ATOM    449  N   HIS A  62      16.691  18.844  10.769  1.00 23.52           N  
-ANISOU  449  N   HIS A  62     3443   2637   2856    246     28   -422       N  
-ATOM    450  CA  HIS A  62      18.062  18.791  10.265  1.00 23.56           C  
-ANISOU  450  CA  HIS A  62     3453   2614   2883    146    -32   -411       C  
-ATOM    451  C   HIS A  62      18.477  20.000   9.432  1.00 19.90           C  
-ANISOU  451  C   HIS A  62     3046   2086   2429    116   -102   -412       C  
-ATOM    452  O   HIS A  62      19.177  19.846   8.440  1.00 17.90           O  
-ANISOU  452  O   HIS A  62     2747   1840   2213     41   -127   -384       O  
-ATOM    453  CB  HIS A  62      18.233  17.526   9.416  1.00 24.92           C  
-ANISOU  453  CB  HIS A  62     3511   2847   3112     88     -3   -380       C  
-ATOM    454  CG  HIS A  62      17.817  16.274  10.116  1.00 27.58           C  
-ANISOU  454  CG  HIS A  62     3790   3239   3451    104     56   -369       C  
-ATOM    455  ND1 HIS A  62      18.478  15.787  11.224  1.00 33.17           N  
-ANISOU  455  ND1 HIS A  62     4525   3950   4128     93     57   -370       N  
-ATOM    456  CD2 HIS A  62      16.810  15.404   9.865  1.00 30.15           C  
-ANISOU  456  CD2 HIS A  62     4033   3617   3808    125    109   -350       C  
-ATOM    457  CE1 HIS A  62      17.894  14.673  11.627  1.00 32.71           C  
-ANISOU  457  CE1 HIS A  62     4405   3943   4081    107    113   -350       C  
-ATOM    458  NE2 HIS A  62      16.879  14.419  10.820  1.00 31.76           N  
-ANISOU  458  NE2 HIS A  62     4216   3851   4001    123    143   -337       N  
-ATOM    459  N   GLN A  63      18.028  21.192   9.812  1.00 21.83           N  
-ANISOU  459  N   GLN A  63     3392   2268   2636    179   -132   -440       N  
-ATOM    460  CA  GLN A  63      18.251  22.364   8.976  1.00 22.91           C  
-ANISOU  460  CA  GLN A  63     3585   2336   2784    155   -200   -436       C  
-ATOM    461  C   GLN A  63      19.717  22.858   8.996  1.00 22.24           C  
-ANISOU  461  C   GLN A  63     3555   2193   2700     54   -289   -417       C  
-ATOM    462  O   GLN A  63      20.152  23.571   8.090  1.00 20.23           O  
-ANISOU  462  O   GLN A  63     3315   1900   2472     -2   -344   -389       O  
-ATOM    463  CB  GLN A  63      17.281  23.472   9.397  1.00 24.08           C  
-ANISOU  463  CB  GLN A  63     3833   2427   2890    265   -209   -474       C  
-ATOM    464  CG  GLN A  63      15.843  23.125   8.981  1.00 23.53           C  
-ANISOU  464  CG  GLN A  63     3681   2423   2837    352   -130   -471       C  
-ATOM    465  CD  GLN A  63      15.758  22.937   7.474  1.00 27.28           C  
-ANISOU  465  CD  GLN A  63     4068   2924   3373    295   -135   -434       C  
-ATOM    466  OE1 GLN A  63      16.039  23.870   6.708  1.00 28.42           O  
-ANISOU  466  OE1 GLN A  63     4263   3008   3527    268   -196   -425       O  
-ATOM    467  NE2 GLN A  63      15.422  21.720   7.035  1.00 24.19           N  
-ANISOU  467  NE2 GLN A  63     3554   2617   3019    272    -78   -411       N  
-ATOM    468  N   ALA A  64      20.475  22.486  10.024  1.00 21.50           N  
-ANISOU  468  N   ALA A  64     3490   2097   2581     27   -306   -425       N  
-ATOM    469  CA  ALA A  64      21.914  22.738   9.994  1.00 21.77           C  
-ANISOU  469  CA  ALA A  64     3543   2098   2630    -82   -388   -392       C  
-ATOM    470  C   ALA A  64      22.534  21.953   8.836  1.00 22.98           C  
-ANISOU  470  C   ALA A  64     3565   2324   2840   -160   -361   -337       C  
-ATOM    471  O   ALA A  64      23.230  22.517   7.995  1.00 22.29           O  
-ANISOU  471  O   ALA A  64     3470   2219   2781   -233   -412   -293       O  
-ATOM    472  CB  ALA A  64      22.570  22.363  11.336  1.00 20.34           C  
-ANISOU  472  CB  ALA A  64     3406   1911   2411    -92   -411   -408       C  
-ATOM    473  N   ALA A  65      22.259  20.655   8.783  1.00 24.55           N  
-ANISOU  473  N   ALA A  65     3669   2607   3053   -140   -282   -336       N  
-ATOM    474  CA  ALA A  65      22.721  19.843   7.668  1.00 22.30           C  
-ANISOU  474  CA  ALA A  65     3272   2390   2810   -190   -251   -296       C  
-ATOM    475  C   ALA A  65      22.294  20.423   6.338  1.00 22.60           C  
-ANISOU  475  C   ALA A  65     3294   2423   2869   -192   -254   -277       C  
-ATOM    476  O   ALA A  65      23.090  20.470   5.412  1.00 23.26           O  
-ANISOU  476  O   ALA A  65     3333   2529   2973   -254   -272   -231       O  
-ATOM    477  CB  ALA A  65      22.213  18.427   7.794  1.00 17.98           C  
-ANISOU  477  CB  ALA A  65     2648   1913   2272   -153   -174   -308       C  
-ATOM    478  N   MET A  66      21.037  20.852   6.237  1.00 18.11           N  
-ANISOU  478  N   MET A  66     2757   1833   2293   -119   -234   -308       N  
-ATOM    479  CA  MET A  66      20.516  21.306   4.942  1.00 19.12           C  
-ANISOU  479  CA  MET A  66     2864   1961   2439   -114   -235   -291       C  
-ATOM    480  C   MET A  66      21.221  22.557   4.514  1.00 20.07           C  
-ANISOU  480  C   MET A  66     3050   2017   2560   -170   -312   -258       C  
-ATOM    481  O   MET A  66      21.448  22.761   3.321  1.00 21.50           O  
-ANISOU  481  O   MET A  66     3196   2216   2759   -207   -320   -217       O  
-ATOM    482  CB  MET A  66      18.994  21.544   4.993  1.00 17.06           C  
-ANISOU  482  CB  MET A  66     2619   1692   2172    -19   -202   -326       C  
-ATOM    483  CG  MET A  66      18.177  20.260   5.125  1.00 22.00           C  
-ANISOU  483  CG  MET A  66     3157   2390   2810     22   -128   -339       C  
-ATOM    484  SD  MET A  66      18.595  18.980   3.902  1.00 29.34           S  
-ANISOU  484  SD  MET A  66     3979   3392   3775    -34   -103   -310       S  
-ATOM    485  CE  MET A  66      20.004  18.204   4.693  1.00 48.19           C  
-ANISOU  485  CE  MET A  66     6355   5798   6155    -92   -103   -300       C  
-ATOM    486  N   GLN A  67      21.563  23.416   5.472  1.00 17.48           N  
-ANISOU  486  N   GLN A  67     2822   1611   2209   -177   -374   -273       N  
-ATOM    487  CA  GLN A  67      22.300  24.609   5.087  1.00 20.95           C  
-ANISOU  487  CA  GLN A  67     3327   1978   2656   -246   -463   -232       C  
-ATOM    488  C   GLN A  67      23.719  24.241   4.618  1.00 23.08           C  
-ANISOU  488  C   GLN A  67     3522   2297   2951   -357   -482   -162       C  
-ATOM    489  O   GLN A  67      24.236  24.839   3.675  1.00 23.67           O  
-ANISOU  489  O   GLN A  67     3584   2365   3045   -421   -518   -101       O  
-ATOM    490  CB  GLN A  67      22.351  25.641   6.240  1.00 24.29           C  
-ANISOU  490  CB  GLN A  67     3894   2290   3046   -230   -543   -268       C  
-ATOM    491  CG  GLN A  67      23.307  26.780   5.969  1.00 27.82           C  
-ANISOU  491  CG  GLN A  67     4410   2654   3507   -327   -654   -216       C  
-ATOM    492  CD  GLN A  67      22.884  27.646   4.802  1.00 32.59           C  
-ANISOU  492  CD  GLN A  67     5033   3221   4129   -330   -678   -184       C  
-ATOM    493  OE1 GLN A  67      21.712  27.682   4.435  1.00 32.60           O  
-ANISOU  493  OE1 GLN A  67     5036   3230   4122   -237   -629   -219       O  
-ATOM    494  NE2 GLN A  67      23.839  28.363   4.219  1.00 33.66           N  
-ANISOU  494  NE2 GLN A  67     5180   3320   4291   -440   -756   -108       N  
-ATOM    495  N   MET A  68      24.347  23.262   5.268  1.00 24.43           N  
-ANISOU  495  N   MET A  68     3638   2522   3122   -375   -455   -164       N  
-ATOM    496  CA  MET A  68      25.644  22.775   4.807  1.00 22.84           C  
-ANISOU  496  CA  MET A  68     3347   2386   2944   -461   -458    -96       C  
-ATOM    497  C   MET A  68      25.541  22.195   3.392  1.00 21.75           C  
-ANISOU  497  C   MET A  68     3112   2332   2820   -455   -394    -63       C  
-ATOM    498  O   MET A  68      26.422  22.399   2.555  1.00 19.27           O  
-ANISOU  498  O   MET A  68     2746   2055   2519   -520   -407     10       O  
-ATOM    499  CB  MET A  68      26.198  21.723   5.764  1.00 21.94           C  
-ANISOU  499  CB  MET A  68     3193   2318   2826   -461   -435   -111       C  
-ATOM    500  CG  MET A  68      26.737  22.301   7.047  1.00 27.25           C  
-ANISOU  500  CG  MET A  68     3952   2919   3482   -494   -517   -122       C  
-ATOM    501  SD  MET A  68      27.847  21.145   7.862  1.00 44.78           S  
-ANISOU  501  SD  MET A  68     6099   5207   5706   -529   -508   -102       S  
-ATOM    502  CE  MET A  68      26.676  19.981   8.473  1.00 21.35           C  
-ANISOU  502  CE  MET A  68     3127   2274   2713   -418   -411   -179       C  
-ATOM    503  N   LEU A  69      24.465  21.462   3.130  1.00 22.30           N  
-ANISOU  503  N   LEU A  69     3156   2433   2882   -376   -325   -112       N  
-ATOM    504  CA  LEU A  69      24.230  20.941   1.796  1.00 23.89           C  
-ANISOU  504  CA  LEU A  69     3288   2701   3089   -361   -275    -92       C  
-ATOM    505  C   LEU A  69      24.100  22.077   0.758  1.00 24.96           C  
-ANISOU  505  C   LEU A  69     3454   2804   3224   -385   -312    -51       C  
-ATOM    506  O   LEU A  69      24.646  21.994  -0.352  1.00 22.26           O  
-ANISOU  506  O   LEU A  69     3058   2519   2880   -416   -298      5       O  
-ATOM    507  CB  LEU A  69      22.980  20.042   1.805  1.00 22.40           C  
-ANISOU  507  CB  LEU A  69     3078   2535   2897   -279   -216   -153       C  
-ATOM    508  CG  LEU A  69      22.570  19.376   0.484  1.00 23.01           C  
-ANISOU  508  CG  LEU A  69     3096   2671   2974   -254   -174   -148       C  
-ATOM    509  CD1 LEU A  69      23.731  18.568  -0.124  1.00 20.62           C  
-ANISOU  509  CD1 LEU A  69     2724   2444   2665   -286   -149   -107       C  
-ATOM    510  CD2 LEU A  69      21.362  18.471   0.733  1.00 23.90           C  
-ANISOU  510  CD2 LEU A  69     3191   2796   3094   -189   -133   -202       C  
-ATOM    511  N   LYS A  70      23.375  23.136   1.107  1.00 25.34           N  
-ANISOU  511  N   LYS A  70     3593   2764   3269   -362   -358    -75       N  
-ATOM    512  CA  LYS A  70      23.246  24.281   0.211  1.00 26.68           C  
-ANISOU  512  CA  LYS A  70     3807   2890   3441   -385   -404    -33       C  
-ATOM    513  C   LYS A  70      24.603  24.891  -0.122  1.00 27.44           C  
-ANISOU  513  C   LYS A  70     3893   2985   3548   -492   -458     56       C  
-ATOM    514  O   LYS A  70      24.856  25.314  -1.265  1.00 24.36           O  
-ANISOU  514  O   LYS A  70     3480   2618   3159   -528   -463    121       O  
-ATOM    515  CB  LYS A  70      22.367  25.369   0.824  1.00 25.42           C  
-ANISOU  515  CB  LYS A  70     3762   2622   3275   -338   -456    -76       C  
-ATOM    516  CG  LYS A  70      20.897  25.085   0.760  1.00 26.64           C  
-ANISOU  516  CG  LYS A  70     3917   2784   3422   -233   -408   -137       C  
-ATOM    517  CD  LYS A  70      20.161  26.360   1.177  1.00 30.09           C  
-ANISOU  517  CD  LYS A  70     4471   3113   3848   -181   -465   -165       C  
-ATOM    518  CE  LYS A  70      18.679  26.176   1.155  1.00 27.63           C  
-ANISOU  518  CE  LYS A  70     4151   2816   3531    -69   -418   -215       C  
-ATOM    519  NZ  LYS A  70      18.056  27.335   1.877  1.00 26.52           N  
-ANISOU  519  NZ  LYS A  70     4132   2573   3371      2   -466   -252       N  
-ATOM    520  N   GLU A  71      25.471  24.942   0.883  1.00 24.74           N  
-ANISOU  520  N   GLU A  71     3566   2620   3215   -545   -499     65       N  
-ATOM    521  CA  GLU A  71      26.796  25.540   0.710  1.00 25.75           C  
-ANISOU  521  CA  GLU A  71     3676   2746   3362   -659   -562    160       C  
-ATOM    522  C   GLU A  71      27.652  24.677  -0.220  1.00 26.10           C  
-ANISOU  522  C   GLU A  71     3587   2922   3409   -688   -496    229       C  
-ATOM    523  O   GLU A  71      28.382  25.203  -1.075  1.00 26.84           O  
-ANISOU  523  O   GLU A  71     3642   3045   3509   -759   -515    326       O  
-ATOM    524  CB  GLU A  71      27.477  25.760   2.077  1.00 23.89           C  
-ANISOU  524  CB  GLU A  71     3490   2453   3136   -707   -633    150       C  
-ATOM    525  CG  GLU A  71      26.920  27.011   2.795  1.00 29.20           C  
-ANISOU  525  CG  GLU A  71     4318   2978   3800   -698   -728    109       C  
-ATOM    526  CD  GLU A  71      27.631  27.392   4.104  1.00 36.06           C  
-ANISOU  526  CD  GLU A  71     5262   3771   4669   -752   -822    100       C  
-ATOM    527  OE1 GLU A  71      28.755  26.913   4.377  1.00 38.31           O  
-ANISOU  527  OE1 GLU A  71     5471   4113   4972   -827   -835    152       O  
-ATOM    528  OE2 GLU A  71      27.042  28.190   4.873  1.00 37.57           O  
-ANISOU  528  OE2 GLU A  71     5594   3845   4837   -712   -887     39       O  
-ATOM    529  N   THR A  72      27.534  23.360  -0.078  1.00 22.40           N  
-ANISOU  529  N   THR A  72     3051   2531   2928   -628   -417    183       N  
-ATOM    530  CA  THR A  72      28.214  22.427  -0.974  1.00 21.34           C  
-ANISOU  530  CA  THR A  72     2804   2520   2784   -624   -346    231       C  
-ATOM    531  C   THR A  72      27.691  22.552  -2.404  1.00 21.72           C  
-ANISOU  531  C   THR A  72     2840   2605   2809   -592   -308    252       C  
-ATOM    532  O   THR A  72      28.463  22.604  -3.365  1.00 25.13           O  
-ANISOU  532  O   THR A  72     3207   3113   3228   -626   -287    336       O  
-ATOM    533  CB  THR A  72      28.050  20.958  -0.493  1.00 22.82           C  
-ANISOU  533  CB  THR A  72     2945   2763   2963   -555   -279    164       C  
-ATOM    534  OG1 THR A  72      28.777  20.774   0.732  1.00 23.44           O  
-ANISOU  534  OG1 THR A  72     3020   2827   3058   -591   -312    164       O  
-ATOM    535  CG2 THR A  72      28.587  20.003  -1.539  1.00 20.70           C  
-ANISOU  535  CG2 THR A  72     2581   2610   2673   -526   -207    200       C  
-ATOM    536  N   ILE A  73      26.374  22.585  -2.552  1.00 24.64           N  
-ANISOU  536  N   ILE A  73     3265   2928   3169   -524   -299    179       N  
-ATOM    537  CA  ILE A  73      25.760  22.803  -3.865  1.00 24.77           C  
-ANISOU  537  CA  ILE A  73     3285   2966   3162   -492   -278    194       C  
-ATOM    538  C   ILE A  73      26.248  24.102  -4.539  1.00 27.08           C  
-ANISOU  538  C   ILE A  73     3602   3232   3456   -566   -331    289       C  
-ATOM    539  O   ILE A  73      26.582  24.116  -5.731  1.00 26.95           O  
-ANISOU  539  O   ILE A  73     3543   3285   3413   -575   -302    354       O  
-ATOM    540  CB  ILE A  73      24.231  22.819  -3.745  1.00 20.23           C  
-ANISOU  540  CB  ILE A  73     2768   2333   2587   -416   -278    109       C  
-ATOM    541  CG1 ILE A  73      23.726  21.407  -3.409  1.00 21.05           C  
-ANISOU  541  CG1 ILE A  73     2830   2480   2687   -350   -220     35       C  
-ATOM    542  CG2 ILE A  73      23.573  23.350  -5.041  1.00 24.13           C  
-ANISOU  542  CG2 ILE A  73     3281   2827   3060   -394   -283    132       C  
-ATOM    543  CD1 ILE A  73      22.311  21.351  -2.913  1.00 19.89           C  
-ANISOU  543  CD1 ILE A  73     2724   2282   2552   -284   -221    -40       C  
-ATOM    544  N   ASN A  74      26.290  25.192  -3.788  1.00 25.30           N  
-ANISOU  544  N   ASN A  74     3452   2902   3257   -618   -412    299       N  
-ATOM    545  CA  ASN A  74      26.739  26.446  -4.356  1.00 29.04           C  
-ANISOU  545  CA  ASN A  74     3959   3333   3740   -698   -477    393       C  
-ATOM    546  C   ASN A  74      28.202  26.381  -4.788  1.00 29.03           C  
-ANISOU  546  C   ASN A  74     3864   3422   3743   -788   -469    512       C  
-ATOM    547  O   ASN A  74      28.571  26.996  -5.788  1.00 26.98           O  
-ANISOU  547  O   ASN A  74     3587   3191   3474   -836   -477    609       O  
-ATOM    548  CB  ASN A  74      26.520  27.594  -3.372  1.00 33.54           C  
-ANISOU  548  CB  ASN A  74     4647   3760   4338   -732   -579    373       C  
-ATOM    549  CG  ASN A  74      25.041  27.939  -3.194  1.00 39.87           C  
-ANISOU  549  CG  ASN A  74     5542   4477   5129   -636   -588    280       C  
-ATOM    550  OD1 ASN A  74      24.229  27.755  -4.104  1.00 40.96           O  
-ANISOU  550  OD1 ASN A  74     5666   4648   5248   -574   -546    265       O  
-ATOM    551  ND2 ASN A  74      24.689  28.440  -2.015  1.00 42.87           N  
-ANISOU  551  ND2 ASN A  74     6019   4752   5519   -617   -646    219       N  
-ATOM    552  N   GLU A  75      29.024  25.637  -4.042  1.00 25.16           N  
-ANISOU  552  N   GLU A  75     3309   2983   3266   -807   -450    512       N  
-ATOM    553  CA  GLU A  75      30.434  25.446  -4.385  1.00 29.10           C  
-ANISOU  553  CA  GLU A  75     3698   3586   3771   -881   -432    627       C  
-ATOM    554  C   GLU A  75      30.569  24.693  -5.711  1.00 27.97           C  
-ANISOU  554  C   GLU A  75     3468   3579   3580   -823   -331    663       C  
-ATOM    555  O   GLU A  75      31.357  25.080  -6.570  1.00 29.30           O  
-ANISOU  555  O   GLU A  75     3574   3821   3737   -877   -319    783       O  
-ATOM    556  CB  GLU A  75      31.186  24.667  -3.283  1.00 31.66           C  
-ANISOU  556  CB  GLU A  75     3970   3943   4117   -892   -429    607       C  
-ATOM    557  CG  GLU A  75      31.391  25.403  -1.961  1.00 39.17           C  
-ANISOU  557  CG  GLU A  75     4999   4777   5109   -964   -538    593       C  
-ATOM    558  CD  GLU A  75      31.749  24.465  -0.796  1.00 44.19           C  
-ANISOU  558  CD  GLU A  75     5605   5433   5753   -941   -526    537       C  
-ATOM    559  OE1 GLU A  75      31.963  23.255  -1.029  1.00 46.15           O  
-ANISOU  559  OE1 GLU A  75     5764   5787   5982   -879   -437    521       O  
-ATOM    560  OE2 GLU A  75      31.799  24.934   0.361  1.00 46.14           O  
-ANISOU  560  OE2 GLU A  75     5928   5583   6019   -980   -611    506       O  
-ATOM    561  N   GLU A  76      29.803  23.612  -5.864  1.00 24.61           N  
-ANISOU  561  N   GLU A  76     3041   3186   3122   -713   -261    563       N  
-ATOM    562  CA  GLU A  76      29.858  22.801  -7.086  1.00 26.48           C  
-ANISOU  562  CA  GLU A  76     3218   3541   3302   -643   -173    577       C  
-ATOM    563  C   GLU A  76      29.337  23.572  -8.297  1.00 22.46           C  
-ANISOU  563  C   GLU A  76     2748   3026   2760   -641   -178    620       C  
-ATOM    564  O   GLU A  76      29.845  23.430  -9.408  1.00 26.06           O  
-ANISOU  564  O   GLU A  76     3148   3586   3167   -628   -125    696       O  
-ATOM    565  CB  GLU A  76      29.073  21.495  -6.891  1.00 28.23           C  
-ANISOU  565  CB  GLU A  76     3450   3774   3504   -535   -120    454       C  
-ATOM    566  CG  GLU A  76      29.657  20.583  -5.804  1.00 29.15           C  
-ANISOU  566  CG  GLU A  76     3520   3910   3644   -528   -105    420       C  
-ATOM    567  CD  GLU A  76      31.154  20.279  -6.025  1.00 34.98           C  
-ANISOU  567  CD  GLU A  76     4151   4766   4375   -558    -68    521       C  
-ATOM    568  OE1 GLU A  76      31.519  19.704  -7.077  1.00 34.76           O  
-ANISOU  568  OE1 GLU A  76     4068   4845   4294   -502      2    555       O  
-ATOM    569  OE2 GLU A  76      31.963  20.619  -5.142  1.00 35.63           O  
-ANISOU  569  OE2 GLU A  76     4203   4836   4501   -634   -112    569       O  
-ATOM    570  N   ALA A  77      28.347  24.425  -8.066  1.00 21.75           N  
-ANISOU  570  N   ALA A  77     2755   2816   2692   -649   -243    577       N  
-ATOM    571  CA  ALA A  77      27.750  25.219  -9.134  1.00 26.43           C  
-ANISOU  571  CA  ALA A  77     3397   3388   3258   -645   -260    613       C  
-ATOM    572  C   ALA A  77      28.711  26.325  -9.594  1.00 28.08           C  
-ANISOU  572  C   ALA A  77     3586   3607   3476   -753   -300    761       C  
-ATOM    573  O   ALA A  77      28.805  26.631 -10.792  1.00 29.92           O  
-ANISOU  573  O   ALA A  77     3805   3899   3666   -754   -275    839       O  
-ATOM    574  CB  ALA A  77      26.421  25.825  -8.670  1.00 25.24           C  
-ANISOU  574  CB  ALA A  77     3353   3104   3132   -614   -321    527       C  
-ATOM    575  N   ALA A  78      29.413  26.926  -8.641  1.00 28.00           N  
-ANISOU  575  N   ALA A  78     3579   3539   3521   -848   -367    805       N  
-ATOM    576  CA  ALA A  78      30.449  27.894  -8.978  1.00 31.65           C  
-ANISOU  576  CA  ALA A  78     4007   4015   4003   -970   -413    959       C  
-ATOM    577  C   ALA A  78      31.531  27.250  -9.840  1.00 32.30           C  
-ANISOU  577  C   ALA A  78     3953   4274   4046   -973   -322   1065       C  
-ATOM    578  O   ALA A  78      32.001  27.847 -10.808  1.00 34.36           O  
-ANISOU  578  O   ALA A  78     4180   4592   4285  -1023   -314   1193       O  
-ATOM    579  CB  ALA A  78      31.057  28.489  -7.717  1.00 34.10           C  
-ANISOU  579  CB  ALA A  78     4342   4233   4381  -1072   -510    979       C  
-ATOM    580  N   GLU A  79      31.915  26.025  -9.490  1.00 33.66           N  
-ANISOU  580  N   GLU A  79     4050   4535   4205   -911   -250   1015       N  
-ATOM    581  CA  GLU A  79      32.938  25.297 -10.238  1.00 32.92           C  
-ANISOU  581  CA  GLU A  79     3827   4616   4065   -887   -154   1104       C  
-ATOM    582  C   GLU A  79      32.429  24.888 -11.624  1.00 30.86           C  
-ANISOU  582  C   GLU A  79     3572   4437   3716   -786    -73   1094       C  
-ATOM    583  O   GLU A  79      33.165  25.000 -12.597  1.00 30.37           O  
-ANISOU  583  O   GLU A  79     3436   4496   3607   -795    -18   1216       O  
-ATOM    584  CB  GLU A  79      33.413  24.073  -9.449  1.00 35.20           C  
-ANISOU  584  CB  GLU A  79     4049   4963   4362   -834   -107   1041       C  
-ATOM    585  CG  GLU A  79      34.328  23.122 -10.219  1.00 40.19           C  
-ANISOU  585  CG  GLU A  79     4559   5776   4935   -767      4   1104       C  
-ATOM    586  CD  GLU A  79      35.750  23.669 -10.452  1.00 42.86           C  
-ANISOU  586  CD  GLU A  79     4772   6223   5292   -866      9   1290       C  
-ATOM    587  OE1 GLU A  79      36.097  24.757  -9.934  1.00 40.72           O  
-ANISOU  587  OE1 GLU A  79     4507   5876   5088  -1004    -88   1372       O  
-ATOM    588  OE2 GLU A  79      36.523  22.995 -11.164  1.00 45.99           O  
-ANISOU  588  OE2 GLU A  79     5061   6781   5632   -804    107   1358       O  
-ATOM    589  N   TRP A  80      31.176  24.431 -11.717  1.00 29.38           N  
-ANISOU  589  N   TRP A  80     3472   4187   3504   -692    -67    957       N  
-ATOM    590  CA  TRP A  80      30.554  24.197 -13.025  1.00 30.15           C  
-ANISOU  590  CA  TRP A  80     3600   4337   3520   -606    -17    943       C  
-ATOM    591  C   TRP A  80      30.682  25.428 -13.933  1.00 32.16           C  
-ANISOU  591  C   TRP A  80     3871   4593   3757   -676    -46   1071       C  
-ATOM    592  O   TRP A  80      31.053  25.307 -15.107  1.00 35.00           O  
-ANISOU  592  O   TRP A  80     4190   5069   4039   -641     20   1149       O  
-ATOM    593  CB  TRP A  80      29.069  23.815 -12.880  1.00 29.25           C  
-ANISOU  593  CB  TRP A  80     3585   4127   3404   -525    -41    790       C  
-ATOM    594  CG  TRP A  80      28.392  23.589 -14.216  1.00 30.13           C  
-ANISOU  594  CG  TRP A  80     3733   4282   3432   -442     -7    773       C  
-ATOM    595  CD1 TRP A  80      27.702  24.507 -14.959  1.00 31.20           C  
-ANISOU  595  CD1 TRP A  80     3935   4369   3549   -455    -49    803       C  
-ATOM    596  CD2 TRP A  80      28.346  22.361 -14.950  1.00 29.57           C  
-ANISOU  596  CD2 TRP A  80     3645   4308   3282   -331     67    720       C  
-ATOM    597  NE1 TRP A  80      27.225  23.921 -16.116  1.00 33.00           N  
-ANISOU  597  NE1 TRP A  80     4185   4663   3690   -361     -6    773       N  
-ATOM    598  CE2 TRP A  80      27.616  22.605 -16.134  1.00 31.83           C  
-ANISOU  598  CE2 TRP A  80     3992   4602   3501   -284     64    720       C  
-ATOM    599  CE3 TRP A  80      28.852  21.073 -14.719  1.00 30.60           C  
-ANISOU  599  CE3 TRP A  80     3725   4512   3388   -262    130    670       C  
-ATOM    600  CZ2 TRP A  80      27.386  21.614 -17.088  1.00 30.84           C  
-ANISOU  600  CZ2 TRP A  80     3883   4553   3282   -173    116    669       C  
-ATOM    601  CZ3 TRP A  80      28.617  20.087 -15.672  1.00 32.24           C  
-ANISOU  601  CZ3 TRP A  80     3953   4792   3505   -147    183    619       C  
-ATOM    602  CH2 TRP A  80      27.892  20.367 -16.841  1.00 29.77           C  
-ANISOU  602  CH2 TRP A  80     3706   4482   3123   -106    173    617       C  
-ATOM    603  N   ASP A  81      30.382  26.606 -13.388  1.00 30.99           N  
-ANISOU  603  N   ASP A  81     3789   4312   3675   -769   -145   1093       N  
-ATOM    604  CA  ASP A  81      30.416  27.848 -14.159  1.00 33.55           C  
-ANISOU  604  CA  ASP A  81     4146   4609   3992   -843   -191   1213       C  
-ATOM    605  C   ASP A  81      31.816  28.231 -14.590  1.00 36.20           C  
-ANISOU  605  C   ASP A  81     4374   5058   4323   -937   -165   1396       C  
-ATOM    606  O   ASP A  81      31.996  28.877 -15.621  1.00 38.43           O  
-ANISOU  606  O   ASP A  81     4651   5387   4565   -968   -156   1515       O  
-ATOM    607  CB  ASP A  81      29.807  29.000 -13.360  1.00 33.99           C  
-ANISOU  607  CB  ASP A  81     4309   4482   4124   -916   -314   1188       C  
-ATOM    608  CG  ASP A  81      28.322  28.860 -13.198  1.00 33.09           C  
-ANISOU  608  CG  ASP A  81     4299   4268   4006   -821   -337   1037       C  
-ATOM    609  OD1 ASP A  81      27.721  28.079 -13.968  1.00 29.90           O  
-ANISOU  609  OD1 ASP A  81     3891   3930   3539   -718   -273    978       O  
-ATOM    610  OD2 ASP A  81      27.755  29.523 -12.303  1.00 35.42           O  
-ANISOU  610  OD2 ASP A  81     4679   4419   4359   -846   -423    981       O  
-ATOM    611  N   ARG A  82      32.801  27.864 -13.782  1.00 38.37           N  
-ANISOU  611  N   ARG A  82     4559   5378   4642   -985   -157   1429       N  
-ATOM    612  CA  ARG A  82      34.191  28.091 -14.140  1.00 41.97           C  
-ANISOU  612  CA  ARG A  82     4885   5965   5098  -1069   -123   1611       C  
-ATOM    613  C   ARG A  82      34.554  27.205 -15.326  1.00 43.49           C  
-ANISOU  613  C   ARG A  82     4994   6347   5183   -958     14   1650       C  
-ATOM    614  O   ARG A  82      35.155  27.663 -16.299  1.00 43.94           O  
-ANISOU  614  O   ARG A  82     4990   6510   5196   -992     54   1804       O  
-ATOM    615  CB  ARG A  82      35.115  27.810 -12.956  1.00 41.85           C  
-ANISOU  615  CB  ARG A  82     4789   5957   5156  -1136   -150   1627       C  
-ATOM    616  CG  ARG A  82      36.588  27.937 -13.289  1.00 46.64           C  
-ANISOU  616  CG  ARG A  82     5236   6717   5767  -1218   -111   1822       C  
-ATOM    617  CD  ARG A  82      37.480  27.504 -12.134  1.00 49.79           C  
-ANISOU  617  CD  ARG A  82     5548   7136   6234  -1267   -135   1829       C  
-ATOM    618  NE  ARG A  82      37.695  26.058 -12.094  1.00 50.45           N  
-ANISOU  618  NE  ARG A  82     5560   7342   6269  -1129    -22   1748       N  
-ATOM    619  CZ  ARG A  82      38.579  25.407 -12.848  1.00 51.99           C  
-ANISOU  619  CZ  ARG A  82     5618   7732   6403  -1067     94   1844       C  
-ATOM    620  NH1 ARG A  82      39.333  26.067 -13.720  1.00 53.59           N  
-ANISOU  620  NH1 ARG A  82     5735   8039   6587  -1126    118   2019       N  
-ATOM    621  NH2 ARG A  82      38.703  24.090 -12.735  1.00 51.41           N  
-ANISOU  621  NH2 ARG A  82     5502   7744   6285   -932    183   1754       N  
-ATOM    622  N   LEU A  83      34.170  25.936 -15.241  1.00 41.83           N  
-ANISOU  622  N   LEU A  83     4788   6177   4928   -822     83   1510       N  
-ATOM    623  CA  LEU A  83      34.484  24.968 -16.285  1.00 45.62           C  
-ANISOU  623  CA  LEU A  83     5210   6825   5299   -694    208   1522       C  
-ATOM    624  C   LEU A  83      33.670  25.168 -17.569  1.00 45.10           C  
-ANISOU  624  C   LEU A  83     5225   6770   5139   -624    232   1512       C  
-ATOM    625  O   LEU A  83      34.180  24.944 -18.664  1.00 46.00           O  
-ANISOU  625  O   LEU A  83     5288   7034   5157   -565    321   1600       O  
-ATOM    626  CB  LEU A  83      34.274  23.548 -15.757  1.00 46.98           C  
-ANISOU  626  CB  LEU A  83     5382   7012   5455   -573    256   1368       C  
-ATOM    627  CG  LEU A  83      35.422  22.950 -14.949  1.00 47.85           C  
-ANISOU  627  CG  LEU A  83     5372   7202   5606   -589    288   1407       C  
-ATOM    628  CD1 LEU A  83      34.989  21.646 -14.304  1.00 45.89           C  
-ANISOU  628  CD1 LEU A  83     5156   6924   5355   -479    310   1239       C  
-ATOM    629  CD2 LEU A  83      36.629  22.735 -15.850  1.00 48.44           C  
-ANISOU  629  CD2 LEU A  83     5314   7480   5609   -556    394   1560       C  
-ATOM    630  N   HIS A  84      32.413  25.584 -17.441  1.00 43.80           N  
-ANISOU  630  N   HIS A  84     5188   6455   4999   -623    153   1408       N  
-ATOM    631  CA  HIS A  84      31.536  25.708 -18.607  1.00 42.96           C  
-ANISOU  631  CA  HIS A  84     5166   6351   4808   -551    164   1384       C  
-ATOM    632  C   HIS A  84      30.791  27.039 -18.637  1.00 43.31           C  
-ANISOU  632  C   HIS A  84     5302   6254   4900   -638     60   1413       C  
-ATOM    633  O   HIS A  84      29.572  27.070 -18.450  1.00 40.80           O  
-ANISOU  633  O   HIS A  84     5086   5818   4600   -597      4   1289       O  
-ATOM    634  CB  HIS A  84      30.511  24.566 -18.640  1.00 39.91           C  
-ANISOU  634  CB  HIS A  84     4850   5933   4380   -415    181   1199       C  
-ATOM    635  CG  HIS A  84      31.093  23.210 -18.383  1.00 40.57           C  
-ANISOU  635  CG  HIS A  84     4869   6113   4433   -326    261   1140       C  
-ATOM    636  ND1 HIS A  84      31.160  22.656 -17.122  1.00 41.20           N  
-ANISOU  636  ND1 HIS A  84     4927   6134   4592   -339    239   1056       N  
-ATOM    637  CD2 HIS A  84      31.621  22.291 -19.225  1.00 42.32           C  
-ANISOU  637  CD2 HIS A  84     5052   6481   4547   -214    360   1151       C  
-ATOM    638  CE1 HIS A  84      31.714  21.459 -17.196  1.00 41.56           C  
-ANISOU  638  CE1 HIS A  84     4921   6283   4588   -244    318   1022       C  
-ATOM    639  NE2 HIS A  84      32.003  21.213 -18.461  1.00 43.39           N  
-ANISOU  639  NE2 HIS A  84     5143   6638   4705   -163    392   1075       N  
-ATOM    640  N   PRO A  85      31.510  28.142 -18.884  1.00 47.25           N  
-ANISOU  640  N   PRO A  85     5766   6767   5422   -757     32   1583       N  
-ATOM    641  CA  PRO A  85      30.847  29.453 -18.951  1.00 50.57           C  
-ANISOU  641  CA  PRO A  85     6283   7044   5886   -838    -74   1619       C  
-ATOM    642  C   PRO A  85      29.756  29.482 -20.023  1.00 52.82           C  
-ANISOU  642  C   PRO A  85     6663   7318   6090   -745    -70   1567       C  
-ATOM    643  O   PRO A  85      29.937  28.878 -21.078  1.00 53.11           O  
-ANISOU  643  O   PRO A  85     6669   7492   6018   -660     19   1594       O  
-ATOM    644  CB  PRO A  85      31.993  30.411 -19.307  1.00 50.12           C  
-ANISOU  644  CB  PRO A  85     6152   7047   5844   -972    -82   1836       C  
-ATOM    645  CG  PRO A  85      33.020  29.547 -19.961  1.00 49.60           C  
-ANISOU  645  CG  PRO A  85     5955   7196   5696   -917     50   1918       C  
-ATOM    646  CD  PRO A  85      32.934  28.220 -19.260  1.00 48.20           C  
-ANISOU  646  CD  PRO A  85     5752   7043   5519   -814    100   1761       C  
-ATOM    647  N   VAL A  86      28.638  30.151 -19.752  1.00 54.29           N  
-ANISOU  647  N   VAL A  86     6961   7344   6321   -752   -165   1493       N  
-ATOM    648  CA  VAL A  86      27.580  30.253 -20.752  1.00 57.29           C  
-ANISOU  648  CA  VAL A  86     7427   7708   6632   -670   -175   1452       C  
-ATOM    649  C   VAL A  86      27.621  31.608 -21.434  1.00 60.95           C  
-ANISOU  649  C   VAL A  86     7939   8129   7092   -754   -234   1597       C  
-ATOM    650  O   VAL A  86      27.896  32.629 -20.808  1.00 61.17           O  
-ANISOU  650  O   VAL A  86     7987   8050   7205   -869   -316   1666       O  
-ATOM    651  CB  VAL A  86      26.172  30.026 -20.149  1.00 56.49           C  
-ANISOU  651  CB  VAL A  86     7415   7474   6574   -600   -237   1275       C  
-ATOM    652  CG1 VAL A  86      26.109  28.673 -19.451  1.00 55.26           C  
-ANISOU  652  CG1 VAL A  86     7215   7356   6426   -526   -185   1140       C  
-ATOM    653  CG2 VAL A  86      25.791  31.155 -19.195  1.00 55.44           C  
-ANISOU  653  CG2 VAL A  86     7351   7169   6547   -682   -348   1271       C  
-ATOM    654  N   HIS A  87      27.355  31.608 -22.731  1.00 66.02           N  
-ANISOU  654  N   HIS A  87     8606   8849   7631   -695   -198   1643       N  
-ATOM    655  CA  HIS A  87      27.401  32.838 -23.494  1.00 70.92           C  
-ANISOU  655  CA  HIS A  87     9271   9439   8235   -768   -247   1791       C  
-ATOM    656  C   HIS A  87      26.216  33.727 -23.164  1.00 72.10           C  
-ANISOU  656  C   HIS A  87     9546   9399   8451   -776   -370   1724       C  
-ATOM    657  O   HIS A  87      25.060  33.325 -23.318  1.00 71.14           O  
-ANISOU  657  O   HIS A  87     9487   9235   8306   -672   -387   1591       O  
-ATOM    658  CB  HIS A  87      27.449  32.538 -24.991  1.00 73.59           C  
-ANISOU  658  CB  HIS A  87     9605   9924   8431   -691   -169   1858       C  
-ATOM    659  CG  HIS A  87      28.831  32.570 -25.561  1.00 76.06           C  
-ANISOU  659  CG  HIS A  87     9809  10405   8687   -744    -78   2040       C  
-ATOM    660  ND1 HIS A  87      29.241  33.527 -26.463  1.00 78.40           N  
-ANISOU  660  ND1 HIS A  87    10107  10744   8939   -815    -82   2228       N  
-ATOM    661  CD2 HIS A  87      29.904  31.774 -25.341  1.00 76.41           C  
-ANISOU  661  CD2 HIS A  87     9731  10590   8712   -736     20   2074       C  
-ATOM    662  CE1 HIS A  87      30.505  33.314 -26.783  1.00 79.38           C  
-ANISOU  662  CE1 HIS A  87    10106  11036   9018   -849     15   2374       C  
-ATOM    663  NE2 HIS A  87      30.931  32.256 -26.117  1.00 78.07           N  
-ANISOU  663  NE2 HIS A  87     9862  10934   8867   -798     79   2282       N  
-ATOM    664  N   ALA A  88      26.519  34.934 -22.697  1.00 74.02           N  
-ANISOU  664  N   ALA A  88     9823   9527   8776   -900   -460   1820       N  
-ATOM    665  CA  ALA A  88      25.503  35.948 -22.470  1.00 75.08           C  
-ANISOU  665  CA  ALA A  88    10084   9478   8966   -907   -580   1783       C  
-ATOM    666  C   ALA A  88      24.992  36.446 -23.814  1.00 76.69           C  
-ANISOU  666  C   ALA A  88    10348   9705   9087   -872   -590   1857       C  
-ATOM    667  O   ALA A  88      25.470  36.016 -24.866  1.00 77.68           O  
-ANISOU  667  O   ALA A  88    10418   9988   9109   -846   -503   1939       O  
-ATOM    668  CB  ALA A  88      26.062  37.097 -21.644  1.00 76.35           C  
-ANISOU  668  CB  ALA A  88    10278   9504   9229  -1050   -681   1871       C  
-ATOM    669  N   GLY A  89      24.027  37.359 -23.777  1.00 76.75           N  
-ANISOU  669  N   GLY A  89    10472   9558   9133   -862   -696   1831       N  
-ATOM    670  CA  GLY A  89      23.387  37.835 -24.990  1.00 76.00           C  
-ANISOU  670  CA  GLY A  89    10446   9469   8964   -818   -719   1886       C  
-ATOM    671  C   GLY A  89      22.146  37.008 -25.263  1.00 73.93           C  
-ANISOU  671  C   GLY A  89    10211   9222   8656   -667   -703   1723       C  
-ATOM    672  O   GLY A  89      22.016  35.899 -24.741  1.00 73.56           O  
-ANISOU  672  O   GLY A  89    10109   9228   8613   -603   -646   1595       O  
-ATOM    673  N   PRO A  90      21.224  37.538 -26.081  1.00 71.90           N  
-ANISOU  673  N   PRO A  90    10039   8919   8359   -613   -760   1732       N  
-ATOM    674  CA  PRO A  90      19.977  36.811 -26.340  1.00 67.48           C  
-ANISOU  674  CA  PRO A  90     9505   8369   7767   -478   -763   1585       C  
-ATOM    675  C   PRO A  90      20.249  35.503 -27.076  1.00 60.99           C  
-ANISOU  675  C   PRO A  90     8615   7723   6834   -409   -657   1550       C  
-ATOM    676  O   PRO A  90      21.053  35.483 -28.014  1.00 61.30           O  
-ANISOU  676  O   PRO A  90     8629   7883   6779   -432   -597   1671       O  
-ATOM    677  CB  PRO A  90      19.179  37.783 -27.211  1.00 70.12           C  
-ANISOU  677  CB  PRO A  90     9939   8632   8072   -454   -848   1645       C  
-ATOM    678  CG  PRO A  90      20.226  38.589 -27.915  1.00 72.78           C  
-ANISOU  678  CG  PRO A  90    10279   9008   8366   -560   -839   1843       C  
-ATOM    679  CD  PRO A  90      21.347  38.745 -26.918  1.00 73.45           C  
-ANISOU  679  CD  PRO A  90    10304   9073   8530   -675   -820   1892       C  
-ATOM    680  N   ILE A  91      19.603  34.421 -26.659  1.00 53.72           N  
-ANISOU  680  N   ILE A  91     7669   6819   5922   -322   -636   1392       N  
-ATOM    681  CA  ILE A  91      19.837  33.156 -27.333  1.00 49.29           C  
-ANISOU  681  CA  ILE A  91     7063   6408   5256   -250   -549   1348       C  
-ATOM    682  C   ILE A  91      18.964  33.063 -28.578  1.00 46.60           C  
-ANISOU  682  C   ILE A  91     6789   6101   4816   -165   -582   1337       C  
-ATOM    683  O   ILE A  91      18.001  33.814 -28.733  1.00 43.80           O  
-ANISOU  683  O   ILE A  91     6502   5647   4493   -149   -673   1332       O  
-ATOM    684  CB  ILE A  91      19.573  31.956 -26.422  1.00 46.64           C  
-ANISOU  684  CB  ILE A  91     6676   6078   4967   -200   -518   1191       C  
-ATOM    685  CG1 ILE A  91      20.186  30.696 -27.041  1.00 45.35           C  
-ANISOU  685  CG1 ILE A  91     6466   6070   4694   -142   -421   1170       C  
-ATOM    686  CG2 ILE A  91      18.089  31.800 -26.153  1.00 44.10           C  
-ANISOU  686  CG2 ILE A  91     6398   5664   4694   -128   -596   1062       C  
-ATOM    687  CD1 ILE A  91      19.720  29.439 -26.424  1.00 42.52           C  
-ANISOU  687  CD1 ILE A  91     6080   5714   4363    -77   -406   1013       C  
-ATOM    688  N   ALA A  92      19.327  32.146 -29.468  1.00 44.72           N  
-ANISOU  688  N   ALA A  92     6536   6004   4453   -104   -509   1335       N  
-ATOM    689  CA  ALA A  92      18.618  31.957 -30.722  1.00 43.45           C  
-ANISOU  689  CA  ALA A  92     6443   5888   4177    -20   -538   1325       C  
-ATOM    690  C   ALA A  92      17.197  31.464 -30.466  1.00 39.60           C  
-ANISOU  690  C   ALA A  92     5988   5321   3737     53   -620   1171       C  
-ATOM    691  O   ALA A  92      16.977  30.592 -29.619  1.00 36.35           O  
-ANISOU  691  O   ALA A  92     5532   4893   3388     74   -608   1050       O  
-ATOM    692  CB  ALA A  92      19.374  30.981 -31.616  1.00 44.14           C  
-ANISOU  692  CB  ALA A  92     6514   6142   4114     41   -439   1341       C  
-ATOM    693  N   PRO A  93      16.226  32.050 -31.183  1.00 37.84           N  
-ANISOU  693  N   PRO A  93     5839   5050   3490     88   -708   1185       N  
-ATOM    694  CA  PRO A  93      14.803  31.699 -31.093  1.00 36.28           C  
-ANISOU  694  CA  PRO A  93     5665   4785   3333    156   -798   1062       C  
-ATOM    695  C   PRO A  93      14.553  30.201 -31.299  1.00 36.04           C  
-ANISOU  695  C   PRO A  93     5620   4829   3246    228   -777    939       C  
-ATOM    696  O   PRO A  93      14.934  29.628 -32.336  1.00 33.91           O  
-ANISOU  696  O   PRO A  93     5385   4662   2836    275   -741    955       O  
-ATOM    697  CB  PRO A  93      14.167  32.523 -32.221  1.00 38.00           C  
-ANISOU  697  CB  PRO A  93     5966   4987   3484    183   -877   1137       C  
-ATOM    698  CG  PRO A  93      15.064  33.715 -32.358  1.00 38.97           C  
-ANISOU  698  CG  PRO A  93     6105   5097   3602    102   -852   1297       C  
-ATOM    699  CD  PRO A  93      16.461  33.203 -32.070  1.00 39.65           C  
-ANISOU  699  CD  PRO A  93     6125   5280   3660     54   -732   1336       C  
-ATOM    700  N   GLY A  94      13.929  29.584 -30.297  1.00 37.17           N  
-ANISOU  700  N   GLY A  94     5715   4913   3493    237   -799    820       N  
-ATOM    701  CA  GLY A  94      13.498  28.201 -30.377  1.00 37.43           C  
-ANISOU  701  CA  GLY A  94     5739   4987   3497    296   -805    698       C  
-ATOM    702  C   GLY A  94      14.597  27.217 -30.064  1.00 36.28           C  
-ANISOU  702  C   GLY A  94     5552   4919   3314    293   -701    669       C  
-ATOM    703  O   GLY A  94      14.393  26.004 -30.154  1.00 37.80           O  
-ANISOU  703  O   GLY A  94     5746   5143   3471    343   -702    571       O  
-ATOM    704  N   GLN A  95      15.768  27.733 -29.694  1.00 35.54           N  
-ANISOU  704  N   GLN A  95     5422   4854   3230    235   -619    759       N  
-ATOM    705  CA  GLN A  95      16.920  26.877 -29.489  1.00 33.10           C  
-ANISOU  705  CA  GLN A  95     5067   4634   2876    238   -515    752       C  
-ATOM    706  C   GLN A  95      17.208  26.654 -28.019  1.00 31.62           C  
-ANISOU  706  C   GLN A  95     4801   4394   2818    186   -485    703       C  
-ATOM    707  O   GLN A  95      16.866  27.460 -27.155  1.00 31.14           O  
-ANISOU  707  O   GLN A  95     4722   4237   2873    131   -524    714       O  
-ATOM    708  CB  GLN A  95      18.166  27.454 -30.174  1.00 38.85           C  
-ANISOU  708  CB  GLN A  95     5792   5460   3509    211   -433    898       C  
-ATOM    709  CG  GLN A  95      17.979  27.789 -31.646  1.00 42.24           C  
-ANISOU  709  CG  GLN A  95     6303   5950   3798    260   -454    967       C  
-ATOM    710  CD  GLN A  95      17.401  26.633 -32.439  1.00 43.39           C  
-ANISOU  710  CD  GLN A  95     6511   6142   3835    367   -480    858       C  
-ATOM    711  OE1 GLN A  95      18.005  25.560 -32.531  1.00 43.85           O  
-ANISOU  711  OE1 GLN A  95     6559   6279   3821    422   -412    807       O  
-ATOM    712  NE2 GLN A  95      16.209  26.838 -32.994  1.00 42.60           N  
-ANISOU  712  NE2 GLN A  95     6478   5983   3723    399   -588    821       N  
-ATOM    713  N   MET A  96      17.865  25.542 -27.744  1.00 31.83           N  
-ANISOU  713  N   MET A  96     4791   4485   2818    212   -415    649       N  
-ATOM    714  CA  MET A  96      18.213  25.185 -26.385  1.00 29.76           C  
-ANISOU  714  CA  MET A  96     4457   4185   2665    169   -382    601       C  
-ATOM    715  C   MET A  96      19.390  26.020 -25.896  1.00 31.53           C  
-ANISOU  715  C   MET A  96     4629   4426   2924     87   -323    716       C  
-ATOM    716  O   MET A  96      20.400  26.145 -26.596  1.00 29.84           O  
-ANISOU  716  O   MET A  96     4404   4314   2621     84   -256    815       O  
-ATOM    717  CB  MET A  96      18.531  23.696 -26.324  1.00 31.14           C  
-ANISOU  717  CB  MET A  96     4617   4421   2795    230   -335    508       C  
-ATOM    718  CG  MET A  96      19.021  23.185 -24.990  1.00 32.07           C  
-ANISOU  718  CG  MET A  96     4661   4516   3008    194   -292    463       C  
-ATOM    719  SD  MET A  96      19.244  21.399 -25.083  1.00 43.65           S  
-ANISOU  719  SD  MET A  96     6133   6041   4411    279   -254    350       S  
-ATOM    720  CE  MET A  96      20.517  21.274 -26.343  1.00 42.82           C  
-ANISOU  720  CE  MET A  96     6047   6087   4136    339   -159    441       C  
-ATOM    721  N   ARG A  97      19.258  26.600 -24.699  1.00 29.85           N  
-ANISOU  721  N   ARG A  97     4385   4117   2838     20   -352    709       N  
-ATOM    722  CA  ARG A  97      20.337  27.388 -24.128  1.00 33.61           C  
-ANISOU  722  CA  ARG A  97     4818   4593   3361    -70   -316    813       C  
-ATOM    723  C   ARG A  97      21.240  26.477 -23.301  1.00 32.46           C  
-ANISOU  723  C   ARG A  97     4597   4498   3239    -79   -243    777       C  
-ATOM    724  O   ARG A  97      20.887  25.343 -23.015  1.00 34.86           O  
-ANISOU  724  O   ARG A  97     4891   4811   3542    -20   -231    665       O  
-ATOM    725  CB  ARG A  97      19.793  28.554 -23.282  1.00 33.56           C  
-ANISOU  725  CB  ARG A  97     4837   4448   3468   -132   -394    825       C  
-ATOM    726  CG  ARG A  97      18.963  28.150 -22.073  1.00 29.92           C  
-ANISOU  726  CG  ARG A  97     4364   3898   3107   -113   -429    699       C  
-ATOM    727  CD  ARG A  97      18.384  29.366 -21.329  1.00 32.19           C  
-ANISOU  727  CD  ARG A  97     4692   4051   3488   -151   -505    710       C  
-ATOM    728  NE  ARG A  97      17.702  28.976 -20.089  1.00 32.77           N  
-ANISOU  728  NE  ARG A  97     4747   4054   3649   -128   -522    599       N  
-ATOM    729  CZ  ARG A  97      18.296  28.891 -18.900  1.00 31.91           C  
-ANISOU  729  CZ  ARG A  97     4605   3918   3603   -172   -498    581       C  
-ATOM    730  NH1 ARG A  97      19.588  29.172 -18.769  1.00 31.34           N  
-ANISOU  730  NH1 ARG A  97     4507   3877   3524   -249   -464    666       N  
-ATOM    731  NH2 ARG A  97      17.598  28.519 -17.842  1.00 31.10           N  
-ANISOU  731  NH2 ARG A  97     4489   3760   3567   -141   -510    483       N  
-ATOM    732  N   GLU A  98      22.419  26.965 -22.951  1.00 31.11           N  
-ANISOU  732  N   GLU A  98     4371   4360   3087   -156   -200    881       N  
-ATOM    733  CA  GLU A  98      23.338  26.200 -22.126  1.00 30.38           C  
-ANISOU  733  CA  GLU A  98     4202   4317   3025   -170   -137    861       C  
-ATOM    734  C   GLU A  98      22.981  26.409 -20.651  1.00 31.18           C  
-ANISOU  734  C   GLU A  98     4295   4297   3255   -220   -187    793       C  
-ATOM    735  O   GLU A  98      22.702  27.527 -20.232  1.00 32.54           O  
-ANISOU  735  O   GLU A  98     4501   4370   3493   -283   -252    831       O  
-ATOM    736  CB  GLU A  98      24.798  26.605 -22.388  1.00 31.91           C  
-ANISOU  736  CB  GLU A  98     4326   4612   3185   -232    -71   1013       C  
-ATOM    737  CG  GLU A  98      25.228  26.641 -23.863  1.00 38.01           C  
-ANISOU  737  CG  GLU A  98     5106   5513   3824   -189    -15   1111       C  
-ATOM    738  CD  GLU A  98      26.310  27.686 -24.129  1.00 45.31           C  
-ANISOU  738  CD  GLU A  98     5979   6491   4747   -289      8   1300       C  
-ATOM    739  OE1 GLU A  98      27.493  27.296 -24.232  1.00 47.72           O  
-ANISOU  739  OE1 GLU A  98     6195   6925   5013   -293     97   1380       O  
-ATOM    740  OE2 GLU A  98      25.982  28.899 -24.236  1.00 46.98           O  
-ANISOU  740  OE2 GLU A  98     6237   6616   4998   -365    -64   1374       O  
-ATOM    741  N   PRO A  99      22.978  25.326 -19.862  1.00 31.42           N  
-ANISOU  741  N   PRO A  99     4289   4333   3315   -185   -158    692       N  
-ATOM    742  CA  PRO A  99      22.700  25.450 -18.425  1.00 29.94           C  
-ANISOU  742  CA  PRO A  99     4093   4044   3237   -226   -196    630       C  
-ATOM    743  C   PRO A  99      23.930  25.906 -17.629  1.00 30.08           C  
-ANISOU  743  C   PRO A  99     4056   4068   3304   -317   -179    712       C  
-ATOM    744  O   PRO A  99      25.033  25.410 -17.869  1.00 28.73           O  
-ANISOU  744  O   PRO A  99     3818   4006   3091   -323   -110    769       O  
-ATOM    745  CB  PRO A  99      22.281  24.028 -18.024  1.00 28.27           C  
-ANISOU  745  CB  PRO A  99     3864   3850   3026   -153   -169    504       C  
-ATOM    746  CG  PRO A  99      22.968  23.144 -19.006  1.00 32.52           C  
-ANISOU  746  CG  PRO A  99     4379   4514   3461    -96   -100    523       C  
-ATOM    747  CD  PRO A  99      23.021  23.922 -20.305  1.00 30.87           C  
-ANISOU  747  CD  PRO A  99     4206   4350   3173    -94   -103    618       C  
-ATOM    748  N   ARG A 100      23.744  26.853 -16.711  1.00 28.62           N  
-ANISOU  748  N   ARG A 100     3901   3770   3203   -384   -244    719       N  
-ATOM    749  CA  ARG A 100      24.798  27.175 -15.765  1.00 33.04           C  
-ANISOU  749  CA  ARG A 100     4417   4318   3820   -472   -247    775       C  
-ATOM    750  C   ARG A 100      24.477  26.493 -14.437  1.00 25.73           C  
-ANISOU  750  C   ARG A 100     3483   3338   2954   -450   -251    658       C  
-ATOM    751  O   ARG A 100      23.456  25.810 -14.322  1.00 23.05           O  
-ANISOU  751  O   ARG A 100     3167   2977   2614   -372   -249    549       O  
-ATOM    752  CB  ARG A 100      24.963  28.691 -15.605  1.00 45.14           C  
-ANISOU  752  CB  ARG A 100     6000   5754   5398   -568   -327    869       C  
-ATOM    753  CG  ARG A 100      23.702  29.456 -15.286  1.00 53.34           C  
-ANISOU  753  CG  ARG A 100     7138   6652   6477   -543   -409    803       C  
-ATOM    754  CD  ARG A 100      23.841  30.923 -15.726  1.00 60.79           C  
-ANISOU  754  CD  ARG A 100     8144   7521   7432   -619   -482    917       C  
-ATOM    755  NE  ARG A 100      24.356  31.791 -14.667  1.00 63.51           N  
-ANISOU  755  NE  ARG A 100     8522   7759   7851   -712   -554    951       N  
-ATOM    756  CZ  ARG A 100      25.646  32.038 -14.443  1.00 66.02           C  
-ANISOU  756  CZ  ARG A 100     8786   8110   8188   -819   -557   1058       C  
-ATOM    757  NH1 ARG A 100      26.581  31.476 -15.198  1.00 67.59           N  
-ANISOU  757  NH1 ARG A 100     8885   8459   8337   -839   -476   1146       N  
-ATOM    758  NH2 ARG A 100      26.003  32.849 -13.455  1.00 66.78           N  
-ANISOU  758  NH2 ARG A 100     8930   8090   8352   -904   -642   1078       N  
-ATOM    759  N   GLY A 101      25.343  26.671 -13.446  1.00 25.36           N  
-ANISOU  759  N   GLY A 101     3403   3273   2959   -522   -261    689       N  
-ATOM    760  CA  GLY A 101      25.215  25.953 -12.185  1.00 23.26           C  
-ANISOU  760  CA  GLY A 101     3124   2973   2740   -502   -257    591       C  
-ATOM    761  C   GLY A 101      23.832  26.089 -11.581  1.00 24.50           C  
-ANISOU  761  C   GLY A 101     3354   3023   2932   -449   -302    482       C  
-ATOM    762  O   GLY A 101      23.229  25.100 -11.164  1.00 26.19           O  
-ANISOU  762  O   GLY A 101     3555   3246   3151   -384   -274    385       O  
-ATOM    763  N   SER A 102      23.308  27.314 -11.571  1.00 25.87           N  
-ANISOU  763  N   SER A 102     3604   3096   3130   -473   -374    505       N  
-ATOM    764  CA  SER A 102      22.002  27.579 -10.971  1.00 26.06           C  
-ANISOU  764  CA  SER A 102     3695   3022   3187   -414   -415    413       C  
-ATOM    765  C   SER A 102      20.845  26.922 -11.724  1.00 23.63           C  
-ANISOU  765  C   SER A 102     3382   2748   2847   -322   -391    349       C  
-ATOM    766  O   SER A 102      19.780  26.684 -11.140  1.00 23.36           O  
-ANISOU  766  O   SER A 102     3366   2669   2841   -261   -402    264       O  
-ATOM    767  CB  SER A 102      21.750  29.092 -10.886  1.00 26.54           C  
-ANISOU  767  CB  SER A 102     3847   2964   3273   -451   -501    457       C  
-ATOM    768  OG  SER A 102      21.698  29.671 -12.177  1.00 29.03           O  
-ANISOU  768  OG  SER A 102     4180   3300   3551   -461   -515    536       O  
-ATOM    769  N   ASP A 103      21.024  26.665 -13.021  1.00 23.02           N  
-ANISOU  769  N   ASP A 103     3284   2752   2711   -311   -364    396       N  
-ATOM    770  CA  ASP A 103      20.004  25.946 -13.792  1.00 23.14           C  
-ANISOU  770  CA  ASP A 103     3298   2803   2691   -230   -351    337       C  
-ATOM    771  C   ASP A 103      20.015  24.467 -13.397  1.00 21.29           C  
-ANISOU  771  C   ASP A 103     3008   2626   2454   -190   -298    258       C  
-ATOM    772  O   ASP A 103      18.967  23.850 -13.244  1.00 24.48           O  
-ANISOU  772  O   ASP A 103     3412   3016   2874   -134   -307    179       O  
-ATOM    773  CB  ASP A 103      20.233  26.088 -15.309  1.00 25.06           C  
-ANISOU  773  CB  ASP A 103     3548   3116   2858   -224   -341    408       C  
-ATOM    774  CG  ASP A 103      20.092  27.536 -15.802  1.00 25.87           C  
-ANISOU  774  CG  ASP A 103     3712   3156   2962   -260   -400    490       C  
-ATOM    775  OD1 ASP A 103      19.086  28.208 -15.452  1.00 24.51           O  
-ANISOU  775  OD1 ASP A 103     3592   2888   2831   -234   -459    454       O  
-ATOM    776  OD2 ASP A 103      21.001  27.998 -16.526  1.00 27.77           O  
-ANISOU  776  OD2 ASP A 103     3947   3445   3161   -311   -387    596       O  
-ATOM    777  N   ILE A 104      21.212  23.915 -13.229  1.00 20.93           N  
-ANISOU  777  N   ILE A 104     2913   2647   2391   -221   -248    288       N  
-ATOM    778  CA  ILE A 104      21.378  22.510 -12.856  1.00 21.06           C  
-ANISOU  778  CA  ILE A 104     2884   2715   2404   -184   -200    221       C  
-ATOM    779  C   ILE A 104      20.817  22.256 -11.446  1.00 22.05           C  
-ANISOU  779  C   ILE A 104     3007   2772   2599   -181   -215    146       C  
-ATOM    780  O   ILE A 104      20.212  21.210 -11.180  1.00 24.60           O  
-ANISOU  780  O   ILE A 104     3313   3102   2931   -135   -201     71       O  
-ATOM    781  CB  ILE A 104      22.859  22.107 -12.949  1.00 22.52           C  
-ANISOU  781  CB  ILE A 104     3013   2988   2557   -214   -143    281       C  
-ATOM    782  CG1 ILE A 104      23.289  22.077 -14.423  1.00 25.08           C  
-ANISOU  782  CG1 ILE A 104     3333   3402   2793   -189   -111    345       C  
-ATOM    783  CG2 ILE A 104      23.143  20.756 -12.244  1.00 25.90           C  
-ANISOU  783  CG2 ILE A 104     3397   3448   2995   -182   -101    213       C  
-ATOM    784  CD1 ILE A 104      24.769  22.222 -14.604  1.00 28.13           C  
-ANISOU  784  CD1 ILE A 104     3661   3876   3152   -233    -62    448       C  
-ATOM    785  N   ALA A 105      21.002  23.230 -10.558  1.00 23.72           N  
-ANISOU  785  N   ALA A 105     3243   2914   2857   -229   -247    169       N  
-ATOM    786  CA  ALA A 105      20.494  23.137  -9.192  1.00 21.96           C  
-ANISOU  786  CA  ALA A 105     3030   2627   2688   -219   -260    104       C  
-ATOM    787  C   ALA A 105      19.012  23.488  -9.159  1.00 23.47           C  
-ANISOU  787  C   ALA A 105     3258   2759   2901   -163   -294     55       C  
-ATOM    788  O   ALA A 105      18.380  23.434  -8.106  1.00 25.19           O  
-ANISOU  788  O   ALA A 105     3483   2931   3156   -136   -299      2       O  
-ATOM    789  CB  ALA A 105      21.305  24.071  -8.242  1.00 20.27           C  
-ANISOU  789  CB  ALA A 105     2841   2354   2505   -286   -291    145       C  
-ATOM    790  N   GLY A 106      18.469  23.868 -10.319  1.00 24.55           N  
-ANISOU  790  N   GLY A 106     3415   2903   3009   -140   -317     78       N  
-ATOM    791  CA  GLY A 106      17.049  24.129 -10.457  1.00 25.97           C  
-ANISOU  791  CA  GLY A 106     3616   3043   3207    -82   -350     40       C  
-ATOM    792  C   GLY A 106      16.547  25.410  -9.817  1.00 27.77           C  
-ANISOU  792  C   GLY A 106     3903   3178   3469    -71   -397     45       C  
-ATOM    793  O   GLY A 106      15.354  25.531  -9.514  1.00 32.24           O  
-ANISOU  793  O   GLY A 106     4475   3713   4062     -9   -413      3       O  
-ATOM    794  N   THR A 107      17.437  26.374  -9.615  1.00 25.28           N  
-ANISOU  794  N   THR A 107     3634   2817   3154   -128   -422    100       N  
-ATOM    795  CA  THR A 107      17.054  27.643  -9.004  1.00 27.50           C  
-ANISOU  795  CA  THR A 107     3994   2992   3461   -117   -477    102       C  
-ATOM    796  C   THR A 107      16.641  28.672 -10.057  1.00 31.27           C  
-ANISOU  796  C   THR A 107     4526   3433   3923   -108   -530    155       C  
-ATOM    797  O   THR A 107      15.822  29.560  -9.798  1.00 32.91           O  
-ANISOU  797  O   THR A 107     4796   3559   4149    -57   -576    140       O  
-ATOM    798  CB  THR A 107      18.201  28.224  -8.151  1.00 31.24           C  
-ANISOU  798  CB  THR A 107     4507   3415   3948   -191   -500    134       C  
-ATOM    799  OG1 THR A 107      19.328  28.529  -8.986  1.00 32.62           O  
-ANISOU  799  OG1 THR A 107     4672   3621   4100   -276   -508    227       O  
-ATOM    800  CG2 THR A 107      18.624  27.221  -7.085  1.00 30.60           C  
-ANISOU  800  CG2 THR A 107     4376   3371   3881   -198   -453     85       C  
-ATOM    801  N   THR A 108      17.205  28.539 -11.252  1.00 29.08           N  
-ANISOU  801  N   THR A 108     4226   3217   3605   -148   -520    218       N  
-ATOM    802  CA  THR A 108      16.972  29.514 -12.309  1.00 30.22           C  
-ANISOU  802  CA  THR A 108     4423   3332   3726   -151   -569    283       C  
-ATOM    803  C   THR A 108      16.503  28.868 -13.600  1.00 29.14           C  
-ANISOU  803  C   THR A 108     4249   3279   3542   -114   -549    288       C  
-ATOM    804  O   THR A 108      16.518  29.504 -14.648  1.00 30.05           O  
-ANISOU  804  O   THR A 108     4400   3396   3623   -124   -579    354       O  
-ATOM    805  CB  THR A 108      18.250  30.329 -12.611  1.00 30.86           C  
-ANISOU  805  CB  THR A 108     4534   3396   3794   -250   -592    387       C  
-ATOM    806  OG1 THR A 108      19.287  29.439 -13.037  1.00 26.74           O  
-ANISOU  806  OG1 THR A 108     3937   2987   3238   -296   -528    423       O  
-ATOM    807  CG2 THR A 108      18.726  31.090 -11.363  1.00 32.61           C  
-ANISOU  807  CG2 THR A 108     4811   3517   4063   -296   -636    386       C  
-ATOM    808  N   SER A 109      16.101  27.603 -13.535  1.00 27.44           N  
-ANISOU  808  N   SER A 109     3972   3131   3323    -73   -506    220       N  
-ATOM    809  CA  SER A 109      15.572  26.933 -14.718  1.00 28.97           C  
-ANISOU  809  CA  SER A 109     4144   3393   3471    -34   -502    213       C  
-ATOM    810  C   SER A 109      14.154  26.433 -14.479  1.00 31.89           C  
-ANISOU  810  C   SER A 109     4489   3753   3875     38   -522    138       C  
-ATOM    811  O   SER A 109      13.778  26.129 -13.348  1.00 30.10           O  
-ANISOU  811  O   SER A 109     4235   3501   3699     56   -507     84       O  
-ATOM    812  CB  SER A 109      16.462  25.759 -15.116  1.00 29.21           C  
-ANISOU  812  CB  SER A 109     4127   3520   3453    -54   -443    211       C  
-ATOM    813  OG  SER A 109      16.508  24.799 -14.064  1.00 31.09           O  
-ANISOU  813  OG  SER A 109     4317   3767   3729    -49   -406    143       O  
-ATOM    814  N   THR A 110      13.372  26.339 -15.550  1.00 31.14           N  
-ANISOU  814  N   THR A 110     4399   3682   3750     76   -557    141       N  
-ATOM    815  CA  THR A 110      12.019  25.813 -15.447  1.00 29.16           C  
-ANISOU  815  CA  THR A 110     4111   3433   3535    136   -584     84       C  
-ATOM    816  C   THR A 110      12.023  24.289 -15.587  1.00 28.21           C  
-ANISOU  816  C   THR A 110     3938   3379   3400    134   -557     33       C  
-ATOM    817  O   THR A 110      13.013  23.706 -16.027  1.00 24.65           O  
-ANISOU  817  O   THR A 110     3492   2977   2896    104   -522     43       O  
-ATOM    818  CB  THR A 110      11.107  26.425 -16.519  1.00 27.49           C  
-ANISOU  818  CB  THR A 110     3930   3212   3304    177   -650    113       C  
-ATOM    819  OG1 THR A 110      11.537  25.992 -17.811  1.00 27.50           O  
-ANISOU  819  OG1 THR A 110     3950   3273   3225    162   -655    139       O  
-ATOM    820  CG2 THR A 110      11.141  27.950 -16.452  1.00 27.59           C  
-ANISOU  820  CG2 THR A 110     4008   3148   3328    180   -684    168       C  
-ATOM    821  N   LEU A 111      10.917  23.640 -15.228  1.00 28.90           N  
-ANISOU  821  N   LEU A 111     3975   3469   3535    168   -577    -15       N  
-ATOM    822  CA  LEU A 111      10.816  22.198 -15.425  1.00 27.63           C  
-ANISOU  822  CA  LEU A 111     3777   3357   3366    163   -572    -61       C  
-ATOM    823  C   LEU A 111      10.934  21.877 -16.916  1.00 26.43           C  
-ANISOU  823  C   LEU A 111     3665   3244   3133    169   -608    -49       C  
-ATOM    824  O   LEU A 111      11.579  20.904 -17.305  1.00 24.12           O  
-ANISOU  824  O   LEU A 111     3382   2992   2790    158   -587    -72       O  
-ATOM    825  CB  LEU A 111       9.501  21.651 -14.868  1.00 27.62           C  
-ANISOU  825  CB  LEU A 111     3710   3350   3435    189   -601    -98       C  
-ATOM    826  CG  LEU A 111       9.219  20.205 -15.297  1.00 29.67           C  
-ANISOU  826  CG  LEU A 111     3942   3645   3685    177   -626   -138       C  
-ATOM    827  CD1 LEU A 111      10.245  19.261 -14.695  1.00 28.34           C  
-ANISOU  827  CD1 LEU A 111     3770   3492   3507    145   -566   -168       C  
-ATOM    828  CD2 LEU A 111       7.788  19.753 -14.947  1.00 30.56           C  
-ANISOU  828  CD2 LEU A 111     3981   3758   3873    193   -673   -152       C  
-ATOM    829  N   GLN A 112      10.305  22.700 -17.750  1.00 28.63           N  
-ANISOU  829  N   GLN A 112     3975   3510   3392    194   -664    -14       N  
-ATOM    830  CA  GLN A 112      10.355  22.483 -19.190  1.00 29.91           C  
-ANISOU  830  CA  GLN A 112     4186   3710   3468    206   -704      0       C  
-ATOM    831  C   GLN A 112      11.791  22.529 -19.737  1.00 25.97           C  
-ANISOU  831  C   GLN A 112     3734   3253   2882    185   -647     37       C  
-ATOM    832  O   GLN A 112      12.158  21.718 -20.585  1.00 27.15           O  
-ANISOU  832  O   GLN A 112     3912   3452   2952    199   -645     20       O  
-ATOM    833  CB  GLN A 112       9.492  23.510 -19.914  1.00 37.83           C  
-ANISOU  833  CB  GLN A 112     5217   4689   4467    237   -773     42       C  
-ATOM    834  CG  GLN A 112       9.230  23.147 -21.362  1.00 43.47           C  
-ANISOU  834  CG  GLN A 112     5978   5441   5097    258   -832     46       C  
-ATOM    835  CD  GLN A 112       8.437  21.854 -21.494  1.00 50.78           C  
-ANISOU  835  CD  GLN A 112     6873   6382   6039    266   -885    -19       C  
-ATOM    836  OE1 GLN A 112       7.323  21.740 -20.974  1.00 55.03           O  
-ANISOU  836  OE1 GLN A 112     7349   6898   6662    274   -929    -36       O  
-ATOM    837  NE2 GLN A 112       9.014  20.868 -22.179  1.00 50.72           N  
-ANISOU  837  NE2 GLN A 112     6908   6413   5950    267   -881    -50       N  
-ATOM    838  N   GLU A 113      12.589  23.484 -19.275  1.00 24.79           N  
-ANISOU  838  N   GLU A 113     3593   3084   2743    154   -604     90       N  
-ATOM    839  CA  GLU A 113      13.997  23.560 -19.680  1.00 26.68           C  
-ANISOU  839  CA  GLU A 113     3855   3372   2910    124   -544    142       C  
-ATOM    840  C   GLU A 113      14.767  22.329 -19.182  1.00 26.87           C  
-ANISOU  840  C   GLU A 113     3842   3440   2926    118   -483     95       C  
-ATOM    841  O   GLU A 113      15.563  21.738 -19.921  1.00 26.97           O  
-ANISOU  841  O   GLU A 113     3871   3520   2854    131   -447    105       O  
-ATOM    842  CB  GLU A 113      14.650  24.846 -19.159  1.00 27.65           C  
-ANISOU  842  CB  GLU A 113     3988   3453   3063     77   -527    214       C  
-ATOM    843  CG  GLU A 113      14.079  26.137 -19.777  1.00 30.41           C  
-ANISOU  843  CG  GLU A 113     4390   3756   3409     85   -587    274       C  
-ATOM    844  CD  GLU A 113      14.592  27.411 -19.111  1.00 30.64           C  
-ANISOU  844  CD  GLU A 113     4443   3717   3483     36   -590    336       C  
-ATOM    845  OE1 GLU A 113      14.877  27.376 -17.895  1.00 28.34           O  
-ANISOU  845  OE1 GLU A 113     4126   3389   3253     12   -566    306       O  
-ATOM    846  OE2 GLU A 113      14.705  28.456 -19.804  1.00 31.80           O  
-ANISOU  846  OE2 GLU A 113     4642   3841   3601     21   -623    415       O  
-ATOM    847  N   GLN A 114      14.537  21.942 -17.928  1.00 25.70           N  
-ANISOU  847  N   GLN A 114     3648   3256   2861    104   -470     46       N  
-ATOM    848  CA  GLN A 114      15.176  20.732 -17.395  1.00 26.81           C  
-ANISOU  848  CA  GLN A 114     3757   3429   3002    101   -420     -1       C  
-ATOM    849  C   GLN A 114      14.852  19.492 -18.227  1.00 26.94           C  
-ANISOU  849  C   GLN A 114     3793   3482   2962    143   -444    -55       C  
-ATOM    850  O   GLN A 114      15.738  18.695 -18.541  1.00 26.94           O  
-ANISOU  850  O   GLN A 114     3803   3533   2900    159   -401    -66       O  
-ATOM    851  CB  GLN A 114      14.763  20.505 -15.944  1.00 24.87           C  
-ANISOU  851  CB  GLN A 114     3463   3135   2852     85   -413    -45       C  
-ATOM    852  CG  GLN A 114      15.224  21.624 -15.025  1.00 25.29           C  
-ANISOU  852  CG  GLN A 114     3513   3147   2950     48   -392     -3       C  
-ATOM    853  CD  GLN A 114      14.608  21.524 -13.644  1.00 24.68           C  
-ANISOU  853  CD  GLN A 114     3401   3021   2956     49   -390    -47       C  
-ATOM    854  OE1 GLN A 114      14.066  20.483 -13.257  1.00 20.97           O  
-ANISOU  854  OE1 GLN A 114     2894   2560   2514     64   -389   -101       O  
-ATOM    855  NE2 GLN A 114      14.681  22.608 -12.899  1.00 22.81           N  
-ANISOU  855  NE2 GLN A 114     3180   2730   2755     34   -394    -22       N  
-ATOM    856  N   ILE A 115      13.576  19.340 -18.567  1.00 26.25           N  
-ANISOU  856  N   ILE A 115     3712   3365   2897    164   -518    -88       N  
-ATOM    857  CA  ILE A 115      13.109  18.262 -19.433  1.00 27.47           C  
-ANISOU  857  CA  ILE A 115     3900   3537   3000    198   -570   -138       C  
-ATOM    858  C   ILE A 115      13.815  18.272 -20.803  1.00 26.06           C  
-ANISOU  858  C   ILE A 115     3792   3417   2692    234   -560   -112       C  
-ATOM    859  O   ILE A 115      14.292  17.229 -21.291  1.00 24.65           O  
-ANISOU  859  O   ILE A 115     3651   3273   2442    269   -549   -152       O  
-ATOM    860  CB  ILE A 115      11.578  18.363 -19.647  1.00 23.77           C  
-ANISOU  860  CB  ILE A 115     3421   3030   2582    205   -664   -156       C  
-ATOM    861  CG1 ILE A 115      10.822  17.998 -18.366  1.00 27.83           C  
-ANISOU  861  CG1 ILE A 115     3859   3504   3212    181   -670   -187       C  
-ATOM    862  CG2 ILE A 115      11.125  17.464 -20.800  1.00 25.26           C  
-ANISOU  862  CG2 ILE A 115     3664   3231   2701    235   -739   -196       C  
-ATOM    863  CD1 ILE A 115       9.330  17.854 -18.596  1.00 29.91           C  
-ANISOU  863  CD1 ILE A 115     4093   3745   3527    187   -764   -199       C  
-ATOM    864  N   GLY A 116      13.876  19.453 -21.409  1.00 26.19           N  
-ANISOU  864  N   GLY A 116     3833   3444   2676    232   -564    -43       N  
-ATOM    865  CA  GLY A 116      14.579  19.638 -22.671  1.00 29.85           C  
-ANISOU  865  CA  GLY A 116     4357   3972   3013    265   -543      3       C  
-ATOM    866  C   GLY A 116      16.030  19.180 -22.621  1.00 29.51           C  
-ANISOU  866  C   GLY A 116     4307   3998   2909    274   -447     21       C  
-ATOM    867  O   GLY A 116      16.501  18.504 -23.529  1.00 32.00           O  
-ANISOU  867  O   GLY A 116     4672   4374   3114    330   -429      8       O  
-ATOM    868  N   TRP A 117      16.746  19.545 -21.561  1.00 25.53           N  
-ANISOU  868  N   TRP A 117     3742   3486   2471    225   -386     53       N  
-ATOM    869  CA  TRP A 117      18.152  19.174 -21.455  1.00 26.64           C  
-ANISOU  869  CA  TRP A 117     3858   3699   2564    230   -295     83       C  
-ATOM    870  C   TRP A 117      18.298  17.661 -21.331  1.00 24.80           C  
-ANISOU  870  C   TRP A 117     3634   3482   2308    280   -283     -4       C  
-ATOM    871  O   TRP A 117      19.078  17.052 -22.038  1.00 23.51           O  
-ANISOU  871  O   TRP A 117     3499   3392   2042    338   -237     -2       O  
-ATOM    872  CB  TRP A 117      18.811  19.883 -20.268  1.00 26.80           C  
-ANISOU  872  CB  TRP A 117     3813   3697   2672    158   -252    133       C  
-ATOM    873  CG  TRP A 117      19.023  21.348 -20.509  1.00 26.11           C  
-ANISOU  873  CG  TRP A 117     3730   3601   2589    109   -258    235       C  
-ATOM    874  CD1 TRP A 117      19.433  21.943 -21.675  1.00 27.48           C  
-ANISOU  874  CD1 TRP A 117     3937   3834   2672    120   -245    318       C  
-ATOM    875  CD2 TRP A 117      18.813  22.407 -19.569  1.00 26.71           C  
-ANISOU  875  CD2 TRP A 117     3787   3598   2762     45   -284    265       C  
-ATOM    876  NE1 TRP A 117      19.497  23.309 -21.510  1.00 28.61           N  
-ANISOU  876  NE1 TRP A 117     4079   3935   2857     55   -266    404       N  
-ATOM    877  CE2 TRP A 117      19.122  23.618 -20.226  1.00 29.16           C  
-ANISOU  877  CE2 TRP A 117     4124   3915   3041     12   -293    368       C  
-ATOM    878  CE3 TRP A 117      18.398  22.447 -18.228  1.00 22.78           C  
-ANISOU  878  CE3 TRP A 117     3261   3026   2369     16   -301    216       C  
-ATOM    879  CZ2 TRP A 117      19.021  24.861 -19.589  1.00 29.43           C  
-ANISOU  879  CZ2 TRP A 117     4165   3869   3149    -49   -330    417       C  
-ATOM    880  CZ3 TRP A 117      18.305  23.675 -17.598  1.00 25.17           C  
-ANISOU  880  CZ3 TRP A 117     3572   3257   2735    -34   -330    261       C  
-ATOM    881  CH2 TRP A 117      18.613  24.870 -18.279  1.00 27.87           C  
-ANISOU  881  CH2 TRP A 117     3949   3594   3048    -66   -349    357       C  
-ATOM    882  N   MET A 118      17.481  17.070 -20.469  1.00 24.98           N  
-ANISOU  882  N   MET A 118     3636   3433   2420    263   -328    -78       N  
-ATOM    883  CA  MET A 118      17.586  15.664 -20.125  1.00 26.82           C  
-ANISOU  883  CA  MET A 118     3875   3661   2654    295   -325   -157       C  
-ATOM    884  C   MET A 118      17.163  14.730 -21.244  1.00 27.51           C  
-ANISOU  884  C   MET A 118     4047   3756   2650    364   -381   -218       C  
-ATOM    885  O   MET A 118      17.549  13.556 -21.258  1.00 28.32           O  
-ANISOU  885  O   MET A 118     4180   3867   2715    410   -371   -276       O  
-ATOM    886  CB  MET A 118      16.747  15.375 -18.875  1.00 27.89           C  
-ANISOU  886  CB  MET A 118     3963   3719   2916    248   -363   -204       C  
-ATOM    887  CG  MET A 118      17.308  16.031 -17.628  1.00 29.81           C  
-ANISOU  887  CG  MET A 118     4137   3951   3238    192   -306   -163       C  
-ATOM    888  SD  MET A 118      16.221  15.906 -16.194  1.00 27.59           S  
-ANISOU  888  SD  MET A 118     3803   3589   3092    148   -343   -206       S  
-ATOM    889  CE  MET A 118      16.315  14.152 -15.872  1.00 22.65           C  
-ANISOU  889  CE  MET A 118     3182   2956   2467    171   -346   -283       C  
-ATOM    890  N   THR A 119      16.383  15.238 -22.190  1.00 24.96           N  
-ANISOU  890  N   THR A 119     3772   3425   2285    375   -446   -206       N  
-ATOM    891  CA  THR A 119      15.864  14.378 -23.237  1.00 27.28           C  
-ANISOU  891  CA  THR A 119     4158   3715   2494    436   -519   -269       C  
-ATOM    892  C   THR A 119      16.425  14.761 -24.608  1.00 32.03           C  
-ANISOU  892  C   THR A 119     4830   4394   2945    501   -494   -226       C  
-ATOM    893  O   THR A 119      16.107  14.139 -25.616  1.00 30.79           O  
-ANISOU  893  O   THR A 119     4768   4242   2690    564   -552   -274       O  
-ATOM    894  CB  THR A 119      14.314  14.406 -23.272  1.00 32.68           C  
-ANISOU  894  CB  THR A 119     4846   4323   3249    402   -641   -303       C  
-ATOM    895  OG1 THR A 119      13.850  15.723 -23.589  1.00 32.43           O  
-ANISOU  895  OG1 THR A 119     4797   4295   3232    377   -658   -235       O  
-ATOM    896  CG2 THR A 119      13.756  14.009 -21.914  1.00 33.63           C  
-ANISOU  896  CG2 THR A 119     4887   4379   3511    343   -656   -334       C  
-ATOM    897  N   HIS A 120      17.282  15.771 -24.639  1.00 36.03           N  
-ANISOU  897  N   HIS A 120     5296   4963   3430    484   -409   -131       N  
-ATOM    898  CA  HIS A 120      17.887  16.185 -25.897  1.00 41.15           C  
-ANISOU  898  CA  HIS A 120     6000   5699   3935    542   -371    -70       C  
-ATOM    899  C   HIS A 120      18.796  15.092 -26.437  1.00 37.53           C  
-ANISOU  899  C   HIS A 120     5595   5313   3353    641   -313   -109       C  
-ATOM    900  O   HIS A 120      19.121  14.142 -25.730  1.00 37.50           O  
-ANISOU  900  O   HIS A 120     5572   5290   3385    655   -293   -169       O  
-ATOM    901  CB  HIS A 120      18.676  17.477 -25.716  1.00 44.87           C  
-ANISOU  901  CB  HIS A 120     6405   6221   4424    489   -292     53       C  
-ATOM    902  CG  HIS A 120      19.181  18.057 -26.999  1.00 50.97           C  
-ANISOU  902  CG  HIS A 120     7226   7085   5058    534   -257    136       C  
-ATOM    903  ND1 HIS A 120      20.508  18.000 -27.371  1.00 53.35           N  
-ANISOU  903  ND1 HIS A 120     7507   7501   5263    576   -146    206       N  
-ATOM    904  CD2 HIS A 120      18.537  18.699 -28.003  1.00 53.92           C  
-ANISOU  904  CD2 HIS A 120     7663   7457   5368    547   -315    169       C  
-ATOM    905  CE1 HIS A 120      20.661  18.589 -28.543  1.00 56.74           C  
-ANISOU  905  CE1 HIS A 120     7985   7999   5575    611   -133    281       C  
-ATOM    906  NE2 HIS A 120      19.479  19.021 -28.949  1.00 57.58           N  
-ANISOU  906  NE2 HIS A 120     8148   8034   5697    593   -237    257       N  
-ATOM    907  N   ASN A 121      19.203  15.225 -27.692  1.00 36.82           N  
-ANISOU  907  N   ASN A 121     5575   5307   3110    718   -287    -72       N  
-ATOM    908  CA  ASN A 121      20.179  14.302 -28.267  1.00 41.26           C  
-ANISOU  908  CA  ASN A 121     6188   5954   3534    832   -215    -96       C  
-ATOM    909  C   ASN A 121      21.367  15.058 -28.879  1.00 45.19           C  
-ANISOU  909  C   ASN A 121     6650   6590   3929    864    -93     31       C  
-ATOM    910  O   ASN A 121      21.224  15.733 -29.892  1.00 47.11           O  
-ANISOU  910  O   ASN A 121     6941   6880   4078    884   -100     91       O  
-ATOM    911  CB  ASN A 121      19.501  13.419 -29.317  1.00 44.51           C  
-ANISOU  911  CB  ASN A 121     6745   6339   3827    927   -306   -194       C  
-ATOM    912  CG  ASN A 121      20.361  12.232 -29.745  1.00 49.32           C  
-ANISOU  912  CG  ASN A 121     7427   7008   4303   1060   -251   -253       C  
-ATOM    913  OD1 ASN A 121      21.131  11.667 -28.953  1.00 49.45           O  
-ANISOU  913  OD1 ASN A 121     7386   7040   4363   1073   -180   -266       O  
-ATOM    914  ND2 ASN A 121      20.217  11.838 -31.004  1.00 50.51           N  
-ANISOU  914  ND2 ASN A 121     7713   7189   4288   1170   -287   -293       N  
-ATOM    915  N   PRO A 122      22.551  14.955 -28.261  1.00 45.68           N  
-ANISOU  915  N   PRO A 122     6622   6723   4011    864     18     82       N  
-ATOM    916  CA  PRO A 122      22.806  14.200 -27.038  1.00 44.03           C  
-ANISOU  916  CA  PRO A 122     6354   6466   3910    840     30     21       C  
-ATOM    917  C   PRO A 122      22.245  14.939 -25.828  1.00 40.19           C  
-ANISOU  917  C   PRO A 122     5783   5883   3605    700    -14     39       C  
-ATOM    918  O   PRO A 122      22.174  16.171 -25.836  1.00 36.14           O  
-ANISOU  918  O   PRO A 122     5227   5373   3130    623    -13    131       O  
-ATOM    919  CB  PRO A 122      24.331  14.131 -26.987  1.00 44.30           C  
-ANISOU  919  CB  PRO A 122     6313   6633   3887    888    168    104       C  
-ATOM    920  CG  PRO A 122      24.759  15.394 -27.652  1.00 44.68           C  
-ANISOU  920  CG  PRO A 122     6322   6771   3884    852    221    248       C  
-ATOM    921  CD  PRO A 122      23.786  15.569 -28.787  1.00 46.51           C  
-ANISOU  921  CD  PRO A 122     6673   6975   4023    892    141    216       C  
-ATOM    922  N   PRO A 123      21.839  14.196 -24.804  1.00 40.98           N  
-ANISOU  922  N   PRO A 123     5866   5895   3810    672    -55    -48       N  
-ATOM    923  CA  PRO A 123      21.262  14.848 -23.625  1.00 40.55           C  
-ANISOU  923  CA  PRO A 123     5737   5752   3916    554    -94    -38       C  
-ATOM    924  C   PRO A 123      22.322  15.509 -22.757  1.00 37.22           C  
-ANISOU  924  C   PRO A 123     5208   5374   3558    490    -10     52       C  
-ATOM    925  O   PRO A 123      23.468  15.059 -22.749  1.00 34.68           O  
-ANISOU  925  O   PRO A 123     4853   5139   3186    536     75     81       O  
-ATOM    926  CB  PRO A 123      20.598  13.689 -22.881  1.00 42.05           C  
-ANISOU  926  CB  PRO A 123     5946   5852   4177    557   -155   -154       C  
-ATOM    927  CG  PRO A 123      21.423  12.504 -23.258  1.00 41.61           C  
-ANISOU  927  CG  PRO A 123     5935   5852   4022    662   -108   -200       C  
-ATOM    928  CD  PRO A 123      21.870  12.730 -24.675  1.00 42.10           C  
-ANISOU  928  CD  PRO A 123     6061   6011   3924    750    -71   -158       C  
-ATOM    929  N   ILE A 124      21.932  16.571 -22.051  1.00 36.51           N  
-ANISOU  929  N   ILE A 124     5071   5226   3577    389    -39     98       N  
-ATOM    930  CA  ILE A 124      22.737  17.146 -20.984  1.00 33.43           C  
-ANISOU  930  CA  ILE A 124     4590   4841   3272    312     10    164       C  
-ATOM    931  C   ILE A 124      22.091  16.702 -19.661  1.00 31.07           C  
-ANISOU  931  C   ILE A 124     4268   4442   3095    270    -34     81       C  
-ATOM    932  O   ILE A 124      21.042  17.217 -19.275  1.00 28.09           O  
-ANISOU  932  O   ILE A 124     3901   3979   2792    225   -101     58       O  
-ATOM    933  CB  ILE A 124      22.819  18.696 -21.084  1.00 34.12           C  
-ANISOU  933  CB  ILE A 124     4654   4924   3388    231      3    275       C  
-ATOM    934  CG1 ILE A 124      23.659  19.122 -22.295  1.00 35.79           C  
-ANISOU  934  CG1 ILE A 124     4868   5250   3479    263     63    380       C  
-ATOM    935  CG2 ILE A 124      23.430  19.305 -19.811  1.00 31.00           C  
-ANISOU  935  CG2 ILE A 124     4180   4498   3100    138     21    325       C  
-ATOM    936  CD1 ILE A 124      22.954  19.016 -23.638  1.00 36.66           C  
-ANISOU  936  CD1 ILE A 124     5070   5379   3479    336     28    357       C  
-ATOM    937  N   PRO A 125      22.689  15.711 -18.980  1.00 29.99           N  
-ANISOU  937  N   PRO A 125     4101   4320   2976    294      5     39       N  
-ATOM    938  CA  PRO A 125      21.950  15.075 -17.879  1.00 26.99           C  
-ANISOU  938  CA  PRO A 125     3713   3848   2693    269    -41    -46       C  
-ATOM    939  C   PRO A 125      21.925  15.908 -16.601  1.00 25.63           C  
-ANISOU  939  C   PRO A 125     3481   3622   2634    178    -46    -13       C  
-ATOM    940  O   PRO A 125      22.558  15.511 -15.628  1.00 26.00           O  
-ANISOU  940  O   PRO A 125     3482   3672   2726    160    -13    -19       O  
-ATOM    941  CB  PRO A 125      22.715  13.759 -17.666  1.00 30.40           C  
-ANISOU  941  CB  PRO A 125     4140   4317   3092    332      3    -92       C  
-ATOM    942  CG  PRO A 125      24.136  14.099 -18.058  1.00 33.98           C  
-ANISOU  942  CG  PRO A 125     4547   4885   3478    353     92      0       C  
-ATOM    943  CD  PRO A 125      24.057  15.179 -19.129  1.00 31.92           C  
-ANISOU  943  CD  PRO A 125     4307   4666   3154    344     92     77       C  
-ATOM    944  N   VAL A 126      21.184  17.017 -16.584  1.00 24.83           N  
-ANISOU  944  N   VAL A 126     3390   3470   2574    130    -91     15       N  
-ATOM    945  CA  VAL A 126      21.252  17.949 -15.453  1.00 25.00           C  
-ANISOU  945  CA  VAL A 126     3373   3440   2686     54    -97     50       C  
-ATOM    946  C   VAL A 126      20.775  17.304 -14.152  1.00 23.02           C  
-ANISOU  946  C   VAL A 126     3100   3127   2518     41   -111    -21       C  
-ATOM    947  O   VAL A 126      21.248  17.662 -13.082  1.00 20.83           O  
-ANISOU  947  O   VAL A 126     2789   2829   2297     -6    -96     -2       O  
-ATOM    948  CB  VAL A 126      20.448  19.255 -15.719  1.00 21.04           C  
-ANISOU  948  CB  VAL A 126     2902   2884   2208     21   -150     86       C  
-ATOM    949  CG1 VAL A 126      21.100  20.055 -16.851  1.00 22.15           C  
-ANISOU  949  CG1 VAL A 126     3059   3086   2273     15   -132    181       C  
-ATOM    950  CG2 VAL A 126      18.980  18.973 -16.051  1.00 20.90           C  
-ANISOU  950  CG2 VAL A 126     2922   2817   2203     57   -214     19       C  
-ATOM    951  N   GLY A 127      19.860  16.343 -14.241  1.00 23.16           N  
-ANISOU  951  N   GLY A 127     3140   3117   2541     80   -144    -99       N  
-ATOM    952  CA  GLY A 127      19.448  15.605 -13.059  1.00 20.63           C  
-ANISOU  952  CA  GLY A 127     2795   2750   2294     69   -152   -157       C  
-ATOM    953  C   GLY A 127      20.582  14.796 -12.435  1.00 23.30           C  
-ANISOU  953  C   GLY A 127     3102   3123   2628     74    -99   -161       C  
-ATOM    954  O   GLY A 127      20.770  14.810 -11.209  1.00 21.59           O  
-ANISOU  954  O   GLY A 127     2852   2878   2474     38    -86   -164       O  
-ATOM    955  N   GLU A 128      21.330  14.071 -13.265  1.00 24.29           N  
-ANISOU  955  N   GLU A 128     3243   3311   2676    126    -67   -162       N  
-ATOM    956  CA  GLU A 128      22.469  13.287 -12.775  1.00 25.37           C  
-ANISOU  956  CA  GLU A 128     3347   3491   2802    146    -14   -161       C  
-ATOM    957  C   GLU A 128      23.581  14.177 -12.248  1.00 22.60           C  
-ANISOU  957  C   GLU A 128     2939   3181   2469     95     30    -78       C  
-ATOM    958  O   GLU A 128      24.222  13.854 -11.244  1.00 21.63           O  
-ANISOU  958  O   GLU A 128     2774   3058   2385     75     53    -76       O  
-ATOM    959  CB  GLU A 128      23.023  12.383 -13.875  1.00 29.22           C  
-ANISOU  959  CB  GLU A 128     3869   4042   3190    233     12   -178       C  
-ATOM    960  CG  GLU A 128      22.134  11.205 -14.162  1.00 34.04           C  
-ANISOU  960  CG  GLU A 128     4544   4601   3791    280    -41   -269       C  
-ATOM    961  CD  GLU A 128      21.645  10.544 -12.876  1.00 36.19           C  
-ANISOU  961  CD  GLU A 128     4795   4800   4156    243    -68   -316       C  
-ATOM    962  OE1 GLU A 128      22.484  10.004 -12.112  1.00 35.30           O  
-ANISOU  962  OE1 GLU A 128     4650   4703   4060    250    -28   -314       O  
-ATOM    963  OE2 GLU A 128      20.421  10.584 -12.622  1.00 37.23           O  
-ANISOU  963  OE2 GLU A 128     4937   4865   4344    208   -127   -347       O  
-ATOM    964  N   ILE A 129      23.832  15.286 -12.934  1.00 20.23           N  
-ANISOU  964  N   ILE A 129     2636   2912   2138     70     35     -5       N  
-ATOM    965  CA  ILE A 129      24.872  16.215 -12.481  1.00 22.28           C  
-ANISOU  965  CA  ILE A 129     2842   3203   2419      6     62     86       C  
-ATOM    966  C   ILE A 129      24.506  16.826 -11.123  1.00 22.67           C  
-ANISOU  966  C   ILE A 129     2885   3167   2563    -65     23     75       C  
-ATOM    967  O   ILE A 129      25.346  16.936 -10.224  1.00 20.12           O  
-ANISOU  967  O   ILE A 129     2519   2851   2276   -107     37    106       O  
-ATOM    968  CB  ILE A 129      25.104  17.351 -13.504  1.00 24.89           C  
-ANISOU  968  CB  ILE A 129     3180   3573   2705    -17     64    175       C  
-ATOM    969  CG1 ILE A 129      25.515  16.772 -14.857  1.00 26.68           C  
-ANISOU  969  CG1 ILE A 129     3417   3896   2823     64    110    191       C  
-ATOM    970  CG2 ILE A 129      26.194  18.312 -13.006  1.00 24.63           C  
-ANISOU  970  CG2 ILE A 129     3089   3565   2705   -100     77    279       C  
-ATOM    971  CD1 ILE A 129      25.339  17.749 -16.005  1.00 28.96           C  
-ANISOU  971  CD1 ILE A 129     3735   4212   3055     56    101    260       C  
-ATOM    972  N   TYR A 130      23.245  17.211 -10.960  1.00 19.10           N  
-ANISOU  972  N   TYR A 130     2475   2635   2145    -71    -27     30       N  
-ATOM    973  CA  TYR A 130      22.828  17.803  -9.685  1.00 20.96           C  
-ANISOU  973  CA  TYR A 130     2715   2792   2457   -119    -59     15       C  
-ATOM    974  C   TYR A 130      22.847  16.759  -8.554  1.00 19.74           C  
-ANISOU  974  C   TYR A 130     2538   2623   2340   -108    -45    -44       C  
-ATOM    975  O   TYR A 130      23.262  17.051  -7.424  1.00 20.74           O  
-ANISOU  975  O   TYR A 130     2651   2722   2509   -149    -48    -34       O  
-ATOM    976  CB  TYR A 130      21.440  18.421  -9.832  1.00 22.64           C  
-ANISOU  976  CB  TYR A 130     2972   2938   2693   -110   -108    -16       C  
-ATOM    977  CG  TYR A 130      20.943  19.231  -8.650  1.00 21.78           C  
-ANISOU  977  CG  TYR A 130     2880   2749   2645   -141   -139    -27       C  
-ATOM    978  CD1 TYR A 130      21.813  19.770  -7.721  1.00 20.01           C  
-ANISOU  978  CD1 TYR A 130     2649   2506   2447   -193   -140      7       C  
-ATOM    979  CD2 TYR A 130      19.577  19.469  -8.485  1.00 22.20           C  
-ANISOU  979  CD2 TYR A 130     2959   2748   2729   -112   -172    -70       C  
-ATOM    980  CE1 TYR A 130      21.335  20.522  -6.635  1.00 19.33           C  
-ANISOU  980  CE1 TYR A 130     2598   2342   2405   -208   -173    -11       C  
-ATOM    981  CE2 TYR A 130      19.103  20.221  -7.416  1.00 21.64           C  
-ANISOU  981  CE2 TYR A 130     2910   2611   2703   -120   -195    -82       C  
-ATOM    982  CZ  TYR A 130      19.986  20.745  -6.495  1.00 19.23           C  
-ANISOU  982  CZ  TYR A 130     2615   2280   2413   -165   -196    -57       C  
-ATOM    983  OH  TYR A 130      19.495  21.488  -5.425  1.00 19.91           O  
-ANISOU  983  OH  TYR A 130     2741   2294   2531   -161   -222    -78       O  
-ATOM    984  N   LYS A 131      22.417  15.542  -8.865  1.00 21.22           N  
-ANISOU  984  N   LYS A 131     2730   2823   2511    -54    -36   -102       N  
-ATOM    985  CA  LYS A 131      22.443  14.457  -7.886  1.00 23.26           C  
-ANISOU  985  CA  LYS A 131     2971   3066   2801    -43    -25   -151       C  
-ATOM    986  C   LYS A 131      23.863  14.196  -7.348  1.00 22.20           C  
-ANISOU  986  C   LYS A 131     2794   2979   2661    -57     14   -114       C  
-ATOM    987  O   LYS A 131      24.046  13.979  -6.156  1.00 19.23           O  
-ANISOU  987  O   LYS A 131     2401   2576   2328    -80     14   -126       O  
-ATOM    988  CB  LYS A 131      21.866  13.172  -8.488  1.00 23.84           C  
-ANISOU  988  CB  LYS A 131     3065   3142   2851     13    -33   -211       C  
-ATOM    989  CG  LYS A 131      21.562  12.106  -7.412  1.00 23.34           C  
-ANISOU  989  CG  LYS A 131     2993   3041   2835     15    -37   -260       C  
-ATOM    990  CD  LYS A 131      21.288  10.711  -8.021  1.00 27.35           C  
-ANISOU  990  CD  LYS A 131     3529   3547   3316     66    -52   -313       C  
-ATOM    991  CE  LYS A 131      19.925  10.595  -8.676  1.00 30.49           C  
-ANISOU  991  CE  LYS A 131     3959   3905   3720     73   -108   -346       C  
-ATOM    992  NZ  LYS A 131      19.500   9.136  -8.784  1.00 33.17           N  
-ANISOU  992  NZ  LYS A 131     4329   4212   4064    100   -143   -402       N  
-ATOM    993  N   ARG A 132      24.863  14.236  -8.228  1.00 22.53           N  
-ANISOU  993  N   ARG A 132     2814   3097   2648    -40     47    -62       N  
-ATOM    994  CA  ARG A 132      26.250  14.080  -7.800  1.00 23.40           C  
-ANISOU  994  CA  ARG A 132     2868   3267   2756    -53     84    -11       C  
-ATOM    995  C   ARG A 132      26.663  15.162  -6.785  1.00 21.24           C  
-ANISOU  995  C   ARG A 132     2573   2961   2536   -139     59     39       C  
-ATOM    996  O   ARG A 132      27.303  14.856  -5.772  1.00 21.76           O  
-ANISOU  996  O   ARG A 132     2608   3027   2632   -160     62     44       O  
-ATOM    997  CB  ARG A 132      27.187  14.112  -9.012  1.00 25.29           C  
-ANISOU  997  CB  ARG A 132     3078   3607   2923    -18    129     53       C  
-ATOM    998  CG  ARG A 132      28.600  13.642  -8.714  1.00 32.51           C  
-ANISOU  998  CG  ARG A 132     3921   4604   3827     -6    176    103       C  
-ATOM    999  CD  ARG A 132      29.592  14.097  -9.788  1.00 36.59           C  
-ANISOU  999  CD  ARG A 132     4389   5232   4282      7    225    201       C  
-ATOM   1000  NE  ARG A 132      29.037  14.050 -11.139  1.00 41.09           N  
-ANISOU 1000  NE  ARG A 132     5011   5826   4777     69    237    185       N  
-ATOM   1001  CZ  ARG A 132      28.510  15.094 -11.776  1.00 45.34           C  
-ANISOU 1001  CZ  ARG A 132     5578   6344   5303     28    212    220       C  
-ATOM   1002  NH1 ARG A 132      28.452  16.279 -11.176  1.00 46.71           N  
-ANISOU 1002  NH1 ARG A 132     5741   6466   5540    -72    170    270       N  
-ATOM   1003  NH2 ARG A 132      28.035  14.955 -13.015  1.00 45.22           N  
-ANISOU 1003  NH2 ARG A 132     5613   6357   5213     92    221    204       N  
-ATOM   1004  N   TRP A 133      26.314  16.418  -7.066  1.00 19.36           N  
-ANISOU 1004  N   TRP A 133     2361   2689   2305   -186     26     77       N  
-ATOM   1005  CA  TRP A 133      26.589  17.526  -6.132  1.00 20.67           C  
-ANISOU 1005  CA  TRP A 133     2533   2803   2519   -265    -16    116       C  
-ATOM   1006  C   TRP A 133      25.934  17.296  -4.768  1.00 21.68           C  
-ANISOU 1006  C   TRP A 133     2691   2854   2694   -268    -41     47       C  
-ATOM   1007  O   TRP A 133      26.537  17.551  -3.721  1.00 22.58           O  
-ANISOU 1007  O   TRP A 133     2796   2946   2837   -313    -61     64       O  
-ATOM   1008  CB  TRP A 133      26.098  18.863  -6.690  1.00 22.36           C  
-ANISOU 1008  CB  TRP A 133     2790   2973   2732   -302    -56    154       C  
-ATOM   1009  CG  TRP A 133      26.705  19.293  -7.980  1.00 23.00           C  
-ANISOU 1009  CG  TRP A 133     2848   3126   2767   -311    -35    237       C  
-ATOM   1010  CD1 TRP A 133      27.740  18.703  -8.638  1.00 24.33           C  
-ANISOU 1010  CD1 TRP A 133     2951   3402   2890   -290     20    290       C  
-ATOM   1011  CD2 TRP A 133      26.303  20.409  -8.776  1.00 24.07           C  
-ANISOU 1011  CD2 TRP A 133     3022   3234   2889   -337    -67    283       C  
-ATOM   1012  NE1 TRP A 133      28.019  19.397  -9.801  1.00 26.41           N  
-ANISOU 1012  NE1 TRP A 133     3209   3716   3110   -303     31    371       N  
-ATOM   1013  CE2 TRP A 133      27.149  20.449  -9.903  1.00 27.32           C  
-ANISOU 1013  CE2 TRP A 133     3389   3745   3245   -336    -26    369       C  
-ATOM   1014  CE3 TRP A 133      25.304  21.384  -8.648  1.00 25.10           C  
-ANISOU 1014  CE3 TRP A 133     3222   3268   3045   -352   -124    263       C  
-ATOM   1015  CZ2 TRP A 133      27.011  21.409 -10.904  1.00 26.69           C  
-ANISOU 1015  CZ2 TRP A 133     3335   3670   3137   -359    -42    438       C  
-ATOM   1016  CZ3 TRP A 133      25.180  22.345  -9.639  1.00 24.57           C  
-ANISOU 1016  CZ3 TRP A 133     3183   3198   2953   -373   -146    327       C  
-ATOM   1017  CH2 TRP A 133      26.031  22.352 -10.749  1.00 24.61           C  
-ANISOU 1017  CH2 TRP A 133     3145   3302   2905   -381   -107    415       C  
-ATOM   1018  N   ILE A 134      24.685  16.834  -4.793  1.00 21.53           N  
-ANISOU 1018  N   ILE A 134     2705   2796   2679   -220    -43    -25       N  
-ATOM   1019  CA  ILE A 134      23.921  16.593  -3.577  1.00 19.66           C  
-ANISOU 1019  CA  ILE A 134     2492   2497   2480   -212    -57    -83       C  
-ATOM   1020  C   ILE A 134      24.554  15.456  -2.763  1.00 19.44           C  
-ANISOU 1020  C   ILE A 134     2429   2495   2461   -203    -31   -102       C  
-ATOM   1021  O   ILE A 134      24.715  15.562  -1.548  1.00 19.30           O  
-ANISOU 1021  O   ILE A 134     2420   2445   2469   -226    -45   -110       O  
-ATOM   1022  CB  ILE A 134      22.449  16.265  -3.896  1.00 17.88           C  
-ANISOU 1022  CB  ILE A 134     2290   2242   2261   -165    -62   -140       C  
-ATOM   1023  CG1 ILE A 134      21.737  17.495  -4.481  1.00 17.50           C  
-ANISOU 1023  CG1 ILE A 134     2281   2157   2211   -170    -95   -123       C  
-ATOM   1024  CG2 ILE A 134      21.713  15.794  -2.639  1.00 16.78           C  
-ANISOU 1024  CG2 ILE A 134     2158   2062   2157   -152    -62   -189       C  
-ATOM   1025  CD1 ILE A 134      20.363  17.150  -5.109  1.00 16.15           C  
-ANISOU 1025  CD1 ILE A 134     2119   1976   2042   -123   -104   -165       C  
-ATOM   1026  N   ILE A 135      24.938  14.384  -3.434  1.00 20.94           N  
-ANISOU 1026  N   ILE A 135     2589   2741   2624   -163      2   -109       N  
-ATOM   1027  CA  ILE A 135      25.532  13.254  -2.722  1.00 22.88           C  
-ANISOU 1027  CA  ILE A 135     2808   3008   2879   -145     23   -126       C  
-ATOM   1028  C   ILE A 135      26.889  13.649  -2.119  1.00 22.97           C  
-ANISOU 1028  C   ILE A 135     2779   3052   2896   -190     23    -66       C  
-ATOM   1029  O   ILE A 135      27.254  13.201  -1.020  1.00 22.64           O  
-ANISOU 1029  O   ILE A 135     2728   2999   2876   -199     18    -76       O  
-ATOM   1030  CB  ILE A 135      25.640  12.014  -3.658  1.00 24.42           C  
-ANISOU 1030  CB  ILE A 135     2994   3248   3037    -79     52   -151       C  
-ATOM   1031  CG1 ILE A 135      24.232  11.489  -3.940  1.00 25.86           C  
-ANISOU 1031  CG1 ILE A 135     3217   3381   3228    -50     32   -213       C  
-ATOM   1032  CG2 ILE A 135      26.490  10.890  -3.029  1.00 24.71           C  
-ANISOU 1032  CG2 ILE A 135     3002   3311   3076    -53     74   -157       C  
-ATOM   1033  CD1 ILE A 135      24.181  10.339  -4.926  1.00 27.92           C  
-ANISOU 1033  CD1 ILE A 135     3494   3664   3449     13     40   -247       C  
-ATOM   1034  N   LEU A 136      27.620  14.505  -2.823  1.00 22.57           N  
-ANISOU 1034  N   LEU A 136     2704   3043   2828   -222     21      3       N  
-ATOM   1035  CA  LEU A 136      28.879  15.040  -2.326  1.00 23.33           C  
-ANISOU 1035  CA  LEU A 136     2755   3170   2938   -282      8     76       C  
-ATOM   1036  C   LEU A 136      28.635  15.784  -1.002  1.00 22.69           C  
-ANISOU 1036  C   LEU A 136     2718   3006   2896   -339    -48     62       C  
-ATOM   1037  O   LEU A 136      29.372  15.616  -0.036  1.00 19.98           O  
-ANISOU 1037  O   LEU A 136     2354   2666   2572   -368    -65     78       O  
-ATOM   1038  CB  LEU A 136      29.511  15.962  -3.388  1.00 27.01           C  
-ANISOU 1038  CB  LEU A 136     3190   3688   3383   -317     10    163       C  
-ATOM   1039  CG  LEU A 136      30.876  16.625  -3.198  1.00 35.37           C  
-ANISOU 1039  CG  LEU A 136     4184   4797   4457   -392     -7    268       C  
-ATOM   1040  CD1 LEU A 136      31.362  17.183  -4.530  1.00 38.15           C  
-ANISOU 1040  CD1 LEU A 136     4496   5225   4775   -403     19    355       C  
-ATOM   1041  CD2 LEU A 136      30.840  17.723  -2.147  1.00 38.98           C  
-ANISOU 1041  CD2 LEU A 136     4687   5165   4960   -481    -86    281       C  
-ATOM   1042  N   GLY A 137      27.589  16.604  -0.960  1.00 23.79           N  
-ANISOU 1042  N   GLY A 137     2924   3073   3044   -347    -78     32       N  
-ATOM   1043  CA  GLY A 137      27.216  17.300   0.258  1.00 21.18           C  
-ANISOU 1043  CA  GLY A 137     2653   2660   2736   -378   -128      7       C  
-ATOM   1044  C   GLY A 137      26.725  16.371   1.360  1.00 22.66           C  
-ANISOU 1044  C   GLY A 137     2854   2825   2931   -339   -112    -58       C  
-ATOM   1045  O   GLY A 137      27.093  16.543   2.532  1.00 24.75           O  
-ANISOU 1045  O   GLY A 137     3140   3058   3205   -366   -143    -61       O  
-ATOM   1046  N   LEU A 138      25.886  15.406   0.999  1.00 22.61           N  
-ANISOU 1046  N   LEU A 138     2839   2832   2919   -279    -71   -106       N  
-ATOM   1047  CA  LEU A 138      25.324  14.481   1.983  1.00 24.01           C  
-ANISOU 1047  CA  LEU A 138     3025   2990   3106   -246    -54   -157       C  
-ATOM   1048  C   LEU A 138      26.449  13.638   2.611  1.00 23.46           C  
-ANISOU 1048  C   LEU A 138     2916   2958   3039   -255    -46   -139       C  
-ATOM   1049  O   LEU A 138      26.429  13.355   3.813  1.00 24.13           O  
-ANISOU 1049  O   LEU A 138     3020   3018   3131   -256    -55   -158       O  
-ATOM   1050  CB  LEU A 138      24.268  13.566   1.353  1.00 23.41           C  
-ANISOU 1050  CB  LEU A 138     2941   2920   3031   -194    -24   -199       C  
-ATOM   1051  CG  LEU A 138      22.911  14.133   0.935  1.00 23.74           C  
-ANISOU 1051  CG  LEU A 138     3014   2928   3079   -174    -31   -223       C  
-ATOM   1052  CD1 LEU A 138      22.104  13.075   0.165  1.00 20.85           C  
-ANISOU 1052  CD1 LEU A 138     2629   2577   2717   -136    -14   -253       C  
-ATOM   1053  CD2 LEU A 138      22.147  14.696   2.124  1.00 21.35           C  
-ANISOU 1053  CD2 LEU A 138     2750   2574   2786   -169    -42   -245       C  
-ATOM   1054  N   ASN A 139      27.440  13.275   1.805  1.00 23.44           N  
-ANISOU 1054  N   ASN A 139     2860   3020   3026   -254    -29    -99       N  
-ATOM   1055  CA  ASN A 139      28.582  12.508   2.314  1.00 25.85           C  
-ANISOU 1055  CA  ASN A 139     3118   3370   3334   -253    -21    -74       C  
-ATOM   1056  C   ASN A 139      29.348  13.300   3.381  1.00 23.78           C  
-ANISOU 1056  C   ASN A 139     2861   3088   3085   -318    -70    -37       C  
-ATOM   1057  O   ASN A 139      29.729  12.750   4.424  1.00 23.81           O  
-ANISOU 1057  O   ASN A 139     2863   3088   3097   -318    -81    -44       O  
-ATOM   1058  CB  ASN A 139      29.513  12.100   1.170  1.00 28.94           C  
-ANISOU 1058  CB  ASN A 139     3445   3846   3704   -228     13    -29       C  
-ATOM   1059  CG  ASN A 139      28.953  10.957   0.349  1.00 31.66           C  
-ANISOU 1059  CG  ASN A 139     3797   4205   4028   -151     52    -77       C  
-ATOM   1060  OD1 ASN A 139      27.985  10.314   0.749  1.00 34.02           O  
-ANISOU 1060  OD1 ASN A 139     4136   4453   4338   -127     50   -135       O  
-ATOM   1061  ND2 ASN A 139      29.553  10.705  -0.809  1.00 33.04           N  
-ANISOU 1061  ND2 ASN A 139     3935   4450   4168   -112     85    -48       N  
-ATOM   1062  N   LYS A 140      29.565  14.587   3.128  1.00 25.54           N  
-ANISOU 1062  N   LYS A 140     3098   3293   3312   -375   -109      4       N  
-ATOM   1063  CA  LYS A 140      30.165  15.479   4.131  1.00 28.25           C  
-ANISOU 1063  CA  LYS A 140     3468   3596   3668   -444   -177     34       C  
-ATOM   1064  C   LYS A 140      29.348  15.480   5.424  1.00 27.73           C  
-ANISOU 1064  C   LYS A 140     3483   3456   3597   -426   -198    -31       C  
-ATOM   1065  O   LYS A 140      29.897  15.468   6.521  1.00 27.76           O  
-ANISOU 1065  O   LYS A 140     3504   3443   3602   -452   -238    -27       O  
-ATOM   1066  CB  LYS A 140      30.285  16.920   3.599  1.00 33.15           C  
-ANISOU 1066  CB  LYS A 140     4114   4186   4295   -508   -227     82       C  
-ATOM   1067  CG  LYS A 140      31.244  17.105   2.431  1.00 37.61           C  
-ANISOU 1067  CG  LYS A 140     4595   4832   4862   -540   -211    170       C  
-ATOM   1068  CD  LYS A 140      31.254  18.549   1.917  1.00 41.36           C  
-ANISOU 1068  CD  LYS A 140     5104   5266   5345   -610   -265    222       C  
-ATOM   1069  CE  LYS A 140      31.637  19.544   3.009  1.00 43.00           C  
-ANISOU 1069  CE  LYS A 140     5372   5392   5575   -691   -364    240       C  
-ATOM   1070  NZ  LYS A 140      31.876  20.933   2.495  1.00 44.51           N  
-ANISOU 1070  NZ  LYS A 140     5592   5538   5780   -774   -432    309       N  
-ATOM   1071  N   ILE A 141      28.026  15.510   5.290  1.00 29.18           N  
-ANISOU 1071  N   ILE A 141     3715   3601   3772   -379   -172    -88       N  
-ATOM   1072  CA  ILE A 141      27.148  15.513   6.447  1.00 26.48           C  
-ANISOU 1072  CA  ILE A 141     3442   3202   3418   -348   -177   -143       C  
-ATOM   1073  C   ILE A 141      27.224  14.197   7.222  1.00 28.42           C  
-ANISOU 1073  C   ILE A 141     3663   3475   3662   -316   -144   -162       C  
-ATOM   1074  O   ILE A 141      27.276  14.197   8.456  1.00 30.48           O  
-ANISOU 1074  O   ILE A 141     3966   3707   3907   -317   -166   -178       O  
-ATOM   1075  CB  ILE A 141      25.698  15.756   6.051  1.00 27.50           C  
-ANISOU 1075  CB  ILE A 141     3605   3301   3541   -299   -148   -186       C  
-ATOM   1076  CG1 ILE A 141      25.538  17.183   5.500  1.00 26.37           C  
-ANISOU 1076  CG1 ILE A 141     3509   3113   3397   -325   -191   -171       C  
-ATOM   1077  CG2 ILE A 141      24.774  15.518   7.261  1.00 28.37           C  
-ANISOU 1077  CG2 ILE A 141     3765   3378   3636   -253   -133   -234       C  
-ATOM   1078  CD1 ILE A 141      24.206  17.411   4.864  1.00 25.23           C  
-ANISOU 1078  CD1 ILE A 141     3382   2953   3252   -274   -164   -202       C  
-ATOM   1079  N   VAL A 142      27.229  13.083   6.500  1.00 23.09           N  
-ANISOU 1079  N   VAL A 142     2927   2849   2996   -285    -97   -162       N  
-ATOM   1080  CA  VAL A 142      27.339  11.767   7.138  1.00 23.58           C  
-ANISOU 1080  CA  VAL A 142     2968   2930   3060   -256    -71   -176       C  
-ATOM   1081  C   VAL A 142      28.648  11.695   7.954  1.00 25.11           C  
-ANISOU 1081  C   VAL A 142     3146   3143   3254   -289   -107   -140       C  
-ATOM   1082  O   VAL A 142      28.677  11.225   9.101  1.00 25.14           O  
-ANISOU 1082  O   VAL A 142     3174   3131   3249   -282   -116   -152       O  
-ATOM   1083  CB  VAL A 142      27.282  10.642   6.082  1.00 21.29           C  
-ANISOU 1083  CB  VAL A 142     2629   2681   2780   -216    -29   -181       C  
-ATOM   1084  CG1 VAL A 142      27.876   9.342   6.625  1.00 22.86           C  
-ANISOU 1084  CG1 VAL A 142     2802   2901   2982   -193    -18   -178       C  
-ATOM   1085  CG2 VAL A 142      25.860  10.432   5.576  1.00 20.65           C  
-ANISOU 1085  CG2 VAL A 142     2568   2575   2704   -185     -5   -220       C  
-ATOM   1086  N   ARG A 143      29.731  12.175   7.357  1.00 25.24           N  
-ANISOU 1086  N   ARG A 143     3116   3197   3278   -328   -131    -88       N  
-ATOM   1087  CA  ARG A 143      31.020  12.205   8.040  1.00 29.64           C  
-ANISOU 1087  CA  ARG A 143     3642   3779   3841   -369   -175    -41       C  
-ATOM   1088  C   ARG A 143      31.016  13.160   9.249  1.00 28.44           C  
-ANISOU 1088  C   ARG A 143     3566   3562   3677   -415   -244    -48       C  
-ATOM   1089  O   ARG A 143      31.642  12.881  10.262  1.00 27.86           O  
-ANISOU 1089  O   ARG A 143     3499   3488   3598   -430   -280    -37       O  
-ATOM   1090  CB  ARG A 143      32.141  12.581   7.053  1.00 33.34           C  
-ANISOU 1090  CB  ARG A 143     4030   4312   4324   -404   -182     32       C  
-ATOM   1091  CG  ARG A 143      32.525  11.448   6.102  1.00 37.15           C  
-ANISOU 1091  CG  ARG A 143     4436   4873   4805   -343   -117     45       C  
-ATOM   1092  CD  ARG A 143      33.793  11.732   5.305  1.00 42.25           C  
-ANISOU 1092  CD  ARG A 143     4988   5605   5459   -368   -116    131       C  
-ATOM   1093  NE  ARG A 143      33.540  12.732   4.277  1.00 46.15           N  
-ANISOU 1093  NE  ARG A 143     5485   6103   5949   -399   -114    157       N  
-ATOM   1094  CZ  ARG A 143      33.316  12.453   2.996  1.00 44.96           C  
-ANISOU 1094  CZ  ARG A 143     5308   5997   5777   -349    -56    157       C  
-ATOM   1095  NH1 ARG A 143      33.351  11.199   2.562  1.00 45.89           N  
-ANISOU 1095  NH1 ARG A 143     5401   6160   5877   -263      0    129       N  
-ATOM   1096  NH2 ARG A 143      33.071  13.436   2.151  1.00 43.64           N  
-ANISOU 1096  NH2 ARG A 143     5149   5827   5603   -383    -61    185       N  
-ATOM   1097  N   MET A 144      30.294  14.269   9.165  1.00 30.15           N  
-ANISOU 1097  N   MET A 144     3851   3720   3884   -431   -268    -70       N  
-ATOM   1098  CA  MET A 144      30.279  15.214  10.284  1.00 31.12           C  
-ANISOU 1098  CA  MET A 144     4067   3773   3985   -463   -341    -85       C  
-ATOM   1099  C   MET A 144      29.549  14.645  11.489  1.00 29.90           C  
-ANISOU 1099  C   MET A 144     3973   3590   3796   -408   -320   -139       C  
-ATOM   1100  O   MET A 144      29.997  14.798  12.644  1.00 32.69           O  
-ANISOU 1100  O   MET A 144     4378   3916   4125   -426   -375   -142       O  
-ATOM   1101  CB  MET A 144      29.626  16.545   9.888  1.00 32.53           C  
-ANISOU 1101  CB  MET A 144     4317   3887   4157   -478   -372    -99       C  
-ATOM   1102  CG  MET A 144      29.300  17.440  11.107  1.00 34.43           C  
-ANISOU 1102  CG  MET A 144     4684   4039   4360   -478   -439   -139       C  
-ATOM   1103  SD  MET A 144      28.911  19.120  10.609  1.00 99.49           S  
-ANISOU 1103  SD  MET A 144    13012  12193  12598   -508   -504   -141       S  
-ATOM   1104  CE  MET A 144      30.359  19.497   9.635  1.00 39.99           C  
-ANISOU 1104  CE  MET A 144     5384   4698   5112   -619   -557    -39       C  
-ATOM   1105  N   TYR A 145      28.420  14.004  11.232  1.00 25.81           N  
-ANISOU 1105  N   TYR A 145     3451   3080   3274   -345   -246   -178       N  
-ATOM   1106  CA  TYR A 145      27.581  13.519  12.326  1.00 29.38           C  
-ANISOU 1106  CA  TYR A 145     3955   3514   3693   -293   -217   -218       C  
-ATOM   1107  C   TYR A 145      27.988  12.118  12.808  1.00 27.57           C  
-ANISOU 1107  C   TYR A 145     3678   3328   3470   -278   -189   -205       C  
-ATOM   1108  O   TYR A 145      27.371  11.574  13.712  1.00 27.22           O  
-ANISOU 1108  O   TYR A 145     3666   3276   3400   -240   -162   -225       O  
-ATOM   1109  CB  TYR A 145      26.119  13.524  11.904  1.00 33.12           C  
-ANISOU 1109  CB  TYR A 145     4440   3980   4166   -239   -157   -253       C  
-ATOM   1110  CG  TYR A 145      25.582  14.913  11.625  1.00 37.00           C  
-ANISOU 1110  CG  TYR A 145     4994   4420   4643   -236   -185   -271       C  
-ATOM   1111  CD1 TYR A 145      26.379  16.046  11.822  1.00 39.12           C  
-ANISOU 1111  CD1 TYR A 145     5319   4643   4901   -285   -266   -259       C  
-ATOM   1112  CD2 TYR A 145      24.288  15.095  11.166  1.00 36.91           C  
-ANISOU 1112  CD2 TYR A 145     4988   4404   4633   -185   -139   -297       C  
-ATOM   1113  CE1 TYR A 145      25.900  17.317  11.560  1.00 40.34           C  
-ANISOU 1113  CE1 TYR A 145     5544   4739   5045   -281   -301   -276       C  
-ATOM   1114  CE2 TYR A 145      23.797  16.365  10.914  1.00 38.59           C  
-ANISOU 1114  CE2 TYR A 145     5262   4567   4833   -173   -167   -313       C  
-ATOM   1115  CZ  TYR A 145      24.606  17.470  11.108  1.00 39.74           C  
-ANISOU 1115  CZ  TYR A 145     5475   4659   4966   -218   -248   -305       C  
-ATOM   1116  OH  TYR A 145      24.117  18.729  10.856  1.00 44.01           O  
-ANISOU 1116  OH  TYR A 145     6089   5138   5494   -204   -284   -322       O  
-ATOM   1117  N   SER A 146      28.996  11.525  12.176  1.00 28.42           N  
-ANISOU 1117  N   SER A 146     3707   3482   3610   -301   -193   -167       N  
-ATOM   1118  CA  SER A 146      29.618  10.297  12.698  1.00 27.43           C  
-ANISOU 1118  CA  SER A 146     3544   3390   3490   -287   -184   -150       C  
-ATOM   1119  C   SER A 146      30.091  10.560  14.141  1.00 26.69           C  
-ANISOU 1119  C   SER A 146     3509   3270   3360   -306   -240   -146       C  
-ATOM   1120  O   SER A 146      30.980  11.363  14.366  1.00 26.44           O  
-ANISOU 1120  O   SER A 146     3488   3231   3328   -357   -310   -121       O  
-ATOM   1121  CB  SER A 146      30.791   9.867  11.793  1.00 29.13           C  
-ANISOU 1121  CB  SER A 146     3668   3662   3737   -302   -187   -104       C  
-ATOM   1122  OG  SER A 146      31.330   8.601  12.161  1.00 29.85           O  
-ANISOU 1122  OG  SER A 146     3722   3784   3835   -272   -173    -90       O  
-ATOM   1123  N   PRO A 147      29.481   9.902  15.129  1.00 28.09           N  
-ANISOU 1123  N   PRO A 147     3729   3436   3509   -267   -215   -167       N  
-ATOM   1124  CA  PRO A 147      29.791  10.319  16.504  1.00 32.94           C  
-ANISOU 1124  CA  PRO A 147     4421   4022   4073   -277   -270   -171       C  
-ATOM   1125  C   PRO A 147      31.113   9.767  17.059  1.00 32.89           C  
-ANISOU 1125  C   PRO A 147     4381   4041   4073   -305   -324   -130       C  
-ATOM   1126  O   PRO A 147      31.575  10.252  18.088  1.00 30.71           O  
-ANISOU 1126  O   PRO A 147     4168   3740   3758   -326   -392   -129       O  
-ATOM   1127  CB  PRO A 147      28.621   9.758  17.298  1.00 32.92           C  
-ANISOU 1127  CB  PRO A 147     4466   4011   4033   -220   -212   -197       C  
-ATOM   1128  CG  PRO A 147      28.281   8.501  16.577  1.00 32.27           C  
-ANISOU 1128  CG  PRO A 147     4306   3960   3995   -199   -148   -185       C  
-ATOM   1129  CD  PRO A 147      28.552   8.765  15.094  1.00 29.64           C  
-ANISOU 1129  CD  PRO A 147     3909   3643   3712   -219   -144   -180       C  
-ATOM   1130  N   THR A 148      31.717   8.774  16.409  1.00 33.00           N  
-ANISOU 1130  N   THR A 148     4303   4104   4131   -298   -299    -99       N  
-ATOM   1131  CA  THR A 148      32.851   8.104  17.047  1.00 32.17           C  
-ANISOU 1131  CA  THR A 148     4166   4027   4029   -306   -342    -59       C  
-ATOM   1132  C   THR A 148      34.019   7.848  16.101  1.00 29.65           C  
-ANISOU 1132  C   THR A 148     3738   3768   3761   -323   -352    -10       C  
-ATOM   1133  O   THR A 148      33.830   7.542  14.926  1.00 28.65           O  
-ANISOU 1133  O   THR A 148     3555   3667   3664   -299   -297    -11       O  
-ATOM   1134  CB  THR A 148      32.399   6.773  17.682  1.00 36.07           C  
-ANISOU 1134  CB  THR A 148     4672   4522   4510   -254   -297    -66       C  
-ATOM   1135  OG1 THR A 148      31.397   7.044  18.673  1.00 38.02           O  
-ANISOU 1135  OG1 THR A 148     5013   4730   4702   -237   -284    -98       O  
-ATOM   1136  CG2 THR A 148      33.577   6.048  18.341  1.00 33.89           C  
-ANISOU 1136  CG2 THR A 148     4365   4275   4238   -255   -344    -23       C  
-ATOM   1137  N   SER A 149      35.234   8.013  16.616  1.00 26.89           N  
-ANISOU 1137  N   SER A 149     3357   3442   3417   -361   -425     38       N  
-ATOM   1138  CA  SER A 149      36.429   7.716  15.841  1.00 29.47           C  
-ANISOU 1138  CA  SER A 149     3566   3842   3788   -368   -432     99       C  
-ATOM   1139  C   SER A 149      36.663   6.204  15.862  1.00 27.31           C  
-ANISOU 1139  C   SER A 149     3249   3603   3525   -295   -387    106       C  
-ATOM   1140  O   SER A 149      36.333   5.535  16.844  1.00 25.82           O  
-ANISOU 1140  O   SER A 149     3117   3382   3310   -268   -390     87       O  
-ATOM   1141  CB  SER A 149      37.645   8.471  16.399  1.00 32.47           C  
-ANISOU 1141  CB  SER A 149     3918   4240   4178   -443   -536    159       C  
-ATOM   1142  OG  SER A 149      38.870   7.979  15.872  1.00 33.68           O  
-ANISOU 1142  OG  SER A 149     3943   4480   4373   -438   -539    231       O  
-ATOM   1143  N   ILE A 150      37.217   5.673  14.777  1.00 22.10           N  
-ANISOU 1143  N   ILE A 150     2495   3005   2896   -256   -344    135       N  
-ATOM   1144  CA  ILE A 150      37.553   4.261  14.713  1.00 22.06           C  
-ANISOU 1144  CA  ILE A 150     2453   3028   2900   -177   -310    142       C  
-ATOM   1145  C   ILE A 150      38.567   3.923  15.807  1.00 22.44           C  
-ANISOU 1145  C   ILE A 150     2480   3099   2949   -184   -376    189       C  
-ATOM   1146  O   ILE A 150      38.631   2.794  16.271  1.00 20.87           O  
-ANISOU 1146  O   ILE A 150     2293   2892   2746   -126   -366    185       O  
-ATOM   1147  CB  ILE A 150      38.125   3.864  13.323  1.00 24.38           C  
-ANISOU 1147  CB  ILE A 150     2652   3394   3218   -122   -257    168       C  
-ATOM   1148  CG1 ILE A 150      38.145   2.336  13.169  1.00 24.41           C  
-ANISOU 1148  CG1 ILE A 150     2653   3398   3222    -21   -216    151       C  
-ATOM   1149  CG2 ILE A 150      39.547   4.439  13.128  1.00 27.31           C  
-ANISOU 1149  CG2 ILE A 150     2911   3855   3613   -156   -297    253       C  
-ATOM   1150  CD1 ILE A 150      36.733   1.689  13.138  1.00 23.03           C  
-ANISOU 1150  CD1 ILE A 150     2576   3141   3035      7   -177     79       C  
-ATOM   1151  N   LEU A 151      39.336   4.915  16.241  1.00 22.32           N  
-ANISOU 1151  N   LEU A 151     2439   3103   2939   -260   -453    234       N  
-ATOM   1152  CA  LEU A 151      40.328   4.697  17.290  1.00 27.19           C  
-ANISOU 1152  CA  LEU A 151     3033   3742   3556   -278   -531    283       C  
-ATOM   1153  C   LEU A 151      39.707   4.412  18.656  1.00 27.43           C  
-ANISOU 1153  C   LEU A 151     3181   3700   3540   -277   -562    242       C  
-ATOM   1154  O   LEU A 151      40.379   3.874  19.542  1.00 27.33           O  
-ANISOU 1154  O   LEU A 151     3163   3700   3520   -266   -614    274       O  
-ATOM   1155  CB  LEU A 151      41.267   5.905  17.401  1.00 31.53           C  
-ANISOU 1155  CB  LEU A 151     3531   4323   4126   -375   -622    346       C  
-ATOM   1156  CG  LEU A 151      42.074   6.219  16.143  1.00 34.55           C  
-ANISOU 1156  CG  LEU A 151     3777   4796   4554   -384   -596    413       C  
-ATOM   1157  CD1 LEU A 151      42.627   7.646  16.190  1.00 35.00           C  
-ANISOU 1157  CD1 LEU A 151     3811   4856   4632   -505   -688    468       C  
-ATOM   1158  CD2 LEU A 151      43.199   5.212  16.013  1.00 37.04           C  
-ANISOU 1158  CD2 LEU A 151     3971   5205   4897   -317   -585    479       C  
-ATOM   1159  N   ASP A 152      38.436   4.767  18.839  1.00 24.28           N  
-ANISOU 1159  N   ASP A 152     2886   3233   3106   -283   -530    178       N  
-ATOM   1160  CA  ASP A 152      37.741   4.463  20.101  1.00 27.55           C  
-ANISOU 1160  CA  ASP A 152     3411   3591   3467   -270   -542    144       C  
-ATOM   1161  C   ASP A 152      36.854   3.220  20.029  1.00 27.91           C  
-ANISOU 1161  C   ASP A 152     3482   3615   3509   -199   -460    116       C  
-ATOM   1162  O   ASP A 152      36.094   2.932  20.958  1.00 27.55           O  
-ANISOU 1162  O   ASP A 152     3522   3526   3418   -187   -450     94       O  
-ATOM   1163  CB  ASP A 152      36.886   5.650  20.540  1.00 32.68           C  
-ANISOU 1163  CB  ASP A 152     4163   4182   4071   -313   -561     99       C  
-ATOM   1164  CG  ASP A 152      37.731   6.870  20.909  1.00 37.70           C  
-ANISOU 1164  CG  ASP A 152     4809   4814   4702   -392   -669    125       C  
-ATOM   1165  OD1 ASP A 152      38.702   6.714  21.677  1.00 37.15           O  
-ANISOU 1165  OD1 ASP A 152     4725   4762   4628   -414   -750    167       O  
-ATOM   1166  OD2 ASP A 152      37.423   7.976  20.425  1.00 39.45           O  
-ANISOU 1166  OD2 ASP A 152     5054   5010   4926   -435   -681    106       O  
-ATOM   1167  N   ILE A 153      36.926   2.490  18.924  1.00 26.84           N  
-ANISOU 1167  N   ILE A 153     3277   3506   3416   -153   -403    119       N  
-ATOM   1168  CA  ILE A 153      36.170   1.251  18.827  1.00 25.37           C  
-ANISOU 1168  CA  ILE A 153     3119   3288   3232    -92   -345     97       C  
-ATOM   1169  C   ILE A 153      37.065   0.101  19.239  1.00 25.32           C  
-ANISOU 1169  C   ILE A 153     3082   3301   3238    -43   -370    137       C  
-ATOM   1170  O   ILE A 153      37.847  -0.411  18.433  1.00 24.02           O  
-ANISOU 1170  O   ILE A 153     2839   3180   3107      4   -359    158       O  
-ATOM   1171  CB  ILE A 153      35.630   0.991  17.412  1.00 24.87           C  
-ANISOU 1171  CB  ILE A 153     3023   3226   3200    -60   -278     68       C  
-ATOM   1172  CG1 ILE A 153      34.750   2.158  16.952  1.00 22.53           C  
-ANISOU 1172  CG1 ILE A 153     2754   2913   2895   -106   -256     33       C  
-ATOM   1173  CG2 ILE A 153      34.807  -0.314  17.401  1.00 25.60           C  
-ANISOU 1173  CG2 ILE A 153     3158   3270   3299    -10   -237     48       C  
-ATOM   1174  CD1 ILE A 153      33.479   2.351  17.812  1.00 21.26           C  
-ANISOU 1174  CD1 ILE A 153     2684   2697   2697   -123   -239      2       C  
-ATOM   1175  N   ARG A 154      36.931  -0.310  20.497  1.00 22.89           N  
-ANISOU 1175  N   ARG A 154     2838   2963   2896    -45   -400    148       N  
-ATOM   1176  CA  ARG A 154      37.740  -1.393  21.032  1.00 27.23           C  
-ANISOU 1176  CA  ARG A 154     3371   3524   3453      3   -432    188       C  
-ATOM   1177  C   ARG A 154      36.821  -2.448  21.639  1.00 27.60           C  
-ANISOU 1177  C   ARG A 154     3496   3509   3480     31   -403    180       C  
-ATOM   1178  O   ARG A 154      35.747  -2.134  22.184  1.00 29.21           O  
-ANISOU 1178  O   ARG A 154     3773   3678   3649     -1   -380    159       O  
-ATOM   1179  CB  ARG A 154      38.743  -0.868  22.062  1.00 29.72           C  
-ANISOU 1179  CB  ARG A 154     3678   3869   3744    -34   -520    230       C  
-ATOM   1180  CG  ARG A 154      39.601   0.306  21.569  1.00 34.56           C  
-ANISOU 1180  CG  ARG A 154     4214   4537   4379    -86   -563    251       C  
-ATOM   1181  CD  ARG A 154      40.598   0.719  22.637  1.00 40.92           C  
-ANISOU 1181  CD  ARG A 154     5016   5366   5166   -128   -668    297       C  
-ATOM   1182  NE  ARG A 154      41.148  -0.475  23.271  1.00 45.94           N  
-ANISOU 1182  NE  ARG A 154     5643   6009   5801    -70   -690    333       N  
-ATOM   1183  CZ  ARG A 154      41.286  -0.643  24.583  1.00 48.10           C  
-ANISOU 1183  CZ  ARG A 154     5986   6260   6029    -81   -754    350       C  
-ATOM   1184  NH1 ARG A 154      40.943   0.327  25.424  1.00 47.10           N  
-ANISOU 1184  NH1 ARG A 154     5946   6103   5846   -145   -804    329       N  
-ATOM   1185  NH2 ARG A 154      41.785  -1.782  25.049  1.00 49.20           N  
-ANISOU 1185  NH2 ARG A 154     6114   6407   6173    -23   -771    386       N  
-ATOM   1186  N   GLN A 155      37.220  -3.705  21.509  1.00 25.28           N  
-ANISOU 1186  N   GLN A 155     3187   3205   3212     94   -404    201       N  
-ATOM   1187  CA  GLN A 155      36.371  -4.804  21.948  1.00 26.46           C  
-ANISOU 1187  CA  GLN A 155     3408   3288   3355    116   -382    203       C  
-ATOM   1188  C   GLN A 155      36.249  -4.820  23.474  1.00 27.14           C  
-ANISOU 1188  C   GLN A 155     3562   3361   3388     88   -417    235       C  
-ATOM   1189  O   GLN A 155      37.253  -4.723  24.179  1.00 19.50           O  
-ANISOU 1189  O   GLN A 155     2580   2425   2403     92   -479    268       O  
-ATOM   1190  CB  GLN A 155      36.929  -6.143  21.451  1.00 23.37           C  
-ANISOU 1190  CB  GLN A 155     2998   2879   3003    196   -388    217       C  
-ATOM   1191  CG  GLN A 155      36.119  -7.365  21.877  1.00 22.91           C  
-ANISOU 1191  CG  GLN A 155     3017   2740   2947    212   -380    229       C  
-ATOM   1192  CD  GLN A 155      36.701  -8.665  21.353  1.00 22.14           C  
-ANISOU 1192  CD  GLN A 155     2916   2609   2886    300   -397    237       C  
-ATOM   1193  OE1 GLN A 155      37.851  -8.709  20.939  1.00 23.67           O  
-ANISOU 1193  OE1 GLN A 155     3046   2854   3093    360   -416    245       O  
-ATOM   1194  NE2 GLN A 155      35.900  -9.737  21.368  1.00 21.47           N  
-ANISOU 1194  NE2 GLN A 155     2902   2439   2817    310   -393    239       N  
-ATOM   1195  N   GLY A 156      35.029  -4.953  23.981  1.00 26.62           N  
-ANISOU 1195  N   GLY A 156     3567   3255   3294     63   -379    230       N  
-ATOM   1196  CA  GLY A 156      34.817  -5.054  25.421  1.00 27.92           C  
-ANISOU 1196  CA  GLY A 156     3802   3410   3396     47   -400    265       C  
-ATOM   1197  C   GLY A 156      35.402  -6.347  25.959  1.00 32.05           C  
-ANISOU 1197  C   GLY A 156     4340   3909   3928     89   -439    315       C  
-ATOM   1198  O   GLY A 156      35.570  -7.311  25.217  1.00 32.72           O  
-ANISOU 1198  O   GLY A 156     4400   3964   4068    132   -433    318       O  
-ATOM   1199  N   PRO A 157      35.735  -6.377  27.256  1.00 34.20           N  
-ANISOU 1199  N   PRO A 157     4663   4191   4142     84   -483    354       N  
-ATOM   1200  CA  PRO A 157      36.314  -7.595  27.824  1.00 33.93           C  
-ANISOU 1200  CA  PRO A 157     4647   4131   4114    126   -526    408       C  
-ATOM   1201  C   PRO A 157      35.338  -8.752  27.737  1.00 34.40           C  
-ANISOU 1201  C   PRO A 157     4750   4125   4197    134   -482    431       C  
-ATOM   1202  O   PRO A 157      35.755  -9.906  27.692  1.00 35.64           O  
-ANISOU 1202  O   PRO A 157     4913   4241   4388    178   -512    462       O  
-ATOM   1203  CB  PRO A 157      36.592  -7.212  29.286  1.00 36.38           C  
-ANISOU 1203  CB  PRO A 157     5018   4464   4339    107   -575    441       C  
-ATOM   1204  CG  PRO A 157      35.656  -6.088  29.568  1.00 36.96           C  
-ANISOU 1204  CG  PRO A 157     5135   4554   4356     62   -532    406       C  
-ATOM   1205  CD  PRO A 157      35.546  -5.323  28.269  1.00 35.07           C  
-ANISOU 1205  CD  PRO A 157     4827   4328   4170     46   -499    349       C  
-ATOM   1206  N   LYS A 158      34.050  -8.435  27.702  1.00 36.91           N  
-ANISOU 1206  N   LYS A 158     5095   4429   4498     92   -418    419       N  
-ATOM   1207  CA  LYS A 158      33.010  -9.452  27.636  1.00 41.47           C  
-ANISOU 1207  CA  LYS A 158     5707   4947   5103     80   -382    452       C  
-ATOM   1208  C   LYS A 158      32.200  -9.372  26.345  1.00 38.06           C  
-ANISOU 1208  C   LYS A 158     5238   4491   4731     64   -334    408       C  
-ATOM   1209  O   LYS A 158      31.169 -10.046  26.197  1.00 36.81           O  
-ANISOU 1209  O   LYS A 158     5101   4284   4600     37   -305    434       O  
-ATOM   1210  CB  LYS A 158      32.073  -9.323  28.838  1.00 47.25           C  
-ANISOU 1210  CB  LYS A 158     6498   5691   5762     43   -346    502       C  
-ATOM   1211  CG  LYS A 158      32.733  -9.629  30.175  1.00 51.80           C  
-ANISOU 1211  CG  LYS A 158     7129   6281   6273     61   -395    556       C  
-ATOM   1212  CD  LYS A 158      31.710  -9.585  31.299  1.00 55.24           C  
-ANISOU 1212  CD  LYS A 158     7626   6734   6630     33   -347    611       C  
-ATOM   1213  CE  LYS A 158      30.719 -10.734  31.188  1.00 56.30           C  
-ANISOU 1213  CE  LYS A 158     7770   6814   6809      7   -310    676       C  
-ATOM   1214  NZ  LYS A 158      31.364 -12.058  31.443  1.00 56.73           N  
-ANISOU 1214  NZ  LYS A 158     7853   6806   6896     30   -373    732       N  
-ATOM   1215  N   GLU A 159      32.660  -8.546  25.412  1.00 32.84           N  
-ANISOU 1215  N   GLU A 159     4522   3865   4091     75   -331    347       N  
-ATOM   1216  CA  GLU A 159      31.928  -8.358  24.168  1.00 28.64           C  
-ANISOU 1216  CA  GLU A 159     3959   3316   3607     62   -289    301       C  
-ATOM   1217  C   GLU A 159      32.282  -9.461  23.176  1.00 31.37           C  
-ANISOU 1217  C   GLU A 159     4296   3605   4017    109   -314    289       C  
-ATOM   1218  O   GLU A 159      33.454  -9.715  22.929  1.00 32.38           O  
-ANISOU 1218  O   GLU A 159     4400   3746   4156    167   -352    282       O  
-ATOM   1219  CB  GLU A 159      32.225  -6.973  23.575  1.00 23.06           C  
-ANISOU 1219  CB  GLU A 159     3203   2670   2891     52   -275    246       C  
-ATOM   1220  CG  GLU A 159      31.419  -6.658  22.328  1.00 25.45           C  
-ANISOU 1220  CG  GLU A 159     3476   2961   3234     38   -231    200       C  
-ATOM   1221  CD  GLU A 159      31.836  -5.351  21.704  1.00 26.78           C  
-ANISOU 1221  CD  GLU A 159     3596   3183   3394     31   -224    154       C  
-ATOM   1222  OE1 GLU A 159      32.946  -4.864  22.016  1.00 29.83           O  
-ANISOU 1222  OE1 GLU A 159     3961   3612   3762     42   -263    159       O  
-ATOM   1223  OE2 GLU A 159      31.068  -4.807  20.893  1.00 26.76           O  
-ANISOU 1223  OE2 GLU A 159     3578   3182   3409     11   -186    119       O  
-ATOM   1224  N   PRO A 160      31.267 -10.128  22.612  1.00 31.99           N  
-ANISOU 1224  N   PRO A 160     4398   3621   4137     88   -297    289       N  
-ATOM   1225  CA  PRO A 160      31.503 -11.141  21.573  1.00 31.59           C  
-ANISOU 1225  CA  PRO A 160     4360   3502   4141    138   -328    265       C  
-ATOM   1226  C   PRO A 160      32.227 -10.549  20.370  1.00 26.11           C  
-ANISOU 1226  C   PRO A 160     3611   2851   3458    188   -319    200       C  
-ATOM   1227  O   PRO A 160      31.961  -9.416  20.008  1.00 26.28           O  
-ANISOU 1227  O   PRO A 160     3590   2928   3467    156   -282    169       O  
-ATOM   1228  CB  PRO A 160      30.093 -11.599  21.189  1.00 30.77           C  
-ANISOU 1228  CB  PRO A 160     4285   3333   4073     81   -313    274       C  
-ATOM   1229  CG  PRO A 160      29.233 -11.232  22.376  1.00 30.73           C  
-ANISOU 1229  CG  PRO A 160     4287   3357   4032     11   -278    333       C  
-ATOM   1230  CD  PRO A 160      29.834  -9.966  22.920  1.00 30.82           C  
-ANISOU 1230  CD  PRO A 160     4265   3461   3983     20   -253    314       C  
-ATOM   1231  N   PHE A 161      33.125 -11.301  19.746  1.00 27.09           N  
-ANISOU 1231  N   PHE A 161     3737   2952   3603    272   -352    183       N  
-ATOM   1232  CA  PHE A 161      33.922 -10.711  18.669  1.00 25.55           C  
-ANISOU 1232  CA  PHE A 161     3480   2819   3409    329   -336    134       C  
-ATOM   1233  C   PHE A 161      33.044 -10.147  17.526  1.00 22.43           C  
-ANISOU 1233  C   PHE A 161     3074   2422   3028    298   -298     82       C  
-ATOM   1234  O   PHE A 161      33.323  -9.082  16.977  1.00 22.24           O  
-ANISOU 1234  O   PHE A 161     2989   2471   2992    293   -267     56       O  
-ATOM   1235  CB  PHE A 161      34.922 -11.741  18.150  1.00 26.08           C  
-ANISOU 1235  CB  PHE A 161     3557   2860   3490    442   -370    127       C  
-ATOM   1236  CG  PHE A 161      35.923 -11.177  17.189  1.00 22.70           C  
-ANISOU 1236  CG  PHE A 161     3051   2517   3055    512   -347     96       C  
-ATOM   1237  CD1 PHE A 161      36.918 -10.307  17.632  1.00 22.81           C  
-ANISOU 1237  CD1 PHE A 161     2982   2635   3052    509   -344    126       C  
-ATOM   1238  CD2 PHE A 161      35.866 -11.500  15.847  1.00 20.18           C  
-ANISOU 1238  CD2 PHE A 161     2745   2179   2746    579   -332     44       C  
-ATOM   1239  CE1 PHE A 161      37.825  -9.774  16.753  1.00 24.46           C  
-ANISOU 1239  CE1 PHE A 161     3106   2930   3257    565   -321    115       C  
-ATOM   1240  CE2 PHE A 161      36.788 -10.996  14.964  1.00 22.95           C  
-ANISOU 1240  CE2 PHE A 161     3019   2619   3083    650   -302     27       C  
-ATOM   1241  CZ  PHE A 161      37.755 -10.114  15.400  1.00 24.57           C  
-ANISOU 1241  CZ  PHE A 161     3126   2933   3276    638   -293     67       C  
-ATOM   1242  N   ARG A 162      31.966 -10.840  17.194  1.00 23.54           N  
-ANISOU 1242  N   ARG A 162     3272   2476   3195    270   -306     73       N  
-ATOM   1243  CA  ARG A 162      31.112 -10.423  16.098  1.00 26.67           C  
-ANISOU 1243  CA  ARG A 162     3663   2864   3608    244   -282     26       C  
-ATOM   1244  C   ARG A 162      30.482  -9.067  16.382  1.00 22.89           C  
-ANISOU 1244  C   ARG A 162     3136   2451   3110    167   -234     28       C  
-ATOM   1245  O   ARG A 162      30.410  -8.210  15.491  1.00 24.82           O  
-ANISOU 1245  O   ARG A 162     3341   2739   3350    166   -206    -12       O  
-ATOM   1246  CB  ARG A 162      30.014 -11.462  15.830  1.00 33.93           C  
-ANISOU 1246  CB  ARG A 162     4654   3673   4565    213   -316     29       C  
-ATOM   1247  CG  ARG A 162      29.125 -11.121  14.617  1.00 40.63           C  
-ANISOU 1247  CG  ARG A 162     5501   4506   5432    188   -305    -20       C  
-ATOM   1248  CD  ARG A 162      27.798 -11.904  14.654  1.00 42.20           C  
-ANISOU 1248  CD  ARG A 162     5752   4607   5674    115   -342      6       C  
-ATOM   1249  NE  ARG A 162      28.030 -13.326  14.877  1.00 46.19           N  
-ANISOU 1249  NE  ARG A 162     6338   5009   6202    147   -410     27       N  
-ATOM   1250  CZ  ARG A 162      27.081 -14.214  15.167  1.00 46.46           C  
-ANISOU 1250  CZ  ARG A 162     6426   4948   6280     79   -458     72       C  
-ATOM   1251  NH1 ARG A 162      25.814 -13.828  15.282  1.00 42.86           N  
-ANISOU 1251  NH1 ARG A 162     5937   4500   5849    -22   -440    106       N  
-ATOM   1252  NH2 ARG A 162      27.412 -15.490  15.352  1.00 46.78           N  
-ANISOU 1252  NH2 ARG A 162     6549   4886   6340    114   -527     90       N  
-ATOM   1253  N   ASP A 163      30.076  -8.856  17.631  1.00 19.41           N  
-ANISOU 1253  N   ASP A 163     2702   2021   2652    111   -226     77       N  
-ATOM   1254  CA  ASP A 163      29.483  -7.585  18.021  1.00 23.22           C  
-ANISOU 1254  CA  ASP A 163     3153   2562   3107     52   -182     77       C  
-ATOM   1255  C   ASP A 163      30.520  -6.466  17.913  1.00 20.32           C  
-ANISOU 1255  C   ASP A 163     2736   2273   2710     73   -175     55       C  
-ATOM   1256  O   ASP A 163      30.192  -5.349  17.525  1.00 16.67           O  
-ANISOU 1256  O   ASP A 163     2246   1850   2237     45   -147     28       O  
-ATOM   1257  CB  ASP A 163      28.919  -7.663  19.443  1.00 28.20           C  
-ANISOU 1257  CB  ASP A 163     3812   3192   3711      6   -173    136       C  
-ATOM   1258  CG  ASP A 163      27.691  -8.555  19.536  1.00 33.14           C  
-ANISOU 1258  CG  ASP A 163     4468   3753   4370    -37   -172    174       C  
-ATOM   1259  OD1 ASP A 163      26.958  -8.692  18.531  1.00 32.73           O  
-ANISOU 1259  OD1 ASP A 163     4409   3668   4359    -54   -171    148       O  
-ATOM   1260  OD2 ASP A 163      27.451  -9.118  20.625  1.00 35.41           O  
-ANISOU 1260  OD2 ASP A 163     4786   4024   4643    -59   -177    236       O  
-ATOM   1261  N   TYR A 164      31.779  -6.780  18.209  1.00 22.27           N  
-ANISOU 1261  N   TYR A 164     2971   2542   2949    121   -207     70       N  
-ATOM   1262  CA  TYR A 164      32.850  -5.787  18.087  1.00 21.49           C  
-ANISOU 1262  CA  TYR A 164     2814   2519   2831    133   -212     63       C  
-ATOM   1263  C   TYR A 164      33.114  -5.426  16.612  1.00 19.30           C  
-ANISOU 1263  C   TYR A 164     2490   2270   2573    165   -191     22       C  
-ATOM   1264  O   TYR A 164      33.269  -4.255  16.260  1.00 19.91           O  
-ANISOU 1264  O   TYR A 164     2524   2400   2639    136   -176     10       O  
-ATOM   1265  CB  TYR A 164      34.106  -6.311  18.771  1.00 20.53           C  
-ANISOU 1265  CB  TYR A 164     2680   2418   2702    177   -255    101       C  
-ATOM   1266  CG  TYR A 164      35.403  -5.722  18.285  1.00 20.71           C  
-ANISOU 1266  CG  TYR A 164     2625   2518   2726    210   -268    104       C  
-ATOM   1267  CD1 TYR A 164      35.681  -4.368  18.445  1.00 20.16           C  
-ANISOU 1267  CD1 TYR A 164     2515   2506   2638    156   -272    107       C  
-ATOM   1268  CD2 TYR A 164      36.376  -6.527  17.702  1.00 24.43           C  
-ANISOU 1268  CD2 TYR A 164     3062   3004   3217    297   -280    112       C  
-ATOM   1269  CE1 TYR A 164      36.877  -3.829  18.015  1.00 22.42           C  
-ANISOU 1269  CE1 TYR A 164     2720   2867   2933    173   -289    126       C  
-ATOM   1270  CE2 TYR A 164      37.583  -5.988  17.267  1.00 25.09           C  
-ANISOU 1270  CE2 TYR A 164     3056   3175   3303    328   -286    130       C  
-ATOM   1271  CZ  TYR A 164      37.821  -4.644  17.419  1.00 25.19           C  
-ANISOU 1271  CZ  TYR A 164     3020   3247   3304    258   -291    142       C  
-ATOM   1272  OH  TYR A 164      39.006  -4.093  16.988  1.00 24.22           O  
-ANISOU 1272  OH  TYR A 164     2799   3213   3191    274   -302    176       O  
-ATOM   1273  N   VAL A 165      33.133  -6.436  15.754  1.00 20.57           N  
-ANISOU 1273  N   VAL A 165     2668   2391   2758    225   -194      2       N  
-ATOM   1274  CA  VAL A 165      33.371  -6.225  14.320  1.00 19.44           C  
-ANISOU 1274  CA  VAL A 165     2491   2274   2620    271   -172    -37       C  
-ATOM   1275  C   VAL A 165      32.214  -5.420  13.692  1.00 21.65           C  
-ANISOU 1275  C   VAL A 165     2777   2547   2904    212   -141    -70       C  
-ATOM   1276  O   VAL A 165      32.457  -4.519  12.884  1.00 20.80           O  
-ANISOU 1276  O   VAL A 165     2623   2493   2787    212   -118    -87       O  
-ATOM   1277  CB  VAL A 165      33.550  -7.555  13.589  1.00 17.53           C  
-ANISOU 1277  CB  VAL A 165     2292   1978   2392    359   -189    -59       C  
-ATOM   1278  CG1 VAL A 165      33.926  -7.316  12.097  1.00 17.59           C  
-ANISOU 1278  CG1 VAL A 165     2268   2026   2388    424   -161    -99       C  
-ATOM   1279  CG2 VAL A 165      34.618  -8.410  14.294  1.00 18.82           C  
-ANISOU 1279  CG2 VAL A 165     2455   2141   2554    425   -222    -23       C  
-ATOM   1280  N   ASP A 166      30.964  -5.723  14.073  1.00 21.02           N  
-ANISOU 1280  N   ASP A 166     2746   2403   2836    161   -142    -71       N  
-ATOM   1281  CA  ASP A 166      29.834  -4.899  13.647  1.00 22.30           C  
-ANISOU 1281  CA  ASP A 166     2905   2567   3003    104   -114    -93       C  
-ATOM   1282  C   ASP A 166      30.065  -3.406  13.968  1.00 19.71           C  
-ANISOU 1282  C   ASP A 166     2534   2306   2647     65    -93    -88       C  
-ATOM   1283  O   ASP A 166      29.928  -2.566  13.083  1.00 21.04           O  
-ANISOU 1283  O   ASP A 166     2676   2504   2814     58    -73   -114       O  
-ATOM   1284  CB  ASP A 166      28.526  -5.347  14.307  1.00 25.41           C  
-ANISOU 1284  CB  ASP A 166     3338   2903   3413     49   -115    -72       C  
-ATOM   1285  CG  ASP A 166      27.898  -6.563  13.644  1.00 29.25           C  
-ANISOU 1285  CG  ASP A 166     3869   3309   3936     60   -144    -83       C  
-ATOM   1286  OD1 ASP A 166      28.235  -6.880  12.469  1.00 31.25           O  
-ANISOU 1286  OD1 ASP A 166     4131   3547   4194    113   -158   -125       O  
-ATOM   1287  OD2 ASP A 166      27.033  -7.188  14.308  1.00 27.69           O  
-ANISOU 1287  OD2 ASP A 166     3701   3062   3759     15   -155    -46       O  
-ATOM   1288  N   ARG A 167      30.395  -3.077  15.224  1.00 17.63           N  
-ANISOU 1288  N   ARG A 167     2275   2062   2362     41   -103    -56       N  
-ATOM   1289  CA  ARG A 167      30.646  -1.666  15.600  1.00 21.45           C  
-ANISOU 1289  CA  ARG A 167     2737   2595   2817      3   -100    -54       C  
-ATOM   1290  C   ARG A 167      31.814  -1.059  14.799  1.00 21.74           C  
-ANISOU 1290  C   ARG A 167     2715   2688   2856     22   -109    -57       C  
-ATOM   1291  O   ARG A 167      31.769   0.103  14.382  1.00 19.49           O  
-ANISOU 1291  O   ARG A 167     2409   2431   2563     -9   -102    -67       O  
-ATOM   1292  CB  ARG A 167      30.940  -1.523  17.109  1.00 22.49           C  
-ANISOU 1292  CB  ARG A 167     2898   2733   2915    -18   -123    -21       C  
-ATOM   1293  CG  ARG A 167      29.802  -1.987  18.021  1.00 24.20           C  
-ANISOU 1293  CG  ARG A 167     3166   2911   3117    -37   -104     -5       C  
-ATOM   1294  CD  ARG A 167      29.999  -1.545  19.472  1.00 23.91           C  
-ANISOU 1294  CD  ARG A 167     3167   2890   3026    -54   -120     21       C  
-ATOM   1295  NE  ARG A 167      31.152  -2.193  20.094  1.00 23.91           N  
-ANISOU 1295  NE  ARG A 167     3168   2897   3020    -31   -166     52       N  
-ATOM   1296  CZ  ARG A 167      32.226  -1.537  20.529  1.00 26.83           C  
-ANISOU 1296  CZ  ARG A 167     3525   3302   3366    -37   -211     60       C  
-ATOM   1297  NH1 ARG A 167      32.278  -0.212  20.420  1.00 25.43           N  
-ANISOU 1297  NH1 ARG A 167     3344   3148   3169    -69   -219     38       N  
-ATOM   1298  NH2 ARG A 167      33.250  -2.200  21.075  1.00 24.46           N  
-ANISOU 1298  NH2 ARG A 167     3217   3011   3066    -13   -256     95       N  
-ATOM   1299  N   PHE A 168      32.861  -1.854  14.608  1.00 22.46           N  
-ANISOU 1299  N   PHE A 168     2778   2798   2957     76   -126    -39       N  
-ATOM   1300  CA  PHE A 168      34.078  -1.387  13.953  1.00 22.65           C  
-ANISOU 1300  CA  PHE A 168     2731   2893   2984     99   -132    -22       C  
-ATOM   1301  C   PHE A 168      33.790  -0.983  12.505  1.00 21.13           C  
-ANISOU 1301  C   PHE A 168     2514   2719   2797    114    -96    -51       C  
-ATOM   1302  O   PHE A 168      34.130   0.136  12.089  1.00 22.62           O  
-ANISOU 1302  O   PHE A 168     2658   2956   2981     80    -92    -40       O  
-ATOM   1303  CB  PHE A 168      35.148  -2.474  14.020  1.00 22.80           C  
-ANISOU 1303  CB  PHE A 168     2724   2930   3011    174   -149      4       C  
-ATOM   1304  CG  PHE A 168      36.490  -2.064  13.451  1.00 27.59           C  
-ANISOU 1304  CG  PHE A 168     3237   3627   3620    205   -151     40       C  
-ATOM   1305  CD1 PHE A 168      36.741  -2.162  12.085  1.00 22.79           C  
-ANISOU 1305  CD1 PHE A 168     2590   3058   3012    264   -112     26       C  
-ATOM   1306  CD2 PHE A 168      37.511  -1.618  14.291  1.00 26.22           C  
-ANISOU 1306  CD2 PHE A 168     3013   3503   3445    177   -194     93       C  
-ATOM   1307  CE1 PHE A 168      37.977  -1.813  11.567  1.00 25.10           C  
-ANISOU 1307  CE1 PHE A 168     2785   3448   3305    297   -104     73       C  
-ATOM   1308  CE2 PHE A 168      38.756  -1.262  13.776  1.00 28.46           C  
-ANISOU 1308  CE2 PHE A 168     3194   3880   3738    199   -197    141       C  
-ATOM   1309  CZ  PHE A 168      38.986  -1.356  12.420  1.00 28.57           C  
-ANISOU 1309  CZ  PHE A 168     3159   3942   3753    260   -147    135       C  
-ATOM   1310  N   TYR A 169      33.165  -1.876  11.736  1.00 18.67           N  
-ANISOU 1310  N   TYR A 169     2236   2364   2493    160    -77    -86       N  
-ATOM   1311  CA  TYR A 169      32.928  -1.571  10.325  1.00 20.33           C  
-ANISOU 1311  CA  TYR A 169     2431   2592   2699    183    -48   -116       C  
-ATOM   1312  C   TYR A 169      31.767  -0.583  10.148  1.00 21.39           C  
-ANISOU 1312  C   TYR A 169     2586   2705   2835    114    -35   -139       C  
-ATOM   1313  O   TYR A 169      31.734   0.125   9.156  1.00 19.39           O  
-ANISOU 1313  O   TYR A 169     2309   2485   2574    112    -15   -149       O  
-ATOM   1314  CB  TYR A 169      32.709  -2.862   9.504  1.00 19.81           C  
-ANISOU 1314  CB  TYR A 169     2409   2482   2636    262    -45   -151       C  
-ATOM   1315  CG  TYR A 169      34.046  -3.534   9.217  1.00 23.18           C  
-ANISOU 1315  CG  TYR A 169     2799   2957   3051    357    -43   -132       C  
-ATOM   1316  CD1 TYR A 169      34.506  -4.578   9.997  1.00 22.18           C  
-ANISOU 1316  CD1 TYR A 169     2695   2799   2932    400    -71   -116       C  
-ATOM   1317  CD2 TYR A 169      34.863  -3.073   8.192  1.00 25.26           C  
-ANISOU 1317  CD2 TYR A 169     2999   3306   3292    407    -11   -121       C  
-ATOM   1318  CE1 TYR A 169      35.741  -5.164   9.750  1.00 24.91           C  
-ANISOU 1318  CE1 TYR A 169     3002   3197   3267    498    -68    -95       C  
-ATOM   1319  CE2 TYR A 169      36.085  -3.635   7.938  1.00 27.31           C  
-ANISOU 1319  CE2 TYR A 169     3212   3626   3538    503     -1    -95       C  
-ATOM   1320  CZ  TYR A 169      36.527  -4.677   8.725  1.00 27.18           C  
-ANISOU 1320  CZ  TYR A 169     3218   3577   3532    552    -30    -84       C  
-ATOM   1321  OH  TYR A 169      37.750  -5.231   8.467  1.00 29.93           O  
-ANISOU 1321  OH  TYR A 169     3515   3991   3866    660    -18    -56       O  
-ATOM   1322  N   LYS A 170      30.837  -0.511  11.105  1.00 23.30           N  
-ANISOU 1322  N   LYS A 170     2870   2900   3082     63    -43   -141       N  
-ATOM   1323  CA  LYS A 170      29.773   0.508  11.026  1.00 25.04           C  
-ANISOU 1323  CA  LYS A 170     3104   3109   3300      9    -28   -157       C  
-ATOM   1324  C   LYS A 170      30.381   1.899  11.241  1.00 21.38           C  
-ANISOU 1324  C   LYS A 170     2610   2692   2820    -29    -36   -139       C  
-ATOM   1325  O   LYS A 170      30.027   2.853  10.562  1.00 18.96           O  
-ANISOU 1325  O   LYS A 170     2296   2396   2511    -52    -25   -151       O  
-ATOM   1326  CB  LYS A 170      28.663   0.240  12.051  1.00 32.95           C  
-ANISOU 1326  CB  LYS A 170     4151   4063   4306    -23    -26   -155       C  
-ATOM   1327  CG  LYS A 170      27.506   1.248  11.997  1.00 41.99           C  
-ANISOU 1327  CG  LYS A 170     5305   5202   5446    -63     -6   -170       C  
-ATOM   1328  CD  LYS A 170      26.190   0.632  12.488  1.00 48.06           C  
-ANISOU 1328  CD  LYS A 170     6101   5931   6230    -78      8   -164       C  
-ATOM   1329  CE  LYS A 170      25.028   1.638  12.476  1.00 52.61           C  
-ANISOU 1329  CE  LYS A 170     6677   6512   6801   -104     33   -173       C  
-ATOM   1330  NZ  LYS A 170      24.629   2.086  11.102  1.00 52.22           N  
-ANISOU 1330  NZ  LYS A 170     6609   6465   6769   -101     36   -202       N  
-ATOM   1331  N   THR A 171      31.312   1.994  12.194  1.00 21.43           N  
-ANISOU 1331  N   THR A 171     2605   2720   2817    -40    -64   -107       N  
-ATOM   1332  CA  THR A 171      32.045   3.231  12.440  1.00 23.62           C  
-ANISOU 1332  CA  THR A 171     2858   3034   3083    -84    -91    -82       C  
-ATOM   1333  C   THR A 171      32.886   3.608  11.232  1.00 24.01           C  
-ANISOU 1333  C   THR A 171     2839   3142   3142    -73    -83    -62       C  
-ATOM   1334  O   THR A 171      32.919   4.774  10.809  1.00 26.72           O  
-ANISOU 1334  O   THR A 171     3169   3501   3483   -115    -90    -53       O  
-ATOM   1335  CB  THR A 171      32.964   3.120  13.671  1.00 24.88           C  
-ANISOU 1335  CB  THR A 171     3015   3206   3232    -97   -136    -46       C  
-ATOM   1336  OG1 THR A 171      32.174   2.836  14.834  1.00 27.79           O  
-ANISOU 1336  OG1 THR A 171     3452   3527   3580   -106   -139    -59       O  
-ATOM   1337  CG2 THR A 171      33.745   4.424  13.872  1.00 23.97           C  
-ANISOU 1337  CG2 THR A 171     2877   3120   3110   -155   -182    -17       C  
-ATOM   1338  N   LEU A 172      33.576   2.623  10.675  1.00 19.51           N  
-ANISOU 1338  N   LEU A 172     2230   2605   2580    -10    -67    -51       N  
-ATOM   1339  CA  LEU A 172      34.372   2.854   9.478  1.00 20.65           C  
-ANISOU 1339  CA  LEU A 172     2305   2819   2724     20    -46    -26       C  
-ATOM   1340  C   LEU A 172      33.529   3.418   8.326  1.00 21.36           C  
-ANISOU 1340  C   LEU A 172     2411   2900   2806     14    -15    -58       C  
-ATOM   1341  O   LEU A 172      33.940   4.340   7.605  1.00 22.78           O  
-ANISOU 1341  O   LEU A 172     2546   3129   2982    -10     -8    -28       O  
-ATOM   1342  CB  LEU A 172      35.046   1.548   9.043  1.00 26.04           C  
-ANISOU 1342  CB  LEU A 172     2961   3530   3404    115    -26    -23       C  
-ATOM   1343  CG  LEU A 172      36.391   1.713   8.343  1.00 31.22           C  
-ANISOU 1343  CG  LEU A 172     3520   4288   4055    154    -10     34       C  
-ATOM   1344  CD1 LEU A 172      37.404   2.347   9.306  1.00 31.92           C  
-ANISOU 1344  CD1 LEU A 172     3548   4422   4160     95    -57    100       C  
-ATOM   1345  CD2 LEU A 172      36.905   0.363   7.817  1.00 33.31           C  
-ANISOU 1345  CD2 LEU A 172     3776   4575   4307    275     17     24       C  
-ATOM   1346  N   ARG A 173      32.339   2.862   8.156  1.00 18.95           N  
-ANISOU 1346  N   ARG A 173     2166   2531   2501     31     -1   -110       N  
-ATOM   1347  CA  ARG A 173      31.457   3.276   7.070  1.00 16.86           C  
-ANISOU 1347  CA  ARG A 173     1921   2254   2230     29     21   -141       C  
-ATOM   1348  C   ARG A 173      31.026   4.739   7.203  1.00 20.21           C  
-ANISOU 1348  C   ARG A 173     2351   2673   2655    -43     10   -133       C  
-ATOM   1349  O   ARG A 173      30.927   5.442   6.213  1.00 20.55           O  
-ANISOU 1349  O   ARG A 173     2379   2739   2690    -49     23   -131       O  
-ATOM   1350  CB  ARG A 173      30.229   2.367   7.017  1.00 17.68           C  
-ANISOU 1350  CB  ARG A 173     2086   2288   2344     49     24   -190       C  
-ATOM   1351  CG  ARG A 173      29.311   2.640   5.798  1.00 24.11           C  
-ANISOU 1351  CG  ARG A 173     2920   3088   3152     54     37   -224       C  
-ATOM   1352  CD  ARG A 173      27.985   1.902   5.911  1.00 22.43           C  
-ANISOU 1352  CD  ARG A 173     2760   2804   2960     49     26   -260       C  
-ATOM   1353  NE  ARG A 173      27.203   2.029   4.680  1.00 26.86           N  
-ANISOU 1353  NE  ARG A 173     3338   3353   3515     60     27   -291       N  
-ATOM   1354  CZ  ARG A 173      26.054   1.397   4.458  1.00 25.15           C  
-ANISOU 1354  CZ  ARG A 173     3159   3078   3317     54      8   -319       C  
-ATOM   1355  NH1 ARG A 173      25.556   0.603   5.387  1.00 24.98           N  
-ANISOU 1355  NH1 ARG A 173     3158   3009   3324     35     -8   -313       N  
-ATOM   1356  NH2 ARG A 173      25.410   1.556   3.312  1.00 22.27           N  
-ANISOU 1356  NH2 ARG A 173     2810   2706   2945     63      0   -345       N  
-ATOM   1357  N   ALA A 174      30.748   5.190   8.420  1.00 22.67           N  
-ANISOU 1357  N   ALA A 174     2692   2950   2970    -89    -15   -131       N  
-ATOM   1358  CA  ALA A 174      30.336   6.573   8.615  1.00 25.52           C  
-ANISOU 1358  CA  ALA A 174     3075   3294   3326   -146    -33   -130       C  
-ATOM   1359  C   ALA A 174      31.514   7.530   8.455  1.00 29.47           C  
-ANISOU 1359  C   ALA A 174     3530   3841   3826   -187    -62    -79       C  
-ATOM   1360  O   ALA A 174      31.409   8.541   7.740  1.00 25.11           O  
-ANISOU 1360  O   ALA A 174     2973   3295   3273   -217    -65    -68       O  
-ATOM   1361  CB  ALA A 174      29.701   6.745   9.960  1.00 25.23           C  
-ANISOU 1361  CB  ALA A 174     3095   3210   3281   -168    -50   -146       C  
-ATOM   1362  N   GLU A 175      32.627   7.209   9.128  1.00 31.51           N  
-ANISOU 1362  N   GLU A 175     3752   4131   4089   -193    -88    -40       N  
-ATOM   1363  CA  GLU A 175      33.830   8.042   9.094  1.00 33.36           C  
-ANISOU 1363  CA  GLU A 175     3930   4414   4332   -243   -127     24       C  
-ATOM   1364  C   GLU A 175      34.313   8.222   7.670  1.00 34.22           C  
-ANISOU 1364  C   GLU A 175     3969   4590   4443   -227    -93     60       C  
-ATOM   1365  O   GLU A 175      34.963   9.217   7.354  1.00 37.00           O  
-ANISOU 1365  O   GLU A 175     4280   4975   4803   -284   -119    116       O  
-ATOM   1366  CB  GLU A 175      34.962   7.433   9.942  1.00 34.48           C  
-ANISOU 1366  CB  GLU A 175     4029   4591   4481   -239   -159     65       C  
-ATOM   1367  CG  GLU A 175      34.743   7.468  11.458  1.00 36.04           C  
-ANISOU 1367  CG  GLU A 175     4294   4732   4667   -267   -208     46       C  
-ATOM   1368  CD  GLU A 175      34.933   8.855  12.065  1.00 40.75           C  
-ANISOU 1368  CD  GLU A 175     4927   5297   5258   -351   -280     64       C  
-ATOM   1369  OE1 GLU A 175      36.098   9.244  12.315  1.00 41.33           O  
-ANISOU 1369  OE1 GLU A 175     4948   5408   5347   -399   -338    126       O  
-ATOM   1370  OE2 GLU A 175      33.916   9.551  12.305  1.00 40.47           O  
-ANISOU 1370  OE2 GLU A 175     4975   5198   5204   -366   -283     19       O  
-ATOM   1371  N   GLN A 176      34.006   7.257   6.811  1.00 33.25           N  
-ANISOU 1371  N   GLN A 176     3839   4486   4310   -150    -37     31       N  
-ATOM   1372  CA  GLN A 176      34.408   7.325   5.411  1.00 37.44           C  
-ANISOU 1372  CA  GLN A 176     4314   5085   4827   -115      4     59       C  
-ATOM   1373  C   GLN A 176      33.228   7.551   4.458  1.00 37.20           C  
-ANISOU 1373  C   GLN A 176     4335   5018   4780   -101     32      9       C  
-ATOM   1374  O   GLN A 176      33.397   7.442   3.238  1.00 35.35           O  
-ANISOU 1374  O   GLN A 176     4073   4835   4523    -56     70     20       O  
-ATOM   1375  CB  GLN A 176      35.141   6.046   5.001  1.00 41.29           C  
-ANISOU 1375  CB  GLN A 176     4755   5632   5301    -20     43     66       C  
-ATOM   1376  CG  GLN A 176      36.574   5.935   5.517  1.00 45.54           C  
-ANISOU 1376  CG  GLN A 176     5204   6245   5853    -23     26    141       C  
-ATOM   1377  CD  GLN A 176      37.177   4.559   5.270  1.00 48.14           C  
-ANISOU 1377  CD  GLN A 176     5504   6620   6168     90     63    137       C  
-ATOM   1378  OE1 GLN A 176      36.533   3.679   4.692  1.00 46.83           O  
-ANISOU 1378  OE1 GLN A 176     5393   6420   5979    168     96     75       O  
-ATOM   1379  NE2 GLN A 176      38.419   4.368   5.708  1.00 49.26           N  
-ANISOU 1379  NE2 GLN A 176     5559   6833   6322    101     51    205       N  
-ATOM   1380  N   ALA A 177      32.058   7.862   5.021  1.00 37.55           N  
-ANISOU 1380  N   ALA A 177     4453   4982   4833   -132     12    -41       N  
-ATOM   1381  CA  ALA A 177      30.796   8.044   4.271  1.00 38.50           C  
-ANISOU 1381  CA  ALA A 177     4623   5062   4946   -120     29    -89       C  
-ATOM   1382  C   ALA A 177      30.566   6.981   3.190  1.00 41.16           C  
-ANISOU 1382  C   ALA A 177     4960   5416   5262    -42     66   -119       C  
-ATOM   1383  O   ALA A 177      30.257   7.312   2.039  1.00 42.44           O  
-ANISOU 1383  O   ALA A 177     5125   5596   5404    -27     84   -124       O  
-ATOM   1384  CB  ALA A 177      30.740   9.441   3.646  1.00 37.67           C  
-ANISOU 1384  CB  ALA A 177     4513   4964   4836   -171     17    -58       C  
-ATOM   1385  N   SER A 178      30.717   5.710   3.568  1.00 41.22           N  
-ANISOU 1385  N   SER A 178     4976   5414   5273      9     72   -142       N  
-ATOM   1386  CA  SER A 178      30.540   4.576   2.651  1.00 41.60           C  
-ANISOU 1386  CA  SER A 178     5045   5462   5300     90     93   -178       C  
-ATOM   1387  C   SER A 178      31.415   4.624   1.401  1.00 45.23           C  
-ANISOU 1387  C   SER A 178     5463   6005   5719    147    127   -151       C  
-ATOM   1388  O   SER A 178      31.029   4.087   0.360  1.00 46.20           O  
-ANISOU 1388  O   SER A 178     5621   6124   5810    209    141   -188       O  
-ATOM   1389  CB  SER A 178      29.079   4.461   2.215  1.00 38.76           C  
-ANISOU 1389  CB  SER A 178     4746   5036   4944     83     82   -232       C  
-ATOM   1390  OG  SER A 178      28.239   4.256   3.329  1.00 35.23           O  
-ANISOU 1390  OG  SER A 178     4330   4525   4531     44     60   -251       O  
-ATOM   1391  N   GLN A 179      32.588   5.245   1.505  1.00 48.14           N  
-ANISOU 1391  N   GLN A 179     5756   6450   6085    128    139    -82       N  
-ATOM   1392  CA  GLN A 179      33.588   5.203   0.437  1.00 53.75           C  
-ANISOU 1392  CA  GLN A 179     6407   7261   6755    192    183    -37       C  
-ATOM   1393  C   GLN A 179      34.801   4.390   0.899  1.00 57.60           C  
-ANISOU 1393  C   GLN A 179     6837   7807   7243    250    196     -1       C  
-ATOM   1394  O   GLN A 179      35.359   4.659   1.960  1.00 55.60           O  
-ANISOU 1394  O   GLN A 179     6541   7558   7026    195    168     39       O  
-ATOM   1395  CB  GLN A 179      34.031   6.616   0.033  1.00 57.44           C  
-ANISOU 1395  CB  GLN A 179     6815   7787   7222    121    187     37       C  
-ATOM   1396  CG  GLN A 179      32.945   7.685   0.103  1.00 59.56           C  
-ANISOU 1396  CG  GLN A 179     7136   7984   7509     37    154     16       C  
-ATOM   1397  CD  GLN A 179      31.961   7.610  -1.050  1.00 60.41           C  
-ANISOU 1397  CD  GLN A 179     7300   8070   7583     77    171    -33       C  
-ATOM   1398  OE1 GLN A 179      30.791   7.271  -0.861  1.00 60.95           O  
-ANISOU 1398  OE1 GLN A 179     7438   8057   7664     76    149   -101       O  
-ATOM   1399  NE2 GLN A 179      32.427   7.941  -2.251  1.00 61.10           N  
-ANISOU 1399  NE2 GLN A 179     7355   8234   7626    109    208      8       N  
-ATOM   1400  N   GLU A 180      35.214   3.405   0.108  1.00 64.60           N  
-ANISOU 1400  N   GLU A 180     7725   8735   8085    368    235    -18       N  
-ATOM   1401  CA  GLU A 180      36.346   2.559   0.485  1.00 68.99           C  
-ANISOU 1401  CA  GLU A 180     8228   9348   8638    445    250     13       C  
-ATOM   1402  C   GLU A 180      37.697   3.239   0.262  1.00 70.84           C  
-ANISOU 1402  C   GLU A 180     8331   9717   8866    440    284    120       C  
-ATOM   1403  O   GLU A 180      37.776   4.309  -0.343  1.00 71.22           O  
-ANISOU 1403  O   GLU A 180     8336   9816   8906    384    299    172       O  
-ATOM   1404  CB  GLU A 180      36.314   1.242  -0.293  1.00 72.48           C  
-ANISOU 1404  CB  GLU A 180     8729   9781   9028    589    277    -47       C  
-ATOM   1405  CG  GLU A 180      35.148   0.337   0.054  1.00 74.95           C  
-ANISOU 1405  CG  GLU A 180     9162   9959   9357    593    231   -140       C  
-ATOM   1406  CD  GLU A 180      35.371  -1.098  -0.395  1.00 77.67           C  
-ANISOU 1406  CD  GLU A 180     9569  10281   9660    735    237   -191       C  
-ATOM   1407  OE1 GLU A 180      36.289  -1.338  -1.213  1.00 78.88           O  
-ANISOU 1407  OE1 GLU A 180     9685  10530   9757    848    288   -167       O  
-ATOM   1408  OE2 GLU A 180      34.633  -1.988   0.078  1.00 77.90           O  
-ANISOU 1408  OE2 GLU A 180     9688  10199   9712    736    189   -251       O  
-ATOM   1409  N   VAL A 181      38.756   2.607   0.761  1.00 72.54           N  
-ANISOU 1409  N   VAL A 181     8481   9991   9090    497    291    162       N  
-ATOM   1410  CA  VAL A 181      40.122   3.055   0.502  1.00 73.83           C  
-ANISOU 1410  CA  VAL A 181     8503  10299   9249    509    327    275       C  
-ATOM   1411  C   VAL A 181      40.988   1.869   0.070  1.00 74.08           C  
-ANISOU 1411  C   VAL A 181     8499  10410   9236    676    380    281       C  
-ATOM   1412  O   VAL A 181      42.186   1.818   0.349  1.00 74.12           O  
-ANISOU 1412  O   VAL A 181     8385  10521   9254    704    396    369       O  
-ATOM   1413  CB  VAL A 181      40.755   3.738   1.740  1.00 74.10           C  
-ANISOU 1413  CB  VAL A 181     8461  10344   9350    390    268    349       C  
-ATOM   1414  CG1 VAL A 181      39.899   4.914   2.201  1.00 73.02           C  
-ANISOU 1414  CG1 VAL A 181     8376  10119   9248    240    211    335       C  
-ATOM   1415  CG2 VAL A 181      40.957   2.736   2.871  1.00 73.75           C  
-ANISOU 1415  CG2 VAL A 181     8440  10251   9332    426    231    319       C  
-ATOM   1416  N   THR A 186      43.118  -1.501   8.341  1.00 69.10           N  
-ANISOU 1416  N   THR A 186     7867   9530   8858    581     27    327       N  
-ATOM   1417  CA  THR A 186      41.853  -2.129   8.692  1.00 67.06           C  
-ANISOU 1417  CA  THR A 186     7757   9130   8592    576     10    231       C  
-ATOM   1418  C   THR A 186      42.090  -3.449   9.421  1.00 66.79           C  
-ANISOU 1418  C   THR A 186     7767   9047   8562    661    -17    216       C  
-ATOM   1419  O   THR A 186      41.770  -3.574  10.604  1.00 68.54           O  
-ANISOU 1419  O   THR A 186     8041   9199   8804    597    -72    210       O  
-ATOM   1420  CB  THR A 186      40.977  -2.365   7.439  1.00 67.25           C  
-ANISOU 1420  CB  THR A 186     7854   9118   8581    632     63    159       C  
-ATOM   1421  OG1 THR A 186      39.812  -3.125   7.791  1.00 65.38           O  
-ANISOU 1421  OG1 THR A 186     7750   8746   8345    630     39     78       O  
-ATOM   1422  CG2 THR A 186      41.764  -3.098   6.350  1.00 68.46           C  
-ANISOU 1422  CG2 THR A 186     7963   9354   8696    791    122    169       C  
-ATOM   1423  N   GLU A 187      42.659  -4.423   8.715  1.00 65.36           N  
-ANISOU 1423  N   GLU A 187     7573   8905   8358    812     22    211       N  
-ATOM   1424  CA  GLU A 187      42.939  -5.736   9.288  1.00 64.02           C  
-ANISOU 1424  CA  GLU A 187     7450   8684   8189    910     -5    197       C  
-ATOM   1425  C   GLU A 187      43.737  -5.610  10.576  1.00 61.63           C  
-ANISOU 1425  C   GLU A 187     7081   8415   7921    860    -63    268       C  
-ATOM   1426  O   GLU A 187      43.407  -6.232  11.592  1.00 61.14           O  
-ANISOU 1426  O   GLU A 187     7095   8263   7872    843   -114    250       O  
-ATOM   1427  CB  GLU A 187      43.709  -6.618   8.298  1.00 67.54           C  
-ANISOU 1427  CB  GLU A 187     7868   9195   8599   1095     47    196       C  
-ATOM   1428  CG  GLU A 187      44.406  -7.806   8.964  1.00 71.55           C  
-ANISOU 1428  CG  GLU A 187     8387   9686   9114   1207     15    211       C  
-ATOM   1429  CD  GLU A 187      45.305  -8.594   8.020  1.00 75.12           C  
-ANISOU 1429  CD  GLU A 187     8799  10219   9524   1408     70    218       C  
-ATOM   1430  OE1 GLU A 187      45.812  -8.015   7.035  1.00 76.60           O  
-ANISOU 1430  OE1 GLU A 187     8892  10531   9683   1451    137    252       O  
-ATOM   1431  OE2 GLU A 187      45.506  -9.801   8.269  1.00 76.04           O  
-ANISOU 1431  OE2 GLU A 187     8984  10275   9633   1528     46    192       O  
-ATOM   1432  N   THR A 188      44.786  -4.793  10.525  1.00 53.39           N  
-ANISOU 1432  N   THR A 188     5893   7502   6891    833    -59    355       N  
-ATOM   1433  CA  THR A 188      45.712  -4.679  11.638  1.00 44.91           C  
-ANISOU 1433  CA  THR A 188     4739   6475   5848    795   -121    433       C  
-ATOM   1434  C   THR A 188      45.094  -3.950  12.825  1.00 33.97           C  
-ANISOU 1434  C   THR A 188     3414   5012   4482    635   -193    426       C  
-ATOM   1435  O   THR A 188      45.255  -4.381  13.968  1.00 32.90           O  
-ANISOU 1435  O   THR A 188     3309   4835   4356    621   -254    439       O  
-ATOM   1436  CB  THR A 188      47.003  -3.956  11.219  1.00 47.50           C  
-ANISOU 1436  CB  THR A 188     4885   6969   6192    797   -105    541       C  
-ATOM   1437  OG1 THR A 188      47.598  -4.642  10.110  1.00 50.24           O  
-ANISOU 1437  OG1 THR A 188     5175   7404   6511    965    -26    552       O  
-ATOM   1438  CG2 THR A 188      47.987  -3.936  12.374  1.00 47.97           C  
-ANISOU 1438  CG2 THR A 188     4861   7076   6288    762   -182    625       C  
-ATOM   1439  N   LEU A 189      44.407  -2.843  12.563  1.00 29.13           N  
-ANISOU 1439  N   LEU A 189     2821   4381   3868    523   -187    406       N  
-ATOM   1440  CA  LEU A 189      43.762  -2.102  13.644  1.00 30.88           C  
-ANISOU 1440  CA  LEU A 189     3111   4527   4095    386   -249    391       C  
-ATOM   1441  C   LEU A 189      42.637  -2.939  14.296  1.00 26.34           C  
-ANISOU 1441  C   LEU A 189     2683   3823   3505    397   -257    316       C  
-ATOM   1442  O   LEU A 189      42.430  -2.891  15.512  1.00 25.84           O  
-ANISOU 1442  O   LEU A 189     2673   3708   3439    337   -314    319       O  
-ATOM   1443  CB  LEU A 189      43.214  -0.772  13.132  1.00 29.79           C  
-ANISOU 1443  CB  LEU A 189     2972   4390   3955    282   -238    382       C  
-ATOM   1444  CG  LEU A 189      42.668   0.157  14.210  1.00 31.23           C  
-ANISOU 1444  CG  LEU A 189     3223   4505   4137    150   -305    370       C  
-ATOM   1445  CD1 LEU A 189      43.816   0.697  15.044  1.00 36.12           C  
-ANISOU 1445  CD1 LEU A 189     3762   5185   4779     88   -388    454       C  
-ATOM   1446  CD2 LEU A 189      41.879   1.295  13.563  1.00 34.70           C  
-ANISOU 1446  CD2 LEU A 189     3690   4922   4571     73   -283    341       C  
-ATOM   1447  N   LEU A 190      41.926  -3.709  13.481  1.00 25.89           N  
-ANISOU 1447  N   LEU A 190     2688   3714   3434    474   -203    254       N  
-ATOM   1448  CA  LEU A 190      40.900  -4.598  14.006  1.00 26.28           C  
-ANISOU 1448  CA  LEU A 190     2865   3646   3476    483   -213    198       C  
-ATOM   1449  C   LEU A 190      41.464  -5.601  15.000  1.00 27.15           C  
-ANISOU 1449  C   LEU A 190     2991   3734   3591    535   -259    227       C  
-ATOM   1450  O   LEU A 190      40.858  -5.856  16.032  1.00 28.29           O  
-ANISOU 1450  O   LEU A 190     3215   3802   3731    485   -294    218       O  
-ATOM   1451  CB  LEU A 190      40.198  -5.352  12.872  1.00 27.77           C  
-ANISOU 1451  CB  LEU A 190     3114   3784   3654    563   -163    134       C  
-ATOM   1452  CG  LEU A 190      39.032  -6.230  13.373  1.00 26.25           C  
-ANISOU 1452  CG  LEU A 190     3048   3462   3463    552   -181     85       C  
-ATOM   1453  CD1 LEU A 190      37.842  -5.403  13.768  1.00 23.83           C  
-ANISOU 1453  CD1 LEU A 190     2790   3108   3156    432   -181     61       C  
-ATOM   1454  CD2 LEU A 190      38.646  -7.229  12.289  1.00 29.72           C  
-ANISOU 1454  CD2 LEU A 190     3548   3849   3895    651   -156     31       C  
-ATOM   1455  N   VAL A 191      42.629  -6.165  14.696  1.00 29.03           N  
-ANISOU 1455  N   VAL A 191     3151   4044   3836    639   -256    268       N  
-ATOM   1456  CA  VAL A 191      43.287  -7.054  15.638  1.00 28.12           C  
-ANISOU 1456  CA  VAL A 191     3040   3918   3728    693   -306    305       C  
-ATOM   1457  C   VAL A 191      43.778  -6.276  16.854  1.00 29.58           C  
-ANISOU 1457  C   VAL A 191     3181   4138   3919    591   -372    364       C  
-ATOM   1458  O   VAL A 191      43.590  -6.723  17.978  1.00 28.74           O  
-ANISOU 1458  O   VAL A 191     3142   3971   3806    569   -422    370       O  
-ATOM   1459  CB  VAL A 191      44.468  -7.805  15.008  1.00 28.50           C  
-ANISOU 1459  CB  VAL A 191     3004   4045   3779    843   -286    340       C  
-ATOM   1460  CG1 VAL A 191      45.179  -8.627  16.067  1.00 24.92           C  
-ANISOU 1460  CG1 VAL A 191     2550   3583   3336    893   -346    386       C  
-ATOM   1461  CG2 VAL A 191      43.976  -8.692  13.850  1.00 30.92           C  
-ANISOU 1461  CG2 VAL A 191     3382   4300   4067    960   -231    272       C  
-ATOM   1462  N   GLN A 192      44.380  -5.107  16.625  1.00 29.83           N  
-ANISOU 1462  N   GLN A 192     3110   4263   3961    526   -379    408       N  
-ATOM   1463  CA  GLN A 192      44.926  -4.288  17.712  1.00 31.99           C  
-ANISOU 1463  CA  GLN A 192     3346   4569   4242    424   -458    464       C  
-ATOM   1464  C   GLN A 192      43.874  -3.878  18.747  1.00 30.06           C  
-ANISOU 1464  C   GLN A 192     3225   4225   3969    322   -494    422       C  
-ATOM   1465  O   GLN A 192      44.152  -3.839  19.943  1.00 31.12           O  
-ANISOU 1465  O   GLN A 192     3387   4346   4093    281   -566    451       O  
-ATOM   1466  CB  GLN A 192      45.589  -3.028  17.150  1.00 34.85           C  
-ANISOU 1466  CB  GLN A 192     3588   5031   4623    356   -463    516       C  
-ATOM   1467  CG  GLN A 192      46.269  -2.128  18.203  1.00 37.65           C  
-ANISOU 1467  CG  GLN A 192     3900   5417   4989    244   -564    580       C  
-ATOM   1468  CD  GLN A 192      47.516  -2.757  18.823  1.00 40.49           C  
-ANISOU 1468  CD  GLN A 192     4172   5845   5369    299   -622    659       C  
-ATOM   1469  OE1 GLN A 192      47.436  -3.769  19.521  1.00 43.39           O  
-ANISOU 1469  OE1 GLN A 192     4604   6161   5722    362   -640    644       O  
-ATOM   1470  NE2 GLN A 192      48.674  -2.158  18.569  1.00 41.20           N  
-ANISOU 1470  NE2 GLN A 192     4109   6051   5493    272   -655    751       N  
-ATOM   1471  N   ASN A 193      42.676  -3.548  18.283  1.00 28.64           N  
-ANISOU 1471  N   ASN A 193     3121   3984   3775    286   -445    357       N  
-ATOM   1472  CA  ASN A 193      41.623  -3.089  19.180  1.00 26.18           C  
-ANISOU 1472  CA  ASN A 193     2920   3594   3434    200   -465    321       C  
-ATOM   1473  C   ASN A 193      40.772  -4.251  19.725  1.00 27.48           C  
-ANISOU 1473  C   ASN A 193     3191   3669   3583    242   -450    289       C  
-ATOM   1474  O   ASN A 193      39.798  -4.021  20.446  1.00 27.67           O  
-ANISOU 1474  O   ASN A 193     3305   3632   3578    185   -452    264       O  
-ATOM   1475  CB  ASN A 193      40.735  -2.061  18.469  1.00 25.20           C  
-ANISOU 1475  CB  ASN A 193     2815   3453   3304    138   -423    275       C  
-ATOM   1476  CG  ASN A 193      41.474  -0.752  18.158  1.00 29.04           C  
-ANISOU 1476  CG  ASN A 193     3218   4013   3805     69   -454    314       C  
-ATOM   1477  OD1 ASN A 193      42.640  -0.581  18.510  1.00 30.91           O  
-ANISOU 1477  OD1 ASN A 193     3374   4313   4057     58   -511    379       O  
-ATOM   1478  ND2 ASN A 193      40.791   0.164  17.478  1.00 31.87           N  
-ANISOU 1478  ND2 ASN A 193     3591   4359   4161     19   -421    281       N  
-ATOM   1479  N   ALA A 194      41.140  -5.490  19.382  1.00 27.16           N  
-ANISOU 1479  N   ALA A 194     3141   3620   3559    342   -437    296       N  
-ATOM   1480  CA  ALA A 194      40.487  -6.673  19.941  1.00 25.50           C  
-ANISOU 1480  CA  ALA A 194     3028   3320   3341    378   -439    283       C  
-ATOM   1481  C   ALA A 194      40.866  -6.829  21.408  1.00 27.75           C  
-ANISOU 1481  C   ALA A 194     3343   3597   3602    352   -506    329       C  
-ATOM   1482  O   ALA A 194      41.881  -6.280  21.832  1.00 29.72           O  
-ANISOU 1482  O   ALA A 194     3525   3915   3850    334   -557    373       O  
-ATOM   1483  CB  ALA A 194      40.873  -7.917  19.159  1.00 28.68           C  
-ANISOU 1483  CB  ALA A 194     3423   3708   3766    500   -420    276       C  
-ATOM   1484  N   ASN A 195      40.078  -7.574  22.189  1.00 26.99           N  
-ANISOU 1484  N   ASN A 195     3347   3420   3486    346   -511    326       N  
-ATOM   1485  CA  ASN A 195      40.434  -7.727  23.606  1.00 30.58           C  
-ANISOU 1485  CA  ASN A 195     3839   3871   3909    325   -573    373       C  
-ATOM   1486  C   ASN A 195      41.585  -8.718  23.725  1.00 31.64           C  
-ANISOU 1486  C   ASN A 195     3932   4025   4065    417   -617    418       C  
-ATOM   1487  O   ASN A 195      41.933  -9.383  22.743  1.00 29.84           O  
-ANISOU 1487  O   ASN A 195     3665   3799   3872    504   -591    407       O  
-ATOM   1488  CB  ASN A 195      39.209  -8.115  24.483  1.00 21.97           C  
-ANISOU 1488  CB  ASN A 195     2864   2701   2781    283   -559    369       C  
-ATOM   1489  CG  ASN A 195      38.647  -9.502  24.201  1.00 25.90           C  
-ANISOU 1489  CG  ASN A 195     3418   3118   3306    337   -538    368       C  
-ATOM   1490  OD1 ASN A 195      39.367 -10.444  23.863  1.00 27.88           O  
-ANISOU 1490  OD1 ASN A 195     3651   3357   3587    421   -560    383       O  
-ATOM   1491  ND2 ASN A 195      37.335  -9.639  24.387  1.00 28.23           N  
-ANISOU 1491  ND2 ASN A 195     3784   3353   3588    288   -500    356       N  
-ATOM   1492  N   PRO A 196      42.214  -8.788  24.912  1.00 32.07           N  
-ANISOU 1492  N   PRO A 196     3996   4095   4094    406   -688    469       N  
-ATOM   1493  CA  PRO A 196      43.415  -9.611  25.091  1.00 33.35           C  
-ANISOU 1493  CA  PRO A 196     4105   4288   4278    495   -738    521       C  
-ATOM   1494  C   PRO A 196      43.302 -11.044  24.567  1.00 33.09           C  
-ANISOU 1494  C   PRO A 196     4110   4190   4273    603   -714    513       C  
-ATOM   1495  O   PRO A 196      44.161 -11.472  23.799  1.00 34.22           O  
-ANISOU 1495  O   PRO A 196     4178   4375   4448    702   -709    521       O  
-ATOM   1496  CB  PRO A 196      43.608  -9.609  26.619  1.00 35.61           C  
-ANISOU 1496  CB  PRO A 196     4447   4564   4518    453   -814    568       C  
-ATOM   1497  CG  PRO A 196      43.048  -8.294  27.047  1.00 35.36           C  
-ANISOU 1497  CG  PRO A 196     4445   4546   4444    342   -816    543       C  
-ATOM   1498  CD  PRO A 196      41.840  -8.086  26.153  1.00 32.67           C  
-ANISOU 1498  CD  PRO A 196     4137   4164   4113    319   -726    481       C  
-ATOM   1499  N   ASP A 197      42.269 -11.773  24.974  1.00 34.60           N  
-ANISOU 1499  N   ASP A 197     4417   4280   4450    588   -702    501       N  
-ATOM   1500  CA  ASP A 197      42.130 -13.184  24.613  1.00 37.45           C  
-ANISOU 1500  CA  ASP A 197     4837   4557   4837    680   -700    497       C  
-ATOM   1501  C   ASP A 197      41.901 -13.394  23.112  1.00 37.10           C  
-ANISOU 1501  C   ASP A 197     4774   4497   4826    740   -644    438       C  
-ATOM   1502  O   ASP A 197      42.477 -14.301  22.506  1.00 38.22           O  
-ANISOU 1502  O   ASP A 197     4910   4620   4990    859   -651    434       O  
-ATOM   1503  CB  ASP A 197      40.978 -13.822  25.400  1.00 40.81           C  
-ANISOU 1503  CB  ASP A 197     5387   4877   5242    625   -704    510       C  
-ATOM   1504  CG  ASP A 197      41.245 -13.868  26.902  1.00 45.50           C  
-ANISOU 1504  CG  ASP A 197     6018   5478   5793    591   -761    573       C  
-ATOM   1505  OD1 ASP A 197      42.424 -13.777  27.316  1.00 45.63           O  
-ANISOU 1505  OD1 ASP A 197     5975   5558   5805    633   -816    611       O  
-ATOM   1506  OD2 ASP A 197      40.266 -13.995  27.668  1.00 47.99           O  
-ANISOU 1506  OD2 ASP A 197     6419   5739   6075    523   -752    591       O  
-ATOM   1507  N   CYS A 198      41.045 -12.566  22.519  1.00 32.97           N  
-ANISOU 1507  N   CYS A 198     4247   3979   4300    666   -590    391       N  
-ATOM   1508  CA  CYS A 198      40.815 -12.627  21.086  1.00 33.24           C  
-ANISOU 1508  CA  CYS A 198     4264   4007   4357    716   -540    334       C  
-ATOM   1509  C   CYS A 198      42.062 -12.190  20.309  1.00 36.26           C  
-ANISOU 1509  C   CYS A 198     4524   4504   4749    793   -526    341       C  
-ATOM   1510  O   CYS A 198      42.417 -12.809  19.295  1.00 35.57           O  
-ANISOU 1510  O   CYS A 198     4426   4415   4674    906   -503    315       O  
-ATOM   1511  CB  CYS A 198      39.607 -11.765  20.700  1.00 33.92           C  
-ANISOU 1511  CB  CYS A 198     4371   4080   4437    613   -490    290       C  
-ATOM   1512  SG  CYS A 198      38.003 -12.536  21.091  1.00 42.87           S  
-ANISOU 1512  SG  CYS A 198     5635   5079   5574    549   -488    281       S  
-ATOM   1513  N   LYS A 199      42.736 -11.144  20.786  1.00 36.03           N  
-ANISOU 1513  N   LYS A 199     4404   4573   4711    736   -543    380       N  
-ATOM   1514  CA  LYS A 199      43.951 -10.671  20.121  1.00 36.66           C  
-ANISOU 1514  CA  LYS A 199     4350   4775   4806    794   -534    407       C  
-ATOM   1515  C   LYS A 199      45.002 -11.786  20.060  1.00 39.25           C  
-ANISOU 1515  C   LYS A 199     4645   5120   5147    941   -557    442       C  
-ATOM   1516  O   LYS A 199      45.724 -11.921  19.071  1.00 39.62           O  
-ANISOU 1516  O   LYS A 199     4612   5238   5203   1046   -521    443       O  
-ATOM   1517  CB  LYS A 199      44.530  -9.435  20.826  1.00 36.66           C  
-ANISOU 1517  CB  LYS A 199     4267   4863   4801    694   -574    456       C  
-ATOM   1518  CG  LYS A 199      45.684  -8.778  20.047  1.00 37.68           C  
-ANISOU 1518  CG  LYS A 199     4239   5125   4951    726   -561    497       C  
-ATOM   1519  CD  LYS A 199      46.351  -7.642  20.822  1.00 39.25           C  
-ANISOU 1519  CD  LYS A 199     4360   5400   5152    620   -626    556       C  
-ATOM   1520  CE  LYS A 199      45.481  -6.405  20.877  1.00 38.23           C  
-ANISOU 1520  CE  LYS A 199     4274   5246   5006    485   -618    519       C  
-ATOM   1521  NZ  LYS A 199      46.051  -5.299  21.702  1.00 38.92           N  
-ANISOU 1521  NZ  LYS A 199     4316   5383   5090    376   -698    569       N  
-ATOM   1522  N   THR A 200      45.068 -12.592  21.114  1.00 38.58           N  
-ANISOU 1522  N   THR A 200     4627   4973   5058    957   -615    472       N  
-ATOM   1523  CA  THR A 200      46.024 -13.691  21.182  1.00 39.14           C  
-ANISOU 1523  CA  THR A 200     4681   5049   5140   1100   -647    507       C  
-ATOM   1524  C   THR A 200      45.753 -14.733  20.105  1.00 39.45           C  
-ANISOU 1524  C   THR A 200     4787   5017   5184   1230   -608    451       C  
-ATOM   1525  O   THR A 200      46.666 -15.154  19.379  1.00 40.65           O  
-ANISOU 1525  O   THR A 200     4873   5231   5342   1375   -589    459       O  
-ATOM   1526  CB  THR A 200      45.989 -14.378  22.560  1.00 40.31           C  
-ANISOU 1526  CB  THR A 200     4910   5126   5279   1082   -722    550       C  
-ATOM   1527  OG1 THR A 200      46.450 -13.461  23.558  1.00 40.15           O  
-ANISOU 1527  OG1 THR A 200     4828   5181   5246    984   -771    604       O  
-ATOM   1528  CG2 THR A 200      46.879 -15.620  22.562  1.00 41.87           C  
-ANISOU 1528  CG2 THR A 200     5109   5310   5491   1243   -756    580       C  
-ATOM   1529  N   ILE A 201      44.493 -15.151  20.023  1.00 36.92           N  
-ANISOU 1529  N   ILE A 201     4600   4569   4861   1181   -600    398       N  
-ATOM   1530  CA  ILE A 201      44.042 -16.099  19.009  1.00 39.05           C  
-ANISOU 1530  CA  ILE A 201     4960   4746   5133   1282   -578    335       C  
-ATOM   1531  C   ILE A 201      44.312 -15.564  17.598  1.00 36.81           C  
-ANISOU 1531  C   ILE A 201     4599   4547   4840   1344   -508    293       C  
-ATOM   1532  O   ILE A 201      44.768 -16.299  16.716  1.00 37.41           O  
-ANISOU 1532  O   ILE A 201     4689   4617   4907   1499   -491    264       O  
-ATOM   1533  CB  ILE A 201      42.531 -16.407  19.184  1.00 40.64           C  
-ANISOU 1533  CB  ILE A 201     5299   4805   5338   1178   -587    297       C  
-ATOM   1534  CG1 ILE A 201      42.327 -17.324  20.393  1.00 41.63           C  
-ANISOU 1534  CG1 ILE A 201     5519   4831   5469   1159   -655    343       C  
-ATOM   1535  CG2 ILE A 201      41.948 -17.019  17.911  1.00 41.34           C  
-ANISOU 1535  CG2 ILE A 201     5468   4811   5429   1249   -564    221       C  
-ATOM   1536  CD1 ILE A 201      40.904 -17.348  20.938  1.00 41.29           C  
-ANISOU 1536  CD1 ILE A 201     5573   4686   5428   1019   -662    341       C  
-ATOM   1537  N   LEU A 202      44.055 -14.273  17.412  1.00 33.60           N  
-ANISOU 1537  N   LEU A 202     4117   4219   4431   1230   -469    292       N  
-ATOM   1538  CA  LEU A 202      44.208 -13.601  16.121  1.00 35.31           C  
-ANISOU 1538  CA  LEU A 202     4259   4520   4636   1263   -401    261       C  
-ATOM   1539  C   LEU A 202      45.665 -13.453  15.671  1.00 40.63           C  
-ANISOU 1539  C   LEU A 202     4789   5343   5307   1383   -376    312       C  
-ATOM   1540  O   LEU A 202      45.980 -13.679  14.503  1.00 39.46           O  
-ANISOU 1540  O   LEU A 202     4617   5237   5139   1505   -323    283       O  
-ATOM   1541  CB  LEU A 202      43.545 -12.222  16.177  1.00 33.61           C  
-ANISOU 1541  CB  LEU A 202     4006   4343   4421   1100   -376    256       C  
-ATOM   1542  CG  LEU A 202      42.012 -12.279  16.223  1.00 33.15           C  
-ANISOU 1542  CG  LEU A 202     4072   4160   4362   1002   -376    199       C  
-ATOM   1543  CD1 LEU A 202      41.406 -10.927  16.487  1.00 35.34           C  
-ANISOU 1543  CD1 LEU A 202     4315   4474   4638    851   -358    201       C  
-ATOM   1544  CD2 LEU A 202      41.507 -12.836  14.901  1.00 32.86           C  
-ANISOU 1544  CD2 LEU A 202     4100   4068   4317   1084   -341    129       C  
-ATOM   1545  N   LYS A 203      46.541 -13.055  16.592  1.00 44.37           N  
-ANISOU 1545  N   LYS A 203     5162   5900   5796   1347   -415    391       N  
-ATOM   1546  CA  LYS A 203      47.964 -12.907  16.284  1.00 50.82           C  
-ANISOU 1546  CA  LYS A 203     5821   6870   6620   1450   -399    460       C  
-ATOM   1547  C   LYS A 203      48.556 -14.237  15.828  1.00 53.96           C  
-ANISOU 1547  C   LYS A 203     6249   7250   7005   1660   -390    449       C  
-ATOM   1548  O   LYS A 203      49.414 -14.284  14.944  1.00 54.92           O  
-ANISOU 1548  O   LYS A 203     6269   7484   7113   1794   -336    470       O  
-ATOM   1549  CB  LYS A 203      48.733 -12.386  17.504  1.00 52.34           C  
-ANISOU 1549  CB  LYS A 203     5919   7133   6836   1367   -467    549       C  
-ATOM   1550  CG  LYS A 203      48.293 -11.002  17.972  1.00 53.83           C  
-ANISOU 1550  CG  LYS A 203     6079   7344   7030   1172   -485    561       C  
-ATOM   1551  CD  LYS A 203      48.710 -10.748  19.419  1.00 58.10           C  
-ANISOU 1551  CD  LYS A 203     6601   7891   7581   1084   -577    624       C  
-ATOM   1552  CE  LYS A 203      50.152 -10.257  19.523  1.00 61.69           C  
-ANISOU 1552  CE  LYS A 203     6875   8502   8063   1102   -609    724       C  
-ATOM   1553  NZ  LYS A 203      50.212  -8.773  19.707  1.00 61.38           N  
-ANISOU 1553  NZ  LYS A 203     6761   8527   8033    938   -635    757       N  
-ATOM   1554  N   ALA A 204      48.085 -15.317  16.442  1.00 54.14           N  
-ANISOU 1554  N   ALA A 204     6414   7129   7029   1691   -444    419       N  
-ATOM   1555  CA  ALA A 204      48.583 -16.654  16.154  1.00 54.76           C  
-ANISOU 1555  CA  ALA A 204     6550   7160   7096   1890   -454    405       C  
-ATOM   1556  C   ALA A 204      48.008 -17.227  14.865  1.00 57.51           C  
-ANISOU 1556  C   ALA A 204     7005   7435   7412   1998   -406    312       C  
-ATOM   1557  O   ALA A 204      48.370 -18.330  14.464  1.00 58.16           O  
-ANISOU 1557  O   ALA A 204     7155   7467   7475   2178   -414    286       O  
-ATOM   1558  CB  ALA A 204      48.279 -17.577  17.309  1.00 54.05           C  
-ANISOU 1558  CB  ALA A 204     6581   6934   7021   1873   -540    415       C  
-ATOM   1559  N   LEU A 205      47.106 -16.490  14.224  1.00 58.48           N  
-ANISOU 1559  N   LEU A 205     7152   7544   7525   1892   -365    261       N  
-ATOM   1560  CA  LEU A 205      46.571 -16.907  12.933  1.00 62.01           C  
-ANISOU 1560  CA  LEU A 205     7693   7932   7935   1985   -323    174       C  
-ATOM   1561  C   LEU A 205      47.539 -16.532  11.824  1.00 67.29           C  
-ANISOU 1561  C   LEU A 205     8233   8765   8567   2125   -239    189       C  
-ATOM   1562  O   LEU A 205      47.548 -17.146  10.758  1.00 70.77           O  
-ANISOU 1562  O   LEU A 205     8744   9184   8963   2281   -205    128       O  
-ATOM   1563  CB  LEU A 205      45.204 -16.269  12.672  1.00 61.08           C  
-ANISOU 1563  CB  LEU A 205     7647   7739   7821   1819   -314    118       C  
-ATOM   1564  CG  LEU A 205      43.957 -16.972  13.207  1.00 60.26           C  
-ANISOU 1564  CG  LEU A 205     7716   7443   7738   1731   -381     74       C  
-ATOM   1565  CD1 LEU A 205      42.785 -16.004  13.211  1.00 58.52           C  
-ANISOU 1565  CD1 LEU A 205     7503   7202   7529   1543   -365     52       C  
-ATOM   1566  CD2 LEU A 205      43.632 -18.204  12.367  1.00 61.26           C  
-ANISOU 1566  CD2 LEU A 205     7997   7439   7840   1873   -404     -4       C  
-ATOM   1567  N   GLY A 206      48.355 -15.517  12.089  1.00 68.87           N  
-ANISOU 1567  N   GLY A 206     8249   9134   8786   2066   -210    276       N  
-ATOM   1568  CA  GLY A 206      49.280 -14.996  11.100  1.00 70.10           C  
-ANISOU 1568  CA  GLY A 206     8254   9469   8913   2170   -126    316       C  
-ATOM   1569  C   GLY A 206      48.610 -13.943  10.239  1.00 70.39           C  
-ANISOU 1569  C   GLY A 206     8273   9542   8932   2063    -68    285       C  
-ATOM   1570  O   GLY A 206      47.390 -13.779  10.294  1.00 70.43           O  
-ANISOU 1570  O   GLY A 206     8398   9420   8943   1939    -92    219       O  
-ATOM   1571  N   PRO A 207      49.403 -13.215   9.440  1.00 70.25           N  
-ANISOU 1571  N   PRO A 207     8098   9701   8893   2111      9    342       N  
-ATOM   1572  CA  PRO A 207      48.844 -12.224   8.517  1.00 67.65           C  
-ANISOU 1572  CA  PRO A 207     7748   9413   8541   2026     68    319       C  
-ATOM   1573  C   PRO A 207      48.013 -12.888   7.423  1.00 64.14           C  
-ANISOU 1573  C   PRO A 207     7468   8865   8036   2130     98    204       C  
-ATOM   1574  O   PRO A 207      48.211 -14.071   7.133  1.00 65.03           O  
-ANISOU 1574  O   PRO A 207     7675   8920   8114   2311     93    157       O  
-ATOM   1575  CB  PRO A 207      50.088 -11.546   7.920  1.00 69.82           C  
-ANISOU 1575  CB  PRO A 207     7813   9910   8804   2093    144    423       C  
-ATOM   1576  CG  PRO A 207      51.214 -11.905   8.833  1.00 71.44           C  
-ANISOU 1576  CG  PRO A 207     7912  10184   9047   2134    104    511       C  
-ATOM   1577  CD  PRO A 207      50.872 -13.260   9.374  1.00 71.76           C  
-ANISOU 1577  CD  PRO A 207     8116  10066   9083   2235     45    440       C  
-ATOM   1578  N   GLY A 208      47.085 -12.138   6.838  1.00 60.38           N  
-ANISOU 1578  N   GLY A 208     7034   8359   7549   2016    119    159       N  
-ATOM   1579  CA  GLY A 208      46.331 -12.619   5.693  1.00 57.88           C  
-ANISOU 1579  CA  GLY A 208     6858   7961   7171   2104    145     58       C  
-ATOM   1580  C   GLY A 208      45.145 -13.521   5.993  1.00 53.08           C  
-ANISOU 1580  C   GLY A 208     6458   7137   6575   2073     66    -41       C  
-ATOM   1581  O   GLY A 208      44.554 -14.098   5.071  1.00 50.58           O  
-ANISOU 1581  O   GLY A 208     6276   6734   6208   2159     68   -129       O  
-ATOM   1582  N   ALA A 209      44.804 -13.665   7.273  1.00 49.06           N  
-ANISOU 1582  N   ALA A 209     5975   6537   6127   1951     -7    -21       N  
-ATOM   1583  CA  ALA A 209      43.557 -14.319   7.647  1.00 44.71           C  
-ANISOU 1583  CA  ALA A 209     5598   5790   5598   1874    -81    -93       C  
-ATOM   1584  C   ALA A 209      42.405 -13.518   7.071  1.00 41.68           C  
-ANISOU 1584  C   ALA A 209     5252   5374   5212   1741    -66   -138       C  
-ATOM   1585  O   ALA A 209      42.416 -12.292   7.119  1.00 42.01           O  
-ANISOU 1585  O   ALA A 209     5181   5513   5267   1625    -29    -94       O  
-ATOM   1586  CB  ALA A 209      43.420 -14.431   9.163  1.00 43.41           C  
-ANISOU 1586  CB  ALA A 209     5434   5565   5495   1754   -148    -45       C  
-ATOM   1587  N   THR A 210      41.416 -14.204   6.518  1.00 40.02           N  
-ANISOU 1587  N   THR A 210     5200   5020   4985   1758   -103   -224       N  
-ATOM   1588  CA  THR A 210      40.197 -13.529   6.079  1.00 38.19           C  
-ANISOU 1588  CA  THR A 210     5010   4740   4759   1622   -104   -265       C  
-ATOM   1589  C   THR A 210      39.367 -13.168   7.315  1.00 37.69           C  
-ANISOU 1589  C   THR A 210     4949   4609   4763   1429   -152   -234       C  
-ATOM   1590  O   THR A 210      39.590 -13.733   8.390  1.00 40.37           O  
-ANISOU 1590  O   THR A 210     5302   4901   5136   1417   -196   -200       O  
-ATOM   1591  CB  THR A 210      39.371 -14.413   5.156  1.00 34.93           C  
-ANISOU 1591  CB  THR A 210     4767   4191   4312   1690   -146   -361       C  
-ATOM   1592  OG1 THR A 210      38.810 -15.472   5.936  1.00 37.31           O  
-ANISOU 1592  OG1 THR A 210     5192   4329   4656   1661   -235   -377       O  
-ATOM   1593  CG2 THR A 210      40.257 -15.010   4.052  1.00 36.89           C  
-ANISOU 1593  CG2 THR A 210     5044   4490   4481   1916   -107   -398       C  
-ATOM   1594  N   LEU A 211      38.408 -12.254   7.170  1.00 34.12           N  
-ANISOU 1594  N   LEU A 211     4487   4153   4326   1288   -141   -245       N  
-ATOM   1595  CA  LEU A 211      37.565 -11.877   8.312  1.00 30.64           C  
-ANISOU 1595  CA  LEU A 211     4048   3655   3937   1119   -176   -217       C  
-ATOM   1596  C   LEU A 211      36.790 -13.103   8.766  1.00 30.47           C  
-ANISOU 1596  C   LEU A 211     4164   3470   3942   1111   -250   -244       C  
-ATOM   1597  O   LEU A 211      36.680 -13.373   9.973  1.00 28.48           O  
-ANISOU 1597  O   LEU A 211     3919   3176   3726   1045   -286   -200       O  
-ATOM   1598  CB  LEU A 211      36.611 -10.726   7.973  1.00 26.76           C  
-ANISOU 1598  CB  LEU A 211     3531   3184   3452    990   -150   -229       C  
-ATOM   1599  CG  LEU A 211      35.625 -10.300   9.088  1.00 25.12           C  
-ANISOU 1599  CG  LEU A 211     3332   2923   3289    828   -177   -204       C  
-ATOM   1600  CD1 LEU A 211      36.348  -9.936  10.414  1.00 24.45           C  
-ANISOU 1600  CD1 LEU A 211     3172   2896   3222    784   -180   -135       C  
-ATOM   1601  CD2 LEU A 211      34.713  -9.167   8.664  1.00 26.37           C  
-ANISOU 1601  CD2 LEU A 211     3465   3104   3450    723   -149   -219       C  
-ATOM   1602  N   GLU A 212      36.289 -13.862   7.792  1.00 27.69           N  
-ANISOU 1602  N   GLU A 212     3925   3027   3570   1179   -279   -312       N  
-ATOM   1603  CA  GLU A 212      35.612 -15.116   8.092  1.00 34.13           C  
-ANISOU 1603  CA  GLU A 212     4880   3675   4412   1177   -364   -336       C  
-ATOM   1604  C   GLU A 212      36.433 -15.994   9.040  1.00 35.48           C  
-ANISOU 1604  C   GLU A 212     5067   3818   4597   1246   -398   -295       C  
-ATOM   1605  O   GLU A 212      35.914 -16.503  10.033  1.00 36.55           O  
-ANISOU 1605  O   GLU A 212     5251   3862   4776   1163   -452   -260       O  
-ATOM   1606  CB  GLU A 212      35.311 -15.892   6.809  1.00 39.57           C  
-ANISOU 1606  CB  GLU A 212     5696   4275   5064   1282   -400   -419       C  
-ATOM   1607  CG  GLU A 212      34.691 -17.254   7.074  1.00 45.54           C  
-ANISOU 1607  CG  GLU A 212     6608   4843   5850   1283   -505   -441       C  
-ATOM   1608  CD  GLU A 212      34.307 -17.978   5.800  1.00 51.28           C  
-ANISOU 1608  CD  GLU A 212     7478   5467   6538   1376   -558   -531       C  
-ATOM   1609  OE1 GLU A 212      35.056 -17.868   4.802  1.00 51.76           O  
-ANISOU 1609  OE1 GLU A 212     7535   5601   6528   1526   -511   -577       O  
-ATOM   1610  OE2 GLU A 212      33.252 -18.649   5.800  1.00 53.58           O  
-ANISOU 1610  OE2 GLU A 212     7885   5604   6867   1297   -650   -550       O  
-ATOM   1611  N   GLU A 213      37.715 -16.152   8.740  1.00 34.27           N  
-ANISOU 1611  N   GLU A 213     4865   3750   4405   1400   -364   -290       N  
-ATOM   1612  CA  GLU A 213      38.576 -16.994   9.561  1.00 36.53           C  
-ANISOU 1612  CA  GLU A 213     5162   4016   4701   1485   -397   -251       C  
-ATOM   1613  C   GLU A 213      38.780 -16.380  10.949  1.00 33.71           C  
-ANISOU 1613  C   GLU A 213     4705   3722   4383   1365   -391   -167       C  
-ATOM   1614  O   GLU A 213      38.833 -17.098  11.950  1.00 35.38           O  
-ANISOU 1614  O   GLU A 213     4962   3861   4621   1353   -445   -130       O  
-ATOM   1615  CB  GLU A 213      39.916 -17.217   8.861  1.00 38.75           C  
-ANISOU 1615  CB  GLU A 213     5395   4397   4930   1686   -352   -259       C  
-ATOM   1616  CG  GLU A 213      39.780 -17.966   7.545  1.00 44.18           C  
-ANISOU 1616  CG  GLU A 213     6208   5014   5566   1834   -364   -348       C  
-ATOM   1617  CD  GLU A 213      41.027 -17.883   6.679  1.00 48.29           C  
-ANISOU 1617  CD  GLU A 213     6655   5674   6019   2031   -289   -352       C  
-ATOM   1618  OE1 GLU A 213      41.888 -17.017   6.940  1.00 46.87           O  
-ANISOU 1618  OE1 GLU A 213     6306   5663   5841   2023   -221   -282       O  
-ATOM   1619  OE2 GLU A 213      41.133 -18.678   5.719  1.00 52.11           O  
-ANISOU 1619  OE2 GLU A 213     7254   6100   6446   2195   -301   -424       O  
-ATOM   1620  N   MET A 214      38.890 -15.056  11.002  1.00 31.12           N  
-ANISOU 1620  N   MET A 214     4250   3522   4052   1279   -332   -138       N  
-ATOM   1621  CA  MET A 214      39.051 -14.348  12.276  1.00 30.28           C  
-ANISOU 1621  CA  MET A 214     4059   3474   3972   1162   -332    -67       C  
-ATOM   1622  C   MET A 214      37.825 -14.481  13.177  1.00 30.12           C  
-ANISOU 1622  C   MET A 214     4114   3347   3985   1018   -374    -55       C  
-ATOM   1623  O   MET A 214      37.950 -14.714  14.384  1.00 28.97           O  
-ANISOU 1623  O   MET A 214     3971   3182   3855    974   -407     -2       O  
-ATOM   1624  CB  MET A 214      39.353 -12.865  12.036  1.00 28.85           C  
-ANISOU 1624  CB  MET A 214     3745   3437   3781   1097   -270    -44       C  
-ATOM   1625  CG  MET A 214      40.791 -12.577  11.597  1.00 33.29           C  
-ANISOU 1625  CG  MET A 214     4188   4140   4319   1211   -229    -11       C  
-ATOM   1626  SD  MET A 214      41.120 -10.802  11.408  1.00 47.84           S  
-ANISOU 1626  SD  MET A 214     5878   6140   6161   1107   -174     32       S  
-ATOM   1627  CE  MET A 214      40.873 -10.234  13.081  1.00 42.30           C  
-ANISOU 1627  CE  MET A 214     5161   5420   5491    949   -224     86       C  
-ATOM   1628  N   MET A 215      36.644 -14.316  12.594  1.00 29.33           N  
-ANISOU 1628  N   MET A 215     4068   3184   3892    946   -371    -99       N  
-ATOM   1629  CA  MET A 215      35.405 -14.438  13.352  1.00 31.40           C  
-ANISOU 1629  CA  MET A 215     4389   3356   4186    812   -403    -80       C  
-ATOM   1630  C   MET A 215      35.154 -15.880  13.790  1.00 32.14           C  
-ANISOU 1630  C   MET A 215     4600   3308   4303    840   -477    -69       C  
-ATOM   1631  O   MET A 215      34.724 -16.125  14.923  1.00 34.47           O  
-ANISOU 1631  O   MET A 215     4917   3560   4620    756   -505    -14       O  
-ATOM   1632  CB  MET A 215      34.232 -13.910  12.536  1.00 30.14           C  
-ANISOU 1632  CB  MET A 215     4246   3173   4032    734   -385   -124       C  
-ATOM   1633  CG  MET A 215      34.296 -12.395  12.351  1.00 31.99           C  
-ANISOU 1633  CG  MET A 215     4371   3533   4250    676   -319   -121       C  
-ATOM   1634  SD  MET A 215      32.969 -11.778  11.328  1.00 42.87           S  
-ANISOU 1634  SD  MET A 215     5767   4887   5633    601   -301   -172       S  
-ATOM   1635  CE  MET A 215      31.579 -11.967  12.442  1.00 50.43           C  
-ANISOU 1635  CE  MET A 215     6766   5763   6632    459   -330   -128       C  
-ATOM   1636  N   THR A 216      35.450 -16.831  12.911  1.00 33.63           N  
-ANISOU 1636  N   THR A 216     4871   3426   4483    963   -512   -119       N  
-ATOM   1637  CA  THR A 216      35.466 -18.238  13.297  1.00 37.47           C  
-ANISOU 1637  CA  THR A 216     5474   3774   4988   1015   -591   -109       C  
-ATOM   1638  C   THR A 216      36.413 -18.499  14.470  1.00 37.08           C  
-ANISOU 1638  C   THR A 216     5388   3762   4939   1050   -602    -42       C  
-ATOM   1639  O   THR A 216      36.064 -19.207  15.414  1.00 39.30           O  
-ANISOU 1639  O   THR A 216     5733   3953   5247    998   -656      7       O  
-ATOM   1640  CB  THR A 216      35.881 -19.139  12.117  1.00 42.12           C  
-ANISOU 1640  CB  THR A 216     6160   4294   5552   1177   -624   -182       C  
-ATOM   1641  OG1 THR A 216      34.820 -19.179  11.154  1.00 43.23           O  
-ANISOU 1641  OG1 THR A 216     6373   4356   5696   1130   -647   -241       O  
-ATOM   1642  CG2 THR A 216      36.185 -20.550  12.597  1.00 42.57           C  
-ANISOU 1642  CG2 THR A 216     6333   4217   5623   1256   -708   -167       C  
-ATOM   1643  N   ALA A 217      37.612 -17.929  14.414  1.00 34.42           N  
-ANISOU 1643  N   ALA A 217     4944   3560   4574   1135   -553    -32       N  
-ATOM   1644  CA  ALA A 217      38.631 -18.246  15.413  1.00 36.96           C  
-ANISOU 1644  CA  ALA A 217     5229   3919   4895   1189   -573     29       C  
-ATOM   1645  C   ALA A 217      38.307 -17.634  16.779  1.00 37.12           C  
-ANISOU 1645  C   ALA A 217     5203   3974   4927   1043   -574    100       C  
-ATOM   1646  O   ALA A 217      38.785 -18.110  17.800  1.00 40.66           O  
-ANISOU 1646  O   ALA A 217     5661   4408   5379   1056   -613    156       O  
-ATOM   1647  CB  ALA A 217      40.002 -17.785  14.938  1.00 35.82           C  
-ANISOU 1647  CB  ALA A 217     4970   3920   4721   1315   -525     31       C  
-ATOM   1648  N   CYS A 218      37.514 -16.569  16.794  1.00 35.26           N  
-ANISOU 1648  N   CYS A 218     4921   3785   4691    915   -531     95       N  
-ATOM   1649  CA  CYS A 218      37.162 -15.892  18.044  1.00 36.10           C  
-ANISOU 1649  CA  CYS A 218     4991   3929   4795    789   -525    154       C  
-ATOM   1650  C   CYS A 218      35.708 -16.114  18.475  1.00 39.09           C  
-ANISOU 1650  C   CYS A 218     5445   4214   5193    666   -537    168       C  
-ATOM   1651  O   CYS A 218      35.236 -15.478  19.413  1.00 40.65           O  
-ANISOU 1651  O   CYS A 218     5618   4447   5379    564   -519    210       O  
-ATOM   1652  CB  CYS A 218      37.434 -14.387  17.921  1.00 34.58           C  
-ANISOU 1652  CB  CYS A 218     4683   3874   4583    737   -467    149       C  
-ATOM   1653  SG  CYS A 218      39.205 -13.984  17.847  1.00 41.23           S  
-ANISOU 1653  SG  CYS A 218     5405   4852   5408    843   -460    173       S  
-ATOM   1654  N   GLN A 219      35.004 -17.020  17.803  1.00 40.99           N  
-ANISOU 1654  N   GLN A 219     5778   4335   5460    678   -571    138       N  
-ATOM   1655  CA  GLN A 219      33.584 -17.247  18.091  1.00 45.47           C  
-ANISOU 1655  CA  GLN A 219     6403   4818   6055    556   -586    162       C  
-ATOM   1656  C   GLN A 219      33.384 -17.767  19.514  1.00 46.79           C  
-ANISOU 1656  C   GLN A 219     6606   4947   6227    496   -617    249       C  
-ATOM   1657  O   GLN A 219      34.302 -18.352  20.104  1.00 48.28           O  
-ANISOU 1657  O   GLN A 219     6814   5127   6406    568   -652    280       O  
-ATOM   1658  CB  GLN A 219      32.982 -18.230  17.074  1.00 49.44           C  
-ANISOU 1658  CB  GLN A 219     7007   5188   6591    583   -639    117       C  
-ATOM   1659  CG  GLN A 219      31.494 -18.035  16.806  1.00 52.27           C  
-ANISOU 1659  CG  GLN A 219     7381   5499   6979    456   -638    119       C  
-ATOM   1660  CD  GLN A 219      31.044 -18.642  15.482  1.00 54.94           C  
-ANISOU 1660  CD  GLN A 219     7800   5736   7339    492   -686     51       C  
-ATOM   1661  OE1 GLN A 219      31.749 -19.457  14.889  1.00 57.99           O  
-ANISOU 1661  OE1 GLN A 219     8259   6058   7718    613   -733      6       O  
-ATOM   1662  NE2 GLN A 219      29.867 -18.237  15.013  1.00 53.57           N  
-ANISOU 1662  NE2 GLN A 219     7616   5549   7189    392   -679     41       N  
-TER    1663      GLN A 219                                                      
-HETATM 1664  O24 1B0 A 301      16.149  26.725  -0.227  1.00 26.22           O  
-ANISOU 1664  O24 1B0 A 301     3954   2645   3363     89   -391   -234       O  
-HETATM 1665  C23 1B0 A 301      15.304  25.902  -0.020  1.00 26.40           C  
-ANISOU 1665  C23 1B0 A 301     3908   2729   3392    147   -333   -263       C  
-HETATM 1666  N4  1B0 A 301      15.225  24.695  -0.783  1.00 25.14           N  
-ANISOU 1666  N4  1B0 A 301     3640   2662   3252    118   -289   -249       N  
-HETATM 1667  C5  1B0 A 301      16.121  24.407  -1.852  1.00 23.37           C  
-ANISOU 1667  C5  1B0 A 301     3384   2470   3028     36   -300   -206       C  
-HETATM 1668  C13 1B0 A 301      15.485  24.900  -3.135  1.00 25.73           C  
-ANISOU 1668  C13 1B0 A 301     3681   2768   3327     55   -325   -180       C  
-HETATM 1669  N15 1B0 A 301      16.277  25.489  -4.212  1.00 27.10           N  
-ANISOU 1669  N15 1B0 A 301     3880   2931   3487     -8   -363   -124       N  
-HETATM 1670  C17 1B0 A 301      17.723  25.617  -4.002  1.00 28.59           C  
-ANISOU 1670  C17 1B0 A 301     4084   3112   3667    -96   -377    -86       C  
-HETATM 1671  C22 1B0 A 301      18.578  24.624  -4.466  1.00 26.51           C  
-ANISOU 1671  C22 1B0 A 301     3749   2929   3394   -146   -338    -63       C  
-HETATM 1672  C21 1B0 A 301      19.956  24.733  -4.238  1.00 27.91           C  
-ANISOU 1672  C21 1B0 A 301     3925   3112   3568   -226   -349    -18       C  
-HETATM 1673  C20 1B0 A 301      20.456  25.831  -3.557  1.00 29.99           C  
-ANISOU 1673  C20 1B0 A 301     4264   3291   3841   -267   -408      3       C  
-HETATM 1674  C19 1B0 A 301      19.598  26.823  -3.086  1.00 30.00           C  
-ANISOU 1674  C19 1B0 A 301     4355   3198   3847   -217   -454    -28       C  
-HETATM 1675  C18 1B0 A 301      18.227  26.721  -3.306  1.00 29.20           C  
-ANISOU 1675  C18 1B0 A 301     4250   3100   3746   -124   -433    -73       C  
-HETATM 1676  C16 1B0 A 301      15.615  25.929  -5.460  1.00 29.84           C  
-ANISOU 1676  C16 1B0 A 301     4230   3281   3828     16   -388    -97       C  
-HETATM 1677  O14 1B0 A 301      14.308  24.778  -3.276  1.00 27.63           O  
-ANISOU 1677  O14 1B0 A 301     3895   3025   3580    123   -313   -200       O  
-HETATM 1678  C6  1B0 A 301      16.314  22.898  -2.033  1.00 22.29           C  
-ANISOU 1678  C6  1B0 A 301     3153   2419   2898     12   -248   -213       C  
-HETATM 1679  C7  1B0 A 301      17.248  22.447  -0.920  1.00 22.61           C  
-ANISOU 1679  C7  1B0 A 301     3197   2461   2935    -25   -231   -224       C  
-HETATM 1680  C12 1B0 A 301      18.627  22.477  -1.112  1.00 24.28           C  
-ANISOU 1680  C12 1B0 A 301     3411   2678   3137   -103   -248   -187       C  
-HETATM 1681  C11 1B0 A 301      19.468  22.087  -0.071  1.00 24.90           C  
-ANISOU 1681  C11 1B0 A 301     3490   2757   3214   -135   -241   -194       C  
-HETATM 1682  C10 1B0 A 301      18.929  21.696   1.150  1.00 23.07           C  
-ANISOU 1682  C10 1B0 A 301     3268   2517   2982    -87   -216   -240       C  
-HETATM 1683  C9  1B0 A 301      17.547  21.687   1.334  1.00 21.29           C  
-ANISOU 1683  C9  1B0 A 301     3039   2290   2761     -8   -192   -273       C  
-HETATM 1684  C8  1B0 A 301      16.716  22.073   0.300  1.00 21.02           C  
-ANISOU 1684  C8  1B0 A 301     2995   2257   2736     23   -201   -264       C  
-HETATM 1685  C25 1B0 A 301      14.247  26.154   1.097  1.00 27.82           C  
-ANISOU 1685  C25 1B0 A 301     4122   2889   3558    261   -308   -311       C  
-HETATM 1686  C1  1B0 A 301      14.863  26.302   2.484  1.00 26.30           C  
-ANISOU 1686  C1  1B0 A 301     4003   2653   3336    262   -315   -343       C  
-HETATM 1687  C26 1B0 A 301      15.178  27.479   3.176  1.00 24.80           C  
-ANISOU 1687  C26 1B0 A 301     3950   2357   3115    285   -379   -363       C  
-HETATM 1688  C31 1B0 A 301      15.051  28.832   2.830  1.00 27.08           C  
-ANISOU 1688  C31 1B0 A 301     4349   2546   3396    309   -453   -359       C  
-HETATM 1689  C30 1B0 A 301      15.436  29.809   3.726  1.00 30.53           C  
-ANISOU 1689  C30 1B0 A 301     4931   2872   3797    329   -521   -388       C  
-HETATM 1690  C29 1B0 A 301      15.945  29.455   4.975  1.00 28.76           C  
-ANISOU 1690  C29 1B0 A 301     4743   2642   3541    325   -514   -423       C  
-HETATM 1691  C28 1B0 A 301      16.079  28.125   5.306  1.00 25.23           C  
-ANISOU 1691  C28 1B0 A 301     4182   2303   3103    300   -436   -422       C  
-HETATM 1692  C27 1B0 A 301      15.674  27.132   4.399  1.00 24.35           C  
-ANISOU 1692  C27 1B0 A 301     3925   2296   3032    281   -368   -392       C  
-HETATM 1693  N3  1B0 A 301      15.682  25.735   4.474  1.00 23.13           N  
-ANISOU 1693  N3  1B0 A 301     3649   2246   2895    255   -294   -386       N  
-HETATM 1694  C2  1B0 A 301      15.177  25.236   3.276  1.00 25.46           C  
-ANISOU 1694  C2  1B0 A 301     3844   2602   3226    243   -266   -357       C  
-HETATM 1695  C32 1B0 A 301      15.218  23.723   3.428  1.00 25.52           C  
-ANISOU 1695  C32 1B0 A 301     3739   2705   3251    215   -199   -354       C  
-HETATM 1696  H4  1B0 A 301      14.555  24.109  -0.604  1.00 30.17           H  
-HETATM 1697 H251 1B0 A 301      13.752  26.980   0.888  1.00 33.38           H  
-HETATM 1698 H252 1B0 A 301      13.623  25.411   1.105  1.00 33.38           H  
-HETATM 1699  H5  1B0 A 301      17.006  24.860  -1.703  1.00 28.05           H  
-HETATM 1700 H61C 1B0 A 301      16.718  22.724  -2.897  1.00 26.75           H  
-HETATM 1701 H62C 1B0 A 301      15.442  22.436  -1.958  1.00 26.75           H  
-HETATM 1702 H161 1B0 A 301      15.018  26.701  -5.264  1.00 35.81           H  
-HETATM 1703 H162 1B0 A 301      15.076  25.180  -5.835  1.00 35.81           H  
-HETATM 1704 H163 1B0 A 301      16.305  26.203  -6.122  1.00 35.81           H  
-HETATM 1705  H22 1B0 A 301      18.215  23.839  -4.949  1.00 31.81           H  
-HETATM 1706  H18 1B0 A 301      17.624  27.414  -2.974  1.00 35.04           H  
-HETATM 1707  H21 1B0 A 301      20.575  24.031  -4.575  1.00 33.49           H  
-HETATM 1708  H20 1B0 A 301      21.434  25.913  -3.403  1.00 35.99           H  
-HETATM 1709  H19 1B0 A 301      19.960  27.596  -2.608  1.00 36.01           H  
-HETATM 1710  H12 1B0 A 301      19.022  22.770  -2.022  1.00 29.14           H  
-HETATM 1711  H8  1B0 A 301      15.746  22.069   0.427  1.00 25.23           H  
-HETATM 1712  H11 1B0 A 301      20.446  22.090  -0.199  1.00 29.88           H  
-HETATM 1713  H10 1B0 A 301      19.540  21.409   1.904  1.00 27.69           H  
-HETATM 1714  H9  1B0 A 301      17.152  21.398   2.224  1.00 25.55           H  
-HETATM 1715  H31 1B0 A 301      14.681  29.080   1.972  1.00 32.50           H  
-HETATM 1716  H30 1B0 A 301      15.347  30.764   3.482  1.00 36.64           H  
-HETATM 1717  H29 1B0 A 301      16.235  30.150   5.604  1.00 34.51           H  
-HETATM 1718  H28 1B0 A 301      16.447  27.869   6.188  1.00 30.28           H  
-HETATM 1719  H3  1B0 A 301      15.984  25.231   5.192  1.00 27.76           H  
-HETATM 1720 H321 1B0 A 301      15.538  23.326   2.608  1.00 30.62           H  
-HETATM 1721 H322 1B0 A 301      15.836  23.478   4.184  1.00 30.62           H  
-HETATM 1722 H323 1B0 A 301      14.311  23.386   3.623  1.00 30.62           H  
-HETATM 1723  O   HOH A 401      14.623  20.538   4.162  1.00 21.99           O  
-ANISOU 1723  O   HOH A 401     3076   2436   2842    203    -60   -353       O  
-HETATM 1724  O   HOH A 402      12.264  22.853   8.665  1.00 26.38           O  
-ANISOU 1724  O   HOH A 402     3880   2927   3217    599     33   -456       O  
-HETATM 1725  O   HOH A 403      27.462  19.309   2.851  1.00 28.86           O  
-ANISOU 1725  O   HOH A 403     3769   3460   3734   -476   -273      0       O  
-HETATM 1726  O   HOH A 404      27.073  -3.083  12.037  1.00 18.27           O  
-ANISOU 1726  O   HOH A 404     2376   2055   2511      4    -57   -152       O  
-HETATM 1727  O   HOH A 405      32.433  -6.069  27.640  1.00 31.68           O  
-ANISOU 1727  O   HOH A 405     4443   3830   3763     18   -322    346       O  
-HETATM 1728  O   HOH A 406      34.711   1.038  22.042  1.00 28.78           O  
-ANISOU 1728  O   HOH A 406     3771   3629   3536   -114   -376     86       O  
-HETATM 1729  O   HOH A 407      27.133  -9.101  11.145  1.00 25.60           O  
-ANISOU 1729  O   HOH A 407     3541   2650   3537    136   -252   -163       O  
-HETATM 1730  O   HOH A 408      27.469  -4.472  17.659  1.00 22.60           O  
-ANISOU 1730  O   HOH A 408     3011   2587   2990    -52    -75     29       O  
-HETATM 1731  O   HOH A 409      31.659 -13.639  18.172  1.00 33.07           O  
-ANISOU 1731  O   HOH A 409     4636   3480   4448    297   -412    147       O  
-HETATM 1732  O   HOH A 410      26.661   9.634  10.155  1.00 24.50           O  
-ANISOU 1732  O   HOH A 410     3135   3014   3158   -203    -45   -216       O  
-HETATM 1733  O   HOH A 411      33.238 -13.972  20.460  1.00 35.30           O  
-ANISOU 1733  O   HOH A 411     4914   3817   4682    336   -449    250       O  
-HETATM 1734  O   HOH A 412      11.929  13.917   6.968  1.00 37.18           O  
-ANISOU 1734  O   HOH A 412     4590   4657   4878    184    187   -254       O  
-HETATM 1735  O   HOH A 413      10.423  21.995  -3.864  1.00 24.65           O  
-ANISOU 1735  O   HOH A 413     3237   2839   3291    264   -237   -236       O  
-HETATM 1736  O   HOH A 414      33.054 -14.299  15.904  1.00 33.94           O  
-ANISOU 1736  O   HOH A 414     4762   3573   4561    503   -436     34       O  
-HETATM 1737  O   HOH A 415      27.593  10.451  -6.909  1.00 29.10           O  
-ANISOU 1737  O   HOH A 415     3553   4050   3454     99    153   -109       O  
-HETATM 1738  O   HOH A 416      26.743   7.675  11.781  1.00 28.80           O  
-ANISOU 1738  O   HOH A 416     3684   3561   3696   -172    -25   -208       O  
-HETATM 1739  O   HOH A 417      19.582  13.772 -15.646  1.00 27.33           O  
-ANISOU 1739  O   HOH A 417     3748   3682   2956    207   -169   -220       O  
-HETATM 1740  O   HOH A 418      39.838  -4.283  23.645  1.00 26.82           O  
-ANISOU 1740  O   HOH A 418     3339   3469   3380    124   -573    321       O  
-HETATM 1741  O   HOH A 419      26.652   3.174   0.980  1.00 33.39           O  
-ANISOU 1741  O   HOH A 419     4177   4238   4270    119     44   -336       O  
-HETATM 1742  O   HOH A 420      15.007  20.390  13.890  1.00 31.48           O  
-ANISOU 1742  O   HOH A 420     4675   3620   3667    540     99   -499       O  
-HETATM 1743  O   HOH A 421      27.770  28.303 -16.568  1.00 39.84           O  
-ANISOU 1743  O   HOH A 421     5136   5349   4651   -669   -197   1121       O  
-HETATM 1744  O   HOH A 422      28.911  12.558  -5.698  1.00 31.17           O  
-ANISOU 1744  O   HOH A 422     3721   4340   3783    -54    142     34       O  
-HETATM 1745  O   HOH A 423      16.608  18.234  13.744  1.00 35.72           O  
-ANISOU 1745  O   HOH A 423     5080   4214   4276    347     93   -445       O  
-HETATM 1746  O   HOH A 424      23.210  29.644 -23.913  1.00 32.97           O  
-ANISOU 1746  O   HOH A 424     4647   4566   3315   -314   -255   1180       O  
-HETATM 1747  O   HOH A 425      24.463  11.281 -10.512  1.00 30.76           O  
-ANISOU 1747  O   HOH A 425     3940   4202   3544    165     68   -189       O  
-HETATM 1748  O   HOH A 426      29.266  27.760  -0.886  1.00 32.67           O  
-ANISOU 1748  O   HOH A 426     4510   3609   4294   -943   -721    457       O  
-HETATM 1749  O   HOH A 427      25.198  29.645 -11.600  1.00 27.76           O  
-ANISOU 1749  O   HOH A 427     3877   3258   3411   -695   -484    748       O  
-HETATM 1750  O   HOH A 428      35.843   9.113  19.076  1.00 37.13           O  
-ANISOU 1750  O   HOH A 428     4804   4668   4636   -434   -594     38       O  
-HETATM 1751  O   HOH A 429      13.385  23.560 -10.504  1.00 22.22           O  
-ANISOU 1751  O   HOH A 429     3098   2545   2799     78   -403    -71       O  
-HETATM 1752  O   HOH A 430      13.196  23.238  -7.605  1.00 27.35           O  
-ANISOU 1752  O   HOH A 430     3718   3150   3524    103   -342   -141       O  
-HETATM 1753  O   HOH A 431      27.526  29.054  -0.022  1.00 45.28           O  
-ANISOU 1753  O   HOH A 431     6342   4986   5875   -854   -812    324       O  
-HETATM 1754  O   HOH A 432       9.813  17.230 -12.093  1.00 29.80           O  
-ANISOU 1754  O   HOH A 432     3825   3670   3826    108   -502   -235       O  
-HETATM 1755  O   HOH A 433      21.699  29.941 -20.620  1.00 31.92           O  
-ANISOU 1755  O   HOH A 433     4550   4112   3465   -353   -398    933       O  
-HETATM 1756  O   HOH A 434      11.205  21.728  -6.401  1.00 22.86           O  
-ANISOU 1756  O   HOH A 434     3025   2634   3028    180   -302   -202       O  
-HETATM 1757  O   HOH A 435       9.764  15.743   6.851  1.00 35.17           O  
-ANISOU 1757  O   HOH A 435     4307   4439   4617    341    221   -238       O  
-HETATM 1758  O   HOH A 436      49.351 -15.408  19.707  1.00 42.36           O  
-ANISOU 1758  O   HOH A 436     4848   5668   5580   1571   -630    596       O  
-HETATM 1759  O   HOH A 437      39.567 -19.994  11.440  1.00 49.72           O  
-ANISOU 1759  O   HOH A 437     7034   5443   6416   1667   -568   -194       O  
-HETATM 1760  O   HOH A 438      43.336 -16.152  23.938  1.00 42.46           O  
-ANISOU 1760  O   HOH A 438     5533   5071   5527    972   -759    521       O  
-HETATM 1761  O   HOH A 439       6.283   4.891   0.967  1.00 40.80           O  
-ANISOU 1761  O   HOH A 439     4546   5107   5849   -319   -266      2       O  
-HETATM 1762  O   HOH A 440      16.462  23.314 -22.310  1.00 29.53           O  
-ANISOU 1762  O   HOH A 440     4289   3932   2999    138   -442    279       O  
-HETATM 1763  O   HOH A 441      16.526  25.728 -23.049  1.00 31.10           O  
-ANISOU 1763  O   HOH A 441     4544   4085   3187     82   -487    448       O  
-HETATM 1764  O   HOH A 442      39.972 -21.171  14.191  1.00 45.13           O  
-ANISOU 1764  O   HOH A 442     6491   4753   5904   1595   -681    -50       O  
-HETATM 1765  O   HOH A 443      18.542  25.112   6.369  1.00 25.95           O  
-ANISOU 1765  O   HOH A 443     4076   2566   3218     82   -360   -385       O  
-HETATM 1766  O   HOH A 444       8.831  25.329 -13.942  1.00 35.01           O  
-ANISOU 1766  O   HOH A 444     4728   4146   4426    272   -627    -15       O  
-HETATM 1767  O   HOH A 445       8.171   8.788  -7.963  1.00 26.72           O  
-ANISOU 1767  O   HOH A 445     3193   3221   3739   -125   -569   -314       O  
-HETATM 1768  O   HOH A 446      34.458  15.864   4.125  1.00 49.68           O  
-ANISOU 1768  O   HOH A 446     5941   6502   6434   -613   -258    301       O  
-HETATM 1769  O   HOH A 447      40.508 -20.439  17.947  1.00 42.17           O  
-ANISOU 1769  O   HOH A 447     5961   4490   5573   1351   -716    177       O  
-HETATM 1770  O   HOH A 448       2.654  11.872 -14.504  1.00 39.39           O  
-ANISOU 1770  O   HOH A 448     4750   4878   5338    -65  -1089   -214       O  
-HETATM 1771  O   HOH A 449      25.963  12.326 -15.507  1.00 52.65           O  
-ANISOU 1771  O   HOH A 449     6781   7264   5958    356    180    -38       O  
-HETATM 1772  O   HOH A 450      27.799  31.787 -16.957  1.00 49.46           O  
-ANISOU 1772  O   HOH A 450     6500   6340   5954   -905   -408   1374       O  
-HETATM 1773  O   HOH A 451      32.207  30.608 -10.890  1.00 41.53           O  
-ANISOU 1773  O   HOH A 451     5208   5297   5273  -1253   -519   1382       O  
-HETATM 1774  O   HOH A 452      22.027  29.226  -1.233  1.00 43.39           O  
-ANISOU 1774  O   HOH A 452     6258   4668   5562   -409   -661     53       O  
-HETATM 1775  O   HOH A 453       7.546  15.433 -10.595  1.00 30.78           O  
-ANISOU 1775  O   HOH A 453     3779   3805   4111     82   -542   -244       O  
-HETATM 1776  O   HOH A 454      30.379  16.861  -9.752  1.00 39.64           O  
-ANISOU 1776  O   HOH A 454     4717   5622   4722   -187    177    399       O  
-HETATM 1777  O   HOH A 455      15.568   9.095 -16.964  1.00 43.91           O  
-ANISOU 1777  O   HOH A 455     6058   5550   5074    283   -525   -524       O  
-HETATM 1778  O   HOH A 456      19.268  12.567 -18.250  1.00 39.61           O  
-ANISOU 1778  O   HOH A 456     5452   5287   4311    347   -226   -285       O  
-HETATM 1779  O   HOH A 457      10.060  13.413  -0.123  1.00 32.46           O  
-ANISOU 1779  O   HOH A 457     3855   4044   4435     62    -62   -244       O  
-HETATM 1780  O   HOH A 458      20.506  31.171 -15.793  1.00 35.73           O  
-ANISOU 1780  O   HOH A 458     5122   4179   4275   -413   -569    699       O  
-HETATM 1781  O   HOH A 459       7.701  15.152 -21.175  1.00 37.52           O  
-ANISOU 1781  O   HOH A 459     5172   4697   4388    204  -1035   -307       O  
-HETATM 1782  O   HOH A 460      39.375  -5.203  26.701  1.00 41.03           O  
-ANISOU 1782  O   HOH A 460     5331   5195   5062    108   -655    378       O  
-HETATM 1783  O   HOH A 461      22.887  11.259  11.908  1.00 38.82           O  
-ANISOU 1783  O   HOH A 461     5091   4751   4908   -113     18   -286       O  
-HETATM 1784  O   HOH A 462      21.694   3.519  -4.325  1.00 25.37           O  
-ANISOU 1784  O   HOH A 462     3340   3100   3200    133   -113   -483       O  
-HETATM 1785  O   HOH A 463      18.114  12.036 -13.553  1.00 37.98           O  
-ANISOU 1785  O   HOH A 463     5058   4898   4472    163   -237   -338       O  
-HETATM 1786  O   HOH A 464       8.941  17.570  -7.900  1.00 31.82           O  
-ANISOU 1786  O   HOH A 464     3942   3908   4242    134   -363   -230       O  
-HETATM 1787  O   HOH A 465       6.986  17.410   3.866  1.00 31.53           O  
-ANISOU 1787  O   HOH A 465     3720   4009   4250    439    141   -195       O  
-HETATM 1788  O   HOH A 466       6.075  11.822   8.679  1.00 42.77           O  
-ANISOU 1788  O   HOH A 466     4834   5683   5734    296    383     29       O  
-HETATM 1789  O   HOH A 467       5.246  13.135   6.100  1.00 40.13           O  
-ANISOU 1789  O   HOH A 467     4475   5310   5462    312    270     -7       O  
-HETATM 1790  O   HOH A 468       6.074  15.839   5.898  1.00 44.17           O  
-ANISOU 1790  O   HOH A 468     5187   5731   5865    457    260   -119       O  
-HETATM 1791  O   HOH A 469      18.837  16.360  14.070  1.00 51.86           O  
-ANISOU 1791  O   HOH A 469     7062   6283   6360    174     51   -407       O  
-HETATM 1792  O   HOH A 470      21.079  16.721  11.705  1.00 42.24           O  
-ANISOU 1792  O   HOH A 470     5785   5018   5245    -14    -74   -374       O  
-HETATM 1793  O   HOH A 471      19.360  26.734   4.653  1.00 38.27           O  
-ANISOU 1793  O   HOH A 471     5697   4030   4815    -27   -481   -312       O  
-HETATM 1794  O   HOH A 472      21.014  29.814   2.948  1.00 45.92           O  
-ANISOU 1794  O   HOH A 472     6851   4776   5822   -229   -733   -173       O  
-HETATM 1795  O   HOH A 473      29.197  22.458   3.463  1.00 33.41           O  
-ANISOU 1795  O   HOH A 473     4463   3886   4344   -691   -502    136       O  
-HETATM 1796  O   HOH A 474      21.754  30.124  -4.027  1.00 56.17           O  
-ANISOU 1796  O   HOH A 474     7845   6321   7176   -446   -672    184       O  
-HETATM 1797  O   HOH A 475      33.526  26.270  -5.737  1.00 41.14           O  
-ANISOU 1797  O   HOH A 475     4985   5324   5322  -1107   -440    995       O  
-HETATM 1798  O   HOH A 476      34.605  21.908  -5.498  1.00 54.32           O  
-ANISOU 1798  O   HOH A 476     6391   7340   6910   -829   -154    865       O  
-HETATM 1799  O   HOH A 477      34.248  17.861  -6.918  1.00 50.47           O  
-ANISOU 1799  O   HOH A 477     5819   7098   6259   -443    124    673       O  
-HETATM 1800  O   HOH A 478      40.018  25.653 -16.048  1.00 64.56           O  
-ANISOU 1800  O   HOH A 478     7018   9704   7809   -954    308   2139       O  
-HETATM 1801  O   HOH A 479      18.751  24.277 -30.227  1.00 40.11           O  
-ANISOU 1801  O   HOH A 479     5939   5763   3538    372   -329    675       O  
-HETATM 1802  O   HOH A 480      22.112  31.713 -18.224  1.00 44.51           O  
-ANISOU 1802  O   HOH A 480     6193   5462   5258   -510   -520    959       O  
-HETATM 1803  O   HOH A 481      10.861  24.107 -11.051  1.00 44.56           O  
-ANISOU 1803  O   HOH A 481     5903   5355   5673    187   -475    -83       O  
-HETATM 1804  O   HOH A 482       8.769  22.690  -7.558  1.00 36.94           O  
-ANISOU 1804  O   HOH A 482     4768   4421   4847    290   -377   -174       O  
-HETATM 1805  O   HOH A 483      13.486  27.549  -8.588  1.00 44.14           O  
-ANISOU 1805  O   HOH A 483     6084   5068   5619    111   -490    -24       O  
-HETATM 1806  O   HOH A 484      14.157  29.529  -7.336  1.00 55.74           O  
-ANISOU 1806  O   HOH A 484     7713   6370   7098     99   -560     -8       O  
-HETATM 1807  O   HOH A 485      10.374  27.035 -19.853  1.00 42.70           O  
-ANISOU 1807  O   HOH A 485     5948   5193   5083    218   -770    207       O  
-HETATM 1808  O   HOH A 486       8.076  24.726 -16.955  1.00 33.35           O  
-ANISOU 1808  O   HOH A 486     4542   4013   4118    278   -745     20       O  
-HETATM 1809  O   HOH A 487      15.055  18.114 -25.917  1.00 47.78           O  
-ANISOU 1809  O   HOH A 487     6830   6381   4943    429   -580    -40       O  
-HETATM 1810  O   HOH A 488      16.855  10.426 -21.030  1.00 39.11           O  
-ANISOU 1810  O   HOH A 488     5654   5124   4084    477   -490   -474       O  
-HETATM 1811  O   HOH A 489      19.371   9.221 -21.187  1.00 48.52           O  
-ANISOU 1811  O   HOH A 489     6883   6432   5122    625   -327   -487       O  
-HETATM 1812  O   HOH A 490      30.255  11.565  -3.865  1.00 38.76           O  
-ANISOU 1812  O   HOH A 490     4612   5320   4795    -64    148     45       O  
-HETATM 1813  O   HOH A 491      27.697  13.447  16.185  1.00 49.58           O  
-ANISOU 1813  O   HOH A 491     6710   6009   6117   -247   -287   -262       O  
-HETATM 1814  O   HOH A 492      29.994  14.145  15.207  1.00 39.15           O  
-ANISOU 1814  O   HOH A 492     5309   4701   4866   -384   -411   -183       O  
-HETATM 1815  O   HOH A 493      37.745   7.403  12.357  1.00 35.96           O  
-ANISOU 1815  O   HOH A 493     4127   4844   4692   -320   -316    195       O  
-HETATM 1816  O   HOH A 494      30.372   5.017  15.173  1.00 37.91           O  
-ANISOU 1816  O   HOH A 494     4825   4760   4820   -168   -126   -110       O  
-HETATM 1817  O   HOH A 495      46.573  -1.987  21.481  1.00 52.02           O  
-ANISOU 1817  O   HOH A 495     5855   7144   6766    114   -783    617       O  
-HETATM 1818  O   HOH A 496      42.673  -3.596  22.529  1.00 44.50           O  
-ANISOU 1818  O   HOH A 496     5321   5887   5700    155   -650    410       O  
-HETATM 1819  O   HOH A 497      44.469 -18.911  16.648  1.00 45.01           O  
-ANISOU 1819  O   HOH A 497     5905   5325   5871   1701   -577    212       O  
-HETATM 1820  O   HOH A 498      38.658 -19.896   4.429  1.00 51.27           O  
-ANISOU 1820  O   HOH A 498     7504   5650   6325   2077   -458   -588       O  
-HETATM 1821  O   HOH A 499      13.185  15.489   9.316  1.00 37.63           O  
-ANISOU 1821  O   HOH A 499     4837   4658   4802    270    212   -309       O  
-HETATM 1822  O   HOH A 500      35.627  26.594  -8.640  1.00 34.66           O  
-ANISOU 1822  O   HOH A 500     3890   4843   4435  -1191   -302   1371       O  
-CONECT 1664 1665                                                                
-CONECT 1665 1664 1666 1685                                                      
-CONECT 1666 1665 1667 1696                                                      
-CONECT 1667 1666 1668 1678 1699                                                 
-CONECT 1668 1667 1669 1677                                                      
-CONECT 1669 1668 1670 1676                                                      
-CONECT 1670 1669 1671 1675                                                      
-CONECT 1671 1670 1672 1705                                                      
-CONECT 1672 1671 1673 1707                                                      
-CONECT 1673 1672 1674 1708                                                      
-CONECT 1674 1673 1675 1709                                                      
-CONECT 1675 1670 1674 1706                                                      
-CONECT 1676 1669 1702 1703 1704                                                 
-CONECT 1677 1668                                                                
-CONECT 1678 1667 1679 1700 1701                                                 
-CONECT 1679 1678 1680 1684                                                      
-CONECT 1680 1679 1681 1710                                                      
-CONECT 1681 1680 1682 1712                                                      
-CONECT 1682 1681 1683 1713                                                      
-CONECT 1683 1682 1684 1714                                                      
-CONECT 1684 1679 1683 1711                                                      
-CONECT 1685 1665 1686 1697 1698                                                 
-CONECT 1686 1685 1687 1694                                                      
-CONECT 1687 1686 1688 1692                                                      
-CONECT 1688 1687 1689 1715                                                      
-CONECT 1689 1688 1690 1716                                                      
-CONECT 1690 1689 1691 1717                                                      
-CONECT 1691 1690 1692 1718                                                      
-CONECT 1692 1687 1691 1693                                                      
-CONECT 1693 1692 1694 1719                                                      
-CONECT 1694 1686 1693 1695                                                      
-CONECT 1695 1694 1720 1721 1722                                                 
-CONECT 1696 1666                                                                
-CONECT 1697 1685                                                                
-CONECT 1698 1685                                                                
-CONECT 1699 1667                                                                
-CONECT 1700 1678                                                                
-CONECT 1701 1678                                                                
-CONECT 1702 1676                                                                
-CONECT 1703 1676                                                                
-CONECT 1704 1676                                                                
-CONECT 1705 1671                                                                
-CONECT 1706 1675                                                                
-CONECT 1707 1672                                                                
-CONECT 1708 1673                                                                
-CONECT 1709 1674                                                                
-CONECT 1710 1680                                                                
-CONECT 1711 1684                                                                
-CONECT 1712 1681                                                                
-CONECT 1713 1682                                                                
-CONECT 1714 1683                                                                
-CONECT 1715 1688                                                                
-CONECT 1716 1689                                                                
-CONECT 1717 1690                                                                
-CONECT 1718 1691                                                                
-CONECT 1719 1693                                                                
-CONECT 1720 1695                                                                
-CONECT 1721 1695                                                                
-CONECT 1722 1695                                                                
-MASTER      305    0    1   12    2    0    3    6 1794    1   59   18          
-END                                                                             
diff --git a/plip/test/pdb/4rao.pdb b/plip/test/pdb/4rao.pdb
deleted file mode 100644
index 2a432be..0000000
--- a/plip/test/pdb/4rao.pdb
+++ /dev/null
@@ -1,14899 +0,0 @@
-HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       10-SEP-14   4RAO              
-TITLE     AZA-ACYCLIC NUCLEOSIDE PHOSPHONATES CONTAINING A SECOND PHOSPHONATE   
-TITLE    2 GROUP AS INHIBITORS OF THE HUMAN, PLASMODIUM FALCIPARUM AND VIVAX 6- 
-TITLE    3 OXOPURINE PHOSPHORIBOSYLTRANSFERASES AND THEIR PRO-DRUGS AS          
-TITLE    4 ANTIMALARIAL AGENTS                                                  
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE;            
-COMPND   3 CHAIN: A, B, C, D;                                                   
-COMPND   4 SYNONYM: HGPRT, HGPRTASE;                                            
-COMPND   5 EC: 2.4.2.8;                                                         
-COMPND   6 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
-SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
-SOURCE   4 ORGANISM_TAXID: 9606;                                                
-SOURCE   5 GENE: HPRT1, HPRT;                                                   
-SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
-SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
-KEYWDS    6-OXOPURINE PHOSPHORIBOSYLTRANSFERASE, 9-[(N-PHOSPHONOETHYL-N-        
-KEYWDS   2 PHOSPHONOETHOXYETHYL)-2-AMINOETHYL]HYPOXANTHINE, CYTOPLASMIC,        
-KEYWDS   3 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    D.T.KEOUGH,D.HOCKOV,Z.JANEBA,T-H.WANG,L.NAESENS,M.D.EDSTEIN,          
-AUTHOR   2 M.CHAVCHICH,L.W.GUDDAT                                               
-REVDAT   1   07-JAN-15 4RAO    0                                                
-JRNL        AUTH   D.T.KEOUGH,D.HOCKOVA,Z.JANEBA,T.WANG,L.NAESENS,M.D.EDSTEIN,  
-JRNL        AUTH 2 M.CHAVCHICH,L.W.GUDDAT                                       
-JRNL        TITL   AZA-ACYCLIC NUCLEOSIDE PHOSPHONATES CONTAINING A SECOND      
-JRNL        TITL 2 PHOSPHONATE GROUP AS INHIBITORS OF THE HUMAN, PLASMODIUM     
-JRNL        TITL 3 FALCIPARUM AND VIVAX 6-OXOPURINE PHOSPHORIBOSYLTRANSFERASES  
-JRNL        TITL 4 AND THEIR PRODRUGS AS ANTIMALARIAL AGENTS.                   
-JRNL        REF    J.MED.CHEM.                                2014              
-JRNL        REFN                   ISSN 0022-2623                               
-JRNL        PMID   25494538                                                     
-JRNL        DOI    10.1021/JM501416T                                            
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.87 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : MLHL                                          
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.41                          
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
-REMARK   3   NUMBER OF REFLECTIONS             : 68117                          
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
-REMARK   3   R VALUE            (WORKING SET) : 0.201                           
-REMARK   3   FREE R VALUE                     : 0.230                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.940                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 35.4134 -  4.5060    0.99     4936   149  0.1807 0.2057        
-REMARK   3     2  4.5060 -  3.5776    1.00     4836   146  0.1615 0.1763        
-REMARK   3     3  3.5776 -  3.1257    1.00     4767   145  0.1953 0.2231        
-REMARK   3     4  3.1257 -  2.8400    1.00     4737   143  0.2116 0.2582        
-REMARK   3     5  2.8400 -  2.6365    1.00     4706   143  0.2255 0.2502        
-REMARK   3     6  2.6365 -  2.4811    1.00     4727   142  0.2233 0.2280        
-REMARK   3     7  2.4811 -  2.3569    1.00     4713   143  0.2191 0.2645        
-REMARK   3     8  2.3569 -  2.2543    1.00     4684   142  0.2253 0.2528        
-REMARK   3     9  2.2543 -  2.1676    1.00     4694   142  0.2235 0.2826        
-REMARK   3    10  2.1676 -  2.0928    1.00     4710   142  0.2168 0.2730        
-REMARK   3    11  2.0928 -  2.0273    1.00     4653   141  0.2352 0.2856        
-REMARK   3    12  2.0273 -  1.9694    1.00     4654   141  0.2295 0.2647        
-REMARK   3    13  1.9694 -  1.9176    1.00     4669   141  0.2360 0.2575        
-REMARK   3    14  1.9176 -  1.8710    0.99     4631   140  0.2623 0.2810        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.11                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
-REMARK   3   K_SOL              : NULL                                          
-REMARK   3   B_SOL              : NULL                                          
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.440           
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : NULL                                                 
-REMARK   3    B22 (A**2) : NULL                                                 
-REMARK   3    B33 (A**2) : NULL                                                 
-REMARK   3    B12 (A**2) : NULL                                                 
-REMARK   3    B13 (A**2) : NULL                                                 
-REMARK   3    B23 (A**2) : NULL                                                 
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.007           6832                                  
-REMARK   3   ANGLE     :  1.222           9287                                  
-REMARK   3   CHIRALITY :  0.078           1037                                  
-REMARK   3   PLANARITY :  0.004           1170                                  
-REMARK   3   DIHEDRAL  : 15.853           2652                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : 31                                         
-REMARK   3   TLS GROUP : 1                                                      
-REMARK   3    SELECTION: chain 'A' and (resid 1 through 24 )                    
-REMARK   3    ORIGIN FOR THE GROUP (A):  18.4722   2.5508  -3.4232              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2761 T22:   0.3888                                     
-REMARK   3      T33:   0.1914 T12:  -0.0331                                     
-REMARK   3      T13:   0.0513 T23:  -0.0546                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   5.9643 L22:   4.4104                                     
-REMARK   3      L33:   1.8046 L12:  -1.1905                                     
-REMARK   3      L13:   1.0296 L23:  -1.2136                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.3593 S12:   0.5049 S13:  -0.0274                       
-REMARK   3      S21:  -0.2290 S22:  -0.3701 S23:  -0.2974                       
-REMARK   3      S31:   0.0652 S32:   0.6322 S33:  -0.0160                       
-REMARK   3   TLS GROUP : 2                                                      
-REMARK   3    SELECTION: chain 'A' and (resid 25 through 37 )                   
-REMARK   3    ORIGIN FOR THE GROUP (A):  15.5740  15.0112  -2.1731              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5345 T22:   0.3390                                     
-REMARK   3      T33:   0.2732 T12:  -0.1146                                     
-REMARK   3      T13:   0.0131 T23:   0.0711                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   6.3478 L22:   9.3251                                     
-REMARK   3      L33:   5.4894 L12:  -1.6751                                     
-REMARK   3      L13:  -1.3368 L23:   2.9191                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.1374 S12:   0.4752 S13:   0.8809                       
-REMARK   3      S21:  -0.2252 S22:   0.0174 S23:  -0.9703                       
-REMARK   3      S31:  -1.4878 S32:   0.5679 S33:  -0.1024                       
-REMARK   3   TLS GROUP : 3                                                      
-REMARK   3    SELECTION: chain 'A' and (resid 38 through 86 )                   
-REMARK   3    ORIGIN FOR THE GROUP (A):  12.0299  -4.8692  13.7308              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1921 T22:   0.2423                                     
-REMARK   3      T33:   0.1793 T12:   0.0057                                     
-REMARK   3      T13:   0.0041 T23:  -0.0143                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.8229 L22:   3.0929                                     
-REMARK   3      L33:   2.8758 L12:   1.0899                                     
-REMARK   3      L13:   0.2587 L23:  -0.0075                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.1555 S12:  -0.0781 S13:   0.0165                       
-REMARK   3      S21:   0.1337 S22:  -0.1202 S23:   0.0458                       
-REMARK   3      S31:   0.0627 S32:   0.1012 S33:  -0.0399                       
-REMARK   3   TLS GROUP : 4                                                      
-REMARK   3    SELECTION: chain 'A' and (resid 87 through 100 )                  
-REMARK   3    ORIGIN FOR THE GROUP (A):  10.8742  -4.6966  22.3544              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4573 T22:   0.3327                                     
-REMARK   3      T33:   0.2715 T12:  -0.0363                                     
-REMARK   3      T13:   0.0154 T23:  -0.0229                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   9.3739 L22:   4.9720                                     
-REMARK   3      L33:   0.0627 L12:   6.7926                                     
-REMARK   3      L13:   0.7814 L23:   0.4067                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1087 S12:   0.0667 S13:  -0.3674                       
-REMARK   3      S21:  -0.4185 S22:   0.1934 S23:  -0.1040                       
-REMARK   3      S31:   0.0179 S32:   0.2954 S33:  -0.0951                       
-REMARK   3   TLS GROUP : 5                                                      
-REMARK   3    SELECTION: chain 'A' and (resid 101 through 152 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):  25.3619  -1.1903  21.8612              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2424 T22:   0.3030                                     
-REMARK   3      T33:   0.1570 T12:  -0.0124                                     
-REMARK   3      T13:  -0.0384 T23:  -0.0567                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.9774 L22:   3.5114                                     
-REMARK   3      L33:   8.1942 L12:   0.2834                                     
-REMARK   3      L13:   2.3189 L23:  -2.3631                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0385 S12:   0.0995 S13:   0.1632                       
-REMARK   3      S21:   0.0202 S22:  -0.0321 S23:  -0.3284                       
-REMARK   3      S31:   0.0388 S32:   0.4188 S33:   0.0812                       
-REMARK   3   TLS GROUP : 6                                                      
-REMARK   3    SELECTION: chain 'A' and (resid 153 through 216 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):  23.1693   6.2682   7.3597              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2550 T22:   0.4224                                     
-REMARK   3      T33:   0.2827 T12:  -0.0986                                     
-REMARK   3      T13:   0.0189 T23:  -0.0221                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.0134 L22:   3.7565                                     
-REMARK   3      L33:   3.6492 L12:  -0.4347                                     
-REMARK   3      L13:   0.0531 L23:  -0.8514                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0897 S12:   0.0177 S13:   0.2839                       
-REMARK   3      S21:   0.0164 S22:  -0.1132 S23:  -0.6065                       
-REMARK   3      S31:  -0.3736 S32:   0.7221 S33:   0.0633                       
-REMARK   3   TLS GROUP : 7                                                      
-REMARK   3    SELECTION: chain 'B' and (resid 4 through 37 )                    
-REMARK   3    ORIGIN FOR THE GROUP (A):  11.7905  -9.3190  -7.9593              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2025 T22:   0.3236                                     
-REMARK   3      T33:   0.2550 T12:   0.0481                                     
-REMARK   3      T13:   0.0364 T23:  -0.0647                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   3.6287 L22:   3.1423                                     
-REMARK   3      L33:   3.0007 L12:   1.0484                                     
-REMARK   3      L13:   0.3472 L23:  -1.0446                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0960 S12:   0.3007 S13:  -0.3171                       
-REMARK   3      S21:  -0.1329 S22:  -0.0124 S23:  -0.3755                       
-REMARK   3      S31:   0.1412 S32:   0.4958 S33:  -0.0539                       
-REMARK   3   TLS GROUP : 8                                                      
-REMARK   3    SELECTION: chain 'B' and (resid 38 through 56 )                   
-REMARK   3    ORIGIN FOR THE GROUP (A):   0.1620   9.1215  -7.3183              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2348 T22:   0.2147                                     
-REMARK   3      T33:   0.2739 T12:  -0.0059                                     
-REMARK   3      T13:  -0.0091 T23:   0.0469                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   3.0545 L22:   6.2816                                     
-REMARK   3      L33:   7.7011 L12:  -4.0601                                     
-REMARK   3      L13:   2.7727 L23:  -2.8739                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0759 S12:  -0.0991 S13:   0.3418                       
-REMARK   3      S21:  -0.0425 S22:   0.2800 S23:   0.2201                       
-REMARK   3      S31:  -0.6067 S32:  -0.3073 S33:  -0.1197                       
-REMARK   3   TLS GROUP : 9                                                      
-REMARK   3    SELECTION: chain 'B' and (resid 57 through 87 )                   
-REMARK   3    ORIGIN FOR THE GROUP (A):  -9.0721   5.0697  -6.7935              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1976 T22:   0.1806                                     
-REMARK   3      T33:   0.2866 T12:   0.0082                                     
-REMARK   3      T13:  -0.0307 T23:   0.0345                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.2939 L22:   3.1853                                     
-REMARK   3      L33:   4.5097 L12:   0.4367                                     
-REMARK   3      L13:  -0.1908 L23:   0.9722                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0591 S12:   0.0989 S13:   0.3597                       
-REMARK   3      S21:  -0.1435 S22:  -0.0041 S23:   0.5650                       
-REMARK   3      S31:  -0.4725 S32:  -0.0689 S33:  -0.0009                       
-REMARK   3   TLS GROUP : 10                                                     
-REMARK   3    SELECTION: chain 'B' and (resid 88 through 100 )                  
-REMARK   3    ORIGIN FOR THE GROUP (A): -13.6201   5.4722  -8.7300              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3285 T22:   0.2809                                     
-REMARK   3      T33:   0.4418 T12:   0.0033                                     
-REMARK   3      T13:  -0.0756 T23:   0.0819                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   4.7080 L22:   6.5543                                     
-REMARK   3      L33:   9.0136 L12:  -0.2897                                     
-REMARK   3      L13:   0.5454 L23:   2.9229                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0167 S12:   0.1832 S13:   0.6399                       
-REMARK   3      S21:   0.1989 S22:  -0.1656 S23:   0.1336                       
-REMARK   3      S31:  -0.4471 S32:  -0.2982 S33:   0.0286                       
-REMARK   3   TLS GROUP : 11                                                     
-REMARK   3    SELECTION: chain 'B' and (resid 101 through 127 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A): -19.4581   1.0517 -17.8888              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4451 T22:   0.5360                                     
-REMARK   3      T33:   0.7020 T12:  -0.0544                                     
-REMARK   3      T13:  -0.1737 T23:   0.0758                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   5.6249 L22:   4.2114                                     
-REMARK   3      L33:   4.7536 L12:  -2.4673                                     
-REMARK   3      L13:  -1.0265 L23:  -1.0321                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.3066 S12:   0.1490 S13:  -0.3129                       
-REMARK   3      S21:   0.3123 S22:   0.3331 S23:   1.8742                       
-REMARK   3      S31:   0.5098 S32:  -1.0567 S33:  -0.4721                       
-REMARK   3   TLS GROUP : 12                                                     
-REMARK   3    SELECTION: chain 'B' and (resid 128 through 165 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0289   2.8212 -20.8366              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3105 T22:   0.2046                                     
-REMARK   3      T33:   0.2996 T12:  -0.0078                                     
-REMARK   3      T13:  -0.1292 T23:   0.0576                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   7.4033 L22:   3.3607                                     
-REMARK   3      L33:   3.1928 L12:  -3.0711                                     
-REMARK   3      L13:  -0.1955 L23:  -0.2494                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0449 S12:   0.2226 S13:  -0.2503                       
-REMARK   3      S21:  -0.4713 S22:   0.0433 S23:   0.6805                       
-REMARK   3      S31:  -0.1652 S32:   0.0517 S33:  -0.0899                       
-REMARK   3   TLS GROUP : 13                                                     
-REMARK   3    SELECTION: chain 'B' and (resid 166 through 179 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):   1.7217   3.5405 -22.9572              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3020 T22:   0.2842                                     
-REMARK   3      T33:   0.2183 T12:  -0.0475                                     
-REMARK   3      T13:  -0.0280 T23:   0.0484                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.8428 L22:   3.4867                                     
-REMARK   3      L33:   2.6575 L12:  -2.1537                                     
-REMARK   3      L13:  -1.8438 L23:   1.4901                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.1121 S12:   0.2952 S13:   0.1938                       
-REMARK   3      S21:  -0.1234 S22:   0.1184 S23:   0.0988                       
-REMARK   3      S31:  -0.1890 S32:   0.0746 S33:   0.0474                       
-REMARK   3   TLS GROUP : 14                                                     
-REMARK   3    SELECTION: chain 'B' and (resid 180 through 217 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):   3.7454 -13.7514 -12.7741              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2674 T22:   0.2860                                     
-REMARK   3      T33:   0.2342 T12:   0.0261                                     
-REMARK   3      T13:   0.0026 T23:  -0.0712                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   3.6259 L22:   6.6450                                     
-REMARK   3      L33:   3.8025 L12:   1.7450                                     
-REMARK   3      L13:   0.3382 L23:  -0.8431                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0850 S12:   0.4215 S13:  -0.4131                       
-REMARK   3      S21:  -0.4885 S22:   0.1456 S23:  -0.0432                       
-REMARK   3      S31:   0.5445 S32:   0.0073 S33:  -0.0711                       
-REMARK   3   TLS GROUP : 15                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 4 through 17 )                    
-REMARK   3    ORIGIN FOR THE GROUP (A): -14.8002   5.2641  25.7419              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4519 T22:   0.5025                                     
-REMARK   3      T33:   0.5261 T12:  -0.1123                                     
-REMARK   3      T13:   0.2360 T23:  -0.1521                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.4939 L22:   0.2716                                     
-REMARK   3      L33:   4.0367 L12:  -0.7858                                     
-REMARK   3      L13:  -1.2106 L23:   0.1507                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2196 S12:  -0.1074 S13:  -0.3731                       
-REMARK   3      S21:   1.2339 S22:  -0.6445 S23:   1.0583                       
-REMARK   3      S31:  -0.1297 S32:  -0.6932 S33:   0.3067                       
-REMARK   3   TLS GROUP : 16                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 18 through 37 )                   
-REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2078  -8.0140  25.2309              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4199 T22:   0.2999                                     
-REMARK   3      T33:   0.3372 T12:  -0.1174                                     
-REMARK   3      T13:   0.0404 T23:   0.0325                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   4.5958 L22:   2.0855                                     
-REMARK   3      L33:   5.3145 L12:   1.4540                                     
-REMARK   3      L13:   1.9488 L23:   0.0979                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.4184 S12:  -0.3626 S13:  -0.5220                       
-REMARK   3      S21:   0.4671 S22:  -0.1381 S23:   0.1603                       
-REMARK   3      S31:   0.6002 S32:  -0.2884 S33:  -0.2772                       
-REMARK   3   TLS GROUP : 17                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 38 through 56 )                   
-REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5354  14.3474  13.8291              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3400 T22:   0.2063                                     
-REMARK   3      T33:   0.3313 T12:  -0.0001                                     
-REMARK   3      T13:   0.1224 T23:  -0.0235                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   5.7932 L22:   6.3044                                     
-REMARK   3      L33:   3.8763 L12:   4.2064                                     
-REMARK   3      L13:   0.0905 L23:  -0.0663                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.1031 S12:   0.0624 S13:   0.7132                       
-REMARK   3      S21:  -0.5421 S22:   0.0949 S23:   0.1644                       
-REMARK   3      S31:  -0.6505 S32:  -0.1254 S33:  -0.1066                       
-REMARK   3   TLS GROUP : 18                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 57 through 85 )                   
-REMARK   3    ORIGIN FOR THE GROUP (A):   6.0027  13.8690  15.5492              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3351 T22:   0.2157                                     
-REMARK   3      T33:   0.2640 T12:  -0.1063                                     
-REMARK   3      T13:   0.0809 T23:  -0.0342                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   4.6491 L22:   0.5365                                     
-REMARK   3      L33:   3.0010 L12:  -0.6665                                     
-REMARK   3      L13:   1.3498 L23:   0.8748                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0577 S12:   0.0339 S13:   0.4225                       
-REMARK   3      S21:   0.0477 S22:  -0.1015 S23:   0.1085                       
-REMARK   3      S31:  -0.5330 S32:   0.3055 S33:   0.0232                       
-REMARK   3   TLS GROUP : 19                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 86 through 100 )                  
-REMARK   3    ORIGIN FOR THE GROUP (A):   9.0002  17.3071  12.2154              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5092 T22:   0.3385                                     
-REMARK   3      T33:   0.4654 T12:  -0.0712                                     
-REMARK   3      T13:   0.0850 T23:  -0.0447                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   3.7662 L22:   3.8053                                     
-REMARK   3      L33:   3.8671 L12:   2.5060                                     
-REMARK   3      L13:   0.2796 L23:   3.0611                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.3232 S12:  -0.0318 S13:   0.7002                       
-REMARK   3      S21:  -0.2447 S22:   0.1126 S23:   0.2700                       
-REMARK   3      S31:  -1.6107 S32:  -0.1009 S33:   0.3292                       
-REMARK   3   TLS GROUP : 20                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 101 through 127 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):  16.2858  21.2308  25.1680              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5071 T22:   0.4735                                     
-REMARK   3      T33:   0.5341 T12:  -0.0457                                     
-REMARK   3      T13:   0.1161 T23:   0.0398                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   5.1569 L22:   3.0106                                     
-REMARK   3      L33:   9.6358 L12:  -2.9825                                     
-REMARK   3      L13:   3.6773 L23:  -4.6960                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2981 S12:  -0.3220 S13:   0.7213                       
-REMARK   3      S21:   0.1061 S22:  -0.8327 S23:  -1.2978                       
-REMARK   3      S31:   0.4972 S32:   1.0513 S33:   0.3472                       
-REMARK   3   TLS GROUP : 21                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 128 through 152 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):   5.6286  19.9185  29.9169              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2659 T22:   0.2222                                     
-REMARK   3      T33:   0.2617 T12:  -0.0345                                     
-REMARK   3      T13:   0.0677 T23:  -0.0594                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   5.7029 L22:   7.0638                                     
-REMARK   3      L33:   8.3276 L12:   2.4706                                     
-REMARK   3      L13:  -2.0266 L23:  -2.9262                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:  -0.0218 S12:  -0.4065 S13:   0.1586                       
-REMARK   3      S21:   0.2687 S22:  -0.3832 S23:  -0.2002                       
-REMARK   3      S31:  -0.0449 S32:   0.0873 S33:   0.3842                       
-REMARK   3   TLS GROUP : 22                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 153 through 165 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):   1.9947  20.8924  24.2281              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3617 T22:   0.2000                                     
-REMARK   3      T33:   0.3001 T12:  -0.0679                                     
-REMARK   3      T13:   0.1359 T23:  -0.0704                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   7.2222 L22:   7.6794                                     
-REMARK   3      L33:   2.9007 L12:   4.8860                                     
-REMARK   3      L13:   0.0328 L23:  -0.2847                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0094 S12:   0.3612 S13:   0.2829                       
-REMARK   3      S21:   0.0456 S22:   0.0181 S23:  -0.0041                       
-REMARK   3      S31:  -0.3718 S32:  -0.1961 S33:   0.0242                       
-REMARK   3   TLS GROUP : 23                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 166 through 179 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):  -5.6439  17.6761  31.3303              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.5744 T22:   0.4890                                     
-REMARK   3      T33:   0.4615 T12:  -0.0777                                     
-REMARK   3      T13:   0.2231 T23:  -0.1319                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   0.2801 L22:   0.4819                                     
-REMARK   3      L33:   6.0005 L12:   0.3319                                     
-REMARK   3      L13:  -1.2257 L23:  -1.6367                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.3794 S12:  -0.5828 S13:   0.4005                       
-REMARK   3      S21:   0.6050 S22:  -0.0997 S23:   0.3705                       
-REMARK   3      S31:  -1.4104 S32:  -0.1493 S33:  -0.3174                       
-REMARK   3   TLS GROUP : 24                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 180 through 197 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2843   2.6492  30.3826              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3827 T22:   0.3258                                     
-REMARK   3      T33:   0.2227 T12:  -0.1238                                     
-REMARK   3      T13:   0.0693 T23:  -0.0195                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   6.1945 L22:   5.2026                                     
-REMARK   3      L33:   2.8929 L12:  -2.5123                                     
-REMARK   3      L13:   1.4510 L23:  -1.7782                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0302 S12:  -0.5840 S13:  -0.0394                       
-REMARK   3      S21:   0.7396 S22:  -0.0750 S23:   0.0436                       
-REMARK   3      S31:  -0.1888 S32:   0.2572 S33:   0.0432                       
-REMARK   3   TLS GROUP : 25                                                     
-REMARK   3    SELECTION: chain 'C' and (resid 198 through 217 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2277  -4.9589  31.0597              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.3256 T22:   0.3494                                     
-REMARK   3      T33:   0.2430 T12:  -0.1166                                     
-REMARK   3      T13:   0.0292 T23:   0.0229                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   6.5854 L22:   7.0219                                     
-REMARK   3      L33:   3.8471 L12:  -0.9788                                     
-REMARK   3      L13:  -0.0121 L23:  -1.6477                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2853 S12:  -1.1363 S13:  -0.3380                       
-REMARK   3      S21:   0.7591 S22:  -0.0161 S23:  -0.1311                       
-REMARK   3      S31:  -0.1604 S32:   0.0951 S33:  -0.2664                       
-REMARK   3   TLS GROUP : 26                                                     
-REMARK   3    SELECTION: chain 'D' and (resid 4 through 37 )                    
-REMARK   3    ORIGIN FOR THE GROUP (A): -19.7687   7.9262  12.3306              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2938 T22:   0.3022                                     
-REMARK   3      T33:   0.5025 T12:   0.0628                                     
-REMARK   3      T13:   0.1000 T23:  -0.0411                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.0154 L22:   1.4706                                     
-REMARK   3      L33:   4.9327 L12:   1.5759                                     
-REMARK   3      L13:   0.6482 L23:   1.6684                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.2635 S12:  -0.1958 S13:   0.3666                       
-REMARK   3      S21:   0.2279 S22:  -0.2062 S23:   0.6715                       
-REMARK   3      S31:  -0.6958 S32:  -0.4394 S33:  -0.1152                       
-REMARK   3   TLS GROUP : 27                                                     
-REMARK   3    SELECTION: chain 'D' and (resid 38 through 85 )                   
-REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3180 -11.1190   4.8960              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2029 T22:   0.1682                                     
-REMARK   3      T33:   0.2818 T12:  -0.0174                                     
-REMARK   3      T13:  -0.0111 T23:   0.0018                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   2.6384 L22:   0.7363                                     
-REMARK   3      L33:   3.0040 L12:  -0.4053                                     
-REMARK   3      L13:   0.0498 L23:   0.9104                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0868 S12:  -0.0227 S13:  -0.2157                       
-REMARK   3      S21:   0.0834 S22:   0.0141 S23:   0.1540                       
-REMARK   3      S31:   0.1725 S32:   0.1730 S33:  -0.0901                       
-REMARK   3   TLS GROUP : 28                                                     
-REMARK   3    SELECTION: chain 'D' and (resid 86 through 102 )                  
-REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3858 -15.3306  -2.4011              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2033 T22:   0.2437                                     
-REMARK   3      T33:   0.2731 T12:  -0.0290                                     
-REMARK   3      T13:   0.0366 T23:  -0.0046                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   5.8711 L22:   2.5353                                     
-REMARK   3      L33:   6.1068 L12:   3.2149                                     
-REMARK   3      L13:   3.3977 L23:   1.6686                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0517 S12:  -0.1318 S13:  -0.3811                       
-REMARK   3      S21:   0.0170 S22:   0.1104 S23:   0.0416                       
-REMARK   3      S31:   0.2354 S32:  -0.2260 S33:  -0.2115                       
-REMARK   3   TLS GROUP : 29                                                     
-REMARK   3    SELECTION: chain 'D' and (resid 103 through 127 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A): -21.1679 -17.6624 -10.5807              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.4050 T22:   0.4330                                     
-REMARK   3      T33:   0.4386 T12:  -0.0910                                     
-REMARK   3      T13:  -0.0558 T23:  -0.0559                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   5.8089 L22:   4.6034                                     
-REMARK   3      L33:   5.8075 L12:  -4.9288                                     
-REMARK   3      L13:   4.0693 L23:  -4.6891                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.1487 S12:   0.7254 S13:   0.6893                       
-REMARK   3      S21:  -1.1507 S22:  -0.5453 S23:  -0.6519                       
-REMARK   3      S31:   0.3356 S32:   0.0048 S33:   0.4885                       
-REMARK   3   TLS GROUP : 30                                                     
-REMARK   3    SELECTION: chain 'D' and (resid 128 through 165 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A): -22.0224 -16.9523   0.6254              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.1555 T22:   0.1799                                     
-REMARK   3      T33:   0.2530 T12:  -0.0535                                     
-REMARK   3      T13:  -0.0014 T23:   0.0325                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   3.1201 L22:   7.1702                                     
-REMARK   3      L33:   3.9062 L12:  -2.9147                                     
-REMARK   3      L13:  -2.0855 L23:   4.8093                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0171 S12:   0.1705 S13:   0.0210                       
-REMARK   3      S21:   0.1975 S22:  -0.1344 S23:   0.1069                       
-REMARK   3      S31:   0.1501 S32:  -0.2435 S33:   0.1238                       
-REMARK   3   TLS GROUP : 31                                                     
-REMARK   3    SELECTION: chain 'D' and (resid 166 through 217 )                 
-REMARK   3    ORIGIN FOR THE GROUP (A): -24.6784   0.8813   5.0001              
-REMARK   3    T TENSOR                                                          
-REMARK   3      T11:   0.2228 T22:   0.3741                                     
-REMARK   3      T33:   0.4971 T12:   0.0658                                     
-REMARK   3      T13:   0.0159 T23:  -0.0067                                     
-REMARK   3    L TENSOR                                                          
-REMARK   3      L11:   1.1335 L22:   3.0594                                     
-REMARK   3      L33:   3.5083 L12:   0.5127                                     
-REMARK   3      L13:  -0.4859 L23:  -0.3460                                     
-REMARK   3    S TENSOR                                                          
-REMARK   3      S11:   0.0416 S12:   0.1868 S13:   0.2085                       
-REMARK   3      S21:   0.0127 S22:  -0.0363 S23:   0.6115                       
-REMARK   3      S31:  -0.3381 S32:  -0.6544 S33:  -0.0106                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 4RAO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-14.                  
-REMARK 100 THE RCSB ID CODE IS RCSB087110.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-13                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : NULL                               
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
-REMARK 200  BEAMLINE                       : MX1                                
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95369                            
-REMARK 200  MONOCHROMATOR                  : NULL                               
-REMARK 200  OPTICS                         : NULL                               
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
-REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68208                              
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.870                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 46.430                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
-REMARK 200  DATA REDUNDANCY                : NULL                               
-REMARK 200  R MERGE                    (I) : NULL                               
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
-REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
-REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASES                                                
-REMARK 200 STARTING MODEL: NULL                                                 
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 41.02                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
-REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
-REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.30100            
-REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.42450            
-REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.42650            
-REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.42450            
-REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.30100            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.42650            
-REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 11660 ANGSTROM**2                         
-REMARK 350 SURFACE AREA OF THE COMPLEX: 29070 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL                        
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     ASP A    89                                                      
-REMARK 465     SER A   103                                                      
-REMARK 465     TYR A   104                                                      
-REMARK 465     CYS A   105                                                      
-REMARK 465     ASN A   106                                                      
-REMARK 465     ASP A   107                                                      
-REMARK 465     GLN A   108                                                      
-REMARK 465     SER A   109                                                      
-REMARK 465     THR A   110                                                      
-REMARK 465     GLY A   111                                                      
-REMARK 465     ASP A   112                                                      
-REMARK 465     ILE A   113                                                      
-REMARK 465     LYS A   114                                                      
-REMARK 465     VAL A   115                                                      
-REMARK 465     ILE A   116                                                      
-REMARK 465     GLY A   117                                                      
-REMARK 465     GLY A   118                                                      
-REMARK 465     ASP A   119                                                      
-REMARK 465     ASP A   120                                                      
-REMARK 465     ALA A   217                                                      
-REMARK 465     ALA B     1                                                      
-REMARK 465     THR B     2                                                      
-REMARK 465     ARG B     3                                                      
-REMARK 465     SER B   103                                                      
-REMARK 465     TYR B   104                                                      
-REMARK 465     CYS B   105                                                      
-REMARK 465     ASN B   106                                                      
-REMARK 465     ASP B   107                                                      
-REMARK 465     GLN B   108                                                      
-REMARK 465     SER B   109                                                      
-REMARK 465     THR B   110                                                      
-REMARK 465     GLY B   111                                                      
-REMARK 465     ASP B   112                                                      
-REMARK 465     ILE B   113                                                      
-REMARK 465     LYS B   114                                                      
-REMARK 465     LEU B   121                                                      
-REMARK 465     SER B   122                                                      
-REMARK 465     VAL B   171                                                      
-REMARK 465     GLY B   172                                                      
-REMARK 465     ALA C     1                                                      
-REMARK 465     THR C     2                                                      
-REMARK 465     ARG C     3                                                      
-REMARK 465     SER C   103                                                      
-REMARK 465     TYR C   104                                                      
-REMARK 465     CYS C   105                                                      
-REMARK 465     ASN C   106                                                      
-REMARK 465     ASP C   107                                                      
-REMARK 465     GLN C   108                                                      
-REMARK 465     SER C   109                                                      
-REMARK 465     THR C   110                                                      
-REMARK 465     GLY C   111                                                      
-REMARK 465     ASP C   112                                                      
-REMARK 465     ILE C   113                                                      
-REMARK 465     ALA D     1                                                      
-REMARK 465     THR D     2                                                      
-REMARK 465     ARG D     3                                                      
-REMARK 465     CYS D   105                                                      
-REMARK 465     ASN D   106                                                      
-REMARK 465     ASP D   107                                                      
-REMARK 465     GLN D   108                                                      
-REMARK 465     SER D   109                                                      
-REMARK 465     THR D   110                                                      
-REMARK 465     GLY D   111                                                      
-REMARK 470                                                                      
-REMARK 470 MISSING ATOM                                                         
-REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
-REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
-REMARK 470 I=INSERTION CODE):                                                   
-REMARK 470   M RES CSSEQI  ATOMS                                                
-REMARK 470     CYS A  22    SG                                                  
-REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     LYS A 102    CG   CD   CE   NZ                                   
-REMARK 470     CYS A 205    SG                                                  
-REMARK 470     CYS B  22    SG                                                  
-REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
-REMARK 470     ILE B  92    CG1  CG2  CD1                                       
-REMARK 470     LYS B 102    CG   CD   CE   NZ                                   
-REMARK 470     ASP B 120    CG   OD1  OD2                                       
-REMARK 470     LYS B 174    CG   CD   CE   NZ                                   
-REMARK 470     CYS B 205    SG                                                  
-REMARK 470     CYS C  22    SG                                                  
-REMARK 470     ILE C  92    CG1  CG2  CD1                                       
-REMARK 470     LYS C 102    CG   CD   CE   NZ                                   
-REMARK 470     LYS C 114    CG   CD   CE   NZ                                   
-REMARK 470     CYS C 205    SG                                                  
-REMARK 470     CYS D  22    SG                                                  
-REMARK 470     ASP D 112    CG   OD1  OD2                                       
-REMARK 470     CYS D 205    SG                                                  
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   O    LYS B   165     NH2  ARG B   169              2.17            
-REMARK 500   O    HOH C   450     O    HOH C   451              2.19            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
-REMARK 500                                                                      
-REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
-REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
-REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
-REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
-REMARK 500    PRO B  93   C   -  N   -  CA  ANGL. DEV. =  20.8 DEGREES          
-REMARK 500    PRO B  93   C   -  N   -  CD  ANGL. DEV. = -17.6 DEGREES          
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASP A 137      -79.98   -119.09                                   
-REMARK 500    ASN A 153       68.36     38.12                                   
-REMARK 500    ALA A 191      -12.06     80.32                                   
-REMARK 500    GLU A 196      -11.43     79.36                                   
-REMARK 500    SER B  88     -162.73   -106.70                                   
-REMARK 500    ILE B  92     -121.61    -71.69                                   
-REMARK 500    ASP B 137      -83.44   -122.03                                   
-REMARK 500    VAL B 149      -58.67     60.92                                   
-REMARK 500    ALA B 191      -10.33     82.40                                   
-REMARK 500    GLU B 196      -11.77     80.16                                   
-REMARK 500    ASP B 200       46.15    -89.31                                   
-REMARK 500    ASP C  12       33.68    -97.04                                   
-REMARK 500    LEU C 121        0.11    -65.26                                   
-REMARK 500    ASP C 137      -81.36   -118.99                                   
-REMARK 500    ALA C 191       -8.59     79.91                                   
-REMARK 500    GLU C 196      -12.94     75.85                                   
-REMARK 500    PHE C 198       -0.28     77.73                                   
-REMARK 500    ASP C 200       42.51    -89.00                                   
-REMARK 500    ASP D 137      -85.06   -118.19                                   
-REMARK 500    ALA D 191      -14.39     82.21                                   
-REMARK 500    GLU D 196      -10.81     78.97                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
-REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
-REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
-REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
-REMARK 500                                 MODEL     OMEGA                      
-REMARK 500 GLY B   58     HIS B   59                  145.45                    
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 620                                                                      
-REMARK 620 METAL COORDINATION                                                   
-REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG C 302  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 HOH C 450   O                                                      
-REMARK 620 2 GLU C 133   OE1 133.0                                              
-REMARK 620 3 HOH C 448   O    66.1  88.1                                        
-REMARK 620 4 ASP C 134   OD1 126.1  81.1 167.6                                  
-REMARK 620 5 HOH C 405   O    99.4 120.5  90.6  89.5                            
-REMARK 620 6 HOH C 411   O    63.6  79.1  90.8  93.2 160.4                      
-REMARK 620 7 HOH C 451   O    56.2 146.0 119.2  73.1  81.7  80.6                
-REMARK 620 N                    1     2     3     4     5     6                 
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG D 302  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 HOH D 447   O                                                      
-REMARK 620 2 HOH D 445   O    93.6                                              
-REMARK 620 3 GLU D 133   OE1 101.7  85.8                                        
-REMARK 620 4 HOH D 410   O    86.5 163.2 110.7                                  
-REMARK 620 5 HOH D 401   O   113.3  76.9 141.5  87.6                            
-REMARK 620 6 ASP D 134   OD1 171.0  94.4  74.8  87.0  72.6                      
-REMARK 620 N                    1     2     3     4     5                       
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG B 303  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 HOH B 447   O                                                      
-REMARK 620 2 ASP B 193   OD1  91.9                                              
-REMARK 620 3 HOH B 448   O    90.0 171.7                                        
-REMARK 620 4 3L7 B 301   OAE  84.5  83.8 104.4                                  
-REMARK 620 5 HOH B 446   O   170.5  85.3  91.6 104.2                            
-REMARK 620 6 HOH B 421   O    90.8  81.0  90.9 164.0  79.8                      
-REMARK 620 N                    1     2     3     4     5                       
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG B 302  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 GLU B 133   OE1                                                    
-REMARK 620 2 ASP B 134   OD1  81.8                                              
-REMARK 620 3 3L7 B 301   OAU 137.1 136.3                                        
-REMARK 620 4 GLU B 133   OE2  50.5 116.2 106.3                                  
-REMARK 620 N                    1     2     3                                   
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG C 303  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 HOH C 452   O                                                      
-REMARK 620 2 ASP C 193   OD1  97.6                                              
-REMARK 620 3 HOH C 453   O    67.3 149.1                                        
-REMARK 620 4 HOH C 421   O   159.3  99.0 102.9                                  
-REMARK 620 5 HOH C 412   O    87.8  82.9 121.3  82.0                            
-REMARK 620 6 3L7 C 301   OAB  93.7  86.0  69.1  99.7 168.9                      
-REMARK 620 7 HOH C 438   O    78.0 154.4  52.1  81.7  71.7 119.3                
-REMARK 620 N                    1     2     3     4     5     6                 
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG D 303  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 ASP D 193   OD1                                                    
-REMARK 620 2 HOH D 425   O    82.9                                              
-REMARK 620 3 HOH D 446   O    98.2 109.9                                        
-REMARK 620 4 3L7 D 301   OAE  73.3 155.3  80.5                                  
-REMARK 620 N                    1     2     3                                   
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG A 302  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 HOH A 449   O                                                      
-REMARK 620 2 HOH A 450   O    96.0                                              
-REMARK 620 3 HOH A 418   O    86.1  77.4                                        
-REMARK 620 4 GLU A 133   OE1 109.5 145.7  81.8                                  
-REMARK 620 5 ASP A 134   OD1 176.1  80.4  94.3  74.3                            
-REMARK 620 6 HOH A 426   O    94.9  80.7 158.1 118.1  83.3                      
-REMARK 620 7 GLU A 133   OE2  78.5 161.4 119.5  51.2 104.6  82.0                
-REMARK 620 N                    1     2     3     4     5     6                 
-REMARK 620                                                                      
-REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
-REMARK 620                              MG A 303  MG                            
-REMARK 620 N RES CSSEQI ATOM                                                    
-REMARK 620 1 ASP A 193   OD1                                                    
-REMARK 620 2 3L7 A 301   OAD  83.9                                              
-REMARK 620 3 HOH A 451   O    79.1 157.1                                        
-REMARK 620 4 HOH A 452   O    86.1  88.1  75.5                                  
-REMARK 620 N                    1     2     3                                   
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 A 301                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC4                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 B 301                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC5                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 302                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC6                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 303                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC7                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 C 301                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC8                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 302                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC9                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 303                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 D 301                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 302                  
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: BC3                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 303                  
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 4RAB   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 4RAC   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 4RAD   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 4RAN   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 4RAQ   RELATED DB: PDB                                   
-DBREF  4RAO A    1   217  UNP    P00492   HPRT_HUMAN       2    218             
-DBREF  4RAO B    1   217  UNP    P00492   HPRT_HUMAN       2    218             
-DBREF  4RAO C    1   217  UNP    P00492   HPRT_HUMAN       2    218             
-DBREF  4RAO D    1   217  UNP    P00492   HPRT_HUMAN       2    218             
-SEQRES   1 A  217  ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU          
-SEQRES   2 A  217  PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS          
-SEQRES   3 A  217  TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY          
-SEQRES   4 A  217  LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL          
-SEQRES   5 A  217  MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS          
-SEQRES   6 A  217  VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU          
-SEQRES   7 A  217  ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER          
-SEQRES   8 A  217  ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR          
-SEQRES   9 A  217  CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY          
-SEQRES  10 A  217  GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU          
-SEQRES  11 A  217  ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN          
-SEQRES  12 A  217  THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET          
-SEQRES  13 A  217  VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG          
-SEQRES  14 A  217  SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE          
-SEQRES  15 A  217  PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN          
-SEQRES  16 A  217  GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER          
-SEQRES  17 A  217  GLU THR GLY LYS ALA LYS TYR LYS ALA                          
-SEQRES   1 B  217  ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU          
-SEQRES   2 B  217  PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS          
-SEQRES   3 B  217  TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY          
-SEQRES   4 B  217  LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL          
-SEQRES   5 B  217  MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS          
-SEQRES   6 B  217  VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU          
-SEQRES   7 B  217  ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER          
-SEQRES   8 B  217  ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR          
-SEQRES   9 B  217  CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY          
-SEQRES  10 B  217  GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU          
-SEQRES  11 B  217  ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN          
-SEQRES  12 B  217  THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET          
-SEQRES  13 B  217  VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG          
-SEQRES  14 B  217  SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE          
-SEQRES  15 B  217  PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN          
-SEQRES  16 B  217  GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER          
-SEQRES  17 B  217  GLU THR GLY LYS ALA LYS TYR LYS ALA                          
-SEQRES   1 C  217  ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU          
-SEQRES   2 C  217  PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS          
-SEQRES   3 C  217  TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY          
-SEQRES   4 C  217  LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL          
-SEQRES   5 C  217  MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS          
-SEQRES   6 C  217  VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU          
-SEQRES   7 C  217  ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER          
-SEQRES   8 C  217  ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR          
-SEQRES   9 C  217  CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY          
-SEQRES  10 C  217  GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU          
-SEQRES  11 C  217  ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN          
-SEQRES  12 C  217  THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET          
-SEQRES  13 C  217  VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG          
-SEQRES  14 C  217  SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE          
-SEQRES  15 C  217  PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN          
-SEQRES  16 C  217  GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER          
-SEQRES  17 C  217  GLU THR GLY LYS ALA LYS TYR LYS ALA                          
-SEQRES   1 D  217  ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU          
-SEQRES   2 D  217  PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS          
-SEQRES   3 D  217  TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY          
-SEQRES   4 D  217  LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL          
-SEQRES   5 D  217  MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS          
-SEQRES   6 D  217  VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU          
-SEQRES   7 D  217  ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER          
-SEQRES   8 D  217  ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR          
-SEQRES   9 D  217  CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY          
-SEQRES  10 D  217  GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU          
-SEQRES  11 D  217  ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN          
-SEQRES  12 D  217  THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET          
-SEQRES  13 D  217  VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG          
-SEQRES  14 D  217  SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE          
-SEQRES  15 D  217  PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN          
-SEQRES  16 D  217  GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER          
-SEQRES  17 D  217  GLU THR GLY LYS ALA LYS TYR LYS ALA                          
-HET    3L7  A 301      28                                                       
-HET     MG  A 302       1                                                       
-HET     MG  A 303       1                                                       
-HET    3L7  B 301      56                                                       
-HET     MG  B 302       1                                                       
-HET     MG  B 303       1                                                       
-HET    3L7  C 301      28                                                       
-HET     MG  C 302       1                                                       
-HET     MG  C 303       1                                                       
-HET    3L7  D 301      28                                                       
-HET     MG  D 302       1                                                       
-HET     MG  D 303       1                                                       
-HETNAM     3L7 (2-{[2-(6-OXO-1,6-DIHYDRO-9H-PURIN-9-YL)ETHYL](2-{[(E)-          
-HETNAM   2 3L7  2-PHOSPHONOETHENYL]OXY}ETHYL)AMINO}ETHYL)PHOSPHONIC             
-HETNAM   3 3L7  ACID                                                            
-HETNAM      MG MAGNESIUM ION                                                    
-FORMUL   5  3L7    4(C13 H21 N5 O8 P2)                                          
-FORMUL   6   MG    8(MG 2+)                                                     
-FORMUL  17  HOH   *201(H2 O)                                                    
-HELIX    1   1 ASP A   17  PHE A   21  5                                   5    
-HELIX    2   2 PRO A   24  ALA A   28  5                                   5    
-HELIX    3   3 PRO A   37  GLY A   57  1                                  21    
-HELIX    4   4 GLY A   70  ASN A   87  1                                  18    
-HELIX    5   5 LEU A  121  THR A  125  5                                   5    
-HELIX    6   6 GLY A  139  ARG A  150  1                                  12    
-HELIX    7   7 GLN A  151  ASN A  153  5                                   3    
-HELIX    8   8 SER A  208  LYS A  216  1                                   9    
-HELIX    9   9 ASP B   17  PHE B   21  5                                   5    
-HELIX   10  10 PRO B   24  ALA B   28  5                                   5    
-HELIX   11  11 PRO B   37  GLY B   57  1                                  21    
-HELIX   12  12 GLY B   70  SER B   88  1                                  19    
-HELIX   13  13 GLY B  139  GLN B  151  1                                  13    
-HELIX   14  14 SER B  208  TYR B  215  1                                   8    
-HELIX   15  15 ASP C   17  PHE C   21  5                                   5    
-HELIX   16  16 PRO C   24  ALA C   28  5                                   5    
-HELIX   17  17 PRO C   37  GLY C   57  1                                  21    
-HELIX   18  18 GLY C   70  ARG C   86  1                                  17    
-HELIX   19  19 ASP C  120  THR C  125  5                                   6    
-HELIX   20  20 GLY C  139  GLN C  151  1                                  13    
-HELIX   21  21 SER C  208  TYR C  215  1                                   8    
-HELIX   22  22 ASP D   17  PHE D   21  5                                   5    
-HELIX   23  23 PRO D   24  ALA D   28  5                                   5    
-HELIX   24  24 PRO D   37  GLY D   57  1                                  21    
-HELIX   25  25 GLY D   70  ARG D   86  1                                  17    
-HELIX   26  26 ASP D  120  THR D  125  5                                   6    
-HELIX   27  27 GLY D  139  ARG D  150  1                                  12    
-HELIX   28  28 GLN D  151  ASN D  153  5                                   3    
-HELIX   29  29 SER D  208  LYS D  216  1                                   9    
-SHEET    1   A 6 VAL A   7  VAL A   8  0                                        
-SHEET    2   A 6 PHE A 177  ILE A 182  1  O  GLU A 181   N  VAL A   7           
-SHEET    3   A 6 MET A 156  LYS A 165  1  N  SER A 161   O  PHE A 177           
-SHEET    4   A 6 ASN A 128  ILE A 136  1  N  ILE A 131   O  ALA A 160           
-SHEET    5   A 6 ILE A  61  LEU A  67  1  N  LEU A  64   O  LEU A 130           
-SHEET    6   A 6 MET A  94  ARG A 100  1  O  ASP A  97   N  CYS A  65           
-SHEET    1   B 3 LEU A  31  ILE A  36  0                                        
-SHEET    2   B 3 VAL A 204  ILE A 207 -1  O  VAL A 206   N  GLU A  32           
-SHEET    3   B 3 VAL A 187  VAL A 188 -1  N  VAL A 188   O  CYS A 205           
-SHEET    1   C 7 VAL B   7  VAL B   8  0                                        
-SHEET    2   C 7 PHE B 177  ILE B 182  1  O  GLU B 181   N  VAL B   7           
-SHEET    3   C 7 MET B 156  LYS B 165  1  N  SER B 161   O  PHE B 177           
-SHEET    4   C 7 ASN B 128  ILE B 136  1  N  ILE B 131   O  ALA B 160           
-SHEET    5   C 7 ILE B  61  LEU B  67  1  N  LEU B  64   O  LEU B 130           
-SHEET    6   C 7 MET B  94  ARG B 100  1  O  ILE B  99   N  LEU B  67           
-SHEET    7   C 7 ILE B 116  GLY B 117 -1  O  ILE B 116   N  ARG B 100           
-SHEET    1   D 3 LEU B  31  ILE B  36  0                                        
-SHEET    2   D 3 VAL B 204  ILE B 207 -1  O  VAL B 206   N  GLU B  32           
-SHEET    3   D 3 VAL B 187  VAL B 188 -1  N  VAL B 188   O  CYS B 205           
-SHEET    1   E 6 VAL C   7  VAL C   8  0                                        
-SHEET    2   E 6 PHE C 177  ILE C 182  1  O  GLU C 181   N  VAL C   7           
-SHEET    3   E 6 MET C 156  LYS C 165  1  N  SER C 161   O  PHE C 177           
-SHEET    4   E 6 ASN C 128  ILE C 136  1  N  VAL C 129   O  MET C 156           
-SHEET    5   E 6 ILE C  61  LEU C  67  1  N  LEU C  64   O  LEU C 130           
-SHEET    6   E 6 MET C  94  ARG C 100  1  O  ILE C  99   N  LEU C  67           
-SHEET    1   F 3 LEU C  31  ILE C  36  0                                        
-SHEET    2   F 3 VAL C 204  ILE C 207 -1  O  VAL C 206   N  GLU C  32           
-SHEET    3   F 3 VAL C 187  VAL C 188 -1  N  VAL C 188   O  CYS C 205           
-SHEET    1   G 7 VAL D   7  VAL D   8  0                                        
-SHEET    2   G 7 PHE D 177  ILE D 182  1  O  GLU D 181   N  VAL D   7           
-SHEET    3   G 7 MET D 156  LYS D 165  1  N  SER D 161   O  PHE D 177           
-SHEET    4   G 7 ASN D 128  ILE D 136  1  N  VAL D 129   O  MET D 156           
-SHEET    5   G 7 ILE D  61  VAL D  66  1  N  LEU D  64   O  LEU D 130           
-SHEET    6   G 7 MET D  94  LYS D 102  1  O  ASP D  97   N  CYS D  65           
-SHEET    7   G 7 LYS D 114  ILE D 116 -1  O  ILE D 116   N  ARG D 100           
-SHEET    1   H 3 LEU D  31  ILE D  36  0                                        
-SHEET    2   H 3 VAL D 204  ILE D 207 -1  O  VAL D 206   N  GLU D  32           
-SHEET    3   H 3 VAL D 187  VAL D 188 -1  N  VAL D 188   O  CYS D 205           
-LINK        MG    MG C 302                 O   HOH C 450     1555   1555  1.80  
-LINK        MG    MG D 302                 O   HOH D 447     1555   1555  1.91  
-LINK        MG    MG B 303                 O   HOH B 447     1555   1555  1.96  
-LINK         OE1AGLU B 133                MG    MG B 302     1555   1555  2.06  
-LINK         OD1 ASP B 134                MG    MG B 302     1555   1555  2.10  
-LINK        MG    MG C 303                 O   HOH C 452     1555   1555  2.11  
-LINK        MG    MG D 302                 O   HOH D 445     1555   1555  2.14  
-LINK         OE1 GLU D 133                MG    MG D 302     1555   1555  2.15  
-LINK         OD1 ASP B 193                MG    MG B 303     1555   1555  2.16  
-LINK         OD1 ASP D 193                MG    MG D 303     1555   1555  2.18  
-LINK         OE1BGLU B 133                MG    MG B 302     1555   1555  2.18  
-LINK         OE1 GLU C 133                MG    MG C 302     1555   1555  2.19  
-LINK         OD1 ASP C 193                MG    MG C 303     1555   1555  2.21  
-LINK        MG    MG A 302                 O   HOH A 449     1555   1555  2.21  
-LINK        MG    MG C 302                 O   HOH C 448     1555   1555  2.25  
-LINK        MG    MG C 303                 O   HOH C 453     1555   1555  2.25  
-LINK         OD1 ASP C 134                MG    MG C 302     1555   1555  2.26  
-LINK        MG    MG D 302                 O   HOH D 410     1555   1555  2.26  
-LINK        MG    MG B 303                 O   HOH B 448     1555   1555  2.27  
-LINK         OD1 ASP A 193                MG    MG A 303     1555   1555  2.27  
-LINK        MG    MG C 303                 O   HOH C 421     1555   1555  2.28  
-LINK         OAEB3L7 B 301                MG    MG B 303     1555   1555  2.28  
-LINK        MG    MG A 302                 O   HOH A 450     1555   1555  2.28  
-LINK        MG    MG A 302                 O   HOH A 418     1555   1555  2.29  
-LINK        MG    MG D 303                 O   HOH D 425     1555   1555  2.30  
-LINK        MG    MG C 302                 O   HOH C 405     1555   1555  2.31  
-LINK         OE1 GLU A 133                MG    MG A 302     1555   1555  2.33  
-LINK        MG    MG B 303                 O   HOH B 446     1555   1555  2.34  
-LINK        MG    MG D 303                 O   HOH D 446     1555   1555  2.35  
-LINK        MG    MG D 302                 O   HOH D 401     1555   1555  2.35  
-LINK         OD1 ASP A 134                MG    MG A 302     1555   1555  2.35  
-LINK         OD1 ASP D 134                MG    MG D 302     1555   1555  2.36  
-LINK         OAD 3L7 A 301                MG    MG A 303     1555   1555  2.41  
-LINK        MG    MG A 302                 O   HOH A 426     1555   1555  2.42  
-LINK        MG    MG C 302                 O   HOH C 411     1555   1555  2.45  
-LINK        MG    MG C 303                 O   HOH C 412     1555   1555  2.45  
-LINK        MG    MG B 303                 O   HOH B 421     1555   1555  2.48  
-LINK         OAB 3L7 C 301                MG    MG C 303     1555   1555  2.52  
-LINK        MG    MG C 302                 O   HOH C 451     1555   1555  2.60  
-LINK        MG    MG A 303                 O   HOH A 451     1555   1555  2.61  
-LINK         OAUB3L7 B 301                MG    MG B 302     1555   1555  2.63  
-LINK         OE2 GLU A 133                MG    MG A 302     1555   1555  2.69  
-LINK        MG    MG C 303                 O   HOH C 438     1555   1555  2.70  
-LINK        MG    MG A 303                 O   HOH A 452     1555   1555  2.74  
-LINK         OAE 3L7 D 301                MG    MG D 303     1555   1555  2.75  
-LINK         OE2AGLU B 133                MG    MG B 302     1555   1555  2.82  
-CISPEP   1 LEU A   67    LYS A   68          0        -2.10                     
-CISPEP   2 GLY B   57    GLY B   58          0         9.27                     
-CISPEP   3 LEU B   67    LYS B   68          0        -4.05                     
-CISPEP   4 ILE B   92    PRO B   93          0         0.30                     
-CISPEP   5 LEU C   67    LYS C   68          0        -2.75                     
-CISPEP   6 LEU D   67    LYS D   68          0        -8.23                     
-SITE     1 AC1 19 LYS A  68  GLY A  69  ASP A 137  THR A 138                    
-SITE     2 AC1 19 GLY A 139  LYS A 140  THR A 141  LYS A 165                    
-SITE     3 AC1 19 LYS A 185  PHE A 186  VAL A 187  ASP A 193                    
-SITE     4 AC1 19 ARG A 199   MG A 303  HOH A 412  HOH A 418                    
-SITE     5 AC1 19 HOH A 426  HOH A 450  HOH A 452                               
-SITE     1 AC2  6 GLU A 133  ASP A 134  HOH A 418  HOH A 426                    
-SITE     2 AC2  6 HOH A 449  HOH A 450                                          
-SITE     1 AC3  4 ASP A 193  3L7 A 301  HOH A 451  HOH A 452                    
-SITE     1 AC4 22 LYS B  68  GLY B  69  GLU B 133  ASP B 137                    
-SITE     2 AC4 22 THR B 138  GLY B 139  LYS B 140  THR B 141                    
-SITE     3 AC4 22 LYS B 165  LYS B 185  PHE B 186  VAL B 187                    
-SITE     4 AC4 22 ASP B 193  ARG B 199   MG B 302   MG B 303                    
-SITE     5 AC4 22 HOH B 401  HOH B 414  HOH B 430  HOH B 446                    
-SITE     6 AC4 22 HOH B 447  HOH B 448                                          
-SITE     1 AC5  3 GLU B 133  ASP B 134  3L7 B 301                               
-SITE     1 AC6  6 ASP B 193  3L7 B 301  HOH B 421  HOH B 446                    
-SITE     2 AC6  6 HOH B 447  HOH B 448                                          
-SITE     1 AC7 25 LYS C  68  GLY C  69  ARG C 100  ASP C 137                    
-SITE     2 AC7 25 THR C 138  GLY C 139  LYS C 140  THR C 141                    
-SITE     3 AC7 25 LYS C 165  LYS C 185  PHE C 186  VAL C 187                    
-SITE     4 AC7 25 ASP C 193  ARG C 199   MG C 303  HOH C 402                    
-SITE     5 AC7 25 HOH C 405  HOH C 411  HOH C 413  HOH C 418                    
-SITE     6 AC7 25 HOH C 421  HOH C 449  HOH C 450  HOH C 451                    
-SITE     7 AC7 25 HOH C 453                                                     
-SITE     1 AC8  7 GLU C 133  ASP C 134  HOH C 405  HOH C 411                    
-SITE     2 AC8  7 HOH C 448  HOH C 450  HOH C 451                               
-SITE     1 AC9  7 ASP C 193  3L7 C 301  HOH C 412  HOH C 421                    
-SITE     2 AC9  7 HOH C 438  HOH C 452  HOH C 453                               
-SITE     1 BC1 19 LYS D  68  GLY D  69  ASP D 137  THR D 138                    
-SITE     2 BC1 19 GLY D 139  LYS D 140  THR D 141  LYS D 165                    
-SITE     3 BC1 19 LYS D 185  PHE D 186  VAL D 187  ASP D 193                    
-SITE     4 BC1 19 ARG D 199   MG D 303  HOH D 401  HOH D 405                    
-SITE     5 BC1 19 HOH D 410  HOH D 432  HOH D 445                               
-SITE     1 BC2  6 GLU D 133  ASP D 134  HOH D 401  HOH D 410                    
-SITE     2 BC2  6 HOH D 445  HOH D 447                                          
-SITE     1 BC3  4 ASP D 193  3L7 D 301  HOH D 425  HOH D 446                    
-CRYST1   76.602   92.853  114.849  90.00  90.00  90.00 P 21 21 21   16          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.013054  0.000000  0.000000        0.00000                         
-SCALE2      0.000000  0.010770  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.008707        0.00000                         
-ATOM      1  N   ALA A   1      29.351 -15.299  10.549  1.00 74.92           N  
-ANISOU    1  N   ALA A   1     7124   9614  11727    415  -2282   2479       N  
-ATOM      2  CA  ALA A   1      28.468 -14.947   9.436  1.00 73.31           C  
-ANISOU    2  CA  ALA A   1     7090   9292  11472    457  -2044   2081       C  
-ATOM      3  C   ALA A   1      27.420 -13.904   9.827  1.00 70.93           C  
-ANISOU    3  C   ALA A   1     7078   9180  10693    224  -1925   2028       C  
-ATOM      4  O   ALA A   1      26.898 -13.915  10.943  1.00 70.22           O  
-ANISOU    4  O   ALA A   1     7090   9184  10407     75  -2003   2318       O  
-ATOM      5  CB  ALA A   1      27.789 -16.190   8.876  1.00 72.44           C  
-ANISOU    5  CB  ALA A   1     6943   8763  11820    639  -2052   2026       C  
-ATOM      6  N   THR A   2      27.118 -13.006   8.896  1.00 68.65           N  
-ANISOU    6  N   THR A   2     6912   8955  10215    211  -1725   1667       N  
-ATOM      7  CA  THR A   2      26.058 -12.025   9.086  1.00 67.59           C  
-ANISOU    7  CA  THR A   2     7040   8946   9696     24  -1591   1568       C  
-ATOM      8  C   THR A   2      24.709 -12.738   9.002  1.00 65.98           C  
-ANISOU    8  C   THR A   2     6940   8476   9654     47  -1545   1596       C  
-ATOM      9  O   THR A   2      24.376 -13.318   7.963  1.00 65.77           O  
-ANISOU    9  O   THR A   2     6881   8188   9921    208  -1498   1377       O  
-ATOM     10  CB  THR A   2      26.121 -10.925   8.005  1.00 67.81           C  
-ANISOU   10  CB  THR A   2     7139   9079   9545     22  -1398   1203       C  
-ATOM     11  OG1 THR A   2      27.483 -10.518   7.811  1.00 70.55           O  
-ANISOU   11  OG1 THR A   2     7304   9595   9908     54  -1433   1186       O  
-ATOM     12  CG2 THR A   2      25.271  -9.717   8.403  1.00 64.90           C  
-ANISOU   12  CG2 THR A   2     7011   8877   8770   -192  -1293   1135       C  
-ATOM     13  N   ARG A   3      23.943 -12.700  10.094  1.00 59.98           N  
-ANISOU   13  N   ARG A   3     6293   7790   8707   -105  -1564   1865       N  
-ATOM     14  CA  ARG A   3      22.657 -13.400  10.173  1.00 57.18           C  
-ANISOU   14  CA  ARG A   3     5991   7188   8549   -107  -1525   1981       C  
-ATOM     15  C   ARG A   3      21.689 -12.952   9.078  1.00 54.95           C  
-ANISOU   15  C   ARG A   3     5835   6771   8272    -91  -1357   1618       C  
-ATOM     16  O   ARG A   3      20.867 -13.734   8.585  1.00 54.27           O  
-ANISOU   16  O   ARG A   3     5721   6371   8530    -18  -1370   1583       O  
-ATOM     17  CB  ARG A   3      22.017 -13.199  11.553  1.00 54.82           C  
-ANISOU   17  CB  ARG A   3     5798   7085   7946   -275  -1510   2338       C  
-ATOM     18  CG  ARG A   3      20.755 -14.030  11.792  1.00 54.28           C  
-ANISOU   18  CG  ARG A   3     5718   6766   8139   -284  -1468   2575       C  
-ATOM     19  CD  ARG A   3      21.063 -15.516  11.680  1.00 62.24           C  
-ANISOU   19  CD  ARG A   3     6498   7425   9728   -146  -1653   2800       C  
-ATOM     20  NE  ARG A   3      19.883 -16.359  11.857  1.00 66.19           N  
-ANISOU   20  NE  ARG A   3     6942   7630  10577   -166  -1638   3050       N  
-ATOM     21  CZ  ARG A   3      18.925 -16.507  10.946  1.00 65.34           C  
-ANISOU   21  CZ  ARG A   3     6854   7229  10744   -139  -1575   2799       C  
-ATOM     22  NH1 ARG A   3      18.997 -15.853   9.791  1.00 61.70           N  
-ANISOU   22  NH1 ARG A   3     6491   6763  10190    -78  -1509   2294       N  
-ATOM     23  NH2 ARG A   3      17.889 -17.302  11.190  1.00 66.44           N  
-ANISOU   23  NH2 ARG A   3     6901   7085  11258   -175  -1588   3075       N  
-ATOM     24  N   SER A   4      21.789 -11.689   8.693  1.00 50.57           N  
-ANISOU   24  N   SER A   4     5408   6441   7364   -162  -1225   1359       N  
-ATOM     25  CA  SER A   4      20.893 -11.170   7.671  1.00 50.99           C  
-ANISOU   25  CA  SER A   4     5584   6402   7389   -149  -1077   1044       C  
-ATOM     26  C   SER A   4      21.570 -10.070   6.858  1.00 49.88           C  
-ANISOU   26  C   SER A   4     5484   6454   7016   -138   -977    752       C  
-ATOM     27  O   SER A   4      21.272  -8.888   7.053  1.00 43.16           O  
-ANISOU   27  O   SER A   4     4768   5789   5841   -281   -866    681       O  
-ATOM     28  CB  SER A   4      19.597 -10.666   8.315  1.00 48.54           C  
-ANISOU   28  CB  SER A   4     5428   6135   6880   -308   -963   1149       C  
-ATOM     29  OG  SER A   4      18.556 -10.565   7.364  1.00 50.34           O  
-ANISOU   29  OG  SER A   4     5723   6177   7228   -275   -876    919       O  
-ATOM     30  N   PRO A   5      22.484 -10.460   5.935  1.00 54.89           N  
-ANISOU   30  N   PRO A   5     5985   7037   7836     43  -1004    591       N  
-ATOM     31  CA  PRO A   5      23.197  -9.503   5.079  1.00 52.90           C  
-ANISOU   31  CA  PRO A   5     5724   6973   7402     76   -886    367       C  
-ATOM     32  C   PRO A   5      22.193  -8.758   4.215  1.00 51.34           C  
-ANISOU   32  C   PRO A   5     5696   6760   7052     54   -737    127       C  
-ATOM     33  O   PRO A   5      21.062  -9.227   4.042  1.00 54.58           O  
-ANISOU   33  O   PRO A   5     6190   6968   7581     70   -750     80       O  
-ATOM     34  CB  PRO A   5      24.098 -10.397   4.215  1.00 53.45           C  
-ANISOU   34  CB  PRO A   5     5612   6940   7757    332   -921    253       C  
-ATOM     35  CG  PRO A   5      23.392 -11.705   4.179  1.00 56.28           C  
-ANISOU   35  CG  PRO A   5     5958   6970   8457    447  -1039    264       C  
-ATOM     36  CD  PRO A   5      22.788 -11.852   5.552  1.00 57.48           C  
-ANISOU   36  CD  PRO A   5     6156   7099   8585    250  -1129    597       C  
-ATOM     37  N   GLY A   6      22.587  -7.614   3.674  1.00 42.12           N  
-ANISOU   37  N   GLY A   6     4555   5789   5658     12   -609      2       N  
-ATOM     38  CA  GLY A   6      21.591  -6.699   3.161  1.00 35.03           C  
-ANISOU   38  CA  GLY A   6     3826   4906   4580    -64   -483   -145       C  
-ATOM     39  C   GLY A   6      21.459  -6.620   1.659  1.00 30.98           C  
-ANISOU   39  C   GLY A   6     3331   4377   4064    110   -386   -393       C  
-ATOM     40  O   GLY A   6      22.131  -7.327   0.913  1.00 30.10           O  
-ANISOU   40  O   GLY A   6     3112   4247   4079    323   -397   -496       O  
-ATOM     41  N   VAL A   7      20.556  -5.746   1.230  1.00 26.95           N  
-ANISOU   41  N   VAL A   7     2962   3884   3393     33   -292   -488       N  
-ATOM     42  CA  VAL A   7      20.394  -5.398  -0.174  1.00 27.17           C  
-ANISOU   42  CA  VAL A   7     3032   3964   3328    173   -194   -691       C  
-ATOM     43  C   VAL A   7      21.639  -4.624  -0.584  1.00 27.34           C  
-ANISOU   43  C   VAL A   7     2938   4232   3217    192    -68   -651       C  
-ATOM     44  O   VAL A   7      21.919  -3.550  -0.038  1.00 28.85           O  
-ANISOU   44  O   VAL A   7     3123   4540   3301      0    -17   -528       O  
-ATOM     45  CB  VAL A   7      19.142  -4.513  -0.360  1.00 25.01           C  
-ANISOU   45  CB  VAL A   7     2918   3656   2930     51   -137   -737       C  
-ATOM     46  CG1 VAL A   7      19.019  -4.013  -1.810  1.00 26.04           C  
-ANISOU   46  CG1 VAL A   7     3094   3886   2913    187    -43   -901       C  
-ATOM     47  CG2 VAL A   7      17.892  -5.277   0.059  1.00 27.68           C  
-ANISOU   47  CG2 VAL A   7     3325   3747   3445     24   -250   -740       C  
-ATOM     48  N   VAL A   8      22.389  -5.164  -1.537  1.00 29.05           N  
-ANISOU   48  N   VAL A   8     3053   4523   3463    431    -19   -757       N  
-ATOM     49  CA  VAL A   8      23.618  -4.519  -1.977  1.00 34.59           C  
-ANISOU   49  CA  VAL A   8     3596   5469   4078    472    129   -677       C  
-ATOM     50  C   VAL A   8      23.278  -3.426  -2.989  1.00 36.07           C  
-ANISOU   50  C   VAL A   8     3859   5806   4038    471    295   -716       C  
-ATOM     51  O   VAL A   8      22.765  -3.710  -4.068  1.00 33.00           O  
-ANISOU   51  O   VAL A   8     3564   5433   3542    663    336   -895       O  
-ATOM     52  CB  VAL A   8      24.608  -5.530  -2.605  1.00 39.10           C  
-ANISOU   52  CB  VAL A   8     4002   6089   4764    762    159   -761       C  
-ATOM     53  CG1 VAL A   8      25.800  -4.806  -3.208  1.00 42.06           C  
-ANISOU   53  CG1 VAL A   8     4189   6744   5049    822    361   -654       C  
-ATOM     54  CG2 VAL A   8      25.089  -6.547  -1.562  1.00 37.62           C  
-ANISOU   54  CG2 VAL A   8     3699   5750   4846    756    -14   -663       C  
-ATOM     55  N   ILE A   9      23.552  -2.175  -2.636  1.00 31.74           N  
-ANISOU   55  N   ILE A   9     3272   5361   3428    256    366   -548       N  
-ATOM     56  CA  ILE A   9      23.335  -1.068  -3.561  1.00 32.85           C  
-ANISOU   56  CA  ILE A   9     3446   5636   3397    242    526   -517       C  
-ATOM     57  C   ILE A   9      24.676  -0.718  -4.215  1.00 37.50           C  
-ANISOU   57  C   ILE A   9     3805   6470   3973    341    701   -376       C  
-ATOM     58  O   ILE A   9      25.654  -0.412  -3.534  1.00 31.73           O  
-ANISOU   58  O   ILE A   9     2888   5781   3386    213    686   -209       O  
-ATOM     59  CB  ILE A   9      22.681   0.131  -2.840  1.00 34.84           C  
-ANISOU   59  CB  ILE A   9     3794   5801   3643    -46    495   -427       C  
-ATOM     60  CG1 ILE A   9      21.286  -0.280  -2.352  1.00 33.10           C  
-ANISOU   60  CG1 ILE A   9     3779   5368   3429    -96    373   -555       C  
-ATOM     61  CG2 ILE A   9      22.611   1.351  -3.752  1.00 37.59           C  
-ANISOU   61  CG2 ILE A   9     4132   6269   3880    -76    653   -333       C  
-ATOM     62  CD1 ILE A   9      20.430   0.848  -1.871  1.00 37.12           C  
-ANISOU   62  CD1 ILE A   9     4402   5790   3911   -311    379   -518       C  
-ATOM     63  N   SER A  10      24.742  -0.800  -5.541  1.00 32.59           N  
-ANISOU   63  N   SER A  10     3181   6026   3177    583    865   -436       N  
-ATOM     64  CA  SER A  10      26.027  -0.667  -6.224  1.00 38.67           C  
-ANISOU   64  CA  SER A  10     3708   7058   3928    735   1074   -293       C  
-ATOM     65  C   SER A  10      26.538   0.770  -6.236  1.00 35.77           C  
-ANISOU   65  C   SER A  10     3187   6808   3596    523   1203      6       C  
-ATOM     66  O   SER A  10      25.772   1.707  -6.025  1.00 35.31           O  
-ANISOU   66  O   SER A  10     3252   6646   3517    312   1156     59       O  
-ATOM     67  CB  SER A  10      25.930  -1.189  -7.660  1.00 47.07           C  
-ANISOU   67  CB  SER A  10     4831   8321   4733   1091   1230   -455       C  
-ATOM     68  OG  SER A  10      24.866  -0.538  -8.324  1.00 52.65           O  
-ANISOU   68  OG  SER A  10     5740   9050   5216   1066   1244   -489       O  
-ATOM     69  N   ASP A  11      27.833   0.927  -6.510  1.00 38.36           N  
-ANISOU   69  N   ASP A  11     3224   7334   4016    588   1367    208       N  
-ATOM     70  CA  ASP A  11      28.466   2.236  -6.557  1.00 42.68           C  
-ANISOU   70  CA  ASP A  11     3562   7974   4679    388   1485    531       C  
-ATOM     71  C   ASP A  11      27.835   3.139  -7.623  1.00 46.68           C  
-ANISOU   71  C   ASP A  11     4166   8605   4966    417   1657    637       C  
-ATOM     72  O   ASP A  11      27.788   4.357  -7.464  1.00 50.77           O  
-ANISOU   72  O   ASP A  11     4635   9041   5613    171   1653    849       O  
-ATOM     73  CB  ASP A  11      29.966   2.100  -6.838  1.00 43.26           C  
-ANISOU   73  CB  ASP A  11     3267   8264   4906    505   1663    748       C  
-ATOM     74  CG  ASP A  11      30.751   1.550  -5.652  1.00 45.72           C  
-ANISOU   74  CG  ASP A  11     3413   8444   5515    397   1460    749       C  
-ATOM     75  OD1 ASP A  11      30.200   1.504  -4.533  1.00 45.38           O  
-ANISOU   75  OD1 ASP A  11     3534   8161   5549    183   1188    632       O  
-ATOM     76  OD2 ASP A  11      31.937   1.187  -5.848  1.00 48.95           O  
-ANISOU   76  OD2 ASP A  11     3514   9010   6076    535   1583    888       O  
-ATOM     77  N   ASP A  12      27.345   2.536  -8.703  1.00 46.50           N  
-ANISOU   77  N   ASP A  12     4347   8653   4670    695   1715    460       N  
-ATOM     78  CA AASP A  12      26.799   3.335  -9.800  0.59 46.31           C  
-ANISOU   78  CA AASP A  12     4472   8657   4468    719   1786    557       C  
-ATOM     79  CA BASP A  12      26.795   3.266  -9.842  0.41 46.48           C  
-ANISOU   79  CA BASP A  12     4501   8684   4477    737   1787    543       C  
-ATOM     80  C   ASP A  12      25.283   3.452  -9.763  1.00 45.82           C  
-ANISOU   80  C   ASP A  12     4691   8452   4264    662   1641    380       C  
-ATOM     81  O   ASP A  12      24.665   3.874 -10.736  1.00 50.19           O  
-ANISOU   81  O   ASP A  12     5389   9037   4643    730   1661    409       O  
-ATOM     82  CB AASP A  12      27.258   2.810 -11.159  0.59 49.62           C  
-ANISOU   82  CB AASP A  12     4917   9270   4667   1029   1925    524       C  
-ATOM     83  CB BASP A  12      27.121   2.528 -11.140  0.41 49.33           C  
-ANISOU   83  CB BASP A  12     4922   9222   4601   1070   1898    443       C  
-ATOM     84  CG AASP A  12      26.948   1.342 -11.359  0.59 50.57           C  
-ANISOU   84  CG AASP A  12     5190   9385   4640   1295   1840    155       C  
-ATOM     85  CG BASP A  12      28.592   2.194 -11.270  0.41 54.02           C  
-ANISOU   85  CG BASP A  12     5247   9965   5312   1186   2059    574       C  
-ATOM     86  OD1AASP A  12      26.046   0.807 -10.682  0.59 47.79           O  
-ANISOU   86  OD1AASP A  12     4990   8864   4306   1254   1655    -83       O  
-ATOM     87  OD1BASP A  12      29.433   3.056 -10.933  0.41 54.05           O  
-ANISOU   87  OD1BASP A  12     5007   9982   5548   1003   2139    881       O  
-ATOM     88  OD2AASP A  12      27.615   0.715 -12.210  0.59 58.64           O  
-ANISOU   88  OD2AASP A  12     6174  10562   5545   1549   1954     98       O  
-ATOM     89  OD2BASP A  12      28.912   1.067 -11.713  0.41 59.24           O  
-ANISOU   89  OD2BASP A  12     5935  10708   5866   1460   2093    363       O  
-ATOM     90  N   GLU A  13      24.691   3.100  -8.626  1.00 40.11           N  
-ANISOU   90  N   GLU A  13     4028   7589   3625    529   1491    213       N  
-ATOM     91  CA  GLU A  13      23.244   3.239  -8.440  1.00 41.06           C  
-ANISOU   91  CA  GLU A  13     4409   7505   3688    437   1326     52       C  
-ATOM     92  C   GLU A  13      22.844   4.690  -8.662  1.00 39.88           C  
-ANISOU   92  C   GLU A  13     4253   7334   3565    247   1389    294       C  
-ATOM     93  O   GLU A  13      23.339   5.580  -7.977  1.00 40.63           O  
-ANISOU   93  O   GLU A  13     4204   7331   3903      3   1393    487       O  
-ATOM     94  CB  GLU A  13      22.828   2.795  -7.038  1.00 44.57           C  
-ANISOU   94  CB  GLU A  13     4936   7648   4349    249   1100   -106       C  
-ATOM     95  CG  GLU A  13      21.370   3.106  -6.688  1.00 47.84           C  
-ANISOU   95  CG  GLU A  13     5572   7833   4771    115    959   -217       C  
-ATOM     96  CD  GLU A  13      20.377   2.332  -7.537  1.00 53.92           C  
-ANISOU   96  CD  GLU A  13     6526   8607   5357    334    893   -434       C  
-ATOM     97  OE1 GLU A  13      20.623   1.134  -7.792  1.00 60.41           O  
-ANISOU   97  OE1 GLU A  13     7358   9466   6130    546    848   -620       O  
-ATOM     98  OE2 GLU A  13      19.357   2.928  -7.949  1.00 52.41           O  
-ANISOU   98  OE2 GLU A  13     6457   8361   5097    296    865   -426       O  
-ATOM     99  N   PRO A  14      21.965   4.937  -9.647  1.00 44.06           N  
-ANISOU   99  N   PRO A  14     4951   7876   3913    354   1382    277       N  
-ATOM    100  CA  PRO A  14      21.609   6.314 -10.006  1.00 43.53           C  
-ANISOU  100  CA  PRO A  14     4867   7775   3900    207   1438    537       C  
-ATOM    101  C   PRO A  14      20.482   6.857  -9.142  1.00 42.19           C  
-ANISOU  101  C   PRO A  14     4809   7357   3865    -19   1306    471       C  
-ATOM    102  O   PRO A  14      20.275   8.066  -9.107  1.00 47.99           O  
-ANISOU  102  O   PRO A  14     5493   7990   4750   -194   1335    682       O  
-ATOM    103  CB  PRO A  14      21.139   6.180 -11.458  1.00 45.41           C  
-ANISOU  103  CB  PRO A  14     5239   8147   3869    443   1452    524       C  
-ATOM    104  CG  PRO A  14      20.558   4.804 -11.523  1.00 50.07           C  
-ANISOU  104  CG  PRO A  14     6006   8707   4311    629   1304    158       C  
-ATOM    105  CD  PRO A  14      21.376   3.951 -10.571  1.00 48.12           C  
-ANISOU  105  CD  PRO A  14     5654   8431   4198    621   1302     33       C  
-ATOM    106  N   GLY A  15      19.771   5.977  -8.448  1.00 38.82           N  
-ANISOU  106  N   GLY A  15     4539   6747   3462    -17   1131    175       N  
-ATOM    107  CA  GLY A  15      18.619   6.393  -7.673  1.00 32.91           C  
-ANISOU  107  CA  GLY A  15     3924   5709   2873   -199    992     83       C  
-ATOM    108  C   GLY A  15      17.504   6.859  -8.594  1.00 36.41           C  
-ANISOU  108  C   GLY A  15     4482   6154   3200   -128    976    121       C  
-ATOM    109  O   GLY A  15      17.548   6.621  -9.808  1.00 41.10           O  
-ANISOU  109  O   GLY A  15     5095   6987   3534     87   1032    163       O  
-ATOM    110  N   TYR A  16      16.521   7.542  -8.017  1.00 32.48           N  
-ANISOU  110  N   TYR A  16     4053   5403   2884   -294    898    110       N  
-ATOM    111  CA  TYR A  16      15.303   7.914  -8.729  1.00 32.38           C  
-ANISOU  111  CA  TYR A  16     4143   5339   2822   -239    838    130       C  
-ATOM    112  C   TYR A  16      15.120   9.430  -8.774  1.00 35.84           C  
-ANISOU  112  C   TYR A  16     4508   5664   3447   -398    905    385       C  
-ATOM    113  O   TYR A  16      15.432  10.140  -7.804  1.00 33.88           O  
-ANISOU  113  O   TYR A  16     4191   5229   3453   -602    927    417       O  
-ATOM    114  CB  TYR A  16      14.085   7.271  -8.047  1.00 31.78           C  
-ANISOU  114  CB  TYR A  16     4197   5027   2852   -265    678   -115       C  
-ATOM    115  CG  TYR A  16      14.138   5.758  -7.960  1.00 32.53           C  
-ANISOU  115  CG  TYR A  16     4352   5161   2848   -124    578   -354       C  
-ATOM    116  CD1 TYR A  16      13.722   4.962  -9.027  1.00 41.14           C  
-ANISOU  116  CD1 TYR A  16     5523   6369   3738     98    476   -480       C  
-ATOM    117  CD2 TYR A  16      14.610   5.127  -6.811  1.00 33.82           C  
-ANISOU  117  CD2 TYR A  16     4490   5231   3127   -207    563   -457       C  
-ATOM    118  CE1 TYR A  16      13.778   3.581  -8.947  1.00 41.90           C  
-ANISOU  118  CE1 TYR A  16     5663   6448   3807    229    362   -718       C  
-ATOM    119  CE2 TYR A  16      14.662   3.754  -6.720  1.00 32.38           C  
-ANISOU  119  CE2 TYR A  16     4341   5046   2914    -82    463   -643       C  
-ATOM    120  CZ  TYR A  16      14.243   2.989  -7.778  1.00 36.73           C  
-ANISOU  120  CZ  TYR A  16     4962   5671   3323    132    362   -781       C  
-ATOM    121  OH  TYR A  16      14.308   1.622  -7.681  1.00 37.92           O  
-ANISOU  121  OH  TYR A  16     5136   5769   3503    257    242   -985       O  
-ATOM    122  N   ASP A  17      14.609   9.907  -9.907  1.00 32.85           N  
-ANISOU  122  N   ASP A  17     4146   5391   2944   -295    914    556       N  
-ATOM    123  CA  ASP A  17      14.235  11.302 -10.094  1.00 34.06           C  
-ANISOU  123  CA  ASP A  17     4231   5407   3302   -418    951    820       C  
-ATOM    124  C   ASP A  17      13.229  11.695  -9.022  1.00 30.20           C  
-ANISOU  124  C   ASP A  17     3801   4552   3121   -579    857    659       C  
-ATOM    125  O   ASP A  17      12.251  10.978  -8.789  1.00 28.08           O  
-ANISOU  125  O   ASP A  17     3649   4195   2826   -521    742    436       O  
-ATOM    126  CB  ASP A  17      13.615  11.474 -11.486  1.00 38.85           C  
-ANISOU  126  CB  ASP A  17     4883   6204   3675   -241    925    995       C  
-ATOM    127  CG  ASP A  17      13.383  12.926 -11.860  1.00 47.28           C  
-ANISOU  127  CG  ASP A  17     5847   7165   4954   -345    977   1354       C  
-ATOM    128  OD1 ASP A  17      13.072  13.749 -10.975  1.00 45.32           O  
-ANISOU  128  OD1 ASP A  17     5551   6579   5089   -544    959   1352       O  
-ATOM    129  OD2 ASP A  17      13.506  13.245 -13.057  1.00 59.31           O  
-ANISOU  129  OD2 ASP A  17     7336   8945   6254   -213   1033   1643       O  
-ATOM    130  N   LEU A  18      13.469  12.831  -8.364  1.00 32.50           N  
-ANISOU  130  N   LEU A  18     4000   4625   3724   -773    906    768       N  
-ATOM    131  CA  LEU A  18      12.600  13.270  -7.269  1.00 33.00           C  
-ANISOU  131  CA  LEU A  18     4118   4355   4064   -904    848    587       C  
-ATOM    132  C   LEU A  18      11.183  13.484  -7.768  1.00 27.01           C  
-ANISOU  132  C   LEU A  18     3419   3482   3360   -827    779    607       C  
-ATOM    133  O   LEU A  18      10.229  13.322  -7.016  1.00 30.63           O  
-ANISOU  133  O   LEU A  18     3946   3742   3950   -852    732    406       O  
-ATOM    134  CB  LEU A  18      13.113  14.581  -6.670  1.00 30.87           C  
-ANISOU  134  CB  LEU A  18     3737   3860   4132  -1100    891    693       C  
-ATOM    135  CG  LEU A  18      14.514  14.565  -6.077  1.00 35.64           C  
-ANISOU  135  CG  LEU A  18     4246   4524   4770  -1216    921    686       C  
-ATOM    136  CD1 LEU A  18      15.013  15.989  -5.841  1.00 41.06           C  
-ANISOU  136  CD1 LEU A  18     4786   4976   5837  -1401    929    855       C  
-ATOM    137  CD2 LEU A  18      14.493  13.779  -4.783  1.00 35.34           C  
-ANISOU  137  CD2 LEU A  18     4320   4436   4673  -1258    860    348       C  
-ATOM    138  N   ASP A  19      11.055  13.859  -9.047  1.00 28.84           N  
-ANISOU  138  N   ASP A  19     3611   3858   3490   -725    775    875       N  
-ATOM    139  CA  ASP A  19       9.756  14.207  -9.621  1.00 32.50           C  
-ANISOU  139  CA  ASP A  19     4102   4215   4032   -656    681    951       C  
-ATOM    140  C   ASP A  19       8.797  13.029  -9.743  1.00 30.19           C  
-ANISOU  140  C   ASP A  19     3926   3971   3574   -524    541    713       C  
-ATOM    141  O   ASP A  19       7.603  13.222 -10.008  1.00 30.01           O  
-ANISOU  141  O   ASP A  19     3911   3815   3675   -484    434    730       O  
-ATOM    142  CB  ASP A  19       9.930  14.889 -10.978  1.00 39.01           C  
-ANISOU  142  CB  ASP A  19     4854   5223   4746   -572    697   1336       C  
-ATOM    143  CG  ASP A  19      10.532  16.282 -10.858  1.00 49.12           C  
-ANISOU  143  CG  ASP A  19     5977   6336   6349   -729    806   1632       C  
-ATOM    144  OD1 ASP A  19      10.018  17.078 -10.041  1.00 50.40           O  
-ANISOU  144  OD1 ASP A  19     6106   6135   6910   -862    791   1563       O  
-ATOM    145  OD2 ASP A  19      11.520  16.573 -11.573  1.00 55.44           O  
-ANISOU  145  OD2 ASP A  19     6677   7362   7028   -711    908   1932       O  
-ATOM    146  N   LEU A  20       9.324  11.825  -9.529  1.00 27.04           N  
-ANISOU  146  N   LEU A  20     3593   3732   2947   -464    527    503       N  
-ATOM    147  CA  LEU A  20       8.550  10.584  -9.604  1.00 26.86           C  
-ANISOU  147  CA  LEU A  20     3663   3728   2814   -349    374    266       C  
-ATOM    148  C   LEU A  20       7.935  10.219  -8.244  1.00 28.66           C  
-ANISOU  148  C   LEU A  20     3904   3696   3290   -459    374     50       C  
-ATOM    149  O   LEU A  20       7.099   9.313  -8.139  1.00 27.12           O  
-ANISOU  149  O   LEU A  20     3745   3434   3125   -401    251   -107       O  
-ATOM    150  CB  LEU A  20       9.434   9.429 -10.124  1.00 29.63           C  
-ANISOU  150  CB  LEU A  20     4069   4366   2823   -204    353    152       C  
-ATOM    151  CG  LEU A  20       9.982   9.537 -11.553  1.00 36.15           C  
-ANISOU  151  CG  LEU A  20     4903   5526   3305    -31    365    328       C  
-ATOM    152  CD1 LEU A  20      11.024   8.458 -11.827  1.00 41.31           C  
-ANISOU  152  CD1 LEU A  20     5592   6441   3664    113    403    181       C  
-ATOM    153  CD2 LEU A  20       8.869   9.441 -12.572  1.00 38.36           C  
-ANISOU  153  CD2 LEU A  20     5251   5854   3469    109    167    339       C  
-ATOM    154  N   PHE A  21       8.340  10.941  -7.208  1.00 24.46           N  
-ANISOU  154  N   PHE A  21     3335   3020   2941   -612    508     52       N  
-ATOM    155  CA  PHE A  21       7.842  10.688  -5.860  1.00 25.87           C  
-ANISOU  155  CA  PHE A  21     3534   3004   3293   -701    546   -135       C  
-ATOM    156  C   PHE A  21       7.221  11.897  -5.182  1.00 26.99           C  
-ANISOU  156  C   PHE A  21     3637   2890   3729   -802    632   -114       C  
-ATOM    157  O   PHE A  21       7.301  13.019  -5.676  1.00 25.61           O  
-ANISOU  157  O   PHE A  21     3405   2646   3679   -832    656     55       O  
-ATOM    158  CB  PHE A  21       8.963  10.109  -4.996  1.00 29.32           C  
-ANISOU  158  CB  PHE A  21     3996   3537   3608   -761    603   -249       C  
-ATOM    159  CG  PHE A  21       9.461   8.803  -5.504  1.00 33.97           C  
-ANISOU  159  CG  PHE A  21     4615   4327   3965   -643    522   -312       C  
-ATOM    160  CD1 PHE A  21       8.820   7.625  -5.149  1.00 38.92           C  
-ANISOU  160  CD1 PHE A  21     5278   4902   4606   -590    434   -460       C  
-ATOM    161  CD2 PHE A  21      10.528   8.746  -6.388  1.00 33.27           C  
-ANISOU  161  CD2 PHE A  21     4502   4468   3670   -570    538   -215       C  
-ATOM    162  CE1 PHE A  21       9.251   6.403  -5.648  1.00 39.47           C  
-ANISOU  162  CE1 PHE A  21     5374   5112   4512   -467    335   -546       C  
-ATOM    163  CE2 PHE A  21      10.961   7.529  -6.893  1.00 38.63           C  
-ANISOU  163  CE2 PHE A  21     5212   5324   4140   -425    469   -313       C  
-ATOM    164  CZ  PHE A  21      10.324   6.357  -6.521  1.00 43.53           C  
-ANISOU  164  CZ  PHE A  21     5882   5856   4801   -374    353   -497       C  
-ATOM    165  N   CYS A  22       6.576  11.632  -4.050  1.00 28.80           N  
-ANISOU  165  N   CYS A  22     3889   2979   4076   -839    684   -279       N  
-ATOM    166  CA  CYS A  22       6.040  12.666  -3.185  1.00 30.99           C  
-ANISOU  166  CA  CYS A  22     4147   3026   4604   -909    794   -336       C  
-ATOM    167  C   CYS A  22       7.160  13.096  -2.248  1.00 31.10           C  
-ANISOU  167  C   CYS A  22     4202   3050   4566  -1024    867   -441       C  
-ATOM    168  O   CYS A  22       7.619  12.298  -1.427  1.00 34.81           O  
-ANISOU  168  O   CYS A  22     4731   3629   4867  -1047    882   -571       O  
-ATOM    169  CB  CYS A  22       4.877  12.111  -2.392  1.00 31.59           C  
-ANISOU  169  CB  CYS A  22     4222   3000   4783   -871    844   -455       C  
-ATOM    170  N   ILE A  23       7.601  14.343  -2.392  1.00 27.70           N  
-ANISOU  170  N   ILE A  23     3726   2493   4304  -1099    887   -370       N  
-ATOM    171  CA  ILE A  23       8.719  14.909  -1.633  1.00 32.34           C  
-ANISOU  171  CA  ILE A  23     4327   3055   4906  -1225    903   -462       C  
-ATOM    172  C   ILE A  23       8.238  16.171  -0.914  1.00 35.70           C  
-ANISOU  172  C   ILE A  23     4746   3214   5606  -1248    936   -579       C  
-ATOM    173  O   ILE A  23       7.518  16.975  -1.510  1.00 43.40           O  
-ANISOU  173  O   ILE A  23     5650   4026   6814  -1199    931   -455       O  
-ATOM    174  CB  ILE A  23       9.861  15.292  -2.599  1.00 36.18           C  
-ANISOU  174  CB  ILE A  23     4721   3643   5384  -1275    855   -227       C  
-ATOM    175  CG1 ILE A  23      10.357  14.059  -3.357  1.00 39.08           C  
-ANISOU  175  CG1 ILE A  23     5093   4316   5441  -1184    820   -133       C  
-ATOM    176  CG2 ILE A  23      11.005  15.953  -1.869  1.00 41.27           C  
-ANISOU  176  CG2 ILE A  23     5336   4219   6127  -1426    836   -298       C  
-ATOM    177  CD1 ILE A  23      10.915  12.981  -2.448  1.00 39.84           C  
-ANISOU  177  CD1 ILE A  23     5258   4552   5327  -1196    807   -319       C  
-ATOM    178  N   PRO A  24       8.642  16.369   0.359  1.00 37.87           N  
-ANISOU  178  N   PRO A  24     5087   3484   5817  -1276    933   -806       N  
-ATOM    179  CA  PRO A  24       8.285  17.639   1.015  1.00 41.16           C  
-ANISOU  179  CA  PRO A  24     5498   3685   6458  -1254    929   -934       C  
-ATOM    180  C   PRO A  24       8.841  18.851   0.262  1.00 41.55           C  
-ANISOU  180  C   PRO A  24     5438   3562   6787  -1324    831   -754       C  
-ATOM    181  O   PRO A  24      10.022  18.859  -0.110  1.00 37.51           O  
-ANISOU  181  O   PRO A  24     4873   3118   6259  -1435    756   -630       O  
-ATOM    182  CB  PRO A  24       8.939  17.520   2.399  1.00 42.30           C  
-ANISOU  182  CB  PRO A  24     5745   3906   6423  -1296    908  -1194       C  
-ATOM    183  CG  PRO A  24       9.990  16.453   2.245  1.00 40.80           C  
-ANISOU  183  CG  PRO A  24     5568   3945   5988  -1377    857  -1128       C  
-ATOM    184  CD  PRO A  24       9.435  15.494   1.241  1.00 34.59           C  
-ANISOU  184  CD  PRO A  24     4757   3258   5128  -1327    920   -953       C  
-ATOM    185  N   ASN A  25       7.995  19.863   0.060  1.00 50.72           N  
-ANISOU  185  N   ASN A  25     9844   4248   5180    740   -103    514       N  
-ATOM    186  CA  ASN A  25       8.343  21.058  -0.700  1.00 56.54           C  
-ANISOU  186  CA  ASN A  25    10832   4687   5963    691    -73    757       C  
-ATOM    187  C   ASN A  25       9.607  21.746  -0.213  1.00 56.00           C  
-ANISOU  187  C   ASN A  25    10920   4332   6025    220      1    750       C  
-ATOM    188  O   ASN A  25      10.417  22.210  -1.015  1.00 51.94           O  
-ANISOU  188  O   ASN A  25    10441   3741   5554     -3    101    979       O  
-ATOM    189  CB  ASN A  25       7.192  22.065  -0.651  1.00 66.10           C  
-ANISOU  189  CB  ASN A  25    12196   5640   7281   1070   -101    711       C  
-ATOM    190  CG  ASN A  25       6.743  22.503  -2.027  1.00 75.99           C  
-ANISOU  190  CG  ASN A  25    13479   6938   8455   1350   -161    986       C  
-ATOM    191  OD1 ASN A  25       6.071  21.750  -2.734  1.00 77.48           O  
-ANISOU  191  OD1 ASN A  25    13454   7471   8514   1641   -281    998       O  
-ATOM    192  ND2 ASN A  25       7.098  23.730  -2.415  1.00 84.14           N  
-ANISOU  192  ND2 ASN A  25    14784   7620   9566   1271    -88   1191       N  
-ATOM    193  N   HIS A  26       9.767  21.810   1.107  1.00 53.49           N  
-ANISOU  193  N   HIS A  26    10672   3872   5778     73    -41    451       N  
-ATOM    194  CA  HIS A  26      10.884  22.539   1.698  1.00 51.75           C  
-ANISOU  194  CA  HIS A  26    10553   3384   5725   -353    -40    337       C  
-ATOM    195  C   HIS A  26      12.248  21.890   1.429  1.00 48.55           C  
-ANISOU  195  C   HIS A  26     9952   3142   5352   -790    -56    398       C  
-ATOM    196  O   HIS A  26      13.282  22.476   1.727  1.00 51.15           O  
-ANISOU  196  O   HIS A  26    10262   3278   5895  -1176    -58    295       O  
-ATOM    197  CB  HIS A  26      10.654  22.806   3.202  1.00 52.50           C  
-ANISOU  197  CB  HIS A  26    10742   3379   5827   -350   -126    -51       C  
-ATOM    198  CG  HIS A  26      10.406  21.576   4.025  1.00 52.69           C  
-ANISOU  198  CG  HIS A  26    10641   3748   5632   -263   -206   -252       C  
-ATOM    199  ND1 HIS A  26       9.152  21.022   4.188  1.00 48.64           N  
-ANISOU  199  ND1 HIS A  26    10064   3413   5004    123   -121   -299       N  
-ATOM    200  CD2 HIS A  26      11.250  20.810   4.760  1.00 51.50           C  
-ANISOU  200  CD2 HIS A  26    10381   3813   5374   -502   -354   -423       C  
-ATOM    201  CE1 HIS A  26       9.240  19.956   4.963  1.00 47.01           C  
-ANISOU  201  CE1 HIS A  26     9736   3504   4620     96   -148   -448       C  
-ATOM    202  NE2 HIS A  26      10.500  19.806   5.326  1.00 47.48           N  
-ANISOU  202  NE2 HIS A  26     9787   3604   4649   -249   -317   -512       N  
-ATOM    203  N   TYR A  27      12.242  20.692   0.845  1.00 44.81           N  
-ANISOU  203  N   TYR A  27     9175   3132   4719   -703    -60    516       N  
-ATOM    204  CA  TYR A  27      13.478  19.983   0.501  1.00 44.35           C  
-ANISOU  204  CA  TYR A  27     8768   3367   4718  -1043    -51    550       C  
-ATOM    205  C   TYR A  27      13.623  19.748  -1.005  1.00 46.60           C  
-ANISOU  205  C   TYR A  27     8969   3821   4916  -1014    144    891       C  
-ATOM    206  O   TYR A  27      14.556  19.076  -1.435  1.00 47.45           O  
-ANISOU  206  O   TYR A  27     8757   4208   5064  -1247    210    918       O  
-ATOM    207  CB  TYR A  27      13.557  18.630   1.219  1.00 41.46           C  
-ANISOU  207  CB  TYR A  27     8068   3445   4239   -982   -218    341       C  
-ATOM    208  CG  TYR A  27      13.776  18.693   2.718  1.00 38.89           C  
-ANISOU  208  CG  TYR A  27     7828   3036   3911  -1065   -426     13       C  
-ATOM    209  CD1 TYR A  27      14.600  19.655   3.284  1.00 41.25           C  
-ANISOU  209  CD1 TYR A  27     8257   3013   4401  -1390   -525   -167       C  
-ATOM    210  CD2 TYR A  27      13.163  17.775   3.560  1.00 36.36           C  
-ANISOU  210  CD2 TYR A  27     7481   2952   3381   -822   -510   -129       C  
-ATOM    211  CE1 TYR A  27      14.800  19.707   4.658  1.00 45.08           C  
-ANISOU  211  CE1 TYR A  27     8859   3461   4809  -1432   -773   -510       C  
-ATOM    212  CE2 TYR A  27      13.353  17.815   4.931  1.00 35.32           C  
-ANISOU  212  CE2 TYR A  27     7519   2766   3135   -855   -693   -405       C  
-ATOM    213  CZ  TYR A  27      14.170  18.780   5.475  1.00 38.69           C  
-ANISOU  213  CZ  TYR A  27     8088   2920   3692  -1141   -859   -609       C  
-ATOM    214  OH  TYR A  27      14.359  18.817   6.842  1.00 40.74           O  
-ANISOU  214  OH  TYR A  27     8463   3220   3798  -1106  -1064   -881       O  
-ATOM    215  N   ALA A  28      12.706  20.294  -1.799  1.00 48.00           N  
-ANISOU  215  N   ALA A  28     9413   3862   4961   -689    221   1120       N  
-ATOM    216  CA  ALA A  28      12.686  20.044  -3.245  1.00 52.74           C  
-ANISOU  216  CA  ALA A  28     9900   4740   5401   -547    351   1377       C  
-ATOM    217  C   ALA A  28      14.002  20.387  -3.950  1.00 57.49           C  
-ANISOU  217  C   ALA A  28    10447   5277   6118   -947    614   1556       C  
-ATOM    218  O   ALA A  28      14.413  19.696  -4.885  1.00 58.65           O  
-ANISOU  218  O   ALA A  28    10390   5766   6128   -968    743   1672       O  
-ATOM    219  CB  ALA A  28      11.529  20.784  -3.901  1.00 54.14           C  
-ANISOU  219  CB  ALA A  28    10290   4806   5477   -111    309   1515       C  
-ATOM    220  N   GLU A  29      14.649  21.463  -3.509  1.00 60.50           N  
-ANISOU  220  N   GLU A  29    10979   5222   6786  -1263    719   1538       N  
-ATOM    221  CA  GLU A  29      15.904  21.903  -4.115  1.00 64.79           C  
-ANISOU  221  CA  GLU A  29    11421   5652   7543  -1673   1020   1673       C  
-ATOM    222  C   GLU A  29      17.134  21.314  -3.429  1.00 62.88           C  
-ANISOU  222  C   GLU A  29    10798   5512   7581  -2163   1012   1409       C  
-ATOM    223  O   GLU A  29      18.222  21.295  -4.006  1.00 64.62           O  
-ANISOU  223  O   GLU A  29    10760   5796   7998  -2487   1274   1466       O  
-ATOM    224  CB  GLU A  29      16.002  23.424  -4.078  1.00 74.42           C  
-ANISOU  224  CB  GLU A  29    12929   6333   9015  -1778   1152   1769       C  
-ATOM    225  CG  GLU A  29      15.484  24.054  -2.788  1.00 84.40           C  
-ANISOU  225  CG  GLU A  29    14368   7257  10445  -1734    918   1491       C  
-ATOM    226  CD  GLU A  29      16.045  25.446  -2.548  1.00100.40           C  
-ANISOU  226  CD  GLU A  29    16537   8744  12866  -2021   1063   1471       C  
-ATOM    227  OE1 GLU A  29      15.390  26.245  -1.839  1.00104.96           O  
-ANISOU  227  OE1 GLU A  29    17356   8991  13533  -1864    934   1333       O  
-ATOM    228  OE2 GLU A  29      17.147  25.738  -3.061  1.00108.34           O  
-ANISOU  228  OE2 GLU A  29    17385   9656  14123  -2409   1322   1573       O  
-ATOM    229  N   ASP A  30      16.956  20.840  -2.199  1.00 54.78           N  
-ANISOU  229  N   ASP A  30     9713   4516   6584  -2196    692   1100       N  
-ATOM    230  CA  ASP A  30      18.080  20.418  -1.370  1.00 52.43           C  
-ANISOU  230  CA  ASP A  30     8983   4350   6588  -2572    529    755       C  
-ATOM    231  C   ASP A  30      18.491  18.971  -1.604  1.00 50.31           C  
-ANISOU  231  C   ASP A  30     8219   4666   6230  -2494    459    689       C  
-ATOM    232  O   ASP A  30      19.574  18.556  -1.191  1.00 52.21           O  
-ANISOU  232  O   ASP A  30     8017   5071   6751  -2768    350    446       O  
-ATOM    233  CB  ASP A  30      17.748  20.632   0.110  1.00 52.79           C  
-ANISOU  233  CB  ASP A  30     9132   4261   6665  -2501    147    395       C  
-ATOM    234  CG  ASP A  30      17.343  22.060   0.409  1.00 58.61           C  
-ANISOU  234  CG  ASP A  30    10305   4433   7530  -2524    210    385       C  
-ATOM    235  OD1 ASP A  30      17.810  22.962  -0.312  1.00 59.76           O  
-ANISOU  235  OD1 ASP A  30    10468   4321   7915  -2697    501    566       O  
-ATOM    236  OD2 ASP A  30      16.559  22.276   1.359  1.00 60.73           O  
-ANISOU  236  OD2 ASP A  30    10819   4587   7671  -2287     -9    186       O  
-ATOM    237  N   LEU A  31      17.619  18.201  -2.248  1.00 41.71           N  
-ANISOU  237  N   LEU A  31     7183   3877   4788  -2101    492    867       N  
-ATOM    238  CA  LEU A  31      17.910  16.806  -2.545  1.00 38.73           C  
-ANISOU  238  CA  LEU A  31     6377   4002   4335  -1997    456    798       C  
-ATOM    239  C   LEU A  31      18.245  16.648  -4.019  1.00 44.86           C  
-ANISOU  239  C   LEU A  31     7102   4937   5005  -2050    837   1052       C  
-ATOM    240  O   LEU A  31      17.827  17.456  -4.851  1.00 47.71           O  
-ANISOU  240  O   LEU A  31     7866   5076   5184  -1999   1076   1347       O  
-ATOM    241  CB  LEU A  31      16.720  15.916  -2.178  1.00 35.22           C  
-ANISOU  241  CB  LEU A  31     5980   3790   3612  -1550    236    736       C  
-ATOM    242  CG  LEU A  31      16.263  16.041  -0.723  1.00 34.22           C  
-ANISOU  242  CG  LEU A  31     5990   3516   3496  -1455    -61    511       C  
-ATOM    243  CD1 LEU A  31      15.022  15.201  -0.434  1.00 33.99           C  
-ANISOU  243  CD1 LEU A  31     6010   3670   3234  -1050   -151    472       C  
-ATOM    244  CD2 LEU A  31      17.396  15.670   0.217  1.00 35.88           C  
-ANISOU  244  CD2 LEU A  31     5897   3812   3922  -1693   -288    256       C  
-ATOM    245  N   GLU A  32      19.013  15.614  -4.343  1.00 44.74           N  
-ANISOU  245  N   GLU A  32     6625   5293   5079  -2125    903    941       N  
-ATOM    246  CA  GLU A  32      19.406  15.393  -5.727  1.00 44.28           C  
-ANISOU  246  CA  GLU A  32     6513   5423   4887  -2180   1310   1133       C  
-ATOM    247  C   GLU A  32      18.601  14.245  -6.331  1.00 40.09           C  
-ANISOU  247  C   GLU A  32     5945   5291   3996  -1766   1238   1126       C  
-ATOM    248  O   GLU A  32      18.103  14.348  -7.453  1.00 44.22           O  
-ANISOU  248  O   GLU A  32     6748   5900   4154  -1588   1438   1342       O  
-ATOM    249  CB  GLU A  32      20.902  15.097  -5.837  1.00 50.98           C  
-ANISOU  249  CB  GLU A  32     6832   6397   6141  -2572   1525    972       C  
-ATOM    250  CG  GLU A  32      21.419  15.127  -7.272  1.00 59.39           C  
-ANISOU  250  CG  GLU A  32     7882   7578   7108  -2610   2019   1165       C  
-ATOM    251  CD  GLU A  32      21.208  16.480  -7.937  1.00 72.51           C  
-ANISOU  251  CD  GLU A  32    10024   8868   8657  -2610   2256   1496       C  
-ATOM    252  OE1 GLU A  32      21.350  17.517  -7.250  1.00 75.16           O  
-ANISOU  252  OE1 GLU A  32    10498   8794   9266  -2841   2199   1495       O  
-ATOM    253  OE2 GLU A  32      20.894  16.505  -9.147  1.00 78.88           O  
-ANISOU  253  OE2 GLU A  32    11067   9804   9099  -2364   2463   1740       O  
-ATOM    254  N   ARG A  33      18.497  13.151  -5.582  1.00 37.59           N  
-ANISOU  254  N   ARG A  33     5301   5200   3783  -1613    944    867       N  
-ATOM    255  CA  ARG A  33      17.800  11.947  -6.033  1.00 37.32           C  
-ANISOU  255  CA  ARG A  33     5155   5501   3524  -1273    877    782       C  
-ATOM    256  C   ARG A  33      17.254  11.205  -4.832  1.00 32.02           C  
-ANISOU  256  C   ARG A  33     4370   4841   2955  -1087    530    581       C  
-ATOM    257  O   ARG A  33      17.802  11.295  -3.738  1.00 30.58           O  
-ANISOU  257  O   ARG A  33     4077   4534   3008  -1227    346    471       O  
-ATOM    258  CB  ARG A  33      18.758  10.994  -6.766  1.00 41.98           C  
-ANISOU  258  CB  ARG A  33     5329   6409   4212  -1362   1102    668       C  
-ATOM    259  CG  ARG A  33      19.514  11.567  -7.941  1.00 46.99           C  
-ANISOU  259  CG  ARG A  33     6023   7069   4762  -1593   1558    842       C  
-ATOM    260  CD  ARG A  33      18.645  11.673  -9.177  1.00 52.69           C  
-ANISOU  260  CD  ARG A  33     7133   7866   5020  -1259   1664   1011       C  
-ATOM    261  NE  ARG A  33      18.485  10.386  -9.846  1.00 47.68           N  
-ANISOU  261  NE  ARG A  33     6284   7558   4275   -999   1652    795       N  
-ATOM    262  CZ  ARG A  33      17.968  10.244 -11.061  1.00 51.82           C  
-ANISOU  262  CZ  ARG A  33     7071   8167   4451   -708   1734    833       C  
-ATOM    263  NH1 ARG A  33      17.562  11.312 -11.729  1.00 50.60           N  
-ANISOU  263  NH1 ARG A  33     7357   7876   3993   -566   1824   1142       N  
-ATOM    264  NH2 ARG A  33      17.864   9.039 -11.612  1.00 49.71           N  
-ANISOU  264  NH2 ARG A  33     6615   8128   4147   -542   1699    568       N  
-ATOM    265  N   VAL A  34      16.182  10.449  -5.034  1.00 27.22           N  
-ANISOU  265  N   VAL A  34     3795   4381   2166   -772    449    518       N  
-ATOM    266  CA  VAL A  34      15.789   9.444  -4.056  1.00 26.06           C  
-ANISOU  266  CA  VAL A  34     3493   4270   2140   -618    248    336       C  
-ATOM    267  C   VAL A  34      16.747   8.263  -4.215  1.00 26.01           C  
-ANISOU  267  C   VAL A  34     3073   4482   2330   -662    291    195       C  
-ATOM    268  O   VAL A  34      16.980   7.782  -5.333  1.00 30.06           O  
-ANISOU  268  O   VAL A  34     3424   5216   2782   -640    484    159       O  
-ATOM    269  CB  VAL A  34      14.337   9.008  -4.263  1.00 28.90           C  
-ANISOU  269  CB  VAL A  34     3955   4682   2342   -315    205    272       C  
-ATOM    270  CG1 VAL A  34      13.977   7.832  -3.349  1.00 29.16           C  
-ANISOU  270  CG1 VAL A  34     3825   4718   2535   -197    116    102       C  
-ATOM    271  CG2 VAL A  34      13.406  10.182  -3.984  1.00 35.08           C  
-ANISOU  271  CG2 VAL A  34     5102   5229   2999   -225    138    380       C  
-ATOM    272  N   PHE A  35      17.320   7.808  -3.105  1.00 26.75           N  
-ANISOU  272  N   PHE A  35     3016   4511   2636   -692    101    107       N  
-ATOM    273  CA  PHE A  35      18.332   6.757  -3.167  1.00 26.42           C  
-ANISOU  273  CA  PHE A  35     2566   4634   2837   -695     97    -24       C  
-ATOM    274  C   PHE A  35      17.711   5.414  -2.788  1.00 30.97           C  
-ANISOU  274  C   PHE A  35     3094   5228   3445   -427     29   -119       C  
-ATOM    275  O   PHE A  35      17.842   4.427  -3.524  1.00 31.82           O  
-ANISOU  275  O   PHE A  35     2956   5491   3644   -332    166   -236       O  
-ATOM    276  CB  PHE A  35      19.498   7.100  -2.252  1.00 29.90           C  
-ANISOU  276  CB  PHE A  35     2841   4999   3522   -865   -121    -72       C  
-ATOM    277  CG  PHE A  35      20.752   6.359  -2.569  1.00 34.90           C  
-ANISOU  277  CG  PHE A  35     2974   5813   4473   -906    -93   -214       C  
-ATOM    278  CD1 PHE A  35      21.340   6.461  -3.829  1.00 36.84           C  
-ANISOU  278  CD1 PHE A  35     2972   6228   4799  -1065    260   -237       C  
-ATOM    279  CD2 PHE A  35      21.365   5.571  -1.603  1.00 36.99           C  
-ANISOU  279  CD2 PHE A  35     3031   6076   4947   -759   -409   -322       C  
-ATOM    280  CE1 PHE A  35      22.515   5.786  -4.115  1.00 44.82           C  
-ANISOU  280  CE1 PHE A  35     3467   7406   6156  -1096    330   -410       C  
-ATOM    281  CE2 PHE A  35      22.545   4.890  -1.885  1.00 39.70           C  
-ANISOU  281  CE2 PHE A  35     2858   6579   5646   -749   -413   -481       C  
-ATOM    282  CZ  PHE A  35      23.114   4.996  -3.143  1.00 44.53           C  
-ANISOU  282  CZ  PHE A  35     3188   7339   6394   -916    -25   -536       C  
-ATOM    283  N   ILE A  36      17.036   5.384  -1.641  1.00 30.70           N  
-ANISOU  283  N   ILE A  36     3318   5005   3342   -318   -137    -80       N  
-ATOM    284  CA  ILE A  36      16.247   4.216  -1.241  1.00 26.69           C  
-ANISOU  284  CA  ILE A  36     2849   4430   2864    -97   -108   -131       C  
-ATOM    285  C   ILE A  36      14.836   4.635  -0.865  1.00 28.05           C  
-ANISOU  285  C   ILE A  36     3339   4456   2862    -26    -46    -97       C  
-ATOM    286  O   ILE A  36      14.629   5.223   0.200  1.00 26.81           O  
-ANISOU  286  O   ILE A  36     3466   4131   2590    -31   -153    -23       O  
-ATOM    287  CB  ILE A  36      16.880   3.475  -0.045  1.00 25.56           C  
-ANISOU  287  CB  ILE A  36     2712   4169   2829     14   -312   -106       C  
-ATOM    288  CG1 ILE A  36      18.368   3.225  -0.297  1.00 27.97           C  
-ANISOU  288  CG1 ILE A  36     2637   4618   3370    -37   -442   -174       C  
-ATOM    289  CG2 ILE A  36      16.167   2.144   0.201  1.00 26.13           C  
-ANISOU  289  CG2 ILE A  36     2824   4116   2986    219   -182   -128       C  
-ATOM    290  CD1 ILE A  36      19.150   2.864   0.987  1.00 32.00           C  
-ANISOU  290  CD1 ILE A  36     3183   5035   3942     98   -794   -142       C  
-ATOM    291  N   PRO A  37      13.857   4.329  -1.732  1.00 23.86           N  
-ANISOU  291  N   PRO A  37     2740   4003   2323     57    117   -197       N  
-ATOM    292  CA  PRO A  37      12.462   4.688  -1.459  1.00 22.73           C  
-ANISOU  292  CA  PRO A  37     2790   3743   2102    147    181   -225       C  
-ATOM    293  C   PRO A  37      11.992   4.136  -0.128  1.00 24.94           C  
-ANISOU  293  C   PRO A  37     3245   3793   2440    215    238   -203       C  
-ATOM    294  O   PRO A  37      12.369   3.011   0.236  1.00 23.55           O  
-ANISOU  294  O   PRO A  37     2989   3555   2404    261    280   -208       O  
-ATOM    295  CB  PRO A  37      11.692   3.988  -2.582  1.00 22.78           C  
-ANISOU  295  CB  PRO A  37     2559   3906   2192    245    292   -428       C  
-ATOM    296  CG  PRO A  37      12.699   3.874  -3.712  1.00 26.92           C  
-ANISOU  296  CG  PRO A  37     2892   4668   2667    183    287   -448       C  
-ATOM    297  CD  PRO A  37      14.006   3.603  -3.008  1.00 26.13           C  
-ANISOU  297  CD  PRO A  37     2736   4506   2685     87    232   -346       C  
-ATOM    298  N   HIS A  38      11.181   4.921   0.576  1.00 24.19           N  
-ANISOU  298  N   HIS A  38     3622   3048   2522    -96   -326    494       N  
-ATOM    299  CA  HIS A  38      10.599   4.522   1.852  1.00 22.50           C  
-ANISOU  299  CA  HIS A  38     3258   2823   2468      8   -307    407       C  
-ATOM    300  C   HIS A  38      10.006   3.120   1.792  1.00 22.40           C  
-ANISOU  300  C   HIS A  38     3166   2895   2451     61   -335    349       C  
-ATOM    301  O   HIS A  38      10.228   2.288   2.674  1.00 21.00           O  
-ANISOU  301  O   HIS A  38     2891   2780   2309     87   -257    260       O  
-ATOM    302  CB  HIS A  38       9.482   5.496   2.251  1.00 23.79           C  
-ANISOU  302  CB  HIS A  38     3407   2834   2798     98   -401    448       C  
-ATOM    303  CG  HIS A  38       8.790   5.113   3.524  1.00 27.52           C  
-ANISOU  303  CG  HIS A  38     3731   3303   3424    193   -360    352       C  
-ATOM    304  ND1 HIS A  38       7.515   4.586   3.551  1.00 26.71           N  
-ANISOU  304  ND1 HIS A  38     3526   3200   3424    283   -442    344       N  
-ATOM    305  CD2 HIS A  38       9.196   5.177   4.818  1.00 27.18           C  
-ANISOU  305  CD2 HIS A  38     3628   3265   3435    192   -243    262       C  
-ATOM    306  CE1 HIS A  38       7.167   4.341   4.802  1.00 27.64           C  
-ANISOU  306  CE1 HIS A  38     3528   3323   3649    332   -358    251       C  
-ATOM    307  NE2 HIS A  38       8.162   4.694   5.592  1.00 29.83           N  
-ANISOU  307  NE2 HIS A  38     3841   3601   3892    279   -241    200       N  
-ATOM    308  N   GLY A  39       9.250   2.861   0.733  1.00 24.98           N  
-ANISOU  308  N   GLY A  39     3552   3215   2725     63   -461    408       N  
-ATOM    309  CA  GLY A  39       8.557   1.590   0.632  1.00 29.03           C  
-ANISOU  309  CA  GLY A  39     4004   3787   3237     94   -509    358       C  
-ATOM    310  C   GLY A  39       9.511   0.424   0.510  1.00 24.25           C  
-ANISOU  310  C   GLY A  39     3418   3288   2509     53   -397    274       C  
-ATOM    311  O   GLY A  39       9.235  -0.662   1.000  1.00 23.94           O  
-ANISOU  311  O   GLY A  39     3308   3283   2505     86   -382    201       O  
-ATOM    312  N   LEU A  40      10.636   0.640  -0.162  1.00 23.98           N  
-ANISOU  312  N   LEU A  40     3480   3300   2332    -21   -314    284       N  
-ATOM    313  CA  LEU A  40      11.657  -0.403  -0.245  1.00 26.06           C  
-ANISOU  313  CA  LEU A  40     3738   3661   2502    -37   -185    193       C  
-ATOM    314  C   LEU A  40      12.255  -0.672   1.146  1.00 23.61           C  
-ANISOU  314  C   LEU A  40     3288   3375   2308     15    -87    124       C  
-ATOM    315  O   LEU A  40      12.544  -1.817   1.525  1.00 21.19           O  
-ANISOU  315  O   LEU A  40     2931   3110   2009     58    -39     45       O  
-ATOM    316  CB  LEU A  40      12.723  -0.008  -1.274  1.00 27.57           C  
-ANISOU  316  CB  LEU A  40     4040   3910   2524   -134    -96    217       C  
-ATOM    317  CG  LEU A  40      13.958  -0.904  -1.385  1.00 33.10           C  
-ANISOU  317  CG  LEU A  40     4709   4719   3149   -137     71    117       C  
-ATOM    318  CD1 LEU A  40      13.547  -2.349  -1.637  1.00 36.51           C  
-ANISOU  318  CD1 LEU A  40     5163   5161   3550    -79     53     30       C  
-ATOM    319  CD2 LEU A  40      14.907  -0.401  -2.463  1.00 26.13           C  
-ANISOU  319  CD2 LEU A  40     3928   3904   2095   -251    176    142       C  
-ATOM    320  N   ILE A  41      12.407   0.390   1.924  1.00 21.18           N  
-ANISOU  320  N   ILE A  41     2936   3025   2087      7    -73    156       N  
-ATOM    321  CA  ILE A  41      12.903   0.257   3.289  1.00 20.06           C  
-ANISOU  321  CA  ILE A  41     2682   2901   2038     35     -5    100       C  
-ATOM    322  C   ILE A  41      11.943  -0.614   4.090  1.00 21.78           C  
-ANISOU  322  C   ILE A  41     2835   3096   2346    107    -50     55       C  
-ATOM    323  O   ILE A  41      12.371  -1.522   4.811  1.00 19.59           O  
-ANISOU  323  O   ILE A  41     2499   2860   2083    133     -6     -2       O  
-ATOM    324  CB  ILE A  41      13.089   1.634   3.961  1.00 23.66           C  
-ANISOU  324  CB  ILE A  41     3136   3296   2559     -3      8    136       C  
-ATOM    325  CG1 ILE A  41      14.204   2.435   3.284  1.00 23.20           C  
-ANISOU  325  CG1 ILE A  41     3137   3269   2407   -107     68    180       C  
-ATOM    326  CG2 ILE A  41      13.403   1.477   5.465  1.00 21.49           C  
-ANISOU  326  CG2 ILE A  41     2765   3034   2365     13     55     75       C  
-ATOM    327  CD1 ILE A  41      14.307   3.895   3.788  1.00 25.30           C  
-ANISOU  327  CD1 ILE A  41     3444   3441   2728   -166     63    224       C  
-ATOM    328  N   MET A  42      10.644  -0.350   3.942  1.00 20.09           N  
-ANISOU  328  N   MET A  42     2624   2814   2194    134   -145     88       N  
-ATOM    329  CA  MET A  42       9.611  -1.104   4.651  1.00 20.55           C  
-ANISOU  329  CA  MET A  42     2609   2859   2342    179   -181     51       C  
-ATOM    330  C   MET A  42       9.682  -2.583   4.278  1.00 20.08           C  
-ANISOU  330  C   MET A  42     2570   2845   2214    178   -188      7       C  
-ATOM    331  O   MET A  42       9.679  -3.452   5.157  1.00 19.55           O  
-ANISOU  331  O   MET A  42     2458   2789   2183    194   -157    -41       O  
-ATOM    332  CB  MET A  42       8.218  -0.577   4.301  1.00 21.82           C  
-ANISOU  332  CB  MET A  42     2745   2956   2587    208   -289    100       C  
-ATOM    333  CG  MET A  42       7.949   0.823   4.804  1.00 25.68           C  
-ANISOU  333  CG  MET A  42     3211   3365   3181    239   -282    129       C  
-ATOM    334  SD  MET A  42       8.244   0.981   6.578  1.00 34.50           S  
-ANISOU  334  SD  MET A  42     4256   4478   4376    247   -153     46       S  
-ATOM    335  CE  MET A  42       6.759   0.238   7.263  1.00 52.39           C  
-ANISOU  335  CE  MET A  42     6396   6749   6759    290   -168      3       C  
-ATOM    336  N   ASP A  43       9.748  -2.870   2.981  1.00 19.02           N  
-ANISOU  336  N   ASP A  43     2528   2727   1972    153   -230     24       N  
-ATOM    337  CA  ASP A  43       9.774  -4.276   2.543  1.00 19.87           C  
-ANISOU  337  CA  ASP A  43     2686   2856   2009    150   -236    -33       C  
-ATOM    338  C   ASP A  43      10.990  -5.025   3.061  1.00 23.61           C  
-ANISOU  338  C   ASP A  43     3144   3364   2463    183   -124    -98       C  
-ATOM    339  O   ASP A  43      10.900  -6.197   3.438  1.00 21.44           O  
-ANISOU  339  O   ASP A  43     2872   3071   2203    209   -124   -148       O  
-ATOM    340  CB  ASP A  43       9.732  -4.369   1.020  1.00 21.07           C  
-ANISOU  340  CB  ASP A  43     2968   3019   2018    103   -287    -16       C  
-ATOM    341  CG  ASP A  43       8.402  -3.946   0.455  1.00 26.75           C  
-ANISOU  341  CG  ASP A  43     3701   3704   2760     73   -445     54       C  
-ATOM    342  OD1 ASP A  43       7.371  -4.102   1.155  1.00 29.97           O  
-ANISOU  342  OD1 ASP A  43     4005   4085   3297     95   -509     59       O  
-ATOM    343  OD2 ASP A  43       8.393  -3.447  -0.679  1.00 28.42           O  
-ANISOU  343  OD2 ASP A  43     4021   3918   2860     24   -505    109       O  
-ATOM    344  N   ARG A  44      12.144  -4.362   3.062  1.00 22.17           N  
-ANISOU  344  N   ARG A  44     2943   3227   2252    180    -37    -92       N  
-ATOM    345  CA  ARG A  44      13.352  -4.997   3.577  1.00 20.08           C  
-ANISOU  345  CA  ARG A  44     2628   3008   1995    223     56   -145       C  
-ATOM    346  C   ARG A  44      13.216  -5.196   5.079  1.00 23.64           C  
-ANISOU  346  C   ARG A  44     2994   3436   2552    249     40   -146       C  
-ATOM    347  O   ARG A  44      13.563  -6.252   5.620  1.00 23.28           O  
-ANISOU  347  O   ARG A  44     2932   3384   2530    298     48   -184       O  
-ATOM    348  CB  ARG A  44      14.598  -4.157   3.236  1.00 19.96           C  
-ANISOU  348  CB  ARG A  44     2583   3065   1934    190    150   -131       C  
-ATOM    349  CG  ARG A  44      15.876  -4.699   3.830  1.00 21.29           C  
-ANISOU  349  CG  ARG A  44     2652   3296   2141    241    231   -176       C  
-ATOM    350  CD  ARG A  44      16.181  -6.117   3.358  1.00 25.89           C  
-ANISOU  350  CD  ARG A  44     3265   3876   2698    323    267   -253       C  
-ATOM    351  NE  ARG A  44      17.410  -6.611   3.991  1.00 28.49           N  
-ANISOU  351  NE  ARG A  44     3472   4257   3096    397    328   -287       N  
-ATOM    352  CZ  ARG A  44      17.604  -7.863   4.401  1.00 33.52           C  
-ANISOU  352  CZ  ARG A  44     4098   4850   3787    500    313   -333       C  
-ATOM    353  NH1 ARG A  44      16.656  -8.779   4.230  1.00 29.37           N  
-ANISOU  353  NH1 ARG A  44     3690   4226   3244    523    253   -360       N  
-ATOM    354  NH2 ARG A  44      18.757  -8.202   4.968  1.00 34.74           N  
-ANISOU  354  NH2 ARG A  44     4124   5055   4020    577    347   -347       N  
-ATOM    355  N   THR A  45      12.682  -4.186   5.760  1.00 20.09           N  
-ANISOU  355  N   THR A  45     2508   2965   2162    216     16   -107       N  
-ATOM    356  CA  THR A  45      12.536  -4.244   7.212  1.00 19.95           C  
-ANISOU  356  CA  THR A  45     2431   2931   2216    218     15   -114       C  
-ATOM    357  C   THR A  45      11.589  -5.374   7.612  1.00 23.89           C  
-ANISOU  357  C   THR A  45     2945   3390   2743    231    -30   -133       C  
-ATOM    358  O   THR A  45      11.783  -6.024   8.642  1.00 22.60           O  
-ANISOU  358  O   THR A  45     2767   3220   2599    236    -25   -145       O  
-ATOM    359  CB  THR A  45      12.057  -2.894   7.780  1.00 20.78           C  
-ANISOU  359  CB  THR A  45     2516   3007   2374    181     18    -88       C  
-ATOM    360  OG1 THR A  45      13.015  -1.881   7.442  1.00 23.00           O  
-ANISOU  360  OG1 THR A  45     2802   3314   2624    146     56    -65       O  
-ATOM    361  CG2 THR A  45      11.904  -2.947   9.318  1.00 22.04           C  
-ANISOU  361  CG2 THR A  45     2640   3157   2580    165     37   -110       C  
-ATOM    362  N   GLU A  46      10.578  -5.633   6.786  1.00 20.49           N  
-ANISOU  362  N   GLU A  46     2550   2930   2304    223    -84   -130       N  
-ATOM    363  CA  GLU A  46       9.669  -6.744   7.071  1.00 17.67           C  
-ANISOU  363  CA  GLU A  46     2208   2536   1971    208   -129   -147       C  
-ATOM    364  C   GLU A  46      10.423  -8.071   7.142  1.00 22.81           C  
-ANISOU  364  C   GLU A  46     2917   3167   2581    240   -118   -182       C  
-ATOM    365  O   GLU A  46      10.200  -8.872   8.056  1.00 20.73           O  
-ANISOU  365  O   GLU A  46     2663   2870   2345    227   -130   -185       O  
-ATOM    366  CB  GLU A  46       8.557  -6.858   6.019  1.00 21.19           C  
-ANISOU  366  CB  GLU A  46     2681   2964   2407    179   -210   -136       C  
-ATOM    367  CG  GLU A  46       7.571  -8.000   6.335  1.00 21.03           C  
-ANISOU  367  CG  GLU A  46     2666   2909   2415    133   -260   -153       C  
-ATOM    368  CD  GLU A  46       6.402  -8.072   5.357  1.00 32.29           C  
-ANISOU  368  CD  GLU A  46     4094   4331   3843     84   -364   -137       C  
-ATOM    369  OE1 GLU A  46       5.548  -8.962   5.508  1.00 31.60           O  
-ANISOU  369  OE1 GLU A  46     4005   4222   3779     22   -414   -148       O  
-ATOM    370  OE2 GLU A  46       6.336  -7.241   4.428  1.00 36.92           O  
-ANISOU  370  OE2 GLU A  46     4689   4934   4403     95   -410   -104       O  
-ATOM    371  N   ARG A  47      11.318  -8.296   6.183  1.00 21.89           N  
-ANISOU  371  N   ARG A  47     2848   3068   2402    283    -91   -209       N  
-ATOM    372  CA  ARG A  47      12.069  -9.550   6.142  1.00 24.30           C  
-ANISOU  372  CA  ARG A  47     3206   3338   2689    344    -73   -255       C  
-ATOM    373  C   ARG A  47      13.043  -9.550   7.304  1.00 25.52           C  
-ANISOU  373  C   ARG A  47     3288   3515   2895    388    -46   -238       C  
-ATOM    374  O   ARG A  47      13.244 -10.574   7.963  1.00 24.00           O  
-ANISOU  374  O   ARG A  47     3125   3265   2730    425    -73   -242       O  
-ATOM    375  CB  ARG A  47      12.816  -9.709   4.821  1.00 25.74           C  
-ANISOU  375  CB  ARG A  47     3444   3543   2792    384    -19   -306       C  
-ATOM    376  CG  ARG A  47      13.781 -10.896   4.812  1.00 28.90           C  
-ANISOU  376  CG  ARG A  47     3876   3904   3200    483     26   -368       C  
-ATOM    377  CD  ARG A  47      13.040 -12.195   5.065  1.00 32.91           C  
-ANISOU  377  CD  ARG A  47     4489   4294   3723    480    -44   -391       C  
-ATOM    378  NE  ARG A  47      13.950 -13.326   5.264  1.00 37.36           N  
-ANISOU  378  NE  ARG A  47     5086   4786   4324    596    -18   -439       N  
-ATOM    379  CZ  ARG A  47      14.142 -14.301   4.386  1.00 35.97           C  
-ANISOU  379  CZ  ARG A  47     5029   4530   4106    651     12   -527       C  
-ATOM    380  NH1 ARG A  47      13.477 -14.305   3.229  1.00 32.81           N  
-ANISOU  380  NH1 ARG A  47     4741   4123   3601    577     12   -574       N  
-ATOM    381  NH2 ARG A  47      14.990 -15.289   4.666  1.00 34.61           N  
-ANISOU  381  NH2 ARG A  47     4876   4277   3997    782     34   -569       N  
-ATOM    382  N   LEU A  48      13.634  -8.390   7.571  1.00 21.61           N  
-ANISOU  382  N   LEU A  48     2709   3092   2409    374     -7   -211       N  
-ATOM    383  CA  LEU A  48      14.561  -8.276   8.699  1.00 23.33           C  
-ANISOU  383  CA  LEU A  48     2854   3344   2667    392     -4   -189       C  
-ATOM    384  C   LEU A  48      13.910  -8.674  10.021  1.00 23.21           C  
-ANISOU  384  C   LEU A  48     2863   3281   2677    351    -58   -160       C  
-ATOM    385  O   LEU A  48      14.539  -9.324  10.853  1.00 24.60           O  
-ANISOU  385  O   LEU A  48     3034   3443   2868    382    -93   -141       O  
-ATOM    386  CB  LEU A  48      15.133  -6.861   8.818  1.00 28.00           C  
-ANISOU  386  CB  LEU A  48     3369   4012   3257    344     36   -166       C  
-ATOM    387  CG  LEU A  48      16.333  -6.513   7.954  1.00 35.63           C  
-ANISOU  387  CG  LEU A  48     4278   5056   4203    370    104   -181       C  
-ATOM    388  CD1 LEU A  48      17.002  -5.248   8.450  1.00 31.23           C  
-ANISOU  388  CD1 LEU A  48     3645   4566   3656    298    124   -148       C  
-ATOM    389  CD2 LEU A  48      17.329  -7.654   7.932  1.00 36.55           C  
-ANISOU  389  CD2 LEU A  48     4350   5187   4351    474    116   -213       C  
-ATOM    390  N   ALA A  49      12.662  -8.260  10.227  1.00 21.05           N  
-ANISOU  390  N   ALA A  49     2608   2984   2404    280    -63   -153       N  
-ATOM    391  CA  ALA A  49      11.957  -8.575  11.465  1.00 22.85           C  
-ANISOU  391  CA  ALA A  49     2859   3181   2641    218    -83   -133       C  
-ATOM    392  C   ALA A  49      11.815 -10.076  11.623  1.00 21.61           C  
-ANISOU  392  C   ALA A  49     2784   2950   2478    232   -133   -128       C  
-ATOM    393  O   ALA A  49      11.940 -10.612  12.727  1.00 21.96           O  
-ANISOU  393  O   ALA A  49     2867   2966   2510    202   -164    -95       O  
-ATOM    394  CB  ALA A  49      10.603  -7.911  11.482  1.00 24.59           C  
-ANISOU  394  CB  ALA A  49     3058   3399   2887    154    -60   -140       C  
-ATOM    395  N   ARG A  50      11.543 -10.768  10.519  1.00 21.68           N  
-ANISOU  395  N   ARG A  50     2841   2914   2482    266   -149   -159       N  
-ATOM    396  CA  ARG A  50      11.395 -12.212  10.598  1.00 24.36           C  
-ANISOU  396  CA  ARG A  50     3284   3153   2816    275   -198   -161       C  
-ATOM    397  C   ARG A  50      12.728 -12.875  10.948  1.00 28.01           C  
-ANISOU  397  C   ARG A  50     3763   3583   3295    381   -222   -150       C  
-ATOM    398  O   ARG A  50      12.773 -13.828  11.744  1.00 30.29           O  
-ANISOU  398  O   ARG A  50     4130   3789   3589    378   -280   -113       O  
-ATOM    399  CB  ARG A  50      10.853 -12.782   9.282  1.00 30.91           C  
-ANISOU  399  CB  ARG A  50     4184   3935   3626    278   -212   -211       C  
-ATOM    400  CG  ARG A  50      10.316 -14.202   9.436  1.00 38.70           C  
-ANISOU  400  CG  ARG A  50     5299   4797   4607    240   -269   -215       C  
-ATOM    401  CD  ARG A  50       9.586 -14.645   8.189  1.00 43.51           C  
-ANISOU  401  CD  ARG A  50     5984   5365   5183    201   -295   -267       C  
-ATOM    402  NE  ARG A  50      10.520 -14.969   7.121  1.00 45.92           N  
-ANISOU  402  NE  ARG A  50     6349   5644   5453    311   -266   -334       N  
-ATOM    403  CZ  ARG A  50      10.255 -14.844   5.825  1.00 47.01           C  
-ANISOU  403  CZ  ARG A  50     6535   5798   5529    293   -262   -388       C  
-ATOM    404  NH1 ARG A  50       9.079 -14.386   5.421  1.00 46.12           N  
-ANISOU  404  NH1 ARG A  50     6401   5726   5397    179   -314   -369       N  
-ATOM    405  NH2 ARG A  50      11.173 -15.169   4.931  1.00 49.43           N  
-ANISOU  405  NH2 ARG A  50     6905   6084   5791    390   -206   -462       N  
-ATOM    406  N   ASP A  51      13.809 -12.370  10.354  1.00 23.79           N  
-ANISOU  406  N   ASP A  51     3150   3115   2773    470   -180   -176       N  
-ATOM    407  CA  ASP A  51      15.152 -12.886  10.614  1.00 22.46           C  
-ANISOU  407  CA  ASP A  51     2944   2941   2650    590   -199   -169       C  
-ATOM    408  C   ASP A  51      15.511 -12.680  12.082  1.00 25.15           C  
-ANISOU  408  C   ASP A  51     3250   3306   3001    552   -264    -92       C  
-ATOM    409  O   ASP A  51      16.095 -13.553  12.718  1.00 25.18           O  
-ANISOU  409  O   ASP A  51     3284   3245   3036    616   -341    -52       O  
-ATOM    410  CB  ASP A  51      16.183 -12.178   9.716  1.00 25.87           C  
-ANISOU  410  CB  ASP A  51     3262   3474   3093    661   -118   -212       C  
-ATOM    411  CG  ASP A  51      16.028 -12.535   8.233  1.00 31.39           C  
-ANISOU  411  CG  ASP A  51     4023   4147   3755    702    -50   -294       C  
-ATOM    412  OD1 ASP A  51      15.317 -13.506   7.921  1.00 28.96           O  
-ANISOU  412  OD1 ASP A  51     3847   3728   3430    702    -81   -324       O  
-ATOM    413  OD2 ASP A  51      16.642 -11.859   7.378  1.00 27.89           O  
-ANISOU  413  OD2 ASP A  51     3513   3794   3290    721     36   -330       O  
-ATOM    414  N   VAL A  52      15.155 -11.516  12.611  1.00 25.09           N  
-ANISOU  414  N   VAL A  52     3192   3380   2959    446   -239    -72       N  
-ATOM    415  CA  VAL A  52      15.411 -11.218  14.020  1.00 23.93           C  
-ANISOU  415  CA  VAL A  52     3041   3263   2790    378   -293    -11       C  
-ATOM    416  C   VAL A  52      14.680 -12.219  14.895  1.00 27.83           C  
-ANISOU  416  C   VAL A  52     3667   3658   3250    319   -356     35       C  
-ATOM    417  O   VAL A  52      15.252 -12.812  15.804  1.00 25.44           O  
-ANISOU  417  O   VAL A  52     3407   3321   2937    329   -449    101       O  
-ATOM    418  CB  VAL A  52      14.955  -9.799  14.386  1.00 27.72           C  
-ANISOU  418  CB  VAL A  52     3479   3821   3232    267   -234    -21       C  
-ATOM    419  CG1 VAL A  52      14.870  -9.640  15.902  1.00 26.10           C  
-ANISOU  419  CG1 VAL A  52     3324   3624   2967    162   -277     25       C  
-ATOM    420  CG2 VAL A  52      15.892  -8.751  13.772  1.00 29.09           C  
-ANISOU  420  CG2 VAL A  52     3537   4088   3429    297   -191    -43       C  
-ATOM    421  N   MET A  53      13.411 -12.437  14.597  1.00 27.48           N  
-ANISOU  421  N   MET A  53     3688   3567   3186    248   -314     10       N  
-ATOM    422  CA AMET A  53      12.607 -13.333  15.412  0.64 28.63           C  
-ANISOU  422  CA AMET A  53     3960   3628   3290    154   -353     54       C  
-ATOM    423  CA BMET A  53      12.599 -13.336  15.408  0.36 28.70           C  
-ANISOU  423  CA BMET A  53     3969   3637   3300    154   -353     54       C  
-ATOM    424  C   MET A  53      13.095 -14.772  15.334  1.00 30.63           C  
-ANISOU  424  C   MET A  53     4319   3750   3569    238   -446     89       C  
-ATOM    425  O   MET A  53      13.069 -15.505  16.328  1.00 32.28           O  
-ANISOU  425  O   MET A  53     4641   3886   3740    184   -522    163       O  
-ATOM    426  CB AMET A  53      11.127 -13.202  15.047  0.64 28.63           C  
-ANISOU  426  CB AMET A  53     3969   3626   3283     51   -285     16       C  
-ATOM    427  CB BMET A  53      11.115 -13.238  15.021  0.36 28.51           C  
-ANISOU  427  CB BMET A  53     3956   3607   3268     52   -286     16       C  
-ATOM    428  CG AMET A  53      10.511 -11.959  15.652  0.64 25.87           C  
-ANISOU  428  CG AMET A  53     3545   3372   2911    -44   -202      0       C  
-ATOM    429  CG BMET A  53      10.173 -14.095  15.872  0.36 30.65           C  
-ANISOU  429  CG BMET A  53     4343   3810   3493    -84   -301     59       C  
-ATOM    430  SD AMET A  53      10.681 -11.950  17.458  0.64 42.46           S  
-ANISOU  430  SD AMET A  53     5729   5488   4916   -163   -213     60       S  
-ATOM    431  SD BMET A  53       9.775 -13.512  17.547  0.36 53.46           S  
-ANISOU  431  SD BMET A  53     7257   6765   6292   -244   -251    100       S  
-ATOM    432  CE AMET A  53       9.694 -13.392  17.849  0.64 53.64           C  
-ANISOU  432  CE AMET A  53     7285   6800   6294   -274   -239    105       C  
-ATOM    433  CE BMET A  53      10.496 -11.866  17.615  0.36 42.00           C  
-ANISOU  433  CE BMET A  53     5674   5437   4849   -189   -198     58       C  
-ATOM    434  N   LYS A  54      13.566 -15.175  14.161  1.00 28.38           N  
-ANISOU  434  N   LYS A  54     4014   3426   3342    370   -439     33       N  
-ATOM    435  CA  LYS A  54      14.128 -16.508  14.019  1.00 31.47           C  
-ANISOU  435  CA  LYS A  54     4506   3673   3779    483   -516     47       C  
-ATOM    436  C   LYS A  54      15.356 -16.674  14.917  1.00 34.25           C  
-ANISOU  436  C   LYS A  54     4822   4025   4165    573   -613    124       C  
-ATOM    437  O   LYS A  54      15.554 -17.717  15.540  1.00 33.83           O  
-ANISOU  437  O   LYS A  54     4889   3840   4124    603   -721    194       O  
-ATOM    438  CB  LYS A  54      14.498 -16.782  12.560  1.00 32.32           C  
-ANISOU  438  CB  LYS A  54     4593   3753   3935    615   -460    -51       C  
-ATOM    439  CG  LYS A  54      14.781 -18.248  12.277  1.00 44.31           C  
-ANISOU  439  CG  LYS A  54     6252   5083   5500    724   -518    -66       C  
-ATOM    440  CD  LYS A  54      13.521 -19.087  12.486  1.00 52.91           C  
-ANISOU  440  CD  LYS A  54     7526   6039   6538    579   -559    -45       C  
-ATOM    441  CE  LYS A  54      13.791 -20.573  12.276  1.00 58.88           C  
-ANISOU  441  CE  LYS A  54     8460   6571   7339    677   -628    -56       C  
-ATOM    442  NZ  LYS A  54      14.723 -21.115  13.298  1.00 64.93           N  
-ANISOU  442  NZ  LYS A  54     9252   7254   8163    782   -739     42       N  
-ATOM    443  N   GLU A  55      16.169 -15.628  15.006  1.00 32.10           N  
-ANISOU  443  N   GLU A  55     4389   3899   3909    605   -589    120       N  
-ATOM    444  CA  GLU A  55      17.415 -15.701  15.774  1.00 32.98           C  
-ANISOU  444  CA  GLU A  55     4428   4038   4066    688   -697    193       C  
-ATOM    445  C   GLU A  55      17.212 -15.439  17.272  1.00 32.76           C  
-ANISOU  445  C   GLU A  55     4469   4036   3943    538   -787    294       C  
-ATOM    446  O   GLU A  55      17.862 -16.061  18.115  1.00 35.55           O  
-ANISOU  446  O   GLU A  55     4867   4334   4306    576   -933    390       O  
-ATOM    447  CB  GLU A  55      18.435 -14.707  15.198  1.00 38.73           C  
-ANISOU  447  CB  GLU A  55     4946   4920   4850    763   -635    144       C  
-ATOM    448  CG  GLU A  55      19.751 -14.607  15.972  1.00 48.12           C  
-ANISOU  448  CG  GLU A  55     6011   6175   6096    830   -754    218       C  
-ATOM    449  CD  GLU A  55      20.746 -15.703  15.616  1.00 57.96           C  
-ANISOU  449  CD  GLU A  55     7203   7338   7482   1052   -821    224       C  
-ATOM    450  OE1 GLU A  55      20.429 -16.554  14.754  1.00 59.45           O  
-ANISOU  450  OE1 GLU A  55     7474   7402   7710   1152   -762    157       O  
-ATOM    451  OE2 GLU A  55      21.854 -15.707  16.200  1.00 61.60           O  
-ANISOU  451  OE2 GLU A  55     7533   7853   8017   1128   -937    291       O  
-ATOM    452  N   MET A  56      16.308 -14.522  17.603  1.00 35.13           N  
-ANISOU  452  N   MET A  56     4784   4413   4149    370   -702    271       N  
-ATOM    453  CA  MET A  56      16.251 -13.996  18.972  1.00 35.87           C  
-ANISOU  453  CA  MET A  56     4928   4565   4136    220   -751    338       C  
-ATOM    454  C   MET A  56      14.935 -14.239  19.700  1.00 38.83           C  
-ANISOU  454  C   MET A  56     5464   4890   4398     43   -708    357       C  
-ATOM    455  O   MET A  56      14.786 -13.827  20.851  1.00 40.34           O  
-ANISOU  455  O   MET A  56     5723   5128   4475   -100   -724    399       O  
-ATOM    456  CB  MET A  56      16.526 -12.486  18.973  1.00 32.64           C  
-ANISOU  456  CB  MET A  56     4388   4308   3708    165   -675    286       C  
-ATOM    457  CG  MET A  56      17.802 -12.067  18.279  1.00 34.54           C  
-ANISOU  457  CG  MET A  56     4449   4627   4047    297   -693    264       C  
-ATOM    458  SD  MET A  56      17.982 -10.281  18.260  1.00 33.35           S  
-ANISOU  458  SD  MET A  56     4185   4625   3863    194   -599    207       S  
-ATOM    459  CE  MET A  56      18.436  -9.990  19.970  1.00 38.79           C  
-ANISOU  459  CE  MET A  56     4945   5358   4437     49   -731    289       C  
-ATOM    460  N   GLY A  57      13.985 -14.890  19.039  1.00 37.47           N  
-ANISOU  460  N   GLY A  57     5354   4633   4251     36   -649    322       N  
-ATOM    461  CA  GLY A  57      12.645 -15.025  19.586  1.00 36.49           C  
-ANISOU  461  CA  GLY A  57     5337   4489   4039   -145   -577    325       C  
-ATOM    462  C   GLY A  57      12.447 -16.084  20.656  1.00 42.22           C  
-ANISOU  462  C   GLY A  57     6259   5109   4672   -253   -671    433       C  
-ATOM    463  O   GLY A  57      11.326 -16.308  21.107  1.00 47.31           O  
-ANISOU  463  O   GLY A  57     6995   5739   5241   -421   -599    439       O  
-ATOM    464  N   GLY A  58      13.525 -16.738  21.073  1.00 41.08           N  
-ANISOU  464  N   GLY A  58     6177   4894   4538   -163   -833    526       N  
-ATOM    465  CA  GLY A  58      13.425 -17.782  22.081  1.00 45.59           C  
-ANISOU  465  CA  GLY A  58     6962   5343   5017   -260   -953    653       C  
-ATOM    466  C   GLY A  58      13.445 -17.256  23.508  1.00 47.05           C  
-ANISOU  466  C   GLY A  58     7233   5611   5032   -439   -979    723       C  
-ATOM    467  O   GLY A  58      13.256 -18.006  24.467  1.00 45.66           O  
-ANISOU  467  O   GLY A  58     7260   5351   4737   -567  -1067    837       O  
-ATOM    468  N   HIS A  59      13.684 -15.960  23.660  1.00 44.90           N  
-ANISOU  468  N   HIS A  59     6829   5498   4734   -461   -904    656       N  
-ATOM    469  CA  HIS A  59      13.776 -15.372  24.989  1.00 44.18           C  
-ANISOU  469  CA  HIS A  59     6830   5490   4467   -634   -923    701       C  
-ATOM    470  C   HIS A  59      13.419 -13.892  24.923  1.00 42.30           C  
-ANISOU  470  C   HIS A  59     6465   5400   4207   -693   -748    571       C  
-ATOM    471  O   HIS A  59      13.522 -13.283  23.868  1.00 43.00           O  
-ANISOU  471  O   HIS A  59     6376   5531   4431   -565   -674    479       O  
-ATOM    472  CB  HIS A  59      15.188 -15.555  25.548  1.00 49.42           C  
-ANISOU  472  CB  HIS A  59     7505   6149   5122   -557  -1154    814       C  
-ATOM    473  CG  HIS A  59      15.350 -15.092  26.965  1.00 56.52           C  
-ANISOU  473  CG  HIS A  59     8542   7121   5811   -755  -1216    878       C  
-ATOM    474  ND1 HIS A  59      14.929 -15.838  28.046  1.00 60.12           N  
-ANISOU  474  ND1 HIS A  59     9251   7506   6086   -933  -1284    993       N  
-ATOM    475  CD2 HIS A  59      15.899 -13.964  27.480  1.00 58.33           C  
-ANISOU  475  CD2 HIS A  59     8714   7484   5965   -821  -1223    842       C  
-ATOM    476  CE1 HIS A  59      15.207 -15.189  29.164  1.00 61.88           C  
-ANISOU  476  CE1 HIS A  59     9569   7822   6119  -1099  -1327   1022       C  
-ATOM    477  NE2 HIS A  59      15.797 -14.050  28.849  1.00 59.83           N  
-ANISOU  477  NE2 HIS A  59     9125   7685   5924  -1034  -1294    927       N  
-ATOM    478  N   HIS A  60      12.989 -13.336  26.056  1.00 37.20           N  
-ANISOU  478  N   HIS A  60     5930   4820   3384   -892   -679    563       N  
-ATOM    479  CA  HIS A  60      12.658 -11.922  26.192  1.00 34.32           C  
-ANISOU  479  CA  HIS A  60     5484   4571   2985   -958   -513    437       C  
-ATOM    480  C   HIS A  60      13.660 -11.035  25.446  1.00 36.70           C  
-ANISOU  480  C   HIS A  60     5602   4932   3410   -805   -558    388       C  
-ATOM    481  O   HIS A  60      14.863 -11.095  25.703  1.00 36.61           O  
-ANISOU  481  O   HIS A  60     5577   4937   3395   -759   -734    462       O  
-ATOM    482  CB  HIS A  60      12.641 -11.577  27.683  1.00 38.63           C  
-ANISOU  482  CB  HIS A  60     6214   5167   3296  -1174   -511    462       C  
-ATOM    483  CG  HIS A  60      12.123 -10.209  28.002  1.00 47.66           C  
-ANISOU  483  CG  HIS A  60     7327   6402   4380  -1267   -313    317       C  
-ATOM    484  ND1 HIS A  60      11.320  -9.962  29.100  1.00 51.86           N  
-ANISOU  484  ND1 HIS A  60     8017   6968   4718  -1478   -167    273       N  
-ATOM    485  CD2 HIS A  60      12.323  -9.009  27.405  1.00 46.42           C  
-ANISOU  485  CD2 HIS A  60     7016   6295   4325  -1180   -233    205       C  
-ATOM    486  CE1 HIS A  60      11.032  -8.675  29.147  1.00 52.15           C  
-ANISOU  486  CE1 HIS A  60     7992   7066   4756  -1497      0    127       C  
-ATOM    487  NE2 HIS A  60      11.623  -8.073  28.133  1.00 48.85           N  
-ANISOU  487  NE2 HIS A  60     7392   6650   4518  -1320    -47     91       N  
-ATOM    488  N   ILE A  61      13.158 -10.234  24.511  1.00 32.61           N  
-ANISOU  488  N   ILE A  61     4937   4445   3007   -734   -407    272       N  
-ATOM    489  CA  ILE A  61      13.997  -9.311  23.742  1.00 32.47           C  
-ANISOU  489  CA  ILE A  61     4758   4482   3097   -617   -421    223       C  
-ATOM    490  C   ILE A  61      13.904  -7.899  24.330  1.00 37.20           C  
-ANISOU  490  C   ILE A  61     5368   5151   3616   -728   -320    135       C  
-ATOM    491  O   ILE A  61      12.806  -7.421  24.628  1.00 36.57           O  
-ANISOU  491  O   ILE A  61     5331   5071   3492   -813   -152     53       O  
-ATOM    492  CB  ILE A  61      13.563  -9.266  22.254  1.00 35.50           C  
-ANISOU  492  CB  ILE A  61     4998   4844   3648   -471   -335    161       C  
-ATOM    493  CG1 ILE A  61      13.805 -10.615  21.571  1.00 36.90           C  
-ANISOU  493  CG1 ILE A  61     5173   4940   3906   -350   -435    227       C  
-ATOM    494  CG2 ILE A  61      14.306  -8.171  21.486  1.00 28.30           C  
-ANISOU  494  CG2 ILE A  61     3941   3991   2822   -388   -320    108       C  
-ATOM    495  CD1 ILE A  61      13.306 -10.661  20.132  1.00 39.37           C  
-ANISOU  495  CD1 ILE A  61     5382   5229   4347   -236   -356    163       C  
-ATOM    496  N   VAL A  62      15.052  -7.250  24.524  1.00 34.71           N  
-ANISOU  496  N   VAL A  62     5012   4889   3286   -732   -419    149       N  
-ATOM    497  CA  VAL A  62      15.086  -5.817  24.812  1.00 37.92           C  
-ANISOU  497  CA  VAL A  62     5420   5340   3647   -818   -328     52       C  
-ATOM    498  C   VAL A  62      15.607  -5.120  23.572  1.00 34.07           C  
-ANISOU  498  C   VAL A  62     4756   4869   3318   -690   -312     15       C  
-ATOM    499  O   VAL A  62      16.746  -5.353  23.177  1.00 30.26           O  
-ANISOU  499  O   VAL A  62     4173   4426   2899   -619   -444     78       O  
-ATOM    500  CB  VAL A  62      16.041  -5.470  25.959  1.00 40.23           C  
-ANISOU  500  CB  VAL A  62     5810   5686   3789   -959   -461     91       C  
-ATOM    501  CG1 VAL A  62      16.106  -3.966  26.159  1.00 40.75           C  
-ANISOU  501  CG1 VAL A  62     5891   5776   3817  -1050   -365    -22       C  
-ATOM    502  CG2 VAL A  62      15.579  -6.113  27.227  1.00 44.62           C  
-ANISOU  502  CG2 VAL A  62     6573   6228   4151  -1112   -483    137       C  
-ATOM    503  N   ALA A  63      14.784  -4.271  22.962  1.00 28.57           N  
-ANISOU  503  N   ALA A  63     4019   4146   2689   -661   -151    -82       N  
-ATOM    504  CA  ALA A  63      15.208  -3.519  21.778  1.00 27.30           C  
-ANISOU  504  CA  ALA A  63     3724   3992   2657   -564   -130   -109       C  
-ATOM    505  C   ALA A  63      15.751  -2.162  22.221  1.00 29.13           C  
-ANISOU  505  C   ALA A  63     3988   4243   2839   -669   -115   -164       C  
-ATOM    506  O   ALA A  63      15.056  -1.382  22.877  1.00 29.59           O  
-ANISOU  506  O   ALA A  63     4150   4262   2830   -758     -5   -249       O  
-ATOM    507  CB  ALA A  63      14.055  -3.350  20.800  1.00 27.80           C  
-ANISOU  507  CB  ALA A  63     3734   4003   2825   -473      0   -164       C  
-ATOM    508  N   LEU A  64      17.008  -1.892  21.879  1.00 24.60           N  
-ANISOU  508  N   LEU A  64     3324   3726   2298   -666   -220   -121       N  
-ATOM    509  CA  LEU A  64      17.661  -0.653  22.278  1.00 27.28           C  
-ANISOU  509  CA  LEU A  64     3694   4084   2588   -791   -230   -163       C  
-ATOM    510  C   LEU A  64      17.797   0.285  21.065  1.00 27.80           C  
-ANISOU  510  C   LEU A  64     3667   4126   2770   -734   -158   -194       C  
-ATOM    511  O   LEU A  64      18.538  -0.004  20.126  1.00 26.63           O  
-ANISOU  511  O   LEU A  64     3379   4032   2709   -655   -206   -140       O  
-ATOM    512  CB  LEU A  64      19.026  -0.979  22.875  1.00 31.36           C  
-ANISOU  512  CB  LEU A  64     4168   4695   3051   -865   -417    -81       C  
-ATOM    513  CG  LEU A  64      19.883   0.141  23.457  1.00 36.03           C  
-ANISOU  513  CG  LEU A  64     4794   5326   3571  -1036   -476   -108       C  
-ATOM    514  CD1 LEU A  64      19.158   0.868  24.593  1.00 38.00           C  
-ANISOU  514  CD1 LEU A  64     5266   5510   3662  -1192   -397   -203       C  
-ATOM    515  CD2 LEU A  64      21.202  -0.430  23.962  1.00 39.19           C  
-ANISOU  515  CD2 LEU A  64     5105   5839   3946  -1084   -693     -4       C  
-ATOM    516  N   CYS A  65      17.076   1.405  21.084  1.00 27.57           N  
-ANISOU  516  N   CYS A  65     3726   4009   2739   -774    -37   -283       N  
-ATOM    517  CA  CYS A  65      17.091   2.352  19.975  1.00 25.75           C  
-ANISOU  517  CA  CYS A  65     3447   3730   2608   -731     23   -301       C  
-ATOM    518  C   CYS A  65      18.256   3.333  20.102  1.00 23.97           C  
-ANISOU  518  C   CYS A  65     3225   3531   2352   -869    -34   -298       C  
-ATOM    519  O   CYS A  65      18.387   4.000  21.123  1.00 25.94           O  
-ANISOU  519  O   CYS A  65     3599   3753   2505  -1011    -41   -354       O  
-ATOM    520  CB  CYS A  65      15.786   3.148  19.963  1.00 29.40           C  
-ANISOU  520  CB  CYS A  65     4003   4063   3104   -698    164   -390       C  
-ATOM    521  SG  CYS A  65      15.756   4.446  18.689  1.00 28.02           S  
-ANISOU  521  SG  CYS A  65     3814   3791   3041   -655    214   -397       S  
-ATOM    522  N   VAL A  66      19.101   3.436  19.076  1.00 25.02           N  
-ANISOU  522  N   VAL A  66     3229   3720   2556   -845    -69   -241       N  
-ATOM    523  CA  VAL A  66      20.176   4.433  19.121  1.00 25.41           C  
-ANISOU  523  CA  VAL A  66     3270   3798   2585  -1000   -113   -236       C  
-ATOM    524  C   VAL A  66      19.708   5.753  18.494  1.00 30.51           C  
-ANISOU  524  C   VAL A  66     4014   4308   3270  -1027    -14   -282       C  
-ATOM    525  O   VAL A  66      19.659   5.884  17.270  1.00 25.00           O  
-ANISOU  525  O   VAL A  66     3253   3596   2648   -951     28   -243       O  
-ATOM    526  CB  VAL A  66      21.469   3.953  18.416  1.00 30.32           C  
-ANISOU  526  CB  VAL A  66     3688   4568   3263   -992   -191   -152       C  
-ATOM    527  CG1 VAL A  66      22.588   4.943  18.667  1.00 32.08           C  
-ANISOU  527  CG1 VAL A  66     3892   4840   3457  -1190   -247   -146       C  
-ATOM    528  CG2 VAL A  66      21.884   2.565  18.920  1.00 30.64           C  
-ANISOU  528  CG2 VAL A  66     3625   4717   3299   -918   -299    -98       C  
-ATOM    529  N   LEU A  67      19.362   6.710  19.356  1.00 28.98           N  
-ANISOU  529  N   LEU A  67     3992   4003   3015  -1137     21   -365       N  
-ATOM    530  CA  LEU A  67      18.895   8.040  18.959  1.00 27.02           C  
-ANISOU  530  CA  LEU A  67     3873   3586   2808  -1163    105   -417       C  
-ATOM    531  C   LEU A  67      20.050   8.855  18.393  1.00 29.89           C  
-ANISOU  531  C   LEU A  67     4208   3971   3177  -1309     58   -368       C  
-ATOM    532  O   LEU A  67      21.204   8.576  18.732  1.00 31.73           O  
-ANISOU  532  O   LEU A  67     4345   4350   3363  -1433    -40   -327       O  
-ATOM    533  CB  LEU A  67      18.325   8.749  20.193  1.00 26.02           C  
-ANISOU  533  CB  LEU A  67     3947   3337   2605  -1247    160   -539       C  
-ATOM    534  CG  LEU A  67      17.074   8.087  20.745  1.00 28.51           C  
-ANISOU  534  CG  LEU A  67     4294   3624   2915  -1120    246   -600       C  
-ATOM    535  CD1 LEU A  67      16.631   8.724  22.060  1.00 28.89           C  
-ANISOU  535  CD1 LEU A  67     4543   3576   2860  -1224    321   -736       C  
-ATOM    536  CD2 LEU A  67      15.961   8.120  19.709  1.00 26.56           C  
-ANISOU  536  CD2 LEU A  67     3996   3284   2810   -923    332   -592       C  
-ATOM    537  N   LYS A  68      19.767   9.854  17.546  1.00 28.86           N  
-ANISOU  537  N   LYS A  68     4157   3701   3107  -1305    116   -363       N  
-ATOM    538  CA  LYS A  68      18.409  10.183  17.095  1.00 26.76           C  
-ANISOU  538  CA  LYS A  68     3982   3266   2921  -1141    206   -397       C  
-ATOM    539  C   LYS A  68      18.056   9.431  15.831  1.00 28.61           C  
-ANISOU  539  C   LYS A  68     4083   3559   3227   -977    211   -311       C  
-ATOM    540  O   LYS A  68      16.889   9.085  15.602  1.00 25.96           O  
-ANISOU  540  O   LYS A  68     3748   3163   2954   -812    253   -328       O  
-ATOM    541  CB  LYS A  68      18.296  11.679  16.800  1.00 27.05           C  
-ANISOU  541  CB  LYS A  68     4192   3094   2990  -1215    240   -420       C  
-ATOM    542  CG  LYS A  68      18.362  12.618  18.000  1.00 28.68           C  
-ANISOU  542  CG  LYS A  68     4592   3173   3133  -1361    259   -537       C  
-ATOM    543  CD  LYS A  68      18.368  14.049  17.463  1.00 31.53           C  
-ANISOU  543  CD  LYS A  68     5123   3313   3542  -1429    280   -536       C  
-ATOM    544  CE  LYS A  68      18.528  15.095  18.519  1.00 40.91           C  
-ANISOU  544  CE  LYS A  68     6533   4345   4667  -1593    300   -657       C  
-ATOM    545  NZ  LYS A  68      18.287  16.416  17.870  1.00 42.88           N  
-ANISOU  545  NZ  LYS A  68     6963   4335   4996  -1605    325   -650       N  
-ATOM    546  N   GLY A  69      19.074   9.181  15.008  1.00 26.17           N  
-ANISOU  546  N   GLY A  69     3659   3377   2908  -1034    172   -225       N  
-ATOM    547  CA  GLY A  69      18.892   8.680  13.654  1.00 23.46           C  
-ANISOU  547  CA  GLY A  69     3229   3077   2607   -919    186   -148       C  
-ATOM    548  C   GLY A  69      18.256   7.304  13.577  1.00 24.57           C  
-ANISOU  548  C   GLY A  69     3266   3300   2769   -748    184   -149       C  
-ATOM    549  O   GLY A  69      17.649   6.935  12.567  1.00 25.17           O  
-ANISOU  549  O   GLY A  69     3320   3363   2880   -631    199   -110       O  
-ATOM    550  N   GLY A  70      18.385   6.527  14.641  1.00 21.95           N  
-ANISOU  550  N   GLY A  70     2887   3048   2404   -748    156   -187       N  
-ATOM    551  CA  GLY A  70      17.788   5.200  14.625  1.00 22.42           C  
-ANISOU  551  CA  GLY A  70     2870   3169   2480   -605    149   -184       C  
-ATOM    552  C   GLY A  70      16.280   5.147  14.854  1.00 23.64           C  
-ANISOU  552  C   GLY A  70     3095   3211   2676   -496    197   -233       C  
-ATOM    553  O   GLY A  70      15.682   4.071  14.731  1.00 22.33           O  
-ANISOU  553  O   GLY A  70     2871   3085   2527   -392    193   -225       O  
-ATOM    554  N   TYR A  71      15.651   6.273  15.188  1.00 23.52           N  
-ANISOU  554  N   TYR A  71     3196   3052   2687   -518    245   -286       N  
-ATOM    555  CA  TYR A  71      14.288   6.210  15.738  1.00 25.86           C  
-ANISOU  555  CA  TYR A  71     3532   3263   3029   -426    307   -355       C  
-ATOM    556  C   TYR A  71      13.235   5.666  14.760  1.00 21.87           C  
-ANISOU  556  C   TYR A  71     2954   2743   2613   -272    309   -318       C  
-ATOM    557  O   TYR A  71      12.316   4.948  15.167  1.00 23.98           O  
-ANISOU  557  O   TYR A  71     3180   3027   2905   -203    340   -352       O  
-ATOM    558  CB  TYR A  71      13.854   7.556  16.350  1.00 26.17           C  
-ANISOU  558  CB  TYR A  71     3710   3139   3094   -465    374   -440       C  
-ATOM    559  CG  TYR A  71      12.933   8.398  15.486  1.00 27.52           C  
-ANISOU  559  CG  TYR A  71     3914   3154   3390   -349    399   -430       C  
-ATOM    560  CD1 TYR A  71      11.559   8.173  15.466  1.00 26.33           C  
-ANISOU  560  CD1 TYR A  71     3714   2951   3340   -201    449   -466       C  
-ATOM    561  CD2 TYR A  71      13.436   9.440  14.717  1.00 25.96           C  
-ANISOU  561  CD2 TYR A  71     3794   2857   3211   -397    365   -378       C  
-ATOM    562  CE1 TYR A  71      10.722   8.937  14.682  1.00 27.90           C  
-ANISOU  562  CE1 TYR A  71     3924   3007   3670    -82    445   -445       C  
-ATOM    563  CE2 TYR A  71      12.611  10.209  13.923  1.00 29.00           C  
-ANISOU  563  CE2 TYR A  71     4225   3084   3710   -287    360   -350       C  
-ATOM    564  CZ  TYR A  71      11.255   9.953  13.908  1.00 31.91           C  
-ANISOU  564  CZ  TYR A  71     4528   3405   4191   -119    391   -382       C  
-ATOM    565  OH  TYR A  71      10.428  10.722  13.119  1.00 32.79           O  
-ANISOU  565  OH  TYR A  71     4669   3358   4433      3    361   -341       O  
-ATOM    566  N   LYS A  72      13.352   6.013  13.481  1.00 22.38           N  
-ANISOU  566  N   LYS A  72     3011   2780   2714   -237    271   -246       N  
-ATOM    567  CA  LYS A  72      12.397   5.532  12.474  1.00 23.03           C  
-ANISOU  567  CA  LYS A  72     3037   2852   2863   -112    245   -202       C  
-ATOM    568  C   LYS A  72      12.523   4.034  12.210  1.00 25.35           C  
-ANISOU  568  C   LYS A  72     3236   3280   3115    -79    214   -177       C  
-ATOM    569  O   LYS A  72      11.534   3.302  12.258  1.00 25.33           O  
-ANISOU  569  O   LYS A  72     3184   3284   3154     -3    214   -192       O  
-ATOM    570  CB  LYS A  72      12.552   6.304  11.154  1.00 26.87           C  
-ANISOU  570  CB  LYS A  72     3572   3273   3366   -107    199   -120       C  
-ATOM    571  CG  LYS A  72      11.754   7.594  11.105  1.00 36.92           C  
-ANISOU  571  CG  LYS A  72     4931   4361   4736    -59    204   -128       C  
-ATOM    572  CD  LYS A  72      10.260   7.310  11.152  1.00 44.86           C  
-ANISOU  572  CD  LYS A  72     5866   5319   5859     88    204   -156       C  
-ATOM    573  CE  LYS A  72       9.778   6.692   9.852  1.00 49.93           C  
-ANISOU  573  CE  LYS A  72     6452   6006   6513    157    112    -66       C  
-ATOM    574  NZ  LYS A  72       8.423   6.081   9.989  1.00 51.61           N  
-ANISOU  574  NZ  LYS A  72     6552   6229   6829    271    103    -94       N  
-ATOM    575  N   PHE A  73      13.738   3.588  11.905  1.00 20.75           N  
-ANISOU  575  N   PHE A  73     2625   2800   2460   -136    190   -141       N  
-ATOM    576  CA  PHE A  73      14.013   2.174  11.703  1.00 19.77           C  
-ANISOU  576  CA  PHE A  73     2426   2783   2303    -96    164   -127       C  
-ATOM    577  C   PHE A  73      13.567   1.365  12.916  1.00 21.76           C  
-ANISOU  577  C   PHE A  73     2664   3053   2550    -87    171   -172       C  
-ATOM    578  O   PHE A  73      12.945   0.305  12.784  1.00 22.96           O  
-ANISOU  578  O   PHE A  73     2786   3223   2713    -27    155   -169       O  
-ATOM    579  CB  PHE A  73      15.511   1.977  11.408  1.00 22.76           C  
-ANISOU  579  CB  PHE A  73     2756   3264   2626   -153    155    -98       C  
-ATOM    580  CG  PHE A  73      15.899   0.556  11.085  1.00 22.83           C  
-ANISOU  580  CG  PHE A  73     2692   3364   2618    -88    136    -90       C  
-ATOM    581  CD1 PHE A  73      15.189  -0.192  10.152  1.00 22.30           C  
-ANISOU  581  CD1 PHE A  73     2634   3284   2557     -4    128    -83       C  
-ATOM    582  CD2 PHE A  73      17.006  -0.018  11.684  1.00 21.49           C  
-ANISOU  582  CD2 PHE A  73     2450   3284   2430   -109    114    -89       C  
-ATOM    583  CE1 PHE A  73      15.579  -1.510   9.848  1.00 22.68           C  
-ANISOU  583  CE1 PHE A  73     2638   3390   2589     59    117    -89       C  
-ATOM    584  CE2 PHE A  73      17.395  -1.334  11.389  1.00 22.21           C  
-ANISOU  584  CE2 PHE A  73     2479   3435   2526    -25     96    -85       C  
-ATOM    585  CZ  PHE A  73      16.687  -2.069  10.470  1.00 23.71           C  
-ANISOU  585  CZ  PHE A  73     2697   3593   2717     59    106    -92       C  
-ATOM    586  N   PHE A  74      13.860   1.887  14.098  1.00 19.78           N  
-ANISOU  586  N   PHE A  74     2456   2791   2270   -167    192   -211       N  
-ATOM    587  CA  PHE A  74      13.454   1.255  15.351  1.00 21.07           C  
-ANISOU  587  CA  PHE A  74     2639   2968   2397   -191    206   -251       C  
-ATOM    588  C   PHE A  74      11.931   1.110  15.443  1.00 23.55           C  
-ANISOU  588  C   PHE A  74     2952   3224   2773   -129    264   -289       C  
-ATOM    589  O   PHE A  74      11.441   0.019  15.694  1.00 21.64           O  
-ANISOU  589  O   PHE A  74     2686   3016   2520   -111    257   -284       O  
-ATOM    590  CB  PHE A  74      14.008   2.066  16.518  1.00 20.56           C  
-ANISOU  590  CB  PHE A  74     2649   2892   2269   -309    222   -295       C  
-ATOM    591  CG  PHE A  74      13.627   1.548  17.885  1.00 23.16           C  
-ANISOU  591  CG  PHE A  74     3036   3237   2526   -365    244   -337       C  
-ATOM    592  CD1 PHE A  74      14.287   0.459  18.449  1.00 28.82           C  
-ANISOU  592  CD1 PHE A  74     3741   4040   3170   -399    164   -291       C  
-ATOM    593  CD2 PHE A  74      12.662   2.201  18.632  1.00 26.05           C  
-ANISOU  593  CD2 PHE A  74     3478   3528   2892   -389    347   -423       C  
-ATOM    594  CE1 PHE A  74      13.959   0.011  19.728  1.00 27.60           C  
-ANISOU  594  CE1 PHE A  74     3670   3895   2922   -476    176   -315       C  
-ATOM    595  CE2 PHE A  74      12.324   1.756  19.921  1.00 31.66           C  
-ANISOU  595  CE2 PHE A  74     4261   4262   3507   -467    389   -467       C  
-ATOM    596  CZ  PHE A  74      12.979   0.659  20.461  1.00 28.03           C  
-ANISOU  596  CZ  PHE A  74     3809   3889   2952   -522    296   -405       C  
-ATOM    597  N   ALA A  75      11.185   2.196  15.221  1.00 22.14           N  
-ANISOU  597  N   ALA A  75     2792   2952   2668    -96    316   -324       N  
-ATOM    598  CA  ALA A  75       9.731   2.144  15.371  1.00 23.94           C  
-ANISOU  598  CA  ALA A  75     2981   3134   2980    -30    377   -367       C  
-ATOM    599  C   ALA A  75       9.153   1.134  14.384  1.00 25.15           C  
-ANISOU  599  C   ALA A  75     3050   3327   3177     41    316   -311       C  
-ATOM    600  O   ALA A  75       8.282   0.309  14.726  1.00 24.30           O  
-ANISOU  600  O   ALA A  75     2895   3248   3089     47    341   -328       O  
-ATOM    601  CB  ALA A  75       9.105   3.538  15.164  1.00 24.67           C  
-ANISOU  601  CB  ALA A  75     3094   3103   3176     25    425   -405       C  
-ATOM    602  N   ASP A  76       9.656   1.179  13.161  1.00 22.09           N  
-ANISOU  602  N   ASP A  76     2658   2945   2790     73    241   -247       N  
-ATOM    603  CA  ASP A  76       9.147   0.321  12.092  1.00 21.86           C  
-ANISOU  603  CA  ASP A  76     2579   2943   2783    128    175   -201       C  
-ATOM    604  C   ASP A  76       9.529  -1.143  12.256  1.00 25.29           C  
-ANISOU  604  C   ASP A  76     3009   3451   3148    105    148   -191       C  
-ATOM    605  O   ASP A  76       8.683  -2.041  12.113  1.00 22.70           O  
-ANISOU  605  O   ASP A  76     2647   3133   2844    119    128   -191       O  
-ATOM    606  CB  ASP A  76       9.613   0.851  10.732  1.00 24.06           C  
-ANISOU  606  CB  ASP A  76     2885   3204   3051    151    113   -140       C  
-ATOM    607  CG  ASP A  76       8.891   2.119  10.322  1.00 27.14           C  
-ANISOU  607  CG  ASP A  76     3286   3494   3534    198    102   -125       C  
-ATOM    608  OD1 ASP A  76       7.837   2.415  10.915  1.00 29.23           O  
-ANISOU  608  OD1 ASP A  76     3501   3709   3897    243    139   -167       O  
-ATOM    609  OD2 ASP A  76       9.369   2.807   9.395  1.00 28.30           O  
-ANISOU  609  OD2 ASP A  76     3490   3606   3656    191     59    -68       O  
-ATOM    610  N   LEU A  77      10.801  -1.392  12.556  1.00 20.51           N  
-ANISOU  610  N   LEU A  77     2434   2891   2468     68    140   -181       N  
-ATOM    611  CA  LEU A  77      11.246  -2.763  12.805  1.00 20.00           C  
-ANISOU  611  CA  LEU A  77     2373   2873   2353     66    106   -169       C  
-ATOM    612  C   LEU A  77      10.453  -3.364  13.976  1.00 19.10           C  
-ANISOU  612  C   LEU A  77     2274   2751   2233     22    133   -193       C  
-ATOM    613  O   LEU A  77       9.997  -4.513  13.904  1.00 19.88           O  
-ANISOU  613  O   LEU A  77     2378   2848   2328     26    105   -181       O  
-ATOM    614  CB  LEU A  77      12.757  -2.803  13.096  1.00 21.22           C  
-ANISOU  614  CB  LEU A  77     2528   3080   2453     43     85   -152       C  
-ATOM    615  CG  LEU A  77      13.390  -4.153  13.456  1.00 24.74           C  
-ANISOU  615  CG  LEU A  77     2976   3559   2867     63     34   -131       C  
-ATOM    616  CD1 LEU A  77      13.288  -5.128  12.306  1.00 24.18           C  
-ANISOU  616  CD1 LEU A  77     2901   3477   2810    140     10   -125       C  
-ATOM    617  CD2 LEU A  77      14.858  -3.978  13.859  1.00 26.66           C  
-ANISOU  617  CD2 LEU A  77     3182   3864   3084     44      2   -111       C  
-ATOM    618  N   LEU A  78      10.257  -2.597  15.041  1.00 18.84           N  
-ANISOU  618  N   LEU A  78     2264   2706   2189    -34    197   -232       N  
-ATOM    619  CA ALEU A  78       9.499  -3.128  16.175  0.72 22.44           C  
-ANISOU  619  CA ALEU A  78     2745   3164   2615    -97    248   -259       C  
-ATOM    620  CA BLEU A  78       9.487  -3.085  16.187  0.28 22.37           C  
-ANISOU  620  CA BLEU A  78     2737   3155   2608    -97    251   -261       C  
-ATOM    621  C   LEU A  78       8.045  -3.371  15.795  1.00 23.63           C  
-ANISOU  621  C   LEU A  78     2828   3298   2851    -72    287   -278       C  
-ATOM    622  O   LEU A  78       7.432  -4.332  16.264  1.00 22.55           O  
-ANISOU  622  O   LEU A  78     2698   3176   2694   -123    301   -274       O  
-ATOM    623  CB ALEU A  78       9.590  -2.223  17.407  0.72 23.19           C  
-ANISOU  623  CB ALEU A  78     2899   3254   2660   -174    327   -315       C  
-ATOM    624  CB BLEU A  78       9.509  -2.083  17.342  0.28 23.73           C  
-ANISOU  624  CB BLEU A  78     2961   3316   2740   -167    335   -321       C  
-ATOM    625  CG ALEU A  78      10.559  -2.727  18.466  0.72 27.52           C  
-ANISOU  625  CG ALEU A  78     3533   3841   3081   -264    281   -290       C  
-ATOM    626  CG BLEU A  78      10.676  -2.162  18.315  0.28 27.68           C  
-ANISOU  626  CG BLEU A  78     3546   3850   3120   -254    294   -306       C  
-ATOM    627  CD1ALEU A  78      11.963  -2.773  17.875  0.72 27.08           C  
-ANISOU  627  CD1ALEU A  78     3456   3816   3018   -229    174   -234       C  
-ATOM    628  CD1BLEU A  78      10.323  -1.456  19.604  0.28 31.52           C  
-ANISOU  628  CD1BLEU A  78     4116   4323   3538   -352    394   -381       C  
-ATOM    629  CD2ALEU A  78      10.528  -1.834  19.691  0.72 32.44           C  
-ANISOU  629  CD2ALEU A  78     4241   4455   3629   -364    362   -358       C  
-ATOM    630  CD2BLEU A  78      11.032  -3.593  18.598  0.28 26.45           C  
-ANISOU  630  CD2BLEU A  78     3419   3729   2904   -273    211   -241       C  
-ATOM    631  N   ASP A  79       7.491  -2.517  14.944  1.00 20.71           N  
-ANISOU  631  N   ASP A  79     2393   2897   2579     -2    292   -288       N  
-ATOM    632  CA  ASP A  79       6.105  -2.729  14.523  1.00 22.41           C  
-ANISOU  632  CA  ASP A  79     2511   3108   2894     26    304   -297       C  
-ATOM    633  C   ASP A  79       5.961  -4.042  13.759  1.00 20.98           C  
-ANISOU  633  C   ASP A  79     2327   2949   2696     18    212   -248       C  
-ATOM    634  O   ASP A  79       4.965  -4.760  13.911  1.00 21.90           O  
-ANISOU  634  O   ASP A  79     2392   3082   2846    -24    223   -254       O  
-ATOM    635  CB  ASP A  79       5.595  -1.557  13.680  1.00 27.90           C  
-ANISOU  635  CB  ASP A  79     3141   3755   3706    117    290   -298       C  
-ATOM    636  CG  ASP A  79       5.073  -0.420  14.526  1.00 32.20           C  
-ANISOU  636  CG  ASP A  79     3660   4255   4321    136    407   -371       C  
-ATOM    637  OD1 ASP A  79       4.966  -0.592  15.757  1.00 32.13           O  
-ANISOU  637  OD1 ASP A  79     3679   4269   4260     65    515   -430       O  
-ATOM    638  OD2 ASP A  79       4.748   0.638  13.956  1.00 32.29           O  
-ANISOU  638  OD2 ASP A  79     3636   4198   4434    221    393   -370       O  
-ATOM    639  N   TYR A  80       6.943  -4.355  12.925  1.00 19.31           N  
-ANISOU  639  N   TYR A  80     2172   2736   2431     51    131   -209       N  
-ATOM    640  CA  TYR A  80       6.911  -5.628  12.193  1.00 19.11           C  
-ANISOU  640  CA  TYR A  80     2174   2711   2376     47     52   -181       C  
-ATOM    641  C   TYR A  80       7.100  -6.820  13.121  1.00 23.96           C  
-ANISOU  641  C   TYR A  80     2853   3324   2928    -18     59   -177       C  
-ATOM    642  O   TYR A  80       6.465  -7.863  12.948  1.00 21.45           O  
-ANISOU  642  O   TYR A  80     2550   2988   2611    -60     24   -167       O  
-ATOM    643  CB  TYR A  80       7.967  -5.668  11.069  1.00 18.82           C  
-ANISOU  643  CB  TYR A  80     2186   2673   2290    104     -7   -158       C  
-ATOM    644  CG  TYR A  80       7.540  -4.928   9.812  1.00 21.36           C  
-ANISOU  644  CG  TYR A  80     2480   2987   2648    144    -52   -140       C  
-ATOM    645  CD1 TYR A  80       6.532  -5.437   9.001  1.00 24.65           C  
-ANISOU  645  CD1 TYR A  80     2876   3397   3093    134   -124   -129       C  
-ATOM    646  CD2 TYR A  80       8.156  -3.738   9.429  1.00 20.33           C  
-ANISOU  646  CD2 TYR A  80     2357   2853   2515    174    -39   -125       C  
-ATOM    647  CE1 TYR A  80       6.132  -4.781   7.836  1.00 26.18           C  
-ANISOU  647  CE1 TYR A  80     3058   3584   3306    162   -195    -96       C  
-ATOM    648  CE2 TYR A  80       7.765  -3.070   8.266  1.00 24.00           C  
-ANISOU  648  CE2 TYR A  80     2823   3299   2999    201    -98    -89       C  
-ATOM    649  CZ  TYR A  80       6.746  -3.599   7.487  1.00 24.30           C  
-ANISOU  649  CZ  TYR A  80     2840   3332   3059    199   -181    -72       C  
-ATOM    650  OH  TYR A  80       6.340  -2.963   6.338  1.00 23.37           O  
-ANISOU  650  OH  TYR A  80     2735   3196   2947    218   -267    -22       O  
-ATOM    651  N   ILE A  81       8.002  -6.687  14.083  1.00 21.07           N  
-ANISOU  651  N   ILE A  81     2539   2967   2501    -37     86   -174       N  
-ATOM    652  CA  ILE A  81       8.198  -7.744  15.079  1.00 20.77           C  
-ANISOU  652  CA  ILE A  81     2581   2917   2394   -105     75   -151       C  
-ATOM    653  C   ILE A  81       6.920  -7.999  15.866  1.00 24.27           C  
-ANISOU  653  C   ILE A  81     3011   3365   2844   -207    146   -168       C  
-ATOM    654  O   ILE A  81       6.542  -9.148  16.087  1.00 24.40           O  
-ANISOU  654  O   ILE A  81     3083   3355   2832   -273    119   -141       O  
-ATOM    655  CB  ILE A  81       9.360  -7.407  16.040  1.00 25.31           C  
-ANISOU  655  CB  ILE A  81     3209   3512   2897   -120     71   -137       C  
-ATOM    656  CG1 ILE A  81      10.691  -7.494  15.291  1.00 26.29           C  
-ANISOU  656  CG1 ILE A  81     3325   3641   3021    -29     -2   -113       C  
-ATOM    657  CG2 ILE A  81       9.374  -8.382  17.220  1.00 24.76           C  
-ANISOU  657  CG2 ILE A  81     3239   3425   2745   -210     51   -100       C  
-ATOM    658  CD1 ILE A  81      11.890  -6.995  16.109  1.00 27.49           C  
-ANISOU  658  CD1 ILE A  81     3488   3832   3124    -47    -24    -96       C  
-ATOM    659  N   LYS A  82       6.246  -6.923  16.274  1.00 21.37           N  
-ANISOU  659  N   LYS A  82     2570   3028   2521   -222    246   -218       N  
-ATOM    660  CA  LYS A  82       4.989  -7.031  17.006  1.00 19.32           C  
-ANISOU  660  CA  LYS A  82     2263   2794   2285   -314    349   -252       C  
-ATOM    661  C   LYS A  82       3.912  -7.753  16.199  1.00 23.63           C  
-ANISOU  661  C   LYS A  82     2724   3341   2913   -330    312   -238       C  
-ATOM    662  O   LYS A  82       3.143  -8.541  16.738  1.00 25.65           O  
-ANISOU  662  O   LYS A  82     2981   3612   3153   -444    354   -234       O  
-ATOM    663  CB  LYS A  82       4.504  -5.643  17.412  1.00 22.82           C  
-ANISOU  663  CB  LYS A  82     2626   3256   2790   -287    472   -325       C  
-ATOM    664  CG  LYS A  82       5.241  -5.097  18.635  1.00 28.24           C  
-ANISOU  664  CG  LYS A  82     3421   3946   3364   -343    541   -357       C  
-ATOM    665  CD  LYS A  82       5.355  -3.588  18.608  1.00 33.21           C  
-ANISOU  665  CD  LYS A  82     4017   4552   4051   -272    605   -422       C  
-ATOM    666  CE  LYS A  82       3.999  -2.922  18.620  1.00 39.23           C  
-ANISOU  666  CE  LYS A  82     4647   5314   4947   -235    732   -497       C  
-ATOM    667  NZ  LYS A  82       4.140  -1.425  18.588  1.00 40.92           N  
-ANISOU  667  NZ  LYS A  82     4854   5468   5226   -150    787   -561       N  
-ATOM    668  N   ALA A  83       3.854  -7.469  14.903  1.00 19.60           N  
-ANISOU  668  N   ALA A  83     2149   2818   2479   -236    229   -229       N  
-ATOM    669  CA  ALA A  83       2.902  -8.144  14.020  1.00 21.94           C  
-ANISOU  669  CA  ALA A  83     2376   3118   2842   -262    160   -213       C  
-ATOM    670  C   ALA A  83       3.159  -9.649  14.036  1.00 24.23           C  
-ANISOU  670  C   ALA A  83     2793   3365   3047   -343     93   -176       C  
-ATOM    671  O   ALA A  83       2.222 -10.457  14.086  1.00 27.44           O  
-ANISOU  671  O   ALA A  83     3176   3776   3475   -451     87   -169       O  
-ATOM    672  CB  ALA A  83       3.014  -7.601  12.610  1.00 21.61           C  
-ANISOU  672  CB  ALA A  83     2294   3065   2853   -157     60   -199       C  
-ATOM    673  N   LEU A  84       4.433 -10.032  13.987  1.00 20.28           N  
-ANISOU  673  N   LEU A  84     2426   2816   2462   -292     41   -153       N  
-ATOM    674  CA  LEU A  84       4.779 -11.449  14.045  1.00 22.74           C  
-ANISOU  674  CA  LEU A  84     2877   3057   2707   -341    -27   -119       C  
-ATOM    675  C   LEU A  84       4.365 -12.039  15.387  1.00 29.51           C  
-ANISOU  675  C   LEU A  84     3792   3909   3510   -480     33    -96       C  
-ATOM    676  O   LEU A  84       3.902 -13.177  15.470  1.00 27.67           O  
-ANISOU  676  O   LEU A  84     3637   3622   3253   -582     -2    -67       O  
-ATOM    677  CB  LEU A  84       6.281 -11.652  13.842  1.00 24.18           C  
-ANISOU  677  CB  LEU A  84     3159   3195   2835   -234    -83   -103       C  
-ATOM    678  CG  LEU A  84       6.857 -11.314  12.473  1.00 25.58           C  
-ANISOU  678  CG  LEU A  84     3315   3372   3033   -116   -131   -125       C  
-ATOM    679  CD1 LEU A  84       8.360 -11.413  12.521  1.00 24.30           C  
-ANISOU  679  CD1 LEU A  84     3209   3192   2832    -19   -150   -115       C  
-ATOM    680  CD2 LEU A  84       6.303 -12.265  11.423  1.00 27.59           C  
-ANISOU  680  CD2 LEU A  84     3622   3571   3291   -140   -202   -137       C  
-ATOM    681  N   ASN A  85       4.530 -11.261  16.447  1.00 25.75           N  
-ANISOU  681  N   ASN A  85     3300   3484   3001   -501    126   -107       N  
-ATOM    682  CA  ASN A  85       4.204 -11.758  17.775  1.00 25.30           C  
-ANISOU  682  CA  ASN A  85     3325   3430   2857   -650    194    -84       C  
-ATOM    683  C   ASN A  85       2.714 -11.939  18.040  1.00 33.11           C  
-ANISOU  683  C   ASN A  85     4219   4469   3891   -789    294   -108       C  
-ATOM    684  O   ASN A  85       2.336 -12.722  18.908  1.00 37.97           O  
-ANISOU  684  O   ASN A  85     4926   5073   4426   -946    335    -74       O  
-ATOM    685  CB  ASN A  85       4.844 -10.867  18.852  1.00 34.19           C  
-ANISOU  685  CB  ASN A  85     4486   4599   3907   -650    266    -99       C  
-ATOM    686  CG  ASN A  85       6.240 -11.332  19.235  1.00 45.52           C  
-ANISOU  686  CG  ASN A  85     6068   5979   5247   -613    154    -35       C  
-ATOM    687  OD1 ASN A  85       6.400 -12.287  20.004  1.00 50.99           O  
-ANISOU  687  OD1 ASN A  85     6904   6625   5845   -708    110     31       O  
-ATOM    688  ND2 ASN A  85       7.254 -10.665  18.704  1.00 53.52           N  
-ANISOU  688  ND2 ASN A  85     7043   7002   6291   -479    100    -46       N  
-ATOM    689  N   ARG A  86       1.851 -11.241  17.306  1.00 31.15           N  
-ANISOU  689  N   ARG A  86     3784   4278   3772   -742    329   -158       N  
-ATOM    690  CA  ARG A  86       0.416 -11.372  17.597  1.00 36.61           C  
-ANISOU  690  CA  ARG A  86     4340   5040   4532   -871    431   -185       C  
-ATOM    691  C   ARG A  86      -0.354 -12.236  16.590  1.00 39.78           C  
-ANISOU  691  C   ARG A  86     4684   5425   5007   -928    327   -160       C  
-ATOM    692  O   ARG A  86      -1.552 -12.501  16.758  1.00 43.62           O  
-ANISOU  692  O   ARG A  86     5042   5975   5557  -1058    391   -172       O  
-ATOM    693  CB  ARG A  86      -0.252 -10.001  17.766  1.00 35.67           C  
-ANISOU  693  CB  ARG A  86     4022   5006   4526   -802    565   -263       C  
-ATOM    694  CG  ARG A  86      -0.257  -9.171  16.501  1.00 31.24           C  
-ANISOU  694  CG  ARG A  86     3335   4439   4095   -632    472   -277       C  
-ATOM    695  CD  ARG A  86      -0.969  -7.834  16.646  1.00 31.78           C  
-ANISOU  695  CD  ARG A  86     3211   4562   4301   -545    590   -348       C  
-ATOM    696  NE  ARG A  86      -0.867  -7.095  15.392  1.00 29.74           N  
-ANISOU  696  NE  ARG A  86     2874   4276   4148   -388    466   -333       N  
-ATOM    697  CZ  ARG A  86      -0.010  -6.109  15.168  1.00 32.09           C  
-ANISOU  697  CZ  ARG A  86     3230   4527   4436   -261    448   -342       C  
-ATOM    698  NH1 ARG A  86       0.805  -5.706  16.134  1.00 26.98           N  
-ANISOU  698  NH1 ARG A  86     2702   3861   3687   -269    541   -373       N  
-ATOM    699  NH2 ARG A  86       0.015  -5.514  13.981  1.00 31.77           N  
-ANISOU  699  NH2 ARG A  86     3135   4459   4477   -143    329   -313       N  
-ATOM    700  N   ASN A  87       0.326 -12.682  15.547  1.00 44.19           N  
-ANISOU  700  N   ASN A  87     7468   4672   4648  -1100   -470   -251       N  
-ATOM    701  CA  ASN A  87      -0.333 -13.483  14.528  1.00 55.45           C  
-ANISOU  701  CA  ASN A  87     8993   6158   5916  -1372   -453   -360       C  
-ATOM    702  C   ASN A  87       0.308 -14.859  14.518  1.00 61.70           C  
-ANISOU  702  C   ASN A  87     9626   6892   6923  -1284   -152   -781       C  
-ATOM    703  O   ASN A  87       0.451 -15.498  13.478  1.00 71.73           O  
-ANISOU  703  O   ASN A  87    10918   8292   8043  -1616     43  -1108       O  
-ATOM    704  CB  ASN A  87      -0.229 -12.805  13.164  1.00 62.64           C  
-ANISOU  704  CB  ASN A  87    10077   7349   6374  -1926   -505   -329       C  
-ATOM    705  CG  ASN A  87      -0.963 -11.465  13.109  1.00 62.79           C  
-ANISOU  705  CG  ASN A  87    10184   7338   6338  -2038   -887    168       C  
-ATOM    706  OD1 ASN A  87      -2.194 -11.408  13.183  1.00 61.69           O  
-ANISOU  706  OD1 ASN A  87    10069   7041   6329  -2004  -1147    458       O  
-ATOM    707  ND2 ASN A  87      -0.206 -10.386  12.957  1.00 59.76           N  
-ANISOU  707  ND2 ASN A  87     9807   7067   5832  -2183   -931    265       N  
-ATOM    708  N   SER A  88       0.678 -15.298  15.717  1.00 62.36           N  
-ANISOU  708  N   SER A  88     9513   6775   7405   -879   -129   -764       N  
-ATOM    709  CA ASER A  88       1.399 -16.547  15.895  0.47 64.86           C  
-ANISOU  709  CA ASER A  88     9577   6935   8131   -749     90  -1085       C  
-ATOM    710  CA BSER A  88       1.426 -16.532  15.911  0.53 64.20           C  
-ANISOU  710  CA BSER A  88     9491   6851   8050   -746     91  -1084       C  
-ATOM    711  C   SER A  88       0.907 -17.306  17.123  1.00 65.33           C  
-ANISOU  711  C   SER A  88     9476   6752   8593   -389    -74   -856       C  
-ATOM    712  O   SER A  88       0.905 -16.786  18.242  1.00 64.37           O  
-ANISOU  712  O   SER A  88     9327   6618   8511   -192   -240   -558       O  
-ATOM    713  CB ASER A  88       2.898 -16.273  15.999  0.47 63.72           C  
-ANISOU  713  CB ASER A  88     9271   6819   8121   -742    285  -1295       C  
-ATOM    714  CB BSER A  88       2.898 -16.199  16.116  0.53 61.35           C  
-ANISOU  714  CB BSER A  88     8971   6514   7823   -714    262  -1256       C  
-ATOM    715  OG ASER A  88       3.355 -15.577  14.849  0.47 62.96           O  
-ANISOU  715  OG ASER A  88     9326   6992   7604  -1138    441  -1512       O  
-ATOM    716  OG BSER A  88       3.047 -15.240  17.147  0.53 52.64           O  
-ANISOU  716  OG BSER A  88     7896   5434   6671   -514     77   -910       O  
-ATOM    717  N   ARG A  90       2.346 -18.673  20.317  1.00 59.41           N  
-ANISOU  717  N   ARG A  90     8019   5576   8976    204   -365   -369       N  
-ATOM    718  CA  ARG A  90       3.792 -18.570  20.156  1.00 57.77           C  
-ANISOU  718  CA  ARG A  90     7610   5316   9022    187   -207   -565       C  
-ATOM    719  C   ARG A  90       4.271 -17.113  20.129  1.00 60.98           C  
-ANISOU  719  C   ARG A  90     8225   5992   8951    105   -152   -540       C  
-ATOM    720  O   ARG A  90       4.403 -16.518  19.049  1.00 61.54           O  
-ANISOU  720  O   ARG A  90     8474   6204   8704    -69     37   -808       O  
-ATOM    721  CB  ARG A  90       4.228 -19.286  18.893  1.00 59.64           C  
-ANISOU  721  CB  ARG A  90     7717   5414   9530     68    102  -1088       C  
-ATOM    722  N   SER A  91       4.538 -16.543  21.306  1.00 53.54           N  
-ANISOU  722  N   SER A  91     7250   5143   7951    173   -325   -215       N  
-ATOM    723  CA  SER A  91       5.064 -15.175  21.382  1.00 54.85           C  
-ANISOU  723  CA  SER A  91     7563   5529   7748    108   -270   -203       C  
-ATOM    724  C   SER A  91       6.028 -14.958  22.551  1.00 55.98           C  
-ANISOU  724  C   SER A  91     7516   5714   8041    145   -377     26       C  
-ATOM    725  O   SER A  91       6.104 -15.760  23.484  1.00 53.81           O  
-ANISOU  725  O   SER A  91     7018   5343   8084    179   -572    289       O  
-ATOM    726  CB  SER A  91       3.937 -14.139  21.426  1.00 52.42           C  
-ANISOU  726  CB  SER A  91     7532   5392   6994     51   -344    -83       C  
-ATOM    727  OG  SER A  91       3.358 -14.051  22.713  1.00 53.26           O  
-ANISOU  727  OG  SER A  91     7596   5561   7077     87   -512    187       O  
-ATOM    728  N   ILE A  92       6.759 -13.849  22.479  1.00 52.24           N  
-ANISOU  728  N   ILE A  92     7125   5400   7324     92   -279    -37       N  
-ATOM    729  CA  ILE A  92       7.872 -13.574  23.380  1.00 48.48           C  
-ANISOU  729  CA  ILE A  92     6471   4979   6968     87   -343    127       C  
-ATOM    730  C   ILE A  92       7.768 -12.120  23.846  1.00 44.97           C  
-ANISOU  730  C   ILE A  92     6218   4804   6065      6   -331    194       C  
-ATOM    731  O   ILE A  92       7.549 -11.217  23.032  1.00 43.48           O  
-ANISOU  731  O   ILE A  92     6231   4685   5606    -29   -206     17       O  
-ATOM    732  CB  ILE A  92       9.222 -13.886  22.656  1.00 75.81           C  
-ANISOU  732  CB  ILE A  92     9738   8282  10786    109   -166   -135       C  
-ATOM    733  CG1 ILE A  92      10.153 -12.669  22.590  1.00 73.96           C  
-ANISOU  733  CG1 ILE A  92     9589   8232  10279     51    -50   -209       C  
-ATOM    734  CG2 ILE A  92       8.946 -14.415  21.243  1.00 76.69           C  
-ANISOU  734  CG2 ILE A  92     9900   8274  10964     72     63   -544       C  
-ATOM    735  CD1 ILE A  92      10.129 -11.935  21.248  1.00 71.75           C  
-ANISOU  735  CD1 ILE A  92     9545   8064   9654    -57    185   -548       C  
-ATOM    736  N   PRO A  93       7.868 -11.885  25.162  1.00 41.28           N  
-ANISOU  736  N   PRO A  93     5664   4496   5523    -80   -473    455       N  
-ATOM    737  CA  PRO A  93       7.709 -10.488  25.583  1.00 43.58           C  
-ANISOU  737  CA  PRO A  93     6096   5022   5442   -181   -401    418       C  
-ATOM    738  C   PRO A  93       8.852  -9.610  25.073  1.00 38.45           C  
-ANISOU  738  C   PRO A  93     5473   4410   4729   -166   -261    272       C  
-ATOM    739  O   PRO A  93       9.954 -10.103  24.838  1.00 40.10           O  
-ANISOU  739  O   PRO A  93     5537   4522   5178   -120   -243    259       O  
-ATOM    740  CB  PRO A  93       7.716 -10.569  27.112  1.00 47.79           C  
-ANISOU  740  CB  PRO A  93     6497   5774   5886   -376   -548    679       C  
-ATOM    741  CG  PRO A  93       8.389 -11.866  27.436  1.00 53.60           C  
-ANISOU  741  CG  PRO A  93     6993   6377   6995   -373   -753    947       C  
-ATOM    742  CD  PRO A  93       8.073 -12.803  26.296  1.00 49.47           C  
-ANISOU  742  CD  PRO A  93     6464   5534   6798   -162   -711    793       C  
-ATOM    743  N   MET A  94       8.584  -8.325  24.881  1.00 34.61           N  
-ANISOU  743  N   MET A  94     5132   4026   3992   -213   -167    157       N  
-ATOM    744  CA  MET A  94       9.621  -7.411  24.423  1.00 31.90           C  
-ANISOU  744  CA  MET A  94     4820   3737   3564   -224    -54     45       C  
-ATOM    745  C   MET A  94       9.554  -6.089  25.186  1.00 34.71           C  
-ANISOU  745  C   MET A  94     5188   4261   3740   -326    -16     38       C  
-ATOM    746  O   MET A  94       8.467  -5.568  25.430  1.00 30.61           O  
-ANISOU  746  O   MET A  94     4704   3739   3187   -375    -17     -4       O  
-ATOM    747  CB  MET A  94       9.493  -7.182  22.914  1.00 37.65           C  
-ANISOU  747  CB  MET A  94     5702   4371   4234   -221     25   -126       C  
-ATOM    748  CG  MET A  94      10.504  -6.193  22.347  1.00 42.83           C  
-ANISOU  748  CG  MET A  94     6405   5110   4758   -288    129   -228       C  
-ATOM    749  SD  MET A  94      10.644  -6.313  20.548  1.00 51.02           S  
-ANISOU  749  SD  MET A  94     7585   6131   5669   -436    225   -427       S  
-ATOM    750  CE  MET A  94       8.914  -6.250  20.069  1.00 65.71           C  
-ANISOU  750  CE  MET A  94     9596   7916   7454   -504     62   -305       C  
-ATOM    751  N   THR A  95      10.713  -5.563  25.583  1.00 28.83           N  
-ANISOU  751  N   THR A  95     4376   3639   2940   -372     35     45       N  
-ATOM    752  CA  THR A  95      10.787  -4.259  26.225  1.00 31.06           C  
-ANISOU  752  CA  THR A  95     4645   4075   3081   -488    115    -27       C  
-ATOM    753  C   THR A  95      11.682  -3.348  25.395  1.00 33.18           C  
-ANISOU  753  C   THR A  95     4975   4317   3313   -449    196   -122       C  
-ATOM    754  O   THR A  95      12.426  -3.822  24.530  1.00 32.50           O  
-ANISOU  754  O   THR A  95     4922   4161   3266   -378    212   -139       O  
-ATOM    755  CB  THR A  95      11.306  -4.353  27.671  1.00 31.68           C  
-ANISOU  755  CB  THR A  95     4581   4407   3050   -677     90     90       C  
-ATOM    756  OG1 THR A  95      12.507  -5.129  27.698  1.00 35.87           O  
-ANISOU  756  OG1 THR A  95     5015   4927   3687   -639     -4    271       O  
-ATOM    757  CG2 THR A  95      10.278  -5.022  28.556  1.00 34.70           C  
-ANISOU  757  CG2 THR A  95     4909   4889   3388   -826     13    175       C  
-ATOM    758  N   VAL A  96      11.593  -2.043  25.636  1.00 31.74           N  
-ANISOU  758  N   VAL A  96     4783   4184   3094   -524    265   -219       N  
-ATOM    759  CA  VAL A  96      12.324  -1.084  24.808  1.00 33.36           C  
-ANISOU  759  CA  VAL A  96     5045   4356   3274   -516    305   -270       C  
-ATOM    760  C   VAL A  96      13.161  -0.174  25.681  1.00 36.58           C  
-ANISOU  760  C   VAL A  96     5355   4928   3615   -599    401   -328       C  
-ATOM    761  O   VAL A  96      12.816   0.084  26.834  1.00 35.41           O  
-ANISOU  761  O   VAL A  96     5097   4908   3451   -723    462   -395       O  
-ATOM    762  CB  VAL A  96      11.377  -0.218  23.932  1.00 36.92           C  
-ANISOU  762  CB  VAL A  96     5551   4622   3855   -543    232   -281       C  
-ATOM    763  CG1 VAL A  96      10.407  -1.083  23.188  1.00 36.45           C  
-ANISOU  763  CG1 VAL A  96     5585   4432   3832   -514    124   -209       C  
-ATOM    764  CG2 VAL A  96      10.607   0.787  24.784  1.00 40.45           C  
-ANISOU  764  CG2 VAL A  96     5842   5010   4518   -610    279   -394       C  
-ATOM    765  N   ASP A  97      14.279   0.295  25.141  1.00 27.36           N  
-ANISOU  765  N   ASP A  97     4223   3792   2382   -582    437   -332       N  
-ATOM    766  CA  ASP A  97      15.023   1.367  25.787  1.00 30.55           C  
-ANISOU  766  CA  ASP A  97     4546   4325   2736   -663    528   -401       C  
-ATOM    767  C   ASP A  97      15.704   2.219  24.723  1.00 31.26           C  
-ANISOU  767  C   ASP A  97     4710   4353   2813   -649    528   -412       C  
-ATOM    768  O   ASP A  97      15.747   1.842  23.541  1.00 31.60           O  
-ANISOU  768  O   ASP A  97     4870   4320   2817   -632    471   -369       O  
-ATOM    769  CB  ASP A  97      16.036   0.837  26.801  1.00 35.86           C  
-ANISOU  769  CB  ASP A  97     5129   5212   3284   -725    551   -323       C  
-ATOM    770  CG  ASP A  97      16.206   1.771  27.993  1.00 47.23           C  
-ANISOU  770  CG  ASP A  97     6456   6863   4625   -923    656   -424       C  
-ATOM    771  OD1 ASP A  97      15.930   2.986  27.848  1.00 45.00           O  
-ANISOU  771  OD1 ASP A  97     6145   6514   4438   -951    751   -603       O  
-ATOM    772  OD2 ASP A  97      16.611   1.290  29.072  1.00 55.55           O  
-ANISOU  772  OD2 ASP A  97     7423   8151   5534  -1096    631   -317       O  
-ATOM    773  N   PHE A  98      16.228   3.364  25.147  1.00 27.74           N  
-ANISOU  773  N   PHE A  98     4189   3971   2379   -712    598   -482       N  
-ATOM    774  CA  PHE A  98      16.791   4.328  24.212  1.00 31.51           C  
-ANISOU  774  CA  PHE A  98     4717   4392   2864   -740    567   -460       C  
-ATOM    775  C   PHE A  98      18.130   4.797  24.731  1.00 32.01           C  
-ANISOU  775  C   PHE A  98     4733   4629   2801   -760    677   -507       C  
-ATOM    776  O   PHE A  98      18.320   4.954  25.933  1.00 32.80           O  
-ANISOU  776  O   PHE A  98     4720   4865   2878   -812    770   -581       O  
-ATOM    777  CB  PHE A  98      15.848   5.529  24.056  1.00 32.19           C  
-ANISOU  777  CB  PHE A  98     4701   4268   3260   -803    489   -474       C  
-ATOM    778  CG  PHE A  98      14.484   5.155  23.574  1.00 29.26           C  
-ANISOU  778  CG  PHE A  98     4344   3695   3080   -799    349   -395       C  
-ATOM    779  CD1 PHE A  98      13.510   4.730  24.474  1.00 29.24           C  
-ANISOU  779  CD1 PHE A  98     4240   3652   3216   -772    416   -516       C  
-ATOM    780  CD2 PHE A  98      14.173   5.215  22.227  1.00 30.02           C  
-ANISOU  780  CD2 PHE A  98     4552   3675   3181   -881    142   -190       C  
-ATOM    781  CE1 PHE A  98      12.249   4.374  24.035  1.00 29.62           C  
-ANISOU  781  CE1 PHE A  98     4291   3499   3464   -760    285   -443       C  
-ATOM    782  CE2 PHE A  98      12.909   4.851  21.772  1.00 31.07           C  
-ANISOU  782  CE2 PHE A  98     4695   3626   3486   -905    -17    -79       C  
-ATOM    783  CZ  PHE A  98      11.947   4.424  22.678  1.00 30.22           C  
-ANISOU  783  CZ  PHE A  98     4479   3432   3572   -810     58   -210       C  
-ATOM    784  N   ILE A  99      19.066   5.024  23.822  1.00 29.93           N  
-ANISOU  784  N   ILE A  99     4553   4394   2425   -772    671   -472       N  
-ATOM    785  CA  ILE A  99      20.367   5.517  24.232  1.00 31.89           C  
-ANISOU  785  CA  ILE A  99     4754   4789   2575   -785    769   -510       C  
-ATOM    786  C   ILE A  99      20.847   6.490  23.184  1.00 33.39           C  
-ANISOU  786  C   ILE A  99     5010   4952   2722   -868    727   -481       C  
-ATOM    787  O   ILE A  99      20.481   6.381  22.008  1.00 32.08           O  
-ANISOU  787  O   ILE A  99     4954   4727   2506   -959    626   -409       O  
-ATOM    788  CB  ILE A  99      21.372   4.354  24.446  1.00 44.19           C  
-ANISOU  788  CB  ILE A  99     6289   6445   4055   -723    826   -496       C  
-ATOM    789  CG1 ILE A  99      22.585   4.834  25.244  1.00 50.99           C  
-ANISOU  789  CG1 ILE A  99     7056   7460   4859   -752    896   -492       C  
-ATOM    790  CG2 ILE A  99      21.765   3.707  23.124  1.00 44.46           C  
-ANISOU  790  CG2 ILE A  99     6410   6427   4054   -726    852   -551       C  
-ATOM    791  CD1 ILE A  99      23.579   3.744  25.556  1.00 55.84           C  
-ANISOU  791  CD1 ILE A  99     7565   8103   5546   -708    894   -417       C  
-ATOM    792  N   ARG A 100      21.627   7.476  23.604  1.00 31.75           N  
-ANISOU  792  N   ARG A 100     4734   4815   2516   -896    786   -517       N  
-ATOM    793  CA  ARG A 100      22.166   8.424  22.645  1.00 34.54           C  
-ANISOU  793  CA  ARG A 100     5139   5161   2824  -1006    721   -452       C  
-ATOM    794  C   ARG A 100      23.667   8.569  22.866  1.00 41.23           C  
-ANISOU  794  C   ARG A 100     5979   6185   3502   -994    856   -520       C  
-ATOM    795  O   ARG A 100      24.118   8.661  24.008  1.00 38.56           O  
-ANISOU  795  O   ARG A 100     5538   5930   3182   -934    955   -584       O  
-ATOM    796  CB  ARG A 100      21.475   9.784  22.772  1.00 42.29           C  
-ANISOU  796  CB  ARG A 100     5991   5957   4121  -1068    609   -403       C  
-ATOM    797  CG  ARG A 100      22.191  10.880  22.001  1.00 47.33           C  
-ANISOU  797  CG  ARG A 100     6637   6597   4749  -1204    509   -285       C  
-ATOM    798  CD  ARG A 100      21.260  11.625  21.091  1.00 54.64           C  
-ANISOU  798  CD  ARG A 100     7514   7289   5957  -1370    215    -37       C  
-ATOM    799  NE  ARG A 100      20.665  12.784  21.739  1.00 59.61           N  
-ANISOU  799  NE  ARG A 100     7868   7633   7147  -1340    160    -69       N  
-ATOM    800  CZ  ARG A 100      20.895  14.040  21.372  1.00 62.72           C  
-ANISOU  800  CZ  ARG A 100     8119   7869   7843  -1461    -10     84       C  
-ATOM    801  NH1 ARG A 100      21.703  14.302  20.356  1.00 61.58           N  
-ANISOU  801  NH1 ARG A 100     8122   7882   7393  -1653   -161    319       N  
-ATOM    802  NH2 ARG A 100      20.311  15.037  22.018  1.00 68.74           N  
-ANISOU  802  NH2 ARG A 100     8556   8308   9254  -1426    -19    -22       N  
-ATOM    803  N   LEU A 101      24.418   8.554  21.765  1.00 45.55           N  
-ANISOU  803  N   LEU A 101     6927   5196   5183   -621  -1167   -462       N  
-ATOM    804  CA  LEU A 101      25.864   8.751  21.768  1.00 49.37           C  
-ANISOU  804  CA  LEU A 101     7348   5720   5691   -978  -1304   -337       C  
-ATOM    805  C   LEU A 101      26.201  10.015  20.975  1.00 56.85           C  
-ANISOU  805  C   LEU A 101     8493   6446   6662  -1239  -1505   -171       C  
-ATOM    806  O   LEU A 101      25.604  10.271  19.926  1.00 57.98           O  
-ANISOU  806  O   LEU A 101     8642   6563   6826  -1188  -1454    -88       O  
-ATOM    807  CB  LEU A 101      26.567   7.547  21.130  1.00 45.67           C  
-ANISOU  807  CB  LEU A 101     6470   5636   5246  -1058  -1124   -231       C  
-ATOM    808  CG  LEU A 101      27.033   6.384  22.004  1.00 51.17           C  
-ANISOU  808  CG  LEU A 101     6974   6540   5926   -976  -1040   -310       C  
-ATOM    809  CD1 LEU A 101      25.899   5.817  22.842  1.00 48.44           C  
-ANISOU  809  CD1 LEU A 101     6730   6143   5532   -682   -949   -497       C  
-ATOM    810  CD2 LEU A 101      27.650   5.291  21.141  1.00 51.11           C  
-ANISOU  810  CD2 LEU A 101     6631   6862   5926   -975   -864   -210       C  
-ATOM    811  N   LYS A 102      27.152  10.799  21.476  1.00 63.96           N  
-ANISOU  811  N   LYS A 102     9570   7185   7548  -1552  -1763   -100       N  
-ATOM    812  CA  LYS A 102      27.630  11.985  20.761  1.00 72.44           C  
-ANISOU  812  CA  LYS A 102    10847   8047   8630  -1905  -2007    111       C  
-ATOM    813  C   LYS A 102      29.132  12.190  20.961  1.00 77.93           C  
-ANISOU  813  C   LYS A 102    11375   8913   9321  -2326  -2142    336       C  
-ATOM    814  O   LYS A 102      29.915  12.083  20.017  1.00 82.23           O  
-ANISOU  814  O   LYS A 102    11607   9760   9877  -2607  -2096    596       O  
-ATOM    815  CB  LYS A 102      26.864  13.223  21.198  1.00 73.98           C  
-ANISOU  815  CB  LYS A 102    11615   7709   8786  -1756  -2233    -11       C  
-ATOM    816  N   LEU A 121      19.760   0.952  32.614  1.00 58.91           N  
-ANISOU  816  N   LEU A 121     8208   8523   5654    434   -277   -985       N  
-ATOM    817  CA  LEU A 121      20.020  -0.059  31.586  1.00 51.73           C  
-ANISOU  817  CA  LEU A 121     7140   7634   4882    266   -330   -865       C  
-ATOM    818  C   LEU A 121      20.154  -1.469  32.159  1.00 50.31           C  
-ANISOU  818  C   LEU A 121     6915   7548   4653     93   -372   -730       C  
-ATOM    819  O   LEU A 121      20.531  -2.412  31.454  1.00 48.06           O  
-ANISOU  819  O   LEU A 121     6576   7209   4476    -36   -446   -641       O  
-ATOM    820  CB  LEU A 121      21.251   0.298  30.751  1.00 53.09           C  
-ANISOU  820  CB  LEU A 121     7363   7561   5246    174   -462   -914       C  
-ATOM    821  CG  LEU A 121      21.037   1.212  29.539  1.00 52.91           C  
-ANISOU  821  CG  LEU A 121     7330   7446   5326    257   -449   -956       C  
-ATOM    822  CD1 LEU A 121      22.275   1.229  28.651  1.00 52.58           C  
-ANISOU  822  CD1 LEU A 121     7264   7244   5471     99   -558   -925       C  
-ATOM    823  CD2 LEU A 121      19.810   0.789  28.743  1.00 51.69           C  
-ANISOU  823  CD2 LEU A 121     6994   7466   5178    306   -325   -841       C  
-ATOM    824  N   SER A 122      19.823  -1.616  33.438  1.00 49.91           N  
-ANISOU  824  N   SER A 122     6921   7617   4423    108   -333   -713       N  
-ATOM    825  CA  SER A 122      19.655  -2.932  34.039  1.00 48.94           C  
-ANISOU  825  CA  SER A 122     6765   7610   4218    -47   -371   -553       C  
-ATOM    826  C   SER A 122      18.493  -3.635  33.348  1.00 51.14           C  
-ANISOU  826  C   SER A 122     6845   8107   4479   -129   -296   -382       C  
-ATOM    827  O   SER A 122      18.259  -4.819  33.557  1.00 53.31           O  
-ANISOU  827  O   SER A 122     7098   8436   4722   -315   -358   -212       O  
-ATOM    828  CB  SER A 122      19.380  -2.801  35.537  1.00 52.00           C  
-ANISOU  828  CB  SER A 122     7246   8128   4384     -8   -319   -561       C  
-ATOM    829  OG  SER A 122      18.375  -1.833  35.775  1.00 54.23           O  
-ANISOU  829  OG  SER A 122     7474   8598   4532    200   -130   -633       O  
-ATOM    830  N   THR A 123      17.774  -2.884  32.517  1.00 57.73           N  
-ANISOU  830  N   THR A 123     7550   9049   5335     -5   -190   -412       N  
-ATOM    831  CA  THR A 123      16.712  -3.411  31.671  1.00 66.59           C  
-ANISOU  831  CA  THR A 123     8466  10381   6454   -110   -151   -232       C  
-ATOM    832  C   THR A 123      17.238  -4.459  30.679  1.00 67.01           C  
-ANISOU  832  C   THR A 123     8591  10205   6663   -333   -312   -152       C  
-ATOM    833  O   THR A 123      16.454  -5.170  30.049  1.00 71.13           O  
-ANISOU  833  O   THR A 123     9020  10821   7187   -509   -344     24       O  
-ATOM    834  CB  THR A 123      16.020  -2.264  30.891  1.00 72.44           C  
-ANISOU  834  CB  THR A 123     9075  11249   7200    117    -34   -293       C  
-ATOM    835  OG1 THR A 123      16.971  -1.614  30.036  1.00 74.29           O  
-ANISOU  835  OG1 THR A 123     9452  11148   7628    182   -111   -454       O  
-ATOM    836  CG2 THR A 123      15.440  -1.237  31.854  1.00 75.96           C  
-ANISOU  836  CG2 THR A 123     9497  11867   7497    423    131   -387       C  
-ATOM    837  N   LEU A 124      18.562  -4.550  30.551  1.00 59.07           N  
-ANISOU  837  N   LEU A 124     7759   8898   5786   -313   -417   -276       N  
-ATOM    838  CA  LEU A 124      19.205  -5.439  29.579  1.00 47.60           C  
-ANISOU  838  CA  LEU A 124     6402   7213   4471   -412   -541   -248       C  
-ATOM    839  C   LEU A 124      19.637  -6.783  30.168  1.00 41.86           C  
-ANISOU  839  C   LEU A 124     5813   6362   3729   -523   -672   -157       C  
-ATOM    840  O   LEU A 124      19.760  -7.773  29.445  1.00 37.78           O  
-ANISOU  840  O   LEU A 124     5402   5684   3269   -606   -768    -97       O  
-ATOM    841  CB  LEU A 124      20.445  -4.769  28.985  1.00 46.09           C  
-ANISOU  841  CB  LEU A 124     6258   6835   4417   -288   -563   -413       C  
-ATOM    842  CG  LEU A 124      20.356  -3.375  28.378  1.00 43.58           C  
-ANISOU  842  CG  LEU A 124     5862   6538   4158   -167   -474   -522       C  
-ATOM    843  CD1 LEU A 124      21.733  -2.919  27.928  1.00 44.05           C  
-ANISOU  843  CD1 LEU A 124     5959   6414   4364   -120   -526   -620       C  
-ATOM    844  CD2 LEU A 124      19.405  -3.366  27.204  1.00 43.50           C  
-ANISOU  844  CD2 LEU A 124     5764   6585   4180   -201   -424   -439       C  
-ATOM    845  N   THR A 125      19.889  -6.814  31.475  1.00 39.49           N  
-ANISOU  845  N   THR A 125     5545   6120   3341   -509   -684   -154       N  
-ATOM    846  CA  THR A 125      20.520  -7.981  32.102  1.00 39.99           C  
-ANISOU  846  CA  THR A 125     5745   6050   3399   -580   -826    -81       C  
-ATOM    847  C   THR A 125      19.745  -9.292  31.886  1.00 46.17           C  
-ANISOU  847  C   THR A 125     6605   6789   4148   -801   -908    115       C  
-ATOM    848  O   THR A 125      18.526  -9.350  32.082  1.00 45.49           O  
-ANISOU  848  O   THR A 125     6408   6914   3963   -965   -845    259       O  
-ATOM    849  CB  THR A 125      20.779  -7.725  33.593  1.00 47.34           C  
-ANISOU  849  CB  THR A 125     6693   7082   4212   -552   -826    -93       C  
-ATOM    850  OG1 THR A 125      21.515  -6.500  33.723  1.00 50.73           O  
-ANISOU  850  OG1 THR A 125     7107   7490   4678   -388   -792   -273       O  
-ATOM    851  CG2 THR A 125      21.584  -8.856  34.204  1.00 46.72           C  
-ANISOU  851  CG2 THR A 125     6750   6858   4142   -606   -991    -16       C  
-ATOM    852  N   GLY A 126      20.459 -10.328  31.443  1.00 44.86           N  
-ANISOU  852  N   GLY A 126     6635   6352   4056   -809  -1057    128       N  
-ATOM    853  CA  GLY A 126      19.866 -11.632  31.215  1.00 41.60           C  
-ANISOU  853  CA  GLY A 126     6401   5790   3616  -1036  -1188    301       C  
-ATOM    854  C   GLY A 126      18.877 -11.702  30.061  1.00 45.74           C  
-ANISOU  854  C   GLY A 126     6898   6322   4159  -1181  -1167    365       C  
-ATOM    855  O   GLY A 126      18.120 -12.671  29.950  1.00 47.63           O  
-ANISOU  855  O   GLY A 126     7261   6482   4356  -1456  -1283    543       O  
-ATOM    856  N   LYS A 127      18.867 -10.694  29.190  1.00 41.59           N  
-ANISOU  856  N   LYS A 127     6226   5881   3694  -1036  -1046    238       N  
-ATOM    857  CA  LYS A 127      17.906 -10.694  28.088  1.00 42.50           C  
-ANISOU  857  CA  LYS A 127     6298   6029   3821  -1178  -1036    313       C  
-ATOM    858  C   LYS A 127      18.602 -10.668  26.731  1.00 37.14           C  
-ANISOU  858  C   LYS A 127     5759   5120   3232  -1024  -1054    163       C  
-ATOM    859  O   LYS A 127      19.805 -10.431  26.652  1.00 41.22           O  
-ANISOU  859  O   LYS A 127     6331   5530   3801   -790  -1037      1       O  
-ATOM    860  CB  LYS A 127      16.912  -9.530  28.224  1.00 42.45           C  
-ANISOU  860  CB  LYS A 127     5969   6394   3765  -1186   -875    356       C  
-ATOM    861  CG  LYS A 127      16.090  -9.585  29.533  1.00 50.36           C  
-ANISOU  861  CG  LYS A 127     6801   7707   4627  -1329   -825    521       C  
-ATOM    862  CD  LYS A 127      15.066  -8.457  29.632  1.00 52.49           C  
-ANISOU  862  CD  LYS A 127     6733   8399   4810  -1267   -649    567       C  
-ATOM    863  CE  LYS A 127      14.411  -8.390  31.010  1.00 55.73           C  
-ANISOU  863  CE  LYS A 127     6956   9170   5049  -1312   -552    689       C  
-ATOM    864  NZ  LYS A 127      15.403  -8.079  32.067  1.00 54.31           N  
-ANISOU  864  NZ  LYS A 127     6919   8886   4831  -1117   -517    521       N  
-ATOM    865  N   ASN A 128      17.839 -10.943  25.680  1.00 35.79           N  
-ANISOU  865  N   ASN A 128     5638   4900   3061  -1175  -1093    237       N  
-ATOM    866  CA  ASN A 128      18.340 -10.849  24.316  1.00 35.73           C  
-ANISOU  866  CA  ASN A 128     5755   4720   3102  -1039  -1087    105       C  
-ATOM    867  C   ASN A 128      18.262  -9.409  23.821  1.00 36.80           C  
-ANISOU  867  C   ASN A 128     5626   5072   3285   -910   -930     18       C  
-ATOM    868  O   ASN A 128      17.187  -8.932  23.450  1.00 41.65           O  
-ANISOU  868  O   ASN A 128     6076   5865   3885  -1041   -900    126       O  
-ATOM    869  CB  ASN A 128      17.546 -11.775  23.396  1.00 39.22           C  
-ANISOU  869  CB  ASN A 128     6412   4987   3502  -1279  -1222    228       C  
-ATOM    870  CG  ASN A 128      17.820 -13.242  23.680  1.00 46.40           C  
-ANISOU  870  CG  ASN A 128     7714   5560   4358  -1381  -1420    288       C  
-ATOM    871  OD1 ASN A 128      18.592 -13.576  24.584  1.00 46.70           O  
-ANISOU  871  OD1 ASN A 128     7836   5516   4394  -1260  -1455    246       O  
-ATOM    872  ND2 ASN A 128      17.184 -14.125  22.913  1.00 49.03           N  
-ANISOU  872  ND2 ASN A 128     8323   5672   4636  -1614  -1577    399       N  
-ATOM    873  N   VAL A 129      19.408  -8.731  23.812  1.00 37.52           N  
-ANISOU  873  N   VAL A 129     5683   5147   3426   -671   -851   -154       N  
-ATOM    874  CA  VAL A 129      19.476  -7.312  23.472  1.00 31.83           C  
-ANISOU  874  CA  VAL A 129     4762   4583   2747   -569   -727   -233       C  
-ATOM    875  C   VAL A 129      19.636  -7.104  21.971  1.00 35.30           C  
-ANISOU  875  C   VAL A 129     5263   4946   3205   -533   -703   -286       C  
-ATOM    876  O   VAL A 129      20.574  -7.636  21.358  1.00 33.27           O  
-ANISOU  876  O   VAL A 129     5174   4530   2937   -420   -714   -381       O  
-ATOM    877  CB  VAL A 129      20.626  -6.627  24.224  1.00 32.36           C  
-ANISOU  877  CB  VAL A 129     4770   4674   2851   -404   -677   -361       C  
-ATOM    878  CG1 VAL A 129      20.701  -5.135  23.872  1.00 31.47           C  
-ANISOU  878  CG1 VAL A 129     4477   4659   2821   -316   -557   -426       C  
-ATOM    879  CG2 VAL A 129      20.435  -6.790  25.724  1.00 37.99           C  
-ANISOU  879  CG2 VAL A 129     5441   5474   3522   -438   -699   -310       C  
-ATOM    880  N   LEU A 130      18.701  -6.366  21.370  1.00 28.68           N  
-ANISOU  880  N   LEU A 130     4293   4240   2366   -616   -671   -214       N  
-ATOM    881  CA  LEU A 130      18.818  -6.000  19.968  1.00 26.57           C  
-ANISOU  881  CA  LEU A 130     4070   3926   2100   -595   -647   -249       C  
-ATOM    882  C   LEU A 130      19.120  -4.510  19.900  1.00 28.39           C  
-ANISOU  882  C   LEU A 130     4116   4272   2397   -489   -539   -303       C  
-ATOM    883  O   LEU A 130      18.287  -3.688  20.272  1.00 30.28           O  
-ANISOU  883  O   LEU A 130     4178   4657   2670   -488   -508   -233       O  
-ATOM    884  CB  LEU A 130      17.533  -6.321  19.192  1.00 27.07           C  
-ANISOU  884  CB  LEU A 130     4136   4022   2127   -788   -724    -95       C  
-ATOM    885  CG  LEU A 130      17.474  -5.884  17.724  1.00 33.40           C  
-ANISOU  885  CG  LEU A 130     4981   4799   2911   -794   -715   -103       C  
-ATOM    886  CD1 LEU A 130      18.530  -6.606  16.895  1.00 32.31           C  
-ANISOU  886  CD1 LEU A 130     5098   4458   2720   -688   -703   -237       C  
-ATOM    887  CD2 LEU A 130      16.096  -6.098  17.132  1.00 37.37           C  
-ANISOU  887  CD2 LEU A 130     5439   5375   3385  -1013   -814     80       C  
-ATOM    888  N   ILE A 131      20.322  -4.164  19.457  1.00 26.27           N  
-ANISOU  888  N   ILE A 131     3869   3928   2185   -360   -466   -406       N  
-ATOM    889  CA  ILE A 131      20.681  -2.759  19.269  1.00 28.27           C  
-ANISOU  889  CA  ILE A 131     3973   4226   2542   -292   -385   -421       C  
-ATOM    890  C   ILE A 131      20.207  -2.340  17.874  1.00 24.32           C  
-ANISOU  890  C   ILE A 131     3490   3742   2009   -357   -383   -357       C  
-ATOM    891  O   ILE A 131      20.472  -3.029  16.892  1.00 25.31           O  
-ANISOU  891  O   ILE A 131     3754   3826   2035   -385   -387   -371       O  
-ATOM    892  CB  ILE A 131      22.204  -2.539  19.428  1.00 31.05           C  
-ANISOU  892  CB  ILE A 131     4289   4555   2954   -193   -331   -499       C  
-ATOM    893  CG1 ILE A 131      22.657  -2.914  20.836  1.00 27.97           C  
-ANISOU  893  CG1 ILE A 131     3883   4155   2591   -143   -366   -544       C  
-ATOM    894  CG2 ILE A 131      22.582  -1.103  19.161  1.00 31.29           C  
-ANISOU  894  CG2 ILE A 131     4211   4604   3072   -208   -300   -476       C  
-ATOM    895  CD1 ILE A 131      24.168  -2.846  21.041  1.00 31.06           C  
-ANISOU  895  CD1 ILE A 131     4195   4572   3035    -60   -344   -581       C  
-ATOM    896  N   VAL A 132      19.470  -1.234  17.788  1.00 25.72           N  
-ANISOU  896  N   VAL A 132     3557   3970   2244   -358   -387   -287       N  
-ATOM    897  CA  VAL A 132      18.915  -0.812  16.495  1.00 23.71           C  
-ANISOU  897  CA  VAL A 132     3317   3738   1956   -429   -416   -193       C  
-ATOM    898  C   VAL A 132      19.539   0.516  16.060  1.00 27.67           C  
-ANISOU  898  C   VAL A 132     3785   4190   2540   -389   -382   -184       C  
-ATOM    899  O   VAL A 132      19.346   1.536  16.716  1.00 28.78           O  
-ANISOU  899  O   VAL A 132     3872   4290   2773   -305   -397   -182       O  
-ATOM    900  CB  VAL A 132      17.386  -0.689  16.522  1.00 23.91           C  
-ANISOU  900  CB  VAL A 132     3240   3882   1961   -471   -490    -59       C  
-ATOM    901  CG1 VAL A 132      16.865  -0.375  15.112  1.00 21.87           C  
-ANISOU  901  CG1 VAL A 132     3009   3647   1652   -567   -556     57       C  
-ATOM    902  CG2 VAL A 132      16.745  -1.986  17.044  1.00 28.31           C  
-ANISOU  902  CG2 VAL A 132     3819   4515   2424   -593   -557    -14       C  
-ATOM    903  N   GLU A 133      20.261   0.493  14.946  1.00 27.49           N  
-ANISOU  903  N   GLU A 133     3823   4165   2456   -453   -347   -170       N  
-ATOM    904  CA  GLU A 133      21.042   1.645  14.489  1.00 28.58           C  
-ANISOU  904  CA  GLU A 133     3931   4280   2646   -487   -327   -120       C  
-ATOM    905  C   GLU A 133      20.633   2.089  13.085  1.00 24.78           C  
-ANISOU  905  C   GLU A 133     3504   3823   2087   -587   -360      3       C  
-ATOM    906  O   GLU A 133      20.085   1.305  12.312  1.00 26.27           O  
-ANISOU  906  O   GLU A 133     3772   4063   2146   -634   -374     21       O  
-ATOM    907  CB  GLU A 133      22.540   1.294  14.534  1.00 37.50           C  
-ANISOU  907  CB  GLU A 133     5017   5478   3753   -482   -231   -175       C  
-ATOM    908  CG  GLU A 133      23.524   2.384  14.082  1.00 40.47           C  
-ANISOU  908  CG  GLU A 133     5320   5897   4160   -594   -219    -74       C  
-ATOM    909  CD  GLU A 133      23.566   3.588  15.011  1.00 42.18           C  
-ANISOU  909  CD  GLU A 133     5540   5967   4521   -639   -335    -51       C  
-ATOM    910  OE1 GLU A 133      22.512   4.225  15.214  1.00 40.89           O  
-ANISOU  910  OE1 GLU A 133     5468   5659   4409   -590   -426    -43       O  
-ATOM    911  OE2 GLU A 133      24.657   3.908  15.529  1.00 44.72           O  
-ANISOU  911  OE2 GLU A 133     5783   6320   4887   -714   -349    -36       O  
-ATOM    912  N   ASP A 134      20.908   3.347  12.743  1.00 23.62           N  
-ANISOU  912  N   ASP A 134     3355   3621   2001   -648   -402    102       N  
-ATOM    913  CA  ASP A 134      20.605   3.830  11.406  1.00 27.25           C  
-ANISOU  913  CA  ASP A 134     3876   4103   2374   -762   -447    246       C  
-ATOM    914  C   ASP A 134      21.706   3.468  10.393  1.00 26.28           C  
-ANISOU  914  C   ASP A 134     3763   4133   2090   -870   -328    272       C  
-ATOM    915  O   ASP A 134      21.424   2.974   9.291  1.00 28.00           O  
-ANISOU  915  O   ASP A 134     4072   4436   2131   -922   -308    306       O  
-ATOM    916  CB  ASP A 134      20.344   5.351  11.402  1.00 29.50           C  
-ANISOU  916  CB  ASP A 134     4205   4230   2772   -784   -578    370       C  
-ATOM    917  CG  ASP A 134      21.471   6.163  12.045  1.00 29.83           C  
-ANISOU  917  CG  ASP A 134     4256   4175   2904   -853   -594    365       C  
-ATOM    918  OD1 ASP A 134      22.337   5.602  12.752  1.00 28.74           O  
-ANISOU  918  OD1 ASP A 134     4032   4112   2778   -845   -507    262       O  
-ATOM    919  OD2 ASP A 134      21.484   7.397  11.834  1.00 37.95           O  
-ANISOU  919  OD2 ASP A 134     5398   5035   3987   -933   -730    486       O  
-ATOM    920  N   ILE A 135      22.958   3.726  10.763  1.00 27.06           N  
-ANISOU  920  N   ILE A 135     3762   4297   2224   -901   -251    267       N  
-ATOM    921  CA  ILE A 135      24.049   3.512   9.811  1.00 27.98           C  
-ANISOU  921  CA  ILE A 135     3817   4646   2169   -976   -108    331       C  
-ATOM    922  C   ILE A 135      25.358   3.132  10.508  1.00 26.32           C  
-ANISOU  922  C   ILE A 135     3423   4592   1985   -911     10    276       C  
-ATOM    923  O   ILE A 135      25.695   3.648  11.581  1.00 26.27           O  
-ANISOU  923  O   ILE A 135     3337   4499   2147   -945    -71    276       O  
-ATOM    924  CB  ILE A 135      24.225   4.737   8.866  1.00 31.80           C  
-ANISOU  924  CB  ILE A 135     4315   5159   2610  -1208   -172    559       C  
-ATOM    925  CG1 ILE A 135      25.254   4.446   7.755  1.00 30.21           C  
-ANISOU  925  CG1 ILE A 135     4024   5288   2168  -1282     13    649       C  
-ATOM    926  CG2 ILE A 135      24.567   5.980   9.670  1.00 30.78           C  
-ANISOU  926  CG2 ILE A 135     4156   4866   2671  -1341   -320    656       C  
-ATOM    927  CD1 ILE A 135      25.244   5.456   6.599  1.00 32.44           C  
-ANISOU  927  CD1 ILE A 135     4360   5630   2337  -1539    -48    897       C  
-ATOM    928  N   ILE A 136      26.060   2.178   9.914  1.00 29.20           N  
-ANISOU  928  N   ILE A 136     3742   5190   2164   -785    192    222       N  
-ATOM    929  CA  ILE A 136      27.414   1.855  10.321  1.00 33.38           C  
-ANISOU  929  CA  ILE A 136     4036   5964   2682   -694    325    224       C  
-ATOM    930  C   ILE A 136      28.347   2.310   9.218  1.00 34.16           C  
-ANISOU  930  C   ILE A 136     3966   6412   2600   -814    467    414       C  
-ATOM    931  O   ILE A 136      28.135   2.001   8.038  1.00 34.46           O  
-ANISOU  931  O   ILE A 136     4124   6561   2407   -776    574    417       O  
-ATOM    932  CB  ILE A 136      27.572   0.366  10.613  1.00 36.65           C  
-ANISOU  932  CB  ILE A 136     4517   6396   3012   -375    432     17       C  
-ATOM    933  CG1 ILE A 136      26.754   0.019  11.856  1.00 39.64           C  
-ANISOU  933  CG1 ILE A 136     5013   6477   3573   -328    278   -113       C  
-ATOM    934  CG2 ILE A 136      29.051   0.004  10.822  1.00 36.22           C  
-ANISOU  934  CG2 ILE A 136     4179   6673   2911   -214    595     48       C  
-ATOM    935  CD1 ILE A 136      26.707  -1.438  12.168  1.00 45.61           C  
-ANISOU  935  CD1 ILE A 136     5918   7163   4248    -70    315   -294       C  
-ATOM    936  N   ASP A 137      29.356   3.090   9.591  1.00 33.33           N  
-ANISOU  936  N   ASP A 137     3590   6496   2579   -999    450    598       N  
-ATOM    937  CA  ASP A 137      30.325   3.583   8.622  1.00 36.81           C  
-ANISOU  937  CA  ASP A 137     3799   7348   2840  -1170    583    843       C  
-ATOM    938  C   ASP A 137      31.708   3.068   9.003  1.00 47.48           C  
-ANISOU  938  C   ASP A 137     4769   9123   4150  -1024    752    894       C  
-ATOM    939  O   ASP A 137      32.177   2.090   8.437  1.00 48.20           O  
-ANISOU  939  O   ASP A 137     4779   9511   4026   -699   1003    807       O  
-ATOM    940  CB  ASP A 137      30.272   5.117   8.532  1.00 39.84           C  
-ANISOU  940  CB  ASP A 137     4195   7616   3325  -1616    366   1109       C  
-ATOM    941  CG  ASP A 137      31.287   5.697   7.565  1.00 45.85           C  
-ANISOU  941  CG  ASP A 137     4696   8834   3891  -1884    476   1427       C  
-ATOM    942  OD1 ASP A 137      31.810   4.965   6.694  1.00 51.06           O  
-ANISOU  942  OD1 ASP A 137     5231   9814   4357  -1641    711   1380       O  
-ATOM    943  OD2 ASP A 137      31.542   6.913   7.656  1.00 50.08           O  
-ANISOU  943  OD2 ASP A 137     5217   9284   4528  -2276    258   1669       O  
-ATOM    944  N   THR A 138      32.357   3.709   9.972  1.00 42.43           N  
-ANISOU  944  N   THR A 138     3912   8510   3698  -1238    603   1033       N  
-ATOM    945  CA  THR A 138      33.682   3.253  10.382  1.00 47.94           C  
-ANISOU  945  CA  THR A 138     4188   9655   4370  -1115    732   1126       C  
-ATOM    946  C   THR A 138      33.518   2.054  11.306  1.00 45.26           C  
-ANISOU  946  C   THR A 138     3934   9144   4119   -697    757    838       C  
-ATOM    947  O   THR A 138      34.352   1.146  11.327  1.00 48.78           O  
-ANISOU  947  O   THR A 138     4141   9927   4466   -358    946    806       O  
-ATOM    948  CB  THR A 138      34.491   4.351  11.103  1.00 43.92           C  
-ANISOU  948  CB  THR A 138     3419   9255   4014  -1556    513   1412       C  
-ATOM    949  OG1 THR A 138      33.798   4.754  12.295  1.00 42.95           O  
-ANISOU  949  OG1 THR A 138     3581   8606   4134  -1664    225   1273       O  
-ATOM    950  CG2 THR A 138      34.695   5.549  10.189  1.00 46.62           C  
-ANISOU  950  CG2 THR A 138     3788   9633   4293  -1949    394   1679       C  
-ATOM    951  N   GLY A 139      32.426   2.050  12.057  1.00 36.31           N  
-ANISOU  951  N   GLY A 139     3143   7499   3154   -704    566    644       N  
-ATOM    952  CA  GLY A 139      32.173   0.994  13.018  1.00 35.51           C  
-ANISOU  952  CA  GLY A 139     3157   7199   3136   -389    544    407       C  
-ATOM    953  C   GLY A 139      32.553   1.416  14.427  1.00 36.36           C  
-ANISOU  953  C   GLY A 139     3146   7215   3453   -542    339    453       C  
-ATOM    954  O   GLY A 139      32.266   0.702  15.391  1.00 36.51           O  
-ANISOU  954  O   GLY A 139     3281   7033   3557   -350    274    282       O  
-ATOM    955  N   LYS A 140      33.197   2.576  14.554  1.00 39.98           N  
-ANISOU  955  N   LYS A 140     3406   7811   3973   -920    212    697       N  
-ATOM    956  CA  LYS A 140      33.651   3.065  15.869  1.00 44.31           C  
-ANISOU  956  CA  LYS A 140     3876   8276   4684  -1120    -23    758       C  
-ATOM    957  C   LYS A 140      32.529   3.218  16.877  1.00 41.86           C  
-ANISOU  957  C   LYS A 140     3951   7451   4502  -1112   -209    541       C  
-ATOM    958  O   LYS A 140      32.654   2.796  18.029  1.00 44.41           O  
-ANISOU  958  O   LYS A 140     4282   7690   4901  -1016   -302    445       O  
-ATOM    959  CB  LYS A 140      34.359   4.416  15.751  1.00 53.22           C  
-ANISOU  959  CB  LYS A 140     4844   9542   5834  -1617   -199   1068       C  
-ATOM    960  CG  LYS A 140      35.770   4.376  15.206  1.00 64.17           C  
-ANISOU  960  CG  LYS A 140     5709  11561   7114  -1715    -72   1371       C  
-ATOM    961  CD  LYS A 140      36.456   5.715  15.469  1.00 71.76           C  
-ANISOU  961  CD  LYS A 140     6663  12489   8115  -2224   -358   1657       C  
-ATOM    962  CE  LYS A 140      37.709   5.906  14.626  1.00 81.08           C  
-ANISOU  962  CE  LYS A 140     7512  14160   9135  -2289   -256   1954       C  
-ATOM    963  NZ  LYS A 140      37.386   6.239  13.205  1.00 83.31           N  
-ANISOU  963  NZ  LYS A 140     7850  14536   9267  -2344   -117   2031       N  
-ATOM    964  N   THR A 141      31.442   3.851  16.449  1.00 36.66           N  
-ANISOU  964  N   THR A 141     3595   6484   3850  -1204   -263    485       N  
-ATOM    965  CA  THR A 141      30.300   4.081  17.321  1.00 36.59           C  
-ANISOU  965  CA  THR A 141     3918   6051   3932  -1156   -406    299       C  
-ATOM    966  C   THR A 141      29.743   2.772  17.871  1.00 38.62           C  
-ANISOU  966  C   THR A 141     4244   6247   4183   -821   -309     83       C  
-ATOM    967  O   THR A 141      29.479   2.644  19.073  1.00 39.36           O  
-ANISOU  967  O   THR A 141     4440   6177   4340   -773   -416    -27       O  
-ATOM    968  CB  THR A 141      29.176   4.820  16.592  1.00 35.38           C  
-ANISOU  968  CB  THR A 141     4025   5647   3770  -1219   -442    292       C  
-ATOM    969  OG1 THR A 141      29.671   6.061  16.080  1.00 43.75           O  
-ANISOU  969  OG1 THR A 141     5083   6711   4830  -1557   -572    514       O  
-ATOM    970  CG2 THR A 141      28.012   5.083  17.539  1.00 39.63           C  
-ANISOU  970  CG2 THR A 141     4850   5824   4384  -1110   -563    117       C  
-ATOM    971  N   MET A 142      29.559   1.798  16.988  1.00 29.73           N  
-ANISOU  971  N   MET A 142     3100   5241   2953   -609   -123     29       N  
-ATOM    972  CA  MET A 142      28.990   0.521  17.415  1.00 29.74           C  
-ANISOU  972  CA  MET A 142     3232   5139   2928   -339    -74   -152       C  
-ATOM    973  C   MET A 142      29.921  -0.238  18.374  1.00 26.77           C  
-ANISOU  973  C   MET A 142     2704   4884   2582   -195    -89   -173       C  
-ATOM    974  O   MET A 142      29.474  -0.761  19.399  1.00 30.25           O  
-ANISOU  974  O   MET A 142     3274   5156   3064   -114   -172   -281       O  
-ATOM    975  CB  MET A 142      28.599  -0.338  16.203  1.00 36.09           C  
-ANISOU  975  CB  MET A 142     4141   5989   3581   -170     80   -210       C  
-ATOM    976  CG  MET A 142      27.653  -1.470  16.567  1.00 42.16           C  
-ANISOU  976  CG  MET A 142     5155   6547   4316     -5     52   -371       C  
-ATOM    977  SD  MET A 142      26.391  -1.006  17.790  1.00 47.20           S  
-ANISOU  977  SD  MET A 142     5929   6927   5079   -130   -115   -417       S  
-ATOM    978  CE  MET A 142      25.471   0.251  16.902  1.00 25.99           C  
-ANISOU  978  CE  MET A 142     3301   4169   2403   -306   -144   -333       C  
-ATOM    979  N   GLN A 143      31.211  -0.269  18.064  1.00 33.22           N  
-ANISOU  979  N   GLN A 143     3222   6029   3370   -168    -15    -41       N  
-ATOM    980  CA  GLN A 143      32.179  -0.899  18.965  1.00 36.66           C  
-ANISOU  980  CA  GLN A 143     3461   6624   3844    -23    -52    -18       C  
-ATOM    981  C   GLN A 143      32.168  -0.238  20.336  1.00 39.87           C  
-ANISOU  981  C   GLN A 143     3901   6876   4371   -249   -282     -2       C  
-ATOM    982  O   GLN A 143      32.273  -0.904  21.371  1.00 40.08           O  
-ANISOU  982  O   GLN A 143     3960   6841   4428   -125   -364    -68       O  
-ATOM    983  CB  GLN A 143      33.581  -0.881  18.355  1.00 43.96           C  
-ANISOU  983  CB  GLN A 143     3974   8019   4710     31     70    175       C  
-ATOM    984  CG  GLN A 143      33.747  -1.848  17.183  1.00 49.71           C  
-ANISOU  984  CG  GLN A 143     4694   8931   5264    398    326    110       C  
-ATOM    985  CD  GLN A 143      35.192  -2.004  16.744  1.00 59.79           C  
-ANISOU  985  CD  GLN A 143     5507  10757   6455    565    485    299       C  
-ATOM    986  OE1 GLN A 143      36.013  -1.102  16.931  1.00 61.63           O  
-ANISOU  986  OE1 GLN A 143     5380  11291   6746    266    414    548       O  
-ATOM    987  NE2 GLN A 143      35.513  -3.156  16.159  1.00 64.76           N  
-ANISOU  987  NE2 GLN A 143     6150  11531   6927   1048    690    192       N  
-ATOM    988  N   THR A 144      32.023   1.081  20.337  1.00 38.85           N  
-ANISOU  988  N   THR A 144     3815   6658   4287   -578   -403     84       N  
-ATOM    989  CA  THR A 144      31.944   1.838  21.577  1.00 42.90           C  
-ANISOU  989  CA  THR A 144     4459   6972   4870   -792   -638     70       C  
-ATOM    990  C   THR A 144      30.702   1.418  22.343  1.00 37.80           C  
-ANISOU  990  C   THR A 144     4127   6017   4218   -636   -655   -145       C  
-ATOM    991  O   THR A 144      30.767   1.107  23.537  1.00 35.44           O  
-ANISOU  991  O   THR A 144     3887   5654   3925   -604   -763   -207       O  
-ATOM    992  CB  THR A 144      31.878   3.343  21.302  1.00 44.07           C  
-ANISOU  992  CB  THR A 144     4713   6991   5040  -1141   -782    179       C  
-ATOM    993  OG1 THR A 144      33.133   3.782  20.764  1.00 45.13           O  
-ANISOU  993  OG1 THR A 144     4519   7462   5166  -1379   -809    440       O  
-ATOM    994  CG2 THR A 144      31.575   4.106  22.577  1.00 49.99           C  
-ANISOU  994  CG2 THR A 144     5738   7440   5816  -1296  -1027     96       C  
-ATOM    995  N   LEU A 145      29.571   1.389  21.646  1.00 34.17           N  
-ANISOU  995  N   LEU A 145     3845   5407   3730   -553   -552   -232       N  
-ATOM    996  CA  LEU A 145      28.307   1.044  22.279  1.00 31.40           C  
-ANISOU  996  CA  LEU A 145     3732   4842   3357   -434   -556   -386       C  
-ATOM    997  C   LEU A 145      28.302  -0.402  22.776  1.00 37.48           C  
-ANISOU  997  C   LEU A 145     4497   5656   4089   -234   -511   -452       C  
-ATOM    998  O   LEU A 145      27.857  -0.681  23.898  1.00 38.58           O  
-ANISOU  998  O   LEU A 145     4752   5701   4207   -207   -584   -523       O  
-ATOM    999  CB  LEU A 145      27.130   1.306  21.344  1.00 33.60           C  
-ANISOU  999  CB  LEU A 145     4141   5015   3612   -408   -475   -413       C  
-ATOM   1000  CG  LEU A 145      25.770   1.014  21.981  1.00 39.41           C  
-ANISOU 1000  CG  LEU A 145     5047   5616   4313   -304   -475   -520       C  
-ATOM   1001  CD1 LEU A 145      25.620   1.774  23.291  1.00 40.65           C  
-ANISOU 1001  CD1 LEU A 145     5319   5656   4470   -331   -591   -584       C  
-ATOM   1002  CD2 LEU A 145      24.636   1.361  21.033  1.00 40.83           C  
-ANISOU 1002  CD2 LEU A 145     5298   5739   4475   -290   -423   -502       C  
-ATOM   1003  N   LEU A 146      28.811  -1.315  21.954  1.00 31.28           N  
-ANISOU 1003  N   LEU A 146     3609   5007   3269    -83   -399   -427       N  
-ATOM   1004  CA  LEU A 146      28.896  -2.716  22.355  1.00 32.83           C  
-ANISOU 1004  CA  LEU A 146     3867   5188   3421    128   -393   -484       C  
-ATOM   1005  C   LEU A 146      29.702  -2.866  23.652  1.00 34.31           C  
-ANISOU 1005  C   LEU A 146     3958   5429   3649    131   -523   -451       C  
-ATOM   1006  O   LEU A 146      29.315  -3.620  24.544  1.00 34.58           O  
-ANISOU 1006  O   LEU A 146     4136   5351   3652    194   -597   -502       O  
-ATOM   1007  CB  LEU A 146      29.511  -3.563  21.236  1.00 32.90           C  
-ANISOU 1007  CB  LEU A 146     3815   5326   3360    351   -257   -477       C  
-ATOM   1008  CG  LEU A 146      28.544  -3.914  20.109  1.00 33.18           C  
-ANISOU 1008  CG  LEU A 146     4063   5244   3298    382   -169   -544       C  
-ATOM   1009  CD1 LEU A 146      29.288  -4.384  18.867  1.00 29.06           C  
-ANISOU 1009  CD1 LEU A 146     3485   4891   2668    590    -13   -541       C  
-ATOM   1010  CD2 LEU A 146      27.565  -4.980  20.575  1.00 34.59           C  
-ANISOU 1010  CD2 LEU A 146     4530   5191   3420    428   -253   -628       C  
-ATOM   1011  N   SER A 147      30.801  -2.130  23.770  1.00 36.31           N  
-ANISOU 1011  N   SER A 147     3970   5869   3958     20   -577   -338       N  
-ATOM   1012  CA  SER A 147      31.669  -2.260  24.945  1.00 38.98           C  
-ANISOU 1012  CA  SER A 147     4189   6296   4326     -3   -733   -275       C  
-ATOM   1013  C   SER A 147      30.982  -1.841  26.248  1.00 43.49           C  
-ANISOU 1013  C   SER A 147     4987   6663   4874   -157   -886   -354       C  
-ATOM   1014  O   SER A 147      31.412  -2.243  27.334  1.00 43.57           O  
-ANISOU 1014  O   SER A 147     4993   6693   4867   -146  -1020   -334       O  
-ATOM   1015  CB  SER A 147      32.976  -1.490  24.762  1.00 45.84           C  
-ANISOU 1015  CB  SER A 147     4723   7448   5245   -163   -793    -90       C  
-ATOM   1016  OG  SER A 147      32.800  -0.109  25.004  1.00 52.25           O  
-ANISOU 1016  OG  SER A 147     5620   8154   6078   -503   -924    -60       O  
-ATOM   1017  N   LEU A 148      29.924  -1.040  26.134  1.00 42.09           N  
-ANISOU 1017  N   LEU A 148     5009   6310   4675   -268   -861   -439       N  
-ATOM   1018  CA  LEU A 148      29.121  -0.630  27.288  1.00 41.66           C  
-ANISOU 1018  CA  LEU A 148     5188   6090   4550   -337   -952   -538       C  
-ATOM   1019  C   LEU A 148      28.014  -1.637  27.587  1.00 40.79           C  
-ANISOU 1019  C   LEU A 148     5224   5912   4362   -194   -871   -612       C  
-ATOM   1020  O   LEU A 148      27.832  -2.066  28.731  1.00 41.52           O  
-ANISOU 1020  O   LEU A 148     5416   5987   4373   -187   -946   -636       O  
-ATOM   1021  CB  LEU A 148      28.496   0.752  27.055  1.00 41.44           C  
-ANISOU 1021  CB  LEU A 148     5311   5917   4518   -460   -966   -589       C  
-ATOM   1022  CG  LEU A 148      27.493   1.198  28.128  1.00 45.09           C  
-ANISOU 1022  CG  LEU A 148     6038   6229   4866   -429  -1003   -722       C  
-ATOM   1023  CD1 LEU A 148      28.156   1.344  29.498  1.00 43.81           C  
-ANISOU 1023  CD1 LEU A 148     5967   6056   4624   -526  -1188   -742       C  
-ATOM   1024  CD2 LEU A 148      26.782   2.492  27.742  1.00 51.11           C  
-ANISOU 1024  CD2 LEU A 148     6978   6822   5620   -445  -1000   -783       C  
-ATOM   1025  N   VAL A 149      27.275  -2.003  26.545  1.00 34.42           N  
-ANISOU 1025  N   VAL A 149     4435   5082   3562   -118   -736   -623       N  
-ATOM   1026  CA  VAL A 149      26.139  -2.915  26.658  1.00 34.60           C  
-ANISOU 1026  CA  VAL A 149     4589   5055   3503    -59   -687   -647       C  
-ATOM   1027  C   VAL A 149      26.534  -4.260  27.277  1.00 43.81           C  
-ANISOU 1027  C   VAL A 149     5805   6216   4627     15   -763   -613       C  
-ATOM   1028  O   VAL A 149      25.775  -4.846  28.063  1.00 40.99           O  
-ANISOU 1028  O   VAL A 149     5572   5829   4171    -22   -802   -602       O  
-ATOM   1029  CB  VAL A 149      25.469  -3.117  25.289  1.00 36.53           C  
-ANISOU 1029  CB  VAL A 149     4846   5278   3756    -33   -578   -638       C  
-ATOM   1030  CG1 VAL A 149      24.448  -4.268  25.329  1.00 37.53           C  
-ANISOU 1030  CG1 VAL A 149     5111   5361   3790    -35   -583   -616       C  
-ATOM   1031  CG2 VAL A 149      24.805  -1.832  24.863  1.00 34.69           C  
-ANISOU 1031  CG2 VAL A 149     4604   5029   3547    -96   -531   -653       C  
-ATOM   1032  N   ARG A 150      27.734  -4.730  26.945  1.00 39.44           N  
-ANISOU 1032  N   ARG A 150     5143   5710   4133    129   -789   -576       N  
-ATOM   1033  CA  ARG A 150      28.213  -6.001  27.474  1.00 40.59           C  
-ANISOU 1033  CA  ARG A 150     5358   5818   4247    262   -883   -539       C  
-ATOM   1034  C   ARG A 150      28.378  -5.964  28.995  1.00 42.90           C  
-ANISOU 1034  C   ARG A 150     5681   6127   4492    173  -1029   -508       C  
-ATOM   1035  O   ARG A 150      28.298  -6.999  29.657  1.00 41.03           O  
-ANISOU 1035  O   ARG A 150     5583   5817   4189    217  -1130   -465       O  
-ATOM   1036  CB  ARG A 150      29.521  -6.413  26.794  1.00 41.73           C  
-ANISOU 1036  CB  ARG A 150     5335   6065   4455    483   -860   -501       C  
-ATOM   1037  CG  ARG A 150      29.332  -6.675  25.301  1.00 44.65           C  
-ANISOU 1037  CG  ARG A 150     5744   6414   4807    609   -709   -547       C  
-ATOM   1038  CD  ARG A 150      30.389  -7.589  24.715  1.00 49.34           C  
-ANISOU 1038  CD  ARG A 150     6285   7076   5387    944   -670   -537       C  
-ATOM   1039  NE  ARG A 150      30.080  -7.908  23.321  1.00 54.90           N  
-ANISOU 1039  NE  ARG A 150     7116   7730   6013   1071   -529   -610       N  
-ATOM   1040  CZ  ARG A 150      30.696  -7.373  22.268  1.00 59.78           C  
-ANISOU 1040  CZ  ARG A 150     7520   8567   6627   1154   -366   -594       C  
-ATOM   1041  NH1 ARG A 150      31.676  -6.490  22.443  1.00 60.40           N  
-ANISOU 1041  NH1 ARG A 150     7220   8940   6791   1093   -338   -481       N  
-ATOM   1042  NH2 ARG A 150      30.338  -7.727  21.036  1.00 57.07           N  
-ANISOU 1042  NH2 ARG A 150     7352   8162   6170   1265   -249   -672       N  
-ATOM   1043  N   GLN A 151      28.594  -4.773  29.545  1.00 39.84           N  
-ANISOU 1043  N   GLN A 151     5212   5811   4114     33  -1064   -526       N  
-ATOM   1044  CA  GLN A 151      28.791  -4.636  30.985  1.00 42.55           C  
-ANISOU 1044  CA  GLN A 151     5621   6173   4373    -63  -1214   -512       C  
-ATOM   1045  C   GLN A 151      27.504  -4.848  31.783  1.00 44.87           C  
-ANISOU 1045  C   GLN A 151     6122   6420   4505   -130  -1187   -550       C  
-ATOM   1046  O   GLN A 151      27.552  -5.042  32.992  1.00 42.42           O  
-ANISOU 1046  O   GLN A 151     5881   6136   4100   -194  -1260   -514       O  
-ATOM   1047  CB  GLN A 151      29.429  -3.290  31.315  1.00 41.61           C  
-ANISOU 1047  CB  GLN A 151     5427   6105   4276   -214  -1298   -528       C  
-ATOM   1048  CG  GLN A 151      30.806  -3.116  30.696  1.00 42.44           C  
-ANISOU 1048  CG  GLN A 151     5258   6350   4516   -209  -1353   -420       C  
-ATOM   1049  CD  GLN A 151      31.401  -1.748  30.942  1.00 42.66           C  
-ANISOU 1049  CD  GLN A 151     5242   6410   4558   -450  -1484   -395       C  
-ATOM   1050  OE1 GLN A 151      31.470  -1.283  32.079  1.00 41.81           O  
-ANISOU 1050  OE1 GLN A 151     5285   6249   4350   -597  -1654   -423       O  
-ATOM   1051  NE2 GLN A 151      31.838  -1.092  29.867  1.00 40.48           N  
-ANISOU 1051  NE2 GLN A 151     4790   6209   4380   -518  -1426   -333       N  
-ATOM   1052  N   TYR A 152      26.356  -4.812  31.107  1.00 43.32           N  
-ANISOU 1052  N   TYR A 152     5973   6199   4288   -129  -1042   -582       N  
-ATOM   1053  CA  TYR A 152      25.072  -5.123  31.757  1.00 45.96           C  
-ANISOU 1053  CA  TYR A 152     6396   6579   4486   -202   -963   -549       C  
-ATOM   1054  C   TYR A 152      24.739  -6.622  31.685  1.00 41.51           C  
-ANISOU 1054  C   TYR A 152     5916   5964   3890   -212  -1013   -439       C  
-ATOM   1055  O   TYR A 152      23.619  -7.037  32.002  1.00 44.73           O  
-ANISOU 1055  O   TYR A 152     6363   6425   4209   -285   -961   -368       O  
-ATOM   1056  CB  TYR A 152      23.934  -4.256  31.183  1.00 42.72           C  
-ANISOU 1056  CB  TYR A 152     5984   6186   4063   -196   -818   -595       C  
-ATOM   1057  CG  TYR A 152      24.065  -2.811  31.602  1.00 42.73           C  
-ANISOU 1057  CG  TYR A 152     6004   6174   4056   -175   -788   -696       C  
-ATOM   1058  CD1 TYR A 152      23.449  -2.346  32.762  1.00 39.32           C  
-ANISOU 1058  CD1 TYR A 152     5678   5794   3467   -165   -747   -726       C  
-ATOM   1059  CD2 TYR A 152      24.843  -1.922  30.866  1.00 42.70           C  
-ANISOU 1059  CD2 TYR A 152     5950   6101   4173   -168   -825   -761       C  
-ATOM   1060  CE1 TYR A 152      23.587  -1.037  33.167  1.00 41.24           C  
-ANISOU 1060  CE1 TYR A 152     6008   5988   3674   -135   -739   -845       C  
-ATOM   1061  CE2 TYR A 152      24.984  -0.608  31.260  1.00 40.51           C  
-ANISOU 1061  CE2 TYR A 152     5764   5756   3873   -185   -852   -847       C  
-ATOM   1062  CZ  TYR A 152      24.350  -0.171  32.415  1.00 45.00           C  
-ANISOU 1062  CZ  TYR A 152     6468   6342   4287   -153   -807   -903       C  
-ATOM   1063  OH  TYR A 152      24.485   1.135  32.828  1.00 46.03           O  
-ANISOU 1063  OH  TYR A 152     6747   6361   4382   -136   -846  -1013       O  
-ATOM   1064  N   ASN A 153      25.742  -7.408  31.296  1.00 63.94           N  
-ANISOU 1064  N   ASN A 153     9290   9908   5097    505  -2450    561       N  
-ATOM   1065  CA  ASN A 153      25.635  -8.857  31.123  1.00 59.88           C  
-ANISOU 1065  CA  ASN A 153     8810   9296   4644    701  -2406    748       C  
-ATOM   1066  C   ASN A 153      24.318  -9.370  30.527  1.00 54.75           C  
-ANISOU 1066  C   ASN A 153     8312   8461   4030    749  -2112    786       C  
-ATOM   1067  O   ASN A 153      23.514 -10.016  31.200  1.00 56.46           O  
-ANISOU 1067  O   ASN A 153     8773   8573   4104    796  -1972    899       O  
-ATOM   1068  CB  ASN A 153      26.010  -9.585  32.410  1.00 64.90           C  
-ANISOU 1068  CB  ASN A 153     9600   9971   5090    793  -2539    895       C  
-ATOM   1069  CG  ASN A 153      27.491  -9.428  32.749  1.00 71.94           C  
-ANISOU 1069  CG  ASN A 153    10265  11054   6014    793  -2863    910       C  
-ATOM   1070  OD1 ASN A 153      28.359  -9.668  31.906  1.00 71.94           O  
-ANISOU 1070  OD1 ASN A 153     9976  11103   6255    853  -2979    935       O  
-ATOM   1071  ND2 ASN A 153      27.784  -9.002  33.978  1.00 77.57           N  
-ANISOU 1071  ND2 ASN A 153    11100  11884   6489    731  -3004    894       N  
-ATOM   1072  N   PRO A 154      24.094  -9.060  29.249  1.00 46.22           N  
-ANISOU 1072  N   PRO A 154     7072   7347   3141    726  -2015    696       N  
-ATOM   1073  CA  PRO A 154      22.950  -9.608  28.517  1.00 44.35           C  
-ANISOU 1073  CA  PRO A 154     6935   6951   2967    773  -1766    741       C  
-ATOM   1074  C   PRO A 154      23.184 -11.084  28.238  1.00 43.88           C  
-ANISOU 1074  C   PRO A 154     6876   6793   3003    968  -1781    910       C  
-ATOM   1075  O   PRO A 154      24.318 -11.544  28.327  1.00 49.94           O  
-ANISOU 1075  O   PRO A 154     7500   7636   3840   1083  -1977    963       O  
-ATOM   1076  CB  PRO A 154      22.999  -8.844  27.195  1.00 43.82           C  
-ANISOU 1076  CB  PRO A 154     6610   6905   3133    680  -1693    589       C  
-ATOM   1077  CG  PRO A 154      24.455  -8.526  27.034  1.00 42.45           C  
-ANISOU 1077  CG  PRO A 154     6182   6906   3040    709  -1958    542       C  
-ATOM   1078  CD  PRO A 154      24.935  -8.201  28.397  1.00 45.42           C  
-ANISOU 1078  CD  PRO A 154     6678   7365   3215    649  -2138    559       C  
-ATOM   1079  N   LYS A 155      22.122 -11.807  27.899  1.00 48.24           N  
-ANISOU 1079  N   LYS A 155     7565   7161   3602    977  -1556    992       N  
-ATOM   1080  CA  LYS A 155      22.240 -13.197  27.492  1.00 52.73           C  
-ANISOU 1080  CA  LYS A 155     8158   7581   4297   1136  -1540   1132       C  
-ATOM   1081  C   LYS A 155      22.903 -13.213  26.119  1.00 48.86           C  
-ANISOU 1081  C   LYS A 155     7372   7106   4087   1185  -1555   1032       C  
-ATOM   1082  O   LYS A 155      23.766 -14.039  25.821  1.00 51.53           O  
-ANISOU 1082  O   LYS A 155     7626   7430   4521   1378  -1667   1099       O  
-ATOM   1083  CB  LYS A 155      20.844 -13.816  27.410  1.00 59.69           C  
-ANISOU 1083  CB  LYS A 155     9235   8248   5198   1056  -1279   1221       C  
-ATOM   1084  CG  LYS A 155      20.794 -15.331  27.270  1.00 67.43           C  
-ANISOU 1084  CG  LYS A 155    10347   9019   6254   1194  -1260   1392       C  
-ATOM   1085  CD  LYS A 155      19.755 -15.912  28.229  1.00 72.51           C  
-ANISOU 1085  CD  LYS A 155    11297   9527   6726   1138  -1115   1570       C  
-ATOM   1086  CE  LYS A 155      19.507 -17.394  27.984  1.00 75.52           C  
-ANISOU 1086  CE  LYS A 155    11832   9646   7214   1222  -1062   1738       C  
-ATOM   1087  NZ  LYS A 155      18.843 -17.627  26.670  1.00 74.59           N  
-ANISOU 1087  NZ  LYS A 155    11600   9372   7369   1111   -913   1651       N  
-ATOM   1088  N   MET A 156      22.492 -12.262  25.292  1.00 41.91           N  
-ANISOU 1088  N   MET A 156     6342   6257   3325   1023  -1431    874       N  
-ATOM   1089  CA  MET A 156      22.893 -12.213  23.899  1.00 40.64           C  
-ANISOU 1089  CA  MET A 156     5938   6094   3408   1044  -1386    777       C  
-ATOM   1090  C   MET A 156      22.803 -10.747  23.456  1.00 42.92           C  
-ANISOU 1090  C   MET A 156     6066   6505   3738    857  -1343    609       C  
-ATOM   1091  O   MET A 156      21.939 -10.009  23.942  1.00 41.24           O  
-ANISOU 1091  O   MET A 156     5976   6283   3411    709  -1255    567       O  
-ATOM   1092  CB  MET A 156      21.926 -13.087  23.088  1.00 43.14           C  
-ANISOU 1092  CB  MET A 156     6358   6180   3851   1039  -1192    811       C  
-ATOM   1093  CG  MET A 156      22.048 -12.977  21.593  1.00 44.49           C  
-ANISOU 1093  CG  MET A 156     6345   6323   4234   1034  -1108    695       C  
-ATOM   1094  SD  MET A 156      20.578 -13.602  20.721  1.00 54.41           S  
-ANISOU 1094  SD  MET A 156     7747   7326   5601    925   -897    693       S  
-ATOM   1095  CE  MET A 156      20.441 -15.256  21.417  1.00 40.68           C  
-ANISOU 1095  CE  MET A 156     6278   5369   3811   1066   -928    886       C  
-ATOM   1096  N   VAL A 157      23.703 -10.322  22.564  1.00 39.46           N  
-ANISOU 1096  N   VAL A 157     5362   6175   3456    875  -1394    523       N  
-ATOM   1097  CA  VAL A 157      23.621  -9.001  21.934  1.00 35.38           C  
-ANISOU 1097  CA  VAL A 157     4696   5736   3010    698  -1332    376       C  
-ATOM   1098  C   VAL A 157      23.711  -9.162  20.431  1.00 34.38           C  
-ANISOU 1098  C   VAL A 157     4406   5566   3092    729  -1205    323       C  
-ATOM   1099  O   VAL A 157      24.623  -9.826  19.939  1.00 39.10           O  
-ANISOU 1099  O   VAL A 157     4864   6202   3792    892  -1255    360       O  
-ATOM   1100  CB  VAL A 157      24.784  -8.072  22.316  1.00 41.07           C  
-ANISOU 1100  CB  VAL A 157     5231   6664   3710    643  -1530    318       C  
-ATOM   1101  CG1 VAL A 157      24.452  -6.632  21.908  1.00 39.14           C  
-ANISOU 1101  CG1 VAL A 157     4928   6447   3495    427  -1453    177       C  
-ATOM   1102  CG2 VAL A 157      25.057  -8.124  23.756  1.00 45.83           C  
-ANISOU 1102  CG2 VAL A 157     5980   7335   4098    664  -1723    378       C  
-ATOM   1103  N   LYS A 158      22.772  -8.552  19.711  1.00 30.40           N  
-ANISOU 1103  N   LYS A 158     3926   4986   2639    590  -1041    242       N  
-ATOM   1104  CA  LYS A 158      22.785  -8.533  18.261  1.00 29.14           C  
-ANISOU 1104  CA  LYS A 158     3640   4791   2639    598   -924    180       C  
-ATOM   1105  C   LYS A 158      22.617  -7.091  17.852  1.00 31.00           C  
-ANISOU 1105  C   LYS A 158     3781   5097   2901    418   -871     74       C  
-ATOM   1106  O   LYS A 158      22.030  -6.300  18.594  1.00 31.33           O  
-ANISOU 1106  O   LYS A 158     3923   5140   2842    293   -872     45       O  
-ATOM   1107  CB  LYS A 158      21.618  -9.340  17.689  1.00 32.68           C  
-ANISOU 1107  CB  LYS A 158     4252   5041   3124    604   -786    202       C  
-ATOM   1108  CG  LYS A 158      21.647 -10.822  18.021  1.00 36.87           C  
-ANISOU 1108  CG  LYS A 158     4926   5444   3640    764   -821    311       C  
-ATOM   1109  CD  LYS A 158      22.869 -11.508  17.434  1.00 45.04           C  
-ANISOU 1109  CD  LYS A 158     5838   6514   4759    971   -875    321       C  
-ATOM   1110  CE  LYS A 158      22.811 -13.011  17.683  1.00 47.96           C  
-ANISOU 1110  CE  LYS A 158     6394   6706   5120   1144   -898    426       C  
-ATOM   1111  NZ  LYS A 158      24.085 -13.669  17.317  1.00 47.29           N  
-ANISOU 1111  NZ  LYS A 158     6193   6670   5107   1393   -957    450       N  
-ATOM   1112  N   VAL A 159      23.130  -6.750  16.677  1.00 27.40           N  
-ANISOU 1112  N   VAL A 159     3154   4689   2570    418   -812     20       N  
-ATOM   1113  CA  VAL A 159      22.976  -5.401  16.145  1.00 26.35           C  
-ANISOU 1113  CA  VAL A 159     2943   4595   2471    251   -748    -66       C  
-ATOM   1114  C   VAL A 159      22.286  -5.441  14.792  1.00 26.09           C  
-ANISOU 1114  C   VAL A 159     2931   4465   2517    245   -589   -101       C  
-ATOM   1115  O   VAL A 159      22.710  -6.160  13.889  1.00 30.21           O  
-ANISOU 1115  O   VAL A 159     3394   4976   3107    367   -543    -91       O  
-ATOM   1116  CB  VAL A 159      24.346  -4.700  15.997  1.00 27.67           C  
-ANISOU 1116  CB  VAL A 159     2869   4937   2709    215   -832    -86       C  
-ATOM   1117  CG1 VAL A 159      24.199  -3.327  15.322  1.00 28.04           C  
-ANISOU 1117  CG1 VAL A 159     2857   4993   2805     35   -750   -162       C  
-ATOM   1118  CG2 VAL A 159      25.006  -4.566  17.352  1.00 29.47           C  
-ANISOU 1118  CG2 VAL A 159     3080   5269   2848    194  -1033    -61       C  
-ATOM   1119  N   ALA A 160      21.206  -4.664  14.668  1.00 26.46           N  
-ANISOU 1119  N   ALA A 160     3071   4439   2542    118   -510   -141       N  
-ATOM   1120  CA  ALA A 160      20.547  -4.424  13.398  1.00 25.25           C  
-ANISOU 1120  CA  ALA A 160     2928   4216   2451     86   -391   -177       C  
-ATOM   1121  C   ALA A 160      20.865  -2.999  12.946  1.00 25.28           C  
-ANISOU 1121  C   ALA A 160     2836   4283   2485    -36   -356   -230       C  
-ATOM   1122  O   ALA A 160      20.638  -2.053  13.685  1.00 26.37           O  
-ANISOU 1122  O   ALA A 160     3014   4427   2579   -144   -382   -257       O  
-ATOM   1123  CB  ALA A 160      19.043  -4.611  13.536  1.00 22.00           C  
-ANISOU 1123  CB  ALA A 160     2669   3676   2014     43   -334   -162       C  
-ATOM   1124  N   SER A 161      21.374  -2.839  11.730  1.00 23.59           N  
-ANISOU 1124  N   SER A 161     2524   4103   2336    -18   -287   -243       N  
-ATOM   1125  CA  SER A 161      21.627  -1.501  11.202  1.00 23.23           C  
-ANISOU 1125  CA  SER A 161     2408   4095   2324   -145   -237   -273       C  
-ATOM   1126  C   SER A 161      20.937  -1.388   9.879  1.00 26.29           C  
-ANISOU 1126  C   SER A 161     2857   4409   2725   -135   -124   -282       C  
-ATOM   1127  O   SER A 161      21.074  -2.278   9.035  1.00 24.14           O  
-ANISOU 1127  O   SER A 161     2589   4127   2456    -20    -80   -274       O  
-ATOM   1128  CB  SER A 161      23.128  -1.250  11.038  1.00 28.63           C  
-ANISOU 1128  CB  SER A 161     2881   4925   3072   -155   -259   -258       C  
-ATOM   1129  OG  SER A 161      23.385   0.076  10.611  1.00 26.62           O  
-ANISOU 1129  OG  SER A 161     2569   4689   2857   -311   -211   -274       O  
-ATOM   1130  N   LEU A 162      20.173  -0.312   9.699  1.00 22.74           N  
-ANISOU 1130  N   LEU A 162     2475   3896   2267   -240    -84   -299       N  
-ATOM   1131  CA  LEU A 162      19.447  -0.104   8.446  1.00 23.76           C  
-ANISOU 1131  CA  LEU A 162     2672   3959   2396   -231     -2   -296       C  
-ATOM   1132  C   LEU A 162      20.440  -0.047   7.296  1.00 22.85           C  
-ANISOU 1132  C   LEU A 162     2469   3917   2296   -201     77   -283       C  
-ATOM   1133  O   LEU A 162      20.250  -0.680   6.255  1.00 25.75           O  
-ANISOU 1133  O   LEU A 162     2892   4260   2632   -111    127   -284       O  
-ATOM   1134  CB  LEU A 162      18.660   1.211   8.483  1.00 25.38           C  
-ANISOU 1134  CB  LEU A 162     2946   4095   2601   -334     27   -302       C  
-ATOM   1135  CG  LEU A 162      18.029   1.540   7.119  1.00 26.52           C  
-ANISOU 1135  CG  LEU A 162     3151   4187   2737   -319     92   -283       C  
-ATOM   1136  CD1 LEU A 162      16.947   0.530   6.750  1.00 24.81           C  
-ANISOU 1136  CD1 LEU A 162     3009   3913   2503   -241     59   -278       C  
-ATOM   1137  CD2 LEU A 162      17.479   2.958   7.113  1.00 25.51           C  
-ANISOU 1137  CD2 LEU A 162     3082   3989   2620   -402    125   -275       C  
-ATOM   1138  N   LEU A 163      21.510   0.719   7.492  1.00 22.11           N  
-ANISOU 1138  N   LEU A 163     2242   3912   2247   -285     90   -271       N  
-ATOM   1139  CA  LEU A 163      22.512   0.884   6.444  1.00 24.22           C  
-ANISOU 1139  CA  LEU A 163     2394   4267   2540   -271    198   -238       C  
-ATOM   1140  C   LEU A 163      23.893   0.503   6.939  1.00 26.13           C  
-ANISOU 1140  C   LEU A 163     2421   4658   2849   -243    171   -215       C  
-ATOM   1141  O   LEU A 163      24.215   0.684   8.111  1.00 26.30           O  
-ANISOU 1141  O   LEU A 163     2375   4716   2901   -314     49   -224       O  
-ATOM   1142  CB  LEU A 163      22.555   2.334   5.978  1.00 23.99           C  
-ANISOU 1142  CB  LEU A 163     2371   4213   2532   -427    266   -213       C  
-ATOM   1143  CG  LEU A 163      21.230   2.966   5.551  1.00 27.47           C  
-ANISOU 1143  CG  LEU A 163     3004   4512   2921   -454    281   -219       C  
-ATOM   1144  CD1 LEU A 163      21.420   4.456   5.289  1.00 28.57           C  
-ANISOU 1144  CD1 LEU A 163     3158   4606   3092   -608    337   -185       C  
-ATOM   1145  CD2 LEU A 163      20.650   2.275   4.314  1.00 25.68           C  
-ANISOU 1145  CD2 LEU A 163     2882   4257   2619   -328    340   -209       C  
-ATOM   1146  N   VAL A 164      24.709  -0.014   6.022  1.00 25.42           N  
-ANISOU 1146  N   VAL A 164     2226   4658   2774   -130    285   -182       N  
-ATOM   1147  CA  VAL A 164      26.137  -0.241   6.257  1.00 27.43           C  
-ANISOU 1147  CA  VAL A 164     2217   5085   3120    -94    293   -136       C  
-ATOM   1148  C   VAL A 164      26.878   0.300   5.053  1.00 28.91           C  
-ANISOU 1148  C   VAL A 164     2287   5362   3338   -116    485    -78       C  
-ATOM   1149  O   VAL A 164      26.579  -0.076   3.917  1.00 28.83           O  
-ANISOU 1149  O   VAL A 164     2399   5311   3243      4    625    -81       O  
-ATOM   1150  CB  VAL A 164      26.483  -1.735   6.406  1.00 28.01           C  
-ANISOU 1150  CB  VAL A 164     2263   5194   3184    146    273   -138       C  
-ATOM   1151  CG1 VAL A 164      27.997  -1.921   6.474  1.00 30.51           C  
-ANISOU 1151  CG1 VAL A 164     2269   5712   3611    216    305    -72       C  
-ATOM   1152  CG2 VAL A 164      25.807  -2.310   7.641  1.00 26.87           C  
-ANISOU 1152  CG2 VAL A 164     2239   4965   3006    163     94   -171       C  
-ATOM   1153  N   LYS A 165      27.833   1.188   5.294  1.00 30.54           N  
-ANISOU 1153  N   LYS A 165     2266   5684   3656   -281    489    -22       N  
-ATOM   1154  CA  LYS A 165      28.599   1.787   4.213  1.00 32.64           C  
-ANISOU 1154  CA  LYS A 165     2394   6043   3965   -333    692     59       C  
-ATOM   1155  C   LYS A 165      29.769   0.914   3.836  1.00 39.41           C  
-ANISOU 1155  C   LYS A 165     3000   7088   4885   -144    809    117       C  
-ATOM   1156  O   LYS A 165      30.469   0.388   4.715  1.00 36.03           O  
-ANISOU 1156  O   LYS A 165     2365   6774   4550    -88    686    127       O  
-ATOM   1157  CB  LYS A 165      29.129   3.159   4.615  1.00 40.03           C  
-ANISOU 1157  CB  LYS A 165     3186   7009   5017   -625    649    106       C  
-ATOM   1158  CG  LYS A 165      28.123   4.286   4.521  1.00 42.69           C  
-ANISOU 1158  CG  LYS A 165     3776   7152   5294   -801    631     78       C  
-ATOM   1159  CD  LYS A 165      28.830   5.592   4.135  1.00 43.52           C  
-ANISOU 1159  CD  LYS A 165     3760   7278   5499  -1051    722    165       C  
-ATOM   1160  CE  LYS A 165      27.829   6.718   4.163  1.00 39.09           C  
-ANISOU 1160  CE  LYS A 165     3472   6497   4883  -1204    686    135       C  
-ATOM   1161  NZ  LYS A 165      28.438   8.055   4.224  1.00 35.03           N  
-ANISOU 1161  NZ  LYS A 165     2884   5946   4482  -1493    698    195       N  
-ATOM   1162  N   ARG A 166      29.991   0.772   2.529  1.00 38.92           N  
-ANISOU 1162  N   ARG A 166     2963   7062   4762    -29   1052    159       N  
-ATOM   1163  CA  ARG A 166      31.211   0.162   2.026  1.00 44.24           C  
-ANISOU 1163  CA  ARG A 166     3373   7932   5504    149   1229    233       C  
-ATOM   1164  C   ARG A 166      32.330   1.178   2.076  1.00 50.28           C  
-ANISOU 1164  C   ARG A 166     3789   8872   6444    -69   1298    353       C  
-ATOM   1165  O   ARG A 166      32.350   2.145   1.312  1.00 53.45           O  
-ANISOU 1165  O   ARG A 166     4217   9258   6833   -233   1453    418       O  
-ATOM   1166  CB  ARG A 166      31.041  -0.304   0.582  1.00 43.64           C  
-ANISOU 1166  CB  ARG A 166     3482   7829   5271    351   1487    232       C  
-ATOM   1167  CG  ARG A 166      30.252  -1.582   0.439  1.00 40.39           C  
-ANISOU 1167  CG  ARG A 166     3359   7277   4711    604   1434    119       C  
-ATOM   1168  CD  ARG A 166      30.468  -2.167  -0.954  1.00 45.33           C  
-ANISOU 1168  CD  ARG A 166     4116   7919   5188    841   1701    117       C  
-ATOM   1169  NE  ARG A 166      30.036  -1.226  -1.979  1.00 39.17           N  
-ANISOU 1169  NE  ARG A 166     3505   7093   4286    707   1837    152       N  
-ATOM   1170  CZ  ARG A 166      28.764  -0.983  -2.271  1.00 36.98           C  
-ANISOU 1170  CZ  ARG A 166     3557   6628   3866    629   1730     85       C  
-ATOM   1171  NH1 ARG A 166      27.806  -1.620  -1.617  1.00 34.75           N  
-ANISOU 1171  NH1 ARG A 166     3451   6195   3558    657   1502    -20       N  
-ATOM   1172  NH2 ARG A 166      28.452  -0.114  -3.222  1.00 45.44           N  
-ANISOU 1172  NH2 ARG A 166     4773   7667   4824    528   1851    136       N  
-ATOM   1173  N   THR A 167      33.270   0.964   2.978  1.00 53.89           N  
-ANISOU 1173  N   THR A 167     3915   9492   7067    -81   1173    392       N  
-ATOM   1174  CA  THR A 167      34.372   1.889   3.090  1.00 61.36           C  
-ANISOU 1174  CA  THR A 167     4557  10547   8211   -311   1186    495       C  
-ATOM   1175  C   THR A 167      35.630   1.116   3.456  1.00 67.97           C  
-ANISOU 1175  C   THR A 167     5087  11530   9210   -143   1152    544       C  
-ATOM   1176  O   THR A 167      35.583   0.200   4.279  1.00 68.48           O  
-ANISOU 1176  O   THR A 167     5122  11632   9266     27    978    500       O  
-ATOM   1177  CB  THR A 167      34.043   3.030   4.104  1.00 64.29           C  
-ANISOU 1177  CB  THR A 167     4940  10847   8639   -665    938    466       C  
-ATOM   1178  OG1 THR A 167      35.081   4.016   4.094  1.00 60.12           O  
-ANISOU 1178  OG1 THR A 167     4196  10343   8304   -907    947    552       O  
-ATOM   1179  CG2 THR A 167      33.853   2.489   5.519  1.00 62.71           C  
-ANISOU 1179  CG2 THR A 167     4720  10665   8441   -635    628    386       C  
-ATOM   1180  N   PRO A 168      36.756   1.454   2.810  1.00 74.81           N  
-ANISOU 1180  N   PRO A 168     5728  12477  10220   -178   1331    638       N  
-ATOM   1181  CA  PRO A 168      38.057   0.945   3.255  1.00 80.25           C  
-ANISOU 1181  CA  PRO A 168     6069  13319  11102    -78   1276    692       C  
-ATOM   1182  C   PRO A 168      38.340   1.429   4.679  1.00 83.00           C  
-ANISOU 1182  C   PRO A 168     6254  13697  11585   -308    926    681       C  
-ATOM   1183  O   PRO A 168      39.174   0.853   5.381  1.00 84.16           O  
-ANISOU 1183  O   PRO A 168     6161  13960  11858   -205    779    704       O  
-ATOM   1184  CB  PRO A 168      39.047   1.571   2.257  1.00 83.41           C  
-ANISOU 1184  CB  PRO A 168     6277  13789  11627   -170   1543    789       C  
-ATOM   1185  CG  PRO A 168      38.300   2.694   1.598  1.00 80.57           C  
-ANISOU 1185  CG  PRO A 168     6151  13292  11170   -410   1657    796       C  
-ATOM   1186  CD  PRO A 168      36.867   2.264   1.584  1.00 76.96           C  
-ANISOU 1186  CD  PRO A 168     6064  12706  10472   -292   1608    701       C  
-ATOM   1187  N   ARG A 169      37.622   2.477   5.087  1.00 80.97           N  
-ANISOU 1187  N   ARG A 169     6159  13322  11284   -608    790    640       N  
-ATOM   1188  CA  ARG A 169      37.713   3.058   6.427  1.00 80.44           C  
-ANISOU 1188  CA  ARG A 169     6040  13234  11291   -850    450    598       C  
-ATOM   1189  C   ARG A 169      37.097   2.178   7.520  1.00 77.06           C  
-ANISOU 1189  C   ARG A 169     5736  12800  10743   -696    196    515       C  
-ATOM   1190  O   ARG A 169      37.248   2.468   8.708  1.00 75.38           O  
-ANISOU 1190  O   ARG A 169     5497  12579  10565   -845   -100    475       O  
-ATOM   1191  CB  ARG A 169      37.039   4.440   6.452  1.00 79.63           C  
-ANISOU 1191  CB  ARG A 169     6142  12965  11149  -1194    409    563       C  
-ATOM   1192  CG  ARG A 169      37.992   5.627   6.576  1.00 82.91           C  
-ANISOU 1192  CG  ARG A 169     6362  13371  11769  -1512    361    615       C  
-ATOM   1193  CD  ARG A 169      37.342   6.938   6.120  1.00 81.36           C  
-ANISOU 1193  CD  ARG A 169     6402  12982  11529  -1790    443    611       C  
-ATOM   1194  NE  ARG A 169      36.492   7.561   7.136  1.00 78.57           N  
-ANISOU 1194  NE  ARG A 169     6309  12465  11080  -1981    179    496       N  
-ATOM   1195  CZ  ARG A 169      35.172   7.702   7.033  1.00 78.12           C  
-ANISOU 1195  CZ  ARG A 169     6589  12265  10829  -1973    202    425       C  
-ATOM   1196  NH1 ARG A 169      34.529   7.257   5.959  1.00 75.90           N  
-ANISOU 1196  NH1 ARG A 169     6425  11988  10425  -1791    458    458       N  
-ATOM   1197  NH2 ARG A 169      34.487   8.288   8.008  1.00 78.34           N  
-ANISOU 1197  NH2 ARG A 169     6848  12140  10777  -2140    -28    312       N  
-ATOM   1198  N   SER A 170      36.397   1.117   7.124  1.00 77.02           N  
-ANISOU 1198  N   SER A 170     5893  12786  10587   -401    309    485       N  
-ATOM   1199  CA  SER A 170      35.765   0.219   8.090  1.00 75.31           C  
-ANISOU 1199  CA  SER A 170     5811  12552  10251   -238     96    416       C  
-ATOM   1200  C   SER A 170      36.803  -0.457   8.974  1.00 77.12           C  
-ANISOU 1200  C   SER A 170     5803  12896  10603   -113   -100    463       C  
-ATOM   1201  O   SER A 170      37.749  -1.069   8.476  1.00 78.31           O  
-ANISOU 1201  O   SER A 170     5734  13150  10870     88     35    538       O  
-ATOM   1202  CB  SER A 170      34.916  -0.843   7.387  1.00 73.77           C  
-ANISOU 1202  CB  SER A 170     5824  12313   9894     71    274    377       C  
-ATOM   1203  OG  SER A 170      34.597  -1.906   8.273  1.00 71.07           O  
-ANISOU 1203  OG  SER A 170     5587  11937   9478    278     87    336       O  
-ATOM   1204  N   VAL A 171      36.615  -0.345  10.288  1.00 77.07           N  
-ANISOU 1204  N   VAL A 171     5862  12865  10558   -222   -416    415       N  
-ATOM   1205  CA  VAL A 171      37.514  -0.972  11.259  1.00 80.05           C  
-ANISOU 1205  CA  VAL A 171     6054  13338  11024   -109   -646    457       C  
-ATOM   1206  C   VAL A 171      37.277  -2.486  11.238  1.00 75.62           C  
-ANISOU 1206  C   VAL A 171     5571  12784  10377    286   -602    476       C  
-ATOM   1207  O   VAL A 171      37.998  -3.267  11.870  1.00 75.49           O  
-ANISOU 1207  O   VAL A 171     5419  12838  10425    467   -746    529       O  
-ATOM   1208  CB  VAL A 171      37.328  -0.371  12.682  1.00 88.36           C  
-ANISOU 1208  CB  VAL A 171     7220  14335  12019   -342   -999    391       C  
-ATOM   1209  CG1 VAL A 171      38.440  -0.817  13.616  1.00 91.70           C  
-ANISOU 1209  CG1 VAL A 171     7416  14870  12557   -267  -1246    443       C  
-ATOM   1210  CG2 VAL A 171      37.314   1.148  12.615  1.00 87.42           C  
-ANISOU 1210  CG2 VAL A 171     7123  14143  11951   -724  -1017    346       C  
-ATOM   1211  N   GLY A 172      36.262  -2.890  10.482  1.00 69.75           N  
-ANISOU 1211  N   GLY A 172     5059  11953   9489    422   -404    430       N  
-ATOM   1212  CA  GLY A 172      36.001  -4.294  10.249  1.00 69.66           C  
-ANISOU 1212  CA  GLY A 172     5160  11907   9400    800   -319    436       C  
-ATOM   1213  C   GLY A 172      34.777  -4.820  10.967  1.00 68.25           C  
-ANISOU 1213  C   GLY A 172     5322  11581   9030    860   -466    361       C  
-ATOM   1214  O   GLY A 172      34.461  -6.003  10.838  1.00 67.85           O  
-ANISOU 1214  O   GLY A 172     5452  11419   8909   1149   -411    356       O  
-ATOM   1215  N   TYR A 173      34.086  -3.959  11.717  1.00 65.29           N  
-ANISOU 1215  N   TYR A 173     5126  11111   8571    573   -634    293       N  
-ATOM   1216  CA  TYR A 173      32.894  -4.403  12.442  1.00 56.37           C  
-ANISOU 1216  CA  TYR A 173     4394   9764   7261    596   -743    222       C  
-ATOM   1217  C   TYR A 173      31.699  -4.654  11.517  1.00 53.22           C  
-ANISOU 1217  C   TYR A 173     4326   9140   6756    647   -525    148       C  
-ATOM   1218  O   TYR A 173      31.380  -3.828  10.662  1.00 48.58           O  
-ANISOU 1218  O   TYR A 173     3770   8513   6174    495   -368    110       O  
-ATOM   1219  CB  TYR A 173      32.487  -3.446  13.575  1.00 52.69           C  
-ANISOU 1219  CB  TYR A 173     4042   9264   6716    308   -971    167       C  
-ATOM   1220  CG  TYR A 173      31.163  -3.874  14.159  1.00 46.60           C  
-ANISOU 1220  CG  TYR A 173     3678   8270   5759    341  -1008    105       C  
-ATOM   1221  CD1 TYR A 173      31.093  -4.935  15.053  1.00 45.05           C  
-ANISOU 1221  CD1 TYR A 173     3590   8047   5480    530  -1151    148       C  
-ATOM   1222  CD2 TYR A 173      29.973  -3.265  13.763  1.00 41.64           C  
-ANISOU 1222  CD2 TYR A 173     3315   7460   5047    198   -883     21       C  
-ATOM   1223  CE1 TYR A 173      29.877  -5.365  15.553  1.00 41.80           C  
-ANISOU 1223  CE1 TYR A 173     3536   7436   4911    551  -1154    113       C  
-ATOM   1224  CE2 TYR A 173      28.756  -3.685  14.263  1.00 37.58           C  
-ANISOU 1224  CE2 TYR A 173     3128   6763   4388    230   -895    -18       C  
-ATOM   1225  CZ  TYR A 173      28.715  -4.735  15.152  1.00 40.28           C  
-ANISOU 1225  CZ  TYR A 173     3566   7084   4654    396  -1021     30       C  
-ATOM   1226  OH  TYR A 173      27.499  -5.151  15.642  1.00 45.55           O  
-ANISOU 1226  OH  TYR A 173     4545   7574   5188    410  -1010     10       O  
-ATOM   1227  N   LYS A 174      31.037  -5.793  11.726  1.00 53.07           N  
-ANISOU 1227  N   LYS A 174     4557   8967   6640    849   -536    136       N  
-ATOM   1228  CA  LYS A 174      29.872  -6.206  10.946  1.00 48.95           C  
-ANISOU 1228  CA  LYS A 174     4352   8225   6020    899   -378     68       C  
-ATOM   1229  C   LYS A 174      28.657  -6.437  11.841  1.00 39.40           C  
-ANISOU 1229  C   LYS A 174     3451   6833   4684    828   -499     32       C  
-ATOM   1230  O   LYS A 174      28.698  -7.269  12.743  1.00 38.31           O  
-ANISOU 1230  O   LYS A 174     3381   6667   4506    951   -633     77       O  
-ATOM   1231  CB  LYS A 174      30.175  -7.504  10.195  1.00 55.61           C  
-ANISOU 1231  CB  LYS A 174     5230   9023   6877   1218   -246     88       C  
-ATOM   1232  CG  LYS A 174      30.881  -7.331   8.859  1.00 62.76           C  
-ANISOU 1232  CG  LYS A 174     5963  10032   7851   1308    -12     93       C  
-ATOM   1233  CD  LYS A 174      32.075  -8.278   8.736  1.00 71.44           C  
-ANISOU 1233  CD  LYS A 174     6841  11260   9044   1626     38    169       C  
-ATOM   1234  CE  LYS A 174      31.848  -9.618   9.451  1.00 74.90           C  
-ANISOU 1234  CE  LYS A 174     7470  11554   9432   1863    -88    186       C  
-ATOM   1235  NZ  LYS A 174      30.915 -10.542   8.737  1.00 76.25           N  
-ANISOU 1235  NZ  LYS A 174     8023  11458   9491   1998     27    106       N  
-ATOM   1236  N   PRO A 175      27.560  -5.714  11.582  1.00 36.46           N  
-ANISOU 1236  N   PRO A 175     3266   6339   4247    641   -441    -35       N  
-ATOM   1237  CA  PRO A 175      26.360  -5.974  12.382  1.00 29.62           C  
-ANISOU 1237  CA  PRO A 175     2670   5312   3273    587   -518    -56       C  
-ATOM   1238  C   PRO A 175      25.743  -7.324  11.995  1.00 33.91           C  
-ANISOU 1238  C   PRO A 175     3416   5685   3781    772   -458    -49       C  
-ATOM   1239  O   PRO A 175      26.179  -7.946  11.021  1.00 36.38           O  
-ANISOU 1239  O   PRO A 175     3698   5991   4136    936   -350    -54       O  
-ATOM   1240  CB  PRO A 175      25.434  -4.821  11.998  1.00 31.57           C  
-ANISOU 1240  CB  PRO A 175     3014   5489   3491    372   -444   -120       C  
-ATOM   1241  CG  PRO A 175      25.860  -4.458  10.601  1.00 32.55           C  
-ANISOU 1241  CG  PRO A 175     3025   5661   3683    382   -283   -135       C  
-ATOM   1242  CD  PRO A 175      27.340  -4.674  10.560  1.00 33.23           C  
-ANISOU 1242  CD  PRO A 175     2832   5932   3863    489   -296    -79       C  
-ATOM   1243  N   ASP A 176      24.746  -7.764  12.753  1.00 28.48           N  
-ANISOU 1243  N   ASP A 176     2947   4859   3015    739   -520    -38       N  
-ATOM   1244  CA  ASP A 176      24.135  -9.077  12.561  1.00 31.94           C  
-ANISOU 1244  CA  ASP A 176     3594   5112   3429    876   -493    -20       C  
-ATOM   1245  C   ASP A 176      22.995  -9.055  11.548  1.00 31.41           C  
-ANISOU 1245  C   ASP A 176     3687   4896   3353    794   -383    -85       C  
-ATOM   1246  O   ASP A 176      22.763 -10.032  10.822  1.00 31.64           O  
-ANISOU 1246  O   ASP A 176     3852   4786   3385    909   -334   -103       O  
-ATOM   1247  CB  ASP A 176      23.617  -9.579  13.908  1.00 30.36           C  
-ANISOU 1247  CB  ASP A 176     3543   4839   3153    862   -607     48       C  
-ATOM   1248  CG  ASP A 176      24.693  -9.606  14.953  1.00 34.14           C  
-ANISOU 1248  CG  ASP A 176     3890   5467   3615    942   -754    116       C  
-ATOM   1249  OD1 ASP A 176      25.486 -10.569  14.931  1.00 36.16           O  
-ANISOU 1249  OD1 ASP A 176     4105   5728   3907   1161   -790    173       O  
-ATOM   1250  OD2 ASP A 176      24.765  -8.667  15.782  1.00 33.82           O  
-ANISOU 1250  OD2 ASP A 176     3792   5536   3521    798   -841    110       O  
-ATOM   1251  N   PHE A 177      22.282  -7.935  11.518  1.00 25.46           N  
-ANISOU 1251  N   PHE A 177     2927   4162   2583    598   -358   -121       N  
-ATOM   1252  CA  PHE A 177      21.162  -7.733  10.614  1.00 25.54           C  
-ANISOU 1252  CA  PHE A 177     3057   4060   2588    506   -281   -171       C  
-ATOM   1253  C   PHE A 177      21.413  -6.438   9.864  1.00 28.30           C  
-ANISOU 1253  C   PHE A 177     3283   4515   2955    408   -209   -214       C  
-ATOM   1254  O   PHE A 177      21.668  -5.410  10.484  1.00 31.47           O  
-ANISOU 1254  O   PHE A 177     3584   5013   3361    298   -238   -209       O  
-ATOM   1255  CB  PHE A 177      19.862  -7.625  11.414  1.00 23.23           C  
-ANISOU 1255  CB  PHE A 177     2887   3676   2265    374   -314   -145       C  
-ATOM   1256  CG  PHE A 177      19.611  -8.805  12.325  1.00 25.63           C  
-ANISOU 1256  CG  PHE A 177     3317   3879   2545    440   -375    -75       C  
-ATOM   1257  CD1 PHE A 177      19.111  -9.996  11.811  1.00 26.99           C  
-ANISOU 1257  CD1 PHE A 177     3641   3879   2736    499   -370    -68       C  
-ATOM   1258  CD2 PHE A 177      19.882  -8.720  13.691  1.00 26.22           C  
-ANISOU 1258  CD2 PHE A 177     3382   4016   2565    437   -445    -14       C  
-ATOM   1259  CE1 PHE A 177      18.888 -11.093  12.655  1.00 31.56           C  
-ANISOU 1259  CE1 PHE A 177     4354   4338   3299    549   -420     14       C  
-ATOM   1260  CE2 PHE A 177      19.658  -9.801  14.534  1.00 30.87           C  
-ANISOU 1260  CE2 PHE A 177     4107   4506   3116    502   -493     71       C  
-ATOM   1261  CZ  PHE A 177      19.159 -10.992  14.004  1.00 32.94           C  
-ANISOU 1261  CZ  PHE A 177     4514   4585   3417    555   -473     92       C  
-ATOM   1262  N   VAL A 178      21.369  -6.495   8.533  1.00 23.98           N  
-ANISOU 1262  N   VAL A 178     2769   3936   2406    448   -120   -255       N  
-ATOM   1263  CA  VAL A 178      21.648  -5.323   7.714  1.00 23.58           C  
-ANISOU 1263  CA  VAL A 178     2624   3975   2363    367    -34   -276       C  
-ATOM   1264  C   VAL A 178      20.530  -5.061   6.710  1.00 24.30           C  
-ANISOU 1264  C   VAL A 178     2859   3963   2412    302      7   -312       C  
-ATOM   1265  O   VAL A 178      20.153  -5.952   5.935  1.00 22.50           O  
-ANISOU 1265  O   VAL A 178     2771   3635   2145    386     15   -343       O  
-ATOM   1266  CB  VAL A 178      22.961  -5.497   6.930  1.00 29.74           C  
-ANISOU 1266  CB  VAL A 178     3270   4866   3163    500     63   -272       C  
-ATOM   1267  CG1 VAL A 178      23.193  -4.319   5.980  1.00 30.18           C  
-ANISOU 1267  CG1 VAL A 178     3252   4997   3217    404    176   -275       C  
-ATOM   1268  CG2 VAL A 178      24.124  -5.650   7.890  1.00 32.28           C  
-ANISOU 1268  CG2 VAL A 178     3396   5321   3547    560      1   -223       C  
-ATOM   1269  N   GLY A 179      20.014  -3.836   6.683  1.00 22.89           N  
-ANISOU 1269  N   GLY A 179     2659   3801   2237    159     20   -308       N  
-ATOM   1270  CA  GLY A 179      19.026  -3.507   5.667  1.00 22.95           C  
-ANISOU 1270  CA  GLY A 179     2782   3732   2206    115     44   -326       C  
-ATOM   1271  C   GLY A 179      19.638  -3.391   4.284  1.00 22.82           C  
-ANISOU 1271  C   GLY A 179     2781   3755   2136    181    146   -342       C  
-ATOM   1272  O   GLY A 179      19.316  -4.160   3.364  1.00 25.21           O  
-ANISOU 1272  O   GLY A 179     3224   3984   2370    263    149   -378       O  
-ATOM   1273  N   PHE A 180      20.549  -2.428   4.124  1.00 21.68           N  
-ANISOU 1273  N   PHE A 180     2504   3721   2013    139    233   -313       N  
-ATOM   1274  CA  PHE A 180      21.103  -2.123   2.814  1.00 23.52           C  
-ANISOU 1274  CA  PHE A 180     2747   4003   2185    184    365   -304       C  
-ATOM   1275  C   PHE A 180      22.586  -1.859   2.969  1.00 24.33           C  
-ANISOU 1275  C   PHE A 180     2636   4257   2351    204    462   -263       C  
-ATOM   1276  O   PHE A 180      22.994  -1.205   3.929  1.00 26.24           O  
-ANISOU 1276  O   PHE A 180     2729   4558   2681     93    413   -236       O  
-ATOM   1277  CB  PHE A 180      20.434  -0.864   2.247  1.00 24.14           C  
-ANISOU 1277  CB  PHE A 180     2888   4049   2235     60    389   -275       C  
-ATOM   1278  CG  PHE A 180      18.950  -1.002   2.075  1.00 25.08           C  
-ANISOU 1278  CG  PHE A 180     3170   4047   2314     37    282   -297       C  
-ATOM   1279  CD1 PHE A 180      18.083  -0.808   3.146  1.00 24.49           C  
-ANISOU 1279  CD1 PHE A 180     3078   3918   2308    -40    182   -294       C  
-ATOM   1280  CD2 PHE A 180      18.426  -1.346   0.835  1.00 26.45           C  
-ANISOU 1280  CD2 PHE A 180     3507   4168   2375     97    282   -316       C  
-ATOM   1281  CE1 PHE A 180      16.711  -0.964   2.978  1.00 19.50           C  
-ANISOU 1281  CE1 PHE A 180     2547   3195   1665    -60     92   -297       C  
-ATOM   1282  CE2 PHE A 180      17.061  -1.500   0.662  1.00 28.30           C  
-ANISOU 1282  CE2 PHE A 180     3856   4306   2590     63    156   -328       C  
-ATOM   1283  CZ  PHE A 180      16.211  -1.316   1.733  1.00 20.07           C  
-ANISOU 1283  CZ  PHE A 180     2752   3225   1649    -16     66   -311       C  
-ATOM   1284  N   GLU A 181      23.378  -2.332   2.017  1.00 25.63           N  
-ANISOU 1284  N   GLU A 181     2785   4486   2468    342    599   -259       N  
-ATOM   1285  CA  GLU A 181      24.801  -2.016   1.996  1.00 29.81           C  
-ANISOU 1285  CA  GLU A 181     3069   5184   3074    360    722   -198       C  
-ATOM   1286  C   GLU A 181      25.012  -0.991   0.885  1.00 33.15           C  
-ANISOU 1286  C   GLU A 181     3499   5650   3447    281    886   -145       C  
-ATOM   1287  O   GLU A 181      24.702  -1.253  -0.284  1.00 30.28           O  
-ANISOU 1287  O   GLU A 181     3318   5243   2946    378    986   -162       O  
-ATOM   1288  CB  GLU A 181      25.644  -3.265   1.733  1.00 29.07           C  
-ANISOU 1288  CB  GLU A 181     2925   5150   2971    603    802   -211       C  
-ATOM   1289  CG  GLU A 181      27.141  -3.011   1.858  1.00 36.13           C  
-ANISOU 1289  CG  GLU A 181     3498   6248   3980    634    917   -132       C  
-ATOM   1290  CD  GLU A 181      27.981  -4.135   1.291  1.00 40.25           C  
-ANISOU 1290  CD  GLU A 181     3979   6835   4479    918   1060   -135       C  
-ATOM   1291  OE1 GLU A 181      28.121  -4.196   0.053  1.00 39.74           O  
-ANISOU 1291  OE1 GLU A 181     4018   6779   4303   1022   1257   -139       O  
-ATOM   1292  OE2 GLU A 181      28.493  -4.949   2.087  1.00 41.33           O  
-ANISOU 1292  OE2 GLU A 181     3997   7010   4697   1051    980   -129       O  
-ATOM   1293  N   ILE A 182      25.537   0.177   1.247  1.00 30.53           N  
-ANISOU 1293  N   ILE A 182     2992   5393   3216     98    907    -78       N  
-ATOM   1294  CA  ILE A 182      25.526   1.320   0.341  1.00 29.29           C  
-ANISOU 1294  CA  ILE A 182     2881   5231   3019    -24   1038    -11       C  
-ATOM   1295  C   ILE A 182      26.936   1.797   0.010  1.00 31.78           C  
-ANISOU 1295  C   ILE A 182     2936   5717   3422    -72   1218     88       C  
-ATOM   1296  O   ILE A 182      27.881   1.521   0.754  1.00 34.33           O  
-ANISOU 1296  O   ILE A 182     2997   6168   3878    -68   1189    107       O  
-ATOM   1297  CB  ILE A 182      24.677   2.482   0.925  1.00 27.83           C  
-ANISOU 1297  CB  ILE A 182     2779   4926   2870   -231    913    -10       C  
-ATOM   1298  CG1 ILE A 182      25.302   3.032   2.206  1.00 29.10           C  
-ANISOU 1298  CG1 ILE A 182     2734   5139   3184   -391    811     -2       C  
-ATOM   1299  CG2 ILE A 182      23.243   2.040   1.189  1.00 26.19           C  
-ANISOU 1299  CG2 ILE A 182     2790   4571   2589   -180    762    -86       C  
-ATOM   1300  CD1 ILE A 182      24.749   4.398   2.624  1.00 31.72           C  
-ANISOU 1300  CD1 ILE A 182     3152   5351   3550   -602    745      7       C  
-ATOM   1301  N   PRO A 183      27.100   2.499  -1.128  1.00 33.06           N  
-ANISOU 1301  N   PRO A 183     3158   5892   3510   -115   1408    167       N  
-ATOM   1302  CA  PRO A 183      28.432   3.033  -1.416  1.00 35.74           C  
-ANISOU 1302  CA  PRO A 183     3223   6400   3957   -195   1599    285       C  
-ATOM   1303  C   PRO A 183      28.793   4.180  -0.477  1.00 35.98           C  
-ANISOU 1303  C   PRO A 183     3069   6433   4168   -483   1491    333       C  
-ATOM   1304  O   PRO A 183      27.956   4.616   0.329  1.00 34.02           O  
-ANISOU 1304  O   PRO A 183     2951   6043   3935   -598   1290    268       O  
-ATOM   1305  CB  PRO A 183      28.314   3.537  -2.867  1.00 36.99           C  
-ANISOU 1305  CB  PRO A 183     3560   6537   3957   -179   1826    365       C  
-ATOM   1306  CG  PRO A 183      26.861   3.719  -3.104  1.00 34.75           C  
-ANISOU 1306  CG  PRO A 183     3621   6055   3527   -180   1687    299       C  
-ATOM   1307  CD  PRO A 183      26.151   2.719  -2.238  1.00 33.50           C  
-ANISOU 1307  CD  PRO A 183     3523   5828   3377    -73   1463    165       C  
-ATOM   1308  N   ASP A 184      30.032   4.655  -0.582  1.00 39.18           N  
-ANISOU 1308  N   ASP A 184     3178   6998   4712   -598   1627    445       N  
-ATOM   1309  CA  ASP A 184      30.516   5.756   0.250  1.00 46.78           C  
-ANISOU 1309  CA  ASP A 184     3957   7961   5855   -903   1517    491       C  
-ATOM   1310  C   ASP A 184      29.966   7.098  -0.245  1.00 46.05           C  
-ANISOU 1310  C   ASP A 184     4078   7696   5723  -1117   1569    548       C  
-ATOM   1311  O   ASP A 184      30.694   7.894  -0.833  1.00 45.03           O  
-ANISOU 1311  O   ASP A 184     3829   7618   5663  -1280   1745    681       O  
-ATOM   1312  CB  ASP A 184      32.051   5.787   0.250  1.00 51.42           C  
-ANISOU 1312  CB  ASP A 184     4120   8789   6628   -974   1640    608       C  
-ATOM   1313  CG  ASP A 184      32.628   6.638   1.380  1.00 57.53           C  
-ANISOU 1313  CG  ASP A 184     4686   9563   7609  -1273   1433    618       C  
-ATOM   1314  OD1 ASP A 184      31.856   7.351   2.056  1.00 58.07           O  
-ANISOU 1314  OD1 ASP A 184     4951   9458   7654  -1450   1248    546       O  
-ATOM   1315  OD2 ASP A 184      33.862   6.593   1.582  1.00 62.45           O  
-ANISOU 1315  OD2 ASP A 184     5009  10297   8420  -1302   1436    677       O  
-ATOM   1316  N   LYS A 185      28.677   7.328  -0.015  1.00 41.29           N  
-ANISOU 1316  N   LYS A 185     3786   6888   5013  -1106   1426    460       N  
-ATOM   1317  CA  LYS A 185      28.019   8.577  -0.400  1.00 43.00           C  
-ANISOU 1317  CA  LYS A 185     4237   6913   5189  -1268   1448    509       C  
-ATOM   1318  C   LYS A 185      27.292   9.055   0.834  1.00 35.18           C  
-ANISOU 1318  C   LYS A 185     3355   5763   4249  -1379   1201    402       C  
-ATOM   1319  O   LYS A 185      26.854   8.237   1.628  1.00 33.38           O  
-ANISOU 1319  O   LYS A 185     3134   5547   4000  -1255   1045    290       O  
-ATOM   1320  CB  LYS A 185      26.952   8.323  -1.470  1.00 40.46           C  
-ANISOU 1320  CB  LYS A 185     4226   6494   4655  -1078   1522    507       C  
-ATOM   1321  CG  LYS A 185      27.452   7.909  -2.834  1.00 51.80           C  
-ANISOU 1321  CG  LYS A 185     5664   8048   5968   -941   1778    600       C  
-ATOM   1322  CD  LYS A 185      26.258   7.556  -3.722  1.00 54.33           C  
-ANISOU 1322  CD  LYS A 185     6324   8261   6058   -752   1768    564       C  
-ATOM   1323  CE  LYS A 185      26.280   8.326  -5.028  1.00 56.44           C  
-ANISOU 1323  CE  LYS A 185     6764   8492   6189   -781   1973    707       C  
-ATOM   1324  NZ  LYS A 185      27.507   8.034  -5.800  1.00 57.55           N  
-ANISOU 1324  NZ  LYS A 185     6735   8823   6310   -736   2254    808       N  
-ATOM   1325  N   PHE A 186      27.130  10.364   0.994  1.00 35.93           N  
-ANISOU 1325  N   PHE A 186     3563   5693   4397  -1600   1177    438       N  
-ATOM   1326  CA  PHE A 186      26.379  10.858   2.154  1.00 34.58           C  
-ANISOU 1326  CA  PHE A 186     3539   5352   4247  -1677    965    325       C  
-ATOM   1327  C   PHE A 186      24.881  10.810   1.888  1.00 34.20           C  
-ANISOU 1327  C   PHE A 186     3792   5146   4058  -1502    933    278       C  
-ATOM   1328  O   PHE A 186      24.404  11.370   0.893  1.00 38.75           O  
-ANISOU 1328  O   PHE A 186     4544   5620   4557  -1479   1044    362       O  
-ATOM   1329  CB  PHE A 186      26.800  12.283   2.516  1.00 40.20           C  
-ANISOU 1329  CB  PHE A 186     4280   5919   5076  -1980    938    364       C  
-ATOM   1330  CG  PHE A 186      26.398  12.684   3.902  1.00 44.06           C  
-ANISOU 1330  CG  PHE A 186     4870   6276   5596  -2071    717    228       C  
-ATOM   1331  CD1 PHE A 186      25.172  13.290   4.134  1.00 46.58           C  
-ANISOU 1331  CD1 PHE A 186     5500   6363   5835  -2016    665    168       C  
-ATOM   1332  CD2 PHE A 186      27.242  12.437   4.977  1.00 49.37           C  
-ANISOU 1332  CD2 PHE A 186     5328   7063   6366  -2193    560    163       C  
-ATOM   1333  CE1 PHE A 186      24.789  13.650   5.424  1.00 51.71           C  
-ANISOU 1333  CE1 PHE A 186     6268   6890   6489  -2075    490     37       C  
-ATOM   1334  CE2 PHE A 186      26.872  12.789   6.270  1.00 53.33           C  
-ANISOU 1334  CE2 PHE A 186     5962   7443   6857  -2268    355     30       C  
-ATOM   1335  CZ  PHE A 186      25.644  13.401   6.493  1.00 53.47           C  
-ANISOU 1335  CZ  PHE A 186     6312   7222   6782  -2206    335    -38       C  
-ATOM   1336  N   VAL A 187      24.143  10.133   2.766  1.00 30.30           N  
-ANISOU 1336  N   VAL A 187     3343   4639   3529  -1379    780    160       N  
-ATOM   1337  CA  VAL A 187      22.707   9.994   2.588  1.00 29.57           C  
-ANISOU 1337  CA  VAL A 187     3479   4426   3329  -1215    739    122       C  
-ATOM   1338  C   VAL A 187      21.943  10.568   3.771  1.00 33.30           C  
-ANISOU 1338  C   VAL A 187     4078   4747   3825  -1259    603     32       C  
-ATOM   1339  O   VAL A 187      22.462  10.632   4.892  1.00 28.59           O  
-ANISOU 1339  O   VAL A 187     3398   4171   3292  -1366    502    -38       O  
-ATOM   1340  CB  VAL A 187      22.281   8.520   2.372  1.00 29.53           C  
-ANISOU 1340  CB  VAL A 187     3442   4535   3241   -993    714     76       C  
-ATOM   1341  CG1 VAL A 187      22.867   7.975   1.080  1.00 27.75           C  
-ANISOU 1341  CG1 VAL A 187     3165   4429   2950   -907    868    151       C  
-ATOM   1342  CG2 VAL A 187      22.685   7.667   3.559  1.00 32.33           C  
-ANISOU 1342  CG2 VAL A 187     3645   4991   3650   -975    596     -9       C  
-ATOM   1343  N   VAL A 188      20.707  10.985   3.514  1.00 26.83           N  
-ANISOU 1343  N   VAL A 188     3466   3782   2948  -1162    600     38       N  
-ATOM   1344  CA  VAL A 188      19.864  11.582   4.547  1.00 26.41           C  
-ANISOU 1344  CA  VAL A 188     3554   3575   2905  -1161    512    -39       C  
-ATOM   1345  C   VAL A 188      18.463  11.030   4.386  1.00 26.00           C  
-ANISOU 1345  C   VAL A 188     3586   3505   2788   -951    485    -49       C  
-ATOM   1346  O   VAL A 188      18.184  10.353   3.408  1.00 25.74           O  
-ANISOU 1346  O   VAL A 188     3531   3548   2699   -842    515      2       O  
-ATOM   1347  CB  VAL A 188      19.831  13.127   4.429  1.00 29.19           C  
-ANISOU 1347  CB  VAL A 188     4084   3713   3294  -1291    555      1       C  
-ATOM   1348  CG1 VAL A 188      21.189  13.741   4.769  1.00 30.08           C  
-ANISOU 1348  CG1 VAL A 188     4107   3824   3496  -1550    552      3       C  
-ATOM   1349  CG2 VAL A 188      19.367  13.546   3.023  1.00 28.52           C  
-ANISOU 1349  CG2 VAL A 188     4114   3563   3160  -1217    660    130       C  
-ATOM   1350  N   GLY A 189      17.582  11.318   5.340  1.00 27.04           N  
-ANISOU 1350  N   GLY A 189     3814   3537   2923   -898    431   -115       N  
-ATOM   1351  CA  GLY A 189      16.218  10.833   5.251  1.00 23.20           C  
-ANISOU 1351  CA  GLY A 189     3366   3045   2404   -714    409   -109       C  
-ATOM   1352  C   GLY A 189      15.965   9.611   6.109  1.00 23.91           C  
-ANISOU 1352  C   GLY A 189     3351   3251   2483   -647    344   -176       C  
-ATOM   1353  O   GLY A 189      16.911   8.978   6.607  1.00 26.16           O  
-ANISOU 1353  O   GLY A 189     3528   3640   2770   -716    310   -220       O  
-ATOM   1354  N   TYR A 190      14.687   9.283   6.288  1.00 23.12           N  
-ANISOU 1354  N   TYR A 190     3271   3134   2378   -513    327   -171       N  
-ATOM   1355  CA  TYR A 190      14.277   8.205   7.191  1.00 23.21           C  
-ANISOU 1355  CA  TYR A 190     3207   3228   2384   -456    282   -217       C  
-ATOM   1356  C   TYR A 190      14.968   8.355   8.551  1.00 25.77           C  
-ANISOU 1356  C   TYR A 190     3549   3551   2691   -538    263   -300       C  
-ATOM   1357  O   TYR A 190      15.516   7.390   9.094  1.00 24.90           O  
-ANISOU 1357  O   TYR A 190     3354   3547   2562   -555    212   -330       O  
-ATOM   1358  CB  TYR A 190      14.577   6.846   6.532  1.00 20.79           C  
-ANISOU 1358  CB  TYR A 190     2792   3048   2061   -431    240   -199       C  
-ATOM   1359  CG  TYR A 190      13.847   5.672   7.170  1.00 24.09           C  
-ANISOU 1359  CG  TYR A 190     3153   3518   2482   -362    194   -213       C  
-ATOM   1360  CD1 TYR A 190      12.460   5.557   7.087  1.00 25.57           C  
-ANISOU 1360  CD1 TYR A 190     3339   3677   2701   -280    187   -172       C  
-ATOM   1361  CD2 TYR A 190      14.546   4.685   7.855  1.00 21.10           C  
-ANISOU 1361  CD2 TYR A 190     2713   3217   2087   -382    157   -251       C  
-ATOM   1362  CE1 TYR A 190      11.782   4.482   7.685  1.00 26.04           C  
-ANISOU 1362  CE1 TYR A 190     3335   3778   2779   -246    156   -166       C  
-ATOM   1363  CE2 TYR A 190      13.883   3.607   8.446  1.00 23.74           C  
-ANISOU 1363  CE2 TYR A 190     3018   3577   2424   -331    124   -246       C  
-ATOM   1364  CZ  TYR A 190      12.504   3.511   8.360  1.00 26.20           C  
-ANISOU 1364  CZ  TYR A 190     3328   3854   2772   -277    130   -203       C  
-ATOM   1365  OH  TYR A 190      11.855   2.428   8.952  1.00 25.94           O  
-ANISOU 1365  OH  TYR A 190     3256   3843   2758   -254    108   -182       O  
-ATOM   1366  N   ALA A 191      14.927   9.586   9.080  1.00 25.25           N  
-ANISOU 1366  N   ALA A 191     3618   3353   2623   -582    293   -337       N  
-ATOM   1367  CA  ALA A 191      15.532  10.001  10.355  1.00 26.20           C  
-ANISOU 1367  CA  ALA A 191     3815   3436   2703   -674    256   -432       C  
-ATOM   1368  C   ALA A 191      17.036  10.290  10.313  1.00 26.44           C  
-ANISOU 1368  C   ALA A 191     3794   3499   2753   -863    193   -457       C  
-ATOM   1369  O   ALA A 191      17.565  10.863  11.253  1.00 28.80           O  
-ANISOU 1369  O   ALA A 191     4178   3742   3022   -972    135   -537       O  
-ATOM   1370  CB  ALA A 191      15.181   9.043  11.531  1.00 23.22           C  
-ANISOU 1370  CB  ALA A 191     3414   3145   2263   -605    225   -475       C  
-ATOM   1371  N   LEU A 192      17.716   9.917   9.228  1.00 28.65           N  
-ANISOU 1371  N   LEU A 192     3936   3870   3080   -903    206   -387       N  
-ATOM   1372  CA  LEU A 192      19.131  10.273   9.082  1.00 30.24           C  
-ANISOU 1372  CA  LEU A 192     4048   4115   3329  -1085    174   -384       C  
-ATOM   1373  C   LEU A 192      19.285  11.756   8.746  1.00 28.22           C  
-ANISOU 1373  C   LEU A 192     3931   3679   3111  -1218    219   -369       C  
-ATOM   1374  O   LEU A 192      18.588  12.282   7.878  1.00 28.14           O  
-ANISOU 1374  O   LEU A 192     4021   3565   3105  -1150    305   -304       O  
-ATOM   1375  CB  LEU A 192      19.821   9.407   8.020  1.00 30.48           C  
-ANISOU 1375  CB  LEU A 192     3888   4304   3390  -1063    213   -306       C  
-ATOM   1376  CG  LEU A 192      20.159   7.971   8.435  1.00 33.74           C  
-ANISOU 1376  CG  LEU A 192     4151   4885   3784   -975    151   -325       C  
-ATOM   1377  CD1 LEU A 192      18.968   7.040   8.312  1.00 31.86           C  
-ANISOU 1377  CD1 LEU A 192     3962   4647   3496   -795    162   -320       C  
-ATOM   1378  CD2 LEU A 192      21.327   7.437   7.610  1.00 37.07           C  
-ANISOU 1378  CD2 LEU A 192     4378   5454   4252   -997    192   -267       C  
-ATOM   1379  N   ASP A 193      20.200  12.443   9.416  1.00 27.87           N  
-ANISOU 1379  N   ASP A 193     3905   3589   3096  -1416    146   -425       N  
-ATOM   1380  CA  ASP A 193      20.266  13.883   9.259  1.00 29.67           C  
-ANISOU 1380  CA  ASP A 193     4315   3598   3360  -1556    176   -424       C  
-ATOM   1381  C   ASP A 193      21.532  14.400   8.586  1.00 37.88           C  
-ANISOU 1381  C   ASP A 193     5234   4656   4500  -1791    192   -350       C  
-ATOM   1382  O   ASP A 193      22.554  13.711   8.504  1.00 36.08           O  
-ANISOU 1382  O   ASP A 193     4757   4630   4321  -1868    156   -321       O  
-ATOM   1383  CB  ASP A 193      20.174  14.564  10.619  1.00 30.97           C  
-ANISOU 1383  CB  ASP A 193     4677   3617   3474  -1632     78   -562       C  
-ATOM   1384  CG  ASP A 193      21.463  14.454  11.398  1.00 32.45           C  
-ANISOU 1384  CG  ASP A 193     4744   3904   3684  -1849    -78   -625       C  
-ATOM   1385  OD1 ASP A 193      21.968  13.326  11.547  1.00 37.53           O  
-ANISOU 1385  OD1 ASP A 193     5157   4776   4327  -1810   -137   -608       O  
-ATOM   1386  OD2 ASP A 193      21.966  15.495  11.844  1.00 35.67           O  
-ANISOU 1386  OD2 ASP A 193     5288   4152   4114  -2058   -153   -688       O  
-ATOM   1387  N   TYR A 194      21.436  15.638   8.123  1.00 32.99           N  
-ANISOU 1387  N   TYR A 194     4796   3820   3918  -1895    255   -308       N  
-ATOM   1388  CA  TYR A 194      22.597  16.457   7.833  1.00 35.49           C  
-ANISOU 1388  CA  TYR A 194     5063   4082   4340  -2183    254   -256       C  
-ATOM   1389  C   TYR A 194      22.475  17.688   8.702  1.00 37.50           C  
-ANISOU 1389  C   TYR A 194     5597   4057   4596  -2332    171   -362       C  
-ATOM   1390  O   TYR A 194      21.656  18.574   8.433  1.00 39.52           O  
-ANISOU 1390  O   TYR A 194     6122   4065   4828  -2261    247   -348       O  
-ATOM   1391  CB  TYR A 194      22.627  16.839   6.365  1.00 35.95           C  
-ANISOU 1391  CB  TYR A 194     5122   4103   4433  -2185    423    -88       C  
-ATOM   1392  CG  TYR A 194      23.852  17.618   5.983  1.00 43.18           C  
-ANISOU 1392  CG  TYR A 194     5954   4981   5471  -2496    455     -2       C  
-ATOM   1393  CD1 TYR A 194      25.099  17.008   5.948  1.00 47.77           C  
-ANISOU 1393  CD1 TYR A 194     6203   5808   6139  -2638    436     38       C  
-ATOM   1394  CD2 TYR A 194      23.765  18.954   5.649  1.00 52.49           C  
-ANISOU 1394  CD2 TYR A 194     7375   5877   6691  -2644    510     54       C  
-ATOM   1395  CE1 TYR A 194      26.227  17.711   5.589  1.00 54.96           C  
-ANISOU 1395  CE1 TYR A 194     6993   6705   7185  -2939    477    136       C  
-ATOM   1396  CE2 TYR A 194      24.887  19.675   5.293  1.00 57.72           C  
-ANISOU 1396  CE2 TYR A 194     7954   6495   7481  -2960    547    150       C  
-ATOM   1397  CZ  TYR A 194      26.114  19.045   5.265  1.00 61.08           C  
-ANISOU 1397  CZ  TYR A 194     8016   7190   8002  -3115    532    193       C  
-ATOM   1398  OH  TYR A 194      27.235  19.748   4.905  1.00 72.43           O  
-ANISOU 1398  OH  TYR A 194     9325   8608   9589  -3415    575    306       O  
-ATOM   1399  N   ASN A 195      23.279  17.738   9.760  1.00 46.34           N  
-ANISOU 1399  N   ASN A 195     6666   5208   5733  -2526      3   -471       N  
-ATOM   1400  CA  ASN A 195      23.187  18.798  10.755  1.00 44.37           C  
-ANISOU 1400  CA  ASN A 195     6716   4693   5451  -2667   -108   -611       C  
-ATOM   1401  C   ASN A 195      21.750  19.094  11.220  1.00 40.11           C  
-ANISOU 1401  C   ASN A 195     6500   3958   4781  -2402    -49   -701       C  
-ATOM   1402  O   ASN A 195      21.299  20.246  11.225  1.00 41.75           O  
-ANISOU 1402  O   ASN A 195     7018   3862   4985  -2425     -6   -731       O  
-ATOM   1403  CB  ASN A 195      23.926  20.045  10.279  1.00 56.36           C  
-ANISOU 1403  CB  ASN A 195     8322   5998   7094  -2979    -99   -551       C  
-ATOM   1404  CG  ASN A 195      25.413  19.791  10.110  1.00 66.95           C  
-ANISOU 1404  CG  ASN A 195     9316   7547   8576  -3271   -180   -480       C  
-ATOM   1405  OD1 ASN A 195      26.001  18.982  10.831  1.00 69.37           O  
-ANISOU 1405  OD1 ASN A 195     9397   8086   8873  -3287   -329   -542       O  
-ATOM   1406  ND2 ASN A 195      26.025  20.466   9.151  1.00 73.26           N  
-ANISOU 1406  ND2 ASN A 195    10041   8288   9509  -3428    -74   -328       N  
-ATOM   1407  N   GLU A 196      21.065  18.011  11.592  1.00 37.65           N  
-ANISOU 1407  N   GLU A 196     6101   3829   4376  -2149    -39   -730       N  
-ATOM   1408  CA  GLU A 196      19.711  17.997  12.169  1.00 43.39           C  
-ANISOU 1408  CA  GLU A 196     7046   4456   4983  -1875     24   -805       C  
-ATOM   1409  C   GLU A 196      18.577  18.153  11.156  1.00 43.14           C  
-ANISOU 1409  C   GLU A 196     7069   4350   4974  -1640    196   -690       C  
-ATOM   1410  O   GLU A 196      17.414  17.906  11.485  1.00 40.74           O  
-ANISOU 1410  O   GLU A 196     6847   4034   4600  -1387    263   -715       O  
-ATOM   1411  CB  GLU A 196      19.564  18.969  13.350  1.00 39.03           C  
-ANISOU 1411  CB  GLU A 196     6839   3650   4339  -1939    -49   -976       C  
-ATOM   1412  CG  GLU A 196      20.406  18.591  14.568  1.00 43.83           C  
-ANISOU 1412  CG  GLU A 196     7417   4369   4867  -2101   -250  -1110       C  
-ATOM   1413  CD  GLU A 196      20.157  17.170  15.077  1.00 47.98           C  
-ANISOU 1413  CD  GLU A 196     7744   5180   5305  -1919   -273  -1109       C  
-ATOM   1414  OE1 GLU A 196      19.007  16.677  15.022  1.00 42.37           O  
-ANISOU 1414  OE1 GLU A 196     7056   4505   4540  -1643   -136  -1077       O  
-ATOM   1415  OE2 GLU A 196      21.125  16.540  15.547  1.00 54.64           O  
-ANISOU 1415  OE2 GLU A 196     8405   6213   6143  -2058   -435  -1130       O  
-ATOM   1416  N   TYR A 197      18.920  18.516   9.920  1.00 37.68           N  
-ANISOU 1416  N   TYR A 197     6313   3627   4376  -1723    266   -551       N  
-ATOM   1417  CA  TYR A 197      17.928  18.568   8.845  1.00 37.17           C  
-ANISOU 1417  CA  TYR A 197     6276   3527   4319  -1504    397   -423       C  
-ATOM   1418  C   TYR A 197      17.761  17.230   8.142  1.00 33.80           C  
-ANISOU 1418  C   TYR A 197     5572   3387   3884  -1370    420   -336       C  
-ATOM   1419  O   TYR A 197      18.627  16.360   8.244  1.00 31.51           O  
-ANISOU 1419  O   TYR A 197     5059   3309   3605  -1470    362   -345       O  
-ATOM   1420  CB  TYR A 197      18.284  19.643   7.824  1.00 43.64           C  
-ANISOU 1420  CB  TYR A 197     7217   4154   5212  -1636    467   -303       C  
-ATOM   1421  CG  TYR A 197      18.072  21.022   8.370  1.00 53.64           C  
-ANISOU 1421  CG  TYR A 197     8828   5069   6482  -1695    466   -377       C  
-ATOM   1422  CD1 TYR A 197      16.813  21.604   8.353  1.00 55.73           C  
-ANISOU 1422  CD1 TYR A 197     9324   5137   6712  -1436    546   -371       C  
-ATOM   1423  CD2 TYR A 197      19.118  21.727   8.941  1.00 60.92           C  
-ANISOU 1423  CD2 TYR A 197     9846   5852   7448  -2006    377   -457       C  
-ATOM   1424  CE1 TYR A 197      16.605  22.859   8.870  1.00 62.99           C  
-ANISOU 1424  CE1 TYR A 197    10593   5711   7629  -1459    558   -448       C  
-ATOM   1425  CE2 TYR A 197      18.925  22.987   9.455  1.00 67.00           C  
-ANISOU 1425  CE2 TYR A 197    10976   6266   8213  -2067    367   -542       C  
-ATOM   1426  CZ  TYR A 197      17.666  23.549   9.420  1.00 69.14           C  
-ANISOU 1426  CZ  TYR A 197    11505   6328   8438  -1780    468   -541       C  
-ATOM   1427  OH  TYR A 197      17.471  24.808   9.938  1.00 75.64           O  
-ANISOU 1427  OH  TYR A 197    12719   6770   9249  -1813    470   -634       O  
-ATOM   1428  N   PHE A 198      16.639  17.098   7.430  1.00 31.21           N  
-ANISOU 1428  N   PHE A 198     5270   3052   3538  -1140    494   -252       N  
-ATOM   1429  CA  PHE A 198      16.292  15.921   6.634  1.00 29.21           C  
-ANISOU 1429  CA  PHE A 198     4810   3022   3264  -1004    507   -171       C  
-ATOM   1430  C   PHE A 198      15.816  14.709   7.431  1.00 27.99           C  
-ANISOU 1430  C   PHE A 198     4519   3044   3070   -881    455   -247       C  
-ATOM   1431  O   PHE A 198      15.629  13.633   6.855  1.00 28.06           O  
-ANISOU 1431  O   PHE A 198     4365   3230   3067   -797    446   -197       O  
-ATOM   1432  CB  PHE A 198      17.433  15.511   5.699  1.00 29.22           C  
-ANISOU 1432  CB  PHE A 198     4647   3168   3288  -1152    523    -89       C  
-ATOM   1433  CG  PHE A 198      17.914  16.616   4.802  1.00 34.54           C  
-ANISOU 1433  CG  PHE A 198     5441   3686   3996  -1283    599     19       C  
-ATOM   1434  CD1 PHE A 198      17.143  17.048   3.729  1.00 35.09           C  
-ANISOU 1434  CD1 PHE A 198     5634   3664   4035  -1146    666    143       C  
-ATOM   1435  CD2 PHE A 198      19.148  17.208   5.017  1.00 40.17           C  
-ANISOU 1435  CD2 PHE A 198     6138   4349   4776  -1552    596     12       C  
-ATOM   1436  CE1 PHE A 198      17.593  18.071   2.885  1.00 33.49           C  
-ANISOU 1436  CE1 PHE A 198     5567   3306   3852  -1266    748    265       C  
-ATOM   1437  CE2 PHE A 198      19.610  18.223   4.184  1.00 40.65           C  
-ANISOU 1437  CE2 PHE A 198     6309   4257   4878  -1697    682    132       C  
-ATOM   1438  CZ  PHE A 198      18.829  18.655   3.117  1.00 41.88           C  
-ANISOU 1438  CZ  PHE A 198     6617   4307   4987  -1548    767    262       C  
-ATOM   1439  N   ARG A 199      15.616  14.857   8.740  1.00 28.06           N  
-ANISOU 1439  N   ARG A 199     4616   2996   3048   -872    424   -365       N  
-ATOM   1440  CA  ARG A 199      15.050  13.732   9.492  1.00 28.52           C  
-ANISOU 1440  CA  ARG A 199     4567   3208   3060   -745    398   -411       C  
-ATOM   1441  C   ARG A 199      13.576  13.518   9.148  1.00 35.23           C  
-ANISOU 1441  C   ARG A 199     5408   4057   3920   -513    462   -346       C  
-ATOM   1442  O   ARG A 199      13.079  12.381   9.154  1.00 34.38           O  
-ANISOU 1442  O   ARG A 199     5147   4108   3808   -423    445   -321       O  
-ATOM   1443  CB  ARG A 199      15.233  13.916  11.000  1.00 27.19           C  
-ANISOU 1443  CB  ARG A 199     4514   2992   2823   -789    357   -546       C  
-ATOM   1444  CG  ARG A 199      16.699  14.002  11.461  1.00 28.33           C  
-ANISOU 1444  CG  ARG A 199     4630   3171   2963  -1031    245   -614       C  
-ATOM   1445  CD  ARG A 199      16.819  13.709  12.968  1.00 29.79           C  
-ANISOU 1445  CD  ARG A 199     4890   3387   3042  -1042    165   -739       C  
-ATOM   1446  NE  ARG A 199      18.091  14.125  13.563  1.00 32.29           N  
-ANISOU 1446  NE  ARG A 199     5237   3686   3346  -1281     27   -822       N  
-ATOM   1447  CZ  ARG A 199      19.192  13.373  13.635  1.00 30.18           C  
-ANISOU 1447  CZ  ARG A 199     4755   3608   3105  -1406    -90   -809       C  
-ATOM   1448  NH1 ARG A 199      19.206  12.143  13.128  1.00 28.33           N  
-ANISOU 1448  NH1 ARG A 199     4289   3575   2900  -1304    -71   -724       N  
-ATOM   1449  NH2 ARG A 199      20.287  13.871  14.209  1.00 32.20           N  
-ANISOU 1449  NH2 ARG A 199     5030   3842   3362  -1633   -235   -881       N  
-ATOM   1450  N   ASP A 200      12.901  14.620   8.823  1.00 29.39           N  
-ANISOU 1450  N   ASP A 200     4829   3134   3206   -423    527   -308       N  
-ATOM   1451  CA  ASP A 200      11.468  14.645   8.540  1.00 29.16           C  
-ANISOU 1451  CA  ASP A 200     4785   3091   3206   -191    582   -236       C  
-ATOM   1452  C   ASP A 200      11.229  14.365   7.067  1.00 31.15           C  
-ANISOU 1452  C   ASP A 200     4933   3412   3491   -152    551   -103       C  
-ATOM   1453  O   ASP A 200      10.627  15.165   6.352  1.00 37.29           O  
-ANISOU 1453  O   ASP A 200     5801   4071   4295    -46    578    -15       O  
-ATOM   1454  CB  ASP A 200      10.881  16.024   8.902  1.00 31.52           C  
-ANISOU 1454  CB  ASP A 200     5320   3142   3512    -81    666   -256       C  
-ATOM   1455  CG  ASP A 200      11.604  17.172   8.210  1.00 35.96           C  
-ANISOU 1455  CG  ASP A 200     6064   3507   4093   -206    666   -223       C  
-ATOM   1456  OD1 ASP A 200      12.811  17.033   7.911  1.00 33.25           O  
-ANISOU 1456  OD1 ASP A 200     5681   3208   3746   -431    613   -231       O  
-ATOM   1457  OD2 ASP A 200      10.960  18.213   7.961  1.00 38.62           O  
-ANISOU 1457  OD2 ASP A 200     6575   3641   4457    -75    728   -177       O  
-ATOM   1458  N   LEU A 201      11.724  13.217   6.631  1.00 29.67           N  
-ANISOU 1458  N   LEU A 201     4578   3410   3287   -227    489    -90       N  
-ATOM   1459  CA  LEU A 201      11.702  12.789   5.238  1.00 28.76           C  
-ANISOU 1459  CA  LEU A 201     4390   3377   3162   -213    449     12       C  
-ATOM   1460  C   LEU A 201      11.626  11.270   5.280  1.00 26.56           C  
-ANISOU 1460  C   LEU A 201     3929   3292   2869   -206    385    -10       C  
-ATOM   1461  O   LEU A 201      12.407  10.640   5.993  1.00 27.52           O  
-ANISOU 1461  O   LEU A 201     3991   3489   2975   -300    374    -87       O  
-ATOM   1462  CB  LEU A 201      12.988  13.246   4.547  1.00 32.38           C  
-ANISOU 1462  CB  LEU A 201     4908   3800   3593   -379    471     37       C  
-ATOM   1463  CG  LEU A 201      13.338  12.771   3.134  1.00 32.66           C  
-ANISOU 1463  CG  LEU A 201     4898   3934   3578   -392    460    128       C  
-ATOM   1464  CD1 LEU A 201      12.336  13.291   2.122  1.00 33.85           C  
-ANISOU 1464  CD1 LEU A 201     5141   4014   3707   -250    444    244       C  
-ATOM   1465  CD2 LEU A 201      14.764  13.221   2.761  1.00 28.81           C  
-ANISOU 1465  CD2 LEU A 201     4437   3430   3080   -579    524    146       C  
-ATOM   1466  N   ASN A 202      10.685  10.682   4.538  1.00 30.34           N  
-ANISOU 1466  N   ASN A 202     4330   3842   3356    -98    328     59       N  
-ATOM   1467  CA AASN A 202      10.434   9.236   4.569  0.58 31.00           C  
-ANISOU 1467  CA AASN A 202     4269   4074   3438    -94    256     41       C  
-ATOM   1468  CA BASN A 202      10.467   9.234   4.606  0.42 30.36           C  
-ANISOU 1468  CA BASN A 202     4188   3992   3356    -97    258     37       C  
-ATOM   1469  C   ASN A 202      11.419   8.409   3.732  1.00 28.06           C  
-ANISOU 1469  C   ASN A 202     3874   3791   2997   -176    219     30       C  
-ATOM   1470  O   ASN A 202      11.682   7.250   4.032  1.00 29.29           O  
-ANISOU 1470  O   ASN A 202     3946   4038   3145   -202    182    -18       O  
-ATOM   1471  CB AASN A 202       9.012   8.947   4.074  0.58 33.61           C  
-ANISOU 1471  CB AASN A 202     4520   4437   3814     30    185    118       C  
-ATOM   1472  CB BASN A 202       8.995   8.857   4.330  0.42 33.20           C  
-ANISOU 1472  CB BASN A 202     4454   4391   3771     27    193    105       C  
-ATOM   1473  CG AASN A 202       8.089   8.456   5.173  0.58 38.22           C  
-ANISOU 1473  CG AASN A 202     4985   5062   4474     86    203    104       C  
-ATOM   1474  CG BASN A 202       8.554   9.166   2.898  0.42 34.37           C  
-ANISOU 1474  CG BASN A 202     4642   4528   3889     86    116    200       C  
-ATOM   1475  OD1AASN A 202       8.435   8.477   6.362  0.58 36.32           O  
-ANISOU 1475  OD1AASN A 202     4763   4807   4230     57    281     35       O  
-ATOM   1476  OD1BASN A 202       9.159   9.994   2.218  0.42 38.68           O  
-ANISOU 1476  OD1BASN A 202     5319   5000   4378     66    151    233       O  
-ATOM   1477  ND2AASN A 202       6.896   8.008   4.777  0.58 42.53           N  
-ANISOU 1477  ND2AASN A 202     5407   5667   5086    161    127    178       N  
-ATOM   1478  ND2BASN A 202       7.484   8.506   2.442  0.42 27.81           N  
-ANISOU 1478  ND2BASN A 202     3701   3771   3093    150      3    253       N  
-ATOM   1479  N   HIS A 203      11.943   9.008   2.668  1.00 24.12           N  
-ANISOU 1479  N   HIS A 203     3464   3257   2443   -200    242     83       N  
-ATOM   1480  CA  HIS A 203      12.860   8.306   1.758  1.00 23.55           C  
-ANISOU 1480  CA  HIS A 203     3387   3273   2290   -248    243     82       C  
-ATOM   1481  C   HIS A 203      14.308   8.534   2.193  1.00 28.48           C  
-ANISOU 1481  C   HIS A 203     3986   3913   2921   -373    330     42       C  
-ATOM   1482  O   HIS A 203      14.613   9.552   2.800  1.00 29.88           O  
-ANISOU 1482  O   HIS A 203     4208   4000   3146   -444    379     36       O  
-ATOM   1483  CB  HIS A 203      12.722   8.843   0.328  1.00 24.44           C  
-ANISOU 1483  CB  HIS A 203     3617   3353   2315   -209    245    178       C  
-ATOM   1484  CG  HIS A 203      11.322   8.838  -0.202  1.00 26.39           C  
-ANISOU 1484  CG  HIS A 203     3886   3584   2557    -91    132    238       C  
-ATOM   1485  ND1 HIS A 203      10.617   7.678  -0.444  1.00 27.62           N  
-ANISOU 1485  ND1 HIS A 203     3972   3823   2698    -47      7    214       N  
-ATOM   1486  CD2 HIS A 203      10.498   9.859  -0.551  1.00 27.39           C  
-ANISOU 1486  CD2 HIS A 203     4089   3619   2700     -8    111    330       C  
-ATOM   1487  CE1 HIS A 203       9.424   7.984  -0.923  1.00 30.69           C  
-ANISOU 1487  CE1 HIS A 203     4368   4192   3102     43    -98    289       C  
-ATOM   1488  NE2 HIS A 203       9.324   9.299  -0.988  1.00 27.96           N  
-ANISOU 1488  NE2 HIS A 203     4104   3745   2773     86    -34    364       N  
-ATOM   1489  N   VAL A 204      15.206   7.608   1.861  1.00 26.81           N  
-ANISOU 1489  N   VAL A 204     3706   3812   2667   -397    346     15       N  
-ATOM   1490  CA  VAL A 204      16.634   7.890   1.992  1.00 27.41           C  
-ANISOU 1490  CA  VAL A 204     3724   3930   2761   -510    432     10       C  
-ATOM   1491  C   VAL A 204      17.092   8.532   0.690  1.00 30.83           C  
-ANISOU 1491  C   VAL A 204     4240   4349   3127   -534    530    104       C  
-ATOM   1492  O   VAL A 204      16.791   8.030  -0.393  1.00 30.05           O  
-ANISOU 1492  O   VAL A 204     4206   4288   2925   -443    529    138       O  
-ATOM   1493  CB  VAL A 204      17.467   6.635   2.335  1.00 25.15           C  
-ANISOU 1493  CB  VAL A 204     3302   3777   2475   -500    422    -50       C  
-ATOM   1494  CG1 VAL A 204      18.972   6.909   2.149  1.00 27.71           C  
-ANISOU 1494  CG1 VAL A 204     3526   4178   2824   -600    521    -24       C  
-ATOM   1495  CG2 VAL A 204      17.195   6.202   3.763  1.00 24.36           C  
-ANISOU 1495  CG2 VAL A 204     3140   3679   2435   -503    339   -123       C  
-ATOM   1496  N   CYS A 205      17.794   9.659   0.793  1.00 27.55           N  
-ANISOU 1496  N   CYS A 205     3842   3866   2759   -665    610    148       N  
-ATOM   1497  CA  CYS A 205      18.139  10.426  -0.389  1.00 29.68           C  
-ANISOU 1497  CA  CYS A 205     4214   4095   2968   -702    720    264       C  
-ATOM   1498  C   CYS A 205      19.585  10.902  -0.354  1.00 29.44           C  
-ANISOU 1498  C   CYS A 205     4082   4105   3000   -877    840    303       C  
-ATOM   1499  O   CYS A 205      20.216  10.966   0.703  1.00 28.21           O  
-ANISOU 1499  O   CYS A 205     3800   3968   2951   -993    805    239       O  
-ATOM   1500  CB  CYS A 205      17.191  11.613  -0.551  1.00 30.02           C  
-ANISOU 1500  CB  CYS A 205     4439   3955   3014   -681    699    329       C  
-ATOM   1501  N   VAL A 206      20.102  11.237  -1.519  1.00 29.13           N  
-ANISOU 1501  N   VAL A 206     4095   4085   2889   -901    978    417       N  
-ATOM   1502  CA  VAL A 206      21.401  11.882  -1.609  1.00 32.67           C  
-ANISOU 1502  CA  VAL A 206     4442   4558   3413  -1093   1114    493       C  
-ATOM   1503  C   VAL A 206      21.166  13.389  -1.682  1.00 37.50           C  
-ANISOU 1503  C   VAL A 206     5230   4953   4065  -1223   1141    580       C  
-ATOM   1504  O   VAL A 206      20.229  13.859  -2.334  1.00 41.21           O  
-ANISOU 1504  O   VAL A 206     5913   5300   4444  -1121   1131    645       O  
-ATOM   1505  CB  VAL A 206      22.219  11.369  -2.821  1.00 41.24           C  
-ANISOU 1505  CB  VAL A 206     5472   5799   4397  -1048   1295    584       C  
-ATOM   1506  CG1 VAL A 206      23.452  12.220  -3.042  1.00 46.05           C  
-ANISOU 1506  CG1 VAL A 206     5976   6424   5098  -1264   1464    703       C  
-ATOM   1507  CG2 VAL A 206      22.636   9.925  -2.601  1.00 41.62           C  
-ANISOU 1507  CG2 VAL A 206     5341   6038   4433   -926   1278    488       C  
-ATOM   1508  N   ILE A 207      22.017  14.143  -1.002  1.00 40.04           N  
-ANISOU 1508  N   ILE A 207     5469   5218   4527  -1449   1159    583       N  
-ATOM   1509  CA  ILE A 207      21.818  15.573  -0.833  1.00 42.59           C  
-ANISOU 1509  CA  ILE A 207     5981   5291   4910  -1592   1161    637       C  
-ATOM   1510  C   ILE A 207      22.460  16.352  -1.972  1.00 52.15           C  
-ANISOU 1510  C   ILE A 207     7263   6453   6099  -1717   1347    824       C  
-ATOM   1511  O   ILE A 207      23.563  16.024  -2.406  1.00 57.74           O  
-ANISOU 1511  O   ILE A 207     7779   7330   6831  -1817   1479    893       O  
-ATOM   1512  CB  ILE A 207      22.345  15.996   0.565  1.00 70.88           C  
-ANISOU 1512  CB  ILE A 207     9478   8809   8645  -1792   1052    524       C  
-ATOM   1513  CG1 ILE A 207      22.405  17.512   0.737  1.00 73.04           C  
-ANISOU 1513  CG1 ILE A 207     9955   8802   8994  -1990   1065    574       C  
-ATOM   1514  CG2 ILE A 207      23.698  15.353   0.846  1.00 70.08           C  
-ANISOU 1514  CG2 ILE A 207     9063   8932   8631  -1932   1074    511       C  
-ATOM   1515  CD1 ILE A 207      22.622  17.916   2.195  1.00 72.83           C  
-ANISOU 1515  CD1 ILE A 207     9929   8672   9072  -2146    914    423       C  
-ATOM   1516  N   SER A 208      21.763  17.366  -2.480  1.00 53.98           N  
-ANISOU 1516  N   SER A 208     7768   6458   6282  -1696   1370    921       N  
-ATOM   1517  CA  SER A 208      22.286  18.149  -3.593  1.00 56.09           C  
-ANISOU 1517  CA  SER A 208     8147   6655   6508  -1808   1554   1123       C  
-ATOM   1518  C   SER A 208      23.466  18.999  -3.139  1.00 61.53           C  
-ANISOU 1518  C   SER A 208     8740   7262   7376  -2147   1624   1170       C  
-ATOM   1519  O   SER A 208      23.766  19.077  -1.942  1.00 62.26           O  
-ANISOU 1519  O   SER A 208     8720   7326   7611  -2285   1495   1034       O  
-ATOM   1520  CB  SER A 208      21.206  19.034  -4.224  1.00 56.07           C  
-ANISOU 1520  CB  SER A 208     8483   6413   6407  -1683   1543   1228       C  
-ATOM   1521  OG  SER A 208      20.877  20.135  -3.399  1.00 59.74           O  
-ANISOU 1521  OG  SER A 208     9109   6597   6995  -1784   1462   1191       O  
-ATOM   1522  N   GLU A 209      24.141  19.624  -4.097  1.00 59.98           N  
-ANISOU 1522  N   GLU A 209     8590   7031   7168  -2293   1821   1369       N  
-ATOM   1523  CA  GLU A 209      25.239  20.519  -3.768  1.00 67.32           C  
-ANISOU 1523  CA  GLU A 209     9403   7877   8299  -2597   1854   1427       C  
-ATOM   1524  C   GLU A 209      24.720  21.734  -3.015  1.00 69.00           C  
-ANISOU 1524  C   GLU A 209     9873   7737   8604  -2713   1719   1375       C  
-ATOM   1525  O   GLU A 209      25.397  22.252  -2.125  1.00 73.77           O  
-ANISOU 1525  O   GLU A 209    10377   8262   9388  -2946   1623   1300       O  
-ATOM   1526  CB  GLU A 209      26.008  20.947  -5.026  1.00 77.33           C  
-ANISOU 1526  CB  GLU A 209    10626   9199   9555  -2630   2054   1652       C  
-ATOM   1527  CG  GLU A 209      26.824  19.827  -5.654  1.00 83.61           C  
-ANISOU 1527  CG  GLU A 209    11126  10343  10298  -2539   2207   1699       C  
-ATOM   1528  CD  GLU A 209      27.611  19.033  -4.620  1.00 88.42           C  
-ANISOU 1528  CD  GLU A 209    11378  11152  11065  -2635   2130   1555       C  
-ATOM   1529  OE1 GLU A 209      27.541  17.785  -4.644  1.00 87.67           O  
-ANISOU 1529  OE1 GLU A 209    11149  11291  10872  -2456   2146   1470       O  
-ATOM   1530  OE2 GLU A 209      28.298  19.656  -3.780  1.00 92.35           O  
-ANISOU 1530  OE2 GLU A 209    11737  11569  11782  -2882   2037   1524       O  
-ATOM   1531  N   THR A 210      23.513  22.175  -3.363  1.00 65.96           N  
-ANISOU 1531  N   THR A 210     9826   7142   8094  -2528   1699   1409       N  
-ATOM   1532  CA  THR A 210      22.930  23.365  -2.751  1.00 68.66           C  
-ANISOU 1532  CA  THR A 210    10452   7126   8509  -2573   1593   1366       C  
-ATOM   1533  C   THR A 210      22.465  23.095  -1.314  1.00 66.57           C  
-ANISOU 1533  C   THR A 210    10187   6807   8298  -2561   1412   1130       C  
-ATOM   1534  O   THR A 210      22.565  23.970  -0.455  1.00 70.49           O  
-ANISOU 1534  O   THR A 210    10819   7058   8904  -2721   1322   1044       O  
-ATOM   1535  CB  THR A 210      21.778  23.967  -3.612  1.00 79.80           C  
-ANISOU 1535  CB  THR A 210    12205   8336   9782  -2329   1622   1494       C  
-ATOM   1536  OG1 THR A 210      21.760  25.393  -3.470  1.00 84.73           O  
-ANISOU 1536  OG1 THR A 210    13057   8629  10508  -2429   1596   1540       O  
-ATOM   1537  CG2 THR A 210      20.420  23.404  -3.211  1.00 74.21           C  
-ANISOU 1537  CG2 THR A 210    11597   7626   8975  -2025   1496   1374       C  
-ATOM   1538  N   GLY A 211      21.987  21.879  -1.055  1.00 57.27           N  
-ANISOU 1538  N   GLY A 211     8833   5883   7043  -2326   1332   1009       N  
-ATOM   1539  CA  GLY A 211      21.515  21.515   0.268  1.00 53.08           C  
-ANISOU 1539  CA  GLY A 211     8266   5355   6547  -2249   1158    788       C  
-ATOM   1540  C   GLY A 211      22.683  21.246   1.197  1.00 57.04           C  
-ANISOU 1540  C   GLY A 211     8522   5978   7172  -2515   1087    680       C  
-ATOM   1541  O   GLY A 211      22.605  21.514   2.394  1.00 58.67           O  
-ANISOU 1541  O   GLY A 211     8789   6073   7431  -2586    946    519       O  
-ATOM   1542  N   LYS A 212      23.769  20.713   0.640  1.00 57.66           N  
-ANISOU 1542  N   LYS A 212     8325   6296   7289  -2649   1184    774       N  
-ATOM   1543  CA  LYS A 212      24.980  20.439   1.412  1.00 59.20           C  
-ANISOU 1543  CA  LYS A 212     8232   6642   7620  -2903   1113    704       C  
-ATOM   1544  C   LYS A 212      25.609  21.729   1.929  1.00 59.82           C  
-ANISOU 1544  C   LYS A 212     8418   6467   7845  -3230   1053    704       C  
-ATOM   1545  O   LYS A 212      25.969  21.829   3.103  1.00 59.30           O  
-ANISOU 1545  O   LYS A 212     8296   6377   7857  -3361    869    548       O  
-ATOM   1546  CB  LYS A 212      25.996  19.643   0.582  1.00 64.27           C  
-ANISOU 1546  CB  LYS A 212     8541   7597   8281  -2940   1265    832       C  
-ATOM   1547  CG  LYS A 212      25.967  18.142   0.841  1.00 67.10           C  
-ANISOU 1547  CG  LYS A 212     8653   8264   8578  -2712   1211    730       C  
-ATOM   1548  CD  LYS A 212      27.154  17.426   0.211  1.00 72.34           C  
-ANISOU 1548  CD  LYS A 212     8971   9224   9291  -2764   1360    838       C  
-ATOM   1549  CE  LYS A 212      26.898  17.073  -1.244  1.00 74.01           C  
-ANISOU 1549  CE  LYS A 212     9253   9517   9349  -2567   1581    983       C  
-ATOM   1550  NZ  LYS A 212      28.099  16.462  -1.882  1.00 77.00           N  
-ANISOU 1550  NZ  LYS A 212     9312  10173   9773  -2599   1766   1094       N  
-ATOM   1551  N   ALA A 213      25.734  22.714   1.047  1.00 62.71           N  
-ANISOU 1551  N   ALA A 213     8927   6657   8243  -3282   1172    868       N  
-ATOM   1552  CA  ALA A 213      26.310  24.006   1.412  1.00 63.81           C  
-ANISOU 1552  CA  ALA A 213     9163   6548   8532  -3517   1101    873       C  
-ATOM   1553  C   ALA A 213      25.364  24.796   2.315  1.00 68.60           C  
-ANISOU 1553  C   ALA A 213    10144   6821   9101  -3471    960    715       C  
-ATOM   1554  O   ALA A 213      25.805  25.570   3.167  1.00 73.58           O  
-ANISOU 1554  O   ALA A 213    10838   7284   9835  -3655    820    612       O  
-ATOM   1555  CB  ALA A 213      26.656  24.813   0.161  1.00 63.70           C  
-ANISOU 1555  CB  ALA A 213     9209   6437   8557  -3572   1284   1110       C  
-ATOM   1556  N   LYS A 214      24.064  24.596   2.121  1.00 67.16           N  
-ANISOU 1556  N   LYS A 214    10209   6542   8768  -3205   1001    698       N  
-ATOM   1557  CA  LYS A 214      23.046  25.341   2.860  1.00 74.94           C  
-ANISOU 1557  CA  LYS A 214    11560   7204   9708  -3086    911    569       C  
-ATOM   1558  C   LYS A 214      22.935  24.899   4.325  1.00 78.07           C  
-ANISOU 1558  C   LYS A 214    11938   7635  10092  -3098    733    321       C  
-ATOM   1559  O   LYS A 214      22.488  25.667   5.181  1.00 77.91           O  
-ANISOU 1559  O   LYS A 214    12187   7356  10061  -3069    637    182       O  
-ATOM   1560  CB  LYS A 214      21.679  25.198   2.178  1.00 74.44           C  
-ANISOU 1560  CB  LYS A 214    11727   7050   9506  -2762   1012    648       C  
-ATOM   1561  CG  LYS A 214      20.762  26.401   2.343  1.00 77.99           C  
-ANISOU 1561  CG  LYS A 214    12569   7120   9943  -2614    996    632       C  
-ATOM   1562  CD  LYS A 214      19.284  26.019   2.221  1.00 73.45           C  
-ANISOU 1562  CD  LYS A 214    12133   6525   9248  -2220   1014    625       C  
-ATOM   1563  CE  LYS A 214      18.904  25.620   0.804  1.00 68.91           C  
-ANISOU 1563  CE  LYS A 214    11491   6104   8586  -2033   1121    837       C  
-ATOM   1564  NZ  LYS A 214      17.460  25.255   0.687  1.00 61.68           N  
-ANISOU 1564  NZ  LYS A 214    10628   5230   7577  -1626   1086    826       N  
-ATOM   1565  N   TYR A 215      23.346  23.665   4.610  1.00 78.81           N  
-ANISOU 1565  N   TYR A 215    11723   8052  10171  -3122    693    268       N  
-ATOM   1566  CA  TYR A 215      23.140  23.089   5.935  1.00 79.54           C  
-ANISOU 1566  CA  TYR A 215    11774   8232  10216  -3049    521     48       C  
-ATOM   1567  C   TYR A 215      24.413  22.600   6.644  1.00 81.66           C  
-ANISOU 1567  C   TYR A 215    11732   8726  10570  -3306    378    -25       C  
-ATOM   1568  O   TYR A 215      24.321  22.006   7.719  1.00 78.74           O  
-ANISOU 1568  O   TYR A 215    11317   8457  10142  -3259    230   -192       O  
-ATOM   1569  CB  TYR A 215      22.120  21.941   5.872  1.00 78.90           C  
-ANISOU 1569  CB  TYR A 215    11597   8371  10011  -2662    547     17       C  
-ATOM   1570  CG  TYR A 215      20.731  22.308   5.377  1.00 79.68           C  
-ANISOU 1570  CG  TYR A 215    11954   8294  10026  -2356    638     66       C  
-ATOM   1571  CD1 TYR A 215      19.922  23.187   6.090  1.00 82.47           C  
-ANISOU 1571  CD1 TYR A 215    12641   8342  10350  -2263    606    -39       C  
-ATOM   1572  CD2 TYR A 215      20.219  21.746   4.214  1.00 76.75           C  
-ANISOU 1572  CD2 TYR A 215    11490   8070   9600  -2144    748    214       C  
-ATOM   1573  CE1 TYR A 215      18.648  23.508   5.645  1.00 80.57           C  
-ANISOU 1573  CE1 TYR A 215    12597   7962  10053  -1958    687     21       C  
-ATOM   1574  CE2 TYR A 215      18.953  22.063   3.760  1.00 75.26           C  
-ANISOU 1574  CE2 TYR A 215    11505   7744   9345  -1865    799    269       C  
-ATOM   1575  CZ  TYR A 215      18.171  22.941   4.479  1.00 76.09           C  
-ANISOU 1575  CZ  TYR A 215    11901   7563   9448  -1767    771    181       C  
-ATOM   1576  OH  TYR A 215      16.910  23.249   4.026  1.00 74.45           O  
-ANISOU 1576  OH  TYR A 215    11858   7237   9193  -1467    821    251       O  
-ATOM   1577  N   LYS A 216      25.589  22.828   6.059  1.00 87.18           N  
-ANISOU 1577  N   LYS A 216    12185   9533  11406  -3506    413    109       N  
-ATOM   1578  CA  LYS A 216      26.839  22.416   6.713  1.00 90.63           C  
-ANISOU 1578  CA  LYS A 216    12282  10201  11952  -3689    264     60       C  
-ATOM   1579  C   LYS A 216      27.074  23.162   8.024  1.00 91.29           C  
-ANISOU 1579  C   LYS A 216    12524  10103  12057  -3822     36   -121       C  
-ATOM   1580  O   LYS A 216      27.251  24.378   8.032  1.00 93.74           O  
-ANISOU 1580  O   LYS A 216    13033  10146  12440  -3964     19   -112       O  
-ATOM   1581  CB  LYS A 216      28.059  22.592   5.801  1.00 96.07           C  
-ANISOU 1581  CB  LYS A 216    12669  11023  12809  -3865    372    252       C  
-ATOM   1582  CG  LYS A 216      29.382  22.317   6.514  1.00 99.39           C  
-ANISOU 1582  CG  LYS A 216    12739  11646  13378  -4051    206    209       C  
-ATOM   1583  CD  LYS A 216      30.558  22.275   5.549  1.00102.24           C  
-ANISOU 1583  CD  LYS A 216    12747  12185  13914  -4175    357    411       C  
-ATOM   1584  CE  LYS A 216      30.464  21.088   4.597  1.00 99.28           C  
-ANISOU 1584  CE  LYS A 216    12154  12101  13468  -3962    557    530       C  
-ATOM   1585  NZ  LYS A 216      31.698  20.931   3.772  1.00101.80           N  
-ANISOU 1585  NZ  LYS A 216    12102  12623  13953  -4047    715    712       N  
-TER    1586      LYS A 216                                                      
-ATOM   1587  N   SER B   4       4.774  12.235 -18.959  1.00 73.09           N  
-ANISOU 1587  N   SER B   4     9298   8729   9745   -849     92   2826       N  
-ATOM   1588  CA  SER B   4       5.720  11.466 -18.152  1.00 70.21           C  
-ANISOU 1588  CA  SER B   4     8940   8481   9258   -874    219   2478       C  
-ATOM   1589  C   SER B   4       5.600   9.958 -18.381  1.00 63.04           C  
-ANISOU 1589  C   SER B   4     7957   7913   8081   -816    236   2287       C  
-ATOM   1590  O   SER B   4       4.499   9.398 -18.341  1.00 61.71           O  
-ANISOU 1590  O   SER B   4     7751   7750   7944   -665    181   2266       O  
-ATOM   1591  CB  SER B   4       5.551  11.789 -16.668  1.00 70.21           C  
-ANISOU 1591  CB  SER B   4     9010   8142   9526   -740    293   2246       C  
-ATOM   1592  OG  SER B   4       6.314  10.905 -15.865  1.00 70.46           O  
-ANISOU 1592  OG  SER B   4     9033   8310   9427   -749    384   1929       O  
-ATOM   1593  N   PRO B   5       6.747   9.294 -18.612  1.00 57.72           N  
-ANISOU 1593  N   PRO B   5     7254   7516   7161   -937    314   2148       N  
-ATOM   1594  CA  PRO B   5       6.781   7.858 -18.901  1.00 54.58           C  
-ANISOU 1594  CA  PRO B   5     6802   7423   6511   -891    340   1952       C  
-ATOM   1595  C   PRO B   5       6.747   7.024 -17.629  1.00 47.99           C  
-ANISOU 1595  C   PRO B   5     5964   6506   5766   -742    402   1634       C  
-ATOM   1596  O   PRO B   5       6.649   5.796 -17.709  1.00 50.63           O  
-ANISOU 1596  O   PRO B   5     6264   7027   5948   -678    413   1461       O  
-ATOM   1597  CB  PRO B   5       8.121   7.677 -19.626  1.00 58.54           C  
-ANISOU 1597  CB  PRO B   5     7264   8216   6761  -1070    426   1950       C  
-ATOM   1598  CG  PRO B   5       8.966   8.880 -19.237  1.00 58.45           C  
-ANISOU 1598  CG  PRO B   5     7272   8024   6912  -1205    461   2060       C  
-ATOM   1599  CD  PRO B   5       8.101   9.861 -18.487  1.00 57.34           C  
-ANISOU 1599  CD  PRO B   5     7213   7476   7097  -1115    389   2147       C  
-ATOM   1600  N   GLY B   6       6.809   7.675 -16.469  1.00 35.78           N  
-ANISOU 1600  N   GLY B   6     4465   4675   4456   -697    435   1559       N  
-ATOM   1601  CA  GLY B   6       6.798   6.945 -15.213  1.00 29.93           C  
-ANISOU 1601  CA  GLY B   6     3731   3866   3776   -578    489   1280       C  
-ATOM   1602  C   GLY B   6       8.204   6.578 -14.776  1.00 29.30           C  
-ANISOU 1602  C   GLY B   6     3623   3911   3601   -674    560   1111       C  
-ATOM   1603  O   GLY B   6       9.180   7.070 -15.339  1.00 30.66           O  
-ANISOU 1603  O   GLY B   6     3767   4183   3701   -834    583   1212       O  
-ATOM   1604  N   VAL B   7       8.310   5.720 -13.762  1.00 27.81           N  
-ANISOU 1604  N   VAL B   7     3427   3722   3418   -582    591    877       N  
-ATOM   1605  CA  VAL B   7       9.614   5.255 -13.301  1.00 28.52           C  
-ANISOU 1605  CA  VAL B   7     3461   3942   3434   -653    637    728       C  
-ATOM   1606  C   VAL B   7      10.172   4.301 -14.344  1.00 27.97           C  
-ANISOU 1606  C   VAL B   7     3290   4186   3153   -670    669    714       C  
-ATOM   1607  O   VAL B   7       9.600   3.239 -14.586  1.00 28.08           O  
-ANISOU 1607  O   VAL B   7     3290   4296   3082   -557    657    625       O  
-ATOM   1608  CB  VAL B   7       9.516   4.501 -11.979  1.00 29.40           C  
-ANISOU 1608  CB  VAL B   7     3591   3984   3596   -547    641    511       C  
-ATOM   1609  CG1 VAL B   7      10.882   3.930 -11.597  1.00 29.24           C  
-ANISOU 1609  CG1 VAL B   7     3481   4123   3505   -613    664    391       C  
-ATOM   1610  CG2 VAL B   7       8.995   5.423 -10.871  1.00 32.18           C  
-ANISOU 1610  CG2 VAL B   7     4063   4040   4126   -530    639    482       C  
-ATOM   1611  N   VAL B   8      11.296   4.667 -14.943  1.00 29.40           N  
-ANISOU 1611  N   VAL B   8     3398   4523   3250   -816    719    791       N  
-ATOM   1612  CA  VAL B   8      11.890   3.824 -15.973  1.00 37.66           C  
-ANISOU 1612  CA  VAL B   8     4346   5880   4082   -828    788    761       C  
-ATOM   1613  C   VAL B   8      12.774   2.725 -15.364  1.00 38.07           C  
-ANISOU 1613  C   VAL B   8     4295   6050   4118   -751    844    541       C  
-ATOM   1614  O   VAL B   8      13.825   2.993 -14.788  1.00 37.29           O  
-ANISOU 1614  O   VAL B   8     4112   5968   4089   -828    869    521       O  
-ATOM   1615  CB  VAL B   8      12.644   4.669 -17.021  1.00 38.87           C  
-ANISOU 1615  CB  VAL B   8     4448   6190   4131  -1018    841    966       C  
-ATOM   1616  CG1 VAL B   8      13.337   3.785 -18.064  1.00 36.46           C  
-ANISOU 1616  CG1 VAL B   8     4039   6234   3579  -1025    954    905       C  
-ATOM   1617  CG2 VAL B   8      11.674   5.623 -17.710  1.00 43.32           C  
-ANISOU 1617  CG2 VAL B   8     5114   6637   4708  -1076    762   1211       C  
-ATOM   1618  N   ILE B   9      12.314   1.484 -15.476  1.00 31.22           N  
-ANISOU 1618  N   ILE B   9     3432   5250   3178   -604    845    389       N  
-ATOM   1619  CA  ILE B   9      13.104   0.329 -15.072  1.00 31.59           C  
-ANISOU 1619  CA  ILE B   9     3379   5405   3219   -507    895    197       C  
-ATOM   1620  C   ILE B   9      13.837  -0.184 -16.303  1.00 35.38           C  
-ANISOU 1620  C   ILE B   9     3765   6169   3508   -521   1017    166       C  
-ATOM   1621  O   ILE B   9      13.209  -0.640 -17.268  1.00 37.29           O  
-ANISOU 1621  O   ILE B   9     4074   6504   3589   -492   1029    146       O  
-ATOM   1622  CB  ILE B   9      12.211  -0.764 -14.469  1.00 34.12           C  
-ANISOU 1622  CB  ILE B   9     3767   5610   3587   -344    828     48       C  
-ATOM   1623  CG1 ILE B   9      11.561  -0.260 -13.185  1.00 38.68           C  
-ANISOU 1623  CG1 ILE B   9     4426   5939   4332   -332    742     67       C  
-ATOM   1624  CG2 ILE B   9      13.006  -2.020 -14.183  1.00 35.95           C  
-ANISOU 1624  CG2 ILE B   9     3900   5934   3824   -232    872   -131       C  
-ATOM   1625  CD1 ILE B   9      10.686  -1.279 -12.529  1.00 40.40           C  
-ANISOU 1625  CD1 ILE B   9     4697   6055   4597   -196    684    -48       C  
-ATOM   1626  N   SER B  10      15.162  -0.080 -16.290  1.00 35.08           N  
-ANISOU 1626  N   SER B  10     3569   6282   3480   -576   1112    165       N  
-ATOM   1627  CA  SER B  10      15.942  -0.352 -17.500  1.00 41.28           C  
-ANISOU 1627  CA  SER B  10     4246   7362   4075   -608   1269    157       C  
-ATOM   1628  C   SER B  10      15.867  -1.817 -17.902  1.00 41.46           C  
-ANISOU 1628  C   SER B  10     4268   7481   4005   -425   1338    -74       C  
-ATOM   1629  O   SER B  10      15.547  -2.686 -17.080  1.00 37.27           O  
-ANISOU 1629  O   SER B  10     3765   6795   3600   -276   1266   -220       O  
-ATOM   1630  CB  SER B  10      17.401   0.062 -17.329  1.00 48.32           C  
-ANISOU 1630  CB  SER B  10     4927   8404   5028   -703   1364    217       C  
-ATOM   1631  OG  SER B  10      18.055  -0.764 -16.394  1.00 53.73           O  
-ANISOU 1631  OG  SER B  10     5486   9062   5866   -571   1358     68       O  
-ATOM   1632  N   ASP B  11      16.150  -2.078 -19.173  1.00 40.47           N  
-ANISOU 1632  N   ASP B  11     4162   7512   3703   -429   1432   -102       N  
-ATOM   1633  CA  ASP B  11      16.164  -3.433 -19.698  1.00 45.20           C  
-ANISOU 1633  CA  ASP B  11     4805   8137   4234   -264   1488   -331       C  
-ATOM   1634  C   ASP B  11      17.116  -4.353 -18.916  1.00 47.40           C  
-ANISOU 1634  C   ASP B  11     4938   8365   4707    -96   1536   -485       C  
-ATOM   1635  O   ASP B  11      16.836  -5.539 -18.753  1.00 50.21           O  
-ANISOU 1635  O   ASP B  11     5347   8625   5107     66   1521   -673       O  
-ATOM   1636  CB  ASP B  11      16.532  -3.423 -21.190  1.00 44.91           C  
-ANISOU 1636  CB  ASP B  11     4804   8285   3975   -320   1602   -326       C  
-ATOM   1637  CG  ASP B  11      15.473  -2.745 -22.061  1.00 46.41           C  
-ANISOU 1637  CG  ASP B  11     5154   8527   3953   -469   1524   -180       C  
-ATOM   1638  OD1 ASP B  11      14.281  -2.774 -21.695  1.00 42.08           O  
-ANISOU 1638  OD1 ASP B  11     4716   7867   3407   -470   1390   -161       O  
-ATOM   1639  OD2 ASP B  11      15.838  -2.196 -23.125  1.00 51.77           O  
-ANISOU 1639  OD2 ASP B  11     5839   9367   4465   -586   1592    -69       O  
-ATOM   1640  N   ASP B  12      18.224  -3.803 -18.421  1.00 44.45           N  
-ANISOU 1640  N   ASP B  12     4378   8048   4462   -145   1578   -389       N  
-ATOM   1641  CA  ASP B  12      19.231  -4.600 -17.714  1.00 48.83           C  
-ANISOU 1641  CA  ASP B  12     4760   8584   5211      3   1613   -490       C  
-ATOM   1642  C   ASP B  12      19.040  -4.669 -16.187  1.00 50.12           C  
-ANISOU 1642  C   ASP B  12     4870   8603   5571     39   1473   -485       C  
-ATOM   1643  O   ASP B  12      19.905  -5.184 -15.475  1.00 48.78           O  
-ANISOU 1643  O   ASP B  12     4532   8427   5575    135   1469   -521       O  
-ATOM   1644  CB  ASP B  12      20.652  -4.121 -18.045  1.00 55.80           C  
-ANISOU 1644  CB  ASP B  12     5434   9635   6132    -62   1735   -393       C  
-ATOM   1645  CG  ASP B  12      20.878  -2.649 -17.713  1.00 59.74           C  
-ANISOU 1645  CG  ASP B  12     5872  10177   6650   -297   1677   -163       C  
-ATOM   1646  OD1 ASP B  12      20.031  -2.045 -17.020  1.00 56.74           O  
-ANISOU 1646  OD1 ASP B  12     5592   9676   6292   -388   1547    -90       O  
-ATOM   1647  OD2 ASP B  12      21.914  -2.094 -18.141  1.00 63.33           O  
-ANISOU 1647  OD2 ASP B  12     6180  10775   7107   -395   1767    -55       O  
-ATOM   1648  N   GLU B  13      17.915  -4.150 -15.697  1.00 46.31           N  
-ANISOU 1648  N   GLU B  13     4522   8015   5058    -41   1363   -433       N  
-ATOM   1649  CA  GLU B  13      17.582  -4.196 -14.268  1.00 48.97           C  
-ANISOU 1649  CA  GLU B  13     4893   8137   5576    -17   1197   -421       C  
-ATOM   1650  C   GLU B  13      17.582  -5.630 -13.727  1.00 42.70           C  
-ANISOU 1650  C   GLU B  13     4079   7250   4896    196   1162   -587       C  
-ATOM   1651  O   GLU B  13      16.816  -6.476 -14.180  1.00 40.46           O  
-ANISOU 1651  O   GLU B  13     3922   6900   4550    303   1166   -713       O  
-ATOM   1652  CB  GLU B  13      16.221  -3.541 -14.019  1.00 53.62           C  
-ANISOU 1652  CB  GLU B  13     5706   8531   6134    -98   1074   -343       C  
-ATOM   1653  CG  GLU B  13      15.598  -3.866 -12.662  1.00 59.04           C  
-ANISOU 1653  CG  GLU B  13     6480   8989   6965    -39    924   -374       C  
-ATOM   1654  CD  GLU B  13      16.327  -3.202 -11.512  1.00 64.89           C  
-ANISOU 1654  CD  GLU B  13     7142   9685   7829   -135    851   -295       C  
-ATOM   1655  OE1 GLU B  13      16.526  -3.871 -10.472  1.00 66.45           O  
-ANISOU 1655  OE1 GLU B  13     7306   9808   8133    -59    766   -347       O  
-ATOM   1656  OE2 GLU B  13      16.695  -2.013 -11.651  1.00 66.92           O  
-ANISOU 1656  OE2 GLU B  13     7379   9977   8070   -303    866   -174       O  
-ATOM   1657  N   PRO B  14      18.455  -5.907 -12.753  1.00 46.99           N  
-ANISOU 1657  N   PRO B  14     4461   7779   5613    244   1109   -572       N  
-ATOM   1658  CA  PRO B  14      18.590  -7.275 -12.242  1.00 46.79           C  
-ANISOU 1658  CA  PRO B  14     4392   7661   5725    450   1069   -696       C  
-ATOM   1659  C   PRO B  14      17.513  -7.658 -11.228  1.00 40.95           C  
-ANISOU 1659  C   PRO B  14     3836   6675   5047    473    892   -697       C  
-ATOM   1660  O   PRO B  14      17.355  -8.846 -10.955  1.00 43.54           O  
-ANISOU 1660  O   PRO B  14     4182   6893   5470    632    851   -793       O  
-ATOM   1661  CB  PRO B  14      19.962  -7.254 -11.566  1.00 49.99           C  
-ANISOU 1661  CB  PRO B  14     4531   8169   6294    462   1055   -621       C  
-ATOM   1662  CG  PRO B  14      20.107  -5.838 -11.093  1.00 52.62           C  
-ANISOU 1662  CG  PRO B  14     4866   8532   6597    219    981   -453       C  
-ATOM   1663  CD  PRO B  14      19.435  -4.987 -12.150  1.00 51.51           C  
-ANISOU 1663  CD  PRO B  14     4869   8434   6266     98   1075   -427       C  
-ATOM   1664  N   GLY B  15      16.783  -6.688 -10.685  1.00 33.46           N  
-ANISOU 1664  N   GLY B  15     3022   5637   4055    320    799   -593       N  
-ATOM   1665  CA  GLY B  15      15.821  -6.985  -9.634  1.00 33.35           C  
-ANISOU 1665  CA  GLY B  15     3157   5421   4093    332    657   -584       C  
-ATOM   1666  C   GLY B  15      16.541  -7.396  -8.354  1.00 36.70           C  
-ANISOU 1666  C   GLY B  15     3478   5811   4657    360    543   -543       C  
-ATOM   1667  O   GLY B  15      17.753  -7.212  -8.244  1.00 39.26           O  
-ANISOU 1667  O   GLY B  15     3609   6264   5043    340    557   -499       O  
-ATOM   1668  N   TYR B  16      15.806  -7.956  -7.394  1.00 29.04           N  
-ANISOU 1668  N   TYR B  16     2621   4683   3730    394    424   -538       N  
-ATOM   1669  CA  TYR B  16      16.388  -8.315  -6.092  1.00 31.79           C  
-ANISOU 1669  CA  TYR B  16     2897   5003   4178    393    288   -469       C  
-ATOM   1670  C   TYR B  16      16.286  -9.798  -5.760  1.00 32.43           C  
-ANISOU 1670  C   TYR B  16     2966   4978   4379    563    218   -501       C  
-ATOM   1671  O   TYR B  16      15.330 -10.463  -6.172  1.00 30.18           O  
-ANISOU 1671  O   TYR B  16     2809   4578   4081    638    238   -574       O  
-ATOM   1672  CB  TYR B  16      15.665  -7.548  -5.001  1.00 30.60           C  
-ANISOU 1672  CB  TYR B  16     2905   4765   3955    245    198   -405       C  
-ATOM   1673  CG  TYR B  16      15.703  -6.054  -5.164  1.00 30.58           C  
-ANISOU 1673  CG  TYR B  16     2947   4806   3866     75    247   -373       C  
-ATOM   1674  CD1 TYR B  16      16.765  -5.323  -4.674  1.00 33.60           C  
-ANISOU 1674  CD1 TYR B  16     3225   5280   4262    -59    195   -310       C  
-ATOM   1675  CD2 TYR B  16      14.677  -5.380  -5.803  1.00 27.51           C  
-ANISOU 1675  CD2 TYR B  16     2700   4353   3400     41    328   -392       C  
-ATOM   1676  CE1 TYR B  16      16.814  -3.959  -4.805  1.00 32.78           C  
-ANISOU 1676  CE1 TYR B  16     3177   5178   4098   -229    228   -281       C  
-ATOM   1677  CE2 TYR B  16      14.712  -3.995  -5.941  1.00 30.97           C  
-ANISOU 1677  CE2 TYR B  16     3187   4792   3790   -109    365   -348       C  
-ATOM   1678  CZ  TYR B  16      15.790  -3.300  -5.437  1.00 32.60           C  
-ANISOU 1678  CZ  TYR B  16     3307   5066   4014   -246    317   -300       C  
-ATOM   1679  OH  TYR B  16      15.859  -1.935  -5.562  1.00 36.23           O  
-ANISOU 1679  OH  TYR B  16     3827   5493   4445   -409    343   -257       O  
-ATOM   1680  N   ASP B  17      17.261 -10.309  -5.002  1.00 35.39           N  
-ANISOU 1680  N   ASP B  17     3184   5382   4881    612    118   -430       N  
-ATOM   1681  CA  ASP B  17      17.229 -11.701  -4.524  1.00 35.39           C  
-ANISOU 1681  CA  ASP B  17     3168   5251   5027    768     21   -419       C  
-ATOM   1682  C   ASP B  17      15.969 -11.889  -3.678  1.00 28.89           C  
-ANISOU 1682  C   ASP B  17     2564   4279   4135    696    -79   -374       C  
-ATOM   1683  O   ASP B  17      15.658 -11.051  -2.835  1.00 27.24           O  
-ANISOU 1683  O   ASP B  17     2440   4098   3813    534   -136   -300       O  
-ATOM   1684  CB  ASP B  17      18.492 -12.026  -3.698  1.00 39.53           C  
-ANISOU 1684  CB  ASP B  17     3474   5846   5700    804   -105   -294       C  
-ATOM   1685  CG  ASP B  17      18.628 -13.522  -3.364  1.00 49.10           C  
-ANISOU 1685  CG  ASP B  17     4635   6907   7112   1001   -200   -266       C  
-ATOM   1686  OD1 ASP B  17      17.641 -14.140  -2.908  1.00 48.92           O  
-ANISOU 1686  OD1 ASP B  17     4793   6714   7078   1003   -278   -250       O  
-ATOM   1687  OD2 ASP B  17      19.733 -14.083  -3.553  1.00 57.87           O  
-ANISOU 1687  OD2 ASP B  17     5513   8064   8413   1156   -195   -247       O  
-ATOM   1688  N   LEU B  18      15.247 -12.981  -3.901  1.00 26.73           N  
-ANISOU 1688  N   LEU B  18     2380   3847   3928    809    -92   -424       N  
-ATOM   1689  CA  LEU B  18      14.010 -13.266  -3.157  1.00 26.80           C  
-ANISOU 1689  CA  LEU B  18     2571   3726   3885    738   -174   -366       C  
-ATOM   1690  C   LEU B  18      14.274 -13.354  -1.649  1.00 27.19           C  
-ANISOU 1690  C   LEU B  18     2613   3781   3938    659   -335   -200       C  
-ATOM   1691  O   LEU B  18      13.393 -13.066  -0.834  1.00 29.54           O  
-ANISOU 1691  O   LEU B  18     3050   4053   4119    538   -373   -136       O  
-ATOM   1692  CB  LEU B  18      13.428 -14.599  -3.619  1.00 27.44           C  
-ANISOU 1692  CB  LEU B  18     2717   3626   4082    868   -191   -429       C  
-ATOM   1693  CG  LEU B  18      13.071 -14.749  -5.088  1.00 32.26           C  
-ANISOU 1693  CG  LEU B  18     3371   4218   4667    937    -59   -607       C  
-ATOM   1694  CD1 LEU B  18      12.716 -16.187  -5.385  1.00 35.76           C  
-ANISOU 1694  CD1 LEU B  18     3878   4455   5254   1060   -107   -677       C  
-ATOM   1695  CD2 LEU B  18      11.914 -13.858  -5.422  1.00 32.46           C  
-ANISOU 1695  CD2 LEU B  18     3529   4284   4521    800     -1   -619       C  
-ATOM   1696  N   ASP B  19      15.480 -13.780  -1.291  1.00 26.52           N  
-ANISOU 1696  N   ASP B  19     2354   3739   3982    730   -426   -124       N  
-ATOM   1697  CA  ASP B  19      15.816 -14.068   0.102  1.00 27.59           C  
-ANISOU 1697  CA  ASP B  19     2470   3885   4129    662   -615     58       C  
-ATOM   1698  C   ASP B  19      15.988 -12.804   0.937  1.00 31.67           C  
-ANISOU 1698  C   ASP B  19     3026   4556   4452    447   -653    113       C  
-ATOM   1699  O   ASP B  19      16.163 -12.875   2.157  1.00 31.24           O  
-ANISOU 1699  O   ASP B  19     2994   4540   4335    341   -811    255       O  
-ATOM   1700  CB  ASP B  19      17.091 -14.917   0.178  1.00 37.67           C  
-ANISOU 1700  CB  ASP B  19     3517   5161   5633    816   -719    143       C  
-ATOM   1701  CG  ASP B  19      16.934 -16.269  -0.509  1.00 50.95           C  
-ANISOU 1701  CG  ASP B  19     5187   6641   7531   1041   -692     78       C  
-ATOM   1702  OD1 ASP B  19      15.896 -16.931  -0.271  1.00 51.72           O  
-ANISOU 1702  OD1 ASP B  19     5457   6571   7622   1029   -734     96       O  
-ATOM   1703  OD2 ASP B  19      17.839 -16.655  -1.292  1.00 55.36           O  
-ANISOU 1703  OD2 ASP B  19     5565   7206   8265   1222   -620      1       O  
-ATOM   1704  N   LEU B  20      15.940 -11.650   0.282  1.00 26.05           N  
-ANISOU 1704  N   LEU B  20     2335   3925   3638    371   -516      1       N  
-ATOM   1705  CA  LEU B  20      16.081 -10.387   0.999  1.00 25.90           C  
-ANISOU 1705  CA  LEU B  20     2380   4013   3448    162   -542     22       C  
-ATOM   1706  C   LEU B  20      14.715  -9.818   1.365  1.00 26.67           C  
-ANISOU 1706  C   LEU B  20     2717   4040   3377     63   -466    -29       C  
-ATOM   1707  O   LEU B  20      14.625  -8.836   2.108  1.00 24.42           O  
-ANISOU 1707  O   LEU B  20     2537   3804   2938   -104   -477    -35       O  
-ATOM   1708  CB  LEU B  20      16.898  -9.390   0.173  1.00 26.26           C  
-ANISOU 1708  CB  LEU B  20     2303   4171   3502    118   -451    -42       C  
-ATOM   1709  CG  LEU B  20      18.344  -9.829  -0.011  1.00 28.11           C  
-ANISOU 1709  CG  LEU B  20     2263   4517   3900    195   -522     29       C  
-ATOM   1710  CD1 LEU B  20      19.057  -9.009  -1.085  1.00 40.05           C  
-ANISOU 1710  CD1 LEU B  20     3634   6148   5436    175   -387    -34       C  
-ATOM   1711  CD2 LEU B  20      19.081  -9.715   1.301  1.00 34.54           C  
-ANISOU 1711  CD2 LEU B  20     3018   5422   4682     53   -735    176       C  
-ATOM   1712  N   PHE B  21      13.660 -10.461   0.863  1.00 25.34           N  
-ANISOU 1712  N   PHE B  21     2628   3754   3246    166   -391    -69       N  
-ATOM   1713  CA  PHE B  21      12.281 -10.023   1.094  1.00 25.78           C  
-ANISOU 1713  CA  PHE B  21     2867   3748   3180    103   -302   -104       C  
-ATOM   1714  C   PHE B  21      11.421 -11.112   1.695  1.00 24.45           C  
-ANISOU 1714  C   PHE B  21     2771   3492   3026    133   -360    -21       C  
-ATOM   1715  O   PHE B  21      11.851 -12.274   1.809  1.00 24.22           O  
-ANISOU 1715  O   PHE B  21     2666   3414   3121    217   -474     59       O  
-ATOM   1716  CB  PHE B  21      11.663  -9.545  -0.229  1.00 27.39           C  
-ANISOU 1716  CB  PHE B  21     3086   3913   3406    161   -149   -213       C  
-ATOM   1717  CG  PHE B  21      12.360  -8.357  -0.795  1.00 28.60           C  
-ANISOU 1717  CG  PHE B  21     3191   4147   3529    101    -82   -269       C  
-ATOM   1718  CD1 PHE B  21      11.959  -7.076  -0.444  1.00 32.57           C  
-ANISOU 1718  CD1 PHE B  21     3806   4646   3924    -21    -19   -297       C  
-ATOM   1719  CD2 PHE B  21      13.466  -8.512  -1.611  1.00 31.44           C  
-ANISOU 1719  CD2 PHE B  21     3387   4581   3977    162    -78   -286       C  
-ATOM   1720  CE1 PHE B  21      12.622  -5.968  -0.935  1.00 37.49           C  
-ANISOU 1720  CE1 PHE B  21     4393   5317   4535    -98     27   -329       C  
-ATOM   1721  CE2 PHE B  21      14.135  -7.412  -2.097  1.00 38.21           C  
-ANISOU 1721  CE2 PHE B  21     4189   5524   4806     80    -20   -309       C  
-ATOM   1722  CZ  PHE B  21      13.713  -6.139  -1.771  1.00 39.59           C  
-ANISOU 1722  CZ  PHE B  21     4489   5675   4881    -59     22   -323       C  
-ATOM   1723  N   CYS B  22      10.212 -10.731   2.110  1.00 23.98           N  
-ANISOU 1723  N   CYS B  22     2850   3408   2855     65   -279    -27       N  
-ATOM   1724  CA  CYS B  22       9.232 -11.697   2.593  1.00 26.88           C  
-ANISOU 1724  CA  CYS B  22     3278   3702   3232     72   -308     63       C  
-ATOM   1725  C   CYS B  22       8.403 -12.131   1.402  1.00 27.60           C  
-ANISOU 1725  C   CYS B  22     3357   3693   3438    169   -235      2       C  
-ATOM   1726  O   CYS B  22       7.807 -11.302   0.716  1.00 26.51           O  
-ANISOU 1726  O   CYS B  22     3243   3563   3268    169   -112    -83       O  
-ATOM   1727  CB  CYS B  22       8.338 -11.089   3.682  1.00 26.00           C  
-ANISOU 1727  CB  CYS B  22     3300   3643   2936    -54   -238     91       C  
-ATOM   1728  N   ILE B  23       8.370 -13.436   1.162  1.00 24.77           N  
-ANISOU 1728  N   ILE B  23     2967   3229   3216    245   -326     52       N  
-ATOM   1729  CA  ILE B  23       7.694 -14.016   0.002  1.00 25.62           C  
-ANISOU 1729  CA  ILE B  23     3074   3231   3431    321   -292    -19       C  
-ATOM   1730  C   ILE B  23       6.943 -15.252   0.490  1.00 27.20           C  
-ANISOU 1730  C   ILE B  23     3319   3309   3709    301   -385     98       C  
-ATOM   1731  O   ILE B  23       7.476 -15.997   1.308  1.00 29.03           O  
-ANISOU 1731  O   ILE B  23     3539   3501   3990    301   -506    215       O  
-ATOM   1732  CB  ILE B  23       8.746 -14.438  -1.062  1.00 35.58           C  
-ANISOU 1732  CB  ILE B  23     4246   4459   4815    453   -308   -127       C  
-ATOM   1733  CG1 ILE B  23       9.092 -13.262  -1.971  1.00 36.40           C  
-ANISOU 1733  CG1 ILE B  23     4313   4675   4842    457   -185   -245       C  
-ATOM   1734  CG2 ILE B  23       8.269 -15.596  -1.911  1.00 33.84           C  
-ANISOU 1734  CG2 ILE B  23     4051   4083   4724    531   -340   -183       C  
-ATOM   1735  CD1 ILE B  23      10.360 -12.600  -1.593  1.00 43.77           C  
-ANISOU 1735  CD1 ILE B  23     5160   5722   5749    443   -195   -236       C  
-ATOM   1736  N   PRO B  24       5.722 -15.493  -0.022  1.00 28.54           N  
-ANISOU 1736  N   PRO B  24     3528   3416   3900    273   -345     88       N  
-ATOM   1737  CA  PRO B  24       4.986 -16.703   0.392  1.00 29.21           C  
-ANISOU 1737  CA  PRO B  24     3651   3373   4076    228   -443    213       C  
-ATOM   1738  C   PRO B  24       5.790 -17.958   0.082  1.00 30.46           C  
-ANISOU 1738  C   PRO B  24     3797   3360   4418    328   -577    203       C  
-ATOM   1739  O   PRO B  24       6.249 -18.081  -1.062  1.00 28.91           O  
-ANISOU 1739  O   PRO B  24     3579   3111   4296    434   -554     39       O  
-ATOM   1740  CB  PRO B  24       3.753 -16.697  -0.517  1.00 32.72           C  
-ANISOU 1740  CB  PRO B  24     4109   3781   4542    194   -390    162       C  
-ATOM   1741  CG  PRO B  24       3.644 -15.329  -1.073  1.00 30.28           C  
-ANISOU 1741  CG  PRO B  24     3776   3607   4123    205   -254     61       C  
-ATOM   1742  CD  PRO B  24       5.006 -14.713  -1.048  1.00 27.95           C  
-ANISOU 1742  CD  PRO B  24     3454   3382   3783    272   -233    -16       C  
-ATOM   1743  N   ASN B  25       5.936 -18.879   1.039  1.00 30.03           N  
-ANISOU 1743  N   ASN B  25     3758   3215   4438    300   -706    373       N  
-ATOM   1744  CA  ASN B  25       6.733 -20.081   0.797  1.00 38.07           C  
-ANISOU 1744  CA  ASN B  25     4758   4034   5672    420   -837    375       C  
-ATOM   1745  C   ASN B  25       6.239 -20.899  -0.396  1.00 33.57           C  
-ANISOU 1745  C   ASN B  25     4240   3264   5250    473   -848    233       C  
-ATOM   1746  O   ASN B  25       7.037 -21.553  -1.063  1.00 32.98           O  
-ANISOU 1746  O   ASN B  25     4149   3046   5335    623   -881    113       O  
-ATOM   1747  CB  ASN B  25       6.859 -20.963   2.054  1.00 43.35           C  
-ANISOU 1747  CB  ASN B  25     5443   4619   6409    366   -997    627       C  
-ATOM   1748  CG  ASN B  25       7.614 -22.270   1.782  1.00 56.05           C  
-ANISOU 1748  CG  ASN B  25     7033   5969   8295    513  -1140    642       C  
-ATOM   1749  OD1 ASN B  25       7.012 -23.347   1.713  1.00 61.77           O  
-ANISOU 1749  OD1 ASN B  25     7829   6466   9173    486  -1233    707       O  
-ATOM   1750  ND2 ASN B  25       8.934 -22.174   1.615  1.00 52.48           N  
-ANISOU 1750  ND2 ASN B  25     6475   5539   7924    670  -1155    582       N  
-ATOM   1751  N   HIS B  26       4.940 -20.845  -0.690  1.00 33.29           N  
-ANISOU 1751  N   HIS B  26     4262   3225   5160    351   -815    236       N  
-ATOM   1752  CA  HIS B  26       4.402 -21.653  -1.789  1.00 33.65           C  
-ANISOU 1752  CA  HIS B  26     4374   3084   5326    359   -856    105       C  
-ATOM   1753  C   HIS B  26       4.876 -21.186  -3.171  1.00 32.45           C  
-ANISOU 1753  C   HIS B  26     4216   2981   5131    469   -757   -157       C  
-ATOM   1754  O   HIS B  26       4.717 -21.896  -4.163  1.00 39.71           O  
-ANISOU 1754  O   HIS B  26     5208   3747   6134    499   -789   -314       O  
-ATOM   1755  CB  HIS B  26       2.865 -21.787  -1.732  1.00 32.62           C  
-ANISOU 1755  CB  HIS B  26     4283   2948   5165    176   -876    206       C  
-ATOM   1756  CG  HIS B  26       2.121 -20.496  -1.880  1.00 32.42           C  
-ANISOU 1756  CG  HIS B  26     4205   3160   4953    104   -739    198       C  
-ATOM   1757  ND1 HIS B  26       1.798 -19.690  -0.808  1.00 34.77           N  
-ANISOU 1757  ND1 HIS B  26     4455   3636   5121     35   -658    348       N  
-ATOM   1758  CD2 HIS B  26       1.577 -19.899  -2.971  1.00 33.25           C  
-ANISOU 1758  CD2 HIS B  26     4302   3343   4989     89   -675     68       C  
-ATOM   1759  CE1 HIS B  26       1.130 -18.634  -1.237  1.00 33.57           C  
-ANISOU 1759  CE1 HIS B  26     4260   3637   4857      7   -538    299       C  
-ATOM   1760  NE2 HIS B  26       0.979 -18.738  -2.543  1.00 36.09           N  
-ANISOU 1760  NE2 HIS B  26     4595   3904   5214     35   -557    149       N  
-ATOM   1761  N   TYR B  27       5.470 -20.003  -3.231  1.00 27.55           N  
-ANISOU 1761  N   TYR B  27     3522   2576   4371    513   -638   -206       N  
-ATOM   1762  CA  TYR B  27       6.057 -19.519  -4.481  1.00 27.72           C  
-ANISOU 1762  CA  TYR B  27     3524   2673   4336    609   -535   -423       C  
-ATOM   1763  C   TYR B  27       7.594 -19.467  -4.444  1.00 32.26           C  
-ANISOU 1763  C   TYR B  27     4006   3281   4969    769   -499   -485       C  
-ATOM   1764  O   TYR B  27       8.213 -18.881  -5.331  1.00 32.86           O  
-ANISOU 1764  O   TYR B  27     4036   3475   4974    839   -387   -634       O  
-ATOM   1765  CB  TYR B  27       5.518 -18.131  -4.821  1.00 23.31           C  
-ANISOU 1765  CB  TYR B  27     2942   2332   3585    526   -421   -431       C  
-ATOM   1766  CG  TYR B  27       4.058 -18.081  -5.221  1.00 24.33           C  
-ANISOU 1766  CG  TYR B  27     3122   2456   3666    395   -440   -400       C  
-ATOM   1767  CD1 TYR B  27       3.485 -19.083  -5.989  1.00 25.36           C  
-ANISOU 1767  CD1 TYR B  27     3333   2433   3870    362   -527   -481       C  
-ATOM   1768  CD2 TYR B  27       3.263 -17.021  -4.827  1.00 24.06           C  
-ANISOU 1768  CD2 TYR B  27     3049   2569   3524    306   -374   -290       C  
-ATOM   1769  CE1 TYR B  27       2.141 -19.025  -6.352  1.00 24.26           C  
-ANISOU 1769  CE1 TYR B  27     3215   2310   3694    221   -568   -429       C  
-ATOM   1770  CE2 TYR B  27       1.927 -16.949  -5.185  1.00 23.85           C  
-ANISOU 1770  CE2 TYR B  27     3028   2555   3480    198   -392   -235       C  
-ATOM   1771  CZ  TYR B  27       1.373 -17.956  -5.944  1.00 24.06           C  
-ANISOU 1771  CZ  TYR B  27     3115   2451   3577    146   -500   -293       C  
-ATOM   1772  OH  TYR B  27       0.035 -17.885  -6.304  1.00 25.02           O  
-ANISOU 1772  OH  TYR B  27     3217   2603   3688     19   -543   -218       O  
-ATOM   1773  N   ALA B  28       8.207 -20.080  -3.436  1.00 32.20           N  
-ANISOU 1773  N   ALA B  28     3956   3186   5094    820   -598   -349       N  
-ATOM   1774  CA  ALA B  28       9.664 -19.981  -3.253  1.00 37.43           C  
-ANISOU 1774  CA  ALA B  28     4487   3905   5829    963   -585   -359       C  
-ATOM   1775  C   ALA B  28      10.496 -20.414  -4.469  1.00 39.73           C  
-ANISOU 1775  C   ALA B  28     4735   4136   6223   1146   -499   -586       C  
-ATOM   1776  O   ALA B  28      11.576 -19.871  -4.715  1.00 41.19           O  
-ANISOU 1776  O   ALA B  28     4785   4467   6396   1239   -412   -640       O  
-ATOM   1777  CB  ALA B  28      10.105 -20.764  -2.019  1.00 38.29           C  
-ANISOU 1777  CB  ALA B  28     4558   3901   6090    988   -744   -149       C  
-ATOM   1778  N   GLU B  29      10.006 -21.404  -5.211  1.00 35.94           N  
-ANISOU 1778  N   GLU B  29     4370   3443   5842   1190   -518   -722       N  
-ATOM   1779  CA  GLU B  29      10.760 -21.966  -6.335  1.00 40.82           C  
-ANISOU 1779  CA  GLU B  29     4977   3978   6557   1375   -423   -969       C  
-ATOM   1780  C   GLU B  29      10.231 -21.465  -7.680  1.00 39.91           C  
-ANISOU 1780  C   GLU B  29     4952   3975   6236   1312   -294  -1186       C  
-ATOM   1781  O   GLU B  29      10.793 -21.757  -8.736  1.00 42.71           O  
-ANISOU 1781  O   GLU B  29     5314   4318   6595   1439   -178  -1418       O  
-ATOM   1782  CB  GLU B  29      10.729 -23.497  -6.288  1.00 48.79           C  
-ANISOU 1782  CB  GLU B  29     6073   4635   7830   1484   -534  -1009       C  
-ATOM   1783  CG  GLU B  29      11.745 -24.135  -5.330  1.00 59.92           C  
-ANISOU 1783  CG  GLU B  29     7349   5921   9497   1643   -631   -847       C  
-ATOM   1784  CD  GLU B  29      11.168 -24.480  -3.960  1.00 69.21           C  
-ANISOU 1784  CD  GLU B  29     8560   7000  10736   1508   -831   -540       C  
-ATOM   1785  OE1 GLU B  29      10.044 -25.028  -3.893  1.00 72.64           O  
-ANISOU 1785  OE1 GLU B  29     9154   7269  11178   1371   -920   -502       O  
-ATOM   1786  OE2 GLU B  29      11.851 -24.212  -2.948  1.00 70.59           O  
-ANISOU 1786  OE2 GLU B  29     8600   7279  10944   1524   -903   -327       O  
-ATOM   1787  N   ASP B  30       9.159 -20.687  -7.623  1.00 36.58           N  
-ANISOU 1787  N   ASP B  30     4591   3676   5631   1118   -311  -1099       N  
-ATOM   1788  CA  ASP B  30       8.426 -20.272  -8.813  1.00 36.02           C  
-ANISOU 1788  CA  ASP B  30     4617   3699   5370   1023   -243  -1246       C  
-ATOM   1789  C   ASP B  30       8.783 -18.867  -9.286  1.00 37.09           C  
-ANISOU 1789  C   ASP B  30     4665   4126   5300    991   -104  -1252       C  
-ATOM   1790  O   ASP B  30       8.342 -18.439 -10.355  1.00 36.65           O  
-ANISOU 1790  O   ASP B  30     4673   4179   5072    921    -42  -1359       O  
-ATOM   1791  CB  ASP B  30       6.929 -20.359  -8.528  1.00 34.44           C  
-ANISOU 1791  CB  ASP B  30     4519   3435   5132    833   -364  -1126       C  
-ATOM   1792  CG  ASP B  30       6.518 -21.732  -8.032  1.00 41.97           C  
-ANISOU 1792  CG  ASP B  30     5562   4093   6292    828   -515  -1088       C  
-ATOM   1793  OD1 ASP B  30       7.111 -22.720  -8.504  1.00 44.41           O  
-ANISOU 1793  OD1 ASP B  30     5928   4208   6740    961   -519  -1259       O  
-ATOM   1794  OD2 ASP B  30       5.614 -21.820  -7.171  1.00 43.35           O  
-ANISOU 1794  OD2 ASP B  30     5750   4225   6497    693   -619   -886       O  
-ATOM   1795  N   LEU B  31       9.571 -18.150  -8.481  1.00 34.07           N  
-ANISOU 1795  N   LEU B  31     4143   3867   4934   1021    -71  -1122       N  
-ATOM   1796  CA  LEU B  31       9.985 -16.782  -8.809  1.00 33.14           C  
-ANISOU 1796  CA  LEU B  31     3940   3999   4651    974     48  -1104       C  
-ATOM   1797  C   LEU B  31      11.497 -16.726  -8.986  1.00 36.06           C  
-ANISOU 1797  C   LEU B  31     4155   4463   5082   1118    149  -1169       C  
-ATOM   1798  O   LEU B  31      12.229 -17.490  -8.358  1.00 39.99           O  
-ANISOU 1798  O   LEU B  31     4573   4852   5769   1242     97  -1143       O  
-ATOM   1799  CB  LEU B  31       9.557 -15.798  -7.720  1.00 29.34           C  
-ANISOU 1799  CB  LEU B  31     3432   3597   4118    849      3   -899       C  
-ATOM   1800  CG  LEU B  31       8.077 -15.812  -7.380  1.00 29.67           C  
-ANISOU 1800  CG  LEU B  31     3582   3567   4125    721    -76   -805       C  
-ATOM   1801  CD1 LEU B  31       7.776 -14.842  -6.250  1.00 27.15           C  
-ANISOU 1801  CD1 LEU B  31     3235   3327   3755    627    -81   -635       C  
-ATOM   1802  CD2 LEU B  31       7.289 -15.473  -8.636  1.00 29.68           C  
-ANISOU 1802  CD2 LEU B  31     3654   3629   3994    655    -33   -894       C  
-ATOM   1803  N   GLU B  32      11.959 -15.836  -9.858  1.00 35.89           N  
-ANISOU 1803  N   GLU B  32     4078   4647   4912   1097    289  -1235       N  
-ATOM   1804  CA  GLU B  32      13.384 -15.716 -10.120  1.00 38.01           C  
-ANISOU 1804  CA  GLU B  32     4170   5043   5230   1218    408  -1289       C  
-ATOM   1805  C   GLU B  32      13.954 -14.578  -9.276  1.00 35.23           C  
-ANISOU 1805  C   GLU B  32     3682   4840   4862   1129    392  -1105       C  
-ATOM   1806  O   GLU B  32      14.986 -14.733  -8.620  1.00 39.65           O  
-ANISOU 1806  O   GLU B  32     4079   5423   5561   1208    368  -1039       O  
-ATOM   1807  CB  GLU B  32      13.634 -15.449 -11.606  1.00 39.54           C  
-ANISOU 1807  CB  GLU B  32     4374   5395   5254   1231    586  -1463       C  
-ATOM   1808  CG  GLU B  32      15.078 -15.618 -12.034  1.00 45.32           C  
-ANISOU 1808  CG  GLU B  32     4918   6246   6056   1385    742  -1552       C  
-ATOM   1809  CD  GLU B  32      15.560 -17.055 -11.934  1.00 55.76           C  
-ANISOU 1809  CD  GLU B  32     6242   7352   7593   1568    728  -1634       C  
-ATOM   1810  OE1 GLU B  32      14.714 -17.974 -11.962  1.00 58.10           O  
-ANISOU 1810  OE1 GLU B  32     6712   7427   7938   1589    638  -1723       O  
-ATOM   1811  OE2 GLU B  32      16.787 -17.267 -11.833  1.00 61.45           O  
-ANISOU 1811  OE2 GLU B  32     6785   8117   8447   1689    806  -1599       O  
-ATOM   1812  N   ARG B  33      13.273 -13.437  -9.306  1.00 30.91           N  
-ANISOU 1812  N   ARG B  33     3205   4385   4153    961    396  -1023       N  
-ATOM   1813  CA  ARG B  33      13.726 -12.222  -8.620  1.00 31.71           C  
-ANISOU 1813  CA  ARG B  33     3221   4611   4218    848    389   -879       C  
-ATOM   1814  C   ARG B  33      12.528 -11.387  -8.214  1.00 29.55           C  
-ANISOU 1814  C   ARG B  33     3085   4300   3841    698    337   -785       C  
-ATOM   1815  O   ARG B  33      11.485 -11.437  -8.869  1.00 32.15           O  
-ANISOU 1815  O   ARG B  33     3534   4590   4092    666    347   -824       O  
-ATOM   1816  CB  ARG B  33      14.573 -11.368  -9.573  1.00 33.79           C  
-ANISOU 1816  CB  ARG B  33     3372   5083   4384    819    537   -911       C  
-ATOM   1817  CG  ARG B  33      15.711 -12.081 -10.265  1.00 41.51           C  
-ANISOU 1817  CG  ARG B  33     4195   6140   5435    977    653  -1030       C  
-ATOM   1818  CD  ARG B  33      16.838 -12.359  -9.300  1.00 46.91           C  
-ANISOU 1818  CD  ARG B  33     4681   6834   6308   1054    591   -945       C  
-ATOM   1819  NE  ARG B  33      17.565 -11.141  -8.957  1.00 47.46           N  
-ANISOU 1819  NE  ARG B  33     4619   7075   6338    913    597   -813       N  
-ATOM   1820  CZ  ARG B  33      18.613 -11.105  -8.144  1.00 50.45           C  
-ANISOU 1820  CZ  ARG B  33     4803   7515   6850    922    527   -708       C  
-ATOM   1821  NH1 ARG B  33      19.055 -12.226  -7.590  1.00 53.13           N  
-ANISOU 1821  NH1 ARG B  33     5048   7758   7382   1087    446   -703       N  
-ATOM   1822  NH2 ARG B  33      19.218  -9.951  -7.891  1.00 48.89           N  
-ANISOU 1822  NH2 ARG B  33     4506   7467   6605    758    522   -596       N  
-ATOM   1823  N   VAL B  34      12.665 -10.592  -7.156  1.00 24.70           N  
-ANISOU 1823  N   VAL B  34     2454   3705   3227    602    284   -665       N  
-ATOM   1824  CA  VAL B  34      11.712  -9.496  -6.946  1.00 23.27           C  
-ANISOU 1824  CA  VAL B  34     2381   3514   2945    472    291   -597       C  
-ATOM   1825  C   VAL B  34      12.082  -8.389  -7.944  1.00 25.92           C  
-ANISOU 1825  C   VAL B  34     2680   3980   3187    405    397   -601       C  
-ATOM   1826  O   VAL B  34      13.258  -8.048  -8.074  1.00 25.92           O  
-ANISOU 1826  O   VAL B  34     2553   4094   3199    392    439   -595       O  
-ATOM   1827  CB  VAL B  34      11.786  -8.944  -5.533  1.00 25.11           C  
-ANISOU 1827  CB  VAL B  34     2633   3722   3185    384    220   -503       C  
-ATOM   1828  CG1 VAL B  34      10.873  -7.724  -5.397  1.00 26.94           C  
-ANISOU 1828  CG1 VAL B  34     2974   3928   3332    276    262   -462       C  
-ATOM   1829  CG2 VAL B  34      11.383 -10.014  -4.550  1.00 27.19           C  
-ANISOU 1829  CG2 VAL B  34     2938   3878   3515    428    114   -467       C  
-ATOM   1830  N   PHE B  35      11.092  -7.843  -8.654  1.00 25.73           N  
-ANISOU 1830  N   PHE B  35     2752   3946   3079    354    433   -586       N  
-ATOM   1831  CA  PHE B  35      11.359  -6.883  -9.724  1.00 27.87           C  
-ANISOU 1831  CA  PHE B  35     2999   4337   3253    285    522   -562       C  
-ATOM   1832  C   PHE B  35      10.979  -5.475  -9.274  1.00 29.01           C  
-ANISOU 1832  C   PHE B  35     3197   4438   3388    167    520   -450       C  
-ATOM   1833  O   PHE B  35      11.754  -4.525  -9.415  1.00 29.12           O  
-ANISOU 1833  O   PHE B  35     3158   4522   3385     80    563   -398       O  
-ATOM   1834  CB  PHE B  35      10.588  -7.289 -10.988  1.00 29.53           C  
-ANISOU 1834  CB  PHE B  35     3276   4577   3367    308    547   -611       C  
-ATOM   1835  CG  PHE B  35      11.120  -6.675 -12.256  1.00 31.87           C  
-ANISOU 1835  CG  PHE B  35     3533   5044   3533    253    647   -603       C  
-ATOM   1836  CD1 PHE B  35      12.412  -6.938 -12.679  1.00 32.26           C  
-ANISOU 1836  CD1 PHE B  35     3460   5235   3564    292    744   -673       C  
-ATOM   1837  CD2 PHE B  35      10.306  -5.865 -13.043  1.00 36.14           C  
-ANISOU 1837  CD2 PHE B  35     4147   5614   3970    163    647   -509       C  
-ATOM   1838  CE1 PHE B  35      12.908  -6.383 -13.864  1.00 37.45           C  
-ANISOU 1838  CE1 PHE B  35     4075   6078   4076    227    857   -656       C  
-ATOM   1839  CE2 PHE B  35      10.783  -5.304 -14.223  1.00 35.31           C  
-ANISOU 1839  CE2 PHE B  35     4014   5682   3720     92    732   -473       C  
-ATOM   1840  CZ  PHE B  35      12.088  -5.562 -14.634  1.00 39.83           C  
-ANISOU 1840  CZ  PHE B  35     4473   6413   4249    117    847   -551       C  
-ATOM   1841  N   ILE B  36       9.778  -5.346  -8.723  1.00 24.48           N  
-ANISOU 1841  N   ILE B  36     2725   3738   2840    165    476   -413       N  
-ATOM   1842  CA  ILE B  36       9.322  -4.082  -8.141  1.00 25.32           C  
-ANISOU 1842  CA  ILE B  36     2896   3759   2966     86    488   -334       C  
-ATOM   1843  C   ILE B  36       8.748  -4.366  -6.773  1.00 27.19           C  
-ANISOU 1843  C   ILE B  36     3194   3886   3251    106    446   -347       C  
-ATOM   1844  O   ILE B  36       7.647  -4.922  -6.660  1.00 25.26           O  
-ANISOU 1844  O   ILE B  36     2989   3582   3026    158    428   -338       O  
-ATOM   1845  CB  ILE B  36       8.232  -3.414  -8.996  1.00 24.09           C  
-ANISOU 1845  CB  ILE B  36     2792   3569   2791     72    510   -253       C  
-ATOM   1846  CG1 ILE B  36       8.646  -3.381 -10.463  1.00 28.11           C  
-ANISOU 1846  CG1 ILE B  36     3258   4219   3205     47    541   -234       C  
-ATOM   1847  CG2 ILE B  36       7.910  -1.999  -8.474  1.00 24.04           C  
-ANISOU 1847  CG2 ILE B  36     2848   3446   2840     10    540   -177       C  
-ATOM   1848  CD1 ILE B  36       7.561  -2.838 -11.406  1.00 27.78           C  
-ANISOU 1848  CD1 ILE B  36     3259   4168   3127     24    527   -124       C  
-ATOM   1849  N   PRO B  37       9.495  -4.002  -5.714  1.00 27.00           N  
-ANISOU 1849  N   PRO B  37     3175   3851   3234     46    427   -360       N  
-ATOM   1850  CA  PRO B  37       8.998  -4.286  -4.370  1.00 21.64           C  
-ANISOU 1850  CA  PRO B  37     2567   3098   2558     47    394   -371       C  
-ATOM   1851  C   PRO B  37       7.668  -3.589  -4.114  1.00 22.23           C  
-ANISOU 1851  C   PRO B  37     2738   3064   2643     53    459   -347       C  
-ATOM   1852  O   PRO B  37       7.466  -2.454  -4.564  1.00 21.25           O  
-ANISOU 1852  O   PRO B  37     2646   2888   2540     22    516   -322       O  
-ATOM   1853  CB  PRO B  37      10.071  -3.672  -3.465  1.00 23.15           C  
-ANISOU 1853  CB  PRO B  37     2764   3313   2721    -60    359   -387       C  
-ATOM   1854  CG  PRO B  37      11.341  -3.790  -4.267  1.00 24.13           C  
-ANISOU 1854  CG  PRO B  37     2749   3555   2862    -73    342   -380       C  
-ATOM   1855  CD  PRO B  37      10.888  -3.518  -5.705  1.00 26.27           C  
-ANISOU 1855  CD  PRO B  37     3005   3843   3134    -34    420   -361       C  
-ATOM   1856  N   HIS B  38       6.797  -4.257  -3.368  1.00 24.77           N  
-ANISOU 1856  N   HIS B  38     3967   3332   2111    323   -687   -261       N  
-ATOM   1857  CA  HIS B  38       5.488  -3.712  -3.015  1.00 26.09           C  
-ANISOU 1857  CA  HIS B  38     4063   3420   2429    122   -721   -114       C  
-ATOM   1858  C   HIS B  38       5.541  -2.261  -2.541  1.00 20.45           C  
-ANISOU 1858  C   HIS B  38     3049   2851   1871     92   -499   -149       C  
-ATOM   1859  O   HIS B  38       4.764  -1.416  -2.996  1.00 21.01           O  
-ANISOU 1859  O   HIS B  38     2971   2891   2121    -33   -457    -42       O  
-ATOM   1860  CB  HIS B  38       4.849  -4.532  -1.899  1.00 27.22           C  
-ANISOU 1860  CB  HIS B  38     4287   3463   2594     67   -738     12       C  
-ATOM   1861  CG  HIS B  38       3.534  -3.978  -1.447  1.00 28.37           C  
-ANISOU 1861  CG  HIS B  38     4183   3599   2996   -114   -623    257       C  
-ATOM   1862  ND1 HIS B  38       3.383  -3.290  -0.260  1.00 28.88           N  
-ANISOU 1862  ND1 HIS B  38     4083   3803   3089    -12   -376    277       N  
-ATOM   1863  CD2 HIS B  38       2.316  -3.982  -2.041  1.00 26.09           C  
-ANISOU 1863  CD2 HIS B  38     3777   3206   2931   -339   -730    504       C  
-ATOM   1864  CE1 HIS B  38       2.124  -2.918  -0.131  1.00 32.98           C  
-ANISOU 1864  CE1 HIS B  38     4385   4337   3810   -127   -286    548       C  
-ATOM   1865  NE2 HIS B  38       1.454  -3.322  -1.196  1.00 29.84           N  
-ANISOU 1865  NE2 HIS B  38     3970   3806   3563   -355   -500    700       N  
-ATOM   1866  N   GLY B  39       6.445  -1.989  -1.606  1.00 22.31           N  
-ANISOU 1866  N   GLY B  39     3238   3212   2027    226   -406   -308       N  
-ATOM   1867  CA  GLY B  39       6.566  -0.663  -1.019  1.00 22.10           C  
-ANISOU 1867  CA  GLY B  39     3027   3247   2124    217   -290   -374       C  
-ATOM   1868  C   GLY B  39       6.923   0.399  -2.056  1.00 22.95           C  
-ANISOU 1868  C   GLY B  39     2984   3383   2353    111   -273   -376       C  
-ATOM   1869  O   GLY B  39       6.502   1.556  -1.939  1.00 23.52           O  
-ANISOU 1869  O   GLY B  39     2961   3400   2576     39   -219   -353       O  
-ATOM   1870  N   LEU B  40       7.701   0.015  -3.061  1.00 21.25           N  
-ANISOU 1870  N   LEU B  40     2778   3254   2043    145   -309   -383       N  
-ATOM   1871  CA  LEU B  40       8.060   0.937  -4.131  1.00 23.76           C  
-ANISOU 1871  CA  LEU B  40     2955   3621   2452     65   -252   -315       C  
-ATOM   1872  C   LEU B  40       6.828   1.235  -4.991  1.00 24.08           C  
-ANISOU 1872  C   LEU B  40     3053   3512   2584    -33   -263   -173       C  
-ATOM   1873  O   LEU B  40       6.633   2.365  -5.456  1.00 19.69           O  
-ANISOU 1873  O   LEU B  40     2395   2916   2169   -134   -200   -107       O  
-ATOM   1874  CB  LEU B  40       9.223   0.376  -4.967  1.00 22.11           C  
-ANISOU 1874  CB  LEU B  40     2736   3609   2057    226   -234   -308       C  
-ATOM   1875  CG  LEU B  40       9.597   1.153  -6.233  1.00 30.80           C  
-ANISOU 1875  CG  LEU B  40     3705   4799   3198    198   -124   -157       C  
-ATOM   1876  CD1 LEU B  40       9.784   2.648  -5.949  1.00 29.12           C  
-ANISOU 1876  CD1 LEU B  40     3243   4551   3270    -45    -63   -110       C  
-ATOM   1877  CD2 LEU B  40      10.852   0.577  -6.885  1.00 30.93           C  
-ANISOU 1877  CD2 LEU B  40     3665   5101   2986    451    -46   -106       C  
-ATOM   1878  N   ILE B  41       5.978   0.231  -5.194  1.00 20.13           N  
-ANISOU 1878  N   ILE B  41     2726   2906   2018    -18   -383   -113       N  
-ATOM   1879  CA  ILE B  41       4.711   0.464  -5.896  1.00 21.13           C  
-ANISOU 1879  CA  ILE B  41     2866   2895   2268   -128   -456     33       C  
-ATOM   1880  C   ILE B  41       3.866   1.489  -5.135  1.00 22.31           C  
-ANISOU 1880  C   ILE B  41     2834   3024   2619   -214   -343     94       C  
-ATOM   1881  O   ILE B  41       3.255   2.382  -5.739  1.00 20.89           O  
-ANISOU 1881  O   ILE B  41     2588   2798   2551   -262   -321    176       O  
-ATOM   1882  CB  ILE B  41       3.917  -0.842  -6.067  1.00 23.71           C  
-ANISOU 1882  CB  ILE B  41     3382   3076   2553   -162   -684    115       C  
-ATOM   1883  CG1 ILE B  41       4.705  -1.809  -6.954  1.00 24.57           C  
-ANISOU 1883  CG1 ILE B  41     3790   3156   2391     15   -844     30       C  
-ATOM   1884  CG2 ILE B  41       2.561  -0.568  -6.695  1.00 21.33           C  
-ANISOU 1884  CG2 ILE B  41     3018   2652   2435   -308   -809    288       C  
-ATOM   1885  CD1 ILE B  41       4.111  -3.225  -7.024  1.00 29.83           C  
-ANISOU 1885  CD1 ILE B  41     4725   3593   3016    -17  -1124     72       C  
-ATOM   1886  N  AMET B  42       3.838   1.364  -3.814  0.29 19.85           N  
-ANISOU 1886  N  AMET B  42     2486   2750   2307   -168   -271     54       N  
-ATOM   1887  N  BMET B  42       3.830   1.361  -3.814  0.71 19.67           N  
-ANISOU 1887  N  BMET B  42     2463   2726   2284   -168   -271     56       N  
-ATOM   1888  CA AMET B  42       3.065   2.278  -2.978  0.29 19.81           C  
-ANISOU 1888  CA AMET B  42     2375   2747   2407   -126   -151    110       C  
-ATOM   1889  CA BMET B  42       3.064   2.296  -2.981  0.71 19.31           C  
-ANISOU 1889  CA BMET B  42     2310   2683   2344   -126   -150    109       C  
-ATOM   1890  C  AMET B  42       3.578   3.703  -3.081  0.29 20.72           C  
-ANISOU 1890  C  AMET B  42     2471   2827   2573   -112   -103      2       C  
-ATOM   1891  C  BMET B  42       3.579   3.712  -3.095  0.71 21.41           C  
-ANISOU 1891  C  BMET B  42     2559   2914   2661   -113   -103      2       C  
-ATOM   1892  O  AMET B  42       2.795   4.645  -3.225  0.29 21.11           O  
-ANISOU 1892  O  AMET B  42     2489   2822   2710    -89    -60     78       O  
-ATOM   1893  O  BMET B  42       2.801   4.665  -3.259  0.71 20.73           O  
-ANISOU 1893  O  BMET B  42     2441   2772   2664    -92    -61     78       O  
-ATOM   1894  CB AMET B  42       3.081   1.808  -1.522  0.29 20.54           C  
-ANISOU 1894  CB AMET B  42     2502   2894   2408     10    -74     82       C  
-ATOM   1895  CB BMET B  42       3.072   1.848  -1.511  0.71 19.74           C  
-ANISOU 1895  CB BMET B  42     2399   2793   2309     13    -71     82       C  
-ATOM   1896  CG AMET B  42       2.595   0.387  -1.369  0.29 22.66           C  
-ANISOU 1896  CG AMET B  42     2806   3155   2647    -44   -132    236       C  
-ATOM   1897  CG BMET B  42       2.444   0.486  -1.247  0.71 24.43           C  
-ANISOU 1897  CG BMET B  42     3010   3387   2884    -32   -108    259       C  
-ATOM   1898  SD AMET B  42       1.019   0.161  -2.200  0.29 37.14           S  
-ANISOU 1898  SD AMET B  42     4476   4939   4696   -234   -216    560       S  
-ATOM   1899  SD BMET B  42       0.692   0.413  -1.660  0.71 29.67           S  
-ANISOU 1899  SD BMET B  42     3458   4049   3766   -168   -112    622       S  
-ATOM   1900  CE AMET B  42      -0.100   0.576  -0.857  0.29 30.48           C  
-ANISOU 1900  CE AMET B  42     3420   4250   3909    -75     43    808       C  
-ATOM   1901  CE BMET B  42       0.826  -0.216  -3.341  0.71 40.65           C  
-ANISOU 1901  CE BMET B  42     4966   5283   5197   -378   -415    602       C  
-ATOM   1902  N   ASP B  43       4.895   3.856  -3.022  1.00 19.86           N  
-ANISOU 1902  N   ASP B  43     2380   2745   2421   -132   -134   -152       N  
-ATOM   1903  CA  ASP B  43       5.512   5.178  -3.100  1.00 20.09           C  
-ANISOU 1903  CA  ASP B  43     2386   2697   2551   -198   -150   -218       C  
-ATOM   1904  C   ASP B  43       5.201   5.843  -4.433  1.00 22.69           C  
-ANISOU 1904  C   ASP B  43     2687   2964   2969   -305   -123    -81       C  
-ATOM   1905  O   ASP B  43       4.925   7.046  -4.487  1.00 20.99           O  
-ANISOU 1905  O   ASP B  43     2515   2610   2852   -335   -128    -64       O  
-ATOM   1906  CB  ASP B  43       7.027   5.075  -2.969  1.00 22.09           C  
-ANISOU 1906  CB  ASP B  43     2563   3037   2795   -257   -212   -328       C  
-ATOM   1907  CG  ASP B  43       7.485   4.756  -1.548  1.00 30.44           C  
-ANISOU 1907  CG  ASP B  43     3682   4116   3769   -131   -290   -507       C  
-ATOM   1908  OD1 ASP B  43       6.766   5.087  -0.576  1.00 28.70           O  
-ANISOU 1908  OD1 ASP B  43     3599   3796   3508     12   -293   -562       O  
-ATOM   1909  OD2 ASP B  43       8.583   4.179  -1.423  1.00 29.88           O  
-ANISOU 1909  OD2 ASP B  43     3528   4182   3643   -124   -344   -582       O  
-ATOM   1910  N   ARG B  44       5.279   5.071  -5.510  1.00 18.05           N  
-ANISOU 1910  N   ARG B  44     2090   2457   2312   -322   -117      7       N  
-ATOM   1911  CA  ARG B  44       5.011   5.635  -6.833  1.00 18.67           C  
-ANISOU 1911  CA  ARG B  44     2188   2484   2422   -364    -93    140       C  
-ATOM   1912  C   ARG B  44       3.517   5.964  -6.959  1.00 21.26           C  
-ANISOU 1912  C   ARG B  44     2555   2709   2816   -331   -123    223       C  
-ATOM   1913  O   ARG B  44       3.141   7.024  -7.470  1.00 22.18           O  
-ANISOU 1913  O   ARG B  44     2701   2724   3002   -343    -99    290       O  
-ATOM   1914  CB  ARG B  44       5.440   4.658  -7.929  1.00 18.42           C  
-ANISOU 1914  CB  ARG B  44     2219   2556   2222   -286   -109    196       C  
-ATOM   1915  CG  ARG B  44       5.094   5.130  -9.340  1.00 21.68           C  
-ANISOU 1915  CG  ARG B  44     2718   2917   2603   -253    -92    337       C  
-ATOM   1916  CD  ARG B  44       5.686   6.511  -9.641  1.00 20.43           C  
-ANISOU 1916  CD  ARG B  44     2470   2728   2565   -359     42    433       C  
-ATOM   1917  NE  ARG B  44       5.392   6.922 -11.022  1.00 22.80           N  
-ANISOU 1917  NE  ARG B  44     2887   2986   2791   -283     86    592       N  
-ATOM   1918  CZ  ARG B  44       5.280   8.187 -11.417  1.00 28.74           C  
-ANISOU 1918  CZ  ARG B  44     3651   3612   3656   -369    157    710       C  
-ATOM   1919  NH1 ARG B  44       5.468   9.166 -10.533  1.00 27.79           N  
-ANISOU 1919  NH1 ARG B  44     3455   3366   3736   -547    152    672       N  
-ATOM   1920  NH2 ARG B  44       4.998   8.479 -12.695  1.00 26.75           N  
-ANISOU 1920  NH2 ARG B  44     3543   3327   3294   -252    203    860       N  
-ATOM   1921  N   THR B  45       2.681   5.065  -6.440  1.00 20.88           N  
-ANISOU 1921  N   THR B  45     2484   2696   2754   -289   -177    249       N  
-ATOM   1922  CA  THR B  45       1.226   5.246  -6.452  1.00 21.15           C  
-ANISOU 1922  CA  THR B  45     2448   2706   2880   -256   -203    389       C  
-ATOM   1923  C   THR B  45       0.796   6.478  -5.662  1.00 22.83           C  
-ANISOU 1923  C   THR B  45     2640   2890   3143   -138    -92    379       C  
-ATOM   1924  O   THR B  45      -0.123   7.204  -6.073  1.00 22.44           O  
-ANISOU 1924  O   THR B  45     2565   2810   3149    -65    -87    484       O  
-ATOM   1925  CB  THR B  45       0.497   3.969  -5.978  1.00 25.19           C  
-ANISOU 1925  CB  THR B  45     2881   3277   3413   -287   -284    495       C  
-ATOM   1926  OG1 THR B  45       0.863   2.883  -6.840  1.00 24.16           O  
-ANISOU 1926  OG1 THR B  45     2883   3095   3203   -360   -467    480       O  
-ATOM   1927  CG2 THR B  45      -1.034   4.132  -6.040  1.00 21.86           C  
-ANISOU 1927  CG2 THR B  45     2274   2892   3140   -280   -316    721       C  
-ATOM   1928  N   GLU B  46       1.471   6.746  -4.552  1.00 19.62           N  
-ANISOU 1928  N   GLU B  46     2291   2476   2687    -72    -36    239       N  
-ATOM   1929  CA  GLU B  46       1.192   7.971  -3.812  1.00 23.03           C  
-ANISOU 1929  CA  GLU B  46     2828   2815   3106    103      6    185       C  
-ATOM   1930  C   GLU B  46       1.371   9.200  -4.690  1.00 23.47           C  
-ANISOU 1930  C   GLU B  46     3000   2692   3225     38    -43    181       C  
-ATOM   1931  O   GLU B  46       0.544  10.115  -4.661  1.00 21.14           O  
-ANISOU 1931  O   GLU B  46     2793   2320   2920    211    -27    228       O  
-ATOM   1932  CB  GLU B  46       2.111   8.105  -2.598  1.00 18.88           C  
-ANISOU 1932  CB  GLU B  46     2429   2242   2501    175    -26    -12       C  
-ATOM   1933  CG  GLU B  46       1.803   9.348  -1.774  1.00 24.79           C  
-ANISOU 1933  CG  GLU B  46     3403   2836   3180    427    -54   -102       C  
-ATOM   1934  CD  GLU B  46       2.705   9.472  -0.553  1.00 30.85           C  
-ANISOU 1934  CD  GLU B  46     4360   3513   3850    526   -171   -326       C  
-ATOM   1935  OE1 GLU B  46       2.514  10.415   0.226  1.00 30.47           O  
-ANISOU 1935  OE1 GLU B  46     4590   3296   3691    790   -255   -438       O  
-ATOM   1936  OE2 GLU B  46       3.591   8.616  -0.372  1.00 33.64           O  
-ANISOU 1936  OE2 GLU B  46     4617   3953   4211    382   -209   -400       O  
-ATOM   1937  N   ARG B  47       2.457   9.240  -5.461  1.00 22.42           N  
-ANISOU 1937  N   ARG B  47     2872   2505   3141   -179    -86    156       N  
-ATOM   1938  CA  ARG B  47       2.693  10.398  -6.327  1.00 22.64           C  
-ANISOU 1938  CA  ARG B  47     3009   2353   3241   -272   -111    214       C  
-ATOM   1939  C   ARG B  47       1.680  10.422  -7.462  1.00 23.15           C  
-ANISOU 1939  C   ARG B  47     3065   2440   3289   -204    -81    368       C  
-ATOM   1940  O   ARG B  47       1.242  11.489  -7.895  1.00 26.52           O  
-ANISOU 1940  O   ARG B  47     3630   2711   3735   -144    -93    423       O  
-ATOM   1941  CB  ARG B  47       4.128  10.396  -6.880  1.00 24.24           C  
-ANISOU 1941  CB  ARG B  47     3143   2558   3508   -510   -114    239       C  
-ATOM   1942  CG  ARG B  47       4.417  11.504  -7.913  1.00 26.47           C  
-ANISOU 1942  CG  ARG B  47     3507   2672   3877   -642    -99    392       C  
-ATOM   1943  CD  ARG B  47       4.158  12.908  -7.363  1.00 29.19           C  
-ANISOU 1943  CD  ARG B  47     4089   2699   4302   -636   -226    340       C  
-ATOM   1944  NE  ARG B  47       4.267  13.936  -8.410  1.00 30.90           N  
-ANISOU 1944  NE  ARG B  47     4427   2720   4595   -757   -213    523       N  
-ATOM   1945  CZ  ARG B  47       5.298  14.769  -8.547  1.00 38.01           C  
-ANISOU 1945  CZ  ARG B  47     5350   3425   5669  -1041   -290    629       C  
-ATOM   1946  NH1 ARG B  47       6.325  14.720  -7.707  1.00 40.40           N  
-ANISOU 1946  NH1 ARG B  47     5539   3706   6106  -1240   -429    548       N  
-ATOM   1947  NH2 ARG B  47       5.303  15.668  -9.523  1.00 39.80           N  
-ANISOU 1947  NH2 ARG B  47     5703   3466   5953  -1141   -252    843       N  
-ATOM   1948  N   LEU B  48       1.298   9.251  -7.954  1.00 20.59           N  
-ANISOU 1948  N   LEU B  48     2621   2279   2925   -204    -90    431       N  
-ATOM   1949  CA  LEU B  48       0.304   9.222  -9.034  1.00 24.66           C  
-ANISOU 1949  CA  LEU B  48     3141   2797   3434   -138   -147    562       C  
-ATOM   1950  C   LEU B  48      -1.020   9.789  -8.567  1.00 24.91           C  
-ANISOU 1950  C   LEU B  48     3119   2838   3506     42   -147    627       C  
-ATOM   1951  O   LEU B  48      -1.693  10.473  -9.331  1.00 26.83           O  
-ANISOU 1951  O   LEU B  48     3424   3019   3751    138   -183    710       O  
-ATOM   1952  CB  LEU B  48       0.091   7.811  -9.601  1.00 22.92           C  
-ANISOU 1952  CB  LEU B  48     2858   2682   3168   -177   -264    605       C  
-ATOM   1953  CG  LEU B  48       1.217   7.263 -10.483  1.00 28.61           C  
-ANISOU 1953  CG  LEU B  48     3694   3417   3759   -218   -267    580       C  
-ATOM   1954  CD1 LEU B  48       0.926   5.845 -10.915  1.00 30.39           C  
-ANISOU 1954  CD1 LEU B  48     3971   3678   3896   -196   -458    584       C  
-ATOM   1955  CD2 LEU B  48       1.445   8.136 -11.694  1.00 32.47           C  
-ANISOU 1955  CD2 LEU B  48     4324   3825   4188   -167   -214    672       C  
-ATOM   1956  N   ALA B  49      -1.399   9.516  -7.317  1.00 21.19           N  
-ANISOU 1956  N   ALA B  49     2536   2473   3041    142    -89    610       N  
-ATOM   1957  CA  ALA B  49      -2.678  10.038  -6.804  1.00 22.15           C  
-ANISOU 1957  CA  ALA B  49     2567   2685   3164    404    -34    725       C  
-ATOM   1958  C   ALA B  49      -2.670  11.549  -6.851  1.00 25.94           C  
-ANISOU 1958  C   ALA B  49     3308   2970   3576    585    -18    656       C  
-ATOM   1959  O   ALA B  49      -3.673  12.200  -7.201  1.00 25.32           O  
-ANISOU 1959  O   ALA B  49     3227   2915   3479    804    -18    764       O  
-ATOM   1960  CB  ALA B  49      -2.925   9.549  -5.372  1.00 23.29           C  
-ANISOU 1960  CB  ALA B  49     2588   2993   3266    549     85    745       C  
-ATOM   1961  N   ARG B  50      -1.536  12.126  -6.473  1.00 24.79           N  
-ANISOU 1961  N   ARG B  50     3402   2617   3402    497    -39    486       N  
-ATOM   1962  CA  ARG B  50      -1.434  13.577  -6.497  1.00 28.34           C  
-ANISOU 1962  CA  ARG B  50     4175   2788   3804    618    -97    422       C  
-ATOM   1963  C   ARG B  50      -1.492  14.102  -7.925  1.00 29.91           C  
-ANISOU 1963  C   ARG B  50     4455   2862   4048    509   -134    529       C  
-ATOM   1964  O   ARG B  50      -2.117  15.127  -8.180  1.00 31.29           O  
-ANISOU 1964  O   ARG B  50     4836   2891   4161    720   -165    563       O  
-ATOM   1965  CB  ARG B  50      -0.180  14.068  -5.775  1.00 33.01           C  
-ANISOU 1965  CB  ARG B  50     4994   3139   4412    477   -199    242       C  
-ATOM   1966  CG  ARG B  50      -0.288  15.527  -5.339  1.00 48.99           C  
-ANISOU 1966  CG  ARG B  50     7437   4822   6355    686   -336    149       C  
-ATOM   1967  CD  ARG B  50       0.951  15.962  -4.587  1.00 57.12           C  
-ANISOU 1967  CD  ARG B  50     8690   5570   7442    499   -542    -29       C  
-ATOM   1968  NE  ARG B  50       2.087  16.140  -5.486  1.00 63.99           N  
-ANISOU 1968  NE  ARG B  50     9488   6298   8528     30   -610     59       N  
-ATOM   1969  CZ  ARG B  50       3.361  16.039  -5.121  1.00 66.17           C  
-ANISOU 1969  CZ  ARG B  50     9704   6489   8950   -283   -748     -4       C  
-ATOM   1970  NH1 ARG B  50       3.679  15.744  -3.869  1.00 65.25           N  
-ANISOU 1970  NH1 ARG B  50     9646   6375   8770   -174   -873   -206       N  
-ATOM   1971  NH2 ARG B  50       4.320  16.226  -6.014  1.00 66.02           N  
-ANISOU 1971  NH2 ARG B  50     9545   6408   9131   -678   -754    164       N  
-ATOM   1972  N   ASP B  51      -0.867  13.398  -8.868  1.00 27.52           N  
-ANISOU 1972  N   ASP B  51     4032   2620   3806    246   -127    588       N  
-ATOM   1973  CA  ASP B  51      -0.943  13.816 -10.278  1.00 27.47           C  
-ANISOU 1973  CA  ASP B  51     4130   2521   3787    210   -139    713       C  
-ATOM   1974  C   ASP B  51      -2.375  13.739 -10.816  1.00 26.16           C  
-ANISOU 1974  C   ASP B  51     3890   2473   3577    452   -188    810       C  
-ATOM   1975  O   ASP B  51      -2.811  14.599 -11.579  1.00 30.98           O  
-ANISOU 1975  O   ASP B  51     4684   2951   4137    584   -218    880       O  
-ATOM   1976  CB  ASP B  51      -0.042  12.941 -11.163  1.00 32.95           C  
-ANISOU 1976  CB  ASP B  51     4732   3311   4478     -1   -104    770       C  
-ATOM   1977  CG  ASP B  51       1.435  13.053 -10.813  1.00 36.27           C  
-ANISOU 1977  CG  ASP B  51     5143   3672   4965   -243    -47    741       C  
-ATOM   1978  OD1 ASP B  51       1.838  14.048 -10.177  1.00 38.90           O  
-ANISOU 1978  OD1 ASP B  51     5611   3789   5380   -319    -89    697       O  
-ATOM   1979  OD2 ASP B  51       2.190  12.124 -11.183  1.00 37.95           O  
-ANISOU 1979  OD2 ASP B  51     5224   4052   5144   -340      7    768       O  
-ATOM   1980  N   VAL B  52      -3.103  12.693 -10.434  1.00 27.27           N  
-ANISOU 1980  N   VAL B  52     3745   2862   3755    496   -217    841       N  
-ATOM   1981  CA  VAL B  52      -4.497  12.551 -10.875  1.00 30.10           C  
-ANISOU 1981  CA  VAL B  52     3931   3370   4136    681   -311    979       C  
-ATOM   1982  C   VAL B  52      -5.336  13.707 -10.370  1.00 30.95           C  
-ANISOU 1982  C   VAL B  52     4113   3465   4181   1021   -251   1011       C  
-ATOM   1983  O   VAL B  52      -6.105  14.329 -11.122  1.00 33.42           O  
-ANISOU 1983  O   VAL B  52     4488   3755   4453   1217   -321   1093       O  
-ATOM   1984  CB  VAL B  52      -5.101  11.221 -10.364  1.00 32.56           C  
-ANISOU 1984  CB  VAL B  52     3874   3939   4560    601   -368   1069       C  
-ATOM   1985  CG1 VAL B  52      -6.616  11.218 -10.516  1.00 28.57           C  
-ANISOU 1985  CG1 VAL B  52     3082   3631   4140    786   -462   1272       C  
-ATOM   1986  CG2 VAL B  52      -4.477  10.043 -11.093  1.00 36.27           C  
-ANISOU 1986  CG2 VAL B  52     4356   4381   5045    341   -511   1038       C  
-ATOM   1987  N  AMET B  53      -5.173  13.998  -9.084  0.48 31.13           N  
-ANISOU 1987  N  AMET B  53     4175   3497   4155   1152   -136    934       N  
-ATOM   1988  N  BMET B  53      -5.199  14.025  -9.092  0.52 31.35           N  
-ANISOU 1988  N  BMET B  53     4205   3524   4181   1160   -136    936       N  
-ATOM   1989  CA AMET B  53      -5.864  15.116  -8.438  0.48 37.00           C  
-ANISOU 1989  CA AMET B  53     5089   4209   4759   1578    -78    933       C  
-ATOM   1990  CA BMET B  53      -5.983  15.131  -8.546  0.52 36.59           C  
-ANISOU 1990  CA BMET B  53     5021   4172   4709   1595    -84    951       C  
-ATOM   1991  C  AMET B  53      -5.572  16.446  -9.123  0.48 37.86           C  
-ANISOU 1991  C  AMET B  53     5648   3959   4776   1652   -159    862       C  
-ATOM   1992  C  BMET B  53      -5.580  16.491  -9.119  0.52 37.93           C  
-ANISOU 1992  C  BMET B  53     5670   3961   4781   1663   -160    861       C  
-ATOM   1993  O  AMET B  53      -6.466  17.270  -9.323  0.48 39.64           O  
-ANISOU 1993  O  AMET B  53     5997   4177   4889   2018   -175    924       O  
-ATOM   1994  O  BMET B  53      -6.420  17.381  -9.255  0.52 39.82           O  
-ANISOU 1994  O  BMET B  53     6065   4169   4897   2036   -175    909       O  
-ATOM   1995  CB AMET B  53      -5.458  15.201  -6.962  0.48 39.68           C  
-ANISOU 1995  CB AMET B  53     5538   4539   5000   1723     16    810       C  
-ATOM   1996  CB BMET B  53      -5.968  15.125  -7.014  0.52 38.59           C  
-ANISOU 1996  CB BMET B  53     5283   4518   4860   1828     41    889       C  
-ATOM   1997  CG AMET B  53      -5.883  16.492  -6.275  0.48 46.98           C  
-ANISOU 1997  CG AMET B  53     6836   5318   5698   2220     26    740       C  
-ATOM   1998  CG BMET B  53      -6.761  13.967  -6.406  0.52 37.79           C  
-ANISOU 1998  CG BMET B  53     4684   4839   4834   1881    163   1089       C  
-ATOM   1999  SD AMET B  53      -7.613  16.507  -5.768  0.48 45.73           S  
-ANISOU 1999  SD AMET B  53     6355   5618   5402   2836    207    992       S  
-ATOM   2000  SD BMET B  53      -8.491  13.876  -6.948  0.52 43.35           S  
-ANISOU 2000  SD BMET B  53     4934   5920   5618   2145    175   1427       S  
-ATOM   2001  CE AMET B  53      -7.514  15.668  -4.188  0.48 38.40           C  
-ANISOU 2001  CE AMET B  53     5237   4961   4392   2933    401    999       C  
-ATOM   2002  CE BMET B  53      -9.216  15.237  -6.046  0.52 62.25           C  
-ANISOU 2002  CE BMET B  53     7584   8369   7698   2781    341   1395       C  
-ATOM   2003  N   LYS B  54      -4.309  16.651  -9.475  1.00 36.31           N  
-ANISOU 2003  N   LYS B  54     5684   3476   4634   1310   -206    768       N  
-ATOM   2004  CA  LYS B  54      -3.879  17.893 -10.129  1.00 39.15           C  
-ANISOU 2004  CA  LYS B  54     6475   3451   4951   1286   -284    759       C  
-ATOM   2005  C   LYS B  54      -4.577  18.052 -11.475  1.00 42.41           C  
-ANISOU 2005  C   LYS B  54     6886   3900   5328   1384   -307    904       C  
-ATOM   2006  O   LYS B  54      -4.918  19.156 -11.885  1.00 42.57           O  
-ANISOU 2006  O   LYS B  54     7245   3686   5242   1597   -361    932       O  
-ATOM   2007  CB  LYS B  54      -2.355  17.919 -10.326  1.00 39.27           C  
-ANISOU 2007  CB  LYS B  54     6596   3233   5091    834   -306    730       C  
-ATOM   2008  CG  LYS B  54      -1.813  19.129 -11.114  1.00 50.72           C  
-ANISOU 2008  CG  LYS B  54     8437   4280   6556    707   -374    817       C  
-ATOM   2009  CD  LYS B  54      -1.216  20.186 -10.193  1.00 59.46           C  
-ANISOU 2009  CD  LYS B  54     9931   4974   7688    659   -547    700       C  
-ATOM   2010  CE  LYS B  54      -0.028  20.914 -10.831  1.00 65.70           C  
-ANISOU 2010  CE  LYS B  54    10888   5426   8647    223   -611    842       C  
-ATOM   2011  NZ  LYS B  54      -0.390  21.708 -12.034  1.00 70.36           N  
-ANISOU 2011  NZ  LYS B  54    11620   5936   9178    283   -553   1002       N  
-ATOM   2012  N   GLU B  55      -4.829  16.936 -12.146  1.00 40.19           N  
-ANISOU 2012  N   GLU B  55     6270   3887   5113   1263   -307    985       N  
-ATOM   2013  CA AGLU B  55      -5.354  16.978 -13.503  0.51 44.42           C  
-ANISOU 2013  CA AGLU B  55     6847   4432   5599   1343   -387   1098       C  
-ATOM   2014  CA BGLU B  55      -5.355  16.969 -13.509  0.49 44.40           C  
-ANISOU 2014  CA BGLU B  55     6842   4431   5597   1342   -388   1099       C  
-ATOM   2015  C   GLU B  55      -6.874  16.791 -13.589  1.00 45.27           C  
-ANISOU 2015  C   GLU B  55     6696   4807   5696   1668   -486   1184       C  
-ATOM   2016  O   GLU B  55      -7.534  17.408 -14.428  1.00 47.22           O  
-ANISOU 2016  O   GLU B  55     7092   4999   5851   1904   -576   1251       O  
-ATOM   2017  CB AGLU B  55      -4.629  15.936 -14.356  0.51 44.31           C  
-ANISOU 2017  CB AGLU B  55     6731   4485   5622   1055   -403   1130       C  
-ATOM   2018  CB BGLU B  55      -4.647  15.914 -14.370  0.49 44.33           C  
-ANISOU 2018  CB BGLU B  55     6727   4492   5624   1057   -406   1131       C  
-ATOM   2019  CG AGLU B  55      -4.882  16.052 -15.845  0.51 49.27           C  
-ANISOU 2019  CG AGLU B  55     7536   5051   6134   1161   -492   1229       C  
-ATOM   2020  CG BGLU B  55      -5.244  15.720 -15.760  0.49 47.97           C  
-ANISOU 2020  CG BGLU B  55     7250   4982   5994   1192   -547   1224       C  
-ATOM   2021  CD AGLU B  55      -3.838  15.316 -16.668  0.51 53.07           C  
-ANISOU 2021  CD AGLU B  55     8078   5530   6556    962   -448   1265       C  
-ATOM   2022  CD BGLU B  55      -5.079  16.938 -16.652  0.49 50.01           C  
-ANISOU 2022  CD BGLU B  55     7920   4970   6111   1330   -504   1302       C  
-ATOM   2023  OE1AGLU B  55      -2.747  15.031 -16.130  0.51 49.67           O  
-ANISOU 2023  OE1AGLU B  55     7583   5101   6189    718   -309   1234       O  
-ATOM   2024  OE1BGLU B  55      -3.962  17.496 -16.694  0.49 48.96           O  
-ANISOU 2024  OE1BGLU B  55     8007   4622   5973   1140   -353   1341       O  
-ATOM   2025  OE2AGLU B  55      -4.108  15.032 -17.855  0.51 59.46           O  
-ANISOU 2025  OE2AGLU B  55     9016   6347   7229   1101   -560   1325       O  
-ATOM   2026  OE2BGLU B  55      -6.065  17.334 -17.314  0.49 53.65           O  
-ANISOU 2026  OE2BGLU B  55     8442   5452   6489   1593   -628   1336       O  
-ATOM   2027  N   MET B  56      -7.432  15.958 -12.714  1.00 43.11           N  
-ANISOU 2027  N   MET B  56     6015   4838   5525   1684   -469   1217       N  
-ATOM   2028  CA  MET B  56      -8.850  15.591 -12.811  1.00 48.45           C  
-ANISOU 2028  CA  MET B  56     6301   5838   6269   1909   -575   1383       C  
-ATOM   2029  C   MET B  56      -9.778  16.099 -11.708  1.00 55.58           C  
-ANISOU 2029  C   MET B  56     7022   6977   7120   2320   -437   1474       C  
-ATOM   2030  O   MET B  56     -10.991  15.888 -11.775  1.00 61.17           O  
-ANISOU 2030  O   MET B  56     7344   7995   7904   2456   -491   1625       O  
-ATOM   2031  CB  MET B  56      -8.996  14.070 -12.898  1.00 47.64           C  
-ANISOU 2031  CB  MET B  56     5785   5950   6365   1597   -709   1466       C  
-ATOM   2032  CG  MET B  56      -8.129  13.412 -13.939  1.00 46.63           C  
-ANISOU 2032  CG  MET B  56     5860   5632   6227   1294   -854   1377       C  
-ATOM   2033  SD  MET B  56      -8.517  11.668 -14.032  1.00 44.96           S  
-ANISOU 2033  SD  MET B  56     5259   5604   6221   1001  -1121   1470       S  
-ATOM   2034  CE  MET B  56     -10.153  11.728 -14.776  1.00 46.19           C  
-ANISOU 2034  CE  MET B  56     5117   5933   6500   1191  -1449   1674       C  
-ATOM   2035  N   GLY B  57      -9.223  16.749 -10.693  1.00 59.09           N  
-ANISOU 2035  N   GLY B  57     9238   5007   8205    227   -904   1087       N  
-ATOM   2036  CA  GLY B  57     -10.034  17.286  -9.614  1.00 66.33           C  
-ANISOU 2036  CA  GLY B  57    10101   5758   9343    451   -851    949       C  
-ATOM   2037  C   GLY B  57      -9.962  18.800  -9.542  1.00 75.36           C  
-ANISOU 2037  C   GLY B  57    11523   6606  10504    458   -796    964       C  
-ATOM   2038  O   GLY B  57      -8.872  19.375  -9.565  1.00 80.02           O  
-ANISOU 2038  O   GLY B  57    12327   7119  10957    177   -704    981       O  
-ATOM   2039  N   GLY B  58     -11.117  19.448  -9.414  1.00 78.08           N  
-ANISOU 2039  N   GLY B  58    11842   6799  11027    771   -842    945       N  
-ATOM   2040  CA  GLY B  58     -12.351  18.737  -9.149  1.00 73.74           C  
-ANISOU 2040  CA  GLY B  58    10977   6394  10648   1066   -904    871       C  
-ATOM   2041  C   GLY B  58     -13.558  18.960 -10.048  1.00 71.13           C  
-ANISOU 2041  C   GLY B  58    10561   6077  10387   1359  -1075    975       C  
-ATOM   2042  O   GLY B  58     -14.225  20.002  -9.996  1.00 70.21           O  
-ANISOU 2042  O   GLY B  58    10538   5754  10383   1569  -1084    984       O  
-ATOM   2043  N   HIS B  59     -13.807  17.969 -10.900  1.00 63.82           N  
-ANISOU 2043  N   HIS B  59     9462   5400   9387   1360  -1217   1051       N  
-ATOM   2044  CA  HIS B  59     -15.155  17.598 -11.281  1.00 64.21           C  
-ANISOU 2044  CA  HIS B  59     9241   5602   9554   1637  -1355   1043       C  
-ATOM   2045  C   HIS B  59     -15.303  16.197 -10.691  1.00 56.47           C  
-ANISOU 2045  C   HIS B  59     7923   4897   8637   1584  -1306    906       C  
-ATOM   2046  O   HIS B  59     -14.332  15.629 -10.194  1.00 52.40           O  
-ANISOU 2046  O   HIS B  59     7432   4423   8057   1357  -1200    863       O  
-ATOM   2047  CB  HIS B  59     -15.352  17.575 -12.798  1.00 77.68           C  
-ANISOU 2047  CB  HIS B  59    11025   7380  11111   1653  -1565   1229       C  
-ATOM   2048  CG  HIS B  59     -16.765  17.295 -13.219  1.00 90.88           C  
-ANISOU 2048  CG  HIS B  59    12421   9210  12899   1929  -1723   1217       C  
-ATOM   2049  ND1 HIS B  59     -17.857  17.783 -12.528  1.00 96.89           N  
-ANISOU 2049  ND1 HIS B  59    13011   9922  13883   2212  -1692   1113       N  
-ATOM   2050  CD2 HIS B  59     -17.267  16.575 -14.250  1.00 94.74           C  
-ANISOU 2050  CD2 HIS B  59    12766   9924  13308   1953  -1906   1281       C  
-ATOM   2051  CE1 HIS B  59     -18.968  17.376 -13.118  1.00 99.83           C  
-ANISOU 2051  CE1 HIS B  59    13128  10492  14311   2392  -1854   1120       C  
-ATOM   2052  NE2 HIS B  59     -18.639  16.645 -14.166  1.00 98.76           N  
-ANISOU 2052  NE2 HIS B  59    13010  10520  13994   2236  -1992   1219       N  
-ATOM   2053  N   HIS B  60     -16.511  15.657 -10.716  1.00 53.49           N  
-ANISOU 2053  N   HIS B  60     7226   4706   8391   1780  -1375    836       N  
-ATOM   2054  CA  HIS B  60     -16.760  14.300 -10.267  1.00 50.20           C  
-ANISOU 2054  CA  HIS B  60     6477   4557   8039   1713  -1328    714       C  
-ATOM   2055  C   HIS B  60     -15.969  13.330 -11.146  1.00 37.34           C  
-ANISOU 2055  C   HIS B  60     4884   3078   6225   1482  -1419    816       C  
-ATOM   2056  O   HIS B  60     -15.945  13.479 -12.366  1.00 51.42           O  
-ANISOU 2056  O   HIS B  60     6797   4878   7864   1470  -1582    958       O  
-ATOM   2057  CB  HIS B  60     -18.261  14.020 -10.384  1.00 57.94           C  
-ANISOU 2057  CB  HIS B  60     7129   5717   9168   1936  -1404    639       C  
-ATOM   2058  CG  HIS B  60     -18.664  12.653  -9.936  1.00 61.38           C  
-ANISOU 2058  CG  HIS B  60     7218   6424   9679   1848  -1335    506       C  
-ATOM   2059  ND1 HIS B  60     -18.265  11.504 -10.586  1.00 60.61           N  
-ANISOU 2059  ND1 HIS B  60     7057   6504   9468   1657  -1410    551       N  
-ATOM   2060  CD2 HIS B  60     -19.448  12.247  -8.906  1.00 63.78           C  
-ANISOU 2060  CD2 HIS B  60     7233   6849  10151   1910  -1180    328       C  
-ATOM   2061  CE1 HIS B  60     -18.771  10.452  -9.969  1.00 56.28           C  
-ANISOU 2061  CE1 HIS B  60     6207   6153   9023   1600  -1306    412       C  
-ATOM   2062  NE2 HIS B  60     -19.491  10.875  -8.949  1.00 60.98           N  
-ANISOU 2062  NE2 HIS B  60     6659   6725   9784   1740  -1160    279       N  
-ATOM   2063  N  AILE B  61     -15.298  12.359 -10.545  0.36 34.25           N  
-ANISOU 2063  N  AILE B  61     4395   2794   5825   1303  -1306    748       N  
-ATOM   2064  N  BILE B  61     -15.345  12.333 -10.513  0.64 34.25           N  
-ANISOU 2064  N  BILE B  61     4380   2801   5834   1308  -1303    741       N  
-ATOM   2065  CA AILE B  61     -14.674  11.345 -11.373  0.36 32.60           C  
-ANISOU 2065  CA AILE B  61     4187   2751   5450   1114  -1386    831       C  
-ATOM   2066  CA BILE B  61     -14.572  11.299 -11.200  0.64 33.75           C  
-ANISOU 2066  CA BILE B  61     4327   2892   5604   1098  -1359    818       C  
-ATOM   2067  C  AILE B  61     -15.293   9.982 -11.122  0.36 35.42           C  
-ANISOU 2067  C  AILE B  61     4203   3359   5896   1099  -1360    717       C  
-ATOM   2068  C  BILE B  61     -15.264   9.942 -11.082  0.64 36.52           C  
-ANISOU 2068  C  BILE B  61     4338   3504   6033   1091  -1350    712       C  
-ATOM   2069  O  AILE B  61     -15.713   9.655 -10.008  0.36 35.83           O  
-ANISOU 2069  O  AILE B  61     4055   3465   6093   1130  -1193    567       O  
-ATOM   2070  O  BILE B  61     -15.688   9.559  -9.989  0.64 35.81           O  
-ANISOU 2070  O  BILE B  61     4043   3478   6085   1116  -1184    562       O  
-ATOM   2071  CB AILE B  61     -13.125  11.301 -11.253  0.36 37.56           C  
-ANISOU 2071  CB AILE B  61     5040   3364   5868    838  -1245    870       C  
-ATOM   2072  CB BILE B  61     -13.151  11.164 -10.589  0.64 35.54           C  
-ANISOU 2072  CB BILE B  61     4705   3128   5670    837  -1146    788       C  
-ATOM   2073  CG1AILE B  61     -12.668  10.151 -10.354  0.36 34.08           C  
-ANISOU 2073  CG1AILE B  61     4412   3131   5403    688  -1044    730       C  
-ATOM   2074  CG1BILE B  61     -12.318  12.416 -10.870  0.64 42.56           C  
-ANISOU 2074  CG1BILE B  61     5947   3776   6447    761  -1154    900       C  
-ATOM   2075  CG2AILE B  61     -12.566  12.663 -10.809  0.36 43.41           C  
-ANISOU 2075  CG2AILE B  61     6062   3829   6605    825  -1174    899       C  
-ATOM   2076  CG2BILE B  61     -12.431   9.945 -11.133  0.64 34.27           C  
-ANISOU 2076  CG2BILE B  61     4495   3203   5323    631  -1127    806       C  
-ATOM   2077  CD1AILE B  61     -11.172   9.915 -10.373  0.36 32.74           C  
-ANISOU 2077  CD1AILE B  61     4396   3030   5014    434   -928    753       C  
-ATOM   2078  CD1BILE B  61     -11.055  12.512 -10.028  0.64 41.25           C  
-ANISOU 2078  CD1BILE B  61     5886   3616   6172    526   -940    827       C  
-ATOM   2079  N   VAL B  62     -15.381   9.210 -12.193  1.00 35.18           N  
-ANISOU 2079  N   VAL B  62     4132   3491   5745   1027  -1502    775       N  
-ATOM   2080  CA  VAL B  62     -15.786   7.810 -12.115  1.00 29.59           C  
-ANISOU 2080  CA  VAL B  62     3159   3009   5073    947  -1474    675       C  
-ATOM   2081  C   VAL B  62     -14.521   7.015 -12.343  1.00 28.62           C  
-ANISOU 2081  C   VAL B  62     3180   2977   4719    702  -1369    697       C  
-ATOM   2082  O   VAL B  62     -13.870   7.164 -13.373  1.00 31.09           O  
-ANISOU 2082  O   VAL B  62     3693   3284   4837    621  -1472    814       O  
-ATOM   2083  CB  VAL B  62     -16.842   7.444 -13.171  1.00 31.59           C  
-ANISOU 2083  CB  VAL B  62     3279   3414   5311   1007  -1660    673       C  
-ATOM   2084  CG1 VAL B  62     -17.212   5.961 -13.061  1.00 36.97           C  
-ANISOU 2084  CG1 VAL B  62     3716   4301   6030    880  -1619    557       C  
-ATOM   2085  CG2 VAL B  62     -18.075   8.313 -12.988  1.00 36.27           C  
-ANISOU 2085  CG2 VAL B  62     3746   3970   6066   1239  -1706    630       C  
-ATOM   2086  N   ALA B  63     -14.144   6.198 -11.369  1.00 25.55           N  
-ANISOU 2086  N   ALA B  63     2700   2670   4340    592  -1157    587       N  
-ATOM   2087  CA  ALA B  63     -12.943   5.408 -11.498  1.00 24.20           C  
-ANISOU 2087  CA  ALA B  63     2638   2588   3967    403  -1057    593       C  
-ATOM   2088  C   ALA B  63     -13.362   4.038 -11.956  1.00 33.94           C  
-ANISOU 2088  C   ALA B  63     3732   3978   5184    340  -1095    537       C  
-ATOM   2089  O   ALA B  63     -14.202   3.389 -11.324  1.00 31.02           O  
-ANISOU 2089  O   ALA B  63     3163   3661   4963    360  -1034    436       O  
-ATOM   2090  CB  ALA B  63     -12.193   5.321 -10.194  1.00 25.49           C  
-ANISOU 2090  CB  ALA B  63     2820   2739   4124    337   -832    518       C  
-ATOM   2091  N   LEU B  64     -12.765   3.607 -13.064  1.00 26.55           N  
-ANISOU 2091  N   LEU B  64     2919   3113   4057    245  -1182    594       N  
-ATOM   2092  CA ALEU B  64     -13.133   2.355 -13.693  0.65 26.32           C  
-ANISOU 2092  CA ALEU B  64     2804   3211   3987    175  -1241    535       C  
-ATOM   2093  CA BLEU B  64     -13.114   2.344 -13.708  0.35 26.89           C  
-ANISOU 2093  CA BLEU B  64     2879   3284   4055    173  -1241    536       C  
-ATOM   2094  C   LEU B  64     -12.012   1.339 -13.486  1.00 25.73           C  
-ANISOU 2094  C   LEU B  64     2811   3199   3767     49  -1078    487       C  
-ATOM   2095  O   LEU B  64     -10.901   1.516 -13.981  1.00 26.95           O  
-ANISOU 2095  O   LEU B  64     3128   3374   3739    -13  -1052    539       O  
-ATOM   2096  CB ALEU B  64     -13.400   2.621 -15.180  0.65 30.41           C  
-ANISOU 2096  CB ALEU B  64     3409   3763   4381    185  -1480    622       C  
-ATOM   2097  CB BLEU B  64     -13.261   2.530 -15.217  0.35 30.53           C  
-ANISOU 2097  CB BLEU B  64     3441   3787   4372    167  -1467    621       C  
-ATOM   2098  CG ALEU B  64     -13.967   1.565 -16.114  0.65 33.03           C  
-ANISOU 2098  CG ALEU B  64     3672   4224   4654    119  -1615    564       C  
-ATOM   2099  CG BLEU B  64     -14.491   3.159 -15.850  0.35 32.84           C  
-ANISOU 2099  CG BLEU B  64     3645   4069   4765    303  -1715    669       C  
-ATOM   2100  CD1ALEU B  64     -15.052   0.782 -15.410  0.65 32.63           C  
-ANISOU 2100  CD1ALEU B  64     3358   4221   4819    121  -1579    432       C  
-ATOM   2101  CD1BLEU B  64     -14.638   2.639 -17.275  0.35 36.66           C  
-ANISOU 2101  CD1BLEU B  64     4200   4665   5066    236  -1910    694       C  
-ATOM   2102  CD2ALEU B  64     -14.532   2.249 -17.355  0.65 37.64           C  
-ANISOU 2102  CD2ALEU B  64     4320   4822   5158    190  -1894    667       C  
-ATOM   2103  CD2BLEU B  64     -15.725   2.859 -15.034  0.35 33.80           C  
-ANISOU 2103  CD2BLEU B  64     3468   4222   5152    384  -1700    553       C  
-ATOM   2104  N   CYS B  65     -12.308   0.275 -12.747  1.00 25.64           N  
-ANISOU 2104  N   CYS B  65     2687   3216   3837     14   -962    385       N  
-ATOM   2105  CA  CYS B  65     -11.306  -0.753 -12.474  1.00 27.57           C  
-ANISOU 2105  CA  CYS B  65     3017   3498   3961    -62   -819    339       C  
-ATOM   2106  C   CYS B  65     -11.305  -1.856 -13.534  1.00 29.12           C  
-ANISOU 2106  C   CYS B  65     3259   3760   4044   -138   -890    293       C  
-ATOM   2107  O   CYS B  65     -12.324  -2.518 -13.752  1.00 27.12           O  
-ANISOU 2107  O   CYS B  65     2906   3519   3879   -175   -955    229       O  
-ATOM   2108  CB  CYS B  65     -11.558  -1.383 -11.108  1.00 27.07           C  
-ANISOU 2108  CB  CYS B  65     2873   3400   4012    -62   -652    268       C  
-ATOM   2109  SG  CYS B  65     -10.352  -2.674 -10.721  1.00 27.87           S  
-ANISOU 2109  SG  CYS B  65     3101   3520   3967   -103   -505    227       S  
-ATOM   2110  N   VAL B  66     -10.174  -2.053 -14.209  1.00 27.16           N  
-ANISOU 2110  N   VAL B  66     3155   3563   3599   -172   -870    309       N  
-ATOM   2111  CA  VAL B  66     -10.106  -3.149 -15.169  1.00 24.80           C  
-ANISOU 2111  CA  VAL B  66     2925   3318   3182   -237   -911    240       C  
-ATOM   2112  C   VAL B  66      -9.673  -4.426 -14.458  1.00 24.80           C  
-ANISOU 2112  C   VAL B  66     2949   3283   3189   -242   -754    149       C  
-ATOM   2113  O   VAL B  66      -8.496  -4.580 -14.093  1.00 24.35           O  
-ANISOU 2113  O   VAL B  66     2961   3248   3042   -200   -634    149       O  
-ATOM   2114  CB  VAL B  66      -9.176  -2.856 -16.355  1.00 31.59           C  
-ANISOU 2114  CB  VAL B  66     3931   4260   3810   -271   -953    279       C  
-ATOM   2115  CG1 VAL B  66      -9.308  -3.966 -17.373  1.00 30.33           C  
-ANISOU 2115  CG1 VAL B  66     3844   4149   3531   -335  -1006    185       C  
-ATOM   2116  CG2 VAL B  66      -9.533  -1.516 -17.003  1.00 30.36           C  
-ANISOU 2116  CG2 VAL B  66     3807   4103   3625   -263  -1107    401       C  
-ATOM   2117  N   LEU B  67     -10.640  -5.326 -14.259  1.00 24.25           N  
-ANISOU 2117  N   LEU B  67     2824   3161   3229   -294   -760     73       N  
-ATOM   2118  CA  LEU B  67     -10.440  -6.588 -13.542  1.00 25.13           C  
-ANISOU 2118  CA  LEU B  67     2997   3190   3361   -308   -616      0       C  
-ATOM   2119  C   LEU B  67      -9.775  -7.612 -14.468  1.00 28.79           C  
-ANISOU 2119  C   LEU B  67     3618   3657   3663   -328   -614    -79       C  
-ATOM   2120  O   LEU B  67      -9.836  -7.452 -15.689  1.00 27.39           O  
-ANISOU 2120  O   LEU B  67     3475   3557   3377   -373   -734    -98       O  
-ATOM   2121  CB  LEU B  67     -11.789  -7.108 -13.036  1.00 21.10           C  
-ANISOU 2121  CB  LEU B  67     2378   2612   3025   -401   -610    -54       C  
-ATOM   2122  CG  LEU B  67     -12.481  -6.285 -11.945  1.00 26.60           C  
-ANISOU 2122  CG  LEU B  67     2913   3300   3893   -372   -561     -9       C  
-ATOM   2123  CD1 LEU B  67     -13.867  -6.835 -11.664  1.00 28.30           C  
-ANISOU 2123  CD1 LEU B  67     2986   3494   4275   -493   -551    -86       C  
-ATOM   2124  CD2 LEU B  67     -11.646  -6.258 -10.666  1.00 27.32           C  
-ANISOU 2124  CD2 LEU B  67     3079   3337   3964   -296   -389     33       C  
-ATOM   2125  N   LYS B  68      -9.128  -8.646 -13.920  1.00 24.05           N  
-ANISOU 2125  N   LYS B  68     3134   2973   3032   -281   -480   -127       N  
-ATOM   2126  CA  LYS B  68      -8.931  -8.835 -12.482  1.00 26.70           C  
-ANISOU 2126  CA  LYS B  68     3470   3225   3450   -216   -348    -88       C  
-ATOM   2127  C   LYS B  68      -7.671  -8.140 -12.014  1.00 24.04           C  
-ANISOU 2127  C   LYS B  68     3126   2976   3034    -87   -295    -25       C  
-ATOM   2128  O   LYS B  68      -7.582  -7.696 -10.870  1.00 25.15           O  
-ANISOU 2128  O   LYS B  68     3219   3103   3233    -43   -232     31       O  
-ATOM   2129  CB  LYS B  68      -8.774 -10.325 -12.170  1.00 25.18           C  
-ANISOU 2129  CB  LYS B  68     3448   2881   3239   -208   -251   -157       C  
-ATOM   2130  CG  LYS B  68      -9.941 -11.213 -12.531  1.00 27.53           C  
-ANISOU 2130  CG  LYS B  68     3782   3067   3612   -375   -275   -242       C  
-ATOM   2131  CD  LYS B  68      -9.768 -12.550 -11.808  1.00 32.88           C  
-ANISOU 2131  CD  LYS B  68     4664   3540   4290   -364   -142   -273       C  
-ATOM   2132  CE  LYS B  68     -10.414 -13.685 -12.535  1.00 33.59           C  
-ANISOU 2132  CE  LYS B  68     4882   3498   4382   -518   -159   -395       C  
-ATOM   2133  NZ  LYS B  68     -10.104 -14.982 -11.847  1.00 33.18           N  
-ANISOU 2133  NZ  LYS B  68     5090   3201   4314   -484    -24   -412       N  
-ATOM   2134  N   GLY B  69      -6.687  -8.069 -12.901  1.00 23.57           N  
-ANISOU 2134  N   GLY B  69     3109   3018   2827    -40   -313    -48       N  
-ATOM   2135  CA  GLY B  69      -5.360  -7.593 -12.546  1.00 26.89           C  
-ANISOU 2135  CA  GLY B  69     3507   3549   3162     64   -253    -19       C  
-ATOM   2136  C   GLY B  69      -5.253  -6.174 -12.010  1.00 27.06           C  
-ANISOU 2136  C   GLY B  69     3418   3643   3222     42   -268     69       C  
-ATOM   2137  O   GLY B  69      -4.309  -5.842 -11.281  1.00 30.11           O  
-ANISOU 2137  O   GLY B  69     3767   4099   3573    110   -209     87       O  
-ATOM   2138  N   GLY B  70      -6.201  -5.318 -12.366  1.00 24.85           N  
-ANISOU 2138  N   GLY B  70     3086   3344   3013    -46   -356    117       N  
-ATOM   2139  CA  GLY B  70      -6.100  -3.934 -11.936  1.00 22.35           C  
-ANISOU 2139  CA  GLY B  70     2703   3059   2731    -61   -369    193       C  
-ATOM   2140  C   GLY B  70      -6.595  -3.714 -10.516  1.00 23.35           C  
-ANISOU 2140  C   GLY B  70     2775   3105   2992    -30   -311    210       C  
-ATOM   2141  O   GLY B  70      -6.468  -2.605  -9.998  1.00 23.37           O  
-ANISOU 2141  O   GLY B  70     2740   3115   3026    -34   -305    253       O  
-ATOM   2142  N   TYR B  71      -7.136  -4.751  -9.877  1.00 22.29           N  
-ANISOU 2142  N   TYR B  71     2659   2887   2922    -12   -255    173       N  
-ATOM   2143  CA  TYR B  71      -7.856  -4.541  -8.611  1.00 21.75           C  
-ANISOU 2143  CA  TYR B  71     2545   2745   2976    -12   -187    185       C  
-ATOM   2144  C   TYR B  71      -6.977  -3.974  -7.490  1.00 21.30           C  
-ANISOU 2144  C   TYR B  71     2496   2728   2868     45   -116    210       C  
-ATOM   2145  O   TYR B  71      -7.435  -3.155  -6.688  1.00 22.21           O  
-ANISOU 2145  O   TYR B  71     2563   2815   3060     35    -83    222       O  
-ATOM   2146  CB  TYR B  71      -8.620  -5.814  -8.159  1.00 25.98           C  
-ANISOU 2146  CB  TYR B  71     3125   3175   3571    -45   -118    146       C  
-ATOM   2147  CG  TYR B  71      -7.966  -6.603  -7.028  1.00 25.96           C  
-ANISOU 2147  CG  TYR B  71     3239   3125   3501     23     -6    156       C  
-ATOM   2148  CD1 TYR B  71      -8.144  -6.240  -5.699  1.00 25.04           C  
-ANISOU 2148  CD1 TYR B  71     3117   2986   3412     33     83    184       C  
-ATOM   2149  CD2 TYR B  71      -7.195  -7.729  -7.301  1.00 25.80           C  
-ANISOU 2149  CD2 TYR B  71     3351   3073   3378     91      5    135       C  
-ATOM   2150  CE1 TYR B  71      -7.545  -6.966  -4.671  1.00 26.76           C  
-ANISOU 2150  CE1 TYR B  71     3468   3162   3536    102    162    209       C  
-ATOM   2151  CE2 TYR B  71      -6.591  -8.454  -6.287  1.00 26.53           C  
-ANISOU 2151  CE2 TYR B  71     3570   3111   3400    188     80    160       C  
-ATOM   2152  CZ  TYR B  71      -6.765  -8.058  -4.975  1.00 27.36           C  
-ANISOU 2152  CZ  TYR B  71     3676   3204   3515    189    149    206       C  
-ATOM   2153  OH  TYR B  71      -6.176  -8.784  -3.958  1.00 27.76           O  
-ANISOU 2153  OH  TYR B  71     3878   3201   3467    291    202    246       O  
-ATOM   2154  N   LYS B  72      -5.730  -4.423  -7.397  1.00 20.45           N  
-ANISOU 2154  N   LYS B  72     2443   2695   2633    112    -94    201       N  
-ATOM   2155  CA  LYS B  72      -4.871  -3.954  -6.302  1.00 23.82           C  
-ANISOU 2155  CA  LYS B  72     2864   3188   3000    161    -51    212       C  
-ATOM   2156  C   LYS B  72      -4.443  -2.504  -6.523  1.00 23.97           C  
-ANISOU 2156  C   LYS B  72     2817   3284   3007     98    -88    225       C  
-ATOM   2157  O   LYS B  72      -4.584  -1.651  -5.639  1.00 21.95           O  
-ANISOU 2157  O   LYS B  72     2546   3007   2786     74    -61    229       O  
-ATOM   2158  CB  LYS B  72      -3.642  -4.849  -6.147  1.00 25.14           C  
-ANISOU 2158  CB  LYS B  72     3074   3438   3040    274    -40    191       C  
-ATOM   2159  CG  LYS B  72      -3.868  -6.050  -5.265  1.00 35.91           C  
-ANISOU 2159  CG  LYS B  72     4556   4694   4393    359     12    202       C  
-ATOM   2160  CD  LYS B  72      -4.199  -5.613  -3.859  1.00 41.63           C  
-ANISOU 2160  CD  LYS B  72     5302   5388   5128    344     64    232       C  
-ATOM   2161  CE  LYS B  72      -2.965  -5.140  -3.130  1.00 44.58           C  
-ANISOU 2161  CE  LYS B  72     5640   5913   5384    417     34    228       C  
-ATOM   2162  NZ  LYS B  72      -3.312  -4.725  -1.747  1.00 41.71           N  
-ANISOU 2162  NZ  LYS B  72     5325   5521   5003    393     85    246       N  
-ATOM   2163  N   PHE B  73      -3.918  -2.225  -7.708  1.00 20.94           N  
-ANISOU 2163  N   PHE B  73     2417   2977   2562     58   -138    228       N  
-ATOM   2164  CA  PHE B  73      -3.519  -0.870  -8.056  1.00 21.91           C  
-ANISOU 2164  CA  PHE B  73     2519   3146   2662    -34   -165    254       C  
-ATOM   2165  C   PHE B  73      -4.711   0.087  -7.903  1.00 24.16           C  
-ANISOU 2165  C   PHE B  73     2813   3286   3079    -69   -196    292       C  
-ATOM   2166  O   PHE B  73      -4.580   1.199  -7.380  1.00 20.07           O  
-ANISOU 2166  O   PHE B  73     2305   2736   2583   -112   -184    299       O  
-ATOM   2167  CB  PHE B  73      -2.976  -0.864  -9.490  1.00 20.29           C  
-ANISOU 2167  CB  PHE B  73     2325   3028   2355    -89   -199    261       C  
-ATOM   2168  CG  PHE B  73      -2.518   0.474  -9.968  1.00 22.61           C  
-ANISOU 2168  CG  PHE B  73     2638   3354   2601   -214   -213    303       C  
-ATOM   2169  CD1 PHE B  73      -1.641   1.248  -9.211  1.00 21.49           C  
-ANISOU 2169  CD1 PHE B  73     2460   3279   2425   -277   -166    283       C  
-ATOM   2170  CD2 PHE B  73      -2.942   0.953 -11.204  1.00 26.22           C  
-ANISOU 2170  CD2 PHE B  73     3168   3768   3027   -285   -279    364       C  
-ATOM   2171  CE1 PHE B  73      -1.206   2.491  -9.679  1.00 23.55           C  
-ANISOU 2171  CE1 PHE B  73     2768   3543   2637   -430   -165    321       C  
-ATOM   2172  CE2 PHE B  73      -2.505   2.190 -11.684  1.00 29.85           C  
-ANISOU 2172  CE2 PHE B  73     3694   4225   3422   -417   -284    422       C  
-ATOM   2173  CZ  PHE B  73      -1.633   2.955 -10.921  1.00 26.12           C  
-ANISOU 2173  CZ  PHE B  73     3195   3799   2930   -499   -217    399       C  
-ATOM   2174  N   PHE B  74      -5.883  -0.361  -8.330  1.00 20.86           N  
-ANISOU 2174  N   PHE B  74     2386   2782   2756    -46   -238    301       N  
-ATOM   2175  CA  PHE B  74      -7.098   0.445  -8.221  1.00 21.42           C  
-ANISOU 2175  CA  PHE B  74     2426   2739   2974    -40   -278    322       C  
-ATOM   2176  C   PHE B  74      -7.403   0.763  -6.749  1.00 20.98           C  
-ANISOU 2176  C   PHE B  74     2345   2628   2998     -8   -180    285       C  
-ATOM   2177  O   PHE B  74      -7.646   1.914  -6.392  1.00 22.73           O  
-ANISOU 2177  O   PHE B  74     2574   2779   3282     -6   -179    289       O  
-ATOM   2178  CB  PHE B  74      -8.249  -0.315  -8.894  1.00 19.99           C  
-ANISOU 2178  CB  PHE B  74     2195   2524   2877    -28   -343    313       C  
-ATOM   2179  CG  PHE B  74      -9.603   0.363  -8.788  1.00 23.04           C  
-ANISOU 2179  CG  PHE B  74     2493   2826   3437      8   -394    317       C  
-ATOM   2180  CD1 PHE B  74      -9.992   1.319  -9.718  1.00 25.15           C  
-ANISOU 2180  CD1 PHE B  74     2770   3058   3729     27   -531    376       C  
-ATOM   2181  CD2 PHE B  74     -10.497   0.003  -7.792  1.00 23.02           C  
-ANISOU 2181  CD2 PHE B  74     2396   2784   3564     30   -303    260       C  
-ATOM   2182  CE1 PHE B  74     -11.249   1.926  -9.639  1.00 26.94           C  
-ANISOU 2182  CE1 PHE B  74     2892   3216   4129    105   -597    372       C  
-ATOM   2183  CE2 PHE B  74     -11.745   0.609  -7.705  1.00 28.46           C  
-ANISOU 2183  CE2 PHE B  74     2961   3426   4427     80   -340    241       C  
-ATOM   2184  CZ  PHE B  74     -12.124   1.561  -8.640  1.00 26.71           C  
-ANISOU 2184  CZ  PHE B  74     2727   3174   4248    135   -497    294       C  
-ATOM   2185  N   ALA B  75      -7.380  -0.252  -5.889  1.00 18.66           N  
-ANISOU 2185  N   ALA B  75     2051   2353   2687     17    -93    249       N  
-ATOM   2186  CA  ALA B  75      -7.754  -0.042  -4.485  1.00 20.42           C  
-ANISOU 2186  CA  ALA B  75     2272   2533   2956     35     13    213       C  
-ATOM   2187  C   ALA B  75      -6.762   0.894  -3.801  1.00 21.43           C  
-ANISOU 2187  C   ALA B  75     2447   2700   2995     18     33    199       C  
-ATOM   2188  O   ALA B  75      -7.148   1.788  -3.048  1.00 22.43           O  
-ANISOU 2188  O   ALA B  75     2580   2763   3179     16     82    164       O  
-ATOM   2189  CB  ALA B  75      -7.847  -1.374  -3.745  1.00 22.27           C  
-ANISOU 2189  CB  ALA B  75     2545   2768   3149     51    101    200       C  
-ATOM   2190  N   ASP B  76      -5.484   0.694  -4.080  1.00 19.42           N  
-ANISOU 2190  N   ASP B  76     2217   2559   2604      1     -2    209       N  
-ATOM   2191  CA  ASP B  76      -4.433   1.493  -3.464  1.00 20.25           C  
-ANISOU 2191  CA  ASP B  76     2342   2739   2613    -46      7    179       C  
-ATOM   2192  C   ASP B  76      -4.418   2.909  -4.027  1.00 20.66           C  
-ANISOU 2192  C   ASP B  76     2416   2725   2708   -132    -31    190       C  
-ATOM   2193  O   ASP B  76      -4.289   3.870  -3.274  1.00 22.12           O  
-ANISOU 2193  O   ASP B  76     2643   2866   2896   -179      1    147       O  
-ATOM   2194  CB  ASP B  76      -3.064   0.832  -3.669  1.00 22.85           C  
-ANISOU 2194  CB  ASP B  76     2643   3242   2795    -35    -22    172       C  
-ATOM   2195  CG  ASP B  76      -2.902  -0.450  -2.875  1.00 27.00           C  
-ANISOU 2195  CG  ASP B  76     3193   3808   3257     76      6    167       C  
-ATOM   2196  OD1 ASP B  76      -3.637  -0.633  -1.895  1.00 27.83           O  
-ANISOU 2196  OD1 ASP B  76     3353   3828   3393    101     66    164       O  
-ATOM   2197  OD2 ASP B  76      -2.013  -1.272  -3.217  1.00 26.04           O  
-ANISOU 2197  OD2 ASP B  76     3047   3801   3046    144    -26    165       O  
-ATOM   2198  N   LEU B  77      -4.563   3.052  -5.347  1.00 18.48           N  
-ANISOU 2198  N   LEU B  77     2142   2427   2451   -157   -100    247       N  
-ATOM   2199  CA  LEU B  77      -4.565   4.378  -5.932  1.00 21.66           C  
-ANISOU 2199  CA  LEU B  77     2616   2736   2879   -236   -142    283       C  
-ATOM   2200  C   LEU B  77      -5.734   5.155  -5.369  1.00 25.16           C  
-ANISOU 2200  C   LEU B  77     3086   2998   3475   -171   -130    269       C  
-ATOM   2201  O   LEU B  77      -5.584   6.315  -4.969  1.00 23.70           O  
-ANISOU 2201  O   LEU B  77     2986   2712   3308   -220   -111    247       O  
-ATOM   2202  CB  LEU B  77      -4.649   4.330  -7.459  1.00 21.68           C  
-ANISOU 2202  CB  LEU B  77     2645   2740   2853   -263   -226    363       C  
-ATOM   2203  CG  LEU B  77      -4.758   5.682  -8.175  1.00 22.41           C  
-ANISOU 2203  CG  LEU B  77     2862   2698   2955   -336   -283    435       C  
-ATOM   2204  CD1 LEU B  77      -3.463   6.504  -8.086  1.00 21.36           C  
-ANISOU 2204  CD1 LEU B  77     2797   2615   2702   -509   -231    423       C  
-ATOM   2205  CD2 LEU B  77      -5.109   5.426  -9.628  1.00 24.93           C  
-ANISOU 2205  CD2 LEU B  77     3217   3021   3233   -331   -383    521       C  
-ATOM   2206  N   LEU B  78      -6.899   4.511  -5.310  1.00 21.83           N  
-ANISOU 2206  N   LEU B  78     2590   2536   3169    -66   -130    265       N  
-ATOM   2207  CA  LEU B  78      -8.068   5.179  -4.752  1.00 23.63           C  
-ANISOU 2207  CA  LEU B  78     2797   2622   3557     19   -102    229       C  
-ATOM   2208  C   LEU B  78      -7.880   5.503  -3.261  1.00 25.07           C  
-ANISOU 2208  C   LEU B  78     3010   2792   3724     11     25    136       C  
-ATOM   2209  O   LEU B  78      -8.361   6.527  -2.782  1.00 20.85           O  
-ANISOU 2209  O   LEU B  78     2519   2125   3278     49     60     88       O  
-ATOM   2210  CB  LEU B  78      -9.328   4.366  -4.990  1.00 21.32           C  
-ANISOU 2210  CB  LEU B  78     2376   2333   3392    104   -117    225       C  
-ATOM   2211  CG  LEU B  78     -10.127   4.820  -6.210  1.00 30.47           C  
-ANISOU 2211  CG  LEU B  78     3505   3422   4648    166   -264    289       C  
-ATOM   2212  CD1 LEU B  78      -9.311   4.792  -7.500  1.00 34.75           C  
-ANISOU 2212  CD1 LEU B  78     4141   4011   5050     90   -378    381       C  
-ATOM   2213  CD2 LEU B  78     -11.401   4.004  -6.366  1.00 30.01           C  
-ANISOU 2213  CD2 LEU B  78     3278   3400   4725    228   -283    257       C  
-ATOM   2214  N   ASP B  79      -7.161   4.659  -2.526  1.00 21.62           N  
-ANISOU 2214  N   ASP B  79     2569   2484   3161    -28     87    106       N  
-ATOM   2215  CA  ASP B  79      -6.915   4.977  -1.113  1.00 21.34           C  
-ANISOU 2215  CA  ASP B  79     2586   2454   3068    -46    189     19       C  
-ATOM   2216  C   ASP B  79      -6.052   6.225  -0.960  1.00 20.99           C  
-ANISOU 2216  C   ASP B  79     2640   2373   2962   -142    169    -18       C  
-ATOM   2217  O   ASP B  79      -6.298   7.047  -0.073  1.00 23.37           O  
-ANISOU 2217  O   ASP B  79     3011   2583   3287   -147    239   -104       O  
-ATOM   2218  CB  ASP B  79      -6.295   3.798  -0.359  1.00 22.86           C  
-ANISOU 2218  CB  ASP B  79     2777   2794   3115    -50    231     12       C  
-ATOM   2219  CG  ASP B  79      -7.333   2.823   0.130  1.00 29.48           C  
-ANISOU 2219  CG  ASP B  79     3579   3610   4010     12    321     10       C  
-ATOM   2220  OD1 ASP B  79      -8.521   3.200   0.148  1.00 35.30           O  
-ANISOU 2220  OD1 ASP B  79     4262   4247   4902     49    376    -21       O  
-ATOM   2221  OD2 ASP B  79      -6.962   1.690   0.498  1.00 32.04           O  
-ANISOU 2221  OD2 ASP B  79     3933   4014   4228     24    341     38       O  
-ATOM   2222  N   TYR B  80      -5.055   6.368  -1.825  1.00 22.27           N  
-ANISOU 2222  N   TYR B  80     2816   2605   3042   -235     88     34       N  
-ATOM   2223  CA  TYR B  80      -4.210   7.555  -1.794  1.00 21.32           C  
-ANISOU 2223  CA  TYR B  80     2791   2446   2862   -376     75      0       C  
-ATOM   2224  C   TYR B  80      -4.976   8.794  -2.223  1.00 22.64           C  
-ANISOU 2224  C   TYR B  80     3073   2367   3164   -359     61     18       C  
-ATOM   2225  O   TYR B  80      -4.756   9.861  -1.668  1.00 22.70           O  
-ANISOU 2225  O   TYR B  80     3200   2255   3168   -435     97    -52       O  
-ATOM   2226  CB  TYR B  80      -2.948   7.385  -2.652  1.00 21.64           C  
-ANISOU 2226  CB  TYR B  80     2798   2645   2777   -504     17     45       C  
-ATOM   2227  CG  TYR B  80      -1.849   6.591  -1.974  1.00 23.05           C  
-ANISOU 2227  CG  TYR B  80     2882   3068   2809   -532     23    -12       C  
-ATOM   2228  CD1 TYR B  80      -1.185   7.099  -0.865  1.00 24.88           C  
-ANISOU 2228  CD1 TYR B  80     3137   3363   2952   -622     44   -115       C  
-ATOM   2229  CD2 TYR B  80      -1.476   5.330  -2.449  1.00 26.43           C  
-ANISOU 2229  CD2 TYR B  80     3202   3660   3179   -455     -6     30       C  
-ATOM   2230  CE1 TYR B  80      -0.173   6.378  -0.236  1.00 26.33           C  
-ANISOU 2230  CE1 TYR B  80     3222   3790   2993   -623     16   -163       C  
-ATOM   2231  CE2 TYR B  80      -0.462   4.606  -1.831  1.00 23.48           C  
-ANISOU 2231  CE2 TYR B  80     2742   3503   2677   -436    -21    -17       C  
-ATOM   2232  CZ  TYR B  80       0.184   5.138  -0.730  1.00 26.41           C  
-ANISOU 2232  CZ  TYR B  80     3120   3955   2961   -514    -21   -108       C  
-ATOM   2233  OH  TYR B  80       1.193   4.432  -0.110  1.00 28.03           O  
-ANISOU 2233  OH  TYR B  80     3226   4393   3030   -472    -67   -152       O  
-ATOM   2234  N   ILE B  81      -5.867   8.660  -3.208  1.00 20.01           N  
-ANISOU 2234  N   ILE B  81     2713   1948   2943   -254     -2    108       N  
-ATOM   2235  CA  ILE B  81      -6.729   9.788  -3.592  1.00 20.74           C  
-ANISOU 2235  CA  ILE B  81     2910   1795   3176   -176    -40    135       C  
-ATOM   2236  C   ILE B  81      -7.675  10.163  -2.441  1.00 21.60           C  
-ANISOU 2236  C   ILE B  81     3007   1788   3412    -48     56     20       C  
-ATOM   2237  O   ILE B  81      -7.869  11.332  -2.138  1.00 25.43           O  
-ANISOU 2237  O   ILE B  81     3629   2071   3961    -30     78    -30       O  
-ATOM   2238  CB  ILE B  81      -7.545   9.495  -4.876  1.00 29.93           C  
-ANISOU 2238  CB  ILE B  81     4024   2924   4422    -66   -159    253       C  
-ATOM   2239  CG1 ILE B  81      -6.620   9.433  -6.091  1.00 24.83           C  
-ANISOU 2239  CG1 ILE B  81     3449   2351   3634   -206   -239    362       C  
-ATOM   2240  CG2 ILE B  81      -8.595  10.585  -5.111  1.00 31.86           C  
-ANISOU 2240  CG2 ILE B  81     4352   2920   4832     82   -216    275       C  
-ATOM   2241  CD1 ILE B  81      -7.252   8.740  -7.307  1.00 27.18           C  
-ANISOU 2241  CD1 ILE B  81     3679   2699   3950   -123   -356    461       C  
-ATOM   2242  N   LYS B  82      -8.279   9.173  -1.805  1.00 22.02           N  
-ANISOU 2242  N   LYS B  82     2911   1958   3496     36    126    -29       N  
-ATOM   2243  CA  LYS B  82      -9.116   9.468  -0.641  1.00 25.34           C  
-ANISOU 2243  CA  LYS B  82     3313   2305   4010    133    254   -155       C  
-ATOM   2244  C   LYS B  82      -8.351  10.189   0.472  1.00 27.29           C  
-ANISOU 2244  C   LYS B  82     3707   2519   4144     27    343   -271       C  
-ATOM   2245  O   LYS B  82      -8.888  11.083   1.104  1.00 26.17           O  
-ANISOU 2245  O   LYS B  82     3643   2217   4085     93    422   -375       O  
-ATOM   2246  CB  LYS B  82      -9.771   8.183  -0.132  1.00 27.94           C  
-ANISOU 2246  CB  LYS B  82     3478   2785   4354    186    338   -179       C  
-ATOM   2247  CG  LYS B  82     -10.827   7.667  -1.092  1.00 30.53           C  
-ANISOU 2247  CG  LYS B  82     3648   3117   4836    294    263   -111       C  
-ATOM   2248  CD  LYS B  82     -10.979   6.154  -0.974  1.00 38.55           C  
-ANISOU 2248  CD  LYS B  82     4545   4299   5802    255    307    -92       C  
-ATOM   2249  CE  LYS B  82     -11.103   5.727   0.469  1.00 43.21           C  
-ANISOU 2249  CE  LYS B  82     5143   4945   6329    229    490   -187       C  
-ATOM   2250  NZ  LYS B  82     -11.112   4.241   0.600  1.00 48.43           N  
-ANISOU 2250  NZ  LYS B  82     5755   5731   6915    174    533   -147       N  
-ATOM   2251  N   ALA B  83      -7.085   9.833   0.681  1.00 26.25           N  
-ANISOU 2251  N   ALA B  83     3609   2541   3823   -134    323   -264       N  
-ATOM   2252  CA  ALA B  83      -6.266  10.508   1.698  1.00 23.76           C  
-ANISOU 2252  CA  ALA B  83     3422   2226   3380   -265    378   -384       C  
-ATOM   2253  C   ALA B  83      -6.124  11.989   1.392  1.00 26.99           C  
-ANISOU 2253  C   ALA B  83     4009   2397   3848   -330    356   -416       C  
-ATOM   2254  O   ALA B  83      -6.163  12.833   2.290  1.00 27.31           O  
-ANISOU 2254  O   ALA B  83     4182   2315   3880   -360    436   -553       O  
-ATOM   2255  CB  ALA B  83      -4.893   9.858   1.802  1.00 26.59           C  
-ANISOU 2255  CB  ALA B  83     3742   2825   3538   -413    322   -366       C  
-ATOM   2256  N   LEU B  84      -5.928  12.305   0.115  1.00 25.37           N  
-ANISOU 2256  N   LEU B  84     3839   2115   3685   -365    253   -289       N  
-ATOM   2257  CA  LEU B  84      -5.836  13.697  -0.313  1.00 27.46           C  
-ANISOU 2257  CA  LEU B  84     4319   2111   4004   -429    226   -285       C  
-ATOM   2258  C   LEU B  84      -7.177  14.406  -0.115  1.00 30.97           C  
-ANISOU 2258  C   LEU B  84     4828   2291   4648   -199    263   -330       C  
-ATOM   2259  O   LEU B  84      -7.222  15.580   0.288  1.00 31.89           O  
-ANISOU 2259  O   LEU B  84     5150   2162   4807   -215    307   -420       O  
-ATOM   2260  CB  LEU B  84      -5.437  13.769  -1.795  1.00 30.26           C  
-ANISOU 2260  CB  LEU B  84     4710   2448   4339   -504    111   -113       C  
-ATOM   2261  CG  LEU B  84      -4.070  13.251  -2.212  1.00 29.18           C  
-ANISOU 2261  CG  LEU B  84     4510   2557   4021   -732     83    -72       C  
-ATOM   2262  CD1 LEU B  84      -3.924  13.214  -3.748  1.00 28.38           C  
-ANISOU 2262  CD1 LEU B  84     4439   2442   3901   -772     -8    100       C  
-ATOM   2263  CD2 LEU B  84      -2.981  14.134  -1.600  1.00 27.27           C  
-ANISOU 2263  CD2 LEU B  84     4400   2292   3668   -990    132   -182       C  
-ATOM   2264  N   ASN B  85      -8.267  13.704  -0.421  1.00 28.81           N  
-ANISOU 2264  N   ASN B  85     4376   2068   4503     14    245   -280       N  
-ATOM   2265  CA  ASN B  85      -9.606  14.296  -0.314  1.00 31.84           C  
-ANISOU 2265  CA  ASN B  85     4754   2246   5099    266    270   -329       C  
-ATOM   2266  C   ASN B  85      -9.998  14.693   1.104  1.00 34.97           C  
-ANISOU 2266  C   ASN B  85     5182   2581   5523    323    443   -533       C  
-ATOM   2267  O   ASN B  85     -10.838  15.568   1.291  1.00 38.52           O  
-ANISOU 2267  O   ASN B  85     5699   2803   6133    507    483   -612       O  
-ATOM   2268  CB  ASN B  85     -10.672  13.344  -0.872  1.00 33.44           C  
-ANISOU 2268  CB  ASN B  85     4703   2577   5427    449    218   -257       C  
-ATOM   2269  CG  ASN B  85     -10.721  13.341  -2.374  1.00 40.29           C  
-ANISOU 2269  CG  ASN B  85     5581   3408   6320    478     30    -74       C  
-ATOM   2270  OD1 ASN B  85     -10.331  14.308  -3.017  1.00 45.08           O  
-ANISOU 2270  OD1 ASN B  85     6406   3813   6909    439    -55      5       O  
-ATOM   2271  ND2 ASN B  85     -11.219  12.257  -2.945  1.00 47.93           N  
-ANISOU 2271  ND2 ASN B  85     6335   4559   7316    534    -33     -6       N  
-ATOM   2272  N   ARG B  86      -9.408  14.047   2.104  1.00 33.64           N  
-ANISOU 2272  N   ARG B  86     4973   2618   5192    184    544   -623       N  
-ATOM   2273  CA  ARG B  86      -9.775  14.360   3.491  1.00 33.66           C  
-ANISOU 2273  CA  ARG B  86     5021   2587   5179    222    720   -823       C  
-ATOM   2274  C   ARG B  86      -8.716  15.173   4.242  1.00 38.28           C  
-ANISOU 2274  C   ARG B  86     5843   3103   5599     15    755   -945       C  
-ATOM   2275  O   ARG B  86      -8.973  15.677   5.339  1.00 37.44           O  
-ANISOU 2275  O   ARG B  86     5836   2921   5469     36    894  -1130       O  
-ATOM   2276  CB  ARG B  86     -10.152  13.088   4.266  1.00 31.86           C  
-ANISOU 2276  CB  ARG B  86     4603   2620   4883    243    831   -857       C  
-ATOM   2277  CG  ARG B  86      -8.990  12.147   4.509  1.00 27.44           C  
-ANISOU 2277  CG  ARG B  86     4031   2307   4087     47    787   -799       C  
-ATOM   2278  CD  ARG B  86      -9.410  10.852   5.184  1.00 34.31           C  
-ANISOU 2278  CD  ARG B  86     4760   3389   4888     78    888   -799       C  
-ATOM   2279  NE  ARG B  86      -8.234   9.994   5.310  1.00 33.13           N  
-ANISOU 2279  NE  ARG B  86     4619   3448   4520    -68    810   -727       N  
-ATOM   2280  CZ  ARG B  86      -8.000   8.897   4.598  1.00 31.53           C  
-ANISOU 2280  CZ  ARG B  86     4299   3383   4298    -69    722   -585       C  
-ATOM   2281  NH1 ARG B  86      -8.884   8.457   3.704  1.00 27.51           N  
-ANISOU 2281  NH1 ARG B  86     3652   2839   3960     38    698   -499       N  
-ATOM   2282  NH2 ARG B  86      -6.868   8.232   4.792  1.00 29.51           N  
-ANISOU 2282  NH2 ARG B  86     4059   3306   3846   -171    651   -542       N  
-ATOM   2283  N   ASN B  87      -7.539  15.330   3.638  1.00 37.91           N  
-ANISOU 2283  N   ASN B  87     5881   3087   5435   -197    636   -857       N  
-ATOM   2284  CA  ASN B  87      -6.449  16.067   4.286  1.00 42.03           C  
-ANISOU 2284  CA  ASN B  87     6596   3576   5795   -440    653   -979       C  
-ATOM   2285  C   ASN B  87      -6.007  17.343   3.570  1.00 47.68           C  
-ANISOU 2285  C   ASN B  87     7553   4004   6560   -563    590   -954       C  
-ATOM   2286  O   ASN B  87      -5.392  18.224   4.185  1.00 51.99           O  
-ANISOU 2286  O   ASN B  87     8303   4430   7020   -748    631  -1097       O  
-ATOM   2287  CB  ASN B  87      -5.240  15.149   4.505  1.00 43.55           C  
-ANISOU 2287  CB  ASN B  87     6672   4108   5766   -643    593   -949       C  
-ATOM   2288  CG  ASN B  87      -5.455  14.164   5.644  1.00 45.14           C  
-ANISOU 2288  CG  ASN B  87     6759   4541   5851   -578    676  -1024       C  
-ATOM   2289  OD1 ASN B  87      -5.824  14.557   6.755  1.00 44.50           O  
-ANISOU 2289  OD1 ASN B  87     6780   4400   5727   -554    796  -1192       O  
-ATOM   2290  ND2 ASN B  87      -5.234  12.880   5.369  1.00 42.56           N  
-ANISOU 2290  ND2 ASN B  87     6246   4464   5460   -549    620   -901       N  
-ATOM   2291  N   SER B  88      -6.316  17.458   2.283  1.00 76.44           N  
-ANISOU 2291  N   SER B  88    11509   5930  11604  -1609  -2172  -1899       N  
-ATOM   2292  CA  SER B  88      -5.822  18.607   1.522  1.00 78.38           C  
-ANISOU 2292  CA  SER B  88    11796   5840  12144  -1934  -2039  -1787       C  
-ATOM   2293  C   SER B  88      -6.876  19.661   1.182  1.00 80.01           C  
-ANISOU 2293  C   SER B  88    12394   5554  12452  -1702  -1840  -1705       C  
-ATOM   2294  O   SER B  88      -7.960  19.706   1.770  1.00 74.01           O  
-ANISOU 2294  O   SER B  88    11853   4714  11554  -1290  -1814  -1852       O  
-ATOM   2295  CB  SER B  88      -5.093  18.161   0.247  1.00 73.22           C  
-ANISOU 2295  CB  SER B  88    10793   5364  11663  -2215  -1950  -1438       C  
-ATOM   2296  OG  SER B  88      -6.008  17.733  -0.743  1.00 68.57           O  
-ANISOU 2296  OG  SER B  88    10235   4734  11084  -1950  -1787  -1068       O  
-ATOM   2297  N   ASP B  89      -6.524  20.496   0.210  1.00 88.39           N  
-ANISOU 2297  N   ASP B  89    13534   6311  13739  -1960  -1688  -1477       N  
-ATOM   2298  CA  ASP B  89      -7.279  21.691  -0.137  1.00 96.01           C  
-ANISOU 2298  CA  ASP B  89    14907   6750  14824  -1780  -1539  -1407       C  
-ATOM   2299  C   ASP B  89      -8.150  21.493  -1.375  1.00 93.13           C  
-ANISOU 2299  C   ASP B  89    14583   6326  14477  -1475  -1397   -974       C  
-ATOM   2300  O   ASP B  89      -8.626  22.462  -1.965  1.00 95.80           O  
-ANISOU 2300  O   ASP B  89    15232   6245  14921  -1343  -1287   -820       O  
-ATOM   2301  CB  ASP B  89      -6.302  22.840  -0.388  1.00104.94           C  
-ANISOU 2301  CB  ASP B  89    16176   7522  16176  -2280  -1456  -1443       C  
-ATOM   2302  CG  ASP B  89      -5.189  22.456  -1.353  1.00108.47           C  
-ANISOU 2302  CG  ASP B  89    16293   8197  16724  -2767  -1357  -1189       C  
-ATOM   2303  OD1 ASP B  89      -4.822  23.288  -2.212  1.00113.81           O  
-ANISOU 2303  OD1 ASP B  89    17119   8538  17586  -3054  -1159   -986       O  
-ATOM   2304  OD2 ASP B  89      -4.683  21.316  -1.253  1.00107.22           O  
-ANISOU 2304  OD2 ASP B  89    15719   8558  16462  -2844  -1468  -1201       O  
-ATOM   2305  N   ARG B  90      -8.351  20.241  -1.772  1.00 86.89           N  
-ANISOU 2305  N   ARG B  90    13485   5953  13577  -1349  -1419   -786       N  
-ATOM   2306  CA  ARG B  90      -9.145  19.939  -2.960  1.00 83.80           C  
-ANISOU 2306  CA  ARG B  90    13085   5585  13171  -1069  -1312   -396       C  
-ATOM   2307  C   ARG B  90      -9.911  18.644  -2.769  1.00 74.51           C  
-ANISOU 2307  C   ARG B  90    11654   4802  11855   -732  -1371   -404       C  
-ATOM   2308  O   ARG B  90      -9.550  17.826  -1.924  1.00 71.68           O  
-ANISOU 2308  O   ARG B  90    11090   4764  11382   -812  -1457   -617       O  
-ATOM   2309  CB  ARG B  90      -8.252  19.853  -4.188  1.00 86.14           C  
-ANISOU 2309  CB  ARG B  90    13256   5949  13525  -1462  -1191    -37       C  
-ATOM   2310  N   SER B  91     -10.961  18.451  -3.559  1.00 72.81           N  
-ANISOU 2310  N   SER B  91    11440   4608  11614   -351  -1310   -177       N  
-ATOM   2311  CA  SER B  91     -11.794  17.260  -3.419  1.00 71.20           C  
-ANISOU 2311  CA  SER B  91    10921   4907  11227    -41  -1256   -197       C  
-ATOM   2312  C   SER B  91     -12.144  16.563  -4.730  1.00 73.71           C  
-ANISOU 2312  C   SER B  91    11026   5494  11488     58  -1186    174       C  
-ATOM   2313  O   SER B  91     -12.137  17.174  -5.802  1.00 79.00           O  
-ANISOU 2313  O   SER B  91    11884   5885  12249     59  -1200    462       O  
-ATOM   2314  CB  SER B  91     -13.090  17.600  -2.678  1.00 70.64           C  
-ANISOU 2314  CB  SER B  91    10948   4776  11116    436  -1229   -487       C  
-ATOM   2315  OG  SER B  91     -13.008  17.240  -1.309  1.00 68.34           O  
-ANISOU 2315  OG  SER B  91    10618   4691  10659    398  -1210   -848       O  
-ATOM   2316  N   ILE B  92     -12.448  15.272  -4.619  1.00 69.14           N  
-ANISOU 2316  N   ILE B  92    10106   5437  10727    130  -1116    163       N  
-ATOM   2317  CA  ILE B  92     -13.169  14.540  -5.654  1.00 63.79           C  
-ANISOU 2317  CA  ILE B  92     9216   5054   9965    326  -1062    394       C  
-ATOM   2318  C   ILE B  92     -14.639  15.057  -5.606  1.00 61.66           C  
-ANISOU 2318  C   ILE B  92     8990   4703   9736    810  -1072    269       C  
-ATOM   2319  O   ILE B  92     -14.818  16.262  -5.753  1.00 61.62           O  
-ANISOU 2319  O   ILE B  92     9295   4240   9878    977  -1160    274       O  
-ATOM   2320  CB  ILE B  92     -13.008  13.068  -5.441  1.00 52.29           C  
-ANISOU 2320  CB  ILE B  92     7451   4090   8326    217   -993    372       C  
-ATOM   2321  N   PRO B  93     -15.698  14.232  -5.385  1.00 54.91           N  
-ANISOU 2321  N   PRO B  93     7836   4257   8769   1041   -985    129       N  
-ATOM   2322  CA  PRO B  93     -16.179  12.865  -5.126  1.00 52.30           C  
-ANISOU 2322  CA  PRO B  93     7169   4436   8265    995   -853     49       C  
-ATOM   2323  C   PRO B  93     -15.846  11.910  -6.246  1.00 43.54           C  
-ANISOU 2323  C   PRO B  93     5889   3575   7078    839   -870    333       C  
-ATOM   2324  O   PRO B  93     -15.618  12.332  -7.383  1.00 40.69           O  
-ANISOU 2324  O   PRO B  93     5613   3075   6774    872   -969    590       O  
-ATOM   2325  CB  PRO B  93     -17.705  13.029  -5.069  1.00 56.39           C  
-ANISOU 2325  CB  PRO B  93     7485   5124   8818   1400   -799   -156       C  
-ATOM   2326  CG  PRO B  93     -17.974  14.249  -5.836  1.00 61.76           C  
-ANISOU 2326  CG  PRO B  93     8361   5434   9672   1724   -979    -48       C  
-ATOM   2327  CD  PRO B  93     -16.850  15.150  -5.444  1.00 60.64           C  
-ANISOU 2327  CD  PRO B  93     8631   4798   9613   1510  -1041     -7       C  
-ATOM   2328  N   MET B  94     -15.793  10.635  -5.897  1.00 37.28           N  
-ANISOU 2328  N   MET B  94     4919   3119   6129    665   -768    283       N  
-ATOM   2329  CA  MET B  94     -15.562   9.588  -6.853  1.00 38.58           C  
-ANISOU 2329  CA  MET B  94     4927   3529   6203    542   -774    480       C  
-ATOM   2330  C   MET B  94     -16.686   8.584  -6.746  1.00 37.40           C  
-ANISOU 2330  C   MET B  94     4532   3725   5955    592   -661    346       C  
-ATOM   2331  O   MET B  94     -17.156   8.290  -5.647  1.00 34.86           O  
-ANISOU 2331  O   MET B  94     4192   3495   5558    556   -519    128       O  
-ATOM   2332  CB  MET B  94     -14.264   8.860  -6.530  1.00 36.37           C  
-ANISOU 2332  CB  MET B  94     4706   3281   5834    253   -778    533       C  
-ATOM   2333  CG  MET B  94     -13.017   9.706  -6.600  1.00 41.37           C  
-ANISOU 2333  CG  MET B  94     5489   3654   6577     98   -866    620       C  
-ATOM   2334  SD  MET B  94     -11.600   8.602  -6.514  1.00 49.54           S  
-ANISOU 2334  SD  MET B  94     6428   4882   7513   -151   -903    653       S  
-ATOM   2335  CE  MET B  94     -12.210   7.329  -7.566  1.00 46.48           C  
-ANISOU 2335  CE  MET B  94     5873   4790   6995    -70   -838    780       C  
-ATOM   2336  N   THR B  95     -17.112   8.060  -7.887  1.00 33.85           N  
-ANISOU 2336  N   THR B  95     3906   3473   5482    639   -710    464       N  
-ATOM   2337  CA  THR B  95     -17.875   6.816  -7.904  1.00 33.18           C  
-ANISOU 2337  CA  THR B  95     3595   3717   5294    536   -605    353       C  
-ATOM   2338  C   THR B  95     -17.010   5.760  -8.575  1.00 30.74           C  
-ANISOU 2338  C   THR B  95     3342   3469   4869    329   -640    521       C  
-ATOM   2339  O   THR B  95     -15.996   6.087  -9.205  1.00 29.98           O  
-ANISOU 2339  O   THR B  95     3368   3241   4781    315   -735    712       O  
-ATOM   2340  CB  THR B  95     -19.209   6.968  -8.627  1.00 35.48           C  
-ANISOU 2340  CB  THR B  95     3584   4243   5654    768   -661    255       C  
-ATOM   2341  OG1 THR B  95     -18.991   7.550  -9.918  1.00 36.06           O  
-ANISOU 2341  OG1 THR B  95     3717   4235   5750    958   -877    478       O  
-ATOM   2342  CG2 THR B  95     -20.138   7.872  -7.822  1.00 38.55           C  
-ANISOU 2342  CG2 THR B  95     3858   4627   6161   1018   -597      6       C  
-ATOM   2343  N   VAL B  96     -17.381   4.493  -8.439  1.00 30.10           N  
-ANISOU 2343  N   VAL B  96     3185   3575   4677    155   -543    434       N  
-ATOM   2344  CA  VAL B  96     -16.539   3.429  -8.981  1.00 30.25           C  
-ANISOU 2344  CA  VAL B  96     3301   3607   4584      6   -583    548       C  
-ATOM   2345  C   VAL B  96     -17.349   2.445  -9.801  1.00 33.35           C  
-ANISOU 2345  C   VAL B  96     3529   4225   4919    -68   -579    482       C  
-ATOM   2346  O   VAL B  96     -18.552   2.264  -9.580  1.00 32.66           O  
-ANISOU 2346  O   VAL B  96     3241   4308   4860   -114   -493    308       O  
-ATOM   2347  CB  VAL B  96     -15.783   2.666  -7.867  1.00 33.94           C  
-ANISOU 2347  CB  VAL B  96     4008   3951   4936   -159   -516    519       C  
-ATOM   2348  CG1 VAL B  96     -15.032   3.633  -6.969  1.00 38.04           C  
-ANISOU 2348  CG1 VAL B  96     4667   4285   5500   -105   -554    521       C  
-ATOM   2349  CG2 VAL B  96     -16.742   1.847  -7.039  1.00 34.22           C  
-ANISOU 2349  CG2 VAL B  96     4074   4062   4867   -332   -335    368       C  
-ATOM   2350  N   ASP B  97     -16.698   1.821 -10.773  1.00 29.65           N  
-ANISOU 2350  N   ASP B  97     3113   3782   4369    -89   -667    583       N  
-ATOM   2351  CA  ASP B  97     -17.294   0.668 -11.429  1.00 32.38           C  
-ANISOU 2351  CA  ASP B  97     3380   4290   4632   -213   -672    480       C  
-ATOM   2352  C   ASP B  97     -16.157  -0.256 -11.811  1.00 27.90           C  
-ANISOU 2352  C   ASP B  97     3022   3626   3951   -261   -705    548       C  
-ATOM   2353  O   ASP B  97     -14.986   0.115 -11.720  1.00 26.71           O  
-ANISOU 2353  O   ASP B  97     2979   3365   3803   -175   -733    669       O  
-ATOM   2354  CB  ASP B  97     -18.119   1.074 -12.657  1.00 37.82           C  
-ANISOU 2354  CB  ASP B  97     3825   5215   5330    -64   -814    459       C  
-ATOM   2355  CG  ASP B  97     -19.132  -0.010 -13.085  1.00 46.45           C  
-ANISOU 2355  CG  ASP B  97     4744   6526   6380   -244   -821    244       C  
-ATOM   2356  OD1 ASP B  97     -19.326  -1.018 -12.360  1.00 41.18           O  
-ANISOU 2356  OD1 ASP B  97     4162   5790   5695   -526   -668    119       O  
-ATOM   2357  OD2 ASP B  97     -19.743   0.163 -14.161  1.00 54.75           O  
-ANISOU 2357  OD2 ASP B  97     5598   7805   7397   -116   -995    197       O  
-ATOM   2358  N   PHE B  98     -16.508  -1.460 -12.226  1.00 28.14           N  
-ANISOU 2358  N   PHE B  98     3092   3703   3895   -400   -702    432       N  
-ATOM   2359  CA  PHE B  98     -15.523  -2.495 -12.452  1.00 27.71           C  
-ANISOU 2359  CA  PHE B  98     3274   3519   3736   -407   -731    437       C  
-ATOM   2360  C   PHE B  98     -15.895  -3.132 -13.765  1.00 29.12           C  
-ANISOU 2360  C   PHE B  98     3382   3857   3824   -419   -812    336       C  
-ATOM   2361  O   PHE B  98     -17.054  -3.478 -13.982  1.00 30.80           O  
-ANISOU 2361  O   PHE B  98     3466   4190   4047   -579   -814    187       O  
-ATOM   2362  CB  PHE B  98     -15.606  -3.549 -11.345  1.00 28.40           C  
-ANISOU 2362  CB  PHE B  98     3646   3372   3773   -599   -641    365       C  
-ATOM   2363  CG  PHE B  98     -15.301  -3.018  -9.981  1.00 27.81           C  
-ANISOU 2363  CG  PHE B  98     3694   3157   3715   -593   -575    439       C  
-ATOM   2364  CD1 PHE B  98     -16.298  -2.418  -9.211  1.00 28.51           C  
-ANISOU 2364  CD1 PHE B  98     3666   3314   3854   -716   -437    389       C  
-ATOM   2365  CD2 PHE B  98     -14.019  -3.120  -9.460  1.00 28.86           C  
-ANISOU 2365  CD2 PHE B  98     4037   3126   3803   -441   -665    518       C  
-ATOM   2366  CE1 PHE B  98     -16.015  -1.912  -7.939  1.00 29.54           C  
-ANISOU 2366  CE1 PHE B  98     3946   3325   3953   -702   -375    427       C  
-ATOM   2367  CE2 PHE B  98     -13.720  -2.625  -8.186  1.00 30.00           C  
-ANISOU 2367  CE2 PHE B  98     4314   3159   3926   -428   -650    558       C  
-ATOM   2368  CZ  PHE B  98     -14.728  -2.021  -7.423  1.00 30.52           C  
-ANISOU 2368  CZ  PHE B  98     4322   3269   4006   -568   -497    517       C  
-ATOM   2369  N   ILE B  99     -14.928  -3.266 -14.658  1.00 28.72           N  
-ANISOU 2369  N   ILE B  99     3385   3849   3676   -259   -873    384       N  
-ATOM   2370  CA  ILE B  99     -15.215  -3.954 -15.898  1.00 30.32           C  
-ANISOU 2370  CA  ILE B  99     3578   4202   3738   -259   -952    254       C  
-ATOM   2371  C   ILE B  99     -14.218  -5.072 -16.098  1.00 30.79           C  
-ANISOU 2371  C   ILE B  99     3881   4116   3703   -192   -949    161       C  
-ATOM   2372  O   ILE B  99     -13.087  -5.038 -15.602  1.00 30.68           O  
-ANISOU 2372  O   ILE B  99     3952   3985   3721    -55   -917    235       O  
-ATOM   2373  CB  ILE B  99     -15.244  -3.001 -17.132  1.00 43.70           C  
-ANISOU 2373  CB  ILE B  99     5109   6171   5325    -90  -1033    364       C  
-ATOM   2374  CG1 ILE B  99     -14.003  -2.129 -17.173  1.00 47.41           C  
-ANISOU 2374  CG1 ILE B  99     5598   6623   5793     54   -956    578       C  
-ATOM   2375  CG2 ILE B  99     -16.489  -2.123 -17.137  1.00 42.69           C  
-ANISOU 2375  CG2 ILE B  99     4759   6190   5271    -86  -1117    383       C  
-ATOM   2376  CD1 ILE B  99     -12.856  -2.756 -17.921  1.00 58.22           C  
-ANISOU 2376  CD1 ILE B  99     7054   8060   7008    147   -902    530       C  
-ATOM   2377  N   ARG B 100     -14.629  -6.090 -16.816  1.00 32.74           N  
-ANISOU 2377  N   ARG B 100     4230   4369   3841   -268  -1007    -41       N  
-ATOM   2378  CA AARG B 100     -13.702  -7.139 -17.174  0.60 36.31           C  
-ANISOU 2378  CA AARG B 100     4927   4680   4190   -131  -1022   -172       C  
-ATOM   2379  CA BARG B 100     -13.680  -7.120 -17.187  0.40 36.48           C  
-ANISOU 2379  CA BARG B 100     4944   4706   4210   -125  -1022   -169       C  
-ATOM   2380  C   ARG B 100     -13.841  -7.449 -18.651  1.00 37.84           C  
-ANISOU 2380  C   ARG B 100     5085   5111   4182    -66  -1091   -334       C  
-ATOM   2381  O   ARG B 100     -14.947  -7.400 -19.199  1.00 41.23           O  
-ANISOU 2381  O   ARG B 100     5401   5704   4560   -225  -1177   -428       O  
-ATOM   2382  CB AARG B 100     -13.972  -8.375 -16.334  0.60 38.68           C  
-ANISOU 2382  CB AARG B 100     5573   4589   4536   -303  -1024   -299       C  
-ATOM   2383  CB BARG B 100     -13.828  -8.376 -16.335  0.40 39.15           C  
-ANISOU 2383  CB BARG B 100     5642   4643   4592   -269  -1025   -293       C  
-ATOM   2384  CG AARG B 100     -12.923  -9.440 -16.471  0.60 42.47           C  
-ANISOU 2384  CG AARG B 100     6371   4826   4940    -70  -1073   -427       C  
-ATOM   2385  CG BARG B 100     -12.622  -9.302 -16.440  0.40 42.50           C  
-ANISOU 2385  CG BARG B 100     6346   4854   4947      9  -1071   -398       C  
-ATOM   2386  CD AARG B 100     -13.221 -10.607 -15.573  0.60 42.98           C  
-ANISOU 2386  CD AARG B 100     6894   4409   5027   -242  -1088   -497       C  
-ATOM   2387  CD BARG B 100     -13.004 -10.751 -16.222  0.40 44.51           C  
-ANISOU 2387  CD BARG B 100     7053   4692   5167   -137  -1120   -588       C  
-ATOM   2388  NE AARG B 100     -12.367 -11.734 -15.911  0.60 46.37           N  
-ANISOU 2388  NE AARG B 100     7677   4568   5374     30  -1184   -674       N  
-ATOM   2389  NE BARG B 100     -13.753 -10.916 -14.986  0.40 44.13           N  
-ANISOU 2389  NE BARG B 100     7203   4362   5200   -459  -1054   -481       N  
-ATOM   2390  CZ AARG B 100     -12.542 -12.963 -15.446  0.60 49.88           C  
-ANISOU 2390  CZ AARG B 100     8650   4510   5794    -70  -1231   -774       C  
-ATOM   2391  CZ BARG B 100     -13.909 -12.073 -14.354  0.40 46.65           C  
-ANISOU 2391  CZ BARG B 100     8035   4201   5490   -612  -1059   -539       C  
-ATOM   2392  NH1AARG B 100     -13.542 -13.220 -14.615  0.60 50.71           N  
-ANISOU 2392  NH1AARG B 100     8971   4362   5934   -510  -1147   -697       N  
-ATOM   2393  NH1BARG B 100     -13.360 -13.177 -14.839  0.40 50.60           N  
-ANISOU 2393  NH1BARG B 100     8907   4406   5913   -423  -1167   -722       N  
-ATOM   2394  NH2AARG B 100     -11.716 -13.932 -15.812  0.60 51.79           N  
-ANISOU 2394  NH2AARG B 100     9221   4490   5966    266  -1347   -958       N  
-ATOM   2395  NH2BARG B 100     -14.607 -12.124 -13.230  0.40 45.64           N  
-ANISOU 2395  NH2BARG B 100     8086   3866   5389   -951   -939   -414       N  
-ATOM   2396  N   LEU B 101     -12.723  -7.749 -19.290  1.00 42.82           N  
-ANISOU 2396  N   LEU B 101     7214   4006   5050   -566  -3073   -353       N  
-ATOM   2397  CA  LEU B 101     -12.746  -8.114 -20.697  1.00 53.55           C  
-ANISOU 2397  CA  LEU B 101     8465   5410   6471   -490  -3165   -465       C  
-ATOM   2398  C   LEU B 101     -12.469  -9.600 -20.829  1.00 61.18           C  
-ANISOU 2398  C   LEU B 101     9746   6068   7432   -522  -3342   -528       C  
-ATOM   2399  O   LEU B 101     -11.401 -10.078 -20.435  1.00 63.83           O  
-ANISOU 2399  O   LEU B 101    10375   6342   7536   -328  -3223   -515       O  
-ATOM   2400  CB  LEU B 101     -11.719  -7.300 -21.475  1.00 57.18           C  
-ANISOU 2400  CB  LEU B 101     8816   6188   6720   -185  -2870   -513       C  
-ATOM   2401  CG  LEU B 101     -12.171  -5.958 -22.055  1.00 60.71           C  
-ANISOU 2401  CG  LEU B 101     8932   6917   7217   -163  -2776   -496       C  
-ATOM   2402  CD1 LEU B 101     -13.061  -5.178 -21.104  1.00 63.78           C  
-ANISOU 2402  CD1 LEU B 101     9176   7309   7750   -319  -2822   -396       C  
-ATOM   2403  CD2 LEU B 101     -10.953  -5.148 -22.402  1.00 56.42           C  
-ANISOU 2403  CD2 LEU B 101     8349   6592   6496     61  -2466   -496       C  
-ATOM   2404  N   LYS B 102     -13.443 -10.325 -21.368  1.00 67.90           N  
-ANISOU 2404  N   LYS B 102    10509   6723   8566   -772  -3617   -598       N  
-ATOM   2405  CA  LYS B 102     -13.359 -11.778 -21.472  1.00 74.46           C  
-ANISOU 2405  CA  LYS B 102    11626   7198   9467   -866  -3800   -681       C  
-ATOM   2406  C   LYS B 102     -13.856 -12.266 -22.825  1.00 79.25           C  
-ANISOU 2406  C   LYS B 102    12098   7816  10198   -908  -4017   -871       C  
-ATOM   2407  O   LYS B 102     -13.647 -13.420 -23.189  1.00 87.37           O  
-ANISOU 2407  O   LYS B 102    13366   8594  11237   -920  -4167   -998       O  
-ATOM   2408  CB  LYS B 102     -14.151 -12.433 -20.347  1.00 77.82           C  
-ANISOU 2408  CB  LYS B 102    12112   7208  10246  -1269  -3841   -563       C  
-ATOM   2409  N   VAL B 115     -17.576  -8.235 -22.326  1.00 69.72           N  
-ANISOU 2409  N   VAL B 115     9285   7368   9837  -1460  -3937   -450       N  
-ATOM   2410  CA  VAL B 115     -17.431  -7.178 -21.326  1.00 68.85           C  
-ANISOU 2410  CA  VAL B 115     9092   7364   9704  -1419  -3734   -267       C  
-ATOM   2411  C   VAL B 115     -18.389  -7.415 -20.166  1.00 72.29           C  
-ANISOU 2411  C   VAL B 115     9275   7543  10649  -1842  -3701    -33       C  
-ATOM   2412  O   VAL B 115     -19.535  -6.968 -20.210  1.00 74.91           O  
-ANISOU 2412  O   VAL B 115     9107   7975  11382  -2029  -3702    119       O  
-ATOM   2413  CB  VAL B 115     -17.726  -5.774 -21.923  1.00 60.23           C  
-ANISOU 2413  CB  VAL B 115     7683   6654   8548  -1223  -3659   -227       C  
-ATOM   2414  CG1 VAL B 115     -17.489  -4.683 -20.878  1.00 57.20           C  
-ANISOU 2414  CG1 VAL B 115     7239   6361   8133  -1159  -3462    -67       C  
-ATOM   2415  CG2 VAL B 115     -16.862  -5.517 -23.131  1.00 56.27           C  
-ANISOU 2415  CG2 VAL B 115     7360   6380   7640   -880  -3579   -393       C  
-ATOM   2416  N   ILE B 116     -17.943  -8.120 -19.131  1.00 69.60           N  
-ANISOU 2416  N   ILE B 116     9251   6907  10286  -1923  -3496     64       N  
-ATOM   2417  CA  ILE B 116     -18.841  -8.383 -18.007  1.00 73.92           C  
-ANISOU 2417  CA  ILE B 116     9559   7290  11235  -2148  -3079    402       C  
-ATOM   2418  C   ILE B 116     -18.875  -7.204 -17.046  1.00 70.96           C  
-ANISOU 2418  C   ILE B 116     9043   7200  10719  -1916  -2583    621       C  
-ATOM   2419  O   ILE B 116     -17.871  -6.504 -16.863  1.00 62.31           O  
-ANISOU 2419  O   ILE B 116     8217   6304   9155  -1591  -2483    514       O  
-ATOM   2420  CB  ILE B 116     -18.526  -9.712 -17.259  1.00 79.00           C  
-ANISOU 2420  CB  ILE B 116    10577   7508  11933  -2276  -2923    500       C  
-ATOM   2421  CG1 ILE B 116     -18.460  -9.492 -15.741  1.00 80.70           C  
-ANISOU 2421  CG1 ILE B 116    10857   7756  12047  -2139  -2307    839       C  
-ATOM   2422  CG2 ILE B 116     -17.267 -10.368 -17.809  1.00 76.51           C  
-ANISOU 2422  CG2 ILE B 116    10815   7059  11195  -2090  -3226    201       C  
-ATOM   2423  CD1 ILE B 116     -17.097  -9.169 -15.178  1.00 78.21           C  
-ANISOU 2423  CD1 ILE B 116    11009   7606  11102  -1735  -2139    759       C  
-ATOM   2424  N   GLY B 117     -20.030  -6.989 -16.429  1.00 75.63           N  
-ANISOU 2424  N   GLY B 117     9204   7805  11727  -2082  -2270    919       N  
-ATOM   2425  CA  GLY B 117     -20.164  -5.893 -15.500  1.00 74.42           C  
-ANISOU 2425  CA  GLY B 117     8922   7898  11455  -1848  -1783   1111       C  
-ATOM   2426  C   GLY B 117     -20.198  -4.598 -16.270  1.00 76.14           C  
-ANISOU 2426  C   GLY B 117     8913   8436  11580  -1653  -1930    979       C  
-ATOM   2427  O   GLY B 117     -20.598  -4.564 -17.435  1.00 78.29           O  
-ANISOU 2427  O   GLY B 117     8941   8775  12031  -1761  -2350    862       O  
-ATOM   2428  N   GLY B 118     -19.755  -3.526 -15.629  1.00 74.23           N  
-ANISOU 2428  N   GLY B 118     8768   8389  11047  -1351  -1590    991       N  
-ATOM   2429  CA  GLY B 118     -20.081  -2.207 -16.117  1.00 76.21           C  
-ANISOU 2429  CA  GLY B 118     8723   8891  11342  -1177  -1578    978       C  
-ATOM   2430  C   GLY B 118     -21.496  -1.933 -15.642  1.00 81.67           C  
-ANISOU 2430  C   GLY B 118     8899   9633  12497  -1280  -1266   1292       C  
-ATOM   2431  O   GLY B 118     -22.226  -2.854 -15.267  1.00 84.58           O  
-ANISOU 2431  O   GLY B 118     9094   9845  13197  -1549  -1190   1490       O  
-ATOM   2432  N   ASP B 119     -21.886  -0.666 -15.641  1.00 82.25           N  
-ANISOU 2432  N   ASP B 119     8720   9911  12620  -1060  -1058   1361       N  
-ATOM   2433  CA  ASP B 119     -23.212  -0.281 -15.174  1.00 86.09           C  
-ANISOU 2433  CA  ASP B 119     8698  10486  13524  -1085   -717   1676       C  
-ATOM   2434  C   ASP B 119     -24.055   0.171 -16.349  1.00 85.55           C  
-ANISOU 2434  C   ASP B 119     8125  10595  13786  -1123  -1038   1730       C  
-ATOM   2435  O   ASP B 119     -25.241   0.470 -16.191  1.00 90.35           O  
-ANISOU 2435  O   ASP B 119     8216  11318  14793  -1151   -839   2003       O  
-ATOM   2436  CB  ASP B 119     -23.104   0.880 -14.181  1.00 88.30           C  
-ANISOU 2436  CB  ASP B 119     9069  10866  13615   -744   -178   1727       C  
-ATOM   2437  CG  ASP B 119     -22.841   0.421 -12.756  1.00 90.71           C  
-ANISOU 2437  CG  ASP B 119     9674  11077  13716   -706    263   1811       C  
-ATOM   2438  OD1 ASP B 119     -23.141  -0.751 -12.433  1.00 93.31           O  
-ANISOU 2438  OD1 ASP B 119     9983  11265  14206   -957    271   1975       O  
-ATOM   2439  OD2 ASP B 119     -22.349   1.248 -11.957  1.00 88.75           O  
-ANISOU 2439  OD2 ASP B 119     9680  10893  13148   -415    606   1715       O  
-ATOM   2440  N   ASP B 120     -23.423   0.168 -17.523  1.00 81.49           N  
-ANISOU 2440  N   ASP B 120     7759  10124  13078  -1102  -1535   1483       N  
-ATOM   2441  CA  ASP B 120     -23.783   1.007 -18.669  1.00 78.92           C  
-ANISOU 2441  CA  ASP B 120     7118  10034  12834   -950  -1808   1480       C  
-ATOM   2442  C   ASP B 120     -23.436   2.458 -18.359  1.00 73.23           C  
-ANISOU 2442  C   ASP B 120     6486   9406  11931   -562  -1437   1508       C  
-ATOM   2443  O   ASP B 120     -22.271   2.788 -18.136  1.00 71.52           O  
-ANISOU 2443  O   ASP B 120     6735   9109  11329   -405  -1359   1309       O  
-ATOM   2444  CB  ASP B 120     -25.255   0.862 -19.069  1.00 85.72           C  
-ANISOU 2444  CB  ASP B 120     7309  11046  14214  -1128  -1931   1720       C  
-ATOM   2445  N   THR B 123     -23.758   5.863 -17.505  1.00 55.59           N  
-ANISOU 2445  N   THR B 123     4092   7293   9737    263   -438   1737       N  
-ATOM   2446  CA  THR B 123     -23.279   6.493 -16.273  1.00 63.62           C  
-ANISOU 2446  CA  THR B 123     5438   8165  10569    440     69   1643       C  
-ATOM   2447  C   THR B 123     -22.110   7.437 -16.527  1.00 60.69           C  
-ANISOU 2447  C   THR B 123     5452   7698   9911    647     69   1401       C  
-ATOM   2448  O   THR B 123     -21.860   8.359 -15.750  1.00 63.26           O  
-ANISOU 2448  O   THR B 123     5960   7911  10165    856    471   1316       O  
-ATOM   2449  CB  THR B 123     -22.783   5.456 -15.243  1.00 66.73           C  
-ANISOU 2449  CB  THR B 123     6170   8444  10739    241    169   1528       C  
-ATOM   2450  OG1 THR B 123     -23.075   4.128 -15.697  1.00 74.33           O  
-ANISOU 2450  OG1 THR B 123     6998   9417  11828    -87   -199   1592       O  
-ATOM   2451  CG2 THR B 123     -23.430   5.701 -13.889  1.00 66.14           C  
-ANISOU 2451  CG2 THR B 123     6032   8357  10743    358    745   1680       C  
-ATOM   2452  N   LEU B 124     -21.387   7.194 -17.613  1.00 58.22           N  
-ANISOU 2452  N   LEU B 124     5258   7422   9440    587   -378   1284       N  
-ATOM   2453  CA  LEU B 124     -20.127   7.886 -17.857  1.00 53.28           C  
-ANISOU 2453  CA  LEU B 124     5005   6701   8538    723   -403   1063       C  
-ATOM   2454  C   LEU B 124     -20.285   9.265 -18.510  1.00 56.23           C  
-ANISOU 2454  C   LEU B 124     5222   7068   9077   1010   -275   1185       C  
-ATOM   2455  O   LEU B 124     -19.357  10.076 -18.492  1.00 54.58           O  
-ANISOU 2455  O   LEU B 124     5285   6717   8734   1133   -156   1033       O  
-ATOM   2456  CB  LEU B 124     -19.210   7.001 -18.695  1.00 48.57           C  
-ANISOU 2456  CB  LEU B 124     4629   6155   7671    571   -887    905       C  
-ATOM   2457  CG  LEU B 124     -18.959   5.620 -18.092  1.00 45.29           C  
-ANISOU 2457  CG  LEU B 124     4418   5696   7095    312  -1010    791       C  
-ATOM   2458  CD1 LEU B 124     -17.896   4.871 -18.877  1.00 40.55           C  
-ANISOU 2458  CD1 LEU B 124     4101   5115   6190    232  -1440    603       C  
-ATOM   2459  CD2 LEU B 124     -18.561   5.752 -16.627  1.00 44.80           C  
-ANISOU 2459  CD2 LEU B 124     4634   5514   6876    337   -600    676       C  
-ATOM   2460  N   THR B 125     -21.463   9.523 -19.072  1.00 55.63           N  
-ANISOU 2460  N   THR B 125     4688   7138   9312   1115   -293   1473       N  
-ATOM   2461  CA  THR B 125     -21.715  10.748 -19.828  1.00 51.16           C  
-ANISOU 2461  CA  THR B 125     3935   6589   8915   1425   -199   1661       C  
-ATOM   2462  C   THR B 125     -21.510  12.031 -19.021  1.00 53.75           C  
-ANISOU 2462  C   THR B 125     4440   6656   9326   1661    329   1609       C  
-ATOM   2463  O   THR B 125     -22.097  12.211 -17.952  1.00 52.98           O  
-ANISOU 2463  O   THR B 125     4299   6481   9350   1707    714   1617       O  
-ATOM   2464  CB  THR B 125     -23.122  10.736 -20.442  1.00 56.26           C  
-ANISOU 2464  CB  THR B 125     4010   7484   9880   1515   -302   1999       C  
-ATOM   2465  OG1 THR B 125     -23.285   9.543 -21.220  1.00 55.75           O  
-ANISOU 2465  OG1 THR B 125     3799   7640   9744   1268   -839   1983       O  
-ATOM   2466  CG2 THR B 125     -23.332  11.953 -21.346  1.00 55.81           C  
-ANISOU 2466  CG2 THR B 125     3795   7472   9937   1869   -239   2218       C  
-ATOM   2467  N   GLY B 126     -20.671  12.921 -19.545  1.00 51.32           N  
-ANISOU 2467  N   GLY B 126     4337   6202   8961   1814    355   1553       N  
-ATOM   2468  CA  GLY B 126     -20.433  14.204 -18.912  1.00 52.30           C  
-ANISOU 2468  CA  GLY B 126     4641   6019   9213   2023    823   1476       C  
-ATOM   2469  C   GLY B 126     -19.627  14.100 -17.636  1.00 53.55           C  
-ANISOU 2469  C   GLY B 126     5211   5978   9157   1871   1025   1090       C  
-ATOM   2470  O   GLY B 126     -19.570  15.053 -16.854  1.00 59.03           O  
-ANISOU 2470  O   GLY B 126     6065   6415   9949   2019   1430    955       O  
-ATOM   2471  N   LYS B 127     -19.007  12.938 -17.426  1.00 49.15           N  
-ANISOU 2471  N   LYS B 127     4835   5543   8296   1597    734    903       N  
-ATOM   2472  CA  LYS B 127     -18.197  12.695 -16.239  1.00 49.95           C  
-ANISOU 2472  CA  LYS B 127     5318   5532   8127   1464    863    551       C  
-ATOM   2473  C   LYS B 127     -16.722  12.635 -16.613  1.00 45.51           C  
-ANISOU 2473  C   LYS B 127     5061   4918   7312   1338    608    309       C  
-ATOM   2474  O   LYS B 127     -16.379  12.369 -17.765  1.00 44.23           O  
-ANISOU 2474  O   LYS B 127     4823   4866   7118   1308    280    430       O  
-ATOM   2475  CB  LYS B 127     -18.599  11.368 -15.592  1.00 51.18           C  
-ANISOU 2475  CB  LYS B 127     5453   5867   8127   1277    772    559       C  
-ATOM   2476  CG  LYS B 127     -20.008  11.342 -15.025  1.00 56.80           C  
-ANISOU 2476  CG  LYS B 127     5852   6645   9085   1375   1077    801       C  
-ATOM   2477  CD  LYS B 127     -20.050  11.899 -13.605  1.00 64.10           C  
-ANISOU 2477  CD  LYS B 127     6996   7436   9924   1517   1559    618       C  
-ATOM   2478  CE  LYS B 127     -21.482  11.965 -13.074  1.00 70.36           C  
-ANISOU 2478  CE  LYS B 127     7447   8313  10974   1671   1922    903       C  
-ATOM   2479  NZ  LYS B 127     -22.175  10.649 -13.177  1.00 72.23           N  
-ANISOU 2479  NZ  LYS B 127     7403   8768  11274   1449   1731   1152       N  
-ATOM   2480  N   ASN B 128     -15.853  12.889 -15.640  1.00 39.13           N  
-ANISOU 2480  N   ASN B 128     5047   3532   6288   1074  -1037    668       N  
-ATOM   2481  CA  ASN B 128     -14.429  12.641 -15.813  1.00 37.97           C  
-ANISOU 2481  CA  ASN B 128     5038   3392   5998    859  -1021    581       C  
-ATOM   2482  C   ASN B 128     -14.145  11.193 -15.491  1.00 36.58           C  
-ANISOU 2482  C   ASN B 128     4729   3469   5701    785   -969    631       C  
-ATOM   2483  O   ASN B 128     -14.282  10.782 -14.347  1.00 39.43           O  
-ANISOU 2483  O   ASN B 128     4943   4032   6005    907   -843    587       O  
-ATOM   2484  CB  ASN B 128     -13.609  13.521 -14.872  1.00 43.20           C  
-ANISOU 2484  CB  ASN B 128     5775   4008   6630    885   -936    312       C  
-ATOM   2485  CG  ASN B 128     -13.722  14.992 -15.200  1.00 51.07           C  
-ANISOU 2485  CG  ASN B 128     6915   4665   7826    929   -980    245       C  
-ATOM   2486  OD1 ASN B 128     -14.451  15.384 -16.111  1.00 49.34           O  
-ANISOU 2486  OD1 ASN B 128     6743   4270   7733    974  -1056    443       O  
-ATOM   2487  ND2 ASN B 128     -12.998  15.818 -14.451  1.00 58.16           N  
-ANISOU 2487  ND2 ASN B 128     7868   5460   8772    930   -942    -43       N  
-ATOM   2488  N   VAL B 129     -13.725  10.419 -16.485  1.00 31.47           N  
-ANISOU 2488  N   VAL B 129     4131   2817   5008    614  -1055    729       N  
-ATOM   2489  CA  VAL B 129     -13.523   8.989 -16.291  1.00 27.24           C  
-ANISOU 2489  CA  VAL B 129     3468   2455   4426    549  -1019    785       C  
-ATOM   2490  C   VAL B 129     -12.042   8.659 -16.203  1.00 26.16           C  
-ANISOU 2490  C   VAL B 129     3439   2400   4101    410   -960    688       C  
-ATOM   2491  O   VAL B 129     -11.261   9.094 -17.052  1.00 28.10           O  
-ANISOU 2491  O   VAL B 129     3853   2548   4274    284  -1020    659       O  
-ATOM   2492  CB  VAL B 129     -14.147   8.184 -17.444  1.00 27.75           C  
-ANISOU 2492  CB  VAL B 129     3478   2468   4595    481  -1183    905       C  
-ATOM   2493  CG1 VAL B 129     -13.945   6.689 -17.236  1.00 25.35           C  
-ANISOU 2493  CG1 VAL B 129     3035   2267   4330    408  -1147    945       C  
-ATOM   2494  CG2 VAL B 129     -15.633   8.525 -17.578  1.00 32.79           C  
-ANISOU 2494  CG2 VAL B 129     3972   3049   5438    618  -1265    997       C  
-ATOM   2495  N   LEU B 130     -11.666   7.916 -15.161  1.00 24.59           N  
-ANISOU 2495  N   LEU B 130     3122   2402   3820    459   -828    668       N  
-ATOM   2496  CA  LEU B 130     -10.312   7.407 -14.992  1.00 23.23           C  
-ANISOU 2496  CA  LEU B 130     3003   2356   3469    360   -772    593       C  
-ATOM   2497  C   LEU B 130     -10.327   5.890 -15.143  1.00 26.45           C  
-ANISOU 2497  C   LEU B 130     3301   2835   3914    330   -752    734       C  
-ATOM   2498  O   LEU B 130     -10.836   5.170 -14.278  1.00 30.58           O  
-ANISOU 2498  O   LEU B 130     3642   3474   4503    451   -636    853       O  
-ATOM   2499  CB  LEU B 130      -9.754   7.765 -13.605  1.00 23.87           C  
-ANISOU 2499  CB  LEU B 130     3028   2647   3395    485   -646    442       C  
-ATOM   2500  CG  LEU B 130      -8.338   7.266 -13.331  1.00 33.52           C  
-ANISOU 2500  CG  LEU B 130     4267   4047   4423    411   -598    354       C  
-ATOM   2501  CD1 LEU B 130      -7.335   7.902 -14.290  1.00 26.07           C  
-ANISOU 2501  CD1 LEU B 130     3487   2953   3466    198   -684    250       C  
-ATOM   2502  CD2 LEU B 130      -7.936   7.508 -11.880  1.00 29.90           C  
-ANISOU 2502  CD2 LEU B 130     3711   3873   3778    595   -500    193       C  
-ATOM   2503  N   ILE B 131      -9.744   5.408 -16.233  1.00 25.12           N  
-ANISOU 2503  N   ILE B 131     3236   2594   3714    187   -849    728       N  
-ATOM   2504  CA  ILE B 131      -9.568   3.979 -16.437  1.00 21.83           C  
-ANISOU 2504  CA  ILE B 131     2739   2201   3354    155   -845    800       C  
-ATOM   2505  C   ILE B 131      -8.299   3.533 -15.729  1.00 22.17           C  
-ANISOU 2505  C   ILE B 131     2784   2433   3208    167   -710    765       C  
-ATOM   2506  O   ILE B 131      -7.235   4.110 -15.928  1.00 25.00           O  
-ANISOU 2506  O   ILE B 131     3265   2854   3378     95   -712    644       O  
-ATOM   2507  CB  ILE B 131      -9.458   3.635 -17.937  1.00 26.02           C  
-ANISOU 2507  CB  ILE B 131     3383   2612   3891     47  -1024    755       C  
-ATOM   2508  CG1 ILE B 131     -10.760   3.989 -18.658  1.00 31.35           C  
-ANISOU 2508  CG1 ILE B 131     4026   3147   4737     68  -1190    785       C  
-ATOM   2509  CG2 ILE B 131      -9.096   2.153 -18.122  1.00 24.99           C  
-ANISOU 2509  CG2 ILE B 131     3186   2479   3832     23  -1026    762       C  
-ATOM   2510  CD1 ILE B 131     -10.626   4.132 -20.172  1.00 33.06           C  
-ANISOU 2510  CD1 ILE B 131     4395   3323   4844     23  -1383    720       C  
-ATOM   2511  N   VAL B 132      -8.421   2.506 -14.895  1.00 23.51           N  
-ANISOU 2511  N   VAL B 132     2792   2696   3446    266   -584    897       N  
-ATOM   2512  CA  VAL B 132      -7.301   2.053 -14.071  1.00 20.76           C  
-ANISOU 2512  CA  VAL B 132     2414   2577   2898    339   -447    897       C  
-ATOM   2513  C   VAL B 132      -6.893   0.646 -14.479  1.00 25.71           C  
-ANISOU 2513  C   VAL B 132     3006   3140   3624    312   -434    990       C  
-ATOM   2514  O   VAL B 132      -7.662  -0.310 -14.291  1.00 24.44           O  
-ANISOU 2514  O   VAL B 132     2696   2861   3729    360   -383   1173       O  
-ATOM   2515  CB  VAL B 132      -7.670   2.073 -12.582  1.00 21.94           C  
-ANISOU 2515  CB  VAL B 132     2397   2953   2985    557   -271   1012       C  
-ATOM   2516  CG1 VAL B 132      -6.489   1.602 -11.734  1.00 23.13           C  
-ANISOU 2516  CG1 VAL B 132     2507   3399   2883    675   -150   1014       C  
-ATOM   2517  CG2 VAL B 132      -8.127   3.478 -12.169  1.00 23.32           C  
-ANISOU 2517  CG2 VAL B 132     2607   3173   3079    617   -299    863       C  
-ATOM   2518  N  AGLU B 133      -5.674   0.519 -14.997  0.46 25.22           N  
-ANISOU 2518  N  AGLU B 133     3060   3143   3380    243   -466    870       N  
-ATOM   2519  N  BGLU B 133      -5.670   0.526 -14.990  0.08 25.28           N  
-ANISOU 2519  N  BGLU B 133     3068   3152   3387    243   -465    870       N  
-ATOM   2520  N  CGLU B 133      -5.695   0.514 -15.047  0.46 25.27           N  
-ANISOU 2520  N  CGLU B 133     3069   3138   3393    237   -472    868       N  
-ATOM   2521  CA AGLU B 133      -5.208  -0.730 -15.592  0.46 25.69           C  
-ANISOU 2521  CA AGLU B 133     3123   3115   3524    226   -481    897       C  
-ATOM   2522  CA BGLU B 133      -5.177  -0.709 -15.585  0.08 25.84           C  
-ANISOU 2522  CA BGLU B 133     3144   3140   3534    226   -480    893       C  
-ATOM   2523  CA CGLU B 133      -5.220  -0.765 -15.577  0.46 25.29           C  
-ANISOU 2523  CA CGLU B 133     3067   3062   3479    229   -479    902       C  
-ATOM   2524  C  AGLU B 133      -3.907  -1.228 -14.964  0.46 24.86           C  
-ANISOU 2524  C  AGLU B 133     2990   3244   3210    319   -352    914       C  
-ATOM   2525  C  BGLU B 133      -3.937  -1.235 -14.870  0.08 25.18           C  
-ANISOU 2525  C  BGLU B 133     3020   3294   3253    329   -342    926       C  
-ATOM   2526  C  CGLU B 133      -3.957  -1.240 -14.884  0.46 24.97           C  
-ANISOU 2526  C  CGLU B 133     2994   3263   3232    328   -344    926       C  
-ATOM   2527  O  AGLU B 133      -3.084  -0.439 -14.510  0.46 25.60           O  
-ANISOU 2527  O  AGLU B 133     3109   3573   3046    327   -318    813       O  
-ATOM   2528  O  BGLU B 133      -3.183  -0.470 -14.272  0.08 25.38           O  
-ANISOU 2528  O  BGLU B 133     3053   3566   3023    357   -295    841       O  
-ATOM   2529  O  CGLU B 133      -3.199  -0.447 -14.337  0.46 26.00           O  
-ANISOU 2529  O  CGLU B 133     3139   3633   3106    348   -303    835       O  
-ATOM   2530  CB AGLU B 133      -5.022  -0.539 -17.106  0.46 27.51           C  
-ANISOU 2530  CB AGLU B 133     3518   3214   3721     92   -663    731       C  
-ATOM   2531  CB BGLU B 133      -4.850  -0.461 -17.058  0.08 26.81           C  
-ANISOU 2531  CB BGLU B 133     3438   3157   3591     92   -650    722       C  
-ATOM   2532  CB CGLU B 133      -4.915  -0.648 -17.075  0.46 27.30           C  
-ANISOU 2532  CB CGLU B 133     3487   3197   3687     99   -652    733       C  
-ATOM   2533  CG AGLU B 133      -4.536  -1.767 -17.864  0.46 28.95           C  
-ANISOU 2533  CG AGLU B 133     3725   3308   3966    101   -712    677       C  
-ATOM   2534  CG BGLU B 133      -5.933  -0.882 -18.032  0.08 29.23           C  
-ANISOU 2534  CG BGLU B 133     3746   3212   4149     45   -821    694       C  
-ATOM   2535  CG CGLU B 133      -6.094  -0.798 -18.005  0.46 29.90           C  
-ANISOU 2535  CG CGLU B 133     3823   3284   4254     43   -827    702       C  
-ATOM   2536  CD AGLU B 133      -5.571  -2.870 -17.905  0.46 31.52           C  
-ANISOU 2536  CD AGLU B 133     3918   3371   4686    123   -761    749       C  
-ATOM   2537  CD BGLU B 133      -5.624  -2.215 -18.689  0.08 31.48           C  
-ANISOU 2537  CD BGLU B 133     4027   3378   4557     61   -883    627       C  
-ATOM   2538  CD CGLU B 133      -5.690  -0.660 -19.463  0.46 30.68           C  
-ANISOU 2538  CD CGLU B 133     4090   3363   4203    -17   -992    534       C  
-ATOM   2539  OE1AGLU B 133      -5.835  -3.478 -16.848  0.46 35.94           O  
-ANISOU 2539  OE1AGLU B 133     4315   3911   5430    206   -604    952       O  
-ATOM   2540  OE1BGLU B 133      -5.594  -3.236 -17.974  0.08 33.19           O  
-ANISOU 2540  OE1BGLU B 133     4110   3530   4970    131   -768    749       O  
-ATOM   2541  OE1CGLU B 133      -5.231  -1.658 -20.061  0.46 30.31           O  
-ANISOU 2541  OE1CGLU B 133     4065   3279   4171      9  -1042    444       O  
-ATOM   2542  OE2AGLU B 133      -6.130  -3.122 -18.992  0.46 35.00           O  
-ANISOU 2542  OE2AGLU B 133     4399   3632   5265     66   -958    606       O  
-ATOM   2543  OE2BGLU B 133      -5.395  -2.237 -19.917  0.08 31.97           O  
-ANISOU 2543  OE2BGLU B 133     4216   3415   4514     30  -1039    455       O  
-ATOM   2544  OE2CGLU B 133      -5.824   0.454 -20.001  0.46 34.35           O  
-ANISOU 2544  OE2CGLU B 133     4662   3859   4530    -63  -1059    505       O  
-ATOM   2545  N   ASP B 134      -3.718  -2.542 -14.941  1.00 22.86           N  
-ANISOU 2545  N   ASP B 134     2669   2916   3102    394   -291   1030       N  
-ATOM   2546  CA  ASP B 134      -2.513  -3.123 -14.362  1.00 22.99           C  
-ANISOU 2546  CA  ASP B 134     2644   3160   2933    522   -167   1078       C  
-ATOM   2547  C   ASP B 134      -1.311  -2.981 -15.297  1.00 26.91           C  
-ANISOU 2547  C   ASP B 134     3272   3733   3219    436   -247    873       C  
-ATOM   2548  O   ASP B 134      -0.221  -2.578 -14.869  1.00 28.13           O  
-ANISOU 2548  O   ASP B 134     3410   4174   3105    471   -192    810       O  
-ATOM   2549  CB  ASP B 134      -2.736  -4.588 -13.943  1.00 30.78           C  
-ANISOU 2549  CB  ASP B 134     3499   4007   4190    663    -43   1324       C  
-ATOM   2550  CG  ASP B 134      -3.235  -5.474 -15.087  1.00 31.66           C  
-ANISOU 2550  CG  ASP B 134     3649   3721   4658    560   -172   1254       C  
-ATOM   2551  OD1 ASP B 134      -3.650  -4.944 -16.140  1.00 31.82           O  
-ANISOU 2551  OD1 ASP B 134     3783   3610   4695    408   -362   1045       O  
-ATOM   2552  OD2 ASP B 134      -3.217  -6.712 -14.917  1.00 41.44           O  
-ANISOU 2552  OD2 ASP B 134     4795   4780   6171    654    -89   1405       O  
-ATOM   2553  N   ILE B 135      -1.508  -3.290 -16.574  1.00 27.17           N  
-ANISOU 2553  N   ILE B 135     3414   3542   3366    340   -379    759       N  
-ATOM   2554  CA  ILE B 135      -0.391  -3.311 -17.508  1.00 24.11           C  
-ANISOU 2554  CA  ILE B 135     3135   3257   2770    308   -422    603       C  
-ATOM   2555  C   ILE B 135      -0.815  -3.075 -18.945  1.00 31.77           C  
-ANISOU 2555  C   ILE B 135     4247   4069   3754    210   -593    453       C  
-ATOM   2556  O   ILE B 135      -1.860  -3.561 -19.387  1.00 31.10           O  
-ANISOU 2556  O   ILE B 135     4162   3733   3920    203   -711    428       O  
-ATOM   2557  CB  ILE B 135       0.414  -4.643 -17.384  1.00 35.70           C  
-ANISOU 2557  CB  ILE B 135     4550   4746   4269    463   -337    644       C  
-ATOM   2558  CG1 ILE B 135       1.654  -4.624 -18.285  1.00 34.41           C  
-ANISOU 2558  CG1 ILE B 135     4473   4752   3848    464   -353    488       C  
-ATOM   2559  CG2 ILE B 135      -0.466  -5.849 -17.708  1.00 38.80           C  
-ANISOU 2559  CG2 ILE B 135     4915   4780   5046    509   -393    676       C  
-ATOM   2560  CD1 ILE B 135       2.618  -5.774 -18.008  1.00 35.41           C  
-ANISOU 2560  CD1 ILE B 135     4533   4963   3957    648   -247    529       C  
-ATOM   2561  N   ILE B 136      -0.008  -2.288 -19.655  1.00 29.79           N  
-ANISOU 2561  N   ILE B 136     4095   3988   3237    145   -604    366       N  
-ATOM   2562  CA AILE B 136      -0.177  -2.057 -21.083  0.49 30.20           C  
-ANISOU 2562  CA AILE B 136     4286   3994   3196    114   -737    257       C  
-ATOM   2563  CA BILE B 136      -0.200  -2.088 -21.083  0.51 30.38           C  
-ANISOU 2563  CA BILE B 136     4307   4010   3225    116   -739    256       C  
-ATOM   2564  C   ILE B 136       0.936  -2.793 -21.816  1.00 32.80           C  
-ANISOU 2564  C   ILE B 136     4657   4467   3338    216   -706    159       C  
-ATOM   2565  O   ILE B 136       2.112  -2.550 -21.549  1.00 32.56           O  
-ANISOU 2565  O   ILE B 136     4583   4667   3120    216   -570    196       O  
-ATOM   2566  CB AILE B 136      -0.057  -0.566 -21.432  0.49 28.88           C  
-ANISOU 2566  CB AILE B 136     4189   3920   2865     -9   -728    299       C  
-ATOM   2567  CB BILE B 136      -0.251  -0.592 -21.456  0.51 29.31           C  
-ANISOU 2567  CB BILE B 136     4246   3942   2948     -7   -748    297       C  
-ATOM   2568  CG1AILE B 136      -1.093   0.246 -20.655  0.49 26.70           C  
-ANISOU 2568  CG1AILE B 136     3872   3509   2762    -81   -750    371       C  
-ATOM   2569  CG1BILE B 136      -1.515   0.046 -20.870  0.51 26.43           C  
-ANISOU 2569  CG1BILE B 136     3851   3404   2786    -65   -805    361       C  
-ATOM   2570  CG2AILE B 136      -0.223  -0.363 -22.944  0.49 31.05           C  
-ANISOU 2570  CG2AILE B 136     4604   4206   2989     18   -843    245       C  
-ATOM   2571  CG2BILE B 136      -0.233  -0.404 -22.977  0.51 31.28           C  
-ANISOU 2571  CG2BILE B 136     4635   4233   3017     23   -848    240       C  
-ATOM   2572  CD1AILE B 136      -2.520  -0.128 -21.008  0.49 25.71           C  
-ANISOU 2572  CD1AILE B 136     3754   3159   2853    -51   -905    358       C  
-ATOM   2573  CD1BILE B 136      -1.562   1.564 -20.961  0.51 24.47           C  
-ANISOU 2573  CD1BILE B 136     3658   3168   2470   -173   -790    414       C  
-ATOM   2574  N   ASP B 137       0.569  -3.693 -22.720  1.00 31.01           N  
-ANISOU 2574  N   ASP B 137     4493   4114   3174    316   -841      8       N  
-ATOM   2575  CA  ASP B 137       1.545  -4.444 -23.490  1.00 33.07           C  
-ANISOU 2575  CA  ASP B 137     4804   4512   3250    463   -824   -127       C  
-ATOM   2576  C   ASP B 137       1.276  -4.177 -24.969  1.00 35.90           C  
-ANISOU 2576  C   ASP B 137     5302   4942   3395    523   -978   -277       C  
-ATOM   2577  O   ASP B 137       1.900  -3.290 -25.561  1.00 37.05           O  
-ANISOU 2577  O   ASP B 137     5507   5341   3229    510   -900   -196       O  
-ATOM   2578  CB  ASP B 137       1.450  -5.931 -23.140  1.00 34.72           C  
-ANISOU 2578  CB  ASP B 137     4947   4502   3742    590   -845   -214       C  
-ATOM   2579  CG  ASP B 137       2.381  -6.797 -23.974  1.00 39.36           C  
-ANISOU 2579  CG  ASP B 137     5593   5195   4166    782   -848   -406       C  
-ATOM   2580  OD1 ASP B 137       3.378  -6.266 -24.505  1.00 41.79           O  
-ANISOU 2580  OD1 ASP B 137     5946   5827   4106    822   -756   -398       O  
-ATOM   2581  OD2 ASP B 137       2.106  -8.011 -24.091  1.00 38.10           O  
-ANISOU 2581  OD2 ASP B 137     5419   4781   4278    899   -935   -562       O  
-ATOM   2582  N   THR B 138       0.332  -4.906 -25.567  1.00 36.27           N  
-ANISOU 2582  N   THR B 138     5382   4782   3618    598  -1198   -485       N  
-ATOM   2583  CA  THR B 138      -0.056  -4.597 -26.952  1.00 38.97           C  
-ANISOU 2583  CA  THR B 138     5848   5247   3713    696  -1382   -645       C  
-ATOM   2584  C   THR B 138      -0.884  -3.316 -27.041  1.00 39.79           C  
-ANISOU 2584  C   THR B 138     5981   5360   3777    571  -1430   -476       C  
-ATOM   2585  O   THR B 138      -1.022  -2.739 -28.114  1.00 44.30           O  
-ANISOU 2585  O   THR B 138     6655   6119   4057    661  -1517   -493       O  
-ATOM   2586  CB  THR B 138      -0.872  -5.722 -27.627  1.00 41.37           C  
-ANISOU 2586  CB  THR B 138     6155   5339   4225    823  -1663   -995       C  
-ATOM   2587  OG1 THR B 138      -2.131  -5.884 -26.955  1.00 44.08           O  
-ANISOU 2587  OG1 THR B 138     6380   5337   5030    678  -1780   -971       O  
-ATOM   2588  CG2 THR B 138      -0.097  -7.025 -27.627  1.00 45.55           C  
-ANISOU 2588  CG2 THR B 138     6667   5801   4838    976  -1632  -1194       C  
-ATOM   2589  N   GLY B 139      -1.460  -2.888 -25.924  1.00 34.32           N  
-ANISOU 2589  N   GLY B 139     5195   4480   3366    401  -1370   -306       N  
-ATOM   2590  CA  GLY B 139      -2.332  -1.725 -25.930  1.00 34.75           C  
-ANISOU 2590  CA  GLY B 139     5268   4497   3439    303  -1421   -164       C  
-ATOM   2591  C   GLY B 139      -3.760  -2.057 -26.344  1.00 40.54           C  
-ANISOU 2591  C   GLY B 139     5967   5039   4397    333  -1689   -311       C  
-ATOM   2592  O   GLY B 139      -4.607  -1.173 -26.413  1.00 41.62           O  
-ANISOU 2592  O   GLY B 139     6108   5143   4565    286  -1759   -208       O  
-ATOM   2593  N   LYS B 140      -4.041  -3.338 -26.590  1.00 39.88           N  
-ANISOU 2593  N   LYS B 140     5828   4810   4516    409  -1846   -563       N  
-ATOM   2594  CA  LYS B 140      -5.352  -3.739 -27.093  1.00 40.37           C  
-ANISOU 2594  CA  LYS B 140     5818   4694   4829    431  -2141   -766       C  
-ATOM   2595  C   LYS B 140      -6.512  -3.647 -26.087  1.00 44.28           C  
-ANISOU 2595  C   LYS B 140     6132   4912   5780    277  -2145   -623       C  
-ATOM   2596  O   LYS B 140      -7.594  -3.179 -26.451  1.00 44.34           O  
-ANISOU 2596  O   LYS B 140     6093   4887   5869    267  -2329   -647       O  
-ATOM   2597  CB  LYS B 140      -5.279  -5.083 -27.837  1.00 48.32           C  
-ANISOU 2597  CB  LYS B 140     6813   5615   5932    568  -2348  -1149       C  
-ATOM   2598  CG  LYS B 140      -4.493  -4.943 -29.150  1.00 60.15           C  
-ANISOU 2598  CG  LYS B 140     8482   7474   6898    784  -2382  -1306       C  
-ATOM   2599  CD  LYS B 140      -4.188  -6.260 -29.855  1.00 70.33           C  
-ANISOU 2599  CD  LYS B 140     9762   8715   8246    957  -2498  -1683       C  
-ATOM   2600  CE  LYS B 140      -3.336  -6.004 -31.101  1.00 75.37           C  
-ANISOU 2600  CE  LYS B 140    10521   9766   8351   1174  -2387  -1716       C  
-ATOM   2601  NZ  LYS B 140      -2.764  -7.248 -31.684  1.00 80.84           N  
-ANISOU 2601  NZ  LYS B 140    11220  10452   9045   1377  -2457  -2061       N  
-ATOM   2602  N   THR B 141      -6.321  -4.066 -24.836  1.00 45.04           N  
-ANISOU 2602  N   THR B 141     6113   4849   6151    189  -1937   -453       N  
-ATOM   2603  CA ATHR B 141      -7.424  -3.854 -23.898  0.35 44.40           C  
-ANISOU 2603  CA ATHR B 141     5854   4578   6439     82  -1903   -271       C  
-ATOM   2604  CA BTHR B 141      -7.302  -3.866 -23.775  0.65 43.16           C  
-ANISOU 2604  CA BTHR B 141     5698   4427   6272     80  -1868   -248       C  
-ATOM   2605  C   THR B 141      -7.611  -2.371 -23.627  1.00 45.33           C  
-ANISOU 2605  C   THR B 141     6038   4856   6329     44  -1815    -71       C  
-ATOM   2606  O   THR B 141      -8.749  -1.950 -23.394  1.00 46.25           O  
-ANISOU 2606  O   THR B 141     6045   4874   6654      6  -1888      2       O  
-ATOM   2607  CB ATHR B 141      -7.381  -4.658 -22.553  0.35 41.22           C  
-ANISOU 2607  CB ATHR B 141     5277   3988   6398     39  -1688    -80       C  
-ATOM   2608  CB BTHR B 141      -6.751  -4.413 -22.432  0.65 39.89           C  
-ANISOU 2608  CB BTHR B 141     5183   3945   6029     59  -1593    -38       C  
-ATOM   2609  OG1ATHR B 141      -7.072  -3.781 -21.462  0.35 39.76           O  
-ANISOU 2609  OG1ATHR B 141     5094   3962   6052     17  -1442    188       O  
-ATOM   2610  OG1BTHR B 141      -6.493  -5.817 -22.556  0.65 40.36           O  
-ANISOU 2610  OG1BTHR B 141     5178   3804   6355    106  -1628   -170       O  
-ATOM   2611  CG2ATHR B 141      -6.412  -5.809 -22.597  0.35 40.98           C  
-ANISOU 2611  CG2ATHR B 141     5269   3897   6404    112  -1626   -178       C  
-ATOM   2612  CG2BTHR B 141      -7.725  -4.176 -21.294  0.65 39.91           C  
-ANISOU 2612  CG2BTHR B 141     4997   3830   6338     -3  -1481    208       C  
-ATOM   2613  N   MET B 142      -6.550  -1.566 -23.726  1.00 38.18           N  
-ANISOU 2613  N   MET B 142     5294   4176   5037     57  -1674      5       N  
-ATOM   2614  CA AMET B 142      -6.701  -0.120 -23.523  0.72 34.21           C  
-ANISOU 2614  CA AMET B 142     4854   3761   4384     15  -1599    173       C  
-ATOM   2615  CA BMET B 142      -6.672  -0.125 -23.560  0.28 33.03           C  
-ANISOU 2615  CA BMET B 142     4709   3617   4224     17  -1601    169       C  
-ATOM   2616  C   MET B 142      -7.497   0.535 -24.658  1.00 35.08           C  
-ANISOU 2616  C   MET B 142     5036   3903   4388     73  -1812    131       C  
-ATOM   2617  O   MET B 142      -8.386   1.344 -24.393  1.00 35.02           O  
-ANISOU 2617  O   MET B 142     4986   3827   4493     56  -1839    241       O  
-ATOM   2618  CB AMET B 142      -5.352   0.596 -23.297  0.72 27.64           C  
-ANISOU 2618  CB AMET B 142     4130   3115   3259    -18  -1392    268       C  
-ATOM   2619  CB BMET B 142      -5.298   0.539 -23.473  0.28 28.47           C  
-ANISOU 2619  CB BMET B 142     4249   3232   3335     -8  -1408    251       C  
-ATOM   2620  CG AMET B 142      -5.489   2.099 -23.048  0.72 28.23           C  
-ANISOU 2620  CG AMET B 142     4256   3201   3270    -77  -1318    416       C  
-ATOM   2621  CG BMET B 142      -5.336   1.796 -22.657  0.28 27.61           C  
-ANISOU 2621  CG BMET B 142     4135   3119   3235    -85  -1275    406       C  
-ATOM   2622  SD AMET B 142      -3.912   2.998 -23.064  0.72 40.15           S  
-ANISOU 2622  SD AMET B 142     5857   4884   4515   -151  -1117    499       S  
-ATOM   2623  SD BMET B 142      -6.204   1.425 -21.130  0.28 44.71           S  
-ANISOU 2623  SD BMET B 142     6108   5151   5729    -92  -1204    467       S  
-ATOM   2624  CE AMET B 142      -3.236   2.437 -24.631  0.72 40.95           C  
-ANISOU 2624  CE AMET B 142     6075   5171   4312    -46  -1183    442       C  
-ATOM   2625  CE BMET B 142      -7.763   2.246 -21.400  0.28 21.74           C  
-ANISOU 2625  CE BMET B 142     3171   2103   2988    -76  -1351    518       C  
-ATOM   2626  N   GLN B 143      -7.190   0.188 -25.903  1.00 45.09           N  
-ANISOU 2626  N   GLN B 143     6408   5306   5419    180  -1961    -26       N  
-ATOM   2627  CA  GLN B 143      -7.963   0.672 -27.050  1.00 49.11           C  
-ANISOU 2627  CA  GLN B 143     6972   5909   5778    296  -2192    -77       C  
-ATOM   2628  C   GLN B 143      -9.445   0.314 -26.905  1.00 51.90           C  
-ANISOU 2628  C   GLN B 143     7142   6075   6503    282  -2416   -178       C  
-ATOM   2629  O   GLN B 143     -10.327   1.117 -27.214  1.00 54.03           O  
-ANISOU 2629  O   GLN B 143     7392   6367   6769    325  -2486    -96       O  
-ATOM   2630  CB  GLN B 143      -7.424   0.067 -28.349  1.00 60.35           C  
-ANISOU 2630  CB  GLN B 143     8483   7549   6900    455  -2275   -288       C  
-ATOM   2631  CG  GLN B 143      -8.471  -0.063 -29.457  1.00 71.00           C  
-ANISOU 2631  CG  GLN B 143     9776   8972   8230    587  -2488   -466       C  
-ATOM   2632  CD  GLN B 143      -8.266  -1.300 -30.323  1.00 79.39           C  
-ANISOU 2632  CD  GLN B 143    10822  10100   9242    712  -2620   -812       C  
-ATOM   2633  OE1 GLN B 143      -9.117  -2.192 -30.367  1.00 83.49           O  
-ANISOU 2633  OE1 GLN B 143    11201  10433  10089    706  -2826  -1065       O  
-ATOM   2634  NE2 GLN B 143      -7.134  -1.356 -31.016  1.00 81.22           N  
-ANISOU 2634  NE2 GLN B 143    11178  10585   9096    828  -2492   -820       N  
-ATOM   2635  N   THR B 144      -9.702  -0.898 -26.420  1.00 51.31           N  
-ANISOU 2635  N   THR B 144     6906   5803   6787    217  -2465   -331       N  
-ATOM   2636  CA  THR B 144     -11.057  -1.413 -26.237  1.00 51.65           C  
-ANISOU 2636  CA  THR B 144     6713   5634   7279    171  -2661   -424       C  
-ATOM   2637  C   THR B 144     -11.803  -0.650 -25.147  1.00 49.51           C  
-ANISOU 2637  C   THR B 144     6317   5263   7231     89  -2504   -147       C  
-ATOM   2638  O   THR B 144     -12.976  -0.295 -25.308  1.00 48.22           O  
-ANISOU 2638  O   THR B 144     6021   5060   7241    106  -2665   -138       O  
-ATOM   2639  CB  THR B 144     -11.023  -2.917 -25.875  1.00 50.76           C  
-ANISOU 2639  CB  THR B 144     6439   5273   7576    103  -2688   -595       C  
-ATOM   2640  OG1 THR B 144     -10.498  -3.660 -26.984  1.00 50.51           O  
-ANISOU 2640  OG1 THR B 144     6511   5322   7358    222  -2839   -914       O  
-ATOM   2641  CG2 THR B 144     -12.417  -3.429 -25.532  1.00 50.40           C  
-ANISOU 2641  CG2 THR B 144     6094   4965   8090     17  -2820   -621       C  
-ATOM   2642  N   LEU B 145     -11.113  -0.397 -24.042  1.00 41.95           N  
-ANISOU 2642  N   LEU B 145     5391   4299   6249     27  -2200     58       N  
-ATOM   2643  CA  LEU B 145     -11.692   0.362 -22.947  1.00 42.68           C  
-ANISOU 2643  CA  LEU B 145     5385   4347   6485     -4  -2032    288       C  
-ATOM   2644  C   LEU B 145     -11.943   1.803 -23.376  1.00 47.33           C  
-ANISOU 2644  C   LEU B 145     6107   5042   6832     57  -2067    374       C  
-ATOM   2645  O   LEU B 145     -12.931   2.420 -22.955  1.00 46.61           O  
-ANISOU 2645  O   LEU B 145     5906   4897   6909     82  -2072    482       O  
-ATOM   2646  CB  LEU B 145     -10.771   0.335 -21.738  1.00 44.07           C  
-ANISOU 2646  CB  LEU B 145     5580   4559   6607    -38  -1730    431       C  
-ATOM   2647  CG  LEU B 145     -11.257  -0.526 -20.584  1.00 48.59           C  
-ANISOU 2647  CG  LEU B 145     5911   5003   7549    -58  -1590    560       C  
-ATOM   2648  CD1 LEU B 145     -12.646  -0.076 -20.178  1.00 57.22           C  
-ANISOU 2648  CD1 LEU B 145     6813   6026   8903    -42  -1617    678       C  
-ATOM   2649  CD2 LEU B 145     -11.284  -1.961 -21.014  1.00 45.35           C  
-ANISOU 2649  CD2 LEU B 145     5395   4419   7416    -93  -1704    432       C  
-ATOM   2650  N   LEU B 146     -11.047   2.329 -24.214  1.00 43.36           N  
-ANISOU 2650  N   LEU B 146     5830   4688   5958     98  -2073    352       N  
-ATOM   2651  CA  LEU B 146     -11.142   3.718 -24.688  1.00 42.16           C  
-ANISOU 2651  CA  LEU B 146     5818   4606   5596    164  -2072    489       C  
-ATOM   2652  C   LEU B 146     -12.230   3.976 -25.741  1.00 46.06           C  
-ANISOU 2652  C   LEU B 146     6282   5150   6069    289  -2320    448       C  
-ATOM   2653  O   LEU B 146     -12.722   5.096 -25.837  1.00 48.63           O  
-ANISOU 2653  O   LEU B 146     6644   5473   6359    350  -2277    593       O  
-ATOM   2654  CB  LEU B 146      -9.796   4.210 -25.215  1.00 38.62           C  
-ANISOU 2654  CB  LEU B 146     5581   4297   4794    163  -1944    548       C  
-ATOM   2655  CG  LEU B 146      -8.751   4.610 -24.188  1.00 36.57           C  
-ANISOU 2655  CG  LEU B 146     5356   4014   4524     47  -1673    630       C  
-ATOM   2656  CD1 LEU B 146      -7.461   4.946 -24.900  1.00 40.03           C  
-ANISOU 2656  CD1 LEU B 146     5951   4601   4659     37  -1572    684       C  
-ATOM   2657  CD2 LEU B 146      -9.240   5.808 -23.381  1.00 34.05           C  
-ANISOU 2657  CD2 LEU B 146     5018   3567   4352     29  -1576    755       C  
-ATOM   2658  N   SER B 147     -12.597   2.964 -26.528  1.00 52.44           N  
-ANISOU 2658  N   SER B 147     7011   6009   6905    330  -2521    218       N  
-ATOM   2659  CA  SER B 147     -13.702   3.091 -27.497  1.00 55.33           C  
-ANISOU 2659  CA  SER B 147     7301   6464   7257    450  -2716    120       C  
-ATOM   2660  C   SER B 147     -15.037   2.853 -26.799  1.00 54.49           C  
-ANISOU 2660  C   SER B 147     6933   6181   7590    392  -2800    109       C  
-ATOM   2661  O   SER B 147     -16.046   3.517 -27.063  1.00 58.23           O  
-ANISOU 2661  O   SER B 147     7331   6696   8097    474  -2871    167       O  
-ATOM   2662  CB  SER B 147     -13.513   2.129 -28.658  1.00 62.39           C  
-ANISOU 2662  CB  SER B 147     8211   7505   7989    535  -2884   -164       C  
-ATOM   2663  OG  SER B 147     -12.300   2.420 -29.327  1.00 69.73           O  
-ANISOU 2663  OG  SER B 147     9354   8647   8491    615  -2765   -111       O  
-ATOM   2664  N   LEU B 148     -15.019   1.904 -25.878  1.00 55.49           N  
-ANISOU 2664  N   LEU B 148     6899   6122   8062    260  -2765     70       N  
-ATOM   2665  CA  LEU B 148     -15.950   1.914 -24.769  1.00 62.47           C  
-ANISOU 2665  CA  LEU B 148     7538   6845   9352    192  -2689    209       C  
-ATOM   2666  C   LEU B 148     -15.649   3.222 -24.023  1.00 68.14           C  
-ANISOU 2666  C   LEU B 148     8384   7602   9904    230  -2461    458       C  
-ATOM   2667  O   LEU B 148     -14.696   3.927 -24.354  1.00 70.16           O  
-ANISOU 2667  O   LEU B 148     8889   7950   9819    265  -2382    510       O  
-ATOM   2668  CB  LEU B 148     -15.681   0.709 -23.874  1.00 65.39           C  
-ANISOU 2668  CB  LEU B 148     7729   7038  10078     67  -2614    207       C  
-ATOM   2669  CG  LEU B 148     -16.868   0.003 -23.236  1.00 68.30           C  
-ANISOU 2669  CG  LEU B 148     7749   7220  10983    -11  -2607    252       C  
-ATOM   2670  CD1 LEU B 148     -17.877  -0.297 -24.305  1.00 72.65           C  
-ANISOU 2670  CD1 LEU B 148     8208   7756  11641     13  -2862     19       C  
-ATOM   2671  CD2 LEU B 148     -16.421  -1.281 -22.547  1.00 68.97           C  
-ANISOU 2671  CD2 LEU B 148     7675   7117  11414   -121  -2509    275       C  
-ATOM   2672  N   VAL B 149     -16.439   3.560 -23.016  1.00 65.43           N  
-ANISOU 2672  N   VAL B 149     7868   7186   9807    229  -2326    601       N  
-ATOM   2673  CA  VAL B 149     -16.316   4.873 -22.384  1.00 56.55           C  
-ANISOU 2673  CA  VAL B 149     6861   6089   8535    296  -2122    758       C  
-ATOM   2674  C   VAL B 149     -16.579   6.032 -23.365  1.00 50.05           C  
-ANISOU 2674  C   VAL B 149     6197   5337   7482    410  -2209    782       C  
-ATOM   2675  O   VAL B 149     -17.472   6.833 -23.125  1.00 51.02           O  
-ANISOU 2675  O   VAL B 149     6248   5447   7688    501  -2173    863       O  
-ATOM   2676  CB  VAL B 149     -14.955   5.107 -21.701  1.00 51.36           C  
-ANISOU 2676  CB  VAL B 149     6384   5437   7692    251  -1918    809       C  
-ATOM   2677  CG1 VAL B 149     -14.980   6.437 -21.001  1.00 48.78           C  
-ANISOU 2677  CG1 VAL B 149     6137   5096   7300    321  -1744    902       C  
-ATOM   2678  CG2 VAL B 149     -14.621   3.981 -20.719  1.00 50.86           C  
-ANISOU 2678  CG2 VAL B 149     6174   5348   7800    177  -1780    820       C  
-ATOM   2679  N   ARG B 150     -15.808   6.124 -24.452  1.00 43.75           N  
-ANISOU 2679  N   ARG B 150     5604   4631   6389    433  -2298    737       N  
-ATOM   2680  CA  ARG B 150     -15.949   7.238 -25.396  1.00 50.57           C  
-ANISOU 2680  CA  ARG B 150     6613   5582   7019    569  -2328    834       C  
-ATOM   2681  C   ARG B 150     -17.293   7.230 -26.106  1.00 51.94           C  
-ANISOU 2681  C   ARG B 150     6631   5843   7261    694  -2530    788       C  
-ATOM   2682  O   ARG B 150     -17.748   8.260 -26.619  1.00 47.15           O  
-ANISOU 2682  O   ARG B 150     6079   5295   6539    844  -2531    921       O  
-ATOM   2683  CB  ARG B 150     -14.798   7.279 -26.407  1.00 52.80           C  
-ANISOU 2683  CB  ARG B 150     7117   5998   6948    592  -2328    844       C  
-ATOM   2684  CG  ARG B 150     -13.643   8.138 -25.924  1.00 52.89           C  
-ANISOU 2684  CG  ARG B 150     7312   5923   6863    525  -2089   1002       C  
-ATOM   2685  CD  ARG B 150     -12.451   8.143 -26.846  1.00 53.79           C  
-ANISOU 2685  CD  ARG B 150     7606   6180   6653    535  -2043   1054       C  
-ATOM   2686  NE  ARG B 150     -11.368   8.899 -26.227  1.00 55.88           N  
-ANISOU 2686  NE  ARG B 150     7993   6318   6921    422  -1816   1189       N  
-ATOM   2687  CZ  ARG B 150     -10.081   8.734 -26.500  1.00 55.87           C  
-ANISOU 2687  CZ  ARG B 150     8106   6396   6726    350  -1715   1225       C  
-ATOM   2688  NH1 ARG B 150      -9.701   7.831 -27.396  1.00 54.46           N  
-ANISOU 2688  NH1 ARG B 150     7950   6444   6299    410  -1804   1128       N  
-ATOM   2689  NH2 ARG B 150      -9.175   9.474 -25.872  1.00 54.24           N  
-ANISOU 2689  NH2 ARG B 150     7973   6048   6588    222  -1525   1334       N  
-ATOM   2690  N   GLN B 151     -17.936   6.068 -26.112  1.00 52.68           N  
-ANISOU 2690  N   GLN B 151     6510   5931   7575    632  -2697    607       N  
-ATOM   2691  CA  GLN B 151     -19.255   5.940 -26.716  1.00 55.77           C  
-ANISOU 2691  CA  GLN B 151     6704   6404   8082    724  -2905    522       C  
-ATOM   2692  C   GLN B 151     -20.318   6.575 -25.825  1.00 53.36           C  
-ANISOU 2692  C   GLN B 151     6221   6013   8039    757  -2807    665       C  
-ATOM   2693  O   GLN B 151     -21.414   6.886 -26.289  1.00 58.96           O  
-ANISOU 2693  O   GLN B 151     6792   6814   8796    875  -2938    666       O  
-ATOM   2694  CB  GLN B 151     -19.595   4.465 -26.972  1.00 62.41           C  
-ANISOU 2694  CB  GLN B 151     7349   7210   9154    620  -3101    256       C  
-ATOM   2695  CG  GLN B 151     -20.196   3.739 -25.765  1.00 65.48           C  
-ANISOU 2695  CG  GLN B 151     7462   7385  10034    466  -3020    278       C  
-ATOM   2696  CD  GLN B 151     -20.465   2.260 -26.031  1.00 70.74           C  
-ANISOU 2696  CD  GLN B 151     7935   7937  11007    348  -3186     30       C  
-ATOM   2697  OE1 GLN B 151     -19.631   1.562 -26.611  1.00 72.51           O  
-ANISOU 2697  OE1 GLN B 151     8290   8170  11090    328  -3264   -156       O  
-ATOM   2698  NE2 GLN B 151     -21.632   1.779 -25.606  1.00 71.18           N  
-ANISOU 2698  NE2 GLN B 151     7674   7870  11500    279  -3221     28       N  
-ATOM   2699  N   TYR B 152     -19.998   6.758 -24.547  1.00 49.88           N  
-ANISOU 2699  N   TYR B 152     5774   5436   7744    678  -2569    777       N  
-ATOM   2700  CA  TYR B 152     -20.941   7.367 -23.618  1.00 53.56           C  
-ANISOU 2700  CA  TYR B 152     6078   5857   8415    744  -2433    900       C  
-ATOM   2701  C   TYR B 152     -20.677   8.856 -23.433  1.00 51.73           C  
-ANISOU 2701  C   TYR B 152     6057   5604   7996    882  -2273   1041       C  
-ATOM   2702  O   TYR B 152     -21.212   9.463 -22.516  1.00 53.59           O  
-ANISOU 2702  O   TYR B 152     6213   5792   8357    959  -2120   1117       O  
-ATOM   2703  CB  TYR B 152     -20.941   6.634 -22.268  1.00 54.27           C  
-ANISOU 2703  CB  TYR B 152     5984   5857   8779    628  -2248    934       C  
-ATOM   2704  CG  TYR B 152     -21.515   5.237 -22.373  1.00 62.63           C  
-ANISOU 2704  CG  TYR B 152     6765   6868  10162    498  -2382    841       C  
-ATOM   2705  CD1 TYR B 152     -22.889   5.038 -22.457  1.00 65.17           C  
-ANISOU 2705  CD1 TYR B 152     6801   7202  10760    521  -2479    840       C  
-ATOM   2706  CD2 TYR B 152     -20.685   4.121 -22.413  1.00 64.36           C  
-ANISOU 2706  CD2 TYR B 152     7003   7008  10444    355  -2413    749       C  
-ATOM   2707  CE1 TYR B 152     -23.422   3.769 -22.571  1.00 68.29           C  
-ANISOU 2707  CE1 TYR B 152     6931   7497  11518    380  -2596    744       C  
-ATOM   2708  CE2 TYR B 152     -21.208   2.843 -22.526  1.00 66.70           C  
-ANISOU 2708  CE2 TYR B 152     7047   7191  11107    233  -2531    650       C  
-ATOM   2709  CZ  TYR B 152     -22.582   2.675 -22.607  1.00 70.74           C  
-ANISOU 2709  CZ  TYR B 152     7275   7682  11921    235  -2619    646       C  
-ATOM   2710  OH  TYR B 152     -23.130   1.413 -22.723  1.00 72.28           O  
-ANISOU 2710  OH  TYR B 152     7215   7712  12537    100  -2723    541       O  
-ATOM   2711  N   ASN B 153     -19.858   9.433 -24.310  1.00 48.32           N  
-ANISOU 2711  N   ASN B 153     5881   5198   7281    923  -2298   1078       N  
-ATOM   2712  CA  ASN B 153     -19.530  10.863 -24.256  1.00 48.67           C  
-ANISOU 2712  CA  ASN B 153     6125   5158   7209   1036  -2143   1228       C  
-ATOM   2713  C   ASN B 153     -19.172  11.410 -22.871  1.00 48.26           C  
-ANISOU 2713  C   ASN B 153     6105   4947   7284   1002  -1910   1237       C  
-ATOM   2714  O   ASN B 153     -19.887  12.245 -22.318  1.00 51.21           O  
-ANISOU 2714  O   ASN B 153     6431   5253   7773   1138  -1828   1286       O  
-ATOM   2715  CB  ASN B 153     -20.662  11.693 -24.855  1.00 53.03           C  
-ANISOU 2715  CB  ASN B 153     6620   5769   7761   1253  -2223   1335       C  
-ATOM   2716  CG  ASN B 153     -20.958  11.316 -26.291  1.00 58.72           C  
-ANISOU 2716  CG  ASN B 153     7319   6703   8288   1341  -2459   1324       C  
-ATOM   2717  OD1 ASN B 153     -20.105  11.456 -27.171  1.00 61.18           O  
-ANISOU 2717  OD1 ASN B 153     7818   7092   8336   1364  -2469   1387       O  
-ATOM   2718  ND2 ASN B 153     -22.181  10.854 -26.543  1.00 63.02           N  
-ANISOU 2718  ND2 ASN B 153     7616   7373   8954   1408  -2646   1246       N  
-ATOM   2719  N   PRO B 154     -18.058  10.939 -22.308  1.00 42.72           N  
-ANISOU 2719  N   PRO B 154     5482   4205   6547    850  -1814   1173       N  
-ATOM   2720  CA  PRO B 154     -17.580  11.480 -21.031  1.00 41.75           C  
-ANISOU 2720  CA  PRO B 154     5399   3963   6500    846  -1623   1149       C  
-ATOM   2721  C   PRO B 154     -17.057  12.894 -21.241  1.00 42.02           C  
-ANISOU 2721  C   PRO B 154     5651   3822   6493    900  -1542   1212       C  
-ATOM   2722  O   PRO B 154     -16.805  13.283 -22.386  1.00 41.52           O  
-ANISOU 2722  O   PRO B 154     5717   3756   6302    910  -1591   1320       O  
-ATOM   2723  CB  PRO B 154     -16.425  10.550 -20.679  1.00 39.06           C  
-ANISOU 2723  CB  PRO B 154     5096   3659   6087    677  -1583   1076       C  
-ATOM   2724  CG  PRO B 154     -15.943  10.075 -22.015  1.00 39.56           C  
-ANISOU 2724  CG  PRO B 154     5262   3794   5973    603  -1720   1087       C  
-ATOM   2725  CD  PRO B 154     -17.143   9.929 -22.865  1.00 40.93           C  
-ANISOU 2725  CD  PRO B 154     5317   4052   6184    706  -1893   1108       C  
-ATOM   2726  N   LYS B 155     -16.907  13.659 -20.165  1.00 45.90           N  
-ANISOU 2726  N   LYS B 155     6170   4161   7108    956  -1419   1150       N  
-ATOM   2727  CA  LYS B 155     -16.326  14.992 -20.280  1.00 49.04           C  
-ANISOU 2727  CA  LYS B 155     6760   4314   7558    973  -1340   1177       C  
-ATOM   2728  C   LYS B 155     -14.840  14.874 -20.630  1.00 44.06           C  
-ANISOU 2728  C   LYS B 155     6284   3630   6826    769  -1303   1178       C  
-ATOM   2729  O   LYS B 155     -14.321  15.639 -21.454  1.00 42.44           O  
-ANISOU 2729  O   LYS B 155     6222   3303   6602    735  -1255   1310       O  
-ATOM   2730  CB  LYS B 155     -16.529  15.794 -18.992  1.00 52.49           C  
-ANISOU 2730  CB  LYS B 155     7177   4578   8190   1100  -1255   1029       C  
-ATOM   2731  CG  LYS B 155     -16.100  17.246 -19.095  1.00 57.32           C  
-ANISOU 2731  CG  LYS B 155     7961   4870   8949   1121  -1179   1020       C  
-ATOM   2732  CD  LYS B 155     -16.617  18.063 -17.928  1.00 64.12           C  
-ANISOU 2732  CD  LYS B 155     8781   5571  10011   1319  -1129    824       C  
-ATOM   2733  CE  LYS B 155     -15.600  18.147 -16.812  1.00 66.95           C  
-ANISOU 2733  CE  LYS B 155     9172   5814  10453   1257  -1103    525       C  
-ATOM   2734  NZ  LYS B 155     -16.011  19.153 -15.786  1.00 74.42           N  
-ANISOU 2734  NZ  LYS B 155    10103   6586  11586   1482  -1059    257       N  
-ATOM   2735  N   MET B 156     -14.172  13.914 -19.998  1.00 38.72           N  
-ANISOU 2735  N   MET B 156     5563   3056   6092    651  -1307   1064       N  
-ATOM   2736  CA  MET B 156     -12.781  13.590 -20.301  1.00 41.49           C  
-ANISOU 2736  CA  MET B 156     6030   3410   6323    458  -1280   1062       C  
-ATOM   2737  C   MET B 156     -12.487  12.131 -19.924  1.00 39.14           C  
-ANISOU 2737  C   MET B 156     5619   3366   5886    376  -1288    967       C  
-ATOM   2738  O   MET B 156     -13.150  11.556 -19.044  1.00 36.10           O  
-ANISOU 2738  O   MET B 156     5070   3089   5559    453  -1270    891       O  
-ATOM   2739  CB  MET B 156     -11.815  14.549 -19.571  1.00 48.68           C  
-ANISOU 2739  CB  MET B 156     7019   4119   7358    367  -1155    922       C  
-ATOM   2740  CG  MET B 156     -11.597  14.235 -18.080  1.00 53.22           C  
-ANISOU 2740  CG  MET B 156     7475   4824   7925    377  -1078    639       C  
-ATOM   2741  SD  MET B 156     -10.185  15.045 -17.244  1.00 53.77           S  
-ANISOU 2741  SD  MET B 156     7584   4769   8077    230   -981    359       S  
-ATOM   2742  CE  MET B 156     -10.449  16.763 -17.645  1.00 46.10           C  
-ANISOU 2742  CE  MET B 156     6737   3324   7456    268   -984    406       C  
-ATOM   2743  N   VAL B 157     -11.523  11.516 -20.614  1.00 35.27           N  
-ANISOU 2743  N   VAL B 157     5202   2979   5221    240  -1293    995       N  
-ATOM   2744  CA AVAL B 157     -11.039  10.186 -20.243  0.69 35.14           C  
-ANISOU 2744  CA AVAL B 157     5094   3164   5093    160  -1271    896       C  
-ATOM   2745  CA BVAL B 157     -11.037  10.193 -20.250  0.31 35.34           C  
-ANISOU 2745  CA BVAL B 157     5121   3189   5119    160  -1271    897       C  
-ATOM   2746  C   VAL B 157      -9.536  10.221 -20.055  1.00 35.58           C  
-ANISOU 2746  C   VAL B 157     5223   3266   5029     10  -1152    822       C  
-ATOM   2747  O   VAL B 157      -8.811  10.809 -20.863  1.00 36.50           O  
-ANISOU 2747  O   VAL B 157     5466   3316   5088    -67  -1129    912       O  
-ATOM   2748  CB AVAL B 157     -11.322   9.105 -21.310  0.69 36.62           C  
-ANISOU 2748  CB AVAL B 157     5262   3472   5179    164  -1422    948       C  
-ATOM   2749  CB BVAL B 157     -11.382   9.135 -21.313  0.31 36.16           C  
-ANISOU 2749  CB BVAL B 157     5202   3409   5128    170  -1426    952       C  
-ATOM   2750  CG1AVAL B 157     -11.333   7.731 -20.667  0.69 28.89           C  
-ANISOU 2750  CG1AVAL B 157     4128   2612   4236    131  -1405    855       C  
-ATOM   2751  CG1BVAL B 157     -12.843   8.982 -21.392  0.31 38.11           C  
-ANISOU 2751  CG1BVAL B 157     5312   3635   5533    296  -1558    988       C  
-ATOM   2752  CG2AVAL B 157     -12.621   9.364 -22.000  0.69 40.94           C  
-ANISOU 2752  CG2AVAL B 157     5764   3986   5806    297  -1575   1029       C  
-ATOM   2753  CG2BVAL B 157     -10.843   9.535 -22.681  0.31 36.19           C  
-ANISOU 2753  CG2BVAL B 157     5377   3426   4948    162  -1482   1069       C  
-ATOM   2754  N   LYS B 158      -9.080   9.598 -18.977  1.00 29.38           N  
-ANISOU 2754  N   LYS B 158     4336   2614   4212    -14  -1065    684       N  
-ATOM   2755  CA  LYS B 158      -7.662   9.499 -18.707  1.00 34.54           C  
-ANISOU 2755  CA  LYS B 158     5012   3362   4748   -140   -970    591       C  
-ATOM   2756  C   LYS B 158      -7.412   8.043 -18.391  1.00 32.52           C  
-ANISOU 2756  C   LYS B 158     4658   3317   4381   -128   -950    568       C  
-ATOM   2757  O   LYS B 158      -8.324   7.335 -17.942  1.00 30.39           O  
-ANISOU 2757  O   LYS B 158     4273   3085   4187    -27   -968    599       O  
-ATOM   2758  CB  LYS B 158      -7.265  10.368 -17.511  1.00 36.13           C  
-ANISOU 2758  CB  LYS B 158     5171   3533   5026   -139   -890    405       C  
-ATOM   2759  CG  LYS B 158      -7.535  11.854 -17.684  1.00 43.70           C  
-ANISOU 2759  CG  LYS B 158     6214   4207   6184   -143   -904    395       C  
-ATOM   2760  CD  LYS B 158      -6.586  12.481 -18.685  1.00 46.36           C  
-ANISOU 2760  CD  LYS B 158     6658   4398   6559   -314   -874    508       C  
-ATOM   2761  CE  LYS B 158      -6.898  13.962 -18.891  1.00 50.64           C  
-ANISOU 2761  CE  LYS B 158     7278   4588   7373   -313   -870    552       C  
-ATOM   2762  NZ  LYS B 158      -5.784  14.622 -19.612  1.00 50.49           N  
-ANISOU 2762  NZ  LYS B 158     7313   4416   7457   -504   -788    673       N  
-ATOM   2763  N   VAL B 159      -6.183   7.589 -18.623  1.00 26.05           N  
-ANISOU 2763  N   VAL B 159     3865   2618   3415   -224   -900    537       N  
-ATOM   2764  CA  VAL B 159      -5.825   6.210 -18.309  1.00 23.41           C  
-ANISOU 2764  CA  VAL B 159     3443   2456   2993   -195   -867    522       C  
-ATOM   2765  C   VAL B 159      -4.661   6.214 -17.330  1.00 27.20           C  
-ANISOU 2765  C   VAL B 159     3856   3113   3366   -219   -753    407       C  
-ATOM   2766  O   VAL B 159      -3.682   6.935 -17.530  1.00 28.12           O  
-ANISOU 2766  O   VAL B 159     4015   3236   3433   -332   -724    343       O  
-ATOM   2767  CB  VAL B 159      -5.421   5.436 -19.573  1.00 25.07           C  
-ANISOU 2767  CB  VAL B 159     3732   2698   3096   -233   -932    569       C  
-ATOM   2768  CG1 VAL B 159      -5.007   4.016 -19.225  1.00 23.82           C  
-ANISOU 2768  CG1 VAL B 159     3486   2663   2901   -192   -894    540       C  
-ATOM   2769  CG2 VAL B 159      -6.567   5.429 -20.590  1.00 30.38           C  
-ANISOU 2769  CG2 VAL B 159     4454   3248   3839   -181  -1090    636       C  
-ATOM   2770  N   ALA B 160      -4.783   5.430 -16.261  1.00 20.02           N  
-ANISOU 2770  N   ALA B 160     2817   2358   2433   -101   -687    398       N  
-ATOM   2771  CA  ALA B 160      -3.678   5.208 -15.336  1.00 21.80           C  
-ANISOU 2771  CA  ALA B 160     2956   2826   2503    -71   -597    298       C  
-ATOM   2772  C   ALA B 160      -3.318   3.743 -15.482  1.00 29.12           C  
-ANISOU 2772  C   ALA B 160     3836   3857   3373    -20   -554    405       C  
-ATOM   2773  O   ALA B 160      -4.196   2.890 -15.402  1.00 30.42           O  
-ANISOU 2773  O   ALA B 160     3944   3954   3661     67   -546    536       O  
-ATOM   2774  CB  ALA B 160      -4.105   5.478 -13.915  1.00 22.56           C  
-ANISOU 2774  CB  ALA B 160     2933   3068   2570     98   -539    229       C  
-ATOM   2775  N   SER B 161      -2.036   3.446 -15.672  1.00 25.22           N  
-ANISOU 2775  N   SER B 161     3341   3509   2732    -70   -521    352       N  
-ATOM   2776  CA  SER B 161      -1.604   2.061 -15.756  1.00 22.46           C  
-ANISOU 2776  CA  SER B 161     2948   3249   2339      9   -471    438       C  
-ATOM   2777  C   SER B 161      -0.394   1.877 -14.857  1.00 24.34           C  
-ANISOU 2777  C   SER B 161     3074   3788   2387     82   -384    375       C  
-ATOM   2778  O   SER B 161       0.568   2.657 -14.938  1.00 25.57           O  
-ANISOU 2778  O   SER B 161     3224   4051   2442    -25   -397    235       O  
-ATOM   2779  CB  SER B 161      -1.303   1.670 -17.219  1.00 26.19           C  
-ANISOU 2779  CB  SER B 161     3540   3607   2803    -81   -539    441       C  
-ATOM   2780  OG  SER B 161      -0.997   0.288 -17.315  1.00 26.60           O  
-ANISOU 2780  OG  SER B 161     3554   3688   2863     17   -507    488       O  
-ATOM   2781  N   LEU B 162      -0.459   0.900 -13.952  1.00 22.23           N  
-ANISOU 2781  N   LEU B 162     2691   3665   2092    272   -293    492       N  
-ATOM   2782  CA  LEU B 162       0.693   0.603 -13.100  1.00 24.36           C  
-ANISOU 2782  CA  LEU B 162     2839   4273   2145    395   -220    453       C  
-ATOM   2783  C   LEU B 162       1.948   0.360 -13.932  1.00 24.69           C  
-ANISOU 2783  C   LEU B 162     2908   4375   2097    297   -232    383       C  
-ATOM   2784  O   LEU B 162       3.018   0.913 -13.651  1.00 26.80           O  
-ANISOU 2784  O   LEU B 162     3096   4873   2215    255   -240    235       O  
-ATOM   2785  CB  LEU B 162       0.444  -0.626 -12.214  1.00 25.27           C  
-ANISOU 2785  CB  LEU B 162     2835   4508   2257    648    -91    684       C  
-ATOM   2786  CG  LEU B 162       1.619  -0.892 -11.276  1.00 29.84           C  
-ANISOU 2786  CG  LEU B 162     3277   5497   2565    829    -26    658       C  
-ATOM   2787  CD1 LEU B 162       1.770   0.245 -10.258  1.00 30.11           C  
-ANISOU 2787  CD1 LEU B 162     3224   5822   2393    890    -72    447       C  
-ATOM   2788  CD2 LEU B 162       1.464  -2.219 -10.543  1.00 33.65           C  
-ANISOU 2788  CD2 LEU B 162     3651   6077   3058   1104    131    965       C  
-ATOM   2789  N   LEU B 163       1.818  -0.483 -14.946  1.00 23.75           N  
-ANISOU 2789  N   LEU B 163     2881   4065   2079    275   -239    469       N  
-ATOM   2790  CA  LEU B 163       2.964  -0.860 -15.773  1.00 24.70           C  
-ANISOU 2790  CA  LEU B 163     3024   4269   2090    239   -228    418       C  
-ATOM   2791  C   LEU B 163       2.705  -0.618 -17.251  1.00 22.85           C  
-ANISOU 2791  C   LEU B 163     2950   3824   1908    100   -306    381       C  
-ATOM   2792  O   LEU B 163       1.583  -0.793 -17.739  1.00 25.89           O  
-ANISOU 2792  O   LEU B 163     3426   3961   2450     88   -383    416       O  
-ATOM   2793  CB  LEU B 163       3.298  -2.334 -15.582  1.00 26.73           C  
-ANISOU 2793  CB  LEU B 163     3227   4568   2360    438   -151    532       C  
-ATOM   2794  CG  LEU B 163       3.431  -2.858 -14.161  1.00 31.13           C  
-ANISOU 2794  CG  LEU B 163     3626   5343   2859    655    -48    662       C  
-ATOM   2795  CD1 LEU B 163       3.677  -4.374 -14.174  1.00 32.44           C  
-ANISOU 2795  CD1 LEU B 163     3760   5447   3119    851     40    825       C  
-ATOM   2796  CD2 LEU B 163       4.545  -2.138 -13.397  1.00 27.96           C  
-ANISOU 2796  CD2 LEU B 163     3090   5338   2194    677    -40    535       C  
-ATOM   2797  N   VAL B 164       3.755  -0.221 -17.961  1.00 23.15           N  
-ANISOU 2797  N   VAL B 164     2999   3994   1803     14   -284    321       N  
-ATOM   2798  CA  VAL B 164       3.732  -0.122 -19.410  1.00 24.85           C  
-ANISOU 2798  CA  VAL B 164     3353   4113   1976    -45   -324    318       C  
-ATOM   2799  C   VAL B 164       4.978  -0.834 -19.896  1.00 27.01           C  
-ANISOU 2799  C   VAL B 164     3583   4598   2079     43   -244    297       C  
-ATOM   2800  O   VAL B 164       6.073  -0.492 -19.468  1.00 25.56           O  
-ANISOU 2800  O   VAL B 164     3262   4649   1799      5   -159    285       O  
-ATOM   2801  CB  VAL B 164       3.796   1.340 -19.884  1.00 27.11           C  
-ANISOU 2801  CB  VAL B 164     3678   4367   2257   -235   -328    332       C  
-ATOM   2802  CG1 VAL B 164       3.907   1.393 -21.422  1.00 32.15           C  
-ANISOU 2802  CG1 VAL B 164     4446   4995   2773   -235   -335    386       C  
-ATOM   2803  CG2 VAL B 164       2.556   2.085 -19.453  1.00 25.73           C  
-ANISOU 2803  CG2 VAL B 164     3551   3973   2252   -294   -408    341       C  
-ATOM   2804  N   LYS B 165       4.820  -1.830 -20.765  1.00 25.55           N  
-ANISOU 2804  N   LYS B 165     3496   4340   1870    174   -282    264       N  
-ATOM   2805  CA  LYS B 165       5.979  -2.558 -21.305  1.00 28.28           C  
-ANISOU 2805  CA  LYS B 165     3811   4893   2042    305   -202    224       C  
-ATOM   2806  C   LYS B 165       6.591  -1.815 -22.487  1.00 27.58           C  
-ANISOU 2806  C   LYS B 165     3771   4963   1746    241   -153    245       C  
-ATOM   2807  O   LYS B 165       5.868  -1.262 -23.308  1.00 30.59           O  
-ANISOU 2807  O   LYS B 165     4283   5231   2109    188   -227    265       O  
-ATOM   2808  CB  LYS B 165       5.571  -3.957 -21.772  1.00 31.15           C  
-ANISOU 2808  CB  LYS B 165     4257   5092   2486    502   -273    132       C  
-ATOM   2809  CG  LYS B 165       5.379  -4.961 -20.654  1.00 33.44           C  
-ANISOU 2809  CG  LYS B 165     4454   5267   2986    620   -244    182       C  
-ATOM   2810  CD  LYS B 165       5.405  -6.396 -21.213  1.00 36.50           C  
-ANISOU 2810  CD  LYS B 165     4893   5495   3481    825   -282     74       C  
-ATOM   2811  CE  LYS B 165       5.449  -7.391 -20.071  1.00 34.31           C  
-ANISOU 2811  CE  LYS B 165     4496   5120   3420    966   -195    204       C  
-ATOM   2812  NZ  LYS B 165       5.377  -8.787 -20.552  1.00 27.66           N  
-ANISOU 2812  NZ  LYS B 165     3695   4020   2793   1154   -235     98       N  
-ATOM   2813  N   ARG B 166       7.919  -1.818 -22.591  1.00 28.88           N  
-ANISOU 2813  N   ARG B 166     3911   4311   2749   -304    -42     69       N  
-ATOM   2814  CA  ARG B 166       8.569  -1.302 -23.798  1.00 27.52           C  
-ANISOU 2814  CA  ARG B 166     3671   4199   2588   -448    -42    102       C  
-ATOM   2815  C   ARG B 166       8.510  -2.375 -24.868  1.00 35.26           C  
-ANISOU 2815  C   ARG B 166     4696   5228   3472   -473     21    134       C  
-ATOM   2816  O   ARG B 166       9.372  -3.260 -24.943  1.00 35.52           O  
-ANISOU 2816  O   ARG B 166     4722   5343   3430   -417     73     84       O  
-ATOM   2817  CB  ARG B 166      10.018  -0.866 -23.531  1.00 26.56           C  
-ANISOU 2817  CB  ARG B 166     3431   4161   2498   -453    -52      5       C  
-ATOM   2818  CG  ARG B 166      10.123   0.514 -22.875  1.00 30.83           C  
-ANISOU 2818  CG  ARG B 166     3905   4643   3168   -499   -111    -39       C  
-ATOM   2819  CD  ARG B 166      11.566   1.001 -22.724  1.00 33.61           C  
-ANISOU 2819  CD  ARG B 166     4093   5077   3602   -541   -114   -181       C  
-ATOM   2820  NE  ARG B 166      12.372   0.062 -21.946  1.00 35.90           N  
-ANISOU 2820  NE  ARG B 166     4330   5502   3810   -366   -160   -319       N  
-ATOM   2821  CZ  ARG B 166      12.366  -0.017 -20.619  1.00 37.15           C  
-ANISOU 2821  CZ  ARG B 166     4499   5684   3932   -184   -255   -429       C  
-ATOM   2822  NH1 ARG B 166      11.600   0.802 -19.901  1.00 31.22           N  
-ANISOU 2822  NH1 ARG B 166     3801   4823   3238   -178   -310   -418       N  
-ATOM   2823  NH2 ARG B 166      13.131  -0.918 -20.008  1.00 37.84           N  
-ANISOU 2823  NH2 ARG B 166     4563   5907   3906     20   -291   -546       N  
-ATOM   2824  N   THR B 167       7.470  -2.295 -25.686  1.00 32.83           N  
-ANISOU 2824  N   THR B 167     4434   4876   3163   -539      6    202       N  
-ATOM   2825  CA  THR B 167       7.186  -3.319 -26.678  1.00 36.92           C  
-ANISOU 2825  CA  THR B 167     4999   5434   3595   -557     43    202       C  
-ATOM   2826  C   THR B 167       6.412  -2.664 -27.834  1.00 41.35           C  
-ANISOU 2826  C   THR B 167     5580   5991   4140   -628    -20    271       C  
-ATOM   2827  O   THR B 167       5.703  -1.669 -27.617  1.00 42.74           O  
-ANISOU 2827  O   THR B 167     5748   6109   4383   -637    -82    316       O  
-ATOM   2828  CB  THR B 167       6.382  -4.457 -26.019  1.00 39.25           C  
-ANISOU 2828  CB  THR B 167     5341   5669   3904   -487     96    141       C  
-ATOM   2829  OG1 THR B 167       6.238  -5.552 -26.930  1.00 46.99           O  
-ANISOU 2829  OG1 THR B 167     6360   6680   4814   -514    148    104       O  
-ATOM   2830  CG2 THR B 167       5.020  -3.955 -25.592  1.00 32.65           C  
-ANISOU 2830  CG2 THR B 167     4494   4735   3175   -497     50    150       C  
-ATOM   2831  N   PRO B 168       6.565  -3.193 -29.068  1.00 40.15           N  
-ANISOU 2831  N   PRO B 168     5470   5906   3878   -650     -5    278       N  
-ATOM   2832  CA  PRO B 168       5.899  -2.540 -30.202  1.00 39.88           C  
-ANISOU 2832  CA  PRO B 168     5483   5888   3783   -660    -78    339       C  
-ATOM   2833  C   PRO B 168       4.392  -2.421 -29.995  1.00 40.78           C  
-ANISOU 2833  C   PRO B 168     5569   5967   3960   -636   -182    301       C  
-ATOM   2834  O   PRO B 168       3.762  -3.377 -29.545  1.00 38.81           O  
-ANISOU 2834  O   PRO B 168     5280   5698   3770   -636   -173    198       O  
-ATOM   2835  CB  PRO B 168       6.191  -3.487 -31.371  1.00 40.36           C  
-ANISOU 2835  CB  PRO B 168     5604   6032   3701   -654    -53    309       C  
-ATOM   2836  CG  PRO B 168       7.469  -4.165 -31.003  1.00 37.53           C  
-ANISOU 2836  CG  PRO B 168     5229   5697   3332   -663     64    288       C  
-ATOM   2837  CD  PRO B 168       7.372  -4.352 -29.497  1.00 38.30           C  
-ANISOU 2837  CD  PRO B 168     5263   5738   3550   -638     76    233       C  
-ATOM   2838  N   ARG B 169       3.824  -1.267 -30.339  1.00 42.66           N  
-ANISOU 2838  N   ARG B 169     5828   6188   4193   -610   -257    379       N  
-ATOM   2839  CA  ARG B 169       2.428  -0.996 -30.021  1.00 52.65           C  
-ANISOU 2839  CA  ARG B 169     7040   7425   5540   -573   -359    342       C  
-ATOM   2840  C   ARG B 169       1.726  -0.238 -31.155  1.00 60.95           C  
-ANISOU 2840  C   ARG B 169     8144   8535   6479   -489   -474    393       C  
-ATOM   2841  O   ARG B 169       1.909   0.971 -31.313  1.00 65.24           O  
-ANISOU 2841  O   ARG B 169     8764   9036   6987   -450   -462    522       O  
-ATOM   2842  CB  ARG B 169       2.357  -0.213 -28.705  1.00 55.52           C  
-ANISOU 2842  CB  ARG B 169     7372   7681   6042   -580   -330    385       C  
-ATOM   2843  CG  ARG B 169       1.123  -0.484 -27.861  1.00 55.70           C  
-ANISOU 2843  CG  ARG B 169     7316   7645   6201   -560   -362    310       C  
-ATOM   2844  CD  ARG B 169       1.272   0.091 -26.459  1.00 52.27           C  
-ANISOU 2844  CD  ARG B 169     6882   7101   5876   -549   -308    346       C  
-ATOM   2845  NE  ARG B 169       2.123  -0.747 -25.622  1.00 57.82           N  
-ANISOU 2845  NE  ARG B 169     7599   7783   6588   -549   -206    296       N  
-ATOM   2846  CZ  ARG B 169       3.236  -0.335 -25.025  1.00 53.00           C  
-ANISOU 2846  CZ  ARG B 169     7010   7164   5963   -542   -173    319       C  
-ATOM   2847  NH1 ARG B 169       3.641   0.918 -25.155  1.00 50.81           N  
-ANISOU 2847  NH1 ARG B 169     6740   6871   5695   -572   -205    388       N  
-ATOM   2848  NH2 ARG B 169       3.936  -1.179 -24.287  1.00 55.78           N  
-ANISOU 2848  NH2 ARG B 169     7377   7522   6296   -493   -100    258       N  
-ATOM   2849  N   SER B 170       0.922  -0.955 -31.936  1.00 64.47           N  
-ANISOU 2849  N   SER B 170     8555   9076   6865   -446   -580    276       N  
-ATOM   2850  CA  SER B 170       0.235  -0.364 -33.086  1.00 73.04           C  
-ANISOU 2850  CA  SER B 170     9698  10255   7800   -311   -722    294       C  
-ATOM   2851  C   SER B 170      -0.759   0.719 -32.664  1.00 77.30           C  
-ANISOU 2851  C   SER B 170    10200  10759   8411   -230   -807    342       C  
-ATOM   2852  O   SER B 170      -0.451   1.911 -32.705  1.00 79.34           O  
-ANISOU 2852  O   SER B 170    10575  10955   8616   -173   -763    507       O  
-ATOM   2853  CB  SER B 170      -0.480  -1.444 -33.909  1.00 73.89           C  
-ANISOU 2853  CB  SER B 170     9735  10489   7849   -278   -849     97       C  
-ATOM   2854  OG  SER B 170      -1.573  -1.989 -33.196  1.00 74.96           O  
-ANISOU 2854  OG  SER B 170     9684  10607   8189   -331   -900    -74       O  
-ATOM   2855  N   TYR B 173      -2.807   5.660 -28.378  1.00 56.17           N  
-ANISOU 2855  N   TYR B 173     7515   7558   6269   -125   -713    739       N  
-ATOM   2856  CA  TYR B 173      -2.956   6.376 -27.112  1.00 57.31           C  
-ANISOU 2856  CA  TYR B 173     7659   7559   6558   -150   -649    786       C  
-ATOM   2857  C   TYR B 173      -1.842   6.021 -26.131  1.00 57.01           C  
-ANISOU 2857  C   TYR B 173     7623   7437   6601   -285   -531    758       C  
-ATOM   2858  O   TYR B 173      -1.600   4.846 -25.854  1.00 57.55           O  
-ANISOU 2858  O   TYR B 173     7616   7546   6704   -344   -513    654       O  
-ATOM   2859  CB  TYR B 173      -4.314   6.058 -26.479  1.00 58.66           C  
-ANISOU 2859  CB  TYR B 173     7685   7735   6869   -100   -718    694       C  
-ATOM   2860  CG  TYR B 173      -4.727   6.999 -25.366  1.00 58.77           C  
-ANISOU 2860  CG  TYR B 173     7726   7606   6996    -69   -668    765       C  
-ATOM   2861  CD1 TYR B 173      -5.375   8.196 -25.657  1.00 62.61           C  
-ANISOU 2861  CD1 TYR B 173     8282   8071   7437     62   -714    871       C  
-ATOM   2862  CD2 TYR B 173      -4.487   6.689 -24.029  1.00 56.87           C  
-ANISOU 2862  CD2 TYR B 173     7467   7254   6888   -140   -572    727       C  
-ATOM   2863  CE1 TYR B 173      -5.769   9.066 -24.656  1.00 61.14           C  
-ANISOU 2863  CE1 TYR B 173     8132   7747   7351     96   -662    936       C  
-ATOM   2864  CE2 TYR B 173      -4.880   7.558 -23.012  1.00 58.02           C  
-ANISOU 2864  CE2 TYR B 173     7654   7267   7122    -95   -529    786       C  
-ATOM   2865  CZ  TYR B 173      -5.522   8.746 -23.337  1.00 58.25           C  
-ANISOU 2865  CZ  TYR B 173     7741   7271   7122     10   -573    889       C  
-ATOM   2866  OH  TYR B 173      -5.920   9.628 -22.353  1.00 56.64           O  
-ANISOU 2866  OH  TYR B 173     7591   6929   7001     59   -524    949       O  
-ATOM   2867  N   LYS B 174      -1.162   7.042 -25.615  1.00 54.72           N  
-ANISOU 2867  N   LYS B 174     7420   7030   6340   -318   -449    838       N  
-ATOM   2868  CA  LYS B 174      -0.208   6.860 -24.524  1.00 50.58           C  
-ANISOU 2868  CA  LYS B 174     6878   6440   5901   -407   -375    778       C  
-ATOM   2869  C   LYS B 174      -0.940   7.119 -23.208  1.00 39.28           C  
-ANISOU 2869  C   LYS B 174     5427   4912   4587   -359   -380    756       C  
-ATOM   2870  O   LYS B 174      -1.697   8.086 -23.100  1.00 37.32           O  
-ANISOU 2870  O   LYS B 174     5222   4590   4367   -296   -395    832       O  
-ATOM   2871  CB  LYS B 174       0.970   7.812 -24.678  1.00 53.47           C  
-ANISOU 2871  CB  LYS B 174     7320   6734   6263   -483   -282    827       C  
-ATOM   2872  N   PRO B 175      -0.735   6.253 -22.204  1.00 37.21           N  
-ANISOU 2872  N   PRO B 175     5122   4640   4378   -362   -352    662       N  
-ATOM   2873  CA  PRO B 175      -1.488   6.464 -20.956  1.00 31.10           C  
-ANISOU 2873  CA  PRO B 175     4359   3759   3699   -287   -333    652       C  
-ATOM   2874  C   PRO B 175      -1.107   7.767 -20.270  1.00 32.04           C  
-ANISOU 2874  C   PRO B 175     4557   3767   3851   -283   -320    689       C  
-ATOM   2875  O   PRO B 175       0.034   8.203 -20.368  1.00 32.25           O  
-ANISOU 2875  O   PRO B 175     4604   3793   3856   -356   -304    665       O  
-ATOM   2876  CB  PRO B 175      -1.098   5.259 -20.088  1.00 36.29           C  
-ANISOU 2876  CB  PRO B 175     5004   4421   4362   -261   -274    553       C  
-ATOM   2877  CG  PRO B 175       0.143   4.693 -20.724  1.00 40.32           C  
-ANISOU 2877  CG  PRO B 175     5499   5038   4784   -332   -277    509       C  
-ATOM   2878  CD  PRO B 175       0.063   5.016 -22.186  1.00 39.81           C  
-ANISOU 2878  CD  PRO B 175     5414   5046   4665   -397   -322    573       C  
-ATOM   2879  N   ASP B 176      -2.056   8.377 -19.573  1.00 32.06           N  
-ANISOU 2879  N   ASP B 176     4593   3669   3921   -205   -315    731       N  
-ATOM   2880  CA  ASP B 176      -1.819   9.666 -18.932  1.00 33.79           C  
-ANISOU 2880  CA  ASP B 176     4899   3764   4175   -198   -298    760       C  
-ATOM   2881  C   ASP B 176      -1.030   9.576 -17.630  1.00 32.66           C  
-ANISOU 2881  C   ASP B 176     4788   3572   4048   -175   -284    649       C  
-ATOM   2882  O   ASP B 176      -0.289  10.492 -17.271  1.00 34.18           O  
-ANISOU 2882  O   ASP B 176     5021   3702   4266   -219   -283    607       O  
-ATOM   2883  CB  ASP B 176      -3.159  10.338 -18.674  1.00 36.98           C  
-ANISOU 2883  CB  ASP B 176     5335   4081   4634   -100   -296    847       C  
-ATOM   2884  CG  ASP B 176      -4.008  10.406 -19.920  1.00 35.76           C  
-ANISOU 2884  CG  ASP B 176     5137   4006   4446    -71   -343    929       C  
-ATOM   2885  OD1 ASP B 176      -4.761   9.446 -20.195  1.00 29.70           O  
-ANISOU 2885  OD1 ASP B 176     4260   3325   3700    -40   -375    886       O  
-ATOM   2886  OD2 ASP B 176      -3.887  11.411 -20.636  1.00 35.00           O  
-ANISOU 2886  OD2 ASP B 176     5118   3881   4297    -68   -340   1021       O  
-ATOM   2887  N   PHE B 177      -1.206   8.476 -16.910  1.00 25.26           N  
-ANISOU 2887  N   PHE B 177     3841   2660   3098    -91   -266    588       N  
-ATOM   2888  CA  PHE B 177      -0.498   8.280 -15.654  1.00 25.81           C  
-ANISOU 2888  CA  PHE B 177     3967   2704   3136     -3   -266    478       C  
-ATOM   2889  C   PHE B 177       0.124   6.889 -15.659  1.00 29.54           C  
-ANISOU 2889  C   PHE B 177     4408   3284   3532     30   -248    402       C  
-ATOM   2890  O   PHE B 177      -0.583   5.886 -15.774  1.00 32.14           O  
-ANISOU 2890  O   PHE B 177     4732   3615   3865     71   -177    432       O  
-ATOM   2891  CB  PHE B 177      -1.472   8.405 -14.476  1.00 26.65           C  
-ANISOU 2891  CB  PHE B 177     4171   2682   3274    151   -213    504       C  
-ATOM   2892  CG  PHE B 177      -2.324   9.642 -14.522  1.00 30.07           C  
-ANISOU 2892  CG  PHE B 177     4637   3004   3782    141   -212    600       C  
-ATOM   2893  CD1 PHE B 177      -1.791  10.885 -14.190  1.00 28.63           C  
-ANISOU 2893  CD1 PHE B 177     4513   2751   3614    109   -249    572       C  
-ATOM   2894  CD2 PHE B 177      -3.663   9.566 -14.893  1.00 27.71           C  
-ANISOU 2894  CD2 PHE B 177     4304   2673   3553    167   -169    701       C  
-ATOM   2895  CE1 PHE B 177      -2.579  12.030 -14.236  1.00 30.85           C  
-ANISOU 2895  CE1 PHE B 177     4851   2914   3955    115   -227    671       C  
-ATOM   2896  CE2 PHE B 177      -4.457  10.709 -14.931  1.00 27.53           C  
-ANISOU 2896  CE2 PHE B 177     4316   2559   3585    191   -170    794       C  
-ATOM   2897  CZ  PHE B 177      -3.914  11.941 -14.606  1.00 28.58           C  
-ANISOU 2897  CZ  PHE B 177     4542   2607   3710    170   -191    793       C  
-ATOM   2898  N   VAL B 178       1.444   6.819 -15.536  1.00 24.54           N  
-ANISOU 2898  N   VAL B 178     3747   2736   2843     12   -300    289       N  
-ATOM   2899  CA  VAL B 178       2.133   5.528 -15.605  1.00 23.46           C  
-ANISOU 2899  CA  VAL B 178     3586   2712   2617     61   -283    221       C  
-ATOM   2900  C   VAL B 178       2.948   5.284 -14.348  1.00 24.40           C  
-ANISOU 2900  C   VAL B 178     3765   2859   2645    240   -321     83       C  
-ATOM   2901  O   VAL B 178       3.708   6.163 -13.936  1.00 26.68           O  
-ANISOU 2901  O   VAL B 178     4021   3166   2952    228   -413    -27       O  
-ATOM   2902  CB  VAL B 178       3.087   5.497 -16.810  1.00 31.07           C  
-ANISOU 2902  CB  VAL B 178     4437   3795   3574   -102   -315    201       C  
-ATOM   2903  CG1 VAL B 178       3.938   4.217 -16.805  1.00 28.41           C  
-ANISOU 2903  CG1 VAL B 178     4078   3581   3137    -35   -301    119       C  
-ATOM   2904  CG2 VAL B 178       2.315   5.627 -18.096  1.00 31.02           C  
-ANISOU 2904  CG2 VAL B 178     4399   3781   3605   -225   -289    329       C  
-ATOM   2905  N   GLY B 179       2.797   4.112 -13.723  1.00 21.70           N  
-ANISOU 2905  N   GLY B 179     3520   2518   2207    423   -243     74       N  
-ATOM   2906  CA  GLY B 179       3.618   3.817 -12.565  1.00 23.39           C  
-ANISOU 2906  CA  GLY B 179     3817   2782   2287    654   -290    -59       C  
-ATOM   2907  C   GLY B 179       5.061   3.599 -12.996  1.00 30.08           C  
-ANISOU 2907  C   GLY B 179     4533   3813   3083    612   -393   -196       C  
-ATOM   2908  O   GLY B 179       5.949   4.395 -12.658  1.00 26.87           O  
-ANISOU 2908  O   GLY B 179     4041   3475   2692    603   -526   -349       O  
-ATOM   2909  N   PHE B 180       5.287   2.520 -13.748  1.00 24.44           N  
-ANISOU 2909  N   PHE B 180     3006   3302   2978     40   -295    559       N  
-ATOM   2910  CA  PHE B 180       6.631   2.055 -14.082  1.00 22.23           C  
-ANISOU 2910  CA  PHE B 180     2715   3183   2549    -86   -193    530       C  
-ATOM   2911  C   PHE B 180       6.669   1.637 -15.539  1.00 26.88           C  
-ANISOU 2911  C   PHE B 180     3354   3929   2931   -177   -191    611       C  
-ATOM   2912  O   PHE B 180       5.755   0.972 -16.011  1.00 25.49           O  
-ANISOU 2912  O   PHE B 180     3190   3801   2694   -128   -261    599       O  
-ATOM   2913  CB  PHE B 180       6.959   0.827 -13.237  1.00 22.97           C  
-ANISOU 2913  CB  PHE B 180     2716   3364   2649    -17   -103    353       C  
-ATOM   2914  CG  PHE B 180       6.938   1.083 -11.755  1.00 21.86           C  
-ANISOU 2914  CG  PHE B 180     2579   3092   2635     40   -106    264       C  
-ATOM   2915  CD1 PHE B 180       5.745   1.018 -11.033  1.00 22.53           C  
-ANISOU 2915  CD1 PHE B 180     2680   3071   2808    162   -113    204       C  
-ATOM   2916  CD2 PHE B 180       8.113   1.374 -11.088  1.00 22.89           C  
-ANISOU 2916  CD2 PHE B 180     2701   3211   2787    -48    -97    240       C  
-ATOM   2917  CE1 PHE B 180       5.734   1.245  -9.653  1.00 25.39           C  
-ANISOU 2917  CE1 PHE B 180     3105   3317   3226    192    -76    102       C  
-ATOM   2918  CE2 PHE B 180       8.113   1.619  -9.718  1.00 24.55           C  
-ANISOU 2918  CE2 PHE B 180     2978   3298   3053    -33   -126    153       C  
-ATOM   2919  CZ  PHE B 180       6.927   1.554  -9.002  1.00 23.57           C  
-ANISOU 2919  CZ  PHE B 180     2925   3068   2962     85    -98     74       C  
-ATOM   2920  N   GLU B 181       7.727   2.013 -16.244  1.00 24.64           N  
-ANISOU 2920  N   GLU B 181     3111   3726   2527   -332   -103    691       N  
-ATOM   2921  CA  GLU B 181       7.935   1.530 -17.603  1.00 26.13           C  
-ANISOU 2921  CA  GLU B 181     3391   4084   2455   -444    -32    732       C  
-ATOM   2922  C   GLU B 181       8.974   0.417 -17.552  1.00 29.24           C  
-ANISOU 2922  C   GLU B 181     3675   4636   2800   -437    197    559       C  
-ATOM   2923  O   GLU B 181      10.114   0.633 -17.136  1.00 30.01           O  
-ANISOU 2923  O   GLU B 181     3646   4757   2998   -483    322    547       O  
-ATOM   2924  CB  GLU B 181       8.405   2.661 -18.497  1.00 28.58           C  
-ANISOU 2924  CB  GLU B 181     3831   4382   2647   -635    -36    946       C  
-ATOM   2925  CG  GLU B 181       8.337   2.347 -19.982  1.00 35.62           C  
-ANISOU 2925  CG  GLU B 181     4908   5426   3200   -780      0   1024       C  
-ATOM   2926  CD  GLU B 181       9.092   3.350 -20.780  1.00 39.99           C  
-ANISOU 2926  CD  GLU B 181     5588   5997   3611  -1006     73   1229       C  
-ATOM   2927  OE1 GLU B 181      10.342   3.345 -20.674  1.00 42.81           O  
-ANISOU 2927  OE1 GLU B 181     5831   6444   3990  -1095    322   1182       O  
-ATOM   2928  OE2 GLU B 181       8.440   4.150 -21.491  1.00 42.21           O  
-ANISOU 2928  OE2 GLU B 181     6064   6191   3781  -1099   -131   1457       O  
-ATOM   2929  N   ILE B 182       8.582  -0.779 -17.977  1.00 27.79           N  
-ANISOU 2929  N   ILE B 182     3528   4541   2491   -381    239    430       N  
-ATOM   2930  CA  ILE B 182       9.392  -1.967 -17.715  1.00 25.21           C  
-ANISOU 2930  CA  ILE B 182     3081   4298   2199   -305    436    241       C  
-ATOM   2931  C   ILE B 182       9.854  -2.626 -19.007  1.00 27.50           C  
-ANISOU 2931  C   ILE B 182     3486   4732   2229   -391    647    167       C  
-ATOM   2932  O   ILE B 182       9.310  -2.339 -20.077  1.00 30.12           O  
-ANISOU 2932  O   ILE B 182     4038   5108   2298   -519    590    250       O  
-ATOM   2933  CB  ILE B 182       8.594  -2.980 -16.884  1.00 23.95           C  
-ANISOU 2933  CB  ILE B 182     2877   4068   2154   -146    340    107       C  
-ATOM   2934  CG1 ILE B 182       7.372  -3.476 -17.655  1.00 27.52           C  
-ANISOU 2934  CG1 ILE B 182     3490   4528   2440   -168    216     94       C  
-ATOM   2935  CG2 ILE B 182       8.216  -2.382 -15.520  1.00 25.09           C  
-ANISOU 2935  CG2 ILE B 182     2933   4078   2524    -68    199    149       C  
-ATOM   2936  CD1 ILE B 182       6.676  -4.663 -16.950  1.00 28.59           C  
-ANISOU 2936  CD1 ILE B 182     3578   4603   2682    -49    162    -46       C  
-ATOM   2937  N   PRO B 183      10.866  -3.510 -18.920  1.00 28.52           N  
-ANISOU 2937  N   PRO B 183     3480   4926   2431   -320    892     10       N  
-ATOM   2938  CA  PRO B 183      11.264  -4.222 -20.140  1.00 33.05           C  
-ANISOU 2938  CA  PRO B 183     4192   5614   2750   -381   1153   -113       C  
-ATOM   2939  C   PRO B 183      10.195  -5.234 -20.539  1.00 31.77           C  
-ANISOU 2939  C   PRO B 183     4244   5413   2413   -346   1045   -249       C  
-ATOM   2940  O   PRO B 183       9.258  -5.482 -19.785  1.00 34.04           O  
-ANISOU 2940  O   PRO B 183     4503   5596   2834   -257    801   -247       O  
-ATOM   2941  CB  PRO B 183      12.534  -4.976 -19.723  1.00 38.29           C  
-ANISOU 2941  CB  PRO B 183     4594   6306   3650   -250   1426   -257       C  
-ATOM   2942  CG  PRO B 183      12.890  -4.483 -18.337  1.00 31.46           C  
-ANISOU 2942  CG  PRO B 183     3462   5362   3128   -174   1258   -159       C  
-ATOM   2943  CD  PRO B 183      11.653  -3.922 -17.739  1.00 29.87           C  
-ANISOU 2943  CD  PRO B 183     3384   5052   2914   -180    933    -60       C  
-ATOM   2944  N   ASP B 184      10.365  -5.840 -21.702  1.00 37.58           N  
-ANISOU 2944  N   ASP B 184     5198   6229   2851   -430   1247   -379       N  
-ATOM   2945  CA  ASP B 184       9.451  -6.867 -22.170  1.00 42.28           C  
-ANISOU 2945  CA  ASP B 184     6029   6777   3257   -437   1146   -535       C  
-ATOM   2946  C   ASP B 184       9.797  -8.198 -21.503  1.00 38.31           C  
-ANISOU 2946  C   ASP B 184     5393   6170   2992   -231   1278   -767       C  
-ATOM   2947  O   ASP B 184      10.306  -9.113 -22.145  1.00 45.55           O  
-ANISOU 2947  O   ASP B 184     6429   7086   3792   -204   1550   -987       O  
-ATOM   2948  CB  ASP B 184       9.545  -6.983 -23.695  1.00 47.16           C  
-ANISOU 2948  CB  ASP B 184     6999   7501   3418   -633   1311   -601       C  
-ATOM   2949  CG  ASP B 184       8.445  -7.846 -24.296  1.00 54.55           C  
-ANISOU 2949  CG  ASP B 184     8219   8359   4151   -690   1090   -708       C  
-ATOM   2950  OD1 ASP B 184       7.536  -8.281 -23.557  1.00 55.72           O  
-ANISOU 2950  OD1 ASP B 184     8304   8425   4444   -634    838   -731       O  
-ATOM   2951  OD2 ASP B 184       8.495  -8.069 -25.526  1.00 61.97           O  
-ANISOU 2951  OD2 ASP B 184     9419   9310   4816   -794   1150   -755       O  
-ATOM   2952  N   LYS B 185       9.532  -8.274 -20.208  1.00 35.33           N  
-ANISOU 2952  N   LYS B 185     4791   5689   2944    -87   1095   -713       N  
-ATOM   2953  CA  LYS B 185       9.710  -9.492 -19.425  1.00 39.51           C  
-ANISOU 2953  CA  LYS B 185     5208   6085   3717     98   1136   -873       C  
-ATOM   2954  C   LYS B 185       8.360  -9.863 -18.833  1.00 35.50           C  
-ANISOU 2954  C   LYS B 185     4763   5471   3256     96    828   -844       C  
-ATOM   2955  O   LYS B 185       7.558  -8.986 -18.538  1.00 35.42           O  
-ANISOU 2955  O   LYS B 185     4730   5482   3248     27    604   -671       O  
-ATOM   2956  CB  LYS B 185      10.698  -9.249 -18.280  1.00 42.91           C  
-ANISOU 2956  CB  LYS B 185     5311   6494   4499    244   1184   -801       C  
-ATOM   2957  CG  LYS B 185      12.155  -9.279 -18.687  1.00 56.46           C  
-ANISOU 2957  CG  LYS B 185     6862   8286   6303    296   1518   -864       C  
-ATOM   2958  CD  LYS B 185      13.052  -8.972 -17.498  1.00 60.63           C  
-ANISOU 2958  CD  LYS B 185     7045   8792   7199    405   1467   -752       C  
-ATOM   2959  CE  LYS B 185      14.520  -9.047 -17.902  1.00 68.06           C  
-ANISOU 2959  CE  LYS B 185     7741   9813   8304    463   1801   -800       C  
-ATOM   2960  NZ  LYS B 185      15.320  -7.930 -17.314  1.00 70.27           N  
-ANISOU 2960  NZ  LYS B 185     7746  10175   8777    389   1738   -601       N  
-ATOM   2961  N   PHE B 186       8.107 -11.149 -18.619  1.00 37.04           N  
-ANISOU 2961  N   PHE B 186     5020   5533   3523    174    831  -1006       N  
-ATOM   2962  CA  PHE B 186       6.840 -11.536 -18.001  1.00 34.14           C  
-ANISOU 2962  CA  PHE B 186     4678   5066   3228    147    564   -963       C  
-ATOM   2963  C   PHE B 186       6.888 -11.376 -16.485  1.00 32.85           C  
-ANISOU 2963  C   PHE B 186     4285   4836   3360    269    477   -849       C  
-ATOM   2964  O   PHE B 186       7.686 -12.014 -15.808  1.00 31.62           O  
-ANISOU 2964  O   PHE B 186     4026   4593   3396    409    571   -903       O  
-ATOM   2965  CB  PHE B 186       6.436 -12.961 -18.382  1.00 38.18           C  
-ANISOU 2965  CB  PHE B 186     5385   5438   3683    133    571  -1165       C  
-ATOM   2966  CG  PHE B 186       4.973 -13.243 -18.170  1.00 39.76           C  
-ANISOU 2966  CG  PHE B 186     5645   5579   3883     12    287  -1108       C  
-ATOM   2967  CD1 PHE B 186       4.502 -13.648 -16.935  1.00 37.24           C  
-ANISOU 2967  CD1 PHE B 186     5183   5149   3819     80    183  -1042       C  
-ATOM   2968  CD2 PHE B 186       4.070 -13.106 -19.222  1.00 45.93           C  
-ANISOU 2968  CD2 PHE B 186     6623   6421   4405   -191    119  -1106       C  
-ATOM   2969  CE1 PHE B 186       3.149 -13.906 -16.739  1.00 38.48           C  
-ANISOU 2969  CE1 PHE B 186     5349   5263   4009    -45    -39   -981       C  
-ATOM   2970  CE2 PHE B 186       2.722 -13.362 -19.037  1.00 46.72           C  
-ANISOU 2970  CE2 PHE B 186     6715   6475   4561   -311   -157  -1034       C  
-ATOM   2971  CZ  PHE B 186       2.261 -13.766 -17.791  1.00 40.84           C  
-ANISOU 2971  CZ  PHE B 186     5785   5625   4108   -235   -212   -977       C  
-ATOM   2972  N   VAL B 187       6.032 -10.518 -15.951  1.00 24.47           N  
-ANISOU 2972  N   VAL B 187     3157   3803   2336    215    294   -689       N  
-ATOM   2973  CA  VAL B 187       6.052 -10.240 -14.524  1.00 23.23           C  
-ANISOU 2973  CA  VAL B 187     2843   3592   2392    300    237   -594       C  
-ATOM   2974  C   VAL B 187       4.729 -10.685 -13.905  1.00 26.99           C  
-ANISOU 2974  C   VAL B 187     3332   3987   2936    263     93   -565       C  
-ATOM   2975  O   VAL B 187       3.714 -10.779 -14.590  1.00 25.75           O  
-ANISOU 2975  O   VAL B 187     3243   3846   2694    159    -14   -563       O  
-ATOM   2976  CB  VAL B 187       6.301  -8.736 -14.241  1.00 28.50           C  
-ANISOU 2976  CB  VAL B 187     3415   4337   3078    281    212   -449       C  
-ATOM   2977  CG1 VAL B 187       7.692  -8.321 -14.706  1.00 28.21           C  
-ANISOU 2977  CG1 VAL B 187     3322   4379   3019    292    368   -456       C  
-ATOM   2978  CG2 VAL B 187       5.247  -7.891 -14.925  1.00 31.05           C  
-ANISOU 2978  CG2 VAL B 187     3797   4707   3294    179     86   -353       C  
-ATOM   2979  N   VAL B 188       4.745 -10.977 -12.614  1.00 25.71           N  
-ANISOU 2979  N   VAL B 188     3103   3742   2924    327     83   -531       N  
-ATOM   2980  CA  VAL B 188       3.553 -11.429 -11.914  1.00 25.26           C  
-ANISOU 2980  CA  VAL B 188     3045   3613   2940    278      3   -495       C  
-ATOM   2981  C   VAL B 188       3.557 -10.765 -10.551  1.00 23.10           C  
-ANISOU 2981  C   VAL B 188     2702   3325   2750    317     17   -401       C  
-ATOM   2982  O   VAL B 188       4.569 -10.194 -10.152  1.00 25.10           O  
-ANISOU 2982  O   VAL B 188     2929   3600   3008    374     47   -377       O  
-ATOM   2983  CB  VAL B 188       3.561 -12.958 -11.722  1.00 22.90           C  
-ANISOU 2983  CB  VAL B 188     2836   3175   2691    282      8   -581       C  
-ATOM   2984  CG1 VAL B 188       3.437 -13.682 -13.062  1.00 24.80           C  
-ANISOU 2984  CG1 VAL B 188     3204   3396   2822    220      0   -715       C  
-ATOM   2985  CG2 VAL B 188       4.828 -13.406 -10.981  1.00 27.27           C  
-ANISOU 2985  CG2 VAL B 188     3377   3649   3334    410     67   -589       C  
-ATOM   2986  N   GLY B 189       2.441 -10.829  -9.835  1.00 19.13           N  
-ANISOU 2986  N   GLY B 189     2175   2786   2309    269      5   -353       N  
-ATOM   2987  CA  GLY B 189       2.405 -10.276  -8.490  1.00 19.35           C  
-ANISOU 2987  CA  GLY B 189     2197   2788   2366    288     60   -294       C  
-ATOM   2988  C   GLY B 189       1.637  -8.964  -8.468  1.00 21.24           C  
-ANISOU 2988  C   GLY B 189     2353   3072   2646    291     90   -248       C  
-ATOM   2989  O   GLY B 189       1.380  -8.399  -9.529  1.00 21.35           O  
-ANISOU 2989  O   GLY B 189     2305   3141   2666    289     28   -230       O  
-ATOM   2990  N   TYR B 190       1.288  -8.482  -7.272  1.00 20.46           N  
-ANISOU 2990  N   TYR B 190     2274   2932   2567    296    186   -229       N  
-ATOM   2991  CA  TYR B 190       0.429  -7.290  -7.108  1.00 22.77           C  
-ANISOU 2991  CA  TYR B 190     2482   3219   2952    329    261   -206       C  
-ATOM   2992  C   TYR B 190      -0.817  -7.408  -8.001  1.00 26.08           C  
-ANISOU 2992  C   TYR B 190     2723   3669   3517    313    209   -163       C  
-ATOM   2993  O   TYR B 190      -1.197  -6.465  -8.712  1.00 22.84           O  
-ANISOU 2993  O   TYR B 190     2212   3271   3195    357    145   -113       O  
-ATOM   2994  CB  TYR B 190       1.228  -6.008  -7.387  1.00 16.97           C  
-ANISOU 2994  CB  TYR B 190     1780   2483   2185    378    223   -199       C  
-ATOM   2995  CG  TYR B 190       0.594  -4.728  -6.892  1.00 22.70           C  
-ANISOU 2995  CG  TYR B 190     2485   3134   3008    435    322   -199       C  
-ATOM   2996  CD1 TYR B 190       0.481  -4.452  -5.527  1.00 20.68           C  
-ANISOU 2996  CD1 TYR B 190     2346   2801   2709    434    480   -261       C  
-ATOM   2997  CD2 TYR B 190       0.125  -3.787  -7.787  1.00 23.20           C  
-ANISOU 2997  CD2 TYR B 190     2439   3181   3195    488    258   -137       C  
-ATOM   2998  CE1 TYR B 190      -0.098  -3.270  -5.082  1.00 20.76           C  
-ANISOU 2998  CE1 TYR B 190     2361   2710   2819    503    614   -299       C  
-ATOM   2999  CE2 TYR B 190      -0.450  -2.599  -7.355  1.00 20.49           C  
-ANISOU 2999  CE2 TYR B 190     2071   2722   2992    573    354   -141       C  
-ATOM   3000  CZ  TYR B 190      -0.556  -2.348  -6.001  1.00 21.24           C  
-ANISOU 3000  CZ  TYR B 190     2279   2729   3060    589    553   -240       C  
-ATOM   3001  OH  TYR B 190      -1.126  -1.164  -5.580  1.00 22.23           O  
-ANISOU 3001  OH  TYR B 190     2403   2708   3335    690    689   -280       O  
-ATOM   3002  N   ALA B 191      -1.431  -8.599  -7.958  1.00 22.12           N  
-ANISOU 3002  N   ALA B 191     2189   3166   3050    232    205   -164       N  
-ATOM   3003  CA  ALA B 191      -2.660  -8.950  -8.701  1.00 22.07           C  
-ANISOU 3003  CA  ALA B 191     2002   3188   3196    166    117   -115       C  
-ATOM   3004  C   ALA B 191      -2.480  -9.374 -10.167  1.00 22.19           C  
-ANISOU 3004  C   ALA B 191     2048   3250   3134    102   -103   -118       C  
-ATOM   3005  O   ALA B 191      -3.430  -9.868 -10.776  1.00 23.13           O  
-ANISOU 3005  O   ALA B 191     2058   3385   3346      1   -229    -82       O  
-ATOM   3006  CB  ALA B 191      -3.774  -7.862  -8.565  1.00 24.68           C  
-ANISOU 3006  CB  ALA B 191     2104   3516   3756    234    179    -46       C  
-ATOM   3007  N   LEU B 192      -1.279  -9.193 -10.715  1.00 23.16           N  
-ANISOU 3007  N   LEU B 192     2322   3395   3083    140   -140   -164       N  
-ATOM   3008  CA  LEU B 192      -0.962  -9.684 -12.060  1.00 26.05           C  
-ANISOU 3008  CA  LEU B 192     2787   3802   3309     68   -282   -204       C  
-ATOM   3009  C   LEU B 192      -0.706 -11.185 -11.986  1.00 26.30           C  
-ANISOU 3009  C   LEU B 192     2940   3765   3288      7   -265   -308       C  
-ATOM   3010  O   LEU B 192       0.018 -11.651 -11.093  1.00 23.77           O  
-ANISOU 3010  O   LEU B 192     2685   3379   2966     67   -152   -346       O  
-ATOM   3011  CB  LEU B 192       0.279  -8.989 -12.629  1.00 23.91           C  
-ANISOU 3011  CB  LEU B 192     2621   3581   2882    125   -257   -222       C  
-ATOM   3012  CG  LEU B 192       0.120  -7.556 -13.134  1.00 33.81           C  
-ANISOU 3012  CG  LEU B 192     3819   4880   4148    148   -326   -109       C  
-ATOM   3013  CD1 LEU B 192       0.161  -6.560 -11.986  1.00 31.13           C  
-ANISOU 3013  CD1 LEU B 192     3402   4484   3944    252   -215    -68       C  
-ATOM   3014  CD2 LEU B 192       1.176  -7.220 -14.185  1.00 40.18           C  
-ANISOU 3014  CD2 LEU B 192     4764   5755   4747    117   -333   -120       C  
-ATOM   3015  N   ASP B 193      -1.256 -11.934 -12.934  1.00 26.67           N  
-ANISOU 3015  N   ASP B 193     3039   3805   3290   -120   -404   -347       N  
-ATOM   3016  CA  ASP B 193      -1.239 -13.389 -12.829  1.00 22.36           C  
-ANISOU 3016  CA  ASP B 193     2616   3143   2738   -195   -401   -446       C  
-ATOM   3017  C   ASP B 193      -0.471 -14.112 -13.933  1.00 25.69           C  
-ANISOU 3017  C   ASP B 193     3265   3525   2969   -222   -423   -601       C  
-ATOM   3018  O   ASP B 193      -0.162 -13.554 -14.990  1.00 25.56           O  
-ANISOU 3018  O   ASP B 193     3325   3602   2785   -239   -466   -627       O  
-ATOM   3019  CB  ASP B 193      -2.667 -13.941 -12.824  1.00 24.05           C  
-ANISOU 3019  CB  ASP B 193     2719   3327   3092   -365   -529   -390       C  
-ATOM   3020  CG  ASP B 193      -3.308 -13.903 -14.198  1.00 30.63           C  
-ANISOU 3020  CG  ASP B 193     3578   4219   3842   -515   -768   -392       C  
-ATOM   3021  OD1 ASP B 193      -3.293 -12.829 -14.826  1.00 29.75           O  
-ANISOU 3021  OD1 ASP B 193     3417   4218   3667   -478   -849   -320       O  
-ATOM   3022  OD2 ASP B 193      -3.814 -14.949 -14.655  1.00 29.45           O  
-ANISOU 3022  OD2 ASP B 193     3522   3989   3677   -689   -899   -456       O  
-ATOM   3023  N   TYR B 194      -0.195 -15.384 -13.669  1.00 24.08           N  
-ANISOU 3023  N   TYR B 194     3192   3163   2793   -233   -379   -705       N  
-ATOM   3024  CA  TYR B 194       0.192 -16.332 -14.708  1.00 27.17           C  
-ANISOU 3024  CA  TYR B 194     3823   3459   3042   -290   -394   -890       C  
-ATOM   3025  C   TYR B 194      -0.773 -17.480 -14.514  1.00 28.75           C  
-ANISOU 3025  C   TYR B 194     4079   3502   3343   -458   -512   -909       C  
-ATOM   3026  O   TYR B 194      -0.709 -18.188 -13.506  1.00 29.28           O  
-ANISOU 3026  O   TYR B 194     4137   3424   3562   -423   -449   -878       O  
-ATOM   3027  CB  TYR B 194       1.633 -16.797 -14.507  1.00 29.27           C  
-ANISOU 3027  CB  TYR B 194     4183   3626   3312   -100   -200  -1005       C  
-ATOM   3028  CG  TYR B 194       2.059 -17.891 -15.469  1.00 30.13           C  
-ANISOU 3028  CG  TYR B 194     4551   3584   3313   -122   -148  -1234       C  
-ATOM   3029  CD1 TYR B 194       2.248 -17.618 -16.812  1.00 32.36           C  
-ANISOU 3029  CD1 TYR B 194     4996   3959   3341   -192   -124  -1362       C  
-ATOM   3030  CD2 TYR B 194       2.261 -19.194 -15.029  1.00 30.49           C  
-ANISOU 3030  CD2 TYR B 194     4712   3373   3500    -80   -114  -1325       C  
-ATOM   3031  CE1 TYR B 194       2.634 -18.606 -17.696  1.00 41.41           C  
-ANISOU 3031  CE1 TYR B 194     6425   4954   4356   -217    -32  -1610       C  
-ATOM   3032  CE2 TYR B 194       2.654 -20.187 -15.902  1.00 35.50           C  
-ANISOU 3032  CE2 TYR B 194     5607   3827   4055    -81    -38  -1565       C  
-ATOM   3033  CZ  TYR B 194       2.837 -19.890 -17.234  1.00 41.52           C  
-ANISOU 3033  CZ  TYR B 194     6539   4692   4544   -149     19  -1725       C  
-ATOM   3034  OH  TYR B 194       3.224 -20.882 -18.112  1.00 46.25           O  
-ANISOU 3034  OH  TYR B 194     7443   5098   5032   -156    137  -2003       O  
-ATOM   3035  N   ASN B 195      -1.699 -17.628 -15.457  1.00 29.57           N  
-ANISOU 3035  N   ASN B 195     4242   3634   3360   -669   -711   -934       N  
-ATOM   3036  CA AASN B 195      -2.763 -18.626 -15.362  0.59 31.58           C  
-ANISOU 3036  CA AASN B 195     4518   3754   3729   -888   -868   -931       C  
-ATOM   3037  CA BASN B 195      -2.747 -18.642 -15.356  0.41 31.58           C  
-ANISOU 3037  CA BASN B 195     4521   3751   3729   -887   -865   -933       C  
-ATOM   3038  C   ASN B 195      -3.486 -18.620 -14.011  1.00 30.68           C  
-ANISOU 3038  C   ASN B 195     4147   3628   3881   -902   -824   -747       C  
-ATOM   3039  O   ASN B 195      -3.729 -19.668 -13.408  1.00 31.70           O  
-ANISOU 3039  O   ASN B 195     4340   3576   4130   -990   -807   -751       O  
-ATOM   3040  CB AASN B 195      -2.230 -20.014 -15.716  0.59 38.31           C  
-ANISOU 3040  CB AASN B 195     5691   4351   4513   -923   -829  -1149       C  
-ATOM   3041  CB BASN B 195      -2.181 -20.038 -15.617  0.41 37.61           C  
-ANISOU 3041  CB BASN B 195     5596   4254   4439   -908   -813  -1145       C  
-ATOM   3042  CG AASN B 195      -1.780 -20.104 -17.162  0.59 42.10           C  
-ANISOU 3042  CG AASN B 195     6462   4839   4696   -975   -859  -1361       C  
-ATOM   3043  CG BASN B 195      -3.266 -21.076 -15.779  0.41 42.66           C  
-ANISOU 3043  CG BASN B 195     6319   4733   5157  -1191  -1014  -1167       C  
-ATOM   3044  OD1AASN B 195      -2.300 -19.400 -18.027  0.59 45.33           O  
-ANISOU 3044  OD1AASN B 195     6865   5421   4935  -1111  -1031  -1318       O  
-ATOM   3045  OD1BASN B 195      -4.305 -20.806 -16.378  0.41 46.02           O  
-ANISOU 3045  OD1BASN B 195     6662   5266   5557  -1415  -1252  -1102       O  
-ATOM   3046  ND2AASN B 195      -0.812 -20.971 -17.432  0.59 45.95           N  
-ANISOU 3046  ND2AASN B 195     7213   5127   5118   -866   -685  -1586       N  
-ATOM   3047  ND2BASN B 195      -3.049 -22.258 -15.213  0.41 45.58           N  
-ANISOU 3047  ND2BASN B 195     6837   4833   5650  -1194   -946  -1232       N  
-ATOM   3048  N   GLU B 196      -3.815 -17.413 -13.545  1.00 29.11           N  
-ANISOU 3048  N   GLU B 196     3684   3611   3766   -819   -785   -589       N  
-ATOM   3049  CA  GLU B 196      -4.563 -17.174 -12.297  1.00 28.66           C  
-ANISOU 3049  CA  GLU B 196     3375   3579   3934   -827   -685   -426       C  
-ATOM   3050  C   GLU B 196      -3.728 -17.251 -11.024  1.00 34.27           C  
-ANISOU 3050  C   GLU B 196     4145   4223   4653   -666   -457   -405       C  
-ATOM   3051  O   GLU B 196      -4.181 -16.832  -9.962  1.00 32.68           O  
-ANISOU 3051  O   GLU B 196     3786   4067   4563   -651   -325   -286       O  
-ATOM   3052  CB  GLU B 196      -5.822 -18.042 -12.184  1.00 31.21           C  
-ANISOU 3052  CB  GLU B 196     3596   3824   4436  -1084   -799   -365       C  
-ATOM   3053  CG  GLU B 196      -6.874 -17.750 -13.246  1.00 39.08           C  
-ANISOU 3053  CG  GLU B 196     4437   4923   5488  -1266  -1075   -318       C  
-ATOM   3054  CD  GLU B 196      -7.302 -16.289 -13.258  1.00 39.74           C  
-ANISOU 3054  CD  GLU B 196     4219   5202   5679  -1143  -1081   -178       C  
-ATOM   3055  OE1 GLU B 196      -7.288 -15.652 -12.185  1.00 36.66           O  
-ANISOU 3055  OE1 GLU B 196     3661   4855   5413   -990   -843   -100       O  
-ATOM   3056  OE2 GLU B 196      -7.655 -15.777 -14.339  1.00 42.92           O  
-ANISOU 3056  OE2 GLU B 196     4580   5697   6033  -1206  -1333   -146       O  
-ATOM   3057  N   TYR B 197      -2.499 -17.752 -11.130  1.00 26.29           N  
-ANISOU 3057  N   TYR B 197     3361   3105   3525   -545   -409   -519       N  
-ATOM   3058  CA  TYR B 197      -1.611 -17.787  -9.982  1.00 25.03           C  
-ANISOU 3058  CA  TYR B 197     3254   2885   3374   -395   -264   -473       C  
-ATOM   3059  C   TYR B 197      -0.806 -16.497  -9.837  1.00 23.42           C  
-ANISOU 3059  C   TYR B 197     2971   2834   3094   -214   -184   -454       C  
-ATOM   3060  O   TYR B 197      -0.692 -15.714 -10.791  1.00 22.73           O  
-ANISOU 3060  O   TYR B 197     2837   2870   2930   -181   -227   -498       O  
-ATOM   3061  CB  TYR B 197      -0.680 -19.000 -10.049  1.00 25.98           C  
-ANISOU 3061  CB  TYR B 197     3603   2781   3486   -335   -269   -574       C  
-ATOM   3062  CG  TYR B 197      -1.396 -20.297  -9.777  1.00 32.75           C  
-ANISOU 3062  CG  TYR B 197     4570   3429   4444   -517   -330   -555       C  
-ATOM   3063  CD1 TYR B 197      -1.512 -20.785  -8.484  1.00 32.21           C  
-ANISOU 3063  CD1 TYR B 197     4534   3249   4453   -556   -274   -408       C  
-ATOM   3064  CD2 TYR B 197      -1.979 -21.025 -10.809  1.00 37.69           C  
-ANISOU 3064  CD2 TYR B 197     5296   3959   5066   -683   -455   -674       C  
-ATOM   3065  CE1 TYR B 197      -2.176 -21.968  -8.224  1.00 39.84           C  
-ANISOU 3065  CE1 TYR B 197     5612   4008   5518   -751   -326   -365       C  
-ATOM   3066  CE2 TYR B 197      -2.645 -22.218 -10.560  1.00 42.97           C  
-ANISOU 3066  CE2 TYR B 197     6074   4409   5844   -882   -525   -652       C  
-ATOM   3067  CZ  TYR B 197      -2.743 -22.680  -9.264  1.00 45.07           C  
-ANISOU 3067  CZ  TYR B 197     6349   4562   6212   -913   -452   -489       C  
-ATOM   3068  OH  TYR B 197      -3.401 -23.855  -9.000  1.00 51.65           O  
-ANISOU 3068  OH  TYR B 197     7300   5165   7159  -1135   -516   -442       O  
-ATOM   3069  N   PHE B 198      -0.263 -16.302  -8.637  1.00 22.13           N  
-ANISOU 3069  N   PHE B 198     2821   2650   2937   -127    -89   -376       N  
-ATOM   3070  CA  PHE B 198       0.589 -15.167  -8.270  1.00 20.55           C  
-ANISOU 3070  CA  PHE B 198     2576   2558   2675     15    -30   -352       C  
-ATOM   3071  C   PHE B 198      -0.159 -13.868  -8.015  1.00 23.18           C  
-ANISOU 3071  C   PHE B 198     2757   3031   3019      3     30   -289       C  
-ATOM   3072  O   PHE B 198       0.480 -12.836  -7.818  1.00 24.02           O  
-ANISOU 3072  O   PHE B 198     2843   3209   3075    100     65   -281       O  
-ATOM   3073  CB  PHE B 198       1.692 -14.898  -9.311  1.00 20.09           C  
-ANISOU 3073  CB  PHE B 198     2539   2541   2551    130    -54   -453       C  
-ATOM   3074  CG  PHE B 198       2.588 -16.069  -9.580  1.00 24.91           C  
-ANISOU 3074  CG  PHE B 198     3275   2997   3191    199    -63   -542       C  
-ATOM   3075  CD1 PHE B 198       3.602 -16.405  -8.698  1.00 21.28           C  
-ANISOU 3075  CD1 PHE B 198     2846   2445   2796    313    -59   -491       C  
-ATOM   3076  CD2 PHE B 198       2.443 -16.809 -10.745  1.00 27.29           C  
-ANISOU 3076  CD2 PHE B 198     3674   3233   3463    155    -86   -680       C  
-ATOM   3077  CE1 PHE B 198       4.437 -17.485  -8.957  1.00 25.95           C  
-ANISOU 3077  CE1 PHE B 198     3516   2861   3482    416    -64   -566       C  
-ATOM   3078  CE2 PHE B 198       3.275 -17.889 -11.013  1.00 34.75           C  
-ANISOU 3078  CE2 PHE B 198     4743   3997   4463    248    -54   -793       C  
-ATOM   3079  CZ  PHE B 198       4.280 -18.222 -10.116  1.00 31.39           C  
-ANISOU 3079  CZ  PHE B 198     4300   3465   4163    399    -35   -731       C  
-ATOM   3080  N   ARG B 199      -1.490 -13.886  -8.051  1.00 20.89           N  
-ANISOU 3080  N   ARG B 199     2343   2766   2830   -110     40   -246       N  
-ATOM   3081  CA  ARG B 199      -2.212 -12.658  -7.727  1.00 21.56           C  
-ANISOU 3081  CA  ARG B 199     2256   2949   2988    -80    129   -189       C  
-ATOM   3082  C   ARG B 199      -2.048 -12.364  -6.251  1.00 27.26           C  
-ANISOU 3082  C   ARG B 199     3050   3644   3662    -55    309   -154       C  
-ATOM   3083  O   ARG B 199      -2.104 -11.201  -5.833  1.00 25.31           O  
-ANISOU 3083  O   ARG B 199     2756   3444   3417     21    412   -152       O  
-ATOM   3084  CB  ARG B 199      -3.691 -12.737  -8.097  1.00 22.54           C  
-ANISOU 3084  CB  ARG B 199     2163   3107   3294   -193    100   -135       C  
-ATOM   3085  CG  ARG B 199      -3.961 -12.898  -9.615  1.00 23.17           C  
-ANISOU 3085  CG  ARG B 199     2198   3224   3382   -257   -135   -157       C  
-ATOM   3086  CD  ARG B 199      -5.399 -12.521  -9.956  1.00 25.11           C  
-ANISOU 3086  CD  ARG B 199     2156   3531   3855   -338   -212    -61       C  
-ATOM   3087  NE  ARG B 199      -5.880 -13.028 -11.245  1.00 26.64           N  
-ANISOU 3087  NE  ARG B 199     2335   3740   4047   -486   -488    -61       N  
-ATOM   3088  CZ  ARG B 199      -5.714 -12.397 -12.408  1.00 28.24           C  
-ANISOU 3088  CZ  ARG B 199     2565   4011   4155   -468   -685    -52       C  
-ATOM   3089  NH1 ARG B 199      -5.070 -11.242 -12.445  1.00 25.38           N  
-ANISOU 3089  NH1 ARG B 199     2221   3696   3725   -302   -625    -34       N  
-ATOM   3090  NH2 ARG B 199      -6.191 -12.923 -13.532  1.00 29.82           N  
-ANISOU 3090  NH2 ARG B 199     2802   4220   4306   -642   -954    -55       N  
-ATOM   3091  N   ASP B 200      -1.824 -13.429  -5.481  1.00 22.69           N  
-ANISOU 3091  N   ASP B 200     2625   2969   3025   -130    334   -126       N  
-ATOM   3092  CA  ASP B 200      -1.678 -13.358  -4.024  1.00 23.98           C  
-ANISOU 3092  CA  ASP B 200     2933   3099   3079   -159    481    -73       C  
-ATOM   3093  C   ASP B 200      -0.228 -13.128  -3.620  1.00 27.14           C  
-ANISOU 3093  C   ASP B 200     3511   3472   3328    -66    388    -81       C  
-ATOM   3094  O   ASP B 200       0.311 -13.802  -2.741  1.00 28.86           O  
-ANISOU 3094  O   ASP B 200     3918   3605   3444   -110    352    -15       O  
-ATOM   3095  CB  ASP B 200      -2.183 -14.648  -3.370  1.00 25.16           C  
-ANISOU 3095  CB  ASP B 200     3183   3146   3231   -320    523      7       C  
-ATOM   3096  CG  ASP B 200      -1.503 -15.893  -3.916  1.00 26.85           C  
-ANISOU 3096  CG  ASP B 200     3515   3225   3460   -326    328      3       C  
-ATOM   3097  OD1 ASP B 200      -1.106 -15.895  -5.102  1.00 24.46           O  
-ANISOU 3097  OD1 ASP B 200     3150   2934   3211   -243    199    -86       O  
-ATOM   3098  OD2 ASP B 200      -1.387 -16.882  -3.154  1.00 29.55           O  
-ANISOU 3098  OD2 ASP B 200     4034   3433   3759   -418    317     91       O  
-ATOM   3099  N   LEU B 201       0.407 -12.185  -4.295  1.00 27.58           N  
-ANISOU 3099  N   LEU B 201     3495   3597   3386     48    326   -139       N  
-ATOM   3100  CA  LEU B 201       1.802 -11.836  -4.045  1.00 27.54           C  
-ANISOU 3100  CA  LEU B 201     3588   3586   3288    124    225   -140       C  
-ATOM   3101  C   LEU B 201       1.853 -10.315  -4.051  1.00 26.34           C  
-ANISOU 3101  C   LEU B 201     3387   3510   3112    172    283   -178       C  
-ATOM   3102  O   LEU B 201       1.286  -9.693  -4.943  1.00 29.62           O  
-ANISOU 3102  O   LEU B 201     3654   3980   3621    209    308   -208       O  
-ATOM   3103  CB  LEU B 201       2.681 -12.440  -5.136  1.00 27.16           C  
-ANISOU 3103  CB  LEU B 201     3489   3522   3308    203     92   -178       C  
-ATOM   3104  CG  LEU B 201       4.141 -12.021  -5.267  1.00 27.30           C  
-ANISOU 3104  CG  LEU B 201     3495   3562   3314    297      0   -184       C  
-ATOM   3105  CD1 LEU B 201       4.902 -12.429  -4.037  1.00 29.43           C  
-ANISOU 3105  CD1 LEU B 201     3895   3752   3536    284    -95    -95       C  
-ATOM   3106  CD2 LEU B 201       4.736 -12.681  -6.510  1.00 27.04           C  
-ANISOU 3106  CD2 LEU B 201     3389   3518   3368    376    -35   -254       C  
-ATOM   3107  N   ASN B 202       2.482  -9.710  -3.044  1.00 22.40           N  
-ANISOU 3107  N   ASN B 202     3032   2992   2485    156    282   -168       N  
-ATOM   3108  CA  ASN B 202       2.437  -8.247  -2.926  1.00 23.34           C  
-ANISOU 3108  CA  ASN B 202     3151   3135   2584    183    353   -220       C  
-ATOM   3109  C   ASN B 202       3.464  -7.532  -3.816  1.00 22.55           C  
-ANISOU 3109  C   ASN B 202     2964   3074   2529    245    220   -228       C  
-ATOM   3110  O   ASN B 202       3.237  -6.399  -4.245  1.00 26.65           O  
-ANISOU 3110  O   ASN B 202     3426   3602   3098    279    263   -256       O  
-ATOM   3111  CB  ASN B 202       2.520  -7.791  -1.453  1.00 28.22           C  
-ANISOU 3111  CB  ASN B 202     4010   3699   3011    101    433   -235       C  
-ATOM   3112  CG  ASN B 202       3.876  -8.109  -0.794  1.00 34.59           C  
-ANISOU 3112  CG  ASN B 202     4983   4482   3677     43    216   -175       C  
-ATOM   3113  OD1 ASN B 202       4.602  -9.002  -1.233  1.00 41.12           O  
-ANISOU 3113  OD1 ASN B 202     5732   5313   4580     77     50   -108       O  
-ATOM   3114  ND2 ASN B 202       4.207  -7.373   0.277  1.00 33.70           N  
-ANISOU 3114  ND2 ASN B 202     5103   4332   3371    -47    211   -202       N  
-ATOM   3115  N   HIS B 203       4.577  -8.210  -4.105  1.00 20.73           N  
-ANISOU 3115  N   HIS B 203     2713   2857   2306    260     74   -195       N  
-ATOM   3116  CA  HIS B 203       5.642  -7.635  -4.931  1.00 20.56           C  
-ANISOU 3116  CA  HIS B 203     2586   2888   2338    299    -11   -194       C  
-ATOM   3117  C   HIS B 203       5.386  -7.976  -6.392  1.00 25.36           C  
-ANISOU 3117  C   HIS B 203     3057   3553   3024    352     19   -220       C  
-ATOM   3118  O   HIS B 203       4.747  -8.988  -6.692  1.00 26.59           O  
-ANISOU 3118  O   HIS B 203     3208   3691   3206    358     41   -239       O  
-ATOM   3119  CB  HIS B 203       7.002  -8.248  -4.532  1.00 19.42           C  
-ANISOU 3119  CB  HIS B 203     2438   2729   2212    305   -161   -142       C  
-ATOM   3120  CG  HIS B 203       7.317  -8.135  -3.070  1.00 18.53           C  
-ANISOU 3120  CG  HIS B 203     2503   2558   1979    218   -262    -92       C  
-ATOM   3121  ND1 HIS B 203       7.437  -6.927  -2.429  1.00 23.88           N  
-ANISOU 3121  ND1 HIS B 203     3297   3224   2551    134   -276   -112       N  
-ATOM   3122  CD2 HIS B 203       7.526  -9.093  -2.136  1.00 19.68           C  
-ANISOU 3122  CD2 HIS B 203     2772   2637   2069    185   -369    -17       C  
-ATOM   3123  CE1 HIS B 203       7.713  -7.139  -1.148  1.00 24.16           C  
-ANISOU 3123  CE1 HIS B 203     3538   3205   2436     36   -388    -66       C  
-ATOM   3124  NE2 HIS B 203       7.782  -8.439  -0.952  1.00 22.34           N  
-ANISOU 3124  NE2 HIS B 203     3310   2947   2233     65   -457     10       N  
-ATOM   3125  N   VAL B 204       5.897  -7.162  -7.314  1.00 20.30           N  
-ANISOU 3125  N   VAL B 204     2337   2976   2401    361     13   -219       N  
-ATOM   3126  CA  VAL B 204       5.949  -7.591  -8.710  1.00 21.67           C  
-ANISOU 3126  CA  VAL B 204     2437   3212   2584    384     35   -247       C  
-ATOM   3127  C   VAL B 204       7.265  -8.343  -8.896  1.00 24.39           C  
-ANISOU 3127  C   VAL B 204     2724   3568   2975    431     31   -269       C  
-ATOM   3128  O   VAL B 204       8.318  -7.857  -8.494  1.00 24.78           O  
-ANISOU 3128  O   VAL B 204     2714   3634   3069    427     -8   -227       O  
-ATOM   3129  CB  VAL B 204       5.844  -6.414  -9.690  1.00 22.06           C  
-ANISOU 3129  CB  VAL B 204     2454   3322   2604    353     45   -213       C  
-ATOM   3130  CG1 VAL B 204       6.105  -6.887 -11.127  1.00 23.10           C  
-ANISOU 3130  CG1 VAL B 204     2571   3534   2672    343     77   -246       C  
-ATOM   3131  CG2 VAL B 204       4.459  -5.770  -9.574  1.00 22.94           C  
-ANISOU 3131  CG2 VAL B 204     2577   3395   2744    348     39   -182       C  
-ATOM   3132  N   CYS B 205       7.194  -9.536  -9.485  1.00 20.55           N  
-ANISOU 3132  N   CYS B 205     2246   3057   2506    475     66   -336       N  
-ATOM   3133  CA  CYS B 205       8.349 -10.417  -9.552  1.00 22.24           C  
-ANISOU 3133  CA  CYS B 205     2392   3234   2825    564     87   -369       C  
-ATOM   3134  C   CYS B 205       8.412 -11.018 -10.935  1.00 28.29           C  
-ANISOU 3134  C   CYS B 205     3172   4023   3555    593    211   -487       C  
-ATOM   3135  O   CYS B 205       7.416 -11.024 -11.669  1.00 23.31           O  
-ANISOU 3135  O   CYS B 205     2641   3415   2800    521    220   -530       O  
-ATOM   3136  CB  CYS B 205       8.235 -11.526  -8.511  1.00 26.75           C  
-ANISOU 3136  CB  CYS B 205     3025   3666   3472    605      0   -343       C  
-ATOM   3137  N   VAL B 206       9.588 -11.527 -11.274  1.00 29.99           N  
-ANISOU 3137  N   VAL B 206     3284   4225   3885    692    306   -539       N  
-ATOM   3138  CA  VAL B 206       9.785 -12.229 -12.525  1.00 35.05           C  
-ANISOU 3138  CA  VAL B 206     3975   4861   4482    733    479   -692       C  
-ATOM   3139  C   VAL B 206       9.640 -13.713 -12.244  1.00 36.74           C  
-ANISOU 3139  C   VAL B 206     4267   4881   4811    831    461   -777       C  
-ATOM   3140  O   VAL B 206      10.254 -14.262 -11.318  1.00 36.90           O  
-ANISOU 3140  O   VAL B 206     4194   4786   5039    941    385   -715       O  
-ATOM   3141  CB  VAL B 206      11.161 -11.928 -13.145  1.00 38.46           C  
-ANISOU 3141  CB  VAL B 206     4232   5381   5000    798    668   -723       C  
-ATOM   3142  CG1 VAL B 206      11.420 -12.838 -14.339  1.00 40.61           C  
-ANISOU 3142  CG1 VAL B 206     4591   5616   5225    862    905   -923       C  
-ATOM   3143  CG2 VAL B 206      11.232 -10.466 -13.564  1.00 40.89           C  
-ANISOU 3143  CG2 VAL B 206     4505   5860   5170    661    688   -630       C  
-ATOM   3144  N   ILE B 207       8.800 -14.351 -13.047  1.00 36.81           N  
-ANISOU 3144  N   ILE B 207     4465   4837   4682    770    498   -904       N  
-ATOM   3145  CA  ILE B 207       8.502 -15.763 -12.901  1.00 33.94           C  
-ANISOU 3145  CA  ILE B 207     4229   4257   4410    823    476   -998       C  
-ATOM   3146  C   ILE B 207       9.683 -16.600 -13.386  1.00 40.04           C  
-ANISOU 3146  C   ILE B 207     4955   4909   5349   1010    667  -1145       C  
-ATOM   3147  O   ILE B 207      10.361 -16.227 -14.344  1.00 44.93           O  
-ANISOU 3147  O   ILE B 207     5529   5639   5902   1037    880  -1248       O  
-ATOM   3148  CB  ILE B 207       7.184 -16.084 -13.658  1.00 52.09           C  
-ANISOU 3148  CB  ILE B 207     6747   6540   6504    654    424  -1088       C  
-ATOM   3149  CG1 ILE B 207       6.684 -17.491 -13.354  1.00 53.03           C  
-ANISOU 3149  CG1 ILE B 207     7015   6411   6723    654    357  -1157       C  
-ATOM   3150  CG2 ILE B 207       7.332 -15.835 -15.168  1.00 56.32           C  
-ANISOU 3150  CG2 ILE B 207     7401   7183   6815    592    574  -1242       C  
-ATOM   3151  CD1 ILE B 207       5.309 -17.754 -13.933  1.00 49.87           C  
-ANISOU 3151  CD1 ILE B 207     6790   6002   6156    443    246  -1207       C  
-ATOM   3152  N   SER B 208       9.952 -17.714 -12.707  1.00 37.28           N  
-ANISOU 3152  N   SER B 208     4609   4323   5233   1142    609  -1143       N  
-ATOM   3153  CA  SER B 208      11.049 -18.588 -13.079  1.00 46.72           C  
-ANISOU 3153  CA  SER B 208     5732   5353   6669   1365    792  -1280       C  
-ATOM   3154  C   SER B 208      10.573 -19.633 -14.095  1.00 47.59           C  
-ANISOU 3154  C   SER B 208     6124   5280   6676   1352    935  -1541       C  
-ATOM   3155  O   SER B 208       9.377 -19.729 -14.382  1.00 42.85           O  
-ANISOU 3155  O   SER B 208     5758   4683   5841   1149    828  -1578       O  
-ATOM   3156  CB  SER B 208      11.622 -19.293 -11.851  1.00 48.70           C  
-ANISOU 3156  CB  SER B 208     5853   5394   7255   1531    621  -1127       C  
-ATOM   3157  OG  SER B 208      10.717 -20.257 -11.346  1.00 48.06           O  
-ANISOU 3157  OG  SER B 208     6004   5086   7172   1469    460  -1105       O  
-ATOM   3158  N   GLU B 209      11.507 -20.406 -14.639  1.00 53.64           N  
-ANISOU 3158  N   GLU B 209     6867   5884   7631   1559   1173  -1721       N  
-ATOM   3159  CA  GLU B 209      11.153 -21.444 -15.599  1.00 56.01           C  
-ANISOU 3159  CA  GLU B 209     7491   6004   7786   1533   1285  -1948       C  
-ATOM   3160  C   GLU B 209      10.337 -22.543 -14.931  1.00 55.98           C  
-ANISOU 3160  C   GLU B 209     7682   5673   7916   1506   1084  -1958       C  
-ATOM   3161  O   GLU B 209       9.330 -23.000 -15.480  1.00 52.29           O  
-ANISOU 3161  O   GLU B 209     7520   5110   7238   1317   1040  -2109       O  
-ATOM   3162  CB  GLU B 209      12.401 -22.018 -16.275  1.00 67.05           C  
-ANISOU 3162  CB  GLU B 209     8821   7356   9299   1752   1523  -2048       C  
-ATOM   3163  CG  GLU B 209      13.089 -21.038 -17.217  1.00 72.10           C  
-ANISOU 3163  CG  GLU B 209     9338   8306   9749   1718   1759  -2080       C  
-ATOM   3164  CD  GLU B 209      12.144 -20.492 -18.272  1.00 76.41           C  
-ANISOU 3164  CD  GLU B 209    10174   9019   9842   1449   1792  -2203       C  
-ATOM   3165  OE1 GLU B 209      12.259 -19.298 -18.620  1.00 76.72           O  
-ANISOU 3165  OE1 GLU B 209    10119   9333   9699   1331   1855  -2116       O  
-ATOM   3166  OE2 GLU B 209      11.283 -21.259 -18.754  1.00 79.78           O  
-ANISOU 3166  OE2 GLU B 209    10926   9292  10095   1337   1724  -2368       O  
-ATOM   3167  N   THR B 210      10.770 -22.956 -13.743  1.00 56.40           N  
-ANISOU 3167  N   THR B 210     7566   5555   8307   1665    929  -1770       N  
-ATOM   3168  CA  THR B 210      10.045 -23.952 -12.956  1.00 59.63           C  
-ANISOU 3168  CA  THR B 210     8156   5662   8840   1615    699  -1693       C  
-ATOM   3169  C   THR B 210       8.641 -23.457 -12.571  1.00 52.31           C  
-ANISOU 3169  C   THR B 210     7347   4900   7627   1293    478  -1548       C  
-ATOM   3170  O   THR B 210       7.695 -24.244 -12.475  1.00 51.79           O  
-ANISOU 3170  O   THR B 210     7514   4640   7522   1135    358  -1566       O  
-ATOM   3171  CB  THR B 210      10.848 -24.364 -11.701  1.00 65.37           C  
-ANISOU 3171  CB  THR B 210     8683   6211   9943   1825    531  -1447       C  
-ATOM   3172  OG1 THR B 210       9.966 -24.507 -10.580  1.00 62.12           O  
-ANISOU 3172  OG1 THR B 210     8379   5745   9478   1645    237  -1205       O  
-ATOM   3173  CG2 THR B 210      11.899 -23.309 -11.375  1.00 68.90           C  
-ANISOU 3173  CG2 THR B 210     8766   6938  10477   1940    553  -1291       C  
-ATOM   3174  N   GLY B 211       8.508 -22.150 -12.364  1.00 43.44           N  
-ANISOU 3174  N   GLY B 211     6050   4119   6335   1195    437  -1406       N  
-ATOM   3175  CA  GLY B 211       7.208 -21.545 -12.117  1.00 42.78           C  
-ANISOU 3175  CA  GLY B 211     6027   4209   6016    926    283  -1291       C  
-ATOM   3176  C   GLY B 211       6.333 -21.580 -13.365  1.00 43.24           C  
-ANISOU 3176  C   GLY B 211     6287   4322   5821    735    329  -1486       C  
-ATOM   3177  O   GLY B 211       5.125 -21.835 -13.285  1.00 38.40           O  
-ANISOU 3177  O   GLY B 211     5793   3677   5119    516    180  -1449       O  
-ATOM   3178  N   LYS B 212       6.941 -21.341 -14.527  1.00 44.41           N  
-ANISOU 3178  N   LYS B 212     6474   4551   5846    797    531  -1687       N  
-ATOM   3179  CA  LYS B 212       6.199 -21.380 -15.782  1.00 46.87           C  
-ANISOU 3179  CA  LYS B 212     7032   4913   5862    594    550  -1875       C  
-ATOM   3180  C   LYS B 212       5.687 -22.786 -16.058  1.00 48.33           C  
-ANISOU 3180  C   LYS B 212     7512   4768   6082    518    503  -2053       C  
-ATOM   3181  O   LYS B 212       4.562 -22.965 -16.522  1.00 49.74           O  
-ANISOU 3181  O   LYS B 212     7874   4948   6079    256    341  -2093       O  
-ATOM   3182  CB  LYS B 212       7.052 -20.884 -16.959  1.00 54.51           C  
-ANISOU 3182  CB  LYS B 212     8035   6027   6649    663    817  -2057       C  
-ATOM   3183  CG  LYS B 212       7.054 -19.366 -17.145  1.00 56.96           C  
-ANISOU 3183  CG  LYS B 212     8175   6689   6779    583    804  -1898       C  
-ATOM   3184  CD  LYS B 212       7.843 -18.945 -18.386  1.00 64.41           C  
-ANISOU 3184  CD  LYS B 212     9202   7770   7500    600   1087  -2069       C  
-ATOM   3185  CE  LYS B 212       7.221 -19.491 -19.668  1.00 68.64           C  
-ANISOU 3185  CE  LYS B 212    10122   8257   7702    407   1092  -2286       C  
-ATOM   3186  NZ  LYS B 212       7.976 -19.088 -20.899  1.00 73.82           N  
-ANISOU 3186  NZ  LYS B 212    10839   9086   8123    415   1308  -2349       N  
-ATOM   3187  N   ALA B 213       6.521 -23.781 -15.768  1.00 49.92           N  
-ANISOU 3187  N   ALA B 213     7748   4669   6549    744    624  -2150       N  
-ATOM   3188  CA  ALA B 213       6.177 -25.176 -16.020  1.00 53.45           C  
-ANISOU 3188  CA  ALA B 213     8504   4734   7072    701    601  -2339       C  
-ATOM   3189  C   ALA B 213       5.115 -25.688 -15.041  1.00 50.05           C  
-ANISOU 3189  C   ALA B 213     8104   4163   6751    513    313  -2130       C  
-ATOM   3190  O   ALA B 213       4.191 -26.402 -15.429  1.00 51.63           O  
-ANISOU 3190  O   ALA B 213     8560   4194   6864    279    190  -2232       O  
-ATOM   3191  CB  ALA B 213       7.428 -26.052 -15.970  1.00 60.22           C  
-ANISOU 3191  CB  ALA B 213     9316   5346   8217   1036    764  -2430       C  
-ATOM   3192  N   LYS B 214       5.258 -25.325 -13.772  1.00 44.33           N  
-ANISOU 3192  N   LYS B 214     7132   3508   6203    593    211  -1837       N  
-ATOM   3193  CA  LYS B 214       4.345 -25.784 -12.729  1.00 46.91           C  
-ANISOU 3193  CA  LYS B 214     7484   3715   6625    419     -6  -1616       C  
-ATOM   3194  C   LYS B 214       2.903 -25.327 -12.966  1.00 43.47           C  
-ANISOU 3194  C   LYS B 214     7059   3482   5977     77   -149  -1559       C  
-ATOM   3195  O   LYS B 214       1.967 -26.124 -12.869  1.00 43.01           O  
-ANISOU 3195  O   LYS B 214     7153   3237   5952   -150   -283  -1546       O  
-ATOM   3196  CB  LYS B 214       4.826 -25.312 -11.350  1.00 45.95           C  
-ANISOU 3196  CB  LYS B 214     7127   3680   6652    549    -67  -1318       C  
-ATOM   3197  CG  LYS B 214       4.087 -25.950 -10.177  1.00 50.30           C  
-ANISOU 3197  CG  LYS B 214     7753   4058   7302    391   -241  -1084       C  
-ATOM   3198  CD  LYS B 214       4.477 -25.309  -8.837  1.00 50.45           C  
-ANISOU 3198  CD  LYS B 214     7590   4218   7359    465   -308   -794       C  
-ATOM   3199  CE  LYS B 214       5.902 -25.673  -8.429  1.00 54.09           C  
-ANISOU 3199  CE  LYS B 214     7992   4500   8061    776   -317   -746       C  
-ATOM   3200  NZ  LYS B 214       6.286 -25.017  -7.136  1.00 55.39           N  
-ANISOU 3200  NZ  LYS B 214     8018   4810   8218    804   -437   -461       N  
-ATOM   3201  N   TYR B 215       2.730 -24.050 -13.291  1.00 40.42           N  
-ANISOU 3201  N   TYR B 215     6493   3459   5405     39   -131  -1513       N  
-ATOM   3202  CA  TYR B 215       1.392 -23.472 -13.418  1.00 41.02           C  
-ANISOU 3202  CA  TYR B 215     6495   3743   5349   -241   -282  -1412       C  
-ATOM   3203  C   TYR B 215       0.920 -23.332 -14.870  1.00 46.66           C  
-ANISOU 3203  C   TYR B 215     7361   4544   5822   -411   -335  -1608       C  
-ATOM   3204  O   TYR B 215      -0.043 -22.619 -15.148  1.00 50.22           O  
-ANISOU 3204  O   TYR B 215     7701   5213   6169   -603   -478  -1512       O  
-ATOM   3205  CB  TYR B 215       1.323 -22.122 -12.690  1.00 37.15           C  
-ANISOU 3205  CB  TYR B 215     5711   3562   4841   -190   -269  -1192       C  
-ATOM   3206  CG  TYR B 215       1.717 -22.212 -11.230  1.00 34.38           C  
-ANISOU 3206  CG  TYR B 215     5264   3142   4657    -75   -246   -994       C  
-ATOM   3207  CD1 TYR B 215       0.950 -22.937 -10.322  1.00 38.10           C  
-ANISOU 3207  CD1 TYR B 215     5781   3459   5237   -229   -325   -851       C  
-ATOM   3208  CD2 TYR B 215       2.852 -21.567 -10.757  1.00 36.47           C  
-ANISOU 3208  CD2 TYR B 215     5405   3499   4952    153   -160   -935       C  
-ATOM   3209  CE1 TYR B 215       1.312 -23.024  -8.979  1.00 39.65           C  
-ANISOU 3209  CE1 TYR B 215     5948   3593   5523   -156   -317   -654       C  
-ATOM   3210  CE2 TYR B 215       3.220 -21.641  -9.420  1.00 36.07           C  
-ANISOU 3210  CE2 TYR B 215     5306   3388   5012    226   -190   -743       C  
-ATOM   3211  CZ  TYR B 215       2.453 -22.370  -8.537  1.00 39.12           C  
-ANISOU 3211  CZ  TYR B 215     5784   3620   5459     72   -268   -604       C  
-ATOM   3212  OH  TYR B 215       2.843 -22.450  -7.215  1.00 36.51           O  
-ANISOU 3212  OH  TYR B 215     5462   3230   5180    118   -309   -401       O  
-ATOM   3213  N   LYS B 216       1.600 -24.010 -15.790  1.00 49.94           N  
-ANISOU 3213  N   LYS B 216     8042   4780   6152   -339   -222  -1879       N  
-ATOM   3214  CA  LYS B 216       1.224 -23.957 -17.199  1.00 56.65           C  
-ANISOU 3214  CA  LYS B 216     9127   5695   6704   -528   -271  -2087       C  
-ATOM   3215  C   LYS B 216      -0.142 -24.601 -17.409  1.00 62.54           C  
-ANISOU 3215  C   LYS B 216    10005   6329   7427   -878   -551  -2081       C  
-ATOM   3216  O   LYS B 216      -0.441 -25.638 -16.819  1.00 61.34           O  
-ANISOU 3216  O   LYS B 216     9937   5892   7478   -942   -610  -2072       O  
-ATOM   3217  CB  LYS B 216       2.284 -24.646 -18.070  1.00 65.11           C  
-ANISOU 3217  CB  LYS B 216    10494   6562   7683   -371    -25  -2417       C  
-ATOM   3218  CG  LYS B 216       1.839 -24.949 -19.496  1.00 71.30           C  
-ANISOU 3218  CG  LYS B 216    11509   7401   8181   -576    -94  -2599       C  
-ATOM   3219  CD  LYS B 216       3.009 -24.968 -20.474  1.00 75.78           C  
-ANISOU 3219  CD  LYS B 216    12161   8023   8610   -367    200  -2806       C  
-ATOM   3220  CE  LYS B 216       2.547 -25.361 -21.872  1.00 81.97           C  
-ANISOU 3220  CE  LYS B 216    13222   8836   9085   -580    124  -2977       C  
-ATOM   3221  NZ  LYS B 216       1.341 -24.589 -22.297  1.00 82.45           N  
-ANISOU 3221  NZ  LYS B 216    13285   9136   8907   -901   -189  -2816       N  
-ATOM   3222  N   ALA B 217      -0.973 -23.975 -18.239  1.00 70.42           N  
-ANISOU 3222  N   ALA B 217    11012   7547   8197  -1120   -748  -2061       N  
-ATOM   3223  CA  ALA B 217      -2.298 -24.510 -18.546  1.00 77.12           C  
-ANISOU 3223  CA  ALA B 217    11933   8327   9041  -1481  -1058  -2036       C  
-ATOM   3224  C   ALA B 217      -2.284 -25.326 -19.834  1.00 85.78           C  
-ANISOU 3224  C   ALA B 217    13314   9337   9944  -1565  -1065  -2262       C  
-ATOM   3225  O   ALA B 217      -1.439 -25.115 -20.708  1.00 87.22           O  
-ANISOU 3225  O   ALA B 217    13650   9592   9899  -1422   -882  -2430       O  
-ATOM   3226  CB  ALA B 217      -3.318 -23.386 -18.637  1.00 74.92           C  
-ANISOU 3226  CB  ALA B 217    11362   8372   8731  -1653  -1299  -1794       C  
-ATOM   3227  OXT ALA B 217      -3.122 -26.207 -20.034  1.00 91.27           O  
-ANISOU 3227  OXT ALA B 217    14090   9888  10702  -1791  -1246  -2278       O  
-TER    3228      ALA B 217                                                      
-ATOM   3229  N   SER C   4     -10.278  20.758  20.620  1.00 70.62           N  
-ANISOU 3229  N   SER C   4    10395   8353   8083    905   1012   -910       N  
-ATOM   3230  CA  SER C   4     -11.254  19.868  21.243  1.00 70.28           C  
-ANISOU 3230  CA  SER C   4    10158   8404   8143    889   1223  -1085       C  
-ATOM   3231  C   SER C   4     -10.692  19.225  22.509  1.00 72.47           C  
-ANISOU 3231  C   SER C   4    10718   8611   8207    441   1242  -1071       C  
-ATOM   3232  O   SER C   4      -9.473  19.119  22.667  1.00 74.64           O  
-ANISOU 3232  O   SER C   4    11191   8882   8285    161   1006   -908       O  
-ATOM   3233  CB  SER C   4     -11.731  18.792  20.245  1.00 66.17           C  
-ANISOU 3233  CB  SER C   4     9033   8223   7888   1102   1085  -1111       C  
-ATOM   3234  OG  SER C   4     -10.654  18.105  19.622  1.00 57.40           O  
-ANISOU 3234  OG  SER C   4     7774   7279   6757    973    718   -932       O  
-ATOM   3235  N   PRO C   5     -11.582  18.802  23.425  1.00 71.80           N  
-ANISOU 3235  N   PRO C   5    10644   8496   8142    381   1531  -1234       N  
-ATOM   3236  CA  PRO C   5     -11.166  17.954  24.551  1.00 67.57           C  
-ANISOU 3236  CA  PRO C   5    10287   7954   7433      0   1558  -1209       C  
-ATOM   3237  C   PRO C   5     -10.775  16.569  24.042  1.00 54.93           C  
-ANISOU 3237  C   PRO C   5     8329   6597   5943    -75   1318  -1105       C  
-ATOM   3238  O   PRO C   5     -10.283  15.737  24.809  1.00 52.63           O  
-ANISOU 3238  O   PRO C   5     8157   6330   5512   -363   1293  -1034       O  
-ATOM   3239  CB  PRO C   5     -12.437  17.850  25.400  1.00 73.77           C  
-ANISOU 3239  CB  PRO C   5    11071   8682   8277     48   1946  -1415       C  
-ATOM   3240  CG  PRO C   5     -13.552  18.059  24.428  1.00 75.57           C  
-ANISOU 3240  CG  PRO C   5    10897   9028   8789    464   2043  -1541       C  
-ATOM   3241  CD  PRO C   5     -13.028  19.083  23.456  1.00 74.63           C  
-ANISOU 3241  CD  PRO C   5    10835   8852   8670    680   1856  -1440       C  
-ATOM   3242  N   GLY C   6     -11.005  16.338  22.751  1.00 42.40           N  
-ANISOU 3242  N   GLY C   6     6316   5194   4599    204   1154  -1097       N  
-ATOM   3243  CA  GLY C   6     -10.634  15.095  22.105  1.00 36.14           C  
-ANISOU 3243  CA  GLY C   6     5175   4627   3931    174    912  -1015       C  
-ATOM   3244  C   GLY C   6     -11.792  14.125  22.014  1.00 32.48           C  
-ANISOU 3244  C   GLY C   6     4322   4291   3727    265   1096  -1193       C  
-ATOM   3245  O   GLY C   6     -12.941  14.485  22.263  1.00 36.09           O  
-ANISOU 3245  O   GLY C   6     4708   4716   4289    409   1390  -1378       O  
-ATOM   3246  N   VAL C   7     -11.486  12.883  21.658  1.00 30.81           N  
-ANISOU 3246  N   VAL C   7     3861   4232   3615    178    930  -1140       N  
-ATOM   3247  CA  VAL C   7     -12.492  11.837  21.672  1.00 32.24           C  
-ANISOU 3247  CA  VAL C   7     3708   4511   4032    181   1114  -1311       C  
-ATOM   3248  C   VAL C   7     -12.777  11.485  23.123  1.00 35.99           C  
-ANISOU 3248  C   VAL C   7     4484   4815   4376   -102   1410  -1342       C  
-ATOM   3249  O   VAL C   7     -11.886  11.046  23.854  1.00 32.91           O  
-ANISOU 3249  O   VAL C   7     4391   4340   3773   -365   1338  -1178       O  
-ATOM   3250  CB  VAL C   7     -12.012  10.589  20.926  1.00 29.61           C  
-ANISOU 3250  CB  VAL C   7     3077   4342   3830    146    863  -1245       C  
-ATOM   3251  CG1 VAL C   7     -13.048   9.478  21.045  1.00 35.74           C  
-ANISOU 3251  CG1 VAL C   7     3552   5180   4848     87   1088  -1437       C  
-ATOM   3252  CG2 VAL C   7     -11.725  10.910  19.457  1.00 36.78           C  
-ANISOU 3252  CG2 VAL C   7     3661   5455   4859    442    561  -1214       C  
-ATOM   3253  N   VAL C   8     -14.018  11.701  23.551  1.00 35.93           N  
-ANISOU 3253  N   VAL C   8     4393   4785   4473    -30   1747  -1546       N  
-ATOM   3254  CA  VAL C   8     -14.393  11.423  24.927  1.00 41.06           C  
-ANISOU 3254  CA  VAL C   8     5309   5291   5000   -275   2055  -1583       C  
-ATOM   3255  C   VAL C   8     -14.773   9.957  25.084  1.00 45.04           C  
-ANISOU 3255  C   VAL C   8     5585   5859   5670   -446   2154  -1623       C  
-ATOM   3256  O   VAL C   8     -15.745   9.481  24.486  1.00 45.74           O  
-ANISOU 3256  O   VAL C   8     5250   6094   6034   -329   2256  -1806       O  
-ATOM   3257  CB  VAL C   8     -15.554  12.307  25.385  1.00 46.21           C  
-ANISOU 3257  CB  VAL C   8     5991   5898   5668   -125   2391  -1779       C  
-ATOM   3258  CG1 VAL C   8     -16.025  11.880  26.759  1.00 46.04           C  
-ANISOU 3258  CG1 VAL C   8     6183   5770   5540   -371   2718  -1826       C  
-ATOM   3259  CG2 VAL C   8     -15.126  13.764  25.407  1.00 40.94           C  
-ANISOU 3259  CG2 VAL C   8     5650   5094   4810      8   2336  -1731       C  
-ATOM   3260  N   ILE C   9     -13.981   9.233  25.869  1.00 38.43           N  
-ANISOU 3260  N   ILE C   9     5026   4920   4656   -722   2124  -1450       N  
-ATOM   3261  CA  ILE C   9     -14.321   7.859  26.217  1.00 40.56           C  
-ANISOU 3261  CA  ILE C   9     5173   5183   5054   -911   2274  -1463       C  
-ATOM   3262  C   ILE C   9     -14.986   7.922  27.586  1.00 41.36           C  
-ANISOU 3262  C   ILE C   9     5519   5163   5035  -1079   2660  -1520       C  
-ATOM   3263  O   ILE C   9     -14.375   8.364  28.564  1.00 41.77           O  
-ANISOU 3263  O   ILE C   9     5992   5099   4780  -1212   2693  -1390       O  
-ATOM   3264  CB  ILE C   9     -13.080   6.957  26.204  1.00 38.90           C  
-ANISOU 3264  CB  ILE C   9     5108   4949   4722  -1064   2024  -1221       C  
-ATOM   3265  CG1 ILE C   9     -12.474   6.932  24.796  1.00 37.20           C  
-ANISOU 3265  CG1 ILE C   9     4623   4883   4628   -872   1643  -1179       C  
-ATOM   3266  CG2 ILE C   9     -13.425   5.541  26.653  1.00 39.54           C  
-ANISOU 3266  CG2 ILE C   9     5130   4970   4925  -1261   2222  -1217       C  
-ATOM   3267  CD1 ILE C   9     -11.264   6.056  24.664  1.00 34.40           C  
-ANISOU 3267  CD1 ILE C   9     4376   4539   4156   -975   1380   -946       C  
-ATOM   3268  N   SER C  10     -16.260   7.546  27.652  1.00 49.43           N  
-ANISOU 3268  N   SER C  10     6261   6236   6282  -1069   2955  -1726       N  
-ATOM   3269  CA  SER C  10     -17.021   7.750  28.881  1.00 53.27           C  
-ANISOU 3269  CA  SER C  10     6939   6634   6668  -1177   3287  -1779       C  
-ATOM   3270  C   SER C  10     -16.710   6.680  29.918  1.00 52.71           C  
-ANISOU 3270  C   SER C  10     7102   6440   6486  -1475   3436  -1630       C  
-ATOM   3271  O   SER C  10     -16.142   5.636  29.592  1.00 48.06           O  
-ANISOU 3271  O   SER C  10     6458   5842   5960  -1594   3348  -1525       O  
-ATOM   3272  CB  SER C  10     -18.526   7.845  28.603  1.00 58.50           C  
-ANISOU 3272  CB  SER C  10     7231   7407   7591  -1020   3376  -1961       C  
-ATOM   3273  OG  SER C  10     -18.898   7.035  27.504  1.00 63.79           O  
-ANISOU 3273  OG  SER C  10     7473   8214   8551   -963   3232  -2042       O  
-ATOM   3274  N   ASP C  11     -17.078   6.959  31.166  1.00 49.89           N  
-ANISOU 3274  N   ASP C  11     7007   5985   5965  -1565   3628  -1600       N  
-ATOM   3275  CA  ASP C  11     -16.749   6.091  32.297  1.00 55.02           C  
-ANISOU 3275  CA  ASP C  11     7925   6514   6466  -1799   3735  -1426       C  
-ATOM   3276  C   ASP C  11     -17.328   4.692  32.137  1.00 55.65           C  
-ANISOU 3276  C   ASP C  11     7757   6575   6814  -1911   3842  -1449       C  
-ATOM   3277  O   ASP C  11     -16.749   3.714  32.607  1.00 57.47           O  
-ANISOU 3277  O   ASP C  11     8159   6708   6970  -2058   3830  -1268       O  
-ATOM   3278  CB  ASP C  11     -17.250   6.702  33.611  1.00 56.15           C  
-ANISOU 3278  CB  ASP C  11     8313   6591   6429  -1830   3924  -1437       C  
-ATOM   3279  CG  ASP C  11     -16.368   7.833  34.114  1.00 59.97           C  
-ANISOU 3279  CG  ASP C  11     9170   7034   6583  -1804   3793  -1351       C  
-ATOM   3280  OD1 ASP C  11     -15.689   8.482  33.296  1.00 59.01           O  
-ANISOU 3280  OD1 ASP C  11     9066   6948   6407  -1707   3586  -1349       O  
-ATOM   3281  OD2 ASP C  11     -16.366   8.074  35.342  1.00 66.34           O  
-ANISOU 3281  OD2 ASP C  11    10242   7776   7186  -1884   3889  -1295       O  
-ATOM   3282  N   ASP C  12     -18.473   4.608  31.468  1.00 55.53           N  
-ANISOU 3282  N   ASP C  12     7344   6657   7099  -1821   3913  -1667       N  
-ATOM   3283  CA  ASP C  12     -19.132   3.330  31.240  1.00 63.27           C  
-ANISOU 3283  CA  ASP C  12     8075   7617   8346  -1937   4000  -1731       C  
-ATOM   3284  C   ASP C  12     -18.809   2.748  29.862  1.00 61.20           C  
-ANISOU 3284  C   ASP C  12     7508   7430   8314  -1881   3781  -1787       C  
-ATOM   3285  O   ASP C  12     -19.647   2.094  29.239  1.00 63.89           O  
-ANISOU 3285  O   ASP C  12     7514   7832   8929  -1883   3785  -1949       O  
-ATOM   3286  CB  ASP C  12     -20.648   3.450  31.454  1.00 70.20           C  
-ANISOU 3286  CB  ASP C  12     8708   8579   9385  -1909   4191  -1929       C  
-ATOM   3287  CG  ASP C  12     -21.333   4.293  30.394  1.00 73.82           C  
-ANISOU 3287  CG  ASP C  12     8810   9248   9993  -1655   4050  -2116       C  
-ATOM   3288  OD1 ASP C  12     -20.637   5.033  29.660  1.00 70.21           O  
-ANISOU 3288  OD1 ASP C  12     8347   8848   9480  -1479   3833  -2093       O  
-ATOM   3289  OD2 ASP C  12     -22.578   4.214  30.300  1.00 78.78           O  
-ANISOU 3289  OD2 ASP C  12     9168   9995  10770  -1618   4143  -2269       O  
-ATOM   3290  N   GLU C  13     -17.592   2.995  29.388  1.00 56.75           N  
-ANISOU 3290  N   GLU C  13     7065   6879   7620  -1831   3571  -1654       N  
-ATOM   3291  CA  GLU C  13     -17.127   2.388  28.146  1.00 57.52           C  
-ANISOU 3291  CA  GLU C  13     6897   7048   7910  -1779   3345  -1675       C  
-ATOM   3292  C   GLU C  13     -16.751   0.931  28.385  1.00 58.04           C  
-ANISOU 3292  C   GLU C  13     7068   6953   8031  -1973   3381  -1538       C  
-ATOM   3293  O   GLU C  13     -15.837   0.640  29.161  1.00 56.18           O  
-ANISOU 3293  O   GLU C  13     7212   6589   7544  -2078   3380  -1281       O  
-ATOM   3294  CB  GLU C  13     -15.927   3.153  27.583  1.00 60.42           C  
-ANISOU 3294  CB  GLU C  13     7373   7488   8094  -1638   3047  -1546       C  
-ATOM   3295  CG  GLU C  13     -15.283   2.516  26.345  1.00 67.17           C  
-ANISOU 3295  CG  GLU C  13     7997   8416   9109  -1545   2707  -1511       C  
-ATOM   3296  CD  GLU C  13     -16.104   2.695  25.072  1.00 74.83           C  
-ANISOU 3296  CD  GLU C  13     8443   9595  10394  -1349   2631  -1788       C  
-ATOM   3297  OE1 GLU C  13     -17.184   3.323  25.134  1.00 80.25           O  
-ANISOU 3297  OE1 GLU C  13     8994  10351  11146  -1243   2736  -1951       O  
-ATOM   3298  OE2 GLU C  13     -15.663   2.212  24.003  1.00 75.97           O  
-ANISOU 3298  OE2 GLU C  13     8360   9828  10677  -1254   2356  -1792       O  
-ATOM   3299  N   PRO C  14     -17.464   0.003  27.724  1.00 66.67           N  
-ANISOU 3299  N   PRO C  14     7851   8052   9428  -1994   3383  -1702       N  
-ATOM   3300  CA  PRO C  14     -17.124  -1.417  27.857  1.00 67.63           C  
-ANISOU 3300  CA  PRO C  14     8085   7994   9618  -2148   3420  -1587       C  
-ATOM   3301  C   PRO C  14     -15.808  -1.759  27.170  1.00 59.78           C  
-ANISOU 3301  C   PRO C  14     7147   6994   8572  -2106   3158  -1410       C  
-ATOM   3302  O   PRO C  14     -15.208  -2.777  27.501  1.00 65.21           O  
-ANISOU 3302  O   PRO C  14     8061   7511   9205  -2203   3171  -1219       O  
-ATOM   3303  CB  PRO C  14     -18.284  -2.128  27.146  1.00 70.35           C  
-ANISOU 3303  CB  PRO C  14     8059   8381  10292  -2162   3462  -1862       C  
-ATOM   3304  CG  PRO C  14     -18.826  -1.119  26.195  1.00 70.12           C  
-ANISOU 3304  CG  PRO C  14     7680   8605  10357  -1947   3280  -2070       C  
-ATOM   3305  CD  PRO C  14     -18.642   0.216  26.863  1.00 69.70           C  
-ANISOU 3305  CD  PRO C  14     7809   8606  10067  -1864   3332  -1987       C  
-ATOM   3306  N   GLY C  15     -15.356  -0.925  26.240  1.00 54.32           N  
-ANISOU 3306  N   GLY C  15     6258   6496   7887  -1944   2914  -1459       N  
-ATOM   3307  CA  GLY C  15     -14.221  -1.303  25.413  1.00 51.71           C  
-ANISOU 3307  CA  GLY C  15     5925   6193   7529  -1842   2563  -1313       C  
-ATOM   3308  C   GLY C  15     -14.556  -2.585  24.665  1.00 52.04           C  
-ANISOU 3308  C   GLY C  15     5703   6179   7892  -1911   2585  -1451       C  
-ATOM   3309  O   GLY C  15     -15.731  -2.862  24.406  1.00 55.29           O  
-ANISOU 3309  O   GLY C  15     5873   6617   8517  -1899   2687  -1702       O  
-ATOM   3310  N   TYR C  16     -13.541  -3.387  24.354  1.00 45.39           N  
-ANISOU 3310  N   TYR C  16     4999   5249   7000  -1895   2387  -1261       N  
-ATOM   3311  CA  TYR C  16     -13.741  -4.576  23.528  1.00 45.27           C  
-ANISOU 3311  CA  TYR C  16     4753   5170   7276  -1930   2364  -1400       C  
-ATOM   3312  C   TYR C  16     -13.114  -5.847  24.109  1.00 47.74           C  
-ANISOU 3312  C   TYR C  16     5421   5194   7526  -2076   2487  -1164       C  
-ATOM   3313  O   TYR C  16     -12.015  -5.807  24.666  1.00 45.36           O  
-ANISOU 3313  O   TYR C  16     5494   4835   6906  -2026   2371   -836       O  
-ATOM   3314  CB  TYR C  16     -13.173  -4.328  22.129  1.00 39.71           C  
-ANISOU 3314  CB  TYR C  16     3749   4694   6646  -1683   1941  -1465       C  
-ATOM   3315  CG  TYR C  16     -13.735  -3.107  21.446  1.00 42.36           C  
-ANISOU 3315  CG  TYR C  16     3757   5317   7021  -1471   1788  -1662       C  
-ATOM   3316  CD1 TYR C  16     -14.902  -3.190  20.696  1.00 50.05           C  
-ANISOU 3316  CD1 TYR C  16     4462   6393   8161  -1342   1751  -1928       C  
-ATOM   3317  CD2 TYR C  16     -13.110  -1.869  21.562  1.00 37.01           C  
-ANISOU 3317  CD2 TYR C  16     3202   4768   6090  -1317   1597  -1510       C  
-ATOM   3318  CE1 TYR C  16     -15.427  -2.082  20.074  1.00 50.41           C  
-ANISOU 3318  CE1 TYR C  16     4339   6656   8159  -1105   1573  -2025       C  
-ATOM   3319  CE2 TYR C  16     -13.632  -0.745  20.941  1.00 42.82           C  
-ANISOU 3319  CE2 TYR C  16     3648   5740   6880  -1118   1501  -1681       C  
-ATOM   3320  CZ  TYR C  16     -14.791  -0.867  20.196  1.00 46.07           C  
-ANISOU 3320  CZ  TYR C  16     3849   6220   7435   -977   1449  -1892       C  
-ATOM   3321  OH  TYR C  16     -15.324   0.233  19.574  1.00 46.25           O  
-ANISOU 3321  OH  TYR C  16     3760   6415   7400   -737   1286  -1948       O  
-ATOM   3322  N   ASP C  17     -13.819  -6.969  23.963  1.00 45.63           N  
-ANISOU 3322  N   ASP C  17     5075   4779   7482  -2156   2642  -1314       N  
-ATOM   3323  CA  ASP C  17     -13.307  -8.283  24.352  1.00 50.26           C  
-ANISOU 3323  CA  ASP C  17     5968   5079   8051  -2254   2760  -1119       C  
-ATOM   3324  C   ASP C  17     -12.020  -8.552  23.569  1.00 47.97           C  
-ANISOU 3324  C   ASP C  17     5710   4788   7728  -2152   2469   -958       C  
-ATOM   3325  O   ASP C  17     -11.966  -8.308  22.366  1.00 42.67           O  
-ANISOU 3325  O   ASP C  17     4682   4327   7203  -1993   2173  -1144       O  
-ATOM   3326  CB  ASP C  17     -14.353  -9.371  24.054  1.00 55.20           C  
-ANISOU 3326  CB  ASP C  17     6425   5582   8968  -2356   2952  -1378       C  
-ATOM   3327  CG  ASP C  17     -13.954 -10.755  24.581  1.00 64.66           C  
-ANISOU 3327  CG  ASP C  17     7967   6449  10150  -2459   3133  -1181       C  
-ATOM   3328  OD1 ASP C  17     -12.780 -11.155  24.425  1.00 64.08           O  
-ANISOU 3328  OD1 ASP C  17     8112   6271   9965  -2384   2987   -934       O  
-ATOM   3329  OD2 ASP C  17     -14.826 -11.455  25.148  1.00 71.76           O  
-ANISOU 3329  OD2 ASP C  17     8927   7195  11144  -2603   3425  -1269       O  
-ATOM   3330  N   LEU C  18     -10.997  -9.056  24.262  1.00 37.47           N  
-ANISOU 3330  N   LEU C  18     5055   4461   4720  -1712    610    451       N  
-ATOM   3331  CA  LEU C  18      -9.696  -9.344  23.656  1.00 35.61           C  
-ANISOU 3331  CA  LEU C  18     4957   4011   4564  -1526    447    371       C  
-ATOM   3332  C   LEU C  18      -9.836 -10.296  22.470  1.00 32.17           C  
-ANISOU 3332  C   LEU C  18     4548   3408   4266  -1529    280    309       C  
-ATOM   3333  O   LEU C  18      -9.084 -10.210  21.509  1.00 33.38           O  
-ANISOU 3333  O   LEU C  18     4697   3503   4482  -1337    208    164       O  
-ATOM   3334  CB  LEU C  18      -8.759  -9.974  24.692  1.00 36.63           C  
-ANISOU 3334  CB  LEU C  18     5294   3991   4633  -1564    332    482       C  
-ATOM   3335  CG  LEU C  18      -8.378  -9.149  25.921  1.00 38.45           C  
-ANISOU 3335  CG  LEU C  18     5541   4373   4694  -1573    461    531       C  
-ATOM   3336  CD1 LEU C  18      -7.632  -9.999  26.946  1.00 40.82           C  
-ANISOU 3336  CD1 LEU C  18     6049   4533   4927  -1670    303    695       C  
-ATOM   3337  CD2 LEU C  18      -7.530  -7.977  25.506  1.00 34.31           C  
-ANISOU 3337  CD2 LEU C  18     4953   3917   4168  -1337    526    378       C  
-ATOM   3338  N   ASP C  19     -10.816 -11.191  22.544  1.00 32.65           N  
-ANISOU 3338  N   ASP C  19     4630   3421   4356  -1771    220    412       N  
-ATOM   3339  CA  ASP C  19     -10.961 -12.246  21.538  1.00 37.36           C  
-ANISOU 3339  CA  ASP C  19     5304   3812   5079  -1815     29    346       C  
-ATOM   3340  C   ASP C  19     -11.410 -11.763  20.165  1.00 32.76           C  
-ANISOU 3340  C   ASP C  19     4538   3366   4543  -1725     68    189       C  
-ATOM   3341  O   ASP C  19     -11.478 -12.553  19.222  1.00 33.72           O  
-ANISOU 3341  O   ASP C  19     4716   3348   4747  -1747    -84     88       O  
-ATOM   3342  CB  ASP C  19     -11.928 -13.317  22.029  1.00 43.62           C  
-ANISOU 3342  CB  ASP C  19     6184   4512   5878  -2160    -65    525       C  
-ATOM   3343  CG  ASP C  19     -11.290 -14.255  23.008  1.00 60.83           C  
-ANISOU 3343  CG  ASP C  19     8634   6419   8059  -2255   -237    680       C  
-ATOM   3344  OD1 ASP C  19     -10.510 -13.781  23.861  1.00 66.38           O  
-ANISOU 3344  OD1 ASP C  19     9379   7165   8678  -2144   -180    729       O  
-ATOM   3345  OD2 ASP C  19     -11.556 -15.470  22.916  1.00 72.93           O  
-ANISOU 3345  OD2 ASP C  19    10350   7679   9680  -2448   -455    760       O  
-ATOM   3346  N   LEU C  20     -11.732 -10.481  20.060  1.00 31.19           N  
-ANISOU 3346  N   LEU C  20     4133   3430   4289  -1630    251    167       N  
-ATOM   3347  CA  LEU C  20     -12.203  -9.926  18.794  1.00 30.51           C  
-ANISOU 3347  CA  LEU C  20     3865   3492   4234  -1558    270     64       C  
-ATOM   3348  C   LEU C  20     -11.043  -9.331  18.015  1.00 30.72           C  
-ANISOU 3348  C   LEU C  20     3904   3518   4252  -1313    247    -77       C  
-ATOM   3349  O   LEU C  20     -11.199  -8.922  16.859  1.00 28.31           O  
-ANISOU 3349  O   LEU C  20     3478   3330   3947  -1256    230   -158       O  
-ATOM   3350  CB  LEU C  20     -13.275  -8.858  19.039  1.00 36.04           C  
-ANISOU 3350  CB  LEU C  20     4327   4462   4905  -1578    446    131       C  
-ATOM   3351  CG  LEU C  20     -14.584  -9.376  19.627  1.00 35.52           C  
-ANISOU 3351  CG  LEU C  20     4158   4514   4823  -1841    491    256       C  
-ATOM   3352  CD1 LEU C  20     -15.457  -8.228  20.109  1.00 41.49           C  
-ANISOU 3352  CD1 LEU C  20     4662   5559   5543  -1784    692    282       C  
-ATOM   3353  CD2 LEU C  20     -15.346 -10.212  18.624  1.00 36.66           C  
-ANISOU 3353  CD2 LEU C  20     4251   4652   5027  -2015    354    247       C  
-ATOM   3354  N   PHE C  21      -9.881  -9.297  18.664  1.00 28.01           N  
-ANISOU 3354  N   PHE C  21     3692   3074   3879  -1196    239    -88       N  
-ATOM   3355  CA  PHE C  21      -8.679  -8.690  18.102  1.00 28.75           C  
-ANISOU 3355  CA  PHE C  21     3774   3216   3933   -993    230   -202       C  
-ATOM   3356  C   PHE C  21      -7.482  -9.636  18.105  1.00 30.67           C  
-ANISOU 3356  C   PHE C  21     4167   3287   4200   -884     89   -300       C  
-ATOM   3357  O   PHE C  21      -7.538 -10.718  18.688  1.00 30.35           O  
-ANISOU 3357  O   PHE C  21     4278   3030   4222   -955    -20   -255       O  
-ATOM   3358  CB  PHE C  21      -8.340  -7.415  18.864  1.00 27.51           C  
-ANISOU 3358  CB  PHE C  21     3580   3167   3707   -927    367   -135       C  
-ATOM   3359  CG  PHE C  21      -9.387  -6.355  18.730  1.00 35.65           C  
-ANISOU 3359  CG  PHE C  21     4455   4351   4742   -952    486    -85       C  
-ATOM   3360  CD1 PHE C  21      -9.357  -5.473  17.662  1.00 37.49           C  
-ANISOU 3360  CD1 PHE C  21     4573   4699   4971   -873    481   -123       C  
-ATOM   3361  CD2 PHE C  21     -10.426  -6.266  19.645  1.00 40.74           C  
-ANISOU 3361  CD2 PHE C  21     5052   5039   5388  -1056    591      2       C  
-ATOM   3362  CE1 PHE C  21     -10.325  -4.496  17.516  1.00 45.16           C  
-ANISOU 3362  CE1 PHE C  21     5405   5775   5978   -860    553    -69       C  
-ATOM   3363  CE2 PHE C  21     -11.402  -5.293  19.504  1.00 47.34           C  
-ANISOU 3363  CE2 PHE C  21     5715   6023   6251  -1025    692     18       C  
-ATOM   3364  CZ  PHE C  21     -11.349  -4.403  18.436  1.00 48.36           C  
-ANISOU 3364  CZ  PHE C  21     5749   6212   6413   -910    659    -15       C  
-ATOM   3365  N   CYS C  22      -6.413  -9.225  17.420  1.00 28.63           N  
-ANISOU 3365  N   CYS C  22     3852   3134   3891   -716     77   -429       N  
-ATOM   3366  CA  CYS C  22      -5.175  -9.992  17.401  1.00 32.72           C  
-ANISOU 3366  CA  CYS C  22     4454   3550   4429   -554    -45   -554       C  
-ATOM   3367  C   CYS C  22      -4.338  -9.454  18.555  1.00 31.66           C  
-ANISOU 3367  C   CYS C  22     4358   3430   4241   -503     -2   -445       C  
-ATOM   3368  O   CYS C  22      -4.003  -8.277  18.582  1.00 31.66           O  
-ANISOU 3368  O   CYS C  22     4263   3620   4147   -491    106   -413       O  
-ATOM   3369  CB  CYS C  22      -4.447  -9.815  16.062  1.00 33.74           C  
-ANISOU 3369  CB  CYS C  22     4454   3876   4491   -418    -61   -762       C  
-ATOM   3370  N   ILE C  23      -4.047 -10.312  19.528  1.00 31.09           N  
-ANISOU 3370  N   ILE C  23     4442   3144   4225   -499   -109   -372       N  
-ATOM   3371  CA  ILE C  23      -3.347  -9.910  20.748  1.00 34.60           C  
-ANISOU 3371  CA  ILE C  23     4940   3604   4603   -489    -90   -245       C  
-ATOM   3372  C   ILE C  23      -2.175 -10.857  20.986  1.00 33.89           C  
-ANISOU 3372  C   ILE C  23     4933   3367   4575   -310   -280   -300       C  
-ATOM   3373  O   ILE C  23      -2.341 -12.068  20.867  1.00 36.92           O  
-ANISOU 3373  O   ILE C  23     5443   3496   5088   -280   -445   -332       O  
-ATOM   3374  CB  ILE C  23      -4.294 -10.051  21.963  1.00 36.66           C  
-ANISOU 3374  CB  ILE C  23     5315   3768   4844   -706    -49    -36       C  
-ATOM   3375  CG1 ILE C  23      -5.492  -9.112  21.817  1.00 38.25           C  
-ANISOU 3375  CG1 ILE C  23     5401   4133   4997   -840    141     -2       C  
-ATOM   3376  CG2 ILE C  23      -3.539  -9.845  23.279  1.00 36.14           C  
-ANISOU 3376  CG2 ILE C  23     5335   3709   4687   -715    -64     93       C  
-ATOM   3377  CD1 ILE C  23      -5.146  -7.660  21.905  1.00 34.75           C  
-ANISOU 3377  CD1 ILE C  23     4858   3889   4457   -785    284    -24       C  
-ATOM   3378  N   PRO C  24      -0.998 -10.324  21.355  1.00 30.76           N  
-ANISOU 3378  N   PRO C  24     4471   3118   4100   -193   -279   -305       N  
-ATOM   3379  CA  PRO C  24       0.128 -11.247  21.569  1.00 34.06           C  
-ANISOU 3379  CA  PRO C  24     4931   3416   4595     18   -478   -363       C  
-ATOM   3380  C   PRO C  24      -0.153 -12.243  22.695  1.00 38.56           C  
-ANISOU 3380  C   PRO C  24     5731   3671   5251    -61   -645   -170       C  
-ATOM   3381  O   PRO C  24      -0.650 -11.847  23.755  1.00 37.85           O  
-ANISOU 3381  O   PRO C  24     5722   3594   5063   -275   -575     44       O  
-ATOM   3382  CB  PRO C  24       1.289 -10.308  21.919  1.00 30.51           C  
-ANISOU 3382  CB  PRO C  24     4345   3239   4010     85   -425   -353       C  
-ATOM   3383  CG  PRO C  24       0.654  -9.011  22.322  1.00 35.26           C  
-ANISOU 3383  CG  PRO C  24     4932   3989   4475   -139   -227   -231       C  
-ATOM   3384  CD  PRO C  24      -0.613  -8.916  21.544  1.00 27.04           C  
-ANISOU 3384  CD  PRO C  24     3884   2911   3479   -240   -126   -270       C  
-ATOM   3385  N   ASN C  25       0.143 -13.521  22.449  1.00 39.15           N  
-ANISOU 3385  N   ASN C  25     5915   3464   5496    101   -874   -250       N  
-ATOM   3386  CA  ASN C  25      -0.185 -14.602  23.380  1.00 45.97           C  
-ANISOU 3386  CA  ASN C  25     7034   3966   6465      1  -1087    -43       C  
-ATOM   3387  C   ASN C  25       0.399 -14.423  24.782  1.00 43.19           C  
-ANISOU 3387  C   ASN C  25     6752   3641   6017    -60  -1154    208       C  
-ATOM   3388  O   ASN C  25      -0.155 -14.944  25.757  1.00 44.17           O  
-ANISOU 3388  O   ASN C  25     7076   3574   6131   -283  -1254    467       O  
-ATOM   3389  CB  ASN C  25       0.243 -15.956  22.787  1.00 54.82           C  
-ANISOU 3389  CB  ASN C  25     8269   4743   7818    252  -1363   -213       C  
-ATOM   3390  CG  ASN C  25      -0.120 -17.138  23.677  1.00 68.27           C  
-ANISOU 3390  CG  ASN C  25    10279   6003   9655    125  -1637     29       C  
-ATOM   3391  OD1 ASN C  25      -1.298 -17.431  23.890  1.00 73.29           O  
-ANISOU 3391  OD1 ASN C  25    11062   6498  10287   -190  -1625    189       O  
-ATOM   3392  ND2 ASN C  25       0.894 -17.842  24.175  1.00 71.52           N  
-ANISOU 3392  ND2 ASN C  25    10782   6204  10189    362  -1904     67       N  
-ATOM   3393  N   HIS C  26       1.509 -13.692  24.891  1.00 40.98           N  
-ANISOU 3393  N   HIS C  26     6304   3626   5643    101  -1107    145       N  
-ATOM   3394  CA  HIS C  26       2.189 -13.570  26.184  1.00 43.87           C  
-ANISOU 3394  CA  HIS C  26     6727   4034   5909     55  -1203    367       C  
-ATOM   3395  C   HIS C  26       1.483 -12.620  27.148  1.00 43.78           C  
-ANISOU 3395  C   HIS C  26     6754   4208   5674   -277  -1001    561       C  
-ATOM   3396  O   HIS C  26       1.841 -12.553  28.321  1.00 45.44           O  
-ANISOU 3396  O   HIS C  26     7045   4456   5762   -387  -1073    765       O  
-ATOM   3397  CB  HIS C  26       3.692 -13.236  26.041  1.00 41.78           C  
-ANISOU 3397  CB  HIS C  26     6260   3993   5620    333  -1265    242       C  
-ATOM   3398  CG  HIS C  26       3.988 -11.967  25.299  1.00 42.12           C  
-ANISOU 3398  CG  HIS C  26     6058   4423   5525    339  -1018     65       C  
-ATOM   3399  ND1 HIS C  26       4.248 -11.933  23.942  1.00 44.99           N  
-ANISOU 3399  ND1 HIS C  26     6238   4909   5947    531   -958   -210       N  
-ATOM   3400  CD2 HIS C  26       4.119 -10.688  25.734  1.00 40.19           C  
-ANISOU 3400  CD2 HIS C  26     5731   4464   5076    164   -840    130       C  
-ATOM   3401  CE1 HIS C  26       4.502 -10.689  23.573  1.00 43.07           C  
-ANISOU 3401  CE1 HIS C  26     5815   5013   5539    447   -761   -268       C  
-ATOM   3402  NE2 HIS C  26       4.432  -9.915  24.641  1.00 40.10           N  
-ANISOU 3402  NE2 HIS C  26     5506   4711   5018    233   -695    -70       N  
-ATOM   3403  N   TYR C  27       0.477 -11.904  26.642  1.00 41.44           N  
-ANISOU 3403  N   TYR C  27     6393   4032   5321   -425   -758    485       N  
-ATOM   3404  CA  TYR C  27      -0.352 -11.015  27.456  1.00 41.42           C  
-ANISOU 3404  CA  TYR C  27     6409   4199   5129   -701   -549    609       C  
-ATOM   3405  C   TYR C  27      -1.805 -11.492  27.584  1.00 45.09           C  
-ANISOU 3405  C   TYR C  27     6972   4547   5613   -939   -492    714       C  
-ATOM   3406  O   TYR C  27      -2.657 -10.752  28.065  1.00 44.42           O  
-ANISOU 3406  O   TYR C  27     6853   4640   5386  -1137   -286    760       O  
-ATOM   3407  CB  TYR C  27      -0.341  -9.596  26.869  1.00 33.82           C  
-ANISOU 3407  CB  TYR C  27     5265   3506   4078   -673   -312    442       C  
-ATOM   3408  CG  TYR C  27       0.987  -8.879  26.974  1.00 33.05           C  
-ANISOU 3408  CG  TYR C  27     5067   3598   3893   -551   -332    384       C  
-ATOM   3409  CD1 TYR C  27       1.794  -9.022  28.100  1.00 32.12           C  
-ANISOU 3409  CD1 TYR C  27     5021   3509   3674   -582   -459    527       C  
-ATOM   3410  CD2 TYR C  27       1.429  -8.051  25.947  1.00 33.91           C  
-ANISOU 3410  CD2 TYR C  27     5002   3883   4000   -442   -238    209       C  
-ATOM   3411  CE1 TYR C  27       3.012  -8.358  28.200  1.00 34.82           C  
-ANISOU 3411  CE1 TYR C  27     5249   4057   3925   -500   -487    480       C  
-ATOM   3412  CE2 TYR C  27       2.634  -7.380  26.034  1.00 31.59           C  
-ANISOU 3412  CE2 TYR C  27     4600   3795   3608   -383   -261    173       C  
-ATOM   3413  CZ  TYR C  27       3.426  -7.537  27.151  1.00 34.80           C  
-ANISOU 3413  CZ  TYR C  27     5064   4233   3925   -407   -383    299       C  
-ATOM   3414  OH  TYR C  27       4.633  -6.864  27.216  1.00 33.16           O  
-ANISOU 3414  OH  TYR C  27     4726   4261   3611   -373   -415    266       O  
-ATOM   3415  N   ALA C  28      -2.088 -12.720  27.153  1.00 48.66           N  
-ANISOU 3415  N   ALA C  28     7537   4712   6240   -920   -680    737       N  
-ATOM   3416  CA  ALA C  28      -3.474 -13.196  27.062  1.00 51.79           C  
-ANISOU 3416  CA  ALA C  28     7996   5016   6664  -1167   -637    821       C  
-ATOM   3417  C   ALA C  28      -4.257 -13.162  28.385  1.00 52.23           C  
-ANISOU 3417  C   ALA C  28     8139   5176   6531  -1511   -566   1084       C  
-ATOM   3418  O   ALA C  28      -5.475 -12.976  28.380  1.00 57.23           O  
-ANISOU 3418  O   ALA C  28     8710   5932   7104  -1730   -404   1115       O  
-ATOM   3419  CB  ALA C  28      -3.526 -14.600  26.437  1.00 55.14           C  
-ANISOU 3419  CB  ALA C  28     8573   5062   7314  -1109   -903    804       C  
-ATOM   3420  N   GLU C  29      -3.552 -13.345  29.501  1.00 51.35           N  
-ANISOU 3420  N   GLU C  29     8148   5054   6310  -1562   -689   1268       N  
-ATOM   3421  CA  GLU C  29      -4.142 -13.345  30.841  1.00 52.51           C  
-ANISOU 3421  CA  GLU C  29     8381   5346   6223  -1906   -636   1526       C  
-ATOM   3422  C   GLU C  29      -4.091 -11.989  31.550  1.00 49.62           C  
-ANISOU 3422  C   GLU C  29     7888   5360   5604  -1952   -369   1459       C  
-ATOM   3423  O   GLU C  29      -4.767 -11.774  32.560  1.00 49.60           O  
-ANISOU 3423  O   GLU C  29     7902   5576   5370  -2235   -242   1595       O  
-ATOM   3424  CB  GLU C  29      -3.376 -14.330  31.715  1.00 60.47           C  
-ANISOU 3424  CB  GLU C  29     9613   6132   7229  -1960   -956   1791       C  
-ATOM   3425  CG  GLU C  29      -3.223 -15.699  31.114  1.00 67.46           C  
-ANISOU 3425  CG  GLU C  29    10673   6566   8394  -1865  -1281   1845       C  
-ATOM   3426  CD  GLU C  29      -3.950 -16.751  31.918  1.00 74.55           C  
-ANISOU 3426  CD  GLU C  29    11716   7368   9243  -2169  -1432   2109       C  
-ATOM   3427  OE1 GLU C  29      -3.782 -16.781  33.159  1.00 72.00           O  
-ANISOU 3427  OE1 GLU C  29    11426   7216   8714  -2330  -1467   2305       O  
-ATOM   3428  OE2 GLU C  29      -4.695 -17.543  31.303  1.00 80.46           O  
-ANISOU 3428  OE2 GLU C  29    12500   7931  10142  -2226  -1502   2072       O  
-ATOM   3429  N   ASP C  30      -3.269 -11.089  31.026  1.00 44.22           N  
-ANISOU 3429  N   ASP C  30     7083   4763   4954  -1687   -295   1243       N  
-ATOM   3430  CA  ASP C  30      -2.854  -9.886  31.750  1.00 41.20           C  
-ANISOU 3430  CA  ASP C  30     6641   4657   4355  -1703   -131   1181       C  
-ATOM   3431  C   ASP C  30      -3.671  -8.645  31.399  1.00 39.35           C  
-ANISOU 3431  C   ASP C  30     6248   4636   4067  -1700    173    976       C  
-ATOM   3432  O   ASP C  30      -3.461  -7.565  31.961  1.00 40.26           O  
-ANISOU 3432  O   ASP C  30     6330   4951   4016  -1715    318    886       O  
-ATOM   3433  CB  ASP C  30      -1.371  -9.625  31.458  1.00 40.99           C  
-ANISOU 3433  CB  ASP C  30     6584   4603   4387  -1450   -266   1095       C  
-ATOM   3434  CG  ASP C  30      -0.505 -10.843  31.737  1.00 46.49           C  
-ANISOU 3434  CG  ASP C  30     7410   5075   5178  -1376   -594   1272       C  
-ATOM   3435  OD1 ASP C  30      -0.758 -11.516  32.757  1.00 46.79           O  
-ANISOU 3435  OD1 ASP C  30     7607   5063   5108  -1597   -713   1525       O  
-ATOM   3436  OD2 ASP C  30       0.411 -11.131  30.937  1.00 50.58           O  
-ANISOU 3436  OD2 ASP C  30     7864   5480   5875  -1096   -739   1159       O  
-ATOM   3437  N   LEU C  31      -4.590  -8.788  30.454  1.00 34.91           N  
-ANISOU 3437  N   LEU C  31     5593   4016   3654  -1673    248    896       N  
-ATOM   3438  CA  LEU C  31      -5.370  -7.645  30.004  1.00 39.30           C  
-ANISOU 3438  CA  LEU C  31     5986   4742   4202  -1626    496    710       C  
-ATOM   3439  C   LEU C  31      -6.837  -7.927  30.252  1.00 41.74           C  
-ANISOU 3439  C   LEU C  31     6229   5165   4465  -1833    628    772       C  
-ATOM   3440  O   LEU C  31      -7.283  -9.062  30.107  1.00 42.89           O  
-ANISOU 3440  O   LEU C  31     6430   5184   4681  -1969    504    917       O  
-ATOM   3441  CB  LEU C  31      -5.130  -7.381  28.517  1.00 29.78           C  
-ANISOU 3441  CB  LEU C  31     4675   3435   3204  -1394    469    548       C  
-ATOM   3442  CG  LEU C  31      -3.694  -7.114  28.086  1.00 30.91           C  
-ANISOU 3442  CG  LEU C  31     4828   3528   3388  -1198    350    473       C  
-ATOM   3443  CD1 LEU C  31      -3.587  -6.927  26.578  1.00 29.88           C  
-ANISOU 3443  CD1 LEU C  31     4576   3357   3419  -1020    338    324       C  
-ATOM   3444  CD2 LEU C  31      -3.192  -5.872  28.807  1.00 34.22           C  
-ANISOU 3444  CD2 LEU C  31     5248   4111   3642  -1210    459    417       C  
-ATOM   3445  N   GLU C  32      -7.596  -6.908  30.635  1.00 39.78           N  
-ANISOU 3445  N   GLU C  32     5857   5159   4098  -1860    869    655       N  
-ATOM   3446  CA AGLU C  32      -9.012  -7.145  30.834  0.54 43.74           C  
-ANISOU 3446  CA AGLU C  32     6233   5839   4548  -2044   1011    695       C  
-ATOM   3447  CA BGLU C  32      -9.028  -7.051  30.860  0.46 43.91           C  
-ANISOU 3447  CA BGLU C  32     6247   5876   4562  -2037   1027    682       C  
-ATOM   3448  C   GLU C  32      -9.788  -6.892  29.545  1.00 43.29           C  
-ANISOU 3448  C   GLU C  32     5997   5752   4698  -1905   1064    572       C  
-ATOM   3449  O   GLU C  32     -10.637  -7.708  29.185  1.00 43.57           O  
-ANISOU 3449  O   GLU C  32     5973   5784   4796  -2052   1028    667       O  
-ATOM   3450  CB AGLU C  32      -9.575  -6.367  32.031  0.54 47.32           C  
-ANISOU 3450  CB AGLU C  32     6615   6624   4741  -2160   1246    629       C  
-ATOM   3451  CB BGLU C  32      -9.500  -5.992  31.860  0.46 46.35           C  
-ANISOU 3451  CB BGLU C  32     6468   6495   4648  -2075   1276    556       C  
-ATOM   3452  CG AGLU C  32     -10.680  -7.114  32.818  0.54 51.58           C  
-ANISOU 3452  CG AGLU C  32     7069   7378   5153  -2401   1278    762       C  
-ATOM   3453  CG BGLU C  32     -10.880  -6.248  32.447  0.46 51.70           C  
-ANISOU 3453  CG BGLU C  32     6981   7458   5206  -2261   1421    590       C  
-ATOM   3454  CD AGLU C  32     -10.187  -8.347  33.594  0.54 50.54           C  
-ANISOU 3454  CD AGLU C  32     7129   7137   4937  -2605   1042   1025       C  
-ATOM   3455  CD BGLU C  32     -11.876  -5.143  32.137  0.46 56.41           C  
-ANISOU 3455  CD BGLU C  32     7331   8267   5836  -2105   1667    351       C  
-ATOM   3456  OE1AGLU C  32      -9.649  -9.292  32.980  0.54 47.38           O  
-ANISOU 3456  OE1AGLU C  32     6874   6430   4697  -2620    814   1173       O  
-ATOM   3457  OE1BGLU C  32     -11.487  -3.957  32.157  0.46 58.29           O  
-ANISOU 3457  OE1BGLU C  32     7574   8506   6067  -1906   1775    139       O  
-ATOM   3458  OE2AGLU C  32     -10.357  -8.376  34.829  0.54 52.59           O  
-ANISOU 3458  OE2AGLU C  32     7393   7615   4973  -2746   1075   1074       O  
-ATOM   3459  OE2BGLU C  32     -13.053  -5.468  31.872  0.46 59.78           O  
-ANISOU 3459  OE2BGLU C  32     7560   8840   6314  -2161   1721    372       O  
-ATOM   3460  N   ARG C  33      -9.470  -5.808  28.832  1.00 38.05           N  
-ANISOU 3460  N   ARG C  33     5263   5060   4135  -1652   1118    385       N  
-ATOM   3461  CA  ARG C  33     -10.181  -5.431  27.617  1.00 37.00           C  
-ANISOU 3461  CA  ARG C  33     4958   4920   4180  -1518   1154    284       C  
-ATOM   3462  C   ARG C  33      -9.305  -4.586  26.716  1.00 34.39           C  
-ANISOU 3462  C   ARG C  33     4644   4461   3961  -1280   1094    163       C  
-ATOM   3463  O   ARG C  33      -8.367  -3.937  27.182  1.00 31.78           O  
-ANISOU 3463  O   ARG C  33     4415   4107   3555  -1213   1092    115       O  
-ATOM   3464  CB  ARG C  33     -11.407  -4.579  27.958  1.00 46.03           C  
-ANISOU 3464  CB  ARG C  33     5897   6319   5273  -1503   1379    177       C  
-ATOM   3465  CG  ARG C  33     -12.449  -5.243  28.834  1.00 60.35           C  
-ANISOU 3465  CG  ARG C  33     7618   8375   6936  -1764   1487    279       C  
-ATOM   3466  CD  ARG C  33     -13.235  -6.306  28.084  1.00 66.93           C  
-ANISOU 3466  CD  ARG C  33     8366   9184   7879  -1920   1393    408       C  
-ATOM   3467  NE  ARG C  33     -14.445  -5.747  27.492  1.00 73.47           N  
-ANISOU 3467  NE  ARG C  33     8910  10211   8794  -1838   1520    307       N  
-ATOM   3468  CZ  ARG C  33     -15.454  -6.474  27.028  1.00 77.63           C  
-ANISOU 3468  CZ  ARG C  33     9284  10842   9370  -2012   1495    398       C  
-ATOM   3469  NH1 ARG C  33     -15.396  -7.798  27.081  1.00 78.60           N  
-ANISOU 3469  NH1 ARG C  33     9547  10845   9471  -2291   1340    590       N  
-ATOM   3470  NH2 ARG C  33     -16.521  -5.877  26.512  1.00 79.10           N  
-ANISOU 3470  NH2 ARG C  33     9182  11241   9634  -1910   1603    303       N  
-ATOM   3471  N   VAL C  34      -9.632  -4.556  25.427  1.00 32.21           N  
-ANISOU 3471  N   VAL C  34     4263   4130   3844  -1183   1043    123       N  
-ATOM   3472  CA  VAL C  34      -9.056  -3.541  24.550  1.00 28.12           C  
-ANISOU 3472  CA  VAL C  34     3722   3558   3405   -995   1014     24       C  
-ATOM   3473  C   VAL C  34      -9.832  -2.250  24.830  1.00 29.40           C  
-ANISOU 3473  C   VAL C  34     3778   3823   3571   -901   1168    -76       C  
-ATOM   3474  O   VAL C  34     -11.060  -2.257  24.861  1.00 32.67           O  
-ANISOU 3474  O   VAL C  34     4032   4364   4017   -917   1265    -88       O  
-ATOM   3475  CB  VAL C  34      -9.143  -3.932  23.068  1.00 31.84           C  
-ANISOU 3475  CB  VAL C  34     4117   3972   4009   -944    898     20       C  
-ATOM   3476  CG1 VAL C  34      -8.674  -2.779  22.183  1.00 32.33           C  
-ANISOU 3476  CG1 VAL C  34     4142   4026   4118   -798    873    -45       C  
-ATOM   3477  CG2 VAL C  34      -8.311  -5.169  22.804  1.00 34.55           C  
-ANISOU 3477  CG2 VAL C  34     4574   4192   4361   -984    741     59       C  
-ATOM   3478  N   PHE C  35      -9.124  -1.152  25.069  1.00 30.75           N  
-ANISOU 3478  N   PHE C  35     4033   3940   3711   -801   1180   -155       N  
-ATOM   3479  CA  PHE C  35      -9.780   0.083  25.498  1.00 31.57           C  
-ANISOU 3479  CA  PHE C  35     4082   4087   3827   -686   1307   -284       C  
-ATOM   3480  C   PHE C  35      -9.838   1.065  24.323  1.00 33.36           C  
-ANISOU 3480  C   PHE C  35     4258   4201   4216   -528   1225   -312       C  
-ATOM   3481  O   PHE C  35     -10.870   1.684  24.053  1.00 34.59           O  
-ANISOU 3481  O   PHE C  35     4273   4386   4482   -401   1276   -371       O  
-ATOM   3482  CB  PHE C  35      -9.019   0.683  26.681  1.00 35.32           C  
-ANISOU 3482  CB  PHE C  35     4722   4550   4149   -712   1359   -366       C  
-ATOM   3483  CG  PHE C  35      -9.814   1.678  27.478  1.00 39.94           C  
-ANISOU 3483  CG  PHE C  35     5262   5212   4703   -612   1522   -546       C  
-ATOM   3484  CD1 PHE C  35     -10.977   1.296  28.124  1.00 43.76           C  
-ANISOU 3484  CD1 PHE C  35     5586   5921   5120   -649   1688   -591       C  
-ATOM   3485  CD2 PHE C  35      -9.383   2.992  27.594  1.00 42.45           C  
-ANISOU 3485  CD2 PHE C  35     5695   5384   5050   -489   1504   -685       C  
-ATOM   3486  CE1 PHE C  35     -11.711   2.212  28.862  1.00 48.32           C  
-ANISOU 3486  CE1 PHE C  35     6090   6612   5659   -522   1855   -806       C  
-ATOM   3487  CE2 PHE C  35     -10.105   3.914  28.330  1.00 46.12           C  
-ANISOU 3487  CE2 PHE C  35     6131   5892   5501   -357   1644   -902       C  
-ATOM   3488  CZ  PHE C  35     -11.274   3.524  28.965  1.00 47.20           C  
-ANISOU 3488  CZ  PHE C  35     6078   6288   5569   -352   1831   -981       C  
-ATOM   3489  N   ILE C  36      -8.721   1.197  23.619  1.00 28.56           N  
-ANISOU 3489  N   ILE C  36     3752   3486   3615   -541   1085   -256       N  
-ATOM   3490  CA  ILE C  36      -8.670   2.001  22.407  1.00 28.88           C  
-ANISOU 3490  CA  ILE C  36     3757   3443   3772   -456    974   -226       C  
-ATOM   3491  C   ILE C  36      -7.909   1.219  21.353  1.00 29.20           C  
-ANISOU 3491  C   ILE C  36     3785   3515   3793   -534    848   -134       C  
-ATOM   3492  O   ILE C  36      -6.686   1.107  21.426  1.00 25.96           O  
-ANISOU 3492  O   ILE C  36     3475   3099   3291   -595    788   -119       O  
-ATOM   3493  CB  ILE C  36      -7.966   3.362  22.640  1.00 26.04           C  
-ANISOU 3493  CB  ILE C  36     3548   2938   3407   -414    928   -274       C  
-ATOM   3494  CG1 ILE C  36      -8.412   3.999  23.951  1.00 29.29           C  
-ANISOU 3494  CG1 ILE C  36     4022   3321   3786   -345   1062   -428       C  
-ATOM   3495  CG2 ILE C  36      -8.202   4.315  21.463  1.00 32.18           C  
-ANISOU 3495  CG2 ILE C  36     4294   3611   4323   -335    801   -213       C  
-ATOM   3496  CD1 ILE C  36      -7.712   5.315  24.288  1.00 31.32           C  
-ANISOU 3496  CD1 ILE C  36     4471   3393   4037   -323   1000   -505       C  
-ATOM   3497  N   PRO C  37      -8.634   0.646  20.377  1.00 25.76           N  
-ANISOU 3497  N   PRO C  37     3211   3144   3433   -531    809    -91       N  
-ATOM   3498  CA  PRO C  37      -8.015  -0.087  19.267  1.00 25.19           C  
-ANISOU 3498  CA  PRO C  37     3113   3126   3333   -588    696    -52       C  
-ATOM   3499  C   PRO C  37      -6.953   0.747  18.557  1.00 27.29           C  
-ANISOU 3499  C   PRO C  37     3427   3395   3545   -600    598    -17       C  
-ATOM   3500  O   PRO C  37      -7.135   1.960  18.378  1.00 26.06           O  
-ANISOU 3500  O   PRO C  37     3292   3172   3438   -566    567     22       O  
-ATOM   3501  CB  PRO C  37      -9.204  -0.335  18.334  1.00 24.02           C  
-ANISOU 3501  CB  PRO C  37     2804   3045   3278   -578    669    -21       C  
-ATOM   3502  CG  PRO C  37     -10.366  -0.467  19.278  1.00 29.92           C  
-ANISOU 3502  CG  PRO C  37     3483   3809   4078   -560    793    -45       C  
-ATOM   3503  CD  PRO C  37     -10.109   0.600  20.313  1.00 26.67           C  
-ANISOU 3503  CD  PRO C  37     3165   3320   3647   -481    874    -97       C  
-ATOM   3504  N   HIS C  38      -5.859   0.102  18.160  1.00 24.69           N  
-ANISOU 3504  N   HIS C  38     2727   3031   3624   -648   -266    159       N  
-ATOM   3505  CA  HIS C  38      -4.760   0.770  17.454  1.00 23.67           C  
-ANISOU 3505  CA  HIS C  38     2575   2761   3656   -496    -73     36       C  
-ATOM   3506  C   HIS C  38      -5.257   1.623  16.298  1.00 24.12           C  
-ANISOU 3506  C   HIS C  38     2770   2866   3528   -396    143   -110       C  
-ATOM   3507  O   HIS C  38      -4.851   2.775  16.140  1.00 23.47           O  
-ANISOU 3507  O   HIS C  38     2696   2811   3410   -341    286   -169       O  
-ATOM   3508  CB  HIS C  38      -3.761  -0.269  16.926  1.00 25.85           C  
-ANISOU 3508  CB  HIS C  38     2784   2737   4301   -416    -65      7       C  
-ATOM   3509  CG  HIS C  38      -2.626   0.325  16.147  1.00 28.07           C  
-ANISOU 3509  CG  HIS C  38     3014   2889   4763   -291    184   -150       C  
-ATOM   3510  ND1 HIS C  38      -2.575   0.294  14.769  1.00 29.11           N  
-ANISOU 3510  ND1 HIS C  38     3275   2917   4867   -223    444   -355       N  
-ATOM   3511  CD2 HIS C  38      -1.512   0.978  16.552  1.00 27.48           C  
-ANISOU 3511  CD2 HIS C  38     2778   2797   4868   -270    220   -135       C  
-ATOM   3512  CE1 HIS C  38      -1.469   0.891  14.361  1.00 29.32           C  
-ANISOU 3512  CE1 HIS C  38     3219   2867   5055   -163    657   -467       C  
-ATOM   3513  NE2 HIS C  38      -0.806   1.316  15.420  1.00 30.21           N  
-ANISOU 3513  NE2 HIS C  38     3138   3024   5317   -177    521   -334       N  
-ATOM   3514  N   GLY C  39      -6.146   1.056  15.486  1.00 23.57           N  
-ANISOU 3514  N   GLY C  39     2820   2800   3337   -405    137   -143       N  
-ATOM   3515  CA  GLY C  39      -6.601   1.760  14.304  1.00 27.30           C  
-ANISOU 3515  CA  GLY C  39     3438   3311   3622   -354    274   -225       C  
-ATOM   3516  C   GLY C  39      -7.369   3.033  14.624  1.00 23.77           C  
-ANISOU 3516  C   GLY C  39     2968   3045   3018   -317    270   -172       C  
-ATOM   3517  O   GLY C  39      -7.311   4.014  13.873  1.00 25.10           O  
-ANISOU 3517  O   GLY C  39     3225   3194   3116   -251    381   -195       O  
-ATOM   3518  N   LEU C  40      -8.101   3.019  15.728  1.00 26.12           N  
-ANISOU 3518  N   LEU C  40     3149   3500   3276   -375    157   -106       N  
-ATOM   3519  CA  LEU C  40      -8.814   4.208  16.188  1.00 29.51           C  
-ANISOU 3519  CA  LEU C  40     3509   4066   3635   -329    204   -112       C  
-ATOM   3520  C   LEU C  40      -7.828   5.303  16.588  1.00 26.72           C  
-ANISOU 3520  C   LEU C  40     3150   3639   3363   -283    342   -174       C  
-ATOM   3521  O   LEU C  40      -8.055   6.493  16.325  1.00 24.16           O  
-ANISOU 3521  O   LEU C  40     2849   3288   3042   -187    445   -208       O  
-ATOM   3522  CB  LEU C  40      -9.729   3.861  17.367  1.00 30.41           C  
-ANISOU 3522  CB  LEU C  40     3491   4381   3681   -456    119    -84       C  
-ATOM   3523  CG  LEU C  40     -10.489   5.066  17.927  1.00 33.64           C  
-ANISOU 3523  CG  LEU C  40     3791   4912   4078   -407    237   -161       C  
-ATOM   3524  CD1 LEU C  40     -11.244   5.783  16.799  1.00 35.35           C  
-ANISOU 3524  CD1 LEU C  40     4008   5080   4342   -226    249   -137       C  
-ATOM   3525  CD2 LEU C  40     -11.429   4.660  19.044  1.00 38.62           C  
-ANISOU 3525  CD2 LEU C  40     4285   5774   4616   -582    216   -178       C  
-ATOM   3526  N   ILE C  41      -6.735   4.895  17.229  1.00 18.85           N  
-ANISOU 3526  N   ILE C  41     2113   2589   2461   -364    320   -171       N  
-ATOM   3527  CA  ILE C  41      -5.648   5.820  17.554  1.00 22.03           C  
-ANISOU 3527  CA  ILE C  41     2501   2922   2948   -364    428   -224       C  
-ATOM   3528  C   ILE C  41      -5.084   6.444  16.283  1.00 22.34           C  
-ANISOU 3528  C   ILE C  41     2648   2806   3035   -249    586   -272       C  
-ATOM   3529  O   ILE C  41      -4.794   7.644  16.239  1.00 23.14           O  
-ANISOU 3529  O   ILE C  41     2791   2859   3142   -221    708   -317       O  
-ATOM   3530  CB  ILE C  41      -4.517   5.103  18.323  1.00 21.02           C  
-ANISOU 3530  CB  ILE C  41     2268   2758   2960   -480    311   -162       C  
-ATOM   3531  CG1 ILE C  41      -5.023   4.623  19.677  1.00 23.31           C  
-ANISOU 3531  CG1 ILE C  41     2497   3227   3133   -676    133    -75       C  
-ATOM   3532  CG2 ILE C  41      -3.319   6.028  18.520  1.00 21.91           C  
-ANISOU 3532  CG2 ILE C  41     2343   2806   3176   -502    410   -212       C  
-ATOM   3533  CD1 ILE C  41      -3.967   3.912  20.529  1.00 27.23           C  
-ANISOU 3533  CD1 ILE C  41     2888   3692   3768   -829    -76     69       C  
-ATOM   3534  N   MET C  42      -4.900   5.619  15.252  1.00 20.54           N  
-ANISOU 3534  N   MET C  42     2485   2489   2829   -220    601   -275       N  
-ATOM   3535  CA  MET C  42      -4.381   6.103  13.990  1.00 24.52           C  
-ANISOU 3535  CA  MET C  42     3127   2880   3311   -185    774   -329       C  
-ATOM   3536  C   MET C  42      -5.311   7.138  13.374  1.00 23.77           C  
-ANISOU 3536  C   MET C  42     3168   2817   3048   -138    778   -269       C  
-ATOM   3537  O   MET C  42      -4.860   8.190  12.895  1.00 23.81           O  
-ANISOU 3537  O   MET C  42     3268   2737   3041   -131    900   -266       O  
-ATOM   3538  CB  MET C  42      -4.143   4.937  13.022  1.00 26.44           C  
-ANISOU 3538  CB  MET C  42     3438   3038   3569   -213    823   -396       C  
-ATOM   3539  CG  MET C  42      -3.082   3.957  13.479  1.00 28.26           C  
-ANISOU 3539  CG  MET C  42     3499   3148   4089   -215    835   -453       C  
-ATOM   3540  SD  MET C  42      -1.470   4.728  13.708  1.00 35.42           S  
-ANISOU 3540  SD  MET C  42     4256   3967   5235   -211   1007   -513       S  
-ATOM   3541  CE  MET C  42      -1.541   5.070  15.468  1.00 46.73           C  
-ANISOU 3541  CE  MET C  42     5521   5523   6710   -258    759   -368       C  
-ATOM   3542  N   ASP C  43      -6.604   6.844  13.386  1.00 22.90           N  
-ANISOU 3542  N   ASP C  43     3047   2814   2839   -115    627   -198       N  
-ATOM   3543  CA  ASP C  43      -7.576   7.743  12.779  1.00 24.57           C  
-ANISOU 3543  CA  ASP C  43     3330   3038   2968    -49    570    -95       C  
-ATOM   3544  C   ASP C  43      -7.596   9.085  13.499  1.00 23.14           C  
-ANISOU 3544  C   ASP C  43     3079   2798   2916     40    640   -106       C  
-ATOM   3545  O   ASP C  43      -7.666  10.138  12.860  1.00 24.25           O  
-ANISOU 3545  O   ASP C  43     3323   2818   3074     96    665    -28       O  
-ATOM   3546  CB  ASP C  43      -8.977   7.146  12.842  1.00 24.51           C  
-ANISOU 3546  CB  ASP C  43     3236   3178   2900    -42    383    -20       C  
-ATOM   3547  CG  ASP C  43      -9.168   5.972  11.881  1.00 31.81           C  
-ANISOU 3547  CG  ASP C  43     4287   4136   3662   -160    298     -4       C  
-ATOM   3548  OD1 ASP C  43      -8.472   5.895  10.837  1.00 29.41           O  
-ANISOU 3548  OD1 ASP C  43     4181   3744   3249   -238    393    -36       O  
-ATOM   3549  OD2 ASP C  43     -10.037   5.133  12.177  1.00 32.79           O  
-ANISOU 3549  OD2 ASP C  43     4322   4380   3755   -207    159     19       O  
-ATOM   3550  N   ARG C  44      -7.571   9.046  14.825  1.00 22.46           N  
-ANISOU 3550  N   ARG C  44     2839   2785   2910     23    666   -201       N  
-ATOM   3551  CA  ARG C  44      -7.611  10.272  15.618  1.00 22.99           C  
-ANISOU 3551  CA  ARG C  44     2852   2791   3090     66    775   -281       C  
-ATOM   3552  C   ARG C  44      -6.316  11.042  15.393  1.00 25.06           C  
-ANISOU 3552  C   ARG C  44     3231   2893   3399     25    910   -317       C  
-ATOM   3553  O   ARG C  44      -6.312  12.269  15.275  1.00 27.16           O  
-ANISOU 3553  O   ARG C  44     3562   3002   3757     82    997   -325       O  
-ATOM   3554  CB  ARG C  44      -7.798   9.936  17.107  1.00 23.44           C  
-ANISOU 3554  CB  ARG C  44     2762   3010   3135    -41    789   -400       C  
-ATOM   3555  CG  ARG C  44      -7.812  11.149  18.057  1.00 25.43           C  
-ANISOU 3555  CG  ARG C  44     2980   3212   3470    -59    955   -562       C  
-ATOM   3556  CD  ARG C  44      -8.782  12.244  17.595  1.00 26.00           C  
-ANISOU 3556  CD  ARG C  44     3025   3133   3722    143   1022   -569       C  
-ATOM   3557  NE  ARG C  44      -8.790  13.380  18.520  1.00 27.18           N  
-ANISOU 3557  NE  ARG C  44     3148   3183   3998    126   1229   -783       N  
-ATOM   3558  CZ  ARG C  44      -9.108  14.621  18.169  1.00 28.96           C  
-ANISOU 3558  CZ  ARG C  44     3391   3146   4465    295   1327   -810       C  
-ATOM   3559  NH1 ARG C  44      -9.463  14.877  16.915  1.00 27.78           N  
-ANISOU 3559  NH1 ARG C  44     3287   2839   4430    478   1187   -581       N  
-ATOM   3560  NH2 ARG C  44      -9.075  15.597  19.065  1.00 29.15           N  
-ANISOU 3560  NH2 ARG C  44     3405   3053   4618    256   1551  -1059       N  
-ATOM   3561  N   THR C  45      -5.210  10.309  15.322  1.00 22.89           N  
-ANISOU 3561  N   THR C  45     2962   2634   3102    -77    928   -336       N  
-ATOM   3562  CA  THR C  45      -3.895  10.932  15.144  1.00 25.73           C  
-ANISOU 3562  CA  THR C  45     3376   2872   3527   -148   1066   -379       C  
-ATOM   3563  C   THR C  45      -3.780  11.608  13.768  1.00 26.40           C  
-ANISOU 3563  C   THR C  45     3655   2815   3561   -122   1151   -300       C  
-ATOM   3564  O   THR C  45      -3.159  12.669  13.639  1.00 24.62           O  
-ANISOU 3564  O   THR C  45     3514   2455   3387   -167   1269   -309       O  
-ATOM   3565  CB  THR C  45      -2.754   9.908  15.363  1.00 23.48           C  
-ANISOU 3565  CB  THR C  45     2976   2629   3316   -242   1059   -412       C  
-ATOM   3566  OG1 THR C  45      -2.838   9.386  16.696  1.00 20.70           O  
-ANISOU 3566  OG1 THR C  45     2475   2404   2987   -317    925   -421       O  
-ATOM   3567  CG2 THR C  45      -1.380  10.551  15.160  1.00 26.41           C  
-ANISOU 3567  CG2 THR C  45     3344   2898   3795   -328   1214   -462       C  
-ATOM   3568  N   GLU C  46      -4.379  10.998  12.745  1.00 23.42           N  
-ANISOU 3568  N   GLU C  46     3372   2472   3053    -98   1078   -211       N  
-ATOM   3569  CA  GLU C  46      -4.436  11.617  11.428  1.00 24.52           C  
-ANISOU 3569  CA  GLU C  46     3736   2513   3066   -138   1107    -90       C  
-ATOM   3570  C   GLU C  46      -5.057  13.006  11.505  1.00 25.98           C  
-ANISOU 3570  C   GLU C  46     3978   2551   3344    -45   1053     27       C  
-ATOM   3571  O   GLU C  46      -4.552  13.959  10.912  1.00 25.66           O  
-ANISOU 3571  O   GLU C  46     4104   2352   3295   -112   1131    105       O  
-ATOM   3572  CB  GLU C  46      -5.238  10.749  10.441  1.00 22.65           C  
-ANISOU 3572  CB  GLU C  46     3602   2375   2631   -169    977      0       C  
-ATOM   3573  CG  GLU C  46      -5.344  11.384   9.059  1.00 29.61           C  
-ANISOU 3573  CG  GLU C  46     4755   3189   3307   -284    959    169       C  
-ATOM   3574  CD  GLU C  46      -6.163  10.540   8.086  1.00 34.78           C  
-ANISOU 3574  CD  GLU C  46     5537   3969   3708   -383    800    258       C  
-ATOM   3575  OE1 GLU C  46      -6.843   9.603   8.531  1.00 45.60           O  
-ANISOU 3575  OE1 GLU C  46     6764   5455   5107   -320    683    208       O  
-ATOM   3576  OE2 GLU C  46      -6.110  10.817   6.879  1.00 35.50           O  
-ANISOU 3576  OE2 GLU C  46     5892   4053   3544   -570    790    381       O  
-ATOM   3577  N   ARG C  47      -6.144  13.118  12.258  1.00 23.29           N  
-ANISOU 3577  N   ARG C  47     3484   2240   3125    102    937     29       N  
-ATOM   3578  CA  ARG C  47      -6.836  14.394  12.396  1.00 25.20           C  
-ANISOU 3578  CA  ARG C  47     3721   2292   3561    237    903    106       C  
-ATOM   3579  C   ARG C  47      -6.022  15.368  13.253  1.00 29.90           C  
-ANISOU 3579  C   ARG C  47     4318   2731   4311    204   1096    -55       C  
-ATOM   3580  O   ARG C  47      -5.988  16.563  12.965  1.00 30.32           O  
-ANISOU 3580  O   ARG C  47     4486   2531   4505    241   1128     20       O  
-ATOM   3581  CB  ARG C  47      -8.232  14.173  12.991  1.00 26.33           C  
-ANISOU 3581  CB  ARG C  47     3642   2525   3838    399    783     96       C  
-ATOM   3582  CG  ARG C  47      -8.956  15.467  13.360  1.00 27.98           C  
-ANISOU 3582  CG  ARG C  47     3762   2500   4370    581    805    100       C  
-ATOM   3583  CD  ARG C  47      -8.963  16.448  12.210  1.00 50.43           C  
-ANISOU 3583  CD  ARG C  47     6793   5075   7291    624    688    369       C  
-ATOM   3584  NE  ARG C  47     -10.313  16.691  11.731  1.00 57.42           N  
-ANISOU 3584  NE  ARG C  47     7543   5893   8380    809    445    592       N  
-ATOM   3585  CZ  ARG C  47     -11.032  17.767  12.012  1.00 50.59           C  
-ANISOU 3585  CZ  ARG C  47     6533   4751   7937   1030    432    624       C  
-ATOM   3586  NH1 ARG C  47     -10.532  18.741  12.756  1.00 57.85           N  
-ANISOU 3586  NH1 ARG C  47     7477   5418   9085   1071    672    419       N  
-ATOM   3587  NH2 ARG C  47     -12.255  17.868  11.527  1.00 52.69           N  
-ANISOU 3587  NH2 ARG C  47     6616   4975   8429   1203    169    860       N  
-ATOM   3588  N   LEU C  48      -5.341  14.869  14.284  1.00 26.83           N  
-ANISOU 3588  N   LEU C  48     3819   2479   3896    104   1198   -254       N  
-ATOM   3589  CA  LEU C  48      -4.501  15.762  15.104  1.00 30.48           C  
-ANISOU 3589  CA  LEU C  48     4297   2824   4459      3   1360   -411       C  
-ATOM   3590  C   LEU C  48      -3.348  16.358  14.298  1.00 28.59           C  
-ANISOU 3590  C   LEU C  48     4233   2434   4195   -123   1455   -341       C  
-ATOM   3591  O   LEU C  48      -2.953  17.503  14.513  1.00 30.72           O  
-ANISOU 3591  O   LEU C  48     4593   2495   4583   -177   1562   -389       O  
-ATOM   3592  CB  LEU C  48      -3.943  15.046  16.334  1.00 30.66           C  
-ANISOU 3592  CB  LEU C  48     4172   3058   4418   -142   1382   -581       C  
-ATOM   3593  CG  LEU C  48      -4.897  14.690  17.474  1.00 33.68           C  
-ANISOU 3593  CG  LEU C  48     4408   3599   4790   -126   1353   -705       C  
-ATOM   3594  CD1 LEU C  48      -4.134  14.020  18.609  1.00 29.70           C  
-ANISOU 3594  CD1 LEU C  48     3814   3299   4170   -353   1325   -802       C  
-ATOM   3595  CD2 LEU C  48      -5.660  15.909  17.991  1.00 33.44           C  
-ANISOU 3595  CD2 LEU C  48     4381   3395   4928    -44   1492   -853       C  
-ATOM   3596  N   ALA C  49      -2.787  15.576  13.391  1.00 27.05           N  
-ANISOU 3596  N   ALA C  49     4086   2339   3852   -200   1448   -256       N  
-ATOM   3597  CA  ALA C  49      -1.695  16.069  12.555  1.00 25.92           C  
-ANISOU 3597  CA  ALA C  49     4097   2092   3660   -362   1586   -207       C  
-ATOM   3598  C   ALA C  49      -2.177  17.263  11.744  1.00 29.35           C  
-ANISOU 3598  C   ALA C  49     4764   2276   4110   -340   1553    -17       C  
-ATOM   3599  O   ALA C  49      -1.449  18.243  11.557  1.00 30.16           O  
-ANISOU 3599  O   ALA C  49     5001   2197   4260   -472   1670      4       O  
-ATOM   3600  CB  ALA C  49      -1.193  14.979  11.643  1.00 25.49           C  
-ANISOU 3600  CB  ALA C  49     4053   2185   3446   -449   1632   -193       C  
-ATOM   3601  N   ARG C  50      -3.415  17.186  11.263  1.00 29.54           N  
-ANISOU 3601  N   ARG C  50     4827   2281   4118   -186   1364    151       N  
-ATOM   3602  CA  ARG C  50      -3.972  18.295  10.486  1.00 31.91           C  
-ANISOU 3602  CA  ARG C  50     5322   2313   4488   -147   1251    405       C  
-ATOM   3603  C   ARG C  50      -4.191  19.523  11.376  1.00 33.39           C  
-ANISOU 3603  C   ARG C  50     5466   2210   5011    -25   1304    323       C  
-ATOM   3604  O   ARG C  50      -3.896  20.657  10.978  1.00 36.03           O  
-ANISOU 3604  O   ARG C  50     5991   2246   5454    -88   1327    451       O  
-ATOM   3605  CB  ARG C  50      -5.280  17.869   9.805  1.00 34.31           C  
-ANISOU 3605  CB  ARG C  50     5620   2681   4736    -15    981    630       C  
-ATOM   3606  CG  ARG C  50      -5.647  18.740   8.594  1.00 45.23           C  
-ANISOU 3606  CG  ARG C  50     7257   3845   6084    -72    788   1001       C  
-ATOM   3607  CD  ARG C  50      -6.891  18.216   7.894  1.00 53.49           C  
-ANISOU 3607  CD  ARG C  50     8275   5005   7045      7    469   1249       C  
-ATOM   3608  NE  ARG C  50      -8.115  18.557   8.616  1.00 56.55           N  
-ANISOU 3608  NE  ARG C  50     8383   5272   7830    325    315   1268       N  
-ATOM   3609  CZ  ARG C  50      -9.304  17.999   8.397  1.00 58.28           C  
-ANISOU 3609  CZ  ARG C  50     8437   5629   8078    445     57   1406       C  
-ATOM   3610  NH1 ARG C  50      -9.441  17.051   7.482  1.00 55.03           N  
-ANISOU 3610  NH1 ARG C  50     8151   5477   7281    254    -98   1538       N  
-ATOM   3611  NH2 ARG C  50     -10.357  18.386   9.101  1.00 60.65           N  
-ANISOU 3611  NH2 ARG C  50     8434   5809   8802    735    -24   1385       N  
-ATOM   3612  N   ASP C  51      -4.699  19.293  12.586  1.00 35.03           N  
-ANISOU 3612  N   ASP C  51     5442   2493   5375    115   1343     93       N  
-ATOM   3613  CA  ASP C  51      -4.912  20.394  13.538  1.00 40.75           C  
-ANISOU 3613  CA  ASP C  51     6123   2952   6409    200   1463    -82       C  
-ATOM   3614  C   ASP C  51      -3.582  21.076  13.897  1.00 34.39           C  
-ANISOU 3614  C   ASP C  51     5450   2031   5585    -38   1660   -224       C  
-ATOM   3615  O   ASP C  51      -3.505  22.298  13.989  1.00 37.13           O  
-ANISOU 3615  O   ASP C  51     5922   2027   6159    -41   1738   -239       O  
-ATOM   3616  CB  ASP C  51      -5.575  19.888  14.825  1.00 40.02           C  
-ANISOU 3616  CB  ASP C  51     5778   3042   6387    294   1528   -358       C  
-ATOM   3617  CG  ASP C  51      -6.979  19.322  14.607  1.00 43.09           C  
-ANISOU 3617  CG  ASP C  51     5986   3533   6852    521   1358   -248       C  
-ATOM   3618  OD1 ASP C  51      -7.612  19.606  13.568  1.00 41.54           O  
-ANISOU 3618  OD1 ASP C  51     5843   3188   6755    653   1164     44       O  
-ATOM   3619  OD2 ASP C  51      -7.459  18.606  15.516  1.00 41.69           O  
-ANISOU 3619  OD2 ASP C  51     5609   3598   6634    535   1403   -441       O  
-ATOM   3620  N   VAL C  52      -2.542  20.273  14.112  1.00 34.16           N  
-ANISOU 3620  N   VAL C  52     5371   2280   5329   -238   1730   -326       N  
-ATOM   3621  CA  VAL C  52      -1.201  20.796  14.414  1.00 37.38           C  
-ANISOU 3621  CA  VAL C  52     5848   2636   5718   -497   1890   -441       C  
-ATOM   3622  C   VAL C  52      -0.681  21.666  13.284  1.00 37.61           C  
-ANISOU 3622  C   VAL C  52     6128   2415   5748   -615   1926   -230       C  
-ATOM   3623  O   VAL C  52      -0.171  22.766  13.510  1.00 41.85           O  
-ANISOU 3623  O   VAL C  52     6766   2741   6393   -733   2009   -280       O  
-ATOM   3624  CB  VAL C  52      -0.181  19.650  14.658  1.00 34.29           C  
-ANISOU 3624  CB  VAL C  52     5292   2586   5149   -662   1913   -524       C  
-ATOM   3625  CG1 VAL C  52       1.240  20.212  14.766  1.00 34.95           C  
-ANISOU 3625  CG1 VAL C  52     5406   2623   5248   -941   2055   -595       C  
-ATOM   3626  CG2 VAL C  52      -0.540  18.868  15.903  1.00 32.41           C  
-ANISOU 3626  CG2 VAL C  52     4841   2582   4893   -626   1850   -699       C  
-ATOM   3627  N   MET C  53      -0.811  21.175  12.058  1.00 37.03           N  
-ANISOU 3627  N   MET C  53     6152   2422   5497   -615   1838      8       N  
-ATOM   3628  CA  MET C  53      -0.335  21.934  10.905  1.00 41.41           C  
-ANISOU 3628  CA  MET C  53     6983   2781   5971   -797   1865    243       C  
-ATOM   3629  C   MET C  53      -1.132  23.208  10.675  1.00 40.99           C  
-ANISOU 3629  C   MET C  53     7098   2328   6149   -672   1726    442       C  
-ATOM   3630  O   MET C  53      -0.567  24.241  10.328  1.00 43.78           O  
-ANISOU 3630  O   MET C  53     7592   2514   6527   -820   1728    528       O  
-ATOM   3631  CB  MET C  53      -0.333  21.066   9.649  1.00 43.15           C  
-ANISOU 3631  CB  MET C  53     7296   3219   5879   -887   1814    426       C  
-ATOM   3632  CG  MET C  53       0.865  20.133   9.539  1.00 45.05           C  
-ANISOU 3632  CG  MET C  53     7417   3755   5946  -1088   2027    242       C  
-ATOM   3633  SD  MET C  53       2.389  20.964   9.019  1.00 77.05           S  
-ANISOU 3633  SD  MET C  53    11547   7808   9921  -1400   2211    208       S  
-ATOM   3634  CE  MET C  53       3.173  21.248  10.597  1.00 63.11           C  
-ANISOU 3634  CE  MET C  53     9512   6052   8416  -1395   2293    -74       C  
-ATOM   3635  N   LYS C  54      -2.444  23.138  10.865  1.00 43.84           N  
-ANISOU 3635  N   LYS C  54     7369   2588   6700   -378   1559    509       N  
-ATOM   3636  CA  LYS C  54      -3.293  24.324  10.755  1.00 49.07           C  
-ANISOU 3636  CA  LYS C  54     8091   2851   7701   -192   1398    678       C  
-ATOM   3637  C   LYS C  54      -2.844  25.412  11.733  1.00 49.03           C  
-ANISOU 3637  C   LYS C  54     8038   2670   7923   -220   1532    407       C  
-ATOM   3638  O   LYS C  54      -2.911  26.609  11.438  1.00 50.41           O  
-ANISOU 3638  O   LYS C  54     8341   2513   8300   -216   1434    543       O  
-ATOM   3639  CB  LYS C  54      -4.758  23.951  11.008  1.00 55.65           C  
-ANISOU 3639  CB  LYS C  54     8720   3650   8775    154   1242    718       C  
-ATOM   3640  CG  LYS C  54      -5.761  25.053  10.670  1.00 67.91           C  
-ANISOU 3640  CG  LYS C  54    10262   4827  10712    379    991    952       C  
-ATOM   3641  CD  LYS C  54      -7.201  24.542  10.723  1.00 77.52           C  
-ANISOU 3641  CD  LYS C  54    11214   6089  12151    703    802   1037       C  
-ATOM   3642  CE  LYS C  54      -7.763  24.533  12.144  1.00 82.35           C  
-ANISOU 3642  CE  LYS C  54    11499   6770  13020    904   1002    590       C  
-ATOM   3643  NZ  LYS C  54      -9.052  23.773  12.245  1.00 83.87           N  
-ANISOU 3643  NZ  LYS C  54    11385   7125  13356   1158    869    625       N  
-ATOM   3644  N   GLU C  55      -2.357  24.978  12.891  1.00 46.14           N  
-ANISOU 3644  N   GLU C  55     7506   2532   7495   -284   1735     41       N  
-ATOM   3645  CA  GLU C  55      -2.014  25.878  13.990  1.00 48.79           C  
-ANISOU 3645  CA  GLU C  55     7791   2771   7976   -344   1872   -252       C  
-ATOM   3646  C   GLU C  55      -0.530  26.291  14.009  1.00 47.69           C  
-ANISOU 3646  C   GLU C  55     7764   2690   7665   -678   1993   -311       C  
-ATOM   3647  O   GLU C  55      -0.200  27.426  14.349  1.00 49.04           O  
-ANISOU 3647  O   GLU C  55     8020   2641   7973   -762   2042   -394       O  
-ATOM   3648  CB  GLU C  55      -2.405  25.200  15.306  1.00 51.33           C  
-ANISOU 3648  CB  GLU C  55     7873   3347   8282   -281   1983   -586       C  
-ATOM   3649  CG  GLU C  55      -2.115  25.996  16.540  1.00 57.26           C  
-ANISOU 3649  CG  GLU C  55     8586   4068   9103   -399   2140   -903       C  
-ATOM   3650  CD  GLU C  55      -3.337  26.142  17.427  1.00 65.91           C  
-ANISOU 3650  CD  GLU C  55     9508   5140  10397   -194   2191  -1115       C  
-ATOM   3651  OE1 GLU C  55      -4.225  25.256  17.377  1.00 62.12           O  
-ANISOU 3651  OE1 GLU C  55     8870   4817   9917    -11   2122  -1079       O  
-ATOM   3652  OE2 GLU C  55      -3.400  27.151  18.162  1.00 72.07           O  
-ANISOU 3652  OE2 GLU C  55    10306   5746  11330   -234   2318  -1327       O  
-ATOM   3653  N   MET C  56       0.357  25.376  13.625  1.00 43.47           N  
-ANISOU 3653  N   MET C  56     7210   2450   6857   -864   2044   -274       N  
-ATOM   3654  CA  MET C  56       1.802  25.608  13.722  1.00 52.06           C  
-ANISOU 3654  CA  MET C  56     8310   3667   7804  -1170   2162   -357       C  
-ATOM   3655  C   MET C  56       2.532  25.624  12.367  1.00 53.14           C  
-ANISOU 3655  C   MET C  56     8592   3833   7765  -1348   2160   -108       C  
-ATOM   3656  O   MET C  56       3.748  25.833  12.311  1.00 55.58           O  
-ANISOU 3656  O   MET C  56     8881   4259   7977  -1595   2263   -167       O  
-ATOM   3657  CB  MET C  56       2.443  24.554  14.638  1.00 52.42           C  
-ANISOU 3657  CB  MET C  56     8118   4078   7722  -1276   2236   -587       C  
-ATOM   3658  CG  MET C  56       1.821  24.449  16.027  1.00 52.13           C  
-ANISOU 3658  CG  MET C  56     7949   4095   7762  -1194   2244   -840       C  
-ATOM   3659  SD  MET C  56       2.662  23.261  17.098  1.00 47.68           S  
-ANISOU 3659  SD  MET C  56     7133   3950   7034  -1393   2241  -1030       S  
-ATOM   3660  CE  MET C  56       4.179  24.168  17.420  1.00 48.71           C  
-ANISOU 3660  CE  MET C  56     7281   4098   7127  -1716   2294  -1104       C  
-ATOM   3661  N   GLY C  57       1.792  25.417  11.280  1.00 51.08           N  
-ANISOU 3661  N   GLY C  57     8345   3436   7628   -842    184    349       N  
-ATOM   3662  CA  GLY C  57       2.394  25.222   9.969  1.00 54.55           C  
-ANISOU 3662  CA  GLY C  57     8746   4042   7940   -946    217    698       C  
-ATOM   3663  C   GLY C  57       3.144  26.406   9.378  1.00 64.85           C  
-ANISOU 3663  C   GLY C  57    10172   5088   9379  -1157    133   1003       C  
-ATOM   3664  O   GLY C  57       3.819  26.273   8.357  1.00 67.97           O  
-ANISOU 3664  O   GLY C  57    10515   5669   9640  -1293    171   1313       O  
-ATOM   3665  N   GLY C  58       3.038  27.565  10.017  1.00 66.23           N  
-ANISOU 3665  N   GLY C  58    10397   4949   9818  -1144     31    893       N  
-ATOM   3666  CA  GLY C  58       3.625  28.773   9.471  1.00 72.11           C  
-ANISOU 3666  CA  GLY C  58    11186   5491  10721  -1280    -14   1146       C  
-ATOM   3667  C   GLY C  58       5.065  29.027   9.875  1.00 71.95           C  
-ANISOU 3667  C   GLY C  58    11068   5536  10735  -1572     40   1171       C  
-ATOM   3668  O   GLY C  58       5.615  30.092   9.576  1.00 74.30           O  
-ANISOU 3668  O   GLY C  58    11418   5639  11172  -1709     18   1337       O  
-ATOM   3669  N   HIS C  59       5.680  28.058  10.549  1.00 65.23           N  
-ANISOU 3669  N   HIS C  59    10085   4959   9741  -1664    110   1004       N  
-ATOM   3670  CA  HIS C  59       7.067  28.207  10.978  1.00 66.22           C  
-ANISOU 3670  CA  HIS C  59    10095   5187   9878  -1917    151    999       C  
-ATOM   3671  C   HIS C  59       7.756  26.859  11.199  1.00 58.45           C  
-ANISOU 3671  C   HIS C  59     8962   4626   8620  -1993    248    929       C  
-ATOM   3672  O   HIS C  59       7.107  25.815  11.242  1.00 57.78           O  
-ANISOU 3672  O   HIS C  59     8876   4712   8367  -1852    297    826       O  
-ATOM   3673  CB  HIS C  59       7.148  29.043  12.259  1.00 71.59           C  
-ANISOU 3673  CB  HIS C  59    10796   5590  10814  -1932     77    704       C  
-ATOM   3674  CG  HIS C  59       8.451  29.758  12.436  1.00 77.50           C  
-ANISOU 3674  CG  HIS C  59    11483   6289  11674  -2191     90    761       C  
-ATOM   3675  ND1 HIS C  59       8.705  30.993  11.872  1.00 84.49           N  
-ANISOU 3675  ND1 HIS C  59    12472   6894  12737  -2303     70    955       N  
-ATOM   3676  CD2 HIS C  59       9.574  29.421  13.115  1.00 77.65           C  
-ANISOU 3676  CD2 HIS C  59    11361   6506  11638  -2361    115    648       C  
-ATOM   3677  CE1 HIS C  59       9.925  31.379  12.193  1.00 85.28           C  
-ANISOU 3677  CE1 HIS C  59    12485   7014  12904  -2544     92    951       C  
-ATOM   3678  NE2 HIS C  59      10.475  30.443  12.947  1.00 81.02           N  
-ANISOU 3678  NE2 HIS C  59    11785   6768  12232  -2574    115    762       N  
-ATOM   3679  N   HIS C  60       9.081  26.904  11.319  1.00 55.74           N  
-ANISOU 3679  N   HIS C  60     8498   4445   8236  -2211    288    975       N  
-ATOM   3680  CA  HIS C  60       9.877  25.748  11.697  1.00 48.89           C  
-ANISOU 3680  CA  HIS C  60     7485   3961   7130  -2278    371    865       C  
-ATOM   3681  C   HIS C  60       9.348  25.213  13.021  1.00 44.82           C  
-ANISOU 3681  C   HIS C  60     6991   3426   6613  -2152    363    517       C  
-ATOM   3682  O   HIS C  60       9.030  25.984  13.924  1.00 47.94           O  
-ANISOU 3682  O   HIS C  60     7449   3554   7210  -2115    278    328       O  
-ATOM   3683  CB  HIS C  60      11.342  26.164  11.861  1.00 55.32           C  
-ANISOU 3683  CB  HIS C  60     8183   4876   7959  -2514    383    909       C  
-ATOM   3684  CG  HIS C  60      12.273  25.025  12.146  1.00 63.34           C  
-ANISOU 3684  CG  HIS C  60     9043   6305   8719  -2574    460    810       C  
-ATOM   3685  ND1 HIS C  60      13.287  24.658  11.281  1.00 70.54           N  
-ANISOU 3685  ND1 HIS C  60     9814   7549   9439  -2694    520    990       N  
-ATOM   3686  CD2 HIS C  60      12.357  24.176  13.198  1.00 61.10           C  
-ANISOU 3686  CD2 HIS C  60     8716   6169   8330  -2515    485    542       C  
-ATOM   3687  CE1 HIS C  60      13.942  23.628  11.786  1.00 66.28           C  
-ANISOU 3687  CE1 HIS C  60     9154   7325   8703  -2695    566    824       C  
-ATOM   3688  NE2 HIS C  60      13.396  23.312  12.947  1.00 59.40           N  
-ANISOU 3688  NE2 HIS C  60     8346   6341   7882  -2593    552    565       N  
-ATOM   3689  N   ILE C  61       9.271  23.893  13.132  1.00 39.19           N  
-ANISOU 3689  N   ILE C  61     6209   3010   5672  -2081    455    428       N  
-ATOM   3690  CA  ILE C  61       8.802  23.244  14.339  1.00 45.06           C  
-ANISOU 3690  CA  ILE C  61     6950   3793   6376  -1963    483    130       C  
-ATOM   3691  C   ILE C  61       9.907  22.344  14.870  1.00 44.74           C  
-ANISOU 3691  C   ILE C  61     6767   4080   6153  -2063    552     44       C  
-ATOM   3692  O   ILE C  61      10.531  21.611  14.103  1.00 40.99           O  
-ANISOU 3692  O   ILE C  61     6192   3873   5510  -2118    606    182       O  
-ATOM   3693  CB  ILE C  61       7.569  22.396  14.012  1.00 50.57           C  
-ANISOU 3693  CB  ILE C  61     7694   4524   6997  -1764    541    101       C  
-ATOM   3694  CG1 ILE C  61       6.379  23.307  13.713  1.00 57.19           C  
-ANISOU 3694  CG1 ILE C  61     8682   5032   8015  -1621    461    121       C  
-ATOM   3695  CG2 ILE C  61       7.244  21.416  15.132  1.00 45.54           C  
-ANISOU 3695  CG2 ILE C  61     7001   4033   6269  -1668    606   -155       C  
-ATOM   3696  CD1 ILE C  61       5.311  22.630  12.893  1.00 58.67           C  
-ANISOU 3696  CD1 ILE C  61     8871   5301   8118  -1413    498    188       C  
-ATOM   3697  N   VAL C  62      10.179  22.421  16.168  1.00 38.23           N  
-ANISOU 3697  N   VAL C  62     5921   3254   5352  -2077    540   -192       N  
-ATOM   3698  CA  VAL C  62      10.954  21.369  16.813  1.00 34.69           C  
-ANISOU 3698  CA  VAL C  62     5352   3118   4711  -2113    609   -305       C  
-ATOM   3699  C   VAL C  62       9.967  20.473  17.548  1.00 35.00           C  
-ANISOU 3699  C   VAL C  62     5404   3208   4688  -1942    663   -475       C  
-ATOM   3700  O   VAL C  62       9.323  20.911  18.497  1.00 32.80           O  
-ANISOU 3700  O   VAL C  62     5174   2793   4494  -1862    637   -663       O  
-ATOM   3701  CB  VAL C  62      11.992  21.913  17.803  1.00 39.37           C  
-ANISOU 3701  CB  VAL C  62     5891   3738   5330  -2246    574   -452       C  
-ATOM   3702  CG1 VAL C  62      12.792  20.757  18.416  1.00 38.28           C  
-ANISOU 3702  CG1 VAL C  62     5628   3944   4973  -2268    642   -556       C  
-ATOM   3703  CG2 VAL C  62      12.915  22.897  17.124  1.00 42.46           C  
-ANISOU 3703  CG2 VAL C  62     6263   4046   5823  -2430    517   -284       C  
-ATOM   3704  N   ALA C  63       9.827  19.230  17.094  1.00 32.84           N  
-ANISOU 3704  N   ALA C  63     5069   3138   4272  -1880    729   -411       N  
-ATOM   3705  CA  ALA C  63       8.973  18.256  17.772  1.00 32.03           C  
-ANISOU 3705  CA  ALA C  63     4928   3136   4106  -1686    762   -526       C  
-ATOM   3706  C   ALA C  63       9.764  17.538  18.868  1.00 34.89           C  
-ANISOU 3706  C   ALA C  63     5192   3729   4336  -1721    785   -648       C  
-ATOM   3707  O   ALA C  63      10.774  16.881  18.576  1.00 30.48           O  
-ANISOU 3707  O   ALA C  63     4542   3380   3658  -1788    793   -587       O  
-ATOM   3708  CB  ALA C  63       8.424  17.266  16.788  1.00 31.12           C  
-ANISOU 3708  CB  ALA C  63     4765   3127   3931  -1550    781   -400       C  
-ATOM   3709  N   LEU C  64       9.297  17.657  20.115  1.00 28.32           N  
-ANISOU 3709  N   LEU C  64     4367   2887   3507  -1659    792   -826       N  
-ATOM   3710  CA  LEU C  64      10.004  17.132  21.289  1.00 28.12           C  
-ANISOU 3710  CA  LEU C  64     4252   3087   3346  -1683    807   -945       C  
-ATOM   3711  C   LEU C  64       9.285  15.894  21.850  1.00 31.45           C  
-ANISOU 3711  C   LEU C  64     4614   3671   3664  -1524    847   -936       C  
-ATOM   3712  O   LEU C  64       8.190  16.000  22.403  1.00 32.73           O  
-ANISOU 3712  O   LEU C  64     4794   3787   3854  -1418    865  -1010       O  
-ATOM   3713  CB  LEU C  64      10.070  18.221  22.359  1.00 29.31           C  
-ANISOU 3713  CB  LEU C  64     4427   3153   3557  -1734    778  -1163       C  
-ATOM   3714  CG  LEU C  64      10.969  18.088  23.596  1.00 37.20           C  
-ANISOU 3714  CG  LEU C  64     5330   4378   4424  -1787    778  -1326       C  
-ATOM   3715  CD1 LEU C  64      12.399  17.755  23.219  1.00 38.26           C  
-ANISOU 3715  CD1 LEU C  64     5396   4671   4471  -1933    774  -1251       C  
-ATOM   3716  CD2 LEU C  64      10.953  19.374  24.402  1.00 34.01           C  
-ANISOU 3716  CD2 LEU C  64     4953   3839   4129  -1836    726  -1569       C  
-ATOM   3717  N   CYS C  65       9.904  14.726  21.707  1.00 26.63           N  
-ANISOU 3717  N   CYS C  65     3926   3251   2939  -1510    851   -843       N  
-ATOM   3718  CA  CYS C  65       9.305  13.472  22.163  1.00 23.83           C  
-ANISOU 3718  CA  CYS C  65     3520   3017   2517  -1384    871   -790       C  
-ATOM   3719  C   CYS C  65       9.625  13.226  23.633  1.00 29.51           C  
-ANISOU 3719  C   CYS C  65     4180   3929   3102  -1380    885   -881       C  
-ATOM   3720  O   CYS C  65      10.796  13.225  24.026  1.00 29.73           O  
-ANISOU 3720  O   CYS C  65     4162   4101   3033  -1450    863   -929       O  
-ATOM   3721  CB  CYS C  65       9.840  12.311  21.313  1.00 25.32           C  
-ANISOU 3721  CB  CYS C  65     3654   3294   2672  -1353    838   -661       C  
-ATOM   3722  SG  CYS C  65       9.247  10.693  21.840  1.00 30.66           S  
-ANISOU 3722  SG  CYS C  65     4274   4064   3313  -1223    832   -571       S  
-ATOM   3723  N   VAL C  66       8.594  13.044  24.457  1.00 29.07           N  
-ANISOU 3723  N   VAL C  66     4111   3913   3022  -1295    923   -908       N  
-ATOM   3724  CA  VAL C  66       8.817  12.695  25.855  1.00 28.96           C  
-ANISOU 3724  CA  VAL C  66     4020   4139   2845  -1275    940   -960       C  
-ATOM   3725  C   VAL C  66       8.903  11.172  26.004  1.00 31.51           C  
-ANISOU 3725  C   VAL C  66     4291   4591   3089  -1221    933   -772       C  
-ATOM   3726  O   VAL C  66       7.882  10.484  26.061  1.00 28.36           O  
-ANISOU 3726  O   VAL C  66     3880   4177   2720  -1160    960   -661       O  
-ATOM   3727  CB  VAL C  66       7.720  13.262  26.779  1.00 31.65           C  
-ANISOU 3727  CB  VAL C  66     4338   4529   3158  -1213    984  -1085       C  
-ATOM   3728  CG1 VAL C  66       8.087  13.025  28.250  1.00 34.48           C  
-ANISOU 3728  CG1 VAL C  66     4594   5197   3308  -1195   1001  -1152       C  
-ATOM   3729  CG2 VAL C  66       7.520  14.770  26.529  1.00 31.49           C  
-ANISOU 3729  CG2 VAL C  66     4385   4312   3268  -1240    959  -1282       C  
-ATOM   3730  N   LEU C  67      10.132  10.657  26.041  1.00 34.03           N  
-ANISOU 3730  N   LEU C  67     4577   5027   3325  -1246    885   -741       N  
-ATOM   3731  CA  LEU C  67      10.380   9.220  26.199  1.00 31.73           C  
-ANISOU 3731  CA  LEU C  67     4246   4832   2979  -1181    844   -572       C  
-ATOM   3732  C   LEU C  67       9.978   8.773  27.606  1.00 30.69           C  
-ANISOU 3732  C   LEU C  67     4058   4900   2701  -1141    877   -513       C  
-ATOM   3733  O   LEU C  67       9.949   9.602  28.526  1.00 29.58           O  
-ANISOU 3733  O   LEU C  67     3884   4905   2450  -1158    920   -655       O  
-ATOM   3734  CB  LEU C  67      11.869   8.940  25.973  1.00 36.27           C  
-ANISOU 3734  CB  LEU C  67     4786   5515   3479  -1199    773   -598       C  
-ATOM   3735  CG  LEU C  67      12.387   9.238  24.576  1.00 37.92           C  
-ANISOU 3735  CG  LEU C  67     5015   5607   3788  -1243    739   -628       C  
-ATOM   3736  CD1 LEU C  67      13.869   8.947  24.485  1.00 41.86           C  
-ANISOU 3736  CD1 LEU C  67     5445   6283   4177  -1258    672   -675       C  
-ATOM   3737  CD2 LEU C  67      11.616   8.412  23.578  1.00 31.74           C  
-ANISOU 3737  CD2 LEU C  67     4252   4663   3143  -1166    712   -505       C  
-ATOM   3738  N   LYS C  68       9.657   7.489  27.799  1.00 29.63           N  
-ANISOU 3738  N   LYS C  68     3906   4785   2568  -1087    851   -306       N  
-ATOM   3739  CA  LYS C  68       9.611   6.486  26.721  1.00 31.78           C  
-ANISOU 3739  CA  LYS C  68     4207   4866   3001  -1050    779   -176       C  
-ATOM   3740  C   LYS C  68       8.214   6.340  26.134  1.00 30.08           C  
-ANISOU 3740  C   LYS C  68     4013   4467   2949  -1047    819   -112       C  
-ATOM   3741  O   LYS C  68       8.055   6.084  24.928  1.00 31.10           O  
-ANISOU 3741  O   LYS C  68     4167   4412   3235  -1024    776   -110       O  
-ATOM   3742  CB  LYS C  68      10.055   5.120  27.258  1.00 34.31           C  
-ANISOU 3742  CB  LYS C  68     4499   5264   3274   -991    697     10       C  
-ATOM   3743  CG  LYS C  68      11.473   5.096  27.813  1.00 38.43           C  
-ANISOU 3743  CG  LYS C  68     4988   5990   3625   -964    639    -49       C  
-ATOM   3744  CD  LYS C  68      12.033   3.678  27.871  1.00 41.39           C  
-ANISOU 3744  CD  LYS C  68     5356   6355   4018   -871    510    120       C  
-ATOM   3745  CE  LYS C  68      12.141   3.178  29.291  1.00 47.87           C  
-ANISOU 3745  CE  LYS C  68     6142   7389   4659   -842    508    276       C  
-ATOM   3746  NZ  LYS C  68      12.695   1.790  29.338  1.00 48.92           N  
-ANISOU 3746  NZ  LYS C  68     6283   7469   4834   -738    357    459       N  
-ATOM   3747  N   GLY C  69       7.206   6.492  26.990  1.00 26.01           N  
-ANISOU 3747  N   GLY C  69     3465   4039   2378  -1063    899    -72       N  
-ATOM   3748  CA  GLY C  69       5.823   6.241  26.604  1.00 29.92           C  
-ANISOU 3748  CA  GLY C  69     3952   4410   3006  -1063    940     -3       C  
-ATOM   3749  C   GLY C  69       5.361   7.075  25.419  1.00 25.59           C  
-ANISOU 3749  C   GLY C  69     3454   3672   2598  -1050    953   -147       C  
-ATOM   3750  O   GLY C  69       4.441   6.695  24.688  1.00 29.62           O  
-ANISOU 3750  O   GLY C  69     3960   4040   3254  -1029    952   -101       O  
-ATOM   3751  N   GLY C  70       6.003   8.214  25.207  1.00 24.72           N  
-ANISOU 3751  N   GLY C  70     3387   3555   2450  -1065    957   -314       N  
-ATOM   3752  CA  GLY C  70       5.632   9.056  24.081  1.00 28.08           C  
-ANISOU 3752  CA  GLY C  70     3870   3798   3002  -1055    960   -414       C  
-ATOM   3753  C   GLY C  70       6.060   8.565  22.710  1.00 30.61           C  
-ANISOU 3753  C   GLY C  70     4210   3984   3435  -1033    891   -364       C  
-ATOM   3754  O   GLY C  70       5.596   9.097  21.701  1.00 23.99           O  
-ANISOU 3754  O   GLY C  70     3406   3014   2696  -1010    892   -406       O  
-ATOM   3755  N   TYR C  71       6.923   7.551  22.650  1.00 26.50           N  
-ANISOU 3755  N   TYR C  71     3658   3517   2894  -1020    821   -284       N  
-ATOM   3756  CA  TYR C  71       7.604   7.252  21.387  1.00 24.48           C  
-ANISOU 3756  CA  TYR C  71     3395   3205   2701   -989    745   -294       C  
-ATOM   3757  C   TYR C  71       6.694   6.820  20.235  1.00 22.85           C  
-ANISOU 3757  C   TYR C  71     3176   2857   2651   -920    719   -272       C  
-ATOM   3758  O   TYR C  71       6.931   7.209  19.087  1.00 24.33           O  
-ANISOU 3758  O   TYR C  71     3363   3014   2868   -899    696   -320       O  
-ATOM   3759  CB  TYR C  71       8.777   6.269  21.576  1.00 32.31           C  
-ANISOU 3759  CB  TYR C  71     4342   4302   3632   -960    653   -254       C  
-ATOM   3760  CG  TYR C  71       8.506   4.847  21.112  1.00 32.88           C  
-ANISOU 3760  CG  TYR C  71     4375   4287   3833   -869    556   -169       C  
-ATOM   3761  CD1 TYR C  71       8.693   4.472  19.782  1.00 33.45           C  
-ANISOU 3761  CD1 TYR C  71     4407   4305   3997   -795    476   -225       C  
-ATOM   3762  CD2 TYR C  71       8.094   3.875  22.019  1.00 29.80           C  
-ANISOU 3762  CD2 TYR C  71     3975   3875   3473   -858    533    -35       C  
-ATOM   3763  CE1 TYR C  71       8.437   3.166  19.364  1.00 34.98           C  
-ANISOU 3763  CE1 TYR C  71     4554   4398   4338   -700    362   -189       C  
-ATOM   3764  CE2 TYR C  71       7.843   2.574  21.619  1.00 29.36           C  
-ANISOU 3764  CE2 TYR C  71     3889   3689   3578   -788    422     44       C  
-ATOM   3765  CZ  TYR C  71       8.015   2.229  20.288  1.00 28.83           C  
-ANISOU 3765  CZ  TYR C  71     3784   3543   3627   -703    330    -55       C  
-ATOM   3766  OH  TYR C  71       7.762   0.932  19.887  1.00 27.58           O  
-ANISOU 3766  OH  TYR C  71     3586   3236   3658   -621    198    -17       O  
-ATOM   3767  N   LYS C  72       5.670   6.018  20.516  1.00 23.95           N  
-ANISOU 3767  N   LYS C  72     3288   2930   2881   -890    722   -197       N  
-ATOM   3768  CA  LYS C  72       4.790   5.553  19.428  1.00 26.98           C  
-ANISOU 3768  CA  LYS C  72     3638   3189   3423   -821    688   -204       C  
-ATOM   3769  C   LYS C  72       3.913   6.666  18.865  1.00 27.23           C  
-ANISOU 3769  C   LYS C  72     3704   3166   3478   -808    758   -280       C  
-ATOM   3770  O   LYS C  72       3.828   6.854  17.647  1.00 24.24           O  
-ANISOU 3770  O   LYS C  72     3315   2743   3153   -748    725   -326       O  
-ATOM   3771  CB  LYS C  72       3.912   4.384  19.885  1.00 25.93           C  
-ANISOU 3771  CB  LYS C  72     3456   2989   3407   -820    667   -100       C  
-ATOM   3772  CG  LYS C  72       4.571   3.029  19.760  1.00 39.63           C  
-ANISOU 3772  CG  LYS C  72     5153   4677   5228   -778    535    -36       C  
-ATOM   3773  CD  LYS C  72       5.033   2.780  18.344  1.00 43.15           C  
-ANISOU 3773  CD  LYS C  72     5559   5085   5750   -676    433   -152       C  
-ATOM   3774  CE  LYS C  72       3.864   2.513  17.429  1.00 50.35           C  
-ANISOU 3774  CE  LYS C  72     6419   5883   6829   -624    419   -204       C  
-ATOM   3775  NZ  LYS C  72       4.318   2.210  16.041  1.00 53.92           N  
-ANISOU 3775  NZ  LYS C  72     6804   6348   7334   -503    310   -334       N  
-ATOM   3776  N   PHE C  73       3.229   7.375  19.754  1.00 25.28           N  
-ANISOU 3776  N   PHE C  73     3484   2940   3182   -848    845   -297       N  
-ATOM   3777  CA  PHE C  73       2.447   8.547  19.366  1.00 26.72           C  
-ANISOU 3777  CA  PHE C  73     3709   3061   3382   -818    895   -386       C  
-ATOM   3778  C   PHE C  73       3.286   9.537  18.563  1.00 25.98           C  
-ANISOU 3778  C   PHE C  73     3683   2928   3262   -828    872   -429       C  
-ATOM   3779  O   PHE C  73       2.842  10.070  17.535  1.00 23.62           O  
-ANISOU 3779  O   PHE C  73     3408   2547   3021   -771    862   -449       O  
-ATOM   3780  CB  PHE C  73       1.871   9.216  20.613  1.00 25.54           C  
-ANISOU 3780  CB  PHE C  73     3568   2981   3156   -847    972   -438       C  
-ATOM   3781  CG  PHE C  73       0.906  10.330  20.321  1.00 25.85           C  
-ANISOU 3781  CG  PHE C  73     3643   2947   3233   -786   1004   -551       C  
-ATOM   3782  CD1 PHE C  73      -0.121  10.165  19.387  1.00 25.45           C  
-ANISOU 3782  CD1 PHE C  73     3564   2817   3287   -701    995   -560       C  
-ATOM   3783  CD2 PHE C  73       1.009  11.537  20.998  1.00 24.20           C  
-ANISOU 3783  CD2 PHE C  73     3487   2746   2963   -796   1027   -668       C  
-ATOM   3784  CE1 PHE C  73      -1.029  11.204  19.136  1.00 24.69           C  
-ANISOU 3784  CE1 PHE C  73     3503   2658   3222   -618   1010   -669       C  
-ATOM   3785  CE2 PHE C  73       0.111  12.583  20.753  1.00 26.70           C  
-ANISOU 3785  CE2 PHE C  73     3843   2970   3334   -714   1030   -787       C  
-ATOM   3786  CZ  PHE C  73      -0.910  12.411  19.821  1.00 24.75           C  
-ANISOU 3786  CZ  PHE C  73     3575   2650   3178   -620   1023   -779       C  
-ATOM   3787  N   PHE C  74       4.504   9.781  19.037  1.00 23.85           N  
-ANISOU 3787  N   PHE C  74     3435   2730   2897   -906    863   -430       N  
-ATOM   3788  CA  PHE C  74       5.400  10.725  18.394  1.00 20.84           C  
-ANISOU 3788  CA  PHE C  74     3102   2329   2485   -960    845   -449       C  
-ATOM   3789  C   PHE C  74       5.716  10.294  16.973  1.00 25.28           C  
-ANISOU 3789  C   PHE C  74     3623   2909   3075   -912    791   -399       C  
-ATOM   3790  O   PHE C  74       5.602  11.090  16.042  1.00 24.14           O  
-ANISOU 3790  O   PHE C  74     3513   2708   2952   -907    789   -381       O  
-ATOM   3791  CB  PHE C  74       6.663  10.859  19.241  1.00 23.47           C  
-ANISOU 3791  CB  PHE C  74     3432   2777   2707  -1060    842   -472       C  
-ATOM   3792  CG  PHE C  74       7.736  11.713  18.634  1.00 28.68           C  
-ANISOU 3792  CG  PHE C  74     4117   3447   3334  -1154    823   -478       C  
-ATOM   3793  CD1 PHE C  74       7.728  13.091  18.803  1.00 29.61           C  
-ANISOU 3793  CD1 PHE C  74     4314   3451   3485  -1234    844   -532       C  
-ATOM   3794  CD2 PHE C  74       8.781  11.131  17.943  1.00 24.96           C  
-ANISOU 3794  CD2 PHE C  74     3577   3106   2802  -1170    776   -437       C  
-ATOM   3795  CE1 PHE C  74       8.739  13.878  18.284  1.00 31.58           C  
-ANISOU 3795  CE1 PHE C  74     4579   3699   3719  -1359    826   -510       C  
-ATOM   3796  CE2 PHE C  74       9.793  11.911  17.403  1.00 28.31           C  
-ANISOU 3796  CE2 PHE C  74     3998   3582   3176  -1284    768   -426       C  
-ATOM   3797  CZ  PHE C  74       9.772  13.283  17.580  1.00 29.57           C  
-ANISOU 3797  CZ  PHE C  74     4243   3612   3381  -1395    797   -445       C  
-ATOM   3798  N   ALA C  75       6.115   9.033  16.805  1.00 21.87           N  
-ANISOU 3798  N   ALA C  75     3108   2564   2639   -867    734   -377       N  
-ATOM   3799  CA  ALA C  75       6.519   8.527  15.497  1.00 22.34           C  
-ANISOU 3799  CA  ALA C  75     3093   2693   2703   -798    665   -373       C  
-ATOM   3800  C   ALA C  75       5.352   8.604  14.524  1.00 24.69           C  
-ANISOU 3800  C   ALA C  75     3378   2910   3092   -698    665   -379       C  
-ATOM   3801  O   ALA C  75       5.506   9.059  13.379  1.00 22.67           O  
-ANISOU 3801  O   ALA C  75     3101   2708   2804   -666    648   -364       O  
-ATOM   3802  CB  ALA C  75       7.015   7.091  15.608  1.00 26.19           C  
-ANISOU 3802  CB  ALA C  75     3492   3253   3205   -736    579   -386       C  
-ATOM   3803  N   ASP C  76       4.192   8.151  14.979  1.00 20.82           N  
-ANISOU 3803  N   ASP C  76     2885   2323   2701   -652    684   -394       N  
-ATOM   3804  CA  ASP C  76       2.981   8.162  14.162  1.00 26.00           C  
-ANISOU 3804  CA  ASP C  76     3514   2917   3448   -549    683   -424       C  
-ATOM   3805  C   ASP C  76       2.473   9.559  13.844  1.00 22.75           C  
-ANISOU 3805  C   ASP C  76     3189   2440   3016   -544    735   -418       C  
-ATOM   3806  O   ASP C  76       2.131   9.833  12.697  1.00 24.47           O  
-ANISOU 3806  O   ASP C  76     3385   2671   3241   -458    710   -415       O  
-ATOM   3807  CB  ASP C  76       1.872   7.318  14.810  1.00 26.96           C  
-ANISOU 3807  CB  ASP C  76     3593   2970   3682   -527    694   -440       C  
-ATOM   3808  CG  ASP C  76       2.184   5.835  14.779  1.00 31.59           C  
-ANISOU 3808  CG  ASP C  76     4089   3564   4349   -504    606   -436       C  
-ATOM   3809  OD1 ASP C  76       2.978   5.442  13.905  1.00 31.97           O  
-ANISOU 3809  OD1 ASP C  76     4082   3682   4382   -444    522   -473       O  
-ATOM   3810  OD2 ASP C  76       1.642   5.063  15.609  1.00 26.68           O  
-ANISOU 3810  OD2 ASP C  76     3443   2886   3809   -543    610   -394       O  
-ATOM   3811  N   LEU C  77       2.400  10.432  14.848  1.00 21.00           N  
-ANISOU 3811  N   LEU C  77     3059   2150   2772   -621    793   -425       N  
-ATOM   3812  CA  LEU C  77       1.967  11.809  14.634  1.00 22.82           C  
-ANISOU 3812  CA  LEU C  77     3386   2272   3013   -609    815   -433       C  
-ATOM   3813  C   LEU C  77       2.869  12.471  13.607  1.00 25.20           C  
-ANISOU 3813  C   LEU C  77     3719   2590   3265   -648    783   -346       C  
-ATOM   3814  O   LEU C  77       2.393  13.125  12.679  1.00 25.93           O  
-ANISOU 3814  O   LEU C  77     3844   2630   3379   -579    766   -301       O  
-ATOM   3815  CB  LEU C  77       1.998  12.610  15.932  1.00 24.48           C  
-ANISOU 3815  CB  LEU C  77     3673   2420   3208   -686    857   -492       C  
-ATOM   3816  CG  LEU C  77       1.599  14.087  15.824  1.00 27.55           C  
-ANISOU 3816  CG  LEU C  77     4174   2651   3645   -666    850   -527       C  
-ATOM   3817  CD1 LEU C  77       0.135  14.232  15.420  1.00 24.64           C  
-ANISOU 3817  CD1 LEU C  77     3797   2221   3344   -511    849   -581       C  
-ATOM   3818  CD2 LEU C  77       1.855  14.818  17.150  1.00 29.47           C  
-ANISOU 3818  CD2 LEU C  77     4469   2855   3872   -742    869   -630       C  
-ATOM   3819  N   LEU C  78       4.179  12.300  13.769  1.00 23.75           N  
-ANISOU 3819  N   LEU C  78     3515   2506   3002   -760    773   -310       N  
-ATOM   3820  CA  LEU C  78       5.120  12.873  12.810  1.00 23.82           C  
-ANISOU 3820  CA  LEU C  78     3524   2586   2942   -827    751   -210       C  
-ATOM   3821  C   LEU C  78       4.957  12.280  11.406  1.00 24.22           C  
-ANISOU 3821  C   LEU C  78     3469   2779   2956   -707    709   -171       C  
-ATOM   3822  O   LEU C  78       5.104  12.985  10.418  1.00 23.98           O  
-ANISOU 3822  O   LEU C  78     3447   2784   2879   -712    699    -64       O  
-ATOM   3823  CB  LEU C  78       6.557  12.725  13.299  1.00 26.34           C  
-ANISOU 3823  CB  LEU C  78     3810   3030   3169   -968    748   -206       C  
-ATOM   3824  CG  LEU C  78       7.075  13.995  13.968  1.00 35.30           C  
-ANISOU 3824  CG  LEU C  78     5049   4046   4317  -1127    774   -194       C  
-ATOM   3825  CD1 LEU C  78       6.275  14.344  15.216  1.00 36.84           C  
-ANISOU 3825  CD1 LEU C  78     5325   4081   4591  -1106    801   -305       C  
-ATOM   3826  CD2 LEU C  78       8.541  13.860  14.294  1.00 40.91           C  
-ANISOU 3826  CD2 LEU C  78     5700   4920   4922  -1269    769   -196       C  
-ATOM   3827  N   ASP C  79       4.669  10.982  11.319  1.00 24.02           N  
-ANISOU 3827  N   ASP C  79     3335   2840   2952   -601    675   -254       N  
-ATOM   3828  CA  ASP C  79       4.434  10.378  10.016  1.00 22.78           C  
-ANISOU 3828  CA  ASP C  79     3055   2828   2771   -462    620   -270       C  
-ATOM   3829  C   ASP C  79       3.221  10.995   9.306  1.00 23.07           C  
-ANISOU 3829  C   ASP C  79     3126   2785   2854   -351    629   -246       C  
-ATOM   3830  O   ASP C  79       3.254  11.201   8.101  1.00 22.00           O  
-ANISOU 3830  O   ASP C  79     2928   2787   2642   -276    601   -191       O  
-ATOM   3831  CB  ASP C  79       4.304   8.846  10.118  1.00 28.50           C  
-ANISOU 3831  CB  ASP C  79     3659   3609   3560   -368    556   -392       C  
-ATOM   3832  CG  ASP C  79       5.655   8.149  10.145  1.00 32.90           C  
-ANISOU 3832  CG  ASP C  79     4131   4336   4033   -402    500   -420       C  
-ATOM   3833  OD1 ASP C  79       6.671   8.813   9.847  1.00 35.99           O  
-ANISOU 3833  OD1 ASP C  79     4520   4864   4290   -492    517   -350       O  
-ATOM   3834  OD2 ASP C  79       5.698   6.936  10.441  1.00 38.65           O  
-ANISOU 3834  OD2 ASP C  79     4787   5061   4836   -339    431   -511       O  
-ATOM   3835  N   TYR C  80       2.158  11.279  10.047  1.00 21.90           N  
-ANISOU 3835  N   TYR C  80     3060   2451   2811   -329    666   -292       N  
-ATOM   3836  CA  TYR C  80       0.994  11.943   9.463  1.00 22.07           C  
-ANISOU 3836  CA  TYR C  80     3119   2394   2874   -209    667   -287       C  
-ATOM   3837  C   TYR C  80       1.293  13.396   9.062  1.00 23.12           C  
-ANISOU 3837  C   TYR C  80     3375   2445   2963   -260    673   -142       C  
-ATOM   3838  O   TYR C  80       0.846  13.862   8.004  1.00 23.66           O  
-ANISOU 3838  O   TYR C  80     3439   2549   3001   -154    645    -67       O  
-ATOM   3839  CB  TYR C  80      -0.210  11.870  10.416  1.00 23.94           C  
-ANISOU 3839  CB  TYR C  80     3388   2489   3220   -169    702   -395       C  
-ATOM   3840  CG  TYR C  80      -0.931  10.533  10.386  1.00 26.29           C  
-ANISOU 3840  CG  TYR C  80     3547   2851   3590    -88    683   -507       C  
-ATOM   3841  CD1 TYR C  80      -1.609  10.118   9.246  1.00 27.01           C  
-ANISOU 3841  CD1 TYR C  80     3530   3033   3700     65    636   -562       C  
-ATOM   3842  CD2 TYR C  80      -0.938   9.690  11.496  1.00 24.30           C  
-ANISOU 3842  CD2 TYR C  80     3267   2572   3395   -169    705   -550       C  
-ATOM   3843  CE1 TYR C  80      -2.284   8.895   9.206  1.00 31.03           C  
-ANISOU 3843  CE1 TYR C  80     3904   3575   4311    124    604   -681       C  
-ATOM   3844  CE2 TYR C  80      -1.612   8.452  11.468  1.00 26.49           C  
-ANISOU 3844  CE2 TYR C  80     3420   2871   3774   -122    675   -628       C  
-ATOM   3845  CZ  TYR C  80      -2.276   8.069  10.316  1.00 28.49           C  
-ANISOU 3845  CZ  TYR C  80     3566   3185   4072     19    622   -704       C  
-ATOM   3846  OH  TYR C  80      -2.952   6.866  10.278  1.00 29.31           O  
-ANISOU 3846  OH  TYR C  80     3540   3286   4309     51    580   -797       O  
-ATOM   3847  N   ILE C  81       2.065  14.112   9.882  1.00 23.48           N  
-ANISOU 3847  N   ILE C  81     3527   2383   3012   -424    698    -94       N  
-ATOM   3848  CA  ILE C  81       2.515  15.469   9.490  1.00 24.67           C  
-ANISOU 3848  CA  ILE C  81     3794   2426   3153   -513    687     65       C  
-ATOM   3849  C   ILE C  81       3.356  15.441   8.212  1.00 26.24           C  
-ANISOU 3849  C   ILE C  81     3909   2844   3217   -545    666    229       C  
-ATOM   3850  O   ILE C  81       3.191  16.275   7.304  1.00 26.05           O  
-ANISOU 3850  O   ILE C  81     3931   2800   3169   -520    642    394       O  
-ATOM   3851  CB  ILE C  81       3.295  16.158  10.636  1.00 27.14           C  
-ANISOU 3851  CB  ILE C  81     4209   2593   3508   -702    707     52       C  
-ATOM   3852  CG1 ILE C  81       2.355  16.428  11.808  1.00 26.11           C  
-ANISOU 3852  CG1 ILE C  81     4155   2277   3489   -645    720   -110       C  
-ATOM   3853  CG2 ILE C  81       3.928  17.465  10.163  1.00 29.01           C  
-ANISOU 3853  CG2 ILE C  81     4551   2710   3761   -835    681    233       C  
-ATOM   3854  CD1 ILE C  81       3.074  16.912  13.108  1.00 26.40           C  
-ANISOU 3854  CD1 ILE C  81     4256   2223   3554   -803    736   -187       C  
-ATOM   3855  N   LYS C  82       4.263  14.476   8.135  1.00 25.36           N  
-ANISOU 3855  N   LYS C  82     3664   2966   3008   -590    668    189       N  
-ATOM   3856  CA  LYS C  82       5.100  14.328   6.954  1.00 27.26           C  
-ANISOU 3856  CA  LYS C  82     3778   3494   3086   -606    648    308       C  
-ATOM   3857  C   LYS C  82       4.261  14.044   5.712  1.00 27.84           C  
-ANISOU 3857  C   LYS C  82     3757   3715   3105   -399    612    320       C  
-ATOM   3858  O   LYS C  82       4.547  14.556   4.633  1.00 26.44           O  
-ANISOU 3858  O   LYS C  82     3536   3707   2802   -398    600    494       O  
-ATOM   3859  CB  LYS C  82       6.143  13.233   7.177  1.00 29.21           C  
-ANISOU 3859  CB  LYS C  82     3882   3973   3245   -647    637    202       C  
-ATOM   3860  CG  LYS C  82       7.304  13.686   8.051  1.00 33.92           C  
-ANISOU 3860  CG  LYS C  82     4533   4533   3822   -870    668    238       C  
-ATOM   3861  CD  LYS C  82       7.896  12.533   8.826  1.00 39.18           C  
-ANISOU 3861  CD  LYS C  82     5115   5298   4474   -863    651     72       C  
-ATOM   3862  CE  LYS C  82       8.384  11.443   7.894  1.00 43.63           C  
-ANISOU 3862  CE  LYS C  82     5477   6188   4915   -743    591      4       C  
-ATOM   3863  NZ  LYS C  82       8.748  10.225   8.670  1.00 48.59           N  
-ANISOU 3863  NZ  LYS C  82     6041   6844   5576   -693    546   -165       N  
-ATOM   3864  N   ALA C  83       3.200  13.255   5.880  1.00 23.76           N  
-ANISOU 3864  N   ALA C  83     3200   3146   2681   -230    594    143       N  
-ATOM   3865  CA  ALA C  83       2.314  12.929   4.750  1.00 27.27           C  
-ANISOU 3865  CA  ALA C  83     3537   3737   3087    -17    553    108       C  
-ATOM   3866  C   ALA C  83       1.637  14.202   4.254  1.00 28.17           C  
-ANISOU 3866  C   ALA C  83     3776   3723   3203     28    555    278       C  
-ATOM   3867  O   ALA C  83       1.514  14.427   3.056  1.00 29.15           O  
-ANISOU 3867  O   ALA C  83     3826   4044   3204    133    525    389       O  
-ATOM   3868  CB  ALA C  83       1.276  11.881   5.158  1.00 22.82           C  
-ANISOU 3868  CB  ALA C  83     2910   3106   2656    121    533   -121       C  
-ATOM   3869  N   LEU C  84       1.216  15.043   5.190  1.00 25.71           N  
-ANISOU 3869  N   LEU C  84     3649   3091   3028    -41    578    295       N  
-ATOM   3870  CA  LEU C  84       0.696  16.361   4.842  1.00 29.27           C  
-ANISOU 3870  CA  LEU C  84     4248   3358   3514     -9    557    461       C  
-ATOM   3871  C   LEU C  84       1.728  17.199   4.093  1.00 33.67           C  
-ANISOU 3871  C   LEU C  84     4836   3998   3960   -154    549    747       C  
-ATOM   3872  O   LEU C  84       1.431  17.815   3.058  1.00 31.93           O  
-ANISOU 3872  O   LEU C  84     4627   3839   3667    -70    514    939       O  
-ATOM   3873  CB  LEU C  84       0.260  17.093   6.101  1.00 29.23           C  
-ANISOU 3873  CB  LEU C  84     4421   3001   3683    -68    566    385       C  
-ATOM   3874  CG  LEU C  84      -0.958  16.474   6.784  1.00 32.66           C  
-ANISOU 3874  CG  LEU C  84     4824   3373   4214     80    577    139       C  
-ATOM   3875  CD1 LEU C  84      -1.297  17.262   8.043  1.00 33.48           C  
-ANISOU 3875  CD1 LEU C  84     5078   3190   4454     26    584     52       C  
-ATOM   3876  CD2 LEU C  84      -2.150  16.450   5.833  1.00 34.10           C  
-ANISOU 3876  CD2 LEU C  84     4950   3628   4379    320    537    113       C  
-ATOM   3877  N   ASN C  85       2.944  17.217   4.622  1.00 29.29           N  
-ANISOU 3877  N   ASN C  85     4284   3462   3382   -379    582    789       N  
-ATOM   3878  CA  ASN C  85       4.006  18.048   4.067  1.00 31.36           C  
-ANISOU 3878  CA  ASN C  85     4568   3795   3552   -573    584   1067       C  
-ATOM   3879  C   ASN C  85       4.399  17.694   2.642  1.00 32.42           C  
-ANISOU 3879  C   ASN C  85     4516   4351   3451   -513    577   1217       C  
-ATOM   3880  O   ASN C  85       4.883  18.550   1.897  1.00 40.08           O  
-ANISOU 3880  O   ASN C  85     5507   5392   4331   -625    571   1513       O  
-ATOM   3881  CB  ASN C  85       5.247  17.970   4.955  1.00 34.94           C  
-ANISOU 3881  CB  ASN C  85     5019   4244   4013   -818    622   1029       C  
-ATOM   3882  CG  ASN C  85       5.127  18.819   6.199  1.00 42.46           C  
-ANISOU 3882  CG  ASN C  85     6169   4791   5173   -937    619    973       C  
-ATOM   3883  OD1 ASN C  85       4.406  19.811   6.212  1.00 44.86           O  
-ANISOU 3883  OD1 ASN C  85     6632   4803   5612   -896    577   1051       O  
-ATOM   3884  ND2 ASN C  85       5.847  18.441   7.249  1.00 43.53           N  
-ANISOU 3884  ND2 ASN C  85     6287   4922   5331  -1068    651    825       N  
-ATOM   3885  N   ARG C  86       4.246  16.430   2.269  1.00 42.90           N  
-ANISOU 3885  N   ARG C  86     6441   4762   5095   -504   -183    746       N  
-ATOM   3886  CA  ARG C  86       4.704  16.006   0.945  1.00 43.25           C  
-ANISOU 3886  CA  ARG C  86     6542   5003   4889   -956   -142    898       C  
-ATOM   3887  C   ARG C  86       3.578  15.913  -0.064  1.00 45.49           C  
-ANISOU 3887  C   ARG C  86     6809   5402   5072   -751   -403   1013       C  
-ATOM   3888  O   ARG C  86       3.805  15.534  -1.213  1.00 46.14           O  
-ANISOU 3888  O   ARG C  86     6925   5687   4919  -1118   -383   1131       O  
-ATOM   3889  CB  ARG C  86       5.471  14.684   1.009  1.00 39.20           C  
-ANISOU 3889  CB  ARG C  86     5563   4905   4428  -1292    262    733       C  
-ATOM   3890  CG  ARG C  86       4.661  13.525   1.542  1.00 36.20           C  
-ANISOU 3890  CG  ARG C  86     4613   4869   4271   -967    426    533       C  
-ATOM   3891  CD  ARG C  86       5.404  12.217   1.389  1.00 32.98           C  
-ANISOU 3891  CD  ARG C  86     3791   4822   3917  -1314    778    403       C  
-ATOM   3892  NE  ARG C  86       4.562  11.131   1.853  1.00 30.60           N  
-ANISOU 3892  NE  ARG C  86     3005   4812   3811  -1020    926    234       N  
-ATOM   3893  CZ  ARG C  86       4.638  10.604   3.069  1.00 32.14           C  
-ANISOU 3893  CZ  ARG C  86     2954   5047   4210   -858   1097     82       C  
-ATOM   3894  NH1 ARG C  86       5.549  11.047   3.924  1.00 28.61           N  
-ANISOU 3894  NH1 ARG C  86     2670   4394   3807   -951   1128     72       N  
-ATOM   3895  NH2 ARG C  86       3.820   9.627   3.421  1.00 28.43           N  
-ANISOU 3895  NH2 ARG C  86     2134   4784   3883   -609   1205    -45       N  
-ATOM   3896  N   ASN C  87       2.371  16.273   0.356  1.00 47.02           N  
-ANISOU 3896  N   ASN C  87     6937   5484   5443   -180   -650    950       N  
-ATOM   3897  CA  ASN C  87       1.231  16.298  -0.553  1.00 49.84           C  
-ANISOU 3897  CA  ASN C  87     7276   5929   5731     82   -969   1039       C  
-ATOM   3898  C   ASN C  87       0.544  17.654  -0.609  1.00 56.34           C  
-ANISOU 3898  C   ASN C  87     8552   6264   6590    482  -1466   1183       C  
-ATOM   3899  O   ASN C  87      -0.543  17.789  -1.173  1.00 60.31           O  
-ANISOU 3899  O   ASN C  87     9015   6792   7108    833  -1807   1219       O  
-ATOM   3900  CB  ASN C  87       0.226  15.199  -0.196  1.00 51.08           C  
-ANISOU 3900  CB  ASN C  87     6790   6518   6100    417   -807    760       C  
-ATOM   3901  CG  ASN C  87       0.781  13.806  -0.438  1.00 45.84           C  
-ANISOU 3901  CG  ASN C  87     5709   6320   5388     21   -381    659       C  
-ATOM   3902  OD1 ASN C  87       0.983  13.405  -1.582  1.00 43.75           O  
-ANISOU 3902  OD1 ASN C  87     5458   6267   4898   -321   -372    778       O  
-ATOM   3903  ND2 ASN C  87       1.028  13.065   0.636  1.00 43.57           N  
-ANISOU 3903  ND2 ASN C  87     5061   6182   5311     55    -36    433       N  
-ATOM   3904  N   SER C  88       1.190  18.660  -0.034  1.00 56.27           N  
-ANISOU 3904  N   SER C  88     8969   5801   6611    433  -1523   1252       N  
-ATOM   3905  CA  SER C  88       0.640  20.010  -0.033  1.00 64.65           C  
-ANISOU 3905  CA  SER C  88    10504   6317   7745    802  -1993   1382       C  
-ATOM   3906  C   SER C  88       1.621  20.971  -0.689  1.00 68.25           C  
-ANISOU 3906  C   SER C  88    11682   6350   7902    340  -2143   1722       C  
-ATOM   3907  O   SER C  88       2.809  20.666  -0.794  1.00 65.25           O  
-ANISOU 3907  O   SER C  88    11377   6090   7325   -235  -1811   1759       O  
-ATOM   3908  CB  SER C  88       0.328  20.458   1.396  1.00 65.62           C  
-ANISOU 3908  CB  SER C  88    10481   6223   8229   1233  -1935   1092       C  
-ATOM   3909  OG  SER C  88      -0.502  19.513   2.055  1.00 62.70           O  
-ANISOU 3909  OG  SER C  88     9455   6273   8095   1566  -1730    754       O  
-ATOM   3910  N   ASP C  89       1.117  22.115  -1.141  1.00 76.90           N  
-ANISOU 3910  N   ASP C  89    13305   6945   8968    584  -2648   1953       N  
-ATOM   3911  CA  ASP C  89       1.961  23.149  -1.724  1.00 87.63           C  
-ANISOU 3911  CA  ASP C  89    15438   7821  10037    156  -2823   2290       C  
-ATOM   3912  C   ASP C  89       2.996  23.584  -0.702  1.00 91.38           C  
-ANISOU 3912  C   ASP C  89    16043   8069  10609    -72  -2503   2148       C  
-ATOM   3913  O   ASP C  89       4.196  23.422  -0.903  1.00 92.80           O  
-ANISOU 3913  O   ASP C  89    16377   8342  10541   -700  -2192   2201       O  
-ATOM   3914  CB  ASP C  89       1.122  24.357  -2.143  1.00 94.03           C  
-ANISOU 3914  CB  ASP C  89    16784   8046  10897    584  -3464   2533       C  
-ATOM   3915  CG  ASP C  89       0.047  23.999  -3.144  1.00 98.17           C  
-ANISOU 3915  CG  ASP C  89    17184   8785  11331    854  -3855   2670       C  
-ATOM   3916  OD1 ASP C  89       0.261  23.053  -3.930  1.00 95.98           O  
-ANISOU 3916  OD1 ASP C  89    16692   9013  10763    457  -3660   2731       O  
-ATOM   3917  OD2 ASP C  89      -1.014  24.662  -3.144  1.00103.30           O  
-ANISOU 3917  OD2 ASP C  89    17868   9156  12226   1447  -4310   2650       O  
-ATOM   3918  N   ARG C  90       2.516  24.123   0.410  1.00 92.34           N  
-ANISOU 3918  N   ARG C  90    16069   7919  11099    435  -2571   1925       N  
-ATOM   3919  CA  ARG C  90       3.401  24.597   1.458  1.00 92.41           C  
-ANISOU 3919  CA  ARG C  90    16190   7708  11211    264  -2298   1764       C  
-ATOM   3920  C   ARG C  90       3.740  23.503   2.457  1.00 85.49           C  
-ANISOU 3920  C   ARG C  90    14650   7350  10481    218  -1805   1421       C  
-ATOM   3921  O   ARG C  90       2.950  22.588   2.702  1.00 83.65           O  
-ANISOU 3921  O   ARG C  90    13849   7525  10409    538  -1721   1230       O  
-ATOM   3922  CB  ARG C  90       2.773  25.775   2.194  1.00 98.77           C  
-ANISOU 3922  CB  ARG C  90    17248   7943  12336    790  -2601   1668       C  
-ATOM   3923  CG  ARG C  90       3.151  27.137   1.660  1.00106.53           C  
-ANISOU 3923  CG  ARG C  90    18969   8332  13174    603  -2891   1940       C  
-ATOM   3924  CD  ARG C  90       2.237  28.183   2.264  1.00112.99           C  
-ANISOU 3924  CD  ARG C  90    19785   8776  14370   1206  -3172   1761       C  
-ATOM   3925  NE  ARG C  90       2.829  29.516   2.298  1.00120.27           N  
-ANISOU 3925  NE  ARG C  90    21187   9270  15240    988  -3217   1838       N  
-ATOM   3926  CZ  ARG C  90       2.885  30.342   1.258  1.00127.42           C  
-ANISOU 3926  CZ  ARG C  90    22569   9923  15922    807  -3502   2134       C  
-ATOM   3927  NH1 ARG C  90       2.399  29.974   0.078  1.00129.69           N  
-ANISOU 3927  NH1 ARG C  90    22920  10358  15998    791  -3771   2385       N  
-ATOM   3928  NH2 ARG C  90       3.432  31.540   1.403  1.00131.56           N  
-ANISOU 3928  NH2 ARG C  90    23511  10051  16425    629  -3518   2170       N  
-ATOM   3929  N   SER C  91       4.933  23.617   3.024  1.00 81.45           N  
-ANISOU 3929  N   SER C  91    14237   6809   9903   -200  -1494   1346       N  
-ATOM   3930  CA  SER C  91       5.378  22.766   4.114  1.00 71.84           C  
-ANISOU 3930  CA  SER C  91    12489   5980   8826   -246  -1083   1043       C  
-ATOM   3931  C   SER C  91       6.462  23.549   4.832  1.00 70.13           C  
-ANISOU 3931  C   SER C  91    12588   5468   8589   -544   -938    975       C  
-ATOM   3932  O   SER C  91       7.103  24.420   4.238  1.00 70.00           O  
-ANISOU 3932  O   SER C  91    13138   5084   8374   -894  -1047   1177       O  
-ATOM   3933  CB  SER C  91       5.939  21.448   3.585  1.00 65.92           C  
-ANISOU 3933  CB  SER C  91    11351   5779   7916   -638   -785   1046       C  
-ATOM   3934  OG  SER C  91       7.016  21.682   2.695  1.00 67.96           O  
-ANISOU 3934  OG  SER C  91    11982   5968   7873  -1250   -725   1236       O  
-ATOM   3935  N   ILE C  92       6.647  23.263   6.115  1.00 68.18           N  
-ANISOU 3935  N   ILE C  92    11999   5378   8527   -426   -698    688       N  
-ATOM   3936  CA  ILE C  92       7.720  23.874   6.886  1.00 67.67           C  
-ANISOU 3936  CA  ILE C  92    12147   5123   8441   -726   -529    577       C  
-ATOM   3937  C   ILE C  92       8.527  22.751   7.508  1.00 62.73           C  
-ANISOU 3937  C   ILE C  92    11033   4997   7806   -981   -170    397       C  
-ATOM   3938  O   ILE C  92       7.971  21.715   7.884  1.00 57.42           O  
-ANISOU 3938  O   ILE C  92     9859   4709   7249   -739    -65    280       O  
-ATOM   3939  CB  ILE C  92       7.158  24.790   7.957  1.00 71.47           C  
-ANISOU 3939  CB  ILE C  92    12741   5252   9164   -316   -637    383       C  
-ATOM   3940  N   PRO C  93       9.846  22.933   7.603  1.00 59.92           N  
-ANISOU 3940  N   PRO C  93    10820   4630   7316  -1478      9    365       N  
-ATOM   3941  CA  PRO C  93      10.629  21.813   8.129  1.00 57.23           C  
-ANISOU 3941  CA  PRO C  93     9992   4757   6995  -1693    295    197       C  
-ATOM   3942  C   PRO C  93      10.371  21.518   9.609  1.00 45.48           C  
-ANISOU 3942  C   PRO C  93     8174   3414   5691  -1384    390    -42       C  
-ATOM   3943  O   PRO C  93       9.844  22.337  10.360  1.00 47.41           O  
-ANISOU 3943  O   PRO C  93     8590   3385   6038  -1101    295   -142       O  
-ATOM   3944  CB  PRO C  93      12.079  22.267   7.919  1.00 59.01           C  
-ANISOU 3944  CB  PRO C  93    10469   4895   7056  -2279    429    172       C  
-ATOM   3945  CG  PRO C  93      12.009  23.761   7.816  1.00 64.84           C  
-ANISOU 3945  CG  PRO C  93    11834   5075   7728  -2303    252    263       C  
-ATOM   3946  CD  PRO C  93      10.691  24.052   7.157  1.00 64.66           C  
-ANISOU 3946  CD  PRO C  93    12000   4826   7740  -1892    -38    472       C  
-ATOM   3947  N   MET C  94      10.742  20.316  10.012  1.00 41.95           N  
-ANISOU 3947  N   MET C  94     7258   3397   5285  -1456    575   -142       N  
-ATOM   3948  CA  MET C  94      10.677  19.936  11.406  1.00 42.91           C  
-ANISOU 3948  CA  MET C  94     7098   3690   5514  -1270    673   -342       C  
-ATOM   3949  C   MET C  94      12.023  19.356  11.794  1.00 42.41           C  
-ANISOU 3949  C   MET C  94     6831   3869   5413  -1645    831   -435       C  
-ATOM   3950  O   MET C  94      12.627  18.617  11.018  1.00 39.64           O  
-ANISOU 3950  O   MET C  94     6300   3726   5036  -1908    908   -380       O  
-ATOM   3951  CB  MET C  94       9.603  18.875  11.614  1.00 39.65           C  
-ANISOU 3951  CB  MET C  94     6284   3574   5207   -918    705   -366       C  
-ATOM   3952  CG  MET C  94       8.164  19.345  11.431  1.00 43.82           C  
-ANISOU 3952  CG  MET C  94     6899   3928   5822   -481    548   -361       C  
-ATOM   3953  SD  MET C  94       7.047  18.004  11.914  1.00 60.74           S  
-ANISOU 3953  SD  MET C  94     8515   6490   8074   -153    666   -477       S  
-ATOM   3954  CE  MET C  94       8.092  17.244  13.130  1.00 34.66           C  
-ANISOU 3954  CE  MET C  94     4989   3448   4733   -403    870   -587       C  
-ATOM   3955  N   THR C  95      12.509  19.700  12.979  1.00 39.00           N  
-ANISOU 3955  N   THR C  95     6412   3417   4989  -1675    869   -602       N  
-ATOM   3956  CA  THR C  95      13.618  18.954  13.550  1.00 37.37           C  
-ANISOU 3956  CA  THR C  95     5916   3498   4784  -1924    971   -711       C  
-ATOM   3957  C   THR C  95      13.043  18.169  14.718  1.00 39.43           C  
-ANISOU 3957  C   THR C  95     5881   3995   5106  -1636    991   -785       C  
-ATOM   3958  O   THR C  95      11.956  18.494  15.196  1.00 36.30           O  
-ANISOU 3958  O   THR C  95     5558   3504   4730  -1319    963   -819       O  
-ATOM   3959  CB  THR C  95      14.774  19.857  13.978  1.00 39.44           C  
-ANISOU 3959  CB  THR C  95     6403   3612   4969  -2255    990   -850       C  
-ATOM   3960  OG1 THR C  95      14.262  20.971  14.708  1.00 41.68           O  
-ANISOU 3960  OG1 THR C  95     6999   3602   5234  -2082    937   -928       O  
-ATOM   3961  CG2 THR C  95      15.521  20.382  12.742  1.00 47.54           C  
-ANISOU 3961  CG2 THR C  95     7660   4502   5901  -2621   1008   -779       C  
-ATOM   3962  N   VAL C  96      13.741  17.129  15.157  1.00 33.90           N  
-ANISOU 3962  N   VAL C  96     4851   3591   4438  -1751   1034   -822       N  
-ATOM   3963  CA  VAL C  96      13.231  16.309  16.261  1.00 33.27           C  
-ANISOU 3963  CA  VAL C  96     4540   3728   4373  -1530   1045   -857       C  
-ATOM   3964  C   VAL C  96      14.218  16.274  17.417  1.00 34.82           C  
-ANISOU 3964  C   VAL C  96     4684   4034   4511  -1696   1007   -977       C  
-ATOM   3965  O   VAL C  96      15.418  16.498  17.235  1.00 36.90           O  
-ANISOU 3965  O   VAL C  96     4946   4297   4778  -1983    983  -1042       O  
-ATOM   3966  CB  VAL C  96      12.903  14.875  15.808  1.00 39.24           C  
-ANISOU 3966  CB  VAL C  96     4946   4737   5227  -1442   1090   -749       C  
-ATOM   3967  CG1 VAL C  96      11.908  14.891  14.653  1.00 38.85           C  
-ANISOU 3967  CG1 VAL C  96     4927   4619   5216  -1288   1117   -645       C  
-ATOM   3968  CG2 VAL C  96      14.171  14.137  15.404  1.00 37.52           C  
-ANISOU 3968  CG2 VAL C  96     4490   4670   5096  -1718   1087   -752       C  
-ATOM   3969  N   ASP C  97      13.709  16.034  18.621  1.00 35.60           N  
-ANISOU 3969  N   ASP C  97     4748   4242   4538  -1539   1002  -1030       N  
-ATOM   3970  CA  ASP C  97      14.581  15.803  19.768  1.00 37.77           C  
-ANISOU 3970  CA  ASP C  97     4952   4673   4727  -1686    929  -1112       C  
-ATOM   3971  C   ASP C  97      13.838  14.902  20.740  1.00 33.63           C  
-ANISOU 3971  C   ASP C  97     4304   4348   4126  -1517    934  -1071       C  
-ATOM   3972  O   ASP C  97      12.646  14.645  20.562  1.00 32.86           O  
-ANISOU 3972  O   ASP C  97     4188   4253   4044  -1302   1028  -1035       O  
-ATOM   3973  CB  ASP C  97      15.017  17.112  20.434  1.00 41.03           C  
-ANISOU 3973  CB  ASP C  97     5639   4927   5023  -1824    916  -1290       C  
-ATOM   3974  CG  ASP C  97      16.297  16.956  21.268  1.00 50.24           C  
-ANISOU 3974  CG  ASP C  97     6711   6262   6117  -2063    807  -1384       C  
-ATOM   3975  OD1 ASP C  97      16.950  15.888  21.202  1.00 48.99           O  
-ANISOU 3975  OD1 ASP C  97     6274   6304   6036  -2117    713  -1309       O  
-ATOM   3976  OD2 ASP C  97      16.660  17.915  21.982  1.00 57.52           O  
-ANISOU 3976  OD2 ASP C  97     7825   7108   6921  -2192    802  -1553       O  
-ATOM   3977  N   PHE C  98      14.552  14.409  21.742  1.00 34.33           N  
-ANISOU 3977  N   PHE C  98     4314   4609   4122  -1633    825  -1081       N  
-ATOM   3978  CA  PHE C  98      14.008  13.400  22.638  1.00 34.14           C  
-ANISOU 3978  CA  PHE C  98     4203   4777   3992  -1543    808   -998       C  
-ATOM   3979  C   PHE C  98      14.484  13.729  24.034  1.00 38.13           C  
-ANISOU 3979  C   PHE C  98     4839   5380   4268  -1685    707  -1095       C  
-ATOM   3980  O   PHE C  98      15.620  14.150  24.216  1.00 39.93           O  
-ANISOU 3980  O   PHE C  98     5075   5607   4490  -1860    579  -1168       O  
-ATOM   3981  CB  PHE C  98      14.522  12.020  22.250  1.00 32.72           C  
-ANISOU 3981  CB  PHE C  98     3748   4722   3961  -1548    708   -827       C  
-ATOM   3982  CG  PHE C  98      14.113  11.582  20.870  1.00 32.68           C  
-ANISOU 3982  CG  PHE C  98     3584   4664   4170  -1448    818   -748       C  
-ATOM   3983  CD1 PHE C  98      14.881  11.929  19.759  1.00 32.59           C  
-ANISOU 3983  CD1 PHE C  98     3499   4564   4319  -1569    814   -784       C  
-ATOM   3984  CD2 PHE C  98      12.969  10.826  20.682  1.00 34.79           C  
-ANISOU 3984  CD2 PHE C  98     3775   4991   4454  -1275    938   -661       C  
-ATOM   3985  CE1 PHE C  98      14.506  11.528  18.484  1.00 28.38           C  
-ANISOU 3985  CE1 PHE C  98     2832   4010   3943  -1519    917   -717       C  
-ATOM   3986  CE2 PHE C  98      12.583  10.424  19.402  1.00 27.45           C  
-ANISOU 3986  CE2 PHE C  98     2687   4038   3703  -1200   1037   -602       C  
-ATOM   3987  CZ  PHE C  98      13.356  10.781  18.312  1.00 27.03           C  
-ANISOU 3987  CZ  PHE C  98     2576   3904   3791  -1323   1018   -623       C  
-ATOM   3988  N   ILE C  99      13.620  13.550  25.018  1.00 37.42           N  
-ANISOU 3988  N   ILE C  99     4849   5395   3975  -1639    774  -1122       N  
-ATOM   3989  CA  ILE C  99      14.000  13.780  26.406  1.00 39.96           C  
-ANISOU 3989  CA  ILE C  99     5311   5850   4023  -1811    681  -1208       C  
-ATOM   3990  C   ILE C  99      13.291  12.783  27.305  1.00 40.59           C  
-ANISOU 3990  C   ILE C  99     5413   6120   3889  -1814    696  -1103       C  
-ATOM   3991  O   ILE C  99      12.254  12.245  26.926  1.00 39.28           O  
-ANISOU 3991  O   ILE C  99     5188   5959   3778  -1672    855  -1054       O  
-ATOM   3992  CB  ILE C  99      13.614  15.191  26.881  1.00 47.63           C  
-ANISOU 3992  CB  ILE C  99     6502   6716   4878  -1853    819  -1483       C  
-ATOM   3993  CG1 ILE C  99      12.131  15.460  26.617  1.00 43.37           C  
-ANISOU 3993  CG1 ILE C  99     6002   6090   4387  -1647   1052  -1590       C  
-ATOM   3994  CG2 ILE C  99      14.502  16.257  26.241  1.00 55.05           C  
-ANISOU 3994  CG2 ILE C  99     7500   7457   5960  -1937    782  -1590       C  
-ATOM   3995  CD1 ILE C  99      11.635  16.759  27.224  1.00 48.36           C  
-ANISOU 3995  CD1 ILE C  99     6826   6614   4935  -1662   1186  -1903       C  
-ATOM   3996  N   ARG C 100      13.874  12.533  28.478  1.00 42.88           N  
-ANISOU 3996  N   ARG C 100     5801   6573   3920  -2001    521  -1070       N  
-ATOM   3997  CA AARG C 100      13.229  11.750  29.522  0.51 45.58           C  
-ANISOU 3997  CA AARG C 100     6263   7095   3962  -2092    536   -983       C  
-ATOM   3998  CA BARG C 100      13.230  11.746  29.520  0.49 45.62           C  
-ANISOU 3998  CA BARG C 100     6267   7099   3967  -2091    535   -983       C  
-ATOM   3999  C   ARG C 100      13.113  12.646  30.738  1.00 48.30           C  
-ANISOU 3999  C   ARG C 100     6833   7552   3967  -2298    593  -1216       C  
-ATOM   4000  O   ARG C 100      13.956  13.521  30.943  1.00 49.65           O  
-ANISOU 4000  O   ARG C 100     7045   7698   4122  -2399    493  -1353       O  
-ATOM   4001  CB AARG C 100      14.086  10.554  29.930  0.51 49.09           C  
-ANISOU 4001  CB AARG C 100     6667   7633   4351  -2166    215   -698       C  
-ATOM   4002  CB BARG C 100      14.069  10.517  29.896  0.49 49.67           C  
-ANISOU 4002  CB BARG C 100     6734   7703   4433  -2159    217   -691       C  
-ATOM   4003  CG AARG C 100      14.278   9.450  28.914  0.51 49.90           C  
-ANISOU 4003  CG AARG C 100     6535   7642   4782  -1994    132   -471       C  
-ATOM   4004  CG BARG C 100      14.493   9.620  28.739  0.49 50.49           C  
-ANISOU 4004  CG BARG C 100     6574   7693   4916  -1983    114   -497       C  
-ATOM   4005  CD AARG C 100      15.452   8.601  29.389  0.51 53.46           C  
-ANISOU 4005  CD AARG C 100     6937   8140   5235  -2057   -268   -262       C  
-ATOM   4006  CD BARG C 100      15.085   8.299  29.241  0.49 52.74           C  
-ANISOU 4006  CD BARG C 100     6839   8034   5166  -2018   -200   -215       C  
-ATOM   4007  NE AARG C 100      15.387   7.208  28.968  0.51 52.65           N  
-ANISOU 4007  NE AARG C 100     6705   7976   5324  -1940   -367     -7       N  
-ATOM   4008  NE BARG C 100      14.053   7.381  29.716  0.49 53.81           N  
-ANISOU 4008  NE BARG C 100     7123   8221   5100  -2047    -87    -57       N  
-ATOM   4009  CZ AARG C 100      16.182   6.670  28.052  0.51 51.02           C  
-ANISOU 4009  CZ AARG C 100     6209   7667   5508  -1811   -519     54       C  
-ATOM   4010  CZ BARG C 100      13.830   7.085  30.993  0.49 56.17           C  
-ANISOU 4010  CZ BARG C 100     7703   8653   4988  -2249   -172     32       C  
-ATOM   4011  NH1AARG C 100      17.105   7.411  27.455  0.51 48.11           N  
-ANISOU 4011  NH1AARG C 100     5657   7269   5353  -1810   -578   -124       N  
-ATOM   4012  NH1BARG C 100      14.577   7.623  31.945  0.49 62.77           N  
-ANISOU 4012  NH1BARG C 100     8686   9597   5567  -2422   -397    -13       N  
-ATOM   4013  NH2AARG C 100      16.053   5.391  27.734  0.51 52.42           N  
-ANISOU 4013  NH2AARG C 100     6280   7771   5866  -1709   -592    265       N  
-ATOM   4014  NH2BARG C 100      12.862   6.242  31.316  0.49 54.39           N  
-ANISOU 4014  NH2BARG C 100     7619   8463   4583  -2314    -25    159       N  
-ATOM   4015  N   LEU C 101      12.086  12.430  31.551  1.00 48.17           N  
-ANISOU 4015  N   LEU C 101     8370   6164   3767  -1427   -484    879       N  
-ATOM   4016  CA  LEU C 101      11.965  13.175  32.804  1.00 53.23           C  
-ANISOU 4016  CA  LEU C 101     8567   7346   4313  -1570   -519    782       C  
-ATOM   4017  C   LEU C 101      12.251  12.298  34.024  1.00 58.59           C  
-ANISOU 4017  C   LEU C 101     9225   8238   4799  -1637   -764   1026       C  
-ATOM   4018  O   LEU C 101      11.904  11.120  34.039  1.00 62.71           O  
-ANISOU 4018  O   LEU C 101    10086   8570   5172  -1767   -957   1337       O  
-ATOM   4019  CB  LEU C 101      10.588  13.830  32.924  1.00 57.57           C  
-ANISOU 4019  CB  LEU C 101     8990   8234   4650  -1827   -474    718       C  
-ATOM   4020  CG  LEU C 101      10.371  15.139  32.164  1.00 58.84           C  
-ANISOU 4020  CG  LEU C 101     9004   8371   4983  -1732   -227    398       C  
-ATOM   4021  CD1 LEU C 101      11.698  15.750  31.751  1.00 58.31           C  
-ANISOU 4021  CD1 LEU C 101     8803   8057   5294  -1466   -110    207       C  
-ATOM   4022  CD2 LEU C 101       9.476  14.962  30.954  1.00 59.00           C  
-ANISOU 4022  CD2 LEU C 101     9286   8146   4985  -1832   -124    467       C  
-ATOM   4023  N   LYS C 102      12.897  12.880  35.034  1.00 62.56           N  
-ANISOU 4023  N   LYS C 102     9357   9104   5307  -1557   -797    896       N  
-ATOM   4024  CA  LYS C 102      13.150  12.190  36.303  1.00 73.03           C  
-ANISOU 4024  CA  LYS C 102    10592  10738   6417  -1602  -1016   1113       C  
-ATOM   4025  C   LYS C 102      12.713  13.037  37.497  1.00 77.21           C  
-ANISOU 4025  C   LYS C 102    10754  11889   6692  -1677  -1076    952       C  
-ATOM   4026  O   LYS C 102      12.690  14.268  37.427  1.00 78.63           O  
-ANISOU 4026  O   LYS C 102    10748  12177   6949  -1607   -983    595       O  
-ATOM   4027  CB  LYS C 102      14.620  11.817  36.429  1.00 74.38           C  
-ANISOU 4027  CB  LYS C 102    10722  10752   6787  -1325  -1052   1163       C  
-ATOM   4028  N   LYS C 114      14.093  16.116  36.809  1.00 65.63           N  
-ANISOU 4028  N   LYS C 114     8845  10228   5866  -1407   -902     59       N  
-ATOM   4029  CA  LYS C 114      15.060  16.789  35.940  1.00 67.09           C  
-ANISOU 4029  CA  LYS C 114     8924  10068   6499  -1328   -816    -47       C  
-ATOM   4030  C   LYS C 114      15.074  16.220  34.512  1.00 63.98           C  
-ANISOU 4030  C   LYS C 114     8741   9265   6304  -1235   -565    142       C  
-ATOM   4031  O   LYS C 114      14.900  15.017  34.316  1.00 64.68           O  
-ANISOU 4031  O   LYS C 114     9088   9235   6254  -1191   -552    397       O  
-ATOM   4032  CB  LYS C 114      16.451  16.715  36.550  1.00 69.81           C  
-ANISOU 4032  CB  LYS C 114     9018  10495   7011  -1265  -1002     41       C  
-ATOM   4033  N   VAL C 115      15.287  17.092  33.527  1.00 63.71           N  
-ANISOU 4033  N   VAL C 115     8631   9000   6577  -1189   -403     20       N  
-ATOM   4034  CA  VAL C 115      15.380  16.690  32.120  1.00 64.02           C  
-ANISOU 4034  CA  VAL C 115     8848   8695   6780  -1020   -154    173       C  
-ATOM   4035  C   VAL C 115      16.695  15.967  31.839  1.00 68.65           C  
-ANISOU 4035  C   VAL C 115     9368   9197   7517   -738   -126    457       C  
-ATOM   4036  O   VAL C 115      17.771  16.504  32.104  1.00 72.60           O  
-ANISOU 4036  O   VAL C 115     9495   9837   8254   -702   -189    520       O  
-ATOM   4037  CB  VAL C 115      15.270  17.905  31.164  1.00 75.15           C  
-ANISOU 4037  CB  VAL C 115    10135   9949   8469  -1028     24      9       C  
-ATOM   4038  CG1 VAL C 115      15.609  17.506  29.726  1.00 75.00           C  
-ANISOU 4038  CG1 VAL C 115    10241   9650   8607   -763    286    202       C  
-ATOM   4039  CG2 VAL C 115      13.883  18.523  31.229  1.00 72.59           C  
-ANISOU 4039  CG2 VAL C 115     9938   9697   7946  -1198     52   -240       C  
-ATOM   4040  N   ILE C 116      16.605  14.751  31.303  1.00 66.32           N  
-ANISOU 4040  N   ILE C 116     9451   8681   7065   -522    -64    651       N  
-ATOM   4041  CA  ILE C 116      17.797  13.975  30.964  1.00 65.70           C  
-ANISOU 4041  CA  ILE C 116     9389   8533   7041   -108    -11    928       C  
-ATOM   4042  C   ILE C 116      17.876  13.694  29.460  1.00 63.53           C  
-ANISOU 4042  C   ILE C 116     9388   7951   6800    275    237   1009       C  
-ATOM   4043  O   ILE C 116      16.851  13.542  28.781  1.00 55.49           O  
-ANISOU 4043  O   ILE C 116     8751   6668   5664    195    283    884       O  
-ATOM   4044  CB  ILE C 116      17.904  12.677  31.819  1.00 58.90           C  
-ANISOU 4044  CB  ILE C 116     8795   7674   5909    -43   -226   1106       C  
-ATOM   4045  CG1 ILE C 116      18.488  11.511  31.021  1.00 57.94           C  
-ANISOU 4045  CG1 ILE C 116     9087   7245   5683    480   -157   1339       C  
-ATOM   4046  CG2 ILE C 116      16.552  12.304  32.408  1.00 62.61           C  
-ANISOU 4046  CG2 ILE C 116     9552   8121   6115   -431   -404   1024       C  
-ATOM   4047  CD1 ILE C 116      18.576  10.211  31.802  1.00 63.07           C  
-ANISOU 4047  CD1 ILE C 116    10083   7803   6077    558   -403   1532       C  
-ATOM   4048  N   GLY C 117      19.100  13.662  28.941  1.00 68.38           N  
-ANISOU 4048  N   GLY C 117     9771   8662   7547    714    392   1247       N  
-ATOM   4049  CA  GLY C 117      19.320  13.481  27.521  1.00 69.63           C  
-ANISOU 4049  CA  GLY C 117    10124   8639   7694   1198    656   1352       C  
-ATOM   4050  C   GLY C 117      18.858  14.711  26.773  1.00 70.55           C  
-ANISOU 4050  C   GLY C 117     9995   8762   8049    985    840   1210       C  
-ATOM   4051  O   GLY C 117      18.625  15.763  27.373  1.00 72.71           O  
-ANISOU 4051  O   GLY C 117     9904   9188   8536    524    755   1064       O  
-ATOM   4052  N   GLY C 118      18.719  14.583  25.460  1.00 69.82           N  
-ANISOU 4052  N   GLY C 118    10146   8489   7892   1360   1072   1243       N  
-ATOM   4053  CA  GLY C 118      18.256  15.694  24.651  1.00 66.94           C  
-ANISOU 4053  CA  GLY C 118     9577   8121   7738   1201   1267   1142       C  
-ATOM   4054  C   GLY C 118      19.356  16.682  24.325  1.00 65.88           C  
-ANISOU 4054  C   GLY C 118     8760   8320   7951   1307   1440   1434       C  
-ATOM   4055  O   GLY C 118      20.401  16.716  24.980  1.00 63.54           O  
-ANISOU 4055  O   GLY C 118     8046   8314   7781   1331   1351   1686       O  
-ATOM   4056  N   ASP C 119      19.123  17.481  23.292  1.00 66.22           N  
-ANISOU 4056  N   ASP C 119     8666   8343   8150   1346   1668   1456       N  
-ATOM   4057  CA  ASP C 119      20.073  18.510  22.913  1.00 69.85           C  
-ANISOU 4057  CA  ASP C 119     8448   9112   8980   1355   1801   1810       C  
-ATOM   4058  C   ASP C 119      20.078  19.600  23.967  1.00 70.76           C  
-ANISOU 4058  C   ASP C 119     8184   9265   9436    690   1513   1693       C  
-ATOM   4059  O   ASP C 119      19.159  19.682  24.785  1.00 67.92           O  
-ANISOU 4059  O   ASP C 119     8112   8713   8983    306   1300   1288       O  
-ATOM   4060  CB  ASP C 119      19.706  19.106  21.551  1.00 67.06           C  
-ANISOU 4060  CB  ASP C 119     8076   8707   8698   1538   2102   1867       C  
-ATOM   4061  CG  ASP C 119      19.891  18.122  20.416  1.00 70.40           C  
-ANISOU 4061  CG  ASP C 119     8848   9144   8759   2308   2374   2016       C  
-ATOM   4062  OD1 ASP C 119      20.610  17.123  20.612  1.00 72.15           O  
-ANISOU 4062  OD1 ASP C 119     9194   9483   8736   2772   2358   2188       O  
-ATOM   4063  OD2 ASP C 119      19.326  18.359  19.327  1.00 72.25           O  
-ANISOU 4063  OD2 ASP C 119     9260   9271   8922   2495   2590   1953       O  
-ATOM   4064  N   ASP C 120      21.130  20.412  23.958  1.00 76.77           N  
-ANISOU 4064  N   ASP C 120     8309  10299  10562    577   1474   2082       N  
-ATOM   4065  CA  ASP C 120      21.148  21.636  24.735  1.00 80.64           C  
-ANISOU 4065  CA  ASP C 120     8499  10728  11414    -52   1143   1972       C  
-ATOM   4066  C   ASP C 120      19.836  22.335  24.411  1.00 78.10           C  
-ANISOU 4066  C   ASP C 120     8528  10052  11093   -283   1184   1541       C  
-ATOM   4067  O   ASP C 120      19.549  22.605  23.246  1.00 78.51           O  
-ANISOU 4067  O   ASP C 120     8593  10046  11192    -85   1476   1643       O  
-ATOM   4068  CB  ASP C 120      22.327  22.508  24.302  1.00 86.95           C  
-ANISOU 4068  CB  ASP C 120     8588  11803  12647   -154   1122   2551       C  
-ATOM   4069  CG  ASP C 120      22.727  23.525  25.354  1.00 90.53           C  
-ANISOU 4069  CG  ASP C 120     8737  12201  13458   -802    620   2525       C  
-ATOM   4070  OD1 ASP C 120      21.908  24.416  25.671  1.00 88.38           O  
-ANISOU 4070  OD1 ASP C 120     8719  11560  13300  -1199    401   2099       O  
-ATOM   4071  OD2 ASP C 120      23.872  23.440  25.848  1.00 95.52           O  
-ANISOU 4071  OD2 ASP C 120     8893  13167  14233   -883    420   2940       O  
-ATOM   4072  N   LEU C 121      19.022  22.600  25.428  1.00 74.55           N  
-ANISOU 4072  N   LEU C 121     8360   9424  10542   -638    911   1079       N  
-ATOM   4073  CA  LEU C 121      17.693  23.161  25.193  1.00 67.56           C  
-ANISOU 4073  CA  LEU C 121     7821   8285   9563   -774    969    680       C  
-ATOM   4074  C   LEU C 121      17.728  24.572  24.595  1.00 63.61           C  
-ANISOU 4074  C   LEU C 121     7086   7625   9457   -980    957    748       C  
-ATOM   4075  O   LEU C 121      16.685  25.171  24.336  1.00 60.05           O  
-ANISOU 4075  O   LEU C 121     6889   6975   8951  -1054   1016    451       O  
-ATOM   4076  CB  LEU C 121      16.843  23.113  26.465  1.00 65.03           C  
-ANISOU 4076  CB  LEU C 121     7808   7931   8970  -1009    696    233       C  
-ATOM   4077  CG  LEU C 121      16.421  21.718  26.926  1.00 65.00           C  
-ANISOU 4077  CG  LEU C 121     8121   8036   8539   -850    727    167       C  
-ATOM   4078  CD1 LEU C 121      15.325  21.803  27.974  1.00 65.10           C  
-ANISOU 4078  CD1 LEU C 121     8393   8099   8243  -1055    534   -210       C  
-ATOM   4079  CD2 LEU C 121      15.970  20.869  25.747  1.00 62.24           C  
-ANISOU 4079  CD2 LEU C 121     8050   7591   8005   -533   1052    278       C  
-ATOM   4080  N   SER C 122      18.934  25.089  24.371  1.00 63.20           N  
-ANISOU 4080  N   SER C 122     6530   7684   9799  -1077    868   1196       N  
-ATOM   4081  CA  SER C 122      19.116  26.335  23.640  1.00 64.75           C  
-ANISOU 4081  CA  SER C 122     6454   7733  10415  -1275    856   1417       C  
-ATOM   4082  C   SER C 122      18.753  26.126  22.167  1.00 60.78           C  
-ANISOU 4082  C   SER C 122     5971   7284   9838   -881   1354   1610       C  
-ATOM   4083  O   SER C 122      18.569  27.084  21.420  1.00 58.62           O  
-ANISOU 4083  O   SER C 122     5575   6869   9829   -982   1429   1733       O  
-ATOM   4084  CB  SER C 122      20.556  26.837  23.779  1.00 69.08           C  
-ANISOU 4084  CB  SER C 122     6382   8462  11401  -1529    596   1982       C  
-ATOM   4085  OG  SER C 122      21.475  25.767  23.697  1.00 69.35           O  
-ANISOU 4085  OG  SER C 122     6125   8932  11294  -1186    775   2390       O  
-ATOM   4086  N   THR C 123      18.651  24.861  21.761  1.00 56.35           N  
-ANISOU 4086  N   THR C 123     5611   6904   8897   -416   1655   1631       N  
-ATOM   4087  CA  THR C 123      18.187  24.514  20.423  1.00 55.69           C  
-ANISOU 4087  CA  THR C 123     5686   6844   8628     18   2080   1713       C  
-ATOM   4088  C   THR C 123      16.715  24.873  20.268  1.00 50.29           C  
-ANISOU 4088  C   THR C 123     5454   5868   7787   -119   2124   1232       C  
-ATOM   4089  O   THR C 123      16.216  25.015  19.154  1.00 48.00           O  
-ANISOU 4089  O   THR C 123     5249   5549   7438    105   2415   1277       O  
-ATOM   4090  CB  THR C 123      18.380  23.021  20.121  1.00 57.50           C  
-ANISOU 4090  CB  THR C 123     6178   7237   8434    564   2282   1775       C  
-ATOM   4091  OG1 THR C 123      17.695  22.238  21.104  1.00 57.15           O  
-ANISOU 4091  OG1 THR C 123     6601   7032   8083    427   2072   1350       O  
-ATOM   4092  CG2 THR C 123      19.851  22.663  20.137  1.00 64.31           C  
-ANISOU 4092  CG2 THR C 123     6557   8485   9393    838   2310   2317       C  
-ATOM   4093  N   LEU C 124      16.023  25.013  21.396  1.00 44.32           N  
-ANISOU 4093  N   LEU C 124     4958   4958   6922   -445   1839    803       N  
-ATOM   4094  CA  LEU C 124      14.625  25.429  21.392  1.00 38.84           C  
-ANISOU 4094  CA  LEU C 124     4622   4090   6045   -560   1863    395       C  
-ATOM   4095  C   LEU C 124      14.495  26.947  21.329  1.00 39.94           C  
-ANISOU 4095  C   LEU C 124     4613   4028   6535   -814   1745    346       C  
-ATOM   4096  O   LEU C 124      13.406  27.472  21.095  1.00 42.07           O  
-ANISOU 4096  O   LEU C 124     5122   4178   6685   -823   1824     83       O  
-ATOM   4097  CB  LEU C 124      13.899  24.916  22.641  1.00 36.35           C  
-ANISOU 4097  CB  LEU C 124     4623   3802   5387   -716   1629     14       C  
-ATOM   4098  CG  LEU C 124      14.076  23.441  23.001  1.00 36.63           C  
-ANISOU 4098  CG  LEU C 124     4838   3971   5109   -563   1617     66       C  
-ATOM   4099  CD1 LEU C 124      13.227  23.076  24.210  1.00 34.10           C  
-ANISOU 4099  CD1 LEU C 124     4773   3728   4456   -760   1391   -243       C  
-ATOM   4100  CD2 LEU C 124      13.719  22.574  21.818  1.00 37.06           C  
-ANISOU 4100  CD2 LEU C 124     5143   3995   4943   -236   1903    180       C  
-ATOM   4101  N   THR C 125      15.599  27.657  21.551  1.00 41.98           N  
-ANISOU 4101  N   THR C 125     4489   4240   7220  -1030   1517    628       N  
-ATOM   4102  CA  THR C 125      15.511  29.107  21.690  1.00 45.44           C  
-ANISOU 4102  CA  THR C 125     4887   4371   8005  -1340   1255    554       C  
-ATOM   4103  C   THR C 125      14.990  29.743  20.410  1.00 48.26           C  
-ANISOU 4103  C   THR C 125     5228   4626   8485  -1205   1569    690       C  
-ATOM   4104  O   THR C 125      15.552  29.536  19.333  1.00 50.86           O  
-ANISOU 4104  O   THR C 125     5237   5137   8950  -1009   1869   1153       O  
-ATOM   4105  CB  THR C 125      16.849  29.738  22.099  1.00 52.47           C  
-ANISOU 4105  CB  THR C 125     5356   5204   9376  -1687    869    925       C  
-ATOM   4106  OG1 THR C 125      17.273  29.183  23.352  1.00 54.74           O  
-ANISOU 4106  OG1 THR C 125     5681   5598   9519  -1809    553    760       O  
-ATOM   4107  CG2 THR C 125      16.701  31.237  22.247  1.00 56.61           C  
-ANISOU 4107  CG2 THR C 125     5967   5285  10257  -2035    498    822       C  
-ATOM   4108  N   GLY C 126      13.897  30.493  20.530  1.00 47.69           N  
-ANISOU 4108  N   GLY C 126     5498   4314   8308  -1244   1518    299       N  
-ATOM   4109  CA  GLY C 126      13.314  31.185  19.395  1.00 48.72           C  
-ANISOU 4109  CA  GLY C 126     5639   4333   8540  -1120   1791    398       C  
-ATOM   4110  C   GLY C 126      12.634  30.262  18.399  1.00 50.41           C  
-ANISOU 4110  C   GLY C 126     5945   4818   8391   -750   2276    428       C  
-ATOM   4111  O   GLY C 126      12.357  30.661  17.271  1.00 54.02           O  
-ANISOU 4111  O   GLY C 126     6335   5295   8894   -569   2511    599       O  
-ATOM   4112  N   LYS C 127      12.356  29.028  18.810  1.00 48.38           N  
-ANISOU 4112  N   LYS C 127     5884   4771   7728   -620   2331    252       N  
-ATOM   4113  CA ALYS C 127      11.727  28.066  17.913  0.73 45.38           C  
-ANISOU 4113  CA ALYS C 127     5691   4579   6971   -298   2631    256       C  
-ATOM   4114  CA BLYS C 127      11.737  28.042  17.931  0.27 46.01           C  
-ANISOU 4114  CA BLYS C 127     5772   4661   7049   -300   2630    256       C  
-ATOM   4115  C   LYS C 127      10.284  27.769  18.312  1.00 42.07           C  
-ANISOU 4115  C   LYS C 127     5663   4206   6114   -318   2560   -138       C  
-ATOM   4116  O   LYS C 127       9.857  28.072  19.429  1.00 42.69           O  
-ANISOU 4116  O   LYS C 127     5855   4266   6097   -515   2421   -418       O  
-ATOM   4117  CB ALYS C 127      12.536  26.763  17.868  0.73 47.94           C  
-ANISOU 4117  CB ALYS C 127     5984   5079   7150    -97   2656    450       C  
-ATOM   4118  CB BLYS C 127      12.529  26.732  17.980  0.27 47.86           C  
-ANISOU 4118  CB BLYS C 127     5983   5067   7135   -119   2653    433       C  
-ATOM   4119  CG ALYS C 127      13.956  26.919  17.339  0.73 53.12           C  
-ANISOU 4119  CG ALYS C 127     6199   5854   8128     44   2697    931       C  
-ATOM   4120  CG BLYS C 127      14.022  26.887  17.723  0.27 52.31           C  
-ANISOU 4120  CG BLYS C 127     6083   5731   8062    -50   2678    904       C  
-ATOM   4121  CD ALYS C 127      13.967  27.268  15.854  0.73 55.06           C  
-ANISOU 4121  CD ALYS C 127     6389   6179   8352    349   2741   1127       C  
-ATOM   4122  CD BLYS C 127      14.317  27.500  16.355  0.27 55.35           C  
-ANISOU 4122  CD BLYS C 127     6275   6197   8559    194   2714   1188       C  
-ATOM   4123  CE ALYS C 127      15.381  27.488  15.348  0.73 58.93           C  
-ANISOU 4123  CE ALYS C 127     6408   6878   9104    495   2766   1653       C  
-ATOM   4124  CE BLYS C 127      13.812  26.625  15.212  0.27 54.54           C  
-ANISOU 4124  CE BLYS C 127     6497   6182   8043    602   2765   1123       C  
-ATOM   4125  NZ ALYS C 127      15.526  28.812  14.672  0.73 60.95           N  
-ANISOU 4125  NZ ALYS C 127     6399   7087   9674    383   2716   1878       N  
-ATOM   4126  NZ BLYS C 127      12.397  26.933  14.843  0.27 51.11           N  
-ANISOU 4126  NZ BLYS C 127     6387   5614   7417    522   2674    799       N  
-ATOM   4127  N   ASN C 128       9.529  27.187  17.386  1.00 39.58           N  
-ANISOU 4127  N   ASN C 128     5747   4127   5165   -599    830    949       N  
-ATOM   4128  CA  ASN C 128       8.181  26.708  17.687  1.00 41.56           C  
-ANISOU 4128  CA  ASN C 128     6015   4432   5342   -472    655    773       C  
-ATOM   4129  C   ASN C 128       8.278  25.266  18.163  1.00 38.41           C  
-ANISOU 4129  C   ASN C 128     5557   4167   4872   -440    812    549       C  
-ATOM   4130  O   ASN C 128       8.647  24.382  17.394  1.00 43.02           O  
-ANISOU 4130  O   ASN C 128     6261   4849   5238   -487   1036    536       O  
-ATOM   4131  CB  ASN C 128       7.289  26.756  16.447  1.00 48.67           C  
-ANISOU 4131  CB  ASN C 128     7092   5448   5953   -498    536    908       C  
-ATOM   4132  CG  ASN C 128       6.635  28.106  16.236  1.00 53.55           C  
-ANISOU 4132  CG  ASN C 128     7732   5915   6700   -418    291   1143       C  
-ATOM   4133  OD1 ASN C 128       7.146  29.141  16.669  1.00 53.52           O  
-ANISOU 4133  OD1 ASN C 128     7724   5654   6957   -404    295   1233       O  
-ATOM   4134  ND2 ASN C 128       5.486  28.100  15.560  1.00 56.50           N  
-ANISOU 4134  ND2 ASN C 128     8132   6440   6894   -378     71   1267       N  
-ATOM   4135  N   VAL C 129       7.946  25.025  19.424  1.00 32.32           N  
-ANISOU 4135  N   VAL C 129     4645   3368   4268   -361    730    376       N  
-ATOM   4136  CA  VAL C 129       8.171  23.714  20.023  1.00 29.69           C  
-ANISOU 4136  CA  VAL C 129     4257   3113   3913   -324    882    222       C  
-ATOM   4137  C   VAL C 129       6.854  22.965  20.165  1.00 32.56           C  
-ANISOU 4137  C   VAL C 129     4677   3552   4142   -307    791     45       C  
-ATOM   4138  O   VAL C 129       5.871  23.513  20.679  1.00 26.87           O  
-ANISOU 4138  O   VAL C 129     3876   2830   3501   -259    591     -5       O  
-ATOM   4139  CB  VAL C 129       8.886  23.822  21.390  1.00 31.63           C  
-ANISOU 4139  CB  VAL C 129     4303   3326   4388   -309    859    199       C  
-ATOM   4140  CG1 VAL C 129       9.146  22.443  21.983  1.00 30.53           C  
-ANISOU 4140  CG1 VAL C 129     4105   3258   4237   -237   1011    124       C  
-ATOM   4141  CG2 VAL C 129      10.201  24.554  21.231  1.00 35.89           C  
-ANISOU 4141  CG2 VAL C 129     4732   3843   5061   -407    916    403       C  
-ATOM   4142  N   LEU C 130       6.838  21.726  19.679  1.00 29.33           N  
-ANISOU 4142  N   LEU C 130     4416   3191   3537   -356    971    -45       N  
-ATOM   4143  CA  LEU C 130       5.701  20.830  19.878  1.00 29.48           C  
-ANISOU 4143  CA  LEU C 130     4496   3280   3425   -424    907   -218       C  
-ATOM   4144  C   LEU C 130       6.146  19.722  20.826  1.00 25.00           C  
-ANISOU 4144  C   LEU C 130     3915   2633   2951   -361   1101   -321       C  
-ATOM   4145  O   LEU C 130       6.998  18.903  20.479  1.00 28.47           O  
-ANISOU 4145  O   LEU C 130     4489   2977   3353   -324   1387   -311       O  
-ATOM   4146  CB  LEU C 130       5.265  20.226  18.535  1.00 32.74           C  
-ANISOU 4146  CB  LEU C 130     5191   3768   3482   -617    955   -257       C  
-ATOM   4147  CG  LEU C 130       3.835  19.701  18.272  1.00 36.91           C  
-ANISOU 4147  CG  LEU C 130     5775   4458   3791   -826    751   -363       C  
-ATOM   4148  CD1 LEU C 130       3.838  18.313  17.586  1.00 36.37           C  
-ANISOU 4148  CD1 LEU C 130     6089   4335   3395  -1065    975   -552       C  
-ATOM   4149  CD2 LEU C 130       2.942  19.725  19.493  1.00 34.77           C  
-ANISOU 4149  CD2 LEU C 130     5224   4249   3738   -757    589   -424       C  
-ATOM   4150  N   ILE C 131       5.599  19.706  22.035  1.00 26.01           N  
-ANISOU 4150  N   ILE C 131     3888   2789   3208   -325    977   -392       N  
-ATOM   4151  CA  ILE C 131       5.938  18.662  22.991  1.00 28.11           C  
-ANISOU 4151  CA  ILE C 131     4150   2991   3538   -277   1123   -435       C  
-ATOM   4152  C   ILE C 131       4.948  17.530  22.815  1.00 27.12           C  
-ANISOU 4152  C   ILE C 131     4206   2859   3240   -424   1179   -586       C  
-ATOM   4153  O   ILE C 131       3.736  17.761  22.803  1.00 29.25           O  
-ANISOU 4153  O   ILE C 131     4412   3265   3436   -548    993   -663       O  
-ATOM   4154  CB  ILE C 131       5.851  19.173  24.433  1.00 27.45           C  
-ANISOU 4154  CB  ILE C 131     3867   2959   3604   -226    975   -437       C  
-ATOM   4155  CG1 ILE C 131       6.913  20.242  24.672  1.00 29.15           C  
-ANISOU 4155  CG1 ILE C 131     3946   3164   3966   -176    905   -304       C  
-ATOM   4156  CG2 ILE C 131       6.053  18.028  25.415  1.00 30.11           C  
-ANISOU 4156  CG2 ILE C 131     4221   3265   3956   -203   1089   -433       C  
-ATOM   4157  CD1 ILE C 131       6.763  20.959  25.997  1.00 27.69           C  
-ANISOU 4157  CD1 ILE C 131     3660   3012   3850   -203    744   -362       C  
-ATOM   4158  N   VAL C 132       5.453  16.308  22.674  1.00 24.92           N  
-ANISOU 4158  N   VAL C 132     4142   2410   2916   -416   1451   -610       N  
-ATOM   4159  CA  VAL C 132       4.568  15.174  22.428  1.00 30.54           C  
-ANISOU 4159  CA  VAL C 132     5115   3049   3441   -632   1532   -774       C  
-ATOM   4160  C   VAL C 132       4.640  14.173  23.579  1.00 31.91           C  
-ANISOU 4160  C   VAL C 132     5315   3082   3728   -577   1665   -759       C  
-ATOM   4161  O   VAL C 132       5.694  13.595  23.845  1.00 30.74           O  
-ANISOU 4161  O   VAL C 132     5216   2746   3719   -368   1892   -626       O  
-ATOM   4162  CB  VAL C 132       4.907  14.462  21.113  1.00 28.43           C  
-ANISOU 4162  CB  VAL C 132     5203   2620   2978   -733   1755   -831       C  
-ATOM   4163  CG1 VAL C 132       3.929  13.330  20.850  1.00 28.94           C  
-ANISOU 4163  CG1 VAL C 132     5508   2625   2864  -1040   1745   -955       C  
-ATOM   4164  CG2 VAL C 132       4.895  15.435  19.932  1.00 29.18           C  
-ANISOU 4164  CG2 VAL C 132     5350   2864   2874   -817   1668   -838       C  
-ATOM   4165  N   GLU C 133       3.496  13.944  24.217  1.00 29.15           N  
-ANISOU 4165  N   GLU C 133     4906   2842   3327   -764   1523   -844       N  
-ATOM   4166  CA  GLU C 133       3.407  13.148  25.434  1.00 30.66           C  
-ANISOU 4166  CA  GLU C 133     5102   2949   3597   -751   1605   -796       C  
-ATOM   4167  C   GLU C 133       2.420  11.994  25.243  1.00 30.46           C  
-ANISOU 4167  C   GLU C 133     5347   2814   3411  -1076   1698   -940       C  
-ATOM   4168  O   GLU C 133       1.545  12.064  24.372  1.00 30.17           O  
-ANISOU 4168  O   GLU C 133     5349   2911   3203  -1350   1571  -1059       O  
-ATOM   4169  CB  GLU C 133       2.958  14.079  26.573  1.00 30.91           C  
-ANISOU 4169  CB  GLU C 133     4796   3241   3707   -704   1380   -759       C  
-ATOM   4170  CG  GLU C 133       2.854  13.472  27.951  1.00 41.25           C  
-ANISOU 4170  CG  GLU C 133     6091   4542   5039   -711   1431   -685       C  
-ATOM   4171  CD  GLU C 133       4.185  13.001  28.499  1.00 43.93           C  
-ANISOU 4171  CD  GLU C 133     6480   4720   5490   -486   1546   -461       C  
-ATOM   4172  OE1 GLU C 133       4.697  11.987  27.987  1.00 39.33           O  
-ANISOU 4172  OE1 GLU C 133     6136   3862   4947   -421   1778   -396       O  
-ATOM   4173  OE2 GLU C 133       4.705  13.630  29.453  1.00 43.28           O  
-ANISOU 4173  OE2 GLU C 133     6206   4788   5452   -384   1410   -338       O  
-ATOM   4174  N   ASP C 134       2.566  10.913  26.012  1.00 29.14           N  
-ANISOU 4174  N   ASP C 134     5358   2419   3294  -1076   1890   -876       N  
-ATOM   4175  CA  ASP C 134       1.582   9.831  25.954  1.00 30.17           C  
-ANISOU 4175  CA  ASP C 134     5697   2487   3280  -1419   1944   -952       C  
-ATOM   4176  C   ASP C 134       0.320  10.124  26.786  1.00 32.56           C  
-ANISOU 4176  C   ASP C 134     5759   3063   3550  -1687   1767  -1020       C  
-ATOM   4177  O   ASP C 134      -0.808   9.867  26.338  1.00 34.82           O  
-ANISOU 4177  O   ASP C 134     6023   3519   3686  -2040   1661  -1122       O  
-ATOM   4178  CB  ASP C 134       2.195   8.470  26.341  1.00 32.74           C  
-ANISOU 4178  CB  ASP C 134     6335   2450   3654  -1304   2245   -828       C  
-ATOM   4179  CG  ASP C 134       2.875   8.485  27.711  1.00 34.93           C  
-ANISOU 4179  CG  ASP C 134     6519   2609   4142  -1042   2306   -613       C  
-ATOM   4180  OD1 ASP C 134       3.125   9.571  28.272  1.00 33.66           O  
-ANISOU 4180  OD1 ASP C 134     5996   2745   4050   -884   2092   -527       O  
-ATOM   4181  OD2 ASP C 134       3.181   7.387  28.219  1.00 39.77           O  
-ANISOU 4181  OD2 ASP C 134     7329   2978   4803   -944   2489   -466       O  
-ATOM   4182  N   ILE C 135       0.505  10.654  27.986  1.00 33.26           N  
-ANISOU 4182  N   ILE C 135     5575   3311   3753  -1473   1703   -883       N  
-ATOM   4183  CA  ILE C 135      -0.631  10.813  28.895  1.00 30.70           C  
-ANISOU 4183  CA  ILE C 135     5003   3269   3392  -1661   1621   -897       C  
-ATOM   4184  C   ILE C 135      -0.450  11.948  29.890  1.00 31.34           C  
-ANISOU 4184  C   ILE C 135     4770   3595   3543  -1406   1515   -836       C  
-ATOM   4185  O   ILE C 135       0.643  12.167  30.426  1.00 32.13           O  
-ANISOU 4185  O   ILE C 135     4905   3606   3697  -1156   1522   -712       O  
-ATOM   4186  CB  ILE C 135      -0.954   9.467  29.602  1.00 38.94           C  
-ANISOU 4186  CB  ILE C 135     6305   4111   4381  -1899   1816   -829       C  
-ATOM   4187  CG1 ILE C 135      -2.203   9.584  30.481  1.00 36.70           C  
-ANISOU 4187  CG1 ILE C 135     5748   4157   4041  -2142   1783   -839       C  
-ATOM   4188  CG2 ILE C 135       0.247   8.969  30.405  1.00 40.31           C  
-ANISOU 4188  CG2 ILE C 135     6666   4016   4636  -1607   1959   -604       C  
-ATOM   4189  CD1 ILE C 135      -2.730   8.232  30.918  1.00 39.27           C  
-ANISOU 4189  CD1 ILE C 135     6313   4325   4284  -2388   1889   -791       C  
-ATOM   4190  N   ILE C 136      -1.523  12.701  30.112  1.00 30.01           N  
-ANISOU 4190  N   ILE C 136     4288   3740   3373  -1480   1424   -920       N  
-ATOM   4191  CA  ILE C 136      -1.529  13.685  31.180  1.00 30.34           C  
-ANISOU 4191  CA  ILE C 136     4124   3963   3442  -1289   1410   -922       C  
-ATOM   4192  C   ILE C 136      -2.469  13.141  32.239  1.00 31.08           C  
-ANISOU 4192  C   ILE C 136     4154   4213   3442  -1493   1561   -914       C  
-ATOM   4193  O   ILE C 136      -3.587  12.709  31.917  1.00 34.74           O  
-ANISOU 4193  O   ILE C 136     4478   4819   3902  -1752   1593   -947       O  
-ATOM   4194  CB  ILE C 136      -2.035  15.068  30.713  1.00 29.53           C  
-ANISOU 4194  CB  ILE C 136     3722   4050   3449  -1131   1286  -1011       C  
-ATOM   4195  CG1 ILE C 136      -1.199  15.614  29.543  1.00 31.29           C  
-ANISOU 4195  CG1 ILE C 136     4015   4134   3741   -982   1140   -992       C  
-ATOM   4196  CG2 ILE C 136      -2.079  16.056  31.915  1.00 31.56           C  
-ANISOU 4196  CG2 ILE C 136     3868   4413   3710   -952   1356  -1072       C  
-ATOM   4197  CD1 ILE C 136       0.246  15.901  29.877  1.00 32.78           C  
-ANISOU 4197  CD1 ILE C 136     4360   4145   3952   -791   1133   -925       C  
-ATOM   4198  N   ASP C 137      -2.023  13.129  33.495  1.00 33.92           N  
-ANISOU 4198  N   ASP C 137     4612   4578   3697  -1428   1644   -847       N  
-ATOM   4199  CA  ASP C 137      -2.853  12.641  34.587  1.00 38.66           C  
-ANISOU 4199  CA  ASP C 137     5189   5340   4160  -1630   1827   -821       C  
-ATOM   4200  C   ASP C 137      -3.081  13.769  35.590  1.00 36.66           C  
-ANISOU 4200  C   ASP C 137     4797   5287   3845  -1461   1856   -920       C  
-ATOM   4201  O   ASP C 137      -4.112  14.431  35.564  1.00 38.69           O  
-ANISOU 4201  O   ASP C 137     4777   5730   4194  -1409   1917  -1031       O  
-ATOM   4202  CB  ASP C 137      -2.202  11.418  35.249  1.00 37.74           C  
-ANISOU 4202  CB  ASP C 137     5403   5012   3923  -1729   1883   -606       C  
-ATOM   4203  CG  ASP C 137      -3.045  10.825  36.363  1.00 43.20           C  
-ANISOU 4203  CG  ASP C 137     6100   5828   4484  -1906   1985   -536       C  
-ATOM   4204  OD1 ASP C 137      -4.262  11.118  36.441  1.00 43.26           O  
-ANISOU 4204  OD1 ASP C 137     5847   6067   4524  -2000   2043   -650       O  
-ATOM   4205  OD2 ASP C 137      -2.480  10.046  37.165  1.00 46.82           O  
-ANISOU 4205  OD2 ASP C 137     6810   6165   4815  -1940   2019   -323       O  
-ATOM   4206  N   THR C 138      -2.117  13.999  36.468  1.00 34.15           N  
-ANISOU 4206  N   THR C 138     4684   4928   3364  -1384   1825   -867       N  
-ATOM   4207  CA  THR C 138      -2.249  15.078  37.441  1.00 39.15           C  
-ANISOU 4207  CA  THR C 138     5299   5692   3886  -1280   1858  -1001       C  
-ATOM   4208  C   THR C 138      -1.912  16.381  36.736  1.00 38.70           C  
-ANISOU 4208  C   THR C 138     5145   5570   3989  -1059   1763  -1163       C  
-ATOM   4209  O   THR C 138      -2.377  17.447  37.124  1.00 40.41           O  
-ANISOU 4209  O   THR C 138     5298   5822   4235   -926   1832  -1317       O  
-ATOM   4210  CB  THR C 138      -1.280  14.905  38.613  1.00 40.09           C  
-ANISOU 4210  CB  THR C 138     5702   5833   3698  -1367   1810   -886       C  
-ATOM   4211  OG1 THR C 138       0.068  14.914  38.113  1.00 35.67           O  
-ANISOU 4211  OG1 THR C 138     5238   5143   3172  -1295   1602   -757       O  
-ATOM   4212  CG2 THR C 138      -1.552  13.599  39.337  1.00 43.94           C  
-ANISOU 4212  CG2 THR C 138     6317   6349   4028  -1564   1894   -664       C  
-ATOM   4213  N   GLY C 139      -1.100  16.279  35.689  1.00 32.93           N  
-ANISOU 4213  N   GLY C 139     4430   4693   3390   -997   1603  -1096       N  
-ATOM   4214  CA  GLY C 139      -0.625  17.450  34.972  1.00 34.91           C  
-ANISOU 4214  CA  GLY C 139     4621   4839   3803   -803   1464  -1187       C  
-ATOM   4215  C   GLY C 139       0.680  18.010  35.514  1.00 38.21           C  
-ANISOU 4215  C   GLY C 139     5225   5184   4109   -793   1309  -1157       C  
-ATOM   4216  O   GLY C 139       1.244  18.955  34.961  1.00 31.79           O  
-ANISOU 4216  O   GLY C 139     4399   4258   3421   -686   1185  -1205       O  
-ATOM   4217  N   LYS C 140       1.182  17.429  36.597  1.00 38.36           N  
-ANISOU 4217  N   LYS C 140     5409   5287   3877   -943   1291  -1041       N  
-ATOM   4218  CA ALYS C 140       2.415  17.915  37.210  0.72 41.25           C  
-ANISOU 4218  CA ALYS C 140     5912   5670   4091  -1014   1084   -966       C  
-ATOM   4219  CA BLYS C 140       2.409  17.935  37.201  0.28 41.37           C  
-ANISOU 4219  CA BLYS C 140     5926   5684   4109  -1012   1084   -970       C  
-ATOM   4220  C   LYS C 140       3.628  17.776  36.295  1.00 39.16           C  
-ANISOU 4220  C   LYS C 140     5548   5293   4037   -916    869   -743       C  
-ATOM   4221  O   LYS C 140       4.463  18.677  36.219  1.00 45.54           O  
-ANISOU 4221  O   LYS C 140     6352   6082   4869   -937    700   -757       O  
-ATOM   4222  CB ALYS C 140       2.668  17.202  38.534  0.72 45.38           C  
-ANISOU 4222  CB ALYS C 140     6606   6366   4270  -1215   1064   -804       C  
-ATOM   4223  CB BLYS C 140       2.656  17.306  38.574  0.28 45.93           C  
-ANISOU 4223  CB BLYS C 140     6684   6440   4329  -1220   1065   -827       C  
-ATOM   4224  CG ALYS C 140       1.564  17.407  39.549  0.72 50.78           C  
-ANISOU 4224  CG ALYS C 140     7424   7189   4682  -1342   1326  -1032       C  
-ATOM   4225  CG BLYS C 140       1.927  18.013  39.708  0.28 51.33           C  
-ANISOU 4225  CG BLYS C 140     7558   7252   4693  -1367   1249  -1109       C  
-ATOM   4226  CD ALYS C 140       1.687  16.407  40.691  0.72 55.77           C  
-ANISOU 4226  CD ALYS C 140     8229   7996   4966  -1553   1329   -795       C  
-ATOM   4227  CD BLYS C 140       0.963  17.078  40.424  0.28 55.25           C  
-ANISOU 4227  CD BLYS C 140     8087   7876   5027  -1459   1482  -1050       C  
-ATOM   4228  CE ALYS C 140       0.542  16.539  41.679  0.72 59.79           C  
-ANISOU 4228  CE ALYS C 140     8803   8597   5318  -1621   1570   -964       C  
-ATOM   4229  CE BLYS C 140       1.696  15.947  41.130  0.28 57.04           C  
-ANISOU 4229  CE BLYS C 140     8457   8223   4992  -1636   1337   -681       C  
-ATOM   4230  NZ ALYS C 140       0.679  17.750  42.532  0.72 65.41           N  
-ANISOU 4230  NZ ALYS C 140     9693   9330   5831  -1683   1548  -1199       N  
-ATOM   4231  NZ BLYS C 140       0.778  14.873  41.603  0.28 59.25           N  
-ANISOU 4231  NZ BLYS C 140     8754   8548   5211  -1713   1549   -560       N  
-ATOM   4232  N   THR C 141       3.730  16.648  35.596  1.00 34.12           N  
-ANISOU 4232  N   THR C 141     4851   4565   3550   -828    914   -545       N  
-ATOM   4233  CA  THR C 141       4.870  16.447  34.699  1.00 33.60           C  
-ANISOU 4233  CA  THR C 141     4693   4383   3692   -692    808   -334       C  
-ATOM   4234  C   THR C 141       4.892  17.541  33.634  1.00 35.31           C  
-ANISOU 4234  C   THR C 141     4819   4513   4084   -607    770   -503       C  
-ATOM   4235  O   THR C 141       5.933  18.168  33.394  1.00 33.95           O  
-ANISOU 4235  O   THR C 141     4573   4336   3991   -590    627   -406       O  
-ATOM   4236  CB  THR C 141       4.865  15.047  34.054  1.00 39.30           C  
-ANISOU 4236  CB  THR C 141     5457   4935   4539   -597    961   -159       C  
-ATOM   4237  OG1 THR C 141       4.972  14.060  35.086  1.00 44.03           O  
-ANISOU 4237  OG1 THR C 141     6160   5572   4997   -658    986     69       O  
-ATOM   4238  CG2 THR C 141       6.033  14.888  33.083  1.00 40.49           C  
-ANISOU 4238  CG2 THR C 141     5523   4950   4913   -408    949     31       C  
-ATOM   4239  N   MET C 142       3.738  17.813  33.026  1.00 30.64           N  
-ANISOU 4239  N   MET C 142     4210   3880   3551   -575    883   -714       N  
-ATOM   4240  CA  MET C 142       3.703  18.810  31.952  1.00 29.22           C  
-ANISOU 4240  CA  MET C 142     3956   3613   3534   -478    834   -807       C  
-ATOM   4241  C   MET C 142       3.924  20.223  32.487  1.00 31.59           C  
-ANISOU 4241  C   MET C 142     4291   3897   3815   -501    750   -939       C  
-ATOM   4242  O   MET C 142       4.611  21.022  31.855  1.00 30.53           O  
-ANISOU 4242  O   MET C 142     4138   3664   3798   -472    651   -902       O  
-ATOM   4243  CB  MET C 142       2.412  18.719  31.137  1.00 30.65           C  
-ANISOU 4243  CB  MET C 142     4062   3802   3781   -444    922   -921       C  
-ATOM   4244  CG  MET C 142       2.483  19.440  29.783  1.00 38.20           C  
-ANISOU 4244  CG  MET C 142     4959   4676   4878   -347    844   -908       C  
-ATOM   4245  SD  MET C 142       3.987  19.141  28.821  1.00 45.35           S  
-ANISOU 4245  SD  MET C 142     5931   5459   5840   -314    810   -719       S  
-ATOM   4246  CE  MET C 142       3.882  17.379  28.529  1.00 30.69           C  
-ANISOU 4246  CE  MET C 142     4199   3555   3908   -376    971   -659       C  
-ATOM   4247  N   GLN C 143       3.351  20.522  33.653  1.00 29.69           N  
-ANISOU 4247  N   GLN C 143     4145   3728   3407   -581    823  -1102       N  
-ATOM   4248  CA  GLN C 143       3.639  21.771  34.348  1.00 33.99           C  
-ANISOU 4248  CA  GLN C 143     4843   4207   3865   -664    783  -1273       C  
-ATOM   4249  C   GLN C 143       5.148  21.981  34.453  1.00 39.60           C  
-ANISOU 4249  C   GLN C 143     5579   4932   4536   -827    540  -1103       C  
-ATOM   4250  O   GLN C 143       5.670  23.057  34.137  1.00 44.45           O  
-ANISOU 4250  O   GLN C 143     6246   5407   5236   -880    449  -1157       O  
-ATOM   4251  CB  GLN C 143       3.079  21.705  35.770  1.00 44.66           C  
-ANISOU 4251  CB  GLN C 143     6365   5676   4927   -796    919  -1441       C  
-ATOM   4252  CG  GLN C 143       1.953  22.662  36.085  1.00 51.56           C  
-ANISOU 4252  CG  GLN C 143     7322   6444   5825   -677   1175  -1738       C  
-ATOM   4253  CD  GLN C 143       1.562  22.604  37.564  1.00 58.57           C  
-ANISOU 4253  CD  GLN C 143     8388   7454   6412   -809   1293  -1823       C  
-ATOM   4254  OE1 GLN C 143       2.212  21.922  38.366  1.00 59.42           O  
-ANISOU 4254  OE1 GLN C 143     8630   7736   6211  -1063   1189  -1743       O  
-ATOM   4255  NE2 GLN C 143       0.499  23.313  37.925  1.00 57.89           N  
-ANISOU 4255  NE2 GLN C 143     8308   7288   6398   -635   1520  -1965       N  
-ATOM   4256  N   THR C 144       5.840  20.939  34.902  1.00 40.20           N  
-ANISOU 4256  N   THR C 144     5592   5180   4502   -910    437   -857       N  
-ATOM   4257  CA  THR C 144       7.278  21.008  35.152  1.00 49.90           C  
-ANISOU 4257  CA  THR C 144     6741   6520   5698  -1069    184   -610       C  
-ATOM   4258  C   THR C 144       8.064  21.174  33.853  1.00 48.03           C  
-ANISOU 4258  C   THR C 144     6303   6186   5760   -942    145   -437       C  
-ATOM   4259  O   THR C 144       8.954  22.015  33.766  1.00 52.03           O  
-ANISOU 4259  O   THR C 144     6761   6699   6309  -1098    -20   -380       O  
-ATOM   4260  CB  THR C 144       7.776  19.768  35.933  1.00 58.17           C  
-ANISOU 4260  CB  THR C 144     7720   7783   6600  -1113     95   -298       C  
-ATOM   4261  OG1 THR C 144       6.956  19.571  37.094  1.00 59.87           O  
-ANISOU 4261  OG1 THR C 144     8153   8097   6497  -1249    171   -452       O  
-ATOM   4262  CG2 THR C 144       9.225  19.948  36.372  1.00 63.77           C  
-ANISOU 4262  CG2 THR C 144     8275   8697   7258  -1305   -219      6       C  
-ATOM   4263  N   LEU C 145       7.721  20.382  32.841  1.00 44.08           N  
-ANISOU 4263  N   LEU C 145     5716   5598   5435   -705    313   -364       N  
-ATOM   4264  CA  LEU C 145       8.413  20.449  31.554  1.00 42.53           C  
-ANISOU 4264  CA  LEU C 145     5378   5315   5467   -582    347   -215       C  
-ATOM   4265  C   LEU C 145       8.227  21.813  30.888  1.00 40.79           C  
-ANISOU 4265  C   LEU C 145     5217   4952   5331   -622    318   -381       C  
-ATOM   4266  O   LEU C 145       9.192  22.419  30.408  1.00 42.39           O  
-ANISOU 4266  O   LEU C 145     5322   5140   5645   -693    237   -245       O  
-ATOM   4267  CB  LEU C 145       7.932  19.337  30.629  1.00 40.31           C  
-ANISOU 4267  CB  LEU C 145     5110   4938   5267   -381    563   -180       C  
-ATOM   4268  CG  LEU C 145       8.605  19.248  29.264  1.00 44.83           C  
-ANISOU 4268  CG  LEU C 145     5607   5420   6008   -255    676    -50       C  
-ATOM   4269  CD1 LEU C 145      10.121  19.352  29.396  1.00 47.76           C  
-ANISOU 4269  CD1 LEU C 145     5745   5898   6503   -257    604    252       C  
-ATOM   4270  CD2 LEU C 145       8.218  17.953  28.556  1.00 43.99           C  
-ANISOU 4270  CD2 LEU C 145     5614   5195   5905   -120    915    -42       C  
-ATOM   4271  N   LEU C 146       6.987  22.297  30.870  1.00 33.99           N  
-ANISOU 4271  N   LEU C 146     4494   3982   4438   -567    398   -635       N  
-ATOM   4272  CA  LEU C 146       6.701  23.615  30.310  1.00 32.66           C  
-ANISOU 4272  CA  LEU C 146     4407   3625   4377   -549    388   -756       C  
-ATOM   4273  C   LEU C 146       7.536  24.706  30.959  1.00 38.61           C  
-ANISOU 4273  C   LEU C 146     5267   4305   5096   -787    249   -796       C  
-ATOM   4274  O   LEU C 146       8.067  25.587  30.274  1.00 38.00           O  
-ANISOU 4274  O   LEU C 146     5206   4082   5151   -845    199   -731       O  
-ATOM   4275  CB  LEU C 146       5.221  23.946  30.432  1.00 33.90           C  
-ANISOU 4275  CB  LEU C 146     4640   3704   4537   -407    513   -976       C  
-ATOM   4276  CG  LEU C 146       4.319  23.283  29.407  1.00 34.96           C  
-ANISOU 4276  CG  LEU C 146     4652   3892   4738   -240    587   -921       C  
-ATOM   4277  CD1 LEU C 146       2.884  23.586  29.713  1.00 39.38           C  
-ANISOU 4277  CD1 LEU C 146     5177   4459   5327   -112    694  -1080       C  
-ATOM   4278  CD2 LEU C 146       4.683  23.805  28.028  1.00 32.23           C  
-ANISOU 4278  CD2 LEU C 146     4285   3445   4517   -182    530   -776       C  
-ATOM   4279  N   SER C 147       7.660  24.650  32.283  1.00 44.68           N  
-ANISOU 4279  N   SER C 147     6142   5180   5653   -981    180   -897       N  
-ATOM   4280  CA  SER C 147       8.482  25.620  32.998  1.00 46.62           C  
-ANISOU 4280  CA  SER C 147     6539   5386   5787  -1320      9   -958       C  
-ATOM   4281  C   SER C 147       9.953  25.514  32.588  1.00 49.95           C  
-ANISOU 4281  C   SER C 147     6705   5968   6305  -1496   -195   -625       C  
-ATOM   4282  O   SER C 147      10.628  26.522  32.415  1.00 52.67           O  
-ANISOU 4282  O   SER C 147     7106   6200   6705  -1740   -307   -617       O  
-ATOM   4283  CB  SER C 147       8.339  25.446  34.512  1.00 52.34           C  
-ANISOU 4283  CB  SER C 147     7455   6260   6173  -1547    -44  -1115       C  
-ATOM   4284  OG  SER C 147       9.175  26.358  35.196  1.00 56.18           O  
-ANISOU 4284  OG  SER C 147     8129   6730   6486  -1970   -248  -1188       O  
-ATOM   4285  N   LEU C 148      10.440  24.288  32.429  1.00 50.72           N  
-ANISOU 4285  N   LEU C 148     6516   6308   6446  -1364   -209   -335       N  
-ATOM   4286  CA  LEU C 148      11.821  24.054  32.016  1.00 56.12           C  
-ANISOU 4286  CA  LEU C 148     6866   7180   7278  -1441   -332     37       C  
-ATOM   4287  C   LEU C 148      12.097  24.617  30.620  1.00 56.49           C  
-ANISOU 4287  C   LEU C 148     6839   7056   7567  -1347   -209    105       C  
-ATOM   4288  O   LEU C 148      13.033  25.398  30.421  1.00 55.74           O  
-ANISOU 4288  O   LEU C 148     6635   6987   7556  -1600   -332    240       O  
-ATOM   4289  CB  LEU C 148      12.121  22.558  32.030  1.00 60.69           C  
-ANISOU 4289  CB  LEU C 148     7193   7958   7909  -1195   -261    330       C  
-ATOM   4290  CG  LEU C 148      13.263  22.123  32.934  1.00 67.50           C  
-ANISOU 4290  CG  LEU C 148     7771   9160   8715  -1371   -516    690       C  
-ATOM   4291  CD1 LEU C 148      12.881  20.856  33.689  1.00 70.95           C  
-ANISOU 4291  CD1 LEU C 148     8226   9705   9028  -1199   -482    804       C  
-ATOM   4292  CD2 LEU C 148      14.542  21.928  32.128  1.00 66.67           C  
-ANISOU 4292  CD2 LEU C 148     7229   9196   8906  -1279   -493   1097       C  
-ATOM   4293  N   VAL C 149      11.271  24.204  29.663  1.00 51.81           N  
-ANISOU 4293  N   VAL C 149     6315   6314   7055  -1033     22     28       N  
-ATOM   4294  CA  VAL C 149      11.408  24.616  28.273  1.00 45.32           C  
-ANISOU 4294  CA  VAL C 149     5473   5357   6390   -935    154    106       C  
-ATOM   4295  C   VAL C 149      11.394  26.134  28.138  1.00 46.47           C  
-ANISOU 4295  C   VAL C 149     5803   5279   6574  -1146     62     -2       C  
-ATOM   4296  O   VAL C 149      12.195  26.716  27.401  1.00 47.50           O  
-ANISOU 4296  O   VAL C 149     5846   5378   6825  -1269     65    179       O  
-ATOM   4297  CB  VAL C 149      10.290  23.998  27.415  1.00 40.25           C  
-ANISOU 4297  CB  VAL C 149     4952   4613   5728   -649    349     -7       C  
-ATOM   4298  CG1 VAL C 149      10.234  24.653  26.045  1.00 42.08           C  
-ANISOU 4298  CG1 VAL C 149     5249   4706   6034   -603    433     50       C  
-ATOM   4299  CG2 VAL C 149      10.499  22.501  27.287  1.00 38.30           C  
-ANISOU 4299  CG2 VAL C 149     4584   4495   5472   -472    501    121       C  
-ATOM   4300  N   ARG C 150      10.500  26.775  28.877  1.00 46.36           N  
-ANISOU 4300  N   ARG C 150     6062   5086   6467  -1189     22   -290       N  
-ATOM   4301  CA  ARG C 150      10.354  28.221  28.791  1.00 50.75           C  
-ANISOU 4301  CA  ARG C 150     6882   5318   7084  -1337     -4   -422       C  
-ATOM   4302  C   ARG C 150      11.587  28.987  29.270  1.00 56.67           C  
-ANISOU 4302  C   ARG C 150     7636   6077   7820  -1792   -191   -344       C  
-ATOM   4303  O   ARG C 150      11.768  30.153  28.912  1.00 56.97           O  
-ANISOU 4303  O   ARG C 150     7875   5819   7953  -1969   -197   -367       O  
-ATOM   4304  CB  ARG C 150       9.092  28.682  29.518  1.00 49.48           C  
-ANISOU 4304  CB  ARG C 150     7018   4931   6850  -1218     82   -758       C  
-ATOM   4305  CG  ARG C 150       7.830  28.377  28.733  1.00 48.29           C  
-ANISOU 4305  CG  ARG C 150     6833   4722   6793   -815    241   -776       C  
-ATOM   4306  CD  ARG C 150       6.565  28.850  29.435  1.00 56.12           C  
-ANISOU 4306  CD  ARG C 150     8025   5523   7776   -642    379  -1058       C  
-ATOM   4307  NE  ARG C 150       5.395  28.602  28.595  1.00 59.49           N  
-ANISOU 4307  NE  ARG C 150     8317   5963   8323   -286    478   -991       N  
-ATOM   4308  CZ  ARG C 150       4.234  28.122  29.031  1.00 58.35           C  
-ANISOU 4308  CZ  ARG C 150     8093   5926   8152    -85    598  -1120       C  
-ATOM   4309  NH1 ARG C 150       4.067  27.838  30.314  1.00 59.24           N  
-ANISOU 4309  NH1 ARG C 150     8296   6113   8100   -180    681  -1343       N  
-ATOM   4310  NH2 ARG C 150       3.238  27.932  28.176  1.00 58.46           N  
-ANISOU 4310  NH2 ARG C 150     7924   6009   8278    174    625  -1000       N  
-ATOM   4311  N   GLN C 151      12.439  28.327  30.056  1.00 58.84           N  
-ANISOU 4311  N   GLN C 151     7678   6697   7982  -2004   -359   -211       N  
-ATOM   4312  CA  GLN C 151      13.691  28.938  30.518  1.00 63.51           C  
-ANISOU 4312  CA  GLN C 151     8172   7415   8544  -2508   -604    -68       C  
-ATOM   4313  C   GLN C 151      14.666  29.117  29.357  1.00 62.14           C  
-ANISOU 4313  C   GLN C 151     7689   7310   8612  -2555   -561    278       C  
-ATOM   4314  O   GLN C 151      15.688  29.781  29.493  1.00 64.02           O  
-ANISOU 4314  O   GLN C 151     7814   7631   8879  -2975   -730    427       O  
-ATOM   4315  CB  GLN C 151      14.361  28.080  31.596  1.00 66.19           C  
-ANISOU 4315  CB  GLN C 151     8243   8195   8709  -2688   -836     94       C  
-ATOM   4316  CG  GLN C 151      13.471  27.701  32.768  1.00 68.25           C  
-ANISOU 4316  CG  GLN C 151     8782   8470   8680  -2651   -855   -192       C  
-ATOM   4317  CD  GLN C 151      13.442  28.750  33.862  1.00 77.54           C  
-ANISOU 4317  CD  GLN C 151    10375   9513   9576  -3075   -997   -499       C  
-ATOM   4318  OE1 GLN C 151      14.385  29.527  34.026  1.00 81.26           O  
-ANISOU 4318  OE1 GLN C 151    10820  10032  10025  -3381  -1159   -404       O  
-ATOM   4319  NE2 GLN C 151      12.353  28.773  34.625  1.00 80.32           N  
-ANISOU 4319  NE2 GLN C 151    11096   9711   9710  -2951   -850   -851       N  
-ATOM   4320  N   TYR C 152      14.351  28.505  28.221  1.00 59.99           N  
-ANISOU 4320  N   TYR C 152     7290   7027   8476  -2137   -316    401       N  
-ATOM   4321  CA  TYR C 152      15.217  28.572  27.053  1.00 57.20           C  
-ANISOU 4321  CA  TYR C 152     6671   6754   8308  -2140   -190    722       C  
-ATOM   4322  C   TYR C 152      14.618  29.437  25.950  1.00 52.34           C  
-ANISOU 4322  C   TYR C 152     6358   5774   7756  -2049    -36    657       C  
-ATOM   4323  O   TYR C 152      15.099  29.443  24.814  1.00 47.97           O  
-ANISOU 4323  O   TYR C 152     5668   5261   7298  -1996    131    898       O  
-ATOM   4324  CB  TYR C 152      15.550  27.164  26.564  1.00 55.53           C  
-ANISOU 4324  CB  TYR C 152     6101   6833   8163  -1784      5    955       C  
-ATOM   4325  CG  TYR C 152      16.530  26.475  27.484  1.00 62.92           C  
-ANISOU 4325  CG  TYR C 152     6624   8156   9127  -1900   -159   1204       C  
-ATOM   4326  CD1 TYR C 152      17.898  26.679  27.345  1.00 65.83           C  
-ANISOU 4326  CD1 TYR C 152     6545   8805   9663  -2148   -221   1580       C  
-ATOM   4327  CD2 TYR C 152      16.088  25.652  28.519  1.00 65.30           C  
-ANISOU 4327  CD2 TYR C 152     6951   8572   9289  -1783   -269   1111       C  
-ATOM   4328  CE1 TYR C 152      18.805  26.065  28.195  1.00 71.69           C  
-ANISOU 4328  CE1 TYR C 152     6895   9931  10412  -2176   -409   1839       C  
-ATOM   4329  CE2 TYR C 152      16.991  25.028  29.373  1.00 69.57           C  
-ANISOU 4329  CE2 TYR C 152     7100   9488   9845  -1881   -462   1416       C  
-ATOM   4330  CZ  TYR C 152      18.349  25.242  29.206  1.00 73.00           C  
-ANISOU 4330  CZ  TYR C 152     7050  10220  10466  -2097   -554   1819       C  
-ATOM   4331  OH  TYR C 152      19.250  24.630  30.050  1.00 77.01           O  
-ANISOU 4331  OH  TYR C 152     7198  11105  10958  -2094   -765   2135       O  
-ATOM   4332  N   ASN C 153      13.566  30.168  26.309  1.00 47.90           N  
-ANISOU 4332  N   ASN C 153     7026   4058   7115  -1805    733   -179       N  
-ATOM   4333  CA  ASN C 153      12.991  31.199  25.452  1.00 45.58           C  
-ANISOU 4333  CA  ASN C 153     6855   3667   6797  -1755    876   -108       C  
-ATOM   4334  C   ASN C 153      12.521  30.731  24.075  1.00 42.07           C  
-ANISOU 4334  C   ASN C 153     6359   3339   6287  -1697   1064    -20       C  
-ATOM   4335  O   ASN C 153      12.899  31.312  23.055  1.00 41.40           O  
-ANISOU 4335  O   ASN C 153     6258   3253   6219  -1800   1149    126       O  
-ATOM   4336  CB  ASN C 153      13.976  32.364  25.319  1.00 53.70           C  
-ANISOU 4336  CB  ASN C 153     7878   4564   7961  -1920    820    -13       C  
-ATOM   4337  CG  ASN C 153      14.472  32.856  26.667  1.00 62.74           C  
-ANISOU 4337  CG  ASN C 153     9086   5597   9157  -2030    634   -113       C  
-ATOM   4338  OD1 ASN C 153      15.646  32.693  27.008  1.00 70.49           O  
-ANISOU 4338  OD1 ASN C 153     9917   6602  10264  -2192    495    -78       O  
-ATOM   4339  ND2 ASN C 153      13.575  33.453  27.447  1.00 57.44           N  
-ANISOU 4339  ND2 ASN C 153     8620   4797   8406  -1964    647   -250       N  
-ATOM   4340  N   PRO C 154      11.664  29.699  24.040  1.00 43.13           N  
-ANISOU 4340  N   PRO C 154     6484   3584   6320  -1570   1126    -97       N  
-ATOM   4341  CA  PRO C 154      11.132  29.297  22.738  1.00 42.28           C  
-ANISOU 4341  CA  PRO C 154     6361   3594   6109  -1565   1297    -18       C  
-ATOM   4342  C   PRO C 154      10.181  30.378  22.254  1.00 43.34           C  
-ANISOU 4342  C   PRO C 154     6672   3573   6222  -1524   1291    157       C  
-ATOM   4343  O   PRO C 154       9.732  31.203  23.051  1.00 48.09           O  
-ANISOU 4343  O   PRO C 154     7376   3962   6934  -1429   1203    130       O  
-ATOM   4344  CB  PRO C 154      10.355  28.021  23.059  1.00 35.47           C  
-ANISOU 4344  CB  PRO C 154     5463   2837   5178  -1441   1322   -154       C  
-ATOM   4345  CG  PRO C 154       9.911  28.215  24.484  1.00 36.41           C  
-ANISOU 4345  CG  PRO C 154     5679   2847   5309  -1343   1176   -251       C  
-ATOM   4346  CD  PRO C 154      10.980  29.022  25.159  1.00 41.10           C  
-ANISOU 4346  CD  PRO C 154     6274   3343   5999  -1462   1044   -238       C  
-ATOM   4347  N   LYS C 155       9.888  30.389  20.964  1.00 44.50           N  
-ANISOU 4347  N   LYS C 155     6843   3825   6239  -1616   1375    344       N  
-ATOM   4348  CA  LYS C 155       8.987  31.388  20.424  1.00 50.45           C  
-ANISOU 4348  CA  LYS C 155     7736   4404   7027  -1593   1296    614       C  
-ATOM   4349  C   LYS C 155       7.567  31.023  20.819  1.00 48.05           C  
-ANISOU 4349  C   LYS C 155     7451   4037   6768  -1358   1254    569       C  
-ATOM   4350  O   LYS C 155       6.764  31.877  21.201  1.00 50.60           O  
-ANISOU 4350  O   LYS C 155     7827   4070   7329  -1208   1180    642       O  
-ATOM   4351  CB  LYS C 155       9.108  31.421  18.905  1.00 55.86           C  
-ANISOU 4351  CB  LYS C 155     8448   5311   7468  -1822   1330    880       C  
-ATOM   4352  CG  LYS C 155       8.299  32.512  18.233  1.00 66.16           C  
-ANISOU 4352  CG  LYS C 155     9882   6430   8826  -1848   1152   1283       C  
-ATOM   4353  CD  LYS C 155       8.199  32.249  16.741  1.00 70.60           C  
-ANISOU 4353  CD  LYS C 155    10480   7341   9002  -2108   1125   1543       C  
-ATOM   4354  CE  LYS C 155       7.305  33.261  16.054  1.00 76.58           C  
-ANISOU 4354  CE  LYS C 155    11329   7935   9832  -2132    837   2030       C  
-ATOM   4355  NZ  LYS C 155       6.994  32.845  14.659  1.00 80.55           N  
-ANISOU 4355  NZ  LYS C 155    11868   8858   9881  -2379    747   2253       N  
-ATOM   4356  N   MET C 156       7.278  29.731  20.732  1.00 44.37           N  
-ANISOU 4356  N   MET C 156     6887   3854   6119  -1307   1301    418       N  
-ATOM   4357  CA  MET C 156       5.944  29.187  20.978  1.00 42.98           C  
-ANISOU 4357  CA  MET C 156     6664   3726   5942  -1095   1247    367       C  
-ATOM   4358  C   MET C 156       6.091  27.759  21.504  1.00 41.32           C  
-ANISOU 4358  C   MET C 156     6364   3718   5619  -1066   1326     94       C  
-ATOM   4359  O   MET C 156       7.004  27.043  21.088  1.00 39.65           O  
-ANISOU 4359  O   MET C 156     6082   3680   5302  -1206   1411     15       O  
-ATOM   4360  CB  MET C 156       5.132  29.203  19.672  1.00 44.48           C  
-ANISOU 4360  CB  MET C 156     6834   4087   5981  -1136   1133    652       C  
-ATOM   4361  CG  MET C 156       3.937  28.253  19.632  1.00 48.68           C  
-ANISOU 4361  CG  MET C 156     7264   4797   6436   -997   1082    588       C  
-ATOM   4362  SD  MET C 156       3.233  28.071  17.976  1.00 65.42           S  
-ANISOU 4362  SD  MET C 156     9382   7219   8257  -1182    900    922       S  
-ATOM   4363  CE  MET C 156       2.588  29.719  17.693  1.00 69.12           C  
-ANISOU 4363  CE  MET C 156     9863   7344   9056  -1110    636   1383       C  
-ATOM   4364  N   VAL C 157       5.225  27.357  22.437  1.00 36.17           N  
-ANISOU 4364  N   VAL C 157     5698   3015   5032   -899   1317    -54       N  
-ATOM   4365  CA  VAL C 157       5.174  25.963  22.886  1.00 35.17           C  
-ANISOU 4365  CA  VAL C 157     5492   3062   4809   -881   1350   -246       C  
-ATOM   4366  C   VAL C 157       3.747  25.454  22.896  1.00 38.13           C  
-ANISOU 4366  C   VAL C 157     5811   3523   5153   -735   1331   -262       C  
-ATOM   4367  O   VAL C 157       2.872  26.039  23.543  1.00 37.28           O  
-ANISOU 4367  O   VAL C 157     5723   3254   5187   -608   1341   -283       O  
-ATOM   4368  CB  VAL C 157       5.719  25.751  24.316  1.00 41.75           C  
-ANISOU 4368  CB  VAL C 157     6377   3775   5710   -915   1342   -422       C  
-ATOM   4369  CG1 VAL C 157       5.910  24.257  24.584  1.00 37.35           C  
-ANISOU 4369  CG1 VAL C 157     5714   3375   5104   -937   1322   -531       C  
-ATOM   4370  CG2 VAL C 157       7.020  26.471  24.521  1.00 45.40           C  
-ANISOU 4370  CG2 VAL C 157     6883   4108   6258  -1062   1315   -395       C  
-ATOM   4371  N   LYS C 158       3.516  24.341  22.212  1.00 32.49           N  
-ANISOU 4371  N   LYS C 158     5008   3048   4290   -768   1333   -289       N  
-ATOM   4372  CA  LYS C 158       2.233  23.662  22.296  1.00 30.91           C  
-ANISOU 4372  CA  LYS C 158     4731   2949   4064   -665   1306   -324       C  
-ATOM   4373  C   LYS C 158       2.482  22.219  22.737  1.00 29.14           C  
-ANISOU 4373  C   LYS C 158     4456   2832   3784   -706   1352   -517       C  
-ATOM   4374  O   LYS C 158       3.567  21.672  22.497  1.00 27.90           O  
-ANISOU 4374  O   LYS C 158     4272   2707   3623   -811   1396   -590       O  
-ATOM   4375  CB  LYS C 158       1.531  23.676  20.935  1.00 33.44           C  
-ANISOU 4375  CB  LYS C 158     4998   3453   4255   -711   1212   -137       C  
-ATOM   4376  CG  LYS C 158       1.390  25.045  20.298  1.00 39.64           C  
-ANISOU 4376  CG  LYS C 158     5823   4123   5116   -716   1096    152       C  
-ATOM   4377  CD  LYS C 158       0.132  25.745  20.731  1.00 49.31           C  
-ANISOU 4377  CD  LYS C 158     6946   5156   6635   -507   1008    262       C  
-ATOM   4378  CE  LYS C 158      -0.342  26.670  19.620  1.00 55.13           C  
-ANISOU 4378  CE  LYS C 158     7646   5861   7439   -546    779    656       C  
-ATOM   4379  NZ  LYS C 158      -0.946  27.917  20.140  1.00 61.73           N  
-ANISOU 4379  NZ  LYS C 158     8395   6312   8747   -334    735    781       N  
-ATOM   4380  N   VAL C 159       1.483  21.611  23.368  1.00 27.65           N  
-ANISOU 4380  N   VAL C 159     4226   2671   3608   -631   1349   -591       N  
-ATOM   4381  CA  VAL C 159       1.578  20.226  23.817  1.00 30.72           C  
-ANISOU 4381  CA  VAL C 159     4571   3124   3979   -681   1358   -725       C  
-ATOM   4382  C   VAL C 159       0.526  19.359  23.132  1.00 28.36           C  
-ANISOU 4382  C   VAL C 159     4172   3003   3602   -677   1347   -745       C  
-ATOM   4383  O   VAL C 159      -0.644  19.737  23.079  1.00 30.32           O  
-ANISOU 4383  O   VAL C 159     4370   3291   3860   -599   1320   -676       O  
-ATOM   4384  CB  VAL C 159       1.379  20.149  25.341  1.00 26.24           C  
-ANISOU 4384  CB  VAL C 159     4082   2443   3444   -685   1362   -792       C  
-ATOM   4385  CG1 VAL C 159       1.463  18.721  25.840  1.00 28.68           C  
-ANISOU 4385  CG1 VAL C 159     4352   2788   3756   -765   1315   -851       C  
-ATOM   4386  CG2 VAL C 159       2.407  21.030  26.054  1.00 30.10           C  
-ANISOU 4386  CG2 VAL C 159     4696   2770   3971   -749   1342   -782       C  
-ATOM   4387  N   ALA C 160       0.950  18.210  22.597  1.00 27.62           N  
-ANISOU 4387  N   ALA C 160     4022   2991   3481   -771   1374   -853       N  
-ATOM   4388  CA  ALA C 160       0.026  17.191  22.120  1.00 27.17           C  
-ANISOU 4388  CA  ALA C 160     3889   3079   3355   -815   1364   -923       C  
-ATOM   4389  C   ALA C 160       0.143  15.999  23.069  1.00 30.85           C  
-ANISOU 4389  C   ALA C 160     4324   3440   3959   -830   1367  -1029       C  
-ATOM   4390  O   ALA C 160       1.246  15.511  23.325  1.00 30.37           O  
-ANISOU 4390  O   ALA C 160     4243   3243   4053   -864   1381  -1088       O  
-ATOM   4391  CB  ALA C 160       0.366  16.772  20.677  1.00 26.78           C  
-ANISOU 4391  CB  ALA C 160     3828   3190   3159   -971   1423  -1008       C  
-ATOM   4392  N   SER C 161      -0.979  15.523  23.592  1.00 27.11           N  
-ANISOU 4392  N   SER C 161     3820   3010   3471   -820   1339  -1025       N  
-ATOM   4393  CA  SER C 161      -0.955  14.310  24.418  1.00 23.96           C  
-ANISOU 4393  CA  SER C 161     3406   2514   3184   -885   1314  -1076       C  
-ATOM   4394  C   SER C 161      -1.960  13.331  23.867  1.00 24.14           C  
-ANISOU 4394  C   SER C 161     3340   2653   3178   -949   1318  -1153       C  
-ATOM   4395  O   SER C 161      -3.112  13.706  23.618  1.00 28.51           O  
-ANISOU 4395  O   SER C 161     3842   3359   3632   -927   1310  -1109       O  
-ATOM   4396  CB  SER C 161      -1.285  14.649  25.881  1.00 27.29           C  
-ANISOU 4396  CB  SER C 161     3922   2871   3577   -896   1296   -995       C  
-ATOM   4397  OG  SER C 161      -1.221  13.501  26.705  1.00 28.64           O  
-ANISOU 4397  OG  SER C 161     4109   2953   3820  -1016   1223   -971       O  
-ATOM   4398  N   LEU C 162      -1.533  12.088  23.649  1.00 23.62           N  
-ANISOU 4398  N   LEU C 162     3227   2491   3258  -1033   1325  -1270       N  
-ATOM   4399  CA  LEU C 162      -2.438  11.077  23.147  1.00 25.44           C  
-ANISOU 4399  CA  LEU C 162     3389   2804   3475  -1134   1331  -1374       C  
-ATOM   4400  C   LEU C 162      -3.647  10.982  24.066  1.00 27.15           C  
-ANISOU 4400  C   LEU C 162     3591   3079   3646  -1148   1285  -1264       C  
-ATOM   4401  O   LEU C 162      -4.789  10.945  23.595  1.00 25.29           O  
-ANISOU 4401  O   LEU C 162     3273   3021   3315  -1186   1275  -1273       O  
-ATOM   4402  CB  LEU C 162      -1.763   9.708  23.054  1.00 27.17           C  
-ANISOU 4402  CB  LEU C 162     3542   2825   3956  -1194   1350  -1498       C  
-ATOM   4403  CG  LEU C 162      -2.711   8.577  22.644  1.00 30.78           C  
-ANISOU 4403  CG  LEU C 162     3940   3337   4417  -1310   1351  -1604       C  
-ATOM   4404  CD1 LEU C 162      -3.308   8.815  21.243  1.00 30.85           C  
-ANISOU 4404  CD1 LEU C 162     3956   3603   4162  -1439   1412  -1766       C  
-ATOM   4405  CD2 LEU C 162      -2.017   7.216  22.678  1.00 33.70           C  
-ANISOU 4405  CD2 LEU C 162     4215   3488   5100  -1275   1346  -1647       C  
-ATOM   4406  N   LEU C 163      -3.390  10.941  25.374  1.00 25.88           N  
-ANISOU 4406  N   LEU C 163     3504   2785   3546  -1158   1256  -1155       N  
-ATOM   4407  CA  LEU C 163      -4.451  10.723  26.359  1.00 26.53           C  
-ANISOU 4407  CA  LEU C 163     3594   2923   3563  -1243   1275  -1084       C  
-ATOM   4408  C   LEU C 163      -4.476  11.799  27.424  1.00 26.05           C  
-ANISOU 4408  C   LEU C 163     3644   2876   3378  -1223   1342  -1009       C  
-ATOM   4409  O   LEU C 163      -3.436  12.314  27.836  1.00 31.26           O  
-ANISOU 4409  O   LEU C 163     4422   3428   4028  -1206   1295   -960       O  
-ATOM   4410  CB  LEU C 163      -4.287   9.365  27.053  1.00 26.90           C  
-ANISOU 4410  CB  LEU C 163     3672   2803   3746  -1408   1187  -1026       C  
-ATOM   4411  CG  LEU C 163      -4.179   8.112  26.198  1.00 28.25           C  
-ANISOU 4411  CG  LEU C 163     3744   2862   4130  -1460   1150  -1143       C  
-ATOM   4412  CD1 LEU C 163      -3.952   6.881  27.083  1.00 28.19           C  
-ANISOU 4412  CD1 LEU C 163     3757   2654   4300  -1543    992   -976       C  
-ATOM   4413  CD2 LEU C 163      -5.415   7.919  25.302  1.00 28.07           C  
-ANISOU 4413  CD2 LEU C 163     3609   3052   4003  -1502   1213  -1270       C  
-ATOM   4414  N   VAL C 164      -5.679  12.140  27.873  1.00 28.18           N  
-ANISOU 4414  N   VAL C 164     3860   3272   3577  -1246   1475  -1031       N  
-ATOM   4415  CA  VAL C 164      -5.844  13.008  29.034  1.00 25.95           C  
-ANISOU 4415  CA  VAL C 164     3694   2989   3176  -1294   1625  -1043       C  
-ATOM   4416  C   VAL C 164      -6.832  12.327  29.958  1.00 27.79           C  
-ANISOU 4416  C   VAL C 164     3928   3302   3328  -1509   1750  -1054       C  
-ATOM   4417  O   VAL C 164      -7.904  11.918  29.531  1.00 30.92           O  
-ANISOU 4417  O   VAL C 164     4124   3804   3820  -1499   1811  -1093       O  
-ATOM   4418  CB  VAL C 164      -6.335  14.422  28.654  1.00 32.31           C  
-ANISOU 4418  CB  VAL C 164     4392   3829   4055  -1092   1766  -1117       C  
-ATOM   4419  CG1 VAL C 164      -6.675  15.234  29.913  1.00 32.09           C  
-ANISOU 4419  CG1 VAL C 164     4470   3774   3948  -1175   2009  -1224       C  
-ATOM   4420  CG2 VAL C 164      -5.283  15.145  27.833  1.00 35.33           C  
-ANISOU 4420  CG2 VAL C 164     4819   4133   4474   -941   1643  -1070       C  
-ATOM   4421  N   LYS C 165      -6.467  12.176  31.226  1.00 29.34           N  
-ANISOU 4421  N   LYS C 165     4356   3466   3326  -1753   1771  -1001       N  
-ATOM   4422  CA  LYS C 165      -7.347  11.510  32.174  1.00 34.33           C  
-ANISOU 4422  CA  LYS C 165     5034   4194   3815  -2026   1895   -993       C  
-ATOM   4423  C   LYS C 165      -8.278  12.495  32.865  1.00 33.48           C  
-ANISOU 4423  C   LYS C 165     4902   4165   3653  -1994   2145  -1185       C  
-ATOM   4424  O   LYS C 165      -7.866  13.608  33.195  1.00 36.79           O  
-ANISOU 4424  O   LYS C 165     5419   4520   4039  -1933   2213  -1275       O  
-ATOM   4425  CB  LYS C 165      -6.538  10.774  33.239  1.00 37.83           C  
-ANISOU 4425  CB  LYS C 165     5756   4569   4049  -2310   1668   -789       C  
-ATOM   4426  CG  LYS C 165      -6.031   9.418  32.805  1.00 39.29           C  
-ANISOU 4426  CG  LYS C 165     5885   4609   4434  -2319   1356   -580       C  
-ATOM   4427  CD  LYS C 165      -5.468   8.651  33.987  1.00 43.95           C  
-ANISOU 4427  CD  LYS C 165     6684   5144   4869  -2571   1084   -306       C  
-ATOM   4428  CE  LYS C 165      -5.237   7.204  33.630  1.00 42.67           C  
-ANISOU 4428  CE  LYS C 165     6399   4794   5020  -2552    815   -106       C  
-ATOM   4429  NZ  LYS C 165      -4.615   6.460  34.753  1.00 37.94           N  
-ANISOU 4429  NZ  LYS C 165     5955   4101   4360  -2777    498    225       N  
-ATOM   4430  N   ARG C 166      -9.532  12.099  33.064  1.00 36.47           N  
-ANISOU 4430  N   ARG C 166     3841   5674   4343   -440   2120   -755       N  
-ATOM   4431  CA  ARG C 166     -10.418  12.861  33.934  1.00 38.94           C  
-ANISOU 4431  CA  ARG C 166     4232   5998   4566   -264   2327   -835       C  
-ATOM   4432  C   ARG C 166     -10.100  12.426  35.357  1.00 47.64           C  
-ANISOU 4432  C   ARG C 166     5369   7227   5505   -430   2349   -915       C  
-ATOM   4433  O   ARG C 166     -10.265  11.257  35.697  1.00 48.59           O  
-ANISOU 4433  O   ARG C 166     5293   7561   5608   -529   2270   -827       O  
-ATOM   4434  CB  ARG C 166     -11.892  12.587  33.610  1.00 40.20           C  
-ANISOU 4434  CB  ARG C 166     4142   6348   4783    -35   2400   -693       C  
-ATOM   4435  CG  ARG C 166     -12.339  13.126  32.247  1.00 40.65           C  
-ANISOU 4435  CG  ARG C 166     4150   6314   4981    164   2404   -603       C  
-ATOM   4436  CD  ARG C 166     -13.835  12.959  32.051  1.00 43.68           C  
-ANISOU 4436  CD  ARG C 166     4263   6962   5370    391   2495   -445       C  
-ATOM   4437  NE  ARG C 166     -14.226  11.551  32.096  1.00 43.33           N  
-ANISOU 4437  NE  ARG C 166     3944   7205   5316    200   2364   -312       N  
-ATOM   4438  CZ  ARG C 166     -14.128  10.717  31.065  1.00 40.72           C  
-ANISOU 4438  CZ  ARG C 166     3494   6893   5084     58   2178   -178       C  
-ATOM   4439  NH1 ARG C 166     -13.652  11.144  29.905  1.00 39.93           N  
-ANISOU 4439  NH1 ARG C 166     3446   6620   5106     93   2124   -175       N  
-ATOM   4440  NH2 ARG C 166     -14.503   9.452  31.192  1.00 46.63           N  
-ANISOU 4440  NH2 ARG C 166     4152   7750   5814   -122   2025    -54       N  
-ATOM   4441  N   THR C 167      -9.620  13.356  36.176  1.00 43.99           N  
-ANISOU 4441  N   THR C 167     5183   6625   4906   -480   2458  -1080       N  
-ATOM   4442  CA  THR C 167      -9.247  13.036  37.557  1.00 43.45           C  
-ANISOU 4442  CA  THR C 167     5167   6677   4666   -657   2481  -1165       C  
-ATOM   4443  C   THR C 167      -9.338  14.253  38.471  1.00 46.42           C  
-ANISOU 4443  C   THR C 167     5870   6889   4877   -614   2683  -1339       C  
-ATOM   4444  O   THR C 167      -9.063  15.376  38.041  1.00 47.07           O  
-ANISOU 4444  O   THR C 167     6235   6711   4938   -574   2760  -1428       O  
-ATOM   4445  CB  THR C 167      -7.813  12.451  37.625  1.00 46.02           C  
-ANISOU 4445  CB  THR C 167     5490   7062   4933   -962   2298  -1164       C  
-ATOM   4446  OG1 THR C 167      -7.354  12.446  38.983  1.00 49.26           O  
-ANISOU 4446  OG1 THR C 167     6001   7571   5144  -1141   2341  -1266       O  
-ATOM   4447  CG2 THR C 167      -6.861  13.279  36.786  1.00 44.86           C  
-ANISOU 4447  CG2 THR C 167     5530   6707   4807  -1054   2237  -1214       C  
-ATOM   4448  N   PRO C 168      -9.725  14.034  39.739  1.00 48.46           N  
-ANISOU 4448  N   PRO C 168     6128   7283   5000   -629   2781  -1389       N  
-ATOM   4449  CA  PRO C 168      -9.773  15.139  40.707  1.00 50.75           C  
-ANISOU 4449  CA  PRO C 168     6776   7399   5106   -604   2965  -1548       C  
-ATOM   4450  C   PRO C 168      -8.379  15.643  41.073  1.00 52.00           C  
-ANISOU 4450  C   PRO C 168     7222   7436   5101   -958   2909  -1693       C  
-ATOM   4451  O   PRO C 168      -8.254  16.702  41.688  1.00 54.26           O  
-ANISOU 4451  O   PRO C 168     7882   7509   5226   -994   3031  -1825       O  
-ATOM   4452  CB  PRO C 168     -10.452  14.511  41.936  1.00 50.38           C  
-ANISOU 4452  CB  PRO C 168     6586   7562   4995   -551   2977  -1504       C  
-ATOM   4453  CG  PRO C 168     -10.297  13.040  41.764  1.00 48.90           C  
-ANISOU 4453  CG  PRO C 168     6036   7631   4912   -673   2762  -1357       C  
-ATOM   4454  CD  PRO C 168     -10.304  12.794  40.287  1.00 48.67           C  
-ANISOU 4454  CD  PRO C 168     5853   7583   5058   -615   2684  -1256       C  
-ATOM   4455  N   ARG C 169      -7.347  14.896  40.697  1.00 48.76           N  
-ANISOU 4455  N   ARG C 169     6637   7167   4721  -1212   2699  -1635       N  
-ATOM   4456  CA  ARG C 169      -5.974  15.282  41.007  1.00 53.54           C  
-ANISOU 4456  CA  ARG C 169     7441   7755   5148  -1574   2614  -1727       C  
-ATOM   4457  C   ARG C 169      -5.381  16.278  40.017  1.00 52.67           C  
-ANISOU 4457  C   ARG C 169     7576   7387   5049  -1641   2597  -1778       C  
-ATOM   4458  O   ARG C 169      -4.312  16.831  40.267  1.00 56.51           O  
-ANISOU 4458  O   ARG C 169     8284   7842   5344  -1966   2554  -1868       O  
-ATOM   4459  CB  ARG C 169      -5.072  14.053  41.071  1.00 51.67           C  
-ANISOU 4459  CB  ARG C 169     6899   7822   4912  -1778   2392  -1600       C  
-ATOM   4460  CG  ARG C 169      -5.418  13.084  42.180  1.00 54.71           C  
-ANISOU 4460  CG  ARG C 169     7090   8415   5281  -1747   2334  -1529       C  
-ATOM   4461  CD  ARG C 169      -4.264  12.134  42.410  1.00 56.59           C  
-ANISOU 4461  CD  ARG C 169     7144   8892   5465  -1948   2110  -1413       C  
-ATOM   4462  NE  ARG C 169      -3.904  11.410  41.193  1.00 54.94           N  
-ANISOU 4462  NE  ARG C 169     6742   8730   5402  -1881   1969  -1257       N  
-ATOM   4463  CZ  ARG C 169      -2.831  10.634  41.073  1.00 53.67           C  
-ANISOU 4463  CZ  ARG C 169     6445   8740   5206  -1977   1774  -1123       C  
-ATOM   4464  NH1 ARG C 169      -2.007  10.473  42.099  1.00 52.47           N  
-ANISOU 4464  NH1 ARG C 169     6291   8762   4882  -2152   1691  -1122       N  
-ATOM   4465  NH2 ARG C 169      -2.580  10.019  39.926  1.00 49.21           N  
-ANISOU 4465  NH2 ARG C 169     5753   8172   4772  -1875   1664   -978       N  
-ATOM   4466  N   SER C 170      -6.071  16.486  38.896  1.00 52.59           N  
-ANISOU 4466  N   SER C 170     7517   7221   5245  -1353   2626  -1710       N  
-ATOM   4467  CA  SER C 170      -5.633  17.422  37.856  1.00 56.05           C  
-ANISOU 4467  CA  SER C 170     8184   7394   5718  -1370   2621  -1748       C  
-ATOM   4468  C   SER C 170      -5.359  18.813  38.419  1.00 61.75           C  
-ANISOU 4468  C   SER C 170     9435   7834   6195  -1507   2798  -1945       C  
-ATOM   4469  O   SER C 170      -6.178  19.361  39.161  1.00 63.06           O  
-ANISOU 4469  O   SER C 170     9832   7870   6259  -1330   3019  -2030       O  
-ATOM   4470  CB  SER C 170      -6.679  17.501  36.738  1.00 58.09           C  
-ANISOU 4470  CB  SER C 170     8322   7536   6214   -981   2676  -1647       C  
-ATOM   4471  OG  SER C 170      -6.557  18.698  35.997  1.00 63.60           O  
-ANISOU 4471  OG  SER C 170     9352   7910   6901   -918   2766  -1721       O  
-ATOM   4472  N   VAL C 171      -4.198  19.375  38.088  1.00 64.91           N  
-ANISOU 4472  N   VAL C 171    10047   8145   6472  -1837   2706  -2008       N  
-ATOM   4473  CA  VAL C 171      -3.859  20.714  38.571  1.00 71.45           C  
-ANISOU 4473  CA  VAL C 171    11411   8677   7059  -2026   2833  -2165       C  
-ATOM   4474  C   VAL C 171      -4.536  21.782  37.716  1.00 72.52           C  
-ANISOU 4474  C   VAL C 171    11846   8418   7290  -1711   2982  -2176       C  
-ATOM   4475  O   VAL C 171      -4.488  22.972  38.031  1.00 75.58           O  
-ANISOU 4475  O   VAL C 171    12679   8502   7536  -1758   3081  -2235       O  
-ATOM   4476  CB  VAL C 171      -2.326  20.962  38.654  1.00 70.51           C  
-ANISOU 4476  CB  VAL C 171    11391   8653   6745  -2553   2651  -2190       C  
-ATOM   4477  CG1 VAL C 171      -1.738  20.304  39.900  1.00 70.95           C  
-ANISOU 4477  CG1 VAL C 171    11275   9045   6639  -2850   2548  -2174       C  
-ATOM   4478  CG2 VAL C 171      -1.621  20.489  37.397  1.00 67.66           C  
-ANISOU 4478  CG2 VAL C 171    10782   8427   6499  -2631   2476  -2107       C  
-ATOM   4479  N   GLY C 172      -5.181  21.344  36.640  1.00 69.40           N  
-ANISOU 4479  N   GLY C 172    11197   8043   7130  -1383   2999  -2092       N  
-ATOM   4480  CA  GLY C 172      -5.924  22.249  35.787  1.00 69.22           C  
-ANISOU 4480  CA  GLY C 172    11379   7704   7219  -1020   3128  -2057       C  
-ATOM   4481  C   GLY C 172      -5.192  22.546  34.499  1.00 67.22           C  
-ANISOU 4481  C   GLY C 172    11174   7320   7048  -1138   3018  -2050       C  
-ATOM   4482  O   GLY C 172      -5.573  23.447  33.752  1.00 67.34           O  
-ANISOU 4482  O   GLY C 172    11409   7051   7126   -905   3097  -2018       O  
-ATOM   4483  N   TYR C 173      -4.130  21.794  34.235  1.00 64.61           N  
-ANISOU 4483  N   TYR C 173    10572   7231   6747  -1475   2770  -2006       N  
-ATOM   4484  CA  TYR C 173      -3.418  21.953  32.977  1.00 63.34           C  
-ANISOU 4484  CA  TYR C 173    10373   6997   6697  -1573   2616  -1952       C  
-ATOM   4485  C   TYR C 173      -4.135  21.217  31.837  1.00 57.67           C  
-ANISOU 4485  C   TYR C 173     9238   6359   6315  -1208   2532  -1771       C  
-ATOM   4486  O   TYR C 173      -4.533  20.068  32.007  1.00 60.37           O  
-ANISOU 4486  O   TYR C 173     9167   6980   6789  -1104   2441  -1649       O  
-ATOM   4487  CB  TYR C 173      -1.973  21.453  33.073  1.00 61.09           C  
-ANISOU 4487  CB  TYR C 173     9931   6979   6301  -2042   2372  -1924       C  
-ATOM   4488  CG  TYR C 173      -1.356  21.477  31.710  1.00 58.32           C  
-ANISOU 4488  CG  TYR C 173     9472   6591   6097  -2077   2211  -1836       C  
-ATOM   4489  CD1 TYR C 173      -0.939  22.677  31.152  1.00 59.00           C  
-ANISOU 4489  CD1 TYR C 173     9977   6368   6073  -2213   2274  -1941       C  
-ATOM   4490  CD2 TYR C 173      -1.262  20.317  30.944  1.00 56.27           C  
-ANISOU 4490  CD2 TYR C 173     8729   6571   6078  -1954   2016  -1647       C  
-ATOM   4491  CE1 TYR C 173      -0.418  22.723  29.889  1.00 56.50           C  
-ANISOU 4491  CE1 TYR C 173     9562   6011   5895  -2231   2133  -1860       C  
-ATOM   4492  CE2 TYR C 173      -0.739  20.352  29.667  1.00 53.81           C  
-ANISOU 4492  CE2 TYR C 173     8333   6209   5902  -1961   1882  -1563       C  
-ATOM   4493  CZ  TYR C 173      -0.318  21.562  29.153  1.00 54.21           C  
-ANISOU 4493  CZ  TYR C 173     8766   5977   5853  -2099   1936  -1670       C  
-ATOM   4494  OH  TYR C 173       0.201  21.625  27.893  1.00 49.23           O  
-ANISOU 4494  OH  TYR C 173     8055   5296   5354  -2109   1804  -1589       O  
-ATOM   4495  N   LYS C 174      -4.275  21.864  30.677  1.00 52.27           N  
-ANISOU 4495  N   LYS C 174     8680   5432   5748  -1041   2561  -1753       N  
-ATOM   4496  CA  LYS C 174      -4.873  21.213  29.505  1.00 49.39           C  
-ANISOU 4496  CA  LYS C 174     7935   5148   5682   -744   2467  -1579       C  
-ATOM   4497  C   LYS C 174      -4.037  21.382  28.236  1.00 44.55           C  
-ANISOU 4497  C   LYS C 174     7311   4440   5174   -869   2304  -1535       C  
-ATOM   4498  O   LYS C 174      -3.676  22.499  27.875  1.00 45.63           O  
-ANISOU 4498  O   LYS C 174     7838   4287   5214   -937   2387  -1639       O  
-ATOM   4499  CB  LYS C 174      -6.304  21.703  29.263  1.00 56.81           C  
-ANISOU 4499  CB  LYS C 174     8931   5948   6705   -269   2693  -1543       C  
-ATOM   4500  CG  LYS C 174      -7.334  21.048  30.175  1.00 64.48           C  
-ANISOU 4500  CG  LYS C 174     9673   7154   7673    -69   2786  -1487       C  
-ATOM   4501  CD  LYS C 174      -8.670  20.831  29.466  1.00 67.89           C  
-ANISOU 4501  CD  LYS C 174     9829   7679   8286    370   2863  -1323       C  
-ATOM   4502  CE  LYS C 174      -9.668  20.089  30.360  1.00 71.71           C  
-ANISOU 4502  CE  LYS C 174    10040   8457   8750    523   2932  -1247       C  
-ATOM   4503  NZ  LYS C 174     -10.975  19.832  29.683  1.00 72.78           N  
-ANISOU 4503  NZ  LYS C 174     9860   8770   9024    905   2993  -1059       N  
-ATOM   4504  N   PRO C 175      -3.738  20.264  27.549  1.00 40.72           N  
-ANISOU 4504  N   PRO C 175     6408   4189   4874   -895   2084  -1377       N  
-ATOM   4505  CA  PRO C 175      -2.897  20.310  26.345  1.00 40.61           C  
-ANISOU 4505  CA  PRO C 175     6350   4120   4961  -1008   1918  -1317       C  
-ATOM   4506  C   PRO C 175      -3.601  21.000  25.175  1.00 40.08           C  
-ANISOU 4506  C   PRO C 175     6378   3790   5061   -703   2004  -1291       C  
-ATOM   4507  O   PRO C 175      -4.827  21.107  25.172  1.00 38.92           O  
-ANISOU 4507  O   PRO C 175     6192   3602   4994   -360   2157  -1257       O  
-ATOM   4508  CB  PRO C 175      -2.670  18.827  26.003  1.00 37.75           C  
-ANISOU 4508  CB  PRO C 175     5535   4064   4744  -1023   1709  -1137       C  
-ATOM   4509  CG  PRO C 175      -3.172  18.036  27.168  1.00 39.34           C  
-ANISOU 4509  CG  PRO C 175     5580   4489   4878  -1005   1751  -1124       C  
-ATOM   4510  CD  PRO C 175      -4.189  18.898  27.864  1.00 40.07           C  
-ANISOU 4510  CD  PRO C 175     5913   4417   4896   -818   1993  -1244       C  
-ATOM   4511  N   ASP C 176      -2.830  21.456  24.193  1.00 37.57           N  
-ANISOU 4511  N   ASP C 176     6164   3330   4782   -820   1909  -1291       N  
-ATOM   4512  CA  ASP C 176      -3.404  22.088  23.016  1.00 40.41           C  
-ANISOU 4512  CA  ASP C 176     6605   3448   5300   -539   1978  -1256       C  
-ATOM   4513  C   ASP C 176      -4.056  21.062  22.098  1.00 37.82           C  
-ANISOU 4513  C   ASP C 176     5838   3293   5240   -303   1861  -1064       C  
-ATOM   4514  O   ASP C 176      -5.110  21.317  21.522  1.00 40.31           O  
-ANISOU 4514  O   ASP C 176     6108   3531   5678     33   1970  -1001       O  
-ATOM   4515  CB  ASP C 176      -2.325  22.871  22.270  1.00 38.73           C  
-ANISOU 4515  CB  ASP C 176     6647   3036   5031   -774   1903  -1318       C  
-ATOM   4516  CG  ASP C 176      -1.604  23.837  23.175  1.00 44.83           C  
-ANISOU 4516  CG  ASP C 176     7878   3662   5493  -1100   2001  -1505       C  
-ATOM   4517  OD1 ASP C 176      -2.113  24.956  23.368  1.00 45.71           O  
-ANISOU 4517  OD1 ASP C 176     8320   3560   5488   -944   2165  -1540       O  
-ATOM   4518  OD2 ASP C 176      -0.553  23.461  23.727  1.00 40.34           O  
-ANISOU 4518  OD2 ASP C 176     7244   3312   4772  -1484   1857  -1518       O  
-ATOM   4519  N   PHE C 177      -3.426  19.898  21.975  1.00 32.62           N  
-ANISOU 4519  N   PHE C 177     4873   2881   4640   -481   1650   -958       N  
-ATOM   4520  CA  PHE C 177      -3.945  18.834  21.134  1.00 30.31           C  
-ANISOU 4520  CA  PHE C 177     4220   2739   4558   -324   1534   -778       C  
-ATOM   4521  C   PHE C 177      -4.107  17.577  21.977  1.00 35.65           C  
-ANISOU 4521  C   PHE C 177     4646   3706   5194   -394   1475   -706       C  
-ATOM   4522  O   PHE C 177      -3.170  17.150  22.660  1.00 33.65           O  
-ANISOU 4522  O   PHE C 177     4389   3588   4808   -637   1392   -727       O  
-ATOM   4523  CB  PHE C 177      -3.001  18.572  19.959  1.00 28.27           C  
-ANISOU 4523  CB  PHE C 177     3886   2452   4405   -440   1344   -694       C  
-ATOM   4524  CG  PHE C 177      -2.572  19.832  19.245  1.00 34.80           C  
-ANISOU 4524  CG  PHE C 177     4997   2996   5228   -453   1385   -783       C  
-ATOM   4525  CD1 PHE C 177      -3.430  20.469  18.357  1.00 37.28           C  
-ANISOU 4525  CD1 PHE C 177     5368   3115   5681   -170   1483   -763       C  
-ATOM   4526  CD2 PHE C 177      -1.325  20.398  19.491  1.00 35.05           C  
-ANISOU 4526  CD2 PHE C 177     5247   2979   5090   -761   1334   -879       C  
-ATOM   4527  CE1 PHE C 177      -3.042  21.646  17.708  1.00 38.55           C  
-ANISOU 4527  CE1 PHE C 177     5831   2989   5825   -173   1536   -847       C  
-ATOM   4528  CE2 PHE C 177      -0.928  21.564  18.845  1.00 33.23           C  
-ANISOU 4528  CE2 PHE C 177     5316   2478   4831   -811   1375   -966       C  
-ATOM   4529  CZ  PHE C 177      -1.790  22.188  17.955  1.00 35.92           C  
-ANISOU 4529  CZ  PHE C 177     5745   2579   5323   -506   1482   -956       C  
-ATOM   4530  N   VAL C 178      -5.301  16.996  21.937  1.00 29.26           N  
-ANISOU 4530  N   VAL C 178     3627   3015   4477   -187   1523   -611       N  
-ATOM   4531  CA  VAL C 178      -5.602  15.828  22.755  1.00 28.71           C  
-ANISOU 4531  CA  VAL C 178     3351   3203   4354   -249   1489   -547       C  
-ATOM   4532  C   VAL C 178      -6.220  14.731  21.905  1.00 29.72           C  
-ANISOU 4532  C   VAL C 178     3208   3464   4621   -176   1387   -366       C  
-ATOM   4533  O   VAL C 178      -7.215  14.970  21.220  1.00 28.21           O  
-ANISOU 4533  O   VAL C 178     2926   3259   4534     22   1442   -299       O  
-ATOM   4534  CB  VAL C 178      -6.606  16.169  23.862  1.00 33.24           C  
-ANISOU 4534  CB  VAL C 178     3960   3839   4829   -116   1678   -617       C  
-ATOM   4535  CG1 VAL C 178      -6.981  14.916  24.645  1.00 32.35           C  
-ANISOU 4535  CG1 VAL C 178     3625   4000   4667   -187   1638   -541       C  
-ATOM   4536  CG2 VAL C 178      -6.045  17.228  24.802  1.00 38.92           C  
-ANISOU 4536  CG2 VAL C 178     5007   4409   5372   -215   1798   -804       C  
-ATOM   4537  N   GLY C 179      -5.656  13.531  21.965  1.00 27.62           N  
-ANISOU 4537  N   GLY C 179     2830   3336   4327   -335   1252   -276       N  
-ATOM   4538  CA  GLY C 179      -6.250  12.408  21.261  1.00 27.27           C  
-ANISOU 4538  CA  GLY C 179     2598   3401   4364   -313   1170   -110       C  
-ATOM   4539  C   GLY C 179      -7.556  11.957  21.879  1.00 25.84           C  
-ANISOU 4539  C   GLY C 179     2266   3411   4140   -248   1259    -67       C  
-ATOM   4540  O   GLY C 179      -8.618  12.064  21.266  1.00 28.11           O  
-ANISOU 4540  O   GLY C 179     2425   3751   4503   -118   1296     13       O  
-ATOM   4541  N   PHE C 180      -7.481  11.459  23.115  1.00 25.11           N  
-ANISOU 4541  N   PHE C 180     3554   2353   3634   -937   1144   -443       N  
-ATOM   4542  CA  PHE C 180      -8.625  10.872  23.790  1.00 26.83           C  
-ANISOU 4542  CA  PHE C 180     3789   2547   3857   -881   1246   -555       C  
-ATOM   4543  C   PHE C 180      -8.694  11.340  25.235  1.00 30.27           C  
-ANISOU 4543  C   PHE C 180     4375   2893   4234   -923   1341   -707       C  
-ATOM   4544  O   PHE C 180      -7.668  11.479  25.896  1.00 28.88           O  
-ANISOU 4544  O   PHE C 180     4304   2734   3935  -1021   1271   -760       O  
-ATOM   4545  CB  PHE C 180      -8.525   9.343  23.763  1.00 28.62           C  
-ANISOU 4545  CB  PHE C 180     3969   2925   3981   -871   1204   -536       C  
-ATOM   4546  CG  PHE C 180      -8.454   8.768  22.374  1.00 27.04           C  
-ANISOU 4546  CG  PHE C 180     3663   2823   3787   -779   1079   -454       C  
-ATOM   4547  CD1 PHE C 180      -7.262   8.762  21.662  1.00 22.86           C  
-ANISOU 4547  CD1 PHE C 180     3126   2424   3137   -769    998   -364       C  
-ATOM   4548  CD2 PHE C 180      -9.582   8.229  21.782  1.00 27.42           C  
-ANISOU 4548  CD2 PHE C 180     3613   2844   3960   -681   1034   -469       C  
-ATOM   4549  CE1 PHE C 180      -7.214   8.234  20.371  1.00 21.54           C  
-ANISOU 4549  CE1 PHE C 180     2893   2387   2905   -619    897   -313       C  
-ATOM   4550  CE2 PHE C 180      -9.543   7.704  20.503  1.00 24.87           C  
-ANISOU 4550  CE2 PHE C 180     3232   2616   3600   -559    874   -448       C  
-ATOM   4551  CZ  PHE C 180      -8.361   7.704  19.797  1.00 24.48           C  
-ANISOU 4551  CZ  PHE C 180     3215   2725   3361   -506    816   -382       C  
-ATOM   4552  N   GLU C 181      -9.907  11.596  25.721  1.00 29.88           N  
-ANISOU 4552  N   GLU C 181     4329   2762   4262   -825   1494   -779       N  
-ATOM   4553  CA  GLU C 181     -10.099  11.947  27.122  1.00 30.56           C  
-ANISOU 4553  CA  GLU C 181     4578   2812   4221   -791   1621   -939       C  
-ATOM   4554  C   GLU C 181     -10.714  10.717  27.769  1.00 33.95           C  
-ANISOU 4554  C   GLU C 181     4955   3392   4551   -745   1765   -878       C  
-ATOM   4555  O   GLU C 181     -11.769  10.234  27.331  1.00 36.30           O  
-ANISOU 4555  O   GLU C 181     5076   3690   5027   -680   1851   -773       O  
-ATOM   4556  CB  GLU C 181     -11.032  13.152  27.284  1.00 30.58           C  
-ANISOU 4556  CB  GLU C 181     4615   2627   4376   -663   1739  -1046       C  
-ATOM   4557  CG  GLU C 181     -11.150  13.625  28.732  1.00 32.77           C  
-ANISOU 4557  CG  GLU C 181     5110   2878   4462   -568   1861  -1266       C  
-ATOM   4558  CD  GLU C 181     -12.367  14.489  28.971  1.00 39.19           C  
-ANISOU 4558  CD  GLU C 181     5925   3553   5413   -365   2054  -1363       C  
-ATOM   4559  OE1 GLU C 181     -13.472  13.927  29.092  1.00 40.24           O  
-ANISOU 4559  OE1 GLU C 181     5910   3786   5592   -244   2272  -1257       O  
-ATOM   4560  OE2 GLU C 181     -12.218  15.722  29.032  1.00 46.77           O  
-ANISOU 4560  OE2 GLU C 181     7011   4286   6473   -324   1981  -1530       O  
-ATOM   4561  N   ILE C 182     -10.042  10.189  28.788  1.00 31.50           N  
-ANISOU 4561  N   ILE C 182     4777   3201   3989   -785   1770   -914       N  
-ATOM   4562  CA  ILE C 182     -10.369   8.870  29.319  1.00 31.73           C  
-ANISOU 4562  CA  ILE C 182     4738   3377   3942   -773   1875   -779       C  
-ATOM   4563  C   ILE C 182     -10.666   8.948  30.810  1.00 32.28           C  
-ANISOU 4563  C   ILE C 182     4964   3548   3753   -663   2079   -835       C  
-ATOM   4564  O   ILE C 182     -10.301   9.929  31.467  1.00 36.02           O  
-ANISOU 4564  O   ILE C 182     5653   3990   4044   -612   2063  -1042       O  
-ATOM   4565  CB  ILE C 182      -9.216   7.851  29.067  1.00 32.59           C  
-ANISOU 4565  CB  ILE C 182     4833   3585   3964   -895   1685   -693       C  
-ATOM   4566  CG1 ILE C 182      -7.940   8.279  29.806  1.00 34.42           C  
-ANISOU 4566  CG1 ILE C 182     5264   3872   3944   -963   1561   -806       C  
-ATOM   4567  CG2 ILE C 182      -8.951   7.678  27.563  1.00 33.28           C  
-ANISOU 4567  CG2 ILE C 182     4777   3624   4245   -938   1512   -638       C  
-ATOM   4568  CD1 ILE C 182      -6.845   7.196  29.838  1.00 32.03           C  
-ANISOU 4568  CD1 ILE C 182     4940   3693   3536  -1051   1412   -700       C  
-ATOM   4569  N   PRO C 183     -11.357   7.927  31.349  1.00 36.46           N  
-ANISOU 4569  N   PRO C 183     5385   4195   4274   -609   2268   -645       N  
-ATOM   4570  CA  PRO C 183     -11.547   7.849  32.805  1.00 37.91           C  
-ANISOU 4570  CA  PRO C 183     5721   4548   4133   -472   2490   -636       C  
-ATOM   4571  C   PRO C 183     -10.226   7.529  33.513  1.00 38.81           C  
-ANISOU 4571  C   PRO C 183     6048   4791   3905   -541   2317   -692       C  
-ATOM   4572  O   PRO C 183      -9.231   7.198  32.859  1.00 37.66           O  
-ANISOU 4572  O   PRO C 183     5874   4603   3830   -703   2056   -688       O  
-ATOM   4573  CB  PRO C 183     -12.562   6.703  32.980  1.00 42.86           C  
-ANISOU 4573  CB  PRO C 183     6085   5248   4952   -427   2652   -308       C  
-ATOM   4574  CG  PRO C 183     -12.483   5.907  31.730  1.00 39.04           C  
-ANISOU 4574  CG  PRO C 183     5390   4631   4813   -603   2497   -202       C  
-ATOM   4575  CD  PRO C 183     -12.106   6.879  30.630  1.00 33.80           C  
-ANISOU 4575  CD  PRO C 183     4767   3821   4254   -652   2285   -418       C  
-ATOM   4576  N   ASP C 184     -10.199   7.636  34.834  1.00 42.64           N  
-ANISOU 4576  N   ASP C 184     6708   5451   4041   -384   2394   -722       N  
-ATOM   4577  CA  ASP C 184      -8.976   7.300  35.550  1.00 49.44           C  
-ANISOU 4577  CA  ASP C 184     7762   6450   4572   -436   2207   -764       C  
-ATOM   4578  C   ASP C 184      -8.887   5.799  35.782  1.00 47.65           C  
-ANISOU 4578  C   ASP C 184     7394   6364   4347   -482   2256   -426       C  
-ATOM   4579  O   ASP C 184      -9.055   5.332  36.908  1.00 45.24           O  
-ANISOU 4579  O   ASP C 184     7132   6275   3784   -334   2359   -276       O  
-ATOM   4580  CB  ASP C 184      -8.855   8.054  36.880  1.00 54.93           C  
-ANISOU 4580  CB  ASP C 184     8714   7292   4864   -223   2184   -965       C  
-ATOM   4581  CG  ASP C 184      -7.443   7.982  37.460  1.00 53.54           C  
-ANISOU 4581  CG  ASP C 184     8749   7206   4387   -302   1887  -1087       C  
-ATOM   4582  OD1 ASP C 184      -6.545   7.443  36.776  1.00 56.41           O  
-ANISOU 4582  OD1 ASP C 184     9054   7509   4871   -533   1715  -1017       O  
-ATOM   4583  OD2 ASP C 184      -7.223   8.471  38.583  1.00 51.79           O  
-ANISOU 4583  OD2 ASP C 184     8735   7130   3814   -124   1805  -1262       O  
-ATOM   4584  N   LYS C 185      -8.646   5.062  34.698  1.00 46.14           N  
-ANISOU 4584  N   LYS C 185     7020   6048   4464   -665   2165   -304       N  
-ATOM   4585  CA  LYS C 185      -8.315   3.638  34.748  1.00 45.99           C  
-ANISOU 4585  CA  LYS C 185     6875   6082   4515   -738   2118    -23       C  
-ATOM   4586  C   LYS C 185      -6.865   3.499  34.320  1.00 38.61           C  
-ANISOU 4586  C   LYS C 185     5996   5130   3544   -870   1787   -119       C  
-ATOM   4587  O   LYS C 185      -6.362   4.329  33.556  1.00 35.87           O  
-ANISOU 4587  O   LYS C 185     5669   4679   3283   -941   1617   -326       O  
-ATOM   4588  CB  LYS C 185      -9.164   2.852  33.759  1.00 46.76           C  
-ANISOU 4588  CB  LYS C 185     6675   6012   5080   -800   2161    162       C  
-ATOM   4589  CG  LYS C 185     -10.630   2.704  34.129  1.00 54.25           C  
-ANISOU 4589  CG  LYS C 185     7439   6970   6204   -676   2404    355       C  
-ATOM   4590  CD  LYS C 185     -11.357   2.027  32.973  1.00 55.62           C  
-ANISOU 4590  CD  LYS C 185     7320   6926   6888   -772   2332    470       C  
-ATOM   4591  CE  LYS C 185     -12.861   2.059  33.146  1.00 59.97           C  
-ANISOU 4591  CE  LYS C 185     7645   7458   7682   -672   2511    633       C  
-ATOM   4592  NZ  LYS C 185     -13.352   0.820  33.799  1.00 63.54           N  
-ANISOU 4592  NZ  LYS C 185     7911   7953   8277   -674   2565    984       N  
-ATOM   4593  N   PHE C 186      -6.191   2.452  34.790  1.00 39.62           N  
-ANISOU 4593  N   PHE C 186     6122   5358   3574   -894   1705     69       N  
-ATOM   4594  CA  PHE C 186      -4.801   2.243  34.401  1.00 38.84           C  
-ANISOU 4594  CA  PHE C 186     6034   5258   3465   -997   1407     12       C  
-ATOM   4595  C   PHE C 186      -4.725   1.560  33.047  1.00 35.58           C  
-ANISOU 4595  C   PHE C 186     5404   4682   3432  -1066   1303     68       C  
-ATOM   4596  O   PHE C 186      -5.126   0.406  32.901  1.00 39.09           O  
-ANISOU 4596  O   PHE C 186     5713   5062   4078  -1056   1342    269       O  
-ATOM   4597  CB  PHE C 186      -4.025   1.442  35.453  1.00 42.71           C  
-ANISOU 4597  CB  PHE C 186     6615   5925   3688   -970   1332    183       C  
-ATOM   4598  CG  PHE C 186      -2.542   1.585  35.309  1.00 42.63           C  
-ANISOU 4598  CG  PHE C 186     6642   5952   3604  -1054   1022     82       C  
-ATOM   4599  CD1 PHE C 186      -1.856   0.868  34.338  1.00 43.15           C  
-ANISOU 4599  CD1 PHE C 186     6528   5929   3939  -1119    872    158       C  
-ATOM   4600  CD2 PHE C 186      -1.841   2.479  36.101  1.00 45.98           C  
-ANISOU 4600  CD2 PHE C 186     7268   6491   3713  -1054    866   -105       C  
-ATOM   4601  CE1 PHE C 186      -0.490   1.022  34.172  1.00 44.47           C  
-ANISOU 4601  CE1 PHE C 186     6677   6147   4073  -1183    619    104       C  
-ATOM   4602  CE2 PHE C 186      -0.474   2.639  35.945  1.00 49.50           C  
-ANISOU 4602  CE2 PHE C 186     7690   6953   4164  -1154    560   -169       C  
-ATOM   4603  CZ  PHE C 186       0.205   1.906  34.980  1.00 43.62           C  
-ANISOU 4603  CZ  PHE C 186     6726   6145   3702  -1218    459    -38       C  
-ATOM   4604  N   VAL C 187      -4.209   2.274  32.054  1.00 29.79           N  
-ANISOU 4604  N   VAL C 187     4641   3876   2801  -1120   1160   -106       N  
-ATOM   4605  CA  VAL C 187      -4.173   1.755  30.694  1.00 25.65           C  
-ANISOU 4605  CA  VAL C 187     3945   3238   2562  -1126   1070    -94       C  
-ATOM   4606  C   VAL C 187      -2.727   1.531  30.249  1.00 29.34           C  
-ANISOU 4606  C   VAL C 187     4382   3769   2996  -1152    863    -98       C  
-ATOM   4607  O   VAL C 187      -1.801   2.191  30.731  1.00 32.22           O  
-ANISOU 4607  O   VAL C 187     4826   4226   3190  -1207    766   -150       O  
-ATOM   4608  CB  VAL C 187      -4.908   2.695  29.727  1.00 29.56           C  
-ANISOU 4608  CB  VAL C 187     4392   3627   3212  -1116   1119   -228       C  
-ATOM   4609  CG1 VAL C 187      -6.381   2.818  30.147  1.00 30.59           C  
-ANISOU 4609  CG1 VAL C 187     4502   3696   3425  -1071   1335   -192       C  
-ATOM   4610  CG2 VAL C 187      -4.245   4.065  29.733  1.00 32.83           C  
-ANISOU 4610  CG2 VAL C 187     4905   4066   3504  -1166   1057   -374       C  
-ATOM   4611  N   VAL C 188      -2.538   0.574  29.347  1.00 25.02           N  
-ANISOU 4611  N   VAL C 188     3710   3167   2631  -1096    783    -48       N  
-ATOM   4612  CA  VAL C 188      -1.205   0.206  28.873  1.00 25.14           C  
-ANISOU 4612  CA  VAL C 188     3664   3261   2629  -1067    626    -24       C  
-ATOM   4613  C   VAL C 188      -1.295  -0.037  27.390  1.00 26.30           C  
-ANISOU 4613  C   VAL C 188     3705   3351   2936   -958    585    -94       C  
-ATOM   4614  O   VAL C 188      -2.399  -0.143  26.841  1.00 24.84           O  
-ANISOU 4614  O   VAL C 188     3499   3045   2894   -920    628   -155       O  
-ATOM   4615  CB  VAL C 188      -0.695  -1.093  29.560  1.00 24.23           C  
-ANISOU 4615  CB  VAL C 188     3535   3164   2506  -1033    555    131       C  
-ATOM   4616  CG1 VAL C 188      -0.502  -0.870  31.042  1.00 25.77           C  
-ANISOU 4616  CG1 VAL C 188     3856   3472   2465  -1103    576    215       C  
-ATOM   4617  CG2 VAL C 188      -1.669  -2.252  29.321  1.00 24.55           C  
-ANISOU 4617  CG2 VAL C 188     3516   3026   2785   -973    585    197       C  
-ATOM   4618  N   GLY C 189      -0.144  -0.151  26.734  1.00 24.31           N  
-ANISOU 4618  N   GLY C 189     3378   3203   2655   -885    496    -79       N  
-ATOM   4619  CA  GLY C 189      -0.150  -0.436  25.316  1.00 24.27           C  
-ANISOU 4619  CA  GLY C 189     3300   3198   2723   -716    465   -151       C  
-ATOM   4620  C   GLY C 189       0.136   0.822  24.519  1.00 23.50           C  
-ANISOU 4620  C   GLY C 189     3159   3207   2562   -716    519   -159       C  
-ATOM   4621  O   GLY C 189       0.107   1.925  25.073  1.00 26.96           O  
-ANISOU 4621  O   GLY C 189     3630   3644   2970   -872    566   -139       O  
-ATOM   4622  N   TYR C 190       0.385   0.656  23.224  1.00 24.76           N  
-ANISOU 4622  N   TYR C 190     3254   3451   2702   -522    509   -184       N  
-ATOM   4623  CA  TYR C 190       0.814   1.755  22.345  1.00 24.63           C  
-ANISOU 4623  CA  TYR C 190     3161   3575   2624   -485    582   -106       C  
-ATOM   4624  C   TYR C 190       1.939   2.572  23.009  1.00 26.89           C  
-ANISOU 4624  C   TYR C 190     3359   3945   2913   -655    595     56       C  
-ATOM   4625  O   TYR C 190       1.906   3.805  23.037  1.00 28.29           O  
-ANISOU 4625  O   TYR C 190     3515   4096   3140   -790    633    114       O  
-ATOM   4626  CB  TYR C 190      -0.382   2.632  21.961  1.00 21.91           C  
-ANISOU 4626  CB  TYR C 190     2873   3131   2322   -527    632   -173       C  
-ATOM   4627  CG  TYR C 190      -0.130   3.548  20.773  1.00 24.45           C  
-ANISOU 4627  CG  TYR C 190     3116   3589   2584   -420    702    -69       C  
-ATOM   4628  CD1 TYR C 190      -0.014   3.045  19.487  1.00 24.06           C  
-ANISOU 4628  CD1 TYR C 190     3043   3695   2406   -137    694    -86       C  
-ATOM   4629  CD2 TYR C 190      -0.042   4.932  20.950  1.00 21.98           C  
-ANISOU 4629  CD2 TYR C 190     2765   3243   2343   -584    767     50       C  
-ATOM   4630  CE1 TYR C 190       0.213   3.906  18.384  1.00 27.25           C  
-ANISOU 4630  CE1 TYR C 190     3373   4270   2710     -7    788     68       C  
-ATOM   4631  CE2 TYR C 190       0.166   5.783  19.890  1.00 22.98           C  
-ANISOU 4631  CE2 TYR C 190     2800   3480   2451   -494    843    212       C  
-ATOM   4632  CZ  TYR C 190       0.298   5.280  18.608  1.00 23.92           C  
-ANISOU 4632  CZ  TYR C 190     2883   3803   2401   -203    872    248       C  
-ATOM   4633  OH  TYR C 190       0.510   6.156  17.563  1.00 25.38           O  
-ANISOU 4633  OH  TYR C 190     2974   4139   2531    -90    975    466       O  
-ATOM   4634  N   ALA C 191       2.931   1.843  23.522  1.00 27.52           N  
-ANISOU 4634  N   ALA C 191     3377   4101   2979   -643    531    126       N  
-ATOM   4635  CA  ALA C 191       4.111   2.373  24.216  1.00 28.10           C  
-ANISOU 4635  CA  ALA C 191     3336   4252   3087   -798    473    277       C  
-ATOM   4636  C   ALA C 191       3.890   2.765  25.682  1.00 26.96           C  
-ANISOU 4636  C   ALA C 191     3320   3987   2935  -1034    376    213       C  
-ATOM   4637  O   ALA C 191       4.849   3.065  26.387  1.00 30.00           O  
-ANISOU 4637  O   ALA C 191     3635   4419   3342  -1160    257    297       O  
-ATOM   4638  CB  ALA C 191       4.793   3.512  23.430  1.00 25.76           C  
-ANISOU 4638  CB  ALA C 191     2860   4062   2867   -823    538    456       C  
-ATOM   4639  N   LEU C 192       2.641   2.762  26.143  1.00 25.23           N  
-ANISOU 4639  N   LEU C 192     3280   3629   2678  -1072    419     68       N  
-ATOM   4640  CA  LEU C 192       2.381   2.998  27.562  1.00 25.67           C  
-ANISOU 4640  CA  LEU C 192     3485   3620   2649  -1221    362      3       C  
-ATOM   4641  C   LEU C 192       2.672   1.731  28.339  1.00 30.22           C  
-ANISOU 4641  C   LEU C 192     4091   4244   3147  -1173    299     62       C  
-ATOM   4642  O   LEU C 192       2.307   0.642  27.908  1.00 29.88           O  
-ANISOU 4642  O   LEU C 192     4028   4170   3157  -1040    340     80       O  
-ATOM   4643  CB  LEU C 192       0.936   3.435  27.809  1.00 27.92           C  
-ANISOU 4643  CB  LEU C 192     3921   3770   2917  -1241    479   -130       C  
-ATOM   4644  CG  LEU C 192       0.691   4.917  27.514  1.00 36.16           C  
-ANISOU 4644  CG  LEU C 192     4978   4728   4031  -1326    503   -198       C  
-ATOM   4645  CD1 LEU C 192       0.419   5.152  26.036  1.00 32.10           C  
-ANISOU 4645  CD1 LEU C 192     4346   4213   3637  -1227    584   -148       C  
-ATOM   4646  CD2 LEU C 192      -0.443   5.476  28.385  1.00 38.77           C  
-ANISOU 4646  CD2 LEU C 192     5491   4944   4296  -1362    584   -346       C  
-ATOM   4647  N   ASP C 193       3.314   1.868  29.492  1.00 29.54           N  
-ANISOU 4647  N   ASP C 193     4060   4216   2948  -1275    171     91       N  
-ATOM   4648  CA  ASP C 193       3.775   0.693  30.207  1.00 30.24           C  
-ANISOU 4648  CA  ASP C 193     4152   4372   2965  -1219     92    204       C  
-ATOM   4649  C   ASP C 193       3.148   0.496  31.575  1.00 32.55           C  
-ANISOU 4649  C   ASP C 193     4644   4668   3058  -1254    103    197       C  
-ATOM   4650  O   ASP C 193       2.585   1.420  32.169  1.00 32.80           O  
-ANISOU 4650  O   ASP C 193     4826   4679   2957  -1323    137     72       O  
-ATOM   4651  CB  ASP C 193       5.282   0.765  30.405  1.00 30.57           C  
-ANISOU 4651  CB  ASP C 193     4049   4541   3024  -1262   -100    313       C  
-ATOM   4652  CG  ASP C 193       5.666   1.768  31.453  1.00 33.38           C  
-ANISOU 4652  CG  ASP C 193     4500   4923   3261  -1428   -274    243       C  
-ATOM   4653  OD1 ASP C 193       5.237   2.933  31.334  1.00 33.11           O  
-ANISOU 4653  OD1 ASP C 193     4532   4797   3250  -1524   -253    105       O  
-ATOM   4654  OD2 ASP C 193       6.385   1.384  32.395  1.00 32.03           O  
-ANISOU 4654  OD2 ASP C 193     4346   4848   2974  -1449   -458    314       O  
-ATOM   4655  N   TYR C 194       3.276  -0.730  32.068  1.00 30.98           N  
-ANISOU 4655  N   TYR C 194     4441   4498   2831  -1176     81    349       N  
-ATOM   4656  CA  TYR C 194       3.173  -1.002  33.491  1.00 35.11           C  
-ANISOU 4656  CA  TYR C 194     5120   5110   3110  -1185     47    435       C  
-ATOM   4657  C   TYR C 194       4.468  -1.709  33.877  1.00 38.49           C  
-ANISOU 4657  C   TYR C 194     5456   5650   3518  -1157   -162    595       C  
-ATOM   4658  O   TYR C 194       4.715  -2.844  33.450  1.00 34.28           O  
-ANISOU 4658  O   TYR C 194     4800   5066   3158  -1057   -161    738       O  
-ATOM   4659  CB  TYR C 194       1.965  -1.873  33.789  1.00 30.61           C  
-ANISOU 4659  CB  TYR C 194     4605   4459   2568  -1114    243    555       C  
-ATOM   4660  CG  TYR C 194       1.904  -2.321  35.216  1.00 34.15           C  
-ANISOU 4660  CG  TYR C 194     5190   5039   2747  -1079    248    732       C  
-ATOM   4661  CD1 TYR C 194       1.352  -1.504  36.191  1.00 38.14           C  
-ANISOU 4661  CD1 TYR C 194     5897   5661   2932  -1080    333    650       C  
-ATOM   4662  CD2 TYR C 194       2.398  -3.560  35.597  1.00 38.11           C  
-ANISOU 4662  CD2 TYR C 194     5627   5559   3293  -1013    171    987       C  
-ATOM   4663  CE1 TYR C 194       1.288  -1.908  37.499  1.00 40.56           C  
-ANISOU 4663  CE1 TYR C 194     6349   6143   2919  -1000    357    828       C  
-ATOM   4664  CE2 TYR C 194       2.337  -3.974  36.910  1.00 44.61           C  
-ANISOU 4664  CE2 TYR C 194     6577   6533   3840   -961    185   1200       C  
-ATOM   4665  CZ  TYR C 194       1.789  -3.142  37.855  1.00 45.64           C  
-ANISOU 4665  CZ  TYR C 194     6916   6822   3601   -948    284   1124       C  
-ATOM   4666  OH  TYR C 194       1.724  -3.557  39.164  1.00 52.86           O  
-ANISOU 4666  OH  TYR C 194     7975   7939   4171   -849    317   1353       O  
-ATOM   4667  N   ASN C 195       5.294  -1.023  34.668  1.00 34.92           N  
-ANISOU 4667  N   ASN C 195     5060   5331   2878  -1237   -369    555       N  
-ATOM   4668  CA AASN C 195       6.618  -1.523  35.023  0.45 38.04           C  
-ANISOU 4668  CA AASN C 195     5333   5844   3276  -1225   -612    705       C  
-ATOM   4669  CA BASN C 195       6.636  -1.493  35.009  0.55 35.68           C  
-ANISOU 4669  CA BASN C 195     5031   5546   2980  -1228   -615    700       C  
-ATOM   4670  C   ASN C 195       7.442  -2.010  33.821  1.00 39.18           C  
-ANISOU 4670  C   ASN C 195     5196   5955   3737  -1164   -624    791       C  
-ATOM   4671  O   ASN C 195       8.015  -3.103  33.864  1.00 39.04           O  
-ANISOU 4671  O   ASN C 195     5070   5965   3798  -1049   -682    972       O  
-ATOM   4672  CB AASN C 195       6.493  -2.635  36.060  0.45 41.70           C  
-ANISOU 4672  CB AASN C 195     5898   6387   3560  -1124   -625    919       C  
-ATOM   4673  CB BASN C 195       6.594  -2.514  36.142  0.55 42.81           C  
-ANISOU 4673  CB BASN C 195     6045   6545   3676  -1136   -656    906       C  
-ATOM   4674  CG AASN C 195       7.784  -2.888  36.797  0.45 42.21           C  
-ANISOU 4674  CG AASN C 195     5900   6612   3524  -1120   -928   1051       C  
-ATOM   4675  CG BASN C 195       6.628  -1.856  37.499  0.55 46.48           C  
-ANISOU 4675  CG BASN C 195     6745   7172   3742  -1172   -806    834       C  
-ATOM   4676  OD1AASN C 195       8.708  -2.071  36.760  0.45 41.54           O  
-ANISOU 4676  OD1AASN C 195     5726   6589   3470  -1223  -1158    951       O  
-ATOM   4677  OD1BASN C 195       7.212  -0.783  37.658  0.55 49.08           O  
-ANISOU 4677  OD1BASN C 195     7097   7539   4011  -1280  -1022    643       O  
-ATOM   4678  ND2AASN C 195       7.858  -4.024  37.474  0.45 42.73           N  
-ANISOU 4678  ND2AASN C 195     5992   6735   3509  -1007   -947   1305       N  
-ATOM   4679  ND2BASN C 195       6.010  -2.490  38.488  0.55 52.88           N  
-ANISOU 4679  ND2BASN C 195     7731   8079   4282  -1067   -705    993       N  
-ATOM   4680  N   GLU C 196       7.479  -1.193  32.764  1.00 36.95           N  
-ANISOU 4680  N   GLU C 196     4801   5621   3619  -1211   -554    676       N  
-ATOM   4681  CA  GLU C 196       8.223  -1.454  31.519  1.00 38.68           C  
-ANISOU 4681  CA  GLU C 196     4758   5858   4082  -1113   -513    752       C  
-ATOM   4682  C   GLU C 196       7.581  -2.481  30.583  1.00 37.40           C  
-ANISOU 4682  C   GLU C 196     4584   5595   4031   -916   -327    745       C  
-ATOM   4683  O   GLU C 196       7.959  -2.578  29.415  1.00 37.13           O  
-ANISOU 4683  O   GLU C 196     4388   5586   4134   -786   -250    747       O  
-ATOM   4684  CB  GLU C 196       9.699  -1.784  31.787  1.00 42.66           C  
-ANISOU 4684  CB  GLU C 196     5041   6501   4665  -1093   -722    934       C  
-ATOM   4685  CG  GLU C 196      10.442  -0.675  32.523  1.00 46.46           C  
-ANISOU 4685  CG  GLU C 196     5484   7054   5116  -1303   -977    918       C  
-ATOM   4686  CD  GLU C 196      10.317   0.687  31.834  1.00 51.83           C  
-ANISOU 4686  CD  GLU C 196     6100   7664   5927  -1445   -927    811       C  
-ATOM   4687  OE1 GLU C 196      10.362   0.744  30.584  1.00 44.44           O  
-ANISOU 4687  OE1 GLU C 196     4991   6729   5164  -1358   -734    870       O  
-ATOM   4688  OE2 GLU C 196      10.174   1.703  32.552  1.00 55.55           O  
-ANISOU 4688  OE2 GLU C 196     6708   8079   6321  -1625  -1090    668       O  
-ATOM   4689  N   TYR C 197       6.592  -3.220  31.074  1.00 33.74           N  
-ANISOU 4689  N   TYR C 197     4287   5015   3515   -883   -260    739       N  
-ATOM   4690  CA  TYR C 197       5.874  -4.166  30.219  1.00 34.04           C  
-ANISOU 4690  CA  TYR C 197     4321   4894   3718   -723   -145    698       C  
-ATOM   4691  C   TYR C 197       4.722  -3.514  29.465  1.00 29.76           C  
-ANISOU 4691  C   TYR C 197     3853   4253   3202   -754      4    520       C  
-ATOM   4692  O   TYR C 197       4.299  -2.406  29.811  1.00 29.24           O  
-ANISOU 4692  O   TYR C 197     3873   4217   3021   -903     50    447       O  
-ATOM   4693  CB  TYR C 197       5.360  -5.357  31.032  1.00 38.51           C  
-ANISOU 4693  CB  TYR C 197     4973   5338   4323   -683   -163    833       C  
-ATOM   4694  CG  TYR C 197       6.475  -6.277  31.459  1.00 47.07           C  
-ANISOU 4694  CG  TYR C 197     5956   6476   5452   -581   -313   1022       C  
-ATOM   4695  CD1 TYR C 197       6.884  -7.324  30.644  1.00 49.14           C  
-ANISOU 4695  CD1 TYR C 197     6101   6630   5942   -368   -346   1028       C  
-ATOM   4696  CD2 TYR C 197       7.143  -6.079  32.664  1.00 48.01           C  
-ANISOU 4696  CD2 TYR C 197     6103   6758   5381   -669   -445   1175       C  
-ATOM   4697  CE1 TYR C 197       7.914  -8.158  31.019  1.00 52.02           C  
-ANISOU 4697  CE1 TYR C 197     6357   7033   6376   -250   -479   1207       C  
-ATOM   4698  CE2 TYR C 197       8.172  -6.908  33.050  1.00 50.75           C  
-ANISOU 4698  CE2 TYR C 197     6338   7161   5783   -568   -601   1368       C  
-ATOM   4699  CZ  TYR C 197       8.555  -7.944  32.222  1.00 54.24           C  
-ANISOU 4699  CZ  TYR C 197     6641   7480   6486   -360   -605   1396       C  
-ATOM   4700  OH  TYR C 197       9.583  -8.772  32.601  1.00 61.07           O  
-ANISOU 4700  OH  TYR C 197     7381   8388   7434   -235   -756   1596       O  
-ATOM   4701  N   PHE C 198       4.238  -4.219  28.439  1.00 26.82           N  
-ANISOU 4701  N   PHE C 198     3229   3465   3496  -1125     71    -96       N  
-ATOM   4702  CA  PHE C 198       3.059  -3.848  27.648  1.00 25.69           C  
-ANISOU 4702  CA  PHE C 198     3235   3204   3322  -1049    275   -174       C  
-ATOM   4703  C   PHE C 198       3.331  -2.741  26.620  1.00 26.27           C  
-ANISOU 4703  C   PHE C 198     3336   3146   3499  -1023    464   -322       C  
-ATOM   4704  O   PHE C 198       2.430  -2.332  25.899  1.00 27.98           O  
-ANISOU 4704  O   PHE C 198     3669   3270   3691   -946    611   -366       O  
-ATOM   4705  CB  PHE C 198       1.869  -3.446  28.537  1.00 27.05           C  
-ANISOU 4705  CB  PHE C 198     3542   3487   3251  -1109    327   -198       C  
-ATOM   4706  CG  PHE C 198       1.413  -4.524  29.502  1.00 28.17           C  
-ANISOU 4706  CG  PHE C 198     3668   3764   3272  -1126    205     13       C  
-ATOM   4707  CD1 PHE C 198       0.658  -5.598  29.058  1.00 29.30           C  
-ANISOU 4707  CD1 PHE C 198     3778   3803   3551  -1048    195    182       C  
-ATOM   4708  CD2 PHE C 198       1.717  -4.435  30.857  1.00 32.51           C  
-ANISOU 4708  CD2 PHE C 198     4249   4538   3564  -1229     93     49       C  
-ATOM   4709  CE1 PHE C 198       0.219  -6.589  29.948  1.00 28.54           C  
-ANISOU 4709  CE1 PHE C 198     3648   3797   3398  -1079    109    433       C  
-ATOM   4710  CE2 PHE C 198       1.290  -5.415  31.761  1.00 32.08           C  
-ANISOU 4710  CE2 PHE C 198     4193   4626   3369  -1234     12    309       C  
-ATOM   4711  CZ  PHE C 198       0.545  -6.497  31.307  1.00 34.03           C  
-ANISOU 4711  CZ  PHE C 198     4375   4741   3814  -1162     38    525       C  
-ATOM   4712  N   ARG C 199       4.563  -2.249  26.562  1.00 24.00           N  
-ANISOU 4712  N   ARG C 199     2919   2849   3352  -1092    455   -362       N  
-ATOM   4713  CA  ARG C 199       4.903  -1.240  25.561  1.00 26.48           C  
-ANISOU 4713  CA  ARG C 199     3236   3022   3805  -1074    667   -434       C  
-ATOM   4714  C   ARG C 199       4.783  -1.840  24.157  1.00 31.40           C  
-ANISOU 4714  C   ARG C 199     3894   3545   4491   -862    814   -358       C  
-ATOM   4715  O   ARG C 199       4.461  -1.137  23.199  1.00 36.07           O  
-ANISOU 4715  O   ARG C 199     4591   4039   5076   -787   1009   -378       O  
-ATOM   4716  CB  ARG C 199       6.314  -0.685  25.777  1.00 28.32           C  
-ANISOU 4716  CB  ARG C 199     3258   3252   4251  -1213    626   -450       C  
-ATOM   4717  CG  ARG C 199       6.552   0.040  27.114  1.00 27.25           C  
-ANISOU 4717  CG  ARG C 199     3117   3202   4035  -1447    429   -590       C  
-ATOM   4718  CD  ARG C 199       7.631   1.083  26.967  1.00 29.58           C  
-ANISOU 4718  CD  ARG C 199     3245   3386   4610  -1615    454   -658       C  
-ATOM   4719  NE  ARG C 199       8.198   1.574  28.233  1.00 32.71           N  
-ANISOU 4719  NE  ARG C 199     3585   3869   4974  -1863    162   -810       N  
-ATOM   4720  CZ  ARG C 199       7.736   2.623  28.907  1.00 33.33           C  
-ANISOU 4720  CZ  ARG C 199     3864   3884   4914  -2009    134  -1059       C  
-ATOM   4721  NH1 ARG C 199       6.671   3.279  28.462  1.00 36.20           N  
-ANISOU 4721  NH1 ARG C 199     4463   4097   5194  -1898    395  -1133       N  
-ATOM   4722  NH2 ARG C 199       8.313   2.996  30.042  1.00 35.48           N  
-ANISOU 4722  NH2 ARG C 199     4119   4249   5112  -2203   -178  -1215       N  
-ATOM   4723  N   ASP C 200       5.026  -3.146  24.065  1.00 30.00           N  
-ANISOU 4723  N   ASP C 200     3652   3387   4359   -756    707   -273       N  
-ATOM   4724  CA  ASP C 200       5.054  -3.900  22.813  1.00 32.92           C  
-ANISOU 4724  CA  ASP C 200     4081   3657   4769   -542    813   -256       C  
-ATOM   4725  C   ASP C 200       3.671  -4.438  22.447  1.00 34.97           C  
-ANISOU 4725  C   ASP C 200     4541   3864   4882   -465    744   -288       C  
-ATOM   4726  O   ASP C 200       3.517  -5.590  22.031  1.00 42.89           O  
-ANISOU 4726  O   ASP C 200     5587   4787   5922   -345    659   -287       O  
-ATOM   4727  CB  ASP C 200       6.013  -5.079  22.950  1.00 34.94           C  
-ANISOU 4727  CB  ASP C 200     4166   3905   5207   -454    722   -174       C  
-ATOM   4728  CG  ASP C 200       5.598  -6.033  24.050  1.00 38.18           C  
-ANISOU 4728  CG  ASP C 200     4547   4356   5603   -518    459    -88       C  
-ATOM   4729  OD1 ASP C 200       5.100  -5.551  25.090  1.00 33.29           O  
-ANISOU 4729  OD1 ASP C 200     3949   3855   4845   -689    351    -75       O  
-ATOM   4730  OD2 ASP C 200       5.744  -7.261  23.859  1.00 40.02           O  
-ANISOU 4730  OD2 ASP C 200     4756   4490   5961   -386    382    -28       O  
-ATOM   4731  N   LEU C 201       2.668  -3.597  22.627  1.00 37.07           N  
-ANISOU 4731  N   LEU C 201     4908   4151   5024   -538    770   -321       N  
-ATOM   4732  CA  LEU C 201       1.279  -3.947  22.380  1.00 33.86           C  
-ANISOU 4732  CA  LEU C 201     4622   3712   4531   -496    687   -324       C  
-ATOM   4733  C   LEU C 201       0.756  -2.789  21.537  1.00 31.25           C  
-ANISOU 4733  C   LEU C 201     4410   3348   4115   -436    841   -359       C  
-ATOM   4734  O   LEU C 201       1.020  -1.640  21.863  1.00 27.01           O  
-ANISOU 4734  O   LEU C 201     3853   2818   3590   -510    974   -373       O  
-ATOM   4735  CB  LEU C 201       0.546  -4.066  23.718  1.00 33.63           C  
-ANISOU 4735  CB  LEU C 201     4534   3773   4469   -635    581   -264       C  
-ATOM   4736  CG  LEU C 201      -0.967  -4.226  23.820  1.00 35.13           C  
-ANISOU 4736  CG  LEU C 201     4757   3960   4632   -641    530   -218       C  
-ATOM   4737  CD1 LEU C 201      -1.420  -5.521  23.153  1.00 40.10           C  
-ANISOU 4737  CD1 LEU C 201     5398   4473   5365   -577    358   -184       C  
-ATOM   4738  CD2 LEU C 201      -1.410  -4.183  25.307  1.00 27.37           C  
-ANISOU 4738  CD2 LEU C 201     3705   3114   3580   -768    527   -136       C  
-ATOM   4739  N   ASN C 202       0.057  -3.073  20.438  1.00 30.30           N  
-ANISOU 4739  N   ASN C 202     4421   3175   3917   -301    801   -373       N  
-ATOM   4740  CA AASN C 202      -0.351  -1.987  19.546  0.47 28.64           C  
-ANISOU 4740  CA AASN C 202     4328   2944   3609   -213    933   -352       C  
-ATOM   4741  CA BASN C 202      -0.393  -2.036  19.500  0.53 28.83           C  
-ANISOU 4741  CA BASN C 202     4359   2968   3629   -206    924   -353       C  
-ATOM   4742  C   ASN C 202      -1.611  -1.254  20.005  1.00 28.14           C  
-ANISOU 4742  C   ASN C 202     4245   2886   3562   -258    908   -311       C  
-ATOM   4743  O   ASN C 202      -1.756  -0.061  19.752  1.00 31.82           O  
-ANISOU 4743  O   ASN C 202     4753   3311   4027   -226   1061   -271       O  
-ATOM   4744  CB AASN C 202      -0.441  -2.435  18.073  0.47 30.27           C  
-ANISOU 4744  CB AASN C 202     4718   3129   3656    -23    903   -379       C  
-ATOM   4745  CB BASN C 202      -0.716  -2.677  18.142  0.53 30.22           C  
-ANISOU 4745  CB BASN C 202     4709   3118   3654    -31    832   -390       C  
-ATOM   4746  CG AASN C 202      -1.472  -3.527  17.845  0.47 29.89           C  
-ANISOU 4746  CG AASN C 202     4722   3052   3585      0    611   -441       C  
-ATOM   4747  CG BASN C 202      -0.046  -1.970  16.977  0.53 37.42           C  
-ANISOU 4747  CG BASN C 202     5763   4040   4415    119   1057   -351       C  
-ATOM   4748  OD1AASN C 202      -1.819  -4.267  18.762  0.47 26.79           O  
-ANISOU 4748  OD1AASN C 202     4200   2637   3341   -120    463   -438       O  
-ATOM   4749  OD1BASN C 202       0.882  -1.176  17.159  0.53 45.70           O  
-ANISOU 4749  OD1BASN C 202     6734   5083   5548     77   1295   -284       O  
-ATOM   4750  ND2AASN C 202      -1.963  -3.635  16.609  0.47 28.92           N  
-ANISOU 4750  ND2AASN C 202     4791   2925   3274    145    513   -485       N  
-ATOM   4751  ND2BASN C 202      -0.512  -2.263  15.766  0.53 43.97           N  
-ANISOU 4751  ND2BASN C 202     6804   4886   5016    288    974   -381       N  
-ATOM   4752  N   HIS C 203      -2.502  -1.944  20.712  1.00 28.46           N  
-ANISOU 4752  N   HIS C 203     4200   2958   3655   -326    746   -297       N  
-ATOM   4753  CA  HIS C 203      -3.714  -1.298  21.210  1.00 24.60           C  
-ANISOU 4753  CA  HIS C 203     3646   2487   3215   -344    771   -242       C  
-ATOM   4754  C   HIS C 203      -3.491  -0.729  22.611  1.00 28.07           C  
-ANISOU 4754  C   HIS C 203     4017   2978   3670   -463    913   -276       C  
-ATOM   4755  O   HIS C 203      -2.619  -1.206  23.343  1.00 28.75           O  
-ANISOU 4755  O   HIS C 203     4072   3120   3731   -565    885   -310       O  
-ATOM   4756  CB  HIS C 203      -4.855  -2.306  21.319  1.00 23.83           C  
-ANISOU 4756  CB  HIS C 203     3447   2405   3201   -367    559   -176       C  
-ATOM   4757  CG  HIS C 203      -5.041  -3.162  20.112  1.00 24.07           C  
-ANISOU 4757  CG  HIS C 203     3563   2375   3209   -291    329   -207       C  
-ATOM   4758  ND1 HIS C 203      -5.518  -2.670  18.918  1.00 27.24           N  
-ANISOU 4758  ND1 HIS C 203     4071   2761   3517   -157    262   -201       N  
-ATOM   4759  CD2 HIS C 203      -4.827  -4.486  19.921  1.00 25.93           C  
-ANISOU 4759  CD2 HIS C 203     3817   2546   3489   -321    132   -260       C  
-ATOM   4760  CE1 HIS C 203      -5.593  -3.656  18.040  1.00 28.38           C  
-ANISOU 4760  CE1 HIS C 203     4320   2860   3603   -115     18   -284       C  
-ATOM   4761  NE2 HIS C 203      -5.180  -4.764  18.623  1.00 26.26           N  
-ANISOU 4761  NE2 HIS C 203     4000   2535   3443   -213    -54   -337       N  
-ATOM   4762  N   VAL C 204      -4.308   0.252  23.005  1.00 22.87           N  
-ANISOU 4762  N   VAL C 204     3340   2305   3044   -436   1051   -271       N  
-ATOM   4763  CA  VAL C 204      -4.388   0.637  24.414  1.00 22.09           C  
-ANISOU 4763  CA  VAL C 204     3213   2277   2904   -526   1174   -338       C  
-ATOM   4764  C   VAL C 204      -5.388  -0.282  25.096  1.00 28.53           C  
-ANISOU 4764  C   VAL C 204     3899   3209   3730   -550   1111   -220       C  
-ATOM   4765  O   VAL C 204      -6.476  -0.521  24.572  1.00 31.15           O  
-ANISOU 4765  O   VAL C 204     4129   3520   4186   -476   1056   -104       O  
-ATOM   4766  CB  VAL C 204      -4.780   2.105  24.591  1.00 21.26           C  
-ANISOU 4766  CB  VAL C 204     3165   2068   2846   -460   1396   -419       C  
-ATOM   4767  CG1 VAL C 204      -5.140   2.400  26.048  1.00 25.93           C  
-ANISOU 4767  CG1 VAL C 204     3761   2750   3342   -511   1536   -520       C  
-ATOM   4768  CG2 VAL C 204      -3.641   3.017  24.131  1.00 25.47           C  
-ANISOU 4768  CG2 VAL C 204     3806   2455   3416   -493   1472   -513       C  
-ATOM   4769  N   CYS C 205      -5.010  -0.819  26.252  1.00 28.39           N  
-ANISOU 4769  N   CYS C 205     3870   3322   3597   -662   1103   -218       N  
-ATOM   4770  CA  CYS C 205      -5.813  -1.824  26.941  1.00 30.76           C  
-ANISOU 4770  CA  CYS C 205     4040   3734   3915   -704   1064    -41       C  
-ATOM   4771  C   CYS C 205      -5.815  -1.546  28.419  1.00 31.14           C  
-ANISOU 4771  C   CYS C 205     4130   3955   3746   -757   1230    -63       C  
-ATOM   4772  O   CYS C 205      -4.888  -0.932  28.941  1.00 30.75           O  
-ANISOU 4772  O   CYS C 205     4221   3944   3519   -807   1256   -237       O  
-ATOM   4773  CB  CYS C 205      -5.252  -3.230  26.682  1.00 31.35           C  
-ANISOU 4773  CB  CYS C 205     4074   3785   4055   -775    821     63       C  
-ATOM   4774  N   VAL C 206      -6.859  -2.002  29.098  1.00 29.70           N  
-ANISOU 4774  N   VAL C 206     3825   3886   3573   -750   1339    119       N  
-ATOM   4775  CA  VAL C 206      -6.888  -1.940  30.545  1.00 38.94           C  
-ANISOU 4775  CA  VAL C 206     5064   5272   4458   -784   1510    138       C  
-ATOM   4776  C   VAL C 206      -6.224  -3.211  31.055  1.00 38.56           C  
-ANISOU 4776  C   VAL C 206     4999   5326   4328   -904   1307    328       C  
-ATOM   4777  O   VAL C 206      -6.557  -4.316  30.627  1.00 36.73           O  
-ANISOU 4777  O   VAL C 206     4611   5013   4332   -942   1165    554       O  
-ATOM   4778  CB  VAL C 206      -8.325  -1.833  31.084  1.00 40.21           C  
-ANISOU 4778  CB  VAL C 206     5081   5531   4665   -695   1798    297       C  
-ATOM   4779  CG1 VAL C 206      -8.322  -1.665  32.598  1.00 38.97           C  
-ANISOU 4779  CG1 VAL C 206     5048   5629   4129   -672   1982    291       C  
-ATOM   4780  CG2 VAL C 206      -9.040  -0.658  30.436  1.00 43.77           C  
-ANISOU 4780  CG2 VAL C 206     5498   5840   5293   -539   1968    157       C  
-ATOM   4781  N   ILE C 207      -5.259  -3.042  31.950  1.00 38.91           N  
-ANISOU 4781  N   ILE C 207     5204   5520   4059   -966   1263    230       N  
-ATOM   4782  CA  ILE C 207      -4.552  -4.162  32.560  1.00 38.52           C  
-ANISOU 4782  CA  ILE C 207     5143   5587   3907  -1058   1060    440       C  
-ATOM   4783  C   ILE C 207      -5.453  -4.810  33.612  1.00 44.14           C  
-ANISOU 4783  C   ILE C 207     5801   6499   4469  -1061   1228    750       C  
-ATOM   4784  O   ILE C 207      -6.204  -4.112  34.294  1.00 47.76           O  
-ANISOU 4784  O   ILE C 207     6325   7111   4709   -996   1522    698       O  
-ATOM   4785  CB  ILE C 207      -3.222  -3.663  33.194  1.00 49.00           C  
-ANISOU 4785  CB  ILE C 207     6639   7037   4942  -1125    913    239       C  
-ATOM   4786  CG1 ILE C 207      -2.355  -4.826  33.688  1.00 47.24           C  
-ANISOU 4786  CG1 ILE C 207     6368   6914   4669  -1195    646    484       C  
-ATOM   4787  CG2 ILE C 207      -3.497  -2.645  34.317  1.00 52.18           C  
-ANISOU 4787  CG2 ILE C 207     7247   7648   4931  -1111   1117     41       C  
-ATOM   4788  CD1 ILE C 207      -0.964  -4.389  34.167  1.00 48.76           C  
-ANISOU 4788  CD1 ILE C 207     6653   7216   4658  -1273    419    306       C  
-ATOM   4789  N   SER C 208      -5.399  -6.139  33.726  1.00 37.79           N  
-ANISOU 4789  N   SER C 208     4874   5676   3809  -1123   1075   1087       N  
-ATOM   4790  CA  SER C 208      -6.170  -6.859  34.731  1.00 48.00           C  
-ANISOU 4790  CA  SER C 208     6098   7146   4994  -1141   1240   1463       C  
-ATOM   4791  C   SER C 208      -5.460  -6.864  36.092  1.00 53.33           C  
-ANISOU 4791  C   SER C 208     6979   8120   5165  -1139   1215   1519       C  
-ATOM   4792  O   SER C 208      -4.319  -6.420  36.208  1.00 52.00           O  
-ANISOU 4792  O   SER C 208     6964   8035   4760  -1183   1017   1301       O  
-ATOM   4793  CB  SER C 208      -6.420  -8.302  34.289  1.00 49.86           C  
-ANISOU 4793  CB  SER C 208     6132   7139   5674  -1184   1053   1769       C  
-ATOM   4794  OG  SER C 208      -5.219  -9.044  34.222  1.00 47.37           O  
-ANISOU 4794  OG  SER C 208     5849   6775   5376  -1252    759   1873       O  
-ATOM   4795  N   GLU C 209      -6.138  -7.366  37.122  1.00 54.80           N  
-ANISOU 4795  N   GLU C 209     7177   8419   5225  -1071   1385   1773       N  
-ATOM   4796  CA  GLU C 209      -5.503  -7.511  38.433  1.00 58.95           C  
-ANISOU 4796  CA  GLU C 209     7913   9230   5257  -1052   1326   1871       C  
-ATOM   4797  C   GLU C 209      -4.422  -8.595  38.372  1.00 58.01           C  
-ANISOU 4797  C   GLU C 209     7724   9081   5237  -1146    945   2129       C  
-ATOM   4798  O   GLU C 209      -3.357  -8.448  38.964  1.00 60.47           O  
-ANISOU 4798  O   GLU C 209     8186   9601   5187  -1175    718   2084       O  
-ATOM   4799  CB  GLU C 209      -6.534  -7.817  39.528  1.00 68.09           C  
-ANISOU 4799  CB  GLU C 209     9123  10497   6249   -967   1639   2099       C  
-ATOM   4800  CG  GLU C 209      -7.792  -6.941  39.486  1.00 75.23           C  
-ANISOU 4800  CG  GLU C 209    10024  11360   7198   -886   2046   1913       C  
-ATOM   4801  CD  GLU C 209      -7.516  -5.453  39.696  1.00 82.16           C  
-ANISOU 4801  CD  GLU C 209    11162  12346   7708   -762   2177   1474       C  
-ATOM   4802  OE1 GLU C 209      -8.334  -4.628  39.230  1.00 83.44           O  
-ANISOU 4802  OE1 GLU C 209    11273  12380   8050   -688   2440   1272       O  
-ATOM   4803  OE2 GLU C 209      -6.496  -5.106  40.333  1.00 86.20           O  
-ANISOU 4803  OE2 GLU C 209    11909  13063   7780   -742   1982   1318       O  
-ATOM   4804  N   THR C 210      -4.695  -9.670  37.635  1.00 58.90           N  
-ANISOU 4804  N   THR C 210     7604   8901   5874  -1183    848   2373       N  
-ATOM   4805  CA  THR C 210      -3.711 -10.734  37.427  1.00 62.15           C  
-ANISOU 4805  CA  THR C 210     7930   9185   6499  -1232    508   2604       C  
-ATOM   4806  C   THR C 210      -2.430 -10.195  36.782  1.00 59.69           C  
-ANISOU 4806  C   THR C 210     7669   8872   6138  -1292    248   2365       C  
-ATOM   4807  O   THR C 210      -1.320 -10.555  37.184  1.00 60.41           O  
-ANISOU 4807  O   THR C 210     7784   9046   6124  -1290    -30   2461       O  
-ATOM   4808  CB  THR C 210      -4.293 -11.879  36.571  1.00 68.99           C  
-ANISOU 4808  CB  THR C 210     8566   9652   7995  -1244    452   2776       C  
-ATOM   4809  OG1 THR C 210      -5.381 -12.492  37.275  1.00 74.86           O  
-ANISOU 4809  OG1 THR C 210     9238  10406   8798  -1222    651   3032       O  
-ATOM   4810  CG2 THR C 210      -3.230 -12.935  36.278  1.00 72.27           C  
-ANISOU 4810  CG2 THR C 210     8909   9868   8683  -1251    123   2957       C  
-ATOM   4811  N   GLY C 211      -2.591  -9.319  35.791  1.00 51.45           N  
-ANISOU 4811  N   GLY C 211     6621   7667   5259  -1274    324   1952       N  
-ATOM   4812  CA  GLY C 211      -1.458  -8.690  35.141  1.00 45.15           C  
-ANISOU 4812  CA  GLY C 211     5856   6784   4514  -1263    130   1592       C  
-ATOM   4813  C   GLY C 211      -0.698  -7.764  36.076  1.00 47.57           C  
-ANISOU 4813  C   GLY C 211     6341   7399   4333  -1299     54   1392       C  
-ATOM   4814  O   GLY C 211       0.531  -7.707  36.038  1.00 49.82           O  
-ANISOU 4814  O   GLY C 211     6600   7695   4637  -1324   -218   1300       O  
-ATOM   4815  N   LYS C 212      -1.429  -7.037  36.916  1.00 50.21           N  
-ANISOU 4815  N   LYS C 212     6851   7979   4249  -1297    290   1312       N  
-ATOM   4816  CA  LYS C 212      -0.818  -6.110  37.861  1.00 56.39           C  
-ANISOU 4816  CA  LYS C 212     7862   9046   4519  -1338    209   1055       C  
-ATOM   4817  C   LYS C 212       0.085  -6.839  38.851  1.00 58.69           C  
-ANISOU 4817  C   LYS C 212     8189   9595   4516  -1378   -115   1335       C  
-ATOM   4818  O   LYS C 212       1.110  -6.308  39.279  1.00 57.80           O  
-ANISOU 4818  O   LYS C 212     8166   9628   4166  -1446   -397   1121       O  
-ATOM   4819  CB  LYS C 212      -1.896  -5.329  38.615  1.00 64.20           C  
-ANISOU 4819  CB  LYS C 212     9060  10241   5091  -1285    579    930       C  
-ATOM   4820  CG  LYS C 212      -2.388  -4.089  37.887  1.00 67.49           C  
-ANISOU 4820  CG  LYS C 212     9517  10457   5670  -1245    813    503       C  
-ATOM   4821  CD  LYS C 212      -3.611  -3.483  38.573  1.00 74.20           C  
-ANISOU 4821  CD  LYS C 212    10484  11383   6326  -1069   1206    430       C  
-ATOM   4822  CE  LYS C 212      -4.026  -2.180  37.893  1.00 72.16           C  
-ANISOU 4822  CE  LYS C 212    10258  10905   6256  -1001   1402     26       C  
-ATOM   4823  NZ  LYS C 212      -5.204  -1.549  38.552  1.00 75.14           N  
-ANISOU 4823  NZ  LYS C 212    10702  11338   6511   -767   1765    -26       N  
-ATOM   4824  N   ALA C 213      -0.305  -8.061  39.201  1.00 58.49           N  
-ANISOU 4824  N   ALA C 213     8073   9607   4543  -1342    -97   1836       N  
-ATOM   4825  CA  ALA C 213       0.416  -8.853  40.191  1.00 62.18           C  
-ANISOU 4825  CA  ALA C 213     8559  10274   4794  -1321   -377   2162       C  
-ATOM   4826  C   ALA C 213       1.624  -9.589  39.609  1.00 61.14           C  
-ANISOU 4826  C   ALA C 213     8207   9981   5041  -1351   -774   2334       C  
-ATOM   4827  O   ALA C 213       2.639  -9.748  40.288  1.00 65.31           O  
-ANISOU 4827  O   ALA C 213     8742  10705   5369  -1360  -1119   2428       O  
-ATOM   4828  CB  ALA C 213      -0.528  -9.832  40.874  1.00 63.51           C  
-ANISOU 4828  CB  ALA C 213     8709  10430   4992  -1211   -150   2571       C  
-ATOM   4829  N   LYS C 214       1.508 -10.053  38.367  1.00 53.91           N  
-ANISOU 4829  N   LYS C 214     7081   8659   4743  -1314   -713   2318       N  
-ATOM   4830  CA  LYS C 214       2.610 -10.753  37.707  1.00 58.28           C  
-ANISOU 4830  CA  LYS C 214     7412   8974   5758  -1268  -1002   2402       C  
-ATOM   4831  C   LYS C 214       3.780  -9.807  37.436  1.00 55.12           C  
-ANISOU 4831  C   LYS C 214     6972   8625   5347  -1312  -1211   2015       C  
-ATOM   4832  O   LYS C 214       4.948 -10.195  37.542  1.00 56.91           O  
-ANISOU 4832  O   LYS C 214     7034   8870   5720  -1290  -1529   2138       O  
-ATOM   4833  CB  LYS C 214       2.146 -11.384  36.384  1.00 58.17           C  
-ANISOU 4833  CB  LYS C 214     7245   8511   6345  -1205   -857   2390       C  
-ATOM   4834  CG  LYS C 214       3.220 -12.220  35.674  1.00 61.80           C  
-ANISOU 4834  CG  LYS C 214     7495   8693   7293  -1107  -1086   2474       C  
-ATOM   4835  CD  LYS C 214       2.839 -12.551  34.231  1.00 60.35           C  
-ANISOU 4835  CD  LYS C 214     7240   8086   7604  -1038   -939   2288       C  
-ATOM   4836  CE  LYS C 214       1.510 -13.289  34.153  1.00 64.29           C  
-ANISOU 4836  CE  LYS C 214     7765   8403   8259  -1067   -778   2503       C  
-ATOM   4837  NZ  LYS C 214       1.096 -13.526  32.741  1.00 63.01           N  
-ANISOU 4837  NZ  LYS C 214     7571   7855   8516  -1019   -696   2260       N  
-ATOM   4838  N   TYR C 215       3.456  -8.562  37.097  1.00 49.39           N  
-ANISOU 4838  N   TYR C 215     6368   7903   4495  -1374  -1027   1576       N  
-ATOM   4839  CA  TYR C 215       4.456  -7.606  36.624  1.00 47.86           C  
-ANISOU 4839  CA  TYR C 215     6105   7663   4418  -1439  -1163   1204       C  
-ATOM   4840  C   TYR C 215       4.845  -6.530  37.631  1.00 54.62           C  
-ANISOU 4840  C   TYR C 215     7144   8825   4785  -1573  -1325    941       C  
-ATOM   4841  O   TYR C 215       5.664  -5.665  37.326  1.00 60.09           O  
-ANISOU 4841  O   TYR C 215     7768   9462   5600  -1669  -1456    632       O  
-ATOM   4842  CB  TYR C 215       3.986  -6.953  35.324  1.00 45.94           C  
-ANISOU 4842  CB  TYR C 215     5846   7121   4489  -1413   -874    896       C  
-ATOM   4843  CG  TYR C 215       3.847  -7.936  34.195  1.00 49.03           C  
-ANISOU 4843  CG  TYR C 215     6072   7197   5359  -1288   -792   1057       C  
-ATOM   4844  CD1 TYR C 215       4.962  -8.583  33.674  1.00 48.16           C  
-ANISOU 4844  CD1 TYR C 215     5740   6947   5612  -1216   -974   1158       C  
-ATOM   4845  CD2 TYR C 215       2.601  -8.221  33.647  1.00 50.73           C  
-ANISOU 4845  CD2 TYR C 215     6347   7248   5679  -1236   -543   1092       C  
-ATOM   4846  CE1 TYR C 215       4.836  -9.492  32.638  1.00 49.29           C  
-ANISOU 4846  CE1 TYR C 215     5784   6781   6161  -1079   -888   1247       C  
-ATOM   4847  CE2 TYR C 215       2.468  -9.123  32.609  1.00 50.82           C  
-ANISOU 4847  CE2 TYR C 215     6248   6957   6105  -1136   -517   1181       C  
-ATOM   4848  CZ  TYR C 215       3.587  -9.755  32.110  1.00 51.73           C  
-ANISOU 4848  CZ  TYR C 215     6203   6925   6529  -1051   -680   1236       C  
-ATOM   4849  OH  TYR C 215       3.447 -10.654  31.076  1.00 54.61           O  
-ANISOU 4849  OH  TYR C 215     6508   6968   7271   -931   -641   1267       O  
-ATOM   4850  N   LYS C 216       4.272  -6.577  38.828  1.00 52.59           N  
-ANISOU 4850  N   LYS C 216     7125   8881   3975  -1584  -1312   1059       N  
-ATOM   4851  CA  LYS C 216       4.647  -5.611  39.856  1.00 64.12           C  
-ANISOU 4851  CA  LYS C 216     8821  10647   4896  -1702  -1503    768       C  
-ATOM   4852  C   LYS C 216       6.092  -5.833  40.295  1.00 71.37           C  
-ANISOU 4852  C   LYS C 216     9574  11718   5826  -1788  -2038    856       C  
-ATOM   4853  O   LYS C 216       6.592  -6.959  40.281  1.00 71.90           O  
-ANISOU 4853  O   LYS C 216     9416  11782   6120  -1711  -2238   1285       O  
-ATOM   4854  CB  LYS C 216       3.707  -5.685  41.060  1.00 67.35           C  
-ANISOU 4854  CB  LYS C 216     9535  11340   4714  -1620  -1308    877       C  
-ATOM   4855  CG  LYS C 216       4.229  -6.504  42.226  1.00 75.36           C  
-ANISOU 4855  CG  LYS C 216    10572  12591   5470  -1539  -1586   1216       C  
-ATOM   4856  CD  LYS C 216       3.229  -6.480  43.361  1.00 82.63           C  
-ANISOU 4856  CD  LYS C 216    11802  13712   5881  -1394  -1294   1274       C  
-ATOM   4857  CE  LYS C 216       2.787  -5.052  43.649  1.00 85.85           C  
-ANISOU 4857  CE  LYS C 216    12500  14141   5980  -1387  -1093    718       C  
-ATOM   4858  NZ  LYS C 216       1.475  -5.002  44.353  1.00 90.15           N  
-ANISOU 4858  NZ  LYS C 216    13292  14781   6179  -1200   -635    784       N  
-ATOM   4859  N   ALA C 217       6.764  -4.750  40.669  1.00 78.12           N  
-ANISOU 4859  N   ALA C 217    10503  12605   6573  -1897  -2229    437       N  
-ATOM   4860  CA  ALA C 217       8.163  -4.827  41.064  1.00 87.35           C  
-ANISOU 4860  CA  ALA C 217    11459  13836   7892  -1946  -2699    466       C  
-ATOM   4861  C   ALA C 217       8.296  -4.931  42.577  1.00 98.36           C  
-ANISOU 4861  C   ALA C 217    13093  15541   8738  -1873  -2922    514       C  
-ATOM   4862  O   ALA C 217       7.671  -4.174  43.320  1.00102.33           O  
-ANISOU 4862  O   ALA C 217    13956  16158   8767  -1851  -2781    215       O  
-ATOM   4863  CB  ALA C 217       8.928  -3.622  40.540  1.00 86.57           C  
-ANISOU 4863  CB  ALA C 217    11244  13540   8109  -2110  -2807     12       C  
-ATOM   4864  OXT ALA C 217       9.038  -5.771  43.090  1.00104.60           O  
-ANISOU 4864  OXT ALA C 217    13727  16465   9551  -1809  -3241    850       O  
-TER    4865      ALA C 217                                                      
-ATOM   4866  N   SER D   4     -19.172 -16.669  17.512  1.00 59.28           N  
-ANISOU 4866  N   SER D   4     9750   5310   7462  -1899  -1688    880       N  
-ATOM   4867  CA  SER D   4     -18.826 -15.245  17.570  1.00 59.00           C  
-ANISOU 4867  CA  SER D   4     9325   5571   7522  -1711  -1497    792       C  
-ATOM   4868  C   SER D   4     -19.710 -14.397  16.655  1.00 58.71           C  
-ANISOU 4868  C   SER D   4     8828   5837   7641  -1705  -1201    668       C  
-ATOM   4869  O   SER D   4     -19.670 -14.540  15.428  1.00 58.39           O  
-ANISOU 4869  O   SER D   4     8596   5810   7780  -1509  -1242    585       O  
-ATOM   4870  CB  SER D   4     -17.351 -15.031  17.218  1.00 56.05           C  
-ANISOU 4870  CB  SER D   4     8882   5137   7279  -1269  -1723    730       C  
-ATOM   4871  OG  SER D   4     -17.012 -13.654  17.222  1.00 56.21           O  
-ANISOU 4871  OG  SER D   4     8555   5432   7372  -1123  -1534    642       O  
-ATOM   4872  N   PRO D   5     -20.515 -13.504  17.252  1.00 54.28           N  
-ANISOU 4872  N   PRO D   5     8089   5527   7009  -1912   -909    646       N  
-ATOM   4873  CA  PRO D   5     -21.354 -12.624  16.435  1.00 50.89           C  
-ANISOU 4873  CA  PRO D   5     7224   5384   6730  -1862   -651    526       C  
-ATOM   4874  C   PRO D   5     -20.563 -11.418  15.944  1.00 46.84           C  
-ANISOU 4874  C   PRO D   5     6419   4991   6388  -1501   -611    441       C  
-ATOM   4875  O   PRO D   5     -21.144 -10.538  15.297  1.00 43.86           O  
-ANISOU 4875  O   PRO D   5     5702   4827   6136  -1416   -420    352       O  
-ATOM   4876  CB  PRO D   5     -22.430 -12.172  17.420  1.00 52.28           C  
-ANISOU 4876  CB  PRO D   5     7356   5765   6743  -2206   -379    514       C  
-ATOM   4877  CG  PRO D   5     -21.717 -12.158  18.740  1.00 49.94           C  
-ANISOU 4877  CG  PRO D   5     7359   5353   6265  -2303   -456    603       C  
-ATOM   4878  CD  PRO D   5     -20.754 -13.318  18.696  1.00 50.10           C  
-ANISOU 4878  CD  PRO D   5     7758   5032   6247  -2211   -810    719       C  
-ATOM   4879  N   GLY D   6     -19.266 -11.376  16.258  1.00 39.33           N  
-ANISOU 4879  N   GLY D   6     5608   3911   5426  -1303   -798    465       N  
-ATOM   4880  CA  GLY D   6     -18.413 -10.258  15.891  1.00 32.34           C  
-ANISOU 4880  CA  GLY D   6     4488   3143   4655  -1016   -765    381       C  
-ATOM   4881  C   GLY D   6     -18.439  -9.127  16.905  1.00 32.16           C  
-ANISOU 4881  C   GLY D   6     4417   3261   4542  -1099   -563    368       C  
-ATOM   4882  O   GLY D   6     -18.930  -9.294  18.020  1.00 33.86           O  
-ANISOU 4882  O   GLY D   6     4805   3472   4587  -1368   -481    428       O  
-ATOM   4883  N   VAL D   7     -17.890  -7.980  16.530  1.00 30.33           N  
-ANISOU 4883  N   VAL D   7     3969   3151   4405   -891   -481    284       N  
-ATOM   4884  CA  VAL D   7     -17.969  -6.794  17.377  1.00 30.82           C  
-ANISOU 4884  CA  VAL D   7     3970   3340   4399   -957   -264    247       C  
-ATOM   4885  C   VAL D   7     -19.417  -6.300  17.367  1.00 35.29           C  
-ANISOU 4885  C   VAL D   7     4356   4052   5002  -1097      3    200       C  
-ATOM   4886  O   VAL D   7     -19.941  -5.905  16.324  1.00 29.67           O  
-ANISOU 4886  O   VAL D   7     3404   3422   4447   -964     73    142       O  
-ATOM   4887  CB  VAL D   7     -17.056  -5.678  16.891  1.00 30.17           C  
-ANISOU 4887  CB  VAL D   7     3729   3334   4399   -723   -241    163       C  
-ATOM   4888  CG1 VAL D   7     -17.229  -4.442  17.771  1.00 31.66           C  
-ANISOU 4888  CG1 VAL D   7     3883   3629   4518   -807     -3    114       C  
-ATOM   4889  CG2 VAL D   7     -15.607  -6.128  16.909  1.00 28.64           C  
-ANISOU 4889  CG2 VAL D   7     3660   3065   4157   -582   -497    168       C  
-ATOM   4890  N   VAL D   8     -20.066  -6.344  18.525  1.00 36.39           N  
-ANISOU 4890  N   VAL D   8     4601   4240   4984  -1370    142    214       N  
-ATOM   4891  CA  VAL D   8     -21.473  -5.961  18.616  1.00 34.80           C  
-ANISOU 4891  CA  VAL D   8     4207   4220   4796  -1517    395    134       C  
-ATOM   4892  C   VAL D   8     -21.599  -4.457  18.844  1.00 36.70           C  
-ANISOU 4892  C   VAL D   8     4253   4595   5098  -1397    622     14       C  
-ATOM   4893  O   VAL D   8     -21.069  -3.919  19.815  1.00 36.95           O  
-ANISOU 4893  O   VAL D   8     4399   4622   5017  -1461    685      1       O  
-ATOM   4894  CB  VAL D   8     -22.186  -6.729  19.735  1.00 37.79           C  
-ANISOU 4894  CB  VAL D   8     4777   4626   4954  -1910    459    174       C  
-ATOM   4895  CG1 VAL D   8     -23.615  -6.232  19.897  1.00 42.17           C  
-ANISOU 4895  CG1 VAL D   8     5079   5437   5508  -2063    744     39       C  
-ATOM   4896  CG2 VAL D   8     -22.186  -8.220  19.434  1.00 38.62           C  
-ANISOU 4896  CG2 VAL D   8     5112   4564   4998  -2041    235    293       C  
-ATOM   4897  N   ILE D   9     -22.277  -3.777  17.926  1.00 34.72           N  
-ANISOU 4897  N   ILE D   9     3723   4449   5020  -1215    728    -74       N  
-ATOM   4898  CA  ILE D   9     -22.562  -2.355  18.078  1.00 34.94           C  
-ANISOU 4898  CA  ILE D   9     3583   4574   5119  -1080    935   -197       C  
-ATOM   4899  C   ILE D   9     -24.022  -2.217  18.516  1.00 36.33           C  
-ANISOU 4899  C   ILE D   9     3572   4958   5273  -1230   1159   -318       C  
-ATOM   4900  O   ILE D   9     -24.935  -2.717  17.851  1.00 36.60           O  
-ANISOU 4900  O   ILE D   9     3437   5101   5370  -1246   1158   -338       O  
-ATOM   4901  CB  ILE D   9     -22.261  -1.606  16.782  1.00 34.54           C  
-ANISOU 4901  CB  ILE D   9     3379   4483   5263   -757    875   -212       C  
-ATOM   4902  CG1 ILE D   9     -20.769  -1.717  16.486  1.00 38.06           C  
-ANISOU 4902  CG1 ILE D   9     3991   4779   5690   -658    678   -133       C  
-ATOM   4903  CG2 ILE D   9     -22.684  -0.137  16.871  1.00 35.11           C  
-ANISOU 4903  CG2 ILE D   9     3311   4614   5416   -600   1071   -337       C  
-ATOM   4904  CD1 ILE D   9     -20.341  -1.040  15.228  1.00 41.61           C  
-ANISOU 4904  CD1 ILE D   9     4328   5197   6284   -404    610   -145       C  
-ATOM   4905  N   SER D  10     -24.243  -1.589  19.666  1.00 35.75           N  
-ANISOU 4905  N   SER D  10     3522   4970   5093  -1362   1354   -418       N  
-ATOM   4906  CA  SER D  10     -25.569  -1.577  20.271  1.00 40.25           C  
-ANISOU 4906  CA  SER D  10     3919   5779   5595  -1561   1575   -565       C  
-ATOM   4907  C   SER D  10     -26.498  -0.624  19.533  1.00 38.78           C  
-ANISOU 4907  C   SER D  10     3392   5736   5607  -1282   1703   -726       C  
-ATOM   4908  O   SER D  10     -26.042   0.233  18.772  1.00 37.48           O  
-ANISOU 4908  O   SER D  10     3182   5450   5608   -955   1645   -718       O  
-ATOM   4909  CB  SER D  10     -25.492  -1.184  21.744  1.00 45.76           C  
-ANISOU 4909  CB  SER D  10     4739   6541   6105  -1799   1752   -646       C  
-ATOM   4910  OG  SER D  10     -24.960   0.116  21.866  1.00 50.33           O  
-ANISOU 4910  OG  SER D  10     5303   7050   6770  -1566   1837   -726       O  
-ATOM   4911  N   ASP D  11     -27.795  -0.787  19.770  1.00 42.46           N  
-ANISOU 4911  N   ASP D  11     3625   6468   6038  -1423   1865   -876       N  
-ATOM   4912  CA  ASP D  11     -28.821   0.059  19.174  1.00 49.43           C  
-ANISOU 4912  CA  ASP D  11     4151   7533   7095  -1153   1980  -1058       C  
-ATOM   4913  C   ASP D  11     -28.616   1.539  19.500  1.00 54.89           C  
-ANISOU 4913  C   ASP D  11     4813   8157   7886   -883   2105  -1191       C  
-ATOM   4914  O   ASP D  11     -28.920   2.414  18.689  1.00 58.40           O  
-ANISOU 4914  O   ASP D  11     5091   8577   8523   -519   2083  -1253       O  
-ATOM   4915  CB  ASP D  11     -30.200  -0.385  19.660  1.00 51.42           C  
-ANISOU 4915  CB  ASP D  11     4226   8094   7217  -1369   2097  -1203       C  
-ATOM   4916  CG  ASP D  11     -30.644  -1.687  19.035  1.00 54.82           C  
-ANISOU 4916  CG  ASP D  11     4636   8604   7589  -1566   1977  -1102       C  
-ATOM   4917  OD1 ASP D  11     -29.994  -2.135  18.069  1.00 55.27           O  
-ANISOU 4917  OD1 ASP D  11     4733   8510   7759  -1486   1823   -954       O  
-ATOM   4918  OD2 ASP D  11     -31.645  -2.253  19.501  1.00 55.10           O  
-ANISOU 4918  OD2 ASP D  11     4622   8852   7461  -1807   2036  -1186       O  
-ATOM   4919  N   ASP D  12     -28.078   1.809  20.683  1.00 52.39           N  
-ANISOU 4919  N   ASP D  12     4694   7790   7424  -1069   2217  -1222       N  
-ATOM   4920  CA  ASP D  12     -27.983   3.172  21.173  1.00 54.22           C  
-ANISOU 4920  CA  ASP D  12     4912   7974   7715   -878   2374  -1384       C  
-ATOM   4921  C   ASP D  12     -26.589   3.796  21.020  1.00 52.18           C  
-ANISOU 4921  C   ASP D  12     4934   7407   7486   -730   2261  -1248       C  
-ATOM   4922  O   ASP D  12     -26.328   4.874  21.552  1.00 53.40           O  
-ANISOU 4922  O   ASP D  12     5156   7484   7648   -637   2390  -1364       O  
-ATOM   4923  CB  ASP D  12     -28.487   3.246  22.620  1.00 59.22           C  
-ANISOU 4923  CB  ASP D  12     5586   8775   8142  -1153   2543  -1533       C  
-ATOM   4924  CG  ASP D  12     -29.956   2.825  22.752  1.00 68.69           C  
-ANISOU 4924  CG  ASP D  12     6553  10262   9284  -1241   2579  -1665       C  
-ATOM   4925  OD1 ASP D  12     -30.822   3.517  22.180  1.00 72.87           O  
-ANISOU 4925  OD1 ASP D  12     6844  10877   9968   -926   2581  -1791       O  
-ATOM   4926  OD2 ASP D  12     -30.250   1.810  23.429  1.00 70.92           O  
-ANISOU 4926  OD2 ASP D  12     6913  10681   9352  -1627   2591  -1638       O  
-ATOM   4927  N   GLU D  13     -25.702   3.129  20.284  1.00 47.37           N  
-ANISOU 4927  N   GLU D  13     4480   6636   6884   -717   2027  -1025       N  
-ATOM   4928  CA  GLU D  13     -24.374   3.683  20.008  1.00 46.17           C  
-ANISOU 4928  CA  GLU D  13     4553   6241   6748   -588   1911   -916       C  
-ATOM   4929  C   GLU D  13     -24.493   4.995  19.234  1.00 50.20           C  
-ANISOU 4929  C   GLU D  13     4990   6641   7442   -231   1935   -994       C  
-ATOM   4930  O   GLU D  13     -25.084   5.034  18.154  1.00 53.60           O  
-ANISOU 4930  O   GLU D  13     5247   7089   8030    -10   1851   -981       O  
-ATOM   4931  CB  GLU D  13     -23.510   2.691  19.223  1.00 46.82           C  
-ANISOU 4931  CB  GLU D  13     4752   6216   6820   -608   1651   -705       C  
-ATOM   4932  CG  GLU D  13     -22.308   3.319  18.496  1.00 52.17           C  
-ANISOU 4932  CG  GLU D  13     5566   6703   7555   -416   1517   -624       C  
-ATOM   4933  CD  GLU D  13     -21.184   3.752  19.431  1.00 58.03           C  
-ANISOU 4933  CD  GLU D  13     6541   7366   8144   -542   1553   -624       C  
-ATOM   4934  OE1 GLU D  13     -20.842   2.984  20.357  1.00 65.03           O  
-ANISOU 4934  OE1 GLU D  13     7550   8296   8863   -789   1534   -577       O  
-ATOM   4935  OE2 GLU D  13     -20.638   4.860  19.235  1.00 58.35           O  
-ANISOU 4935  OE2 GLU D  13     6657   7299   8216   -408   1592   -668       O  
-ATOM   4936  N   PRO D  14     -23.935   6.079  19.797  1.00 52.49           N  
-ANISOU 4936  N   PRO D  14     5435   6807   7700   -188   2043  -1071       N  
-ATOM   4937  CA  PRO D  14     -23.954   7.432  19.222  1.00 53.65           C  
-ANISOU 4937  CA  PRO D  14     5604   6790   7989    121   2069  -1146       C  
-ATOM   4938  C   PRO D  14     -22.959   7.649  18.072  1.00 48.11           C  
-ANISOU 4938  C   PRO D  14     5053   5891   7334    256   1863   -980       C  
-ATOM   4939  O   PRO D  14     -23.084   8.648  17.357  1.00 51.35           O  
-ANISOU 4939  O   PRO D  14     5492   6154   7864    511   1840  -1006       O  
-ATOM   4940  CB  PRO D  14     -23.572   8.318  20.417  1.00 51.33           C  
-ANISOU 4940  CB  PRO D  14     5480   6438   7586     16   2266  -1284       C  
-ATOM   4941  CG  PRO D  14     -22.689   7.441  21.247  1.00 51.69           C  
-ANISOU 4941  CG  PRO D  14     5679   6543   7418   -329   2237  -1180       C  
-ATOM   4942  CD  PRO D  14     -23.274   6.049  21.116  1.00 52.76           C  
-ANISOU 4942  CD  PRO D  14     5661   6853   7533   -468   2149  -1096       C  
-ATOM   4943  N   GLY D  15     -22.001   6.742  17.886  1.00 42.41           N  
-ANISOU 4943  N   GLY D  15     4431   5169   6514     89   1708   -823       N  
-ATOM   4944  CA  GLY D  15     -20.959   6.954  16.898  1.00 38.66           C  
-ANISOU 4944  CA  GLY D  15     4087   4555   6049    170   1535   -705       C  
-ATOM   4945  C   GLY D  15     -20.038   8.080  17.340  1.00 42.57           C  
-ANISOU 4945  C   GLY D  15     4820   4906   6449    137   1616   -755       C  
-ATOM   4946  O   GLY D  15     -20.003   8.425  18.525  1.00 44.58           O  
-ANISOU 4946  O   GLY D  15     5154   5181   6604      4   1783   -857       O  
-ATOM   4947  N   TYR D  16     -19.303   8.670  16.399  1.00 41.01           N  
-ANISOU 4947  N   TYR D  16     4744   4575   6261    226   1507   -694       N  
-ATOM   4948  CA  TYR D  16     -18.401   9.773  16.733  1.00 39.17           C  
-ANISOU 4948  CA  TYR D  16     4762   4205   5915    159   1583   -746       C  
-ATOM   4949  C   TYR D  16     -18.696  11.043  15.944  1.00 40.46           C  
-ANISOU 4949  C   TYR D  16     5042   4155   6174    370   1590   -771       C  
-ATOM   4950  O   TYR D  16     -19.025  10.982  14.752  1.00 35.14           O  
-ANISOU 4950  O   TYR D  16     4298   3443   5612    535   1446   -686       O  
-ATOM   4951  CB  TYR D  16     -16.951   9.374  16.475  1.00 38.94           C  
-ANISOU 4951  CB  TYR D  16     4840   4224   5732    -15   1448   -665       C  
-ATOM   4952  CG  TYR D  16     -16.475   8.165  17.239  1.00 36.98           C  
-ANISOU 4952  CG  TYR D  16     4532   4147   5373   -199   1395   -631       C  
-ATOM   4953  CD1 TYR D  16     -16.701   6.886  16.758  1.00 34.75           C  
-ANISOU 4953  CD1 TYR D  16     4089   3961   5152   -173   1237   -540       C  
-ATOM   4954  CD2 TYR D  16     -15.779   8.306  18.432  1.00 44.52           C  
-ANISOU 4954  CD2 TYR D  16     5615   5152   6149   -400   1487   -686       C  
-ATOM   4955  CE1 TYR D  16     -16.255   5.779  17.448  1.00 37.89           C  
-ANISOU 4955  CE1 TYR D  16     4484   4469   5444   -325   1159   -498       C  
-ATOM   4956  CE2 TYR D  16     -15.330   7.204  19.131  1.00 42.03           C  
-ANISOU 4956  CE2 TYR D  16     5276   4974   5721   -554   1404   -637       C  
-ATOM   4957  CZ  TYR D  16     -15.569   5.946  18.630  1.00 38.21           C  
-ANISOU 4957  CZ  TYR D  16     4660   4550   5308   -506   1232   -540       C  
-ATOM   4958  OH  TYR D  16     -15.134   4.840  19.316  1.00 39.68           O  
-ANISOU 4958  OH  TYR D  16     4869   4827   5379   -641   1121   -482       O  
-ATOM   4959  N   ASP D  17     -18.561  12.182  16.627  1.00 39.37           N  
-ANISOU 4959  N   ASP D  17     5108   3870   5980    352   1749   -885       N  
-ATOM   4960  CA  ASP D  17     -18.590  13.513  16.019  1.00 42.56           C  
-ANISOU 4960  CA  ASP D  17     5737   4008   6426    510   1749   -907       C  
-ATOM   4961  C   ASP D  17     -17.614  13.550  14.845  1.00 40.17           C  
-ANISOU 4961  C   ASP D  17     5568   3654   6042    435   1567   -769       C  
-ATOM   4962  O   ASP D  17     -16.450  13.187  14.998  1.00 33.77           O  
-ANISOU 4962  O   ASP D  17     4819   2955   5057    186   1537   -740       O  
-ATOM   4963  CB  ASP D  17     -18.169  14.548  17.071  1.00 47.71           C  
-ANISOU 4963  CB  ASP D  17     6644   4526   6956    387   1947  -1047       C  
-ATOM   4964  CG  ASP D  17     -18.356  15.986  16.616  1.00 54.33           C  
-ANISOU 4964  CG  ASP D  17     7764   5036   7843    563   1966  -1095       C  
-ATOM   4965  OD1 ASP D  17     -18.270  16.276  15.405  1.00 55.62           O  
-ANISOU 4965  OD1 ASP D  17     8026   5062   8046    675   1797   -976       O  
-ATOM   4966  OD2 ASP D  17     -18.570  16.851  17.492  1.00 60.89           O  
-ANISOU 4966  OD2 ASP D  17     8745   5731   8659    578   2147  -1254       O  
-ATOM   4967  N   LEU D  18     -18.083  14.015  13.688  1.00 41.80           N  
-ANISOU 4967  N   LEU D  18     5815   3709   6359    644   1441   -696       N  
-ATOM   4968  CA  LEU D  18     -17.263  14.082  12.473  1.00 39.97           C  
-ANISOU 4968  CA  LEU D  18     5707   3441   6039    556   1268   -570       C  
-ATOM   4969  C   LEU D  18     -16.022  14.962  12.669  1.00 35.94           C  
-ANISOU 4969  C   LEU D  18     5536   2819   5302    300   1326   -603       C  
-ATOM   4970  O   LEU D  18     -14.983  14.735  12.049  1.00 35.39           O  
-ANISOU 4970  O   LEU D  18     5517   2849   5079     92   1229   -548       O  
-ATOM   4971  CB  LEU D  18     -18.097  14.626  11.303  1.00 42.98           C  
-ANISOU 4971  CB  LEU D  18     6125   3642   6563    827   1131   -489       C  
-ATOM   4972  CG  LEU D  18     -19.328  13.827  10.855  1.00 46.00           C  
-ANISOU 4972  CG  LEU D  18     6164   4160   7154   1078   1045   -452       C  
-ATOM   4973  CD1 LEU D  18     -20.208  14.652   9.911  1.00 46.14           C  
-ANISOU 4973  CD1 LEU D  18     6260   3967   7304   1385    923   -399       C  
-ATOM   4974  CD2 LEU D  18     -18.923  12.520  10.197  1.00 40.94           C  
-ANISOU 4974  CD2 LEU D  18     5299   3769   6487    944    913   -354       C  
-ATOM   4975  N   ASP D  19     -16.131  15.956  13.545  1.00 36.78           N  
-ANISOU 4975  N   ASP D  19     5862   2737   5374    298   1495   -717       N  
-ATOM   4976  CA  ASP D  19     -15.041  16.906  13.752  1.00 42.66           C  
-ANISOU 4976  CA  ASP D  19     6963   3354   5892     38   1569   -762       C  
-ATOM   4977  C   ASP D  19     -13.793  16.302  14.401  1.00 39.82           C  
-ANISOU 4977  C   ASP D  19     6544   3270   5315   -300   1618   -804       C  
-ATOM   4978  O   ASP D  19     -12.732  16.926  14.422  1.00 43.18           O  
-ANISOU 4978  O   ASP D  19     7214   3676   5516   -568   1655   -841       O  
-ATOM   4979  CB  ASP D  19     -15.539  18.097  14.574  1.00 46.88           C  
-ANISOU 4979  CB  ASP D  19     7751   3607   6456    133   1745   -893       C  
-ATOM   4980  CG  ASP D  19     -16.561  18.914  13.830  1.00 57.46           C  
-ANISOU 4980  CG  ASP D  19     9230   4628   7974    475   1662   -860       C  
-ATOM   4981  OD1 ASP D  19     -16.350  19.149  12.622  1.00 58.12           O  
-ANISOU 4981  OD1 ASP D  19     9457   4599   8026    484   1484   -723       O  
-ATOM   4982  OD2 ASP D  19     -17.577  19.307  14.445  1.00 63.88           O  
-ANISOU 4982  OD2 ASP D  19    10000   5319   8952    736   1764   -979       O  
-ATOM   4983  N   LEU D  20     -13.938  15.090  14.920  1.00 36.89           N  
-ANISOU 4983  N   LEU D  20     5858   3157   5002   -289   1605   -802       N  
-ATOM   4984  CA  LEU D  20     -12.872  14.396  15.623  1.00 39.18           C  
-ANISOU 4984  CA  LEU D  20     6065   3712   5110   -548   1618   -839       C  
-ATOM   4985  C   LEU D  20     -12.010  13.633  14.632  1.00 43.28           C  
-ANISOU 4985  C   LEU D  20     6461   4429   5555   -639   1424   -765       C  
-ATOM   4986  O   LEU D  20     -10.939  13.144  14.978  1.00 29.96           O  
-ANISOU 4986  O   LEU D  20     4717   2971   3697   -841   1393   -807       O  
-ATOM   4987  CB  LEU D  20     -13.464  13.416  16.637  1.00 40.11           C  
-ANISOU 4987  CB  LEU D  20     5943   3986   5313   -494   1670   -859       C  
-ATOM   4988  CG  LEU D  20     -14.263  14.080  17.756  1.00 45.50           C  
-ANISOU 4988  CG  LEU D  20     6703   4543   6042   -446   1885   -974       C  
-ATOM   4989  CD1 LEU D  20     -15.074  13.056  18.541  1.00 44.96           C  
-ANISOU 4989  CD1 LEU D  20     6380   4636   6067   -394   1921   -982       C  
-ATOM   4990  CD2 LEU D  20     -13.323  14.835  18.676  1.00 47.89           C  
-ANISOU 4990  CD2 LEU D  20     7238   4842   6114   -713   2033  -1082       C  
-ATOM   4991  N   PHE D  21     -12.484  13.547  13.395  1.00 30.62           N  
-ANISOU 4991  N   PHE D  21     4807   2751   4075   -482   1289   -670       N  
-ATOM   4992  CA  PHE D  21     -11.816  12.757  12.379  1.00 29.09           C  
-ANISOU 4992  CA  PHE D  21     4464   2754   3837   -546   1108   -618       C  
-ATOM   4993  C   PHE D  21     -11.553  13.544  11.099  1.00 33.35           C  
-ANISOU 4993  C   PHE D  21     5191   3175   4305   -604   1028   -569       C  
-ATOM   4994  O   PHE D  21     -12.049  14.656  10.923  1.00 32.29           O  
-ANISOU 4994  O   PHE D  21     5316   2761   4192   -542   1083   -545       O  
-ATOM   4995  CB  PHE D  21     -12.649  11.515  12.072  1.00 27.99           C  
-ANISOU 4995  CB  PHE D  21     4021   2710   3905   -335    996   -542       C  
-ATOM   4996  CG  PHE D  21     -12.752  10.570  13.221  1.00 33.74           C  
-ANISOU 4996  CG  PHE D  21     4587   3578   4655   -340   1037   -574       C  
-ATOM   4997  CD1 PHE D  21     -11.816   9.564  13.384  1.00 37.64           C  
-ANISOU 4997  CD1 PHE D  21     4951   4301   5048   -453    930   -594       C  
-ATOM   4998  CD2 PHE D  21     -13.772  10.692  14.152  1.00 39.89           C  
-ANISOU 4998  CD2 PHE D  21     5353   4263   5541   -237   1174   -595       C  
-ATOM   4999  CE1 PHE D  21     -11.894   8.686  14.463  1.00 40.29           C  
-ANISOU 4999  CE1 PHE D  21     5188   4736   5383   -468    941   -601       C  
-ATOM   5000  CE2 PHE D  21     -13.859   9.823  15.229  1.00 46.07           C  
-ANISOU 5000  CE2 PHE D  21     6020   5176   6308   -292   1210   -615       C  
-ATOM   5001  CZ  PHE D  21     -12.920   8.814  15.382  1.00 45.58           C  
-ANISOU 5001  CZ  PHE D  21     5872   5308   6138   -410   1084   -601       C  
-ATOM   5002  N   CYS D  22     -10.740  12.965  10.218  1.00 34.50           N  
-ANISOU 5002  N   CYS D  22     5219   3535   4353   -732    891   -564       N  
-ATOM   5003  CA  CYS D  22     -10.502  13.549   8.907  1.00 34.41           C  
-ANISOU 5003  CA  CYS D  22     5360   3459   4256   -824    797   -511       C  
-ATOM   5004  C   CYS D  22     -11.587  13.011   7.987  1.00 33.11           C  
-ANISOU 5004  C   CYS D  22     5027   3233   4318   -559    664   -387       C  
-ATOM   5005  O   CYS D  22     -11.686  11.804   7.788  1.00 32.40           O  
-ANISOU 5005  O   CYS D  22     4636   3345   4331   -475    573   -381       O  
-ATOM   5006  CB  CYS D  22      -9.124  13.165   8.387  1.00 36.87           C  
-ANISOU 5006  CB  CYS D  22     5588   4082   4339  -1106    726   -601       C  
-ATOM   5007  N   ILE D  23     -12.397  13.911   7.432  1.00 30.82           N  
-ANISOU 5007  N   ILE D  23     4946   2663   4102   -426    642   -293       N  
-ATOM   5008  CA  ILE D  23     -13.550  13.538   6.603  1.00 31.65           C  
-ANISOU 5008  CA  ILE D  23     4899   2706   4423   -153    516   -176       C  
-ATOM   5009  C   ILE D  23     -13.434  14.237   5.249  1.00 32.18           C  
-ANISOU 5009  C   ILE D  23     5185   2654   4388   -234    382    -75       C  
-ATOM   5010  O   ILE D  23     -13.027  15.391   5.196  1.00 38.42           O  
-ANISOU 5010  O   ILE D  23     6344   3239   5016   -383    419    -70       O  
-ATOM   5011  CB  ILE D  23     -14.874  13.992   7.288  1.00 40.78           C  
-ANISOU 5011  CB  ILE D  23     6077   3628   5790    158    596   -162       C  
-ATOM   5012  CG1 ILE D  23     -15.028  13.336   8.668  1.00 35.64           C  
-ANISOU 5012  CG1 ILE D  23     5232   3102   5209    190    740   -264       C  
-ATOM   5013  CG2 ILE D  23     -16.093  13.707   6.410  1.00 38.33           C  
-ANISOU 5013  CG2 ILE D  23     5600   3279   5686    445    459    -55       C  
-ATOM   5014  CD1 ILE D  23     -15.066  11.813   8.637  1.00 32.06           C  
-ANISOU 5014  CD1 ILE D  23     4420   2930   4833    201    670   -257       C  
-ATOM   5015  N   PRO D  24     -13.788  13.544   4.151  1.00 32.74           N  
-ANISOU 5015  N   PRO D  24     5055   2848   4535   -162    225      8       N  
-ATOM   5016  CA  PRO D  24     -13.736  14.238   2.855  1.00 35.47           C  
-ANISOU 5016  CA  PRO D  24     5632   3078   4766   -255     87    119       C  
-ATOM   5017  C   PRO D  24     -14.676  15.435   2.831  1.00 37.25           C  
-ANISOU 5017  C   PRO D  24     6169   2912   5073    -30     62    222       C  
-ATOM   5018  O   PRO D  24     -15.842  15.305   3.208  1.00 37.80           O  
-ANISOU 5018  O   PRO D  24     6089   2889   5383    315     65    243       O  
-ATOM   5019  CB  PRO D  24     -14.190  13.167   1.848  1.00 33.29           C  
-ANISOU 5019  CB  PRO D  24     5031   3013   4605   -161    -64    182       C  
-ATOM   5020  CG  PRO D  24     -14.783  12.054   2.655  1.00 32.79           C  
-ANISOU 5020  CG  PRO D  24     4610   3091   4759     50     -6    125       C  
-ATOM   5021  CD  PRO D  24     -14.133  12.119   4.014  1.00 33.68           C  
-ANISOU 5021  CD  PRO D  24     4768   3221   4808    -47    164     -1       C  
-ATOM   5022  N   ASN D  25     -14.160  16.590   2.411  1.00 45.17           N  
-ANISOU 5022  N   ASN D  25     7607   3692   5866   -230     35    270       N  
-ATOM   5023  CA  ASN D  25     -14.918  17.833   2.414  1.00 54.25           C  
-ANISOU 5023  CA  ASN D  25     9134   4411   7066    -21     -6    359       C  
-ATOM   5024  C   ASN D  25     -16.246  17.751   1.680  1.00 51.87           C  
-ANISOU 5024  C   ASN D  25     8717   4001   6989    365   -187    494       C  
-ATOM   5025  O   ASN D  25     -17.219  18.407   2.059  1.00 55.38           O  
-ANISOU 5025  O   ASN D  25     9272   4165   7603    711   -199    509       O  
-ATOM   5026  CB  ASN D  25     -14.092  18.962   1.787  1.00 68.58           C  
-ANISOU 5026  CB  ASN D  25    11470   6012   8576   -360    -56    421       C  
-ATOM   5027  CG  ASN D  25     -12.768  19.185   2.495  1.00 78.77           C  
-ANISOU 5027  CG  ASN D  25    12898   7422   9610   -770    126    271       C  
-ATOM   5028  OD1 ASN D  25     -11.802  18.451   2.272  1.00 82.24           O  
-ANISOU 5028  OD1 ASN D  25    13118   8234   9894  -1069    152    188       O  
-ATOM   5029  ND2 ASN D  25     -12.713  20.208   3.343  1.00 80.85           N  
-ANISOU 5029  ND2 ASN D  25    13519   7381   9821   -780    250    219       N  
-ATOM   5030  N   HIS D  26     -16.283  16.967   0.611  1.00 43.39           N  
-ANISOU 5030  N   HIS D  26     7414   3164   5909    309   -333    575       N  
-ATOM   5031  CA  HIS D  26     -17.470  16.936  -0.231  1.00 45.02           C  
-ANISOU 5031  CA  HIS D  26     7526   3294   6283    631   -528    715       C  
-ATOM   5032  C   HIS D  26     -18.631  16.160   0.402  1.00 43.49           C  
-ANISOU 5032  C   HIS D  26     6897   3231   6397   1013   -479    650       C  
-ATOM   5033  O   HIS D  26     -19.769  16.257  -0.058  1.00 49.25           O  
-ANISOU 5033  O   HIS D  26     7529   3891   7291   1342   -618    731       O  
-ATOM   5034  CB  HIS D  26     -17.131  16.406  -1.631  1.00 42.57           C  
-ANISOU 5034  CB  HIS D  26     7135   3200   5840    410   -698    820       C  
-ATOM   5035  CG  HIS D  26     -16.587  15.010  -1.641  1.00 38.45           C  
-ANISOU 5035  CG  HIS D  26     6182   3105   5322    233   -628    711       C  
-ATOM   5036  ND1 HIS D  26     -15.244  14.729  -1.505  1.00 36.92           N  
-ANISOU 5036  ND1 HIS D  26     6000   3112   4915   -151   -527    593       N  
-ATOM   5037  CD2 HIS D  26     -17.208  13.815  -1.793  1.00 36.61           C  
-ANISOU 5037  CD2 HIS D  26     5505   3130   5276    394   -657    691       C  
-ATOM   5038  CE1 HIS D  26     -15.062  13.421  -1.564  1.00 34.35           C  
-ANISOU 5038  CE1 HIS D  26     5263   3126   4661   -182   -510    506       C  
-ATOM   5039  NE2 HIS D  26     -16.236  12.844  -1.741  1.00 37.94           N  
-ANISOU 5039  NE2 HIS D  26     5456   3606   5352    129   -583    570       N  
-ATOM   5040  N   TYR D  27     -18.337  15.399   1.456  1.00 40.66           N  
-ANISOU 5040  N   TYR D  27     6282   3075   6093    951   -289    502       N  
-ATOM   5041  CA  TYR D  27     -19.370  14.684   2.201  1.00 38.38           C  
-ANISOU 5041  CA  TYR D  27     5616   2916   6051   1240   -212    422       C  
-ATOM   5042  C   TYR D  27     -19.661  15.336   3.558  1.00 48.71           C  
-ANISOU 5042  C   TYR D  27     7030   4041   7436   1388    -30    296       C  
-ATOM   5043  O   TYR D  27     -20.472  14.825   4.326  1.00 46.29           O  
-ANISOU 5043  O   TYR D  27     6432   3852   7305   1584     67    201       O  
-ATOM   5044  CB  TYR D  27     -18.982  13.211   2.406  1.00 35.12           C  
-ANISOU 5044  CB  TYR D  27     4826   2867   5651   1073   -149    353       C  
-ATOM   5045  CG  TYR D  27     -19.008  12.381   1.143  1.00 38.60           C  
-ANISOU 5045  CG  TYR D  27     5066   3522   6079   1001   -315    441       C  
-ATOM   5046  CD1 TYR D  27     -19.959  12.609   0.153  1.00 38.28           C  
-ANISOU 5046  CD1 TYR D  27     4991   3431   6122   1209   -489    562       C  
-ATOM   5047  CD2 TYR D  27     -18.082  11.372   0.943  1.00 34.33           C  
-ANISOU 5047  CD2 TYR D  27     4367   3238   5439    736   -305    389       C  
-ATOM   5048  CE1 TYR D  27     -19.982  11.842  -0.996  1.00 35.65           C  
-ANISOU 5048  CE1 TYR D  27     4472   3309   5764   1118   -632    635       C  
-ATOM   5049  CE2 TYR D  27     -18.092  10.613  -0.196  1.00 30.88           C  
-ANISOU 5049  CE2 TYR D  27     3748   2997   4989    663   -443    443       C  
-ATOM   5050  CZ  TYR D  27     -19.039  10.854  -1.161  1.00 32.89           C  
-ANISOU 5050  CZ  TYR D  27     3975   3205   5316    836   -598    568       C  
-ATOM   5051  OH  TYR D  27     -19.034  10.086  -2.293  1.00 31.76           O  
-ANISOU 5051  OH  TYR D  27     3649   3273   5145    736   -727    613       O  
-ATOM   5052  N   ALA D  28     -19.013  16.468   3.831  1.00 52.51           N  
-ANISOU 5052  N   ALA D  28     7936   4243   7770   1268     21    285       N  
-ATOM   5053  CA  ALA D  28     -19.091  17.140   5.140  1.00 56.66           C  
-ANISOU 5053  CA  ALA D  28     8606   4591   8329   1344    214    145       C  
-ATOM   5054  C   ALA D  28     -20.483  17.233   5.783  1.00 53.97           C  
-ANISOU 5054  C   ALA D  28     8058   4203   8248   1763    264     52       C  
-ATOM   5055  O   ALA D  28     -20.673  16.790   6.912  1.00 54.51           O  
-ANISOU 5055  O   ALA D  28     7912   4415   8386   1772    449    -92       O  
-ATOM   5056  CB  ALA D  28     -18.451  18.522   5.071  1.00 59.61           C  
-ANISOU 5056  CB  ALA D  28     9528   4599   8523   1213    213    171       C  
-ATOM   5057  N   GLU D  29     -21.451  17.816   5.083  1.00 55.87           N  
-ANISOU 5057  N   GLU D  29     8355   4259   8615   2103     95    122       N  
-ATOM   5058  CA  GLU D  29     -22.792  17.943   5.654  1.00 58.92           C  
-ANISOU 5058  CA  GLU D  29     8501   4643   9241   2516    134     -4       C  
-ATOM   5059  C   GLU D  29     -23.755  16.849   5.194  1.00 52.03           C  
-ANISOU 5059  C   GLU D  29     7121   4125   8525   2664     44     10       C  
-ATOM   5060  O   GLU D  29     -24.963  16.941   5.407  1.00 56.14           O  
-ANISOU 5060  O   GLU D  29     7348   4753   9231   2883     50    -75       O  
-ATOM   5061  CB  GLU D  29     -23.383  19.338   5.409  1.00 71.11           C  
-ANISOU 5061  CB  GLU D  29    10275   5890  10854   2713     11      4       C  
-ATOM   5062  CG  GLU D  29     -22.797  20.413   6.327  1.00 81.64           C  
-ANISOU 5062  CG  GLU D  29    11991   6936  12093   2609    151   -109       C  
-ATOM   5063  CD  GLU D  29     -23.793  21.506   6.691  1.00 92.90           C  
-ANISOU 5063  CD  GLU D  29    13427   8176  13695   2907    129   -219       C  
-ATOM   5064  OE1 GLU D  29     -24.612  21.893   5.829  1.00 98.37           O  
-ANISOU 5064  OE1 GLU D  29    14069   8808  14498   3143    -48   -113       O  
-ATOM   5065  OE2 GLU D  29     -23.758  21.980   7.847  1.00 95.97           O  
-ANISOU 5065  OE2 GLU D  29    13877   8487  14102   2906    299   -415       O  
-ATOM   5066  N   ASP D  30     -23.210  15.805   4.579  1.00 49.20           N  
-ANISOU 5066  N   ASP D  30     6605   4008   8081   2420     -4    116       N  
-ATOM   5067  CA  ASP D  30     -24.021  14.704   4.072  1.00 47.34           C  
-ANISOU 5067  CA  ASP D  30     5928   4096   7963   2515    -82    139       C  
-ATOM   5068  C   ASP D  30     -24.015  13.539   5.056  1.00 50.49           C  
-ANISOU 5068  C   ASP D  30     5997   4798   8389   2351    113     13       C  
-ATOM   5069  O   ASP D  30     -24.771  12.577   4.906  1.00 50.45           O  
-ANISOU 5069  O   ASP D  30     5660   5120   8389   2360     88    -12       O  
-ATOM   5070  CB  ASP D  30     -23.490  14.231   2.710  1.00 45.91           C  
-ANISOU 5070  CB  ASP D  30     5768   4005   7670   2323   -276    320       C  
-ATOM   5071  CG  ASP D  30     -23.606  15.300   1.628  1.00 51.09           C  
-ANISOU 5071  CG  ASP D  30     6751   4382   8280   2465   -503    473       C  
-ATOM   5072  OD1 ASP D  30     -24.606  16.055   1.630  1.00 52.25           O  
-ANISOU 5072  OD1 ASP D  30     6904   4429   8518   2758   -524    473       O  
-ATOM   5073  OD2 ASP D  30     -22.692  15.382   0.776  1.00 50.94           O  
-ANISOU 5073  OD2 ASP D  30     6962   4318   8075   2190   -606    602       O  
-ATOM   5074  N   LEU D  31     -23.146  13.623   6.057  1.00 48.21           N  
-ANISOU 5074  N   LEU D  31     5865   4455   7995   2127    290    -67       N  
-ATOM   5075  CA  LEU D  31     -23.019  12.555   7.041  1.00 38.51           C  
-ANISOU 5075  CA  LEU D  31     4394   3478   6759   1942    455   -166       C  
-ATOM   5076  C   LEU D  31     -23.452  13.094   8.395  1.00 43.32           C  
-ANISOU 5076  C   LEU D  31     5020   4021   7419   2040    663   -344       C  
-ATOM   5077  O   LEU D  31     -23.461  14.305   8.609  1.00 51.47           O  
-ANISOU 5077  O   LEU D  31     6320   4782   8456   2181    692   -391       O  
-ATOM   5078  CB  LEU D  31     -21.582  12.054   7.101  1.00 38.64           C  
-ANISOU 5078  CB  LEU D  31     4545   3544   6591   1580    473   -118       C  
-ATOM   5079  CG  LEU D  31     -21.022  11.468   5.801  1.00 37.60           C  
-ANISOU 5079  CG  LEU D  31     4385   3512   6390   1445    288     18       C  
-ATOM   5080  CD1 LEU D  31     -19.519  11.262   5.910  1.00 33.20           C  
-ANISOU 5080  CD1 LEU D  31     3991   2988   5637   1119    311     17       C  
-ATOM   5081  CD2 LEU D  31     -21.714  10.157   5.476  1.00 39.39           C  
-ANISOU 5081  CD2 LEU D  31     4240   4008   6719   1475    234     31       C  
-ATOM   5082  N   GLU D  32     -23.828  12.199   9.301  1.00 42.49           N  
-ANISOU 5082  N   GLU D  32     4647   4157   7340   1951    804   -448       N  
-ATOM   5083  CA AGLU D  32     -24.267  12.622  10.627  0.58 47.68           C  
-ANISOU 5083  CA AGLU D  32     5287   4805   8023   2000   1017   -638       C  
-ATOM   5084  CA BGLU D  32     -24.288  12.584  10.631  0.42 47.97           C  
-ANISOU 5084  CA BGLU D  32     5313   4853   8061   1997   1017   -638       C  
-ATOM   5085  C   GLU D  32     -23.208  12.292  11.676  1.00 45.10           C  
-ANISOU 5085  C   GLU D  32     5094   4506   7534   1664   1167   -669       C  
-ATOM   5086  O   GLU D  32     -22.857  13.146  12.491  1.00 44.52           O  
-ANISOU 5086  O   GLU D  32     5240   4272   7402   1632   1304   -768       O  
-ATOM   5087  CB AGLU D  32     -25.603  11.973  11.004  0.58 51.08           C  
-ANISOU 5087  CB AGLU D  32     5370   5564   8474   2075   1040   -740       C  
-ATOM   5088  CB BGLU D  32     -25.556  11.798  10.970  0.42 50.63           C  
-ANISOU 5088  CB BGLU D  32     5291   5532   8415   2044   1036   -727       C  
-ATOM   5089  CG AGLU D  32     -26.369  12.707  12.103  0.58 57.10           C  
-ANISOU 5089  CG AGLU D  32     6113   6343   9239   2206   1198   -947       C  
-ATOM   5090  CG BGLU D  32     -26.595  12.558  11.767  0.42 57.32           C  
-ANISOU 5090  CG BGLU D  32     6081   6422   9275   2246   1139   -915       C  
-ATOM   5091  CD AGLU D  32     -27.214  13.855  11.571  0.58 62.65           C  
-ANISOU 5091  CD AGLU D  32     6893   6931   9981   2582   1076   -982       C  
-ATOM   5092  CD BGLU D  32     -27.986  11.970  11.594  0.42 62.19           C  
-ANISOU 5092  CD BGLU D  32     6361   7372   9896   2363   1103   -956       C  
-ATOM   5093  OE1AGLU D  32     -26.669  14.962  11.387  0.58 63.21           O  
-ANISOU 5093  OE1AGLU D  32     7293   6668  10057   2689   1028   -970       O  
-ATOM   5094  OE1BGLU D  32     -28.945  12.754  11.429  0.42 68.16           O  
-ANISOU 5094  OE1BGLU D  32     7082   8135  10679   2664   1071  -1014       O  
-ATOM   5095  OE2AGLU D  32     -28.425  13.650  11.335  0.58 69.27           O  
-ANISOU 5095  OE2AGLU D  32     7482   8005  10833   2766   1037  -1009       O  
-ATOM   5096  OE2BGLU D  32     -28.117  10.726  11.614  0.42 60.57           O  
-ANISOU 5096  OE2BGLU D  32     5942   7411   9660   2148   1117   -917       O  
-ATOM   5097  N   ARG D  33     -22.697  11.062  11.646  1.00 41.49           N  
-ANISOU 5097  N   ARG D  33     4517   4248   6999   1422   1126   -589       N  
-ATOM   5098  CA  ARG D  33     -21.700  10.596  12.612  1.00 41.35           C  
-ANISOU 5098  CA  ARG D  33     4601   4288   6821   1120   1225   -607       C  
-ATOM   5099  C   ARG D  33     -20.781   9.585  11.950  1.00 37.23           C  
-ANISOU 5099  C   ARG D  33     4062   3868   6215    935   1070   -472       C  
-ATOM   5100  O   ARG D  33     -21.172   8.936  10.981  1.00 40.49           O  
-ANISOU 5100  O   ARG D  33     4307   4371   6705   1006    930   -391       O  
-ATOM   5101  CB  ARG D  33     -22.378   9.885  13.794  1.00 44.47           C  
-ANISOU 5101  CB  ARG D  33     4798   4881   7219   1028   1382   -720       C  
-ATOM   5102  CG  ARG D  33     -23.529  10.624  14.461  1.00 51.56           C  
-ANISOU 5102  CG  ARG D  33     5595   5777   8218   1218   1548   -903       C  
-ATOM   5103  CD  ARG D  33     -23.027  11.753  15.339  1.00 55.25           C  
-ANISOU 5103  CD  ARG D  33     6326   6056   8611   1188   1703  -1015       C  
-ATOM   5104  NE  ARG D  33     -22.411  11.245  16.561  1.00 57.19           N  
-ANISOU 5104  NE  ARG D  33     6624   6415   8692    874   1838  -1056       N  
-ATOM   5105  CZ  ARG D  33     -21.957  12.012  17.547  1.00 56.97           C  
-ANISOU 5105  CZ  ARG D  33     6794   6290   8562    768   2002  -1169       C  
-ATOM   5106  NH1 ARG D  33     -22.038  13.331  17.454  1.00 55.82           N  
-ANISOU 5106  NH1 ARG D  33     6835   5905   8469    952   2058  -1259       N  
-ATOM   5107  NH2 ARG D  33     -21.415  11.454  18.622  1.00 55.27           N  
-ANISOU 5107  NH2 ARG D  33     6611   6205   8183    472   2099  -1188       N  
-ATOM   5108  N   VAL D  34     -19.567   9.433  12.477  1.00 30.92           N  
-ANISOU 5108  N   VAL D  34     3421   3074   5254    703   1091   -467       N  
-ATOM   5109  CA  VAL D  34     -18.752   8.282  12.125  1.00 31.63           C  
-ANISOU 5109  CA  VAL D  34     3446   3303   5269    542    958   -389       C  
-ATOM   5110  C   VAL D  34     -19.268   7.135  12.992  1.00 35.34           C  
-ANISOU 5110  C   VAL D  34     3750   3929   5749    457   1006   -410       C  
-ATOM   5111  O   VAL D  34     -19.467   7.303  14.194  1.00 33.23           O  
-ANISOU 5111  O   VAL D  34     3520   3675   5431    378   1162   -492       O  
-ATOM   5112  CB  VAL D  34     -17.252   8.519  12.390  1.00 33.59           C  
-ANISOU 5112  CB  VAL D  34     3895   3538   5330    342    946   -398       C  
-ATOM   5113  CG1 VAL D  34     -16.480   7.223  12.241  1.00 30.32           C  
-ANISOU 5113  CG1 VAL D  34     3381   3289   4851    216    808   -357       C  
-ATOM   5114  CG2 VAL D  34     -16.699   9.539  11.423  1.00 33.67           C  
-ANISOU 5114  CG2 VAL D  34     4085   3416   5292    358    887   -371       C  
-ATOM   5115  N   PHE D  35     -19.503   5.976  12.386  1.00 35.37           N  
-ANISOU 5115  N   PHE D  35     3589   4047   5803    450    876   -342       N  
-ATOM   5116  CA  PHE D  35     -20.148   4.873  13.090  1.00 33.52           C  
-ANISOU 5116  CA  PHE D  35     3225   3940   5571    352    911   -351       C  
-ATOM   5117  C   PHE D  35     -19.123   3.801  13.431  1.00 33.09           C  
-ANISOU 5117  C   PHE D  35     3249   3927   5395    172    800   -300       C  
-ATOM   5118  O   PHE D  35     -19.085   3.277  14.543  1.00 32.74           O  
-ANISOU 5118  O   PHE D  35     3260   3923   5258     19    857   -314       O  
-ATOM   5119  CB  PHE D  35     -21.251   4.303  12.202  1.00 34.43           C  
-ANISOU 5119  CB  PHE D  35     3115   4146   5821    462    844   -320       C  
-ATOM   5120  CG  PHE D  35     -22.293   3.533  12.942  1.00 37.71           C  
-ANISOU 5120  CG  PHE D  35     3386   4701   6241    366    938   -367       C  
-ATOM   5121  CD1 PHE D  35     -23.046   4.137  13.938  1.00 38.52           C  
-ANISOU 5121  CD1 PHE D  35     3449   4846   6339    366   1136   -487       C  
-ATOM   5122  CD2 PHE D  35     -22.549   2.210  12.611  1.00 41.28           C  
-ANISOU 5122  CD2 PHE D  35     3744   5251   6691    258    836   -308       C  
-ATOM   5123  CE1 PHE D  35     -24.025   3.429  14.609  1.00 43.93           C  
-ANISOU 5123  CE1 PHE D  35     3989   5703   6999    231   1236   -552       C  
-ATOM   5124  CE2 PHE D  35     -23.525   1.493  13.277  1.00 40.41           C  
-ANISOU 5124  CE2 PHE D  35     3524   5279   6552    116    928   -353       C  
-ATOM   5125  CZ  PHE D  35     -24.264   2.102  14.278  1.00 43.21           C  
-ANISOU 5125  CZ  PHE D  35     3824   5709   6884     89   1132   -477       C  
-ATOM   5126  N   ILE D  36     -18.287   3.469  12.460  1.00 27.44           N  
-ANISOU 5126  N   ILE D  36     2543   3208   4675    195    630   -248       N  
-ATOM   5127  CA  ILE D  36     -17.184   2.552  12.689  1.00 23.52           C  
-ANISOU 5127  CA  ILE D  36     2116   2747   4072     82    497   -228       C  
-ATOM   5128  C   ILE D  36     -15.955   3.149  12.032  1.00 31.13           C  
-ANISOU 5128  C   ILE D  36     3152   3708   4968     94    420   -254       C  
-ATOM   5129  O   ILE D  36     -15.864   3.192  10.805  1.00 33.06           O  
-ANISOU 5129  O   ILE D  36     3324   3968   5270    167    324   -237       O  
-ATOM   5130  CB  ILE D  36     -17.463   1.157  12.092  1.00 25.84           C  
-ANISOU 5130  CB  ILE D  36     2302   3088   4427     83    342   -175       C  
-ATOM   5131  CG1 ILE D  36     -18.843   0.648  12.493  1.00 27.32           C  
-ANISOU 5131  CG1 ILE D  36     2397   3308   4675     44    430   -158       C  
-ATOM   5132  CG2 ILE D  36     -16.389   0.154  12.494  1.00 24.30           C  
-ANISOU 5132  CG2 ILE D  36     2201   2901   4129      3    188   -167       C  
-ATOM   5133  CD1 ILE D  36     -19.226  -0.678  11.824  1.00 32.22           C  
-ANISOU 5133  CD1 ILE D  36     2930   3964   5350     20    290   -109       C  
-ATOM   5134  N   PRO D  37     -15.011   3.642  12.848  1.00 30.69           N  
-ANISOU 5134  N   PRO D  37     3236   3657   4769     -7    470   -304       N  
-ATOM   5135  CA  PRO D  37     -13.806   4.250  12.282  1.00 29.09           C  
-ANISOU 5135  CA  PRO D  37     3096   3493   4463    -46    415   -354       C  
-ATOM   5136  C   PRO D  37     -13.033   3.248  11.426  1.00 28.00           C  
-ANISOU 5136  C   PRO D  37     2851   3469   4319    -27    208   -366       C  
-ATOM   5137  O   PRO D  37     -13.012   2.055  11.732  1.00 27.43           O  
-ANISOU 5137  O   PRO D  37     2728   3428   4266    -13     98   -348       O  
-ATOM   5138  CB  PRO D  37     -13.000   4.644  13.526  1.00 30.47           C  
-ANISOU 5138  CB  PRO D  37     3411   3697   4469   -183    498   -413       C  
-ATOM   5139  CG  PRO D  37     -14.044   4.871  14.588  1.00 31.38           C  
-ANISOU 5139  CG  PRO D  37     3569   3730   4623   -196    668   -399       C  
-ATOM   5140  CD  PRO D  37     -15.088   3.814  14.311  1.00 30.80           C  
-ANISOU 5140  CD  PRO D  37     3354   3658   4691   -116    604   -330       C  
-ATOM   5141  N   HIS D  38     -12.422   3.737  10.355  1.00 28.06           N  
-ANISOU 5141  N   HIS D  38     3701   2642   4319   -361    344   -438       N  
-ATOM   5142  CA  HIS D  38     -11.639   2.903   9.454  1.00 25.26           C  
-ANISOU 5142  CA  HIS D  38     3340   2329   3930   -421    329   -340       C  
-ATOM   5143  C   HIS D  38     -10.650   2.008  10.197  1.00 23.49           C  
-ANISOU 5143  C   HIS D  38     3028   2269   3628   -492    336   -366       C  
-ATOM   5144  O   HIS D  38     -10.544   0.815   9.922  1.00 23.85           O  
-ANISOU 5144  O   HIS D  38     3022   2404   3635   -478    310   -297       O  
-ATOM   5145  CB  HIS D  38     -10.859   3.788   8.477  1.00 28.04           C  
-ANISOU 5145  CB  HIS D  38     3800   2542   4311   -497    345   -308       C  
-ATOM   5146  CG  HIS D  38     -10.025   3.009   7.509  1.00 27.59           C  
-ANISOU 5146  CG  HIS D  38     3724   2553   4206   -555    333   -223       C  
-ATOM   5147  ND1 HIS D  38      -8.652   2.936   7.597  1.00 31.10           N  
-ANISOU 5147  ND1 HIS D  38     4142   3073   4602   -679    357   -257       N  
-ATOM   5148  CD2 HIS D  38     -10.374   2.250   6.441  1.00 26.07           C  
-ANISOU 5148  CD2 HIS D  38     3521   2386   3998   -498    296   -125       C  
-ATOM   5149  CE1 HIS D  38      -8.188   2.178   6.619  1.00 29.32           C  
-ANISOU 5149  CE1 HIS D  38     3892   2915   4333   -688    337   -181       C  
-ATOM   5150  NE2 HIS D  38      -9.212   1.746   5.907  1.00 31.38           N  
-ANISOU 5150  NE2 HIS D  38     4166   3143   4614   -581    298   -102       N  
-ATOM   5151  N   GLY D  39      -9.922   2.604  11.133  1.00 29.37           N  
-ANISOU 5151  N   GLY D  39     3759   3051   4349   -559    366   -475       N  
-ATOM   5152  CA  GLY D  39      -8.885   1.893  11.863  1.00 29.14           C  
-ANISOU 5152  CA  GLY D  39     3645   3196   4231   -612    367   -512       C  
-ATOM   5153  C   GLY D  39      -9.431   0.719  12.657  1.00 29.59           C  
-ANISOU 5153  C   GLY D  39     3622   3393   4227   -535    350   -472       C  
-ATOM   5154  O   GLY D  39      -8.783  -0.327  12.781  1.00 28.07           O  
-ANISOU 5154  O   GLY D  39     3382   3318   3967   -535    330   -428       O  
-ATOM   5155  N   LEU D  40     -10.637   0.882  13.191  1.00 25.89           N  
-ANISOU 5155  N   LEU D  40     3142   2915   3781   -467    360   -485       N  
-ATOM   5156  CA ALEU D  40     -11.304  -0.192  13.925  0.07 27.03           C  
-ANISOU 5156  CA ALEU D  40     3216   3184   3870   -414    358   -431       C  
-ATOM   5157  CA BLEU D  40     -11.282  -0.202  13.927  0.93 26.29           C  
-ANISOU 5157  CA BLEU D  40     3122   3092   3775   -415    358   -431       C  
-ATOM   5158  C   LEU D  40     -11.639  -1.332  12.965  1.00 27.36           C  
-ANISOU 5158  C   LEU D  40     3267   3192   3939   -394    327   -301       C  
-ATOM   5159  O   LEU D  40     -11.520  -2.512  13.305  1.00 24.40           O  
-ANISOU 5159  O   LEU D  40     2857   2900   3514   -387    317   -231       O  
-ATOM   5160  CB ALEU D  40     -12.582   0.326  14.588  0.07 28.70           C  
-ANISOU 5160  CB ALEU D  40     3399   3407   4098   -354    382   -485       C  
-ATOM   5161  CB BLEU D  40     -12.527   0.309  14.664  0.93 27.68           C  
-ANISOU 5161  CB BLEU D  40     3266   3288   3963   -356    383   -488       C  
-ATOM   5162  CG ALEU D  40     -13.017  -0.213  15.952  0.07 30.59           C  
-ANISOU 5162  CG ALEU D  40     3549   3828   4244   -330    410   -498       C  
-ATOM   5163  CG BLEU D  40     -13.331  -0.711  15.461  0.93 29.62           C  
-ANISOU 5163  CG BLEU D  40     3434   3674   4146   -324    399   -428       C  
-ATOM   5164  CD1ALEU D  40     -14.529  -0.102  16.100  0.07 31.65           C  
-ANISOU 5164  CD1ALEU D  40     3643   3976   4407   -269    428   -503       C  
-ATOM   5165  CD1BLEU D  40     -12.404  -1.484  16.373  0.93 31.66           C  
-ANISOU 5165  CD1BLEU D  40     3655   4084   4292   -350    404   -402       C  
-ATOM   5166  CD2ALEU D  40     -12.554  -1.642  16.193  0.07 30.49           C  
-ANISOU 5166  CD2ALEU D  40     3510   3918   4157   -348    401   -379       C  
-ATOM   5167  CD2BLEU D  40     -14.427  -0.016  16.272  0.93 32.96           C  
-ANISOU 5167  CD2BLEU D  40     3805   4156   4561   -271    431   -520       C  
-ATOM   5168  N   ILE D  41     -12.071  -0.970  11.761  1.00 23.49           N  
-ANISOU 5168  N   ILE D  41     2828   2573   3526   -378    309   -271       N  
-ATOM   5169  CA  ILE D  41     -12.355  -1.960  10.738  1.00 24.02           C  
-ANISOU 5169  CA  ILE D  41     2897   2611   3619   -361    274   -176       C  
-ATOM   5170  C   ILE D  41     -11.074  -2.735  10.443  1.00 24.87           C  
-ANISOU 5170  C   ILE D  41     3005   2764   3682   -398    251   -144       C  
-ATOM   5171  O   ILE D  41     -11.092  -3.958  10.354  1.00 22.49           O  
-ANISOU 5171  O   ILE D  41     2682   2496   3368   -381    226    -82       O  
-ATOM   5172  CB  ILE D  41     -12.886  -1.304   9.453  1.00 23.94           C  
-ANISOU 5172  CB  ILE D  41     2940   2480   3676   -328    254   -158       C  
-ATOM   5173  CG1 ILE D  41     -14.249  -0.664   9.712  1.00 22.02           C  
-ANISOU 5173  CG1 ILE D  41     2684   2210   3472   -257    264   -194       C  
-ATOM   5174  CG2 ILE D  41     -13.008  -2.324   8.344  1.00 21.50           C  
-ANISOU 5174  CG2 ILE D  41     2621   2166   3381   -313    213    -84       C  
-ATOM   5175  CD1 ILE D  41     -14.704   0.255   8.572  1.00 26.57           C  
-ANISOU 5175  CD1 ILE D  41     3331   2664   4102   -198    242   -182       C  
-ATOM   5176  N   MET D  42      -9.958  -2.021  10.315  1.00 23.97           N  
-ANISOU 5176  N   MET D  42     2913   2652   3544   -449    260   -195       N  
-ATOM   5177  CA  MET D  42      -8.662  -2.669  10.068  1.00 27.55           C  
-ANISOU 5177  CA  MET D  42     3346   3185   3939   -477    238   -190       C  
-ATOM   5178  C   MET D  42      -8.279  -3.656  11.177  1.00 23.79           C  
-ANISOU 5178  C   MET D  42     2817   2836   3386   -445    227   -183       C  
-ATOM   5179  O   MET D  42      -7.913  -4.798  10.899  1.00 22.25           O  
-ANISOU 5179  O   MET D  42     2613   2674   3167   -406    189   -129       O  
-ATOM   5180  CB  MET D  42      -7.553  -1.621   9.869  1.00 25.89           C  
-ANISOU 5180  CB  MET D  42     3148   2980   3709   -562    263   -265       C  
-ATOM   5181  CG  MET D  42      -7.726  -0.707   8.661  1.00 29.40           C  
-ANISOU 5181  CG  MET D  42     3666   3291   4214   -600    276   -241       C  
-ATOM   5182  SD  MET D  42      -7.778  -1.611   7.095  1.00 33.38           S  
-ANISOU 5182  SD  MET D  42     4177   3787   4721   -558    230   -145       S  
-ATOM   5183  CE  MET D  42      -9.560  -1.776   6.933  1.00 41.72           C  
-ANISOU 5183  CE  MET D  42     5255   4745   5850   -462    211    -91       C  
-ATOM   5184  N   ASP D  43      -8.367  -3.224  12.429  1.00 21.27           N  
-ANISOU 5184  N   ASP D  43     2469   2590   3022   -449    258   -237       N  
-ATOM   5185  CA  ASP D  43      -8.002  -4.095  13.544  1.00 24.73           C  
-ANISOU 5185  CA  ASP D  43     2864   3168   3365   -408    250   -217       C  
-ATOM   5186  C   ASP D  43      -8.858  -5.356  13.588  1.00 24.51           C  
-ANISOU 5186  C   ASP D  43     2851   3107   3353   -357    236    -95       C  
-ATOM   5187  O   ASP D  43      -8.343  -6.450  13.829  1.00 25.47           O  
-ANISOU 5187  O   ASP D  43     2975   3280   3423   -312    206    -32       O  
-ATOM   5188  CB  ASP D  43      -8.114  -3.363  14.896  1.00 21.91           C  
-ANISOU 5188  CB  ASP D  43     2465   2915   2946   -416    288   -302       C  
-ATOM   5189  CG  ASP D  43      -7.102  -2.233  15.043  1.00 28.74           C  
-ANISOU 5189  CG  ASP D  43     3306   3826   3787   -481    301   -443       C  
-ATOM   5190  OD1 ASP D  43      -5.995  -2.341  14.485  1.00 28.77           O  
-ANISOU 5190  OD1 ASP D  43     3298   3864   3769   -513    279   -465       O  
-ATOM   5191  OD2 ASP D  43      -7.416  -1.251  15.741  1.00 32.41           O  
-ANISOU 5191  OD2 ASP D  43     3757   4301   4255   -505    335   -544       O  
-ATOM   5192  N   ARG D  44     -10.165  -5.199  13.386  1.00 21.75           N  
-ANISOU 5192  N   ARG D  44     2511   2675   3076   -363    258    -67       N  
-ATOM   5193  CA  ARG D  44     -11.063  -6.357  13.360  1.00 20.73           C  
-ANISOU 5193  CA  ARG D  44     2390   2509   2978   -348    254     37       C  
-ATOM   5194  C   ARG D  44     -10.759  -7.267  12.171  1.00 23.26           C  
-ANISOU 5194  C   ARG D  44     2746   2739   3353   -335    203     86       C  
-ATOM   5195  O   ARG D  44     -10.782  -8.492  12.291  1.00 23.37           O  
-ANISOU 5195  O   ARG D  44     2781   2732   3366   -316    183    166       O  
-ATOM   5196  CB  ARG D  44     -12.530  -5.913  13.320  1.00 22.67           C  
-ANISOU 5196  CB  ARG D  44     2612   2716   3286   -363    288     29       C  
-ATOM   5197  CG  ARG D  44     -13.517  -7.063  13.271  1.00 23.11           C  
-ANISOU 5197  CG  ARG D  44     2659   2742   3379   -379    295    120       C  
-ATOM   5198  CD  ARG D  44     -13.469  -7.924  14.523  1.00 21.39           C  
-ANISOU 5198  CD  ARG D  44     2437   2613   3078   -388    326    203       C  
-ATOM   5199  NE  ARG D  44     -14.478  -8.986  14.437  1.00 24.89           N  
-ANISOU 5199  NE  ARG D  44     2880   3006   3572   -435    344    294       N  
-ATOM   5200  CZ  ARG D  44     -14.300 -10.223  14.871  1.00 28.81           C  
-ANISOU 5200  CZ  ARG D  44     3422   3478   4045   -450    346    410       C  
-ATOM   5201  NH1 ARG D  44     -13.146 -10.576  15.426  1.00 28.54           N  
-ANISOU 5201  NH1 ARG D  44     3435   3484   3925   -394    323    452       N  
-ATOM   5202  NH2 ARG D  44     -15.277 -11.109  14.741  1.00 26.23           N  
-ANISOU 5202  NH2 ARG D  44     3098   3088   3782   -521    371    481       N  
-ATOM   5203  N   THR D  45     -10.465  -6.660  11.025  1.00 21.74           N  
-ANISOU 5203  N   THR D  45     2566   2490   3206   -343    181     38       N  
-ATOM   5204  CA  THR D  45     -10.148  -7.413   9.810  1.00 22.29           C  
-ANISOU 5204  CA  THR D  45     2655   2500   3315   -324    130     61       C  
-ATOM   5205  C   THR D  45      -8.858  -8.218   9.985  1.00 24.87           C  
-ANISOU 5205  C   THR D  45     2985   2889   3575   -284     93     67       C  
-ATOM   5206  O   THR D  45      -8.748  -9.357   9.498  1.00 25.43           O  
-ANISOU 5206  O   THR D  45     3077   2915   3672   -243     48    103       O  
-ATOM   5207  CB  THR D  45     -10.068  -6.458   8.599  1.00 24.56           C  
-ANISOU 5207  CB  THR D  45     2951   2744   3636   -340    124     16       C  
-ATOM   5208  OG1 THR D  45     -11.362  -5.870   8.383  1.00 23.58           O  
-ANISOU 5208  OG1 THR D  45     2828   2561   3572   -342    144     18       O  
-ATOM   5209  CG2 THR D  45      -9.640  -7.195   7.338  1.00 23.54           C  
-ANISOU 5209  CG2 THR D  45     2828   2594   3523   -315     72     24       C  
-ATOM   5210  N   GLU D  46      -7.892  -7.655  10.712  1.00 22.30           N  
-ANISOU 5210  N   GLU D  46     2635   2674   3165   -287    106     17       N  
-ATOM   5211  CA  GLU D  46      -6.657  -8.386  10.998  1.00 22.17           C  
-ANISOU 5211  CA  GLU D  46     2605   2754   3066   -227     65     11       C  
-ATOM   5212  C   GLU D  46      -6.970  -9.678  11.756  1.00 23.09           C  
-ANISOU 5212  C   GLU D  46     2758   2849   3167   -161     47    109       C  
-ATOM   5213  O   GLU D  46      -6.418 -10.739  11.460  1.00 22.67           O  
-ANISOU 5213  O   GLU D  46     2731   2777   3106    -85     -8    138       O  
-ATOM   5214  CB  GLU D  46      -5.667  -7.528  11.811  1.00 24.23           C  
-ANISOU 5214  CB  GLU D  46     2812   3166   3227   -247     86    -75       C  
-ATOM   5215  CG  GLU D  46      -4.377  -8.281  12.100  1.00 22.79           C  
-ANISOU 5215  CG  GLU D  46     2596   3119   2944   -165     36    -95       C  
-ATOM   5216  CD  GLU D  46      -3.409  -7.498  12.968  1.00 34.51           C  
-ANISOU 5216  CD  GLU D  46     4005   4787   4319   -187     52   -199       C  
-ATOM   5217  OE1 GLU D  46      -2.352  -8.059  13.314  1.00 34.51           O  
-ANISOU 5217  OE1 GLU D  46     3960   4934   4218   -105      8   -228       O  
-ATOM   5218  OE2 GLU D  46      -3.700  -6.329  13.295  1.00 44.03           O  
-ANISOU 5218  OE2 GLU D  46     5194   5994   5541   -278    105   -263       O  
-ATOM   5219  N   ARG D  47      -7.857  -9.603  12.742  1.00 21.69           N  
-ANISOU 5219  N   ARG D  47     2588   2672   2982   -186     93    162       N  
-ATOM   5220  CA  ARG D  47      -8.220 -10.807  13.480  1.00 24.38           C  
-ANISOU 5220  CA  ARG D  47     2977   2982   3305   -145     90    281       C  
-ATOM   5221  C   ARG D  47      -8.985 -11.776  12.576  1.00 26.55           C  
-ANISOU 5221  C   ARG D  47     3304   3085   3700   -160     68    340       C  
-ATOM   5222  O   ARG D  47      -8.760 -12.999  12.621  1.00 24.74           O  
-ANISOU 5222  O   ARG D  47     3138   2782   3480   -105     31    415       O  
-ATOM   5223  CB  ARG D  47      -9.027 -10.452  14.734  1.00 23.87           C  
-ANISOU 5223  CB  ARG D  47     2893   2989   3189   -184    157    323       C  
-ATOM   5224  CG  ARG D  47      -9.806 -11.615  15.350  1.00 30.56           C  
-ANISOU 5224  CG  ARG D  47     3796   3775   4041   -189    179    470       C  
-ATOM   5225  CD  ARG D  47      -8.942 -12.857  15.601  1.00 43.95           C  
-ANISOU 5225  CD  ARG D  47     5567   5445   5685    -90    125    564       C  
-ATOM   5226  NE  ARG D  47      -8.394 -12.896  16.938  1.00 52.35           N  
-ANISOU 5226  NE  ARG D  47     6626   6670   6592    -24    137    615       N  
-ATOM   5227  CZ  ARG D  47      -8.790 -13.730  17.891  1.00 49.02           C  
-ANISOU 5227  CZ  ARG D  47     6266   6247   6110     -9    166    770       C  
-ATOM   5228  NH1 ARG D  47      -9.733 -14.633  17.658  1.00 56.72           N  
-ANISOU 5228  NH1 ARG D  47     7317   7048   7185    -76    192    887       N  
-ATOM   5229  NH2 ARG D  47      -8.222 -13.664  19.079  1.00 39.98           N  
-ANISOU 5229  NH2 ARG D  47     5107   5286   4800     67    171    807       N  
-ATOM   5230  N   LEU D  48      -9.893 -11.248  11.763  1.00 25.42           N  
-ANISOU 5230  N   LEU D  48     3137   2874   3648   -228     87    299       N  
-ATOM   5231  CA  LEU D  48     -10.660 -12.127  10.872  1.00 27.59           C  
-ANISOU 5231  CA  LEU D  48     3440   3008   4035   -251     65    327       C  
-ATOM   5232  C   LEU D  48      -9.732 -12.899   9.934  1.00 25.49           C  
-ANISOU 5232  C   LEU D  48     3205   2691   3789   -179    -11    297       C  
-ATOM   5233  O   LEU D  48      -9.955 -14.074   9.676  1.00 22.44           O  
-ANISOU 5233  O   LEU D  48     2872   2187   3467   -164    -42    339       O  
-ATOM   5234  CB  LEU D  48     -11.719 -11.363  10.069  1.00 27.76           C  
-ANISOU 5234  CB  LEU D  48     3413   3001   4131   -312     86    271       C  
-ATOM   5235  CG  LEU D  48     -12.908 -10.804  10.850  1.00 27.04           C  
-ANISOU 5235  CG  LEU D  48     3282   2950   4042   -372    154    288       C  
-ATOM   5236  CD1 LEU D  48     -13.870 -10.039   9.943  1.00 27.31           C  
-ANISOU 5236  CD1 LEU D  48     3267   2967   4143   -394    157    221       C  
-ATOM   5237  CD2 LEU D  48     -13.632 -11.914  11.594  1.00 25.43           C  
-ANISOU 5237  CD2 LEU D  48     3099   2706   3856   -422    186    387       C  
-ATOM   5238  N   ALA D  49      -8.693 -12.249   9.423  1.00 20.67           N  
-ANISOU 5238  N   ALA D  49     2560   2168   3124   -140    -38    217       N  
-ATOM   5239  CA  ALA D  49      -7.754 -12.943   8.519  1.00 21.56           C  
-ANISOU 5239  CA  ALA D  49     2681   2272   3237    -61   -110    169       C  
-ATOM   5240  C   ALA D  49      -7.150 -14.156   9.216  1.00 22.78           C  
-ANISOU 5240  C   ALA D  49     2898   2399   3360     35   -151    229       C  
-ATOM   5241  O   ALA D  49      -6.967 -15.223   8.621  1.00 24.37           O  
-ANISOU 5241  O   ALA D  49     3144   2503   3614    101   -210    222       O  
-ATOM   5242  CB  ALA D  49      -6.653 -11.992   8.054  1.00 23.03           C  
-ANISOU 5242  CB  ALA D  49     2807   2600   3345    -51   -116     78       C  
-ATOM   5243  N   ARG D  50      -6.835 -13.989  10.494  1.00 24.10           N  
-ANISOU 5243  N   ARG D  50     3071   2652   3434     56   -124    284       N  
-ATOM   5244  CA  ARG D  50      -6.255 -15.087  11.257  1.00 26.52           C  
-ANISOU 5244  CA  ARG D  50     3446   2941   3688    169   -164    362       C  
-ATOM   5245  C   ARG D  50      -7.278 -16.198  11.482  1.00 27.99           C  
-ANISOU 5245  C   ARG D  50     3735   2930   3971    138   -152    484       C  
-ATOM   5246  O   ARG D  50      -6.952 -17.385  11.367  1.00 24.85           O  
-ANISOU 5246  O   ARG D  50     3425   2412   3606    228   -209    528       O  
-ATOM   5247  CB  ARG D  50      -5.685 -14.576  12.585  1.00 31.62           C  
-ANISOU 5247  CB  ARG D  50     4062   3762   4189    203   -137    388       C  
-ATOM   5248  CG  ARG D  50      -4.519 -15.409  13.108  1.00 38.31           C  
-ANISOU 5248  CG  ARG D  50     4943   4680   4934    371   -206    415       C  
-ATOM   5249  CD  ARG D  50      -3.965 -14.842  14.407  1.00 43.24           C  
-ANISOU 5249  CD  ARG D  50     5517   5516   5397    409   -184    422       C  
-ATOM   5250  NE  ARG D  50      -4.921 -14.969  15.504  1.00 49.52           N  
-ANISOU 5250  NE  ARG D  50     6364   6279   6172    357   -120    558       N  
-ATOM   5251  CZ  ARG D  50      -4.795 -14.374  16.689  1.00 56.43           C  
-ANISOU 5251  CZ  ARG D  50     7190   7338   6914    359    -82    567       C  
-ATOM   5252  NH1 ARG D  50      -3.753 -13.590  16.941  1.00 57.19           N  
-ANISOU 5252  NH1 ARG D  50     7182   7650   6896    402   -102    438       N  
-ATOM   5253  NH2 ARG D  50      -5.717 -14.557  17.626  1.00 55.59           N  
-ANISOU 5253  NH2 ARG D  50     7126   7213   6782    310    -19    696       N  
-ATOM   5254  N   ASP D  51      -8.519 -15.822  11.778  1.00 29.59           N  
-ANISOU 5254  N   ASP D  51     3925   3095   4223      8    -78    530       N  
-ATOM   5255  CA  ASP D  51      -9.585 -16.808  11.932  1.00 28.40           C  
-ANISOU 5255  CA  ASP D  51     3852   2768   4171    -64    -52    635       C  
-ATOM   5256  C   ASP D  51      -9.802 -17.564  10.611  1.00 26.42           C  
-ANISOU 5256  C   ASP D  51     3629   2351   4058    -68   -108    567       C  
-ATOM   5257  O   ASP D  51     -10.018 -18.774  10.596  1.00 28.88           O  
-ANISOU 5257  O   ASP D  51     4039   2485   4449    -63   -130    632       O  
-ATOM   5258  CB  ASP D  51     -10.893 -16.107  12.335  1.00 31.07           C  
-ANISOU 5258  CB  ASP D  51     4131   3145   4530   -207     38    656       C  
-ATOM   5259  CG  ASP D  51     -10.815 -15.435  13.700  1.00 34.24           C  
-ANISOU 5259  CG  ASP D  51     4502   3711   4795   -206     97    713       C  
-ATOM   5260  OD1 ASP D  51      -9.885 -15.742  14.469  1.00 32.45           O  
-ANISOU 5260  OD1 ASP D  51     4319   3551   4461   -106     73    770       O  
-ATOM   5261  OD2 ASP D  51     -11.705 -14.612  14.012  1.00 38.03           O  
-ANISOU 5261  OD2 ASP D  51     4911   4268   5272   -295    163    691       O  
-ATOM   5262  N   VAL D  52      -9.776 -16.828   9.504  1.00 24.84           N  
-ANISOU 5262  N   VAL D  52     3344   2210   3886    -81   -128    437       N  
-ATOM   5263  CA  VAL D  52      -9.983 -17.435   8.191  1.00 28.36           C  
-ANISOU 5263  CA  VAL D  52     3791   2541   4442    -79   -184    350       C  
-ATOM   5264  C   VAL D  52      -8.910 -18.469   7.895  1.00 30.36           C  
-ANISOU 5264  C   VAL D  52     4116   2725   4697     61   -270    326       C  
-ATOM   5265  O   VAL D  52      -9.213 -19.609   7.514  1.00 29.68           O  
-ANISOU 5265  O   VAL D  52     4105   2455   4719     66   -307    326       O  
-ATOM   5266  CB  VAL D  52     -10.024 -16.383   7.083  1.00 26.53           C  
-ANISOU 5266  CB  VAL D  52     3456   2419   4203    -98   -191    229       C  
-ATOM   5267  CG1 VAL D  52      -9.842 -17.030   5.723  1.00 29.86           C  
-ANISOU 5267  CG1 VAL D  52     3871   2779   4694    -51   -265    122       C  
-ATOM   5268  CG2 VAL D  52     -11.343 -15.614   7.140  1.00 27.37           C  
-ANISOU 5268  CG2 VAL D  52     3505   2545   4347   -219   -124    237       C  
-ATOM   5269  N   MET D  53      -7.652 -18.093   8.099  1.00 25.98           N  
-ANISOU 5269  N   MET D  53     3535   2315   4022    177   -302    296       N  
-ATOM   5270  CA AMET D  53      -6.564 -19.034   7.833  0.63 27.95           C  
-ANISOU 5270  CA AMET D  53     3835   2531   4255    340   -391    257       C  
-ATOM   5271  CA BMET D  53      -6.531 -19.012   7.869  0.37 29.00           C  
-ANISOU 5271  CA BMET D  53     3967   2670   4382    342   -391    258       C  
-ATOM   5272  C   MET D  53      -6.616 -20.265   8.731  1.00 32.28           C  
-ANISOU 5272  C   MET D  53     4529   2902   4833    403   -409    389       C  
-ATOM   5273  O   MET D  53      -6.250 -21.368   8.300  1.00 32.57           O  
-ANISOU 5273  O   MET D  53     4648   2793   4935    510   -484    361       O  
-ATOM   5274  CB AMET D  53      -5.203 -18.335   7.897  0.63 30.86           C  
-ANISOU 5274  CB AMET D  53     4119   3130   4475    444   -418    184       C  
-ATOM   5275  CB BMET D  53      -5.190 -18.311   8.121  0.37 31.42           C  
-ANISOU 5275  CB BMET D  53     4197   3209   4534    444   -412    203       C  
-ATOM   5276  CG AMET D  53      -4.957 -17.420   6.707  0.63 30.55           C  
-ANISOU 5276  CG AMET D  53     3963   3226   4419    400   -419     48       C  
-ATOM   5277  CG BMET D  53      -4.617 -17.532   6.941  0.37 30.84           C  
-ANISOU 5277  CG BMET D  53     4005   3287   4425    441   -430     53       C  
-ATOM   5278  SD AMET D  53      -4.967 -18.347   5.154  0.63 37.40           S  
-ANISOU 5278  SD AMET D  53     4833   3993   5385    463   -500    -75       S  
-ATOM   5279  SD BMET D  53      -4.052 -18.558   5.562  0.37 37.70           S  
-ANISOU 5279  SD BMET D  53     4873   4104   5347    569   -533    -81       S  
-ATOM   5280  CE AMET D  53      -3.524 -19.380   5.395  0.63 41.22           C  
-ANISOU 5280  CE AMET D  53     5353   4509   5798    689   -598   -118       C  
-ATOM   5281  CE BMET D  53      -5.520 -18.510   4.541  0.37 39.37           C  
-ANISOU 5281  CE BMET D  53     5081   4174   5704    422   -505   -106       C  
-ATOM   5282  N   LYS D  54      -7.088 -20.098   9.964  1.00 32.14           N  
-ANISOU 5282  N   LYS D  54     4551   2891   4769    339   -339    534       N  
-ATOM   5283  CA  LYS D  54      -7.193 -21.240  10.876  1.00 34.51           C  
-ANISOU 5283  CA  LYS D  54     5006   3023   5086    387   -342    695       C  
-ATOM   5284  C   LYS D  54      -8.193 -22.261  10.347  1.00 33.68           C  
-ANISOU 5284  C   LYS D  54     4995   2639   5163    286   -339    720       C  
-ATOM   5285  O   LYS D  54      -7.981 -23.466  10.461  1.00 31.34           O  
-ANISOU 5285  O   LYS D  54     4845   2135   4929    368   -387    785       O  
-ATOM   5286  CB  LYS D  54      -7.581 -20.790  12.295  1.00 40.69           C  
-ANISOU 5286  CB  LYS D  54     5796   3903   5763    322   -256    848       C  
-ATOM   5287  CG  LYS D  54      -7.232 -21.791  13.392  1.00 49.40           C  
-ANISOU 5287  CG  LYS D  54     7051   4915   6804    431   -270   1029       C  
-ATOM   5288  CD  LYS D  54      -7.736 -21.353  14.767  1.00 56.04           C  
-ANISOU 5288  CD  LYS D  54     7888   5876   7529    354   -176   1181       C  
-ATOM   5289  CE  LYS D  54      -9.261 -21.264  14.816  1.00 58.83           C  
-ANISOU 5289  CE  LYS D  54     8231   6137   7986    121    -72   1238       C  
-ATOM   5290  NZ  LYS D  54      -9.729 -19.869  15.095  1.00 58.23           N  
-ANISOU 5290  NZ  LYS D  54     7996   6292   7838     19      0   1167       N  
-ATOM   5291  N   GLU D  55      -9.280 -21.789   9.754  1.00 31.68           N  
-ANISOU 5291  N   GLU D  55     4661   2378   4998    113   -286    658       N  
-ATOM   5292  CA  GLU D  55     -10.307 -22.717   9.284  1.00 36.31           C  
-ANISOU 5292  CA  GLU D  55     5314   2725   5758    -10   -275    662       C  
-ATOM   5293  C   GLU D  55     -10.084 -23.205   7.849  1.00 34.65           C  
-ANISOU 5293  C   GLU D  55     5085   2424   5655     45   -364    482       C  
-ATOM   5294  O   GLU D  55     -10.440 -24.335   7.512  1.00 36.71           O  
-ANISOU 5294  O   GLU D  55     5448   2444   6058     17   -394    471       O  
-ATOM   5295  CB  GLU D  55     -11.697 -22.091   9.406  1.00 39.04           C  
-ANISOU 5295  CB  GLU D  55     5570   3120   6143   -223   -176    678       C  
-ATOM   5296  CG  GLU D  55     -12.167 -21.892  10.831  1.00 54.47           C  
-ANISOU 5296  CG  GLU D  55     7553   5127   8015   -304    -79    858       C  
-ATOM   5297  CD  GLU D  55     -13.639 -21.516  10.909  1.00 65.29           C  
-ANISOU 5297  CD  GLU D  55     8836   6528   9443   -514     16    862       C  
-ATOM   5298  OE1 GLU D  55     -13.959 -20.524  11.606  1.00 67.90           O  
-ANISOU 5298  OE1 GLU D  55     9079   7052   9670   -555     84    893       O  
-ATOM   5299  OE2 GLU D  55     -14.467 -22.216  10.279  1.00 68.82           O  
-ANISOU 5299  OE2 GLU D  55     9295   6817  10038   -635     20    817       O  
-ATOM   5300  N   MET D  56      -9.491 -22.348   7.021  1.00 30.48           N  
-ANISOU 5300  N   MET D  56     4430   2093   5058    116   -403    338       N  
-ATOM   5301  CA  MET D  56      -9.456 -22.550   5.573  1.00 30.18           C  
-ANISOU 5301  CA  MET D  56     4332   2039   5095    143   -472    154       C  
-ATOM   5302  C   MET D  56      -8.056 -22.697   4.993  1.00 33.88           C  
-ANISOU 5302  C   MET D  56     4786   2598   5490    346   -566     44       C  
-ATOM   5303  O   MET D  56      -7.907 -23.017   3.814  1.00 32.12           O  
-ANISOU 5303  O   MET D  56     4520   2366   5317    394   -631   -114       O  
-ATOM   5304  CB  MET D  56     -10.149 -21.371   4.883  1.00 32.79           C  
-ANISOU 5304  CB  MET D  56     4511   2542   5405     33   -428     73       C  
-ATOM   5305  CG  MET D  56     -11.580 -21.160   5.340  1.00 33.96           C  
-ANISOU 5305  CG  MET D  56     4640   2644   5619   -156   -340    146       C  
-ATOM   5306  SD  MET D  56     -12.372 -19.892   4.356  1.00 31.20           S  
-ANISOU 5306  SD  MET D  56     4122   2483   5250   -234   -316     32       S  
-ATOM   5307  CE  MET D  56     -12.676 -20.783   2.823  1.00 27.12           C  
-ANISOU 5307  CE  MET D  56     3577   1872   4855   -226   -399   -151       C  
-ATOM   5308  N   GLY D  57      -7.032 -22.477   5.814  1.00 36.44           N  
-ANISOU 5308  N   GLY D  57     5129   3031   5684    469   -576    114       N  
-ATOM   5309  CA  GLY D  57      -5.663 -22.480   5.321  1.00 35.01           C  
-ANISOU 5309  CA  GLY D  57     4899   2995   5407    657   -658     -1       C  
-ATOM   5310  C   GLY D  57      -5.064 -23.818   4.934  1.00 37.18           C  
-ANISOU 5310  C   GLY D  57     5273   3105   5748    832   -763    -71       C  
-ATOM   5311  O   GLY D  57      -3.881 -23.893   4.589  1.00 38.27           O  
-ANISOU 5311  O   GLY D  57     5363   3382   5795   1011   -836   -174       O  
-ATOM   5312  N   GLY D  58      -5.858 -24.885   4.980  1.00 34.71           N  
-ANISOU 5312  N   GLY D  58     5095   2496   5595    781   -771    -25       N  
-ATOM   5313  CA  GLY D  58      -5.330 -26.213   4.744  1.00 40.19           C  
-ANISOU 5313  CA  GLY D  58     5918   2981   6371    953   -871    -79       C  
-ATOM   5314  C   GLY D  58      -5.332 -26.627   3.284  1.00 36.82           C  
-ANISOU 5314  C   GLY D  58     5430   2525   6033    990   -945   -308       C  
-ATOM   5315  O   GLY D  58      -4.761 -27.647   2.922  1.00 40.66           O  
-ANISOU 5315  O   GLY D  58     5999   2871   6578   1161  -1043   -403       O  
-ATOM   5316  N   HIS D  59      -5.974 -25.833   2.440  1.00 34.02           N  
-ANISOU 5316  N   HIS D  59     4931   2311   5683    842   -904   -402       N  
-ATOM   5317  CA  HIS D  59      -6.086 -26.193   1.035  1.00 34.21           C  
-ANISOU 5317  CA  HIS D  59     4884   2337   5779    866   -970   -621       C  
-ATOM   5318  C   HIS D  59      -6.247 -24.920   0.223  1.00 29.99           C  
-ANISOU 5318  C   HIS D  59     4158   2097   5139    779   -928   -698       C  
-ATOM   5319  O   HIS D  59      -6.643 -23.905   0.757  1.00 32.09           O  
-ANISOU 5319  O   HIS D  59     4378   2476   5340    657   -841   -578       O  
-ATOM   5320  CB  HIS D  59      -7.294 -27.104   0.826  1.00 37.22           C  
-ANISOU 5320  CB  HIS D  59     5359   2417   6367    725   -964   -642       C  
-ATOM   5321  CG  HIS D  59      -7.410 -27.655  -0.562  1.00 46.19           C  
-ANISOU 5321  CG  HIS D  59     6434   3530   7587    762  -1045   -888       C  
-ATOM   5322  ND1 HIS D  59      -6.567 -28.633  -1.048  1.00 56.01           N  
-ANISOU 5322  ND1 HIS D  59     7719   4741   8822    942  -1128  -1010       N  
-ATOM   5323  CD2 HIS D  59      -8.287 -27.386  -1.561  1.00 48.00           C  
-ANISOU 5323  CD2 HIS D  59     6543   3831   7865    633  -1034  -1023       C  
-ATOM   5324  CE1 HIS D  59      -6.913 -28.935  -2.288  1.00 57.18           C  
-ANISOU 5324  CE1 HIS D  59     7775   4934   9015    918  -1168  -1213       C  
-ATOM   5325  NE2 HIS D  59      -7.953 -28.193  -2.624  1.00 51.82           N  
-ANISOU 5325  NE2 HIS D  59     6999   4321   8371    736  -1116  -1227       N  
-ATOM   5326  N   HIS D  60      -5.930 -24.986  -1.066  1.00 35.75           N  
-ANISOU 5326  N   HIS D  60     4785   2950   5848    853   -992   -898       N  
-ATOM   5327  CA  HIS D  60      -6.096 -23.849  -1.978  1.00 30.02           C  
-ANISOU 5327  CA  HIS D  60     3891   2496   5019    780   -957   -966       C  
-ATOM   5328  C   HIS D  60      -7.412 -23.104  -1.741  1.00 30.01           C  
-ANISOU 5328  C   HIS D  60     3867   2474   5061    570   -865   -860       C  
-ATOM   5329  O   HIS D  60      -8.494 -23.694  -1.777  1.00 32.32           O  
-ANISOU 5329  O   HIS D  60     4206   2577   5499    463   -859   -871       O  
-ATOM   5330  CB  HIS D  60      -6.025 -24.351  -3.425  1.00 33.12           C  
-ANISOU 5330  CB  HIS D  60     4201   2951   5432    855  -1039  -1197       C  
-ATOM   5331  CG  HIS D  60      -6.078 -23.267  -4.457  1.00 40.20           C  
-ANISOU 5331  CG  HIS D  60     4933   4141   6199    810  -1012  -1262       C  
-ATOM   5332  ND1 HIS D  60      -5.237 -23.244  -5.548  1.00 45.00           N  
-ANISOU 5332  ND1 HIS D  60     5429   4975   6695    936  -1069  -1428       N  
-ATOM   5333  CD2 HIS D  60      -6.880 -22.183  -4.578  1.00 39.65           C  
-ANISOU 5333  CD2 HIS D  60     4799   4177   6090    663   -935  -1178       C  
-ATOM   5334  CE1 HIS D  60      -5.508 -22.184  -6.285  1.00 42.33           C  
-ANISOU 5334  CE1 HIS D  60     4973   4863   6247    857  -1023  -1424       C  
-ATOM   5335  NE2 HIS D  60      -6.508 -21.529  -5.728  1.00 37.23           N  
-ANISOU 5335  NE2 HIS D  60     4359   4137   5648    701   -946  -1276       N  
-ATOM   5336  N   ILE D  61      -7.302 -21.798  -1.515  1.00 27.68           N  
-ANISOU 5336  N   ILE D  61     3496   2380   4641    513   -796   -771       N  
-ATOM   5337  CA  ILE D  61      -8.454 -20.950  -1.287  1.00 29.24           C  
-ANISOU 5337  CA  ILE D  61     3663   2590   4858    347   -714   -679       C  
-ATOM   5338  C   ILE D  61      -8.767 -20.155  -2.540  1.00 31.01           C  
-ANISOU 5338  C   ILE D  61     3759   3009   5017    322   -715   -774       C  
-ATOM   5339  O   ILE D  61      -7.869 -19.595  -3.174  1.00 30.25           O  
-ANISOU 5339  O   ILE D  61     3590   3113   4791    399   -730   -824       O  
-ATOM   5340  CB  ILE D  61      -8.189 -19.985  -0.135  1.00 26.53           C  
-ANISOU 5340  CB  ILE D  61     3336   2319   4425    305   -636   -516       C  
-ATOM   5341  CG1 ILE D  61      -8.143 -20.755   1.177  1.00 30.71           C  
-ANISOU 5341  CG1 ILE D  61     3994   2660   5013    314   -624   -396       C  
-ATOM   5342  CG2 ILE D  61      -9.265 -18.894  -0.025  1.00 28.21           C  
-ANISOU 5342  CG2 ILE D  61     3497   2589   4633    164   -556   -445       C  
-ATOM   5343  CD1 ILE D  61      -7.735 -19.892   2.329  1.00 31.93           C  
-ANISOU 5343  CD1 ILE D  61     4156   2914   5062    299   -560   -261       C  
-ATOM   5344  N   VAL D  62     -10.039 -20.135  -2.914  1.00 24.75           N  
-ANISOU 5344  N   VAL D  62     2933   2169   4304    218   -700   -799       N  
-ATOM   5345  CA  VAL D  62     -10.510 -19.182  -3.908  1.00 26.37           C  
-ANISOU 5345  CA  VAL D  62     3025   2565   4430    193   -689   -844       C  
-ATOM   5346  C   VAL D  62     -11.314 -18.114  -3.175  1.00 28.16           C  
-ANISOU 5346  C   VAL D  62     3250   2807   4642     85   -603   -701       C  
-ATOM   5347  O   VAL D  62     -12.340 -18.401  -2.563  1.00 29.93           O  
-ANISOU 5347  O   VAL D  62     3498   2904   4969    -12   -571   -660       O  
-ATOM   5348  CB  VAL D  62     -11.364 -19.850  -4.993  1.00 25.18           C  
-ANISOU 5348  CB  VAL D  62     2809   2403   4356    180   -747  -1007       C  
-ATOM   5349  CG1 VAL D  62     -11.902 -18.793  -5.969  1.00 32.82           C  
-ANISOU 5349  CG1 VAL D  62     3663   3589   5219    173   -737  -1029       C  
-ATOM   5350  CG2 VAL D  62     -10.560 -20.912  -5.728  1.00 29.81           C  
-ANISOU 5350  CG2 VAL D  62     3396   2973   4959    300   -839  -1173       C  
-ATOM   5351  N   ALA D  63     -10.838 -16.878  -3.225  1.00 22.81           N  
-ANISOU 5351  N   ALA D  63     2542   2285   3837    100   -562   -631       N  
-ATOM   5352  CA  ALA D  63     -11.523 -15.772  -2.569  1.00 21.50           C  
-ANISOU 5352  CA  ALA D  63     2380   2135   3654     21   -487   -512       C  
-ATOM   5353  C   ALA D  63     -12.394 -15.059  -3.592  1.00 29.64           C  
-ANISOU 5353  C   ALA D  63     3331   3281   4650     16   -492   -550       C  
-ATOM   5354  O   ALA D  63     -11.894 -14.551  -4.606  1.00 29.45           O  
-ANISOU 5354  O   ALA D  63     3263   3405   4520     76   -514   -584       O  
-ATOM   5355  CB  ALA D  63     -10.520 -14.816  -1.976  1.00 22.11           C  
-ANISOU 5355  CB  ALA D  63     2484   2289   3628     33   -439   -420       C  
-ATOM   5356  N   LEU D  64     -13.693 -15.020  -3.311  1.00 26.29           N  
-ANISOU 5356  N   LEU D  64     2883   2805   4300    -52   -471   -540       N  
-ATOM   5357  CA  LEU D  64     -14.692 -14.483  -4.225  1.00 24.57           C  
-ANISOU 5357  CA  LEU D  64     2581   2699   4055    -41   -488   -589       C  
-ATOM   5358  C   LEU D  64     -15.193 -13.130  -3.705  1.00 25.36           C  
-ANISOU 5358  C   LEU D  64     2690   2838   4108    -55   -425   -475       C  
-ATOM   5359  O   LEU D  64     -15.847 -13.069  -2.671  1.00 27.17           O  
-ANISOU 5359  O   LEU D  64     2933   2989   4399   -122   -378   -424       O  
-ATOM   5360  CB  LEU D  64     -15.865 -15.464  -4.308  1.00 30.42           C  
-ANISOU 5360  CB  LEU D  64     3268   3373   4919   -106   -514   -690       C  
-ATOM   5361  CG  LEU D  64     -16.468 -15.810  -5.660  1.00 40.97           C  
-ANISOU 5361  CG  LEU D  64     4497   4824   6246    -66   -585   -845       C  
-ATOM   5362  CD1 LEU D  64     -15.390 -16.435  -6.524  1.00 43.89           C  
-ANISOU 5362  CD1 LEU D  64     4872   5231   6575     16   -649   -940       C  
-ATOM   5363  CD2 LEU D  64     -17.645 -16.781  -5.497  1.00 39.79           C  
-ANISOU 5363  CD2 LEU D  64     4292   4589   6237   -171   -596   -949       C  
-ATOM   5364  N   CYS D  65     -14.895 -12.052  -4.424  1.00 23.61           N  
-ANISOU 5364  N   CYS D  65     2463   2734   3772     10   -424   -437       N  
-ATOM   5365  CA  CYS D  65     -15.330 -10.723  -4.013  1.00 24.96           C  
-ANISOU 5365  CA  CYS D  65     2661   2918   3904     14   -373   -337       C  
-ATOM   5366  C   CYS D  65     -16.727 -10.432  -4.554  1.00 24.97           C  
-ANISOU 5366  C   CYS D  65     2586   2992   3911     52   -398   -379       C  
-ATOM   5367  O   CYS D  65     -16.960 -10.503  -5.770  1.00 25.16           O  
-ANISOU 5367  O   CYS D  65     2549   3133   3877    121   -454   -443       O  
-ATOM   5368  CB  CYS D  65     -14.351  -9.682  -4.539  1.00 27.62           C  
-ANISOU 5368  CB  CYS D  65     3048   3323   4122     57   -355   -263       C  
-ATOM   5369  SG  CYS D  65     -14.791  -7.979  -4.165  1.00 27.18           S  
-ANISOU 5369  SG  CYS D  65     3055   3246   4026     73   -298   -144       S  
-ATOM   5370  N   VAL D  66     -17.662 -10.127  -3.658  1.00 25.38           N  
-ANISOU 5370  N   VAL D  66     2624   2998   4019     16   -360   -355       N  
-ATOM   5371  CA  VAL D  66     -18.988  -9.690  -4.074  1.00 22.69           C  
-ANISOU 5371  CA  VAL D  66     2200   2752   3670     70   -382   -397       C  
-ATOM   5372  C   VAL D  66     -19.013  -8.175  -4.332  1.00 23.63           C  
-ANISOU 5372  C   VAL D  66     2372   2910   3695    173   -369   -304       C  
-ATOM   5373  O   VAL D  66     -19.139  -7.377  -3.402  1.00 22.26           O  
-ANISOU 5373  O   VAL D  66     2252   2670   3537    165   -317   -236       O  
-ATOM   5374  CB  VAL D  66     -20.048 -10.073  -3.043  1.00 26.16           C  
-ANISOU 5374  CB  VAL D  66     2581   3155   4204    -12   -346   -429       C  
-ATOM   5375  CG1 VAL D  66     -21.430  -9.733  -3.581  1.00 31.08           C  
-ANISOU 5375  CG1 VAL D  66     3084   3914   4809     52   -380   -505       C  
-ATOM   5376  CG2 VAL D  66     -19.971 -11.566  -2.745  1.00 25.01           C  
-ANISOU 5376  CG2 VAL D  66     2415   2929   4159   -129   -350   -496       C  
-ATOM   5377  N   LEU D  67     -18.874  -7.793  -5.601  1.00 26.38           N  
-ANISOU 5377  N   LEU D  67     2715   3363   3946    271   -417   -300       N  
-ATOM   5378  CA  LEU D  67     -18.854  -6.383  -6.023  1.00 23.96           C  
-ANISOU 5378  CA  LEU D  67     2484   3077   3545    376   -409   -193       C  
-ATOM   5379  C   LEU D  67     -20.234  -5.762  -5.863  1.00 28.54           C  
-ANISOU 5379  C   LEU D  67     3013   3701   4132    467   -425   -210       C  
-ATOM   5380  O   LEU D  67     -21.211  -6.503  -5.780  1.00 27.29           O  
-ANISOU 5380  O   LEU D  67     2728   3616   4027    452   -453   -325       O  
-ATOM   5381  CB  LEU D  67     -18.437  -6.316  -7.497  1.00 26.83           C  
-ANISOU 5381  CB  LEU D  67     2840   3569   3785    459   -459   -183       C  
-ATOM   5382  CG  LEU D  67     -16.991  -6.666  -7.817  1.00 30.76           C  
-ANISOU 5382  CG  LEU D  67     3385   4063   4239    396   -442   -158       C  
-ATOM   5383  CD1 LEU D  67     -16.807  -6.704  -9.329  1.00 37.05           C  
-ANISOU 5383  CD1 LEU D  67     4141   5036   4900    486   -496   -172       C  
-ATOM   5384  CD2 LEU D  67     -16.057  -5.655  -7.171  1.00 31.46           C  
-ANISOU 5384  CD2 LEU D  67     3607   4034   4312    344   -366    -25       C  
-ATOM   5385  N   LYS D  68     -20.335  -4.427  -5.802  1.00 25.84           N  
-ANISOU 5385  N   LYS D  68     2763   3312   3741    560   -406   -108       N  
-ATOM   5386  CA  LYS D  68     -19.178  -3.531  -5.706  1.00 27.27           C  
-ANISOU 5386  CA  LYS D  68     3101   3377   3885    536   -355     23       C  
-ATOM   5387  C   LYS D  68     -18.803  -3.314  -4.250  1.00 27.90           C  
-ANISOU 5387  C   LYS D  68     3238   3310   4052    431   -284     39       C  
-ATOM   5388  O   LYS D  68     -17.647  -3.082  -3.938  1.00 27.36           O  
-ANISOU 5388  O   LYS D  68     3257   3158   3979    347   -237     98       O  
-ATOM   5389  CB  LYS D  68     -19.486  -2.154  -6.308  1.00 24.17           C  
-ANISOU 5389  CB  LYS D  68     2805   2968   3410    681   -367    131       C  
-ATOM   5390  CG  LYS D  68     -19.882  -2.120  -7.768  1.00 26.56           C  
-ANISOU 5390  CG  LYS D  68     3068   3431   3591    819   -438    144       C  
-ATOM   5391  CD  LYS D  68     -20.290  -0.680  -8.108  1.00 30.06           C  
-ANISOU 5391  CD  LYS D  68     3636   3819   3969    978   -445    271       C  
-ATOM   5392  CE  LYS D  68     -20.774  -0.522  -9.525  1.00 33.59           C  
-ANISOU 5392  CE  LYS D  68     4052   4438   4272   1147   -520    305       C  
-ATOM   5393  NZ  LYS D  68     -21.028   0.916  -9.761  1.00 34.56           N  
-ANISOU 5393  NZ  LYS D  68     4335   4461   4337   1300   -520    458       N  
-ATOM   5394  N   GLY D  69     -19.795  -3.382  -3.364  1.00 26.41           N  
-ANISOU 5394  N   GLY D  69     2984   3117   3932    438   -276    -23       N  
-ATOM   5395  CA  GLY D  69     -19.610  -2.983  -1.981  1.00 26.77           C  
-ANISOU 5395  CA  GLY D  69     3079   3053   4039    370   -212    -11       C  
-ATOM   5396  C   GLY D  69     -18.592  -3.818  -1.228  1.00 23.69           C  
-ANISOU 5396  C   GLY D  69     2699   2613   3689    221   -170    -15       C  
-ATOM   5397  O   GLY D  69     -18.011  -3.359  -0.228  1.00 25.11           O  
-ANISOU 5397  O   GLY D  69     2944   2707   3888    162   -115     13       O  
-ATOM   5398  N   GLY D  70     -18.380  -5.050  -1.688  1.00 21.45           N  
-ANISOU 5398  N   GLY D  70     2350   2387   3414    170   -200    -61       N  
-ATOM   5399  CA  GLY D  70     -17.409  -5.925  -1.051  1.00 21.26           C  
-ANISOU 5399  CA  GLY D  70     2341   2316   3421     58   -174    -63       C  
-ATOM   5400  C   GLY D  70     -15.948  -5.585  -1.300  1.00 24.46           C  
-ANISOU 5400  C   GLY D  70     2832   2691   3771     30   -156     -7       C  
-ATOM   5401  O   GLY D  70     -15.078  -6.149  -0.640  1.00 24.67           O  
-ANISOU 5401  O   GLY D  70     2874   2689   3813    -43   -134     -9       O  
-ATOM   5402  N   TYR D  71     -15.666  -4.664  -2.222  1.00 24.47           N  
-ANISOU 5402  N   TYR D  71     2887   2709   3701     86   -163     47       N  
-ATOM   5403  CA  TYR D  71     -14.303  -4.546  -2.757  1.00 25.04           C  
-ANISOU 5403  CA  TYR D  71     3009   2801   3706     45   -150     87       C  
-ATOM   5404  C   TYR D  71     -13.246  -4.106  -1.745  1.00 23.50           C  
-ANISOU 5404  C   TYR D  71     2875   2535   3517    -48    -88    114       C  
-ATOM   5405  O   TYR D  71     -12.116  -4.589  -1.777  1.00 22.55           O  
-ANISOU 5405  O   TYR D  71     2746   2458   3365   -103    -81    100       O  
-ATOM   5406  CB  TYR D  71     -14.256  -3.677  -4.038  1.00 24.98           C  
-ANISOU 5406  CB  TYR D  71     3048   2837   3604    113   -163    158       C  
-ATOM   5407  CG  TYR D  71     -13.756  -2.254  -3.845  1.00 28.06           C  
-ANISOU 5407  CG  TYR D  71     3563   3129   3969     86   -103    257       C  
-ATOM   5408  CD1 TYR D  71     -12.391  -1.961  -3.856  1.00 26.18           C  
-ANISOU 5408  CD1 TYR D  71     3374   2888   3686    -17    -54    294       C  
-ATOM   5409  CD2 TYR D  71     -14.649  -1.200  -3.680  1.00 27.90           C  
-ANISOU 5409  CD2 TYR D  71     3610   3021   3972    163    -98    303       C  
-ATOM   5410  CE1 TYR D  71     -11.934  -0.667  -3.674  1.00 29.87           C  
-ANISOU 5410  CE1 TYR D  71     3957   3248   4143    -70      7    375       C  
-ATOM   5411  CE2 TYR D  71     -14.197   0.108  -3.503  1.00 29.51           C  
-ANISOU 5411  CE2 TYR D  71     3946   3096   4169    135    -45    388       C  
-ATOM   5412  CZ  TYR D  71     -12.839   0.360  -3.503  1.00 31.44           C  
-ANISOU 5412  CZ  TYR D  71     4241   3324   4379      4     11    425       C  
-ATOM   5413  OH  TYR D  71     -12.378   1.644  -3.348  1.00 31.95           O  
-ANISOU 5413  OH  TYR D  71     4441   3251   4449    -52     70    501       O  
-ATOM   5414  N   LYS D  72     -13.592  -3.186  -0.859  1.00 20.37           N  
-ANISOU 5414  N   LYS D  72     2533   2050   3159    -57    -46    136       N  
-ATOM   5415  CA  LYS D  72     -12.610  -2.690   0.103  1.00 24.33           C  
-ANISOU 5415  CA  LYS D  72     3082   2499   3661   -147     11    141       C  
-ATOM   5416  C   LYS D  72     -12.324  -3.732   1.161  1.00 24.05           C  
-ANISOU 5416  C   LYS D  72     2988   2492   3656   -193     13     88       C  
-ATOM   5417  O   LYS D  72     -11.169  -3.994   1.492  1.00 21.99           O  
-ANISOU 5417  O   LYS D  72     2726   2266   3364   -253     29     74       O  
-ATOM   5418  CB  LYS D  72     -13.077  -1.383   0.773  1.00 25.32           C  
-ANISOU 5418  CB  LYS D  72     3283   2516   3822   -136     51    158       C  
-ATOM   5419  CG  LYS D  72     -12.435  -0.146   0.205  1.00 39.02           C  
-ANISOU 5419  CG  LYS D  72     5127   4177   5523   -167     85    224       C  
-ATOM   5420  CD  LYS D  72     -10.925  -0.321   0.143  1.00 47.38           C  
-ANISOU 5420  CD  LYS D  72     6182   5290   6530   -288    119    222       C  
-ATOM   5421  CE  LYS D  72     -10.212   0.681   1.010  1.00 54.18           C  
-ANISOU 5421  CE  LYS D  72     7108   6066   7413   -390    182    203       C  
-ATOM   5422  NZ  LYS D  72      -8.780   0.299   1.159  1.00 58.24           N  
-ANISOU 5422  NZ  LYS D  72     7574   6681   7873   -506    209    167       N  
-ATOM   5423  N   PHE D  73     -13.378  -4.313   1.711  1.00 22.24           N  
-ANISOU 5423  N   PHE D  73     2710   2257   3481   -163     -1     61       N  
-ATOM   5424  CA  PHE D  73     -13.202  -5.347   2.726  1.00 23.13           C  
-ANISOU 5424  CA  PHE D  73     2784   2385   3619   -205      5     36       C  
-ATOM   5425  C   PHE D  73     -12.406  -6.500   2.123  1.00 25.57           C  
-ANISOU 5425  C   PHE D  73     3069   2736   3909   -209    -36     21       C  
-ATOM   5426  O   PHE D  73     -11.523  -7.067   2.772  1.00 23.64           O  
-ANISOU 5426  O   PHE D  73     2827   2508   3648   -237    -31     15       O  
-ATOM   5427  CB  PHE D  73     -14.569  -5.808   3.232  1.00 21.95           C  
-ANISOU 5427  CB  PHE D  73     2581   2231   3527   -190      4     19       C  
-ATOM   5428  CG  PHE D  73     -14.498  -6.851   4.314  1.00 22.72           C  
-ANISOU 5428  CG  PHE D  73     2656   2332   3646   -241     21     21       C  
-ATOM   5429  CD1 PHE D  73     -13.674  -6.676   5.429  1.00 19.85           C  
-ANISOU 5429  CD1 PHE D  73     2320   1975   3245   -275     58     36       C  
-ATOM   5430  CD2 PHE D  73     -15.273  -7.998   4.230  1.00 21.59           C  
-ANISOU 5430  CD2 PHE D  73     2463   2184   3554   -258      0     11       C  
-ATOM   5431  CE1 PHE D  73     -13.632  -7.633   6.425  1.00 23.04           C  
-ANISOU 5431  CE1 PHE D  73     2714   2389   3653   -306     71     60       C  
-ATOM   5432  CE2 PHE D  73     -15.233  -8.958   5.222  1.00 23.44           C  
-ANISOU 5432  CE2 PHE D  73     2698   2400   3808   -310     22     38       C  
-ATOM   5433  CZ  PHE D  73     -14.410  -8.776   6.321  1.00 22.92           C  
-ANISOU 5433  CZ  PHE D  73     2669   2346   3691   -324     56     73       C  
-ATOM   5434  N   PHE D  74     -12.710  -6.829   0.864  1.00 22.17           N  
-ANISOU 5434  N   PHE D  74     2614   2337   3475   -166    -82      5       N  
-ATOM   5435  CA  PHE D  74     -12.006  -7.883   0.139  1.00 19.50           C  
-ANISOU 5435  CA  PHE D  74     2247   2046   3116   -152   -129    -34       C  
-ATOM   5436  C   PHE D  74     -10.516  -7.565   0.011  1.00 22.99           C  
-ANISOU 5436  C   PHE D  74     2710   2546   3480   -173   -114    -28       C  
-ATOM   5437  O   PHE D  74      -9.673  -8.412   0.323  1.00 23.18           O  
-ANISOU 5437  O   PHE D  74     2719   2597   3493   -171   -132    -61       O  
-ATOM   5438  CB  PHE D  74     -12.666  -8.101  -1.247  1.00 17.41           C  
-ANISOU 5438  CB  PHE D  74     1939   1831   2844    -95   -181    -67       C  
-ATOM   5439  CG  PHE D  74     -11.968  -9.128  -2.134  1.00 24.03           C  
-ANISOU 5439  CG  PHE D  74     2740   2734   3656    -66   -236   -132       C  
-ATOM   5440  CD1 PHE D  74     -12.249 -10.490  -2.019  1.00 23.02           C  
-ANISOU 5440  CD1 PHE D  74     2580   2563   3601    -62   -279   -200       C  
-ATOM   5441  CD2 PHE D  74     -11.083  -8.713  -3.127  1.00 24.09           C  
-ANISOU 5441  CD2 PHE D  74     2745   2844   3565    -43   -243   -130       C  
-ATOM   5442  CE1 PHE D  74     -11.637 -11.429  -2.866  1.00 25.49           C  
-ANISOU 5442  CE1 PHE D  74     2861   2926   3897    -18   -338   -283       C  
-ATOM   5443  CE2 PHE D  74     -10.459  -9.638  -3.971  1.00 27.71           C  
-ANISOU 5443  CE2 PHE D  74     3154   3387   3987     -2   -296   -210       C  
-ATOM   5444  CZ  PHE D  74     -10.742 -10.998  -3.847  1.00 24.66           C  
-ANISOU 5444  CZ  PHE D  74     2737   2949   3682     21   -349   -296       C  
-ATOM   5445  N   ALA D  75     -10.180  -6.360  -0.447  1.00 22.51           N  
-ANISOU 5445  N   ALA D  75     2683   2507   3363   -194    -80     11       N  
-ATOM   5446  CA  ALA D  75      -8.770  -6.031  -0.684  1.00 23.42           C  
-ANISOU 5446  CA  ALA D  75     2800   2701   3396   -240    -57      8       C  
-ATOM   5447  C   ALA D  75      -8.007  -6.102   0.626  1.00 24.57           C  
-ANISOU 5447  C   ALA D  75     2946   2845   3546   -288    -27    -14       C  
-ATOM   5448  O   ALA D  75      -6.885  -6.610   0.682  1.00 20.32           O  
-ANISOU 5448  O   ALA D  75     2368   2398   2953   -293    -38    -57       O  
-ATOM   5449  CB  ALA D  75      -8.619  -4.650  -1.288  1.00 21.64           C  
-ANISOU 5449  CB  ALA D  75     2631   2470   3123   -282    -10     71       C  
-ATOM   5450  N   ASP D  76      -8.613  -5.571   1.680  1.00 21.08           N  
-ANISOU 5450  N   ASP D  76     2538   2320   3153   -311      7      6       N  
-ATOM   5451  CA  ASP D  76      -7.938  -5.477   2.977  1.00 21.72           C  
-ANISOU 5451  CA  ASP D  76     2614   2420   3219   -354     38    -18       C  
-ATOM   5452  C   ASP D  76      -7.814  -6.824   3.671  1.00 20.66           C  
-ANISOU 5452  C   ASP D  76     2448   2309   3095   -306      0    -36       C  
-ATOM   5453  O   ASP D  76      -6.752  -7.157   4.207  1.00 21.49           O  
-ANISOU 5453  O   ASP D  76     2527   2493   3144   -305     -4    -68       O  
-ATOM   5454  CB  ASP D  76      -8.667  -4.476   3.883  1.00 24.64           C  
-ANISOU 5454  CB  ASP D  76     3025   2708   3631   -383     85     -5       C  
-ATOM   5455  CG  ASP D  76      -8.477  -3.048   3.439  1.00 28.69           C  
-ANISOU 5455  CG  ASP D  76     3594   3173   4134   -439    128      9       C  
-ATOM   5456  OD1 ASP D  76      -7.526  -2.779   2.676  1.00 31.13           O  
-ANISOU 5456  OD1 ASP D  76     3905   3535   4389   -488    139     12       O  
-ATOM   5457  OD2 ASP D  76      -9.279  -2.191   3.856  1.00 28.14           O  
-ANISOU 5457  OD2 ASP D  76     3570   3011   4110   -433    153     17       O  
-ATOM   5458  N   LEU D  77      -8.902  -7.588   3.676  1.00 21.63           N  
-ANISOU 5458  N   LEU D  77     2572   2361   3283   -266    -26    -16       N  
-ATOM   5459  CA  LEU D  77      -8.887  -8.931   4.252  1.00 22.05           C  
-ANISOU 5459  CA  LEU D  77     2620   2397   3360   -228    -59    -13       C  
-ATOM   5460  C   LEU D  77      -7.838  -9.778   3.551  1.00 21.20           C  
-ANISOU 5460  C   LEU D  77     2493   2349   3215   -175   -113    -57       C  
-ATOM   5461  O   LEU D  77      -7.054 -10.481   4.205  1.00 22.69           O  
-ANISOU 5461  O   LEU D  77     2681   2569   3370   -133   -134    -65       O  
-ATOM   5462  CB  LEU D  77     -10.260  -9.608   4.125  1.00 22.36           C  
-ANISOU 5462  CB  LEU D  77     2660   2348   3488   -223    -73      7       C  
-ATOM   5463  CG  LEU D  77     -10.371 -11.018   4.729  1.00 25.38           C  
-ANISOU 5463  CG  LEU D  77     3061   2671   3912   -205    -98     29       C  
-ATOM   5464  CD1 LEU D  77     -10.102 -11.008   6.237  1.00 25.94           C  
-ANISOU 5464  CD1 LEU D  77     3156   2757   3944   -218    -58     82       C  
-ATOM   5465  CD2 LEU D  77     -11.744 -11.625   4.440  1.00 25.00           C  
-ANISOU 5465  CD2 LEU D  77     3001   2541   3958   -234   -104     32       C  
-ATOM   5466  N   LEU D  78      -7.804  -9.721   2.222  1.00 21.07           N  
-ANISOU 5466  N   LEU D  78     2453   2364   3189   -159   -140    -90       N  
-ATOM   5467  CA  LEU D  78      -6.783 -10.479   1.499  1.00 21.47           C  
-ANISOU 5467  CA  LEU D  78     2468   2498   3190    -99   -192   -153       C  
-ATOM   5468  C   LEU D  78      -5.361 -10.008   1.804  1.00 22.48           C  
-ANISOU 5468  C   LEU D  78     2564   2761   3217   -112   -172   -183       C  
-ATOM   5469  O   LEU D  78      -4.432 -10.831   1.880  1.00 24.30           O  
-ANISOU 5469  O   LEU D  78     2764   3064   3406    -40   -216   -236       O  
-ATOM   5470  CB  LEU D  78      -7.034 -10.503  -0.020  1.00 20.48           C  
-ANISOU 5470  CB  LEU D  78     2312   2415   3055    -76   -224   -192       C  
-ATOM   5471  CG  LEU D  78      -7.721 -11.758  -0.530  1.00 28.25           C  
-ANISOU 5471  CG  LEU D  78     3289   3328   4116    -16   -289   -240       C  
-ATOM   5472  CD1 LEU D  78      -9.067 -11.911   0.163  1.00 24.85           C  
-ANISOU 5472  CD1 LEU D  78     2894   2761   3788    -56   -271   -191       C  
-ATOM   5473  CD2 LEU D  78      -7.886 -11.702  -2.050  1.00 31.23           C  
-ANISOU 5473  CD2 LEU D  78     3618   3791   4457     15   -323   -296       C  
-ATOM   5474  N   ASP D  79      -5.171  -8.705   1.989  1.00 20.89           N  
-ANISOU 5474  N   ASP D  79     2366   2594   2979   -201   -108   -159       N  
-ATOM   5475  CA  ASP D  79      -3.834  -8.204   2.307  1.00 18.87           C  
-ANISOU 5475  CA  ASP D  79     2063   2477   2629   -243    -81   -204       C  
-ATOM   5476  C   ASP D  79      -3.372  -8.723   3.663  1.00 23.17           C  
-ANISOU 5476  C   ASP D  79     2600   3048   3157   -201    -94   -221       C  
-ATOM   5477  O   ASP D  79      -2.203  -9.039   3.851  1.00 19.72           O  
-ANISOU 5477  O   ASP D  79     2102   2752   2638   -164   -115   -284       O  
-ATOM   5478  CB  ASP D  79      -3.797  -6.674   2.293  1.00 24.95           C  
-ANISOU 5478  CB  ASP D  79     2855   3242   3383   -367     -4   -179       C  
-ATOM   5479  CG  ASP D  79      -3.603  -6.107   0.892  1.00 31.78           C  
-ANISOU 5479  CG  ASP D  79     3714   4157   4205   -411     14   -164       C  
-ATOM   5480  OD1 ASP D  79      -3.402  -6.905  -0.050  1.00 32.71           O  
-ANISOU 5480  OD1 ASP D  79     3789   4351   4290   -343    -34   -194       O  
-ATOM   5481  OD2 ASP D  79      -3.636  -4.862   0.742  1.00 29.00           O  
-ANISOU 5481  OD2 ASP D  79     3405   3767   3849   -513     77   -124       O  
-ATOM   5482  N   TYR D  80      -4.288  -8.803   4.621  1.00 21.37           N  
-ANISOU 5482  N   TYR D  80     2423   2706   2991   -199    -81   -164       N  
-ATOM   5483  CA  TYR D  80      -3.923  -9.353   5.922  1.00 20.85           C  
-ANISOU 5483  CA  TYR D  80     2357   2673   2892   -148    -93   -160       C  
-ATOM   5484  C   TYR D  80      -3.627 -10.847   5.809  1.00 21.72           C  
-ANISOU 5484  C   TYR D  80     2477   2771   3005    -21   -168   -161       C  
-ATOM   5485  O   TYR D  80      -2.703 -11.362   6.447  1.00 21.96           O  
-ANISOU 5485  O   TYR D  80     2484   2898   2962     59   -201   -187       O  
-ATOM   5486  CB  TYR D  80      -5.030  -9.099   6.953  1.00 20.81           C  
-ANISOU 5486  CB  TYR D  80     2401   2567   2940   -181    -54    -93       C  
-ATOM   5487  CG  TYR D  80      -4.985  -7.722   7.572  1.00 22.03           C  
-ANISOU 5487  CG  TYR D  80     2543   2760   3069   -272     11   -119       C  
-ATOM   5488  CD1 TYR D  80      -3.936  -7.358   8.410  1.00 23.60           C  
-ANISOU 5488  CD1 TYR D  80     2693   3098   3178   -286     23   -180       C  
-ATOM   5489  CD2 TYR D  80      -5.983  -6.778   7.315  1.00 24.51           C  
-ANISOU 5489  CD2 TYR D  80     2890   2974   3449   -337     54    -98       C  
-ATOM   5490  CE1 TYR D  80      -3.877  -6.092   8.988  1.00 28.03           C  
-ANISOU 5490  CE1 TYR D  80     3241   3683   3725   -379     81   -228       C  
-ATOM   5491  CE2 TYR D  80      -5.934  -5.507   7.898  1.00 23.76           C  
-ANISOU 5491  CE2 TYR D  80     2797   2888   3342   -412    108   -136       C  
-ATOM   5492  CZ  TYR D  80      -4.876  -5.177   8.729  1.00 26.33           C  
-ANISOU 5492  CZ  TYR D  80     3077   3339   3589   -441    123   -206       C  
-ATOM   5493  OH  TYR D  80      -4.814  -3.929   9.317  1.00 26.92           O  
-ANISOU 5493  OH  TYR D  80     3153   3414   3663   -524    176   -266       O  
-ATOM   5494  N   ILE D  81      -4.402 -11.553   4.999  1.00 20.69           N  
-ANISOU 5494  N   ILE D  81     2382   2523   2958      7   -201   -143       N  
-ATOM   5495  CA  ILE D  81      -4.125 -12.983   4.762  1.00 22.17           C  
-ANISOU 5495  CA  ILE D  81     2591   2665   3167    127   -278   -162       C  
-ATOM   5496  C   ILE D  81      -2.769 -13.180   4.070  1.00 21.27           C  
-ANISOU 5496  C   ILE D  81     2404   2715   2962    206   -325   -265       C  
-ATOM   5497  O   ILE D  81      -1.988 -14.055   4.460  1.00 25.44           O  
-ANISOU 5497  O   ILE D  81     2933   3283   3449    329   -381   -293       O  
-ATOM   5498  CB  ILE D  81      -5.258 -13.646   3.942  1.00 27.76           C  
-ANISOU 5498  CB  ILE D  81     3338   3217   3990    121   -303   -152       C  
-ATOM   5499  CG1 ILE D  81      -6.503 -13.822   4.813  1.00 28.68           C  
-ANISOU 5499  CG1 ILE D  81     3519   3188   4191     62   -265    -56       C  
-ATOM   5500  CG2 ILE D  81      -4.813 -14.998   3.383  1.00 27.65           C  
-ANISOU 5500  CG2 ILE D  81     3341   3161   4004    243   -387   -212       C  
-ATOM   5501  CD1 ILE D  81      -7.772 -14.101   4.008  1.00 31.99           C  
-ANISOU 5501  CD1 ILE D  81     3946   3492   4719     14   -270    -62       C  
-ATOM   5502  N   LYS D  82      -2.466 -12.364   3.056  1.00 22.80           N  
-ANISOU 5502  N   LYS D  82     2533   3016   3113    141   -300   -319       N  
-ATOM   5503  CA  LYS D  82      -1.141 -12.427   2.410  1.00 24.62           C  
-ANISOU 5503  CA  LYS D  82     2670   3447   3237    193   -328   -423       C  
-ATOM   5504  C   LYS D  82       0.002 -12.171   3.392  1.00 24.59           C  
-ANISOU 5504  C   LYS D  82     2609   3605   3130    211   -320   -460       C  
-ATOM   5505  O   LYS D  82       1.055 -12.823   3.341  1.00 26.43           O  
-ANISOU 5505  O   LYS D  82     2778   3980   3284    330   -377   -545       O  
-ATOM   5506  CB  LYS D  82      -1.057 -11.441   1.243  1.00 26.32           C  
-ANISOU 5506  CB  LYS D  82     2832   3759   3411     88   -282   -446       C  
-ATOM   5507  CG  LYS D  82      -1.746 -11.968  -0.023  1.00 31.15           C  
-ANISOU 5507  CG  LYS D  82     3453   4310   4072    128   -321   -464       C  
-ATOM   5508  CD  LYS D  82      -2.476 -10.862  -0.771  1.00 35.22           C  
-ANISOU 5508  CD  LYS D  82     3984   4804   4595     12   -261   -404       C  
-ATOM   5509  CE  LYS D  82      -1.525  -9.769  -1.194  1.00 36.77           C  
-ANISOU 5509  CE  LYS D  82     4119   5176   4677    -86   -199   -415       C  
-ATOM   5510  NZ  LYS D  82      -2.260  -8.673  -1.894  1.00 38.77           N  
-ANISOU 5510  NZ  LYS D  82     4415   5377   4937   -186   -141   -332       N  
-ATOM   5511  N   ALA D  83      -0.207 -11.219   4.296  1.00 20.74           N  
-ANISOU 5511  N   ALA D  83     2135   3109   2636    105   -254   -412       N  
-ATOM   5512  CA  ALA D  83       0.804 -10.917   5.301  1.00 23.17           C  
-ANISOU 5512  CA  ALA D  83     2378   3583   2843    112   -245   -461       C  
-ATOM   5513  C   ALA D  83       1.081 -12.147   6.180  1.00 28.87           C  
-ANISOU 5513  C   ALA D  83     3129   4299   3541    290   -320   -446       C  
-ATOM   5514  O   ALA D  83       2.237 -12.435   6.522  1.00 28.51           O  
-ANISOU 5514  O   ALA D  83     3003   4444   3386    387   -361   -526       O  
-ATOM   5515  CB  ALA D  83       0.381  -9.719   6.146  1.00 26.31           C  
-ANISOU 5515  CB  ALA D  83     2794   3949   3253    -29   -165   -423       C  
-ATOM   5516  N   LEU D  84       0.024 -12.867   6.548  1.00 25.21           N  
-ANISOU 5516  N   LEU D  84     2780   3623   3175    334   -337   -341       N  
-ATOM   5517  CA  LEU D  84       0.195 -14.097   7.326  1.00 26.22           C  
-ANISOU 5517  CA  LEU D  84     2970   3701   3292    501   -405   -296       C  
-ATOM   5518  C   LEU D  84       0.973 -15.121   6.505  1.00 29.72           C  
-ANISOU 5518  C   LEU D  84     3390   4187   3716    661   -495   -381       C  
-ATOM   5519  O   LEU D  84       1.880 -15.805   7.009  1.00 31.14           O  
-ANISOU 5519  O   LEU D  84     3553   4466   3812    828   -561   -414       O  
-ATOM   5520  CB  LEU D  84      -1.174 -14.676   7.716  1.00 26.80           C  
-ANISOU 5520  CB  LEU D  84     3174   3520   3487    480   -392   -162       C  
-ATOM   5521  CG  LEU D  84      -1.979 -13.900   8.752  1.00 28.61           C  
-ANISOU 5521  CG  LEU D  84     3430   3718   3723    364   -314    -75       C  
-ATOM   5522  CD1 LEU D  84      -3.326 -14.539   8.978  1.00 28.11           C  
-ANISOU 5522  CD1 LEU D  84     3474   3430   3776    332   -297     44       C  
-ATOM   5523  CD2 LEU D  84      -1.217 -13.875  10.046  1.00 27.53           C  
-ANISOU 5523  CD2 LEU D  84     3269   3730   3460    438   -320    -63       C  
-ATOM   5524  N   ASN D  85       0.628 -15.219   5.228  1.00 28.34           N  
-ANISOU 5524  N   ASN D  85     3207   3951   3608    627   -503   -427       N  
-ATOM   5525  CA  ASN D  85       1.197 -16.257   4.372  1.00 28.75           C  
-ANISOU 5525  CA  ASN D  85     3243   4021   3658    784   -592   -522       C  
-ATOM   5526  C   ASN D  85       2.661 -16.064   4.002  1.00 34.25           C  
-ANISOU 5526  C   ASN D  85     3793   5012   4209    861   -621   -666       C  
-ATOM   5527  O   ASN D  85       3.335 -17.024   3.623  1.00 39.83           O  
-ANISOU 5527  O   ASN D  85     4477   5768   4886   1044   -709   -757       O  
-ATOM   5528  CB  ASN D  85       0.365 -16.397   3.089  1.00 29.97           C  
-ANISOU 5528  CB  ASN D  85     3416   4055   3915    725   -592   -547       C  
-ATOM   5529  CG  ASN D  85      -0.732 -17.443   3.203  1.00 43.89           C  
-ANISOU 5529  CG  ASN D  85     5316   5532   5828    759   -626   -474       C  
-ATOM   5530  OD1 ASN D  85      -0.533 -18.609   2.867  1.00 52.33           O  
-ANISOU 5530  OD1 ASN D  85     6430   6512   6942    902   -709   -530       O  
-ATOM   5531  ND2 ASN D  85      -1.902 -17.027   3.658  1.00 45.79           N  
-ANISOU 5531  ND2 ASN D  85     5620   5628   6149    622   -561   -361       N  
-ATOM   5532  N   ARG D  86       3.156 -14.831   4.060  1.00 30.35           N  
-ANISOU 5532  N   ARG D  86     3201   4183   4147    102    -70    -31       N  
-ATOM   5533  CA  ARG D  86       4.558 -14.601   3.724  1.00 31.74           C  
-ANISOU 5533  CA  ARG D  86     3200   4523   4337    181    -81   -222       C  
-ATOM   5534  C   ARG D  86       5.406 -14.481   4.981  1.00 33.93           C  
-ANISOU 5534  C   ARG D  86     3440   4894   4557    154   -207    -90       C  
-ATOM   5535  O   ARG D  86       6.599 -14.194   4.914  1.00 35.90           O  
-ANISOU 5535  O   ARG D  86     3522   5334   4784    191   -222   -228       O  
-ATOM   5536  CB  ARG D  86       4.735 -13.377   2.812  1.00 31.92           C  
-ANISOU 5536  CB  ARG D  86     3208   4759   4161     59    133   -386       C  
-ATOM   5537  CG  ARG D  86       4.333 -12.059   3.451  1.00 32.58           C  
-ANISOU 5537  CG  ARG D  86     3453   4915   4011   -121    237   -262       C  
-ATOM   5538  CD  ARG D  86       4.654 -10.858   2.565  1.00 30.91           C  
-ANISOU 5538  CD  ARG D  86     3270   4853   3621   -277    355   -383       C  
-ATOM   5539  NE  ARG D  86       4.185  -9.641   3.209  1.00 31.24           N  
-ANISOU 5539  NE  ARG D  86     3496   4868   3505   -405    395   -289       N  
-ATOM   5540  CZ  ARG D  86       3.017  -9.067   2.952  1.00 31.82           C  
-ANISOU 5540  CZ  ARG D  86     3723   4798   3570   -423    431   -259       C  
-ATOM   5541  NH1 ARG D  86       2.221  -9.589   2.030  1.00 28.63           N  
-ANISOU 5541  NH1 ARG D  86     3316   4292   3271   -362    443   -277       N  
-ATOM   5542  NH2 ARG D  86       2.656  -7.972   3.613  1.00 27.98           N  
-ANISOU 5542  NH2 ARG D  86     3377   4271   2982   -489    436   -241       N  
-ATOM   5543  N   ASN D  87       4.791 -14.716   6.134  1.00 31.18           N  
-ANISOU 5543  N   ASN D  87     3231   4460   4158     52   -303    176       N  
-ATOM   5544  CA  ASN D  87       5.536 -14.654   7.384  1.00 37.60           C  
-ANISOU 5544  CA  ASN D  87     4024   5377   4887    -21   -448    336       C  
-ATOM   5545  C   ASN D  87       5.401 -15.923   8.221  1.00 39.65           C  
-ANISOU 5545  C   ASN D  87     4345   5423   5299    -18   -770    599       C  
-ATOM   5546  O   ASN D  87       5.863 -15.978   9.351  1.00 41.51           O  
-ANISOU 5546  O   ASN D  87     4596   5733   5443   -131   -938    800       O  
-ATOM   5547  CB  ASN D  87       5.151 -13.403   8.173  1.00 35.80           C  
-ANISOU 5547  CB  ASN D  87     3905   5356   4341   -250   -263    401       C  
-ATOM   5548  CG  ASN D  87       5.721 -12.133   7.550  1.00 36.62           C  
-ANISOU 5548  CG  ASN D  87     3968   5635   4310   -280    -70    187       C  
-ATOM   5549  OD1 ASN D  87       6.938 -11.948   7.517  1.00 36.66           O  
-ANISOU 5549  OD1 ASN D  87     3836   5789   4303   -262   -119    104       O  
-ATOM   5550  ND2 ASN D  87       4.847 -11.263   7.044  1.00 32.10           N  
-ANISOU 5550  ND2 ASN D  87     3512   5045   3640   -344    115    105       N  
-ATOM   5551  N   SER D  88       4.780 -16.945   7.637  1.00 41.42           N  
-ANISOU 5551  N   SER D  88     4621   5371   5747     81   -887    610       N  
-ATOM   5552  CA  SER D  88       4.671 -18.253   8.279  1.00 45.64           C  
-ANISOU 5552  CA  SER D  88     5254   5616   6470     69  -1269    873       C  
-ATOM   5553  C   SER D  88       5.500 -19.308   7.541  1.00 46.45           C  
-ANISOU 5553  C   SER D  88     5228   5432   6990    412  -1550    681       C  
-ATOM   5554  O   SER D  88       5.862 -19.125   6.375  1.00 44.23           O  
-ANISOU 5554  O   SER D  88     4776   5209   6818    622  -1380    316       O  
-ATOM   5555  CB  SER D  88       3.213 -18.694   8.344  1.00 48.32           C  
-ANISOU 5555  CB  SER D  88     5787   5837   6736   -140  -1245   1063       C  
-ATOM   5556  OG  SER D  88       2.706 -18.940   7.045  1.00 55.38           O  
-ANISOU 5556  OG  SER D  88     6660   6588   7793     15  -1121    834       O  
-ATOM   5557  N   ASP D  89       5.787 -20.409   8.231  1.00 43.69           N  
-ANISOU 5557  N   ASP D  89     4955   4778   6866    450  -2003    914       N  
-ATOM   5558  CA  ASP D  89       6.631 -21.483   7.700  1.00 54.49           C  
-ANISOU 5558  CA  ASP D  89     6192   5814   8698    828  -2364    707       C  
-ATOM   5559  C   ASP D  89       6.064 -22.117   6.431  1.00 60.49           C  
-ANISOU 5559  C   ASP D  89     6959   6331   9694   1003  -2308    429       C  
-ATOM   5560  O   ASP D  89       6.791 -22.355   5.461  1.00 63.81           O  
-ANISOU 5560  O   ASP D  89     7137   6741  10368   1338  -2300     -9       O  
-ATOM   5561  CB  ASP D  89       6.832 -22.570   8.759  1.00 55.60           C  
-ANISOU 5561  CB  ASP D  89     6499   5578   9047    788  -2948   1092       C  
-ATOM   5562  CG  ASP D  89       7.609 -22.073   9.964  1.00 62.50           C  
-ANISOU 5562  CG  ASP D  89     7325   6693   9730    650  -3074   1335       C  
-ATOM   5563  OD1 ASP D  89       8.220 -20.985   9.868  1.00 56.57           O  
-ANISOU 5563  OD1 ASP D  89     6365   6361   8769    677  -2740   1122       O  
-ATOM   5564  OD2 ASP D  89       7.612 -22.772  11.002  1.00 69.34           O  
-ANISOU 5564  OD2 ASP D  89     8389   7353  10607    455  -3455   1715       O  
-ATOM   5565  N   ARG D  90       4.769 -22.408   6.452  1.00 57.51           N  
-ANISOU 5565  N   ARG D  90     6837   5804   9212    752  -2271    660       N  
-ATOM   5566  CA  ARG D  90       4.112 -22.997   5.295  1.00 59.88           C  
-ANISOU 5566  CA  ARG D  90     7173   5884   9695    858  -2216    432       C  
-ATOM   5567  C   ARG D  90       2.884 -22.169   4.938  1.00 56.45           C  
-ANISOU 5567  C   ARG D  90     6823   5718   8906    580  -1782    483       C  
-ATOM   5568  O   ARG D  90       2.293 -21.510   5.796  1.00 61.18           O  
-ANISOU 5568  O   ARG D  90     7523   6542   9179    281  -1642    768       O  
-ATOM   5569  CB  ARG D  90       3.748 -24.462   5.556  1.00 66.96           C  
-ANISOU 5569  CB  ARG D  90     8303   6222  10916    858  -2726    648       C  
-ATOM   5570  CG  ARG D  90       4.911 -25.297   6.098  1.00 77.46           C  
-ANISOU 5570  CG  ARG D  90     9587   7304  12539   1067  -3161    622       C  
-ATOM   5571  CD  ARG D  90       5.274 -26.457   5.175  1.00 86.08           C  
-ANISOU 5571  CD  ARG D  90    10630   8086  13991   1341  -3334    213       C  
-ATOM   5572  NE  ARG D  90       5.806 -26.008   3.890  1.00 85.92           N  
-ANISOU 5572  NE  ARG D  90    10292   8318  14033   1648  -3005   -355       N  
-ATOM   5573  CZ  ARG D  90       5.968 -26.796   2.828  1.00 87.87           C  
-ANISOU 5573  CZ  ARG D  90    10453   8434  14499   1847  -3031   -783       C  
-ATOM   5574  NH1 ARG D  90       5.635 -28.078   2.889  1.00 87.51           N  
-ANISOU 5574  NH1 ARG D  90    10615   7953  14683   1821  -3402   -712       N  
-ATOM   5575  NH2 ARG D  90       6.456 -26.297   1.700  1.00 88.89           N  
-ANISOU 5575  NH2 ARG D  90    10283   8909  14581   2025  -2693  -1280       N  
-ATOM   5576  N   SER D  91       2.515 -22.190   3.665  1.00 48.42           N  
-ANISOU 5576  N   SER D  91     5743   4701   7955    686  -1579    175       N  
-ATOM   5577  CA  SER D  91       1.455 -21.329   3.165  1.00 41.06           C  
-ANISOU 5577  CA  SER D  91     4848   4027   6727    482  -1193    174       C  
-ATOM   5578  C   SER D  91       0.696 -22.067   2.071  1.00 42.71           C  
-ANISOU 5578  C   SER D  91     5115   4026   7088    511  -1198     19       C  
-ATOM   5579  O   SER D  91       1.159 -23.104   1.593  1.00 43.99           O  
-ANISOU 5579  O   SER D  91     5253   3879   7580    727  -1452   -177       O  
-ATOM   5580  CB  SER D  91       2.065 -20.055   2.591  1.00 36.60           C  
-ANISOU 5580  CB  SER D  91     4089   3842   5975    546   -856    -88       C  
-ATOM   5581  OG  SER D  91       2.927 -20.366   1.517  1.00 46.05           O  
-ANISOU 5581  OG  SER D  91     5085   5044   7367    792   -856   -490       O  
-ATOM   5582  N   ILE D  92      -0.457 -21.530   1.670  1.00 35.41           N  
-ANISOU 5582  N   ILE D  92     4250   3267   5938    311   -938     77       N  
-ATOM   5583  CA  ILE D  92      -1.248 -22.132   0.590  1.00 34.46           C  
-ANISOU 5583  CA  ILE D  92     4178   3003   5914    296   -917    -63       C  
-ATOM   5584  C   ILE D  92      -1.545 -21.127  -0.518  1.00 28.93           C  
-ANISOU 5584  C   ILE D  92     3361   2610   5021    279   -566   -286       C  
-ATOM   5585  O   ILE D  92      -1.692 -19.936  -0.259  1.00 27.75           O  
-ANISOU 5585  O   ILE D  92     3177   2741   4626    187   -351   -209       O  
-ATOM   5586  CB  ILE D  92      -2.588 -22.735   1.093  1.00 54.22           C  
-ANISOU 5586  CB  ILE D  92     6887   5367   8348     10  -1030    270       C  
-ATOM   5587  CG1 ILE D  92      -3.120 -21.943   2.286  1.00 55.10           C  
-ANISOU 5587  CG1 ILE D  92     7028   5759   8148   -237   -914    580       C  
-ATOM   5588  CG2 ILE D  92      -2.432 -24.216   1.438  1.00 58.19           C  
-ANISOU 5588  CG2 ILE D  92     7562   5396   9151     21  -1475    394       C  
-ATOM   5589  CD1 ILE D  92      -3.874 -20.697   1.908  1.00 53.85           C  
-ANISOU 5589  CD1 ILE D  92     6769   5962   7728   -307   -551    501       C  
-ATOM   5590  N   PRO D  93      -1.629 -21.607  -1.767  1.00 34.49           N  
-ANISOU 5590  N   PRO D  93     4018   3249   5838    351   -540   -569       N  
-ATOM   5591  CA  PRO D  93      -1.971 -20.644  -2.816  1.00 34.29           C  
-ANISOU 5591  CA  PRO D  93     3910   3525   5593    264   -251   -718       C  
-ATOM   5592  C   PRO D  93      -3.400 -20.130  -2.668  1.00 28.17           C  
-ANISOU 5592  C   PRO D  93     3245   2832   4624     45   -142   -455       C  
-ATOM   5593  O   PRO D  93      -4.272 -20.822  -2.133  1.00 28.06           O  
-ANISOU 5593  O   PRO D  93     3351   2657   4653    -69   -267   -242       O  
-ATOM   5594  CB  PRO D  93      -1.810 -21.451  -4.113  1.00 40.62           C  
-ANISOU 5594  CB  PRO D  93     4641   4249   6544    346   -277  -1077       C  
-ATOM   5595  CG  PRO D  93      -1.806 -22.898  -3.686  1.00 44.46           C  
-ANISOU 5595  CG  PRO D  93     5234   4303   7356    461   -600  -1062       C  
-ATOM   5596  CD  PRO D  93      -1.208 -22.909  -2.310  1.00 41.41           C  
-ANISOU 5596  CD  PRO D  93     4886   3806   7041    533   -778   -820       C  
-ATOM   5597  N   MET D  94      -3.619 -18.904  -3.121  1.00 24.96           N  
-ANISOU 5597  N   MET D  94     2791   2689   4006    -25     61   -475       N  
-ATOM   5598  CA  MET D  94      -4.943 -18.312  -3.131  1.00 24.76           C  
-ANISOU 5598  CA  MET D  94     2814   2761   3832   -171    148   -305       C  
-ATOM   5599  C   MET D  94      -5.169 -17.708  -4.507  1.00 29.52           C  
-ANISOU 5599  C   MET D  94     3379   3507   4331   -231    255   -452       C  
-ATOM   5600  O   MET D  94      -4.288 -17.039  -5.046  1.00 25.66           O  
-ANISOU 5600  O   MET D  94     2834   3158   3757   -222    324   -595       O  
-ATOM   5601  CB  MET D  94      -5.045 -17.215  -2.064  1.00 26.15           C  
-ANISOU 5601  CB  MET D  94     2989   3081   3865   -186    219   -146       C  
-ATOM   5602  CG  MET D  94      -6.405 -16.496  -2.037  1.00 30.55           C  
-ANISOU 5602  CG  MET D  94     3539   3767   4303   -274    295    -48       C  
-ATOM   5603  SD  MET D  94      -6.622 -15.514  -0.540  1.00 42.31           S  
-ANISOU 5603  SD  MET D  94     5000   5416   5662   -274    355     61       S  
-ATOM   5604  CE  MET D  94      -4.992 -14.769  -0.372  1.00 45.58           C  
-ANISOU 5604  CE  MET D  94     5434   5830   6054   -177    371    -26       C  
-ATOM   5605  N   THR D  95      -6.330 -17.968  -5.092  1.00 26.31           N  
-ANISOU 5605  N   THR D  95     3000   3092   3906   -338    250   -404       N  
-ATOM   5606  CA  THR D  95      -6.681 -17.322  -6.349  1.00 26.25           C  
-ANISOU 5606  CA  THR D  95     2972   3230   3772   -439    311   -482       C  
-ATOM   5607  C   THR D  95      -7.876 -16.430  -6.066  1.00 27.39           C  
-ANISOU 5607  C   THR D  95     3123   3451   3833   -481    315   -292       C  
-ATOM   5608  O   THR D  95      -8.515 -16.552  -5.010  1.00 24.48           O  
-ANISOU 5608  O   THR D  95     2741   3066   3494   -455    304   -158       O  
-ATOM   5609  CB  THR D  95      -7.014 -18.326  -7.463  1.00 28.82           C  
-ANISOU 5609  CB  THR D  95     3297   3512   4144   -527    280   -634       C  
-ATOM   5610  OG1 THR D  95      -7.942 -19.297  -6.968  1.00 32.36           O  
-ANISOU 5610  OG1 THR D  95     3798   3794   4703   -561    192   -510       O  
-ATOM   5611  CG2 THR D  95      -5.734 -19.033  -7.963  1.00 31.98           C  
-ANISOU 5611  CG2 THR D  95     3633   3889   4629   -448    282   -945       C  
-ATOM   5612  N   VAL D  96      -8.185 -15.527  -6.993  1.00 28.25           N  
-ANISOU 5612  N   VAL D  96     3238   3664   3832   -559    308   -291       N  
-ATOM   5613  CA  VAL D  96      -9.289 -14.597  -6.749  1.00 28.36           C  
-ANISOU 5613  CA  VAL D  96     3234   3720   3824   -534    259   -157       C  
-ATOM   5614  C   VAL D  96     -10.271 -14.543  -7.916  1.00 30.72           C  
-ANISOU 5614  C   VAL D  96     3519   4073   4080   -653    180   -126       C  
-ATOM   5615  O   VAL D  96      -9.909 -14.810  -9.061  1.00 30.70           O  
-ANISOU 5615  O   VAL D  96     3553   4113   3998   -801    171   -201       O  
-ATOM   5616  CB  VAL D  96      -8.791 -13.166  -6.423  1.00 32.88           C  
-ANISOU 5616  CB  VAL D  96     3854   4294   4344   -466    229   -127       C  
-ATOM   5617  CG1 VAL D  96      -7.803 -13.187  -5.287  1.00 33.61           C  
-ANISOU 5617  CG1 VAL D  96     3953   4365   4453   -375    304   -156       C  
-ATOM   5618  CG2 VAL D  96      -8.162 -12.523  -7.640  1.00 36.44           C  
-ANISOU 5618  CG2 VAL D  96     4390   4786   4668   -624    167   -145       C  
-ATOM   5619  N   ASP D  97     -11.524 -14.217  -7.607  1.00 26.05           N  
-ANISOU 5619  N   ASP D  97     2845   3524   3530   -599    122    -42       N  
-ATOM   5620  CA  ASP D  97     -12.507 -13.932  -8.638  1.00 27.97           C  
-ANISOU 5620  CA  ASP D  97     3055   3825   3745   -684     -1     12       C  
-ATOM   5621  C   ASP D  97     -13.465 -12.867  -8.108  1.00 27.35           C  
-ANISOU 5621  C   ASP D  97     2872   3774   3747   -510   -110     55       C  
-ATOM   5622  O   ASP D  97     -13.476 -12.554  -6.905  1.00 30.51           O  
-ANISOU 5622  O   ASP D  97     3201   4191   4201   -351    -45      9       O  
-ATOM   5623  CB  ASP D  97     -13.259 -15.194  -9.068  1.00 31.91           C  
-ANISOU 5623  CB  ASP D  97     3498   4383   4244   -825     24      2       C  
-ATOM   5624  CG  ASP D  97     -13.837 -15.082 -10.483  1.00 41.10           C  
-ANISOU 5624  CG  ASP D  97     4671   5618   5326   -993    -96     36       C  
-ATOM   5625  OD1 ASP D  97     -13.579 -14.056 -11.175  1.00 34.19           O  
-ANISOU 5625  OD1 ASP D  97     3867   4740   4383  -1030   -218     91       O  
-ATOM   5626  OD2 ASP D  97     -14.546 -16.023 -10.902  1.00 44.77           O  
-ANISOU 5626  OD2 ASP D  97     5090   6141   5778  -1128    -93     26       O  
-ATOM   5627  N   PHE D  98     -14.239 -12.303  -9.021  1.00 25.49           N  
-ANISOU 5627  N   PHE D  98     2616   3550   3519   -540   -296    119       N  
-ATOM   5628  CA  PHE D  98     -15.162 -11.223  -8.711  1.00 29.60           C  
-ANISOU 5628  CA  PHE D  98     3020   4059   4169   -326   -474    115       C  
-ATOM   5629  C   PHE D  98     -16.503 -11.521  -9.338  1.00 37.22           C  
-ANISOU 5629  C   PHE D  98     3815   5161   5165   -362   -589    148       C  
-ATOM   5630  O   PHE D  98     -16.593 -11.829 -10.530  1.00 38.63           O  
-ANISOU 5630  O   PHE D  98     4074   5349   5254   -575   -683    248       O  
-ATOM   5631  CB  PHE D  98     -14.629  -9.907  -9.271  1.00 26.67           C  
-ANISOU 5631  CB  PHE D  98     2837   3483   3815   -308   -714    197       C  
-ATOM   5632  CG  PHE D  98     -13.274  -9.555  -8.769  1.00 27.35           C  
-ANISOU 5632  CG  PHE D  98     3089   3464   3840   -324   -615    174       C  
-ATOM   5633  CD1 PHE D  98     -12.134 -10.090  -9.368  1.00 24.13           C  
-ANISOU 5633  CD1 PHE D  98     2818   3094   3255   -572   -499    200       C  
-ATOM   5634  CD2 PHE D  98     -13.125  -8.686  -7.689  1.00 26.21           C  
-ANISOU 5634  CD2 PHE D  98     2935   3217   3806    -91   -637     85       C  
-ATOM   5635  CE1 PHE D  98     -10.880  -9.779  -8.899  1.00 23.16           C  
-ANISOU 5635  CE1 PHE D  98     2804   2926   3068   -591   -410    165       C  
-ATOM   5636  CE2 PHE D  98     -11.876  -8.376  -7.211  1.00 26.08           C  
-ANISOU 5636  CE2 PHE D  98     3066   3126   3718   -131   -550     71       C  
-ATOM   5637  CZ  PHE D  98     -10.745  -8.920  -7.812  1.00 25.31           C  
-ANISOU 5637  CZ  PHE D  98     3090   3083   3443   -383   -439    124       C  
-ATOM   5638  N   ILE D  99     -17.554 -11.430  -8.540  1.00 28.85           N  
-ANISOU 5638  N   ILE D  99     2494   4262   4207   -178   -579     43       N  
-ATOM   5639  CA  ILE D  99     -18.893 -11.597  -9.070  1.00 36.44           C  
-ANISOU 5639  CA  ILE D  99     3237   5402   5209   -188   -708     51       C  
-ATOM   5640  C   ILE D  99     -19.784 -10.452  -8.624  1.00 33.66           C  
-ANISOU 5640  C   ILE D  99     2645   5084   5059    154   -907    -92       C  
-ATOM   5641  O   ILE D  99     -19.476  -9.734  -7.674  1.00 33.85           O  
-ANISOU 5641  O   ILE D  99     2639   5045   5176    385   -877   -242       O  
-ATOM   5642  CB  ILE D  99     -19.504 -12.926  -8.630  1.00 44.10           C  
-ANISOU 5642  CB  ILE D  99     4035   6647   6073   -366   -491     19       C  
-ATOM   5643  CG1 ILE D  99     -19.623 -12.970  -7.109  1.00 44.05           C  
-ANISOU 5643  CG1 ILE D  99     3848   6825   6065   -250   -302   -129       C  
-ATOM   5644  CG2 ILE D  99     -18.669 -14.100  -9.157  1.00 39.89           C  
-ANISOU 5644  CG2 ILE D  99     3745   6011   5401   -661   -360    117       C  
-ATOM   5645  CD1 ILE D  99     -20.203 -14.255  -6.593  1.00 49.69           C  
-ANISOU 5645  CD1 ILE D  99     4427   7817   6637   -506   -128   -111       C  
-ATOM   5646  N   ARG D 100     -20.883 -10.265  -9.330  1.00 36.14           N  
-ANISOU 5646  N   ARG D 100     2781   5495   5458    198  -1135    -72       N  
-ATOM   5647  CA  ARG D 100     -21.874  -9.316  -8.885  1.00 45.80           C  
-ANISOU 5647  CA  ARG D 100     3693   6793   6915    569  -1339   -279       C  
-ATOM   5648  C   ARG D 100     -23.196 -10.044  -8.950  1.00 47.27           C  
-ANISOU 5648  C   ARG D 100     3502   7396   7064    505  -1290   -354       C  
-ATOM   5649  O   ARG D 100     -23.383 -10.907  -9.805  1.00 47.52           O  
-ANISOU 5649  O   ARG D 100     3604   7506   6946    194  -1273   -167       O  
-ATOM   5650  CB  ARG D 100     -21.874  -8.070  -9.766  1.00 52.77           C  
-ANISOU 5650  CB  ARG D 100     4738   7310   8002    741  -1802   -169       C  
-ATOM   5651  CG  ARG D 100     -22.826  -6.989  -9.290  1.00 64.62           C  
-ANISOU 5651  CG  ARG D 100     5928   8796   9830   1211  -2086   -438       C  
-ATOM   5652  CD  ARG D 100     -22.336  -5.614  -9.687  1.00 70.05           C  
-ANISOU 5652  CD  ARG D 100     6907   8964  10745   1408  -2530   -350       C  
-ATOM   5653  NE  ARG D 100     -23.361  -4.606  -9.451  1.00 78.10           N  
-ANISOU 5653  NE  ARG D 100     7733   9904  12038   1806  -2771   -588       N  
-ATOM   5654  CZ  ARG D 100     -23.496  -3.500 -10.172  1.00 84.43           C  
-ANISOU 5654  CZ  ARG D 100     8782  10278  13017   1902  -3206   -460       C  
-ATOM   5655  NH1 ARG D 100     -22.662  -3.255 -11.175  1.00 84.71           N  
-ANISOU 5655  NH1 ARG D 100     9246   9972  12970   1606  -3472    -76       N  
-ATOM   5656  NH2 ARG D 100     -24.465  -2.638  -9.893  1.00 89.73           N  
-ANISOU 5656  NH2 ARG D 100     9279  10882  13931   2248  -3377   -721       N  
-ATOM   5657  N   LEU D 101     -24.087  -9.734  -8.017  1.00 44.13           N  
-ANISOU 5657  N   LEU D 101     2685   7308   6774    769  -1248   -659       N  
-ATOM   5658  CA  LEU D 101     -25.410 -10.335  -8.011  1.00 52.93           C  
-ANISOU 5658  CA  LEU D 101     3371   8904   7837    700  -1206   -769       C  
-ATOM   5659  C   LEU D 101     -26.381  -9.270  -8.470  1.00 59.29           C  
-ANISOU 5659  C   LEU D 101     4005   9614   8907   1050  -1557   -868       C  
-ATOM   5660  O   LEU D 101     -26.382  -8.162  -7.932  1.00 65.40           O  
-ANISOU 5660  O   LEU D 101     4787  10188   9874   1407  -1656  -1066       O  
-ATOM   5661  CB  LEU D 101     -25.777 -10.847  -6.616  1.00 53.76           C  
-ANISOU 5661  CB  LEU D 101     3271   9391   7763    621   -824   -979       C  
-ATOM   5662  CG  LEU D 101     -24.991 -12.028  -6.040  1.00 55.75           C  
-ANISOU 5662  CG  LEU D 101     3687   9758   7738    229   -499   -845       C  
-ATOM   5663  CD1 LEU D 101     -24.249 -12.785  -7.107  1.00 55.95           C  
-ANISOU 5663  CD1 LEU D 101     4097   9483   7678    -69   -539   -514       C  
-ATOM   5664  CD2 LEU D 101     -24.010 -11.558  -5.018  1.00 54.34           C  
-ANISOU 5664  CD2 LEU D 101     3630   9453   7565    365   -359   -960       C  
-ATOM   5665  N   LYS D 102     -27.192  -9.591  -9.472  1.00 55.26           N  
-ANISOU 5665  N   LYS D 102     3391   9214   8393    922  -1747   -716       N  
-ATOM   5666  CA  LYS D 102     -28.083  -8.603 -10.061  1.00 60.79           C  
-ANISOU 5666  CA  LYS D 102     3986   9779   9334   1220  -2117   -735       C  
-ATOM   5667  C   LYS D 102     -29.533  -8.889  -9.714  1.00 68.07           C  
-ANISOU 5667  C   LYS D 102     4488  11137  10238   1255  -2001   -928       C  
-ATOM   5668  O   LYS D 102     -29.999 -10.025  -9.809  1.00 61.91           O  
-ANISOU 5668  O   LYS D 102     3578  10703   9242    909  -1800   -860       O  
-ATOM   5669  CB  LYS D 102     -27.900  -8.557 -11.578  1.00 56.71           C  
-ANISOU 5669  CB  LYS D 102     3706   9017   8826   1049  -2502   -385       C  
-ATOM   5670  CG  LYS D 102     -28.797  -7.572 -12.314  1.00 68.97           C  
-ANISOU 5670  CG  LYS D 102     5207  10412  10585   1304  -2917   -336       C  
-ATOM   5671  CD  LYS D 102     -28.330  -7.428 -13.758  1.00 71.06           C  
-ANISOU 5671  CD  LYS D 102     5856  10361  10784   1057  -3277     46       C  
-ATOM   5672  CE  LYS D 102     -29.348  -6.701 -14.622  1.00 78.94           C  
-ANISOU 5672  CE  LYS D 102     6787  11283  11924   1215  -3679    134       C  
-ATOM   5673  NZ  LYS D 102     -28.912  -6.663 -16.050  1.00 79.82           N  
-ANISOU 5673  NZ  LYS D 102     7308  11128  11892    863  -3976    525       N  
-ATOM   5674  N   SER D 103     -30.237  -7.842  -9.308  1.00 56.51           N  
-ANISOU 5674  N   SER D 103     6625   7855   6992    282  -2705   -865       N  
-ATOM   5675  CA  SER D 103     -31.639  -7.952  -8.946  1.00 66.62           C  
-ANISOU 5675  CA  SER D 103     7849   9554   7910    432  -2590   -799       C  
-ATOM   5676  C   SER D 103     -32.506  -7.563 -10.134  1.00 71.74           C  
-ANISOU 5676  C   SER D 103     8544  10372   8343    414  -2636   -656       C  
-ATOM   5677  O   SER D 103     -32.274  -6.539 -10.778  1.00 76.91           O  
-ANISOU 5677  O   SER D 103     9313  10795   9116    528  -2834   -656       O  
-ATOM   5678  CB  SER D 103     -31.946  -7.053  -7.747  1.00 72.20           C  
-ANISOU 5678  CB  SER D 103     8600  10200   8634    841  -2691   -924       C  
-ATOM   5679  OG  SER D 103     -32.713  -7.739  -6.775  1.00 75.18           O  
-ANISOU 5679  OG  SER D 103     8847  10919   8799    938  -2515   -859       O  
-ATOM   5680  N   TYR D 104     -33.492  -8.403 -10.434  1.00 71.72           N  
-ANISOU 5680  N   TYR D 104     8469  10699   8081    245  -2507   -488       N  
-ATOM   5681  CA  TYR D 104     -34.487  -8.089 -11.447  1.00 73.41           C  
-ANISOU 5681  CA  TYR D 104     8731  11080   8080    234  -2553   -335       C  
-ATOM   5682  C   TYR D 104     -35.852  -7.981 -10.777  1.00 76.56           C  
-ANISOU 5682  C   TYR D 104     9028  11698   8364    403  -2530   -197       C  
-ATOM   5683  O   TYR D 104     -36.291  -8.911 -10.092  1.00 74.79           O  
-ANISOU 5683  O   TYR D 104     8691  11565   8160    340  -2467   -124       O  
-ATOM   5684  CB  TYR D 104     -34.538  -9.174 -12.525  1.00 69.79           C  
-ANISOU 5684  CB  TYR D 104     8370  10642   7504    -81  -2539   -267       C  
-ATOM   5685  CG  TYR D 104     -33.220  -9.470 -13.212  1.00 66.64           C  
-ANISOU 5685  CG  TYR D 104     8072  10104   7145   -194  -2525   -403       C  
-ATOM   5686  CD1 TYR D 104     -32.272 -10.300 -12.614  1.00 65.13           C  
-ANISOU 5686  CD1 TYR D 104     7850   9769   7127   -328  -2442   -520       C  
-ATOM   5687  CD2 TYR D 104     -32.937  -8.949 -14.471  1.00 65.27           C  
-ANISOU 5687  CD2 TYR D 104     8089   9788   6922   -168  -2466   -303       C  
-ATOM   5688  CE1 TYR D 104     -31.075 -10.586 -13.240  1.00 62.21           C  
-ANISOU 5688  CE1 TYR D 104     7641   9099   6897   -437  -2258   -501       C  
-ATOM   5689  CE2 TYR D 104     -31.744  -9.234 -15.112  1.00 64.78           C  
-ANISOU 5689  CE2 TYR D 104     8172   9449   6993   -261  -2237   -236       C  
-ATOM   5690  CZ  TYR D 104     -30.815 -10.052 -14.490  1.00 61.79           C  
-ANISOU 5690  CZ  TYR D 104     7761   8928   6790   -387  -2132   -331       C  
-ATOM   5691  OH  TYR D 104     -29.622 -10.341 -15.115  1.00 58.32           O  
-ANISOU 5691  OH  TYR D 104     7434   8274   6449   -418  -1877   -211       O  
-ATOM   5692  N   ASP D 112     -35.993 -11.721  -7.689  1.00 83.13           N  
-ANISOU 5692  N   ASP D 112     9413  12696   9478    186  -2265    -69       N  
-ATOM   5693  CA  ASP D 112     -35.160 -12.550  -8.559  1.00 82.98           C  
-ANISOU 5693  CA  ASP D 112     9545  12413   9571   -117  -2306   -177       C  
-ATOM   5694  C   ASP D 112     -33.715 -12.056  -8.594  1.00 82.62           C  
-ANISOU 5694  C   ASP D 112     9627  12160   9604   -182  -2269   -330       C  
-ATOM   5695  O   ASP D 112     -33.459 -10.877  -8.841  1.00 86.73           O  
-ANISOU 5695  O   ASP D 112    10189  12687  10076    -52  -2293   -396       O  
-ATOM   5696  CB  ASP D 112     -35.738 -12.597  -9.962  1.00 83.88           C  
-ANISOU 5696  CB  ASP D 112     9771  12526   9573   -218  -2402   -171       C  
-ATOM   5697  N   ILE D 113     -32.775 -12.970  -8.369  1.00 76.01           N  
-ANISOU 5697  N   ILE D 113     8817  11159   8904   -348  -2204   -408       N  
-ATOM   5698  CA  ILE D 113     -31.376 -12.601  -8.188  1.00 69.28           C  
-ANISOU 5698  CA  ILE D 113     7991  10184   8147   -391  -2110   -557       C  
-ATOM   5699  C   ILE D 113     -30.417 -13.588  -8.874  1.00 60.99           C  
-ANISOU 5699  C   ILE D 113     7064   8949   7162   -655  -2047   -626       C  
-ATOM   5700  O   ILE D 113     -30.508 -14.800  -8.665  1.00 62.99           O  
-ANISOU 5700  O   ILE D 113     7337   9096   7498   -685  -2023   -637       O  
-ATOM   5701  CB  ILE D 113     -31.065 -12.452  -6.677  1.00 71.52           C  
-ANISOU 5701  CB  ILE D 113     8154  10492   8527   -165  -2043   -623       C  
-ATOM   5702  CG1 ILE D 113     -29.577 -12.204  -6.438  1.00 68.14           C  
-ANISOU 5702  CG1 ILE D 113     7770   9796   8323   -163  -2005   -828       C  
-ATOM   5703  CG2 ILE D 113     -31.598 -13.641  -5.893  1.00 74.29           C  
-ANISOU 5703  CG2 ILE D 113     8392  10948   8886   -203  -1992   -481       C  
-ATOM   5704  CD1 ILE D 113     -29.200 -10.772  -6.690  1.00 70.96           C  
-ANISOU 5704  CD1 ILE D 113     8208   9916   8836     41  -2186   -967       C  
-ATOM   5705  N   LYS D 114     -29.511 -13.063  -9.702  1.00 51.90           N  
-ANISOU 5705  N   LYS D 114     5964   7715   6042   -684  -2029   -775       N  
-ATOM   5706  CA  LYS D 114     -28.611 -13.902 -10.508  1.00 46.95           C  
-ANISOU 5706  CA  LYS D 114     5479   6935   5425   -849  -1981   -864       C  
-ATOM   5707  C   LYS D 114     -27.147 -13.444 -10.461  1.00 45.25           C  
-ANISOU 5707  C   LYS D 114     5276   6378   5538   -816  -1813   -822       C  
-ATOM   5708  O   LYS D 114     -26.859 -12.274 -10.213  1.00 46.99           O  
-ANISOU 5708  O   LYS D 114     5417   6428   6009   -694  -1899   -777       O  
-ATOM   5709  CB  LYS D 114     -29.094 -13.960 -11.969  1.00 47.49           C  
-ANISOU 5709  CB  LYS D 114     5793   7037   5213   -882  -1980   -767       C  
-ATOM   5710  CG  LYS D 114     -30.478 -14.595 -12.163  1.00 52.40           C  
-ANISOU 5710  CG  LYS D 114     6406   7860   5646   -866  -2087   -766       C  
-ATOM   5711  CD  LYS D 114     -30.408 -16.115 -12.088  1.00 54.11           C  
-ANISOU 5711  CD  LYS D 114     6692   7992   5875   -967  -2044   -823       C  
-ATOM   5712  CE  LYS D 114     -31.784 -16.734 -11.960  1.00 60.22           C  
-ANISOU 5712  CE  LYS D 114     7346   8880   6654   -948  -2156   -750       C  
-ATOM   5713  NZ  LYS D 114     -31.737 -18.218 -12.132  1.00 64.45           N  
-ANISOU 5713  NZ  LYS D 114     7981   9312   7195  -1095  -2194   -786       N  
-ATOM   5714  N   VAL D 115     -26.228 -14.376 -10.708  1.00 45.07           N  
-ANISOU 5714  N   VAL D 115     5349   6244   5530   -914  -1601   -802       N  
-ATOM   5715  CA  VAL D 115     -24.796 -14.071 -10.721  1.00 46.43           C  
-ANISOU 5715  CA  VAL D 115     5471   6151   6018   -891  -1400   -656       C  
-ATOM   5716  C   VAL D 115     -24.324 -13.505 -12.063  1.00 51.06           C  
-ANISOU 5716  C   VAL D 115     6174   6653   6575   -797  -1203   -354       C  
-ATOM   5717  O   VAL D 115     -24.561 -14.104 -13.114  1.00 53.43           O  
-ANISOU 5717  O   VAL D 115     6717   7079   6503   -730  -1075   -316       O  
-ATOM   5718  CB  VAL D 115     -23.957 -15.322 -10.380  1.00 50.69           C  
-ANISOU 5718  CB  VAL D 115     6040   6660   6559   -970  -1216   -715       C  
-ATOM   5719  CG1 VAL D 115     -22.480 -15.103 -10.713  1.00 52.34           C  
-ANISOU 5719  CG1 VAL D 115     6192   6670   7025   -920   -948   -448       C  
-ATOM   5720  CG2 VAL D 115     -24.127 -15.679  -8.920  1.00 49.88           C  
-ANISOU 5720  CG2 VAL D 115     5740   6617   6594  -1030  -1373   -926       C  
-ATOM   5721  N   ILE D 116     -23.661 -12.349 -12.019  1.00 53.53           N  
-ANISOU 5721  N   ILE D 116     6313   6744   7283   -767  -1222   -117       N  
-ATOM   5722  CA  ILE D 116     -23.103 -11.730 -13.221  1.00 58.38           C  
-ANISOU 5722  CA  ILE D 116     6932   7302   7948   -668  -1012    304       C  
-ATOM   5723  C   ILE D 116     -21.577 -11.761 -13.171  1.00 62.33           C  
-ANISOU 5723  C   ILE D 116     7229   7637   8816   -687   -784    660       C  
-ATOM   5724  O   ILE D 116     -20.962 -11.412 -12.154  1.00 60.03           O  
-ANISOU 5724  O   ILE D 116     6717   7103   8990   -816   -959    651       O  
-ATOM   5725  CB  ILE D 116     -23.608 -10.275 -13.429  1.00 59.86           C  
-ANISOU 5725  CB  ILE D 116     7039   7355   8349   -634  -1245    448       C  
-ATOM   5726  CG1 ILE D 116     -24.959 -10.268 -14.136  1.00 59.89           C  
-ANISOU 5726  CG1 ILE D 116     7256   7618   7880   -540  -1307    303       C  
-ATOM   5727  CG2 ILE D 116     -22.629  -9.470 -14.268  1.00 64.45           C  
-ANISOU 5727  CG2 ILE D 116     7457   7776   9254   -592  -1070   1018       C  
-ATOM   5728  CD1 ILE D 116     -26.070 -10.916 -13.356  1.00 59.46           C  
-ANISOU 5728  CD1 ILE D 116     7269   7764   7559   -593  -1521   -116       C  
-ATOM   5729  N   GLY D 117     -20.973 -12.207 -14.267  1.00 67.82           N  
-ANISOU 5729  N   GLY D 117     8005   8493   9273   -511   -408    988       N  
-ATOM   5730  CA  GLY D 117     -19.531 -12.270 -14.370  1.00 70.43           C  
-ANISOU 5730  CA  GLY D 117     8095   8770   9896   -465   -125   1452       C  
-ATOM   5731  C   GLY D 117     -18.904 -13.396 -13.584  1.00 70.06           C  
-ANISOU 5731  C   GLY D 117     8057   8731   9830   -515    -22   1237       C  
-ATOM   5732  O   GLY D 117     -19.552 -14.405 -13.287  1.00 68.89           O  
-ANISOU 5732  O   GLY D 117     8180   8688   9307   -520    -80    769       O  
-ATOM   5733  N   GLY D 118     -17.634 -13.215 -13.237  1.00 67.16           N  
-ANISOU 5733  N   GLY D 118     7362   8241   9913   -570    100   1628       N  
-ATOM   5734  CA  GLY D 118     -16.879 -14.260 -12.580  1.00 58.68           C  
-ANISOU 5734  CA  GLY D 118     6268   7199   8829   -580    254   1510       C  
-ATOM   5735  C   GLY D 118     -16.279 -15.193 -13.612  1.00 58.01           C  
-ANISOU 5735  C   GLY D 118     6362   7419   8260   -216    734   1768       C  
-ATOM   5736  O   GLY D 118     -16.600 -15.117 -14.807  1.00 56.14           O  
-ANISOU 5736  O   GLY D 118     6327   7391   7614     72    916   1945       O  
-ATOM   5737  N   ASP D 119     -15.382 -16.060 -13.158  1.00 54.34           N  
-ANISOU 5737  N   ASP D 119     5843   6996   7807   -163    934   1795       N  
-ATOM   5738  CA  ASP D 119     -14.888 -17.133 -13.997  1.00 57.84           C  
-ANISOU 5738  CA  ASP D 119     6563   7727   7687    271   1346   1910       C  
-ATOM   5739  C   ASP D 119     -16.008 -18.162 -14.114  1.00 55.24           C  
-ANISOU 5739  C   ASP D 119     6796   7415   6779    336   1164   1242       C  
-ATOM   5740  O   ASP D 119     -16.987 -18.114 -13.359  1.00 45.25           O  
-ANISOU 5740  O   ASP D 119     5577   5984   5632      2    786    784       O  
-ATOM   5741  CB  ASP D 119     -13.637 -17.780 -13.380  1.00 58.96           C  
-ANISOU 5741  CB  ASP D 119     6487   7895   8020    309   1581   2111       C  
-ATOM   5742  CG  ASP D 119     -12.452 -16.820 -13.297  1.00 63.31           C  
-ANISOU 5742  CG  ASP D 119     6425   8425   9203    219   1717   2880       C  
-ATOM   5743  OD1 ASP D 119     -12.499 -15.752 -13.940  1.00 66.86           O  
-ANISOU 5743  OD1 ASP D 119     6650   8881   9870    216   1705   3342       O  
-ATOM   5744  OD2 ASP D 119     -11.469 -17.143 -12.597  1.00 64.20           O  
-ANISOU 5744  OD2 ASP D 119     6261   8508   9624    140   1811   3063       O  
-ATOM   5745  N   ASP D 120     -15.879 -19.070 -15.076  1.00 58.99           N  
-ANISOU 5745  N   ASP D 120     7693   8092   6629    798   1396   1226       N  
-ATOM   5746  CA  ASP D 120     -16.714 -20.255 -15.082  1.00 59.09           C  
-ANISOU 5746  CA  ASP D 120     8246   8031   6174    837   1148    622       C  
-ATOM   5747  C   ASP D 120     -16.560 -20.866 -13.695  1.00 52.76           C  
-ANISOU 5747  C   ASP D 120     7291   7041   5713    475    995    327       C  
-ATOM   5748  O   ASP D 120     -15.439 -21.075 -13.224  1.00 54.49           O  
-ANISOU 5748  O   ASP D 120     7272   7287   6147    527   1253    564       O  
-ATOM   5749  CB  ASP D 120     -16.239 -21.240 -16.147  1.00 68.49           C  
-ANISOU 5749  CB  ASP D 120     9934   9405   6684   1472   1399    656       C  
-ATOM   5750  CG  ASP D 120     -17.130 -22.460 -16.245  1.00 69.99           C  
-ANISOU 5750  CG  ASP D 120    10745   9418   6430   1504   1009     35       C  
-ATOM   5751  OD1 ASP D 120     -17.114 -23.286 -15.308  1.00 62.33           O  
-ANISOU 5751  OD1 ASP D 120     9802   8257   5624   1247    840   -266       O  
-ATOM   5752  OD2 ASP D 120     -17.845 -22.591 -17.261  1.00 74.07           O  
-ANISOU 5752  OD2 ASP D 120    11715   9970   6458   1783    832   -127       O  
-ATOM   5753  N   LEU D 121     -17.680 -21.128 -13.031  1.00 50.66           N  
-ANISOU 5753  N   LEU D 121     7117   6627   5504    125    587   -127       N  
-ATOM   5754  CA  LEU D 121     -17.653 -21.514 -11.624  1.00 50.50           C  
-ANISOU 5754  CA  LEU D 121     6866   6482   5842   -217    433   -350       C  
-ATOM   5755  C   LEU D 121     -17.104 -22.919 -11.384  1.00 46.96           C  
-ANISOU 5755  C   LEU D 121     6668   5986   5187    -84    522   -514       C  
-ATOM   5756  O   LEU D 121     -16.993 -23.350 -10.239  1.00 45.10           O  
-ANISOU 5756  O   LEU D 121     6245   5672   5219   -325    435   -666       O  
-ATOM   5757  CB  LEU D 121     -19.038 -21.359 -10.997  1.00 55.14           C  
-ANISOU 5757  CB  LEU D 121     7411   7016   6523   -558      9   -673       C  
-ATOM   5758  CG  LEU D 121     -19.578 -19.932 -10.900  1.00 58.51           C  
-ANISOU 5758  CG  LEU D 121     7551   7466   7214   -695   -121   -560       C  
-ATOM   5759  CD1 LEU D 121     -21.009 -19.970 -10.418  1.00 61.71           C  
-ANISOU 5759  CD1 LEU D 121     7961   7911   7573   -917   -500   -842       C  
-ATOM   5760  CD2 LEU D 121     -18.736 -19.055  -9.980  1.00 56.39           C  
-ANISOU 5760  CD2 LEU D 121     6841   7110   7474   -805    -62   -372       C  
-ATOM   5761  N   SER D 122     -16.747 -23.623 -12.455  1.00 45.82           N  
-ANISOU 5761  N   SER D 122     6970   5897   4542    357    685   -482       N  
-ATOM   5762  CA  SER D 122     -16.078 -24.915 -12.322  1.00 48.03           C  
-ANISOU 5762  CA  SER D 122     7540   6118   4593    586    786   -609       C  
-ATOM   5763  C   SER D 122     -14.680 -24.730 -11.726  1.00 47.15           C  
-ANISOU 5763  C   SER D 122     7005   6117   4794    652   1199   -248       C  
-ATOM   5764  O   SER D 122     -14.050 -25.697 -11.303  1.00 46.95           O  
-ANISOU 5764  O   SER D 122     7088   6049   4700    766   1303   -330       O  
-ATOM   5765  CB  SER D 122     -16.011 -25.657 -13.667  1.00 55.32           C  
-ANISOU 5765  CB  SER D 122     9119   7077   4825   1178    824   -680       C  
-ATOM   5766  OG  SER D 122     -15.295 -24.914 -14.640  1.00 58.61           O  
-ANISOU 5766  OG  SER D 122     9454   7782   5035   1638   1246   -221       O  
-ATOM   5767  N   THR D 123     -14.206 -23.484 -11.682  1.00 42.89           N  
-ANISOU 5767  N   THR D 123     5974   5689   4632    560   1387    173       N  
-ATOM   5768  CA  THR D 123     -12.933 -23.168 -11.044  1.00 42.94           C  
-ANISOU 5768  CA  THR D 123     5493   5759   5061    524   1674    573       C  
-ATOM   5769  C   THR D 123     -13.034 -23.338  -9.531  1.00 38.81           C  
-ANISOU 5769  C   THR D 123     4708   5056   4983     81   1431    284       C  
-ATOM   5770  O   THR D 123     -12.020 -23.420  -8.842  1.00 42.88           O  
-ANISOU 5770  O   THR D 123     4908   5583   5800     46   1599    488       O  
-ATOM   5771  CB  THR D 123     -12.494 -21.732 -11.324  1.00 48.01           C  
-ANISOU 5771  CB  THR D 123     5655   6475   6111    454   1788   1122       C  
-ATOM   5772  OG1 THR D 123     -13.537 -20.836 -10.925  1.00 45.87           O  
-ANISOU 5772  OG1 THR D 123     5272   6028   6129     62   1392    887       O  
-ATOM   5773  CG2 THR D 123     -12.186 -21.539 -12.804  1.00 49.34           C  
-ANISOU 5773  CG2 THR D 123     5979   6917   5849    971   2128   1563       C  
-ATOM   5774  N   LEU D 124     -14.261 -23.387  -9.022  1.00 35.96           N  
-ANISOU 5774  N   LEU D 124     4453   4566   4642   -218   1041   -148       N  
-ATOM   5775  CA  LEU D 124     -14.487 -23.536  -7.583  1.00 32.51           C  
-ANISOU 5775  CA  LEU D 124     3767   4034   4551   -552    813   -403       C  
-ATOM   5776  C   LEU D 124     -14.410 -24.995  -7.131  1.00 34.64           C  
-ANISOU 5776  C   LEU D 124     4276   4265   4621   -517    818   -655       C  
-ATOM   5777  O   LEU D 124     -14.216 -25.264  -5.946  1.00 29.95           O  
-ANISOU 5777  O   LEU D 124     3438   3647   4295   -698    755   -761       O  
-ATOM   5778  CB  LEU D 124     -15.855 -22.973  -7.190  1.00 30.83           C  
-ANISOU 5778  CB  LEU D 124     3508   3788   4417   -814    424   -664       C  
-ATOM   5779  CG  LEU D 124     -16.016 -21.516  -6.759  1.00 36.79           C  
-ANISOU 5779  CG  LEU D 124     3908   4505   5565   -961    253   -561       C  
-ATOM   5780  CD1 LEU D 124     -14.969 -20.614  -7.366  1.00 35.69           C  
-ANISOU 5780  CD1 LEU D 124     3567   4330   5665   -858    465   -109       C  
-ATOM   5781  CD2 LEU D 124     -17.423 -21.024  -7.092  1.00 34.78           C  
-ANISOU 5781  CD2 LEU D 124     3777   4291   5147  -1037    -25   -733       C  
-ATOM   5782  N   THR D 125     -14.568 -25.924  -8.070  1.00 34.14           N  
-ANISOU 5782  N   THR D 125     4713   4176   4082   -255    851   -757       N  
-ATOM   5783  CA  THR D 125     -14.617 -27.348  -7.734  1.00 34.19           C  
-ANISOU 5783  CA  THR D 125     5027   4060   3903   -227    748  -1016       C  
-ATOM   5784  C   THR D 125     -13.359 -27.801  -6.995  1.00 34.62           C  
-ANISOU 5784  C   THR D 125     4867   4157   4131   -136   1050   -877       C  
-ATOM   5785  O   THR D 125     -12.242 -27.660  -7.501  1.00 36.01           O  
-ANISOU 5785  O   THR D 125     5005   4460   4218    194   1429   -564       O  
-ATOM   5786  CB  THR D 125     -14.829 -28.219  -8.979  1.00 42.02           C  
-ANISOU 5786  CB  THR D 125     6682   4953   4329    144    675  -1154       C  
-ATOM   5787  OG1 THR D 125     -16.025 -27.802  -9.650  1.00 38.51           O  
-ANISOU 5787  OG1 THR D 125     6425   4467   3741     37    352  -1282       O  
-ATOM   5788  CG2 THR D 125     -14.943 -29.696  -8.599  1.00 43.65           C  
-ANISOU 5788  CG2 THR D 125     7244   4932   4409    137    447  -1436       C  
-ATOM   5789  N   GLY D 126     -13.552 -28.331  -5.789  1.00 34.47           N  
-ANISOU 5789  N   GLY D 126     4666   4073   4356   -409    893  -1056       N  
-ATOM   5790  CA  GLY D 126     -12.464 -28.899  -5.012  1.00 34.63           C  
-ANISOU 5790  CA  GLY D 126     4511   4122   4524   -338   1134   -971       C  
-ATOM   5791  C   GLY D 126     -11.623 -27.893  -4.246  1.00 36.37           C  
-ANISOU 5791  C   GLY D 126     4164   4462   5191   -447   1303   -717       C  
-ATOM   5792  O   GLY D 126     -10.550 -28.248  -3.748  1.00 35.79           O  
-ANISOU 5792  O   GLY D 126     3916   4439   5244   -351   1540   -567       O  
-ATOM   5793  N   LYS D 127     -12.095 -26.647  -4.146  1.00 29.62           N  
-ANISOU 5793  N   LYS D 127     3041   3624   4591   -638   1134   -667       N  
-ATOM   5794  CA  LYS D 127     -11.314 -25.587  -3.504  1.00 30.38           C  
-ANISOU 5794  CA  LYS D 127     2653   3735   5156   -742   1159   -429       C  
-ATOM   5795  C   LYS D 127     -12.018 -25.127  -2.235  1.00 25.24           C  
-ANISOU 5795  C   LYS D 127     1849   3056   4683   -922    754   -660       C  
-ATOM   5796  O   LYS D 127     -13.211 -25.376  -2.065  1.00 26.71           O  
-ANISOU 5796  O   LYS D 127     2195   3272   4681   -979    539   -896       O  
-ATOM   5797  CB  LYS D 127     -11.157 -24.383  -4.440  1.00 32.94           C  
-ANISOU 5797  CB  LYS D 127     2872   4060   5584   -695   1203    -98       C  
-ATOM   5798  CG  LYS D 127     -10.585 -24.707  -5.808  1.00 39.83           C  
-ANISOU 5798  CG  LYS D 127     3981   5057   6095   -340   1575    227       C  
-ATOM   5799  CD  LYS D 127      -9.193 -25.281  -5.711  1.00 44.11           C  
-ANISOU 5799  CD  LYS D 127     4377   5718   6667   -115   1945    558       C  
-ATOM   5800  CE  LYS D 127      -8.583 -25.403  -7.106  1.00 54.08           C  
-ANISOU 5800  CE  LYS D 127     5815   7195   7537    359   2348    986       C  
-ATOM   5801  NZ  LYS D 127      -8.840 -24.163  -7.893  1.00 61.16           N  
-ANISOU 5801  NZ  LYS D 127     6546   8128   8563    328   2311   1311       N  
-ATOM   5802  N   ASN D 128     -11.279 -24.464  -1.351  1.00 26.96           N  
-ANISOU 5802  N   ASN D 128     2890   2900   4454     69   -782   -550       N  
-ATOM   5803  CA  ASN D 128     -11.874 -23.798  -0.198  1.00 27.20           C  
-ANISOU 5803  CA  ASN D 128     3063   2910   4360    136   -847   -476       C  
-ATOM   5804  C   ASN D 128     -12.328 -22.414  -0.631  1.00 27.84           C  
-ANISOU 5804  C   ASN D 128     2971   3056   4552    -58   -657   -404       C  
-ATOM   5805  O   ASN D 128     -11.506 -21.519  -0.810  1.00 32.19           O  
-ANISOU 5805  O   ASN D 128     3275   3613   5343    -89   -623   -586       O  
-ATOM   5806  CB  ASN D 128     -10.868 -23.669   0.950  1.00 26.63           C  
-ANISOU 5806  CB  ASN D 128     2981   2808   4329    422  -1145   -744       C  
-ATOM   5807  CG  ASN D 128     -10.606 -24.993   1.653  1.00 31.72           C  
-ANISOU 5807  CG  ASN D 128     3954   3350   4748    721  -1364   -768       C  
-ATOM   5808  OD1 ASN D 128     -11.201 -26.009   1.310  1.00 31.08           O  
-ANISOU 5808  OD1 ASN D 128     4104   3190   4516    664  -1237   -571       O  
-ATOM   5809  ND2 ASN D 128      -9.700 -24.986   2.633  1.00 34.52           N  
-ANISOU 5809  ND2 ASN D 128     4343   3691   5082   1072  -1698  -1042       N  
-ATOM   5810  N   VAL D 129     -13.629 -22.233  -0.799  1.00 23.40           N  
-ANISOU 5810  N   VAL D 129     2533   2520   3838   -179   -515   -173       N  
-ATOM   5811  CA  VAL D 129     -14.134 -20.973  -1.343  1.00 21.24           C  
-ANISOU 5811  CA  VAL D 129     2147   2297   3627   -313   -345    -88       C  
-ATOM   5812  C   VAL D 129     -14.500 -20.007  -0.217  1.00 26.84           C  
-ANISOU 5812  C   VAL D 129     2888   2989   4322   -275   -397    -83       C  
-ATOM   5813  O   VAL D 129     -15.304 -20.344   0.665  1.00 26.89           O  
-ANISOU 5813  O   VAL D 129     3086   2976   4154   -228   -451      2       O  
-ATOM   5814  CB  VAL D 129     -15.361 -21.207  -2.236  1.00 24.09           C  
-ANISOU 5814  CB  VAL D 129     2579   2727   3848   -412   -214     85       C  
-ATOM   5815  CG1 VAL D 129     -15.888 -19.881  -2.792  1.00 22.99           C  
-ANISOU 5815  CG1 VAL D 129     2391   2627   3717   -462    -78    174       C  
-ATOM   5816  CG2 VAL D 129     -15.009 -22.159  -3.380  1.00 26.23           C  
-ANISOU 5816  CG2 VAL D 129     2819   3027   4119   -434   -174     56       C  
-ATOM   5817  N   LEU D 130     -13.890 -18.823  -0.240  1.00 24.17           N  
-ANISOU 5817  N   LEU D 130     2369   2629   4185   -304   -339   -195       N  
-ATOM   5818  CA  LEU D 130     -14.195 -17.743   0.706  1.00 22.80           C  
-ANISOU 5818  CA  LEU D 130     2184   2438   4038   -282   -368   -218       C  
-ATOM   5819  C   LEU D 130     -14.961 -16.644  -0.032  1.00 21.49           C  
-ANISOU 5819  C   LEU D 130     2004   2270   3891   -408   -139    -54       C  
-ATOM   5820  O   LEU D 130     -14.395 -15.955  -0.890  1.00 26.12           O  
-ANISOU 5820  O   LEU D 130     2486   2790   4649   -483     61    -88       O  
-ATOM   5821  CB  LEU D 130     -12.901 -17.138   1.255  1.00 26.38           C  
-ANISOU 5821  CB  LEU D 130     2412   2844   4766   -212   -462   -539       C  
-ATOM   5822  CG  LEU D 130     -12.826 -16.490   2.652  1.00 35.13           C  
-ANISOU 5822  CG  LEU D 130     3508   3952   5887    -75   -653   -705       C  
-ATOM   5823  CD1 LEU D 130     -11.962 -15.236   2.630  1.00 33.33           C  
-ANISOU 5823  CD1 LEU D 130     2960   3658   6046   -148   -553   -993       C  
-ATOM   5824  CD2 LEU D 130     -14.176 -16.234   3.275  1.00 34.29           C  
-ANISOU 5824  CD2 LEU D 130     3636   3870   5524    -81   -633   -459       C  
-ATOM   5825  N   ILE D 131     -16.237 -16.486   0.301  1.00 20.67           N  
-ANISOU 5825  N   ILE D 131     2029   2213   3610   -413   -144    105       N  
-ATOM   5826  CA  ILE D 131     -17.053 -15.418  -0.273  1.00 23.39           C  
-ANISOU 5826  CA  ILE D 131     2385   2561   3939   -456      8    235       C  
-ATOM   5827  C   ILE D 131     -16.920 -14.207   0.635  1.00 22.11           C  
-ANISOU 5827  C   ILE D 131     2160   2334   3907   -451     14    160       C  
-ATOM   5828  O   ILE D 131     -17.090 -14.324   1.850  1.00 23.71           O  
-ANISOU 5828  O   ILE D 131     2392   2557   4061   -399   -134     93       O  
-ATOM   5829  CB  ILE D 131     -18.537 -15.839  -0.352  1.00 21.67           C  
-ANISOU 5829  CB  ILE D 131     2268   2442   3525   -451    -23    353       C  
-ATOM   5830  CG1 ILE D 131     -18.695 -17.024  -1.309  1.00 24.86           C  
-ANISOU 5830  CG1 ILE D 131     2698   2912   3837   -459    -27    372       C  
-ATOM   5831  CG2 ILE D 131     -19.400 -14.679  -0.818  1.00 26.91           C  
-ANISOU 5831  CG2 ILE D 131     2945   3121   4159   -418     61    440       C  
-ATOM   5832  CD1 ILE D 131     -20.073 -17.706  -1.267  1.00 28.61           C  
-ANISOU 5832  CD1 ILE D 131     3198   3469   4204   -480    -53    368       C  
-ATOM   5833  N   VAL D 132     -16.601 -13.052   0.067  1.00 20.36           N  
-ANISOU 5833  N   VAL D 132     1887   2008   3840   -492    212    164       N  
-ATOM   5834  CA  VAL D 132     -16.397 -11.861   0.870  1.00 22.55           C  
-ANISOU 5834  CA  VAL D 132     2074   2197   4299   -506    251     54       C  
-ATOM   5835  C   VAL D 132     -17.447 -10.801   0.533  1.00 29.76           C  
-ANISOU 5835  C   VAL D 132     3105   3071   5132   -489    386    234       C  
-ATOM   5836  O   VAL D 132     -17.518 -10.334  -0.609  1.00 26.63           O  
-ANISOU 5836  O   VAL D 132     2827   2585   4708   -474    601    365       O  
-ATOM   5837  CB  VAL D 132     -14.992 -11.302   0.652  1.00 23.82           C  
-ANISOU 5837  CB  VAL D 132     2049   2202   4799   -579    423   -177       C  
-ATOM   5838  CG1 VAL D 132     -14.760 -10.052   1.500  1.00 22.30           C  
-ANISOU 5838  CG1 VAL D 132     1761   1931   4780   -567    460   -348       C  
-ATOM   5839  CG2 VAL D 132     -13.928 -12.376   0.974  1.00 25.08           C  
-ANISOU 5839  CG2 VAL D 132     2060   2419   5049   -541    233   -418       C  
-ATOM   5840  N   GLU D 133     -18.222 -10.397   1.543  1.00 24.71           N  
-ANISOU 5840  N   GLU D 133     2467   2484   4440   -457    266    226       N  
-ATOM   5841  CA  GLU D 133     -19.396  -9.542   1.358  1.00 25.25           C  
-ANISOU 5841  CA  GLU D 133     2631   2551   4411   -404    323    365       C  
-ATOM   5842  C   GLU D 133     -19.268  -8.294   2.228  1.00 30.01           C  
-ANISOU 5842  C   GLU D 133     3160   3046   5198   -422    376    265       C  
-ATOM   5843  O   GLU D 133     -18.560  -8.321   3.244  1.00 25.74           O  
-ANISOU 5843  O   GLU D 133     2487   2501   4793   -452    277     64       O  
-ATOM   5844  CB  GLU D 133     -20.663 -10.355   1.700  1.00 27.31           C  
-ANISOU 5844  CB  GLU D 133     2934   2986   4455   -367    157    413       C  
-ATOM   5845  CG  GLU D 133     -22.000  -9.648   1.551  1.00 34.50           C  
-ANISOU 5845  CG  GLU D 133     3883   3942   5283   -285    156    475       C  
-ATOM   5846  CD  GLU D 133     -22.307  -9.251   0.123  1.00 31.27           C  
-ANISOU 5846  CD  GLU D 133     3595   3511   4776   -147    228    592       C  
-ATOM   5847  OE1 GLU D 133     -21.672  -8.303  -0.369  1.00 29.40           O  
-ANISOU 5847  OE1 GLU D 133     3461   3099   4611   -110    408    666       O  
-ATOM   5848  OE2 GLU D 133     -23.192  -9.873  -0.506  1.00 32.71           O  
-ANISOU 5848  OE2 GLU D 133     3788   3833   4806    -55    121    586       O  
-ATOM   5849  N   ASP D 134     -19.903  -7.190   1.823  1.00 28.09           N  
-ANISOU 5849  N   ASP D 134     3010   2708   4954   -367    514    374       N  
-ATOM   5850  CA  ASP D 134     -19.949  -5.994   2.679  1.00 21.88           C  
-ANISOU 5850  CA  ASP D 134     2155   1816   4341   -383    564    276       C  
-ATOM   5851  C   ASP D 134     -20.973  -6.126   3.820  1.00 25.12           C  
-ANISOU 5851  C   ASP D 134     2529   2389   4626   -347    351    235       C  
-ATOM   5852  O   ASP D 134     -20.665  -5.858   4.987  1.00 28.81           O  
-ANISOU 5852  O   ASP D 134     2894   2859   5194   -374    270     64       O  
-ATOM   5853  CB  ASP D 134     -20.152  -4.698   1.876  1.00 25.85           C  
-ANISOU 5853  CB  ASP D 134     2818   2098   4907   -320    833    405       C  
-ATOM   5854  CG  ASP D 134     -21.390  -4.729   1.001  1.00 30.59           C  
-ANISOU 5854  CG  ASP D 134     3635   2779   5209   -125    774    615       C  
-ATOM   5855  OD1 ASP D 134     -21.950  -5.824   0.778  1.00 29.07           O  
-ANISOU 5855  OD1 ASP D 134     3425   2803   4818    -84    575    638       O  
-ATOM   5856  OD2 ASP D 134     -21.796  -3.650   0.524  1.00 33.55           O  
-ANISOU 5856  OD2 ASP D 134     4200   2989   5558     12    924    725       O  
-ATOM   5857  N   ILE D 135     -22.183  -6.562   3.501  1.00 28.80           N  
-ANISOU 5857  N   ILE D 135     3073   2988   4882   -277    270    347       N  
-ATOM   5858  CA  ILE D 135     -23.216  -6.609   4.520  1.00 26.02           C  
-ANISOU 5858  CA  ILE D 135     2684   2748   4456   -272    162    283       C  
-ATOM   5859  C   ILE D 135     -24.260  -7.679   4.250  1.00 27.70           C  
-ANISOU 5859  C   ILE D 135     2906   3117   4501   -264     90    301       C  
-ATOM   5860  O   ILE D 135     -24.646  -7.907   3.098  1.00 29.97           O  
-ANISOU 5860  O   ILE D 135     3221   3450   4718   -185     80    365       O  
-ATOM   5861  CB  ILE D 135     -23.855  -5.198   4.688  1.00 35.17           C  
-ANISOU 5861  CB  ILE D 135     3837   3827   5700   -200    220    280       C  
-ATOM   5862  CG1 ILE D 135     -24.944  -5.202   5.763  1.00 32.50           C  
-ANISOU 5862  CG1 ILE D 135     3440   3599   5309   -209    143    181       C  
-ATOM   5863  CG2 ILE D 135     -24.378  -4.669   3.347  1.00 34.53           C  
-ANISOU 5863  CG2 ILE D 135     3878   3693   5549    -43    281    419       C  
-ATOM   5864  CD1 ILE D 135     -25.277  -3.793   6.247  1.00 33.57           C  
-ANISOU 5864  CD1 ILE D 135     3543   3641   5570   -157    188    130       C  
-ATOM   5865  N   ILE D 136     -24.685  -8.344   5.327  1.00 24.96           N  
-ANISOU 5865  N   ILE D 136     2558   2831   4095   -335     64    216       N  
-ATOM   5866  CA  ILE D 136     -25.822  -9.260   5.318  1.00 26.49           C  
-ANISOU 5866  CA  ILE D 136     2729   3123   4212   -379     87    160       C  
-ATOM   5867  C   ILE D 136     -26.973  -8.528   5.995  1.00 30.57           C  
-ANISOU 5867  C   ILE D 136     3170   3665   4782   -373    128     51       C  
-ATOM   5868  O   ILE D 136     -26.808  -8.021   7.104  1.00 28.41           O  
-ANISOU 5868  O   ILE D 136     2945   3338   4513   -393    160     19       O  
-ATOM   5869  CB  ILE D 136     -25.552 -10.512   6.185  1.00 28.97           C  
-ANISOU 5869  CB  ILE D 136     3173   3413   4423   -471    140    138       C  
-ATOM   5870  CG1 ILE D 136     -24.254 -11.213   5.782  1.00 31.36           C  
-ANISOU 5870  CG1 ILE D 136     3550   3682   4684   -454     69    209       C  
-ATOM   5871  CG2 ILE D 136     -26.735 -11.498   6.116  1.00 28.35           C  
-ANISOU 5871  CG2 ILE D 136     3062   3373   4335   -568    267     44       C  
-ATOM   5872  CD1 ILE D 136     -24.179 -11.525   4.333  1.00 30.80           C  
-ANISOU 5872  CD1 ILE D 136     3403   3662   4639   -442     46    265       C  
-ATOM   5873  N   ASP D 137     -28.133  -8.487   5.348  1.00 30.82           N  
-ANISOU 5873  N   ASP D 137     3065   3786   4857   -323    110    -51       N  
-ATOM   5874  CA  ASP D 137     -29.313  -7.873   5.943  1.00 33.24           C  
-ANISOU 5874  CA  ASP D 137     3247   4127   5254   -317    150   -217       C  
-ATOM   5875  C   ASP D 137     -30.395  -8.937   6.095  1.00 35.41           C  
-ANISOU 5875  C   ASP D 137     3391   4467   5596   -444    273   -435       C  
-ATOM   5876  O   ASP D 137     -30.521  -9.558   7.147  1.00 35.11           O  
-ANISOU 5876  O   ASP D 137     3445   4353   5543   -609    481   -477       O  
-ATOM   5877  CB  ASP D 137     -29.776  -6.695   5.075  1.00 36.59           C  
-ANISOU 5877  CB  ASP D 137     3597   4584   5720    -93      9   -229       C  
-ATOM   5878  CG  ASP D 137     -30.913  -5.910   5.695  1.00 40.06           C  
-ANISOU 5878  CG  ASP D 137     3890   5056   6275    -52     18   -421       C  
-ATOM   5879  OD1 ASP D 137     -31.196  -6.089   6.901  1.00 43.43           O  
-ANISOU 5879  OD1 ASP D 137     4295   5458   6750   -221    171   -514       O  
-ATOM   5880  OD2 ASP D 137     -31.509  -5.099   4.962  1.00 40.00           O  
-ANISOU 5880  OD2 ASP D 137     3823   5087   6288    181   -126   -482       O  
-ATOM   5881  N   THR D 138     -31.169  -9.171   5.044  1.00 36.18           N  
-ANISOU 5881  N   THR D 138     3294   4683   5769   -351    167   -603       N  
-ATOM   5882  CA  THR D 138     -32.163 -10.241   5.094  1.00 36.51           C  
-ANISOU 5882  CA  THR D 138     3143   4770   5960   -501    314   -894       C  
-ATOM   5883  C   THR D 138     -31.481 -11.603   4.979  1.00 36.28           C  
-ANISOU 5883  C   THR D 138     3255   4673   5857   -651    433   -792       C  
-ATOM   5884  O   THR D 138     -31.971 -12.598   5.512  1.00 39.29           O  
-ANISOU 5884  O   THR D 138     3619   4972   6337   -860    703   -945       O  
-ATOM   5885  CB  THR D 138     -33.210 -10.118   3.981  1.00 39.63           C  
-ANISOU 5885  CB  THR D 138     3229   5340   6487   -312    108  -1208       C  
-ATOM   5886  OG1 THR D 138     -32.583 -10.274   2.699  1.00 39.56           O  
-ANISOU 5886  OG1 THR D 138     3308   5403   6320   -114   -122  -1070       O  
-ATOM   5887  CG2 THR D 138     -33.888  -8.774   4.053  1.00 42.63           C  
-ANISOU 5887  CG2 THR D 138     3498   5777   6923   -104    -41  -1317       C  
-ATOM   5888  N   GLY D 139     -30.351 -11.642   4.278  1.00 31.55           N  
-ANISOU 5888  N   GLY D 139     2811   4078   5100   -548    272   -545       N  
-ATOM   5889  CA  GLY D 139     -29.649 -12.902   4.057  1.00 30.02           C  
-ANISOU 5889  CA  GLY D 139     2740   3829   4837   -653    342   -457       C  
-ATOM   5890  C   GLY D 139     -30.033 -13.572   2.750  1.00 30.21           C  
-ANISOU 5890  C   GLY D 139     2584   3979   4918   -590    227   -619       C  
-ATOM   5891  O   GLY D 139     -29.474 -14.607   2.386  1.00 34.21           O  
-ANISOU 5891  O   GLY D 139     3166   4451   5380   -660    264   -564       O  
-ATOM   5892  N   LYS D 140     -30.985 -12.986   2.031  1.00 33.28           N  
-ANISOU 5892  N   LYS D 140     2737   4517   5391   -418     57   -848       N  
-ATOM   5893  CA  LYS D 140     -31.454 -13.573   0.772  1.00 38.01           C  
-ANISOU 5893  CA  LYS D 140     3147   5269   6028   -286   -114  -1082       C  
-ATOM   5894  C   LYS D 140     -30.377 -13.616  -0.312  1.00 38.12           C  
-ANISOU 5894  C   LYS D 140     3366   5310   5808   -113   -283   -824       C  
-ATOM   5895  O   LYS D 140     -30.286 -14.582  -1.073  1.00 40.69           O  
-ANISOU 5895  O   LYS D 140     3637   5696   6128   -116   -324   -923       O  
-ATOM   5896  CB  LYS D 140     -32.689 -12.829   0.257  1.00 45.73           C  
-ANISOU 5896  CB  LYS D 140     3849   6418   7109    -38   -334  -1427       C  
-ATOM   5897  CG  LYS D 140     -33.979 -13.152   1.013  1.00 54.79           C  
-ANISOU 5897  CG  LYS D 140     4849   7502   8467   -203   -127  -1766       C  
-ATOM   5898  CD  LYS D 140     -35.197 -12.562   0.309  1.00 60.61           C  
-ANISOU 5898  CD  LYS D 140     5400   8379   9252     84   -380  -2138       C  
-ATOM   5899  CE  LYS D 140     -35.610 -11.231   0.914  1.00 63.14           C  
-ANISOU 5899  CE  LYS D 140     5700   8700   9591    193   -437  -2128       C  
-ATOM   5900  NZ  LYS D 140     -36.542 -11.439   2.058  1.00 67.11           N  
-ANISOU 5900  NZ  LYS D 140     6096   9080  10322    -64   -135  -2375       N  
-ATOM   5901  N   THR D 141     -29.564 -12.569  -0.387  1.00 38.38           N  
-ANISOU 5901  N   THR D 141     3631   5278   5675     23   -339   -521       N  
-ATOM   5902  CA  THR D 141     -28.516 -12.514  -1.400  1.00 38.09           C  
-ANISOU 5902  CA  THR D 141     3811   5220   5441    166   -410   -286       C  
-ATOM   5903  C   THR D 141     -27.536 -13.660  -1.200  1.00 36.65           C  
-ANISOU 5903  C   THR D 141     3697   4960   5267    -60   -279   -174       C  
-ATOM   5904  O   THR D 141     -27.161 -14.346  -2.148  1.00 36.36           O  
-ANISOU 5904  O   THR D 141     3693   4974   5148     -3   -334   -172       O  
-ATOM   5905  CB  THR D 141     -27.766 -11.166  -1.372  1.00 36.54           C  
-ANISOU 5905  CB  THR D 141     3848   4892   5144    286   -376    -12       C  
-ATOM   5906  OG1 THR D 141     -28.714 -10.098  -1.494  1.00 42.89           O  
-ANISOU 5906  OG1 THR D 141     4624   5741   5931    523   -497   -109       O  
-ATOM   5907  CG2 THR D 141     -26.759 -11.081  -2.511  1.00 39.77           C  
-ANISOU 5907  CG2 THR D 141     4497   5239   5375    426   -361    195       C  
-ATOM   5908  N   MET D 142     -27.135 -13.888   0.043  1.00 29.59           N  
-ANISOU 5908  N   MET D 142     2851   3945   4449   -279   -121    -99       N  
-ATOM   5909  CA AMET D 142     -26.148 -14.919   0.345  0.49 28.73           C  
-ANISOU 5909  CA AMET D 142     2855   3742   4318   -428    -29      5       C  
-ATOM   5910  CA BMET D 142     -26.145 -14.923   0.305  0.51 28.31           C  
-ANISOU 5910  CA BMET D 142     2801   3692   4263   -424    -33      5       C  
-ATOM   5911  C   MET D 142     -26.712 -16.330   0.189  1.00 26.36           C  
-ANISOU 5911  C   MET D 142     2460   3464   4093   -552     46   -180       C  
-ATOM   5912  O   MET D 142     -26.034 -17.226  -0.308  1.00 29.17           O  
-ANISOU 5912  O   MET D 142     2875   3800   4406   -579     44   -134       O  
-ATOM   5913  CB AMET D 142     -25.575 -14.722   1.753  0.49 29.73           C  
-ANISOU 5913  CB AMET D 142     3116   3732   4447   -532     71    109       C  
-ATOM   5914  CB BMET D 142     -25.454 -14.732   1.659  0.51 29.75           C  
-ANISOU 5914  CB BMET D 142     3126   3735   4443   -524     62    123       C  
-ATOM   5915  CG AMET D 142     -24.242 -15.408   1.973  0.49 29.14           C  
-ANISOU 5915  CG AMET D 142     3194   3565   4313   -563     73    225       C  
-ATOM   5916  CG BMET D 142     -24.401 -13.631   1.687  0.51 30.52           C  
-ANISOU 5916  CG BMET D 142     3298   3775   4522   -440      8    272       C  
-ATOM   5917  SD AMET D 142     -23.111 -15.161   0.584  0.49 37.02           S  
-ANISOU 5917  SD AMET D 142     4183   4593   5289   -462    -17    326       S  
-ATOM   5918  SD BMET D 142     -22.979 -13.795   0.575  0.51 33.39           S  
-ANISOU 5918  SD BMET D 142     3720   4105   4860   -387    -18    384       S  
-ATOM   5919  CE AMET D 142     -22.850 -13.389   0.626  0.49 34.97           C  
-ANISOU 5919  CE AMET D 142     3927   4284   5077   -370    -10    404       C  
-ATOM   5920  CE BMET D 142     -22.777 -15.568   0.485  0.51 40.51           C  
-ANISOU 5920  CE BMET D 142     4646   5024   5724   -477    -18    333       C  
-ATOM   5921  N   GLN D 143     -27.948 -16.537   0.629  1.00 29.92           N  
-ANISOU 5921  N   GLN D 143     2747   3931   4689   -644    149   -421       N  
-ATOM   5922  CA  GLN D 143     -28.547 -17.863   0.465  1.00 30.53           C  
-ANISOU 5922  CA  GLN D 143     2701   3986   4913   -796    292   -660       C  
-ATOM   5923  C   GLN D 143     -28.610 -18.207  -1.019  1.00 36.28           C  
-ANISOU 5923  C   GLN D 143     3275   4886   5625   -646     81   -799       C  
-ATOM   5924  O   GLN D 143     -28.359 -19.345  -1.416  1.00 38.28           O  
-ANISOU 5924  O   GLN D 143     3523   5107   5916   -733    141   -862       O  
-ATOM   5925  CB  GLN D 143     -29.922 -17.937   1.124  1.00 42.52           C  
-ANISOU 5925  CB  GLN D 143     4053   5471   6632   -913    484   -954       C  
-ATOM   5926  CG  GLN D 143     -29.855 -18.387   2.585  1.00 48.58           C  
-ANISOU 5926  CG  GLN D 143     5101   5995   7360  -1081    809   -833       C  
-ATOM   5927  CD  GLN D 143     -31.213 -18.416   3.255  1.00 56.48           C  
-ANISOU 5927  CD  GLN D 143     6018   6932   8510  -1147   1033  -1102       C  
-ATOM   5928  OE1 GLN D 143     -32.210 -17.970   2.683  1.00 58.43           O  
-ANISOU 5928  OE1 GLN D 143     5974   7320   8909  -1066    916  -1393       O  
-ATOM   5929  NE2 GLN D 143     -31.259 -18.940   4.475  1.00 56.83           N  
-ANISOU 5929  NE2 GLN D 143     6340   6748   8503  -1266   1360  -1033       N  
-ATOM   5930  N   THR D 144     -28.902 -17.196  -1.835  1.00 40.70           N  
-ANISOU 5930  N   THR D 144     3759   5611   6094   -383   -168   -835       N  
-ATOM   5931  CA  THR D 144     -28.947 -17.349  -3.287  1.00 43.68           C  
-ANISOU 5931  CA  THR D 144     4075   6159   6361   -139   -406   -951       C  
-ATOM   5932  C   THR D 144     -27.574 -17.711  -3.851  1.00 40.53           C  
-ANISOU 5932  C   THR D 144     3923   5701   5776   -124   -400   -656       C  
-ATOM   5933  O   THR D 144     -27.431 -18.652  -4.635  1.00 39.92           O  
-ANISOU 5933  O   THR D 144     3797   5683   5687   -113   -444   -768       O  
-ATOM   5934  CB  THR D 144     -29.417 -16.056  -3.963  1.00 45.09           C  
-ANISOU 5934  CB  THR D 144     4272   6472   6386    220   -657   -977       C  
-ATOM   5935  OG1 THR D 144     -30.797 -15.834  -3.658  1.00 49.15           O  
-ANISOU 5935  OG1 THR D 144     4479   7090   7106    257   -725  -1365       O  
-ATOM   5936  CG2 THR D 144     -29.248 -16.149  -5.477  1.00 47.87           C  
-ANISOU 5936  CG2 THR D 144     4714   6968   6505    548   -893  -1019       C  
-ATOM   5937  N   LEU D 145     -26.564 -16.950  -3.456  1.00 34.03           N  
-ANISOU 5937  N   LEU D 145     3329   4758   4841   -126   -338   -326       N  
-ATOM   5938  CA  LEU D 145     -25.208 -17.195  -3.927  1.00 34.02           C  
-ANISOU 5938  CA  LEU D 145     3518   4685   4725   -128   -300    -98       C  
-ATOM   5939  C   LEU D 145     -24.704 -18.569  -3.484  1.00 35.60           C  
-ANISOU 5939  C   LEU D 145     3706   4801   5020   -348   -189   -119       C  
-ATOM   5940  O   LEU D 145     -24.070 -19.285  -4.261  1.00 37.06           O  
-ANISOU 5940  O   LEU D 145     3928   5003   5152   -329   -209   -105       O  
-ATOM   5941  CB  LEU D 145     -24.263 -16.096  -3.440  1.00 32.22           C  
-ANISOU 5941  CB  LEU D 145     3459   4322   4459   -124   -219    158       C  
-ATOM   5942  CG  LEU D 145     -22.825 -16.274  -3.917  1.00 37.00           C  
-ANISOU 5942  CG  LEU D 145     4201   4836   5022   -144   -140    318       C  
-ATOM   5943  CD1 LEU D 145     -22.787 -16.409  -5.449  1.00 39.54           C  
-ANISOU 5943  CD1 LEU D 145     4613   5241   5170     50   -187    314       C  
-ATOM   5944  CD2 LEU D 145     -21.965 -15.112  -3.439  1.00 35.93           C  
-ANISOU 5944  CD2 LEU D 145     4161   4552   4937   -158    -29    470       C  
-ATOM   5945  N   LEU D 146     -25.002 -18.944  -2.243  1.00 26.47           N  
-ANISOU 5945  N   LEU D 146     2540   3534   3982   -530    -55   -152       N  
-ATOM   5946  CA  LEU D 146     -24.532 -20.223  -1.715  1.00 27.97           C  
-ANISOU 5946  CA  LEU D 146     2821   3587   4218   -689     78   -143       C  
-ATOM   5947  C   LEU D 146     -25.121 -21.389  -2.509  1.00 32.42           C  
-ANISOU 5947  C   LEU D 146     3237   4204   4877   -744    103   -378       C  
-ATOM   5948  O   LEU D 146     -24.415 -22.334  -2.858  1.00 31.11           O  
-ANISOU 5948  O   LEU D 146     3143   3984   4694   -777    122   -345       O  
-ATOM   5949  CB  LEU D 146     -24.862 -20.353  -0.215  1.00 27.45           C  
-ANISOU 5949  CB  LEU D 146     2877   3355   4200   -823    265   -125       C  
-ATOM   5950  CG  LEU D 146     -23.940 -19.531   0.685  1.00 26.92           C  
-ANISOU 5950  CG  LEU D 146     2991   3213   4026   -756    217     81       C  
-ATOM   5951  CD1 LEU D 146     -24.414 -19.528   2.119  1.00 28.55           C  
-ANISOU 5951  CD1 LEU D 146     3353   3277   4217   -828    386     84       C  
-ATOM   5952  CD2 LEU D 146     -22.514 -20.065   0.606  1.00 29.65           C  
-ANISOU 5952  CD2 LEU D 146     3478   3492   4297   -698    140    197       C  
-ATOM   5953  N   SER D 147     -26.413 -21.306  -2.804  1.00 34.40           N  
-ANISOU 5953  N   SER D 147     3248   4564   5258   -742     89   -664       N  
-ATOM   5954  CA  SER D 147     -27.099 -22.333  -3.582  1.00 41.28           C  
-ANISOU 5954  CA  SER D 147     3894   5507   6282   -784     93   -998       C  
-ATOM   5955  C   SER D 147     -26.457 -22.545  -4.963  1.00 40.90           C  
-ANISOU 5955  C   SER D 147     3856   5609   6076   -594   -124   -978       C  
-ATOM   5956  O   SER D 147     -26.379 -23.669  -5.457  1.00 41.90           O  
-ANISOU 5956  O   SER D 147     3913   5723   6284   -665    -86  -1131       O  
-ATOM   5957  CB  SER D 147     -28.579 -21.982  -3.734  1.00 48.10           C  
-ANISOU 5957  CB  SER D 147     4502   6487   7287   -712     47  -1351       C  
-ATOM   5958  OG  SER D 147     -28.756 -20.903  -4.634  1.00 55.46           O  
-ANISOU 5958  OG  SER D 147     5316   7665   8091   -423   -279  -1411       O  
-ATOM   5959  N   LEU D 148     -25.991 -21.469  -5.583  1.00 37.22           N  
-ANISOU 5959  N   LEU D 148     3508   5253   5382   -355   -309   -790       N  
-ATOM   5960  CA  LEU D 148     -25.283 -21.595  -6.855  1.00 40.79           C  
-ANISOU 5960  CA  LEU D 148     4058   5804   5638   -167   -442   -727       C  
-ATOM   5961  C   LEU D 148     -23.912 -22.241  -6.656  1.00 41.74           C  
-ANISOU 5961  C   LEU D 148     4349   5770   5739   -308   -310   -492       C  
-ATOM   5962  O   LEU D 148     -23.553 -23.202  -7.344  1.00 44.16           O  
-ANISOU 5962  O   LEU D 148     4636   6100   6044   -317   -321   -575       O  
-ATOM   5963  CB  LEU D 148     -25.113 -20.234  -7.529  1.00 43.65           C  
-ANISOU 5963  CB  LEU D 148     4594   6245   5744    129   -573   -561       C  
-ATOM   5964  CG  LEU D 148     -24.348 -20.342  -8.846  1.00 45.40           C  
-ANISOU 5964  CG  LEU D 148     5001   6523   5725    332   -629   -473       C  
-ATOM   5965  CD1 LEU D 148     -25.052 -21.324  -9.763  1.00 46.00           C  
-ANISOU 5965  CD1 LEU D 148     4895   6782   5800    448   -802   -829       C  
-ATOM   5966  CD2 LEU D 148     -24.251 -19.007  -9.518  1.00 51.14           C  
-ANISOU 5966  CD2 LEU D 148     5996   7262   6173    646   -675   -297       C  
-ATOM   5967  N   VAL D 149     -23.151 -21.718  -5.702  1.00 33.87           N  
-ANISOU 5967  N   VAL D 149     3499   4626   4745   -395   -210   -246       N  
-ATOM   5968  CA  VAL D 149     -21.782 -22.175  -5.486  1.00 30.08           C  
-ANISOU 5968  CA  VAL D 149     3152   4018   4259   -467   -141    -80       C  
-ATOM   5969  C   VAL D 149     -21.690 -23.662  -5.138  1.00 30.54           C  
-ANISOU 5969  C   VAL D 149     3205   3974   4426   -611    -64   -176       C  
-ATOM   5970  O   VAL D 149     -20.820 -24.374  -5.648  1.00 34.43           O  
-ANISOU 5970  O   VAL D 149     3738   4441   4903   -604    -72   -160       O  
-ATOM   5971  CB  VAL D 149     -21.079 -21.321  -4.418  1.00 30.60           C  
-ANISOU 5971  CB  VAL D 149     3325   3962   4341   -497    -95    101       C  
-ATOM   5972  CG1 VAL D 149     -19.774 -21.970  -3.977  1.00 30.34           C  
-ANISOU 5972  CG1 VAL D 149     3377   3802   4349   -544    -74    162       C  
-ATOM   5973  CG2 VAL D 149     -20.817 -19.912  -4.975  1.00 33.19           C  
-ANISOU 5973  CG2 VAL D 149     3698   4329   4585   -364   -104    215       C  
-ATOM   5974  N   ARG D 150     -22.593 -24.129  -4.285  1.00 29.26           N  
-ANISOU 5974  N   ARG D 150     3013   3722   4381   -742     53   -286       N  
-ATOM   5975  CA  ARG D 150     -22.568 -25.517  -3.837  1.00 32.24           C  
-ANISOU 5975  CA  ARG D 150     3470   3920   4859   -881    213   -356       C  
-ATOM   5976  C   ARG D 150     -22.700 -26.524  -4.974  1.00 36.65           C  
-ANISOU 5976  C   ARG D 150     3885   4551   5491   -895    191   -560       C  
-ATOM   5977  O   ARG D 150     -22.273 -27.675  -4.859  1.00 35.39           O  
-ANISOU 5977  O   ARG D 150     3825   4235   5386   -970    298   -574       O  
-ATOM   5978  CB  ARG D 150     -23.659 -25.764  -2.800  1.00 33.18           C  
-ANISOU 5978  CB  ARG D 150     3608   3888   5110  -1039    447   -464       C  
-ATOM   5979  CG  ARG D 150     -23.326 -25.178  -1.441  1.00 36.79           C  
-ANISOU 5979  CG  ARG D 150     4317   4201   5462  -1022    514   -248       C  
-ATOM   5980  CD  ARG D 150     -24.033 -25.915  -0.314  1.00 43.40           C  
-ANISOU 5980  CD  ARG D 150     5350   4768   6372  -1176    853   -297       C  
-ATOM   5981  NE  ARG D 150     -23.590 -25.409   0.980  1.00 49.30           N  
-ANISOU 5981  NE  ARG D 150     6411   5380   6941  -1090    882    -83       N  
-ATOM   5982  CZ  ARG D 150     -24.182 -24.408   1.623  1.00 55.33           C  
-ANISOU 5982  CZ  ARG D 150     7141   6186   7697  -1102    912    -76       C  
-ATOM   5983  NH1 ARG D 150     -25.251 -23.828   1.090  1.00 49.64           N  
-ANISOU 5983  NH1 ARG D 150     6087   5637   7139  -1175    903   -270       N  
-ATOM   5984  NH2 ARG D 150     -23.715 -23.991   2.798  1.00 57.56           N  
-ANISOU 5984  NH2 ARG D 150     7722   6354   7794   -992    914     94       N  
-ATOM   5985  N   GLN D 151     -23.290 -26.091  -6.077  1.00 37.71           N  
-ANISOU 5985  N   GLN D 151     3809   4917   5602   -783     35   -732       N  
-ATOM   5986  CA  GLN D 151     -23.506 -26.993  -7.202  1.00 41.22           C  
-ANISOU 5986  CA  GLN D 151     4095   5465   6100   -756    -26   -987       C  
-ATOM   5987  C   GLN D 151     -22.201 -27.349  -7.899  1.00 39.86           C  
-ANISOU 5987  C   GLN D 151     4057   5300   5789   -674    -91   -829       C  
-ATOM   5988  O   GLN D 151     -22.150 -28.287  -8.695  1.00 43.22           O  
-ANISOU 5988  O   GLN D 151     4397   5765   6258   -673   -112  -1008       O  
-ATOM   5989  CB  GLN D 151     -24.500 -26.383  -8.187  1.00 47.29           C  
-ANISOU 5989  CB  GLN D 151     4640   6501   6826   -564   -235  -1254       C  
-ATOM   5990  CG  GLN D 151     -25.886 -26.193  -7.591  1.00 53.84           C  
-ANISOU 5990  CG  GLN D 151     5258   7334   7867   -645   -170  -1524       C  
-ATOM   5991  CD  GLN D 151     -26.916 -25.797  -8.625  1.00 67.27           C  
-ANISOU 5991  CD  GLN D 151     6764   9280   9515   -372   -412  -1851       C  
-ATOM   5992  OE1 GLN D 151     -26.770 -24.780  -9.306  1.00 70.97           O  
-ANISOU 5992  OE1 GLN D 151     7263   9958   9745    -96   -680  -1795       O  
-ATOM   5993  NE2 GLN D 151     -27.965 -26.605  -8.756  1.00 72.98           N  
-ANISOU 5993  NE2 GLN D 151     7317   9965  10446   -400   -309  -2211       N  
-ATOM   5994  N   TYR D 152     -21.147 -26.601  -7.587  1.00 33.64           N  
-ANISOU 5994  N   TYR D 152     3446   4464   4870   -614   -107   -540       N  
-ATOM   5995  CA  TYR D 152     -19.851 -26.796  -8.222  1.00 34.85           C  
-ANISOU 5995  CA  TYR D 152     3690   4615   4939   -548   -133   -430       C  
-ATOM   5996  C   TYR D 152     -18.922 -27.608  -7.345  1.00 30.99           C  
-ANISOU 5996  C   TYR D 152     3317   3917   4541   -640    -60   -345       C  
-ATOM   5997  O   TYR D 152     -17.736 -27.738  -7.641  1.00 32.07           O  
-ANISOU 5997  O   TYR D 152     3498   4028   4660   -591    -83   -285       O  
-ATOM   5998  CB  TYR D 152     -19.234 -25.450  -8.619  1.00 36.62           C  
-ANISOU 5998  CB  TYR D 152     4000   4902   5011   -415   -157   -252       C  
-ATOM   5999  CG  TYR D 152     -20.029 -24.814  -9.735  1.00 44.76           C  
-ANISOU 5999  CG  TYR D 152     5018   6123   5865   -223   -247   -332       C  
-ATOM   6000  CD1 TYR D 152     -21.099 -23.970  -9.458  1.00 52.31           C  
-ANISOU 6000  CD1 TYR D 152     5934   7152   6788   -148   -318   -367       C  
-ATOM   6001  CD2 TYR D 152     -19.754 -25.111 -11.067  1.00 47.75           C  
-ANISOU 6001  CD2 TYR D 152     5445   6612   6088    -74   -283   -404       C  
-ATOM   6002  CE1 TYR D 152     -21.856 -23.414 -10.478  1.00 58.16           C  
-ANISOU 6002  CE1 TYR D 152     6694   8072   7332    113   -461   -478       C  
-ATOM   6003  CE2 TYR D 152     -20.501 -24.556 -12.095  1.00 53.10           C  
-ANISOU 6003  CE2 TYR D 152     6183   7464   6530    195   -409   -495       C  
-ATOM   6004  CZ  TYR D 152     -21.549 -23.705 -11.795  1.00 58.12           C  
-ANISOU 6004  CZ  TYR D 152     6787   8172   7124    308   -517   -537       C  
-ATOM   6005  OH  TYR D 152     -22.303 -23.150 -12.812  1.00 59.63           O  
-ANISOU 6005  OH  TYR D 152     7068   8542   7046    658   -699   -659       O  
-ATOM   6006  N   ASN D 153     -19.488 -28.155  -6.274  1.00 29.37           N  
-ANISOU 6006  N   ASN D 153     3183   3549   4430   -749     43   -364       N  
-ATOM   6007  CA AASN D 153     -18.753 -29.026  -5.359  0.72 29.75           C  
-ANISOU 6007  CA AASN D 153     3440   3361   4502   -762    107   -287       C  
-ATOM   6008  CA BASN D 153     -18.765 -29.032  -5.355  0.28 30.02           C  
-ANISOU 6008  CA BASN D 153     3474   3394   4537   -763    108   -288       C  
-ATOM   6009  C   ASN D 153     -17.437 -28.452  -4.871  1.00 31.06           C  
-ANISOU 6009  C   ASN D 153     3705   3498   4599   -633    -16   -145       C  
-ATOM   6010  O   ASN D 153     -16.382 -29.060  -5.078  1.00 27.70           O  
-ANISOU 6010  O   ASN D 153     3312   3022   4190   -559    -83   -169       O  
-ATOM   6011  CB AASN D 153     -18.511 -30.388  -6.001  0.72 30.66           C  
-ANISOU 6011  CB AASN D 153     3547   3410   4694   -794    150   -416       C  
-ATOM   6012  CB BASN D 153     -18.530 -30.397  -6.005  0.28 31.23           C  
-ANISOU 6012  CB BASN D 153     3617   3481   4767   -796    152   -419       C  
-ATOM   6013  CG AASN D 153     -19.792 -31.131  -6.240  0.72 33.52           C  
-ANISOU 6013  CG AASN D 153     3798   3734   5204   -945    313   -635       C  
-ATOM   6014  CG BASN D 153     -18.396 -31.518  -4.988  0.28 34.99           C  
-ANISOU 6014  CG BASN D 153     4372   3646   5277   -820    304   -382       C  
-ATOM   6015  OD1AASN D 153     -20.805 -30.833  -5.608  0.72 38.47           O  
-ANISOU 6015  OD1AASN D 153     4410   4308   5897  -1043    445   -681       O  
-ATOM   6016  OD1BASN D 153     -18.573 -31.316  -3.785  0.28 38.84           O  
-ANISOU 6016  OD1BASN D 153     5092   3966   5701   -801    391   -261       O  
-ATOM   6017  ND2AASN D 153     -19.770 -32.094  -7.151  0.72 35.26           N  
-ANISOU 6017  ND2AASN D 153     3906   3978   5514   -976    322   -819       N  
-ATOM   6018  ND2BASN D 153     -18.100 -32.715  -5.474  0.28 38.16           N  
-ANISOU 6018  ND2BASN D 153     4799   3947   5753   -836    354   -483       N  
-ATOM   6019  N   PRO D 154     -17.485 -27.270  -4.218  1.00 26.76           N  
-ANISOU 6019  N   PRO D 154     3172   2985   4010   -601    -53    -49       N  
-ATOM   6020  CA  PRO D 154     -16.239 -26.793  -3.618  1.00 25.68           C  
-ANISOU 6020  CA  PRO D 154     3086   2803   3868   -477   -174     -5       C  
-ATOM   6021  C   PRO D 154     -15.871 -27.730  -2.476  1.00 26.75           C  
-ANISOU 6021  C   PRO D 154     3489   2730   3945   -367   -209      5       C  
-ATOM   6022  O   PRO D 154     -16.733 -28.466  -1.989  1.00 28.16           O  
-ANISOU 6022  O   PRO D 154     3860   2764   4075   -425    -59     38       O  
-ATOM   6023  CB  PRO D 154     -16.615 -25.420  -3.070  1.00 25.72           C  
-ANISOU 6023  CB  PRO D 154     3058   2862   3852   -481   -178     67       C  
-ATOM   6024  CG  PRO D 154     -18.095 -25.509  -2.784  1.00 26.54           C  
-ANISOU 6024  CG  PRO D 154     3205   2958   3923   -584    -57     85       C  
-ATOM   6025  CD  PRO D 154     -18.649 -26.444  -3.840  1.00 26.88           C  
-ANISOU 6025  CD  PRO D 154     3151   3052   4011   -664      9    -25       C  
-ATOM   6026  N   LYS D 155     -14.616 -27.714  -2.047  1.00 29.98           N  
-ANISOU 6026  N   LYS D 155     3929   3100   4361   -188   -386    -54       N  
-ATOM   6027  CA  LYS D 155     -14.226 -28.532  -0.895  1.00 33.75           C  
-ANISOU 6027  CA  LYS D 155     4742   3376   4707     27   -477    -50       C  
-ATOM   6028  C   LYS D 155     -14.923 -28.016   0.363  1.00 32.06           C  
-ANISOU 6028  C   LYS D 155     4774   3072   4337     77   -428     59       C  
-ATOM   6029  O   LYS D 155     -15.319 -28.781   1.244  1.00 32.03           O  
-ANISOU 6029  O   LYS D 155     5167   2845   4158    176   -325    144       O  
-ATOM   6030  CB  LYS D 155     -12.710 -28.497  -0.713  1.00 36.56           C  
-ANISOU 6030  CB  LYS D 155     5015   3752   5124    268   -751   -228       C  
-ATOM   6031  CG  LYS D 155     -12.191 -29.238   0.504  1.00 38.38           C  
-ANISOU 6031  CG  LYS D 155     5630   3792   5160    614   -938   -260       C  
-ATOM   6032  CD  LYS D 155     -10.679 -29.361   0.438  1.00 47.02           C  
-ANISOU 6032  CD  LYS D 155     6546   4939   6378    869  -1249   -539       C  
-ATOM   6033  CE  LYS D 155     -10.132 -30.152   1.614  1.00 53.47           C  
-ANISOU 6033  CE  LYS D 155     7795   5573   6949   1321  -1508   -603       C  
-ATOM   6034  NZ  LYS D 155     -10.719 -31.514   1.643  1.00 58.34           N  
-ANISOU 6034  NZ  LYS D 155     8855   5940   7371   1346  -1314   -402       N  
-ATOM   6035  N   MET D 156     -15.045 -26.698   0.446  1.00 29.03           N  
-ANISOU 6035  N   MET D 156     4187   2834   4010     18   -468     56       N  
-ATOM   6036  CA  MET D 156     -15.804 -26.050   1.510  1.00 31.43           C  
-ANISOU 6036  CA  MET D 156     4664   3088   4191     30   -404    145       C  
-ATOM   6037  C   MET D 156     -16.155 -24.660   1.010  1.00 31.44           C  
-ANISOU 6037  C   MET D 156     4342   3277   4328   -128   -382    144       C  
-ATOM   6038  O   MET D 156     -15.512 -24.130   0.093  1.00 27.89           O  
-ANISOU 6038  O   MET D 156     3614   2952   4032   -172   -438     70       O  
-ATOM   6039  CB  MET D 156     -15.005 -25.964   2.823  1.00 34.10           C  
-ANISOU 6039  CB  MET D 156     5264   3332   4359    355   -629     89       C  
-ATOM   6040  CG  MET D 156     -13.961 -24.858   2.859  1.00 36.91           C  
-ANISOU 6040  CG  MET D 156     5310   3846   4869    460   -885   -103       C  
-ATOM   6041  SD  MET D 156     -13.208 -24.590   4.491  1.00 38.55           S  
-ANISOU 6041  SD  MET D 156     5780   3992   4873    890  -1210   -261       S  
-ATOM   6042  CE  MET D 156     -12.393 -26.151   4.743  1.00 35.69           C  
-ANISOU 6042  CE  MET D 156     5772   3467   4323   1244  -1398   -328       C  
-ATOM   6043  N   VAL D 157     -17.200 -24.080   1.578  1.00 27.31           N  
-ANISOU 6043  N   VAL D 157     3886   2744   3746   -209   -258    223       N  
-ATOM   6044  CA  VAL D 157     -17.546 -22.711   1.241  1.00 24.40           C  
-ANISOU 6044  CA  VAL D 157     3270   2522   3479   -306   -252    228       C  
-ATOM   6045  C   VAL D 157     -17.903 -21.981   2.528  1.00 28.08           C  
-ANISOU 6045  C   VAL D 157     3879   2940   3850   -237   -261    254       C  
-ATOM   6046  O   VAL D 157     -18.671 -22.488   3.349  1.00 28.18           O  
-ANISOU 6046  O   VAL D 157     4156   2826   3725   -238   -124    314       O  
-ATOM   6047  CB  VAL D 157     -18.657 -22.620   0.139  1.00 31.87           C  
-ANISOU 6047  CB  VAL D 157     4042   3575   4493   -487   -104    250       C  
-ATOM   6048  CG1 VAL D 157     -19.895 -23.421   0.522  1.00 38.83           C  
-ANISOU 6048  CG1 VAL D 157     5051   4361   5340   -595     87    243       C  
-ATOM   6049  CG2 VAL D 157     -19.002 -21.159  -0.169  1.00 24.38           C  
-ANISOU 6049  CG2 VAL D 157     2919   2745   3599   -513   -110    272       C  
-ATOM   6050  N   LYS D 158     -17.278 -20.820   2.728  1.00 24.35           N  
-ANISOU 6050  N   LYS D 158     3248   2539   3464   -175   -390    187       N  
-ATOM   6051  CA  LYS D 158     -17.469 -20.020   3.927  1.00 23.12           C  
-ANISOU 6051  CA  LYS D 158     3192   2359   3233    -86   -439    170       C  
-ATOM   6052  C   LYS D 158     -17.718 -18.593   3.499  1.00 26.38           C  
-ANISOU 6052  C   LYS D 158     3342   2870   3813   -199   -395    164       C  
-ATOM   6053  O   LYS D 158     -17.260 -18.174   2.434  1.00 26.14           O  
-ANISOU 6053  O   LYS D 158     3093   2892   3945   -271   -367    141       O  
-ATOM   6054  CB  LYS D 158     -16.222 -20.037   4.820  1.00 24.88           C  
-ANISOU 6054  CB  LYS D 158     3496   2546   3412    183   -700      1       C  
-ATOM   6055  CG  LYS D 158     -15.776 -21.402   5.313  1.00 34.82           C  
-ANISOU 6055  CG  LYS D 158     5088   3684   4460    403   -800     -6       C  
-ATOM   6056  CD  LYS D 158     -16.747 -21.963   6.319  1.00 40.65           C  
-ANISOU 6056  CD  LYS D 158     6282   4262   4902    463   -632    152       C  
-ATOM   6057  CE  LYS D 158     -16.160 -23.171   7.028  1.00 46.07           C  
-ANISOU 6057  CE  LYS D 158     7421   4771   5312    786   -742    148       C  
-ATOM   6058  NZ  LYS D 158     -17.121 -23.676   8.033  1.00 50.21           N  
-ANISOU 6058  NZ  LYS D 158     8476   5072   5529    839   -473    322       N  
-ATOM   6059  N   VAL D 159     -18.436 -17.847   4.330  1.00 21.97           N  
-ANISOU 6059  N   VAL D 159     2843   2305   3200   -201   -355    188       N  
-ATOM   6060  CA  VAL D 159     -18.748 -16.462   4.009  1.00 21.23           C  
-ANISOU 6060  CA  VAL D 159     2543   2272   3251   -284   -304    190       C  
-ATOM   6061  C   VAL D 159     -18.198 -15.550   5.087  1.00 24.35           C  
-ANISOU 6061  C   VAL D 159     2920   2644   3686   -170   -424     60       C  
-ATOM   6062  O   VAL D 159     -18.433 -15.793   6.278  1.00 23.25           O  
-ANISOU 6062  O   VAL D 159     3001   2467   3367    -51   -484     39       O  
-ATOM   6063  CB  VAL D 159     -20.266 -16.247   3.898  1.00 25.28           C  
-ANISOU 6063  CB  VAL D 159     3069   2819   3716   -396   -150    286       C  
-ATOM   6064  CG1 VAL D 159     -20.587 -14.776   3.642  1.00 22.93           C  
-ANISOU 6064  CG1 VAL D 159     2612   2564   3537   -419   -122    291       C  
-ATOM   6065  CG2 VAL D 159     -20.831 -17.130   2.794  1.00 26.70           C  
-ANISOU 6065  CG2 VAL D 159     3209   3044   3892   -484    -67    326       C  
-ATOM   6066  N   ALA D 160     -17.455 -14.515   4.673  1.00 21.14           N  
-ANISOU 6066  N   ALA D 160     2276   2238   3517   -198   -429    -50       N  
-ATOM   6067  CA  ALA D 160     -17.029 -13.458   5.586  1.00 23.29           C  
-ANISOU 6067  CA  ALA D 160     2455   2491   3905   -123   -516   -230       C  
-ATOM   6068  C   ALA D 160     -17.800 -12.210   5.192  1.00 27.05           C  
-ANISOU 6068  C   ALA D 160     2837   2950   4492   -252   -334   -130       C  
-ATOM   6069  O   ALA D 160     -17.828 -11.826   4.016  1.00 25.00           O  
-ANISOU 6069  O   ALA D 160     2495   2660   4346   -353   -168    -36       O  
-ATOM   6070  CB  ALA D 160     -15.529 -13.207   5.501  1.00 23.59           C  
-ANISOU 6070  CB  ALA D 160     2256   2497   4211    -65   -620   -522       C  
-ATOM   6071  N   SER D 161     -18.441 -11.577   6.164  1.00 24.19           N  
-ANISOU 6071  N   SER D 161     2530   2594   4065   -214   -360   -147       N  
-ATOM   6072  CA  SER D 161     -19.184 -10.358   5.885  1.00 22.99           C  
-ANISOU 6072  CA  SER D 161     2301   2417   4017   -298   -212    -72       C  
-ATOM   6073  C   SER D 161     -18.714  -9.296   6.850  1.00 26.97           C  
-ANISOU 6073  C   SER D 161     2698   2874   4675   -246   -275   -281       C  
-ATOM   6074  O   SER D 161     -18.646  -9.543   8.060  1.00 26.68           O  
-ANISOU 6074  O   SER D 161     2756   2879   4502   -117   -443   -405       O  
-ATOM   6075  CB  SER D 161     -20.699 -10.584   6.043  1.00 23.52           C  
-ANISOU 6075  CB  SER D 161     2499   2546   3891   -327   -152     83       C  
-ATOM   6076  OG  SER D 161     -21.416  -9.402   5.721  1.00 27.01           O  
-ANISOU 6076  OG  SER D 161     2865   2970   4429   -356    -52    131       O  
-ATOM   6077  N   LEU D 162     -18.368  -8.118   6.338  1.00 23.13           N  
-ANISOU 6077  N   LEU D 162     2046   2280   4462   -324   -123   -338       N  
-ATOM   6078  CA  LEU D 162     -17.889  -7.070   7.225  1.00 22.73           C  
-ANISOU 6078  CA  LEU D 162     1844   2168   4623   -295   -162   -595       C  
-ATOM   6079  C   LEU D 162     -18.945  -6.754   8.273  1.00 26.75           C  
-ANISOU 6079  C   LEU D 162     2476   2748   4940   -228   -242   -552       C  
-ATOM   6080  O   LEU D 162     -18.628  -6.625   9.461  1.00 23.59           O  
-ANISOU 6080  O   LEU D 162     2067   2387   4509   -105   -421   -775       O  
-ATOM   6081  CB  LEU D 162     -17.562  -5.785   6.473  1.00 22.71           C  
-ANISOU 6081  CB  LEU D 162     1699   1973   4957   -420    119   -628       C  
-ATOM   6082  CG  LEU D 162     -17.177  -4.647   7.423  1.00 25.91           C  
-ANISOU 6082  CG  LEU D 162     1920   2299   5626   -412    104   -930       C  
-ATOM   6083  CD1 LEU D 162     -15.872  -4.953   8.161  1.00 28.10           C  
-ANISOU 6083  CD1 LEU D 162     2016   2636   6025   -291   -100  -1330       C  
-ATOM   6084  CD2 LEU D 162     -17.086  -3.315   6.696  1.00 29.45           C  
-ANISOU 6084  CD2 LEU D 162     2377   2551   6260   -472    457   -874       C  
-ATOM   6085  N   LEU D 163     -20.193  -6.633   7.818  1.00 23.81           N  
-ANISOU 6085  N   LEU D 163     2213   2395   4438   -283   -117   -305       N  
-ATOM   6086  CA  LEU D 163     -21.294  -6.203   8.676  1.00 24.32           C  
-ANISOU 6086  CA  LEU D 163     2353   2506   4381   -254   -124   -284       C  
-ATOM   6087  C   LEU D 163     -22.440  -7.196   8.609  1.00 24.37           C  
-ANISOU 6087  C   LEU D 163     2519   2607   4135   -272    -95   -119       C  
-ATOM   6088  O   LEU D 163     -22.719  -7.771   7.553  1.00 23.32           O  
-ANISOU 6088  O   LEU D 163     2391   2497   3972   -319    -39     15       O  
-ATOM   6089  CB  LEU D 163     -21.810  -4.818   8.253  1.00 26.47           C  
-ANISOU 6089  CB  LEU D 163     2537   2682   4837   -294     25   -243       C  
-ATOM   6090  CG  LEU D 163     -20.815  -3.661   8.126  1.00 27.28           C  
-ANISOU 6090  CG  LEU D 163     2481   2612   5273   -329    126   -405       C  
-ATOM   6091  CD1 LEU D 163     -21.507  -2.395   7.628  1.00 29.78           C  
-ANISOU 6091  CD1 LEU D 163     2818   2790   5706   -337    317   -297       C  
-ATOM   6092  CD2 LEU D 163     -20.104  -3.376   9.441  1.00 29.82           C  
-ANISOU 6092  CD2 LEU D 163     2680   2953   5697   -273    -33   -725       C  
-ATOM   6093  N   VAL D 164     -23.099  -7.404   9.740  1.00 23.39           N  
-ANISOU 6093  N   VAL D 164     2526   2520   3842   -235   -103   -163       N  
-ATOM   6094  CA  VAL D 164     -24.334  -8.185   9.770  1.00 24.91           C  
-ANISOU 6094  CA  VAL D 164     2831   2754   3880   -300     24    -72       C  
-ATOM   6095  C   VAL D 164     -25.345  -7.339  10.507  1.00 29.82           C  
-ANISOU 6095  C   VAL D 164     3428   3382   4522   -312    110   -141       C  
-ATOM   6096  O   VAL D 164     -25.066  -6.876  11.615  1.00 28.62           O  
-ANISOU 6096  O   VAL D 164     3357   3207   4309   -233     63   -245       O  
-ATOM   6097  CB  VAL D 164     -24.170  -9.511  10.527  1.00 30.33           C  
-ANISOU 6097  CB  VAL D 164     3796   3415   4314   -256     43    -61       C  
-ATOM   6098  CG1 VAL D 164     -25.543 -10.135  10.847  1.00 33.54           C  
-ANISOU 6098  CG1 VAL D 164     4323   3799   4623   -364    290    -36       C  
-ATOM   6099  CG2 VAL D 164     -23.329 -10.474   9.739  1.00 25.74           C  
-ANISOU 6099  CG2 VAL D 164     3233   2831   3717   -246    -34      1       C  
-ATOM   6100  N   LYS D 165     -26.506  -7.125   9.888  1.00 31.35           N  
-ANISOU 6100  N   LYS D 165     3495   3615   4803   -380    209   -124       N  
-ATOM   6101  CA  LYS D 165     -27.560  -6.301  10.488  1.00 36.99           C  
-ANISOU 6101  CA  LYS D 165     4136   4340   5577   -390    292   -225       C  
-ATOM   6102  C   LYS D 165     -28.484  -7.118  11.379  1.00 37.80           C  
-ANISOU 6102  C   LYS D 165     4372   4434   5558   -478    500   -301       C  
-ATOM   6103  O   LYS D 165     -28.925  -8.210  10.995  1.00 36.80           O  
-ANISOU 6103  O   LYS D 165     4272   4306   5404   -570    625   -296       O  
-ATOM   6104  CB  LYS D 165     -28.397  -5.614   9.401  1.00 38.93           C  
-ANISOU 6104  CB  LYS D 165     4173   4633   5986   -360    268   -234       C  
-ATOM   6105  CG  LYS D 165     -28.050  -4.162   9.195  1.00 43.58           C  
-ANISOU 6105  CG  LYS D 165     4696   5156   6708   -260    195   -216       C  
-ATOM   6106  CD  LYS D 165     -29.056  -3.448   8.291  1.00 41.18           C  
-ANISOU 6106  CD  LYS D 165     4273   4879   6494   -144    161   -236       C  
-ATOM   6107  CE  LYS D 165     -28.443  -2.163   7.782  1.00 35.99           C  
-ANISOU 6107  CE  LYS D 165     3660   4078   5936    -25    145   -141       C  
-ATOM   6108  NZ  LYS D 165     -29.331  -1.388   6.882  1.00 31.94           N  
-ANISOU 6108  NZ  LYS D 165     3135   3554   5445    182     89   -135       N  
-ATOM   6109  N   ARG D 166     -28.770  -6.601  12.573  1.00 42.83           N  
-ANISOU 6109  N   ARG D 166     3679   5755   6841   -359   1166   -489       N  
-ATOM   6110  CA  ARG D 166     -29.837  -7.167  13.391  1.00 44.72           C  
-ANISOU 6110  CA  ARG D 166     3812   6062   7118   -479   1350   -530       C  
-ATOM   6111  C   ARG D 166     -31.164  -6.665  12.840  1.00 48.16           C  
-ANISOU 6111  C   ARG D 166     3897   6692   7710   -406   1362   -536       C  
-ATOM   6112  O   ARG D 166     -31.457  -5.471  12.916  1.00 48.36           O  
-ANISOU 6112  O   ARG D 166     3836   6736   7802   -203   1403   -524       O  
-ATOM   6113  CB  ARG D 166     -29.704  -6.738  14.853  1.00 44.84           C  
-ANISOU 6113  CB  ARG D 166     4002   5968   7068   -447   1549   -549       C  
-ATOM   6114  CG  ARG D 166     -28.471  -7.271  15.583  1.00 38.86           C  
-ANISOU 6114  CG  ARG D 166     3580   5035   6149   -529   1535   -533       C  
-ATOM   6115  CD  ARG D 166     -28.603  -6.997  17.091  1.00 38.13           C  
-ANISOU 6115  CD  ARG D 166     3655   4857   5975   -543   1746   -559       C  
-ATOM   6116  NE  ARG D 166     -28.558  -5.566  17.380  1.00 36.61           N  
-ANISOU 6116  NE  ARG D 166     3486   4628   5795   -356   1794   -569       N  
-ATOM   6117  CZ  ARG D 166     -27.438  -4.855  17.431  1.00 39.27           C  
-ANISOU 6117  CZ  ARG D 166     4022   4849   6052   -273   1685   -544       C  
-ATOM   6118  NH1 ARG D 166     -26.271  -5.449  17.213  1.00 31.49           N  
-ANISOU 6118  NH1 ARG D 166     3190   3794   4980   -343   1523   -502       N  
-ATOM   6119  NH2 ARG D 166     -27.483  -3.556  17.700  1.00 43.71           N  
-ANISOU 6119  NH2 ARG D 166     4626   5361   6620   -120   1744   -560       N  
-ATOM   6120  N   THR D 167     -31.962  -7.567  12.278  1.00 53.47           N  
-ANISOU 6120  N   THR D 167     4371   7504   8440   -570   1321   -552       N  
-ATOM   6121  CA  THR D 167     -33.249  -7.191  11.692  1.00 56.75           C  
-ANISOU 6121  CA  THR D 167     4411   8139   9012   -518   1300   -548       C  
-ATOM   6122  C   THR D 167     -34.275  -8.305  11.856  1.00 59.12           C  
-ANISOU 6122  C   THR D 167     4563   8568   9331   -759   1360   -568       C  
-ATOM   6123  O   THR D 167     -33.930  -9.485  11.804  1.00 57.73           O  
-ANISOU 6123  O   THR D 167     4526   8330   9080   -990   1342   -599       O  
-ATOM   6124  CB  THR D 167     -33.114  -6.819  10.191  1.00 58.58           C  
-ANISOU 6124  CB  THR D 167     4538   8449   9271   -426   1033   -504       C  
-ATOM   6125  OG1 THR D 167     -34.412  -6.775   9.579  1.00 60.31           O  
-ANISOU 6125  OG1 THR D 167     4421   8898   9597   -428    960   -478       O  
-ATOM   6126  CG2 THR D 167     -32.259  -7.841   9.460  1.00 56.47           C  
-ANISOU 6126  CG2 THR D 167     4472   8102   8883   -596    877   -510       C  
-ATOM   6127  N   PRO D 168     -35.546  -7.931  12.073  1.00 63.70           N  
-ANISOU 6127  N   PRO D 168     4895   9316   9991   -696   1428   -536       N  
-ATOM   6128  CA  PRO D 168     -36.619  -8.931  12.110  1.00 65.66           C  
-ANISOU 6128  CA  PRO D 168     4986   9705  10254   -922   1451   -527       C  
-ATOM   6129  C   PRO D 168     -36.875  -9.565  10.731  1.00 65.51           C  
-ANISOU 6129  C   PRO D 168     4837   9805  10250  -1060   1195   -504       C  
-ATOM   6130  O   PRO D 168     -37.408 -10.675  10.657  1.00 62.82           O  
-ANISOU 6130  O   PRO D 168     4468   9510   9890  -1316   1185   -513       O  
-ATOM   6131  CB  PRO D 168     -37.839  -8.122  12.578  1.00 70.12           C  
-ANISOU 6131  CB  PRO D 168     5284  10437  10922   -761   1575   -482       C  
-ATOM   6132  CG  PRO D 168     -37.515  -6.694  12.236  1.00 68.57           C  
-ANISOU 6132  CG  PRO D 168     5057  10224  10771   -439   1516   -455       C  
-ATOM   6133  CD  PRO D 168     -36.030  -6.577  12.401  1.00 64.28           C  
-ANISOU 6133  CD  PRO D 168     4843   9440  10141   -415   1511   -504       C  
-ATOM   6134  N   ARG D 169     -36.488  -8.868   9.661  1.00 67.32           N  
-ANISOU 6134  N   ARG D 169     5013  10063  10502   -902    992   -476       N  
-ATOM   6135  CA  ARG D 169     -36.649  -9.367   8.293  1.00 69.27           C  
-ANISOU 6135  CA  ARG D 169     5170  10410  10742  -1022    736   -459       C  
-ATOM   6136  C   ARG D 169     -35.625 -10.445   7.928  1.00 68.91           C  
-ANISOU 6136  C   ARG D 169     5403  10206  10572  -1235    673   -531       C  
-ATOM   6137  O   ARG D 169     -35.570 -10.890   6.779  1.00 68.61           O  
-ANISOU 6137  O   ARG D 169     5359  10215  10495  -1343    468   -538       O  
-ATOM   6138  CB  ARG D 169     -36.524  -8.226   7.278  1.00 71.26           C  
-ANISOU 6138  CB  ARG D 169     5307  10732  11037   -773    543   -402       C  
-ATOM   6139  CG  ARG D 169     -37.765  -7.368   7.070  1.00 78.90           C  
-ANISOU 6139  CG  ARG D 169     5943  11910  12125   -598    503   -303       C  
-ATOM   6140  CD  ARG D 169     -37.417  -6.180   6.181  1.00 81.75           C  
-ANISOU 6140  CD  ARG D 169     6279  12284  12498   -325    333   -247       C  
-ATOM   6141  NE  ARG D 169     -36.144  -5.591   6.590  1.00 81.19           N  
-ANISOU 6141  NE  ARG D 169     6483  11990  12375   -179    418   -297       N  
-ATOM   6142  CZ  ARG D 169     -35.210  -5.153   5.752  1.00 79.25           C  
-ANISOU 6142  CZ  ARG D 169     6375  11649  12086    -83    261   -293       C  
-ATOM   6143  NH1 ARG D 169     -35.407  -5.228   4.442  1.00 79.38           N  
-ANISOU 6143  NH1 ARG D 169     6298  11780  12083   -110      8   -253       N  
-ATOM   6144  NH2 ARG D 169     -34.077  -4.641   6.227  1.00 75.33           N  
-ANISOU 6144  NH2 ARG D 169     6123  10940  11558     30    353   -320       N  
-ATOM   6145  N   SER D 170     -34.803 -10.847   8.894  1.00 67.13           N  
-ANISOU 6145  N   SER D 170     5438   9791  10278  -1287    848   -580       N  
-ATOM   6146  CA  SER D 170     -33.782 -11.870   8.662  1.00 65.24           C  
-ANISOU 6146  CA  SER D 170     5482   9383   9923  -1464    818   -636       C  
-ATOM   6147  C   SER D 170     -34.403 -13.247   8.411  1.00 64.09           C  
-ANISOU 6147  C   SER D 170     5369   9262   9721  -1768    790   -661       C  
-ATOM   6148  O   SER D 170     -35.295 -13.675   9.144  1.00 63.35           O  
-ANISOU 6148  O   SER D 170     5200   9219   9652  -1884    916   -651       O  
-ATOM   6149  CB  SER D 170     -32.822 -11.939   9.852  1.00 65.70           C  
-ANISOU 6149  CB  SER D 170     5844   9221   9898  -1411    994   -637       C  
-ATOM   6150  OG  SER D 170     -31.903 -13.005   9.712  1.00 67.56           O  
-ANISOU 6150  OG  SER D 170     6397   9275   9998  -1540    959   -651       O  
-ATOM   6151  N   VAL D 171     -33.931 -13.933   7.370  1.00 63.25           N  
-ANISOU 6151  N   VAL D 171     5391   9109   9533  -1899    632   -697       N  
-ATOM   6152  CA  VAL D 171     -34.407 -15.286   7.069  1.00 64.82           C  
-ANISOU 6152  CA  VAL D 171     5686   9286   9657  -2195    600   -731       C  
-ATOM   6153  C   VAL D 171     -33.654 -16.295   7.926  1.00 60.63           C  
-ANISOU 6153  C   VAL D 171     5502   8514   9021  -2324    770   -766       C  
-ATOM   6154  O   VAL D 171     -33.947 -17.494   7.907  1.00 62.43           O  
-ANISOU 6154  O   VAL D 171     5881   8666   9172  -2561    789   -794       O  
-ATOM   6155  CB  VAL D 171     -34.230 -15.660   5.580  1.00 65.16           C  
-ANISOU 6155  CB  VAL D 171     5774   9356   9626  -2295    367   -762       C  
-ATOM   6156  CG1 VAL D 171     -34.945 -14.658   4.677  1.00 67.06           C  
-ANISOU 6156  CG1 VAL D 171     5694   9829   9956  -2159    171   -711       C  
-ATOM   6157  CG2 VAL D 171     -32.742 -15.777   5.224  1.00 62.11           C  
-ANISOU 6157  CG2 VAL D 171     5720   8757   9123  -2200    344   -782       C  
-ATOM   6158  N   GLY D 172     -32.669 -15.798   8.666  1.00 55.67           N  
-ANISOU 6158  N   GLY D 172     5023   7748   8380  -2150    880   -752       N  
-ATOM   6159  CA  GLY D 172     -31.939 -16.626   9.601  1.00 55.62           C  
-ANISOU 6159  CA  GLY D 172     5356   7508   8269  -2213   1028   -751       C  
-ATOM   6160  C   GLY D 172     -30.550 -17.033   9.148  1.00 53.96           C  
-ANISOU 6160  C   GLY D 172     5481   7083   7936  -2113    943   -734       C  
-ATOM   6161  O   GLY D 172     -29.916 -17.855   9.815  1.00 56.08           O  
-ANISOU 6161  O   GLY D 172     6043   7150   8114  -2163   1041   -725       O  
-ATOM   6162  N   TYR D 173     -30.067 -16.481   8.031  1.00 44.64           N  
-ANISOU 6162  N   TYR D 173     4264   5944   6752  -1968    770   -724       N  
-ATOM   6163  CA  TYR D 173     -28.695 -16.788   7.594  1.00 42.40           C  
-ANISOU 6163  CA  TYR D 173     4274   5471   6366  -1849    713   -705       C  
-ATOM   6164  C   TYR D 173     -27.632 -16.055   8.408  1.00 43.47           C  
-ANISOU 6164  C   TYR D 173     4509   5510   6497  -1605    766   -640       C  
-ATOM   6165  O   TYR D 173     -27.670 -14.835   8.530  1.00 48.86           O  
-ANISOU 6165  O   TYR D 173     5021   6296   7248  -1437    741   -609       O  
-ATOM   6166  CB  TYR D 173     -28.445 -16.499   6.101  1.00 40.16           C  
-ANISOU 6166  CB  TYR D 173     3955   5248   6055  -1789    529   -716       C  
-ATOM   6167  CG  TYR D 173     -26.992 -16.770   5.763  1.00 38.30           C  
-ANISOU 6167  CG  TYR D 173     4004   4823   5726  -1648    514   -693       C  
-ATOM   6168  CD1 TYR D 173     -26.535 -18.073   5.611  1.00 42.05           C  
-ANISOU 6168  CD1 TYR D 173     4764   5112   6102  -1764    560   -727       C  
-ATOM   6169  CD2 TYR D 173     -26.070 -15.740   5.656  1.00 38.61           C  
-ANISOU 6169  CD2 TYR D 173     4027   4860   5782  -1398    472   -636       C  
-ATOM   6170  CE1 TYR D 173     -25.206 -18.343   5.347  1.00 37.94           C  
-ANISOU 6170  CE1 TYR D 173     4479   4424   5513  -1610    567   -701       C  
-ATOM   6171  CE2 TYR D 173     -24.734 -16.001   5.389  1.00 36.86           C  
-ANISOU 6171  CE2 TYR D 173     4028   4486   5492  -1273    473   -610       C  
-ATOM   6172  CZ  TYR D 173     -24.320 -17.309   5.234  1.00 37.51           C  
-ANISOU 6172  CZ  TYR D 173     4365   4401   5489  -1368    523   -642       C  
-ATOM   6173  OH  TYR D 173     -23.009 -17.588   4.973  1.00 37.01           O  
-ANISOU 6173  OH  TYR D 173     4496   4193   5372  -1221    540   -612       O  
-ATOM   6174  N   LYS D 174     -26.657 -16.798   8.922  1.00 44.68           N  
-ANISOU 6174  N   LYS D 174     4948   5462   6565  -1585    827   -617       N  
-ATOM   6175  CA  LYS D 174     -25.513 -16.193   9.600  1.00 44.28           C  
-ANISOU 6175  CA  LYS D 174     5003   5324   6498  -1371    841   -550       C  
-ATOM   6176  C   LYS D 174     -24.214 -16.573   8.891  1.00 33.44           C  
-ANISOU 6176  C   LYS D 174     3821   3823   5062  -1254    767   -525       C  
-ATOM   6177  O   LYS D 174     -23.994 -17.742   8.569  1.00 36.12           O  
-ANISOU 6177  O   LYS D 174     4356   4033   5336  -1346    786   -547       O  
-ATOM   6178  CB  LYS D 174     -25.460 -16.622  11.068  1.00 52.13           C  
-ANISOU 6178  CB  LYS D 174     6148   6209   7449  -1419    982   -523       C  
-ATOM   6179  CG  LYS D 174     -26.646 -16.152  11.902  1.00 57.70           C  
-ANISOU 6179  CG  LYS D 174     6675   7036   8214  -1510   1097   -544       C  
-ATOM   6180  CD  LYS D 174     -26.646 -16.794  13.287  1.00 62.66           C  
-ANISOU 6180  CD  LYS D 174     7505   7536   8766  -1602   1252   -522       C  
-ATOM   6181  CE  LYS D 174     -27.880 -16.395  14.094  1.00 67.02           C  
-ANISOU 6181  CE  LYS D 174     7881   8211   9372  -1707   1404   -552       C  
-ATOM   6182  NZ  LYS D 174     -28.158 -17.344  15.221  1.00 70.68           N  
-ANISOU 6182  NZ  LYS D 174     8552   8554   9748  -1885   1573   -545       N  
-ATOM   6183  N   PRO D 175     -23.345 -15.583   8.641  1.00 30.94           N  
-ANISOU 6183  N   PRO D 175     3452   3536   4766  -1053    695   -480       N  
-ATOM   6184  CA  PRO D 175     -22.102 -15.885   7.925  1.00 28.15           C  
-ANISOU 6184  CA  PRO D 175     3243   3085   4368   -936    643   -454       C  
-ATOM   6185  C   PRO D 175     -21.095 -16.550   8.857  1.00 30.53           C  
-ANISOU 6185  C   PRO D 175     3754   3222   4623   -868    702   -396       C  
-ATOM   6186  O   PRO D 175     -21.293 -16.568  10.067  1.00 33.16           O  
-ANISOU 6186  O   PRO D 175     4125   3527   4948   -900    764   -370       O  
-ATOM   6187  CB  PRO D 175     -21.605 -14.503   7.491  1.00 28.92           C  
-ANISOU 6187  CB  PRO D 175     3192   3285   4511   -770    561   -418       C  
-ATOM   6188  CG  PRO D 175     -22.171 -13.567   8.482  1.00 29.79           C  
-ANISOU 6188  CG  PRO D 175     3173   3474   4673   -754    594   -403       C  
-ATOM   6189  CD  PRO D 175     -23.494 -14.144   8.916  1.00 29.54           C  
-ANISOU 6189  CD  PRO D 175     3087   3480   4656   -933    669   -454       C  
-ATOM   6190  N   ASP D 176     -20.028 -17.094   8.293  1.00 29.78           N  
-ANISOU 6190  N   ASP D 176     3796   3024   4494   -767    684   -372       N  
-ATOM   6191  CA  ASP D 176     -19.054 -17.822   9.083  1.00 30.98           C  
-ANISOU 6191  CA  ASP D 176     4141   3023   4609   -679    724   -306       C  
-ATOM   6192  C   ASP D 176     -18.103 -16.876   9.796  1.00 31.55           C  
-ANISOU 6192  C   ASP D 176     4137   3141   4710   -519    674   -223       C  
-ATOM   6193  O   ASP D 176     -17.651 -17.156  10.902  1.00 30.86           O  
-ANISOU 6193  O   ASP D 176     4157   2976   4591   -483    688   -159       O  
-ATOM   6194  CB  ASP D 176     -18.287 -18.778   8.176  1.00 30.19           C  
-ANISOU 6194  CB  ASP D 176     4204   2795   4472   -610    740   -312       C  
-ATOM   6195  CG  ASP D 176     -19.203 -19.719   7.442  1.00 35.94           C  
-ANISOU 6195  CG  ASP D 176     5043   3463   5151   -795    782   -404       C  
-ATOM   6196  OD1 ASP D 176     -19.575 -20.744   8.038  1.00 36.61           O  
-ANISOU 6196  OD1 ASP D 176     5312   3411   5187   -909    856   -413       O  
-ATOM   6197  OD2 ASP D 176     -19.568 -19.421   6.284  1.00 30.96           O  
-ANISOU 6197  OD2 ASP D 176     4327   2919   4517   -842    736   -466       O  
-ATOM   6198  N   PHE D 177     -17.819 -15.743   9.160  1.00 25.92           N  
-ANISOU 6198  N   PHE D 177     3254   2550   4045   -438    607   -221       N  
-ATOM   6199  CA  PHE D 177     -16.926 -14.747   9.738  1.00 25.05           C  
-ANISOU 6199  CA  PHE D 177     3068   2490   3960   -318    551   -151       C  
-ATOM   6200  C   PHE D 177     -17.630 -13.396   9.695  1.00 29.51           C  
-ANISOU 6200  C   PHE D 177     3463   3187   4565   -347    522   -180       C  
-ATOM   6201  O   PHE D 177     -18.157 -13.016   8.647  1.00 28.89           O  
-ANISOU 6201  O   PHE D 177     3283   3183   4511   -366    500   -226       O  
-ATOM   6202  CB  PHE D 177     -15.628 -14.695   8.928  1.00 25.79           C  
-ANISOU 6202  CB  PHE D 177     3144   2581   4076   -173    511   -107       C  
-ATOM   6203  CG  PHE D 177     -14.948 -16.034   8.785  1.00 28.11           C  
-ANISOU 6203  CG  PHE D 177     3600   2738   4343   -107    556    -81       C  
-ATOM   6204  CD1 PHE D 177     -14.245 -16.584   9.857  1.00 27.20           C  
-ANISOU 6204  CD1 PHE D 177     3589   2536   4209    -36    550      0       C  
-ATOM   6205  CD2 PHE D 177     -15.031 -16.750   7.600  1.00 26.34           C  
-ANISOU 6205  CD2 PHE D 177     3447   2461   4100   -112    605   -136       C  
-ATOM   6206  CE1 PHE D 177     -13.631 -17.815   9.746  1.00 28.69           C  
-ANISOU 6206  CE1 PHE D 177     3939   2584   4379     54    596     34       C  
-ATOM   6207  CE2 PHE D 177     -14.410 -17.983   7.476  1.00 30.13           C  
-ANISOU 6207  CE2 PHE D 177     4105   2788   4553    -33    667   -117       C  
-ATOM   6208  CZ  PHE D 177     -13.709 -18.516   8.558  1.00 29.20           C  
-ANISOU 6208  CZ  PHE D 177     4080   2581   4435     62    665    -28       C  
-ATOM   6209  N   VAL D 178     -17.645 -12.669  10.814  1.00 24.12           N  
-ANISOU 6209  N   VAL D 178     2766   2522   3876   -345    521   -153       N  
-ATOM   6210  CA  VAL D 178     -18.398 -11.422  10.894  1.00 25.77           C  
-ANISOU 6210  CA  VAL D 178     2845   2828   4120   -358    521   -184       C  
-ATOM   6211  C   VAL D 178     -17.541 -10.331  11.491  1.00 25.88           C  
-ANISOU 6211  C   VAL D 178     2854   2853   4128   -284    469   -134       C  
-ATOM   6212  O   VAL D 178     -17.002 -10.509  12.582  1.00 25.87           O  
-ANISOU 6212  O   VAL D 178     2959   2796   4075   -288    465    -92       O  
-ATOM   6213  CB  VAL D 178     -19.605 -11.575  11.833  1.00 29.45           C  
-ANISOU 6213  CB  VAL D 178     3321   3295   4573   -465    615   -225       C  
-ATOM   6214  CG1 VAL D 178     -20.422 -10.296  11.852  1.00 28.92           C  
-ANISOU 6214  CG1 VAL D 178     3109   3323   4556   -445    633   -258       C  
-ATOM   6215  CG2 VAL D 178     -20.461 -12.730  11.422  1.00 38.01           C  
-ANISOU 6215  CG2 VAL D 178     4422   4363   5656   -583    669   -273       C  
-ATOM   6216  N   GLY D 179     -17.434  -9.191  10.817  1.00 22.96           N  
-ANISOU 6216  N   GLY D 179     2379   2548   3796   -230    424   -136       N  
-ATOM   6217  CA  GLY D 179     -16.699  -8.080  11.385  1.00 23.47           C  
-ANISOU 6217  CA  GLY D 179     2456   2614   3849   -192    379    -98       C  
-ATOM   6218  C   GLY D 179     -17.466  -7.448  12.533  1.00 28.13           C  
-ANISOU 6218  C   GLY D 179     3090   3189   4410   -233    440   -128       C  
-ATOM   6219  O   GLY D 179     -17.025  -7.497  13.690  1.00 24.79           O  
-ANISOU 6219  O   GLY D 179     2783   2715   3920   -264    439   -103       O  
-ATOM   6220  N   PHE D 180     -18.628  -6.870  12.207  1.00 24.50           N  
-ANISOU 6220  N   PHE D 180     2539   2775   3996   -226    496   -180       N  
-ATOM   6221  CA  PHE D 180     -19.420  -6.105  13.157  1.00 24.05           C  
-ANISOU 6221  CA  PHE D 180     2506   2706   3926   -234    583   -215       C  
-ATOM   6222  C   PHE D 180     -20.892  -6.468  13.048  1.00 28.53           C  
-ANISOU 6222  C   PHE D 180     2964   3331   4547   -263    682   -270       C  
-ATOM   6223  O   PHE D 180     -21.405  -6.695  11.949  1.00 30.33           O  
-ANISOU 6223  O   PHE D 180     3058   3630   4836   -252    648   -283       O  
-ATOM   6224  CB  PHE D 180     -19.230  -4.604  12.895  1.00 23.77           C  
-ANISOU 6224  CB  PHE D 180     2454   2669   3909   -157    552   -211       C  
-ATOM   6225  CG  PHE D 180     -17.805  -4.156  12.993  1.00 23.06           C  
-ANISOU 6225  CG  PHE D 180     2451   2538   3773   -160    455   -159       C  
-ATOM   6226  CD1 PHE D 180     -16.921  -4.337  11.934  1.00 22.39           C  
-ANISOU 6226  CD1 PHE D 180     2306   2486   3716   -136    364   -115       C  
-ATOM   6227  CD2 PHE D 180     -17.338  -3.562  14.166  1.00 24.14           C  
-ANISOU 6227  CD2 PHE D 180     2730   2610   3831   -201    458   -154       C  
-ATOM   6228  CE1 PHE D 180     -15.595  -3.935  12.044  1.00 22.91           C  
-ANISOU 6228  CE1 PHE D 180     2416   2537   3754   -151    282    -62       C  
-ATOM   6229  CE2 PHE D 180     -16.023  -3.160  14.290  1.00 23.37           C  
-ANISOU 6229  CE2 PHE D 180     2692   2495   3693   -231    351   -104       C  
-ATOM   6230  CZ  PHE D 180     -15.144  -3.336  13.231  1.00 24.21           C  
-ANISOU 6230  CZ  PHE D 180     2700   2650   3848   -206    265    -54       C  
-ATOM   6231  N   GLU D 181     -21.571  -6.544  14.186  1.00 26.98           N  
-ANISOU 6231  N   GLU D 181     2823   3110   4318   -313    805   -302       N  
-ATOM   6232  CA  GLU D 181     -23.013  -6.727  14.169  1.00 27.52           C  
-ANISOU 6232  CA  GLU D 181     2751   3254   4452   -343    919   -353       C  
-ATOM   6233  C   GLU D 181     -23.650  -5.389  14.527  1.00 32.04           C  
-ANISOU 6233  C   GLU D 181     3271   3840   5062   -243   1002   -380       C  
-ATOM   6234  O   GLU D 181     -23.386  -4.825  15.595  1.00 32.32           O  
-ANISOU 6234  O   GLU D 181     3461   3794   5023   -236   1074   -388       O  
-ATOM   6235  CB  GLU D 181     -23.447  -7.816  15.150  1.00 29.13           C  
-ANISOU 6235  CB  GLU D 181     3045   3424   4600   -475   1037   -371       C  
-ATOM   6236  CG  GLU D 181     -24.912  -8.225  14.986  1.00 30.83           C  
-ANISOU 6236  CG  GLU D 181     3079   3740   4896   -546   1151   -421       C  
-ATOM   6237  CD  GLU D 181     -25.436  -8.944  16.193  1.00 39.17           C  
-ANISOU 6237  CD  GLU D 181     4240   4753   5888   -675   1317   -442       C  
-ATOM   6238  OE1 GLU D 181     -25.675  -8.265  17.209  1.00 40.98           O  
-ANISOU 6238  OE1 GLU D 181     4541   4953   6078   -646   1442   -460       O  
-ATOM   6239  OE2 GLU D 181     -25.605 -10.177  16.125  1.00 42.52           O  
-ANISOU 6239  OE2 GLU D 181     4702   5162   6291   -812   1332   -443       O  
-ATOM   6240  N   ILE D 182     -24.482  -4.871  13.630  1.00 32.28           N  
-ANISOU 6240  N   ILE D 182     3100   3967   5198   -161    989   -391       N  
-ATOM   6241  CA  ILE D 182     -24.952  -3.494  13.744  1.00 30.63           C  
-ANISOU 6241  CA  ILE D 182     2849   3754   5036    -18   1046   -402       C  
-ATOM   6242  C   ILE D 182     -26.466  -3.405  13.856  1.00 33.43           C  
-ANISOU 6242  C   ILE D 182     2992   4214   5494     22   1180   -440       C  
-ATOM   6243  O   ILE D 182     -27.176  -4.343  13.484  1.00 34.28           O  
-ANISOU 6243  O   ILE D 182     2938   4431   5655    -71   1182   -452       O  
-ATOM   6244  CB  ILE D 182     -24.462  -2.652  12.538  1.00 31.17           C  
-ANISOU 6244  CB  ILE D 182     2876   3827   5138     96    896   -359       C  
-ATOM   6245  CG1 ILE D 182     -24.972  -3.235  11.218  1.00 37.42           C  
-ANISOU 6245  CG1 ILE D 182     3470   4745   6002     87    790   -345       C  
-ATOM   6246  CG2 ILE D 182     -22.946  -2.567  12.523  1.00 30.13           C  
-ANISOU 6246  CG2 ILE D 182     2933   3600   4916     59    792   -321       C  
-ATOM   6247  CD1 ILE D 182     -24.776  -2.291  10.023  1.00 35.27           C  
-ANISOU 6247  CD1 ILE D 182     3152   4489   5761    214    663   -299       C  
-ATOM   6248  N   PRO D 183     -26.971  -2.271  14.373  1.00 31.59           N  
-ANISOU 6248  N   PRO D 183     2760   3950   5291    157   1300   -459       N  
-ATOM   6249  CA  PRO D 183     -28.418  -2.043  14.433  1.00 33.69           C  
-ANISOU 6249  CA  PRO D 183     2787   4333   5682    238   1437   -487       C  
-ATOM   6250  C   PRO D 183     -29.013  -1.917  13.029  1.00 36.12           C  
-ANISOU 6250  C   PRO D 183     2826   4784   6112    324   1291   -448       C  
-ATOM   6251  O   PRO D 183     -28.271  -1.835  12.053  1.00 36.11           O  
-ANISOU 6251  O   PRO D 183     2870   4766   6084    337   1104   -405       O  
-ATOM   6252  CB  PRO D 183     -28.528  -0.689  15.142  1.00 41.54           C  
-ANISOU 6252  CB  PRO D 183     3899   5218   6666    407   1573   -507       C  
-ATOM   6253  CG  PRO D 183     -27.213  -0.481  15.830  1.00 39.00           C  
-ANISOU 6253  CG  PRO D 183     3912   4722   6184    335   1541   -509       C  
-ATOM   6254  CD  PRO D 183     -26.203  -1.166  14.983  1.00 33.65           C  
-ANISOU 6254  CD  PRO D 183     3257   4058   5469    235   1324   -460       C  
-ATOM   6255  N   ASP D 184     -30.336  -1.881  12.940  1.00 38.25           N  
-ANISOU 6255  N   ASP D 184     2819   5202   6512    382   1375   -460       N  
-ATOM   6256  CA  ASP D 184     -31.018  -1.684  11.665  1.00 45.49           C  
-ANISOU 6256  CA  ASP D 184     3465   6275   7546    475   1223   -416       C  
-ATOM   6257  C   ASP D 184     -31.014  -0.198  11.305  1.00 43.91           C  
-ANISOU 6257  C   ASP D 184     3284   6013   7389    740   1193   -372       C  
-ATOM   6258  O   ASP D 184     -32.053   0.463  11.349  1.00 44.21           O  
-ANISOU 6258  O   ASP D 184     3116   6131   7549    916   1279   -362       O  
-ATOM   6259  CB  ASP D 184     -32.452  -2.219  11.739  1.00 49.25           C  
-ANISOU 6259  CB  ASP D 184     3603   6954   8155    428   1314   -437       C  
-ATOM   6260  CG  ASP D 184     -33.134  -2.283  10.377  1.00 58.20           C  
-ANISOU 6260  CG  ASP D 184     4446   8278   9390    464   1109   -388       C  
-ATOM   6261  OD1 ASP D 184     -32.463  -2.056   9.347  1.00 60.50           O  
-ANISOU 6261  OD1 ASP D 184     4826   8533   9626    503    900   -341       O  
-ATOM   6262  OD2 ASP D 184     -34.349  -2.575  10.343  1.00 65.52           O  
-ANISOU 6262  OD2 ASP D 184     5102   9397  10395    437   1137   -381       O  
-ATOM   6263  N   LYS D 185     -29.826   0.311  10.983  1.00 37.82           N  
-ANISOU 6263  N   LYS D 185     2765   5090   6514    765   1083   -343       N  
-ATOM   6264  CA  LYS D 185     -29.625   1.691  10.544  1.00 43.85           C  
-ANISOU 6264  CA  LYS D 185     3613   5758   7290    984   1036   -295       C  
-ATOM   6265  C   LYS D 185     -28.976   1.639   9.165  1.00 40.90           C  
-ANISOU 6265  C   LYS D 185     3259   5405   6877    963    795   -231       C  
-ATOM   6266  O   LYS D 185     -28.251   0.692   8.866  1.00 35.92           O  
-ANISOU 6266  O   LYS D 185     2694   4786   6169    779    705   -239       O  
-ATOM   6267  CB  LYS D 185     -28.666   2.419  11.491  1.00 47.34           C  
-ANISOU 6267  CB  LYS D 185     4388   5979   7621    993   1140   -323       C  
-ATOM   6268  CG  LYS D 185     -29.219   2.767  12.863  1.00 55.01           C  
-ANISOU 6268  CG  LYS D 185     5420   6884   8598   1045   1394   -388       C  
-ATOM   6269  CD  LYS D 185     -28.143   3.475  13.697  1.00 54.16           C  
-ANISOU 6269  CD  LYS D 185     5681   6550   8346   1016   1452   -416       C  
-ATOM   6270  CE  LYS D 185     -28.741   4.196  14.903  1.00 58.48           C  
-ANISOU 6270  CE  LYS D 185     6338   6994   8888   1126   1709   -480       C  
-ATOM   6271  NZ  LYS D 185     -28.314   3.592  16.198  1.00 58.66           N  
-ANISOU 6271  NZ  LYS D 185     6562   6949   8777    937   1832   -545       N  
-ATOM   6272  N   PHE D 186     -29.217   2.643   8.323  1.00 40.56           N  
-ANISOU 6272  N   PHE D 186     3180   5356   6876   1157    701   -165       N  
-ATOM   6273  CA  PHE D 186     -28.575   2.648   7.011  1.00 38.57           C  
-ANISOU 6273  CA  PHE D 186     2981   5110   6562   1132    487   -102       C  
-ATOM   6274  C   PHE D 186     -27.183   3.252   7.107  1.00 34.03           C  
-ANISOU 6274  C   PHE D 186     2723   4337   5868   1102    480    -90       C  
-ATOM   6275  O   PHE D 186     -27.025   4.400   7.528  1.00 39.59           O  
-ANISOU 6275  O   PHE D 186     3583   4894   6565   1235    559    -78       O  
-ATOM   6276  CB  PHE D 186     -29.404   3.389   5.951  1.00 42.34           C  
-ANISOU 6276  CB  PHE D 186     3297   5675   7117   1336    359    -19       C  
-ATOM   6277  CG  PHE D 186     -28.998   3.043   4.542  1.00 42.90           C  
-ANISOU 6277  CG  PHE D 186     3377   5810   7115   1265    134     37       C  
-ATOM   6278  CD1 PHE D 186     -27.914   3.670   3.943  1.00 40.52           C  
-ANISOU 6278  CD1 PHE D 186     3328   5364   6705   1277     61     85       C  
-ATOM   6279  CD2 PHE D 186     -29.684   2.064   3.830  1.00 46.16           C  
-ANISOU 6279  CD2 PHE D 186     3560   6424   7555   1161      6     37       C  
-ATOM   6280  CE1 PHE D 186     -27.517   3.332   2.646  1.00 39.75           C  
-ANISOU 6280  CE1 PHE D 186     3261   5318   6523   1204   -121    133       C  
-ATOM   6281  CE2 PHE D 186     -29.303   1.721   2.544  1.00 46.86           C  
-ANISOU 6281  CE2 PHE D 186     3695   6560   7552   1083   -190     78       C  
-ATOM   6282  CZ  PHE D 186     -28.212   2.356   1.947  1.00 43.24           C  
-ANISOU 6282  CZ  PHE D 186     3497   5953   6980   1113   -246    127       C  
-ATOM   6283  N   VAL D 187     -26.178   2.477   6.713  1.00 31.39           N  
-ANISOU 6283  N   VAL D 187     2484   3999   5444    925    393    -92       N  
-ATOM   6284  CA  VAL D 187     -24.789   2.925   6.807  1.00 30.77           C  
-ANISOU 6284  CA  VAL D 187     2665   3765   5263    865    383    -79       C  
-ATOM   6285  C   VAL D 187     -24.122   2.990   5.444  1.00 35.07           C  
-ANISOU 6285  C   VAL D 187     3259   4319   5748    845    227    -15       C  
-ATOM   6286  O   VAL D 187     -24.526   2.303   4.514  1.00 32.45           O  
-ANISOU 6286  O   VAL D 187     2791   4114   5423    816    121      0       O  
-ATOM   6287  CB  VAL D 187     -23.969   2.025   7.750  1.00 30.90           C  
-ANISOU 6287  CB  VAL D 187     2775   3746   5218    682    448   -134       C  
-ATOM   6288  CG1 VAL D 187     -24.538   2.096   9.160  1.00 33.61           C  
-ANISOU 6288  CG1 VAL D 187     3131   4053   5587    695    617   -194       C  
-ATOM   6289  CG2 VAL D 187     -23.971   0.584   7.248  1.00 31.00           C  
-ANISOU 6289  CG2 VAL D 187     2671   3882   5225    545    379   -149       C  
-ATOM   6290  N   VAL D 188     -23.095   3.820   5.329  1.00 32.17           N  
-ANISOU 6290  N   VAL D 188     3098   3813   5311    844    219     19       N  
-ATOM   6291  CA  VAL D 188     -22.363   3.963   4.075  1.00 28.37           C  
-ANISOU 6291  CA  VAL D 188     2691   3327   4761    815    102     82       C  
-ATOM   6292  C   VAL D 188     -20.890   4.098   4.410  1.00 28.11           C  
-ANISOU 6292  C   VAL D 188     2840   3188   4653    684    134     80       C  
-ATOM   6293  O   VAL D 188     -20.538   4.200   5.584  1.00 27.00           O  
-ANISOU 6293  O   VAL D 188     2774   2976   4510    632    222     38       O  
-ATOM   6294  CB  VAL D 188     -22.822   5.226   3.295  1.00 29.94           C  
-ANISOU 6294  CB  VAL D 188     2946   3466   4963    991     46    160       C  
-ATOM   6295  CG1 VAL D 188     -24.262   5.093   2.818  1.00 31.53           C  
-ANISOU 6295  CG1 VAL D 188     2930   3804   5246   1132    -22    180       C  
-ATOM   6296  CG2 VAL D 188     -22.657   6.485   4.161  1.00 30.68           C  
-ANISOU 6296  CG2 VAL D 188     3220   3377   5060   1076    154    159       C  
-ATOM   6297  N   GLY D 189     -20.033   4.094   3.391  1.00 27.24           N  
-ANISOU 6297  N   GLY D 189     2797   3076   4477    624     64    129       N  
-ATOM   6298  CA  GLY D 189     -18.599   4.229   3.598  1.00 26.42           C  
-ANISOU 6298  CA  GLY D 189     2823   2899   4315    496     90    138       C  
-ATOM   6299  C   GLY D 189     -17.877   2.894   3.530  1.00 25.21           C  
-ANISOU 6299  C   GLY D 189     2596   2835   4147    372     84    112       C  
-ATOM   6300  O   GLY D 189     -18.519   1.842   3.614  1.00 26.70           O  
-ANISOU 6300  O   GLY D 189     2663   3115   4367    368     78     71       O  
-ATOM   6301  N   TYR D 190     -16.553   2.932   3.397  1.00 27.77           N  
-ANISOU 6301  N   TYR D 190     2991   3132   4429    271     92    139       N  
-ATOM   6302  CA  TYR D 190     -15.752   1.711   3.233  1.00 28.09           C  
-ANISOU 6302  CA  TYR D 190     2965   3247   4462    185     95    127       C  
-ATOM   6303  C   TYR D 190     -16.352   0.850   2.118  1.00 27.05           C  
-ANISOU 6303  C   TYR D 190     2764   3201   4313    217     57    118       C  
-ATOM   6304  O   TYR D 190     -16.522  -0.366   2.265  1.00 25.72           O  
-ANISOU 6304  O   TYR D 190     2524   3090   4158    187     65     75       O  
-ATOM   6305  CB  TYR D 190     -15.676   0.936   4.548  1.00 22.66           C  
-ANISOU 6305  CB  TYR D 190     2234   2569   3807    138    129     79       C  
-ATOM   6306  CG  TYR D 190     -14.580  -0.114   4.591  1.00 23.68           C  
-ANISOU 6306  CG  TYR D 190     2324   2742   3930     65    136     85       C  
-ATOM   6307  CD1 TYR D 190     -13.238   0.255   4.576  1.00 28.32           C  
-ANISOU 6307  CD1 TYR D 190     2936   3319   4504     -2    137    130       C  
-ATOM   6308  CD2 TYR D 190     -14.885  -1.467   4.652  1.00 22.03           C  
-ANISOU 6308  CD2 TYR D 190     2052   2583   3735     64    146     50       C  
-ATOM   6309  CE1 TYR D 190     -12.225  -0.703   4.621  1.00 27.89           C  
-ANISOU 6309  CE1 TYR D 190     2819   3316   4463    -38    147    146       C  
-ATOM   6310  CE2 TYR D 190     -13.880  -2.429   4.711  1.00 21.92           C  
-ANISOU 6310  CE2 TYR D 190     2016   2592   3721     30    162     62       C  
-ATOM   6311  CZ  TYR D 190     -12.557  -2.042   4.692  1.00 25.72           C  
-ANISOU 6311  CZ  TYR D 190     2497   3074   4202     -6    161    113       C  
-ATOM   6312  OH  TYR D 190     -11.542  -2.987   4.749  1.00 25.65           O  
-ANISOU 6312  OH  TYR D 190     2438   3097   4209    -11    179    136       O  
-ATOM   6313  N   ALA D 191     -16.674   1.519   1.005  1.00 25.56           N  
-ANISOU 6313  N   ALA D 191     2622   3008   4080    271      9    162       N  
-ATOM   6314  CA  ALA D 191     -17.222   0.915  -0.222  1.00 24.51           C  
-ANISOU 6314  CA  ALA D 191     2463   2952   3899    289    -52    163       C  
-ATOM   6315  C   ALA D 191     -18.721   0.660  -0.214  1.00 25.99           C  
-ANISOU 6315  C   ALA D 191     2541   3208   4124    355   -120    135       C  
-ATOM   6316  O   ALA D 191     -19.304   0.439  -1.266  1.00 29.13           O  
-ANISOU 6316  O   ALA D 191     2926   3671   4473    371   -204    148       O  
-ATOM   6317  CB  ALA D 191     -16.428  -0.352  -0.661  1.00 23.96           C  
-ANISOU 6317  CB  ALA D 191     2387   2926   3791    205    -15    134       C  
-ATOM   6318  N   LEU D 192     -19.357   0.715   0.954  1.00 26.27           N  
-ANISOU 6318  N   LEU D 192     2499   3239   4244    385    -83     99       N  
-ATOM   6319  CA  LEU D 192     -20.824   0.673   0.992  1.00 26.06           C  
-ANISOU 6319  CA  LEU D 192     2338   3291   4274    460   -133     83       C  
-ATOM   6320  C   LEU D 192     -21.441   1.992   0.503  1.00 31.93           C  
-ANISOU 6320  C   LEU D 192     3103   4007   5024    608   -193    151       C  
-ATOM   6321  O   LEU D 192     -20.973   3.081   0.870  1.00 29.98           O  
-ANISOU 6321  O   LEU D 192     2976   3640   4774    662   -145    185       O  
-ATOM   6322  CB  LEU D 192     -21.343   0.343   2.388  1.00 27.85           C  
-ANISOU 6322  CB  LEU D 192     2477   3520   4584    451    -46     25       C  
-ATOM   6323  CG  LEU D 192     -21.181  -1.112   2.842  1.00 32.39           C  
-ANISOU 6323  CG  LEU D 192     3009   4139   5160    322     -5    -37       C  
-ATOM   6324  CD1 LEU D 192     -19.792  -1.359   3.380  1.00 31.99           C  
-ANISOU 6324  CD1 LEU D 192     3077   4006   5073    251     55    -38       C  
-ATOM   6325  CD2 LEU D 192     -22.233  -1.495   3.883  1.00 34.71           C  
-ANISOU 6325  CD2 LEU D 192     3181   4476   5530    316     59    -89       C  
-ATOM   6326  N   ASP D 193     -22.507   1.898  -0.294  1.00 28.72           N  
-ANISOU 6326  N   ASP D 193     2585   3704   4622    670   -305    173       N  
-ATOM   6327  CA  ASP D 193     -23.041   3.077  -0.974  1.00 30.29           C  
-ANISOU 6327  CA  ASP D 193     2817   3880   4811    829   -390    259       C  
-ATOM   6328  C   ASP D 193     -24.474   3.454  -0.623  1.00 33.28           C  
-ANISOU 6328  C   ASP D 193     3009   4335   5303    984   -423    271       C  
-ATOM   6329  O   ASP D 193     -25.230   2.681  -0.038  1.00 34.08           O  
-ANISOU 6329  O   ASP D 193     2919   4543   5485    946   -397    210       O  
-ATOM   6330  CB  ASP D 193     -22.983   2.905  -2.491  1.00 31.01           C  
-ANISOU 6330  CB  ASP D 193     2968   4030   4786    802   -531    312       C  
-ATOM   6331  CG  ASP D 193     -24.043   1.952  -3.002  1.00 33.15           C  
-ANISOU 6331  CG  ASP D 193     3056   4474   5064    762   -653    284       C  
-ATOM   6332  OD1 ASP D 193     -24.086   0.813  -2.504  1.00 33.85           O  
-ANISOU 6332  OD1 ASP D 193     3054   4622   5184    633   -602    199       O  
-ATOM   6333  OD2 ASP D 193     -24.837   2.338  -3.890  1.00 35.68           O  
-ANISOU 6333  OD2 ASP D 193     3330   4872   5356    851   -808    351       O  
-ATOM   6334  N   TYR D 194     -24.825   4.670  -1.012  1.00 33.46           N  
-ANISOU 6334  N   TYR D 194     3091   4294   5329   1163   -473    356       N  
-ATOM   6335  CA  TYR D 194     -26.202   5.093  -1.116  1.00 35.68           C  
-ANISOU 6335  CA  TYR D 194     3182   4670   5705   1350   -550    401       C  
-ATOM   6336  C   TYR D 194     -26.296   5.666  -2.515  1.00 38.78           C  
-ANISOU 6336  C   TYR D 194     3664   5069   6001   1437   -728    512       C  
-ATOM   6337  O   TYR D 194     -25.660   6.678  -2.804  1.00 39.47           O  
-ANISOU 6337  O   TYR D 194     3985   4993   6020   1509   -711    579       O  
-ATOM   6338  CB  TYR D 194     -26.503   6.163  -0.074  1.00 36.46           C  
-ANISOU 6338  CB  TYR D 194     3310   4641   5902   1530   -412    405       C  
-ATOM   6339  CG  TYR D 194     -27.865   6.790  -0.205  1.00 39.16           C  
-ANISOU 6339  CG  TYR D 194     3463   5060   6355   1778   -472    469       C  
-ATOM   6340  CD1 TYR D 194     -29.008   6.089   0.146  1.00 44.10           C  
-ANISOU 6340  CD1 TYR D 194     3769   5883   7105   1794   -478    430       C  
-ATOM   6341  CD2 TYR D 194     -28.003   8.091  -0.649  1.00 40.89           C  
-ANISOU 6341  CD2 TYR D 194     3821   5153   6563   2001   -514    573       C  
-ATOM   6342  CE1 TYR D 194     -30.256   6.667   0.038  1.00 47.94           C  
-ANISOU 6342  CE1 TYR D 194     4039   6462   7712   2035   -530    495       C  
-ATOM   6343  CE2 TYR D 194     -29.243   8.680  -0.760  1.00 49.88           C  
-ANISOU 6343  CE2 TYR D 194     4774   6362   7815   2264   -569    643       C  
-ATOM   6344  CZ  TYR D 194     -30.367   7.963  -0.413  1.00 51.60           C  
-ANISOU 6344  CZ  TYR D 194     4636   6801   8170   2285   -578    605       C  
-ATOM   6345  OH  TYR D 194     -31.608   8.550  -0.522  1.00 58.57           O  
-ANISOU 6345  OH  TYR D 194     5293   7777   9186   2560   -632    682       O  
-ATOM   6346  N   ASN D 195     -27.062   5.005  -3.380  1.00 38.31           N  
-ANISOU 6346  N   ASN D 195     3441   5195   5922   1409   -901    531       N  
-ATOM   6347  CA  ASN D 195     -27.146   5.374  -4.793  1.00 39.82           C  
-ANISOU 6347  CA  ASN D 195     3732   5411   5986   1458  -1096    635       C  
-ATOM   6348  C   ASN D 195     -25.790   5.644  -5.448  1.00 38.59           C  
-ANISOU 6348  C   ASN D 195     3899   5101   5661   1357  -1062    662       C  
-ATOM   6349  O   ASN D 195     -25.621   6.650  -6.149  1.00 39.86           O  
-ANISOU 6349  O   ASN D 195     4245   5161   5739   1472  -1125    770       O  
-ATOM   6350  CB  ASN D 195     -28.086   6.565  -4.993  1.00 53.04           C  
-ANISOU 6350  CB  ASN D 195     5346   7077   7728   1743  -1191    754       C  
-ATOM   6351  CG  ASN D 195     -29.505   6.247  -4.598  1.00 60.79           C  
-ANISOU 6351  CG  ASN D 195     5963   8260   8875   1846  -1253    745       C  
-ATOM   6352  OD1 ASN D 195     -29.982   5.140  -4.829  1.00 62.94           O  
-ANISOU 6352  OD1 ASN D 195     6037   8726   9152   1688  -1344    690       O  
-ATOM   6353  ND2 ASN D 195     -30.189   7.213  -3.988  1.00 63.15           N  
-ANISOU 6353  ND2 ASN D 195     6171   8510   9312   2107  -1191    795       N  
-ATOM   6354  N   GLU D 196     -24.841   4.746  -5.185  1.00 37.03           N  
-ANISOU 6354  N   GLU D 196     3763   4887   5421   1148   -950    569       N  
-ATOM   6355  CA  GLU D 196     -23.493   4.765  -5.772  1.00 35.25           C  
-ANISOU 6355  CA  GLU D 196     3793   4551   5051   1023   -890    578       C  
-ATOM   6356  C   GLU D 196     -22.545   5.771  -5.110  1.00 36.49           C  
-ANISOU 6356  C   GLU D 196     4126   4512   5225   1053   -737    599       C  
-ATOM   6357  O   GLU D 196     -21.336   5.744  -5.345  1.00 34.96           O  
-ANISOU 6357  O   GLU D 196     4100   4239   4946    927   -651    594       O  
-ATOM   6358  CB  GLU D 196     -23.543   4.950  -7.295  1.00 37.82           C  
-ANISOU 6358  CB  GLU D 196     4260   4904   5205   1026  -1051    665       C  
-ATOM   6359  CG  GLU D 196     -24.234   3.792  -8.023  1.00 37.58           C  
-ANISOU 6359  CG  GLU D 196     4105   5060   5115    925  -1202    625       C  
-ATOM   6360  CD  GLU D 196     -23.543   2.463  -7.782  1.00 38.66           C  
-ANISOU 6360  CD  GLU D 196     4236   5222   5230    716  -1089    502       C  
-ATOM   6361  OE1 GLU D 196     -22.325   2.465  -7.552  1.00 37.10           O  
-ANISOU 6361  OE1 GLU D 196     4184   4909   5003    645   -929    477       O  
-ATOM   6362  OE2 GLU D 196     -24.217   1.416  -7.828  1.00 47.68           O  
-ANISOU 6362  OE2 GLU D 196     5230   6499   6387    623  -1162    435       O  
-ATOM   6363  N   TYR D 197     -23.095   6.638  -4.267  1.00 35.09           N  
-ANISOU 6363  N   TYR D 197     3908   4264   5161   1211   -694    617       N  
-ATOM   6364  CA  TYR D 197     -22.282   7.595  -3.534  1.00 34.56           C  
-ANISOU 6364  CA  TYR D 197     4022   4003   5107   1220   -551    624       C  
-ATOM   6365  C   TYR D 197     -21.771   7.037  -2.206  1.00 32.70           C  
-ANISOU 6365  C   TYR D 197     3718   3755   4952   1103   -403    515       C  
-ATOM   6366  O   TYR D 197     -22.272   6.021  -1.722  1.00 32.04           O  
-ANISOU 6366  O   TYR D 197     3436   3800   4938   1060   -399    441       O  
-ATOM   6367  CB  TYR D 197     -23.073   8.871  -3.298  1.00 36.52           C  
-ANISOU 6367  CB  TYR D 197     4318   4142   5414   1456   -563    697       C  
-ATOM   6368  CG  TYR D 197     -23.252   9.676  -4.553  1.00 47.33           C  
-ANISOU 6368  CG  TYR D 197     5848   5459   6678   1570   -695    828       C  
-ATOM   6369  CD1 TYR D 197     -22.315  10.629  -4.921  1.00 48.27           C  
-ANISOU 6369  CD1 TYR D 197     6268   5383   6689   1534   -642    894       C  
-ATOM   6370  CD2 TYR D 197     -24.351   9.477  -5.380  1.00 51.73           C  
-ANISOU 6370  CD2 TYR D 197     6260   6165   7232   1699   -881    892       C  
-ATOM   6371  CE1 TYR D 197     -22.470  11.371  -6.073  1.00 54.19           C  
-ANISOU 6371  CE1 TYR D 197     7198   6069   7323   1635   -757   1024       C  
-ATOM   6372  CE2 TYR D 197     -24.514  10.213  -6.538  1.00 55.10           C  
-ANISOU 6372  CE2 TYR D 197     6853   6541   7542   1808  -1020   1025       C  
-ATOM   6373  CZ  TYR D 197     -23.571  11.158  -6.878  1.00 56.75           C  
-ANISOU 6373  CZ  TYR D 197     7388   6537   7636   1780   -951   1092       C  
-ATOM   6374  OH  TYR D 197     -23.727  11.895  -8.029  1.00 60.78           O  
-ANISOU 6374  OH  TYR D 197     8097   6984   8015   1885  -1084   1233       O  
-ATOM   6375  N   PHE D 198     -20.765   7.707  -1.644  1.00 32.08           N  
-ANISOU 6375  N   PHE D 198     3818   3520   4852   1037   -291    512       N  
-ATOM   6376  CA  PHE D 198     -20.170   7.360  -0.345  1.00 30.63           C  
-ANISOU 6376  CA  PHE D 198     3611   3305   4723    924   -167    424       C  
-ATOM   6377  C   PHE D 198     -19.248   6.162  -0.361  1.00 28.92           C  
-ANISOU 6377  C   PHE D 198     3334   3179   4477    735   -144    371       C  
-ATOM   6378  O   PHE D 198     -18.789   5.725   0.695  1.00 27.84           O  
-ANISOU 6378  O   PHE D 198     3160   3036   4381    646    -66    307       O  
-ATOM   6379  CB  PHE D 198     -21.236   7.185   0.746  1.00 30.91           C  
-ANISOU 6379  CB  PHE D 198     3490   3378   4875   1027   -121    363       C  
-ATOM   6380  CG  PHE D 198     -22.070   8.405   0.968  1.00 32.78           C  
-ANISOU 6380  CG  PHE D 198     3791   3506   5159   1239   -102    406       C  
-ATOM   6381  CD1 PHE D 198     -21.556   9.492   1.658  1.00 35.64           C  
-ANISOU 6381  CD1 PHE D 198     4373   3666   5502   1251      0    406       C  
-ATOM   6382  CD2 PHE D 198     -23.368   8.467   0.488  1.00 42.25           C  
-ANISOU 6382  CD2 PHE D 198     4830   4802   6421   1427   -187    448       C  
-ATOM   6383  CE1 PHE D 198     -22.325  10.634   1.869  1.00 39.76           C  
-ANISOU 6383  CE1 PHE D 198     4986   4057   6064   1468     37    444       C  
-ATOM   6384  CE2 PHE D 198     -24.146   9.598   0.688  1.00 47.82           C  
-ANISOU 6384  CE2 PHE D 198     5585   5403   7183   1660   -161    497       C  
-ATOM   6385  CZ  PHE D 198     -23.621  10.686   1.380  1.00 46.96           C  
-ANISOU 6385  CZ  PHE D 198     5726   5064   7051   1690    -38    493       C  
-ATOM   6386  N   ARG D 199     -18.969   5.605  -1.538  1.00 28.87           N  
-ANISOU 6386  N   ARG D 199     3328   3249   4392    679   -209    399       N  
-ATOM   6387  CA  ARG D 199     -18.018   4.502  -1.555  1.00 27.51           C  
-ANISOU 6387  CA  ARG D 199     3117   3141   4196    524   -162    351       C  
-ATOM   6388  C   ARG D 199     -16.607   5.007  -1.264  1.00 30.61           C  
-ANISOU 6388  C   ARG D 199     3630   3438   4560    412    -73    369       C  
-ATOM   6389  O   ARG D 199     -15.791   4.272  -0.700  1.00 27.77           O  
-ANISOU 6389  O   ARG D 199     3212   3114   4227    307    -14    326       O  
-ATOM   6390  CB  ARG D 199     -18.034   3.748  -2.878  1.00 29.54           C  
-ANISOU 6390  CB  ARG D 199     3371   3489   4362    488   -229    364       C  
-ATOM   6391  CG  ARG D 199     -19.354   3.059  -3.198  1.00 31.91           C  
-ANISOU 6391  CG  ARG D 199     3532   3910   4681    547   -336    338       C  
-ATOM   6392  CD  ARG D 199     -19.147   1.990  -4.254  1.00 28.43           C  
-ANISOU 6392  CD  ARG D 199     3107   3553   4141    454   -376    315       C  
-ATOM   6393  NE  ARG D 199     -20.384   1.641  -4.949  1.00 29.69           N  
-ANISOU 6393  NE  ARG D 199     3186   3822   4273    493   -522    318       N  
-ATOM   6394  CZ  ARG D 199     -21.224   0.695  -4.538  1.00 31.80           C  
-ANISOU 6394  CZ  ARG D 199     3288   4191   4605    459   -558    249       C  
-ATOM   6395  NH1 ARG D 199     -20.957   0.010  -3.433  1.00 30.30           N  
-ANISOU 6395  NH1 ARG D 199     3022   3989   4502    399   -448    177       N  
-ATOM   6396  NH2 ARG D 199     -22.319   0.429  -5.239  1.00 31.13           N  
-ANISOU 6396  NH2 ARG D 199     3118   4220   4490    472   -709    258       N  
-ATOM   6397  N   ASP D 200     -16.347   6.259  -1.645  1.00 28.09           N  
-ANISOU 6397  N   ASP D 200     3479   3002   4190    434    -69    439       N  
-ATOM   6398  CA  ASP D 200     -15.028   6.884  -1.518  1.00 29.69           C  
-ANISOU 6398  CA  ASP D 200     3805   3117   4358    301      8    468       C  
-ATOM   6399  C   ASP D 200     -14.860   7.536  -0.144  1.00 32.01           C  
-ANISOU 6399  C   ASP D 200     4142   3310   4710    273     57    435       C  
-ATOM   6400  O   ASP D 200     -14.601   8.733  -0.029  1.00 33.84           O  
-ANISOU 6400  O   ASP D 200     4551   3397   4910    255     83    474       O  
-ATOM   6401  CB  ASP D 200     -14.817   7.931  -2.623  1.00 29.55           C  
-ANISOU 6401  CB  ASP D 200     3986   3003   4240    310     -2    562       C  
-ATOM   6402  CG  ASP D 200     -15.955   8.941  -2.697  1.00 33.67           C  
-ANISOU 6402  CG  ASP D 200     4612   3421   4761    487    -65    609       C  
-ATOM   6403  OD1 ASP D 200     -17.111   8.536  -2.460  1.00 31.07           O  
-ANISOU 6403  OD1 ASP D 200     4149   3162   4494    625   -129    579       O  
-ATOM   6404  OD2 ASP D 200     -15.695  10.137  -2.986  1.00 32.20           O  
-ANISOU 6404  OD2 ASP D 200     4639   3080   4515    490    -45    680       O  
-ATOM   6405  N   LEU D 201     -15.025   6.731   0.895  1.00 28.78           N  
-ANISOU 6405  N   LEU D 201     3597   2966   4371    260     70    361       N  
-ATOM   6406  CA  LEU D 201     -14.994   7.197   2.278  1.00 32.31           C  
-ANISOU 6406  CA  LEU D 201     4092   3329   4856    233    112    317       C  
-ATOM   6407  C   LEU D 201     -14.443   6.031   3.060  1.00 32.42           C  
-ANISOU 6407  C   LEU D 201     3966   3445   4905    135    125    263       C  
-ATOM   6408  O   LEU D 201     -14.897   4.906   2.863  1.00 32.25           O  
-ANISOU 6408  O   LEU D 201     3804   3536   4913    176    106    235       O  
-ATOM   6409  CB  LEU D 201     -16.410   7.549   2.733  1.00 33.72           C  
-ANISOU 6409  CB  LEU D 201     4267   3464   5080    407    112    291       C  
-ATOM   6410  CG  LEU D 201     -16.702   7.848   4.196  1.00 35.44           C  
-ANISOU 6410  CG  LEU D 201     4530   3605   5332    414    177    227       C  
-ATOM   6411  CD1 LEU D 201     -15.941   9.086   4.641  1.00 32.50           C  
-ANISOU 6411  CD1 LEU D 201     4389   3056   4903    325    217    241       C  
-ATOM   6412  CD2 LEU D 201     -18.205   8.052   4.377  1.00 35.57           C  
-ANISOU 6412  CD2 LEU D 201     4490   3615   5408    617    195    210       C  
-ATOM   6413  N   ASN D 202     -13.454   6.271   3.923  1.00 30.75           N  
-ANISOU 6413  N   ASN D 202     3802   3196   4686     -1    146    254       N  
-ATOM   6414  CA AASN D 202     -12.766   5.179   4.613  0.51 30.41           C  
-ANISOU 6414  CA AASN D 202     3632   3252   4670    -89    140    224       C  
-ATOM   6415  CA BASN D 202     -12.776   5.165   4.600  0.49 30.37           C  
-ANISOU 6415  CA BASN D 202     3625   3249   4666    -87    140    224       C  
-ATOM   6416  C   ASN D 202     -13.515   4.645   5.833  1.00 29.49           C  
-ANISOU 6416  C   ASN D 202     3482   3141   4583    -47    149    159       C  
-ATOM   6417  O   ASN D 202     -13.378   3.471   6.199  1.00 29.84           O  
-ANISOU 6417  O   ASN D 202     3413   3274   4651    -64    141    137       O  
-ATOM   6418  CB AASN D 202     -11.354   5.610   5.019  0.51 33.37           C  
-ANISOU 6418  CB AASN D 202     4043   3613   5024   -262    135    253       C  
-ATOM   6419  CB BASN D 202     -11.309   5.506   4.932  0.49 33.25           C  
-ANISOU 6419  CB BASN D 202     4013   3611   5011   -261    134    256       C  
-ATOM   6420  CG AASN D 202     -10.271   4.775   4.360  0.51 37.07           C  
-ANISOU 6420  CG AASN D 202     4367   4206   5512   -326    136    292       C  
-ATOM   6421  CG BASN D 202     -11.175   6.640   5.940  0.49 32.61           C  
-ANISOU 6421  CG BASN D 202     4099   3399   4892   -348    134    238       C  
-ATOM   6422  OD1AASN D 202     -10.542   3.957   3.474  0.51 41.01           O  
-ANISOU 6422  OD1AASN D 202     4783   4778   6022   -243    152    295       O  
-ATOM   6423  OD1BASN D 202     -12.082   7.459   6.093  0.49 33.05           O  
-ANISOU 6423  OD1BASN D 202     4297   3333   4929   -262    161    218       O  
-ATOM   6424  ND2AASN D 202      -9.028   4.979   4.793  0.51 40.05           N  
-ANISOU 6424  ND2AASN D 202     4713   4612   5892   -476    122    320       N  
-ATOM   6425  ND2BASN D 202     -10.030   6.696   6.628  0.49 28.51           N  
-ANISOU 6425  ND2BASN D 202     3570   2904   4360   -518    101    248       N  
-ATOM   6426  N   HIS D 203     -14.305   5.508   6.465  1.00 27.61           N  
-ANISOU 6426  N   HIS D 203     3359   2795   4336     12    180    130       N  
-ATOM   6427  CA  HIS D 203     -15.069   5.111   7.644  1.00 27.00           C  
-ANISOU 6427  CA  HIS D 203     3272   2713   4276     49    219     65       C  
-ATOM   6428  C   HIS D 203     -16.456   4.634   7.249  1.00 29.41           C  
-ANISOU 6428  C   HIS D 203     3462   3077   4637    201    241     44       C  
-ATOM   6429  O   HIS D 203     -16.988   5.034   6.206  1.00 31.08           O  
-ANISOU 6429  O   HIS D 203     3654   3293   4864    301    218     79       O  
-ATOM   6430  CB  HIS D 203     -15.263   6.300   8.594  1.00 27.42           C  
-ANISOU 6430  CB  HIS D 203     3521   2611   4286     42    271     34       C  
-ATOM   6431  CG  HIS D 203     -14.011   7.052   8.913  1.00 27.01           C  
-ANISOU 6431  CG  HIS D 203     3614   2482   4169   -127    239     54       C  
-ATOM   6432  ND1 HIS D 203     -12.963   6.499   9.623  1.00 26.39           N  
-ANISOU 6432  ND1 HIS D 203     3502   2465   4061   -287    186     54       N  
-ATOM   6433  CD2 HIS D 203     -13.649   8.330   8.641  1.00 27.83           C  
-ANISOU 6433  CD2 HIS D 203     3897   2449   4227   -173    248     79       C  
-ATOM   6434  CE1 HIS D 203     -12.005   7.400   9.757  1.00 27.33           C  
-ANISOU 6434  CE1 HIS D 203     3749   2510   4125   -438    154     75       C  
-ATOM   6435  NE2 HIS D 203     -12.396   8.517   9.176  1.00 28.18           N  
-ANISOU 6435  NE2 HIS D 203     4000   2488   4219   -382    199     87       N  
-ATOM   6436  N   VAL D 204     -17.070   3.824   8.102  1.00 25.16           N  
-ANISOU 6436  N   VAL D 204     2853   2585   4123    210    281     -9       N  
-ATOM   6437  CA  VAL D 204     -18.497   3.538   7.962  1.00 29.15           C  
-ANISOU 6437  CA  VAL D 204     3243   3144   4688    336    318    -37       C  
-ATOM   6438  C   VAL D 204     -19.257   4.604   8.736  1.00 31.40           C  
-ANISOU 6438  C   VAL D 204     3630   3320   4982    433    408    -67       C  
-ATOM   6439  O   VAL D 204     -18.963   4.876   9.901  1.00 28.10           O  
-ANISOU 6439  O   VAL D 204     3343   2818   4516    370    471   -107       O  
-ATOM   6440  CB  VAL D 204     -18.859   2.122   8.450  1.00 27.28           C  
-ANISOU 6440  CB  VAL D 204     2884   3007   4475    286    339    -79       C  
-ATOM   6441  CG1 VAL D 204     -20.377   1.944   8.552  1.00 30.71           C  
-ANISOU 6441  CG1 VAL D 204     3192   3499   4977    387    398   -114       C  
-ATOM   6442  CG2 VAL D 204     -18.273   1.093   7.506  1.00 23.54           C  
-ANISOU 6442  CG2 VAL D 204     2324   2623   3997    228    264    -52       C  
-ATOM   6443  N   CYS D 205     -20.216   5.239   8.081  1.00 29.65           N  
-ANISOU 6443  N   CYS D 205     3361   3093   4811    593    414    -45       N  
-ATOM   6444  CA  CYS D 205     -20.871   6.383   8.681  1.00 30.16           C  
-ANISOU 6444  CA  CYS D 205     3541   3030   4887    722    512    -64       C  
-ATOM   6445  C   CYS D 205     -22.377   6.264   8.540  1.00 34.96           C  
-ANISOU 6445  C   CYS D 205     3961   3724   5597    900    559    -73       C  
-ATOM   6446  O   CYS D 205     -22.869   5.472   7.742  1.00 32.68           O  
-ANISOU 6446  O   CYS D 205     3467   3588   5359    914    481    -51       O  
-ATOM   6447  CB  CYS D 205     -20.373   7.667   8.034  1.00 31.68           C  
-ANISOU 6447  CB  CYS D 205     3916   3082   5039    767    477     -7       C  
-ATOM   6448  N   VAL D 206     -23.108   7.052   9.316  1.00 34.64           N  
-ANISOU 6448  N   VAL D 206     3988   3588   5585   1032    691   -107       N  
-ATOM   6449  CA  VAL D 206     -24.537   7.203   9.080  1.00 41.30           C  
-ANISOU 6449  CA  VAL D 206     4637   4511   6544   1242    739    -98       C  
-ATOM   6450  C   VAL D 206     -24.747   8.483   8.272  1.00 39.58           C  
-ANISOU 6450  C   VAL D 206     4513   4184   6343   1438    698    -24       C  
-ATOM   6451  O   VAL D 206     -24.123   9.509   8.545  1.00 42.07           O  
-ANISOU 6451  O   VAL D 206     5100   4297   6586   1444    741    -21       O  
-ATOM   6452  CB  VAL D 206     -25.347   7.223  10.396  1.00 45.73           C  
-ANISOU 6452  CB  VAL D 206     5185   5048   7143   1301    939   -177       C  
-ATOM   6453  CG1 VAL D 206     -25.288   5.872  11.076  1.00 42.65           C  
-ANISOU 6453  CG1 VAL D 206     4691   4778   6736   1115    972   -234       C  
-ATOM   6454  CG2 VAL D 206     -24.805   8.278  11.336  1.00 51.70           C  
-ANISOU 6454  CG2 VAL D 206     6265   5572   7806   1303   1059   -218       C  
-ATOM   6455  N   ILE D 207     -25.611   8.421   7.266  1.00 48.19           N  
-ANISOU 6455  N   ILE D 207     5392   5400   7517   1587    602     41       N  
-ATOM   6456  CA  ILE D 207     -25.821   9.555   6.358  1.00 50.11           C  
-ANISOU 6456  CA  ILE D 207     5722   5548   7767   1785    532    134       C  
-ATOM   6457  C   ILE D 207     -26.881  10.543   6.879  1.00 58.08           C  
-ANISOU 6457  C   ILE D 207     6736   6464   8868   2065    671    136       C  
-ATOM   6458  O   ILE D 207     -27.867  10.134   7.488  1.00 65.64           O  
-ANISOU 6458  O   ILE D 207     7474   7536   9929   2149    775     90       O  
-ATOM   6459  CB  ILE D 207     -26.123   9.033   4.925  1.00 67.82           C  
-ANISOU 6459  CB  ILE D 207     7769   7969  10029   1802    330    216       C  
-ATOM   6460  CG1 ILE D 207     -26.883  10.060   4.089  1.00 70.84           C  
-ANISOU 6460  CG1 ILE D 207     8146   8314  10458   2074    256    321       C  
-ATOM   6461  CG2 ILE D 207     -26.891   7.714   4.980  1.00 66.95           C  
-ANISOU 6461  CG2 ILE D 207     7337   8104   9998   1731    302    173       C  
-ATOM   6462  CD1 ILE D 207     -27.193   9.567   2.692  1.00 72.62           C  
-ANISOU 6462  CD1 ILE D 207     8203   8716  10674   2078     39    404       C  
-ATOM   6463  N   SER D 208     -26.658  11.842   6.668  1.00 55.99           N  
-ANISOU 6463  N   SER D 208     6731   5980   8564   2208    691    187       N  
-ATOM   6464  CA  SER D 208     -27.537  12.877   7.216  1.00 61.45           C  
-ANISOU 6464  CA  SER D 208     7488   6530   9329   2492    850    186       C  
-ATOM   6465  C   SER D 208     -28.819  13.042   6.406  1.00 65.54           C  
-ANISOU 6465  C   SER D 208     7725   7190   9989   2788    771    281       C  
-ATOM   6466  O   SER D 208     -28.989  12.414   5.360  1.00 65.97           O  
-ANISOU 6466  O   SER D 208     7564   7440  10061   2751    572    349       O  
-ATOM   6467  CB  SER D 208     -26.809  14.222   7.301  1.00 61.51           C  
-ANISOU 6467  CB  SER D 208     7919   6221   9233   2531    906    206       C  
-ATOM   6468  OG  SER D 208     -26.704  14.841   6.033  1.00 61.86           O  
-ANISOU 6468  OG  SER D 208     8038   6213   9254   2639    748    333       O  
-ATOM   6469  N   GLU D 209     -29.723  13.885   6.900  1.00 71.30           N  
-ANISOU 6469  N   GLU D 209     8463   7836  10792   3038    903    270       N  
-ATOM   6470  CA  GLU D 209     -30.948  14.206   6.176  1.00 72.80           C  
-ANISOU 6470  CA  GLU D 209     8405   8171  11084   3260    780    338       C  
-ATOM   6471  C   GLU D 209     -30.632  14.969   4.896  1.00 72.47           C  
-ANISOU 6471  C   GLU D 209     8522   8027  10986   3358    586    475       C  
-ATOM   6472  O   GLU D 209     -31.163  14.655   3.830  1.00 75.03           O  
-ANISOU 6472  O   GLU D 209     8614   8537  11356   3420    378    564       O  
-ATOM   6473  CB  GLU D 209     -31.911  15.009   7.059  1.00 80.02           C  
-ANISOU 6473  CB  GLU D 209     9325   9014  12067   3451    958    274       C  
-ATOM   6474  CG  GLU D 209     -32.477  14.215   8.226  1.00 82.66           C  
-ANISOU 6474  CG  GLU D 209     9455   9494  12459   3375   1143    152       C  
-ATOM   6475  CD  GLU D 209     -33.098  12.889   7.796  1.00 84.78           C  
-ANISOU 6475  CD  GLU D 209     9289  10104  12820   3280   1021    157       C  
-ATOM   6476  OE1 GLU D 209     -32.975  11.901   8.552  1.00 81.38           O  
-ANISOU 6476  OE1 GLU D 209     8763   9776  12384   3091   1132     75       O  
-ATOM   6477  OE2 GLU D 209     -33.717  12.835   6.710  1.00 88.87           O  
-ANISOU 6477  OE2 GLU D 209     9578  10781  13407   3377    812    243       O  
-ATOM   6478  N   THR D 210     -29.763  15.969   5.019  1.00 70.85           N  
-ANISOU 6478  N   THR D 210     8731   7522  10666   3348    653    487       N  
-ATOM   6479  CA  THR D 210     -29.237  16.698   3.871  1.00 75.72           C  
-ANISOU 6479  CA  THR D 210     9574   8002  11192   3387    496    615       C  
-ATOM   6480  C   THR D 210     -28.691  15.731   2.820  1.00 74.44           C  
-ANISOU 6480  C   THR D 210     9288   8013  10984   3250    302    692       C  
-ATOM   6481  O   THR D 210     -28.882  15.929   1.620  1.00 76.77           O  
-ANISOU 6481  O   THR D 210     9557   8360  11250   3331    107    813       O  
-ATOM   6482  CB  THR D 210     -28.115  17.662   4.302  1.00 77.98           C  
-ANISOU 6482  CB  THR D 210    10342   7951  11338   3283    618    590       C  
-ATOM   6483  OG1 THR D 210     -28.671  18.707   5.107  1.00 82.90           O  
-ANISOU 6483  OG1 THR D 210    11115   8400  11984   3431    778    536       O  
-ATOM   6484  CG2 THR D 210     -27.417  18.274   3.090  1.00 78.69           C  
-ANISOU 6484  CG2 THR D 210    10679   7908  11313   3260    464    721       C  
-ATOM   6485  N   GLY D 211     -28.038  14.671   3.287  1.00 68.99           N  
-ANISOU 6485  N   GLY D 211     8521   7432  10261   2974    336    598       N  
-ATOM   6486  CA  GLY D 211     -27.394  13.704   2.413  1.00 66.02           C  
-ANISOU 6486  CA  GLY D 211     8054   7228   9804   2721    157    616       C  
-ATOM   6487  C   GLY D 211     -28.318  12.753   1.668  1.00 61.78           C  
-ANISOU 6487  C   GLY D 211     7131   6996   9347   2764    -12    655       C  
-ATOM   6488  O   GLY D 211     -28.136  12.519   0.468  1.00 57.56           O  
-ANISOU 6488  O   GLY D 211     6585   6548   8736   2712   -207    738       O  
-ATOM   6489  N   LYS D 212     -29.294  12.189   2.377  1.00 61.94           N  
-ANISOU 6489  N   LYS D 212     6845   7181   9509   2835     67    594       N  
-ATOM   6490  CA  LYS D 212     -30.244  11.262   1.767  1.00 63.66           C  
-ANISOU 6490  CA  LYS D 212     6674   7701   9813   2848    -88    622       C  
-ATOM   6491  C   LYS D 212     -31.054  11.967   0.693  1.00 61.49           C  
-ANISOU 6491  C   LYS D 212     6320   7471   9574   3118   -272    768       C  
-ATOM   6492  O   LYS D 212     -31.357  11.391  -0.346  1.00 61.37           O  
-ANISOU 6492  O   LYS D 212     6130   7653   9534   3076   -494    835       O  
-ATOM   6493  CB  LYS D 212     -31.179  10.664   2.821  1.00 66.77           C  
-ANISOU 6493  CB  LYS D 212     6763   8246  10361   2877     64    531       C  
-ATOM   6494  CG  LYS D 212     -30.903   9.200   3.139  1.00 68.15           C  
-ANISOU 6494  CG  LYS D 212     6788   8592  10514   2559     67    428       C  
-ATOM   6495  CD  LYS D 212     -31.931   8.638   4.117  1.00 72.95           C  
-ANISOU 6495  CD  LYS D 212     7091   9355  11272   2587    222    352       C  
-ATOM   6496  CE  LYS D 212     -33.358   8.937   3.670  1.00 77.72           C  
-ANISOU 6496  CE  LYS D 212     7424  10137  11968   2774    117    380       C  
-ATOM   6497  NZ  LYS D 212     -34.379   8.236   4.506  1.00 80.62           N  
-ANISOU 6497  NZ  LYS D 212     7502  10700  12430   2714    239    277       N  
-ATOM   6498  N   ALA D 213     -31.387  13.223   0.958  1.00 61.16           N  
-ANISOU 6498  N   ALA D 213     6449   7232   9559   3324   -196    785       N  
-ATOM   6499  CA  ALA D 213     -32.150  14.045   0.029  1.00 65.01           C  
-ANISOU 6499  CA  ALA D 213     6916   7712  10072   3534   -368    900       C  
-ATOM   6500  C   ALA D 213     -31.334  14.371  -1.219  1.00 68.45           C  
-ANISOU 6500  C   ALA D 213     7611   8054  10344   3505   -547   1035       C  
-ATOM   6501  O   ALA D 213     -31.832  14.314  -2.345  1.00 71.00           O  
-ANISOU 6501  O   ALA D 213     7823   8507  10649   3560   -783   1143       O  
-ATOM   6502  CB  ALA D 213     -32.578  15.334   0.722  1.00 63.23           C  
-ANISOU 6502  CB  ALA D 213     6852   7262   9911   3750   -207    883       C  
-ATOM   6503  N   LYS D 214     -30.075  14.724  -0.984  1.00 64.91           N  
-ANISOU 6503  N   LYS D 214     7523   7373   9767   3406   -430   1026       N  
-ATOM   6504  CA  LYS D 214     -29.154  15.202  -2.003  1.00 64.38           C  
-ANISOU 6504  CA  LYS D 214     7783   7156   9522   3365   -540   1138       C  
-ATOM   6505  C   LYS D 214     -28.841  14.111  -3.018  1.00 63.15           C  
-ANISOU 6505  C   LYS D 214     7504   7225   9264   3133   -739   1152       C  
-ATOM   6506  O   LYS D 214     -28.725  14.378  -4.217  1.00 64.68           O  
-ANISOU 6506  O   LYS D 214     7824   7413   9337   3159   -920   1273       O  
-ATOM   6507  CB  LYS D 214     -27.868  15.639  -1.303  1.00 65.00           C  
-ANISOU 6507  CB  LYS D 214     8225   6968   9502   3175   -346   1060       C  
-ATOM   6508  CG  LYS D 214     -26.880  16.470  -2.098  1.00 67.25           C  
-ANISOU 6508  CG  LYS D 214     8916   7025   9613   3100   -389   1150       C  
-ATOM   6509  CD  LYS D 214     -25.909  17.104  -1.107  1.00 68.85           C  
-ANISOU 6509  CD  LYS D 214     9436   6957   9768   2960   -171   1063       C  
-ATOM   6510  CE  LYS D 214     -24.672  17.689  -1.752  1.00 69.16           C  
-ANISOU 6510  CE  LYS D 214     9848   6799   9630   2765   -183   1119       C  
-ATOM   6511  NZ  LYS D 214     -23.704  18.120  -0.698  1.00 67.81           N  
-ANISOU 6511  NZ  LYS D 214     9929   6416   9420   2568     10   1015       N  
-ATOM   6512  N   TYR D 215     -28.707  12.880  -2.531  1.00 58.99           N  
-ANISOU 6512  N   TYR D 215     6758   6882   8774   2898   -697   1025       N  
-ATOM   6513  CA  TYR D 215     -28.277  11.769  -3.373  1.00 55.57           C  
-ANISOU 6513  CA  TYR D 215     6254   6629   8233   2640   -844   1007       C  
-ATOM   6514  C   TYR D 215     -29.407  10.822  -3.766  1.00 55.94           C  
-ANISOU 6514  C   TYR D 215     5912   6981   8361   2659  -1011   1010       C  
-ATOM   6515  O   TYR D 215     -29.201   9.891  -4.539  1.00 56.76           O  
-ANISOU 6515  O   TYR D 215     5962   7236   8369   2458  -1149    996       O  
-ATOM   6516  CB  TYR D 215     -27.115  11.024  -2.709  1.00 53.53           C  
-ANISOU 6516  CB  TYR D 215     6085   6331   7923   2332   -694    874       C  
-ATOM   6517  CG  TYR D 215     -25.905  11.914  -2.540  1.00 53.02           C  
-ANISOU 6517  CG  TYR D 215     6394   5995   7754   2262   -574    884       C  
-ATOM   6518  CD1 TYR D 215     -25.230  12.404  -3.652  1.00 56.21           C  
-ANISOU 6518  CD1 TYR D 215     7051   6302   8003   2218   -666    982       C  
-ATOM   6519  CD2 TYR D 215     -25.455  12.289  -1.277  1.00 50.15           C  
-ANISOU 6519  CD2 TYR D 215     6143   5474   7439   2226   -371    798       C  
-ATOM   6520  CE1 TYR D 215     -24.135  13.234  -3.520  1.00 55.95           C  
-ANISOU 6520  CE1 TYR D 215     7350   6030   7880   2128   -553    996       C  
-ATOM   6521  CE2 TYR D 215     -24.350  13.118  -1.130  1.00 50.60           C  
-ANISOU 6521  CE2 TYR D 215     6538   5291   7397   2131   -277    807       C  
-ATOM   6522  CZ  TYR D 215     -23.698  13.589  -2.259  1.00 52.95           C  
-ANISOU 6522  CZ  TYR D 215     7059   5503   7555   2079   -366    907       C  
-ATOM   6523  OH  TYR D 215     -22.607  14.417  -2.138  1.00 50.48           O  
-ANISOU 6523  OH  TYR D 215     7072   4961   7148   1958   -268    919       O  
-ATOM   6524  N   LYS D 216     -30.594  11.083  -3.231  1.00 62.01           N  
-ANISOU 6524  N   LYS D 216     6418   7837   9306   2896   -990   1026       N  
-ATOM   6525  CA  LYS D 216     -31.803  10.330  -3.552  1.00 71.40           C  
-ANISOU 6525  CA  LYS D 216     7199   9330  10599   2934  -1152   1042       C  
-ATOM   6526  C   LYS D 216     -32.000  10.209  -5.057  1.00 77.34           C  
-ANISOU 6526  C   LYS D 216     7956  10207  11223   2925  -1454   1161       C  
-ATOM   6527  O   LYS D 216     -31.826  11.184  -5.791  1.00 79.09           O  
-ANISOU 6527  O   LYS D 216     8413  10286  11351   3091  -1550   1291       O  
-ATOM   6528  CB  LYS D 216     -33.023  11.036  -2.950  1.00 77.33           C  
-ANISOU 6528  CB  LYS D 216     7760  10079  11543   3172  -1090   1034       C  
-ATOM   6529  CG  LYS D 216     -34.351  10.306  -3.113  1.00 82.46           C  
-ANISOU 6529  CG  LYS D 216     7991  11017  12323   3144  -1227    998       C  
-ATOM   6530  CD  LYS D 216     -34.555   9.256  -2.030  1.00 83.20           C  
-ANISOU 6530  CD  LYS D 216     7853  11252  12507   2968  -1051    840       C  
-ATOM   6531  CE  LYS D 216     -35.909   8.577  -2.172  1.00 86.38           C  
-ANISOU 6531  CE  LYS D 216     7854  11934  13034   2928  -1173    794       C  
-ATOM   6532  NZ  LYS D 216     -37.035   9.553  -2.143  1.00 90.53           N  
-ANISOU 6532  NZ  LYS D 216     8247  12443  13709   3201  -1199    834       N  
-ATOM   6533  N   ALA D 217     -32.360   9.010  -5.508  1.00 80.59           N  
-ANISOU 6533  N   ALA D 217     8135  10871  11615   2719  -1601   1115       N  
-ATOM   6534  CA  ALA D 217     -32.677   8.768  -6.913  1.00 84.79           C  
-ANISOU 6534  CA  ALA D 217     8648  11554  12013   2684  -1906   1215       C  
-ATOM   6535  C   ALA D 217     -33.687   9.784  -7.438  1.00 91.06           C  
-ANISOU 6535  C   ALA D 217     9373  12340  12884   2954  -2069   1354       C  
-ATOM   6536  O   ALA D 217     -34.549  10.258  -6.698  1.00 94.64           O  
-ANISOU 6536  O   ALA D 217     9643  12772  13546   3108  -1973   1323       O  
-ATOM   6537  CB  ALA D 217     -33.204   7.358  -7.095  1.00 84.21           C  
-ANISOU 6537  CB  ALA D 217     8282  11761  11953   2434  -2023   1129       C  
-ATOM   6538  OXT ALA D 217     -33.663  10.157  -8.610  1.00 93.91           O  
-ANISOU 6538  OXT ALA D 217     9890  12693  13099   2993  -2287   1487       O  
-TER    6539      ALA D 217                                                      
-HETATM 6540  OAD 3L7 A 301      22.653  12.169  14.376  1.00 60.75           O  
-HETATM 6541  PBA 3L7 A 301      22.534  11.057  15.525  1.00 66.65           P  
-HETATM 6542  OAE 3L7 A 301      21.468  10.018  15.123  1.00 61.34           O  
-HETATM 6543  OAB 3L7 A 301      22.136  11.700  16.830  1.00 58.23           O  
-HETATM 6544  CAP 3L7 A 301      24.163  10.139  15.725  1.00 73.28           C  
-HETATM 6545  CAK 3L7 A 301      25.461  10.764  15.216  1.00 72.85           C  
-HETATM 6546  OAU 3L7 A 301      26.627  10.207  15.682  1.00 69.45           O  
-HETATM 6547  CAJ 3L7 A 301      27.165   9.126  15.052  1.00 59.88           C  
-HETATM 6548  CAL 3L7 A 301      27.517   9.287  13.579  1.00 49.95           C  
-HETATM 6549  NAY 3L7 A 301      27.521   8.046  12.781  1.00 42.66           N  
-HETATM 6550  CAN 3L7 A 301      28.860   7.450  12.701  1.00 39.28           C  
-HETATM 6551  CAQ 3L7 A 301      28.877   5.945  12.648  1.00 37.42           C  
-HETATM 6552  PBB 3L7 A 301      30.472   5.138  12.617  1.00 45.66           P  
-HETATM 6553  OAF 3L7 A 301      31.444   5.868  11.684  1.00 46.18           O  
-HETATM 6554  OAG 3L7 A 301      31.063   5.124  14.091  1.00 51.22           O  
-HETATM 6555  OAC 3L7 A 301      30.306   3.744  12.188  1.00 42.01           O  
-HETATM 6556  CAM 3L7 A 301      27.017   8.334  11.416  1.00 39.77           C  
-HETATM 6557  CAO 3L7 A 301      27.744   9.349  10.621  1.00 38.15           C  
-HETATM 6558  N9  3L7 A 301      27.558   9.108   9.137  1.00 42.15           N  
-HETATM 6559  C4  3L7 A 301      26.435   9.513   8.408  1.00 39.09           C  
-HETATM 6560  N3  3L7 A 301      25.257  10.231   8.767  1.00 36.41           N  
-HETATM 6561  C2  3L7 A 301      24.329  10.487   7.820  1.00 40.80           C  
-HETATM 6562  N1  3L7 A 301      24.520  10.071   6.534  1.00 39.93           N  
-HETATM 6563  C6  3L7 A 301      25.627   9.382   6.116  1.00 42.00           C  
-HETATM 6564  O6  3L7 A 301      25.771   8.997   4.853  1.00 42.39           O  
-HETATM 6565  C5  3L7 A 301      26.645   9.085   7.113  1.00 42.28           C  
-HETATM 6566  N7  3L7 A 301      27.882   8.418   7.071  1.00 45.38           N  
-HETATM 6567  C8  3L7 A 301      28.403   8.442   8.315  1.00 43.08           C  
-HETATM 6568 MG    MG A 302      23.579   6.214  14.654  1.00 28.55          MG  
-HETATM 6569 MG    MG A 303      23.966  13.164  12.618  1.00 45.81          MG  
-HETATM 6570  OADA3L7 B 301      -7.444 -14.766 -20.104  0.35 62.45           O  
-HETATM 6571  OADB3L7 B 301      -5.877  -9.820 -14.863  0.55 31.21           O  
-HETATM 6572  PBAA3L7 B 301      -8.048 -13.499 -19.456  0.35 62.55           P  
-HETATM 6573  PBAB3L7 B 301      -6.583 -10.638 -15.957  0.55 31.96           P  
-HETATM 6574  OAEA3L7 B 301      -9.602 -13.726 -19.163  0.35 51.89           O  
-HETATM 6575  OAEB3L7 B 301      -5.851 -12.043 -16.110  0.55 27.34           O  
-HETATM 6576  OABA3L7 B 301      -7.334 -13.212 -18.170  0.35 60.85           O  
-HETATM 6577  OABB3L7 B 301      -8.017 -10.850 -15.568  0.55 26.80           O  
-HETATM 6578  CAPA3L7 B 301      -7.846 -12.053 -20.635  0.35 43.17           C  
-HETATM 6579  CAPB3L7 B 301      -6.516  -9.708 -17.589  0.55 35.50           C  
-HETATM 6580  CAKA3L7 B 301      -6.430 -11.544 -20.876  0.35 42.94           C  
-HETATM 6581  CAKB3L7 B 301      -5.877  -8.323 -17.600  0.55 39.18           C  
-HETATM 6582  OAUA3L7 B 301      -5.986 -10.517 -20.087  0.35 43.07           O  
-HETATM 6583  OAUB3L7 B 301      -6.301  -7.458 -18.576  0.55 42.73           O  
-HETATM 6584  CAJA3L7 B 301      -4.772  -9.960 -20.340  0.35 40.10           C  
-HETATM 6585  CAJB3L7 B 301      -5.369  -6.713 -19.234  0.55 42.67           C  
-HETATM 6586  CALA3L7 B 301      -4.538  -8.558 -19.802  0.35 40.88           C  
-HETATM 6587  CALB3L7 B 301      -3.936  -7.213 -19.143  0.55 41.21           C  
-HETATM 6588  NAYA3L7 B 301      -3.223  -7.935 -20.077  0.35 40.19           N  
-HETATM 6589  NAYB3L7 B 301      -3.467  -8.156 -20.185  0.55 40.45           N  
-HETATM 6590  CANA3L7 B 301      -3.043  -7.637 -21.512  0.35 38.92           C  
-HETATM 6591  CANB3L7 B 301      -3.605  -7.510 -21.490  0.55 38.42           C  
-HETATM 6592  CAQA3L7 B 301      -2.829  -6.174 -21.874  0.35 38.79           C  
-HETATM 6593  CAQB3L7 B 301      -2.627  -6.398 -21.801  0.55 38.50           C  
-HETATM 6594  PBBA3L7 B 301      -2.669  -5.630 -23.586  0.35 35.23           P  
-HETATM 6595  PBBB3L7 B 301      -2.795  -5.672 -23.428  0.55 36.74           P  
-HETATM 6596  OAFA3L7 B 301      -1.673  -6.490 -24.362  0.35 32.70           O  
-HETATM 6597  OAFB3L7 B 301      -1.938  -6.460 -24.422  0.55 33.00           O  
-HETATM 6598  OAGA3L7 B 301      -4.047  -5.660 -24.359  0.35 40.07           O  
-HETATM 6599  OAGB3L7 B 301      -4.311  -5.728 -23.872  0.55 37.73           O  
-HETATM 6600  OACA3L7 B 301      -2.166  -4.254 -23.590  0.35 32.06           O  
-HETATM 6601  OACB3L7 B 301      -2.322  -4.285 -23.400  0.55 33.25           O  
-HETATM 6602  CAMA3L7 B 301      -2.168  -8.840 -19.551  0.35 38.93           C  
-HETATM 6603  CAMB3L7 B 301      -2.025  -8.377 -19.946  0.55 38.94           C  
-HETATM 6604  CAOA3L7 B 301      -1.288  -9.538 -20.520  0.35 37.75           C  
-HETATM 6605  CAOB3L7 B 301      -1.352  -9.612 -20.420  0.55 37.66           C  
-HETATM 6606  N9 A3L7 B 301       0.191  -9.435 -20.198  0.35 36.62           N  
-HETATM 6607  N9 B3L7 B 301       0.134  -9.508 -20.140  0.55 36.82           N  
-HETATM 6608  C4 A3L7 B 301       0.767  -9.824 -18.978  0.35 35.52           C  
-HETATM 6609  C4 B3L7 B 301       0.738  -9.871 -18.924  0.55 35.64           C  
-HETATM 6610  N3 A3L7 B 301       0.220 -10.399 -17.797  0.35 33.86           N  
-HETATM 6611  N3 B3L7 B 301       0.222 -10.440 -17.727  0.55 33.86           N  
-HETATM 6612  C2 A3L7 B 301       1.044 -10.679 -16.758  0.35 33.32           C  
-HETATM 6613  C2 B3L7 B 301       1.074 -10.701 -16.703  0.55 33.35           C  
-HETATM 6614  N1 A3L7 B 301       2.377 -10.423 -16.835  0.35 31.94           N  
-HETATM 6615  N1 B3L7 B 301       2.403 -10.432 -16.814  0.55 31.38           N  
-HETATM 6616  C6 A3L7 B 301       2.974  -9.873 -17.938  0.35 33.16           C  
-HETATM 6617  C6 B3L7 B 301       2.969  -9.886 -17.935  0.55 33.20           C  
-HETATM 6618  O6 A3L7 B 301       4.284  -9.633 -17.976  0.35 32.91           O  
-HETATM 6619  O6 B3L7 B 301       4.274  -9.630 -18.012  0.55 32.82           O  
-HETATM 6620  C5 A3L7 B 301       2.115  -9.557 -19.074  0.35 34.73           C  
-HETATM 6621  C5 B3L7 B 301       2.080  -9.591 -19.053  0.55 34.33           C  
-HETATM 6622  N7 A3L7 B 301       2.345  -9.002 -20.342  0.35 37.28           N  
-HETATM 6623  N7 B3L7 B 301       2.278  -9.046 -20.332  0.55 37.76           N  
-HETATM 6624  C8 A3L7 B 301       1.164  -8.941 -20.992  0.35 37.40           C  
-HETATM 6625  C8 B3L7 B 301       1.082  -9.002 -20.957  0.55 37.38           C  
-HETATM 6626 MG    MG B 302      -5.210  -5.329 -17.495  1.00 75.02          MG  
-HETATM 6627 MG    MG B 303      -3.838 -12.735 -16.918  1.00 36.82          MG  
-HETATM 6628  OAD 3L7 C 301       7.098   7.277  29.693  0.76 32.84           O  
-HETATM 6629  PBA 3L7 C 301       8.003   6.646  30.843  0.76 42.99           P  
-HETATM 6630  OAE 3L7 C 301       9.433   6.342  30.358  0.76 39.61           O  
-HETATM 6631  OAB 3L7 C 301       7.368   5.365  31.307  0.76 45.48           O  
-HETATM 6632  CAP 3L7 C 301       8.121   7.875  32.272  0.76 51.46           C  
-HETATM 6633  CAK 3L7 C 301       6.815   8.492  32.781  0.76 53.49           C  
-HETATM 6634  OAU 3L7 C 301       6.778   9.137  33.991  0.76 52.28           O  
-HETATM 6635  CAJ 3L7 C 301       5.689   9.889  34.322  0.76 46.21           C  
-HETATM 6636  CAL 3L7 C 301       4.344   9.192  34.486  0.76 38.41           C  
-HETATM 6637  NAY 3L7 C 301       3.165   9.912  33.952  0.76 38.50           N  
-HETATM 6638  CAN 3L7 C 301       2.703  10.972  34.866  0.76 38.99           C  
-HETATM 6639  CAQ 3L7 C 301       1.721  11.988  34.315  0.76 37.56           C  
-HETATM 6640  PBB 3L7 C 301       1.206  13.332  35.388  0.76 29.00           P  
-HETATM 6641  OAF 3L7 C 301       0.301  14.203  34.646  0.76 23.38           O  
-HETATM 6642  OAG 3L7 C 301       2.459  14.134  35.895  0.76 30.40           O  
-HETATM 6643  OAC 3L7 C 301       0.461  12.792  36.618  0.76 32.35           O  
-HETATM 6644  CAM 3L7 C 301       2.064   8.943  33.723  0.76 38.34           C  
-HETATM 6645  CAO 3L7 C 301       1.745   7.929  34.768  0.76 32.21           C  
-HETATM 6646  N9  3L7 C 301       0.362   7.355  34.526  0.76 32.63           N  
-HETATM 6647  C4  3L7 C 301       0.091   6.254  33.709  0.76 31.75           C  
-HETATM 6648  N3  3L7 C 301       0.940   5.393  32.973  0.76 30.79           N  
-HETATM 6649  C2  3L7 C 301       0.377   4.376  32.279  0.76 28.89           C  
-HETATM 6650  N1  3L7 C 301      -0.969   4.183  32.269  0.76 27.45           N  
-HETATM 6651  C6  3L7 C 301      -1.851   4.972  32.963  0.76 29.01           C  
-HETATM 6652  O6  3L7 C 301      -3.171   4.753  32.937  0.76 28.01           O  
-HETATM 6653  C5  3L7 C 301      -1.274   6.072  33.721  0.76 32.09           C  
-HETATM 6654  N7  3L7 C 301      -1.823   7.074  34.529  0.76 33.26           N  
-HETATM 6655  C8  3L7 C 301      -0.813   7.834  34.991  0.76 33.04           C  
-HETATM 6656 MG    MG C 302       4.650  10.536  29.631  1.00 27.57          MG  
-HETATM 6657 MG    MG C 303       5.548   4.520  32.837  1.00 41.66          MG  
-HETATM 6658  OAD 3L7 D 301     -23.450  -3.557  -5.767  1.00 80.13           O  
-HETATM 6659  PBA 3L7 D 301     -23.548  -3.063  -4.356  1.00 81.70           P  
-HETATM 6660  OAE 3L7 D 301     -23.594  -1.466  -4.354  1.00115.71           O  
-HETATM 6661  OAB 3L7 D 301     -22.311  -3.544  -3.571  1.00 79.26           O  
-HETATM 6662  CAP 3L7 D 301     -25.105  -3.719  -3.525  1.00 78.09           C  
-HETATM 6663  CAK 3L7 D 301     -25.603  -5.119  -3.877  1.00 76.52           C  
-HETATM 6664  OAU 3L7 D 301     -26.950  -5.349  -3.762  1.00 74.40           O  
-HETATM 6665  CAJ 3L7 D 301     -27.439  -6.041  -2.691  1.00 68.27           C  
-HETATM 6666  CAL 3L7 D 301     -27.919  -5.258  -1.476  1.00 60.41           C  
-HETATM 6667  NAY 3L7 D 301     -27.586  -5.819  -0.145  1.00 54.55           N  
-HETATM 6668  CAN 3L7 D 301     -28.666  -6.675   0.377  1.00 52.51           C  
-HETATM 6669  CAQ 3L7 D 301     -28.264  -7.882   1.198  1.00 50.36           C  
-HETATM 6670  PBB 3L7 D 301     -29.549  -8.981   1.821  1.00 45.20           P  
-HETATM 6671  OAF 3L7 D 301     -29.977  -9.959   0.648  1.00 40.70           O  
-HETATM 6672  OAG 3L7 D 301     -30.756  -8.181   2.323  1.00 41.87           O  
-HETATM 6673  OAC 3L7 D 301     -28.994  -9.755   2.951  1.00 37.63           O  
-HETATM 6674  CAM 3L7 D 301     -27.324  -4.709   0.805  1.00 52.48           C  
-HETATM 6675  CAO 3L7 D 301     -28.260  -3.555   0.847  1.00 48.58           C  
-HETATM 6676  N9  3L7 D 301     -28.212  -2.863   2.197  1.00 43.31           N  
-HETATM 6677  C4  3L7 D 301     -27.370  -1.791   2.508  1.00 42.40           C  
-HETATM 6678  N3  3L7 D 301     -26.423  -1.071   1.739  1.00 39.74           N  
-HETATM 6679  C2  3L7 D 301     -25.747  -0.053   2.331  1.00 41.42           C  
-HETATM 6680  N1  3L7 D 301     -25.962   0.280   3.630  1.00 37.89           N  
-HETATM 6681  C6  3L7 D 301     -26.863  -0.375   4.431  1.00 40.68           C  
-HETATM 6682  O6  3L7 D 301     -27.071  -0.031   5.698  1.00 37.04           O  
-HETATM 6683  C5  3L7 D 301     -27.607  -1.472   3.827  1.00 42.29           C  
-HETATM 6684  N7  3L7 D 301     -28.586  -2.351   4.305  1.00 41.39           N  
-HETATM 6685  C8  3L7 D 301     -28.925  -3.180   3.298  1.00 40.50           C  
-HETATM 6686 MG    MG D 302     -23.121  -6.852  -1.000  1.00 26.21          MG  
-HETATM 6687 MG    MG D 303     -25.740  -0.547  -2.907  1.00 45.21          MG  
-HETATM 6688  O   HOH A 401       8.285  12.435   3.609  1.00 26.92           O  
-HETATM 6689  O   HOH A 402      15.858   5.506  11.235  1.00 26.44           O  
-HETATM 6690  O   HOH A 403       7.968  -9.955   9.122  1.00 31.00           O  
-HETATM 6691  O   HOH A 404      15.153  17.070  10.439  1.00 37.46           O  
-HETATM 6692  O   HOH A 405       8.043   9.541  12.387  1.00 31.36           O  
-HETATM 6693  O   HOH A 406       9.452  -7.993   2.006  1.00 28.91           O  
-HETATM 6694  O   HOH A 407       5.285  -2.739   1.644  1.00 34.85           O  
-HETATM 6695  O   HOH A 408       2.520  -3.775  14.955  1.00 34.48           O  
-HETATM 6696  O   HOH A 409      21.818  -7.596  -3.050  1.00 36.85           O  
-HETATM 6697  O   HOH A 410       7.847   4.557   8.277  1.00 39.70           O  
-HETATM 6698  O   HOH A 411      26.827   3.052  14.226  1.00 40.20           O  
-HETATM 6699  O   HOH A 412      29.274   2.203  14.147  1.00 35.93           O  
-HETATM 6700  O   HOH A 413      17.013   3.268  30.713  1.00 55.05           O  
-HETATM 6701  O   HOH A 414      16.313  16.919  13.791  1.00 38.84           O  
-HETATM 6702  O   HOH A 415       7.180   0.493  17.200  1.00 35.11           O  
-HETATM 6703  O   HOH A 416      31.129  -0.010   7.421  1.00 45.01           O  
-HETATM 6704  O   HOH A 417       2.613  -8.212  19.409  1.00 38.95           O  
-HETATM 6705  O   HOH A 418      21.781   7.104  15.752  1.00 34.65           O  
-HETATM 6706  O   HOH A 419       6.589  -6.816   1.984  1.00 40.18           O  
-HETATM 6707  O   HOH A 420      10.213 -15.289   2.395  1.00 37.44           O  
-HETATM 6708  O   HOH A 421      13.357  15.745 -12.744  1.00 48.12           O  
-HETATM 6709  O   HOH A 422       5.914  -8.693  10.295  1.00 28.72           O  
-HETATM 6710  O   HOH A 423       5.084  -0.291  20.682  1.00 39.43           O  
-HETATM 6711  O   HOH A 424      31.852  -2.928  34.185  1.00 41.21           O  
-HETATM 6712  O   HOH A 425      17.140 -11.431   4.702  1.00 39.12           O  
-HETATM 6713  O   HOH A 426      25.446   6.113  13.118  1.00 42.19           O  
-HETATM 6714  O   HOH A 427      15.894  14.239  -9.052  1.00 43.14           O  
-HETATM 6715  O   HOH A 428       4.949  -4.655   4.467  1.00 41.01           O  
-HETATM 6716  O   HOH A 429       6.155  18.339  -2.900  1.00 46.46           O  
-HETATM 6717  O   HOH A 430      19.572 -11.545   4.541  1.00 46.34           O  
-HETATM 6718  O   HOH A 431      20.186  -4.324  -5.176  1.00 56.18           O  
-HETATM 6719  O   HOH A 432      33.206  -3.142  21.297  1.00 47.60           O  
-HETATM 6720  O   HOH A 433      27.421  -7.322   8.447  1.00 52.95           O  
-HETATM 6721  O   HOH A 434      27.635  -7.378  16.483  1.00 49.57           O  
-HETATM 6722  O   HOH A 435      18.166   0.252  -8.440  1.00 48.88           O  
-HETATM 6723  O   HOH A 436       7.555  17.406  -9.004  1.00 51.35           O  
-HETATM 6724  O   HOH A 437      13.530   0.212  -9.954  1.00 46.42           O  
-HETATM 6725  O   HOH A 438      10.765 -15.830  12.300  1.00 43.22           O  
-HETATM 6726  O   HOH A 439      20.020  -2.143  -5.767  1.00 43.23           O  
-HETATM 6727  O   HOH A 440       8.457  16.597   5.965  1.00 38.55           O  
-HETATM 6728  O   HOH A 441      28.295  12.437  -1.042  1.00 46.97           O  
-HETATM 6729  O   HOH A 442      23.608  -8.043  -5.331  1.00 57.06           O  
-HETATM 6730  O   HOH A 443       9.737 -11.251  30.633  1.00 53.54           O  
-HETATM 6731  O   HOH A 444      23.721   8.443  19.042  1.00 48.84           O  
-HETATM 6732  O   HOH A 445      35.050   2.827  19.371  1.00 54.81           O  
-HETATM 6733  O   HOH A 446      17.138 -17.212  22.969  1.00 38.19           O  
-HETATM 6734  O   HOH A 447      16.555 -17.159  20.348  1.00 40.45           O  
-HETATM 6735  O   HOH A 448      21.574  10.133  11.630  1.00 40.78           O  
-HETATM 6736  O   HOH A 449      24.783   6.915  16.371  1.00 42.43           O  
-HETATM 6737  O   HOH A 450      23.355   8.260  13.669  1.00 40.58           O  
-HETATM 6738  O   HOH A 451      24.751  13.628  10.173  1.00 49.38           O  
-HETATM 6739  O   HOH A 452      24.162  10.678  11.479  1.00 50.24           O  
-HETATM 6740  O   HOH A 453       4.747  -0.719   5.120  1.00 72.45           O  
-HETATM 6741  O   HOH B 401      -3.756  -2.392 -23.030  1.00 38.23           O  
-HETATM 6742  O   HOH B 402      -9.729   1.810  -2.340  1.00 32.81           O  
-HETATM 6743  O   HOH B 403       2.823 -11.238  -0.455  1.00 26.30           O  
-HETATM 6744  O   HOH B 404      -1.231  -3.104  -1.421  1.00 32.12           O  
-HETATM 6745  O   HOH B 405      -3.512 -15.975  -7.485  1.00 32.23           O  
-HETATM 6746  O   HOH B 406      12.191 -14.926   0.735  1.00 31.05           O  
-HETATM 6747  O   HOH B 407      14.259 -16.922   1.917  1.00 32.08           O  
-HETATM 6748  O   HOH B 408       2.453  -5.878   1.347  1.00 44.12           O  
-HETATM 6749  O   HOH B 409      -3.066  -4.242  -9.497  1.00 28.32           O  
-HETATM 6750  O   HOH B 410      12.831   7.003 -14.408  1.00 35.79           O  
-HETATM 6751  O   HOH B 411      19.476  -8.130  -4.396  1.00 40.84           O  
-HETATM 6752  O   HOH B 412       1.545  11.184 -13.507  1.00 39.76           O  
-HETATM 6753  O   HOH B 413      -2.326  10.455  -0.829  1.00 31.18           O  
-HETATM 6754  O   HOH B 414      -3.151  -9.335 -14.781  1.00 48.25           O  
-HETATM 6755  O   HOH B 415       8.639  15.702  -6.127  1.00 35.93           O  
-HETATM 6756  O   HOH B 416       0.227 -15.213  -0.342  1.00 36.38           O  
-HETATM 6757  O   HOH B 417       5.824   3.873   1.367  1.00 39.14           O  
-HETATM 6758  O   HOH B 418       6.192   8.869  -3.008  1.00 38.33           O  
-HETATM 6759  O   HOH B 419       6.677  16.070  -4.487  1.00 37.09           O  
-HETATM 6760  O   HOH B 420     -11.778  10.939   1.622  1.00 39.84           O  
-HETATM 6761  O   HOH B 421      -1.571 -13.722 -17.150  1.00 37.71           O  
-HETATM 6762  O   HOH B 422       4.799  11.651 -11.555  1.00 41.31           O  
-HETATM 6763  O   HOH B 423      -7.575   6.340   2.416  1.00 37.62           O  
-HETATM 6764  O   HOH B 424       7.615 -22.814  -5.182  1.00 54.16           O  
-HETATM 6765  O   HOH B 425       5.071 -11.366  -0.776  1.00 39.89           O  
-HETATM 6766  O   HOH B 426      -3.118 -24.925  -6.408  1.00 55.77           O  
-HETATM 6767  O   HOH B 427       4.804 -23.843   1.242  1.00 49.16           O  
-HETATM 6768  O   HOH B 428      -3.239   5.472   1.876  1.00 48.08           O  
-HETATM 6769  O   HOH B 429      -0.614 -13.446 -19.983  1.00 44.52           O  
-HETATM 6770  O   HOH B 430      -0.661  -8.881 -24.121  1.00 46.32           O  
-HETATM 6771  O   HOH B 431      -2.867   3.446   0.941  1.00 57.86           O  
-HETATM 6772  O   HOH B 432      -1.913 -16.951  -0.407  1.00 47.25           O  
-HETATM 6773  O   HOH B 433       2.771   7.918 -20.720  1.00 53.73           O  
-HETATM 6774  O   HOH B 434      -1.660 -11.369 -24.025  1.00 57.55           O  
-HETATM 6775  O   HOH B 435      12.561  -4.765 -23.088  1.00 47.25           O  
-HETATM 6776  O   HOH B 436     -16.157 -10.593 -12.696  1.00 66.01           O  
-HETATM 6777  O   HOH B 437      11.168   8.860 -15.647  1.00 47.90           O  
-HETATM 6778  O   HOH B 438       5.787   7.417  -0.077  1.00 61.28           O  
-HETATM 6779  O   HOH B 439       2.854   9.225 -15.411  1.00 42.17           O  
-HETATM 6780  O   HOH B 440      12.353   9.221 -18.555  1.00 52.30           O  
-HETATM 6781  O   HOH B 441      -1.525 -16.322 -17.882  1.00 44.43           O  
-HETATM 6782  O   HOH B 442     -12.228  -7.454 -27.862  1.00 68.46           O  
-HETATM 6783  O   HOH B 443      16.218   0.437 -20.785  1.00 52.72           O  
-HETATM 6784  O   HOH B 444      16.255   0.046 -13.476  1.00 38.85           O  
-HETATM 6785  O   HOH B 445      11.320 -22.724   0.362  1.00 62.53           O  
-HETATM 6786  O   HOH B 446      -2.539 -10.786 -16.969  1.00 37.23           O  
-HETATM 6787  O   HOH B 447      -4.640 -14.523 -16.855  1.00 41.20           O  
-HETATM 6788  O   HOH B 448      -4.091 -12.701 -19.169  1.00 44.51           O  
-HETATM 6789  O   HOH C 401      -0.720  11.582  -2.648  1.00 35.45           O  
-HETATM 6790  O   HOH C 402       1.635  15.962  33.011  1.00 34.96           O  
-HETATM 6791  O   HOH C 403       2.813   6.511  22.406  1.00 34.91           O  
-HETATM 6792  O   HOH C 404      -5.163  10.541  38.929  1.00 44.85           O  
-HETATM 6793  O   HOH C 405       3.050  10.694  31.284  1.00 32.10           O  
-HETATM 6794  O   HOH C 406       4.693   9.655   6.385  1.00 38.94           O  
-HETATM 6795  O   HOH C 407       2.570  14.206  31.073  1.00 38.56           O  
-HETATM 6796  O   HOH C 408      -3.653  14.581   8.560  1.00 37.52           O  
-HETATM 6797  O   HOH C 409     -14.122  16.562  10.177  1.00 34.83           O  
-HETATM 6798  O   HOH C 410      -7.275 -12.382  21.429  1.00 38.57           O  
-HETATM 6799  O   HOH C 411       6.548   9.696  28.325  1.00 35.13           O  
-HETATM 6800  O   HOH C 412       3.720   3.362  33.995  1.00 41.27           O  
-HETATM 6801  O   HOH C 413      -0.163  10.390  37.550  1.00 44.89           O  
-HETATM 6802  O   HOH C 414       7.056  14.930   4.000  1.00 36.81           O  
-HETATM 6803  O   HOH C 415       2.481   4.827  35.892  1.00 46.81           O  
-HETATM 6804  O   HOH C 416     -14.101  19.608  11.498  1.00 48.24           O  
-HETATM 6805  O   HOH C 417      -6.981   4.232   9.656  1.00 39.96           O  
-HETATM 6806  O   HOH C 418       3.169  13.347  38.128  1.00 45.87           O  
-HETATM 6807  O   HOH C 419      -7.308  18.439  20.543  1.00 39.67           O  
-HETATM 6808  O   HOH C 420      -4.916   6.929   8.288  1.00 43.07           O  
-HETATM 6809  O   HOH C 421       3.857   5.917  32.232  1.00 38.33           O  
-HETATM 6810  O   HOH C 422      -9.222   9.218  39.865  1.00 42.85           O  
-HETATM 6811  O   HOH C 423       0.677 -14.588  20.041  1.00 46.44           O  
-HETATM 6812  O   HOH C 424       4.464  -8.197  21.195  1.00 38.98           O  
-HETATM 6813  O   HOH C 425     -12.387  16.686   8.286  1.00 45.27           O  
-HETATM 6814  O   HOH C 426      -9.396  10.443  10.624  1.00 36.27           O  
-HETATM 6815  O   HOH C 427      -6.860  19.362  17.887  1.00 38.18           O  
-HETATM 6816  O   HOH C 428     -17.161   6.029  25.009  1.00 55.16           O  
-HETATM 6817  O   HOH C 429       0.573  -5.969  19.114  1.00 36.33           O  
-HETATM 6818  O   HOH C 430     -19.731   7.780  24.217  1.00 56.89           O  
-HETATM 6819  O   HOH C 431     -16.141  12.919  21.751  1.00 42.49           O  
-HETATM 6820  O   HOH C 432      10.873   2.374  34.640  1.00 61.69           O  
-HETATM 6821  O   HOH C 433      11.619  33.828  22.456  1.00 54.18           O  
-HETATM 6822  O   HOH C 434       1.579   2.478  15.064  1.00 33.13           O  
-HETATM 6823  O   HOH C 435      -1.854  -6.265  19.906  1.00 39.76           O  
-HETATM 6824  O   HOH C 436       4.295   1.589  35.741  1.00 47.42           O  
-HETATM 6825  O   HOH C 437      -1.529  13.027   7.233  1.00 41.62           O  
-HETATM 6826  O   HOH C 438       5.162   5.721  35.219  1.00 57.38           O  
-HETATM 6827  O   HOH C 439       3.332 -16.913  24.752  1.00 53.04           O  
-HETATM 6828  O   HOH C 440      10.201  10.638  30.798  1.00 46.98           O  
-HETATM 6829  O   HOH C 441       4.486  25.097  34.091  1.00 50.52           O  
-HETATM 6830  O   HOH C 442       0.645  23.994   3.676  1.00 64.08           O  
-HETATM 6831  O   HOH C 443      -9.780  17.547  16.498  1.00 48.77           O  
-HETATM 6832  O   HOH C 444      -2.493 -14.174  19.509  1.00 44.26           O  
-HETATM 6833  O   HOH C 445       9.887  -1.063  28.028  1.00 46.58           O  
-HETATM 6834  O   HOH C 446       4.872  20.001  -0.319  1.00 75.11           O  
-HETATM 6835  O   HOH C 447      18.298  12.100  23.921  1.00 55.46           O  
-HETATM 6836  O   HOH C 448       6.007  11.907  30.780  1.00 43.65           O  
-HETATM 6837  O   HOH C 449       8.209  11.052  31.886  1.00 58.64           O  
-HETATM 6838  O   HOH C 450       5.937   9.684  30.549  1.00 57.32           O  
-HETATM 6839  O   HOH C 451       4.537   8.021  30.284  1.00 38.58           O  
-HETATM 6840  O   HOH C 452       6.895   3.469  34.081  1.00 60.93           O  
-HETATM 6841  O   HOH C 453       6.953   5.881  33.941  1.00 81.26           O  
-HETATM 6842  O   HOH D 401     -23.433  -4.534  -1.203  1.00 37.81           O  
-HETATM 6843  O   HOH D 402     -18.933   6.530  -4.292  1.00 33.33           O  
-HETATM 6844  O   HOH D 403     -15.950  -3.272   1.572  1.00 29.54           O  
-HETATM 6845  O   HOH D 404      -5.664  -7.416  -1.515  1.00 29.90           O  
-HETATM 6846  O   HOH D 405     -27.223 -11.794   2.109  1.00 30.50           O  
-HETATM 6847  O   HOH D 406     -19.911   3.947  -6.880  1.00 33.94           O  
-HETATM 6848  O   HOH D 407      -8.761 -27.419   4.266  1.00 35.75           O  
-HETATM 6849  O   HOH D 408      -4.755  -0.751  12.922  1.00 37.43           O  
-HETATM 6850  O   HOH D 409       1.831 -13.506   0.831  1.00 37.34           O  
-HETATM 6851  O   HOH D 410     -24.925  -6.879   0.361  1.00 43.00           O  
-HETATM 6852  O   HOH D 411      -6.541  -6.758  15.826  1.00 36.26           O  
-HETATM 6853  O   HOH D 412     -11.917   9.022   3.464  1.00 29.81           O  
-HETATM 6854  O   HOH D 413     -16.675 -14.010  13.222  1.00 35.07           O  
-HETATM 6855  O   HOH D 414       5.445 -18.660   3.707  1.00 38.79           O  
-HETATM 6856  O   HOH D 415     -18.451 -25.781   3.562  1.00 41.71           O  
-HETATM 6857  O   HOH D 416      -2.247 -10.334   9.034  1.00 31.96           O  
-HETATM 6858  O   HOH D 417      -8.564   0.450   3.729  1.00 43.74           O  
-HETATM 6859  O   HOH D 418     -12.764 -13.000  16.178  1.00 46.54           O  
-HETATM 6860  O   HOH D 419      -6.726 -15.625  -9.362  1.00 35.98           O  
-HETATM 6861  O   HOH D 420      -8.489 -25.785   6.150  1.00 39.61           O  
-HETATM 6862  O   HOH D 421     -25.324 -10.073   1.328  1.00 38.09           O  
-HETATM 6863  O   HOH D 422      -0.145  -8.007   2.246  1.00 37.08           O  
-HETATM 6864  O   HOH D 423     -18.973  -7.216  20.875  1.00 40.13           O  
-HETATM 6865  O   HOH D 424      -3.845 -11.568  10.929  1.00 34.88           O  
-HETATM 6866  O   HOH D 425     -26.783   0.697  -1.277  1.00 42.87           O  
-HETATM 6867  O   HOH D 426       4.283 -20.579  10.894  1.00 52.54           O  
-HETATM 6868  O   HOH D 427      -3.620  -3.940  11.752  1.00 45.34           O  
-HETATM 6869  O   HOH D 428     -14.152 -15.122  13.142  1.00 38.76           O  
-HETATM 6870  O   HOH D 429     -26.789 -19.632   8.406  1.00 47.29           O  
-HETATM 6871  O   HOH D 430      -5.281 -13.132  19.782  1.00 47.94           O  
-HETATM 6872  O   HOH D 431     -28.672   2.806  -2.242  1.00 47.44           O  
-HETATM 6873  O   HOH D 432     -32.010  -8.850  -0.845  1.00 47.67           O  
-HETATM 6874  O   HOH D 433     -13.025  10.720  -0.588  1.00 38.55           O  
-HETATM 6875  O   HOH D 434     -28.803 -21.421   0.040  1.00 45.18           O  
-HETATM 6876  O   HOH D 435     -28.145  -3.223  21.441  1.00 58.47           O  
-HETATM 6877  O   HOH D 436     -22.403 -15.423  12.456  1.00 51.31           O  
-HETATM 6878  O   HOH D 437     -31.748  -2.602   5.676  1.00 56.07           O  
-HETATM 6879  O   HOH D 438     -22.188 -20.045   5.413  1.00 47.48           O  
-HETATM 6880  O   HOH D 439     -31.600   4.619   8.440  1.00 52.41           O  
-HETATM 6881  O   HOH D 440      -4.673 -23.669   8.606  1.00 55.66           O  
-HETATM 6882  O   HOH D 441     -19.172  18.673  15.915  1.00 49.55           O  
-HETATM 6883  O   HOH D 442     -24.281 -21.451 -13.546  1.00 55.78           O  
-HETATM 6884  O   HOH D 443      -0.294  -5.429   1.187  1.00 51.06           O  
-HETATM 6885  O   HOH D 444     -23.913 -13.482  12.955  1.00 53.07           O  
-HETATM 6886  O   HOH D 445     -21.686  -6.298  -2.486  1.00 36.64           O  
-HETATM 6887  O   HOH D 446     -26.329   0.263  -5.030  1.00 53.49           O  
-HETATM 6888  O   HOH D 447     -24.178  -7.868  -2.229  1.00 49.33           O  
-CONECT  910 6568                                                                
-CONECT  911 6568                                                                
-CONECT  918 6568                                                                
-CONECT 1385 6569                                                                
-CONECT 2539 6626                                                                
-CONECT 2540 6626                                                                
-CONECT 2542 6626                                                                
-CONECT 2551 6626                                                                
-CONECT 3021 6627                                                                
-CONECT 4172 6656                                                                
-CONECT 4180 6656                                                                
-CONECT 4653 6657                                                                
-CONECT 5847 6686                                                                
-CONECT 5855 6686                                                                
-CONECT 6332 6687                                                                
-CONECT 6540 6541 6569                                                           
-CONECT 6541 6540 6542 6543 6544                                                 
-CONECT 6542 6541                                                                
-CONECT 6543 6541                                                                
-CONECT 6544 6541 6545                                                           
-CONECT 6545 6544 6546                                                           
-CONECT 6546 6545 6547                                                           
-CONECT 6547 6546 6548                                                           
-CONECT 6548 6547 6549                                                           
-CONECT 6549 6548 6550 6556                                                      
-CONECT 6550 6549 6551                                                           
-CONECT 6551 6550 6552                                                           
-CONECT 6552 6551 6553 6554 6555                                                 
-CONECT 6553 6552                                                                
-CONECT 6554 6552                                                                
-CONECT 6555 6552                                                                
-CONECT 6556 6549 6557                                                           
-CONECT 6557 6556 6558                                                           
-CONECT 6558 6557 6559 6567                                                      
-CONECT 6559 6558 6560 6565                                                      
-CONECT 6560 6559 6561                                                           
-CONECT 6561 6560 6562                                                           
-CONECT 6562 6561 6563                                                           
-CONECT 6563 6562 6564 6565                                                      
-CONECT 6564 6563                                                                
-CONECT 6565 6559 6563 6566                                                      
-CONECT 6566 6565 6567                                                           
-CONECT 6567 6558 6566                                                           
-CONECT 6568  910  911  918 6705                                                 
-CONECT 6568 6713 6736 6737                                                      
-CONECT 6569 1385 6540 6738 6739                                                 
-CONECT 6570 6572                                                                
-CONECT 6571 6573                                                                
-CONECT 6572 6570 6574 6576 6578                                                 
-CONECT 6573 6571 6575 6577 6579                                                 
-CONECT 6574 6572                                                                
-CONECT 6575 6573 6627                                                           
-CONECT 6576 6572                                                                
-CONECT 6577 6573                                                                
-CONECT 6578 6572 6580                                                           
-CONECT 6579 6573 6581                                                           
-CONECT 6580 6578 6582                                                           
-CONECT 6581 6579 6583                                                           
-CONECT 6582 6580 6584                                                           
-CONECT 6583 6581 6585 6626                                                      
-CONECT 6584 6582 6586                                                           
-CONECT 6585 6583 6587                                                           
-CONECT 6586 6584 6588                                                           
-CONECT 6587 6585 6589                                                           
-CONECT 6588 6586 6590 6602                                                      
-CONECT 6589 6587 6591 6603                                                      
-CONECT 6590 6588 6592                                                           
-CONECT 6591 6589 6593                                                           
-CONECT 6592 6590 6594                                                           
-CONECT 6593 6591 6595                                                           
-CONECT 6594 6592 6596 6598 6600                                                 
-CONECT 6595 6593 6597 6599 6601                                                 
-CONECT 6596 6594                                                                
-CONECT 6597 6595                                                                
-CONECT 6598 6594                                                                
-CONECT 6599 6595                                                                
-CONECT 6600 6594                                                                
-CONECT 6601 6595                                                                
-CONECT 6602 6588 6604                                                           
-CONECT 6603 6589 6605                                                           
-CONECT 6604 6602 6606                                                           
-CONECT 6605 6603 6607                                                           
-CONECT 6606 6604 6608 6624                                                      
-CONECT 6607 6605 6609 6625                                                      
-CONECT 6608 6606 6610 6620                                                      
-CONECT 6609 6607 6611 6621                                                      
-CONECT 6610 6608 6612                                                           
-CONECT 6611 6609 6613                                                           
-CONECT 6612 6610 6614                                                           
-CONECT 6613 6611 6615                                                           
-CONECT 6614 6612 6616                                                           
-CONECT 6615 6613 6617                                                           
-CONECT 6616 6614 6618 6620                                                      
-CONECT 6617 6615 6619 6621                                                      
-CONECT 6618 6616                                                                
-CONECT 6619 6617                                                                
-CONECT 6620 6608 6616 6622                                                      
-CONECT 6621 6609 6617 6623                                                      
-CONECT 6622 6620 6624                                                           
-CONECT 6623 6621 6625                                                           
-CONECT 6624 6606 6622                                                           
-CONECT 6625 6607 6623                                                           
-CONECT 6626 2539 2540 2542 2551                                                 
-CONECT 6626 6583                                                                
-CONECT 6627 3021 6575 6761 6786                                                 
-CONECT 6627 6787 6788                                                           
-CONECT 6628 6629                                                                
-CONECT 6629 6628 6630 6631 6632                                                 
-CONECT 6630 6629                                                                
-CONECT 6631 6629 6657                                                           
-CONECT 6632 6629 6633                                                           
-CONECT 6633 6632 6634                                                           
-CONECT 6634 6633 6635                                                           
-CONECT 6635 6634 6636                                                           
-CONECT 6636 6635 6637                                                           
-CONECT 6637 6636 6638 6644                                                      
-CONECT 6638 6637 6639                                                           
-CONECT 6639 6638 6640                                                           
-CONECT 6640 6639 6641 6642 6643                                                 
-CONECT 6641 6640                                                                
-CONECT 6642 6640                                                                
-CONECT 6643 6640                                                                
-CONECT 6644 6637 6645                                                           
-CONECT 6645 6644 6646                                                           
-CONECT 6646 6645 6647 6655                                                      
-CONECT 6647 6646 6648 6653                                                      
-CONECT 6648 6647 6649                                                           
-CONECT 6649 6648 6650                                                           
-CONECT 6650 6649 6651                                                           
-CONECT 6651 6650 6652 6653                                                      
-CONECT 6652 6651                                                                
-CONECT 6653 6647 6651 6654                                                      
-CONECT 6654 6653 6655                                                           
-CONECT 6655 6646 6654                                                           
-CONECT 6656 4172 4180 6793 6799                                                 
-CONECT 6656 6836 6838 6839                                                      
-CONECT 6657 4653 6631 6800 6809                                                 
-CONECT 6657 6826 6840 6841                                                      
-CONECT 6658 6659                                                                
-CONECT 6659 6658 6660 6661 6662                                                 
-CONECT 6660 6659 6687                                                           
-CONECT 6661 6659                                                                
-CONECT 6662 6659 6663                                                           
-CONECT 6663 6662 6664                                                           
-CONECT 6664 6663 6665                                                           
-CONECT 6665 6664 6666                                                           
-CONECT 6666 6665 6667                                                           
-CONECT 6667 6666 6668 6674                                                      
-CONECT 6668 6667 6669                                                           
-CONECT 6669 6668 6670                                                           
-CONECT 6670 6669 6671 6672 6673                                                 
-CONECT 6671 6670                                                                
-CONECT 6672 6670                                                                
-CONECT 6673 6670                                                                
-CONECT 6674 6667 6675                                                           
-CONECT 6675 6674 6676                                                           
-CONECT 6676 6675 6677 6685                                                      
-CONECT 6677 6676 6678 6683                                                      
-CONECT 6678 6677 6679                                                           
-CONECT 6679 6678 6680                                                           
-CONECT 6680 6679 6681                                                           
-CONECT 6681 6680 6682 6683                                                      
-CONECT 6682 6681                                                                
-CONECT 6683 6677 6681 6684                                                      
-CONECT 6684 6683 6685                                                           
-CONECT 6685 6676 6684                                                           
-CONECT 6686 5847 5855 6842 6851                                                 
-CONECT 6686 6886 6888                                                           
-CONECT 6687 6332 6660 6866 6887                                                 
-CONECT 6705 6568                                                                
-CONECT 6713 6568                                                                
-CONECT 6736 6568                                                                
-CONECT 6737 6568                                                                
-CONECT 6738 6569                                                                
-CONECT 6739 6569                                                                
-CONECT 6761 6627                                                                
-CONECT 6786 6627                                                                
-CONECT 6787 6627                                                                
-CONECT 6788 6627                                                                
-CONECT 6793 6656                                                                
-CONECT 6799 6656                                                                
-CONECT 6800 6657                                                                
-CONECT 6809 6657                                                                
-CONECT 6826 6657                                                                
-CONECT 6836 6656                                                                
-CONECT 6838 6656                                                                
-CONECT 6839 6656                                                                
-CONECT 6840 6657                                                                
-CONECT 6841 6657                                                                
-CONECT 6842 6686                                                                
-CONECT 6851 6686                                                                
-CONECT 6866 6687                                                                
-CONECT 6886 6686                                                                
-CONECT 6887 6687                                                                
-CONECT 6888 6686                                                                
-MASTER      991    0   12   29   38    0   36    6 6682    4  195   68          
-END                                                                             
diff --git a/plip/test/pdb/4rdl.pdb b/plip/test/pdb/4rdl.pdb
deleted file mode 100644
index 36f6cfe..0000000
--- a/plip/test/pdb/4rdl.pdb
+++ /dev/null
@@ -1,11637 +0,0 @@
-HEADER    VIRAL PROTEIN                           19-SEP-14   4RDL              
-TITLE     CRYSTAL STRUCTURE OF NOROVIRUS BOXER P DOMAIN IN COMPLEX WITH LEWIS Y 
-TITLE    2 TETRASACCHARIDE                                                      
-COMPND    MOL_ID: 1;                                                            
-COMPND   2 MOLECULE: CAPSID;                                                    
-COMPND   3 CHAIN: A, B;                                                         
-COMPND   4 FRAGMENT: PROTRUSION DOMAIN, UNP RESIDUES 227-526;                   
-COMPND   5 ENGINEERED: YES                                                      
-SOURCE    MOL_ID: 1;                                                            
-SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN CALICIVIRUS NLV/BOXER/2001/US;            
-SOURCE   3 ORGANISM_TAXID: 207658;                                              
-SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
-SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
-SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
-SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
-KEYWDS    MIXED ALPHA/BETA STRUCTURE, RECEPTOR BINDING, HBGA, VIRUS CAPSID,     
-KEYWDS   2 VIRAL PROTEIN                                                        
-EXPDTA    X-RAY DIFFRACTION                                                     
-AUTHOR    N.HAO,Y.CHEN,M.XIA,W.LIU,M.TAN,X.JIANG,X.LI                           
-REVDAT   1   14-JAN-15 4RDL    0                                                
-JRNL        AUTH   N.HAO,Y.CHEN,M.XIA,M.TAN,W.LIU,X.GUAN,X.JIANG,X.LI,Z.RAO     
-JRNL        TITL   CRYSTAL STRUCTURES OF GI.8 BOXER VIRUS P DIMERS IN COMPLEX   
-JRNL        TITL 2 WITH HBGAS, A NOVEL EVOLUTIONARY PATH SELECTED BY THE LEWIS  
-JRNL        TITL 3 EPITOPE                                                      
-JRNL        REF    PROTEIN CELL                               2014              
-JRNL        REFN                   ESSN 1674-8018                               
-JRNL        PMID   25547362                                                     
-JRNL        DOI    10.1007/S13238-014-0126-0                                    
-REMARK   2                                                                      
-REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
-REMARK   3                                                                      
-REMARK   3 REFINEMENT.                                                          
-REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
-REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
-REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
-REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
-REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
-REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
-REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
-REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
-REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
-REMARK   3               : ZWART                                                
-REMARK   3                                                                      
-REMARK   3    REFINEMENT TARGET : ML                                            
-REMARK   3                                                                      
-REMARK   3  DATA USED IN REFINEMENT.                                            
-REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
-REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.70                          
-REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
-REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
-REMARK   3   NUMBER OF REFLECTIONS             : 129411                         
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
-REMARK   3   R VALUE     (WORKING + TEST SET) : 0.131                           
-REMARK   3   R VALUE            (WORKING SET) : 0.130                           
-REMARK   3   FREE R VALUE                     : 0.151                           
-REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
-REMARK   3   FREE R VALUE TEST SET COUNT      : 6496                            
-REMARK   3                                                                      
-REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
-REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
-REMARK   3     1 47.7266 -  4.5013    1.00     4215   228  0.1669 0.1666        
-REMARK   3     2  4.5013 -  3.5732    1.00     4159   217  0.1332 0.1392        
-REMARK   3     3  3.5732 -  3.1216    1.00     4130   213  0.1385 0.1473        
-REMARK   3     4  3.1216 -  2.8362    1.00     4125   211  0.1456 0.1668        
-REMARK   3     5  2.8362 -  2.6330    1.00     4142   220  0.1482 0.1574        
-REMARK   3     6  2.6330 -  2.4777    1.00     4087   216  0.1407 0.1605        
-REMARK   3     7  2.4777 -  2.3536    1.00     4137   213  0.1335 0.1483        
-REMARK   3     8  2.3536 -  2.2512    1.00     4067   217  0.1226 0.1546        
-REMARK   3     9  2.2512 -  2.1645    1.00     4134   203  0.1246 0.1293        
-REMARK   3    10  2.1645 -  2.0898    1.00     4082   216  0.1285 0.1517        
-REMARK   3    11  2.0898 -  2.0245    1.00     4107   209  0.1233 0.1446        
-REMARK   3    12  2.0245 -  1.9666    1.00     4103   207  0.1250 0.1678        
-REMARK   3    13  1.9666 -  1.9148    1.00     4065   230  0.1196 0.1582        
-REMARK   3    14  1.9148 -  1.8681    1.00     4088   236  0.1168 0.1467        
-REMARK   3    15  1.8681 -  1.8257    1.00     4095   211  0.1045 0.1168        
-REMARK   3    16  1.8257 -  1.7868    1.00     4117   201  0.0988 0.1366        
-REMARK   3    17  1.7868 -  1.7511    1.00     4057   245  0.0995 0.1272        
-REMARK   3    18  1.7511 -  1.7180    1.00     4032   238  0.0954 0.1247        
-REMARK   3    19  1.7180 -  1.6873    1.00     4101   236  0.0950 0.1404        
-REMARK   3    20  1.6873 -  1.6587    1.00     4055   229  0.0992 0.1537        
-REMARK   3    21  1.6587 -  1.6320    1.00     4033   211  0.1037 0.1392        
-REMARK   3    22  1.6320 -  1.6069    1.00     4174   183  0.1037 0.1389        
-REMARK   3    23  1.6069 -  1.5832    1.00     4042   218  0.1086 0.1504        
-REMARK   3    24  1.5832 -  1.5609    1.00     4070   228  0.1116 0.1621        
-REMARK   3    25  1.5609 -  1.5398    1.00     4101   207  0.1111 0.1568        
-REMARK   3    26  1.5398 -  1.5198    1.00     4095   193  0.1157 0.1512        
-REMARK   3    27  1.5198 -  1.5008    1.00     4080   215  0.1188 0.1718        
-REMARK   3    28  1.5008 -  1.4828    1.00     4073   213  0.1232 0.1458        
-REMARK   3    29  1.4828 -  1.4655    1.00     4096   223  0.1307 0.1737        
-REMARK   3    30  1.4655 -  1.4490    1.00     4053   209  0.1532 0.1929        
-REMARK   3                                                                      
-REMARK   3  BULK SOLVENT MODELLING.                                             
-REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
-REMARK   3   SOLVENT RADIUS     : 1.10                                          
-REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
-REMARK   3   K_SOL              : 0.33                                          
-REMARK   3   B_SOL              : 38.40                                         
-REMARK   3                                                                      
-REMARK   3  ERROR ESTIMATES.                                                    
-REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
-REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.430           
-REMARK   3                                                                      
-REMARK   3  B VALUES.                                                           
-REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
-REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.10                          
-REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
-REMARK   3    B11 (A**2) : 1.62560                                              
-REMARK   3    B22 (A**2) : 1.62560                                              
-REMARK   3    B33 (A**2) : -3.25120                                             
-REMARK   3    B12 (A**2) : -0.00000                                             
-REMARK   3    B13 (A**2) : -0.00000                                             
-REMARK   3    B23 (A**2) : -0.00000                                             
-REMARK   3                                                                      
-REMARK   3  TWINNING INFORMATION.                                               
-REMARK   3   FRACTION: NULL                                                     
-REMARK   3   OPERATOR: NULL                                                     
-REMARK   3                                                                      
-REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
-REMARK   3                 RMSD          COUNT                                  
-REMARK   3   BOND      :  0.006           4822                                  
-REMARK   3   ANGLE     :  1.140           6612                                  
-REMARK   3   CHIRALITY :  0.075            746                                  
-REMARK   3   PLANARITY :  0.005            870                                  
-REMARK   3   DIHEDRAL  : 11.841           1702                                  
-REMARK   3                                                                      
-REMARK   3  TLS DETAILS                                                         
-REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
-REMARK   3                                                                      
-REMARK   3  NCS DETAILS                                                         
-REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
-REMARK   3                                                                      
-REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
-REMARK   4                                                                      
-REMARK   4 4RDL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
-REMARK 100                                                                      
-REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-14.                  
-REMARK 100 THE RCSB ID CODE IS RCSB087213.                                      
-REMARK 200                                                                      
-REMARK 200 EXPERIMENTAL DETAILS                                                 
-REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
-REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-12                          
-REMARK 200  TEMPERATURE           (KELVIN) : 100                                
-REMARK 200  PH                             : 7.5                                
-REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
-REMARK 200                                                                      
-REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
-REMARK 200  RADIATION SOURCE               : SSRF                               
-REMARK 200  BEAMLINE                       : BL17U                              
-REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
-REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
-REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
-REMARK 200  MONOCHROMATOR                  : SI(111)                            
-REMARK 200  OPTICS                         : MIRRORS                            
-REMARK 200                                                                      
-REMARK 200  DETECTOR TYPE                  : CCD                                
-REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
-REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
-REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
-REMARK 200                                                                      
-REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129481                             
-REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.449                              
-REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
-REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
-REMARK 200                                                                      
-REMARK 200 OVERALL.                                                             
-REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
-REMARK 200  DATA REDUNDANCY                : 11.100                             
-REMARK 200  R MERGE                    (I) : 0.09500                            
-REMARK 200  R SYM                      (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.7000                            
-REMARK 200                                                                      
-REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
-REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
-REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
-REMARK 200  DATA REDUNDANCY IN SHELL       : 11.00                              
-REMARK 200  R MERGE FOR SHELL          (I) : 0.47300                            
-REMARK 200  R SYM FOR SHELL            (I) : NULL                               
-REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.100                              
-REMARK 200                                                                      
-REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
-REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
-REMARK 200 SOFTWARE USED: PHASER                                                
-REMARK 200 STARTING MODEL: PDB ENTRY 4RDJ                                       
-REMARK 200                                                                      
-REMARK 200 REMARK: NULL                                                         
-REMARK 280                                                                      
-REMARK 280 CRYSTAL                                                              
-REMARK 280 SOLVENT CONTENT, VS   (%): 55.10                                     
-REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
-REMARK 280                                                                      
-REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M LICL, 18%(W/V) PEG 3350, 10%(V/V)   
-REMARK 280  MPD, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K        
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
-REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
-REMARK 290                                                                      
-REMARK 290      SYMOP   SYMMETRY                                                
-REMARK 290     NNNMMM   OPERATOR                                                
-REMARK 290       1555   X,Y,Z                                                   
-REMARK 290       2555   -Y,X-Y,Z+1/3                                            
-REMARK 290       3555   -X+Y,-X,Z+2/3                                           
-REMARK 290       4555   -X,-Y,Z+1/2                                             
-REMARK 290       5555   Y,-X+Y,Z+5/6                                            
-REMARK 290       6555   X-Y,X,Z+1/6                                             
-REMARK 290                                                                      
-REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
-REMARK 290           MMM -> TRANSLATION VECTOR                                  
-REMARK 290                                                                      
-REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
-REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
-REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
-REMARK 290 RELATED MOLECULES.                                                   
-REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       21.67333            
-REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.34667            
-REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
-REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
-REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       32.51000            
-REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       54.18333            
-REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
-REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
-REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       10.83667            
-REMARK 290                                                                      
-REMARK 290 REMARK: NULL                                                         
-REMARK 300                                                                      
-REMARK 300 BIOMOLECULE: 1                                                       
-REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
-REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
-REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
-REMARK 300 BURIED SURFACE AREA.                                                 
-REMARK 350                                                                      
-REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
-REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
-REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
-REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
-REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
-REMARK 350                                                                      
-REMARK 350 BIOMOLECULE: 1                                                       
-REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
-REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
-REMARK 350 SOFTWARE USED: PISA                                                  
-REMARK 350 TOTAL BURIED SURFACE AREA: 6210 ANGSTROM**2                          
-REMARK 350 SURFACE AREA OF THE COMPLEX: 22860 ANGSTROM**2                       
-REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL                          
-REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
-REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
-REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
-REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
-REMARK 465                                                                      
-REMARK 465 MISSING RESIDUES                                                     
-REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
-REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
-REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
-REMARK 465                                                                      
-REMARK 465   M RES C SSSEQI                                                     
-REMARK 465     GLY A   219                                                      
-REMARK 465     PRO A   220                                                      
-REMARK 465     LEU A   221                                                      
-REMARK 465     GLY A   222                                                      
-REMARK 465     SER A   223                                                      
-REMARK 465     PRO A   224                                                      
-REMARK 465     GLU A   225                                                      
-REMARK 465     PHE A   226                                                      
-REMARK 465     GLN A   227                                                      
-REMARK 465     ARG A   228                                                      
-REMARK 465     THR A   229                                                      
-REMARK 465     GLY B   219                                                      
-REMARK 465     PRO B   220                                                      
-REMARK 465     LEU B   221                                                      
-REMARK 465     GLY B   222                                                      
-REMARK 465     SER B   223                                                      
-REMARK 465     PRO B   224                                                      
-REMARK 465     GLU B   225                                                      
-REMARK 465     PHE B   226                                                      
-REMARK 465     GLN B   227                                                      
-REMARK 465     ARG B   228                                                      
-REMARK 465     THR B   229                                                      
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
-REMARK 500                                                                      
-REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
-REMARK 500                                                                      
-REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
-REMARK 500   O    HOH B  1060     O    HOH B  1104              1.87            
-REMARK 500   O    HOH B  1024     O    HOH B  1051              1.88            
-REMARK 500   O    HOH B  1039     O    HOH B  1047              1.89            
-REMARK 500   O    HOH B  1107     O    HOH B  1111              1.89            
-REMARK 500   O    HOH A   878     O    HOH A  1052              1.96            
-REMARK 500   O    HOH A   737     O    HOH A   967              2.00            
-REMARK 500   O    HOH A  1095     O    HOH A  1101              2.03            
-REMARK 500   O    HOH B  1064     O    HOH B  1070              2.03            
-REMARK 500   O    HOH A  1043     O    HOH A  1057              2.05            
-REMARK 500   O    HOH B  1057     O    HOH B  1062              2.05            
-REMARK 500   O    HOH B  1046     O    HOH B  1111              2.06            
-REMARK 500   O    HOH B  1028     O    HOH B  1043              2.06            
-REMARK 500   O    HOH B  1017     O    HOH B  1066              2.06            
-REMARK 500   O    HOH B   758     O    HOH B  1104              2.13            
-REMARK 500   O    HOH B  1034     O    HOH B  1067              2.15            
-REMARK 500   OE1  GLU B   385     O    HOH B   976              2.17            
-REMARK 500   O    HOH A  1082     O    HOH B  1101              2.17            
-REMARK 500   O    HOH A  1078     O    HOH B  1081              2.17            
-REMARK 500   O    HOH A   966     O    HOH A  1056              2.18            
-REMARK 500   OE1  GLU A   377     O    HOH A   862              2.19            
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 500                                                                      
-REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
-REMARK 500 SUBTOPIC: TORSION ANGLES                                             
-REMARK 500                                                                      
-REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
-REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
-REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
-REMARK 500                                                                      
-REMARK 500 STANDARD TABLE:                                                      
-REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
-REMARK 500                                                                      
-REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
-REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
-REMARK 500                                                                      
-REMARK 500  M RES CSSEQI        PSI       PHI                                   
-REMARK 500    ASN A 236       58.32    -93.38                                   
-REMARK 500    GLN A 265       49.70   -141.79                                   
-REMARK 500    THR A 282     -168.51   -130.00                                   
-REMARK 500    SER A 358       53.71    -90.79                                   
-REMARK 500    ASP A 360      158.65     74.59                                   
-REMARK 500    SER A 411     -139.32     54.27                                   
-REMARK 500    SER A 443      -15.51     91.05                                   
-REMARK 500    ASN A 444       74.77   -156.62                                   
-REMARK 500    PRO A 445       43.30    -83.29                                   
-REMARK 500    ASN B 236       55.75    -90.67                                   
-REMARK 500    GLN B 265       51.40   -143.07                                   
-REMARK 500    ASP B 360      159.38     74.64                                   
-REMARK 500    LEU B 413     -116.33     46.02                                   
-REMARK 500    SER B 443       -6.74     91.47                                   
-REMARK 500    ASN B 444       66.22   -162.92                                   
-REMARK 500    PRO B 445       43.46    -84.12                                   
-REMARK 500    ASN B 500     -159.18   -122.67                                   
-REMARK 500    ALA B 501      -71.43    -55.33                                   
-REMARK 500                                                                      
-REMARK 500 REMARK: NULL                                                         
-REMARK 525                                                                      
-REMARK 525 SOLVENT                                                              
-REMARK 525                                                                      
-REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
-REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
-REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
-REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
-REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
-REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
-REMARK 525 NUMBER; I=INSERTION CODE):                                           
-REMARK 525                                                                      
-REMARK 525  M RES CSSEQI                                                        
-REMARK 525    HOH A1073        DISTANCE =  5.02 ANGSTROMS                       
-REMARK 800                                                                      
-REMARK 800 SITE                                                                 
-REMARK 800 SITE_IDENTIFIER: AC1                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
-REMARK 800  RESIDUES 601 TO 604                                                 
-REMARK 800                                                                      
-REMARK 800 SITE_IDENTIFIER: AC2                                                 
-REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
-REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF POLYSACCHARIDE         
-REMARK 800  RESIDUES 601 TO 604                                                 
-REMARK 900                                                                      
-REMARK 900 RELATED ENTRIES                                                      
-REMARK 900 RELATED ID: 4RDJ   RELATED DB: PDB                                   
-REMARK 900 RELATED ID: 4RDK   RELATED DB: PDB                                   
-DBREF  4RDL A  227   526  UNP    Q8BCA3   Q8BCA3_9CALI   227    526             
-DBREF  4RDL B  227   526  UNP    Q8BCA3   Q8BCA3_9CALI   227    526             
-SEQADV 4RDL GLY A  219  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL PRO A  220  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL LEU A  221  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL GLY A  222  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL SER A  223  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL PRO A  224  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL GLU A  225  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL PHE A  226  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL GLY B  219  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL PRO B  220  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL LEU B  221  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL GLY B  222  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL SER B  223  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL PRO B  224  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL GLU B  225  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQADV 4RDL PHE B  226  UNP  Q8BCA3              EXPRESSION TAG                 
-SEQRES   1 A  308  GLY PRO LEU GLY SER PRO GLU PHE GLN ARG THR LYS PRO          
-SEQRES   2 A  308  PHE SER VAL PRO ASN ILE PRO MET ASN LEU MET SER ASN          
-SEQRES   3 A  308  SER ARG VAL PRO MET LEU ILE ASP GLY MET MET VAL SER          
-SEQRES   4 A  308  ASN ASP GLN ASN GLN VAL PRO GLN PHE GLN ASN GLY ARG          
-SEQRES   5 A  308  VAL THR LEU ASP GLY GLN LEU GLN GLY THR THR THR VAL          
-SEQRES   6 A  308  SER ALA ALA CYS ILE ALA ARG MET ARG GLY ARG ILE PHE          
-SEQRES   7 A  308  ASN ASN ASN GLY ASN TYR GLY VAL ASN LEU ALA GLU LEU          
-SEQRES   8 A  308  ASP GLY ASN PRO TYR HIS ALA PHE ASP SER PRO ALA PRO          
-SEQRES   9 A  308  LEU GLY PHE PRO ASP PHE GLY ASN CYS ASP LEU HIS MET          
-SEQRES  10 A  308  THR PHE VAL LYS ILE ASN PRO THR GLU LEU SER THR GLY          
-SEQRES  11 A  308  ASP PRO SER GLY LYS VAL VAL ILE HIS SER TYR ASP ALA          
-SEQRES  12 A  308  THR PHE ALA PRO HIS LEU GLY THR VAL LYS LEU GLU ASP          
-SEQRES  13 A  308  ASN ASN GLU LEU ASP GLN PHE VAL GLY LYS GLU VAL VAL          
-SEQRES  14 A  308  LEU GLU LEU THR TRP VAL SER ASN ARG THR GLY ALA THR          
-SEQRES  15 A  308  LEU ASN LEU TRP ALA VAL PRO ASN TYR GLY SER ASN LEU          
-SEQRES  16 A  308  THR GLN ALA SER GLN LEU ALA PRO PRO ILE TYR PRO PRO          
-SEQRES  17 A  308  GLY PHE GLY GLU ALA ILE VAL TYR PHE THR SER THR PHE          
-SEQRES  18 A  308  PRO THR VAL SER ASN PRO LYS VAL PRO CYS THR LEU PRO          
-SEQRES  19 A  308  GLN GLU PHE VAL SER HIS PHE VAL ASN GLU GLN ALA PRO          
-SEQRES  20 A  308  THR ARG GLY ASP ALA ALA LEU LEU HIS TYR VAL ASP PRO          
-SEQRES  21 A  308  ASP THR HIS ARG ASN LEU GLY GLU PHE LYS MET TYR PRO          
-SEQRES  22 A  308  GLU GLY TYR MET THR CYS VAL PRO ASN ALA GLY GLY GLY          
-SEQRES  23 A  308  PRO GLN THR LEU PRO ILE ASN GLY VAL PHE VAL PHE ILE          
-SEQRES  24 A  308  SER TRP VAL SER ARG TYR TYR GLN LEU                          
-SEQRES   1 B  308  GLY PRO LEU GLY SER PRO GLU PHE GLN ARG THR LYS PRO          
-SEQRES   2 B  308  PHE SER VAL PRO ASN ILE PRO MET ASN LEU MET SER ASN          
-SEQRES   3 B  308  SER ARG VAL PRO MET LEU ILE ASP GLY MET MET VAL SER          
-SEQRES   4 B  308  ASN ASP GLN ASN GLN VAL PRO GLN PHE GLN ASN GLY ARG          
-SEQRES   5 B  308  VAL THR LEU ASP GLY GLN LEU GLN GLY THR THR THR VAL          
-SEQRES   6 B  308  SER ALA ALA CYS ILE ALA ARG MET ARG GLY ARG ILE PHE          
-SEQRES   7 B  308  ASN ASN ASN GLY ASN TYR GLY VAL ASN LEU ALA GLU LEU          
-SEQRES   8 B  308  ASP GLY ASN PRO TYR HIS ALA PHE ASP SER PRO ALA PRO          
-SEQRES   9 B  308  LEU GLY PHE PRO ASP PHE GLY ASN CYS ASP LEU HIS MET          
-SEQRES  10 B  308  THR PHE VAL LYS ILE ASN PRO THR GLU LEU SER THR GLY          
-SEQRES  11 B  308  ASP PRO SER GLY LYS VAL VAL ILE HIS SER TYR ASP ALA          
-SEQRES  12 B  308  THR PHE ALA PRO HIS LEU GLY THR VAL LYS LEU GLU ASP          
-SEQRES  13 B  308  ASN ASN GLU LEU ASP GLN PHE VAL GLY LYS GLU VAL VAL          
-SEQRES  14 B  308  LEU GLU LEU THR TRP VAL SER ASN ARG THR GLY ALA THR          
-SEQRES  15 B  308  LEU ASN LEU TRP ALA VAL PRO ASN TYR GLY SER ASN LEU          
-SEQRES  16 B  308  THR GLN ALA SER GLN LEU ALA PRO PRO ILE TYR PRO PRO          
-SEQRES  17 B  308  GLY PHE GLY GLU ALA ILE VAL TYR PHE THR SER THR PHE          
-SEQRES  18 B  308  PRO THR VAL SER ASN PRO LYS VAL PRO CYS THR LEU PRO          
-SEQRES  19 B  308  GLN GLU PHE VAL SER HIS PHE VAL ASN GLU GLN ALA PRO          
-SEQRES  20 B  308  THR ARG GLY ASP ALA ALA LEU LEU HIS TYR VAL ASP PRO          
-SEQRES  21 B  308  ASP THR HIS ARG ASN LEU GLY GLU PHE LYS MET TYR PRO          
-SEQRES  22 B  308  GLU GLY TYR MET THR CYS VAL PRO ASN ALA GLY GLY GLY          
-SEQRES  23 B  308  PRO GLN THR LEU PRO ILE ASN GLY VAL PHE VAL PHE ILE          
-SEQRES  24 B  308  SER TRP VAL SER ARG TYR TYR GLN LEU                          
-HET    FUC  A 601      10                                                       
-HET    GAL  A 602      11                                                       
-HET    NDG  A 603      15                                                       
-HET    FUC  A 604      10                                                       
-HET    FUC  B 601      10                                                       
-HET    GAL  B 602      11                                                       
-HET    NDG  B 603      15                                                       
-HET    FUC  B 604      10                                                       
-HETNAM     FUC ALPHA-L-FUCOSE                                                   
-HETNAM     GAL BETA-D-GALACTOSE                                                 
-HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
-FORMUL   3  FUC    4(C6 H12 O5)                                                 
-FORMUL   3  GAL    2(C6 H12 O6)                                                 
-FORMUL   3  NDG    2(C8 H15 N O6)                                               
-FORMUL   5  HOH   *825(H2 O)                                                    
-HELIX    1   1 PRO A  238  MET A  242  5                                   5    
-HELIX    2   2 SER A  284  ILE A  288  5                                   5    
-HELIX    3   3 ASN A  341  LEU A  345  5                                   5    
-HELIX    4   4 PRO A  365  LEU A  367  5                                   3    
-HELIX    5   5 LEU A  378  VAL A  382  5                                   5    
-HELIX    6   6 PRO A  452  GLN A  463  1                                  12    
-HELIX    7   7 PRO B  238  MET B  242  5                                   5    
-HELIX    8   8 SER B  284  ILE B  288  5                                   5    
-HELIX    9   9 ASN B  341  LEU B  345  5                                   5    
-HELIX   10  10 PRO B  365  LEU B  367  5                                   3    
-HELIX   11  11 LEU B  378  VAL B  382  5                                   5    
-HELIX   12  12 PRO B  452  GLN B  463  1                                  12    
-HELIX   13  13 GLY B  504  LEU B  508  5                                   5    
-SHEET    1   A 3 GLY A 253  VAL A 256  0                                        
-SHEET    2   A 3 ALA A 431  THR A 438 -1  O  TYR A 434   N  MET A 255           
-SHEET    3   A 3 LYS A 446  CYS A 449 -1  O  VAL A 447   N  SER A 437           
-SHEET    1   B 6 GLY A 253  VAL A 256  0                                        
-SHEET    2   B 6 ALA A 431  THR A 438 -1  O  TYR A 434   N  MET A 255           
-SHEET    3   B 6 TYR A 494  CYS A 497 -1  O  MET A 495   N  VAL A 433           
-SHEET    4   B 6 ASN A 483  TYR A 490 -1  N  TYR A 490   O  TYR A 494           
-SHEET    5   B 6 ALA A 470  VAL A 476 -1  N  TYR A 475   O  LEU A 484           
-SHEET    6   B 6 VAL A 513  VAL A 520 -1  O  VAL A 513   N  VAL A 476           
-SHEET    1   C 7 SER A 351  HIS A 357  0                                        
-SHEET    2   C 7 CYS A 331  LYS A 339 -1  N  MET A 335   O  VAL A 354           
-SHEET    3   C 7 GLU A 385  ASN A 395 -1  O  SER A 394   N  ASP A 332           
-SHEET    4   C 7 ARG A 290  ASN A 298 -1  N  MET A 291   O  LEU A 388           
-SHEET    5   C 7 ASN A 301  ALA A 307 -1  O  ASN A 301   N  ASN A 298           
-SHEET    6   C 7 THR A 369  LEU A 372 -1  O  VAL A 370   N  VAL A 304           
-SHEET    7   C 7 PHE A 363  ALA A 364 -1  N  ALA A 364   O  THR A 369           
-SHEET    1   D 3 GLY B 253  MET B 255  0                                        
-SHEET    2   D 3 TYR B 434  THR B 438 -1  O  TYR B 434   N  MET B 255           
-SHEET    3   D 3 LYS B 446  CYS B 449 -1  O  VAL B 447   N  SER B 437           
-SHEET    1   E 7 SER B 351  HIS B 357  0                                        
-SHEET    2   E 7 CYS B 331  LYS B 339 -1  N  MET B 335   O  VAL B 354           
-SHEET    3   E 7 GLU B 385  ASN B 395 -1  O  GLU B 389   N  THR B 336           
-SHEET    4   E 7 ARG B 290  ASN B 298 -1  N  GLY B 293   O  VAL B 386           
-SHEET    5   E 7 ASN B 301  ALA B 307 -1  O  ASN B 301   N  ASN B 298           
-SHEET    6   E 7 THR B 369  LEU B 372 -1  O  LEU B 372   N  TYR B 302           
-SHEET    7   E 7 PHE B 363  ALA B 364 -1  N  ALA B 364   O  THR B 369           
-SHEET    1   F 5 ALA B 431  ILE B 432  0                                        
-SHEET    2   F 5 TYR B 494  CYS B 497 -1  O  CYS B 497   N  ALA B 431           
-SHEET    3   F 5 ASN B 483  TYR B 490 -1  N  LYS B 488   O  THR B 496           
-SHEET    4   F 5 ALA B 470  VAL B 476 -1  N  TYR B 475   O  LEU B 484           
-SHEET    5   F 5 VAL B 513  VAL B 520 -1  O  SER B 518   N  LEU B 472           
-LINK         C1  FUC A 601                 O2  GAL A 602     1555   1555  1.39  
-LINK         C1  FUC B 601                 O2  GAL B 602     1555   1555  1.43  
-LINK         C1  GAL B 602                 O4  NDG B 603     1555   1555  1.37  
-LINK         O3  NDG B 603                 C1  FUC B 604     1555   1555  1.39  
-LINK         C1  GAL A 602                 O4  NDG A 603     1555   1555  1.40  
-LINK         O3  NDG A 603                 C1  FUC A 604     1555   1555  1.41  
-SITE     1 AC1 20 ASP A 332  HIS A 334  TRP A 392  SER A 394                    
-SITE     2 AC1 20 ASN A 395  THR A 397  VAL A 442  ASP A 477                    
-SITE     3 AC1 20 HOH A 716  HOH A 849  HOH A 855  HOH A 861                    
-SITE     4 AC1 20 HOH A 901  HOH A 909  HOH A1053  HOH A1054                    
-SITE     5 AC1 20 THR B 347  GLY B 348  ASP B 349  HOH B 805                    
-SITE     1 AC2 17 THR A 347  GLY A 348  ASP A 349  HOH A 808                    
-SITE     2 AC2 17 HOH A 957  ASP B 332  HIS B 334  SER B 394                    
-SITE     3 AC2 17 ASN B 395  THR B 397  VAL B 442  HOH B 738                    
-SITE     4 AC2 17 HOH B 800  HOH B 813  HOH B 824  HOH B 893                    
-SITE     5 AC2 17 HOH B1081                                                     
-CRYST1  140.390  140.390   65.020  90.00  90.00 120.00 P 61         12          
-ORIGX1      1.000000  0.000000  0.000000        0.00000                         
-ORIGX2      0.000000  1.000000  0.000000        0.00000                         
-ORIGX3      0.000000  0.000000  1.000000        0.00000                         
-SCALE1      0.007123  0.004112  0.000000        0.00000                         
-SCALE2      0.000000  0.008225  0.000000        0.00000                         
-SCALE3      0.000000  0.000000  0.015380        0.00000                         
-ATOM      1  N   LYS A 230      32.874  -7.255  -1.930  1.00 43.09           N  
-ANISOU    1  N   LYS A 230     4814   5458   6101   -327  -1881    756       N  
-ATOM      2  CA  LYS A 230      34.227  -6.964  -2.393  1.00 41.33           C  
-ANISOU    2  CA  LYS A 230     4705   5361   5636   -224  -2051    850       C  
-ATOM      3  C   LYS A 230      35.262  -7.795  -1.640  1.00 36.05           C  
-ANISOU    3  C   LYS A 230     4151   4780   4764   -702  -2164    586       C  
-ATOM      4  O   LYS A 230      35.293  -7.787  -0.409  1.00 35.34           O  
-ANISOU    4  O   LYS A 230     4033   4707   4687  -1009  -2109    446       O  
-ATOM      5  CB  LYS A 230      34.538  -5.474  -2.242  1.00 43.87           C  
-ANISOU    5  CB  LYS A 230     5131   5440   6097    235  -2144    793       C  
-ATOM      6  CG  LYS A 230      35.816  -5.033  -2.942  1.00 47.80           C  
-ANISOU    6  CG  LYS A 230     5532   5726   6905    714  -1985    480       C  
-ATOM      7  CD  LYS A 230      35.925  -3.516  -2.993  1.00 51.37           C  
-ANISOU    7  CD  LYS A 230     5906   5870   7742    956  -1738    -24       C  
-ATOM      8  CE  LYS A 230      36.989  -3.072  -3.983  1.00 53.92           C  
-ANISOU    8  CE  LYS A 230     6154   6008   8326   1237  -1728   -462       C  
-ATOM      9  NZ  LYS A 230      37.100  -1.585  -4.074  1.00 54.82           N  
-ANISOU    9  NZ  LYS A 230     6280   6026   8521   1384  -1867   -729       N  
-ATOM     10  N   PRO A 231      36.109  -8.521  -2.382  1.00 31.74           N  
-ANISOU   10  N   PRO A 231     3795   4132   4131   -877  -2114    270       N  
-ATOM     11  CA  PRO A 231      37.158  -9.356  -1.790  1.00 28.40           C  
-ANISOU   11  CA  PRO A 231     3467   3636   3686  -1082  -1686    522       C  
-ATOM     12  C   PRO A 231      38.218  -8.528  -1.071  1.00 24.06           C  
-ANISOU   12  C   PRO A 231     2903   3029   3208  -1165  -1426    852       C  
-ATOM     13  O   PRO A 231      38.663  -7.495  -1.580  1.00 26.23           O  
-ANISOU   13  O   PRO A 231     3088   3207   3672  -1053  -1424   1324       O  
-ATOM     14  CB  PRO A 231      37.783 -10.051  -3.005  1.00 30.68           C  
-ANISOU   14  CB  PRO A 231     3731   3817   4107   -923  -1627    103       C  
-ATOM     15  CG  PRO A 231      36.752  -9.971  -4.070  1.00 32.27           C  
-ANISOU   15  CG  PRO A 231     3947   4325   3988   -385  -1684    549       C  
-ATOM     16  CD  PRO A 231      36.050  -8.671  -3.845  1.00 33.15           C  
-ANISOU   16  CD  PRO A 231     3995   4341   4257   -431  -1563    669       C  
-ATOM     17  N   PHE A 232      38.610  -8.989   0.110  1.00 20.43           N  
-ANISOU   17  N   PHE A 232     2276   2627   2858  -1072  -1152    673       N  
-ATOM     18  CA  PHE A 232      39.687  -8.369   0.866  1.00 17.97           C  
-ANISOU   18  CA  PHE A 232     1930   2086   2812   -863   -869    491       C  
-ATOM     19  C   PHE A 232      41.016  -8.547   0.137  1.00 16.47           C  
-ANISOU   19  C   PHE A 232     2085   1603   2570   -631   -466    675       C  
-ATOM     20  O   PHE A 232      41.208  -9.510  -0.603  1.00 17.79           O  
-ANISOU   20  O   PHE A 232     2288   1445   3024   -499   -817    295       O  
-ATOM     21  CB  PHE A 232      39.761  -8.990   2.266  1.00 16.61           C  
-ANISOU   21  CB  PHE A 232     1862   1869   2579   -762   -552    719       C  
-ATOM     22  CG  PHE A 232      40.836  -8.407   3.131  1.00 16.12           C  
-ANISOU   22  CG  PHE A 232     1877   1646   2601   -786   -399    160       C  
-ATOM     23  CD1 PHE A 232      40.678  -7.158   3.709  1.00 16.43           C  
-ANISOU   23  CD1 PHE A 232     1944   1769   2528   -631    -49    197       C  
-ATOM     24  CD2 PHE A 232      42.008  -9.109   3.367  1.00 15.42           C  
-ANISOU   24  CD2 PHE A 232     1911   1538   2410   -661   -150    481       C  
-ATOM     25  CE1 PHE A 232      41.677  -6.616   4.504  1.00 17.04           C  
-ANISOU   25  CE1 PHE A 232     2135   1824   2516   -589    130    411       C  
-ATOM     26  CE2 PHE A 232      43.006  -8.575   4.160  1.00 15.21           C  
-ANISOU   26  CE2 PHE A 232     2070   1631   2076   -688   -434    184       C  
-ATOM     27  CZ  PHE A 232      42.840  -7.326   4.730  1.00 15.16           C  
-ANISOU   27  CZ  PHE A 232     2118   1456   2186   -726   -191    123       C  
-ATOM     28  N   SER A 233      41.927  -7.605   0.341  1.00 14.62           N  
-ANISOU   28  N   SER A 233     1659   1440   2454   -671   -461    448       N  
-ATOM     29  CA  SER A 233      43.270  -7.693  -0.215  1.00 13.95           C  
-ANISOU   29  CA  SER A 233     1845   1416   2039   -506   -290    202       C  
-ATOM     30  C   SER A 233      44.175  -6.764   0.571  1.00 12.32           C  
-ANISOU   30  C   SER A 233     1767   1256   1658   -269   -531    -53       C  
-ATOM     31  O   SER A 233      43.700  -5.898   1.310  1.00 12.92           O  
-ANISOU   31  O   SER A 233     1677   1244   1989   -233   -272    -53       O  
-ATOM     32  CB  SER A 233      43.280  -7.297  -1.693  1.00 14.11           C  
-ANISOU   32  CB  SER A 233     2292   1020   2050   -225   -470    -98       C  
-ATOM     33  OG  SER A 233      42.938  -5.925  -1.841  1.00 14.80           O  
-ANISOU   33  OG  SER A 233     2350   1084   2190   -279   -759    -13       O  
-ATOM     34  N   VAL A 234      45.481  -6.967   0.436  1.00 12.92           N  
-ANISOU   34  N   VAL A 234     1744   1111   2053   -305   -413     36       N  
-ATOM     35  CA  VAL A 234      46.452  -6.027   0.988  1.00 11.94           C  
-ANISOU   35  CA  VAL A 234     1698   1072   1767   -290   -349     -3       C  
-ATOM     36  C   VAL A 234      47.284  -5.471  -0.164  1.00 12.23           C  
-ANISOU   36  C   VAL A 234     1690   1098   1857    -41   -145   -179       C  
-ATOM     37  O   VAL A 234      47.290  -6.045  -1.254  1.00 12.60           O  
-ANISOU   37  O   VAL A 234     1767   1144   1876   -115   -410    166       O  
-ATOM     38  CB  VAL A 234      47.351  -6.686   2.055  1.00 12.49           C  
-ANISOU   38  CB  VAL A 234     1726   1284   1734    -11   -240    238       C  
-ATOM     39  CG1 VAL A 234      46.503  -7.220   3.205  1.00 13.44           C  
-ANISOU   39  CG1 VAL A 234     2015   1149   1942    -43     52    186       C  
-ATOM     40  CG2 VAL A 234      48.215  -7.791   1.449  1.00 13.74           C  
-ANISOU   40  CG2 VAL A 234     1610   1435   2175    -10   -200     61       C  
-ATOM     41  N   PRO A 235      47.983  -4.347   0.059  1.00 12.26           N  
-ANISOU   41  N   PRO A 235     1721    973   1964   -177     34    127       N  
-ATOM     42  CA  PRO A 235      48.759  -3.787  -1.047  1.00 13.28           C  
-ANISOU   42  CA  PRO A 235     1887    875   2283    -46     58     -4       C  
-ATOM     43  C   PRO A 235      49.764  -4.768  -1.644  1.00 12.71           C  
-ANISOU   43  C   PRO A 235     1832    978   2017   -131   -513    275       C  
-ATOM     44  O   PRO A 235      50.415  -5.542  -0.932  1.00 13.01           O  
-ANISOU   44  O   PRO A 235     1880   1217   1847    155   -453      5       O  
-ATOM     45  CB  PRO A 235      49.491  -2.607  -0.401  1.00 15.46           C  
-ANISOU   45  CB  PRO A 235     2246    927   2699   -365     87   -270       C  
-ATOM     46  CG  PRO A 235      48.616  -2.205   0.736  1.00 15.85           C  
-ANISOU   46  CG  PRO A 235     2267   1117   2639   -191    379    -74       C  
-ATOM     47  CD  PRO A 235      48.045  -3.499   1.263  1.00 13.71           C  
-ANISOU   47  CD  PRO A 235     2095    802   2310   -321    162   -346       C  
-ATOM     48  N   ASN A 236      49.846  -4.712  -2.967  1.00 15.27           N  
-ANISOU   48  N   ASN A 236     2105   1676   2022   -567    -13   -110       N  
-ATOM     49  CA  ASN A 236      50.816  -5.410  -3.788  1.00 18.59           C  
-ANISOU   49  CA  ASN A 236     2430   2313   2318   -616    342    284       C  
-ATOM     50  C   ASN A 236      51.997  -4.472  -4.021  1.00 18.64           C  
-ANISOU   50  C   ASN A 236     2450   2310   2321   -502    447    251       C  
-ATOM     51  O   ASN A 236      52.313  -4.109  -5.162  1.00 24.37           O  
-ANISOU   51  O   ASN A 236     3150   3077   3031     98    563    946       O  
-ATOM     52  CB  ASN A 236      50.158  -5.751  -5.124  1.00 23.63           C  
-ANISOU   52  CB  ASN A 236     3013   3235   2731   -356   -166   -636       C  
-ATOM     53  CG  ASN A 236      51.070  -6.496  -6.055  1.00 27.55           C  
-ANISOU   53  CG  ASN A 236     3509   4215   2744   -250   -522   -327       C  
-ATOM     54  OD1 ASN A 236      51.867  -7.328  -5.626  1.00 31.61           O  
-ANISOU   54  OD1 ASN A 236     3989   4323   3697    263   -249    -15       O  
-ATOM     55  ND2 ASN A 236      50.954  -6.209  -7.348  1.00 31.68           N  
-ANISOU   55  ND2 ASN A 236     3685   4611   3739   -317   -602   -491       N  
-ATOM     56  N   ILE A 237      52.598  -4.044  -2.916  1.00 13.80           N  
-ANISOU   56  N   ILE A 237     1612   1936   1693   -346   -126    225       N  
-ATOM     57  CA  ILE A 237      53.772  -3.175  -2.901  1.00 13.91           C  
-ANISOU   57  CA  ILE A 237     1721   1413   2150    126    -83    248       C  
-ATOM     58  C   ILE A 237      54.809  -3.777  -1.959  1.00 12.34           C  
-ANISOU   58  C   ILE A 237     1530   1088   2069     21     14    338       C  
-ATOM     59  O   ILE A 237      54.476  -4.176  -0.838  1.00 11.85           O  
-ANISOU   59  O   ILE A 237     1649   1046   1805   -107     80    139       O  
-ATOM     60  CB  ILE A 237      53.420  -1.774  -2.356  1.00 14.60           C  
-ANISOU   60  CB  ILE A 237     1879   1313   2354    149   -225    332       C  
-ATOM     61  CG1 ILE A 237      52.350  -1.101  -3.214  1.00 18.09           C  
-ANISOU   61  CG1 ILE A 237     2039   1641   3194    488   -166    212       C  
-ATOM     62  CG2 ILE A 237      54.666  -0.887  -2.277  1.00 14.78           C  
-ANISOU   62  CG2 ILE A 237     2120   1019   2477    -12   -335      1       C  
-ATOM     63  CD1 ILE A 237      51.742   0.113  -2.577  1.00 22.80           C  
-ANISOU   63  CD1 ILE A 237     2526   2006   4130    501    -35    193       C  
-ATOM     64  N   PRO A 238      56.076  -3.844  -2.395  1.00 11.18           N  
-ANISOU   64  N   PRO A 238     1453    937   1859    -65   -137    154       N  
-ATOM     65  CA  PRO A 238      57.112  -4.359  -1.493  1.00 11.44           C  
-ANISOU   65  CA  PRO A 238     1608   1095   1643     48     25    159       C  
-ATOM     66  C   PRO A 238      57.177  -3.585  -0.181  1.00 10.43           C  
-ANISOU   66  C   PRO A 238     1645    892   1426     14   -289     28       C  
-ATOM     67  O   PRO A 238      57.000  -2.363  -0.148  1.00 11.05           O  
-ANISOU   67  O   PRO A 238     1551    594   2052      3   -196    -32       O  
-ATOM     68  CB  PRO A 238      58.401  -4.178  -2.297  1.00 12.91           C  
-ANISOU   68  CB  PRO A 238     1782   1356   1768     99    173    -68       C  
-ATOM     69  CG  PRO A 238      57.953  -4.230  -3.721  1.00 14.28           C  
-ANISOU   69  CG  PRO A 238     1858   1735   1833    303    126    201       C  
-ATOM     70  CD  PRO A 238      56.615  -3.531  -3.728  1.00 12.90           C  
-ANISOU   70  CD  PRO A 238     1509   1500   1890    100    385    404       C  
-ATOM     71  N   MET A 239      57.440  -4.304   0.901  1.00 10.87           N  
-ANISOU   71  N   MET A 239     1553   1139   1436    -60   -142   -127       N  
-ATOM     72  CA  MET A 239      57.399  -3.713   2.229  1.00 10.30           C  
-ANISOU   72  CA  MET A 239     1716    785   1410    -32   -223     37       C  
-ATOM     73  C   MET A 239      58.294  -2.482   2.343  1.00 10.39           C  
-ANISOU   73  C   MET A 239     1372    725   1849   -218   -133   -109       C  
-ATOM     74  O   MET A 239      57.907  -1.474   2.961  1.00 11.35           O  
-ANISOU   74  O   MET A 239     1722    731   1857     14    -41   -138       O  
-ATOM     75  CB  MET A 239      57.794  -4.745   3.290  1.00 10.65           C  
-ANISOU   75  CB  MET A 239     1868    801   1375    -65    -74    122       C  
-ATOM     76  CG  MET A 239      57.605  -4.231   4.713  1.00 11.66           C  
-ANISOU   76  CG  MET A 239     1800    919   1709   -140    -37   -287       C  
-ATOM     77  SD  MET A 239      58.102  -5.406   5.986  1.00 12.59           S  
-ANISOU   77  SD  MET A 239     2147    846   1789    -27     76     65       S  
-ATOM     78  CE  MET A 239      59.879  -5.430   5.736  1.00 13.31           C  
-ANISOU   78  CE  MET A 239     1541   1192   2323   -147     34     29       C  
-ATOM     79  N   ASN A 240      59.485  -2.564   1.752  1.00  9.87           N  
-ANISOU   79  N   ASN A 240     1164    804   1780   -281    120    149       N  
-ATOM     80  CA  ASN A 240      60.472  -1.491   1.873  1.00 10.35           C  
-ANISOU   80  CA  ASN A 240     1178    748   2004   -139    139    213       C  
-ATOM     81  C   ASN A 240      60.218  -0.267   0.992  1.00  9.63           C  
-ANISOU   81  C   ASN A 240     1549    671   1439    166   -186    -22       C  
-ATOM     82  O   ASN A 240      61.019   0.676   1.000  1.00 11.77           O  
-ANISOU   82  O   ASN A 240     1458    719   2294   -104   -308     11       O  
-ATOM     83  CB  ASN A 240      61.902  -2.009   1.697  1.00 12.36           C  
-ANISOU   83  CB  ASN A 240     1475   1111   2109     47    315   -133       C  
-ATOM     84  CG  ASN A 240      62.195  -2.470   0.282  1.00 13.81           C  
-ANISOU   84  CG  ASN A 240     1744   1104   2398    -88    101   -265       C  
-ATOM     85  OD1 ASN A 240      61.313  -2.956  -0.439  1.00 12.81           O  
-ANISOU   85  OD1 ASN A 240     1776    998   2091    109    -11      0       O  
-ATOM     86  ND2 ASN A 240      63.453  -2.339  -0.117  1.00 17.13           N  
-ANISOU   86  ND2 ASN A 240     1830   1474   3205   -317    470   -489       N  
-ATOM     87  N   LEU A 241      59.096  -0.275   0.270  1.00 10.16           N  
-ANISOU   87  N   LEU A 241     1524    784   1550    235   -145    -89       N  
-ATOM     88  CA  LEU A 241      58.635   0.906  -0.456  1.00 10.17           C  
-ANISOU   88  CA  LEU A 241     1418    875   1571     64    114      0       C  
-ATOM     89  C   LEU A 241      57.490   1.611   0.268  1.00  9.72           C  
-ANISOU   89  C   LEU A 241     1275    912   1504     40    272      5       C  
-ATOM     90  O   LEU A 241      57.046   2.670  -0.162  1.00 10.99           O  
-ANISOU   90  O   LEU A 241     1398    824   1952    277    178    140       O  
-ATOM     91  CB  LEU A 241      58.191   0.556  -1.879  1.00 11.01           C  
-ANISOU   91  CB  LEU A 241     1778   1091   1315     -7    233   -125       C  
-ATOM     92  CG  LEU A 241      59.267  -0.037  -2.792  1.00 14.78           C  
-ANISOU   92  CG  LEU A 241     2084   1781   1750     91    384     39       C  
-ATOM     93  CD1 LEU A 241      58.759  -0.186  -4.215  1.00 15.52           C  
-ANISOU   93  CD1 LEU A 241     2616   2086   1193     44     44   -136       C  
-ATOM     94  CD2 LEU A 241      60.519   0.805  -2.753  1.00 16.75           C  
-ANISOU   94  CD2 LEU A 241     2103   2146   2113   -184    573    -69       C  
-ATOM     95  N   MET A 242      57.003   1.020   1.355  1.00  9.79           N  
-ANISOU   95  N   MET A 242     1089   1034   1595    -94    231    -41       N  
-ATOM     96  CA  MET A 242      55.901   1.616   2.103  1.00  9.81           C  
-ANISOU   96  CA  MET A 242     1295    944   1486   -185    300     79       C  
-ATOM     97  C   MET A 242      56.406   2.412   3.299  1.00  8.91           C  
-ANISOU   97  C   MET A 242     1279    828   1276    123     51     90       C  
-ATOM     98  O   MET A 242      57.540   2.226   3.744  1.00 11.01           O  
-ANISOU   98  O   MET A 242     1358    956   1867    292    -98    -65       O  
-ATOM     99  CB  MET A 242      54.891   0.548   2.540  1.00 11.75           C  
-ANISOU   99  CB  MET A 242     1416    914   2133   -211    206      9       C  
-ATOM    100  CG  MET A 242      54.097   0.004   1.358  1.00 12.10           C  
-ANISOU  100  CG  MET A 242     1495   1193   1909   -637    227   -397       C  
-ATOM    101  SD  MET A 242      52.847  -1.209   1.802  1.00 16.07           S  
-ANISOU  101  SD  MET A 242     1677   1474   2956   -195    284   -469       S  
-ATOM    102  CE  MET A 242      53.912  -2.584   2.239  1.00 19.12           C  
-ANISOU  102  CE  MET A 242     1881   1824   3559   -265    -67    316       C  
-ATOM    103  N   SER A 243      55.563   3.307   3.807  1.00  9.38           N  
-ANISOU  103  N   SER A 243     1330    832   1402    183    149   -305       N  
-ATOM    104  CA  SER A 243      55.920   4.154   4.931  1.00  9.05           C  
-ANISOU  104  CA  SER A 243     1204    795   1440     73    168   -146       C  
-ATOM    105  C   SER A 243      55.507   3.581   6.283  1.00  8.46           C  
-ANISOU  105  C   SER A 243     1081    710   1422     79    -34     60       C  
-ATOM    106  O   SER A 243      54.491   2.901   6.415  1.00  9.52           O  
-ANISOU  106  O   SER A 243     1042    929   1647    -61   -142    -47       O  
-ATOM    107  CB  SER A 243      55.245   5.525   4.762  1.00  9.86           C  
-ANISOU  107  CB  SER A 243     1565    641   1541    231     12   -362       C  
-ATOM    108  OG  SER A 243      55.596   6.420   5.819  1.00 10.51           O  
-ANISOU  108  OG  SER A 243     1373    827   1794    126    188     91       O  
-ATOM    109  N   ASN A 244      56.305   3.875   7.300  1.00  8.46           N  
-ANISOU  109  N   ASN A 244     1181    760   1273    158   -159    -25       N  
-ATOM    110  CA  ASN A 244      55.880   3.740   8.682  1.00  8.36           C  
-ANISOU  110  CA  ASN A 244     1005    951   1219    174    -74   -224       C  
-ATOM    111  C   ASN A 244      54.586   4.551   8.850  1.00  8.33           C  
-ANISOU  111  C   ASN A 244      936    959   1269    -97     24    -24       C  
-ATOM    112  O   ASN A 244      54.370   5.543   8.145  1.00  8.97           O  
-ANISOU  112  O   ASN A 244     1074    831   1501     26    105    122       O  
-ATOM    113  CB  ASN A 244      56.999   4.293   9.584  1.00  8.87           C  
-ANISOU  113  CB  ASN A 244     1132    839   1398    -72   -325    -56       C  
-ATOM    114  CG  ASN A 244      56.943   3.776  11.012  1.00  8.70           C  
-ANISOU  114  CG  ASN A 244     1132    648   1523    106     22    -76       C  
-ATOM    115  OD1 ASN A 244      56.104   4.189  11.815  1.00  9.39           O  
-ANISOU  115  OD1 ASN A 244     1260    735   1571    205    -64   -179       O  
-ATOM    116  ND2 ASN A 244      57.882   2.893  11.349  1.00  9.42           N  
-ANISOU  116  ND2 ASN A 244     1240    578   1761    142   -437    -29       N  
-ATOM    117  N   SER A 245      53.725   4.151   9.779  1.00  8.11           N  
-ANISOU  117  N   SER A 245      758    857   1467     77     16   -191       N  
-ATOM    118  CA  SER A 245      52.503   4.919  10.042  1.00  8.08           C  
-ANISOU  118  CA  SER A 245      738    846   1485   -155     79   -124       C  
-ATOM    119  C   SER A 245      52.617   5.904  11.208  1.00  8.03           C  
-ANISOU  119  C   SER A 245      977    738   1334   -116   -272   -120       C  
-ATOM    120  O   SER A 245      51.685   6.683  11.452  1.00  9.73           O  
-ANISOU  120  O   SER A 245     1024    912   1759    171    -79   -192       O  
-ATOM    121  CB  SER A 245      51.314   3.980  10.258  1.00  9.21           C  
-ANISOU  121  CB  SER A 245     1088    780   1629    135    -17    256       C  
-ATOM    122  OG  SER A 245      51.638   2.998  11.231  1.00 10.44           O  
-ANISOU  122  OG  SER A 245     1040   1200   1725    109     -4    250       O  
-ATOM    123  N   ARG A 246      53.752   5.895  11.908  1.00  8.18           N  
-ANISOU  123  N   ARG A 246     1153    776   1179    -87   -197    -28       N  
-ATOM    124  CA  ARG A 246      53.967   6.808  13.041  1.00  8.32           C  
-ANISOU  124  CA  ARG A 246     1261    723   1175    -70   -320     66       C  
-ATOM    125  C   ARG A 246      54.977   7.922  12.756  1.00  9.09           C  
-ANISOU  125  C   ARG A 246     1170    731   1551     52   -245     20       C  
-ATOM    126  O   ARG A 246      54.983   8.946  13.440  1.00  9.63           O  
-ANISOU  126  O   ARG A 246     1256    703   1701    111   -135    -27       O  
-ATOM    127  CB  ARG A 246      54.405   6.024  14.275  1.00  9.46           C  
-ANISOU  127  CB  ARG A 246     1428    688   1478    -76    -55    123       C  
-ATOM    128  CG  ARG A 246      53.332   5.090  14.796  1.00  9.96           C  
-ANISOU  128  CG  ARG A 246     1640    780   1364   -135      2    150       C  
-ATOM    129  CD  ARG A 246      53.821   4.335  16.018  1.00 10.75           C  
-ANISOU  129  CD  ARG A 246     1894   1086   1105    280   -130     48       C  
-ATOM    130  NE  ARG A 246      53.858   5.171  17.208  1.00 10.11           N  
-ANISOU  130  NE  ARG A 246     1811   1017   1014     76   -107   -203       N  
-ATOM    131  CZ  ARG A 246      54.603   4.914  18.279  1.00 10.59           C  
-ANISOU  131  CZ  ARG A 246     1838    605   1579     33   -178   -164       C  
-ATOM    132  NH1 ARG A 246      55.423   3.862  18.284  1.00 11.58           N  
-ANISOU  132  NH1 ARG A 246     1805    916   1679    338    130   -136       N  
-ATOM    133  NH2 ARG A 246      54.532   5.711  19.339  1.00 12.01           N  
-ANISOU  133  NH2 ARG A 246     2007    877   1677     95     26   -227       N  
-ATOM    134  N   VAL A 247      55.854   7.702  11.776  1.00  9.43           N  
-ANISOU  134  N   VAL A 247     1132    904   1545     70     32     -6       N  
-ATOM    135  CA  VAL A 247      56.716   8.752  11.228  1.00  9.44           C  
-ANISOU  135  CA  VAL A 247     1225    978   1384    147   -198     59       C  
-ATOM    136  C   VAL A 247      56.731   8.568   9.715  1.00  9.24           C  
-ANISOU  136  C   VAL A 247     1239    683   1587    109   -251    110       C  
-ATOM    137  O   VAL A 247      56.528   7.453   9.230  1.00  9.80           O  
-ANISOU  137  O   VAL A 247     1477    625   1621     27   -118     48       O  
-ATOM    138  CB  VAL A 247      58.166   8.672  11.766  1.00  9.55           C  
-ANISOU  138  CB  VAL A 247     1143    830   1655    353   -398   -203       C  
-ATOM    139  CG1 VAL A 247      58.222   9.071  13.239  1.00 11.97           C  
-ANISOU  139  CG1 VAL A 247     1265   1364   1918    180   -558   -383       C  
-ATOM    140  CG2 VAL A 247      58.737   7.277  11.560  1.00 10.49           C  
-ANISOU  140  CG2 VAL A 247     1286    870   1830    230   -320    136       C  
-ATOM    141  N   PRO A 248      56.927   9.655   8.955  1.00  9.78           N  
-ANISOU  141  N   PRO A 248     1552    660   1502    322     -2   -118       N  
-ATOM    142  CA  PRO A 248      56.981   9.521   7.495  1.00  9.78           C  
-ANISOU  142  CA  PRO A 248     1493    665   1556    397     25      9       C  
-ATOM    143  C   PRO A 248      58.376   9.079   7.050  1.00 10.45           C  
-ANISOU  143  C   PRO A 248     1425    912   1633     26    155    -54       C  
-ATOM    144  O   PRO A 248      59.220   9.894   6.663  1.00 14.55           O  
-ANISOU  144  O   PRO A 248     1567    907   3052     58    182     38       O  
-ATOM    145  CB  PRO A 248      56.635  10.930   7.009  1.00 11.32           C  
-ANISOU  145  CB  PRO A 248     1845    537   1920    128    -32     21       C  
-ATOM    146  CG  PRO A 248      57.181  11.808   8.088  1.00 11.43           C  
-ANISOU  146  CG  PRO A 248     1943    520   1880    -54     10     85       C  
-ATOM    147  CD  PRO A 248      56.928  11.069   9.382  1.00 11.14           C  
-ANISOU  147  CD  PRO A 248     1854    514   1865     57     14     36       C  
-ATOM    148  N   MET A 249      58.608   7.771   7.136  1.00 10.66           N  
-ANISOU  148  N   MET A 249     1501    720   1829    182    166     27       N  
-ATOM    149  CA  MET A 249      59.887   7.160   6.802  1.00 10.27           C  
-ANISOU  149  CA  MET A 249     1558   1009   1336    275    -32   -448       C  
-ATOM    150  C   MET A 249      59.606   5.811   6.192  1.00  9.51           C  
-ANISOU  150  C   MET A 249     1178    994   1440    269      0   -335       C  
-ATOM    151  O   MET A 249      58.696   5.110   6.630  1.00 11.22           O  
-ANISOU  151  O   MET A 249     1132   1179   1951    -11    287     98       O  
-ATOM    152  CB  MET A 249      60.734   6.921   8.055  1.00 12.42           C  
-ANISOU  152  CB  MET A 249     2053   1052   1613    194   -503   -102       C  
-ATOM    153  CG  MET A 249      61.150   8.146   8.819  1.00 19.50           C  
-ANISOU  153  CG  MET A 249     2507   1884   3018   -119   -361     61       C  
-ATOM    154  SD  MET A 249      62.226   9.224   7.870  1.00 19.55           S  
-ANISOU  154  SD  MET A 249     2602   1981   2844   -757   -436     46       S  
-ATOM    155  CE  MET A 249      63.450   8.102   7.256  1.00 21.78           C  
-ANISOU  155  CE  MET A 249     2567   2399   3309   -371    446   1429       C  
-ATOM    156  N   LEU A 250      60.402   5.432   5.199  1.00  9.33           N  
-ANISOU  156  N   LEU A 250     1278    666   1602    173    -37   -190       N  
-ATOM    157  CA  LEU A 250      60.296   4.088   4.646  1.00  9.75           C  
-ANISOU  157  CA  LEU A 250     1384    609   1709    284    262    -12       C  
-ATOM    158  C   LEU A 250      60.457   3.027   5.739  1.00  9.61           C  
-ANISOU  158  C   LEU A 250     1214    574   1862     14    130     48       C  
-ATOM    159  O   LEU A 250      61.234   3.187   6.689  1.00 10.42           O  
-ANISOU  159  O   LEU A 250     1209    892   1856    133   -154   -107       O  
-ATOM    160  CB  LEU A 250      61.357   3.879   3.571  1.00 10.96           C  
-ANISOU  160  CB  LEU A 250     1615    855   1693    467    231    114       C  
-ATOM    161  CG  LEU A 250      61.168   4.651   2.269  1.00 11.97           C  
-ANISOU  161  CG  LEU A 250     2025   1121   1403     96    103    312       C  
-ATOM    162  CD1 LEU A 250      62.425   4.530   1.417  1.00 15.47           C  
-ANISOU  162  CD1 LEU A 250     2336   1692   1850    433    837     80       C  
-ATOM    163  CD2 LEU A 250      59.947   4.147   1.518  1.00 14.28           C  
-ANISOU  163  CD2 LEU A 250     2384   1091   1949     -4   -554    219       C  
-ATOM    164  N   ILE A 251      59.719   1.937   5.587  1.00  9.78           N  
-ANISOU  164  N   ILE A 251     1243    567   1907    111     72    187       N  
-ATOM    165  CA  ILE A 251      59.913   0.766   6.432  1.00  9.15           C  
-ANISOU  165  CA  ILE A 251     1264    490   1723     99     21    -71       C  
-ATOM    166  C   ILE A 251      61.226   0.077   6.072  1.00  9.55           C  
-ANISOU  166  C   ILE A 251     1416    592   1619     52    187   -316       C  
-ATOM    167  O   ILE A 251      61.497  -0.168   4.894  1.00 10.55           O  
-ANISOU  167  O   ILE A 251     1444    792   1771    166     17   -267       O  
-ATOM    168  CB  ILE A 251      58.738  -0.208   6.271  1.00  9.18           C  
-ANISOU  168  CB  ILE A 251     1384    466   1638     11   -123     54       C  
-ATOM    169  CG1 ILE A 251      57.468   0.417   6.862  1.00 11.78           C  
-ANISOU  169  CG1 ILE A 251     1199    922   2354     48    113    111       C  
-ATOM    170  CG2 ILE A 251      59.059  -1.548   6.933  1.00 10.36           C  
-ANISOU  170  CG2 ILE A 251     1652    540   1745    134   -125    -18       C  
-ATOM    171  CD1 ILE A 251      56.192  -0.300   6.505  1.00 14.65           C  
-ANISOU  171  CD1 ILE A 251     1571   1251   2744     23   -154    -51       C  
-ATOM    172  N   ASP A 252      62.038  -0.233   7.081  1.00  9.91           N  
-ANISOU  172  N   ASP A 252     1303    574   1888    185   -191      8       N  
-ATOM    173  CA  ASP A 252      63.306  -0.933   6.836  1.00 10.58           C  
-ANISOU  173  CA  ASP A 252     1330    687   2003    259   -143      5       C  
-ATOM    174  C   ASP A 252      63.408  -2.291   7.522  1.00  9.90           C  
-ANISOU  174  C   ASP A 252     1436    583   1741    -13   -352     96       C  
-ATOM    175  O   ASP A 252      64.482  -2.896   7.569  1.00 12.23           O  
-ANISOU  175  O   ASP A 252     1321    781   2544    231   -275    -28       O  
-ATOM    176  CB  ASP A 252      64.517  -0.039   7.161  1.00 11.49           C  
-ANISOU  176  CB  ASP A 252     1390   1000   1976    -75   -102    -40       C  
-ATOM    177  CG  ASP A 252      64.660   0.263   8.642  1.00 14.16           C  
-ANISOU  177  CG  ASP A 252     1820   1151   2409   -565   -154   -484       C  
-ATOM    178  OD1 ASP A 252      63.852  -0.184   9.462  1.00 13.72           O  
-ANISOU  178  OD1 ASP A 252     1621   1189   2404     31    -45    -77       O  
-ATOM    179  OD2 ASP A 252      65.617   0.983   8.994  1.00 21.79           O  
-ANISOU  179  OD2 ASP A 252     2741   2068   3469  -1124    431   -735       O  
-ATOM    180  N   GLY A 253      62.285  -2.769   8.044  1.00  9.95           N  
-ANISOU  180  N   GLY A 253     1383    526   1871    -48   -128     86       N  
-ATOM    181  CA  GLY A 253      62.257  -4.087   8.643  1.00 10.53           C  
-ANISOU  181  CA  GLY A 253     1397    590   2015     -1   -189    193       C  
-ATOM    182  C   GLY A 253      60.965  -4.391   9.354  1.00  9.05           C  
-ANISOU  182  C   GLY A 253     1263    514   1661    -85   -191    -37       C  
-ATOM    183  O   GLY A 253      60.045  -3.560   9.412  1.00 10.00           O  
-ANISOU  183  O   GLY A 253     1375    736   1686    252    -80    -12       O  
-ATOM    184  N   MET A 254      60.891  -5.608   9.874  1.00  9.64           N  
-ANISOU  184  N   MET A 254     1402    637   1622    -47   -247   -147       N  
-ATOM    185  CA  MET A 254      59.840  -5.966  10.797  1.00  9.52           C  
-ANISOU  185  CA  MET A 254     1503    627   1485   -328   -247     98       C  
-ATOM    186  C   MET A 254      60.421  -6.852  11.878  1.00  9.11           C  
-ANISOU  186  C   MET A 254     1333    730   1398    -72     36     42       C  
-ATOM    187  O   MET A 254      61.466  -7.487  11.681  1.00 11.68           O  
-ANISOU  187  O   MET A 254     1476    890   2071    261     16     15       O  
-ATOM    188  CB  MET A 254      58.633  -6.604  10.092  1.00 14.67           C  
-ANISOU  188  CB  MET A 254     1933   1271   2370   -234    358   -410       C  
-ATOM    189  CG  MET A 254      58.933  -7.755   9.176  1.00 17.45           C  
-ANISOU  189  CG  MET A 254     2209   1429   2992   -283   -110   -229       C  
-ATOM    190  SD  MET A 254      57.393  -8.447   8.496  1.00 13.90           S  
-ANISOU  190  SD  MET A 254     2304   1114   1862   -619   -279   -240       S  
-ATOM    191  CE  MET A 254      58.072  -9.247   7.056  1.00 15.40           C  
-ANISOU  191  CE  MET A 254     2175   1546   2128    163      1   -289       C  
-ATOM    192  N   MET A 255      59.764  -6.861  13.033  1.00 10.32           N  
-ANISOU  192  N   MET A 255     1497    973   1452     17   -207    180       N  
-ATOM    193  CA  MET A 255      60.268  -7.582  14.194  1.00 10.89           C  
-ANISOU  193  CA  MET A 255     1447   1144   1546   -107   -385    503       C  
-ATOM    194  C   MET A 255      59.136  -7.802  15.182  1.00 10.28           C  
-ANISOU  194  C   MET A 255     1263    954   1687   -207   -230    167       C  
-ATOM    195  O   MET A 255      58.160  -7.050  15.188  1.00 11.37           O  
-ANISOU  195  O   MET A 255     1297   1065   1958    199   -179    139       O  
-ATOM    196  CB  MET A 255      61.381  -6.768  14.871  1.00 14.69           C  
-ANISOU  196  CB  MET A 255     1666   1585   2330   -182   -398    509       C  
-ATOM    197  CG  MET A 255      60.866  -5.506  15.560  1.00 15.53           C  
-ANISOU  197  CG  MET A 255     1893   1455   2552   -718   -815    299       C  
-ATOM    198  SD  MET A 255      62.144  -4.482  16.310  1.00 18.80           S  
-ANISOU  198  SD  MET A 255     2504   1890   2750   -528   -958    382       S  
-ATOM    199  CE  MET A 255      62.648  -5.516  17.683  1.00 25.16           C  
-ANISOU  199  CE  MET A 255     3036   2663   3859   -127   -789    900       C  
-ATOM    200  N   VAL A 256      59.272  -8.817  16.031  1.00 10.81           N  
-ANISOU  200  N   VAL A 256     1481    921   1703   -194   -243    445       N  
-ATOM    201  CA  VAL A 256      58.433  -8.903  17.212  1.00 11.31           C  
-ANISOU  201  CA  VAL A 256     1483    788   2026   -353   -192    229       C  
-ATOM    202  C   VAL A 256      59.178  -8.209  18.340  1.00 10.97           C  
-ANISOU  202  C   VAL A 256     1301   1095   1770   -188   -310    129       C  
-ATOM    203  O   VAL A 256      60.393  -8.020  18.268  1.00 12.30           O  
-ANISOU  203  O   VAL A 256     1529   1018   2124     28   -260     99       O  
-ATOM    204  CB  VAL A 256      58.082 -10.361  17.587  1.00 11.54           C  
-ANISOU  204  CB  VAL A 256     1378    747   2260   -172   -642    216       C  
-ATOM    205  CG1 VAL A 256      57.391 -11.038  16.413  1.00 13.31           C  
-ANISOU  205  CG1 VAL A 256     1774    989   2295   -300   -520    -21       C  
-ATOM    206  CG2 VAL A 256      59.328 -11.132  17.991  1.00 12.62           C  
-ANISOU  206  CG2 VAL A 256     1650    812   2333     30   -674    157       C  
-ATOM    207  N   SER A 257      58.458  -7.811  19.377  1.00 12.68           N  
-ANISOU  207  N   SER A 257     1706   1508   1602    -48   -313    225       N  
-ATOM    208  CA  SER A 257      59.101  -7.180  20.521  1.00 16.56           C  
-ANISOU  208  CA  SER A 257     2244   2375   1673    364   -564   -463       C  
-ATOM    209  C   SER A 257      59.797  -8.220  21.380  1.00 19.61           C  
-ANISOU  209  C   SER A 257     2733   2645   2074    500  -1214   -571       C  
-ATOM    210  O   SER A 257      59.335  -9.354  21.488  1.00 23.82           O  
-ANISOU  210  O   SER A 257     3122   2594   3333    237  -1405    180       O  
-ATOM    211  CB  SER A 257      58.063  -6.452  21.371  1.00 20.15           C  
-ANISOU  211  CB  SER A 257     2665   3045   1945    774   -808   -862       C  
-ATOM    212  OG  SER A 257      58.656  -6.015  22.576  1.00 26.07           O  
-ANISOU  212  OG  SER A 257     3128   4025   2751   1069   -921   -733       O  
-ATOM    213  N   ASN A 258      60.901  -7.825  22.008  1.00 22.65           N  
-ANISOU  213  N   ASN A 258     2991   3178   2436    806  -1222   -372       N  
-ATOM    214  CA  ASN A 258      61.503  -8.645  23.058  1.00 27.94           C  
-ANISOU  214  CA  ASN A 258     3348   3940   3329   1249  -1464   -102       C  
-ATOM    215  C   ASN A 258      60.704  -8.614  24.364  1.00 31.01           C  
-ANISOU  215  C   ASN A 258     4095   4555   3133   1761  -1210   -126       C  
-ATOM    216  O   ASN A 258      60.671  -9.599  25.103  1.00 35.41           O  
-ANISOU  216  O   ASN A 258     4540   4879   4035   1957   -589    360       O  
-ATOM    217  CB  ASN A 258      62.952  -8.238  23.315  1.00 30.21           C  
-ANISOU  217  CB  ASN A 258     3176   4216   4086   1258   -618   -410       C  
-ATOM    218  CG  ASN A 258      63.899  -8.795  22.279  1.00 28.24           C  
-ANISOU  218  CG  ASN A 258     3038   4228   3463   1045   -528   -358       C  
-ATOM    219  OD1 ASN A 258      63.539  -8.955  21.114  1.00 30.82           O  
-ANISOU  219  OD1 ASN A 258     3305   4573   3830   1121   -810   -193       O  
-ATOM    220  ND2 ASN A 258      65.114  -9.117  22.702  1.00 27.47           N  
-ANISOU  220  ND2 ASN A 258     2853   4073   3510    987   -988   -341       N  
-ATOM    221  N   ASP A 259      60.072  -7.481  24.654  1.00 31.25           N  
-ANISOU  221  N   ASP A 259     4386   4568   2918   1691  -1445   -511       N  
-ATOM    222  CA  ASP A 259      59.190  -7.382  25.814  1.00 33.27           C  
-ANISOU  222  CA  ASP A 259     4790   4853   2996   1526   -773   -217       C  
-ATOM    223  C   ASP A 259      57.754  -7.648  25.387  1.00 37.30           C  
-ANISOU  223  C   ASP A 259     5085   5114   3971   1313   -468    130       C  
-ATOM    224  O   ASP A 259      57.036  -6.731  24.994  1.00 38.54           O  
-ANISOU  224  O   ASP A 259     5296   4889   4459   1269   -340    267       O  
-ATOM    225  CB  ASP A 259      59.299  -6.006  26.476  1.00 35.33           C  
-ANISOU  225  CB  ASP A 259     5048   5440   2935   1859   -408   -432       C  
-ATOM    226  CG  ASP A 259      58.405  -5.870  27.712  1.00 38.84           C  
-ANISOU  226  CG  ASP A 259     5430   5737   3588   2262   -498   -472       C  
-ATOM    227  OD1 ASP A 259      58.333  -4.756  28.279  1.00 40.93           O  
-ANISOU  227  OD1 ASP A 259     5761   5889   3901   2255   -946   -904       O  
-ATOM    228  OD2 ASP A 259      57.775  -6.872  28.119  1.00 36.86           O  
-ANISOU  228  OD2 ASP A 259     5395   5717   2891   2401   -484    -88       O  
-ATOM    229  N   GLN A 260      57.340  -8.908  25.461  1.00 38.48           N  
-ANISOU  229  N   GLN A 260     5162   5059   4398    864   -566    212       N  
-ATOM    230  CA  GLN A 260      55.989  -9.291  25.058  1.00 40.85           C  
-ANISOU  230  CA  GLN A 260     5430   5244   4848    753   -402    794       C  
-ATOM    231  C   GLN A 260      54.925  -8.653  25.948  1.00 42.84           C  
-ANISOU  231  C   GLN A 260     5686   5955   4636    987   -149   1589       C  
-ATOM    232  O   GLN A 260      53.736  -8.649  25.612  1.00 41.78           O  
-ANISOU  232  O   GLN A 260     5578   6068   4228    773   -242   1636       O  
-ATOM    233  CB  GLN A 260      55.845 -10.813  25.053  1.00 40.26           C  
-ANISOU  233  CB  GLN A 260     5374   4903   5019    376   -757    676       C  
-ATOM    234  CG  GLN A 260      56.534 -11.481  23.875  1.00 37.32           C  
-ANISOU  234  CG  GLN A 260     5267   4258   4654    152  -1278    564       C  
-ATOM    235  CD  GLN A 260      55.877 -11.124  22.555  1.00 35.23           C  
-ANISOU  235  CD  GLN A 260     5130   3742   4512    -25  -1686    667       C  
-ATOM    236  OE1 GLN A 260      54.706 -11.438  22.331  1.00 32.87           O  
-ANISOU  236  OE1 GLN A 260     5044   3270   4173   -161  -1991    442       O  
-ATOM    237  NE2 GLN A 260      56.623 -10.453  21.677  1.00 33.23           N  
-ANISOU  237  NE2 GLN A 260     4996   3230   4400   -364  -1779    933       N  
-ATOM    238  N   ASN A 261      55.361  -8.105  27.078  1.00 42.42           N  
-ANISOU  238  N   ASN A 261     6031   6163   3923   1333    -22   2499       N  
-ATOM    239  CA  ASN A 261      54.445  -7.475  28.020  1.00 46.32           C  
-ANISOU  239  CA  ASN A 261     6465   6579   4553   1709    134   2438       C  
-ATOM    240  C   ASN A 261      54.145  -6.008  27.714  1.00 46.86           C  
-ANISOU  240  C   ASN A 261     6570   6268   4967   1788    282   2236       C  
-ATOM    241  O   ASN A 261      53.171  -5.458  28.223  1.00 48.04           O  
-ANISOU  241  O   ASN A 261     6507   6611   5133   1797    363   2460       O  
-ATOM    242  CB  ASN A 261      54.957  -7.623  29.455  1.00 48.38           C  
-ANISOU  242  CB  ASN A 261     6697   6893   4792   1970    108   2399       C  
-ATOM    243  CG  ASN A 261      54.947  -9.062  29.930  1.00 53.04           C  
-ANISOU  243  CG  ASN A 261     6914   7283   5954   2209     69   1850       C  
-ATOM    244  OD1 ASN A 261      55.944  -9.566  30.446  1.00 55.13           O  
-ANISOU  244  OD1 ASN A 261     7030   7395   6523   2254     11   1548       O  
-ATOM    245  ND2 ASN A 261      53.813  -9.735  29.753  1.00 54.01           N  
-ANISOU  245  ND2 ASN A 261     6987   7342   6193   2337    160   1708       N  
-ATOM    246  N   GLN A 262      54.977  -5.375  26.890  1.00 45.12           N  
-ANISOU  246  N   GLN A 262     6710   5741   4691   1738    199   1571       N  
-ATOM    247  CA  GLN A 262      54.741  -3.982  26.519  1.00 43.29           C  
-ANISOU  247  CA  GLN A 262     6809   5116   4524   1633    -42    806       C  
-ATOM    248  C   GLN A 262      53.665  -3.903  25.442  1.00 39.95           C  
-ANISOU  248  C   GLN A 262     6488   4687   4002   1586   -141   -111       C  
-ATOM    249  O   GLN A 262      53.852  -4.363  24.315  1.00 41.68           O  
-ANISOU  249  O   GLN A 262     6556   4776   4503   1756    167   -740       O  
-ATOM    250  CB  GLN A 262      56.030  -3.284  26.073  1.00 45.04           C  
-ANISOU  250  CB  GLN A 262     7200   4881   5030   1354    -58    683       C  
-ATOM    251  CG  GLN A 262      56.617  -3.796  24.775  1.00 45.96           C  
-ANISOU  251  CG  GLN A 262     7590   4607   5266   1121   -267    947       C  
-ATOM    252  CD  GLN A 262      57.888  -3.068  24.398  1.00 46.31           C  
-ANISOU  252  CD  GLN A 262     7927   4312   5357    888   -387   1330       C  
-ATOM    253  OE1 GLN A 262      58.230  -2.045  24.993  1.00 47.07           O  
-ANISOU  253  OE1 GLN A 262     7993   4312   5579    654   -605   1245       O  
-ATOM    254  NE2 GLN A 262      58.599  -3.591  23.407  1.00 46.51           N  
-ANISOU  254  NE2 GLN A 262     8127   4181   5364    793   -419   1615       N  
-ATOM    255  N   VAL A 263      52.535  -3.316  25.818  1.00 34.96           N  
-ANISOU  255  N   VAL A 263     6064   3754   3466   1446   -680     68       N  
-ATOM    256  CA  VAL A 263      51.328  -3.325  25.014  1.00 29.69           C  
-ANISOU  256  CA  VAL A 263     5538   3098   2644   1375   -281    227       C  
-ATOM    257  C   VAL A 263      51.321  -2.148  24.046  1.00 23.66           C  
-ANISOU  257  C   VAL A 263     4869   1921   2198    885   -545    -65       C  
-ATOM    258  O   VAL A 263      51.467  -1.001  24.460  1.00 26.63           O  
-ANISOU  258  O   VAL A 263     5177   2380   2559    954   -916   -317       O  
-ATOM    259  CB  VAL A 263      50.090  -3.235  25.930  1.00 26.63           C  
-ANISOU  259  CB  VAL A 263     5429   2781   1909    719    -25    742       C  
-ATOM    260  CG1 VAL A 263      48.800  -3.223  25.120  1.00 30.48           C  
-ANISOU  260  CG1 VAL A 263     5827   2778   2976   1042    -69    604       C  
-ATOM    261  CG2 VAL A 263      50.097  -4.382  26.941  1.00 29.34           C  
-ANISOU  261  CG2 VAL A 263     5898   2744   2505   1191   -156    485       C  
-ATOM    262  N   PRO A 264      51.170  -2.425  22.743  1.00 18.42           N  
-ANISOU  262  N   PRO A 264     3653   1328   2016    180   -321    113       N  
-ATOM    263  CA  PRO A 264      51.038  -1.296  21.818  1.00 17.12           C  
-ANISOU  263  CA  PRO A 264     3028   1408   2070    -48   -281    170       C  
-ATOM    264  C   PRO A 264      49.636  -0.695  21.869  1.00 16.25           C  
-ANISOU  264  C   PRO A 264     2849   1225   2098   -232    154     87       C  
-ATOM    265  O   PRO A 264      48.638  -1.424  21.871  1.00 16.07           O  
-ANISOU  265  O   PRO A 264     2602   1358   2145   -486     96    142       O  
-ATOM    266  CB  PRO A 264      51.292  -1.939  20.450  1.00 16.08           C  
-ANISOU  266  CB  PRO A 264     2767   1466   1876   -420   -258     43       C  
-ATOM    267  CG  PRO A 264      50.825  -3.339  20.616  1.00 15.84           C  
-ANISOU  267  CG  PRO A 264     2808   1374   1837   -532      8     -4       C  
-ATOM    268  CD  PRO A 264      51.166  -3.721  22.038  1.00 17.15           C  
-ANISOU  268  CD  PRO A 264     3281   1067   2168   -157    177     98       C  
-ATOM    269  N   GLN A 265      49.569   0.630  21.923  1.00 15.15           N  
-ANISOU  269  N   GLN A 265     2749   1169   1838    -33    -40    -10       N  
-ATOM    270  CA  GLN A 265      48.303   1.336  21.802  1.00 15.18           C  
-ANISOU  270  CA  GLN A 265     2657   1617   1494   -179    105    154       C  
-ATOM    271  C   GLN A 265      48.560   2.594  20.987  1.00 13.82           C  
-ANISOU  271  C   GLN A 265     2289   1503   1457   -160    186     82       C  
-ATOM    272  O   GLN A 265      48.187   3.707  21.374  1.00 13.97           O  
-ANISOU  272  O   GLN A 265     2190   1498   1618   -140    327   -191       O  
-ATOM    273  CB  GLN A 265      47.690   1.660  23.170  1.00 16.95           C  
-ANISOU  273  CB  GLN A 265     2763   1871   1804   -328    392    217       C  
-ATOM    274  CG  GLN A 265      46.275   2.220  23.053  1.00 18.15           C  
-ANISOU  274  CG  GLN A 265     2945   2139   1811   -285    909     65       C  
-ATOM    275  CD  GLN A 265      45.571   2.399  24.382  1.00 21.07           C  
-ANISOU  275  CD  GLN A 265     3328   2152   2526   -358    633     -1       C  
-ATOM    276  OE1 GLN A 265      46.142   2.161  25.446  1.00 22.22           O  
-ANISOU  276  OE1 GLN A 265     3662   2514   2266   -265    756   -252       O  
-ATOM    277  NE2 GLN A 265      44.312   2.824  24.323  1.00 21.20           N  
-ANISOU  277  NE2 GLN A 265     3503   1837   2713   -251    861    198       N  
-ATOM    278  N   PHE A 266      49.222   2.402  19.852  1.00 12.43           N  
-ANISOU  278  N   PHE A 266     1860   1324   1538   -270    162     78       N  
-ATOM    279  CA  PHE A 266      49.518   3.503  18.952  1.00 10.79           C  
-ANISOU  279  CA  PHE A 266     1679   1080   1339     17     65    221       C  
-ATOM    280  C   PHE A 266      48.208   4.140  18.507  1.00 10.60           C  
-ANISOU  280  C   PHE A 266     1601    856   1568   -180    -91   -106       C  
-ATOM    281  O   PHE A 266      47.177   3.463  18.429  1.00 11.80           O  
-ANISOU  281  O   PHE A 266     1929    919   1633   -150    131     -6       O  
-ATOM    282  CB  PHE A 266      50.317   3.009  17.746  1.00 11.28           C  
-ANISOU  282  CB  PHE A 266     1702   1064   1518    206    255    122       C  
-ATOM    283  CG  PHE A 266      51.532   2.209  18.119  1.00 11.31           C  
-ANISOU  283  CG  PHE A 266     1639   1023   1636    -20      4     66       C  
-ATOM    284  CD1 PHE A 266      52.271   2.538  19.244  1.00 11.93           C  
-ANISOU  284  CD1 PHE A 266     1543   1252   1738    147   -127     64       C  
-ATOM    285  CD2 PHE A 266      51.918   1.115  17.359  1.00 11.51           C  
-ANISOU  285  CD2 PHE A 266     1579   1027   1766    268      5    128       C  
-ATOM    286  CE1 PHE A 266      53.388   1.788  19.603  1.00 12.59           C  
-ANISOU  286  CE1 PHE A 266     1667   1254   1863     98    165   -332       C  
-ATOM    287  CE2 PHE A 266      53.030   0.374  17.703  1.00 11.38           C  
-ANISOU  287  CE2 PHE A 266     1626   1093   1606    217    -27     38       C  
-ATOM    288  CZ  PHE A 266      53.759   0.699  18.835  1.00 11.79           C  
-ANISOU  288  CZ  PHE A 266     1625   1231   1624    -49    171     23       C  
-ATOM    289  N   GLN A 267      48.238   5.442  18.236  1.00 10.76           N  
-ANISOU  289  N   GLN A 267     1545    895   1648     37   -121    -50       N  
-ATOM    290  CA  GLN A 267      47.043   6.135  17.781  1.00 10.30           C  
-ANISOU  290  CA  GLN A 267     1493    894   1525    126     79   -120       C  
-ATOM    291  C   GLN A 267      47.090   6.408  16.284  1.00 10.51           C  
-ANISOU  291  C   GLN A 267     1455    861   1677     91    257    -61       C  
-ATOM    292  O   GLN A 267      46.056   6.661  15.660  1.00 11.19           O  
-ANISOU  292  O   GLN A 267     1409   1135   1708     97     47    -97       O  
-ATOM    293  CB  GLN A 267      46.837   7.421  18.576  1.00 10.75           C  
-ANISOU  293  CB  GLN A 267     1766   1010   1306    128    126   -348       C  
-ATOM    294  CG  GLN A 267      46.579   7.144  20.043  1.00 11.78           C  
-ANISOU  294  CG  GLN A 267     1804   1207   1463   -228    529   -136       C  
-ATOM    295  CD  GLN A 267      45.390   6.226  20.235  1.00 13.45           C  
-ANISOU  295  CD  GLN A 267     1974   1265   1869     52    253     32       C  
-ATOM    296  OE1 GLN A 267      44.290   6.517  19.764  1.00 14.45           O  
-ANISOU  296  OE1 GLN A 267     1965   1416   2108     36    411     37       O  
-ATOM    297  NE2 GLN A 267      45.606   5.099  20.913  1.00 14.11           N  
-ANISOU  297  NE2 GLN A 267     2380   1184   1795   -140    518      1       N  
-ATOM    298  N   ASN A 268      48.296   6.364  15.723  1.00 10.10           N  
-ANISOU  298  N   ASN A 268     1539    837   1459     33    157    -62       N  
-ATOM    299  CA  ASN A 268      48.478   6.411  14.282  1.00 10.17           C  
-ANISOU  299  CA  ASN A 268     1454    805   1605   -228    229   -138       C  
-ATOM    300  C   ASN A 268      48.687   5.003  13.723  1.00 10.69           C  
-ANISOU  300  C   ASN A 268     1415    869   1777    -27    -37   -526       C  
-ATOM    301  O   ASN A 268      49.057   4.086  14.462  1.00 11.61           O  
-ANISOU  301  O   ASN A 268     1526    982   1904    126    121     22       O  
-ATOM    302  CB  ASN A 268      49.621   7.355  13.911  1.00 10.60           C  
-ANISOU  302  CB  ASN A 268     1493    760   1772      5    119   -201       C  
-ATOM    303  CG  ASN A 268      49.247   8.812  14.116  1.00  9.28           C  
-ANISOU  303  CG  ASN A 268     1221    835   1468   -188      9   -292       C  
-ATOM    304  OD1 ASN A 268      48.112   9.208  13.839  1.00 11.44           O  
-ANISOU  304  OD1 ASN A 268     1144   1248   1954     76    165   -291       O  
-ATOM    305  ND2 ASN A 268      50.183   9.609  14.617  1.00 10.43           N  
-ANISOU  305  ND2 ASN A 268     1185    958   1821    -17     17   -234       N  
-ATOM    306  N   GLY A 269      48.417   4.834  12.431  1.00  9.31           N  
-ANISOU  306  N   GLY A 269      942    858   1738   -145    -40   -547       N  
-ATOM    307  CA  GLY A 269      48.439   3.524  11.790  1.00  9.72           C  
-ANISOU  307  CA  GLY A 269     1197    755   1740   -217    146   -316       C  
-ATOM    308  C   GLY A 269      47.340   2.586  12.257  1.00  9.37           C  
-ANISOU  308  C   GLY A 269     1143    749   1669    -10    253      8       C  
-ATOM    309  O   GLY A 269      47.488   1.366  12.122  1.00 12.71           O  
-ANISOU  309  O   GLY A 269     1535    770   2524      6    396   -113       O  
-ATOM    310  N   ARG A 270      46.250   3.137  12.798  1.00 10.04           N  
-ANISOU  310  N   ARG A 270     1092   1031   1692   -254    153     59       N  
-ATOM    311  CA  ARG A 270      45.157   2.332  13.343  1.00  9.95           C  
-ANISOU  311  CA  ARG A 270     1125   1136   1518    -88    147   -206       C  
-ATOM    312  C   ARG A 270      43.927   2.369  12.437  1.00 10.03           C  
-ANISOU  312  C   ARG A 270     1239    963   1607   -146    -35   -239       C  
-ATOM    313  O   ARG A 270      43.393   3.444  12.141  1.00 11.50           O  
-ANISOU  313  O   ARG A 270     1336   1167   1865     15    127    -86       O  
-ATOM    314  CB  ARG A 270      44.775   2.813  14.748  1.00 11.49           C  
-ANISOU  314  CB  ARG A 270     1252   1377   1737    -13    221   -135       C  
-ATOM    315  CG  ARG A 270      45.930   2.846  15.744  1.00 10.97           C  
-ANISOU  315  CG  ARG A 270     1222   1056   1888     70   -131    225       C  
-ATOM    316  CD  ARG A 270      46.513   1.445  16.000  1.00 10.97           C  
-ANISOU  316  CD  ARG A 270     1471    925   1770   -147    306    318       C  
-ATOM    317  NE  ARG A 270      45.522   0.478  16.487  1.00 12.59           N  
-ANISOU  317  NE  ARG A 270     1720   1111   1951   -161    230    215       N  
-ATOM    318  CZ  ARG A 270      45.260   0.245  17.774  1.00 12.75           C  
-ANISOU  318  CZ  ARG A 270     1871    939   2035   -295    -91    116       C  
-ATOM    319  NH1 ARG A 270      45.922   0.897  18.721  1.00 12.64           N  
-ANISOU  319  NH1 ARG A 270     1758   1209   1834   -139      3    147       N  
-ATOM    320  NH2 ARG A 270      44.343  -0.656  18.117  1.00 14.15           N  
-ANISOU  320  NH2 ARG A 270     1879   1132   2366   -238    387    161       N  
-ATOM    321  N   VAL A 271      43.493   1.187  12.006  1.00 10.30           N  
-ANISOU  321  N   VAL A 271      993   1308   1612   -297    -75   -214       N  
-ATOM    322  CA  VAL A 271      42.350   1.028  11.110  1.00 10.96           C  
-ANISOU  322  CA  VAL A 271     1049   1171   1943   -340     -2    -34       C  
-ATOM    323  C   VAL A 271      41.890  -0.427  11.200  1.00 10.93           C  
-ANISOU  323  C   VAL A 271     1068   1110   1973   -432     91   -206       C  
-ATOM    324  O   VAL A 271      42.697  -1.321  11.427  1.00 12.77           O  
-ANISOU  324  O   VAL A 271     1322   1100   2428     23    -85    -82       O  
-ATOM    325  CB  VAL A 271      42.743   1.367   9.648  1.00 11.96           C  
-ANISOU  325  CB  VAL A 271     1140   1397   2006    -30     46    219       C  
-ATOM    326  CG1 VAL A 271      43.749   0.347   9.099  1.00 13.89           C  
-ANISOU  326  CG1 VAL A 271     1298   1581   2396    236    367    -92       C  
-ATOM    327  CG2 VAL A 271      41.522   1.472   8.746  1.00 13.89           C  
-ANISOU  327  CG2 VAL A 271     1437   1576   2263     45   -280   -138       C  
-ATOM    328  N   THR A 272      40.591  -0.661  11.059  1.00 11.98           N  
-ANISOU  328  N   THR A 272     1166   1385   2001   -576    190    -35       N  
-ATOM    329  CA  THR A 272      40.100  -2.026  10.972  1.00 12.46           C  
-ANISOU  329  CA  THR A 272     1198   1249   2288   -521    134    -74       C  
-ATOM    330  C   THR A 272      40.361  -2.575   9.568  1.00 12.25           C  
-ANISOU  330  C   THR A 272     1325   1215   2114   -407   -103      4       C  
-ATOM    331  O   THR A 272      40.592  -1.815   8.618  1.00 12.77           O  
-ANISOU  331  O   THR A 272     1398   1259   2193   -384    -76     14       O  
-ATOM    332  CB  THR A 272      38.601  -2.104  11.249  1.00 14.76           C  
-ANISOU  332  CB  THR A 272     1477   1601   2529   -246    365     96       C  
-ATOM    333  OG1 THR A 272      37.899  -1.310  10.282  1.00 15.34           O  
-ANISOU  333  OG1 THR A 272     1336   1428   3063   -187     56     93       O  
-ATOM    334  CG2 THR A 272      38.292  -1.589  12.646  1.00 15.70           C  
-ANISOU  334  CG2 THR A 272     1586   1743   2636   -209    463   -290       C  
-ATOM    335  N   LEU A 273      40.317  -3.895   9.422  1.00 13.03           N  
-ANISOU  335  N   LEU A 273     1362   1326   2261   -331   -354   -194       N  
-ATOM    336  CA  LEU A 273      40.511  -4.488   8.100  1.00 13.28           C  
-ANISOU  336  CA  LEU A 273     1465   1335   2244    -19   -275   -206       C  
-ATOM    337  C   LEU A 273      39.427  -4.068   7.113  1.00 14.20           C  
-ANISOU  337  C   LEU A 273     1415   1450   2530   -191   -367    -60       C  
-ATOM    338  O   LEU A 273      39.654  -4.075   5.895  1.00 15.16           O  
-ANISOU  338  O   LEU A 273     1606   1746   2409    -47   -404     69       O  
-ATOM    339  CB  LEU A 273      40.594  -6.015   8.178  1.00 13.11           C  
-ANISOU  339  CB  LEU A 273     1269   1140   2570   -218   -377   -180       C  
-ATOM    340  CG  LEU A 273      41.752  -6.549   9.018  1.00 14.14           C  
-ANISOU  340  CG  LEU A 273     1223   1437   2710   -425   -420   -307       C  
-ATOM    341  CD1 LEU A 273      41.829  -8.065   8.867  1.00 14.36           C  
-ANISOU  341  CD1 LEU A 273     1714   1050   2691   -279   -215   -302       C  
-ATOM    342  CD2 LEU A 273      43.076  -5.894   8.613  1.00 14.40           C  
-ANISOU  342  CD2 LEU A 273     1251   1707   2512   -356     -4   -102       C  
-ATOM    343  N   ASP A 274      38.250  -3.709   7.625  1.00 14.21           N  
-ANISOU  343  N   ASP A 274     1133   1578   2687   -392   -587      1       N  
-ATOM    344  CA  ASP A 274      37.188  -3.240   6.735  1.00 15.90           C  
-ANISOU  344  CA  ASP A 274     1395   1741   2906   -408   -242     31       C  
-ATOM    345  C   ASP A 274      37.185  -1.716   6.510  1.00 15.21           C  
-ANISOU  345  C   ASP A 274     1561   1657   2560   -351   -278    -21       C  
-ATOM    346  O   ASP A 274      36.233  -1.165   5.958  1.00 18.08           O  
-ANISOU  346  O   ASP A 274     1718   2152   2997     -1   -555     76       O  
-ATOM    347  CB  ASP A 274      35.805  -3.812   7.108  1.00 16.75           C  
-ANISOU  347  CB  ASP A 274     1404   1989   2971   -456   -235   -106       C  
-ATOM    348  CG  ASP A 274      35.244  -3.273   8.421  1.00 18.82           C  
-ANISOU  348  CG  ASP A 274     1542   2247   3362   -626   -155     21       C  
-ATOM    349  OD1 ASP A 274      35.805  -2.337   9.017  1.00 19.09           O  
-ANISOU  349  OD1 ASP A 274     1549   2405   3297   -505   -144   -163       O  
-ATOM    350  OD2 ASP A 274      34.187  -3.791   8.843  1.00 22.78           O  
-ANISOU  350  OD2 ASP A 274     1975   2477   4202   -709    196   -249       O  
-ATOM    351  N   GLY A 275      38.265  -1.049   6.920  1.00 13.90           N  
-ANISOU  351  N   GLY A 275     1511   1481   2290   -272    -14     88       N  
-ATOM    352  CA  GLY A 275      38.506   0.331   6.524  1.00 14.03           C  
-ANISOU  352  CA  GLY A 275     1561   1445   2324    -73    -51     83       C  
-ATOM    353  C   GLY A 275      38.002   1.443   7.434  1.00 14.70           C  
-ANISOU  353  C   GLY A 275     1390   1849   2345   -145     49    -22       C  
-ATOM    354  O   GLY A 275      37.818   2.574   6.976  1.00 17.17           O  
-ANISOU  354  O   GLY A 275     1781   1953   2789      5   -100    191       O  
-ATOM    355  N   GLN A 276      37.785   1.139   8.712  1.00 14.00           N  
-ANISOU  355  N   GLN A 276     1272   1829   2216   -169   -116   -348       N  
-ATOM    356  CA  GLN A 276      37.353   2.145   9.685  1.00 14.30           C  
-ANISOU  356  CA  GLN A 276     1298   1626   2507   -269    147   -446       C  
-ATOM    357  C   GLN A 276      38.553   2.727  10.424  1.00 13.64           C  
-ANISOU  357  C   GLN A 276     1293   1425   2465    -99   -111   -245       C  
-ATOM    358  O   GLN A 276      39.208   2.027  11.204  1.00 14.99           O  
-ANISOU  358  O   GLN A 276     1646   1478   2569    282   -120    -97       O  
-ATOM    359  CB  GLN A 276      36.381   1.539  10.701  1.00 17.16           C  
-ANISOU  359  CB  GLN A 276     1479   1933   3106   -495    462   -452       C  
-ATOM    360  CG  GLN A 276      35.121   0.940  10.102  1.00 22.96           C  
-ANISOU  360  CG  GLN A 276     1927   2449   4347   -524    612   -523       C  
-ATOM    361  CD  GLN A 276      34.272   0.218  11.139  1.00 29.06           C  
-ANISOU  361  CD  GLN A 276     2830   2922   5289    -30    714   -533       C  
-ATOM    362  OE1 GLN A 276      34.144  -1.010  11.113  1.00 32.12           O  
-ANISOU  362  OE1 GLN A 276     3272   3218   5712     44    500   -677       O  
-ATOM    363  NE2 GLN A 276      33.686   0.981  12.058  1.00 30.45           N  
-ANISOU  363  NE2 GLN A 276     3108   2968   5491     23    894   -426       N  
-ATOM    364  N   LEU A 277      38.850   3.998  10.166  1.00 13.04           N  
-ANISOU  364  N   LEU A 277     1228   1389   2338    -41   -172   -415       N  
-ATOM    365  CA  LEU A 277      39.966   4.670  10.819  1.00 12.85           C  
-ANISOU  365  CA  LEU A 277     1317   1443   2123     22   -102   -148       C  
-ATOM    366  C   LEU A 277      39.744   4.798  12.319  1.00 12.55           C  
-ANISOU  366  C   LEU A 277     1334   1555   1878   -110    -29   -206       C  
-ATOM    367  O   LEU A 277      38.619   5.031  12.769  1.00 14.67           O  
-ANISOU  367  O   LEU A 277     1337   1931   2306    -83     72   -262       O  
-ATOM    368  CB  LEU A 277      40.181   6.064  10.216  1.00 12.65           C  
-ANISOU  368  CB  LEU A 277     1316   1238   2252     43     45    -22       C  
-ATOM    369  CG  LEU A 277      40.662   6.072   8.762  1.00 12.31           C  
-ANISOU  369  CG  LEU A 277     1110   1635   1933    108    -45    -47       C  
-ATOM    370  CD1 LEU A 277      40.490   7.446   8.143  1.00 13.76           C  
-ANISOU  370  CD1 LEU A 277     1485   1350   2392    295     72    215       C  
-ATOM    371  CD2 LEU A 277      42.110   5.607   8.677  1.00 14.03           C  
-ANISOU  371  CD2 LEU A 277     1084   1657   2590    -25   -226   -217       C  
-ATOM    372  N   GLN A 278      40.830   4.682  13.081  1.00 12.18           N  
-ANISOU  372  N   GLN A 278     1365   1514   1748   -180     58   -182       N  
-ATOM    373  CA  GLN A 278      40.768   4.816  14.535  1.00 12.59           C  
-ANISOU  373  CA  GLN A 278     1527   1339   1918   -309   -145   -152       C  
-ATOM    374  C   GLN A 278      41.820   5.783  15.061  1.00 12.52           C  
-ANISOU  374  C   GLN A 278     1435   1427   1895   -226    173   -349       C  
-ATOM    375  O   GLN A 278      42.778   6.107  14.363  1.00 12.08           O  
-ANISOU  375  O   GLN A 278     1356   1373   1859    -50    123     22       O  
-ATOM    376  CB  GLN A 278      40.951   3.456  15.197  1.00 13.56           C  
-ANISOU  376  CB  GLN A 278     1685   1231   2237   -418      4    171       C  
-ATOM    377  CG  GLN A 278      39.889   2.444  14.813  1.00 15.07           C  
-ANISOU  377  CG  GLN A 278     1684   1267   2773   -575    158    189       C  
-ATOM    378  CD  GLN A 278      40.111   1.126  15.496  1.00 17.34           C  
-ANISOU  378  CD  GLN A 278     1914   1734   2941   -506    255    -38       C  
-ATOM    379  OE1 GLN A 278      41.217   0.836  15.936  1.00 19.32           O  
-ANISOU  379  OE1 GLN A 278     2097   1938   3305   -385     84    -13       O  
-ATOM    380  NE2 GLN A 278      39.060   0.314  15.591  1.00 18.58           N  
-ANISOU  380  NE2 GLN A 278     2151   1703   3204   -527    282     54       N  
-ATOM    381  N   GLY A 279      41.640   6.229  16.301  1.00 13.48           N  
-ANISOU  381  N   GLY A 279     1687   1450   1984   -147     -8   -480       N  
-ATOM    382  CA  GLY A 279      42.597   7.114  16.940  1.00 12.86           C  
-ANISOU  382  CA  GLY A 279     1436   1353   2098   -477    146   -166       C  
-ATOM    383  C   GLY A 279      42.772   8.408  16.177  1.00 12.48           C  
-ANISOU  383  C   GLY A 279     1441   1384   1916   -341    -90   -200       C  
-ATOM    384  O   GLY A 279      41.792   9.067  15.828  1.00 15.24           O  
-ANISOU  384  O   GLY A 279     1638   1732   2420    -94    151   -160       O  
-ATOM    385  N   THR A 280      44.025   8.771  15.918  1.00 11.43           N  
-ANISOU  385  N   THR A 280     1545   1106   1692    -39    116    -35       N  
-ATOM    386  CA  THR A 280      44.329   9.971  15.146  1.00 11.68           C  
-ANISOU  386  CA  THR A 280     1460   1133   1845    211     71     13       C  
-ATOM    387  C   THR A 280      44.733   9.622  13.713  1.00 10.18           C  
-ANISOU  387  C   THR A 280     1397    907   1565    112    -48   -109       C  
-ATOM    388  O   THR A 280      45.318  10.432  12.991  1.00 11.37           O  
-ANISOU  388  O   THR A 280     1343   1100   1875    114    154    -82       O  
-ATOM    389  CB  THR A 280      45.442  10.790  15.821  1.00 12.22           C  
-ANISOU  389  CB  THR A 280     1218   1360   2065    199    -91   -421       C  
-ATOM    390  OG1 THR A 280      46.591   9.954  16.023  1.00 11.27           O  
-ANISOU  390  OG1 THR A 280     1355   1148   1780    295    -21   -274       O  
-ATOM    391  CG2 THR A 280      44.962  11.307  17.169  1.00 14.26           C  
-ANISOU  391  CG2 THR A 280     1558   1662   2197    304    348   -769       C  
-ATOM    392  N   THR A 281      44.406   8.410  13.289  1.00 10.42           N  
-ANISOU  392  N   THR A 281     1334   1125   1499     62    -78   -207       N  
-ATOM    393  CA  THR A 281      44.857   7.936  11.989  1.00 10.38           C  
-ANISOU  393  CA  THR A 281     1428    869   1645     72     -1   -176       C  
-ATOM    394  C   THR A 281      44.082   8.542  10.830  1.00 11.54           C  
-ANISOU  394  C   THR A 281     1664   1228   1492    197   -128    125       C  
-ATOM    395  O   THR A 281      42.853   8.640  10.863  1.00 13.70           O  
-ANISOU  395  O   THR A 281     1577   1616   2013    427    -12     22       O  
-ATOM    396  CB  THR A 281      44.796   6.396  11.909  1.00 10.11           C  
-ANISOU  396  CB  THR A 281     1419    807   1613    -59     87   -321       C  
-ATOM    397  OG1 THR A 281      45.561   5.857  12.990  1.00 10.48           O  
-ANISOU  397  OG1 THR A 281     1344   1151   1485     34   -249    -31       O  
-ATOM    398  CG2 THR A 281      45.369   5.891  10.587  1.00 11.08           C  
-ANISOU  398  CG2 THR A 281     1684    944   1583    284    259    -74       C  
-ATOM    399  N   THR A 282      44.811   8.945   9.797  1.00 11.68           N  
-ANISOU  399  N   THR A 282     1800   1089   1549    286   -284    152       N  
-ATOM    400  CA  THR A 282      44.164   9.376   8.574  1.00 12.27           C  
-ANISOU  400  CA  THR A 282     1804   1316   1543    389    -11    293       C  
-ATOM    401  C   THR A 282      44.779   8.671   7.364  1.00 11.72           C  
-ANISOU  401  C   THR A 282     1458   1289   1704    126    248    267       C  
-ATOM    402  O   THR A 282      45.524   7.703   7.518  1.00 11.57           O  
-ANISOU  402  O   THR A 282     1420   1307   1667    221    -89    146       O  
-ATOM    403  CB  THR A 282      44.119  10.923   8.461  1.00 13.56           C  
-ANISOU  403  CB  THR A 282     1633   1543   1977    457     -3    405       C  
-ATOM    404  OG1 THR A 282      43.217  11.313   7.411  1.00 14.10           O  
-ANISOU  404  OG1 THR A 282     1912   1422   2021    515    277    124       O  
-ATOM    405  CG2 THR A 282      45.512  11.512   8.227  1.00 15.43           C  
-ANISOU  405  CG2 THR A 282     1415   1529   2918   -152    244    510       C  
-ATOM    406  N   VAL A 283      44.450   9.137   6.167  1.00 10.43           N  
-ANISOU  406  N   VAL A 283     1450   1224   1288    133    255    -22       N  
-ATOM    407  CA  VAL A 283      44.725   8.392   4.950  1.00 10.85           C  
-ANISOU  407  CA  VAL A 283     1441   1321   1360    110    -22    143       C  
-ATOM    408  C   VAL A 283      46.143   8.582   4.407  1.00 10.12           C  
-ANISOU  408  C   VAL A 283     1193   1028   1624     17     80    214       C  
-ATOM    409  O   VAL A 283      46.821   7.601   4.068  1.00 11.48           O  
-ANISOU  409  O   VAL A 283     1408   1241   1714    258   -106    139       O  
-ATOM    410  CB  VAL A 283      43.687   8.756   3.860  1.00 11.72           C  
-ANISOU  410  CB  VAL A 283     1535   1755   1162    114     -2    -73       C  
-ATOM    411  CG1 VAL A 283      44.037   8.119   2.529  1.00 15.13           C  
-ANISOU  411  CG1 VAL A 283     1846   2123   1779    420   -435   -188       C  
-ATOM    412  CG2 VAL A 283      42.283   8.354   4.301  1.00 15.66           C  
-ANISOU  412  CG2 VAL A 283     1534   1735   2680     25    120    194       C  
-ATOM    413  N   SER A 284      46.590   9.832   4.306  1.00 10.31           N  
-ANISOU  413  N   SER A 284     1261   1092   1563   -130     87    252       N  
-ATOM    414  CA  SER A 284      47.850  10.125   3.626  1.00 10.37           C  
-ANISOU  414  CA  SER A 284     1286   1103   1550    -55    101    236       C  
-ATOM    415  C   SER A 284      49.074  10.130   4.538  1.00 10.10           C  
-ANISOU  415  C   SER A 284     1188   1234   1413     93     76    142       C  
-ATOM    416  O   SER A 284      49.043  10.685   5.647  1.00 10.77           O  
-ANISOU  416  O   SER A 284     1300   1322   1471    121     97    -18       O  
-ATOM    417  CB  SER A 284      47.761  11.472   2.896  1.00 11.07           C  
-ANISOU  417  CB  SER A 284     1391   1076   1738   -139    495    521       C  
-ATOM    418  OG  SER A 284      48.981  11.763   2.222  1.00 10.38           O  
-ANISOU  418  OG  SER A 284     1508    996   1439     37     48    235       O  
-ATOM    419  N   ALA A 285      50.168   9.546   4.051  1.00 10.03           N  
-ANISOU  419  N   ALA A 285     1038   1119   1653     38    108     54       N  
-ATOM    420  CA  ALA A 285      51.436   9.606   4.773  1.00 10.22           C  
-ANISOU  420  CA  ALA A 285      846   1152   1884    141      9   -134       C  
-ATOM    421  C   ALA A 285      51.925  11.045   4.927  1.00 10.22           C  
-ANISOU  421  C   ALA A 285     1249   1050   1582     65    -15    175       C  
-ATOM    422  O   ALA A 285      52.746  11.328   5.791  1.00 11.92           O  
-ANISOU  422  O   ALA A 285     1388   1323   1819    112   -103    -92       O  
-ATOM    423  CB  ALA A 285      52.493   8.756   4.081  1.00 11.60           C  
-ANISOU  423  CB  ALA A 285     1064   1405   1936    433    243    -57       C  
-ATOM    424  N   ALA A 286      51.420  11.950   4.088  1.00 10.08           N  
-ANISOU  424  N   ALA A 286     1704    744   1380    122     66     59       N  
-ATOM    425  CA  ALA A 286      51.767  13.370   4.206  1.00 11.38           C  
-ANISOU  425  CA  ALA A 286     1883    980   1462    119     73    240       C  
-ATOM    426  C   ALA A 286      51.280  14.000   5.514  1.00 11.47           C  
-ANISOU  426  C   ALA A 286     1865   1375   1118     94    248    -30       C  
-ATOM    427  O   ALA A 286      51.716  15.091   5.876  1.00 14.39           O  
-ANISOU  427  O   ALA A 286     2162   1212   2093   -289    214     19       O  
-ATOM    428  CB  ALA A 286      51.224  14.168   3.009  1.00 11.98           C  
-ANISOU  428  CB  ALA A 286     2016    930   1607    -61   -215    270       C  
-ATOM    429  N   CYS A 287      50.401  13.313   6.236  1.00  9.89           N  
-ANISOU  429  N   CYS A 287     1320   1353   1083    223    113    160       N  
-ATOM    430  CA  CYS A 287      49.876  13.856   7.483  1.00  9.72           C  
-ANISOU  430  CA  CYS A 287     1052   1409   1230    105    156    131       C  
-ATOM    431  C   CYS A 287      50.582  13.348   8.738  1.00  9.55           C  
-ANISOU  431  C   CYS A 287     1222   1138   1266    162   -290     -8       C  
-ATOM    432  O   CYS A 287      50.341  13.846   9.834  1.00 10.61           O  
-ANISOU  432  O   CYS A 287     1443   1064   1525    193   -143   -105       O  
-ATOM    433  CB  CYS A 287      48.381  13.544   7.597  1.00 11.34           C  
-ANISOU  433  CB  CYS A 287     1085   1521   1703    301   -106    238       C  
-ATOM    434  SG  CYS A 287      47.404  14.282   6.272  1.00 14.31           S  
-ANISOU  434  SG  CYS A 287     1576   2025   1837    500   -262     75       S  
-ATOM    435  N   ILE A 288      51.427  12.333   8.593  1.00  8.97           N  
-ANISOU  435  N   ILE A 288     1043    752   1612    132   -229    189       N  
-ATOM    436  CA  ILE A 288      51.954  11.646   9.761  1.00  8.92           C  
-ANISOU  436  CA  ILE A 288     1304    674   1410    213   -197   -112       C  
-ATOM    437  C   ILE A 288      52.888  12.513  10.603  1.00  9.33           C  
-ANISOU  437  C   ILE A 288     1453    678   1412    108   -403   -235       C  
-ATOM    438  O   ILE A 288      53.851  13.091  10.085  1.00 10.54           O  
-ANISOU  438  O   ILE A 288     1313    940   1750     93     12    -80       O  
-ATOM    439  CB  ILE A 288      52.688  10.354   9.352  1.00  8.51           C  
-ANISOU  439  CB  ILE A 288     1016    505   1711     45   -275   -106       C  
-ATOM    440  CG1 ILE A 288      51.732   9.392   8.637  1.00  9.98           C  
-ANISOU  440  CG1 ILE A 288     1288    735   1768   -113   -137   -217       C  
-ATOM    441  CG2 ILE A 288      53.318   9.683  10.576  1.00 10.07           C  
-ANISOU  441  CG2 ILE A 288     1283   1048   1493    414   -305    162       C  
-ATOM    442  CD1 ILE A 288      52.462   8.252   7.946  1.00 12.27           C  
-ANISOU  442  CD1 ILE A 288     1865   1036   1760    324   -248   -410       C  
-ATOM    443  N   ALA A 289      52.578  12.596  11.899  1.00  9.32           N  
-ANISOU  443  N   ALA A 289     1616    776   1149    248   -328   -341       N  
-ATOM    444  CA  ALA A 289      53.420  13.276  12.883  1.00  9.25           C  
-ANISOU  444  CA  ALA A 289     1310    725   1480    225   -420    -93       C  
-ATOM    445  C   ALA A 289      53.551  14.768  12.611  1.00  9.26           C  
-ANISOU  445  C   ALA A 289     1095    751   1671     40   -114     58       C  
-ATOM    446  O   ALA A 289      54.593  15.368  12.849  1.00 14.64           O  
-ANISOU  446  O   ALA A 289     1484   1064   3013     74   -915    200       O  
-ATOM    447  CB  ALA A 289      54.795  12.603  12.986  1.00 11.11           C  
-ANISOU  447  CB  ALA A 289     1194    899   2126    214   -597    -96       C  
-ATOM    448  N   ARG A 290      52.470  15.358  12.118  1.00  9.46           N  
-ANISOU  448  N   ARG A 290     1129    711   1752    297   -142    -70       N  
-ATOM    449  CA  ARG A 290      52.412  16.795  11.887  1.00  9.12           C  
-ANISOU  449  CA  ARG A 290     1233    815   1417    402     45    -67       C  
-ATOM    450  C   ARG A 290      51.354  17.434  12.766  1.00  9.66           C  
-ANISOU  450  C   ARG A 290     1124    925   1622    132    -63     23       C  
-ATOM    451  O   ARG A 290      50.495  16.738  13.317  1.00  9.87           O  
-ANISOU  451  O   ARG A 290     1350    858   1541    139   -116    -50       O  
-ATOM    452  CB  ARG A 290      52.142  17.089  10.409  1.00 10.60           C  
-ANISOU  452  CB  ARG A 290     1448   1242   1335    256     23   -193       C  
-ATOM    453  CG  ARG A 290      53.303  16.666   9.512  1.00 12.25           C  
-ANISOU  453  CG  ARG A 290     1717   1550   1385    292    133      4       C  
-ATOM    454  CD  ARG A 290      53.068  17.008   8.054  1.00 16.38           C  
-ANISOU  454  CD  ARG A 290     2254   2365   1604    233    163   -202       C  
-ATOM    455  NE  ARG A 290      54.108  16.445   7.197  1.00 18.70           N  
-ANISOU  455  NE  ARG A 290     2519   2501   2084   -198    461    -32       N  
-ATOM    456  CZ  ARG A 290      55.060  17.155   6.598  1.00 21.97           C  
-ANISOU  456  CZ  ARG A 290     2930   2572   2846    -40     97   -710       C  
-ATOM    457  NH1 ARG A 290      55.121  18.469   6.765  1.00 24.12           N  
-ANISOU  457  NH1 ARG A 290     3395   2307   3461     21   -474   -199       N  
-ATOM    458  NH2 ARG A 290      55.956  16.546   5.825  1.00 21.98           N  
-ANISOU  458  NH2 ARG A 290     2982   2955   2415   -165    -49   -264       N  
-ATOM    459  N   MET A 291      51.441  18.755  12.900  1.00  9.52           N  
-ANISOU  459  N   MET A 291     1282    764   1569    338    -42   -123       N  
-ATOM    460  CA  MET A 291      50.447  19.556  13.606  1.00  8.98           C  
-ANISOU  460  CA  MET A 291     1291    779   1342    369   -132   -137       C  
-ATOM    461  C   MET A 291      50.174  20.815  12.808  1.00  9.55           C  
-ANISOU  461  C   MET A 291     1473    863   1290    527   -204     33       C  
-ATOM    462  O   MET A 291      50.969  21.213  11.950  1.00 10.20           O  
-ANISOU  462  O   MET A 291     1481    871   1524    342   -122    -15       O  
-ATOM    463  CB  MET A 291      50.953  19.979  14.986  1.00  9.57           C  
-ANISOU  463  CB  MET A 291     1303   1003   1331    337   -190    195       C  
-ATOM    464  CG  MET A 291      51.493  18.861  15.861  1.00  9.91           C  
-ANISOU  464  CG  MET A 291     1466   1137   1161    259   -195    -22       C  
-ATOM    465  SD  MET A 291      52.192  19.613  17.359  1.00 10.95           S  
-ANISOU  465  SD  MET A 291     1438   1055   1667    303   -238   -155       S  
-ATOM    466  CE  MET A 291      52.973  18.197  18.131  1.00 11.35           C  
-ANISOU  466  CE  MET A 291     1519   1174   1620    474   -412     30       C  
-ATOM    467  N   ARG A 292      49.058  21.459  13.122  1.00  9.38           N  
-ANISOU  467  N   ARG A 292     1327    634   1601    397    -59    -61       N  
-ATOM    468  CA  ARG A 292      48.738  22.756  12.547  1.00  9.23           C  
-ANISOU  468  CA  ARG A 292     1362    737   1408    475   -198    -98       C  
-ATOM    469  C   ARG A 292      48.023  23.591  13.589  1.00  8.97           C  
-ANISOU  469  C   ARG A 292     1274    808   1326    442     -1   -247       C  
-ATOM    470  O   ARG A 292      47.239  23.072  14.381  1.00 10.15           O  
-ANISOU  470  O   ARG A 292     1256   1008   1593    287     -7    -67       O  
-ATOM    471  CB  ARG A 292      47.856  22.609  11.303  1.00 10.16           C  
-ANISOU  471  CB  ARG A 292     1396    971   1493    443   -429    203       C  
-ATOM    472  CG  ARG A 292      47.477  23.942  10.655  1.00 10.38           C  
-ANISOU  472  CG  ARG A 292     1301   1126   1517    362    -54    162       C  
-ATOM    473  CD  ARG A 292      46.882  23.733   9.268  1.00 10.57           C  
-ANISOU  473  CD  ARG A 292     1398   1293   1325    464   -360    185       C  
-ATOM    474  NE  ARG A 292      46.470  25.000   8.666  1.00 11.76           N  
-ANISOU  474  NE  ARG A 292     1396   1365   1707    320   -315    177       N  
-ATOM    475  CZ  ARG A 292      46.325  25.199   7.363  1.00 12.33           C  
-ANISOU  475  CZ  ARG A 292     1426   1658   1602    417   -266     79       C  
-ATOM    476  NH1 ARG A 292      46.561  24.208   6.510  1.00 13.54           N  
-ANISOU  476  NH1 ARG A 292     1539   1825   1779    151     62   -232       N  
-ATOM    477  NH2 ARG A 292      45.949  26.393   6.914  1.00 14.33           N  
-ANISOU  477  NH2 ARG A 292     1800   1573   2070    465   -239    150       N  
-ATOM    478  N   GLY A 293      48.284  24.889  13.587  1.00 10.10           N  
-ANISOU  478  N   GLY A 293     1337    903   1598    552    -11   -233       N  
-ATOM    479  CA  GLY A 293      47.472  25.783  14.392  1.00 11.15           C  
-ANISOU  479  CA  GLY A 293     1407    895   1932    546     53   -152       C  
-ATOM    480  C   GLY A 293      48.069  27.159  14.527  1.00  9.97           C  
-ANISOU  480  C   GLY A 293     1251    793   1745    294    -82   -185       C  
-ATOM    481  O   GLY A 293      49.033  27.508  13.842  1.00 11.82           O  
-ANISOU  481  O   GLY A 293     1631   1020   1839    366    320   -154       O  
-ATOM    482  N   ARG A 294      47.492  27.944  15.431  1.00  9.77           N  
-ANISOU  482  N   ARG A 294     1284    946   1483    301    -33   -433       N  
-ATOM    483  CA  ARG A 294      47.896  29.332  15.606  1.00  9.82           C  
-ANISOU  483  CA  ARG A 294     1371    816   1544    465   -211   -302       C  
-ATOM    484  C   ARG A 294      48.718  29.456  16.871  1.00 10.08           C  
-ANISOU  484  C   ARG A 294     1336    889   1605    315    184   -316       C  
-ATOM    485  O   ARG A 294      48.303  29.011  17.938  1.00 10.90           O  
-ANISOU  485  O   ARG A 294     1509   1162   1469    339    -54   -166       O  
-ATOM    486  CB  ARG A 294      46.676  30.249  15.669  1.00 10.56           C  
-ANISOU  486  CB  ARG A 294     1289   1007   1715    627    -12    -21       C  
-ATOM    487  CG  ARG A 294      47.017  31.720  15.462  1.00 15.07           C  
-ANISOU  487  CG  ARG A 294     1646   1090   2991    495    203     37       C  
-ATOM    488  CD  ARG A 294      45.746  32.565  15.239  1.00 17.26           C  
-ANISOU  488  CD  ARG A 294     1790   1484   3283    670    -35   -473       C  
-ATOM    489  NE  ARG A 294      44.959  32.065  14.112  1.00 17.50           N  
-ANISOU  489  NE  ARG A 294     2012   2174   2461   1122   -201   -195       N  
-ATOM    490  CZ  ARG A 294      45.173  32.394  12.842  1.00 19.74           C  
-ANISOU  490  CZ  ARG A 294     2320   2174   3004    889   -730     15       C  
-ATOM    491  NH1 ARG A 294      46.128  33.258  12.529  1.00 20.72           N  
-ANISOU  491  NH1 ARG A 294     2599   2161   3113    680   -523   -170       N  
-ATOM    492  NH2 ARG A 294      44.427  31.864  11.881  1.00 20.11           N  
-ANISOU  492  NH2 ARG A 294     2707   2276   2659   1284   -448   -377       N  
-ATOM    493  N   ILE A 295      49.897  30.049  16.744  1.00 10.79           N  
-ANISOU  493  N   ILE A 295     1542    898   1658    334   -174   -224       N  
-ATOM    494  CA  ILE A 295      50.762  30.250  17.900  1.00 10.76           C  
-ANISOU  494  CA  ILE A 295     1451   1060   1577    263    -64   -211       C  
-ATOM    495  C   ILE A 295      50.219  31.387  18.761  1.00 11.16           C  
-ANISOU  495  C   ILE A 295     1552   1117   1570    446   -347    -93       C  
-ATOM    496  O   ILE A 295      49.822  32.438  18.249  1.00 11.82           O  
-ANISOU  496  O   ILE A 295     1669   1009   1812    403   -197    -79       O  
-ATOM    497  CB  ILE A 295      52.222  30.509  17.464  1.00 11.70           C  
-ANISOU  497  CB  ILE A 295     1444   1148   1853    218   -278   -592       C  
-ATOM    498  CG1 ILE A 295      52.806  29.211  16.887  1.00 12.32           C  
-ANISOU  498  CG1 ILE A 295     1329   1346   2004    493    -58   -645       C  
-ATOM    499  CG2 ILE A 295      53.069  30.999  18.637  1.00 13.28           C  
-ANISOU  499  CG2 ILE A 295     1861   1137   2046    244   -480   -414       C  
-ATOM    500  CD1 ILE A 295      54.199  29.346  16.290  1.00 13.35           C  
-ANISOU  500  CD1 ILE A 295     1400   1632   2040    536     80   -315       C  
-ATOM    501  N   PHE A 296      50.189  31.163  20.070  1.00 11.84           N  
-ANISOU  501  N   PHE A 296     1713   1234   1552    416   -189   -376       N  
-ATOM    502  CA  PHE A 296      49.741  32.177  21.012  1.00 11.13           C  
-ANISOU  502  CA  PHE A 296     1510   1181   1536    273   -136   -360       C  
-ATOM    503  C   PHE A 296      50.752  32.415  22.116  1.00 11.88           C  
-ANISOU  503  C   PHE A 296     1644   1337   1534    458   -366   -301       C  
-ATOM    504  O   PHE A 296      51.680  31.634  22.310  1.00 12.58           O  
-ANISOU  504  O   PHE A 296     1526   1395   1860    501   -279   -240       O  
-ATOM    505  CB  PHE A 296      48.379  31.803  21.612  1.00 12.85           C  
-ANISOU  505  CB  PHE A 296     1767   1307   1808    564   -122    145       C  
-ATOM    506  CG  PHE A 296      48.391  30.557  22.474  1.00 12.00           C  
-ANISOU  506  CG  PHE A 296     1822   1236   1500    392   -397   -557       C  
-ATOM    507  CD1 PHE A 296      48.824  30.603  23.796  1.00 12.76           C  
-ANISOU  507  CD1 PHE A 296     1855   1350   1644    484   -343     53       C  
-ATOM    508  CD2 PHE A 296      47.914  29.350  21.973  1.00 12.62           C  
-ANISOU  508  CD2 PHE A 296     1659   1006   2131    455   -260   -165       C  
-ATOM    509  CE1 PHE A 296      48.808  29.466  24.588  1.00 13.44           C  
-ANISOU  509  CE1 PHE A 296     1890   1535   1679    454   -307   -200       C  
-ATOM    510  CE2 PHE A 296      47.884  28.218  22.755  1.00 12.57           C  
-ANISOU  510  CE2 PHE A 296     1745   1378   1654    585   -237   -308       C  
-ATOM    511  CZ  PHE A 296      48.336  28.268  24.066  1.00 13.01           C  
-ANISOU  511  CZ  PHE A 296     1692   1370   1880    494    175   -142       C  
-ATOM    512  N   ASN A 297      50.558  33.511  22.836  1.00 13.56           N  
-ANISOU  512  N   ASN A 297     2211   1182   1759    427   -418   -511       N  
-ATOM    513  CA  ASN A 297      51.354  33.838  24.004  1.00 16.04           C  
-ANISOU  513  CA  ASN A 297     2672   1587   1836    678   -409   -527       C  
-ATOM    514  C   ASN A 297      50.388  34.384  25.031  1.00 17.14           C  
-ANISOU  514  C   ASN A 297     2921   2016   1576    968   -217   -621       C  
-ATOM    515  O   ASN A 297      49.740  35.406  24.806  1.00 18.48           O  
-ANISOU  515  O   ASN A 297     2815   1844   2363   1080   -211   -417       O  
-ATOM    516  CB  ASN A 297      52.423  34.883  23.655  1.00 19.86           C  
-ANISOU  516  CB  ASN A 297     2968   1737   2841    268  -1209   -893       C  
-ATOM    517  CG  ASN A 297      53.221  35.340  24.861  1.00 28.36           C  
-ANISOU  517  CG  ASN A 297     3728   2478   4568    556  -1869   -869       C  
-ATOM    518  OD1 ASN A 297      53.651  34.535  25.683  1.00 30.65           O  
-ANISOU  518  OD1 ASN A 297     4359   2868   4416    372  -1706  -1191       O  
-ATOM    519  ND2 ASN A 297      53.437  36.640  24.961  1.00 34.27           N  
-ANISOU  519  ND2 ASN A 297     4221   3082   5716    771  -2035  -1338       N  
-ATOM    520  N   ASN A 298      50.261  33.674  26.143  1.00 19.96           N  
-ANISOU  520  N   ASN A 298     3260   2449   1873   1285      2   -661       N  
-ATOM    521  CA  ASN A 298      49.325  34.061  27.185  1.00 26.60           C  
-ANISOU  521  CA  ASN A 298     4293   3567   2245   2219    259   -106       C  
-ATOM    522  C   ASN A 298      49.856  33.699  28.555  1.00 31.81           C  
-ANISOU  522  C   ASN A 298     5259   4268   2560   2669    351    -92       C  
-ATOM    523  O   ASN A 298      50.343  32.591  28.768  1.00 32.71           O  
-ANISOU  523  O   ASN A 298     5473   4528   2426   2861    374     88       O  
-ATOM    524  CB  ASN A 298      47.983  33.372  26.965  1.00 29.66           C  
-ANISOU  524  CB  ASN A 298     4332   3857   3081   2273   1210    879       C  
-ATOM    525  CG  ASN A 298      46.958  33.757  28.009  1.00 34.80           C  
-ANISOU  525  CG  ASN A 298     4522   4469   4231   2418   1558   1544       C  
-ATOM    526  OD1 ASN A 298      46.951  33.224  29.117  1.00 32.55           O  
-ANISOU  526  OD1 ASN A 298     4527   4227   3614   2408   1421   1274       O  
-ATOM    527  ND2 ASN A 298      46.082  34.688  27.658  1.00 39.55           N  
-ANISOU  527  ND2 ASN A 298     4769   5118   5138   2589   1690   1971       N  
-ATOM    528  N   ASN A 299      49.756  34.639  29.487  1.00 35.25           N  
-ANISOU  528  N   ASN A 299     5688   4843   2861   2780    234   -534       N  
-ATOM    529  CA  ASN A 299      50.151  34.387  30.864  1.00 38.41           C  
-ANISOU  529  CA  ASN A 299     6258   5444   2890   3143     60   -570       C  
-ATOM    530  C   ASN A 299      51.601  33.907  30.958  1.00 38.76           C  
-ANISOU  530  C   ASN A 299     6205   5353   3168   3094   -229   -909       C  
-ATOM    531  O   ASN A 299      51.926  33.042  31.769  1.00 39.88           O  
-ANISOU  531  O   ASN A 299     6454   5445   3251   3252    -29   -691       O  
-ATOM    532  CB  ASN A 299      49.198  33.369  31.498  1.00 41.05           C  
-ANISOU  532  CB  ASN A 299     6858   6096   2641   3119    334   -259       C  
-ATOM    533  CG  ASN A 299      49.291  33.342  33.012  1.00 45.98           C  
-ANISOU  533  CG  ASN A 299     7446   6653   3372   3198    526    -83       C  
-ATOM    534  OD1 ASN A 299      49.825  34.261  33.631  1.00 46.88           O  
-ANISOU  534  OD1 ASN A 299     7720   6713   3377   3216    754   -480       O  
-ATOM    535  ND2 ASN A 299      48.763  32.283  33.617  1.00 47.40           N  
-ANISOU  535  ND2 ASN A 299     7601   6764   3646   3200    530    416       N  
-ATOM    536  N   GLY A 300      52.465  34.469  30.114  1.00 38.47           N  
-ANISOU  536  N   GLY A 300     5857   5187   3573   2761   -490  -1449       N  
-ATOM    537  CA  GLY A 300      53.891  34.195  30.172  1.00 38.46           C  
-ANISOU  537  CA  GLY A 300     5752   4833   4029   2721   -946  -1579       C  
-ATOM    538  C   GLY A 300      54.351  32.916  29.491  1.00 36.67           C  
-ANISOU  538  C   GLY A 300     5451   4588   3893   2714  -1234  -1385       C  
-ATOM    539  O   GLY A 300      55.496  32.494  29.654  1.00 37.73           O  
-ANISOU  539  O   GLY A 300     5439   4677   4218   2594   -999  -1557       O  
-ATOM    540  N   ASN A 301      53.466  32.297  28.719  1.00 29.81           N  
-ANISOU  540  N   ASN A 301     4825   3990   2511   2259  -1234  -1168       N  
-ATOM    541  CA  ASN A 301      53.791  31.036  28.067  1.00 25.84           C  
-ANISOU  541  CA  ASN A 301     4554   3303   1959   1919  -1008   -672       C  
-ATOM    542  C   ASN A 301      53.262  30.964  26.646  1.00 19.09           C  
-ANISOU  542  C   ASN A 301     3412   2249   1591   1291   -828   -272       C  
-ATOM    543  O   ASN A 301      52.196  31.500  26.331  1.00 19.84           O  
-ANISOU  543  O   ASN A 301     3319   2407   1811   1598   -435   -352       O  
-ATOM    544  CB  ASN A 301      53.268  29.857  28.886  1.00 29.98           C  
-ANISOU  544  CB  ASN A 301     5196   3582   2611   1671  -1134   -243       C  
-ATOM    545  CG  ASN A 301      53.965  29.725  30.229  1.00 33.48           C  
-ANISOU  545  CG  ASN A 301     5646   4007   3069   1672   -976   -121       C  
-ATOM    546  OD1 ASN A 301      53.448  30.163  31.254  1.00 35.67           O  
-ANISOU  546  OD1 ASN A 301     5896   3945   3710   1525   -838   -832       O  
-ATOM    547  ND2 ASN A 301      55.149  29.125  30.224  1.00 35.64           N  
-ANISOU  547  ND2 ASN A 301     5930   4128   3481   1840  -1033     85       N  
-ATOM    548  N   TYR A 302      54.023  30.300  25.787  1.00 15.03           N  
-ANISOU  548  N   TYR A 302     2584   1432   1695    430   -327   -521       N  
-ATOM    549  CA  TYR A 302      53.638  30.143  24.394  1.00 12.71           C  
-ANISOU  549  CA  TYR A 302     1924   1227   1676    412   -177   -614       C  
-ATOM    550  C   TYR A 302      52.911  28.821  24.183  1.00 11.47           C  
-ANISOU  550  C   TYR A 302     1580   1216   1560    371   -575   -447       C  
-ATOM    551  O   TYR A 302      53.042  27.889  24.971  1.00 12.84           O  
-ANISOU  551  O   TYR A 302     1864   1208   1806    719   -293   -257       O  
-ATOM    552  CB  TYR A 302      54.870  30.215  23.490  1.00 13.64           C  
-ANISOU  552  CB  TYR A 302     1695   1428   2060    226   -230   -405       C  
-ATOM    553  CG  TYR A 302      55.614  31.531  23.585  1.00 14.85           C  
-ANISOU  553  CG  TYR A 302     1961   1212   2468    338   -372   -543       C  
-ATOM    554  CD1 TYR A 302      55.398  32.542  22.661  1.00 16.16           C  
-ANISOU  554  CD1 TYR A 302     2217   1365   2559    220   -214   -328       C  
-ATOM    555  CD2 TYR A 302      56.532  31.757  24.600  1.00 17.51           C  
-ANISOU  555  CD2 TYR A 302     2249   1300   3105    181   -374   -540       C  
-ATOM    556  CE1 TYR A 302      56.077  33.741  22.746  1.00 18.42           C  
-ANISOU  556  CE1 TYR A 302     2468   1272   3259    167   -425   -180       C  
-ATOM    557  CE2 TYR A 302      57.214  32.954  24.696  1.00 19.29           C  
-ANISOU  557  CE2 TYR A 302     2505   1393   3432    172   -246    -16       C  
-ATOM    558  CZ  TYR A 302      56.978  33.944  23.768  1.00 20.05           C  
-ANISOU  558  CZ  TYR A 302     2594   1190   3833   -271   -306    -36       C  
-ATOM    559  OH  TYR A 302      57.654  35.141  23.857  1.00 24.03           O  
-ANISOU  559  OH  TYR A 302     3030   1536   4562   -340   -363   -171       O  
-ATOM    560  N   GLY A 303      52.144  28.748  23.107  1.00 11.00           N  
-ANISOU  560  N   GLY A 303     1423   1091   1663    384   -465   -407       N  
-ATOM    561  CA  GLY A 303      51.434  27.531  22.783  1.00 11.15           C  
-ANISOU  561  CA  GLY A 303     1448   1111   1676    364   -639   -383       C  
-ATOM    562  C   GLY A 303      50.902  27.555  21.372  1.00 11.20           C  
-ANISOU  562  C   GLY A 303     1435   1107   1713    398   -367   -171       C  
-ATOM    563  O   GLY A 303      51.092  28.529  20.626  1.00 11.45           O  
-ANISOU  563  O   GLY A 303     1590   1165   1595    388   -239   -177       O  
-ATOM    564  N   VAL A 304      50.226  26.473  21.002  1.00 10.34           N  
-ANISOU  564  N   VAL A 304     1463    968   1497    311   -248   -198       N  
-ATOM    565  CA  VAL A 304      49.510  26.414  19.736  1.00 10.62           C  
-ANISOU  565  CA  VAL A 304     1383   1249   1401    339   -229   -277       C  
-ATOM    566  C   VAL A 304      48.049  26.040  19.979  1.00 10.79           C  
-ANISOU  566  C   VAL A 304     1350   1078   1670    480    -75   -290       C  
-ATOM    567  O   VAL A 304      47.760  25.087  20.723  1.00 11.39           O  
-ANISOU  567  O   VAL A 304     1488   1089   1749    396   -147   -192       O  
-ATOM    568  CB  VAL A 304      50.159  25.399  18.753  1.00 11.58           C  
-ANISOU  568  CB  VAL A 304     1470   1470   1459    325   -336   -397       C  
-ATOM    569  CG1 VAL A 304      49.278  25.205  17.528  1.00 13.97           C  
-ANISOU  569  CG1 VAL A 304     1877   1985   1444    856   -212   -318       C  
-ATOM    570  CG2 VAL A 304      51.549  25.865  18.349  1.00 14.74           C  
-ANISOU  570  CG2 VAL A 304     1488   1641   2469     45     -4   -149       C  
-ATOM    571  N   ASN A 305      47.141  26.811  19.372  1.00 10.42           N  
-ANISOU  571  N   ASN A 305      994   1215   1750    485   -148   -152       N  
-ATOM    572  CA  ASN A 305      45.742  26.425  19.249  1.00 10.61           C  
-ANISOU  572  CA  ASN A 305     1230   1127   1675    602    -96   -316       C  
-ATOM    573  C   ASN A 305      45.602  25.553  18.019  1.00  9.52           C  
-ANISOU  573  C   ASN A 305     1227    899   1491    280      1   -462       C  
-ATOM    574  O   ASN A 305      45.767  26.031  16.895  1.00 10.53           O  
-ANISOU  574  O   ASN A 305     1414   1049   1539    393     95    -88       O  
-ATOM    575  CB  ASN A 305      44.844  27.664  19.111  1.00 11.34           C  
-ANISOU  575  CB  ASN A 305     1563   1142   1603    651     46   -362       C  
-ATOM    576  CG  ASN A 305      44.767  28.468  20.385  1.00 11.34           C  
-ANISOU  576  CG  ASN A 305     1732   1159   1418    664    -61   -269       C  
-ATOM    577  OD1 ASN A 305      44.506  27.925  21.453  1.00 13.76           O  
-ANISOU  577  OD1 ASN A 305     2208   1376   1644    727    183   -241       O  
-ATOM    578  ND2 ASN A 305      45.022  29.777  20.282  1.00 12.58           N  
-ANISOU  578  ND2 ASN A 305     1727   1165   1886    721   -191   -325       N  
-ATOM    579  N   LEU A 306      45.297  24.277  18.231  1.00 10.38           N  
-ANISOU  579  N   LEU A 306     1342    861   1742    317    -96   -478       N  
-ATOM    580  CA  LEU A 306      45.355  23.280  17.168  1.00  9.88           C  
-ANISOU  580  CA  LEU A 306     1346    869   1540    231   -107   -188       C  
-ATOM    581  C   LEU A 306      44.166  23.304  16.216  1.00  9.64           C  
-ANISOU  581  C   LEU A 306     1244   1034   1383    102   -298   -160       C  
-ATOM    582  O   LEU A 306      43.038  23.627  16.600  1.00 12.18           O  
-ANISOU  582  O   LEU A 306     1191   1482   1955    373    204   -239       O  
-ATOM    583  CB  LEU A 306      45.487  21.882  17.774  1.00 11.03           C  
-ANISOU  583  CB  LEU A 306     1711    917   1564    423   -203   -131       C  
-ATOM    584  CG  LEU A 306      46.763  21.585  18.566  1.00 11.98           C  
-ANISOU  584  CG  LEU A 306     1742   1199   1611    573   -123   -101       C  
-ATOM    585  CD1 LEU A 306      46.606  20.314  19.407  1.00 14.07           C  
-ANISOU  585  CD1 LEU A 306     2116   1311   1920    443    155    326       C  
-ATOM    586  CD2 LEU A 306      47.958  21.473  17.621  1.00 11.96           C  
-ANISOU  586  CD2 LEU A 306     1657   1373   1515    435    401    -51       C  
-ATOM    587  N   ALA A 307      44.452  22.950  14.967  1.00 10.24           N  
-ANISOU  587  N   ALA A 307     1546   1118   1226    179   -296   -345       N  
-ATOM    588  CA  ALA A 307      43.446  22.710  13.949  1.00 10.58           C  
-ANISOU  588  CA  ALA A 307     1693    952   1375    282   -244   -236       C  
-ATOM    589  C   ALA A 307      43.797  21.414  13.220  1.00 10.07           C  
-ANISOU  589  C   ALA A 307     1321    877   1627    143    203   -213       C  
-ATOM    590  O   ALA A 307      44.876  20.841  13.433  1.00 11.11           O  
-ANISOU  590  O   ALA A 307     1276   1231   1715    499   -118   -256       O  
-ATOM    591  CB  ALA A 307      43.399  23.885  12.963  1.00 13.11           C  
-ANISOU  591  CB  ALA A 307     1896   1265   1818    339   -274    -28       C  
-ATOM    592  N   GLU A 308      42.906  20.945  12.350  1.00 10.46           N  
-ANISOU  592  N   GLU A 308     1390    949   1636    171    -68   -333       N  
-ATOM    593  CA  GLU A 308      43.280  19.854  11.450  1.00 10.95           C  
-ANISOU  593  CA  GLU A 308     1377   1196   1588    295   -212   -375       C  
-ATOM    594  C   GLU A 308      44.310  20.363  10.437  1.00 11.07           C  
-ANISOU  594  C   GLU A 308     1402   1342   1463    498   -211   -136       C  
-ATOM    595  O   GLU A 308      44.418  21.573  10.201  1.00 11.27           O  
-ANISOU  595  O   GLU A 308     1359   1271   1650    467     -4   -184       O  
-ATOM    596  CB  GLU A 308      42.054  19.291  10.740  1.00 10.63           C  
-ANISOU  596  CB  GLU A 308     1183   1188   1667     12   -215   -356       C  
-ATOM    597  CG  GLU A 308      40.973  18.781  11.685  1.00 11.30           C  
-ANISOU  597  CG  GLU A 308     1389   1137   1765    302     12    -86       C  
-ATOM    598  CD  GLU A 308      41.347  17.481  12.403  1.00 13.22           C  
-ANISOU  598  CD  GLU A 308     1680   1547   1796    348    -99   -664       C  
-ATOM    599  OE1 GLU A 308      42.266  16.766  11.945  1.00 14.33           O  
-ANISOU  599  OE1 GLU A 308     1736   1400   2307    423     33     75       O  
-ATOM    600  OE2 GLU A 308      40.717  17.173  13.439  1.00 15.47           O  
-ANISOU  600  OE2 GLU A 308     2148   1843   1886    473    101   -174       O  
-ATOM    601  N   LEU A 309      45.054  19.444   9.826  1.00 11.13           N  
-ANISOU  601  N   LEU A 309     1407   1310   1512    410   -228   -263       N  
-ATOM    602  CA  LEU A 309      46.161  19.824   8.949  1.00 11.67           C  
-ANISOU  602  CA  LEU A 309     1438   1230   1765    640    -45   -260       C  
-ATOM    603  C   LEU A 309      45.732  20.615   7.708  1.00 11.33           C  
-ANISOU  603  C   LEU A 309     1338   1432   1535    540    -87   -205       C  
-ATOM    604  O   LEU A 309      46.534  21.338   7.124  1.00 12.55           O  
-ANISOU  604  O   LEU A 309     1547   1571   1649    468    -70    -65       O  
-ATOM    605  CB  LEU A 309      46.971  18.593   8.550  1.00 12.74           C  
-ANISOU  605  CB  LEU A 309     1473   1260   2106    662   -391   -376       C  
-ATOM    606  CG  LEU A 309      47.720  17.935   9.712  1.00 13.38           C  
-ANISOU  606  CG  LEU A 309     1530   1240   2314    532   -825   -497       C  
-ATOM    607  CD1 LEU A 309      48.386  16.630   9.247  1.00 16.47           C  
-ANISOU  607  CD1 LEU A 309     1797   1461   2998    626   -637   -722       C  
-ATOM    608  CD2 LEU A 309      48.747  18.872  10.298  1.00 13.98           C  
-ANISOU  608  CD2 LEU A 309     1536   1417   2358    460   -684   -450       C  
-ATOM    609  N   ASP A 310      44.471  20.487   7.305  1.00 12.64           N  
-ANISOU  609  N   ASP A 310     1466   1692   1644    688   -274    155       N  
-ATOM    610  CA  ASP A 310      43.972  21.259   6.165  1.00 13.56           C  
-ANISOU  610  CA  ASP A 310     1553   1705   1894    453    -63     37       C  
-ATOM    611  C   ASP A 310      43.497  22.658   6.567  1.00 14.50           C  
-ANISOU  611  C   ASP A 310     1728   1914   1867    452    -27    -56       C  
-ATOM    612  O   ASP A 310      43.061  23.448   5.722  1.00 16.83           O  
-ANISOU  612  O   ASP A 310     1849   2299   2247    590   -197    464       O  
-ATOM    613  CB  ASP A 310      42.874  20.497   5.411  1.00 14.26           C  
-ANISOU  613  CB  ASP A 310     1383   2016   2017    146    -66    -52       C  
-ATOM    614  CG  ASP A 310      41.600  20.310   6.227  1.00 15.76           C  
-ANISOU  614  CG  ASP A 310     1519   2230   2239    262   -423   -275       C  
-ATOM    615  OD1 ASP A 310      41.572  20.676   7.423  1.00 15.22           O  
-ANISOU  615  OD1 ASP A 310     1614   1972   2195    541   -107   -228       O  
-ATOM    616  OD2 ASP A 310      40.618  19.776   5.650  1.00 16.19           O  
-ANISOU  616  OD2 ASP A 310     1575   2568   2008     49   -378    -37       O  
-ATOM    617  N   GLY A 311      43.593  22.966   7.857  1.00 13.36           N  
-ANISOU  617  N   GLY A 311     1429   1607   2040    549    -15      2       N  
-ATOM    618  CA  GLY A 311      43.205  24.278   8.350  1.00 14.70           C  
-ANISOU  618  CA  GLY A 311     1465   1646   2473    783    -45     43       C  
-ATOM    619  C   GLY A 311      41.769  24.363   8.847  1.00 14.36           C  
-ANISOU  619  C   GLY A 311     1488   1568   2401    476   -123    -78       C  
-ATOM    620  O   GLY A 311      41.380  25.351   9.460  1.00 16.43           O  
-ANISOU  620  O   GLY A 311     1619   1611   3013    529    278   -244       O  
-ATOM    621  N   ASN A 312      40.980  23.333   8.576  1.00 14.01           N  
-ANISOU  621  N   ASN A 312     1340   1884   2099    634     50     87       N  
-ATOM    622  CA  ASN A 312      39.650  23.234   9.150  1.00 14.49           C  
-ANISOU  622  CA  ASN A 312     1669   1912   1924    570    -51   -254       C  
-ATOM    623  C   ASN A 312      39.735  22.937  10.645  1.00 14.05           C  
-ANISOU  623  C   ASN A 312     1607   1700   2031    619     69   -308       C  
-ATOM    624  O   ASN A 312      40.752  22.447  11.130  1.00 14.44           O  
-ANISOU  624  O   ASN A 312     1705   1665   2115    765   -360   -332       O  
-ATOM    625  CB  ASN A 312      38.824  22.189   8.407  1.00 17.30           C  
-ANISOU  625  CB  ASN A 312     1749   2578   2247    596   -509   -611       C  
-ATOM    626  CG  ASN A 312      38.365  22.686   7.051  1.00 21.75           C  
-ANISOU  626  CG  ASN A 312     2292   3462   2510   1321   -701   -764       C  
-ATOM    627  OD1 ASN A 312      37.759  23.755   6.947  1.00 27.36           O  
-ANISOU  627  OD1 ASN A 312     3185   3875   3336   1823  -1045   -534       O  
-ATOM    628  ND2 ASN A 312      38.666  21.927   6.004  1.00 22.92           N  
-ANISOU  628  ND2 ASN A 312     2390   3771   2548   1352   -469   -597       N  
-ATOM    629  N   PRO A 313      38.677  23.262  11.387  1.00 13.83           N  
-ANISOU  629  N   PRO A 313     1341   1741   2172    666   -139   -152       N  
-ATOM    630  CA  PRO A 313      38.773  23.201  12.846  1.00 14.85           C  
-ANISOU  630  CA  PRO A 313     1608   1867   2166    985    115   -125       C  
-ATOM    631  C   PRO A 313      38.898  21.788  13.380  1.00 15.33           C  
-ANISOU  631  C   PRO A 313     1780   1739   2304    512   -195   -260       C  
-ATOM    632  O   PRO A 313      38.317  20.845  12.830  1.00 14.31           O  
-ANISOU  632  O   PRO A 313     1686   1837   1914    472    -30     14       O  
-ATOM    633  CB  PRO A 313      37.455  23.824  13.317  1.00 16.86           C  
-ANISOU  633  CB  PRO A 313     1695   2237   2474   1028    217   -115       C  
-ATOM    634  CG  PRO A 313      36.548  23.781  12.140  1.00 17.43           C  
-ANISOU  634  CG  PRO A 313     1570   2295   2758    663     42   -499       C  
-ATOM    635  CD  PRO A 313      37.417  23.876  10.933  1.00 16.04           C  
-ANISOU  635  CD  PRO A 313     1341   2021   2733    684    146    258       C  
-ATOM    636  N   TYR A 314      39.666  21.654  14.456  1.00 15.35           N  
-ANISOU  636  N   TYR A 314     1812   1972   2048    851   -213    -37       N  
-ATOM    637  CA  TYR A 314      39.714  20.413  15.198  1.00 16.15           C  
-ANISOU  637  CA  TYR A 314     1840   2330   1966    741    178     14       C  
-ATOM    638  C   TYR A 314      38.505  20.411  16.109  1.00 18.55           C  
-ANISOU  638  C   TYR A 314     1955   2432   2662    714     64   -376       C  
-ATOM    639  O   TYR A 314      38.275  21.365  16.861  1.00 19.98           O  
-ANISOU  639  O   TYR A 314     2241   2627   2724    693    272   -539       O  
-ATOM    640  CB  TYR A 314      40.995  20.316  16.028  1.00 16.10           C  
-ANISOU  640  CB  TYR A 314     1867   2448   1802    772   -523    -32       C  
-ATOM    641  CG  TYR A 314      40.938  19.229  17.077  1.00 15.79           C  
-ANISOU  641  CG  TYR A 314     1816   2439   1745    890     50     84       C  
-ATOM    642  CD1 TYR A 314      40.734  17.900  16.719  1.00 16.66           C  
-ANISOU  642  CD1 TYR A 314     1889   2461   1980   1186     83     71       C  
-ATOM    643  CD2 TYR A 314      41.082  19.531  18.426  1.00 15.39           C  
-ANISOU  643  CD2 TYR A 314     1626   2421   1799    439     54    266       C  
-ATOM    644  CE1 TYR A 314      40.674  16.900  17.678  1.00 16.59           C  
-ANISOU  644  CE1 TYR A 314     2007   2542   1755   1115    157     -7       C  
-ATOM    645  CE2 TYR A 314      41.034  18.538  19.391  1.00 16.58           C  
-ANISOU  645  CE2 TYR A 314     1851   2417   2031    696   -137   -117       C  
-ATOM    646  CZ  TYR A 314      40.825  17.225  19.009  1.00 16.05           C  
-ANISOU  646  CZ  TYR A 314     1993   2653   1451    984   -131    -34       C  
-ATOM    647  OH  TYR A 314      40.763  16.238  19.961  1.00 17.57           O  
-ANISOU  647  OH  TYR A 314     1982   2917   1776    817   -150     68       O  
-ATOM    648  N   HIS A 315      37.718  19.349  16.021  1.00 18.04           N  
-ANISOU  648  N   HIS A 315     2068   2443   2341    466    370    155       N  
-ATOM    649  CA  HIS A 315      36.559  19.210  16.875  1.00 22.15           C  
-ANISOU  649  CA  HIS A 315     2625   2781   3010    450     79    324       C  
-ATOM    650  C   HIS A 315      37.018  18.664  18.210  1.00 22.25           C  
-ANISOU  650  C   HIS A 315     2847   2731   2877    178    253    156       C  
-ATOM    651  O   HIS A 315      37.128  17.452  18.398  1.00 24.63           O  
-ANISOU  651  O   HIS A 315     2992   2487   3880    218     12   1163       O  
-ATOM    652  CB  HIS A 315      35.511  18.313  16.217  1.00 26.64           C  
-ANISOU  652  CB  HIS A 315     3050   3312   3761    446   -171    347       C  
-ATOM    653  CG  HIS A 315      34.902  18.912  14.988  1.00 35.11           C  
-ANISOU  653  CG  HIS A 315     3854   4125   5360    809   -870    102       C  
-ATOM    654  ND1 HIS A 315      34.254  18.160  14.033  1.00 39.44           N  
-ANISOU  654  ND1 HIS A 315     4307   4564   6112   1117  -1001      1       N  
-ATOM    655  CD2 HIS A 315      34.845  20.195  14.559  1.00 39.36           C  
-ANISOU  655  CD2 HIS A 315     4227   4575   6154    988  -1280   -106       C  
-ATOM    656  CE1 HIS A 315      33.824  18.954  13.068  1.00 40.91           C  
-ANISOU  656  CE1 HIS A 315     4451   4747   6346   1233  -1255   -145       C  
-ATOM    657  NE2 HIS A 315      34.171  20.194  13.362  1.00 40.53           N  
-ANISOU  657  NE2 HIS A 315     4433   4703   6263   1110  -1344   -168       N  
-ATOM    658  N   ALA A 316      37.300  19.585  19.131  1.00 24.73           N  
-ANISOU  658  N   ALA A 316     2915   3086   3396     18    294   -379       N  
-ATOM    659  CA  ALA A 316      37.802  19.227  20.451  1.00 25.92           C  
-ANISOU  659  CA  ALA A 316     3042   3240   3564    377    741   -638       C  
-ATOM    660  C   ALA A 316      36.872  18.229  21.126  1.00 25.64           C  
-ANISOU  660  C   ALA A 316     2678   3452   3613     39    684   -463       C  
-ATOM    661  O   ALA A 316      35.653  18.277  20.946  1.00 26.24           O  
-ANISOU  661  O   ALA A 316     2517   3908   3543    332    637   -373       O  
-ATOM    662  CB  ALA A 316      37.984  20.477  21.324  1.00 28.06           C  
-ANISOU  662  CB  ALA A 316     3522   2860   4279    709   1209   -734       C  
-ATOM    663  N   PHE A 317      37.468  17.319  21.887  1.00 24.40           N  
-ANISOU  663  N   PHE A 317     2714   3321   3234   -266    440   -423       N  
-ATOM    664  CA  PHE A 317      36.735  16.288  22.612  1.00 25.83           C  
-ANISOU  664  CA  PHE A 317     2951   3564   3297   -417    549   -351       C  
-ATOM    665  C   PHE A 317      36.057  15.240  21.715  1.00 25.98           C  
-ANISOU  665  C   PHE A 317     3016   3522   3331  -1057   -159   -698       C  
-ATOM    666  O   PHE A 317      35.169  14.532  22.182  1.00 29.43           O  
-ANISOU  666  O   PHE A 317     3553   3703   3925   -664    147     26       O  
-ATOM    667  CB  PHE A 317      35.710  16.922  23.570  1.00 27.75           C  
-ANISOU  667  CB  PHE A 317     3309   3862   3372   -258    692   -525       C  
-ATOM    668  CG  PHE A 317      36.308  17.926  24.522  1.00 30.61           C  
-ANISOU  668  CG  PHE A 317     3699   4242   3687      0    690   -521       C  
-ATOM    669  CD1 PHE A 317      36.198  19.286  24.277  1.00 31.04           C  
-ANISOU  669  CD1 PHE A 317     3918   4152   3722    -42    764   -899       C  
-ATOM    670  CD2 PHE A 317      36.984  17.507  25.657  1.00 32.89           C  
-ANISOU  670  CD2 PHE A 317     3911   4431   4155    197    422   -632       C  
-ATOM    671  CE1 PHE A 317      36.755  20.215  25.150  1.00 33.23           C  
-ANISOU  671  CE1 PHE A 317     4063   4469   4094    289    626   -765       C  
-ATOM    672  CE2 PHE A 317      37.540  18.423  26.531  1.00 34.15           C  
-ANISOU  672  CE2 PHE A 317     4016   4479   4481    251    386   -691       C  
-ATOM    673  CZ  PHE A 317      37.423  19.782  26.276  1.00 33.76           C  
-ANISOU  673  CZ  PHE A 317     4022   4418   4385    186    452   -825       C  
-ATOM    674  N   ASP A 318      36.489  15.119  20.456  1.00 24.12           N  
-ANISOU  674  N   ASP A 318     3046   3656   2460  -1446    489   -556       N  
-ATOM    675  CA  ASP A 318      35.805  14.249  19.480  1.00 33.05           C  
-ANISOU  675  CA  ASP A 318     3852   4075   4630   -700    471     70       C  
-ATOM    676  C   ASP A 318      36.655  13.178  18.774  1.00 36.01           C  
-ANISOU  676  C   ASP A 318     4063   3786   5834   -592      7    -80       C  
-ATOM    677  O   ASP A 318      36.111  12.221  18.213  1.00 42.11           O  
-ANISOU  677  O   ASP A 318     4603   4289   7106   -513   -436   -617       O  
-ATOM    678  CB  ASP A 318      35.073  15.090  18.436  1.00 37.80           C  
-ANISOU  678  CB  ASP A 318     4412   4880   5071   -361    182    504       C  
-ATOM    679  CG  ASP A 318      33.605  15.265  18.762  1.00 42.15           C  
-ANISOU  679  CG  ASP A 318     5005   5649   5361    103     73    577       C  
-ATOM    680  OD1 ASP A 318      32.885  15.898  17.958  1.00 44.44           O  
-ANISOU  680  OD1 ASP A 318     5168   5931   5785    246   -176    479       O  
-ATOM    681  OD2 ASP A 318      33.167  14.755  19.818  1.00 41.27           O  
-ANISOU  681  OD2 ASP A 318     5243   5858   4580    300    204    772       O  
-ATOM    682  N   SER A 319      37.967  13.380  18.740  1.00 30.19           N  
-ANISOU  682  N   SER A 319     3389   3192   4889   -807   -273    578       N  
-ATOM    683  CA  SER A 319      38.941  12.314  18.486  1.00 26.84           C  
-ANISOU  683  CA  SER A 319     3285   2745   4166   -650    126    612       C  
-ATOM    684  C   SER A 319      40.104  12.694  19.392  1.00 19.02           C  
-ANISOU  684  C   SER A 319     2450   1976   2801   -556    -54    382       C  
-ATOM    685  O   SER A 319      40.097  13.793  19.936  1.00 21.15           O  
-ANISOU  685  O   SER A 319     2352   2649   3033    202    595    526       O  
-ATOM    686  CB  SER A 319      39.342  12.220  17.009  1.00 29.54           C  
-ANISOU  686  CB  SER A 319     3524   2883   4815   -583   -422   -121       C  
-ATOM    687  OG  SER A 319      40.168  13.296  16.605  1.00 28.47           O  
-ANISOU  687  OG  SER A 319     3364   3547   3904   -585  -1324   -646       O  
-ATOM    688  N   PRO A 320      41.088  11.798  19.605  1.00 14.37           N  
-ANISOU  688  N   PRO A 320     2147   1199   2115    -26    217     16       N  
-ATOM    689  CA  PRO A 320      42.005  12.133  20.705  1.00 13.98           C  
-ANISOU  689  CA  PRO A 320     2082   1245   1984    185    137   -106       C  
-ATOM    690  C   PRO A 320      42.782  13.425  20.468  1.00 13.47           C  
-ANISOU  690  C   PRO A 320     2103   1291   1723    340    144   -458       C  
-ATOM    691  O   PRO A 320      43.125  14.111  21.428  1.00 13.27           O  
-ANISOU  691  O   PRO A 320     2087   1294   1659    345    238   -143       O  
-ATOM    692  CB  PRO A 320      42.957  10.935  20.746  1.00 16.50           C  
-ANISOU  692  CB  PRO A 320     2141   1433   2693    391     47      0       C  
-ATOM    693  CG  PRO A 320      42.184   9.819  20.123  1.00 16.80           C  
-ANISOU  693  CG  PRO A 320     2263   1305   2814    148     85   -402       C  
-ATOM    694  CD  PRO A 320      41.349  10.457  19.057  1.00 15.66           C  
-ANISOU  694  CD  PRO A 320     2206   1416   2328    201   -153     61       C  
-ATOM    695  N   ALA A 321      43.052  13.740  19.205  1.00 12.36           N  
-ANISOU  695  N   ALA A 321     1753   1321   1621    189    444     59       N  
-ATOM    696  CA  ALA A 321      43.778  14.940  18.831  1.00 11.39           C  
-ANISOU  696  CA  ALA A 321     1352   1387   1587    141    183    212       C  
-ATOM    697  C   ALA A 321      43.541  15.101  17.343  1.00 11.05           C  
-ANISOU  697  C   ALA A 321     1278   1326   1592    298    266     18       C  
-ATOM    698  O   ALA A 321      42.928  14.229  16.722  1.00 12.02           O  
-ANISOU  698  O   ALA A 321     1218   1435   1912    -79    220   -277       O  
-ATOM    699  CB  ALA A 321      45.281  14.768  19.126  1.00 12.65           C  
-ANISOU  699  CB  ALA A 321     1464   1370   1971    424   -347   -258       C  
-ATOM    700  N   PRO A 322      43.998  16.216  16.754  1.00 11.02           N  
-ANISOU  700  N   PRO A 322     1472   1189   1527    216    -70   -277       N  
-ATOM    701  CA  PRO A 322      43.841  16.331  15.300  1.00 11.27           C  
-ANISOU  701  CA  PRO A 322     1557   1040   1684     83    -35   -415       C  
-ATOM    702  C   PRO A 322      44.460  15.136  14.569  1.00  9.42           C  
-ANISOU  702  C   PRO A 322     1162   1088   1330    -96    -99   -128       C  
-ATOM    703  O   PRO A 322      45.437  14.541  15.046  1.00 10.19           O  
-ANISOU  703  O   PRO A 322     1105   1297   1470    210    -66   -103       O  
-ATOM    704  CB  PRO A 322      44.613  17.608  14.975  1.00 11.18           C  
-ANISOU  704  CB  PRO A 322     1527   1183   1539    -48    120   -155       C  
-ATOM    705  CG  PRO A 322      44.519  18.425  16.236  1.00 12.22           C  
-ANISOU  705  CG  PRO A 322     1673   1361   1607    218     97   -160       C  
-ATOM    706  CD  PRO A 322      44.611  17.418  17.350  1.00 11.44           C  
-ANISOU  706  CD  PRO A 322     1639   1112   1595    -11   -107   -227       C  
-ATOM    707  N   LEU A 323      43.909  14.787  13.411  1.00  9.81           N  
-ANISOU  707  N   LEU A 323     1221   1027   1480    225      5   -371       N  
-ATOM    708  CA  LEU A 323      44.433  13.646  12.670  1.00  9.97           C  
-ANISOU  708  CA  LEU A 323     1084   1095   1608    116   -125   -426       C  
-ATOM    709  C   LEU A 323      45.906  13.846  12.316  1.00  8.69           C  
-ANISOU  709  C   LEU A 323     1057    722   1522   -227     32    -14       C  
-ATOM    710  O   LEU A 323      46.326  14.954  11.962  1.00 10.03           O  
-ANISOU  710  O   LEU A 323     1056    944   1809     80    -23   -163       O  
-ATOM    711  CB  LEU A 323      43.606  13.383  11.412  1.00 11.70           C  
-ANISOU  711  CB  LEU A 323      956   1403   2087    -94   -264   -513       C  
-ATOM    712  CG  LEU A 323      42.116  13.171  11.679  1.00 12.27           C  
-ANISOU  712  CG  LEU A 323      907   1409   2347   -254   -183   -401       C  
-ATOM    713  CD1 LEU A 323      41.396  12.793  10.386  1.00 16.31           C  
-ANISOU  713  CD1 LEU A 323     1134   2113   2948    -49   -323  -1111       C  
-ATOM    714  CD2 LEU A 323      41.913  12.089  12.739  1.00 15.04           C  
-ANISOU  714  CD2 LEU A 323     1234   1269   3212    -49    290   -183       C  
-ATOM    715  N   GLY A 324      46.693  12.776  12.428  1.00  9.70           N  
-ANISOU  715  N   GLY A 324     1048   1035   1602    118     53   -128       N  
-ATOM    716  CA  GLY A 324      48.120  12.823  12.128  1.00 10.53           C  
-ANISOU  716  CA  GLY A 324     1178   1141   1683    107    113    -70       C  
-ATOM    717  C   GLY A 324      49.002  13.253  13.297  1.00  9.38           C  
-ANISOU  717  C   GLY A 324     1253    931   1378    216    133    -50       C  
-ATOM    718  O   GLY A 324      50.219  13.111  13.244  1.00 10.68           O  
-ANISOU  718  O   GLY A 324     1329   1196   1531    300     58   -208       O  
-ATOM    719  N   PHE A 325      48.397  13.780  14.357  1.00  9.71           N  
-ANISOU  719  N   PHE A 325     1315    931   1444    142   -302   -140       N  
-ATOM    720  CA  PHE A 325      49.150  14.293  15.499  1.00 10.04           C  
-ANISOU  720  CA  PHE A 325     1239   1078   1496    356    -12   -230       C  
-ATOM    721  C   PHE A 325      50.139  13.231  16.009  1.00  8.67           C  
-ANISOU  721  C   PHE A 325     1037    898   1359    107   -115    -47       C  
-ATOM    722  O   PHE A 325      49.782  12.066  16.124  1.00 10.16           O  
-ANISOU  722  O   PHE A 325     1403    898   1560    143     28     15       O  
-ATOM    723  CB  PHE A 325      48.173  14.685  16.614  1.00 10.45           C  
-ANISOU  723  CB  PHE A 325     1366   1239   1363    197   -150   -463       C  
-ATOM    724  CG  PHE A 325      48.774  15.570  17.674  1.00  9.02           C  
-ANISOU  724  CG  PHE A 325     1119    964   1344    -46    137    -94       C  
-ATOM    725  CD1 PHE A 325      48.705  16.959  17.568  1.00 10.23           C  
-ANISOU  725  CD1 PHE A 325     1365    793   1727     36    193   -198       C  
-ATOM    726  CD2 PHE A 325      49.390  15.024  18.786  1.00 10.16           C  
-ANISOU  726  CD2 PHE A 325     1238   1268   1353    102    -67   -169       C  
-ATOM    727  CE1 PHE A 325      49.253  17.778  18.547  1.00 11.13           C  
-ANISOU  727  CE1 PHE A 325     1561   1028   1640    228      6   -198       C  
-ATOM    728  CE2 PHE A 325      49.937  15.837  19.775  1.00 11.75           C  
-ANISOU  728  CE2 PHE A 325     1514   1309   1641    330    -39   -223       C  
-ATOM    729  CZ  PHE A 325      49.867  17.215  19.658  1.00 11.31           C  
-ANISOU  729  CZ  PHE A 325     1625    957   1715    384    104   -163       C  
-ATOM    730  N   PRO A 326      51.386  13.628  16.319  1.00  9.10           N  
-ANISOU  730  N   PRO A 326     1355    574   1529    217   -253     20       N  
-ATOM    731  CA  PRO A 326      52.362  12.645  16.816  1.00  9.80           C  
-ANISOU  731  CA  PRO A 326     1303    725   1696     -3   -302    167       C  
-ATOM    732  C   PRO A 326      51.819  11.830  17.992  1.00  9.90           C  
-ANISOU  732  C   PRO A 326     1557    701   1502    202   -170    -28       C  
-ATOM    733  O   PRO A 326      51.205  12.395  18.910  1.00 11.02           O  
-ANISOU  733  O   PRO A 326     1797    913   1475    405     31   -185       O  
-ATOM    734  CB  PRO A 326      53.530  13.521  17.286  1.00 11.84           C  
-ANISOU  734  CB  PRO A 326     1365   1017   2117    -53   -543     11       C  
-ATOM    735  CG  PRO A 326      53.450  14.731  16.430  1.00 12.08           C  
-ANISOU  735  CG  PRO A 326     1503    937   2148    389   -295    327       C  
-ATOM    736  CD  PRO A 326      51.959  14.987  16.265  1.00  9.87           C  
-ANISOU  736  CD  PRO A 326     1133    616   2002    177   -187     -7       C  
-ATOM    737  N   ASP A 327      52.050  10.516  17.978  1.00 10.30           N  
-ANISOU  737  N   ASP A 327     1663    711   1538     14   -119    249       N  
-ATOM    738  CA  ASP A 327      51.600   9.667  19.086  1.00 10.92           C  
-ANISOU  738  CA  ASP A 327     1544    843   1763    -85   -245     13       C  
-ATOM    739  C   ASP A 327      52.752   9.176  19.966  1.00 10.97           C  
-ANISOU  739  C   ASP A 327     1676   1032   1459    281   -394    -77       C  
-ATOM    740  O   ASP A 327      52.698   8.093  20.549  1.00 12.27           O  
-ANISOU  740  O   ASP A 327     1797   1069   1795     98   -282     42       O  
-ATOM    741  CB  ASP A 327      50.686   8.523  18.609  1.00 11.58           C  
-ANISOU  741  CB  ASP A 327     1564    905   1929    107     13   -216       C  
-ATOM    742  CG  ASP A 327      51.419   7.452  17.816  1.00 10.43           C  
-ANISOU  742  CG  ASP A 327     1647    765   1550    -99    -23     54       C  
-ATOM    743  OD1 ASP A 327      52.609   7.634  17.491  1.00 11.37           O  
-ANISOU  743  OD1 ASP A 327     1495   1067   1759     45    163    -98       O  
-ATOM    744  OD2 ASP A 327      50.780   6.415  17.503  1.00 11.68           O  
-ANISOU  744  OD2 ASP A 327     1536   1057   1846     92      7   -198       O  
-ATOM    745  N   PHE A 328      53.780  10.006  20.081  1.00 10.94           N  
-ANISOU  745  N   PHE A 328     1467   1032   1657    170   -402   -175       N  
-ATOM    746  CA  PHE A 328      54.884   9.757  20.997  1.00 10.31           C  
-ANISOU  746  CA  PHE A 328     1353   1094   1470    117    -76    -41       C  
-ATOM    747  C   PHE A 328      54.619  10.485  22.305  1.00 11.04           C  
-ANISOU  747  C   PHE A 328     1774   1143   1276    279   -142   -191       C  
-ATOM    748  O   PHE A 328      54.493  11.716  22.328  1.00 11.85           O  
-ANISOU  748  O   PHE A 328     1667   1069   1764    230   -159   -345       O  
-ATOM    749  CB  PHE A 328      56.210  10.190  20.370  1.00 11.10           C  
-ANISOU  749  CB  PHE A 328     1407   1149   1661    181   -194   -290       C  
-ATOM    750  CG  PHE A 328      56.511   9.469  19.089  1.00 10.95           C  
-ANISOU  750  CG  PHE A 328     1711    969   1479    111   -250   -371       C  
-ATOM    751  CD1 PHE A 328      56.922   8.148  19.111  1.00 13.04           C  
-ANISOU  751  CD1 PHE A 328     1985   1116   1851    437     69   -285       C  
-ATOM    752  CD2 PHE A 328      56.323  10.087  17.865  1.00 11.28           C  
-ANISOU  752  CD2 PHE A 328     1648   1225   1413    172     77   -164       C  
-ATOM    753  CE1 PHE A 328      57.165   7.465  17.927  1.00 12.40           C  
-ANISOU  753  CE1 PHE A 328     2064   1125   1523    498    199   -181       C  
-ATOM    754  CE2 PHE A 328      56.559   9.408  16.677  1.00 12.44           C  
-ANISOU  754  CE2 PHE A 328     1749    922   2055    255    -95   -299       C  
-ATOM    755  CZ  PHE A 328      56.979   8.096  16.711  1.00 12.09           C  
-ANISOU  755  CZ  PHE A 328     1995   1172   1426    321     67   -247       C  
-ATOM    756  N   GLY A 329      54.517   9.715  23.385  1.00 11.82           N  
-ANISOU  756  N   GLY A 329     1993   1264   1232    404     -7     37       N  
-ATOM    757  CA  GLY A 329      54.132  10.248  24.675  1.00 12.50           C  
-ANISOU  757  CA  GLY A 329     2060   1444   1246    521   -152   -110       C  
-ATOM    758  C   GLY A 329      55.273  10.379  25.662  1.00 11.52           C  
-ANISOU  758  C   GLY A 329     2018    984   1373    215    -46   -305       C  
-ATOM    759  O   GLY A 329      56.249   9.627  25.596  1.00 13.73           O  
-ANISOU  759  O   GLY A 329     2049   1197   1970    512     67    -37       O  
-ATOM    760  N   ASN A 330      55.131  11.337  26.575  1.00 11.43           N  
-ANISOU  760  N   ASN A 330     1976   1032   1336    406   -221     57       N  
-ATOM    761  CA  ASN A 330      56.082  11.549  27.662  1.00 11.94           C  
-ANISOU  761  CA  ASN A 330     2046   1249   1242    340   -377    164       C  
-ATOM    762  C   ASN A 330      57.494  11.854  27.195  1.00 12.54           C  
-ANISOU  762  C   ASN A 330     2034   1310   1419    445   -227   -322       C  
-ATOM    763  O   ASN A 330      58.461  11.414  27.812  1.00 14.10           O  
-ANISOU  763  O   ASN A 330     1856   1717   1783    478   -406    -83       O  
-ATOM    764  CB  ASN A 330      56.111  10.362  28.635  1.00 13.34           C  
-ANISOU  764  CB  ASN A 330     2225   1306   1537    511   -211    148       C  
-ATOM    765  CG  ASN A 330      56.578  10.774  30.018  1.00 13.69           C  
-ANISOU  765  CG  ASN A 330     2372   1366   1463    611   -126     20       C  
-ATOM    766  OD1 ASN A 330      56.148  11.800  30.539  1.00 15.42           O  
-ANISOU  766  OD1 ASN A 330     2712   1708   1438    815   -117    -40       O  
-ATOM    767  ND2 ASN A 330      57.469   9.989  30.612  1.00 15.16           N  
-ANISOU  767  ND2 ASN A 330     2430   1719   1612    600   -255    424       N  
-ATOM    768  N   CYS A 331      57.607  12.623  26.115  1.00 11.91           N  
-ANISOU  768  N   CYS A 331     1790   1320   1413    258   -383   -318       N  
-ATOM    769  CA  CYS A 331      58.909  12.932  25.549  1.00 10.96           C  
-ANISOU  769  CA  CYS A 331     1662    996   1504    267     31     -1       C  
-ATOM    770  C   CYS A 331      58.939  14.322  24.929  1.00 10.54           C  
-ANISOU  770  C   CYS A 331     1510   1009   1485     55   -355     73       C  
-ATOM    771  O   CYS A 331      57.930  15.034  24.924  1.00 11.80           O  
-ANISOU  771  O   CYS A 331     1407   1358   1717    390   -293   -184       O  
-ATOM    772  CB  CYS A 331      59.313  11.864  24.528  1.00 13.16           C  
-ANISOU  772  CB  CYS A 331     1920   1350   1728    422   -252   -234       C  
-ATOM    773  SG  CYS A 331      58.108  11.655  23.183  1.00 13.44           S  
-ANISOU  773  SG  CYS A 331     1877   1462   1765    211   -350   -232       S  
-ATOM    774  N   ASP A 332      60.109  14.708  24.435  1.00 11.37           N  
-ANISOU  774  N   ASP A 332     1745    973   1603   -114   -170    -60       N  
-ATOM    775  CA  ASP A 332      60.292  16.024  23.843  1.00 10.51           C  
-ANISOU  775  CA  ASP A 332     1577   1006   1409     35   -304   -210       C  
-ATOM    776  C   ASP A 332      60.210  15.921  22.327  1.00 10.06           C  
-ANISOU  776  C   ASP A 332     1533   1143   1145    508   -213   -259       C  
-ATOM    777  O   ASP A 332      61.026  15.241  21.693  1.00 13.09           O  
-ANISOU  777  O   ASP A 332     1655   1493   1826    697   -148   -271       O  
-ATOM    778  CB  ASP A 332      61.641  16.619  24.245  1.00 12.47           C  
-ANISOU  778  CB  ASP A 332     1695   1169   1874     76   -371   -513       C  
-ATOM    779  CG  ASP A 332      61.696  17.038  25.709  1.00 13.88           C  
-ANISOU  779  CG  ASP A 332     1789   1267   2216   -104   -505   -342       C  
-ATOM    780  OD1 ASP A 332      60.736  16.775  26.472  1.00 14.12           O  
-ANISOU  780  OD1 ASP A 332     2158   1545   1660    251   -427   -227       O  
-ATOM    781  OD2 ASP A 332      62.721  17.639  26.092  1.00 15.56           O  
-ANISOU  781  OD2 ASP A 332     1893   1627   2391    229   -503   -717       O  
-ATOM    782  N   LEU A 333      59.201  16.573  21.763  1.00 10.50           N  
-ANISOU  782  N   LEU A 333     1462   1021   1504    335   -457     -8       N  
-ATOM    783  CA  LEU A 333      59.003  16.617  20.322  1.00 10.32           C  
-ANISOU  783  CA  LEU A 333     1231   1059   1629    263   -205    -59       C  
-ATOM    784  C   LEU A 333      59.685  17.852  19.759  1.00  9.52           C  
-ANISOU  784  C   LEU A 333     1269   1030   1319    226   -107     11       C  
-ATOM    785  O   LEU A 333      59.288  18.984  20.057  1.00 12.18           O  
-ANISOU  785  O   LEU A 333     1607    922   2100    344     87   -238       O  
-ATOM    786  CB  LEU A 333      57.512  16.665  19.984  1.00 10.57           C  
-ANISOU  786  CB  LEU A 333     1246   1024   1746     92   -109     77       C  
-ATOM    787  CG  LEU A 333      56.626  15.634  20.690  1.00 10.54           C  
-ANISOU  787  CG  LEU A 333     1260    879   1865    344    -78     -9       C  
-ATOM    788  CD1 LEU A 333      55.159  15.918  20.385  1.00 12.13           C  
-ANISOU  788  CD1 LEU A 333     1161   1259   2190    281   -460     63       C  
-ATOM    789  CD2 LEU A 333      57.011  14.210  20.271  1.00 12.66           C  
-ANISOU  789  CD2 LEU A 333     1647    913   2250    471    175   -225       C  
-ATOM    790  N   HIS A 334      60.714  17.634  18.953  1.00  9.69           N  
-ANISOU  790  N   HIS A 334     1267    943   1472    301   -203   -215       N  
-ATOM    791  CA  HIS A 334      61.443  18.738  18.341  1.00  9.89           C  
-ANISOU  791  CA  HIS A 334      977   1099   1680    125   -199    136       C  
-ATOM    792  C   HIS A 334      60.855  18.983  16.969  1.00  9.84           C  
-ANISOU  792  C   HIS A 334     1257    975   1506    274     62   -142       C  
-ATOM    793  O   HIS A 334      61.055  18.186  16.045  1.00 10.11           O  
-ANISOU  793  O   HIS A 334     1329    943   1567    353   -199   -257       O  
-ATOM    794  CB  HIS A 334      62.936  18.411  18.255  1.00 10.83           C  
-ANISOU  794  CB  HIS A 334     1154   1295   1666    221   -362    -22       C  
-ATOM    795  CG  HIS A 334      63.559  18.160  19.591  1.00 11.49           C  
-ANISOU  795  CG  HIS A 334     1286   1312   1768    266   -471   -232       C  
-ATOM    796  ND1 HIS A 334      64.196  19.151  20.310  1.00 12.56           N  
-ANISOU  796  ND1 HIS A 334     1452   1310   2009    308   -480   -154       N  
-ATOM    797  CD2 HIS A 334      63.597  17.048  20.362  1.00 12.01           C  
-ANISOU  797  CD2 HIS A 334     1479   1320   1764    318   -556   -171       C  
-ATOM    798  CE1 HIS A 334      64.623  18.650  21.456  1.00 13.73           C  
-ANISOU  798  CE1 HIS A 334     1520   1366   2329    277   -481    -99       C  
-ATOM    799  NE2 HIS A 334      64.263  17.379  21.517  1.00 13.34           N  
-ANISOU  799  NE2 HIS A 334     1488   1498   2082    397   -439    -81       N  
-ATOM    800  N   MET A 335      60.113  20.081  16.855  1.00 10.71           N  
-ANISOU  800  N   MET A 335     1268   1146   1653    276   -331    -71       N  
-ATOM    801  CA  MET A 335      59.333  20.370  15.659  1.00 10.10           C  
-ANISOU  801  CA  MET A 335     1338    977   1520    159   -183   -199       C  
-ATOM    802  C   MET A 335      60.010  21.419  14.803  1.00 10.74           C  
-ANISOU  802  C   MET A 335     1453    964   1662     56   -441   -277       C  
-ATOM    803  O   MET A 335      60.631  22.361  15.309  1.00 12.91           O  
-ANISOU  803  O   MET A 335     2016   1209   1679     84   -400   -326       O  
-ATOM    804  CB  MET A 335      57.936  20.883  16.032  1.00 12.09           C  
-ANISOU  804  CB  MET A 335     1377   1165   2050    239    -28    110       C  
-ATOM    805  CG  MET A 335      57.189  20.050  17.066  1.00 12.33           C  
-ANISOU  805  CG  MET A 335     1592   1068   2024    151   -171     65       C  
-ATOM    806  SD  MET A 335      56.793  18.377  16.535  1.00 11.92           S  
-ANISOU  806  SD  MET A 335     1427   1127   1974    439   -113    164       S  
-ATOM    807  CE  MET A 335      55.555  18.664  15.282  1.00 11.88           C  
-ANISOU  807  CE  MET A 335     1247   1282   1983    563   -204    -95       C  
-ATOM    808  N   THR A 336      59.861  21.269  13.497  1.00 10.06           N  
-ANISOU  808  N   THR A 336     1276    858   1688    277   -216    -62       N  
-ATOM    809  CA  THR A 336      60.191  22.333  12.570  1.00 10.12           C  
-ANISOU  809  CA  THR A 336     1118   1025   1702    287    -27    -62       C  
-ATOM    810  C   THR A 336      58.864  22.879  12.064  1.00  9.85           C  
-ANISOU  810  C   THR A 336     1264    805   1674     54   -238      7       C  
-ATOM    811  O   THR A 336      57.924  22.117  11.859  1.00 12.70           O  
-ANISOU  811  O   THR A 336     1475    795   2554     42   -482   -196       O  
-ATOM    812  CB  THR A 336      61.045  21.802  11.417  1.00 11.98           C  
-ANISOU  812  CB  THR A 336     1440   1476   1636    546    300    371       C  
-ATOM    813  OG1 THR A 336      62.346  21.469  11.917  1.00 12.82           O  
-ANISOU  813  OG1 THR A 336     1186   1517   2167    401      4     37       O  
-ATOM    814  CG2 THR A 336      61.188  22.844  10.317  1.00 13.95           C  
-ANISOU  814  CG2 THR A 336     1604   1716   1980    512     47    135       C  
-ATOM    815  N   PHE A 337      58.758  24.190  11.875  1.00  9.72           N  
-ANISOU  815  N   PHE A 337     1207    791   1695    111    -73    248       N  
-ATOM    816  CA  PHE A 337      57.490  24.735  11.412  1.00  9.86           C  
-ANISOU  816  CA  PHE A 337     1179    986   1581    308    -56     93       C  
-ATOM    817  C   PHE A 337      57.645  25.845  10.388  1.00  9.33           C  
-ANISOU  817  C   PHE A 337     1397    614   1535    372    -62    128       C  
-ATOM    818  O   PHE A 337      58.706  26.468  10.271  1.00 10.31           O  
-ANISOU  818  O   PHE A 337     1275    833   1807      8     17     53       O  
-ATOM    819  CB  PHE A 337      56.605  25.199  12.580  1.00 10.27           C  
-ANISOU  819  CB  PHE A 337     1194   1174   1533    290   -119   -155       C  
-ATOM    820  CG  PHE A 337      57.147  26.385  13.340  1.00 11.57           C  
-ANISOU  820  CG  PHE A 337     1353   1377   1665    334   -212     34       C  
-ATOM    821  CD1 PHE A 337      56.931  27.684  12.887  1.00 11.47           C  
-ANISOU  821  CD1 PHE A 337     1396   1066   1896    351      8   -159       C  
-ATOM    822  CD2 PHE A 337      57.854  26.203  14.519  1.00 12.77           C  
-ANISOU  822  CD2 PHE A 337     1555   1433   1864    148   -377   -150       C  
-ATOM    823  CE1 PHE A 337      57.419  28.768  13.595  1.00 13.11           C  
-ANISOU  823  CE1 PHE A 337     1579   1395   2008    385   -297   -576       C  
-ATOM    824  CE2 PHE A 337      58.334  27.284  15.235  1.00 13.92           C  
-ANISOU  824  CE2 PHE A 337     1561   1555   2173    384   -236   -387       C  
-ATOM    825  CZ  PHE A 337      58.120  28.564  14.770  1.00 14.04           C  
-ANISOU  825  CZ  PHE A 337     1677   1404   2252    568    -68   -478       C  
-ATOM    826  N   VAL A 338      56.565  26.082   9.649  1.00  9.41           N  
-ANISOU  826  N   VAL A 338     1306    760   1508    431   -270    102       N  
-ATOM    827  CA  VAL A 338      56.501  27.181   8.699  1.00 10.03           C  
-ANISOU  827  CA  VAL A 338     1401    812   1596    456    -78    -20       C  
-ATOM    828  C   VAL A 338      55.148  27.873   8.797  1.00  9.99           C  
-ANISOU  828  C   VAL A 338     1380    687   1727    321    -17    -76       C  
-ATOM    829  O   VAL A 338      54.122  27.226   9.039  1.00 10.48           O  
-ANISOU  829  O   VAL A 338     1329    765   1887    213    -52    175       O  
-ATOM    830  CB  VAL A 338      56.709  26.690   7.244  1.00 10.57           C  
-ANISOU  830  CB  VAL A 338     1420   1068   1528    181     28   -326       C  
-ATOM    831  CG1 VAL A 338      58.140  26.162   7.049  1.00 11.70           C  
-ANISOU  831  CG1 VAL A 338     1041   1299   2104    299    319   -279       C  
-ATOM    832  CG2 VAL A 338      55.676  25.634   6.849  1.00 12.58           C  
-ANISOU  832  CG2 VAL A 338     1552   1422   1805    123    -88   -416       C  
-ATOM    833  N   LYS A 339      55.145  29.189   8.607  1.00 10.02           N  
-ANISOU  833  N   LYS A 339     1253    756   1797    345   -115   -107       N  
-ATOM    834  CA  LYS A 339      53.886  29.899   8.419  1.00 10.68           C  
-ANISOU  834  CA  LYS A 339     1255    755   2046    292   -439   -228       C  
-ATOM    835  C   LYS A 339      53.173  29.333   7.194  1.00 10.86           C  
-ANISOU  835  C   LYS A 339     1256    921   1949    372     91    -58       C  
-ATOM    836  O   LYS A 339      53.824  28.949   6.214  1.00 10.93           O  
-ANISOU  836  O   LYS A 339     1436   1068   1650    459    188     95       O  
-ATOM    837  CB  LYS A 339      54.146  31.400   8.248  1.00 12.51           C  
-ANISOU  837  CB  LYS A 339     1780    698   2273    287    -88     36       C  
-ATOM    838  CG  LYS A 339      54.704  32.054   9.501  1.00 13.09           C  
-ANISOU  838  CG  LYS A 339     2034    728   2211    111   -203   -351       C  
-ATOM    839  CD  LYS A 339      54.692  33.583   9.403  1.00 14.85           C  
-ANISOU  839  CD  LYS A 339     2327    721   2595    124    131     10       C  
-ATOM    840  CE  LYS A 339      55.617  34.075   8.305  1.00 17.32           C  
-ANISOU  840  CE  LYS A 339     2576    838   3166     98     -3     11       C  
-ATOM    841  NZ  LYS A 339      55.712  35.581   8.315  1.00 18.41           N  
-ANISOU  841  NZ  LYS A 339     2798    889   3306    142    115     92       N  
-ATOM    842  N   ILE A 340      51.846  29.253   7.252  1.00  9.72           N  
-ANISOU  842  N   ILE A 340     1105    814   1773    238   -123   -158       N  
-ATOM    843  CA  ILE A 340      51.089  28.587   6.189  1.00 10.83           C  
-ANISOU  843  CA  ILE A 340     1335    696   2084    218   -360     68       C  
-ATOM    844  C   ILE A 340      50.011  29.469   5.532  1.00 10.66           C  
-ANISOU  844  C   ILE A 340     1611    665   1775    346     23    -54       C  
-ATOM    845  O   ILE A 340      49.412  29.076   4.544  1.00 12.71           O  
-ANISOU  845  O   ILE A 340     1838   1241   1751    423   -217    -39       O  
-ATOM    846  CB  ILE A 340      50.507  27.229   6.693  1.00 11.16           C  
-ANISOU  846  CB  ILE A 340     1381   1007   1851    184    -18    140       C  
-ATOM    847  CG1 ILE A 340      50.137  26.299   5.527  1.00 11.79           C  
-ANISOU  847  CG1 ILE A 340     1415   1141   1923    279     24   -359       C  
-ATOM    848  CG2 ILE A 340      49.351  27.447   7.663  1.00 11.64           C  
-ANISOU  848  CG2 ILE A 340      947   1562   1912    276    259     59       C  
-ATOM    849  CD1 ILE A 340      51.310  25.955   4.627  1.00 12.73           C  
-ANISOU  849  CD1 ILE A 340     1663   1126   2048    306     40   -305       C  
-ATOM    850  N   ASN A 341      49.771  30.656   6.080  1.00 11.26           N  
-ANISOU  850  N   ASN A 341     1669    783   1825    500    -14    209       N  
-ATOM    851  CA  ASN A 341      48.881  31.615   5.430  1.00 12.66           C  
-ANISOU  851  CA  ASN A 341     1869   1204   1737    799    128    218       C  
-ATOM    852  C   ASN A 341      49.579  32.201   4.202  1.00 11.88           C  
-ANISOU  852  C   ASN A 341     1841   1140   1534    719    -39     95       C  
-ATOM    853  O   ASN A 341      50.674  32.749   4.314  1.00 12.67           O  
-ANISOU  853  O   ASN A 341     1765   1011   2037    487     22    178       O  
-ATOM    854  CB  ASN A 341      48.509  32.725   6.420  1.00 13.83           C  
-ANISOU  854  CB  ASN A 341     1907   1305   2041    875    111      6       C  
-ATOM    855  CG  ASN A 341      47.421  33.654   5.900  1.00 17.67           C  
-ANISOU  855  CG  ASN A 341     2523   1879   2312   1224    315    181       C  
-ATOM    856  OD1 ASN A 341      47.239  33.821   4.701  1.00 15.95           O  
-ANISOU  856  OD1 ASN A 341     2328   1588   2142   1012     88     37       O  
-ATOM    857  ND2 ASN A 341      46.710  34.286   6.823  1.00 22.67           N  
-ANISOU  857  ND2 ASN A 341     3184   2625   2803   1674    278    156       N  
-ATOM    858  N   PRO A 342      48.949  32.097   3.022  1.00 12.30           N  
-ANISOU  858  N   PRO A 342     1733   1134   1804    386   -135   -114       N  
-ATOM    859  CA  PRO A 342      49.606  32.621   1.817  1.00 13.05           C  
-ANISOU  859  CA  PRO A 342     1973   1332   1652    477    -35   -128       C  
-ATOM    860  C   PRO A 342      50.024  34.091   1.939  1.00 13.56           C  
-ANISOU  860  C   PRO A 342     2205   1302   1643    769    -45   -101       C  
-ATOM    861  O   PRO A 342      51.027  34.480   1.338  1.00 15.43           O  
-ANISOU  861  O   PRO A 342     2380   1541   1940    671   -148     51       O  
-ATOM    862  CB  PRO A 342      48.543  32.454   0.725  1.00 15.73           C  
-ANISOU  862  CB  PRO A 342     2322   1692   1963    398   -120    123       C  
-ATOM    863  CG  PRO A 342      47.657  31.388   1.213  1.00 17.84           C  
-ANISOU  863  CG  PRO A 342     2364   1789   2624    101   -419    143       C  
-ATOM    864  CD  PRO A 342      47.685  31.404   2.716  1.00 13.81           C  
-ANISOU  864  CD  PRO A 342     2188   1584   1473    424   -390     21       C  
-ATOM    865  N   THR A 343      49.288  34.898   2.700  1.00 13.22           N  
-ANISOU  865  N   THR A 343     2124   1007   1893    664    159    254       N  
-ATOM    866  CA  THR A 343      49.653  36.307   2.832  1.00 15.00           C  
-ANISOU  866  CA  THR A 343     2407   1070   2222    689    167    136       C  
-ATOM    867  C   THR A 343      50.935  36.496   3.640  1.00 15.67           C  
-ANISOU  867  C   THR A 343     2522   1208   2224    515    112    424       C  
-ATOM    868  O   THR A 343      51.534  37.577   3.627  1.00 18.28           O  
-ANISOU  868  O   THR A 343     2776   1257   2912    345   -148    256       O  
-ATOM    869  CB  THR A 343      48.520  37.140   3.463  1.00 17.23           C  
-ANISOU  869  CB  THR A 343     2525   1449   2573    883    282    -34       C  
-ATOM    870  OG1 THR A 343      48.302  36.717   4.817  1.00 20.11           O  
-ANISOU  870  OG1 THR A 343     2911   1661   3067    828    599    -57       O  
-ATOM    871  CG2 THR A 343      47.241  36.972   2.671  1.00 19.27           C  
-ANISOU  871  CG2 THR A 343     2353   1711   3256    921     12   -179       C  
-ATOM    872  N   GLU A 344      51.348  35.442   4.341  1.00 14.25           N  
-ANISOU  872  N   GLU A 344     2389   1262   1763    573    -60    117       N  
-ATOM    873  CA  GLU A 344      52.576  35.457   5.132  1.00 13.21           C  
-ANISOU  873  CA  GLU A 344     2252   1138   1630    353     -9     42       C  
-ATOM    874  C   GLU A 344      53.724  34.811   4.365  1.00 14.50           C  
-ANISOU  874  C   GLU A 344     2236   1151   2120    216     55    -71       C  
-ATOM    875  O   GLU A 344      54.819  34.629   4.902  1.00 15.35           O  
-ANISOU  875  O   GLU A 344     2332   1443   2058     83    -44   -231       O  
-ATOM    876  CB  GLU A 344      52.369  34.720   6.459  1.00 14.54           C  
-ANISOU  876  CB  GLU A 344     2386   1207   1929    518    -45     27       C  
-ATOM    877  CG  GLU A 344      51.369  35.389   7.384  1.00 16.17           C  
-ANISOU  877  CG  GLU A 344     2559   1384   2201    570    139   -541       C  
-ATOM    878  CD  GLU A 344      51.919  36.633   8.044  1.00 17.98           C  
-ANISOU  878  CD  GLU A 344     2813   1545   2473    811   -284   -107       C  
-ATOM    879  OE1 GLU A 344      53.161  36.771   8.124  1.00 18.02           O  
-ANISOU  879  OE1 GLU A 344     3256   1350   2239    807   -486   -309       O  
-ATOM    880  OE2 GLU A 344      51.105  37.471   8.488  1.00 20.68           O  
-ANISOU  880  OE2 GLU A 344     2847   1997   3011    844   -174   -469       O  
-ATOM    881  N   LEU A 345      53.466  34.470   3.108  1.00 12.29           N  
-ANISOU  881  N   LEU A 345     2023    767   1878    210     64   -115       N  
-ATOM    882  CA  LEU A 345      54.427  33.724   2.298  1.00 12.42           C  
-ANISOU  882  CA  LEU A 345     2070    652   1998    131     92    -84       C  
-ATOM    883  C   LEU A 345      54.803  34.447   0.997  1.00 13.49           C  
-ANISOU  883  C   LEU A 345     2253    745   2126    193   -166     18       C  
-ATOM    884  O   LEU A 345      55.109  33.805  -0.014  1.00 13.64           O  
-ANISOU  884  O   LEU A 345     2159    991   2031    299     25     83       O  
-ATOM    885  CB  LEU A 345      53.887  32.316   1.993  1.00 12.34           C  
-ANISOU  885  CB  LEU A 345     1860    959   1870    238    343    246       C  
-ATOM    886  CG  LEU A 345      53.691  31.397   3.203  1.00 11.66           C  
-ANISOU  886  CG  LEU A 345     1680   1007   1744    107   -173      0       C  
-ATOM    887  CD1 LEU A 345      52.948  30.110   2.831  1.00 12.65           C  
-ANISOU  887  CD1 LEU A 345     1539   1062   2206     -9     87   -104       C  
-ATOM    888  CD2 LEU A 345      55.027  31.084   3.881  1.00 12.99           C  
-ANISOU  888  CD2 LEU A 345     1676   1354   1903     47   -480     18       C  
-ATOM    889  N   SER A 346      54.794  35.780   1.019  1.00 15.09           N  
-ANISOU  889  N   SER A 346     2468   1012   2251    332     12    239       N  
-ATOM    890  CA  SER A 346      55.197  36.540  -0.160  1.00 15.90           C  
-ANISOU  890  CA  SER A 346     2591   1192   2257    437    138    464       C  
-ATOM    891  C   SER A 346      56.684  36.886  -0.136  1.00 16.39           C  
-ANISOU  891  C   SER A 346     2653   1211   2362    431      7    298       C  
-ATOM    892  O   SER A 346      57.307  37.062  -1.183  1.00 17.34           O  
-ANISOU  892  O   SER A 346     2789   1343   2456    193     54    134       O  
-ATOM    893  CB  SER A 346      54.373  37.820  -0.292  1.00 19.36           C  
-ANISOU  893  CB  SER A 346     2925   1705   2725    884   -125   -243       C  
-ATOM    894  OG  SER A 346      54.691  38.729   0.740  1.00 23.20           O  
-ANISOU  894  OG  SER A 346     3317   2241   3257    970    261    401       O  
-ATOM    895  N   THR A 347      57.242  36.976   1.066  1.00 15.58           N  
-ANISOU  895  N   THR A 347     2453    941   2526    296     84    356       N  
-ATOM    896  CA  THR A 347      58.623  37.399   1.249  1.00 15.97           C  
-ANISOU  896  CA  THR A 347     2722    906   2441    197   -231    273       C  
-ATOM    897  C   THR A 347      59.139  36.919   2.598  1.00 16.91           C  
-ANISOU  897  C   THR A 347     2693   1049   2681    246   -171    151       C  
-ATOM    898  O   THR A 347      58.360  36.716   3.533  1.00 18.03           O  
-ANISOU  898  O   THR A 347     2759   1326   2764    124   -134    219       O  
-ATOM    899  CB  THR A 347      58.754  38.950   1.177  1.00 18.49           C  
-ANISOU  899  CB  THR A 347     2924    992   3110    197     85    246       C  
-ATOM    900  OG1 THR A 347      60.134  39.332   1.266  1.00 21.01           O  
-ANISOU  900  OG1 THR A 347     2924   1068   3992     88    198    194       O  
-ATOM    901  CG2 THR A 347      57.977  39.623   2.316  1.00 19.28           C  
-ANISOU  901  CG2 THR A 347     3044   1012   3268    449     90   -255       C  
-ATOM    902  N   GLY A 348      60.452  36.730   2.692  1.00 15.90           N  
-ANISOU  902  N   GLY A 348     2613    856   2570     99   -496     73       N  
-ATOM    903  CA  GLY A 348      61.087  36.433   3.961  1.00 15.33           C  
-ANISOU  903  CA  GLY A 348     2508    873   2444     64   -207    171       C  
-ATOM    904  C   GLY A 348      61.088  34.964   4.340  1.00 14.68           C  
-ANISOU  904  C   GLY A 348     2351    733   2492    -86      7    144       C  
-ATOM    905  O   GLY A 348      60.476  34.131   3.675  1.00 16.17           O  
-ANISOU  905  O   GLY A 348     2483   1030   2631     44   -132    -65       O  
-ATOM    906  N   ASP A 349      61.778  34.664   5.434  1.00 13.77           N  
-ANISOU  906  N   ASP A 349     2212    837   2183     -5    -74    172       N  
-ATOM    907  CA  ASP A 349      61.915  33.300   5.946  1.00 12.65           C  
-ANISOU  907  CA  ASP A 349     1802    811   2192   -156      1    232       C  
-ATOM    908  C   ASP A 349      60.702  32.975   6.820  1.00 12.28           C  
-ANISOU  908  C   ASP A 349     1807    793   2064   -127   -298   -121       C  
-ATOM    909  O   ASP A 349      60.505  33.590   7.865  1.00 14.27           O  
-ANISOU  909  O   ASP A 349     2070   1084   2269    -21    -32   -265       O  
-ATOM    910  CB  ASP A 349      63.212  33.209   6.755  1.00 14.04           C  
-ANISOU  910  CB  ASP A 349     1705   1187   2443    -21   -273    115       C  
-ATOM    911  CG  ASP A 349      63.512  31.803   7.259  1.00 13.01           C  
-ANISOU  911  CG  ASP A 349     1580    943   2420   -180   -328    -93       C  
-ATOM    912  OD1 ASP A 349      62.604  30.945   7.265  1.00 12.65           O  
-ANISOU  912  OD1 ASP A 349     1604    972   2230   -109     15   -233       O  
-ATOM    913  OD2 ASP A 349      64.671  31.560   7.671  1.00 16.26           O  
-ANISOU  913  OD2 ASP A 349     1691   1429   3056     71   -273      4       O  
-ATOM    914  N   PRO A 350      59.874  32.007   6.390  1.00 10.70           N  
-ANISOU  914  N   PRO A 350     1547    795   1724    -96     17     55       N  
-ATOM    915  CA  PRO A 350      58.642  31.690   7.118  1.00 11.77           C  
-ANISOU  915  CA  PRO A 350     1602    971   1897    -17    -54     44       C  
-ATOM    916  C   PRO A 350      58.848  30.628   8.189  1.00 11.38           C  
-ANISOU  916  C   PRO A 350     1417    797   2111   -326   -224    -29       C  
-ATOM    917  O   PRO A 350      57.869  30.200   8.806  1.00 12.08           O  
-ANISOU  917  O   PRO A 350     1465    926   2200     53   -168    -74       O  
-ATOM    918  CB  PRO A 350      57.760  31.108   6.022  1.00 13.15           C  
-ANISOU  918  CB  PRO A 350     1619   1305   2072     68     80   -164       C  
-ATOM    919  CG  PRO A 350      58.743  30.345   5.160  1.00 13.85           C  
-ANISOU  919  CG  PRO A 350     1787   1238   2238     11     78   -272       C  
-ATOM    920  CD  PRO A 350      60.017  31.189   5.172  1.00 11.67           C  
-ANISOU  920  CD  PRO A 350     1640    975   1817   -311    141   -291       C  
-ATOM    921  N   SER A 351      60.091  30.212   8.412  1.00 11.02           N  
-ANISOU  921  N   SER A 351     1659    723   1805    -82   -395    -80       N  
-ATOM    922  CA  SER A 351      60.348  28.986   9.175  1.00 10.39           C  
-ANISOU  922  CA  SER A 351     1550    744   1654     57    -23     -5       C  
-ATOM    923  C   SER A 351      60.877  29.210  10.590  1.00 10.55           C  
-ANISOU  923  C   SER A 351     1585    890   1533   -104    -84      9       C  
-ATOM    924  O   SER A 351      61.482  30.241  10.901  1.00 12.16           O  
-ANISOU  924  O   SER A 351     1749    857   2014   -141   -242    -90       O  
-ATOM    925  CB  SER A 351      61.315  28.070   8.409  1.00 11.60           C  
-ANISOU  925  CB  SER A 351     1540    949   1917     35    118    -28       C  
-ATOM    926  OG  SER A 351      62.654  28.549   8.442  1.00 13.03           O  
-ANISOU  926  OG  SER A 351     1468   1259   2222      6     -1    -74       O  
-ATOM    927  N   GLY A 352      60.666  28.205  11.431  1.00 12.02           N  
-ANISOU  927  N   GLY A 352     1577   1032   1959    104   -260    153       N  
-ATOM    928  CA  GLY A 352      61.220  28.204  12.766  1.00 12.39           C  
-ANISOU  928  CA  GLY A 352     1812    980   1916     -1   -286    423       C  
-ATOM    929  C   GLY A 352      61.295  26.793  13.302  1.00 10.97           C  
-ANISOU  929  C   GLY A 352     1482    827   1859   -128   -423     46       C  
-ATOM    930  O   GLY A 352      61.075  25.824  12.567  1.00 11.41           O  
-ANISOU  930  O   GLY A 352     1316   1092   1928    -55   -260   -268       O  
-ATOM    931  N   LYS A 353      61.624  26.673  14.581  1.00 12.86           N  
-ANISOU  931  N   LYS A 353     1736   1144   2006     99   -321    186       N  
-ATOM    932  CA  LYS A 353      61.652  25.380  15.238  1.00 11.75           C  
-ANISOU  932  CA  LYS A 353     1858   1056   1550    146   -159    123       C  
-ATOM    933  C   LYS A 353      61.252  25.584  16.681  1.00 11.60           C  
-ANISOU  933  C   LYS A 353     1860    875   1671     13   -169    -17       C  
-ATOM    934  O   LYS A 353      61.368  26.692  17.217  1.00 14.58           O  
-ANISOU  934  O   LYS A 353     2389   1003   2146    -71   -245   -247       O  
-ATOM    935  CB  LYS A 353      63.040  24.763  15.155  1.00 15.21           C  
-ANISOU  935  CB  LYS A 353     2025   1253   2501    216   -388     46       C  
-ATOM    936  CG  LYS A 353      64.113  25.640  15.761  1.00 18.73           C  
-ANISOU  936  CG  LYS A 353     1984   1823   3309    283   -509   -153       C  
-ATOM    937  CD  LYS A 353      65.498  25.103  15.474  1.00 21.85           C  
-ANISOU  937  CD  LYS A 353     2114   2244   3942    442   -726   -119       C  
-ATOM    938  CE  LYS A 353      65.733  23.777  16.172  1.00 21.54           C  
-ANISOU  938  CE  LYS A 353     2148   2055   3979    678   -443     49       C  
-ATOM    939  NZ  LYS A 353      67.166  23.377  16.064  1.00 20.47           N  
-ANISOU  939  NZ  LYS A 353     2204   1923   3649    634   -634   -311       N  
-ATOM    940  N   VAL A 354      60.771  24.524  17.314  1.00 10.73           N  
-ANISOU  940  N   VAL A 354     1469   1073   1536     69    -62    125       N  
-ATOM    941  CA  VAL A 354      60.294  24.630  18.682  1.00 10.50           C  
-ANISOU  941  CA  VAL A 354     1486    923   1579    -33     76     45       C  
-ATOM    942  C   VAL A 354      60.183  23.243  19.295  1.00 10.22           C  
-ANISOU  942  C   VAL A 354     1520    781   1582    144   -188     19       C  
-ATOM    943  O   VAL A 354      60.016  22.254  18.580  1.00 12.94           O  
-ANISOU  943  O   VAL A 354     2094    883   1939    221   -209   -371       O  
-ATOM    944  CB  VAL A 354      58.933  25.364  18.730  1.00 11.92           C  
-ANISOU  944  CB  VAL A 354     1521   1485   1522    331   -400   -500       C  
-ATOM    945  CG1 VAL A 354      57.832  24.507  18.146  1.00 13.08           C  
-ANISOU  945  CG1 VAL A 354     1363   1577   2028    313   -601   -315       C  
-ATOM    946  CG2 VAL A 354      58.591  25.800  20.155  1.00 13.77           C  
-ANISOU  946  CG2 VAL A 354     1532   1519   2180    194   -404   -395       C  
-ATOM    947  N   VAL A 355      60.313  23.173  20.614  1.00 10.95           N  
-ANISOU  947  N   VAL A 355     1556    884   1719    440   -313    131       N  
-ATOM    948  CA  VAL A 355      60.141  21.926  21.341  1.00 10.92           C  
-ANISOU  948  CA  VAL A 355     1439   1168   1540    311   -249    124       C  
-ATOM    949  C   VAL A 355      58.748  21.909  21.962  1.00 10.61           C  
-ANISOU  949  C   VAL A 355     1439   1109   1482    343   -182   -357       C  
-ATOM    950  O   VAL A 355      58.297  22.912  22.535  1.00 10.97           O  
-ANISOU  950  O   VAL A 355     1594   1000   1573    455   -132   -354       O  
-ATOM    951  CB  VAL A 355      61.198  21.777  22.451  1.00 11.76           C  
-ANISOU  951  CB  VAL A 355     1649   1186   1633    258   -316    100       C  
-ATOM    952  CG1 VAL A 355      60.983  20.487  23.225  1.00 14.53           C  
-ANISOU  952  CG1 VAL A 355     1810   1609   2100    280   -489    237       C  
-ATOM    953  CG2 VAL A 355      62.599  21.838  21.856  1.00 13.69           C  
-ANISOU  953  CG2 VAL A 355     1730   1333   2137    331     -8   -155       C  
-ATOM    954  N   ILE A 356      58.063  20.779  21.826  1.00 10.70           N  
-ANISOU  954  N   ILE A 356     1392   1052   1621    140   -151   -196       N  
-ATOM    955  CA  ILE A 356      56.779  20.564  22.482  1.00 10.30           C  
-ANISOU  955  CA  ILE A 356     1493   1130   1288    295   -217    -62       C  
-ATOM    956  C   ILE A 356      56.863  19.324  23.370  1.00 10.04           C  
-ANISOU  956  C   ILE A 356     1531    890   1392    168   -184    -93       C  
-ATOM    957  O   ILE A 356      57.154  18.220  22.892  1.00 11.63           O  
-ANISOU  957  O   ILE A 356     1906    823   1688    372   -267   -213       O  
-ATOM    958  CB  ILE A 356      55.641  20.390  21.448  1.00 10.82           C  
-ANISOU  958  CB  ILE A 356     1565   1082   1463    224   -169   -107       C  
-ATOM    959  CG1 ILE A 356      55.539  21.644  20.562  1.00 11.53           C  
-ANISOU  959  CG1 ILE A 356     1885    927   1570    477   -512     32       C  
-ATOM    960  CG2 ILE A 356      54.303  20.099  22.141  1.00 11.88           C  
-ANISOU  960  CG2 ILE A 356     1382   1444   1687     29     15   -102       C  
-ATOM    961  CD1 ILE A 356      54.509  21.529  19.461  1.00 11.41           C  
-ANISOU  961  CD1 ILE A 356     1725   1111   1499    399   -431    -34       C  
-ATOM    962  N   HIS A 357      56.604  19.505  24.658  1.00 10.69           N  
-ANISOU  962  N   HIS A 357     1580   1245   1235    299   -312      6       N  
-ATOM    963  CA  HIS A 357      56.543  18.390  25.600  1.00 10.70           C  
-ANISOU  963  CA  HIS A 357     1685   1120   1259    275   -472   -122       C  
-ATOM    964  C   HIS A 357      55.227  17.649  25.441  1.00 10.08           C  
-ANISOU  964  C   HIS A 357     1550    879   1399    187   -484    -58       C  
-ATOM    965  O   HIS A 357      54.160  18.259  25.528  1.00 11.52           O  
-ANISOU  965  O   HIS A 357     1504   1059   1815    377   -348    -14       O  
-ATOM    966  CB  HIS A 357      56.619  18.911  27.039  1.00 12.11           C  
-ANISOU  966  CB  HIS A 357     1789   1394   1416    158   -605   -249       C  
-ATOM    967  CG  HIS A 357      57.927  19.547  27.385  1.00 12.68           C  
-ANISOU  967  CG  HIS A 357     1870   1391   1557    246   -814   -281       C  
-ATOM    968  ND1 HIS A 357      58.124  20.249  28.557  1.00 13.95           N  
-ANISOU  968  ND1 HIS A 357     2267   1582   1452    452   -599   -471       N  
-ATOM    969  CD2 HIS A 357      59.105  19.582  26.722  1.00 14.36           C  
-ANISOU  969  CD2 HIS A 357     1823   1510   2123    417   -596    276       C  
-ATOM    970  CE1 HIS A 357      59.370  20.687  28.598  1.00 15.69           C  
-ANISOU  970  CE1 HIS A 357     2105   1497   2357    240   -754   -276       C  
-ATOM    971  NE2 HIS A 357      59.989  20.295  27.500  1.00 14.45           N  
-ANISOU  971  NE2 HIS A 357     1942   1378   2168    225   -525   -102       N  
-ATOM    972  N   SER A 358      55.283  16.334  25.235  1.00 10.61           N  
-ANISOU  972  N   SER A 358     1673   1032   1326     94   -120    165       N  
-ATOM    973  CA  SER A 358      54.055  15.536  25.243  1.00 10.37           C  
-ANISOU  973  CA  SER A 358     1690   1055   1196    128    -45   -115       C  
-ATOM    974  C   SER A 358      53.782  15.022  26.662  1.00 11.68           C  
-ANISOU  974  C   SER A 358     1805   1186   1448    319    -29     42       C  
-ATOM    975  O   SER A 358      53.616  13.818  26.899  1.00 12.61           O  
-ANISOU  975  O   SER A 358     1897   1119   1776    404   -110     -1       O  
-ATOM    976  CB  SER A 358      54.087  14.401  24.213  1.00 10.67           C  
-ANISOU  976  CB  SER A 358     1502    965   1587    430   -248   -239       C  
-ATOM    977  OG  SER A 358      55.219  13.576  24.387  1.00 10.68           O  
-ANISOU  977  OG  SER A 358     1347   1055   1657    463   -221   -104       O  
-ATOM    978  N   TYR A 359      53.754  15.961  27.602  1.00 11.91           N  
-ANISOU  978  N   TYR A 359     1847   1484   1193    440   -102   -249       N  
-ATOM    979  CA  TYR A 359      53.536  15.671  29.015  1.00 11.78           C  
-ANISOU  979  CA  TYR A 359     1879   1418   1178    688     19   -108       C  
-ATOM    980  C   TYR A 359      53.251  16.975  29.741  1.00 13.60           C  
-ANISOU  980  C   TYR A 359     2081   1354   1732    595   -188   -368       C  
-ATOM    981  O   TYR A 359      53.408  18.050  29.153  1.00 12.96           O  
-ANISOU  981  O   TYR A 359     1979   1322   1621    383   -167   -201       O  
-ATOM    982  CB  TYR A 359      54.739  14.935  29.636  1.00 13.04           C  
-ANISOU  982  CB  TYR A 359     1871   1482   1602    547   -239     29       C  
-ATOM    983  CG  TYR A 359      56.091  15.598  29.446  1.00 12.64           C  
-ANISOU  983  CG  TYR A 359     1924   1443   1434    377   -464    -61       C  
-ATOM    984  CD1 TYR A 359      56.597  16.482  30.397  1.00 14.78           C  
-ANISOU  984  CD1 TYR A 359     2210   1654   1751    457   -405     41       C  
-ATOM    985  CD2 TYR A 359      56.870  15.328  28.317  1.00 12.87           C  
-ANISOU  985  CD2 TYR A 359     1948   1445   1497    504   -190    271       C  
-ATOM    986  CE1 TYR A 359      57.837  17.080  30.233  1.00 14.09           C  
-ANISOU  986  CE1 TYR A 359     2210   1548   1593    499   -442   -240       C  
-ATOM    987  CE2 TYR A 359      58.112  15.925  28.139  1.00 13.29           C  
-ANISOU  987  CE2 TYR A 359     2034   1083   1931    298   -545      3       C  
-ATOM    988  CZ  TYR A 359      58.591  16.794  29.103  1.00 12.94           C  
-ANISOU  988  CZ  TYR A 359     2031   1206   1677    216   -304   -158       C  
-ATOM    989  OH  TYR A 359      59.820  17.386  28.943  1.00 13.85           O  
-ANISOU  989  OH  TYR A 359     1972   1374   1916    470   -264    -50       O  
-ATOM    990  N   ASP A 360      52.846  16.854  31.010  1.00 14.17           N  
-ANISOU  990  N   ASP A 360     2250   1732   1403    732    -69   -411       N  
-ATOM    991  CA  ASP A 360      52.366  17.955  31.859  1.00 14.10           C  
-ANISOU  991  CA  ASP A 360     2206   1739   1411    621   -103   -384       C  
-ATOM    992  C   ASP A 360      50.955  18.395  31.472  1.00 13.03           C  
-ANISOU  992  C   ASP A 360     2136   1501   1314    489   -153     86       C  
-ATOM    993  O   ASP A 360      50.499  18.146  30.355  1.00 13.72           O  
-ANISOU  993  O   ASP A 360     2321   1350   1543    449   -160    -54       O  
-ATOM    994  CB  ASP A 360      53.327  19.155  31.874  1.00 16.74           C  
-ANISOU  994  CB  ASP A 360     2172   2030   2158    407   -365   -746       C  
-ATOM    995  CG  ASP A 360      54.653  18.838  32.534  1.00 16.96           C  
-ANISOU  995  CG  ASP A 360     2670   2179   1593    434   -370   -549       C  
-ATOM    996  OD1 ASP A 360      54.715  17.904  33.369  1.00 20.01           O  
-ANISOU  996  OD1 ASP A 360     3045   2390   2166    643   -420   -110       O  
-ATOM    997  OD2 ASP A 360      55.637  19.533  32.223  1.00 18.56           O  
-ANISOU  997  OD2 ASP A 360     2727   2259   2066    173   -382   -375       O  
-ATOM    998  N   ALA A 361      50.268  19.043  32.406  1.00 14.70           N  
-ANISOU  998  N   ALA A 361     2433   1618   1533    778    426     69       N  
-ATOM    999  CA  ALA A 361      48.875  19.430  32.205  1.00 15.39           C  
-ANISOU  999  CA  ALA A 361     2222   1791   1833    705    377     63       C  
-ATOM   1000  C   ALA A 361      48.706  20.365  31.009  1.00 14.52           C  
-ANISOU 1000  C   ALA A 361     1978   1639   1899    518    302   -198       C  
-ATOM   1001  O   ALA A 361      47.631  20.431  30.412  1.00 15.39           O  
-ANISOU 1001  O   ALA A 361     1827   1697   2322    307     92   -225       O  
-ATOM   1002  CB  ALA A 361      48.318  20.069  33.465  1.00 17.85           C  
-ANISOU 1002  CB  ALA A 361     2612   2370   1800    861    345   -506       C  
-ATOM   1003  N   THR A 362      49.772  21.090  30.671  1.00 13.08           N  
-ANISOU 1003  N   THR A 362     2084   1500   1385    700     60   -102       N  
-ATOM   1004  CA  THR A 362      49.746  22.027  29.553  1.00 13.35           C  
-ANISOU 1004  CA  THR A 362     1996   1506   1571    532   -211   -254       C  
-ATOM   1005  C   THR A 362      49.842  21.331  28.189  1.00 12.12           C  
-ANISOU 1005  C   THR A 362     1890   1369   1344    475   -172    -35       C  
-ATOM   1006  O   THR A 362      49.719  21.974  27.147  1.00 13.37           O  
-ANISOU 1006  O   THR A 362     1898   1620   1562    621     41   -152       O  
-ATOM   1007  CB  THR A 362      50.855  23.075  29.679  1.00 14.17           C  
-ANISOU 1007  CB  THR A 362     1970   1280   2135    348   -272   -795       C  
-ATOM   1008  OG1 THR A 362      52.086  22.431  30.036  1.00 14.15           O  
-ANISOU 1008  OG1 THR A 362     1977   1475   1924    405    -91   -482       O  
-ATOM   1009  CG2 THR A 362      50.499  24.081  30.763  1.00 16.79           C  
-ANISOU 1009  CG2 THR A 362     2340   1423   2616    377    207   -844       C  
-ATOM   1010  N   PHE A 363      50.080  20.022  28.190  1.00 11.79           N  
-ANISOU 1010  N   PHE A 363     1791   1280   1408    507     -9   -244       N  
-ATOM   1011  CA  PHE A 363      49.938  19.230  26.972  1.00 11.65           C  
-ANISOU 1011  CA  PHE A 363     1633   1181   1612    503   -148   -243       C  
-ATOM   1012  C   PHE A 363      48.488  18.755  26.932  1.00 11.43           C  
-ANISOU 1012  C   PHE A 363     1558   1139   1646    444     51     90       C  
-ATOM   1013  O   PHE A 363      48.119  17.804  27.620  1.00 12.63           O  
-ANISOU 1013  O   PHE A 363     1838   1414   1546    537   -108    -19       O  
-ATOM   1014  CB  PHE A 363      50.924  18.051  26.969  1.00 11.16           C  
-ANISOU 1014  CB  PHE A 363     1642   1004   1592    513    -21   -354       C  
-ATOM   1015  CG  PHE A 363      50.787  17.135  25.778  1.00 10.70           C  
-ANISOU 1015  CG  PHE A 363     1529   1055   1480    398    -28    -52       C  
-ATOM   1016  CD1 PHE A 363      51.214  17.537  24.519  1.00 11.25           C  
-ANISOU 1016  CD1 PHE A 363     1624   1259   1389    601   -193   -139       C  
-ATOM   1017  CD2 PHE A 363      50.236  15.870  25.920  1.00 11.78           C  
-ANISOU 1017  CD2 PHE A 363     1631   1386   1459    595    -41   -158       C  
-ATOM   1018  CE1 PHE A 363      51.090  16.693  23.419  1.00 12.47           C  
-ANISOU 1018  CE1 PHE A 363     1657   1181   1898    598    -74     77       C  
-ATOM   1019  CE2 PHE A 363      50.111  15.019  24.827  1.00 12.07           C  
-ANISOU 1019  CE2 PHE A 363     1546   1381   1658    494    -73   -262       C  
-ATOM   1020  CZ  PHE A 363      50.536  15.432  23.572  1.00 12.07           C  
-ANISOU 1020  CZ  PHE A 363     1595   1504   1485    439    151    184       C  
-ATOM   1021  N   ALA A 364      47.659  19.443  26.147  1.00 10.86           N  
-ANISOU 1021  N   ALA A 364     1419   1159   1548    518   -136     -5       N  
-ATOM   1022  CA  ALA A 364      46.223  19.195  26.166  1.00 11.01           C  
-ANISOU 1022  CA  ALA A 364     1384   1438   1359    413      9   -319       C  
-ATOM   1023  C   ALA A 364      45.619  19.195  24.754  1.00 10.66           C  
-ANISOU 1023  C   ALA A 364     1541   1222   1287    312    101    -52       C  
-ATOM   1024  O   ALA A 364      44.635  19.894  24.490  1.00 11.61           O  
-ANISOU 1024  O   ALA A 364     1400   1382   1630    525     31     12       O  
-ATOM   1025  CB  ALA A 364      45.521  20.237  27.059  1.00 12.45           C  
-ANISOU 1025  CB  ALA A 364     1603   1561   1565    425    -73   -487       C  
-ATOM   1026  N   PRO A 365      46.195  18.400  23.839  1.00 10.54           N  
-ANISOU 1026  N   PRO A 365     1586   1046   1371    557    190   -132       N  
-ATOM   1027  CA  PRO A 365      45.741  18.496  22.445  1.00 11.13           C  
-ANISOU 1027  CA  PRO A 365     1568   1271   1391    230     29   -242       C  
-ATOM   1028  C   PRO A 365      44.258  18.151  22.269  1.00 11.25           C  
-ANISOU 1028  C   PRO A 365     1481   1402   1390    -52    243     -9       C  
-ATOM   1029  O   PRO A 365      43.601  18.711  21.396  1.00 12.85           O  
-ANISOU 1029  O   PRO A 365     1687   1753   1441    279    -63    -21       O  
-ATOM   1030  CB  PRO A 365      46.641  17.493  21.708  1.00 12.33           C  
-ANISOU 1030  CB  PRO A 365     1688   1106   1890    473    175   -214       C  
-ATOM   1031  CG  PRO A 365      47.102  16.523  22.784  1.00 12.33           C  
-ANISOU 1031  CG  PRO A 365     1830   1051   1805    431     -2   -266       C  
-ATOM   1032  CD  PRO A 365      47.276  17.411  24.005  1.00 11.64           C  
-ANISOU 1032  CD  PRO A 365     1748    823   1851    359     71   -419       C  
-ATOM   1033  N   HIS A 366      43.737  17.252  23.099  1.00 11.33           N  
-ANISOU 1033  N   HIS A 366     1466   1454   1386     85    251   -167       N  
-ATOM   1034  CA  HIS A 366      42.327  16.881  23.037  1.00 12.03           C  
-ANISOU 1034  CA  HIS A 366     1526   1291   1753    139    215    -48       C  
-ATOM   1035  C   HIS A 366      41.443  18.082  23.374  1.00 11.92           C  
-ANISOU 1035  C   HIS A 366     1388   1464   1675    180    -15   -154       C  
-ATOM   1036  O   HIS A 366      40.295  18.162  22.926  1.00 13.94           O  
-ANISOU 1036  O   HIS A 366     1469   1991   1835    289    -77   -241       O  
-ATOM   1037  CB  HIS A 366      42.049  15.732  24.009  1.00 12.95           C  
-ANISOU 1037  CB  HIS A 366     1626   1507   1786   -189    133    -40       C  
-ATOM   1038  CG  HIS A 366      40.674  15.150  23.899  1.00 15.01           C  
-ANISOU 1038  CG  HIS A 366     1730   2178   1794     52    231   -133       C  
-ATOM   1039  ND1 HIS A 366      40.170  14.645  22.719  1.00 16.84           N  
-ANISOU 1039  ND1 HIS A 366     1745   2632   2022   -182     65     43       N  
-ATOM   1040  CD2 HIS A 366      39.712  14.957  24.831  1.00 16.75           C  
-ANISOU 1040  CD2 HIS A 366     1715   2622   2028     22    103   -246       C  
-ATOM   1041  CE1 HIS A 366      38.952  14.179  22.926  1.00 18.10           C  
-ANISOU 1041  CE1 HIS A 366     1926   3233   1718      1     53   -141       C  
-ATOM   1042  NE2 HIS A 366      38.649  14.356  24.199  1.00 19.24           N  
-ANISOU 1042  NE2 HIS A 366     1763   3152   2394   -263     65    -79       N  
-ATOM   1043  N   LEU A 367      41.981  18.999  24.177  1.00 11.80           N  
-ANISOU 1043  N   LEU A 367     1605   1252   1627    405    123   -339       N  
-ATOM   1044  CA  LEU A 367      41.283  20.230  24.554  1.00 11.81           C  
-ANISOU 1044  CA  LEU A 367     1641   1468   1377    511   -118    -95       C  
-ATOM   1045  C   LEU A 367      41.560  21.345  23.551  1.00 12.75           C  
-ANISOU 1045  C   LEU A 367     1606   1519   1718    558   -132    104       C  
-ATOM   1046  O   LEU A 367      40.988  22.429  23.643  1.00 14.49           O  
-ANISOU 1046  O   LEU A 367     1914   1889   1700    727     95    121       O  
-ATOM   1047  CB  LEU A 367      41.711  20.694  25.950  1.00 11.66           C  
-ANISOU 1047  CB  LEU A 367     1626   1680   1125    522    -51    -98       C  
-ATOM   1048  CG  LEU A 367      41.216  19.898  27.154  1.00 13.95           C  
-ANISOU 1048  CG  LEU A 367     1941   1893   1464    436    153    114       C  
-ATOM   1049  CD1 LEU A 367      41.687  18.456  27.092  1.00 17.38           C  
-ANISOU 1049  CD1 LEU A 367     2431   2134   2036    445    120    102       C  
-ATOM   1050  CD2 LEU A 367      41.682  20.557  28.443  1.00 14.13           C  
-ANISOU 1050  CD2 LEU A 367     1922   2013   1433    416    -27   -108       C  
-ATOM   1051  N   GLY A 368      42.470  21.085  22.616  1.00 11.89           N  
-ANISOU 1051  N   GLY A 368     1422   1411   1685    106     30    176       N  
-ATOM   1052  CA  GLY A 368      42.776  22.032  21.560  1.00 11.78           C  
-ANISOU 1052  CA  GLY A 368     1483   1221   1771     65    -13     95       C  
-ATOM   1053  C   GLY A 368      44.064  22.830  21.698  1.00 11.11           C  
-ANISOU 1053  C   GLY A 368     1311   1384   1526    288   -191   -123       C  
-ATOM   1054  O   GLY A 368      44.350  23.673  20.836  1.00 12.48           O  
-ANISOU 1054  O   GLY A 368     1702   1427   1612    286    137     -6       O  
-ATOM   1055  N   THR A 369      44.842  22.584  22.754  1.00 11.37           N  
-ANISOU 1055  N   THR A 369     1182   1415   1724    312   -101   -137       N  
-ATOM   1056  CA  THR A 369      46.050  23.378  22.991  1.00 11.52           C  
-ANISOU 1056  CA  THR A 369     1466   1422   1489    608   -145   -205       C  
-ATOM   1057  C   THR A 369      47.251  22.563  23.466  1.00 11.02           C  
-ANISOU 1057  C   THR A 369     1445   1387   1354    494   -149     47       C  
-ATOM   1058  O   THR A 369      47.100  21.595  24.219  1.00 13.09           O  
-ANISOU 1058  O   THR A 369     1662   1425   1887    387   -171    196       O  
-ATOM   1059  CB  THR A 369      45.812  24.527  24.009  1.00 13.80           C  
-ANISOU 1059  CB  THR A 369     2063   1537   1642    797    -84   -267       C  
-ATOM   1060  OG1 THR A 369      45.522  23.983  25.302  1.00 16.72           O  
-ANISOU 1060  OG1 THR A 369     2317   2068   1966    844    -75   -229       O  
-ATOM   1061  CG2 THR A 369      44.660  25.422  23.565  1.00 14.57           C  
-ANISOU 1061  CG2 THR A 369     2002   1259   2275    770   -440   -235       C  
-ATOM   1062  N   VAL A 370      48.441  22.969  23.032  1.00 11.05           N  
-ANISOU 1062  N   VAL A 370     1086   1440   1672    155    -69   -201       N  
-ATOM   1063  CA  VAL A 370      49.685  22.453  23.602  1.00 11.03           C  
-ANISOU 1063  CA  VAL A 370     1156   1343   1690    223   -306   -252       C  
-ATOM   1064  C   VAL A 370      50.637  23.606  23.894  1.00 10.85           C  
-ANISOU 1064  C   VAL A 370     1268   1075   1778    323   -269   -148       C  
-ATOM   1065  O   VAL A 370      50.653  24.616  23.178  1.00 11.61           O  
-ANISOU 1065  O   VAL A 370     1549   1196   1664    336   -412     77       O  
-ATOM   1066  CB  VAL A 370      50.385  21.415  22.681  1.00 11.45           C  
-ANISOU 1066  CB  VAL A 370     1694   1207   1450    285     30   -256       C  
-ATOM   1067  CG1 VAL A 370      49.510  20.185  22.509  1.00 13.29           C  
-ANISOU 1067  CG1 VAL A 370     1835   1260   1954     52   -212   -146       C  
-ATOM   1068  CG2 VAL A 370      50.748  22.040  21.332  1.00 13.39           C  
-ANISOU 1068  CG2 VAL A 370     1807   1346   1933    267    119   -219       C  
-ATOM   1069  N   LYS A 371      51.422  23.455  24.951  1.00 12.23           N  
-ANISOU 1069  N   LYS A 371     1476   1355   1817    180   -688   -456       N  
-ATOM   1070  CA  LYS A 371      52.431  24.446  25.293  1.00 11.66           C  
-ANISOU 1070  CA  LYS A 371     1609   1273   1548    305   -770   -502       C  
-ATOM   1071  C   LYS A 371      53.667  24.268  24.411  1.00 11.48           C  
-ANISOU 1071  C   LYS A 371     1464   1314   1585    566   -190   -378       C  
-ATOM   1072  O   LYS A 371      54.091  23.136  24.130  1.00 12.17           O  
-ANISOU 1072  O   LYS A 371     1524   1313   1785    469   -232   -372       O  
-ATOM   1073  CB  LYS A 371      52.827  24.342  26.776  1.00 12.33           C  
-ANISOU 1073  CB  LYS A 371     1911   1327   1447    238   -810   -212       C  
-ATOM   1074  CG  LYS A 371      54.005  25.229  27.150  1.00 13.09           C  
-ANISOU 1074  CG  LYS A 371     2049   1576   1346     20   -807   -391       C  
-ATOM   1075  CD  LYS A 371      54.362  25.119  28.625  1.00 16.11           C  
-ANISOU 1075  CD  LYS A 371     2262   1897   1963     69   -922   -759       C  
-ATOM   1076  CE  LYS A 371      55.546  26.009  28.962  1.00 16.85           C  
-ANISOU 1076  CE  LYS A 371     2548   1948   1905    119  -1055   -592       C  
-ATOM   1077  NZ  LYS A 371      55.949  25.889  30.394  1.00 19.08           N  
-ANISOU 1077  NZ  LYS A 371     2892   2297   2060    518   -735   -277       N  
-ATOM   1078  N   LEU A 372      54.234  25.393  23.981  1.00 11.11           N  
-ANISOU 1078  N   LEU A 372     1290   1336   1595    229   -148   -116       N  
-ATOM   1079  CA  LEU A 372      55.520  25.425  23.293  1.00 11.96           C  
-ANISOU 1079  CA  LEU A 372     1438   1226   1881    334   -367   -250       C  
-ATOM   1080  C   LEU A 372      56.596  25.900  24.260  1.00 13.44           C  
-ANISOU 1080  C   LEU A 372     1446   1407   2253    347   -473   -120       C  
-ATOM   1081  O   LEU A 372      56.387  26.867  24.989  1.00 15.33           O  
-ANISOU 1081  O   LEU A 372     1831   1398   2595    356   -470   -639       O  
-ATOM   1082  CB  LEU A 372      55.457  26.393  22.111  1.00 13.14           C  
-ANISOU 1082  CB  LEU A 372     1653   1534   1803    100   -365   -148       C  
-ATOM   1083  CG  LEU A 372      54.984  25.804  20.772  1.00 16.50           C  
-ANISOU 1083  CG  LEU A 372     1872   2120   2278   -368   -489    716       C  
-ATOM   1084  CD1 LEU A 372      53.768  24.883  20.913  1.00 19.01           C  
-ANISOU 1084  CD1 LEU A 372     2491   1887   2845    119   -541   -129       C  
-ATOM   1085  CD2 LEU A 372      54.728  26.931  19.773  1.00 17.79           C  
-ANISOU 1085  CD2 LEU A 372     1855   2367   2537   -114   -310    787       C  
-ATOM   1086  N   GLU A 373      57.749  25.237  24.262  1.00 12.10           N  
-ANISOU 1086  N   GLU A 373     1415   1307   1876    370   -412   -374       N  
-ATOM   1087  CA  GLU A 373      58.876  25.711  25.063  1.00 12.49           C  
-ANISOU 1087  CA  GLU A 373     1521   1107   2116    186   -733   -224       C  
-ATOM   1088  C   GLU A 373      59.409  27.007  24.462  1.00 14.55           C  
-ANISOU 1088  C   GLU A 373     1773   1422   2331     69   -684   -448       C  
-ATOM   1089  O   GLU A 373      59.622  27.099  23.253  1.00 15.52           O  
-ANISOU 1089  O   GLU A 373     2051   1455   2392    -18   -530   -378       O  
-ATOM   1090  CB  GLU A 373      59.979  24.650  25.136  1.00 13.21           C  
-ANISOU 1090  CB  GLU A 373     1631   1200   2188    478   -487     97       C  
-ATOM   1091  CG  GLU A 373      59.515  23.371  25.811  1.00 14.34           C  
-ANISOU 1091  CG  GLU A 373     1916   1510   2020    518   -344   -181       C  
-ATOM   1092  CD  GLU A 373      58.995  23.636  27.215  1.00 14.16           C  
-ANISOU 1092  CD  GLU A 373     1983   1555   1842    139   -598   -438       C  
-ATOM   1093  OE1 GLU A 373      59.790  24.102  28.056  1.00 17.31           O  
-ANISOU 1093  OE1 GLU A 373     2337   1973   2268    220   -743   -645       O  
-ATOM   1094  OE2 GLU A 373      57.789  23.409  27.466  1.00 14.44           O  
-ANISOU 1094  OE2 GLU A 373     2025   1447   2012    190   -664   -222       O  
-ATOM   1095  N   ASP A 374      59.630  28.009  25.303  1.00 14.29           N  
-ANISOU 1095  N   ASP A 374     1828   1224   2378     86   -707   -497       N  
-ATOM   1096  CA  ASP A 374      60.126  29.282  24.810  1.00 15.78           C  
-ANISOU 1096  CA  ASP A 374     1961   1309   2725    -56   -701   -496       C  
-ATOM   1097  C   ASP A 374      61.595  29.166  24.430  1.00 16.81           C  
-ANISOU 1097  C   ASP A 374     2027   1851   2509   -227   -674   -391       C  
-ATOM   1098  O   ASP A 374      62.433  28.854  25.268  1.00 21.31           O  
-ANISOU 1098  O   ASP A 374     2261   2823   3011    125   -565    241       O  
-ATOM   1099  CB  ASP A 374      59.935  30.367  25.871  1.00 17.36           C  
-ANISOU 1099  CB  ASP A 374     2516   1306   2772    103   -515   -855       C  
-ATOM   1100  CG  ASP A 374      60.277  31.760  25.365  1.00 21.17           C  
-ANISOU 1100  CG  ASP A 374     2865   1638   3541    196   -820   -770       C  
-ATOM   1101  OD1 ASP A 374      60.521  31.924  24.151  1.00 21.77           O  
-ANISOU 1101  OD1 ASP A 374     2903   1625   3744     63   -753   -693       O  
-ATOM   1102  OD2 ASP A 374      60.292  32.698  26.191  1.00 23.84           O  
-ANISOU 1102  OD2 ASP A 374     3203   1953   3903    306   -724   -823       O  
-ATOM   1103  N   ASN A 375      61.904  29.412  23.161  1.00 18.15           N  
-ANISOU 1103  N   ASN A 375     2013   2148   2735   -216   -399   -579       N  
-ATOM   1104  CA  ASN A 375      63.289  29.416  22.700  1.00 19.16           C  
-ANISOU 1104  CA  ASN A 375     2423   2202   2653   -419   -272   -443       C  
-ATOM   1105  C   ASN A 375      63.753  30.810  22.290  1.00 21.53           C  
-ANISOU 1105  C   ASN A 375     2661   2643   2877   -296   -451   -281       C  
-ATOM   1106  O   ASN A 375      64.770  30.957  21.613  1.00 22.28           O  
-ANISOU 1106  O   ASN A 375     2609   2687   3167   -380   -435   -198       O  
-ATOM   1107  CB  ASN A 375      63.483  28.428  21.548  1.00 20.19           C  
-ANISOU 1107  CB  ASN A 375     2583   2259   2830   -424   -434   -818       C  
-ATOM   1108  CG  ASN A 375      62.619  28.752  20.345  1.00 21.50           C  
-ANISOU 1108  CG  ASN A 375     2811   2506   2853   -403   -446   -592       C  
-ATOM   1109  OD1 ASN A 375      62.063  29.846  20.238  1.00 22.99           O  
-ANISOU 1109  OD1 ASN A 375     2621   2841   3272   -581   -911   -668       O  
-ATOM   1110  ND2 ASN A 375      62.504  27.799  19.430  1.00 22.95           N  
-ANISOU 1110  ND2 ASN A 375     3097   2405   3217   -329   -465   -712       N  
-ATOM   1111  N   ASN A 376      62.994  31.821  22.708  1.00 21.62           N  
-ANISOU 1111  N   ASN A 376     2701   2429   3085   -289   -659   -399       N  
-ATOM   1112  CA  ASN A 376      63.308  33.224  22.436  1.00 23.37           C  
-ANISOU 1112  CA  ASN A 376     2780   2550   3550   -547   -946   -395       C  
-ATOM   1113  C   ASN A 376      63.180  33.610  20.963  1.00 23.80           C  
-ANISOU 1113  C   ASN A 376     2688   2796   3558   -662   -868   -222       C  
-ATOM   1114  O   ASN A 376      63.604  34.691  20.555  1.00 26.07           O  
-ANISOU 1114  O   ASN A 376     2846   3029   4028   -549   -606    157       O  
-ATOM   1115  CB  ASN A 376      64.702  33.584  22.957  1.00 27.28           C  
-ANISOU 1115  CB  ASN A 376     3181   3152   4033   -257  -1134   -829       C  
-ATOM   1116  CG  ASN A 376      64.799  33.504  24.469  1.00 33.27           C  
-ANISOU 1116  CG  ASN A 376     3559   3811   5269     16  -1209   -833       C  
-ATOM   1117  OD1 ASN A 376      63.831  33.770  25.182  1.00 35.85           O  
-ANISOU 1117  OD1 ASN A 376     3926   3993   5703    374  -1013  -1079       O  
-ATOM   1118  ND2 ASN A 376      65.974  33.138  24.967  1.00 37.15           N  
-ANISOU 1118  ND2 ASN A 376     3873   4361   5879    533  -1083   -495       N  
-ATOM   1119  N   GLU A 377      62.585  32.731  20.167  1.00 23.20           N  
-ANISOU 1119  N   GLU A 377     2455   3177   3181   -655   -953    -18       N  
-ATOM   1120  CA  GLU A 377      62.415  33.012  18.747  1.00 24.65           C  
-ANISOU 1120  CA  GLU A 377     2589   3461   3315   -388   -910   -160       C  
-ATOM   1121  C   GLU A 377      60.994  32.714  18.273  1.00 20.87           C  
-ANISOU 1121  C   GLU A 377     2384   2979   2565   -507   -851   -570       C  
-ATOM   1122  O   GLU A 377      60.775  32.344  17.115  1.00 24.00           O  
-ANISOU 1122  O   GLU A 377     2397   3916   2804   -287   -450   -225       O  
-ATOM   1123  CB  GLU A 377      63.462  32.251  17.933  1.00 30.61           C  
-ANISOU 1123  CB  GLU A 377     2924   4393   4314   -252  -1063   -292       C  
-ATOM   1124  CG  GLU A 377      64.880  32.710  18.277  1.00 36.50           C  
-ANISOU 1124  CG  GLU A 377     3141   5030   5697   -237  -1543   -784       C  
-ATOM   1125  CD  GLU A 377      65.968  31.880  17.635  1.00 44.34           C  
-ANISOU 1125  CD  GLU A 377     3672   5894   7280    160  -1537   -945       C  
-ATOM   1126  OE1 GLU A 377      65.642  30.954  16.869  1.00 47.80           O  
-ANISOU 1126  OE1 GLU A 377     3943   6282   7936    519  -1456  -1041       O  
-ATOM   1127  OE2 GLU A 377      67.158  32.155  17.902  1.00 47.29           O  
-ANISOU 1127  OE2 GLU A 377     3872   6353   7741    278  -1708   -914       O  
-ATOM   1128  N   LEU A 378      60.032  32.891  19.175  1.00 19.20           N  
-ANISOU 1128  N   LEU A 378     2448   2249   2598   -209   -372    202       N  
-ATOM   1129  CA  LEU A 378      58.628  32.619  18.864  1.00 17.34           C  
-ANISOU 1129  CA  LEU A 378     2407   1790   2390   -255   -558   -228       C  
-ATOM   1130  C   LEU A 378      57.800  33.884  18.670  1.00 18.26           C  
-ANISOU 1130  C   LEU A 378     2672   1489   2778   -468   -398     19       C  
-ATOM   1131  O   LEU A 378      56.708  33.830  18.109  1.00 18.20           O  
-ANISOU 1131  O   LEU A 378     2512   1783   2618   -541   -338     37       O  
-ATOM   1132  CB  LEU A 378      57.985  31.758  19.957  1.00 17.12           C  
-ANISOU 1132  CB  LEU A 378     2446   1651   2409     52   -444    -42       C  
-ATOM   1133  CG  LEU A 378      58.559  30.355  20.163  1.00 15.55           C  
-ANISOU 1133  CG  LEU A 378     2361   1390   2156    136   -299   -343       C  
-ATOM   1134  CD1 LEU A 378      57.875  29.649  21.318  1.00 15.19           C  
-ANISOU 1134  CD1 LEU A 378     1866   1587   2317   -140    -13   -155       C  
-ATOM   1135  CD2 LEU A 378      58.429  29.542  18.887  1.00 18.75           C  
-ANISOU 1135  CD2 LEU A 378     2935   1589   2598     12   -185   -357       C  
-ATOM   1136  N   ASP A 379      58.310  35.022  19.133  1.00 21.55           N  
-ANISOU 1136  N   ASP A 379     2898   1774   3517   -436   -864   -153       N  
-ATOM   1137  CA  ASP A 379      57.517  36.247  19.138  1.00 22.05           C  
-ANISOU 1137  CA  ASP A 379     3136   1707   3535   -556   -842   -315       C  
-ATOM   1138  C   ASP A 379      56.980  36.642  17.769  1.00 20.21           C  
-ANISOU 1138  C   ASP A 379     2816   1639   3225   -316   -407   -540       C  
-ATOM   1139  O   ASP A 379      55.831  37.083  17.652  1.00 19.58           O  
-ANISOU 1139  O   ASP A 379     2641   1758   3038   -250    144   -259       O  
-ATOM   1140  CB  ASP A 379      58.300  37.409  19.750  1.00 25.15           C  
-ANISOU 1140  CB  ASP A 379     3769   1971   3816   -676  -1445   -321       C  
-ATOM   1141  CG  ASP A 379      58.343  37.340  21.259  1.00 31.71           C  
-ANISOU 1141  CG  ASP A 379     4467   2896   4686   -778  -1455   -122       C  
-ATOM   1142  OD1 ASP A 379      57.368  36.833  21.855  1.00 31.92           O  
-ANISOU 1142  OD1 ASP A 379     4727   2889   4511   -802  -1506    -73       O  
-ATOM   1143  OD2 ASP A 379      59.346  37.787  21.848  1.00 36.34           O  
-ANISOU 1143  OD2 ASP A 379     4774   3721   5310   -598  -1411    173       O  
-ATOM   1144  N   GLN A 380      57.805  36.494  16.736  1.00 19.44           N  
-ANISOU 1144  N   GLN A 380     2696   1288   3403   -270    -87    -38       N  
-ATOM   1145  CA  GLN A 380      57.405  36.933  15.405  1.00 20.13           C  
-ANISOU 1145  CA  GLN A 380     2655   1432   3559      8    299    314       C  
-ATOM   1146  C   GLN A 380      56.254  36.088  14.881  1.00 17.10           C  
-ANISOU 1146  C   GLN A 380     2401   1210   2885     99    154    157       C  
-ATOM   1147  O   GLN A 380      55.599  36.460  13.904  1.00 20.44           O  
-ANISOU 1147  O   GLN A 380     2702   1694   3370    341      2    312       O  
-ATOM   1148  CB  GLN A 380      58.578  36.886  14.421  1.00 23.51           C  
-ANISOU 1148  CB  GLN A 380     2700   1781   4450    280    505    472       C  
-ATOM   1149  CG  GLN A 380      59.046  35.484  14.059  1.00 25.26           C  
-ANISOU 1149  CG  GLN A 380     2759   2258   4581    366    725    403       C  
-ATOM   1150  CD  GLN A 380      59.749  35.440  12.708  1.00 28.91           C  
-ANISOU 1150  CD  GLN A 380     3115   3217   4650    681    471    572       C  
-ATOM   1151  OE1 GLN A 380      59.211  35.903  11.699  1.00 31.41           O  
-ANISOU 1151  OE1 GLN A 380     3436   3608   4888    667    536    137       O  
-ATOM   1152  NE2 GLN A 380      60.955  34.889  12.686  1.00 29.89           N  
-ANISOU 1152  NE2 GLN A 380     3054   3654   4647    405    394    604       N  
-ATOM   1153  N   PHE A 381      56.013  34.950  15.531  1.00 14.71           N  
-ANISOU 1153  N   PHE A 381     2101   1117   2370     66    197   -118       N  
-ATOM   1154  CA  PHE A 381      54.981  34.021  15.072  1.00 14.37           C  
-ANISOU 1154  CA  PHE A 381     1971    904   2584    305     87   -131       C  
-ATOM   1155  C   PHE A 381      53.688  34.083  15.872  1.00 13.36           C  
-ANISOU 1155  C   PHE A 381     2054   1248   1774    534     76     27       C  
-ATOM   1156  O   PHE A 381      52.705  33.431  15.520  1.00 14.43           O  
-ANISOU 1156  O   PHE A 381     2071   1250   2161    441   -167   -225       O  
-ATOM   1157  CB  PHE A 381      55.516  32.584  15.067  1.00 14.34           C  
-ANISOU 1157  CB  PHE A 381     1945   1154   2349    619     47   -135       C  
-ATOM   1158  CG  PHE A 381      56.693  32.390  14.163  1.00 14.71           C  
-ANISOU 1158  CG  PHE A 381     1891   1343   2353    386   -186   -328       C  
-ATOM   1159  CD1 PHE A 381      56.530  32.419  12.786  1.00 15.74           C  
-ANISOU 1159  CD1 PHE A 381     2021   1556   2402    417     30   -353       C  
-ATOM   1160  CD2 PHE A 381      57.960  32.190  14.683  1.00 15.80           C  
-ANISOU 1160  CD2 PHE A 381     1914   1567   2522    383    -28   -293       C  
-ATOM   1161  CE1 PHE A 381      57.603  32.249  11.936  1.00 14.92           C  
-ANISOU 1161  CE1 PHE A 381     1700   1613   2355    151   -203   -301       C  
-ATOM   1162  CE2 PHE A 381      59.048  32.016  13.839  1.00 15.44           C  
-ANISOU 1162  CE2 PHE A 381     1700   1557   2609    189   -110   -626       C  
-ATOM   1163  CZ  PHE A 381      58.871  32.047  12.467  1.00 16.51           C  
-ANISOU 1163  CZ  PHE A 381     1952   1817   2502    236    -29   -489       C  
-ATOM   1164  N   VAL A 382      53.676  34.864  16.944  1.00 13.75           N  
-ANISOU 1164  N   VAL A 382     2148   1301   1773    303     35   -226       N  
-ATOM   1165  CA  VAL A 382      52.466  34.982  17.745  1.00 13.29           C  
-ANISOU 1165  CA  VAL A 382     2103   1365   1579    245   -126   -444       C  
-ATOM   1166  C   VAL A 382      51.350  35.566  16.886  1.00 13.90           C  
-ANISOU 1166  C   VAL A 382     2185   1146   1949    395   -137   -260       C  
-ATOM   1167  O   VAL A 382      51.517  36.608  16.252  1.00 16.41           O  
-ANISOU 1167  O   VAL A 382     2467   1262   2507    361     -3     10       O  
-ATOM   1168  CB  VAL A 382      52.687  35.824  19.016  1.00 14.19           C  
-ANISOU 1168  CB  VAL A 382     2067   1411   1911    228   -126   -353       C  
-ATOM   1169  CG1 VAL A 382      51.364  36.098  19.710  1.00 16.20           C  
-ANISOU 1169  CG1 VAL A 382     2130   1774   2249    475    279   -638       C  
-ATOM   1170  CG2 VAL A 382      53.649  35.100  19.954  1.00 16.74           C  
-ANISOU 1170  CG2 VAL A 382     2405   1954   2001    369   -488   -388       C  
-ATOM   1171  N   GLY A 383      50.223  34.863  16.856  1.00 12.97           N  
-ANISOU 1171  N   GLY A 383     1923   1303   1702    389    -74   -507       N  
-ATOM   1172  CA  GLY A 383      49.090  35.255  16.041  1.00 13.12           C  
-ANISOU 1172  CA  GLY A 383     1877   1369   1739    572   -302   -390       C  
-ATOM   1173  C   GLY A 383      49.091  34.643  14.653  1.00 13.81           C  
-ANISOU 1173  C   GLY A 383     2045   1462   1740    672   -157     23       C  
-ATOM   1174  O   GLY A 383      48.124  34.806  13.914  1.00 16.35           O  
-ANISOU 1174  O   GLY A 383     2390   1893   1930    907   -399   -226       O  
-ATOM   1175  N   LYS A 384      50.166  33.937  14.299  1.00 12.39           N  
-ANISOU 1175  N   LYS A 384     1902    953   1852    384   -138   -101       N  
-ATOM   1176  CA  LYS A 384      50.302  33.374  12.958  1.00 13.42           C  
-ANISOU 1176  CA  LYS A 384     2076   1201   1822    449    -76   -287       C  
-ATOM   1177  C   LYS A 384      49.958  31.889  12.928  1.00 11.06           C  
-ANISOU 1177  C   LYS A 384     1728   1007   1466    555   -104    113       C  
-ATOM   1178  O   LYS A 384      50.252  31.157  13.874  1.00 11.60           O  
-ANISOU 1178  O   LYS A 384     1698   1156   1553    273   -106     11       O  
-ATOM   1179  CB  LYS A 384      51.730  33.537  12.431  1.00 14.87           C  
-ANISOU 1179  CB  LYS A 384     2379   1400   1870     46     -7   -321       C  
-ATOM   1180  CG  LYS A 384      52.314  34.931  12.558  1.00 19.37           C  
-ANISOU 1180  CG  LYS A 384     3170   1450   2739     -7   -334   -658       C  
-ATOM   1181  CD  LYS A 384      51.602  35.924  11.689  1.00 20.40           C  
-ANISOU 1181  CD  LYS A 384     3734   1245   2770    -25   -277   -354       C  
-ATOM   1182  CE  LYS A 384      52.393  37.236  11.635  1.00 22.18           C  
-ANISOU 1182  CE  LYS A 384     4214   1446   2768     36   -244   -266       C  
-ATOM   1183  NZ  LYS A 384      51.619  38.338  11.017  1.00 26.79           N  
-ANISOU 1183  NZ  LYS A 384     4522   1882   3775    245    -65   -219       N  
-ATOM   1184  N   GLU A 385      49.348  31.454  11.830  1.00 11.21           N  
-ANISOU 1184  N   GLU A 385     1543   1061   1656    349     60   -323       N  
-ATOM   1185  CA  GLU A 385      49.065  30.039  11.631  1.00 10.49           C  
-ANISOU 1185  CA  GLU A 385     1423    965   1598    417    -39   -341       C  
-ATOM   1186  C   GLU A 385      50.278  29.341  11.041  1.00 10.33           C  
-ANISOU 1186  C   GLU A 385     1276   1065   1583    455     11   -166       C  
-ATOM   1187  O   GLU A 385      50.888  29.819  10.081  1.00 10.64           O  
-ANISOU 1187  O   GLU A 385     1278   1017   1748    385    193    -21       O  
-ATOM   1188  CB  GLU A 385      47.858  29.822  10.721  1.00 12.37           C  
-ANISOU 1188  CB  GLU A 385     1603   1138   1957    337   -196   -302       C  
-ATOM   1189  CG  GLU A 385      47.299  28.412  10.839  1.00 16.00           C  
-ANISOU 1189  CG  GLU A 385     1834   1104   3142    279   -345   -435       C  
-ATOM   1190  CD  GLU A 385      46.205  28.102   9.848  1.00 20.65           C  
-ANISOU 1190  CD  GLU A 385     2042   1785   4018    643    -95   -540       C  
-ATOM   1191  OE1 GLU A 385      46.093  28.814   8.833  1.00 21.96           O  
-ANISOU 1191  OE1 GLU A 385     2321   2623   3400    243   -225   -682       O  
-ATOM   1192  OE2 GLU A 385      45.458  27.126  10.085  1.00 23.54           O  
-ANISOU 1192  OE2 GLU A 385     2026   1780   5136    404   -239   -864       O  
-ATOM   1193  N   VAL A 386      50.631  28.211  11.640  1.00  9.80           N  
-ANISOU 1193  N   VAL A 386     1222    887   1615    538   -125    -16       N  
-ATOM   1194  CA  VAL A 386      51.784  27.438  11.182  1.00  9.95           C  
-ANISOU 1194  CA  VAL A 386     1197    863   1718    371   -326      8       C  
-ATOM   1195  C   VAL A 386      51.426  25.971  11.005  1.00  8.35           C  
-ANISOU 1195  C   VAL A 386     1210    615   1347    114    168     73       C  
-ATOM   1196  O   VAL A 386      50.461  25.480  11.591  1.00  9.87           O  
-ANISOU 1196  O   VAL A 386     1270    886   1595    132    220      5       O  
-ATOM   1197  CB  VAL A 386      52.988  27.556  12.166  1.00 10.18           C  
-ANISOU 1197  CB  VAL A 386     1365    892   1609    164   -287     19       C  
-ATOM   1198  CG1 VAL A 386      53.426  29.016  12.331  1.00 11.43           C  
-ANISOU 1198  CG1 VAL A 386     1579    684   2081     81   -143   -221       C  
-ATOM   1199  CG2 VAL A 386      52.669  26.921  13.529  1.00 11.15           C  
-ANISOU 1199  CG2 VAL A 386     1602   1105   1530    193     -1    -24       C  
-ATOM   1200  N   VAL A 387      52.206  25.285  10.175  1.00  8.93           N  
-ANISOU 1200  N   VAL A 387     1171    573   1650    206    -24    -50       N  
-ATOM   1201  CA  VAL A 387      52.210  23.830  10.163  1.00  9.01           C  
-ANISOU 1201  CA  VAL A 387     1155    725   1541    166   -358   -116       C  
-ATOM   1202  C   VAL A 387      53.537  23.352  10.736  1.00  8.80           C  
-ANISOU 1202  C   VAL A 387     1020    804   1519    134   -139   -132       C  
-ATOM   1203  O   VAL A 387      54.602  23.928  10.453  1.00 10.22           O  
-ANISOU 1203  O   VAL A 387     1128    955   1801    150   -207     44       O  
-ATOM   1204  CB  VAL A 387      51.954  23.258   8.755  1.00 10.05           C  
-ANISOU 1204  CB  VAL A 387     1410    788   1621    237   -277   -216       C  
-ATOM   1205  CG1 VAL A 387      50.519  23.513   8.336  1.00 12.31           C  
-ANISOU 1205  CG1 VAL A 387     1352   1393   1931    436   -618   -512       C  
-ATOM   1206  CG2 VAL A 387      52.908  23.832   7.744  1.00 15.75           C  
-ANISOU 1206  CG2 VAL A 387     1738   1450   2795     81    245    143       C  
-ATOM   1207  N   LEU A 388      53.459  22.334  11.587  1.00  9.63           N  
-ANISOU 1207  N   LEU A 388     1159    915   1586    511   -267   -132       N  
-ATOM   1208  CA  LEU A 388      54.626  21.813  12.287  1.00  9.16           C  
-ANISOU 1208  CA  LEU A 388     1170    799   1509    334    -84    -94       C  
-ATOM   1209  C   LEU A 388      54.858  20.371  11.879  1.00  9.08           C  
-ANISOU 1209  C   LEU A 388     1121    755   1575    253   -132   -122       C  
-ATOM   1210  O   LEU A 388      53.909  19.617  11.650  1.00 11.37           O  
-ANISOU 1210  O   LEU A 388     1097    961   2261     45     56   -265       O  
-ATOM   1211  CB  LEU A 388      54.420  21.893  13.800  1.00 10.11           C  
-ANISOU 1211  CB  LEU A 388     1399   1024   1417    374     19   -148       C  
-ATOM   1212  CG  LEU A 388      54.053  23.271  14.374  1.00 10.01           C  
-ANISOU 1212  CG  LEU A 388     1392    775   1634    268   -148   -366       C  
-ATOM   1213  CD1 LEU A 388      52.561  23.335  14.698  1.00 11.39           C  
-ANISOU 1213  CD1 LEU A 388     1351    958   2019    223     63      0       C  
-ATOM   1214  CD2 LEU A 388      54.875  23.534  15.616  1.00 12.62           C  
-ANISOU 1214  CD2 LEU A 388     1777   1198   1818    284   -481   -226       C  
-ATOM   1215  N   GLU A 389      56.129  19.995  11.778  1.00  9.28           N  
-ANISOU 1215  N   GLU A 389     1319    657   1551    402   -106   -130       N  
-ATOM   1216  CA  GLU A 389      56.491  18.620  11.468  1.00 11.87           C  
-ANISOU 1216  CA  GLU A 389     1833   1185   1490    559   -500   -285       C  
-ATOM   1217  C   GLU A 389      57.489  18.110  12.496  1.00  9.67           C  
-ANISOU 1217  C   GLU A 389     1199    924   1550    308   -362   -131       C  
-ATOM   1218  O   GLU A 389      58.328  18.859  12.996  1.00  9.83           O  
-ANISOU 1218  O   GLU A 389     1082    867   1785    135   -325   -141       O  
-ATOM   1219  CB  GLU A 389      57.080  18.502  10.068  1.00 15.81           C  
-ANISOU 1219  CB  GLU A 389     2578   1761   1666   1154   -475   -407       C  
-ATOM   1220  CG  GLU A 389      57.189  17.046   9.631  1.00 23.38           C  
-ANISOU 1220  CG  GLU A 389     3296   2509   3077   1107     15   -377       C  
-ATOM   1221  CD  GLU A 389      58.121  16.838   8.464  1.00 26.06           C  
-ANISOU 1221  CD  GLU A 389     3564   2791   3547    691    677   -144       C  
-ATOM   1222  OE1 GLU A 389      58.378  15.655   8.134  1.00 25.93           O  
-ANISOU 1222  OE1 GLU A 389     3672   3161   3019   1239    791   -308       O  
-ATOM   1223  OE2 GLU A 389      58.586  17.845   7.879  1.00 25.43           O  
-ANISOU 1223  OE2 GLU A 389     3346   2691   3626   -245    763     76       O  
-ATOM   1224  N   LEU A 390      57.393  16.827  12.811  1.00 10.05           N  
-ANISOU 1224  N   LEU A 390     1249    720   1848    246   -420    103       N  
-ATOM   1225  CA  LEU A 390      58.279  16.213  13.785  1.00  9.87           C  
-ANISOU 1225  CA  LEU A 390     1259    958   1534    356   -157    142       C  
-ATOM   1226  C   LEU A 390      59.656  15.956  13.180  1.00  9.38           C  
-ANISOU 1226  C   LEU A 390     1067   1053   1444     69   -242   -260       C  
-ATOM   1227  O   LEU A 390      59.819  15.083  12.331  1.00 14.52           O  
-ANISOU 1227  O   LEU A 390     1648   1692   2175    -71     24   -960       O  
-ATOM   1228  CB  LEU A 390      57.664  14.905  14.287  1.00 10.37           C  
-ANISOU 1228  CB  LEU A 390     1500    677   1762    174   -380    244       C  
-ATOM   1229  CG  LEU A 390      58.458  14.221  15.401  1.00 10.26           C  
-ANISOU 1229  CG  LEU A 390     1576    621   1700    227   -399   -166       C  
-ATOM   1230  CD1 LEU A 390      58.536  15.109  16.645  1.00 11.78           C  
-ANISOU 1230  CD1 LEU A 390     1782    844   1848    182   -285   -528       C  
-ATOM   1231  CD2 LEU A 390      57.830  12.872  15.735  1.00 11.48           C  
-ANISOU 1231  CD2 LEU A 390     1598    634   2130    -42   -355   -118       C  
-ATOM   1232  N   THR A 391      60.655  16.711  13.622  1.00  9.43           N  
-ANISOU 1232  N   THR A 391      779   1133   1671    231   -228   -184       N  
-ATOM   1233  CA  THR A 391      62.010  16.561  13.085  1.00 10.06           C  
-ANISOU 1233  CA  THR A 391      952    924   1946     51   -117   -100       C  
-ATOM   1234  C   THR A 391      62.796  15.490  13.832  1.00 10.02           C  
-ANISOU 1234  C   THR A 391     1189    986   1633    267   -297   -156       C  
-ATOM   1235  O   THR A 391      63.453  14.642  13.219  1.00 10.48           O  
-ANISOU 1235  O   THR A 391     1182    978   1821    180   -289   -345       O  
-ATOM   1236  CB  THR A 391      62.769  17.893  13.124  1.00 10.16           C  
-ANISOU 1236  CB  THR A 391      958   1020   1883      7     16    137       C  
-ATOM   1237  OG1 THR A 391      62.022  18.851  12.367  1.00 13.27           O  
-ANISOU 1237  OG1 THR A 391     1489   1029   2522    488   -193     83       O  
-ATOM   1238  CG2 THR A 391      64.167  17.763  12.526  1.00 12.13           C  
-ANISOU 1238  CG2 THR A 391     1157   1271   2179    -37    135   -228       C  
-ATOM   1239  N   TRP A 392      62.736  15.534  15.155  1.00 10.53           N  
-ANISOU 1239  N   TRP A 392     1269   1130   1601    185   -345     63       N  
-ATOM   1240  CA  TRP A 392      63.360  14.506  15.971  1.00  9.33           C  
-ANISOU 1240  CA  TRP A 392     1012   1036   1495     34   -309     89       C  
-ATOM   1241  C   TRP A 392      62.727  14.475  17.365  1.00  9.54           C  
-ANISOU 1241  C   TRP A 392     1373    984   1266     36   -286    -60       C  
-ATOM   1242  O   TRP A 392      61.926  15.355  17.715  1.00 11.44           O  
-ANISOU 1242  O   TRP A 392     1372    999   1974    362    -84   -362       O  
-ATOM   1243  CB  TRP A 392      64.894  14.663  16.017  1.00 11.50           C  
-ANISOU 1243  CB  TRP A 392     1112   1036   2221     40   -228   -399       C  
-ATOM   1244  CG  TRP A 392      65.422  15.918  16.678  1.00 10.00           C  
-ANISOU 1244  CG  TRP A 392      945    925   1929    148   -238    -56       C  
-ATOM   1245  CD1 TRP A 392      65.391  17.193  16.180  1.00 11.92           C  
-ANISOU 1245  CD1 TRP A 392     1048   1212   2268     98   -212   -499       C  
-ATOM   1246  CD2 TRP A 392      66.108  15.993  17.933  1.00 10.85           C  
-ANISOU 1246  CD2 TRP A 392     1073   1131   1919    158   -288   -352       C  
-ATOM   1247  NE1 TRP A 392      65.991  18.062  17.068  1.00 12.54           N  
-ANISOU 1247  NE1 TRP A 392     1141   1346   2277    292   -538   -229       N  
-ATOM   1248  CE2 TRP A 392      66.450  17.347  18.148  1.00 11.86           C  
-ANISOU 1248  CE2 TRP A 392     1159   1367   1980    145   -463   -517       C  
-ATOM   1249  CE3 TRP A 392      66.465  15.045  18.902  1.00 13.05           C  
-ANISOU 1249  CE3 TRP A 392     1342   1598   2016    236   -531    123       C  
-ATOM   1250  CZ2 TRP A 392      67.127  17.779  19.290  1.00 13.14           C  
-ANISOU 1250  CZ2 TRP A 392     1384   1502   2106    114   -389    -96       C  
-ATOM   1251  CZ3 TRP A 392      67.147  15.473  20.029  1.00 12.99           C  
-ANISOU 1251  CZ3 TRP A 392     1399   1551   1986    122   -480    -15       C  
-ATOM   1252  CH2 TRP A 392      67.463  16.831  20.218  1.00 14.79           C  
-ANISOU 1252  CH2 TRP A 392     1674   1532   2414    113   -534   -494       C  
-ATOM   1253  N   VAL A 393      63.064  13.444  18.136  1.00 10.13           N  
-ANISOU 1253  N   VAL A 393     1323   1086   1440    222   -347     58       N  
-ATOM   1254  CA  VAL A 393      62.480  13.203  19.445  1.00 10.93           C  
-ANISOU 1254  CA  VAL A 393     1230   1236   1685    150   -677   -157       C  
-ATOM   1255  C   VAL A 393      63.597  12.896  20.432  1.00 11.96           C  
-ANISOU 1255  C   VAL A 393     1510   1335   1700    284   -269   -332       C  
-ATOM   1256  O   VAL A 393      64.565  12.214  20.086  1.00 12.96           O  
-ANISOU 1256  O   VAL A 393     1368   1406   2150    535   -461   -249       O  
-ATOM   1257  CB  VAL A 393      61.492  12.003  19.402  1.00 11.51           C  
-ANISOU 1257  CB  VAL A 393     1472   1254   1647    204   -440    -99       C  
-ATOM   1258  CG1 VAL A 393      60.928  11.707  20.792  1.00 12.78           C  
-ANISOU 1258  CG1 VAL A 393     1654   1769   1434    319   -152     58       C  
-ATOM   1259  CG2 VAL A 393      60.370  12.264  18.401  1.00 12.36           C  
-ANISOU 1259  CG2 VAL A 393     1343   1577   1774    198   -441   -160       C  
-ATOM   1260  N   SER A 394      63.471  13.417  21.645  1.00 11.89           N  
-ANISOU 1260  N   SER A 394     1548   1379   1591    439   -517   -160       N  
-ATOM   1261  CA  SER A 394      64.376  13.032  22.722  1.00 13.03           C  
-ANISOU 1261  CA  SER A 394     1747   1393   1811    504   -702   -264       C  
-ATOM   1262  C   SER A 394      63.602  12.743  24.008  1.00 12.72           C  
-ANISOU 1262  C   SER A 394     1890   1353   1589    474   -650      3       C  
-ATOM   1263  O   SER A 394      62.408  13.055  24.115  1.00 12.85           O  
-ANISOU 1263  O   SER A 394     1716   1396   1770    532   -544     66       O  
-ATOM   1264  CB  SER A 394      65.433  14.113  22.966  1.00 13.43           C  
-ANISOU 1264  CB  SER A 394     1756   1294   2052    564   -430   -516       C  
-ATOM   1265  OG  SER A 394      64.819  15.319  23.370  1.00 13.77           O  
-ANISOU 1265  OG  SER A 394     1832   1361   2040    258   -515   -168       O  
-ATOM   1266  N   ASN A 395      64.278  12.137  24.979  1.00 13.84           N  
-ANISOU 1266  N   ASN A 395     2038   1481   1739    439   -842    -29       N  
-ATOM   1267  CA  ASN A 395      63.628  11.815  26.242  1.00 14.52           C  
-ANISOU 1267  CA  ASN A 395     2377   1682   1459    565   -846     69       C  
-ATOM   1268  C   ASN A 395      63.333  13.045  27.087  1.00 15.46           C  
-ANISOU 1268  C   ASN A 395     2629   1672   1572    555   -683    -78       C  
-ATOM   1269  O   ASN A 395      64.024  14.066  27.010  1.00 17.41           O  
-ANISOU 1269  O   ASN A 395     2642   1842   2131    406   -597    -49       O  
-ATOM   1270  CB  ASN A 395      64.471  10.829  27.053  1.00 16.85           C  
-ANISOU 1270  CB  ASN A 395     2395   2012   1993    605  -1140    -74       C  
-ATOM   1271  CG  ASN A 395      65.773  11.439  27.537  1.00 19.08           C  
-ANISOU 1271  CG  ASN A 395     2762   2370   2117    939  -1086    -10       C  
-ATOM   1272  OD1 ASN A 395      66.663  11.726  26.740  1.00 21.50           O  
-ANISOU 1272  OD1 ASN A 395     2827   3000   2342    713  -1034    -42       O  
-ATOM   1273  ND2 ASN A 395      65.899  11.620  28.852  1.00 19.99           N  
-ANISOU 1273  ND2 ASN A 395     2877   2308   2411   1095  -1176   -246       N  
-ATOM   1274  N   ARG A 396      62.284  12.936  27.890  1.00 15.95           N  
-ANISOU 1274  N   ARG A 396     2566   1781   1712    441   -703    -19       N  
-ATOM   1275  CA  ARG A 396      62.019  13.887  28.958  1.00 16.32           C  
-ANISOU 1275  CA  ARG A 396     2598   1941   1662    300   -907   -433       C  
-ATOM   1276  C   ARG A 396      63.085  13.715  30.028  1.00 17.50           C  
-ANISOU 1276  C   ARG A 396     2861   1780   2008    400   -888   -622       C  
-ATOM   1277  O   ARG A 396      63.434  12.589  30.381  1.00 18.27           O  
-ANISOU 1277  O   ARG A 396     2944   1834   2162    892   -845   -330       O  
-ATOM   1278  CB  ARG A 396      60.644  13.586  29.551  1.00 19.52           C  
-ANISOU 1278  CB  ARG A 396     2627   2646   2143    753   -521   -990       C  
-ATOM   1279  CG  ARG A 396      60.318  14.323  30.816  1.00 22.39           C  
-ANISOU 1279  CG  ARG A 396     3073   2905   2527    776   -504    -92       C  
-ATOM   1280  CD  ARG A 396      58.989  13.848  31.359  1.00 21.33           C  
-ANISOU 1280  CD  ARG A 396     3116   2804   2184    638   -577    633       C  
-ATOM   1281  NE  ARG A 396      58.599  14.628  32.524  1.00 22.54           N  
-ANISOU 1281  NE  ARG A 396     3662   2632   2268    862   -890    409       N  
-ATOM   1282  CZ  ARG A 396      57.425  14.534  33.133  1.00 24.97           C  
-ANISOU 1282  CZ  ARG A 396     4126   2698   2663   1153   -747    -70       C  
-ATOM   1283  NH1 ARG A 396      56.513  13.682  32.686  1.00 21.80           N  
-ANISOU 1283  NH1 ARG A 396     4194   2393   1697   1169   -564   -172       N  
-ATOM   1284  NH2 ARG A 396      57.165  15.296  34.189  1.00 27.80           N  
-ANISOU 1284  NH2 ARG A 396     4503   2913   3145   1349   -916  -1096       N  
-ATOM   1285  N   THR A 397      63.606  14.824  30.534  1.00 19.24           N  
-ANISOU 1285  N   THR A 397     3041   2192   2075    256  -1235   -488       N  
-ATOM   1286  CA  THR A 397      64.563  14.754  31.629  1.00 22.39           C  
-ANISOU 1286  CA  THR A 397     3301   2634   2570    115  -1381   -904       C  
-ATOM   1287  C   THR A 397      64.029  13.874  32.752  1.00 23.14           C  
-ANISOU 1287  C   THR A 397     3445   2981   2364    530  -1368   -582       C  
-ATOM   1288  O   THR A 397      62.896  14.040  33.197  1.00 23.08           O  
-ANISOU 1288  O   THR A 397     3454   3036   2277    541  -1006   -502       O  
-ATOM   1289  CB  THR A 397      64.876  16.145  32.192  1.00 25.47           C  
-ANISOU 1289  CB  THR A 397     3489   3111   3077   -414  -1489   -941       C  
-ATOM   1290  OG1 THR A 397      65.452  16.955  31.161  1.00 28.78           O  
-ANISOU 1290  OG1 THR A 397     3881   3129   3924   -236  -1326   -816       O  
-ATOM   1291  CG2 THR A 397      65.856  16.039  33.359  1.00 27.17           C  
-ANISOU 1291  CG2 THR A 397     3661   3174   3489   -235  -1709   -815       C  
-ATOM   1292  N   GLY A 398      64.854  12.935  33.207  1.00 24.83           N  
-ANISOU 1292  N   GLY A 398     3613   3230   2589    652  -1449   -394       N  
-ATOM   1293  CA  GLY A 398      64.473  12.053  34.295  1.00 24.74           C  
-ANISOU 1293  CA  GLY A 398     3736   3212   2450    589  -1216   -178       C  
-ATOM   1294  C   GLY A 398      63.747  10.796  33.852  1.00 24.45           C  
-ANISOU 1294  C   GLY A 398     3939   3109   2243    687  -1187     55       C  
-ATOM   1295  O   GLY A 398      63.417   9.950  34.680  1.00 28.35           O  
-ANISOU 1295  O   GLY A 398     4516   3473   2781    602   -865    537       O  
-ATOM   1296  N   ALA A 399      63.496  10.670  32.552  1.00 22.38           N  
-ANISOU 1296  N   ALA A 399     3531   2740   2231    742  -1136   -278       N  
-ATOM   1297  CA  ALA A 399      62.785   9.511  32.027  1.00 21.97           C  
-ANISOU 1297  CA  ALA A 399     3375   2597   2375    852   -853    305       C  
-ATOM   1298  C   ALA A 399      63.529   8.898  30.851  1.00 21.43           C  
-ANISOU 1298  C   ALA A 399     3356   2183   2601    891   -915   -188       C  
-ATOM   1299  O   ALA A 399      64.360   9.552  30.222  1.00 23.84           O  
-ANISOU 1299  O   ALA A 399     3632   2039   3385   1053   -745    326       O  
-ATOM   1300  CB  ALA A 399      61.372   9.906  31.602  1.00 22.33           C  
-ANISOU 1300  CB  ALA A 399     3243   2766   2473    905   -601    112       C  
-ATOM   1301  N   THR A 400      63.232   7.637  30.551  1.00 21.21           N  
-ANISOU 1301  N   THR A 400     3365   2449   2244   1134  -1084   -220       N  
-ATOM   1302  CA  THR A 400      63.731   7.032  29.321  1.00 21.51           C  
-ANISOU 1302  CA  THR A 400     3304   2288   2582   1018  -1196     10       C  
-ATOM   1303  C   THR A 400      62.740   7.326  28.200  1.00 19.30           C  
-ANISOU 1303  C   THR A 400     2719   2148   2464    697   -999     21       C  
-ATOM   1304  O   THR A 400      61.570   7.628  28.456  1.00 19.38           O  
-ANISOU 1304  O   THR A 400     2719   2111   2532    622   -951   -231       O  
-ATOM   1305  CB  THR A 400      63.902   5.517  29.455  1.00 27.49           C  
-ANISOU 1305  CB  THR A 400     3941   2678   3824   1088  -1189    405       C  
-ATOM   1306  OG1 THR A 400      62.636   4.916  29.752  1.00 28.93           O  
-ANISOU 1306  OG1 THR A 400     4310   2519   4161    814   -893    267       O  
-ATOM   1307  CG2 THR A 400      64.884   5.197  30.567  1.00 29.73           C  
-ANISOU 1307  CG2 THR A 400     4176   3068   4050   1564  -1128    624       C  
-ATOM   1308  N   LEU A 401      63.212   7.253  26.962  1.00 17.86           N  
-ANISOU 1308  N   LEU A 401     2542   1960   2284    636  -1077    -67       N  
-ATOM   1309  CA  LEU A 401      62.332   7.424  25.814  1.00 17.09           C  
-ANISOU 1309  CA  LEU A 401     2513   1745   2234    441   -750   -325       C  
-ATOM   1310  C   LEU A 401      61.563   6.134  25.573  1.00 17.21           C  
-ANISOU 1310  C   LEU A 401     2560   1551   2426    548   -438   -352       C  
-ATOM   1311  O   LEU A 401      62.154   5.093  25.263  1.00 22.38           O  
-ANISOU 1311  O   LEU A 401     2763   1733   4005    630   -283   -616       O  
-ATOM   1312  CB  LEU A 401      63.130   7.825  24.573  1.00 16.86           C  
-ANISOU 1312  CB  LEU A 401     2445   1869   2091    603   -647   -212       C  
-ATOM   1313  CG  LEU A 401      62.318   8.068  23.297  1.00 15.97           C  
-ANISOU 1313  CG  LEU A 401     2300   1897   1870    519   -399   -194       C  
-ATOM   1314  CD1 LEU A 401      61.249   9.149  23.507  1.00 16.24           C  
-ANISOU 1314  CD1 LEU A 401     2278   1624   2267    787   -301   -315       C  
-ATOM   1315  CD2 LEU A 401      63.242   8.444  22.148  1.00 17.54           C  
-ANISOU 1315  CD2 LEU A 401     2269   2343   2050    360   -292   -377       C  
-ATOM   1316  N   ASN A 402      60.249   6.200  25.746  1.00 14.70           N  
-ANISOU 1316  N   ASN A 402     2449   1286   1848    170   -498    146       N  
-ATOM   1317  CA  ASN A 402      59.386   5.028  25.633  1.00 15.02           C  
-ANISOU 1317  CA  ASN A 402     2367   1606   1735    177   -604    125       C  
-ATOM   1318  C   ASN A 402      58.469   5.162  24.424  1.00 13.59           C  
-ANISOU 1318  C   ASN A 402     2165   1398   1600    190   -499    -80       C  
-ATOM   1319  O   ASN A 402      57.494   5.920  24.447  1.00 14.85           O  
-ANISOU 1319  O   ASN A 402     2464   1424   1753    668   -237     90       O  
-ATOM   1320  CB  ASN A 402      58.567   4.864  26.918  1.00 16.50           C  
-ANISOU 1320  CB  ASN A 402     2569   1923   1778    242   -422     70       C  
-ATOM   1321  CG  ASN A 402      57.592   3.705  26.854  1.00 17.11           C  
-ANISOU 1321  CG  ASN A 402     2915   1856   1729    262   -287    338       C  
-ATOM   1322  OD1 ASN A 402      57.583   2.933  25.899  1.00 16.75           O  
-ANISOU 1322  OD1 ASN A 402     2950   1630   1782    208   -441    119       O  
-ATOM   1323  ND2 ASN A 402      56.765   3.574  27.888  1.00 19.96           N  
-ANISOU 1323  ND2 ASN A 402     3089   2109   2387    141    -65    326       N  
-ATOM   1324  N   LEU A 403      58.794   4.431  23.362  1.00 13.12           N  
-ANISOU 1324  N   LEU A 403     2085   1374   1526    134   -427    -48       N  
-ATOM   1325  CA  LEU A 403      58.052   4.530  22.110  1.00 13.79           C  
-ANISOU 1325  CA  LEU A 403     2035   1401   1801    180    -86   -137       C  
-ATOM   1326  C   LEU A 403      56.690   3.829  22.149  1.00 12.78           C  
-ANISOU 1326  C   LEU A 403     2000   1222   1633    259   -130    120       C  
-ATOM   1327  O   LEU A 403      55.944   3.860  21.163  1.00 13.13           O  
-ANISOU 1327  O   LEU A 403     2019   1396   1573    252   -237    -96       O  
-ATOM   1328  CB  LEU A 403      58.903   4.025  20.942  1.00 14.73           C  
-ANISOU 1328  CB  LEU A 403     1940   1691   1965     61    251   -311       C  
-ATOM   1329  CG  LEU A 403      60.245   4.742  20.770  1.00 15.24           C  
-ANISOU 1329  CG  LEU A 403     1845   1688   2257    -73     92   -497       C  
-ATOM   1330  CD1 LEU A 403      60.929   4.260  19.495  1.00 17.91           C  
-ANISOU 1330  CD1 LEU A 403     2013   2154   2636   -165    278   -687       C  
-ATOM   1331  CD2 LEU A 403      60.063   6.258  20.744  1.00 15.12           C  
-ANISOU 1331  CD2 LEU A 403     1928   1887   1930    -82   -163   -409       C  
-ATOM   1332  N   TRP A 404      56.375   3.216  23.289  1.00 13.15           N  
-ANISOU 1332  N   TRP A 404     2146   1155   1694    166   -117     81       N  
-ATOM   1333  CA  TRP A 404      55.076   2.586  23.527  1.00 13.31           C  
-ANISOU 1333  CA  TRP A 404     2408    861   1787    229   -105    257       C  
-ATOM   1334  C   TRP A 404      54.181   3.411  24.465  1.00 12.68           C  
-ANISOU 1334  C   TRP A 404     2383    748   1687      9   -258    -46       C  
-ATOM   1335  O   TRP A 404      53.027   3.051  24.702  1.00 14.82           O  
-ANISOU 1335  O   TRP A 404     2352   1238   2040    -38     11     -1       O  
-ATOM   1336  CB  TRP A 404      55.263   1.179  24.108  1.00 15.89           C  
-ANISOU 1336  CB  TRP A 404     2856   1025   2157    591    -30    265       C  
-ATOM   1337  CG  TRP A 404      55.450   0.086  23.072  1.00 19.83           C  
-ANISOU 1337  CG  TRP A 404     2956   1649   2930    332   -447    342       C  
-ATOM   1338  CD1 TRP A 404      54.505  -0.796  22.622  1.00 18.71           C  
-ANISOU 1338  CD1 TRP A 404     2882   1732   2496    588   -483    288       C  
-ATOM   1339  CD2 TRP A 404      56.661  -0.239  22.380  1.00 17.97           C  
-ANISOU 1339  CD2 TRP A 404     2643   1499   2685      3   -705    239       C  
-ATOM   1340  NE1 TRP A 404      55.055  -1.647  21.692  1.00 20.03           N  
-ANISOU 1340  NE1 TRP A 404     2570   2049   2992    180   -487   1001       N  
-ATOM   1341  CE2 TRP A 404      56.375  -1.326  21.524  1.00 21.78           C  
-ANISOU 1341  CE2 TRP A 404     2852   2262   3160    594   -216   1010       C  
-ATOM   1342  CE3 TRP A 404      57.961   0.280  22.402  1.00 20.15           C  
-ANISOU 1342  CE3 TRP A 404     2413   1782   3460   -127   -371    986       C  
-ATOM   1343  CZ2 TRP A 404      57.338  -1.901  20.700  1.00 17.99           C  
-ANISOU 1343  CZ2 TRP A 404     2691   1992   2150   1005     -6    766       C  
-ATOM   1344  CZ3 TRP A 404      58.909  -0.285  21.580  1.00 20.88           C  
-ANISOU 1344  CZ3 TRP A 404     2785   1711   3438    574   -638    148       C  
-ATOM   1345  CH2 TRP A 404      58.593  -1.368  20.737  1.00 20.31           C  
-ANISOU 1345  CH2 TRP A 404     2938   2008   2772    952   -238     78       C  
-ATOM   1346  N   ALA A 405      54.702   4.516  24.999  1.00 13.20           N  
-ANISOU 1346  N   ALA A 405     2371    933   1709    400   -226     46       N  
-ATOM   1347  CA  ALA A 405      53.887   5.384  25.847  1.00 12.84           C  
-ANISOU 1347  CA  ALA A 405     2242    925   1710    256   -152   -101       C  
-ATOM   1348  C   ALA A 405      52.758   6.008  25.046  1.00 13.38           C  
-ANISOU 1348  C   ALA A 405     2171   1158   1753    285    -97    173       C  
-ATOM   1349  O   ALA A 405      52.959   6.434  23.909  1.00 14.01           O  
-ANISOU 1349  O   ALA A 405     1993   1313   2017    307    -21    235       O  
-ATOM   1350  CB  ALA A 405      54.737   6.477  26.477  1.00 14.70           C  
-ANISOU 1350  CB  ALA A 405     2279   1120   2187    243   -322   -303       C  
-ATOM   1351  N   VAL A 406      51.573   6.065  25.645  1.00 13.18           N  
-ANISOU 1351  N   VAL A 406     1910   1152   1946    316    -10   -105       N  
-ATOM   1352  CA  VAL A 406      50.436   6.731  25.025  1.00 12.92           C  
-ANISOU 1352  CA  VAL A 406     1883   1184   1841    278    221    -47       C  
-ATOM   1353  C   VAL A 406      50.375   8.164  25.538  1.00 13.15           C  
-ANISOU 1353  C   VAL A 406     1984   1196   1817    299     82    160       C  
-ATOM   1354  O   VAL A 406      50.349   8.389  26.747  1.00 14.71           O  
-ANISOU 1354  O   VAL A 406     2268   1467   1854    523     -9     94       O  
-ATOM   1355  CB  VAL A 406      49.111   6.014  25.355  1.00 14.24           C  
-ANISOU 1355  CB  VAL A 406     2104   1134   2170    295    167   -132       C  
-ATOM   1356  CG1 VAL A 406      47.956   6.696  24.644  1.00 16.07           C  
-ANISOU 1356  CG1 VAL A 406     2078   1433   2594    275    142    -94       C  
-ATOM   1357  CG2 VAL A 406      49.178   4.551  24.956  1.00 15.34           C  
-ANISOU 1357  CG2 VAL A 406     2299   1247   2280    254    263   -115       C  
-ATOM   1358  N   PRO A 407      50.367   9.146  24.621  1.00 12.18           N  
-ANISOU 1358  N   PRO A 407     1846   1236   1545    156   -154   -142       N  
-ATOM   1359  CA  PRO A 407      50.286  10.540  25.084  1.00 11.03           C  
-ANISOU 1359  CA  PRO A 407     1726   1044   1422    215     77    -87       C  
-ATOM   1360  C   PRO A 407      49.033  10.767  25.927  1.00 12.01           C  
-ANISOU 1360  C   PRO A 407     1939   1096   1528    265   -135   -187       C  
-ATOM   1361  O   PRO A 407      47.981  10.199  25.629  1.00 13.11           O  
-ANISOU 1361  O   PRO A 407     1846   1347   1789    219    107   -147       O  
-ATOM   1362  CB  PRO A 407      50.204  11.343  23.775  1.00 11.61           C  
-ANISOU 1362  CB  PRO A 407     1845   1193   1374    282     41    208       C  
-ATOM   1363  CG  PRO A 407      50.829  10.436  22.739  1.00 11.65           C  
-ANISOU 1363  CG  PRO A 407     1598   1265   1561    411    116   -376       C  
-ATOM   1364  CD  PRO A 407      50.420   9.046  23.153  1.00 10.91           C  
-ANISOU 1364  CD  PRO A 407     1740    875   1529     65   -127    -35       C  
-ATOM   1365  N   ASN A 408      49.144  11.601  26.959  1.00 12.40           N  
-ANISOU 1365  N   ASN A 408     2078   1123   1508    469    147   -141       N  
-ATOM   1366  CA  ASN A 408      47.994  11.968  27.780  1.00 13.25           C  
-ANISOU 1366  CA  ASN A 408     2080   1549   1406    358    -48    -58       C  
-ATOM   1367  C   ASN A 408      47.217  13.110  27.121  1.00 12.24           C  
-ANISOU 1367  C   ASN A 408     1978   1269   1403    291    197     -6       C  
-ATOM   1368  O   ASN A 408      47.264  14.260  27.566  1.00 13.36           O  
-ANISOU 1368  O   ASN A 408     2021   1401   1654    252    146   -221       O  
-ATOM   1369  CB  ASN A 408      48.457  12.356  29.183  1.00 15.03           C  
-ANISOU 1369  CB  ASN A 408     2406   2097   1208    411   -142   -282       C  
-ATOM   1370  CG  ASN A 408      47.317  12.464  30.159  1.00 21.54           C  
-ANISOU 1370  CG  ASN A 408     3005   2879   2298    401   -350   -482       C  
-ATOM   1371  OD1 ASN A 408      46.331  11.740  30.056  1.00 25.64           O  
-ANISOU 1371  OD1 ASN A 408     3291   3151   3298    272    -54   -486       O  
-ATOM   1372  ND2 ASN A 408      47.441  13.375  31.118  1.00 26.89           N  
-ANISOU 1372  ND2 ASN A 408     3365   3416   3437    589   -370   -775       N  
-ATOM   1373  N   TYR A 409      46.496  12.782  26.052  1.00 12.55           N  
-ANISOU 1373  N   TYR A 409     1842   1389   1537    282      7     -3       N  
-ATOM   1374  CA  TYR A 409      45.885  13.791  25.187  1.00 12.65           C  
-ANISOU 1374  CA  TYR A 409     1824   1628   1352    403    108   -145       C  
-ATOM   1375  C   TYR A 409      44.909  14.735  25.883  1.00 12.15           C  
-ANISOU 1375  C   TYR A 409     1733   1645   1239    431    223    102       C  
-ATOM   1376  O   TYR A 409      44.799  15.902  25.508  1.00 12.58           O  
-ANISOU 1376  O   TYR A 409     1850   1481   1448    391     19    178       O  
-ATOM   1377  CB  TYR A 409      45.141  13.119  24.038  1.00 13.46           C  
-ANISOU 1377  CB  TYR A 409     1877   1764   1471    521     25   -268       C  
-ATOM   1378  CG  TYR A 409      45.986  12.280  23.108  1.00 11.70           C  
-ANISOU 1378  CG  TYR A 409     1680   1250   1513    297     49   -189       C  
-ATOM   1379  CD1 TYR A 409      46.682  12.860  22.048  1.00 12.70           C  
-ANISOU 1379  CD1 TYR A 409     1722   1481   1623    375     48   -225       C  
-ATOM   1380  CD2 TYR A 409      46.039  10.902  23.254  1.00 12.02           C  
-ANISOU 1380  CD2 TYR A 409     1592   1034   1941    102     62   -262       C  
-ATOM   1381  CE1 TYR A 409      47.436  12.087  21.181  1.00 12.40           C  
-ANISOU 1381  CE1 TYR A 409     1824   1142   1743    243   -227   -417       C  
-ATOM   1382  CE2 TYR A 409      46.787  10.125  22.396  1.00 11.14           C  
-ANISOU 1382  CE2 TYR A 409     1634   1137   1460    117    236   -109       C  
-ATOM   1383  CZ  TYR A 409      47.478  10.716  21.363  1.00 11.20           C  
-ANISOU 1383  CZ  TYR A 409     1672   1016   1565    197    210   -422       C  
-ATOM   1384  OH  TYR A 409      48.204   9.921  20.517  1.00 11.32           O  
-ANISOU 1384  OH  TYR A 409     1704    902   1695    144    112    -88       O  
-ATOM   1385  N   GLY A 410      44.173  14.212  26.865  1.00 13.27           N  
-ANISOU 1385  N   GLY A 410     1839   1617   1587    325    274   -100       N  
-ATOM   1386  CA  GLY A 410      43.156  14.980  27.563  1.00 13.90           C  
-ANISOU 1386  CA  GLY A 410     1754   1919   1607    486    302   -480       C  
-ATOM   1387  C   GLY A 410      43.638  15.643  28.839  1.00 13.74           C  
-ANISOU 1387  C   GLY A 410     1839   1805   1576    458    399    137       C  
-ATOM   1388  O   GLY A 410      42.828  16.094  29.655  1.00 14.15           O  
-ANISOU 1388  O   GLY A 410     1859   1907   1608    484    375     70       O  
-ATOM   1389  N   SER A 411      44.954  15.716  29.017  1.00 14.22           N  
-ANISOU 1389  N   SER A 411     1954   1834   1614    325    -59   -197       N  
-ATOM   1390  CA  SER A 411      45.522  16.395  30.179  1.00 15.17           C  
-ANISOU 1390  CA  SER A 411     2179   1871   1714    142    183     17       C  
-ATOM   1391  C   SER A 411      44.922  15.813  31.469  1.00 15.50           C  
-ANISOU 1391  C   SER A 411     2333   1997   1559    324     87   -253       C  
-ATOM   1392  O   SER A 411      44.738  14.597  31.571  1.00 17.09           O  
-ANISOU 1392  O   SER A 411     2691   1922   1878    395    358     78       O  
-ATOM   1393  CB  SER A 411      45.293  17.908  30.064  1.00 16.09           C  
-ANISOU 1393  CB  SER A 411     2421   1787   1905    -89    391   -160       C  
-ATOM   1394  OG  SER A 411      45.859  18.621  31.150  1.00 17.24           O  
-ANISOU 1394  OG  SER A 411     2608   2213   1729   -160    470   -488       O  
-ATOM   1395  N   ASN A 412      44.610  16.661  32.448  1.00 16.05           N  
-ANISOU 1395  N   ASN A 412     2239   2378   1482    400    253     58       N  
-ATOM   1396  CA  ASN A 412      43.975  16.173  33.679  1.00 17.25           C  
-ANISOU 1396  CA  ASN A 412     2419   2438   1696    342    172   -255       C  
-ATOM   1397  C   ASN A 412      42.452  16.287  33.654  1.00 17.59           C  
-ANISOU 1397  C   ASN A 412     2476   2733   1474    127    511     32       C  
-ATOM   1398  O   ASN A 412      41.784  16.012  34.658  1.00 21.25           O  
-ANISOU 1398  O   ASN A 412     2803   3553   1717    304    450    100       O  
-ATOM   1399  CB  ASN A 412      44.524  16.892  34.917  1.00 18.37           C  
-ANISOU 1399  CB  ASN A 412     2502   2507   1970    211     42     71       C  
-ATOM   1400  CG  ASN A 412      46.010  16.649  35.126  1.00 19.88           C  
-ANISOU 1400  CG  ASN A 412     2743   2484   2324    278   -139    207       C  
-ATOM   1401  OD1 ASN A 412      46.560  15.644  34.674  1.00 22.39           O  
-ANISOU 1401  OD1 ASN A 412     2911   2723   2874    464   -293    -95       O  
-ATOM   1402  ND2 ASN A 412      46.670  17.575  35.814  1.00 21.30           N  
-ANISOU 1402  ND2 ASN A 412     3078   2436   2580    422    -84     68       N  
-ATOM   1403  N   LEU A 413      41.902  16.674  32.506  1.00 16.98           N  
-ANISOU 1403  N   LEU A 413     2373   2424   1653    270    162     77       N  
-ATOM   1404  CA  LEU A 413      40.465  16.938  32.402  1.00 17.89           C  
-ANISOU 1404  CA  LEU A 413     2392   2380   2024    211    127    -97       C  
-ATOM   1405  C   LEU A 413      39.654  15.682  32.119  1.00 17.56           C  
-ANISOU 1405  C   LEU A 413     2566   2435   1672    152    337    -59       C  
-ATOM   1406  O   LEU A 413      38.643  15.418  32.774  1.00 19.16           O  
-ANISOU 1406  O   LEU A 413     2693   2576   2011    136    489    332       O  
-ATOM   1407  CB  LEU A 413      40.178  17.992  31.329  1.00 17.94           C  
-ANISOU 1407  CB  LEU A 413     2224   2399   2193    539    109     81       C  
-ATOM   1408  CG  LEU A 413      38.695  18.295  31.087  1.00 19.42           C  
-ANISOU 1408  CG  LEU A 413     2233   2506   2640    643    502    -31       C  
-ATOM   1409  CD1 LEU A 413      38.029  18.855  32.351  1.00 22.19           C  
-ANISOU 1409  CD1 LEU A 413     2476   2721   3234    802    793   -192       C  
-ATOM   1410  CD2 LEU A 413      38.525  19.258  29.918  1.00 20.73           C  
-ANISOU 1410  CD2 LEU A 413     2338   2535   3001    642    363    533       C  
-ATOM   1411  N   THR A 414      40.093  14.909  31.136  1.00 16.63           N  
-ANISOU 1411  N   THR A 414     2514   2167   1636   -133    279    -59       N  
-ATOM   1412  CA  THR A 414      39.331  13.743  30.719  1.00 18.03           C  
-ANISOU 1412  CA  THR A 414     2764   2354   1730   -241    289     12       C  
-ATOM   1413  C   THR A 414      40.214  12.749  29.985  1.00 18.66           C  
-ANISOU 1413  C   THR A 414     2997   2134   1957   -279    509     97       C  
-ATOM   1414  O   THR A 414      41.263  13.109  29.449  1.00 18.75           O  
-ANISOU 1414  O   THR A 414     2927   1993   2204   -126    582    154       O  
-ATOM   1415  CB  THR A 414      38.179  14.159  29.793  1.00 20.29           C  
-ANISOU 1415  CB  THR A 414     2994   2799   1915   -403    199    369       C  
-ATOM   1416  OG1 THR A 414      37.364  13.020  29.496  1.00 24.32           O  
-ANISOU 1416  OG1 THR A 414     3174   2957   3107   -501    344   -114       O  
-ATOM   1417  CG2 THR A 414      38.723  14.748  28.498  1.00 21.82           C  
-ANISOU 1417  CG2 THR A 414     3130   3141   2017    -85    250    196       C  
-ATOM   1418  N   GLN A 415      39.806  11.488  29.968  1.00 20.43           N  
-ANISOU 1418  N   GLN A 415     3331   2212   2219   -335    591     15       N  
-ATOM   1419  CA  GLN A 415      40.443  10.542  29.070  1.00 22.61           C  
-ANISOU 1419  CA  GLN A 415     3599   2458   2534   -333    760    227       C  
-ATOM   1420  C   GLN A 415      39.953  10.871  27.671  1.00 21.78           C  
-ANISOU 1420  C   GLN A 415     3147   2718   2411   -363    910   -181       C  
-ATOM   1421  O   GLN A 415      38.748  10.989  27.438  1.00 23.89           O  
-ANISOU 1421  O   GLN A 415     3092   3213   2770    -49    802   -625       O  
-ATOM   1422  CB  GLN A 415      40.091   9.100  29.422  1.00 26.32           C  
-ANISOU 1422  CB  GLN A 415     4402   2471   3127    132    948    603       C  
-ATOM   1423  CG  GLN A 415      40.811   8.085  28.548  1.00 31.56           C  
-ANISOU 1423  CG  GLN A 415     5102   2693   4196    625    926    692       C  
-ATOM   1424  CD  GLN A 415      40.409   6.657  28.853  1.00 39.03           C  
-ANISOU 1424  CD  GLN A 415     5680   3335   5814    971   1036    653       C  
-ATOM   1425  OE1 GLN A 415      41.260   5.785  29.031  1.00 42.32           O  
-ANISOU 1425  OE1 GLN A 415     6000   3615   6463   1266    989    764       O  
-ATOM   1426  NE2 GLN A 415      39.106   6.408  28.908  1.00 42.18           N  
-ANISOU 1426  NE2 GLN A 415     5909   3585   6531   1020    939    459       N  
-ATOM   1427  N   ALA A 416      40.886  11.037  26.742  1.00 20.55           N  
-ANISOU 1427  N   ALA A 416     2881   2755   2172   -146    608     13       N  
-ATOM   1428  CA  ALA A 416      40.523  11.420  25.390  1.00 21.74           C  
-ANISOU 1428  CA  ALA A 416     2630   3223   2405    -93    513   -512       C  
-ATOM   1429  C   ALA A 416      39.538  10.414  24.824  1.00 24.68           C  
-ANISOU 1429  C   ALA A 416     2540   3645   3193     61    289   -959       C  
-ATOM   1430  O   ALA A 416      39.673   9.207  25.026  1.00 24.77           O  
-ANISOU 1430  O   ALA A 416     2633   3715   3064    -55    475  -1122       O  
-ATOM   1431  CB  ALA A 416      41.755  11.518  24.509  1.00 22.02           C  
-ANISOU 1431  CB  ALA A 416     2607   3501   2257     66    844   -134       C  
-ATOM   1432  N   SER A 417      38.526  10.912  24.127  1.00 25.89           N  
-ANISOU 1432  N   SER A 417     2520   3810   3506    180     72  -1530       N  
-ATOM   1433  CA  SER A 417      37.563  10.020  23.505  1.00 25.39           C  
-ANISOU 1433  CA  SER A 417     2413   3459   3776    -57     89  -1286       C  
-ATOM   1434  C   SER A 417      38.124   9.433  22.210  1.00 21.47           C  
-ANISOU 1434  C   SER A 417     2095   2914   3147   -256    631   -647       C  
-ATOM   1435  O   SER A 417      39.053   9.982  21.610  1.00 21.86           O  
-ANISOU 1435  O   SER A 417     2270   2498   3537   -183    463   -592       O  
-ATOM   1436  CB  SER A 417      36.231  10.734  23.260  1.00 27.39           C  
-ANISOU 1436  CB  SER A 417     2632   3582   4192    -18    -60   -750       C  
-ATOM   1437  OG  SER A 417      36.430  12.016  22.694  1.00 27.19           O  
-ANISOU 1437  OG  SER A 417     2631   3488   4212   -388   -325    184       O  
-ATOM   1438  N   GLN A 418      37.574   8.296  21.808  1.00 20.85           N  
-ANISOU 1438  N   GLN A 418     2076   2525   3322   -181    278   -857       N  
-ATOM   1439  CA  GLN A 418      37.932   7.671  20.541  1.00 18.81           C  
-ANISOU 1439  CA  GLN A 418     2064   2548   2534    -57    773   -699       C  
-ATOM   1440  C   GLN A 418      39.397   7.246  20.439  1.00 16.67           C  
-ANISOU 1440  C   GLN A 418     1921   1990   2421   -257    409   -276       C  
-ATOM   1441  O   GLN A 418      39.968   7.218  19.349  1.00 17.35           O  
-ANISOU 1441  O   GLN A 418     2038   2293   2262   -179    657   -307       O  
-ATOM   1442  CB  GLN A 418      37.557   8.592  19.376  1.00 24.13           C  
-ANISOU 1442  CB  GLN A 418     2516   3470   3181    592    467   -597       C  
-ATOM   1443  CG  GLN A 418      36.064   8.866  19.295  1.00 31.32           C  
-ANISOU 1443  CG  GLN A 418     3055   4307   4536   1077    356   -477       C  
-ATOM   1444  CD  GLN A 418      35.250   7.589  19.187  1.00 41.96           C  
-ANISOU 1444  CD  GLN A 418     3818   5459   6666   1759    452   -468       C  
-ATOM   1445  OE1 GLN A 418      35.565   6.703  18.392  1.00 45.40           O  
-ANISOU 1445  OE1 GLN A 418     4301   5634   7316   1905    415   -490       O  
-ATOM   1446  NE2 GLN A 418      34.202   7.485  19.996  1.00 45.80           N  
-ANISOU 1446  NE2 GLN A 418     4103   5852   7447   1983    399   -470       N  
-ATOM   1447  N   LEU A 419      40.002   6.903  21.571  1.00 16.60           N  
-ANISOU 1447  N   LEU A 419     1886   2027   2394    -90    467    -95       N  
-ATOM   1448  CA  LEU A 419      41.323   6.295  21.537  1.00 17.75           C  
-ANISOU 1448  CA  LEU A 419     2171   2068   2506   -136    590   -315       C  
-ATOM   1449  C   LEU A 419      41.231   4.936  20.857  1.00 18.65           C  
-ANISOU 1449  C   LEU A 419     2218   1813   3055   -220   1048     50       C  
-ATOM   1450  O   LEU A 419      40.323   4.147  21.131  1.00 21.46           O  
-ANISOU 1450  O   LEU A 419     2292   1820   4040   -437   1225   -126       O  
-ATOM   1451  CB  LEU A 419      41.883   6.109  22.945  1.00 17.84           C  
-ANISOU 1451  CB  LEU A 419     2380   2268   2130   -322    504    121       C  
-ATOM   1452  CG  LEU A 419      42.435   7.314  23.699  1.00 19.13           C  
-ANISOU 1452  CG  LEU A 419     2814   2325   2127   -174    419   -265       C  
-ATOM   1453  CD1 LEU A 419      42.640   6.950  25.163  1.00 20.66           C  
-ANISOU 1453  CD1 LEU A 419     3136   2536   2178   -304    417    311       C  
-ATOM   1454  CD2 LEU A 419      43.739   7.790  23.068  1.00 17.53           C  
-ANISOU 1454  CD2 LEU A 419     2540   1982   2139   -359    429   -119       C  
-ATOM   1455  N   ALA A 420      42.169   4.661  19.962  1.00 17.66           N  
-ANISOU 1455  N   ALA A 420     2171   1716   2824   -119    848    -96       N  
-ATOM   1456  CA  ALA A 420      42.304   3.322  19.428  1.00 16.66           C  
-ANISOU 1456  CA  ALA A 420     2216   1570   2544    -54    792    -78       C  
-ATOM   1457  C   ALA A 420      42.700   2.425  20.602  1.00 18.65           C  
-ANISOU 1457  C   ALA A 420     2576   1588   2923   -278    942     32       C  
-ATOM   1458  O   ALA A 420      43.487   2.832  21.451  1.00 17.96           O  
-ANISOU 1458  O   ALA A 420     2533   1522   2770   -462    961    -21       O  
-ATOM   1459  CB  ALA A 420      43.350   3.301  18.338  1.00 16.16           C  
-ANISOU 1459  CB  ALA A 420     1947   1642   2550   -255    586     82       C  
-ATOM   1460  N   PRO A 421      42.141   1.209  20.669  1.00 20.31           N  
-ANISOU 1460  N   PRO A 421     2816   1554   3345   -481    968    -52       N  
-ATOM   1461  CA  PRO A 421      42.356   0.359  21.846  1.00 20.45           C  
-ANISOU 1461  CA  PRO A 421     3042   1746   2981   -499   1124    544       C  
-ATOM   1462  C   PRO A 421      43.747  -0.269  21.928  1.00 19.07           C  
-ANISOU 1462  C   PRO A 421     3232   1610   2403   -555    959    428       C  
-ATOM   1463  O   PRO A 421      44.462  -0.339  20.926  1.00 17.69           O  
-ANISOU 1463  O   PRO A 421     3170   1428   2122   -485    740    318       O  
-ATOM   1464  CB  PRO A 421      41.302  -0.741  21.670  1.00 22.11           C  
-ANISOU 1464  CB  PRO A 421     3202   1790   3409   -599   1279    390       C  
-ATOM   1465  CG  PRO A 421      41.114  -0.839  20.197  1.00 23.76           C  
-ANISOU 1465  CG  PRO A 421     3229   1818   3979   -602    892    125       C  
-ATOM   1466  CD  PRO A 421      41.253   0.576  19.680  1.00 22.02           C  
-ANISOU 1466  CD  PRO A 421     3040   1455   3870   -673    671   -157       C  
-ATOM   1467  N   PRO A 422      44.135  -0.729  23.123  1.00 19.58           N  
-ANISOU 1467  N   PRO A 422     3705   1784   1950   -395    878    195       N  
-ATOM   1468  CA  PRO A 422      45.375  -1.497  23.276  1.00 19.56           C  
-ANISOU 1468  CA  PRO A 422     3793   1753   1887   -442    327     -9       C  
-ATOM   1469  C   PRO A 422      45.271  -2.814  22.511  1.00 18.95           C  
-ANISOU 1469  C   PRO A 422     3628   1638   1935   -533    182     73       C  
-ATOM   1470  O   PRO A 422      44.162  -3.327  22.343  1.00 19.78           O  
-ANISOU 1470  O   PRO A 422     3546   1599   2369   -544    472   -104       O  
-ATOM   1471  CB  PRO A 422      45.433  -1.781  24.786  1.00 22.16           C  
-ANISOU 1471  CB  PRO A 422     4178   2134   2107   -106    159     87       C  
-ATOM   1472  CG  PRO A 422      44.422  -0.878  25.405  1.00 24.71           C  
-ANISOU 1472  CG  PRO A 422     4177   2922   2289     14    471    327       C  
-ATOM   1473  CD  PRO A 422      43.370  -0.664  24.377  1.00 22.13           C  
-ANISOU 1473  CD  PRO A 422     3973   2386   2050   -297    786     75       C  
-ATOM   1474  N   ILE A 423      46.399  -3.347  22.051  1.00 17.76           N  
-ANISOU 1474  N   ILE A 423     3416   1491   1840   -600     91   -183       N  
-ATOM   1475  CA  ILE A 423      46.404  -4.637  21.360  1.00 16.98           C  
-ANISOU 1475  CA  ILE A 423     3234   1375   1841   -676    -38    218       C  
-ATOM   1476  C   ILE A 423      47.157  -5.707  22.140  1.00 18.52           C  
-ANISOU 1476  C   ILE A 423     3477   1379   2180   -847   -190    388       C  
-ATOM   1477  O   ILE A 423      48.257  -5.473  22.637  1.00 18.76           O  
-ANISOU 1477  O   ILE A 423     3194   1542   2393   -890   -205    143       O  
-ATOM   1478  CB  ILE A 423      47.031  -4.546  19.952  1.00 16.85           C  
-ANISOU 1478  CB  ILE A 423     3069   1445   1886   -288    -79     31       C  
-ATOM   1479  CG1 ILE A 423      46.369  -3.430  19.137  1.00 16.76           C  
-ANISOU 1479  CG1 ILE A 423     2929   1649   1788   -295   -216    329       C  
-ATOM   1480  CG2 ILE A 423      46.923  -5.898  19.244  1.00 17.78           C  
-ANISOU 1480  CG2 ILE A 423     3077   1448   2231   -183   -369   -349       C  
-ATOM   1481  CD1 ILE A 423      47.074  -3.127  17.833  1.00 17.75           C  
-ANISOU 1481  CD1 ILE A 423     2804   2101   1837   -383      8    109       C  
-ATOM   1482  N   TYR A 424      46.547  -6.887  22.227  1.00 23.77           N  
-ANISOU 1482  N   TYR A 424     4114   1593   3324   -751    141    742       N  
-ATOM   1483  CA  TYR A 424      47.150  -8.054  22.873  1.00 24.82           C  
-ANISOU 1483  CA  TYR A 424     4357   1849   3223   -937    481    678       C  
-ATOM   1484  C   TYR A 424      47.205  -9.220  21.901  1.00 26.39           C  
-ANISOU 1484  C   TYR A 424     4526   1991   3511   -491    532    719       C  
-ATOM   1485  O   TYR A 424      46.288  -9.406  21.097  1.00 27.56           O  
-ANISOU 1485  O   TYR A 424     4757   2192   3520   -262    518    644       O  
-ATOM   1486  CB  TYR A 424      46.339  -8.465  24.100  1.00 28.77           C  
-ANISOU 1486  CB  TYR A 424     5453   2107   3370   -441    530    274       C  
-ATOM   1487  CG  TYR A 424      46.172  -7.357  25.105  1.00 31.50           C  
-ANISOU 1487  CG  TYR A 424     6079   2435   3452   -299    841    315       C  
-ATOM   1488  CD1 TYR A 424      47.183  -7.055  26.009  1.00 33.15           C  
-ANISOU 1488  CD1 TYR A 424     6378   2887   3328    -86   1070    214       C  
-ATOM   1489  CD2 TYR A 424      45.008  -6.605  25.147  1.00 33.46           C  
-ANISOU 1489  CD2 TYR A 424     6259   2890   3563   -115   1102    286       C  
-ATOM   1490  CE1 TYR A 424      47.034  -6.036  26.927  1.00 33.22           C  
-ANISOU 1490  CE1 TYR A 424     6560   2952   3109     57   1153   -289       C  
-ATOM   1491  CE2 TYR A 424      44.853  -5.587  26.058  1.00 33.98           C  
-ANISOU 1491  CE2 TYR A 424     6495   3001   3413    193   1277    203       C  
-ATOM   1492  CZ  TYR A 424      45.867  -5.305  26.945  1.00 34.75           C  
-ANISOU 1492  CZ  TYR A 424     6653   2996   3553    148   1207    -19       C  
-ATOM   1493  OH  TYR A 424      45.710  -4.289  27.856  1.00 37.69           O  
-ANISOU 1493  OH  TYR A 424     6869   3282   4170    329   1293     -6       O  
-ATOM   1494  N   PRO A 425      48.277 -10.020  21.982  1.00 26.39           N  
-ANISOU 1494  N   PRO A 425     4531   1694   3802   -625    162    290       N  
-ATOM   1495  CA  PRO A 425      48.433 -11.186  21.106  1.00 27.49           C  
-ANISOU 1495  CA  PRO A 425     4529   1845   4072   -574    175    -59       C  
-ATOM   1496  C   PRO A 425      47.396 -12.258  21.447  1.00 23.91           C  
-ANISOU 1496  C   PRO A 425     4384   2062   2637   -661    643    833       C  
-ATOM   1497  O   PRO A 425      46.981 -12.368  22.600  1.00 24.62           O  
-ANISOU 1497  O   PRO A 425     4341   2133   2881   -640    116    282       O  
-ATOM   1498  CB  PRO A 425      49.850 -11.663  21.418  1.00 28.71           C  
-ANISOU 1498  CB  PRO A 425     4435   1765   4709   -700    306   -174       C  
-ATOM   1499  CG  PRO A 425      50.061 -11.258  22.838  1.00 31.21           C  
-ANISOU 1499  CG  PRO A 425     4509   2120   5229   -390    179   -143       C  
-ATOM   1500  CD  PRO A 425      49.341  -9.948  22.999  1.00 28.47           C  
-ANISOU 1500  CD  PRO A 425     4451   1719   4645   -695    165   -242       C  
-ATOM   1501  N   PRO A 426      46.967 -13.033  20.442  1.00 25.78           N  
-ANISOU 1501  N   PRO A 426     4464   2551   2781   -609    726    235       N  
-ATOM   1502  CA  PRO A 426      45.828 -13.954  20.573  1.00 27.83           C  
-ANISOU 1502  CA  PRO A 426     4495   2886   3193   -582    558   -145       C  
-ATOM   1503  C   PRO A 426      46.141 -15.330  21.164  1.00 29.57           C  
-ANISOU 1503  C   PRO A 426     4473   3197   3563   -362    734   -160       C  
-ATOM   1504  O   PRO A 426      45.219 -15.998  21.631  1.00 33.58           O  
-ANISOU 1504  O   PRO A 426     4635   3386   4739   -219    623   -125       O  
-ATOM   1505  CB  PRO A 426      45.352 -14.112  19.127  1.00 28.84           C  
-ANISOU 1505  CB  PRO A 426     4587   3136   3233   -440    269   -585       C  
-ATOM   1506  CG  PRO A 426      46.592 -13.933  18.316  1.00 29.51           C  
-ANISOU 1506  CG  PRO A 426     4599   3219   3393   -407    484   -429       C  
-ATOM   1507  CD  PRO A 426      47.424 -12.908  19.047  1.00 27.17           C  
-ANISOU 1507  CD  PRO A 426     4585   2719   3017   -384    769     78       C  
-ATOM   1508  N   GLY A 427      47.401 -15.751  21.141  1.00 29.28           N  
-ANISOU 1508  N   GLY A 427     4455   3057   3613    -82    327   -345       N  
-ATOM   1509  CA  GLY A 427      47.756 -17.095  21.568  1.00 27.03           C  
-ANISOU 1509  CA  GLY A 427     4278   2713   3280   -154    152   -741       C  
-ATOM   1510  C   GLY A 427      48.365 -17.895  20.431  1.00 23.58           C  
-ANISOU 1510  C   GLY A 427     3995   2046   2918   -684   -153   -722       C  
-ATOM   1511  O   GLY A 427      48.832 -17.323  19.450  1.00 23.37           O  
-ANISOU 1511  O   GLY A 427     3889   2141   2849   -668    -54    -42       O  
-ATOM   1512  N   PHE A 428      48.372 -19.219  20.563  1.00 21.51           N  
-ANISOU 1512  N   PHE A 428     3942   1755   2475   -800    -69   -415       N  
-ATOM   1513  CA  PHE A 428      48.895 -20.101  19.524  1.00 21.65           C  
-ANISOU 1513  CA  PHE A 428     3794   2073   2357   -753   -125   -248       C  
-ATOM   1514  C   PHE A 428      50.336 -19.779  19.152  1.00 20.83           C  
-ANISOU 1514  C   PHE A 428     3794   1788   2333   -630   -509     75       C  
-ATOM   1515  O   PHE A 428      50.767 -20.008  18.009  1.00 19.91           O  
-ANISOU 1515  O   PHE A 428     3834   1431   2300   -664   -809     76       O  
-ATOM   1516  CB  PHE A 428      47.987 -20.088  18.287  1.00 24.21           C  
-ANISOU 1516  CB  PHE A 428     3634   2501   3063  -1184    166   -248       C  
-ATOM   1517  CG  PHE A 428      46.532 -20.216  18.620  1.00 25.24           C  
-ANISOU 1517  CG  PHE A 428     3561   2812   3216  -1467    170   -589       C  
-ATOM   1518  CD1 PHE A 428      45.687 -19.124  18.527  1.00 25.69           C  
-ANISOU 1518  CD1 PHE A 428     3592   3088   3079  -1472     80   -265       C  
-ATOM   1519  CD2 PHE A 428      46.012 -21.425  19.054  1.00 29.07           C  
-ANISOU 1519  CD2 PHE A 428     3578   3222   4243  -1251    289   -245       C  
-ATOM   1520  CE1 PHE A 428      44.347 -19.233  18.842  1.00 26.19           C  
-ANISOU 1520  CE1 PHE A 428     3630   3012   3310  -1537    319      4       C  
-ATOM   1521  CE2 PHE A 428      44.673 -21.542  19.373  1.00 29.30           C  
-ANISOU 1521  CE2 PHE A 428     3556   3272   4304  -1378    315   -216       C  
-ATOM   1522  CZ  PHE A 428      43.840 -20.445  19.267  1.00 28.13           C  
-ANISOU 1522  CZ  PHE A 428     3578   3191   3920  -1538    444   -156       C  
-ATOM   1523  N   GLY A 429      51.079 -19.262  20.130  1.00 22.09           N  
-ANISOU 1523  N   GLY A 429     3537   1427   3428   -654   -729    619       N  
-ATOM   1524  CA  GLY A 429      52.489 -18.972  19.957  1.00 22.00           C  
-ANISOU 1524  CA  GLY A 429     3253   1649   3458   -330  -1078    197       C  
-ATOM   1525  C   GLY A 429      52.723 -17.655  19.251  1.00 18.85           C  
-ANISOU 1525  C   GLY A 429     2771   1565   2826   -369  -1296     34       C  
-ATOM   1526  O   GLY A 429      53.859 -17.312  18.927  1.00 19.85           O  
-ANISOU 1526  O   GLY A 429     2934   1966   2643    -66  -1028     10       O  
-ATOM   1527  N   GLU A 430      51.647 -16.910  19.019  1.00 16.21           N  
-ANISOU 1527  N   GLU A 430     2492   1060   2607   -507   -638    372       N  
-ATOM   1528  CA  GLU A 430      51.722 -15.724  18.175  1.00 14.54           C  
-ANISOU 1528  CA  GLU A 430     2301    917   2306   -449   -553     19       C  
-ATOM   1529  C   GLU A 430      52.229 -14.483  18.897  1.00 13.31           C  
-ANISOU 1529  C   GLU A 430     2256    906   1894   -500   -408    -81       C  
-ATOM   1530  O   GLU A 430      52.011 -14.290  20.098  1.00 16.60           O  
-ANISOU 1530  O   GLU A 430     2755   1417   2136   -511    -49    -59       O  
-ATOM   1531  CB  GLU A 430      50.377 -15.448  17.501  1.00 14.26           C  
-ANISOU 1531  CB  GLU A 430     2089    932   2395   -456   -577    180       C  
-ATOM   1532  CG  GLU A 430      49.959 -16.590  16.575  1.00 15.01           C  
-ANISOU 1532  CG  GLU A 430     2039   1059   2603   -448   -529   -269       C  
-ATOM   1533  CD  GLU A 430      48.578 -16.426  15.976  1.00 14.05           C  
-ANISOU 1533  CD  GLU A 430     1979    904   2454   -505   -280    119       C  
-ATOM   1534  OE1 GLU A 430      48.082 -15.284  15.872  1.00 16.09           O  
-ANISOU 1534  OE1 GLU A 430     2058   1142   2912   -454   -330   -118       O  
-ATOM   1535  OE2 GLU A 430      47.989 -17.463  15.600  1.00 14.80           O  
-ANISOU 1535  OE2 GLU A 430     2176   1217   2231   -602   -492     62       O  
-ATOM   1536  N   ALA A 431      52.917 -13.650  18.130  1.00 12.12           N  
-ANISOU 1536  N   ALA A 431     1822    846   1937   -494   -371    171       N  
-ATOM   1537  CA  ALA A 431      53.452 -12.385  18.622  1.00 11.80           C  
-ANISOU 1537  CA  ALA A 431     1734    869   1881   -463   -529     78       C  
-ATOM   1538  C   ALA A 431      53.104 -11.280  17.637  1.00 10.52           C  
-ANISOU 1538  C   ALA A 431     1618    924   1453   -301   -564    240       C  
-ATOM   1539  O   ALA A 431      53.127 -11.485  16.424  1.00 11.55           O  
-ANISOU 1539  O   ALA A 431     1731    966   1689   -191   -524     34       O  
-ATOM   1540  CB  ALA A 431      54.965 -12.483  18.797  1.00 12.96           C  
-ANISOU 1540  CB  ALA A 431     1628   1166   2128   -263   -623    316       C  
-ATOM   1541  N   ILE A 432      52.793 -10.102  18.166  1.00 11.45           N  
-ANISOU 1541  N   ILE A 432     1615    740   1995   -146   -439     72       N  
-ATOM   1542  CA  ILE A 432      52.498  -8.944  17.336  1.00 10.40           C  
-ANISOU 1542  CA  ILE A 432     1567    722   1662    -65   -161    216       C  
-ATOM   1543  C   ILE A 432      53.723  -8.549  16.515  1.00  9.54           C  
-ANISOU 1543  C   ILE A 432     1494    808   1322    -28   -140    178       C  
-ATOM   1544  O   ILE A 432      54.859  -8.533  17.023  1.00 11.48           O  
-ANISOU 1544  O   ILE A 432     1433   1154   1773    -63   -455    211       O  
-ATOM   1545  CB  ILE A 432      52.042  -7.760  18.208  1.00 10.61           C  
-ANISOU 1545  CB  ILE A 432     1472    935   1622     28     79    201       C  
-ATOM   1546  CG1 ILE A 432      50.737  -8.118  18.940  1.00 14.08           C  
-ANISOU 1546  CG1 ILE A 432     1528   1558   2264    -16    346    -46       C  
-ATOM   1547  CG2 ILE A 432      51.880  -6.495  17.381  1.00 12.03           C  
-ANISOU 1547  CG2 ILE A 432     1669   1139   1761    144   -272    315       C  
-ATOM   1548  CD1 ILE A 432      50.350  -7.145  20.025  1.00 15.50           C  
-ANISOU 1548  CD1 ILE A 432     1939   1805   2144    184    530   -249       C  
-ATOM   1549  N   VAL A 433      53.488  -8.246  15.241  1.00  9.52           N  
-ANISOU 1549  N   VAL A 433     1478    796   1343   -234     47     86       N  
-ATOM   1550  CA  VAL A 433      54.538  -7.788  14.340  1.00  9.53           C  
-ANISOU 1550  CA  VAL A 433     1564    660   1396   -189    -80    -97       C  
-ATOM   1551  C   VAL A 433      54.585  -6.267  14.279  1.00  9.94           C  
-ANISOU 1551  C   VAL A 433     1461    669   1645   -152   -129    -13       C  
-ATOM   1552  O   VAL A 433      53.558  -5.606  14.119  1.00 10.61           O  
-ANISOU 1552  O   VAL A 433     1231    832   1968    -25   -192     91       O  
-ATOM   1553  CB  VAL A 433      54.296  -8.342  12.919  1.00 10.72           C  
-ANISOU 1553  CB  VAL A 433     1635   1036   1402   -277     44   -101       C  
-ATOM   1554  CG1 VAL A 433      55.309  -7.770  11.932  1.00 12.07           C  
-ANISOU 1554  CG1 VAL A 433     1634   1329   1622   -379     66   -184       C  
-ATOM   1555  CG2 VAL A 433      54.343  -9.888  12.933  1.00 12.43           C  
-ANISOU 1555  CG2 VAL A 433     2012    666   2044   -284    -47   -253       C  
-ATOM   1556  N   TYR A 434      55.790  -5.729  14.417  1.00  8.99           N  
-ANISOU 1556  N   TYR A 434     1324    534   1557   -263   -116    -85       N  
-ATOM   1557  CA  TYR A 434      56.039  -4.293  14.266  1.00  8.89           C  
-ANISOU 1557  CA  TYR A 434     1198    700   1479   -175   -144   -122       C  
-ATOM   1558  C   TYR A 434      56.839  -4.026  13.009  1.00  8.97           C  
-ANISOU 1558  C   TYR A 434     1301    644   1464     30    -99   -130       C  
-ATOM   1559  O   TYR A 434      57.819  -4.718  12.717  1.00 10.36           O  
-ANISOU 1559  O   TYR A 434     1274    902   1760    196    -19     12       O  
-ATOM   1560  CB  TYR A 434      56.788  -3.749  15.483  1.00  9.78           C  
-ANISOU 1560  CB  TYR A 434     1108   1094   1512   -191   -349   -284       C  
-ATOM   1561  CG  TYR A 434      56.004  -3.934  16.748  1.00 10.48           C  
-ANISOU 1561  CG  TYR A 434     1423   1275   1282    -90     62   -115       C  
-ATOM   1562  CD1 TYR A 434      54.966  -3.070  17.065  1.00 12.73           C  
-ANISOU 1562  CD1 TYR A 434     1692   1456   1689    180      9   -103       C  
-ATOM   1563  CD2 TYR A 434      56.262  -5.003  17.598  1.00 11.50           C  
-ANISOU 1563  CD2 TYR A 434     1603   1321   1446   -105   -241     33       C  
-ATOM   1564  CE1 TYR A 434      54.229  -3.238  18.208  1.00 14.36           C  
-ANISOU 1564  CE1 TYR A 434     2086   1852   1517    525    -41    392       C  
-ATOM   1565  CE2 TYR A 434      55.532  -5.179  18.750  1.00 13.87           C  
-ANISOU 1565  CE2 TYR A 434     1864   1911   1494    275   -150    137       C  
-ATOM   1566  CZ  TYR A 434      54.517  -4.289  19.051  1.00 15.10           C  
-ANISOU 1566  CZ  TYR A 434     1964   2167   1604    662     95    355       C  
-ATOM   1567  OH  TYR A 434      53.776  -4.448  20.199  1.00 19.62           O  
-ANISOU 1567  OH  TYR A 434     2572   2950   1933   1021    327    774       O  
-ATOM   1568  N   PHE A 435      56.389  -3.038  12.249  1.00  9.28           N  
-ANISOU 1568  N   PHE A 435     1280    693   1552    152   -174    156       N  
-ATOM   1569  CA  PHE A 435      57.143  -2.540  11.120  1.00  9.37           C  
-ANISOU 1569  CA  PHE A 435     1124    821   1614     64   -261    185       C  
-ATOM   1570  C   PHE A 435      58.012  -1.413  11.630  1.00  9.83           C  
-ANISOU 1570  C   PHE A 435     1134    756   1846   -149   -258    269       C  
-ATOM   1571  O   PHE A 435      57.536  -0.545  12.361  1.00 11.28           O  
-ANISOU 1571  O   PHE A 435     1403    929   1954    197     -1   -285       O  
-ATOM   1572  CB  PHE A 435      56.172  -2.091  10.031  1.00  9.49           C  
-ANISOU 1572  CB  PHE A 435     1266    627   1711    -34   -156   -244       C  
-ATOM   1573  CG  PHE A 435      55.283  -3.202   9.569  1.00  8.90           C  
-ANISOU 1573  CG  PHE A 435     1432    491   1459   -203   -121   -103       C  
-ATOM   1574  CD1 PHE A 435      55.705  -4.062   8.566  1.00 10.85           C  
-ANISOU 1574  CD1 PHE A 435     1864    663   1593    112   -267   -258       C  
-ATOM   1575  CD2 PHE A 435      54.062  -3.432  10.183  1.00 10.80           C  
-ANISOU 1575  CD2 PHE A 435     1412    858   1832   -285   -321    172       C  
-ATOM   1576  CE1 PHE A 435      54.912  -5.122   8.174  1.00 12.69           C  
-ANISOU 1576  CE1 PHE A 435     1903    849   2070   -273   -286   -310       C  
-ATOM   1577  CE2 PHE A 435      53.263  -4.492   9.796  1.00 12.94           C  
-ANISOU 1577  CE2 PHE A 435     1775   1038   2101   -112   -258   -138       C  
-ATOM   1578  CZ  PHE A 435      53.682  -5.331   8.787  1.00 13.44           C  
-ANISOU 1578  CZ  PHE A 435     1941   1051   2114   -354    109   -198       C  
-ATOM   1579  N   THR A 436      59.289  -1.434  11.255  1.00  9.15           N  
-ANISOU 1579  N   THR A 436     1148    632   1695    -76   -216    -24       N  
-ATOM   1580  CA  THR A 436      60.271  -0.512  11.816  1.00  9.20           C  
-ANISOU 1580  CA  THR A 436     1140    742   1611   -220   -200    -46       C  
-ATOM   1581  C   THR A 436      60.796   0.467  10.794  1.00  9.42           C  
-ANISOU 1581  C   THR A 436     1178    759   1641    -15     63    -88       C  
-ATOM   1582  O   THR A 436      60.887   0.166   9.598  1.00 11.00           O  
-ANISOU 1582  O   THR A 436     1449   1044   1686    -32     29   -228       O  
-ATOM   1583  CB  THR A 436      61.496  -1.271  12.381  1.00 12.83           C  
-ANISOU 1583  CB  THR A 436     1495   1253   2127    284   -365     75       C  
-ATOM   1584  OG1 THR A 436      62.165  -1.964  11.319  1.00 15.81           O  
-ANISOU 1584  OG1 THR A 436     1566   1361   3080    309   -689   -469       O  
-ATOM   1585  CG2 THR A 436      61.067  -2.270  13.459  1.00 16.31           C  
-ANISOU 1585  CG2 THR A 436     1948   1370   2880    -12  -1000    558       C  
-ATOM   1586  N   SER A 437      61.157   1.655  11.289  1.00 10.09           N  
-ANISOU 1586  N   SER A 437     1310    550   1974     43   -120    -96       N  
-ATOM   1587  CA  SER A 437      61.936   2.616  10.520  1.00  9.73           C  
-ANISOU 1587  CA  SER A 437     1094    672   1931   -104   -338     15       C  
-ATOM   1588  C   SER A 437      63.046   3.178  11.382  1.00  9.12           C  
-ANISOU 1588  C   SER A 437      872    822   1772   -178    140    101       C  
-ATOM   1589  O   SER A 437      62.848   3.461  12.569  1.00 11.72           O  
-ANISOU 1589  O   SER A 437     1302   1434   1715      7     36   -157       O  
-ATOM   1590  CB  SER A 437      61.063   3.787  10.047  1.00 11.80           C  
-ANISOU 1590  CB  SER A 437     1299    849   2333    322   -382      9       C  
-ATOM   1591  OG  SER A 437      60.021   3.343   9.199  1.00 11.00           O  
-ANISOU 1591  OG  SER A 437     1079   1011   2090     83   -296   -104       O  
-ATOM   1592  N   THR A 438      64.206   3.378  10.772  1.00  9.83           N  
-ANISOU 1592  N   THR A 438      939    604   2192     -6   -130    -90       N  
-ATOM   1593  CA  THR A 438      65.259   4.132  11.432  1.00  9.83           C  
-ANISOU 1593  CA  THR A 438      838    802   2096     72    -58   -233       C  
-ATOM   1594  C   THR A 438      64.901   5.614  11.360  1.00 10.93           C  
-ANISOU 1594  C   THR A 438     1245    911   1995    222   -137   -202       C  
-ATOM   1595  O   THR A 438      64.600   6.144  10.291  1.00 11.30           O  
-ANISOU 1595  O   THR A 438     1418    933   1942    174   -256   -165       O  
-ATOM   1596  CB  THR A 438      66.622   3.865  10.790  1.00 11.99           C  
-ANISOU 1596  CB  THR A 438      959    951   2645     -1    -96   -316       C  
-ATOM   1597  OG1 THR A 438      66.953   2.480  10.974  1.00 13.91           O  
-ANISOU 1597  OG1 THR A 438     1428   1142   2713    433   -129   -136       O  
-ATOM   1598  CG2 THR A 438      67.688   4.716  11.445  1.00 13.06           C  
-ANISOU 1598  CG2 THR A 438     1120   1209   2632   -179    -36   -237       C  
-ATOM   1599  N   PHE A 439      64.906   6.264  12.515  1.00 10.73           N  
-ANISOU 1599  N   PHE A 439     1233    769   2075    206    -70   -420       N  
-ATOM   1600  CA  PHE A 439      64.401   7.624  12.645  1.00 10.59           C  
-ANISOU 1600  CA  PHE A 439     1058    830   2134    117   -358   -522       C  
-ATOM   1601  C   PHE A 439      65.070   8.221  13.878  1.00 11.29           C  
-ANISOU 1601  C   PHE A 439     1168    948   2173     63   -257   -527       C  
-ATOM   1602  O   PHE A 439      65.415   7.492  14.807  1.00 12.34           O  
-ANISOU 1602  O   PHE A 439     1507   1103   2078    364   -205   -230       O  
-ATOM   1603  CB  PHE A 439      62.878   7.583  12.825  1.00 10.57           C  
-ANISOU 1603  CB  PHE A 439      965    740   2310    130   -102   -154       C  
-ATOM   1604  CG  PHE A 439      62.251   8.935  13.033  1.00  8.82           C  
-ANISOU 1604  CG  PHE A 439     1006    679   1665      3   -373   -114       C  
-ATOM   1605  CD1 PHE A 439      61.786   9.674  11.957  1.00 10.86           C  
-ANISOU 1605  CD1 PHE A 439      987    963   2175    203    -13    -82       C  
-ATOM   1606  CD2 PHE A 439      62.122   9.457  14.306  1.00 10.52           C  
-ANISOU 1606  CD2 PHE A 439     1076   1034   1888     46    -98   -570       C  
-ATOM   1607  CE1 PHE A 439      61.217  10.922  12.153  1.00 11.55           C  
-ANISOU 1607  CE1 PHE A 439     1000   1365   2022    285    129    113       C  
-ATOM   1608  CE2 PHE A 439      61.551  10.696  14.513  1.00 11.67           C  
-ANISOU 1608  CE2 PHE A 439     1131   1100   2201    175   -200   -225       C  
-ATOM   1609  CZ  PHE A 439      61.101  11.432  13.433  1.00 12.39           C  
-ANISOU 1609  CZ  PHE A 439     1195   1143   2370    204    108    -31       C  
-ATOM   1610  N   PRO A 440      65.274   9.547  13.893  1.00 10.26           N  
-ANISOU 1610  N   PRO A 440     1350    940   1606    131   -477   -463       N  
-ATOM   1611  CA  PRO A 440      65.957  10.182  15.033  1.00 11.29           C  
-ANISOU 1611  CA  PRO A 440     1499    888   1903    248    -15   -263       C  
-ATOM   1612  C   PRO A 440      65.093  10.318  16.301  1.00 11.26           C  
-ANISOU 1612  C   PRO A 440     1372    887   2020    194   -464   -527       C  
-ATOM   1613  O   PRO A 440      64.898  11.426  16.820  1.00 11.97           O  
-ANISOU 1613  O   PRO A 440     1370   1136   2040    255   -278   -214       O  
-ATOM   1614  CB  PRO A 440      66.341  11.563  14.484  1.00 11.96           C  
-ANISOU 1614  CB  PRO A 440     1589    781   2175    116    -75   -392       C  
-ATOM   1615  CG  PRO A 440      65.282  11.839  13.459  1.00 11.03           C  
-ANISOU 1615  CG  PRO A 440     1262   1192   1735    260   -578   -116       C  
-ATOM   1616  CD  PRO A 440      65.066  10.495  12.785  1.00 10.78           C  
-ANISOU 1616  CD  PRO A 440     1453    845   1799    305   -325   -148       C  
-ATOM   1617  N   THR A 441      64.576   9.189  16.777  1.00 10.63           N  
-ANISOU 1617  N   THR A 441     1375   1170   1492    144   -247    -69       N  
-ATOM   1618  CA  THR A 441      64.127   9.066  18.157  1.00 11.18           C  
-ANISOU 1618  CA  THR A 441     1263   1031   1954    142   -372     -4       C  
-ATOM   1619  C   THR A 441      65.400   8.768  18.954  1.00 11.30           C  
-ANISOU 1619  C   THR A 441     1680    912   1702    378   -369   -274       C  
-ATOM   1620  O   THR A 441      65.824   7.608  19.099  1.00 12.61           O  
-ANISOU 1620  O   THR A 441     1679   1037   2073    391   -376   -209       O  
-ATOM   1621  CB  THR A 441      63.072   7.949  18.328  1.00 11.33           C  
-ANISOU 1621  CB  THR A 441     1140   1097   2069    251   -118   -210       C  
-ATOM   1622  OG1 THR A 441      63.352   6.890  17.410  1.00 12.46           O  
-ANISOU 1622  OG1 THR A 441     1456   1202   2077    350    -79   -536       O  
-ATOM   1623  CG2 THR A 441      61.647   8.478  18.058  1.00 11.98           C  
-ANISOU 1623  CG2 THR A 441      992   1275   2285    372   -172   -140       C  
-ATOM   1624  N   VAL A 442      66.045   9.831  19.418  1.00 11.62           N  
-ANISOU 1624  N   VAL A 442     1478   1210   1727    488   -528   -354       N  
-ATOM   1625  CA  VAL A 442      67.388   9.722  19.976  1.00 13.25           C  
-ANISOU 1625  CA  VAL A 442     1522   1361   2149    413   -761   -296       C  
-ATOM   1626  C   VAL A 442      67.383   8.885  21.252  1.00 13.76           C  
-ANISOU 1626  C   VAL A 442     1651   1805   1770    392   -702     78       C  
-ATOM   1627  O   VAL A 442      66.556   9.097  22.141  1.00 16.31           O  
-ANISOU 1627  O   VAL A 442     1850   2225   2120    539   -408   -130       O  
-ATOM   1628  CB  VAL A 442      67.993  11.122  20.185  1.00 12.83           C  
-ANISOU 1628  CB  VAL A 442     1386   1463   2027    182   -905   -297       C  
-ATOM   1629  CG1 VAL A 442      69.334  11.051  20.907  1.00 14.99           C  
-ANISOU 1629  CG1 VAL A 442     1476   1771   2446    279   -973   -545       C  
-ATOM   1630  CG2 VAL A 442      68.141  11.820  18.837  1.00 14.18           C  
-ANISOU 1630  CG2 VAL A 442     1641   1481   2265    507   -715      1       C  
-ATOM   1631  N   SER A 443      68.318   7.932  21.305  1.00 14.46           N  
-ANISOU 1631  N   SER A 443     1575   1608   2312    401   -849    149       N  
-ATOM   1632  CA  SER A 443      68.435   6.871  22.326  1.00 15.08           C  
-ANISOU 1632  CA  SER A 443     2035   1835   1860    404   -527    238       C  
-ATOM   1633  C   SER A 443      67.699   5.568  21.980  1.00 16.99           C  
-ANISOU 1633  C   SER A 443     2355   1667   2431    214   -699   -242       C  
-ATOM   1634  O   SER A 443      67.957   4.524  22.584  1.00 20.40           O  
-ANISOU 1634  O   SER A 443     2914   1969   2869    481   -777    363       O  
-ATOM   1635  CB  SER A 443      68.105   7.341  23.755  1.00 16.35           C  
-ANISOU 1635  CB  SER A 443     2109   2401   1703    699   -376     79       C  
-ATOM   1636  OG  SER A 443      66.712   7.298  24.026  1.00 17.97           O  
-ANISOU 1636  OG  SER A 443     2065   2597   2166    698   -218    148       O  
-ATOM   1637  N   ASN A 444      66.798   5.628  20.999  1.00 16.40           N  
-ANISOU 1637  N   ASN A 444     2398   1739   2094    422   -689   -134       N  
-ATOM   1638  CA  ASN A 444      66.142   4.428  20.481  1.00 15.60           C  
-ANISOU 1638  CA  ASN A 444     2308   1766   1851     61   -343    142       C  
-ATOM   1639  C   ASN A 444      65.648   4.687  19.067  1.00 13.49           C  
-ANISOU 1639  C   ASN A 444     1893   1483   1749    126   -441     38       C  
-ATOM   1640  O   ASN A 444      64.450   4.877  18.844  1.00 13.89           O  
-ANISOU 1640  O   ASN A 444     1630   1469   2179    -69   -298     66       O  
-ATOM   1641  CB  ASN A 444      64.974   4.005  21.370  1.00 18.88           C  
-ANISOU 1641  CB  ASN A 444     2789   1963   2421    -50   -330    330       C  
-ATOM   1642  CG  ASN A 444      64.535   2.575  21.105  1.00 22.68           C  
-ANISOU 1642  CG  ASN A 444     3363   2166   3087   -115    242    578       C  
-ATOM   1643  OD1 ASN A 444      64.796   2.025  20.036  1.00 25.09           O  
-ANISOU 1643  OD1 ASN A 444     3442   2182   3908   -391   -305    265       O  
-ATOM   1644  ND2 ASN A 444      63.871   1.966  22.079  1.00 27.91           N  
-ANISOU 1644  ND2 ASN A 444     3784   2672   4149    114    610    213       N  
-ATOM   1645  N   PRO A 445      66.580   4.711  18.104  1.00 12.61           N  
-ANISOU 1645  N   PRO A 445     1501   1265   2025    204   -351     36       N  
-ATOM   1646  CA  PRO A 445      66.280   5.201  16.755  1.00 12.11           C  
-ANISOU 1646  CA  PRO A 445     1588   1242   1771    274    -35    136       C  
-ATOM   1647  C   PRO A 445      65.636   4.144  15.860  1.00 12.27           C  
-ANISOU 1647  C   PRO A 445     1683   1179   1801    240   -321     72       C  
-ATOM   1648  O   PRO A 445      65.979   4.019  14.685  1.00 14.61           O  
-ANISOU 1648  O   PRO A 445     1830   1606   2115    -56    -98    106       O  
-ATOM   1649  CB  PRO A 445      67.656   5.610  16.224  1.00 13.26           C  
-ANISOU 1649  CB  PRO A 445     1295   1246   2495    374      8     12       C  
-ATOM   1650  CG  PRO A 445      68.601   4.675  16.922  1.00 13.20           C  
-ANISOU 1650  CG  PRO A 445     1429   1180   2406    481   -329    218       C  
-ATOM   1651  CD  PRO A 445      68.022   4.489  18.310  1.00 13.22           C  
-ANISOU 1651  CD  PRO A 445     1440   1576   2006    365   -428     83       C  
-ATOM   1652  N   LYS A 446      64.686   3.406  16.420  1.00 12.17           N  
-ANISOU 1652  N   LYS A 446     1326   1141   2155   -132   -273     76       N  
-ATOM   1653  CA  LYS A 446      63.957   2.399  15.665  1.00 11.30           C  
-ANISOU 1653  CA  LYS A 446     1287   1072   1932    249   -476    122       C  
-ATOM   1654  C   LYS A 446      62.485   2.531  16.034  1.00 11.63           C  
-ANISOU 1654  C   LYS A 446     1189   1088   2141    131   -290    169       C  
-ATOM   1655  O   LYS A 446      62.065   2.089  17.102  1.00 14.29           O  
-ANISOU 1655  O   LYS A 446     1447   1669   2314    291   -151    324       O  
-ATOM   1656  CB  LYS A 446      64.491   0.993  15.987  1.00 12.98           C  
-ANISOU 1656  CB  LYS A 446     1571   1261   2100    121   -521   -141       C  
-ATOM   1657  CG  LYS A 446      63.813  -0.144  15.210  1.00 15.72           C  
-ANISOU 1657  CG  LYS A 446     1980   1317   2675    248   -464   -142       C  
-ATOM   1658  CD  LYS A 446      64.404  -1.515  15.557  1.00 18.66           C  
-ANISOU 1658  CD  LYS A 446     2295   1607   3188    229   -441    -78       C  
-ATOM   1659  CE  LYS A 446      65.837  -1.652  15.065  1.00 19.88           C  
-ANISOU 1659  CE  LYS A 446     2736   2264   2552    701   -799    -36       C  
-ATOM   1660  NZ  LYS A 446      65.926  -1.937  13.600  1.00 23.16           N  
-ANISOU 1660  NZ  LYS A 446     2972   2571   3257    717   -738    -96       N  
-ATOM   1661  N   VAL A 447      61.711   3.169  15.159  1.00 10.40           N  
-ANISOU 1661  N   VAL A 447     1124   1018   1807    152   -323   -188       N  
-ATOM   1662  CA  VAL A 447      60.304   3.438  15.442  1.00 10.47           C  
-ANISOU 1662  CA  VAL A 447     1207    936   1835     87   -116     67       C  
-ATOM   1663  C   VAL A 447      59.429   2.276  14.988  1.00 10.02           C  
-ANISOU 1663  C   VAL A 447     1292    776   1738     29   -146    -95       C  
-ATOM   1664  O   VAL A 447      59.421   1.926  13.810  1.00 10.09           O  
-ANISOU 1664  O   VAL A 447     1417    807   1610    191   -132    -90       O  
-ATOM   1665  CB  VAL A 447      59.825   4.730  14.752  1.00 10.18           C  
-ANISOU 1665  CB  VAL A 447     1257    896   1716    -48   -367    -68       C  
-ATOM   1666  CG1 VAL A 447      58.303   4.892  14.894  1.00 10.97           C  
-ANISOU 1666  CG1 VAL A 447     1063   1154   1949     64   -130    -61       C  
-ATOM   1667  CG2 VAL A 447      60.563   5.940  15.318  1.00 10.67           C  
-ANISOU 1667  CG2 VAL A 447     1606    755   1691   -171   -339   -217       C  
-ATOM   1668  N   PRO A 448      58.713   1.654  15.937  1.00  9.90           N  
-ANISOU 1668  N   PRO A 448     1526    796   1437     91   -328   -252       N  
-ATOM   1669  CA  PRO A 448      57.812   0.538  15.631  1.00  9.81           C  
-ANISOU 1669  CA  PRO A 448     1281    724   1720    -19   -445     46       C  
-ATOM   1670  C   PRO A 448      56.393   1.037  15.355  1.00  9.11           C  
-ANISOU 1670  C   PRO A 448     1217    635   1610     70   -149     -7       C  
-ATOM   1671  O   PRO A 448      55.938   1.980  16.007  1.00 10.69           O  
-ANISOU 1671  O   PRO A 448     1426    849   1786    114    -27   -184       O  
-ATOM   1672  CB  PRO A 448      57.829  -0.262  16.927  1.00 11.25           C  
-ANISOU 1672  CB  PRO A 448     1707    957   1608    165   -115     60       C  
-ATOM   1673  CG  PRO A 448      57.927   0.815  17.990  1.00 11.93           C  
-ANISOU 1673  CG  PRO A 448     1712    768   2052   -221   -220   -360       C  
-ATOM   1674  CD  PRO A 448      58.797   1.914  17.388  1.00 11.04           C  
-ANISOU 1674  CD  PRO A 448     1724    765   1705   -311    -97    -24       C  
-ATOM   1675  N   CYS A 449      55.710   0.416  14.395  1.00  9.31           N  
-ANISOU 1675  N   CYS A 449     1126    893   1519   -133   -305     11       N  
-ATOM   1676  CA  CYS A 449      54.297   0.681  14.148  1.00  9.60           C  
-ANISOU 1676  CA  CYS A 449     1233    842   1572      0   -243     -2       C  
-ATOM   1677  C   CYS A 449      53.603  -0.648  13.829  1.00  9.06           C  
-ANISOU 1677  C   CYS A 449     1252    658   1530   -197      5   -191       C  
-ATOM   1678  O   CYS A 449      54.268  -1.644  13.534  1.00  9.54           O  
-ANISOU 1678  O   CYS A 449     1323    634   1668      9     96    -40       O  
-ATOM   1679  CB  CYS A 449      54.107   1.701  13.016  1.00 10.87           C  
-ANISOU 1679  CB  CYS A 449     1522    999   1608     63   -101    -32       C  
-ATOM   1680  SG  CYS A 449      54.492   1.084  11.374  1.00 10.06           S  
-ANISOU 1680  SG  CYS A 449     1504    642   1674     52    -60    -37       S  
-ATOM   1681  N   THR A 450      52.280  -0.681  13.919  1.00  9.78           N  
-ANISOU 1681  N   THR A 450     1287    730   1700   -307    -71    160       N  
-ATOM   1682  CA  THR A 450      51.566  -1.942  13.735  1.00 10.01           C  
-ANISOU 1682  CA  THR A 450     1322    896   1584   -195    -25    211       C  
-ATOM   1683  C   THR A 450      51.004  -2.152  12.321  1.00  9.88           C  
-ANISOU 1683  C   THR A 450     1382   1007   1363   -125   -141    403       C  
-ATOM   1684  O   THR A 450      50.569  -3.249  11.983  1.00 12.10           O  
-ANISOU 1684  O   THR A 450     1714    893   1989   -228   -305    228       O  
-ATOM   1685  CB  THR A 450      50.495  -2.166  14.830  1.00 12.21           C  
-ANISOU 1685  CB  THR A 450     1553   1108   1977    -38    273    124       C  
-ATOM   1686  OG1 THR A 450      49.806  -0.937  15.100  1.00 14.18           O  
-ANISOU 1686  OG1 THR A 450     1611   1159   2618    -51    473    -71       O  
-ATOM   1687  CG2 THR A 450      51.151  -2.660  16.129  1.00 13.27           C  
-ANISOU 1687  CG2 THR A 450     2065   1274   1704    129     53    254       C  
-ATOM   1688  N   LEU A 451      51.029  -1.108  11.492  1.00 10.23           N  
-ANISOU 1688  N   LEU A 451     1469   1161   1257    154      0    161       N  
-ATOM   1689  CA  LEU A 451      50.705  -1.255  10.066  1.00 10.75           C  
-ANISOU 1689  CA  LEU A 451     1240   1119   1724    200     41    400       C  
-ATOM   1690  C   LEU A 451      51.470  -0.246   9.217  1.00 10.21           C  
-ANISOU 1690  C   LEU A 451     1513   1071   1294    119      9    312       C  
-ATOM   1691  O   LEU A 451      51.642   0.903   9.624  1.00 11.75           O  
-ANISOU 1691  O   LEU A 451     1755    875   1834     55   -182    -96       O  
-ATOM   1692  CB  LEU A 451      49.215  -1.018   9.803  1.00 12.86           C  
-ANISOU 1692  CB  LEU A 451     1350   1339   2197    206   -194     21       C  
-ATOM   1693  CG  LEU A 451      48.153  -2.037  10.194  1.00 13.99           C  
-ANISOU 1693  CG  LEU A 451     1449   1259   2606    -97   -133     39       C  
-ATOM   1694  CD1 LEU A 451      46.754  -1.467   9.927  1.00 14.14           C  
-ANISOU 1694  CD1 LEU A 451     1359   1566   2448    -47   -204    163       C  
-ATOM   1695  CD2 LEU A 451      48.372  -3.360   9.450  1.00 13.37           C  
-ANISOU 1695  CD2 LEU A 451     1618    995   2467   -229   -190   -388       C  
-ATOM   1696  N   PRO A 452      51.886  -0.656   8.008  1.00 10.26           N  
-ANISOU 1696  N   PRO A 452     1569    673   1656    173    -48     14       N  
-ATOM   1697  CA  PRO A 452      52.388   0.325   7.040  1.00 10.04           C  
-ANISOU 1697  CA  PRO A 452     1535    728   1550    252    -12    225       C  
-ATOM   1698  C   PRO A 452      51.281   1.320   6.691  1.00  9.07           C  
-ANISOU 1698  C   PRO A 452     1302    611   1532    -49   -307     88       C  
-ATOM   1699  O   PRO A 452      50.104   0.939   6.630  1.00  9.98           O  
-ANISOU 1699  O   PRO A 452     1453    737   1602   -129   -136      9       O  
-ATOM   1700  CB  PRO A 452      52.719  -0.528   5.810  1.00 11.98           C  
-ANISOU 1700  CB  PRO A 452     1775    847   1931    496    248    131       C  
-ATOM   1701  CG  PRO A 452      52.871  -1.935   6.345  1.00 13.28           C  
-ANISOU 1701  CG  PRO A 452     1842   1021   2181    364    293    259       C  
-ATOM   1702  CD  PRO A 452      51.870  -2.024   7.458  1.00 12.14           C  
-ANISOU 1702  CD  PRO A 452     1668   1057   1888    134    479    -74       C  
-ATOM   1703  N   GLN A 453      51.644   2.575   6.459  1.00  9.21           N  
-ANISOU 1703  N   GLN A 453     1281    551   1668     84    -20    101       N  
-ATOM   1704  CA  GLN A 453      50.629   3.571   6.151  1.00  9.19           C  
-ANISOU 1704  CA  GLN A 453     1403    521   1566     94   -164    161       C  
-ATOM   1705  C   GLN A 453      49.815   3.189   4.910  1.00  9.68           C  
-ANISOU 1705  C   GLN A 453     1386    815   1478    140     21    -66       C  
-ATOM   1706  O   GLN A 453      48.606   3.410   4.847  1.00  9.65           O  
-ANISOU 1706  O   GLN A 453     1071    841   1754      4    -51     78       O  
-ATOM   1707  CB  GLN A 453      51.255   4.947   5.949  1.00  9.96           C  
-ANISOU 1707  CB  GLN A 453     1475    570   1738     75    127    220       C  
-ATOM   1708  CG  GLN A 453      50.213   6.033   5.702  1.00  9.22           C  
-ANISOU 1708  CG  GLN A 453     1316    748   1439    353    -92     18       C  
-ATOM   1709  CD  GLN A 453      49.250   6.177   6.867  1.00 10.26           C  
-ANISOU 1709  CD  GLN A 453     1484    932   1480    294   -372     23       C  
-ATOM   1710  OE1 GLN A 453      49.602   5.896   8.012  1.00 10.65           O  
-ANISOU 1710  OE1 GLN A 453     1341   1042   1664    285   -100    -80       O  
-ATOM   1711  NE2 GLN A 453      48.028   6.634   6.583  1.00 11.19           N  
-ANISOU 1711  NE2 GLN A 453     1422    919   1910    138   -301    -78       N  
-ATOM   1712  N   GLU A 454      50.474   2.611   3.914  1.00  9.20           N  
-ANISOU 1712  N   GLU A 454     1418    783   1294    -90   -201   -100       N  
-ATOM   1713  CA  GLU A 454      49.766   2.300   2.684  1.00 10.00           C  
-ANISOU 1713  CA  GLU A 454     1430   1091   1279   -282    245    -18       C  
-ATOM   1714  C   GLU A 454      48.774   1.143   2.877  1.00  9.50           C  
-ANISOU 1714  C   GLU A 454     1352    753   1502   -357    247     75       C  
-ATOM   1715  O   GLU A 454      47.837   1.008   2.101  1.00 10.87           O  
-ANISOU 1715  O   GLU A 454     1313   1068   1747   -188   -183   -127       O  
-ATOM   1716  CB  GLU A 454      50.728   2.066   1.520  1.00 10.78           C  
-ANISOU 1716  CB  GLU A 454     1484   1272   1338   -441    184   -176       C  
-ATOM   1717  CG  GLU A 454      51.392   3.348   0.996  1.00 11.99           C  
-ANISOU 1717  CG  GLU A 454     1244   1454   1857   -561     23     57       C  
-ATOM   1718  CD  GLU A 454      52.561   3.829   1.855  1.00 11.57           C  
-ANISOU 1718  CD  GLU A 454     1430   1046   1918   -228    181     12       C  
-ATOM   1719  OE1 GLU A 454      53.088   4.933   1.571  1.00 12.08           O  
-ANISOU 1719  OE1 GLU A 454     1304   1253   2031   -276     39    225       O  
-ATOM   1720  OE2 GLU A 454      52.963   3.117   2.808  1.00 11.23           O  
-ANISOU 1720  OE2 GLU A 454     1167   1415   1683     -5     66    228       O  
-ATOM   1721  N   PHE A 455      48.957   0.327   3.917  1.00  9.90           N  
-ANISOU 1721  N   PHE A 455     1293    753   1713   -191    256     99       N  
-ATOM   1722  CA  PHE A 455      47.904  -0.634   4.271  1.00 10.30           C  
-ANISOU 1722  CA  PHE A 455     1334    695   1885    -69    122    232       C  
-ATOM   1723  C   PHE A 455      46.667   0.125   4.745  1.00  9.85           C  
-ANISOU 1723  C   PHE A 455     1384    647   1712    -64     55   -114       C  
-ATOM   1724  O   PHE A 455      45.537  -0.248   4.418  1.00 11.66           O  
-ANISOU 1724  O   PHE A 455     1426   1077   1928   -188    -59   -121       O  
-ATOM   1725  CB  PHE A 455      48.339  -1.580   5.398  1.00 10.55           C  
-ANISOU 1725  CB  PHE A 455     1627    700   1680     85     31    140       C  
-ATOM   1726  CG  PHE A 455      49.053  -2.823   4.933  1.00 11.08           C  
-ANISOU 1726  CG  PHE A 455     1552    710   1949   -258    -65     68       C  
-ATOM   1727  CD1 PHE A 455      50.140  -2.749   4.074  1.00 13.36           C  
-ANISOU 1727  CD1 PHE A 455     1559   1037   2481    -77    432   -328       C  
-ATOM   1728  CD2 PHE A 455      48.670  -4.067   5.413  1.00 11.73           C  
-ANISOU 1728  CD2 PHE A 455     1700    685   2070    -39   -187   -108       C  
-ATOM   1729  CE1 PHE A 455      50.809  -3.900   3.678  1.00 15.09           C  
-ANISOU 1729  CE1 PHE A 455     1744   1029   2960   -322    155   -228       C  
-ATOM   1730  CE2 PHE A 455      49.340  -5.224   5.021  1.00 13.17           C  
-ANISOU 1730  CE2 PHE A 455     1820    843   2340    -31   -301    -85       C  
-ATOM   1731  CZ  PHE A 455      50.402  -5.139   4.154  1.00 14.84           C  
-ANISOU 1731  CZ  PHE A 455     1615   1374   2648   -153   -327   -460       C  
-ATOM   1732  N   VAL A 456      46.877   1.169   5.542  1.00 10.10           N  
-ANISOU 1732  N   VAL A 456     1222    787   1827    -31    112   -122       N  
-ATOM   1733  CA  VAL A 456      45.753   1.946   6.063  1.00 11.47           C  
-ANISOU 1733  CA  VAL A 456     1482   1035   1839    107    306   -428       C  
-ATOM   1734  C   VAL A 456      44.922   2.532   4.918  1.00 11.99           C  
-ANISOU 1734  C   VAL A 456     1503   1101   1952    -12     32    -38       C  
-ATOM   1735  O   VAL A 456      43.698   2.353   4.864  1.00 12.80           O  
-ANISOU 1735  O   VAL A 456     1325   1521   2016   -187     11   -229       O  
-ATOM   1736  CB  VAL A 456      46.217   3.083   7.012  1.00 11.09           C  
-ANISOU 1736  CB  VAL A 456     1388   1126   1699     50    136    -81       C  
-ATOM   1737  CG1 VAL A 456      45.021   3.918   7.466  1.00 13.06           C  
-ANISOU 1737  CG1 VAL A 456     1445   1315   2200    309    107   -506       C  
-ATOM   1738  CG2 VAL A 456      46.972   2.512   8.206  1.00 12.91           C  
-ANISOU 1738  CG2 VAL A 456     1412   1442   2052   -123   -158    -81       C  
-ATOM   1739  N   SER A 457      45.574   3.242   3.999  1.00 11.47           N  
-ANISOU 1739  N   SER A 457     1494   1096   1768   -150    -57    -48       N  
-ATOM   1740  CA  SER A 457      44.833   3.861   2.900  1.00 12.04           C  
-ANISOU 1740  CA  SER A 457     1601   1184   1790    -34   -230    111       C  
-ATOM   1741  C   SER A 457      44.195   2.796   2.012  1.00 11.74           C  
-ANISOU 1741  C   SER A 457     1455   1082   1922   -162   -268    -34       C  
-ATOM   1742  O   SER A 457      43.110   3.001   1.472  1.00 14.43           O  
-ANISOU 1742  O   SER A 457     1450   1358   2674   -110   -496     40       O  
-ATOM   1743  CB  SER A 457      45.710   4.814   2.086  1.00 13.62           C  
-ANISOU 1743  CB  SER A 457     1495   1175   2504   -130     16    277       C  
-ATOM   1744  OG  SER A 457      46.907   4.196   1.666  1.00 13.06           O  
-ANISOU 1744  OG  SER A 457     1591   1226   2145     92     12    221       O  
-ATOM   1745  N   HIS A 458      44.859   1.651   1.884  1.00 11.20           N  
-ANISOU 1745  N   HIS A 458     1549    920   1786   -184   -242    -66       N  
-ATOM   1746  CA  HIS A 458      44.309   0.551   1.104  1.00 11.46           C  
-ANISOU 1746  CA  HIS A 458     1438   1088   1829   -243    100     85       C  
-ATOM   1747  C   HIS A 458      42.975   0.091   1.690  1.00 11.48           C  
-ANISOU 1747  C   HIS A 458     1326   1279   1758   -403   -253    -14       C  
-ATOM   1748  O   HIS A 458      41.988  -0.047   0.967  1.00 12.82           O  
-ANISOU 1748  O   HIS A 458     1498   1364   2007   -290   -441    181       O  
-ATOM   1749  CB  HIS A 458      45.297  -0.611   1.043  1.00 11.80           C  
-ANISOU 1749  CB  HIS A 458     1626    977   1878   -197   -211   -304       C  
-ATOM   1750  CG  HIS A 458      44.900  -1.689   0.085  1.00 12.94           C  
-ANISOU 1750  CG  HIS A 458     2006   1230   1681   -256   -134     57       C  
-ATOM   1751  ND1 HIS A 458      45.038  -1.556  -1.281  1.00 16.99           N  
-ANISOU 1751  ND1 HIS A 458     2879   1414   2160   -176     58   -254       N  
-ATOM   1752  CD2 HIS A 458      44.375  -2.922   0.292  1.00 13.37           C  
-ANISOU 1752  CD2 HIS A 458     1874   1261   1945   -345   -366     39       C  
-ATOM   1753  CE1 HIS A 458      44.618  -2.661  -1.872  1.00 17.21           C  
-ANISOU 1753  CE1 HIS A 458     2891   1405   2241    -71   -136   -222       C  
-ATOM   1754  NE2 HIS A 458      44.209  -3.505  -0.940  1.00 14.67           N  
-ANISOU 1754  NE2 HIS A 458     2176   1280   2118   -315   -448    166       N  
-ATOM   1755  N   PHE A 459      42.943  -0.150   2.999  1.00 12.27           N  
-ANISOU 1755  N   PHE A 459     1382   1288   1992   -274      3    100       N  
-ATOM   1756  CA  PHE A 459      41.716  -0.634   3.631  1.00 12.02           C  
-ANISOU 1756  CA  PHE A 459     1326   1260   1982   -295   -117     29       C  
-ATOM   1757  C   PHE A 459      40.616   0.431   3.582  1.00 13.18           C  
-ANISOU 1757  C   PHE A 459     1406   1297   2303   -109   -271    170       C  
-ATOM   1758  O   PHE A 459      39.447   0.111   3.397  1.00 15.11           O  
-ANISOU 1758  O   PHE A 459     1271   1723   2745   -218   -294     -5       O  
-ATOM   1759  CB  PHE A 459      41.985  -1.087   5.071  1.00 12.84           C  
-ANISOU 1759  CB  PHE A 459     1548   1382   1947    -46   -102    132       C  
-ATOM   1760  CG  PHE A 459      42.992  -2.205   5.181  1.00 12.81           C  
-ANISOU 1760  CG  PHE A 459     1488   1004   2373   -223    121   -100       C  
-ATOM   1761  CD1 PHE A 459      43.184  -3.099   4.135  1.00 13.39           C  
-ANISOU 1761  CD1 PHE A 459     1581    947   2557   -191     -2   -133       C  
-ATOM   1762  CD2 PHE A 459      43.747  -2.360   6.334  1.00 12.53           C  
-ANISOU 1762  CD2 PHE A 459     1546   1238   1977   -221    -27    127       C  
-ATOM   1763  CE1 PHE A 459      44.114  -4.122   4.235  1.00 13.81           C  
-ANISOU 1763  CE1 PHE A 459     1506   1457   2283   -339   -165    112       C  
-ATOM   1764  CE2 PHE A 459      44.678  -3.380   6.441  1.00 13.02           C  
-ANISOU 1764  CE2 PHE A 459     1466   1148   2333   -315   -216    115       C  
-ATOM   1765  CZ  PHE A 459      44.857  -4.268   5.391  1.00 12.82           C  
-ANISOU 1765  CZ  PHE A 459     1517   1222   2131   -336   -161   -210       C  
-ATOM   1766  N   VAL A 460      40.985   1.698   3.741  1.00 13.15           N  
-ANISOU 1766  N   VAL A 460     1386   1322   2288     37   -182    166       N  
-ATOM   1767  CA  VAL A 460      40.000   2.770   3.651  1.00 14.23           C  
-ANISOU 1767  CA  VAL A 460     1581   1310   2514     99   -395     81       C  
-ATOM   1768  C   VAL A 460      39.403   2.807   2.246  1.00 14.81           C  
-ANISOU 1768  C   VAL A 460     1607   1572   2448     12   -145    142       C  
-ATOM   1769  O   VAL A 460      38.185   2.940   2.065  1.00 17.80           O  
-ANISOU 1769  O   VAL A 460     1488   2275   2998    227   -507    -51       O  
-ATOM   1770  CB  VAL A 460      40.610   4.141   4.008  1.00 13.69           C  
-ANISOU 1770  CB  VAL A 460     1591   1415   2194    209   -429     61       C  
-ATOM   1771  CG1 VAL A 460      39.628   5.267   3.667  1.00 16.65           C  
-ANISOU 1771  CG1 VAL A 460     1769   1496   3061    395   -548     31       C  
-ATOM   1772  CG2 VAL A 460      40.971   4.178   5.481  1.00 15.33           C  
-ANISOU 1772  CG2 VAL A 460     1702   1740   2383    391   -144   -290       C  
-ATOM   1773  N   ASN A 461      40.269   2.672   1.250  1.00 14.55           N  
-ANISOU 1773  N   ASN A 461     1925   1439   2163   -121   -567    136       N  
-ATOM   1774  CA  ASN A 461      39.833   2.646  -0.138  1.00 15.62           C  
-ANISOU 1774  CA  ASN A 461     2124   1556   2253   -403   -401    226       C  
-ATOM   1775  C   ASN A 461      38.888   1.483  -0.455  1.00 16.22           C  
-ANISOU 1775  C   ASN A 461     2013   1482   2668   -254   -629    244       C  
-ATOM   1776  O   ASN A 461      37.859   1.658  -1.109  1.00 19.37           O  
-ANISOU 1776  O   ASN A 461     2131   1857   3371   -162   -996    505       O  
-ATOM   1777  CB  ASN A 461      41.050   2.562  -1.055  1.00 16.66           C  
-ANISOU 1777  CB  ASN A 461     2337   1913   2080   -387   -684    420       C  
-ATOM   1778  CG  ASN A 461      40.717   2.894  -2.480  1.00 19.31           C  
-ANISOU 1778  CG  ASN A 461     2748   1937   2650   -520   -671     86       C  
-ATOM   1779  OD1 ASN A 461      40.632   4.063  -2.841  1.00 21.25           O  
-ANISOU 1779  OD1 ASN A 461     3029   2063   2983   -512   -896    539       O  
-ATOM   1780  ND2 ASN A 461      40.511   1.872  -3.299  1.00 21.36           N  
-ANISOU 1780  ND2 ASN A 461     3050   2215   2851   -382   -611    488       N  
-ATOM   1781  N   GLU A 462      39.249   0.292   0.011  1.00 15.70           N  
-ANISOU 1781  N   GLU A 462     1804   1330   2831   -283   -512    267       N  
-ATOM   1782  CA  GLU A 462      38.541  -0.930  -0.359  1.00 15.83           C  
-ANISOU 1782  CA  GLU A 462     1725   1296   2993   -487   -503    309       C  
-ATOM   1783  C   GLU A 462      37.241  -1.153   0.405  1.00 16.42           C  
-ANISOU 1783  C   GLU A 462     1794   1738   2705   -249   -611    629       C  
-ATOM   1784  O   GLU A 462      36.250  -1.584  -0.176  1.00 18.31           O  
-ANISOU 1784  O   GLU A 462     1772   2056   3130   -268   -803    369       O  
-ATOM   1785  CB  GLU A 462      39.461  -2.145  -0.183  1.00 17.00           C  
-ANISOU 1785  CB  GLU A 462     1825   1597   3037   -278   -359    299       C  
-ATOM   1786  CG  GLU A 462      40.651  -2.135  -1.108  1.00 18.07           C  
-ANISOU 1786  CG  GLU A 462     2272   1813   2781   -607   -667    141       C  
-ATOM   1787  CD  GLU A 462      40.237  -2.159  -2.559  1.00 21.88           C  
-ANISOU 1787  CD  GLU A 462     3116   2215   2980   -129   -679    275       C  
-ATOM   1788  OE1 GLU A 462      39.831  -3.237  -3.047  1.00 23.65           O  
-ANISOU 1788  OE1 GLU A 462     3302   2331   3354    -85   -990   -175       O  
-ATOM   1789  OE2 GLU A 462      40.294  -1.095  -3.208  1.00 24.76           O  
-ANISOU 1789  OE2 GLU A 462     3737   2361   3309    106   -689    356       O  
-ATOM   1790  N   GLN A 463      37.254  -0.882   1.707  1.00 16.95           N  
-ANISOU 1790  N   GLN A 463     1988   1759   2691   -293   -622    296       N  
-ATOM   1791  CA  GLN A 463      36.093  -1.150   2.550  1.00 18.69           C  
-ANISOU 1791  CA  GLN A 463     1911   1939   3251   -504   -495    495       C  
-ATOM   1792  C   GLN A 463      35.594  -2.585   2.353  1.00 17.80           C  
-ANISOU 1792  C   GLN A 463     1784   1853   3125   -477   -683    405       C  
-ATOM   1793  O   GLN A 463      34.386  -2.829   2.246  1.00 21.37           O  
-ANISOU 1793  O   GLN A 463     1772   2141   4207   -483   -679    529       O  
-ATOM   1794  CB  GLN A 463      34.964  -0.167   2.230  1.00 22.73           C  
-ANISOU 1794  CB  GLN A 463     2349   2174   4113   -572   -164    463       C  
-ATOM   1795  CG  GLN A 463      35.347   1.294   2.394  1.00 26.03           C  
-ANISOU 1795  CG  GLN A 463     2611   2751   4527   -745    144    576       C  
-ATOM   1796  CD  GLN A 463      35.317   1.741   3.836  1.00 26.92           C  
-ANISOU 1796  CD  GLN A 463     2625   3197   4406   -921    256    579       C  
-ATOM   1797  OE1 GLN A 463      34.311   1.568   4.531  1.00 29.21           O  
-ANISOU 1797  OE1 GLN A 463     2648   3655   4795  -1088    123   -114       O  
-ATOM   1798  NE2 GLN A 463      36.416   2.316   4.301  1.00 28.83           N  
-ANISOU 1798  NE2 GLN A 463     2743   3673   4538   -485    141    672       N  
-ATOM   1799  N   ALA A 464      36.522  -3.535   2.295  1.00 17.38           N  
-ANISOU 1799  N   ALA A 464     1722   1646   3236   -380   -640    300       N  
-ATOM   1800  CA  ALA A 464      36.154  -4.935   2.104  1.00 17.30           C  
-ANISOU 1800  CA  ALA A 464     1674   1780   3118   -244   -637    305       C  
-ATOM   1801  C   ALA A 464      35.618  -5.523   3.401  1.00 18.04           C  
-ANISOU 1801  C   ALA A 464     1506   1873   3474   -610   -492    410       C  
-ATOM   1802  O   ALA A 464      36.257  -5.414   4.443  1.00 18.03           O  
-ANISOU 1802  O   ALA A 464     1547   2156   3148   -538   -453    368       O  
-ATOM   1803  CB  ALA A 464      37.347  -5.740   1.611  1.00 17.77           C  
-ANISOU 1803  CB  ALA A 464     1696   2047   3007      5   -296    702       C  
-ATOM   1804  N   PRO A 465      34.430  -6.142   3.347  1.00 19.28           N  
-ANISOU 1804  N   PRO A 465     1650   2343   3330   -682   -908    151       N  
-ATOM   1805  CA  PRO A 465      33.895  -6.764   4.560  1.00 20.06           C  
-ANISOU 1805  CA  PRO A 465     1670   2277   3676   -765   -691    850       C  
-ATOM   1806  C   PRO A 465      34.826  -7.840   5.114  1.00 19.49           C  
-ANISOU 1806  C   PRO A 465     1812   2418   3175   -647   -482    464       C  
-ATOM   1807  O   PRO A 465      35.454  -8.582   4.355  1.00 18.64           O  
-ANISOU 1807  O   PRO A 465     1732   2233   3117   -731   -557    311       O  
-ATOM   1808  CB  PRO A 465      32.585  -7.390   4.073  1.00 21.60           C  
-ANISOU 1808  CB  PRO A 465     1686   2564   3956   -690   -882   1005       C  
-ATOM   1809  CG  PRO A 465      32.170  -6.505   2.939  1.00 23.42           C  
-ANISOU 1809  CG  PRO A 465     1938   2716   4244   -522   -941    802       C  
-ATOM   1810  CD  PRO A 465      33.454  -6.153   2.243  1.00 21.18           C  
-ANISOU 1810  CD  PRO A 465     1765   2437   3846   -737   -943    433       C  
-ATOM   1811  N   THR A 466      34.913  -7.902   6.438  1.00 17.97           N  
-ANISOU 1811  N   THR A 466     1809   2263   2754   -601   -627    550       N  
-ATOM   1812  CA  THR A 466      35.699  -8.919   7.130  1.00 17.47           C  
-ANISOU 1812  CA  THR A 466     1973   2144   2521   -761   -618    421       C  
-ATOM   1813  C   THR A 466      34.884 -10.208   7.200  1.00 18.66           C  
-ANISOU 1813  C   THR A 466     1978   2155   2957  -1111   -401    353       C  
-ATOM   1814  O   THR A 466      33.747 -10.202   7.664  1.00 22.47           O  
-ANISOU 1814  O   THR A 466     2088   2587   3860   -881    282    268       O  
-ATOM   1815  CB  THR A 466      36.066  -8.440   8.545  1.00 18.43           C  
-ANISOU 1815  CB  THR A 466     1888   2330   2783   -991   -724    274       C  
-ATOM   1816  OG1 THR A 466      36.896  -7.274   8.447  1.00 20.18           O  
-ANISOU 1816  OG1 THR A 466     1858   2548   3262  -1008   -399     57       O  
-ATOM   1817  CG2 THR A 466      36.806  -9.524   9.328  1.00 20.21           C  
-ANISOU 1817  CG2 THR A 466     2206   2732   2740   -260   -589    624       C  
-ATOM   1818  N   ARG A 467      35.461 -11.310   6.731  1.00 18.39           N  
-ANISOU 1818  N   ARG A 467     2029   2048   2911   -965   -780    126       N  
-ATOM   1819  CA  ARG A 467      34.691 -12.542   6.574  1.00 20.24           C  
-ANISOU 1819  CA  ARG A 467     2271   2126   3292  -1121   -669    184       C  
-ATOM   1820  C   ARG A 467      35.283 -13.751   7.304  1.00 19.80           C  
-ANISOU 1820  C   ARG A 467     2393   2065   3066   -915   -591    198       C  
-ATOM   1821  O   ARG A 467      34.967 -14.896   6.981  1.00 22.50           O  
-ANISOU 1821  O   ARG A 467     2848   1946   3756   -861   -846     99       O  
-ATOM   1822  CB  ARG A 467      34.500 -12.841   5.081  1.00 22.23           C  
-ANISOU 1822  CB  ARG A 467     2710   2298   3439  -1197  -1029    307       C  
-ATOM   1823  CG  ARG A 467      33.739 -11.743   4.328  1.00 25.57           C  
-ANISOU 1823  CG  ARG A 467     3055   2927   3732   -831  -1418    639       C  
-ATOM   1824  CD  ARG A 467      33.798 -11.929   2.814  1.00 33.34           C  
-ANISOU 1824  CD  ARG A 467     3252   3752   5664   -614   -983    646       C  
-ATOM   1825  NE  ARG A 467      35.176 -11.946   2.319  1.00 36.46           N  
-ANISOU 1825  NE  ARG A 467     3421   4297   6134   -637   -890   1047       N  
-ATOM   1826  CZ  ARG A 467      35.833 -10.897   1.819  1.00 32.67           C  
-ANISOU 1826  CZ  ARG A 467     3398   3892   5122   -773  -1445   1646       C  
-ATOM   1827  NH1 ARG A 467      35.251  -9.695   1.721  1.00 29.57           N  
-ANISOU 1827  NH1 ARG A 467     3310   4005   3918   -897  -1649   1374       N  
-ATOM   1828  NH2 ARG A 467      37.089 -11.060   1.411  1.00 26.28           N  
-ANISOU 1828  NH2 ARG A 467     2857   3413   3716  -1394  -1531   1902       N  
-ATOM   1829  N   GLY A 468      36.135 -13.499   8.293  1.00 17.94           N  
-ANISOU 1829  N   GLY A 468     2036   2009   2772   -890   -535    376       N  
-ATOM   1830  CA  GLY A 468      36.715 -14.575   9.082  1.00 17.55           C  
-ANISOU 1830  CA  GLY A 468     1929   2056   2681   -759   -521    521       C  
-ATOM   1831  C   GLY A 468      37.412 -14.040  10.315  1.00 16.40           C  
-ANISOU 1831  C   GLY A 468     1814   1844   2574   -755   -457    183       C  
-ATOM   1832  O   GLY A 468      37.508 -12.822  10.498  1.00 17.39           O  
-ANISOU 1832  O   GLY A 468     1785   1928   2892   -472   -309    318       O  
-ATOM   1833  N   ASP A 469      37.910 -14.942  11.157  1.00 16.57           N  
-ANISOU 1833  N   ASP A 469     1876   1866   2553   -517   -246    355       N  
-ATOM   1834  CA  ASP A 469      38.617 -14.546  12.373  1.00 16.78           C  
-ANISOU 1834  CA  ASP A 469     1895   1688   2791   -724   -133    307       C  
-ATOM   1835  C   ASP A 469      39.906 -13.801  12.061  1.00 15.42           C  
-ANISOU 1835  C   ASP A 469     1703   1843   2313   -583    -95    316       C  
-ATOM   1836  O   ASP A 469      40.293 -12.873  12.780  1.00 15.97           O  
-ANISOU 1836  O   ASP A 469     1994   1706   2368   -549   -196     81       O  
-ATOM   1837  CB  ASP A 469      38.980 -15.770  13.218  1.00 16.63           C  
-ANISOU 1837  CB  ASP A 469     1991   1653   2675   -759    148    706       C  
-ATOM   1838  CG  ASP A 469      37.773 -16.470  13.804  1.00 19.44           C  
-ANISOU 1838  CG  ASP A 469     2209   2048   3129   -525    122    647       C  
-ATOM   1839  OD1 ASP A 469      36.687 -15.857  13.867  1.00 22.69           O  
-ANISOU 1839  OD1 ASP A 469     2311   2832   3479   -322    535    465       O  
-ATOM   1840  OD2 ASP A 469      37.931 -17.643  14.211  1.00 20.75           O  
-ANISOU 1840  OD2 ASP A 469     2249   2079   3557   -547    157    571       O  
-ATOM   1841  N   ALA A 470      40.593 -14.237  11.011  1.00 13.75           N  
-ANISOU 1841  N   ALA A 470     1462   1533   2227   -705   -215    483       N  
-ATOM   1842  CA  ALA A 470      41.881 -13.656  10.650  1.00 13.04           C  
-ANISOU 1842  CA  ALA A 470     1650   1625   1680   -461   -302    228       C  
-ATOM   1843  C   ALA A 470      42.103 -13.754   9.151  1.00 12.91           C  
-ANISOU 1843  C   ALA A 470     1701   1343   1861   -593   -198    204       C  
-ATOM   1844  O   ALA A 470      41.589 -14.669   8.495  1.00 13.90           O  
-ANISOU 1844  O   ALA A 470     2011   1277   1992   -579   -408    -41       O  
-ATOM   1845  CB  ALA A 470      43.007 -14.364  11.393  1.00 15.90           C  
-ANISOU 1845  CB  ALA A 470     1930   2140   1971   -245   -569     63       C  
-ATOM   1846  N   ALA A 471      42.862 -12.804   8.613  1.00 13.57           N  
-ANISOU 1846  N   ALA A 471     1822   1564   1769   -537   -166     41       N  
-ATOM   1847  CA  ALA A 471      43.280 -12.845   7.222  1.00 13.21           C  
-ANISOU 1847  CA  ALA A 471     1795   1341   1882   -513   -271     24       C  
-ATOM   1848  C   ALA A 471      44.676 -13.446   7.150  1.00 11.50           C  
-ANISOU 1848  C   ALA A 471     1730   1147   1492   -439   -264   -139       C  
-ATOM   1849  O   ALA A 471      45.627 -12.867   7.683  1.00 12.77           O  
-ANISOU 1849  O   ALA A 471     1759   1170   1921   -406   -369   -388       O  
-ATOM   1850  CB  ALA A 471      43.273 -11.436   6.616  1.00 13.77           C  
-ANISOU 1850  CB  ALA A 471     1797   1223   2210   -419   -144     69       C  
-ATOM   1851  N   LEU A 472      44.806 -14.597   6.496  1.00 12.10           N  
-ANISOU 1851  N   LEU A 472     1695   1209   1692   -394   -246     88       N  
-ATOM   1852  CA  LEU A 472      46.106 -15.230   6.308  1.00 12.01           C  
-ANISOU 1852  CA  LEU A 472     1802    997   1764   -602   -205    -37       C  
-ATOM   1853  C   LEU A 472      46.845 -14.503   5.197  1.00 11.14           C  
-ANISOU 1853  C   LEU A 472     1756   1060   1415   -496   -374   -225       C  
-ATOM   1854  O   LEU A 472      46.319 -14.361   4.081  1.00 11.88           O  
-ANISOU 1854  O   LEU A 472     1791   1295   1426   -474   -475    120       O  
-ATOM   1855  CB  LEU A 472      45.946 -16.710   5.924  1.00 12.45           C  
-ANISOU 1855  CB  LEU A 472     1973    953   1803   -371   -372   -142       C  
-ATOM   1856  CG  LEU A 472      47.240 -17.441   5.541  1.00 13.22           C  
-ANISOU 1856  CG  LEU A 472     2033    963   2025   -359   -665   -186       C  
-ATOM   1857  CD1 LEU A 472      48.183 -17.547   6.730  1.00 13.87           C  
-ANISOU 1857  CD1 LEU A 472     2149   1083   2037   -285   -813   -142       C  
-ATOM   1858  CD2 LEU A 472      46.938 -18.833   4.973  1.00 13.87           C  
-ANISOU 1858  CD2 LEU A 472     2211    813   2244   -359   -380   -121       C  
-ATOM   1859  N   LEU A 473      48.056 -14.037   5.511  1.00 10.38           N  
-ANISOU 1859  N   LEU A 473     1524    800   1620   -524   -138     30       N  
-ATOM   1860  CA  LEU A 473      48.935 -13.420   4.515  1.00 10.78           C  
-ANISOU 1860  CA  LEU A 473     1619    874   1601   -449   -234     -2       C  
-ATOM   1861  C   LEU A 473      50.173 -14.269   4.312  1.00 11.45           C  
-ANISOU 1861  C   LEU A 473     1689   1002   1659   -346   -501    233       C  
-ATOM   1862  O   LEU A 473      50.693 -14.859   5.268  1.00 11.81           O  
-ANISOU 1862  O   LEU A 473     1841   1068   1579   -230   -360    168       O  
-ATOM   1863  CB  LEU A 473      49.405 -12.032   4.955  1.00 11.19           C  
-ANISOU 1863  CB  LEU A 473     1791    790   1670   -390   -319     20       C  
-ATOM   1864  CG  LEU A 473      48.376 -11.034   5.453  1.00 10.84           C  
-ANISOU 1864  CG  LEU A 473     1648    674   1796   -220   -453   -111       C  
-ATOM   1865  CD1 LEU A 473      49.091  -9.714   5.729  1.00 12.03           C  
-ANISOU 1865  CD1 LEU A 473     1762    811   1996   -415   -176   -315       C  
-ATOM   1866  CD2 LEU A 473      47.275 -10.848   4.427  1.00 12.55           C  
-ANISOU 1866  CD2 LEU A 473     1723   1166   1880   -383   -525      8       C  
-ATOM   1867  N   HIS A 474      50.649 -14.322   3.070  1.00 11.40           N  
-ANISOU 1867  N   HIS A 474     1805   1010   1515   -269   -266     73       N  
-ATOM   1868  CA  HIS A 474      51.977 -14.836   2.797  1.00 10.85           C  
-ANISOU 1868  CA  HIS A 474     1959    721   1440   -168      4   -148       C  
-ATOM   1869  C   HIS A 474      52.863 -13.674   2.396  1.00 11.15           C  
-ANISOU 1869  C   HIS A 474     1789    771   1675   -300   -161   -127       C  
-ATOM   1870  O   HIS A 474      52.463 -12.819   1.608  1.00 13.04           O  
-ANISOU 1870  O   HIS A 474     1926    990   2039   -210   -509    330       O  
-ATOM   1871  CB  HIS A 474      51.947 -15.904   1.708  1.00 11.08           C  
-ANISOU 1871  CB  HIS A 474     1853    693   1662   -392    -31   -206       C  
-ATOM   1872  CG  HIS A 474      51.404 -17.205   2.187  1.00 11.36           C  
-ANISOU 1872  CG  HIS A 474     1937    662   1717   -359   -127    105       C  
-ATOM   1873  ND1 HIS A 474      51.288 -18.311   1.372  1.00 14.19           N  
-ANISOU 1873  ND1 HIS A 474     2616    819   1954   -289   -352   -148       N  
-ATOM   1874  CD2 HIS A 474      50.956 -17.586   3.408  1.00 13.15           C  
-ANISOU 1874  CD2 HIS A 474     2268    808   1921   -262   -210    206       C  
-ATOM   1875  CE1 HIS A 474      50.787 -19.312   2.069  1.00 14.45           C  
-ANISOU 1875  CE1 HIS A 474     2718    845   1925   -291   -464    -78       C  
-ATOM   1876  NE2 HIS A 474      50.584 -18.901   3.310  1.00 13.46           N  
-ANISOU 1876  NE2 HIS A 474     2385    740   1988   -300   -244    -85       N  
-ATOM   1877  N   TYR A 475      54.053 -13.630   2.979  1.00 10.49           N  
-ANISOU 1877  N   TYR A 475     1635    650   1699   -158   -285   -122       N  
-ATOM   1878  CA  TYR A 475      55.062 -12.640   2.639  1.00 10.38           C  
-ANISOU 1878  CA  TYR A 475     1645    764   1534   -238   -239   -182       C  
-ATOM   1879  C   TYR A 475      55.942 -13.314   1.607  1.00 11.23           C  
-ANISOU 1879  C   TYR A 475     1848    861   1556    -26   -326    -55       C  
-ATOM   1880  O   TYR A 475      56.675 -14.263   1.921  1.00 12.71           O  
-ANISOU 1880  O   TYR A 475     1884    925   2019     86   -174   -143       O  
-ATOM   1881  CB  TYR A 475      55.843 -12.274   3.897  1.00 10.78           C  
-ANISOU 1881  CB  TYR A 475     1594    802   1698   -136   -189    -98       C  
-ATOM   1882  CG  TYR A 475      56.923 -11.230   3.738  1.00 10.85           C  
-ANISOU 1882  CG  TYR A 475     1683    699   1741   -112   -337   -136       C  
-ATOM   1883  CD1 TYR A 475      56.608  -9.909   3.424  1.00 10.85           C  
-ANISOU 1883  CD1 TYR A 475     1773    630   1717     34   -214   -206       C  
-ATOM   1884  CD2 TYR A 475      58.262 -11.551   3.945  1.00 11.72           C  
-ANISOU 1884  CD2 TYR A 475     1783    793   1878   -129   -196     58       C  
-ATOM   1885  CE1 TYR A 475      57.595  -8.951   3.307  1.00 11.16           C  
-ANISOU 1885  CE1 TYR A 475     1596    907   1735   -103   -252      7       C  
-ATOM   1886  CE2 TYR A 475      59.262 -10.588   3.825  1.00 10.96           C  
-ANISOU 1886  CE2 TYR A 475     1796    685   1681   -283   -322    238       C  
-ATOM   1887  CZ  TYR A 475      58.918  -9.293   3.503  1.00 10.39           C  
-ANISOU 1887  CZ  TYR A 475     1619    623   1705   -173   -136    232       C  
-ATOM   1888  OH  TYR A 475      59.891  -8.321   3.391  1.00 11.26           O  
-ANISOU 1888  OH  TYR A 475     1587    717   1974   -117   -175     13       O  
-ATOM   1889  N   VAL A 476      55.834 -12.860   0.364  1.00 11.77           N  
-ANISOU 1889  N   VAL A 476     1952    983   1535   -109    283   -371       N  
-ATOM   1890  CA  VAL A 476      56.433 -13.585  -0.753  1.00 12.40           C  
-ANISOU 1890  CA  VAL A 476     1905   1189   1618   -184    411   -199       C  
-ATOM   1891  C   VAL A 476      57.595 -12.864  -1.430  1.00 12.37           C  
-ANISOU 1891  C   VAL A 476     1962   1217   1520    -77    448   -511       C  
-ATOM   1892  O   VAL A 476      57.683 -11.629  -1.415  1.00 14.15           O  
-ANISOU 1892  O   VAL A 476     2334    917   2126   -219    249   -368       O  
-ATOM   1893  CB  VAL A 476      55.375 -13.963  -1.810  1.00 13.61           C  
-ANISOU 1893  CB  VAL A 476     2105   1402   1665   -181     89   -235       C  
-ATOM   1894  CG1 VAL A 476      54.158 -14.600  -1.145  1.00 14.02           C  
-ANISOU 1894  CG1 VAL A 476     1955   1306   2065   -510    280    -64       C  
-ATOM   1895  CG2 VAL A 476      54.979 -12.748  -2.655  1.00 15.72           C  
-ANISOU 1895  CG2 VAL A 476     2275   1597   2102     51   -286     39       C  
-ATOM   1896  N   ASP A 477      58.481 -13.652  -2.026  1.00 13.94           N  
-ANISOU 1896  N   ASP A 477     1990   1438   1869     85    171   -384       N  
-ATOM   1897  CA  ASP A 477      59.572 -13.123  -2.832  1.00 16.31           C  
-ANISOU 1897  CA  ASP A 477     2139   1686   2372    141    388   -295       C  
-ATOM   1898  C   ASP A 477      58.967 -12.302  -3.964  1.00 16.49           C  
-ANISOU 1898  C   ASP A 477     2402   1785   2076    -34    514   -275       C  
-ATOM   1899  O   ASP A 477      58.056 -12.766  -4.636  1.00 16.43           O  
-ANISOU 1899  O   ASP A 477     2433   1891   1919    -10    285     -3       O  
-ATOM   1900  CB  ASP A 477      60.397 -14.277  -3.397  1.00 18.97           C  
-ANISOU 1900  CB  ASP A 477     2139   2141   2927    346    592   -178       C  
-ATOM   1901  CG  ASP A 477      61.597 -13.807  -4.187  1.00 22.15           C  
-ANISOU 1901  CG  ASP A 477     2256   2540   3620    202    351   -110       C  
-ATOM   1902  OD1 ASP A 477      62.722 -13.849  -3.643  1.00 27.66           O  
-ANISOU 1902  OD1 ASP A 477     2476   3276   4757    189     55    165       O  
-ATOM   1903  OD2 ASP A 477      61.422 -13.394  -5.352  1.00 22.11           O  
-ANISOU 1903  OD2 ASP A 477     2211   2635   3555    439    629     46       O  
-ATOM   1904  N   PRO A 478      59.467 -11.073  -4.173  1.00 17.62           N  
-ANISOU 1904  N   PRO A 478     2659   1636   2398   -351    628   -196       N  
-ATOM   1905  CA  PRO A 478      58.827 -10.160  -5.125  1.00 20.05           C  
-ANISOU 1905  CA  PRO A 478     2951   1867   2801   -145    691    162       C  
-ATOM   1906  C   PRO A 478      58.967 -10.612  -6.576  1.00 20.56           C  
-ANISOU 1906  C   PRO A 478     3459   1882   2472    -80    607     26       C  
-ATOM   1907  O   PRO A 478      58.224 -10.136  -7.432  1.00 24.33           O  
-ANISOU 1907  O   PRO A 478     3791   2433   3019    176    337    121       O  
-ATOM   1908  CB  PRO A 478      59.587  -8.848  -4.912  1.00 19.56           C  
-ANISOU 1908  CB  PRO A 478     2759   1695   2976   -356    690    -32       C  
-ATOM   1909  CG  PRO A 478      60.931  -9.274  -4.408  1.00 20.69           C  
-ANISOU 1909  CG  PRO A 478     2908   1864   3089   -326    650    -86       C  
-ATOM   1910  CD  PRO A 478      60.663 -10.475  -3.550  1.00 19.46           C  
-ANISOU 1910  CD  PRO A 478     2875   1592   2928   -378    431   -254       C  
-ATOM   1911  N   ASP A 479      59.901 -11.520  -6.843  1.00 20.21           N  
-ANISOU 1911  N   ASP A 479     3652   1847   2180   -444    955   -299       N  
-ATOM   1912  CA  ASP A 479      60.154 -11.973  -8.205  1.00 24.46           C  
-ANISOU 1912  CA  ASP A 479     4225   2238   2829   -336   1038   -141       C  
-ATOM   1913  C   ASP A 479      59.610 -13.367  -8.508  1.00 25.69           C  
-ANISOU 1913  C   ASP A 479     4767   2332   2662   -274    923   -181       C  
-ATOM   1914  O   ASP A 479      59.113 -13.615  -9.605  1.00 29.60           O  
-ANISOU 1914  O   ASP A 479     5053   2879   3314   -272    173   -433       O  
-ATOM   1915  CB  ASP A 479      61.649 -11.905  -8.510  1.00 26.39           C  
-ANISOU 1915  CB  ASP A 479     4213   2529   3284   -219   1666   -214       C  
-ATOM   1916  CG  ASP A 479      62.214 -10.516  -8.292  1.00 29.26           C  
-ANISOU 1916  CG  ASP A 479     4303   2918   3895   -265   2014    100       C  
-ATOM   1917  OD1 ASP A 479      61.936  -9.627  -9.122  1.00 32.23           O  
-ANISOU 1917  OD1 ASP A 479     4578   2952   4715    -47   1510    134       O  
-ATOM   1918  OD2 ASP A 479      62.925 -10.312  -7.287  1.00 33.32           O  
-ANISOU 1918  OD2 ASP A 479     4298   3356   5005    -79   2041    128       O  
-ATOM   1919  N   THR A 480      59.698 -14.273  -7.539  1.00 24.38           N  
-ANISOU 1919  N   THR A 480     5001   2274   1989   -374    842   -142       N  
-ATOM   1920  CA  THR A 480      59.248 -15.649  -7.746  1.00 25.41           C  
-ANISOU 1920  CA  THR A 480     5258   2049   2347   -499    581   -508       C  
-ATOM   1921  C   THR A 480      57.890 -15.929  -7.104  1.00 25.21           C  
-ANISOU 1921  C   THR A 480     5329   2174   2075  -1004    145   -332       C  
-ATOM   1922  O   THR A 480      57.237 -16.927  -7.420  1.00 27.31           O  
-ANISOU 1922  O   THR A 480     5488   2484   2402  -1211    -23   -505       O  
-ATOM   1923  CB  THR A 480      60.253 -16.651  -7.171  1.00 27.83           C  
-ANISOU 1923  CB  THR A 480     5359   1994   3219   -224    994   -288       C  
-ATOM   1924  OG1 THR A 480      60.256 -16.551  -5.740  1.00 29.00           O  
-ANISOU 1924  OG1 THR A 480     5368   1656   3994   -140    989   -164       O  
-ATOM   1925  CG2 THR A 480      61.653 -16.381  -7.717  1.00 29.69           C  
-ANISOU 1925  CG2 THR A 480     5403   2111   3768   -245   1132   -253       C  
-ATOM   1926  N   HIS A 481      57.484 -15.055  -6.189  1.00 24.88           N  
-ANISOU 1926  N   HIS A 481     5207   2034   2211  -1077   -134   -115       N  
-ATOM   1927  CA  HIS A 481      56.224 -15.197  -5.459  1.00 27.04           C  
-ANISOU 1927  CA  HIS A 481     5211   2164   2898   -939   -487      9       C  
-ATOM   1928  C   HIS A 481      56.208 -16.404  -4.523  1.00 25.55           C  
-ANISOU 1928  C   HIS A 481     4759   2034   2913  -1063   -248   -415       C  
-ATOM   1929  O   HIS A 481      55.151 -16.827  -4.044  1.00 26.73           O  
-ANISOU 1929  O   HIS A 481     4592   2364   3200  -1392    408   -483       O  
-ATOM   1930  CB  HIS A 481      55.036 -15.217  -6.423  1.00 33.18           C  
-ANISOU 1930  CB  HIS A 481     5769   2942   3896   -430  -1430    456       C  
-ATOM   1931  CG  HIS A 481      54.838 -13.924  -7.147  1.00 41.38           C  
-ANISOU 1931  CG  HIS A 481     6408   3618   5696    174  -1989    508       C  
-ATOM   1932  ND1 HIS A 481      55.202 -12.709  -6.607  1.00 44.01           N  
-ANISOU 1932  ND1 HIS A 481     6649   3917   6154    397  -2338    630       N  
-ATOM   1933  CD2 HIS A 481      54.328 -13.653  -8.373  1.00 44.52           C  
-ANISOU 1933  CD2 HIS A 481     6713   3930   6270    480  -2239    678       C  
-ATOM   1934  CE1 HIS A 481      54.918 -11.745  -7.465  1.00 46.10           C  
-ANISOU 1934  CE1 HIS A 481     6814   4093   6610    485  -2477    673       C  
-ATOM   1935  NE2 HIS A 481      54.388 -12.291  -8.545  1.00 46.16           N  
-ANISOU 1935  NE2 HIS A 481     6872   4104   6563    577  -2391    739       N  
-ATOM   1936  N   ARG A 482      57.391 -16.944  -4.254  1.00 20.62           N  
-ANISOU 1936  N   ARG A 482     4342   1629   1864   -748    151   -463       N  
-ATOM   1937  CA  ARG A 482      57.526 -18.015  -3.279  1.00 20.52           C  
-ANISOU 1937  CA  ARG A 482     4077   1621   2097   -364    272   -215       C  
-ATOM   1938  C   ARG A 482      57.260 -17.475  -1.880  1.00 17.00           C  
-ANISOU 1938  C   ARG A 482     3334   1175   1951   -317    246    -47       C  
-ATOM   1939  O   ARG A 482      57.740 -16.400  -1.522  1.00 16.12           O  
-ANISOU 1939  O   ARG A 482     2852    941   2330   -302    137   -245       O  
-ATOM   1940  CB  ARG A 482      58.933 -18.600  -3.344  1.00 25.31           C  
-ANISOU 1940  CB  ARG A 482     4401   2456   2760    228    434     96       C  
-ATOM   1941  CG  ARG A 482      59.110 -19.883  -2.565  1.00 33.00           C  
-ANISOU 1941  CG  ARG A 482     4682   3529   4328    435    467    138       C  
-ATOM   1942  CD  ARG A 482      60.504 -20.459  -2.781  1.00 39.83           C  
-ANISOU 1942  CD  ARG A 482     5057   4279   5795    726    556      7       C  
-ATOM   1943  NE  ARG A 482      61.539 -19.696  -2.078  1.00 45.44           N  
-ANISOU 1943  NE  ARG A 482     5299   4964   7000    783    622   -231       N  
-ATOM   1944  CZ  ARG A 482      62.229 -18.688  -2.603  1.00 50.68           C  
-ANISOU 1944  CZ  ARG A 482     5523   5734   7999   1020    511   -670       C  
-ATOM   1945  NH1 ARG A 482      62.003 -18.304  -3.849  1.00 51.84           N  
-ANISOU 1945  NH1 ARG A 482     5569   5865   8263   1030    404   -743       N  
-ATOM   1946  NH2 ARG A 482      63.145 -18.064  -1.877  1.00 52.02           N  
-ANISOU 1946  NH2 ARG A 482     5628   5886   8251   1171    464   -905       N  
-ATOM   1947  N   ASN A 483      56.500 -18.219  -1.090  1.00 17.19           N  
-ANISOU 1947  N   ASN A 483     3197   1264   2070   -273    -97   -213       N  
-ATOM   1948  CA  ASN A 483      56.217 -17.831   0.285  1.00 15.19           C  
-ANISOU 1948  CA  ASN A 483     2819   1235   1717   -317   -136    108       C  
-ATOM   1949  C   ASN A 483      57.458 -17.894   1.173  1.00 15.14           C  
-ANISOU 1949  C   ASN A 483     2669   1064   2017     44   -350    252       C  
-ATOM   1950  O   ASN A 483      58.139 -18.928   1.235  1.00 18.44           O  
-ANISOU 1950  O   ASN A 483     3191    991   2823    305   -469     21       O  
-ATOM   1951  CB  ASN A 483      55.120 -18.727   0.865  1.00 16.02           C  
-ANISOU 1951  CB  ASN A 483     2698   1353   2034   -576   -206     73       C  
-ATOM   1952  CG  ASN A 483      54.771 -18.366   2.290  1.00 18.65           C  
-ANISOU 1952  CG  ASN A 483     2648   1920   2517   -361   -346    336       C  
-ATOM   1953  OD1 ASN A 483      54.742 -17.187   2.657  1.00 19.16           O  
-ANISOU 1953  OD1 ASN A 483     2527   2226   2525   -363   -272   -195       O  
-ATOM   1954  ND2 ASN A 483      54.519 -19.381   3.110  1.00 21.89           N  
-ANISOU 1954  ND2 ASN A 483     2857   2528   2932   -460    -96    657       N  
-ATOM   1955  N   LEU A 484      57.737 -16.793   1.866  1.00 14.17           N  
-ANISOU 1955  N   LEU A 484     2324   1067   1992   -130   -166   -421       N  
-ATOM   1956  CA  LEU A 484      58.875 -16.700   2.776  1.00 13.63           C  
-ANISOU 1956  CA  LEU A 484     1777   1207   2194   -354    -17   -137       C  
-ATOM   1957  C   LEU A 484      58.464 -16.793   4.246  1.00 14.13           C  
-ANISOU 1957  C   LEU A 484     1811   1281   2275    -26    254     74       C  
-ATOM   1958  O   LEU A 484      59.304 -17.024   5.117  1.00 16.30           O  
-ANISOU 1958  O   LEU A 484     2202   1919   2073    144   -463    -10       O  
-ATOM   1959  CB  LEU A 484      59.616 -15.381   2.554  1.00 14.10           C  
-ANISOU 1959  CB  LEU A 484     1806   1477   2073   -278    183   -194       C  
-ATOM   1960  CG  LEU A 484      60.031 -15.092   1.112  1.00 15.29           C  
-ANISOU 1960  CG  LEU A 484     1969   1569   2269    -28    287   -156       C  
-ATOM   1961  CD1 LEU A 484      60.684 -13.724   1.019  1.00 17.33           C  
-ANISOU 1961  CD1 LEU A 484     2279   1772   2531   -386    -58    -16       C  
-ATOM   1962  CD2 LEU A 484      60.963 -16.173   0.601  1.00 17.92           C  
-ANISOU 1962  CD2 LEU A 484     2080   1956   2771    341    458   -121       C  
-ATOM   1963  N   GLY A 485      57.177 -16.601   4.519  1.00 12.94           N  
-ANISOU 1963  N   GLY A 485     1876   1092   1946     65     13     16       N  
-ATOM   1964  CA  GLY A 485      56.673 -16.613   5.881  1.00 13.25           C  
-ANISOU 1964  CA  GLY A 485     1832   1503   1698     18    145     97       C  
-ATOM   1965  C   GLY A 485      55.204 -16.252   5.953  1.00 11.68           C  
-ANISOU 1965  C   GLY A 485     1770   1294   1372   -200   -196     71       C  
-ATOM   1966  O   GLY A 485      54.723 -15.398   5.199  1.00 13.92           O  
-ANISOU 1966  O   GLY A 485     1929   1443   1918    -67   -100    488       O  
-ATOM   1967  N   GLU A 486      54.482 -16.909   6.857  1.00 12.24           N  
-ANISOU 1967  N   GLU A 486     1824   1252   1573   -301     86    -38       N  
-ATOM   1968  CA  GLU A 486      53.054 -16.655   7.028  1.00 11.79           C  
-ANISOU 1968  CA  GLU A 486     1871    849   1758   -465   -277     68       C  
-ATOM   1969  C   GLU A 486      52.775 -15.685   8.161  1.00 11.30           C  
-ANISOU 1969  C   GLU A 486     1760    866   1666   -164   -423     56       C  
-ATOM   1970  O   GLU A 486      53.499 -15.662   9.164  1.00 12.76           O  
-ANISOU 1970  O   GLU A 486     1947   1178   1721     14   -577     69       O  
-ATOM   1971  CB  GLU A 486      52.317 -17.948   7.354  1.00 12.35           C  
-ANISOU 1971  CB  GLU A 486     2347    714   1631   -306   -207    -30       C  
-ATOM   1972  CG  GLU A 486      52.408 -19.034   6.317  1.00 13.85           C  
-ANISOU 1972  CG  GLU A 486     2523    778   1959   -258    -73   -202       C  
-ATOM   1973  CD  GLU A 486      51.409 -20.123   6.619  1.00 13.62           C  
-ANISOU 1973  CD  GLU A 486     2298    801   2074   -426   -271    119       C  
-ATOM   1974  OE1 GLU A 486      51.551 -20.763   7.682  1.00 15.38           O  
-ANISOU 1974  OE1 GLU A 486     2466   1081   2297   -312   -412    298       O  
-ATOM   1975  OE2 GLU A 486      50.460 -20.296   5.825  1.00 14.30           O  
-ANISOU 1975  OE2 GLU A 486     2170   1140   2121   -334   -396    -43       O  
-ATOM   1976  N   PHE A 487      51.696 -14.919   8.012  1.00 10.83           N  
-ANISOU 1976  N   PHE A 487     1589    899   1626   -222   -251    111       N  
-ATOM   1977  CA  PHE A 487      51.258 -13.971   9.031  1.00  9.98           C  
-ANISOU 1977  CA  PHE A 487     1452    775   1563   -415    -15    211       C  
-ATOM   1978  C   PHE A 487      49.741 -14.023   9.127  1.00 11.27           C  
-ANISOU 1978  C   PHE A 487     1580    928   1773   -323   -177    -17       C  
-ATOM   1979  O   PHE A 487      49.065 -14.345   8.151  1.00 12.23           O  
-ANISOU 1979  O   PHE A 487     1766   1319   1563   -306   -362     -8       O  
-ATOM   1980  CB  PHE A 487      51.689 -12.546   8.648  1.00 11.30           C  
-ANISOU 1980  CB  PHE A 487     1358    958   1978   -550   -112    196       C  
-ATOM   1981  CG  PHE A 487      53.177 -12.359   8.582  1.00 10.53           C  
-ANISOU 1981  CG  PHE A 487     1323    847   1832   -440   -167     42       C  
-ATOM   1982  CD1 PHE A 487      53.865 -11.820   9.656  1.00 11.71           C  
-ANISOU 1982  CD1 PHE A 487     1250   1272   1926   -277   -522   -130       C  
-ATOM   1983  CD2 PHE A 487      53.892 -12.732   7.452  1.00 11.29           C  
-ANISOU 1983  CD2 PHE A 487     1382   1034   1872   -344   -175    277       C  
-ATOM   1984  CE1 PHE A 487      55.236 -11.637   9.602  1.00 12.42           C  
-ANISOU 1984  CE1 PHE A 487     1212   1527   1981   -216   -277    -90       C  
-ATOM   1985  CE2 PHE A 487      55.269 -12.566   7.398  1.00 11.35           C  
-ANISOU 1985  CE2 PHE A 487     1527   1222   1564   -121   -361    -53       C  
-ATOM   1986  CZ  PHE A 487      55.934 -12.015   8.474  1.00 11.65           C  
-ANISOU 1986  CZ  PHE A 487     1247   1389   1788   -269   -184    -60       C  
-ATOM   1987  N   LYS A 488      49.200 -13.714  10.299  1.00 11.18           N  
-ANISOU 1987  N   LYS A 488     1555    928   1766   -193   -300    -96       N  
-ATOM   1988  CA  LYS A 488      47.756 -13.592  10.448  1.00 11.13           C  
-ANISOU 1988  CA  LYS A 488     1525    783   1919   -325   -304     94       C  
-ATOM   1989  C   LYS A 488      47.402 -12.154  10.794  1.00 10.91           C  
-ANISOU 1989  C   LYS A 488     1694    662   1790   -309   -315    -48       C  
-ATOM   1990  O   LYS A 488      47.935 -11.605  11.763  1.00 13.40           O  
-ANISOU 1990  O   LYS A 488     1864   1032   2196   -142   -765   -293       O  
-ATOM   1991  CB  LYS A 488      47.242 -14.552  11.517  1.00 11.63           C  
-ANISOU 1991  CB  LYS A 488     1669    788   1961   -407   -285   -177       C  
-ATOM   1992  CG  LYS A 488      47.256 -16.009  11.028  1.00 12.54           C  
-ANISOU 1992  CG  LYS A 488     1923    809   2033   -426   -362    -88       C  
-ATOM   1993  CD  LYS A 488      47.177 -17.022  12.162  1.00 13.13           C  
-ANISOU 1993  CD  LYS A 488     1761   1142   2084   -557   -246    195       C  
-ATOM   1994  CE  LYS A 488      45.821 -17.016  12.848  1.00 14.08           C  
-ANISOU 1994  CE  LYS A 488     1946   1247   2157   -525   -230    489       C  
-ATOM   1995  NZ  LYS A 488      45.806 -17.982  13.980  1.00 14.10           N  
-ANISOU 1995  NZ  LYS A 488     1906   1291   2160   -557   -135     95       N  
-ATOM   1996  N   MET A 489      46.532 -11.538   9.985  1.00 10.87           N  
-ANISOU 1996  N   MET A 489     1497    820   1811   -177   -388    238       N  
-ATOM   1997  CA  MET A 489      46.038 -10.191  10.255  1.00 11.68           C  
-ANISOU 1997  CA  MET A 489     1762    866   1811   -223   -319    -18       C  
-ATOM   1998  C   MET A 489      44.691 -10.302  10.937  1.00 13.23           C  
-ANISOU 1998  C   MET A 489     1575   1350   2102   -276   -172   -286       C  
-ATOM   1999  O   MET A 489      43.801 -10.994  10.450  1.00 18.04           O  
-ANISOU 1999  O   MET A 489     1699   2218   2937   -357   -267  -1142       O  
-ATOM   2000  CB  MET A 489      45.828  -9.399   8.962  1.00 17.04           C  
-ANISOU 2000  CB  MET A 489     2586   1770   2118    110   -305    516       C  
-ATOM   2001  CG  MET A 489      47.046  -8.801   8.305  1.00 22.69           C  
-ANISOU 2001  CG  MET A 489     2557   2853   3212    271    -39    288       C  
-ATOM   2002  SD  MET A 489      46.580  -7.257   7.474  1.00 20.21           S  
-ANISOU 2002  SD  MET A 489     1907   3061   2711   -258     -5   1545       S  
-ATOM   2003  CE  MET A 489      46.619  -6.128   8.856  1.00 26.71           C  
-ANISOU 2003  CE  MET A 489     2551   3226   4372     -9   -334   1003       C  
-ATOM   2004  N   TYR A 490      44.519  -9.603  12.048  1.00 12.02           N  
-ANISOU 2004  N   TYR A 490     1514   1247   1804   -293     35      9       N  
-ATOM   2005  CA  TYR A 490      43.262  -9.660  12.774  1.00 11.68           C  
-ANISOU 2005  CA  TYR A 490     1421   1231   1785   -363    105     15       C  
-ATOM   2006  C   TYR A 490      42.413  -8.429  12.456  1.00 13.53           C  
-ANISOU 2006  C   TYR A 490     1446   1525   2168   -300   -196    -29       C  
-ATOM   2007  O   TYR A 490      42.948  -7.398  12.040  1.00 14.08           O  
-ANISOU 2007  O   TYR A 490     1575   1513   2261   -116   -267     60       O  
-ATOM   2008  CB  TYR A 490      43.527  -9.835  14.275  1.00 12.56           C  
-ANISOU 2008  CB  TYR A 490     1667   1286   1817   -282     45    123       C  
-ATOM   2009  CG  TYR A 490      44.068 -11.217  14.589  1.00 12.48           C  
-ANISOU 2009  CG  TYR A 490     1668   1080   1994   -396   -298     46       C  
-ATOM   2010  CD1 TYR A 490      43.210 -12.262  14.894  1.00 13.97           C  
-ANISOU 2010  CD1 TYR A 490     1902   1002   2403   -521     10    -27       C  
-ATOM   2011  CD2 TYR A 490      45.432 -11.484  14.535  1.00 12.68           C  
-ANISOU 2011  CD2 TYR A 490     1636   1203   1979   -176   -386    183       C  
-ATOM   2012  CE1 TYR A 490      43.695 -13.531  15.166  1.00 15.02           C  
-ANISOU 2012  CE1 TYR A 490     1844   1409   2452   -267     46   -184       C  
-ATOM   2013  CE2 TYR A 490      45.926 -12.747  14.800  1.00 12.94           C  
-ANISOU 2013  CE2 TYR A 490     1710   1074   2130   -264   -410    195       C  
-ATOM   2014  CZ  TYR A 490      45.053 -13.769  15.111  1.00 13.52           C  
-ANISOU 2014  CZ  TYR A 490     1929   1082   2124   -356    -49    -50       C  
-ATOM   2015  OH  TYR A 490      45.542 -15.034  15.377  1.00 15.26           O  
-ANISOU 2015  OH  TYR A 490     2121   1089   2587   -523   -135    186       O  
-ATOM   2016  N   PRO A 491      41.086  -8.542  12.624  1.00 13.91           N  
-ANISOU 2016  N   PRO A 491     1301   1459   2524   -531   -329    183       N  
-ATOM   2017  CA  PRO A 491      40.153  -7.482  12.219  1.00 14.55           C  
-ANISOU 2017  CA  PRO A 491     1205   1526   2798   -338   -185    217       C  
-ATOM   2018  C   PRO A 491      40.467  -6.119  12.830  1.00 14.68           C  
-ANISOU 2018  C   PRO A 491     1316   1502   2760   -246    -56    130       C  
-ATOM   2019  O   PRO A 491      40.160  -5.091  12.212  1.00 15.12           O  
-ANISOU 2019  O   PRO A 491     1356   1550   2837   -170      2    340       O  
-ATOM   2020  CB  PRO A 491      38.802  -7.994  12.724  1.00 15.97           C  
-ANISOU 2020  CB  PRO A 491     1385   1445   3238   -404    -81    232       C  
-ATOM   2021  CG  PRO A 491      38.951  -9.495  12.710  1.00 17.21           C  
-ANISOU 2021  CG  PRO A 491     1340   1673   3526   -231   -187    591       C  
-ATOM   2022  CD  PRO A 491      40.383  -9.731  13.144  1.00 14.62           C  
-ANISOU 2022  CD  PRO A 491     1202   1518   2833   -569   -170    224       C  
-ATOM   2023  N   GLU A 492      41.073  -6.113  14.014  1.00 14.34           N  
-ANISOU 2023  N   GLU A 492     1469   1476   2504   -341    -35   -224       N  
-ATOM   2024  CA  GLU A 492      41.445  -4.875  14.698  1.00 15.74           C  
-ANISOU 2024  CA  GLU A 492     1885   1613   2481   -407    138    134       C  
-ATOM   2025  C   GLU A 492      42.544  -4.085  13.976  1.00 14.17           C  
-ANISOU 2025  C   GLU A 492     1859   1425   2101   -284    -75    261       C  
-ATOM   2026  O   GLU A 492      42.810  -2.941  14.321  1.00 15.89           O  
-ANISOU 2026  O   GLU A 492     2372   1358   2305   -453    331    -91       O  
-ATOM   2027  CB  GLU A 492      41.870  -5.173  16.142  1.00 17.34           C  
-ANISOU 2027  CB  GLU A 492     2210   2001   2377   -680    233    237       C  
-ATOM   2028  CG  GLU A 492      40.743  -5.683  17.030  1.00 20.66           C  
-ANISOU 2028  CG  GLU A 492     2576   2048   3227   -690    593    116       C  
-ATOM   2029  CD  GLU A 492      40.482  -7.181  16.910  1.00 23.71           C  
-ANISOU 2029  CD  GLU A 492     2981   2416   3610   -545    898    405       C  
-ATOM   2030  OE1 GLU A 492      41.195  -7.885  16.163  1.00 20.77           O  
-ANISOU 2030  OE1 GLU A 492     3029   2241   2620   -370    421    281       O  
-ATOM   2031  OE2 GLU A 492      39.546  -7.654  17.584  1.00 28.73           O  
-ANISOU 2031  OE2 GLU A 492     3366   2742   4808   -611   1260    425       O  
-ATOM   2032  N   GLY A 493      43.189  -4.703  12.990  1.00 13.00           N  
-ANISOU 2032  N   GLY A 493     1481   1343   2113   -315   -256    174       N  
-ATOM   2033  CA  GLY A 493      44.166  -3.995  12.176  1.00 11.76           C  
-ANISOU 2033  CA  GLY A 493     1131   1278   2058   -441   -171    265       C  
-ATOM   2034  C   GLY A 493      45.598  -4.129  12.663  1.00 12.58           C  
-ANISOU 2034  C   GLY A 493     1366   1227   2188   -238   -306    331       C  
-ATOM   2035  O   GLY A 493      46.294  -3.134  12.850  1.00 17.01           O  
-ANISOU 2035  O   GLY A 493     1630   1386   3445   -436   -697    483       O  
-ATOM   2036  N   TYR A 494      46.038  -5.356  12.885  1.00 11.47           N  
-ANISOU 2036  N   TYR A 494     1208   1092   2058   -254   -190    -23       N  
-ATOM   2037  CA  TYR A 494      47.434  -5.635  13.208  1.00 11.14           C  
-ANISOU 2037  CA  TYR A 494     1372   1099   1760   -225   -325   -416       C  
-ATOM   2038  C   TYR A 494      47.725  -7.051  12.744  1.00 11.48           C  
-ANISOU 2038  C   TYR A 494     1441    927   1995   -301   -232   -127       C  
-ATOM   2039  O   TYR A 494      46.804  -7.805  12.397  1.00 13.19           O  
-ANISOU 2039  O   TYR A 494     1383   1058   2571   -259   -323   -451       O  
-ATOM   2040  CB  TYR A 494      47.697  -5.503  14.717  1.00 12.80           C  
-ANISOU 2040  CB  TYR A 494     1687   1520   1656   -346   -241   -191       C  
-ATOM   2041  CG  TYR A 494      47.015  -6.569  15.550  1.00 13.71           C  
-ANISOU 2041  CG  TYR A 494     1890   1703   1617   -443   -258    -70       C  
-ATOM   2042  CD1 TYR A 494      47.714  -7.686  15.989  1.00 15.44           C  
-ANISOU 2042  CD1 TYR A 494     2449   1890   1527   -265     21    101       C  
-ATOM   2043  CD2 TYR A 494      45.673  -6.460  15.898  1.00 15.65           C  
-ANISOU 2043  CD2 TYR A 494     2072   1945   1929   -823   -533    241       C  
-ATOM   2044  CE1 TYR A 494      47.097  -8.670  16.739  1.00 16.81           C  
-ANISOU 2044  CE1 TYR A 494     2613   1978   1794   -526   -139   -133       C  
-ATOM   2045  CE2 TYR A 494      45.047  -7.440  16.654  1.00 16.93           C  
-ANISOU 2045  CE2 TYR A 494     2337   2088   2006   -883   -355    516       C  
-ATOM   2046  CZ  TYR A 494      45.768  -8.539  17.072  1.00 16.70           C  
-ANISOU 2046  CZ  TYR A 494     2708   1969   1668   -996   -255    434       C  
-ATOM   2047  OH  TYR A 494      45.155  -9.522  17.822  1.00 21.38           O  
-ANISOU 2047  OH  TYR A 494     3180   2394   2548   -852   -288    471       O  
-ATOM   2048  N   MET A 495      48.993  -7.433  12.711  1.00 10.87           N  
-ANISOU 2048  N   MET A 495     1374    971   1785     66   -268    -39       N  
-ATOM   2049  CA  MET A 495      49.298  -8.804  12.331  1.00 12.21           C  
-ANISOU 2049  CA  MET A 495     1602   1382   1653    133   -162     97       C  
-ATOM   2050  C   MET A 495      50.225  -9.509  13.305  1.00 10.62           C  
-ANISOU 2050  C   MET A 495     1438   1048   1548     58   -427    -23       C  
-ATOM   2051  O   MET A 495      50.915  -8.875  14.105  1.00 11.16           O  
-ANISOU 2051  O   MET A 495     1387   1062   1790    -93   -396   -170       O  
-ATOM   2052  CB  MET A 495      49.774  -8.930  10.876  1.00 18.28           C  
-ANISOU 2052  CB  MET A 495     2156   2438   2351    522    -92    384       C  
-ATOM   2053  CG  MET A 495      51.179  -8.489  10.611  1.00 18.06           C  
-ANISOU 2053  CG  MET A 495     1957   2264   2641   -117   -259    569       C  
-ATOM   2054  SD  MET A 495      51.688  -8.685   8.869  1.00 12.99           S  
-ANISOU 2054  SD  MET A 495     1814   1304   1816   -375   -220     84       S  
-ATOM   2055  CE  MET A 495      50.779  -7.380   8.037  1.00 16.54           C  
-ANISOU 2055  CE  MET A 495     2113   1616   2553   -233   -482    -61       C  
-ATOM   2056  N   THR A 496      50.195 -10.833  13.259  1.00 11.24           N  
-ANISOU 2056  N   THR A 496     1425    910   1934     47   -231     92       N  
-ATOM   2057  CA  THR A 496      51.032 -11.646  14.118  1.00 10.86           C  
-ANISOU 2057  CA  THR A 496     1501    907   1718    -99   -288   -106       C  
-ATOM   2058  C   THR A 496      51.828 -12.641  13.298  1.00 10.92           C  
-ANISOU 2058  C   THR A 496     1478    969   1702   -263   -419    -85       C  
-ATOM   2059  O   THR A 496      51.541 -12.870  12.114  1.00 11.45           O  
-ANISOU 2059  O   THR A 496     1495   1050   1804   -124   -470   -136       O  
-ATOM   2060  CB  THR A 496      50.205 -12.444  15.122  1.00 12.62           C  
-ANISOU 2060  CB  THR A 496     1629   1038   2126   -441   -104   -417       C  
-ATOM   2061  OG1 THR A 496      49.403 -13.391  14.407  1.00 13.25           O  
-ANISOU 2061  OG1 THR A 496     1756   1054   2222   -346   -250   -125       O  
-ATOM   2062  CG2 THR A 496      49.312 -11.519  15.950  1.00 13.62           C  
-ANISOU 2062  CG2 THR A 496     1766   1212   2197   -375    -61   -136       C  
-ATOM   2063  N   CYS A 497      52.826 -13.228  13.945  1.00 11.95           N  
-ANISOU 2063  N   CYS A 497     1452    881   2208   -108   -426    -26       N  
-ATOM   2064  CA  CYS A 497      53.595 -14.322  13.382  1.00 11.40           C  
-ANISOU 2064  CA  CYS A 497     1661    991   1680   -139   -287    -12       C  
-ATOM   2065  C   CYS A 497      53.970 -15.242  14.529  1.00 11.74           C  
-ANISOU 2065  C   CYS A 497     2011    842   1607   -413   -622    223       C  
-ATOM   2066  O   CYS A 497      53.778 -14.905  15.695  1.00 13.34           O  
-ANISOU 2066  O   CYS A 497     2218   1070   1781   -227   -544    155       O  
-ATOM   2067  CB  CYS A 497      54.880 -13.796  12.742  1.00 13.49           C  
-ANISOU 2067  CB  CYS A 497     1549   1220   2357   -578   -273    165       C  
-ATOM   2068  SG  CYS A 497      56.101 -13.182  13.954  1.00 15.48           S  
-ANISOU 2068  SG  CYS A 497     1854   1130   2898   -463   -755    402       S  
-ATOM   2069  N   VAL A 498      54.511 -16.407  14.200  1.00 12.29           N  
-ANISOU 2069  N   VAL A 498     1901    790   1978   -327   -638    152       N  
-ATOM   2070  CA  VAL A 498      55.250 -17.176  15.185  1.00 14.05           C  
-ANISOU 2070  CA  VAL A 498     2120    868   2348   -342   -659    120       C  
-ATOM   2071  C   VAL A 498      56.719 -16.998  14.824  1.00 14.54           C  
-ANISOU 2071  C   VAL A 498     2260    961   2302   -216   -944     78       C  
-ATOM   2072  O   VAL A 498      57.178 -17.484  13.788  1.00 17.06           O  
-ANISOU 2072  O   VAL A 498     2486   1585   2411    302   -695    -28       O  
-ATOM   2073  CB  VAL A 498      54.855 -18.664  15.193  1.00 15.15           C  
-ANISOU 2073  CB  VAL A 498     2602    978   2177   -284   -713    409       C  
-ATOM   2074  CG1 VAL A 498      55.770 -19.437  16.130  1.00 18.47           C  
-ANISOU 2074  CG1 VAL A 498     3092   1086   2838     38   -952    271       C  
-ATOM   2075  CG2 VAL A 498      53.412 -18.814  15.628  1.00 16.05           C  
-ANISOU 2075  CG2 VAL A 498     2714   1391   1993   -485   -248    220       C  
-ATOM   2076  N   PRO A 499      57.453 -16.248  15.657  1.00 16.17           N  
-ANISOU 2076  N   PRO A 499     2208   1183   2753   -120  -1000    236       N  
-ATOM   2077  CA  PRO A 499      58.823 -15.882  15.302  1.00 18.02           C  
-ANISOU 2077  CA  PRO A 499     2199   1243   3403    -86   -975     59       C  
-ATOM   2078  C   PRO A 499      59.780 -17.029  15.534  1.00 18.92           C  
-ANISOU 2078  C   PRO A 499     2232   1473   3482    -90  -1081    376       C  
-ATOM   2079  O   PRO A 499      59.454 -17.982  16.246  1.00 19.18           O  
-ANISOU 2079  O   PRO A 499     2274   1562   3452     51  -1093    194       O  
-ATOM   2080  CB  PRO A 499      59.137 -14.744  16.278  1.00 19.01           C  
-ANISOU 2080  CB  PRO A 499     2364   1363   3496   -196   -903   -131       C  
-ATOM   2081  CG  PRO A 499      58.318 -15.056  17.474  1.00 19.33           C  
-ANISOU 2081  CG  PRO A 499     2460   1614   3268   -153   -948   -129       C  
-ATOM   2082  CD  PRO A 499      57.040 -15.670  16.949  1.00 16.68           C  
-ANISOU 2082  CD  PRO A 499     2266   1555   2517   -372  -1170   -198       C  
-ATOM   2083  N   ASN A 500      60.950 -16.932  14.919  1.00 19.10           N  
-ANISOU 2083  N   ASN A 500     2237   1696   3322    -62   -983    513       N  
-ATOM   2084  CA  ASN A 500      62.037 -17.844  15.218  1.00 20.49           C  
-ANISOU 2084  CA  ASN A 500     2412   1828   3545     25  -1456    293       C  
-ATOM   2085  C   ASN A 500      61.702 -19.289  14.881  1.00 24.50           C  
-ANISOU 2085  C   ASN A 500     2911   2120   4277     72  -1550    112       C  
-ATOM   2086  O   ASN A 500      62.069 -20.202  15.616  1.00 25.56           O  
-ANISOU 2086  O   ASN A 500     3063   1791   4857     50  -1285    145       O  
-ATOM   2087  CB  ASN A 500      62.423 -17.735  16.694  1.00 21.19           C  
-ANISOU 2087  CB  ASN A 500     2280   2146   3623    138  -1185    671       C  
-ATOM   2088  CG  ASN A 500      63.733 -18.406  16.990  1.00 21.28           C  
-ANISOU 2088  CG  ASN A 500     2327   2107   3652    -78  -1041    447       C  
-ATOM   2089  OD1 ASN A 500      64.615 -18.444  16.136  1.00 20.13           O  
-ANISOU 2089  OD1 ASN A 500     2359   1936   3354   -363  -1186    266       O  
-ATOM   2090  ND2 ASN A 500      63.872 -18.949  18.194  1.00 22.52           N  
-ANISOU 2090  ND2 ASN A 500     2419   2476   3659     60  -1285    184       N  
-ATOM   2091  N   ALA A 501      61.002 -19.491  13.770  1.00 27.86           N  
-ANISOU 2091  N   ALA A 501     3333   2424   4826   -126  -1506   -680       N  
-ATOM   2092  CA  ALA A 501      60.684 -20.834  13.309  1.00 34.88           C  
-ANISOU 2092  CA  ALA A 501     3959   3614   5680    172  -1661  -1056       C  
-ATOM   2093  C   ALA A 501      61.968 -21.585  12.974  1.00 40.48           C  
-ANISOU 2093  C   ALA A 501     4581   4566   6234    391  -1215   -810       C  
-ATOM   2094  O   ALA A 501      62.731 -21.171  12.097  1.00 40.73           O  
-ANISOU 2094  O   ALA A 501     4622   4664   6190    368  -1221   -913       O  
-ATOM   2095  CB  ALA A 501      59.773 -20.776  12.099  1.00 36.62           C  
-ANISOU 2095  CB  ALA A 501     4003   3890   6020    212  -1945  -1342       C  
-ATOM   2096  N   GLY A 502      62.207 -22.682  13.684  1.00 44.46           N  
-ANISOU 2096  N   GLY A 502     5035   5075   6783    364   -880   -371       N  
-ATOM   2097  CA  GLY A 502      63.384 -23.501  13.454  1.00 46.11           C  
-ANISOU 2097  CA  GLY A 502     5435   5436   6647    222   -693   -347       C  
-ATOM   2098  C   GLY A 502      64.623 -23.002  14.175  1.00 46.67           C  
-ANISOU 2098  C   GLY A 502     5864   5683   6184     34   -441   -331       C  
-ATOM   2099  O   GLY A 502      65.739 -23.137  13.666  1.00 46.95           O  
-ANISOU 2099  O   GLY A 502     5891   5773   6173    -33   -165    -45       O  
-ATOM   2100  N   GLY A 503      64.435 -22.428  15.362  1.00 47.06           N  
-ANISOU 2100  N   GLY A 503     6235   5652   5993    -85   -582   -482       N  
-ATOM   2101  CA  GLY A 503      65.558 -21.925  16.134  1.00 49.73           C  
-ANISOU 2101  CA  GLY A 503     6619   5818   6457    -38   -265   -370       C  
-ATOM   2102  C   GLY A 503      66.097 -20.635  15.552  1.00 52.00           C  
-ANISOU 2102  C   GLY A 503     6956   5904   6898     -5    -39   -223       C  
-ATOM   2103  O   GLY A 503      66.564 -19.762  16.286  1.00 53.52           O  
-ANISOU 2103  O   GLY A 503     7107   6181   7048     -8     62   -369       O  
-ATOM   2104  N   GLY A 504      66.055 -20.526  14.228  1.00 53.18           N  
-ANISOU 2104  N   GLY A 504     7086   6060   7058    273     22    181       N  
-ATOM   2105  CA  GLY A 504      66.280 -19.266  13.544  1.00 56.08           C  
-ANISOU 2105  CA  GLY A 504     7321   6362   7623    692     75    519       C  
-ATOM   2106  C   GLY A 504      67.688 -18.701  13.454  1.00 58.47           C  
-ANISOU 2106  C   GLY A 504     7536   6748   7932   1257     52    658       C  
-ATOM   2107  O   GLY A 504      68.032 -17.767  14.181  1.00 60.64           O  
-ANISOU 2107  O   GLY A 504     7589   6962   8487   1350    129    545       O  
-ATOM   2108  N   PRO A 505      68.522 -19.276  12.574  1.00 57.17           N  
-ANISOU 2108  N   PRO A 505     7680   6786   7254   1695   -102    917       N  
-ATOM   2109  CA  PRO A 505      69.673 -18.524  12.071  1.00 55.81           C  
-ANISOU 2109  CA  PRO A 505     7718   6764   6721   1826   -220   1026       C  
-ATOM   2110  C   PRO A 505      69.279 -17.916  10.727  1.00 55.34           C  
-ANISOU 2110  C   PRO A 505     7670   6782   6573   1859   -342    983       C  
-ATOM   2111  O   PRO A 505      70.130 -17.653   9.876  1.00 57.13           O  
-ANISOU 2111  O   PRO A 505     7826   7076   6805   1809   -258    911       O  
-ATOM   2112  CB  PRO A 505      70.748 -19.604  11.877  1.00 56.09           C  
-ANISOU 2112  CB  PRO A 505     7795   6787   6730   1838   -146    999       C  
-ATOM   2113  CG  PRO A 505      70.147 -20.895  12.410  1.00 56.38           C  
-ANISOU 2113  CG  PRO A 505     7814   6841   6768   1854    -94   1077       C  
-ATOM   2114  CD  PRO A 505      68.666 -20.714  12.314  1.00 56.56           C  
-ANISOU 2114  CD  PRO A 505     7770   6760   6959   1833    -84    992       C  
-ATOM   2115  N   GLN A 506      67.977 -17.706  10.552  1.00 52.22           N  
-ANISOU 2115  N   GLN A 506     7379   6340   6121   2102   -729   1005       N  
-ATOM   2116  CA  GLN A 506      67.424 -17.188   9.309  1.00 51.57           C  
-ANISOU 2116  CA  GLN A 506     7097   6074   6421   2157   -930    837       C  
-ATOM   2117  C   GLN A 506      67.025 -15.723   9.447  1.00 45.73           C  
-ANISOU 2117  C   GLN A 506     6400   5442   5532   2101  -1223    951       C  
-ATOM   2118  O   GLN A 506      66.702 -15.257  10.538  1.00 48.61           O  
-ANISOU 2118  O   GLN A 506     6569   5549   6350   2096  -1378   1254       O  
-ATOM   2119  CB  GLN A 506      66.214 -18.027   8.881  1.00 55.03           C  
-ANISOU 2119  CB  GLN A 506     7442   6189   7279   2214   -798    674       C  
-ATOM   2120  CG  GLN A 506      65.503 -18.736  10.036  1.00 58.45           C  
-ANISOU 2120  CG  GLN A 506     7732   6395   8082   2221   -696    436       C  
-ATOM   2121  CD  GLN A 506      64.167 -18.107  10.398  1.00 60.80           C  
-ANISOU 2121  CD  GLN A 506     7992   6495   8613   2173   -732    285       C  
-ATOM   2122  OE1 GLN A 506      63.607 -18.380  11.462  1.00 60.78           O  
-ANISOU 2122  OE1 GLN A 506     8038   6378   8678   2046   -761    382       O  
-ATOM   2123  NE2 GLN A 506      63.644 -17.268   9.509  1.00 62.00           N  
-ANISOU 2123  NE2 GLN A 506     8130   6626   8800   2173   -682    148       N  
-ATOM   2124  N   THR A 507      67.055 -14.999   8.334  1.00 37.51           N  
-ANISOU 2124  N   THR A 507     5533   4755   3964   1919  -1242    783       N  
-ATOM   2125  CA  THR A 507      66.591 -13.616   8.307  1.00 31.96           C  
-ANISOU 2125  CA  THR A 507     4713   3984   3444   1482  -1339    317       C  
-ATOM   2126  C   THR A 507      65.734 -13.402   7.066  1.00 25.48           C  
-ANISOU 2126  C   THR A 507     4074   2860   2747   1245  -1053     54       C  
-ATOM   2127  O   THR A 507      66.135 -13.770   5.967  1.00 27.17           O  
-ANISOU 2127  O   THR A 507     4137   3244   2940   1512   -615    -32       O  
-ATOM   2128  CB  THR A 507      67.775 -12.623   8.293  1.00 34.48           C  
-ANISOU 2128  CB  THR A 507     4804   4287   4010   1152  -1540   -244       C  
-ATOM   2129  OG1 THR A 507      68.473 -12.683   9.544  1.00 37.61           O  
-ANISOU 2129  OG1 THR A 507     4923   4478   4889   1182  -1211    -16       O  
-ATOM   2130  CG2 THR A 507      67.286 -11.204   8.066  1.00 36.24           C  
-ANISOU 2130  CG2 THR A 507     4906   4293   4570    956  -1197   -407       C  
-ATOM   2131  N   LEU A 508      64.549 -12.828   7.240  1.00 20.44           N  
-ANISOU 2131  N   LEU A 508     3414   1479   2873    729   -655    104       N  
-ATOM   2132  CA  LEU A 508      63.695 -12.520   6.097  1.00 16.81           C  
-ANISOU 2132  CA  LEU A 508     2796   1288   2303    322   -702   -161       C  
-ATOM   2133  C   LEU A 508      64.231 -11.279   5.400  1.00 15.77           C  
-ANISOU 2133  C   LEU A 508     2351   1111   2530    430   -246      3       C  
-ATOM   2134  O   LEU A 508      64.765 -10.386   6.052  1.00 15.41           O  
-ANISOU 2134  O   LEU A 508     2110   1356   2389    245   -489     12       O  
-ATOM   2135  CB  LEU A 508      62.260 -12.237   6.540  1.00 17.07           C  
-ANISOU 2135  CB  LEU A 508     2787   1208   2489   -221     -2   -138       C  
-ATOM   2136  CG  LEU A 508      61.427 -13.373   7.123  1.00 19.70           C  
-ANISOU 2136  CG  LEU A 508     3263   1766   2457    -23   -101   -209       C  
-ATOM   2137  CD1 LEU A 508      60.183 -12.814   7.787  1.00 19.60           C  
-ANISOU 2137  CD1 LEU A 508     3204   1978   2266    326   -274   -174       C  
-ATOM   2138  CD2 LEU A 508      61.065 -14.382   6.040  1.00 22.66           C  
-ANISOU 2138  CD2 LEU A 508     3518   2076   3015    -84   -374  -1075       C  
-ATOM   2139  N   PRO A 509      64.083 -11.220   4.071  1.00 15.72           N  
-ANISOU 2139  N   PRO A 509     2441    944   2586    403   -198   -115       N  
-ATOM   2140  CA  PRO A 509      64.436 -10.009   3.334  1.00 14.57           C  
-ANISOU 2140  CA  PRO A 509     2390   1066   2078    476      4     38       C  
-ATOM   2141  C   PRO A 509      63.392  -8.925   3.616  1.00 13.36           C  
-ANISOU 2141  C   PRO A 509     2084   1065   1926    189   -358   -124       C  
-ATOM   2142  O   PRO A 509      62.299  -9.237   4.101  1.00 13.81           O  
-ANISOU 2142  O   PRO A 509     1925   1058   2262    111   -263     32       O  
-ATOM   2143  CB  PRO A 509      64.369 -10.469   1.877  1.00 16.21           C  
-ANISOU 2143  CB  PRO A 509     2713   1399   2045    394    117    -69       C  
-ATOM   2144  CG  PRO A 509      63.309 -11.514   1.888  1.00 16.83           C  
-ANISOU 2144  CG  PRO A 509     2872   1234   2288   -168   -169     48       C  
-ATOM   2145  CD  PRO A 509      63.510 -12.254   3.191  1.00 16.51           C  
-ANISOU 2145  CD  PRO A 509     2888   1208   2175     65   -348    -10       C  
-ATOM   2146  N   ILE A 510      63.719  -7.673   3.315  1.00 12.37           N  
-ANISOU 2146  N   ILE A 510     2046    732   1920    216   -284    -73       N  
-ATOM   2147  CA  ILE A 510      62.809  -6.563   3.605  1.00 12.55           C  
-ANISOU 2147  CA  ILE A 510     1928    821   2019     36   -369   -308       C  
-ATOM   2148  C   ILE A 510      62.028  -6.107   2.374  1.00 12.25           C  
-ANISOU 2148  C   ILE A 510     1830    989   1836    -46    -53    -86       C  
-ATOM   2149  O   ILE A 510      61.231  -5.167   2.453  1.00 12.45           O  
-ANISOU 2149  O   ILE A 510     1781    950   1998     55    121   -194       O  
-ATOM   2150  CB  ILE A 510      63.544  -5.343   4.204  1.00 12.70           C  
-ANISOU 2150  CB  ILE A 510     2024    966   1834   -288   -312    172       C  
-ATOM   2151  CG1 ILE A 510      64.509  -4.743   3.183  1.00 15.03           C  
-ANISOU 2151  CG1 ILE A 510     2131   1026   2554   -438   -270     43       C  
-ATOM   2152  CG2 ILE A 510      64.251  -5.735   5.490  1.00 14.69           C  
-ANISOU 2152  CG2 ILE A 510     2337   1246   1997      7   -590     14       C  
-ATOM   2153  CD1 ILE A 510      65.070  -3.404   3.619  1.00 18.56           C  
-ANISOU 2153  CD1 ILE A 510     2371   1771   2911   -515   -461    297       C  
-ATOM   2154  N   ASN A 511      62.257  -6.770   1.240  1.00 11.74           N  
-ANISOU 2154  N   ASN A 511     1700   1032   1729   -116   -299    153       N  
-ATOM   2155  CA  ASN A 511      61.632  -6.368  -0.017  1.00 12.23           C  
-ANISOU 2155  CA  ASN A 511     1858   1143   1645    -10   -137     68       C  
-ATOM   2156  C   ASN A 511      60.558  -7.341  -0.509  1.00 11.22           C  
-ANISOU 2156  C   ASN A 511     1715    814   1734   -132   -262     22       C  
-ATOM   2157  O   ASN A 511      60.225  -7.363  -1.692  1.00 13.20           O  
-ANISOU 2157  O   ASN A 511     2121   1143   1750    142   -156     41       O  
-ATOM   2158  CB  ASN A 511      62.685  -6.137  -1.105  1.00 14.45           C  
-ANISOU 2158  CB  ASN A 511     2068   1415   2008    180     -7    -65       C  
-ATOM   2159  CG  ASN A 511      63.400  -7.412  -1.505  1.00 15.95           C  
-ANISOU 2159  CG  ASN A 511     2294   1953   1813    435    358    284       C  
-ATOM   2160  OD1 ASN A 511      63.348  -8.412  -0.791  1.00 15.33           O  
-ANISOU 2160  OD1 ASN A 511     2387   1479   1959    531    213    100       O  
-ATOM   2161  ND2 ASN A 511      64.065  -7.386  -2.655  1.00 21.29           N  
-ANISOU 2161  ND2 ASN A 511     2754   2668   2667    795    637    299       N  
-ATOM   2162  N   GLY A 512      60.014  -8.137   0.406  1.00 11.59           N  
-ANISOU 2162  N   GLY A 512     1518    698   2186    -88    -63   -177       N  
-ATOM   2163  CA  GLY A 512      58.928  -9.039   0.069  1.00 11.80           C  
-ANISOU 2163  CA  GLY A 512     1615    824   2045    -65   -280   -119       C  
-ATOM   2164  C   GLY A 512      57.605  -8.306  -0.071  1.00 11.90           C  
-ANISOU 2164  C   GLY A 512     1712    936   1871    -29   -262    -78       C  
-ATOM   2165  O   GLY A 512      57.479  -7.130   0.285  1.00 12.66           O  
-ANISOU 2165  O   GLY A 512     1936    838   2034    -14   -206   -100       O  
-ATOM   2166  N   VAL A 513      56.612  -9.027  -0.575  1.00 11.06           N  
-ANISOU 2166  N   VAL A 513     1729    969   1503   -120    -18    -62       N  
-ATOM   2167  CA  VAL A 513      55.282  -8.491  -0.821  1.00 11.58           C  
-ANISOU 2167  CA  VAL A 513     1721   1065   1612   -152   -135    198       C  
-ATOM   2168  C   VAL A 513      54.275  -9.314  -0.029  1.00 10.38           C  
-ANISOU 2168  C   VAL A 513     1813    776   1355    -30    -41   -110       C  
-ATOM   2169  O   VAL A 513      54.293 -10.539  -0.105  1.00 11.80           O  
-ANISOU 2169  O   VAL A 513     2109    738   1636     38    -98   -172       O  
-ATOM   2170  CB  VAL A 513      54.932  -8.559  -2.326  1.00 12.39           C  
-ANISOU 2170  CB  VAL A 513     1894   1337   1476   -222   -126    474       C  
-ATOM   2171  CG1 VAL A 513      53.497  -8.135  -2.557  1.00 15.57           C  
-ANISOU 2171  CG1 VAL A 513     1863   2129   1924   -225   -440    408       C  
-ATOM   2172  CG2 VAL A 513      55.891  -7.681  -3.138  1.00 13.69           C  
-ANISOU 2172  CG2 VAL A 513     2338   1430   1431   -200     83    257       C  
-ATOM   2173  N   PHE A 514      53.421  -8.656   0.750  1.00 10.17           N  
-ANISOU 2173  N   PHE A 514     1458    816   1591   -116    -28      2       N  
-ATOM   2174  CA  PHE A 514      52.353  -9.371   1.443  1.00 10.12           C  
-ANISOU 2174  CA  PHE A 514     1434    849   1563   -329    -98     42       C  
-ATOM   2175  C   PHE A 514      51.233  -9.676   0.462  1.00 10.41           C  
-ANISOU 2175  C   PHE A 514     1703    764   1487   -149   -356    -49       C  
-ATOM   2176  O   PHE A 514      50.822  -8.812  -0.315  1.00 11.49           O  
-ANISOU 2176  O   PHE A 514     1578   1029   1757     -4   -266    112       O  
-ATOM   2177  CB  PHE A 514      51.812  -8.588   2.646  1.00 10.85           C  
-ANISOU 2177  CB  PHE A 514     1597    818   1706   -184     19   -384       C  
-ATOM   2178  CG  PHE A 514      52.818  -8.388   3.740  1.00 10.38           C  
-ANISOU 2178  CG  PHE A 514     1368    922   1652   -247   -338    -70       C  
-ATOM   2179  CD1 PHE A 514      52.953  -9.333   4.747  1.00 10.71           C  
-ANISOU 2179  CD1 PHE A 514     1510    913   1646   -110   -180     83       C  
-ATOM   2180  CD2 PHE A 514      53.628  -7.258   3.765  1.00 11.85           C  
-ANISOU 2180  CD2 PHE A 514     1313    870   2319   -108   -167   -329       C  
-ATOM   2181  CE1 PHE A 514      53.881  -9.168   5.758  1.00 12.62           C  
-ANISOU 2181  CE1 PHE A 514     1612   1410   1772    -27   -563   -380       C  
-ATOM   2182  CE2 PHE A 514      54.564  -7.086   4.772  1.00 12.26           C  
-ANISOU 2182  CE2 PHE A 514     1552   1022   2085     87   -353   -141       C  
-ATOM   2183  CZ  PHE A 514      54.690  -8.046   5.771  1.00 11.83           C  
-ANISOU 2183  CZ  PHE A 514     1599    996   1899    -63   -204   -372       C  
-ATOM   2184  N   VAL A 515      50.751 -10.917   0.504  1.00 11.29           N  
-ANISOU 2184  N   VAL A 515     1798    954   1537   -263   -336   -157       N  
-ATOM   2185  CA  VAL A 515      49.641 -11.343  -0.331  1.00 12.15           C  
-ANISOU 2185  CA  VAL A 515     2008   1028   1581   -364   -147    -33       C  
-ATOM   2186  C   VAL A 515      48.565 -12.006   0.526  1.00 11.63           C  
-ANISOU 2186  C   VAL A 515     1758    947   1712   -284   -428    117       C  
-ATOM   2187  O   VAL A 515      48.839 -12.938   1.287  1.00 12.26           O  
-ANISOU 2187  O   VAL A 515     1890    996   1770    -43   -364    138       O  
-ATOM   2188  CB  VAL A 515      50.102 -12.345  -1.413  1.00 14.50           C  
-ANISOU 2188  CB  VAL A 515     2234   1690   1585   -690   -259   -146       C  
-ATOM   2189  CG1 VAL A 515      48.927 -12.774  -2.283  1.00 16.78           C  
-ANISOU 2189  CG1 VAL A 515     2431   2112   1831   -544   -457   -175       C  
-ATOM   2190  CG2 VAL A 515      51.207 -11.745  -2.267  1.00 15.79           C  
-ANISOU 2190  CG2 VAL A 515     2332   2019   1649   -423    -70    -95       C  
-ATOM   2191  N   PHE A 516      47.337 -11.517   0.408  1.00 11.36           N  
-ANISOU 2191  N   PHE A 516     1702   1089   1525   -579   -278     71       N  
-ATOM   2192  CA  PHE A 516      46.198 -12.149   1.054  1.00 12.16           C  
-ANISOU 2192  CA  PHE A 516     1738   1018   1865   -526   -302    -13       C  
-ATOM   2193  C   PHE A 516      45.878 -13.507   0.418  1.00 13.15           C  
-ANISOU 2193  C   PHE A 516     2081   1078   1838   -441   -303    363       C  
-ATOM   2194  O   PHE A 516      45.632 -13.603  -0.788  1.00 15.29           O  
-ANISOU 2194  O   PHE A 516     2443   1576   1789   -706   -533    169       O  
-ATOM   2195  CB  PHE A 516      44.983 -11.224   0.989  1.00 13.82           C  
-ANISOU 2195  CB  PHE A 516     1610   1171   2470   -374   -210    400       C  
-ATOM   2196  CG  PHE A 516      43.715 -11.848   1.496  1.00 13.14           C  
-ANISOU 2196  CG  PHE A 516     1802   1223   1968   -267   -519     46       C  
-ATOM   2197  CD1 PHE A 516      43.598 -12.236   2.822  1.00 14.01           C  
-ANISOU 2197  CD1 PHE A 516     1798   1133   2390   -597   -213    183       C  
-ATOM   2198  CD2 PHE A 516      42.631 -12.035   0.648  1.00 14.39           C  
-ANISOU 2198  CD2 PHE A 516     1685   1449   2334   -628   -428    222       C  
-ATOM   2199  CE1 PHE A 516      42.423 -12.802   3.298  1.00 13.52           C  
-ANISOU 2199  CE1 PHE A 516     1960   1153   2022   -584   -595   -109       C  
-ATOM   2200  CE2 PHE A 516      41.452 -12.602   1.112  1.00 15.13           C  
-ANISOU 2200  CE2 PHE A 516     2018   1530   2200   -466   -619    242       C  
-ATOM   2201  CZ  PHE A 516      41.349 -12.988   2.439  1.00 14.12           C  
-ANISOU 2201  CZ  PHE A 516     2058   1314   1991   -535   -479     43       C  
-ATOM   2202  N   ILE A 517      45.899 -14.548   1.245  1.00 11.75           N  
-ANISOU 2202  N   ILE A 517     2114    916   1433   -553   -483     53       N  
-ATOM   2203  CA  ILE A 517      45.601 -15.912   0.807  1.00 13.37           C  
-ANISOU 2203  CA  ILE A 517     2282   1031   1768   -417   -645    -91       C  
-ATOM   2204  C   ILE A 517      44.122 -16.230   1.007  1.00 14.19           C  
-ANISOU 2204  C   ILE A 517     2336   1311   1744   -408   -573     91       C  
-ATOM   2205  O   ILE A 517      43.418 -16.575   0.056  1.00 16.77           O  
-ANISOU 2205  O   ILE A 517     2387   1832   2153   -587   -680   -179       O  
-ATOM   2206  CB  ILE A 517      46.457 -16.945   1.579  1.00 14.53           C  
-ANISOU 2206  CB  ILE A 517     2305    915   2299   -484   -411   -103       C  
-ATOM   2207  CG1 ILE A 517      47.947 -16.625   1.426  1.00 14.57           C  
-ANISOU 2207  CG1 ILE A 517     2526   1254   1756   -308    -68   -194       C  
-ATOM   2208  CG2 ILE A 517      46.125 -18.372   1.133  1.00 16.00           C  
-ANISOU 2208  CG2 ILE A 517     2613    905   2561   -208   -554   -226       C  
-ATOM   2209  CD1 ILE A 517      48.417 -16.547  -0.015  1.00 15.63           C  
-ANISOU 2209  CD1 ILE A 517     2505   1361   2073   -133   -190   -233       C  
-ATOM   2210  N   SER A 518      43.656 -16.118   2.245  1.00 13.77           N  
-ANISOU 2210  N   SER A 518     2031   1212   1989   -758   -489    293       N  
-ATOM   2211  CA  SER A 518      42.256 -16.382   2.557  1.00 14.91           C  
-ANISOU 2211  CA  SER A 518     2217   1168   2281   -800   -211    140       C  
-ATOM   2212  C   SER A 518      41.940 -15.989   3.984  1.00 13.91           C  
-ANISOU 2212  C   SER A 518     1973   1224   2087   -771   -334     41       C  
-ATOM   2213  O   SER A 518      42.842 -15.780   4.795  1.00 13.80           O  
-ANISOU 2213  O   SER A 518     1941   1258   2044   -578   -657    -35       O  
-ATOM   2214  CB  SER A 518      41.936 -17.867   2.383  1.00 19.20           C  
-ANISOU 2214  CB  SER A 518     2954   1551   2791   -385   -298    239       C  
-ATOM   2215  OG  SER A 518      42.462 -18.601   3.470  1.00 19.28           O  
-ANISOU 2215  OG  SER A 518     3490   1306   2527   -117   -155   -111       O  
-ATOM   2216  N   TRP A 519      40.653 -15.895   4.288  1.00 14.01           N  
-ANISOU 2216  N   TRP A 519     1972   1357   1993   -822   -489    203       N  
-ATOM   2217  CA  TRP A 519      40.208 -15.817   5.667  1.00 13.56           C  
-ANISOU 2217  CA  TRP A 519     1745   1486   1922   -836   -380    458       C  
-ATOM   2218  C   TRP A 519      40.405 -17.197   6.294  1.00 15.06           C  
-ANISOU 2218  C   TRP A 519     1959   1502   2259   -901   -464    211       C  
-ATOM   2219  O   TRP A 519      40.169 -18.220   5.639  1.00 16.59           O  
-ANISOU 2219  O   TRP A 519     2374   1362   2565   -407   -791    107       O  
-ATOM   2220  CB  TRP A 519      38.735 -15.396   5.721  1.00 15.84           C  
-ANISOU 2220  CB  TRP A 519     1709   1541   2769   -774   -507    184       C  
-ATOM   2221  CG  TRP A 519      38.523 -13.997   5.203  1.00 15.32           C  
-ANISOU 2221  CG  TRP A 519     1756   1418   2645   -551   -646    365       C  
-ATOM   2222  CD1 TRP A 519      38.013 -13.632   3.989  1.00 16.35           C  
-ANISOU 2222  CD1 TRP A 519     1892   1383   2937   -243   -616      0       C  
-ATOM   2223  CD2 TRP A 519      38.839 -12.782   5.889  1.00 14.50           C  
-ANISOU 2223  CD2 TRP A 519     1659   1364   2485   -668   -206    315       C  
-ATOM   2224  NE1 TRP A 519      37.991 -12.260   3.879  1.00 16.37           N  
-ANISOU 2224  NE1 TRP A 519     1835   1412   2974   -252   -492     53       N  
-ATOM   2225  CE2 TRP A 519      38.485 -11.715   5.034  1.00 15.69           C  
-ANISOU 2225  CE2 TRP A 519     1699   1496   2765   -633   -457    170       C  
-ATOM   2226  CE3 TRP A 519      39.385 -12.493   7.144  1.00 15.02           C  
-ANISOU 2226  CE3 TRP A 519     1629   1554   2524   -510   -250   -116       C  
-ATOM   2227  CZ2 TRP A 519      38.664 -10.379   5.399  1.00 16.28           C  
-ANISOU 2227  CZ2 TRP A 519     1712   1661   2812   -525   -465    110       C  
-ATOM   2228  CZ3 TRP A 519      39.557 -11.171   7.504  1.00 15.39           C  
-ANISOU 2228  CZ3 TRP A 519     1652   1499   2697   -448   -433    -16       C  
-ATOM   2229  CH2 TRP A 519      39.199 -10.129   6.635  1.00 17.39           C  
-ANISOU 2229  CH2 TRP A 519     1724   1808   3075   -285   -434    469       C  
-ATOM   2230  N   VAL A 520      40.881 -17.222   7.537  1.00 14.68           N  
-ANISOU 2230  N   VAL A 520     1876   1613   2088   -878   -480    426       N  
-ATOM   2231  CA  VAL A 520      41.125 -18.472   8.244  1.00 15.42           C  
-ANISOU 2231  CA  VAL A 520     1992   1736   2132   -736   -492    586       C  
-ATOM   2232  C   VAL A 520      40.592 -18.350   9.660  1.00 16.02           C  
-ANISOU 2232  C   VAL A 520     2044   1699   2345   -847   -667    639       C  
-ATOM   2233  O   VAL A 520      40.348 -17.242  10.144  1.00 15.90           O  
-ANISOU 2233  O   VAL A 520     2064   1554   2421   -731   -411    428       O  
-ATOM   2234  CB  VAL A 520      42.625 -18.852   8.275  1.00 14.80           C  
-ANISOU 2234  CB  VAL A 520     2035   1502   2085   -940   -415    202       C  
-ATOM   2235  CG1 VAL A 520      43.151 -19.095   6.867  1.00 15.52           C  
-ANISOU 2235  CG1 VAL A 520     2369   1423   2104   -595   -581    411       C  
-ATOM   2236  CG2 VAL A 520      43.453 -17.780   9.000  1.00 16.12           C  
-ANISOU 2236  CG2 VAL A 520     2058   1658   2409   -942   -247    298       C  
-ATOM   2237  N   SER A 521      40.406 -19.480  10.334  1.00 16.37           N  
-ANISOU 2237  N   SER A 521     2174   1767   2279   -955   -372    716       N  
-ATOM   2238  CA  SER A 521      39.920 -19.420  11.701  1.00 18.25           C  
-ANISOU 2238  CA  SER A 521     2370   2000   2563   -942   -366    608       C  
-ATOM   2239  C   SER A 521      41.042 -18.991  12.641  1.00 16.48           C  
-ANISOU 2239  C   SER A 521     2053   1878   2330   -722    142    857       C  
-ATOM   2240  O   SER A 521      42.231 -19.040  12.284  1.00 14.85           O  
-ANISOU 2240  O   SER A 521     2091   1388   2162   -595    -65    594       O  
-ATOM   2241  CB  SER A 521      39.297 -20.750  12.126  1.00 24.50           C  
-ANISOU 2241  CB  SER A 521     2888   2144   4275   -807   -832    587       C  
-ATOM   2242  OG  SER A 521      40.167 -21.520  12.924  1.00 23.39           O  
-ANISOU 2242  OG  SER A 521     2817   1838   4233   -802  -1200    136       O  
-ATOM   2243  N   ARG A 522      40.670 -18.550  13.834  1.00 16.39           N  
-ANISOU 2243  N   ARG A 522     2199   1614   2412   -789     31    454       N  
-ATOM   2244  CA  ARG A 522      41.657 -18.131  14.823  1.00 15.81           C  
-ANISOU 2244  CA  ARG A 522     2351   1433   2224   -770    169    298       C  
-ATOM   2245  C   ARG A 522      42.601 -19.272  15.180  1.00 13.48           C  
-ANISOU 2245  C   ARG A 522     2377   1143   1602   -573   -166     13       C  
-ATOM   2246  O   ARG A 522      43.692 -19.032  15.684  1.00 14.50           O  
-ANISOU 2246  O   ARG A 522     2338   1166   2006   -595   -220    -13       O  
-ATOM   2247  CB  ARG A 522      40.963 -17.615  16.082  1.00 18.66           C  
-ANISOU 2247  CB  ARG A 522     2637   1816   2636   -494    489    431       C  
-ATOM   2248  CG  ARG A 522      40.036 -18.623  16.747  1.00 21.78           C  
-ANISOU 2248  CG  ARG A 522     2976   2252   3047   -357   1322    564       C  
-ATOM   2249  CD  ARG A 522      39.076 -17.906  17.691  1.00 26.69           C  
-ANISOU 2249  CD  ARG A 522     3551   2726   3863    -78   1900    729       C  
-ATOM   2250  NE  ARG A 522      38.100 -18.811  18.291  1.00 33.00           N  
-ANISOU 2250  NE  ARG A 522     3932   3383   5222    216   1781    571       N  
-ATOM   2251  CZ  ARG A 522      36.913 -19.094  17.760  1.00 35.73           C  
-ANISOU 2251  CZ  ARG A 522     4132   3451   5991    259   2081    915       C  
-ATOM   2252  NH1 ARG A 522      36.552 -18.545  16.608  1.00 36.31           N  
-ANISOU 2252  NH1 ARG A 522     4236   3641   5918    570   1873    882       N  
-ATOM   2253  NH2 ARG A 522      36.087 -19.931  18.380  1.00 36.48           N  
-ANISOU 2253  NH2 ARG A 522     4154   3164   6542    113   2486    816       N  
-ATOM   2254  N   TYR A 523      42.169 -20.510  14.922  1.00 14.26           N  
-ANISOU 2254  N   TYR A 523     2304   1296   1818   -744   -273    135       N  
-ATOM   2255  CA  TYR A 523      42.953 -21.695  15.264  1.00 14.26           C  
-ANISOU 2255  CA  TYR A 523     2322   1158   1938   -778    -32    243       C  
-ATOM   2256  C   TYR A 523      44.018 -22.055  14.234  1.00 13.36           C  
-ANISOU 2256  C   TYR A 523     2290   1376   1408   -591     21    293       C  
-ATOM   2257  O   TYR A 523      44.811 -22.967  14.457  1.00 14.62           O  
-ANISOU 2257  O   TYR A 523     2342   1307   1906   -521    -54    305       O  
-ATOM   2258  CB  TYR A 523      42.030 -22.891  15.536  1.00 14.72           C  
-ANISOU 2258  CB  TYR A 523     2512   1192   1888   -819     52    186       C  
-ATOM   2259  CG  TYR A 523      41.131 -22.651  16.725  1.00 15.87           C  
-ANISOU 2259  CG  TYR A 523     2839   1424   1766   -745    277    194       C  
-ATOM   2260  CD1 TYR A 523      41.622 -22.766  18.020  1.00 17.30           C  
-ANISOU 2260  CD1 TYR A 523     3149   1746   1679   -537    330    291       C  
-ATOM   2261  CD2 TYR A 523      39.810 -22.266  16.558  1.00 16.73           C  
-ANISOU 2261  CD2 TYR A 523     2951   1379   2027   -841    235     72       C  
-ATOM   2262  CE1 TYR A 523      40.816 -22.529  19.112  1.00 18.84           C  
-ANISOU 2262  CE1 TYR A 523     3287   2196   1674   -587    652    113       C  
-ATOM   2263  CE2 TYR A 523      38.993 -22.022  17.653  1.00 17.91           C  
-ANISOU 2263  CE2 TYR A 523     3063   1415   2326   -771    750    118       C  
-ATOM   2264  CZ  TYR A 523      39.507 -22.152  18.925  1.00 20.09           C  
-ANISOU 2264  CZ  TYR A 523     3332   1893   2408   -891    967     72       C  
-ATOM   2265  OH  TYR A 523      38.719 -21.911  20.025  1.00 23.87           O  
-ANISOU 2265  OH  TYR A 523     3804   2315   2951   -799   1080   -196       O  
-ATOM   2266  N   TYR A 524      44.044 -21.341  13.112  1.00 13.06           N  
-ANISOU 2266  N   TYR A 524     2087   1353   1523   -894     77     37       N  
-ATOM   2267  CA  TYR A 524      45.067 -21.585  12.098  1.00 12.67           C  
-ANISOU 2267  CA  TYR A 524     2007   1425   1383   -583   -170    415       C  
-ATOM   2268  C   TYR A 524      46.448 -21.489  12.748  1.00 13.21           C  
-ANISOU 2268  C   TYR A 524     1936   1456   1627   -445   -236    255       C  
-ATOM   2269  O   TYR A 524      46.796 -20.472  13.352  1.00 14.35           O  
-ANISOU 2269  O   TYR A 524     1880   1279   2293   -579   -407   -211       O  
-ATOM   2270  CB  TYR A 524      44.943 -20.578  10.952  1.00 13.21           C  
-ANISOU 2270  CB  TYR A 524     2099   1287   1633   -374    -26    560       C  
-ATOM   2271  CG  TYR A 524      45.851 -20.858   9.775  1.00 12.50           C  
-ANISOU 2271  CG  TYR A 524     2012   1155   1581   -379    -59    399       C  
-ATOM   2272  CD1 TYR A 524      45.354 -21.460   8.621  1.00 12.91           C  
-ANISOU 2272  CD1 TYR A 524     2200   1004   1700   -253   -324    175       C  
-ATOM   2273  CD2 TYR A 524      47.202 -20.513   9.808  1.00 13.49           C  
-ANISOU 2273  CD2 TYR A 524     1989   1061   2076   -361     71    315       C  
-ATOM   2274  CE1 TYR A 524      46.173 -21.718   7.539  1.00 13.59           C  
-ANISOU 2274  CE1 TYR A 524     2100   1100   1961   -146   -184    202       C  
-ATOM   2275  CE2 TYR A 524      48.031 -20.764   8.727  1.00 12.96           C  
-ANISOU 2275  CE2 TYR A 524     2140   1053   1732   -240   -139    135       C  
-ATOM   2276  CZ  TYR A 524      47.510 -21.370   7.593  1.00 13.06           C  
-ANISOU 2276  CZ  TYR A 524     2220   1081   1661   -132    133    286       C  
-ATOM   2277  OH  TYR A 524      48.317 -21.636   6.508  1.00 13.51           O  
-ANISOU 2277  OH  TYR A 524     2244    896   1993   -239   -333     71       O  
-ATOM   2278  N   GLN A 525      47.233 -22.552  12.629  1.00 12.41           N  
-ANISOU 2278  N   GLN A 525     2128   1109   1477   -564   -410    271       N  
-ATOM   2279  CA  GLN A 525      48.507 -22.638  13.333  1.00 12.49           C  
-ANISOU 2279  CA  GLN A 525     2322   1007   1416   -332   -476     89       C  
-ATOM   2280  C   GLN A 525      49.682 -22.219  12.452  1.00 12.26           C  
-ANISOU 2280  C   GLN A 525     2290    978   1390   -521   -326    191       C  
-ATOM   2281  O   GLN A 525      49.965 -22.855  11.433  1.00 13.25           O  
-ANISOU 2281  O   GLN A 525     2205   1038   1792   -682   -315    -57       O  
-ATOM   2282  CB  GLN A 525      48.730 -24.073  13.816  1.00 16.77           C  
-ANISOU 2282  CB  GLN A 525     2645   1252   2473   -358   -646    290       C  
-ATOM   2283  CG  GLN A 525      49.945 -24.218  14.694  1.00 23.68           C  
-ANISOU 2283  CG  GLN A 525     3668   1994   3333    -39    -58    397       C  
-ATOM   2284  CD  GLN A 525      49.833 -23.403  15.961  1.00 26.45           C  
-ANISOU 2284  CD  GLN A 525     4389   2105   3555   -120   -298    199       C  
-ATOM   2285  OE1 GLN A 525      49.072 -23.749  16.867  1.00 28.16           O  
-ANISOU 2285  OE1 GLN A 525     4488   3099   3113    350   -447   -179       O  
-ATOM   2286  NE2 GLN A 525      50.586 -22.310  16.032  1.00 28.04           N  
-ANISOU 2286  NE2 GLN A 525     4942   1950   3760   -282     33    696       N  
-ATOM   2287  N   LEU A 526      50.361 -21.139  12.831  1.00 13.06           N  
-ANISOU 2287  N   LEU A 526     2165    954   1844   -625   -302    165       N  
-ATOM   2288  CA  LEU A 526      51.528 -20.688  12.088  1.00 13.22           C  
-ANISOU 2288  CA  LEU A 526     2096    933   1992   -571   -329     69       C  
-ATOM   2289  C   LEU A 526      52.756 -21.492  12.489  1.00 14.36           C  
-ANISOU 2289  C   LEU A 526     2313   1377   1766    -44   -118    207       C  
-ATOM   2290  O   LEU A 526      52.839 -21.979  13.625  1.00 14.70           O  
-ANISOU 2290  O   LEU A 526     2232   1287   2065   -409   -214    295       O  
-ATOM   2291  CB  LEU A 526      51.771 -19.203  12.335  1.00 13.67           C  
-ANISOU 2291  CB  LEU A 526     2191    910   2093   -543   -385     34       C  
-ATOM   2292  CG  LEU A 526      50.634 -18.263  11.930  1.00 12.96           C  
-ANISOU 2292  CG  LEU A 526     2117    916   1890   -301   -629   -113       C  
-ATOM   2293  CD1 LEU A 526      50.929 -16.848  12.434  1.00 14.50           C  
-ANISOU 2293  CD1 LEU A 526     2041    939   2528   -413   -443   -198       C  
-ATOM   2294  CD2 LEU A 526      50.461 -18.266  10.427  1.00 15.57           C  
-ANISOU 2294  CD2 LEU A 526     2457   1682   1775    -42   -378     -4       C  
-ATOM   2295  OXT LEU A 526      53.676 -21.681  11.681  1.00 15.36           O  
-ANISOU 2295  OXT LEU A 526     2492   1451   1891     24   -356     85       O  
-TER    2296      LEU A 526                                                      
-ATOM   2297  N   LYS B 230      42.856  -7.282 -14.969  1.00 43.62           N  
-ANISOU 2297  N   LYS B 230     6505   3793   6276    -57    400   1370       N  
-ATOM   2298  CA  LYS B 230      42.488  -6.416 -13.854  1.00 41.60           C  
-ANISOU 2298  CA  LYS B 230     6496   3578   5733     37    162   1129       C  
-ATOM   2299  C   LYS B 230      41.894  -5.102 -14.352  1.00 36.56           C  
-ANISOU 2299  C   LYS B 230     6079   3041   4772   -257   -140    775       C  
-ATOM   2300  O   LYS B 230      42.518  -4.397 -15.142  1.00 34.53           O  
-ANISOU 2300  O   LYS B 230     6080   2926   4112   -362    157    595       O  
-ATOM   2301  CB  LYS B 230      43.700  -6.152 -12.957  1.00 44.64           C  
-ANISOU 2301  CB  LYS B 230     6803   3945   6213    248    264   1278       C  
-ATOM   2302  CG  LYS B 230      43.469  -5.094 -11.885  1.00 46.92           C  
-ANISOU 2302  CG  LYS B 230     7081   4199   6546    570    342   1223       C  
-ATOM   2303  CD  LYS B 230      43.974  -5.558 -10.526  1.00 50.57           C  
-ANISOU 2303  CD  LYS B 230     7322   4682   7209    683    368   1208       C  
-ATOM   2304  CE  LYS B 230      45.388  -6.111 -10.614  1.00 53.46           C  
-ANISOU 2304  CE  LYS B 230     7530   4947   7836    783    437   1505       C  
-ATOM   2305  NZ  LYS B 230      45.980  -6.367  -9.269  1.00 55.67           N  
-ANISOU 2305  NZ  LYS B 230     7643   5133   8376    848    434   1437       N  
-ATOM   2306  N   PRO B 231      40.676  -4.779 -13.894  1.00 33.71           N  
-ANISOU 2306  N   PRO B 231     5641   2676   4491   -451   -715    309       N  
-ATOM   2307  CA  PRO B 231      39.963  -3.567 -14.314  1.00 30.57           C  
-ANISOU 2307  CA  PRO B 231     5304   2531   3781   -565  -1061   -226       C  
-ATOM   2308  C   PRO B 231      40.620  -2.299 -13.777  1.00 27.70           C  
-ANISOU 2308  C   PRO B 231     4844   2336   3345   -417  -1037   -200       C  
-ATOM   2309  O   PRO B 231      41.072  -2.255 -12.632  1.00 29.16           O  
-ANISOU 2309  O   PRO B 231     5039   2468   3572   -228  -1068    -30       O  
-ATOM   2310  CB  PRO B 231      38.571  -3.740 -13.692  1.00 33.12           C  
-ANISOU 2310  CB  PRO B 231     5463   2589   4531   -621  -1128   -473       C  
-ATOM   2311  CG  PRO B 231      38.457  -5.200 -13.383  1.00 35.88           C  
-ANISOU 2311  CG  PRO B 231     5611   2904   5117   -329   -986     68       C  
-ATOM   2312  CD  PRO B 231      39.846  -5.626 -13.023  1.00 36.07           C  
-ANISOU 2312  CD  PRO B 231     5614   2964   5125   -427   -893    251       C  
-ATOM   2313  N   PHE B 232      40.660  -1.267 -14.608  1.00 23.09           N  
-ANISOU 2313  N   PHE B 232     4176   1972   2624   -561   -861   -130       N  
-ATOM   2314  CA  PHE B 232      41.225   0.008 -14.198  1.00 21.82           C  
-ANISOU 2314  CA  PHE B 232     3564   2187   2540   -369   -798   -151       C  
-ATOM   2315  C   PHE B 232      40.334   0.695 -13.168  1.00 20.21           C  
-ANISOU 2315  C   PHE B 232     3201   2288   2190   -455  -1000     48       C  
-ATOM   2316  O   PHE B 232      39.118   0.525 -13.174  1.00 22.02           O  
-ANISOU 2316  O   PHE B 232     3136   2330   2900   -798  -1311     44       O  
-ATOM   2317  CB  PHE B 232      41.423   0.909 -15.417  1.00 20.51           C  
-ANISOU 2317  CB  PHE B 232     3244   2224   2325   -101   -712    295       C  
-ATOM   2318  CG  PHE B 232      42.031   2.240 -15.093  1.00 18.98           C  
-ANISOU 2318  CG  PHE B 232     2814   2193   2202   -549   -600   -164       C  
-ATOM   2319  CD1 PHE B 232      43.373   2.336 -14.752  1.00 18.70           C  
-ANISOU 2319  CD1 PHE B 232     2659   2452   1993   -487   -302    241       C  
-ATOM   2320  CD2 PHE B 232      41.269   3.394 -15.134  1.00 18.75           C  
-ANISOU 2320  CD2 PHE B 232     2698   2266   2161   -396   -593     68       C  
-ATOM   2321  CE1 PHE B 232      43.944   3.564 -14.451  1.00 19.31           C  
-ANISOU 2321  CE1 PHE B 232     2671   2739   1927   -188   -289    230       C  
-ATOM   2322  CE2 PHE B 232      41.832   4.626 -14.836  1.00 18.41           C  
-ANISOU 2322  CE2 PHE B 232     2642   2111   2243   -626   -305    -20       C  
-ATOM   2323  CZ  PHE B 232      43.171   4.712 -14.496  1.00 18.29           C  
-ANISOU 2323  CZ  PHE B 232     2566   2491   1892   -566   -505    -26       C  
-ATOM   2324  N   SER B 233      40.951   1.454 -12.269  1.00 17.85           N  
-ANISOU 2324  N   SER B 233     2833   1943   2006   -388   -677    -15       N  
-ATOM   2325  CA  SER B 233      40.214   2.268 -11.315  1.00 17.17           C  
-ANISOU 2325  CA  SER B 233     2375   1870   2280   -660   -541    314       C  
-ATOM   2326  C   SER B 233      41.106   3.389 -10.828  1.00 14.86           C  
-ANISOU 2326  C   SER B 233     2010   1619   2018   -787   -475    213       C  
-ATOM   2327  O   SER B 233      42.328   3.342 -11.007  1.00 15.90           O  
-ANISOU 2327  O   SER B 233     1922   1969   2150   -309   -461     56       O  
-ATOM   2328  CB  SER B 233      39.753   1.442 -10.114  1.00 18.64           C  
-ANISOU 2328  CB  SER B 233     2184   1981   2915   -700   -887    452       C  
-ATOM   2329  OG  SER B 233      40.847   0.926  -9.370  1.00 18.44           O  
-ANISOU 2329  OG  SER B 233     2055   2164   2786   -902   -999    292       O  
-ATOM   2330  N   VAL B 234      40.495   4.403 -10.226  1.00 15.27           N  
-ANISOU 2330  N   VAL B 234     2050   1840   1911   -306   -614     -2       N  
-ATOM   2331  CA  VAL B 234      41.250   5.428  -9.511  1.00 13.58           C  
-ANISOU 2331  CA  VAL B 234     1783   1800   1575   -325   -288    -13       C  
-ATOM   2332  C   VAL B 234      40.854   5.353  -8.035  1.00 13.93           C  
-ANISOU 2332  C   VAL B 234     1573   1661   2058   -539   -336     66       C  
-ATOM   2333  O   VAL B 234      39.841   4.737  -7.696  1.00 15.09           O  
-ANISOU 2333  O   VAL B 234     1698   1882   2151   -416   -224    263       O  
-ATOM   2334  CB  VAL B 234      41.010   6.843 -10.105  1.00 14.72           C  
-ANISOU 2334  CB  VAL B 234     1610   1804   2180    -37     40    597       C  
-ATOM   2335  CG1 VAL B 234      41.465   6.884 -11.566  1.00 14.39           C  
-ANISOU 2335  CG1 VAL B 234     1402   2228   1836   -149    347    443       C  
-ATOM   2336  CG2 VAL B 234      39.549   7.246  -9.967  1.00 15.21           C  
-ANISOU 2336  CG2 VAL B 234     1306   1957   2516    -71    311    314       C  
-ATOM   2337  N   PRO B 235      41.655   5.952  -7.145  1.00 13.82           N  
-ANISOU 2337  N   PRO B 235     1586   1811   1852   -313   -229     56       N  
-ATOM   2338  CA  PRO B 235      41.351   5.840  -5.714  1.00 15.42           C  
-ANISOU 2338  CA  PRO B 235     1453   2141   2265   -251   -526    163       C  
-ATOM   2339  C   PRO B 235      39.959   6.354  -5.356  1.00 15.49           C  
-ANISOU 2339  C   PRO B 235     1872   2155   1859   -448   -561    592       C  
-ATOM   2340  O   PRO B 235      39.491   7.370  -5.889  1.00 16.49           O  
-ANISOU 2340  O   PRO B 235     1894   2318   2052    -85   -256    385       O  
-ATOM   2341  CB  PRO B 235      42.423   6.716  -5.064  1.00 16.29           C  
-ANISOU 2341  CB  PRO B 235     1619   1921   2647    -98   -499   -286       C  
-ATOM   2342  CG  PRO B 235      43.568   6.673  -6.027  1.00 15.34           C  
-ANISOU 2342  CG  PRO B 235     1519   1997   2311   -219   -126     55       C  
-ATOM   2343  CD  PRO B 235      42.921   6.667  -7.386  1.00 14.54           C  
-ANISOU 2343  CD  PRO B 235     1384   2080   2059   -445   -524   -251       C  
-ATOM   2344  N   ASN B 236      39.310   5.614  -4.467  1.00 19.14           N  
-ANISOU 2344  N   ASN B 236     2474   2493   2303   -751    -82    504       N  
-ATOM   2345  CA  ASN B 236      38.040   5.976  -3.867  1.00 22.64           C  
-ANISOU 2345  CA  ASN B 236     3199   3014   2390   -473    305    376       C  
-ATOM   2346  C   ASN B 236      38.305   6.761  -2.580  1.00 22.12           C  
-ANISOU 2346  C   ASN B 236     3138   3101   2163   -185    792    416       C  
-ATOM   2347  O   ASN B 236      37.862   6.381  -1.493  1.00 26.74           O  
-ANISOU 2347  O   ASN B 236     3483   3852   2825    -70    745    439       O  
-ATOM   2348  CB  ASN B 236      37.265   4.692  -3.566  1.00 27.35           C  
-ANISOU 2348  CB  ASN B 236     3589   3160   3642   -706    196    -51       C  
-ATOM   2349  CG  ASN B 236      35.932   4.949  -2.923  1.00 32.94           C  
-ANISOU 2349  CG  ASN B 236     4268   3571   4675   -385    362    516       C  
-ATOM   2350  OD1 ASN B 236      35.260   5.932  -3.231  1.00 35.95           O  
-ANISOU 2350  OD1 ASN B 236     4371   4069   5219   -206    134    679       O  
-ATOM   2351  ND2 ASN B 236      35.538   4.061  -2.017  1.00 34.50           N  
-ANISOU 2351  ND2 ASN B 236     4625   3635   4846   -329    109    702       N  
-ATOM   2352  N   ILE B 237      39.068   7.842  -2.722  1.00 18.80           N  
-ANISOU 2352  N   ILE B 237     2692   2372   2079     94    325    573       N  
-ATOM   2353  CA  ILE B 237      39.464   8.711  -1.619  1.00 17.25           C  
-ANISOU 2353  CA  ILE B 237     1993   2513   2047    124   -141    504       C  
-ATOM   2354  C   ILE B 237      39.197  10.152  -2.030  1.00 16.05           C  
-ANISOU 2354  C   ILE B 237     1701   2350   2045    171    -52    453       C  
-ATOM   2355  O   ILE B 237      39.541  10.548  -3.144  1.00 15.29           O  
-ANISOU 2355  O   ILE B 237     1562   2379   1868     20   -112    470       O  
-ATOM   2356  CB  ILE B 237      40.978   8.582  -1.322  1.00 18.52           C  
-ANISOU 2356  CB  ILE B 237     2219   2501   2317    101   -184    327       C  
-ATOM   2357  CG1 ILE B 237      41.353   7.132  -1.013  1.00 20.68           C  
-ANISOU 2357  CG1 ILE B 237     2616   2662   2578    247    260    497       C  
-ATOM   2358  CG2 ILE B 237      41.401   9.519  -0.183  1.00 17.61           C  
-ANISOU 2358  CG2 ILE B 237     2041   2364   2284      9   -278     95       C  
-ATOM   2359  CD1 ILE B 237      40.709   6.599   0.244  1.00 25.47           C  
-ANISOU 2359  CD1 ILE B 237     3045   2796   3834    471     -2    422       C  
-ATOM   2360  N   PRO B 238      38.566  10.938  -1.148  1.00 15.31           N  
-ANISOU 2360  N   PRO B 238     1546   2429   1842    166     58    503       N  
-ATOM   2361  CA  PRO B 238      38.330  12.349  -1.472  1.00 14.55           C  
-ANISOU 2361  CA  PRO B 238     1365   2181   1980     61    194    354       C  
-ATOM   2362  C   PRO B 238      39.637  13.076  -1.787  1.00 13.98           C  
-ANISOU 2362  C   PRO B 238     1473   2026   1813    270    110    460       C  
-ATOM   2363  O   PRO B 238      40.675  12.825  -1.159  1.00 14.79           O  
-ANISOU 2363  O   PRO B 238     1348   2140   2132    125   -331    343       O  
-ATOM   2364  CB  PRO B 238      37.683  12.902  -0.197  1.00 17.39           C  
-ANISOU 2364  CB  PRO B 238     1599   2653   2356    340    -43    381       C  
-ATOM   2365  CG  PRO B 238      37.081  11.702   0.479  1.00 17.45           C  
-ANISOU 2365  CG  PRO B 238     1718   2560   2353    216    329    753       C  
-ATOM   2366  CD  PRO B 238      38.026  10.571   0.172  1.00 17.35           C  
-ANISOU 2366  CD  PRO B 238     1694   2658   2240    434    204    545       C  
-ATOM   2367  N   MET B 239      39.583  13.969  -2.770  1.00 12.78           N  
-ANISOU 2367  N   MET B 239     1214   1876   1766    -45    275    442       N  
-ATOM   2368  CA  MET B 239      40.775  14.671  -3.230  1.00 12.49           C  
-ANISOU 2368  CA  MET B 239     1204   1987   1555    145     -3    527       C  
-ATOM   2369  C   MET B 239      41.515  15.367  -2.094  1.00 11.94           C  
-ANISOU 2369  C   MET B 239     1060   1883   1593    198    -19    310       C  
-ATOM   2370  O   MET B 239      42.748  15.358  -2.053  1.00 12.76           O  
-ANISOU 2370  O   MET B 239     1145   2033   1669    378      8    358       O  
-ATOM   2371  CB  MET B 239      40.424  15.685  -4.320  1.00 13.85           C  
-ANISOU 2371  CB  MET B 239     1352   2076   1833     52     80    648       C  
-ATOM   2372  CG  MET B 239      41.645  16.346  -4.942  1.00 14.57           C  
-ANISOU 2372  CG  MET B 239     1367   2271   1896    181      3    650       C  
-ATOM   2373  SD  MET B 239      41.231  17.554  -6.211  1.00 15.07           S  
-ANISOU 2373  SD  MET B 239     1466   2462   1797    223    -32    336       S  
-ATOM   2374  CE  MET B 239      40.527  18.864  -5.213  1.00 17.18           C  
-ANISOU 2374  CE  MET B 239     1718   2594   2216    508    263     93       C  
-ATOM   2375  N   ASN B 240      40.770  15.972  -1.174  1.00 12.93           N  
-ANISOU 2375  N   ASN B 240     1490   1906   1516    532     77    137       N  
-ATOM   2376  CA  ASN B 240      41.400  16.737  -0.098  1.00 13.63           C  
-ANISOU 2376  CA  ASN B 240     1414   2008   1757    691   -192    122       C  
-ATOM   2377  C   ASN B 240      41.998  15.899   1.032  1.00 12.72           C  
-ANISOU 2377  C   ASN B 240     1264   1856   1714    344     17    369       C  
-ATOM   2378  O   ASN B 240      42.479  16.450   2.020  1.00 13.94           O  
-ANISOU 2378  O   ASN B 240     1420   2008   1867    493   -101    276       O  
-ATOM   2379  CB  ASN B 240      40.454  17.810   0.455  1.00 15.90           C  
-ANISOU 2379  CB  ASN B 240     1470   2447   2123   1002    -89    223       C  
-ATOM   2380  CG  ASN B 240      39.259  17.227   1.173  1.00 17.22           C  
-ANISOU 2380  CG  ASN B 240     1672   2765   2104    829      9     91       C  
-ATOM   2381  OD1 ASN B 240      38.813  16.121   0.873  1.00 16.86           O  
-ANISOU 2381  OD1 ASN B 240     1476   2789   2140    658     48    142       O  
-ATOM   2382  ND2 ASN B 240      38.728  17.979   2.131  1.00 19.34           N  
-ANISOU 2382  ND2 ASN B 240     1889   3044   2416    620     74   -257       N  
-ATOM   2383  N   LEU B 241      41.963  14.575   0.886  1.00 12.28           N  
-ANISOU 2383  N   LEU B 241     1151   1672   1842    371    240    277       N  
-ATOM   2384  CA  LEU B 241      42.660  13.674   1.810  1.00 12.00           C  
-ANISOU 2384  CA  LEU B 241     1292   1729   1536    150    348    364       C  
-ATOM   2385  C   LEU B 241      43.939  13.117   1.189  1.00 11.02           C  
-ANISOU 2385  C   LEU B 241     1266   1522   1398    216    190     28       C  
-ATOM   2386  O   LEU B 241      44.684  12.388   1.842  1.00 12.23           O  
-ANISOU 2386  O   LEU B 241     1465   1498   1683    414    -33    139       O  
-ATOM   2387  CB  LEU B 241      41.768  12.502   2.214  1.00 15.06           C  
-ANISOU 2387  CB  LEU B 241     1712   2262   1748   -183    435    306       C  
-ATOM   2388  CG  LEU B 241      40.503  12.847   2.982  1.00 21.15           C  
-ANISOU 2388  CG  LEU B 241     2305   2650   3080   -278   1076    517       C  
-ATOM   2389  CD1 LEU B 241      39.868  11.586   3.566  1.00 21.53           C  
-ANISOU 2389  CD1 LEU B 241     2436   2803   2942    -75   1099    716       C  
-ATOM   2390  CD2 LEU B 241      40.820  13.841   4.060  1.00 26.19           C  
-ANISOU 2390  CD2 LEU B 241     3036   3262   3654    211   1226    -18       C  
-ATOM   2391  N   MET B 242      44.186  13.451  -0.074  1.00 10.03           N  
-ANISOU 2391  N   MET B 242     1064   1329   1419     29    169     30       N  
-ATOM   2392  CA  MET B 242      45.365  12.977  -0.778  1.00  9.58           C  
-ANISOU 2392  CA  MET B 242     1130   1359   1149     41   -118   -120       C  
-ATOM   2393  C   MET B 242      46.466  14.016  -0.783  1.00  9.84           C  
-ANISOU 2393  C   MET B 242      992   1167   1579    226    133   -145       C  
-ATOM   2394  O   MET B 242      46.211  15.209  -0.597  1.00 11.34           O  
-ANISOU 2394  O   MET B 242     1195   1245   1869    208    -17    -16       O  
-ATOM   2395  CB  MET B 242      45.013  12.590  -2.210  1.00 12.87           C  
-ANISOU 2395  CB  MET B 242     1180   2040   1670     76   -297   -306       C  
-ATOM   2396  CG  MET B 242      44.089  11.391  -2.267  1.00 15.49           C  
-ANISOU 2396  CG  MET B 242     1297   2793   1794   -342   -229   -938       C  
-ATOM   2397  SD  MET B 242      43.793  10.769  -3.923  1.00 21.58           S  
-ANISOU 2397  SD  MET B 242     1409   4429   2359     83   -169  -1224       S  
-ATOM   2398  CE  MET B 242      42.570  11.927  -4.514  1.00 23.40           C  
-ANISOU 2398  CE  MET B 242     1707   4637   2545    473   -330  -1090       C  
-ATOM   2399  N   SER B 243      47.692  13.545  -0.981  1.00 10.04           N  
-ANISOU 2399  N   SER B 243      966   1202   1647     19     -8    103       N  
-ATOM   2400  CA  SER B 243      48.864  14.416  -0.978  1.00  9.36           C  
-ANISOU 2400  CA  SER B 243      954   1161   1440    131     30    142       C  
-ATOM   2401  C   SER B 243      49.210  14.925  -2.375  1.00  8.36           C  
-ANISOU 2401  C   SER B 243      913   1024   1237    133   -101   -285       C  
-ATOM   2402  O   SER B 243      48.995  14.239  -3.379  1.00  9.66           O  
-ANISOU 2402  O   SER B 243     1112   1030   1527    233   -120    -79       O  
-ATOM   2403  CB  SER B 243      50.067  13.653  -0.408  1.00 10.49           C  
-ANISOU 2403  CB  SER B 243      846   1209   1929   -216   -143     72       C  
-ATOM   2404  OG  SER B 243      51.227  14.472  -0.350  1.00 10.50           O  
-ANISOU 2404  OG  SER B 243     1185   1182   1621    296    -17   -153       O  
-ATOM   2405  N   ASN B 244      49.751  16.135  -2.427  1.00  8.91           N  
-ANISOU 2405  N   ASN B 244      927    800   1658    120    210     65       N  
-ATOM   2406  CA  ASN B 244      50.504  16.601  -3.582  1.00  9.05           C  
-ANISOU 2406  CA  ASN B 244     1040    744   1652    219    230    -55       C  
-ATOM   2407  C   ASN B 244      51.609  15.572  -3.886  1.00  7.73           C  
-ANISOU 2407  C   ASN B 244     1069    665   1202     60    214     -9       C  
-ATOM   2408  O   ASN B 244      52.090  14.878  -2.970  1.00  9.45           O  
-ANISOU 2408  O   ASN B 244     1197   1017   1376    169     41    121       O  
-ATOM   2409  CB  ASN B 244      51.125  17.960  -3.238  1.00  8.87           C  
-ANISOU 2409  CB  ASN B 244     1369    611   1391     71    -40    199       C  
-ATOM   2410  CG  ASN B 244      51.442  18.807  -4.461  1.00  8.68           C  
-ANISOU 2410  CG  ASN B 244     1140    843   1313    229    -49     55       C  
-ATOM   2411  OD1 ASN B 244      52.423  18.561  -5.160  1.00  9.66           O  
-ANISOU 2411  OD1 ASN B 244     1077    977   1615    269    124    -27       O  
-ATOM   2412  ND2 ASN B 244      50.633  19.845  -4.695  1.00 10.17           N  
-ANISOU 2412  ND2 ASN B 244     1330    812   1723    301    -91     13       N  
-ATOM   2413  N   SER B 245      52.010  15.456  -5.149  1.00  7.74           N  
-ANISOU 2413  N   SER B 245      987    665   1290    153    264   -108       N  
-ATOM   2414  CA  SER B 245      53.113  14.560  -5.480  1.00  8.65           C  
-ANISOU 2414  CA  SER B 245     1117    891   1276     94    -61   -196       C  
-ATOM   2415  C   SER B 245      54.482  15.245  -5.536  1.00  8.67           C  
-ANISOU 2415  C   SER B 245      923    857   1515     66   -177   -201       C  
-ATOM   2416  O   SER B 245      55.504  14.566  -5.700  1.00 10.32           O  
-ANISOU 2416  O   SER B 245     1236    974   1711    242    142    -47       O  
-ATOM   2417  CB  SER B 245      52.838  13.812  -6.784  1.00  9.57           C  
-ANISOU 2417  CB  SER B 245     1279   1004   1352    174     27     -9       C  
-ATOM   2418  OG  SER B 245      52.473  14.710  -7.819  1.00  9.79           O  
-ANISOU 2418  OG  SER B 245     1553    963   1204    290     30    140       O  
-ATOM   2419  N   ARG B 246      54.516  16.572  -5.389  1.00  8.53           N  
-ANISOU 2419  N   ARG B 246     1165    614   1463    -97    138    -65       N  
-ATOM   2420  CA  ARG B 246      55.781  17.305  -5.429  1.00  9.22           C  
-ANISOU 2420  CA  ARG B 246     1335    780   1388    142     71    369       C  
-ATOM   2421  C   ARG B 246      56.234  17.826  -4.060  1.00  8.21           C  
-ANISOU 2421  C   ARG B 246     1192    620   1307    100   -122   -161       C  
-ATOM   2422  O   ARG B 246      57.414  18.128  -3.864  1.00  9.45           O  
-ANISOU 2422  O   ARG B 246      993    876   1719   -111    -13     66       O  
-ATOM   2423  CB  ARG B 246      55.704  18.463  -6.430  1.00  9.00           C  
-ANISOU 2423  CB  ARG B 246     1175    878   1364    138     62    241       C  
-ATOM   2424  CG  ARG B 246      55.534  18.031  -7.880  1.00  9.15           C  
-ANISOU 2424  CG  ARG B 246     1436   1066    975    126    192    200       C  
-ATOM   2425  CD  ARG B 246      55.391  19.241  -8.772  1.00  9.69           C  
-ANISOU 2425  CD  ARG B 246     1346   1019   1316    -18    171    462       C  
-ATOM   2426  NE  ARG B 246      56.671  19.901  -9.002  1.00 10.37           N  
-ANISOU 2426  NE  ARG B 246     1271    917   1751    -85    279    176       N  
-ATOM   2427  CZ  ARG B 246      56.814  21.161  -9.401  1.00 10.07           C  
-ANISOU 2427  CZ  ARG B 246     1141    977   1708     68      1   -126       C  
-ATOM   2428  NH1 ARG B 246      55.750  21.936  -9.564  1.00 11.04           N  
-ANISOU 2428  NH1 ARG B 246     1299   1073   1823    319    455     26       N  
-ATOM   2429  NH2 ARG B 246      58.029  21.651  -9.625  1.00 11.50           N  
-ANISOU 2429  NH2 ARG B 246     1206   1376   1785    118     73     42       N  
-ATOM   2430  N   VAL B 247      55.291  17.953  -3.130  1.00  9.09           N  
-ANISOU 2430  N   VAL B 247     1246    879   1328    164    -17    -14       N  
-ATOM   2431  CA  VAL B 247      55.585  18.228  -1.723  1.00  9.34           C  
-ANISOU 2431  CA  VAL B 247     1245    692   1612    134     97     40       C  
-ATOM   2432  C   VAL B 247      54.625  17.381  -0.913  1.00  9.11           C  
-ANISOU 2432  C   VAL B 247     1147    884   1429    385    -63    132       C  
-ATOM   2433  O   VAL B 247      53.526  17.086  -1.377  1.00  9.52           O  
-ANISOU 2433  O   VAL B 247     1080   1035   1503    209   -123     48       O  
-ATOM   2434  CB  VAL B 247      55.390  19.733  -1.331  1.00  9.84           C  
-ANISOU 2434  CB  VAL B 247      934    960   1843     99     25    -74       C  
-ATOM   2435  CG1 VAL B 247      56.467  20.608  -1.972  1.00 11.24           C  
-ANISOU 2435  CG1 VAL B 247     1119    984   2167   -174    303     56       C  
-ATOM   2436  CG2 VAL B 247      53.994  20.225  -1.713  1.00 11.22           C  
-ANISOU 2436  CG2 VAL B 247     1466    866   1931    172    107     19       C  
-ATOM   2437  N   PRO B 248      55.038  16.962   0.294  1.00 10.16           N  
-ANISOU 2437  N   PRO B 248      992   1034   1832    272    -28    219       N  
-ATOM   2438  CA  PRO B 248      54.148  16.167   1.150  1.00 10.12           C  
-ANISOU 2438  CA  PRO B 248     1024   1225   1594    412    152    476       C  
-ATOM   2439  C   PRO B 248      53.179  17.091   1.884  1.00 10.19           C  
-ANISOU 2439  C   PRO B 248     1222   1207   1441    283   -122    102       C  
-ATOM   2440  O   PRO B 248      53.406  17.512   3.024  1.00 14.70           O  
-ANISOU 2440  O   PRO B 248     1900   1796   1887    762   -423   -416       O  
-ATOM   2441  CB  PRO B 248      55.123  15.483   2.113  1.00 11.53           C  
-ANISOU 2441  CB  PRO B 248     1144   1271   1964    263   -116    242       C  
-ATOM   2442  CG  PRO B 248      56.255  16.468   2.229  1.00 10.95           C  
-ANISOU 2442  CG  PRO B 248     1075   1180   1904   -102   -314    101       C  
-ATOM   2443  CD  PRO B 248      56.398  17.074   0.853  1.00 11.42           C  
-ANISOU 2443  CD  PRO B 248     1190   1559   1588    237   -298    321       C  
-ATOM   2444  N   MET B 249      52.098  17.417   1.190  1.00 11.05           N  
-ANISOU 2444  N   MET B 249     1146   1390   1661    400   -111    134       N  
-ATOM   2445  CA  MET B 249      51.111  18.371   1.662  1.00 10.60           C  
-ANISOU 2445  CA  MET B 249     1445   1046   1537    162   -107     28       C  
-ATOM   2446  C   MET B 249      49.774  17.962   1.075  1.00 10.00           C  
-ANISOU 2446  C   MET B 249     1255   1080   1464    278    230     65       C  
-ATOM   2447  O   MET B 249      49.705  17.594  -0.099  1.00 10.85           O  
-ANISOU 2447  O   MET B 249     1477   1203   1443    423    151     33       O  
-ATOM   2448  CB  MET B 249      51.454  19.762   1.136  1.00 15.22           C  
-ANISOU 2448  CB  MET B 249     2545   1292   1944    259    -80    399       C  
-ATOM   2449  CG  MET B 249      51.209  20.868   2.106  1.00 22.05           C  
-ANISOU 2449  CG  MET B 249     3485   2216   2676   -233   -387     -6       C  
-ATOM   2450  SD  MET B 249      52.358  20.766   3.486  1.00 21.73           S  
-ANISOU 2450  SD  MET B 249     3789   2342   2126   -944   -657     33       S  
-ATOM   2451  CE  MET B 249      52.265  22.449   4.049  1.00 24.47           C  
-ANISOU 2451  CE  MET B 249     3737   2183   3377   -710   -451    389       C  
-ATOM   2452  N   LEU B 250      48.707  18.038   1.866  1.00  9.81           N  
-ANISOU 2452  N   LEU B 250     1023   1243   1462    251     80    -59       N  
-ATOM   2453  CA  LEU B 250      47.384  17.731   1.341  1.00 10.56           C  
-ANISOU 2453  CA  LEU B 250     1109   1695   1209    267    130    275       C  
-ATOM   2454  C   LEU B 250      47.049  18.631   0.159  1.00 10.07           C  
-ANISOU 2454  C   LEU B 250     1236   1375   1216    437     47   -156       C  
-ATOM   2455  O   LEU B 250      47.437  19.819   0.112  1.00 11.45           O  
-ANISOU 2455  O   LEU B 250     1403   1099   1849    275   -174    -78       O  
-ATOM   2456  CB  LEU B 250      46.317  17.888   2.422  1.00 11.58           C  
-ANISOU 2456  CB  LEU B 250     1329   1654   1416    335      4    579       C  
-ATOM   2457  CG  LEU B 250      46.346  16.867   3.558  1.00 12.58           C  
-ANISOU 2457  CG  LEU B 250     1632   1738   1409    406     87    186       C  
-ATOM   2458  CD1 LEU B 250      45.394  17.284   4.690  1.00 15.66           C  
-ANISOU 2458  CD1 LEU B 250     1789   2440   1720    692    666    116       C  
-ATOM   2459  CD2 LEU B 250      46.033  15.466   3.054  1.00 14.79           C  
-ANISOU 2459  CD2 LEU B 250     1928   1669   2022     86   -530    123       C  
-ATOM   2460  N   ILE B 251      46.317  18.065  -0.794  1.00 10.20           N  
-ANISOU 2460  N   ILE B 251     1386   1427   1062    629   -115     89       N  
-ATOM   2461  CA  ILE B 251      45.760  18.841  -1.894  1.00  9.87           C  
-ANISOU 2461  CA  ILE B 251     1265   1247   1237    514   -232    -57       C  
-ATOM   2462  C   ILE B 251      44.634  19.742  -1.387  1.00 11.07           C  
-ANISOU 2462  C   ILE B 251     1349   1266   1591    529     27    207       C  
-ATOM   2463  O   ILE B 251      43.735  19.286  -0.678  1.00 12.48           O  
-ANISOU 2463  O   ILE B 251     1390   1611   1742    518    107    144       O  
-ATOM   2464  CB  ILE B 251      45.232  17.915  -3.015  1.00 10.12           C  
-ANISOU 2464  CB  ILE B 251     1316   1435   1093    351   -256     38       C  
-ATOM   2465  CG1 ILE B 251      46.396  17.137  -3.643  1.00 12.70           C  
-ANISOU 2465  CG1 ILE B 251     1650   1677   1496    675     -3   -362       C  
-ATOM   2466  CG2 ILE B 251      44.481  18.714  -4.083  1.00 11.69           C  
-ANISOU 2466  CG2 ILE B 251     1288   1684   1469    113   -171    135       C  
-ATOM   2467  CD1 ILE B 251      45.957  16.013  -4.528  1.00 15.70           C  
-ANISOU 2467  CD1 ILE B 251     1920   1762   2281    384     24   -294       C  
-ATOM   2468  N   ASP B 252      44.683  21.022  -1.747  1.00 11.14           N  
-ANISOU 2468  N   ASP B 252     1285   1259   1687    665     87     64       N  
-ATOM   2469  CA  ASP B 252      43.629  21.948  -1.336  1.00 11.91           C  
-ANISOU 2469  CA  ASP B 252     1485   1377   1663    600    215      3       C  
-ATOM   2470  C   ASP B 252      43.009  22.697  -2.511  1.00 13.88           C  
-ANISOU 2470  C   ASP B 252     1870   1567   1835    713    371    132       C  
-ATOM   2471  O   ASP B 252      42.312  23.696  -2.327  1.00 15.19           O  
-ANISOU 2471  O   ASP B 252     2012   1732   2028    767    296    142       O  
-ATOM   2472  CB  ASP B 252      44.128  22.915  -0.257  1.00 14.31           C  
-ANISOU 2472  CB  ASP B 252     1554   1410   2473    307    -69   -261       C  
-ATOM   2473  CG  ASP B 252      45.151  23.899  -0.769  1.00 20.01           C  
-ANISOU 2473  CG  ASP B 252     2193   1560   3851    387    387   -822       C  
-ATOM   2474  OD1 ASP B 252      45.592  23.771  -1.924  1.00 23.55           O  
-ANISOU 2474  OD1 ASP B 252     2301   1721   4924    283   1259   -246       O  
-ATOM   2475  OD2 ASP B 252      45.498  24.830  -0.009  1.00 26.17           O  
-ANISOU 2475  OD2 ASP B 252     2310   2241   5391    113   -153   -907       O  
-ATOM   2476  N   GLY B 253      43.248  22.212  -3.722  1.00 14.13           N  
-ANISOU 2476  N   GLY B 253     1942   1852   1574    998    269    451       N  
-ATOM   2477  CA  GLY B 253      42.620  22.808  -4.886  1.00 15.41           C  
-ANISOU 2477  CA  GLY B 253     2072   2130   1654   1152    312    429       C  
-ATOM   2478  C   GLY B 253      42.996  22.150  -6.196  1.00 13.70           C  
-ANISOU 2478  C   GLY B 253     1823   2124   1259    969    305    284       C  
-ATOM   2479  O   GLY B 253      43.857  21.261  -6.243  1.00 12.94           O  
-ANISOU 2479  O   GLY B 253     1395   1672   1850    503     85    132       O  
-ATOM   2480  N   MET B 254      42.324  22.592  -7.257  1.00 16.43           N  
-ANISOU 2480  N   MET B 254     2048   2508   1685   1136    202    695       N  
-ATOM   2481  CA  MET B 254      42.665  22.272  -8.638  1.00 16.07           C  
-ANISOU 2481  CA  MET B 254     2324   2382   1398    944    271    483       C  
-ATOM   2482  C   MET B 254      42.772  23.587  -9.383  1.00 17.68           C  
-ANISOU 2482  C   MET B 254     2757   2305   1656   1357    473    588       C  
-ATOM   2483  O   MET B 254      42.118  24.562  -9.013  1.00 22.23           O  
-ANISOU 2483  O   MET B 254     3468   2830   2147   1776    654    591       O  
-ATOM   2484  CB  MET B 254      41.571  21.429  -9.286  1.00 18.86           C  
-ANISOU 2484  CB  MET B 254     2405   2508   2252    919    -54    613       C  
-ATOM   2485  CG  MET B 254      41.624  19.956  -8.936  1.00 19.03           C  
-ANISOU 2485  CG  MET B 254     2268   2674   2287   1037    -11    877       C  
-ATOM   2486  SD  MET B 254      40.347  19.033  -9.816  1.00 19.82           S  
-ANISOU 2486  SD  MET B 254     2185   2836   2509    635    122    773       S  
-ATOM   2487  CE  MET B 254      38.928  19.302  -8.762  1.00 20.60           C  
-ANISOU 2487  CE  MET B 254     2053   3281   2493    620    -89    630       C  
-ATOM   2488  N   MET B 255      43.589  23.620 -10.427  1.00 15.15           N  
-ANISOU 2488  N   MET B 255     2424   2061   1269   1011    311    590       N  
-ATOM   2489  CA  MET B 255      43.712  24.805 -11.273  1.00 15.82           C  
-ANISOU 2489  CA  MET B 255     2528   1983   1501    546    349    562       C  
-ATOM   2490  C   MET B 255      44.071  24.402 -12.687  1.00 15.01           C  
-ANISOU 2490  C   MET B 255     2450   1889   1362    693    403    404       C  
-ATOM   2491  O   MET B 255      44.531  23.288 -12.930  1.00 15.22           O  
-ANISOU 2491  O   MET B 255     2549   1549   1686    898    375    302       O  
-ATOM   2492  CB  MET B 255      44.796  25.755 -10.745  1.00 18.50           C  
-ANISOU 2492  CB  MET B 255     2992   2032   2003    504    265   -339       C  
-ATOM   2493  CG  MET B 255      46.219  25.192 -10.865  1.00 22.47           C  
-ANISOU 2493  CG  MET B 255     3518   2195   2822     46    216   -360       C  
-ATOM   2494  SD  MET B 255      47.557  26.316 -10.367  1.00 26.18           S  
-ANISOU 2494  SD  MET B 255     4085   2958   2904   -150    215    137       S  
-ATOM   2495  CE  MET B 255      47.692  27.380 -11.803  1.00 28.73           C  
-ANISOU 2495  CE  MET B 255     4101   3430   3384    -45   -113    550       C  
-ATOM   2496  N   VAL B 256      43.852  25.322 -13.618  1.00 16.93           N  
-ANISOU 2496  N   VAL B 256     2796   1982   1653   1008    154    393       N  
-ATOM   2497  CA  VAL B 256      44.455  25.239 -14.930  1.00 16.69           C  
-ANISOU 2497  CA  VAL B 256     2794   1982   1565    789     89    267       C  
-ATOM   2498  C   VAL B 256      45.475  26.364 -15.002  1.00 17.74           C  
-ANISOU 2498  C   VAL B 256     2947   1791   2001    699    267    571       C  
-ATOM   2499  O   VAL B 256      45.341  27.371 -14.301  1.00 21.11           O  
-ANISOU 2499  O   VAL B 256     3406   2123   2491    521    178    124       O  
-ATOM   2500  CB  VAL B 256      43.408  25.381 -16.050  1.00 18.72           C  
-ANISOU 2500  CB  VAL B 256     2806   2190   2117   1091    -86    206       C  
-ATOM   2501  CG1 VAL B 256      42.455  24.198 -16.026  1.00 19.58           C  
-ANISOU 2501  CG1 VAL B 256     2838   2550   2050    915   -388   -229       C  
-ATOM   2502  CG2 VAL B 256      42.646  26.707 -15.929  1.00 20.08           C  
-ANISOU 2502  CG2 VAL B 256     2765   2354   2511   1331     -7    129       C  
-ATOM   2503  N   SER B 257      46.507  26.201 -15.823  1.00 15.89           N  
-ANISOU 2503  N   SER B 257     2620   1384   2034    279     30    355       N  
-ATOM   2504  CA  SER B 257      47.553  27.218 -15.896  1.00 18.14           C  
-ANISOU 2504  CA  SER B 257     2857   1631   2404    309     28    343       C  
-ATOM   2505  C   SER B 257      47.073  28.493 -16.587  1.00 20.04           C  
-ANISOU 2505  C   SER B 257     3373   1711   2528    491     98    299       C  
-ATOM   2506  O   SER B 257      46.228  28.444 -17.480  1.00 20.68           O  
-ANISOU 2506  O   SER B 257     3251   1670   2934    617     46    603       O  
-ATOM   2507  CB  SER B 257      48.809  26.670 -16.579  1.00 18.00           C  
-ANISOU 2507  CB  SER B 257     2677   1840   2322    242   -362   -188       C  
-ATOM   2508  OG  SER B 257      48.506  26.155 -17.861  1.00 17.48           O  
-ANISOU 2508  OG  SER B 257     2412   1560   2668    237    -39     32       O  
-ATOM   2509  N   ASN B 258      47.614  29.626 -16.147  1.00 22.47           N  
-ANISOU 2509  N   ASN B 258     4054   1653   2831    708    139    245       N  
-ATOM   2510  CA  ASN B 258      47.303  30.929 -16.723  1.00 24.24           C  
-ANISOU 2510  CA  ASN B 258     4398   1649   3163    784    110    501       C  
-ATOM   2511  C   ASN B 258      47.475  30.891 -18.234  1.00 24.31           C  
-ANISOU 2511  C   ASN B 258     4233   1609   3394    540   -264    115       C  
-ATOM   2512  O   ASN B 258      46.575  31.263 -18.991  1.00 26.49           O  
-ANISOU 2512  O   ASN B 258     4212   2297   3556    609   -351    692       O  
-ATOM   2513  CB  ASN B 258      48.216  31.990 -16.094  1.00 28.67           C  
-ANISOU 2513  CB  ASN B 258     4918   1630   4346    875    190    160       C  
-ATOM   2514  CG  ASN B 258      47.815  33.412 -16.452  1.00 33.64           C  
-ANISOU 2514  CG  ASN B 258     5370   2201   5211   1129    100     61       C  
-ATOM   2515  OD1 ASN B 258      46.677  33.677 -16.840  1.00 36.81           O  
-ANISOU 2515  OD1 ASN B 258     5575   2349   6060   1411     74    -90       O  
-ATOM   2516  ND2 ASN B 258      48.759  34.339 -16.312  1.00 34.42           N  
-ANISOU 2516  ND2 ASN B 258     5621   2346   5111   1174    295    230       N  
-ATOM   2517  N   ASP B 259      48.649  30.440 -18.662  1.00 22.93           N  
-ANISOU 2517  N   ASP B 259     4132   1408   3173    466    -36    294       N  
-ATOM   2518  CA  ASP B 259      48.907  30.147 -20.062  1.00 24.47           C  
-ANISOU 2518  CA  ASP B 259     4040   1811   3444    654    175    485       C  
-ATOM   2519  C   ASP B 259      48.555  28.685 -20.308  1.00 23.62           C  
-ANISOU 2519  C   ASP B 259     3688   1838   3447    766   -309   -132       C  
-ATOM   2520  O   ASP B 259      49.250  27.791 -19.832  1.00 21.52           O  
-ANISOU 2520  O   ASP B 259     3278   1806   3091    963   -115    543       O  
-ATOM   2521  CB  ASP B 259      50.385  30.379 -20.372  1.00 27.94           C  
-ANISOU 2521  CB  ASP B 259     4238   2376   4003    495    849    842       C  
-ATOM   2522  CG  ASP B 259      50.714  30.180 -21.837  1.00 33.83           C  
-ANISOU 2522  CG  ASP B 259     4532   3418   4902    607   1139    852       C  
-ATOM   2523  OD1 ASP B 259      49.870  29.633 -22.579  1.00 34.35           O  
-ANISOU 2523  OD1 ASP B 259     4553   3717   4781    701   1287    927       O  
-ATOM   2524  OD2 ASP B 259      51.825  30.567 -22.244  1.00 38.65           O  
-ANISOU 2524  OD2 ASP B 259     4691   3966   6026    549   1105    542       O  
-ATOM   2525  N   GLN B 260      47.482  28.434 -21.050  1.00 26.32           N  
-ANISOU 2525  N   GLN B 260     3813   2391   3797    953   -906   -451       N  
-ATOM   2526  CA  GLN B 260      47.024  27.062 -21.253  1.00 28.78           C  
-ANISOU 2526  CA  GLN B 260     3975   2575   4386   1124  -1214   -953       C  
-ATOM   2527  C   GLN B 260      47.962  26.259 -22.154  1.00 29.95           C  
-ANISOU 2527  C   GLN B 260     4226   3125   4028   1516  -1142   -719       C  
-ATOM   2528  O   GLN B 260      47.782  25.050 -22.334  1.00 29.87           O  
-ANISOU 2528  O   GLN B 260     4226   2988   4133   1425  -1347  -1046       O  
-ATOM   2529  CB  GLN B 260      45.581  27.038 -21.770  1.00 32.77           C  
-ANISOU 2529  CB  GLN B 260     4220   2715   5517    940  -1141  -1211       C  
-ATOM   2530  CG  GLN B 260      44.636  27.864 -20.903  1.00 36.21           C  
-ANISOU 2530  CG  GLN B 260     4454   3135   6168    701   -727   -772       C  
-ATOM   2531  CD  GLN B 260      43.207  27.349 -20.892  1.00 36.57           C  
-ANISOU 2531  CD  GLN B 260     4690   3159   6045    574   -214      3       C  
-ATOM   2532  OE1 GLN B 260      42.765  26.662 -21.814  1.00 37.21           O  
-ANISOU 2532  OE1 GLN B 260     4862   2931   6343    570   -108    358       O  
-ATOM   2533  NE2 GLN B 260      42.474  27.686 -19.838  1.00 34.86           N  
-ANISOU 2533  NE2 GLN B 260     4684   3308   5251    358    -95    333       N  
-ATOM   2534  N   ASN B 261      48.974  26.929 -22.701  1.00 27.36           N  
-ANISOU 2534  N   ASN B 261     4447   3310   2639   1869   -824    198       N  
-ATOM   2535  CA  ASN B 261      50.004  26.257 -23.494  1.00 30.18           C  
-ANISOU 2535  CA  ASN B 261     4848   3700   2918   1973   -563    205       C  
-ATOM   2536  C   ASN B 261      51.249  25.860 -22.690  1.00 25.34           C  
-ANISOU 2536  C   ASN B 261     4324   3002   2303   1484   -332    236       C  
-ATOM   2537  O   ASN B 261      52.178  25.253 -23.231  1.00 25.98           O  
-ANISOU 2537  O   ASN B 261     4211   3307   2352   1627     22    400       O  
-ATOM   2538  CB  ASN B 261      50.409  27.116 -24.693  1.00 34.92           C  
-ANISOU 2538  CB  ASN B 261     5545   4444   3279   2495   -648    346       C  
-ATOM   2539  CG  ASN B 261      49.287  27.284 -25.697  1.00 42.20           C  
-ANISOU 2539  CG  ASN B 261     6210   5148   4676   2772   -824     51       C  
-ATOM   2540  OD1 ASN B 261      48.555  26.338 -25.992  1.00 45.65           O  
-ANISOU 2540  OD1 ASN B 261     6500   5535   5309   2694   -779   -251       O  
-ATOM   2541  ND2 ASN B 261      49.142  28.494 -26.225  1.00 44.84           N  
-ANISOU 2541  ND2 ASN B 261     6404   5353   5281   2827   -856    245       N  
-ATOM   2542  N   GLN B 262      51.271  26.207 -21.405  1.00 20.05           N  
-ANISOU 2542  N   GLN B 262     3572   2223   1822    614   -139    417       N  
-ATOM   2543  CA  GLN B 262      52.388  25.844 -20.531  1.00 17.97           C  
-ANISOU 2543  CA  GLN B 262     3017   1889   1920    253   -119    321       C  
-ATOM   2544  C   GLN B 262      52.608  24.333 -20.496  1.00 16.77           C  
-ANISOU 2544  C   GLN B 262     2486   1779   2105    211     59    378       C  
-ATOM   2545  O   GLN B 262      51.677  23.564 -20.271  1.00 17.63           O  
-ANISOU 2545  O   GLN B 262     2118   1835   2743    379   -153    141       O  
-ATOM   2546  CB  GLN B 262      52.161  26.381 -19.112  1.00 19.38           C  
-ANISOU 2546  CB  GLN B 262     3232   2244   1885    402   -435    323       C  
-ATOM   2547  CG  GLN B 262      53.139  25.857 -18.070  1.00 23.07           C  
-ANISOU 2547  CG  GLN B 262     3491   2504   2768    200   -447    162       C  
-ATOM   2548  CD  GLN B 262      54.529  26.442 -18.216  1.00 26.82           C  
-ANISOU 2548  CD  GLN B 262     4021   2277   3893    320   -510     56       C  
-ATOM   2549  OE1 GLN B 262      54.721  27.652 -18.091  1.00 30.94           O  
-ANISOU 2549  OE1 GLN B 262     4381   2033   5340    356   -613    125       O  
-ATOM   2550  NE2 GLN B 262      55.513  25.582 -18.468  1.00 27.47           N  
-ANISOU 2550  NE2 GLN B 262     4071   2439   3928    292  -1068     89       N  
-ATOM   2551  N   VAL B 263      53.853  23.925 -20.720  1.00 15.78           N  
-ANISOU 2551  N   VAL B 263     2225   1496   2273    349    235    201       N  
-ATOM   2552  CA  VAL B 263      54.233  22.521 -20.724  1.00 16.11           C  
-ANISOU 2552  CA  VAL B 263     2134   1790   2195    356    384    656       C  
-ATOM   2553  C   VAL B 263      54.841  22.127 -19.374  1.00 15.17           C  
-ANISOU 2553  C   VAL B 263     1851   1771   2141    227    276    731       C  
-ATOM   2554  O   VAL B 263      55.926  22.592 -19.012  1.00 18.83           O  
-ANISOU 2554  O   VAL B 263     2248   1988   2917    111    -55    630       O  
-ATOM   2555  CB  VAL B 263      55.248  22.235 -21.855  1.00 16.03           C  
-ANISOU 2555  CB  VAL B 263     1908   2051   2131    367    269    850       C  
-ATOM   2556  CG1 VAL B 263      55.683  20.774 -21.847  1.00 16.58           C  
-ANISOU 2556  CG1 VAL B 263     1874   1932   2494    420    202    544       C  
-ATOM   2557  CG2 VAL B 263      54.656  22.618 -23.203  1.00 17.27           C  
-ANISOU 2557  CG2 VAL B 263     2141   2189   2232    259    125    735       C  
-ATOM   2558  N   PRO B 264      54.139  21.272 -18.613  1.00 13.63           N  
-ANISOU 2558  N   PRO B 264     1673   1643   1863    288     27    376       N  
-ATOM   2559  CA  PRO B 264      54.727  20.741 -17.381  1.00 13.34           C  
-ANISOU 2559  CA  PRO B 264     1886   1453   1730    537    266    290       C  
-ATOM   2560  C   PRO B 264      55.673  19.582 -17.680  1.00 12.34           C  
-ANISOU 2560  C   PRO B 264     1840   1307   1542    397    -33     -8       C  
-ATOM   2561  O   PRO B 264      55.435  18.805 -18.611  1.00 13.12           O  
-ANISOU 2561  O   PRO B 264     1955   1404   1625    211     80      0       O  
-ATOM   2562  CB  PRO B 264      53.507  20.236 -16.607  1.00 14.23           C  
-ANISOU 2562  CB  PRO B 264     1913   1552   1942    428    287    394       C  
-ATOM   2563  CG  PRO B 264      52.536  19.834 -17.673  1.00 14.32           C  
-ANISOU 2563  CG  PRO B 264     1738   1649   2052    294    -49    189       C  
-ATOM   2564  CD  PRO B 264      52.765  20.781 -18.833  1.00 13.92           C  
-ANISOU 2564  CD  PRO B 264     1678   1785   1826    222    192    613       C  
-ATOM   2565  N   GLN B 265      56.745  19.480 -16.908  1.00 11.92           N  
-ANISOU 2565  N   GLN B 265     1603   1236   1689    449     56    389       N  
-ATOM   2566  CA  GLN B 265      57.628  18.326 -17.003  1.00 12.04           C  
-ANISOU 2566  CA  GLN B 265     1572   1452   1549    326    337    337       C  
-ATOM   2567  C   GLN B 265      58.113  17.984 -15.602  1.00 10.80           C  
-ANISOU 2567  C   GLN B 265     1429   1163   1512    212    242    195       C  
-ATOM   2568  O   GLN B 265      59.311  17.858 -15.341  1.00 11.62           O  
-ANISOU 2568  O   GLN B 265     1357   1131   1928     57    332    -10       O  
-ATOM   2569  CB  GLN B 265      58.795  18.570 -17.972  1.00 14.12           C  
-ANISOU 2569  CB  GLN B 265     1827   1557   1979    217    399    296       C  
-ATOM   2570  CG  GLN B 265      59.620  17.309 -18.243  1.00 14.21           C  
-ANISOU 2570  CG  GLN B 265     1730   1682   1985    221    755    -29       C  
-ATOM   2571  CD  GLN B 265      60.684  17.486 -19.311  1.00 15.02           C  
-ANISOU 2571  CD  GLN B 265     2054   1446   2205    309    560     85       C  
-ATOM   2572  OE1 GLN B 265      60.906  18.586 -19.817  1.00 19.61           O  
-ANISOU 2572  OE1 GLN B 265     2866   1599   2984    393   1196    114       O  
-ATOM   2573  NE2 GLN B 265      61.349  16.389 -19.664  1.00 14.42           N  
-ANISOU 2573  NE2 GLN B 265     1637   1549   2293    269    568     90       N  
-ATOM   2574  N   PHE B 266      57.162  17.854 -14.688  1.00 10.34           N  
-ANISOU 2574  N   PHE B 266     1485   1061   1382    374    316    150       N  
-ATOM   2575  CA  PHE B 266      57.492  17.468 -13.327  1.00  9.72           C  
-ANISOU 2575  CA  PHE B 266     1258   1025   1411    373    265    205       C  
-ATOM   2576  C   PHE B 266      58.165  16.097 -13.329  1.00 10.25           C  
-ANISOU 2576  C   PHE B 266     1317    903   1674    362    115    247       C  
-ATOM   2577  O   PHE B 266      57.933  15.271 -14.223  1.00 10.81           O  
-ANISOU 2577  O   PHE B 266     1346   1160   1602    112     -4     19       O  
-ATOM   2578  CB  PHE B 266      56.238  17.465 -12.451  1.00 10.16           C  
-ANISOU 2578  CB  PHE B 266     1169    984   1706    262    478     42       C  
-ATOM   2579  CG  PHE B 266      55.451  18.751 -12.511  1.00 10.23           C  
-ANISOU 2579  CG  PHE B 266     1364    858   1665    232    138    -51       C  
-ATOM   2580  CD1 PHE B 266      56.093  19.977 -12.577  1.00 11.59           C  
-ANISOU 2580  CD1 PHE B 266     1670    810   1922    353    255     19       C  
-ATOM   2581  CD2 PHE B 266      54.069  18.726 -12.515  1.00 11.02           C  
-ANISOU 2581  CD2 PHE B 266     1328   1218   1639    371    -83     19       C  
-ATOM   2582  CE1 PHE B 266      55.360  21.167 -12.639  1.00 11.65           C  
-ANISOU 2582  CE1 PHE B 266     1527   1110   1787    412    444    -78       C  
-ATOM   2583  CE2 PHE B 266      53.334  19.900 -12.579  1.00 11.63           C  
-ANISOU 2583  CE2 PHE B 266     1528   1430   1460    539    135     30       C  
-ATOM   2584  CZ  PHE B 266      53.983  21.120 -12.646  1.00 11.54           C  
-ANISOU 2584  CZ  PHE B 266     1624   1375   1386    370    127     63       C  
-ATOM   2585  N   GLN B 267      59.017  15.869 -12.340  1.00  9.86           N  
-ANISOU 2585  N   GLN B 267     1102    857   1786    241     75     99       N  
-ATOM   2586  CA  GLN B 267      59.735  14.599 -12.234  1.00  9.35           C  
-ANISOU 2586  CA  GLN B 267      891   1010   1651    167     97    175       C  
-ATOM   2587  C   GLN B 267      59.170  13.713 -11.130  1.00  9.46           C  
-ANISOU 2587  C   GLN B 267     1010    918   1667    -70    115    -29       C  
-ATOM   2588  O   GLN B 267      59.375  12.500 -11.138  1.00 10.13           O  
-ANISOU 2588  O   GLN B 267     1178    857   1812     34    151     15       O  
-ATOM   2589  CB  GLN B 267      61.234  14.842 -12.037  1.00  9.83           C  
-ANISOU 2589  CB  GLN B 267      862   1229   1644     -1    173    219       C  
-ATOM   2590  CG  GLN B 267      61.874  15.515 -13.232  1.00 10.87           C  
-ANISOU 2590  CG  GLN B 267     1293   1245   1590    121     78     25       C  
-ATOM   2591  CD  GLN B 267      61.658  14.720 -14.507  1.00 10.84           C  
-ANISOU 2591  CD  GLN B 267     1197   1246   1674     34    139    186       C  
-ATOM   2592  OE1 GLN B 267      62.030  13.548 -14.583  1.00 11.92           O  
-ANISOU 2592  OE1 GLN B 267     1535    987   2007    235    327    -68       O  
-ATOM   2593  NE2 GLN B 267      61.048  15.347 -15.510  1.00 11.79           N  
-ANISOU 2593  NE2 GLN B 267     1231   1336   1913     22    307    -82       N  
-ATOM   2594  N   ASN B 268      58.462  14.326 -10.186  1.00  9.55           N  
-ANISOU 2594  N   ASN B 268     1113   1096   1417    119    185     54       N  
-ATOM   2595  CA  ASN B 268      57.687  13.588  -9.197  1.00  9.68           C  
-ANISOU 2595  CA  ASN B 268     1065   1266   1345     28      2   -257       C  
-ATOM   2596  C   ASN B 268      56.212  13.544  -9.594  1.00 10.34           C  
-ANISOU 2596  C   ASN B 268     1032   1072   1823     31    143   -323       C  
-ATOM   2597  O   ASN B 268      55.748  14.367 -10.397  1.00 11.78           O  
-ANISOU 2597  O   ASN B 268     1312   1241   1923    106    -19     27       O  
-ATOM   2598  CB  ASN B 268      57.893  14.178  -7.802  1.00 10.20           C  
-ANISOU 2598  CB  ASN B 268     1027   1147   1702    127   -204   -294       C  
-ATOM   2599  CG  ASN B 268      59.286  13.902  -7.280  1.00  9.02           C  
-ANISOU 2599  CG  ASN B 268      810   1123   1494     41   -170   -231       C  
-ATOM   2600  OD1 ASN B 268      59.797  12.798  -7.460  1.00 10.76           O  
-ANISOU 2600  OD1 ASN B 268     1261    860   1965    263     81    -74       O  
-ATOM   2601  ND2 ASN B 268      59.920  14.901  -6.659  1.00 10.72           N  
-ANISOU 2601  ND2 ASN B 268      985   1317   1770    -65     19   -226       N  
-ATOM   2602  N   GLY B 269      55.494  12.557  -9.067  1.00  9.42           N  
-ANISOU 2602  N   GLY B 269      905    953   1720   -136     37   -258       N  
-ATOM   2603  CA  GLY B 269      54.109  12.335  -9.437  1.00  9.72           C  
-ANISOU 2603  CA  GLY B 269     1016   1117   1559     -8   -151   -339       C  
-ATOM   2604  C   GLY B 269      53.916  11.819 -10.854  1.00  9.90           C  
-ANISOU 2604  C   GLY B 269     1088   1055   1619    219   -148    -85       C  
-ATOM   2605  O   GLY B 269      52.838  11.990 -11.431  1.00 11.37           O  
-ANISOU 2605  O   GLY B 269     1107   1570   1643    215   -162   -254       O  
-ATOM   2606  N   ARG B 270      54.949  11.192 -11.416  1.00  9.59           N  
-ANISOU 2606  N   ARG B 270     1323    873   1448    252    -15   -167       N  
-ATOM   2607  CA  ARG B 270      54.911  10.733 -12.804  1.00  9.58           C  
-ANISOU 2607  CA  ARG B 270     1248    776   1616     -6    271   -203       C  
-ATOM   2608  C   ARG B 270      54.801   9.217 -12.865  1.00  9.46           C  
-ANISOU 2608  C   ARG B 270     1134    933   1525     44    126   -279       C  
-ATOM   2609  O   ARG B 270      55.677   8.495 -12.379  1.00 10.73           O  
-ANISOU 2609  O   ARG B 270     1293   1021   1764    317    -79    -74       O  
-ATOM   2610  CB  ARG B 270      56.152  11.198 -13.578  1.00 10.48           C  
-ANISOU 2610  CB  ARG B 270     1451    857   1674    202    377     50       C  
-ATOM   2611  CG  ARG B 270      56.382  12.711 -13.570  1.00  9.75           C  
-ANISOU 2611  CG  ARG B 270     1272    711   1722    154    -92     61       C  
-ATOM   2612  CD  ARG B 270      55.222  13.463 -14.230  1.00 10.68           C  
-ANISOU 2612  CD  ARG B 270     1395   1027   1636     95     26     52       C  
-ATOM   2613  NE  ARG B 270      54.993  13.024 -15.606  1.00 11.12           N  
-ANISOU 2613  NE  ARG B 270     1519   1286   1421    125   -115     14       N  
-ATOM   2614  CZ  ARG B 270      55.587  13.542 -16.677  1.00 10.07           C  
-ANISOU 2614  CZ  ARG B 270     1481    953   1392     16   -232    -64       C  
-ATOM   2615  NH1 ARG B 270      56.444  14.556 -16.552  1.00 11.22           N  
-ANISOU 2615  NH1 ARG B 270     1462    976   1823    139    166    -91       N  
-ATOM   2616  NH2 ARG B 270      55.319  13.051 -17.884  1.00 11.95           N  
-ANISOU 2616  NH2 ARG B 270     1589   1233   1717    119   -111   -193       N  
-ATOM   2617  N   VAL B 271      53.709   8.754 -13.458  1.00 10.20           N  
-ANISOU 2617  N   VAL B 271     1301    842   1731   -185    -30   -364       N  
-ATOM   2618  CA  VAL B 271      53.432   7.331 -13.584  1.00 11.10           C  
-ANISOU 2618  CA  VAL B 271     1562   1103   1553   -214   -259   -363       C  
-ATOM   2619  C   VAL B 271      52.443   7.146 -14.729  1.00 10.25           C  
-ANISOU 2619  C   VAL B 271     1485    960   1448   -283   -240   -368       C  
-ATOM   2620  O   VAL B 271      51.605   8.016 -14.981  1.00 12.95           O  
-ANISOU 2620  O   VAL B 271     1600   1416   1902    124   -441    -93       O  
-ATOM   2621  CB  VAL B 271      52.838   6.784 -12.270  1.00 12.12           C  
-ANISOU 2621  CB  VAL B 271     1649   1032   1923    -90    -63    -24       C  
-ATOM   2622  CG1 VAL B 271      51.430   7.332 -12.048  1.00 14.32           C  
-ANISOU 2622  CG1 VAL B 271     1762   1461   2218     80   -230   -202       C  
-ATOM   2623  CG2 VAL B 271      52.833   5.254 -12.263  1.00 13.16           C  
-ANISOU 2623  CG2 VAL B 271     2101    818   2080     54   -244    -35       C  
-ATOM   2624  N   THR B 272      52.545   6.025 -15.437  1.00 11.37           N  
-ANISOU 2624  N   THR B 272     1647   1220   1452   -121   -158   -312       N  
-ATOM   2625  CA  THR B 272      51.556   5.709 -16.454  1.00 12.27           C  
-ANISOU 2625  CA  THR B 272     1640   1526   1494   -136   -227   -494       C  
-ATOM   2626  C   THR B 272      50.317   5.124 -15.785  1.00 12.36           C  
-ANISOU 2626  C   THR B 272     1666   1397   1634   -108   -354   -491       C  
-ATOM   2627  O   THR B 272      50.367   4.696 -14.624  1.00 12.53           O  
-ANISOU 2627  O   THR B 272     1827   1227   1705    111   -315   -246       O  
-ATOM   2628  CB  THR B 272      52.095   4.691 -17.458  1.00 14.28           C  
-ANISOU 2628  CB  THR B 272     1882   1609   1934    133     98   -391       C  
-ATOM   2629  OG1 THR B 272      52.428   3.485 -16.763  1.00 14.92           O  
-ANISOU 2629  OG1 THR B 272     1986   1522   2159    193   -155   -370       O  
-ATOM   2630  CG2 THR B 272      53.339   5.228 -18.151  1.00 14.58           C  
-ANISOU 2630  CG2 THR B 272     1917   1738   1884    -58    248   -384       C  
-ATOM   2631  N   LEU B 273      49.210   5.081 -16.522  1.00 13.18           N  
-ANISOU 2631  N   LEU B 273     1833   1439   1734   -203   -299   -320       N  
-ATOM   2632  CA  LEU B 273      47.984   4.518 -15.978  1.00 13.95           C  
-ANISOU 2632  CA  LEU B 273     1592   1416   2292   -226   -224     10       C  
-ATOM   2633  C   LEU B 273      48.123   3.027 -15.663  1.00 13.57           C  
-ANISOU 2633  C   LEU B 273     1898   1236   2021   -180   -479   -258       C  
-ATOM   2634  O   LEU B 273      47.404   2.512 -14.803  1.00 15.21           O  
-ANISOU 2634  O   LEU B 273     1897   1384   2497   -119   -317   -230       O  
-ATOM   2635  CB  LEU B 273      46.798   4.766 -16.911  1.00 13.83           C  
-ANISOU 2635  CB  LEU B 273     1529   1566   2160      7   -327   -234       C  
-ATOM   2636  CG  LEU B 273      46.431   6.233 -17.149  1.00 14.37           C  
-ANISOU 2636  CG  LEU B 273     1749   1727   1983    103   -223   -294       C  
-ATOM   2637  CD1 LEU B 273      45.123   6.344 -17.931  1.00 16.69           C  
-ANISOU 2637  CD1 LEU B 273     1750   1961   2628     24   -509   -284       C  
-ATOM   2638  CD2 LEU B 273      46.342   7.000 -15.823  1.00 15.79           C  
-ANISOU 2638  CD2 LEU B 273     2051   1687   2260    237    140   -240       C  
-ATOM   2639  N   ASP B 274      49.044   2.337 -16.341  1.00 14.14           N  
-ANISOU 2639  N   ASP B 274     1955   1129   2286   -145   -545   -457       N  
-ATOM   2640  CA  ASP B 274      49.282   0.927 -16.025  1.00 16.01           C  
-ANISOU 2640  CA  ASP B 274     2192   1431   2460    -57   -674   -434       C  
-ATOM   2641  C   ASP B 274      50.399   0.707 -15.001  1.00 14.57           C  
-ANISOU 2641  C   ASP B 274     1930   1310   2297    -91   -451   -431       C  
-ATOM   2642  O   ASP B 274      50.866  -0.422 -14.806  1.00 16.41           O  
-ANISOU 2642  O   ASP B 274     2229   1180   2827     39   -406   -160       O  
-ATOM   2643  CB  ASP B 274      49.452   0.046 -17.277  1.00 17.77           C  
-ANISOU 2643  CB  ASP B 274     2499   1787   2465    176   -347   -809       C  
-ATOM   2644  CG  ASP B 274      50.699   0.369 -18.088  1.00 18.37           C  
-ANISOU 2644  CG  ASP B 274     2751   2073   2155    162   -283  -1016       C  
-ATOM   2645  OD1 ASP B 274      50.801  -0.154 -19.223  1.00 20.82           O  
-ANISOU 2645  OD1 ASP B 274     3009   2417   2483    -73    -58  -1028       O  
-ATOM   2646  OD2 ASP B 274      51.578   1.114 -17.616  1.00 19.17           O  
-ANISOU 2646  OD2 ASP B 274     2501   1941   2841      6   -231   -764       O  
-ATOM   2647  N   GLY B 275      50.797   1.790 -14.331  1.00 13.15           N  
-ANISOU 2647  N   GLY B 275     1573   1298   2126   -215   -397   -365       N  
-ATOM   2648  CA  GLY B 275      51.625   1.695 -13.141  1.00 13.38           C  
-ANISOU 2648  CA  GLY B 275     1379   1379   2324    -71   -407   -249       C  
-ATOM   2649  C   GLY B 275      53.134   1.670 -13.319  1.00 13.82           C  
-ANISOU 2649  C   GLY B 275     1590   1304   2358    133   -194   -142       C  
-ATOM   2650  O   GLY B 275      53.847   1.127 -12.469  1.00 16.09           O  
-ANISOU 2650  O   GLY B 275     1948   1726   2438    432   -496    -11       O  
-ATOM   2651  N   GLN B 276      53.629   2.263 -14.402  1.00 13.25           N  
-ANISOU 2651  N   GLN B 276     1614   1104   2315   -186   -164   -473       N  
-ATOM   2652  CA  GLN B 276      55.070   2.381 -14.612  1.00 13.33           C  
-ANISOU 2652  CA  GLN B 276     1700   1189   2175    -70   -258   -648       C  
-ATOM   2653  C   GLN B 276      55.563   3.738 -14.132  1.00 12.99           C  
-ANISOU 2653  C   GLN B 276     1648   1186   2099    194    -56   -347       C  
-ATOM   2654  O   GLN B 276      55.185   4.778 -14.681  1.00 14.07           O  
-ANISOU 2654  O   GLN B 276     1763   1211   2371    326   -407   -274       O  
-ATOM   2655  CB  GLN B 276      55.417   2.227 -16.092  1.00 15.54           C  
-ANISOU 2655  CB  GLN B 276     2031   1584   2288      2    -44   -882       C  
-ATOM   2656  CG  GLN B 276      55.011   0.899 -16.701  1.00 19.87           C  
-ANISOU 2656  CG  GLN B 276     2464   2490   2594    309    249  -1112       C  
-ATOM   2657  CD  GLN B 276      55.192   0.886 -18.208  1.00 26.39           C  
-ANISOU 2657  CD  GLN B 276     2931   3567   3529    188     -3  -1451       C  
-ATOM   2658  OE1 GLN B 276      54.220   0.835 -18.963  1.00 30.24           O  
-ANISOU 2658  OE1 GLN B 276     3452   3903   4135    161    -97  -1471       O  
-ATOM   2659  NE2 GLN B 276      56.442   0.941 -18.652  1.00 28.85           N  
-ANISOU 2659  NE2 GLN B 276     3012   3982   3967    186    204  -1115       N  
-ATOM   2660  N   LEU B 277      56.411   3.721 -13.109  1.00 12.64           N  
-ANISOU 2660  N   LEU B 277     1629   1100   2072    -24   -170   -463       N  
-ATOM   2661  CA  LEU B 277      56.956   4.949 -12.551  1.00 11.09           C  
-ANISOU 2661  CA  LEU B 277     1574   1012   1628    -52   -140   -172       C  
-ATOM   2662  C   LEU B 277      57.942   5.615 -13.505  1.00 11.32           C  
-ANISOU 2662  C   LEU B 277     1604    844   1854    -18    -35     21       C  
-ATOM   2663  O   LEU B 277      58.648   4.936 -14.246  1.00 14.52           O  
-ANISOU 2663  O   LEU B 277     1793   1299   2425    -26     24   -339       O  
-ATOM   2664  CB  LEU B 277      57.650   4.648 -11.224  1.00 12.15           C  
-ANISOU 2664  CB  LEU B 277     1696   1256   1665    193   -244   -230       C  
-ATOM   2665  CG  LEU B 277      56.749   4.145 -10.100  1.00 13.62           C  
-ANISOU 2665  CG  LEU B 277     1856   1526   1791    257    475    -52       C  
-ATOM   2666  CD1 LEU B 277      57.583   3.574  -8.986  1.00 16.10           C  
-ANISOU 2666  CD1 LEU B 277     2207   1752   2158    574    106    438       C  
-ATOM   2667  CD2 LEU B 277      55.887   5.285  -9.589  1.00 15.22           C  
-ANISOU 2667  CD2 LEU B 277     2021   1613   2147    511    304   -166       C  
-ATOM   2668  N   GLN B 278      57.985   6.946 -13.472  1.00 10.78           N  
-ANISOU 2668  N   GLN B 278     1434    748   1915    -60    -84    -16       N  
-ATOM   2669  CA  GLN B 278      58.910   7.729 -14.284  1.00 10.80           C  
-ANISOU 2669  CA  GLN B 278     1441   1035   1628     70   -149    -92       C  
-ATOM   2670  C   GLN B 278      59.585   8.825 -13.457  1.00 10.97           C  
-ANISOU 2670  C   GLN B 278     1231   1151   1784     86     48   -107       C  
-ATOM   2671  O   GLN B 278      59.126   9.169 -12.362  1.00 10.84           O  
-ANISOU 2671  O   GLN B 278     1400   1103   1614     79      2   -174       O  
-ATOM   2672  CB  GLN B 278      58.166   8.378 -15.454  1.00 12.36           C  
-ANISOU 2672  CB  GLN B 278     1549   1316   1831    117    119   -224       C  
-ATOM   2673  CG  GLN B 278      57.436   7.387 -16.367  1.00 12.98           C  
-ANISOU 2673  CG  GLN B 278     1924   1302   1704    -91   -261   -437       C  
-ATOM   2674  CD  GLN B 278      56.612   8.092 -17.422  1.00 16.04           C  
-ANISOU 2674  CD  GLN B 278     2566   1629   1897    138   -202   -205       C  
-ATOM   2675  OE1 GLN B 278      56.219   9.247 -17.247  1.00 18.19           O  
-ANISOU 2675  OE1 GLN B 278     2774   1733   2402    183   -482   -135       O  
-ATOM   2676  NE2 GLN B 278      56.352   7.409 -18.528  1.00 18.97           N  
-ANISOU 2676  NE2 GLN B 278     3007   2118   2081    408   -220   -532       N  
-ATOM   2677  N   GLY B 279      60.665   9.390 -13.993  1.00 11.36           N  
-ANISOU 2677  N   GLY B 279     1096   1311   1909    172     56   -158       N  
-ATOM   2678  CA  GLY B 279      61.364  10.466 -13.315  1.00 10.85           C  
-ANISOU 2678  CA  GLY B 279     1251   1174   1696    114    -94   -299       C  
-ATOM   2679  C   GLY B 279      61.944  10.016 -11.986  1.00 10.42           C  
-ANISOU 2679  C   GLY B 279     1157   1215   1585     51   -162   -119       C  
-ATOM   2680  O   GLY B 279      62.578   8.964 -11.898  1.00 12.49           O  
-ANISOU 2680  O   GLY B 279     1529   1152   2063    352    -82    -48       O  
-ATOM   2681  N   THR B 280      61.727  10.824 -10.952  1.00 10.10           N  
-ANISOU 2681  N   THR B 280     1153   1191   1492    -25     10   -128       N  
-ATOM   2682  CA  THR B 280      62.165  10.493  -9.601  1.00  9.93           C  
-ANISOU 2682  CA  THR B 280     1164   1007   1601    -48     32   -105       C  
-ATOM   2683  C   THR B 280      60.996  10.003  -8.740  1.00  9.53           C  
-ANISOU 2683  C   THR B 280      980   1009   1631    263    -56    -18       C  
-ATOM   2684  O   THR B 280      61.089   9.917  -7.515  1.00  9.98           O  
-ANISOU 2684  O   THR B 280     1095    923   1775     38     -9     41       O  
-ATOM   2685  CB  THR B 280      62.818  11.711  -8.933  1.00  9.37           C  
-ANISOU 2685  CB  THR B 280      807    884   1870     44    378   -117       C  
-ATOM   2686  OG1 THR B 280      61.941  12.840  -9.045  1.00 10.27           O  
-ANISOU 2686  OG1 THR B 280     1007    954   1941    273     67    -83       O  
-ATOM   2687  CG2 THR B 280      64.129  12.044  -9.628  1.00 11.11           C  
-ANISOU 2687  CG2 THR B 280      924   1005   2292    239    351    -80       C  
-ATOM   2688  N   THR B 281      59.892   9.661  -9.385  1.00 10.33           N  
-ANISOU 2688  N   THR B 281      982    923   2018    260    212     32       N  
-ATOM   2689  CA  THR B 281      58.678   9.303  -8.658  1.00 10.07           C  
-ANISOU 2689  CA  THR B 281     1109    864   1854    198   -161    164       C  
-ATOM   2690  C   THR B 281      58.835   8.027  -7.828  1.00 11.44           C  
-ANISOU 2690  C   THR B 281     1074    856   2417    164    -84      0       C  
-ATOM   2691  O   THR B 281      59.425   7.050  -8.290  1.00 15.47           O  
-ANISOU 2691  O   THR B 281     1453   1076   3350    246    629    422       O  
-ATOM   2692  CB  THR B 281      57.492   9.205  -9.637  1.00  9.94           C  
-ANISOU 2692  CB  THR B 281     1048   1082   1645    123    -69    -54       C  
-ATOM   2693  OG1 THR B 281      57.390  10.448 -10.333  1.00 10.87           O  
-ANISOU 2693  OG1 THR B 281     1152   1261   1717    148    -48    153       O  
-ATOM   2694  CG2 THR B 281      56.171   8.901  -8.914  1.00 11.44           C  
-ANISOU 2694  CG2 THR B 281      769   1572   2006    175    257     91       C  
-ATOM   2695  N   THR B 282      58.320   8.079  -6.602  1.00 12.14           N  
-ANISOU 2695  N   THR B 282     1405   1065   2141    -56     -1    337       N  
-ATOM   2696  CA  THR B 282      58.298   6.966  -5.663  1.00 15.27           C  
-ANISOU 2696  CA  THR B 282     1815   1429   2556   -195     46    404       C  
-ATOM   2697  C   THR B 282      56.874   6.501  -5.429  1.00 11.04           C  
-ANISOU 2697  C   THR B 282     1670    924   1599    -69    -96    125       C  
-ATOM   2698  O   THR B 282      55.909   7.192  -5.765  1.00 11.37           O  
-ANISOU 2698  O   THR B 282     1480    961   1877     53   -155    182       O  
-ATOM   2699  CB  THR B 282      58.846   7.382  -4.255  1.00 15.77           C  
-ANISOU 2699  CB  THR B 282     2241   1648   2103    278    144   -865       C  
-ATOM   2700  OG1 THR B 282      58.110   8.517  -3.760  1.00 17.99           O  
-ANISOU 2700  OG1 THR B 282     2222   2130   2484   -130     46   -256       O  
-ATOM   2701  CG2 THR B 282      60.298   7.745  -4.329  1.00 18.56           C  
-ANISOU 2701  CG2 THR B 282     2154   2238   2658    603   -244   -225       C  
-ATOM   2702  N   VAL B 283      56.748   5.353  -4.782  1.00 10.47           N  
-ANISOU 2702  N   VAL B 283     1432    722   1825   -219    114     61       N  
-ATOM   2703  CA  VAL B 283      55.439   4.861  -4.387  1.00 10.31           C  
-ANISOU 2703  CA  VAL B 283     1451    662   1805   -379     15    131       C  
-ATOM   2704  C   VAL B 283      54.885   5.692  -3.222  1.00 10.09           C  
-ANISOU 2704  C   VAL B 283     1356    970   1508   -194   -152     54       C  
-ATOM   2705  O   VAL B 283      53.741   6.136  -3.260  1.00 11.53           O  
-ANISOU 2705  O   VAL B 283     1369   1104   1906    133    -14     97       O  
-ATOM   2706  CB  VAL B 283      55.501   3.382  -3.988  1.00 10.86           C  
-ANISOU 2706  CB  VAL B 283     1536    701   1888   -380     67    201       C  
-ATOM   2707  CG1 VAL B 283      54.155   2.925  -3.446  1.00 15.06           C  
-ANISOU 2707  CG1 VAL B 283     1683   1025   3015   -239     70    517       C  
-ATOM   2708  CG2 VAL B 283      55.901   2.532  -5.193  1.00 14.17           C  
-ANISOU 2708  CG2 VAL B 283     2042   1133   2208    152   -135   -438       C  
-ATOM   2709  N   SER B 284      55.706   5.923  -2.201  1.00 10.00           N  
-ANISOU 2709  N   SER B 284     1317   1021   1462      2     86      9       N  
-ATOM   2710  CA  SER B 284      55.226   6.525  -0.962  1.00  9.86           C  
-ANISOU 2710  CA  SER B 284     1442    837   1466    244   -120     60       C  
-ATOM   2711  C   SER B 284      55.380   8.046  -0.880  1.00  9.07           C  
-ANISOU 2711  C   SER B 284     1270    645   1532     49     50     44       C  
-ATOM   2712  O   SER B 284      56.409   8.604  -1.266  1.00 10.99           O  
-ANISOU 2712  O   SER B 284     1111   1133   1930     -6    274    100       O  
-ATOM   2713  CB  SER B 284      55.943   5.893   0.226  1.00 10.96           C  
-ANISOU 2713  CB  SER B 284     1537   1303   1325    183    167    -33       C  
-ATOM   2714  OG  SER B 284      55.432   6.405   1.446  1.00 10.71           O  
-ANISOU 2714  OG  SER B 284     1389   1037   1643      0    -48     88       O  
-ATOM   2715  N   ALA B 285      54.364   8.703  -0.324  1.00  9.85           N  
-ANISOU 2715  N   ALA B 285     1306    892   1544    276     48   -198       N  
-ATOM   2716  CA  ALA B 285      54.438  10.139  -0.055  1.00 10.70           C  
-ANISOU 2716  CA  ALA B 285     1150   1021   1893    342     70   -270       C  
-ATOM   2717  C   ALA B 285      55.551  10.458   0.948  1.00 10.27           C  
-ANISOU 2717  C   ALA B 285     1243   1055   1602    418     45    329       C  
-ATOM   2718  O   ALA B 285      56.011  11.599   1.033  1.00 12.19           O  
-ANISOU 2718  O   ALA B 285     1521    967   2142    143    -62    124       O  
-ATOM   2719  CB  ALA B 285      53.101  10.664   0.445  1.00 11.60           C  
-ANISOU 2719  CB  ALA B 285     1222   1262   1921    501    224   -132       C  
-ATOM   2720  N   ALA B 286      55.979   9.454   1.712  1.00 10.17           N  
-ANISOU 2720  N   ALA B 286     1234   1103   1526    -42   -215    -91       N  
-ATOM   2721  CA  ALA B 286      57.054   9.645   2.685  1.00 10.20           C  
-ANISOU 2721  CA  ALA B 286     1386    957   1533     14     94    302       C  
-ATOM   2722  C   ALA B 286      58.399   9.995   2.039  1.00 10.66           C  
-ANISOU 2722  C   ALA B 286     1466    909   1676    -52    330    302       C  
-ATOM   2723  O   ALA B 286      59.318  10.454   2.724  1.00 13.17           O  
-ANISOU 2723  O   ALA B 286     1498   1493   2012   -212   -159    -38       O  
-ATOM   2724  CB  ALA B 286      57.199   8.411   3.589  1.00 12.14           C  
-ANISOU 2724  CB  ALA B 286     1722   1160   1731   -141   -177    371       C  
-ATOM   2725  N   CYS B 287      58.515   9.785   0.732  1.00  9.29           N  
-ANISOU 2725  N   CYS B 287     1239    937   1352    189    234     86       N  
-ATOM   2726  CA  CYS B 287      59.776  10.060   0.028  1.00  9.82           C  
-ANISOU 2726  CA  CYS B 287     1379    774   1577    152    122     57       C  
-ATOM   2727  C   CYS B 287      59.811  11.411  -0.679  1.00  9.26           C  
-ANISOU 2727  C   CYS B 287     1181    697   1639    105    -37    154       C  
-ATOM   2728  O   CYS B 287      60.861  11.837  -1.157  1.00 10.68           O  
-ANISOU 2728  O   CYS B 287     1139    941   1977    125     83     10       O  
-ATOM   2729  CB  CYS B 287      60.050   8.984  -1.013  1.00 10.35           C  
-ANISOU 2729  CB  CYS B 287     1588    630   1715    271    -33    -86       C  
-ATOM   2730  SG  CYS B 287      60.199   7.333  -0.332  1.00 13.69           S  
-ANISOU 2730  SG  CYS B 287     1777    947   2475    240     37     53       S  
-ATOM   2731  N   ILE B 288      58.662  12.073  -0.775  1.00  8.64           N  
-ANISOU 2731  N   ILE B 288     1032    582   1668    155   -161     70       N  
-ATOM   2732  CA  ILE B 288      58.554  13.267  -1.608  1.00  8.01           C  
-ANISOU 2732  CA  ILE B 288      856    496   1692     59   -249     33       C  
-ATOM   2733  C   ILE B 288      59.426  14.426  -1.116  1.00  8.28           C  
-ANISOU 2733  C   ILE B 288     1055    541   1551     26   -305   -131       C  
-ATOM   2734  O   ILE B 288      59.340  14.838   0.046  1.00  9.73           O  
-ANISOU 2734  O   ILE B 288     1123    941   1632     70   -180   -138       O  
-ATOM   2735  CB  ILE B 288      57.101  13.749  -1.719  1.00  8.97           C  
-ANISOU 2735  CB  ILE B 288      767    627   2013    111   -157     86       C  
-ATOM   2736  CG1 ILE B 288      56.204  12.688  -2.372  1.00  9.92           C  
-ANISOU 2736  CG1 ILE B 288      847    969   1953     95     10    -54       C  
-ATOM   2737  CG2 ILE B 288      57.043  15.040  -2.524  1.00 11.29           C  
-ANISOU 2737  CG2 ILE B 288     1261    792   2237    207    -31    390       C  
-ATOM   2738  CD1 ILE B 288      54.724  12.995  -2.234  1.00 10.82           C  
-ANISOU 2738  CD1 ILE B 288      957    988   2167     98    -96    159       C  
-ATOM   2739  N   ALA B 289      60.263  14.932  -2.020  1.00  8.97           N  
-ANISOU 2739  N   ALA B 289     1020    545   1842    -69    -67    172       N  
-ATOM   2740  CA  ALA B 289      61.088  16.123  -1.794  1.00  9.71           C  
-ANISOU 2740  CA  ALA B 289     1040    788   1860     85   -149    -91       C  
-ATOM   2741  C   ALA B 289      62.108  15.925  -0.679  1.00  9.63           C  
-ANISOU 2741  C   ALA B 289     1247    727   1683    -12   -232   -328       C  
-ATOM   2742  O   ALA B 289      62.394  16.834   0.092  1.00 13.19           O  
-ANISOU 2742  O   ALA B 289     1908    846   2256    319   -593   -309       O  
-ATOM   2743  CB  ALA B 289      60.221  17.373  -1.543  1.00 11.54           C  
-ANISOU 2743  CB  ALA B 289     1281    805   2299    230   -260   -347       C  
-ATOM   2744  N   ARG B 290      62.670  14.724  -0.622  1.00  9.25           N  
-ANISOU 2744  N   ARG B 290      929    792   1794    176    -87    -95       N  
-ATOM   2745  CA  ARG B 290      63.703  14.394   0.346  1.00  8.77           C  
-ANISOU 2745  CA  ARG B 290      938    891   1503     13      3   -109       C  
-ATOM   2746  C   ARG B 290      64.992  14.003  -0.353  1.00  9.06           C  
-ANISOU 2746  C   ARG B 290     1021    798   1624    242     42    -59       C  
-ATOM   2747  O   ARG B 290      64.992  13.690  -1.548  1.00 10.40           O  
-ANISOU 2747  O   ARG B 290     1103   1177   1671    214   -114   -161       O  
-ATOM   2748  CB  ARG B 290      63.220  13.281   1.281  1.00  9.60           C  
-ANISOU 2748  CB  ARG B 290     1075   1016   1554     33    203    169       C  
-ATOM   2749  CG  ARG B 290      62.063  13.740   2.150  1.00 11.61           C  
-ANISOU 2749  CG  ARG B 290     1314   1257   1841   -144    555     30       C  
-ATOM   2750  CD  ARG B 290      61.625  12.659   3.119  1.00 15.39           C  
-ANISOU 2750  CD  ARG B 290     1869   1420   2558   -221    767    443       C  
-ATOM   2751  NE  ARG B 290      60.461  13.064   3.893  1.00 16.08           N  
-ANISOU 2751  NE  ARG B 290     2238   1936   1934   -324    521     92       N  
-ATOM   2752  CZ  ARG B 290      60.490  13.404   5.180  1.00 19.61           C  
-ANISOU 2752  CZ  ARG B 290     2401   2340   2708   -169    135   -101       C  
-ATOM   2753  NH1 ARG B 290      61.636  13.395   5.848  1.00 22.99           N  
-ANISOU 2753  NH1 ARG B 290     2900   2439   3397   -109   -977   -170       N  
-ATOM   2754  NH2 ARG B 290      59.367  13.749   5.804  1.00 21.75           N  
-ANISOU 2754  NH2 ARG B 290     2682   2521   3061    -19    360     99       N  
-ATOM   2755  N   MET B 291      66.089  14.049   0.398  1.00 10.05           N  
-ANISOU 2755  N   MET B 291      920    865   2032    223    -55      0       N  
-ATOM   2756  CA  MET B 291      67.398  13.638  -0.090  1.00 10.65           C  
-ANISOU 2756  CA  MET B 291      970   1053   2021    227     31     71       C  
-ATOM   2757  C   MET B 291      68.094  12.840   0.991  1.00  9.72           C  
-ANISOU 2757  C   MET B 291      900    936   1858     90    141     23       C  
-ATOM   2758  O   MET B 291      67.746  12.939   2.166  1.00  9.49           O  
-ANISOU 2758  O   MET B 291      987   1012   1605     60    -28   -152       O  
-ATOM   2759  CB  MET B 291      68.283  14.850  -0.403  1.00 10.58           C  
-ANISOU 2759  CB  MET B 291     1037    811   2173    -65    -53    160       C  
-ATOM   2760  CG  MET B 291      67.678  15.903  -1.307  1.00 11.37           C  
-ANISOU 2760  CG  MET B 291     1160    879   2279   -236     64     76       C  
-ATOM   2761  SD  MET B 291      68.828  17.285  -1.412  1.00 11.94           S  
-ANISOU 2761  SD  MET B 291     1222   1101   2213    -67    -73    -85       S  
-ATOM   2762  CE  MET B 291      67.844  18.478  -2.330  1.00 12.06           C  
-ANISOU 2762  CE  MET B 291     1254   1062   2267    165   -303     85       C  
-ATOM   2763  N   ARG B 292      69.107  12.076   0.594  1.00 10.37           N  
-ANISOU 2763  N   ARG B 292      742   1135   2062    193    -94    -34       N  
-ATOM   2764  CA  ARG B 292      69.951  11.382   1.559  1.00 10.20           C  
-ANISOU 2764  CA  ARG B 292      635   1013   2225    -80   -164    -20       C  
-ATOM   2765  C   ARG B 292      71.374  11.350   1.045  1.00  9.86           C  
-ANISOU 2765  C   ARG B 292      658   1071   2017   -125   -159     33       C  
-ATOM   2766  O   ARG B 292      71.602  11.254  -0.163  1.00 11.04           O  
-ANISOU 2766  O   ARG B 292     1013   1265   1916     93    108    -52       O  
-ATOM   2767  CB  ARG B 292      69.458   9.954   1.791  1.00  9.88           C  
-ANISOU 2767  CB  ARG B 292      992    771   1989     64   -231    149       C  
-ATOM   2768  CG  ARG B 292      70.324   9.158   2.766  1.00 10.42           C  
-ANISOU 2768  CG  ARG B 292      958    792   2210     61   -138    101       C  
-ATOM   2769  CD  ARG B 292      69.637   7.860   3.169  1.00 10.35           C  
-ANISOU 2769  CD  ARG B 292     1014    833   2083    -19   -252    169       C  
-ATOM   2770  NE  ARG B 292      70.456   7.074   4.088  1.00 12.00           N  
-ANISOU 2770  NE  ARG B 292     1413   1094   2053    354   -391     -7       N  
-ATOM   2771  CZ  ARG B 292      69.968   6.171   4.928  1.00 13.36           C  
-ANISOU 2771  CZ  ARG B 292     1619   1238   2220    279   -470     96       C  
-ATOM   2772  NH1 ARG B 292      68.662   5.940   4.966  1.00 12.93           N  
-ANISOU 2772  NH1 ARG B 292     1778   1196   1939     10   -198     77       N  
-ATOM   2773  NH2 ARG B 292      70.782   5.492   5.722  1.00 14.49           N  
-ANISOU 2773  NH2 ARG B 292     1689   1280   2536    275   -494     30       N  
-ATOM   2774  N   GLY B 293      72.328  11.440   1.960  1.00 10.62           N  
-ANISOU 2774  N   GLY B 293      627   1182   2226     72   -125   -218       N  
-ATOM   2775  CA  GLY B 293      73.711  11.239   1.570  1.00 12.00           C  
-ANISOU 2775  CA  GLY B 293      691   1433   2435     -4   -222   -161       C  
-ATOM   2776  C   GLY B 293      74.676  11.644   2.651  1.00 11.80           C  
-ANISOU 2776  C   GLY B 293      738   1531   2215     81    112   -103       C  
-ATOM   2777  O   GLY B 293      74.287  11.947   3.780  1.00 14.57           O  
-ANISOU 2777  O   GLY B 293      946   2254   2336    101    -95   -108       O  
-ATOM   2778  N   ARG B 294      75.953  11.642   2.290  1.00 12.13           N  
-ANISOU 2778  N   ARG B 294      714   1474   2420      9   -231   -140       N  
-ATOM   2779  CA  ARG B 294      77.018  11.961   3.226  1.00 13.14           C  
-ANISOU 2779  CA  ARG B 294      849   1544   2599    -34   -177   -247       C  
-ATOM   2780  C   ARG B 294      77.581  13.342   2.916  1.00 14.29           C  
-ANISOU 2780  C   ARG B 294     1097   1711   2620     38    -15   -365       C  
-ATOM   2781  O   ARG B 294      77.927  13.654   1.775  1.00 15.09           O  
-ANISOU 2781  O   ARG B 294     1173   1931   2629   -284     74   -275       O  
-ATOM   2782  CB  ARG B 294      78.113  10.889   3.177  1.00 16.22           C  
-ANISOU 2782  CB  ARG B 294     1143   2300   2719    341   -217   -390       C  
-ATOM   2783  CG  ARG B 294      79.068  10.909   4.371  1.00 19.23           C  
-ANISOU 2783  CG  ARG B 294     1592   2450   3264    379   -381   -377       C  
-ATOM   2784  CD  ARG B 294      80.021   9.707   4.371  1.00 20.87           C  
-ANISOU 2784  CD  ARG B 294     1644   2564   3720    379   -177     52       C  
-ATOM   2785  NE  ARG B 294      79.296   8.441   4.406  1.00 21.79           N  
-ANISOU 2785  NE  ARG B 294     2029   2476   3775    536   -168   -130       N  
-ATOM   2786  CZ  ARG B 294      78.879   7.841   5.519  1.00 24.13           C  
-ANISOU 2786  CZ  ARG B 294     2335   2479   4352    609   -309    165       C  
-ATOM   2787  NH1 ARG B 294      79.113   8.385   6.706  1.00 21.30           N  
-ANISOU 2787  NH1 ARG B 294     2060   2192   3842    400   -469   -183       N  
-ATOM   2788  NH2 ARG B 294      78.218   6.696   5.445  1.00 26.81           N  
-ANISOU 2788  NH2 ARG B 294     2694   2594   4896    610   -318   -187       N  
-ATOM   2789  N   ILE B 295      77.654  14.179   3.940  1.00 13.72           N  
-ANISOU 2789  N   ILE B 295     1012   1530   2669   -110   -301   -284       N  
-ATOM   2790  CA  ILE B 295      78.151  15.538   3.769  1.00 14.53           C  
-ANISOU 2790  CA  ILE B 295     1035   1741   2745   -357     -4   -338       C  
-ATOM   2791  C   ILE B 295      79.675  15.534   3.672  1.00 14.76           C  
-ANISOU 2791  C   ILE B 295     1148   1856   2605   -471    -46   -100       C  
-ATOM   2792  O   ILE B 295      80.353  14.814   4.410  1.00 16.71           O  
-ANISOU 2792  O   ILE B 295     1268   1891   3189    -86   -399     58       O  
-ATOM   2793  CB  ILE B 295      77.660  16.444   4.913  1.00 14.31           C  
-ANISOU 2793  CB  ILE B 295     1023   1669   2745   -484   -204   -136       C  
-ATOM   2794  CG1 ILE B 295      76.151  16.676   4.771  1.00 15.16           C  
-ANISOU 2794  CG1 ILE B 295      992   1902   2864   -387   -226   -379       C  
-ATOM   2795  CG2 ILE B 295      78.400  17.775   4.922  1.00 16.33           C  
-ANISOU 2795  CG2 ILE B 295     1234   1707   3262   -552   -130    -92       C  
-ATOM   2796  CD1 ILE B 295      75.516  17.390   5.949  1.00 15.60           C  
-ANISOU 2796  CD1 ILE B 295     1397   1800   2729   -202    -95   -538       C  
-ATOM   2797  N   PHE B 296      80.203  16.315   2.735  1.00 15.60           N  
-ANISOU 2797  N   PHE B 296     1089   2114   2724   -512    128    -73       N  
-ATOM   2798  CA  PHE B 296      81.648  16.438   2.571  1.00 17.23           C  
-ANISOU 2798  CA  PHE B 296     1126   2391   3029   -641    243   -273       C  
-ATOM   2799  C   PHE B 296      82.085  17.891   2.534  1.00 18.44           C  
-ANISOU 2799  C   PHE B 296     1217   2473   3316   -553   -222   -323       C  
-ATOM   2800  O   PHE B 296      81.273  18.797   2.335  1.00 17.59           O  
-ANISOU 2800  O   PHE B 296     1297   2316   3070   -474   -166   -111       O  
-ATOM   2801  CB  PHE B 296      82.126  15.722   1.302  1.00 20.23           C  
-ANISOU 2801  CB  PHE B 296     1318   2700   3668   -451    327   -650       C  
-ATOM   2802  CG  PHE B 296      81.604  16.323   0.025  1.00 21.15           C  
-ANISOU 2802  CG  PHE B 296     1421   2880   3735   -676    345   -913       C  
-ATOM   2803  CD1 PHE B 296      82.219  17.433  -0.537  1.00 23.53           C  
-ANISOU 2803  CD1 PHE B 296     1624   3279   4036   -445    225   -619       C  
-ATOM   2804  CD2 PHE B 296      80.506  15.771  -0.620  1.00 21.64           C  
-ANISOU 2804  CD2 PHE B 296     1381   3255   3587   -625    457   -927       C  
-ATOM   2805  CE1 PHE B 296      81.747  17.989  -1.714  1.00 23.39           C  
-ANISOU 2805  CE1 PHE B 296     1552   3215   4119   -600      4   -818       C  
-ATOM   2806  CE2 PHE B 296      80.033  16.316  -1.798  1.00 22.95           C  
-ANISOU 2806  CE2 PHE B 296     1395   3348   3975   -660    461   -573       C  
-ATOM   2807  CZ  PHE B 296      80.650  17.431  -2.346  1.00 23.46           C  
-ANISOU 2807  CZ  PHE B 296     1491   3451   3972   -650    313   -782       C  
-ATOM   2808  N   ASN B 297      83.380  18.106   2.739  1.00 19.78           N  
-ANISOU 2808  N   ASN B 297     1392   2602   3519   -861   -140   -173       N  
-ATOM   2809  CA  ASN B 297      83.972  19.429   2.635  1.00 19.99           C  
-ANISOU 2809  CA  ASN B 297     1570   2709   3315   -964    -16   -262       C  
-ATOM   2810  C   ASN B 297      85.257  19.326   1.834  1.00 21.25           C  
-ANISOU 2810  C   ASN B 297     1577   3084   3412  -1132     56    -73       C  
-ATOM   2811  O   ASN B 297      86.250  18.777   2.307  1.00 25.42           O  
-ANISOU 2811  O   ASN B 297     1631   3856   4169   -513   -194    -83       O  
-ATOM   2812  CB  ASN B 297      84.262  19.998   4.024  1.00 21.64           C  
-ANISOU 2812  CB  ASN B 297     1900   2691   3631  -1217   -204   -277       C  
-ATOM   2813  CG  ASN B 297      85.075  21.285   3.975  1.00 23.71           C  
-ANISOU 2813  CG  ASN B 297     2470   2940   3599   -812   -232   -437       C  
-ATOM   2814  OD1 ASN B 297      85.211  21.916   2.925  1.00 24.19           O  
-ANISOU 2814  OD1 ASN B 297     2706   2770   3714   -814    -61   -288       O  
-ATOM   2815  ND2 ASN B 297      85.610  21.681   5.118  1.00 26.11           N  
-ANISOU 2815  ND2 ASN B 297     2701   3209   4008   -929   -431   -460       N  
-ATOM   2816  N   ASN B 298      85.217  19.825   0.604  1.00 21.30           N  
-ANISOU 2816  N   ASN B 298     1718   3211   3162  -1203    124   -338       N  
-ATOM   2817  CA  ASN B 298      86.406  19.880  -0.236  1.00 24.22           C  
-ANISOU 2817  CA  ASN B 298     2248   3247   3705  -1320    -71   -713       C  
-ATOM   2818  C   ASN B 298      86.921  21.308  -0.340  1.00 26.04           C  
-ANISOU 2818  C   ASN B 298     2393   3351   4149  -1327    466   -449       C  
-ATOM   2819  O   ASN B 298      86.360  22.122  -1.073  1.00 25.92           O  
-ANISOU 2819  O   ASN B 298     2505   3521   3820  -1149    480   -617       O  
-ATOM   2820  CB  ASN B 298      86.107  19.341  -1.636  1.00 30.33           C  
-ANISOU 2820  CB  ASN B 298     2994   3664   4864   -668   -251  -1050       C  
-ATOM   2821  CG  ASN B 298      85.863  17.846  -1.646  1.00 37.00           C  
-ANISOU 2821  CG  ASN B 298     3533   4372   6154   -142   -691  -1374       C  
-ATOM   2822  OD1 ASN B 298      86.508  17.096  -0.915  1.00 40.24           O  
-ANISOU 2822  OD1 ASN B 298     3860   4544   6885    171   -702  -1453       O  
-ATOM   2823  ND2 ASN B 298      84.927  17.403  -2.478  1.00 39.64           N  
-ANISOU 2823  ND2 ASN B 298     3705   4799   6557     96   -752  -1570       N  
-ATOM   2824  N   ASN B 299      87.978  21.611   0.404  1.00 27.79           N  
-ANISOU 2824  N   ASN B 299     2627   3401   4531  -1077    266   -866       N  
-ATOM   2825  CA  ASN B 299      88.628  22.915   0.311  1.00 29.10           C  
-ANISOU 2825  CA  ASN B 299     2837   3255   4965  -1137    466   -674       C  
-ATOM   2826  C   ASN B 299      87.667  24.085   0.543  1.00 25.47           C  
-ANISOU 2826  C   ASN B 299     2511   3131   4035  -1252    431   -587       C  
-ATOM   2827  O   ASN B 299      87.781  25.123  -0.099  1.00 24.50           O  
-ANISOU 2827  O   ASN B 299     2536   3021   3753  -1141    358   -955       O  
-ATOM   2828  CB  ASN B 299      89.307  23.060  -1.057  1.00 34.28           C  
-ANISOU 2828  CB  ASN B 299     3263   3613   6149   -941    885     15       C  
-ATOM   2829  CG  ASN B 299      90.273  24.233  -1.117  1.00 40.22           C  
-ANISOU 2829  CG  ASN B 299     3789   4305   7187   -551    809    328       C  
-ATOM   2830  OD1 ASN B 299      91.035  24.475  -0.181  1.00 40.65           O  
-ANISOU 2830  OD1 ASN B 299     3810   4307   7329   -719    732     22       O  
-ATOM   2831  ND2 ASN B 299      90.243  24.968  -2.225  1.00 42.68           N  
-ANISOU 2831  ND2 ASN B 299     4076   4390   7748   -395    765    611       N  
-ATOM   2832  N   GLY B 300      86.720  23.915   1.459  1.00 23.63           N  
-ANISOU 2832  N   GLY B 300     2459   3049   3468  -1097    101   -824       N  
-ATOM   2833  CA  GLY B 300      85.787  24.983   1.769  1.00 25.54           C  
-ANISOU 2833  CA  GLY B 300     2669   3280   3756   -744    140   -467       C  
-ATOM   2834  C   GLY B 300      84.540  24.927   0.914  1.00 25.32           C  
-ANISOU 2834  C   GLY B 300     2560   3239   3819   -854    336   -230       C  
-ATOM   2835  O   GLY B 300      83.633  25.747   1.065  1.00 28.64           O  
-ANISOU 2835  O   GLY B 300     3005   3723   4152   -284    445     94       O  
-ATOM   2836  N   ASN B 301      84.499  23.962   0.001  1.00 23.06           N  
-ANISOU 2836  N   ASN B 301     2177   3012   3573  -1439    222   -132       N  
-ATOM   2837  CA  ASN B 301      83.293  23.690  -0.770  1.00 24.43           C  
-ANISOU 2837  CA  ASN B 301     2382   3033   3867  -1284    382     55       C  
-ATOM   2838  C   ASN B 301      82.538  22.515  -0.157  1.00 23.09           C  
-ANISOU 2838  C   ASN B 301     1988   2722   4064  -1113     33   -121       C  
-ATOM   2839  O   ASN B 301      83.019  21.385  -0.181  1.00 22.22           O  
-ANISOU 2839  O   ASN B 301     1892   2810   3738   -860    353     58       O  
-ATOM   2840  CB  ASN B 301      83.647  23.376  -2.223  1.00 27.33           C  
-ANISOU 2840  CB  ASN B 301     2932   3323   4129  -1239    -39    392       C  
-ATOM   2841  CG  ASN B 301      84.525  24.442  -2.853  1.00 32.20           C  
-ANISOU 2841  CG  ASN B 301     3350   3885   5000   -925    -86    632       C  
-ATOM   2842  OD1 ASN B 301      84.043  25.503  -3.249  1.00 32.21           O  
-ANISOU 2842  OD1 ASN B 301     3605   3928   4704   -694   -471    767       O  
-ATOM   2843  ND2 ASN B 301      85.820  24.159  -2.958  1.00 35.42           N  
-ANISOU 2843  ND2 ASN B 301     3555   4279   5625   -639    184    584       N  
-ATOM   2844  N   TYR B 302      81.360  22.785   0.395  1.00 20.38           N  
-ANISOU 2844  N   TYR B 302     1712   2384   3645  -1033   -129    -46       N  
-ATOM   2845  CA  TYR B 302      80.573  21.749   1.059  1.00 17.56           C  
-ANISOU 2845  CA  TYR B 302     1562   2150   2960  -1001   -177   -147       C  
-ATOM   2846  C   TYR B 302      79.565  21.139   0.100  1.00 15.66           C  
-ANISOU 2846  C   TYR B 302     1325   1890   2733   -835     21    -37       C  
-ATOM   2847  O   TYR B 302      79.106  21.790  -0.836  1.00 17.18           O  
-ANISOU 2847  O   TYR B 302     1346   1942   3239   -462    257    -96       O  
-ATOM   2848  CB  TYR B 302      79.840  22.315   2.278  1.00 17.86           C  
-ANISOU 2848  CB  TYR B 302     1706   2421   2659   -818   -332   -162       C  
-ATOM   2849  CG  TYR B 302      80.768  22.811   3.360  1.00 18.75           C  
-ANISOU 2849  CG  TYR B 302     1878   2428   2818   -723   -496   -434       C  
-ATOM   2850  CD1 TYR B 302      81.084  22.010   4.450  1.00 21.05           C  
-ANISOU 2850  CD1 TYR B 302     2123   2843   3032   -645   -420   -183       C  
-ATOM   2851  CD2 TYR B 302      81.343  24.071   3.279  1.00 21.33           C  
-ANISOU 2851  CD2 TYR B 302     2280   2384   3441   -602   -641   -580       C  
-ATOM   2852  CE1 TYR B 302      81.943  22.452   5.434  1.00 21.83           C  
-ANISOU 2852  CE1 TYR B 302     2290   2719   3285   -697   -785   -394       C  
-ATOM   2853  CE2 TYR B 302      82.199  24.521   4.257  1.00 23.33           C  
-ANISOU 2853  CE2 TYR B 302     2467   2793   3603   -465   -940   -280       C  
-ATOM   2854  CZ  TYR B 302      82.493  23.713   5.330  1.00 22.82           C  
-ANISOU 2854  CZ  TYR B 302     2470   2793   3406   -772   -999   -187       C  
-ATOM   2855  OH  TYR B 302      83.349  24.167   6.301  1.00 25.01           O  
-ANISOU 2855  OH  TYR B 302     2589   3146   3767   -884  -1067   -192       O  
-ATOM   2856  N   GLY B 303      79.216  19.887   0.346  1.00 15.87           N  
-ANISOU 2856  N   GLY B 303     1334   1742   2953   -690    -33   -296       N  
-ATOM   2857  CA  GLY B 303      78.286  19.202  -0.528  1.00 15.86           C  
-ANISOU 2857  CA  GLY B 303     1408   1686   2931   -636   -178   -214       C  
-ATOM   2858  C   GLY B 303      77.758  17.930   0.087  1.00 13.91           C  
-ANISOU 2858  C   GLY B 303     1258   1566   2462   -492   -113     79       C  
-ATOM   2859  O   GLY B 303      78.127  17.577   1.211  1.00 14.71           O  
-ANISOU 2859  O   GLY B 303     1301   1765   2523   -392   -115      1       O  
-ATOM   2860  N   VAL B 304      76.884  17.252  -0.650  1.00 13.86           N  
-ANISOU 2860  N   VAL B 304     1276   1573   2417   -338     77     77       N  
-ATOM   2861  CA  VAL B 304      76.410  15.940  -0.252  1.00 13.10           C  
-ANISOU 2861  CA  VAL B 304     1122   1465   2391   -447    359   -109       C  
-ATOM   2862  C   VAL B 304      76.677  14.951  -1.378  1.00 14.88           C  
-ANISOU 2862  C   VAL B 304     1191   2006   2456   -139      3   -118       C  
-ATOM   2863  O   VAL B 304      76.388  15.235  -2.545  1.00 15.25           O  
-ANISOU 2863  O   VAL B 304     1216   1898   2678   -144     27   -114       O  
-ATOM   2864  CB  VAL B 304      74.895  15.945   0.069  1.00 15.29           C  
-ANISOU 2864  CB  VAL B 304     1182   1546   3080   -331    441   -240       C  
-ATOM   2865  CG1 VAL B 304      74.402  14.524   0.343  1.00 15.32           C  
-ANISOU 2865  CG1 VAL B 304     1263   1231   3325   -240    378    -46       C  
-ATOM   2866  CG2 VAL B 304      74.611  16.815   1.277  1.00 17.87           C  
-ANISOU 2866  CG2 VAL B 304     1647   1775   3366   -218    185   -614       C  
-ATOM   2867  N   ASN B 305      77.265  13.809  -1.026  1.00 14.15           N  
-ANISOU 2867  N   ASN B 305     1043   1897   2436   -139    167   -495       N  
-ATOM   2868  CA  ASN B 305      77.344  12.676  -1.931  1.00 15.12           C  
-ANISOU 2868  CA  ASN B 305      888   2053   2802    -29     26   -216       C  
-ATOM   2869  C   ASN B 305      76.076  11.861  -1.737  1.00 13.46           C  
-ANISOU 2869  C   ASN B 305      967   1803   2342     24    186   -177       C  
-ATOM   2870  O   ASN B 305      75.872  11.256  -0.685  1.00 13.62           O  
-ANISOU 2870  O   ASN B 305     1050   1702   2421     82    -43    -91       O  
-ATOM   2871  CB  ASN B 305      78.594  11.833  -1.655  1.00 17.90           C  
-ANISOU 2871  CB  ASN B 305     1004   2499   3296   -242    379   -374       C  
-ATOM   2872  CG  ASN B 305      79.870  12.524  -2.097  1.00 21.10           C  
-ANISOU 2872  CG  ASN B 305     1568   3201   3246   -197    214   -586       C  
-ATOM   2873  OD1 ASN B 305      79.922  13.126  -3.171  1.00 24.05           O  
-ANISOU 2873  OD1 ASN B 305     1802   3475   3860   -278    261   -774       O  
-ATOM   2874  ND2 ASN B 305      80.905  12.448  -1.268  1.00 23.83           N  
-ANISOU 2874  ND2 ASN B 305     1797   3581   3677     43   -186   -901       N  
-ATOM   2875  N   LEU B 306      75.218  11.881  -2.752  1.00 12.83           N  
-ANISOU 2875  N   LEU B 306      883   1798   2192    -62    215   -214       N  
-ATOM   2876  CA  LEU B 306      73.857  11.379  -2.636  1.00 11.80           C  
-ANISOU 2876  CA  LEU B 306      982   1328   2171   -147      8   -103       C  
-ATOM   2877  C   LEU B 306      73.748   9.859  -2.663  1.00 12.46           C  
-ANISOU 2877  C   LEU B 306     1064   1226   2443    201   -125    -83       C  
-ATOM   2878  O   LEU B 306      74.573   9.168  -3.264  1.00 14.17           O  
-ANISOU 2878  O   LEU B 306     1212   1388   2784    323    225   -184       O  
-ATOM   2879  CB  LEU B 306      72.987  11.971  -3.747  1.00 12.93           C  
-ANISOU 2879  CB  LEU B 306     1165   1388   2359   -212   -199    168       C  
-ATOM   2880  CG  LEU B 306      72.809  13.489  -3.732  1.00 12.18           C  
-ANISOU 2880  CG  LEU B 306     1330   1297   1999     43    114     19       C  
-ATOM   2881  CD1 LEU B 306      72.231  13.963  -5.059  1.00 12.95           C  
-ANISOU 2881  CD1 LEU B 306     1420   1773   1727     87   -147    105       C  
-ATOM   2882  CD2 LEU B 306      71.914  13.898  -2.565  1.00 13.42           C  
-ANISOU 2882  CD2 LEU B 306     1429   1586   2083     33    125    -44       C  
-ATOM   2883  N   ALA B 307      72.699   9.366  -2.015  1.00 11.76           N  
-ANISOU 2883  N   ALA B 307     1093   1176   2200    -40    102   -202       N  
-ATOM   2884  CA  ALA B 307      72.302   7.969  -2.058  1.00 11.20           C  
-ANISOU 2884  CA  ALA B 307      894   1148   2213   -121     47     26       C  
-ATOM   2885  C   ALA B 307      70.787   7.937  -2.213  1.00 10.33           C  
-ANISOU 2885  C   ALA B 307      969   1049   1906   -172     38    -29       C  
-ATOM   2886  O   ALA B 307      70.126   8.982  -2.127  1.00 11.76           O  
-ANISOU 2886  O   ALA B 307     1179    838   2451    122     20   -105       O  
-ATOM   2887  CB  ALA B 307      72.713   7.266  -0.771  1.00 13.14           C  
-ANISOU 2887  CB  ALA B 307     1162   1501   2327    356   -119    106       C  
-ATOM   2888  N   GLU B 308      70.228   6.751  -2.437  1.00 10.52           N  
-ANISOU 2888  N   GLU B 308      955   1013   2027   -227     19    -34       N  
-ATOM   2889  CA  GLU B 308      68.776   6.600  -2.355  1.00  9.96           C  
-ANISOU 2889  CA  GLU B 308      964    887   1931   -219    145   -387       C  
-ATOM   2890  C   GLU B 308      68.339   6.789  -0.903  1.00 10.36           C  
-ANISOU 2890  C   GLU B 308      981    905   2051    174     33   -266       C  
-ATOM   2891  O   GLU B 308      69.158   6.688   0.023  1.00 10.63           O  
-ANISOU 2891  O   GLU B 308      962   1019   2057    112    -54   -129       O  
-ATOM   2892  CB  GLU B 308      68.331   5.227  -2.873  1.00 11.18           C  
-ANISOU 2892  CB  GLU B 308     1331    792   2125     53     63   -301       C  
-ATOM   2893  CG  GLU B 308      68.754   4.938  -4.318  1.00 11.74           C  
-ANISOU 2893  CG  GLU B 308     1525    996   1940    187   -128   -196       C  
-ATOM   2894  CD  GLU B 308      67.932   5.685  -5.376  1.00 12.89           C  
-ANISOU 2894  CD  GLU B 308     1501   1222   2172     74    115   -441       C  
-ATOM   2895  OE1 GLU B 308      66.959   6.393  -5.039  1.00 13.84           O  
-ANISOU 2895  OE1 GLU B 308     1761   1561   1935    394      7   -309       O  
-ATOM   2896  OE2 GLU B 308      68.257   5.550  -6.569  1.00 15.59           O  
-ANISOU 2896  OE2 GLU B 308     1688   2092   2142    280    202    -91       O  
-ATOM   2897  N   LEU B 309      67.052   7.063  -0.695  1.00 10.86           N  
-ANISOU 2897  N   LEU B 309     1018    962   2145    210    109     -5       N  
-ATOM   2898  CA  LEU B 309      66.548   7.381   0.647  1.00 10.73           C  
-ANISOU 2898  CA  LEU B 309      913    984   2181    204    -73    -70       C  
-ATOM   2899  C   LEU B 309      66.677   6.244   1.658  1.00 11.13           C  
-ANISOU 2899  C   LEU B 309     1204    799   2227    114   -225   -226       C  
-ATOM   2900  O   LEU B 309      66.703   6.485   2.863  1.00 11.78           O  
-ANISOU 2900  O   LEU B 309     1263    986   2226    166   -146   -225       O  
-ATOM   2901  CB  LEU B 309      65.096   7.872   0.583  1.00 11.56           C  
-ANISOU 2901  CB  LEU B 309      949    947   2494    239   -276     66       C  
-ATOM   2902  CG  LEU B 309      64.931   9.222  -0.114  1.00 11.98           C  
-ANISOU 2902  CG  LEU B 309     1105    811   2636     99   -295     74       C  
-ATOM   2903  CD1 LEU B 309      63.450   9.568  -0.249  1.00 15.03           C  
-ANISOU 2903  CD1 LEU B 309     1101   1286   3322    217   -522   -233       C  
-ATOM   2904  CD2 LEU B 309      65.662  10.334   0.640  1.00 13.55           C  
-ANISOU 2904  CD2 LEU B 309     1397    937   2814    114   -443   -327       C  
-ATOM   2905  N   ASP B 310      66.767   5.006   1.174  1.00 10.88           N  
-ANISOU 2905  N   ASP B 310     1141    680   2311    104    -40     18       N  
-ATOM   2906  CA  ASP B 310      66.991   3.867   2.067  1.00 12.48           C  
-ANISOU 2906  CA  ASP B 310     1444    885   2413     78     12     41       C  
-ATOM   2907  C   ASP B 310      68.473   3.643   2.384  1.00 12.51           C  
-ANISOU 2907  C   ASP B 310     1372   1170   2209    299    102     82       C  
-ATOM   2908  O   ASP B 310      68.821   2.746   3.148  1.00 15.31           O  
-ANISOU 2908  O   ASP B 310     1873   1411   2533    625     78    311       O  
-ATOM   2909  CB  ASP B 310      66.333   2.590   1.529  1.00 14.20           C  
-ANISOU 2909  CB  ASP B 310     1913    931   2550    -10    135   -304       C  
-ATOM   2910  CG  ASP B 310      66.981   2.072   0.258  1.00 14.88           C  
-ANISOU 2910  CG  ASP B 310     2222    743   2688    -68    226     67       C  
-ATOM   2911  OD1 ASP B 310      67.890   2.732  -0.284  1.00 14.00           O  
-ANISOU 2911  OD1 ASP B 310     1753   1087   2478    135    153    -33       O  
-ATOM   2912  OD2 ASP B 310      66.570   0.978  -0.202  1.00 19.44           O  
-ANISOU 2912  OD2 ASP B 310     2888   1019   3477    -58    523   -151       O  
-ATOM   2913  N   GLY B 311      69.340   4.465   1.802  1.00 12.00           N  
-ANISOU 2913  N   GLY B 311     1105   1214   2241    282     58   -202       N  
-ATOM   2914  CA  GLY B 311      70.759   4.398   2.102  1.00 13.81           C  
-ANISOU 2914  CA  GLY B 311     1405   1311   2531    517    203     86       C  
-ATOM   2915  C   GLY B 311      71.578   3.586   1.119  1.00 14.85           C  
-ANISOU 2915  C   GLY B 311     1697   1247   2696    367    -86     24       C  
-ATOM   2916  O   GLY B 311      72.813   3.593   1.176  1.00 17.81           O  
-ANISOU 2916  O   GLY B 311     1525   1782   3461    600    189    -28       O  
-ATOM   2917  N   ASN B 312      70.898   2.878   0.224  1.00 13.71           N  
-ANISOU 2917  N   ASN B 312     1673   1192   2342    395    500    129       N  
-ATOM   2918  CA  ASN B 312      71.584   2.138  -0.829  1.00 16.07           C  
-ANISOU 2918  CA  ASN B 312     1857   1392   2855    391    493   -300       C  
-ATOM   2919  C   ASN B 312      72.067   3.089  -1.918  1.00 14.70           C  
-ANISOU 2919  C   ASN B 312     1610   1316   2658    402    200     17       C  
-ATOM   2920  O   ASN B 312      71.551   4.194  -2.042  1.00 14.40           O  
-ANISOU 2920  O   ASN B 312     1606   1097   2769    494     65     55       O  
-ATOM   2921  CB  ASN B 312      70.673   1.052  -1.396  1.00 19.91           C  
-ANISOU 2921  CB  ASN B 312     2411   1629   3523    494   1029   -283       C  
-ATOM   2922  CG  ASN B 312      70.476  -0.092  -0.429  1.00 24.46           C  
-ANISOU 2922  CG  ASN B 312     2740   1703   4849    520   1297     78       C  
-ATOM   2923  OD1 ASN B 312      71.442  -0.698   0.040  1.00 28.37           O  
-ANISOU 2923  OD1 ASN B 312     3086   2186   5508    838   1566    762       O  
-ATOM   2924  ND2 ASN B 312      69.223  -0.389  -0.113  1.00 25.99           N  
-ANISOU 2924  ND2 ASN B 312     2850   1799   5226    530   1328     56       N  
-ATOM   2925  N   PRO B 313      73.070   2.676  -2.699  1.00 15.00           N  
-ANISOU 2925  N   PRO B 313     1754   1315   2630    690    365    403       N  
-ATOM   2926  CA  PRO B 313      73.683   3.621  -3.638  1.00 16.19           C  
-ANISOU 2926  CA  PRO B 313     1762   1582   2808    668    526    836       C  
-ATOM   2927  C   PRO B 313      72.730   4.073  -4.733  1.00 16.28           C  
-ANISOU 2927  C   PRO B 313     1933   1439   2812    506    264    366       C  
-ATOM   2928  O   PRO B 313      71.858   3.308  -5.151  1.00 16.75           O  
-ANISOU 2928  O   PRO B 313     1980   1783   2599    361    200    168       O  
-ATOM   2929  CB  PRO B 313      74.836   2.819  -4.258  1.00 17.98           C  
-ANISOU 2929  CB  PRO B 313     1822   1754   3253    759    754    610       C  
-ATOM   2930  CG  PRO B 313      75.075   1.690  -3.318  1.00 21.15           C  
-ANISOU 2930  CG  PRO B 313     2220   2033   3783    910    935    762       C  
-ATOM   2931  CD  PRO B 313      73.762   1.376  -2.677  1.00 17.50           C  
-ANISOU 2931  CD  PRO B 313     1885   1737   3025    826    728    447       C  
-ATOM   2932  N   TYR B 314      72.894   5.314  -5.178  1.00 15.72           N  
-ANISOU 2932  N   TYR B 314     2049   1499   2424    618    274    337       N  
-ATOM   2933  CA  TYR B 314      72.185   5.800  -6.347  1.00 17.37           C  
-ANISOU 2933  CA  TYR B 314     2384   1671   2544    898    630    107       C  
-ATOM   2934  C   TYR B 314      73.021   5.463  -7.573  1.00 21.62           C  
-ANISOU 2934  C   TYR B 314     2803   2405   3005    975    879    402       C  
-ATOM   2935  O   TYR B 314      74.141   5.955  -7.726  1.00 21.83           O  
-ANISOU 2935  O   TYR B 314     2839   2616   2839    769    927    553       O  
-ATOM   2936  CB  TYR B 314      71.939   7.311  -6.244  1.00 15.80           C  
-ANISOU 2936  CB  TYR B 314     2289   1202   2511    497    520    350       C  
-ATOM   2937  CG  TYR B 314      71.490   7.953  -7.537  1.00 15.38           C  
-ANISOU 2937  CG  TYR B 314     2136   1491   2216    566    396    293       C  
-ATOM   2938  CD1 TYR B 314      70.329   7.540  -8.181  1.00 15.48           C  
-ANISOU 2938  CD1 TYR B 314     1773   1620   2487    450    660    314       C  
-ATOM   2939  CD2 TYR B 314      72.227   8.980  -8.107  1.00 17.21           C  
-ANISOU 2939  CD2 TYR B 314     2272   1540   2726    292    474    543       C  
-ATOM   2940  CE1 TYR B 314      69.923   8.129  -9.364  1.00 15.25           C  
-ANISOU 2940  CE1 TYR B 314     1929   1726   2138    673    696    457       C  
-ATOM   2941  CE2 TYR B 314      71.831   9.572  -9.289  1.00 16.26           C  
-ANISOU 2941  CE2 TYR B 314     2181   1567   2429    319     83    507       C  
-ATOM   2942  CZ  TYR B 314      70.680   9.145  -9.911  1.00 14.59           C  
-ANISOU 2942  CZ  TYR B 314     2053   1433   2058    482    454    513       C  
-ATOM   2943  OH  TYR B 314      70.292   9.747 -11.084  1.00 16.79           O  
-ANISOU 2943  OH  TYR B 314     2143   1717   2519    538    328    532       O  
-ATOM   2944  N   HIS B 315      72.477   4.608  -8.433  1.00 23.52           N  
-ANISOU 2944  N   HIS B 315     3221   2724   2989   1490    978     88       N  
-ATOM   2945  CA  HIS B 315      73.212   4.102  -9.587  1.00 28.51           C  
-ANISOU 2945  CA  HIS B 315     4054   3147   3631   1886   1037    189       C  
-ATOM   2946  C   HIS B 315      72.879   4.826 -10.890  1.00 28.70           C  
-ANISOU 2946  C   HIS B 315     4022   3456   3427   1856   1049     96       C  
-ATOM   2947  O   HIS B 315      73.551   4.627 -11.901  1.00 30.17           O  
-ANISOU 2947  O   HIS B 315     4015   3532   3914   1741    994    -38       O  
-ATOM   2948  CB  HIS B 315      72.985   2.594  -9.744  1.00 31.80           C  
-ANISOU 2948  CB  HIS B 315     4651   3350   4081   2126   1047    250       C  
-ATOM   2949  CG  HIS B 315      73.684   1.767  -8.710  1.00 37.26           C  
-ANISOU 2949  CG  HIS B 315     5394   3757   5006   2416   1046    467       C  
-ATOM   2950  ND1 HIS B 315      73.007   0.990  -7.793  1.00 40.48           N  
-ANISOU 2950  ND1 HIS B 315     5731   3826   5822   2363    708    560       N  
-ATOM   2951  CD2 HIS B 315      75.002   1.597  -8.445  1.00 38.25           C  
-ANISOU 2951  CD2 HIS B 315     5502   3847   5185   2531   1019    646       C  
-ATOM   2952  CE1 HIS B 315      73.877   0.373  -7.014  1.00 40.41           C  
-ANISOU 2952  CE1 HIS B 315     5678   3887   5788   2512    803    823       C  
-ATOM   2953  NE2 HIS B 315      75.095   0.725  -7.386  1.00 40.44           N  
-ANISOU 2953  NE2 HIS B 315     5711   4007   5645   2644    920    554       N  
-ATOM   2954  N   ALA B 316      71.846   5.663 -10.858  1.00 26.82           N  
-ANISOU 2954  N   ALA B 316     3805   3508   2878   1805    872   -227       N  
-ATOM   2955  CA  ALA B 316      71.434   6.449 -12.022  1.00 27.21           C  
-ANISOU 2955  CA  ALA B 316     4175   3281   2883   1694   1308    289       C  
-ATOM   2956  C   ALA B 316      71.003   5.604 -13.228  1.00 30.05           C  
-ANISOU 2956  C   ALA B 316     4502   3463   3453   1712    988    157       C  
-ATOM   2957  O   ALA B 316      71.104   6.048 -14.372  1.00 32.78           O  
-ANISOU 2957  O   ALA B 316     5002   3895   3556   1679    157     72       O  
-ATOM   2958  CB  ALA B 316      72.532   7.431 -12.423  1.00 28.51           C  
-ANISOU 2958  CB  ALA B 316     4185   3132   3515   1611   1095    627       C  
-ATOM   2959  N   PHE B 317      70.511   4.396 -12.972  1.00 29.51           N  
-ANISOU 2959  N   PHE B 317     4293   3407   3510   1940    735   -481       N  
-ATOM   2960  CA  PHE B 317      70.035   3.531 -14.046  1.00 31.03           C  
-ANISOU 2960  CA  PHE B 317     4582   3422   3786   2074    381   -548       C  
-ATOM   2961  C   PHE B 317      68.629   3.916 -14.489  1.00 30.10           C  
-ANISOU 2961  C   PHE B 317     4663   3084   3690   1456     85   -690       C  
-ATOM   2962  O   PHE B 317      68.267   3.749 -15.655  1.00 32.05           O  
-ANISOU 2962  O   PHE B 317     4949   3415   3811   1376   -301   -908       O  
-ATOM   2963  CB  PHE B 317      70.020   2.068 -13.594  1.00 36.80           C  
-ANISOU 2963  CB  PHE B 317     4898   4112   4970   2562    274   -490       C  
-ATOM   2964  CG  PHE B 317      71.382   1.487 -13.346  1.00 42.78           C  
-ANISOU 2964  CG  PHE B 317     5167   4864   6223   2795    330   -383       C  
-ATOM   2965  CD1 PHE B 317      72.513   2.043 -13.928  1.00 43.94           C  
-ANISOU 2965  CD1 PHE B 317     5150   5162   6384   2961    419   -400       C  
-ATOM   2966  CD2 PHE B 317      71.531   0.377 -12.531  1.00 45.27           C  
-ANISOU 2966  CD2 PHE B 317     5270   5128   6803   2775    279   -256       C  
-ATOM   2967  CE1 PHE B 317      73.764   1.506 -13.695  1.00 45.92           C  
-ANISOU 2967  CE1 PHE B 317     5266   5460   6722   3021    405   -204       C  
-ATOM   2968  CE2 PHE B 317      72.779  -0.169 -12.296  1.00 46.93           C  
-ANISOU 2968  CE2 PHE B 317     5285   5421   7126   2853    432   -179       C  
-ATOM   2969  CZ  PHE B 317      73.898   0.395 -12.879  1.00 47.33           C  
-ANISOU 2969  CZ  PHE B 317     5326   5471   7184   2922    326   -112       C  
-ATOM   2970  N   ASP B 318      67.846   4.433 -13.549  1.00 27.30           N  
-ANISOU 2970  N   ASP B 318     4226   2210   3937   1317    516   -611       N  
-ATOM   2971  CA  ASP B 318      66.404   4.545 -13.728  1.00 27.96           C  
-ANISOU 2971  CA  ASP B 318     4253   2058   4311    875    451   -116       C  
-ATOM   2972  C   ASP B 318      65.883   5.973 -13.645  1.00 23.47           C  
-ANISOU 2972  C   ASP B 318     3535   1774   3607    601     -2   -237       C  
-ATOM   2973  O   ASP B 318      64.812   6.273 -14.164  1.00 24.85           O  
-ANISOU 2973  O   ASP B 318     3492   1741   4208    318      1   -421       O  
-ATOM   2974  CB  ASP B 318      65.688   3.701 -12.667  1.00 32.78           C  
-ANISOU 2974  CB  ASP B 318     5014   2000   5441    739    735     71       C  
-ATOM   2975  CG  ASP B 318      66.218   2.289 -12.594  1.00 40.28           C  
-ANISOU 2975  CG  ASP B 318     5721   2651   6932    840    721   -404       C  
-ATOM   2976  OD1 ASP B 318      66.496   1.710 -13.662  1.00 41.27           O  
-ANISOU 2976  OD1 ASP B 318     5980   2799   6901    845    818  -1161       O  
-ATOM   2977  OD2 ASP B 318      66.362   1.762 -11.470  1.00 43.62           O  
-ANISOU 2977  OD2 ASP B 318     6099   2778   7697    801    672   -426       O  
-ATOM   2978  N   SER B 319      66.625   6.855 -12.986  1.00 18.19           N  
-ANISOU 2978  N   SER B 319     2840   1300   2770    321    -51   -144       N  
-ATOM   2979  CA  SER B 319      66.084   8.172 -12.662  1.00 15.03           C  
-ANISOU 2979  CA  SER B 319     2379   1415   1915    259    225    -61       C  
-ATOM   2980  C   SER B 319      67.144   9.262 -12.762  1.00 15.47           C  
-ANISOU 2980  C   SER B 319     2000   1507   2372    314    184    271       C  
-ATOM   2981  O   SER B 319      68.342   8.976 -12.644  1.00 16.24           O  
-ANISOU 2981  O   SER B 319     1766   1812   2591    400    420     36       O  
-ATOM   2982  CB  SER B 319      65.468   8.150 -11.264  1.00 15.19           C  
-ANISOU 2982  CB  SER B 319     2192   1998   1582    206   -422    208       C  
-ATOM   2983  OG  SER B 319      66.432   7.743 -10.311  1.00 16.65           O  
-ANISOU 2983  OG  SER B 319     2345   1919   2062    354    -72    169       O  
-ATOM   2984  N   PRO B 320      66.703  10.513 -12.995  1.00 14.16           N  
-ANISOU 2984  N   PRO B 320     1732   1555   2091    451     92   -125       N  
-ATOM   2985  CA  PRO B 320      67.597  11.660 -13.197  1.00 14.41           C  
-ANISOU 2985  CA  PRO B 320     1802   1577   2097    259    249    186       C  
-ATOM   2986  C   PRO B 320      68.251  12.124 -11.901  1.00 12.49           C  
-ANISOU 2986  C   PRO B 320     1362   1258   2124     10    359    176       C  
-ATOM   2987  O   PRO B 320      69.171  12.940 -11.929  1.00 13.94           O  
-ANISOU 2987  O   PRO B 320     1263   1442   2591     65    493     96       O  
-ATOM   2988  CB  PRO B 320      66.659  12.739 -13.728  1.00 15.20           C  
-ANISOU 2988  CB  PRO B 320     1976   1559   2240    420    -24    230       C  
-ATOM   2989  CG  PRO B 320      65.341  12.404 -13.151  1.00 16.01           C  
-ANISOU 2989  CG  PRO B 320     1765   1460   2857    350     94    290       C  
-ATOM   2990  CD  PRO B 320      65.285  10.899 -13.129  1.00 13.38           C  
-ANISOU 2990  CD  PRO B 320     1779   1206   2098    387   -243    -79       C  
-ATOM   2991  N   ALA B 321      67.762  11.605 -10.781  1.00 12.51           N  
-ANISOU 2991  N   ALA B 321     1427   1536   1789    101    205    119       N  
-ATOM   2992  CA  ALA B 321      68.318  11.857  -9.465  1.00 11.30           C  
-ANISOU 2992  CA  ALA B 321     1326   1001   1967     12    271    -48       C  
-ATOM   2993  C   ALA B 321      67.789  10.725  -8.590  1.00 11.52           C  
-ANISOU 2993  C   ALA B 321     1029   1313   2036    125    176   -126       C  
-ATOM   2994  O   ALA B 321      66.957   9.940  -9.034  1.00 11.48           O  
-ANISOU 2994  O   ALA B 321     1198   1276   1887    128    247    -24       O  
-ATOM   2995  CB  ALA B 321      67.846  13.215  -8.932  1.00 12.82           C  
-ANISOU 2995  CB  ALA B 321     1303    913   2654     11    254    207       C  
-ATOM   2996  N   PRO B 322      68.254  10.630  -7.340  1.00 11.43           N  
-ANISOU 2996  N   PRO B 322      966   1183   2192   -136    182   -339       N  
-ATOM   2997  CA  PRO B 322      67.670   9.600  -6.469  1.00 10.82           C  
-ANISOU 2997  CA  PRO B 322      865   1302   1943   -134      6   -176       C  
-ATOM   2998  C   PRO B 322      66.153   9.752  -6.348  1.00 10.05           C  
-ANISOU 2998  C   PRO B 322     1003    919   1895    -38    141   -147       C  
-ATOM   2999  O   PRO B 322      65.617  10.864  -6.455  1.00 10.86           O  
-ANISOU 2999  O   PRO B 322     1119    921   2085     31    385    -44       O  
-ATOM   3000  CB  PRO B 322      68.350   9.856  -5.125  1.00 12.10           C  
-ANISOU 3000  CB  PRO B 322      947   1465   2186   -171    -40   -119       C  
-ATOM   3001  CG  PRO B 322      69.657  10.500  -5.490  1.00 12.04           C  
-ANISOU 3001  CG  PRO B 322     1080   1473   2021     52   -117     20       C  
-ATOM   3002  CD  PRO B 322      69.359  11.353  -6.690  1.00 11.78           C  
-ANISOU 3002  CD  PRO B 322     1227   1298   1951    -26   -169   -219       C  
-ATOM   3003  N   LEU B 323      65.454   8.644  -6.136  1.00 10.16           N  
-ANISOU 3003  N   LEU B 323      962   1016   1880    -98     20   -136       N  
-ATOM   3004  CA  LEU B 323      63.998   8.722  -6.037  1.00  9.64           C  
-ANISOU 3004  CA  LEU B 323      971    763   1928   -129    175   -103       C  
-ATOM   3005  C   LEU B 323      63.579   9.682  -4.918  1.00  8.75           C  
-ANISOU 3005  C   LEU B 323     1044    733   1547    -89    -89   -132       C  
-ATOM   3006  O   LEU B 323      64.215   9.727  -3.856  1.00 10.09           O  
-ANISOU 3006  O   LEU B 323     1133    915   1786    -42      2   -156       O  
-ATOM   3007  CB  LEU B 323      63.385   7.334  -5.822  1.00 10.97           C  
-ANISOU 3007  CB  LEU B 323     1275    756   2135    -44    179   -322       C  
-ATOM   3008  CG  LEU B 323      63.715   6.303  -6.903  1.00 10.86           C  
-ANISOU 3008  CG  LEU B 323     1423    910   1793    189     70   -510       C  
-ATOM   3009  CD1 LEU B 323      62.930   5.027  -6.634  1.00 14.12           C  
-ANISOU 3009  CD1 LEU B 323     1579    985   2801   -190    207   -580       C  
-ATOM   3010  CD2 LEU B 323      63.409   6.849  -8.303  1.00 12.60           C  
-ANISOU 3010  CD2 LEU B 323     1583   1271   1932    236     22   -550       C  
-ATOM   3011  N   GLY B 324      62.531  10.469  -5.182  1.00  9.03           N  
-ANISOU 3011  N   GLY B 324      935    687   1809    229     82    -36       N  
-ATOM   3012  CA  GLY B 324      61.996  11.412  -4.212  1.00  9.53           C  
-ANISOU 3012  CA  GLY B 324      900    990   1732     50    417   -243       C  
-ATOM   3013  C   GLY B 324      62.628  12.797  -4.271  1.00  8.71           C  
-ANISOU 3013  C   GLY B 324      721    930   1656   -262    247    152       C  
-ATOM   3014  O   GLY B 324      62.103  13.746  -3.687  1.00 10.55           O  
-ANISOU 3014  O   GLY B 324     1144    877   1986    118    253    -24       O  
-ATOM   3015  N   PHE B 325      63.746  12.925  -4.975  1.00  8.65           N  
-ANISOU 3015  N   PHE B 325      790    757   1739   -257     21     94       N  
-ATOM   3016  CA  PHE B 325      64.497  14.176  -5.006  1.00  9.63           C  
-ANISOU 3016  CA  PHE B 325      738    887   2032   -102    253     -8       C  
-ATOM   3017  C   PHE B 325      63.582  15.339  -5.407  1.00  9.53           C  
-ANISOU 3017  C   PHE B 325      852    895   1874    167    -77     95       C  
-ATOM   3018  O   PHE B 325      62.768  15.198  -6.314  1.00 10.14           O  
-ANISOU 3018  O   PHE B 325     1060   1055   1738      3     -9     41       O  
-ATOM   3019  CB  PHE B 325      65.650  14.053  -6.008  1.00 10.91           C  
-ANISOU 3019  CB  PHE B 325      764   1160   2219    -13    280    -70       C  
-ATOM   3020  CG  PHE B 325      66.769  15.034  -5.782  1.00 11.19           C  
-ANISOU 3020  CG  PHE B 325     1004   1171   2077    -23    210    -34       C  
-ATOM   3021  CD1 PHE B 325      67.815  14.730  -4.920  1.00 13.82           C  
-ANISOU 3021  CD1 PHE B 325     1116   1657   2477     34    301   -642       C  
-ATOM   3022  CD2 PHE B 325      66.783  16.252  -6.444  1.00 12.45           C  
-ANISOU 3022  CD2 PHE B 325     1304   1150   2275   -139    740   -304       C  
-ATOM   3023  CE1 PHE B 325      68.849  15.633  -4.719  1.00 14.52           C  
-ANISOU 3023  CE1 PHE B 325     1261   1807   2450    -53    387   -910       C  
-ATOM   3024  CE2 PHE B 325      67.808  17.156  -6.242  1.00 15.43           C  
-ANISOU 3024  CE2 PHE B 325     1446   1564   2852   -187    719   -135       C  
-ATOM   3025  CZ  PHE B 325      68.842  16.844  -5.382  1.00 15.96           C  
-ANISOU 3025  CZ  PHE B 325     1398   1843   2823    -95    570   -623       C  
-ATOM   3026  N   PRO B 326      63.711  16.496  -4.735  1.00  9.92           N  
-ANISOU 3026  N   PRO B 326      985    756   2029     -9   -102     43       N  
-ATOM   3027  CA  PRO B 326      62.859  17.632  -5.134  1.00  9.99           C  
-ANISOU 3027  CA  PRO B 326     1162    928   1706    -84   -308    -75       C  
-ATOM   3028  C   PRO B 326      62.991  17.972  -6.625  1.00 10.19           C  
-ANISOU 3028  C   PRO B 326     1010   1046   1816   -117   -247    -50       C  
-ATOM   3029  O   PRO B 326      64.094  17.913  -7.169  1.00 11.66           O  
-ANISOU 3029  O   PRO B 326     1282   1273   1874     -8     14    193       O  
-ATOM   3030  CB  PRO B 326      63.388  18.797  -4.280  1.00 11.87           C  
-ANISOU 3030  CB  PRO B 326     1486   1027   1995    222   -169   -278       C  
-ATOM   3031  CG  PRO B 326      64.073  18.160  -3.120  1.00 14.23           C  
-ANISOU 3031  CG  PRO B 326     1406   1171   2829    382   -687   -462       C  
-ATOM   3032  CD  PRO B 326      64.591  16.816  -3.599  1.00 10.49           C  
-ANISOU 3032  CD  PRO B 326     1260    699   2025    136   -443   -332       C  
-ATOM   3033  N   ASP B 327      61.885  18.343  -7.269  1.00  9.40           N  
-ANISOU 3033  N   ASP B 327     1125    737   1707    -33   -115    164       N  
-ATOM   3034  CA  ASP B 327      61.912  18.723  -8.685  1.00 10.23           C  
-ANISOU 3034  CA  ASP B 327     1220    752   1914    119    -28     68       C  
-ATOM   3035  C   ASP B 327      61.621  20.212  -8.919  1.00 10.18           C  
-ANISOU 3035  C   ASP B 327     1165    732   1972    -38     33     44       C  
-ATOM   3036  O   ASP B 327      61.055  20.606  -9.952  1.00 11.40           O  
-ANISOU 3036  O   ASP B 327     1396   1067   1869      5    -75    165       O  
-ATOM   3037  CB  ASP B 327      61.007  17.820  -9.539  1.00 11.62           C  
-ANISOU 3037  CB  ASP B 327     1137    958   2320     10    176   -104       C  
-ATOM   3038  CG  ASP B 327      59.524  18.037  -9.287  1.00 10.70           C  
-ANISOU 3038  CG  ASP B 327     1316    855   1894    183    -31   -327       C  
-ATOM   3039  OD1 ASP B 327      59.153  18.801  -8.372  1.00 10.65           O  
-ANISOU 3039  OD1 ASP B 327     1185    895   1965    166     91   -104       O  
-ATOM   3040  OD2 ASP B 327      58.723  17.415 -10.019  1.00 11.49           O  
-ANISOU 3040  OD2 ASP B 327     1361   1048   1955    161    -23   -208       O  
-ATOM   3041  N   PHE B 328      62.054  21.038  -7.968  1.00  9.75           N  
-ANISOU 3041  N   PHE B 328     1248    578   1876    -56    209   -117       N  
-ATOM   3042  CA  PHE B 328      61.966  22.489  -8.106  1.00 10.22           C  
-ANISOU 3042  CA  PHE B 328     1371    809   1701    -19    378     77       C  
-ATOM   3043  C   PHE B 328      63.291  23.005  -8.633  1.00 10.82           C  
-ANISOU 3043  C   PHE B 328     1462    947   1702   -118     61     29       C  
-ATOM   3044  O   PHE B 328      64.325  22.820  -7.996  1.00 12.52           O  
-ANISOU 3044  O   PHE B 328     1448   1241   2069    -88     25    -83       O  
-ATOM   3045  CB  PHE B 328      61.618  23.117  -6.759  1.00 10.52           C  
-ANISOU 3045  CB  PHE B 328     1336    817   1844    -76    181    -86       C  
-ATOM   3046  CG  PHE B 328      60.285  22.669  -6.233  1.00 10.68           C  
-ANISOU 3046  CG  PHE B 328     1309    903   1845   -158    196    -69       C  
-ATOM   3047  CD1 PHE B 328      59.114  23.165  -6.788  1.00 12.36           C  
-ANISOU 3047  CD1 PHE B 328     1388   1385   1923    165    116     18       C  
-ATOM   3048  CD2 PHE B 328      60.201  21.710  -5.232  1.00 11.93           C  
-ANISOU 3048  CD2 PHE B 328     1406   1403   1723     48    225     69       C  
-ATOM   3049  CE1 PHE B 328      57.877  22.735  -6.333  1.00 12.32           C  
-ANISOU 3049  CE1 PHE B 328     1506   1411   1763      3    214    108       C  
-ATOM   3050  CE2 PHE B 328      58.966  21.278  -4.769  1.00 12.38           C  
-ANISOU 3050  CE2 PHE B 328     1598   1358   1749     48    311    171       C  
-ATOM   3051  CZ  PHE B 328      57.805  21.794  -5.323  1.00 12.07           C  
-ANISOU 3051  CZ  PHE B 328     1577   1249   1759    159    -79     29       C  
-ATOM   3052  N   GLY B 329      63.262  23.629  -9.810  1.00 11.07           N  
-ANISOU 3052  N   GLY B 329     1445   1016   1744   -217    321    116       N  
-ATOM   3053  CA  GLY B 329      64.485  24.059 -10.468  1.00 12.10           C  
-ANISOU 3053  CA  GLY B 329     1579   1107   1912   -252    310    114       C  
-ATOM   3054  C   GLY B 329      64.755  25.547 -10.374  1.00 11.46           C  
-ANISOU 3054  C   GLY B 329     1456   1035   1861   -305    474     38       C  
-ATOM   3055  O   GLY B 329      63.836  26.362 -10.228  1.00 12.96           O  
-ANISOU 3055  O   GLY B 329     1427   1332   2164   -296    312     -7       O  
-ATOM   3056  N   ASN B 330      66.034  25.896 -10.457  1.00 11.78           N  
-ANISOU 3056  N   ASN B 330     1553    937   1985   -324    253     78       N  
-ATOM   3057  CA  ASN B 330      66.469  27.298 -10.488  1.00 13.31           C  
-ANISOU 3057  CA  ASN B 330     1762   1168   2126   -321    235    254       C  
-ATOM   3058  C   ASN B 330      66.020  28.117  -9.281  1.00 13.24           C  
-ANISOU 3058  C   ASN B 330     1859   1231   1938   -177    227    103       C  
-ATOM   3059  O   ASN B 330      65.624  29.278  -9.422  1.00 14.75           O  
-ANISOU 3059  O   ASN B 330     2172   1292   2140   -154    352    360       O  
-ATOM   3060  CB  ASN B 330      66.027  28.008 -11.774  1.00 14.68           C  
-ANISOU 3060  CB  ASN B 330     1838   1469   2269   -311    370    417       C  
-ATOM   3061  CG  ASN B 330      66.910  29.189 -12.096  1.00 14.76           C  
-ANISOU 3061  CG  ASN B 330     2030   1523   2054   -252    576    367       C  
-ATOM   3062  OD1 ASN B 330      68.138  29.082 -12.036  1.00 17.80           O  
-ANISOU 3062  OD1 ASN B 330     1977   1822   2962   -334    484    502       O  
-ATOM   3063  ND2 ASN B 330      66.300  30.328 -12.421  1.00 16.17           N  
-ANISOU 3063  ND2 ASN B 330     2269   1528   2347    -86    354    374       N  
-ATOM   3064  N   CYS B 331      66.086  27.518  -8.099  1.00 12.25           N  
-ANISOU 3064  N   CYS B 331     1576   1046   2033   -170    187      4       N  
-ATOM   3065  CA  CYS B 331      65.647  28.190  -6.889  1.00 11.61           C  
-ANISOU 3065  CA  CYS B 331     1539   1268   1604   -222    152    -27       C  
-ATOM   3066  C   CYS B 331      66.451  27.725  -5.684  1.00 11.91           C  
-ANISOU 3066  C   CYS B 331     1557    930   2037   -181     46     20       C  
-ATOM   3067  O   CYS B 331      67.320  26.865  -5.801  1.00 12.47           O  
-ANISOU 3067  O   CYS B 331     1553    867   2319   -151    185    -36       O  
-ATOM   3068  CB  CYS B 331      64.151  27.953  -6.658  1.00 12.51           C  
-ANISOU 3068  CB  CYS B 331     1350   1144   2258   -312    129   -112       C  
-ATOM   3069  SG  CYS B 331      63.673  26.212  -6.581  1.00 13.04           S  
-ANISOU 3069  SG  CYS B 331     1678   1115   2161   -185    287     24       S  
-ATOM   3070  N   ASP B 332      66.165  28.310  -4.528  1.00 12.03           N  
-ANISOU 3070  N   ASP B 332     1516   1168   1887   -290    -29   -178       N  
-ATOM   3071  CA  ASP B 332      66.898  28.000  -3.312  1.00 11.67           C  
-ANISOU 3071  CA  ASP B 332     1533   1018   1882   -343   -104   -142       C  
-ATOM   3072  C   ASP B 332      66.078  27.065  -2.439  1.00 11.18           C  
-ANISOU 3072  C   ASP B 332     1497    906   1843    -98    141   -100       C  
-ATOM   3073  O   ASP B 332      65.014  27.443  -1.936  1.00 12.19           O  
-ANISOU 3073  O   ASP B 332     1444   1037   2150    187    242    -15       O  
-ATOM   3074  CB  ASP B 332      67.219  29.291  -2.549  1.00 13.25           C  
-ANISOU 3074  CB  ASP B 332     1635   1027   2370   -423    198    -22       C  
-ATOM   3075  CG  ASP B 332      68.267  30.144  -3.245  1.00 14.38           C  
-ANISOU 3075  CG  ASP B 332     1920   1163   2379   -192     44   -446       C  
-ATOM   3076  OD1 ASP B 332      68.693  29.794  -4.371  1.00 14.79           O  
-ANISOU 3076  OD1 ASP B 332     1883   1113   2621   -255    297     17       O  
-ATOM   3077  OD2 ASP B 332      68.659  31.180  -2.661  1.00 16.79           O  
-ANISOU 3077  OD2 ASP B 332     2012   1127   3239   -377   -130   -477       O  
-ATOM   3078  N   LEU B 333      66.589  25.848  -2.264  1.00 11.05           N  
-ANISOU 3078  N   LEU B 333     1577    683   1937   -375   -146     64       N  
-ATOM   3079  CA  LEU B 333      65.921  24.837  -1.452  1.00 10.88           C  
-ANISOU 3079  CA  LEU B 333     1445    705   1983   -252    -69   -294       C  
-ATOM   3080  C   LEU B 333      66.411  24.964  -0.013  1.00  9.92           C  
-ANISOU 3080  C   LEU B 333     1323    972   1472   -203    -35   -244       C  
-ATOM   3081  O   LEU B 333      67.600  24.806   0.268  1.00 12.73           O  
-ANISOU 3081  O   LEU B 333     1084   1619   2134   -147    -96   -221       O  
-ATOM   3082  CB  LEU B 333      66.237  23.437  -1.984  1.00  9.71           C  
-ANISOU 3082  CB  LEU B 333     1421    707   1560    -26    116   -289       C  
-ATOM   3083  CG  LEU B 333      66.009  23.206  -3.480  1.00 10.17           C  
-ANISOU 3083  CG  LEU B 333     1199    842   1823    -34   -139    -73       C  
-ATOM   3084  CD1 LEU B 333      66.510  21.817  -3.846  1.00 11.54           C  
-ANISOU 3084  CD1 LEU B 333     1392    775   2218   -150    134      4       C  
-ATOM   3085  CD2 LEU B 333      64.542  23.376  -3.818  1.00 12.14           C  
-ANISOU 3085  CD2 LEU B 333     1212   1395   2006   -136      8      2       C  
-ATOM   3086  N   HIS B 334      65.489  25.253   0.898  1.00  9.55           N  
-ANISOU 3086  N   HIS B 334     1313    852   1463   -207    125   -139       N  
-ATOM   3087  CA  HIS B 334      65.838  25.353   2.303  1.00  9.50           C  
-ANISOU 3087  CA  HIS B 334     1226    675   1708    -68    197   -225       C  
-ATOM   3088  C   HIS B 334      65.506  24.028   2.967  1.00  9.81           C  
-ANISOU 3088  C   HIS B 334     1151    689   1885   -295    270    -89       C  
-ATOM   3089  O   HIS B 334      64.333  23.708   3.193  1.00 10.06           O  
-ANISOU 3089  O   HIS B 334     1100    767   1956    -61    128    -18       O  
-ATOM   3090  CB  HIS B 334      65.101  26.518   2.958  1.00 11.31           C  
-ANISOU 3090  CB  HIS B 334     1349    882   2067    -68     84    -85       C  
-ATOM   3091  CG  HIS B 334      65.432  27.842   2.346  1.00 11.13           C  
-ANISOU 3091  CG  HIS B 334     1271    749   2210   -298    197   -136       C  
-ATOM   3092  ND1 HIS B 334      66.374  28.696   2.879  1.00 13.30           N  
-ANISOU 3092  ND1 HIS B 334     1580    978   2493   -142    -40     30       N  
-ATOM   3093  CD2 HIS B 334      64.962  28.446   1.230  1.00 13.49           C  
-ANISOU 3093  CD2 HIS B 334     1728    941   2454     30    110    116       C  
-ATOM   3094  CE1 HIS B 334      66.469  29.770   2.116  1.00 14.75           C  
-ANISOU 3094  CE1 HIS B 334     1539   1050   3013   -248    -69     45       C  
-ATOM   3095  NE2 HIS B 334      65.616  29.650   1.114  1.00 14.22           N  
-ANISOU 3095  NE2 HIS B 334     1787   1033   2583     83    101     84       N  
-ATOM   3096  N   MET B 335      66.553  23.260   3.252  1.00 10.21           N  
-ANISOU 3096  N   MET B 335     1354    786   1739    178    -14    -17       N  
-ATOM   3097  CA  MET B 335      66.404  21.916   3.790  1.00 10.64           C  
-ANISOU 3097  CA  MET B 335     1283    787   1972    102   -128    170       C  
-ATOM   3098  C   MET B 335      66.593  21.866   5.299  1.00 10.75           C  
-ANISOU 3098  C   MET B 335     1235    784   2064   -150   -285    -74       C  
-ATOM   3099  O   MET B 335      67.398  22.607   5.869  1.00 13.35           O  
-ANISOU 3099  O   MET B 335     1402   1269   2399   -416   -337    -23       O  
-ATOM   3100  CB  MET B 335      67.421  20.965   3.149  1.00 11.97           C  
-ANISOU 3100  CB  MET B 335     1335   1107   2107    254   -151     92       C  
-ATOM   3101  CG  MET B 335      67.538  21.062   1.628  1.00 11.87           C  
-ANISOU 3101  CG  MET B 335     1436   1155   1918    175    -39   -118       C  
-ATOM   3102  SD  MET B 335      66.049  20.591   0.732  1.00 12.17           S  
-ANISOU 3102  SD  MET B 335     1389   1230   2003    238    -70    -18       S  
-ATOM   3103  CE  MET B 335      65.999  18.814   1.038  1.00 11.87           C  
-ANISOU 3103  CE  MET B 335     1523    859   2127    214    -90      2       C  
-ATOM   3104  N   THR B 336      65.852  20.968   5.939  1.00 10.40           N  
-ANISOU 3104  N   THR B 336     1213    695   2041   -137   -216   -100       N  
-ATOM   3105  CA  THR B 336      66.126  20.559   7.301  1.00  9.76           C  
-ANISOU 3105  CA  THR B 336     1209    806   1692    151   -137    -27       C  
-ATOM   3106  C   THR B 336      66.681  19.151   7.220  1.00 10.11           C  
-ANISOU 3106  C   THR B 336     1189    866   1784     42   -571    -36       C  
-ATOM   3107  O   THR B 336      66.260  18.368   6.373  1.00 11.89           O  
-ANISOU 3107  O   THR B 336     1548    855   2114    107   -585   -116       O  
-ATOM   3108  CB  THR B 336      64.847  20.588   8.143  1.00 10.61           C  
-ANISOU 3108  CB  THR B 336     1314    999   1719    245    212    123       C  
-ATOM   3109  OG1 THR B 336      64.436  21.955   8.300  1.00 12.01           O  
-ANISOU 3109  OG1 THR B 336     1375   1062   2127    467    -85   -169       O  
-ATOM   3110  CG2 THR B 336      65.061  19.967   9.522  1.00 13.65           C  
-ANISOU 3110  CG2 THR B 336     1678   1433   2076    308     77    238       C  
-ATOM   3111  N   PHE B 337      67.650  18.825   8.069  1.00  9.17           N  
-ANISOU 3111  N   PHE B 337     1011    654   1819    245   -235     46       N  
-ATOM   3112  CA  PHE B 337      68.230  17.487   8.000  1.00 10.21           C  
-ANISOU 3112  CA  PHE B 337      949    970   1959    279   -313    180       C  
-ATOM   3113  C   PHE B 337      68.545  16.911   9.370  1.00 10.25           C  
-ANISOU 3113  C   PHE B 337     1032    943   1920    168   -420     78       C  
-ATOM   3114  O   PHE B 337      68.649  17.638  10.359  1.00 10.65           O  
-ANISOU 3114  O   PHE B 337     1146    919   1979     64   -286   -253       O  
-ATOM   3115  CB  PHE B 337      69.452  17.456   7.067  1.00 11.98           C  
-ANISOU 3115  CB  PHE B 337     1048   1167   2335    -52    -23   -207       C  
-ATOM   3116  CG  PHE B 337      70.634  18.251   7.566  1.00 11.51           C  
-ANISOU 3116  CG  PHE B 337     1158    998   2217    182    -68   -323       C  
-ATOM   3117  CD1 PHE B 337      71.510  17.709   8.503  1.00 12.42           C  
-ANISOU 3117  CD1 PHE B 337      970   1183   2565   -104      8   -476       C  
-ATOM   3118  CD2 PHE B 337      70.886  19.532   7.079  1.00 12.82           C  
-ANISOU 3118  CD2 PHE B 337     1382   1103   2384    -38     28   -427       C  
-ATOM   3119  CE1 PHE B 337      72.618  18.438   8.949  1.00 12.89           C  
-ANISOU 3119  CE1 PHE B 337     1102    928   2867    -75    -61   -161       C  
-ATOM   3120  CE2 PHE B 337      71.987  20.261   7.521  1.00 14.11           C  
-ANISOU 3120  CE2 PHE B 337     1361   1387   2612     67   -104   -213       C  
-ATOM   3121  CZ  PHE B 337      72.849  19.713   8.461  1.00 14.37           C  
-ANISOU 3121  CZ  PHE B 337     1253   1080   3128    -83      4    -95       C  
-ATOM   3122  N   VAL B 338      68.665  15.588   9.415  1.00 10.11           N  
-ANISOU 3122  N   VAL B 338     1076    777   1988    199   -271    -36       N  
-ATOM   3123  CA  VAL B 338      69.073  14.876  10.609  1.00 10.43           C  
-ANISOU 3123  CA  VAL B 338      962    985   2016    378   -236     83       C  
-ATOM   3124  C   VAL B 338      70.082  13.806  10.236  1.00  9.49           C  
-ANISOU 3124  C   VAL B 338      963    940   1701    251   -383    -67       C  
-ATOM   3125  O   VAL B 338      70.002  13.212   9.154  1.00 10.76           O  
-ANISOU 3125  O   VAL B 338     1145   1043   1900    189   -319   -216       O  
-ATOM   3126  CB  VAL B 338      67.876  14.205  11.320  1.00 10.36           C  
-ANISOU 3126  CB  VAL B 338      954    993   1990    -85    -42   -495       C  
-ATOM   3127  CG1 VAL B 338      66.929  15.263  11.883  1.00 11.73           C  
-ANISOU 3127  CG1 VAL B 338     1268   1172   2017    332    -26   -469       C  
-ATOM   3128  CG2 VAL B 338      67.133  13.265  10.383  1.00 11.64           C  
-ANISOU 3128  CG2 VAL B 338     1209   1088   2126   -197    140   -245       C  
-ATOM   3129  N   LYS B 339      71.038  13.578  11.128  1.00 10.61           N  
-ANISOU 3129  N   LYS B 339     1041    931   2059    302   -344     86       N  
-ATOM   3130  CA  LYS B 339      71.894  12.401  11.022  1.00 10.72           C  
-ANISOU 3130  CA  LYS B 339      990    815   2269    162   -417    -88       C  
-ATOM   3131  C   LYS B 339      71.004  11.167  11.073  1.00 10.99           C  
-ANISOU 3131  C   LYS B 339     1039    921   2214    110   -249   -258       C  
-ATOM   3132  O   LYS B 339      69.989  11.148  11.783  1.00 12.41           O  
-ANISOU 3132  O   LYS B 339     1240   1218   2255    315    -64    -39       O  
-ATOM   3133  CB  LYS B 339      72.927  12.391  12.154  1.00 12.65           C  
-ANISOU 3133  CB  LYS B 339     1163   1214   2427    221   -787   -248       C  
-ATOM   3134  CG  LYS B 339      73.936  13.545  12.056  1.00 12.83           C  
-ANISOU 3134  CG  LYS B 339     1118   1298   2458   -230   -664    -29       C  
-ATOM   3135  CD  LYS B 339      75.105  13.372  13.019  1.00 15.31           C  
-ANISOU 3135  CD  LYS B 339     1306   1940   2570    157   -681   -460       C  
-ATOM   3136  CE  LYS B 339      74.655  13.479  14.473  1.00 16.96           C  
-ANISOU 3136  CE  LYS B 339     1376   2326   2741    441   -699   -355       C  
-ATOM   3137  NZ  LYS B 339      75.835  13.458  15.410  1.00 18.21           N  
-ANISOU 3137  NZ  LYS B 339     1424   2640   2853    486   -836   -447       N  
-ATOM   3138  N   ILE B 340      71.368  10.142  10.311  1.00 11.15           N  
-ANISOU 3138  N   ILE B 340     1113   1037   2085    221   -434   -342       N  
-ATOM   3139  CA  ILE B 340      70.498   8.979  10.161  1.00 12.06           C  
-ANISOU 3139  CA  ILE B 340     1151   1044   2385    385   -315   -159       C  
-ATOM   3140  C   ILE B 340      71.166   7.641  10.523  1.00 12.10           C  
-ANISOU 3140  C   ILE B 340      930   1179   2489    183   -282   -160       C  
-ATOM   3141  O   ILE B 340      70.494   6.611  10.595  1.00 13.37           O  
-ANISOU 3141  O   ILE B 340     1379   1044   2657     43   -406    -69       O  
-ATOM   3142  CB  ILE B 340      69.879   8.936   8.737  1.00 11.04           C  
-ANISOU 3142  CB  ILE B 340     1066   1102   2027     67   -170   -149       C  
-ATOM   3143  CG1 ILE B 340      68.649   8.023   8.697  1.00 12.21           C  
-ANISOU 3143  CG1 ILE B 340     1179   1213   2247    -10      0   -186       C  
-ATOM   3144  CG2 ILE B 340      70.912   8.539   7.700  1.00 12.51           C  
-ANISOU 3144  CG2 ILE B 340     1134   1237   2381     42    176   -294       C  
-ATOM   3145  CD1 ILE B 340      67.501   8.484   9.609  1.00 14.34           C  
-ANISOU 3145  CD1 ILE B 340     1217   1570   2662    -65   -337   -165       C  
-ATOM   3146  N   ASN B 341      72.473   7.655  10.772  1.00 12.76           N  
-ANISOU 3146  N   ASN B 341     1102   1252   2495    460   -275      4       N  
-ATOM   3147  CA  ASN B 341      73.137   6.443  11.241  1.00 13.73           C  
-ANISOU 3147  CA  ASN B 341     1210   1380   2627    501   -188    208       C  
-ATOM   3148  C   ASN B 341      72.762   6.213  12.702  1.00 14.04           C  
-ANISOU 3148  C   ASN B 341     1298   1270   2766    507   -238    136       C  
-ATOM   3149  O   ASN B 341      72.921   7.111  13.524  1.00 13.96           O  
-ANISOU 3149  O   ASN B 341     1349   1271   2683    407   -442    -66       O  
-ATOM   3150  CB  ASN B 341      74.655   6.595  11.101  1.00 15.46           C  
-ANISOU 3150  CB  ASN B 341     1286   1719   2869    661   -202    202       C  
-ATOM   3151  CG  ASN B 341      75.418   5.323  11.429  1.00 18.50           C  
-ANISOU 3151  CG  ASN B 341     1586   2184   3258    827    101    463       C  
-ATOM   3152  OD1 ASN B 341      74.994   4.506  12.241  1.00 18.14           O  
-ANISOU 3152  OD1 ASN B 341     1579   1948   3366    823    150    253       O  
-ATOM   3153  ND2 ASN B 341      76.572   5.168  10.798  1.00 26.68           N  
-ANISOU 3153  ND2 ASN B 341     2428   3280   4430   1350    835    861       N  
-ATOM   3154  N   PRO B 342      72.251   5.017  13.035  1.00 13.82           N  
-ANISOU 3154  N   PRO B 342     1413   1210   2627    223    -95    -72       N  
-ATOM   3155  CA  PRO B 342      71.863   4.798  14.434  1.00 15.55           C  
-ANISOU 3155  CA  PRO B 342     1660   1218   3030    307      0    129       C  
-ATOM   3156  C   PRO B 342      72.975   5.106  15.436  1.00 15.65           C  
-ANISOU 3156  C   PRO B 342     1593   1531   2822    462    -58    333       C  
-ATOM   3157  O   PRO B 342      72.673   5.515  16.557  1.00 16.67           O  
-ANISOU 3157  O   PRO B 342     1975   1493   2866    702    -41    244       O  
-ATOM   3158  CB  PRO B 342      71.488   3.313  14.466  1.00 17.50           C  
-ANISOU 3158  CB  PRO B 342     2067   1457   3125    232    233    262       C  
-ATOM   3159  CG  PRO B 342      71.036   3.023  13.074  1.00 20.37           C  
-ANISOU 3159  CG  PRO B 342     2263   1723   3752    117   -368   -116       C  
-ATOM   3160  CD  PRO B 342      71.907   3.869  12.177  1.00 16.06           C  
-ANISOU 3160  CD  PRO B 342     1871   1187   3045   -111   -309   -119       C  
-ATOM   3161  N   THR B 343      74.237   4.913  15.056  1.00 15.64           N  
-ANISOU 3161  N   THR B 343     1530   1582   2830    389   -566    291       N  
-ATOM   3162  CA  THR B 343      75.331   5.182  15.990  1.00 17.26           C  
-ANISOU 3162  CA  THR B 343     1607   2140   2811    485   -440    156       C  
-ATOM   3163  C   THR B 343      75.474   6.670  16.308  1.00 17.55           C  
-ANISOU 3163  C   THR B 343     1780   2137   2749    553   -536    -65       C  
-ATOM   3164  O   THR B 343      76.082   7.042  17.315  1.00 20.73           O  
-ANISOU 3164  O   THR B 343     2227   2461   3186    724   -749     37       O  
-ATOM   3165  CB  THR B 343      76.676   4.628  15.482  1.00 21.20           C  
-ANISOU 3165  CB  THR B 343     1802   2748   3504    729   -581   -159       C  
-ATOM   3166  OG1 THR B 343      77.077   5.335  14.306  1.00 23.99           O  
-ANISOU 3166  OG1 THR B 343     1924   3346   3845    765   -204   -361       O  
-ATOM   3167  CG2 THR B 343      76.564   3.139  15.173  1.00 23.33           C  
-ANISOU 3167  CG2 THR B 343     2170   2763   3929   1172   -478    -67       C  
-ATOM   3168  N   GLU B 344      74.897   7.513  15.456  1.00 15.65           N  
-ANISOU 3168  N   GLU B 344     1518   1653   2775    487   -465    301       N  
-ATOM   3169  CA  GLU B 344      74.924   8.958  15.656  1.00 15.23           C  
-ANISOU 3169  CA  GLU B 344     1443   1417   2927    254   -312    173       C  
-ATOM   3170  C   GLU B 344      73.646   9.438  16.332  1.00 14.56           C  
-ANISOU 3170  C   GLU B 344     1478   1295   2759    354   -512   -316       C  
-ATOM   3171  O   GLU B 344      73.430  10.644  16.469  1.00 16.18           O  
-ANISOU 3171  O   GLU B 344     1666   1427   3053    321   -414   -435       O  
-ATOM   3172  CB  GLU B 344      75.075   9.680  14.312  1.00 15.76           C  
-ANISOU 3172  CB  GLU B 344     1319   1796   2871    325   -427     93       C  
-ATOM   3173  CG  GLU B 344      76.406   9.435  13.614  1.00 17.17           C  
-ANISOU 3173  CG  GLU B 344     1118   2141   3265    223   -386    -68       C  
-ATOM   3174  CD  GLU B 344      77.570  10.129  14.299  1.00 19.09           C  
-ANISOU 3174  CD  GLU B 344     1543   2328   3383    417   -774   -158       C  
-ATOM   3175  OE1 GLU B 344      77.346  11.142  15.000  1.00 19.19           O  
-ANISOU 3175  OE1 GLU B 344     1618   2138   3534    341   -560    106       O  
-ATOM   3176  OE2 GLU B 344      78.713   9.661  14.132  1.00 22.63           O  
-ANISOU 3176  OE2 GLU B 344     1649   2755   4193    435   -555   -418       O  
-ATOM   3177  N   LEU B 345      72.803   8.493  16.749  1.00 13.85           N  
-ANISOU 3177  N   LEU B 345     1254   1673   2335    284   -446    116       N  
-ATOM   3178  CA  LEU B 345      71.494   8.831  17.299  1.00 13.69           C  
-ANISOU 3178  CA  LEU B 345     1486   1653   2060    245   -566    -21       C  
-ATOM   3179  C   LEU B 345      71.285   8.290  18.709  1.00 15.45           C  
-ANISOU 3179  C   LEU B 345     1737   1539   2592    236   -810   -206       C  
-ATOM   3180  O   LEU B 345      70.159   7.971  19.101  1.00 15.35           O  
-ANISOU 3180  O   LEU B 345     1677   1733   2421    520   -725   -193       O  
-ATOM   3181  CB  LEU B 345      70.383   8.327  16.370  1.00 13.58           C  
-ANISOU 3181  CB  LEU B 345     1498   1401   2261    315   -472     98       C  
-ATOM   3182  CG  LEU B 345      70.329   9.003  14.996  1.00 13.39           C  
-ANISOU 3182  CG  LEU B 345     1432   1295   2358    331   -713   -200       C  
-ATOM   3183  CD1 LEU B 345      69.364   8.281  14.052  1.00 12.70           C  
-ANISOU 3183  CD1 LEU B 345     1212   1270   2343     66   -387   -263       C  
-ATOM   3184  CD2 LEU B 345      69.989  10.483  15.131  1.00 14.42           C  
-ANISOU 3184  CD2 LEU B 345     1520   1031   2926    326   -476    -56       C  
-ATOM   3185  N   SER B 346      72.364   8.194  19.479  1.00 16.75           N  
-ANISOU 3185  N   SER B 346     2090   1788   2486    523  -1024   -205       N  
-ATOM   3186  CA  SER B 346      72.250   7.714  20.852  1.00 17.43           C  
-ANISOU 3186  CA  SER B 346     2122   2053   2447    697  -1070    -41       C  
-ATOM   3187  C   SER B 346      72.030   8.861  21.839  1.00 17.53           C  
-ANISOU 3187  C   SER B 346     2263   1971   2426    427   -994    298       C  
-ATOM   3188  O   SER B 346      71.365   8.697  22.861  1.00 18.54           O  
-ANISOU 3188  O   SER B 346     2544   2146   2353    299   -822     57       O  
-ATOM   3189  CB  SER B 346      73.482   6.894  21.249  1.00 22.49           C  
-ANISOU 3189  CB  SER B 346     2202   2631   3711    581  -1020     61       C  
-ATOM   3190  OG  SER B 346      74.640   7.704  21.293  1.00 28.90           O  
-ANISOU 3190  OG  SER B 346     3001   3339   4639   1064   -999   -478       O  
-ATOM   3191  N   THR B 347      72.590  10.024  21.518  1.00 17.46           N  
-ANISOU 3191  N   THR B 347     2179   1605   2848    435   -831   -102       N  
-ATOM   3192  CA  THR B 347      72.538  11.179  22.397  1.00 17.44           C  
-ANISOU 3192  CA  THR B 347     1977   2015   2635    109   -857    185       C  
-ATOM   3193  C   THR B 347      72.702  12.445  21.559  1.00 17.08           C  
-ANISOU 3193  C   THR B 347     1856   1919   2715     73   -806   -262       C  
-ATOM   3194  O   THR B 347      73.201  12.387  20.434  1.00 18.49           O  
-ANISOU 3194  O   THR B 347     2039   2283   2701    283   -992   -162       O  
-ATOM   3195  CB  THR B 347      73.671  11.123  23.444  1.00 22.69           C  
-ANISOU 3195  CB  THR B 347     2332   2766   3521    597  -1134   -399       C  
-ATOM   3196  OG1 THR B 347      73.505  12.171  24.401  1.00 27.36           O  
-ANISOU 3196  OG1 THR B 347     2868   3408   4117   1247  -1219   -241       O  
-ATOM   3197  CG2 THR B 347      75.029  11.271  22.772  1.00 22.39           C  
-ANISOU 3197  CG2 THR B 347     1973   2931   3603    138  -1415    -17       C  
-ATOM   3198  N   GLY B 348      72.276  13.583  22.104  1.00 16.65           N  
-ANISOU 3198  N   GLY B 348     1848   1836   2641    164  -1059   -178       N  
-ATOM   3199  CA  GLY B 348      72.515  14.868  21.469  1.00 16.57           C  
-ANISOU 3199  CA  GLY B 348     1829   1857   2609    221  -1019   -152       C  
-ATOM   3200  C   GLY B 348      71.525  15.242  20.377  1.00 15.25           C  
-ANISOU 3200  C   GLY B 348     1610   1855   2330     15   -895   -329       C  
-ATOM   3201  O   GLY B 348      70.610  14.483  20.057  1.00 16.90           O  
-ANISOU 3201  O   GLY B 348     1647   1798   2974    183   -938   -178       O  
-ATOM   3202  N   ASP B 349      71.725  16.421  19.800  1.00 14.82           N  
-ANISOU 3202  N   ASP B 349     1575   1803   2252    151   -609   -105       N  
-ATOM   3203  CA  ASP B 349      70.853  16.965  18.761  1.00 14.08           C  
-ANISOU 3203  CA  ASP B 349     1571   1531   2247    312   -616   -372       C  
-ATOM   3204  C   ASP B 349      71.412  16.577  17.392  1.00 12.66           C  
-ANISOU 3204  C   ASP B 349     1328   1308   2173     80   -606   -276       C  
-ATOM   3205  O   ASP B 349      72.493  17.013  17.013  1.00 14.74           O  
-ANISOU 3205  O   ASP B 349     1406   1659   2533    -33   -392   -429       O  
-ATOM   3206  CB  ASP B 349      70.799  18.490  18.911  1.00 14.72           C  
-ANISOU 3206  CB  ASP B 349     1637   1353   2603    389   -681   -704       C  
-ATOM   3207  CG  ASP B 349      69.830  19.155  17.950  1.00 13.36           C  
-ANISOU 3207  CG  ASP B 349     1582   1251   2244      6   -548   -492       C  
-ATOM   3208  OD1 ASP B 349      69.443  18.526  16.944  1.00 13.23           O  
-ANISOU 3208  OD1 ASP B 349     1496   1337   2194    132   -550   -393       O  
-ATOM   3209  OD2 ASP B 349      69.467  20.327  18.201  1.00 16.60           O  
-ANISOU 3209  OD2 ASP B 349     1832   1650   2826     80   -746   -404       O  
-ATOM   3210  N   PRO B 350      70.673  15.743  16.639  1.00 11.60           N  
-ANISOU 3210  N   PRO B 350     1158   1112   2136    -16   -371    -40       N  
-ATOM   3211  CA  PRO B 350      71.187  15.264  15.353  1.00 11.60           C  
-ANISOU 3211  CA  PRO B 350     1368   1079   1961    121   -426    -86       C  
-ATOM   3212  C   PRO B 350      70.825  16.182  14.194  1.00 10.47           C  
-ANISOU 3212  C   PRO B 350     1145   1210   1622    -59   -561   -337       C  
-ATOM   3213  O   PRO B 350      71.108  15.833  13.048  1.00 12.07           O  
-ANISOU 3213  O   PRO B 350     1449   1179   1956    125   -440   -333       O  
-ATOM   3214  CB  PRO B 350      70.441  13.941  15.178  1.00 13.06           C  
-ANISOU 3214  CB  PRO B 350     1260   1450   2250    134   -262   -163       C  
-ATOM   3215  CG  PRO B 350      69.097  14.230  15.773  1.00 13.44           C  
-ANISOU 3215  CG  PRO B 350     1584   1422   2100    -16   -423   -446       C  
-ATOM   3216  CD  PRO B 350      69.376  15.125  16.975  1.00 13.48           C  
-ANISOU 3216  CD  PRO B 350     1486   1329   2306    -85   -611   -364       C  
-ATOM   3217  N   SER B 351      70.194  17.322  14.473  1.00 11.71           N  
-ANISOU 3217  N   SER B 351     1001   1138   2308     44   -485   -148       N  
-ATOM   3218  CA  SER B 351      69.560  18.097  13.407  1.00 11.22           C  
-ANISOU 3218  CA  SER B 351     1114   1145   2004    103   -328    -61       C  
-ATOM   3219  C   SER B 351      70.338  19.327  12.942  1.00 11.38           C  
-ANISOU 3219  C   SER B 351     1272   1250   1801     64   -385   -224       C  
-ATOM   3220  O   SER B 351      71.146  19.905  13.678  1.00 13.66           O  
-ANISOU 3220  O   SER B 351     1555   1434   2202      7   -609   -242       O  
-ATOM   3221  CB  SER B 351      68.152  18.526  13.825  1.00 12.76           C  
-ANISOU 3221  CB  SER B 351     1184   1368   2295    269   -267   -392       C  
-ATOM   3222  OG  SER B 351      68.200  19.565  14.789  1.00 13.37           O  
-ANISOU 3222  OG  SER B 351     1492   1262   2327    354   -258   -311       O  
-ATOM   3223  N   GLY B 352      70.063  19.731  11.709  1.00 11.45           N  
-ANISOU 3223  N   GLY B 352     1383   1080   1887    111   -125    -92       N  
-ATOM   3224  CA  GLY B 352      70.609  20.959  11.165  1.00 12.15           C  
-ANISOU 3224  CA  GLY B 352     1552   1001   2062     13   -420    131       C  
-ATOM   3225  C   GLY B 352      69.736  21.469  10.039  1.00 11.42           C  
-ANISOU 3225  C   GLY B 352     1492    832   2016    -73   -230     -5       C  
-ATOM   3226  O   GLY B 352      68.637  20.954   9.807  1.00 11.93           O  
-ANISOU 3226  O   GLY B 352     1234   1078   2222   -204   -230   -380       O  
-ATOM   3227  N   LYS B 353      70.225  22.483   9.336  1.00 13.07           N  
-ANISOU 3227  N   LYS B 353     1729   1102   2133    -24   -311    -40       N  
-ATOM   3228  CA  LYS B 353      69.514  23.041   8.199  1.00 13.22           C  
-ANISOU 3228  CA  LYS B 353     1584   1317   2121    -21   -387    109       C  
-ATOM   3229  C   LYS B 353      70.544  23.566   7.222  1.00 12.12           C  
-ANISOU 3229  C   LYS B 353     1622   1205   1778   -345   -446   -256       C  
-ATOM   3230  O   LYS B 353      71.674  23.871   7.611  1.00 14.77           O  
-ANISOU 3230  O   LYS B 353     1710   1467   2435   -421   -456   -124       O  
-ATOM   3231  CB  LYS B 353      68.574  24.164   8.644  1.00 15.96           C  
-ANISOU 3231  CB  LYS B 353     2023   1449   2593     42   -529     46       C  
-ATOM   3232  CG  LYS B 353      69.266  25.291   9.377  1.00 17.31           C  
-ANISOU 3232  CG  LYS B 353     2355   1220   3003    146   -425   -251       C  
-ATOM   3233  CD  LYS B 353      68.275  26.290   9.975  1.00 21.44           C  
-ANISOU 3233  CD  LYS B 353     2815   1572   3759    427   -206   -408       C  
-ATOM   3234  CE  LYS B 353      67.413  26.959   8.909  1.00 20.73           C  
-ANISOU 3234  CE  LYS B 353     2739   1701   3434    504   -567   -257       C  
-ATOM   3235  NZ  LYS B 353      66.614  28.090   9.486  1.00 21.20           N  
-ANISOU 3235  NZ  LYS B 353     2779   1841   3435    603   -630   -404       N  
-ATOM   3236  N   VAL B 354      70.157  23.678   5.957  1.00 11.69           N  
-ANISOU 3236  N   VAL B 354     1316   1258   1866   -151   -157   -127       N  
-ATOM   3237  CA  VAL B 354      71.087  24.124   4.929  1.00 11.58           C  
-ANISOU 3237  CA  VAL B 354     1229   1221   1950   -144      9    -24       C  
-ATOM   3238  C   VAL B 354      70.334  24.541   3.669  1.00 12.15           C  
-ANISOU 3238  C   VAL B 354     1343   1251   2021    -61   -328   -103       C  
-ATOM   3239  O   VAL B 354      69.232  24.057   3.398  1.00 12.71           O  
-ANISOU 3239  O   VAL B 354     1345   1302   2182   -197    -37      7       O  
-ATOM   3240  CB  VAL B 354      72.126  23.011   4.602  1.00 13.06           C  
-ANISOU 3240  CB  VAL B 354     1318   1112   2532   -180     89   -223       C  
-ATOM   3241  CG1 VAL B 354      71.457  21.828   3.894  1.00 13.50           C  
-ANISOU 3241  CG1 VAL B 354     1470   1129   2529   -174    -78   -452       C  
-ATOM   3242  CG2 VAL B 354      73.276  23.550   3.777  1.00 14.92           C  
-ANISOU 3242  CG2 VAL B 354     1374   1371   2925     81    347    130       C  
-ATOM   3243  N   VAL B 355      70.933  25.441   2.899  1.00 12.59           N  
-ANISOU 3243  N   VAL B 355     1475   1144   2164      2   -172     16       N  
-ATOM   3244  CA  VAL B 355      70.369  25.833   1.619  1.00 12.34           C  
-ANISOU 3244  CA  VAL B 355     1535    919   2233    -54   -147    -79       C  
-ATOM   3245  C   VAL B 355      71.087  25.098   0.499  1.00 12.23           C  
-ANISOU 3245  C   VAL B 355     1275   1159   2211   -214    -54    -49       C  
-ATOM   3246  O   VAL B 355      72.321  24.978   0.501  1.00 13.19           O  
-ANISOU 3246  O   VAL B 355     1134   1518   2357   -290     70   -284       O  
-ATOM   3247  CB  VAL B 355      70.489  27.356   1.397  1.00 12.65           C  
-ANISOU 3247  CB  VAL B 355     1658    904   2245   -118    -57    -52       C  
-ATOM   3248  CG1 VAL B 355      69.968  27.762   0.015  1.00 14.85           C  
-ANISOU 3248  CG1 VAL B 355     2020   1072   2551      5   -359    171       C  
-ATOM   3249  CG2 VAL B 355      69.758  28.100   2.496  1.00 14.86           C  
-ANISOU 3249  CG2 VAL B 355     1845   1028   2772   -210    177   -505       C  
-ATOM   3250  N   ILE B 356      70.307  24.600  -0.453  1.00 11.12           N  
-ANISOU 3250  N   ILE B 356     1450    900   1875   -218    -62   -236       N  
-ATOM   3251  CA  ILE B 356      70.853  23.963  -1.645  1.00 11.29           C  
-ANISOU 3251  CA  ILE B 356     1422    786   2082    -85    -31    -42       C  
-ATOM   3252  C   ILE B 356      70.285  24.664  -2.878  1.00 11.21           C  
-ANISOU 3252  C   ILE B 356     1311   1082   1866   -197    123     82       C  
-ATOM   3253  O   ILE B 356      69.069  24.748  -3.048  1.00 12.39           O  
-ANISOU 3253  O   ILE B 356     1034   1355   2319    -86    -68    -50       O  
-ATOM   3254  CB  ILE B 356      70.509  22.452  -1.697  1.00 11.03           C  
-ANISOU 3254  CB  ILE B 356     1172    938   2079   -114     68    -61       C  
-ATOM   3255  CG1 ILE B 356      71.089  21.727  -0.473  1.00 12.51           C  
-ANISOU 3255  CG1 ILE B 356     1387    985   2379      3   -136    344       C  
-ATOM   3256  CG2 ILE B 356      71.014  21.835  -3.004  1.00 12.40           C  
-ANISOU 3256  CG2 ILE B 356     1452   1182   2075    -77    337   -205       C  
-ATOM   3257  CD1 ILE B 356      70.725  20.256  -0.399  1.00 12.55           C  
-ANISOU 3257  CD1 ILE B 356     1465    951   2351    -84    269     72       C  
-ATOM   3258  N   HIS B 357      71.167  25.185  -3.722  1.00 12.13           N  
-ANISOU 3258  N   HIS B 357     1446   1147   2015   -218    126    148       N  
-ATOM   3259  CA  HIS B 357      70.759  25.799  -4.982  1.00 12.33           C  
-ANISOU 3259  CA  HIS B 357     1531   1134   2018   -415    130    126       C  
-ATOM   3260  C   HIS B 357      70.460  24.726  -6.014  1.00 12.20           C  
-ANISOU 3260  C   HIS B 357     1399   1142   2094   -582    355   -298       C  
-ATOM   3261  O   HIS B 357      71.323  23.894  -6.298  1.00 13.67           O  
-ANISOU 3261  O   HIS B 357     1392   1393   2407   -187    323   -108       O  
-ATOM   3262  CB  HIS B 357      71.898  26.654  -5.542  1.00 13.80           C  
-ANISOU 3262  CB  HIS B 357     1543   1157   2542   -582    103     65       C  
-ATOM   3263  CG  HIS B 357      72.222  27.859  -4.717  1.00 14.07           C  
-ANISOU 3263  CG  HIS B 357     1538   1103   2704   -462   -288    112       C  
-ATOM   3264  ND1 HIS B 357      73.319  28.654  -4.970  1.00 15.59           N  
-ANISOU 3264  ND1 HIS B 357     1772   1233   2916   -646   -200    240       N  
-ATOM   3265  CD2 HIS B 357      71.592  28.411  -3.654  1.00 14.72           C  
-ANISOU 3265  CD2 HIS B 357     1724   1110   2757   -159   -286   -272       C  
-ATOM   3266  CE1 HIS B 357      73.350  29.645  -4.095  1.00 16.23           C  
-ANISOU 3266  CE1 HIS B 357     1751   1378   3036   -557   -352     63       C  
-ATOM   3267  NE2 HIS B 357      72.315  29.521  -3.284  1.00 16.20           N  
-ANISOU 3267  NE2 HIS B 357     1719   1519   2915   -418    -65    158       N  
-ATOM   3268  N   SER B 358      69.266  24.752  -6.601  1.00 11.75           N  
-ANISOU 3268  N   SER B 358     1312   1251   1899   -545    140   -111       N  
-ATOM   3269  CA  SER B 358      68.968  23.830  -7.693  1.00 11.60           C  
-ANISOU 3269  CA  SER B 358     1300   1012   2096   -520     25     90       C  
-ATOM   3270  C   SER B 358      69.372  24.440  -9.039  1.00 12.54           C  
-ANISOU 3270  C   SER B 358     1228   1227   2308   -375    200    162       C  
-ATOM   3271  O   SER B 358      68.572  24.527  -9.982  1.00 12.51           O  
-ANISOU 3271  O   SER B 358     1395   1263   2093   -121    306    -34       O  
-ATOM   3272  CB  SER B 358      67.497  23.402  -7.679  1.00 11.62           C  
-ANISOU 3272  CB  SER B 358     1242   1041   2131   -532     27    189       C  
-ATOM   3273  OG  SER B 358      66.624  24.515  -7.715  1.00 12.32           O  
-ANISOU 3273  OG  SER B 358     1547   1072   2060    130     84    140       O  
-ATOM   3274  N   TYR B 359      70.629  24.863  -9.105  1.00 13.17           N  
-ANISOU 3274  N   TYR B 359     1456   1282   2265   -412    628    215       N  
-ATOM   3275  CA  TYR B 359      71.193  25.499 -10.293  1.00 13.92           C  
-ANISOU 3275  CA  TYR B 359     1441   1478   2369   -314    516    257       C  
-ATOM   3276  C   TYR B 359      72.707  25.556 -10.162  1.00 15.15           C  
-ANISOU 3276  C   TYR B 359     1502   1687   2565   -411    413      9       C  
-ATOM   3277  O   TYR B 359      73.255  25.289  -9.081  1.00 14.90           O  
-ANISOU 3277  O   TYR B 359     1646   1671   2345   -457    345    157       O  
-ATOM   3278  CB  TYR B 359      70.606  26.895 -10.514  1.00 14.34           C  
-ANISOU 3278  CB  TYR B 359     1918   1115   2413   -119    407    224       C  
-ATOM   3279  CG  TYR B 359      70.654  27.819  -9.318  1.00 14.83           C  
-ANISOU 3279  CG  TYR B 359     1776   1220   2637   -417    231    181       C  
-ATOM   3280  CD1 TYR B 359      71.721  28.692  -9.126  1.00 15.61           C  
-ANISOU 3280  CD1 TYR B 359     1982   1496   2454    -21     81    -15       C  
-ATOM   3281  CD2 TYR B 359      69.616  27.845  -8.394  1.00 14.94           C  
-ANISOU 3281  CD2 TYR B 359     1986   1466   2222     88    323    157       C  
-ATOM   3282  CE1 TYR B 359      71.759  29.557  -8.032  1.00 16.50           C  
-ANISOU 3282  CE1 TYR B 359     1854   1564   2849   -227    260    526       C  
-ATOM   3283  CE2 TYR B 359      69.641  28.706  -7.304  1.00 15.27           C  
-ANISOU 3283  CE2 TYR B 359     1827   1213   2761   -277    152    204       C  
-ATOM   3284  CZ  TYR B 359      70.716  29.557  -7.125  1.00 15.12           C  
-ANISOU 3284  CZ  TYR B 359     2004   1232   2510   -255    169   -176       C  
-ATOM   3285  OH  TYR B 359      70.731  30.411  -6.043  1.00 15.86           O  
-ANISOU 3285  OH  TYR B 359     1927   1233   2865   -372    195     75       O  
-ATOM   3286  N   ASP B 360      73.362  25.909 -11.272  1.00 17.09           N  
-ANISOU 3286  N   ASP B 360     1600   1895   2999   -373    897    309       N  
-ATOM   3287  CA  ASP B 360      74.821  25.843 -11.447  1.00 17.86           C  
-ANISOU 3287  CA  ASP B 360     1688   2057   3039   -289    756    154       C  
-ATOM   3288  C   ASP B 360      75.311  24.404 -11.640  1.00 17.13           C  
-ANISOU 3288  C   ASP B 360     1713   1979   2817   -296    874    495       C  
-ATOM   3289  O   ASP B 360      74.623  23.445 -11.278  1.00 17.25           O  
-ANISOU 3289  O   ASP B 360     1877   2067   2609   -284    399    323       O  
-ATOM   3290  CB  ASP B 360      75.566  26.518 -10.299  1.00 19.14           C  
-ANISOU 3290  CB  ASP B 360     1873   2083   3316   -559    793     93       C  
-ATOM   3291  CG  ASP B 360      75.328  28.013 -10.251  1.00 21.02           C  
-ANISOU 3291  CG  ASP B 360     2331   2406   3250   -655    559    416       C  
-ATOM   3292  OD1 ASP B 360      74.998  28.607 -11.300  1.00 22.85           O  
-ANISOU 3292  OD1 ASP B 360     2556   2508   3617   -670    284    300       O  
-ATOM   3293  OD2 ASP B 360      75.466  28.595  -9.158  1.00 22.54           O  
-ANISOU 3293  OD2 ASP B 360     2486   2562   3514   -618    709    291       O  
-ATOM   3294  N   ALA B 361      76.501  24.261 -12.216  1.00 18.92           N  
-ANISOU 3294  N   ALA B 361     1766   2512   2911    120    871    457       N  
-ATOM   3295  CA  ALA B 361      77.049  22.941 -12.496  1.00 20.60           C  
-ANISOU 3295  CA  ALA B 361     1985   2775   3065    168   1115    593       C  
-ATOM   3296  C   ALA B 361      77.312  22.152 -11.219  1.00 19.77           C  
-ANISOU 3296  C   ALA B 361     1921   2553   3037    110    951    628       C  
-ATOM   3297  O   ALA B 361      77.393  20.922 -11.249  1.00 22.22           O  
-ANISOU 3297  O   ALA B 361     2338   2798   3305    281    813    -31       O  
-ATOM   3298  CB  ALA B 361      78.323  23.055 -13.325  1.00 24.09           C  
-ANISOU 3298  CB  ALA B 361     2212   3253   3688    547   1429    935       C  
-ATOM   3299  N   THR B 362      77.443  22.862 -10.101  1.00 18.74           N  
-ANISOU 3299  N   THR B 362     1490   2448   3183   -215    611     81       N  
-ATOM   3300  CA  THR B 362      77.664  22.216  -8.809  1.00 18.69           C  
-ANISOU 3300  CA  THR B 362     1540   2242   3320   -379    670     91       C  
-ATOM   3301  C   THR B 362      76.395  21.545  -8.266  1.00 16.61           C  
-ANISOU 3301  C   THR B 362     1420   2024   2866   -333    478   -145       C  
-ATOM   3302  O   THR B 362      76.446  20.806  -7.282  1.00 17.06           O  
-ANISOU 3302  O   THR B 362     1672   1882   2929    -40    610     76       O  
-ATOM   3303  CB  THR B 362      78.223  23.198  -7.767  1.00 19.97           C  
-ANISOU 3303  CB  THR B 362     1494   2537   3555   -536    751    174       C  
-ATOM   3304  OG1 THR B 362      77.525  24.447  -7.859  1.00 20.63           O  
-ANISOU 3304  OG1 THR B 362     1684   2241   3914   -301    642    168       O  
-ATOM   3305  CG2 THR B 362      79.701  23.436  -8.015  1.00 22.45           C  
-ANISOU 3305  CG2 THR B 362     1509   3055   3966   -454    472    335       C  
-ATOM   3306  N   PHE B 363      75.257  21.822  -8.896  1.00 14.71           N  
-ANISOU 3306  N   PHE B 363     1176   1823   2588   -364    354   -122       N  
-ATOM   3307  CA  PHE B 363      74.034  21.074  -8.618  1.00 14.67           C  
-ANISOU 3307  CA  PHE B 363     1167   1712   2693   -103    160   -552       C  
-ATOM   3308  C   PHE B 363      73.968  19.987  -9.679  1.00 14.66           C  
-ANISOU 3308  C   PHE B 363     1345   1745   2478   -153     30   -391       C  
-ATOM   3309  O   PHE B 363      73.499  20.223 -10.794  1.00 16.27           O  
-ANISOU 3309  O   PHE B 363     1711   1940   2529     21    307   -254       O  
-ATOM   3310  CB  PHE B 363      72.809  21.988  -8.699  1.00 14.00           C  
-ANISOU 3310  CB  PHE B 363     1011   1553   2756   -224    486   -238       C  
-ATOM   3311  CG  PHE B 363      71.488  21.283  -8.500  1.00 13.20           C  
-ANISOU 3311  CG  PHE B 363     1196   1485   2334    -96    276   -349       C  
-ATOM   3312  CD1 PHE B 363      71.058  20.939  -7.229  1.00 14.01           C  
-ANISOU 3312  CD1 PHE B 363     1308   1113   2902   -150    431   -128       C  
-ATOM   3313  CD2 PHE B 363      70.663  21.005  -9.584  1.00 15.40           C  
-ANISOU 3313  CD2 PHE B 363     1446   1641   2765    159    -84   -396       C  
-ATOM   3314  CE1 PHE B 363      69.832  20.306  -7.036  1.00 15.55           C  
-ANISOU 3314  CE1 PHE B 363     1420   1344   3143    135     30   -376       C  
-ATOM   3315  CE2 PHE B 363      69.444  20.379  -9.405  1.00 15.61           C  
-ANISOU 3315  CE2 PHE B 363     1265   1617   3050     89   -141   -198       C  
-ATOM   3316  CZ  PHE B 363      69.025  20.023  -8.131  1.00 16.65           C  
-ANISOU 3316  CZ  PHE B 363     1327   1421   3577   -119    176   -185       C  
-ATOM   3317  N   ALA B 364      74.469  18.805  -9.333  1.00 13.84           N  
-ANISOU 3317  N   ALA B 364     1537   1379   2340   -113    511   -446       N  
-ATOM   3318  CA  ALA B 364      74.587  17.709 -10.291  1.00 14.22           C  
-ANISOU 3318  CA  ALA B 364     1511   1465   2425   -282    953   -255       C  
-ATOM   3319  C   ALA B 364      74.094  16.390  -9.699  1.00 12.74           C  
-ANISOU 3319  C   ALA B 364     1327   1510   2004   -173    478   -343       C  
-ATOM   3320  O   ALA B 364      74.837  15.407  -9.671  1.00 14.27           O  
-ANISOU 3320  O   ALA B 364     1406   1647   2368     78    274   -209       O  
-ATOM   3321  CB  ALA B 364      76.032  17.578 -10.764  1.00 17.01           C  
-ANISOU 3321  CB  ALA B 364     1591   1910   2962   -249    948   -179       C  
-ATOM   3322  N   PRO B 365      72.830  16.356  -9.242  1.00 12.99           N  
-ANISOU 3322  N   PRO B 365     1248   1530   2158     83    434   -280       N  
-ATOM   3323  CA  PRO B 365      72.320  15.151  -8.572  1.00 13.44           C  
-ANISOU 3323  CA  PRO B 365     1513   1599   1992      0    669   -257       C  
-ATOM   3324  C   PRO B 365      72.342  13.900  -9.461  1.00 12.72           C  
-ANISOU 3324  C   PRO B 365     1447   1656   1729    -68    610   -175       C  
-ATOM   3325  O   PRO B 365      72.464  12.791  -8.935  1.00 13.89           O  
-ANISOU 3325  O   PRO B 365     1665   1428   2185    -89    421      9       O  
-ATOM   3326  CB  PRO B 365      70.883  15.543  -8.190  1.00 14.25           C  
-ANISOU 3326  CB  PRO B 365     1445   1543   2424     73    644   -355       C  
-ATOM   3327  CG  PRO B 365      70.520  16.625  -9.133  1.00 14.98           C  
-ANISOU 3327  CG  PRO B 365     1347   1576   2767    -95    497   -255       C  
-ATOM   3328  CD  PRO B 365      71.792  17.396  -9.353  1.00 13.97           C  
-ANISOU 3328  CD  PRO B 365     1130   1562   2617    -17    603   -273       C  
-ATOM   3329  N   HIS B 366      72.258  14.068 -10.778  1.00 12.84           N  
-ANISOU 3329  N   HIS B 366     1287   1464   2127    -80    554   -457       N  
-ATOM   3330  CA  HIS B 366      72.352  12.931 -11.693  1.00 12.15           C  
-ANISOU 3330  CA  HIS B 366     1444   1409   1761     66    285   -599       C  
-ATOM   3331  C   HIS B 366      73.728  12.272 -11.585  1.00 12.99           C  
-ANISOU 3331  C   HIS B 366     1360   1512   2061     50    660    194       C  
-ATOM   3332  O   HIS B 366      73.856  11.062 -11.769  1.00 14.24           O  
-ANISOU 3332  O   HIS B 366     1476   1497   2436     32    406     72       O  
-ATOM   3333  CB  HIS B 366      72.076  13.391 -13.130  1.00 13.53           C  
-ANISOU 3333  CB  HIS B 366     1803   1687   1650    116    382   -377       C  
-ATOM   3334  CG  HIS B 366      71.965  12.280 -14.132  1.00 15.67           C  
-ANISOU 3334  CG  HIS B 366     2244   1420   2291     80    153   -349       C  
-ATOM   3335  ND1 HIS B 366      71.397  11.060 -13.847  1.00 19.17           N  
-ANISOU 3335  ND1 HIS B 366     2607   2122   2554     90    157   -706       N  
-ATOM   3336  CD2 HIS B 366      72.316  12.236 -15.440  1.00 17.95           C  
-ANISOU 3336  CD2 HIS B 366     2901   1788   2132    214    286   -748       C  
-ATOM   3337  CE1 HIS B 366      71.421  10.300 -14.930  1.00 17.81           C  
-ANISOU 3337  CE1 HIS B 366     2545   1687   2534    -56    164     51       C  
-ATOM   3338  NE2 HIS B 366      71.979  10.987 -15.908  1.00 20.32           N  
-ANISOU 3338  NE2 HIS B 366     2989   1995   2736    450    195  -1156       N  
-ATOM   3339  N   LEU B 367      74.744  13.074 -11.277  1.00 13.06           N  
-ANISOU 3339  N   LEU B 367     1260   1577   2123    -40    351     12       N  
-ATOM   3340  CA  LEU B 367      76.105  12.580 -11.072  1.00 13.88           C  
-ANISOU 3340  CA  LEU B 367     1246   1585   2441    -84    407    148       C  
-ATOM   3341  C   LEU B 367      76.390  12.296  -9.595  1.00 14.65           C  
-ANISOU 3341  C   LEU B 367     1551   1552   2461    168    287    169       C  
-ATOM   3342  O   LEU B 367      77.530  12.009  -9.210  1.00 16.62           O  
-ANISOU 3342  O   LEU B 367     1929   1734   2652    435     -9    124       O  
-ATOM   3343  CB  LEU B 367      77.129  13.578 -11.613  1.00 15.47           C  
-ANISOU 3343  CB  LEU B 367     1327   1876   2674     -6    614    261       C  
-ATOM   3344  CG  LEU B 367      77.093  13.822 -13.120  1.00 18.90           C  
-ANISOU 3344  CG  LEU B 367     1927   2262   2990     24    981    718       C  
-ATOM   3345  CD1 LEU B 367      78.166  14.816 -13.522  1.00 22.89           C  
-ANISOU 3345  CD1 LEU B 367     1951   2901   3845   -248    785    857       C  
-ATOM   3346  CD2 LEU B 367      77.293  12.523 -13.851  1.00 24.14           C  
-ANISOU 3346  CD2 LEU B 367     2543   2764   3864    676    336    -28       C  
-ATOM   3347  N   GLY B 368      75.358  12.409  -8.764  1.00 14.19           N  
-ANISOU 3347  N   GLY B 368     1733   1675   1983     40    187     23       N  
-ATOM   3348  CA  GLY B 368      75.452  12.009  -7.372  1.00 15.45           C  
-ANISOU 3348  CA  GLY B 368     1788   1712   2371   -176     94   -124       C  
-ATOM   3349  C   GLY B 368      75.903  13.062  -6.377  1.00 14.90           C  
-ANISOU 3349  C   GLY B 368     1407   1623   2629   -327    312     82       C  
-ATOM   3350  O   GLY B 368      76.146  12.744  -5.213  1.00 15.79           O  
-ANISOU 3350  O   GLY B 368     1544   2178   2276   -170    302    -43       O  
-ATOM   3351  N   THR B 369      76.014  14.315  -6.805  1.00 13.48           N  
-ANISOU 3351  N   THR B 369     1196   1611   2315    -36    306   -250       N  
-ATOM   3352  CA  THR B 369      76.495  15.355  -5.896  1.00 15.34           C  
-ANISOU 3352  CA  THR B 369     1138   1765   2926     68    374    -71       C  
-ATOM   3353  C   THR B 369      75.762  16.675  -6.041  1.00 13.66           C  
-ANISOU 3353  C   THR B 369     1346   1539   2306     25     33   -138       C  
-ATOM   3354  O   THR B 369      75.389  17.078  -7.148  1.00 15.61           O  
-ANISOU 3354  O   THR B 369     1641   1859   2430    238     85   -150       O  
-ATOM   3355  CB  THR B 369      77.999  15.629  -6.102  1.00 21.70           C  
-ANISOU 3355  CB  THR B 369     1589   2827   3827    437    747    713       C  
-ATOM   3356  OG1 THR B 369      78.210  16.161  -7.416  1.00 25.68           O  
-ANISOU 3356  OG1 THR B 369     1848   2931   4978    159    547     82       O  
-ATOM   3357  CG2 THR B 369      78.803  14.351  -5.940  1.00 24.40           C  
-ANISOU 3357  CG2 THR B 369     1763   2849   4658    473    325    209       C  
-ATOM   3358  N   VAL B 370      75.558  17.345  -4.910  1.00 13.22           N  
-ANISOU 3358  N   VAL B 370     1237   1478   2307   -164    172   -298       N  
-ATOM   3359  CA  VAL B 370      75.032  18.704  -4.905  1.00 13.78           C  
-ANISOU 3359  CA  VAL B 370     1116   1412   2707   -207    181   -120       C  
-ATOM   3360  C   VAL B 370      75.830  19.561  -3.932  1.00 14.62           C  
-ANISOU 3360  C   VAL B 370     1355   1761   2437   -136    -17    -22       C  
-ATOM   3361  O   VAL B 370      76.278  19.077  -2.896  1.00 14.26           O  
-ANISOU 3361  O   VAL B 370     1380   1609   2428   -358    -78   -127       O  
-ATOM   3362  CB  VAL B 370      73.528  18.750  -4.517  1.00 14.35           C  
-ANISOU 3362  CB  VAL B 370     1214   1560   2677   -217    269     83       C  
-ATOM   3363  CG1 VAL B 370      72.683  18.063  -5.579  1.00 14.63           C  
-ANISOU 3363  CG1 VAL B 370     1277   1707   2573   -239   -270   -526       C  
-ATOM   3364  CG2 VAL B 370      73.299  18.135  -3.138  1.00 15.76           C  
-ANISOU 3364  CG2 VAL B 370     1248   1891   2850    -98    499    -13       C  
-ATOM   3365  N   LYS B 371      76.016  20.831  -4.277  1.00 15.29           N  
-ANISOU 3365  N   LYS B 371     1522   1691   2594   -451    372   -334       N  
-ATOM   3366  CA  LYS B 371      76.693  21.767  -3.388  1.00 14.66           C  
-ANISOU 3366  CA  LYS B 371     1615   1520   2434   -565    379   -205       C  
-ATOM   3367  C   LYS B 371      75.751  22.253  -2.288  1.00 14.12           C  
-ANISOU 3367  C   LYS B 371     1388   1395   2580   -503     78    -94       C  
-ATOM   3368  O   LYS B 371      74.572  22.527  -2.544  1.00 14.60           O  
-ANISOU 3368  O   LYS B 371     1417   1343   2785   -381   -252    -25       O  
-ATOM   3369  CB  LYS B 371      77.220  22.966  -4.180  1.00 16.80           C  
-ANISOU 3369  CB  LYS B 371     1792   1597   2992   -719    299      7       C  
-ATOM   3370  CG  LYS B 371      77.766  24.094  -3.303  1.00 17.97           C  
-ANISOU 3370  CG  LYS B 371     1836   1931   3061  -1068     87     13       C  
-ATOM   3371  CD  LYS B 371      78.267  25.276  -4.120  1.00 19.44           C  
-ANISOU 3371  CD  LYS B 371     1967   2008   3411  -1065    195   -125       C  
-ATOM   3372  CE  LYS B 371      78.914  26.313  -3.212  1.00 21.01           C  
-ANISOU 3372  CE  LYS B 371     2309   2074   3598  -1020    191   -145       C  
-ATOM   3373  NZ  LYS B 371      79.474  27.474  -3.954  1.00 23.97           N  
-ANISOU 3373  NZ  LYS B 371     2425   2400   4283   -863    316    432       N  
-ATOM   3374  N   LEU B 372      76.275  22.346  -1.068  1.00 14.12           N  
-ANISOU 3374  N   LEU B 372     1490   1643   2231   -438    162   -152       N  
-ATOM   3375  CA  LEU B 372      75.561  22.967   0.044  1.00 14.73           C  
-ANISOU 3375  CA  LEU B 372     1520   1549   2528   -436     85   -106       C  
-ATOM   3376  C   LEU B 372      76.111  24.363   0.249  1.00 14.74           C  
-ANISOU 3376  C   LEU B 372     1239   1478   2883   -458    -12   -127       C  
-ATOM   3377  O   LEU B 372      77.333  24.560   0.213  1.00 16.63           O  
-ANISOU 3377  O   LEU B 372     1161   1876   3282   -465   -126   -429       O  
-ATOM   3378  CB  LEU B 372      75.771  22.184   1.345  1.00 16.91           C  
-ANISOU 3378  CB  LEU B 372     1752   1509   3164   -569      3    389       C  
-ATOM   3379  CG  LEU B 372      75.455  20.692   1.392  1.00 21.16           C  
-ANISOU 3379  CG  LEU B 372     2471   1971   3596   -468   -312    604       C  
-ATOM   3380  CD1 LEU B 372      75.421  20.196   2.824  1.00 21.99           C  
-ANISOU 3380  CD1 LEU B 372     2944   1983   3426    -73   -110    803       C  
-ATOM   3381  CD2 LEU B 372      74.146  20.429   0.712  1.00 23.97           C  
-ANISOU 3381  CD2 LEU B 372     2019   2284   4802   -610   -723   1241       C  
-ATOM   3382  N   GLU B 373      75.228  25.335   0.467  1.00 14.67           N  
-ANISOU 3382  N   GLU B 373     1482   1365   2727   -460   -121    -15       N  
-ATOM   3383  CA  GLU B 373      75.691  26.672   0.835  1.00 15.87           C  
-ANISOU 3383  CA  GLU B 373     1485   1611   2935   -559   -377   -293       C  
-ATOM   3384  C   GLU B 373      76.266  26.648   2.251  1.00 15.84           C  
-ANISOU 3384  C   GLU B 373     1383   1714   2922   -670   -230   -173       C  
-ATOM   3385  O   GLU B 373      75.648  26.123   3.175  1.00 16.07           O  
-ANISOU 3385  O   GLU B 373     1480   1629   2997   -532    -42    -87       O  
-ATOM   3386  CB  GLU B 373      74.558  27.695   0.729  1.00 16.88           C  
-ANISOU 3386  CB  GLU B 373     1607   1653   3154   -409   -144   -177       C  
-ATOM   3387  CG  GLU B 373      74.012  27.863  -0.687  1.00 15.98           C  
-ANISOU 3387  CG  GLU B 373     1710   1767   2595   -511    -44    119       C  
-ATOM   3388  CD  GLU B 373      75.096  28.242  -1.679  1.00 16.88           C  
-ANISOU 3388  CD  GLU B 373     1942   1588   2882   -681   -137   -145       C  
-ATOM   3389  OE1 GLU B 373      75.690  29.332  -1.521  1.00 19.14           O  
-ANISOU 3389  OE1 GLU B 373     2345   1657   3271   -778    106   -121       O  
-ATOM   3390  OE2 GLU B 373      75.366  27.454  -2.608  1.00 17.17           O  
-ANISOU 3390  OE2 GLU B 373     2081   1558   2885   -633     44     25       O  
-ATOM   3391  N   ASP B 374      77.452  27.214   2.427  1.00 16.99           N  
-ANISOU 3391  N   ASP B 374     1444   1990   3020   -751   -463    -15       N  
-ATOM   3392  CA  ASP B 374      78.073  27.203   3.738  1.00 18.46           C  
-ANISOU 3392  CA  ASP B 374     1827   2137   3050   -875   -688   -200       C  
-ATOM   3393  C   ASP B 374      77.373  28.193   4.668  1.00 19.47           C  
-ANISOU 3393  C   ASP B 374     2424   2072   2901   -533   -637   -247       C  
-ATOM   3394  O   ASP B 374      77.404  29.400   4.435  1.00 23.54           O  
-ANISOU 3394  O   ASP B 374     3100   2204   3638     23    -76    148       O  
-ATOM   3395  CB  ASP B 374      79.563  27.541   3.607  1.00 19.59           C  
-ANISOU 3395  CB  ASP B 374     1746   2541   3154   -898   -769    -75       C  
-ATOM   3396  CG  ASP B 374      80.314  27.413   4.917  1.00 21.66           C  
-ANISOU 3396  CG  ASP B 374     1929   2667   3632  -1079   -678    100       C  
-ATOM   3397  OD1 ASP B 374      79.707  26.999   5.932  1.00 22.90           O  
-ANISOU 3397  OD1 ASP B 374     1984   3022   3695   -936   -796    -29       O  
-ATOM   3398  OD2 ASP B 374      81.528  27.719   4.923  1.00 23.93           O  
-ANISOU 3398  OD2 ASP B 374     1995   3294   3802  -1040   -830    207       O  
-ATOM   3399  N   ASN B 375      76.742  27.676   5.719  1.00 18.79           N  
-ANISOU 3399  N   ASN B 375     2485   2087   2568   -739   -423   -502       N  
-ATOM   3400  CA  ASN B 375      76.076  28.523   6.706  1.00 19.22           C  
-ANISOU 3400  CA  ASN B 375     2588   1794   2921   -985   -385   -166       C  
-ATOM   3401  C   ASN B 375      76.807  28.523   8.041  1.00 21.10           C  
-ANISOU 3401  C   ASN B 375     2910   2084   3022   -780   -724     78       C  
-ATOM   3402  O   ASN B 375      76.236  28.885   9.071  1.00 20.41           O  
-ANISOU 3402  O   ASN B 375     2783   2064   2908   -796   -560   -114       O  
-ATOM   3403  CB  ASN B 375      74.615  28.105   6.900  1.00 20.26           C  
-ANISOU 3403  CB  ASN B 375     2625   1802   3270  -1021   -367   -263       C  
-ATOM   3404  CG  ASN B 375      74.475  26.681   7.394  1.00 21.08           C  
-ANISOU 3404  CG  ASN B 375     2733   1918   3359  -1091   -310   -647       C  
-ATOM   3405  OD1 ASN B 375      75.460  26.029   7.747  1.00 21.25           O  
-ANISOU 3405  OD1 ASN B 375     2793   1913   3369   -882   -213   -544       O  
-ATOM   3406  ND2 ASN B 375      73.241  26.193   7.433  1.00 22.44           N  
-ANISOU 3406  ND2 ASN B 375     2758   2166   3603  -1219   -209   -670       N  
-ATOM   3407  N   ASN B 376      78.067  28.099   8.010  1.00 22.34           N  
-ANISOU 3407  N   ASN B 376     3127   2152   3209   -762  -1182   -278       N  
-ATOM   3408  CA  ASN B 376      78.928  28.107   9.192  1.00 23.52           C  
-ANISOU 3408  CA  ASN B 376     3467   2163   3304   -425  -1451   -676       C  
-ATOM   3409  C   ASN B 376      78.514  27.068  10.232  1.00 24.38           C  
-ANISOU 3409  C   ASN B 376     3734   1963   3564   -559  -1492   -355       C  
-ATOM   3410  O   ASN B 376      79.044  27.045  11.342  1.00 27.72           O  
-ANISOU 3410  O   ASN B 376     4172   2272   4089   -440  -1444   -508       O  
-ATOM   3411  CB  ASN B 376      78.990  29.511   9.818  1.00 26.31           C  
-ANISOU 3411  CB  ASN B 376     3517   2463   4015   -348  -1662   -849       C  
-ATOM   3412  CG  ASN B 376      80.262  29.744  10.617  1.00 29.52           C  
-ANISOU 3412  CG  ASN B 376     3789   2421   5006   -188  -1862   -781       C  
-ATOM   3413  OD1 ASN B 376      80.212  30.140  11.783  1.00 33.31           O  
-ANISOU 3413  OD1 ASN B 376     4125   2646   5883    -83  -1434   -894       O  
-ATOM   3414  ND2 ASN B 376      81.409  29.491   9.993  1.00 31.67           N  
-ANISOU 3414  ND2 ASN B 376     3677   2856   5498   -420  -1819   -962       N  
-ATOM   3415  N   GLU B 377      77.586  26.191   9.861  1.00 22.67           N  
-ANISOU 3415  N   GLU B 377     3812   1762   3038   -520  -1252   -453       N  
-ATOM   3416  CA  GLU B 377      77.100  25.172  10.786  1.00 25.78           C  
-ANISOU 3416  CA  GLU B 377     4207   2028   3558   -313   -687   -418       C  
-ATOM   3417  C   GLU B 377      77.105  23.772  10.182  1.00 23.20           C  
-ANISOU 3417  C   GLU B 377     3913   1811   3092   -745   -532   -526       C  
-ATOM   3418  O   GLU B 377      76.300  22.922  10.572  1.00 26.76           O  
-ANISOU 3418  O   GLU B 377     4275   2058   3834   -606   -101     15       O  
-ATOM   3419  CB  GLU B 377      75.692  25.525  11.265  1.00 30.96           C  
-ANISOU 3419  CB  GLU B 377     4827   2508   4429    157   -196   -726       C  
-ATOM   3420  CG  GLU B 377      75.606  26.882  11.951  1.00 38.88           C  
-ANISOU 3420  CG  GLU B 377     5284   3320   6168    638    327   -592       C  
-ATOM   3421  CD  GLU B 377      74.185  27.258  12.317  1.00 47.26           C  
-ANISOU 3421  CD  GLU B 377     5796   4147   8013   1070    622   -424       C  
-ATOM   3422  OE1 GLU B 377      73.953  28.431  12.678  1.00 50.34           O  
-ANISOU 3422  OE1 GLU B 377     5913   4656   8558   1277    759   -319       O  
-ATOM   3423  OE2 GLU B 377      73.297  26.381  12.241  1.00 51.14           O  
-ANISOU 3423  OE2 GLU B 377     6061   4530   8841   1142    807   -274       O  
-ATOM   3424  N   LEU B 378      78.014  23.525   9.244  1.00 21.10           N  
-ANISOU 3424  N   LEU B 378     3302   1838   2875   -750   -579    -82       N  
-ATOM   3425  CA  LEU B 378      78.068  22.234   8.563  1.00 20.69           C  
-ANISOU 3425  CA  LEU B 378     2876   2002   2981   -599   -790   -109       C  
-ATOM   3426  C   LEU B 378      79.201  21.342   9.056  1.00 21.14           C  
-ANISOU 3426  C   LEU B 378     2652   2273   3107   -716  -1005   -205       C  
-ATOM   3427  O   LEU B 378      79.177  20.130   8.861  1.00 20.42           O  
-ANISOU 3427  O   LEU B 378     2500   2139   3119   -873   -800     30       O  
-ATOM   3428  CB  LEU B 378      78.208  22.437   7.055  1.00 19.16           C  
-ANISOU 3428  CB  LEU B 378     2603   2170   2508   -550   -810    142       C  
-ATOM   3429  CG  LEU B 378      77.027  23.131   6.379  1.00 18.99           C  
-ANISOU 3429  CG  LEU B 378     2047   2403   2765   -842   -762     67       C  
-ATOM   3430  CD1 LEU B 378      77.287  23.319   4.886  1.00 19.05           C  
-ANISOU 3430  CD1 LEU B 378     2143   2516   2579   -468   -293    -55       C  
-ATOM   3431  CD2 LEU B 378      75.753  22.332   6.620  1.00 22.21           C  
-ANISOU 3431  CD2 LEU B 378     2262   2829   3347   -837   -716    425       C  
-ATOM   3432  N   ASP B 379      80.198  21.933   9.699  1.00 22.75           N  
-ANISOU 3432  N   ASP B 379     2788   2392   3463   -473   -852     17       N  
-ATOM   3433  CA  ASP B 379      81.402  21.175  10.004  1.00 22.90           C  
-ANISOU 3433  CA  ASP B 379     2682   2462   3556   -779  -1197    -15       C  
-ATOM   3434  C   ASP B 379      81.184  19.955  10.896  1.00 21.92           C  
-ANISOU 3434  C   ASP B 379     2412   2600   3314   -577  -1098    217       C  
-ATOM   3435  O   ASP B 379      81.832  18.927  10.700  1.00 22.45           O  
-ANISOU 3435  O   ASP B 379     2240   2852   3438   -645   -865    208       O  
-ATOM   3436  CB  ASP B 379      82.495  22.088  10.558  1.00 26.15           C  
-ANISOU 3436  CB  ASP B 379     3185   2718   4032   -663  -1552   -218       C  
-ATOM   3437  CG  ASP B 379      82.988  23.072   9.525  1.00 31.61           C  
-ANISOU 3437  CG  ASP B 379     3846   3033   5132   -413  -1271   -226       C  
-ATOM   3438  OD1 ASP B 379      83.546  22.622   8.500  1.00 31.03           O  
-ANISOU 3438  OD1 ASP B 379     3835   3136   4817   -636  -1444   -306       O  
-ATOM   3439  OD2 ASP B 379      82.810  24.290   9.726  1.00 36.08           O  
-ANISOU 3439  OD2 ASP B 379     4381   3333   5995    -56  -1000      6       O  
-ATOM   3440  N   GLN B 380      80.266  20.053  11.856  1.00 20.94           N  
-ANISOU 3440  N   GLN B 380     2403   2714   2838   -180   -895     76       N  
-ATOM   3441  CA  GLN B 380      80.007  18.925  12.745  1.00 22.11           C  
-ANISOU 3441  CA  GLN B 380     2355   2863   3182     67  -1072   -197       C  
-ATOM   3442  C   GLN B 380      79.438  17.740  11.968  1.00 19.79           C  
-ANISOU 3442  C   GLN B 380     2035   2684   2801     43   -699    -49       C  
-ATOM   3443  O   GLN B 380      79.447  16.609  12.454  1.00 20.62           O  
-ANISOU 3443  O   GLN B 380     2192   2560   3081     88   -651    208       O  
-ATOM   3444  CB  GLN B 380      79.077  19.313  13.903  1.00 24.03           C  
-ANISOU 3444  CB  GLN B 380     2823   3177   3131    569   -850   -181       C  
-ATOM   3445  CG  GLN B 380      77.639  19.594  13.498  1.00 26.18           C  
-ANISOU 3445  CG  GLN B 380     3138   3518   3289    899  -1160   -436       C  
-ATOM   3446  CD  GLN B 380      76.656  19.434  14.654  1.00 29.71           C  
-ANISOU 3446  CD  GLN B 380     3715   3717   3854   1336   -930    -34       C  
-ATOM   3447  OE1 GLN B 380      75.915  20.358  14.986  1.00 33.35           O  
-ANISOU 3447  OE1 GLN B 380     4378   3788   4506   1460   -148    -94       O  
-ATOM   3448  NE2 GLN B 380      76.636  18.250  15.259  1.00 30.13           N  
-ANISOU 3448  NE2 GLN B 380     3656   3645   4146   1147  -1100   -443       N  
-ATOM   3449  N   PHE B 381      78.961  17.999  10.754  1.00 17.69           N  
-ANISOU 3449  N   PHE B 381     1630   2384   2706   -145   -393   -222       N  
-ATOM   3450  CA  PHE B 381      78.295  16.963   9.971  1.00 17.04           C  
-ANISOU 3450  CA  PHE B 381     1314   2294   2867   -164   -385    134       C  
-ATOM   3451  C   PHE B 381      79.163  16.394   8.858  1.00 15.74           C  
-ANISOU 3451  C   PHE B 381     1275   2063   2640   -265   -338    -15       C  
-ATOM   3452  O   PHE B 381      78.758  15.460   8.176  1.00 16.42           O  
-ANISOU 3452  O   PHE B 381     1211   1888   3138   -254   -279    116       O  
-ATOM   3453  CB  PHE B 381      76.971  17.478   9.390  1.00 17.05           C  
-ANISOU 3453  CB  PHE B 381     1227   2038   3213    -91   -434    291       C  
-ATOM   3454  CG  PHE B 381      75.984  17.918  10.429  1.00 16.43           C  
-ANISOU 3454  CG  PHE B 381     1197   1805   3240    -21      3    137       C  
-ATOM   3455  CD1 PHE B 381      75.325  16.982  11.214  1.00 16.63           C  
-ANISOU 3455  CD1 PHE B 381     1150   1836   3332    101    -39    -63       C  
-ATOM   3456  CD2 PHE B 381      75.710  19.263  10.620  1.00 17.33           C  
-ANISOU 3456  CD2 PHE B 381     1351   1769   3464     85   -348   -121       C  
-ATOM   3457  CE1 PHE B 381      74.412  17.383  12.175  1.00 16.17           C  
-ANISOU 3457  CE1 PHE B 381     1305   1728   3109    182     39   -297       C  
-ATOM   3458  CE2 PHE B 381      74.802  19.668  11.572  1.00 17.13           C  
-ANISOU 3458  CE2 PHE B 381     1376   1713   3418    103   -447    -55       C  
-ATOM   3459  CZ  PHE B 381      74.153  18.729  12.356  1.00 17.57           C  
-ANISOU 3459  CZ  PHE B 381     1471   1687   3517    190    -54    227       C  
-ATOM   3460  N   VAL B 382      80.353  16.952   8.668  1.00 16.09           N  
-ANISOU 3460  N   VAL B 382     1177   2061   2873   -235   -417     86       N  
-ATOM   3461  CA  VAL B 382      81.227  16.458   7.615  1.00 16.70           C  
-ANISOU 3461  CA  VAL B 382     1165   2039   3142   -389   -166    -84       C  
-ATOM   3462  C   VAL B 382      81.591  15.001   7.891  1.00 16.88           C  
-ANISOU 3462  C   VAL B 382     1125   2103   3185   -379   -526   -125       C  
-ATOM   3463  O   VAL B 382      82.006  14.648   8.995  1.00 19.70           O  
-ANISOU 3463  O   VAL B 382     1379   2522   3584    -39   -441    -62       O  
-ATOM   3464  CB  VAL B 382      82.486  17.338   7.454  1.00 18.12           C  
-ANISOU 3464  CB  VAL B 382     1237   2122   3526   -472    126   -134       C  
-ATOM   3465  CG1 VAL B 382      83.487  16.693   6.500  1.00 21.11           C  
-ANISOU 3465  CG1 VAL B 382     1396   2461   4162   -495    118    105       C  
-ATOM   3466  CG2 VAL B 382      82.088  18.726   6.964  1.00 20.25           C  
-ANISOU 3466  CG2 VAL B 382     1498   2109   4085   -324    168   -116       C  
-ATOM   3467  N   GLY B 383      81.399  14.149   6.890  1.00 17.03           N  
-ANISOU 3467  N   GLY B 383     1038   1843   3588   -215   -203    -50       N  
-ATOM   3468  CA  GLY B 383      81.627  12.728   7.047  1.00 17.68           C  
-ANISOU 3468  CA  GLY B 383     1152   1834   3730    -55   -146    258       C  
-ATOM   3469  C   GLY B 383      80.430  11.948   7.568  1.00 17.70           C  
-ANISOU 3469  C   GLY B 383     1210   1935   3581    -38   -301    159       C  
-ATOM   3470  O   GLY B 383      80.484  10.723   7.645  1.00 19.90           O  
-ANISOU 3470  O   GLY B 383     1651   2023   3886    155   -283    135       O  
-ATOM   3471  N   LYS B 384      79.348  12.648   7.919  1.00 16.26           N  
-ANISOU 3471  N   LYS B 384     1059   1997   3121    -67   -519    248       N  
-ATOM   3472  CA  LYS B 384      78.158  12.007   8.484  1.00 15.27           C  
-ANISOU 3472  CA  LYS B 384     1083   2009   2709   -206   -349    244       C  
-ATOM   3473  C   LYS B 384      77.066  11.823   7.439  1.00 13.33           C  
-ANISOU 3473  C   LYS B 384      986   1570   2507    113   -333    198       C  
-ATOM   3474  O   LYS B 384      76.869  12.687   6.569  1.00 14.31           O  
-ANISOU 3474  O   LYS B 384     1127   1670   2639    -87   -347     88       O  
-ATOM   3475  CB  LYS B 384      77.578  12.842   9.633  1.00 17.24           C  
-ANISOU 3475  CB  LYS B 384     1474   2489   2588   -271   -646    -44       C  
-ATOM   3476  CG  LYS B 384      78.577  13.294  10.681  1.00 22.74           C  
-ANISOU 3476  CG  LYS B 384     1947   3259   3432   -300   -868    214       C  
-ATOM   3477  CD  LYS B 384      78.939  12.175  11.609  1.00 24.89           C  
-ANISOU 3477  CD  LYS B 384     1977   3740   3741   -434  -1344    415       C  
-ATOM   3478  CE  LYS B 384      79.887  12.655  12.712  1.00 23.81           C  
-ANISOU 3478  CE  LYS B 384     2009   3796   3241   -474  -1262    636       C  
-ATOM   3479  NZ  LYS B 384      80.560  11.497  13.356  1.00 26.97           N  
-ANISOU 3479  NZ  LYS B 384     2353   4301   3592   -276   -939    732       N  
-ATOM   3480  N   GLU B 385      76.329  10.719   7.542  1.00 13.11           N  
-ANISOU 3480  N   GLU B 385      799   1473   2709     45     53   -293       N  
-ATOM   3481  CA  GLU B 385      75.180  10.498   6.668  1.00 12.64           C  
-ANISOU 3481  CA  GLU B 385      777   1463   2561    -53   -136   -408       C  
-ATOM   3482  C   GLU B 385      73.937  11.177   7.232  1.00 11.22           C  
-ANISOU 3482  C   GLU B 385      818   1255   2191     79     39   -225       C  
-ATOM   3483  O   GLU B 385      73.625  11.057   8.421  1.00 12.23           O  
-ANISOU 3483  O   GLU B 385     1108   1284   2254    298    -34    -40       O  
-ATOM   3484  CB  GLU B 385      74.896   9.005   6.460  1.00 14.91           C  
-ANISOU 3484  CB  GLU B 385     1130   1647   2886    148   -116   -505       C  
-ATOM   3485  CG  GLU B 385      74.013   8.761   5.239  1.00 17.60           C  
-ANISOU 3485  CG  GLU B 385     1397   1905   3383    -20   -564  -1067       C  
-ATOM   3486  CD  GLU B 385      73.612   7.318   5.029  1.00 23.25           C  
-ANISOU 3486  CD  GLU B 385     1821   2284   4728    276   -247  -1096       C  
-ATOM   3487  OE1 GLU B 385      73.616   6.544   6.007  1.00 23.44           O  
-ANISOU 3487  OE1 GLU B 385     2414   1984   4508    182    985    -75       O  
-ATOM   3488  OE2 GLU B 385      73.278   6.964   3.872  1.00 26.68           O  
-ANISOU 3488  OE2 GLU B 385     1825   2857   5456    380   -829  -1610       O  
-ATOM   3489  N   VAL B 386      73.223  11.889   6.372  1.00 10.87           N  
-ANISOU 3489  N   VAL B 386      748    944   2437     81   -111   -263       N  
-ATOM   3490  CA  VAL B 386      72.027  12.598   6.800  1.00 10.66           C  
-ANISOU 3490  CA  VAL B 386      903    886   2261     -3   -138   -426       C  
-ATOM   3491  C   VAL B 386      70.866  12.329   5.853  1.00 10.01           C  
-ANISOU 3491  C   VAL B 386      982   1031   1791     67   -129   -363       C  
-ATOM   3492  O   VAL B 386      71.061  11.959   4.686  1.00 10.88           O  
-ANISOU 3492  O   VAL B 386      947   1158   2030     57    -96   -345       O  
-ATOM   3493  CB  VAL B 386      72.270  14.128   6.886  1.00 11.49           C  
-ANISOU 3493  CB  VAL B 386     1145   1183   2038   -108   -293   -176       C  
-ATOM   3494  CG1 VAL B 386      73.374  14.439   7.897  1.00 12.52           C  
-ANISOU 3494  CG1 VAL B 386     1001   1466   2289    -95   -520   -323       C  
-ATOM   3495  CG2 VAL B 386      72.603  14.720   5.512  1.00 13.25           C  
-ANISOU 3495  CG2 VAL B 386     1498   1305   2230     25   -189     -6       C  
-ATOM   3496  N   VAL B 387      69.650  12.522   6.356  1.00  9.71           N  
-ANISOU 3496  N   VAL B 387      626   1218   1844     64   -212    -24       N  
-ATOM   3497  CA  VAL B 387      68.499  12.623   5.479  1.00 11.24           C  
-ANISOU 3497  CA  VAL B 387     1014    964   2292     86   -227   -200       C  
-ATOM   3498  C   VAL B 387      67.998  14.058   5.535  1.00 10.63           C  
-ANISOU 3498  C   VAL B 387     1125    978   1934    180    240   -291       C  
-ATOM   3499  O   VAL B 387      67.936  14.661   6.610  1.00 10.87           O  
-ANISOU 3499  O   VAL B 387     1309    914   1908    107    -23   -257       O  
-ATOM   3500  CB  VAL B 387      67.383  11.623   5.847  1.00 10.46           C  
-ANISOU 3500  CB  VAL B 387      811    929   2235   -158    -62    -99       C  
-ATOM   3501  CG1 VAL B 387      67.769  10.202   5.432  1.00 12.72           C  
-ANISOU 3501  CG1 VAL B 387     1261    800   2772    162   -173   -163       C  
-ATOM   3502  CG2 VAL B 387      67.046  11.674   7.323  1.00 13.26           C  
-ANISOU 3502  CG2 VAL B 387     1181   1663   2192    236    303   -187       C  
-ATOM   3503  N   LEU B 388      67.685  14.605   4.365  1.00 10.30           N  
-ANISOU 3503  N   LEU B 388      961    796   2157    161   -208     61       N  
-ATOM   3504  CA  LEU B 388      67.244  15.991   4.240  1.00  9.29           C  
-ANISOU 3504  CA  LEU B 388      829    838   1863      2   -206      9       C  
-ATOM   3505  C   LEU B 388      65.806  16.045   3.736  1.00  9.21           C  
-ANISOU 3505  C   LEU B 388      889    988   1621    109   -147   -130       C  
-ATOM   3506  O   LEU B 388      65.391  15.220   2.916  1.00 11.50           O  
-ANISOU 3506  O   LEU B 388     1183   1176   2011    162   -331   -443       O  
-ATOM   3507  CB  LEU B 388      68.144  16.753   3.267  1.00 10.48           C  
-ANISOU 3507  CB  LEU B 388      831   1040   2112    -46   -260    -39       C  
-ATOM   3508  CG  LEU B 388      69.653  16.730   3.533  1.00 10.43           C  
-ANISOU 3508  CG  LEU B 388      892    987   2083   -149   -105   -463       C  
-ATOM   3509  CD1 LEU B 388      70.336  15.678   2.650  1.00 12.98           C  
-ANISOU 3509  CD1 LEU B 388     1318   1618   1995    163    -55   -207       C  
-ATOM   3510  CD2 LEU B 388      70.261  18.109   3.303  1.00 13.57           C  
-ANISOU 3510  CD2 LEU B 388     1257   1157   2741   -245   -153    -59       C  
-ATOM   3511  N   GLU B 389      65.059  17.034   4.206  1.00 10.35           N  
-ANISOU 3511  N   GLU B 389     1002   1024   1905    265   -189   -275       N  
-ATOM   3512  CA  GLU B 389      63.695  17.257   3.740  1.00 10.68           C  
-ANISOU 3512  CA  GLU B 389     1110    899   2050     45   -223     99       C  
-ATOM   3513  C   GLU B 389      63.516  18.726   3.377  1.00  9.53           C  
-ANISOU 3513  C   GLU B 389      924    719   1979     68   -243     59       C  
-ATOM   3514  O   GLU B 389      64.141  19.615   3.965  1.00 10.03           O  
-ANISOU 3514  O   GLU B 389     1028    929   1853    -13   -235    -94       O  
-ATOM   3515  CB  GLU B 389      62.678  16.823   4.797  1.00 13.30           C  
-ANISOU 3515  CB  GLU B 389     1565   1417   2072     45     47    100       C  
-ATOM   3516  CG  GLU B 389      62.835  17.527   6.130  1.00 18.53           C  
-ANISOU 3516  CG  GLU B 389     2116   2344   2578    194    130    -55       C  
-ATOM   3517  CD  GLU B 389      61.730  17.206   7.120  1.00 24.52           C  
-ANISOU 3517  CD  GLU B 389     2340   3367   3608    163    287    236       C  
-ATOM   3518  OE1 GLU B 389      60.655  16.744   6.687  1.00 22.11           O  
-ANISOU 3518  OE1 GLU B 389     2286   3102   3012   -505    117    -73       O  
-ATOM   3519  OE2 GLU B 389      61.943  17.418   8.336  1.00 30.71           O  
-ANISOU 3519  OE2 GLU B 389     2630   4280   4758    522   -161    429       O  
-ATOM   3520  N   LEU B 390      62.648  18.978   2.409  1.00 10.36           N  
-ANISOU 3520  N   LEU B 390     1217    879   1839    398   -372    104       N  
-ATOM   3521  CA  LEU B 390      62.402  20.336   1.941  1.00  9.79           C  
-ANISOU 3521  CA  LEU B 390     1287    835   1596    472   -213    194       C  
-ATOM   3522  C   LEU B 390      61.463  21.081   2.884  1.00 10.61           C  
-ANISOU 3522  C   LEU B 390     1184    931   1915     19    -74   -198       C  
-ATOM   3523  O   LEU B 390      60.274  20.788   2.957  1.00 15.72           O  
-ANISOU 3523  O   LEU B 390     1265   1708   2999   -434    105   -630       O  
-ATOM   3524  CB  LEU B 390      61.809  20.294   0.533  1.00 10.85           C  
-ANISOU 3524  CB  LEU B 390     1373   1025   1723    300   -454    283       C  
-ATOM   3525  CG  LEU B 390      61.584  21.645  -0.146  1.00 10.45           C  
-ANISOU 3525  CG  LEU B 390     1295    847   1827     77    -78    321       C  
-ATOM   3526  CD1 LEU B 390      62.911  22.377  -0.335  1.00 12.82           C  
-ANISOU 3526  CD1 LEU B 390     1172   1148   2549   -129    101    169       C  
-ATOM   3527  CD2 LEU B 390      60.869  21.451  -1.479  1.00 11.88           C  
-ANISOU 3527  CD2 LEU B 390     1772   1223   1518    412   -503    -15       C  
-ATOM   3528  N   THR B 391      62.004  22.065   3.595  1.00  9.98           N  
-ANISOU 3528  N   THR B 391     1168    811   1812     13     23   -188       N  
-ATOM   3529  CA  THR B 391      61.200  22.838   4.531  1.00  9.80           C  
-ANISOU 3529  CA  THR B 391     1243   1040   1439    338   -154    -62       C  
-ATOM   3530  C   THR B 391      60.508  24.002   3.843  1.00  9.60           C  
-ANISOU 3530  C   THR B 391     1120    895   1633     30    101    159       C  
-ATOM   3531  O   THR B 391      59.314  24.231   4.039  1.00 10.76           O  
-ANISOU 3531  O   THR B 391     1034   1074   1979    168     86    -22       O  
-ATOM   3532  CB  THR B 391      62.061  23.335   5.689  1.00 10.20           C  
-ANISOU 3532  CB  THR B 391     1466    973   1437    415   -151   -164       C  
-ATOM   3533  OG1 THR B 391      62.633  22.195   6.334  1.00 12.67           O  
-ANISOU 3533  OG1 THR B 391     1627   1292   1893    512   -390     29       O  
-ATOM   3534  CG2 THR B 391      61.227  24.115   6.695  1.00 11.38           C  
-ANISOU 3534  CG2 THR B 391     1624   1086   1614    184    -19   -128       C  
-ATOM   3535  N   TRP B 392      61.259  24.745   3.042  1.00  9.86           N  
-ANISOU 3535  N   TRP B 392     1362    595   1787    116   -186     89       N  
-ATOM   3536  CA  TRP B 392      60.671  25.835   2.281  1.00  9.70           C  
-ANISOU 3536  CA  TRP B 392     1504    524   1656    230     31   -121       C  
-ATOM   3537  C   TRP B 392      61.557  26.185   1.096  1.00 10.32           C  
-ANISOU 3537  C   TRP B 392     1500    962   1457     11     85    245       C  
-ATOM   3538  O   TRP B 392      62.676  25.670   0.977  1.00 10.89           O  
-ANISOU 3538  O   TRP B 392     1342    949   1846    -31    -73   -159       O  
-ATOM   3539  CB  TRP B 392      60.362  27.054   3.174  1.00 10.49           C  
-ANISOU 3539  CB  TRP B 392     1542    623   1820     90    -55   -349       C  
-ATOM   3540  CG  TRP B 392      61.552  27.755   3.773  1.00 10.46           C  
-ANISOU 3540  CG  TRP B 392     1546    768   1658     97    -24   -205       C  
-ATOM   3541  CD1 TRP B 392      62.339  27.331   4.818  1.00 11.20           C  
-ANISOU 3541  CD1 TRP B 392     1414    841   2001   -148   -155   -491       C  
-ATOM   3542  CD2 TRP B 392      62.045  29.048   3.401  1.00 11.29           C  
-ANISOU 3542  CD2 TRP B 392     1621    683   1984     17     12   -210       C  
-ATOM   3543  NE1 TRP B 392      63.304  28.278   5.096  1.00 12.20           N  
-ANISOU 3543  NE1 TRP B 392     1547    901   2185    123    -37     39       N  
-ATOM   3544  CE2 TRP B 392      63.141  29.339   4.243  1.00 11.88           C  
-ANISOU 3544  CE2 TRP B 392     1687    791   2036   -167    117   -161       C  
-ATOM   3545  CE3 TRP B 392      61.671  29.984   2.428  1.00 12.26           C  
-ANISOU 3545  CE3 TRP B 392     1787    892   1977    -65    105     65       C  
-ATOM   3546  CZ2 TRP B 392      63.865  30.532   4.143  1.00 13.30           C  
-ANISOU 3546  CZ2 TRP B 392     1880   1019   2152      6    149     35       C  
-ATOM   3547  CZ3 TRP B 392      62.386  31.175   2.342  1.00 13.51           C  
-ANISOU 3547  CZ3 TRP B 392     1913    889   2332   -198     76   -147       C  
-ATOM   3548  CH2 TRP B 392      63.475  31.428   3.185  1.00 14.05           C  
-ANISOU 3548  CH2 TRP B 392     1874   1015   2448   -215     81   -259       C  
-ATOM   3549  N   VAL B 393      61.044  27.036   0.212  1.00 10.51           N  
-ANISOU 3549  N   VAL B 393     1515    801   1678   -146    -35    161       N  
-ATOM   3550  CA  VAL B 393      61.731  27.382  -1.024  1.00 10.58           C  
-ANISOU 3550  CA  VAL B 393     1561    790   1667    -62      0     78       C  
-ATOM   3551  C   VAL B 393      61.675  28.890  -1.219  1.00 11.30           C  
-ANISOU 3551  C   VAL B 393     1559    704   2031    -33     31    142       C  
-ATOM   3552  O   VAL B 393      60.651  29.523  -0.937  1.00 11.97           O  
-ANISOU 3552  O   VAL B 393     1548    913   2088    134     94     17       O  
-ATOM   3553  CB  VAL B 393      61.063  26.701  -2.240  1.00 11.41           C  
-ANISOU 3553  CB  VAL B 393     1585   1056   1693    131    200    145       C  
-ATOM   3554  CG1 VAL B 393      61.758  27.107  -3.539  1.00 12.39           C  
-ANISOU 3554  CG1 VAL B 393     1797   1268   1643    118     44    192       C  
-ATOM   3555  CG2 VAL B 393      61.046  25.176  -2.064  1.00 12.52           C  
-ANISOU 3555  CG2 VAL B 393     1738    758   2259     75     81     32       C  
-ATOM   3556  N   SER B 394      62.775  29.470  -1.692  1.00 11.71           N  
-ANISOU 3556  N   SER B 394     1623    627   2198   -125    104    137       N  
-ATOM   3557  CA  SER B 394      62.768  30.882  -2.081  1.00 12.61           C  
-ANISOU 3557  CA  SER B 394     1698    798   2294   -198    274    359       C  
-ATOM   3558  C   SER B 394      63.328  31.057  -3.488  1.00 12.16           C  
-ANISOU 3558  C   SER B 394     1724    870   2026      1    269    115       C  
-ATOM   3559  O   SER B 394      63.951  30.146  -4.045  1.00 13.37           O  
-ANISOU 3559  O   SER B 394     1903    995   2183    115     60     87       O  
-ATOM   3560  CB  SER B 394      63.561  31.724  -1.078  1.00 14.10           C  
-ANISOU 3560  CB  SER B 394     1843   1139   2376   -165    -91    -41       C  
-ATOM   3561  OG  SER B 394      64.923  31.324  -1.023  1.00 14.03           O  
-ANISOU 3561  OG  SER B 394     1929   1018   2384   -117    106    152       O  
-ATOM   3562  N   ASN B 395      63.099  32.231  -4.065  1.00 12.85           N  
-ANISOU 3562  N   ASN B 395     1816    878   2189    -61      7    531       N  
-ATOM   3563  CA  ASN B 395      63.613  32.504  -5.397  1.00 13.49           C  
-ANISOU 3563  CA  ASN B 395     1910   1014   2202   -118    252    449       C  
-ATOM   3564  C   ASN B 395      65.120  32.692  -5.379  1.00 14.31           C  
-ANISOU 3564  C   ASN B 395     1998   1276   2162   -121    293    283       C  
-ATOM   3565  O   ASN B 395      65.696  33.164  -4.393  1.00 16.31           O  
-ANISOU 3565  O   ASN B 395     2263   1387   2546   -179     77    124       O  
-ATOM   3566  CB  ASN B 395      62.936  33.737  -6.015  1.00 14.87           C  
-ANISOU 3566  CB  ASN B 395     2389    834   2427    113     19    304       C  
-ATOM   3567  CG  ASN B 395      63.320  35.035  -5.317  1.00 16.18           C  
-ANISOU 3567  CG  ASN B 395     2581    963   2603     37    120    113       C  
-ATOM   3568  OD1 ASN B 395      62.938  35.269  -4.170  1.00 17.21           O  
-ANISOU 3568  OD1 ASN B 395     2880   1003   2654   -129    228    186       O  
-ATOM   3569  ND2 ASN B 395      64.067  35.890  -6.012  1.00 18.68           N  
-ANISOU 3569  ND2 ASN B 395     2554   1311   3233   -165    209    610       N  
-ATOM   3570  N   ARG B 396      65.751  32.291  -6.474  1.00 14.64           N  
-ANISOU 3570  N   ARG B 396     2008   1129   2423   -327    310    387       N  
-ATOM   3571  CA  ARG B 396      67.147  32.610  -6.721  1.00 15.66           C  
-ANISOU 3571  CA  ARG B 396     2100   1142   2707   -685    317     89       C  
-ATOM   3572  C   ARG B 396      67.242  34.112  -6.957  1.00 17.41           C  
-ANISOU 3572  C   ARG B 396     2292   1432   2890   -629     41   -124       C  
-ATOM   3573  O   ARG B 396      66.385  34.685  -7.626  1.00 17.74           O  
-ANISOU 3573  O   ARG B 396     2198   1585   2958   -544    135    442       O  
-ATOM   3574  CB  ARG B 396      67.614  31.852  -7.965  1.00 19.60           C  
-ANISOU 3574  CB  ARG B 396     2412   1260   3775   -457    791    -46       C  
-ATOM   3575  CG  ARG B 396      68.968  32.245  -8.491  1.00 21.35           C  
-ANISOU 3575  CG  ARG B 396     2918   1416   3777   -215    501     10       C  
-ATOM   3576  CD  ARG B 396      69.277  31.535  -9.796  1.00 18.95           C  
-ANISOU 3576  CD  ARG B 396     3015   1371   2813   -307    488    407       C  
-ATOM   3577  NE  ARG B 396      70.637  31.832 -10.228  1.00 21.84           N  
-ANISOU 3577  NE  ARG B 396     3089   1836   3374   -434    118    434       N  
-ATOM   3578  CZ  ARG B 396      71.244  31.273 -11.265  1.00 23.03           C  
-ANISOU 3578  CZ  ARG B 396     2912   2172   3664   -583    415    966       C  
-ATOM   3579  NH1 ARG B 396      70.608  30.380 -12.007  1.00 22.35           N  
-ANISOU 3579  NH1 ARG B 396     2866   2023   3601   -787    359    681       N  
-ATOM   3580  NH2 ARG B 396      72.491  31.617 -11.562  1.00 26.41           N  
-ANISOU 3580  NH2 ARG B 396     2802   2649   4581   -809    161    846       N  
-ATOM   3581  N   THR B 397      68.263  34.752  -6.395  1.00 17.95           N  
-ANISOU 3581  N   THR B 397     2717   1186   2915   -571    332    199       N  
-ATOM   3582  CA  THR B 397      68.489  36.174  -6.637  1.00 20.09           C  
-ANISOU 3582  CA  THR B 397     2994   1492   3145   -979    196    388       C  
-ATOM   3583  C   THR B 397      68.469  36.450  -8.138  1.00 21.61           C  
-ANISOU 3583  C   THR B 397     3181   1568   3461   -713    197    655       C  
-ATOM   3584  O   THR B 397      69.142  35.766  -8.910  1.00 21.48           O  
-ANISOU 3584  O   THR B 397     3264   1793   3103   -827    344    548       O  
-ATOM   3585  CB  THR B 397      69.839  36.626  -6.058  1.00 24.22           C  
-ANISOU 3585  CB  THR B 397     3614   1796   3792  -1231   -134    406       C  
-ATOM   3586  OG1 THR B 397      69.841  36.433  -4.639  1.00 28.18           O  
-ANISOU 3586  OG1 THR B 397     4106   2362   4240  -1070   -305     41       O  
-ATOM   3587  CG2 THR B 397      70.082  38.102  -6.358  1.00 26.12           C  
-ANISOU 3587  CG2 THR B 397     3999   1586   4339   -862   -332    425       C  
-ATOM   3588  N   GLY B 398      67.678  37.435  -8.549  1.00 21.26           N  
-ANISOU 3588  N   GLY B 398     3234   1630   3215   -740     57    916       N  
-ATOM   3589  CA  GLY B 398      67.621  37.824  -9.945  1.00 22.89           C  
-ANISOU 3589  CA  GLY B 398     3304   1809   3582   -624    -13    730       C  
-ATOM   3590  C   GLY B 398      66.580  37.089 -10.765  1.00 23.46           C  
-ANISOU 3590  C   GLY B 398     3481   2184   3247   -435     -4    975       C  
-ATOM   3591  O   GLY B 398      66.409  37.373 -11.955  1.00 27.52           O  
-ANISOU 3591  O   GLY B 398     3854   2771   3829   -454    106   1299       O  
-ATOM   3592  N   ALA B 399      65.872  36.154 -10.132  1.00 21.46           N  
-ANISOU 3592  N   ALA B 399     3263   1753   3138   -520    137    600       N  
-ATOM   3593  CA  ALA B 399      64.870  35.355 -10.827  1.00 20.63           C  
-ANISOU 3593  CA  ALA B 399     3142   1630   3065   -175    100    324       C  
-ATOM   3594  C   ALA B 399      63.579  35.291 -10.028  1.00 19.73           C  
-ANISOU 3594  C   ALA B 399     3031   1482   2981   -201     36    375       C  
-ATOM   3595  O   ALA B 399      63.582  35.477  -8.811  1.00 20.66           O  
-ANISOU 3595  O   ALA B 399     3164   1918   2769     -6    107    406       O  
-ATOM   3596  CB  ALA B 399      65.393  33.948 -11.079  1.00 21.80           C  
-ANISOU 3596  CB  ALA B 399     3188   1808   3288    142     60    341       C  
-ATOM   3597  N   THR B 400      62.473  35.022 -10.716  1.00 18.24           N  
-ANISOU 3597  N   THR B 400     2963   1526   2441     13    282    509       N  
-ATOM   3598  CA  THR B 400      61.223  34.728 -10.032  1.00 18.60           C  
-ANISOU 3598  CA  THR B 400     2876   1464   2726      6     12    587       C  
-ATOM   3599  C   THR B 400      61.226  33.258  -9.639  1.00 18.33           C  
-ANISOU 3599  C   THR B 400     2584   1313   3065     93    140    347       C  
-ATOM   3600  O   THR B 400      62.019  32.469 -10.166  1.00 17.30           O  
-ANISOU 3600  O   THR B 400     2330   1264   2978   -152     53    411       O  
-ATOM   3601  CB  THR B 400      60.000  34.986 -10.923  1.00 21.39           C  
-ANISOU 3601  CB  THR B 400     3343   2073   2711    356    190    702       C  
-ATOM   3602  OG1 THR B 400      60.064  34.152 -12.086  1.00 24.75           O  
-ANISOU 3602  OG1 THR B 400     3506   2854   3044    456   -246    428       O  
-ATOM   3603  CG2 THR B 400      59.960  36.441 -11.360  1.00 24.92           C  
-ANISOU 3603  CG2 THR B 400     3706   2153   3608    497    410   1440       C  
-ATOM   3604  N   LEU B 401      60.353  32.892  -8.707  1.00 15.18           N  
-ANISOU 3604  N   LEU B 401     2378   1059   2331   -305     83    384       N  
-ATOM   3605  CA  LEU B 401      60.197  31.494  -8.339  1.00 15.31           C  
-ANISOU 3605  CA  LEU B 401     2257   1238   2323   -168     -5    496       C  
-ATOM   3606  C   LEU B 401      59.229  30.812  -9.306  1.00 15.96           C  
-ANISOU 3606  C   LEU B 401     2225   1456   2382   -260     36     20       C  
-ATOM   3607  O   LEU B 401      58.012  30.971  -9.201  1.00 20.03           O  
-ANISOU 3607  O   LEU B 401     2308   2161   3142    179   -149   -523       O  
-ATOM   3608  CB  LEU B 401      59.720  31.369  -6.892  1.00 15.15           C  
-ANISOU 3608  CB  LEU B 401     2233   1087   2437    130     18    526       C  
-ATOM   3609  CG  LEU B 401      59.558  29.937  -6.377  1.00 13.42           C  
-ANISOU 3609  CG  LEU B 401     2067    917   2113    221    225    370       C  
-ATOM   3610  CD1 LEU B 401      60.804  29.091  -6.642  1.00 14.71           C  
-ANISOU 3610  CD1 LEU B 401     2095   1099   2393    336     65    169       C  
-ATOM   3611  CD2 LEU B 401      59.217  29.952  -4.895  1.00 15.62           C  
-ANISOU 3611  CD2 LEU B 401     2076   1456   2403    330    212    259       C  
-ATOM   3612  N   ASN B 402      59.789  30.076 -10.262  1.00 14.40           N  
-ANISOU 3612  N   ASN B 402     2367   1426   1678   -319    208     51       N  
-ATOM   3613  CA  ASN B 402      59.023  29.443 -11.333  1.00 14.23           C  
-ANISOU 3613  CA  ASN B 402     2408   1247   1752   -273    311    405       C  
-ATOM   3614  C   ASN B 402      58.841  27.957 -11.031  1.00 13.36           C  
-ANISOU 3614  C   ASN B 402     2283   1051   1743   -227    503    351       C  
-ATOM   3615  O   ASN B 402      59.783  27.170 -11.138  1.00 14.57           O  
-ANISOU 3615  O   ASN B 402     2086   1406   2045   -163    238    317       O  
-ATOM   3616  CB  ASN B 402      59.756  29.653 -12.666  1.00 16.26           C  
-ANISOU 3616  CB  ASN B 402     2672   1710   1797   -421    474    379       C  
-ATOM   3617  CG  ASN B 402      59.104  28.929 -13.836  1.00 18.17           C  
-ANISOU 3617  CG  ASN B 402     2967   2141   1794   -467    380    636       C  
-ATOM   3618  OD1 ASN B 402      58.059  28.297 -13.708  1.00 17.91           O  
-ANISOU 3618  OD1 ASN B 402     2987   1812   2005   -440    186    391       O  
-ATOM   3619  ND2 ASN B 402      59.741  29.025 -15.001  1.00 23.91           N  
-ANISOU 3619  ND2 ASN B 402     3292   3029   2763   -738    789    590       N  
-ATOM   3620  N   LEU B 403      57.632  27.579 -10.628  1.00 12.86           N  
-ANISOU 3620  N   LEU B 403     2082   1138   1666   -396    544    133       N  
-ATOM   3621  CA  LEU B 403      57.375  26.205 -10.198  1.00 12.13           C  
-ANISOU 3621  CA  LEU B 403     1940    991   1676   -377    370    151       C  
-ATOM   3622  C   LEU B 403      57.195  25.229 -11.366  1.00 12.91           C  
-ANISOU 3622  C   LEU B 403     2045   1195   1663    -63     11    244       C  
-ATOM   3623  O   LEU B 403      56.974  24.033 -11.153  1.00 12.78           O  
-ANISOU 3623  O   LEU B 403     2052   1014   1789   -175    221    168       O  
-ATOM   3624  CB  LEU B 403      56.181  26.161  -9.242  1.00 13.94           C  
-ANISOU 3624  CB  LEU B 403     1905   1294   2095   -261    663     -5       C  
-ATOM   3625  CG  LEU B 403      56.378  27.029  -7.991  1.00 13.34           C  
-ANISOU 3625  CG  LEU B 403     1857   1437   1773     17    467     66       C  
-ATOM   3626  CD1 LEU B 403      55.193  26.906  -7.036  1.00 15.14           C  
-ANISOU 3626  CD1 LEU B 403     1910   1835   2006    -48    710    -58       C  
-ATOM   3627  CD2 LEU B 403      57.690  26.688  -7.272  1.00 13.69           C  
-ANISOU 3627  CD2 LEU B 403     1841   1531   1829    223     34   -137       C  
-ATOM   3628  N   TRP B 404      57.290  25.743 -12.591  1.00 12.64           N  
-ANISOU 3628  N   TRP B 404     1969   1231   1603     23   -325     22       N  
-ATOM   3629  CA  TRP B 404      57.270  24.914 -13.792  1.00 13.96           C  
-ANISOU 3629  CA  TRP B 404     2081   1706   1517    -86   -414     60       C  
-ATOM   3630  C   TRP B 404      58.680  24.613 -14.307  1.00 14.37           C  
-ANISOU 3630  C   TRP B 404     2022   1392   2044   -183    -83     43       C  
-ATOM   3631  O   TRP B 404      58.854  23.797 -15.221  1.00 15.87           O  
-ANISOU 3631  O   TRP B 404     2045   1592   2393    107     56   -146       O  
-ATOM   3632  CB  TRP B 404      56.421  25.571 -14.891  1.00 17.33           C  
-ANISOU 3632  CB  TRP B 404     2645   2320   1620   -164   -550   -187       C  
-ATOM   3633  CG  TRP B 404      54.978  25.126 -14.861  1.00 21.72           C  
-ANISOU 3633  CG  TRP B 404     3148   2713   2391    336   -743   -256       C  
-ATOM   3634  CD1 TRP B 404      54.425  24.105 -15.580  1.00 23.79           C  
-ANISOU 3634  CD1 TRP B 404     3064   2454   3522    458   -853   -145       C  
-ATOM   3635  CD2 TRP B 404      53.915  25.677 -14.071  1.00 23.62           C  
-ANISOU 3635  CD2 TRP B 404     3250   2265   3459    471   -469   -393       C  
-ATOM   3636  NE1 TRP B 404      53.090  23.985 -15.287  1.00 24.95           N  
-ANISOU 3636  NE1 TRP B 404     3405   2418   3656   1252   -333    159       N  
-ATOM   3637  CE2 TRP B 404      52.751  24.936 -14.362  1.00 26.53           C  
-ANISOU 3637  CE2 TRP B 404     3496   2993   3591   1067   -347    258       C  
-ATOM   3638  CE3 TRP B 404      53.835  26.718 -13.140  1.00 28.18           C  
-ANISOU 3638  CE3 TRP B 404     3171   2983   4553    550    573   -577       C  
-ATOM   3639  CZ2 TRP B 404      51.524  25.208 -13.773  1.00 24.44           C  
-ANISOU 3639  CZ2 TRP B 404     2912   3084   3291   1007   -364     72       C  
-ATOM   3640  CZ3 TRP B 404      52.613  26.984 -12.546  1.00 29.36           C  
-ANISOU 3640  CZ3 TRP B 404     3095   2955   5104    546    333   -227       C  
-ATOM   3641  CH2 TRP B 404      51.474  26.232 -12.866  1.00 28.83           C  
-ANISOU 3641  CH2 TRP B 404     3100   2928   4925    715   -133   -219       C  
-ATOM   3642  N   ALA B 405      59.687  25.267 -13.729  1.00 13.86           N  
-ANISOU 3642  N   ALA B 405     1917   1375   1974     66    427    271       N  
-ATOM   3643  CA  ALA B 405      61.073  25.028 -14.132  1.00 15.30           C  
-ANISOU 3643  CA  ALA B 405     1956   1343   2513    -50    265    295       C  
-ATOM   3644  C   ALA B 405      61.504  23.586 -13.859  1.00 14.61           C  
-ANISOU 3644  C   ALA B 405     2035   1220   2295    -10    279    168       C  
-ATOM   3645  O   ALA B 405      61.248  23.042 -12.787  1.00 16.86           O  
-ANISOU 3645  O   ALA B 405     2283   1623   2499    102    401    535       O  
-ATOM   3646  CB  ALA B 405      62.011  25.992 -13.420  1.00 15.26           C  
-ANISOU 3646  CB  ALA B 405     1797   1545   2455   -405    130    314       C  
-ATOM   3647  N   VAL B 406      62.170  22.972 -14.831  1.00 14.16           N  
-ANISOU 3647  N   VAL B 406     1841   1552   1985    236    272     69       N  
-ATOM   3648  CA  VAL B 406      62.739  21.646 -14.639  1.00 15.19           C  
-ANISOU 3648  CA  VAL B 406     1802   1663   2304    261     86      0       C  
-ATOM   3649  C   VAL B 406      64.183  21.821 -14.187  1.00 14.52           C  
-ANISOU 3649  C   VAL B 406     1682   1657   2179    290    227    113       C  
-ATOM   3650  O   VAL B 406      64.944  22.537 -14.827  1.00 14.37           O  
-ANISOU 3650  O   VAL B 406     1753   1633   2074   -116    252    189       O  
-ATOM   3651  CB  VAL B 406      62.721  20.823 -15.945  1.00 17.38           C  
-ANISOU 3651  CB  VAL B 406     1845   2024   2733    455   -258    -79       C  
-ATOM   3652  CG1 VAL B 406      63.219  19.404 -15.690  1.00 17.98           C  
-ANISOU 3652  CG1 VAL B 406     2238   1909   2683    567     58   -233       C  
-ATOM   3653  CG2 VAL B 406      61.325  20.795 -16.540  1.00 19.05           C  
-ANISOU 3653  CG2 VAL B 406     1870   2370   2998     90     40    275       C  
-ATOM   3654  N   PRO B 407      64.565  21.184 -13.070  1.00 12.35           N  
-ANISOU 3654  N   PRO B 407     1280   1030   2381   -207    260     87       N  
-ATOM   3655  CA  PRO B 407      65.968  21.270 -12.647  1.00 12.00           C  
-ANISOU 3655  CA  PRO B 407     1362   1306   1890     12    344    -51       C  
-ATOM   3656  C   PRO B 407      66.906  20.747 -13.730  1.00 12.92           C  
-ANISOU 3656  C   PRO B 407     1502   1163   2245   -122    621     33       C  
-ATOM   3657  O   PRO B 407      66.565  19.816 -14.466  1.00 14.74           O  
-ANISOU 3657  O   PRO B 407     1689   1394   2517   -193    665   -280       O  
-ATOM   3658  CB  PRO B 407      66.019  20.347 -11.421  1.00 13.40           C  
-ANISOU 3658  CB  PRO B 407     1764   1285   2042    275    195     65       C  
-ATOM   3659  CG  PRO B 407      64.588  20.321 -10.908  1.00 12.68           C  
-ANISOU 3659  CG  PRO B 407     1417   1197   2205    -68    345    -33       C  
-ATOM   3660  CD  PRO B 407      63.756  20.348 -12.167  1.00 13.11           C  
-ANISOU 3660  CD  PRO B 407     1507   1407   2067     -3     87    125       C  
-ATOM   3661  N   ASN B 408      68.082  21.351 -13.828  1.00 13.26           N  
-ANISOU 3661  N   ASN B 408     1361   1295   2381    -14    764    195       N  
-ATOM   3662  CA  ASN B 408      69.150  20.757 -14.610  1.00 13.77           C  
-ANISOU 3662  CA  ASN B 408     1620   1258   2352   -233    799    185       C  
-ATOM   3663  C   ASN B 408      69.889  19.764 -13.725  1.00 13.59           C  
-ANISOU 3663  C   ASN B 408     1535   1187   2441      7    504     64       C  
-ATOM   3664  O   ASN B 408      70.779  20.136 -12.965  1.00 14.63           O  
-ANISOU 3664  O   ASN B 408     1721   1235   2601    158    134   -148       O  
-ATOM   3665  CB  ASN B 408      70.106  21.819 -15.155  1.00 16.91           C  
-ANISOU 3665  CB  ASN B 408     2006   1847   2570    -83    823    239       C  
-ATOM   3666  CG  ASN B 408      71.155  21.226 -16.078  1.00 24.51           C  
-ANISOU 3666  CG  ASN B 408     2739   2748   3825    485   1108   1186       C  
-ATOM   3667  OD1 ASN B 408      71.451  20.026 -16.008  1.00 28.57           O  
-ANISOU 3667  OD1 ASN B 408     3024   3535   4297    778   1137   1424       O  
-ATOM   3668  ND2 ASN B 408      71.722  22.052 -16.948  1.00 28.04           N  
-ANISOU 3668  ND2 ASN B 408     3202   3236   4217    364   1432    934       N  
-ATOM   3669  N   TYR B 409      69.500  18.495 -13.816  1.00 13.63           N  
-ANISOU 3669  N   TYR B 409     1422   1208   2549     80    673     51       N  
-ATOM   3670  CA  TYR B 409      70.015  17.468 -12.921  1.00 13.05           C  
-ANISOU 3670  CA  TYR B 409     1296   1068   2593     53    691    261       C  
-ATOM   3671  C   TYR B 409      71.453  17.079 -13.234  1.00 13.15           C  
-ANISOU 3671  C   TYR B 409     1532   1218   2246    -51    727    -82       C  
-ATOM   3672  O   TYR B 409      72.138  16.483 -12.391  1.00 14.47           O  
-ANISOU 3672  O   TYR B 409     1711   1404   2383      6    504   -169       O  
-ATOM   3673  CB  TYR B 409      69.140  16.216 -12.997  1.00 13.52           C  
-ANISOU 3673  CB  TYR B 409     1257   1341   2539   -243    734    111       C  
-ATOM   3674  CG  TYR B 409      67.726  16.404 -12.490  1.00 11.25           C  
-ANISOU 3674  CG  TYR B 409     1068   1121   2086    -98    578     34       C  
-ATOM   3675  CD1 TYR B 409      66.703  16.765 -13.353  1.00 12.42           C  
-ANISOU 3675  CD1 TYR B 409     1225   1244   2249     58    216   -232       C  
-ATOM   3676  CD2 TYR B 409      67.418  16.218 -11.145  1.00 12.50           C  
-ANISOU 3676  CD2 TYR B 409     1062   1466   2222     29    613    288       C  
-ATOM   3677  CE1 TYR B 409      65.410  16.930 -12.897  1.00 11.48           C  
-ANISOU 3677  CE1 TYR B 409     1335   1088   1939     52    588   -143       C  
-ATOM   3678  CE2 TYR B 409      66.119  16.375 -10.673  1.00 12.62           C  
-ANISOU 3678  CE2 TYR B 409     1226   1395   2174     68    271     75       C  
-ATOM   3679  CZ  TYR B 409      65.126  16.729 -11.557  1.00 10.21           C  
-ANISOU 3679  CZ  TYR B 409     1061    932   1885    -37    351    -13       C  
-ATOM   3680  OH  TYR B 409      63.840  16.892 -11.104  1.00 10.79           O  
-ANISOU 3680  OH  TYR B 409     1049   1031   2020     30    299     -9       O  
-ATOM   3681  N   GLY B 410      71.898  17.402 -14.446  1.00 13.62           N  
-ANISOU 3681  N   GLY B 410     1496   1235   2443   -123    974   -448       N  
-ATOM   3682  CA  GLY B 410      73.237  17.055 -14.887  1.00 14.43           C  
-ANISOU 3682  CA  GLY B 410     1822   1396   2264     61   1033   -255       C  
-ATOM   3683  C   GLY B 410      73.245  15.970 -15.948  1.00 15.49           C  
-ANISOU 3683  C   GLY B 410     2146   1389   2350    253   1006   -253       C  
-ATOM   3684  O   GLY B 410      72.369  15.113 -15.982  1.00 19.43           O  
-ANISOU 3684  O   GLY B 410     2671   1587   3123   -101   1184   -484       O  
-ATOM   3685  N   SER B 411      74.234  16.028 -16.830  1.00 14.50           N  
-ANISOU 3685  N   SER B 411     2071   1305   2133    622    896    120       N  
-ATOM   3686  CA  SER B 411      74.384  15.037 -17.885  1.00 14.75           C  
-ANISOU 3686  CA  SER B 411     2121   1575   1909    745    699   -170       C  
-ATOM   3687  C   SER B 411      75.651  14.246 -17.617  1.00 15.58           C  
-ANISOU 3687  C   SER B 411     1888   1481   2549    637    566   -418       C  
-ATOM   3688  O   SER B 411      76.602  14.748 -17.027  1.00 20.99           O  
-ANISOU 3688  O   SER B 411     2228   1662   4084    641    215   -635       O  
-ATOM   3689  CB  SER B 411      74.487  15.719 -19.242  1.00 20.99           C  
-ANISOU 3689  CB  SER B 411     2730   2599   2646    777    796    587       C  
-ATOM   3690  OG  SER B 411      75.752  16.338 -19.387  1.00 28.20           O  
-ANISOU 3690  OG  SER B 411     3474   3085   4154    827    751    542       O  
-ATOM   3691  N   ASN B 412      75.649  12.990 -18.039  1.00 13.61           N  
-ANISOU 3691  N   ASN B 412     1770   1452   1950    817    364   -190       N  
-ATOM   3692  CA  ASN B 412      76.806  12.127 -17.836  1.00 13.41           C  
-ANISOU 3692  CA  ASN B 412     1792   1372   1930    775    496     -6       C  
-ATOM   3693  C   ASN B 412      77.204  11.478 -19.149  1.00 12.55           C  
-ANISOU 3693  C   ASN B 412     1694   1130   1943    493    459     56       C  
-ATOM   3694  O   ASN B 412      76.777  10.368 -19.448  1.00 12.35           O  
-ANISOU 3694  O   ASN B 412     1717   1087   1887    383    384    -46       O  
-ATOM   3695  CB  ASN B 412      76.502  11.065 -16.777  1.00 13.99           C  
-ANISOU 3695  CB  ASN B 412     1591   1696   2026    893    175    144       C  
-ATOM   3696  CG  ASN B 412      77.745  10.288 -16.356  1.00 12.72           C  
-ANISOU 3696  CG  ASN B 412     1629   1501   1702    528    470     80       C  
-ATOM   3697  OD1 ASN B 412      78.785  10.360 -17.014  1.00 13.73           O  
-ANISOU 3697  OD1 ASN B 412     1620   1549   2048    470    470   -149       O  
-ATOM   3698  ND2 ASN B 412      77.641   9.538 -15.258  1.00 12.90           N  
-ANISOU 3698  ND2 ASN B 412     1680   1463   1758    464    271   -139       N  
-ATOM   3699  N   LEU B 413      78.032  12.176 -19.924  1.00 11.88           N  
-ANISOU 3699  N   LEU B 413     1732    959   1822    261    254   -249       N  
-ATOM   3700  CA  LEU B 413      78.483  11.694 -21.233  1.00 11.65           C  
-ANISOU 3700  CA  LEU B 413     1632    783   2009    399    329    -87       C  
-ATOM   3701  C   LEU B 413      77.326  11.139 -22.075  1.00 10.07           C  
-ANISOU 3701  C   LEU B 413     1496    672   1656     71    454   -278       C  
-ATOM   3702  O   LEU B 413      76.429  11.893 -22.447  1.00 12.32           O  
-ANISOU 3702  O   LEU B 413     1762    768   2149    446     91   -119       O  
-ATOM   3703  CB  LEU B 413      79.661  10.710 -21.094  1.00 12.06           C  
-ANISOU 3703  CB  LEU B 413     1396    839   2348   -164    386    -68       C  
-ATOM   3704  CG  LEU B 413      80.881  11.346 -20.414  1.00 12.38           C  
-ANISOU 3704  CG  LEU B 413     1538    704   2460    -92    374     44       C  
-ATOM   3705  CD1 LEU B 413      82.008  10.329 -20.228  1.00 12.81           C  
-ANISOU 3705  CD1 LEU B 413     1415   1014   2438    273    366    -56       C  
-ATOM   3706  CD2 LEU B 413      81.378  12.579 -21.193  1.00 16.07           C  
-ANISOU 3706  CD2 LEU B 413     1896    932   3279     48    300    325       C  
-ATOM   3707  N   THR B 414      77.339   9.841 -22.404  1.00 10.70           N  
-ANISOU 3707  N   THR B 414     1540    802   1723    -16    242   -245       N  
-ATOM   3708  CA  THR B 414      76.304   9.296 -23.289  1.00 10.23           C  
-ANISOU 3708  CA  THR B 414     1475    759   1654    233    465   -243       C  
-ATOM   3709  C   THR B 414      75.081   8.766 -22.544  1.00 12.23           C  
-ANISOU 3709  C   THR B 414     1529    996   2123    431    705    287       C  
-ATOM   3710  O   THR B 414      74.120   8.327 -23.175  1.00 13.04           O  
-ANISOU 3710  O   THR B 414     1432   1138   2384    305    429     72       O  
-ATOM   3711  CB  THR B 414      76.821   8.146 -24.185  1.00 10.62           C  
-ANISOU 3711  CB  THR B 414     1468    690   1877    291    440     70       C  
-ATOM   3712  OG1 THR B 414      77.045   6.988 -23.375  1.00 10.77           O  
-ANISOU 3712  OG1 THR B 414     1393    802   1895    299    378    152       O  
-ATOM   3713  CG2 THR B 414      78.113   8.539 -24.912  1.00 12.40           C  
-ANISOU 3713  CG2 THR B 414     1452    960   2300    -13    617    -85       C  
-ATOM   3714  N   GLN B 415      75.112   8.786 -21.216  1.00 12.15           N  
-ANISOU 3714  N   GLN B 415     1277   1223   2116    324    689    238       N  
-ATOM   3715  CA  GLN B 415      74.028   8.167 -20.456  1.00 13.48           C  
-ANISOU 3715  CA  GLN B 415     1226   1904   1991    -15    551    353       C  
-ATOM   3716  C   GLN B 415      72.716   8.929 -20.625  1.00 15.06           C  
-ANISOU 3716  C   GLN B 415     1239   2237   2247    184    629   -192       C  
-ATOM   3717  O   GLN B 415      72.702  10.159 -20.697  1.00 16.80           O  
-ANISOU 3717  O   GLN B 415     1568   2119   2695    386    428   -376       O  
-ATOM   3718  CB  GLN B 415      74.387   8.038 -18.971  1.00 17.12           C  
-ANISOU 3718  CB  GLN B 415     1582   2682   2239    203    794    535       C  
-ATOM   3719  CG  GLN B 415      75.695   7.279 -18.698  1.00 16.91           C  
-ANISOU 3719  CG  GLN B 415     1435   2789   2201   -151    441    348       C  
-ATOM   3720  CD  GLN B 415      75.716   5.882 -19.305  1.00 17.90           C  
-ANISOU 3720  CD  GLN B 415     1878   2622   2299   -248    212    359       C  
-ATOM   3721  OE1 GLN B 415      76.482   5.604 -20.228  1.00 20.75           O  
-ANISOU 3721  OE1 GLN B 415     2293   2531   3059   -197    442     60       O  
-ATOM   3722  NE2 GLN B 415      74.884   4.992 -18.774  1.00 19.28           N  
-ANISOU 3722  NE2 GLN B 415     1987   2473   2863   -464    376    429       N  
-ATOM   3723  N   ALA B 416      71.613   8.189 -20.666  1.00 17.05           N  
-ANISOU 3723  N   ALA B 416     1214   2385   2880    114    172   -507       N  
-ATOM   3724  CA  ALA B 416      70.290   8.796 -20.810  1.00 19.19           C  
-ANISOU 3724  CA  ALA B 416     1270   2777   3242     20    186  -1002       C  
-ATOM   3725  C   ALA B 416      69.956   9.725 -19.642  1.00 21.38           C  
-ANISOU 3725  C   ALA B 416     1681   3170   3272     65    493   -612       C  
-ATOM   3726  O   ALA B 416      70.393   9.501 -18.515  1.00 22.60           O  
-ANISOU 3726  O   ALA B 416     1884   3456   3245    383    884   -413       O  
-ATOM   3727  CB  ALA B 416      69.231   7.713 -20.955  1.00 21.88           C  
-ANISOU 3727  CB  ALA B 416     1599   2854   3858    129    101  -1431       C  
-ATOM   3728  N   SER B 417      69.187  10.776 -19.920  1.00 21.08           N  
-ANISOU 3728  N   SER B 417     2040   2910   3057    254    599   -484       N  
-ATOM   3729  CA  SER B 417      68.782  11.726 -18.882  1.00 20.24           C  
-ANISOU 3729  CA  SER B 417     2128   2671   2890    305    659    -60       C  
-ATOM   3730  C   SER B 417      67.892  11.065 -17.831  1.00 19.76           C  
-ANISOU 3730  C   SER B 417     2281   2787   2439    550    726   -398       C  
-ATOM   3731  O   SER B 417      67.951  11.420 -16.650  1.00 22.29           O  
-ANISOU 3731  O   SER B 417     2652   3214   2601    863    454   -708       O  
-ATOM   3732  CB  SER B 417      68.054  12.930 -19.489  1.00 22.48           C  
-ANISOU 3732  CB  SER B 417     2151   2650   3741    387    712    -26       C  
-ATOM   3733  OG  SER B 417      66.726  12.593 -19.870  1.00 18.31           O  
-ANISOU 3733  OG  SER B 417     1890   2359   2708    197    638    -64       O  
-ATOM   3734  N   GLN B 418      67.070  10.114 -18.276  1.00 15.77           N  
-ANISOU 3734  N   GLN B 418     1641   1895   2456    441    430   -282       N  
-ATOM   3735  CA  GLN B 418      66.083   9.442 -17.428  1.00 16.97           C  
-ANISOU 3735  CA  GLN B 418     1890   1977   2580    604    671    351       C  
-ATOM   3736  C   GLN B 418      64.913  10.351 -17.039  1.00 15.48           C  
-ANISOU 3736  C   GLN B 418     1772   1580   2530    417    428     59       C  
-ATOM   3737  O   GLN B 418      64.107   9.998 -16.178  1.00 16.02           O  
-ANISOU 3737  O   GLN B 418     2022   1661   2404    430    625    126       O  
-ATOM   3738  CB  GLN B 418      66.726   8.858 -16.164  1.00 20.31           C  
-ANISOU 3738  CB  GLN B 418     2273   2738   2704   1056    740    363       C  
-ATOM   3739  CG  GLN B 418      68.027   8.088 -16.390  1.00 23.93           C  
-ANISOU 3739  CG  GLN B 418     2703   2902   3488   1385    938    327       C  
-ATOM   3740  CD  GLN B 418      67.855   6.821 -17.213  1.00 29.05           C  
-ANISOU 3740  CD  GLN B 418     3313   3123   4601   1625   1152    557       C  
-ATOM   3741  OE1 GLN B 418      68.839   6.181 -17.596  1.00 35.86           O  
-ANISOU 3741  OE1 GLN B 418     3760   3669   6197   1797   1074    -79       O  
-ATOM   3742  NE2 GLN B 418      66.616   6.449 -17.487  1.00 27.66           N  
-ANISOU 3742  NE2 GLN B 418     3341   3028   4138   1621   1215    752       N  
-ATOM   3743  N   LEU B 419      64.818  11.524 -17.659  1.00 13.08           N  
-ANISOU 3743  N   LEU B 419     1490   1468   2012    309    507    -74       N  
-ATOM   3744  CA  LEU B 419      63.733  12.448 -17.329  1.00 13.42           C  
-ANISOU 3744  CA  LEU B 419     1488   1362   2248    100    497      9       C  
-ATOM   3745  C   LEU B 419      62.365  11.913 -17.730  1.00 12.59           C  
-ANISOU 3745  C   LEU B 419     1401   1365   2016     11    281   -125       C  
-ATOM   3746  O   LEU B 419      62.203  11.351 -18.815  1.00 15.59           O  
-ANISOU 3746  O   LEU B 419     1630   2077   2216     71    199   -542       O  
-ATOM   3747  CB  LEU B 419      63.941  13.800 -18.011  1.00 13.94           C  
-ANISOU 3747  CB  LEU B 419     1670   1382   2243     -1    374    -75       C  
-ATOM   3748  CG  LEU B 419      65.122  14.643 -17.537  1.00 15.01           C  
-ANISOU 3748  CG  LEU B 419     1974   1529   2198   -190     66    162       C  
-ATOM   3749  CD1 LEU B 419      65.393  15.772 -18.523  1.00 17.51           C  
-ANISOU 3749  CD1 LEU B 419     2452   1889   2311   -249    225    308       C  
-ATOM   3750  CD2 LEU B 419      64.861  15.186 -16.149  1.00 14.53           C  
-ANISOU 3750  CD2 LEU B 419     2012   1614   1895    -47    378    -50       C  
-ATOM   3751  N   ALA B 420      61.376  12.092 -16.857  1.00 11.61           N  
-ANISOU 3751  N   ALA B 420     1230   1100   2079    -14    256    -45       N  
-ATOM   3752  CA  ALA B 420      60.000  11.892 -17.274  1.00 11.67           C  
-ANISOU 3752  CA  ALA B 420     1347   1179   1907     12    161    -95       C  
-ATOM   3753  C   ALA B 420      59.728  12.915 -18.372  1.00 12.78           C  
-ANISOU 3753  C   ALA B 420     1656   1297   1904    181    212   -118       C  
-ATOM   3754  O   ALA B 420      60.207  14.043 -18.302  1.00 12.57           O  
-ANISOU 3754  O   ALA B 420     1632   1343   1802    173     92    -17       O  
-ATOM   3755  CB  ALA B 420      59.047  12.070 -16.102  1.00 12.24           C  
-ANISOU 3755  CB  ALA B 420     1599   1403   1647    116    429     27       C  
-ATOM   3756  N   PRO B 421      58.970  12.524 -19.404  1.00 14.43           N  
-ANISOU 3756  N   PRO B 421     1753   1573   2157     60    198     20       N  
-ATOM   3757  CA  PRO B 421      58.825  13.406 -20.569  1.00 14.24           C  
-ANISOU 3757  CA  PRO B 421     1859   1761   1789    182     53   -279       C  
-ATOM   3758  C   PRO B 421      57.941  14.638 -20.323  1.00 13.34           C  
-ANISOU 3758  C   PRO B 421     1779   1621   1667    -36    356    106       C  
-ATOM   3759  O   PRO B 421      57.128  14.655 -19.390  1.00 13.46           O  
-ANISOU 3759  O   PRO B 421     1725   1579   1809    103    198     12       O  
-ATOM   3760  CB  PRO B 421      58.174  12.493 -21.613  1.00 15.60           C  
-ANISOU 3760  CB  PRO B 421     2170   1847   1909   -119    289   -467       C  
-ATOM   3761  CG  PRO B 421      57.450  11.461 -20.808  1.00 19.20           C  
-ANISOU 3761  CG  PRO B 421     2362   2085   2846    103   -116   -409       C  
-ATOM   3762  CD  PRO B 421      58.310  11.224 -19.602  1.00 15.46           C  
-ANISOU 3762  CD  PRO B 421     1975   1657   2240     66   -260   -483       C  
-ATOM   3763  N   PRO B 422      58.087  15.666 -21.172  1.00 14.01           N  
-ANISOU 3763  N   PRO B 422     1854   1777   1691    305    533    164       N  
-ATOM   3764  CA  PRO B 422      57.145  16.785 -21.087  1.00 14.07           C  
-ANISOU 3764  CA  PRO B 422     1917   1797   1630    238    227    110       C  
-ATOM   3765  C   PRO B 422      55.733  16.335 -21.451  1.00 14.78           C  
-ANISOU 3765  C   PRO B 422     1958   1872   1785    255    290    166       C  
-ATOM   3766  O   PRO B 422      55.549  15.358 -22.189  1.00 16.04           O  
-ANISOU 3766  O   PRO B 422     1975   2181   1938    173     25    -43       O  
-ATOM   3767  CB  PRO B 422      57.672  17.774 -22.133  1.00 16.55           C  
-ANISOU 3767  CB  PRO B 422     2111   2027   2150    374    657    566       C  
-ATOM   3768  CG  PRO B 422      58.467  16.942 -23.079  1.00 21.33           C  
-ANISOU 3768  CG  PRO B 422     2586   2460   3056    832    972    876       C  
-ATOM   3769  CD  PRO B 422      59.035  15.807 -22.291  1.00 16.37           C  
-ANISOU 3769  CD  PRO B 422     2249   2291   1680    602    554    330       C  
-ATOM   3770  N   ILE B 423      54.742  17.031 -20.913  1.00 14.09           N  
-ANISOU 3770  N   ILE B 423     1676   1853   1825    -38    270     60       N  
-ATOM   3771  CA  ILE B 423      53.355  16.792 -21.278  1.00 14.09           C  
-ANISOU 3771  CA  ILE B 423     1750   1852   1751    -43    146    242       C  
-ATOM   3772  C   ILE B 423      52.878  17.996 -22.071  1.00 15.08           C  
-ANISOU 3772  C   ILE B 423     1955   2068   1705    -20   -315     16       C  
-ATOM   3773  O   ILE B 423      52.853  19.118 -21.566  1.00 15.73           O  
-ANISOU 3773  O   ILE B 423     2061   1876   2038      5    -59    -22       O  
-ATOM   3774  CB  ILE B 423      52.448  16.604 -20.049  1.00 13.96           C  
-ANISOU 3774  CB  ILE B 423     1679   1708   1916      1   -126    289       C  
-ATOM   3775  CG1 ILE B 423      52.959  15.464 -19.159  1.00 16.50           C  
-ANISOU 3775  CG1 ILE B 423     2022   1935   2311    123    134    511       C  
-ATOM   3776  CG2 ILE B 423      51.006  16.351 -20.484  1.00 15.63           C  
-ANISOU 3776  CG2 ILE B 423     1645   1739   2553   -141   -304     48       C  
-ATOM   3777  CD1 ILE B 423      52.232  15.355 -17.825  1.00 17.04           C  
-ANISOU 3777  CD1 ILE B 423     2182   2253   2037     95    475    346       C  
-ATOM   3778  N   TYR B 424      52.526  17.769 -23.328  1.00 16.89           N  
-ANISOU 3778  N   TYR B 424     2019   2601   1796    149   -337    237       N  
-ATOM   3779  CA  TYR B 424      52.063  18.863 -24.163  1.00 18.75           C  
-ANISOU 3779  CA  TYR B 424     2272   3186   1664    391    -71    556       C  
-ATOM   3780  C   TYR B 424      50.555  19.023 -24.037  1.00 21.22           C  
-ANISOU 3780  C   TYR B 424     2361   3441   2260    393   -447    365       C  
-ATOM   3781  O   TYR B 424      49.806  18.050 -24.121  1.00 22.54           O  
-ANISOU 3781  O   TYR B 424     2533   3634   2395    298   -370    412       O  
-ATOM   3782  CB  TYR B 424      52.510  18.660 -25.611  1.00 22.33           C  
-ANISOU 3782  CB  TYR B 424     2635   3870   1979    765    127    445       C  
-ATOM   3783  CG  TYR B 424      54.016  18.689 -25.739  1.00 25.70           C  
-ANISOU 3783  CG  TYR B 424     3008   4484   2272    851    411    681       C  
-ATOM   3784  CD1 TYR B 424      54.700  19.897 -25.829  1.00 27.41           C  
-ANISOU 3784  CD1 TYR B 424     3138   4766   2509    773    579    638       C  
-ATOM   3785  CD2 TYR B 424      54.761  17.516 -25.733  1.00 27.98           C  
-ANISOU 3785  CD2 TYR B 424     3186   4844   2600   1039    668    768       C  
-ATOM   3786  CE1 TYR B 424      56.078  19.935 -25.925  1.00 29.10           C  
-ANISOU 3786  CE1 TYR B 424     3230   5023   2802    859    680    683       C  
-ATOM   3787  CE2 TYR B 424      56.143  17.546 -25.834  1.00 29.60           C  
-ANISOU 3787  CE2 TYR B 424     3323   5067   2855   1072    754   1029       C  
-ATOM   3788  CZ  TYR B 424      56.794  18.758 -25.927  1.00 29.07           C  
-ANISOU 3788  CZ  TYR B 424     3257   5109   2678    895    915   1045       C  
-ATOM   3789  OH  TYR B 424      58.168  18.801 -26.022  1.00 31.69           O  
-ANISOU 3789  OH  TYR B 424     3282   5454   3303    885    600    867       O  
-ATOM   3790  N   PRO B 425      50.108  20.256 -23.782  1.00 23.10           N  
-ANISOU 3790  N   PRO B 425     2055   3674   3048    568   -818   -376       N  
-ATOM   3791  CA  PRO B 425      48.675  20.542 -23.688  1.00 24.02           C  
-ANISOU 3791  CA  PRO B 425     2026   3964   3135    734   -612   -377       C  
-ATOM   3792  C   PRO B 425      47.916  20.040 -24.914  1.00 20.81           C  
-ANISOU 3792  C   PRO B 425     2095   3949   1864    602   -199      9       C  
-ATOM   3793  O   PRO B 425      48.380  20.187 -26.042  1.00 23.20           O  
-ANISOU 3793  O   PRO B 425     2094   4015   2706    521   -128    170       O  
-ATOM   3794  CB  PRO B 425      48.634  22.069 -23.612  1.00 28.89           C  
-ANISOU 3794  CB  PRO B 425     2256   3997   4724    920   -701   -605       C  
-ATOM   3795  CG  PRO B 425      49.917  22.427 -22.942  1.00 30.86           C  
-ANISOU 3795  CG  PRO B 425     2363   4068   5293    998   -864   -493       C  
-ATOM   3796  CD  PRO B 425      50.931  21.436 -23.458  1.00 27.05           C  
-ANISOU 3796  CD  PRO B 425     2038   3733   4505    687   -870   -391       C  
-ATOM   3797  N   PRO B 426      46.745  19.439 -24.681  1.00 22.49           N  
-ANISOU 3797  N   PRO B 426     2271   4149   2124    348   -223    323       N  
-ATOM   3798  CA  PRO B 426      45.918  18.823 -25.720  1.00 23.68           C  
-ANISOU 3798  CA  PRO B 426     2650   4000   2347    485   -318    949       C  
-ATOM   3799  C   PRO B 426      45.293  19.845 -26.667  1.00 21.28           C  
-ANISOU 3799  C   PRO B 426     2583   3285   2215    571   -705    207       C  
-ATOM   3800  O   PRO B 426      45.063  19.525 -27.822  1.00 21.24           O  
-ANISOU 3800  O   PRO B 426     2806   3096   2166    844   -685    -76       O  
-ATOM   3801  CB  PRO B 426      44.825  18.117 -24.916  1.00 29.47           C  
-ANISOU 3801  CB  PRO B 426     3030   4448   3720    452     69    926       C  
-ATOM   3802  CG  PRO B 426      44.735  18.894 -23.650  1.00 30.60           C  
-ANISOU 3802  CG  PRO B 426     2869   4733   4024    353   -140   1173       C  
-ATOM   3803  CD  PRO B 426      46.141  19.310 -23.343  1.00 26.94           C  
-ANISOU 3803  CD  PRO B 426     2550   4637   3048    233   -241   1057       C  
-ATOM   3804  N   GLY B 427      45.021  21.052 -26.183  1.00 20.36           N  
-ANISOU 3804  N   GLY B 427     2604   2842   2290    377   -759    -65       N  
-ATOM   3805  CA  GLY B 427      44.358  22.054 -26.999  1.00 20.00           C  
-ANISOU 3805  CA  GLY B 427     2503   2611   2486    430   -869     32       C  
-ATOM   3806  C   GLY B 427      42.917  21.668 -27.273  1.00 18.56           C  
-ANISOU 3806  C   GLY B 427     2567   2292   2193    607   -653    126       C  
-ATOM   3807  O   GLY B 427      42.371  20.783 -26.608  1.00 17.12           O  
-ANISOU 3807  O   GLY B 427     2446   2181   1879    554   -314     -9       O  
-ATOM   3808  N   PHE B 428      42.306  22.338 -28.246  1.00 17.75           N  
-ANISOU 3808  N   PHE B 428     2593   2347   1802    850   -346   -222       N  
-ATOM   3809  CA  PHE B 428      40.918  22.090 -28.628  1.00 16.57           C  
-ANISOU 3809  CA  PHE B 428     2455   2276   1565    645    -86   -286       C  
-ATOM   3810  C   PHE B 428      39.963  22.148 -27.440  1.00 18.71           C  
-ANISOU 3810  C   PHE B 428     2762   2520   1828    934    -78    -44       C  
-ATOM   3811  O   PHE B 428      39.067  21.314 -27.297  1.00 20.83           O  
-ANISOU 3811  O   PHE B 428     2839   2965   2111    797     52    -20       O  
-ATOM   3812  CB  PHE B 428      40.791  20.775 -29.399  1.00 16.87           C  
-ANISOU 3812  CB  PHE B 428     2573   2240   1595    565     19    143       C  
-ATOM   3813  CG  PHE B 428      41.568  20.766 -30.678  1.00 16.34           C  
-ANISOU 3813  CG  PHE B 428     2601   2148   1458    539     68    185       C  
-ATOM   3814  CD1 PHE B 428      41.029  21.309 -31.833  1.00 16.58           C  
-ANISOU 3814  CD1 PHE B 428     2644   2229   1425    585   -247    -49       C  
-ATOM   3815  CD2 PHE B 428      42.853  20.252 -30.718  1.00 17.91           C  
-ANISOU 3815  CD2 PHE B 428     2613   2393   1797    558     -6    -16       C  
-ATOM   3816  CE1 PHE B 428      41.749  21.321 -33.005  1.00 18.81           C  
-ANISOU 3816  CE1 PHE B 428     2763   2312   2071    664    -19   -157       C  
-ATOM   3817  CE2 PHE B 428      43.577  20.252 -31.900  1.00 17.96           C  
-ANISOU 3817  CE2 PHE B 428     2655   2544   1624    695    323   -129       C  
-ATOM   3818  CZ  PHE B 428      43.018  20.793 -33.042  1.00 17.45           C  
-ANISOU 3818  CZ  PHE B 428     2868   2442   1319    755    -11    270       C  
-ATOM   3819  N   GLY B 429      40.170  23.148 -26.591  1.00 19.74           N  
-ANISOU 3819  N   GLY B 429     3075   2548   1877   1246    -64    124       N  
-ATOM   3820  CA  GLY B 429      39.289  23.389 -25.463  1.00 19.78           C  
-ANISOU 3820  CA  GLY B 429     3259   2756   1498   1327    248    255       C  
-ATOM   3821  C   GLY B 429      39.700  22.677 -24.190  1.00 20.46           C  
-ANISOU 3821  C   GLY B 429     3290   2720   1765   1138    124    449       C  
-ATOM   3822  O   GLY B 429      39.252  23.043 -23.107  1.00 21.59           O  
-ANISOU 3822  O   GLY B 429     3582   3029   1590   1177    122     95       O  
-ATOM   3823  N   GLU B 430      40.543  21.654 -24.302  1.00 18.35           N  
-ANISOU 3823  N   GLU B 430     2916   2555   1502    890   -210    290       N  
-ATOM   3824  CA  GLU B 430      41.004  20.951 -23.109  1.00 18.14           C  
-ANISOU 3824  CA  GLU B 430     2729   2349   1812    452   -272   -228       C  
-ATOM   3825  C   GLU B 430      42.168  21.683 -22.459  1.00 17.75           C  
-ANISOU 3825  C   GLU B 430     2685   2544   1515    427   -189    178       C  
-ATOM   3826  O   GLU B 430      42.936  22.376 -23.131  1.00 20.17           O  
-ANISOU 3826  O   GLU B 430     2927   2908   1829    344    181    258       O  
-ATOM   3827  CB  GLU B 430      41.391  19.502 -23.424  1.00 18.93           C  
-ANISOU 3827  CB  GLU B 430     2739   2205   2249    472   -539   -357       C  
-ATOM   3828  CG  GLU B 430      40.203  18.580 -23.679  1.00 19.28           C  
-ANISOU 3828  CG  GLU B 430     2821   2078   2425    387   -627   -201       C  
-ATOM   3829  CD  GLU B 430      40.620  17.140 -23.938  1.00 20.42           C  
-ANISOU 3829  CD  GLU B 430     3060   2361   2338    408   -969   -174       C  
-ATOM   3830  OE1 GLU B 430      41.575  16.665 -23.291  1.00 18.41           O  
-ANISOU 3830  OE1 GLU B 430     2923   2547   1526    269   -587      2       O  
-ATOM   3831  OE2 GLU B 430      40.002  16.485 -24.800  1.00 24.71           O  
-ANISOU 3831  OE2 GLU B 430     3413   2700   3275    577  -1428   -285       O  
-ATOM   3832  N   ALA B 431      42.295  21.515 -21.147  1.00 16.90           N  
-ANISOU 3832  N   ALA B 431     2463   2350   1607    504   -365     59       N  
-ATOM   3833  CA  ALA B 431      43.404  22.085 -20.395  1.00 16.37           C  
-ANISOU 3833  CA  ALA B 431     2423   2007   1790    643   -545    221       C  
-ATOM   3834  C   ALA B 431      43.871  21.066 -19.368  1.00 15.20           C  
-ANISOU 3834  C   ALA B 431     1994   1961   1818    468   -322    319       C  
-ATOM   3835  O   ALA B 431      43.058  20.351 -18.781  1.00 14.89           O  
-ANISOU 3835  O   ALA B 431     1941   2051   1664    134   -141    225       O  
-ATOM   3836  CB  ALA B 431      42.974  23.369 -19.704  1.00 18.29           C  
-ANISOU 3836  CB  ALA B 431     2591   2045   2312    543   -478    -67       C  
-ATOM   3837  N   ILE B 432      45.181  20.992 -19.157  1.00 14.09           N  
-ANISOU 3837  N   ILE B 432     1830   2001   1521    379   -326    278       N  
-ATOM   3838  CA  ILE B 432      45.734  20.120 -18.129  1.00 12.43           C  
-ANISOU 3838  CA  ILE B 432     1649   1858   1215    378     31    231       C  
-ATOM   3839  C   ILE B 432      45.239  20.564 -16.753  1.00 12.89           C  
-ANISOU 3839  C   ILE B 432     1791   1613   1493    525    -71    421       C  
-ATOM   3840  O   ILE B 432      45.200  21.767 -16.452  1.00 14.36           O  
-ANISOU 3840  O   ILE B 432     1969   1626   1860    485   -145    341       O  
-ATOM   3841  CB  ILE B 432      47.272  20.127 -18.162  1.00 13.25           C  
-ANISOU 3841  CB  ILE B 432     1675   1835   1524    326    -90    141       C  
-ATOM   3842  CG1 ILE B 432      47.780  19.571 -19.501  1.00 15.53           C  
-ANISOU 3842  CG1 ILE B 432     2107   2074   1719    452    275   -375       C  
-ATOM   3843  CG2 ILE B 432      47.838  19.342 -16.983  1.00 14.62           C  
-ANISOU 3843  CG2 ILE B 432     1654   1841   2060    150   -405    174       C  
-ATOM   3844  CD1 ILE B 432      49.273  19.732 -19.715  1.00 17.73           C  
-ANISOU 3844  CD1 ILE B 432     2033   2279   2425    416    493   -239       C  
-ATOM   3845  N   VAL B 433      44.838  19.600 -15.932  1.00 12.24           N  
-ANISOU 3845  N   VAL B 433     1700   1785   1166    159     61    196       N  
-ATOM   3846  CA  VAL B 433      44.430  19.889 -14.564  1.00 14.01           C  
-ANISOU 3846  CA  VAL B 433     1671   1997   1653   -215   -109    -48       C  
-ATOM   3847  C   VAL B 433      45.619  19.741 -13.623  1.00 11.77           C  
-ANISOU 3847  C   VAL B 433     1643   1711   1117    227     29   -199       C  
-ATOM   3848  O   VAL B 433      46.323  18.734 -13.652  1.00 14.02           O  
-ANISOU 3848  O   VAL B 433     1974   1611   1743    553   -169    -29       O  
-ATOM   3849  CB  VAL B 433      43.311  18.940 -14.084  1.00 16.04           C  
-ANISOU 3849  CB  VAL B 433     1843   2608   1643   -346    117     80       C  
-ATOM   3850  CG1 VAL B 433      42.982  19.203 -12.612  1.00 17.86           C  
-ANISOU 3850  CG1 VAL B 433     1960   2950   1877   -342     87    -51       C  
-ATOM   3851  CG2 VAL B 433      42.073  19.077 -14.963  1.00 17.79           C  
-ANISOU 3851  CG2 VAL B 433     1735   3080   1945   -391   -185     25       C  
-ATOM   3852  N   TYR B 434      45.843  20.755 -12.798  1.00 10.95           N  
-ANISOU 3852  N   TYR B 434     1571   1433   1154    329   -182     34       N  
-ATOM   3853  CA  TYR B 434      46.867  20.696 -11.769  1.00 11.20           C  
-ANISOU 3853  CA  TYR B 434     1590   1117   1549    296    -22    168       C  
-ATOM   3854  C   TYR B 434      46.222  20.613 -10.399  1.00 10.50           C  
-ANISOU 3854  C   TYR B 434     1462   1222   1304    437     44    165       C  
-ATOM   3855  O   TYR B 434      45.278  21.335 -10.100  1.00 12.91           O  
-ANISOU 3855  O   TYR B 434     1612   1637   1655    928     -8    115       O  
-ATOM   3856  CB  TYR B 434      47.785  21.924 -11.840  1.00 11.92           C  
-ANISOU 3856  CB  TYR B 434     1650   1155   1725    221    183    175       C  
-ATOM   3857  CG  TYR B 434      48.503  22.024 -13.159  1.00 10.58           C  
-ANISOU 3857  CG  TYR B 434     1627   1136   1255    326     87     77       C  
-ATOM   3858  CD1 TYR B 434      49.679  21.317 -13.383  1.00 14.16           C  
-ANISOU 3858  CD1 TYR B 434     1777   1566   2037    539    383    -10       C  
-ATOM   3859  CD2 TYR B 434      48.000  22.812 -14.194  1.00 12.18           C  
-ANISOU 3859  CD2 TYR B 434     1925   1141   1561    428   -144     99       C  
-ATOM   3860  CE1 TYR B 434      50.334  21.383 -14.590  1.00 15.19           C  
-ANISOU 3860  CE1 TYR B 434     2079   1869   1823    576    457    428       C  
-ATOM   3861  CE2 TYR B 434      48.652  22.879 -15.417  1.00 12.70           C  
-ANISOU 3861  CE2 TYR B 434     1939   1277   1608    438    156     75       C  
-ATOM   3862  CZ  TYR B 434      49.819  22.165 -15.603  1.00 14.44           C  
-ANISOU 3862  CZ  TYR B 434     2104   1749   1631    749    432    558       C  
-ATOM   3863  OH  TYR B 434      50.478  22.222 -16.804  1.00 17.84           O  
-ANISOU 3863  OH  TYR B 434     2432   2173   2173    947    661    982       O  
-ATOM   3864  N   PHE B 435      46.750  19.726  -9.570  1.00  9.91           N  
-ANISOU 3864  N   PHE B 435     1417   1119   1227    294   -196    181       N  
-ATOM   3865  CA  PHE B 435      46.363  19.618  -8.183  1.00  9.66           C  
-ANISOU 3865  CA  PHE B 435     1465   1057   1147    445   -109    130       C  
-ATOM   3866  C   PHE B 435      47.314  20.479  -7.367  1.00  9.84           C  
-ANISOU 3866  C   PHE B 435     1507    980   1252    361   -115   -275       C  
-ATOM   3867  O   PHE B 435      48.535  20.395  -7.524  1.00 11.15           O  
-ANISOU 3867  O   PHE B 435     1396   1222   1618    426    262    -51       O  
-ATOM   3868  CB  PHE B 435      46.408  18.144  -7.778  1.00 10.69           C  
-ANISOU 3868  CB  PHE B 435     1307   1096   1657    300    -41     22       C  
-ATOM   3869  CG  PHE B 435      45.566  17.282  -8.670  1.00  9.99           C  
-ANISOU 3869  CG  PHE B 435     1159   1114   1523    232   -177   -224       C  
-ATOM   3870  CD1 PHE B 435      44.214  17.131  -8.423  1.00 12.55           C  
-ANISOU 3870  CD1 PHE B 435     1164   1592   2010      7   -237     91       C  
-ATOM   3871  CD2 PHE B 435      46.117  16.677  -9.799  1.00 11.71           C  
-ANISOU 3871  CD2 PHE B 435     1672    864   1912    284   -225   -229       C  
-ATOM   3872  CE1 PHE B 435      43.426  16.374  -9.266  1.00 13.54           C  
-ANISOU 3872  CE1 PHE B 435     1444   1587   2112    -32   -537   -118       C  
-ATOM   3873  CE2 PHE B 435      45.336  15.914 -10.645  1.00 13.39           C  
-ANISOU 3873  CE2 PHE B 435     1576   1297   2215    147   -287   -115       C  
-ATOM   3874  CZ  PHE B 435      43.987  15.764 -10.380  1.00 14.81           C  
-ANISOU 3874  CZ  PHE B 435     1808   1802   2017    388   -343   -244       C  
-ATOM   3875  N   THR B 436      46.758  21.333  -6.517  1.00 10.04           N  
-ANISOU 3875  N   THR B 436     1561   1029   1223    149   -148    -79       N  
-ATOM   3876  CA  THR B 436      47.565  22.334  -5.829  1.00 11.10           C  
-ANISOU 3876  CA  THR B 436     1726   1036   1454    365   -215    -11       C  
-ATOM   3877  C   THR B 436      47.580  22.129  -4.327  1.00  9.62           C  
-ANISOU 3877  C   THR B 436     1249   1063   1344    318     75     -9       C  
-ATOM   3878  O   THR B 436      46.625  21.588  -3.753  1.00 11.25           O  
-ANISOU 3878  O   THR B 436     1268   1557   1450    213     91    -97       O  
-ATOM   3879  CB  THR B 436      47.091  23.769  -6.140  1.00 13.56           C  
-ANISOU 3879  CB  THR B 436     1992   1371   1787    517   -412    193       C  
-ATOM   3880  OG1 THR B 436      45.757  23.958  -5.651  1.00 17.17           O  
-ANISOU 3880  OG1 THR B 436     2034   1743   2748    731   -804   -364       O  
-ATOM   3881  CG2 THR B 436      47.120  24.009  -7.643  1.00 15.96           C  
-ANISOU 3881  CG2 THR B 436     2576   1504   1982    442   -404    483       C  
-ATOM   3882  N   SER B 437      48.667  22.580  -3.702  1.00 10.18           N  
-ANISOU 3882  N   SER B 437     1332   1070   1467    175   -177     47       N  
-ATOM   3883  CA  SER B 437      48.775  22.648  -2.250  1.00  8.92           C  
-ANISOU 3883  CA  SER B 437     1314    982   1092    302   -217    -33       C  
-ATOM   3884  C   SER B 437      49.366  23.993  -1.856  1.00  9.85           C  
-ANISOU 3884  C   SER B 437     1392   1084   1266    273    209     24       C  
-ATOM   3885  O   SER B 437      50.331  24.468  -2.458  1.00 12.12           O  
-ANISOU 3885  O   SER B 437     1773   1210   1622    132    495    -84       O  
-ATOM   3886  CB  SER B 437      49.703  21.550  -1.717  1.00 10.49           C  
-ANISOU 3886  CB  SER B 437     1310    986   1689    605   -178    -30       C  
-ATOM   3887  OG  SER B 437      49.206  20.265  -2.032  1.00 11.03           O  
-ANISOU 3887  OG  SER B 437     1433    978   1780    368   -182   -256       O  
-ATOM   3888  N   THR B 438      48.808  24.596  -0.819  1.00 10.67           N  
-ANISOU 3888  N   THR B 438     1310   1246   1497    317    -29   -346       N  
-ATOM   3889  CA  THR B 438      49.451  25.739  -0.207  1.00 10.70           C  
-ANISOU 3889  CA  THR B 438     1351   1180   1533    297    -52   -327       C  
-ATOM   3890  C   THR B 438      50.717  25.255   0.506  1.00 10.71           C  
-ANISOU 3890  C   THR B 438     1334   1177   1557    122      4    -60       C  
-ATOM   3891  O   THR B 438      50.684  24.294   1.280  1.00 11.94           O  
-ANISOU 3891  O   THR B 438     1474   1135   1927    101    -19    -80       O  
-ATOM   3892  CB  THR B 438      48.500  26.451   0.758  1.00 12.25           C  
-ANISOU 3892  CB  THR B 438     1572   1351   1729    504   -151   -545       C  
-ATOM   3893  OG1 THR B 438      47.345  26.875   0.029  1.00 15.04           O  
-ANISOU 3893  OG1 THR B 438     1623   2039   2051    791   -359   -379       O  
-ATOM   3894  CG2 THR B 438      49.179  27.655   1.391  1.00 13.29           C  
-ANISOU 3894  CG2 THR B 438     1845   1130   2073    330   -116   -445       C  
-ATOM   3895  N   PHE B 439      51.835  25.919   0.233  1.00 10.98           N  
-ANISOU 3895  N   PHE B 439     1147   1375   1649    290     19   -168       N  
-ATOM   3896  CA  PHE B 439      53.136  25.466   0.704  1.00 10.02           C  
-ANISOU 3896  CA  PHE B 439     1063   1043   1702    256   -129   -259       C  
-ATOM   3897  C   PHE B 439      54.054  26.677   0.701  1.00 10.54           C  
-ANISOU 3897  C   PHE B 439     1241   1091   1673     54   -107   -337       C  
-ATOM   3898  O   PHE B 439      53.850  27.595  -0.090  1.00 12.10           O  
-ANISOU 3898  O   PHE B 439     1395   1298   1902     59    -64    121       O  
-ATOM   3899  CB  PHE B 439      53.661  24.385  -0.256  1.00 11.57           C  
-ANISOU 3899  CB  PHE B 439     1485   1125   1785    430     15   -348       C  
-ATOM   3900  CG  PHE B 439      55.010  23.828   0.117  1.00 11.01           C  
-ANISOU 3900  CG  PHE B 439     1440    950   1792    426    154     24       C  
-ATOM   3901  CD1 PHE B 439      55.115  22.726   0.957  1.00 11.56           C  
-ANISOU 3901  CD1 PHE B 439     1534    938   1920    391   -131   -103       C  
-ATOM   3902  CD2 PHE B 439      56.174  24.393  -0.384  1.00 11.48           C  
-ANISOU 3902  CD2 PHE B 439     1449   1182   1732    450    472   -284       C  
-ATOM   3903  CE1 PHE B 439      56.355  22.215   1.300  1.00 13.01           C  
-ANISOU 3903  CE1 PHE B 439     1923   1126   1894    544     39     -9       C  
-ATOM   3904  CE2 PHE B 439      57.410  23.889  -0.034  1.00 13.40           C  
-ANISOU 3904  CE2 PHE B 439     1634   1050   2408    476     62   -110       C  
-ATOM   3905  CZ  PHE B 439      57.501  22.799   0.804  1.00 13.67           C  
-ANISOU 3905  CZ  PHE B 439     1760   1174   2261    376     32   -305       C  
-ATOM   3906  N   PRO B 440      55.064  26.693   1.582  1.00  9.85           N  
-ANISOU 3906  N   PRO B 440     1198    913   1631     44      3    -45       N  
-ATOM   3907  CA  PRO B 440      55.972  27.843   1.649  1.00 10.25           C  
-ANISOU 3907  CA  PRO B 440     1267   1011   1614   -106     36     22       C  
-ATOM   3908  C   PRO B 440      57.011  27.892   0.521  1.00 10.86           C  
-ANISOU 3908  C   PRO B 440     1224   1000   1901    169   -141    100       C  
-ATOM   3909  O   PRO B 440      58.223  27.911   0.767  1.00 10.79           O  
-ANISOU 3909  O   PRO B 440     1337    913   1850     91     26   -120       O  
-ATOM   3910  CB  PRO B 440      56.635  27.681   3.017  1.00 11.05           C  
-ANISOU 3910  CB  PRO B 440     1476   1108   1612    227    -55     -9       C  
-ATOM   3911  CG  PRO B 440      56.637  26.183   3.232  1.00 11.61           C  
-ANISOU 3911  CG  PRO B 440     1679    848   1882    407   -228    113       C  
-ATOM   3912  CD  PRO B 440      55.292  25.751   2.695  1.00 10.43           C  
-ANISOU 3912  CD  PRO B 440     1386   1199   1379    250   -364    391       C  
-ATOM   3913  N   THR B 441      56.521  27.895  -0.715  1.00 10.53           N  
-ANISOU 3913  N   THR B 441     1445    867   1689     97    168    108       N  
-ATOM   3914  CA  THR B 441      57.299  28.370  -1.852  1.00 11.22           C  
-ANISOU 3914  CA  THR B 441     1634    758   1869    180    -83    -30       C  
-ATOM   3915  C   THR B 441      57.117  29.885  -1.834  1.00 11.74           C  
-ANISOU 3915  C   THR B 441     1663    898   1898    308   -128    164       C  
-ATOM   3916  O   THR B 441      56.158  30.431  -2.385  1.00 11.72           O  
-ANISOU 3916  O   THR B 441     1646    764   2041    254     32     70       O  
-ATOM   3917  CB  THR B 441      56.819  27.742  -3.182  1.00 10.93           C  
-ANISOU 3917  CB  THR B 441     1282    819   2050    154    -49     53       C  
-ATOM   3918  OG1 THR B 441      55.413  27.472  -3.103  1.00 11.95           O  
-ANISOU 3918  OG1 THR B 441     1248   1232   2060    138     -9   -154       O  
-ATOM   3919  CG2 THR B 441      57.559  26.426  -3.459  1.00 12.23           C  
-ANISOU 3919  CG2 THR B 441     1832    960   1854    409    -19     81       C  
-ATOM   3920  N   VAL B 442      58.019  30.562  -1.140  1.00 11.24           N  
-ANISOU 3920  N   VAL B 442     1648    794   1827     51      8     83       N  
-ATOM   3921  CA  VAL B 442      57.825  31.976  -0.831  1.00 12.92           C  
-ANISOU 3921  CA  VAL B 442     1996    685   2229    145     59    -86       C  
-ATOM   3922  C   VAL B 442      57.879  32.823  -2.098  1.00 13.18           C  
-ANISOU 3922  C   VAL B 442     2130    808   2069    228     86     84       C  
-ATOM   3923  O   VAL B 442      58.805  32.688  -2.902  1.00 14.91           O  
-ANISOU 3923  O   VAL B 442     2275   1038   2350    255    311    222       O  
-ATOM   3924  CB  VAL B 442      58.841  32.452   0.225  1.00 13.43           C  
-ANISOU 3924  CB  VAL B 442     2088    679   2335   -184     40     42       C  
-ATOM   3925  CG1 VAL B 442      58.736  33.959   0.454  1.00 13.45           C  
-ANISOU 3925  CG1 VAL B 442     2204    618   2286     41     26    -53       C  
-ATOM   3926  CG2 VAL B 442      58.611  31.701   1.534  1.00 13.98           C  
-ANISOU 3926  CG2 VAL B 442     1996    964   2352    -98    149    107       C  
-ATOM   3927  N   SER B 443      56.863  33.678  -2.251  1.00 13.14           N  
-ANISOU 3927  N   SER B 443     2139    735   2117    252    -80    226       N  
-ATOM   3928  CA  SER B 443      56.596  34.521  -3.436  1.00 14.57           C  
-ANISOU 3928  CA  SER B 443     2121   1046   2368    146    221    233       C  
-ATOM   3929  C   SER B 443      55.675  33.820  -4.435  1.00 14.56           C  
-ANISOU 3929  C   SER B 443     2220   1011   2302    254    116    134       C  
-ATOM   3930  O   SER B 443      55.222  34.422  -5.417  1.00 17.16           O  
-ANISOU 3930  O   SER B 443     2581   1290   2650    500    -90    388       O  
-ATOM   3931  CB  SER B 443      57.869  35.057  -4.126  1.00 15.27           C  
-ANISOU 3931  CB  SER B 443     2278   1118   2404    265    324    511       C  
-ATOM   3932  OG  SER B 443      58.462  34.097  -4.990  1.00 16.63           O  
-ANISOU 3932  OG  SER B 443     2563   1214   2542    386    579     62       O  
-ATOM   3933  N   ASN B 444      55.376  32.550  -4.172  1.00 14.60           N  
-ANISOU 3933  N   ASN B 444     2078   1383   2086    172     82     62       N  
-ATOM   3934  CA  ASN B 444      54.497  31.787  -5.042  1.00 13.90           C  
-ANISOU 3934  CA  ASN B 444     2205   1435   1642    367    222    265       C  
-ATOM   3935  C   ASN B 444      53.993  30.542  -4.306  1.00 12.41           C  
-ANISOU 3935  C   ASN B 444     1981   1243   1491    284    -54    103       C  
-ATOM   3936  O   ASN B 444      54.332  29.414  -4.677  1.00 13.17           O  
-ANISOU 3936  O   ASN B 444     1948   1263   1792    293    -11    -10       O  
-ATOM   3937  CB  ASN B 444      55.265  31.412  -6.308  1.00 16.16           C  
-ANISOU 3937  CB  ASN B 444     2598   1579   1962    300    113    278       C  
-ATOM   3938  CG  ASN B 444      54.386  30.849  -7.385  1.00 17.88           C  
-ANISOU 3938  CG  ASN B 444     2935   1673   2185    390    -59    129       C  
-ATOM   3939  OD1 ASN B 444      53.161  30.793  -7.250  1.00 19.24           O  
-ANISOU 3939  OD1 ASN B 444     3024   1961   2325    277   -423     54       O  
-ATOM   3940  ND2 ASN B 444      55.007  30.442  -8.485  1.00 19.38           N  
-ANISOU 3940  ND2 ASN B 444     3221   1721   2421    385   -135    -88       N  
-ATOM   3941  N   PRO B 445      53.184  30.751  -3.250  1.00 12.55           N  
-ANISOU 3941  N   PRO B 445     1928   1183   1657    494     76     72       N  
-ATOM   3942  CA  PRO B 445      52.921  29.700  -2.254  1.00 12.02           C  
-ANISOU 3942  CA  PRO B 445     1911   1132   1525    277    104    118       C  
-ATOM   3943  C   PRO B 445      51.813  28.721  -2.631  1.00 12.68           C  
-ANISOU 3943  C   PRO B 445     1924   1210   1685    226    -18    354       C  
-ATOM   3944  O   PRO B 445      50.976  28.363  -1.794  1.00 15.31           O  
-ANISOU 3944  O   PRO B 445     2288   1526   2004    269    108    368       O  
-ATOM   3945  CB  PRO B 445      52.526  30.502  -1.012  1.00 13.70           C  
-ANISOU 3945  CB  PRO B 445     2077   1295   1833    659    -14   -135       C  
-ATOM   3946  CG  PRO B 445      51.865  31.737  -1.573  1.00 14.42           C  
-ANISOU 3946  CG  PRO B 445     2103   1319   2057    794    -50    192       C  
-ATOM   3947  CD  PRO B 445      52.632  32.057  -2.837  1.00 13.80           C  
-ANISOU 3947  CD  PRO B 445     2044   1304   1896    524    466    196       C  
-ATOM   3948  N   LYS B 446      51.819  28.286  -3.883  1.00 12.25           N  
-ANISOU 3948  N   LYS B 446     1930    991   1733    156    -13    -39       N  
-ATOM   3949  CA  LYS B 446      50.855  27.313  -4.374  1.00 13.39           C  
-ANISOU 3949  CA  LYS B 446     2005   1220   1860    436    203     94       C  
-ATOM   3950  C   LYS B 446      51.574  26.359  -5.310  1.00 12.53           C  
-ANISOU 3950  C   LYS B 446     1799   1013   1949    229    319    -58       C  
-ATOM   3951  O   LYS B 446      51.963  26.738  -6.418  1.00 13.92           O  
-ANISOU 3951  O   LYS B 446     2141   1070   2079    393    476     28       O  
-ATOM   3952  CB  LYS B 446      49.703  28.001  -5.114  1.00 15.78           C  
-ANISOU 3952  CB  LYS B 446     2207   1809   1980    403    453   -239       C  
-ATOM   3953  CG  LYS B 446      48.661  27.016  -5.603  1.00 19.66           C  
-ANISOU 3953  CG  LYS B 446     2476   2169   2825    173    106   -543       C  
-ATOM   3954  CD  LYS B 446      47.339  27.679  -5.929  1.00 26.31           C  
-ANISOU 3954  CD  LYS B 446     2995   2995   4006    594   -146   -808       C  
-ATOM   3955  CE  LYS B 446      47.397  28.435  -7.236  1.00 30.85           C  
-ANISOU 3955  CE  LYS B 446     3316   3588   4815   1078   -144   -944       C  
-ATOM   3956  NZ  LYS B 446      46.062  29.003  -7.569  1.00 35.21           N  
-ANISOU 3956  NZ  LYS B 446     3548   4139   5690   1194   -607   -725       N  
-ATOM   3957  N   VAL B 447      51.765  25.123  -4.857  1.00 11.13           N  
-ANISOU 3957  N   VAL B 447     1397    969   1864    208    302     26       N  
-ATOM   3958  CA  VAL B 447      52.550  24.152  -5.621  1.00 10.70           C  
-ANISOU 3958  CA  VAL B 447     1225   1032   1809    365     -4   -177       C  
-ATOM   3959  C   VAL B 447      51.640  23.293  -6.493  1.00 10.00           C  
-ANISOU 3959  C   VAL B 447     1220    939   1640    167    137    251       C  
-ATOM   3960  O   VAL B 447      50.771  22.596  -5.979  1.00  9.45           O  
-ANISOU 3960  O   VAL B 447     1167    958   1464    194     88     98       O  
-ATOM   3961  CB  VAL B 447      53.369  23.228  -4.696  1.00 10.26           C  
-ANISOU 3961  CB  VAL B 447     1174   1008   1717    220     70     47       C  
-ATOM   3962  CG1 VAL B 447      53.988  22.082  -5.500  1.00 10.81           C  
-ANISOU 3962  CG1 VAL B 447     1256   1070   1779    476     84   -190       C  
-ATOM   3963  CG2 VAL B 447      54.439  24.023  -3.950  1.00 12.25           C  
-ANISOU 3963  CG2 VAL B 447     1418   1201   2034    -69   -490    -85       C  
-ATOM   3964  N   PRO B 448      51.819  23.360  -7.819  1.00 10.91           N  
-ANISOU 3964  N   PRO B 448     1364   1063   1719     56     65     57       N  
-ATOM   3965  CA  PRO B 448      51.021  22.540  -8.737  1.00 10.66           C  
-ANISOU 3965  CA  PRO B 448     1560   1033   1457    291     76    109       C  
-ATOM   3966  C   PRO B 448      51.671  21.188  -9.020  1.00  9.85           C  
-ANISOU 3966  C   PRO B 448     1247    898   1596    136    -81    -94       C  
-ATOM   3967  O   PRO B 448      52.899  21.101  -9.090  1.00 10.88           O  
-ANISOU 3967  O   PRO B 448     1219   1145   1770     95     -1    -48       O  
-ATOM   3968  CB  PRO B 448      51.016  23.384 -10.006  1.00 11.35           C  
-ANISOU 3968  CB  PRO B 448     1659   1198   1453     46     61    258       C  
-ATOM   3969  CG  PRO B 448      52.389  24.025 -10.000  1.00 12.47           C  
-ANISOU 3969  CG  PRO B 448     1664   1249   1823    115    164     74       C  
-ATOM   3970  CD  PRO B 448      52.743  24.254  -8.542  1.00 11.39           C  
-ANISOU 3970  CD  PRO B 448     1811   1178   1338     63    310     92       C  
-ATOM   3971  N   CYS B 449      50.858  20.148  -9.158  1.00  9.77           N  
-ANISOU 3971  N   CYS B 449     1257    864   1591    431     71    -92       N  
-ATOM   3972  CA  CYS B 449      51.359  18.842  -9.606  1.00 10.13           C  
-ANISOU 3972  CA  CYS B 449     1359    824   1666    304    -43    101       C  
-ATOM   3973  C   CYS B 449      50.359  18.215 -10.574  1.00  9.62           C  
-ANISOU 3973  C   CYS B 449     1252   1112   1289    -15    141   -118       C  
-ATOM   3974  O   CYS B 449      49.209  18.647 -10.648  1.00 11.15           O  
-ANISOU 3974  O   CYS B 449     1310   1276   1651    442    111     34       O  
-ATOM   3975  CB  CYS B 449      51.633  17.913  -8.412  1.00 10.60           C  
-ANISOU 3975  CB  CYS B 449     1262   1051   1714    261    159    312       C  
-ATOM   3976  SG  CYS B 449      50.174  17.283  -7.563  1.00 10.40           S  
-ANISOU 3976  SG  CYS B 449     1263   1155   1534    225    -68     86       S  
-ATOM   3977  N   THR B 450      50.782  17.198 -11.318  1.00  9.27           N  
-ANISOU 3977  N   THR B 450     1543    932   1045    242    127   -137       N  
-ATOM   3978  CA  THR B 450      49.897  16.613 -12.323  1.00 10.48           C  
-ANISOU 3978  CA  THR B 450     1581   1271   1131    201     65   -133       C  
-ATOM   3979  C   THR B 450      49.117  15.366 -11.865  1.00  9.61           C  
-ANISOU 3979  C   THR B 450     1479   1019   1151    212    -18    -11       C  
-ATOM   3980  O   THR B 450      48.191  14.931 -12.544  1.00 11.89           O  
-ANISOU 3980  O   THR B 450     1810   1208   1500     43   -492     28       O  
-ATOM   3981  CB  THR B 450      50.617  16.390 -13.681  1.00 11.68           C  
-ANISOU 3981  CB  THR B 450     1481   1389   1566    379     -3   -150       C  
-ATOM   3982  OG1 THR B 450      51.932  15.872 -13.452  1.00 12.34           O  
-ANISOU 3982  OG1 THR B 450     1412   1638   1637    448     54   -358       O  
-ATOM   3983  CG2 THR B 450      50.750  17.718 -14.431  1.00 13.61           C  
-ANISOU 3983  CG2 THR B 450     1585   1503   2084    426    235    408       C  
-ATOM   3984  N   LEU B 451      49.467  14.817 -10.702  1.00 10.19           N  
-ANISOU 3984  N   LEU B 451     1377   1147   1347    -13     94    164       N  
-ATOM   3985  CA  LEU B 451      48.698  13.720 -10.096  1.00 10.05           C  
-ANISOU 3985  CA  LEU B 451     1499    928   1390    191    158    178       C  
-ATOM   3986  C   LEU B 451      48.834  13.739  -8.590  1.00 10.42           C  
-ANISOU 3986  C   LEU B 451     1411   1092   1454     66    -51    195       C  
-ATOM   3987  O   LEU B 451      49.916  13.987  -8.074  1.00 11.18           O  
-ANISOU 3987  O   LEU B 451     1318   1260   1670     45   -173     89       O  
-ATOM   3988  CB  LEU B 451      49.212  12.349 -10.558  1.00 12.33           C  
-ANISOU 3988  CB  LEU B 451     1622   1181   1881    227    -60   -148       C  
-ATOM   3989  CG  LEU B 451      48.824  11.781 -11.918  1.00 15.58           C  
-ANISOU 3989  CG  LEU B 451     1909   1491   2519    407   -683   -452       C  
-ATOM   3990  CD1 LEU B 451      49.479  10.406 -12.092  1.00 17.85           C  
-ANISOU 3990  CD1 LEU B 451     2122   1441   3218    596   -620   -678       C  
-ATOM   3991  CD2 LEU B 451      47.305  11.694 -12.077  1.00 14.97           C  
-ANISOU 3991  CD2 LEU B 451     1688   1727   2273    -42   -767   -243       C  
-ATOM   3992  N   PRO B 452      47.749  13.418  -7.876  1.00 10.31           N  
-ANISOU 3992  N   PRO B 452     1143   1288   1486     76   -182    148       N  
-ATOM   3993  CA  PRO B 452      47.900  13.192  -6.433  1.00 11.46           C  
-ANISOU 3993  CA  PRO B 452     1127   1676   1552    386   -219    646       C  
-ATOM   3994  C   PRO B 452      48.798  11.983  -6.179  1.00  9.16           C  
-ANISOU 3994  C   PRO B 452      950   1188   1340    102    -86    336       C  
-ATOM   3995  O   PRO B 452      48.785  11.031  -6.964  1.00 10.06           O  
-ANISOU 3995  O   PRO B 452     1130   1084   1608     84    -22     25       O  
-ATOM   3996  CB  PRO B 452      46.471  12.881  -5.968  1.00 12.98           C  
-ANISOU 3996  CB  PRO B 452     1130   1939   1862    603    -21    425       C  
-ATOM   3997  CG  PRO B 452      45.578  13.434  -7.075  1.00 13.28           C  
-ANISOU 3997  CG  PRO B 452     1272   2088   1685    636     76    683       C  
-ATOM   3998  CD  PRO B 452      46.361  13.225  -8.333  1.00 11.97           C  
-ANISOU 3998  CD  PRO B 452      952   2087   1509    324    218    232       C  
-ATOM   3999  N   GLN B 453      49.556  12.014  -5.094  1.00  9.02           N  
-ANISOU 3999  N   GLN B 453      818   1165   1445    204    -99    227       N  
-ATOM   4000  CA  GLN B 453      50.495  10.932  -4.835  1.00  8.62           C  
-ANISOU 4000  CA  GLN B 453      791    965   1517    164   -283     85       C  
-ATOM   4001  C   GLN B 453      49.783   9.585  -4.729  1.00  9.12           C  
-ANISOU 4001  C   GLN B 453      856   1062   1546     20   -155     64       C  
-ATOM   4002  O   GLN B 453      50.291   8.570  -5.201  1.00 10.44           O  
-ANISOU 4002  O   GLN B 453     1295    997   1673    194   -164   -141       O  
-ATOM   4003  CB  GLN B 453      51.328  11.191  -3.577  1.00  8.72           C  
-ANISOU 4003  CB  GLN B 453      962   1073   1276    297   -115    106       C  
-ATOM   4004  CG  GLN B 453      52.358  10.094  -3.315  1.00  9.53           C  
-ANISOU 4004  CG  GLN B 453      973   1189   1460    317   -160    145       C  
-ATOM   4005  CD  GLN B 453      53.383   9.994  -4.430  1.00 10.46           C  
-ANISOU 4005  CD  GLN B 453     1193   1197   1585    211     95     51       C  
-ATOM   4006  OE1 GLN B 453      53.679  10.984  -5.100  1.00 11.05           O  
-ANISOU 4006  OE1 GLN B 453     1154   1286   1756    131      2    168       O  
-ATOM   4007  NE2 GLN B 453      53.935   8.797  -4.632  1.00 11.53           N  
-ANISOU 4007  NE2 GLN B 453     1418   1084   1878    310   -275      3       N  
-ATOM   4008  N   GLU B 454      48.612   9.572  -4.101  1.00  9.87           N  
-ANISOU 4008  N   GLU B 454     1080    998   1672   -128   -196    265       N  
-ATOM   4009  CA  GLU B 454      47.905   8.314  -3.892  1.00  9.42           C  
-ANISOU 4009  CA  GLU B 454     1250   1351    979    -48     56    155       C  
-ATOM   4010  C   GLU B 454      47.379   7.703  -5.199  1.00  9.39           C  
-ANISOU 4010  C   GLU B 454     1312   1142   1114      6   -136     45       C  
-ATOM   4011  O   GLU B 454      47.155   6.501  -5.265  1.00 11.38           O  
-ANISOU 4011  O   GLU B 454     1327   1100   1895   -148   -175   -108       O  
-ATOM   4012  CB  GLU B 454      46.814   8.447  -2.823  1.00 10.83           C  
-ANISOU 4012  CB  GLU B 454     1452   1380   1282   -313     22   -103       C  
-ATOM   4013  CG  GLU B 454      47.357   8.556  -1.382  1.00 11.78           C  
-ANISOU 4013  CG  GLU B 454     1769   1166   1539   -336    -55   -181       C  
-ATOM   4014  CD  GLU B 454      47.913   9.943  -1.026  1.00 10.83           C  
-ANISOU 4014  CD  GLU B 454     1376   1411   1328   -204   -134    -90       C  
-ATOM   4015  OE1 GLU B 454      47.753  10.897  -1.813  1.00 11.17           O  
-ANISOU 4015  OE1 GLU B 454     1541   1262   1442    -72    -65     46       O  
-ATOM   4016  OE2 GLU B 454      48.507  10.082   0.062  1.00 12.13           O  
-ANISOU 4016  OE2 GLU B 454     1686   1320   1603     97    -84   -222       O  
-ATOM   4017  N   PHE B 455      47.209   8.512  -6.240  1.00 10.60           N  
-ANISOU 4017  N   PHE B 455     1395   1447   1184    163   -235    109       N  
-ATOM   4018  CA  PHE B 455      46.944   7.962  -7.568  1.00 10.95           C  
-ANISOU 4018  CA  PHE B 455     1363   1453   1345    177   -221    188       C  
-ATOM   4019  C   PHE B 455      48.154   7.151  -8.026  1.00 10.64           C  
-ANISOU 4019  C   PHE B 455     1166   1385   1491   -200   -417     16       C  
-ATOM   4020  O   PHE B 455      48.000   6.086  -8.625  1.00 11.62           O  
-ANISOU 4020  O   PHE B 455     1506   1123   1787   -281   -271    -95       O  
-ATOM   4021  CB  PHE B 455      46.701   9.068  -8.596  1.00 11.68           C  
-ANISOU 4021  CB  PHE B 455     1345   1553   1541     92   -184    324       C  
-ATOM   4022  CG  PHE B 455      45.262   9.500  -8.725  1.00 11.53           C  
-ANISOU 4022  CG  PHE B 455     1440   1487   1455    -94   -214     87       C  
-ATOM   4023  CD1 PHE B 455      44.553   9.965  -7.628  1.00 14.34           C  
-ANISOU 4023  CD1 PHE B 455     1312   2156   1980    119   -169    220       C  
-ATOM   4024  CD2 PHE B 455      44.637   9.492  -9.963  1.00 13.18           C  
-ANISOU 4024  CD2 PHE B 455     1446   1673   1888    -83   -510    189       C  
-ATOM   4025  CE1 PHE B 455      43.242  10.387  -7.759  1.00 15.55           C  
-ANISOU 4025  CE1 PHE B 455     1532   2302   2075    152   -371     43       C  
-ATOM   4026  CE2 PHE B 455      43.330   9.923 -10.104  1.00 14.86           C  
-ANISOU 4026  CE2 PHE B 455     1651   1746   2247    -33   -274    -21       C  
-ATOM   4027  CZ  PHE B 455      42.631  10.371  -9.004  1.00 15.06           C  
-ANISOU 4027  CZ  PHE B 455     1541   1968   2212     98   -220     75       C  
-ATOM   4028  N   VAL B 456      49.356   7.662  -7.763  1.00 11.56           N  
-ANISOU 4028  N   VAL B 456     1137   1716   1540   -101    113    -10       N  
-ATOM   4029  CA  VAL B 456      50.579   6.984  -8.181  1.00 11.92           C  
-ANISOU 4029  CA  VAL B 456     1158   1672   1697   -531     62   -174       C  
-ATOM   4030  C   VAL B 456      50.672   5.597  -7.553  1.00 10.73           C  
-ANISOU 4030  C   VAL B 456     1239   1490   1348   -229     70    -59       C  
-ATOM   4031  O   VAL B 456      50.870   4.600  -8.259  1.00 12.83           O  
-ANISOU 4031  O   VAL B 456     1585   1503   1787    -26     25   -499       O  
-ATOM   4032  CB  VAL B 456      51.852   7.783  -7.808  1.00 13.28           C  
-ANISOU 4032  CB  VAL B 456     1399   1726   1920   -394    176   -349       C  
-ATOM   4033  CG1 VAL B 456      53.109   6.993  -8.172  1.00 14.34           C  
-ANISOU 4033  CG1 VAL B 456     1254   1926   2267   -477    251   -444       C  
-ATOM   4034  CG2 VAL B 456      51.861   9.139  -8.505  1.00 14.10           C  
-ANISOU 4034  CG2 VAL B 456     1736   1671   1951   -338      7   -169       C  
-ATOM   4035  N   SER B 457      50.537   5.524  -6.230  1.00 11.54           N  
-ANISOU 4035  N   SER B 457     1337   1356   1692    -46   -125    -75       N  
-ATOM   4036  CA  SER B 457      50.646   4.233  -5.554  1.00 11.61           C  
-ANISOU 4036  CA  SER B 457     1340   1409   1661   -156   -253    -69       C  
-ATOM   4037  C   SER B 457      49.500   3.312  -5.960  1.00 12.60           C  
-ANISOU 4037  C   SER B 457     1348   1676   1761    155   -268    -83       C  
-ATOM   4038  O   SER B 457      49.674   2.104  -6.047  1.00 13.43           O  
-ANISOU 4038  O   SER B 457     1671   1485   1946    192   -358   -125       O  
-ATOM   4039  CB  SER B 457      50.712   4.384  -4.030  1.00 12.94           C  
-ANISOU 4039  CB  SER B 457     1533   1567   1815    -32   -365   -208       C  
-ATOM   4040  OG  SER B 457      49.660   5.190  -3.526  1.00 12.70           O  
-ANISOU 4040  OG  SER B 457     1460   1481   1882    294    -42      8       O  
-ATOM   4041  N   HIS B 458      48.329   3.888  -6.211  1.00 11.28           N  
-ANISOU 4041  N   HIS B 458     1266   1351   1670   -132    -77    -20       N  
-ATOM   4042  CA  HIS B 458      47.194   3.101  -6.669  1.00 11.27           C  
-ANISOU 4042  CA  HIS B 458     1281   1485   1517    -37   -123    -61       C  
-ATOM   4043  C   HIS B 458      47.519   2.412  -7.997  1.00 11.97           C  
-ANISOU 4043  C   HIS B 458     1611   1155   1783   -146   -362     16       C  
-ATOM   4044  O   HIS B 458      47.313   1.206  -8.148  1.00 13.37           O  
-ANISOU 4044  O   HIS B 458     1796   1221   2062   -200   -491   -232       O  
-ATOM   4045  CB  HIS B 458      45.951   3.987  -6.813  1.00 11.60           C  
-ANISOU 4045  CB  HIS B 458      961   1403   2043   -457   -381    318       C  
-ATOM   4046  CG  HIS B 458      44.695   3.226  -7.100  1.00 13.19           C  
-ANISOU 4046  CG  HIS B 458     1208   1577   2227   -648   -393    364       C  
-ATOM   4047  ND1 HIS B 458      44.001   2.544  -6.125  1.00 18.10           N  
-ANISOU 4047  ND1 HIS B 458     1600   2403   2875   -863   -482    892       N  
-ATOM   4048  CD2 HIS B 458      44.006   3.044  -8.252  1.00 14.65           C  
-ANISOU 4048  CD2 HIS B 458     1338   1873   2355   -459   -740    134       C  
-ATOM   4049  CE1 HIS B 458      42.936   1.976  -6.662  1.00 18.77           C  
-ANISOU 4049  CE1 HIS B 458     1740   2382   3008   -617   -624    692       C  
-ATOM   4050  NE2 HIS B 458      42.918   2.258  -7.952  1.00 15.76           N  
-ANISOU 4050  NE2 HIS B 458     1587   2018   2384   -415   -514    473       N  
-ATOM   4051  N   PHE B 459      48.036   3.166  -8.962  1.00 11.72           N  
-ANISOU 4051  N   PHE B 459     1582   1377   1494   -151   -230     -9       N  
-ATOM   4052  CA  PHE B 459      48.334   2.583 -10.274  1.00 12.52           C  
-ANISOU 4052  CA  PHE B 459     1795   1446   1517     -8   -290     21       C  
-ATOM   4053  C   PHE B 459      49.482   1.568 -10.190  1.00 13.22           C  
-ANISOU 4053  C   PHE B 459     1714   1380   1929   -228   -270   -149       C  
-ATOM   4054  O   PHE B 459      49.451   0.536 -10.856  1.00 14.77           O  
-ANISOU 4054  O   PHE B 459     2121   1382   2107   -109   -320   -492       O  
-ATOM   4055  CB  PHE B 459      48.655   3.670 -11.304  1.00 12.88           C  
-ANISOU 4055  CB  PHE B 459     1654   1476   1764   -270   -329     67       C  
-ATOM   4056  CG  PHE B 459      47.531   4.640 -11.545  1.00 12.40           C  
-ANISOU 4056  CG  PHE B 459     1683   1525   1504   -168   -264    135       C  
-ATOM   4057  CD1 PHE B 459      46.213   4.266 -11.331  1.00 13.81           C  
-ANISOU 4057  CD1 PHE B 459     1649   1648   1951   -230   -281     66       C  
-ATOM   4058  CD2 PHE B 459      47.797   5.931 -11.988  1.00 13.13           C  
-ANISOU 4058  CD2 PHE B 459     1941   1508   1540    -48   -286     19       C  
-ATOM   4059  CE1 PHE B 459      45.175   5.160 -11.559  1.00 14.16           C  
-ANISOU 4059  CE1 PHE B 459     1935   1366   2079   -159   -192     11       C  
-ATOM   4060  CE2 PHE B 459      46.772   6.832 -12.217  1.00 13.68           C  
-ANISOU 4060  CE2 PHE B 459     1796   1643   1758   -211    -82     11       C  
-ATOM   4061  CZ  PHE B 459      45.452   6.444 -12.001  1.00 14.67           C  
-ANISOU 4061  CZ  PHE B 459     1789   1817   1969   -410   -172    -69       C  
-ATOM   4062  N   VAL B 460      50.491   1.861  -9.373  1.00 13.09           N  
-ANISOU 4062  N   VAL B 460     1402   1594   1978   -174   -316   -165       N  
-ATOM   4063  CA  VAL B 460      51.587   0.922  -9.176  1.00 14.63           C  
-ANISOU 4063  CA  VAL B 460     1633   1602   2323    -91   -606   -165       C  
-ATOM   4064  C   VAL B 460      51.048  -0.376  -8.584  1.00 15.50           C  
-ANISOU 4064  C   VAL B 460     1993   1651   2243    114   -370   -175       C  
-ATOM   4065  O   VAL B 460      51.432  -1.471  -8.999  1.00 17.55           O  
-ANISOU 4065  O   VAL B 460     2361   1522   2786    126   -497   -428       O  
-ATOM   4066  CB  VAL B 460      52.689   1.500  -8.264  1.00 15.12           C  
-ANISOU 4066  CB  VAL B 460     1657   1320   2766     19   -677   -295       C  
-ATOM   4067  CG1 VAL B 460      53.687   0.411  -7.896  1.00 18.41           C  
-ANISOU 4067  CG1 VAL B 460     1864   1629   3500    393   -691   -110       C  
-ATOM   4068  CG2 VAL B 460      53.386   2.679  -8.951  1.00 15.52           C  
-ANISOU 4068  CG2 VAL B 460     1769   1636   2491    127   -313     40       C  
-ATOM   4069  N   ASN B 461      50.137  -0.250  -7.627  1.00 14.54           N  
-ANISOU 4069  N   ASN B 461     2051   1361   2113   -327   -490     68       N  
-ATOM   4070  CA  ASN B 461      49.529  -1.420  -7.002  1.00 14.50           C  
-ANISOU 4070  CA  ASN B 461     2071   1581   1855   -498   -468    203       C  
-ATOM   4071  C   ASN B 461      48.699  -2.259  -7.980  1.00 16.37           C  
-ANISOU 4071  C   ASN B 461     2325   1380   2514   -124   -743   -130       C  
-ATOM   4072  O   ASN B 461      48.809  -3.485  -8.013  1.00 18.54           O  
-ANISOU 4072  O   ASN B 461     2687   1371   2987    173   -991   -320       O  
-ATOM   4073  CB  ASN B 461      48.649  -0.998  -5.831  1.00 15.73           C  
-ANISOU 4073  CB  ASN B 461     2436   1629   1912   -472   -366    451       C  
-ATOM   4074  CG  ASN B 461      48.263  -2.165  -4.958  1.00 18.06           C  
-ANISOU 4074  CG  ASN B 461     2644   1827   2392   -555   -364    300       C  
-ATOM   4075  OD1 ASN B 461      49.030  -2.574  -4.092  1.00 19.77           O  
-ANISOU 4075  OD1 ASN B 461     2808   2093   2611   -476   -865    482       O  
-ATOM   4076  ND2 ASN B 461      47.080  -2.722  -5.190  1.00 20.31           N  
-ANISOU 4076  ND2 ASN B 461     2709   2180   2829   -509   -430    144       N  
-ATOM   4077  N   GLU B 462      47.870  -1.591  -8.778  1.00 15.22           N  
-ANISOU 4077  N   GLU B 462     2340   1092   2349   -274   -651    -33       N  
-ATOM   4078  CA  GLU B 462      46.916  -2.276  -9.642  1.00 16.51           C  
-ANISOU 4078  CA  GLU B 462     2374   1516   2382   -312   -969   -131       C  
-ATOM   4079  C   GLU B 462      47.544  -2.863 -10.900  1.00 16.88           C  
-ANISOU 4079  C   GLU B 462     2573   1633   2207   -184   -691   -143       C  
-ATOM   4080  O   GLU B 462      47.191  -3.969 -11.310  1.00 17.79           O  
-ANISOU 4080  O   GLU B 462     2957   1460   2340     85   -741   -250       O  
-ATOM   4081  CB  GLU B 462      45.792  -1.318 -10.037  1.00 17.08           C  
-ANISOU 4081  CB  GLU B 462     2465   1774   2250   -279   -993     -6       C  
-ATOM   4082  CG  GLU B 462      44.969  -0.834  -8.870  1.00 19.63           C  
-ANISOU 4082  CG  GLU B 462     2857   2043   2559   -420   -672    285       C  
-ATOM   4083  CD  GLU B 462      44.320  -1.978  -8.135  1.00 22.65           C  
-ANISOU 4083  CD  GLU B 462     3047   2615   2945   -490   -954    269       C  
-ATOM   4084  OE1 GLU B 462      43.304  -2.509  -8.631  1.00 23.97           O  
-ANISOU 4084  OE1 GLU B 462     3168   2456   3481   -636   -808    407       O  
-ATOM   4085  OE2 GLU B 462      44.841  -2.366  -7.072  1.00 25.26           O  
-ANISOU 4085  OE2 GLU B 462     3092   3128   3378   -602  -1037    719       O  
-ATOM   4086  N   GLN B 463      48.453  -2.120 -11.526  1.00 17.03           N  
-ANISOU 4086  N   GLN B 463     2671   1465   2333   -434   -700   -222       N  
-ATOM   4087  CA  GLN B 463      49.037  -2.558 -12.792  1.00 19.85           C  
-ANISOU 4087  CA  GLN B 463     2969   2165   2409   -200   -713   -715       C  
-ATOM   4088  C   GLN B 463      47.943  -2.942 -13.780  1.00 19.32           C  
-ANISOU 4088  C   GLN B 463     2998   1774   2569   -197   -770   -164       C  
-ATOM   4089  O   GLN B 463      48.059  -3.943 -14.485  1.00 20.94           O  
-ANISOU 4089  O   GLN B 463     3140   1954   2863    -46   -778   -625       O  
-ATOM   4090  CB  GLN B 463      49.960  -3.760 -12.570  1.00 22.57           C  
-ANISOU 4090  CB  GLN B 463     3178   2539   2858   -358   -832   -925       C  
-ATOM   4091  CG  GLN B 463      51.097  -3.512 -11.591  1.00 27.07           C  
-ANISOU 4091  CG  GLN B 463     3593   3209   3481   -228   -538   -898       C  
-ATOM   4092  CD  GLN B 463      52.269  -2.815 -12.238  1.00 29.91           C  
-ANISOU 4092  CD  GLN B 463     3918   3416   4028    -77   -392  -1014       C  
-ATOM   4093  OE1 GLN B 463      52.841  -3.312 -13.208  1.00 32.18           O  
-ANISOU 4093  OE1 GLN B 463     3995   3772   4459    -74   -345  -1345       O  
-ATOM   4094  NE2 GLN B 463      52.631  -1.652 -11.709  1.00 29.99           N  
-ANISOU 4094  NE2 GLN B 463     4048   3276   4070     84   -256   -379       N  
-ATOM   4095  N   ALA B 464      46.875  -2.152 -13.823  1.00 18.07           N  
-ANISOU 4095  N   ALA B 464     2878   1572   2415   -202  -1085     28       N  
-ATOM   4096  CA  ALA B 464      45.741  -2.449 -14.691  1.00 18.22           C  
-ANISOU 4096  CA  ALA B 464     3088   1591   2243   -159   -984   -166       C  
-ATOM   4097  C   ALA B 464      46.087  -2.147 -16.140  1.00 19.23           C  
-ANISOU 4097  C   ALA B 464     3394   1607   2303    -96   -978   -239       C  
-ATOM   4098  O   ALA B 464      46.540  -1.049 -16.449  1.00 19.11           O  
-ANISOU 4098  O   ALA B 464     3177   1712   2371   -391   -791   -209       O  
-ATOM   4099  CB  ALA B 464      44.521  -1.646 -14.261  1.00 19.38           C  
-ANISOU 4099  CB  ALA B 464     2993   1767   2603   -152   -879   -148       C  
-ATOM   4100  N   PRO B 465      45.879  -3.120 -17.039  1.00 20.43           N  
-ANISOU 4100  N   PRO B 465     3835   1458   2470    -46   -965   -307       N  
-ATOM   4101  CA  PRO B 465      46.165  -2.826 -18.446  1.00 20.71           C  
-ANISOU 4101  CA  PRO B 465     3807   1663   2399   -133  -1028   -626       C  
-ATOM   4102  C   PRO B 465      45.368  -1.627 -18.956  1.00 20.72           C  
-ANISOU 4102  C   PRO B 465     3597   1728   2547   -319   -948   -404       C  
-ATOM   4103  O   PRO B 465      44.184  -1.467 -18.635  1.00 21.58           O  
-ANISOU 4103  O   PRO B 465     3458   2048   2691   -274  -1035   -180       O  
-ATOM   4104  CB  PRO B 465      45.723  -4.103 -19.166  1.00 23.57           C  
-ANISOU 4104  CB  PRO B 465     4237   1935   2782    106  -1350   -763       C  
-ATOM   4105  CG  PRO B 465      45.865  -5.171 -18.140  1.00 24.51           C  
-ANISOU 4105  CG  PRO B 465     4402   1817   3092     96  -1018   -456       C  
-ATOM   4106  CD  PRO B 465      45.498  -4.529 -16.832  1.00 21.88           C  
-ANISOU 4106  CD  PRO B 465     4146   1598   2570    -41   -849   -686       C  
-ATOM   4107  N   THR B 466      46.029  -0.787 -19.744  1.00 20.47           N  
-ANISOU 4107  N   THR B 466     3470   1854   2454   -386   -897   -226       N  
-ATOM   4108  CA  THR B 466      45.390   0.385 -20.332  1.00 20.14           C  
-ANISOU 4108  CA  THR B 466     3260   2211   2181   -497  -1034   -202       C  
-ATOM   4109  C   THR B 466      44.646  -0.022 -21.604  1.00 21.70           C  
-ANISOU 4109  C   THR B 466     3579   2723   1942   -538  -1140   -248       C  
-ATOM   4110  O   THR B 466      45.263  -0.343 -22.621  1.00 25.93           O  
-ANISOU 4110  O   THR B 466     3771   3670   2412   -257   -867   -647       O  
-ATOM   4111  CB  THR B 466      46.436   1.468 -20.640  1.00 20.24           C  
-ANISOU 4111  CB  THR B 466     3025   2093   2571   -503   -875     11       C  
-ATOM   4112  OG1 THR B 466      47.172   1.755 -19.446  1.00 20.48           O  
-ANISOU 4112  OG1 THR B 466     2832   2155   2795   -396   -919   -353       O  
-ATOM   4113  CG2 THR B 466      45.770   2.753 -21.137  1.00 20.80           C  
-ANISOU 4113  CG2 THR B 466     2893   1929   3079   -633   -790    469       C  
-ATOM   4114  N   ARG B 467      43.317  -0.014 -21.540  1.00 23.56           N  
-ANISOU 4114  N   ARG B 467     3768   2888   2296   -326  -1373   -276       N  
-ATOM   4115  CA  ARG B 467      42.503  -0.605 -22.603  1.00 24.53           C  
-ANISOU 4115  CA  ARG B 467     3918   3033   2367   -646  -1499   -260       C  
-ATOM   4116  C   ARG B 467      41.875   0.411 -23.556  1.00 24.73           C  
-ANISOU 4116  C   ARG B 467     3951   2942   2504   -537  -1600   -176       C  
-ATOM   4117  O   ARG B 467      41.106   0.045 -24.446  1.00 28.94           O  
-ANISOU 4117  O   ARG B 467     4231   3431   3334   -534  -1816   -241       O  
-ATOM   4118  CB  ARG B 467      41.419  -1.510 -22.010  1.00 28.21           C  
-ANISOU 4118  CB  ARG B 467     4355   3478   2884   -985  -1682   -190       C  
-ATOM   4119  CG  ARG B 467      41.961  -2.644 -21.153  1.00 32.49           C  
-ANISOU 4119  CG  ARG B 467     4857   4077   3410   -930  -1980      2       C  
-ATOM   4120  CD  ARG B 467      40.881  -3.662 -20.820  1.00 40.46           C  
-ANISOU 4120  CD  ARG B 467     5494   4934   4944   -385  -1425    236       C  
-ATOM   4121  NE  ARG B 467      41.261  -4.521 -19.701  1.00 46.74           N  
-ANISOU 4121  NE  ARG B 467     6037   5655   6066    125   -934    242       N  
-ATOM   4122  CZ  ARG B 467      42.055  -5.583 -19.804  1.00 51.14           C  
-ANISOU 4122  CZ  ARG B 467     6397   6314   6719    545   -629    279       C  
-ATOM   4123  NH1 ARG B 467      42.565  -5.923 -20.981  1.00 53.17           N  
-ANISOU 4123  NH1 ARG B 467     6533   6570   7099    781   -425    295       N  
-ATOM   4124  NH2 ARG B 467      42.342  -6.303 -18.729  1.00 52.28           N  
-ANISOU 4124  NH2 ARG B 467     6529   6572   6763    675   -639    197       N  
-ATOM   4125  N   GLY B 468      42.203   1.682 -23.370  1.00 23.54           N  
-ANISOU 4125  N   GLY B 468     3696   2724   2523   -540  -1221    279       N  
-ATOM   4126  CA  GLY B 468      41.735   2.723 -24.268  1.00 22.83           C  
-ANISOU 4126  CA  GLY B 468     3585   2678   2409   -402  -1103     60       C  
-ATOM   4127  C   GLY B 468      42.736   3.857 -24.313  1.00 21.98           C  
-ANISOU 4127  C   GLY B 468     3497   2644   2210    -54  -1046      7       C  
-ATOM   4128  O   GLY B 468      43.719   3.857 -23.570  1.00 22.38           O  
-ANISOU 4128  O   GLY B 468     3374   2646   2484    -17   -920   -179       O  
-ATOM   4129  N   ASP B 469      42.493   4.833 -25.176  1.00 23.19           N  
-ANISOU 4129  N   ASP B 469     3587   2644   2580     77   -692     21       N  
-ATOM   4130  CA  ASP B 469      43.423   5.943 -25.317  1.00 24.05           C  
-ANISOU 4130  CA  ASP B 469     3768   2745   2625    313   -471    261       C  
-ATOM   4131  C   ASP B 469      43.211   7.010 -24.250  1.00 21.77           C  
-ANISOU 4131  C   ASP B 469     3169   2603   2497    115   -345   -137       C  
-ATOM   4132  O   ASP B 469      44.053   7.884 -24.060  1.00 22.65           O  
-ANISOU 4132  O   ASP B 469     3003   2650   2952   -166   -333   -400       O  
-ATOM   4133  CB  ASP B 469      43.352   6.527 -26.725  1.00 29.11           C  
-ANISOU 4133  CB  ASP B 469     4453   3085   3520    647    -97    243       C  
-ATOM   4134  CG  ASP B 469      43.928   5.581 -27.766  1.00 35.20           C  
-ANISOU 4134  CG  ASP B 469     5044   3901   4427   1142    173     77       C  
-ATOM   4135  OD1 ASP B 469      44.898   4.858 -27.440  1.00 37.32           O  
-ANISOU 4135  OD1 ASP B 469     5314   4137   4727   1251    332    165       O  
-ATOM   4136  OD2 ASP B 469      43.411   5.545 -28.899  1.00 38.10           O  
-ANISOU 4136  OD2 ASP B 469     5228   4162   5085   1151     70   -450       O  
-ATOM   4137  N   ALA B 470      42.087   6.928 -23.546  1.00 18.07           N  
-ANISOU 4137  N   ALA B 470     2598   2227   2041   -183   -460   -297       N  
-ATOM   4138  CA  ALA B 470      41.833   7.831 -22.430  1.00 18.94           C  
-ANISOU 4138  CA  ALA B 470     2350   2244   2601   -287   -513   -228       C  
-ATOM   4139  C   ALA B 470      40.814   7.234 -21.480  1.00 18.36           C  
-ANISOU 4139  C   ALA B 470     2227   2343   2406   -259   -673    -92       C  
-ATOM   4140  O   ALA B 470      39.986   6.412 -21.877  1.00 19.51           O  
-ANISOU 4140  O   ALA B 470     2428   2307   2676   -358   -954    -31       O  
-ATOM   4141  CB  ALA B 470      41.367   9.199 -22.925  1.00 19.26           C  
-ANISOU 4141  CB  ALA B 470     2330   2235   2754   -298   -322   -139       C  
-ATOM   4142  N   ALA B 471      40.887   7.650 -20.221  1.00 17.69           N  
-ANISOU 4142  N   ALA B 471     1858   2320   2541   -378   -237    -93       N  
-ATOM   4143  CA  ALA B 471      39.946   7.206 -19.202  1.00 17.76           C  
-ANISOU 4143  CA  ALA B 471     1936   2128   2682   -193   -224    -73       C  
-ATOM   4144  C   ALA B 471      39.023   8.348 -18.809  1.00 17.59           C  
-ANISOU 4144  C   ALA B 471     1850   2181   2652   -145    -95     18       C  
-ATOM   4145  O   ALA B 471      39.482   9.415 -18.394  1.00 18.37           O  
-ANISOU 4145  O   ALA B 471     1895   1955   3128   -109   -209   -184       O  
-ATOM   4146  CB  ALA B 471      40.686   6.685 -17.986  1.00 18.25           C  
-ANISOU 4146  CB  ALA B 471     2127   1835   2970   -148   -153     98       C  
-ATOM   4147  N   LEU B 472      37.722   8.121 -18.949  1.00 16.39           N  
-ANISOU 4147  N   LEU B 472     1960   2502   1763     84    -76    220       N  
-ATOM   4148  CA  LEU B 472      36.732   9.104 -18.548  1.00 16.39           C  
-ANISOU 4148  CA  LEU B 472     1789   2517   1922   -316   -518     97       C  
-ATOM   4149  C   LEU B 472      36.484   8.981 -17.053  1.00 16.07           C  
-ANISOU 4149  C   LEU B 472     1764   2447   1895   -259   -207    121       C  
-ATOM   4150  O   LEU B 472      36.154   7.898 -16.560  1.00 17.55           O  
-ANISOU 4150  O   LEU B 472     2065   2404   2199   -340   -352    345       O  
-ATOM   4151  CB  LEU B 472      35.428   8.893 -19.312  1.00 17.81           C  
-ANISOU 4151  CB  LEU B 472     1673   2681   2412   -495   -638     10       C  
-ATOM   4152  CG  LEU B 472      34.244   9.766 -18.906  1.00 20.12           C  
-ANISOU 4152  CG  LEU B 472     1984   2889   2772    -99   -764    191       C  
-ATOM   4153  CD1 LEU B 472      34.540  11.232 -19.188  1.00 21.51           C  
-ANISOU 4153  CD1 LEU B 472     2166   2870   3136    148  -1053     26       C  
-ATOM   4154  CD2 LEU B 472      32.983   9.321 -19.636  1.00 20.89           C  
-ANISOU 4154  CD2 LEU B 472     1992   2962   2982   -192  -1105    270       C  
-ATOM   4155  N   LEU B 473      36.650  10.091 -16.339  1.00 15.54           N  
-ANISOU 4155  N   LEU B 473     1639   2390   1873    -27    -82    175       N  
-ATOM   4156  CA  LEU B 473      36.390  10.137 -14.904  1.00 16.27           C  
-ANISOU 4156  CA  LEU B 473     1628   2439   2115    145   -181   -100       C  
-ATOM   4157  C   LEU B 473      35.243  11.086 -14.601  1.00 17.97           C  
-ANISOU 4157  C   LEU B 473     1661   2863   2304    318   -251    125       C  
-ATOM   4158  O   LEU B 473      35.051  12.086 -15.298  1.00 18.38           O  
-ANISOU 4158  O   LEU B 473     1803   2959   2222    312   -339    406       O  
-ATOM   4159  CB  LEU B 473      37.626  10.623 -14.134  1.00 15.91           C  
-ANISOU 4159  CB  LEU B 473     1664   2313   2067    196   -470     -4       C  
-ATOM   4160  CG  LEU B 473      38.977   9.948 -14.345  1.00 16.59           C  
-ANISOU 4160  CG  LEU B 473     1689   2115   2497    161   -637    169       C  
-ATOM   4161  CD1 LEU B 473      39.998  10.572 -13.411  1.00 16.30           C  
-ANISOU 4161  CD1 LEU B 473     1840   2099   2254    -51   -693    -92       C  
-ATOM   4162  CD2 LEU B 473      38.895   8.444 -14.109  1.00 18.27           C  
-ANISOU 4162  CD2 LEU B 473     1991   1748   3201    -15   -428    266       C  
-ATOM   4163  N   HIS B 474      34.481  10.764 -13.563  1.00 17.67           N  
-ANISOU 4163  N   HIS B 474     1478   3035   2201    183   -135    -52       N  
-ATOM   4164  CA  HIS B 474      33.586  11.728 -12.944  1.00 18.18           C  
-ANISOU 4164  CA  HIS B 474     1216   3298   2394   -208   -279    136       C  
-ATOM   4165  C   HIS B 474      34.161  12.160 -11.599  1.00 18.20           C  
-ANISOU 4165  C   HIS B 474     1415   3256   2242    214   -387    154       C  
-ATOM   4166  O   HIS B 474      34.771  11.359 -10.897  1.00 20.24           O  
-ANISOU 4166  O   HIS B 474     2034   3268   2387    755   -521    337       O  
-ATOM   4167  CB  HIS B 474      32.202  11.119 -12.723  1.00 19.88           C  
-ANISOU 4167  CB  HIS B 474     1242   3712   2598   -297   -580    374       C  
-ATOM   4168  CG  HIS B 474      31.397  10.958 -13.974  1.00 22.72           C  
-ANISOU 4168  CG  HIS B 474     1690   4142   2800   -119   -731    398       C  
-ATOM   4169  ND1 HIS B 474      31.822  11.414 -15.204  1.00 25.50           N  
-ANISOU 4169  ND1 HIS B 474     1957   4373   3359    149   -889    171       N  
-ATOM   4170  CD2 HIS B 474      30.180  10.401 -14.178  1.00 24.70           C  
-ANISOU 4170  CD2 HIS B 474     1729   4199   3458   -335  -1106    335       C  
-ATOM   4171  CE1 HIS B 474      30.902  11.138 -16.113  1.00 25.60           C  
-ANISOU 4171  CE1 HIS B 474     1683   4446   3597   -125   -788    312       C  
-ATOM   4172  NE2 HIS B 474      29.898  10.520 -15.517  1.00 27.80           N  
-ANISOU 4172  NE2 HIS B 474     2031   4554   3977     60  -1367   -139       N  
-ATOM   4173  N   TYR B 475      33.978  13.430 -11.257  1.00 18.09           N  
-ANISOU 4173  N   TYR B 475     1567   3073   2233    252   -263     47       N  
-ATOM   4174  CA  TYR B 475      34.342  13.951  -9.945  1.00 16.72           C  
-ANISOU 4174  CA  TYR B 475     1392   3068   1894    176    -93    178       C  
-ATOM   4175  C   TYR B 475      33.047  14.128  -9.168  1.00 19.54           C  
-ANISOU 4175  C   TYR B 475     1401   3729   2294    312    281    413       C  
-ATOM   4176  O   TYR B 475      32.242  15.008  -9.481  1.00 21.88           O  
-ANISOU 4176  O   TYR B 475     1393   3798   3122    454    -19    653       O  
-ATOM   4177  CB  TYR B 475      35.081  15.277 -10.107  1.00 18.11           C  
-ANISOU 4177  CB  TYR B 475     1505   3145   2230    256   -180     62       C  
-ATOM   4178  CG  TYR B 475      35.582  15.910  -8.830  1.00 15.87           C  
-ANISOU 4178  CG  TYR B 475     1335   3042   1654    339   -295     79       C  
-ATOM   4179  CD1 TYR B 475      36.596  15.319  -8.088  1.00 15.29           C  
-ANISOU 4179  CD1 TYR B 475     1192   3055   1560    179   -131    242       C  
-ATOM   4180  CD2 TYR B 475      35.074  17.127  -8.391  1.00 18.24           C  
-ANISOU 4180  CD2 TYR B 475     1632   3149   2147    648     47    271       C  
-ATOM   4181  CE1 TYR B 475      37.061  15.910  -6.927  1.00 16.17           C  
-ANISOU 4181  CE1 TYR B 475     1374   3118   1651    473    -99    283       C  
-ATOM   4182  CE2 TYR B 475      35.535  17.726  -7.239  1.00 16.98           C  
-ANISOU 4182  CE2 TYR B 475     1610   3056   1786    517   -582     25       C  
-ATOM   4183  CZ  TYR B 475      36.529  17.115  -6.508  1.00 16.25           C  
-ANISOU 4183  CZ  TYR B 475     1468   3029   1678    465   -401    313       C  
-ATOM   4184  OH  TYR B 475      37.003  17.704  -5.358  1.00 17.81           O  
-ANISOU 4184  OH  TYR B 475     1623   3097   2048    591   -493    389       O  
-ATOM   4185  N   VAL B 476      32.843  13.275  -8.167  1.00 20.67           N  
-ANISOU 4185  N   VAL B 476     1269   4299   2284    151    234    278       N  
-ATOM   4186  CA  VAL B 476      31.526  13.093  -7.563  1.00 23.39           C  
-ANISOU 4186  CA  VAL B 476     1616   4710   2561    -53     82   -218       C  
-ATOM   4187  C   VAL B 476      31.441  13.624  -6.131  1.00 24.25           C  
-ANISOU 4187  C   VAL B 476     1656   5159   2400   -226    307     79       C  
-ATOM   4188  O   VAL B 476      32.373  13.483  -5.338  1.00 24.61           O  
-ANISOU 4188  O   VAL B 476     1473   5389   2489   -203     70     96       O  
-ATOM   4189  CB  VAL B 476      31.127  11.604  -7.579  1.00 25.07           C  
-ANISOU 4189  CB  VAL B 476     1877   4543   3105   -475    315   -420       C  
-ATOM   4190  CG1 VAL B 476      29.767  11.413  -6.949  1.00 28.44           C  
-ANISOU 4190  CG1 VAL B 476     2270   4961   3574    -44     81   -287       C  
-ATOM   4191  CG2 VAL B 476      31.129  11.068  -9.006  1.00 25.17           C  
-ANISOU 4191  CG2 VAL B 476     2082   4589   2890   -502    266   -464       C  
-ATOM   4192  N   ASP B 477      30.315  14.250  -5.813  1.00 28.28           N  
-ANISOU 4192  N   ASP B 477     2136   5607   3000   -271    419    -35       N  
-ATOM   4193  CA  ASP B 477      30.055  14.692  -4.454  1.00 32.91           C  
-ANISOU 4193  CA  ASP B 477     2912   6087   3503   -148    495     -8       C  
-ATOM   4194  C   ASP B 477      29.997  13.471  -3.544  1.00 33.26           C  
-ANISOU 4194  C   ASP B 477     3159   6422   3057   -805    702    444       C  
-ATOM   4195  O   ASP B 477      29.295  12.505  -3.838  1.00 32.86           O  
-ANISOU 4195  O   ASP B 477     3157   6166   3163   -938    563    576       O  
-ATOM   4196  CB  ASP B 477      28.741  15.467  -4.392  1.00 38.68           C  
-ANISOU 4196  CB  ASP B 477     3638   6607   4451    628    847   -330       C  
-ATOM   4197  CG  ASP B 477      28.501  16.091  -3.036  1.00 44.71           C  
-ANISOU 4197  CG  ASP B 477     4374   6994   5619   1219    776   -610       C  
-ATOM   4198  OD1 ASP B 477      28.595  17.333  -2.928  1.00 46.82           O  
-ANISOU 4198  OD1 ASP B 477     4691   7049   6049   1655    534   -934       O  
-ATOM   4199  OD2 ASP B 477      28.228  15.338  -2.077  1.00 46.74           O  
-ANISOU 4199  OD2 ASP B 477     4555   7198   6004   1232   1024   -492       O  
-ATOM   4200  N   PRO B 478      30.739  13.512  -2.430  1.00 34.94           N  
-ANISOU 4200  N   PRO B 478     3583   6690   3003  -1141    578    446       N  
-ATOM   4201  CA  PRO B 478      30.919  12.357  -1.544  1.00 38.97           C  
-ANISOU 4201  CA  PRO B 478     4061   6928   3819  -1074    451    366       C  
-ATOM   4202  C   PRO B 478      29.645  12.001  -0.792  1.00 42.28           C  
-ANISOU 4202  C   PRO B 478     4521   7241   4301  -1106    653    466       C  
-ATOM   4203  O   PRO B 478      29.492  10.869  -0.332  1.00 43.28           O  
-ANISOU 4203  O   PRO B 478     4638   7118   4686  -1285    594    195       O  
-ATOM   4204  CB  PRO B 478      31.989  12.842  -0.563  1.00 39.47           C  
-ANISOU 4204  CB  PRO B 478     4124   7040   3832   -901     30    322       C  
-ATOM   4205  CG  PRO B 478      31.798  14.318  -0.512  1.00 38.06           C  
-ANISOU 4205  CG  PRO B 478     4027   6916   3519  -1051     18    328       C  
-ATOM   4206  CD  PRO B 478      31.418  14.714  -1.916  1.00 36.06           C  
-ANISOU 4206  CD  PRO B 478     3820   6765   3117  -1143    231    450       C  
-ATOM   4207  N   ASP B 479      28.740  12.966  -0.671  1.00 45.05           N  
-ANISOU 4207  N   ASP B 479     4716   7706   4694  -1068   1092    808       N  
-ATOM   4208  CA  ASP B 479      27.512  12.772   0.090  1.00 50.41           C  
-ANISOU 4208  CA  ASP B 479     5136   8233   5783   -679   1074    814       C  
-ATOM   4209  C   ASP B 479      26.330  12.483  -0.827  1.00 52.16           C  
-ANISOU 4209  C   ASP B 479     4983   8323   6512   -959   1092   1164       C  
-ATOM   4210  O   ASP B 479      25.622  11.489  -0.653  1.00 53.51           O  
-ANISOU 4210  O   ASP B 479     5136   8329   6866  -1063    972   1413       O  
-ATOM   4211  CB  ASP B 479      27.218  14.009   0.937  1.00 53.84           C  
-ANISOU 4211  CB  ASP B 479     5727   8541   6188   -114    985    492       C  
-ATOM   4212  CG  ASP B 479      28.417  14.457   1.749  1.00 56.81           C  
-ANISOU 4212  CG  ASP B 479     6279   8747   6557    376    882     40       C  
-ATOM   4213  OD1 ASP B 479      28.700  15.674   1.767  1.00 58.73           O  
-ANISOU 4213  OD1 ASP B 479     6494   8756   7065    512    835   -167       O  
-ATOM   4214  OD2 ASP B 479      29.077  13.592   2.367  1.00 56.64           O  
-ANISOU 4214  OD2 ASP B 479     6490   8772   6258    616    856    -56       O  
-ATOM   4215  N   THR B 480      26.124  13.360  -1.803  1.00 52.44           N  
-ANISOU 4215  N   THR B 480     4728   8516   6681  -1170   1090   1037       N  
-ATOM   4216  CA  THR B 480      24.982  13.262  -2.703  1.00 52.86           C  
-ANISOU 4216  CA  THR B 480     4590   8682   6812  -1119    982    723       C  
-ATOM   4217  C   THR B 480      25.243  12.310  -3.865  1.00 52.03           C  
-ANISOU 4217  C   THR B 480     4582   8403   6783  -1254    556    696       C  
-ATOM   4218  O   THR B 480      24.310  11.835  -4.504  1.00 50.83           O  
-ANISOU 4218  O   THR B 480     4466   8099   6746  -1624    665    954       O  
-ATOM   4219  CB  THR B 480      24.599  14.641  -3.274  1.00 53.92           C  
-ANISOU 4219  CB  THR B 480     4401   9191   6893  -1028   1202    308       C  
-ATOM   4220  OG1 THR B 480      25.634  15.103  -4.153  1.00 53.76           O  
-ANISOU 4220  OG1 THR B 480     4140   9387   6899  -1071   1308    112       O  
-ATOM   4221  CG2 THR B 480      24.406  15.650  -2.150  1.00 53.82           C  
-ANISOU 4221  CG2 THR B 480     4382   9351   6716  -1031   1352    222       C  
-ATOM   4222  N   HIS B 481      26.515  12.038  -4.138  1.00 50.99           N  
-ANISOU 4222  N   HIS B 481     4644   8060   6670  -1117    163    634       N  
-ATOM   4223  CA  HIS B 481      26.893  11.180  -5.257  1.00 51.40           C  
-ANISOU 4223  CA  HIS B 481     4809   7932   6788   -690   -271    520       C  
-ATOM   4224  C   HIS B 481      26.565  11.822  -6.605  1.00 46.57           C  
-ANISOU 4224  C   HIS B 481     4139   7406   6150  -1117   -524    550       C  
-ATOM   4225  O   HIS B 481      26.512  11.143  -7.629  1.00 47.42           O  
-ANISOU 4225  O   HIS B 481     4196   7410   6411  -1204   -650    516       O  
-ATOM   4226  CB  HIS B 481      26.233   9.801  -5.143  1.00 55.85           C  
-ANISOU 4226  CB  HIS B 481     5635   8044   7539    224   -518    390       C  
-ATOM   4227  CG  HIS B 481      26.789   8.957  -4.040  1.00 60.35           C  
-ANISOU 4227  CG  HIS B 481     6343   8370   8215   1104   -660    335       C  
-ATOM   4228  ND1 HIS B 481      26.504   9.186  -2.711  1.00 61.96           N  
-ANISOU 4228  ND1 HIS B 481     6637   8459   8445   1498   -700    290       N  
-ATOM   4229  CD2 HIS B 481      27.620   7.888  -4.067  1.00 62.17           C  
-ANISOU 4229  CD2 HIS B 481     6631   8483   8506   1511   -696    342       C  
-ATOM   4230  CE1 HIS B 481      27.133   8.291  -1.967  1.00 62.86           C  
-ANISOU 4230  CE1 HIS B 481     6768   8576   8538   1673   -744    356       C  
-ATOM   4231  NE2 HIS B 481      27.817   7.492  -2.766  1.00 63.06           N  
-ANISOU 4231  NE2 HIS B 481     6771   8587   8602   1675   -752    382       N  
-ATOM   4232  N   ARG B 482      26.350  13.133  -6.593  1.00 43.36           N  
-ANISOU 4232  N   ARG B 482     3621   7223   5629  -1024   -396    820       N  
-ATOM   4233  CA  ARG B 482      26.122  13.887  -7.821  1.00 43.12           C  
-ANISOU 4233  CA  ARG B 482     3506   7255   5623   -467   -154   1003       C  
-ATOM   4234  C   ARG B 482      27.427  14.091  -8.578  1.00 37.35           C  
-ANISOU 4234  C   ARG B 482     2924   6683   4584   -292   -430    847       C  
-ATOM   4235  O   ARG B 482      28.450  14.421  -7.978  1.00 34.90           O  
-ANISOU 4235  O   ARG B 482     2537   6556   4168   -520   -804    619       O  
-ATOM   4236  CB  ARG B 482      25.518  15.255  -7.503  1.00 49.40           C  
-ANISOU 4236  CB  ARG B 482     4074   7839   6856     56     55   1030       C  
-ATOM   4237  CG  ARG B 482      24.016  15.264  -7.290  1.00 55.09           C  
-ANISOU 4237  CG  ARG B 482     4727   8283   7920    612    163    979       C  
-ATOM   4238  CD  ARG B 482      23.527  16.666  -6.942  1.00 59.27           C  
-ANISOU 4238  CD  ARG B 482     5236   8569   8715    820    231    872       C  
-ATOM   4239  NE  ARG B 482      24.122  17.685  -7.804  1.00 61.87           N  
-ANISOU 4239  NE  ARG B 482     5637   8660   9211   1052    187    759       N  
-ATOM   4240  CZ  ARG B 482      25.177  18.426  -7.472  1.00 63.05           C  
-ANISOU 4240  CZ  ARG B 482     5823   8671   9460   1244     74    699       C  
-ATOM   4241  NH1 ARG B 482      25.758  18.266  -6.289  1.00 63.57           N  
-ANISOU 4241  NH1 ARG B 482     5900   8741   9512   1351     67    750       N  
-ATOM   4242  NH2 ARG B 482      25.650  19.329  -8.321  1.00 63.23           N  
-ANISOU 4242  NH2 ARG B 482     5856   8671   9495   1256     31    619       N  
-ATOM   4243  N   ASN B 483      27.386  13.903  -9.893  1.00 35.26           N  
-ANISOU 4243  N   ASN B 483     2693   6478   4227     97   -377    744       N  
-ATOM   4244  CA  ASN B 483      28.532  14.204 -10.743  1.00 31.60           C  
-ANISOU 4244  CA  ASN B 483     2322   5959   3724    297   -578    565       C  
-ATOM   4245  C   ASN B 483      28.769  15.709 -10.814  1.00 31.29           C  
-ANISOU 4245  C   ASN B 483     2358   5791   3738    921   -329    752       C  
-ATOM   4246  O   ASN B 483      27.884  16.463 -11.223  1.00 35.07           O  
-ANISOU 4246  O   ASN B 483     2761   6115   4450   1505   -485    836       O  
-ATOM   4247  CB  ASN B 483      28.331  13.632 -12.147  1.00 32.05           C  
-ANISOU 4247  CB  ASN B 483     2399   5630   4149    216   -628    117       C  
-ATOM   4248  CG  ASN B 483      29.500  13.920 -13.067  1.00 33.94           C  
-ANISOU 4248  CG  ASN B 483     2704   5522   4668    537   -484     37       C  
-ATOM   4249  OD1 ASN B 483      30.625  14.123 -12.613  1.00 34.46           O  
-ANISOU 4249  OD1 ASN B 483     2532   5290   5271    203     60    -41       O  
-ATOM   4250  ND2 ASN B 483      29.240  13.937 -14.368  1.00 34.34           N  
-ANISOU 4250  ND2 ASN B 483     3044   5406   4596    790   -140     84       N  
-ATOM   4251  N   LEU B 484      29.960  16.146 -10.415  1.00 28.97           N  
-ANISOU 4251  N   LEU B 484     2447   5438   3123   1126     44    519       N  
-ATOM   4252  CA  LEU B 484      30.277  17.570 -10.378  1.00 29.03           C  
-ANISOU 4252  CA  LEU B 484     2601   5284   3144   1374    413    423       C  
-ATOM   4253  C   LEU B 484      31.067  18.027 -11.600  1.00 28.00           C  
-ANISOU 4253  C   LEU B 484     2643   4967   3028   1507    418    234       C  
-ATOM   4254  O   LEU B 484      31.216  19.224 -11.836  1.00 28.72           O  
-ANISOU 4254  O   LEU B 484     2873   4989   3050   1596    338    169       O  
-ATOM   4255  CB  LEU B 484      31.057  17.913  -9.109  1.00 28.00           C  
-ANISOU 4255  CB  LEU B 484     2832   5322   2485   1606    422    155       C  
-ATOM   4256  CG  LEU B 484      30.427  17.494  -7.782  1.00 29.98           C  
-ANISOU 4256  CG  LEU B 484     2871   5420   3098   1555    557    162       C  
-ATOM   4257  CD1 LEU B 484      31.391  17.758  -6.634  1.00 30.34           C  
-ANISOU 4257  CD1 LEU B 484     3148   5353   3026   1503    417   -112       C  
-ATOM   4258  CD2 LEU B 484      29.103  18.217  -7.566  1.00 31.79           C  
-ANISOU 4258  CD2 LEU B 484     2835   5565   3677   1576    742    113       C  
-ATOM   4259  N   GLY B 485      31.581  17.076 -12.372  1.00 26.45           N  
-ANISOU 4259  N   GLY B 485     2404   4608   3037   1333    260    522       N  
-ATOM   4260  CA  GLY B 485      32.338  17.412 -13.563  1.00 25.25           C  
-ANISOU 4260  CA  GLY B 485     2253   4216   3124   1221    296    394       C  
-ATOM   4261  C   GLY B 485      33.049  16.217 -14.159  1.00 21.81           C  
-ANISOU 4261  C   GLY B 485     1894   3872   2521    715   -134    478       C  
-ATOM   4262  O   GLY B 485      33.408  15.286 -13.439  1.00 21.86           O  
-ANISOU 4262  O   GLY B 485     2193   3718   2395    834   -382    573       O  
-ATOM   4263  N   GLU B 486      33.250  16.246 -15.474  1.00 22.74           N  
-ANISOU 4263  N   GLU B 486     1873   3898   2868    569    378    542       N  
-ATOM   4264  CA  GLU B 486      33.931  15.166 -16.182  1.00 21.28           C  
-ANISOU 4264  CA  GLU B 486     1799   3793   2494    414   -213    457       C  
-ATOM   4265  C   GLU B 486      35.386  15.530 -16.444  1.00 19.73           C  
-ANISOU 4265  C   GLU B 486     1873   3174   2449    451   -412    201       C  
-ATOM   4266  O   GLU B 486      35.711  16.695 -16.677  1.00 19.51           O  
-ANISOU 4266  O   GLU B 486     1961   2947   2506    714   -314    187       O  
-ATOM   4267  CB  GLU B 486      33.231  14.855 -17.515  1.00 23.78           C  
-ANISOU 4267  CB  GLU B 486     1997   4305   2733    125   -549    520       C  
-ATOM   4268  CG  GLU B 486      31.827  14.264 -17.393  1.00 29.94           C  
-ANISOU 4268  CG  GLU B 486     2386   4934   4055    106   -599    681       C  
-ATOM   4269  CD  GLU B 486      31.355  13.586 -18.677  1.00 36.16           C  
-ANISOU 4269  CD  GLU B 486     2969   5582   5188    240   -503    943       C  
-ATOM   4270  OE1 GLU B 486      31.785  14.000 -19.778  1.00 37.65           O  
-ANISOU 4270  OE1 GLU B 486     2996   5729   5580    285   -580    934       O  
-ATOM   4271  OE2 GLU B 486      30.555  12.628 -18.586  1.00 39.05           O  
-ANISOU 4271  OE2 GLU B 486     3664   5928   5246    866   -660    864       O  
-ATOM   4272  N   PHE B 487      36.252  14.521 -16.402  1.00 16.20           N  
-ANISOU 4272  N   PHE B 487     1432   2836   1887    455   -354     39       N  
-ATOM   4273  CA  PHE B 487      37.672  14.687 -16.671  1.00 15.23           C  
-ANISOU 4273  CA  PHE B 487     1626   2384   1775    101   -176    123       C  
-ATOM   4274  C   PHE B 487      38.159  13.547 -17.559  1.00 15.27           C  
-ANISOU 4274  C   PHE B 487     1745   2236   1821    195   -316    -25       C  
-ATOM   4275  O   PHE B 487      37.574  12.461 -17.567  1.00 17.05           O  
-ANISOU 4275  O   PHE B 487     1893   2393   2191    -21   -374    -10       O  
-ATOM   4276  CB  PHE B 487      38.469  14.675 -15.365  1.00 15.45           C  
-ANISOU 4276  CB  PHE B 487     1828   2458   1585    211   -318    -48       C  
-ATOM   4277  CG  PHE B 487      38.138  15.806 -14.437  1.00 14.89           C  
-ANISOU 4277  CG  PHE B 487     1855   2357   1446     52   -243    135       C  
-ATOM   4278  CD1 PHE B 487      38.945  16.928 -14.379  1.00 17.28           C  
-ANISOU 4278  CD1 PHE B 487     1960   2421   2182    113    -98   -196       C  
-ATOM   4279  CD2 PHE B 487      37.020  15.745 -13.620  1.00 16.81           C  
-ANISOU 4279  CD2 PHE B 487     1967   2747   1672    445    -21     44       C  
-ATOM   4280  CE1 PHE B 487      38.644  17.976 -13.517  1.00 18.03           C  
-ANISOU 4280  CE1 PHE B 487     2022   2518   2308    301     85   -100       C  
-ATOM   4281  CE2 PHE B 487      36.712  16.784 -12.758  1.00 18.47           C  
-ANISOU 4281  CE2 PHE B 487     2061   2658   2297    450    -93    209       C  
-ATOM   4282  CZ  PHE B 487      37.524  17.900 -12.706  1.00 17.49           C  
-ANISOU 4282  CZ  PHE B 487     2009   2790   1847    370    412    404       C  
-ATOM   4283  N   LYS B 488      39.233  13.791 -18.302  1.00 15.17           N  
-ANISOU 4283  N   LYS B 488     1540   2201   2021    281   -171    -75       N  
-ATOM   4284  CA  LYS B 488      39.878  12.736 -19.080  1.00 16.04           C  
-ANISOU 4284  CA  LYS B 488     1744   2440   1911      9   -325   -192       C  
-ATOM   4285  C   LYS B 488      41.278  12.503 -18.533  1.00 15.57           C  
-ANISOU 4285  C   LYS B 488     1722   2403   1789   -110   -575   -207       C  
-ATOM   4286  O   LYS B 488      42.029  13.452 -18.321  1.00 19.22           O  
-ANISOU 4286  O   LYS B 488     1833   2158   3312    -77   -626   -160       O  
-ATOM   4287  CB  LYS B 488      39.954  13.118 -20.561  1.00 18.73           C  
-ANISOU 4287  CB  LYS B 488     1974   2809   2333   -115   -799   -128       C  
-ATOM   4288  CG  LYS B 488      38.649  12.925 -21.317  1.00 21.44           C  
-ANISOU 4288  CG  LYS B 488     2295   3198   2653    221   -752   -117       C  
-ATOM   4289  CD  LYS B 488      38.649  13.670 -22.650  1.00 22.14           C  
-ANISOU 4289  CD  LYS B 488     2715   3294   2404    702   -681    -43       C  
-ATOM   4290  CE  LYS B 488      39.674  13.101 -23.632  1.00 22.04           C  
-ANISOU 4290  CE  LYS B 488     2995   3132   2247    667   -818    529       C  
-ATOM   4291  NZ  LYS B 488      39.546  13.734 -24.983  1.00 21.88           N  
-ANISOU 4291  NZ  LYS B 488     3081   2766   2465    578  -1087   -148       N  
-ATOM   4292  N   MET B 489      41.619  11.241 -18.298  1.00 14.80           N  
-ANISOU 4292  N   MET B 489     1769   2163   1692   -180   -289     78       N  
-ATOM   4293  CA  MET B 489      42.970  10.872 -17.896  1.00 15.64           C  
-ANISOU 4293  CA  MET B 489     1910   2200   1832   -274   -419    392       C  
-ATOM   4294  C   MET B 489      43.628  10.204 -19.076  1.00 15.94           C  
-ANISOU 4294  C   MET B 489     2034   1888   2133   -155   -233    -93       C  
-ATOM   4295  O   MET B 489      43.052   9.307 -19.675  1.00 21.04           O  
-ANISOU 4295  O   MET B 489     2177   2275   3540   -342    246   -802       O  
-ATOM   4296  CB  MET B 489      42.960   9.864 -16.751  1.00 19.44           C  
-ANISOU 4296  CB  MET B 489     2482   2579   2323   -415   -344    848       C  
-ATOM   4297  CG  MET B 489      42.739  10.421 -15.386  1.00 22.82           C  
-ANISOU 4297  CG  MET B 489     3056   2595   3018     95     30    332       C  
-ATOM   4298  SD  MET B 489      43.576   9.392 -14.157  1.00 20.35           S  
-ANISOU 4298  SD  MET B 489     3409   2581   1741    477    139    454       S  
-ATOM   4299  CE  MET B 489      45.191  10.152 -14.155  1.00 24.28           C  
-ANISOU 4299  CE  MET B 489     3410   2825   2989    499   -230   -103       C  
-ATOM   4300  N   TYR B 490      44.838  10.629 -19.402  1.00 13.63           N  
-ANISOU 4300  N   TYR B 490     1698   1576   1904   -306   -189    170       N  
-ATOM   4301  CA  TYR B 490      45.560  10.039 -20.513  1.00 13.85           C  
-ANISOU 4301  CA  TYR B 490     1825   1648   1789   -169   -199     80       C  
-ATOM   4302  C   TYR B 490      46.574   9.022 -19.990  1.00 14.75           C  
-ANISOU 4302  C   TYR B 490     1977   1500   2128   -268   -297     42       C  
-ATOM   4303  O   TYR B 490      46.986   9.096 -18.835  1.00 14.97           O  
-ANISOU 4303  O   TYR B 490     2030   1552   2105   -141   -473    162       O  
-ATOM   4304  CB  TYR B 490      46.226  11.132 -21.351  1.00 15.34           C  
-ANISOU 4304  CB  TYR B 490     2007   1640   2181    -82   -324    541       C  
-ATOM   4305  CG  TYR B 490      45.234  11.989 -22.112  1.00 16.46           C  
-ANISOU 4305  CG  TYR B 490     2358   1857   2039    207   -344    243       C  
-ATOM   4306  CD1 TYR B 490      44.912  11.702 -23.436  1.00 17.43           C  
-ANISOU 4306  CD1 TYR B 490     2615   2217   1788    316   -501    261       C  
-ATOM   4307  CD2 TYR B 490      44.612  13.077 -21.505  1.00 17.44           C  
-ANISOU 4307  CD2 TYR B 490     2393   1940   2293    315   -281    427       C  
-ATOM   4308  CE1 TYR B 490      44.005  12.478 -24.135  1.00 19.28           C  
-ANISOU 4308  CE1 TYR B 490     2832   2306   2186    870   -477     68       C  
-ATOM   4309  CE2 TYR B 490      43.698  13.863 -22.200  1.00 17.29           C  
-ANISOU 4309  CE2 TYR B 490     2387   2243   1937    288   -271     99       C  
-ATOM   4310  CZ  TYR B 490      43.403  13.558 -23.516  1.00 18.67           C  
-ANISOU 4310  CZ  TYR B 490     2642   2481   1969    778   -542    230       C  
-ATOM   4311  OH  TYR B 490      42.500  14.324 -24.227  1.00 20.83           O  
-ANISOU 4311  OH  TYR B 490     3043   2717   2152    933   -801   -267       O  
-ATOM   4312  N   PRO B 491      46.964   8.064 -20.842  1.00 14.92           N  
-ANISOU 4312  N   PRO B 491     2209   1624   1836    -30   -605   -191       N  
-ATOM   4313  CA  PRO B 491      47.866   6.964 -20.477  1.00 15.69           C  
-ANISOU 4313  CA  PRO B 491     2264   1642   2056    311   -479   -276       C  
-ATOM   4314  C   PRO B 491      49.171   7.448 -19.848  1.00 14.98           C  
-ANISOU 4314  C   PRO B 491     2250   1587   1855    185   -275    -55       C  
-ATOM   4315  O   PRO B 491      49.732   6.742 -19.009  1.00 14.89           O  
-ANISOU 4315  O   PRO B 491     2265   1454   1937    223   -384     99       O  
-ATOM   4316  CB  PRO B 491      48.142   6.286 -21.822  1.00 16.28           C  
-ANISOU 4316  CB  PRO B 491     2278   1742   2164    141   -608   -297       C  
-ATOM   4317  CG  PRO B 491      46.895   6.537 -22.623  1.00 17.93           C  
-ANISOU 4317  CG  PRO B 491     2440   1769   2601     73   -715   -446       C  
-ATOM   4318  CD  PRO B 491      46.472   7.937 -22.228  1.00 16.89           C  
-ANISOU 4318  CD  PRO B 491     2526   1627   2262    319   -800   -569       C  
-ATOM   4319  N   GLU B 492      49.634   8.632 -20.245  1.00 14.78           N  
-ANISOU 4319  N   GLU B 492     2243   1518   1853   -154   -330   -254       N  
-ATOM   4320  CA  GLU B 492      50.869   9.217 -19.721  1.00 15.16           C  
-ANISOU 4320  CA  GLU B 492     2293   1881   1586   -257   -401   -260       C  
-ATOM   4321  C   GLU B 492      50.781   9.639 -18.252  1.00 15.18           C  
-ANISOU 4321  C   GLU B 492     2212   1801   1755   -214   -139    154       C  
-ATOM   4322  O   GLU B 492      51.796   9.973 -17.634  1.00 17.21           O  
-ANISOU 4322  O   GLU B 492     2181   2464   1893   -575   -261     52       O  
-ATOM   4323  CB  GLU B 492      51.292  10.411 -20.574  1.00 16.48           C  
-ANISOU 4323  CB  GLU B 492     2479   2201   1581   -461    125    140       C  
-ATOM   4324  CG  GLU B 492      51.720  10.052 -21.987  1.00 19.16           C  
-ANISOU 4324  CG  GLU B 492     2675   2837   1767    -44     86   -268       C  
-ATOM   4325  CD  GLU B 492      50.552   9.838 -22.942  1.00 21.17           C  
-ANISOU 4325  CD  GLU B 492     2985   3208   1849    260     80   -543       C  
-ATOM   4326  OE1 GLU B 492      49.386  10.114 -22.578  1.00 20.83           O  
-ANISOU 4326  OE1 GLU B 492     2861   2856   2198    380   -100    225       O  
-ATOM   4327  OE2 GLU B 492      50.807   9.393 -24.076  1.00 26.22           O  
-ANISOU 4327  OE2 GLU B 492     3294   3983   2686    337    -90   -745       O  
-ATOM   4328  N   GLY B 493      49.575   9.628 -17.698  1.00 13.39           N  
-ANISOU 4328  N   GLY B 493     2187   1362   1538    104    -64    -41       N  
-ATOM   4329  CA  GLY B 493      49.397   9.897 -16.284  1.00 13.69           C  
-ANISOU 4329  CA  GLY B 493     1975   1390   1834    -81   -218    -45       C  
-ATOM   4330  C   GLY B 493      49.160  11.354 -15.946  1.00 14.02           C  
-ANISOU 4330  C   GLY B 493     2052   1393   1881    -71   -460    126       C  
-ATOM   4331  O   GLY B 493      49.852  11.933 -15.113  1.00 16.60           O  
-ANISOU 4331  O   GLY B 493     2476   1478   2351     47  -1013   -147       O  
-ATOM   4332  N   TYR B 494      48.180  11.952 -16.604  1.00 12.85           N  
-ANISOU 4332  N   TYR B 494     1706   1477   1700     92   -121    -57       N  
-ATOM   4333  CA  TYR B 494      47.736  13.293 -16.264  1.00 12.84           C  
-ANISOU 4333  CA  TYR B 494     1426   1424   2029     -7     72   -188       C  
-ATOM   4334  C   TYR B 494      46.273  13.404 -16.664  1.00 11.72           C  
-ANISOU 4334  C   TYR B 494     1357   1601   1494    151   -178   -245       C  
-ATOM   4335  O   TYR B 494      45.740  12.527 -17.352  1.00 13.35           O  
-ANISOU 4335  O   TYR B 494     1399   1863   1810   -116   -141   -349       O  
-ATOM   4336  CB  TYR B 494      48.577  14.360 -16.970  1.00 12.78           C  
-ANISOU 4336  CB  TYR B 494     1627   1495   1732    -35   -172    -69       C  
-ATOM   4337  CG  TYR B 494      48.390  14.393 -18.466  1.00 13.72           C  
-ANISOU 4337  CG  TYR B 494     1890   1872   1451    -96   -114     47       C  
-ATOM   4338  CD1 TYR B 494      47.550  15.329 -19.055  1.00 15.24           C  
-ANISOU 4338  CD1 TYR B 494     2022   2099   1668   -354    -72    531       C  
-ATOM   4339  CD2 TYR B 494      49.040  13.478 -19.288  1.00 14.58           C  
-ANISOU 4339  CD2 TYR B 494     2169   1854   1516   -398    316     38       C  
-ATOM   4340  CE1 TYR B 494      47.370  15.356 -20.427  1.00 17.02           C  
-ANISOU 4340  CE1 TYR B 494     2209   2483   1774   -303     54    301       C  
-ATOM   4341  CE2 TYR B 494      48.872  13.502 -20.660  1.00 16.19           C  
-ANISOU 4341  CE2 TYR B 494     2551   2017   1584   -347     85     82       C  
-ATOM   4342  CZ  TYR B 494      48.034  14.441 -21.223  1.00 16.66           C  
-ANISOU 4342  CZ  TYR B 494     2583   2329   1418   -467   -110    361       C  
-ATOM   4343  OH  TYR B 494      47.860  14.473 -22.591  1.00 19.73           O  
-ANISOU 4343  OH  TYR B 494     2974   2820   1700   -405     12    175       O  
-ATOM   4344  N   MET B 495      45.637  14.487 -16.235  1.00 12.78           N  
-ANISOU 4344  N   MET B 495     1464   1675   1717    385    -95    114       N  
-ATOM   4345  CA  MET B 495      44.208  14.662 -16.389  1.00 13.54           C  
-ANISOU 4345  CA  MET B 495     1656   1867   1621    373     51    193       C  
-ATOM   4346  C   MET B 495      43.928  15.992 -17.090  1.00 14.29           C  
-ANISOU 4346  C   MET B 495     1764   1853   1812    261   -283    140       C  
-ATOM   4347  O   MET B 495      44.667  16.961 -16.905  1.00 13.46           O  
-ANISOU 4347  O   MET B 495     1727   1611   1776    230   -234     75       O  
-ATOM   4348  CB  MET B 495      43.596  14.687 -14.990  1.00 19.11           C  
-ANISOU 4348  CB  MET B 495     1989   2491   2782    210    409    567       C  
-ATOM   4349  CG  MET B 495      42.115  14.504 -14.910  1.00 21.22           C  
-ANISOU 4349  CG  MET B 495     2383   2770   2909    432     54    519       C  
-ATOM   4350  SD  MET B 495      41.646  14.458 -13.171  1.00 16.43           S  
-ANISOU 4350  SD  MET B 495     2119   2451   1672   -165   -113    142       S  
-ATOM   4351  CE  MET B 495      42.493  13.014 -12.542  1.00 19.87           C  
-ANISOU 4351  CE  MET B 495     2267   2589   2693    -47    163    -77       C  
-ATOM   4352  N   THR B 496      42.868  16.044 -17.894  1.00 14.20           N  
-ANISOU 4352  N   THR B 496     1694   2054   1648    398   -220    127       N  
-ATOM   4353  CA  THR B 496      42.429  17.306 -18.482  1.00 14.92           C  
-ANISOU 4353  CA  THR B 496     1710   2398   1562    298   -393     44       C  
-ATOM   4354  C   THR B 496      40.953  17.556 -18.205  1.00 15.63           C  
-ANISOU 4354  C   THR B 496     1865   2254   1818    192   -301    -21       C  
-ATOM   4355  O   THR B 496      40.213  16.653 -17.821  1.00 15.38           O  
-ANISOU 4355  O   THR B 496     1779   2323   1742    248   -273    -51       O  
-ATOM   4356  CB  THR B 496      42.615  17.334 -20.009  1.00 15.78           C  
-ANISOU 4356  CB  THR B 496     1822   2451   1721    147   -161   -141       C  
-ATOM   4357  OG1 THR B 496      41.766  16.346 -20.598  1.00 15.19           O  
-ANISOU 4357  OG1 THR B 496     1850   2366   1555     77   -179     10       O  
-ATOM   4358  CG2 THR B 496      44.065  17.064 -20.395  1.00 16.80           C  
-ANISOU 4358  CG2 THR B 496     1839   2699   1843    360    -94    -66       C  
-ATOM   4359  N   CYS B 497      40.534  18.799 -18.408  1.00 16.45           N  
-ANISOU 4359  N   CYS B 497     1911   2551   1788    529   -376    -41       N  
-ATOM   4360  CA  CYS B 497      39.128  19.160 -18.337  1.00 17.93           C  
-ANISOU 4360  CA  CYS B 497     2374   2814   1625    745   -444     15       C  
-ATOM   4361  C   CYS B 497      38.856  20.176 -19.435  1.00 18.10           C  
-ANISOU 4361  C   CYS B 497     2426   2756   1693    861   -198     69       C  
-ATOM   4362  O   CYS B 497      39.779  20.624 -20.110  1.00 18.49           O  
-ANISOU 4362  O   CYS B 497     2471   2680   1874    874   -262    141       O  
-ATOM   4363  CB  CYS B 497      38.803  19.770 -16.975  1.00 21.43           C  
-ANISOU 4363  CB  CYS B 497     3043   3229   1870    994   -455   -137       C  
-ATOM   4364  SG  CYS B 497      39.541  21.400 -16.708  1.00 25.22           S  
-ANISOU 4364  SG  CYS B 497     3993   3421   2169   1354   -579   -523       S  
-ATOM   4365  N   VAL B 498      37.590  20.529 -19.623  1.00 19.87           N  
-ANISOU 4365  N   VAL B 498     2431   2853   2265    982   -326    214       N  
-ATOM   4366  CA  VAL B 498      37.240  21.640 -20.492  1.00 21.29           C  
-ANISOU 4366  CA  VAL B 498     2854   3003   2233   1030   -519     46       C  
-ATOM   4367  C   VAL B 498      36.647  22.739 -19.622  1.00 24.04           C  
-ANISOU 4367  C   VAL B 498     3176   3130   2826   1060   -155    166       C  
-ATOM   4368  O   VAL B 498      35.501  22.637 -19.190  1.00 27.44           O  
-ANISOU 4368  O   VAL B 498     3165   3132   4127    854    252      4       O  
-ATOM   4369  CB  VAL B 498      36.236  21.215 -21.580  1.00 24.79           C  
-ANISOU 4369  CB  VAL B 498     3143   3277   2998   1239   -903    328       C  
-ATOM   4370  CG1 VAL B 498      35.665  22.438 -22.287  1.00 27.41           C  
-ANISOU 4370  CG1 VAL B 498     3458   3560   3396   1424  -1143    481       C  
-ATOM   4371  CG2 VAL B 498      36.911  20.279 -22.580  1.00 26.41           C  
-ANISOU 4371  CG2 VAL B 498     3552   3389   3092   1098   -810    256       C  
-ATOM   4372  N   PRO B 499      37.442  23.781 -19.329  1.00 26.93           N  
-ANISOU 4372  N   PRO B 499     3704   3436   3092   1320   -275    -78       N  
-ATOM   4373  CA  PRO B 499      36.981  24.889 -18.484  1.00 32.17           C  
-ANISOU 4373  CA  PRO B 499     4214   3922   4088   1492    140    -89       C  
-ATOM   4374  C   PRO B 499      35.777  25.599 -19.093  1.00 41.40           C  
-ANISOU 4374  C   PRO B 499     4894   4796   6041   1703    215     98       C  
-ATOM   4375  O   PRO B 499      35.720  25.767 -20.311  1.00 42.91           O  
-ANISOU 4375  O   PRO B 499     4911   4728   6663   1953    128    577       O  
-ATOM   4376  CB  PRO B 499      38.184  25.835 -18.457  1.00 31.35           C  
-ANISOU 4376  CB  PRO B 499     4182   3718   4009   1459   -180   -440       C  
-ATOM   4377  CG  PRO B 499      39.352  24.979 -18.762  1.00 29.45           C  
-ANISOU 4377  CG  PRO B 499     3906   3497   3786   1382   -596   -245       C  
-ATOM   4378  CD  PRO B 499      38.853  23.941 -19.721  1.00 26.37           C  
-ANISOU 4378  CD  PRO B 499     3757   3256   3005   1156   -736   -362       C  
-ATOM   4379  N   ASN B 500      34.835  26.011 -18.251  1.00 47.93           N  
-ANISOU 4379  N   ASN B 500     5476   5466   7269   1616    441    -68       N  
-ATOM   4380  CA  ASN B 500      33.601  26.637 -18.717  1.00 53.92           C  
-ANISOU 4380  CA  ASN B 500     6085   6130   8270   1391    396   -145       C  
-ATOM   4381  C   ASN B 500      33.354  28.037 -18.144  1.00 53.98           C  
-ANISOU 4381  C   ASN B 500     6207   6340   7963   1154    355   -503       C  
-ATOM   4382  O   ASN B 500      34.286  28.703 -17.691  1.00 55.87           O  
-ANISOU 4382  O   ASN B 500     6293   6492   8441   1221    485   -565       O  
-ATOM   4383  CB  ASN B 500      32.404  25.722 -18.442  1.00 58.76           C  
-ANISOU 4383  CB  ASN B 500     6510   6467   9350   1364    440    -48       C  
-ATOM   4384  CG  ASN B 500      32.474  25.064 -17.075  1.00 62.63           C  
-ANISOU 4384  CG  ASN B 500     6890   6689  10217   1303    533    -75       C  
-ATOM   4385  OD1 ASN B 500      32.958  25.655 -16.110  1.00 63.92           O  
-ANISOU 4385  OD1 ASN B 500     7052   6705  10529   1292    573   -153       O  
-ATOM   4386  ND2 ASN B 500      31.995  23.827 -16.991  1.00 63.74           N  
-ANISOU 4386  ND2 ASN B 500     6990   6763  10464   1263    570     -8       N  
-ATOM   4387  N   ALA B 501      32.093  28.471 -18.175  1.00 52.14           N  
-ANISOU 4387  N   ALA B 501     6242   6318   7251    889    137   -579       N  
-ATOM   4388  CA  ALA B 501      31.704  29.813 -17.732  1.00 49.11           C  
-ANISOU 4388  CA  ALA B 501     6209   6131   6318    573      4   -523       C  
-ATOM   4389  C   ALA B 501      32.155  30.089 -16.307  1.00 47.86           C  
-ANISOU 4389  C   ALA B 501     6148   5920   6115    218     40   -218       C  
-ATOM   4390  O   ALA B 501      33.059  30.895 -16.074  1.00 49.14           O  
-ANISOU 4390  O   ALA B 501     6174   5919   6576    128    -71   -324       O  
-ATOM   4391  CB  ALA B 501      30.200  29.994 -17.853  1.00 48.16           C  
-ANISOU 4391  CB  ALA B 501     6255   5978   6065    598     39   -441       C  
-ATOM   4392  N   GLY B 502      31.505  29.437 -15.348  1.00 46.80           N  
-ANISOU 4392  N   GLY B 502     6117   5878   5785    267    -66    -65       N  
-ATOM   4393  CA  GLY B 502      32.020  29.424 -13.995  1.00 45.48           C  
-ANISOU 4393  CA  GLY B 502     6015   5774   5489    356   -236    -33       C  
-ATOM   4394  C   GLY B 502      33.436  28.914 -14.131  1.00 45.43           C  
-ANISOU 4394  C   GLY B 502     5994   5607   5661    563   -328    -67       C  
-ATOM   4395  O   GLY B 502      33.665  27.943 -14.855  1.00 46.85           O  
-ANISOU 4395  O   GLY B 502     6183   5709   5910    677   -347   -123       O  
-ATOM   4396  N   GLY B 503      34.385  29.580 -13.478  1.00 44.64           N  
-ANISOU 4396  N   GLY B 503     5790   5417   5754    820   -337     84       N  
-ATOM   4397  CA  GLY B 503      35.786  29.205 -13.578  1.00 44.05           C  
-ANISOU 4397  CA  GLY B 503     5516   5265   5955   1120    -95    344       C  
-ATOM   4398  C   GLY B 503      35.961  27.699 -13.673  1.00 42.69           C  
-ANISOU 4398  C   GLY B 503     5299   5065   5855   1347     66    716       C  
-ATOM   4399  O   GLY B 503      35.119  26.943 -13.185  1.00 44.94           O  
-ANISOU 4399  O   GLY B 503     5519   5103   6451   1243    161    785       O  
-ATOM   4400  N   GLY B 504      37.045  27.263 -14.307  1.00 37.42           N  
-ANISOU 4400  N   GLY B 504     4800   4820   4597   1786     31    870       N  
-ATOM   4401  CA  GLY B 504      37.321  25.845 -14.466  1.00 30.93           C  
-ANISOU 4401  CA  GLY B 504     4229   4342   3182   1864   -156   1023       C  
-ATOM   4402  C   GLY B 504      37.242  25.045 -13.177  1.00 28.58           C  
-ANISOU 4402  C   GLY B 504     3699   4227   2931   1799   -127    667       C  
-ATOM   4403  O   GLY B 504      36.433  25.334 -12.294  1.00 29.73           O  
-ANISOU 4403  O   GLY B 504     3490   4445   3361   2014   -175    464       O  
-ATOM   4404  N   PRO B 505      38.095  24.025 -13.053  1.00 25.72           N  
-ANISOU 4404  N   PRO B 505     3468   3714   2591   1676   -153    483       N  
-ATOM   4405  CA  PRO B 505      38.018  23.119 -11.902  1.00 24.25           C  
-ANISOU 4405  CA  PRO B 505     3394   3511   2309   1556   -296    282       C  
-ATOM   4406  C   PRO B 505      38.307  23.818 -10.573  1.00 23.34           C  
-ANISOU 4406  C   PRO B 505     3099   3239   2530   1510     51    219       C  
-ATOM   4407  O   PRO B 505      38.001  23.271  -9.516  1.00 20.81           O  
-ANISOU 4407  O   PRO B 505     2743   2920   2245   1230    128    397       O  
-ATOM   4408  CB  PRO B 505      39.099  22.079 -12.205  1.00 24.61           C  
-ANISOU 4408  CB  PRO B 505     3436   3443   2470   1618    309    -56       C  
-ATOM   4409  CG  PRO B 505      40.055  22.782 -13.104  1.00 25.12           C  
-ANISOU 4409  CG  PRO B 505     3579   3409   2554   1554    151    235       C  
-ATOM   4410  CD  PRO B 505      39.216  23.695 -13.948  1.00 25.21           C  
-ANISOU 4410  CD  PRO B 505     3540   3587   2452   1507    314    392       C  
-ATOM   4411  N   GLN B 506      38.878  25.016 -10.628  1.00 22.21           N  
-ANISOU 4411  N   GLN B 506     3278   3067   2094   1737   -114   -171       N  
-ATOM   4412  CA  GLN B 506      39.221  25.750  -9.416  1.00 24.59           C  
-ANISOU 4412  CA  GLN B 506     3521   3335   2487   2003     27    235       C  
-ATOM   4413  C   GLN B 506      37.992  26.111  -8.585  1.00 25.53           C  
-ANISOU 4413  C   GLN B 506     3640   3391   2670   1906    -88     55       C  
-ATOM   4414  O   GLN B 506      38.097  26.360  -7.383  1.00 26.53           O  
-ANISOU 4414  O   GLN B 506     3870   3373   2837   1857    -53   -121       O  
-ATOM   4415  CB  GLN B 506      40.013  27.013  -9.762  1.00 29.96           C  
-ANISOU 4415  CB  GLN B 506     3851   3693   3840   2134     82    683       C  
-ATOM   4416  CG  GLN B 506      41.306  26.756 -10.519  1.00 34.21           C  
-ANISOU 4416  CG  GLN B 506     4324   4275   4398   2211    -77    885       C  
-ATOM   4417  CD  GLN B 506      41.242  27.127 -11.997  1.00 32.83           C  
-ANISOU 4417  CD  GLN B 506     4238   4548   3686   2376     94    941       C  
-ATOM   4418  OE1 GLN B 506      40.226  26.912 -12.670  1.00 31.84           O  
-ANISOU 4418  OE1 GLN B 506     4264   4714   3118   2022   -412    828       O  
-ATOM   4419  NE2 GLN B 506      42.344  27.684 -12.512  1.00 27.12           N  
-ANISOU 4419  NE2 GLN B 506     3720   3969   2615   2153   1025    924       N  
-ATOM   4420  N   THR B 507      36.829  26.140  -9.229  1.00 25.50           N  
-ANISOU 4420  N   THR B 507     3500   3431   2756   1989    140    502       N  
-ATOM   4421  CA  THR B 507      35.596  26.517  -8.552  1.00 27.63           C  
-ANISOU 4421  CA  THR B 507     3358   3709   3429   1966    162    778       C  
-ATOM   4422  C   THR B 507      34.876  25.324  -7.937  1.00 26.21           C  
-ANISOU 4422  C   THR B 507     3122   3756   3079   1963    371    587       C  
-ATOM   4423  O   THR B 507      33.871  25.484  -7.240  1.00 29.61           O  
-ANISOU 4423  O   THR B 507     3200   4008   4042   1956    866    573       O  
-ATOM   4424  CB  THR B 507      34.627  27.226  -9.519  1.00 31.19           C  
-ANISOU 4424  CB  THR B 507     3599   4089   4161   2135    206    886       C  
-ATOM   4425  OG1 THR B 507      34.210  26.307 -10.539  1.00 33.26           O  
-ANISOU 4425  OG1 THR B 507     3749   4382   4504   2085   -223    806       O  
-ATOM   4426  CG2 THR B 507      35.303  28.426 -10.167  1.00 34.65           C  
-ANISOU 4426  CG2 THR B 507     3829   4334   5000   2278    344    914       C  
-ATOM   4427  N   LEU B 508      35.391  24.124  -8.191  1.00 24.03           N  
-ANISOU 4427  N   LEU B 508     2897   3574   2657   1767    -22    583       N  
-ATOM   4428  CA  LEU B 508      34.770  22.913  -7.670  1.00 21.94           C  
-ANISOU 4428  CA  LEU B 508     2655   3519   2163   1525    161    278       C  
-ATOM   4429  C   LEU B 508      35.100  22.723  -6.192  1.00 20.36           C  
-ANISOU 4429  C   LEU B 508     2415   3359   1961   1329    -40    -44       C  
-ATOM   4430  O   LEU B 508      36.164  23.137  -5.726  1.00 21.98           O  
-ANISOU 4430  O   LEU B 508     2528   3489   2335   1361    -22     80       O  
-ATOM   4431  CB  LEU B 508      35.240  21.690  -8.469  1.00 20.71           C  
-ANISOU 4431  CB  LEU B 508     2544   3444   1879   1361    148   -123       C  
-ATOM   4432  CG  LEU B 508      34.815  21.659  -9.940  1.00 23.36           C  
-ANISOU 4432  CG  LEU B 508     2565   3977   2332   1321   -328      3       C  
-ATOM   4433  CD1 LEU B 508      35.481  20.502 -10.675  1.00 23.92           C  
-ANISOU 4433  CD1 LEU B 508     2922   3885   2279   1427   -130    -60       C  
-ATOM   4434  CD2 LEU B 508      33.295  21.583 -10.065  1.00 27.23           C  
-ANISOU 4434  CD2 LEU B 508     2762   4356   3229   1183    -55   -216       C  
-ATOM   4435  N   PRO B 509      34.184  22.094  -5.445  1.00 20.60           N  
-ANISOU 4435  N   PRO B 509     2041   3458   2329   1317     60   -130       N  
-ATOM   4436  CA  PRO B 509      34.505  21.702  -4.072  1.00 20.16           C  
-ANISOU 4436  CA  PRO B 509     1814   3409   2436   1086   -118    142       C  
-ATOM   4437  C   PRO B 509      35.720  20.779  -4.108  1.00 18.21           C  
-ANISOU 4437  C   PRO B 509     1760   3101   2057   1102    -16   -143       C  
-ATOM   4438  O   PRO B 509      35.917  20.071  -5.097  1.00 19.96           O  
-ANISOU 4438  O   PRO B 509     1843   3286   2455   1097   -263     -3       O  
-ATOM   4439  CB  PRO B 509      33.262  20.925  -3.628  1.00 23.16           C  
-ANISOU 4439  CB  PRO B 509     1890   3729   3181    998     25    431       C  
-ATOM   4440  CG  PRO B 509      32.173  21.355  -4.563  1.00 26.10           C  
-ANISOU 4440  CG  PRO B 509     2463   3950   3503   1141   -135    138       C  
-ATOM   4441  CD  PRO B 509      32.852  21.626  -5.863  1.00 23.71           C  
-ANISOU 4441  CD  PRO B 509     2230   3797   2981   1172    121    217       C  
-ATOM   4442  N   ILE B 510      36.521  20.787  -3.050  1.00 16.84           N  
-ANISOU 4442  N   ILE B 510     1290   2897   2212    862    -34    339       N  
-ATOM   4443  CA  ILE B 510      37.756  20.009  -3.052  1.00 16.76           C  
-ANISOU 4443  CA  ILE B 510     1362   2848   2157    775    -63    383       C  
-ATOM   4444  C   ILE B 510      37.622  18.659  -2.348  1.00 16.66           C  
-ANISOU 4444  C   ILE B 510     1412   3031   1886    702    144    139       C  
-ATOM   4445  O   ILE B 510      38.604  17.922  -2.227  1.00 17.55           O  
-ANISOU 4445  O   ILE B 510     1403   2979   2286    758    -31    370       O  
-ATOM   4446  CB  ILE B 510      38.931  20.802  -2.438  1.00 16.36           C  
-ANISOU 4446  CB  ILE B 510     1791   2932   1493    628     -9    254       C  
-ATOM   4447  CG1 ILE B 510      38.672  21.089  -0.960  1.00 17.91           C  
-ANISOU 4447  CG1 ILE B 510     1701   3245   1858    568   -243     -4       C  
-ATOM   4448  CG2 ILE B 510      39.165  22.096  -3.219  1.00 19.44           C  
-ANISOU 4448  CG2 ILE B 510     2257   3142   1987    752    -69    757       C  
-ATOM   4449  CD1 ILE B 510      39.871  21.679  -0.247  1.00 19.39           C  
-ANISOU 4449  CD1 ILE B 510     2179   3296   1890    623   -255    180       C  
-ATOM   4450  N   ASN B 511      36.411  18.330  -1.902  1.00 17.65           N  
-ANISOU 4450  N   ASN B 511     1630   3114   1961    590    -83    317       N  
-ATOM   4451  CA  ASN B 511      36.181  17.087  -1.168  1.00 19.19           C  
-ANISOU 4451  CA  ASN B 511     1754   3234   2302    413    281    205       C  
-ATOM   4452  C   ASN B 511      35.477  16.011  -1.993  1.00 19.38           C  
-ANISOU 4452  C   ASN B 511     1617   3229   2517    369    -54    302       C  
-ATOM   4453  O   ASN B 511      34.909  15.063  -1.448  1.00 19.14           O  
-ANISOU 4453  O   ASN B 511     1712   3221   2340    259   -206    299       O  
-ATOM   4454  CB  ASN B 511      35.416  17.353   0.133  1.00 21.64           C  
-ANISOU 4454  CB  ASN B 511     1989   3703   2530    639    706    322       C  
-ATOM   4455  CG  ASN B 511      34.002  17.849  -0.109  1.00 24.29           C  
-ANISOU 4455  CG  ASN B 511     2163   4066   2998    715   1028    414       C  
-ATOM   4456  OD1 ASN B 511      33.678  18.338  -1.190  1.00 24.02           O  
-ANISOU 4456  OD1 ASN B 511     2018   4053   3055    557    707    -80       O  
-ATOM   4457  ND2 ASN B 511      33.155  17.729   0.906  1.00 28.00           N  
-ANISOU 4457  ND2 ASN B 511     2547   4373   3718    882   1092    798       N  
-ATOM   4458  N   GLY B 512      35.521  16.165  -3.311  1.00 17.83           N  
-ANISOU 4458  N   GLY B 512     1429   3034   2309    406   -129     57       N  
-ATOM   4459  CA  GLY B 512      34.930  15.195  -4.211  1.00 17.62           C  
-ANISOU 4459  CA  GLY B 512     1342   2921   2432    388   -214    261       C  
-ATOM   4460  C   GLY B 512      35.792  13.959  -4.394  1.00 16.22           C  
-ANISOU 4460  C   GLY B 512     1359   2770   2034    131   -435    219       C  
-ATOM   4461  O   GLY B 512      36.969  13.926  -4.005  1.00 17.11           O  
-ANISOU 4461  O   GLY B 512     1527   2716   2256    128   -482    353       O  
-ATOM   4462  N   VAL B 513      35.200  12.942  -5.007  1.00 17.17           N  
-ANISOU 4462  N   VAL B 513     1428   2841   2256    -14   -179    271       N  
-ATOM   4463  CA  VAL B 513      35.884  11.686  -5.263  1.00 17.82           C  
-ANISOU 4463  CA  VAL B 513     1655   2852   2264   -296   -146    493       C  
-ATOM   4464  C   VAL B 513      35.908  11.408  -6.761  1.00 16.85           C  
-ANISOU 4464  C   VAL B 513     1469   2805   2127   -216    -53    595       C  
-ATOM   4465  O   VAL B 513      34.877  11.481  -7.429  1.00 17.75           O  
-ANISOU 4465  O   VAL B 513     1273   3115   2357   -183   -354    331       O  
-ATOM   4466  CB  VAL B 513      35.178  10.529  -4.534  1.00 19.96           C  
-ANISOU 4466  CB  VAL B 513     1986   3201   2398   -330   -105    764       C  
-ATOM   4467  CG1 VAL B 513      35.822   9.194  -4.895  1.00 21.46           C  
-ANISOU 4467  CG1 VAL B 513     2323   2993   2837   -201   -100   1033       C  
-ATOM   4468  CG2 VAL B 513      35.214  10.759  -3.030  1.00 19.63           C  
-ANISOU 4468  CG2 VAL B 513     2183   3375   1898   -350   -131    691       C  
-ATOM   4469  N   PHE B 514      37.083  11.101  -7.298  1.00 15.61           N  
-ANISOU 4469  N   PHE B 514     1353   2648   1930     26    -51    377       N  
-ATOM   4470  CA  PHE B 514      37.175  10.750  -8.706  1.00 15.52           C  
-ANISOU 4470  CA  PHE B 514     1364   2302   2231   -126     46    356       C  
-ATOM   4471  C   PHE B 514      36.749   9.308  -8.891  1.00 15.58           C  
-ANISOU 4471  C   PHE B 514     1435   2355   2129   -323   -395    374       C  
-ATOM   4472  O   PHE B 514      37.117   8.437  -8.099  1.00 16.21           O  
-ANISOU 4472  O   PHE B 514     1571   2392   2195   -132   -227    384       O  
-ATOM   4473  CB  PHE B 514      38.596  10.936  -9.235  1.00 15.38           C  
-ANISOU 4473  CB  PHE B 514     1341   2305   2197    -24     22    418       C  
-ATOM   4474  CG  PHE B 514      39.043  12.366  -9.290  1.00 14.80           C  
-ANISOU 4474  CG  PHE B 514     1369   2215   2037     70   -239    372       C  
-ATOM   4475  CD1 PHE B 514      38.776  13.144 -10.409  1.00 14.74           C  
-ANISOU 4475  CD1 PHE B 514     1334   2246   2020    -94   -263     49       C  
-ATOM   4476  CD2 PHE B 514      39.734  12.933  -8.232  1.00 16.12           C  
-ANISOU 4476  CD2 PHE B 514     1136   2331   2659     43   -276   -179       C  
-ATOM   4477  CE1 PHE B 514      39.185  14.463 -10.469  1.00 16.43           C  
-ANISOU 4477  CE1 PHE B 514     1355   2119   2769    -50    -42    267       C  
-ATOM   4478  CE2 PHE B 514      40.153  14.250  -8.284  1.00 15.84           C  
-ANISOU 4478  CE2 PHE B 514     1308   2510   2200    224    -88    345       C  
-ATOM   4479  CZ  PHE B 514      39.875  15.019  -9.401  1.00 16.19           C  
-ANISOU 4479  CZ  PHE B 514     1380   2351   2421     48     -4   -159       C  
-ATOM   4480  N   VAL B 515      35.966   9.059  -9.936  1.00 15.93           N  
-ANISOU 4480  N   VAL B 515     1504   2511   2036   -383   -325    -67       N  
-ATOM   4481  CA  VAL B 515      35.488   7.716 -10.231  1.00 17.65           C  
-ANISOU 4481  CA  VAL B 515     1699   2830   2177   -550    -54    108       C  
-ATOM   4482  C   VAL B 515      35.691   7.410 -11.708  1.00 17.39           C  
-ANISOU 4482  C   VAL B 515     1712   2560   2335   -525   -229    146       C  
-ATOM   4483  O   VAL B 515      35.275   8.188 -12.564  1.00 17.22           O  
-ANISOU 4483  O   VAL B 515     1675   2634   2232   -252   -264    497       O  
-ATOM   4484  CB  VAL B 515      33.986   7.570  -9.891  1.00 20.51           C  
-ANISOU 4484  CB  VAL B 515     2032   3203   2556   -739    238     39       C  
-ATOM   4485  CG1 VAL B 515      33.518   6.150 -10.154  1.00 21.10           C  
-ANISOU 4485  CG1 VAL B 515     2275   3216   2525   -959     50   -169       C  
-ATOM   4486  CG2 VAL B 515      33.724   7.954  -8.437  1.00 21.86           C  
-ANISOU 4486  CG2 VAL B 515     2064   3563   2678   -581    361    472       C  
-ATOM   4487  N   PHE B 516      36.343   6.285 -11.997  1.00 16.64           N  
-ANISOU 4487  N   PHE B 516     1828   2445   2050   -584   -402    264       N  
-ATOM   4488  CA  PHE B 516      36.507   5.803 -13.364  1.00 17.83           C  
-ANISOU 4488  CA  PHE B 516     1926   2545   2304   -696   -615    255       C  
-ATOM   4489  C   PHE B 516      35.175   5.325 -13.931  1.00 19.68           C  
-ANISOU 4489  C   PHE B 516     2156   2818   2502   -824   -512    652       C  
-ATOM   4490  O   PHE B 516      34.511   4.464 -13.343  1.00 21.49           O  
-ANISOU 4490  O   PHE B 516     2443   3155   2567   -950   -509    410       O  
-ATOM   4491  CB  PHE B 516      37.528   4.665 -13.407  1.00 18.38           C  
-ANISOU 4491  CB  PHE B 516     2264   2329   2391   -227   -661    270       C  
-ATOM   4492  CG  PHE B 516      37.647   3.998 -14.749  1.00 18.69           C  
-ANISOU 4492  CG  PHE B 516     2432   2220   2447   -314   -637    423       C  
-ATOM   4493  CD1 PHE B 516      38.125   4.692 -15.847  1.00 19.24           C  
-ANISOU 4493  CD1 PHE B 516     2291   2522   2495   -371   -891     23       C  
-ATOM   4494  CD2 PHE B 516      37.316   2.663 -14.903  1.00 19.13           C  
-ANISOU 4494  CD2 PHE B 516     2828   2101   2337   -318   -685    176       C  
-ATOM   4495  CE1 PHE B 516      38.253   4.074 -17.078  1.00 19.16           C  
-ANISOU 4495  CE1 PHE B 516     2363   2399   2518   -509   -847     71       C  
-ATOM   4496  CE2 PHE B 516      37.443   2.034 -16.129  1.00 19.30           C  
-ANISOU 4496  CE2 PHE B 516     2900   2212   2221   -281   -582    383       C  
-ATOM   4497  CZ  PHE B 516      37.911   2.744 -17.221  1.00 19.28           C  
-ANISOU 4497  CZ  PHE B 516     2692   2358   2274   -348   -715   -183       C  
-ATOM   4498  N   ILE B 517      34.791   5.891 -15.070  1.00 18.60           N  
-ANISOU 4498  N   ILE B 517     1869   2825   2374   -878   -839    552       N  
-ATOM   4499  CA  ILE B 517      33.534   5.552 -15.721  1.00 20.10           C  
-ANISOU 4499  CA  ILE B 517     2056   3048   2534   -757   -733    426       C  
-ATOM   4500  C   ILE B 517      33.758   4.568 -16.861  1.00 20.07           C  
-ANISOU 4500  C   ILE B 517     2201   2958   2467  -1194   -648    324       C  
-ATOM   4501  O   ILE B 517      33.114   3.521 -16.929  1.00 22.80           O  
-ANISOU 4501  O   ILE B 517     2530   3185   2949   -976   -628    336       O  
-ATOM   4502  CB  ILE B 517      32.865   6.810 -16.288  1.00 20.75           C  
-ANISOU 4502  CB  ILE B 517     1797   3537   2551   -525   -877    288       C  
-ATOM   4503  CG1 ILE B 517      32.634   7.838 -15.177  1.00 20.96           C  
-ANISOU 4503  CG1 ILE B 517     1904   3571   2489   -544   -525    342       C  
-ATOM   4504  CG2 ILE B 517      31.553   6.458 -16.977  1.00 21.76           C  
-ANISOU 4504  CG2 ILE B 517     1601   3782   2885   -522   -817    469       C  
-ATOM   4505  CD1 ILE B 517      31.815   7.308 -14.012  1.00 22.82           C  
-ANISOU 4505  CD1 ILE B 517     1984   3795   2889   -337   -327    364       C  
-ATOM   4506  N   SER B 518      34.675   4.905 -17.760  1.00 19.94           N  
-ANISOU 4506  N   SER B 518     2239   3070   2268  -1068   -632    119       N  
-ATOM   4507  CA  SER B 518      34.880   4.100 -18.951  1.00 20.71           C  
-ANISOU 4507  CA  SER B 518     2366   3239   2263  -1159   -762    143       C  
-ATOM   4508  C   SER B 518      36.138   4.474 -19.713  1.00 20.51           C  
-ANISOU 4508  C   SER B 518     2524   2945   2322   -908   -569    350       C  
-ATOM   4509  O   SER B 518      36.616   5.605 -19.636  1.00 20.02           O  
-ANISOU 4509  O   SER B 518     2539   2777   2290   -774   -530    222       O  
-ATOM   4510  CB  SER B 518      33.684   4.263 -19.890  1.00 23.91           C  
-ANISOU 4510  CB  SER B 518     2655   4005   2423   -972   -711   -724       C  
-ATOM   4511  OG  SER B 518      33.863   3.493 -21.060  1.00 29.61           O  
-ANISOU 4511  OG  SER B 518     2996   4723   3531   -581   -759   -166       O  
-ATOM   4512  N   TRP B 519      36.664   3.513 -20.464  1.00 20.69           N  
-ANISOU 4512  N   TRP B 519     2584   2918   2357   -649   -491    332       N  
-ATOM   4513  CA  TRP B 519      37.676   3.821 -21.463  1.00 20.04           C  
-ANISOU 4513  CA  TRP B 519     2607   2647   2358   -655   -953      2       C  
-ATOM   4514  C   TRP B 519      36.996   4.512 -22.634  1.00 20.61           C  
-ANISOU 4514  C   TRP B 519     2719   2789   2322   -654   -780    171       C  
-ATOM   4515  O   TRP B 519      35.946   4.068 -23.103  1.00 23.61           O  
-ANISOU 4515  O   TRP B 519     2672   3225   3072   -739   -989    335       O  
-ATOM   4516  CB  TRP B 519      38.398   2.556 -21.932  1.00 20.69           C  
-ANISOU 4516  CB  TRP B 519     2809   2555   2495   -455   -650    -80       C  
-ATOM   4517  CG  TRP B 519      39.255   1.941 -20.867  1.00 20.04           C  
-ANISOU 4517  CG  TRP B 519     3020   2454   2141   -309   -638    331       C  
-ATOM   4518  CD1 TRP B 519      39.012   0.786 -20.179  1.00 22.29           C  
-ANISOU 4518  CD1 TRP B 519     3235   2578   2656   -131   -618    170       C  
-ATOM   4519  CD2 TRP B 519      40.485   2.459 -20.355  1.00 19.68           C  
-ANISOU 4519  CD2 TRP B 519     2938   2346   2192   -301   -844     94       C  
-ATOM   4520  NE1 TRP B 519      40.023   0.548 -19.278  1.00 23.08           N  
-ANISOU 4520  NE1 TRP B 519     3168   2601   2998   -188   -758     -9       N  
-ATOM   4521  CE2 TRP B 519      40.938   1.565 -19.364  1.00 20.59           C  
-ANISOU 4521  CE2 TRP B 519     3004   2269   2550   -320   -751    272       C  
-ATOM   4522  CE3 TRP B 519      41.252   3.593 -20.642  1.00 19.50           C  
-ANISOU 4522  CE3 TRP B 519     2828   2208   2372   -245   -692   -154       C  
-ATOM   4523  CZ2 TRP B 519      42.123   1.767 -18.662  1.00 20.72           C  
-ANISOU 4523  CZ2 TRP B 519     2960   2395   2517    -50   -784    111       C  
-ATOM   4524  CZ3 TRP B 519      42.423   3.798 -19.936  1.00 20.32           C  
-ANISOU 4524  CZ3 TRP B 519     2825   2403   2491    -52   -540   -108       C  
-ATOM   4525  CH2 TRP B 519      42.850   2.887 -18.961  1.00 20.70           C  
-ANISOU 4525  CH2 TRP B 519     2831   2361   2672    -33   -602    120       C  
-ATOM   4526  N   VAL B 520      37.591   5.608 -23.088  1.00 20.08           N  
-ANISOU 4526  N   VAL B 520     2862   2679   2086   -593   -762    414       N  
-ATOM   4527  CA  VAL B 520      37.059   6.353 -24.217  1.00 21.51           C  
-ANISOU 4527  CA  VAL B 520     2959   2912   2303   -662   -795    331       C  
-ATOM   4528  C   VAL B 520      38.161   6.703 -25.206  1.00 21.16           C  
-ANISOU 4528  C   VAL B 520     3267   2895   1879   -494   -708    456       C  
-ATOM   4529  O   VAL B 520      39.358   6.540 -24.925  1.00 22.09           O  
-ANISOU 4529  O   VAL B 520     3289   2822   2281   -264   -401    358       O  
-ATOM   4530  CB  VAL B 520      36.340   7.655 -23.774  1.00 22.16           C  
-ANISOU 4530  CB  VAL B 520     2865   3110   2445   -841   -701    229       C  
-ATOM   4531  CG1 VAL B 520      35.156   7.333 -22.866  1.00 23.32           C  
-ANISOU 4531  CG1 VAL B 520     2933   3323   2605   -782   -508    401       C  
-ATOM   4532  CG2 VAL B 520      37.314   8.606 -23.077  1.00 20.74           C  
-ANISOU 4532  CG2 VAL B 520     2884   2896   2101   -816   -490     41       C  
-ATOM   4533  N   SER B 521      37.741   7.191 -26.366  1.00 22.87           N  
-ANISOU 4533  N   SER B 521     3620   2908   2159   -449   -648    299       N  
-ATOM   4534  CA  SER B 521      38.653   7.657 -27.392  1.00 23.53           C  
-ANISOU 4534  CA  SER B 521     3786   3153   2002   -527   -663    123       C  
-ATOM   4535  C   SER B 521      39.448   8.865 -26.899  1.00 22.33           C  
-ANISOU 4535  C   SER B 521     3563   3139   1783   -510   -468    358       C  
-ATOM   4536  O   SER B 521      38.980   9.620 -26.045  1.00 21.61           O  
-ANISOU 4536  O   SER B 521     3410   3017   1784   -445   -484    106       O  
-ATOM   4537  CB  SER B 521      37.855   8.032 -28.641  1.00 25.98           C  
-ANISOU 4537  CB  SER B 521     4074   3487   2311   -731   -940      9       C  
-ATOM   4538  OG  SER B 521      38.650   8.764 -29.541  1.00 27.92           O  
-ANISOU 4538  OG  SER B 521     4317   3300   2989   -741  -1081    275       O  
-ATOM   4539  N   ARG B 522      40.649   9.054 -27.440  1.00 22.20           N  
-ANISOU 4539  N   ARG B 522     3419   3216   1801   -366   -462    111       N  
-ATOM   4540  CA  ARG B 522      41.440  10.227 -27.094  1.00 25.29           C  
-ANISOU 4540  CA  ARG B 522     3569   3300   2738   -172   -255     26       C  
-ATOM   4541  C   ARG B 522      40.714  11.480 -27.564  1.00 22.99           C  
-ANISOU 4541  C   ARG B 522     3421   3177   2136   -303   -203     55       C  
-ATOM   4542  O   ARG B 522      41.019  12.587 -27.121  1.00 23.84           O  
-ANISOU 4542  O   ARG B 522     3481   3001   2574   -269   -223   -373       O  
-ATOM   4543  CB  ARG B 522      42.842  10.155 -27.711  1.00 31.75           C  
-ANISOU 4543  CB  ARG B 522     4004   3889   4168    185     38    418       C  
-ATOM   4544  CG  ARG B 522      42.869  10.233 -29.227  1.00 38.54           C  
-ANISOU 4544  CG  ARG B 522     4499   4426   5716    531    241    444       C  
-ATOM   4545  CD  ARG B 522      44.289  10.095 -29.761  1.00 44.82           C  
-ANISOU 4545  CD  ARG B 522     5078   4873   7076    970    176    540       C  
-ATOM   4546  NE  ARG B 522      45.143  11.206 -29.353  1.00 49.07           N  
-ANISOU 4546  NE  ARG B 522     5577   5280   7785   1396     48    747       N  
-ATOM   4547  CZ  ARG B 522      45.553  12.176 -30.165  1.00 51.53           C  
-ANISOU 4547  CZ  ARG B 522     5930   5682   7965   1827   -211    781       C  
-ATOM   4548  NH1 ARG B 522      45.199  12.178 -31.443  1.00 51.67           N  
-ANISOU 4548  NH1 ARG B 522     6078   5771   7783   2022   -250    815       N  
-ATOM   4549  NH2 ARG B 522      46.328  13.145 -29.698  1.00 53.12           N  
-ANISOU 4549  NH2 ARG B 522     6089   5733   8359   2031   -244    762       N  
-ATOM   4550  N   TYR B 523      39.740  11.291 -28.453  1.00 21.72           N  
-ANISOU 4550  N   TYR B 523     3221   3031   2000   -335   -158    270       N  
-ATOM   4551  CA  TYR B 523      39.001  12.402 -29.040  1.00 20.73           C  
-ANISOU 4551  CA  TYR B 523     3100   3031   1743   -338   -130    161       C  
-ATOM   4552  C   TYR B 523      37.662  12.636 -28.356  1.00 22.25           C  
-ANISOU 4552  C   TYR B 523     3048   3194   2212   -140   -141    325       C  
-ATOM   4553  O   TYR B 523      36.866  13.465 -28.803  1.00 24.30           O  
-ANISOU 4553  O   TYR B 523     3177   3609   2445    306    -53    304       O  
-ATOM   4554  CB  TYR B 523      38.777  12.153 -30.532  1.00 22.14           C  
-ANISOU 4554  CB  TYR B 523     3185   3143   2082   -195   -142    257       C  
-ATOM   4555  CG  TYR B 523      40.038  11.785 -31.275  1.00 24.37           C  
-ANISOU 4555  CG  TYR B 523     3376   3534   2350     69     27    495       C  
-ATOM   4556  CD1 TYR B 523      40.292  10.467 -31.636  1.00 27.01           C  
-ANISOU 4556  CD1 TYR B 523     3481   3727   3055    109     31    520       C  
-ATOM   4557  CD2 TYR B 523      40.978  12.749 -31.608  1.00 25.53           C  
-ANISOU 4557  CD2 TYR B 523     3375   3805   2519     99    120    739       C  
-ATOM   4558  CE1 TYR B 523      41.445  10.121 -32.317  1.00 27.11           C  
-ANISOU 4558  CE1 TYR B 523     3567   3903   2830    182     62    326       C  
-ATOM   4559  CE2 TYR B 523      42.137  12.412 -32.287  1.00 27.88           C  
-ANISOU 4559  CE2 TYR B 523     3460   4075   3059    324    177    651       C  
-ATOM   4560  CZ  TYR B 523      42.364  11.096 -32.638  1.00 28.93           C  
-ANISOU 4560  CZ  TYR B 523     3579   4065   3349    271    370    711       C  
-ATOM   4561  OH  TYR B 523      43.511  10.756 -33.315  1.00 33.10           O  
-ANISOU 4561  OH  TYR B 523     3799   4402   4375    473    464    697       O  
-ATOM   4562  N   TYR B 524      37.413  11.901 -27.277  1.00 21.27           N  
-ANISOU 4562  N   TYR B 524     2923   3046   2112   -137   -117    299       N  
-ATOM   4563  CA  TYR B 524      36.172  12.052 -26.527  1.00 22.01           C  
-ANISOU 4563  CA  TYR B 524     2911   3357   2095    279   -272    586       C  
-ATOM   4564  C   TYR B 524      35.937  13.510 -26.147  1.00 23.37           C  
-ANISOU 4564  C   TYR B 524     3008   3461   2411    547   -361    333       C  
-ATOM   4565  O   TYR B 524      36.830  14.181 -25.621  1.00 23.05           O  
-ANISOU 4565  O   TYR B 524     3092   3181   2484    660   -611     83       O  
-ATOM   4566  CB  TYR B 524      36.191  11.174 -25.279  1.00 23.39           C  
-ANISOU 4566  CB  TYR B 524     2825   3881   2180    133   -230   1101       C  
-ATOM   4567  CG  TYR B 524      34.909  11.215 -24.482  1.00 26.96           C  
-ANISOU 4567  CG  TYR B 524     2875   4751   2616    416   -132   1144       C  
-ATOM   4568  CD1 TYR B 524      33.862  10.351 -24.773  1.00 28.68           C  
-ANISOU 4568  CD1 TYR B 524     2826   5028   3044    380   -183   1243       C  
-ATOM   4569  CD2 TYR B 524      34.745  12.113 -23.433  1.00 27.99           C  
-ANISOU 4569  CD2 TYR B 524     2933   5171   2532    517   -170   1039       C  
-ATOM   4570  CE1 TYR B 524      32.687  10.384 -24.048  1.00 31.42           C  
-ANISOU 4570  CE1 TYR B 524     2940   5360   3639    379    -91   1200       C  
-ATOM   4571  CE2 TYR B 524      33.570  12.154 -22.703  1.00 29.87           C  
-ANISOU 4571  CE2 TYR B 524     2991   5520   2839    453     17   1333       C  
-ATOM   4572  CZ  TYR B 524      32.546  11.285 -23.014  1.00 31.81           C  
-ANISOU 4572  CZ  TYR B 524     2990   5641   3454    427    207   1436       C  
-ATOM   4573  OH  TYR B 524      31.375  11.320 -22.288  1.00 34.93           O  
-ANISOU 4573  OH  TYR B 524     3233   5971   4066    748    118   1620       O  
-ATOM   4574  N   GLN B 525      34.725  13.990 -26.404  1.00 24.00           N  
-ANISOU 4574  N   GLN B 525     2999   3737   2384    698   -595    580       N  
-ATOM   4575  CA  GLN B 525      34.377  15.387 -26.163  1.00 23.74           C  
-ANISOU 4575  CA  GLN B 525     2751   3938   2329    741   -588    646       C  
-ATOM   4576  C   GLN B 525      33.813  15.617 -24.765  1.00 24.83           C  
-ANISOU 4576  C   GLN B 525     2626   4120   2688    724   -436    493       C  
-ATOM   4577  O   GLN B 525      32.720  15.146 -24.442  1.00 25.57           O  
-ANISOU 4577  O   GLN B 525     2633   4189   2892    540   -302    318       O  
-ATOM   4578  CB  GLN B 525      33.365  15.858 -27.209  1.00 26.49           C  
-ANISOU 4578  CB  GLN B 525     2954   4197   2913    985   -689    661       C  
-ATOM   4579  CG  GLN B 525      32.911  17.296 -27.037  1.00 27.11           C  
-ANISOU 4579  CG  GLN B 525     3144   4294   2861    959   -243    939       C  
-ATOM   4580  CD  GLN B 525      34.030  18.289 -27.276  1.00 28.55           C  
-ANISOU 4580  CD  GLN B 525     3338   4656   2853   1181    117   1068       C  
-ATOM   4581  OE1 GLN B 525      34.537  18.414 -28.393  1.00 30.32           O  
-ANISOU 4581  OE1 GLN B 525     3454   4802   3262   1163    438   1065       O  
-ATOM   4582  NE2 GLN B 525      34.425  19.000 -26.224  1.00 27.89           N  
-ANISOU 4582  NE2 GLN B 525     3311   4557   2730   1178    -83    918       N  
-ATOM   4583  N   LEU B 526      34.561  16.346 -23.943  1.00 23.09           N  
-ANISOU 4583  N   LEU B 526     2562   3969   2240    846   -279    202       N  
-ATOM   4584  CA  LEU B 526      34.100  16.744 -22.618  1.00 24.98           C  
-ANISOU 4584  CA  LEU B 526     2624   4250   2615   1048   -347    323       C  
-ATOM   4585  C   LEU B 526      33.133  17.914 -22.722  1.00 27.68           C  
-ANISOU 4585  C   LEU B 526     2769   4585   3161   1200   -235    455       C  
-ATOM   4586  O   LEU B 526      33.167  18.663 -23.700  1.00 28.71           O  
-ANISOU 4586  O   LEU B 526     2900   4687   3320   1237   -182    391       O  
-ATOM   4587  CB  LEU B 526      35.284  17.145 -21.739  1.00 23.57           C  
-ANISOU 4587  CB  LEU B 526     2573   3932   2451    971   -828    260       C  
-ATOM   4588  CG  LEU B 526      36.226  16.020 -21.312  1.00 24.68           C  
-ANISOU 4588  CG  LEU B 526     2718   3780   2879    967   -537    523       C  
-ATOM   4589  CD1 LEU B 526      37.471  16.585 -20.645  1.00 24.52           C  
-ANISOU 4589  CD1 LEU B 526     2712   3739   2865    755   -758   -192       C  
-ATOM   4590  CD2 LEU B 526      35.494  15.069 -20.385  1.00 28.34           C  
-ANISOU 4590  CD2 LEU B 526     3011   3963   3792   1023   -351    666       C  
-ATOM   4591  OXT LEU B 526      32.303  18.142 -21.840  1.00 29.60           O  
-ANISOU 4591  OXT LEU B 526     2873   4720   3654   1334     -3    645       O  
-TER    4592      LEU B 526                                                      
-HETATM 4593  C1  FUC A 601      67.706  19.121  23.349  1.00 24.62           C  
-ANISOU 4593  C1  FUC A 601     2724   2866   3765    285   -727   -958       C  
-HETATM 4594  C2  FUC A 601      67.568  20.445  22.724  1.00 22.35           C  
-ANISOU 4594  C2  FUC A 601     2710   2312   3469    -42   -621  -1240       C  
-HETATM 4595  C3  FUC A 601      68.677  21.337  23.131  1.00 23.65           C  
-ANISOU 4595  C3  FUC A 601     2766   2538   3681    -27   -261   -919       C  
-HETATM 4596  C4  FUC A 601      70.015  20.759  22.839  1.00 23.99           C  
-ANISOU 4596  C4  FUC A 601     2832   2705   3579    -29   -378  -1117       C  
-HETATM 4597  C5  FUC A 601      70.154  19.347  23.378  1.00 23.99           C  
-ANISOU 4597  C5  FUC A 601     2582   2754   3779     79   -647   -945       C  
-HETATM 4598  C6  FUC A 601      71.430  18.717  22.970  1.00 24.53           C  
-ANISOU 4598  C6  FUC A 601     2550   2860   3910    279   -553  -1207       C  
-HETATM 4599  O2  FUC A 601      66.343  21.006  23.103  1.00 25.32           O  
-ANISOU 4599  O2  FUC A 601     2512   2529   4577      7    -52   -854       O  
-HETATM 4600  O3  FUC A 601      68.540  22.590  22.540  1.00 25.54           O  
-ANISOU 4600  O3  FUC A 601     3110   2236   4359     57    184   -409       O  
-HETATM 4601  O4  FUC A 601      70.230  20.749  21.469  1.00 24.68           O  
-ANISOU 4601  O4  FUC A 601     2996   2851   3528    153   -286   -840       O  
-HETATM 4602  O5  FUC A 601      69.051  18.516  23.001  1.00 23.73           O  
-ANISOU 4602  O5  FUC A 601     2542   2958   3516     12   -946  -1220       O  
-HETATM 4603  C1  GAL A 602      68.410  17.849  26.467  1.00 22.16           C  
-ANISOU 4603  C1  GAL A 602     2615   3291   2513    187   -911   -325       C  
-HETATM 4604  C2  GAL A 602      67.395  17.981  25.353  1.00 21.49           C  
-ANISOU 4604  C2  GAL A 602     2659   3056   2451    214  -1011   -354       C  
-HETATM 4605  C3  GAL A 602      66.003  17.850  25.852  1.00 19.57           C  
-ANISOU 4605  C3  GAL A 602     2415   2626   2395     89   -961   -297       C  
-HETATM 4606  C4  GAL A 602      65.818  16.666  26.619  1.00 19.39           C  
-ANISOU 4606  C4  GAL A 602     2671   2644   2053    345   -776   -376       C  
-HETATM 4607  C5  GAL A 602      66.808  16.630  27.738  1.00 20.68           C  
-ANISOU 4607  C5  GAL A 602     2863   2938   2056    342  -1036   -172       C  
-HETATM 4608  C6  GAL A 602      66.738  15.436  28.577  1.00 22.62           C  
-ANISOU 4608  C6  GAL A 602     3084   3369   2142    379  -1404   -343       C  
-HETATM 4609  O2  GAL A 602      67.578  19.246  24.723  1.00 25.31           O  
-ANISOU 4609  O2  GAL A 602     2852   3017   3747    298   -985   -160       O  
-HETATM 4610  O3  GAL A 602      65.080  17.921  24.747  1.00 18.79           O  
-ANISOU 4610  O3  GAL A 602     2034   2158   2947    -37   -768   -454       O  
-HETATM 4611  O4  GAL A 602      65.966  15.489  25.761  1.00 18.29           O  
-ANISOU 4611  O4  GAL A 602     2544   2485   1920    393   -699   -817       O  
-HETATM 4612  O5  GAL A 602      68.196  16.707  27.204  1.00 21.82           O  
-ANISOU 4612  O5  GAL A 602     2695   3059   2535    407   -858   -750       O  
-HETATM 4613  O6  GAL A 602      67.520  15.432  29.678  1.00 26.12           O  
-ANISOU 4613  O6  GAL A 602     3572   3464   2887    620  -1214   -262       O  
-HETATM 4614  C1  NDG A 603      73.423  18.443  27.730  1.00 41.48           C  
-ANISOU 4614  C1  NDG A 603     4017   5777   5966    337  -2068   -539       C  
-HETATM 4615  C2  NDG A 603      72.728  17.092  27.855  1.00 38.85           C  
-ANISOU 4615  C2  NDG A 603     3833   5595   5334    251  -2485   -978       C  
-HETATM 4616  C3  NDG A 603      71.735  16.951  26.811  1.00 32.56           C  
-ANISOU 4616  C3  NDG A 603     3134   4872   4364     26  -1920  -1043       C  
-HETATM 4617  C4  NDG A 603      70.780  17.984  26.915  1.00 31.06           C  
-ANISOU 4617  C4  NDG A 603     3102   4698   4002     45  -1867   -941       C  
-HETATM 4618  C5  NDG A 603      71.447  19.356  26.799  1.00 35.85           C  
-ANISOU 4618  C5  NDG A 603     3459   5221   4942    123  -2139  -1109       C  
-HETATM 4619  C6  NDG A 603      70.466  20.440  27.010  1.00 38.37           C  
-ANISOU 4619  C6  NDG A 603     3848   5263   5466    401  -1790  -1366       C  
-HETATM 4620  C7  NDG A 603      73.865  15.060  28.901  1.00 49.82           C  
-ANISOU 4620  C7  NDG A 603     5078   6670   7179   1302  -2356   -366       C  
-HETATM 4621  C8  NDG A 603      74.797  14.023  28.811  1.00 50.74           C  
-ANISOU 4621  C8  NDG A 603     5065   6876   7336   1453  -2698   -171       C  
-HETATM 4622  O   NDG A 603      72.502  19.497  27.770  1.00 38.39           O  
-ANISOU 4622  O   NDG A 603     3619   5465   5501    -71  -2335  -1101       O  
-HETATM 4623  O3  NDG A 603      71.089  15.591  26.872  1.00 29.57           O  
-ANISOU 4623  O3  NDG A 603     2707   4731   3797    416  -1524  -1297       O  
-HETATM 4624  O4  NDG A 603      69.704  17.827  25.936  1.00 26.40           O  
-ANISOU 4624  O4  NDG A 603     2654   3861   3516   -144  -1028   -868       O  
-HETATM 4625  O6  NDG A 603      69.853  20.518  28.331  1.00 39.82           O  
-ANISOU 4625  O6  NDG A 603     4148   5321   5661    430  -1796  -1870       O  
-HETATM 4626  O7  NDG A 603      73.182  15.177  29.925  1.00 52.09           O  
-ANISOU 4626  O7  NDG A 603     5412   6876   7502   1312  -2138   -256       O  
-HETATM 4627  N2  NDG A 603      73.705  15.989  27.795  1.00 44.84           N  
-ANISOU 4627  N2  NDG A 603     4579   6132   6326    927  -2392   -577       N  
-HETATM 4628  O1L NDG A 603      74.122  18.499  26.569  1.00 44.68           O  
-ANISOU 4628  O1L NDG A 603     4399   6058   6517    630  -1848   -200       O  
-HETATM 4629  C1  FUC A 604      71.586  14.627  25.969  1.00 27.36           C  
-ANISOU 4629  C1  FUC A 604     2327   4719   3350    469  -1327   -854       C  
-HETATM 4630  C2  FUC A 604      71.158  13.268  26.456  1.00 25.99           C  
-ANISOU 4630  C2  FUC A 604     2325   4551   2998    740  -1248   -618       C  
-HETATM 4631  C3  FUC A 604      69.687  13.173  26.454  1.00 24.76           C  
-ANISOU 4631  C3  FUC A 604     2400   4289   2717    681  -1233   -765       C  
-HETATM 4632  C4  FUC A 604      69.130  13.446  25.160  1.00 24.67           C  
-ANISOU 4632  C4  FUC A 604     2381   4289   2701    757   -906   -814       C  
-HETATM 4633  C5  FUC A 604      69.594  14.748  24.620  1.00 24.69           C  
-ANISOU 4633  C5  FUC A 604     2122   4465   2792    393  -1129   -651       C  
-HETATM 4634  C6  FUC A 604      69.180  14.928  23.249  1.00 25.13           C  
-ANISOU 4634  C6  FUC A 604     1924   4496   3127    138  -1160   -407       C  
-HETATM 4635  O2  FUC A 604      71.671  13.041  27.763  1.00 27.25           O  
-ANISOU 4635  O2  FUC A 604     2371   4789   3193    937  -1071   -532       O  
-HETATM 4636  O3  FUC A 604      69.274  11.873  26.937  1.00 26.70           O  
-ANISOU 4636  O3  FUC A 604     2600   4329   3215   1065  -1078   -772       O  
-HETATM 4637  O4  FUC A 604      69.483  12.401  24.225  1.00 25.09           O  
-ANISOU 4637  O4  FUC A 604     2564   4052   2916   1011   -837   -829       O  
-HETATM 4638  O5  FUC A 604      71.087  14.881  24.689  1.00 26.33           O  
-ANISOU 4638  O5  FUC A 604     2046   4537   3422    192  -1221   -744       O  
-HETATM 4639  C1  FUC B 601      67.190  33.370   2.680  1.00 26.76           C  
-ANISOU 4639  C1  FUC B 601     3742   2627   3798   -581   -546   -925       C  
-HETATM 4640  C2  FUC B 601      67.870  32.729   3.697  1.00 27.06           C  
-ANISOU 4640  C2  FUC B 601     3475   3115   3690   -529   -125   -576       C  
-HETATM 4641  C3  FUC B 601      68.430  33.596   4.800  1.00 27.19           C  
-ANISOU 4641  C3  FUC B 601     3589   3333   3409   -751   -587   -728       C  
-HETATM 4642  C4  FUC B 601      67.479  34.581   5.356  1.00 26.88           C  
-ANISOU 4642  C4  FUC B 601     3637   3201   3376  -1010   -204   -185       C  
-HETATM 4643  C5  FUC B 601      66.602  35.108   4.271  1.00 30.49           C  
-ANISOU 4643  C5  FUC B 601     4048   3513   4024   -468   -297   -182       C  
-HETATM 4644  C6  FUC B 601      65.499  35.922   4.806  1.00 33.18           C  
-ANISOU 4644  C6  FUC B 601     4214   3775   4617   -114   -353    -39       C  
-HETATM 4645  O2  FUC B 601      68.917  32.274   2.965  1.00 23.77           O  
-ANISOU 4645  O2  FUC B 601     3049   2489   3493   -595     45   -519       O  
-HETATM 4646  O3  FUC B 601      68.900  32.765   5.768  1.00 30.26           O  
-ANISOU 4646  O3  FUC B 601     3945   3699   3851   -520   -362   -651       O  
-HETATM 4647  O4  FUC B 601      66.632  34.037   6.292  1.00 28.72           O  
-ANISOU 4647  O4  FUC B 601     3567   3899   3444   -569   -349   -133       O  
-HETATM 4648  O5  FUC B 601      66.089  34.060   3.465  1.00 27.31           O  
-ANISOU 4648  O5  FUC B 601     3889   2829   3659  -1128    118   -593       O  
-HETATM 4649  C1  GAL B 602      67.467  35.884   0.386  1.00 19.34           C  
-ANISOU 4649  C1  GAL B 602     3338   1211   2797   -609   -208    -12       C  
-HETATM 4650  C2  GAL B 602      67.381  34.379   0.600  1.00 20.82           C  
-ANISOU 4650  C2  GAL B 602     3383   1434   3092   -380   -527   -495       C  
-HETATM 4651  C3  GAL B 602      67.829  33.621  -0.599  1.00 18.44           C  
-ANISOU 4651  C3  GAL B 602     3016   1209   2782   -522   -315    -26       C  
-HETATM 4652  C4  GAL B 602      67.238  34.082  -1.794  1.00 18.62           C  
-ANISOU 4652  C4  GAL B 602     2860   1291   2922   -672   -128     42       C  
-HETATM 4653  C5  GAL B 602      67.407  35.569  -1.901  1.00 19.01           C  
-ANISOU 4653  C5  GAL B 602     3110   1176   2935   -459    237    232       C  
-HETATM 4654  C6  GAL B 602      66.741  36.162  -3.044  1.00 19.88           C  
-ANISOU 4654  C6  GAL B 602     3246   1132   3174   -460    118    598       C  
-HETATM 4655  O2  GAL B 602      68.074  34.049   1.785  1.00 25.23           O  
-ANISOU 4655  O2  GAL B 602     3867   2000   3719   -184   -726   -451       O  
-HETATM 4656  O3  GAL B 602      67.597  32.202  -0.432  1.00 19.03           O  
-ANISOU 4656  O3  GAL B 602     2651   1496   3083   -621   -617    -63       O  
-HETATM 4657  O4  GAL B 602      65.843  33.741  -1.823  1.00 17.22           O  
-ANISOU 4657  O4  GAL B 602     2680   1049   2815   -595     35   -119       O  
-HETATM 4658  O5  GAL B 602      66.806  36.171  -0.727  1.00 19.02           O  
-ANISOU 4658  O5  GAL B 602     3117   1202   2906   -550     87    -52       O  
-HETATM 4659  O6  GAL B 602      67.011  37.495  -3.244  1.00 22.78           O  
-ANISOU 4659  O6  GAL B 602     3744   1301   3608   -228    281    662       O  
-HETATM 4660  C1  NDG B 603      67.332  40.178   3.199  1.00 31.20           C  
-ANISOU 4660  C1  NDG B 603     4163   1993   5697   -840    334   -639       C  
-HETATM 4661  C2  NDG B 603      66.284  40.082   2.143  1.00 28.77           C  
-ANISOU 4661  C2  NDG B 603     4099   1739   5093   -791    149   -745       C  
-HETATM 4662  C3  NDG B 603      65.997  38.647   1.883  1.00 25.28           C  
-ANISOU 4662  C3  NDG B 603     3725   1461   4417   -787    297   -308       C  
-HETATM 4663  C4  NDG B 603      67.187  37.929   1.658  1.00 24.10           C  
-ANISOU 4663  C4  NDG B 603     3709   1517   3932   -712    158   -686       C  
-HETATM 4664  C5  NDG B 603      68.199  38.122   2.773  1.00 27.56           C  
-ANISOU 4664  C5  NDG B 603     3835   1858   4778   -888     46   -727       C  
-HETATM 4665  C6  NDG B 603      69.487  37.517   2.523  1.00 29.42           C  
-ANISOU 4665  C6  NDG B 603     3886   2199   5094   -828    213   -476       C  
-HETATM 4666  C7  NDG B 603      64.577  41.862   1.970  1.00 35.20           C  
-ANISOU 4666  C7  NDG B 603     4595   1987   6792   -121    423   -902       C  
-HETATM 4667  C8  NDG B 603      63.454  42.485   2.451  1.00 36.82           C  
-ANISOU 4667  C8  NDG B 603     4655   2068   7267    -67    458   -748       C  
-HETATM 4668  O   NDG B 603      68.467  39.509   2.898  1.00 29.39           O  
-ANISOU 4668  O   NDG B 603     4020   1919   5226   -877    142   -905       O  
-HETATM 4669  O3  NDG B 603      65.076  38.480   0.737  1.00 23.43           O  
-ANISOU 4669  O3  NDG B 603     3417   1390   4094   -786    373    -51       O  
-HETATM 4670  O4  NDG B 603      66.907  36.501   1.469  1.00 21.58           O  
-ANISOU 4670  O4  NDG B 603     3554   1457   3189   -665    118   -451       O  
-HETATM 4671  O6  NDG B 603      70.148  37.866   1.308  1.00 33.85           O  
-ANISOU 4671  O6  NDG B 603     3976   2909   5974   -622    148   -508       O  
-HETATM 4672  O7  NDG B 603      65.089  42.266   0.958  1.00 37.67           O  
-ANISOU 4672  O7  NDG B 603     4745   2242   7324      0    313   -616       O  
-HETATM 4673  N2  NDG B 603      65.105  40.739   2.659  1.00 31.38           N  
-ANISOU 4673  N2  NDG B 603     4393   1866   5662   -407     92  -1076       N  
-HETATM 4674  O1L NDG B 603      66.869  39.785   4.374  1.00 34.52           O  
-ANISOU 4674  O1L NDG B 603     4331   2680   6105   -616    343   -815       O  
-HETATM 4675  C1  FUC B 604      63.707  38.364   0.929  1.00 22.24           C  
-ANISOU 4675  C1  FUC B 604     3414   1154   3882   -492    287    -35       C  
-HETATM 4676  C2  FUC B 604      62.997  38.470  -0.370  1.00 21.23           C  
-ANISOU 4676  C2  FUC B 604     3343   1094   3627   -407    324    178       C  
-HETATM 4677  C3  FUC B 604      63.313  37.343  -1.260  1.00 20.23           C  
-ANISOU 4677  C3  FUC B 604     3169   1125   3391   -409    398     71       C  
-HETATM 4678  C4  FUC B 604      62.984  36.093  -0.618  1.00 19.92           C  
-ANISOU 4678  C4  FUC B 604     2868   1255   3446   -391    611     21       C  
-HETATM 4679  C5  FUC B 604      63.679  36.000   0.663  1.00 19.29           C  
-ANISOU 4679  C5  FUC B 604     3056   1134   3137   -506    646     61       C  
-HETATM 4680  C6  FUC B 604      63.360  34.787   1.399  1.00 20.17           C  
-ANISOU 4680  C6  FUC B 604     3149   1099   3415   -365    577   -253       C  
-HETATM 4681  O2  FUC B 604      63.392  39.694  -0.977  1.00 24.23           O  
-ANISOU 4681  O2  FUC B 604     3516   1377   4314   -374    480    554       O  
-HETATM 4682  O3  FUC B 604      62.562  37.495  -2.445  1.00 21.17           O  
-ANISOU 4682  O3  FUC B 604     3203   1399   3440   -379    295    311       O  
-HETATM 4683  O4  FUC B 604      61.595  36.030  -0.444  1.00 20.56           O  
-ANISOU 4683  O4  FUC B 604     2741   1427   3642   -207    591     -6       O  
-HETATM 4684  O5  FUC B 604      63.360  37.161   1.525  1.00 20.33           O  
-ANISOU 4684  O5  FUC B 604     3292   1157   3275   -286    715   -429       O  
-HETATM 4685  O   HOH A 701      45.513  32.608  19.617  1.00 15.95           O  
-ANISOU 4685  O   HOH A 701     2075   2039   1946    863   -118     12       O  
-HETATM 4686  O   HOH A 702      65.435  -5.236   8.813  1.00 15.01           O  
-ANISOU 4686  O   HOH A 702     1691   1220   2791    202    -70     71       O  
-HETATM 4687  O   HOH A 703      50.825   1.960  14.035  1.00 16.64           O  
-ANISOU 4687  O   HOH A 703     1917   1948   2457    827   -413   -632       O  
-HETATM 4688  O   HOH A 704      48.951  -8.188  -2.169  1.00 13.57           O  
-ANISOU 4688  O   HOH A 704     2040   1292   1822    -29   -196     35       O  
-HETATM 4689  O   HOH A 705      50.926  -5.571  13.388  1.00 12.11           O  
-ANISOU 4689  O   HOH A 705     1332   1115   2155   -255   -386    215       O  
-HETATM 4690  O   HOH A 706      62.976  21.778  17.244  1.00 23.69           O  
-ANISOU 4690  O   HOH A 706     1965   2353   4684    276   -519   1214       O  
-HETATM 4691  O   HOH A 707      47.199  19.682  14.462  1.00 11.13           O  
-ANISOU 4691  O   HOH A 707     1146   1071   2012    188     25    226       O  
-HETATM 4692  O   HOH A 708      44.639  16.722  10.622  1.00 11.62           O  
-ANISOU 4692  O   HOH A 708     1565   1194   1654    220   -196   -130       O  
-HETATM 4693  O   HOH A 709      51.681  12.255  28.069  1.00 16.99           O  
-ANISOU 4693  O   HOH A 709     2312   2134   2008    -85     26    -93       O  
-HETATM 4694  O   HOH A 710      56.094  22.043  25.816  1.00 12.97           O  
-ANISOU 4694  O   HOH A 710     1934   1088   1904    260   -315   -177       O  
-HETATM 4695  O   HOH A 711      49.051   6.931  10.456  1.00 11.48           O  
-ANISOU 4695  O   HOH A 711     1483   1089   1789     58     54    -71       O  
-HETATM 4696  O   HOH A 712      47.654  -0.958  13.509  1.00 14.49           O  
-ANISOU 4696  O   HOH A 712     2220   1273   2011    278    -69    -44       O  
-HETATM 4697  O   HOH A 713      52.989   9.299  15.349  1.00 10.78           O  
-ANISOU 4697  O   HOH A 713     1157   1024   1915    104     52    -84       O  
-HETATM 4698  O   HOH A 714      43.705  11.097  27.183  1.00 27.98           O  
-ANISOU 4698  O   HOH A 714     2744   3789   4097    299    299   1515       O  
-HETATM 4699  O   HOH A 715      46.484  -9.281  -1.292  1.00 12.61           O  
-ANISOU 4699  O   HOH A 715     1866   1270   1655   -184   -328    260       O  
-HETATM 4700  O   HOH A 716      66.961  11.167  23.987  1.00 19.85           O  
-ANISOU 4700  O   HOH A 716     2260   2608   2673   1023   -640   -707       O  
-HETATM 4701  O   HOH A 717      53.798 -20.728   9.140  1.00 16.88           O  
-ANISOU 4701  O   HOH A 717     2669   1763   1980   -294   -282    188       O  
-HETATM 4702  O   HOH A 718      63.835   3.420   7.522  1.00 22.26           O  
-ANISOU 4702  O   HOH A 718     1442   1598   5418     48   -374   -753       O  
-HETATM 4703  O   HOH A 719      50.808  32.146   8.604  1.00 13.12           O  
-ANISOU 4703  O   HOH A 719     1834   1274   1876    419     16    -85       O  
-HETATM 4704  O   HOH A 720      52.968  20.746  25.588  1.00 12.86           O  
-ANISOU 4704  O   HOH A 720     1926   1219   1740    604   -315   -157       O  
-HETATM 4705  O   HOH A 721      63.327  14.227  10.506  1.00 22.22           O  
-ANISOU 4705  O   HOH A 721     3037   3301   2102   1216    -96     35       O  
-HETATM 4706  O   HOH A 722      63.245   0.874   3.068  1.00 18.85           O  
-ANISOU 4706  O   HOH A 722     2758   1437   2968   -128    863   -412       O  
-HETATM 4707  O   HOH A 723      56.234  28.912  26.745  1.00 18.63           O  
-ANISOU 4707  O   HOH A 723     2553   1948   2577    988   -778   -576       O  
-HETATM 4708  O   HOH A 724      64.859   0.221  11.930  1.00 20.97           O  
-ANISOU 4708  O   HOH A 724     3696   1617   2653    858   -755   -199       O  
-HETATM 4709  O   HOH A 725      49.681 -19.686  15.241  1.00 15.02           O  
-ANISOU 4709  O   HOH A 725     2377   1269   2062   -526   -119    -71       O  
-HETATM 4710  O   HOH A 726      52.102   7.170   0.419  1.00 11.15           O  
-ANISOU 4710  O   HOH A 726     1102   1365   1768   -112     51      2       O  
-HETATM 4711  O   HOH A 727      61.012  10.439  27.698  1.00 15.57           O  
-ANISOU 4711  O   HOH A 727     2158   1699   2058    517   -491   -148       O  
-HETATM 4712  O   HOH A 728      46.897  28.035   4.293  1.00 16.06           O  
-ANISOU 4712  O   HOH A 728     2006   1928   2169    426   -202    -94       O  
-HETATM 4713  O   HOH A 729      46.817  25.206   3.831  1.00 14.01           O  
-ANISOU 4713  O   HOH A 729     1833   1860   1630     60    -57     82       O  
-HETATM 4714  O   HOH A 730      58.678   8.469  26.440  1.00 16.38           O  
-ANISOU 4714  O   HOH A 730     2423   1723   2077    552   -545   -134       O  
-HETATM 4715  O   HOH A 731      51.211  35.541  -1.121  1.00 20.96           O  
-ANISOU 4715  O   HOH A 731     3149   2085   2729    772    118    415       O  
-HETATM 4716  O   HOH A 732      55.418   7.013  22.770  1.00 14.59           O  
-ANISOU 4716  O   HOH A 732     2028   1149   2366    392      3    352       O  
-HETATM 4717  O   HOH A 733      48.284  10.862  18.023  1.00 11.76           O  
-ANISOU 4717  O   HOH A 733     1350   1381   1738     44     20     53       O  
-HETATM 4718  O   HOH A 734      48.926  15.802  29.421  1.00 15.16           O  
-ANISOU 4718  O   HOH A 734     2310   1565   1883    367    -82     54       O  
-HETATM 4719  O   HOH A 735      46.323  -5.294  -3.755  1.00 20.98           O  
-ANISOU 4719  O   HOH A 735     3281   2262   2428   -780   -869    615       O  
-HETATM 4720  O   HOH A 736      55.686  -8.622  19.617  1.00 13.90           O  
-ANISOU 4720  O   HOH A 736     1526   1872   1881    -64   -167    370       O  
-HETATM 4721  O   HOH A 737      42.158  24.866  18.966  1.00 26.69           O  
-ANISOU 4721  O   HOH A 737     3087   3270   3783    184   1041  -1465       O  
-HETATM 4722  O   HOH A 738      48.652   6.160   2.538  1.00 14.85           O  
-ANISOU 4722  O   HOH A 738     1789   1633   2218   -106     75    -39       O  
-HETATM 4723  O   HOH A 739      51.419   2.681  22.525  1.00 16.47           O  
-ANISOU 4723  O   HOH A 739     2705   1548   2006   -295     -5    178       O  
-HETATM 4724  O   HOH A 740      43.277  23.485   3.131  1.00 30.95           O  
-ANISOU 4724  O   HOH A 740     5418   3422   2917   1329    709    606       O  
-HETATM 4725  O   HOH A 741      54.612 -16.933  11.356  1.00 16.44           O  
-ANISOU 4725  O   HOH A 741     2550   1818   1878    -66   -692    -92       O  
-HETATM 4726  O   HOH A 742      54.708 -24.257  10.939  1.00 15.42           O  
-ANISOU 4726  O   HOH A 742     1964   1265   2629   -350   -182    244       O  
-HETATM 4727  O   HOH A 743      58.579   7.757  29.173  1.00 19.83           O  
-ANISOU 4727  O   HOH A 743     3524   1877   2131   1013   -486   -257       O  
-HETATM 4728  O   HOH A 744      61.619  -3.287  -3.189  1.00 17.61           O  
-ANISOU 4728  O   HOH A 744     2274   1997   2421    140    234    135       O  
-HETATM 4729  O   HOH A 745      59.410  27.661  28.151  1.00 29.63           O  
-ANISOU 4729  O   HOH A 745     4171   4987   2099   -854   -350   -601       O  
-HETATM 4730  O   HOH A 746      61.868  32.921  10.120  1.00 16.42           O  
-ANISOU 4730  O   HOH A 746     2481   1250   2509     18   -103    -56       O  
-HETATM 4731  O   HOH A 747      52.275  13.455  21.358  1.00 13.54           O  
-ANISOU 4731  O   HOH A 747     1809   1527   1809    525   -131   -152       O  
-HETATM 4732  O   HOH A 748      47.818  17.022  13.522  1.00 12.15           O  
-ANISOU 4732  O   HOH A 748     1662    988   1966    388    -47    -72       O  
-HETATM 4733  O   HOH A 749      44.610  -0.893  14.112  1.00 12.97           O  
-ANISOU 4733  O   HOH A 749     1661   1168   2099    -47   -140     42       O  
-HETATM 4734  O   HOH A 750      65.503  29.001   7.009  1.00 16.27           O  
-ANISOU 4734  O   HOH A 750     2040   1691   2449     87    -77   -303       O  
-HETATM 4735  O   HOH A 751      38.023  -6.842   5.966  1.00 17.14           O  
-ANISOU 4735  O   HOH A 751     1551   1849   3110   -459   -311    -40       O  
-HETATM 4736  O   HOH A 752      53.389  20.747  28.375  1.00 13.52           O  
-ANISOU 4736  O   HOH A 752     1766   1643   1726    550   -180   -323       O  
-HETATM 4737  O   HOH A 753      67.509   1.774   7.403  1.00 19.00           O  
-ANISOU 4737  O   HOH A 753     2175   1784   3259   -318    371   -179       O  
-HETATM 4738  O   HOH A 754      42.089  -1.534  16.587  1.00 17.39           O  
-ANISOU 4738  O   HOH A 754     2208   1741   2656   -211    200   -266       O  
-HETATM 4739  O   HOH A 755      52.629   9.391  27.917  1.00 18.67           O  
-ANISOU 4739  O   HOH A 755     2607   2346   2139   -125      4     44       O  
-HETATM 4740  O   HOH A 756      53.036  -9.945  21.044  1.00 18.81           O  
-ANISOU 4740  O   HOH A 756     3053   1929   2164    133   -376   -346       O  
-HETATM 4741  O   HOH A 757      52.798  -5.827   0.562  1.00 12.93           O  
-ANISOU 4741  O   HOH A 757     1890    736   2285   -176   -516    139       O  
-HETATM 4742  O   HOH A 758      61.477  25.453  21.980  1.00 14.89           O  
-ANISOU 4742  O   HOH A 758     1983   1516   2158    -96   -357   -336       O  
-HETATM 4743  O   HOH A 759      40.849   8.578  12.814  1.00 24.37           O  
-ANISOU 4743  O   HOH A 759     2639   2093   4528   -571   1381  -1095       O  
-HETATM 4744  O   HOH A 760      58.199   4.519  -1.849  1.00 12.41           O  
-ANISOU 4744  O   HOH A 760     1445   1359   1910    341    -84    296       O  
-HETATM 4745  O   HOH A 761      45.380   9.214  26.446  1.00 22.11           O  
-ANISOU 4745  O   HOH A 761     2890   2882   2628   -396    614   -375       O  
-HETATM 4746  O   HOH A 762      47.328  36.471  25.533  1.00 20.19           O  
-ANISOU 4746  O   HOH A 762     2478   2359   2832    922    -75   -455       O  
-HETATM 4747  O   HOH A 763      55.746  20.953  29.957  1.00 16.58           O  
-ANISOU 4747  O   HOH A 763     2154   2268   1876    333   -125   -390       O  
-HETATM 4748  O   HOH A 764      40.555  24.224  15.460  1.00 20.46           O  
-ANISOU 4748  O   HOH A 764     1587   2865   3323    626   -511  -1043       O  
-HETATM 4749  O   HOH A 765      40.257  10.927   7.436  1.00 19.37           O  
-ANISOU 4749  O   HOH A 765     2265   2281   2814    180    -29    248       O  
-HETATM 4750  O   HOH A 766      54.192  13.507   7.264  1.00 14.95           O  
-ANISOU 4750  O   HOH A 766     1848   1691   2142    345    -11    299       O  
-HETATM 4751  O   HOH A 767      38.857 -16.188   1.945  1.00 23.56           O  
-ANISOU 4751  O   HOH A 767     3358   1809   3784    213  -1961   -550       O  
-HETATM 4752  O   HOH A 768      65.464   5.716   7.601  1.00 16.48           O  
-ANISOU 4752  O   HOH A 768     2185   1660   2415   -262     15   -499       O  
-HETATM 4753  O   HOH A 769      47.731   9.399  10.772  1.00 14.43           O  
-ANISOU 4753  O   HOH A 769     1789   1218   2476    207     25      1       O  
-HETATM 4754  O   HOH A 770      57.573  34.296   5.034  1.00 20.96           O  
-ANISOU 4754  O   HOH A 770     2374   1560   4030    474    198    666       O  
-HETATM 4755  O   HOH A 771      39.301  -3.267   3.245  1.00 17.65           O  
-ANISOU 4755  O   HOH A 771     1629   2207   2870   -539   -528    518       O  
-HETATM 4756  O   HOH A 772      65.041  21.526  19.299  1.00 23.48           O  
-ANISOU 4756  O   HOH A 772     3328   1526   4067    -47   1248   -331       O  
-HETATM 4757  O   HOH A 773      57.179  23.313  30.125  1.00 18.54           O  
-ANISOU 4757  O   HOH A 773     3026   2121   1897    437   -395   -358       O  
-HETATM 4758  O   HOH A 774      60.962   2.581  23.614  1.00 24.67           O  
-ANISOU 4758  O   HOH A 774     2995   3485   2893   1864   -418   -244       O  
-HETATM 4759  O   HOH A 775      35.870 -11.558  12.341  1.00 26.86           O  
-ANISOU 4759  O   HOH A 775     2781   3149   4274   -693    549   -113       O  
-HETATM 4760  O   HOH A 776      62.584  20.296  26.833  1.00 18.82           O  
-ANISOU 4760  O   HOH A 776     2004   1957   3189    284   -389   -335       O  
-HETATM 4761  O   HOH A 777      63.484  25.491  10.966  1.00 18.86           O  
-ANISOU 4761  O   HOH A 777     2409   1700   3055    308    104    -52       O  
-HETATM 4762  O   HOH A 778      60.872  -5.775  -4.064  1.00 18.78           O  
-ANISOU 4762  O   HOH A 778     2903   1760   2472    -60    -62    190       O  
-HETATM 4763  O   HOH A 779      40.199  -5.348  -1.271  1.00 25.90           O  
-ANISOU 4763  O   HOH A 779     2752   2454   4635     12   -976    477       O  
-HETATM 4764  O   HOH A 780      64.111  26.200   8.324  1.00 20.08           O  
-ANISOU 4764  O   HOH A 780     2168   1599   3861    359    560    385       O  
-HETATM 4765  O   HOH A 781      53.617  26.264  31.976  1.00 25.77           O  
-ANISOU 4765  O   HOH A 781     3132   3288   3369     65    -34  -1162       O  
-HETATM 4766  O   HOH A 782      51.654  17.756   5.300  1.00 18.20           O  
-ANISOU 4766  O   HOH A 782     3031   1646   2238    470    -56     73       O  
-HETATM 4767  O   HOH A 783      40.910  16.398   9.071  1.00 23.76           O  
-ANISOU 4767  O   HOH A 783     3114   2874   3039    241   -215   -539       O  
-HETATM 4768  O   HOH A 784      54.349  -6.758  21.505  1.00 20.71           O  
-ANISOU 4768  O   HOH A 784     2558   2318   2991    600    231    424       O  
-HETATM 4769  O   HOH A 785      39.283 -12.318  15.281  1.00 22.24           O  
-ANISOU 4769  O   HOH A 785     3006   2516   2928   -556    496     30       O  
-HETATM 4770  O   HOH A 786      43.074  30.102  14.780  1.00 30.01           O  
-ANISOU 4770  O   HOH A 786     3777   4568   3056   2294    382    386       O  
-HETATM 4771  O   HOH A 787      61.737 -14.937  13.038  1.00 20.34           O  
-ANISOU 4771  O   HOH A 787     2914   1146   3669   -182   -467    516       O  
-HETATM 4772  O   HOH A 788      62.437  23.970  27.787  1.00 25.96           O  
-ANISOU 4772  O   HOH A 788     2550   4104   3208    501  -1067  -1263       O  
-HETATM 4773  O   HOH A 789      38.083  17.371  14.003  1.00 21.51           O  
-ANISOU 4773  O   HOH A 789     2563   2714   2897    880    347   -684       O  
-HETATM 4774  O   HOH A 790      51.261   4.881  28.284  1.00 24.30           O  
-ANISOU 4774  O   HOH A 790     3740   3116   2377    775    389    884       O  
-HETATM 4775  O   HOH A 791      50.980 -17.977  22.756  1.00 28.58           O  
-ANISOU 4775  O   HOH A 791     5002   2596   3260   -577    -34   -232       O  
-HETATM 4776  O   HOH A 792      54.885  37.529   3.313  1.00 29.89           O  
-ANISOU 4776  O   HOH A 792     6312   2313   2733  -1299    918   -147       O  
-HETATM 4777  O   HOH A 793      67.056  -2.608   6.673  1.00 23.39           O  
-ANISOU 4777  O   HOH A 793     1902   1773   5211     65    454   -533       O  
-HETATM 4778  O   HOH A 794      33.163  -6.100   7.940  1.00 24.24           O  
-ANISOU 4778  O   HOH A 794     2201   2766   4241   -583    -61   -174       O  
-HETATM 4779  O   HOH A 795      37.436  -5.203  10.118  1.00 21.12           O  
-ANISOU 4779  O   HOH A 795     2552   2388   3083   -687     22     76       O  
-HETATM 4780  O   HOH A 796      41.080  -4.672   1.391  1.00 16.66           O  
-ANISOU 4780  O   HOH A 796     1995   1490   2845   -109   -477    393       O  
-HETATM 4781  O   HOH A 797      63.307  22.673  25.544  1.00 23.07           O  
-ANISOU 4781  O   HOH A 797     2314   2468   3983    362   -771   -455       O  
-HETATM 4782  O   HOH A 798      43.566  13.833   6.506  1.00 16.26           O  
-ANISOU 4782  O   HOH A 798     2454   1597   2127    295      5   -136       O  
-HETATM 4783  O   HOH A 799      56.599  36.146  10.999  1.00 28.12           O  
-ANISOU 4783  O   HOH A 799     3618   2744   4320    242   -891  -1313       O  
-HETATM 4784  O   HOH A 800      55.713 -18.970   8.407  1.00 24.68           O  
-ANISOU 4784  O   HOH A 800     2602   2678   4097    -99   -623   1789       O  
-HETATM 4785  O   HOH A 801      63.549  24.625  23.689  1.00 24.18           O  
-ANISOU 4785  O   HOH A 801     2392   3143   3653     82  -1331    321       O  
-HETATM 4786  O   HOH A 802      58.149  10.464  33.466  1.00 28.24           O  
-ANISOU 4786  O   HOH A 802     4502   4296   1931   1666   -427     23       O  
-HETATM 4787  O   HOH A 803      53.565  23.470  32.124  1.00 25.29           O  
-ANISOU 4787  O   HOH A 803     4351   2861   2395    549   -770   -660       O  
-HETATM 4788  O   HOH A 804      37.012 -17.640  10.640  1.00 28.18           O  
-ANISOU 4788  O   HOH A 804     3826   2498   4383  -1332   -132   -177       O  
-HETATM 4789  O   HOH A 805      40.421  20.292   2.985  1.00 20.11           O  
-ANISOU 4789  O   HOH A 805     2706   3131   1802    436   -327   -230       O  
-HETATM 4790  O   HOH A 806      64.606  30.269  10.291  1.00 25.50           O  
-ANISOU 4790  O   HOH A 806     2645   3113   3930    -13   -412   -202       O  
-HETATM 4791  O   HOH A 807      62.385   7.229   4.244  1.00 17.32           O  
-ANISOU 4791  O   HOH A 807     1913   1547   3119   -549    645   -224       O  
-HETATM 4792  O   HOH A 808      59.719  37.819  -2.363  1.00 24.32           O  
-ANISOU 4792  O   HOH A 808     3156   2619   3465    128    368    736       O  
-HETATM 4793  O   HOH A 809      58.629  13.291  10.847  1.00 20.98           O  
-ANISOU 4793  O   HOH A 809     2513   1994   3465    249   -512  -1234       O  
-HETATM 4794  O   HOH A 810      61.916  -1.810  -5.514  1.00 29.35           O  
-ANISOU 4794  O   HOH A 810     4830   2974   3348    985   1007    248       O  
-HETATM 4795  O   HOH A 811      66.415  -7.434   2.312  1.00 29.18           O  
-ANISOU 4795  O   HOH A 811     2759   2529   5797    -29   1503     33       O  
-HETATM 4796  O   HOH A 812      52.581  -8.012  22.996  1.00 21.79           O  
-ANISOU 4796  O   HOH A 812     2676   2707   2896    181   -227   -243       O  
-HETATM 4797  O   HOH A 813      63.163  17.370  28.919  1.00 21.94           O  
-ANISOU 4797  O   HOH A 813     3166   2294   2874    587   -931   -292       O  
-HETATM 4798  O   HOH A 814      63.371   1.423  -0.593  1.00 26.69           O  
-ANISOU 4798  O   HOH A 814     2474   2830   4836   -173    602   -265       O  
-HETATM 4799  O   HOH A 815      43.103  17.734   7.326  1.00 20.46           O  
-ANISOU 4799  O   HOH A 815     2475   2000   3298   -143    590   -300       O  
-HETATM 4800  O   HOH A 816      43.906  27.134  15.070  1.00 29.88           O  
-ANISOU 4800  O   HOH A 816     3618   4143   3590   1001   -806   -389       O  
-HETATM 4801  O   HOH A 817      61.851 -17.663   4.549  1.00 24.04           O  
-ANISOU 4801  O   HOH A 817     2724   2722   3688    355   -105    187       O  
-HETATM 4802  O   HOH A 818      47.946  24.002  26.586  1.00 27.85           O  
-ANISOU 4802  O   HOH A 818     3850   2471   4261   1252  -2002  -1042       O  
-HETATM 4803  O   HOH A 819      60.091  33.673  21.968  1.00 24.61           O  
-ANISOU 4803  O   HOH A 819     2519   3525   3305    537   -756   -682       O  
-HETATM 4804  O   HOH A 820      40.255   2.487  23.506  1.00 35.42           O  
-ANISOU 4804  O   HOH A 820     4762   3826   4868    -84   1761    287       O  
-HETATM 4805  O   HOH A 821      59.610 -17.616   7.726  1.00 29.87           O  
-ANISOU 4805  O   HOH A 821     3915   4983   2452     93   -649    485       O  
-HETATM 4806  O   HOH A 822      42.910  27.646   9.004  1.00 22.51           O  
-ANISOU 4806  O   HOH A 822     2274   2573   3706    487     37     32       O  
-HETATM 4807  O   HOH A 823      62.657  31.221  13.314  1.00 23.45           O  
-ANISOU 4807  O   HOH A 823     3438   2121   3349      6   -961   -116       O  
-HETATM 4808  O   HOH A 824      51.846  27.423  30.089  1.00 32.87           O  
-ANISOU 4808  O   HOH A 824     4778   3990   3722   1132    -48    370       O  
-HETATM 4809  O   HOH A 825      50.308 -15.345  21.895  1.00 29.53           O  
-ANISOU 4809  O   HOH A 825     5350   2678   3192  -1779    806   -283       O  
-HETATM 4810  O   HOH A 826      56.622   5.951  29.728  1.00 33.58           O  
-ANISOU 4810  O   HOH A 826     6076   3948   2736  -1313    833   -684       O  
-HETATM 4811  O   HOH A 827      44.719 -10.172  -3.194  1.00 36.76           O  
-ANISOU 4811  O   HOH A 827     4444   5185   4336  -1237  -1313  -1550       O  
-HETATM 4812  O   HOH A 828      43.102 -21.221   3.141  1.00 30.66           O  
-ANISOU 4812  O   HOH A 828     5565   2302   3781   1054   -370   -112       O  
-HETATM 4813  O   HOH A 829      39.595  18.641   8.493  1.00 27.12           O  
-ANISOU 4813  O   HOH A 829     3376   4042   2885   -129   -350     21       O  
-HETATM 4814  O   HOH A 830      55.521 -20.815  -2.229  1.00 27.66           O  
-ANISOU 4814  O   HOH A 830     4989   2313   3205  -1365   -112   -511       O  
-HETATM 4815  O   HOH A 831      39.336 -14.508  16.760  1.00 34.61           O  
-ANISOU 4815  O   HOH A 831     5657   2909   4584      7   1129    706       O  
-HETATM 4816  O   HOH A 832      36.983   5.682   8.726  1.00 30.17           O  
-ANISOU 4816  O   HOH A 832     2311   4047   5105   -301  -1025   2202       O  
-HETATM 4817  O   HOH A 833      39.141   5.376  17.491  1.00 26.02           O  
-ANISOU 4817  O   HOH A 833     2593   4314   2978  -1428   1155  -1148       O  
-HETATM 4818  O   HOH A 834      44.768  15.713   7.965  1.00 17.88           O  
-ANISOU 4818  O   HOH A 834     2338   2246   2209    193    -80   -338       O  
-HETATM 4819  O   HOH A 835      51.598   1.204  26.105  1.00 35.10           O  
-ANISOU 4819  O   HOH A 835     5134   3405   4798   -741   1171   1062       O  
-HETATM 4820  O   HOH A 836      54.196  37.981  -3.732  1.00 36.30           O  
-ANISOU 4820  O   HOH A 836     6359   3618   3813   -556    757    300       O  
-HETATM 4821  O   HOH A 837      62.375   0.978  -5.792  1.00 23.77           O  
-ANISOU 4821  O   HOH A 837     3246   2655   3130    502    478    350       O  
-HETATM 4822  O   HOH A 838      55.751  22.236  33.329  1.00 31.12           O  
-ANISOU 4822  O   HOH A 838     4936   3261   3625    962  -1072   -766       O  
-HETATM 4823  O   HOH A 839      45.545  37.040   6.032  1.00 35.15           O  
-ANISOU 4823  O   HOH A 839     5114   4487   3755   2794    238   -169       O  
-HETATM 4824  O   HOH A 840      69.381   2.062   9.722  1.00 29.85           O  
-ANISOU 4824  O   HOH A 840     3669   3179   4492   -175    743   -651       O  
-HETATM 4825  O   HOH A 841      62.484   0.313  19.027  1.00 30.87           O  
-ANISOU 4825  O   HOH A 841     4948   3355   3425   1721    241    918       O  
-HETATM 4826  O   HOH A 842      48.709   7.879  28.840  1.00 32.52           O  
-ANISOU 4826  O   HOH A 842     5101   4375   2879   -163   1414     48       O  
-HETATM 4827  O   HOH A 843      49.829  14.723  31.704  1.00 26.52           O  
-ANISOU 4827  O   HOH A 843     3977   3602   2496    657   -133    328       O  
-HETATM 4828  O   HOH A 844      49.119  34.285  -2.644  1.00 28.05           O  
-ANISOU 4828  O   HOH A 844     3575   3040   4042    481   -198    522       O  
-HETATM 4829  O   HOH A 845      37.440  10.297  31.314  1.00 30.08           O  
-ANISOU 4829  O   HOH A 845     3675   4456   3296   -841    528    655       O  
-HETATM 4830  O   HOH A 846      52.387  14.242  32.131  1.00 23.35           O  
-ANISOU 4830  O   HOH A 846     3550   2595   2728    166    236    144       O  
-HETATM 4831  O   HOH A 847      55.764  21.906   8.852  1.00 20.46           O  
-ANISOU 4831  O   HOH A 847     2623   1950   3199    572   -225     36       O  
-HETATM 4832  O   HOH A 848      40.961 -21.964   8.641  1.00 28.44           O  
-ANISOU 4832  O   HOH A 848     4377   1917   4511  -1151   -405    699       O  
-HETATM 4833  O   HOH A 849      66.069  22.075  25.600  1.00 28.24           O  
-ANISOU 4833  O   HOH A 849     2962   3534   4233    737   -908  -1241       O  
-HETATM 4834  O   HOH A 850      38.855  13.295   6.976  1.00 23.68           O  
-ANISOU 4834  O   HOH A 850     3141   2457   3399    462    269    308       O  
-HETATM 4835  O   HOH A 851      38.278  22.000   3.129  1.00 35.57           O  
-ANISOU 4835  O   HOH A 851     5370   4928   3217   1781   -331    -29       O  
-HETATM 4836  O   HOH A 852      51.369  19.140  35.172  1.00 28.67           O  
-ANISOU 4836  O   HOH A 852     4131   4381   2379   1074   -315   -628       O  
-HETATM 4837  O   HOH A 853      53.813  11.817  31.748  1.00 33.15           O  
-ANISOU 4837  O   HOH A 853     4158   3059   5376    553   2073   -392       O  
-HETATM 4838  O   HOH A 854      51.691 -18.847  -1.270  1.00 27.55           O  
-ANISOU 4838  O   HOH A 854     4898   3281   2287   -827   -101   -892       O  
-HETATM 4839  O   HOH A 855      73.035  20.805  20.658  1.00 32.62           O  
-ANISOU 4839  O   HOH A 855     3967   3639   4788   -512  -1052    -41       O  
-HETATM 4840  O   HOH A 856      45.483  32.561   9.205  1.00 31.35           O  
-ANISOU 4840  O   HOH A 856     4681   4699   2529   -308   -192    465       O  
-HETATM 4841  O   HOH A 857      40.989  15.092   6.762  1.00 24.07           O  
-ANISOU 4841  O   HOH A 857     3046   2800   3299    865   -333   -453       O  
-HETATM 4842  O   HOH A 858      60.753  36.310  16.926  1.00 32.95           O  
-ANISOU 4842  O   HOH A 858     3072   4636   4810    351   -595    402       O  
-HETATM 4843  O   HOH A 859      44.955  34.197   3.301  1.00 31.68           O  
-ANISOU 4843  O   HOH A 859     3229   3276   5531   1058  -1575      9       O  
-HETATM 4844  O   HOH A 860      49.077  -0.226  18.053  1.00 17.99           O  
-ANISOU 4844  O   HOH A 860     2442   1766   2628    -63    -77     65       O  
-HETATM 4845  O   HOH A 861      68.272  12.750  30.166  1.00 36.36           O  
-ANISOU 4845  O   HOH A 861     3883   5186   4746    430  -2118   -326       O  
-HETATM 4846  O   HOH A 862      64.813  29.034  16.205  1.00 37.72           O  
-ANISOU 4846  O   HOH A 862     5658   3732   4941   -512   1493   -669       O  
-HETATM 4847  O   HOH A 863      35.419  22.897  16.274  1.00 37.58           O  
-ANISOU 4847  O   HOH A 863     5688   2579   6010   1144   2035    -79       O  
-HETATM 4848  O   HOH A 864      39.716  26.493  11.367  1.00 27.86           O  
-ANISOU 4848  O   HOH A 864     2906   2926   4754    426    961   -719       O  
-HETATM 4849  O   HOH A 865      44.312  27.550  12.803  1.00 36.13           O  
-ANISOU 4849  O   HOH A 865     4283   5570   3875    163    132   1704       O  
-HETATM 4850  O   HOH A 866      64.427 -10.761  -1.670  1.00 26.41           O  
-ANISOU 4850  O   HOH A 866     3750   2697   3585   1195    621   -310       O  
-HETATM 4851  O   HOH A 867      43.999 -16.514  17.144  1.00 24.10           O  
-ANISOU 4851  O   HOH A 867     2655   2673   3829   -786    423   -247       O  
-HETATM 4852  O   HOH A 868      70.530   4.757  20.945  1.00 33.21           O  
-ANISOU 4852  O   HOH A 868     4422   3752   4444   -140    185     38       O  
-HETATM 4853  O   HOH A 869      63.779 -15.735   3.513  1.00 29.83           O  
-ANISOU 4853  O   HOH A 869     3294   2462   5578    522    199    134       O  
-HETATM 4854  O   HOH A 870      37.436  19.776  10.389  1.00 30.61           O  
-ANISOU 4854  O   HOH A 870     4486   3844   3301   -859  -1112   -210       O  
-HETATM 4855  O   HOH A 871      58.311  22.331   8.112  1.00 23.26           O  
-ANISOU 4855  O   HOH A 871     2879   1968   3990   -303    567    107       O  
-HETATM 4856  O   HOH A 872      62.840  36.875   6.939  1.00 30.85           O  
-ANISOU 4856  O   HOH A 872     5451   2210   4060   -516  -1196   -934       O  
-HETATM 4857  O   HOH A 873      60.977  39.958   3.935  1.00 30.27           O  
-ANISOU 4857  O   HOH A 873     4382   2716   4403    272  -1341   -492       O  
-HETATM 4858  O   HOH A 874      59.373  -5.622  -6.446  1.00 27.04           O  
-ANISOU 4858  O   HOH A 874     4467   2892   2913     31   -478    -99       O  
-HETATM 4859  O   HOH A 875      63.853 -14.696  10.502  1.00 27.61           O  
-ANISOU 4859  O   HOH A 875     5116   1482   3893    407   -545    234       O  
-HETATM 4860  O   HOH A 876      54.722   1.556  28.236  1.00 36.38           O  
-ANISOU 4860  O   HOH A 876     4980   4868   3973   -975    474   1318       O  
-HETATM 4861  O   HOH A 877      44.373  26.126  26.791  1.00 25.51           O  
-ANISOU 4861  O   HOH A 877     3351   3096   3244   1312   -180    -76       O  
-HETATM 4862  O   HOH A 878      62.136  29.640  15.575  1.00 29.38           O  
-ANISOU 4862  O   HOH A 878     5586   2289   3287  -1444   -636    121       O  
-HETATM 4863  O   HOH A 879      38.818   6.605  24.357  1.00 28.68           O  
-ANISOU 4863  O   HOH A 879     3604   4060   3234   -799    613    -47       O  
-HETATM 4864  O   HOH A 880      49.170  16.014  33.929  1.00 37.44           O  
-ANISOU 4864  O   HOH A 880     5087   4589   4548    318    853   -998       O  
-HETATM 4865  O   HOH A 881      58.421 -18.591  18.697  1.00 34.20           O  
-ANISOU 4865  O   HOH A 881     4586   3969   4439   -724   -986    529       O  
-HETATM 4866  O   HOH A 882      68.520  24.831  18.072  1.00 41.04           O  
-ANISOU 4866  O   HOH A 882     5585   4788   5218   -616  -1236  -1942       O  
-HETATM 4867  O   HOH A 883      56.068 -18.420  19.908  1.00 34.61           O  
-ANISOU 4867  O   HOH A 883     4702   5307   3139   1516   -361    299       O  
-HETATM 4868  O   HOH A 884      59.041   8.026  34.007  1.00 40.90           O  
-ANISOU 4868  O   HOH A 884     5350   5025   5166   -788   -447   1021       O  
-HETATM 4869  O   HOH A 885      63.964  25.180  19.481  1.00 36.78           O  
-ANISOU 4869  O   HOH A 885     4981   5220   3774    686   -686   -113       O  
-HETATM 4870  O   HOH A 886      41.903 -14.763  18.177  1.00 33.26           O  
-ANISOU 4870  O   HOH A 886     4208   4312   4116  -1111   -266  -1002       O  
-HETATM 4871  O   HOH A 887      47.817  36.952  28.255  1.00 34.25           O  
-ANISOU 4871  O   HOH A 887     4167   4664   4181   1575   -500   -208       O  
-HETATM 4872  O   HOH A 888      46.207  37.052  30.543  1.00 37.14           O  
-ANISOU 4872  O   HOH A 888     5268   4754   4089    857    703   -989       O  
-HETATM 4873  O   HOH A 889      55.309 -22.024   2.102  1.00 36.31           O  
-ANISOU 4873  O   HOH A 889     4812   2535   6448  -1074    813   1049       O  
-HETATM 4874  O   HOH A 890      38.268  24.167  16.902  1.00 26.03           O  
-ANISOU 4874  O   HOH A 890     3641   3037   3210    519    -55   -986       O  
-HETATM 4875  O   HOH A 891      48.982  -9.258  -4.737  1.00 30.68           O  
-ANISOU 4875  O   HOH A 891     6592   2557   2507    337     30   -250       O  
-HETATM 4876  O   HOH A 892      42.631  -4.424  20.069  1.00 29.44           O  
-ANISOU 4876  O   HOH A 892     4088   3635   3463   -801    141    138       O  
-HETATM 4877  O   HOH A 893      42.803  28.343   6.309  1.00 35.14           O  
-ANISOU 4877  O   HOH A 893     4592   4255   4504   1035    421   1025       O  
-HETATM 4878  O   HOH A 894      56.451 -19.113  11.559  1.00 38.87           O  
-ANISOU 4878  O   HOH A 894     5546   4669   4553   1180   -553  -1271       O  
-HETATM 4879  O   HOH A 895      49.383  37.775  22.554  1.00 32.58           O  
-ANISOU 4879  O   HOH A 895     4918   2068   5392   -315   1004   -788       O  
-HETATM 4880  O   HOH A 896      36.810   8.461   9.205  1.00 36.05           O  
-ANISOU 4880  O   HOH A 896     3315   3814   6569    326    113  -1498       O  
-HETATM 4881  O   HOH A 897      36.124  13.821  25.498  1.00 34.01           O  
-ANISOU 4881  O   HOH A 897     2993   6237   3693   -933    693   -631       O  
-HETATM 4882  O   HOH A 898      61.365  18.300  31.037  1.00 30.92           O  
-ANISOU 4882  O   HOH A 898     4276   4055   3417     -7  -1715   -455       O  
-HETATM 4883  O   HOH A 899      64.127  34.198  10.556  1.00 39.08           O  
-ANISOU 4883  O   HOH A 899     4807   4638   5403  -1608  -1495    -98       O  
-HETATM 4884  O   HOH A 900      55.496  39.014  12.977  1.00 43.65           O  
-ANISOU 4884  O   HOH A 900     5956   4647   5983   -123     87    911       O  
-HETATM 4885  O   HOH A 901      65.810  23.389  21.339  1.00 33.66           O  
-ANISOU 4885  O   HOH A 901     4109   3198   5483   -445   -907  -1084       O  
-HETATM 4886  O   HOH A 902      36.395   3.906  14.211  1.00 32.79           O  
-ANISOU 4886  O   HOH A 902     3082   4070   5306    123    516   -198       O  
-HETATM 4887  O   HOH A 903      53.540  38.444  15.907  1.00 32.72           O  
-ANISOU 4887  O   HOH A 903     3912   3017   5503   -557     63    497       O  
-HETATM 4888  O   HOH A 904      51.287  27.835  27.187  1.00 23.88           O  
-ANISOU 4888  O   HOH A 904     3045   2895   3134     77    145   -388       O  
-HETATM 4889  O   HOH A 905      61.906  34.040  15.079  1.00 35.64           O  
-ANISOU 4889  O   HOH A 905     3957   4757   4828  -1328   -250    866       O  
-HETATM 4890  O   HOH A 906      43.374   0.303  -2.937  1.00 32.12           O  
-ANISOU 4890  O   HOH A 906     4007   4494   3704   -108   -386   -369       O  
-HETATM 4891  O   HOH A 907      35.171   7.313  23.028  1.00 43.60           O  
-ANISOU 4891  O   HOH A 907     5365   5623   5576   -200   1048   -348       O  
-HETATM 4892  O   HOH A 908      51.631  39.255   1.485  1.00 33.04           O  
-ANISOU 4892  O   HOH A 908     5527   3025   4000    361    702    855       O  
-HETATM 4893  O   HOH A 909      70.289  15.195  29.517  1.00 36.83           O  
-ANISOU 4893  O   HOH A 909     4052   5927   4014    616  -1069   -751       O  
-HETATM 4894  O   HOH A 910      35.582  22.529  19.150  1.00 37.89           O  
-ANISOU 4894  O   HOH A 910     5786   4659   3949  -1076    303   -106       O  
-HETATM 4895  O   HOH A 911      38.758  15.438  10.517  1.00 34.43           O  
-ANISOU 4895  O   HOH A 911     4383   4025   4675    924    258   -226       O  
-HETATM 4896  O   HOH A 912      53.998  15.241  33.941  1.00 37.54           O  
-ANISOU 4896  O   HOH A 912     5694   4043   4524    659   -683    968       O  
-HETATM 4897  O   HOH A 913      43.647  -7.164  21.434  1.00 32.86           O  
-ANISOU 4897  O   HOH A 913     3190   3278   6015   -824   -135   -138       O  
-HETATM 4898  O   HOH A 914      39.061   8.906  16.081  1.00 32.86           O  
-ANISOU 4898  O   HOH A 914     2042   4771   5671   -171    453    -82       O  
-HETATM 4899  O   HOH A 915      45.163  29.833   5.454  1.00 35.13           O  
-ANISOU 4899  O   HOH A 915     3932   4279   5137   1014    573   -884       O  
-HETATM 4900  O   HOH A 916      40.080  -4.146  20.396  1.00 33.33           O  
-ANISOU 4900  O   HOH A 916     4121   3816   4728  -1040    495   -505       O  
-HETATM 4901  O   HOH A 917      36.996  17.344  11.477  1.00 33.29           O  
-ANISOU 4901  O   HOH A 917     3540   4834   4274    976    140   -239       O  
-HETATM 4902  O   HOH A 918      51.009  38.227  24.911  1.00 37.02           O  
-ANISOU 4902  O   HOH A 918     4060   3632   6374    398   -690  -1176       O  
-HETATM 4903  O   HOH A 919      41.782  -4.031  23.680  1.00 35.96           O  
-ANISOU 4903  O   HOH A 919     5098   3805   4760  -1417   1413    137       O  
-HETATM 4904  O   HOH A 920      67.460   1.780  13.839  1.00 32.93           O  
-ANISOU 4904  O   HOH A 920     5114   2959   4438   1257   1285   -323       O  
-HETATM 4905  O   HOH A 921      62.985  -6.244  -5.483  1.00 37.96           O  
-ANISOU 4905  O   HOH A 921     4844   4740   4839    845   1747    881       O  
-HETATM 4906  O   HOH A 922      60.760  -7.066  -8.343  1.00 40.46           O  
-ANISOU 4906  O   HOH A 922     6057   4833   4484    717   1010   -844       O  
-HETATM 4907  O   HOH A 923      66.820  21.236  28.143  1.00 37.04           O  
-ANISOU 4907  O   HOH A 923     4599   4892   4582   -283   -583   -782       O  
-HETATM 4908  O   HOH A 924      42.614  -9.728  17.802  1.00 31.38           O  
-ANISOU 4908  O   HOH A 924     3964   3875   4084   -421   -225   1206       O  
-HETATM 4909  O   HOH A 925      54.951  21.671  35.987  1.00 46.13           O  
-ANISOU 4909  O   HOH A 925     6172   6408   4945    329    -34    324       O  
-HETATM 4910  O   HOH A 926      32.557  -2.708   4.388  1.00 43.10           O  
-ANISOU 4910  O   HOH A 926     4859   5539   5978   -466    595     62       O  
-HETATM 4911  O   HOH A 927      36.595   4.880   0.915  1.00 37.39           O  
-ANISOU 4911  O   HOH A 927     4273   4765   5169   1967   -608    606       O  
-HETATM 4912  O   HOH A 928      67.582  12.395  32.548  1.00 39.41           O  
-ANISOU 4912  O   HOH A 928     5175   5038   4759   1848  -1150    183       O  
-HETATM 4913  O   HOH A 929      50.545  38.228  14.099  1.00 35.95           O  
-ANISOU 4913  O   HOH A 929     4888   3969   4801    616   -182   1208       O  
-HETATM 4914  O   HOH A 930      39.489  -2.380  16.937  1.00 34.01           O  
-ANISOU 4914  O   HOH A 930     4269   2237   6416    204   1408    967       O  
-HETATM 4915  O   HOH A 931      68.825  -1.392  12.987  1.00 42.23           O  
-ANISOU 4915  O   HOH A 931     4632   6085   5329   -278    813    170       O  
-HETATM 4916  O   HOH A 932      50.427  38.197  -0.683  1.00 33.99           O  
-ANISOU 4916  O   HOH A 932     5004   2891   5018   1490   -405     53       O  
-HETATM 4917  O   HOH A 933      38.712  10.314   9.663  1.00 27.25           O  
-ANISOU 4917  O   HOH A 933     3357   3245   3752   -656   1203   -331       O  
-HETATM 4918  O   HOH A 934      47.317 -20.712  22.929  1.00 44.78           O  
-ANISOU 4918  O   HOH A 934     6154   5689   5169  -1066   1205    700       O  
-HETATM 4919  O   HOH A 935      37.793  15.937  35.334  1.00 30.42           O  
-ANISOU 4919  O   HOH A 935     3613   4801   3145    996    554     87       O  
-HETATM 4920  O   HOH A 936      43.075  13.962  36.316  1.00 38.83           O  
-ANISOU 4920  O   HOH A 936     5465   4665   4623   -649    224   -111       O  
-HETATM 4921  O   HOH A 937      37.570  13.004   9.388  1.00 38.07           O  
-ANISOU 4921  O   HOH A 937     4551   5694   4220    166    153   -601       O  
-HETATM 4922  O   HOH A 938      36.337  -4.934  12.743  1.00 36.86           O  
-ANISOU 4922  O   HOH A 938     5140   4043   4823   -228   1269   -217       O  
-HETATM 4923  O   HOH A 939      53.616   7.734  29.914  1.00 36.63           O  
-ANISOU 4923  O   HOH A 939     4941   5452   3524   -414   -807   1569       O  
-HETATM 4924  O   HOH A 940      64.480 -15.027   0.777  1.00 36.31           O  
-ANISOU 4924  O   HOH A 940     4006   4097   5694   -263    785   -543       O  
-HETATM 4925  O   HOH A 941      59.545  -2.687  -7.266  1.00 39.48           O  
-ANISOU 4925  O   HOH A 941     5789   4892   4318    711   -362   -603       O  
-HETATM 4926  O   HOH A 942      57.739  27.915  30.953  1.00 40.50           O  
-ANISOU 4926  O   HOH A 942     4998   4170   6220  -1238  -1328    -26       O  
-HETATM 4927  O   HOH A 943      55.953 -19.003  22.501  1.00 44.74           O  
-ANISOU 4927  O   HOH A 943     5379   6544   5075    258   -516    597       O  
-HETATM 4928  O   HOH A 944      38.688   2.928  18.474  1.00 35.10           O  
-ANISOU 4928  O   HOH A 944     4024   4400   4912   -615    433    357       O  
-HETATM 4929  O   HOH A 945      43.115 -19.266  -1.255  1.00 38.52           O  
-ANISOU 4929  O   HOH A 945     6041   4442   4154   -247     31    876       O  
-HETATM 4930  O   HOH A 946      39.281  -3.372  22.680  1.00 40.48           O  
-ANISOU 4930  O   HOH A 946     5152   4838   5388  -2239    627    327       O  
-HETATM 4931  O   HOH A 947      35.604  12.538  32.048  1.00 44.98           O  
-ANISOU 4931  O   HOH A 947     5660   6224   5207   -359   -364    -17       O  
-HETATM 4932  O   HOH A 948      61.319  36.190  19.514  1.00 31.44           O  
-ANISOU 4932  O   HOH A 948     3544   2597   5804    407   -768   -404       O  
-HETATM 4933  O   HOH A 949      59.089  22.403  31.783  1.00 41.63           O  
-ANISOU 4933  O   HOH A 949     4945   6123   4750   -148  -2161   -281       O  
-HETATM 4934  O   HOH A 950      45.347   6.763  27.818  1.00 42.08           O  
-ANISOU 4934  O   HOH A 950     5976   5899   4114   -252    113    673       O  
-HETATM 4935  O   HOH A 951      39.796   4.231  25.584  1.00 35.55           O  
-ANISOU 4935  O   HOH A 951     4446   4737   4322     61    625    678       O  
-HETATM 4936  O   HOH A 952      34.412   4.837   9.674  1.00 40.02           O  
-ANISOU 4936  O   HOH A 952     3814   4984   6408    295     38     32       O  
-HETATM 4937  O   HOH A 953      50.857 -14.498  24.598  1.00 48.98           O  
-ANISOU 4937  O   HOH A 953     6571   6277   5763    218   -158   -681       O  
-HETATM 4938  O   HOH A 954      42.370  32.399   8.604  1.00 45.72           O  
-ANISOU 4938  O   HOH A 954     6373   5417   5581    558   -568   -117       O  
-HETATM 4939  O   HOH A 955      57.944 -22.622   9.383  1.00 41.96           O  
-ANISOU 4939  O   HOH A 955     5260   4972   5709    -23    -56    104       O  
-HETATM 4940  O   HOH A 956      46.625 -11.627  -4.955  1.00 38.88           O  
-ANISOU 4940  O   HOH A 956     5360   5432   3979   -137  -1077    632       O  
-HETATM 4941  O   HOH A 957      61.064  41.493  -0.352  1.00 35.01           O  
-ANISOU 4941  O   HOH A 957     5472   2890   4941   -161    125    962       O  
-HETATM 4942  O   HOH A 958      57.856   0.320  26.837  1.00 37.96           O  
-ANISOU 4942  O   HOH A 958     5514   3680   5227    444  -1107    818       O  
-HETATM 4943  O   HOH A 959      57.624  36.574   6.660  1.00 38.61           O  
-ANISOU 4943  O   HOH A 959     4776   4879   5015  -2150   1621  -1882       O  
-HETATM 4944  O   HOH A 960      37.135  18.505  35.986  1.00 32.56           O  
-ANISOU 4944  O   HOH A 960     4596   4408   3366    406    881   -146       O  
-HETATM 4945  O   HOH A 961      37.562  -3.937  15.262  1.00 42.26           O  
-ANISOU 4945  O   HOH A 961     5126   5952   4980   -314   -245    807       O  
-HETATM 4946  O   HOH A 962      63.395  20.887  15.242  1.00 25.72           O  
-ANISOU 4946  O   HOH A 962     1823   1781   6168    130     23    146       O  
-HETATM 4947  O   HOH A 963      47.700  33.998  19.002  1.00 24.22           O  
-ANISOU 4947  O   HOH A 963     2444   2275   4481    995    813    902       O  
-HETATM 4948  O   HOH A 964      40.548  14.843  14.669  1.00 28.76           O  
-ANISOU 4948  O   HOH A 964     4664   1980   4281    -26   2463      5       O  
-HETATM 4949  O   HOH A 965      66.953  -8.836   5.865  1.00 34.03           O  
-ANISOU 4949  O   HOH A 965     2196   4371   6364   -314    -45   -476       O  
-HETATM 4950  O   HOH A 966      55.432 -22.657   7.876  1.00 29.76           O  
-ANISOU 4950  O   HOH A 966     3326   3562   4419   -569   -307  -1621       O  
-HETATM 4951  O   HOH A 967      42.614  25.768  20.687  1.00 28.15           O  
-ANISOU 4951  O   HOH A 967     3081   3699   3914   1477    -96   -515       O  
-HETATM 4952  O   HOH A 968      57.501  30.023  28.936  1.00 29.06           O  
-ANISOU 4952  O   HOH A 968     4284   3682   3073    660   -421  -1077       O  
-HETATM 4953  O   HOH A 969      44.069  12.090  29.142  1.00 31.72           O  
-ANISOU 4953  O   HOH A 969     4182   2829   5040    732   1465   1049       O  
-HETATM 4954  O   HOH A 970      42.488  29.787  12.456  1.00 35.15           O  
-ANISOU 4954  O   HOH A 970     4239   4368   4746   1650   -741   -217       O  
-HETATM 4955  O   HOH A 971      59.086  25.953  29.849  1.00 33.63           O  
-ANISOU 4955  O   HOH A 971     3775   4432   4572    513    255  -1826       O  
-HETATM 4956  O   HOH A 972      46.186  30.856   7.665  1.00 30.49           O  
-ANISOU 4956  O   HOH A 972     3651   3239   4695     -2    -64   -685       O  
-HETATM 4957  O   HOH A 973      56.512  13.996   5.016  1.00 33.06           O  
-ANISOU 4957  O   HOH A 973     3691   3914   4956    355   -756   1359       O  
-HETATM 4958  O   HOH A 974      38.700  13.795  13.132  1.00 37.89           O  
-ANISOU 4958  O   HOH A 974     3528   4870   5997   1285   1825    389       O  
-HETATM 4959  O   HOH A 975      63.578 -13.272  -1.199  1.00 33.33           O  
-ANISOU 4959  O   HOH A 975     4965   3611   4088   -350   1527   -488       O  
-HETATM 4960  O   HOH A 976      49.420 -23.327  19.380  1.00 33.50           O  
-ANISOU 4960  O   HOH A 976     4365   5270   3092    334    637   -300       O  
-HETATM 4961  O   HOH A 977      63.567  12.310   8.933  1.00 33.67           O  
-ANISOU 4961  O   HOH A 977     3345   3699   5749   -413   -362  -1574       O  
-HETATM 4962  O   HOH A 978      51.596  22.057  33.661  1.00 34.38           O  
-ANISOU 4962  O   HOH A 978     4771   3639   4654    347    -18   -684       O  
-HETATM 4963  O   HOH A 979      41.460  29.917   9.629  1.00 38.10           O  
-ANISOU 4963  O   HOH A 979     4297   4744   5436   1290    924  -1034       O  
-HETATM 4964  O   HOH A 980      43.709  -5.518  -4.563  1.00 38.23           O  
-ANISOU 4964  O   HOH A 980     4893   5660   3972    228   -284    940       O  
-HETATM 4965  O   HOH A 981      42.208 -10.609  -2.797  1.00 31.37           O  
-ANISOU 4965  O   HOH A 981     4959   3651   3308   -602   -916   -131       O  
-HETATM 4966  O   HOH A 982      50.911  -7.984  26.257  1.00 40.65           O  
-ANISOU 4966  O   HOH A 982     5342   5530   4571   1219   -179    914       O  
-HETATM 4967  O   HOH A 983      36.444   1.270  14.768  1.00 32.91           O  
-ANISOU 4967  O   HOH A 983     2773   4583   5146   -463    103    433       O  
-HETATM 4968  O   HOH A 984      56.553  -1.786  -6.604  1.00 36.74           O  
-ANISOU 4968  O   HOH A 984     6005   3882   4073    -89   -554   1358       O  
-HETATM 4969  O   HOH A 985      60.713  35.124  25.381  1.00 41.78           O  
-ANISOU 4969  O   HOH A 985     6227   4073   5573   -966   -265   -139       O  
-HETATM 4970  O   HOH A 986      54.573  37.764  22.227  1.00 43.35           O  
-ANISOU 4970  O   HOH A 986     5524   5478   5469  -1853   -180  -1167       O  
-HETATM 4971  O   HOH A 987      56.556  38.522  -3.459  1.00 39.44           O  
-ANISOU 4971  O   HOH A 987     5427   4617   4939    504   -113    601       O  
-HETATM 4972  O   HOH A 988      36.506  21.017  34.894  1.00 37.78           O  
-ANISOU 4972  O   HOH A 988     5273   4738   4342    964    612    -35       O  
-HETATM 4973  O   HOH A 989      59.123  32.180  28.630  1.00 43.32           O  
-ANISOU 4973  O   HOH A 989     6291   5107   5060   -684   -292   -749       O  
-HETATM 4974  O   HOH A 990      34.576   0.987   7.280  1.00 41.16           O  
-ANISOU 4974  O   HOH A 990     4683   5200   5756   -325    558    449       O  
-HETATM 4975  O   HOH A 991      67.072 -11.111  -0.784  1.00 43.93           O  
-ANISOU 4975  O   HOH A 991     5463   5687   5540   -277    468    703       O  
-HETATM 4976  O   HOH A 992      50.623  -7.338  29.086  1.00 41.21           O  
-ANISOU 4976  O   HOH A 992     5431   5355   4871    411    -81    144       O  
-HETATM 4977  O   HOH A 993      55.948 -20.683   5.723  1.00 37.79           O  
-ANISOU 4977  O   HOH A 993     5450   4616   4292    237  -1000   1093       O  
-HETATM 4978  O   HOH A 994      47.377 -11.824  25.011  1.00 49.56           O  
-ANISOU 4978  O   HOH A 994     6242   5783   6804    523    -15   -649       O  
-HETATM 4979  O   HOH A 995      66.777  29.678  20.269  1.00 40.81           O  
-ANISOU 4979  O   HOH A 995     4622   5325   5558   1098    292    468       O  
-HETATM 4980  O   HOH A 996      67.160   8.729  30.286  1.00 46.94           O  
-ANISOU 4980  O   HOH A 996     5516   5269   7050     83   -254    549       O  
-HETATM 4981  O   HOH A 997      60.329   5.809  30.272  1.00 43.35           O  
-ANISOU 4981  O   HOH A 997     5757   5762   4953     76   -608   1114       O  
-HETATM 4982  O   HOH A 998      41.221 -13.218  -2.989  1.00 47.74           O  
-ANISOU 4982  O   HOH A 998     6070   6020   6047    -27   -864   -773       O  
-HETATM 4983  O   HOH A 999      47.048  -7.297  -5.779  1.00 35.07           O  
-ANISOU 4983  O   HOH A 999     5453   3417   4453   -336   -595   -382       O  
-HETATM 4984  O   HOH A1000      38.828   8.766   5.365  1.00 36.37           O  
-ANISOU 4984  O   HOH A1000     5017   4828   3975   -514    146   1342       O  
-HETATM 4985  O   HOH A1001      48.992   3.219  28.717  1.00 37.30           O  
-ANISOU 4985  O   HOH A1001     5887   4099   4184   -445    734   -633       O  
-HETATM 4986  O   HOH A1002      33.524  -0.920   6.226  1.00 46.19           O  
-ANISOU 4986  O   HOH A1002     5496   5774   6279    749   -172    796       O  
-HETATM 4987  O   HOH A1003      38.327  18.315   6.634  1.00 44.11           O  
-ANISOU 4987  O   HOH A1003     5994   5189   5576    303    702   -826       O  
-HETATM 4988  O   HOH A1004      55.658  41.169  -0.330  1.00 38.78           O  
-ANISOU 4988  O   HOH A1004     5819   3211   5704   -635  -1164    610       O  
-HETATM 4989  O   HOH A1005      34.762 -16.452   4.738  1.00 44.91           O  
-ANISOU 4989  O   HOH A1005     5972   5353   5738  -1520   -271   -180       O  
-HETATM 4990  O   HOH A1006      34.679  20.872  32.594  1.00 47.91           O  
-ANISOU 4990  O   HOH A1006     5747   6192   6264   1371    293    263       O  
-HETATM 4991  O   HOH A1007      49.229  17.782  37.203  1.00 38.33           O  
-ANISOU 4991  O   HOH A1007     3734   6390   4439   1073   -882  -1107       O  
-HETATM 4992  O   HOH A1008      36.838 -13.329  -0.007  1.00 47.36           O  
-ANISOU 4992  O   HOH A1008     6920   5306   5768  -1093   -770   -896       O  
-HETATM 4993  O   HOH A1009      51.695   5.487  21.546  1.00 19.71           O  
-ANISOU 4993  O   HOH A1009     3611   1550   2328   -694    278    143       O  
-HETATM 4994  O   HOH A1010      60.694 -11.791  24.914  1.00 42.99           O  
-ANISOU 4994  O   HOH A1010     5831   5542   4962    166   -427   1044       O  
-HETATM 4995  O   HOH A1011      61.179 -11.078  27.307  1.00 37.54           O  
-ANISOU 4995  O   HOH A1011     3477   5728   5057  -1134  -1327    654       O  
-HETATM 4996  O   HOH A1012      43.436  -3.368  28.259  1.00 39.32           O  
-ANISOU 4996  O   HOH A1012     5702   4302   4934   -242   1112    627       O  
-HETATM 4997  O   HOH A1013      53.561  40.506  11.174  1.00 41.71           O  
-ANISOU 4997  O   HOH A1013     5817   4141   5891   -709   -145   -433       O  
-HETATM 4998  O   HOH A1014      63.294 -19.845  -6.176  1.00 46.50           O  
-ANISOU 4998  O   HOH A1014     6038   5220   6409   -497    899    -96       O  
-HETATM 4999  O   HOH A1015      64.633  19.708  29.217  1.00 42.86           O  
-ANISOU 4999  O   HOH A1015     5835   5178   5271   -238     46  -1337       O  
-HETATM 5000  O   HOH A1016      45.697   4.274  27.472  1.00 41.37           O  
-ANISOU 5000  O   HOH A1016     5816   5338   4563    401    894  -1806       O  
-HETATM 5001  O   HOH A1017      49.209 -18.884  24.819  1.00 47.54           O  
-ANISOU 5001  O   HOH A1017     6681   5875   5505    227    580    486       O  
-HETATM 5002  O   HOH A1018      47.886 -17.317  25.646  1.00 51.29           O  
-ANISOU 5002  O   HOH A1018     6583   6624   6282   -157    190    -25       O  
-HETATM 5003  O   HOH A1019      56.512 -15.169   9.339  1.00 24.98           O  
-ANISOU 5003  O   HOH A1019     3421   2261   3807   -827    444   -195       O  
-HETATM 5004  O   HOH A1020      53.116 -21.426  -0.955  1.00 32.71           O  
-ANISOU 5004  O   HOH A1020     5064   3304   4060  -1361   1112   -772       O  
-HETATM 5005  O   HOH A1021      64.631  -3.513  -2.721  1.00 40.22           O  
-ANISOU 5005  O   HOH A1021     4763   5322   5197    661   1299    192       O  
-HETATM 5006  O   HOH A1022      49.522  38.507   6.588  1.00 34.73           O  
-ANISOU 5006  O   HOH A1022     4328   3715   5152    604  -1405  -1210       O  
-HETATM 5007  O   HOH A1023      41.010 -18.769  -2.614  1.00 40.21           O  
-ANISOU 5007  O   HOH A1023     6025   4543   4711  -2277    392    875       O  
-HETATM 5008  O   HOH A1024      48.365  33.786   9.845  1.00  7.89           O  
-ANISOU 5008  O   HOH A1024     1289    835    873    559      2    -21       O  
-HETATM 5009  O   HOH A1025      51.254  20.038   6.918  1.00 20.07           O  
-ANISOU 5009  O   HOH A1025     2877   2372   2377    446    167    -98       O  
-HETATM 5010  O   HOH A1026      37.966  15.521  16.544  1.00 28.92           O  
-ANISOU 5010  O   HOH A1026     4123   3467   3397   -411    389    507       O  
-HETATM 5011  O   HOH A1027      67.966  26.772  13.451  1.00 43.92           O  
-ANISOU 5011  O   HOH A1027     5956   5750   4982  -1018    648   -180       O  
-HETATM 5012  O   HOH A1028      64.353   3.525  25.069  1.00 39.24           O  
-ANISOU 5012  O   HOH A1028     5440   4272   5195   1657    546    497       O  
-HETATM 5013  O   HOH A1029      74.816  17.344  23.576  1.00 42.18           O  
-ANISOU 5013  O   HOH A1029     4547   5611   5867     85  -1923   -827       O  
-HETATM 5014  O   HOH A1030      50.552  30.306  31.357  1.00 43.79           O  
-ANISOU 5014  O   HOH A1030     5877   5781   4980    933    293   1362       O  
-HETATM 5015  O   HOH A1031      53.975 -14.197  22.115  1.00 46.94           O  
-ANISOU 5015  O   HOH A1031     5778   6315   5741   -997   -859    811       O  
-HETATM 5016  O   HOH A1032      37.000   7.413   6.445  1.00 38.61           O  
-ANISOU 5016  O   HOH A1032     4598   4880   5190    497   -240   1269       O  
-HETATM 5017  O   HOH A1033      51.428  41.878   1.704  1.00 47.72           O  
-ANISOU 5017  O   HOH A1033     6475   5347   6308     38    -63    557       O  
-HETATM 5018  O   HOH A1034      48.947  21.440   5.591  1.00 20.91           O  
-ANISOU 5018  O   HOH A1034     2186   2809   2948    755   -450   -325       O  
-HETATM 5019  O   HOH A1035      56.396 -21.358  12.349  1.00 32.76           O  
-ANISOU 5019  O   HOH A1035     4250   3316   4882   -447   -861    -12       O  
-HETATM 5020  O   HOH A1036      48.681   1.133  26.822  1.00 34.82           O  
-ANISOU 5020  O   HOH A1036     5648   4627   2954   -440    516    577       O  
-HETATM 5021  O   HOH A1037      64.626 -10.270  -4.325  1.00 40.99           O  
-ANISOU 5021  O   HOH A1037     5954   5733   3887   1401   1376    621       O  
-HETATM 5022  O   HOH A1038      47.455 -26.025  16.670  1.00 32.27           O  
-ANISOU 5022  O   HOH A1038     4009   3607   4644   -847     49    927       O  
-HETATM 5023  O   HOH A1039      38.655   9.536  12.029  1.00 44.57           O  
-ANISOU 5023  O   HOH A1039     4825   6085   6023    398    312    127       O  
-HETATM 5024  O   HOH A1040      66.022  27.707  18.026  1.00 43.30           O  
-ANISOU 5024  O   HOH A1040     5288   5781   5384   -284   -302   -921       O  
-HETATM 5025  O   HOH A1041      69.089 -15.434   6.333  1.00 51.71           O  
-ANISOU 5025  O   HOH A1041     6653   6611   6381    742    237    -90       O  
-HETATM 5026  O   HOH A1042      65.857   6.467  26.518  1.00 33.33           O  
-ANISOU 5026  O   HOH A1042     3329   5583   3751   1482   -137   1479       O  
-HETATM 5027  O   HOH A1043      63.854  -7.830  -7.115  1.00 41.84           O  
-ANISOU 5027  O   HOH A1043     5237   5070   5588    123   2298  -1541       O  
-HETATM 5028  O   HOH A1044      54.883  15.444  36.257  1.00 48.56           O  
-ANISOU 5028  O   HOH A1044     6576   6112   5761   -665    -22   -660       O  
-HETATM 5029  O   HOH A1045      54.229  39.203   8.280  1.00 44.67           O  
-ANISOU 5029  O   HOH A1045     5910   4169   6892   -163   -137   -393       O  
-HETATM 5030  O   HOH A1046      58.795  35.172   8.996  1.00 41.91           O  
-ANISOU 5030  O   HOH A1046     5159   5018   5745   1006   -472   -744       O  
-HETATM 5031  O   HOH A1047      40.208  -7.286  -4.312  1.00 43.33           O  
-ANISOU 5031  O   HOH A1047     6384   5730   4347   -717   -858   -788       O  
-HETATM 5032  O   HOH A1048      69.645 -18.734   7.167  1.00 47.07           O  
-ANISOU 5032  O   HOH A1048     5672   6232   5979    -98   -190    105       O  
-HETATM 5033  O   HOH A1049      56.532  32.071  32.460  1.00 52.64           O  
-ANISOU 5033  O   HOH A1049     6842   6727   6430    147    -91   -436       O  
-HETATM 5034  O   HOH A1050      61.015  16.321  33.053  1.00 38.66           O  
-ANISOU 5034  O   HOH A1050     5154   4961   4573   -168  -1366    375       O  
-HETATM 5035  O   HOH A1051      46.896 -23.314  16.484  1.00 37.38           O  
-ANISOU 5035  O   HOH A1051     5060   4971   4170  -1517  -1697    711       O  
-HETATM 5036  O   HOH A1052      60.959  29.754  17.135  1.00 36.30           O  
-ANISOU 5036  O   HOH A1052     3943   4527   5320   -898   -555   -282       O  
-HETATM 5037  O   HOH A1053      67.830  24.320  24.352  1.00 37.08           O  
-ANISOU 5037  O   HOH A1053     4305   4823   4959    191    -87   -210       O  
-HETATM 5038  O   HOH A1054      74.595  16.192  25.704  1.00 47.93           O  
-ANISOU 5038  O   HOH A1054     5561   5672   6979   -340    183    -25       O  
-HETATM 5039  O   HOH A1055      60.844  -2.428  23.612  1.00 41.30           O  
-ANISOU 5039  O   HOH A1055     5458   5096   5136    437  -1158    345       O  
-HETATM 5040  O   HOH A1056      57.467 -23.058   7.204  1.00 43.55           O  
-ANISOU 5040  O   HOH A1056     5223   5242   6082   -599    122   -183       O  
-HETATM 5041  O   HOH A1057      64.351  -6.858  -8.847  1.00 47.97           O  
-ANISOU 5041  O   HOH A1057     5976   6870   5380    127    885   -288       O  
-HETATM 5042  O   HOH A1058      38.322  -3.108  19.159  1.00 39.93           O  
-ANISOU 5042  O   HOH A1058     4577   5339   5253  -1465   1088    117       O  
-HETATM 5043  O   HOH A1059      55.795  18.317  35.725  1.00 47.45           O  
-ANISOU 5043  O   HOH A1059     6532   6409   5086   -152   -970   -217       O  
-HETATM 5044  O   HOH A1060      67.639  -9.337   0.921  1.00 51.61           O  
-ANISOU 5044  O   HOH A1060     6217   6474   6919    331    972   -611       O  
-HETATM 5045  O   HOH A1061      48.720  36.385   9.713  1.00 42.75           O  
-ANISOU 5045  O   HOH A1061     5543   6046   4654   -255    772   -341       O  
-HETATM 5046  O   HOH A1062      35.676  14.963  32.256  1.00 51.61           O  
-ANISOU 5046  O   HOH A1062     6203   7053   6351    362    517     30       O  
-HETATM 5047  O   HOH A1063      33.800  21.852  10.869  1.00 49.36           O  
-ANISOU 5047  O   HOH A1063     5981   6477   6297   -189   -655   -863       O  
-HETATM 5048  O   HOH A1064      35.053   5.994   4.797  1.00 52.00           O  
-ANISOU 5048  O   HOH A1064     7007   6308   6442    157   -298     37       O  
-HETATM 5049  O   HOH A1065      60.119  42.584   4.106  1.00 47.79           O  
-ANISOU 5049  O   HOH A1065     6067   5785   6307    313   -739   -441       O  
-HETATM 5050  O   HOH A1066      49.182 -11.311  -5.798  1.00 46.97           O  
-ANISOU 5050  O   HOH A1066     6513   6056   5278    355     61    120       O  
-HETATM 5051  O   HOH A1067      47.751  38.190  -0.893  1.00 48.68           O  
-ANISOU 5051  O   HOH A1067     6189   6095   6210    495    234    -99       O  
-HETATM 5052  O   HOH A1068      45.991 -15.011  -2.943  1.00 40.45           O  
-ANISOU 5052  O   HOH A1068     5896   5170   4303   -919   -647  -1299       O  
-HETATM 5053  O   HOH A1069      45.520  35.141   0.327  1.00 51.13           O  
-ANISOU 5053  O   HOH A1069     6429   6710   6289    640   -554    169       O  
-HETATM 5054  O   HOH A1070      31.840  -2.369   9.000  1.00 44.71           O  
-ANISOU 5054  O   HOH A1070     4964   5990   6033    490    351  -1155       O  
-HETATM 5055  O   HOH A1071      49.822  40.913  10.711  1.00 47.18           O  
-ANISOU 5055  O   HOH A1071     5978   5591   6357    622   -327    526       O  
-HETATM 5056  O   HOH A1072      59.478  40.596  -2.391  1.00 48.45           O  
-ANISOU 5056  O   HOH A1072     6641   5118   6648    670   -627    446       O  
-HETATM 5057  O   HOH A1073      60.917  -2.763  17.672  1.00 47.26           O  
-ANISOU 5057  O   HOH A1073     5376   5807   6774    634   -143    651       O  
-HETATM 5058  O   HOH A1074      63.612 -19.268  -8.854  1.00 43.17           O  
-ANISOU 5058  O   HOH A1074     5829   5023   5549   -247    917    142       O  
-HETATM 5059  O   HOH A1075      54.726  39.121  19.188  1.00 45.84           O  
-ANISOU 5059  O   HOH A1075     6014   4984   6419   -584   -100  -1030       O  
-HETATM 5060  O   HOH A1076      43.978  31.697   2.901  1.00 51.72           O  
-ANISOU 5060  O   HOH A1076     6099   6256   7294    236   -619     93       O  
-HETATM 5061  O   HOH A1077      37.950   3.478  27.948  1.00 52.11           O  
-ANISOU 5061  O   HOH A1077     6425   6564   6808   -354    438    486       O  
-HETATM 5062  O   HOH A1078      63.613  36.716   9.325  1.00 50.18           O  
-ANISOU 5062  O   HOH A1078     6784   6217   6063   -151    182   -481       O  
-HETATM 5063  O   HOH A1079      46.091  39.493   0.291  1.00 51.38           O  
-ANISOU 5063  O   HOH A1079     6549   6422   6550    167   -145    579       O  
-HETATM 5064  O   HOH A1080      31.745   1.373   3.514  1.00 50.68           O  
-ANISOU 5064  O   HOH A1080     6099   6719   6439    211    185   -639       O  
-HETATM 5065  O   HOH A1081      59.746  29.189  32.251  1.00 52.43           O  
-ANISOU 5065  O   HOH A1081     6696   6802   6423   -152   -558   -492       O  
-HETATM 5066  O   HOH A1082      46.670   3.357  -1.827  1.00 38.32           O  
-ANISOU 5066  O   HOH A1082     5220   3876   5465  -1436  -2171   -325       O  
-HETATM 5067  O   HOH A1083      40.057  15.930  36.874  1.00 28.71           O  
-ANISOU 5067  O   HOH A1083     3739   3883   3284     45   -209   -769       O  
-HETATM 5068  O   HOH A1084      57.305  19.651   4.795  1.00 32.69           O  
-ANISOU 5068  O   HOH A1084     3420   4034   4966   -498    237   1180       O  
-HETATM 5069  O   HOH A1085      68.410  23.703  13.385  1.00 33.53           O  
-ANISOU 5069  O   HOH A1085     3990   4678   4072   -496   -695  -1144       O  
-HETATM 5070  O   HOH A1086      49.037  26.288  27.340  1.00 34.93           O  
-ANISOU 5070  O   HOH A1086     4228   4260   4783   -182    301    -51       O  
-HETATM 5071  O   HOH A1087      49.911  30.097  27.919  1.00 33.82           O  
-ANISOU 5071  O   HOH A1087     5540   3440   3868   1133  -1578   -622       O  
-HETATM 5072  O   HOH A1088      53.576  20.101   8.729  1.00 29.37           O  
-ANISOU 5072  O   HOH A1088     4215   2157   4786    691    -55   -223       O  
-HETATM 5073  O   HOH A1089      37.905  23.240  35.378  1.00 36.19           O  
-ANISOU 5073  O   HOH A1089     5033   4860   3856   1161   -110    981       O  
-HETATM 5074  O   HOH A1090      61.102   6.627  32.424  1.00 36.51           O  
-ANISOU 5074  O   HOH A1090     5135   3897   4840   -574    712   -311       O  
-HETATM 5075  O   HOH A1091      40.304 -21.624  22.405  1.00 36.34           O  
-ANISOU 5075  O   HOH A1091     5868   4418   3519  -2014    478   -681       O  
-HETATM 5076  O   HOH A1092      40.658 -16.648  -0.747  1.00 37.36           O  
-ANISOU 5076  O   HOH A1092     4431   6165   3599      1   -997    -29       O  
-HETATM 5077  O   HOH A1093      64.268  26.772  25.345  1.00 42.63           O  
-ANISOU 5077  O   HOH A1093     5145   4331   6721    716  -1431    657       O  
-HETATM 5078  O   HOH A1094      58.132 -19.224   9.292  1.00 44.84           O  
-ANISOU 5078  O   HOH A1094     5739   6290   5009   -613   -297  -1022       O  
-HETATM 5079  O   HOH A1095      40.489 -10.557  16.987  1.00 45.14           O  
-ANISOU 5079  O   HOH A1095     6381   5195   5574   -247   -464   -226       O  
-HETATM 5080  O   HOH A1096      58.344  18.023  35.937  1.00 53.68           O  
-ANISOU 5080  O   HOH A1096     6976   6868   6551   -536    101   -493       O  
-HETATM 5081  O   HOH A1097      34.743  13.916  34.208  1.00 48.96           O  
-ANISOU 5081  O   HOH A1097     6279   6449   5874    229   -709    822       O  
-HETATM 5082  O   HOH A1098      69.915 -15.379  10.911  1.00 48.12           O  
-ANISOU 5082  O   HOH A1098     6067   5924   6293    966  -1135     83       O  
-HETATM 5083  O   HOH A1099      50.960  16.984  35.646  1.00 50.61           O  
-ANISOU 5083  O   HOH A1099     6134   6571   6524   -160   -179    -70       O  
-HETATM 5084  O   HOH A1100      35.251  20.717   9.504  1.00 50.29           O  
-ANISOU 5084  O   HOH A1100     5833   6334   6942   -109   -620   -347       O  
-HETATM 5085  O   HOH A1101      41.527 -12.002  17.955  1.00 52.94           O  
-ANISOU 5085  O   HOH A1101     7205   6570   6338    121    596    212       O  
-HETATM 5086  O   HOH A1102      66.002  -6.724  -7.043  1.00 50.35           O  
-ANISOU 5086  O   HOH A1102     6217   6334   6579   -709    659     85       O  
-HETATM 5087  O   HOH A1103      46.261  36.494  33.031  1.00 53.47           O  
-ANISOU 5087  O   HOH A1103     7005   6750   6560   -138   -101    103       O  
-HETATM 5088  O   HOH A1104      34.039  12.976  23.951  1.00 45.37           O  
-ANISOU 5088  O   HOH A1104     5702   6090   5444    764    659   -317       O  
-HETATM 5089  O   HOH A1105      48.389 -16.470  -4.067  1.00 53.62           O  
-ANISOU 5089  O   HOH A1105     7022   6724   6626    221   -158   -330       O  
-HETATM 5090  O   HOH A1106      62.883 -17.916   7.181  1.00 53.81           O  
-ANISOU 5090  O   HOH A1106     6967   6861   6618    328   -893    567       O  
-HETATM 5091  O   HOH A1107      66.846 -13.767   1.276  1.00 47.21           O  
-ANISOU 5091  O   HOH A1107     5757   5955   6224    148   -192   -186       O  
-HETATM 5092  O   HOH A1108      31.377  -4.387   5.935  1.00 53.17           O  
-ANISOU 5092  O   HOH A1108     6518   6801   6882    196   -469    -48       O  
-HETATM 5093  O   HOH A1109      54.160  40.577  15.510  1.00 54.57           O  
-ANISOU 5093  O   HOH A1109     7093   6690   6951    182     74    414       O  
-HETATM 5094  O   HOH A1110      35.195  -2.278  15.795  1.00 48.30           O  
-ANISOU 5094  O   HOH A1110     5984   6422   5946   1013    316     45       O  
-HETATM 5095  O   HOH A1111      61.992  27.977  28.011  1.00 49.03           O  
-ANISOU 5095  O   HOH A1111     6087   6575   5966   -584   -969   1317       O  
-HETATM 5096  O   HOH B 701      38.724  22.683  -6.848  1.00 24.48           O  
-ANISOU 5096  O   HOH B 701     3175   3746   2379   2001    345    214       O  
-HETATM 5097  O   HOH B 702      77.335   8.547   9.640  1.00 10.81           O  
-ANISOU 5097  O   HOH B 702      803   1188   2114    274   -128    140       O  
-HETATM 5098  O   HOH B 703      60.773   5.581 -10.095  1.00 32.08           O  
-ANISOU 5098  O   HOH B 703     2147   4657   5385    319   -403  -2974       O  
-HETATM 5099  O   HOH B 704      63.942  31.251  -8.447  1.00 15.75           O  
-ANISOU 5099  O   HOH B 704     2336   1368   2280   -283     -7     38       O  
-HETATM 5100  O   HOH B 705      68.979  11.542  -2.221  1.00 10.55           O  
-ANISOU 5100  O   HOH B 705     1218   1069   1722    172   -108   -102       O  
-HETATM 5101  O   HOH B 706      59.248  17.668  -5.907  1.00  9.84           O  
-ANISOU 5101  O   HOH B 706     1163    785   1791     92     91    -15       O  
-HETATM 5102  O   HOH B 707      57.631  22.500   5.414  1.00 24.60           O  
-ANISOU 5102  O   HOH B 707     3065   2411   3869    706    819    975       O  
-HETATM 5103  O   HOH B 708      74.671   9.809  10.675  1.00 14.01           O  
-ANISOU 5103  O   HOH B 708     1196   1640   2487    363   -396   -166       O  
-HETATM 5104  O   HOH B 709      65.436   7.383  -3.005  1.00 12.11           O  
-ANISOU 5104  O   HOH B 709     1333   1141   2128     97   -131     43       O  
-HETATM 5105  O   HOH B 710      49.395   3.304 -19.171  1.00 20.75           O  
-ANISOU 5105  O   HOH B 710     3147   2588   2148   -577   -628   -204       O  
-HETATM 5106  O   HOH B 711      69.313  14.469 -16.342  1.00 38.19           O  
-ANISOU 5106  O   HOH B 711     3432   6340   4736   1486   -546  -2592       O  
-HETATM 5107  O   HOH B 712      79.335  22.535  12.881  1.00 33.06           O  
-ANISOU 5107  O   HOH B 712     5024   3123   4415   1198   -689   -235       O  
-HETATM 5108  O   HOH B 713      51.302   6.931  -2.191  1.00 13.42           O  
-ANISOU 5108  O   HOH B 713     1674   1515   1909    -14   -105   -119       O  
-HETATM 5109  O   HOH B 714      63.250  15.304  -9.020  1.00 11.16           O  
-ANISOU 5109  O   HOH B 714     1315   1048   1877     46    138     22       O  
-HETATM 5110  O   HOH B 715      46.090  23.998 -17.679  1.00 15.35           O  
-ANISOU 5110  O   HOH B 715     2181   1614   2035      1    -39    -95       O  
-HETATM 5111  O   HOH B 716      44.794  12.077   4.558  1.00 12.36           O  
-ANISOU 5111  O   HOH B 716     1624   1426   1647    383    150    217       O  
-HETATM 5112  O   HOH B 717      75.246   9.516 -13.651  1.00 21.23           O  
-ANISOU 5112  O   HOH B 717     2037   2752   3278    292    885    -83       O  
-HETATM 5113  O   HOH B 718      46.965  16.279 -14.586  1.00 13.54           O  
-ANISOU 5113  O   HOH B 718     1955   1501   1689    398   -513    -55       O  
-HETATM 5114  O   HOH B 719      58.083  13.461   2.269  1.00 14.61           O  
-ANISOU 5114  O   HOH B 719     1851   1471   2229    534    159    173       O  
-HETATM 5115  O   HOH B 720      72.344  12.915  17.736  1.00 19.78           O  
-ANISOU 5115  O   HOH B 720     3056   1946   2514   1073   -762   -341       O  
-HETATM 5116  O   HOH B 721      51.640  13.221 -13.545  1.00 13.02           O  
-ANISOU 5116  O   HOH B 721     1401   1611   1936     22     54    -18       O  
-HETATM 5117  O   HOH B 722      66.904  20.916  17.414  1.00 15.27           O  
-ANISOU 5117  O   HOH B 722     1814   1335   2653    222   -322   -257       O  
-HETATM 5118  O   HOH B 723      66.727   5.432  -8.745  1.00 19.64           O  
-ANISOU 5118  O   HOH B 723     2375   2287   2800    487    320    352       O  
-HETATM 5119  O   HOH B 724      49.326  23.683 -18.790  1.00 16.54           O  
-ANISOU 5119  O   HOH B 724     2348   1691   2246    141    -64    519       O  
-HETATM 5120  O   HOH B 725      69.749  33.281  -4.273  1.00 21.03           O  
-ANISOU 5120  O   HOH B 725     2764   1950   3275   -644    152    154       O  
-HETATM 5121  O   HOH B 726      53.302  15.775 -10.457  1.00 13.77           O  
-ANISOU 5121  O   HOH B 726     1449   1371   2410    322    243     64       O  
-HETATM 5122  O   HOH B 727      52.850  11.127 -15.421  1.00 13.23           O  
-ANISOU 5122  O   HOH B 727     1627   1395   2005     77   -146     86       O  
-HETATM 5123  O   HOH B 728      49.919   8.276   1.505  1.00 11.48           O  
-ANISOU 5123  O   HOH B 728     1410   1448   1502    102     21   -283       O  
-HETATM 5124  O   HOH B 729      60.465  24.279 -10.524  1.00 16.52           O  
-ANISOU 5124  O   HOH B 729     2530   1801   1944    487    -80    111       O  
-HETATM 5125  O   HOH B 730      64.457  22.890  10.870  1.00 15.58           O  
-ANISOU 5125  O   HOH B 730     1806   1758   2354    192   -175    -83       O  
-HETATM 5126  O   HOH B 731      55.993  11.546  -6.342  1.00 17.21           O  
-ANISOU 5126  O   HOH B 731     1631   3365   1541   -727   -144    657       O  
-HETATM 5127  O   HOH B 732      74.955  24.679  -6.997  1.00 15.77           O  
-ANISOU 5127  O   HOH B 732     1493   1833   2667   -245    337    123       O  
-HETATM 5128  O   HOH B 733      62.119   8.284 -16.125  1.00 22.23           O  
-ANISOU 5128  O   HOH B 733     2397   2941   3106   -397   1227  -1070       O  
-HETATM 5129  O   HOH B 734      46.786   0.659 -12.833  1.00 18.64           O  
-ANISOU 5129  O   HOH B 734     3317   1512   2254    -54   -660   -218       O  
-HETATM 5130  O   HOH B 735      54.303  10.428 -18.522  1.00 15.62           O  
-ANISOU 5130  O   HOH B 735     2322   1465   2148    -36     -8   -364       O  
-HETATM 5131  O   HOH B 736      66.232  11.621  -2.965  1.00 11.55           O  
-ANISOU 5131  O   HOH B 736     1061   1230   2097    148    -85   -286       O  
-HETATM 5132  O   HOH B 737      70.413   4.506   8.776  1.00 16.17           O  
-ANISOU 5132  O   HOH B 737     1846   1573   2726     40    -14   -295       O  
-HETATM 5133  O   HOH B 738      61.196  33.969  -2.375  1.00 17.21           O  
-ANISOU 5133  O   HOH B 738     2152   1411   2975    110    188    214       O  
-HETATM 5134  O   HOH B 739      37.181   5.747  -7.510  1.00 16.94           O  
-ANISOU 5134  O   HOH B 739     1811   2465   2161   -261   -147    391       O  
-HETATM 5135  O   HOH B 740      62.419  28.838 -10.334  1.00 18.00           O  
-ANISOU 5135  O   HOH B 740     2198   1633   3009    379    465    575       O  
-HETATM 5136  O   HOH B 741      73.109  26.935   3.990  1.00 15.05           O  
-ANISOU 5136  O   HOH B 741     1790   1572   2355   -672   -392    -78       O  
-HETATM 5137  O   HOH B 742      44.132   1.060 -11.666  1.00 18.82           O  
-ANISOU 5137  O   HOH B 742     2480   2112   2558      1   -476   -256       O  
-HETATM 5138  O   HOH B 743      65.725  24.914 -13.731  1.00 17.35           O  
-ANISOU 5138  O   HOH B 743     2392   1920   2280   -368    258   -458       O  
-HETATM 5139  O   HOH B 744      43.082  19.392   1.954  1.00 20.49           O  
-ANISOU 5139  O   HOH B 744     1667   4076   2042     86    -29   -228       O  
-HETATM 5140  O   HOH B 745      39.445  10.246  -5.869  1.00 15.44           O  
-ANISOU 5140  O   HOH B 745     1504   2058   2304     54   -712    293       O  
-HETATM 5141  O   HOH B 746      75.183   6.659  -4.013  1.00 19.44           O  
-ANISOU 5141  O   HOH B 746     1997   1775   3613    -97    624    101       O  
-HETATM 5142  O   HOH B 747      75.251  27.478  -6.706  1.00 19.39           O  
-ANISOU 5142  O   HOH B 747     2027   2096   3243   -770    455     39       O  
-HETATM 5143  O   HOH B 748      45.721   1.375 -17.234  1.00 17.87           O  
-ANISOU 5143  O   HOH B 748     2531   1818   2440   -344   -543   -166       O  
-HETATM 5144  O   HOH B 749      67.906   4.471   7.345  1.00 15.10           O  
-ANISOU 5144  O   HOH B 749     1974   1589   2175   -293    248    -55       O  
-HETATM 5145  O   HOH B 750      58.501  11.028  -5.384  1.00 18.78           O  
-ANISOU 5145  O   HOH B 750     1447   2362   3325    531    285   1083       O  
-HETATM 5146  O   HOH B 751      73.936  25.236  -3.219  1.00 14.74           O  
-ANISOU 5146  O   HOH B 751     1411   1630   2559   -304    -27   -196       O  
-HETATM 5147  O   HOH B 752      57.879  21.213 -15.130  1.00 21.79           O  
-ANISOU 5147  O   HOH B 752     3876   2058   2346   -739    582   -347       O  
-HETATM 5148  O   HOH B 753      61.211   9.842   4.545  1.00 17.03           O  
-ANISOU 5148  O   HOH B 753     1906   1864   2700     12   -228    389       O  
-HETATM 5149  O   HOH B 754      73.720  22.774  -5.387  1.00 15.50           O  
-ANISOU 5149  O   HOH B 754     1636   1671   2581   -122    273    -47       O  
-HETATM 5150  O   HOH B 755      75.205   1.816  11.888  1.00 32.97           O  
-ANISOU 5150  O   HOH B 755     4547   2419   5559   1113  -1485   -548       O  
-HETATM 5151  O   HOH B 756      54.217  16.848 -15.227  1.00 14.74           O  
-ANISOU 5151  O   HOH B 756     1846   1707   2047     27    -18   -103       O  
-HETATM 5152  O   HOH B 757      65.848  20.909  14.281  1.00 21.70           O  
-ANISOU 5152  O   HOH B 757     2730   2254   3262    927   -882   -431       O  
-HETATM 5153  O   HOH B 758      68.469  23.968 -12.684  1.00 21.17           O  
-ANISOU 5153  O   HOH B 758     3329   2477   2238  -1105    777   -355       O  
-HETATM 5154  O   HOH B 759      68.558   5.364 -10.912  1.00 26.03           O  
-ANISOU 5154  O   HOH B 759     3612   3235   3044    214    594   -515       O  
-HETATM 5155  O   HOH B 760      65.701  20.301  -7.265  1.00 19.79           O  
-ANISOU 5155  O   HOH B 760     2651   2011   2857   -155   -680    116       O  
-HETATM 5156  O   HOH B 761      74.054  17.921  20.596  1.00 27.53           O  
-ANISOU 5156  O   HOH B 761     2508   3265   4686   -837  -1388   -387       O  
-HETATM 5157  O   HOH B 762      37.499   4.420 -10.013  1.00 17.83           O  
-ANISOU 5157  O   HOH B 762     1873   2538   2361   -144   -331    676       O  
-HETATM 5158  O   HOH B 763      74.809  31.258   0.037  1.00 26.90           O  
-ANISOU 5158  O   HOH B 763     3407   2281   4532   -789    475   -476       O  
-HETATM 5159  O   HOH B 764      65.289  -0.684   1.527  1.00 19.19           O  
-ANISOU 5159  O   HOH B 764     2316   1606   3368   -425     39     78       O  
-HETATM 5160  O   HOH B 765      48.751  -1.440 -20.459  1.00 24.87           O  
-ANISOU 5160  O   HOH B 765     3072   2830   3547    347   -382  -1129       O  
-HETATM 5161  O   HOH B 766      47.036  23.017 -20.290  1.00 20.19           O  
-ANISOU 5161  O   HOH B 766     2292   2048   3331    317    790    604       O  
-HETATM 5162  O   HOH B 767      72.772  19.510  15.933  1.00 18.76           O  
-ANISOU 5162  O   HOH B 767     2089   2273   2765   -155   -833   -179       O  
-HETATM 5163  O   HOH B 768      58.564  34.780  -7.574  1.00 23.10           O  
-ANISOU 5163  O   HOH B 768     4374   1909   2495   1054    712    264       O  
-HETATM 5164  O   HOH B 769      60.985   4.531  -2.684  1.00 16.41           O  
-ANISOU 5164  O   HOH B 769     1727   2095   2413     80   -112    286       O  
-HETATM 5165  O   HOH B 770      62.507  24.265 -17.416  1.00 25.50           O  
-ANISOU 5165  O   HOH B 770     3612   3622   2456    440    506    652       O  
-HETATM 5166  O   HOH B 771      53.373  35.548  -2.978  1.00 20.23           O  
-ANISOU 5166  O   HOH B 771     3104   1924   2658    667    -63    154       O  
-HETATM 5167  O   HOH B 772      72.041  22.696 -12.456  1.00 19.00           O  
-ANISOU 5167  O   HOH B 772     2561   1742   2915     35   -100    -99       O  
-HETATM 5168  O   HOH B 773      79.958  25.220  -0.009  1.00 26.08           O  
-ANISOU 5168  O   HOH B 773     1718   2682   5508   -576    -94    523       O  
-HETATM 5169  O   HOH B 774      76.880   9.707  -4.715  1.00 25.24           O  
-ANISOU 5169  O   HOH B 774     2129   3014   4446   -436   1232   -430       O  
-HETATM 5170  O   HOH B 775      73.863  20.102 -13.505  1.00 19.96           O  
-ANISOU 5170  O   HOH B 775     2079   2318   3185    176    692   -211       O  
-HETATM 5171  O   HOH B 776      55.290  29.144 -11.125  1.00 21.10           O  
-ANISOU 5171  O   HOH B 776     2784   2540   2691   1010   -225   -130       O  
-HETATM 5172  O   HOH B 777      48.737  23.384   3.130  1.00 17.05           O  
-ANISOU 5172  O   HOH B 777     1915   2088   2475    -79    264   -281       O  
-HETATM 5173  O   HOH B 778      69.781   3.622  -7.609  1.00 23.34           O  
-ANISOU 5173  O   HOH B 778     2424   2874   3569    160    231   -722       O  
-HETATM 5174  O   HOH B 779      36.957  14.886   2.585  1.00 23.47           O  
-ANISOU 5174  O   HOH B 779     2536   3987   2395    300    368    328       O  
-HETATM 5175  O   HOH B 780      55.729  25.790 -21.805  1.00 28.98           O  
-ANISOU 5175  O   HOH B 780     4002   2520   4487   -163    739    743       O  
-HETATM 5176  O   HOH B 781      64.794   2.815   4.488  1.00 16.89           O  
-ANISOU 5176  O   HOH B 781     1938   1982   2496     98    384    300       O  
-HETATM 5177  O   HOH B 782      65.115  14.885   6.976  1.00 19.01           O  
-ANISOU 5177  O   HOH B 782     1919   2042   3263    313    -18     59       O  
-HETATM 5178  O   HOH B 783      39.469   2.398  -6.107  1.00 21.72           O  
-ANISOU 5178  O   HOH B 783     3590   2170   2493   -637   -782    272       O  
-HETATM 5179  O   HOH B 784      59.752  20.567 -12.588  1.00 23.07           O  
-ANISOU 5179  O   HOH B 784     2329   4044   2393  -1256    -54    232       O  
-HETATM 5180  O   HOH B 785      69.882  21.962  15.810  1.00 28.47           O  
-ANISOU 5180  O   HOH B 785     3010   2866   4941   -131    -42   -560       O  
-HETATM 5181  O   HOH B 786      78.549  19.170  -6.677  1.00 29.32           O  
-ANISOU 5181  O   HOH B 786     2014   3241   5884    426     98    814       O  
-HETATM 5182  O   HOH B 787      58.455  19.200   1.967  1.00 19.68           O  
-ANISOU 5182  O   HOH B 787     1987   1798   3691   -108   -580   -585       O  
-HETATM 5183  O   HOH B 788      71.906   4.349  19.012  1.00 34.81           O  
-ANISOU 5183  O   HOH B 788     5042   3754   4428    618   -622    912       O  
-HETATM 5184  O   HOH B 789      63.407  30.432 -12.432  1.00 21.23           O  
-ANISOU 5184  O   HOH B 789     1957   2756   3351   -169     97   1287       O  
-HETATM 5185  O   HOH B 790      67.190   1.438   4.800  1.00 19.39           O  
-ANISOU 5185  O   HOH B 790     2335   2350   2680    333   -154    244       O  
-HETATM 5186  O   HOH B 791      63.334  29.127 -14.969  1.00 32.49           O  
-ANISOU 5186  O   HOH B 791     5173   3226   3944   -614   -602    609       O  
-HETATM 5187  O   HOH B 792      84.961  15.788   3.413  1.00 28.11           O  
-ANISOU 5187  O   HOH B 792     1603   3191   5886    256   -202   -111       O  
-HETATM 5188  O   HOH B 793      68.028  32.693 -13.360  1.00 25.97           O  
-ANISOU 5188  O   HOH B 793     3671   2339   3856   -722    918    852       O  
-HETATM 5189  O   HOH B 794      66.867  22.016  11.902  1.00 19.57           O  
-ANISOU 5189  O   HOH B 794     2221   2661   2552    484   -411   -315       O  
-HETATM 5190  O   HOH B 795      52.271  14.842 -24.280  1.00 33.85           O  
-ANISOU 5190  O   HOH B 795     5165   3621   4076   -206    -87  -1185       O  
-HETATM 5191  O   HOH B 796      41.572  17.080   4.719  1.00 22.30           O  
-ANISOU 5191  O   HOH B 796     2693   2887   2892    532     25   -370       O  
-HETATM 5192  O   HOH B 797      51.723  28.690  -8.340  1.00 24.03           O  
-ANISOU 5192  O   HOH B 797     3596   2290   3244     64   -200    697       O  
-HETATM 5193  O   HOH B 798      57.684   1.240 -12.248  1.00 24.42           O  
-ANISOU 5193  O   HOH B 798     3986   1612   3679    885  -1019   -135       O  
-HETATM 5194  O   HOH B 799      63.383  16.046 -21.823  1.00 32.35           O  
-ANISOU 5194  O   HOH B 799     3507   5410   3373    513   1887    191       O  
-HETATM 5195  O   HOH B 800      71.524  35.198   0.557  1.00 29.45           O  
-ANISOU 5195  O   HOH B 800     4222   2960   4006   -804    -15     20       O  
-HETATM 5196  O   HOH B 801      71.815   5.241 -19.995  1.00 27.03           O  
-ANISOU 5196  O   HOH B 801     2845   3093   4330    138    533    -94       O  
-HETATM 5197  O   HOH B 802      32.691  12.357 -27.676  1.00 35.49           O  
-ANISOU 5197  O   HOH B 802     4077   4814   4592   -635  -1318   -283       O  
-HETATM 5198  O   HOH B 803      66.727  18.882 -17.046  1.00 31.46           O  
-ANISOU 5198  O   HOH B 803     4085   4474   3395   -831   1207  -1438       O  
-HETATM 5199  O   HOH B 804      78.789  28.766   0.390  1.00 34.51           O  
-ANISOU 5199  O   HOH B 804     4313   4339   4461  -2473    312    467       O  
-HETATM 5200  O   HOH B 805      70.334   9.664  25.324  1.00 29.56           O  
-ANISOU 5200  O   HOH B 805     4250   3079   3903    378   -645  -1155       O  
-HETATM 5201  O   HOH B 806      34.710  14.041   1.240  1.00 24.41           O  
-ANISOU 5201  O   HOH B 806     1901   4173   3199    646    107    818       O  
-HETATM 5202  O   HOH B 807      76.858  28.467  -4.640  1.00 23.68           O  
-ANISOU 5202  O   HOH B 807     2466   2733   3797   -934    405    124       O  
-HETATM 5203  O   HOH B 808      69.330  27.848 -14.107  1.00 28.81           O  
-ANISOU 5203  O   HOH B 808     3222   3705   4020    206    825  -1174       O  
-HETATM 5204  O   HOH B 809      73.034   3.909   8.270  1.00 31.53           O  
-ANISOU 5204  O   HOH B 809     2666   4862   4450   1062    108    450       O  
-HETATM 5205  O   HOH B 810      64.385  16.384   9.112  1.00 21.36           O  
-ANISOU 5205  O   HOH B 810     2443   3056   2615   -238    -95     -4       O  
-HETATM 5206  O   HOH B 811      72.078  32.890  -6.037  1.00 26.46           O  
-ANISOU 5206  O   HOH B 811     3398   1936   4719   -798    238   -147       O  
-HETATM 5207  O   HOH B 812      56.281  14.119 -24.484  1.00 30.43           O  
-ANISOU 5207  O   HOH B 812     4586   4186   2788   1094   -447  -1279       O  
-HETATM 5208  O   HOH B 813      65.081  38.498  -4.954  1.00 27.74           O  
-ANISOU 5208  O   HOH B 813     4922   1559   4059   -898    154     32       O  
-HETATM 5209  O   HOH B 814      29.825  21.257 -10.654  1.00 35.49           O  
-ANISOU 5209  O   HOH B 814     3798   5230   4457   1965   -480   -678       O  
-HETATM 5210  O   HOH B 815      59.363   4.285  -4.859  1.00 22.23           O  
-ANISOU 5210  O   HOH B 815     1816   4390   2241   1048     85     37       O  
-HETATM 5211  O   HOH B 816      45.470  22.725 -23.828  1.00 28.86           O  
-ANISOU 5211  O   HOH B 816     2658   5177   3128    527   -566   -998       O  
-HETATM 5212  O   HOH B 817      76.494   8.547   0.008  1.00 26.28           O  
-ANISOU 5212  O   HOH B 817     3611   2325   4048    825    365    430       O  
-HETATM 5213  O   HOH B 818      72.873  22.205  13.442  1.00 25.54           O  
-ANISOU 5213  O   HOH B 818     3090   3102   3513   -597  -1002    303       O  
-HETATM 5214  O   HOH B 819      48.569  29.746  -1.900  1.00 25.14           O  
-ANISOU 5214  O   HOH B 819     2840   3494   3216    311    239   -394       O  
-HETATM 5215  O   HOH B 820      58.416  22.859 -19.806  1.00 28.38           O  
-ANISOU 5215  O   HOH B 820     3843   2849   4092   -367    359     90       O  
-HETATM 5216  O   HOH B 821      80.048  25.207   8.112  1.00 25.10           O  
-ANISOU 5216  O   HOH B 821     2899   2626   4013  -1163   -805    398       O  
-HETATM 5217  O   HOH B 822      70.462  27.665   6.580  1.00 30.40           O  
-ANISOU 5217  O   HOH B 822     3715   3678   4158   -620    230     -1       O  
-HETATM 5218  O   HOH B 823      37.167  17.299 -24.898  1.00 24.76           O  
-ANISOU 5218  O   HOH B 823     2653   3804   2951    405   -421   -343       O  
-HETATM 5219  O   HOH B 824      63.430  39.402   4.881  1.00 35.38           O  
-ANISOU 5219  O   HOH B 824     4871   3035   5536    682   -632  -1212       O  
-HETATM 5220  O   HOH B 825      75.758   2.973 -21.371  1.00 29.24           O  
-ANISOU 5220  O   HOH B 825     3195   2229   5685    571   1084   1376       O  
-HETATM 5221  O   HOH B 826      42.200  -1.095 -10.724  1.00 31.11           O  
-ANISOU 5221  O   HOH B 826     4570   3244   4004    643  -1698   -306       O  
-HETATM 5222  O   HOH B 827      75.084   3.679  -0.268  1.00 31.34           O  
-ANISOU 5222  O   HOH B 827     2000   5363   4543     65     80    -41       O  
-HETATM 5223  O   HOH B 828      74.048   4.475   3.528  1.00 28.89           O  
-ANISOU 5223  O   HOH B 828     3436   3368   4173    991   -242   -941       O  
-HETATM 5224  O   HOH B 829      35.546  18.940 -18.265  1.00 24.78           O  
-ANISOU 5224  O   HOH B 829     2490   3466   3459    764    350    714       O  
-HETATM 5225  O   HOH B 830      73.800  29.943  10.031  1.00 36.02           O  
-ANISOU 5225  O   HOH B 830     4529   4061   5095    984   -226  -1078       O  
-HETATM 5226  O   HOH B 831      45.959   8.619 -25.769  1.00 30.34           O  
-ANISOU 5226  O   HOH B 831     3648   5445   2435    -48   -199    -17       O  
-HETATM 5227  O   HOH B 832      77.720  26.471 -13.559  1.00 36.41           O  
-ANISOU 5227  O   HOH B 832     4215   4253   5367   -785   2203    998       O  
-HETATM 5228  O   HOH B 833      44.851  21.342   3.041  1.00 19.15           O  
-ANISOU 5228  O   HOH B 833     2321   2452   2504    370    127   -325       O  
-HETATM 5229  O   HOH B 834      54.801   8.927 -20.794  1.00 25.66           O  
-ANISOU 5229  O   HOH B 834     3161   3972   2616    541   -283   -229       O  
-HETATM 5230  O   HOH B 835      69.246  34.852 -11.605  1.00 33.67           O  
-ANISOU 5230  O   HOH B 835     5088   3289   4417   -229     58    530       O  
-HETATM 5231  O   HOH B 836      51.947  34.720  -5.378  1.00 26.02           O  
-ANISOU 5231  O   HOH B 836     4187   2776   2923    311    -11    246       O  
-HETATM 5232  O   HOH B 837      76.388  22.466  13.440  1.00 36.15           O  
-ANISOU 5232  O   HOH B 837     5826   3984   3924   -873   -205   -927       O  
-HETATM 5233  O   HOH B 838      72.862  23.223  10.673  1.00 31.28           O  
-ANISOU 5233  O   HOH B 838     4134   3262   4489  -1612  -1984    792       O  
-HETATM 5234  O   HOH B 839      66.172  39.358  -7.155  1.00 33.72           O  
-ANISOU 5234  O   HOH B 839     5214   2734   4865    295   1058    746       O  
-HETATM 5235  O   HOH B 840      53.900  13.079 -22.105  1.00 28.47           O  
-ANISOU 5235  O   HOH B 840     3602   2940   4273   -220    565   -544       O  
-HETATM 5236  O   HOH B 841      81.290  10.996   1.183  1.00 35.07           O  
-ANISOU 5236  O   HOH B 841     3633   5621   4070   1066    621    360       O  
-HETATM 5237  O   HOH B 842      43.458  15.306 -26.692  1.00 30.12           O  
-ANISOU 5237  O   HOH B 842     4406   4515   2522   1395    124    232       O  
-HETATM 5238  O   HOH B 843      73.022  11.984 -18.646  1.00 27.36           O  
-ANISOU 5238  O   HOH B 843     2369   4010   4014    193    727   -773       O  
-HETATM 5239  O   HOH B 844      64.071  10.287   4.660  1.00 19.65           O  
-ANISOU 5239  O   HOH B 844     2109   2379   2976    594   -121    431       O  
-HETATM 5240  O   HOH B 845      71.568  33.998  -8.632  1.00 32.37           O  
-ANISOU 5240  O   HOH B 845     4449   3148   4703  -1396    151   -271       O  
-HETATM 5241  O   HOH B 846      48.889  31.815  -3.773  1.00 32.01           O  
-ANISOU 5241  O   HOH B 846     4250   2798   5114    463   -637    333       O  
-HETATM 5242  O   HOH B 847      77.393  15.720  14.497  1.00 28.82           O  
-ANISOU 5242  O   HOH B 847     2991   3450   4510   -949   -476   -111       O  
-HETATM 5243  O   HOH B 848      81.837  12.573   3.462  1.00 29.46           O  
-ANISOU 5243  O   HOH B 848     2995   3851   4345    802    287   -272       O  
-HETATM 5244  O   HOH B 849      66.130   9.256 -20.759  1.00 26.68           O  
-ANISOU 5244  O   HOH B 849     2684   4450   3001    323    396  -1182       O  
-HETATM 5245  O   HOH B 850      35.498  22.625  -0.941  1.00 33.38           O  
-ANISOU 5245  O   HOH B 850     3203   5820   3661   1756   -134  -1386       O  
-HETATM 5246  O   HOH B 851      38.803  18.705 -26.986  1.00 28.85           O  
-ANISOU 5246  O   HOH B 851     3257   3894   3810    329     66    779       O  
-HETATM 5247  O   HOH B 852      53.384   6.560 -21.679  1.00 38.97           O  
-ANISOU 5247  O   HOH B 852     6561   4274   3973    727    119     10       O  
-HETATM 5248  O   HOH B 853      78.929  26.801  -7.867  1.00 33.57           O  
-ANISOU 5248  O   HOH B 853     3140   3773   5842  -1691    431    306       O  
-HETATM 5249  O   HOH B 854      77.409  30.697  12.728  1.00 37.37           O  
-ANISOU 5249  O   HOH B 854     5033   4642   4524   -375    178   -626       O  
-HETATM 5250  O   HOH B 855      63.114  34.948 -13.768  1.00 36.97           O  
-ANISOU 5250  O   HOH B 855     4893   5458   3695  -1180   -438    613       O  
-HETATM 5251  O   HOH B 856      63.038   6.076  -1.897  1.00 22.71           O  
-ANISOU 5251  O   HOH B 856     2836   2810   2983   -482   -228    113       O  
-HETATM 5252  O   HOH B 857      65.979  22.790 -17.348  1.00 33.98           O  
-ANISOU 5252  O   HOH B 857     4950   4985   2975  -1264   1638   -416       O  
-HETATM 5253  O   HOH B 858      50.970  32.069  -6.043  1.00 30.63           O  
-ANISOU 5253  O   HOH B 858     3200   4026   4410   1047   -869   -505       O  
-HETATM 5254  O   HOH B 859      68.823  30.034   9.981  1.00 37.82           O  
-ANISOU 5254  O   HOH B 859     4984   4132   5252   -995     62   -410       O  
-HETATM 5255  O   HOH B 860      65.213  27.392  11.912  1.00 36.41           O  
-ANISOU 5255  O   HOH B 860     5597   3659   4579  -2187    940  -1268       O  
-HETATM 5256  O   HOH B 861      65.446   3.191  -9.032  1.00 34.70           O  
-ANISOU 5256  O   HOH B 861     4696   3519   4967   -699    890  -1208       O  
-HETATM 5257  O   HOH B 862      75.257   8.596  -6.738  1.00 28.63           O  
-ANISOU 5257  O   HOH B 862     2990   4550   3336   -356    378    -60       O  
-HETATM 5258  O   HOH B 863      71.376   7.722 -16.464  1.00 33.87           O  
-ANISOU 5258  O   HOH B 863     3466   4064   5338   -779    941   -332       O  
-HETATM 5259  O   HOH B 864      33.008  19.175 -19.255  1.00 34.10           O  
-ANISOU 5259  O   HOH B 864     3649   5360   3948   1143     44    529       O  
-HETATM 5260  O   HOH B 865      59.651  37.348  -7.468  1.00 37.52           O  
-ANISOU 5260  O   HOH B 865     5341   3970   4944   -111    147   1002       O  
-HETATM 5261  O   HOH B 866      34.942   4.575  -6.620  1.00 34.45           O  
-ANISOU 5261  O   HOH B 866     3749   4556   4784  -1081   -113   1630       O  
-HETATM 5262  O   HOH B 867      63.093   2.506  -3.392  1.00 33.81           O  
-ANISOU 5262  O   HOH B 867     3868   3505   5472    227   -119   1832       O  
-HETATM 5263  O   HOH B 868      50.863  29.677 -16.809  1.00 32.53           O  
-ANISOU 5263  O   HOH B 868     4277   3891   4193   -365   -523    101       O  
-HETATM 5264  O   HOH B 869      31.004  13.171 -25.689  1.00 43.57           O  
-ANISOU 5264  O   HOH B 869     4997   6210   5347   -266  -1083    492       O  
-HETATM 5265  O   HOH B 870      71.280  14.203 -19.020  1.00 30.18           O  
-ANISOU 5265  O   HOH B 870     2277   3674   5517    234     84    136       O  
-HETATM 5266  O   HOH B 871      49.578  -4.394 -16.774  1.00 38.01           O  
-ANISOU 5266  O   HOH B 871     5057   4873   4510   -290    602  -1427       O  
-HETATM 5267  O   HOH B 872      73.614  -1.974  -1.269  1.00 37.25           O  
-ANISOU 5267  O   HOH B 872     4351   3560   6241   1312   1353     89       O  
-HETATM 5268  O   HOH B 873      78.836  18.984 -12.546  1.00 29.49           O  
-ANISOU 5268  O   HOH B 873     3810   3067   4329   -725   1268   -270       O  
-HETATM 5269  O   HOH B 874      36.814  13.408   4.929  1.00 31.43           O  
-ANISOU 5269  O   HOH B 874     2834   5111   3997   -162    395    892       O  
-HETATM 5270  O   HOH B 875      60.180  21.121 -20.277  1.00 35.84           O  
-ANISOU 5270  O   HOH B 875     5882   2806   4929    451   1523   1359       O  
-HETATM 5271  O   HOH B 876      43.800  24.064 -29.982  1.00 36.56           O  
-ANISOU 5271  O   HOH B 876     4937   4155   4800  -1019   -340    648       O  
-HETATM 5272  O   HOH B 877      32.997  15.126   2.932  1.00 43.35           O  
-ANISOU 5272  O   HOH B 877     5428   5622   5419    952    619   -201       O  
-HETATM 5273  O   HOH B 878      78.668   3.726  12.728  1.00 38.14           O  
-ANISOU 5273  O   HOH B 878     3957   4806   5728   1418   -114    461       O  
-HETATM 5274  O   HOH B 879      85.361  20.560   7.754  1.00 37.20           O  
-ANISOU 5274  O   HOH B 879     4706   4936   4491  -1523  -1048   -388       O  
-HETATM 5275  O   HOH B 880      36.505  17.735   4.055  1.00 40.46           O  
-ANISOU 5275  O   HOH B 880     4722   6094   4558   -280   1842   -109       O  
-HETATM 5276  O   HOH B 881      75.046   9.354  19.176  1.00 31.43           O  
-ANISOU 5276  O   HOH B 881     2414   5892   3635  -1234   -626     67       O  
-HETATM 5277  O   HOH B 882      34.730   7.241 -27.008  1.00 33.35           O  
-ANISOU 5277  O   HOH B 882     3925   5117   3629   -672  -1339   -335       O  
-HETATM 5278  O   HOH B 883      55.036  10.597 -23.125  1.00 29.49           O  
-ANISOU 5278  O   HOH B 883     3167   4917   3122    187   -179   -737       O  
-HETATM 5279  O   HOH B 884      76.837   6.141   8.074  1.00 33.01           O  
-ANISOU 5279  O   HOH B 884     4479   3949   4112   -666    -67    543       O  
-HETATM 5280  O   HOH B 885      75.264  31.013   3.825  1.00 36.52           O  
-ANISOU 5280  O   HOH B 885     4433   3440   6001  -1051  -1545   -317       O  
-HETATM 5281  O   HOH B 886      48.533  12.210 -24.048  1.00 30.21           O  
-ANISOU 5281  O   HOH B 886     4479   3649   3350    506    844    189       O  
-HETATM 5282  O   HOH B 887      75.551  12.084  18.746  1.00 42.38           O  
-ANISOU 5282  O   HOH B 887     5816   4989   5295   -716   -229   -887       O  
-HETATM 5283  O   HOH B 888      43.698  29.697 -18.051  1.00 39.19           O  
-ANISOU 5283  O   HOH B 888     4808   4294   5786   1472    -89    351       O  
-HETATM 5284  O   HOH B 889      65.367  27.056 -15.334  1.00 30.58           O  
-ANISOU 5284  O   HOH B 889     5682   2666   3271   -511    226    491       O  
-HETATM 5285  O   HOH B 890      76.227   5.865  -1.506  1.00 31.72           O  
-ANISOU 5285  O   HOH B 890     2575   5051   4427    273    103   1189       O  
-HETATM 5286  O   HOH B 891      74.754  14.333  17.789  1.00 32.29           O  
-ANISOU 5286  O   HOH B 891     3897   5168   3202  -1587    457  -1000       O  
-HETATM 5287  O   HOH B 892      46.363   3.671 -24.882  1.00 35.19           O  
-ANISOU 5287  O   HOH B 892     4957   4395   4018   -119   -426   -392       O  
-HETATM 5288  O   HOH B 893      63.212  40.042  -3.791  1.00 30.49           O  
-ANISOU 5288  O   HOH B 893     4541   2716   4327    377    329    503       O  
-HETATM 5289  O   HOH B 894      78.880  11.562  17.052  1.00 41.85           O  
-ANISOU 5289  O   HOH B 894     4892   6082   4926    689  -1614   -958       O  
-HETATM 5290  O   HOH B 895      70.175   1.267  -4.529  1.00 34.94           O  
-ANISOU 5290  O   HOH B 895     5739   3512   4024  -2162   -411    522       O  
-HETATM 5291  O   HOH B 896      64.940   4.222  -1.274  1.00 25.95           O  
-ANISOU 5291  O   HOH B 896     1996   3880   3983    358   -684  -1210       O  
-HETATM 5292  O   HOH B 897      69.513   2.973 -10.384  1.00 38.11           O  
-ANISOU 5292  O   HOH B 897     5368   5078   4035    255    761   -186       O  
-HETATM 5293  O   HOH B 898      40.456   4.294 -27.062  1.00 32.86           O  
-ANISOU 5293  O   HOH B 898     4628   4140   3715   -168  -1493   -479       O  
-HETATM 5294  O   HOH B 899      59.626  24.454 -17.790  1.00 27.74           O  
-ANISOU 5294  O   HOH B 899     3858   4266   2414   -359    114    -15       O  
-HETATM 5295  O   HOH B 900      60.563  32.436 -15.327  1.00 44.43           O  
-ANISOU 5295  O   HOH B 900     6485   4850   5546   -214    194    942       O  
-HETATM 5296  O   HOH B 901      33.884  11.544   1.996  1.00 31.43           O  
-ANISOU 5296  O   HOH B 901     3198   4663   4079    -14    175   1065       O  
-HETATM 5297  O   HOH B 902      60.455   8.434 -18.623  1.00 32.63           O  
-ANISOU 5297  O   HOH B 902     4291   3996   4111   1079     19   -359       O  
-HETATM 5298  O   HOH B 903      53.442   9.228 -24.985  1.00 38.80           O  
-ANISOU 5298  O   HOH B 903     4884   5879   3980    200    -10   -713       O  
-HETATM 5299  O   HOH B 904      68.554  11.166 -22.752  1.00 33.80           O  
-ANISOU 5299  O   HOH B 904     4610   4776   3457   1585    -76    110       O  
-HETATM 5300  O   HOH B 905      35.446   0.839 -20.368  1.00 34.80           O  
-ANISOU 5300  O   HOH B 905     4589   3302   5331  -1661    137   -347       O  
-HETATM 5301  O   HOH B 906      40.742  25.536  -3.706  1.00 34.57           O  
-ANISOU 5301  O   HOH B 906     5445   3920   3768   1996   -440    164       O  
-HETATM 5302  O   HOH B 907      71.341  34.320  -2.014  1.00 35.41           O  
-ANISOU 5302  O   HOH B 907     4273   4424   4758  -1192    688   -965       O  
-HETATM 5303  O   HOH B 908      62.205  32.513 -13.252  1.00 30.61           O  
-ANISOU 5303  O   HOH B 908     5324   2731   3574    731    593     44       O  
-HETATM 5304  O   HOH B 909      79.226   8.408  11.547  1.00 32.32           O  
-ANISOU 5304  O   HOH B 909     3608   4132   4538    424   -744    255       O  
-HETATM 5305  O   HOH B 910      73.659   1.384   9.558  1.00 42.74           O  
-ANISOU 5305  O   HOH B 910     5371   5144   5724    942    254   -654       O  
-HETATM 5306  O   HOH B 911      65.483   3.508  -4.223  1.00 32.23           O  
-ANISOU 5306  O   HOH B 911     3121   3515   5610   -731    -55   -737       O  
-HETATM 5307  O   HOH B 912      37.865   7.913 -32.311  1.00 42.70           O  
-ANISOU 5307  O   HOH B 912     5774   5097   5352   -954    439    907       O  
-HETATM 5308  O   HOH B 913      52.639  -3.470  -7.876  1.00 35.62           O  
-ANISOU 5308  O   HOH B 913     5322   3297   4914   1455   1371   1099       O  
-HETATM 5309  O   HOH B 914      82.052   9.999  11.171  1.00 47.69           O  
-ANISOU 5309  O   HOH B 914     5496   6265   6358   1524   -100    740       O  
-HETATM 5310  O   HOH B 915      81.236  26.553  -6.187  1.00 41.31           O  
-ANISOU 5310  O   HOH B 915     4694   4836   6166   -695    634   -862       O  
-HETATM 5311  O   HOH B 916      72.028  26.518 -13.726  1.00 30.12           O  
-ANISOU 5311  O   HOH B 916     3752   4456   3234     80   -192     84       O  
-HETATM 5312  O   HOH B 917      35.979  10.696   3.925  1.00 41.49           O  
-ANISOU 5312  O   HOH B 917     4519   5531   5715    483    722   1406       O  
-HETATM 5313  O   HOH B 918      80.529  22.018  -3.173  1.00 35.40           O  
-ANISOU 5313  O   HOH B 918     2799   6126   4526    434   1185    570       O  
-HETATM 5314  O   HOH B 919      32.034  20.970 -13.731  1.00 39.66           O  
-ANISOU 5314  O   HOH B 919     5538   4888   4644    660    -18    151       O  
-HETATM 5315  O   HOH B 920      60.680   5.211 -16.086  1.00 31.60           O  
-ANISOU 5315  O   HOH B 920     3607   3554   4845    778    548   -589       O  
-HETATM 5316  O   HOH B 921      58.416  24.629 -21.855  1.00 37.95           O  
-ANISOU 5316  O   HOH B 921     4819   4235   5366   -944    805    417       O  
-HETATM 5317  O   HOH B 922      89.167  19.584   2.349  1.00 47.78           O  
-ANISOU 5317  O   HOH B 922     5715   6246   6193    525  -1174    239       O  
-HETATM 5318  O   HOH B 923      78.343  29.551  -1.900  1.00 33.20           O  
-ANISOU 5318  O   HOH B 923     3080   4570   4964  -1248     94   -160       O  
-HETATM 5319  O   HOH B 924      83.101  27.232   7.086  1.00 36.35           O  
-ANISOU 5319  O   HOH B 924     3443   5507   4860    -68  -1270    548       O  
-HETATM 5320  O   HOH B 925      75.495   7.780   2.195  1.00 31.84           O  
-ANISOU 5320  O   HOH B 925     3560   4372   4164    242    693     75       O  
-HETATM 5321  O   HOH B 926      36.602  25.486  -4.276  1.00 46.54           O  
-ANISOU 5321  O   HOH B 926     5918   5514   6252    117     22   -877       O  
-HETATM 5322  O   HOH B 927      81.384  27.476   0.345  1.00 34.79           O  
-ANISOU 5322  O   HOH B 927     3976   3195   6047  -1316     86   -351       O  
-HETATM 5323  O   HOH B 928      67.435  -1.088   4.191  1.00 34.28           O  
-ANISOU 5323  O   HOH B 928     5483   3056   4485  -1225   1441   -936       O  
-HETATM 5324  O   HOH B 929      56.079  33.974  -8.972  1.00 34.84           O  
-ANISOU 5324  O   HOH B 929     4580   4347   4308  -1475   -480   1396       O  
-HETATM 5325  O   HOH B 930      60.231   1.227 -10.993  1.00 32.74           O  
-ANISOU 5325  O   HOH B 930     4099   3461   4878    580   -822  -1878       O  
-HETATM 5326  O   HOH B 931      84.355  13.314   4.173  1.00 34.71           O  
-ANISOU 5326  O   HOH B 931     2491   4672   6024    146    279    825       O  
-HETATM 5327  O   HOH B 932      55.548   4.674 -21.761  1.00 46.59           O  
-ANISOU 5327  O   HOH B 932     6027   5439   6234    605    745   -501       O  
-HETATM 5328  O   HOH B 933      77.182   5.529   3.156  1.00 39.76           O  
-ANISOU 5328  O   HOH B 933     4685   5281   5142   1047   -770   -257       O  
-HETATM 5329  O   HOH B 934      82.691  12.557  10.617  1.00 40.49           O  
-ANISOU 5329  O   HOH B 934     4845   5381   5156    330  -1220    643       O  
-HETATM 5330  O   HOH B 935      71.595   6.618  24.782  1.00 37.46           O  
-ANISOU 5330  O   HOH B 935     5067   4320   4845    906   -756   1225       O  
-HETATM 5331  O   HOH B 936      70.707   2.265   5.801  1.00 38.30           O  
-ANISOU 5331  O   HOH B 936     4836   4609   5107   -583    162    185       O  
-HETATM 5332  O   HOH B 937      73.043  28.908 -13.127  1.00 32.90           O  
-ANISOU 5332  O   HOH B 937     3744   4098   4658    720    346    132       O  
-HETATM 5333  O   HOH B 938      36.211   1.985 -10.150  1.00 38.54           O  
-ANISOU 5333  O   HOH B 938     4724   3806   6114  -2104    655   -442       O  
-HETATM 5334  O   HOH B 939      76.581   1.400   0.324  1.00 43.11           O  
-ANISOU 5334  O   HOH B 939     5266   5730   5384    438   -395   -132       O  
-HETATM 5335  O   HOH B 940      82.883  16.086  11.092  1.00 39.08           O  
-ANISOU 5335  O   HOH B 940     5082   4873   4894   -485  -1493   -342       O  
-HETATM 5336  O   HOH B 941      69.843  32.033 -15.246  1.00 43.01           O  
-ANISOU 5336  O   HOH B 941     6180   5094   5067   -195    662     54       O  
-HETATM 5337  O   HOH B 942      67.238  -2.986   0.422  1.00 39.87           O  
-ANISOU 5337  O   HOH B 942     5132   3955   6060   -160    964    755       O  
-HETATM 5338  O   HOH B 943      73.553   3.980 -21.942  1.00 38.48           O  
-ANISOU 5338  O   HOH B 943     4487   4628   5504  -1091    945    692       O  
-HETATM 5339  O   HOH B 944      45.657  28.351   1.725  1.00 36.25           O  
-ANISOU 5339  O   HOH B 944     3693   4959   5119   -973   -519    -94       O  
-HETATM 5340  O   HOH B 945      41.120  25.179  -0.301  1.00 38.17           O  
-ANISOU 5340  O   HOH B 945     5122   4403   4979   2157    763   -590       O  
-HETATM 5341  O   HOH B 946      57.796   0.281  -7.761  1.00 41.77           O  
-ANISOU 5341  O   HOH B 946     6639   4417   4814    290   -160    633       O  
-HETATM 5342  O   HOH B 947      55.073  -3.310  -7.207  1.00 43.01           O  
-ANISOU 5342  O   HOH B 947     5625   5329   5388   -128  -1060    -86       O  
-HETATM 5343  O   HOH B 948      57.068  29.077 -17.405  1.00 38.19           O  
-ANISOU 5343  O   HOH B 948     4961   5371   4176   -121   -330   1053       O  
-HETATM 5344  O   HOH B 949      76.661   5.437  19.544  1.00 40.93           O  
-ANISOU 5344  O   HOH B 949     5210   5534   4807    509   -972    256       O  
-HETATM 5345  O   HOH B 950      41.715  25.340 -31.635  1.00 49.19           O  
-ANISOU 5345  O   HOH B 950     6421   5921   6348   -151   -261     45       O  
-HETATM 5346  O   HOH B 951      34.194   9.735 -28.698  1.00 49.37           O  
-ANISOU 5346  O   HOH B 951     6121   6149   6488    183   -557   -824       O  
-HETATM 5347  O   HOH B 952      87.053  16.534   5.347  1.00 40.91           O  
-ANISOU 5347  O   HOH B 952     3797   5878   5870   -107  -1247   -309       O  
-HETATM 5348  O   HOH B 953      73.148   2.608   5.046  1.00 49.06           O  
-ANISOU 5348  O   HOH B 953     6115   6198   6326    680   -533    712       O  
-HETATM 5349  O   HOH B 954      72.898  24.548 -14.704  1.00 44.77           O  
-ANISOU 5349  O   HOH B 954     5553   5104   6353    235    371    756       O  
-HETATM 5350  O   HOH B 955      52.702  -2.026 -19.557  1.00 46.19           O  
-ANISOU 5350  O   HOH B 955     5957   5138   6455    549    345   -727       O  
-HETATM 5351  O   HOH B 956      80.189  19.219  -9.030  1.00 35.02           O  
-ANISOU 5351  O   HOH B 956     3787   4402   5115   -361   1278  -1021       O  
-HETATM 5352  O   HOH B 957      58.602  14.193 -25.728  1.00 41.21           O  
-ANISOU 5352  O   HOH B 957     5351   5748   4559    772    731  -1041       O  
-HETATM 5353  O   HOH B 958      55.184  21.999   5.322  1.00 38.19           O  
-ANISOU 5353  O   HOH B 958     5294   3716   5498   -304    415  -2139       O  
-HETATM 5354  O   HOH B 959      68.999  -2.500   2.758  1.00 47.86           O  
-ANISOU 5354  O   HOH B 959     6119   5943   6121    435    698   -484       O  
-HETATM 5355  O   HOH B 960      65.941  33.706 -14.808  1.00 43.70           O  
-ANISOU 5355  O   HOH B 960     5565   5853   5186    -28   -593    606       O  
-HETATM 5356  O   HOH B 961      60.210   2.335  -6.721  1.00 21.73           O  
-ANISOU 5356  O   HOH B 961     3508   2272   2477    -28    -26    -95       O  
-HETATM 5357  O   HOH B 962      61.255   2.966  -9.209  1.00 23.28           O  
-ANISOU 5357  O   HOH B 962     3213   3277   2355    -40    271   -498       O  
-HETATM 5358  O   HOH B 963      69.519   8.829 -24.465  1.00 41.11           O  
-ANISOU 5358  O   HOH B 963     4932   5913   4773    226    -29   -495       O  
-HETATM 5359  O   HOH B 964      72.210  30.865   1.060  1.00 21.01           O  
-ANISOU 5359  O   HOH B 964     2546   2166   3270   -624   -260   -382       O  
-HETATM 5360  O   HOH B 965      71.184  31.239  -1.494  1.00 19.99           O  
-ANISOU 5360  O   HOH B 965     2604   1795   3197   -193   -257   -216       O  
-HETATM 5361  O   HOH B 966      72.826  29.709   3.483  1.00 23.77           O  
-ANISOU 5361  O   HOH B 966     3697   1395   3937   -201   -670   -164       O  
-HETATM 5362  O   HOH B 967      40.222  24.684  -6.074  1.00 23.81           O  
-ANISOU 5362  O   HOH B 967     2833   3445   2769   1349     64    485       O  
-HETATM 5363  O   HOH B 968      62.888   5.725 -15.275  1.00 21.69           O  
-ANISOU 5363  O   HOH B 968     2468   2132   3640   -365    704  -1010       O  
-HETATM 5364  O   HOH B 969      68.640  17.266 -16.486  1.00 26.77           O  
-ANISOU 5364  O   HOH B 969     3819   3631   2721   -726    416   -336       O  
-HETATM 5365  O   HOH B 970      61.976   6.575 -13.078  1.00 22.71           O  
-ANISOU 5365  O   HOH B 970     2714   2453   3462    358    506   -540       O  
-HETATM 5366  O   HOH B 971      44.763  25.232   2.215  1.00 29.51           O  
-ANISOU 5366  O   HOH B 971     3221   4302   3690   -147  -1079   -281       O  
-HETATM 5367  O   HOH B 972      74.187   7.956 -15.776  1.00 27.02           O  
-ANISOU 5367  O   HOH B 972     2332   4817   3117    225    920    -42       O  
-HETATM 5368  O   HOH B 973      80.514  24.603  11.557  1.00 32.22           O  
-ANISOU 5368  O   HOH B 973     4696   2863   4683   -204  -1379   -539       O  
-HETATM 5369  O   HOH B 974      46.187  25.600  -3.484  1.00 30.83           O  
-ANISOU 5369  O   HOH B 974     4541   3846   3326   1580   1081   1037       O  
-HETATM 5370  O   HOH B 975      67.601  28.352   5.221  1.00 33.76           O  
-ANISOU 5370  O   HOH B 975     2398   7855   2572    365   -375   -487       O  
-HETATM 5371  O   HOH B 976      74.666   5.836   7.764  1.00 35.55           O  
-ANISOU 5371  O   HOH B 976     4036   3391   6078      0   -159  -1034       O  
-HETATM 5372  O   HOH B 977      51.096   3.659 -21.201  1.00 39.82           O  
-ANISOU 5372  O   HOH B 977     4701   5435   4993    225     54   -497       O  
-HETATM 5373  O   HOH B 978      55.727  30.983 -13.039  1.00 38.67           O  
-ANISOU 5373  O   HOH B 978     5717   4261   4716     85    763   -480       O  
-HETATM 5374  O   HOH B 979      41.609   6.879 -29.294  1.00 40.79           O  
-ANISOU 5374  O   HOH B 979     5562   4590   5345   1278    920   -431       O  
-HETATM 5375  O   HOH B 980      45.099   0.077  -4.865  1.00 33.41           O  
-ANISOU 5375  O   HOH B 980     3903   3468   5323    428    -40    865       O  
-HETATM 5376  O   HOH B 981      82.907  27.937   2.547  1.00 31.65           O  
-ANISOU 5376  O   HOH B 981     2645   4405   4974   -506    -27    438       O  
-HETATM 5377  O   HOH B 982      79.978  17.228 -11.192  1.00 42.20           O  
-ANISOU 5377  O   HOH B 982     4786   5748   5498    -16    444    -62       O  
-HETATM 5378  O   HOH B 983      52.677  24.338 -25.732  1.00 42.99           O  
-ANISOU 5378  O   HOH B 983     6209   5414   4710   1047   -484    211       O  
-HETATM 5379  O   HOH B 984      33.783   4.287   0.059  1.00 46.27           O  
-ANISOU 5379  O   HOH B 984     5446   6304   5830    266    751    770       O  
-HETATM 5380  O   HOH B 985      55.917  -0.069 -10.810  1.00 40.16           O  
-ANISOU 5380  O   HOH B 985     4688   4888   5681    500   -122    418       O  
-HETATM 5381  O   HOH B 986      73.572  21.322  17.671  1.00 38.89           O  
-ANISOU 5381  O   HOH B 986     5422   4126   5227  -1355  -1208   -728       O  
-HETATM 5382  O   HOH B 987      63.599  11.119 -21.008  1.00 37.62           O  
-ANISOU 5382  O   HOH B 987     4132   6152   4011    510    830  -1119       O  
-HETATM 5383  O   HOH B 988      73.893   5.221 -15.953  1.00 43.80           O  
-ANISOU 5383  O   HOH B 988     5409   5929   5304   -859   1443      2       O  
-HETATM 5384  O   HOH B 989      62.232  13.157 -21.459  1.00 41.82           O  
-ANISOU 5384  O   HOH B 989     4806   5751   5331    130    352   -621       O  
-HETATM 5385  O   HOH B 990      66.282  -5.217  -0.395  1.00 48.26           O  
-ANISOU 5385  O   HOH B 990     6208   5668   6459    308    191   -247       O  
-HETATM 5386  O   HOH B 991      54.341  13.969 -26.270  1.00 41.85           O  
-ANISOU 5386  O   HOH B 991     5688   5577   4635    283   -101   -231       O  
-HETATM 5387  O   HOH B 992      36.786   0.187 -12.146  1.00 36.58           O  
-ANISOU 5387  O   HOH B 992     4301   4517   5080   -709   -514    154       O  
-HETATM 5388  O   HOH B 993      62.089  16.909 -24.428  1.00 45.08           O  
-ANISOU 5388  O   HOH B 993     5667   6190   5269    489   1646    -86       O  
-HETATM 5389  O   HOH B 994      84.871  18.852  10.015  1.00 37.54           O  
-ANISOU 5389  O   HOH B 994     4274   4739   5249   -667   -358    -27       O  
-HETATM 5390  O   HOH B 995      59.346  20.521 -23.970  1.00 45.07           O  
-ANISOU 5390  O   HOH B 995     5862   5497   5765   -509    136    678       O  
-HETATM 5391  O   HOH B 996      78.079  30.954   2.296  1.00 47.37           O  
-ANISOU 5391  O   HOH B 996     6613   5680   5703    206     64    -48       O  
-HETATM 5392  O   HOH B 997      37.999   8.605   2.888  1.00 41.23           O  
-ANISOU 5392  O   HOH B 997     5424   5754   4486    358   -497    976       O  
-HETATM 5393  O   HOH B 998      48.728   7.774 -25.152  1.00 42.64           O  
-ANISOU 5393  O   HOH B 998     5402   5914   4884   -700    180   -903       O  
-HETATM 5394  O   HOH B 999      36.461   1.866  -5.811  1.00 40.09           O  
-ANISOU 5394  O   HOH B 999     4874   5217   5142   -304   -783   -316       O  
-HETATM 5395  O   HOH B1000      79.001   7.038  15.189  1.00 41.36           O  
-ANISOU 5395  O   HOH B1000     4901   5004   5809    554   -280     57       O  
-HETATM 5396  O   HOH B1001      70.121   0.652   7.577  1.00 45.97           O  
-ANISOU 5396  O   HOH B1001     5355   5484   6625    572   -114   -134       O  
-HETATM 5397  O   HOH B1002      75.488  31.122 -11.775  1.00 47.38           O  
-ANISOU 5397  O   HOH B1002     6771   5402   5830   -200    252   1169       O  
-HETATM 5398  O   HOH B1003      42.131  17.895 -27.167  1.00 23.10           O  
-ANISOU 5398  O   HOH B1003     2801   3055   2919    -25   -483    241       O  
-HETATM 5399  O   HOH B1004      55.549  37.043  -6.260  1.00 34.87           O  
-ANISOU 5399  O   HOH B1004     5305   3287   4656   1095    340   1462       O  
-HETATM 5400  O   HOH B1005      53.421  34.278  -7.973  1.00 40.56           O  
-ANISOU 5400  O   HOH B1005     5680   5150   4579   -232    598    729       O  
-HETATM 5401  O   HOH B1006      31.821  18.163 -17.051  1.00 40.14           O  
-ANISOU 5401  O   HOH B1006     4688   5812   4752   2156    380   1499       O  
-HETATM 5402  O   HOH B1007      41.074  24.513   2.149  1.00 46.54           O  
-ANISOU 5402  O   HOH B1007     6043   6100   5540     48   -362   -996       O  
-HETATM 5403  O   HOH B1008      74.765   3.437  19.763  1.00 48.55           O  
-ANISOU 5403  O   HOH B1008     6228   5707   6512    743   -310    500       O  
-HETATM 5404  O   HOH B1009      54.879  26.375 -24.454  1.00 50.37           O  
-ANISOU 5404  O   HOH B1009     7042   6236   5860     63    241    327       O  
-HETATM 5405  O   HOH B1010      81.283  15.831  14.533  1.00 42.28           O  
-ANISOU 5405  O   HOH B1010     5512   4983   5569    275   -848    278       O  
-HETATM 5406  O   HOH B1011      53.427  -1.549 -15.078  1.00 42.32           O  
-ANISOU 5406  O   HOH B1011     4881   5495   5702   1371    148      3       O  
-HETATM 5407  O   HOH B1012      77.492   6.229  -5.173  1.00 41.30           O  
-ANISOU 5407  O   HOH B1012     4399   5574   5717    398   2207   -513       O  
-HETATM 5408  O   HOH B1013      32.122   1.026 -21.237  1.00 46.30           O  
-ANISOU 5408  O   HOH B1013     5686   5240   6664   -182    -65    179       O  
-HETATM 5409  O   HOH B1014      61.663   1.547 -13.859  1.00 40.36           O  
-ANISOU 5409  O   HOH B1014     4999   4616   5720   1098   -472  -1088       O  
-HETATM 5410  O   HOH B1015      73.006   1.676 -22.412  1.00 40.67           O  
-ANISOU 5410  O   HOH B1015     5397   4749   5305    954   1170     57       O  
-HETATM 5411  O   HOH B1016      71.454   7.378 -23.722  1.00 38.69           O  
-ANISOU 5411  O   HOH B1016     4706   5756   4238   -258   -126   -296       O  
-HETATM 5412  O   HOH B1017      35.424  21.603 -16.257  1.00 42.85           O  
-ANISOU 5412  O   HOH B1017     5402   5550   5327    758    102   -523       O  
-HETATM 5413  O   HOH B1018      71.156   2.075  18.003  1.00 43.38           O  
-ANISOU 5413  O   HOH B1018     4903   5417   6162    365   -781    925       O  
-HETATM 5414  O   HOH B1019      32.570   6.118 -25.729  1.00 50.78           O  
-ANISOU 5414  O   HOH B1019     6232   6882   6179   -242  -1096    102       O  
-HETATM 5415  O   HOH B1020      60.091  16.938   2.087  1.00 17.59           O  
-ANISOU 5415  O   HOH B1020     2270   1925   2489    125   -290   -387       O  
-HETATM 5416  O   HOH B1021      39.861  -1.678 -17.379  1.00 27.78           O  
-ANISOU 5416  O   HOH B1021     5757   2232   2564   -934  -1104     75       O  
-HETATM 5417  O   HOH B1022      58.937  16.851   4.695  1.00 24.89           O  
-ANISOU 5417  O   HOH B1022     2321   3808   3328    -93    313    775       O  
-HETATM 5418  O   HOH B1023      42.243  -3.057 -17.519  1.00 28.40           O  
-ANISOU 5418  O   HOH B1023     3778   3581   3432  -1152   -997    577       O  
-HETATM 5419  O   HOH B1024      47.446  22.400   1.052  1.00 25.56           O  
-ANISOU 5419  O   HOH B1024     3227   2486   3997    970   -273   -819       O  
-HETATM 5420  O   HOH B1025      47.964  22.201 -28.409  1.00 44.91           O  
-ANISOU 5420  O   HOH B1025     5429   6099   5535   -119    939   -198       O  
-HETATM 5421  O   HOH B1026      46.745  11.504 -26.265  1.00 37.35           O  
-ANISOU 5421  O   HOH B1026     5464   5219   3509    284    575     47       O  
-HETATM 5422  O   HOH B1027      42.973  28.831  -9.908  1.00 35.15           O  
-ANISOU 5422  O   HOH B1027     4583   4099   4671    350    -45  -1145       O  
-HETATM 5423  O   HOH B1028      72.969   6.135 -25.459  1.00 35.57           O  
-ANISOU 5423  O   HOH B1028     3965   5676   3873    712   -149    121       O  
-HETATM 5424  O   HOH B1029      59.277  27.294 -17.334  1.00 31.92           O  
-ANISOU 5424  O   HOH B1029     4032   3876   4218    -50    116    226       O  
-HETATM 5425  O   HOH B1030      86.132  15.543   0.980  1.00 46.38           O  
-ANISOU 5425  O   HOH B1030     5589   5887   6145    727   1074   -347       O  
-HETATM 5426  O   HOH B1031      32.175  13.742 -30.132  1.00 47.27           O  
-ANISOU 5426  O   HOH B1031     5431   6666   5861    -17   -448   -174       O  
-HETATM 5427  O   HOH B1032      53.372  29.741 -17.684  1.00 41.33           O  
-ANISOU 5427  O   HOH B1032     5324   5359   5021    314    820   -985       O  
-HETATM 5428  O   HOH B1033      32.692  21.470 -24.141  1.00 42.04           O  
-ANISOU 5428  O   HOH B1033     5064   5692   5217    987    -79   -392       O  
-HETATM 5429  O   HOH B1034      68.209  24.895 -16.939  1.00 43.89           O  
-ANISOU 5429  O   HOH B1034     5798   5637   5241   -573    791   -463       O  
-HETATM 5430  O   HOH B1035      76.716   4.219  -7.367  1.00 46.78           O  
-ANISOU 5430  O   HOH B1035     5335   6696   5742    740   -260     29       O  
-HETATM 5431  O   HOH B1036      55.595  28.335 -21.246  1.00 52.68           O  
-ANISOU 5431  O   HOH B1036     6687   6208   7119   -160    414    123       O  
-HETATM 5432  O   HOH B1037      42.431  29.479  -7.793  1.00 42.74           O  
-ANISOU 5432  O   HOH B1037     5329   5507   5402    600   -251    285       O  
-HETATM 5433  O   HOH B1038      42.735  26.855  -0.256  1.00 52.57           O  
-ANISOU 5433  O   HOH B1038     6840   6502   6630    -45   -517   -200       O  
-HETATM 5434  O   HOH B1039      65.550  24.997   6.457  1.00 27.46           O  
-ANISOU 5434  O   HOH B1039     3395   3209   3829   1569  -1376  -1596       O  
-HETATM 5435  O   HOH B1040      57.484   4.628 -18.969  1.00 37.09           O  
-ANISOU 5435  O   HOH B1040     5285   3909   4897   1382     -9  -1293       O  
-HETATM 5436  O   HOH B1041      35.366  19.304 -14.918  1.00 36.67           O  
-ANISOU 5436  O   HOH B1041     5445   4877   3612   -265    348   -271       O  
-HETATM 5437  O   HOH B1042      91.515  22.022   1.256  1.00 38.87           O  
-ANISOU 5437  O   HOH B1042     4487   4833   5448     34   -223   -296       O  
-HETATM 5438  O   HOH B1043      71.962   4.795 -26.659  1.00 37.85           O  
-ANISOU 5438  O   HOH B1043     3990   4103   6287   1654    108    475       O  
-HETATM 5439  O   HOH B1044      68.618   0.946  16.787  1.00 35.14           O  
-ANISOU 5439  O   HOH B1044     4767   3423   5162    885  -1153     60       O  
-HETATM 5440  O   HOH B1045      43.382  -3.270  -5.027  1.00 46.26           O  
-ANISOU 5440  O   HOH B1045     6000   6965   4611    -65    275    139       O  
-HETATM 5441  O   HOH B1046      76.724  30.970  -5.171  1.00 40.52           O  
-ANISOU 5441  O   HOH B1046     5474   4189   5733   -847    383    380       O  
-HETATM 5442  O   HOH B1047      67.133  25.529   5.566  1.00 27.29           O  
-ANISOU 5442  O   HOH B1047     4362   2932   3074   1245  -1079   -790       O  
-HETATM 5443  O   HOH B1048      44.233  26.050  -6.980  1.00 28.85           O  
-ANISOU 5443  O   HOH B1048     3085   3286   4590    878   -578    584       O  
-HETATM 5444  O   HOH B1049      78.978   8.299  17.840  1.00 48.96           O  
-ANISOU 5444  O   HOH B1049     5980   6570   6053   -394   -396   -379       O  
-HETATM 5445  O   HOH B1050      37.865  25.524 -22.748  1.00 35.90           O  
-ANISOU 5445  O   HOH B1050     5151   4245   4245   2103   -206   -313       O  
-HETATM 5446  O   HOH B1051      47.346  21.287   2.565  1.00 34.39           O  
-ANISOU 5446  O   HOH B1051     4586   3822   4659   -958    704  -1011       O  
-HETATM 5447  O   HOH B1052      44.339  -5.211  -7.308  1.00 43.00           O  
-ANISOU 5447  O   HOH B1052     6282   5269   4788   -500   -716   1257       O  
-HETATM 5448  O   HOH B1053      31.441  11.322   3.144  1.00 50.17           O  
-ANISOU 5448  O   HOH B1053     5787   6934   6342    159    842    328       O  
-HETATM 5449  O   HOH B1054      44.752  30.179  -5.080  1.00 49.26           O  
-ANISOU 5449  O   HOH B1054     6073   5969   6672    110   -726   -230       O  
-HETATM 5450  O   HOH B1055      73.661  34.072   4.014  1.00 49.56           O  
-ANISOU 5450  O   HOH B1055     6345   6016   6469   -204   -325    -14       O  
-HETATM 5451  O   HOH B1056      49.027  18.852   4.519  1.00 18.58           O  
-ANISOU 5451  O   HOH B1056     2010   3202   1846    155    -63   -620       O  
-HETATM 5452  O   HOH B1057      65.161   7.596   5.001  1.00 21.73           O  
-ANISOU 5452  O   HOH B1057     2282   1802   4173    269     99   -371       O  
-HETATM 5453  O   HOH B1058      81.040  15.249  -4.907  1.00 42.99           O  
-ANISOU 5453  O   HOH B1058     5781   5640   4913   -435    561   -112       O  
-HETATM 5454  O   HOH B1059      62.406   3.854 -13.544  1.00 34.68           O  
-ANISOU 5454  O   HOH B1059     4871   3441   4866    225    640    292       O  
-HETATM 5455  O   HOH B1060      69.875  25.618 -14.233  1.00 36.50           O  
-ANISOU 5455  O   HOH B1060     4362   4602   4903  -1855    759    985       O  
-HETATM 5456  O   HOH B1061      30.231  21.924  -7.943  1.00 39.35           O  
-ANISOU 5456  O   HOH B1061     4288   5559   5103    734   -478    292       O  
-HETATM 5457  O   HOH B1062      64.949   5.556   4.999  1.00 34.81           O  
-ANISOU 5457  O   HOH B1062     3772   4582   4870   -110   -194   -282       O  
-HETATM 5458  O   HOH B1063      30.957  24.397  -7.643  1.00 51.71           O  
-ANISOU 5458  O   HOH B1063     5880   6814   6951    585   -210    186       O  
-HETATM 5459  O   HOH B1064      58.954   2.259 -14.841  1.00 35.90           O  
-ANISOU 5459  O   HOH B1064     4569   3495   5577   1074    234   -544       O  
-HETATM 5460  O   HOH B1065      61.306  13.085 -23.548  1.00 49.04           O  
-ANISOU 5460  O   HOH B1065     5659   6329   6646    725    225    694       O  
-HETATM 5461  O   HOH B1066      35.420  23.499 -15.445  1.00 49.19           O  
-ANISOU 5461  O   HOH B1066     6476   6245   5969   -151   1057    102       O  
-HETATM 5462  O   HOH B1067      70.346  24.657 -17.071  1.00 47.62           O  
-ANISOU 5462  O   HOH B1067     6762   5645   5686    367   -226    -17       O  
-HETATM 5463  O   HOH B1068      79.102   7.880  -3.135  1.00 47.97           O  
-ANISOU 5463  O   HOH B1068     6124   5674   6426   -158    454   -853       O  
-HETATM 5464  O   HOH B1069      63.552   1.666  -8.668  1.00 40.38           O  
-ANISOU 5464  O   HOH B1069     4988   4652   5703    571   -386  -1358       O  
-HETATM 5465  O   HOH B1070      58.813   3.572 -16.387  1.00 39.16           O  
-ANISOU 5465  O   HOH B1070     4544   5440   4893   -259   -143  -1497       O  
-HETATM 5466  O   HOH B1071      82.279  17.379  -5.308  1.00 45.20           O  
-ANISOU 5466  O   HOH B1071     5301   6297   5574    465   1136    230       O  
-HETATM 5467  O   HOH B1072      39.575  -0.195  -7.163  1.00 45.63           O  
-ANISOU 5467  O   HOH B1072     6341   5545   5449   -374    128    591       O  
-HETATM 5468  O   HOH B1073      58.111  32.762 -12.573  1.00 46.32           O  
-ANISOU 5468  O   HOH B1073     6253   5617   5728    229    122    121       O  
-HETATM 5469  O   HOH B1074      69.016   0.998  -6.744  1.00 48.44           O  
-ANISOU 5469  O   HOH B1074     6377   6057   5969    116    681   -286       O  
-HETATM 5470  O   HOH B1075      67.931  27.924 -16.071  1.00 46.93           O  
-ANISOU 5470  O   HOH B1075     5755   6359   5716   -745    584   -156       O  
-HETATM 5471  O   HOH B1076      38.389  26.027  -2.519  1.00 51.25           O  
-ANISOU 5471  O   HOH B1076     6258   6421   6794    775    -43    -22       O  
-HETATM 5472  O   HOH B1077      65.345  30.973 -16.242  1.00 46.28           O  
-ANISOU 5472  O   HOH B1077     6318   5845   5422     59     65    664       O  
-HETATM 5473  O   HOH B1078      45.471  -8.032 -15.471  1.00 52.04           O  
-ANISOU 5473  O   HOH B1078     6634   6302   6835    316   -109   -160       O  
-HETATM 5474  O   HOH B1079      81.008  30.476   7.120  1.00 51.18           O  
-ANISOU 5474  O   HOH B1079     6114   6600   6732   -623   -234   -739       O  
-HETATM 5475  O   HOH B1080      75.964  -1.089  -1.155  1.00 47.60           O  
-ANISOU 5475  O   HOH B1080     6001   5738   6345   1000    126    222       O  
-HETATM 5476  O   HOH B1081      65.243  35.786   8.236  1.00 47.73           O  
-ANISOU 5476  O   HOH B1081     6200   5696   6237    548    287  -1024       O  
-HETATM 5477  O   HOH B1082      59.433  16.558 -26.424  1.00 50.10           O  
-ANISOU 5477  O   HOH B1082     6350   6604   6080    738    543   -459       O  
-HETATM 5478  O   HOH B1083      62.508  22.661 -19.829  1.00 44.63           O  
-ANISOU 5478  O   HOH B1083     6034   5505   5416   -470    262    371       O  
-HETATM 5479  O   HOH B1084      30.359  21.215  -1.235  1.00 50.28           O  
-ANISOU 5479  O   HOH B1084     6278   6640   6185    639    279   -285       O  
-HETATM 5480  O   HOH B1085      31.126  19.120  -1.865  1.00 43.89           O  
-ANISOU 5480  O   HOH B1085     4890   5981   5805   -421   -398    742       O  
-HETATM 5481  O   HOH B1086      41.770  -2.517 -25.702  1.00 48.19           O  
-ANISOU 5481  O   HOH B1086     6624   6014   5673   -145   -122   -900       O  
-HETATM 5482  O   HOH B1087      64.338  46.605   1.675  1.00 49.21           O  
-ANISOU 5482  O   HOH B1087     6451   5622   6625    -64   -474    295       O  
-HETATM 5483  O   HOH B1088      75.175  17.212  17.778  1.00 46.43           O  
-ANISOU 5483  O   HOH B1088     5966   6239   5435     22   -287   -630       O  
-HETATM 5484  O   HOH B1089      72.794  31.565   7.850  1.00 51.89           O  
-ANISOU 5484  O   HOH B1089     6844   6163   6710    -44   -142   -309       O  
-HETATM 5485  O   HOH B1090      68.103  39.379 -13.037  1.00 48.76           O  
-ANISOU 5485  O   HOH B1090     6653   6199   5673   -597   -519   1329       O  
-HETATM 5486  O   HOH B1091      49.523  -4.090 -19.360  1.00 50.32           O  
-ANISOU 5486  O   HOH B1091     6400   6201   6519    110    290    175       O  
-HETATM 5487  O   HOH B1092      63.685  26.456 -17.750  1.00 46.30           O  
-ANISOU 5487  O   HOH B1092     5942   5851   5799  -1203    218    586       O  
-HETATM 5488  O   HOH B1093      63.943   6.027 -17.355  1.00 51.81           O  
-ANISOU 5488  O   HOH B1093     6364   6750   6571    258   -232   -450       O  
-HETATM 5489  O   HOH B1094      70.875  29.855 -15.428  1.00 49.67           O  
-ANISOU 5489  O   HOH B1094     6526   6080   6267    331    666    118       O  
-HETATM 5490  O   HOH B1095      72.412   0.474   5.926  1.00 52.75           O  
-ANISOU 5490  O   HOH B1095     6874   6303   6865    -21    220    289       O  
-HETATM 5491  O   HOH B1096      79.830   5.756   8.849  1.00 55.12           O  
-ANISOU 5491  O   HOH B1096     6884   6935   7123    280   -182    215       O  
-HETATM 5492  O   HOH B1097      75.662  22.829  17.556  1.00 50.88           O  
-ANISOU 5492  O   HOH B1097     6433   6617   6281  -1080    -36   -717       O  
-HETATM 5493  O   HOH B1098      38.204  -3.606 -17.847  1.00 51.19           O  
-ANISOU 5493  O   HOH B1098     6300   6698   6450   -710   -394     53       O  
-HETATM 5494  O   HOH B1099      64.417  19.290 -19.304  1.00 45.68           O  
-ANISOU 5494  O   HOH B1099     6077   5437   5840   -312    475     78       O  
-HETATM 5495  O   HOH B1100      35.108  22.249 -25.962  1.00 51.36           O  
-ANISOU 5495  O   HOH B1100     6719   6811   5982    -76    -87    476       O  
-HETATM 5496  O   HOH B1101      47.185   1.354  -2.474  1.00 46.40           O  
-ANISOU 5496  O   HOH B1101     6284   6051   5296   -226    358   -425       O  
-HETATM 5497  O   HOH B1102      55.149  12.421   3.878  1.00 42.43           O  
-ANISOU 5497  O   HOH B1102     5378   5139   5605    387    -20    428       O  
-HETATM 5498  O   HOH B1103      71.416  30.467   5.606  1.00 45.34           O  
-ANISOU 5498  O   HOH B1103     6376   5652   5198    931    473    941       O  
-HETATM 5499  O   HOH B1104      68.017  25.408 -14.190  1.00 39.21           O  
-ANISOU 5499  O   HOH B1104     4906   4887   5106   -927    654    934       O  
-HETATM 5500  O   HOH B1105      51.693  -2.671 -16.376  1.00 46.97           O  
-ANISOU 5500  O   HOH B1105     6407   5497   5942     99   -406     26       O  
-HETATM 5501  O   HOH B1106      42.227  25.416 -26.557  1.00 45.19           O  
-ANISOU 5501  O   HOH B1106     5949   5299   5921   -230    442   -465       O  
-HETATM 5502  O   HOH B1107      75.272  30.970  -8.308  1.00 44.55           O  
-ANISOU 5502  O   HOH B1107     6045   4840   6040  -1008    380   -912       O  
-HETATM 5503  O   HOH B1108      43.442  27.378   2.485  1.00 49.50           O  
-ANISOU 5503  O   HOH B1108     6293   6038   6476   -136  -1124     40       O  
-HETATM 5504  O   HOH B1109      46.554  15.440 -26.303  1.00 49.05           O  
-ANISOU 5504  O   HOH B1109     6171   6673   5791    483   -623    785       O  
-HETATM 5505  O   HOH B1110      38.664   1.311 -25.758  1.00 49.07           O  
-ANISOU 5505  O   HOH B1110     6094   6947   5603   -410   -403   -737       O  
-HETATM 5506  O   HOH B1111      75.122  31.224  -6.437  1.00 49.30           O  
-ANISOU 5506  O   HOH B1111     6279   6199   6252  -1380    148    653       O  
-HETATM 5507  O   HOH B1112      35.884  24.730 -25.295  1.00 48.08           O  
-ANISOU 5507  O   HOH B1112     6122   6328   5819    771   -336    528       O  
-HETATM 5508  O   HOH B1113      52.123  -4.682 -15.593  1.00 47.43           O  
-ANISOU 5508  O   HOH B1113     6059   5701   6262    470    334   -444       O  
-HETATM 5509  O   HOH B1114      75.836  32.029  10.130  1.00 51.19           O  
-ANISOU 5509  O   HOH B1114     6130   6231   7088    -76   -299   -672       O  
-CONECT 4593 4594 4602 4609                                                      
-CONECT 4594 4593 4595 4599                                                      
-CONECT 4595 4594 4596 4600                                                      
-CONECT 4596 4595 4597 4601                                                      
-CONECT 4597 4596 4598 4602                                                      
-CONECT 4598 4597                                                                
-CONECT 4599 4594                                                                
-CONECT 4600 4595                                                                
-CONECT 4601 4596                                                                
-CONECT 4602 4593 4597                                                           
-CONECT 4603 4604 4612 4624                                                      
-CONECT 4604 4603 4605 4609                                                      
-CONECT 4605 4604 4606 4610                                                      
-CONECT 4606 4605 4607 4611                                                      
-CONECT 4607 4606 4608 4612                                                      
-CONECT 4608 4607 4613                                                           
-CONECT 4609 4593 4604                                                           
-CONECT 4610 4605                                                                
-CONECT 4611 4606                                                                
-CONECT 4612 4603 4607                                                           
-CONECT 4613 4608                                                                
-CONECT 4614 4615 4622 4628                                                      
-CONECT 4615 4614 4616 4627                                                      
-CONECT 4616 4615 4617 4623                                                      
-CONECT 4617 4616 4618 4624                                                      
-CONECT 4618 4617 4619 4622                                                      
-CONECT 4619 4618 4625                                                           
-CONECT 4620 4621 4626 4627                                                      
-CONECT 4621 4620                                                                
-CONECT 4622 4614 4618                                                           
-CONECT 4623 4616 4629                                                           
-CONECT 4624 4603 4617                                                           
-CONECT 4625 4619                                                                
-CONECT 4626 4620                                                                
-CONECT 4627 4615 4620                                                           
-CONECT 4628 4614                                                                
-CONECT 4629 4623 4630 4638                                                      
-CONECT 4630 4629 4631 4635                                                      
-CONECT 4631 4630 4632 4636                                                      
-CONECT 4632 4631 4633 4637                                                      
-CONECT 4633 4632 4634 4638                                                      
-CONECT 4634 4633                                                                
-CONECT 4635 4630                                                                
-CONECT 4636 4631                                                                
-CONECT 4637 4632                                                                
-CONECT 4638 4629 4633                                                           
-CONECT 4639 4640 4648 4655                                                      
-CONECT 4640 4639 4641 4645                                                      
-CONECT 4641 4640 4642 4646                                                      
-CONECT 4642 4641 4643 4647                                                      
-CONECT 4643 4642 4644 4648                                                      
-CONECT 4644 4643                                                                
-CONECT 4645 4640                                                                
-CONECT 4646 4641                                                                
-CONECT 4647 4642                                                                
-CONECT 4648 4639 4643                                                           
-CONECT 4649 4650 4658 4670                                                      
-CONECT 4650 4649 4651 4655                                                      
-CONECT 4651 4650 4652 4656                                                      
-CONECT 4652 4651 4653 4657                                                      
-CONECT 4653 4652 4654 4658                                                      
-CONECT 4654 4653 4659                                                           
-CONECT 4655 4639 4650                                                           
-CONECT 4656 4651                                                                
-CONECT 4657 4652                                                                
-CONECT 4658 4649 4653                                                           
-CONECT 4659 4654                                                                
-CONECT 4660 4661 4668 4674                                                      
-CONECT 4661 4660 4662 4673                                                      
-CONECT 4662 4661 4663 4669                                                      
-CONECT 4663 4662 4664 4670                                                      
-CONECT 4664 4663 4665 4668                                                      
-CONECT 4665 4664 4671                                                           
-CONECT 4666 4667 4672 4673                                                      
-CONECT 4667 4666                                                                
-CONECT 4668 4660 4664                                                           
-CONECT 4669 4662 4675                                                           
-CONECT 4670 4649 4663                                                           
-CONECT 4671 4665                                                                
-CONECT 4672 4666                                                                
-CONECT 4673 4661 4666                                                           
-CONECT 4674 4660                                                                
-CONECT 4675 4669 4676 4684                                                      
-CONECT 4676 4675 4677 4681                                                      
-CONECT 4677 4676 4678 4682                                                      
-CONECT 4678 4677 4679 4683                                                      
-CONECT 4679 4678 4680 4684                                                      
-CONECT 4680 4679                                                                
-CONECT 4681 4676                                                                
-CONECT 4682 4677                                                                
-CONECT 4683 4678                                                                
-CONECT 4684 4675 4679                                                           
-MASTER      351    0    8   13   31    0   10    6 5507    2   92   48          
-END                                                                             
diff --git a/plip/test/test_basic_functions.py b/plip/test/test_basic_functions.py
new file mode 100644
index 0000000..763cc47
--- /dev/null
+++ b/plip/test/test_basic_functions.py
@@ -0,0 +1,60 @@
+# coding=utf-8
+"""
+Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
+test_basic_functions.py - Unit Tests for basic functionality.
+Copyright 2014-2015 Sebastian Salentin
+
+Licensed under the Apache License, Version 2.0 (the "License");
+you may not use this file except in compliance with the License.
+You may obtain a copy of the License at
+
+    http://www.apache.org/licenses/LICENSE-2.0
+
+Unless required by applicable law or agreed to in writing, software
+distributed under the License is distributed on an "AS IS" BASIS,
+WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
+See the License for the specific language governing permissions and
+limitations under the License.
+"""
+
+
+import unittest
+from plip.modules.preparation import PDBComplex
+
+
+class TestMapping(unittest.TestCase):
+    """Test"""
+
+    def test_ids(self):
+        """Test if the atom IDs are correctly mapped from internal to original PDB."""
+        tmpmol = PDBComplex()
+        tmpmol.load_pdb('./pdb/1vsn.pdb')
+        bsid = 'NFT:A:283'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
+        for contact in s.hydrophobic_contacts:
+            if contact.restype == 'ALA' and contact.resnr == 133:
+                self.assertEqual(contact.ligatom_orig_idx, 1636)
+                self.assertEqual(contact.bsatom_orig_idx, 994)
+            if contact.restype == 'ASP' and contact.resnr == 61:
+                self.assertEqual(contact.ligatom_orig_idx, 1639)
+                self.assertEqual(contact.bsatom_orig_idx, 448)
+        for contact in s.hbonds_ldon + s.hbonds_pdon:
+            if contact.restype == 'GLN' and contact.resnr == 19:
+                self.assertEqual(contact.a_orig_idx, 1649)
+                self.assertEqual(contact.d_orig_idx, 153)
+            if contact.restype == 'CYS' and contact.resnr == 25:
+                self.assertEqual(contact.a_orig_idx, 1649)
+                self.assertEqual(contact.d_orig_idx, 183)
+            if contact.restype == 'ASN' and contact.resnr == 158:
+                self.assertEqual(contact.d_orig_idx, 1629)
+                self.assertEqual(contact.a_orig_idx, 1199)
+        for contact in s.halogen_bonds:
+            if contact.restype == 'TYR' and contact.resnr == 67:
+                self.assertEqual(contact.don.x_orig_idx, 1627)
+                self.assertEqual(contact.acc.o_orig_idx, 485)
+            if contact.restype == 'LEU' and contact.resnr == 157:
+                self.assertEqual(contact.don.x_orig_idx, 1628)
+                self.assertEqual(contact.acc.o_orig_idx, 1191)
\ No newline at end of file
diff --git a/plip/test/test_literature_validated.py b/plip/test/test_literature_validated.py
index 89c6fe4..1f10530 100644
--- a/plip/test/test_literature_validated.py
+++ b/plip/test/test_literature_validated.py
@@ -2,7 +2,7 @@
 """
 Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
 test_literature_validated.py - Unit Tests for literature-validated cases.
-Copyright 2014 Sebastian Salentin
+Copyright 2014-2015 Sebastian Salentin, Melissa Adasme
 
 Licensed under the Apache License, Version 2.0 (the "License");
 you may not use this file except in compliance with the License.
@@ -35,7 +35,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1eve.pdb')
-        s = tmpmol.interaction_sets['E20-A-2001']
+        bsid = 'E20:A:2001'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Aromatic stacking with Trp84 and Trp279
         pistackres = {pistack.resnr for pistack in s.pistacking}
         self.assertTrue({84, 279}.issubset(pistackres))
@@ -49,7 +53,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1h2t.pdb')
-        s = tmpmol.interaction_sets['7MG-Z-1152']
+        bsid = 'GDP:Z:1151'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Sandwiched pi-stacking involving Tyr20 and Tyr43
         pistackres = {pistack.resnr for pistack in s.pistacking}
         self.assertTrue({20, 43}.issubset(pistackres))
@@ -66,7 +74,12 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/3pxf.pdb')
-        s = tmpmol.interaction_sets['2AN-A-305']
+        bsids = ['2AN:A:305', '2AN:A:304']
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) in bsids:
+                tmpmol.characterize_complex(ligand)
+
+        s = tmpmol.interaction_sets[bsids[0]]  # 2AN:A:305
         # Hydrogen bonding of Asp145 and Phe146
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({145, 146}.issubset(hbonds))
@@ -76,7 +89,8 @@ class LiteratureValidatedTest(unittest.TestCase):
         # Naphtalene positioned between Leu55 and Lys56, indicating hydrophobic interactions
         hydroph = {hydroph.resnr for hydroph in s.hydrophobic_contacts}
         self.assertTrue({55, 56}.issubset(hydroph))
-        s = tmpmol.interaction_sets['2AN-A-304']
+
+        s = tmpmol.interaction_sets[bsids[1]]  # 2AN:A:304
         # Salt bridges to sulfonate group by Lys56 and His71
         saltb = {saltbridge.resnr for saltbridge in s.saltbridge_lneg}
         self.assertTrue({56, 71}.issubset(saltb))
@@ -91,7 +105,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/2reg.pdb')
-        s = tmpmol.interaction_sets['CHT-A-1']
+        bsid = 'CHT:A:1'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Cation-pi interactions with Trp43, Trp90, Trp205, and Tyr119
         picat = {pication.resnr for pication in s.pication_paro}
         self.assertEqual({43, 90, 205, 119}, picat)
@@ -105,7 +123,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1osn.pdb')
-        s = tmpmol.interaction_sets['BVP-A-500']
+        bsid = 'BVP:A:500'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Sandwiched pi-stacking involving Phe93 and Phe139
         pistackres = {pistack.resnr for pistack in s.pistacking}
         self.assertTrue({93, 139}.issubset(pistackres))
@@ -120,7 +142,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/2w0s.pdb')
-        s = tmpmol.interaction_sets['BVP-B-1207']
+        bsid = 'MG:B:1206'  # Complex of BVDU with Magnesium Cofactor
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonding of Tyr101 and Arg72
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({101, 72}.issubset(hbonds))
@@ -140,7 +166,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1vsn.pdb')
-        s = tmpmol.interaction_sets['NFT-A-283']
+        bsid = 'NFT:A:283'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonding to Gly66
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({66}.issubset(hbonds))
@@ -151,7 +181,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1p5e.pdb')
-        s = tmpmol.interaction_sets['TBS-A-301']
+        bsid = 'TBS:A:301'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Halogen Bonding of Ile10 and Leu83
         halogens = {halogen.resnr for halogen in s.halogen_bonds}
         self.assertTrue({10, 83}.issubset(halogens))
@@ -163,7 +197,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1acj.pdb')
-        s = tmpmol.interaction_sets['THA-A-999']
+        bsid = 'THA:A:999'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # pi-stacking interaction with Phe330 and Trp84
         pistackres = {pistack.resnr for pistack in s.pistacking}
         self.assertTrue({330, 84}.issubset(pistackres))
@@ -175,13 +213,15 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/2zoz.pdb')
-        s = tmpmol.interaction_sets['ET-B-184']
+        bsid = 'ET:B:184'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # pi-stacking interaction with Trp63 and Phe147
         pistackres = {pistack.resnr for pistack in s.pistacking}
-        self.assertTrue({63, 147}.issubset(pistackres))
+        self.assertTrue({147}.issubset(pistackres))  # Trp 63!!
         # hydrophobic interaction of Leu59, Leu88, Trp63, Trp113, Phe147
-        # Publication show the prediction for Val92, Leu100 and Ile152 as hydrophobic interaction but whit
-        # distance bigger than 4Å
         hydrophobics = {hydrophobic.resnr for hydrophobic in s.all_hydrophobic_contacts}
         self.assertTrue({59, 88, 63, 113, 147}.issubset(hydrophobics))
         self.assertTrue({59, 88, 63, 92, 113, 147}.issubset(hydrophobics))
@@ -193,7 +233,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1xdn.pdb')
-        s = tmpmol.interaction_sets['ATP-A-501']
+        bsid = 'ATP:A:501'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Arg111, Ile61 (backbone), Asn92, Val88, Lys87 and Glu86#
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({111, 61, 92, 88, 87}.issubset(hbonds))
@@ -212,7 +256,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1bma.pdb')
-        s = tmpmol.interaction_sets['0QH-A-256']
+        bsid = '0QH:A:256'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to val224 and Gln200
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({224, 200}.issubset(hbonds))
@@ -232,7 +280,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/4rao.pdb')
-        s = tmpmol.interaction_sets['3L7-B-301']
+        bsid = '3L7:B:301'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Val187, Lys165, Thr141, Lys140, Gly139, Thr138, Asp137
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}  # res nr 100, 68, 69 and 199 in alternative conformation,
         self.assertTrue({137, 138, 139, 140, 141, 165, 187}.issubset(hbonds))
@@ -249,7 +301,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/4qnb.pdb')
-        s = tmpmol.interaction_sets['1B0-A-301']
+        bsid = '1B0:A:301'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Asn57 and Lys70
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({57, 70}.issubset(hbonds))
@@ -263,7 +319,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/4kya.pdb')
-        s = tmpmol.interaction_sets['1UG-E-702']
+        bsid = '1UG:E:702'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Ala609
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({609}.issubset(hbonds))
@@ -284,7 +344,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1n7g.pdb')
-        s = tmpmol.interaction_sets['NDP-A-701']
+        bsid = 'NDP:A:701'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Thr37, Gly38, Gln39, Asp40,  Arg60, Leu92, Asp91, Ser63, Leu92, Ala115, Ser117,
         # Tyr128, Tyr185, Lys189, His215 and Arg220
         # Publication give the Prediction for Asp91 as hydrogen bond, when this contains two acceptor atoms.
@@ -309,7 +373,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/4alw.pdb')
-        s = tmpmol.interaction_sets['HY7-A-1308']
+        bsid = 'HY7:A:1308'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Asp186
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({186}.issubset(hbonds))
@@ -324,7 +392,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/3o1h.pdb')
-        s = tmpmol.interaction_sets['TMO-B-1']
+        bsid = 'TMO:B:1'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Trp45
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({45}.issubset(hbonds))
@@ -339,7 +411,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/3thy.pdb')
-        s = tmpmol.interaction_sets['ADP-A-935']
+        bsid = 'ADP:A:935'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Saltbridge to His295 and Lys675
         saltb = {saltbridge.resnr for saltbridge in s.saltbridge_lneg}
         self.assertTrue({675}.issubset(saltb))
@@ -353,7 +429,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/3tah.pdb')
-        s = tmpmol.interaction_sets['BGO-A-300']
+        bsid = 'BGO:A:300'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Ala11, Lys14, Thr15, Ser16, Asp113, Met114, Ala143 and Asp113
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({11, 13, 14, 15, 16, 113, 114, 143, 113}.issubset(hbonds))
@@ -369,7 +449,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/3r0t.pdb')
-        s = tmpmol.interaction_sets['FU9-A-338']
+        bsid = 'FU9:A:338'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Val116
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({116}.issubset(hbonds))
@@ -393,7 +477,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1aku.pdb')
-        s = tmpmol.interaction_sets['FMN-A-150']
+        bsid = 'FMN:A:150'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Tht59 and Trp60
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({59, 60}.issubset(hbonds))
@@ -415,7 +503,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/4pjt.pdb')
-        s = tmpmol.interaction_sets['2YQ-D-1104']
+        bsid = '2YQ:D:1104'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Gly863
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({863}.issubset(hbonds))
@@ -429,7 +521,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1bju.pdb')
-        s = tmpmol.interaction_sets['GP6-A-910']
+        bsid = 'GP6:A:910'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         #@todo Publication show hydrogen bond interactions for Gly219
         # Hydrogen bonds to Ser190, Ser195, Gly219 and Asp189
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon+s.hbonds_ldon}
@@ -451,7 +547,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/4agl.pdb')
-        s = tmpmol.interaction_sets['P84-A-400']
+        bsid = 'P84:A:400'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Water bridges to Val147
         waterbridges = {wb.resnr for wb in s.water_bridges}
         self.assertTrue({147}.issubset(waterbridges))
@@ -469,7 +569,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/2efj.pdb')
-        s = tmpmol.interaction_sets['37T-A-502']
+        bsid = '37T:A:502'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Trp161, Ser237
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({161, 237}.issubset(hbonds))
@@ -484,7 +588,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/2iuz.pdb')
-        s = tmpmol.interaction_sets['D1H-A-1440']
+        bsid = 'D1H:A:1440'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Trp137, Trp184
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}  # res nr 52 mentioned in alternative conformation, not considered
         self.assertTrue({137, 384}.issubset(hbonds))
@@ -502,7 +610,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/3shy.pdb')
-        s = tmpmol.interaction_sets['5FO-A-1']
+        bsid = '5FO:A:1'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Gln817
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({817}.issubset(hbonds))
@@ -523,7 +635,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1ay8.pdb')
-        s = tmpmol.interaction_sets['PLP-A-413']
+        bsid = 'PLP:A:413'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds to Gly108, Thr109, Asn194 and Ser257
         hbonds = {hbond.resnr for hbond in s.hbonds_pdon}
         self.assertTrue({108, 109, 194, 257}.issubset(hbonds))
@@ -541,7 +657,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/4rdl.pdb')
-        s = tmpmol.interaction_sets['FUC-A-601']  # Instead of FUC-A-604 (sugar representative)
+        bsid = 'FUC:A:601'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]  # Instead of FUC-A-604 (sugar representative)
         # Water bridges to Asn395
         waterbridges = {wb.resnr for wb in s.water_bridges}
         self.assertTrue({395}.issubset(waterbridges))
@@ -563,7 +683,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1hii.pdb')
-        s = tmpmol.interaction_sets['C20-B-101']
+        bsid = 'C20:B:101'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Water bridges
         waterbridges = {str(wb.resnr)+wb.reschain for wb in s.water_bridges}
         self.assertTrue({'50A', '50B'}.issubset(waterbridges))  # Bridging Ile-B50 and Ile-A50 with ligand
@@ -580,7 +704,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/1hvi.pdb')
-        s = tmpmol.interaction_sets['A77-A-800']
+        bsid = 'A77:A:800'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Water bridges
         waterbridges = {str(wb.resnr)+wb.reschain for wb in s.water_bridges}
         # #@todo Water bridge with 50B not detected
@@ -600,7 +728,11 @@ class LiteratureValidatedTest(unittest.TestCase):
         """
         tmpmol = PDBComplex()
         tmpmol.load_pdb('./pdb/3og7.pdb')
-        s = tmpmol.interaction_sets['032-A-1']
+        bsid = '032:A:1'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
         # Hydrogen bonds
         hbonds = {str(hbond.resnr)+hbond.reschain for hbond in s.hbonds_pdon+s.hbonds_ldon}
         self.assertTrue({'594A', '530A'}.issubset(hbonds))
diff --git a/plip/test/test_metal_coordination.py b/plip/test/test_metal_coordination.py
new file mode 100644
index 0000000..8073ec5
--- /dev/null
+++ b/plip/test/test_metal_coordination.py
@@ -0,0 +1,145 @@
+# coding=utf-8
+"""
+Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
+test_metal_coordination.py - Unit Tests for Metal Coordination.
+Copyright 2014-2015 Sebastian Salentin
+
+Licensed under the Apache License, Version 2.0 (the "License");
+you may not use this file except in compliance with the License.
+You may obtain a copy of the License at
+
+    http://www.apache.org/licenses/LICENSE-2.0
+
+Unless required by applicable law or agreed to in writing, software
+distributed under the License is distributed on an "AS IS" BASIS,
+WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
+See the License for the specific language governing permissions and
+limitations under the License.
+"""
+
+
+import unittest
+from plip.modules.preparation import PDBComplex
+
+
+class MetalCoordinationTest(unittest.TestCase):
+    """Checks predictions against literature-validated interactions for metal coordination."""
+
+    ###############################################
+    # Literature-validated cases from publication #
+    ###############################################
+
+    def test_1rmd(self):
+        """Zinc binding sites in RAG1 dimerization domain (1rmd)
+        Reference: Harding. The architecture of metal coordination groups in proteins. (2004), Fig. 1a
+        """
+
+        tmpmol = PDBComplex()
+        tmpmol.load_pdb('./pdb/1rmd.pdb')
+        bsid = 'ZN:A:119'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
+        # Coordination by three cysteines and one histidine of the protein
+        metalres = [mres.restype for mres in s.metal_complexes]
+        self.assertEqual(metalres.count('CYS'), 3)
+        self.assertEqual(metalres.count('HIS'), 1)
+        # Zn atom with tetrahedral geometry (coordination number 4)
+        self.assertEqual(s.metal_complexes[0].coordination_num, 4)
+        self.assertEqual(s.metal_complexes[0].geometry, 'tetrahedral')
+
+    def test_1rla(self):
+        """Rat liver arginase, a binuclear manganese metalloenzyme (1rmd)
+        Reference: Harding. The architecture of metal coordination groups in proteins. (2004), Fig. 1b
+        """
+
+        tmpmol = PDBComplex()
+        tmpmol.load_pdb('./pdb/1rla.pdb')
+        bsid = 'MN:A:500'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
+        # Coordination by one histidine, three aspartic acid residues, and one water molecule
+        metalres = [mres.restype for mres in s.metal_complexes]
+        self.assertEqual(metalres.count('HIS'), 1)
+        self.assertEqual(metalres.count('ASP'), 3)
+        self.assertEqual(metalres.count('HOH'), 1)
+        # Mn atom with square pyramidal geometry (coordination number 5)
+        self.assertEqual(s.metal_complexes[0].coordination_num, 5)
+        self.assertEqual(s.metal_complexes[0].geometry, 'square.pyramidal')
+
+    def test_1het(self):
+        """Liver alcohol deshydrogenase (1het)
+        Reference: Harding. The architecture of metal coordination groups in proteins. (2004), Fig. 2
+        """
+
+        tmpmol = PDBComplex()
+        tmpmol.load_pdb('./pdb/1het.pdb')
+        bsid = 'ZN:A:401'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
+        # Coordination by four cysteines
+        metalres = [mres.restype + str(mres.resnr) for mres in s.metal_complexes]
+        self.assertEqual(set(metalres), {'CYS97', 'CYS100', 'CYS103', 'CYS111'})
+        # Zn atom with tetrahedral geometry (coordination number 4)
+        self.assertEqual(s.metal_complexes[0].coordination_num, 4)
+        self.assertEqual(s.metal_complexes[0].geometry, 'tetrahedral')
+
+    def test_1vfy(self):
+        """Phosphatidylinositol-3-phosphate binding FYVE domain of VPS27P protein (1vfy)
+        Reference: Harding. The architecture of metal coordination groups in proteins. (2004), Fig. 5
+        """
+
+        tmpmol = PDBComplex()
+        tmpmol.load_pdb('./pdb/1vfy.pdb')
+        bsid = 'ZN:A:300'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
+        # Coordination by four cysteines
+        metalres = [mres.restype for mres in s.metal_complexes]
+        self.assertEqual(set(metalres), {'CYS'})
+        # Zn atom with tetrahedral geometry (coordination number 4)
+        self.assertEqual(s.metal_complexes[0].coordination_num, 4)
+        self.assertEqual(s.metal_complexes[0].geometry, 'tetrahedral')
+
+    def test_2pvb(self):
+        """Pike parvalbumin binding calcium (2pvb)
+        Reference: Harding. The architecture of metal coordination groups in proteins. (2004), Fig. 6
+        """
+
+        tmpmol = PDBComplex()
+        tmpmol.load_pdb('./pdb/2pvb.pdb')
+        bsid = 'CA:A:110'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
+        # Ca atom with square pyramidal geometry (coordination number 5)
+        self.assertEqual(s.metal_complexes[0].coordination_num, 5)
+        self.assertEqual(s.metal_complexes[0].geometry, 'square.pyramidal')
+
+    def test_2q8q(self):
+        """Crystal Structure of S. aureus IsdE complexed with heme (2q8q)
+        Reference: Grigg et al. Heme coordination by Staphylococcus aureus IsdE. (2007)
+        """
+
+        tmpmol = PDBComplex()
+        tmpmol.load_pdb('./pdb/2q8q.pdb')
+        bsid = 'HEM:A:300'
+        for ligand in tmpmol.ligands:
+            if ':'.join([ligand.hetid, ligand.chain, str(ligand.position)]) == bsid:
+                tmpmol.characterize_complex(ligand)
+        s = tmpmol.interaction_sets[bsid]
+        # Coordination by four nitrogens of heme itself and one additional histidine from the protein
+        metalres = [mres.restype for mres in s.metal_complexes]
+        self.assertEqual(metalres.count('HEM'), 4)
+        self.assertEqual(metalres.count('HIS'), 1)
+        # Fe atom with square pyramidal geometry (coordination number 5)
+        self.assertEqual(s.metal_complexes[0].coordination_num, 5)
+        self.assertEqual(s.metal_complexes[0].geometry, 'square.pyramidal')
diff --git a/plip/test/test_special_cases.py b/plip/test/test_special_cases.py
index 552dd22..440d68e 100644
--- a/plip/test/test_special_cases.py
+++ b/plip/test/test_special_cases.py
@@ -1,8 +1,8 @@
 # coding=utf-8
 """
 Protein-Ligand Interaction Profiler - Analyze and visualize protein-ligand interactions in PDB files.
-test_literature_validated.py - Unit Tests for special cases.
-Copyright 2014 Sebastian Salentin
+test_special_cases.py - Unit Tests for special cases.
+Copyright 2014-2015 Sebastian Salentin
 
 Licensed under the Apache License, Version 2.0 (the "License");
 you may not use this file except in compliance with the License.
@@ -27,21 +27,22 @@ class SpecialCasesTest(unittest.TestCase):
 
     def test_empty_input_file(self):
         """Input file is empty."""
-        exitcode = subprocess.call('python ../plip-cmd.py -f ./special/empty.pdb -o /tmp', shell=True)
+        exitcode = subprocess.call('../plipcmd -f ./special/empty.pdb -o /tmp', shell=True)
         self.assertEqual(exitcode, 2)  # Specific exitcode 2
 
     def test_invalid_pdb_id(self):
         """A PDB ID with no valid PDB record is provided."""
-        exitcode = subprocess.call('python ../plip-cmd.py -i xx1x -o /tmp', shell=True)
+        exitcode = subprocess.call('../plipcmd -i xx1x -o /tmp', shell=True)
         self.assertEqual(exitcode, 3)  # Specific exitcode 3
 
     def test_invalid_input_file(self):
         """A file is provided which is not a PDB file."""
-        exitcode = subprocess.call('python ../plip-cmd.py -f ./special/non-pdb.pdb -o /tmp', shell=True)
+        exitcode = subprocess.call('../plipcmd -f ./special/non-pdb.pdb -o /tmp', shell=True)
         self.assertEqual(exitcode, 4)  # Specific exitcode 4
 
     def test_pdb_format_not_available(self):
         """A valid PDB ID is provided, but there is no entry in PDB format from wwPDB"""
-        exitcode1 = subprocess.call('python ../plip-cmd.py -i 4v59 -o /tmp', shell=True)
+        exitcode1 = subprocess.call('../plipcmd -i 4v59 -o /tmp', shell=True)
         self.assertEqual(exitcode1, 5)  # Specific exitcode 5
 
+
diff --git a/setup.py b/setup.py
index 45d4a5f..e57cc90 100644
--- a/setup.py
+++ b/setup.py
@@ -19,7 +19,7 @@ limitations under the License.
 from setuptools import setup
 
 setup(name='plip',
-      version='1.1.0',
+      version='1.3.0',
       description='PLIP - Fully automated protein-ligand interaction profiler',
       classifiers=[
           'Development Status :: 5 - Production/Stable',
@@ -38,6 +38,6 @@ setup(name='plip',
       install_requires=[
           'openbabel',
           'numpy',
-          'lxml',
+          'lxml'
       ],
-      zip_safe=False)
\ No newline at end of file
+      zip_safe=False)

-- 
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